REMARK 100 THIS ENTRY IS ALTERED FROM 3EFS. ATOM 1 N PHE A 2 -9.202 -20.441 28.730 1.00 90.68 A N ANISOU 1 N PHE A 2 15439 10046 8968 1362 -369 474 A N ATOM 2 CA PHE A 2 -10.028 -19.284 29.057 1.00 85.72 A C ANISOU 2 CA PHE A 2 14629 9489 8452 1104 -277 316 A C ATOM 3 C PHE A 2 -11.287 -19.694 29.811 1.00 89.94 A C ANISOU 3 C PHE A 2 15437 9868 8869 841 -93 216 A C ATOM 4 O PHE A 2 -12.160 -20.367 29.263 1.00 92.88 A O ANISOU 4 O PHE A 2 15924 10109 9258 765 47 175 A O ATOM 5 CB PHE A 2 -10.409 -18.518 27.791 1.00 77.88 A C ANISOU 5 CB PHE A 2 13282 8574 7734 1093 -222 232 A C ATOM 6 CG PHE A 2 -9.251 -17.842 27.123 1.00 70.62 A C ANISOU 6 CG PHE A 2 12049 7835 6948 1302 -391 304 A C ATOM 7 CD1 PHE A 2 -8.554 -18.476 26.111 1.00 60.03 A C ANISOU 7 CD1 PHE A 2 10668 6493 5647 1546 -464 409 A C ATOM 8 CD2 PHE A 2 -8.864 -16.569 27.504 1.00 73.55 A C ANISOU 8 CD2 PHE A 2 12175 8373 7398 1245 -469 264 A C ATOM 9 CE1 PHE A 2 -7.490 -17.856 25.492 1.00 62.92 A C ANISOU 9 CE1 PHE A 2 10737 7037 6133 1733 -614 477 A C ATOM 10 CE2 PHE A 2 -7.802 -15.943 26.889 1.00 74.29 A C ANISOU 10 CE2 PHE A 2 11980 8640 7605 1419 -627 331 A C ATOM 11 CZ PHE A 2 -7.113 -16.586 25.881 1.00 73.22 A C ANISOU 11 CZ PHE A 2 11789 8519 7513 1665 -701 440 A C ATOM 12 N LYS A 3 -11.378 -19.278 31.069 1.00 86.99 A N ANISOU 12 N LYS A 3 15168 9518 8367 688 -92 178 A N ATOM 13 CA LYS A 3 -12.551 -19.569 31.885 1.00 87.15 A C ANISOU 13 CA LYS A 3 15436 9408 8270 426 87 78 A C ATOM 14 C LYS A 3 -12.866 -18.422 32.842 1.00 79.05 A C ANISOU 14 C LYS A 3 14320 8467 7248 220 137 -36 A C ATOM 15 O LYS A 3 -14.033 -18.120 33.099 1.00 71.35 A O ANISOU 15 O LYS A 3 13356 7439 6314 -8 330 -168 A O ATOM 16 CB LYS A 3 -12.374 -20.880 32.658 1.00 98.01 A C ANISOU 16 CB LYS A 3 17241 10633 9366 455 63 182 A C ATOM 17 CG LYS A 3 -11.079 -20.983 33.452 1.00107.32 A C ANISOU 17 CG LYS A 3 18512 11889 10374 616 -147 329 A C ATOM 18 CD LYS A 3 -9.924 -21.449 32.579 1.00111.68 A C ANISOU 18 CD LYS A 3 18972 12487 10975 948 -309 489 A C ATOM 19 CE LYS A 3 -8.671 -21.691 33.404 1.00117.28 A C ANISOU 19 CE LYS A 3 19785 13278 11496 1114 -517 665 A C ATOM 20 NZ LYS A 3 -8.217 -20.451 34.090 1.00119.82 A N1+ ANISOU 20 NZ LYS A 3 19895 13803 11828 1011 -621 630 A N1+ ATOM 21 N ASN A 4 -11.824 -17.783 33.364 1.00 78.58 A N ANISOU 21 N ASN A 4 14171 8542 7142 295 -30 18 A N ATOM 22 CA ASN A 4 -12.003 -16.651 34.264 1.00 79.24 A C ANISOU 22 CA ASN A 4 14187 8705 7217 99 11 -91 A C ATOM 23 C ASN A 4 -12.277 -15.362 33.500 1.00 61.27 A C ANISOU 23 C ASN A 4 11529 6529 5223 69 73 -201 A C ATOM 24 O ASN A 4 -11.579 -15.038 32.540 1.00 55.41 A O ANISOU 24 O ASN A 4 10526 5890 4637 251 -47 -143 A O ATOM 25 CB ASN A 4 -10.786 -16.480 35.176 1.00 89.56 A C ANISOU 25 CB ASN A 4 15570 10124 8335 155 -196 14 A C ATOM 26 CG ASN A 4 -10.662 -17.594 36.198 1.00 96.64 A C ANISOU 26 CG ASN A 4 16866 10920 8934 130 -234 110 A C ATOM 27 ND2 ASN A 4 -10.553 -18.828 35.721 1.00 97.23 A N ANISOU 27 ND2 ASN A 4 17104 10885 8954 298 -260 224 A N ATOM 28 OD1 ASN A 4 -10.671 -17.348 37.405 1.00101.16 A O ANISOU 28 OD1 ASN A 4 17611 11504 9322 -44 -235 82 A O ATOM 29 N LEU A 5 -13.297 -14.630 33.934 1.00 58.10 A N ANISOU 29 N LEU A 5 11097 6094 4885 -156 268 -355 A N ATOM 30 CA LEU A 5 -13.707 -13.414 33.244 1.00 47.91 A C ANISOU 30 CA LEU A 5 9463 4874 3868 -191 359 -459 A C ATOM 31 C LEU A 5 -13.770 -12.202 34.166 1.00 43.80 A C ANISOU 31 C LEU A 5 8909 4398 3337 -361 425 -572 A C ATOM 32 O LEU A 5 -14.096 -12.317 35.348 1.00 44.72 A O ANISOU 32 O LEU A 5 9281 4450 3259 -534 506 -625 A O ATOM 33 CB LEU A 5 -15.069 -13.614 32.577 1.00 37.81 A C ANISOU 33 CB LEU A 5 8114 3507 2744 -282 577 -537 A C ATOM 34 CG LEU A 5 -15.154 -14.679 31.484 1.00 40.74 A C ANISOU 34 CG LEU A 5 8490 3832 3157 -148 543 -449 A C ATOM 35 CD1 LEU A 5 -16.603 -14.938 31.108 1.00 41.23 A C ANISOU 35 CD1 LEU A 5 8542 3814 3311 -307 768 -527 A C ATOM 36 CD2 LEU A 5 -14.344 -14.263 30.267 1.00 44.04 A C ANISOU 36 CD2 LEU A 5 8599 4365 3768 62 395 -383 A C ATOM 37 N ILE A 6 -13.449 -11.040 33.607 1.00 37.10 A N ANISOU 37 N ILE A 6 7753 3651 2691 -318 395 -610 A N ATOM 38 CA ILE A 6 -13.625 -9.772 34.299 1.00 37.62 A C ANISOU 38 CA ILE A 6 7765 3739 2790 -481 495 -735 A C ATOM 39 C ILE A 6 -14.668 -8.968 33.544 1.00 31.21 A C ANISOU 39 C ILE A 6 6692 2898 2268 -522 704 -841 A C ATOM 40 O ILE A 6 -14.409 -8.491 32.440 1.00 36.91 A O ANISOU 40 O ILE A 6 7120 3695 3209 -390 641 -811 A O ATOM 41 CB ILE A 6 -12.328 -8.956 34.332 1.00 40.94 A C ANISOU 41 CB ILE A 6 8050 4306 3199 -413 287 -689 A C ATOM 42 CG1 ILE A 6 -11.125 -9.861 34.603 1.00 47.24 A C ANISOU 42 CG1 ILE A 6 8995 5180 3773 -280 29 -523 A C ATOM 43 CG2 ILE A 6 -12.429 -7.849 35.373 1.00 32.45 A C ANISOU 43 CG2 ILE A 6 7046 3226 2059 -624 386 -816 A C ATOM 44 CD1 ILE A 6 -9.794 -9.168 34.404 1.00 42.20 A C ANISOU 44 CD1 ILE A 6 8169 4720 3143 -184 -199 -445 A C ATOM 45 N TRP A 7 -15.845 -8.818 34.138 1.00 37.64 A N ANISOU 45 N TRP A 7 7608 3610 3082 -702 953 -957 A N ATOM 46 CA TRP A 7 -16.957 -8.175 33.456 1.00 36.58 A C ANISOU 46 CA TRP A 7 7230 3450 3219 -735 1169 -1038 A C ATOM 47 C TRP A 7 -17.251 -6.791 34.024 1.00 30.32 A C ANISOU 47 C TRP A 7 6364 2641 2517 -855 1332 -1170 A C ATOM 48 O TRP A 7 -17.726 -6.664 35.151 1.00 31.92 A O ANISOU 48 O TRP A 7 6787 2765 2577 -1028 1488 -1265 A O ATOM 49 CB TRP A 7 -18.205 -9.051 33.554 1.00 52.73 A C ANISOU 49 CB TRP A 7 9403 5400 5231 -838 1359 -1061 A C ATOM 50 CG TRP A 7 -19.127 -8.906 32.391 1.00 59.48 A C ANISOU 50 CG TRP A 7 9972 6273 6356 -800 1481 -1059 A C ATOM 51 CD1 TRP A 7 -19.779 -7.775 31.996 1.00 63.48 A C ANISOU 51 CD1 TRP A 7 10202 6801 7118 -819 1644 -1128 A C ATOM 52 CD2 TRP A 7 -19.509 -9.936 31.471 1.00 56.54 A C ANISOU 52 CD2 TRP A 7 9567 5900 6016 -744 1452 -976 A C ATOM 53 CE2 TRP A 7 -20.394 -9.350 30.542 1.00 55.43 A C ANISOU 53 CE2 TRP A 7 9109 5800 6150 -745 1589 -995 A C ATOM 54 CE3 TRP A 7 -19.189 -11.289 31.344 1.00 52.57 A C ANISOU 54 CE3 TRP A 7 9283 5359 5331 -696 1328 -885 A C ATOM 55 NE1 TRP A 7 -20.541 -8.036 30.883 1.00 60.84 A N ANISOU 55 NE1 TRP A 7 9645 6498 6975 -779 1705 -1081 A N ATOM 56 CZ2 TRP A 7 -20.960 -10.080 29.498 1.00 42.18 A C ANISOU 56 CZ2 TRP A 7 7326 4143 4558 -724 1596 -927 A C ATOM 57 CZ3 TRP A 7 -19.753 -12.009 30.306 1.00 49.31 A C ANISOU 57 CZ3 TRP A 7 8786 4945 5005 -671 1350 -830 A C ATOM 58 CH2 TRP A 7 -20.629 -11.403 29.396 1.00 43.10 A C ANISOU 58 CH2 TRP A 7 7679 4216 4482 -696 1478 -852 A C ATOM 59 N LEU A 8 -16.969 -5.758 33.235 1.00 29.14 A N ANISOU 59 N LEU A 8 5917 2555 2599 -765 1304 -1177 A N ATOM 60 CA LEU A 8 -17.302 -4.387 33.610 1.00 29.67 A C ANISOU 60 CA LEU A 8 5897 2587 2788 -860 1481 -1300 A C ATOM 61 C LEU A 8 -18.520 -3.899 32.837 1.00 29.86 A C ANISOU 61 C LEU A 8 5660 2577 3106 -842 1711 -1338 A C ATOM 62 O LEU A 8 -18.784 -4.355 31.724 1.00 35.36 A O ANISOU 62 O LEU A 8 6157 3324 3955 -728 1662 -1254 A O ATOM 63 CB LEU A 8 -16.125 -3.445 33.352 1.00 31.89 A C ANISOU 63 CB LEU A 8 6042 2957 3116 -791 1301 -1282 A C ATOM 64 CG LEU A 8 -14.992 -3.410 34.378 1.00 36.70 A C ANISOU 64 CG LEU A 8 6890 3610 3445 -870 1129 -1277 A C ATOM 65 CD1 LEU A 8 -14.306 -4.762 34.476 1.00 33.70 A C ANISOU 65 CD1 LEU A 8 6672 3287 2846 -792 903 -1145 A C ATOM 66 CD2 LEU A 8 -13.994 -2.324 34.012 1.00 41.77 A C ANISOU 66 CD2 LEU A 8 7352 4348 4172 -826 987 -1270 A C ATOM 67 N LYS A 9 -19.255 -2.964 33.428 1.00 30.00 A N ANISOU 67 N LYS A 9 5683 2514 3201 -954 1965 -1460 A N ATOM 68 CA LYS A 9 -20.436 -2.407 32.783 1.00 49.14 A C ANISOU 68 CA LYS A 9 7849 4912 5912 -931 2202 -1486 A C ATOM 69 C LYS A 9 -20.050 -1.442 31.668 1.00 40.28 A C ANISOU 69 C LYS A 9 6393 3853 5058 -787 2126 -1444 A C ATOM 70 O LYS A 9 -20.554 -1.537 30.550 1.00 42.57 A O ANISOU 70 O LYS A 9 6412 4197 5566 -687 2135 -1369 A O ATOM 71 CB LYS A 9 -21.326 -1.703 33.808 1.00 60.39 A C ANISOU 71 CB LYS A 9 9393 6219 7333 -1079 2518 -1626 A C ATOM 72 CG LYS A 9 -21.858 -2.622 34.895 1.00 72.00 A C ANISOU 72 CG LYS A 9 11181 7626 8550 -1238 2626 -1673 A C ATOM 73 CD LYS A 9 -22.774 -1.875 35.851 1.00 82.11 A C ANISOU 73 CD LYS A 9 12562 8793 9844 -1378 2963 -1815 A C ATOM 74 CE LYS A 9 -24.062 -1.456 35.163 1.00 88.16 A C ANISOU 74 CE LYS A 9 13030 9555 10912 -1324 3218 -1810 A C ATOM 75 NZ LYS A 9 -24.867 -2.632 34.730 1.00 87.78 A N1+ ANISOU 75 NZ LYS A 9 12933 9561 10857 -1337 3230 -1727 A N1+ ATOM 76 N GLU A 10 -19.149 -0.517 31.978 1.00 32.41 A N ANISOU 76 N GLU A 10 5423 2856 4036 -792 2048 -1490 A N ATOM 77 CA GLU A 10 -18.730 0.488 31.012 1.00 36.95 A C ANISOU 77 CA GLU A 10 5707 3481 4849 -674 1981 -1458 A C ATOM 78 C GLU A 10 -17.275 0.884 31.236 1.00 45.61 A C ANISOU 78 C GLU A 10 6882 4640 5808 -671 1741 -1451 A C ATOM 79 O GLU A 10 -16.833 1.057 32.373 1.00 47.24 A O ANISOU 79 O GLU A 10 7355 4805 5791 -805 1743 -1527 A O ATOM 80 CB GLU A 10 -19.634 1.719 31.102 1.00 45.28 A C ANISOU 80 CB GLU A 10 6642 4434 6127 -704 2280 -1550 A C ATOM 81 CG GLU A 10 -19.291 2.827 30.118 1.00 55.42 A C ANISOU 81 CG GLU A 10 7635 5752 7671 -586 2236 -1517 A C ATOM 82 CD GLU A 10 -20.264 3.988 30.201 1.00 73.95 A C ANISOU 82 CD GLU A 10 9870 7981 10247 -595 2553 -1594 A C ATOM 83 OE1 GLU A 10 -19.952 5.069 29.658 1.00 72.25 A O ANISOU 83 OE1 GLU A 10 9483 7754 10215 -527 2552 -1592 A O ATOM 84 OE2 GLU A 10 -21.342 3.818 30.810 1.00 88.98 A O1- ANISOU 84 OE2 GLU A 10 11859 9802 12148 -666 2811 -1653 A O1- ATOM 85 N VAL A 11 -16.536 1.022 30.141 1.00 39.78 A N ANISOU 85 N VAL A 11 5907 4013 5194 -529 1532 -1354 A N ATOM 86 CA VAL A 11 -15.130 1.399 30.203 1.00 33.42 A C ANISOU 86 CA VAL A 11 5123 3298 4276 -516 1289 -1326 A C ATOM 87 C VAL A 11 -14.718 2.115 28.924 1.00 26.62 A C ANISOU 87 C VAL A 11 3933 2520 3662 -380 1185 -1261 A C ATOM 88 O VAL A 11 -15.422 2.057 27.917 1.00 33.94 A O ANISOU 88 O VAL A 11 4624 3453 4820 -278 1253 -1212 A O ATOM 89 CB VAL A 11 -14.225 0.171 30.393 1.00 38.44 A C ANISOU 89 CB VAL A 11 5910 4034 4662 -475 1028 -1228 A C ATOM 90 CG1 VAL A 11 -14.006 -0.528 29.060 1.00 29.31 A C ANISOU 90 CG1 VAL A 11 4524 2980 3634 -287 866 -1095 A C ATOM 91 CG2 VAL A 11 -12.898 0.583 31.002 1.00 53.73 A C ANISOU 91 CG2 VAL A 11 7959 6054 6402 -534 829 -1223 A C ATOM 92 N ASP A 12 -13.573 2.787 28.968 1.00 25.52 A N ANISOU 92 N ASP A 12 3779 2454 3464 -392 1016 -1256 A N ATOM 93 CA ASP A 12 -13.067 3.506 27.806 1.00 29.53 A C ANISOU 93 CA ASP A 12 3990 3046 4183 -278 903 -1195 A C ATOM 94 C ASP A 12 -12.683 2.559 26.668 1.00 30.50 A C ANISOU 94 C ASP A 12 3929 3304 4357 -105 696 -1053 A C ATOM 95 O ASP A 12 -13.067 2.772 25.518 1.00 29.35 A O ANISOU 95 O ASP A 12 3516 3182 4452 1 717 -1002 A O ATOM 96 CB ASP A 12 -11.882 4.399 28.190 1.00 29.90 A C ANISOU 96 CB ASP A 12 4085 3153 4122 -359 763 -1221 A C ATOM 97 CG ASP A 12 -10.723 3.618 28.790 1.00 40.94 A C ANISOU 97 CG ASP A 12 5656 4680 5220 -386 507 -1158 A C ATOM 98 OD1 ASP A 12 -9.592 4.149 28.794 1.00 32.56 A O ANISOU 98 OD1 ASP A 12 4559 3734 4079 -416 322 -1129 A O ATOM 99 OD2 ASP A 12 -10.936 2.479 29.257 1.00 24.27 A O1- ANISOU 99 OD2 ASP A 12 3711 2561 2949 -379 490 -1128 A O1- ATOM 100 N SER A 13 -11.931 1.514 26.997 1.00 33.29 A N ANISOU 100 N SER A 13 4431 3739 4478 -78 503 -985 A N ATOM 101 CA SER A 13 -11.512 0.523 26.012 1.00 27.55 A C ANISOU 101 CA SER A 13 3578 3121 3768 90 319 -855 A C ATOM 102 C SER A 13 -10.788 -0.633 26.688 1.00 25.49 A C ANISOU 102 C SER A 13 3553 2911 3220 107 155 -792 A C ATOM 103 O SER A 13 -9.811 -0.427 27.408 1.00 21.50 A O ANISOU 103 O SER A 13 3163 2477 2530 55 16 -784 A O ATOM 104 CB SER A 13 -10.606 1.155 24.954 1.00 27.28 A C ANISOU 104 CB SER A 13 3271 3222 3873 198 144 -784 A C ATOM 105 OG SER A 13 -10.128 0.176 24.048 1.00 17.39 A O ANISOU 105 OG SER A 13 1917 2073 2616 360 -28 -662 A O ATOM 106 N THR A 14 -11.273 -1.848 26.451 1.00 31.61 A N ANISOU 106 N THR A 14 4404 3653 3955 175 171 -740 A N ATOM 107 CA THR A 14 -10.673 -3.039 27.041 1.00 20.96 A C ANISOU 107 CA THR A 14 3291 2329 2344 212 32 -668 A C ATOM 108 C THR A 14 -9.206 -3.157 26.642 1.00 24.23 A C ANISOU 108 C THR A 14 3609 2911 2687 351 -242 -549 A C ATOM 109 O THR A 14 -8.385 -3.672 27.400 1.00 22.51 A O ANISOU 109 O THR A 14 3569 2749 2234 358 -386 -490 A O ATOM 110 CB THR A 14 -11.432 -4.318 26.638 1.00 23.90 A C ANISOU 110 CB THR A 14 3745 2629 2708 273 97 -625 A C ATOM 111 CG2 THR A 14 -12.863 -4.273 27.157 1.00 28.08 A C ANISOU 111 CG2 THR A 14 4380 3013 3276 120 365 -732 A C ATOM 112 OG1 THR A 14 -11.453 -4.436 25.211 1.00 18.89 A O ANISOU 112 OG1 THR A 14 2853 2051 2272 413 49 -558 A O ATOM 113 N GLN A 15 -8.887 -2.672 25.446 1.00 19.30 A N ANISOU 113 N GLN A 15 2693 2374 2265 462 -312 -507 A N ATOM 114 CA GLN A 15 -7.507 -2.617 24.980 1.00 23.73 A C ANISOU 114 CA GLN A 15 3117 3110 2788 590 -557 -399 A C ATOM 115 C GLN A 15 -6.687 -1.681 25.859 1.00 24.05 A C ANISOU 115 C GLN A 15 3197 3232 2707 467 -646 -428 A C ATOM 116 O GLN A 15 -5.607 -2.040 26.328 1.00 23.55 A O ANISOU 116 O GLN A 15 3209 3294 2446 504 -839 -339 A O ATOM 117 CB GLN A 15 -7.456 -2.140 23.528 1.00 26.71 A C ANISOU 117 CB GLN A 15 3172 3557 3422 701 -585 -366 A C ATOM 118 CG GLN A 15 -7.933 -3.171 22.521 1.00 27.23 A C ANISOU 118 CG GLN A 15 3187 3589 3570 836 -560 -305 A C ATOM 119 CD GLN A 15 -6.933 -4.291 22.325 1.00 24.73 A C ANISOU 119 CD GLN A 15 2940 3360 3098 1010 -745 -176 A C ATOM 120 NE2 GLN A 15 -7.256 -5.467 22.846 1.00 17.33 A N ANISOU 120 NE2 GLN A 15 2261 2327 1998 1027 -707 -154 A N ATOM 121 OE1 GLN A 15 -5.883 -4.103 21.709 1.00 24.33 A O ANISOU 121 OE1 GLN A 15 2713 3459 3072 1133 -914 -93 A O ATOM 122 N GLU A 16 -7.207 -0.478 26.079 1.00 20.37 A N ANISOU 122 N GLU A 16 2686 2699 2357 317 -501 -548 A N ATOM 123 CA GLU A 16 -6.512 0.517 26.886 1.00 38.91 A C ANISOU 123 CA GLU A 16 5089 5105 4591 165 -559 -596 A C ATOM 124 C GLU A 16 -6.324 0.035 28.320 1.00 41.83 A C ANISOU 124 C GLU A 16 5777 5453 4663 37 -579 -611 A C ATOM 125 O GLU A 16 -5.279 0.261 28.927 1.00 28.68 A O ANISOU 125 O GLU A 16 4170 3919 2809 -30 -751 -566 A O ATOM 126 CB GLU A 16 -7.269 1.845 26.879 1.00 43.85 A C ANISOU 126 CB GLU A 16 5648 5613 5400 30 -352 -733 A C ATOM 127 CG GLU A 16 -6.486 3.005 27.479 1.00 49.95 A C ANISOU 127 CG GLU A 16 6451 6445 6083 -130 -414 -784 A C ATOM 128 CD GLU A 16 -5.300 3.409 26.624 1.00 53.98 A C ANISOU 128 CD GLU A 16 6713 7152 6644 -42 -645 -684 A C ATOM 129 OE1 GLU A 16 -5.335 3.153 25.402 1.00 51.89 A O ANISOU 129 OE1 GLU A 16 6212 6936 6569 133 -689 -611 A O ATOM 130 OE2 GLU A 16 -4.337 3.986 27.172 1.00 61.78 A O1- ANISOU 130 OE2 GLU A 16 7744 8254 7476 -163 -780 -677 A O1- ATOM 131 N ARG A 17 -7.341 -0.633 28.855 1.00 23.95 A N ANISOU 131 N ARG A 17 3716 3034 2351 -8 -407 -667 A N ATOM 132 CA ARG A 17 -7.294 -1.120 30.228 1.00 30.02 A C ANISOU 132 CA ARG A 17 4806 3764 2837 -142 -404 -687 A C ATOM 133 C ARG A 17 -6.199 -2.162 30.438 1.00 29.96 A C ANISOU 133 C ARG A 17 4874 3900 2607 -27 -659 -525 A C ATOM 134 O ARG A 17 -5.518 -2.159 31.462 1.00 31.41 A O ANISOU 134 O ARG A 17 5231 4158 2546 -138 -771 -499 A O ATOM 135 CB ARG A 17 -8.651 -1.690 30.643 1.00 26.00 A C ANISOU 135 CB ARG A 17 4481 3064 2335 -203 -161 -772 A C ATOM 136 CG ARG A 17 -9.727 -0.641 30.870 1.00 26.12 A C ANISOU 136 CG ARG A 17 4490 2932 2503 -353 115 -936 A C ATOM 137 CD ARG A 17 -9.251 0.453 31.826 1.00 27.70 A C ANISOU 137 CD ARG A 17 4809 3139 2577 -551 126 -1026 A C ATOM 138 NE ARG A 17 -8.546 1.530 31.134 1.00 36.75 A N ANISOU 138 NE ARG A 17 5718 4381 3864 -526 29 -1017 A N ATOM 139 CZ ARG A 17 -7.900 2.516 31.748 1.00 32.24 A C ANISOU 139 CZ ARG A 17 5213 3849 3187 -689 -11 -1073 A C ATOM 140 NH1 ARG A 17 -7.290 3.453 31.038 1.00 31.78 A N1+ ANISOU 140 NH1 ARG A 17 4935 3876 3265 -666 -97 -1059 A N1+ ATOM 141 NH2 ARG A 17 -7.860 2.564 33.071 1.00 45.02 A N ANISOU 141 NH2 ARG A 17 7128 5423 4553 -892 34 -1144 A N ATOM 142 N LEU A 18 -6.028 -3.051 29.465 1.00 25.36 A N ANISOU 142 N LEU A 18 4167 3360 2110 196 -746 -412 A N ATOM 143 CA LEU A 18 -5.010 -4.090 29.565 1.00 30.32 A C ANISOU 143 CA LEU A 18 4857 4112 2552 348 -970 -244 A C ATOM 144 C LEU A 18 -3.611 -3.554 29.275 1.00 26.38 A C ANISOU 144 C LEU A 18 4155 3844 2026 411 -1211 -139 A C ATOM 145 O LEU A 18 -2.619 -4.265 29.435 1.00 37.20 A O ANISOU 145 O LEU A 18 5548 5352 3234 535 -1412 16 A O ATOM 146 CB LEU A 18 -5.340 -5.265 28.643 1.00 24.99 A C ANISOU 146 CB LEU A 18 4152 3378 1965 562 -954 -166 A C ATOM 147 CG LEU A 18 -6.580 -6.064 29.046 1.00 25.16 A C ANISOU 147 CG LEU A 18 4415 3196 1947 497 -753 -234 A C ATOM 148 CD1 LEU A 18 -6.707 -7.319 28.201 1.00 25.07 A C ANISOU 148 CD1 LEU A 18 4416 3140 1972 698 -769 -139 A C ATOM 149 CD2 LEU A 18 -6.528 -6.415 30.524 1.00 28.86 A C ANISOU 149 CD2 LEU A 18 5205 3625 2135 353 -758 -242 A C ATOM 150 N LYS A 19 -3.535 -2.299 28.847 1.00 31.75 A N ANISOU 150 N LYS A 19 4620 5355 2089 -412 -584 -72 A N ATOM 151 CA LYS A 19 -2.249 -1.648 28.638 1.00 29.54 A C ANISOU 151 CA LYS A 19 4374 5214 1637 -578 -556 -27 A C ATOM 152 C LYS A 19 -1.720 -1.102 29.956 1.00 33.92 A C ANISOU 152 C LYS A 19 4901 5959 2027 -884 -458 -94 A C ATOM 153 O LYS A 19 -0.510 -1.029 30.170 1.00 44.35 A O ANISOU 153 O LYS A 19 6159 7527 3164 -1055 -458 -19 A O ATOM 154 CB LYS A 19 -2.376 -0.517 27.619 1.00 25.51 A C ANISOU 154 CB LYS A 19 4046 4458 1190 -546 -528 -80 A C ATOM 155 CG LYS A 19 -2.560 -0.986 26.186 1.00 32.72 A C ANISOU 155 CG LYS A 19 4989 5247 2197 -282 -634 10 A C ATOM 156 CD LYS A 19 -2.644 0.192 25.230 1.00 37.03 A C ANISOU 156 CD LYS A 19 5725 5563 2783 -272 -608 -22 A C ATOM 157 CE LYS A 19 -2.833 -0.269 23.793 1.00 36.89 A C ANISOU 157 CE LYS A 19 5743 5442 2832 -20 -718 69 A C ATOM 158 NZ LYS A 19 -2.996 0.887 22.869 1.00 34.18 A N1+ ANISOU 158 NZ LYS A 19 5593 4867 2527 -5 -701 56 A N1+ ATOM 159 N GLU A 20 -2.637 -0.717 30.838 1.00 32.14 A N ANISOU 159 N GLU A 20 4718 5633 1862 -956 -374 -240 A N ATOM 160 CA GLU A 20 -2.269 -0.171 32.137 1.00 36.48 A C ANISOU 160 CA GLU A 20 5263 6350 2247 -1254 -272 -334 A C ATOM 161 C GLU A 20 -2.269 -1.247 33.214 1.00 36.50 A C ANISOU 161 C GLU A 20 5095 6610 2164 -1302 -301 -267 A C ATOM 162 O GLU A 20 -1.456 -1.213 34.138 1.00 33.68 A O ANISOU 162 O GLU A 20 4669 6527 1602 -1541 -279 -246 A O ATOM 163 CB GLU A 20 -3.225 0.952 32.533 1.00 53.16 A C ANISOU 163 CB GLU A 20 7535 8208 4456 -1318 -140 -552 A C ATOM 164 CG GLU A 20 -3.125 2.189 31.663 1.00 71.25 A C ANISOU 164 CG GLU A 20 10023 10243 6807 -1325 -97 -620 A C ATOM 165 CD GLU A 20 -3.978 3.327 32.183 1.00 88.98 A C ANISOU 165 CD GLU A 20 12431 12240 9139 -1395 47 -842 A C ATOM 166 OE1 GLU A 20 -4.832 3.078 33.059 1.00 95.57 A O ANISOU 166 OE1 GLU A 20 13211 13080 10020 -1382 111 -945 A O ATOM 167 OE2 GLU A 20 -3.794 4.471 31.717 1.00 95.87 A O1- ANISOU 167 OE2 GLU A 20 13487 12907 10032 -1463 104 -911 A O1- ATOM 168 N TRP A 21 -3.189 -2.197 33.096 1.00 27.08 A N ANISOU 168 N TRP A 21 3835 5331 1123 -1085 -356 -225 A N ATOM 169 CA TRP A 21 -3.297 -3.267 34.078 1.00 31.90 A C ANISOU 169 CA TRP A 21 4298 6153 1671 -1118 -385 -144 A C ATOM 170 C TRP A 21 -2.504 -4.495 33.657 1.00 31.71 A C ANISOU 170 C TRP A 21 4142 6301 1606 -990 -523 77 A C ATOM 171 O TRP A 21 -2.488 -4.867 32.482 1.00 28.75 A O ANISOU 171 O TRP A 21 3784 5795 1346 -769 -603 147 A O ATOM 172 CB TRP A 21 -4.760 -3.642 34.318 1.00 32.90 A C ANISOU 172 CB TRP A 21 4418 6102 1979 -988 -356 -223 A C ATOM 173 CG TRP A 21 -5.624 -2.475 34.674 1.00 42.24 A C ANISOU 173 CG TRP A 21 5719 7099 3230 -1063 -212 -446 A C ATOM 174 CD1 TRP A 21 -5.213 -1.266 35.158 1.00 59.68 A C ANISOU 174 CD1 TRP A 21 8038 9320 5319 -1285 -96 -587 A C ATOM 175 CD2 TRP A 21 -7.055 -2.413 34.601 1.00 31.09 A C ANISOU 175 CD2 TRP A 21 4324 5461 2028 -913 -163 -558 A C ATOM 176 CE2 TRP A 21 -7.435 -1.130 35.044 1.00 42.81 A C ANISOU 176 CE2 TRP A 21 5930 6821 3514 -1031 -10 -767 A C ATOM 177 CE3 TRP A 21 -8.045 -3.314 34.200 1.00 34.84 A C ANISOU 177 CE3 TRP A 21 4719 5828 2690 -697 -235 -505 A C ATOM 178 NE1 TRP A 21 -6.296 -0.451 35.375 1.00 58.12 A N ANISOU 178 NE1 TRP A 21 7937 8895 5249 -1263 29 -786 A N ATOM 179 CZ2 TRP A 21 -8.770 -0.728 35.095 1.00 45.15 A C ANISOU 179 CZ2 TRP A 21 6254 6901 4001 -912 79 -918 A C ATOM 180 CZ3 TRP A 21 -9.368 -2.911 34.252 1.00 30.14 A C ANISOU 180 CZ3 TRP A 21 4140 5037 2276 -604 -156 -649 A C ATOM 181 CH2 TRP A 21 -9.718 -1.629 34.696 1.00 33.71 A C ANISOU 181 CH2 TRP A 21 4697 5379 2732 -698 2 -851 A C ATOM 182 N ASN A 22 -1.839 -5.115 34.626 1.00 36.15 A N ANISOU 182 N ASN A 22 4576 7160 1998 -1127 -548 188 A N ATOM 183 CA ASN A 22 -1.079 -6.335 34.385 1.00 40.05 A C ANISOU 183 CA ASN A 22 4935 7828 2456 -997 -672 406 A C ATOM 184 C ASN A 22 -1.894 -7.571 34.747 1.00 37.36 A C ANISOU 184 C ASN A 22 4528 7445 2222 -859 -727 489 A C ATOM 185 O ASN A 22 -1.955 -7.966 35.912 1.00 44.62 A O ANISOU 185 O ASN A 22 5373 8543 3038 -998 -713 535 A O ATOM 186 CB ASN A 22 0.230 -6.321 35.178 1.00 48.34 A C ANISOU 186 CB ASN A 22 5867 9244 3254 -1213 -687 513 A C ATOM 187 CG ASN A 22 1.168 -5.211 34.741 1.00 57.10 A C ANISOU 187 CG ASN A 22 7024 10420 4252 -1361 -647 458 A C ATOM 188 ND2 ASN A 22 2.114 -4.864 35.606 1.00 65.23 A N ANISOU 188 ND2 ASN A 22 7974 11759 5053 -1628 -634 488 A N ATOM 189 OD1 ASN A 22 1.047 -4.675 33.640 1.00 57.38 A O ANISOU 189 OD1 ASN A 22 7166 10240 4397 -1249 -633 397 A O ATOM 190 N VAL A 23 -2.522 -8.172 33.743 1.00 34.74 A N ANISOU 190 N VAL A 23 4230 6878 2090 -600 -793 509 A N ATOM 191 CA VAL A 23 -3.347 -9.355 33.951 1.00 43.08 A C ANISOU 191 CA VAL A 23 5241 7857 3272 -472 -851 583 A C ATOM 192 C VAL A 23 -2.593 -10.614 33.538 1.00 45.08 A C ANISOU 192 C VAL A 23 5404 8176 3550 -302 -957 783 A C ATOM 193 O VAL A 23 -1.663 -10.554 32.734 1.00 45.93 A O ANISOU 193 O VAL A 23 5484 8297 3669 -216 -962 825 A O ATOM 194 CB VAL A 23 -4.658 -9.269 33.147 1.00 36.52 A C ANISOU 194 CB VAL A 23 4498 6704 2674 -306 -850 463 A C ATOM 195 CG1 VAL A 23 -4.381 -9.473 31.666 1.00 38.55 A C ANISOU 195 CG1 VAL A 23 4810 6809 3027 -77 -939 497 A C ATOM 196 CG2 VAL A 23 -5.660 -10.295 33.649 1.00 46.73 A C ANISOU 196 CG2 VAL A 23 5739 7937 4079 -260 -879 507 A C ATOM 197 N SER A 24 -2.994 -11.752 34.093 1.00 44.70 A N ANISOU 197 N SER A 24 5297 8139 3547 -258 -1007 895 A N ATOM 198 CA SER A 24 -2.374 -13.025 33.753 1.00 49.63 A C ANISOU 198 CA SER A 24 5841 8762 4256 -86 -1070 1066 A C ATOM 199 C SER A 24 -2.951 -13.575 32.454 1.00 48.25 A C ANISOU 199 C SER A 24 5749 8285 4300 164 -1116 1022 A C ATOM 200 O SER A 24 -4.012 -13.143 32.005 1.00 53.59 A O ANISOU 200 O SER A 24 6519 8767 5073 197 -1121 891 A O ATOM 201 CB SER A 24 -2.564 -14.034 34.887 1.00 56.09 A C ANISOU 201 CB SER A 24 6587 9698 5026 -151 -1112 1219 A C ATOM 202 OG SER A 24 -3.938 -14.210 35.188 1.00 63.09 A O ANISOU 202 OG SER A 24 7542 10447 5983 -173 -1128 1158 A O ATOM 203 N TYR A 25 -2.245 -14.526 31.851 1.00 48.20 A N ANISOU 203 N TYR A 25 5707 8249 4357 340 -1150 1126 A N ATOM 204 CA TYR A 25 -2.712 -15.158 30.623 1.00 48.67 A C ANISOU 204 CA TYR A 25 5859 8036 4597 565 -1192 1074 A C ATOM 205 C TYR A 25 -3.923 -16.035 30.902 1.00 54.06 A C ANISOU 205 C TYR A 25 6586 8545 5409 594 -1257 1088 A C ATOM 206 O TYR A 25 -4.073 -16.570 31.999 1.00 62.58 A O ANISOU 206 O TYR A 25 7606 9733 6438 493 -1279 1204 A O ATOM 207 CB TYR A 25 -1.599 -15.992 29.986 1.00 54.97 A C ANISOU 207 CB TYR A 25 6618 8869 5398 743 -1205 1171 A C ATOM 208 CG TYR A 25 -0.328 -15.217 29.729 1.00 49.93 A C ANISOU 208 CG TYR A 25 5904 8443 4622 712 -1149 1184 A C ATOM 209 CD1 TYR A 25 -0.239 -14.326 28.667 1.00 42.18 A C ANISOU 209 CD1 TYR A 25 4995 7385 3647 750 -1112 1061 A C ATOM 210 CD2 TYR A 25 0.782 -15.376 30.549 1.00 58.20 A C ANISOU 210 CD2 TYR A 25 6801 9785 5526 635 -1142 1333 A C ATOM 211 CE1 TYR A 25 0.918 -13.614 28.429 1.00 39.50 A C ANISOU 211 CE1 TYR A 25 4584 7250 3175 702 -1066 1085 A C ATOM 212 CE2 TYR A 25 1.945 -14.671 30.320 1.00 59.76 A C ANISOU 212 CE2 TYR A 25 6912 10203 5592 589 -1101 1353 A C ATOM 213 CZ TYR A 25 2.009 -13.791 29.258 1.00 51.02 A C ANISOU 213 CZ TYR A 25 5882 9010 4495 616 -1061 1227 A C ATOM 214 OH TYR A 25 3.167 -13.084 29.025 1.00 51.75 A O ANISOU 214 OH TYR A 25 5885 9331 4446 550 -1024 1257 A O ATOM 215 N GLY A 26 -4.788 -16.176 29.903 1.00 56.31 A N ANISOU 215 N GLY A 26 6973 8573 5848 720 -1295 979 A N ATOM 216 CA GLY A 26 -5.990 -16.975 30.049 1.00 61.29 A C ANISOU 216 CA GLY A 26 7640 9035 6612 739 -1369 984 A C ATOM 217 C GLY A 26 -7.104 -16.202 30.725 1.00 62.91 A C ANISOU 217 C GLY A 26 7828 9265 6809 590 -1364 911 A C ATOM 218 O GLY A 26 -8.047 -16.788 31.256 1.00 63.55 A O ANISOU 218 O GLY A 26 7892 9300 6954 545 -1419 950 A O ATOM 219 N THR A 27 -6.989 -14.878 30.708 1.00 57.17 A N ANISOU 219 N THR A 27 7107 8618 5996 514 -1301 805 A N ATOM 220 CA THR A 27 -8.002 -14.015 31.300 1.00 54.07 A C ANISOU 220 CA THR A 27 6703 8223 5618 377 -1237 684 A C ATOM 221 C THR A 27 -8.516 -13.007 30.280 1.00 43.14 A C ANISOU 221 C THR A 27 5394 6671 4325 460 -1225 522 A C ATOM 222 O THR A 27 -7.734 -12.345 29.596 1.00 36.11 A O ANISOU 222 O THR A 27 4560 5800 3363 510 -1222 500 A O ATOM 223 CB THR A 27 -7.462 -13.263 32.530 1.00 58.68 A C ANISOU 223 CB THR A 27 7230 9049 6015 154 -1121 681 A C ATOM 224 CG2 THR A 27 -8.558 -12.421 33.167 1.00 46.88 A C ANISOU 224 CG2 THR A 27 5726 7520 4567 17 -1005 523 A C ATOM 225 OG1 THR A 27 -6.972 -14.204 33.494 1.00 68.43 A O ANISOU 225 OG1 THR A 27 8391 10459 7150 76 -1146 854 A O ATOM 226 N ALA A 28 -9.835 -12.902 30.176 1.00 34.91 A N ANISOU 226 N ALA A 28 4347 5474 3443 474 -1221 421 A N ATOM 227 CA ALA A 28 -10.452 -11.984 29.231 1.00 33.00 A C ANISOU 227 CA ALA A 28 4168 5066 3306 568 -1223 283 A C ATOM 228 C ALA A 28 -11.188 -10.862 29.954 1.00 37.21 A C ANISOU 228 C ALA A 28 4671 5606 3860 444 -1089 146 A C ATOM 229 O ALA A 28 -11.959 -11.107 30.883 1.00 30.00 A O ANISOU 229 O ALA A 28 3674 4737 2989 342 -1028 125 A O ATOM 230 CB ALA A 28 -11.400 -12.732 28.305 1.00 35.88 A C ANISOU 230 CB ALA A 28 4546 5234 3853 721 -1346 271 A C ATOM 231 N LEU A 29 -10.937 -9.630 29.525 1.00 35.31 A N ANISOU 231 N LEU A 29 4507 5318 3589 455 -1034 53 A N ATOM 232 CA LEU A 29 -11.634 -8.473 30.066 1.00 28.17 A C ANISOU 232 CA LEU A 29 3603 4376 2724 373 -903 -96 A C ATOM 233 C LEU A 29 -12.832 -8.144 29.186 1.00 35.93 A C ANISOU 233 C LEU A 29 4596 5140 3914 536 -951 -184 A C ATOM 234 O LEU A 29 -12.680 -7.867 27.996 1.00 21.75 A O ANISOU 234 O LEU A 29 2887 3218 2158 679 -1039 -177 A O ATOM 235 CB LEU A 29 -10.697 -7.268 30.143 1.00 24.08 A C ANISOU 235 CB LEU A 29 3178 3907 2062 279 -813 -148 A C ATOM 236 CG LEU A 29 -11.329 -5.976 30.663 1.00 23.31 A C ANISOU 236 CG LEU A 29 3116 3736 2004 202 -666 -319 A C ATOM 237 CD1 LEU A 29 -11.717 -6.119 32.127 1.00 25.92 A C ANISOU 237 CD1 LEU A 29 3354 4217 2278 25 -542 -370 A C ATOM 238 CD2 LEU A 29 -10.386 -4.803 30.467 1.00 23.58 A C ANISOU 238 CD2 LEU A 29 3278 3765 1916 122 -603 -364 A C ATOM 239 N VAL A 30 -14.021 -8.184 29.776 1.00 22.98 A N ANISOU 239 N VAL A 30 2858 3475 2399 512 -895 -258 A N ATOM 240 CA VAL A 30 -15.253 -7.944 29.034 1.00 23.37 A C ANISOU 240 CA VAL A 30 2876 3347 2655 666 -948 -332 A C ATOM 241 C VAL A 30 -15.924 -6.655 29.491 1.00 24.51 A C ANISOU 241 C VAL A 30 3014 3433 2866 651 -798 -487 A C ATOM 242 O VAL A 30 -15.937 -6.338 30.680 1.00 28.63 A O ANISOU 242 O VAL A 30 3495 4068 3315 497 -643 -554 A O ATOM 243 CB VAL A 30 -16.243 -9.112 29.196 1.00 23.89 A C ANISOU 243 CB VAL A 30 2808 3420 2849 676 -1019 -291 A C ATOM 244 CG1 VAL A 30 -17.413 -8.953 28.242 1.00 24.11 A C ANISOU 244 CG1 VAL A 30 2794 3284 3083 843 -1113 -347 A C ATOM 245 CG2 VAL A 30 -15.538 -10.440 28.961 1.00 33.27 A C ANISOU 245 CG2 VAL A 30 4017 4658 3966 671 -1142 -143 A C ATOM 246 N ALA A 31 -16.479 -5.914 28.538 1.00 24.83 A N ANISOU 246 N ALA A 31 3101 3293 3041 818 -845 -542 A N ATOM 247 CA ALA A 31 -17.168 -4.666 28.839 1.00 31.67 A C ANISOU 247 CA ALA A 31 3971 4061 4002 850 -711 -687 A C ATOM 248 C ALA A 31 -18.445 -4.537 28.015 1.00 43.72 A C ANISOU 248 C ALA A 31 5420 5435 5757 1055 -801 -717 A C ATOM 249 O ALA A 31 -18.430 -4.717 26.797 1.00 40.51 A O ANISOU 249 O ALA A 31 5066 4927 5398 1196 -967 -643 A O ATOM 250 CB ALA A 31 -16.251 -3.479 28.593 1.00 26.24 A C ANISOU 250 CB ALA A 31 3466 3294 3210 829 -648 -723 A C ATOM 251 N ASP A 32 -19.548 -4.227 28.687 1.00 28.38 A N ANISOU 251 N ASP A 32 3343 3493 3947 1068 -689 -825 A N ATOM 252 CA ASP A 