TITLE hA3AR-cmp9 REMARK 4 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 888 REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC) ATOM 1 N ALA A 7 -21.922 16.443 19.853 1.00 96.89 N ANISOU 1 N ALA A 7 14529 11500 10785 577 -992 87 ATOM 2 CA ALA A 7 -20.985 16.121 20.963 1.00 96.11 C ANISOU 2 CA ALA A 7 14372 11400 10743 541 -948 35 ATOM 3 C ALA A 7 -19.561 15.735 20.446 1.00 94.30 C ANISOU 3 C ALA A 7 14159 11154 10516 511 -857 59 ATOM 4 O ALA A 7 -18.604 15.754 21.224 1.00 94.66 O ANISOU 4 O ALA A 7 14157 11191 10618 492 -812 45 ATOM 5 CB ALA A 7 -21.563 15.010 21.853 1.00 0.00 C ATOM 6 N LEU A 8 -19.450 15.371 19.162 1.00 92.50 N ANISOU 6 N LEU A 8 13997 10926 10222 508 -829 98 ATOM 7 CA LEU A 8 -18.199 15.072 18.472 1.00 90.40 C ANISOU 7 CA LEU A 8 13749 10647 9950 482 -746 124 ATOM 8 C LEU A 8 -17.374 16.358 18.272 1.00 89.01 C ANISOU 8 C LEU A 8 13602 10475 9740 465 -725 100 ATOM 9 O LEU A 8 -17.945 17.418 18.010 1.00 88.13 O ANISOU 9 O LEU A 8 13530 10379 9573 479 -764 92 ATOM 10 CB LEU A 8 -18.533 14.376 17.132 1.00 0.00 C ATOM 11 CG LEU A 8 -17.332 13.746 16.391 1.00 0.00 C ATOM 12 CD1 LEU A 8 -16.646 12.641 17.222 1.00 0.00 C ATOM 13 CD2 LEU A 8 -17.763 13.234 15.002 1.00 0.00 C ATOM 14 N SER A 9 -16.048 16.243 18.389 1.00 87.07 N ANISOU 14 N SER A 9 13338 10214 9528 435 -662 87 ATOM 15 CA SER A 9 -15.118 17.355 18.185 1.00 85.42 C ANISOU 15 CA SER A 9 13151 9997 9306 416 -638 55 ATOM 16 C SER A 9 -15.000 17.733 16.705 1.00 83.35 C ANISOU 16 C SER A 9 12954 9738 8975 430 -597 97 ATOM 17 O SER A 9 -14.980 16.860 15.826 1.00 83.25 O ANISOU 17 O SER A 9 12953 9728 8950 435 -554 154 ATOM 18 CB SER A 9 -13.738 16.973 18.743 1.00 85.60 C ANISOU 18 CB SER A 9 13129 9997 9396 379 -586 32 ATOM 19 OG SER A 9 -12.774 17.983 18.517 1.00 86.72 O ANISOU 19 OG SER A 9 13296 10121 9531 361 -561 2 ATOM 20 N LEU A 10 -14.796 19.031 16.438 1.00 81.22 N ANISOU 20 N LEU A 10 12725 9474 8661 435 -608 66 ATOM 21 CA LEU A 10 -14.493 19.563 15.110 1.00 79.61 C ANISOU 21 CA LEU A 10 12580 9278 8388 452 -567 96 ATOM 22 C LEU A 10 -13.255 18.901 14.467 1.00 77.12 C ANISOU 22 C LEU A 10 12261 8943 8096 440 -483 129 ATOM 23 O LEU A 10 -13.245 18.708 13.252 1.00 76.31 O ANISOU 23 O LEU A 10 12190 8856 7947 456 -443 183 ATOM 24 CB LEU A 10 -14.366 21.102 15.187 1.00 0.00 C ATOM 25 CG LEU A 10 -14.132 21.830 13.839 1.00 0.00 C ATOM 26 CD1 LEU A 10 -15.232 21.524 12.798 1.00 0.00 C ATOM 27 CD2 LEU A 10 -13.948 23.346 14.059 1.00 0.00 C ATOM 28 N ALA A 11 -12.271 18.501 15.285 1.00 74.92 N ANISOU 28 N ALA A 11 11942 8635 7887 410 -459 99 ATOM 29 CA ALA A 11 -11.097 17.747 14.842 1.00 73.17 C ANISOU 29 CA ALA A 11 11709 8394 7697 395 -386 132 ATOM 30 C ALA A 11 -11.471 16.354 14.307 1.00 71.17 C ANISOU 30 C ALA A 11 11435 8156 7449 397 -366 197 ATOM 31 O ALA A 11 -11.061 15.992 13.203 1.00 69.73 O ANISOU 31 O ALA A 11 11268 7978 7246 402 -314 249 ATOM 32 CB ALA A 11 -10.092 17.636 15.998 1.00 0.00 C ATOM 33 N ASN A 12 -12.292 15.623 15.074 1.00 70.48 N ANISOU 33 N ASN A 12 11313 8075 7390 393 -409 191 ATOM 34 CA ASN A 12 -12.804 14.299 14.703 1.00 69.72 C ANISOU 34 CA ASN A 12 11202 7988 7298 395 -399 243 ATOM 35 C ASN A 12 -13.745 14.393 13.502 1.00 68.54 C ANISOU 35 C ASN A 12 11100 7861 7079 419 -404 300 ATOM 36 O ASN A 12 -13.608 13.585 12.590 1.00 68.68 O ANISOU 36 O ASN A 12 11125 7886 7085 415 -364 357 ATOM 37 CB ASN A 12 -13.515 13.606 15.883 1.00 0.00 C ATOM 38 CG ASN A 12 -12.556 13.140 16.974 1.00 0.00 C ATOM 39 OD1 ASN A 12 -12.127 13.940 17.799 1.00 0.00 O ATOM 40 ND2 ASN A 12 -12.217 11.856 17.013 1.00 0.00 N ATOM 41 N VAL A 13 -14.632 15.399 13.482 1.00 67.10 N ANISOU 41 N VAL A 13 10950 7694 6849 441 -453 285 ATOM 42 CA VAL A 13 -15.490 15.715 12.341 1.00 66.08 C ANISOU 42 CA VAL A 13 10870 7591 6646 462 -457 337 ATOM 43 C VAL A 13 -14.660 15.984 11.071 1.00 65.01 C ANISOU 43 C VAL A 13 10760 7465 6475 464 -389 370 ATOM 44 O VAL A 13 -14.951 15.379 10.041 1.00 64.12 O ANISOU 44 O VAL A 13 10665 7372 6324 468 -365 434 ATOM 45 CB VAL A 13 -16.431 16.925 12.628 1.00 0.00 C ATOM 46 CG1 VAL A 13 -17.131 17.539 11.395 1.00 0.00 C ATOM 47 CG2 VAL A 13 -17.499 16.568 13.677 1.00 0.00 C ATOM 48 N THR A 14 -13.617 16.821 11.170 1.00 64.86 N ANISOU 48 N THR A 14 10742 7431 6470 461 -359 327 ATOM 49 CA THR A 14 -12.696 17.108 10.069 1.00 64.26 C ANISOU 49 CA THR A 14 10686 7358 6370 469 -291 353 ATOM 50 C THR A 14 -11.959 15.846 9.574 1.00 62.67 C ANISOU 50 C THR A 14 10455 7151 6203 451 -238 406 ATOM 51 O THR A 14 -11.908 15.633 8.365 1.00 62.12 O ANISOU 51 O THR A 14 10399 7104 6098 460 -197 464 ATOM 52 CB THR A 14 -11.655 18.198 10.437 1.00 0.00 C ATOM 53 OG1 THR A 14 -12.335 19.380 10.819 1.00 0.00 O ATOM 54 CG2 THR A 14 -10.678 18.585 9.313 1.00 0.00 C ATOM 55 N TYR A 15 -11.451 15.017 10.499 1.00 61.49 N ANISOU 55 N TYR A 15 10264 6977 6123 424 -238 386 ATOM 56 CA TYR A 15 -10.837 13.719 10.229 1.00 60.86 C ANISOU 56 CA TYR A 15 10154 6894 6075 403 -196 433 ATOM 57 C TYR A 15 -11.814 12.793 9.490 1.00 60.47 C ANISOU 57 C TYR A 15 10112 6871 5990 405 -205 497 ATOM 58 O TYR A 15 -11.494 12.325 8.398 1.00 60.50 O ANISOU 58 O TYR A 15 10122 6892 5971 404 -163 556 ATOM 59 CB TYR A 15 -10.328 13.091 11.548 1.00 60.65 C ANISOU 59 CB TYR A 15 10080 6844 6120 375 -204 398 ATOM 60 CG TYR A 15 -9.967 11.617 11.450 1.00 60.24 C ANISOU 60 CG TYR A 15 10000 6796 6092 353 -174 443 ATOM 61 CD1 TYR A 15 -8.849 11.213 10.691 1.00 59.92 C ANISOU 61 CD1 TYR A 15 9951 6753 6060 341 -114 480 ATOM 62 CD2 TYR A 15 -10.806 10.644 12.036 1.00 60.17 C ANISOU 62 CD2 TYR A 15 9973 6791 6096 347 -208 448 ATOM 63 CE1 TYR A 15 -8.599 9.844 10.482 1.00 59.55 C ANISOU 63 CE1 TYR A 15 9879 6714 6030 319 -89 521 ATOM 64 CE2 TYR A 15 -10.558 9.276 11.820 1.00 59.52 C ANISOU 64 CE2 TYR A 15 9869 6713 6031 327 -182 484 ATOM 65 CZ TYR A 15 -9.467 8.878 11.028 1.00 59.23 C ANISOU 65 CZ TYR A 15 9825 6680 5999 311 -123 520 ATOM 66 OH TYR A 15 -9.278 7.560 10.748 1.00 58.85 O ANISOU 66 OH TYR A 15 9757 6639 5963 288 -101 556 ATOM 67 N ILE A 16 -13.019 12.594 10.047 1.00 60.14 N ANISOU 67 N ILE A 16 10073 6832 5946 409 -264 485 ATOM 68 CA ILE A 16 -14.076 11.759 9.448 1.00 59.76 C ANISOU 68 CA ILE A 16 10038 6798 5867 409 -285 541 ATOM 69 C ILE A 16 -14.454 12.254 8.042 1.00 60.04 C ANISOU 69 C ILE A 16 10112 6866 5831 423 -266 596 ATOM 70 O ILE A 16 -14.576 11.450 7.111 1.00 59.72 O ANISOU 70 O ILE A 16 10075 6843 5773 411 -243 660 ATOM 71 CB ILE A 16 -15.330 11.684 10.359 1.00 59.79 C ANISOU 71 CB ILE A 16 10043 6793 5879 419 -357 515 ATOM 72 CG1 ILE A 16 -15.011 10.891 11.637 1.00 59.60 C ANISOU 72 CG1 ILE A 16 9973 6745 5927 405 -368 472 ATOM 73 CG2 ILE A 16 -16.517 11.037 9.637 1.00 59.50 C ANISOU 73 CG2 ILE A 16 10034 6768 5806 421 -383 576 ATOM 74 CD1 ILE A 16 -15.933 11.209 12.797 1.00 59.91 C ANISOU 74 CD1 ILE A 16 10002 6775 5984 422 -437 424 ATOM 75 N THR A 17 -14.609 13.583 7.908 1.00 60.53 N ANISOU 75 N THR A 17 10203 6942 5854 446 -275 570 ATOM 76 CA THR A 17 -14.926 14.285 6.663 1.00 60.77 C ANISOU 76 CA THR A 17 10268 7010 5810 464 -253 615 ATOM 77 C THR A 17 -13.817 14.143 5.600 1.00 60.67 C ANISOU 77 C THR A 17 10246 7012 5791 463 -180 654 ATOM 78 O THR A 17 -14.126 13.840 4.450 1.00 60.53 O ANISOU 78 O THR A 17 10237 7028 5732 462 -157 722 ATOM 79 CB THR A 17 -15.208 15.796 6.885 1.00 0.00 C ATOM 80 OG1 THR A 17 -16.280 15.940 7.798 1.00 0.00 O ATOM 81 CG2 THR A 17 -15.589 16.595 5.625 1.00 0.00 C ATOM 82 N MET A 18 -12.549 14.320 6.002 1.00 60.80 N ANISOU 82 N MET A 18 10246 7004 5852 463 -145 615 ATOM 83 CA MET A 18 -11.365 14.106 5.170 1.00 60.76 C ANISOU 83 CA MET A 18 10229 7007 5851 466 -77 651 ATOM 84 C MET A 18 -11.303 12.659 4.665 1.00 60.27 C ANISOU 84 C MET A 18 10137 6952 5810 436 -59 713 ATOM 85 O MET A 18 -11.174 12.441 3.461 1.00 60.26 O ANISOU 85 O MET A 18 10132 6983 5779 438 -20 777 ATOM 86 CB MET A 18 -10.100 14.523 5.958 1.00 0.00 C ATOM 87 CG MET A 18 -8.749 14.076 5.366 1.00 0.00 C ATOM 88 SD MET A 18 -7.304 14.682 6.277 1.00 0.00 S ATOM 89 CE MET A 18 -7.261 16.407 5.723 1.00 0.00 C ATOM 90 N GLU A 19 -11.447 11.716 5.600 1.00 60.02 N ANISOU 90 N GLU A 19 10081 6894 5828 410 -88 695 ATOM 91 CA GLU A 19 -11.442 10.265 5.321 1.00 59.55 C ANISOU 91 CA GLU A 19 9999 6840 5786 380 -79 746 ATOM 92 C GLU A 19 -12.561 9.864 4.357 1.00 58.91 C ANISOU 92 C GLU A 19 9938 6791 5654 375 -96 810 ATOM 93 O GLU A 19 -12.309 9.205 3.328 1.00 58.47 O ANISOU 93 O GLU A 19 9873 6762 5582 360 -64 874 ATOM 94 CB GLU A 19 -11.568 9.462 6.619 1.00 59.87 C ANISOU 94 CB GLU A 19 10016 6848 5881 358 -113 706 ATOM 95 CG GLU A 19 -10.299 9.427 7.466 1.00 60.13 C ANISOU 95 CG GLU A 19 10019 6856 5971 348 -85 663 ATOM 96 CD GLU A 19 -9.319 8.341 7.049 1.00 60.27 C ANISOU 96 CD GLU A 19 10009 6879 6010 322 -40 706 ATOM 97 OE1 GLU A 19 -9.130 8.121 5.837 1.00 60.35 O ANISOU 97 OE1 GLU A 19 10025 6916 5988 322 -9 767 ATOM 98 OE2 GLU A 19 -8.730 7.699 7.946 1.00 60.85 O1- ANISOU 98 OE2 GLU A 19 10054 6934 6131 301 -34 680 ATOM 99 N ILE A 20 -13.807 10.287 4.625 1.00 58.77 N ANISOU 99 N ILE A 20 9947 6772 5611 385 -149 795 ATOM 100 CA ILE A 20 -14.918 9.964 3.725 1.00 58.94 C ANISOU 100 CA ILE A 20 9992 6820 5580 380 -173 855 ATOM 101 C ILE A 20 -14.792 10.682 2.362 1.00 59.35 C ANISOU 101 C ILE A 20 10055 6920 5574 391 -126 910 ATOM 102 O ILE A 20 -15.112 10.058 1.359 1.00 59.09 O ANISOU 102 O ILE A 20 10020 6915 5514 371 -117 980 ATOM 103 CB ILE A 20 -16.328 10.171 4.352 1.00 0.00 C ATOM 104 CG1 ILE A 20 -17.424 9.394 3.585 1.00 0.00 C ATOM 105 CG2 ILE A 20 -16.739 11.642 4.510 1.00 0.00 C ATOM 106 CD1 ILE A 20 -18.762 9.309 4.333 1.00 0.00 C ATOM 107 N PHE A 21 -14.240 11.907 2.312 1.00 60.04 N ANISOU 107 N PHE A 21 10149 7017 5643 423 -98 876 ATOM 108 CA PHE A 21 -13.834 12.576 1.066 1.00 60.66 C ANISOU 108 CA PHE A 21 10235 7145 5668 444 -48 920 ATOM 109 C PHE A 21 -12.840 11.748 0.230 1.00 60.48 C ANISOU 109 C PHE A 21 10176 7136 5665 430 7 970 ATOM 110 O PHE A 21 -13.089 11.493 -0.949 1.00 60.35 O ANISOU 110 O PHE A 21 10152 7166 5610 422 32 1042 ATOM 111 CB PHE A 21 -13.363 14.033 1.331 1.00 0.00 C ATOM 112 CG PHE A 21 -12.371 14.622 0.336 1.00 0.00 C ATOM 113 CD1 PHE A 21 -12.789 14.991 -0.960 1.00 0.00 C ATOM 114 CD2 PHE A 21 -10.990 14.616 0.635 1.00 0.00 C ATOM 115 CE1 PHE A 21 -11.848 15.366 -1.910 1.00 0.00 C ATOM 116 CE2 PHE A 21 -10.066 14.993 -0.329 1.00 0.00 C ATOM 117 CZ PHE A 21 -10.494 15.366 -1.597 1.00 0.00 C ATOM 118 N ILE A 22 -11.754 11.309 0.877 1.00 60.92 N ANISOU 118 N ILE A 22 10208 7156 5782 425 26 935 ATOM 119 CA ILE A 22 -10.708 10.473 0.260 1.00 61.11 C ANISOU 119 CA ILE A 22 10196 7190 5830 409 73 981 ATOM 120 C ILE A 22 -11.291 9.144 -0.230 1.00 60.92 C ANISOU 120 C ILE A 22 10159 7186 5801 367 57 1047 ATOM 121 O ILE A 22 -11.029 8.732 -1.363 1.00 60.70 O ANISOU 121 O ILE A 22 10111 7199 5751 358 91 1115 ATOM 122 CB ILE A 22 -9.521 10.202 1.223 1.00 60.76 C ANISOU 122 CB ILE A 22 10131 7101 5854 402 86 934 ATOM 123 CG1 ILE A 22 -8.741 11.494 1.492 1.00 61.37 C ANISOU 123 CG1 ILE A 22 10221 7156 5938 441 110 879 ATOM 124 CG2 ILE A 22 -8.568 9.158 0.645 1.00 60.23 C ANISOU 124 CG2 ILE A 22 10028 7046 5810 380 125 989 ATOM 125 CD1 ILE A 22 -7.983 11.488 2.807 1.00 61.45 C ANISOU 125 CD1 ILE A 22 10222 7113 6012 429 100 815 ATOM 126 N GLY A 23 -12.162 8.533 0.584 1.00 61.10 N ANISOU 126 N GLY A 23 10190 7178 5845 342 5 1026 ATOM 127 CA GLY A 23 -12.819 7.265 0.283 1.00 61.01 C ANISOU 127 CA GLY A 23 10176 7176 5827 301 -18 1081 ATOM 128 C GLY A 23 -13.784 7.462 -0.887 1.00 61.38 C ANISOU 128 C GLY A 23 10241 7269 5811 297 -23 1147 ATOM 129 O GLY A 23 -13.813 6.637 -1.801 1.00 60.89 O ANISOU 129 O GLY A 23 10163 7235 5734 265 -11 1216 ATOM 130 N LEU A 24 -14.501 8.596 -0.892 1.00 62.10 N ANISOU 130 N LEU A 24 10363 7368 5863 326 -41 1128 ATOM 131 CA LEU A 24 -15.441 8.970 -1.964 1.00 62.98 C ANISOU 131 CA LEU A 24 10492 7528 5908 324 -44 1190 ATOM 132 C LEU A 24 -14.765 9.295 -3.299 1.00 63.64 C ANISOU 132 C LEU A 24 10552 7672 5955 336 20 1245 ATOM 133 O LEU A 24 -15.384 9.123 -4.350 1.00 63.90 O ANISOU 133 O LEU A 24 10584 7752 5943 317 25 1317 ATOM 134 CB LEU A 24 -16.337 10.155 -1.557 1.00 63.28 C ANISOU 134 CB LEU A 24 10570 7565 5906 355 -77 1153 ATOM 135 CG LEU A 24 -17.557 9.860 -0.678 1.00 63.40 C ANISOU 135 CG LEU A 24 10615 7542 5931 342 -150 1135 ATOM 136 CD1 LEU A 24 -18.165 11.163 -0.173 1.00 63.56 C ANISOU 136 CD1 LEU A 24 10669 7564 5917 379 -179 1088 ATOM 137 CD2 LEU A 24 -18.596 9.020 -1.414 1.00 63.44 C ANISOU 137 CD2 LEU A 24 10632 7560 5910 302 -177 1214 ATOM 138 N CYS A 25 -13.500 9.719 -3.249 1.00 63.99 N ANISOU 138 N CYS A 25 10575 7715 6020 368 68 1213 ATOM 139 CA CYS A 25 -12.655 9.898 -4.421 1.00 64.19 C ANISOU 139 CA CYS A 25 10570 7794 6022 383 131 1265 ATOM 140 C CYS A 25 -12.084 8.536 -4.878 1.00 63.87 C ANISOU 140 C CYS A 25 10488 7760 6017 344 147 1318 ATOM 141 O CYS A 25 -12.222 8.164 -6.046 1.00 63.89 O ANISOU 141 O CYS A 25 10464 7819 5992 333 177 1392 ATOM 142 CB CYS A 25 -11.563 10.953 -4.137 1.00 0.00 C ATOM 143 SG CYS A 25 -10.713 11.479 -5.654 1.00 0.00 S ATOM 144 N ALA A 26 -11.475 7.802 -3.933 1.00 63.45 N ANISOU 144 N ALA A 26 10430 7656 6022 322 127 1281 ATOM 145 CA ALA A 26 -10.732 6.567 -4.167 1.00 63.10 C ANISOU 145 CA ALA A 26 10348 7615 6009 285 140 1322 ATOM 146 C ALA A 26 -11.561 5.410 -4.732 1.00 63.04 C ANISOU 146 C ALA A 26 10335 7633 5982 231 113 1392 ATOM 147 O ALA A 26 -11.073 4.713 -5.621 1.00 63.36 O ANISOU 147 O ALA A 26 10342 7721 6009 212 141 1460 ATOM 148 CB ALA A 26 -10.025 6.126 -2.874 1.00 0.00 C ATOM 149 N ILE A 27 -12.774 5.185 -4.211 1.00 62.62 N ANISOU 149 N ILE A 27 10315 7548 5928 206 57 1376 ATOM 150 CA ILE A 27 -13.563 4.024 -4.622 1.00 62.13 C ANISOU 150 CA ILE A 27 10256 7492 5858 148 22 1431 ATOM 151 C ILE A 27 -14.003 4.110 -6.101 1.00 62.86 C ANISOU 151 C ILE A 27 10338 7650 5896 130 38 1520 ATOM 152 O ILE A 27 -13.694 3.205 -6.875 1.00 62.98 O ANISOU 152 O ILE A 27 10324 7695 5909 87 46 1582 ATOM 153 CB ILE A 27 -14.771 3.752 -3.679 1.00 0.00 C ATOM 154 CG1 ILE A 27 -15.408 2.369 -3.954 1.00 0.00 C ATOM 155 CG2 ILE A 27 -15.851 4.858 -3.663 1.00 0.00 C ATOM 156 CD1 ILE A 27 -16.434 1.945 -2.897 1.00 0.00 C ATOM 157 N VAL A 28 -14.645 5.223 -6.480 1.00 63.61 N ANISOU 157 N VAL A 28 10453 7772 5944 160 43 1527 ATOM 158 CA VAL A 28 -15.257 5.422 -7.793 1.00 63.98 C ANISOU 158 CA VAL A 28 10483 7888 5935 142 63 1614 ATOM 159 C VAL A 28 -14.218 5.367 -8.931 1.00 64.15 C ANISOU 159 C VAL A 28 10450 7974 5950 153 126 1662 ATOM 160 O VAL A 28 -14.437 4.687 -9.930 1.00 64.02 O ANISOU 160 O VAL A 28 10403 8006 5913 111 133 1742 ATOM 161 CB VAL A 28 -16.007 6.786 -7.860 1.00 0.00 C ATOM 162 CG1 VAL A 28 -16.692 7.059 -9.217 1.00 0.00 C ATOM 163 CG2 VAL A 28 -17.043 6.923 -6.726 1.00 0.00 C ATOM 164 N GLY A 29 -13.087 6.047 -8.719 1.00 64.13 N ANISOU 164 N GLY A 29 10433 7967 5965 208 170 1614 ATOM 165 CA GLY A 29 -11.957 6.137 -9.646 1.00 64.26 C ANISOU 165 CA GLY A 29 10397 8037 5981 231 231 1654 ATOM 166 C GLY A 29 -11.371 4.795 -10.027 1.00 63.93 C ANISOU 166 C GLY A 29 10315 8006 5969 181 229 1705 ATOM 167 O GLY A 29 -11.198 4.499 -11.209 1.00 63.37 O ANISOU 167 O GLY A 29 10199 8002 5874 164 255 1783 ATOM 168 N ASN A 30 -11.093 3.974 -9.016 1.00 64.35 N ANISOU 168 N ASN A 30 10380 7998 6070 155 196 1661 ATOM 169 CA ASN A 30 -10.505 2.649 -9.232 1.00 65.12 C ANISOU 169 CA ASN A 30 10445 8101 6194 106 190 1699 ATOM 170 C ASN A 30 -11.504 1.650 -9.819 1.00 65.97 C ANISOU 170 C ASN A 30 10555 8227 6280 34 149 1762 ATOM 171 O ASN A 30 -11.129 0.825 -10.665 1.00 66.49 O ANISOU 171 O ASN A 30 10581 8338 6342 -5 157 1827 ATOM 172 CB ASN A 30 -9.880 2.120 -7.941 1.00 64.72 C ANISOU 172 CB ASN A 30 10409 7983 6196 103 173 1630 ATOM 173 CG ASN A 30 -8.628 2.888 -7.547 1.00 64.70 C ANISOU 173 CG ASN A 30 10392 7967 6221 161 217 1587 ATOM 174 OD1 ASN A 30 -7.605 2.822 -8.234 1.00 64.59 O ANISOU 174 OD1 ASN A 30 10337 7990 6212 175 258 1627 ATOM 175 ND2 ASN A 30 -8.702 3.622 -6.443 1.00 64.65 N ANISOU 175 ND2 ASN A 30 10421 7908 6235 195 208 1507 ATOM 176 N VAL A 31 -12.771 1.733 -9.398 1.00 67.11 N ANISOU 176 N VAL A 31 10748 8339 6411 17 103 1744 ATOM 177 CA VAL A 31 -13.848 0.978 -10.066 1.00 67.96 C ANISOU 177 CA VAL A 31 10864 8462 6492 -48 64 1809 ATOM 178 C VAL A 31 -13.894 1.356 -11.556 1.00 69.40 C ANISOU 178 C VAL A 31 11004 8735 6628 -54 102 1898 ATOM 179 O VAL A 31 -14.019 0.483 -12.414 1.00 69.77 O ANISOU 179 O VAL A 31 11023 8820 6665 -114 93 1970 ATOM 180 CB VAL A 31 -15.233 1.198 -9.398 1.00 67.72 C ANISOU 180 CB VAL A 31 10896 8381 6453 -56 10 1779 ATOM 181 CG1 VAL A 31 -16.367 0.632 -10.256 1.00 68.21 C ANISOU 181 CG1 VAL A 31 10968 8464 6483 -121 -23 1857 ATOM 182 CG2 VAL A 31 -15.274 0.559 -8.016 1.00 67.13 C ANISOU 182 CG2 VAL A 31 10855 8222 6427 -60 -31 1701 ATOM 183 N LEU A 32 -13.772 2.651 -11.846 1.00 70.47 N ANISOU 183 N LEU A 32 11133 8906 6734 6 146 1891 ATOM 184 CA LEU A 32 -13.729 3.152 -13.223 1.00 71.61 C ANISOU 184 CA LEU A 32 11233 9144 6832 14 192 1968 ATOM 185 C LEU A 32 -12.473 2.674 -13.972 1.00 72.14 C ANISOU 185 C LEU A 32 11231 9261 6916 16 235 2012 ATOM 186 O LEU A 32 -12.548 2.365 -15.165 1.00 73.56 O ANISOU 186 O LEU A 32 11363 9515 7068 -16 251 2097 ATOM 187 CB LEU A 32 -13.814 4.685 -13.244 1.00 71.86 C ANISOU 187 CB LEU A 32 11279 9197 6828 89 231 1936 ATOM 188 CG LEU A 32 -14.285 5.338 -14.540 1.00 72.74 C ANISOU 188 CG LEU A 32 11360 9401 6874 95 269 2010 ATOM 189 CD1 LEU A 32 -15.791 5.166 -14.724 1.00 73.39 C ANISOU 189 CD1 LEU A 32 11479 9486 6918 39 222 2053 ATOM 190 CD2 LEU A 32 -13.910 6.814 -14.556 1.00 72.88 C ANISOU 190 CD2 LEU A 32 11383 9442 6863 182 322 1965 ATOM 191 N VAL A 33 -11.330 2.615 -13.278 1.00 71.55 N ANISOU 191 N VAL A 33 11150 9148 6885 51 251 1957 ATOM 192 CA VAL A 33 -10.104 2.022 -13.845 1.00 71.74 C ANISOU 192 CA VAL A 33 11113 9210 6932 49 282 1997 ATOM 193 C VAL A 33 -10.308 0.545 -14.188 1.00 72.04 C ANISOU 193 C VAL A 33 11133 9258 6977 -37 240 2052 ATOM 194 O VAL A 33 -9.940 0.111 -15.287 1.00 71.91 O ANISOU 194 O VAL A 33 11059 9314 6949 -62 259 2131 ATOM 195 CB VAL A 33 -8.877 2.185 -12.904 1.00 71.44 C ANISOU 195 CB VAL A 33 11081 9119 6942 97 300 1927 ATOM 196 CG1 VAL A 33 -7.700 1.319 -13.343 1.00 71.39 C ANISOU 196 CG1 VAL A 33 11020 9141 6962 81 317 1971 ATOM 197 CG2 VAL A 33 -8.437 3.640 -12.852 1.00 71.85 C ANISOU 197 CG2 VAL A 33 11139 9174 6987 184 350 1886 ATOM 198 N ILE A 34 -10.884 -0.217 -13.254 1.00 72.68 N ANISOU 198 N ILE A 34 11264 9270 7081 -82 184 2010 ATOM 199 CA ILE A 34 -11.142 -1.654 -13.476 1.00 73.04 C ANISOU 199 CA ILE A 34 11304 9314 7133 -167 139 2050 ATOM 200 C ILE A 34 -12.155 -1.854 -14.613 1.00 74.30 C ANISOU 200 C ILE A 34 11450 9528 7251 -224 123 2135 ATOM 201 O ILE A 34 -11.988 -2.752 -15.444 1.00 75.19 O ANISOU 201 O ILE A 34 11522 9687 7358 -283 113 2204 ATOM 202 CB ILE A 34 -11.631 -2.372 -12.190 1.00 72.30 C ANISOU 202 CB ILE A 34 11271 9129 7069 -196 83 1979 ATOM 203 CG1 ILE A 34 -10.541 -2.355 -11.115 1.00 71.69 C ANISOU 203 CG1 ILE A 34 11197 9006 7034 -153 100 1904 ATOM 204 CG2 ILE A 34 -12.015 -3.823 -12.480 1.00 72.55 C ANISOU 204 CG2 ILE A 34 11305 9156 7102 -284 34 2017 ATOM 205 CD1 ILE A 34 -11.064 -2.537 -9.708 1.00 71.32 C ANISOU 205 CD1 ILE A 34 11210 8874 7015 -151 60 1818 ATOM 206 N CYS A 35 -13.221 -1.039 -14.640 1.00 74.87 N ANISOU 206 N CYS A 35 11556 9596 7293 -208 118 2133 ATOM 207 CA CYS A 35 -14.262 -1.088 -15.670 1.00 75.64 C ANISOU 207 CA CYS A 35 11641 9753 7346 -254 111 2217 ATOM 208 C CYS A 35 -13.709 -0.752 -17.063 1.00 75.64 C ANISOU 208 C CYS A 35 11559 9859 7322 -243 168 2297 ATOM 209 O CYS A 35 -14.081 -1.419 -18.031 1.00 75.79 O ANISOU 209 O CYS A 35 11537 9931 7328 -311 155 2378 ATOM 210 CB CYS A 35 -15.460 -0.174 -15.351 1.00 0.00 C ATOM 211 SG CYS A 35 -16.469 -0.910 -14.030 1.00 0.00 S ATOM 212 N VAL A 36 -12.807 0.237 -17.143 1.00 75.72 N ANISOU 212 N VAL A 36 11544 9897 7328 -157 228 2271 ATOM 213 CA VAL A 36 -12.164 0.630 -18.390 1.00 76.48 C ANISOU 213 CA VAL A 36 11563 10094 7401 -126 289 2338 ATOM 214 C VAL A 36 -11.348 -0.495 -19.015 1.00 76.80 C ANISOU 214 C VAL A 36 11537 10179 7461 -171 288 2399 ATOM 215 O VAL A 36 -11.522 -0.744 -20.211 1.00 77.53 O ANISOU 215 O VAL A 36 11565 10365 7529 -192 311 2485 ATOM 216 CB VAL A 36 -11.185 1.820 -18.227 1.00 0.00 C ATOM 217 CG1 VAL A 36 -10.173 2.026 -19.379 1.00 0.00 C ATOM 218 CG2 VAL A 36 -11.896 3.123 -17.891 1.00 0.00 C ATOM 219 N VAL A 37 -10.467 -1.121 -18.215 1.00 76.66 N ANISOU 219 N VAL A 37 11535 10103 7489 -186 261 2355 ATOM 220 CA VAL A 37 -9.652 -2.216 -18.755 1.00 76.84 C ANISOU 220 CA VAL A 37 11501 10164 7528 -231 253 2408 ATOM 221 C VAL A 37 -10.534 -3.349 -19.285 1.00 77.44 C ANISOU 221 C VAL A 37 11576 10258 7590 -340 196 2470 ATOM 222 O VAL A 37 -10.218 -3.933 -20.321 1.00 77.23 O ANISOU 222 O VAL A 37 11483 10307 7553 -383 199 2551 ATOM 223 CB VAL A 37 -8.642 -2.753 -17.711 1.00 76.12 C ANISOU 223 CB VAL A 37 11430 10008 7484 -215 241 2342 ATOM 224 CG1 VAL A 37 -7.883 -3.972 -18.235 1.00 76.23 C ANISOU 224 CG1 VAL A 37 11392 10063 7509 -270 225 2398 ATOM 225 CG2 VAL A 37 -7.656 -1.659 -17.316 1.00 75.96 C ANISOU 225 CG2 VAL A 37 11404 9975 7481 -113 298 2293 ATOM 226 N LYS A 38 -11.631 -3.652 -18.587 1.00 78.68 N ANISOU 226 N LYS A 38 11805 10341 7746 -384 144 2432 ATOM 227 CA LYS A 38 -12.509 -4.760 -18.977 1.00 80.41 C ANISOU 227 CA LYS A 38 12037 10558 7957 -489 84 2482 ATOM 228 C LYS A 38 -13.192 -4.512 -20.324 1.00 81.95 C ANISOU 228 C LYS A 38 12186 10842 8110 -530 96 2583 ATOM 229 O LYS A 38 -13.236 -5.407 -21.172 1.00 82.50 O ANISOU 229 O LYS A 38 12212 10961 8172 -609 73 2656 ATOM 230 CB LYS A 38 -13.564 -5.039 -17.899 1.00 80.73 C ANISOU 230 CB LYS A 38 12169 10494 8009 -516 26 2417 ATOM 231 CG LYS A 38 -14.466 -6.221 -18.231 1.00 82.24 C ANISOU 231 CG LYS A 38 12384 10667 8196 -624 -39 2460 ATOM 232 CD LYS A 38 -15.327 -6.656 -17.063 1.00 82.96 C ANISOU 232 CD LYS A 38 12566 10645 8309 -643 -97 2387 ATOM 233 CE LYS A 38 -16.393 -7.642 -17.527 1.00 84.19 C ANISOU 233 CE LYS A 38 12751 10781 8456 -748 -162 2437 ATOM 234 NZ LYS A 38 -17.078 -8.330 -16.395 1.00 84.54 N1+ ANISOU 234 NZ LYS A 38 12880 10711 8528 -769 -223 2363 ATOM 235 N LEU A 39 -13.707 -3.281 -20.473 1.00 82.95 N ANISOU 235 N LEU A 39 12320 10991 8205 -478 132 2585 ATOM 236 CA LEU A 39 -14.411 -2.757 -21.642 1.00 83.74 C ANISOU 236 CA LEU A 39 12376 11182 8259 -511 151 2680 ATOM 237 C LEU A 39 -13.519 -2.683 -22.894 1.00 84.50 C ANISOU 237 C LEU A 39 12367 11395 8342 -487 210 2752 ATOM 238 O LEU A 39 -13.939 -3.080 -23.979 1.00 85.61 O ANISOU 238 O LEU A 39 12451 11614 8461 -555 204 2846 ATOM 239 CB LEU A 39 -14.981 -1.363 -21.253 1.00 0.00 C ATOM 240 CG LEU A 39 -15.681 -0.541 -22.364 1.00 0.00 C ATOM 241 CD1 LEU A 39 -16.892 -1.283 -22.968 1.00 0.00 C ATOM 242 CD2 LEU A 39 -16.053 0.870 -21.857 1.00 0.00 C ATOM 243 N ASN A 40 -12.329 -2.109 -22.720 1.00 85.18 N ANISOU 243 N ASN A 40 12426 11492 8444 -392 263 2710 ATOM 244 CA ASN A 40 -11.401 -1.738 -23.797 1.00 86.56 C ANISOU 244 CA ASN A 40 12504 11774 8609 -347 326 2771 ATOM 245 C ASN A 40 -10.403 -2.864 -24.097 1.00 88.30 C ANISOU 245 C ASN A 40 12668 12020 8862 -386 308 2806 ATOM 246 O ASN A 40 -9.609 -3.242 -23.235 1.00 88.09 O ANISOU 246 O ASN A 40 12668 11928 8873 -363 294 2745 ATOM 247 CB ASN A 40 -10.647 -0.457 -23.406 1.00 85.71 C ANISOU 247 CB ASN A 40 12401 11659 8506 -222 391 2707 ATOM 248 CG ASN A 40 -9.982 0.236 -24.587 1.00 85.81 C ANISOU 248 CG ASN A 40 12322 11786 8497 -161 464 2768 ATOM 249 OD1 ASN A 40 -9.898 -0.309 -25.688 1.00 86.10 O ANISOU 249 OD1 ASN A 40 12279 11913 8522 -208 468 2861 ATOM 250 ND2 ASN A 40 -9.501 1.453 -24.359 1.00 85.41 N ANISOU 250 ND2 ASN A 40 12279 11729 8441 -53 522 2715 ATOM 251 N PRO A 41 -10.459 -3.443 -25.327 1.00 91.23 N ANISOU 251 N PRO A 41 12959 12488 9214 -445 307 2908 ATOM 252 CA PRO A 41 -9.465 -4.444 -25.746 1.00 93.11 C ANISOU 252 CA PRO A 41 13134 12767 9476 -484 290 2953 ATOM 253 C PRO A 41 -8.092 -3.841 -26.091 1.00 94.17 C ANISOU 253 C PRO A 41 13202 12950 9628 -384 352 2955 ATOM 254 O PRO A 41 -7.125 -4.595 -26.171 1.00 95.25 O ANISOU 254 O PRO A 41 13307 13089 9792 -394 336 2964 ATOM 255 CD PRO A 41 -11.445 -3.223 -26.397 1.00 0.00 C ATOM 256 CB PRO A 41 -10.115 -5.124 -26.958 1.00 0.00 C ATOM 257 CG PRO A 41 -10.949 -4.026 -27.596 1.00 0.00 C ATOM 258 N SER A 42 -7.993 -2.513 -26.260 1.00 95.65 N ANISOU 258 N SER A 42 13370 13174 9799 -288 421 2946 ATOM 259 CA SER A 42 -6.715 -1.816 -26.449 1.00 96.75 C ANISOU 259 CA SER A 42 13460 13341 9958 -178 482 2935 ATOM 260 C SER A 42 -5.836 -1.919 -25.188 1.00 97.53 C ANISOU 260 C SER A 42 13623 13332 10100 -126 474 2839 ATOM 261 O SER A 42 -4.613 -1.871 -25.291 1.00 98.32 O ANISOU 261 O SER A 42 13684 13442 10227 -58 507 2837 ATOM 262 CB SER A 42 -6.966 -0.330 -26.778 1.00 0.00 C ATOM 263 OG SER A 42 -7.994 -0.170 -27.742 1.00 0.00 O ATOM 264 N LEU A 43 -6.486 -2.071 -24.025 1.00 98.16 N ANISOU 264 N LEU A 43 13798 13310 10188 -158 431 2763 ATOM 265 CA LEU A 43 -5.831 -2.215 -22.721 1.00 97.57 C ANISOU 265 CA LEU A 43 13786 13132 10154 -128 415 2673 ATOM 266 C LEU A 43 -5.764 -3.681 -22.247 1.00 97.63 C ANISOU 266 C LEU A 43 13813 13099 10181 -220 347 2672 ATOM 267 O LEU A 43 -5.814 -3.941 -21.041 1.00 96.77 O ANISOU 267 O LEU A 43 13776 12895 10094 -227 316 2593 ATOM 268 CB LEU A 43 -6.587 -1.378 -21.677 1.00 97.03 C ANISOU 268 CB LEU A 43 13808 12977 10081 -95 413 2582 ATOM 269 CG LEU A 43 -6.885 0.081 -22.028 1.00 97.17 C ANISOU 269 CG LEU A 43 13824 13025 10068 -13 471 2570 ATOM 270 CD1 LEU A 43 -7.780 0.714 -20.975 1.00 96.46 C ANISOU 270 CD1 LEU A 43 13826 12851 9970 -1 453 2486 ATOM 271 CD2 LEU A 43 -5.590 0.859 -22.172 1.00 97.37 C ANISOU 271 CD2 LEU A 43 13812 13067 10115 90 534 2555 ATOM 272 N GLN A 44 -5.647 -4.623 -23.194 1.00 98.51 N ANISOU 272 N GLN A 44 13860 13285 10284 -290 323 2758 ATOM 273 CA GLN A 44 -5.448 -6.043 -22.887 1.00 98.96 C ANISOU 273 CA GLN A 44 13935 13313 10353 -382 258 2759 ATOM 274 C GLN A 44 -4.014 -6.357 -22.416 1.00 98.26 C ANISOU 274 C GLN A 44 13799 13244 10290 -356 267 2774 ATOM 275 O GLN A 44 -3.799 -7.411 -21.820 1.00 99.58 O ANISOU 275 O GLN A 44 13911 13471 10452 -417 239 2841 ATOM 276 CB GLN A 44 -5.828 -6.902 -24.111 1.00 0.00 C ATOM 277 CG GLN A 44 -4.888 -6.770 -25.330 1.00 0.00 C ATOM 278 CD GLN A 44 -5.398 -7.587 -26.511 1.00 0.00 C ATOM 279 OE1 GLN A 44 -4.975 -8.717 -26.728 1.00 0.00 O ATOM 280 NE2 GLN A 44 -6.325 -7.027 -27.272 1.00 0.00 N ATOM 281 N THR A 45 -3.058 -5.481 -22.745 1.00 96.24 N ANISOU 281 N THR A 45 13570 12933 10061 -268 303 2709 ATOM 282 CA THR A 45 -1.634 -5.631 -22.483 1.00 94.34 C ANISOU 282 CA THR A 45 13289 12706 9847 -222 323 2722 ATOM 283 C THR A 45 -1.296 -5.809 -20.989 1.00 91.65 C ANISOU 283 C THR A 45 13022 12263 9536 -212 306 2631 ATOM 284 O THR A 45 -1.900 -5.156 -20.139 1.00 92.32 O ANISOU 284 O THR A 45 13183 12269 9625 -208 296 2552 ATOM 285 CB THR A 45 -0.874 -4.385 -23.008 1.00 0.00 C ATOM 286 OG1 THR A 45 -1.390 -4.033 -24.283 1.00 0.00 O ATOM 287 CG2 THR A 45 0.647 -4.552 -23.126 1.00 0.00 C ATOM 288 N THR A 46 -0.317 -6.671 -20.709 1.00 88.80 N ANISOU 288 N THR A 46 12636 11908 9194 -208 302 2647 ATOM 289 CA THR A 46 0.107 -7.151 -19.402 1.00 85.77 C ANISOU 289 CA THR A 46 12312 11441 8835 -209 285 2573 ATOM 290 C THR A 46 0.199 -6.116 -18.257 1.00 82.88 C ANISOU 290 C THR A 46 12004 10992 8493 -129 322 2486 ATOM 291 O THR A 46 -0.340 -6.355 -17.177 1.00 82.01 O ANISOU 291 O THR A 46 11964 10804 8391 -150 298 2408 ATOM 292 CB THR A 46 1.488 -7.807 -19.589 1.00 0.00 C ATOM 293 OG1 THR A 46 1.385 -8.834 -20.560 1.00 0.00 O ATOM 294 CG2 THR A 46 2.137 -8.284 -18.292 1.00 0.00 C ATOM 295 N THR A 47 0.825 -4.968 -18.546 1.00 80.59 N ANISOU 295 N THR A 47 11684 10721 8214 -39 378 2499 ATOM 296 CA THR A 47 0.891 -3.755 -17.718 1.00 78.68 C ANISOU 296 CA THR A 47 11493 10406 7994 39 414 2419 ATOM 297 C THR A 47 -0.465 -3.414 -17.098 1.00 77.75 C ANISOU 297 C THR A 47 11442 10238 7861 15 393 2353 ATOM 298 O THR A 47 -0.553 -3.150 -15.898 1.00 76.58 O ANISOU 298 O THR A 47 11357 10007 7732 28 386 2270 ATOM 299 CB THR A 47 1.393 -2.538 -18.535 1.00 78.54 C ANISOU 299 CB THR A 47 11432 10429 7981 135 476 2448 ATOM 300 OG1 THR A 47 2.708 -2.802 -19.041 1.00 78.57 O ANISOU 300 OG1 THR A 47 11376 10471 8005 167 495 2506 ATOM 301 CG2 THR A 47 1.436 -1.271 -17.678 1.00 78.14 C ANISOU 301 CG2 THR A 47 11439 10299 7949 212 510 2360 ATOM 302 N PHE A 48 -1.513 -3.445 -17.918 1.00 78.14 N ANISOU 302 N PHE A 48 11475 10340 7875 -21 382 2396 ATOM 303 CA PHE A 48 -2.855 -3.066 -17.477 1.00 77.72 C ANISOU 303 CA PHE A 48 11480 10247 7803 -41 362 2347 ATOM 304 C PHE A 48 -3.453 -4.104 -16.533 1.00 76.58 C ANISOU 304 C PHE A 48 11393 10040 7664 -118 301 2302 ATOM 305 O PHE A 48 -4.060 -3.736 -15.520 1.00 76.71 O ANISOU 305 O PHE A 48 11474 9983 7688 -108 287 2224 ATOM 306 CB PHE A 48 -3.767 -2.798 -18.676 1.00 79.00 C ANISOU 306 CB PHE A 48 11605 10485 7923 -60 369 2415 ATOM 307 CG PHE A 48 -3.242 -1.730 -19.593 1.00 80.35 C ANISOU 307 CG PHE A 48 11720 10721 8086 21 434 2453 ATOM 308 CD1 PHE A 48 -3.129 -0.417 -19.153 1.00 80.65 C ANISOU 308 CD1 PHE A 48 11792 10721 8130 110 477 2391 ATOM 309 CD2 PHE A 48 -2.822 -2.040 -20.880 1.00 81.89 C ANISOU 309 CD2 PHE A 48 11829 11016 8269 14 452 2549 ATOM 310 CE1 PHE A 48 -2.628 0.572 -19.987 1.00 81.73 C ANISOU 310 CE1 PHE A 48 11880 10913 8257 192 538 2420 ATOM 311 CE2 PHE A 48 -2.323 -1.054 -21.723 1.00 82.88 C ANISOU 311 CE2 PHE A 48 11900 11203 8388 98 515 2582 ATOM 312 CZ PHE A 48 -2.225 0.255 -21.275 1.00 82.69 C ANISOU 312 CZ PHE A 48 11914 11136 8367 189 559 2516 ATOM 313 N TYR A 49 -3.236 -5.400 -16.790 1.00 75.54 N ANISOU 313 N TYR A 49 11235 9936 7528 -190 265 2346 ATOM 314 CA TYR A 49 -3.672 -6.458 -15.867 1.00 74.32 C ANISOU 314 CA TYR A 49 11134 9724 7379 -260 209 2299 ATOM 315 C TYR A 49 -3.106 -6.270 -14.452 1.00 72.24 C ANISOU 315 C TYR A 49 10920 9377 7149 -222 215 2208 ATOM 316 O TYR A 49 -3.822 -6.506 -13.476 1.00 70.44 O ANISOU 316 O TYR A 49 10751 9085 6926 -253 180 2144 ATOM 317 CB TYR A 49 -3.332 -7.848 -16.423 1.00 0.00 C ATOM 318 CG TYR A 49 -4.411 -8.439 -17.311 1.00 0.00 C ATOM 319 CD1 TYR A 49 -5.160 -9.546 -16.857 1.00 0.00 C ATOM 320 CD2 TYR A 49 -4.672 -7.892 -18.585 1.00 0.00 C ATOM 321 CE1 TYR A 49 -6.162 -10.104 -17.673 1.00 0.00 C ATOM 322 CE2 TYR A 49 -5.685 -8.443 -19.392 1.00 0.00 C ATOM 323 CZ TYR A 49 -6.427 -9.551 -18.939 1.00 0.00 C ATOM 324 OH TYR A 49 -7.389 -10.104 -19.730 1.00 0.00 O ATOM 325 N PHE A 50 -1.882 -5.735 -14.356 1.00 71.38 N ANISOU 325 N PHE A 50 10787 9270 7063 -156 259 2205 ATOM 326 CA PHE A 50 -1.331 -5.370 -13.045 1.00 70.63 C ANISOU 326 CA PHE A 50 10734 9098 7001 -114 272 2123 ATOM 327 C PHE A 50 -1.974 -4.090 -12.501 1.00 70.14 C ANISOU 327 C PHE A 50 10716 8986 6946 -58 291 2058 ATOM 328 O PHE A 50 -2.125 -3.946 -11.282 1.00 70.44 O ANISOU 328 O PHE A 50 10804 8953 7005 -50 280 1979 ATOM 329 CB PHE A 50 0.192 -5.199 -13.101 1.00 70.42 C ANISOU 329 CB PHE A 50 10671 9085 6999 -67 309 2146 ATOM 330 CG PHE A 50 0.936 -6.405 -13.620 1.00 70.63 C ANISOU 330 CG PHE A 50 10653 9165 7017 -118 291 2212 ATOM 331 CD1 PHE A 50 0.728 -7.667 -13.073 1.00 70.57 C ANISOU 331 CD1 PHE A 50 10670 9143 6999 -193 245 2194 ATOM 332 CD2 PHE A 50 1.867 -6.273 -14.648 1.00 71.12 C ANISOU 332 CD2 PHE A 50 10648 9293 7080 -86 319 2292 ATOM 333 CE1 PHE A 50 1.416 -8.773 -13.558 1.00 70.94 C ANISOU 333 CE1 PHE A 50 10677 9242 7032 -242 225 2253 ATOM 334 CE2 PHE A 50 2.554 -7.376 -15.135 1.00 71.31 C ANISOU 334 CE2 PHE A 50 10630 9371 7094 -133 298 2356 ATOM 335 CZ PHE A 50 2.332 -8.626 -14.589 1.00 71.23 C ANISOU 335 CZ PHE A 50 10646 9348 7069 -213 250 2336 ATOM 336 N ILE A 51 -2.330 -3.158 -13.390 1.00 69.91 N ANISOU 336 N ILE A 51 10665 8999 6899 -18 319 2092 ATOM 337 CA ILE A 51 -3.049 -1.933 -12.993 1.00 69.86 C ANISOU 337 CA ILE A 51 10700 8955 6888 31 334 2036 ATOM 338 C ILE A 51 -4.452 -2.242 -12.439 1.00 68.84 C ANISOU 338 C ILE A 51 10624 8787 6744 -18 285 1997 ATOM 339 O ILE A 51 -4.939 -1.537 -11.549 1.00 68.02 O ANISOU 339 O ILE A 51 10569 8625 6648 10 280 1926 ATOM 340 CB ILE A 51 -3.089 -0.898 -14.154 1.00 71.08 C ANISOU 340 CB ILE A 51 10816 9172 7019 85 379 2085 ATOM 341 CG1 ILE A 51 -1.678 -0.331 -14.387 1.00 71.31 C ANISOU 341 CG1 ILE A 51 10809 9212 7073 157 430 2097 ATOM 342 CG2 ILE A 51 -4.074 0.241 -13.879 1.00 71.20 C ANISOU 342 CG2 ILE A 51 10876 9161 7014 121 386 2035 ATOM 343 CD1 ILE A 51 -1.501 0.385 -15.711 1.00 71.84 C ANISOU 343 CD1 ILE A 51 10821 9357 7118 207 477 2161 ATOM 344 N VAL A 52 -5.083 -3.297 -12.952 1.00 68.75 N ANISOU 344 N VAL A 52 10604 8805 6712 -94 246 2045 ATOM 345 CA VAL A 52 -6.356 -3.791 -12.411 1.00 68.26 C ANISOU 345 CA VAL A 52 10595 8699 6641 -146 193 2011 ATOM 346 C VAL A 52 -6.137 -4.309 -10.980 1.00 67.71 C ANISOU 346 C VAL A 52 10569 8552 6603 -154 169 1929 ATOM 347 O VAL A 52 -6.881 -3.942 -10.065 1.00 67.68 O ANISOU 347 O VAL A 52 10617 8489 6609 -141 149 1862 ATOM 348 CB VAL A 52 -6.976 -4.904 -13.300 1.00 68.17 C ANISOU 348 CB VAL A 52 10566 8732 6604 -231 154 2082 ATOM 349 CG1 VAL A 52 -8.206 -5.528 -12.640 1.00 67.91 C ANISOU 349 CG1 VAL A 52 10594 8638 6569 -285 95 2042 ATOM 350 CG2 VAL A 52 -7.340 -4.361 -14.674 1.00 68.62 C ANISOU 350 CG2 VAL A 52 10576 8867 6626 -229 177 2164 ATOM 351 N SER A 53 -5.114 -5.147 -10.796 1.00 67.01 N ANISOU 351 N SER A 53 10458 8470 6531 -173 171 1936 ATOM 352 CA SER A 53 -4.758 -5.675 -9.470 1.00 65.95 C ANISOU 352 CA SER A 53 10357 8274 6425 -180 155 1863 ATOM 353 C SER A 53 -4.431 -4.546 -8.494 1.00 65.00 C ANISOU 353 C SER A 53 10260 8103 6333 -110 184 1792 ATOM 354 O SER A 53 -4.880 -4.562 -7.341 1.00 64.54 O ANISOU 354 O SER A 53 10244 7984 6292 -109 163 1718 ATOM 355 CB SER A 53 -3.575 -6.642 -9.573 1.00 66.16 C ANISOU 355 CB SER A 53 10349 8329 6457 -207 161 1893 ATOM 356 OG SER A 53 -3.153 -7.082 -8.292 1.00 66.00 O ANISOU 356 OG SER A 53 10357 8257 6460 -210 