32 -20.838 -4.089 28.024 1.00 29.46 A C ANISOU 252 CA ASP A 32 3364 3518 4311 1259 -766 -853 A C ATOM 253 C ASP A 32 -20.862 -2.892 27.078 1.00 42.74 A C ANISOU 253 C ASP A 32 5177 4994 6069 1441 -801 -879 A C ATOM 254 O ASP A 32 -21.576 -2.896 26.076 1.00 33.49 A O ANISOU 254 O ASP A 32 3961 3722 5043 1623 -949 -839 A O ATOM 255 CB ASP A 32 -21.956 -3.950 29.059 1.00 33.37 A C ANISOU 255 CB ASP A 32 3670 4087 4924 1230 -606 -970 A C ATOM 256 CG ASP A 32 -22.114 -5.189 29.916 1.00 33.74 A C ANISOU 256 CG ASP A 32 3575 4332 4914 1054 -587 -923 A C ATOM 257 OD1 ASP A 32 -21.993 -6.308 29.376 1.00 42.68 A O ANISOU 257 OD1 ASP A 32 4685 5492 6038 1043 -759 -799 A O ATOM 258 OD2 ASP A 32 -22.367 -5.044 31.130 1.00 42.89 A O1- ANISOU 258 OD2 ASP A 32 4652 5611 6032 924 -397 -1011 A O1- ATOM 259 N ARG A 33 -20.077 -1.870 27.403 1.00 30.27 A N ANISOU 259 N ARG A 33 3763 3353 4385 1380 -670 -939 A N ATOM 260 CA ARG A 33 -20.068 -0.641 26.619 1.00 49.06 A C ANISOU 260 CA ARG A 33 6291 5516 6834 1532 -679 -961 A C ATOM 261 C ARG A 33 -18.676 -0.015 26.596 1.00 42.99 A C ANISOU 261 C ARG A 33 5749 4715 5870 1406 -624 -944 A C ATOM 262 O ARG A 33 -17.887 -0.197 27.523 1.00 29.92 A O ANISOU 262 O ARG A 33 4118 3204 4047 1196 -515 -972 A O ATOM 263 CB ARG A 33 -21.088 0.354 27.183 1.00 37.15 A C ANISOU 263 CB ARG A 33 4718 3900 5499 1632 -519 -1112 A C ATOM 264 CG ARG A 33 -21.397 1.528 26.270 1.00 46.03 A C ANISOU 264 CG ARG A 33 5963 4770 6757 1848 -558 -1113 A C ATOM 265 CD ARG A 33 -22.486 2.414 26.860 1.00 53.69 A C ANISOU 265 CD ARG A 33 6844 5635 7922 1978 -395 -1265 A C ATOM 266 NE ARG A 33 -23.737 1.686 27.060 1.00 66.61 A N ANISOU 266 NE ARG A 33 8196 7393 9720 2067 -428 -1280 A N ATOM 267 CZ ARG A 33 -24.850 2.229 27.542 1.00 74.81 A C ANISOU 267 CZ ARG A 33 9085 8391 10948 2202 -299 -1402 A C ATOM 268 NH1 ARG A 33 -25.940 1.490 27.690 1.00 72.34 A N1+ ANISOU 268 NH1 ARG A 33 8495 8220 10771 2259 -338 -1400 A N1+ ATOM 269 NH2 ARG A 33 -24.873 3.511 27.876 1.00 78.20 A N ANISOU 269 NH2 ARG A 33 9643 8635 11436 2280 -127 -1528 A N ATOM 270 N GLN A 34 -18.380 0.719 25.529 1.00 33.45 A N ANISOU 270 N GLN A 34 4701 3331 4677 1524 -707 -887 A N ATOM 271 CA GLN A 34 -17.091 1.386 25.394 1.00 31.86 A C ANISOU 271 CA GLN A 34 4715 3091 4301 1400 -660 -862 A C ATOM 272 C GLN A 34 -17.263 2.823 24.914 1.00 43.43 A C ANISOU 272 C GLN A 34 6349 4292 5858 1512 -612 -903 A C ATOM 273 O GLN A 34 -17.953 3.081 23.926 1.00 47.33 A O ANISOU 273 O GLN A 34 6850 4634 6498 1729 -733 -843 A O ATOM 274 CB GLN A 34 -16.178 0.617 24.436 1.00 28.58 A C ANISOU 274 CB GLN A 34 4354 2759 3744 1387 -828 -703 A C ATOM 275 CG GLN A 34 -15.714 -0.729 24.967 1.00 27.02 A C ANISOU 275 CG GLN A 34 4036 2803 3427 1256 -859 -654 A C ATOM 276 CD GLN A 34 -14.710 -1.398 24.049 1.00 25.61 A C ANISOU 276 CD GLN A 34 3927 2697 3105 1255 -997 -514 A C ATOM 277 NE2 GLN A 34 -13.686 -2.005 24.635 1.00 27.79 A N ANISOU 277 NE2 GLN A 34 4189 3164 3207 1088 -959 -474 A N ATOM 278 OE1 GLN A 34 -14.854 -1.368 22.827 1.00 25.58 A O ANISOU 278 OE1 GLN A 34 3986 2591 3141 1408 -1136 -442 A O ATOM 279 N THR A 35 -16.628 3.754 25.618 1.00 43.50 A N ANISOU 279 N THR A 35 6503 4244 5780 1357 -440 -1000 A N ATOM 280 CA THR A 35 -16.733 5.169 25.288 1.00 42.96 A C ANISOU 280 CA THR A 35 6626 3896 5799 1439 -370 -1049 A C ATOM 281 C THR A 35 -15.657 5.585 24.289 1.00 40.13 A C ANISOU 281 C THR A 35 6478 3460 5310 1392 -458 -915 A C ATOM 282 O THR A 35 -15.839 6.532 23.526 1.00 35.79 A O ANISOU 282 O THR A 35 6084 2664 4852 1521 -486 -876 A O ATOM 283 CB THR A 35 -16.616 6.046 26.549 1.00 48.72 A C ANISOU 283 CB THR A 35 7436 4575 6503 1282 -129 -1243 A C ATOM 284 CG2 THR A 35 -16.930 7.498 26.221 1.00 63.64 A C ANISOU 284 CG2 THR A 35 9523 6127 8530 1404 -52 -1306 A C ATOM 285 OG1 THR A 35 -17.532 5.579 27.547 1.00 44.71 A O ANISOU 285 OG1 THR A 35 6722 4186 6080 1298 -30 -1367 A O ATOM 286 N LYS A 36 -14.539 4.868 24.295 1.00 37.73 A N ANISOU 286 N LYS A 36 6172 3371 4793 1210 -499 -835 A N ATOM 287 CA LYS A 36 -13.413 5.200 23.430 1.00 40.68 A C ANISOU 287 CA LYS A 36 6720 3720 5015 1133 -561 -711 A C ATOM 288 C LYS A 36 -12.945 3.971 22.653 1.00 38.98 A C ANISOU 288 C LYS A 36 6414 3703 4692 1166 -732 -560 A C ATOM 289 O LYS A 36 -11.751 3.670 22.602 1.00 38.08 A O ANISOU 289 O LYS A 36 6336 3751 4381 1004 -733 -492 A O ATOM 290 CB LYS A 36 -12.266 5.782 24.260 1.00 52.02 A C ANISOU 290 CB LYS A 36 8275 5223 6269 842 -406 -778 A C ATOM 291 CG LYS A 36 -11.234 6.563 23.463 1.00 60.26 A C ANISOU 291 CG LYS A 36 9532 6172 7191 747 -422 -681 A C ATOM 292 CD LYS A 36 -10.209 7.203 24.387 1.00 66.92 A C ANISOU 292 CD LYS A 36 10478 7079 7868 436 -263 -770 A C ATOM 293 CE LYS A 36 -9.208 8.042 23.614 1.00 76.61 A C ANISOU 293 CE LYS A 36 11919 8208 8981 315 -268 -673 A C ATOM 294 NZ LYS A 36 -8.213 8.681 24.519 1.00 78.93 A N1+ ANISOU 294 NZ LYS A 36 12309 8572 9111 -15 -120 -765 A N1+ ATOM 295 N GLY A 37 -13.896 3.263 22.051 1.00 37.78 A N ANISOU 295 N GLY A 37 6140 3542 4673 1376 -874 -514 A N ATOM 296 CA GLY A 37 -13.595 2.076 21.270 1.00 34.82 A C ANISOU 296 CA GLY A 37 5692 3323 4216 1428 -1038 -393 A C ATOM 297 C GLY A 37 -12.782 2.405 20.034 1.00 39.74 A C ANISOU 297 C GLY A 37 6482 3900 4717 1450 -1126 -262 A C ATOM 298 O GLY A 37 -13.139 3.295 19.262 1.00 39.28 A O ANISOU 298 O GLY A 37 6554 3638 4733 1567 -1165 -222 A O ATOM 299 N ARG A 38 -11.686 1.679 19.841 1.00 26.93 A N ANISOU 299 N ARG A 38 4853 2474 2905 1345 -1153 -188 A N ATOM 300 CA ARG A 38 -10.762 1.975 18.754 1.00 40.65 A C ANISOU 300 CA ARG A 38 6739 4212 4493 1333 -1206 -69 A C ATOM 301 C ARG A 38 -10.603 0.810 17.782 1.00 41.01 A C ANISOU 301 C ARG A 38 6732 4385 4467 1448 -1364 25 A C ATOM 302 O ARG A 38 -10.765 -0.352 18.153 1.00 33.41 A O ANISOU 302 O ARG A 38 5619 3559 3514 1466 -1405 2 A O ATOM 303 CB ARG A 38 -9.397 2.389 19.313 1.00 39.25 A C ANISOU 303 CB ARG A 38 6627 4159 4129 1086 -1071 -65 A C ATOM 304 CG ARG A 38 -9.393 3.744 20.010 1.00 50.39 A C ANISOU 304 CG ARG A 38 8160 5405 5580 953 -920 -152 A C ATOM 305 CD ARG A 38 -9.598 4.873 19.014 1.00 56.74 A C ANISOU 305 CD ARG A 38 9169 5953 6436 1041 -951 -88 A C ATOM 306 NE ARG A 38 -9.543 6.189 19.644 1.00 68.57 A N ANISOU 306 NE ARG A 38 10817 7260 7977 910 -801 -175 A N ATOM 307 CZ ARG A 38 -10.613 6.889 20.008 1.00 75.08 A C ANISOU 307 CZ ARG A 38 11677 7847 9002 1023 -753 -273 A C ATOM 308 NH1 ARG A 38 -11.829 6.400 19.807 1.00 66.54 A N1+ ANISOU 308 NH1 ARG A 38 10470 6715 8098 1262 -848 -287 A N1+ ATOM 309 NH2 ARG A 38 -10.467 8.081 20.573 1.00 86.92 A N ANISOU 309 NH2 ARG A 38 13337 9160 10529 896 -607 -363 A N ATOM 310 N GLY A 39 -10.287 1.139 16.534 1.00 46.59 A N ANISOU 310 N GLY A 39 7573 5036 5092 1520 -1446 128 A N ATOM 311 CA GLY A 39 -10.049 0.139 15.511 1.00 25.79 A C ANISOU 311 CA GLY A 39 4922 2516 2360 1623 -1583 204 A C ATOM 312 C GLY A 39 -8.564 -0.119 15.334 1.00 27.98 A C ANISOU 312 C GLY A 39 5232 2988 2410 1493 -1522 268 A C ATOM 313 O GLY A 39 -7.769 0.147 16.234 1.00 33.79 A O ANISOU 313 O GLY A 39 5942 3822 3075 1312 -1387 244 A O ATOM 314 N ARG A 40 -8.187 -0.631 14.166 1.00 32.21 A N ANISOU 314 N ARG A 40 5819 3595 2826 1585 -1619 347 A N ATOM 315 CA ARG A 40 -6.796 -0.989 13.900 1.00 47.78 A C ANISOU 315 CA ARG A 40 7797 5776 4583 1493 -1562 409 A C ATOM 316 C ARG A 40 -5.890 0.202 13.587 1.00 57.73 A C ANISOU 316 C ARG A 40 9198 7029 5708 1349 -1463 484 A C ATOM 317 O ARG A 40 -4.670 0.055 13.505 1.00 61.02 A O ANISOU 317 O ARG A 40 9598 7640 5945 1239 -1390 535 A O ATOM 318 CB ARG A 40 -6.713 -2.037 12.787 1.00 49.17 A C ANISOU 318 CB ARG A 40 7964 6027 4694 1631 -1654 417 A C ATOM 319 CG ARG A 40 -6.555 -3.454 13.312 1.00 50.22 A C ANISOU 319 CG ARG A 40 7926 6279 4877 1640 -1616 323 A C ATOM 320 CD ARG A 40 -6.676 -4.496 12.215 1.00 50.73 A C ANISOU 320 CD ARG A 40 7998 6349 4930 1769 -1676 271 A C ATOM 321 NE ARG A 40 -8.055 -4.941 12.039 1.00 58.02 A N ANISOU 321 NE ARG A 40 8907 7129 6010 1868 -1795 190 A N ATOM 322 CZ ARG A 40 -8.801 -4.661 10.977 1.00 68.55 A C ANISOU 322 CZ ARG A 40 10340 8353 7353 1965 -1914 192 A C ATOM 323 NH1 ARG A 40 -10.047 -5.108 10.904 1.00 67.31 A N1+ ANISOU 323 NH1 ARG A 40 10141 8096 7339 2034 -2027 118 A N1+ ATOM 324 NH2 ARG A 40 -8.299 -3.941 9.983 1.00 79.78 A N ANISOU 324 NH2 ARG A 40 11900 9780 8633 1983 -1927 278 A N ATOM 325 N LEU A 41 -6.485 1.378 13.418 1.00 64.71 A N ANISOU 325 N LEU A 41 10218 7688 6682 1348 -1460 496 A N ATOM 326 CA LEU A 41 -5.712 2.584 13.148 1.00 78.76 A C ANISOU 326 CA LEU A 41 12157 9417 8353 1193 -1367 571 A C ATOM 327 C LEU A 41 -6.337 3.815 13.802 1.00 75.90 A C ANISOU 327 C LEU A 41 11892 8801 8147 1131 -1298 519 A C ATOM 328 O LEU A 41 -6.430 4.879 13.189 1.00 73.75 A O ANISOU 328 O LEU A 41 11803 8340 7879 1126 -1299 592 A O ATOM 329 CB LEU A 41 -5.559 2.802 11.642 1.00 92.34 A C ANISOU 329 CB LEU A 41 14023 11110 9952 1284 -1456 699 A C ATOM 330 CG LEU A 41 -4.427 3.742 11.221 1.00101.44 A C ANISOU 330 CG LEU A 41 15318 12299 10923 1096 -1353 804 A C ATOM 331 CD1 LEU A 41 -3.073 3.130 11.554 1.00100.19 A C ANISOU 331 CD1 LEU A 41 15034 12451 10581 945 -1253 809 A C ATOM 332 CD2 LEU A 41 -4.521 4.071 9.741 1.00104.48 A C ANISOU 332 CD2 LEU A 41 15869 12619 11208 1199 -1450 938 A C ATOM 333 N GLY A 42 -6.767 3.658 15.050 1.00 74.86 A N ANISOU 333 N GLY A 42 11643 8661 8141 1087 -1234 393 A N ATOM 334 CA GLY A 42 -7.321 4.759 15.817 1.00 77.75 A C ANISOU 334 CA GLY A 42 12089 8801 8651 1025 -1142 311 A C ATOM 335 C GLY A 42 -8.700 5.209 15.372 1.00 79.37 A C ANISOU 335 C GLY A 42 12354 8738 9065 1249 -1233 306 A C ATOM 336 O GLY A 42 -9.181 6.258 15.802 1.00 80.37 A O ANISOU 336 O GLY A 42 12581 8636 9321 1236 -1158 252 A O ATOM 337 N ARG A 43 -9.338 4.422 14.512 1.00 74.12 A N ANISOU 337 N ARG A 43 11626 8103 8433 1457 -1397 358 A N ATOM 338 CA ARG A 43 -10.686 4.739 14.048 1.00 76.31 A C ANISOU 338 CA ARG A 43 11922 8167 8907 1681 -1510 366 A C ATOM 339 C ARG A 43 -11.732 4.392 15.105 1.00 72.29 A C ANISOU 339 C ARG A 43 11237 7628 8602 1749 -1484 224 A C ATOM 340 O ARG A 43 -11.529 3.495 15.922 1.00 71.17 A O ANISOU 340 O ARG A 43 10938 7669 8434 1666 -1438 144 A O ATOM 341 CB ARG A 43 -11.001 4.028 12.726 1.00 79.64 A C ANISOU 341 CB ARG A 43 12339 8649 9272 1857 -1706 469 A C ATOM 342 CG ARG A 43 -10.688 2.538 12.710 1.00 81.15 A C ANISOU 342 CG ARG A 43 12373 9092 9366 1859 -1764 439 A C ATOM 343 CD ARG A 43 -9.209 2.292 12.469 1.00 84.82 A C ANISOU 343 CD ARG A 43 12888 9753 9586 1703 -1690 496 A C ATOM 344 NE ARG A 43 -8.793 2.730 11.140 1.00 89.88 A N ANISOU 344 NE ARG A 43 13699 10373 10080 1738 -1756 632 A N ATOM 345 CZ ARG A 43 -8.415 1.907 10.168 1.00 93.41 A C ANISOU 345 CZ ARG A 43 14147 10974 10369 1804 -1848 687 A C ATOM 346 NH1 ARG A 43 -8.386 0.598 10.380 1.00 98.76 A N1+ ANISOU 346 NH1 ARG A 43 14675 11816 11034 1848 -1887 616 A N1+ ATOM 347 NH2 ARG A 43 -8.055 2.391 8.988 1.00 90.91 A N ANISOU 347 NH2 ARG A 43 13995 10643 9905 1822 -1896 812 A N ATOM 348 N LYS A 44 -12.848 5.113 15.082 1.00 68.75 A N ANISOU 348 N LYS A 44 10812 6953 8357 1903 -1509 201 A N ATOM 349 CA LYS A 44 -13.916 4.920 16.057 1.00 62.92 A C ANISOU 349 CA LYS A 44 9903 6180 7824 1977 -1468 66 A C ATOM 350 C LYS A 44 -14.634 3.587 15.867 1.00 57.08 A C ANISOU 350 C LYS A 44 8956 5598 7136 2096 -1612 56 A C ATOM 351 O LYS A 44 -15.177 3.310 14.797 1.00 64.53 A O ANISOU 351 O LYS A 44 9897 6519 8103 2261 -1791 144 A O ATOM 352 CB LYS A 44 -14.926 6.065 15.966 1.00 67.42 A C ANISOU 352 CB LYS A 44 10546 6465 8605 2144 -1461 56 A C ATOM 353 CG LYS A 44 -16.118 5.926 16.901 1.00 64.78 A C ANISOU 353 CG LYS A 44 10020 6100 8495 2246 -1410 -85 A C ATOM 354 CD LYS A 44 -15.720 6.181 18.343 1.00 64.65 A C ANISOU 354 CD LYS A 44 9986 6114 8464 2049 -1186 -245 A C ATOM 355 CE LYS A 44 -16.935 6.208 19.256 1.00 66.59 A C ANISOU 355 CE LYS A 44 10058 6313 8929 2157 -1110 -388 A C ATOM 356 NZ LYS A 44 -16.560 6.512 20.664 1.00 63.79 A N1+ ANISOU 356 NZ LYS A 44 9706 5992 8541 1958 -884 -554 A N1+ ATOM 357 N TRP A 45 -14.635 2.767 16.913 1.00 41.15 A N ANISOU 357 N TRP A 45 6771 3737 5127 1998 -1538 -47 A N ATOM 358 CA TRP A 45 -15.370 1.506 16.900 1.00 35.66 A C ANISOU 358 CA TRP A 45 5879 3170 4500 2082 -1657 -68 A C ATOM 359 C TRP A 45 -16.625 1.610 17.760 1.00 40.59 A C ANISOU 359 C TRP A 45 6339 3734 5350 2156 -1607 -179 A C ATOM 360 O TRP A 45 -16.573 1.437 18.978 1.00 36.22 A O ANISOU 360 O TRP A 45 5692 3259 4811 2030 -1462 -283 A O ATOM 361 CB TRP A 45 -14.491 0.355 17.392 1.00 27.42 A C ANISOU 361 CB TRP A 45 4759 2357 3303 1929 -1625 -80 A C ATOM 362 CG TRP A 45 -15.203 -0.963 17.423 1.00 41.26 A C ANISOU 362 CG TRP A 45 6333 4216 5127 1993 -1740 -100 A C ATOM 363 CD1 TRP A 45 -15.854 -1.518 18.485 1.00 40.80 A C ANISOU 363 CD1 TRP A 45 6099 4223 5182 1950 -1682 -189 A C ATOM 364 CD2 TRP A 45 -15.344 -1.889 16.338 1.00 34.62 A C ANISOU 364 CD2 TRP A 45 5483 3426 4243 2095 -1928 -34 A C ATOM 365 CE2 TRP A 45 -16.091 -2.984 16.819 1.00 27.86 A C ANISOU 365 CE2 TRP A 45 4447 2649 3490 2102 -1980 -88 A C ATOM 366 CE3 TRP A 45 -14.910 -1.900 15.009 1.00 40.66 A C ANISOU 366 CE3 TRP A 45 6384 4183 4882 2168 -2050 59 A C ATOM 367 NE1 TRP A 45 -16.390 -2.733 18.132 1.00 25.84 A N ANISOU 367 NE1 TRP A 45 4086 2404 3326 2012 -1826 -173 A N ATOM 368 CZ2 TRP A 45 -16.412 -4.078 16.017 1.00 28.60 A C ANISOU 368 CZ2 TRP A 45 4509 2801 3555 2121 -2116 -99 A C ATOM 369 CZ3 TRP A 45 -15.231 -2.987 14.214 1.00 42.00 A C ANISOU 369 CZ3 TRP A 45 6517 4431 5012 2176 -2163 17 A C ATOM 370 CH2 TRP A 45 -15.975 -4.060 14.721 1.00 39.12 A C ANISOU 370 CH2 TRP A 45 5988 4125 4753 2152 -2197 -63 A C ATOM 371 N LEU A 46 -17.751 1.897 17.115 1.00 41.33 A N ANISOU 371 N LEU A 46 6389 3705 5610 2361 -1728 -151 A N ATOM 372 CA LEU A 46 -19.019 2.075 17.813 1.00 41.98 A C ANISOU 372 CA LEU A 46 6297 3733 5922 2462 -1684 -248 A C ATOM 373 C LEU A 46 -19.341 0.885 18.713 1.00 42.40 A C ANISOU 373 C LEU A 46 6132 3979 5998 2366 -1653 -331 A C ATOM 374 O LEU A 46 -19.532 -0.233 18.237 1.00 33.05 A O ANISOU 374 O LEU A 46 4854 2915 4788 2381 -1804 -286 A O ATOM 375 CB LEU A 46 -20.147 2.305 16.806 1.00 43.70 A C ANISOU 375 CB LEU A 46 6462 3845 6296 2705 -1868 -175 A C ATOM 376 CG LEU A 46 -19.945 3.524 15.902 1.00 55.90 A C ANISOU 376 CG LEU A 46 8226 5180 7834 2819 -1909 -70 A C ATOM 377 CD1 LEU A 46 -20.920 3.513 14.736 1.00 63.34 A C ANISOU 377 CD1 LEU A 46 9115 6074 8878 3048 -2141 39 A C ATOM 378 CD2 LEU A 46 -20.070 4.811 16.705 1.00 61.85 A C ANISOU 378 CD2 LEU A 46 9059 5733 8709 2834 -1710 -154 A C ATOM 379 N SER A 47 -19.400 1.137 20.017 1.00 48.47 A N ANISOU 379 N SER A 47 6836 4772 6810 2259 -1456 -452 A N ATOM 380 CA SER A 47 -19.636 0.080 20.994 1.00 39.99 A C ANISOU 380 CA SER A 47 5571 3883 5738 2140 -1403 -521 A C ATOM 381 C SER A 47 -20.822 0.385 21.904 1.00 35.40 A C ANISOU 381 C SER A 47 4811 3283 5356 2196 -1287 -641 A C ATOM 382 O SER A 47 -20.646 0.774 23.059 1.00 32.52 A O ANISOU 382 O SER A 47 4442 2943 4972 2075 -1084 -752 A O ATOM 383 CB SER A 47 -18.380 -0.156 21.836 1.00 45.11 A C ANISOU 383 CB SER A 47 6296 4658 6186 1906 -1266 -543 A C ATOM 384 OG SER A 47 -17.281 -0.524 21.021 1.00 44.85 A O ANISOU 384 OG SER A 47 6396 4673 5973 1862 -1364 -433 A O ATOM 385 N GLN A 48 -22.029 0.199 21.380 1.00 36.26 A N ANISOU 385 N GLN A 48 4764 3365 5647 2375 -1414 -623 A N ATOM 386 CA GLN A 48 -23.243 0.440 22.150 1.00 35.08 A C ANISOU 386 CA GLN A 48 4409 3221 5701 2452 -1312 -731 A C ATOM 387 C GLN A 48 -23.690 -0.808 22.905 1.00 49.93 A C ANISOU 387 C GLN A 48 6066 5313 7593 2324 -1300 -766 A C ATOM 388 O GLN A 48 -23.104 -1.881 22.758 1.00 41.99 A O ANISOU 388 O GLN A 48 5075 4426 6453 2197 -1391 -699 A O ATOM 389 CB GLN A 48 -24.367 0.933 21.237 1.00 45.90 A C ANISOU 389 CB GLN A 48 5693 4471 7275 2715 -1454 -685 A C ATOM 390 CG GLN A 48 -24.167 2.345 20.712 1.00 54.21 A C ANISOU 390 CG GLN A 48 6948 5281 8366 2865 -1426 -660 A C ATOM 391 CD GLN A 48 -25.272 2.775 19.770 1.00 67.35 A C ANISOU 391 CD GLN A 48 8521 6842 10229 3140 -1591 -586 A C ATOM 392 NE2 GLN A 48 -25.658 4.044 19.850 1.00 67.25 A N ANISOU 392 NE2 GLN A 48 8570 6622 10360 3310 -1493 -621 A N ATOM 393 OE1 GLN A 48 -25.773 1.977 18.977 1.00 74.30 A O ANISOU 393 OE1 GLN A 48 9278 7823 11129 3199 -1808 -498 A O ATOM 394 N GLU A 49 -24.734 -0.658 23.715 1.00 57.34 A N ANISOU 394 N GLU A 49 6801 6294 8694 2362 -1180 -869 A N ATOM 395 CA GLU A 49 -25.253 -1.764 24.511 1.00 62.26 A C ANISOU 395 CA GLU A 49 7203 7117 9336 2228 -1148 -900 A C ATOM 396 C GLU A 49 -25.774 -2.896 23.631 1.00 53.35 A C ANISOU 396 C GLU A 49 5951 6063 8255 2260 -1394 -796 A C ATOM 397 O GLU A 49 -26.369 -2.658 22.580 1.00 42.57 A O ANISOU 397 O GLU A 49 4556 4618 7002 2443 -1566 -739 A O ATOM 398 CB GLU A 49 -26.355 -1.277 25.454 1.00 76.44 A C ANISOU 398 CB GLU A 49 8791 8947 11304 2283 -965 -1032 A C ATOM 399 CG GLU A 49 -27.475 -0.513 24.765 1.00 97.86 A C ANISOU 399 CG GLU A 49 11390 11540 14251 2560 -1036 -1037 A C ATOM 400 CD GLU A 49 -28.540 -0.041 25.736 1.00111.29 A C ANISOU 400 CD GLU A 49 12870 13290 16126 2628 -832 -1178 A C ATOM 401 OE1 GLU A 49 -28.601 -0.581 26.860 1.00117.52 A O ANISOU 401 OE1 GLU A 49 13548 14248 16857 2443 -673 -1256 A O ATOM 402 OE2 GLU A 49 -29.317 0.868 25.374 1.00113.61 A O1- ANISOU 402 OE2 GLU A 49 13100 13457 16610 2874 -828 -1206 A O1- ATOM 403 N GLY A 50 -25.544 -4.129 24.071 1.00 34.04 A N ANISOU 403 N GLY A 50 3444 3768 5721 2074 -1415 -768 A N ATOM 404 CA GLY A 50 -25.993 -5.297 23.337 1.00 38.41 A C ANISOU 404 CA GLY A 50 3900 4383 6311 2066 -1635 -686 A C ATOM 405 C GLY A 50 -24.872 -5.956 22.561 1.00 44.32 A C ANISOU 405 C GLY A 50 4857 5106 6878 2011 -1777 -591 A C ATOM 406 O GLY A 50 -25.020 -7.072 22.067 1.00 31.42 A O ANISOU 406 O GLY A 50 3185 3518 5234 1965 -1940 -535 A O ATOM 407 N GLY A 51 -23.744 -5.261 22.454 1.00 30.82 A N ANISOU 407 N GLY A 51 3366 3320 5022 2012 -1708 -579 A N ATOM 408 CA GLY A 51 -22.592 -5.782 21.743 1.00 29.14 A C ANISOU 408 CA GLY A 51 3347 3098 4628 1972 -1814 -494 A C ATOM 409 C GLY A 51 -21.643 -6.547 22.645 1.00 35.88 A C ANISOU 409 C GLY A 51 4239 4066 5327 1775 -1711 -482 A C ATOM 410 O GLY A 51 -21.784 -6.540 23.868 1.00 27.93 A O ANISOU 410 O GLY A 51 3137 3145 4330 1655 -1545 -538 A O ATOM 411 N LEU A 52 -20.668 -7.211 22.035 1.00 25.20 A N ANISOU 411 N LEU A 52 2657 3173 3744 1600 -744 59 A N ATOM 412 CA LEU A 52 -19.673 -7.962 22.785 1.00 21.83 A C ANISOU 412 CA LEU A 52 2237 2690 3369 1394 -667 101 A C ATOM 413 C LEU A 52 -18.290 -7.367 22.551 1.00 27.30 A C ANISOU 413 C LEU A 52 3104 3259 4011 1363 -614 225 A C ATOM 414 O LEU A 52 -17.787 -7.360 21.427 1.00 22.85 A O ANISOU 414 O LEU A 52 2626 2679 3377 1415 -639 273 A O ATOM 415 CB LEU A 52 -19.698 -9.436 22.376 1.00 32.55 A C ANISOU 415 CB LEU A 52 3480 4131 4757 1311 -688 42 A C ATOM 416 CG LEU A 52 -19.086 -10.430 23.362 1.00 32.64 A C ANISOU 416 CG LEU A 52 3461 4109 4834 1127 -599 61 A C ATOM 417 CD1 LEU A 52 -19.664 -10.220 24.749 1.00 20.96 A C ANISOU 417 CD1 LEU A 52 1932 2620 3412 1079 -535 20 A C ATOM 418 CD2 LEU A 52 -19.320 -11.857 22.891 1.00 40.37 A C ANISOU 418 CD2 LEU A 52 4326 5155 5860 1061 -590 -13 A C ATOM 419 N TYR A 53 -17.680 -6.860 23.617 1.00 17.41 A N ANISOU 419 N TYR A 53 1897 1931 2788 1267 -527 252 A N ATOM 420 CA TYR A 53 -16.374 -6.223 23.516 1.00 17.09 A C ANISOU 420 CA TYR A 53 1998 1780 2715 1218 -451 321 A C ATOM 421 C TYR A 53 -15.436 -6.751 24.589 1.00 16.11 A C ANISOU 421 C TYR A 53 1834 1668 2618 1052 -395 312 A C ATOM 422 O TYR A 53 -15.660 -6.541 25.782 1.00 16.06 A O ANISOU 422 O TYR A 53 1773 1686 2646 1002 -354 273 A O ATOM 423 CB TYR A 53 -16.515 -4.706 23.643 1.00 18.01 A C ANISOU 423 CB TYR A 53 2224 1792 2827 1303 -376 335 A C ATOM 424 CG TYR A 53 -17.726 -4.158 22.927 1.00 19.28 A C ANISOU 424 CG TYR A 53 2399 1970 2954 1507 -436 336 A C ATOM 425 CD1 TYR A 53 -18.894 -3.864 23.623 1.00 21.45 A C ANISOU 425 CD1 TYR A 53 2577 2299 3275 1562 -459 270 A C ATOM 426 CD2 TYR A 53 -17.710 -3.950 21.552 1.00 20.08 A C ANISOU 426 CD2 TYR A 53 2609 2052 2969 1661 -472 397 A C ATOM 427 CE1 TYR A 53 -20.007 -3.369 22.974 1.00 22.63 A C ANISOU 427 CE1 TYR A 53 2724 2490 3385 1771 -525 255 A C ATOM 428 CE2 TYR A 53 -18.820 -3.454 20.893 1.00 27.64 A C ANISOU 428 CE2 TYR A 53 3574 3059 3868 1888 -539 394 A C ATOM 429 CZ TYR A 53 -19.966 -3.167 21.608 1.00 22.33 A C ANISOU 429 CZ TYR A 53 2791 2449 3243 1946 -570 318 A C ATOM 430 OH TYR A 53 -21.073 -2.673 20.958 1.00 25.30 A O ANISOU 430 OH TYR A 53 3161 2897 3553 2194 -647 299 A O ATOM 431 N PHE A 54 -14.384 -7.440 24.165 1.00 15.45 A N ANISOU 431 N PHE A 54 1777 1581 2510 981 -396 344 A N ATOM 432 CA PHE A 54 -13.437 -8.008 25.115 1.00 14.73 A C ANISOU 432 CA PHE A 54 1647 1529 2422 859 -355 336 A C ATOM 433 C PHE A 54 -12.004 -8.043 24.594 1.00 15.73 A C ANISOU 433 C PHE A 54 1848 1614 2516 798 -327 353 A C ATOM 434 O PHE A 54 -11.765 -8.029 23.387 1.00 15.16 A O ANISOU 434 O PHE A 54 1851 1486 2424 831 -347 386 A O ATOM 435 CB PHE A 54 -13.885 -9.406 25.551 1.00 25.04 A C ANISOU 435 CB PHE A 54 2843 2922 3750 825 -386 337 A C ATOM 436 CG PHE A 54 -13.997 -10.392 24.423 1.00 14.14 A C ANISOU 436 CG PHE A 54 1445 1554 2375 837 -438 356 A C ATOM 437 CD1 PHE A 54 -12.989 -11.309 24.187 1.00 19.19 A C ANISOU 437 CD1 PHE A 54 2091 2198 3001 771 -430 393 A C ATOM 438 CD2 PHE A 54 -15.116 -10.408 23.607 1.00 26.39 A C ANISOU 438 CD2 PHE A 54 2957 3128 3944 920 -494 322 A C ATOM 439 CE1 PHE A 54 -13.091 -12.223 23.154 1.00 14.75 A C ANISOU 439 CE1 PHE A 54 1507 1649 2449 759 -460 394 A C ATOM 440 CE2 PHE A 54 -15.223 -11.318 22.572 1.00 27.24 A C ANISOU 440 CE2 PHE A 54 3028 3271 4051 919 -534 309 A C ATOM 441 CZ PHE A 54 -14.209 -12.227 22.346 1.00 21.73 A C ANISOU 441 CZ PHE A 54 2346 2563 3350 827 -510 347 A C ATOM 442 N SER A 55 -11.056 -8.079 25.525 1.00 14.12 A N ANISOU 442 N SER A 55 1615 1451 2298 716 -279 315 A N ATOM 443 CA SER A 55 -9.641 -8.178 25.195 1.00 13.87 A C ANISOU 443 CA SER A 55 1624 1407 2241 648 -250 294 A C ATOM 444 C SER A 55 -8.956 -9.194 26.102 1.00 19.62 A C ANISOU 444 C SER A 55 2261 2258 2935 603 -267 283 A C ATOM 445 O SER A 55 -9.407 -9.442 27.219 1.00 21.28 A O ANISOU 445 O SER A 55 2401 2552 3133 617 -265 278 A O ATOM 446 CB SER A 55 -8.957 -6.816 25.336 1.00 17.70 A C ANISOU 446 CB SER A 55 2174 1818 2733 609 -143 211 A C ATOM 447 OG SER A 55 -9.457 -5.886 24.393 1.00 15.12 A O ANISOU 447 OG SER A 55 1969 1352 2423 674 -101 245 A O ATOM 448 N PHE A 56 -7.871 -9.787 25.614 1.00 13.14 A N ANISOU 448 N PHE A 56 1451 1448 2092 563 -277 283 A N ATOM 449 CA PHE A 56 -7.068 -10.692 26.429 1.00 13.01 A C ANISOU 449 CA PHE A 56 1361 1555 2025 551 -289 274 A C ATOM 450 C PHE A 56 -5.596 -10.623 26.044 1.00 17.75 A C ANISOU 450 C PHE A 56 1972 2170 2602 495 -273 200 A C ATOM 451 O PHE A 56 -5.244 -10.077 24.998 1.00 16.87 A O ANISOU 451 O PHE A 56 1939 1948 2524 451 -246 176 A O ATOM 452 CB PHE A 56 -7.590 -12.131 26.343 1.00 16.40 A C ANISOU 452 CB PHE A 56 1762 2008 2461 587 -327 376 A C ATOM 453 CG PHE A 56 -7.620 -12.690 24.950 1.00 19.02 A C ANISOU 453 CG PHE A 56 2133 2257 2836 570 -358 423 A C ATOM 454 CD1 PHE A 56 -8.763 -12.589 24.172 1.00 20.38 A C ANISOU 454 CD1 PHE A 56 2322 2366 3055 595 -381 449 A C ATOM 455 CD2 PHE A 56 -6.512 -13.331 24.422 1.00 22.77 A C ANISOU 455 CD2 PHE A 56 2616 2737 3296 534 -368 427 A C ATOM 456 CE1 PHE A 56 -8.795 -13.108 22.892 1.00 19.51 A C ANISOU 456 CE1 PHE A 56 2236 2214 2964 574 -407 467 A C ATOM 457 CE2 PHE A 56 -6.538 -13.852 23.144 1.00 18.17 A C ANISOU 457 CE2 PHE A 56 2064 2087 2752 511 -393 463 A C ATOM 458 CZ PHE A 56 -7.681 -13.740 22.377 1.00 17.95 A C ANISOU 458 CZ PHE A 56 2052 2012 2755 521 -406 475 A C ATOM 459 N LEU A 57 -4.741 -11.173 26.901 1.00 19.56 A N ANISOU 459 N LEU A 57 2125 2541 2765 507 -284 158 A N ATOM 460 CA LEU A 57 -3.301 -11.151 26.672 1.00 21.13 A C ANISOU 460 CA LEU A 57 2302 2790 2937 459 -274 51 A C ATOM 461 C LEU A 57 -2.766 -12.488 26.179 1.00 17.30 A C ANISOU 461 C LEU A 57 1811 2326 2435 482 -325 129 A C ATOM 462 O LEU A 57 -3.260 -13.551 26.553 1.00 29.00 A O ANISOU 462 O LEU A 57 3277 3848 3895 555 -352 245 A O ATOM 463 CB LEU A 57 -2.557 -10.748 27.948 1.00 30.61 A C ANISOU 463 CB LEU A 57 3398 4173 4059 474 -255 -94 A C ATOM 464 CG LEU A 57 -2.209 -9.269 28.123 1.00 31.03 A C ANISOU 464 CG LEU A 57 3437 4207 4146 390 -162 -278 A C ATOM 465 CD1 LEU A 57 -3.453 -8.405 28.049 1.00 34.16 A C ANISOU 465 CD1 LEU A 57 3904 4466 4608 383 -116 -221 A C ATOM 466 CD2 LEU A 57 -1.474 -9.049 29.436 1.00 34.92 A C ANISOU 466 CD2 LEU A 57 3787 4932 4547 413 -156 -447 A C ATOM 467 N LEU A 58 -1.745 -12.418 25.334 1.00 15.81 A N ANISOU 467 N LEU A 58 1642 2098 2267 415 -316 58 A N ATOM 468 CA LEU A 58 -1.028 -13.602 24.886 1.00 25.09 A C ANISOU 468 CA LEU A 58 2801 3303 3430 427 -357 102 A C ATOM 469 C LEU A 58 0.468 -13.386 25.061 1.00 23.72 A C ANISOU 469 C LEU A 58 2561 3236 3216 393 -349 -69 A C ATOM 470 O LEU A 58 0.932 -12.250 25.165 1.00 23.35 A O ANISOU 470 O LEU A 58 2500 3190 3181 322 -289 -233 A O ATOM 471 CB LEU A 58 -1.345 -13.907 23.423 1.00 24.67 A C ANISOU 471 CB LEU A 58 2833 3086 3454 370 -362 184 A C ATOM 472 CG LEU A 58 -2.786 -14.310 23.112 1.00 23.49 A C ANISOU 472 CG LEU A 58 2717 2862 3345 408 -380 320 A C ATOM 473 CD1 LEU A 58 -2.942 -14.606 21.628 1.00 21.01 A C ANISOU 473 CD1 LEU A 58 2465 2431 3086 361 -393 365 A C ATOM 474 CD2 LEU A 58 -3.203 -15.508 23.953 1.00 22.29 A C ANISOU 474 CD2 LEU A 58 2509 2790 3169 487 -388 414 A C ATOM 475 N ASN A 59 1.222 -14.479 25.098 1.00 23.58 A N ANISOU 475 N ASN A 59 2495 3307 3157 444 -394 -47 A N ATOM 476 CA ASN A 59 2.670 -14.394 25.229 1.00 28.38 A C ANISOU 476 CA ASN A 59 3019 4043 3723 426 -399 -229 A C ATOM 477 C ASN A 59 3.321 -14.108 23.879 1.00 28.76 A C ANISOU 477 C ASN A 59 3124 3944 3861 286 -360 -305 A C ATOM 478 O ASN A 59 3.235 -14.921 22.959 1.00 36.55 A O ANISOU 478 O ASN A 59 4167 4827 4893 268 -382 -188 A O ATOM 479 CB ASN A 59 3.230 -15.683 25.835 1.00 29.62 A C ANISOU 479 CB ASN A 59 3107 4363 3786 569 -462 -170 A C ATOM 480 CG ASN A 59 4.606 -15.494 26.440 1.00 40.02 A C ANISOU 480 CG ASN A 59 4290 5902 5012 609 -488 -391 A C ATOM 481 ND2 ASN A 59 5.426 -14.665 25.805 1.00 39.45 A N ANISOU 481 ND2 ASN A 59 4191 5792 5005 464 -443 -600 A N ATOM 482 OD1 ASN A 59 4.927 -16.084 27.473 1.00 46.74 A O ANISOU 482 OD1 ASN A 59 5064 6964 5732 778 -537 -384 A O ATOM 483 N PRO A 60 3.966 -12.939 23.756 1.00 42.60 A N ANISOU 483 N PRO A 60 4865 5678 5643 179 -280 -513 A N ATOM 484 CA PRO A 60 4.629 -12.516 22.516 1.00 48.66 A C ANISOU 484 CA PRO A 60 5706 6288 6494 39 -205 -605 A C ATOM 485 C PRO A 60 5.723 -13.488 22.083 1.00 49.76 A C ANISOU 485 C PRO A 60 5788 6492 6629 30 -254 -653 A C ATOM 486 O PRO A 60 6.120 -13.481 20.918 1.00 50.88 A O ANISOU 486 O PRO A 60 6006 6486 6839 -76 -210 -670 A O ATOM 487 CB PRO A 60 5.253 -11.168 22.895 1.00 45.78 A C ANISOU 487 CB PRO A 60 5302 5943 6151 -57 -81 -865 A C ATOM 488 CG PRO A 60 4.457 -10.691 24.061 1.00 38.55 A C ANISOU 488 CG PRO A 60 4338 5124 5186 20 -90 -847 A C ATOM 489 CD PRO A 60 4.085 -11.925 24.817 1.00 43.06 A C ANISOU 489 CD PRO A 60 4839 5858 5662 179 -231 -686 A C ATOM 490 N LYS A 61 6.201 -14.310 23.012 1.00 50.69 A N ANISOU 490 N LYS A 61 5776 6827 6656 153 -340 -672 A N ATOM 491 CA LYS A 61 7.270 -15.259 22.720 1.00 46.90 A C ANISOU 491 CA LYS A 61 5228 6431 6162 174 -391 -722 A C ATOM 492 C LYS A 61 6.727 -16.601 22.239 1.00 52.00 A C ANISOU 492 C LYS A 61 5937 6999 6821 244 -449 -468 A C ATOM 493 O LYS A 61 7.489 -17.473 21.822 1.00 56.81 A O ANISOU 493 O LYS A 61 6513 7633 7439 256 -480 -473 A O ATOM 494 CB LYS A 61 8.150 -15.469 23.953 1.00 40.27 A C ANISOU 494 CB LYS A 61 4215 5889 5198 305 -450 -885 A C ATOM 495 CG LYS A 61 8.868 -14.217 24.426 1.00 37.87 A C ANISOU 495 CG LYS A 61 3803 5699 4888 220 -380 -1204 A C ATOM 496 CD LYS A 61 9.731 -14.507 25.642 1.00 48.97 A C ANISOU 496 CD LYS A 61 5010 7450 6146 378 -460 -1383 A C ATOM 497 CE LYS A 61 10.470 -13.262 26.105 1.00 58.10 A C ANISOU 497 CE LYS A 61 6025 8742 7307 275 -376 -1753 A C ATOM 498 NZ LYS A 61 11.252 -13.518 27.345 1.00 61.70 A N1+ ANISOU 498 NZ LYS A 61 6264 9585 7595 455 -469 -1949 A N1+ ATOM 499 N GLU A 62 5.410 -16.762 22.299 1.00 56.01 A N ANISOU 499 N GLU A 62 6526 7413 7342 285 -450 -265 A N ATOM 500 CA GLU A 62 4.783 -18.024 21.920 1.00 53.55 A C ANISOU 