154 1824 ATOM 357 N LEU A 54 -3.660 -3.568 -8.970 1.00 64.50 N ANISOU 357 N LEU A 54 10166 8063 6275 -52 231 1815 ATOM 358 CA LEU A 54 -3.331 -2.378 -8.182 1.00 63.86 C ANISOU 358 CA LEU A 54 10108 7936 6220 12 259 1751 ATOM 359 C LEU A 54 -4.574 -1.533 -7.853 1.00 63.66 C ANISOU 359 C LEU A 54 10124 7880 6182 31 243 1705 ATOM 360 O LEU A 54 -4.686 -1.004 -6.745 1.00 63.03 O ANISOU 360 O LEU A 54 10079 7744 6125 57 238 1630 ATOM 361 CB LEU A 54 -2.273 -1.539 -8.910 1.00 63.94 C ANISOU 361 CB LEU A 54 10079 7979 6236 71 312 1790 ATOM 362 CG LEU A 54 -1.752 -0.259 -8.251 1.00 63.91 C ANISOU 362 CG LEU A 54 10095 7928 6258 140 345 1731 ATOM 363 CD1 LEU A 54 -1.280 -0.503 -6.831 1.00 63.54 C ANISOU 363 CD1 LEU A 54 10075 7815 6249 132 334 1661 ATOM 364 CD2 LEU A 54 -0.624 0.325 -9.085 1.00 64.27 C ANISOU 364 CD2 LEU A 54 10100 8006 6311 194 394 1778 ATOM 365 N ALA A 55 -5.499 -1.416 -8.810 1.00 63.94 N ANISOU 365 N ALA A 55 10156 7957 6181 17 233 1754 ATOM 366 CA ALA A 55 -6.777 -0.714 -8.593 1.00 63.94 C ANISOU 366 CA ALA A 55 10196 7934 6161 27 211 1722 ATOM 367 C ALA A 55 -7.651 -1.425 -7.561 1.00 63.43 C ANISOU 367 C ALA A 55 10177 7812 6109 -12 157 1669 ATOM 368 O ALA A 55 -8.179 -0.780 -6.656 1.00 63.12 O ANISOU 368 O ALA A 55 10176 7724 6080 14 143 1604 ATOM 369 CB ALA A 55 -7.537 -0.560 -9.903 1.00 64.44 C ANISOU 369 CB ALA A 55 10242 8061 6181 11 213 1797 ATOM 370 N LEU A 56 -7.746 -2.760 -7.684 1.00 63.37 N ANISOU 370 N LEU A 56 10166 7811 6101 -75 127 1696 ATOM 371 CA LEU A 56 -8.454 -3.678 -6.783 1.00 63.14 C ANISOU 371 CA LEU A 56 10178 7725 6085 -113 76 1645 ATOM 372 C LEU A 56 -8.049 -3.478 -5.309 1.00 63.09 C ANISOU 372 C LEU A 56 10191 7662 6117 -79 81 1557 ATOM 373 O LEU A 56 -8.898 -3.411 -4.420 1.00 62.57 O ANISOU 373 O LEU A 56 10164 7545 6062 -71 50 1498 ATOM 374 CB LEU A 56 -8.254 -5.134 -7.270 1.00 0.00 C ATOM 375 CG LEU A 56 -8.897 -6.244 -6.407 1.00 0.00 C ATOM 376 CD1 LEU A 56 -10.428 -6.085 -6.297 1.00 0.00 C ATOM 377 CD2 LEU A 56 -8.480 -7.642 -6.915 1.00 0.00 C ATOM 378 N ALA A 57 -6.743 -3.329 -5.091 1.00 63.60 N ANISOU 378 N ALA A 57 10226 7736 6203 -60 118 1553 ATOM 379 CA ALA A 57 -6.153 -3.004 -3.789 1.00 63.50 C ANISOU 379 CA ALA A 57 10224 7676 6227 -30 129 1478 ATOM 380 C ALA A 57 -6.584 -1.622 -3.276 1.00 63.44 C ANISOU 380 C ALA A 57 10239 7636 6227 23 135 1427 ATOM 381 O ALA A 57 -6.905 -1.467 -2.096 1.00 63.36 O ANISOU 381 O ALA A 57 10254 7579 6241 34 115 1356 ATOM 382 CB ALA A 57 -4.630 -3.096 -3.853 1.00 63.54 C ANISOU 382 CB ALA A 57 10192 7701 6250 -19 171 1497 ATOM 383 N ASP A 58 -6.598 -0.631 -4.168 1.00 63.47 N ANISOU 383 N ASP A 58 10234 7672 6208 57 160 1463 ATOM 384 CA ASP A 58 -7.017 0.728 -3.804 1.00 63.59 C ANISOU 384 CA ASP A 58 10274 7665 6223 108 165 1418 ATOM 385 C ASP A 58 -8.527 0.826 -3.514 1.00 62.53 C ANISOU 385 C ASP A 58 10179 7509 6070 98 117 1395 ATOM 386 O ASP A 58 -8.927 1.547 -2.593 1.00 63.05 O ANISOU 386 O ASP A 58 10271 7535 6148 126 102 1331 ATOM 387 CB ASP A 58 -6.593 1.746 -4.880 1.00 64.82 C ANISOU 387 CB ASP A 58 10410 7864 6355 151 209 1460 ATOM 388 CG ASP A 58 -5.062 1.909 -4.990 1.00 65.53 C ANISOU 388 CG ASP A 58 10468 7960 6471 177 257 1471 ATOM 389 OD1 ASP A 58 -4.328 1.665 -3.997 1.00 65.34 O ANISOU 389 OD1 ASP A 58 10444 7894 6485 174 258 1426 ATOM 390 OD2 ASP A 58 -4.598 2.304 -6.087 1.00 66.34 O1- ANISOU 390 OD2 ASP A 58 10542 8108 6555 202 293 1525 ATOM 391 N ILE A 59 -9.396 0.122 -4.276 1.00 61.28 N ANISOU 391 N ILE A 59 10023 7374 5883 55 91 1449 ATOM 392 CA ILE A 59 -10.834 0.073 -3.934 1.00 60.20 C ANISOU 392 CA ILE A 59 9928 7211 5733 38 39 1435 ATOM 393 C ILE A 59 -11.043 -0.567 -2.558 1.00 58.81 C ANISOU 393 C ILE A 59 9775 6973 5595 32 5 1360 ATOM 394 O ILE A 59 -11.881 -0.074 -1.805 1.00 58.20 O ANISOU 394 O ILE A 59 9729 6859 5523 53 -25 1312 ATOM 395 CB ILE A 59 -11.821 -0.640 -4.919 1.00 0.00 C ATOM 396 CG1 ILE A 59 -11.580 -2.139 -5.171 1.00 0.00 C ATOM 397 CG2 ILE A 59 -11.942 0.093 -6.251 1.00 0.00 C ATOM 398 CD1 ILE A 59 -12.678 -2.840 -5.985 1.00 0.00 C ATOM 399 N ALA A 60 -10.231 -1.586 -2.223 1.00 57.53 N ANISOU 399 N ALA A 60 9595 6806 5458 5 11 1352 ATOM 400 CA ALA A 60 -10.293 -2.191 -0.892 1.00 56.62 C ANISOU 400 CA ALA A 60 9493 6640 5377 0 -13 1281 ATOM 401 C ALA A 60 -9.918 -1.227 0.238 1.00 55.76 C ANISOU 401 C ALA A 60 9385 6501 5299 47 0 1209 ATOM 402 O ALA A 60 -10.485 -1.323 1.323 1.00 55.55 O ANISOU 402 O ALA A 60 9377 6433 5296 55 -31 1148 ATOM 403 CB ALA A 60 -9.420 -3.436 -0.832 1.00 56.52 C ANISOU 403 CB ALA A 60 9458 6639 5377 -38 -1 1291 ATOM 404 N VAL A 61 -8.984 -0.304 -0.012 1.00 54.89 N ANISOU 404 N VAL A 61 9254 6410 5192 78 43 1215 ATOM 405 CA VAL A 61 -8.599 0.701 0.995 1.00 54.15 C ANISOU 405 CA VAL A 61 9162 6286 5126 119 53 1149 ATOM 406 C VAL A 61 -9.794 1.621 1.301 1.00 53.83 C ANISOU 406 C VAL A 61 9155 6225 5073 147 18 1116 ATOM 407 O VAL A 61 -10.228 1.750 2.466 1.00 53.62 O ANISOU 407 O VAL A 61 9140 6161 5072 158 -10 1052 ATOM 408 CB VAL A 61 -7.366 1.528 0.542 1.00 54.23 C ANISOU 408 CB VAL A 61 9149 6314 5140 147 106 1166 ATOM 409 CG1 VAL A 61 -7.073 2.687 1.496 1.00 54.20 C ANISOU 409 CG1 VAL A 61 9154 6276 5163 186 112 1097 ATOM 410 CG2 VAL A 61 -6.135 0.637 0.413 1.00 54.36 C ANISOU 410 CG2 VAL A 61 9134 6347 5174 122 137 1195 ATOM 411 N GLY A 62 -10.328 2.222 0.233 1.00 53.61 N ANISOU 411 N GLY A 62 9138 6228 5003 157 21 1164 ATOM 412 CA GLY A 62 -11.482 3.126 0.312 1.00 53.54 C ANISOU 412 CA GLY A 62 9161 6211 4968 181 -10 1148 ATOM 413 C GLY A 62 -12.777 2.483 0.784 1.00 53.25 C ANISOU 413 C GLY A 62 9154 6146 4933 161 -69 1137 ATOM 414 O GLY A 62 -13.552 3.115 1.498 1.00 53.20 O ANISOU 414 O GLY A 62 9171 6113 4928 185 -103 1093 ATOM 415 N VAL A 63 -13.042 1.218 0.417 1.00 52.95 N ANISOU 415 N VAL A 63 9114 6109 4893 117 -82 1176 ATOM 416 CA VAL A 63 -14.285 0.531 0.789 1.00 52.76 C ANISOU 416 CA VAL A 63 9122 6051 4873 96 -139 1168 ATOM 417 C VAL A 63 -14.155 -0.306 2.082 1.00 52.31 C ANISOU 417 C VAL A 63 9064 5948 4863 96 -161 1099 ATOM 418 O VAL A 63 -15.195 -0.597 2.671 1.00 52.57 O ANISOU 418 O VAL A 63 9124 5942 4907 102 -210 1070 ATOM 419 CB VAL A 63 -14.847 -0.347 -0.375 1.00 0.00 C ATOM 420 CG1 VAL A 63 -14.252 -1.762 -0.477 1.00 0.00 C ATOM 421 CG2 VAL A 63 -16.384 -0.458 -0.334 1.00 0.00 C ATOM 422 N LEU A 64 -12.936 -0.679 2.514 1.00 51.54 N ANISOU 422 N LEU A 64 8933 5855 4792 90 -125 1076 ATOM 423 CA LEU A 64 -12.738 -1.423 3.776 1.00 51.15 C ANISOU 423 CA LEU A 64 8876 5772 4785 88 -136 1011 ATOM 424 C LEU A 64 -11.860 -0.702 4.803 1.00 50.74 C ANISOU 424 C LEU A 64 8798 5714 4767 118 -110 952 ATOM 425 O LEU A 64 -12.264 -0.570 5.967 1.00 50.53 O ANISOU 425 O LEU A 64 8773 5657 4769 139 -136 889 ATOM 426 CB LEU A 64 -12.169 -2.825 3.503 1.00 51.08 C ANISOU 426 CB LEU A 64 8854 5774 4777 44 -123 1034 ATOM 427 CG LEU A 64 -11.899 -3.770 4.689 1.00 50.86 C ANISOU 427 CG LEU A 64 8817 5721 4784 38 -128 972 ATOM 428 CD1 LEU A 64 -13.145 -4.006 5.524 1.00 50.92 C ANISOU 428 CD1 LEU A 64 8854 5684 4810 55 -181 923 ATOM 429 CD2 LEU A 64 -11.334 -5.085 4.189 1.00 50.74 C ANISOU 429 CD2 LEU A 64 8793 5726 4757 -8 -114 1004 ATOM 430 N VAL A 65 -10.642 -0.285 4.448 1.00 50.59 N ANISOU 430 N VAL A 65 8754 5722 4746 120 -61 972 ATOM 431 CA VAL A 65 -9.702 0.269 5.427 1.00 50.51 C ANISOU 431 CA VAL A 65 8718 5701 4771 138 -34 921 ATOM 432 C VAL A 65 -10.220 1.595 6.000 1.00 50.54 C ANISOU 432 C VAL A 65 8734 5686 4783 177 -53 874 ATOM 433 O VAL A 65 -10.208 1.769 7.221 1.00 50.21 O ANISOU 433 O VAL A 65 8679 5620 4776 188 -64 811 ATOM 434 CB VAL A 65 -8.290 0.428 4.816 1.00 50.55 C ANISOU 434 CB VAL A 65 8697 5732 4774 132 21 959 ATOM 435 CG1 VAL A 65 -7.298 1.142 5.754 1.00 50.64 C ANISOU 435 CG1 VAL A 65 8689 5726 4823 150 46 910 ATOM 436 CG2 VAL A 65 -7.723 -0.934 4.376 1.00 50.51 C ANISOU 436 CG2 VAL A 65 8676 5749 4765 92 37 999 ATOM 437 N MET A 66 -10.683 2.527 5.151 1.00 50.68 N ANISOU 437 N MET A 66 8773 5716 4764 196 -58 904 ATOM 438 CA MET A 66 -11.056 3.830 5.676 1.00 50.89 C ANISOU 438 CA MET A 66 8814 5729 4789 232 -77 861 ATOM 439 C MET A 66 -12.360 3.840 6.504 1.00 50.76 C ANISOU 439 C MET A 66 8816 5686 4783 243 -136 817 ATOM 440 O MET A 66 -12.380 4.504 7.542 1.00 50.84 O ANISOU 440 O MET A 66 8819 5677 4819 264 -153 757 ATOM 441 CB MET A 66 -10.982 4.847 4.554 1.00 0.00 C ATOM 442 CG MET A 66 -9.553 4.921 3.970 1.00 0.00 C ATOM 443 SD MET A 66 -9.509 5.677 2.345 1.00 0.00 S ATOM 444 CE MET A 66 -9.960 7.318 2.904 1.00 0.00 C ATOM 445 N PRO A 67 -13.372 3.012 6.149 1.00 50.61 N ANISOU 445 N PRO A 67 8818 5663 4747 229 -171 849 ATOM 446 CA PRO A 67 -14.502 2.759 7.057 1.00 50.66 C ANISOU 446 CA PRO A 67 8840 5637 4771 241 -228 809 ATOM 447 C PRO A 67 -14.121 2.162 8.416 1.00 50.71 C ANISOU 447 C PRO A 67 8816 5620 4831 242 -231 744 ATOM 448 O PRO A 67 -14.615 2.633 9.444 1.00 50.54 O ANISOU 448 O PRO A 67 8790 5578 4832 268 -265 691 ATOM 449 CB PRO A 67 -15.354 1.772 6.270 1.00 50.71 C ANISOU 449 CB PRO A 67 8872 5639 4753 216 -252 863 ATOM 450 CG PRO A 67 -15.144 2.184 4.864 1.00 50.73 C ANISOU 450 CG PRO A 67 8883 5680 4709 203 -222 933 ATOM 451 CD PRO A 67 -13.699 2.594 4.773 1.00 50.57 C ANISOU 451 CD PRO A 67 8830 5683 4699 206 -164 926 ATOM 452 N LEU A 68 -13.223 1.151 8.429 1.00 50.80 N ANISOU 452 N LEU A 68 8805 5638 4858 214 -197 751 ATOM 453 CA LEU A 68 -12.682 0.509 9.636 1.00 51.13 C ANISOU 453 CA LEU A 68 8813 5667 4945 213 -189 693 ATOM 454 C LEU A 68 -12.031 1.537 10.570 1.00 51.45 C ANISOU 454 C LEU A 68 8824 5707 5015 231 -175 642 ATOM 455 O LEU A 68 -12.320 1.554 11.766 1.00 51.79 O ANISOU 455 O LEU A 68 8847 5736 5095 245 -195 584 ATOM 456 CB LEU A 68 -11.654 -0.600 9.296 1.00 51.09 C ANISOU 456 CB LEU A 68 8790 5679 4943 176 -147 716 ATOM 457 CG LEU A 68 -12.209 -1.956 8.805 1.00 51.19 C ANISOU 457 CG LEU A 68 8823 5685 4941 152 -166 741 ATOM 458 CD1 LEU A 68 -11.053 -2.828 8.284 1.00 50.98 C ANISOU 458 CD1 LEU A 68 8781 5686 4902 113 -122 779 ATOM 459 CD2 LEU A 68 -12.998 -2.728 9.874 1.00 51.44 C ANISOU 459 CD2 LEU A 68 8852 5687 5003 167 -199 680 ATOM 460 N ALA A 69 -11.207 2.423 9.992 1.00 51.52 N ANISOU 460 N ALA A 69 8833 5731 5010 231 -141 665 ATOM 461 CA ALA A 69 -10.548 3.533 10.670 1.00 51.76 C ANISOU 461 CA ALA A 69 8844 5757 5066 243 -128 620 ATOM 462 C ALA A 69 -11.559 4.502 11.307 1.00 52.13 C ANISOU 462 C ALA A 69 8903 5790 5115 274 -180 577 ATOM 463 O ALA A 69 -11.418 4.852 12.478 1.00 52.31 O ANISOU 463 O ALA A 69 8898 5801 5174 281 -192 519 ATOM 464 CB ALA A 69 -9.634 4.263 9.672 1.00 51.75 C ANISOU 464 CB ALA A 69 8848 5768 5044 243 -85 656 ATOM 465 N ILE A 70 -12.622 4.874 10.578 1.00 52.52 N ANISOU 465 N ILE A 70 8990 5842 5122 290 -210 608 ATOM 466 CA ILE A 70 -13.700 5.735 11.086 1.00 53.21 C ANISOU 466 CA ILE A 70 9094 5919 5202 320 -266 575 ATOM 467 C ILE A 70 -14.462 5.033 12.223 1.00 53.74 C ANISOU 467 C ILE A 70 9145 5967 5306 329 -310 534 ATOM 468 O ILE A 70 -14.651 5.618 13.301 1.00 54.17 O ANISOU 468 O ILE A 70 9179 6014 5389 347 -339 479 ATOM 469 CB ILE A 70 -14.672 6.168 9.950 1.00 53.14 C ANISOU 469 CB ILE A 70 9133 5923 5136 331 -288 628 ATOM 470 CG1 ILE A 70 -13.947 7.074 8.949 1.00 53.06 C ANISOU 470 CG1 ILE A 70 9134 5936 5089 332 -244 657 ATOM 471 CG2 ILE A 70 -15.888 6.903 10.508 1.00 53.43 C ANISOU 471 CG2 ILE A 70 9189 5950 5162 360 -352 600 ATOM 472 CD1 ILE A 70 -14.589 7.128 7.581 1.00 53.12 C ANISOU 472 CD1 ILE A 70 9176 5967 5038 332 -243 726 ATOM 473 N VAL A 71 -14.950 3.803 12.009 1.00 53.84 N ANISOU 473 N VAL A 71 9165 5971 5320 318 -315 559 ATOM 474 CA VAL A 71 -15.837 3.170 12.992 1.00 54.37 C ANISOU 474 CA VAL A 71 9219 6017 5422 331 -352 519 ATOM 475 C VAL A 71 -15.132 2.804 14.313 1.00 54.70 C ANISOU 475 C VAL A 71 9205 6061 5515 330 -331 458 ATOM 476 O VAL A 71 -15.813 2.751 15.333 1.00 54.93 O ANISOU 476 O VAL A 71 9213 6081 5576 355 -368 408 ATOM 477 CB VAL A 71 -16.603 1.931 12.458 1.00 0.00 C ATOM 478 CG1 VAL A 71 -17.515 2.294 11.272 1.00 0.00 C ATOM 479 CG2 VAL A 71 -15.712 0.722 12.144 1.00 0.00 C ATOM 480 N VAL A 72 -13.798 2.630 14.331 1.00 55.27 N ANISOU 480 N VAL A 72 9254 6150 5596 300 -273 466 ATOM 481 CA VAL A 72 -13.039 2.439 15.571 1.00 56.04 C ANISOU 481 CA VAL A 72 9298 6254 5738 291 -247 415 ATOM 482 C VAL A 72 -12.609 3.790 16.179 1.00 57.02 C ANISOU 482 C VAL A 72 9405 6379 5880 304 -263 375 ATOM 483 O VAL A 72 -12.523 3.888 17.400 1.00 57.13 O ANISOU 483 O VAL A 72 9376 6394 5935 311 -275 322 ATOM 484 CB VAL A 72 -11.819 1.521 15.310 1.00 0.00 C ATOM 485 CG1 VAL A 72 -10.643 2.155 14.542 1.00 0.00 C ATOM 486 CG2 VAL A 72 -11.317 0.860 16.607 1.00 0.00 C ATOM 487 N SER A 73 -12.398 4.842 15.369 1.00 58.07 N ANISOU 487 N SER A 73 9569 6512 5980 307 -262 400 ATOM 488 CA SER A 73 -12.141 6.196 15.847 1.00 59.43 C ANISOU 488 CA SER A 73 9734 6682 6162 318 -281 361 ATOM 489 C SER A 73 -13.392 6.765 16.549 1.00 60.41 C ANISOU 489 C SER A 73 9855 6801 6296 349 -348 322 ATOM 490 O SER A 73 -13.289 7.404 17.595 1.00 60.79 O ANISOU 490 O SER A 73 9863 6851 6382 351 -366 269 ATOM 491 CB SER A 73 -11.726 7.060 14.639 1.00 0.00 C ATOM 492 OG SER A 73 -11.440 8.390 15.009 1.00 0.00 O ATOM 493 N LEU A 74 -14.576 6.481 15.994 1.00 61.28 N ANISOU 493 N LEU A 74 10004 6906 6372 371 -388 351 ATOM 494 CA LEU A 74 -15.876 6.830 16.555 1.00 62.16 C ANISOU 494 CA LEU A 74 10117 7011 6490 405 -457 322 ATOM 495 C LEU A 74 -16.350 5.809 17.617 1.00 63.24 C ANISOU 495 C LEU A 74 10214 7138 6673 419 -477 289 ATOM 496 O LEU A 74 -17.208 6.145 18.430 1.00 63.83 O ANISOU 496 O LEU A 74 10269 7211 6770 448 -529 251 ATOM 497 CB LEU A 74 -16.865 6.956 15.370 1.00 0.00 C ATOM 498 CG LEU A 74 -18.181 7.711 15.663 1.00 0.00 C ATOM 499 CD1 LEU A 74 -17.933 9.174 16.093 1.00 0.00 C ATOM 500 CD2 LEU A 74 -19.139 7.619 14.455 1.00 0.00 C ATOM 501 N GLY A 75 -15.815 4.580 17.578 1.00 64.21 N ANISOU 501 N GLY A 75 10327 7259 6809 401 -436 302 ATOM 502 CA GLY A 75 -16.227 3.471 18.444 1.00 65.55 C ANISOU 502 CA GLY A 75 10467 7420 7017 418 -449 270 ATOM 503 C GLY A 75 -15.606 3.453 19.833 1.00 67.00 C ANISOU 503 C GLY A 75 10580 7621 7254 417 -435 209 ATOM 504 O GLY A 75 -14.870 4.374 20.195 1.00 67.25 O ANISOU 504 O GLY A 75 10586 7667 7297 400 -421 190 ATOM 505 N ILE A 76 -15.893 2.401 20.604 1.00 68.98 N ANISOU 505 N ILE A 76 10800 7870 7537 435 -437 178 ATOM 506 CA ILE A 76 -15.243 2.140 21.882 1.00 70.20 C ANISOU 506 CA ILE A 76 10881 8048 7743 436 -422 121 ATOM 507 C ILE A 76 -13.807 1.612 21.687 1.00 70.78 C ANISOU 507 C ILE A 76 10925 8143 7824 393 -348 123 ATOM 508 O ILE A 76 -13.483 1.048 20.638 1.00 70.91 O ANISOU 508 O ILE A 76 10979 8156 7808 361 -310 170 ATOM 509 CB ILE A 76 -16.054 1.094 22.706 1.00 0.00 C ATOM 510 CG1 ILE A 76 -16.240 -0.282 22.011 1.00 0.00 C ATOM 511 CG2 ILE A 76 -17.406 1.688 23.146 1.00 0.00 C ATOM 512 CD1 ILE A 76 -16.799 -1.369 22.940 1.00 0.00 C ATOM 513 N THR A 77 -12.974 1.739 22.727 1.00 71.45 N ANISOU 513 N THR A 77 10941 8253 7951 391 -327 76 ATOM 514 CA THR A 77 -11.745 0.967 22.924 1.00 71.69 C ANISOU 514 CA THR A 77 10941 8308 7989 354 -259 76 ATOM 515 C THR A 77 -12.129 -0.502 23.181 1.00 71.08 C ANISOU 515 C THR A 77 10896 8221 7889 364 -246 90 ATOM 516 O THR A 77 -13.162 -0.770 23.799 1.00 72.42 O ANISOU 516 O THR A 77 11090 8366 8058 406 -291 79 ATOM 517 CB THR A 77 -10.949 1.559 24.119 1.00 0.00 C ATOM 518 OG1 THR A 77 -11.704 1.621 25.325 1.00 0.00 O ATOM 519 CG2 THR A 77 -10.408 2.964 23.824 1.00 0.00 C ATOM 520 N ILE A 78 -11.333 -1.445 22.681 1.00 69.71 N ANISOU 520 N ILE A 78 10725 8062 7697 323 -188 115 ATOM 521 CA ILE A 78 -11.779 -2.809 22.418 1.00 68.88 C ANISOU 521 CA ILE A 78 10656 7951 7565 322 -174 131 ATOM 522 C ILE A 78 -10.701 -3.807 22.871 1.00 68.35 C ANISOU 522 C ILE A 78 10543 7920 7505 299 -116 108 ATOM 523 O ILE A 78 -9.556 -3.422 23.120 1.00 68.17 O ANISOU 523 O ILE A 78 10469 7928 7502 273 -78 97 ATOM 524 CB ILE A 78 -12.076 -2.949 20.885 1.00 0.00 C ATOM 525 CG1 ILE A 78 -12.971 -4.147 20.499 1.00 0.00 C ATOM 526 CG2 ILE A 78 -10.814 -2.936 20.001 1.00 0.00 C ATOM 527 CD1 ILE A 78 -14.346 -4.139 21.182 1.00 0.00 C ATOM 528 N HIS A 79 -11.097 -5.080 22.974 1.00 67.47 N ANISOU 528 N HIS A 79 10455 7804 7375 307 -109 101 ATOM 529 CA HIS A 79 -10.205 -6.214 23.199 1.00 67.24 C ANISOU 529 CA HIS A 79 10398 7813 7336 279 -50 89 ATOM 530 C HIS A 79 -9.192 -6.391 22.049 1.00 66.61 C ANISOU 530 C HIS A 79 10326 7752 7228 221 -4 147 ATOM 531 O HIS A 79 -9.472 -6.081 20.887 1.00 66.48 O ANISOU 531 O HIS A 79 10352 7714 7193 207 -19 198 ATOM 532 CB HIS A 79 -11.018 -7.503 23.438 1.00 0.00 C ATOM 533 CG HIS A 79 -12.102 -7.738 22.427 1.00 0.00 C ATOM 534 ND1 HIS A 79 -13.429 -7.359 22.650 1.00 0.00 N ATOM 535 CD2 HIS A 79 -11.985 -8.211 21.145 1.00 0.00 C ATOM 536 CE1 HIS A 79 -14.057 -7.627 21.512 1.00 0.00 C ATOM 537 NE2 HIS A 79 -13.242 -8.119 20.582 1.00 0.00 N ATOM 538 N PHE A 80 -8.002 -6.865 22.427 1.00 66.19 N ANISOU 538 N PHE A 80 10233 7741 7172 188 52 141 ATOM 539 CA PHE A 80 -6.800 -6.869 21.599 1.00 65.52 C ANISOU 539 CA PHE A 80 10159 7674 7060 134 96 201 ATOM 540 C PHE A 80 -6.918 -7.573 20.242 1.00 65.16 C ANISOU 540 C PHE A 80 10179 7610 6966 120 87 253 ATOM 541 O PHE A 80 -6.408 -7.035 19.260 1.00 64.64 O ANISOU 541 O PHE A 80 10140 7536 6884 96 91 312 ATOM 542 CB PHE A 80 -5.564 -7.318 22.410 1.00 65.67 C ANISOU 542 CB PHE A 80 10129 7745 7077 101 157 188 ATOM 543 CG PHE A 80 -5.785 -8.446 23.408 1.00 65.09 C ANISOU 543 CG PHE A 80 10058 7688 6982 47 201 251 ATOM 544 CD1 PHE A 80 -5.955 -9.777 22.970 1.00 64.92 C ANISOU 544 CD1 PHE A 80 10008 7666 6990 25 216 269 ATOM 545 CD2 PHE A 80 -5.935 -8.153 24.781 1.00 64.61 C ANISOU 545 CD2 PHE A 80 10032 7642 6874 19 223 294 ATOM 546 CE1 PHE A 80 -6.203 -10.785 23.892 1.00 64.66 C ANISOU 546 CE1 PHE A 80 9982 7642 6942 -19 254 329 ATOM 547 CE2 PHE A 80 -6.185 -9.176 25.685 1.00 64.36 C ANISOU 547 CE2 PHE A 80 10002 7626 6824 -26 260 356 ATOM 548 CZ PHE A 80 -6.312 -10.486 25.244 1.00 64.55 C ANISOU 548 CZ PHE A 80 9999 7645 6881 -43 276 374 ATOM 549 N TYR A 81 -7.614 -8.719 20.176 1.00 65.59 N ANISOU 549 N TYR A 81 10259 7660 7000 135 74 230 ATOM 550 CA TYR A 81 -7.718 -9.488 18.935 1.00 65.38 C ANISOU 550 CA TYR A 81 10291 7620 6928 115 63 275 ATOM 551 C TYR A 81 -8.574 -8.804 17.853 1.00 64.57 C ANISOU 551 C TYR A 81 10237 7476 6820 126 16 318 ATOM 552 O TYR A 81 -8.289 -8.987 16.669 1.00 64.25 O ANISOU 552 O TYR A 81 10228 7436 6746 95 21 380 ATOM 553 CB TYR A 81 -8.165 -10.931 19.239 1.00 0.00 C ATOM 554 CG TYR A 81 -9.388 -11.083 20.131 1.00 0.00 C ATOM 555 CD1 TYR A 81 -9.239 -11.129 21.534 1.00 0.00 C ATOM 556 CD2 TYR A 81 -10.672 -11.208 19.561 1.00 0.00 C ATOM 557 CE1 TYR A 81 -10.368 -11.290 22.359 1.00 0.00 C ATOM 558 CE2 TYR A 81 -11.799 -11.382 20.386 1.00 0.00 C ATOM 559 CZ TYR A 81 -11.648 -11.417 21.787 1.00 0.00 C ATOM 560 OH TYR A 81 -12.734 -11.560 22.596 1.00 0.00 O ATOM 561 N SER A 82 -9.556 -7.979 18.250 1.00 64.18 N ANISOU 561 N SER A 82 10188 7395 6800 170 -27 286 ATOM 562 CA SER A 82 -10.347 -7.202 17.300 1.00 63.78 C ANISOU 562 CA SER A 82 10181 7309 6743 184 -73 323 ATOM 563 C SER A 82 -9.552 -6.019 16.731 1.00 63.21 C ANISOU 563 C SER A 82 10105 7248 6662 160 -52 375 ATOM 564 O SER A 82 -9.586 -5.836 15.513 1.00 62.31 O ANISOU 564 O SER A 82 10029 7125 6518 145 -60 432 ATOM 565 CB SER A 82 -11.691 -6.766 17.908 1.00 0.00 C ATOM 566 OG SER A 82 -12.619 -7.842 17.865 1.00 0.00 O ATOM 567 N CYS A 83 -8.809 -5.306 17.580 1.00 63.30 N ANISOU 567 N CYS A 83 10069 7278 6703 156 -25 353 ATOM 568 CA CYS A 83 -7.929 -4.241 17.130 1.00 63.04 C ANISOU 568 CA CYS A 83 10031 7250 6668 136 -2 393 ATOM 569 C CYS A 83 -6.777 -4.814 16.282 1.00 62.51 C ANISOU 569 C CYS A 83 9972 7207 6571 93 42 450 ATOM 570 O CYS A 83 -6.442 -4.234 15.248 1.00 62.57 O ANISOU 570 O CYS A 83 10002 7210 6559 83 48 504 ATOM 571 CB CYS A 83 -7.409 -3.474 18.349 1.00 63.56 C ANISOU 571 CB CYS A 83 10044 7326 6776 137 13 353 ATOM 572 SG CYS A 83 -6.504 -1.977 17.895 1.00 63.93 S ANISOU 572 SG CYS A 83 10095 7364 6830 121 28 388 ATOM 573 N LEU A 84 -6.241 -5.993 16.653 1.00 62.10 N ANISOU 573 N LEU A 84 9899 7181 6511 71 74 438 ATOM 574 CA LEU A 84 -5.235 -6.694 15.848 1.00 61.80 C ANISOU 574 CA LEU A 84 9869 7170 6440 30 112 493 ATOM 575 C LEU A 84 -5.766 -7.082 14.461 1.00 61.15 C ANISOU 575 C LEU A 84 9837 7077 6317 24 88 545 ATOM 576 O LEU A 84 -5.066 -6.892 13.463 1.00 60.64 O ANISOU 576 O LEU A 84 9783 7025 6232 1 106 607 ATOM 577 CB LEU A 84 -4.713 -7.935 16.583 1.00 62.53 C ANISOU 577 CB LEU A 84 9936 7297 6524 9 145 466 ATOM 578 CG LEU A 84 -3.580 -8.736 15.912 1.00 62.49 C ANISOU 578 CG LEU A 84 9934 7327 6482 -36 184 521 ATOM 579 CD1 LEU A 84 -2.378 -7.855 15.584 1.00 62.45 C ANISOU 579 CD1 LEU A 84 9911 7328 6486 -56 217 572 ATOM 580 CD2 LEU A 84 -3.167 -9.919 16.780 1.00 62.85 C ANISOU 580 CD2 LEU A 84 9952 7410 6515 -53 216 484 ATOM 581 N PHE A 85 -6.970 -7.667 14.383 1.00 60.98 N ANISOU 581 N PHE A 85 9845 7034 6288 43 46 521 ATOM 582 CA PHE A 85 -7.549 -8.093 13.104 1.00 60.60 C ANISOU 582 CA PHE A 85 9845 6973 6204 32 18 569 ATOM 583 C PHE A 85 -7.783 -6.921 12.134 1.00 58.82 C ANISOU 583 C PHE A 85 9640 6735 5974 42 2 618 ATOM 584 O PHE A 85 -7.282 -6.929 11.008 1.00 58.09 O ANISOU 584 O PHE A 85 9566 6655 5850 19 8 681 ATOM 585 CB PHE A 85 -8.800 -8.973 13.333 1.00 0.00 C ATOM 586 CG PHE A 85 -9.652 -9.214 12.096 1.00 0.00 C ATOM 587 CD1 PHE A 85 -9.205 -10.101 11.094 1.00 0.00 C ATOM 588 CD2 PHE A 85 -10.780 -8.404 11.840 1.00 0.00 C ATOM 589 CE1 PHE A 85 -9.899 -10.203 9.896 1.00 0.00 C ATOM 590 CE2 PHE A 85 -11.459 -8.520 10.635 1.00 0.00 C ATOM 591 CZ PHE A 85 -11.022 -9.417 9.669 1.00 0.00 C ATOM 592 N MET A 86 -8.473 -5.891 12.639 1.00 57.80 N ANISOU 592 N MET A 86 9503 6583 5872 77 -17 586 ATOM 593 CA MET A 86 -8.853 -4.649 11.967 1.00 56.85 C ANISOU 593 CA MET A 86 9404 6452 5745 92 -32 622 ATOM 594 C MET A 86 -7.672 -3.910 11.318 1.00 55.65 C ANISOU 594 C MET A 86 9234 6321 5588 76 11 665 ATOM 595 O MET A 86 -7.846 -3.207 10.325 1.00 55.45 O ANISOU 595 O MET A 86 9229 6297 5540 80 10 713 ATOM 596 CB MET A 86 -9.542 -3.783 13.039 1.00 0.00 C ATOM 597 CG MET A 86 -9.894 -2.350 12.633 1.00 0.00 C ATOM 598 SD MET A 86 -10.833 -1.522 13.930 1.00 0.00 S ATOM 599 CE MET A 86 -12.530 -1.788 13.355 1.00 0.00 C ATOM 600 N THR A 87 -6.481 -4.071 11.888 1.00 54.72 N ANISOU 600 N THR A 87 9081 6220 5490 60 51 649 ATOM 601 CA THR A 87 -5.277 -3.348 11.514 1.00 54.06 C ANISOU 601 CA THR A 87 8983 6149 5407 46 93 690 ATOM 602 C THR A 87 -4.586 -3.985 10.280 1.00 53.53 C ANISOU 602 C THR A 87 8926 6108 5303 18 115 764 ATOM 603 O THR A 87 -3.935 -3.288 9.502 1.00 53.69 O ANISOU 603 O THR A 87 8944 6135 5321 18 140 807 ATOM 604 CB THR A 87 -4.342 -3.386 12.757 1.00 0.00 C ATOM 605 OG1 THR A 87 -4.843 -2.550 13.793 1.00 0.00 O ATOM 606 CG2 THR A 87 -2.963 -2.836 12.458 1.00 0.00 C ATOM 607 N CYS A 88 -4.726 -5.299 10.089 1.00 53.08 N ANISOU 607 N CYS A 88 8881 6066 5220 -2 104 776 ATOM 608 CA CYS A 88 -4.039 -6.080 9.037 1.00 52.83 C ANISOU 608 CA CYS A 88 8851 6066 5154 -36 124 843 ATOM 609 C CYS A 88 -4.395 -5.820 7.550 1.00 52.45 C ANISOU 609 C CYS A 88 8827 6026 5075 -36 111 910 ATOM 610 O CYS A 88 -3.490 -5.844 6.694 1.00 52.26 O ANISOU 610 O CYS A 88 8791 6029 5035 -51 138 971 ATOM 611 CB CYS A 88 -4.155 -7.576 9.343 1.00 53.20 C ANISOU 611 CB CYS A 88 8900 6129 5182 -65 119 826 ATOM 612 SG CYS A 88 -3.370 -8.056 10.913 1.00 53.67 S ANISOU 612 SG CYS A 88 8922 6200 5267 -74 152 765 ATOM 613 N LEU A 89 -5.664 -5.483 7.295 1.00 52.23 N ANISOU 613 N LEU A 89 8828 5977 5037 -21 69 903 ATOM 614 CA LEU A 89 -6.222 -5.200 5.972 1.00 51.86 C ANISOU 614 CA LEU A 89 8800 5945 4959 -25 59 969 ATOM 615 C LEU A 89 -5.358 -4.223 5.155 1.00 51.37 C ANISOU 615 C LEU A 89 8722 5900 4894 -9 93 1016 ATOM 616 O LEU A 89 -4.964 -4.553 4.038 1.00 51.23 O ANISOU 616 O LEU A 89 8698 5914 4850 -26 107 1084 ATOM 617 CB LEU A 89 -7.675 -4.686 6.123 1.00 0.00 C ATOM 618 CG LEU A 89 -8.693 -5.707 6.693 1.00 0.00 C ATOM 619 CD1 LEU A 89 -8.734 -7.019 5.885 1.00 0.00 C ATOM 620 CD2 LEU A 89 -8.580 -5.957 8.208 1.00 0.00 C ATOM 621 N LEU A 90 -4.987 -3.063 5.717 1.00 51.16 N ANISOU 621 N LEU A 90 8689 5852 4896 23 105 980 ATOM 622 CA LEU A 90 -4.154 -2.101 4.993 1.00 51.07 C ANISOU 622 CA LEU A 90 8667 5848 4887 43 140 1012 ATOM 623 C LEU A 90 -2.737 -2.642 4.763 1.00 50.79 C ANISOU 623 C LEU A 90 8604 5837 4855 21 181 1055 ATOM 624 O LEU A 90 -2.161 -2.358 3.721 1.00 50.70 O ANISOU 624 O LEU A 90 8586 5847 4830 29 204 1113 ATOM 625 CB LEU A 90 -4.083 -0.746 5.730 1.00 0.00 C ATOM 626 CG LEU A 90 -3.407 0.411 4.935 1.00 0.00 C ATOM 627 CD1 LEU A 90 -3.994 0.629 3.526 1.00 0.00 C ATOM 628 CD2 LEU A 90 -3.424 1.727 5.730 1.00 0.00 C ATOM 629 N LEU A 91 -2.194 -3.451 5.679 1.00 50.58 N ANISOU 629 N LEU A 91 8562 5812 4843 -4 189 1029 ATOM 630 CA LEU A 91 -0.862 -4.040 5.567 1.00 50.35 C ANISOU 630 CA LEU A 91 8509 5809 4813 -30 225 1071 ATOM 631 C LEU A 91 -0.802 -5.052 4.408 1.00 50.32 C ANISOU 631 C LEU A 91 8504 5846 4769 -56 221 1141 ATOM 632 O LEU A 91 0.145 -5.006 3.626 1.00 50.42 O ANISOU 632 O LEU A 91 8499 5883 4774 -59 247 1202 ATOM 633 CB LEU A 91 -0.439 -4.692 6.907 1.00 50.16 C ANISOU 633 CB LEU A 91 8469 5785 4804 -56 233 1027 ATOM 634 CG LEU A 91 -0.605 -3.788 8.156 1.00 50.20 C ANISOU 634 CG LEU A 91 8466 5756 4851 -39 236 956 ATOM 635 CD1 LEU A 91 -0.156 -4.523 9.426 1.00 50.33 C ANISOU 635 CD1 LEU A 91 8460 5785 4875 -68 249 922 ATOM 636 CD2 LEU A 91 0.140 -2.449 8.018 1.00 50.27 C ANISOU 636 CD2 LEU A 91 8468 5744 4888 -18 263 969 ATOM 637 N ILE A 92 -1.844 -5.880 4.210 1.00 50.29 N ANISOU 637 N ILE A 92 8518 5848 4741 -76 185 1132 ATOM 638 CA ILE A 92 -1.987 -6.737 3.024 1.00 50.57 C ANISOU 638 CA ILE A 92 8555 5921 4737 -107 173 1196 ATOM 639 C ILE A 92 -2.057 -5.866 1.768 1.00 51.03 C ANISOU 639 C ILE A 92 8610 5994 4783 -84 180 1255 ATOM 640 O ILE A 92 -1.253 -6.021 0.816 1.00 51.60 O ANISOU 640 O ILE A 92 8659 6105 4840 -93 201 1324 ATOM 641 CB ILE A 92 -3.260 -7.624 3.092 1.00 50.59 C ANISOU 641 CB ILE A 92 8586 5914 4721 -131 128 1170 ATOM 642 CG1 ILE A 92 -3.198 -8.586 4.287 1.00 50.79 C ANISOU 642 CG1 ILE A 92 8613 5929 4754 -150 124 1108 ATOM 643 CG2 ILE A 92 -3.453 -8.413 1.793 1.00 50.63 C ANISOU 643 CG2 ILE A 92 8593 5957 4687 -169 111 1239 ATOM 644 CD1 ILE A 92 -4.552 -9.083 4.752 1.00 50.89 C ANISOU 644 CD1 ILE A 92 8659 5911 4766 -151 80 1055 ATOM 645 N PHE A 93 -3.025 -4.931 1.733 1.00 51.30 N ANISOU 645 N PHE A 93 8665 6003 4822 -52 163 1229 ATOM 646 CA PHE A 93 -3.335 -4.137 0.533 1.00 51.49 C ANISOU 646 CA PHE A 93 8690 6046 4826 -31 166 1280 ATOM 647 C PHE A 93 -2.187 -3.203 0.128 1.00 51.89 C ANISOU 647 C PHE A 93 8717 6109 4889 0 211 1314 ATOM 648 O PHE A 93 -1.915 -3.060 -1.068 1.00 52.00 O ANISOU 648 O PHE A 93 8712 6161 4881 3 226 1382 ATOM 649 CB PHE A 93 -4.638 -3.331 0.712 1.00 0.00 C ATOM 650 CG PHE A 93 -5.860 -4.116 1.164 1.00 0.00 C ATOM 651 CD1 PHE A 93 -6.887 -3.442 1.854 1.00 0.00 C ATOM 652 CD2 PHE A 93 -6.044 -5.475 0.823 1.00 0.00 C ATOM 653 CE1 PHE A 93 -7.999 -4.141 2.298 1.00 0.00 C ATOM 654 CE2 PHE A 93 -7.165 -6.157 1.270 1.00 0.00 C ATOM 655 CZ PHE A 93 -8.130 -5.497 2.018 1.00 0.00 C ATOM 656 N THR A 94 -1.445 -2.642 1.093 1.00 52.42 N ANISOU 656 N THR A 94 8783 6142 4992 24 231 1266 ATOM 657 CA THR A 94 -0.242 -1.830 0.859 1.00 53.08 C ANISOU 657 CA THR A 94 8848 6224 5093 54 272 1292 ATOM 658 C THR A 94 0.842 -2.721 0.235 1.00 53.59 C ANISOU 658 C THR A 94 8884 6327 5151 29 294 1358 ATOM 659 O THR A 94 1.483 -2.313 -0.735 1.00 54.02 O ANISOU 659 O THR A 94 8921 6403 5201 53 320 1415 ATOM 660 CB THR A 94 0.297 -1.205 2.181 1.00 52.98 C ANISOU 660 CB THR A 94 8842 6163 5123 73 286 1227 ATOM 661 OG1 THR A 94 -0.678 -0.370 2.773 1.00 53.05 O ANISOU 661 OG1 THR A 94 8877 6141 5138 95 260 1165 ATOM 662 CG2 THR A 94 1.538 -0.311 2.001 1.00 53.15 C ANISOU 662 CG2 THR A 94 8855 6173 5166 108 325 1252 ATOM 663 N HIS A 95 1.011 -3.954 0.741 1.00 53.94 N ANISOU 663 N HIS A 95 8922 6381 5190 -15 284 1352 ATOM 664 CA HIS A 95 2.015 -4.874 0.184 1.00 54.40 C ANISOU 664 CA HIS A 95 8953 6481 5235 -44 298 1416 ATOM 665 C HIS A 95 1.679 -5.364 -1.231 1.00 55.07 C ANISOU 665 C HIS A 95 9025 6617 5282 -57 286 1489 ATOM 666 O HIS A 95 2.574 -5.423 -2.080 1.00 55.57 O ANISOU 666 O HIS A 95 9059 6715 5338 -52 308 1558 ATOM 667 CB HIS A 95 2.363 -6.006 1.169 1.00 0.00 C ATOM 668 CG HIS A 95 3.412 -5.557 2.150 1.00 0.00 C ATOM 669 ND1 HIS A 95 4.721 -5.299 1.738 1.00 0.00 N ATOM 670 CD2 HIS A 95 3.310 -5.261 3.493 1.00 0.00 C ATOM 671 CE1 HIS A 95 5.334 -4.817 2.808 1.00 0.00 C ATOM 672 NE2 HIS A 95 4.550 -4.783 3.881 1.00 0.00 N ATOM 673 N ALA A 96 0.386 -5.593 -1.495 1.00 55.71 N ANISOU 673 N ALA A 96 9124 6701 5339 -74 252 1476 ATOM 674 CA ALA A 96 -0.140 -5.905 -2.827 1.00 56.47 C ANISOU 674 CA ALA A 96 9208 6846 5401 -91 238 1545 ATOM 675 C ALA A 96 0.189 -4.816 -3.853 1.00 57.35 C ANISOU 675 C ALA A 96 9297 6978 5513 -43 269 1596 ATOM 676 O ALA A 96 0.559 -5.142 -4.983 1.00 57.66 O ANISOU 676 O ALA A 96 9303 7070 5535 -51 279 1672 ATOM 677 CB ALA A 96 -1.651 -6.179 -2.756 1.00 0.00 C ATOM 678 N SER A 97 0.124 -3.548 -3.424 1.00 58.10 N ANISOU 678 N SER A 97 9411 7036 5629 6 284 1552 ATOM 679 CA SER A 97 0.453 -2.411 -4.293 1.00 58.85 C ANISOU 679 CA SER A 97 9491 7145 5724 60 316 1587 ATOM 680 C SER A 97 1.913 -2.412 -4.758 1.00 59.42 C ANISOU 680 C SER A 97 9527 7237 5811 79 352 1641 ATOM 681 O SER A 97 2.196 -2.229 -5.956 1.00 59.58 O ANISOU 681 O SER A 97 9517 7304 5816 100 370 1708 ATOM 682 CB SER A 97 0.144 -1.090 -3.588 1.00 58.92 C ANISOU 682 CB SER A 97 9530 7101 5754 109 325 1518 ATOM 683 OG SER A 97 -1.203 -1.045 -3.145 1.00 59.21 O ANISOU 683 OG SER A 97 9599 7120 5778 96 289 1471 ATOM 684 N ILE A 98 2.821 -2.653 -3.809 1.00 59.81 N ANISOU 684 N ILE A 98 9580 7254 5890 72 362 1614 ATOM 685 CA ILE A 98 4.268 -2.596 -4.059 1.00 60.18 C ANISOU 685 CA ILE A 98 9601 7308 5957 91 395 1661 ATOM 686 C ILE A 98 4.650 -3.672 -5.077 1.00 60.47 C ANISOU 686 C ILE A 98 9598 7412 5965 58 389 1747 ATOM 687 O ILE A 98 5.321 -3.380 -6.091 1.00 60.61 O ANISOU 687 O ILE A 98 9582 7462 5981 91 412 1813 ATOM 688 CB ILE A 98 5.080 -2.780 -2.748 1.00 60.35 C ANISOU 688 CB ILE A 98 9634 7282 6012 77 402 1618 ATOM 689 CG1 ILE A 98 4.772 -1.647 -1.758 1.00 60.36 C ANISOU 689 CG1 ILE A 98 9668 7218 6045 108 407 1536 ATOM 690 CG2 ILE A 98 6.588 -2.820 -3.031 1.00 60.94 C ANISOU 690 CG2 ILE A 98 9684 7364 6107 91 433 1677 ATOM 691 CD1 ILE A 98 5.069 -1.996 -0.315 1.00 60.39 C ANISOU 691 CD1 ILE A 98 9685 7185 6075 77 403 1479 ATOM 692 N MET A 99 4.179 -4.895 -4.788 1.00 60.52 N ANISOU 692 N MET A 99 9608 7439 5947 -4 356 1743 ATOM 693 CA MET A 99 4.361 -6.093 -5.596 1.00 61.07 C ANISOU 693 CA MET A 99 9643 7574 5984 -47 341 1818 ATOM 694 C MET A 99 3.780 -5.931 -7.010 1.00 61.63 C ANISOU 694 C MET A 99 9689 7697 6028 -41 334 1876 ATOM 695 O MET A 99 4.463 -6.268 -7.977 1.00 61.85 O ANISOU 695 O MET A 99 9673 7782 6043 -42 342 1956 ATOM 696 CB MET A 99 3.734 -7.297 -4.864 1.00 0.00 C ATOM 697 CG MET A 99 4.453 -7.713 -3.568 1.00 0.00 C ATOM 698 SD MET A 99 6.097 -8.455 -3.789 1.00 0.00 S ATOM 699 CE MET A 99 5.665 -10.026 -4.588 1.00 0.00 C ATOM 700 N SER A 100 2.567 -5.366 -7.118 1.00 61.94 N ANISOU 700 N SER A 100 9756 7720 6059 -35 320 1837 ATOM 701 CA SER A 100 1.949 -5.081 -8.410 1.00 62.25 C ANISOU 701 CA SER A 100 9773 7805 6073 -24 320 1888 ATOM 702 C SER A 100 2.694 -3.958 -9.166 1.00 62.55 C ANISOU 702 C SER A 100 9777 7864 6123 45 366 1932 ATOM 703 O SER A 100 2.849 -4.073 -10.382 1.00 62.89 O ANISOU 703 O SER A 100 9775 7972 6147 46 373 2009 ATOM 704 CB SER A 100 0.432 -4.823 -8.253 1.00 0.00 C ATOM 705 OG SER A 100 -0.251 -5.105 -9.464 1.00 0.00 O ATOM 706 N LEU A 101 3.227 -2.939 -8.462 1.00 62.63 N ANISOU 706 N LEU A 101 9809 7820 6167 101 395 1884 ATOM 707 CA LEU A 101 4.097 -1.948 -9.126 1.00 63.15 C ANISOU 707 CA LEU A 101 9849 7893 6250 173 440 1918 ATOM 708 C LEU A 101 5.411 -2.563 -9.638 1.00 63.22 C ANISOU 708 C LEU A 101 9813 7938 6270 173 453 1992 ATOM 709 O LEU A 101 5.846 -2.280 -10.776 1.00 63.66 O ANISOU 709 O LEU A 101 9824 8043 6320 212 477 2059 ATOM 710 CB LEU A 101 4.391 -0.761 -8.199 1.00 63.12 C ANISOU 710 CB LEU A 101 9886 7814 6283 227 463 1843 ATOM 711 CG LEU A 101 3.193 0.183 -7.977 1.00 63.01 C ANISOU 711 CG LEU A 101 9909 7775 6256 249 458 1781 ATOM 712 CD1 LEU A 101 3.359 0.986 -6.696 1.00 62.88 C ANISOU 712 CD1 LEU A 101 9938 7678 6275 273 463 1694 ATOM 713 CD2 LEU A 101 2.983 1.114 -9.165 1.00 63.29 C ANISOU 713 CD2 LEU A 101 9924 7851 6270 305 488 1817 ATOM 714 N LEU A 102 6.029 -3.402 -8.802 1.00 62.93 N ANISOU 714 N LEU A 102 9786 7880 6245 132 439 1981 ATOM 715 CA LEU A 102 7.244 -4.128 -9.207 1.00 63.38 C ANISOU 715 CA LEU A 102 9803 7973 6306 122 444 2054 ATOM 716 C LEU A 102 7.008 -5.002 -10.449 1.00 63.76 C ANISOU 716 C LEU A 102 9800 8109 6314 86 424 2137 ATOM 717 O LEU A 102 7.857 -5.034 -11.358 1.00 63.87 O ANISOU 717 O LEU A 102 9766 8170 6332 113 440 2214 ATOM 718 CB LEU A 102 7.797 -4.971 -8.052 1.00 63.19 C ANISOU 718 CB LEU A 102 9799 7917 6290 74 429 2026 ATOM 719 CG LEU A 102 9.110 -5.733 -8.295 1.00 63.64 C ANISOU 719 CG LEU A 102 9822 8007 6349 60 433 2098 ATOM 720 CD1 LEU A 102 10.291 -4.827 -8.616 1.00 64.04 C ANISOU 720 CD1 LEU A 102 9857 8036 6438 133 472 2135 ATOM 721 CD2 LEU A 102 9.448 -6.573 -7.073 1.00 63.49 C ANISOU 721 CD2 LEU A 102 9831 7962 6331 6 418 2060 ATOM 722 N ALA A 103 5.861 -5.691 -10.488 1.00 63.93 N ANISOU 722 N ALA A 103 9834 8152 6303 25 387 2122 ATOM 723 CA ALA A 103 5.457 -6.431 -11.701 1.00 64.40 C ANISOU 723 CA ALA A 103 9849 8294 6326 -15 364 2196 ATOM 724 C ALA A 103 5.397 -5.520 -12.946 1.00 65.29 C ANISOU 724 C ALA A 103 9917 8452 6435 43 395 2251 ATOM 725 O ALA A 103 5.938 -5.863 -14.017 1.00 65.87 O ANISOU 725 O ALA A 103 9931 8597 6499 44 398 2336 ATOM 726 CB ALA A 103 4.118 -7.127 -11.487 1.00 63.97 C ANISOU 726 CB ALA A 103 9824 8238 6241 -84 320 2162 ATOM 727 N ILE A 104 4.758 -4.357 -12.784 