500 CA GLU A 62 6260 7028 7057 341 -474 -50 A C ATOM 501 C GLU A 62 4.178 -17.981 20.521 1.00 50.51 A C ANISOU 501 C GLU A 62 5978 6434 6779 217 -446 27 A C ATOM 502 O GLU A 62 4.357 -18.908 19.731 1.00 54.95 A O ANISOU 502 O GLU A 62 6553 6934 7392 189 -451 93 A O ATOM 503 CB GLU A 62 3.715 -18.422 22.942 1.00 57.82 A C ANISOU 503 CB GLU A 62 6805 7620 7543 476 -479 103 A C ATOM 504 CG GLU A 62 4.268 -18.753 24.319 1.00 69.44 A C ANISOU 504 CG GLU A 62 8190 9314 8881 645 -510 71 A C ATOM 505 CD GLU A 62 3.198 -19.244 25.275 1.00 80.89 A C ANISOU 505 CD GLU A 62 9672 10788 10276 779 -488 241 A C ATOM 506 OE1 GLU A 62 2.088 -19.578 24.808 1.00 81.65 A O ANISOU 506 OE1 GLU A 62 9842 10726 10456 735 -447 380 A O ATOM 507 OE2 GLU A 62 3.467 -19.297 26.494 1.00 86.76 A O1- ANISOU 507 OE2 GLU A 62 10360 11717 10886 931 -507 220 A O1- ATOM 508 N PHE A 63 3.465 -16.902 20.218 1.00 50.95 A N ANISOU 508 N PHE A 63 6106 6392 6860 156 -412 16 A N ATOM 509 CA PHE A 63 2.765 -16.784 18.944 1.00 54.96 A C ANISOU 509 CA PHE A 63 6714 6732 7434 82 -394 94 A C ATOM 510 C PHE A 63 3.375 -15.718 18.040 1.00 58.19 A C ANISOU 510 C PHE A 63 7207 7032 7872 -34 -331 -28 A C ATOM 511 O PHE A 63 3.702 -14.620 18.489 1.00 63.93 A O ANISOU 511 O PHE A 63 7942 7764 8583 -62 -272 -154 A O ATOM 512 CB PHE A 63 1.284 -16.472 19.175 1.00 49.05 A C ANISOU 512 CB PHE A 63 6005 5947 6685 139 -399 205 A C ATOM 513 CG PHE A 63 0.564 -17.505 19.991 1.00 40.04 A C ANISOU 513 CG PHE A 63 4803 4879 5531 237 -423 322 A C ATOM 514 CD1 PHE A 63 0.387 -17.330 21.353 1.00 45.72 A C ANISOU 514 CD1 PHE A 63 5475 5709 6188 325 -424 319 A C ATOM 515 CD2 PHE A 63 0.061 -18.648 19.395 1.00 39.00 A C ANISOU 515 CD2 PHE A 63 4665 4701 5452 236 -423 423 A C ATOM 516 CE1 PHE A 63 -0.276 -18.277 22.105 1.00 46.99 A C ANISOU 516 CE1 PHE A 63 5606 5915 6333 420 -415 433 A C ATOM 517 CE2 PHE A 63 -0.602 -19.598 20.142 1.00 38.33 A C ANISOU 517 CE2 PHE A 63 4545 4657 5361 294 -385 505 A C ATOM 518 CZ PHE A 63 -0.771 -19.413 21.498 1.00 47.86 A C ANISOU 518 CZ PHE A 63 5730 5954 6499 390 -375 519 A C ATOM 519 N GLU A 64 3.525 -16.052 16.762 1.00 49.97 A N ANISOU 519 N GLU A 64 6230 5883 6874 -105 -323 2 A N ATOM 520 CA GLU A 64 3.944 -15.082 15.759 1.00 50.90 A C ANISOU 520 CA GLU A 64 6467 5861 7012 -203 -239 -80 A C ATOM 521 C GLU A 64 2.714 -14.372 15.203 1.00 56.38 A C ANISOU 521 C GLU A 64 7284 6450 7689 -156 -219 29 A C ATOM 522 O GLU A 64 1.914 -14.966 14.479 1.00 55.71 A O ANISOU 522 O GLU A 64 7220 6345 7605 -120 -273 148 A O ATOM 523 CB GLU A 64 4.731 -15.770 14.643 1.00 64.90 A C ANISOU 523 CB GLU A 64 8257 7577 8824 -292 -236 -102 A C ATOM 524 CG GLU A 64 4.175 -17.124 14.236 1.00 81.65 A C ANISOU 524 CG GLU A 64 10328 9728 10967 -256 -317 37 A C ATOM 525 CD GLU A 64 5.126 -17.894 13.340 1.00 92.20 A C ANISOU 525 CD GLU A 64 11636 11074 12321 -315 -310 -1 A C ATOM 526 OE1 GLU A 64 4.880 -19.095 13.101 1.00 96.21 A O ANISOU 526 OE1 GLU A 64 12081 11623 12853 -287 -355 83 A O ATOM 527 OE2 GLU A 64 6.122 -17.298 12.879 1.00 92.57 A O1- ANISOU 527 OE2 GLU A 64 11721 11099 12354 -376 -237 -119 A O1- ATOM 528 N ASN A 65 2.572 -13.096 15.546 1.00 57.52 A N ANISOU 528 N ASN A 65 7500 6537 7818 -151 -135 -29 A N ATOM 529 CA ASN A 65 1.341 -12.359 15.275 1.00 66.32 A C ANISOU 529 CA ASN A 65 8720 7575 8904 -66 -121 76 A C ATOM 530 C ASN A 65 1.364 -11.504 14.011 1.00 69.09 A C ANISOU 530 C ASN A 65 9262 7751 9238 -79 -18 90 A C ATOM 531 O ASN A 65 0.753 -10.437 13.971 1.00 72.52 A O ANISOU 531 O ASN A 65 9813 8097 9646 -14 57 121 A O ATOM 532 CB ASN A 65 0.975 -11.484 16.477 1.00 66.84 A C ANISOU 532 CB ASN A 65 8756 7678 8960 -24 -82 31 A C ATOM 533 CG ASN A 65 1.958 -10.347 16.694 1.00 67.89 A C ANISOU 533 CG ASN A 65 8940 7738 9119 -116 73 -145 A C ATOM 534 ND2 ASN A 65 3.246 -10.643 16.565 1.00 67.77 A N ANISOU 534 ND2 ASN A 65 8875 7745 9131 -223 108 -286 A N ATOM 535 OD1 ASN A 65 1.562 -9.215 16.970 1.00 71.10 A O ANISOU 535 OD1 ASN A 65 9422 8066 9527 -96 174 -170 A O ATOM 536 N LEU A 66 2.058 -11.971 12.979 1.00 71.75 A N ANISOU 536 N LEU A 66 9644 8034 9585 -151 -5 75 A N ATOM 537 CA LEU A 66 2.102 -11.237 11.719 1.00 77.82 A C ANISOU 537 CA LEU A 66 10594 8675 10297 -144 102 99 A C ATOM 538 C LEU A 66 0.787 -11.380 10.954 1.00 59.61 A C ANISOU 538 C LEU A 66 8348 6383 7917 -2 16 255 A C ATOM 539 O LEU A 66 0.008 -10.433 10.861 1.00 56.40 A O ANISOU 539 O LEU A 66 8067 5901 7461 113 65 320 A O ATOM 540 CB LEU A 66 3.275 -11.705 10.856 1.00 93.64 A C ANISOU 540 CB LEU A 66 12597 10681 12302 -259 147 20 A C ATOM 541 CG LEU A 66 3.586 -10.841 9.632 1.00105.72 A C ANISOU 541 CG LEU A 66 14341 12053 13774 -271 308 18 A C ATOM 542 CD1 LEU A 66 3.884 -9.407 10.046 1.00106.33 A C ANISOU 542 CD1 LEU A 66 14553 11976 13872 -295 515 -65 A C ATOM 543 CD2 LEU A 66 4.745 -11.424 8.838 1.00112.37 A C ANISOU 543 CD2 LEU A 66 15157 12917 14621 -388 345 -64 A C ATOM 544 N LEU A 67 0.546 -12.571 10.414 1.00 43.87 A N ANISOU 544 N LEU A 67 6254 4495 5918 -3 -106 299 A N ATOM 545 CA LEU A 67 -0.670 -12.839 9.655 1.00 29.96 A C ANISOU 545 CA LEU A 67 4510 2782 4093 125 -197 405 A C ATOM 546 C LEU A 67 -1.402 -14.073 10.171 1.00 27.21 A C ANISOU 546 C LEU A 67 3959 2588 3794 137 -332 428 A C ATOM 547 O LEU A 67 -2.630 -14.127 10.159 1.00 21.52 A O ANISOU 547 O LEU A 67 3198 1938 3039 253 -402 480 A O ATOM 548 CB LEU A 67 -0.342 -13.021 8.171 1.00 23.71 A C ANISOU 548 CB LEU A 67 3821 1941 3244 113 -177 421 A C ATOM 549 CG LEU A 67 0.067 -11.773 7.387 1.00 18.96 A C ANISOU 549 CG LEU A 67 3471 1169 2565 150 -20 432 A C ATOM 550 CD1 LEU A 67 0.600 -12.159 6.018 1.00 21.78 A C ANISOU 550 CD1 LEU A 67 3913 1487 2876 109 2 434 A C ATOM 551 CD2 LEU A 67 -1.107 -10.818 7.256 1.00 31.02 A C ANISOU 551 CD2 LEU A 67 5131 2661 3995 358 -12 539 A C ATOM 552 N GLN A 68 -0.639 -15.060 10.624 1.00 44.27 A N ANISOU 552 N GLN A 68 5573 4754 6494 560 303 -2 A N ATOM 553 CA GLN A 68 -1.200 -16.342 11.037 1.00 39.59 A C ANISOU 553 CA GLN A 68 4962 4048 6031 526 386 -16 A C ATOM 554 C GLN A 68 -2.151 -16.225 12.226 1.00 35.54 A C ANISOU 554 C GLN A 68 4436 3638 5429 526 232 81 A C ATOM 555 O GLN A 68 -3.231 -16.817 12.222 1.00 27.43 A O ANISOU 555 O GLN A 68 3444 2614 4366 461 255 -5 A O ATOM 556 CB GLN A 68 -0.081 -17.337 11.350 1.00 40.30 A C ANISOU 556 CB GLN A 68 4943 3909 6461 593 543 116 A C ATOM 557 CG GLN A 68 0.753 -17.717 10.137 1.00 45.73 A C ANISOU 557 CG GLN A 68 5637 4440 7298 567 772 -39 A C ATOM 558 CD GLN A 68 1.883 -18.667 10.478 1.00 60.42 A C ANISOU 558 CD GLN A 68 7349 6027 9582 657 961 135 A C ATOM 559 NE2 GLN A 68 2.320 -18.644 11.734 1.00 59.66 A N ANISOU 559 NE2 GLN A 68 7115 5968 9584 764 826 474 A N ATOM 560 OE1 GLN A 68 2.359 -19.413 9.623 1.00 72.96 A O ANISOU 560 OE1 GLN A 68 8915 7393 11412 615 1245 -24 A O ATOM 561 N LEU A 69 -1.744 -15.467 13.240 1.00 27.53 A N ANISOU 561 N LEU A 69 3361 2730 4369 569 94 232 A N ATOM 562 CA LEU A 69 -2.548 -15.313 14.449 1.00 27.06 A C ANISOU 562 CA LEU A 69 3271 2805 4206 533 -31 300 A C ATOM 563 C LEU A 69 -3.937 -14.732 14.171 1.00 23.17 A C ANISOU 563 C LEU A 69 2867 2397 3539 481 -83 149 A C ATOM 564 O LEU A 69 -4.944 -15.321 14.567 1.00 13.60 A O ANISOU 564 O LEU A 69 1668 1200 2300 440 -96 133 A O ATOM 565 CB LEU A 69 -1.812 -14.467 15.493 1.00 22.01 A C ANISOU 565 CB LEU A 69 2532 2331 3499 518 -138 411 A C ATOM 566 CG LEU A 69 -2.539 -14.296 16.826 1.00 16.92 A C ANISOU 566 CG LEU A 69 1831 1886 2714 428 -241 449 A C ATOM 567 CD1 LEU A 69 -2.741 -15.646 17.498 1.00 30.65 A C ANISOU 567 CD1 LEU A 69 3485 3616 4545 433 -233 654 A C ATOM 568 CD2 LEU A 69 -1.776 -13.351 17.738 1.00 21.32 A C ANISOU 568 CD2 LEU A 69 2275 2667 3158 340 -312 470 A C ATOM 569 N PRO A 70 -3.997 -13.575 13.490 1.00 21.43 A N ANISOU 569 N PRO A 70 2681 2230 3232 491 -103 76 A N ATOM 570 CA PRO A 70 -5.294 -12.955 13.198 1.00 22.64 A C ANISOU 570 CA PRO A 70 2861 2468 3271 462 -141 13 A C ATOM 571 C PRO A 70 -6.231 -13.901 12.452 1.00 21.44 A C ANISOU 571 C PRO A 70 2751 2337 3056 403 -106 -65 A C ATOM 572 O PRO A 70 -7.433 -13.909 12.717 1.00 19.27 A O ANISOU 572 O PRO A 70 2476 2137 2710 364 -152 -85 A O ATOM 573 CB PRO A 70 -4.921 -11.772 12.302 1.00 28.25 A C ANISOU 573 CB PRO A 70 3558 3202 3976 504 -120 29 A C ATOM 574 CG PRO A 70 -3.522 -11.450 12.673 1.00 27.45 A C ANISOU 574 CG PRO A 70 3427 3036 3967 539 -100 60 A C ATOM 575 CD PRO A 70 -2.875 -12.766 12.983 1.00 28.90 A C ANISOU 575 CD PRO A 70 3611 3155 4217 536 -77 92 A C ATOM 576 N LEU A 71 -5.683 -14.690 11.534 1.00 16.50 A N ANISOU 576 N LEU A 71 2151 1655 2465 372 0 -137 A N ATOM 577 CA LEU A 71 -6.480 -15.637 10.761 1.00 19.85 A C ANISOU 577 CA LEU A 71 2598 2121 2822 253 83 -287 A C ATOM 578 C LEU A 71 -7.060 -16.736 11.646 1.00 20.83 A C ANISOU 578 C LEU A 71 2722 2132 3060 225 119 -304 A C ATOM 579 O LEU A 71 -8.212 -17.133 11.483 1.00 15.54 A O ANISOU 579 O LEU A 71 2061 1547 2298 129 119 -402 A O ATOM 580 CB LEU A 71 -5.643 -16.252 9.639 1.00 16.19 A C ANISOU 580 CB LEU A 71 2145 1604 2402 184 254 -425 A C ATOM 581 CG LEU A 71 -5.255 -15.302 8.503 1.00 34.15 A C ANISOU 581 CG LEU A 71 4408 4060 4507 165 234 -418 A C ATOM 582 CD1 LEU A 71 -4.257 -15.959 7.558 1.00 17.90 A C ANISOU 582 CD1 LEU A 71 2358 1928 2515 85 433 -579 A C ATOM 583 CD2 LEU A 71 -6.492 -14.836 7.746 1.00 23.79 A C ANISOU 583 CD2 LEU A 71 3054 3066 2919 56 151 -421 A C ATOM 584 N VAL A 72 -6.253 -17.225 12.581 1.00 17.63 A N ANISOU 584 N VAL A 72 2279 1561 2858 303 150 -175 A N ATOM 585 CA VAL A 72 -6.692 -18.275 13.493 1.00 21.67 A C ANISOU 585 CA VAL A 72 2753 1965 3517 294 195 -106 A C ATOM 586 C VAL A 72 -7.742 -17.748 14.465 1.00 22.05 A C ANISOU 586 C VAL A 72 2801 2168 3407 284 33 -45 A C ATOM 587 O VAL A 72 -8.721 -18.431 14.767 1.00 18.22 A O ANISOU 587 O VAL A 72 2320 1671 2934 227 57 -82 A O ATOM 588 CB VAL A 72 -5.513 -18.870 14.286 1.00 16.80 A C ANISOU 588 CB VAL A 72 2031 1194 3160 387 257 126 A C ATOM 589 CG1 VAL A 72 -6.024 -19.748 15.417 1.00 27.89 A C ANISOU 589 CG1 VAL A 72 3352 2554 4689 390 265 303 A C ATOM 590 CG2 VAL A 72 -4.595 -19.657 13.359 1.00 18.37 A C ANISOU 590 CG2 VAL A 72 2204 1158 3617 392 492 52 A C ATOM 591 N LEU A 73 -7.533 -16.532 14.956 1.00 15.20 A N ANISOU 591 N LEU A 73 1923 1432 2419 324 -98 21 A N ATOM 592 CA LEU A 73 -8.497 -15.898 15.845 1.00 16.19 A C ANISOU 592 CA LEU A 73 2038 1692 2422 292 -203 26 A C ATOM 593 C LEU A 73 -9.821 -15.690 15.123 1.00 16.20 A C ANISOU 593 C LEU A 73 2080 1755 2321 247 -213 -96 A C ATOM 594 O LEU A 73 -10.890 -15.932 15.684 1.00 18.75 A O ANISOU 594 O LEU A 73 2397 2123 2605 201 -241 -113 A O ATOM 595 CB LEU A 73 -7.956 -14.567 16.367 1.00 16.79 A C ANISOU 595 CB LEU A 73 2077 1863 2440 307 -265 46 A C ATOM 596 CG LEU A 73 -6.808 -14.676 17.374 1.00 22.17 A C ANISOU 596 CG LEU A 73 2671 2607 3147 297 -291 180 A C ATOM 597 CD1 LEU A 73 -6.234 -13.306 17.697 1.00 17.32 A C ANISOU 597 CD1 LEU A 73 2017 2091 2475 265 -311 116 A C ATOM 598 CD2 LEU A 73 -7.272 -15.377 18.642 1.00 19.14 A C ANISOU 598 CD2 LEU A 73 2216 2341 2718 228 -333 293 A C ATOM 599 N GLY A 74 -9.742 -15.244 13.873 1.00 21.33 A N ANISOU 599 N GLY A 74 2745 2445 2914 248 -194 -153 A N ATOM 600 CA GLY A 74 -10.926 -15.055 13.056 1.00 15.42 A C ANISOU 600 CA GLY A 74 1981 1842 2038 187 -217 -206 A C ATOM 601 C GLY A 74 -11.660 -16.360 12.819 1.00 16.30 A C ANISOU 601 C GLY A 74 2112 1956 2127 71 -154 -333 A C ATOM 602 O GLY A 74 -12.886 -16.421 12.903 1.00 16.32 A O ANISOU 602 O GLY A 74 2087 2067 2048 11 -196 -358 A O ATOM 603 N LEU A 75 -10.904 -17.410 12.518 1.00 15.19 A N ANISOU 603 N LEU A 75 2001 1672 2100 32 -19 -423 A N ATOM 604 CA LEU A 75 -11.472 -18.735 12.319 1.00 16.80 A C ANISOU 604 CA LEU A 75 2208 1805 2369 -97 118 -585 A C ATOM 605 C LEU A 75 -12.225 -19.154 13.576 1.00 16.19 A C ANISOU 605 C LEU A 75 2121 1656 2373 -71 78 -498 A C ATOM 606 O LEU A 75 -13.334 -19.678 13.506 1.00 32.22 A O ANISOU 606 O LEU A 75 4143 3743 4356 -178 102 -607 A O ATOM 607 CB LEU A 75 -10.361 -19.745 12.021 1.00 17.86 A C ANISOU 607 CB LEU A 75 2345 1695 2747 -111 334 -663 A C ATOM 608 CG LEU A 75 -10.670 -20.916 11.086 1.00 20.17 A C ANISOU 608 CG LEU A 75 2628 1930 3107 -314 578 -963 A C ATOM 609 CD1 LEU A 75 -9.738 -22.082 11.380 1.00 22.26 A C ANISOU 609 CD1 LEU A 75 2855 1810 3792 -276 845 -963 A C ATOM 610 CD2 LEU A 75 -12.118 -21.358 11.190 1.00 22.12 A C ANISOU 610 CD2 LEU A 75 2862 2293 3248 -452 566 -1085 A C ATOM 611 N SER A 76 -11.607 -18.912 14.727 1.00 15.40 A N ANISOU 611 N SER A 76 2004 1476 2371 47 17 -302 A N ATOM 612 CA SER A 76 -12.164 -19.308 16.014 1.00 15.38 A C ANISOU 612 CA SER A 76 1969 1455 2419 56 -19 -183 A C ATOM 613 C SER A 76 -13.535 -18.694 16.277 1.00 14.68 A C ANISOU 613 C SER A 76 1889 1534 2156 9 -128 -237 A C ATOM 614 O SER A 76 -14.474 -19.396 16.649 1.00 15.20 A O ANISOU 614 O SER A 76 1945 1586 2244 -54 -98 -268 A O ATOM 615 CB SER A 76 -11.200 -18.934 17.142 1.00 17.87 A C ANISOU 615 CB SER A 76 2228 1792 2772 141 -90 40 A C ATOM 616 OG SER A 76 -9.945 -19.568 16.972 1.00 16.73 A O ANISOU 616 OG SER A 76 2036 1491 2831 199 14 153 A O ATOM 617 N VAL A 77 -13.645 -17.382 16.097 1.00 13.77 A N ANISOU 617 N VAL A 77 1769 1549 1913 46 -228 -233 A N ATOM 618 CA VAL A 77 -14.908 -16.691 16.333 1.00 15.17 A C ANISOU 618 CA VAL A 77 1917 1850 1999 22 -296 -252 A C ATOM 619 C VAL A 77 -15.988 -17.114 15.340 1.00 14.25 A C ANISOU 619 C VAL A 77 1781 1835 1797 -68 -286 -350 A C ATOM 620 O VAL A 77 -17.152 -17.267 15.708 1.00 21.46 A O ANISOU 620 O VAL A 77 2663 2809 2680 -118 -309 -369 A O ATOM 621 CB VAL A 77 -14.740 -15.157 16.315 1.00 29.62 A C ANISOU 621 CB VAL A 77 3704 3736 3815 91 -339 -204 A C ATOM 622 CG1 VAL A 77 -13.805 -14.733 15.198 1.00 47.64 A C ANISOU 622 CG1 VAL A 77 5991 6017 6092 138 -328 -182 A C ATOM 623 CG2 VAL A 77 -16.095 -14.471 16.181 1.00 24.37 A C ANISOU 623 CG2 VAL A 77 2963 3164 3132 81 -362 -193 A C ATOM 624 N SER A 78 -15.602 -17.306 14.083 1.00 23.00 A N ANISOU 624 N SER A 78 2891 3004 2845 -119 -247 -422 A N ATOM 625 CA SER A 78 -16.556 -17.739 13.068 1.00 28.24 A C ANISOU 625 CA SER A 78 3503 3864 3362 -271 -234 -541 A C ATOM 626 C SER A 78 -17.073 -19.138 13.388 1.00 31.35 A C ANISOU 626 C SER A 78 3926 4151 3834 -392 -121 -701 A C ATOM 627 O SER A 78 -18.261 -19.415 13.247 1.00 17.99 A O ANISOU 627 O SER A 78 2182 2605 2049 -506 -138 -774 A O ATOM 628 CB SER A 78 -15.933 -17.703 11.669 1.00 17.41 A C ANISOU 628 CB SER A 78 2111 2640 1864 -356 -191 -618 A C ATOM 629 OG SER A 78 -15.032 -18.779 11.473 1.00 24.82 A O ANISOU 629 OG SER A 78 3120 3384 2927 -418 -20 -791 A O ATOM 630 N GLU A 79 -16.174 -20.012 13.833 1.00 17.36 A N ANISOU 630 N GLU A 79 2211 2116 2271 -362 11 -728 A N ATOM 631 CA GLU A 79 -16.550 -21.373 14.200 1.00 23.81 A C ANISOU 631 CA GLU A 79 3028 2754 3267 -454 173 -835 A C ATOM 632 C GLU A 79 -17.529 -21.384 15.369 1.00 18.08 A C ANISOU 632 C GLU A 79 2287 2033 2550 -419 90 -721 A C ATOM 633 O GLU A 79 -18.448 -22.204 15.413 1.00 19.06 A O ANISOU 633 O GLU A 79 2390 2138 2715 -537 173 -839 A O ATOM 634 CB GLU A 79 -15.310 -22.202 14.546 1.00 19.30 A C ANISOU 634 CB GLU A 79 2464 1868 2999 -382 347 -772 A C ATOM 635 CG GLU A 79 -14.514 -22.659 13.333 1.00 20.80 A C ANISOU 635 CG GLU A 79 2657 1980 3264 -479 540 -983 A C ATOM 636 CD GLU A 79 -13.192 -23.303 13.709 1.00 37.06 A C ANISOU 636 CD GLU A 79 4691 3709 5681 -364 713 -853 A C ATOM 637 OE1 GLU A 79 -12.684 -24.130 12.921 1.00 42.59 A O ANISOU 637 OE1 GLU A 79 5368 4221 6592 -467 986 -1061 A O ATOM 638 OE2 GLU A 79 -12.659 -22.984 14.792 1.00 31.05 A O1- ANISOU 638 OE2 GLU A 79 3905 2898 4995 -190 595 -542 A O1- ATOM 639 N ALA A 80 -17.328 -20.472 16.315 1.00 16.50 A N ANISOU 639 N ALA A 80 2089 1868 2311 -284 -51 -524 A N ATOM 640 CA ALA A 80 -18.199 -20.377 17.480 1.00 33.08 A C ANISOU 640 CA ALA A 80 4168 4006 4395 -274 -115 -435 A C ATOM 641 C ALA A 80 -19.584 -19.866 17.096 1.00 28.60 A C ANISOU 641 C ALA A 80 3563 3626 3679 -342 -190 -522 A C ATOM 642 O ALA A 80 -20.598 -20.412 17.526 1.00 30.40 A O ANISOU 642 O ALA A 80 3769 3862 3920 -412 -168 -560 A O ATOM 643 CB ALA A 80 -17.574 -19.482 18.537 1.00 32.27 A C ANISOU 643 CB ALA A 80 4057 3941 4263 -175 -206 -271 A C ATOM 644 N LEU A 81 -19.618 -18.818 16.279 1.00 28.64 A N ANISOU 644 N LEU A 81 3532 3786 3566 -316 -270 -512 A N ATOM 645 CA LEU A 81 -20.876 -18.212 15.857 1.00 29.95 A C ANISOU 645 CA LEU A 81 3601 4158 3622 -357 -345 -499 A C ATOM 646 C LEU A 81 -21.712 -19.161 15.010 1.00 30.19 A C ANISOU 646 C LEU A 81 3586 4332 3551 -541 -306 -655 A C ATOM 647 O LEU A 81 -22.938 -19.176 15.109 1.00 25.47 A O ANISOU 647 O LEU A 81 2909 3868 2902 -606 -344 -656 A O ATOM 648 CB LEU A 81 -20.612 -16.923 15.078 1.00 27.18 A C ANISOU 648 CB LEU A 81 3171 3941 3214 -278 -415 -373 A C ATOM 649 CG LEU A 81 -19.996 -15.779 15.882 1.00 24.82 A C ANISOU 649 CG LEU A 81 2880 3511 3041 -130 -418 -262 A C ATOM 650 CD1 LEU A 81 -19.861 -14.530 15.024 1.00 23.89 A C ANISOU 650 CD1 LEU A 81 2649 3490 2937 -49 -446 -109 A C ATOM 651 CD2 LEU A 81 -20.831 -15.497 17.118 1.00 21.02 A C ANISOU 651 CD2 LEU A 81 2372 2973 2644 -120 -399 -261 A C ATOM 652 N GLU A 82 -21.043 -19.944 14.172 1.00 28.13 A N ANISOU 652 N GLU A 82 3744 3092 3852 145 -86 -244 A N ATOM 653 CA GLU A 82 -21.730 -20.881 13.293 1.00 30.21 A C ANISOU 653 CA GLU A 82 4018 3262 4200 132 -142 -331 A C ATOM 654 C GLU A 82 -22.363 -22.017 14.085 1.00 29.50 A C ANISOU 654 C GLU A 82 3921 3031 4256 99 -158 -274 A C ATOM 655 O GLU A 82 -23.434 -22.512 13.733 1.00 36.05 A O ANISOU 655 O GLU A 82 4743 3785 5172 48 -200 -304 A O ATOM 656 CB GLU A 82 -20.766 -21.441 12.247 1.00 32.12 A C ANISOU 656 CB GLU A 82 4287 3495 4422 206 -164 -445 A C ATOM 657 CG GLU A 82 -20.296 -20.408 11.240 1.00 35.47 A C ANISOU 657 CG GLU A 82 4714 4049 4714 243 -151 -510 A C ATOM 658 CD GLU A 82 -19.292 -20.970 10.257 1.00 33.33 A C ANISOU 658 CD GLU A 82 4471 3774 4418 330 -165 -611 A C ATOM 659 OE1 GLU A 82 -18.924 -20.247 9.308 1.00 20.78 A O ANISOU 659 OE1 GLU A 82 2884 2284 2728 371 -155 -669 A O ATOM 660 OE2 GLU A 82 -18.871 -22.132 10.434 1.00 34.79 A O1- ANISOU 660 OE2 GLU A 82 4678 3856 4685 362 -179 -626 A O1- ATOM 661 N GLU A 83 -21.695 -22.425 15.157 1.00 28.30 A N ANISOU 661 N GLU A 83 3768 2849 4135 130 -124 -187 A N ATOM 662 CA GLU A 83 -22.192 -23.502 15.999 1.00 31.48 A C ANISOU 662 CA GLU A 83 4161 3121 4679 112 -125 -113 A C ATOM 663 C GLU A 83 -23.440 -23.074 16.764 1.00 33.20 A C ANISOU 663 C GLU A 83 4350 3335 4931 41 -112 -13 A C ATOM 664 O GLU A 83 -24.313 -23.892 17.050 1.00 30.12 A O ANISOU 664 O GLU A 83 3943 2829 4674 3 -128 24 A O ATOM 665 CB GLU A 83 -21.105 -23.953 16.974 1.00 35.24 A C ANISOU 665 CB GLU A 83 4639 3589 5161 175 -84 -34 A C ATOM 666 CG GLU A 83 -21.528 -25.081 17.897 1.00 43.91 A C ANISOU 666 CG GLU A 83 5724 4554 6406 172 -72 57 A C ATOM 667 CD GLU A 83 -20.417 -25.507 18.834 1.00 53.29 A C ANISOU 667 CD GLU A 83 6909 5750 7588 245 -29 139 A C ATOM 668 OE1 GLU A 83 -20.683 -26.323 19.741 1.00 58.58 A O ANISOU 668 OE1 GLU A 83 7564 6331 8364 255 -4 238 A O ATOM 669 OE2 GLU A 83 -19.277 -25.024 18.665 1.00 55.62 A O1- ANISOU 669 OE2 GLU A 83 7213 6146 7774 297 -17 112 A O1- ATOM 670 N ILE A 84 -23.521 -21.787 17.086 1.00 27.96 A N ANISOU 670 N ILE A 84 3678 2793 4151 25 -81 34 A N ATOM 671 CA ILE A 84 -24.623 -21.267 17.889 1.00 26.77 A C ANISOU 671 CA ILE A 84 3506 2652 4015 -29 -57 141 A C ATOM 672 C ILE A 84 -25.811 -20.834 17.036 1.00 32.71 A C ANISOU 672 C ILE A 84 4242 3415 4770 -91 -87 95 A C ATOM 673 O ILE A 84 -26.953 -21.196 17.316 1.00 32.25 A O ANISOU 673 O ILE A 84 4158 3288 4809 -142 -98 151 A O ATOM 674 CB ILE A 84 -24.174 -20.070 18.745 1.00 27.75 A C ANISOU 674 CB ILE A 84 3634 2897 4011 -15 -2 218 A C ATOM 675 CG1 ILE A 84 -22.963 -20.450 19.598 1.00 22.41 A C ANISOU 675 CG1 ILE A 84 2966 2228 3320 47 21 263 A C ATOM 676 CG2 ILE A 84 -25.317 -19.580 19.619 1.00 31.03 A C ANISOU 676 CG2 ILE A 84 4034 3316 4440 -60 29 334 A C ATOM 677 CD1 ILE A 84 -22.356 -19.285 20.348 1.00 26.68 A C ANISOU 677 CD1 ILE A 84 3513 2893 3730 61 63 313 A C ATOM 678 N THR A 85 -25.537 -20.053 15.996 1.00 18.24 A N ANISOU 678 N THR A 85 2421 1677 2833 -82 -98 1 A N ATOM 679 CA THR A 85 -26.596 -19.482 15.172 1.00 26.70 A C ANISOU 679 CA THR A 85 3474 2789 3882 -131 -120 -37 A C ATOM 680 C THR A 85 -26.958 -20.379 13.992 1.00 28.96 A C ANISOU 680 C THR A 85 3757 3006 4241 -143 -194 -160 A C ATOM 681 O THR A 85 -28.009 -20.209 13.373 1.00 36.68 A O ANISOU 681 O THR A 85 4710 3994 5234 -192 -228 -187 A O ATOM 682 CB THR A 85 -26.205 -18.090 14.640 1.00 23.31 A C ANISOU 682 CB THR A 85 3054 2505 3298 -111 -86 -68 A C ATOM 683 CG2 THR A 85 -25.691 -17.210 15.772 1.00 16.31 A C ANISOU 683 CG2 THR A 85 2178 1684 2337 -98 -18 32 A C ATOM 684 OG1 THR A 85 -25.183 -18.227 13.646 1.00 26.91 A O ANISOU 684 OG1 THR A 85 3531 2992 3702 -56 -107 -184 A O ATOM 685 N GLU A 86 -26.084 -21.331 13.685 1.00 31.06 A N ANISOU 685 N GLU A 86 4049 3203 4549 -97 -220 -234 A N ATOM 686 CA GLU A 86 -26.299 -22.231 12.558 1.00 37.42 A C ANISOU 686 CA GLU A 86 4863 3936 5418 -101 -291 -366 A C ATOM 687 C GLU A 86 -26.325 -21.449 11.250 1.00 38.81 A C ANISOU 687 C GLU A 86 5044 4227 5474 -84 -315 -473 A C ATOM 688 O GLU A 86 -27.018 -21.818 10.301 1.00 38.96 A O ANISOU 688 O GLU A 86 5055 4223 5523 -111 -379 -569 A O ATOM 689 CB GLU A 86 -27.596 -23.023 12.739 1.00 35.38 A C ANISOU 689 CB GLU A 86 4572 3560 5312 -178 -335 -342 A C ATOM 690 CG GLU A 86 -27.592 -23.930 13.962 1.00 46.56 A C ANISOU 690 CG GLU A 86 5979 4848 6863 -185 -308 -235 A C ATOM 691 CD GLU A 86 -28.862 -24.750 14.091 1.00 54.32 A C ANISOU 691 CD GLU A 86 6922 5705 8012 -263 -349 -210 A C ATOM 692 OE1 GLU A 86 -29.927 -24.280 13.639 1.00 56.42 A O ANISOU 692 OE1 GLU A 86 7153 6012 8272 -323 -381 -219 A O ATOM 693 OE2 GLU A 86 -28.797 -25.864 14.653 1.00 56.96 A O1- ANISOU 693 OE2 GLU A 86 7255 5899 8489 -263 -346 -174 A O1- ATOM 694 N ILE A 87 -25.562 -20.361 11.216 1.00 37.07 A N ANISOU 694 N ILE A 87 4833 4132 5118 -39 -262 -455 A N ATOM 695 CA ILE A 87 -25.456 -19.517 10.034 1.00 36.94 A C ANISOU 695 CA ILE A 87 4819 4237 4979 -9 -267 -538 A C ATOM 696 C ILE A 87 -24.010 -19.480 9.548 1.00 30.02 A C ANISOU 696 C ILE A 87 3976 3405 4025 81 -246 -601 A C ATOM 697 O ILE A 87 -23.086 -19.348 10.349 1.00 27.32 A O ANISOU 697 O ILE A 87 3642 3070 3669 110 -199 -537 A O ATOM 698 CB ILE A 87 -25.927 -18.078 10.332 1.00 43.45 A C ANISOU 698 CB ILE A 87 5619 5179 5711 -35 -210 -452 A C ATOM 699 CG1 ILE A 87 -27.407 -18.066 10.717 1.00 50.50 A C ANISOU 699 CG1 ILE A 87 6475 6039 6672 -116 -226 -384 A C ATOM 700 CG2 ILE A 87 -25.690 -17.177 9.134 1.00 49.40 A C ANISOU 700 CG2 ILE A 87 6372 6060 6336 10 -199 -526 A C ATOM 701 CD1 ILE A 87 -28.321 -18.559 9.625 1.00 55.01 A C ANISOU 701 CD1 ILE A 87 7026 6593 7281 -145 -304 -481 A C ATOM 702 N PRO A 88 -23.809 -19.605 8.228 1.00 21.50 A N ANISOU 702 N PRO A 88 2912 2362 2893 129 -283 -725 A N ATOM 703 CA PRO A 88 -22.464 -19.579 7.643 1.00 19.55 A C ANISOU 703 CA PRO A 88 2695 2163 2572 224 -262 -785 A C ATOM 704 C PRO A 88 -21.833 -18.192 7.732 1.00 20.02 A C ANISOU 704 C PRO A 88 2738 2358 2511 253 -188 -725 A C ATOM 705 O PRO A 88 -22.525 -17.187 7.558 1.00 30.13 A O ANISOU 705 O PRO A 88 3993 3723 3733 222 -166 -695 A O ATOM 706 CB PRO A 88 -22.712 -19.943 6.174 1.00 20.42 A C ANISOU 706 CB PRO A 88 2822 2289 2648 262 -321 -928 A C ATOM 707 CG PRO A 88 -24.088 -20.539 6.138 1.00 24.55 A C ANISOU 707 CG PRO A 88 3329 2733 3266 179 -389 -954 A C ATOM 708 CD PRO A 88 -24.847 -19.847 7.214 1.00 20.29 A C ANISOU 708 CD PRO A 88 2750 2208 2752 101 -351 -818 A C ATOM 709 N PHE A 89 -20.532 -18.144 8.000 1.00 19.49 A N ANISOU 709 N PHE A 89 2682 2310 2413 313 -148 -705 A N ATOM 710 CA PHE A 89 -19.805 -16.880 8.051 1.00 21.37 A C ANISOU 710 CA PHE A 89 2902 2669 2549 340 -80 -656 A C ATOM 711 C PHE A 89 -18.538 -16.918 7.202 1.00 25.99 A C ANISOU 711 C PHE A 89 3499 3304 3072 441 -64 -717 A C ATOM 712 O PHE A 89 -18.011 -17.988 6.896 1.00 25.86 A O ANISOU 712 O PHE A 89 3510 3219 3096 492 -96 -776 A O ATOM 713 CB PHE A 89 -19.463 -16.506 9.495 1.00 19.52 A C ANISOU 713 CB PHE A 89 2653 2428 2334 300 -37 -540 A C ATOM 714 CG PHE A 89 -20.644 -16.033 10.292 1.00 26.92 A C ANISOU 714 CG PHE A 89 3576 3355 3298 214 -29 -462 A C ATOM 715 CD1 PHE A 89 -21.386 -16.923 11.052 1.00 23.22 A C ANISOU 715 CD1 PHE A 89 3111 2780 2933 164 -63 -425 A C ATOM 716 CD2 PHE A 89 -21.014 -14.699 10.280 1.00 16.66 A C ANISOU 716 CD2 PHE A 89 2258 2150 1921 188 20 -420 A C ATOM 717 CE1 PHE A 89 -22.473 -16.490 11.785 1.00 25.70 A C ANISOU 717 CE1 PHE A 89 3408 3087 3270 93 -49 -344 A C ATOM 718 CE2 PHE A 89 -22.101 -14.260 11.011 1.00 15.52 A C ANISOU 718 CE2 PHE A 89 2104 1997 1797 117 35 -344 A C ATOM 719 CZ PHE A 89 -22.831 -15.156 11.764 1.00 19.72 A C ANISOU 719 CZ PHE A 89 2637 2427 2427 71 -1 -304 A C ATOM 720 N SER A 90 -18.058 -15.738 6.824 1.00 27.62 A N ANISOU 720 N SER A 90 3683 3626 3184 472 -8 -696 A N ATOM 721 CA SER A 90 -16.878 -15.621 5.979 1.00 23.76 A C ANISOU 721 CA SER A 90 3196 3199 2632 572 19 -739 A C ATOM 722 C SER A 90 -15.734 -14.936 6.718 1.00 22.24 A C ANISOU 722 C SER A 90 2976 3056 2417 581 79 -656 A C ATOM 723 O SER A 90 -15.949 -14.255 7.721 1.00 24.01 A O ANISOU 723 O SER A 90 3181 3293 2649 510 107 -576 A O ATOM 724 CB SER A 90 -17.214 -14.846 4.704 1.00 32.21 A C ANISOU 724 CB SER A 90 4256 4371 3611 616 36 -790 A C ATOM 725 OG SER A 90 -18.276 -15.464 3.998 1.00 42.31 A O ANISOU 725 OG SER A 90 5556 5617 4904 606 -29 -873 A O ATOM 726 N LEU A 91 -14.518 -15.122 6.215 1.00 25.34 A N ANISOU 726 N LEU A 91 3368 3479 2782 670 99 -678 A N ATOM 727 CA LEU A 91 -13.336 -14.510 6.811 1.00 32.29 A C ANISOU 727 CA LEU A 91 4212 4412 3643 682 150 -605 A C ATOM 728 C LEU A 91 -12.683 -13.530 5.844 1.00 29.67 A C ANISOU 728 C LEU A 91 3852 4190 3232 749 208 -611 A C ATOM 729 O LEU A 91 -12.348 -13.887 4.715 1.00 28.25 A O ANISOU 729 O LEU A 91 3685 4031 3016 843 206 -675 A O ATOM 730 CB LEU A 91 -12.323 -15.581 7.220 1.00 36.07 A C ANISOU 730 CB LEU A 91 4702 4834 4170 731 133 -598 A C ATOM 731 CG LEU A 91 -12.776 -16.626 8.241 1.00 17.33 A C ANISOU 731 CG LEU A 91 2351 2348 1884 680 88 -577 A C ATOM 732 CD1 LEU A 91 -11.683 -17.662 8.452 1.00 18.02 A C ANISOU 732 CD1 LEU A 91 2447 2389 2009 749 83 -569 A C ATOM 733 CD2 LEU A 91 -13.161 -15.969 9.558 1.00 18.97 A C ANISOU 733 CD2 LEU A 91 2536 2566 2107 585 102 -487 A C ATOM 734 N LYS A 92 -12.508 -12.292 6.292 1.00 30.52 A N ANISOU 734 N LYS A 92 3920 4365 3313 705 262 -545 A N ATOM 735 CA LYS A 92 -11.827 -11.282 5.495 1.00 30.84 A C ANISOU 735 CA LYS A 92 3923 4503 3292 763 329 -533 A C ATOM 736 C LYS A 92 -10.348 -11.235 5.852 1.00 35.36 A C ANISOU 736 C LYS A 92 4458 5102 3876 799 356 -487 A C ATOM 737 O LYS A 92 -9.984 -10.976 6.999 1.00 51.36 A O ANISOU 737 O LYS A 92 6463 7119 5934 733 359 -428 A O ATOM 738 CB LYS A 92 -12.448 -9.906 5.719 1.00 40.64 A C ANISOU 738 CB LYS A 92 5138 5796 4505 694 382 -486 A C ATOM 739 CG LYS A 92 -11.705 -8.783 5.013 1.00 43.92 A C ANISOU 739 CG LYS A 92 5507 6306 4874 747 462 -459 A C ATOM 740 CD LYS A 92 -12.131 -8.660 3.564 1.00 60.28 A C ANISOU 740 CD LYS A 92 7585 8435 6886 834 481 -509 A C ATOM 741 CE LYS A 92 -13.444 -7.904 3.444 1.00 64.15 A C ANISOU 741 CE LYS A 92 8079 8947 7348 780 500 -501 A C ATOM 742 NZ LYS A 92 -13.300 -6.491 3.891 1.00 58.28 A N1+ ANISOU 742 NZ LYS A 92 7294 8233 6615 719 560 -411 A N1+ ATOM 743 N TRP A 93 -9.499 -11.493 4.864 1.00 33.60 A N ANISOU 743 N TRP A 93 4226 4916 3624 909 376 -513 A N ATOM 744 CA TRP A 93 -8.057 -11.435 5.061 1.00 21.17 A C ANISOU 744 CA TRP A 93 2607 3376 2059 955 406 -464 A C ATOM 745 C TRP A 93 -7.637 -10.012 5.416 1.00 23.32 A C ANISOU 745 C TRP A 93 2817 3719 2323 905 469 -395 A C ATOM 746 O TRP A 93 -8.037 -9.060 4.750 1.00 29.94 A O ANISOU 746 O TRP A 93 3642 4611 3125 911 520 -395 A O ATOM 747 CB TRP A 93 -7.337 -11.909 3.796 1.00 17.21 A C ANISOU 747 CB TRP A 93 2110 2907 1521 1095 425 -502 A C ATOM 748 CG TRP A 93 -5.856 -12.080 3.944 1.00 20.10 A C ANISOU 748 CG TRP A 93 2433 3302 1903 1156 451 -449 A C ATOM 749 CD1 TRP A 93 -5.199 -13.187 4.397 1.00 21.02 A C ANISOU 749 CD1 TRP A 93 2563 3366 2057 1189 417 -442 A C ATOM 750 CD2 TRP A 93 -4.844 -11.116 3.626 1.00 23.57 A C ANISOU 750 CD2 TRP A 93 2801 3830 2327 1194 521 -387 A C ATOM 751 CE2 TRP A 93 -3.598 -11.707 