1.00 65.71 N ANISOU 727 N ILE A 104 9999 8468 6498 92 417 2200 ATOM 728 CA ILE A 104 4.669 -3.348 -13.850 1.00 66.78 C ANISOU 728 CA ILE A 104 10100 8643 6628 157 454 2237 ATOM 729 C ILE A 104 6.060 -2.899 -14.299 1.00 67.73 C ANISOU 729 C ILE A 104 10181 8774 6778 226 493 2284 ATOM 730 O ILE A 104 6.318 -2.815 -15.508 1.00 69.01 O ANISOU 730 O ILE A 104 10282 9007 6929 253 511 2359 ATOM 731 CB ILE A 104 3.835 -2.111 -13.427 1.00 66.94 C ANISOU 731 CB ILE A 104 10167 8613 6651 202 472 2163 ATOM 732 CG1 ILE A 104 2.354 -2.486 -13.284 1.00 66.75 C ANISOU 732 CG1 ILE A 104 10173 8593 6595 140 433 2137 ATOM 733 CG2 ILE A 104 3.970 -0.977 -14.440 1.00 67.55 C ANISOU 733 CG2 ILE A 104 10212 8727 6725 281 519 2195 ATOM 734 CD1 ILE A 104 1.500 -1.443 -12.584 1.00 66.64 C ANISOU 734 CD1 ILE A 104 10215 8520 6582 172 439 2055 ATOM 735 N ALA A 105 6.940 -2.607 -13.337 1.00 67.85 N ANISOU 735 N ALA A 105 10229 8719 6831 254 507 2242 ATOM 736 CA ALA A 105 8.330 -2.211 -13.661 1.00 68.48 C ANISOU 736 CA ALA A 105 10279 8794 6944 320 541 2285 ATOM 737 C ALA A 105 9.083 -3.265 -14.488 1.00 68.64 C ANISOU 737 C ALA A 105 10236 8890 6953 291 526 2384 ATOM 738 O ALA A 105 9.667 -2.938 -15.537 1.00 68.63 O ANISOU 738 O ALA A 105 10179 8938 6958 347 552 2453 ATOM 739 CB ALA A 105 9.110 -1.894 -12.394 1.00 68.60 C ANISOU 739 CB ALA A 105 10345 8719 7001 336 550 2226 ATOM 740 N VAL A 106 9.052 -4.519 -14.031 1.00 68.79 N ANISOU 740 N VAL A 106 10260 8921 6954 208 484 2391 ATOM 741 CA VAL A 106 9.710 -5.606 -14.780 1.00 69.87 C ANISOU 741 CA VAL A 106 10339 9134 7073 171 462 2484 ATOM 742 C VAL A 106 9.031 -5.878 -16.132 1.00 70.65 C ANISOU 742 C VAL A 106 10378 9328 7137 152 451 2550 ATOM 743 O VAL A 106 9.719 -6.211 -17.110 1.00 71.16 O ANISOU 743 O VAL A 106 10375 9462 7198 165 452 2639 ATOM 744 CB VAL A 106 9.892 -6.920 -13.963 1.00 69.48 C ANISOU 744 CB VAL A 106 10312 9079 7006 85 420 2473 ATOM 745 CG1 VAL A 106 10.685 -6.654 -12.694 1.00 69.21 C ANISOU 745 CG1 VAL A 106 10326 8962 7007 104 436 2420 ATOM 746 CG2 VAL A 106 8.570 -7.594 -13.627 1.00 69.12 C ANISOU 746 CG2 VAL A 106 10298 9036 6925 6 381 2425 ATOM 747 N ASP A 107 7.702 -5.725 -16.196 1.00 71.51 N ANISOU 747 N ASP A 107 10508 9440 7222 122 440 2512 ATOM 748 CA ASP A 107 7.003 -5.806 -17.493 1.00 73.04 C ANISOU 748 CA ASP A 107 10646 9721 7385 108 435 2575 ATOM 749 C ASP A 107 7.464 -4.696 -18.452 1.00 74.62 C ANISOU 749 C ASP A 107 10794 9955 7600 205 488 2618 ATOM 750 O ASP A 107 7.743 -4.966 -19.628 1.00 75.38 O ANISOU 750 O ASP A 107 10815 10140 7685 210 491 2706 ATOM 751 CB ASP A 107 5.480 -5.749 -17.335 1.00 72.53 C ANISOU 751 CB ASP A 107 10619 9644 7292 61 415 2527 ATOM 752 CG ASP A 107 4.751 -5.993 -18.651 1.00 72.72 C ANISOU 752 CG ASP A 107 10585 9763 7283 28 404 2599 ATOM 753 OD1 ASP A 107 4.876 -7.106 -19.202 1.00 72.72 O ANISOU 753 OD1 ASP A 107 10543 9824 7263 -38 368 2663 ATOM 754 OD2 ASP A 107 4.065 -5.072 -19.141 1.00 73.01 O1- ANISOU 754 OD2 ASP A 107 10615 9813 7310 67 433 2595 ATOM 755 N ARG A 108 7.536 -3.464 -17.947 1.00 75.52 N ANISOU 755 N ARG A 108 10951 10001 7741 282 529 2554 ATOM 756 CA ARG A 108 8.103 -2.344 -18.715 1.00 76.99 C ANISOU 756 CA ARG A 108 11100 10206 7946 387 583 2581 ATOM 757 C ARG A 108 9.556 -2.599 -19.139 1.00 78.49 C ANISOU 757 C ARG A 108 11238 10417 8164 429 595 2653 ATOM 758 O ARG A 108 9.938 -2.258 -20.263 1.00 79.60 O ANISOU 758 O ARG A 108 11311 10625 8308 487 624 2720 ATOM 759 CB ARG A 108 8.032 -1.029 -17.924 1.00 77.05 C ANISOU 759 CB ARG A 108 11173 10122 7978 457 619 2489 ATOM 760 CG ARG A 108 6.667 -0.354 -17.901 1.00 76.91 C ANISOU 760 CG ARG A 108 11189 10102 7931 452 625 2435 ATOM 761 CD ARG A 108 6.206 0.076 -19.292 1.00 77.59 C ANISOU 761 CD ARG A 108 11212 10282 7987 486 654 2495 ATOM 762 NE ARG A 108 5.152 -0.781 -19.829 1.00 77.55 N ANISOU 762 NE ARG A 108 11180 10347 7939 398 616 2537 ATOM 763 CZ ARG A 108 4.570 -0.610 -21.017 1.00 78.24 C ANISOU 763 CZ ARG A 108 11209 10524 7992 401 633 2596 ATOM 764 NH1 ARG A 108 4.932 0.385 -21.830 1.00 79.27 N ANISOU 764 NH1 ARG A 108 11298 10695 8126 495 689 2619 ATOM 765 NH2 ARG A 108 3.607 -1.448 -21.397 1.00 78.30 N1+ ANISOU 765 NH2 ARG A 108 11200 10584 7965 310 593 2632 ATOM 766 N TYR A 109 10.358 -3.182 -18.242 1.00 79.13 N ANISOU 766 N TYR A 109 11350 10446 8267 402 574 2640 ATOM 767 CA TYR A 109 11.731 -3.584 -18.587 1.00 80.49 C ANISOU 767 CA TYR A 109 11478 10641 8464 430 576 2715 ATOM 768 C TYR A 109 11.770 -4.612 -19.718 1.00 81.72 C ANISOU 768 C TYR A 109 11550 10911 8589 383 547 2817 ATOM 769 O TYR A 109 12.422 -4.384 -20.745 1.00 82.26 O ANISOU 769 O TYR A 109 11548 11038 8668 443 568 2893 ATOM 770 CB TYR A 109 12.455 -4.140 -17.359 1.00 80.51 C ANISOU 770 CB TYR A 109 11532 10572 8486 393 554 2683 ATOM 771 CG TYR A 109 13.864 -4.624 -17.631 1.00 81.37 C ANISOU 771 CG TYR A 109 11600 10700 8615 413 551 2764 ATOM 772 CD1 TYR A 109 14.902 -3.717 -17.866 1.00 82.06 C ANISOU 772 CD1 TYR A 109 11677 10753 8749 514 592 2786 ATOM 773 CD2 TYR A 109 14.165 -5.989 -17.652 1.00 81.45 C ANISOU 773 CD2 TYR A 109 11586 10764 8598 332 505 2818 ATOM 774 CE1 TYR A 109 16.197 -4.154 -18.116 1.00 82.64 C ANISOU 774 CE1 TYR A 109 11715 10841 8843 536 586 2865 ATOM 775 CE2 TYR A 109 15.458 -6.435 -17.898 1.00 82.13 C ANISOU 775 CE2 TYR A 109 11634 10870 8698 350 499 2896 ATOM 776 CZ TYR A 109 16.469 -5.514 -18.129 1.00 82.78 C ANISOU 776 CZ TYR A 109 11706 10916 8830 453 539 2922 ATOM 777 OH TYR A 109 17.749 -5.946 -18.376 1.00 83.71 O ANISOU 777 OH TYR A 109 11788 11052 8964 473 531 3004 ATOM 778 N LEU A 110 11.063 -5.730 -19.524 1.00 82.78 N ANISOU 778 N LEU A 110 11692 11075 8685 277 496 2816 ATOM 779 CA LEU A 110 11.083 -6.844 -20.491 1.00 84.08 C ANISOU 779 CA LEU A 110 11784 11345 8817 214 458 2908 ATOM 780 C LEU A 110 10.708 -6.456 -21.931 1.00 86.20 C ANISOU 780 C LEU A 110 11970 11709 9073 247 478 2976 ATOM 781 O LEU A 110 11.312 -6.962 -22.880 1.00 86.95 O ANISOU 781 O LEU A 110 11985 11889 9163 248 467 3070 ATOM 782 CB LEU A 110 10.183 -7.991 -20.019 1.00 83.19 C ANISOU 782 CB LEU A 110 11705 11237 8663 95 402 2879 ATOM 783 CG LEU A 110 10.704 -8.805 -18.830 1.00 82.57 C ANISOU 783 CG LEU A 110 11683 11103 8587 44 372 2840 ATOM 784 CD1 LEU A 110 9.578 -9.628 -18.218 1.00 82.21 C ANISOU 784 CD1 LEU A 110 11688 11041 8506 -54 328 2782 ATOM 785 CD2 LEU A 110 11.863 -9.702 -19.243 1.00 83.03 C ANISOU 785 CD2 LEU A 110 11688 11219 8638 26 349 2926 ATOM 786 N ARG A 111 9.725 -5.564 -22.085 1.00 87.85 N ANISOU 786 N ARG A 111 12197 11907 9274 274 507 2932 ATOM 787 CA ARG A 111 9.278 -5.111 -23.416 1.00 89.80 C ANISOU 787 CA ARG A 111 12367 12247 9504 306 533 2992 ATOM 788 C ARG A 111 10.418 -4.497 -24.220 1.00 91.58 C ANISOU 788 C ARG A 111 12524 12510 9761 414 578 3055 ATOM 789 O ARG A 111 10.704 -4.927 -25.342 1.00 92.77 O ANISOU 789 O ARG A 111 12582 12764 9902 411 572 3150 ATOM 790 CB ARG A 111 8.142 -4.088 -23.295 1.00 89.93 C ANISOU 790 CB ARG A 111 12426 12233 9508 332 565 2924 ATOM 791 CG ARG A 111 6.821 -4.679 -22.844 1.00 89.63 C ANISOU 791 CG ARG A 111 12437 12182 9435 228 521 2882 ATOM 792 CD ARG A 111 5.858 -3.597 -22.399 1.00 89.60 C ANISOU 792 CD ARG A 111 12494 12122 9424 261 550 2801 ATOM 793 NE ARG A 111 5.417 -2.754 -23.512 1.00 90.36 N ANISOU 793 NE ARG A 111 12536 12292 9503 314 594 2840 ATOM 794 CZ ARG A 111 4.472 -3.084 -24.401 1.00 91.35 C ANISOU 794 CZ ARG A 111 12616 12501 9589 256 580 2892 ATOM 795 NH1 ARG A 111 3.838 -4.257 -24.350 1.00 91.61 N ANISOU 795 NH1 ARG A 111 12655 12553 9600 141 519 2913 ATOM 796 NH2 ARG A 111 4.152 -2.227 -25.365 1.00 91.96 N1+ ANISOU 796 NH2 ARG A 111 12643 12646 9650 312 628 2925 ATOM 797 N VAL A 112 11.060 -3.494 -23.629 1.00 92.48 N ANISOU 797 N VAL A 112 12684 12539 9914 507 620 3002 ATOM 798 CA VAL A 112 12.202 -2.820 -24.251 1.00 94.10 C ANISOU 798 CA VAL A 112 12839 12758 10157 620 664 3049 ATOM 799 C VAL A 112 13.481 -3.685 -24.262 1.00 94.74 C ANISOU 799 C VAL A 112 12885 12851 10260 613 635 3121 ATOM 800 O VAL A 112 14.295 -3.565 -25.183 1.00 95.69 O ANISOU 800 O VAL A 112 12928 13029 10398 680 653 3200 ATOM 801 CB VAL A 112 12.460 -1.424 -23.619 1.00 94.49 C ANISOU 801 CB VAL A 112 12954 12703 10242 722 718 2965 ATOM 802 CG1 VAL A 112 12.961 -1.512 -22.174 1.00 93.84 C ANISOU 802 CG1 VAL A 112 12964 12502 10189 702 700 2895 ATOM 803 CG2 VAL A 112 13.424 -0.619 -24.480 1.00 95.71 C ANISOU 803 CG2 VAL A 112 13052 12882 10431 848 769 3013 ATOM 804 N LYS A 113 13.653 -4.549 -23.257 1.00 94.63 N ANISOU 804 N LYS A 113 12926 12786 10241 533 590 3094 ATOM 805 CA LYS A 113 14.858 -5.387 -23.162 1.00 95.30 C ANISOU 805 CA LYS A 113 12987 12880 10340 519 560 3158 ATOM 806 C LYS A 113 14.856 -6.555 -24.155 1.00 96.02 C ANISOU 806 C LYS A 113 12990 13095 10397 452 515 3259 ATOM 807 O LYS A 113 15.871 -6.802 -24.805 1.00 96.78 O ANISOU 807 O LYS A 113 13020 13242 10508 491 511 3346 ATOM 808 CB LYS A 113 15.050 -5.906 -21.728 1.00 94.75 C ANISOU 808 CB LYS A 113 13005 12720 10273 457 531 3094 ATOM 809 CG LYS A 113 16.323 -6.714 -21.481 1.00 94.88 C ANISOU 809 CG LYS A 113 13011 12738 10302 443 503 3154 ATOM 810 CD LYS A 113 17.590 -5.890 -21.636 1.00 95.52 C ANISOU 810 CD LYS A 113 13078 12777 10437 558 543 3188 ATOM 811 CE LYS A 113 18.824 -6.759 -21.437 1.00 96.20 C ANISOU 811 CE LYS A 113 13150 12871 10530 537 510 3259 ATOM 812 NZ LYS A 113 20.090 -5.987 -21.576 1.00 97.05 N1+ ANISOU 812 NZ LYS A 113 13249 12930 10694 648 545 3297 ATOM 813 N LEU A 114 13.748 -7.309 -24.202 1.00 96.37 N ANISOU 813 N LEU A 114 13035 13184 10394 349 477 3248 ATOM 814 CA LEU A 114 13.662 -8.625 -24.845 1.00 97.37 C ANISOU 814 CA LEU A 114 13085 13426 10484 267 427 3337 ATOM 815 C LEU A 114 12.624 -8.646 -25.978 1.00 98.04 C ANISOU 815 C LEU A 114 13127 13586 10537 228 427 3350 ATOM 816 O LEU A 114 12.163 -9.730 -26.328 1.00 98.22 O ANISOU 816 O LEU A 114 13168 13629 10522 118 380 3336 ATOM 817 CB LEU A 114 13.340 -9.714 -23.781 1.00 0.00 C ATOM 818 CG LEU A 114 14.448 -9.972 -22.738 1.00 0.00 C ATOM 819 CD1 LEU A 114 13.997 -11.030 -21.710 1.00 0.00 C ATOM 820 CD2 LEU A 114 15.792 -10.362 -23.389 1.00 0.00 C ATOM 821 N THR A 115 12.296 -7.471 -26.531 1.00 99.23 N ANISOU 821 N THR A 115 13219 13780 10702 318 480 3380 ATOM 822 CA THR A 115 11.226 -7.157 -27.488 1.00100.41 C ANISOU 822 CA THR A 115 13327 14000 10820 288 489 3393 ATOM 823 C THR A 115 10.773 -8.291 -28.447 1.00102.04 C ANISOU 823 C THR A 115 13452 14327 10991 187 436 3483 ATOM 824 O THR A 115 9.586 -8.618 -28.465 1.00102.16 O ANISOU 824 O THR A 115 13469 14373 10971 110 417 3474 ATOM 825 CB THR A 115 11.573 -5.848 -28.271 1.00 0.00 C ATOM 826 OG1 THR A 115 10.529 -5.417 -29.122 1.00 0.00 O ATOM 827 CG2 THR A 115 12.837 -5.924 -29.146 1.00 0.00 C ATOM 828 N VAL A 116 11.724 -8.937 -29.142 1.00103.88 N ANISOU 828 N VAL A 116 13614 14624 11229 185 408 3568 ATOM 829 CA VAL A 116 11.485 -10.037 -30.078 1.00105.42 C ANISOU 829 CA VAL A 116 13727 14936 11390 87 351 3657 ATOM 830 C VAL A 116 10.831 -11.264 -29.403 1.00105.72 C ANISOU 830 C VAL A 116 13831 14945 11391 -53 280 3619 ATOM 831 O VAL A 116 9.856 -11.804 -29.924 1.00106.77 O ANISOU 831 O VAL A 116 13938 15140 11490 -150 244 3644 ATOM 832 CB VAL A 116 12.818 -10.487 -30.754 1.00 0.00 C ATOM 833 CG1 VAL A 116 12.678 -11.687 -31.717 1.00 0.00 C ATOM 834 CG2 VAL A 116 13.499 -9.319 -31.492 1.00 0.00 C ATOM 835 N ARG A 117 11.370 -11.670 -28.247 1.00105.17 N ANISOU 835 N ARG A 117 13848 14781 11328 -64 263 3557 ATOM 836 CA ARG A 117 10.846 -12.796 -27.454 1.00104.67 C ANISOU 836 CA ARG A 117 13856 14681 11230 -187 200 3509 ATOM 837 C ARG A 117 9.775 -12.408 -26.404 1.00103.32 C ANISOU 837 C ARG A 117 13795 14404 11056 -209 211 3392 ATOM 838 O ARG A 117 9.248 -13.289 -25.700 1.00102.23 O ANISOU 838 O ARG A 117 13721 14228 10892 -304 163 3343 ATOM 839 CB ARG A 117 12.012 -13.535 -26.774 1.00104.97 C ANISOU 839 CB ARG A 117 13919 14693 11270 -196 170 3516 ATOM 840 CG ARG A 117 12.943 -14.251 -27.741 1.00105.70 C ANISOU 840 CG ARG A 117 13911 14896 11353 -206 137 3632 ATOM 841 CD ARG A 117 14.267 -14.640 -27.094 1.00106.09 C ANISOU 841 CD ARG A 117 13981 14913 11412 -180 125 3645 ATOM 842 NE ARG A 117 14.116 -15.604 -25.997 1.00105.59 N ANISOU 842 NE ARG A 117 14006 14794 11316 -273 80 3581 ATOM 843 CZ ARG A 117 14.186 -15.337 -24.684 1.00105.28 C ANISOU 843 CZ ARG A 117 14067 14644 11290 -256 101 3488 ATOM 844 NH1 ARG A 117 14.406 -14.104 -24.215 1.00105.25 N ANISOU 844 NH1 ARG A 117 14096 14560 11333 -153 164 3442 ATOM 845 NH2 ARG A 117 14.038 -16.333 -23.813 1.00104.92 N1+ ANISOU 845 NH2 ARG A 117 14087 14567 11208 -346 57 3439 ATOM 846 N TYR A 118 9.438 -11.114 -26.308 1.00102.76 N ANISOU 846 N TYR A 118 13744 14288 11011 -121 273 3348 ATOM 847 CA TYR A 118 8.483 -10.632 -25.296 1.00101.98 C ANISOU 847 CA TYR A 118 13746 14088 10912 -130 285 3240 ATOM 848 C TYR A 118 7.161 -11.402 -25.283 1.00102.78 C ANISOU 848 C TYR A 118 13878 14197 10975 -248 235 3218 ATOM 849 O TYR A 118 6.742 -11.882 -24.231 1.00102.24 O ANISOU 849 O TYR A 118 13895 14052 10897 -303 205 3142 ATOM 850 CB TYR A 118 8.182 -9.135 -25.469 1.00101.35 C ANISOU 850 CB TYR A 118 13669 13984 10855 -27 355 3209 ATOM 851 CG TYR A 118 7.126 -8.616 -24.508 1.00 99.95 C ANISOU 851 CG TYR A 118 13589 13713 10674 -38 363 3104 ATOM 852 CD1 TYR A 118 7.385 -8.528 -23.139 1.00 98.92 C ANISOU 852 CD1 TYR A 118 13549 13473 10563 -27 363 3016 ATOM 853 CD2 TYR A 118 5.861 -8.228 -24.961 1.00 99.03 C ANISOU 853 CD2 TYR A 118 13471 13619 10534 -63 370 3096 ATOM 854 CE1 TYR A 118 6.423 -8.062 -22.252 1.00 97.60 C ANISOU 854 CE1 TYR A 118 13465 13224 10394 -36 367 2921 ATOM 855 CE2 TYR A 118 4.893 -7.763 -24.080 1.00 98.15 C ANISOU 855 CE2 TYR A 118 13449 13423 10419 -72 373 3004 ATOM 856 CZ TYR A 118 5.180 -7.679 -22.727 1.00 97.25 C ANISOU 856 CZ TYR A 118 13421 13203 10326 -57 371 2916 ATOM 857 OH TYR A 118 4.229 -7.218 -21.845 1.00 96.12 O ANISOU 857 OH TYR A 118 13360 12980 10181 -64 372 2826 ATOM 858 N LYS A 119 6.514 -11.513 -26.444 1.00104.98 N ANISOU 858 N LYS A 119 14087 14568 11232 -287 226 3286 ATOM 859 CA LYS A 119 5.193 -12.151 -26.534 1.00105.75 C ANISOU 859 CA LYS A 119 14212 14671 11297 -398 179 3272 ATOM 860 C LYS A 119 5.205 -13.636 -26.169 1.00105.58 C ANISOU 860 C LYS A 119 14219 14646 11249 -513 103 3269 ATOM 861 O LYS A 119 4.258 -14.123 -25.548 1.00105.32 O ANISOU 861 O LYS A 119 14261 14556 11199 -588 67 3208 ATOM 862 CB LYS A 119 4.562 -11.950 -27.922 1.00107.38 C ANISOU 862 CB LYS A 119 14329 14984 11486 -419 186 3356 ATOM 863 CG LYS A 119 3.999 -10.553 -28.148 1.00108.52 C ANISOU 863 CG LYS A 119 14473 15120 11640 -335 254 3335 ATOM 864 CD LYS A 119 2.907 -10.539 -29.218 1.00110.19 C ANISOU 864 CD LYS A 119 14630 15413 11822 -394 248 3394 ATOM 865 CE LYS A 119 2.160 -9.215 -29.247 1.00110.78 C ANISOU 865 CE LYS A 119 14726 15466 11896 -324 309 3357 ATOM 866 NZ LYS A 119 3.025 -8.091 -29.706 1.00111.75 N1+ ANISOU 866 NZ LYS A 119 14792 15626 12042 -189 384 3379 ATOM 867 N ARG A 120 6.312 -14.302 -26.525 1.00105.93 N ANISOU 867 N ARG A 120 14206 14752 11290 -524 79 3334 ATOM 868 CA ARG A 120 6.599 -15.695 -26.194 1.00105.68 C ANISOU 868 CA ARG A 120 14206 14717 11229 -625 10 3326 ATOM 869 C ARG A 120 6.887 -15.876 -24.696 1.00101.96 C ANISOU 869 C ARG A 120 13833 14139 10766 -606 13 3232 ATOM 870 O ARG A 120 6.508 -16.895 -24.123 1.00101.83 O ANISOU 870 O ARG A 120 13878 14087 10724 -692 -36 3183 ATOM 871 CB ARG A 120 7.805 -16.193 -27.023 1.00 0.00 C ATOM 872 CG ARG A 120 7.686 -15.962 -28.541 1.00 0.00 C ATOM 873 CD ARG A 120 8.922 -16.457 -29.311 1.00 0.00 C ATOM 874 NE ARG A 120 8.727 -16.396 -30.770 1.00 0.00 N ATOM 875 CZ ARG A 120 8.194 -17.342 -31.566 1.00 0.00 C ATOM 876 NH1 ARG A 120 7.766 -18.517 -31.086 1.00 0.00 N ATOM 877 NH2 ARG A 120 8.089 -17.101 -32.875 1.00 0.00 N1+ ATOM 878 N VAL A 121 7.588 -14.898 -24.113 1.00 98.33 N ANISOU 878 N VAL A 121 13387 13628 10343 -497 71 3204 ATOM 879 CA VAL A 121 7.974 -14.913 -22.682 1.00 94.91 C ANISOU 879 CA VAL A 121 13043 13094 9922 -477 79 3115 ATOM 880 C VAL A 121 6.799 -14.546 -21.759 1.00 91.09 C ANISOU 880 C VAL A 121 12652 12516 9442 -491 85 3010 ATOM 881 O VAL A 121 6.360 -15.374 -20.963 1.00 89.50 O ANISOU 881 O VAL A 121 12516 12270 9220 -562 46 2950 ATOM 882 CB VAL A 121 9.201 -13.994 -22.400 1.00 94.75 C ANISOU 882 CB VAL A 121 13011 13046 9944 -361 135 3123 ATOM 883 CG1 VAL A 121 9.458 -13.835 -20.902 1.00 93.40 C ANISOU 883 CG1 VAL A 121 12933 12766 9789 -340 150 3027 ATOM 884 CG2 VAL A 121 10.454 -14.535 -23.087 1.00 95.41 C ANISOU 884 CG2 VAL A 121 13017 13209 10023 -352 120 3221 ATOM 885 N THR A 122 6.278 -13.332 -21.902 1.00 88.47 N ANISOU 885 N THR A 122 12324 12156 9135 -419 135 2987 ATOM 886 CA THR A 122 5.281 -12.777 -21.007 1.00 86.22 C ANISOU 886 CA THR A 122 12123 11780 8857 -416 145 2889 ATOM 887 C THR A 122 3.871 -13.124 -21.513 1.00 85.55 C ANISOU 887 C THR A 122 12044 11717 8744 -495 110 2894 ATOM 888 O THR A 122 3.334 -12.410 -22.362 1.00 84.78 O ANISOU 888 O THR A 122 11908 11658 8646 -470 135 2930 ATOM 889 CB THR A 122 5.460 -11.245 -20.932 1.00 0.00 C ATOM 890 OG1 THR A 122 6.785 -10.956 -20.508 1.00 0.00 O ATOM 891 CG2 THR A 122 4.502 -10.556 -19.958 1.00 0.00 C ATOM 892 N THR A 123 3.312 -14.231 -21.008 1.00 85.16 N ANISOU 892 N THR A 123 12044 11642 8670 -590 53 2859 ATOM 893 CA THR A 123 1.996 -14.715 -21.441 1.00 84.40 C ANISOU 893 CA THR A 123 11962 11556 8549 -677 10 2863 ATOM 894 C THR A 123 0.922 -14.442 -20.380 1.00 83.39 C ANISOU 894 C THR A 123 11931 11325 8427 -681 5 2762 ATOM 895 O THR A 123 1.244 -14.334 -19.185 1.00 82.59 O ANISOU 895 O THR A 123 11889 11147 8342 -646 18 2683 ATOM 896 CB THR A 123 2.028 -16.229 -21.732 1.00 84.68 C ANISOU 896 CB THR A 123 11988 11634 8550 -788 -59 2895 ATOM 897 OG1 THR A 123 2.433 -16.947 -20.559 1.00 84.31 O ANISOU 897 OG1 THR A 123 12009 11526 8499 -806 -79 2823 ATOM 898 CG2 THR A 123 2.994 -16.531 -22.866 1.00 85.29 C ANISOU 898 CG2 THR A 123 11964 11823 8618 -790 -62 3003 ATOM 899 N HIS A 124 -0.360 -14.370 -20.758 1.00 83.43 N ANISOU 899 N HIS A 124 11949 11327 8420 -726 -13 2767 ATOM 900 CA HIS A 124 -1.436 -14.023 -19.815 1.00 83.17 C ANISOU 900 CA HIS A 124 12006 11201 8393 -733 -24 2680 ATOM 901 C HIS A 124 -1.619 -15.013 -18.646 1.00 83.28 C ANISOU 901 C HIS A 124 12098 11137 8407 -769 -59 2593 ATOM 902 O HIS A 124 -1.992 -14.587 -17.555 1.00 83.20 O ANISOU 902 O HIS A 124 12150 11045 8417 -720 -40 2509 ATOM 903 CB HIS A 124 -2.746 -13.680 -20.550 1.00 0.00 C ATOM 904 CG HIS A 124 -2.763 -12.253 -21.042 1.00 0.00 C ATOM 905 ND1 HIS A 124 -1.725 -11.729 -21.825 1.00 0.00 N ATOM 906 CD2 HIS A 124 -3.684 -11.255 -20.799 1.00 0.00 C ATOM 907 CE1 HIS A 124 -2.027 -10.447 -21.988 1.00 0.00 C ATOM 908 NE2 HIS A 124 -3.181 -10.113 -21.409 1.00 0.00 N ATOM 909 N ARG A 125 -1.285 -16.300 -18.834 1.00 84.05 N ANISOU 909 N ARG A 125 12191 11263 8480 -852 -111 2614 ATOM 910 CA ARG A 125 -1.241 -17.253 -17.713 1.00 84.10 C ANISOU 910 CA ARG A 125 12268 11206 8478 -890 -144 2534 ATOM 911 C ARG A 125 -0.100 -16.952 -16.734 1.00 82.50 C ANISOU 911 C ARG A 125 12075 10975 8294 -818 -103 2489 ATOM 912 O ARG A 125 -0.298 -16.986 -15.507 1.00 82.22 O ANISOU 912 O ARG A 125 12107 10861 8270 -801 -101 2398 ATOM 913 CB ARG A 125 -1.175 -18.707 -18.210 1.00 85.84 C ANISOU 913 CB ARG A 125 12478 11473 8663 -995 -207 2569 ATOM 914 CG ARG A 125 0.045 -19.098 -19.040 1.00 87.58 C ANISOU 914 CG ARG A 125 12615 11793 8867 -1004 -207 2656 ATOM 915 CD ARG A 125 -0.059 -20.540 -19.503 1.00 89.28 C ANISOU 915 CD ARG A 125 12829 12050 9043 -1116 -277 2684 ATOM 916 NE ARG A 125 0.957 -20.872 -20.505 1.00 90.66 N ANISOU 916 NE ARG A 125 12912 12332 9201 -1131 -283 2783 ATOM 917 CZ ARG A 125 2.250 -21.113 -20.257 1.00 91.47 C ANISOU 917 CZ ARG A 125 12988 12467 9297 -1101 -269 2798 ATOM 918 NH1 ARG A 125 2.748 -21.067 -19.017 1.00 91.02 N ANISOU 918 NH1 ARG A 125 12988 12347 9248 -1055 -245 2721 ATOM 919 NH2 ARG A 125 3.066 -21.407 -21.270 1.00 92.53 N1+ ANISOU 919 NH2 ARG A 125 13036 12703 9416 -1116 -281 2896 ATOM 920 N ARG A 126 1.076 -16.632 -17.278 1.00 81.31 N ANISOU 920 N ARG A 126 11856 10889 8149 -774 -71 2555 ATOM 921 CA ARG A 126 2.237 -16.262 -16.457 1.00 79.77 C ANISOU 921 CA ARG A 126 11664 10669 7974 -705 -30 2526 ATOM 922 C ARG A 126 1.993 -14.950 -15.712 1.00 77.71 C ANISOU 922 C ARG A 126 11438 10336 7751 -618 19 2463 ATOM 923 O ARG A 126 2.334 -14.836 -14.525 1.00 77.19 O ANISOU 923 O ARG A 126 11419 10207 7702 -587 35 2391 ATOM 924 CB ARG A 126 3.514 -16.179 -17.304 1.00 80.70 C ANISOU 924 CB ARG A 126 11700 10869 8092 -675 -10 2618 ATOM 925 CG ARG A 126 4.103 -17.538 -17.623 1.00 82.07 C ANISOU 925 CG ARG A 126 11849 11103 8228 -751 -58 2662 ATOM 926 CD ARG A 126 5.168 -17.465 -18.711 1.00 83.23 C ANISOU 926 CD ARG A 126 11904 11344 8374 -728 -47 2770 ATOM 927 NE ARG A 126 5.450 -18.791 -19.256 1.00 84.08 N ANISOU 927 NE ARG A 126 11982 11522 8439 -817 -105 2822 ATOM 928 CZ ARG A 126 6.188 -19.038 -20.343 1.00 84.90 C ANISOU 928 CZ ARG A 126 12000 11723 8532 -825 -116 2924 ATOM 929 NH1 ARG A 126 6.748 -18.049 -21.039 1.00 85.05 N ANISOU 929 NH1 ARG A 126 11951 11780 8581 -742 -69 2988 ATOM 930 NH2 ARG A 126 6.362 -20.296 -20.737 1.00 85.91 N1+ ANISOU 930 NH2 ARG A 126 12111 11911 8618 -915 -175 2962 ATOM 931 N ILE A 127 1.373 -13.956 -16.375 1.00 75.94 N ANISOU 931 N ILE A 127 11190 10125 7537 -582 42 2491 ATOM 932 CA ILE A 127 1.034 -12.682 -15.723 1.00 74.23 C ANISOU 932 CA ILE A 127 11010 9842 7348 -508 82 2430 ATOM 933 C ILE A 127 -0.012 -12.890 -14.616 1.00 72.82 C ANISOU 933 C ILE A 127 10916 9579 7172 -536 55 2334 ATOM 934 O ILE A 127 0.098 -12.250 -13.576 1.00 72.25 O ANISOU 934 O ILE A 127 10885 9439 7125 -484 80 2261 ATOM 935 CB ILE A 127 0.566 -11.533 -16.679 1.00 0.00 C ATOM 936 CG1 ILE A 127 -0.962 -11.353 -16.891 1.00 0.00 C ATOM 937 CG2 ILE A 127 1.324 -11.559 -18.015 1.00 0.00 C ATOM 938 CD1 ILE A 127 -1.333 -10.267 -17.896 1.00 0.00 C ATOM 939 N TRP A 128 -0.979 -13.796 -14.825 1.00 71.75 N ANISOU 939 N TRP A 128 10804 9446 7013 -618 2 2336 ATOM 940 CA TRP A 128 -1.990 -14.094 -13.819 1.00 70.47 C ANISOU 940 CA TRP A 128 10720 9202 6851 -648 -29 2248 ATOM 941 C TRP A 128 -1.411 -14.888 -12.633 1.00 68.98 C ANISOU 941 C TRP A 128 10568 8973 6667 -650 -33 2180 ATOM 942 O TRP A 128 -1.753 -14.596 -11.489 1.00 68.36 O ANISOU 942 O TRP A 128 10541 8821 6608 -617 -23 2095 ATOM 943 CB TRP A 128 -3.212 -14.772 -14.452 1.00 0.00 C ATOM 944 CG TRP A 128 -4.405 -14.766 -13.549 1.00 0.00 C ATOM 945 CD1 TRP A 128 -4.890 -15.818 -12.851 1.00 0.00 C ATOM 946 CD2 TRP A 128 -5.199 -13.609 -13.143 1.00 0.00 C ATOM 947 NE1 TRP A 128 -5.939 -15.394 -12.057 1.00 0.00 N ATOM 948 CE2 TRP A 128 -6.167 -14.039 -12.186 1.00 0.00 C ATOM 949 CE3 TRP A 128 -5.186 -12.233 -13.476 1.00 0.00 C ATOM 950 CZ2 TRP A 128 -7.076 -13.148 -11.589 1.00 0.00 C ATOM 951 CZ3 TRP A 128 -6.095 -11.329 -12.886 1.00 0.00 C ATOM 952 CH2 TRP A 128 -7.037 -11.785 -11.942 1.00 0.00 C ATOM 953 N LEU A 129 -0.486 -15.820 -12.911 1.00 68.21 N ANISOU 953 N LEU A 129 10440 8926 6548 -689 -46 2219 ATOM 954 CA LEU A 129 0.314 -16.511 -11.897 1.00 67.44 C ANISOU 954 CA LEU A 129 10369 8805 6448 -692 -43 2165 ATOM 955 C LEU A 129 1.173 -15.525 -11.086 1.00 66.47 C ANISOU 955 C LEU A 129 10246 8647 6361 -605 12 2132 ATOM 956 O LEU A 129 1.143 -15.585 -9.858 1.00 65.72 O ANISOU 956 O LEU A 129 10197 8491 6281 -587 21 2049 ATOM 957 CB LEU A 129 1.188 -17.603 -12.554 1.00 0.00 C ATOM 958 CG LEU A 129 0.402 -18.854 -13.009 1.00 0.00 C ATOM 959 CD1 LEU A 129 1.207 -19.681 -14.038 1.00 0.00 C ATOM 960 CD2 LEU A 129 -0.083 -19.699 -11.810 1.00 0.00 C ATOM 961 N ALA A 130 1.858 -14.595 -11.775 1.00 66.14 N ANISOU 961 N ALA A 130 10150 8644 6335 -551 50 2196 ATOM 962 CA ALA A 130 2.568 -13.471 -11.155 1.00 65.59 C ANISOU 962 CA ALA A 130 10079 8538 6303 -467 103 2170 ATOM 963 C ALA A 130 1.640 -12.628 -10.275 1.00 65.11 C ANISOU 963 C ALA A 130 10071 8400 6268 -430 114 2085 ATOM 964 O ALA A 130 1.989 -12.331 -9.129 1.00 65.16 O ANISOU 964 O ALA A 130 10107 8353 6297 -398 134 2021 ATOM 965 CB ALA A 130 3.234 -12.599 -12.211 1.00 65.71 C ANISOU 965 CB ALA A 130 10031 8603 6331 -413 138 2250 ATOM 966 N LEU A 131 0.482 -12.237 -10.817 1.00 64.53 N ANISOU 966 N LEU A 131 10007 8322 6188 -438 98 2089 ATOM 967 CA LEU A 131 -0.527 -11.412 -10.154 1.00 63.76 C ANISOU 967 CA LEU A 131 9961 8154 6109 -408 99 2013 ATOM 968 C LEU A 131 -1.067 -12.088 -8.883 1.00 62.65 C ANISOU 968 C LEU A 131 9876 7957 5971 -439 73 1928 ATOM 969 O LEU A 131 -1.092 -11.464 -7.823 1.00 61.51 O ANISOU 969 O LEU A 131 9756 7761 5852 -398 95 1862 ATOM 970 CB LEU A 131 -1.616 -11.068 -11.195 1.00 0.00 C ATOM 971 CG LEU A 131 -2.638 -9.980 -10.818 1.00 0.00 C ATOM 972 CD1 LEU A 131 -3.169 -9.314 -12.104 1.00 0.00 C ATOM 973 CD2 LEU A 131 -3.786 -10.508 -9.931 1.00 0.00 C ATOM 974 N GLY A 132 -1.412 -13.378 -8.989 1.00 62.62 N ANISOU 974 N GLY A 132 9888 7965 5939 -512 27 1931 ATOM 975 CA GLY A 132 -1.860 -14.205 -7.872 1.00 62.31 C ANISOU 975 CA GLY A 132 9902 7876 5897 -542 0 1849 ATOM 976 C GLY A 132 -0.758 -14.354 -6.814 1.00 62.03 C ANISOU 976 C GLY A 132 9866 7827 5875 -514 32 1807 ATOM 977 O GLY A 132 -1.045 -14.245 -5.623 1.00 62.05 O ANISOU 977 O GLY A 132 9906 7773 5897 -492 38 1725 ATOM 978 N LEU A 133 0.505 -14.535 -7.234 1.00 61.55 N ANISOU 978 N LEU A 133 9759 7820 5804 -514 54 1868 ATOM 979 CA LEU A 133 1.664 -14.640 -6.345 1.00 60.81 C ANISOU 979 CA LEU A 133 9658 7720 5724 -488 88 1846 ATOM 980 C LEU A 133 1.885 -13.375 -5.495 1.00 60.12 C ANISOU 980 C LEU A 133 9583 7577 5681 -418 127 1795 ATOM 981 O LEU A 133 2.204 -13.504 -4.313 1.00 59.94 O ANISOU 981 O LEU A 133 9583 7517 5673 -409 140 1729 ATOM 982 CB LEU A 133 2.922 -15.042 -7.149 1.00 0.00 C ATOM 983 CG LEU A 133 4.191 -15.323 -6.309 1.00 0.00 C ATOM 984 CD1 LEU A 133 3.978 -16.467 -5.294 1.00 0.00 C ATOM 985 CD2 LEU A 133 5.408 -15.576 -7.223 1.00 0.00 C ATOM 986 N CYS A 134 1.646 -12.187 -6.073 1.00 59.76 N ANISOU 986 N CYS A 134 9521 7528 5655 -371 145 1824 ATOM 987 CA CYS A 134 1.657 -10.905 -5.358 1.00 59.07 C ANISOU 987 CA CYS A 134 9447 7389 5608 -305 178 1775 ATOM 988 C CYS A 134 0.672 -10.924 -4.206 1.00 57.51 C ANISOU 988 C CYS A 134 9298 7129 5421 -307 160 1682 ATOM 989 O CYS A 134 1.035 -10.609 -3.081 1.00 56.95 O ANISOU 989 O CYS A 134 9240 7020 5376 -283 180 1624 ATOM 990 CB CYS A 134 1.328 -9.727 -6.276 1.00 59.82 C ANISOU 990 CB CYS A 134 9525 7492 5713 -259 195 1813 ATOM 991 SG CYS A 134 2.473 -9.537 -7.661 1.00 61.60 S ANISOU 991 SG CYS A 134 9685 7788 5930 -240 222 1923 ATOM 992 N TRP A 135 -0.563 -11.326 -4.494 1.00 56.32 N ANISOU 992 N TRP A 135 9173 6972 5253 -338 121 1670 ATOM 993 CA TRP A 135 -1.597 -11.421 -3.465 1.00 55.45 C ANISOU 993 CA TRP A 135 9110 6803 5154 -338 97 1585 ATOM 994 C TRP A 135 -1.270 -12.463 -2.394 1.00 55.12 C ANISOU 994 C TRP A 135 9085 6749 5109 -367 91 1529 ATOM 995 O TRP A 135 -1.436 -12.189 -1.207 1.00 54.90 O ANISOU 995 O TRP A 135 9077 6676 5106 -341 99 1456 ATOM 996 CB TRP A 135 -2.973 -11.685 -4.083 1.00 55.09 C ANISOU 996 CB TRP A 135 9090 6750 5090 -368 53 1593 ATOM 997 CG TRP A 135 -3.567 -10.463 -4.713 1.00 54.52 C ANISOU 997 CG TRP A 135 9013 6674 5026 -329 61 1619 ATOM 998 CD1 TRP A 135 -3.607 -10.164 -6.041 1.00 54.63 C ANISOU 998 CD1 TRP A 135 8997 6737 5021 -335 65 1699 ATOM 999 CD2 TRP A 135 -4.189 -9.370 -4.033 1.00 53.93 C ANISOU 999 CD2 TRP A 135 8963 6550 4976 -278 68 1565 ATOM 1000 NE1 TRP A 135 -4.226 -8.951 -6.235 1.00 54.44 N ANISOU 1000 NE1 TRP A 135 8980 6697 5006 -289 76 1696 ATOM 1001 CE2 TRP A 135 -4.593 -8.443 -5.018 1.00 54.00 C ANISOU 1001 CE2 TRP A 135 8960 6581 4976 -255 76 1614 ATOM 1002 CE3 TRP A 135 -4.450 -9.086 -2.689 1.00 53.67 C ANISOU 1002 CE3 TRP A 135 8959 6461 4972 -250 67 1479 ATOM 1003 CZ2 TRP A 135 -5.247 -7.249 -4.702 1.00 53.76 C ANISOU 1003 CZ2 TRP A 135 8949 6517 4959 -206 82 1580 ATOM 1004 CZ3 TRP A 135 -5.104 -7.890 -2.374 1.00 53.54 C ANISOU 1004 CZ3 TRP A 135 8959 6410 4972 -202 69 1447 ATOM 1005 CH2 TRP A 135 -5.491 -6.989 -3.380 1.00 53.45 C ANISOU 1005 CH2 TRP A 135 8940 6420 4947 -181 76 1496 ATOM 1006 N LEU A 136 -0.748 -13.630 -2.802 1.00 55.10 N ANISOU 1006 N LEU A 136 9071 6789 5072 -419 78 1564 ATOM 1007 CA LEU A 136 -0.290 -14.687 -1.892 1.00 54.91 C ANISOU 1007 CA LEU A 136 9063 6763 5036 -447 76 1513 ATOM 1008 C LEU A 136 0.805 -14.194 -0.932 1.00 54.28 C ANISOU 1008 C LEU A 136 8965 6674 4983 -409 122 1488 ATOM 1009 O LEU A 136 0.626 -14.297 0.281 1.00 53.86 O ANISOU 1009 O LEU A 136 8932 6584 4948 -395 130 1411 ATOM 1010 CB LEU A 136 0.196 -15.921 -2.683 1.00 0.00 C ATOM 1011 CG LEU A 136 -0.928 -16.717 -3.381 1.00 0.00 C ATOM 1012 CD1 LEU A 136 -0.353 -17.668 -4.454 1.00 0.00 C ATOM 1013 CD2 LEU A 136 -1.839 -17.441 -2.365 1.00 0.00 C ATOM 1014 N VAL A 137 1.872 -13.595 -1.481 1.00 53.99 N ANISOU 1014 N VAL A 137 8891 6670 4952 -392 153 1555 ATOM 1015 CA VAL A 137 2.937 -12.946 -0.713 1.00 53.74 C ANISOU 1015 CA VAL A 137 8841 6626 4948 -359 196 1545 ATOM 1016 C VAL A 137 2.388 -11.815 0.181 1.00 53.45 C ANISOU 1016 C VAL A 137 8821 6530 4958 -308 211 1480 ATOM 1017 O VAL A 137 2.781 -11.708 1.337 1.00 52.98 O ANISOU 1017 O VAL A 137 8763 6446 4920 -296 234 1432 ATOM 1018 CB VAL A 137 4.056 -12.386 -1.645 1.00 0.00 C ATOM 1019 CG1 VAL A 137 5.062 -11.414 -0.984 1.00 0.00 C ATOM 1020 CG2 VAL A 137 4.837 -13.536 -2.307 1.00 0.00 C ATOM 1021 N SER A 138 1.442 -11.036 -0.343 1.00 53.55 N ANISOU 1021 N SER A 138 8843 6521 4980 -281 197 1482 ATOM 1022 CA SER A 138 0.811 -9.917 0.377 1.00 53.21 C ANISOU 1022 CA SER A 138 8819 6424 4974 -235 202 1421 ATOM 1023 C SER A 138 0.020 -10.374 1.589 1.00 53.16 C ANISOU 1023 C SER A 138 8841 6382 4975 -243 182 1334 ATOM 1024 O SER A 138 0.133 -9.779 2.662 1.00 53.00 O ANISOU 1024 O SER A 138 8823 6327 4988 -216 199 1278 ATOM 1025 CB SER A 138 -0.128 -9.137 -0.532 1.00 53.16 C ANISOU 1025 CB SER A 138 8821 6412 4965 -212 186 1444 ATOM 1026 OG SER A 138 0.542 -8.722 -1.698 1.00 53.60 O ANISOU 1026 OG SER A 138 8846 6505 5012 -199 206 1523 ATOM 1027 N PHE A 139 -0.798 -11.410 1.405 1.00 53.34 N ANISOU 1027 N PHE A 139 8886 6411 4969 -281 146 1323 ATOM 1028 CA PHE A 139 -1.489 -12.050 2.528 1.00 53.36 C ANISOU 1028 CA PHE A 139 8915 6383 4976 -289 127 1241 ATOM 1029 C PHE A 139 -0.484 -12.634 3.530 1.00 53.47 C ANISOU 1029 C PHE A 139 8913 6411 4990 -301 157 1211 ATOM 1030 O PHE A 139 -0.667 -12.475 4.740 1.00 53.19 O ANISOU 1030 O PHE A 139 8881 6347 4980 -281 165 1141 ATOM 1031 CB PHE A 139 -2.490 -13.119 2.055 1.00 53.45 C ANISOU 1031 CB PHE A 139 8957 6394 4955 -329 81 1239 ATOM 1032 CG PHE A 139 -3.864 -12.574 1.753 1.00 53.27 C ANISOU 1032 CG PHE A 139 8963 6332 4943 -311 46 1226 ATOM 1033 CD1 PHE A 139 -4.730 -12.230 2.784 1.00 53.17 C ANISOU 1033 CD1 PHE A 139 8974 6267 4958 -278 32 1151 ATOM 1034 CD2 PHE A 139 -4.301 -12.412 0.440 1.00 53.38 C ANISOU 1034 CD2 PHE A 139 8978 6364 4937 -328 26 1294 ATOM 1035 CE1 PHE A 139 -5.999 -11.732 2.511 1.00 53.15 C ANISOU 1035 CE1 PHE A 139 9000 6229 4963 -262 -2 1144 ATOM 1036 CE2 PHE A 139 -5.571 -11.917 0.162 1.00 53.20 C ANISOU 1036 CE2 PHE A 139 8983 6308 4921 -315 -5 1289 ATOM 1037 CZ PHE A 139 -6.420 -11.576 1.199 1.00 53.09 C ANISOU 1037 CZ PHE A 139 8998 6239 4934 -282 -21 1214 ATOM 1038 N LEU A 140 0.588 -13.287 3.059 1.00 53.59 N ANISOU 1038 N LEU A 140 8907 6475 4978 -334 173 1268 ATOM 1039 CA LEU A 140 1.630 -13.814 3.948 1.00 53.94 C ANISOU 1039 CA LEU A 140 8935 6541 5018 -348 205 1250 ATOM 1040 C LEU A 140 2.297 -12.706 4.784 1.00 53.65 C ANISOU 1040 C LEU A 140 8878 6476 5027 -309 242 1228 ATOM 1041 O LEU A 140 2.382 -12.848 6.006 1.00 54.05 O ANISOU 1041 O LEU A 140 8928 6513 5094 -305 257 1165 ATOM 1042 CB LEU A 140 2.668 -14.635 3.153 1.00 0.00 C ATOM 1043 CG LEU A 140 2.141 -16.000 2.656 1.00 0.00 C ATOM 1044 CD1 LEU A 140 3.036 -16.571 1.533 1.00 0.00 C ATOM 1045 CD2 LEU A 140 1.928 -16.996 3.818 1.00 0.00 C ATOM 1046 N VAL A 141 2.684 -11.593 4.142 1.00 53.12 N ANISOU 1046 N VAL A 141 8797 6401 4983 -280 257 1278 ATOM 1047 CA VAL A 141 3.329 -10.480 4.854 1.00 52.83 C ANISOU 1047 CA VAL A 141 8746 6334 4991 -246 290 1261 ATOM 1048 C VAL A 141 2.334 -9.761 5.774 1.00 52.76 C ANISOU 1048 C VAL A 141 8753 6276 5016 -215 278 1180 ATOM 1049 O VAL A 141 2.638 -9.484 6.930 1.00 52.48 O ANISOU 1049 O VAL A 141 8707 6222 5009 -208 297 1132 ATOM 1050 CB VAL A 141 3.974 -9.477 3.867 1.00 52.59 C ANISOU 1050 CB VAL A 141 8702 6302 4975 -218 307 1330 ATOM 1051 CG1 VAL A 141 4.476 -8.230 4.588 1.00 52.55 C ANISOU 1051 CG1 VAL A 141 8691 6253 5019 -181 334 1303 ATOM 1052 CG2 VAL A 141 5.125 -10.135 3.101 1.00 52.72 C ANISOU 1052 CG2 VAL A 141 8697 6368 4965 -244 321 1412 ATOM 1053 N GLY A 142 1.149 -9.472 5.253 1.00 52.99 N ANISOU 1053 N GLY A 142 8803 6286 5041 -198 245 1170 ATOM 1054 CA GLY A 142 0.116 -8.764 5.999 1.00 53.18 C ANISOU 1054 CA GLY A 142 8844 6266 5094 -166 226 1100 ATOM 1055 C GLY A 142 -0.523 -9.518 7.154 1.00 53.68 C ANISOU 1055 C GLY A 142 8916 6318 5160 -175 211 1025 ATOM 1056 O GLY A 142 -0.873 -8.893 8.166 1.00 53.67 O ANISOU 1056 O GLY A 142 8911 6286 5193 -149 211 964 ATOM 1057 N LEU A 143 -0.697 -10.837 7.011 1.00 54.27 N ANISOU 1057 N LEU A 143 9000 6418 5199 -210 198 1025 ATOM 1058 CA LEU A 143 -1.267 -11.664 8.094 1.00 54.46 C ANISOU 1058 CA LEU A 143 9034 6434 5223 -215 187 950 ATOM 1059 C LEU A 143 -0.248 -12.133 9.138 1.00 54.96 C ANISOU 1059 C LEU A 143 9069 6523 5289 -231 226 924 ATOM 1060 O LEU A 143 -0.658 -12.676 10.161 1.00 54.85 O ANISOU 1060 O LEU A 143 9055 6505 5280 -227 225 856 ATOM 1061 CB LEU A 143 -2.016 -12.882 7.537 1.00 54.49 C ANISOU 1061 CB LEU A 143 9069 6446 5188 -245 152 950 ATOM 1062 CG LEU A 143 -3.268 -12.622 6.702 1.00 54.37 C ANISOU 1062 CG LEU A 143 9087 6401 5170 -235 106 964 ATOM 1063 CD1 LEU A 143 -3.788 -13.928 6.125 1.00 54.45 C ANISOU 1063 CD1 LEU A 143 9127 6421 5139 -277 74 971 ATOM 1064 CD2 LEU A 143 -4.343 -11.941 7.534 1.00 54.40 C ANISOU 1064 CD2 LEU A 143 9104 6354 5210 -192 85 897 ATOM 1065 N THR A 144 1.052 -11.920 8.907 1.00 55.60 N ANISOU 1065 N THR A 144 9125 6631 5368 -246 262 979 ATOM 1066 CA THR A 144 2.084 -12.303 9.895 1.00 56.21 C ANISOU 1066 CA THR A 144 9174 6734 5447 -265 302 963 ATOM 1067 C THR A 144 1.724 -11.879 11.346 1.00 56.62 C ANISOU 1067 C THR A 144 9210 6762 5539 -241 312 882 ATOM 1068 O THR A 144 1.732 -12.734 12.245 1.00 56.79 O ANISOU 1068 O THR A 144 9222 6806 5547 -254 324 834 ATOM 1069 CB THR A 144 3.499 -11.828 9.464 1.00 56.14 C ANISOU 1069 CB THR A 144 9143 6743 5443 -277 337 1038 ATOM 1070 OG1 THR A 144 3.897 -12.524 8.278 1.00 55.88 O ANISOU 1070 OG1 THR A 144 9117 6747 5366 -304 329 1109 ATOM 1071 CG2 THR A 144 4.537 -12.082 10.558 1.00 56.26 C ANISOU 1071 CG2 THR A 144 9129 6780 5464 -298 378 1024 ATOM 1072 N PRO A 145 1.358 -10.593 11.565 1.00 56.81 N ANISOU 1072 N PRO A 145 9231 6744 5608 -205 304 864 ATOM 1073 CA PRO A 145 0.867 -10.167 12.885 1.00 57.54 C ANISOU 1073 CA PRO A 145 9307 6816 5740 -181 304 787 ATOM 1074 C PRO A 145 -0.249 -11.041 13.486 1.00 58.73 C ANISOU 1074 C PRO A 145 9468 6964 5879 -171 279 718 ATOM 1075 O PRO A 145 -0.241 -11.282 14.699 1.00 58.73 O ANISOU 1075 O PRO A 145 9443 6975 5897 -166 295 660 ATOM 1076 CB PRO A 145 0.344 -8.751 12.623 1.00 57.07 C ANISOU 1076 CB PRO A 145 9256 6710 5716 -145 282 785 ATOM 1077 CG PRO A 145 1.181 -8.254 11.508 1.00 56.66 C ANISOU 1077 CG PRO A 145 9210 6661 5655 -153 296 863 ATOM 1078 CD PRO A 145 1.513 -9.443 10.655 1.00 56.44 C ANISOU 1078 CD PRO A 145 9192 6673 5578 -186 299 914 ATOM 1079 N MET A 146 -1.184 -11.506 12.649 1.00 60.04 N ANISOU 1079 N MET A 146 9673 7118 6020 -167 240 725 ATOM 1080 CA MET A 146 -2.229 -12.444 13.089 1.00 61.26 C ANISOU 1080 CA MET A 146 9847 7264 6162 -157 213 664 ATOM 1081 C MET A 146 -1.659 -13.790 13.554 1.00 61.85 C ANISOU 1081 C MET A 146 9913 7384 6201 -189 240 645 ATOM 1082 O MET A 146 -2.257 -14.429 14.422 1.00 62.80 O ANISOU 1082 O MET A 146 10034 7502 6323 -173 236 575 ATOM 1083 CB MET A 146 -3.265 -12.697 11.987 1.00 62.24 C ANISOU 1083 CB MET A 146 10018 7363 6265 -156 166 687 ATOM 1084 CG MET A 146 -4.144 -11.505 11.648 1.00 62.86 C ANISOU 1084 CG MET A 146 10111 7398 6373 -120 133 692 ATOM 1085 SD MET A 146 -5.614 -11.371 12.686 1.00 64.56 S ANISOU 1085 SD MET A 146 10338 7567 6622 -72 93 605 ATOM 1086 CE MET A 146 -6.549 -12.801 12.157 1.00 64.92 C ANISOU 1086 CE MET A 146 10434 7600 6631 -89 55 594 ATOM 1087 N PHE A 147 -0.526 -14.226 12.986 1.00 61.74 N ANISOU 1087 N PHE A 147 9891 7411 6152 -229 268 705 ATOM 1088 CA PHE A 147 0.086 -15.499 13.400 1.00 61.88 C ANISOU 1088 CA PHE A 147 9903 7480 6128 -263 295 691 ATOM 1089 C PHE A 147 0.744 -15.440 14.786 1.00 61.15 C ANISOU 1089 C PHE A 147 9765 7412 6054 -260 341 649 ATOM 1090 O PHE A 147 0.920 -16.487 15.412 1.00 61.58 O ANISOU 1090 O PHE A 147 9814 7505 6077 -274 361 611 ATOM 1091 CB PHE A 147 1.121 -16.012 12.378 1.00 62.72 C ANISOU 1091 CB PHE A 147 10013 7627 6188 -309 307 774 ATOM 1092 CG PHE A 147 0.593 -16.176 10.965 1.00 63.28 C ANISOU 1092 CG PHE A 147 10121 7686 6236 -321 265 823 ATOM 1093 CD1 PHE A 147 -0.738 -16.553 10.707 1.00 63.37 C ANISOU 1093 CD1 PHE A 147 10171 7663 6244 -308 219 785 ATOM 1094 CD2 PHE A 147 1.459 -15.983 9.877 1.00 63.16 C ANISOU 1094 CD2 PHE A 147 10098 7695 6203 -346 272 913 ATOM 1095 CE1 PHE A 147 -1.186 -16.705 9.398 1.00 63.41 C ANISOU 1095 CE1 PHE A 147 10205 7660 6227 -327 182 836 ATOM 1096 CE2 PHE A 147 1.011 -16.140 8.570 1.00 62.94 C ANISOU 1096 CE2 PHE A 147 10095 7664 6153 -359 235 963 ATOM 1097 CZ PHE A 147 -0.307 -16.511 8.332 1.00 63.20 C ANISOU 1097 CZ PHE A 147 10165 7664 6181 -353 191 925 ATOM 1098 N GLY A 148 1.103 -14.244 15.262 1.00 59.75 N ANISOU 1098 N GLY A 148 9557 7217 5926 -243 357 654 ATOM 1099 CA GLY A 148 1.757 -14.104 16.570 1.00 59.22 C ANISOU 1099 CA GLY A 148 9442 7176 5882 -247 400 620 ATOM 1100 C GLY A 148 2.637 -12.886 16.803 1.00 58.15 C ANISOU 1100 C GLY A 148 9275 7028 5788 -252 424 657 ATOM 1101 O GLY A 148 2.764 -12.441 17.946 1.00 57.86 O ANISOU 1101 O GLY A 148 9200 6994 5789 -245 444 616 ATOM 1102 N TRP A 149 3.254 -12.356 15.746 1.00 57.09 N ANISOU 1102 N TRP A 149 9157 6881 5652 -265 421 733 ATOM 1103 CA TRP A 149 4.199 -11.235 15.877 1.00 56.86 C ANISOU 1103 CA TRP A 149 9106 6836 5663 -271 444 772 ATOM 1104 C TRP A 149 3.539 -9.897 16.308 1.00 57.28 C ANISOU 1104 C TRP A 149 9156 6835 5771 -232 420 732 ATOM 1105 O TRP A 149 3.345 -8.988 15.501 1.00 56.88 O ANISOU 1105 O TRP A 149 9131 6748 5731 -210 394 760 ATOM 1106 CB TRP A 149 5.061 -11.093 14.606 1.00 55.96 C ANISOU 1106 CB TRP A 149 9010 6723 5528 -288 449 863 ATOM 1107 CG TRP A 149 6.379 -10.375 14.798 1.00 55.45 C ANISOU 1107 CG TRP A 149 8923 6652 5491 -307 484 912 ATOM 1108 CD1 TRP A 149 6.803 -9.698 15.911 1.00 55.47 C ANISOU 1108 CD1 TRP A 149 8894 6641 5538 -312 507 884 ATOM 1109 CD2 TRP A 149 7.434 -10.250 13.836 1.00 54.95 C ANISOU 1109 CD2 TRP A 149 8869 6593 5416 -323 496 1000 ATOM 1110 NE1 TRP A 149 8.053 -9.172 15.697 1.00 55.42 N ANISOU 1110 NE1 TRP A 149 8882 6625 5548 -333 532 949 ATOM 1111 CE2 TRP A 149 8.463 -9.491 14.432 1.00 55.08 C ANISOU 1111 CE2 TRP A 149 8862 6591 5471 -336 527 1020 ATOM 1112 CE3 TRP A 149 7.608 -10.705 12.525 1.00 54.73 C ANISOU 1112 CE3 TRP A 149 8862 6583 5349 -327 483 1065 ATOM 1113 CZ2 TRP A 149 9.656 -9.185 13.765 1.00 55.05 C ANISOU 1113 CZ2 TRP A 149 8863 6581 5471 -349 545 1103 ATOM 1114 CZ3 TRP A 149 8.796 -10.389 11.856 1.00 54.69 C ANISOU 1114 CZ3 TRP A 149 8855 6578 5347 -338 502 1148 ATOM 1115 CH2 TRP A 149 9.801 -9.642 12.482 1.00 54.86 C ANISOU 1115 CH2 TRP A 149 8858 6575 5409 -346 532 1165 ATOM 1116 N ASN A 150 3.177 -9.819 17.590 1.00 31.02 N ATOM 1117 CA ASN A 150 2.405 -8.748 18.213 1.00 32.28 C ATOM 1118 C ASN A 150 3.182 -8.109 19.351 1.00 31.44 C ATOM 1119 O ASN A 150 4.203 -8.637 19.798 1.00 32.07 O ATOM 1120 CB ASN A 150 1.127 -9.320 18.871 1.00 0.00 C ATOM 1121 CG ASN A 150 0.303 -10.156 17.928 1.00 0.00 C ATOM 1122 OD1 ASN A 150 -0.013 -11.297 18.227 1.00 0.00 O ATOM 1123 ND2 ASN A 150 0.029 -9.619 16.756 1.00 0.00 N ATOM 1124 N MET A 151 2.583 -7.047 19.896 1.00 31.02 N ATOM 1125 CA MET A 151 2.787 -6.622 21.273 1.00 30.54 C ATOM 1126 C MET A 151 2.460 -7.781 22.248 1.00 30.29 C ATOM 1127 O MET A 151 1.313 -8.227 22.295 1.00 30.82 O ATOM 1128 CB MET A 151 1.902 -5.383 21.526 1.00 0.00 C ATOM 1129 CG MET A 151 2.248 -4.618 22.811 1.00 0.00 C ATOM 1130 SD MET A 151 3.911 -3.894 22.852 1.00 0.00 S ATOM 1131 CE MET A 151 3.708 -2.575 21.619 1.00 0.00 C ATOM 1132 N LYS A 152 3.493 -8.278 22.942 1.00 27.98 N ATOM 1133 CA LYS A 152 3.461 -9.265 24.033 1.00 27.56 C ATOM 1134 C LYS A 152 2.720 -10.591 23.733 1.00 27.51 C ATOM 1135 O LYS A 152 2.123 -11.170 24.639 1.00 28.08 O ATOM 1136 CB LYS A 152 2.950 -8.589 25.327 1.00 0.00 C ATOM 1137 CG LYS A 152 3.868 -7.458 25.834 1.00 0.00 C ATOM 1138 CD LYS A 152 3.311 -6.767 27.089 1.00 0.00 C ATOM 1139 CE LYS A 152 2.085 -5.884 26.789 1.00 0.00 C ATOM 1140 NZ LYS A 152 2.376 -4.446 26.914 1.00 0.00 N1+ ATOM 1141 N LEU A 153 2.769 -11.063 22.475 1.00 34.10 N ATOM 1142 CA LEU A 153 2.107 -12.290 21.985 1.00 35.19 C ATOM 1143 C LEU A 153 0.593 -12.260 22.286 1.00 35.98 C ATOM 1144 O LEU A 153 0.026 -13.215 22.807 1.00 34.65 O ATOM 1145 CB LEU A 153 2.776 -13.588 22.502 1.00 0.00 C ATOM 1146 CG LEU A 153 4.195 -13.871 21.962 1.00 0.00 C ATOM 1147 CD1 LEU A 153 5.253 -12.877 22.481 1.00 0.00 C ATOM 1148 CD2 LEU A 153 4.592 -15.332 22.266 1.00 0.00 C ATOM 1149 N THR A 154 0.022 -11.095 22.004 1.00 37.16 N ATOM 1150 CA THR A 154 -1.326 -10.568 22.165 1.00 37.03 C ATOM 1151 C THR A 154 -1.735 -10.171 23.595 1.00 37.42 C ATOM 1152 O THR A 154 -2.660 -9.370 23.707 1.00 38.84 O ATOM 1153 CB THR A 154 -2.405 -11.448 21.474 1.00 0.00 C ATOM 1154 OG1 THR A 154 -3.458 -10.645 20.969 1.00 0.00 O ATOM 1155 CG2 THR A 154 -3.070 -12.502 22.380 1.00 0.00 C ATOM 1156 N SER A 155 -1.064 -10.678 24.643 1.00 37.75 N ATOM 1157 CA SER A 155 -1.316 -10.381 26.064 1.00 38.36 C ATOM 1158 C SER A 155 -1.078 -8.891 26.417 1.00 39.27 C ATOM 1159 O SER A 155 -0.168 -8.589 27.192 1.00 37.20 O ATOM 1160 CB SER A 155 -0.467 -11.366 26.912 1.00 0.00 C ATOM 1161 OG SER A 155 -0.639 -11.199 28.305 1.00 0.00 O ATOM 1162 N GLU A 156 -1.883 -7.994 25.829 1.00 39.51 N ATOM 1163 CA GLU A 156 -1.729 -6.540 25.821 1.00 40.97 C ATOM 1164 C GLU A 156 -2.128 -5.880 27.158 1.00 41.35 C ATOM 1165 O GLU A 156 -2.986 -5.002 27.219 1.00 41.43 O ATOM 1166 CB GLU A 156 -2.277 -5.944 24.492 1.00 0.00 C ATOM 1167 CG GLU A 156 -2.442 -4.408 24.335 1.00 0.00 C ATOM 1168 CD GLU A 156 -1.281 -3.542 24.819 1.00 0.00 C ATOM 1169 OE1 GLU A 156 -0.204 -4.079 25.134 1.00 0.00 O ATOM 1170 OE2 GLU A 156 -1.518 -2.337 25.019 1.00 0.00 O1- ATOM 1171 N TYR A 157 -1.466 -6.322 28.231 1.00 43.31 N ATOM 1172 CA TYR A 157 -1.690 -5.867 29.596 1.00 44.09 C ATOM 1173 C TYR A 157 -0.539 -4.974 30.080 1.00 43.40 C ATOM 1174 O TYR A 157 0.555 -4.976 29.500 1.00 45.87 O ATOM 1175 CB TYR A 157 -1.817 -7.085 30.542 1.00 0.00 C ATOM 1176 CG TYR A 157 -2.835 -8.153 30.172 1.00 0.00 C ATOM 1177 CD1 TYR A 157 -4.126 -7.808 29.721 1.00 0.00 C ATOM 1178 CD2 TYR A 157 -2.492 -9.516 30.307 1.00 0.00 C ATOM 1179 CE1 TYR A 157 -5.053 -8.814 29.384 1.00 0.00 C ATOM 1180 CE2 TYR A 157 -3.419 -10.521 29.973 1.00 0.00 C ATOM 1181 CZ TYR A 157 -4.701 -10.170 29.509 1.00 0.00 C ATOM 1182 OH TYR A 157 -5.604 -11.141 29.190 1.00 0.00 O ATOM 1183 N HIS A 158 -0.800 -4.265 31.179 1.00 39.43 N ATOM 1184 CA HIS A 158 0.175 -3.690 32.095 1.00 36.39 C ATOM 1185 C HIS A 158 -0.513 -3.665 33.467 1.00 33.98 C ATOM 1186 O HIS A 158 -1.591 -3.093 33.592 1.00 32.93 O ATOM 1187 CB HIS A 158 0.623 -2.293 31.624 1.00 0.00 C ATOM 1188 CG HIS A 158 1.910 -1.789 32.215 1.00 0.00 C ATOM 1189 ND1 HIS A 158 2.466 -2.283 33.404 1.00 0.00 N ATOM 1190 CD2 HIS A 158 2.750 -0.823 31.705 1.00 0.00 C ATOM 1191 CE1 HIS A 158 3.607 -1.620 33.551 1.00 0.00 C ATOM 1192 NE2 HIS A 158 3.825 -0.739 32.574 1.00 0.00 N ATOM 1193 N ARG A 159 0.082 -4.336 34.464 1.00 32.47 N ATOM 1194 CA ARG A 159 -0.500 -4.571 35.800 1.00 31.34 C ATOM 1195 C ARG A 159 -1.802 -5.411 35.761 1.00 30.61 C ATOM 1196 O ARG A 159 -2.658 -5.247 36.625 1.00 29.83 O ATOM 1197 CB ARG A 159 -0.692 -3.249 36.593 1.00 0.00 C ATOM 1198 CG ARG A 159 0.575 -2.391 36.755 1.00 0.00 C ATOM 1199 CD ARG A 159 0.274 -1.059 37.463 1.00 0.00 C ATOM 1200 NE ARG A 159 1.498 -0.374 37.920 1.00 0.00 N ATOM 1201 CZ ARG A 159 1.603 0.907 38.308 1.00 0.00 C ATOM 1202 NH1 ARG A 159 0.552 1.728 38.249 1.00 0.00 N ATOM 1203 NH2 ARG A 159 2.772 1.365 38.759 1.00 0.00 N1+ ATOM 1204 N ASN A 160 -1.923 -6.288 34.753 1.00 29.58 N ATOM 1205 CA ASN A 160 -3.053 -7.197 34.478 1.00 28.20 C ATOM 1206 C ASN A 160 -4.328 -6.500 33.956 1.00 27.13 C ATOM 1207 O ASN A 160 -5.277 -7.191 33.591 1.00 25.24 O ATOM 1208 CB ASN A 160 -3.384 -8.123 35.683 1.00 0.00 C ATOM 1209 CG ASN A 160 -3.700 -9.564 35.272 1.00 0.00 C ATOM 1210 OD1 ASN A 160 -2.943 -10.478 35.573 1.00 0.00 O ATOM 1211 ND2 ASN A 160 -4.804 -9.791 34.574 1.00 0.00 N ATOM 1212 N VAL A 161 -4.326 -5.167 33.881 1.00 24.61 N ATOM 1213 CA VAL A 161 -5.315 -4.376 33.159 1.00 24.99 C ATOM 1214 C VAL A 161 -4.770 -4.186 31.730 1.00 22.89 C ATOM 1215 O VAL A 161 -3.548 -4.138 31.563 1.00 24.46 O ATOM 1216 CB VAL A 161 -5.475 -2.977 33.825 1.00 0.00 C ATOM 1217 CG1 VAL A 161 -6.459 -2.034 33.098 1.00 0.00 C ATOM 1218 CG2 VAL A 161 -5.893 -3.106 35.304 1.00 0.00 C ATOM 1219 N THR A 162 -5.651 -4.105 30.730 1.00 21.81 N ATOM 1220 CA THR A 162 -5.293 -3.835 29.339 1.00 21.55 C ATOM 1221 C THR A 162 -4.807 -2.354 29.202 1.00 20.55 C ATOM 1222 O THR A 162 -5.151 -1.552 30.064 1.00 17.55 O ATOM 1223 CB THR A 162 -6.546 -3.867 28.429 1.00 0.00 C ATOM 1224 OG1 THR A 162 -7.422 -4.904 28.861 1.00 0.00 O ATOM 1225 CG2 THR A 162 -6.200 -4.132 26.956 1.00 0.00 C ATOM 1226 N PHE A 163 -4.100 -1.942 28.142 1.00 31.02 N ATOM 1227 CA PHE A 163 -3.848 -0.508 27.907 1.00 32.28 C ATOM 1228 C PHE A 163 -5.148 0.279 27.608 1.00 31.44 C ATOM 1229 O PHE A 163 -5.204 1.479 27.858 1.00 32.07 O ATOM 1230 CB PHE A 163 -2.842 -0.365 26.752 1.00 0.00 C ATOM 1231 CG PHE A 163 -2.346 1.020 26.353 1.00 0.00 C ATOM 1232 CD1 PHE A 163 -2.224 2.072 27.288 1.00 0.00 C ATOM 1233 CD2 PHE A 163 -1.964 1.245 25.014 1.00 0.00 C ATOM 1234 CE1 PHE A 163 -1.765 3.339 26.877 1.00 0.00 C ATOM 1235 CE2 PHE A 163 -1.499 2.509 24.603 1.00 0.00 C ATOM 1236 CZ PHE A 163 -1.406 3.559 25.534 1.00 0.00 C ATOM 1237 N LEU A 164 -6.197 -0.404 27.112 1.00 31.02 N ATOM 1238 CA LEU A 164 -7.545 0.116 26.845 1.00 30.54 C ATOM 1239 C LEU A 164 -7.477 1.107 25.678 1.00 30.29 C ATOM 1240 O LEU A 164 -7.678 2.309 25.833 1.00 30.82 O ATOM 1241 CB LEU A 164 -8.241 0.678 28.111 1.00 0.00 C ATOM 1242 CG LEU A 164 -8.437 -0.347 29.252 1.00 0.00 C ATOM 1243 CD1 LEU A 164 -8.775 0.354 30.575 1.00 0.00 C ATOM 1244 CD2 LEU A 164 -9.504 -1.402 28.918 1.00 0.00 C ATOM 1245 N SER A 165 -7.102 0.583 24.512 1.00 27.98 N ATOM 1246 CA SER A 165 -6.671 1.325 23.357 1.00 27.56 C ATOM 1247 C SER A 165 -7.261 0.679 22.099 1.00 27.51 C ATOM 1248 O SER A 165 -7.759 -0.449 22.130 1.00 28.08 O ATOM 1249 CB SER A 165 -5.127 1.346 23.409 1.00 0.00 C ATOM 1250 OG SER A 165 -4.550 2.072 22.347 1.00 0.00 O ATOM 1251 N CYS A 166 -7.143 1.387 20.979 1.00 64.12 N ANISOU 1251 N CYS A 166 10036 7360 6965 194 -84 227 ATOM 1252 CA CYS A 166 -6.970 0.795 19.665 1.00 63.85 C ANISOU 1252 CA CYS A 166 10038 7326 6893 171 -47 286 ATOM 1253 C CYS A 166 -6.111 1.735 18.821 1.00 64.13 C ANISOU 1253 C CYS A 166 10094 7351 6922 149 -23 322 ATOM 1254 O CYS A 166 -6.539 2.211 17.772 1.00 64.07 O ANISOU 1254 O CYS A 166 10122 7323 6896 167 -49 335 ATOM 1255 CB CYS A 166 -8.266 0.258 19.018 1.00 63.58 C ANISOU 1255 CB CYS A 166 10057 7277 6820 196 -78 313 ATOM 1256 SG CYS A 166 -7.990 -0.649 17.461 1.00 63.42 S ANISOU 1256 SG CYS A 166 10079 7263 6754 167 -40 388 ATOM 1257 N GLN A 167 -4.902 2.009 19.303 1.00 64.71 N ANISOU 1257 N GLN A 167 10142 7436 7008 111 28 339 ATOM 1258 CA GLN A 167 -3.839 2.558 18.497 1.00 65.15 C ANISOU 1258 CA GLN A 167 10214 7477 7063 90 56 375 ATOM 1259 C GLN A 167 -3.084 1.359 17.877 1.00 64.03 C ANISOU 1259 C GLN A 167 10080 7351 6898 62 105 431 ATOM 1260 O GLN A 167 -2.856 0.332 18.512 1.00 64.05 O ANISOU 1260 O GLN A 167 10055 7379 6900 44 127 428 ATOM 1261 CB GLN A 167 -2.986 3.446 19.441 1.00 0.00 C ATOM 1262 CG GLN A 167 -1.605 3.937 18.980 1.00 0.00 C ATOM 1263 CD GLN A 167 -1.665 4.759 17.699 1.00 0.00 C ATOM 1264 OE1 GLN A 167 -2.210 4.301 16.701 1.00 0.00 O ATOM 1265 NE2 GLN A 167 -1.076 5.945 17.696 1.00 0.00 N ATOM 1266 N PHE A 168 -2.685 1.529 16.620 1.00 63.37 N ANISOU 1266 N PHE A 168 10030 7253 6792 61 121 482 ATOM 1267 CA PHE A 168 -1.814 0.711 15.771 1.00 62.75 C ANISOU 1267 CA PHE A 168 9960 7190 6689 39 162 544 ATOM 1268 C PHE A 168 -0.553 0.274 16.517 1.00 63.45 C ANISOU 1268 C PHE A 168 10011 7294 6804 0 206 548 ATOM 1269 O PHE A 168 -0.233 -0.916 16.570 1.00 63.68 O ANISOU 1269 O PHE A 168 10025 7353 6817 -22 229 567 ATOM 1270 CB PHE A 168 -1.431 1.486 14.510 1.00 61.98 C ANISOU 1270 CB PHE A 168 9900 7076 6572 51 171 593 ATOM 1271 CG PHE A 168 -0.677 0.676 13.500 1.00 61.08 C ANISOU 1271 CG PHE A 168 9794 6981 6430 34 206 662 ATOM 1272 CD1 PHE A 168 -1.353 -0.074 12.550 1.00 60.50 C ANISOU 1272 CD1 PHE A 168 9743 6928 6315 41 193 696 ATOM 1273 CD2 PHE A 168 0.715 0.676 13.487 1.00 60.93 C ANISOU 1273 CD2 PHE A 168 9761 6960 6426 9 248 696 ATOM 1274 CE1 PHE A 168 -0.658 -0.815 11.610 1.00 60.33 C ANISOU 1274 CE1 PHE A 168 9725 6929 6267 23 221 761 ATOM 1275 CE2 PHE A 168 1.417 -0.066 12.552 1.00 60.79 C ANISOU 1275 CE2 PHE A 168 9750 6965 6383 -5 276 763 ATOM 1276 CZ PHE A 168 0.730 -0.813 11.613 1.00 60.55 C ANISOU 1276 CZ PHE A 168 9736 6959 6309 2 262 795 ATOM 1277 N VAL A 169 0.119 1.223 17.175 1.00 64.33 N ANISOU 1277 N VAL A 169 10107 7382 6952 -13 215 532 ATOM 1278 CA VAL A 169 1.340 1.013 17.951 1.00 64.81 C ANISOU 1278 CA VAL A 169 10130 7452 7041 -56 255 539 ATOM 1279 C VAL A 169 1.077 0.198 19.247 1.00 64.87 C ANISOU 1279 C VAL A 169 10088 7495 7064 -74 260 495 ATOM 1280 O VAL A 169 2.024 -0.315 19.839 1.00 65.95 O ANISOU 1280 O VAL A 169 10193 7653 7211 -112 299 511 ATOM 1281 CB VAL A 169 1.971 2.406 18.279 1.00 0.00 C ATOM 1282 CG1 VAL A 169 3.463 2.299 18.653 1.00 0.00 C ATOM 1283 CG2 VAL A 169 1.792 3.460 17.159 1.00 0.00 C ATOM 1284 N SER A 170 -0.185 0.048 19.684 1.00 64.40 N ANISOU 1284 N SER A 170 10020 7443 7006 -44 222 443 ATOM 1285 CA SER A 170 -0.560 -0.760 20.841 1.00 64.46 C ANISOU 1285 CA SER A 170 9979 7486 7025 -49 225 398 ATOM 1286 C SER A 170 -0.623 -2.254 20.475 1.00 63.30 C ANISOU 1286 C SER A 170 9838 7373 6838 -52 244 417 ATOM 1287 O SER A 170 -0.352 -3.075 21.347 1.00 63.41 O ANISOU 1287 O SER A 170 9811 7425 6856 -71 272 398 ATOM 1288 CB SER A 170 -1.931 -0.308 21.389 1.00 0.00 C ATOM 1289 OG SER A 170 -2.003 1.095 21.608 1.00 0.00 O ATOM 1290 N VAL A 171 -1.000 -2.587 19.225 1.00 62.09 N ANISOU 1290 N VAL A 171 