3.916 1.00 21.72 A C ANISOU 751 CE2 TRP A 93 2537 3598 2120 1247 521 -345 A C ATOM 752 CE3 TRP A 93 -4.871 -9.810 3.126 1.00 17.29 A C ANISOU 752 CE3 TRP A 93 1959 3109 1503 1190 589 -357 A C ATOM 753 NE1 TRP A 93 -3.841 -12.971 4.385 1.00 21.61 A N ANISOU 753 NE1 TRP A 93 2578 3500 2135 1246 458 -379 A N ATOM 754 CZ2 TRP A 93 -2.391 -11.038 3.723 1.00 24.47 A C ANISOU 754 CZ2 TRP A 93 2806 4021 2469 1291 580 -274 A C ATOM 755 CZ3 TRP A 93 -3.672 -9.147 2.935 1.00 18.55 A C ANISOU 755 CZ3 TRP A 93 2043 3335 1669 1233 652 -289 A C ATOM 756 CH2 TRP A 93 -2.449 -9.762 3.232 1.00 22.62 A C ANISOU 756 CH2 TRP A 93 2526 3853 2215 1280 644 -249 A C ATOM 757 N PRO A 94 -6.817 -9.863 6.466 1.00 29.50 A N ANISOU 757 N PRO A 94 3561 4505 3141 856 468 -337 A N ATOM 758 CA PRO A 94 -6.281 -10.967 7.266 1.00 29.12 A C ANISOU 758 CA PRO A 94 3523 4406 3133 859 416 -325 A C ATOM 759 C PRO A 94 -6.973 -11.129 8.619 1.00 35.49 A C ANISOU 759 C PRO A 94 4353 5159 3974 751 372 -305 A C ATOM 760 O PRO A 94 -6.662 -12.077 9.345 1.00 33.94 A O ANISOU 760 O PRO A 94 4166 4918 3812 754 330 -289 A O ATOM 761 CB PRO A 94 -4.820 -10.543 7.497 1.00 34.30 A C ANISOU 761 CB PRO A 94 4106 5127 3800 883 449 -263 A C ATOM 762 CG PRO A 94 -4.686 -9.130 6.887 1.00 39.12 A C ANISOU 762 CG PRO A 94 4669 5811 4385 877 521 -243 A C ATOM 763 CD PRO A 94 -6.077 -8.622 6.726 1.00 32.25 A C ANISOU 763 CD PRO A 94 3842 4920 3492 821 526 -278 A C ATOM 764 N ASN A 95 -7.890 -10.227 8.958 1.00 22.18 A N ANISOU 764 N ASN A 95 2675 3478 2276 666 386 -299 A N ATOM 765 CA ASN A 95 -8.439 -10.202 10.311 1.00 39.56 A C ANISOU 765 CA ASN A 95 4891 5641 4501 569 356 -267 A C ATOM 766 C ASN A 95 -9.830 -9.587 10.453 1.00 50.63 A C ANISOU 766 C ASN A 95 6326 7022 5889 496 365 -276 A C ATOM 767 O ASN A 95 -9.969 -8.491 10.992 1.00 65.47 A O ANISOU 767 O ASN A 95 8190 8933 7754 429 399 -244 A O ATOM 768 CB ASN A 95 -7.462 -9.484 11.247 1.00 46.52 A C ANISOU 768 CB ASN A 95 5718 6574 5384 523 371 -212 A C ATOM 769 CG ASN A 95 -7.003 -8.147 10.692 1.00 52.20 A C ANISOU 769 CG ASN A 95 6390 7364 6081 517 436 -202 A C ATOM 770 ND2 ASN A 95 -5.801 -7.729 11.071 1.00 64.71 A N ANISOU 770 ND2 ASN A 95 7912 8999 7675 511 448 -165 A N ATOM 771 OD1 ASN A 95 -7.722 -7.497 9.931 1.00 40.79 A O ANISOU 771 OD1 ASN A 95 4959 5929 4612 518 477 -223 A O ATOM 772 N ASP A 96 -10.851 -10.300 9.986 1.00 41.30 A N ANISOU 772 N ASP A 96 5190 5787 4717 509 334 -317 A N ATOM 773 CA ASP A 96 -12.240 -9.877 10.165 1.00 28.63 A C ANISOU 773 CA ASP A 96 3614 4159 3106 443 336 -317 A C ATOM 774 C ASP A 96 -13.229 -10.992 9.830 1.00 27.94 A C ANISOU 774 C ASP A 96 3569 3997 3049 454 282 -361 A C ATOM 775 O ASP A 96 -12.951 -11.851 8.993 1.00 17.94 A O ANISOU 775 O ASP A 96 2315 2712 1790 526 255 -416 A O ATOM 776 CB ASP A 96 -12.552 -8.632 9.327 1.00 29.20 A C ANISOU 776 CB ASP A 96 3668 4297 3128 446 400 -322 A C ATOM 777 CG ASP A 96 -12.280 -7.337 10.075 1.00 35.22 A C ANISOU 777 CG ASP A 96 4404 5101 3878 381 453 -269 A C ATOM 778 OD1 ASP A 96 -12.237 -7.366 11.322 1.00 42.58 A O ANISOU 778 OD1 ASP A 96 5342 6006 4829 318 433 -233 A O ATOM 779 OD2 ASP A 96 -12.110 -6.288 9.418 1.00 38.37 A O1- ANISOU 779 OD2 ASP A 96 4776 5556 4246 395 518 -263 A O1- ATOM 780 N VAL A 97 -14.380 -10.974 10.497 1.00 13.84 A N ANISOU 780 N VAL A 97 1805 2168 1284 381 266 -338 A N ATOM 781 CA VAL A 97 -15.436 -11.951 10.247 1.00 14.17 A C ANISOU 781 CA VAL A 97 1880 2136 1369 375 214 -374 A C ATOM 782 C VAL A 97 -16.659 -11.278 9.632 1.00 20.45 A C ANISOU 782 C VAL A 97 2679 2959 2134 346 230 -387 A C ATOM 783 O VAL A 97 -17.213 -10.338 10.201 1.00 18.27 A O ANISOU 783 O VAL A 97 2397 2707 1837 287 268 -333 A O ATOM 784 CB VAL A 97 -15.864 -12.680 11.534 1.00 28.41 A C ANISOU 784 CB VAL A 97 3699 3859 3237 321 179 -324 A C ATOM 785 CG1 VAL A 97 -17.037 -13.609 11.252 1.00 34.52 A C ANISOU 785 CG1 VAL A 97 4499 4550 4068 304 129 -357 A C ATOM 786 CG2 VAL A 97 -14.697 -13.456 12.119 1.00 23.93 A C ANISOU 786 CG2 VAL A 97 3125 3267 2699 359 162 -306 A C ATOM 787 N TYR A 98 -17.076 -11.770 8.470 1.00 21.48 A N ANISOU 787 N TYR A 98 2820 3086 2256 391 200 -460 A N ATOM 788 CA TYR A 98 -18.174 -11.163 7.726 1.00 17.59 A C ANISOU 788 CA TYR A 98 2323 2637 1725 378 212 -476 A C ATOM 789 C TYR A 98 -19.341 -12.120 7.519 1.00 19.86 A C ANISOU 789 C TYR A 98 2630 2855 2062 350 142 -518 A C ATOM 790 O TYR A 98 -19.180 -13.338 7.558 1.00 31.71 A O ANISOU 790 O TYR A 98 4151 4275 3622 365 84 -561 A O ATOM 791 CB TYR A 98 -17.681 -10.685 6.357 1.00 16.60 A C ANISOU 791 CB TYR A 98 2183 2599 1526 464 244 -528 A C ATOM 792 CG TYR A 98 -17.002 -9.333 6.365 1.00 21.20 A C ANISOU 792 CG TYR A 98 2734 3266 2056 475 331 -475 A C ATOM 793 CD1 TYR A 98 -15.776 -9.149 6.996 1.00 13.66 A C ANISOU 793 CD1 TYR A 98 1764 2314 1114 480 357 -439 A C ATOM 794 CD2 TYR A 98 -17.579 -8.244 5.722 1.00 30.52 A C ANISOU 794 CD2 TYR A 98 3894 4523 3178 482 388 -459 A C ATOM 795 CE1 TYR A 98 -15.153 -7.917 6.996 1.00 46.19 A C ANISOU 795 CE1 TYR A 98 5850 6503 5199 483 434 -395 A C ATOM 796 CE2 TYR A 98 -16.964 -7.009 5.717 1.00 40.19 A C ANISOU 796 CE2 TYR A 98 5089 5813 4368 490 474 -409 A C ATOM 797 CZ TYR A 98 -15.752 -6.850 6.355 1.00 46.69 A C ANISOU 797 CZ TYR A 98 5898 6629 5213 487 495 -381 A C ATOM 798 OH TYR A 98 -15.138 -5.618 6.350 1.00 57.54 A O ANISOU 798 OH TYR A 98 7235 8047 6582 480 556 -324 A O ATOM 799 N PHE A 99 -20.521 -11.549 7.300 1.00 30.96 A N ANISOU 799 N PHE A 99 4024 4291 3447 310 151 -502 A N ATOM 800 CA PHE A 99 -21.670 -12.306 6.826 1.00 27.33 A C ANISOU 800 CA PHE A 99 3570 3789 3025 287 84 -551 A C ATOM 801 C PHE A 99 -22.129 -11.701 5.508 1.00 27.68 A C ANISOU 801 C PHE A 99 3598 3932 2989 332 95 -599 A C ATOM 802 O PHE A 99 -22.715 -10.619 5.487 1.00 25.00 A O ANISOU 802 O PHE A 99 3235 3662 2601 310 149 -543 A O ATOM 803 CB PHE A 99 -22.813 -12.274 7.838 1.00 30.37 A C ANISOU 803 CB PHE A 99 3950 4122 3468 195 77 -473 A C ATOM 804 CG PHE A 99 -24.096 -12.857 7.314 1.00 37.95 A C ANISOU 804 CG PHE A 99 4900 5052 4466 162 14 -513 A C ATOM 805 CD1 PHE A 99 -24.257 -14.229 7.213 1.00 37.68 A C ANISOU 805 CD1 PHE A 99 4881 4917 4518 155 -67 -577 A C ATOM 806 CD2 PHE A 99 -25.137 -12.035 6.916 1.00 39.31 A C ANISOU 806 CD2 PHE A 99 5046 5297 4593 139 36 -484 A C ATOM 807 CE1 PHE A 99 -25.432 -14.770 6.727 1.00 34.46 A C ANISOU 807 CE1 PHE A 99 4459 4480 4154 116 -133 -619 A C ATOM 808 CE2 PHE A 99 -26.316 -12.571 6.430 1.00 33.57 A C ANISOU 808 CE2 PHE A 99 4301 4551 3902 105 -29 -519 A C ATOM 809 CZ PHE A 99 -26.463 -13.939 6.335 1.00 20.27 A C ANISOU 809 CZ PHE A 99 2629 2765 2308 90 -117 -590 A C ATOM 810 N GLN A 100 -21.847 -12.398 4.411 1.00 35.20 A N ANISOU 810 N GLN A 100 4562 4891 3920 401 47 -702 A N ATOM 811 CA GLN A 100 -22.132 -11.881 3.077 1.00 36.93 A C ANISOU 811 CA GLN A 100 4765 5218 4048 465 56 -755 A C ATOM 812 C GLN A 100 -21.228 -10.693 2.759 1.00 44.09 A C ANISOU 812 C GLN A 100 5652 6226 4872 528 152 -711 A C ATOM 813 O GLN A 100 -20.078 -10.871 2.361 1.00 57.73 A O ANISOU 813 O GLN A 100 7389 7968 6577 605 167 -744 A O ATOM 814 CB GLN A 100 -23.608 -11.495 2.940 1.00 36.59 A C ANISOU 814 CB GLN A 100 4695 5208 3997 407 41 -732 A C ATOM 815 CG GLN A 100 -24.555 -12.685 2.923 1.00 48.96 A C ANISOU 815 CG GLN A 100 6271 6688 5643 354 -63 -793 A C ATOM 816 CD GLN A 100 -26.005 -12.280 2.745 1.00 51.77 A C ANISOU 816 CD GLN A 100 6590 7089 5991 298 -78 -763 A C ATOM 817 NE2 GLN A 100 -26.329 -11.050 3.127 1.00 53.10 A N ANISOU 817 NE2 GLN A 100 6733 7328 6116 278 6 -659 A N ATOM 818 OE1 GLN A 100 -26.825 -13.065 2.268 1.00 61.13 A O ANISOU 818 OE1 GLN A 100 7769 8246 7212 273 -165 -834 A O ATOM 819 N GLU A 101 -21.746 -9.484 2.942 1.00 44.46 A N ANISOU 819 N GLU A 101 5672 6340 4882 498 223 -633 A N ATOM 820 CA GLU A 101 -20.976 -8.280 2.647 1.00 51.34 A C ANISOU 820 CA GLU A 101 6519 7300 5687 551 323 -585 A C ATOM 821 C GLU A 101 -20.811 -7.393 3.877 1.00 46.20 A C ANISOU 821 C GLU A 101 5862 6628 5064 478 391 -484 A C ATOM 822 O GLU A 101 -20.059 -6.419 3.855 1.00 47.78 A O ANISOU 822 O GLU A 101 6043 6878 5232 505 474 -441 A O ATOM 823 CB GLU A 101 -21.635 -7.493 1.512 1.00 62.81 A C ANISOU 823 CB GLU A 101 7943 8869 7054 605 362 -588 A C ATOM 824 CG GLU A 101 -21.671 -8.237 0.185 1.00 71.49 A C ANISOU 824 CG GLU A 101 9048 10013 8102 695 299 -696 A C ATOM 825 CD GLU A 101 -20.307 -8.324 -0.471 1.00 72.85 A C ANISOU 825 CD GLU A 101 9226 10217 8235 802 328 -732 A C ATOM 826 OE1 GLU A 101 -19.556 -7.327 -0.415 1.00 76.98 A O ANISOU 826 OE1 GLU A 101 9721 10787 8742 829 416 -657 A O ATOM 827 OE2 GLU A 101 -19.987 -9.385 -1.047 1.00 68.90 A O1- ANISOU 827 OE2 GLU A 101 8755 9691 7733 857 257 -828 A O1- ATOM 828 N LYS A 102 -21.513 -7.740 4.949 1.00 35.86 A N ANISOU 828 N LYS A 102 4568 5240 3817 388 357 -447 A N ATOM 829 CA LYS A 102 -21.491 -6.945 6.170 1.00 36.65 A C ANISOU 829 CA LYS A 102 4669 5318 3937 319 416 -356 A C ATOM 830 C LYS A 102 -20.551 -7.550 7.209 1.00 30.75 A C ANISOU 830 C LYS A 102 3940 4496 3246 295 389 -349 A C ATOM 831 O LYS A 102 -20.492 -8.769 7.372 1.00 28.03 A O ANISOU 831 O LYS A 102 3614 4082 2954 294 313 -390 A O ATOM 832 CB LYS A 102 -22.902 -6.827 6.748 1.00 44.27 A C ANISOU 832 CB LYS A 102 5637 6257 4926 245 408 -303 A C ATOM 833 CG LYS A 102 -23.946 -6.348 5.751 1.00 41.59 A C ANISOU 833 CG LYS A 102 5273 5995 4533 267 425 -305 A C ATOM 834 CD LYS A 102 -23.771 -4.874 5.423 1.00 41.41 A C ANISOU 834 CD LYS A 102 5225 6047 4462 293 519 -243 A C ATOM 835 CE LYS A 102 -24.926 -4.359 4.578 1.00 43.37 A C ANISOU 835 CE LYS A 102 5440 6364 4675 310 526 -220 A C ATOM 836 NZ LYS A 102 -26.240 -4.563 5.251 1.00 29.80 A N1+ ANISOU 836 NZ LYS A 102 3732 4626 2966 239 526 -180 A N1+ ATOM 837 N LYS A 103 -19.818 -6.693 7.911 1.00 25.03 A N ANISOU 837 N LYS A 103 3211 3788 2512 275 451 -296 A N ATOM 838 CA LYS A 103 -18.902 -7.151 8.948 1.00 29.29 A C ANISOU 838 CA LYS A 103 3761 4275 3094 253 428 -282 A C ATOM 839 C LYS A 103 -19.638 -7.375 10.264 1.00 23.74 A C ANISOU 839 C LYS A 103 3080 3505 2434 174 408 -226 A C ATOM 840 O LYS A 103 -20.437 -6.541 10.688 1.00 26.92 A O ANISOU 840 O LYS A 103 3488 3921 2819 128 453 -172 A O ATOM 841 CB LYS A 103 -17.760 -6.152 9.148 1.00 23.39 A C ANISOU 841 CB LYS A 103 2992 3575 2319 262 496 -256 A C ATOM 842 CG LYS A 103 -16.750 -6.594 10.193 1.00 28.38 A C ANISOU 842 CG LYS A 103 3626 4170 2987 242 468 -241 A C ATOM 843 CD LYS A 103 -15.487 -5.750 10.148 1.00 43.66 A C ANISOU 843 CD LYS A 103 5528 6159 4902 261 521 -231 A C ATOM 844 CE LYS A 103 -15.765 -4.316 10.553 1.00 55.46 A C ANISOU 844 CE LYS A 103 7013 7665 6392 203 575 -177 A C ATOM 845 NZ LYS A 103 -14.514 -3.510 10.580 1.00 62.01 A N1+ ANISOU 845 NZ LYS A 103 7804 8522 7234 205 602 -163 A N1+ ATOM 846 N VAL A 104 -19.360 -8.504 10.906 1.00 17.40 A N ANISOU 846 N VAL A 104 2291 2632 1687 167 345 -233 A N ATOM 847 CA VAL A 104 -20.017 -8.852 12.161 1.00 16.97 A C ANISOU 847 CA VAL A 104 2256 2514 1678 106 325 -173 A C ATOM 848 C VAL A 104 -19.039 -8.838 13.330 1.00 12.11 A C ANISOU 848 C VAL A 104 1644 1888 1069 92 330 -136 A C ATOM 849 O VAL A 104 -19.429 -8.622 14.476 1.00 15.76 A O ANISOU 849 O VAL A 104 2121 2329 1539 45 341 -74 A O ATOM 850 CB VAL A 104 -20.674 -10.242 12.086 1.00 24.16 A C ANISOU 850 CB VAL A 104 3177 3343 2661 104 250 -197 A C ATOM 851 CG1 VAL A 104 -21.523 -10.494 13.325 1.00 27.04 A C ANISOU 851 CG1 VAL A 104 3554 3646 3074 44 242 -120 A C ATOM 852 CG2 VAL A 104 -21.520 -10.363 10.829 1.00 33.37 A C ANISOU 852 CG2 VAL A 104 4335 4527 3818 121 230 -253 A C ATOM 853 N SER A 105 -17.765 -9.070 13.039 1.00 20.07 A N ANISOU 853 N SER A 105 2637 2919 2072 139 321 -172 A N ATOM 854 CA SER A 105 -16.753 -9.128 14.086 1.00 23.28 A C ANISOU 854 CA SER A 105 3037 3327 2482 132 317 -141 A C ATOM 855 C SER A 105 -15.397 -8.636 13.595 1.00 14.66 A C ANISOU 855 C SER A 105 1914 2299 1359 172 342 -168 A C ATOM 856 O SER A 105 -14.961 -8.977 12.495 1.00 20.59 A O ANISOU 856 O SER A 105 2651 3064 2106 234 336 -217 A O ATOM 857 CB SER A 105 -16.629 -10.552 14.633 1.00 24.18 A C ANISOU 857 CB SER A 105 3161 3369 2659 148 256 -134 A C ATOM 858 OG SER A 105 -15.561 -10.654 15.560 1.00 21.08 A O ANISOU 858 OG SER A 105 2755 2992 2263 154 250 -102 A O ATOM 859 N GLY A 106 -14.739 -7.831 14.421 1.00 17.59 A N ANISOU 859 N GLY A 106 2271 2708 1706 139 370 -134 A N ATOM 860 CA GLY A 106 -13.422 -7.315 14.101 1.00 14.71 A C ANISOU 860 CA GLY A 106 1866 2402 1321 166 394 -149 A C ATOM 861 C GLY A 106 -12.375 -7.807 15.081 1.00 17.77 A C ANISOU 861 C GLY A 106 2235 2794 1723 166 357 -126 A C ATOM 862 O GLY A 106 -12.600 -7.817 16.292 1.00 17.49 A O ANISOU 862 O GLY A 106 2215 2744 1686 120 340 -88 A O ATOM 863 N VAL A 107 -11.228 -8.223 14.553 1.00 20.07 A N ANISOU 863 N VAL A 107 2491 3113 2024 224 346 -145 A N ATOM 864 CA VAL A 107 -10.135 -8.723 15.380 1.00 23.26 A C ANISOU 864 CA VAL A 107 2866 3534 2439 235 311 -118 A C ATOM 865 C VAL A 107 -8.961 -7.752 15.369 1.00 22.44 A C ANISOU 865 C VAL A 107 2706 3505 2315 224 341 -114 A C ATOM 866 O VAL A 107 -8.519 -7.308 14.309 1.00 16.05 A O ANISOU 866 O VAL A 107 1869 2729 1502 261 379 -135 A O ATOM 867 CB VAL A 107 -9.640 -10.097 14.899 1.00 32.55 A C ANISOU 867 CB VAL A 107 4039 4678 3650 316 274 -132 A C ATOM 868 CG1 VAL A 107 -8.449 -10.550 15.731 1.00 37.59 A C ANISOU 868 CG1 VAL A 107 4639 5347 4295 334 247 -94 A C ATOM 869 CG2 VAL A 107 -10.764 -11.117 14.960 1.00 28.22 A C ANISOU 869 CG2 VAL A 107 3541 4043 3137 319 242 -139 A C ATOM 870 N LEU A 108 -8.449 -7.439 16.554 1.00 13.85 A N ANISOU 870 N LEU A 108 1599 2447 1215 176 322 -84 A N ATOM 871 CA LEU A 108 -7.375 -6.465 16.688 1.00 19.49 A C ANISOU 871 CA LEU A 108 2257 3230 1919 148 343 -82 A C ATOM 872 C LEU A 108 -6.256 -6.960 17.602 1.00 17.59 A C ANISOU 872 C LEU A 108 1971 3031 1680 153 292 -53 A C ATOM 873 O LEU A 108 -6.511 -7.542 18.655 1.00 26.22 A O ANISOU 873 O LEU A 108 3088 4111 2764 140 250 -28 A O ATOM 874 CB LEU A 108 -7.935 -5.143 17.216 1.00 13.68 A C ANISOU 874 CB LEU A 108 1540 2500 1157 61 380 -86 A C ATOM 875 CG LEU A 108 -6.943 -4.121 17.772 1.00 33.59 A C ANISOU 875 CG LEU A 108 4011 5079 3672 5 388 -88 A C ATOM 876 CD1 LEU A 108 -5.954 -3.681 16.706 1.00 32.95 A C ANISOU 876 CD1 LEU A 108 3862 5037 3618 39 426 -95 A C ATOM 877 CD2 LEU A 108 -7.689 -2.924 18.339 1.00 28.49 A C ANISOU 877 CD2 LEU A 108 3404 4420 3001 -77 426 -98 A C ATOM 878 N ARG A 109 -5.015 -6.726 17.189 1.00 17.53 A N ANISOU 878 N ARG A 109 1895 3081 1685 178 300 -50 A N ATOM 879 CA ARG A 109 -3.861 -7.032 18.026 1.00 31.17 A C ANISOU 879 CA ARG A 109 3565 4867 3411 179 254 -19 A C ATOM 880 C ARG A 109 -2.947 -5.818 18.171 1.00 36.70 A C ANISOU 880 C ARG A 109 4198 5635 4112 120 269 -24 A C ATOM 881 O ARG A 109 -2.699 -5.092 17.208 1.00 37.44 A O ANISOU 881 O ARG A 109 4262 5737 4227 125 323 -38 A O ATOM 882 CB ARG A 109 -3.089 -8.242 17.485 1.00 27.82 A C ANISOU 882 CB ARG A 109 3111 4447 3012 278 236 4 A C ATOM 883 CG ARG A 109 -3.099 -8.382 15.970 1.00 41.80 A C ANISOU 883 CG ARG A 109 4885 6194 4802 351 282 -19 A C ATOM 884 CD ARG A 109 -2.277 -7.299 15.294 1.00 56.06 A C ANISOU 884 CD ARG A 109 6625 8059 6617 342 328 -21 A C ATOM 885 NE ARG A 109 -0.856 -7.407 15.608 1.00 58.62 A N ANISOU 885 NE ARG A 109 6863 8454 6955 361 307 19 A N ATOM 886 CZ ARG A 109 0.074 -6.577 15.147 1.00 61.47 A C ANISOU 886 CZ ARG A 109 7148 8871 7337 355 341 33 A C ATOM 887 NH1 ARG A 109 -0.266 -5.574 14.351 1.00 64.83 A N1+ ANISOU 887 NH1 ARG A 109 7574 9288 7771 336 404 10 A N1+ ATOM 888 NH2 ARG A 109 1.345 -6.750 15.482 1.00 59.19 A N ANISOU 888 NH2 ARG A 109 6776 8650 7065 370 316 75 A N ATOM 889 N GLU A 110 -2.460 -5.597 19.387 1.00 30.71 A N ANISOU 889 N GLU A 110 3412 4924 3332 65 223 -13 A N ATOM 890 CA GLU A 110 -1.587 -4.465 19.669 1.00 38.81 A C ANISOU 890 CA GLU A 110 4372 6011 4365 -4 225 -25 A C ATOM 891 C GLU A 110 -0.434 -4.877 20.572 1.00 36.02 A C ANISOU 891 C GLU A 110 3947 5738 4000 -5 157 4 A C ATOM 892 O GLU A 110 -0.562 -5.800 21.377 1.00 32.99 A O ANISOU 892 O GLU A 110 3584 5362 3587 24 108 31 A O ATOM 893 CB GLU A 110 -2.375 -3.325 20.320 1.00 44.57 A C ANISOU 893 CB GLU A 110 5150 6718 5067 -102 243 -63 A C ATOM 894 CG GLU A 110 -3.274 -2.559 19.366 1.00 43.10 A C ANISOU 894 CG GLU A 110 5008 6472 4896 -113 323 -87 A C ATOM 895 CD GLU A 110 -4.017 -1.428 20.052 1.00 48.48 A C ANISOU 895 CD GLU A 110 5741 7129 5552 -204 347 -118 A C ATOM 896 OE1 GLU A 110 -4.588 -1.662 21.137 1.00 32.02 A O ANISOU 896 OE1 GLU A 110 3708 5036 3421 -231 308 -118 A O ATOM 897 OE2 GLU A 110 -4.032 -0.305 19.505 1.00 66.53 A O1- ANISOU 897 OE2 GLU A 110 8014 9402 7863 -244 412 -139 A O1- ATOM 898 N LEU A 111 0.691 -4.185 20.435 1.00 49.02 A N ANISOU 898 N LEU A 111 5504 7447 5675 -37 157 5 A N ATOM 899 CA LEU A 111 1.859 -4.453 21.264 1.00 53.56 A C ANISOU 899 CA LEU A 111 5996 8113 6240 -44 90 33 A C ATOM 900 C LEU A 111 2.255 -3.220 22.066 1.00 54.99 A C ANISOU 900 C LEU A 111 6139 8341 6413 -160 64 -7 A C ATOM 901 O LEU A 111 2.502 -2.155 21.502 1.00 59.78 A O ANISOU 901 O LEU A 111 6711 8937 7065 -213 109 -34 A O ATOM 902 CB LEU A 111 3.038 -4.922 20.410 1.00 51.36 A C ANISOU 902 CB LEU A 111 5627 7879 6008 31 102 81 A C ATOM 903 CG LEU A 111 2.980 -6.356 19.884 1.00 46.97 A C ANISOU 903 CG LEU A 111 5096 7298 5454 154 106 125 A C ATOM 904 CD1 LEU A 111 1.984 -6.473 18.743 1.00 50.03 A C ANISOU 904 CD1 LEU A 111 5561 7592 5855 200 171 99 A C ATOM 905 CD2 LEU A 111 4.359 -6.808 19.437 1.00 41.38 A C ANISOU 905 CD2 LEU A 111 4286 6659 4779 223 103 181 A C ATOM 906 N SER A 112 2.315 -3.374 23.384 1.00 54.96 A N ANISOU 906 N SER A 112 6141 8388 6354 -196 -8 -12 A N ATOM 907 CA SER A 112 2.670 -2.270 24.266 1.00 63.52 A C ANISOU 907 CA SER A 112 7196 9518 7419 -307 -46 -63 A C ATOM 908 C SER A 112 3.626 -2.727 25.361 1.00 67.79 A C ANISOU 908 C SER A 112 7665 10173 7918 -309 -141 -41 A C ATOM 909 O SER A 112 3.197 -3.108 26.450 1.00 64.65 A O ANISOU 909 O SER A 112 7315 9801 7447 -307 -191 -42 A O ATOM 910 CB SER A 112 1.412 -1.658 24.885 1.00 70.53 A C ANISOU 910 CB SER A 112 8194 10345 8258 -366 -30 -115 A C ATOM 911 OG SER A 112 1.738 -0.564 25.723 1.00 82.77 A O ANISOU 911 OG SER A 112 9727 11933 9789 -472 -65 -175 A O ATOM 912 N LYS A 113 4.921 -2.684 25.062 1.00 82.78 A N ANISOU 912 N LYS A 113 9104 9653 12695 -1358 727 -1908 A N ATOM 913 CA LYS A 113 5.950 -3.083 26.016 1.00 83.97 A C ANISOU 913 CA LYS A 113 9167 10106 12631 -1433 600 -2311 A C ATOM 914 C LYS A 113 5.790 -4.542 26.433 1.00 72.50 A C ANISOU 914 C LYS A 113 7952 9145 10448 -1310 448 -2294 A C ATOM 915 O LYS A 113 5.065 -4.851 27.378 1.00 73.71 A O ANISOU 915 O LYS A 113 8169 9501 10337 -1262 366 -2552 A O ATOM 916 CB LYS A 113 5.929 -2.170 27.245 1.00 91.43 A C ANISOU 916 CB LYS A 113 9872 10944 13924 -1542 568 -2942 A C ATOM 917 CG LYS A 113 6.269 -0.720 26.940 1.00 99.47 A C ANISOU 917 CG LYS A 113 10583 11414 15796 -1686 700 -3026 A C ATOM 918 CD LYS A 113 7.720 -0.564 26.504 1.00107.25 A C ANISOU 918 CD LYS A 113 11383 12351 17016 -1807 730 -2915 A C ATOM 919 CE LYS A 113 8.661 -0.485 27.698 1.00113.33 A C ANISOU 919 CE LYS A 113 11930 13353 17775 -1914 600 -3562 A C ATOM 920 NZ LYS A 113 8.686 -1.738 28.503 1.00112.10 A N1+ ANISOU 920 NZ LYS A 113 11969 13828 16795 -1805 428 -3736 A N1+ ATOM 921 N ASP A 114 6.476 -5.428 25.718 1.00 68.77 A N ANISOU 921 N ASP A 114 7578 8867 9685 -1254 414 -1977 A N ATOM 922 CA ASP A 114 6.431 -6.867 25.980 1.00 65.54 A C ANISOU 922 CA ASP A 114 7359 8856 8686 -1134 270 -1908 A C ATOM 923 C ASP A 114 5.028 -7.389 26.297 1.00 51.24 A C ANISOU 923 C ASP A 114 5736 7112 6620 -1024 230 -1866 A C ATOM 924 O ASP A 114 4.854 -8.251 27.157 1.00 43.63 A O ANISOU 924 O ASP A 114 4834 6460 5282 -970 108 -1977 A O ATOM 925 CB ASP A 114 7.423 -7.257 27.083 1.00 73.10 A C ANISOU 925 CB ASP A 114 8200 10148 9427 -1186 142 -2249 A C ATOM 926 CG ASP A 114 7.177 -6.517 28.384 1.00 81.93 A C ANISOU 926 CG ASP A 114 9150 11322 10657 -1263 116 -2750 A C ATOM 927 OD1 ASP A 114 8.078 -5.771 28.821 1.00 84.93 A O ANISOU 927 OD1 ASP A 114 9285 11672 11311 -1387 118 -3089 A O ATOM 928 OD2 ASP A 114 6.084 -6.679 28.968 1.00 84.20 A O1- ANISOU 928 OD2 ASP A 114 9521 11706 10765 -1194 91 -2831 A O1- ATOM 929 N LYS A 115 4.035 -6.864 25.587 1.00 47.90 A N ANISOU 929 N LYS A 115 5379 6409 6412 -986 337 -1667 A N ATOM 930 CA LYS A 115 2.657 -7.320 25.734 1.00 34.49 A C ANISOU 930 CA LYS A 115 3850 4747 4507 -882 312 -1594 A C ATOM 931 C LYS A 115 1.999 -7.540 24.378 1.00 23.56 A C ANISOU 931 C LYS A 115 2594 3230 3128 -769 375 -1177 A C ATOM 932 O LYS A 115 2.131 -6.716 23.474 1.00 30.41 A O ANISOU 932 O LYS A 115 3377 3862 4313 -786 501 -977 A O ATOM 933 CB LYS A 115 1.833 -6.308 26.530 1.00 33.89 A C ANISOU 933 CB LYS A 115 3683 4507 4688 -935 368 -1898 A C ATOM 934 CG LYS A 115 2.016 -6.372 28.032 1.00 31.11 A C ANISOU 934 CG LYS A 115 3218 4455 4149 -978 272 -2348 A C ATOM 935 CD LYS A 115 1.005 -5.470 28.720 1.00 32.74 A C ANISOU 935 CD LYS A 115 3333 4544 4564 -989 323 -2662 A C ATOM 936 CE LYS A 115 1.167 -5.485 30.227 1.00 35.52 A C ANISOU 936 CE LYS A 115 3512 5302 4681 -1003 231 -3143 A C ATOM 937 NZ LYS A 115 0.151 -4.618 30.883 1.00 45.93 A N1+ ANISOU 937 NZ LYS A 115 4714 6551 6188 -991 276 -3498 A N1+ ATOM 938 N LEU A 116 1.288 -8.654 24.245 1.00 27.73 A N ANISOU 938 N LEU A 116 3290 3928 3317 -649 286 -1041 A N ATOM 939 CA LEU A 116 0.492 -8.919 23.055 1.00 29.33 A C ANISOU 939 CA LEU A 116 3592 4065 3485 -521 322 -727 A C ATOM 940 C LEU A 116 -0.986 -8.879 23.428 1.00 25.47 A C ANISOU 940 C LEU A 116 3197 3503 2976 -475 328 -756 A C ATOM 941 O LEU A 116 -1.509 -9.818 24.026 1.00 30.07 A O ANISOU 941 O LEU A 116 3871 4250 3305 -433 222 -809 A O ATOM 942 CB LEU A 116 0.854 -10.276 22.452 1.00 26.05 A C ANISOU 942 CB LEU A 116 3253 3884 2761 -408 203 -585 A C ATOM 943 CG LEU A 116 0.075 -10.670 21.196 1.00 24.81 A C ANISOU 943 CG LEU A 116 3156 3745 2524 -252 211 -338 A C ATOM 944 CD1 LEU A 116 0.232 -9.616 20.110 1.00 24.16 A C ANISOU 944 CD1 LEU A 116 2964 3564 2651 -234 368 -104 A C ATOM 945 CD2 LEU A 116 0.522 -12.033 20.694 1.00 21.26 A C ANISOU 945 CD2 LEU A 116 2698 3491 1889 -138 65 -292 A C ATOM 946 N ILE A 117 -1.655 -7.785 23.078 1.00 18.06 A N ANISOU 946 N ILE A 117 2214 2311 2337 -482 457 -695 A N ATOM 947 CA ILE A 117 -3.037 -7.576 23.492 1.00 20.28 A C ANISOU 947 CA ILE A 117 2557 2508 2640 -445 476 -758 A C ATOM 948 C ILE A 117 -4.018 -7.754 22.341 1.00 24.99 A C ANISOU 948 C ILE A 117 3234 3060 3201 -306 510 -449 A C ATOM 949 O ILE A 117 -3.982 -7.013 21.359 1.00 27.40 A O ANISOU 949 O ILE A 117 3464 3222 3726 -268 622 -211 A O ATOM 950 CB ILE A 117 -3.232 -6.176 24.099 1.00 21.99 A C ANISOU 950 CB ILE A 117 2635 2459 3260 -539 583 -987 A C ATOM 951 CG1 ILE A 117 -2.128 -5.876 25.117 1.00 19.98 A C ANISOU 951 CG1 ILE A 117 2241 2271 3078 -673 547 -1344 A C ATOM 952 CG2 ILE A 117 -4.605 -6.061 24.736 1.00 20.38 A C ANISOU 952 CG2 ILE A 117 2481 2240 3023 -497 584 -1124 A C ATOM 953 CD1 ILE A 117 -2.226 -4.499 25.736 1.00 25.64 A C ANISOU 953 CD1 ILE A 117 2765 2716 4262 -766 632 -1671 A C ATOM 954 N VAL A 118 -4.901 -8.736 22.476 1.00 20.64 A N ANISOU 954 N VAL A 118 2803 2654 2385 -225 416 -437 A N ATOM 955 CA VAL A 118 -5.896 -9.022 21.452 1.00 20.70 A C ANISOU 955 CA VAL A 118 2867 2668 2329 -85 421 -209 A C ATOM 956 C VAL A 118 -7.261 -8.461 21.838 1.00 22.02 A C ANISOU 956 C VAL A 118 3059 2695 2613 -68 479 -253 A C ATOM 957 O VAL A 118 -7.736 -8.666 22.955 1.00 16.09 A O ANISOU 957 O VAL A 118 2337 1985 1791 -120 439 -456 A O ATOM 958 CB VAL A 118 -6.016 -10.533 21.196 1.00 14.31 A C ANISOU 958 CB VAL A 118 2129 2069 1240 2 261 -177 A C ATOM 959 CG1 VAL A 118 -7.082 -10.809 20.152 1.00 13.55 A C ANISOU 959 CG1 VAL A 118 2032 1984 1133 152 235 -16 A C ATOM 960 CG2 VAL A 118 -4.673 -11.105 20.761 1.00 19.95 A C ANISOU 960 CG2 VAL A 118 2779 2906 1897 6 185 -148 A C ATOM 961 N GLY A 119 -7.885 -7.746 20.909 1.00 13.03 A N ANISOU 961 N GLY A 119 1882 1429 1639 19 579 -41 A N ATOM 962 CA GLY A 119 -9.197 -7.173 21.141 1.00 17.70 A C ANISOU 962 CA GLY A 119 2483 1878 2364 56 638 -60 A C ATOM 963 C GLY A 119 -10.194 -7.611 20.088 1.00 17.78 A C ANISOU 963 C GLY A 119 2529 1992 2234 218 618 171 A C ATOM 964 O GLY A 119 -9.995 -7.379 18.896 1.00 24.17 A O ANISOU 964 O GLY A 119 3269 2859 3055 322 667 438 A O ATOM 965 N ILE A 120 -11.271 -8.249 20.529 1.00 23.09 A N ANISOU 965 N ILE A 120 3280 2732 2763 249 547 72 A N ATOM 966 CA ILE A 120 -12.293 -8.727 19.608 1.00 30.83 A C ANISOU 966 CA ILE A 120 4272 3824 3617 400 508 226 A C ATOM 967 C ILE A 120 -13.640 -8.066 19.872 1.00 24.35 A C ANISOU 967 C ILE A 120 3448 2870 2935 436 580 222 A C ATOM 968 O ILE A 120 -14.122 -8.038 21.005 1.00 16.36 A O ANISOU 968 O ILE A 120 2467 1800 1947 354 576 21 A O ATOM 969 CB ILE A 120 -12.455 -10.257 19.677 1.00 20.64 A C ANISOU 969 CB ILE A 120 3022 2703 2118 423 320 134 A C ATOM 970 CG1 ILE A 120 -11.133 -10.948 19.334 1.00 21.46 A C ANISOU 970 CG1 ILE A 120 3073 2900 2179 413 221 117 A C ATOM 971 CG2 ILE A 120 -13.553 -10.717 18.731 1.00 16.19 A C ANISOU 971 CG2 ILE A 120 2405 2230 1518 582 259 205 A C ATOM 972 CD1 ILE A 120 -11.194 -12.459 19.420 1.00 15.19 A C ANISOU 972 CD1 ILE A 120 2217 2155 1400 435 57 26 A C ATOM 973 N GLY A 121 -14.239 -7.531 18.814 1.00 26.94 A N ANISOU 973 N GLY A 121 3711 3195 3331 576 646 457 A N ATOM 974 CA GLY A 121 -15.560 -6.938 18.899 1.00 18.89 A C ANISOU 974 CA GLY A 121 2673 2063 2442 640 708 484 A C ATOM 975 C GLY A 121 -16.562 -7.750 18.105 1.00 20.00 A C ANISOU 975 C GLY A 121 2816 2427 2354 788 619 565 A C ATOM 976 O GLY A 121 -16.340 -8.045 16.932 1.00 26.50 A O ANISOU 976 O GLY A 121 3573 3465 3030 918 587 739 A O ATOM 977 N ILE A 122 -17.666 -8.118 18.746 1.00 23.70 A N ANISOU 977 N ILE A 122 3329 2885 2789 774 577 420 A N ATOM 978 CA ILE A 122 -18.702 -8.906 18.089 1.00 13.03 A C ANISOU 978 CA ILE A 122 1955 1720 1274 898 483 447 A C ATOM 979 C ILE A 122 -20.063 -8.226 18.174 1.00 17.70 A C ANISOU 979 C ILE A 122 2513 2228 1985 969 556 488 A C ATOM 980 O ILE A 122 -20.540 -7.907 19.264 1.00 13.99 A O ANISOU 980 O ILE A 122 2077 1613 1624 877 601 342 A O ATOM 981 CB ILE A 122 -18.818 -10.315 18.699 1.00 19.20 A C ANISOU 981 CB ILE A 122 2787 2591 1919 817 333 256 A C ATOM 982 CG1 ILE A 122 -17.453 -11.008 18.715 1.00 21.32 A C ANISOU 982 CG1 ILE A 122 3047 2882 2171 751 234 198 A C ATOM 983 CG2 ILE A 122 -19.838 -11.143 17.930 1.00 19.57 A C ANISOU 983 CG2 ILE A 122 2754 2793 1888 941 227 232 A C ATOM 984 CD1 ILE A 122 -17.475 -12.389 19.339 1.00 18.72 A C ANISOU 984 CD1 ILE A 122 2690 2549 1873 672 87 71 A C ATOM 985 N ASN A 123 -20.682 -8.005 17.018 1.00 15.89 A N ANISOU 985 N ASN A 123 2192 2137 1710 1150 565 679 A N ATOM 986 CA ASN A 123 -22.025 -7.437 16.961 1.00 21.91 A C ANISOU 986 CA ASN A 123 2904 2853 2568 1246 621 738 A C ATOM 987 C ASN A 123 -23.071 -8.525 17.146 1.00 33.59 A C ANISOU 987 C ASN A 123 4397 4480 3886 1235 495 562 A C ATOM 988 O ASN A 123 -23.241 -9.387 16.283 1.00 11.94 A O ANISOU 988 O ASN A 123 1599 1987 952 1312 384 540 A O ATOM 989 CB ASN A 123 -22.255 -6.726 15.627 1.00 29.74 A C ANISOU 989 CB ASN A 123 3756 3984 3561 1455 687 1062 A C ATOM 990 CG ASN A 123 -21.281 -5.588 15.393 1.00 32.43 A C ANISOU 990 CG ASN A 123 4039 4149 4135 1452 830 1317 A C ATOM 991 ND2 ASN A 123 -21.058 -5.257 14.127 1.00 26.18 A N ANISOU 991 ND2 ASN A 123 3099 3587 3262 1629 872 1665 A N ATOM 992 OD1 ASN A 123 -20.740 -5.011 16.336 1.00 28.11 A O ANISOU 992 OD1 ASN A 123 3546 3289 3845 1296 904 1203 A O ATOM 993 N VAL A 124 -23.774 -8.487 18.272 1.00 29.86 A N ANISOU 993 N VAL A 124 3969 3871 3504 1135 517 418 A N ATOM 994 CA VAL A 124 -24.733 -9.538 18.593 1.00 30.07 A C ANISOU 994 CA VAL A 124 3987 4004 3433 1095 404 294 A C ATOM 995 C VAL A 124 -26.170 -9.033 18.741 1.00 30.66 A C ANISOU 995 C VAL A 124 4007 4061 3581 1162 459 302 A C ATOM 996 O VAL A 124 -27.052 -9.444 17.989 1.00 24.96 A O ANISOU 996 O VAL A 124 3210 3492 2784 1264 389 326 A O ATOM 997 CB VAL A 124 -24.301 -10.333 19.851 1.00 18.85 A C ANISOU 997 CB VAL A 124 2623 2538 2001 916 354 150 A C ATOM 998 CG1 VAL A 124 -23.644 -9.417 20.868 1.00 42.03 A C ANISOU 998 CG1 VAL A 124 5610 5334 5024 818 473 88 A C ATOM 999 CG2 VAL A 124 -25.485 -11.073 20.455 1.00 17.63 A C ANISOU 999 CG2 VAL A 124 2412 2436 1851 885 308 83 A C ATOM 1000 N ASN A 125 -26.404 -8.138 19.697 1.00 33.49 A N ANISOU 1000 N ASN A 125 4380 4255 4088 1115 579 245 A N ATOM 1001 CA ASN A 125 -27.764 -7.688 19.988 1.00 28.35 A C ANISOU 1001 CA ASN A 125 3667 3592 3514 1175 632 216 A C ATOM 1002 C ASN A 125 -28.010 -6.188 19.813 1.00 30.32 A C ANISOU 1002 C ASN A 125 3864 3655 4003 1286 777 292 A C ATOM 1003 O ASN A 125 -28.958 -5.646 20.381 1.00 37.21 A O ANISOU 1003 O ASN A 125 4682 4466 4989 1314 841 201 A O ATOM 1004 CB ASN A 125 -28.180 -8.119 21.398 1.00 27.45 A C ANISOU 1004 CB ASN A 125 3551 3512 3367 1045 635 33 A C ATOM 1005 CG ASN A 125 -28.307 -9.624 21.535 1.00 26.65 A C ANISOU 1005 CG ASN A 125 3435 3561 3130 972 509 23 A C ATOM 1006 ND2 ASN A 125 -28.196 -10.117 22.762 1.00 20.64 A N ANISOU 1006 ND2 ASN A 125 2663 2868 2312 842 521 -54 A N ATOM 1007 OD1 ASN A 125 -28.505 -10.335 20.551 1.00 31.88 A O ANISOU 1007 OD1 ASN A 125 4064 4296 3754 1036 400 83 A O ATOM 1008 N GLN A 126 -27.169 -5.519 19.031 1.00 29.46 A N ANISOU 1008 N GLN A 126 2938 3899 4356 1153 287 -43 A N ATOM 1009 CA GLN A 126 -27.384 -4.103 18.751 1.00 36.59 A C ANISOU 1009 CA GLN A 126 3907 4646 5352 1340 188 -93 A C ATOM 1010 C GLN A 126 -28.685 -3.904 17.979 1.00 41.45 A C ANISOU 1010 C GLN A 126 4442 5404 5904 1470 157 -81 A C ATOM 1011 O GLN A 126 -28.832 -4.388 16.857 1.00 45.94 A O ANISOU 1011 O GLN A 126 5005 5997 6455 1386 182 46 A O ATOM 1012 CB GLN A 126 -26.214 -3.501 17.969 1.00 40.37 A C ANISOU 1012 CB GLN A 126 4553 4811 5973 1262 149 -4 A C ATOM 1013 CG GLN A 126 -24.966 -3.229 18.797 1.00 36.21 A C ANISOU 1013 CG GLN A 126 4105 4125 5528 1199 147 -81 A C ATOM 1014 CD GLN A 126 -23.955 -4.354 18.721 1.00 30.41 A C ANISOU 1014 CD GLN A 126 3367 3410 4778 987 217 -20 A C ATOM 1015 NE2 GLN A 126 -24.443 -5.583 18.606 1.00 22.03 A N ANISOU 1015 NE2 GLN A 126 2212 2550 3608 910 279 43 A N ATOM 1016 OE1 GLN A 126 -22.747 -4.120 18.755 1.00 28.87 A O ANISOU 1016 OE1 GLN A 126 3253 3051 4666 895 211 -44 A O ATOM 1017 N ARG A 127 -29.626 -3.191 18.589 1.00 53.45 A N ANISOU 1017 N ARG A 127 5885 7039 7383 1686 97 -233 A N ATOM 1018 CA ARG A 127 -30.928 -2.948 17.978 1.00 60.55 A C ANISOU 1018 CA ARG A 127 6684 8114 8207 1853 50 -270 A C ATOM 1019 C ARG A 127 -30.847 -1.824 16.951 1.00 65.02 A C ANISOU 1019 C ARG A 127 7410 8413 8880 2004 -75 -198 A C ATOM 1020 O ARG A 127 -31.265 -1.985 15.804 1.00 63.32 A O ANISOU 1020 O ARG A 127 7193 8234 8631 2009 -87 -90 A O ATOM 1021 CB ARG A 127 -31.960 -2.601 19.052 1.00 67.49 A C ANISOU 1021 CB ARG A 127 7405 9248 8991 2042 21 -496 A C ATOM 1022 CG ARG A 127 -31.884 -3.491 20.284 1.00 79.92 A C ANISOU 1022 CG ARG A 127 8868 11041 10457 1892 134 -570 A C ATOM 1023 CD ARG A 127 -32.548 -4.839 20.054 1.00 85.55 A C ANISOU 1023 CD ARG A 127 9439 12054 11010 1707 261 -517 A C ATOM 1024 NE ARG A 127 -33.923 -4.855 20.543 1.00 94.31 A N ANISOU 1024 NE ARG A 127 10335 13540 11957 1813 275 -703 A N ATOM 1025 CZ ARG A 127 -34.271 -5.221 21.773 1.00102.96 A C ANISOU 1025 CZ ARG A 127 11313 14887 12919 1757 342 -834 A C ATOM 1026 NH1 ARG A 127 -33.343 -5.607 22.638 1.00103.49 A N1+ ANISOU 1026 NH1 ARG A 127 11472 14851 12997 1616 391 -784 A N1+ ATOM 1027 NH2 ARG A 127 -35.545 -5.204 22.140 1.00105.98 A N ANISOU 1027 NH2 ARG A 127 11481 15644 13142 1840 359 -1024 A N ATOM 1028 N GLU A 128 -30.306 -0.685 17.372 1.00 72.18 A N ANISOU 1028 N GLU A 128 8465 9050 9911 2119 -170 -257 A N ATOM 1029 CA GLU A 128 -30.169 0.471 16.493 1.00 81.19 A C ANISOU 1029 CA GLU A 128 9809 9884 11154 2251 -298 -180 A C ATOM 1030 C GLU A 128 -28.766 0.543 15.901 1.00 78.44 A C ANISOU 1030 C GLU A 128 9660 9227 10919 2019 -264 -9 A C ATOM 1031 O GLU A 128 -27.783 0.675 16.629 1.00 74.58 A O ANISOU 1031 O GLU A 128 9230 8598 10511 1910 -232 -58 A O ATOM 1032 CB GLU A 128 -30.473 1.762 17.255 1.00 89.06 A C ANISOU 1032 CB GLU A 128 10870 10744 12226 2520 -436 -361 A C ATOM 1033 CG GLU A 128 -30.676 2.975 16.362 1.00 99.28 A C ANISOU 1033 CG GLU A 128 12382 11743 13598 2718 -599 -296 A C ATOM 1034 CD GLU A 128 -32.029 2.971 15.680 1.00111.74 A C ANISOU 1034 CD GLU A 128 13857 13541 15058 2948 -679 -318 A C ATOM 1035 OE1 GLU A 128 -32.129 3.478 14.543 1.00114.29 A O ANISOU 1035 OE1 GLU A 128 14350 13679 15394 3024 -772 -170 A O ATOM 1036 OE2 GLU A 128 -32.994 2.455 16.283 1.00117.77 A O1- ANISOU 1036 OE2 GLU A 128 14366 14681 15701 3047 -648 -490 A O1- ATOM 1037 N ILE A 129 -28.678 0.463 14.577 1.00 75.35 A N ANISOU 1037 N ILE A 129 9357 8756 10518 1943 -270 175 A N ATOM 1038 CA ILE A 129 -27.389 0.500 13.894 1.00 73.34 A C ANISOU 1038 CA ILE A 129 9268 8254 10343 1700 -230 329 A C ATOM 1039 C ILE A 129 -27.200 1.796 13.110 1.00 71.97 A C ANISOU 1039 C ILE A 129 9356 7743 10245 1777 -349 429 A C ATOM 1040 O ILE A 129 -28.036 2.151 12.279 1.00 79.76 A O ANISOU 1040 O ILE A 129 10390 8739 11177 1939 -436 506 A O ATOM 1041 CB ILE A 129 -27.229 -0.689 12.934 1.00 73.62 A C ANISOU 1041 CB ILE A 129 9210 8462 10300 1490 -129 473 A C ATOM 1042 CG1 ILE A 129 -27.542 -2.002 13.653 1.00 76.02 A C ANISOU 1042 CG1 ILE A 129 9286 9079 10519 1418 -22 389 A C ATOM 1043 CG2 ILE A 129 -25.826 -0.714 12.348 1.00 67.93 A C ANISOU 1043 CG2 ILE A 129 8623 7537 9650 1225 -80 589 A C ATOM 1044 CD1 ILE A 129 -27.469 -3.221 12.754 1.00 73.30 A C ANISOU 1044 CD1 ILE A 129 8842 8902 10106 1227 70 504 A C ATOM 1045 N PRO A 130 -26.094 2.507 13.374 1.00 63.23 A N ANISOU 1045 N PRO A 130 8430 6336 9257 1656 -356 426 A N ATOM 1046 CA PRO A 130 -25.773 3.777 12.711 1.00 58.97 A C ANISOU 1046 CA PRO A 130 8185 5425 8796 1678 -460 527 A C ATOM 1047 C PRO A 130 -25.696 3.633 11.194 1.00 53.48 A C ANISOU 1047 C PRO A 130 7593 4695 8031 1551 -454 763 A C ATOM 1048 O PRO A 130 -25.219 2.616 10.694 1.00 48.80 A O ANISOU 1048 O PRO A 130 6880 4279 7381 1322 -337 841 A O ATOM 1049 CB PRO A 130 -24.393 4.125 13.275 1.00 57.46 A C ANISOU 1049 CB PRO A 130 8098 5012 8720 1456 -402 470 A C ATOM 1050 CG PRO A 130 -24.332 3.411 14.584 1.00 59.67 A C ANISOU 1050 CG PRO A 130 8149 5525 8997 1474 -331 276 A C ATOM 1051 CD PRO A 130 -25.078 2.133 14.372 1.00 57.38 A C ANISOU 1051 CD PRO A 130 7627 5599 8575 1487 -264 312 A C ATOM 1052 N GLU A 131 -26.160 4.652 10.477 1.00 54.46 A N ANISOU 1052 N GLU A 131 7945 4592 8154 1707 -590 870 A N ATOM 1053 CA GLU A 131 -26.173 4.625 9.017 1.00 64.41 A C ANISOU 1053 CA GLU A 131 9325 5822 9327 1612 -602 1104 A C ATOM 1054 C GLU A 131 -24.771 4.630 8.412 1.00 67.04 A C ANISOU 1054 C GLU A 131 9799 5986 9687 1229 -503 1238 A C ATOM 1055 O GLU A 131 -24.558 4.088 7.328 1.00 63.94 A O ANISOU 1055 O GLU A 131 9383 5709 9202 1054 -444 1396 A O ATOM 1056 CB GLU A 131 -26.981 5.804 8.462 1.00 76.09 A C ANISOU 1056 CB GLU A 131 11055 7064 10789 1895 -794 1189 A C ATOM 1057 CG GLU A 131 -28.485 5.679 8.645 1.00 86.14 A C ANISOU 1057 CG GLU A 131 12158 8588 11983 2277 -899 1075 A C ATOM 1058 CD GLU A 131 -28.918 5.906 10.078 1.00 98.89 A C ANISOU 1058 CD GLU A 131 13644 10255 13673 2490 -939 806 A C ATOM 1059 OE1 GLU A 131 -29.848 5.209 10.537 1.00 99.23 A O ANISOU 1059 OE1 GLU A 131 13403 10663 13639 2647 -918 657 A O ATOM 1060 OE2 GLU A 131 -28.326 6.779 10.746 1.00106.99 A O1- ANISOU 1060 OE2 GLU A 131 14849 10971 14831 2486 -986 735 A O1- ATOM 1061 N GLU A 132 -23.818 5.242 9.108 1.00 73.87 A N ANISOU 1061 N GLU A 132 10792 6604 10672 1095 -482 1155 A N ATOM 1062 CA GLU A 132 -22.461 5.366 8.579 1.00 79.45 A C ANISOU 1062 CA GLU A 132 11633 7155 11400 720 -389 1247 A C ATOM 1063 C GLU A 132 -21.746 4.022 8.475 1.00 75.44 A C ANISOU 1063 C GLU A 132 10862 6959 10841 465 -231 1213 A C ATOM 1064 O GLU A 132 -20.751 3.896 7.761 1.00 80.88 A O ANISOU 1064 O GLU A 132 11604 7624 11504 155 -150 1296 A O ATOM 1065 CB GLU A 132 -21.625 6.345 9.409 1.00 84.78 A C ANISOU 1065 CB GLU A 132 12487 7510 12215 635 -401 1128 A C ATOM 1066 CG GLU A 132 -21.493 5.986 10.879 1.00 88.93 A C ANISOU 1066 CG GLU A 132 12801 8164 12823 721 -360 870 A C ATOM 1067 CD GLU A 132 -22.553 6.645 11.739 1.00 98.37 A C ANISOU 1067 CD GLU A 132 14015 9287 14075 1097 -496 740 A C ATOM 1068 OE1 GLU A 132 -23.683 6.844 11.247 1.00104.53 A O ANISOU 1068 OE1 GLU A 132 14833 10090 14793 1351 -607 821 A O ATOM 1069 OE2 GLU A 132 -22.253 6.968 12.907 1.00 95.68 A O1- ANISOU 1069 OE2 GLU A 132 13636 8885 13833 1147 -497 537 A O1- ATOM 1070 N ILE A 133 -22.254 3.021 9.187 1.00 63.77 A N ANISOU 1070 N ILE A 133 9109 5775 9345 593 -192 1083 A N ATOM 1071 CA ILE A 133 -21.672 1.686 9.139 1.00 56.55 A C ANISOU 1071 CA ILE A 133 7960 5141 8387 392 -65 1044 A C ATOM 1072 C ILE A 133 -22.695 0.663 8.663 1.00 50.53 A C ANISOU 1072 C ILE A 133 6997 4686 7517 509 -53 1095 A C ATOM 1073 O ILE A 133 -22.360 -0.496 8.419 1.00 52.66 A O ANISOU 1073 O ILE A 133 7085 5182 7740 358 37 1086 A O ATOM 1074 CB ILE A 133 -21.135 1.248 10.516 1.00 53.66 A C ANISOU 1074 CB ILE A 133 7452 4845 8090 381 -11 832 A C ATOM 1075 CG1 ILE A 133 -22.292 1.012 11.489 1.00 45.62 A C ANISOU 1075 CG1 ILE A 133 6299 3974 7059 673 -55 721 A C ATOM 1076 CG2 ILE A 133 -20.162 2.281 11.064 1.00 60.12 A C ANISOU 1076 CG2 ILE A 133 8445 5380 9017 277 -20 744 A C ATOM 1077 CD1 ILE A 133 -21.858 0.448 12.825 1.00 41.33 A C ANISOU 1077 CD1 ILE A 133 5610 3544 6550 667 -1 534 A C ATOM 1078 N LYS A 134 -23.942 1.101 8.533 1.00 51.55 A N ANISOU 1078 N LYS A 134 7157 4823 7606 783 -152 1131 A N ATOM 1079 CA LYS A 134 -25.041 0.209 8.177 1.00 56.67 A C ANISOU 1079 CA LYS A 134 7601 5783 8149 913 -143 1144 A C ATOM 1080 C LYS A 134 -24.788 -0.545 6.877 1.00 49.24 A C ANISOU 1080 C LYS A 134 6595 4993 7119 717 -78 1287 A C ATOM 1081 O LYS A 134 -25.300 -1.646 6.679 1.00 43.19 A O ANISOU 1081 O LYS A 134 5611 4516 6284 716 -21 1263 A O ATOM 1082 CB LYS A 134 -26.350 0.994 8.066 1.00 63.53 A C ANISOU 1082 CB LYS A 134 8537 6625 8978 1244 -278 1152 A C ATOM 1083 CG LYS A 134 -27.580 0.121 7.886 1.00 72.17 A C ANISOU 1083 CG LYS A 134 9387 8075 9957 1397 -266 1109 A C ATOM 1084 CD LYS A 134 -27.826 -0.736 9.119 1.00 77.21 A C ANISOU 1084 CD LYS A 134 9798 8935 10602 1409 -186 923 A C ATOM 1085 CE LYS A 134 -29.095 -1.562 8.978 1.00 79.18 A C ANISOU 1085 CE LYS A 134 9811 9543 10730 1534 -164 864 A C ATOM 1086 NZ LYS A 134 -30.302 -0.706 8.815 1.00 85.25 A N1+ ANISOU 1086 NZ LYS A 134 10606 10338 11445 1861 -302 820 A N1+ ATOM 1087 N ASP A 135 -23.996 0.049 5.992 1.00 54.95 A N ANISOU 1087 N ASP A 135 7508 5530 7842 536 -85 1427 A N ATOM 1088 CA ASP A 135 -23.765 -0.527 4.672 1.00 64.07 A C ANISOU 1088 CA ASP A 135 8610 6836 8898 353 -35 1564 A C ATOM 1089 C ASP A 135 -22.654 -1.577 4.662 1.00 58.72 A C ANISOU 1089 C ASP A 135 7771 6303 8237 63 91 1494 A C ATOM 1090 O ASP A 135 -22.512 -2.328 3.698 1.00 61.37 A O ANISOU 1090 O ASP A 135 7989 6834 8493 -78 142 1556 A O ATOM 1091 CB ASP A 135 -23.470 0.572 3.645 1.00 78.77 A C ANISOU 1091 CB ASP A 135 10753 8460 10716 276 -99 1759 A C ATOM 1092 CG ASP A 135 -22.260 1.411 4.014 1.00 90.90 A C ANISOU 1092 CG ASP A 135 12501 9693 12343 69 -80 1748 A C ATOM 1093 OD1 ASP A 135 -22.090 1.731 5.209 1.00 97.97 A O ANISOU 1093 OD1 ASP A 135 13414 10459 13353 148 -91 1599 A O ATOM 1094 OD2 ASP A 135 -21.480 1.759 3.102 1.00 93.15 A O1- ANISOU 1094 OD2 ASP A 135 12929 9887 12578 -185 -50 1880 A O1- ATOM 1095 N ARG A 136 -21.870 -1.631 5.735 1.00 47.29 A N ANISOU 1095 N ARG A 136 6310 4773 6887 -8 129 1350 A N ATOM 1096 CA ARG A 136 -20.752 -2.565 5.803 1.00 45.17 A C ANISOU 1096 CA ARG A 136 5900 4627 6634 -251 224 1256 A C ATOM 1097 C ARG A 136 -20.716 -3.328 7.123 1.00 31.42 A C ANISOU 1097 C ARG A 136 4013 2976 4951 -172 252 1078 A C ATOM 1098 O ARG A 136 -19.693 -3.912 7.477 1.00 36.60 A O ANISOU 1098 O ARG A 136 4591 3676 5638 -328 304 967 A O ATOM 1099 CB ARG A 136 -19.427 -1.824 5.618 1.00 54.99 A C ANISOU 1099 CB ARG A 136 7297 5679 7916 -498 249 1254 A C ATOM 1100 CG ARG A 136 -19.502 -0.629 4.689 1.00 68.90 A C ANISOU 1100 CG ARG A 136 9310 7232 9635 -550 199 1438 A C ATOM 1101 CD ARG A 136 -18.208 0.163 4.718 1.00 81.83 A C ANISOU 1101 CD ARG A 136 11113 8663 11317 -816 236 1410 A C ATOM 1102 NE ARG A 136 -18.445 1.584 4.491 1.00 95.18 A N ANISOU 1102 NE ARG A 136 13118 10028 13019 -778 160 1547 A N ATOM 1103 CZ ARG A 136 -18.779 2.443 5.448 1.00 99.84 A C ANISOU 1103 CZ ARG A 136 13853 10373 13711 -588 87 1486 A C ATOM 1104 NH1 ARG A 136 -18.915 2.024 6.698 1.00 90.36 A N1+ ANISOU 1104 NH1 ARG A 136 12495 9244 12594 -431 91 1294 A N1+ ATOM 1105 NH2 ARG A 136 -18.978 3.721 5.159 1.00111.15 A N ANISOU 1105 NH2 ARG A 136 15594 11482 15154 -553 3 1615 A N ATOM 1106 N ALA A 137 -21.828 -3.322 7.850 1.00 24.32 A N ANISOU 1106 N ALA A 137 3074 2117 4049 73 213 1042 A N ATOM 1107 CA ALA A 137 -21.869 -3.962 9.160 1.00 33.84 A C ANISOU 1107 CA ALA A 137 4165 3405 5287 147 238 889 A C ATOM 1108 C ALA A 137 -23.264 -4.456 9.520 1.00 27.00 A C ANISOU 1108 C ALA A 137 3176 2724 4358 348 228 871 A C ATOM 1109 O ALA A 137 -24.266 -3.811 9.209 1.00 28.90 A O ANISOU 1109 O ALA A 137 3458 2958 4564 523 168 925 A O ATOM 1110 CB ALA A 137 -21.352 -3.014 10.230 1.00 23.90 A C ANISOU 1110 CB ALA A 137 3030 1934 4117 196 205 786 A C ATOM 1111 N THR A 138 -23.317 -5.607 10.180 1.00 23.40 A N ANISOU 1111 N THR A 138 2574 2439 3878 320 283 787 A N ATOM 1112 CA THR A 138 -24.578 -6.170 10.643 1.00 24.38 A C ANISOU 1112 CA THR A 138 2572 2762 3929 461 296 750 A C ATOM 1113 C THR A 138 -24.382 -6.849 11.992 1.00 27.38 A C ANISOU 1113 C THR A 138 2894 3201 4308 455 333 631 A C ATOM 1114 O THR A 138 -23.254 -7.031 12.446 1.00 23.16 A O ANISOU 1114 O THR A 138 2402 2572 3827 351 344 581 A O ATOM 1115 CB THR A 138 -25.155 -7.182 9.633 1.00 22.24 A C ANISOU 1115 CB THR A 138 2166 2705 3579 391 342 817 A C ATOM 1116 CG2 THR A 138 -24.308 -8.443 9.598 1.00 29.12 A C ANISOU 1116 CG2 THR A 138 2965 3640 4461 194 404 792 A C ATOM 1117 OG1 THR A 138 -26.495 -7.523 10.007 1.00 34.15 A O ANISOU 1117 OG1 THR A 138 3556 4415 5006 525 356 770 A O ATOM 1118 N THR A 139 -25.486 -7.218 12.632 1.00 27.80 A N ANISOU 1118 N THR A 139 2849 3429 4285 565 351 579 A N ATOM 1119 CA THR A 139 -25.430 -7.887 13.924 1.00 26.88 A C ANISOU 1119 CA THR A 139 2689 3389 4135 553 389 485 A C ATOM 1120 C THR A 139 -26.071 -9.266 13.838 1.00 22.32 A C ANISOU 1120 C THR A 139 1991 3029 3460 461 462 502 A C ATOM 1121 O THR A 139 -26.709 -9.601 12.840 1.00 22.95 A O ANISOU 1121 O THR A 139 1995 3224 3501 434 483 560 A O ATOM 1122 CB THR A 139 -26.144 -7.067 15.013 1.00 25.58 A C ANISOU 1122 CB THR A 139 2521 3250 3948 743 353 380 A C ATOM 1123 CG2 THR A 139 -25.690 -5.615 14.970 1.00 23.38 A C ANISOU 1123 CG2 THR A 139 2374 2737 3774 849 270 361 A C ATOM 1124 OG1 THR A 139 -27.561 -7.126 14.810 1.00 23.38 A O ANISOU 1124 OG1 THR A 139 2127 3182 3573 850 361 364 A O ATOM 1125 N LEU A 140 -25.895 -10.067 14.884 1.00 18.61 A N ANISOU 1125 N LEU A 140 1514 2611 2945 405 498 451 A N ATOM 1126 CA LEU A 140 -26.510 -11.387 14.936 1.00 40.04 A C ANISOU 1126 CA LEU A 140 4148 5502 5562 295 570 468 A C ATOM 1127 C LEU A 140 -28.029 -11.265 14.989 1.00 35.24 A C ANISOU 1127 C LEU A 140 3419 5122 4848 374 607 431 A C ATOM 1128 O LEU A 140 -28.750 -12.135 14.502 1.00 34.54 A O ANISOU 1128 O LEU A 140 3237 5200 4686 280 670 452 A O ATOM 1129 CB LEU A 140 -26.001 -12.174 16.145 1.00 17.98 A C ANISOU 1129 CB LEU A 140 1413 2692 2726 230 588 434 A C ATOM 1130 CG LEU A 140 -24.533 -12.608 16.122 1.00 24.46 A C ANISOU 1130 CG LEU A 140 2330 3339 3626 151 548 442 A C ATOM 1131 CD1 LEU A 140 -24.179 -13.371 17.390 1.00 21.22 A C ANISOU 1131 CD1 LEU A 140 1990 2926 3147 125 550 410 A C ATOM 1132 CD2 LEU A 140 -24.235 -13.450 14.891 1.00 19.52 A C ANISOU 1132 CD2 LEU A 140 1673 2708 3035 22 559 502 A C ATOM 1133 N TYR A 141 -28.508 -10.176 15.583 1.00 34.81 A N ANISOU 1133 N TYR A 141 3357 5085 4785 549 564 354 A N ATOM 1134 CA TYR A 141 -29.941 -9.938 15.709 1.00 23.96 A C ANISOU 1134 CA TYR A 141 1848 3953 3302 658 583 274 A C ATOM 1135 C TYR A 141 -30.577 -9.622 14.360 1.00 26.34 A C ANISOU 1135 C TYR A 141 2082 4319 3608 725 557 315 A C ATOM 1136 O TYR A 141 -31.714 -10.009 14.093 1.00 30.59 A O ANISOU 1136 O TYR A 141 2473 5112 4037 732 603 265 A O ATOM 1137 CB TYR A 141 -30.213 -8.800 16.695 1.00 22.94 A C ANISOU 1137 CB TYR A 141 1726 3820 3173 855 521 153 A C ATOM 1138 CG TYR A 141 -31.645 -8.305 16.677 1.00 37.47 A C ANISOU 1138 CG TYR A 141 3417 5906 4915 1021 506 38 A C ATOM 1139 CD1 TYR A 141 -31.983 -7.123 16.027 1.00 36.22 A C ANISOU 1139 CD1 TYR A 141 3275 5671 4814 1240 399 15 A C ATOM 1140 CD2 TYR A 141 -32.657 -9.022 17.304 1.00 27.92 A C ANISOU 1140 CD2 TYR A 141 2054 5010 3543 957 592 -57 A C ATOM 1141 CE1 TYR A 141 -33.286 -6.667 16.005 1.00 37.40 A C ANISOU 1141 CE1 TYR A 141 3282 6060 4869 1427 363 -117 A C ATOM 1142 CE2 TYR A 141 -33.964 -8.575 17.288 1.00 34.55 A C ANISOU 1142 CE2 TYR A 141 2728 6119 4281 1111 577 -200 A C ATOM 1143 CZ TYR A 141 -34.273 -7.397 16.637 1.00 33.50 A C ANISOU 1143 CZ TYR A 141 2601 5913 4213 1364 454 -239 A C ATOM 1144 OH TYR A 141 -35.574 -6.948 16.617 1.00 43.14 A O ANISOU 1144 OH TYR A 141 3650 7415 5327 1553 418 -407 A O ATOM 1145 N GLU A 142 -29.837 -8.918 13.511 1.00 21.84 A N ANISOU 1145 N GLU A 142 1619 3531 3148 766 487 399 A N ATOM 1146 CA GLU A 142 -30.343 -8.551 12.197 1.00 38.77 A C ANISOU 1146 CA GLU A 142 3728 5717 5285 837 449 459 A C ATOM 1147 C GLU A 142 -30.367 -9.754 11.261 1.00 37.57 A C ANISOU 1147 C GLU A 142 3487 5689 5097 651 526 527 A C ATOM 1148 O GLU A 142 -31.252 -9.875 10.416 1.00 39.61 A O ANISOU 1148 O GLU A 142 3631 6132 5287 693 534 526 A O ATOM 1149 CB GLU A 142 -29.503 -7.428 11.590 1.00 38.97 A C ANISOU 1149 CB GLU A 142 3922 5463 5423 904 355 544 A C ATOM 1150 CG GLU A 142 -30.019 -6.938 10.252 1.00 52.12 A C ANISOU 1150 CG GLU A 142 5586 7156 7063 996 300 625 A C ATOM 1151 CD GLU A 142 -29.211 -5.780 9.707 1.00 66.63 A C ANISOU 1151 CD GLU A 142 7626 8697 8992 1038 209 725 A C ATOM 1152 OE1 GLU A 142 -29.556 -5.275 8.617 1.00 74.68 A O ANISOU 1152 OE1 GLU A 142 8686 9706 9982 1118 149 815 A O ATOM 1153 OE2 GLU A 142 -28.232 -5.374 10.367 1.00 66.12 A O1- ANISOU 1153 OE2 GLU A 142 7686 8415 9021 984 199 713 A O1- ATOM 1154 N ILE A 143 -29.392 -10.643 11.419 1.00 24.63 A N ANISOU 1154 N ILE A 143 1898 3956 3506 458 573 568 A N ATOM 1155 CA ILE A 143 -29.296 -11.825 10.571 1.00 31.97 A C ANISOU 1155 CA ILE A 143 2753 4973 4420 280 635 615 A C ATOM 1156 C ILE A 143 -30.361 -12.859 10.922 1.00 36.59 A C ANISOU 1156 C ILE A 143 3202 5808 4891 201 726 548 A C ATOM 1157 O ILE A 143 -31.133 -13.287 10.063 1.00 43.07 A O ANISOU 1157 O ILE A 143 3893 6818 5654 169 765 540 A O ATOM 1158 CB ILE A 143 -27.913 -12.493 10.688 1.00 33.64 A C ANISOU 1158 CB ILE A 143 3061 5006 4716 121 639 651 A C ATOM 1159 CG1 ILE A 143 -26.802 -11.489 10.375 1.00 28.34 A C ANISOU 1159 CG1 ILE A 143 2511 4110 4145 158 565 695 A C ATOM 1160 CG2 ILE A 143 -27.826 -13.697 9.762 1.00 39.51 A C ANISOU 1160 CG2 ILE A 143 3722 5836 5452 -45 686 678 A C ATOM 1161 CD1 ILE A 143 -25.409 -12.013 10.658 1.00 16.66 A C ANISOU 1161 CD1 ILE A 143 1109 2482 2739 30 558 682 A C ATOM 1162 N THR A 144 -30.395 -13.257 12.190 1.00 31.50 A N ANISOU 1162 N THR A 144 2591 5174 4204 156 764 496 A N ATOM 1163 CA THR A 144 -31.272 -14.333 12.638 1.00 36.05 A C ANISOU 1163 CA THR A 144 3074 5962 4661 21 865 444 A C ATOM 1164 C THR A 144 -32.673 -13.847 13.001 1.00 38.39 A C ANISOU 1164 C THR A 144 3225 6530 4830 134 893 329 A C ATOM 1165 O THR A 144 -33.640 -14.606 12.930 1.00 47.12 A O ANISOU 1165 O THR A 144 4200 7882 5824 23 984 268 A O ATOM 1166 CB THR A 144 -30.674 -15.066 13.851 1.00 45.54 A C ANISOU 1166 CB THR A 144 4398 7061 5846 -100 893 453 A C ATOM 1167 CG2 THR A 144 -29.352 -15.719 13.479 1.00 40.54 A C ANISOU 1167 CG2 THR A 144 3884 6196 5321 -204 858 532 A C ATOM 1168 OG1 THR A 144 -30.453 -14.131 14.913 1.00 47.47 A O ANISOU 1168 OG1 THR A 144 4707 7239 6092 42 844 410 A O ATOM 1169 N GLY A 145 -32.778 -12.582 13.395 1.00 35.24 A N ANISOU 1169 N GLY A 145 2845 6094 4450 352 812 280 A N ATOM 1170 CA GLY A 145 -34.055 -12.011 13.783 1.00 29.50 A C ANISOU 1170 CA GLY A 145 1971 5630 3606 501 813 137 A C ATOM 1171 C GLY A 145 -34.408 -12.301 15.228 1.00 41.43 A C ANISOU 1171 C GLY A 145 3460 7272 5008 438 876 41 A C ATOM 1172 O GLY A 145 -35.561 -12.164 15.635 1.00 43.59 A O ANISOU 1172 O GLY A 145 3574 7843 5147 491 911 -106 A O ATOM 1173 N LYS A 146 -33.408 -12.703 16.006 1.00 44.82 A N ANISOU 1173 N LYS A 146 4043 7503 5483 326 886 114 A N ATOM 1174 CA LYS A 146 -33.605 -13.020 17.415 1.00 45.17 A C ANISOU 1174 CA LYS A 146 4096 7654 5412 251 942 50 A C ATOM 1175 C LYS A 146 -32.373 -12.646 18.234 1.00 38.10 A C ANISOU 1175 C LYS A 146 3376 6492 4609 299 876 97 A C ATOM 1176 O LYS A 146 -31.264 -12.564 17.704 1.00 30.32 A O ANISOU 1176 O LYS A 146 2514 5239 3766 303 818 195 A O ATOM 1177 CB LYS A 146 -33.913 -14.508 17.587 1.00 46.01 A C ANISOU 1177 CB LYS A 146 4198 7880 5403 -34 1068 92 A C ATOM 1178 CG LYS A 146 -32.938 -15.424 16.869 1.00 48.68 A C ANISOU 1178 CG LYS A 146 4670 7977 5849 -184 1067 239 A C ATOM 1179 CD LYS A 146 -33.261 -16.888 17.125 1.00 57.08 A C ANISOU 1179 CD LYS A 146 5764 9123 6802 -462 1179 276 A C ATOM 1180 CE LYS A 146 -33.061 -17.246 18.588 1.00 67.28 A C ANISOU 1180 CE LYS A 146 7180 10401 7984 -550 1208 290 A C ATOM 1181 NZ LYS A 146 -33.290 -18.697 18.834 1.00 73.10 A N1+ ANISOU 1181 NZ LYS A 146 8003 11160 8612 -838 1307 355 A N1+ ATOM 1182 N ASP A 147 -32.574 -12.417 19.527 1.00 34.59 A N ANISOU 1182 N ASP A 147 2924 6149 4070 330 888 9 A N ATOM 1183 CA ASP A 147 -31.474 -12.080 20.422 1.00 33.43 A C ANISOU 1183 CA ASP A 147 2921 5793 3987 380 830 27 A C ATOM 1184 C ASP A 147 -30.664 -13.315 20.802 1.00 39.61 A C ANISOU 1184 C ASP A 147 3851 6456 4743 175 872 146 A C ATOM 1185 O ASP A 147 -31.130 -14.445 20.658 1.00 38.53 A O ANISOU 1185 O ASP A 147 3708 6424 4507 -20 958 200 A O ATOM 1186 CB ASP A 147 -31.997 -11.392 21.684 1.00 35.48 A C ANISOU 1186 CB ASP A 147 3106 6232 4144 496 824 -124 A C ATOM 1187 CG ASP A 147 -32.363 -9.940 21.448 1.00 39.36 A C ANISOU 1187 CG ASP A 147 3515 6723 4718 765 727 -250 A C ATOM 1188 OD1 ASP A 147 -33.020 -9.342 22.327 1.00 51.73 A O ANISOU 1188 OD1 ASP A 147 4975 8486 6196 883 715 -412 A O ATOM 1189 OD2 ASP A 147 -31.995 -9.397 20.386 1.00 41.99 A O1- ANISOU 1189 OD2 ASP A 147 3898 6859 5198 857 657 -190 A O1- ATOM 1190 N TRP A 148 -29.447 -13.089 21.284 1.00 39.80 A N ANISOU 1190 N TRP A 148 4012 6255 4854 227 802 173 A N ATOM 1191 CA TRP A 148 -28.575 -14.177 21.707 1.00 40.64 A C ANISOU 1191 CA TRP A 148 4274 6230 4936 85 808 268 A C ATOM 1192 C TRP A 148 -27.908 -13.856 23.040 1.00 42.74 A C ANISOU 1192 C TRP A 148 4624 6453 5163 162 764 219 A C ATOM 1193 O TRP A 148 -27.550 -12.709 23.306 1.00 39.06 A O ANISOU 1193 O TRP A 148 4130 5931 4780 332 701 128 A O ATOM 1194 CB TRP A 148 -27.516 -14.462 20.639 1.00 30.49 A C ANISOU 1194 CB TRP A 148 3070 4703 3812 60 752 348 A C ATOM 1195 CG TRP A 148 -28.095 -14.872 19.320 1.00 31.00 A C ANISOU 1195 CG TRP A 148 3052 4819 3908 -23 793 396 A C ATOM 1196 CD1 TRP A 148 -28.430 -14.052 18.282 1.00 29.43 A C ANISOU 1196 CD1 TRP A 148 2751 4637 3793 71 773 377 A C ATOM 1197 CD2 TRP A 148 -28.415 -16.203 18.898 1.00 33.08 A C ANISOU 1197 CD2 TRP A 148 3332 5124 4113 -216 857 467 A C ATOM 1198 CE2 TRP A 148 -28.938 -16.114 17.591 1.00 38.43 A C ANISOU 1198 CE2 TRP A 148 3888 5868 4845 -227 879 472 A C ATOM 1199 CE3 TRP A 148 -28.309 -17.462 19.497 1.00 30.11 A C ANISOU 1199 CE3 TRP A 148 3078 4723 3641 -381 892 528 A C ATOM 1200 NE1 TRP A 148 -28.936 -14.790 17.237 1.00 29.83 A N ANISOU 1200 NE1 TRP A 148 2735 4765 3834 -44 824 425 A N ATOM 1201 CZ2 TRP A 148 -29.353 -17.235 16.876 1.00 40.60 A C ANISOU 1201 CZ2 TRP A 148 4134 6202 5090 -400 942 516 A C ATOM 1202 CZ3 TRP A 148 -28.722 -18.573 18.784 1.00 37.13 A C ANISOU 1202 CZ3 TRP A 148 3963 5638 4507 -559 951 581 A C ATOM 1203 CH2 TRP A 148 -29.237 -18.452 17.488 1.00 44.54 A C ANISOU 1203 CH2 TRP A 148 4754 6659 5511 -569 979 565 A C ATOM 1204 N ASP A 149 -27.750 -14.874 23.880 1.00 44.65 A N ANISOU 1204 N ASP A 149 4977 6718 5270 35 794 280 A N ATOM 1205 CA ASP A 149 -27.116 -14.689 25.180 1.00 40.21 A C ANISOU 1205 CA ASP A 149 4499 6138 4641 104 751 241 A C ATOM 1206 C ASP A 149 -25.637 -14.361 25.007 1.00 34.32 A C ANISOU 1206 C ASP A 149 3848 5136 4059 215 643 230 A C ATOM 1207 O ASP A 149 -24.843 -15.214 24.608 1.00 32.05 A O ANISOU 1207 O ASP A 149 3679 4685 3814 148 606 311 A O ATOM 1208 CB ASP A 149 -27.293 -15.934 26.050 1.00 36.72 A C ANISOU 1208 CB ASP A 149 4188 5767 3997 -67 800 336 A C ATOM 1209 CG ASP A 149 -26.888 -15.699 27.492 1.00 46.65 A C ANISOU 1209 CG ASP A 149 5507 7082 5135 7 767 288 A C ATOM 1210 OD1 ASP A 149 -27.733 -15.905 28.388 1.00 52.38 A O ANISOU 1210 OD1 ASP A 149 6204 8043 5653 -83 842 277 A O ATOM 1211 OD2 ASP A 149 -25.729 -15.298 27.729 1.00 53.15 A O1- ANISOU 1211 OD2 ASP A 149 6396 7741 6060 147 669 249 A O1- ATOM 1212 N ARG A 150 -25.276 -13.119 25.312 1.00 33.35 A N ANISOU 1212 N ARG A 150 3663 4985 4023 383 592 110 A N ATOM 1213 CA ARG A 150 -23.915 -12.635 25.103 1.00 25.16 A C ANISOU 1213 CA ARG A 150 2686 3731 3142 473 503 65 A C ATOM 1214 C ARG A 150 -22.871 -13.459 25.851 1.00 31.48 A C ANISOU 1214 C ARG A 150 3626 4453 3881 457 450 86 A C ATOM 1215 O ARG A 150 -21.798 -13.743 25.317 1.00 30.92 A O ANISOU 1215 O ARG A 150 3621 4215 3913 456 388 92 A O ATOM 1216 CB ARG A 150 -23.805 -11.160 25.497 1.00 21.98 A C ANISOU 1216 CB ARG A 150 2206 3322 2824 638 465 -83 A C ATOM 1217 CG ARG A 150 -24.541 -10.221 24.558 1.00 21.96 A C ANISOU 1217 CG ARG A 150 2106 3314 2924 696 474 -106 A C ATOM 1218 CD ARG A 150 -24.303 -8.763 24.920 1.00 22.59 A C ANISOU 1218 CD ARG A 150 2150 3325 3107 862 416 -252 A C ATOM 1219 NE ARG A 150 -24.820 -8.431 26.244 1.00 36.71 A N ANISOU 1219 NE ARG A 150 3872 5299 4777 953 423 -373 A N ATOM 1220 CZ ARG A 150 -24.058 -8.215 27.311 1.00 38.11 A C ANISOU 1220 CZ ARG A 150 4077 5469 4934 1011 388 -471 A C ATOM 1221 NH1 ARG A 150 -24.616 -7.918 28.476 1.00 40.74 A N1+ ANISOU 1221 NH1 ARG A 150 4330 6004 5143 1089 398 -586 A N1+ ATOM 1222 NH2 ARG A 150 -22.738 -8.290 27.212 1.00 40.28 A N ANISOU 1222 NH2 ARG A 150 4444 5560 5302 993 343 -472 A N ATOM 1223 N LYS A 151 -23.184 -13.840 27.085 1.00 31.30 A N ANISOU 1223 N LYS A 151 3647 4568 3677 451 468 89 A N ATOM 1224 CA LYS A 151 -22.254 -14.620 27.894 1.00 34.64 A C ANISOU 1224 CA LYS A 151 4222 4927 4013 462 402 115 A C ATOM 1225 C LYS A 151 -22.006 -15.993 27.279 1.00 31.21 A C ANISOU 1225 C LYS A 151 3929 4367 3562 337 386 256 A C ATOM 1226 O LYS A 151 -20.871 -16.467 27.229 1.00 34.74 A O ANISOU 1226 O LYS A 151 4482 4664 4054 387 290 247 A O ATOM 1227 CB LYS A 151 -22.768 -14.763 29.327 1.00 39.78 A C ANISOU 1227 CB LYS A 151 4900 5773 4441 462 432 110 A C ATOM 1228 CG LYS A 151 -21.858 -15.581 30.229 1.00 48.44 A C ANISOU 1228 CG LYS A 151 6177 6811 5416 492 352 151 A C ATOM 1229 CD LYS A 151 -22.348 -15.588 31.673 1.00 64.59 A C ANISOU 1229 CD LYS A 151 8241 9074 7227 494 382 142 A C ATOM 1230 CE LYS A 151 -22.018 -14.284 32.387 1.00 76.51 A C ANISOU 1230 CE LYS A 151 9607 10684 8781 673 353 -57 A C ATOM 1231 NZ LYS A 151 -22.834 -13.135 31.901 1.00 85.60 A N1+ ANISOU 1231 NZ LYS A 151 10553 11920 10051 704 414 -167 A N1+ ATOM 1232 N GLU A 152 -23.076 -16.627 26.810 1.00 31.80 A N ANISOU 1232 N GLU A 152 3997 4515 3572 181 473 362 A N ATOM 1233 CA GLU A 152 -22.972 -17.937 26.179 1.00 40.69 A C ANISOU 1233 CA GLU A 152 5254 5516 4691 47 464 487 A C ATOM 1234 C GLU A 152 -22.150 -17.869 24.896 1.00 26.34 A C ANISOU 1234 C GLU A 152 3397 3528 3082 84 403 454 A C ATOM 1235 O GLU A 152 -21.338 -18.751 24.622 1.00 24.77 A O ANISOU 1235 O GLU A 152 3321 3177 2914 76 323 484 A O ATOM 1236 CB GLU A 152 -24.363 -18.506 25.895 1.00 52.03 A C ANISOU 1236 CB GLU A 152 6656 7091 6021 -145 588 578 A C ATOM 1237 CG GLU A 152 -25.155 -18.840 27.148 1.00 72.00 A C ANISOU 1237 CG GLU A 152 9247 9804 8307 -241 658 623 A C ATOM 1238 CD GLU A 152 -24.482 -19.902 27.993 1.00 89.09 A C ANISOU 1238 CD GLU A 152 11671 11841 10338 -275 587 728 A C ATOM 1239 OE1 GLU A 152 -24.597 -19.837 29.235 1.00 92.70 A O ANISOU 1239 OE1 GLU A 152 12190 12420 10613 -264 593 733 A O ATOM 1240 OE2 GLU A 152 -23.832 -20.799 27.416 1.00 96.92 A O1- ANISOU 1240 OE2 GLU A 152 12808 12615 11402 -301 514 798 A O1- ATOM 1241 N VAL A 153 -22.361 -16.817 24.112 1.00 30.94 A N ANISOU 1241 N VAL A 153 3815 4143 3798 128 434 387 A N ATOM 1242 CA VAL A 153 -21.586 -16.610 22.895 1.00 19.29 A C ANISOU 1242 CA VAL A 153 2291 2535 2502 146 387 352 A C ATOM 1243 C VAL A 153 -20.120 -16.363 23.236 1.00 24.29 A C ANISOU 1243 C VAL A 153 2976 3050 3202 262 278 248 A C ATOM 1244 O VAL A 153 -19.221 -16.863 22.560 1.00 22.83 A O ANISOU 1244 O VAL A 153 2820 2756 3100 253 212 224 A O ATOM 1245 CB VAL A 153 -22.116 -15.420 22.076 1.00 18.69 A C ANISOU 1245 CB VAL A 153 2059 2509 2533 175 435 313 A C ATOM 1246 CG1 VAL A 153 -21.205 -15.145 20.888 1.00 17.62 A C ANISOU 1246 CG1 VAL A 153 1888 2245 2560 174 388 281 A C ATOM 1247 CG2 VAL A 153 -23.540 -15.687 21.608 1.00 21.02 A C ANISOU 1247 CG2 VAL A 153 2277 2948 2762 76 532 387 A C ATOM 1248 N LEU A 154 -19.889 -15.593 24.293 1.00 21.96 A N ANISOU 1248 N LEU A 154 2674 2803 2865 374 260 162 A N ATOM 1249 CA LEU A 154 -18.536 -15.279 24.735 1.00 22.50 A C ANISOU 1249 CA LEU A 154 2770 2798 2982 489 164 31 A C ATOM 1250 C LEU A 154 -17.778 -16.541 25.124 1.00 22.66 A C ANISOU 1250 C LEU A 154 2940 2749 2921 508 70 54 A C ATOM 1251 O LEU A 154 -16.626 -16.728 24.734 1.00 30.41 A O ANISOU 1251 O LEU A 154 3927 3644 3981 558 -19 -40 A O ATOM 1252 CB LEU A 154 -18.571 -14.311 25.919 1.00 22.51 A C ANISOU 1252 CB LEU A 154 2734 2889 2931 602 168 -69 A C ATOM 1253 CG LEU A 154 -17.216 -13.943 26.526 1.00 24.95 A C ANISOU 1253 CG LEU A 154 3053 3156 3270 724 75 -231 A C ATOM 1254 CD1 LEU A 154 -16.385 -13.136 25.541 1.00 27.25 A C ANISOU 1254 CD1 LEU A 154 3257 3350 3748 713 60 -344 A C ATOM 1255 CD2 LEU A 154 -17.398 -13.177 27.825 1.00 35.14 A C ANISOU 1255 CD2 LEU A 154 4312 4563 4478 830 83 -323 A C ATOM 1256 N LEU A 155 -18.433 -17.405 25.892 1.00 21.18 A N ANISOU 1256 N LEU A 155 2878 2604 2566 467 85 172 A N ATOM 1257 CA LEU A 155 -17.814 -18.646 26.350 1.00 28.17 A C ANISOU 1257 CA LEU A 155 3955 3396 3353 496 -19 219 A C ATOM 1258 C LEU A 155 -17.474 -19.577 25.189 1.00 21.53 A C ANISOU 1258 C LEU A 155 3155 2419 2608 430 -67 252 A C ATOM 1259 O LEU A 155 -16.429 -20.227 25.193 1.00 21.89 A O ANISOU 1259 O LEU A 155 3293 2359 2665 522 -198 190 A O ATOM 1260 CB LEU A 155 -18.721 -19.359 27.355 1.00 32.24 A C ANISOU 1260 CB LEU A 155 4620 3978 3653 421 25 367 A C ATOM 1261 CG LEU A 155 -18.877 -18.669 28.712 1.00 32.96 A C ANISOU 1261 CG LEU A 155 4695 4221 3605 505 42 320 A C ATOM 1262 CD1 LEU A 155 -19.918 -19.379 29.564 1.00 29.57 A C ANISOU 1262 CD1 LEU A 155 4398 3892 2945 376 112 478 A C ATOM 1263 CD2 LEU A 155 -17.540 -18.594 29.439 1.00 28.57 A C ANISOU 1263 CD2 LEU A 155 4201 3621 3031 699 -98 197 A C ATOM 1264 N LYS A 156 -18.360 -19.639 24.201 1.00 20.79 A N ANISOU 1264 N LYS A 156 2981 2343 2577 285 32 331 A N ATOM 1265 CA LYS A 156 -18.123 -20.447 23.009 1.00 27.87 A C ANISOU 1265 CA LYS A 156 3881 3135 3572 213 -1 347 A C ATOM 1266 C LYS A 156 -16.917 -19.933 22.227 1.00 21.43 A C ANISOU 1266 C LYS A 156 2947 2283 2913 296 -76 185 A C ATOM 1267 O LYS A 156 -16.060 -20.710 21.809 1.00 20.01 A O ANISOU 1267 O LYS A 156 2815 2012 2776 334 -185 121 A O ATOM 1268 CB LYS A 156 -19.363 -20.460 22.111 1.00 45.99 A C ANISOU 1268 CB LYS A 156 6078 5500 5896 47 131 444 A C ATOM 1269 CG LYS A 156 -20.411 -21.501 22.486 1.00 59.55 A C ANISOU 1269 CG LYS A 156 7928 7226 7472 -99 194 592 A C ATOM 1270 CD LYS A 156 -20.177 -22.824 21.760 1.00 66.53 A C ANISOU 1270 CD LYS A 156 8922 7961 8395 -178 134 633 A C ATOM 1271 CE LYS A 156 -19.057 -23.634 22.393 1.00 76.60 A C ANISOU 1271 CE LYS A 156 10406 9067 9633 -55 -32 608 A C ATOM 1272 NZ LYS A 156 -19.433 -24.147 23.743 1.00 78.59 A N1+ ANISOU 1272 NZ LYS A 156 10879 9298 9683 -75 -36 725 A N1+ ATOM 1273 N VAL A 157 -16.858 -18.619 22.034 1.00 24.55 A N ANISOU 1273 N VAL A 157 3190 2751 3386 318 -21 108 A N ATOM 1274 CA VAL A 157 -15.754 -17.998 21.311 1.00 17.80 A C ANISOU 1274 CA VAL A 157 2220 1880 2663 354 -69 -46 A C ATOM 1275 C VAL A 157 -14.430 -18.233 22.025 1.00 19.85 A C ANISOU 1275 C VAL A 157 2536 2109 2896 497 -202 -201 A C ATOM 1276 O VAL A 157 -13.423 -18.556 21.396 1.00 18.39 A O ANISOU 1276 O VAL A 157 2308 1901 2778 519 -286 -328 A O ATOM 1277 CB VAL A 157 -15.962 -16.482 21.148 1.00 17.59 A C ANISOU 1277 CB VAL A 157 2066 1908 2710 346 13 -89 A C ATOM 1278 CG1 VAL A 157 -14.725 -15.841 20.539 1.00 16.96 A C ANISOU 1278 CG1 VAL A 157 1892 1810 2742 352 -31 -255 A C ATOM 1279 CG2 VAL A 157 -17.192 -16.199 20.299 1.00 16.73 A C ANISOU 1279 CG2 VAL A 157 1888 1838 2631 236 122 39 A C ATOM 1280 N LEU A 158 -14.436 -18.064 23.343 1.00 24.26 A N ANISOU 1280 N LEU A 158 4040 3217 1963 604 98 332 A N ATOM 1281 CA LEU A 158 -13.232 -18.261 24.140 1.00 28.86 A C ANISOU 1281 CA LEU A 158 4672 3722 2570 760 107 356 A C ATOM 1282 C LEU A 158 -12.778 -19.714 24.121 1.00 25.27 A C ANISOU 1282 C LEU A 158 4473 3070 2058 728 134 435 A C ATOM 1283 O LEU A 158 -11.585 -20.001 24.202 1.00 25.23 A O ANISOU 1283 O LEU A 158 4556 2947 2085 888 138 436 A O ATOM 1284 CB LEU A 158 -13.457 -17.795 25.579 1.00 29.58 A C ANISOU 1284 CB LEU A 158 4614 4002 2623 800 94 364 A C ATOM 1285 CG LEU A 158 -13.081 -16.343 25.877 1.00 31.87 A C ANISOU 1285 CG LEU A 158 4690 4421 2998 949 73 274 A C ATOM 1286 CD1 LEU A 158 -13.652 -15.403 24.829 1.00 24.98 A C ANISOU 1286 CD1 LEU A 158 3730 3583 2180 925 55 205 A C ATOM 1287 CD2 LEU A 158 -13.540 -15.948 27.272 1.00 39.92 A C ANISOU 1287 CD2 LEU A 158 5553 5648 3964 957 59 276 A C ATOM 1288 N LYS A 159 -13.732 -20.631 24.013 1.00 26.42 A N ANISOU 1288 N LYS A 159 4744 3184 2110 523 155 491 A N ATOM 1289 CA LYS A 159 -13.395 -22.046 23.975 1.00 31.29 A C ANISOU 1289 CA LYS A 159 5645 3582 2661 477 186 569 A C ATOM 1290 C LYS A 159 -12.749 -22.404 22.641 1.00 27.48 A C ANISOU 1290 C LYS A 159 5294 2902 2243 521 193 532 A C ATOM 1291 O LYS A 159 -11.784 -23.165 22.596 1.00 42.48 A O ANISOU 1291 O LYS A 159 7382 4616 4141 640 200 559 A O ATOM 1292 CB LYS A 159 -14.630 -22.914 24.228 1.00 36.50 A C ANISOU 1292 CB LYS A 159 6415 4262 3190 206 219 629 A C ATOM 1293 CG LYS A 159 -14.295 -24.301 24.757 1.00 46.30 A C ANISOU 1293 CG LYS A 159 7967 5293 4333 172 254 734 A C ATOM 1294 CD LYS A 159 -15.541 -25.053 25.193 1.00 60.94 A C ANISOU 1294 CD LYS A 159 9921 7194 6041 -127 300 790 A C ATOM 1295 CE LYS A 159 -16.276 -25.641 24.002 1.00 69.13 A C ANISOU 1295 CE LYS A 159 11067 8148 7051 -359 337 755 A C ATOM 1296 NZ LYS A 159 -15.526 -26.781 23.405 1.00 70.55 A N1+ ANISOU 1296 NZ LYS A 159 11577 7998 7228 -323 365 796 A N1+ ATOM 1297 N ARG A 160 -13.277 -21.840 21.559 1.00 26.73 A N ANISOU 1297 N ARG A 160 5099 2862 2197 440 187 467 A N ATOM 1298 CA ARG A 160 -12.732 -22.081 20.227 1.00 26.44 A C ANISOU 1298 CA ARG A 160 5162 2666 2218 468 194 424 A C ATOM 1299 C ARG A 160 -11.345 -21.469 20.073 1.00 30.75 A C ANISOU 1299 C ARG A 160 5651 3171 2860 707 179 370 A C ATOM 1300 O ARG A 160 -10.476 -22.034 19.408 1.00 32.86 A O ANISOU 1300 O ARG A 160 6057 3276 3151 786 188 350 A O ATOM 1301 CB ARG A 160 -13.667 -21.523 19.155 1.00 25.97 A C ANISOU 1301 CB ARG A 160 4989 2706 2172 334 187 368 A C ATOM 1302 CG ARG A 160 -14.978 -22.272 19.029 1.00 27.22 A C ANISOU 1302 CG ARG A 160 5211 2909 2222 75 211 391 A C ATOM 1303 CD ARG A 160 -14.731 -23.760 18.847 1.00 59.67 A C ANISOU 1303 CD ARG A 160 9614 6782 6275 -20 254 442 A C ATOM 1304 NE ARG A 160 -13.926 -24.042 17.662 1.00 63.52 A N ANISOU 1304 NE ARG A 160 10214 7090 6829 58 258 401 A N ATOM 1305 CZ ARG A 160 -13.501 -25.253 17.319 1.00 69.92 A C ANISOU 1305 CZ ARG A 160 11289 7668 7611 29 289 425 A C ATOM 1306 NH1 ARG A 160 -13.802 -26.302 18.073 1.00 71.85 A N1+ ANISOU 1306 NH1 ARG A 160 11739 7806 7756 -82 323 500 A N1+ ATOM 1307 NH2 ARG A 160 -12.773 -25.418 16.224 1.00 72.26 A N ANISOU 1307 NH2 ARG A 160 11657 7832 7967 110 289 372 A N ATOM 1308 N ILE A 161 -11.144 -20.308 20.687 1.00 34.03 A N ANISOU 1308 N ILE A 161 5860 3748 3323 813 159 333 A N ATOM 1309 CA ILE A 161 -9.849 -19.641 20.644 1.00 23.62 A C ANISOU 1309 CA ILE A 161 4467 2425 2081 1011 155 265 A C ATOM 1310 C ILE A 161 -8.796 -20.458 21.384 1.00 29.36 A C ANISOU 1310 C ILE A 161 5314 3069 2774 1163 158 291 A C ATOM 1311 O ILE A 161 -7.720 -20.732 20.853 1.00 34.32 A O ANISOU 1311 O ILE A 161 6012 3601 3428 1287 163 242 A O ATOM 1312 CB ILE A 161 -9.915 -18.233 21.258 1.00 29.32 A C ANISOU 1312 CB ILE A 161 4957 3335 2850 1074 141 215 A C ATOM 1313 CG1 ILE A 161 -10.816 -17.326 20.417 1.00 25.92 A C ANISOU 1313 CG1 ILE A 161 4423 2974 2450 978 130 179 A C ATOM 1314 CG2 ILE A 161 -8.522 -17.636 21.375 1.00 22.10 A C ANISOU 1314 CG2 ILE A 161 3972 2429 1994 1254 151 135 A C ATOM 1315 CD1 ILE A 161 -10.954 -15.922 20.969 1.00 21.88 A C ANISOU 1315 CD1 ILE A 161 3713 2621 1978 1045 115 127 A C ATOM 1316 N SER A 162 -9.114 -20.849 22.613 1.00 25.98 A N ANISOU 1316 N SER A 162 4908 2692 2273 1162 152 364 A N ATOM 1317 CA SER A 162 -8.184 -21.611 23.436 1.00 26.12 A C ANISOU 1317 CA SER A 162 5046 2645 2234 1329 147 400 A C ATOM 1318 C SER A 162 -7.791 -22.924 22.767 1.00 29.81 A C ANISOU 1318 C SER A 162 5790 2876 2661 1347 156 433 A C ATOM 1319 O SER A 162 -6.633 -23.336 22.822 1.00 34.96 A O ANISOU 1319 O SER A 162 6522 3460 3303 1550 145 404 A O ATOM 1320 CB SER A 162 -8.780 -21.877 24.821 1.00 35.15 A C ANISOU 1320 CB SER A 162 6194 3874 3287 1290 142 492 A C ATOM 1321 OG SER A 162 -10.011 -22.571 24.726 1.00 49.91 A O ANISOU 1321 OG SER A 162 8192 5686 5085 1056 161 572 A O ATOM 1322 N GLU A 163 -8.759 -23.574 22.130 1.00 27.86 A N ANISOU 1322 N GLU A 163 5686 2517 2383 1137 176 481 A N ATOM 1323 CA GLU A 163 -8.508 -24.842 21.455 1.00 29.14 A C ANISOU 1323 CA GLU A 163 6131 2437 2503 1127 191 507 A C ATOM 1324 C GLU A 163 -7.666 -24.660 20.197 1.00 28.47 A C ANISOU 1324 C GLU A 163 6028 2288 2499 1223 187 404 A C ATOM 1325 O GLU A 163 -6.751 -25.439 19.938 1.00 32.22 A O ANISOU 1325 O GLU A 163 6672 2615 2954 1374 182 386 A O ATOM 1326 CB GLU A 163 -9.823 -25.544 21.115 1.00 61.12 A C ANISOU 1326 CB GLU A 163 10326 6407 6491 842 224 569 A C ATOM 1327 CG GLU A 163 -10.572 -26.065 22.328 1.00 68.74 A C ANISOU 1327 CG GLU A 163 11385 7391 7341 726 239 677 A C ATOM 1328 CD GLU A 163 -11.797 -26.873 21.951 1.00 83.45 A C ANISOU 1328 CD GLU A 163 13412 9172 9122 420 285 721 A C ATOM 1329 OE1 GLU A 163 -12.137 -26.918 20.749 1.00 86.54 A O ANISOU 1329 OE1 GLU A 163 13807 9522 9553 301 300 661 A O ATOM 1330 OE2 GLU A 163 -12.420 -27.464 22.858 1.00 91.61 A O1- ANISOU 1330 OE2 GLU A 163 14569 10195 10042 286 312 809 A O1- ATOM 1331 N ASN A 164 -7.982 -23.633 19.415 1.00 27.04 A N ANISOU 1331 N ASN A 164 5652 2224 2400 1141 190 335 A N ATOM 1332 CA ASN A 164 -7.242 -23.365 18.187 1.00 26.42 A C ANISOU 1332 CA ASN A 164 5545 2103 2390 1203 193 237 A C ATOM 1333 C ASN A 164 -5.804 -22.926 18.449 1.00 33.29 A C ANISOU 1333 C ASN A 164 6319 3037 3291 1446 181 154 A C ATOM 1334 O ASN A 164 -4.892 -23.295 17.709 1.00 35.09 A O ANISOU 1334 O ASN A 164 6616 3187 3530 1551 183 82 A O ATOM 1335 CB ASN A 164 -7.973 -22.331 17.326 1.00 28.57 A C ANISOU 1335 CB ASN A 164 5649 2483 2723 1058 199 194 A C ATOM 1336 CG ASN A 164 -9.165 -22.921 16.594 1.00 26.96 A C ANISOU 1336 CG ASN A 164 5550 2213 2482 833 212 233 A C ATOM 1337 ND2 ASN A 164 -9.266 -24.244 16.599 1.00 28.56 A N ANISOU 1337 ND2 ASN A 164 5990 2242 2618 779 228 281 A N ATOM 1338 OD1 ASN A 164 -9.985 -22.197 16.029 1.00 32.34 A O ANISOU 1338 OD1 ASN A 164 6105 3000 3182 713 209 213 A O ATOM 1339 N LEU A 165 -5.604 -22.147 19.507 1.00 25.59 A N ANISOU 1339 N LEU A 165 5176 2224 2322 1529 171 149 A N ATOM 1340 CA LEU A 165 -4.272 -21.659 19.853 1.00 34.24 A C ANISOU 1340 CA LEU A 165 6151 3426 3434 1742 166 53 A C ATOM 1341 C LEU A 165 -3.387 -22.777 20.394 1.00 37.14 A C ANISOU 1341 C LEU A 165 6681 3711 3721 1947 145 66 A C ATOM 1342 O LEU A 165 -2.194 -22.834 20.097 1.00 35.29 A O ANISOU 1342 O LEU A 165 6422 3505 3483 2123 140 -37 A O ATOM 1343 CB LEU A 165 -4.357 -20.519 20.869 1.00 24.58 A C ANISOU 1343 CB LEU A 165 4704 2404 2232 1762 165 37 A C ATOM 1344 CG LEU A 165 -4.993 -19.220 20.371 1.00 26.68 A C ANISOU 1344 CG LEU A 165 4799 2763 2575 1620 181 -2 A C ATOM 1345 CD1 LEU A 165 -4.964 -18.160 21.461 1.00 31.17 A C ANISOU 1345 CD1 LEU A 165 5167 3517 3160 1665 180 -30 A C ATOM 1346 CD2 LEU A 165 -4.289 -18.724 19.116 1.00 22.69 A C ANISOU 1346 CD2 LEU A 165 4261 2235 2127 1622 205 -108 A C ATOM 1347 N LYS A 166 -3.976 -23.662 21.191 1.00 43.25 A N ANISOU 1347 N LYS A 166 7628 4391 4416 1927 133 189 A N ATOM 1348 CA LYS A 166 -3.247 -24.801 21.733 1.00 50.41 A C ANISOU 1348 CA LYS A 166 8742 5185 5226 2133 108 225 A C ATOM 1349 C LYS A 166 -2.774 -25.706 20.605 1.00 50.10 A C ANISOU 1349 C LYS A 166 8904 4952 5180 2183 108 182 A C ATOM 1350 O LYS A 166 -1.678 -26.261 20.660 1.00 54.24 A O ANISOU 1350 O LYS A 166 9508 5446 5653 2429 82 126 A O ATOM 1351 CB LYS A 166 -4.125 -25.590 22.706 1.00 64.77 A C ANISOU 1351 CB LYS A 166 10751 6908 6951 2052 107 380 A C ATOM 1352 CG LYS A 166 -3.429 -26.782 23.344 1.00 76.61 A C ANISOU 1352 CG LYS A 166 12509 8267 8332 2277 79 438 A C ATOM 1353 CD LYS A 166 -4.337 -27.481 24.344 1.00 81.69 A C ANISOU 1353 CD LYS A 166 13351 8817 8870 2165 88 600 A C ATOM 1354 CE LYS A 166 -3.631 -28.647 25.015 1.00 85.23 A C ANISOU 1354 CE LYS A 166 14092 9108 9185 2411 58 671 A C ATOM 1355 NZ LYS A 166 -4.505 -29.314 26.019 1.00 86.70 A N1+ ANISOU 1355 NZ LYS A 166 14492 9197 9252 2283 75 837 A N1+ ATOM 1356 N LYS A 167 -3.607 -25.850 19.581 1.00 30.20 A N ANISOU 1356 N LYS A 167 6455 2318 2704 1958 135 198 A N ATOM 1357 CA LYS A 167 -3.264 -26.671 18.430 1.00 46.93 A C ANISOU 1357 CA LYS A 167 8755 4256 4822 1975 140 149 A C ATOM 1358 C LYS A 167 -2.319 -25.921 17.499 1.00 44.43 A C ANISOU 1358 C LYS A 167 8246 4059 4576 2061 142 -5 A C ATOM 1359 O LYS A 167 -1.680 -26.516 16.632 1.00 41.76 A O ANISOU 1359 O LYS A 167 8015 3622 4230 2146 138 -80 A O ATOM 1360 CB LYS A 167 -4.524 -27.091 17.675 1.00 49.94 A C ANISOU 1360 CB LYS A 167 9268 4496 5212 1688 172 212 A C ATOM 1361 CG LYS A 167 -4.283 -28.171 16.639 1.00 64.40 A C ANISOU 1361 CG LYS A 167 11342 6104 7023 1693 180 178 A C ATOM 1362 CD LYS A 167 -5.590 -28.711 16.088 1.00 73.32 A C ANISOU 1362 CD LYS A 167 12620 7101 8137 1394 218 243 A C ATOM 1363 CE LYS A 167 -6.386 -27.621 15.398 1.00 82.11 A C ANISOU 1363 CE LYS A 167 13485 8386 9326 1186 234 208 A C ATOM 1364 NZ LYS A 167 -7.645 -28.154 14.812 1.00 88.82 A N1+ ANISOU 1364 NZ LYS A 167 14454 9148 10145 900 269 247 A N1+ ATOM 1365 N PHE A 168 -2.234 -24.609 17.688 1.00 46.00 A N ANISOU 1365 N PHE A 168 8170 4472 4836 2031 151 -58 A N ATOM 1366 CA PHE A 168 -1.350 -23.774 16.887 1.00 48.69 A C ANISOU 1366 CA PHE A 168 8326 4942 5232 2079 166 -205 A C ATOM 1367 C PHE A 168 0.053 -23.753 17.485 1.00 52.49 A C ANISOU 1367 C PHE A 168 8721 5557 5666 2350 148 -310 A C ATOM 1368 O PHE A 168 1.029 -23.465 16.793 1.00 56.71 A O ANISOU 1368 O PHE A 168 9156 6181 6210 2430 159 -452 A O ATOM 1369 CB PHE A 168 -1.910 -22.352 16.786 1.00 40.30 A C ANISOU 1369 CB PHE A 168 7040 4026 4246 1914 192 -217 A C ATOM 1370 CG PHE A 168 -1.120 -21.452 15.882 1.00 51.07 A C ANISOU 1370 CG PHE A 168 8248 5497 5658 1912 221 -356 A C ATOM 1371 CD1 PHE A 168 -1.284 -21.513 14.510 1.00 57.79 A C ANISOU 1371 CD1 PHE A 168 9153 6267 6539 1795 240 -389 A C ATOM 1372 CD2 PHE A 168 -0.217 -20.542 16.404 1.00 67.90 A C ANISOU 1372 CD2 PHE A 168 10184 7821 7796 2012 236 -458 A C ATOM 1373 CE1 PHE A 168 -0.560 -20.686 13.674 1.00 67.16 A C ANISOU 1373 CE1 PHE A 168 10212 7550 7755 1776 273 -512 A C ATOM 1374 CE2 PHE A 168 0.510 -19.711 15.573 1.00 72.37 A C ANISOU 1374 CE2 PHE A 168 10622 8483 8391 1978 276 -591 A C ATOM 1375 CZ PHE A 168 0.338 -19.783 14.206 1.00 70.95 A C ANISOU 1375 CZ PHE A 168 10510 8212 8237 1859 294 -612 A C ATOM 1376 N LYS A 169 0.144 -24.066 18.773 1.00 46.60 A N ANISOU 1376 N LYS A 169 8005 4846 4855 2488 120 -246 A N ATOM 1377 CA LYS A 169 1.423 -24.079 19.472 1.00 52.23 A C ANISOU 1377 CA LYS A 169 8626 5718 5502 2764 95 -345 A C ATOM 1378 C LYS A 169 2.245 -25.311 19.110 1.00 55.58 A C ANISOU 1378 C LYS A 169 9252 6023 5845 2991 60 -390 A C ATOM 1379 O LYS A 169 3.271 -25.210 18.437 1.00 45.74 A O ANISOU 1379 O LYS A 169 7914 4876 4591 3110 61 -548 A O ATOM 1380 CB LYS A 169 1.205 -24.024 20.986 1.00 52.23 A C ANISOU 1380 CB LYS A 169 8597 5802 5446 2846 72 -255 A C ATOM 1381 CG LYS A 169 0.706 -22.684 21.493 1.00 56.43 A C ANISOU 1381 CG LYS A 169 8882 6513 6048 2691 101 -258 A C ATOM 1382 CD LYS A 169 0.425 -22.728 22.989 1.00 70.34 A C ANISOU 1382 CD LYS A 169 10625 8354 7746 2764 78 -165 A C ATOM 1383 CE LYS A 169 1.664 -23.126 23.774 1.00 79.79 A C ANISOU 1383 CE LYS A 169 11797 9681 8838 3077 42 -236 A C ATOM 1384 NZ LYS A 169 1.393 -23.190 25.238 1.00 80.47 A N1+ ANISOU 1384 NZ LYS A 169 11873 9852 8851 3153 18 -140 A N1+ ATOM 1385 N GLU A 170 1.785 -26.473 19.561 1.00 59.64 A N ANISOU 1385 N GLU A 170 10050 6322 6287 3048 31 -256 A N ATOM 1386 CA GLU A 170 2.519 -27.718 19.362 1.00 68.19 A C ANISOU 1386 CA GLU A 170 11373 7260 7278 3297 -10 -283 A C ATOM 1387 C GLU A 170 2.533 -28.174 17.903 1.00 57.98 A C ANISOU 1387 C GLU A 170 10192 5812 6026 3213 7 -350 A C ATOM 1388 O GLU A 170 3.339 -29.019 17.518 1.00 54.35 A O ANISOU 1388 O GLU A 170 9874 5276 5501 3436 -25 -428 A O ATOM 1389 CB GLU A 170 1.967 -28.815 20.277 1.00 75.92 A C ANISOU 1389 CB GLU A 170 12666 8020 8158 3360 -37 -108 A C ATOM 1390 CG GLU A 170 0.450 -28.894 20.319 1.00 78.15 A C ANISOU 1390 CG GLU A 170 13072 8139 8483 3027 3 54 A C ATOM 1391 CD GLU A 170 -0.120 -29.726 19.190 1.00 91.34 A C ANISOU 1391 CD GLU A 170 14991 9542 10173 2864 28 78 A C ATOM 1392 OE1 GLU A 170 0.580 -30.649 18.723 1.00 98.78 A O ANISOU 1392 OE1 GLU A 170 16135 10336 11060 3057 2 25 A O ATOM 1393 OE2 GLU A 170 -1.268 -29.463 18.775 1.00 93.97 A O1- ANISOU 1393 OE2 GLU A 170 15311 9824 10568 2551 70 140 A O1- ATOM 1394 N LYS A 171 1.645 -27.606 17.094 1.00 57.81 A N ANISOU 1394 N LYS A 171 10102 5758 6106 2907 53 -327 A N ATOM 1395 CA LYS A 171 1.614 -27.910 15.667 1.00 57.34 A C ANISOU 1395 CA LYS A 171 10115 5585 6089 2804 73 -395 A C ATOM 1396 C LYS A 171 1.974 -26.684 14.835 1.00 61.02 A C ANISOU 1396 C LYS A 171 10288 6261 6635 2696 108 -527 A C ATOM 1397 O LYS A 171 2.870 -25.921 15.197 1.00 71.35 A O ANISOU 1397 O LYS A 171 11372 7803 7936 2819 108 -636 A O ATOM 1398 CB LYS A 171 0.244 -28.453 15.256 1.00 51.57 A C ANISOU 1398 CB LYS A 171 9593 4619 5383 2534 100 -261 A C ATOM 1399 CG LYS A 171 -0.065 -29.824 15.830 1.00 57.70 A C ANISOU 1399 CG LYS A 171 10722 5136 6065 2609 80 -145 A C ATOM 1400 CD LYS A 171 -1.490 -30.256 15.533 1.00 63.08 A C ANISOU 1400 CD LYS A 171 11580 5627 6760 2294 120 -24 A C ATOM 1401 CE LYS A 171 -1.791 -31.607 16.163 1.00 69.98 A C ANISOU 1401 CE LYS A 171 12835 6229 7527 2340 114 94 A C ATOM 1402 NZ LYS A 171 -3.199 -32.029 15.933 1.00 72.92 A N1+ ANISOU 1402 NZ LYS A 171 13370 6441 7894 1998 165 198 A N1+ ATOM 1403 N SER A 172 1.275 -26.496 13.721 1.00 57.34 A N ANISOU 1403 N SER A 172 9835 5716 6236 2457 142 -519 A N ATOM 1404 CA SER A 172 1.563 -25.376 12.832 1.00 63.20 A C ANISOU 1404 CA SER A 172 10347 6624 7042 2341 179 -630 A C ATOM 1405 C SER A 172 0.298 -24.763 12.245 1.00 57.14 A C ANISOU 1405 C SER A 172 9551 5811 6347 2045 211 -544 A C ATOM 1406 O SER A 172 -0.816 -25.155 12.592 1.00 45.65 A O ANISOU 1406 O SER A 172 8222 4232 4892 1920 206 -411 A O ATOM 1407 CB SER A 172 2.498 -25.814 11.703 1.00 71.97 A C ANISOU 1407 CB SER A 172 11479 7736 8130 2434 181 -781 A C ATOM 1408 OG SER A 172 1.911 -26.836 10.917 1.00 76.43 A O ANISOU 1408 OG SER A 172 12279 8068 8691 2356 177 -734 A O ATOM 1409 N PHE A 173 0.487 -23.796 11.352 1.00 53.52 A N ANISOU 1409 N PHE A 173 8932 5469 5936 1934 245 -627 A N ATOM 1410 CA PHE A 173 -0.621 -23.121 10.690 1.00 39.25 A C ANISOU 1410 CA PHE A 173 7088 3642 4183 1688 269 -562 A C ATOM 1411 C PHE A 173 -1.235 -24.014 9.617 1.00 42.88 A C ANISOU 1411 C PHE A 173 7723 3934 4636 1572 270 -537 A C ATOM 1412 O PHE A 173 -2.315 -23.729 9.100 1.00 36.94 A O ANISOU 1412 O PHE A 173 6975 3153 3908 1375 281 -472 A O ATOM 1413 CB PHE A 173 -0.141 -21.807 10.069 1.00 43.17 A C ANISOU 1413 CB PHE A 173 7388 4300 4714 1621 307 -656 A C ATOM 1414 CG PHE A 173 -1.241 -20.979 9.473 1.00 42.64 A C ANISOU 1414 CG PHE A 173 7284 4228 4690 1408 324 -586 A C ATOM 1415 CD1 PHE A 173 -1.445 -20.952 8.103 1.00 40.50 A C ANISOU 1415 CD1 PHE A 173 7048 3916 4423 1287 342 -616 A C ATOM 1416 CD2 PHE A 173 -2.072 -20.226 10.284 1.00 44.24 A C ANISOU 1416 CD2 PHE A 173 7414 4478 4919 1345 317 -496 A C ATOM 1417 CE1 PHE A 173 -2.457 -20.188 7.556 1.00 34.72 A C ANISOU 1417 CE1 PHE A 173 6286 3193 3713 1120 349 -552 A C ATOM 1418 CE2 PHE A 173 -3.084 -19.462 9.743 1.00 38.85 A C ANISOU 1418 CE2 PHE A 173 6698 3804 4260 1185 322 -440 A C ATOM 1419 CZ PHE A 173 -3.277 -19.443 8.377 1.00 32.82 A C ANISOU 1419 CZ PHE A 173 5977 3000 3493 1079 337 -465 A C ATOM 1420 N LYS A 174 -0.539 -25.099 9.290 1.00 46.21 A N ANISOU 1420 N LYS A 174 8288 4255 5016 1705 256 -601 A N ATOM 1421 CA LYS A 174 -1.014 -26.054 8.294 1.00 46.51 A C ANISOU 1421 CA LYS A 174 8509 4120 5041 1608 261 -597 A C ATOM 1422 C LYS A 174 -2.358 -26.638 8.715 1.00 44.98 A C ANISOU 1422 C LYS A 174 8473 3781 4837 1452 259 -454 A C ATOM 1423 O LYS A 174 -3.165 -27.042 7.878 1.00 37.07 A O ANISOU 1423 O LYS A 174 7564 2687 3834 1274 275 -435 A O ATOM 1424 CB LYS A 174 0.007 -27.179 8.113 1.00 57.00 A C ANISOU 1424 CB LYS A 174 9988 5353 6317 1822 240 -691 A C ATOM 1425 CG LYS A 174 -0.262 -28.112 6.937 1.00 73.32 A C ANISOU 1425 CG LYS A 174 12231 7256 8371 1737 249 -727 A C ATOM 1426 CD LYS A 174 0.338 -27.578 5.641 1.00 82.49 A C ANISOU 1426 CD LYS A 174 13249 8543 9551 1697 271 -863 A C ATOM 1427 CE LYS A 174 -0.650 -26.721 4.868 1.00 84.43 A C ANISOU 1427 CE LYS A 174 13390 8848 9842 1430 303 -813 A C ATOM 1428 NZ LYS A 174 -1.730 -27.545 4.258 1.00 84.04 A N1+ ANISOU 1428 NZ LYS A 174 13517 8632 9784 1256 310 -755 A N1+ ATOM 1429 N GLU A 175 -2.592 -26.673 10.022 1.00 45.28 A N ANISOU 1429 N GLU A 175 8531 3819 4855 1509 243 -364 A N ATOM 1430 CA GLU A 175 -3.815 -27.238 10.576 1.00 36.86 A C ANISOU 1430 CA GLU A 175 7610 2635 3759 1355 247 -233 A C ATOM 1431 C GLU A 175 -5.035 -26.372 10.284 1.00 35.35 A C ANISOU 1431 C GLU A 175 7277 2553 3602 1113 264 -183 A C ATOM 1432 O GLU A 175 -6.171 -26.831 10.402 1.00 31.99 A O ANISOU 1432 O GLU A 175 6950 2062 3144 931 276 -105 A O ATOM 1433 CB GLU A 175 -3.666 -27.431 12.087 1.00 39.76 A C ANISOU 1433 CB GLU A 175 8021 3000 4085 1489 226 -154 A C ATOM 1434 CG GLU A 175 -2.635 -28.473 12.477 1.00 43.46 A C ANISOU 1434 CG GLU A 175 8683 3338 4491 1745 200 -182 A C ATOM 1435 CD GLU A 175 -3.063 -29.876 12.098 1.00 48.40 A C ANISOU 1435 CD GLU A 175 9636 3694 5062 1680 211 -142 A C ATOM 1436 OE1 GLU A 175 -2.260 -30.595 11.468 1.00 52.54 A O ANISOU 1436 OE1 GLU A 175 10292 4108 5564 1830 199 -230 A O ATOM 1437 OE2 GLU A 175 -4.208 -30.256 12.425 1.00 47.08 A O1- ANISOU 1437 OE2 GLU A 175 9595 3429 4865 1471 235 -34 A O1- ATOM 1438 N PHE A 176 -4.798 -25.122 9.900 1.00 34.52 A N ANISOU 1438 N PHE A 176 6947 2619 3550 1112 266 -235 A N ATOM 1439 CA PHE A 176 -5.887 -24.177 9.685 1.00 39.02 A C ANISOU 1439 CA PHE A 176 7378 3305 4144 933 272 -190 A C ATOM 1440 C PHE A 176 -5.940 -23.646 8.253 1.00 36.49 A C ANISOU 1440 C PHE A 176 6987 3031 3846 842 286 -257 A C ATOM 1441 O PHE A 176 -7.008 -23.287 7.759 1.00 29.42 A O ANISOU 1441 O PHE A 176 6048 2188 2943 682 286 -222 A O ATOM 1442 CB PHE A 176 -5.778 -23.013 10.672 1.00 32.41 A C ANISOU 1442 CB PHE A 176 6354 2625 3336 1004 261 -169 A C ATOM 1443 CG PHE A 176 -5.719 -23.443 12.109 1.00 33.04 A C ANISOU 1443 CG PHE A 176 6481 2688 3386 1097 246 -104 A C ATOM 1444 CD1 PHE A 176 -4.506 -23.545 12.765 1.00 25.79 A C ANISOU 1444 CD1 PHE A 176 5553 1784 2461 1310 237 -149 A C ATOM 1445 CD2 PHE A 176 -6.879 -23.746 12.801 1.00 38.92 A C ANISOU 1445 CD2 PHE A 176 7273 3422 4091 969 242 -4 A C ATOM 1446 CE1 PHE A 176 -4.450 -23.940 14.084 1.00 36.59 A C ANISOU 1446 CE1 PHE A 176 6969 3144 3788 1409 220 -84 A C ATOM 1447 CE2 PHE A 176 -6.829 -24.142 14.120 1.00 37.50 A C ANISOU 1447 CE2 PHE A 176 7146 3229 3871 1046 231 63 A C ATOM 1448 CZ PHE A 176 -5.614 -24.238 14.763 1.00 42.06 A C ANISOU 1448 CZ PHE A 176 7726 3809 4446 1273 218 29 A C ATOM 1449 N LYS A 177 -4.784 -23.604 7.596 1.00 43.15 A N ANISOU 1449 N LYS A 177 7817 3873 4704 951 296 -357 A N ATOM 1450 CA LYS A 177 -4.672 -23.034 6.254 1.00 41.31 A C ANISOU 1450 CA LYS A 177 7517 3695 4484 874 314 -423 A C ATOM 1451 C LYS A 177 -5.832 -23.419 5.340 1.00 42.18 A C ANISOU 1451 C LYS A 177 7694 3763 4569 685 316 -390 A C ATOM 1452 O LYS A 177 -6.468 -22.556 4.733 1.00 30.58 A O ANISOU 1452 O LYS A 177 6127 2391 3100 583 316 -375 A O ATOM 1453 CB LYS A 177 -3.347 -23.443 5.608 1.00 42.60 A C ANISOU 1453 CB LYS A 177 7710 3834 4641 994 326 -545 A C ATOM 1454 CG LYS A 177 -3.195 -22.973 4.171 1.00 42.29 A C ANISOU 1454 CG LYS A 177 7620 3848 4601 902 350 -617 A C ATOM 1455 CD LYS A 177 -1.943 -23.547 3.530 1.00 47.27 A C ANISOU 1455 CD LYS A 177 8284 4465 5212 1013 362 -750 A C ATOM 1456 CE LYS A 177 -1.826 -23.119 2.077 1.00 49.59 A C ANISOU 1456 CE LYS A 177 8532 4818 5493 903 389 -818 A C ATOM 1457 NZ LYS A 177 -3.001 -23.556 1.273 1.00 48.81 A N1+ ANISOU 1457 NZ LYS A 177 8519 4647 5380 738 384 -762 A N1+ ATOM 1458 N GLY A 178 -6.101 -24.716 5.244 1.00 40.48 A N ANISOU 1458 N GLY A 178 7656 3405 4321 643 318 -384 A N ATOM 1459 CA GLY A 178 -7.158 -25.216 4.383 1.00 35.11 A C ANISOU 1459 CA GLY A 178 7043 2692 3604 449 328 -374 A C ATOM 1460 C GLY A 178 -8.535 -24.696 4.751 1.00 38.12 A C ANISOU 1460 C GLY A 178 7339 3182 3963 301 319 -293 A C ATOM 1461 O GLY A 178 -9.296 -24.267 3.885 1.00 38.97 A O ANISOU 1461 O GLY A 178 7373 3387 4047 178 317 -301 A O ATOM 1462 N LYS A 179 -8.859 -24.736 6.039 1.00 45.17 A N ANISOU 1462 N LYS A 179 8236 4077 4850 322 309 -219 A N ATOM 1463 CA LYS A 179 -10.166 -24.293 6.509 1.00 46.73 A C ANISOU 1463 CA LYS A 179 8340 4400 5014 189 298 -154 A C ATOM 1464 C LYS A 179 -10.395 -22.814 6.214 1.00 32.33 A C ANISOU 1464 C LYS A 179 6314 2756 3215 219 275 -156 A C ATOM 1465 O LYS A 179 -11.471 -22.417 5.770 1.00 36.36 A O ANISOU 1465 O LYS A 179 6744 3388 3682 103 262 -146 A O ATOM 1466 CB LYS A 179 -10.319 -24.565 8.007 1.00 52.92 A C ANISOU 1466 CB LYS A 179 9160 5162 5785 222 294 -81 A C ATOM 1467 CG LYS A 179 -10.459 -26.038 8.350 1.00 68.10 A C ANISOU 1467 CG LYS A 179 11320 6902 7654 146 320 -56 A C ATOM 1468 CD LYS A 179 -10.687 -26.247 9.840 1.00 75.74 A C ANISOU 1468 CD LYS A 179 12326 7861 8591 165 317 29 A C ATOM 1469 CE LYS A 179 -9.476 -25.817 10.647 1.00 80.37 A C ANISOU 1469 CE LYS A 179 12868 8442 9229 416 294 34 A C ATOM 1470 NZ LYS A 179 -9.657 -26.095 12.099 1.00 82.35 A N1+ ANISOU 1470 NZ LYS A 179 13169 8682 9439 444 290 119 A N1+ ATOM 1471 N ILE A 180 -9.371 -22.006 6.464 1.00 30.75 A N ANISOU 1471 N ILE A 180 6040 2572 3071 377 271 -175 A N ATOM 1472 CA ILE A 180 -9.459 -20.562 6.277 1.00 28.83 A C ANISOU 1472 CA ILE A 180 5643 2462 2849 416 257 -175 A C ATOM 1473 C ILE A 180 -9.604 -20.185 4.807 1.00 31.13 A C ANISOU 1473 C ILE A 180 5923 2787 3120 354 261 -215 A C ATOM 1474 O ILE A 180 -10.415 -19.329 4.452 1.00 32.29 A O ANISOU 1474 O ILE A 180 5985 3046 3238 317 239 -192 A O ATOM 1475 CB ILE A 180 -8.222 -19.856 6.858 1.00 31.17 A C ANISOU 1475 CB ILE A 180 5881 2760 3202 573 268 -205 A C ATOM 1476 CG1 ILE A 180 -8.112 -20.142 8.358 1.00 29.15 A C ANISOU 1476 CG1 ILE A 180 5621 2498 2957 648 259 -162 A C ATOM 1477 CG2 ILE A 180 -8.285 -18.358 6.590 1.00 27.31 A C ANISOU 1477 CG2 ILE A 180 5274 2374 2729 595 264 -208 A C ATOM 1478 CD1 ILE A 180 -6.791 -19.734 8.966 1.00 30.84 A C ANISOU 1478 CD1 ILE A 180 5786 2721 3211 807 273 -212 A C ATOM 1479 N GLU A 181 -8.812 -20.829 3.959 1.00 23.60 A N ANISOU 1479 N GLU A 181 5055 1740 2170 357 285 -278 A N ATOM 1480 CA GLU A 181 -8.816 -20.536 2.532 1.00 28.07 A C ANISOU 1480 CA GLU A 181 5617 2339 2711 299 293 -322 A C ATOM 1481 C GLU A 181 -10.210 -20.686 1.931 1.00 39.24 A C ANISOU 1481 C GLU A 181 7019 3834 4059 159 273 -295 A C ATOM 1482 O GLU A 181 -10.639 -19.861 1.124 1.00 40.98 A O ANISOU 1482 O GLU A 181 7176 4152 4242 139 258 -291 A O ATOM 1483 CB GLU A 181 -7.830 -21.450 1.805 1.00 30.29 A C ANISOU 1483 CB GLU A 181 5998 2514 2998 315 321 -404 A C ATOM 1484 CG GLU A 181 -7.609 -21.092 0.348 1.00 42.51 A C ANISOU 1484 CG GLU A 181 7533 4102 4517 266 336 -459 A C ATOM 1485 CD GLU A 181 -6.603 -22.003 -0.324 1.00 49.55 A C ANISOU 1485 CD GLU A 181 8509 4906 5411 292 362 -557 A C ATOM 1486 OE1 GLU A 181 -6.010 -21.590 -1.342 1.00 50.43 A O ANISOU 1486 OE1 GLU A 181 8595 5062 5506 285 382 -618 A O ATOM 1487 OE2 GLU A 181 -6.400 -23.132 0.171 1.00 53.67 A O1- ANISOU 1487 OE2 GLU A 181 9134 5316 5943 325 362 -575 A O1- ATOM 1488 N SER A 182 -10.915 -21.739 2.333 1.00 27.15 A N ANISOU 1488 N SER A 182 5551 2267 2497 62 274 -281 A N ATOM 1489 CA SER A 182 -12.237 -22.030 1.790 1.00 26.59 A C ANISOU 1489 CA SER A 182 5458 2298 2346 -96 263 -281 A C ATOM 1490 C SER A 182 -13.309 -21.063 2.294 1.00 31.61 A C ANISOU 1490 C SER A 182 5951 3116 2943 -96 223 -230 A C ATOM 1491 O SER A 182 -14.392 -20.973 1.716 1.00 35.77 A O ANISOU 1491 O SER A 182 6413 3788 3389 -192 203 -243 A O ATOM 1492 CB SER A 182 -12.639 -23.473 2.105 1.00 26.72 A C ANISOU 1492 CB SER A 182 5606 2216 2331 -230 290 -292 A C ATOM 1493 OG SER A 182 -12.733 -23.683 3.502 1.00 50.60 A O ANISOU 1493 OG SER A 182 8652 5202 5370 -207 289 -235 A O ATOM 1494 N LYS A 183 -13.007 -20.343 3.370 1.00 29.63 A N ANISOU 1494 N LYS A 183 5643 2874 2742 20 209 -185 A N ATOM 1495 CA LYS A 183 -13.962 -19.399 3.941 1.00 32.93 A C ANISOU 1495 CA LYS A 183 5927 3461 3126 46 168 -146 A C ATOM 1496 C LYS A 183 -13.606 -17.952 3.611 1.00 29.22 A C ANISOU 1496 C LYS A 183 5390 3035 2678 184 145 -135 A C ATOM 1497 O LYS A 183 -14.297 -17.025 4.033 1.00 34.74 A O ANISOU 1497 O LYS A 183 5991 3859 3351 243 106 -108 A O ATOM 1498 CB LYS A 183 -14.054 -19.576 5.459 1.00 26.95 A C ANISOU 1498 CB LYS A 183 5149 2699 2393 66 167 -104 A C ATOM 1499 CG LYS A 183 -14.438 -20.978 5.900 1.00 42.29 A C ANISOU 1499 CG LYS A 183 7191 4579 4298 -81 195 -102 A C ATOM 1500 CD LYS A 183 -14.537 -21.067 7.415 1.00 44.81 A C ANISOU 1500 CD LYS A 183 7494 4905 4628 -57 194 -50 A C ATOM 1501 CE LYS A 183 -15.662 -20.197 7.945 1.00 41.31 A C ANISOU 1501 CE LYS A 183 6877 4687 4133 -67 154 -36 A C ATOM 1502 NZ LYS A 183 -16.979 -20.602 7.379 1.00 53.82 A N1+ ANISOU 1502 NZ LYS A 183 8415 6428 5605 -246 149 -72 A N1+ ATOM 1503 N MET A 184 -12.527 -17.763 2.860 1.00 28.81 A N ANISOU 1503 N MET A 184 5402 2878 2666 231 173 -163 A N ATOM 1504 CA MET A 184 -12.070 -16.422 2.510 1.00 31.53 A C ANISOU 1504 CA MET A 184 5722 3234 3023 334 169 -154 A C ATOM 1505 C MET A 184 -13.103 -15.656 1.692 1.00 37.20 A C ANISOU 1505 C MET A 184 6398 4083 3652 337 125 -135 A C ATOM 1506 O MET A 184 -13.618 -16.156 0.693 1.00 44.34 A O ANISOU 1506 O MET A 184 7317 5040 4490 255 117 -157 A O ATOM 1507 CB MET A 184 -10.743 -16.477 1.753 1.00 29.67 A C ANISOU 1507 CB MET A 184 5564 2885 2825 346 217 -202 A C ATOM 1508 CG MET A 184 -9.528 -16.687 2.640 1.00 28.25 A C ANISOU 1508 CG MET A 184 5399 2612 2724 412 253 -230 A C ATOM 1509 SD MET A 184 -7.993 -16.242 1.804 1.00 64.35 A S ANISOU 1509 SD MET A 184 10012 7122 7316 440 309 -304 A S ATOM 1510 CE MET A 184 -8.009 -17.399 0.437 1.00130.09 A C ANISOU 1510 CE MET A 184 18415 15416 15599 344 318 -354 A C ATOM 1511 N LEU A 185 -13.397 -14.436 2.126 1.00 35.35 A N ANISOU 1511 N LEU A 185 6116 3904 3411 445 95 -100 A N ATOM 1512 CA LEU A 185 -14.327 -13.572 1.415 1.00 29.95 A C ANISOU 1512 CA LEU A 185 5407 3340 2632 499 44 -79 A C ATOM 1513 C LEU A 185 -13.714 -13.123 0.092 1.00 23.77 A C ANISOU 1513 C LEU A 185 4723 2488 1819 505 66 -82 A C ATOM 1514 O LEU A 185 -12.505 -12.913 0.001 1.00 23.30 A O ANISOU 1514 O LEU A 185 4736 2295 1822 506 121 -95 A O ATOM 1515 CB LEU A 185 -14.683 -12.358 2.274 1.00 29.01 A C ANISOU 1515 CB LEU A 185 5239 3267 2515 636 7 -45 A C ATOM 1516 CG LEU A 185 -15.857 -11.490 1.817 1.00 35.82 A C ANISOU 1516 CG LEU A 185 6064 4282 3263 736 -66 -25 A C ATOM 1517 CD1 LEU A 185 -17.133 -12.311 1.725 1.00 41.21 A C ANISOU 1517 CD1 LEU A 185 6632 5171 3856 661 -111 -54 A C ATOM 1518 CD2 LEU A 185 -16.046 -10.311 2.757 1.00 36.78 A C ANISOU 1518 CD2 LEU A 185 6160 4416 3401 886 -97 -2 A C ATOM 1519 N TYR A 186 -14.555 -12.989 -0.929 1.00 30.21 A N ANISOU 1519 N TYR A 186 5535 3418 2527 503 26 -76 A N ATOM 1520 CA TYR A 186 -14.117 -12.547 -2.252 1.00 36.35 A C ANISOU 1520 CA TYR A 186 6410 4152 3251 507 42 -71 A C ATOM 1521 C TYR A 186 -13.102 -13.491 -2.889 1.00 37.97 A C ANISOU 1521 C TYR A 186 6671 4254 3501 385 106 -122 A C ATOM 1522 O TYR A 186 -12.251 -13.063 -3.668 1.00 39.98 A O ANISOU 1522 O TYR A 186 7013 4428 3748 379 146 -126 A O ATOM 1523 CB TYR A 186 -13.531 -11.134 -2.191 1.00 34.94 A C ANISOU 1523 CB TYR A 186 6325 3871 3079 618 55 -26 A C ATOM 1524 CG TYR A 186 -14.422 -10.123 -1.511 1.00 34.81 A C ANISOU 1524 CG TYR A 186 6274 3929 3023 766 -8 17 A C ATOM 1525 CD1 TYR A 186 -15.776 -10.048 -1.814 1.00 30.88 A C ANISOU 1525 CD1 TYR A 186 5704 3619 2410 833 -89 27 A C ATOM 1526 CD2 TYR A 186 -13.905 -9.233 -0.577 1.00 30.73 A C ANISOU 1526 CD2 TYR A 186 5792 3310 2573 843 12 35 A C ATOM 1527 CE1 TYR A 186 -16.593 -9.124 -1.197 1.00 37.81 A C ANISOU 1527 CE1 TYR A 186 6545 4581 3240 993 -154 52 A C ATOM 1528 CE2 TYR A 186 -14.714 -8.303 0.044 1.00 33.57 A C ANISOU 1528 CE2 TYR A 186 6127 3733 2895 990 -48 65 A C ATOM 1529 CZ TYR A 186 -16.058 -8.253 -0.269 1.00 36.55 A C ANISOU 1529 CZ TYR A 186 6433 4297 3157 1074 -134 74 A C ATOM 1530 OH TYR A 186 -16.871 -7.329 0.346 1.00 37.81 A O ANISOU 1530 OH TYR A 186 6561 4536 3268 1244 -201 90 A O ATOM 1531 N LEU A 187 -13.194 -14.774 -2.557 1.00 38.49 A N ANISOU 1531 N LEU A 187 6695 4324 3604 287 119 -166 A N ATOM 1532 CA LEU A 187 -12.321 -15.770 -3.161 1.00 35.35 A C ANISOU 1532 CA LEU A 187 6355 3834 3242 191 171 -226 A C ATOM 1533 C LEU A 187 -12.641 -15.916 -4.645 1.00 34.25 A C ANISOU 1533 C LEU A 187 6240 3767 3006 131 165 -250 A C ATOM 1534 O LEU A 187 -13.798 -16.101 -5.023 1.00 44.00 A O ANISOU 1534 O LEU A 187 7418 5147 4151 100 121 -249 A O ATOM 1535 CB LEU A 187 -12.474 -17.116 -2.452 1.00 37.40 A C ANISOU 1535 CB LEU A 187 6600 4063 3548 109 182 -261 A C ATOM 1536 CG LEU A 187 -11.556 -18.244 -2.931 1.00 39.69 A C ANISOU 1536 CG LEU A 187 6968 4236 3876 37 231 -331 A C ATOM 1537 CD1 LEU A 187 -10.099 -17.887 -2.688 1.00 43.13 A C ANISOU 1537 CD1 LEU A 187 7443 4559 4388 114 273 -353 A C ATOM 1538 CD2 LEU A 187 -11.910 -19.551 -2.243 1.00 40.96 A C ANISOU 1538 CD2 LEU A 187 7152 4352 4060 -43 238 -352 A C ATOM 1539 N GLY A 188 -11.613 -15.826 -5.482 1.00 30.37 A N ANISOU 1539 N GLY A 188 5821 3198 2520 110 210 -280 A N ATOM 1540 CA GLY A 188 -11.779 -15.974 -6.918 1.00 30.55 A C ANISOU 1540 CA GLY A 188 5869 3288 2449 50 210 -307 A C ATOM 1541 C GLY A 188 -12.362 -14.739 -7.578 1.00 29.67 A C ANISOU 1541 C GLY A 188 5779 3265 2229 128 171 -238 A C ATOM 1542 O GLY A 188 -12.725 -14.765 -8.754 1.00 41.32 A O ANISOU 1542 O GLY A 188 7267 4830 3601 97 157 -247 A O ATOM 1543 N GLU A 189 -12.452 -13.656 -6.815 1.00 29.91 A N ANISOU 1543 N GLU A 189 5824 3267 2275 241 152 -171 A N ATOM 1544 CA GLU A 189 -13.002 -12.406 -7.319 1.00 44.09 A C ANISOU 1544 CA GLU A 189 7673 5116 3963 350 110 -98 A C ATOM 1545 C GLU A 189 -11.920 -11.337 -7.409 1.00 40.57 A C ANISOU 1545 C GLU A 189 7358 4521 3534 379 164 -65 A C ATOM 1546 O GLU A 189 -10.896 -11.417 -6.731 1.00 31.88 A O ANISOU 1546 O GLU A 189 6266 3307 2540 341 223 -99 A O ATOM 1547 CB GLU A 189 -14.145 -11.927 -6.420 1.00 57.14 A C ANISOU 1547 CB GLU A 189 9250 6868 5592 468 37 -55 A C ATOM 1548 CG GLU A 189 -15.321 -12.888 -6.348 1.00 75.22 A C ANISOU 1548 CG GLU A 189 11403 9343 7836 417 -12 -99 A C ATOM 1549 CD GLU A 189 -16.144 -12.897 -7.620 1.00 99.96 A C ANISOU 1549 CD GLU A 189 14518 12647 10814 422 -57 -107 A C ATOM 1550 OE1 GLU A 189 -16.253 -11.833 -8.265 1.00108.15 A O ANISOU 1550 OE1 GLU A 189 15639 13697 11756 544 -87 -48 A O ATOM 1551 OE2 GLU A 189 -16.689 -13.965 -7.973 1.00108.40 A O1- ANISOU 1551 OE2 GLU A 189 15500 13839 11848 304 -60 -175 A O1- ATOM 1552 N GLU A 190 -12.153 -10.339 -8.255 1.00 41.46 A N ANISOU 1552 N GLU A 190 7580 4643 3530 444 147 -2 A N ATOM 1553 CA GLU A 190 -11.223 -9.230 -8.410 1.00 41.03 A C ANISOU 1553 CA GLU A 190 7683 4442 3465 450 206 34 A C ATOM 1554 C GLU A 190 -11.181 -8.399 -7.135 1.00 42.47 A C ANISOU 1554 C GLU A 190 7883 4536 3719 543 204 67 A C ATOM 1555 O GLU A 190 -12.219 -7.968 -6.636 1.00 49.72 A O ANISOU 1555 O GLU A 190 8770 5518 4605 679 129 113 A O ATOM 1556 CB GLU A 190 -11.645 -8.348 -9.584 1.00 56.80 A C ANISOU 1556 CB GLU A 190 9824 6458 5298 512 180 110 A C ATOM 1557 CG GLU A 190 -10.600 -7.332 -9.998 1.00 68.57 A C ANISOU 1557 CG GLU A 190 11512 7789 6754 463 261 142 A C ATOM 1558 CD GLU A 190 -9.446 -7.965 -10.746 1.00 71.97 A C ANISOU 1558 CD GLU A 190 11943 8202 7199 280 349 64 A C ATOM 1559 OE1 GLU A 190 -8.402 -7.300 -10.909 1.00 83.96 A O ANISOU 1559 OE1 GLU A 190 13588 9606 8707 193 436 57 A O ATOM 1560 OE2 GLU A 190 -9.585 -9.131 -11.171 1.00 63.85 A O1- ANISOU 1560 OE2 GLU A 190 10791 7283 6186 217 334 0 A O1- ATOM 1561 N VAL A 191 -9.980 -8.171 -6.614 1.00 27.18 A N ANISOU 1561 N VAL A 191 5983 2475 1869 472 287 28 A N ATOM 1562 CA VAL A 191 -9.823 -7.418 -5.375 1.00 26.77 A C ANISOU 1562 CA VAL A 191 5939 2342 1890 542 296 41 A C ATOM 1563 C VAL A 191 -8.695 -6.396 -5.468 1.00 36.30 A C ANISOU 1563 C VAL A 191 7301 3403 3089 477 390 35 A C ATOM 1564 O VAL A 191 -7.891 -6.419 -6.400 1.00 33.31 A O ANISOU 1564 O VAL A 191 7001 2994 2662 357 457 6 A O ATOM 1565 CB VAL A 191 -9.553 -8.350 -4.177 1.00 25.54 A C ANISOU 1565 CB VAL A 191 5619 2214 1870 517 302 -25 A C ATOM 1566 CG1 VAL A 191 -10.748 -9.261 -3.933 1.00 44.08 A C ANISOU 1566 CG1 VAL A 191 7834 4698 4217 561 219 -16 A C ATOM 1567 CG2 VAL A 191 -8.290 -9.164 -4.411 1.00 30.41 A C ANISOU 1567 CG2 VAL A 191 6207 2804 2545 385 380 -116 A C ATOM 1568 N LYS A 192 -8.646 -5.498 -4.490 1.00 34.70 A N ANISOU 1568 N LYS A 192 7140 3118 2925 545 400 52 A N ATOM 1569 CA LYS A 192 -7.594 -4.494 -4.421 1.00 36.26 A C ANISOU 1569 CA LYS A 192 7485 3176 3115 462 499 31 A C ATOM 1570 C LYS A 192 -7.036 -4.387 -3.003 1.00 32.19 A C ANISOU 1570 C LYS A 192 6873 2637 2720 460 536 -34 A C ATOM 1571 O LYS A 192 -7.785 -4.395 -2.025 1.00 39.18 A O ANISOU 1571 O LYS A 192 7666 3559 3660 584 469 -12 A O ATOM 1572 CB LYS A 192 -8.110 -3.132 -4.893 1.00 35.28 A C ANISOU 1572 CB LYS A 192 7596 2937 2872 548 485 130 A C ATOM 1573 CG LYS A 192 -9.235 -2.560 -4.045 1.00 53.76 A C ANISOU 1573 CG LYS A 192 9929 5280 5219 752 393 188 A C ATOM 1574 CD LYS A 192 -9.602 -1.150 -4.492 1.00 73.92 A C ANISOU 1574 CD LYS A 192 12753 7686 7646 855 385 278 A C ATOM 1575 CE LYS A 192 -10.395 -1.158 -5.788 1.00 83.87 A C ANISOU 1575 CE LYS A 192 14110 9001 8756 938 317 361 A C ATOM 1576 NZ LYS A 192 -11.770 -1.699 -5.596 1.00 87.87 A N1+ ANISOU 1576 NZ LYS A 192 14444 9697 9245 1120 182 381 A N1+ ATOM 1577 N LEU A 193 -5.715 -4.297 -2.899 1.00 26.80 A N ANISOU 1577 N LEU A 193 6197 1917 2067 316 643 -124 A N ATOM 1578 CA LEU A 193 -5.055 -4.161 -1.606 1.00 26.17 A C ANISOU 1578 CA LEU A 193 6021 1836 2086 304 688 -202 A C ATOM 1579 C LEU A 193 -4.361 -2.809 -1.494 1.00 40.93 A C ANISOU 1579 C LEU A 193 8061 3578 3914 220 785 -224 A C ATOM 1580 O LEU A 193 -3.520 -2.464 -2.325 1.00 46.07 A O ANISOU 1580 O LEU A 193 8829 4186 4491 65 877 -262 A O ATOM 1581 CB LEU A 193 -4.039 -5.285 -1.393 1.00 25.39 A C ANISOU 1581 CB LEU A 193 5753 1840 2055 217 731 -319 A C ATOM 1582 CG LEU A 193 -4.588 -6.685 -1.113 1.00 37.23 A C ANISOU 1582 CG LEU A 193 7086 3441 3619 296 648 -316 A C ATOM 1583 CD1 LEU A 193 -5.274 -7.258 -2.344 1.00 32.77 A C ANISOU 1583 CD1 LEU A 193 6562 2903 2985 290 598 -261 A C ATOM 1584 CD2 LEU A 193 -3.473 -7.608 -0.644 1.00 38.31 A C ANISOU 1584 CD2 LEU A 193 7085 3651 3820 249 693 -438 A C ATOM 1585 N LEU A 194 -4.715 -2.047 -0.464 1.00 38.66 A N ANISOU 1585 N LEU A 194 7792 3232 3666 311 770 -207 A N ATOM 1586 CA LEU A 194 -4.119 -0.733 -0.254 1.00 41.25 A C ANISOU 1586 CA LEU A 194 8298 3420 3956 227 866 -235 A C ATOM 1587 C LEU A 194 -3.528 -0.591 1.142 1.00 42.54 A C ANISOU 1587 C LEU A 194 8324 3622 4216 213 909 -336 A C ATOM 1588 O LEU A 194 -3.945 -1.270 2.080 1.00 51.59 A O ANISOU 1588 O LEU A 194 9274 4873 5453 329 837 -344 A O ATOM 1589 CB LEU A 194 -5.140 0.377 -0.504 1.00 46.78 A C ANISOU 1589 CB LEU A 194 9228 3971 4577 359 814 -114 A C ATOM 1590 CG LEU A 194 -5.699 0.481 -1.923 1.00 52.12 A C ANISOU 1590 CG LEU A 194 10081 4598 5126 384 776 -8 A C ATOM 1591 CD1 LEU A 194 -6.821 -0.522 -2.129 1.00 50.04 A C ANISOU 1591 CD1 LEU A 194 9655 4484 4876 539 642 51 A C ATOM 1592 CD2 LEU A 194 -6.190 1.891 -2.192 1.00 61.27 A C ANISOU 1592 CD2 LEU A 194 11546 5558 6178 466 777 83 A C ATOM 1593 N GLY A 195 -2.557 0.306 1.271 1.00 53.77 A N ANISOU 1593 N GLY A 195 9858 4966 5607 58 1033 -418 A N ATOM 1594 CA GLY A 195 -1.876 0.524 2.533 1.00 62.39 A C ANISOU 1594 CA GLY A 195 10821 6110 6773 20 1090 -536 A C ATOM 1595 C GLY A 195 -0.423 0.105 2.439 1.00 77.96 A C ANISOU 1595 C GLY A 195 12679 8207 8737 -175 1204 -693 A C ATOM 1596 O GLY A 195 -0.115 -1.085 2.382 1.00 87.87 A O ANISOU 1596 O GLY A 195 13740 9617 10031 -155 1171 -738 A O ATOM 1597 N GLU A 196 0.472 1.088 2.425 1.00 85.17 A N ANISOU 1597 N GLU A 196 13715 9058 9589 -365 1338 -786 A N ATOM 1598 CA GLU A 196 1.894 0.822 2.242 1.00 96.86 A C ANISOU 1598 CA GLU A 196 15089 10683 11030 -574 1459 -958 A C ATOM 1599 C GLU A 196 2.119 0.073 0.936 1.00 84.88 A C ANISOU 1599 C GLU A 196 13580 9220 9448 -640 1456 -943 A C ATOM 1600 O GLU A 196 2.744 -0.988 0.912 1.00 82.05 A O ANISOU 1600 O GLU A 196 13011 9050 9115 -642 1449 -1039 A O ATOM 1601 CB GLU A 196 2.455 0.022 3.419 1.00114.84 A C ANISOU 1601 CB GLU A 196 17061 13174 13400 -506 1442 -1085 A C ATOM 1602 CG GLU A 196 2.660 0.846 4.681 1.00127.48 A C ANISOU 1602 CG GLU A 196 18630 14768 15039 -516 1491 -1162 A C ATOM 1603 CD GLU A 196 3.312 0.052 5.795 1.00133.02 A C ANISOU 1603 CD GLU A 196 19029 15705 15809 -450 1479 -1295 A C ATOM 1604 OE1 GLU A 196 3.134 -1.184 5.829 1.00132.45 A O ANISOU 1604 OE1 GLU A 196 18794 15746 15786 -308 1386 -1266 A O ATOM 1605 OE2 GLU A 196 3.997 0.665 6.641 1.00134.88 A O1- ANISOU 1605 OE2 GLU A 196 19199 16009 16040 -537 1564 -1429 A O1- ATOM 1606 N GLY A 197 1.599 0.635 -0.150 1.00 70.96 A N ANISOU 1606 N GLY A 197 12071 7294 7596 -680 1458 -823 A N ATOM 1607 CA GLY A 197 1.696 0.017 -1.458 1.00 63.86 A C ANISOU 1607 CA GLY A 197 11202 6437 6625 -740 1452 -795 A C ATOM 1608 C GLY A 197 0.325 -0.227 -2.054 1.00 66.60 A C ANISOU 1608 C GLY A 197 11644 6690 6970 -553 1319 -609 A C ATOM 1609 O GLY A 197 -0.693 0.080 -1.433 1.00 57.96 A O ANISOU 1609 O GLY A 197 10584 5512 5926 -373 1230 -509 A O ATOM 1610 N LYS A 198 0.294 -0.781 -3.261 1.00 70.39 A N ANISOU 1610 N LYS A 198 12154 7208 7382 -595 1304 -576 A N ATOM 1611 CA LYS A 198 -0.971 -1.067 -3.929 1.00 58.26 A C ANISOU 1611 CA LYS A 198 10690 5622 5825 -431 1182 -418 A C ATOM 1612 C LYS A 198 -0.856 -2.221 -4.922 1.00 56.05 A C ANISOU 1612 C LYS A 198 10302 5473 5522 -459 1153 -437 A C ATOM 1613 O LYS A 198 -0.227 -2.093 -5.972 1.00 57.01 A O ANISOU 1613 O LYS A 198 10521 5604 5539 -624 1230 -469 A O ATOM 1614 CB LYS A 198 -1.506 0.186 -4.627 1.00 42.71 A C ANISOU 1614 CB LYS A 198 9047 3452 3731 -439 1199 -290 A C ATOM 1615 CG LYS A 198 -0.472 0.934 -5.451 1.00 51.42 A C ANISOU 1615 CG LYS A 198 10351 4483 4702 -699 1349 -342 A C ATOM 1616 CD LYS A 198 -1.096 2.124 -6.160 1.00 63.41 A C ANISOU 1616 CD LYS A 198 12232 5777 6085 -679 1355 -193 A C ATOM 1617 CE LYS A 198 -1.802 3.038 -5.175 1.00 69.24 A C ANISOU 1617 CE LYS A 198 13089 6355 6865 -518 1313 -128 A C ATOM 1618 NZ LYS A 198 -0.873 3.549 -4.130 1.00 76.15 A N1+ ANISOU 1618 NZ LYS A 198 13924 7210 7798 -664 1427 -265 A N1+ ATOM 1619 N ILE A 199 -1.469 -3.348 -4.577 1.00 54.96 A N ANISOU 1619 N ILE A 199 9973 5435 5476 -308 1045 -423 A N ATOM 1620 CA ILE A 199 -1.480 -4.514 -5.449 1.00 50.00 A C ANISOU 1620 CA ILE A 199 9245 4917 4835 -317 1008 -443 A C ATOM 1621 C ILE A 199 -2.911 -4.859 -5.840 1.00 42.73 A C ANISOU 1621 C ILE A 199 8347 3985 3904 -160 883 -308 A C ATOM 1622 O ILE A 199 -3.797 -4.930 -4.988 1.00 43.45 A O ANISOU 1622 O ILE A 199 8376 4069 4064 -8 799 -251 A O ATOM 1623 CB ILE A 199 -0.836 -5.743 -4.777 1.00 54.44 A C ANISOU 1623 CB ILE A 199 9562 5621 5501 -297 1000 -571 A C ATOM 1624 CG1 ILE A 199 0.657 -5.508 -4.530 1.00 61.42 A C ANISOU 1624 CG1 ILE A 199 10390 6576 6370 -450 1122 -734 A C ATOM 1625 CG2 ILE A 199 -1.043 -6.984 -5.632 1.00 53.80 A C ANISOU 1625 CG2 ILE A 199 9402 5626 5412 -279 947 -582 A C ATOM 1626 CD1 ILE A 199 0.960 -4.665 -3.306 1.00 55.37 A C ANISOU 1626 CD1 ILE A 199 9617 5771 5650 -449 1167 -769 A C ATOM 1627 N THR A 200 -3.134 -5.074 -7.131 1.00 43.84 A N ANISOU 1627 N THR A 200 8563 4147 3947 -204 872 -269 A N ATOM 1628 CA THR A 200 -4.467 -5.391 -7.625 1.00 41.92 A C ANISOU 1628 CA THR A 200 8332 3928 3669 -68 759 -159 A C ATOM 1629 C THR A 200 -4.466 -6.646 -8.492 1.00 43.89 A C ANISOU 1629 C THR A 200 8470 4300 3908 -110 734 -206 A C ATOM 1630 O THR A 200 -3.536 -6.886 -9.264 1.00 48.98 A O ANISOU 1630 O THR A 200 9123 4982 4505 -252 808 -284 A O ATOM 1631 CB THR A 200 -5.067 -4.218 -8.419 1.00 47.78 A C ANISOU 1631 CB THR A 200 9320 4566 4269 -34 750 -33 A C ATOM 1632 CG2 THR A 200 -5.159 -2.976 -7.544 1.00 53.04 A C ANISOU 1632 CG2 THR A 200 10122 5088 4944 26 769 13 A C ATOM 1633 OG1 THR A 200 -4.242 -3.933 -9.555 1.00 59.91 A O ANISOU 1633 OG1 THR A 200 10989 6082 5692 -206 842 -56 A O ATOM 1634 N GLY A 201 -5.518 -7.445 -8.353 1.00 43.74 A N ANISOU 1634 N GLY A 201 8344 4351 3924 5 633 -169 A N ATOM 1635 CA GLY A 201 -5.657 -8.671 -9.115 1.00 40.20 A C ANISOU 1635 CA GLY A 201 7797 4008 3468 -31 605 -216 A C ATOM 1636 C GLY A 201 -6.766 -9.546 -8.567 1.00 42.34 A C ANISOU 1636 C GLY A 201 7940 4348 3800 75 508 -193 A C ATOM 1637 O GLY A 201 -7.687 -9.058 -7.914 1.00 33.86 A O ANISOU 1637 O GLY A 201 6867 3265 2732 191 447 -117 A O ATOM 1638 N LYS A 202 -6.679 -10.844 -8.831 1.00 47.59 A N ANISOU 1638 N LYS A 202 8498 5083 4502 30 498 -268 A N ATOM 1639 CA LYS A 202 -7.693 -11.776 -8.358 1.00 39.14 A C ANISOU 1639 CA LYS A 202 7321 4075 3478 89 422 -259 A C ATOM 1640 C LYS A 202 -7.192 -12.585 -7.165 1.00 35.05 A C ANISOU 1640 C LYS A 202 6705 3524 3090 100 434 -324 A C ATOM 1641 O LYS A 202 -6.093 -13.141 -7.194 1.00 27.10 A O ANISOU 1641 O LYS A 202 5676 2495 2125 46 489 -419 A O ATOM 1642 CB LYS A 202 -8.136 -12.714 -9.482 1.00 33.22 A C ANISOU 1642 CB LYS A 202 6543 3416 2664 28 398 -291 A C ATOM 1643 CG LYS A 202 -9.514 -13.322 -9.257 1.00 32.87 A C ANISOU 1643 CG LYS A 202 6418 3463 2607 73 317 -262 A C ATOM 1644 CD LYS A 202 -9.853 -14.359 -10.313 1.00 41.50 A C ANISOU 1644 CD LYS A 202 7477 4647 3643 -13 307 -320 A C ATOM 1645 CE LYS A 202 -9.057 -15.635 -10.104 1.00 54.97 A C ANISOU 1645 CE LYS A 202 9146 6298 5443 -89 349 -428 A C ATOM 1646 NZ LYS A 202 -9.594 -16.758 -10.918 1.00 60.51 A N1+ ANISOU 1646 NZ LYS A 202 9814 7077 6100 -173 333 -490 A N1+ ATOM 1647 N LEU A 203 -8.006 -12.638 -6.117 1.00 28.54 A N ANISOU 1647 N LEU A 203 5270 2580 2992 395 378 -598 A N ATOM 1648 CA LEU A 203 -7.684 -13.413 -4.926 1.00 22.96 A C ANISOU 1648 CA LEU A 203 4590 1873 2259 490 386 -597 A C ATOM 1649 C LEU A 203 -7.803 -14.902 -5.228 1.00 19.42 A C ANISOU 1649 C LEU A 203 4361 1313 1705 399 474 -576 A C ATOM 1650 O LEU A 203 -8.890 -15.471 -5.172 1.00 28.08 A O ANISOU 1650 O LEU A 203 5573 2399 2696 265 469 -581 A O ATOM 1651 CB LEU A 203 -8.616 -13.025 -3.778 1.00 27.04 A C ANISOU 1651 CB LEU A 203 5055 2484 2735 596 346 -600 A C ATOM 1652 CG LEU A 203 -8.414 -13.747 -2.445 1.00 30.95 A C ANISOU 1652 CG LEU A 203 5572 2993 3196 711 351 -596 A C ATOM 1653 CD1 LEU A 203 -6.950 -13.723 -2.027 1.00 29.84 A C ANISOU 1653 CD1 LEU A 203 5401 2825 3111 786 318 -621 A C ATOM 1654 CD2 LEU A 203 -9.293 -13.125 -1.372 1.00 21.67 A C ANISOU 1654 CD2 LEU A 203 4363 1916 1953 885 332 -585 A C ATOM 1655 N VAL A 204 -6.676 -15.529 -5.546 1.00 26.28 A N ANISOU 1655 N VAL A 204 5343 2087 2555 476 560 -558 A N ATOM 1656 CA VAL A 204 -6.675 -16.918 -5.993 1.00 31.80 A C ANISOU 1656 CA VAL A 204 6402 2596 3084 430 675 -533 A C ATOM 1657 C VAL A 204 -6.557 -17.922 -4.848 1.00 35.21 A C ANISOU 1657 C VAL A 204 6960 2984 3435 542 730 -519 A C ATOM 1658 O VAL A 204 -6.868 -19.101 -5.020 1.00 32.75 A O ANISOU 1658 O VAL A 204 7034 2474 2935 459 808 -509 A O ATOM 1659 CB VAL A 204 -5.555 -17.182 -7.015 1.00 28.68 A C ANISOU 1659 CB VAL A 204 6172 2084 2639 558 811 -499 A C ATOM 1660 CG1 VAL A 204 -5.814 -16.401 -8.294 1.00 25.17 A C ANISOU 1660 CG1 VAL A 204 5686 1641 2235 418 772 -510 A C ATOM 1661 CG2 VAL A 204 -4.201 -16.825 -6.428 1.00 28.08 A C ANISOU 1661 CG2 VAL A 204 5869 2130 2670 831 858 -476 A C ATOM 1662 N GLY A 205 -6.107 -17.460 -3.685 1.00 30.42 A N ANISOU 1662 N GLY A 205 6092 2532 2935 711 682 -523 A N ATOM 1663 CA GLY A 205 -5.989 -18.338 -2.534 1.00 19.25 A C ANISOU 1663 CA GLY A 205 4764 1101 1450 841 733 -504 A C ATOM 1664 C GLY A 205 -5.109 -17.813 -1.418 1.00 35.21 A C ANISOU 1664 C GLY A 205 6528 3286 3563 1049 681 -510 A C ATOM 1665 O GLY A 205 -4.882 -16.609 -1.295 1.00 31.85 A O ANISOU 1665 O GLY A 205 5873 2977 3252 1037 559 -554 A O ATOM 1666 N LEU A 206 -4.612 -18.736 -0.603 1.00 36.54 A N ANISOU 1666 N LEU A 206 6797 3438 3648 1233 773 -471 A N ATOM 1667 CA LEU A 206 -3.809 -18.399 0.563 1.00 32.74 A C ANISOU 1667 CA LEU A 206 6108 3119 3214 1423 720 -479 A C ATOM 1668 C LEU A 206 -2.563 -19.276 0.616 1.00 42.94 A C ANISOU 1668 C LEU A 206 7476 4427 4414 1716 907 -391 A C ATOM 1669 O LEU A 206 -2.624 -20.471 0.324 1.00 51.60 A O ANISOU 1669 O LEU A 206 8893 5358 5353 1810 1087 -318 A O ATOM 1670 CB LEU A 206 -4.634 -18.597 1.834 1.00 36.99 A C ANISOU 1670 CB LEU A 206 6642 3692 3722 1425 653 -492 A C ATOM 1671 CG LEU A 206 -4.029 -18.076 3.137 1.00 37.79 A C ANISOU 1671 CG LEU A 206 6570 3942 3846 1582 551 -528 A C ATOM 1672 CD1 LEU A 206 -4.078 -16.558 3.170 1.00 29.72 A C ANISOU 1672 CD1 LEU A 206 5413 2970 2907 1485 369 -622 A C ATOM 1673 CD2 LEU A 206 -4.756 -18.663 4.335 1.00 38.90 A C ANISOU 1673 CD2 LEU A 206 6778 4091 3911 1654 555 -504 A C ATOM 1674 N SER A 207 -1.432 -18.684 0.989 1.00 43.13 A N ANISOU 1674 N SER A 207 7234 4647 4504 1889 886 -386 A N ATOM 1675 CA SER A 207 -0.181 -19.430 1.076 1.00 41.72 A C ANISOU 1675 CA SER A 207 7011 4612 4229 2241 1090 -214 A C ATOM 1676 C SER A 207 -0.036 -20.097 2.440 1.00 40.39 A C ANISOU 1676 C SER A 207 6836 4534 3975 2432 1115 -174 A C ATOM 1677 O SER A 207 -0.843 -19.869 3.341 1.00 39.29 A O ANISOU 1677 O SER A 207 6709 4349 3870 2286 960 -297 A O ATOM 1678 CB SER A 207 1.017 -18.517 0.800 1.00 44.16 A C ANISOU 1678 CB SER A 207 6921 5240 4618 2226 988 -39 A C ATOM 1679 OG SER A 207 1.250 -17.632 1.882 1.00 44.42 A O ANISOU 1679 OG SER A 207 6682 5477 4718 2058 713 -54 A O ATOM 1680 N GLU A 208 0.997 -20.921 2.585 1.00 45.40 A N ANISOU 1680 N GLU A 208 7449 5328 4474 2787 1322 49 A N ATOM 1681 CA GLU A 208 1.229 -21.640 3.833 1.00 49.88 A C ANISOU 1681 CA GLU A 208 8015 6002 4936 3021 1380 118 A C ATOM 1682 C GLU A 208 1.594 -20.694 4.972 1.00 40.22 A C ANISOU 1682 C GLU A 208 6391 5084 3808 2875 1082 128 A C ATOM 1683 O GLU A 208 1.354 -20.996 6.140 1.00 40.11 A O ANISOU 1683 O GLU A 208 6404 5089 3747 2944 1036 82 A O ATOM 1684 CB GLU A 208 2.324 -22.696 3.654 1.00 62.71 A C ANISOU 1684 CB GLU A 208 9704 7770 6353 3506 1707 412 A C ATOM 1685 CG GLU A 208 1.951 -23.836 2.718 1.00 79.89 A C ANISOU 1685 CG GLU A 208 12483 9547 8324 3685 2014 415 A C ATOM 1686 CD GLU A 208 2.033 -23.441 1.257 1.00 95.78 A C ANISOU 1686 CD GLU A 208 14575 11453 10362 3610 2072 416 A C ATOM 1687 OE1 GLU A 208 1.356 -24.083 0.427 1.00100.17 A O ANISOU 1687 OE1 GLU A 208 15676 11609 10776 3508 2166 364 A O ATOM 1688 OE2 GLU A 208 2.776 -22.488 0.940 1.00100.29 A O1- ANISOU 1688 OE2 GLU A 208 14676 12358 11070 3565 1962 542 A O1- ATOM 1689 N LYS A 209 2.177 -19.550 4.627 1.00 35.05 A N ANISOU 1689 N LYS A 209 5416 4645 3256 2652 870 193 A N ATOM 1690 CA LYS A 209 2.572 -18.564 5.627 1.00 42.69 A C ANISOU 1690 CA LYS A 209 6109 5855 4256 2428 540 209 A C ATOM 1691 C LYS A 209 1.387 -17.708 6.063 1.00 38.76 A C ANISOU 1691 C LYS A 209 5818 5077 3833 2147 320 -98 A C ATOM 1692 O LYS A 209 1.507 -16.874 6.961 1.00 39.80 A O ANISOU 1692 O LYS A 209 5896 5290 3938 1966 47 -141 A O ATOM 1693 CB LYS A 209 3.691 -17.672 5.087 1.00 52.93 A C ANISOU 1693 CB LYS A 209 7031 7491 5590 2236 375 442 A C ATOM 1694 CG LYS A 209 4.980 -18.411 4.767 1.00 61.26 A C ANISOU 1694 CG LYS A 209 7781 8959 6536 2570 594 855 A C ATOM 1695 CD LYS A 209 6.023 -17.465 4.190 1.00 66.13 A C ANISOU 1695 CD LYS A 209 7968 9966 7191 2322 410 1141 A C ATOM 1696 CE LYS A 209 7.311 -18.198 3.854 1.00 71.38 A C ANISOU 1696 CE LYS A 209 8262 11138 7720 2725 668 1645 A C ATOM 1697 NZ LYS A 209 8.311 -17.292 3.225 1.00 76.75 A N1+ ANISOU 1697 NZ LYS A 209 8467 12259 8434 2462 494 1992 A N1+ ATOM 1698 N GLY A 210 0.243 -17.918 5.420 1.00 32.00 A N ANISOU 1698 N GLY A 210 5227 3904 3029 2123 445 -279 A N ATOM 1699 CA GLY A 210 -0.948 -17.146 5.719 1.00 29.07 A C ANISOU 1699 CA GLY A 210 5021 3324 2699 1942 299 -495 A C ATOM 1700 C GLY A 210 -1.019 -15.877 4.893 1.00 33.55 A C ANISOU 1700 C GLY A 210 5556 3839 3351 1680 142 -558 A C ATOM 1701 O GLY A 210 -1.755 -14.948 5.223 1.00 37.19 A O ANISOU 1701 O GLY A 210 6152 4175 3805 1561 -4 -694 A O ATOM 1702 N GLY A 211 -0.246 -15.840 3.813 1.00 36.77 A N ANISOU 1702 N GLY A 211 5816 4341 3813 1634 199 -437 A N ATOM 1703 CA GLY A 211 -0.224 -14.688 2.932 1.00 29.27 A C ANISOU 1703 CA GLY A 211 4831 3345 2945 1387 69 -474 A C ATOM 1704 C GLY A 211 -1.267 -14.789 1.836 1.00 29.26 A C ANISOU 1704 C GLY A 211 5000 3114 3002 1364 211 -590 A C ATOM 1705 O GLY A 211 -1.627 -15.884 1.405 1.00 29.82 A O ANISOU 1705 O GLY A 211 5189 3098 3044 1502 424 -576 A O ATOM 1706 N ALA A 212 -1.757 -13.639 1.386 1.00 21.94 A N ANISOU 1706 N ALA A 212 4131 2082 2124 1173 84 -689 A N ATOM 1707 CA ALA A 212 -2.740 -13.602 0.314 1.00 23.03 A C ANISOU 1707 CA ALA A 212 4383 2061 2305 1125 189 -764 A C ATOM 1708 C ALA A 212 -2.064 -13.776 -1.041 1.00 24.16 A C ANISOU 1708 C ALA A 212 4444 2230 2507 1094 295 -672 A C ATOM 1709 O ALA A 212 -1.039 -13.154 -1.320 1.00 19.62 A O ANISOU 1709 O ALA A 212 3694 1786 1974 1013 210 -570 A O ATOM 1710 CB ALA A 212 -3.523 -12.300 0.357 1.00 18.01 A C ANISOU 1710 CB ALA A 212 3835 1347 1662 996 42 -837 A C ATOM 1711 N LEU A 213 -2.642 -14.635 -1.874 1.00 29.94 A N ANISOU 1711 N LEU A 213 5305 2864 3205 1117 456 -643 A N ATOM 1712 CA LEU A 213 -2.127 -14.872 -3.215 1.00 19.31 A C ANISOU 1712 CA LEU A 213 3992 1475 1870 1148 596 -584 A C ATOM 1713 C LEU A 213 -2.942 -14.092 -4.238 1.00 26.62 A C ANISOU 1713 C LEU A 213 4938 2335 2841 923 524 -611 A C ATOM 1714 O LEU A 213 -4.097 -14.420 -4.504 1.00 36.84 A O ANISOU 1714 O LEU A 213 6343 3576 4077 803 523 -592 A O ATOM 1715 CB LEU A 213 -2.158 -16.365 -3.542 1.00 19.45 A C ANISOU 1715 CB LEU A 213 4250 1399 1740 1286 801 -481 A C ATOM 1716 CG LEU A 213 -1.216 -17.245 -2.720 1.00 32.19 A C ANISOU 1716 CG LEU A 213 5860 3099 3271 1602 945 -397 A C ATOM 1717 CD1 LEU A 213 -1.486 -18.719 -2.980 1.00 26.37 A C ANISOU 1717 CD1 LEU A 213 5519 2174 2328 1717 1142 -309 A C ATOM 1718 CD2 LEU A 213 0.237 -16.898 -3.018 1.00 26.63 A C ANISOU 1718 CD2 LEU A 213 4870 2652 2598 1764 994 -192 A C ATOM 1719 N ILE A 214 -2.334 -13.054 -4.801 1.00 29.46 A N ANISOU 1719 N ILE A 214 5187 2706 3300 878 473 -652 A N ATOM 1720 CA ILE A 214 -3.016 -12.188 -5.755 1.00 22.45 A C ANISOU 1720 CA ILE A 214 4305 1775 2449 698 413 -666 A C ATOM 1721 C ILE A 214 -2.450 -12.348 -7.159 1.00 34.91 A C ANISOU 1721 C ILE A 214 5911 3306 4048 732 550 -614 A C ATOM 1722 O ILE A 214 -1.272 -12.082 -7.400 1.00 41.17 A O ANISOU 1722 O ILE A 214 6546 4206 4892 794 574 -506 A O ATOM 1723 CB ILE A 214 -2.902 -10.707 -5.353 1.00 22.14 A C ANISOU 1723 CB ILE A 214 4216 1724 2472 589 235 -753 A C ATOM 1724 CG1 ILE A 214 -3.495 -10.478 -3.961 1.00 29.29 A C ANISOU 1724 CG1 ILE A 214 5176 2645 3306 611 119 -792 A C ATOM 1725 CG2 ILE A 214 -3.583 -9.824 -6.388 1.00 16.54 A C ANISOU 1725 CG2 ILE A 214 3525 982 1779 467 217 -739 A C ATOM 1726 CD1 ILE A 214 -4.939 -10.896 -3.837 1.00 24.43 A C ANISOU 1726 CD1 ILE A 214 4598 2066 2617 639 167 -730 A C ATOM 1727 N LEU A 215 -3.296 -12.780 -8.087 1.00 38.01 A N ANISOU 1727 N LEU A 215 6447 3633 4362 644 609 -575 A N ATOM 1728 CA LEU A 215 -2.891 -12.920 -9.478 1.00 40.72 A C ANISOU 1728 CA LEU A 215 6890 3900 4683 681 738 -527 A C ATOM 1729 C LEU A 215 -2.960 -11.578 -10.200 1.00 34.35 A C ANISOU 1729 C LEU A 215 5945 3117 3988 552 652 -562 A C ATOM 1730 O LEU A 215 -4.044 -11.089 -10.516 1.00 31.73 A O ANISOU 1730 O LEU A 215 5619 2798 3637 398 573 -579 A O ATOM 1731 CB LEU A 215 -3.773 -13.944 -10.192 1.00 37.65 A C ANISOU 1731 CB LEU A 215 6809 3377 4120 602 813 -496 A C ATOM 1732 CG LEU A 215 -3.522 -14.100 -11.693 1.00 32.50 A C ANISOU 1732 CG LEU A 215 6360 2601 3386 631 938 -456 A C ATOM 1733 CD1 LEU A 215 -2.091 -14.544 -11.958 1.00 23.20 A C ANISOU 1733 CD1 LEU A 215 5244 1393 2176 972 1153 -367 A C ATOM 1734 CD2 LEU A 215 -4.513 -15.075 -12.302 1.00 31.81 A C ANISOU 1734 CD2 LEU A 215 6675 2331 3079 475 958 -459 A C ATOM 1735 N THR A 216 -1.798 -10.985 -10.454 1.00 36.55 A N ANISOU 1735 N THR A 216 6088 3426 4374 632 678 -534 A N ATOM 1736 CA THR A 216 -1.720 -9.715 -11.170 1.00 32.09 A C ANISOU 1736 CA THR A 216 5423 2868 3903 486 596 -535 A C ATOM 1737 C THR A 216 -1.382 -9.952 -12.637 1.00 40.43 A C ANISOU 1737 C THR A 216 6538 3886 4938 573 762 -446 A C ATOM 1738 O THR A 216 -1.253 -11.097 -13.072 1.00 44.32 A O ANISOU 1738 O THR A 216 7215 4313 5312 754 939 -394 A O ATOM 1739 CB THR A 216 -0.663 -8.782 -10.553 1.00 39.76 A C ANISOU 1739 CB THR A 216 6151 4003 4954 371 443 -421 A C ATOM 1740 CG2 THR A 216 -0.891 -8.631 -9.058 1.00 42.81 A C ANISOU 1740 CG2 THR A 216 6554 4400 5312 307 280 -504 A C ATOM 1741 OG1 THR A 216 0.646 -9.318 -10.781 1.00 37.37 A O ANISOU 1741 OG1 THR A 216 5636 3915 4648 505 553 -170 A O ATOM 1742 N GLU A 217 -1.238 -8.872 -13.399 1.00 49.09 A N ANISOU 1742 N GLU A 217 7543 4991 6117 459 714 -424 A N ATOM 1743 CA GLU A 217 -0.883 -8.991 -14.810 1.00 59.40 A C ANISOU 1743 CA GLU A 217 8898 6269 7402 557 874 -327 A C ATOM 1744 C GLU A 217 0.519 -9.565 -14.984 1.00 47.97 A C ANISOU 1744 C GLU A 217 7294 5007 5925 790 1037 -59 A C ATOM 1745 O GLU A 217 0.863 -10.065 -16.054 1.00 49.13 A O ANISOU 1745 O GLU A 217 7566 5119 5984 1001 1245 55 A O ATOM 1746 CB GLU A 217 -0.995 -7.643 -15.528 1.00 77.03 A C ANISOU 1746 CB GLU A 217 11051 8485 9731 389 789 -343 A C ATOM 1747 CG GLU A 217 -2.421 -7.216 -15.834 1.00 91.73 A C ANISOU 1747 CG GLU A 217 13079 10224 11552 274 725 -515 A C ATOM 1748 CD GLU A 217 -3.141 -6.682 -14.615 1.00107.31 A C ANISOU 1748 CD GLU A 217 15016 12255 13504 166 560 -582 A C ATOM 1749 OE1 GLU A 217 -4.364 -6.904 -14.497 1.00108.09 A O ANISOU 1749 OE1 GLU A 217 15159 12416 13497 142 538 -584 A O ATOM 1750 OE2 GLU A 217 -2.480 -6.041 -13.771 1.00118.04 A O1- ANISOU 1750 OE2 GLU A 217 16338 13565 14947 108 451 -618 A O1- ATOM 1751 N GLU A 218 1.323 -9.496 -13.929 1.00 46.39 A N ANISOU 1751 N GLU A 218 6830 5029 5768 776 952 77 A N ATOM 1752 CA GLU A 218 2.686 -10.012 -13.983 1.00 51.97 A C ANISOU 1752 CA GLU A 218 7293 6027 6427 1024 1110 420 A C ATOM 1753 C GLU A 218 2.894 -11.200 -13.049 1.00 38.01 A C ANISOU 1753 C GLU A 218 5585 4319 4540 1268 1211 472 A C ATOM 1754 O GLU A 218 3.986 -11.399 -12.515 1.00 39.28 A O ANISOU 1754 O GLU A 218 5431 4817 4677 1402 1246 768 A O ATOM 1755 CB GLU A 218 3.694 -8.905 -13.674 1.00 70.14 A C ANISOU 1755 CB GLU A 218 9156 8651 8844 777 921 661 A C ATOM 1756 CG GLU A 218 3.457 -8.198 -12.355 1.00 84.53 A C ANISOU 1756 CG GLU A 218 10921 10474 10723 432 605 524 A C ATOM 1757 CD GLU A 218 4.335 -6.977 -12.197 1.00101.26 A C ANISOU 1757 CD GLU A 218 12743 12825 12907 62 360 739 A C ATOM 1758 OE1 GLU A 218 4.886 -6.509 -13.216 1.00108.19 A O ANISOU 1758 OE1 GLU A 218 13459 13823 13826 28 423 943 A O ATOM 1759 OE2 GLU A 218 4.474 -6.484 -11.058 1.00107.64 A O1- ANISOU 1759 OE2 GLU A 218 13515 13683 13699 -221 94 716 A O1- ATOM 1760 N GLY A 219 1.840 -11.986 -12.856 1.00 40.48 A N ANISOU 1760 N GLY A 219 5774 6332 3274 359 1549 1560 A N ATOM 1761 CA GLY A 219 1.939 -13.214 -12.091 1.00 32.99 A C ANISOU 1761 CA GLY A 219 4900 5450 2187 548 1141 1210 A C ATOM 1762 C GLY A 219 1.315 -13.144 -10.713 1.00 40.18 A C ANISOU 1762 C GLY A 219 5919 6079 3267 475 851 1086 A C ATOM 1763 O GLY A 219 0.797 -12.107 -10.300 1.00 40.23 A O ANISOU 1763 O GLY A 219 5908 5850 3526 280 950 1259 A O ATOM 1764 N ILE A 220 1.368 -14.265 -10.001 1.00 34.96 A N ANISOU 1764 N ILE A 220 5404 5435 2444 645 488 783 A N ATOM 1765 CA ILE A 220 0.833 -14.353 -8.650 1.00 34.25 A C ANISOU 1765 CA ILE A 220 5476 5079 2457 605 215 637 A C ATOM 1766 C ILE A 220 1.817 -13.778 -7.642 1.00 27.09 A C ANISOU 1766 C ILE A 220 4291 4060 1941 537 205 351 A C ATOM 1767 O ILE A 220 2.978 -14.179 -7.597 1.00 37.56 A O ANISOU 1767 O ILE A 220 5412 5544 3316 657 154 34 A O ATOM 1768 CB ILE A 220 0.523 -15.811 -8.266 1.00 32.93 A C ANISOU 1768 CB ILE A 220 5647 4932 1932 815 -166 421 A C ATOM 1769 CG1 ILE A 220 -0.579 -16.376 -9.164 1.00 38.51 A C ANISOU 1769 CG1 ILE A 220 6535 5621 2478 866 -175 624 A C ATOM 1770 CG2 ILE A 220 0.124 -15.907 -6.800 1.00 32.81 A C ANISOU 1770 CG2 ILE A 220 5825 4629 2012 777 -410 242 A C ATOM 1771 CD1 ILE A 220 -1.007 -17.776 -8.794 1.00 34.85 A C ANISOU 1771 CD1 ILE A 220 6265 4962 2015 1012 -449 369 A C ATOM 1772 N LYS A 221 1.344 -12.834 -6.836 1.00 32.50 A N ANISOU 1772 N LYS A 221 4961 4475 2911 365 232 438 A N ATOM 1773 CA LYS A 221 2.170 -12.227 -5.801 1.00 31.27 A C ANISOU 1773 CA LYS A 221 4566 4167 3149 315 182 165 A C ATOM 1774 C LYS A 221 1.732 -12.695 -4.420 1.00 36.32 A C ANISOU 1774 C LYS A 221 5494 4568 3740 414 -170 -57 A C ATOM 1775 O LYS A 221 0.539 -12.839 -4.152 1.00 29.39 A O ANISOU 1775 O LYS A 221 4926 3554 2688 378 -244 127 A O ATOM 1776 CB LYS A 221 2.096 -10.702 -5.879 1.00 38.56 A C ANISOU 1776 CB LYS A 221 5253 4938 4460 57 475 411 A C ATOM 1777 CG LYS A 221 2.715 -10.102 -7.130 1.00 45.75 A C ANISOU 1777 CG LYS A 221 5884 6033 5466 -72 872 606 A C ATOM 1778 CD LYS A 221 2.553 -8.590 -7.143 1.00 58.94 A C ANISOU 1778 CD LYS A 221 7405 7493 7497 -337 1136 863 A C ATOM 1779 CE LYS A 221 3.274 -7.959 -8.325 1.00 64.66 A C ANISOU 1779 CE LYS A 221 7879 8362 8326 -494 1573 1046 A C ATOM 1780 NZ LYS A 221 4.747 -8.156 -8.247 1.00 67.45 A N1+ ANISOU 1780 NZ LYS A 221 7826 8880 8921 -490 1652 680 A N1+ ATOM 1781 N GLU A 222 2.704 -12.933 -3.547 1.00 41.24 A N ANISOU 1781 N GLU A 222 6021 5135 4514 549 -381 -471 A N ATOM 1782 CA GLU A 222 2.414 -13.342 -2.180 1.00 37.54 A C ANISOU 1782 CA GLU A 222 5869 4407 3986 675 -712 -708 A C ATOM 1783 C GLU A 222 2.540 -12.161 -1.227 1.00 28.42 A C ANISOU 1783 C GLU A 222 4546 2988 3263 570 -697 -759 A C ATOM 1784 O GLU A 222 3.637 -11.662 -0.982 1.00 42.54 A O ANISOU 1784 O GLU A 222 5990 4772 5403 591 -702 -1019 A O ATOM 1785 CB GLU A 222 3.345 -14.473 -1.744 1.00 43.23 A C ANISOU 1785 CB GLU A 222 6700 5193 4532 967 -1041 -1175 A C ATOM 1786 CG GLU A 222 3.050 -15.008 -0.354 1.00 47.77 A C ANISOU 1786 CG GLU A 222 7711 5473 4966 1132 -1391 -1422 A C ATOM 1787 CD GLU A 222 3.985 -16.128 0.049 1.00 62.04 A C ANISOU 1787 CD GLU A 222 9632 7320 6622 1470 -1736 -1823 A C ATOM 1788 OE1 GLU A 222 4.841 -16.512 -0.775 1.00 73.22 A O ANISOU 1788 OE1 GLU A 222 10841 9024 7954 1555 -1735 -2054 A O ATOM 1789 OE2 GLU A 222 3.865 -16.625 1.188 1.00 58.16 A O1- ANISOU 1789 OE2 GLU A 222 9392 6578 6127 1682 -1993 -1817 A O1- ATOM 1790 N ILE A 223 1.407 -11.714 -0.697 1.00 25.19 A N ANISOU 1790 N ILE A 223 4366 2364 2841 464 -685 -529 A N ATOM 1791 CA ILE A 223 1.383 -10.566 0.199 1.00 23.00 A C ANISOU 1791 CA ILE A 223 3968 1827 2945 379 -686 -545 A C ATOM 1792 C ILE A 223 1.571 -11.002 1.648 1.00 29.89 A C ANISOU 1792 C ILE A 223 5117 2455 3784 598 -1031 -909 A C ATOM 1793 O ILE A 223 0.733 -11.709 2.206 1.00 33.66 A O ANISOU 1793 O ILE A 223 6035 2820 3934 674 -1167 -892 A O ATOM 1794 CB ILE A 223 0.067 -9.781 0.070 1.00 22.38 A C ANISOU 1794 CB ILE A 223 3987 1642 2874 182 -510 -139 A C ATOM 1795 CG1 ILE A 223 -0.273 -9.552 -1.405 1.00 23.62 A C ANISOU 1795 CG1 ILE A 223 4006 2021 2947 26 -215 220 A C ATOM 1796 CG2 ILE A 223 0.160 -8.461 0.816 1.00 22.07 A C ANISOU 1796 CG2 ILE A 223 3765 1361 3258 91 -493 -137 A C ATOM 1797 CD1 ILE A 223 0.802 -8.818 -2.174 1.00 33.37 A C ANISOU 1797 CD1 ILE A 223 4820 3374 4484 -82 18 239 A C ATOM 1798 N LEU A 224 2.671 -10.569 2.255 1.00 34.14 A N ANISOU 1798 N LEU A 224 5407 2898 4666 701 -1167 -1249 A N ATOM 1799 CA LEU A 224 3.014 -10.997 3.606 1.00 28.06 A C ANISOU 1799 CA LEU A 224 4917 1884 3860 974 -1535 -1652 A C ATOM 1800 C LEU A 224 2.885 -9.881 4.640 1.00 33.99 A C ANISOU 1800 C LEU A 224 5585 2383 4946 954 -1601 -1645 A C ATOM 1801 O LEU A 224 3.227 -10.069 5.807 1.00 43.68 A O ANISOU 1801 O LEU A 224 6900 3564 6131 1185 -1921 -1830 A O ATOM 1802 CB LEU A 224 4.429 -11.579 3.636 1.00 28.81 A C ANISOU 1802 CB LEU A 224 4826 2087 4034 1210 -1756 -2137 A C ATOM 1803 CG LEU A 224 4.655 -12.813 2.759 1.00 33.11 A C ANISOU 1803 CG LEU A 224 5469 2922 4190 1305 -1776 -2187 A C ATOM 1804 CD1 LEU A 224 6.126 -13.204 2.742 1.00 34.90 A C ANISOU 1804 CD1 LEU A 224 5409 3283 4568 1536 -1980 -2700 A C ATOM 1805 CD2 LEU A 224 3.790 -13.976 3.226 1.00 30.88 A C ANISOU 1805 CD2 LEU A 224 5683 2639 3412 1463 -1968 -1935 A C ATOM 1806 N SER A 225 2.392 -8.722 4.214 1.00 44.18 A N ANISOU 1806 N SER A 225 6658 3612 6518 692 -1329 -1335 A N ATOM 1807 CA SER A 225 2.210 -7.595 5.123 1.00 49.80 A C ANISOU 1807 CA SER A 225 7309 4056 7558 671 -1393 -1329 A C ATOM 1808 C SER A 225 0.785 -7.538 5.662 1.00 53.01 A C ANISOU 1808 C SER A 225 8009 4513 7619 620 -1380 -989 A C ATOM 1809 O SER A 225 -0.177 -7.747 4.923 1.00 57.43 A O ANISOU 1809 O SER A 225 8701 5171 7950 465 -1168 -685 A O ATOM 1810 CB SER A 225 2.570 -6.278 4.434 1.00 54.34 A C ANISOU 1810 CB SER A 225 7395 4646 8604 409 -1139 -1142 A C ATOM 1811 OG SER A 225 3.933 -6.267 4.046 1.00 69.04 A O ANISOU 1811 OG SER A 225 8845 6628 10760 417 -1131 -1426 A O ATOM 1812 N GLY A 226 0.656 -7.256 6.954 1.00 55.79 A N ANISOU 1812 N GLY A 226 8459 4800 7938 760 -1611 -1076 A N ATOM 1813 CA GLY A 226 -0.644 -7.211 7.597 1.00 66.60 A C ANISOU 1813 CA GLY A 226 10109 6218 8977 723 -1591 -840 A C ATOM 1814 C GLY A 226 -1.238 -5.817 7.657 1.00 73.32 A C ANISOU 1814 C GLY A 226 10760 6984 10113 562 -1458 -654 A C ATOM 1815 O GLY A 226 -2.255 -5.597 8.312 1.00 77.14 A O ANISOU 1815 O GLY A 226 11423 7503 10385 551 -1456 -533 A O ATOM 1816 N GLU A 227 -0.605 -4.871 6.971 1.00 75.94 A N ANISOU 1816 N GLU A 227 10734 7190 10930 438 -1341 -633 A N ATOM 1817 CA GLU A 227 -1.091 -3.494 6.949 1.00 81.76 A C ANISOU 1817 CA GLU A 227 11283 7827 11955 292 -1238 -429 A C ATOM 1818 C GLU A 227 -2.024 -3.236 5.769 1.00 69.79 A C ANISOU 1818 C GLU A 227 9749 6426 10341 68 -938 -58 A C ATOM 1819 O GLU A 227 -2.698 -2.206 5.712 1.00 67.84 A O ANISOU 1819 O GLU A 227 9413 6159 10205 -31 -865 139 A O ATOM 1820 CB GLU A 227 0.078 -2.507 6.920 1.00 94.24 A C ANISOU 1820 CB GLU A 227 12511 9161 14136 261 -1282 -583 A C ATOM 1821 CG GLU A 227 0.778 -2.330 8.258 1.00103.08 A C ANISOU 1821 CG GLU A 227 13595 10153 15418 499 -1634 -936 A C ATOM 1822 CD GLU A 227 1.543 -3.565 8.685 1.00112.69 A C ANISOU 1822 CD GLU A 227 14946 11447 16422 737 -1859 -1277 A C ATOM 1823 OE1 GLU A 227 1.992 -4.322 7.799 1.00116.88 A O ANISOU 1823 OE1 GLU A 227 15448 12061 16901 697 -1731 -1331 A O ATOM 1824 OE2 GLU A 227 1.702 -3.775 9.907 1.00113.96 A O1- ANISOU 1824 OE2 GLU A 227 15264 11585 16449 980 -2183 -1490 A O1- ATOM 1825 N PHE A 228 -2.057 -4.174 4.828 1.00 62.07 A N ANISOU 1825 N PHE A 228 8865 5580 9140 17 -799 20 A N ATOM 1826 CA PHE A 228 -2.906 -4.046 3.650 1.00 59.67 A C ANISOU 1826 CA PHE A 228 8552 5423 8697 -158 -551 355 A C ATOM 1827 C PHE A 228 -4.379 -4.266 3.980 1.00 55.99 A C ANISOU 1827 C PHE A 228 8279 5139 7855 -146 -552 433 A C ATOM 1828 O PHE A 228 -4.733 -5.194 4.706 1.00 63.88 A O ANISOU 1828 O PHE A 228 9528 6204 8541 -43 -662 280 A O ATOM 1829 CB PHE A 228 -2.470 -5.026 2.558 1.00 53.59 A C ANISOU 1829 CB PHE A 228 7830 4739 7792 -194 -429 405 A C ATOM 1830 CG PHE A 228 -1.240 -4.599 1.813 1.00 52.65 A C ANISOU 1830 CG PHE A 228 7377 4644 7986 -292 -298 387 A C ATOM 1831 CD1 PHE A 228 0.009 -5.059 2.190 1.00 51.28 A C ANISOU 1831 CD1 PHE A 228 7058 4481 7945 -170 -432 27 A C ATOM 1832 CD2 PHE A 228 -1.335 -3.741 0.730 1.00 52.99 A C ANISOU 1832 CD2 PHE A 228 7231 4748 8154 -498 -34 700 A C ATOM 1833 CE1 PHE A 228 1.141 -4.670 1.504 1.00 53.71 A C ANISOU 1833 CE1 PHE A 228 6982 4886 8541 -279 -277 -29 A C ATOM 1834 CE2 PHE A 228 -0.207 -3.349 0.040 1.00 56.09 A C ANISOU 1834 CE2 PHE A 228 7297 5213 8804 -618 144 680 A C ATOM 1835 CZ PHE A 228 1.033 -3.814 0.427 1.00 57.80 A C ANISOU 1835 CZ PHE A 228 7312 5464 9184 -523 37 310 A C ATOM 1836 N SER A 229 -5.231 -3.402 3.441 1.00 45.62 A N ANISOU 1836 N SER A 229 6861 3887 6584 -251 -429 649 A N ATOM 1837 CA SER A 229 -6.673 -3.566 3.562 1.00 42.80 A C ANISOU 1837 CA SER A 229 6633 3685 5945 -254 -406 680 A C ATOM 1838 C SER A 229 -7.228 -4.165 2.275 1.00 39.62 A C ANISOU 1838 C SER A 229 6249 3465 5338 -321 -263 811 A C ATOM 1839 O SER A 229 -6.926 -3.690 1.180 1.00 26.88 A O ANISOU 1839 O SER A 229 4498 1871 3845 -390 -145 997 A O ATOM 1840 CB SER A 229 -7.343 -2.222 3.849 1.00 41.48 A C ANISOU 1840 CB SER A 229 6347 3453 5960 -276 -423 771 A C ATOM 1841 OG SER A 229 -8.755 -2.333 3.803 1.00 48.99 A O ANISOU 1841 OG SER A 229 7385 4532 6696 -285 -385 793 A O ATOM 1842 N LEU A 230 -8.035 -5.212 2.409 1.00 37.50 A N ANISOU 1842 N LEU A 230 6172 3316 4762 -300 -273 709 A N ATOM 1843 CA LEU A 230 -8.596 -5.894 1.250 1.00 35.73 A C ANISOU 1843 CA LEU A 230 5968 3246 4360 -341 -184 780 A C ATOM 1844 C LEU A 230 -9.987 -5.365 0.918 1.00 40.35 A C ANISOU 1844 C LEU A 230 6501 3893 4936 -374 -146 853 A C ATOM 1845 O LEU A 230 -10.888 -5.383 1.756 1.00 52.64 A O ANISOU 1845 O LEU A 230 8140 5431 6429 -369 -179 756 A O ATOM 1846 CB LEU A 230 -8.636 -7.408 1.485 1.00 36.42 A C ANISOU 1846 CB LEU A 230 6297 3381 4161 -311 -233 610 A C ATOM 1847 CG LEU A 230 -8.941 -8.304 0.280 1.00 34.41 A C ANISOU 1847 CG LEU A 230 6069 3255 3752 -333 -183 646 A C ATOM 1848 CD1 LEU A 230 -8.372 -9.700 0.490 1.00 37.53 A C ANISOU 1848 CD1 LEU A 230 6699 3629 3934 -286 -261 482 A C ATOM 1849 CD2 LEU A 230 -10.436 -8.368 -0.005 1.00 34.50 A C ANISOU 1849 CD2 LEU A 230 6083 3327 3700 -381 -153 652 A C ATOM 1850 N ARG A 231 -10.152 -4.894 -0.314 0.50 36.61 A N ANISOU 1850 N ARG A 231 5914 3479 4517 -397 -74 1029 A N ATOM 1851 CA ARG A 231 -11.428 -4.361 -0.772 0.50 34.95 A C ANISOU 1851 CA ARG A 231 5674 3303 4303 -403 -69 1104 A C ATOM 1852 C ARG A 231 -11.900 -5.073 -2.035 0.50 34.31 A C ANISOU 1852 C ARG A 231 5628 3340 4066 -393 -32 1159 A C ATOM 1853 O ARG A 231 -11.095 -5.626 -2.784 0.50 24.95 A O ANISOU 1853 O ARG A 231 4452 2212 2815 -380 17 1206 A O ATOM 1854 CB ARG A 231 -11.316 -2.857 -1.025 0.50 33.02 A C ANISOU 1854 CB ARG A 231 5316 2960 4271 -411 -56 1276 A C ATOM 1855 CG ARG A 231 -11.241 -2.016 0.238 0.50 24.62 A C ANISOU 1855 CG ARG A 231 4212 1764 3378 -405 -134 1214 A C ATOM 1856 CD ARG A 231 -12.614 -1.846 0.867 0.50 34.74 A C ANISOU 1856 CD ARG A 231 5539 3052 4608 -380 -195 1134 A C ATOM 1857 NE ARG A 231 -12.586 -0.948 2.018 0.50 42.85 A N ANISOU 1857 NE ARG A 231 6538 3952 5792 -352 -278 1087 A N ATOM 1858 CZ ARG A 231 -13.671 -0.443 2.598 0.50 50.37 A C ANISOU 1858 CZ ARG A 231 7507 4871 6758 -320 -331 1050 A C ATOM 1859 NH1 ARG A 231 -13.552 0.365 3.642 0.50 54.88 A N1+ ANISOU 1859 NH1 ARG A 231 8062 5323 7469 -276 -421 1003 A N1+ ATOM 1860 NH2 ARG A 231 -14.874 -0.743 2.130 0.50 55.29 A N ANISOU 1860 NH2 ARG A 231 8163 5570 7274 -324 -304 1056 A N ATOM 1861 N ARG A 232 -13.208 -5.057 -2.265 1.00 47.35 A N ANISOU 1861 N ARG A 232 7303 5021 5668 -388 -61 1155 A N ATOM 1862 CA ARG A 232 -13.782 -5.703 -3.439 1.00 61.39 A C ANISOU 1862 CA ARG A 232 9122 6889 7313 -359 -58 1200 A C ATOM 1863 C ARG A 232 -13.568 -4.846 -4.681 1.00 69.58 A C ANISOU 1863 C ARG A 232 10136 7922 8378 -302 -11 1415 A C ATOM 1864 O ARG A 232 -13.789 -3.635 -4.656 1.00 73.97 A O ANISOU 1864 O ARG A 232 10666 8389 9052 -295 -17 1522 A O ATOM 1865 CB ARG A 232 -15.274 -5.966 -3.230 1.00 66.90 A C ANISOU 1865 CB ARG A 232 9856 7594 7968 -374 -112 1130 A C ATOM 1866 CG ARG A 232 -15.875 -6.967 -4.203 1.00 74.12 A C ANISOU 1866 CG ARG A 232 10834 8589 8740 -352 -139 1124 A C ATOM 1867 CD ARG A 232 -17.346 -7.202 -3.904 1.00 81.56 A C ANISOU 1867 CD ARG A 232 11796 9521 9672 -390 -183 1067 A C ATOM 1868 NE ARG A 232 -17.877 -8.354 -4.627 1.00 88.26 A N ANISOU 1868 NE ARG A 232 12714 10431 10389 -391 -224 1034 A N ATOM 1869 CZ ARG A 232 -19.140 -8.761 -4.559 1.00 96.69 A C ANISOU 1869 CZ ARG A 232 13803 11498 11436 -439 -260 1003 A C ATOM 1870 NH1 ARG A 232 -20.008 -8.107 -3.799 1.00 99.75 A N1+ ANISOU 1870 NH1 ARG A 232 14144 11826 11932 -488 -239 1001 A N1+ ATOM 1871 NH2 ARG A 232 -19.537 -9.821 -5.250 1.00 98.59 A N ANISOU 1871 NH2 ARG A 232 14111 11791 11558 -438 -316 981 A N ATOM 1872 N SER A 233 -13.133 -5.480 -5.766 1.00 78.03 A N ANISOU 1872 N SER A 233 11253 9073 9322 -252 35 1480 A N ATOM 1873 CA SER A 233 -12.867 -4.770 -7.012 1.00 81.82 A C ANISOU 1873 CA SER A 233 11775 9541 9772 -183 113 1698 A C ATOM 1874 C SER A 233 -13.384 -5.544 -8.220 1.00 90.36 A C ANISOU 1874 C SER A 233 12963 10714 10655 -72 90 1725 A C ATOM 1875 O SER A 233 -14.435 -6.182 -8.158 1.00 94.78 A O ANISOU 1875 O SER A 233 13553 11307 11153 -50 -19 1608 A O ATOM 1876 CB SER A 233 -11.369 -4.503 -7.164 1.00 75.48 A C ANISOU 1876 CB SER A 233 10927 8723 9031 -221 252 1812 A C ATOM 1877 OG SER A 233 -11.092 -3.820 -8.373 1.00 74.27 A O ANISOU 1877 OG SER A 233 10857 8538 8824 -170 373 2046 A O TER HETATM 1878 PA ATP A1001 -10.988 -1.190 9.713 1.00133.52 C P HETATM 1879 PB ATP A1001 -10.243 -2.475 7.314 1.00163.06 C P HETATM 1880 PG ATP A1001 -11.632 -3.567 5.134 1.00184.28 C P HETATM 1881 C5 ATP A1001 -12.796 -0.044 11.222 1.00 61.81 C C HETATM 1882 O5 ATP A1001 -12.379 -1.207 10.517 1.00 66.32 C O HETATM 1883 C4 ATP A1001 -14.145 0.358 10.645 1.00 63.39 C C HETATM 1884 O4 ATP A1001 -15.176 -0.480 11.168 1.00 52.67 C O HETATM 1885 C3 ATP A1001 -14.522 1.791 10.984 1.00 71.22 C C HETATM 1886 O3 ATP A1001 -14.304 2.632 9.848 1.00 84.10 C O HETATM 1887 C2 ATP A1001 -15.997 1.749 11.331 1.00 59.19 C C HETATM 1888 O2 ATP A1001 -16.752 2.455 10.344 1.00 58.16 C O HETATM 1889 C1 ATP A1001 -16.377 0.276 11.321 1.00 47.05 C C HETATM 1890 N1 ATP A1001 -19.298 -3.217 13.904 1.00 22.26 C N HETATM 1891 O1A ATP A1001 -10.788 0.211 9.188 1.00138.45 C O1- HETATM 1892 O1B ATP A1001 -9.184 -1.397 7.323 1.00160.83 C O1- HETATM 1893 O1G ATP A1001 -12.608 -4.254 6.058 1.00182.91 C O HETATM 1894 C2 ATP A1001 -18.843 -3.237 12.638 1.00 14.00 C C HETATM 1895 O2A ATP A1001 -9.935 -1.830 10.583 1.00129.59 C O HETATM 1896 O2B ATP A1001 -9.843 -3.926 7.433 1.00163.87 C O HETATM 1897 O2G ATP A1001 -10.368 -4.347 4.864 1.00185.07 C O1- HETATM 1898 N3 ATP A1001 -18.093 -2.260 12.101 1.00 19.82 C N HETATM 1899 O3A ATP A1001 -11.323 -2.144 8.461 1.00110.14 C O HETATM 1900 O3B ATP A1001 -11.138 -2.295 5.987 1.00135.95 C O HETATM 1901 O3G ATP A1001 -12.267 -2.958 3.908 1.00183.42 C O HETATM 1902 C4 ATP A1001 -17.752 -1.172 12.830 1.00 18.16 C C HETATM 1903 C5 ATP A1001 -18.207 -1.077 14.225 1.00 16.74 C C HETATM 1904 C6 ATP A1001 -19.028 -2.194 14.744 1.00 15.99 C C HETATM 1905 N6 ATP A1001 -19.493 -2.189 16.016 1.00 17.54 C N HETATM 1906 N7 ATP A1001 -17.730 0.083 14.712 1.00 24.37 C N HETATM 1907 C8 ATP A1001 -17.027 0.680 13.718 1.00 32.86 C C HETATM 1908 N9 ATP A1001 -17.035 -0.072 12.601 1.00 33.02 C N HETATM 1909 N1 BTN A2001 -11.407 -2.726 22.473 1.00 16.56 D N HETATM 1910 S1 BTN A2001 -13.935 -4.365 20.688 1.00 21.44 D S HETATM 1911 C2 BTN A2001 -12.555 -4.530 19.758 1.00 24.94 D C HETATM 1912 N2 BTN A2001 -11.258 -2.512 20.308 1.00 29.68 D N HETATM 1913 C3 BTN A2001 -11.283 -1.869 21.469 1.00 27.39 D C HETATM 1914 O3 BTN A2001 -11.193 -0.471 21.614 1.00 30.08 D O HETATM 1915 C4 BTN A2001 -11.358 -3.944 20.496 1.00 27.29 D C HETATM 1916 C5 BTN A2001 -11.562 -4.080 21.993 1.00 23.34 D C HETATM 1917 C6 BTN A2001 -12.981 -4.559 22.214 1.00 22.59 D C HETATM 1918 C7 BTN A2001 -12.756 -3.868 18.395 1.00 23.36 D C HETATM 1919 C8 BTN A2001 -11.622 -4.219 17.431 1.00 18.22 D C HETATM 1920 C9 BTN A2001 -11.954 -3.765 16.008 1.00 24.06 D C HETATM 1921 C10 BTN A2001 -10.803 -4.070 15.050 1.00 24.34 D C HETATM 1922 C11 BTN A2001 -11.133 -3.534 13.674 1.00 35.19 D C HETATM 1923 O11 BTN A2001 -10.511 -2.558 13.202 1.00 29.61 D O HETATM 1924 O12 BTN A2001 -12.036 -4.055 12.983 1.00 22.13 D O HETATM 1925 O1 SO4 A2002 -25.911 4.209 23.345 1.00 93.33 E O HETATM 1926 O2 SO4 A2002 -27.206 2.265 22.862 1.00 92.06 E O HETATM 1927 O3 SO4 A2002 -25.332 2.116 24.330 1.00 89.17 E O1- HETATM 1928 O4 SO4 A2002 -27.306 3.256 25.028 1.00100.91 E O HETATM 1929 S SO4 A2002 -26.439 2.961 23.891 1.00 94.80 E S HETATM 1930 O1 SO4 A2003 -26.778 -11.486 27.206 1.00 82.45 F O HETATM 1931 O2 SO4 A2003 -28.139 -10.046 25.885 1.00 94.44 F O HETATM 1932 O3 SO4 A2003 -28.949 -10.866 27.971 1.00 85.32 F O1- HETATM 1933 O4 SO4 A2003 -27.194 -9.252 27.926 1.00 88.48 F O HETATM 1934 S SO4 A2003 -27.765 -10.412 27.248 1.00 86.92 F S HETATM 1935 O HOH A2005 -16.717 3.500 21.399 1.00 31.28 J O HETATM 1936 O HOH A2006 4.328 -11.995 19.074 1.00 41.35 J O HETATM 1937 O HOH A2007 -27.286 -8.713 7.291 1.00 27.73 J O HETATM 1938 O HOH A2008 -4.475 -29.843 20.499 1.00 31.44 J O HETATM 1939 O HOH A2009 -10.679 -12.518 2.311 1.00 19.72 J O HETATM 1940 O HOH A2010 -15.318 -9.472 -9.081 1.00 35.54 J O HETATM 1941 O HOH A2011 -8.789 4.004 23.249 1.00 43.75 J O HETATM 1942 O HOH A2012 -18.223 -0.381 35.127 1.00 38.62 J O HETATM 1943 O HOH A2013 -2.085 -12.879 -15.271 1.00 33.43 J O HETATM 1944 O HOH A2014 -22.196 -1.030 18.733 1.00 30.08 J O HETATM 1945 O HOH A2015 -25.036 -8.218 2.371 1.00 44.86 J O HETATM 1946 O HOH A2016 -29.482 -10.569 6.972 1.00 28.50 J O HETATM 1947 O HOH A2017 -23.312 -5.103 25.745 1.00 24.42 J O HETATM 1948 O HOH A2018 -30.709 -19.103 14.048 1.00 49.48 J O HETATM 1949 O HOH A2019 -18.757 -5.475 18.211 1.00 31.03 J O HETATM 1950 O HOH A2020 -6.383 -8.557 -13.419 1.00 42.12 J O HETATM 1951 O HOH A2021 -30.149 -4.806 22.887 1.00 47.18 J O HETATM 1952 O HOH A2022 -11.440 -6.453 6.953 1.00 32.99 J O HETATM 1953 O HOH A2023 -4.682 -14.572 -16.336 1.00 23.67 J O HETATM 1954 O HOH A2024 -21.656 -22.237 28.733 1.00 51.79 J O HETATM 1955 O HOH A2025 3.173 -21.779 12.269 1.00 58.15 J O HETATM 1956 O HOH A2026 -25.813 -5.382 29.828 1.00 43.04 J O HETATM 1957 O HOH A2027 -27.458 -22.632 19.721 1.00 32.65 J O HETATM 1958 O HOH A2028 2.413 -16.273 -11.561 1.00 23.91 J O HETATM 1959 O HOH A2029 -10.075 -13.184 9.749 1.00 30.91 J O HETATM 1960 O HOH A2030 -21.089 -15.219 4.640 1.00 33.30 J O HETATM 1961 O HOH A2031 5.238 -9.857 -3.463 1.00 57.74 J O HETATM 1962 O HOH A2032 -16.166 10.465 18.436 1.00 68.98 J O HETATM 1963 O HOH A2033 -1.322 -5.679 -11.272 1.00 47.78 J O HETATM 1964 O HOH A2034 -0.327 -4.950 -8.690 1.00 42.93 J O HETATM 1965 O HOH A2035 2.101 -12.263 32.685 1.00 51.24 J O HETATM 1966 O HOH A2036 7.574 -17.632 29.716 1.00 50.51 J O HETATM 1967 O HOH A2037 6.428 -23.729 23.356 1.00 42.39 J O HETATM 1968 O HOH A2038 3.099 -18.301 32.194 1.00 37.38 J O HETATM 1969 O HOH A2039 -31.371 -3.050 5.938 1.00 47.94 J O HETATM 1970 O HOH A2040 -20.850 5.229 21.066 1.00 53.95 J O HETATM 1971 O HOH A2041 6.899 -22.017 12.950 1.00 55.93 J O HETATM 1972 O HOH A2042 6.140 -5.330 36.016 1.00 43.51 J O HETATM 1973 O HOH A2043 5.497 -12.578 -9.370 1.00 39.44 J O HETATM 1974 O HOH A2044 7.066 -6.023 -7.521 1.00 40.24 J O HETATM 1975 O HOH A2045 -31.307 1.043 6.442 1.00 41.68 J O HETATM 1976 O HOH A2046 3.942 -6.352 7.941 1.00 55.28 J O HETATM 1977 O HOH A2047 5.889 -16.499 -6.856 1.00 50.50 J O HETATM 1978 O HOH A2048 -13.870 -29.720 22.547 1.00 48.71 J O HETATM 1979 O HOH A2049 -2.525 3.145 36.004 1.00 54.82 J O HETATM 1980 O HOH A2050 3.127 -14.851 8.220 1.00 51.87 J O HETATM 1981 O HOH A2051 -15.579 13.539 25.483 1.00 55.81 J O HETATM 1982 O HOH A2052 2.730 -6.000 -19.496 1.00 41.64 J O HETATM 1983 O HOH A2053 4.352 -7.873 1.538 1.00 36.98 J O HETATM 1984 O HOH A2054 -6.391 0.651 20.882 1.00 25.69 J O HETATM 1985 O HOH A2055 -6.039 -4.856 7.500 1.00 34.31 J O HETATM 1986 O HOH A2056 -19.771 -7.038 26.063 1.00 24.91 J O HETATM 1987 O HOH A2057 -14.612 -21.092 27.532 1.00 27.78 J O HETATM 1988 O HOH A2058 0.262 -17.452 25.934 1.00 41.50 J O HETATM 1989 O HOH A2059 -3.863 -5.002 13.833 1.00 35.98 J O HETATM 1990 O HOH A2060 -7.185 -26.894 7.801 1.00 28.83 J O HETATM 1991 O HOH A2061 -11.865 3.357 32.456 1.00 39.49 J O HETATM 1992 O HOH A2062 3.436 -14.613 11.725 1.00 65.57 J O HETATM 1993 O HOH A2063 -5.507 -7.790 13.805 1.00 43.04 J O HETATM 1994 O HOH A2064 -16.209 5.358 12.256 1.00 54.22 J O HETATM 1995 O HOH A2065 -23.722 -0.520 30.366 1.00 48.91 J O HETATM 1996 O HOH A2066 -17.333 -13.600 -1.223 1.00 38.69 J O HETATM 1997 O HOH A2067 -5.076 -19.450 26.781 1.00 57.27 J O HETATM 1998 O HOH A2068 -5.037 1.737 37.086 1.00 34.42 J O HETATM 1999 O HOH A2069 -28.115 -7.382 25.470 1.00 31.05 J O HETATM 2000 O HOH A2070 -0.383 -16.427 33.502 1.00 46.36 J O HETATM 2001 O HOH A2071 -15.749 -26.341 20.718 1.00 44.68 J O HETATM 2002 O HOH A2072 -23.366 -10.333 32.291 1.00 38.97 J O HETATM 2003 O HOH A2073 -19.018 -2.821 36.404 1.00 38.36 J O HETATM 2004 O HOH A2074 -17.984 12.692 24.484 1.00 37.83 J O HETATM 2005 O HOH A2075 6.206 -13.386 -4.519 1.00 50.60 J O HETATM 2006 O HOH A2076 -24.422 8.908 9.552 1.00 34.11 J O HETATM 2007 O HOH A2077 -17.272 -17.785 33.834 1.00 40.25 J O HETATM 2008 O HOH A2078 -4.974 5.593 29.604 1.00 36.90 J O HETATM 2009 O HOH A2079 -25.685 -12.921 29.140 1.00 24.65 J O HETATM 2010 O HOH A2080 -19.566 10.070 18.748 1.00 40.46 J O HETATM 2011 O HOH A2081 4.821 -15.964 -10.137 1.00 46.70 J O HETATM 2012 O HOH A2082 -7.712 -28.894 20.242 1.00 38.45 J O HETATM 2013 O HOH A2083 -21.333 -5.860 34.044 1.00 53.83 J O HETATM 2014 O HOH A2084 -15.031 -18.499 0.456 1.00 45.95 J O HETATM 2015 O HOH A2085 3.637 -18.250 -2.705 1.00 41.57 J O HETATM 2016 O HOH A2086 -29.725 -21.206 21.142 1.00 38.14 J O HETATM 2017 O HOH A2087 -14.866 9.215 21.019 1.00 40.68 J O HETATM 2018 O HOH A2088 -15.243 -3.682 0.472 1.00 37.75 J O HETATM 2019 O HOH A2089 -16.478 -15.142 35.188 1.00 38.09 J O HETATM 2020 O HOH A2090 5.468 -19.034 1.067 1.00 53.18 J O HETATM 2021 O HOH A2091 3.280 -22.936 9.781 1.00 50.47 J O HETATM 2022 O HOH A2092 3.552 -24.274 -1.407 1.00 43.72 J O HETATM 2023 O HOH A2093 -6.342 4.961 34.335 1.00 47.32 J O HETATM 2024 O HOH A2094 -13.891 1.408 34.314 1.00 53.38 J O HETATM 2025 O HOH A2095 -4.733 -11.592 -15.249 1.00 48.23 J O HETATM 2026 O HOH A2096 -20.944 4.888 33.658 1.00 36.04 J O HETATM 2027 O HOH A2097 -27.690 -0.622 20.965 1.00 37.79 J O HETATM 2028 O HOH A2098 -2.388 -8.577 11.479 1.00105.61 J O HETATM 2029 O HOH A2099 -9.016 -19.016 -7.502 1.00 43.31 J O HETATM 2030 O HOH A2100 5.308 -28.420 20.575 1.00 41.60 J O HETATM 2031 O HOH A2101 2.332 -16.072 -14.227 1.00 30.14 J O HETATM 2032 O HOH A2102 -7.429 -27.868 23.865 1.00 37.57 J O HETATM 2033 O HOH A2103 1.205 -2.578 16.898 1.00 33.24 J O CONECT 1878 1882 1891 1895 1899 CONECT 1879 1892 1896 1899 1900 CONECT 1880 1893 1897 1900 1901 CONECT 1881 1883 1882 CONECT 1882 1878 1881 CONECT 1883 1881 1884 1885 CONECT 1884 1883 1889 CONECT 1885 1883 1886 1887 CONECT 1886 1885 CONECT 1887 1885 1888 1889 CONECT 1888 1887 CONECT 1889 1884 1887 1908 CONECT 1890 1894 1904 CONECT 1891 1878 CONECT 1892 1879 CONECT 1893 1880 CONECT 1894 1890 1898 CONECT 1895 1878 CONECT 1896 1879 CONECT 1897 1880 CONECT 1898 1894 1902 CONECT 1899 1878 1879 CONECT 1900 1879 1880 CONECT 1901 1880 CONECT 1902 1898 1903 1908 CONECT 1903 1902 1904 1906 CONECT 1904 1903 1890 1905 CONECT 1905 1904 CONECT 1906 1903 1907 CONECT 1907 1906 1908 CONECT 1908 1889 1902 1907 CONECT 1909 1913 1916 CONECT 1910 1917 1911 CONECT 1911 1910 1915 1918 CONECT 1912 1915 1913 CONECT 1913 1909 1912 1914 CONECT 1914 1913 CONECT 1915 1911 1912 1916 CONECT 1916 1909 1915 1917 CONECT 1917 1910 1916 CONECT 1918 1911 1919 CONECT 1919 1918 1920 CONECT 1920 1919 1921 CONECT 1921 1920 1922 CONECT 1922 1921 1923 1924 CONECT 1923 1922 CONECT 1924 1922 CONECT 1925 1929 CONECT 1926 1929 CONECT 1927 1929 CONECT 1928 1929 CONECT 1929 1925 1926 1927 1928 CONECT 1930 1934 CONECT 1931 1934 CONECT 1932 1934 CONECT 1933 1934 CONECT 1934 1930 1931 1932 1933 END