9733 7210 6645 -34 230 453 ATOM 1291 CA VAL A 171 -1.188 -3.990 18.799 1.00 61.78 C ANISOU 1291 CA VAL A 171 9708 7200 6566 -39 240 469 ATOM 1292 C VAL A 171 -0.139 -4.496 17.797 1.00 61.38 C ANISOU 1292 C VAL A 171 9676 7163 6482 -70 275 542 ATOM 1293 O VAL A 171 0.297 -5.642 17.903 1.00 61.28 O ANISOU 1293 O VAL A 171 9652 7186 6444 -94 303 553 ATOM 1294 CB VAL A 171 -2.624 -4.269 18.263 1.00 61.39 C ANISOU 1294 CB VAL A 171 9695 7134 6494 0 192 453 ATOM 1295 CG1 VAL A 171 -3.667 -3.841 19.286 1.00 61.57 C ANISOU 1295 CG1 VAL A 171 9697 7145 6550 34 155 385 ATOM 1296 CG2 VAL A 171 -2.884 -3.612 16.910 1.00 60.83 C ANISOU 1296 CG2 VAL A 171 9673 7036 6401 12 171 502 ATOM 1297 N MET A 172 0.349 -3.599 16.944 1.00 60.80 N ANISOU 1297 N MET A 172 9630 7063 6406 -68 275 589 ATOM 1298 CA MET A 172 1.419 -3.887 16.018 1.00 60.32 C ANISOU 1298 CA MET A 172 9585 7015 6318 -92 305 663 ATOM 1299 C MET A 172 2.759 -3.671 16.687 1.00 60.51 C ANISOU 1299 C MET A 172 9580 7041 6368 -125 347 684 ATOM 1300 O MET A 172 3.006 -2.635 17.305 1.00 61.02 O ANISOU 1300 O MET A 172 9635 7075 6473 -122 345 663 ATOM 1301 CB MET A 172 1.298 -3.003 14.779 1.00 0.00 C ATOM 1302 CG MET A 172 0.011 -3.320 14.020 1.00 0.00 C ATOM 1303 SD MET A 172 -0.110 -4.990 13.340 1.00 0.00 S ATOM 1304 CE MET A 172 1.465 -4.972 12.461 1.00 0.00 C ATOM 1305 N ARG A 173 3.623 -4.662 16.489 1.00 60.19 N ANISOU 1305 N ARG A 173 9530 7036 6304 -160 382 726 ATOM 1306 CA ARG A 173 5.011 -4.569 16.849 1.00 59.77 C ANISOU 1306 CA ARG A 173 9452 6986 6270 -196 423 758 ATOM 1307 C ARG A 173 5.728 -3.667 15.824 1.00 58.92 C ANISOU 1307 C ARG A 173 9370 6841 6174 -190 429 816 ATOM 1308 O ARG A 173 5.678 -3.920 14.622 1.00 58.27 O ANISOU 1308 O ARG A 173 9316 6762 6062 -176 423 865 ATOM 1309 CB ARG A 173 5.552 -6.005 16.927 1.00 0.00 C ATOM 1310 CG ARG A 173 6.998 -6.113 17.415 1.00 0.00 C ATOM 1311 CD ARG A 173 7.266 -5.796 18.901 1.00 0.00 C ATOM 1312 NE ARG A 173 6.763 -6.849 19.802 1.00 0.00 N ATOM 1313 CZ ARG A 173 7.179 -7.136 21.048 1.00 0.00 C ATOM 1314 NH1 ARG A 173 8.116 -6.415 21.676 1.00 0.00 N ATOM 1315 NH2 ARG A 173 6.638 -8.183 21.675 1.00 0.00 N1+ ATOM 1316 N MET A 174 6.410 -2.623 16.299 1.00 58.62 N ANISOU 1316 N MET A 174 9322 6767 6183 -199 440 809 ATOM 1317 CA MET A 174 7.163 -1.731 15.422 1.00 58.42 C ANISOU 1317 CA MET A 174 9322 6699 6173 -191 449 859 ATOM 1318 C MET A 174 8.446 -2.403 14.904 1.00 58.09 C ANISOU 1318 C MET A 174 9281 6678 6110 -216 483 941 ATOM 1319 O MET A 174 8.897 -2.070 13.814 1.00 57.46 O ANISOU 1319 O MET A 174 9228 6581 6022 -195 485 994 ATOM 1320 CB MET A 174 7.475 -0.413 16.153 1.00 58.93 C ANISOU 1320 CB MET A 174 9379 6715 6294 -200 450 828 ATOM 1321 CG MET A 174 6.249 0.512 16.216 1.00 59.16 C ANISOU 1321 CG MET A 174 9421 6715 6343 -165 410 762 ATOM 1322 SD MET A 174 5.801 1.212 14.605 1.00 58.94 S ANISOU 1322 SD MET A 174 9445 6658 6289 -109 386 782 ATOM 1323 CE MET A 174 4.012 1.407 14.794 1.00 59.01 C ANISOU 1323 CE MET A 174 9454 6682 6281 -78 338 714 ATOM 1324 N ASP A 175 8.990 -3.402 15.623 1.00 58.24 N ANISOU 1324 N ASP A 175 9270 6738 6118 -259 509 950 ATOM 1325 CA ASP A 175 10.099 -4.245 15.162 1.00 58.24 C ANISOU 1325 CA ASP A 175 9268 6770 6088 -287 538 1027 ATOM 1326 C ASP A 175 9.699 -5.041 13.890 1.00 57.46 C ANISOU 1326 C ASP A 175 9192 6699 5938 -266 523 1067 ATOM 1327 O ASP A 175 10.470 -5.083 12.933 1.00 57.15 O ANISOU 1327 O ASP A 175 9168 6658 5889 -261 532 1139 ATOM 1328 CB ASP A 175 10.749 -5.005 16.366 1.00 0.00 C ATOM 1329 CG ASP A 175 10.809 -6.539 16.402 1.00 0.00 C ATOM 1330 OD1 ASP A 175 9.821 -7.143 16.859 1.00 0.00 O ATOM 1331 OD2 ASP A 175 11.806 -7.114 15.926 1.00 0.00 O1- ATOM 1332 N TYR A 176 8.440 -5.505 13.822 1.00 56.90 N ANISOU 1332 N TYR A 176 9125 6654 5839 -252 498 1020 ATOM 1333 CA TYR A 176 7.825 -6.061 12.612 1.00 56.33 C ANISOU 1333 CA TYR A 176 9076 6603 5723 -234 476 1048 ATOM 1334 C TYR A 176 7.732 -5.020 11.481 1.00 55.85 C ANISOU 1334 C TYR A 176 9041 6504 5675 -194 462 1081 ATOM 1335 O TYR A 176 8.149 -5.284 10.348 1.00 55.72 O ANISOU 1335 O TYR A 176 9034 6504 5633 -190 465 1148 ATOM 1336 CB TYR A 176 6.435 -6.658 12.927 1.00 56.15 C ANISOU 1336 CB TYR A 176 9056 6597 5679 -223 447 983 ATOM 1337 CG TYR A 176 5.546 -6.829 11.713 1.00 55.90 C ANISOU 1337 CG TYR A 176 9054 6569 5616 -199 415 1001 ATOM 1338 CD1 TYR A 176 5.713 -7.909 10.850 1.00 55.96 C ANISOU 1338 CD1 TYR A 176 9068 6618 5574 -220 413 1052 ATOM 1339 CD2 TYR A 176 4.544 -5.898 11.420 1.00 55.81 C ANISOU 1339 CD2 TYR A 176 9062 6520 5621 -160 384 971 ATOM 1340 CE1 TYR A 176 4.908 -8.066 9.736 1.00 55.91 C ANISOU 1340 CE1 TYR A 176 9085 6615 5540 -204 383 1072 ATOM 1341 CE2 TYR A 176 3.736 -6.040 10.304 1.00 55.64 C ANISOU 1341 CE2 TYR A 176 9065 6504 5570 -142 357 993 ATOM 1342 CZ TYR A 176 3.921 -7.118 9.462 1.00 55.83 C ANISOU 1342 CZ TYR A 176 9093 6568 5549 -166 356 1045 ATOM 1343 OH TYR A 176 3.115 -7.254 8.354 1.00 56.12 O ANISOU 1343 OH TYR A 176 9152 6611 5558 -154 328 1070 ATOM 1344 N MET A 177 7.217 -3.825 11.811 1.00 55.31 N ANISOU 1344 N MET A 177 8982 6389 5644 -165 447 1033 ATOM 1345 CA MET A 177 6.983 -2.743 10.858 1.00 54.91 C ANISOU 1345 CA MET A 177 8957 6304 5601 -122 435 1052 ATOM 1346 C MET A 177 8.279 -2.257 10.212 1.00 54.83 C ANISOU 1346 C MET A 177 8951 6271 5608 -117 463 1119 ATOM 1347 O MET A 177 8.325 -2.036 9.005 1.00 54.66 O ANISOU 1347 O MET A 177 8945 6252 5570 -89 462 1168 ATOM 1348 CB MET A 177 6.309 -1.528 11.526 1.00 54.98 C ANISOU 1348 CB MET A 177 8977 6270 5643 -95 412 982 ATOM 1349 CG MET A 177 4.894 -1.775 12.054 1.00 54.46 C ANISOU 1349 CG MET A 177 8921 6215 5553 -74 375 937 ATOM 1350 SD MET A 177 3.736 -2.524 10.883 1.00 54.09 S ANISOU 1350 SD MET A 177 8908 6168 5474 -33 356 978 ATOM 1351 CE MET A 177 3.795 -1.341 9.522 1.00 54.11 C ANISOU 1351 CE MET A 177 8906 6228 5424 -58 352 1026 ATOM 1352 N VAL A 178 9.324 -2.097 11.022 1.00 54.90 N ANISOU 1352 N VAL A 178 8947 6261 5651 -145 487 1122 ATOM 1353 CA VAL A 178 10.620 -1.574 10.581 1.00 55.38 C ANISOU 1353 CA VAL A 178 9015 6289 5736 -141 512 1183 ATOM 1354 C VAL A 178 11.472 -2.662 9.920 1.00 55.29 C ANISOU 1354 C VAL A 178 8992 6323 5690 -162 530 1267 ATOM 1355 O VAL A 178 11.852 -2.529 8.743 1.00 55.30 O ANISOU 1355 O VAL A 178 9004 6326 5681 -134 533 1328 ATOM 1356 CB VAL A 178 11.383 -0.917 11.757 1.00 56.00 C ANISOU 1356 CB VAL A 178 9086 6322 5867 -167 528 1158 ATOM 1357 CG1 VAL A 178 12.810 -0.530 11.366 1.00 56.52 C ANISOU 1357 CG1 VAL A 178 9162 6352 5960 -169 554 1227 ATOM 1358 CG2 VAL A 178 10.617 0.305 12.237 1.00 56.05 C ANISOU 1358 CG2 VAL A 178 9107 6281 5908 -142 505 1081 ATOM 1359 N TYR A 179 11.759 -3.731 10.671 1.00 55.05 N ANISOU 1359 N TYR A 179 8940 6336 5641 -210 542 1268 ATOM 1360 CA TYR A 179 12.691 -4.760 10.194 1.00 55.05 C ANISOU 1360 CA TYR A 179 8928 6381 5606 -238 560 1348 ATOM 1361 C TYR A 179 12.059 -5.634 9.112 1.00 54.71 C ANISOU 1361 C TYR A 179 8887 6390 5507 -229 540 1375 ATOM 1362 O TYR A 179 12.638 -5.809 8.033 1.00 54.76 O ANISOU 1362 O TYR A 179 8896 6413 5497 -217 542 1450 ATOM 1363 CB TYR A 179 13.208 -5.639 11.342 1.00 55.27 C ANISOU 1363 CB TYR A 179 8932 6445 5623 -294 581 1340 ATOM 1364 CG TYR A 179 13.860 -4.889 12.498 1.00 55.51 C ANISOU 1364 CG TYR A 179 8952 6430 5707 -316 601 1317 ATOM 1365 CD1 TYR A 179 14.806 -3.882 12.268 1.00 55.76 C ANISOU 1365 CD1 TYR A 179 8999 6400 5785 -303 612 1358 ATOM 1366 CD2 TYR A 179 13.551 -5.209 13.826 1.00 55.41 C ANISOU 1366 CD2 TYR A 179 8915 6437 5700 -350 609 1256 ATOM 1367 CE1 TYR A 179 15.414 -3.213 13.324 1.00 55.99 C ANISOU 1367 CE1 TYR A 179 9022 6385 5865 -330 628 1338 ATOM 1368 CE2 TYR A 179 14.145 -4.537 14.884 1.00 55.69 C ANISOU 1368 CE2 TYR A 179 8936 6436 5785 -376 626 1238 ATOM 1369 CZ TYR A 179 15.079 -3.545 14.631 1.00 55.99 C ANISOU 1369 CZ TYR A 179 8993 6410 5869 -370 634 1280 ATOM 1370 OH TYR A 179 15.671 -2.881 15.681 1.00 56.12 O ANISOU 1370 OH TYR A 179 8998 6387 5937 -403 649 1264 ATOM 1371 N PHE A 180 10.865 -6.160 9.388 1.00 54.53 N ANISOU 1371 N PHE A 180 8865 6393 5459 -233 518 1316 ATOM 1372 CA PHE A 180 10.221 -7.094 8.468 1.00 54.58 C ANISOU 1372 CA PHE A 180 8876 6449 5413 -235 496 1338 ATOM 1373 C PHE A 180 9.559 -6.352 7.303 1.00 54.56 C ANISOU 1373 C PHE A 180 8890 6427 5412 -189 475 1351 ATOM 1374 O PHE A 180 9.996 -6.484 6.160 1.00 54.90 O ANISOU 1374 O PHE A 180 8931 6490 5437 -179 476 1423 ATOM 1375 CB PHE A 180 9.222 -7.998 9.210 1.00 54.29 C ANISOU 1375 CB PHE A 180 8838 6442 5348 -257 480 1270 ATOM 1376 CG PHE A 180 8.814 -9.213 8.440 1.00 54.01 C ANISOU 1376 CG PHE A 180 8807 6459 5255 -276 461 1295 ATOM 1377 CD1 PHE A 180 9.674 -10.295 8.337 1.00 54.31 C ANISOU 1377 CD1 PHE A 180 8834 6549 5253 -317 475 1345 ATOM 1378 CD2 PHE A 180 7.570 -9.283 7.819 1.00 53.57 C ANISOU 1378 CD2 PHE A 180 8769 6402 5182 -258 426 1271 ATOM 1379 CE1 PHE A 180 9.300 -11.431 7.633 1.00 54.38 C ANISOU 1379 CE1 PHE A 180 8848 6606 5205 -339 453 1366 ATOM 1380 CE2 PHE A 180 7.195 -10.407 7.106 1.00 53.68 C ANISOU 1380 CE2 PHE A 180 8789 6461 5144 -282 405 1295 ATOM 1381 CZ PHE A 180 8.062 -11.486 7.014 1.00 53.97 C ANISOU 1381 CZ PHE A 180 8814 6548 5141 -323 418 1340 ATOM 1382 N SER A 181 8.516 -5.557 7.570 1.00 54.55 N ANISOU 1382 N SER A 181 8904 6391 5432 -160 458 1287 ATOM 1383 CA SER A 181 7.728 -4.921 6.534 1.00 54.87 C ANISOU 1383 CA SER A 181 8961 6421 5467 -119 438 1295 ATOM 1384 C SER A 181 8.570 -3.894 5.753 1.00 55.40 C ANISOU 1384 C SER A 181 9031 6459 5557 -82 457 1347 ATOM 1385 O SER A 181 8.712 -4.028 4.545 1.00 55.68 O ANISOU 1385 O SER A 181 9063 6521 5571 -65 456 1410 ATOM 1386 CB SER A 181 6.455 -4.329 7.168 1.00 0.00 C ATOM 1387 OG SER A 181 5.634 -3.692 6.214 1.00 0.00 O ATOM 1388 N PHE A 182 9.170 -2.903 6.413 1.00 55.59 N ANISOU 1388 N PHE A 182 9061 6431 5629 -69 474 1322 ATOM 1389 CA PHE A 182 9.830 -1.780 5.739 1.00 55.66 C ANISOU 1389 CA PHE A 182 9082 6400 5667 -25 490 1354 ATOM 1390 C PHE A 182 11.193 -2.148 5.125 1.00 55.61 C ANISOU 1390 C PHE A 182 9062 6406 5661 -29 514 1442 ATOM 1391 O PHE A 182 11.405 -1.958 3.906 1.00 55.43 O ANISOU 1391 O PHE A 182 9036 6396 5626 5 518 1499 ATOM 1392 CB PHE A 182 9.938 -0.583 6.696 1.00 56.02 C ANISOU 1392 CB PHE A 182 9143 6378 5763 -13 494 1292 ATOM 1393 CG PHE A 182 10.580 0.640 6.090 1.00 56.50 C ANISOU 1393 CG PHE A 182 9223 6388 5855 34 510 1312 ATOM 1394 CD1 PHE A 182 10.173 1.129 4.852 1.00 56.56 C ANISOU 1394 CD1 PHE A 182 9241 6405 5844 84 507 1335 ATOM 1395 CD2 PHE A 182 11.578 1.324 6.781 1.00 57.08 C ANISOU 1395 CD2 PHE A 182 9304 6403 5978 28 527 1305 ATOM 1396 CE1 PHE A 182 10.764 2.257 4.303 1.00 57.08 C ANISOU 1396 CE1 PHE A 182 9325 6424 5936 134 524 1348 ATOM 1397 CE2 PHE A 182 12.169 2.455 6.238 1.00 57.44 C ANISOU 1397 CE2 PHE A 182 9374 6394 6054 75 541 1318 ATOM 1398 CZ PHE A 182 11.763 2.922 4.996 1.00 57.44 C ANISOU 1398 CZ PHE A 182 9384 6405 6033 131 540 1337 ATOM 1399 N LEU A 183 12.114 -2.677 5.937 1.00 55.65 N ANISOU 1399 N LEU A 183 9055 6411 5678 -71 530 1456 ATOM 1400 CA LEU A 183 13.479 -2.959 5.491 1.00 55.86 C ANISOU 1400 CA LEU A 183 9070 6445 5706 -77 551 1544 ATOM 1401 C LEU A 183 13.521 -4.076 4.432 1.00 55.83 C ANISOU 1401 C LEU A 183 9047 6515 5649 -92 543 1613 ATOM 1402 O LEU A 183 14.197 -3.892 3.419 1.00 55.65 O ANISOU 1402 O LEU A 183 9016 6501 5627 -71 553 1691 ATOM 1403 CB LEU A 183 14.398 -3.250 6.702 1.00 0.00 C ATOM 1404 CG LEU A 183 15.206 -2.045 7.245 1.00 0.00 C ATOM 1405 CD1 LEU A 183 14.380 -0.766 7.512 1.00 0.00 C ATOM 1406 CD2 LEU A 183 16.032 -2.463 8.481 1.00 0.00 C ATOM 1407 N THR A 184 12.786 -5.179 4.645 1.00 55.84 N ANISOU 1407 N THR A 184 9040 6567 5606 -127 524 1586 ATOM 1408 CA THR A 184 12.811 -6.295 3.700 1.00 55.97 C ANISOU 1408 CA THR A 184 9040 6655 5569 -148 511 1646 ATOM 1409 C THR A 184 11.689 -6.246 2.639 1.00 55.85 C ANISOU 1409 C THR A 184 9027 6662 5531 -119 488 1651 ATOM 1410 O THR A 184 12.012 -6.528 1.483 1.00 55.91 O ANISOU 1410 O THR A 184 9018 6707 5516 -109 484 1724 ATOM 1411 CB THR A 184 12.888 -7.683 4.397 1.00 0.00 C ATOM 1412 OG1 THR A 184 11.688 -8.192 4.939 1.00 0.00 O ATOM 1413 CG2 THR A 184 14.000 -7.790 5.449 1.00 0.00 C ATOM 1414 N TRP A 185 10.442 -5.855 2.980 1.00 55.88 N ANISOU 1414 N TRP A 185 9048 6645 5539 -108 471 1578 ATOM 1415 CA TRP A 185 9.338 -5.927 2.008 1.00 56.06 C ANISOU 1415 CA TRP A 185 9073 6694 5531 -93 446 1580 ATOM 1416 C TRP A 185 8.911 -4.594 1.366 1.00 56.32 C ANISOU 1416 C TRP A 185 9117 6694 5587 -34 449 1572 ATOM 1417 O TRP A 185 8.077 -4.599 0.452 1.00 55.87 O ANISOU 1417 O TRP A 185 9060 6664 5505 -22 432 1586 ATOM 1418 CB TRP A 185 8.141 -6.650 2.638 1.00 55.72 C ANISOU 1418 CB TRP A 185 9042 6663 5463 -126 418 1515 ATOM 1419 CG TRP A 185 8.447 -8.080 2.934 1.00 55.67 C ANISOU 1419 CG TRP A 185 9026 6704 5420 -181 412 1529 ATOM 1420 CD1 TRP A 185 8.602 -8.655 4.165 1.00 55.55 C ANISOU 1420 CD1 TRP A 185 9012 6687 5405 -215 419 1482 ATOM 1421 CD2 TRP A 185 8.670 -9.112 1.979 1.00 55.88 C ANISOU 1421 CD2 TRP A 185 9038 6791 5401 -210 399 1596 ATOM 1422 NE1 TRP A 185 8.896 -9.989 4.032 1.00 55.56 N ANISOU 1422 NE1 TRP A 185 9005 6743 5359 -260 412 1512 ATOM 1423 CE2 TRP A 185 8.944 -10.296 2.700 1.00 55.78 C ANISOU 1423 CE2 TRP A 185 9024 6810 5360 -261 397 1582 ATOM 1424 CE3 TRP A 185 8.682 -9.150 0.580 1.00 56.19 C ANISOU 1424 CE3 TRP A 185 9062 6865 5420 -199 388 1668 ATOM 1425 CZ2 TRP A 185 9.223 -11.511 2.068 1.00 56.08 C ANISOU 1425 CZ2 TRP A 185 9051 6908 5346 -302 382 1634 ATOM 1426 CZ3 TRP A 185 8.954 -10.363 -0.051 1.00 56.46 C ANISOU 1426 CZ3 TRP A 185 9081 6962 5408 -242 372 1723 ATOM 1427 CH2 TRP A 185 9.214 -11.527 0.694 1.00 56.37 C ANISOU 1427 CH2 TRP A 185 9073 6978 5366 -293 367 1704 ATOM 1428 N ILE A 186 9.447 -3.431 1.760 1.00 56.97 N ANISOU 1428 N ILE A 186 9211 6718 5715 0 471 1550 ATOM 1429 CA ILE A 186 9.130 -2.154 1.098 1.00 57.69 C ANISOU 1429 CA ILE A 186 9313 6779 5824 60 480 1548 ATOM 1430 C ILE A 186 10.398 -1.643 0.414 1.00 58.67 C ANISOU 1430 C ILE A 186 9427 6891 5972 98 509 1616 ATOM 1431 O ILE A 186 10.420 -1.491 -0.807 1.00 59.21 O ANISOU 1431 O ILE A 186 9480 6990 6023 131 513 1669 ATOM 1432 CB ILE A 186 8.504 -1.119 2.082 1.00 0.00 C ATOM 1433 CG1 ILE A 186 7.195 -1.641 2.720 1.00 0.00 C ATOM 1434 CG2 ILE A 186 8.269 0.261 1.434 1.00 0.00 C ATOM 1435 CD1 ILE A 186 6.547 -0.736 3.778 1.00 0.00 C ATOM 1436 N PHE A 187 11.452 -1.376 1.194 1.00 59.31 N ANISOU 1436 N PHE A 187 9514 6926 6092 93 528 1616 ATOM 1437 CA PHE A 187 12.675 -0.708 0.758 1.00 59.99 C ANISOU 1437 CA PHE A 187 9599 6982 6210 139 554 1671 ATOM 1438 C PHE A 187 13.355 -1.350 -0.467 1.00 60.75 C ANISOU 1438 C PHE A 187 9662 7135 6282 149 560 1772 ATOM 1439 O PHE A 187 13.627 -0.660 -1.450 1.00 61.14 O ANISOU 1439 O PHE A 187 9705 7182 6340 208 574 1811 ATOM 1440 CB PHE A 187 13.603 -0.518 1.978 1.00 0.00 C ATOM 1441 CG PHE A 187 14.995 0.013 1.688 1.00 0.00 C ATOM 1442 CD1 PHE A 187 15.181 1.378 1.384 1.00 0.00 C ATOM 1443 CD2 PHE A 187 16.085 -0.876 1.570 1.00 0.00 C ATOM 1444 CE1 PHE A 187 16.441 1.841 1.029 1.00 0.00 C ATOM 1445 CE2 PHE A 187 17.335 -0.393 1.211 1.00 0.00 C ATOM 1446 CZ PHE A 187 17.514 0.960 0.949 1.00 0.00 C ATOM 1447 N ILE A 188 13.565 -2.671 -0.415 1.00 61.37 N ANISOU 1447 N ILE A 188 9719 7269 6329 94 548 1814 ATOM 1448 CA ILE A 188 14.216 -3.425 -1.486 1.00 62.30 C ANISOU 1448 CA ILE A 188 9802 7445 6421 100 548 1911 ATOM 1449 C ILE A 188 13.467 -3.385 -2.855 1.00 63.36 C ANISOU 1449 C ILE A 188 9916 7634 6523 127 536 1936 ATOM 1450 O ILE A 188 14.100 -2.968 -3.828 1.00 64.27 O ANISOU 1450 O ILE A 188 10007 7767 6644 174 549 2003 ATOM 1451 CB ILE A 188 14.585 -4.867 -1.015 1.00 0.00 C ATOM 1452 CG1 ILE A 188 15.665 -4.814 0.092 1.00 0.00 C ATOM 1453 CG2 ILE A 188 15.017 -5.830 -2.144 1.00 0.00 C ATOM 1454 CD1 ILE A 188 15.831 -6.132 0.865 1.00 0.00 C ATOM 1455 N PRO A 189 12.146 -3.707 -2.917 1.00 64.02 N ANISOU 1455 N PRO A 189 10007 7741 6575 99 513 1885 ATOM 1456 CA PRO A 189 11.301 -3.473 -4.094 1.00 64.64 C ANISOU 1456 CA PRO A 189 10070 7861 6628 127 505 1904 ATOM 1457 C PRO A 189 11.399 -2.055 -4.655 1.00 66.07 C ANISOU 1457 C PRO A 189 10258 8006 6839 206 532 1899 ATOM 1458 O PRO A 189 11.556 -1.897 -5.870 1.00 66.70 O ANISOU 1458 O PRO A 189 10307 8127 6908 245 542 1961 ATOM 1459 CB PRO A 189 9.887 -3.747 -3.573 1.00 63.90 C ANISOU 1459 CB PRO A 189 9999 7771 6510 90 478 1833 ATOM 1460 CG PRO A 189 10.090 -4.786 -2.535 1.00 63.74 C ANISOU 1460 CG PRO A 189 9985 7752 6481 28 464 1811 ATOM 1461 CD PRO A 189 11.421 -4.486 -1.890 1.00 63.73 C ANISOU 1461 CD PRO A 189 9986 7708 6517 38 490 1824 ATOM 1462 N LEU A 190 11.327 -1.050 -3.779 1.00 67.33 N ANISOU 1462 N LEU A 190 10456 8092 7034 230 544 1826 ATOM 1463 CA LEU A 190 11.402 0.356 -4.200 1.00 68.70 C ANISOU 1463 CA LEU A 190 10644 8223 7233 305 569 1807 ATOM 1464 C LEU A 190 12.708 0.659 -4.923 1.00 69.91 C ANISOU 1464 C LEU A 190 10778 8370 7414 356 597 1878 ATOM 1465 O LEU A 190 12.690 1.203 -6.040 1.00 70.48 O ANISOU 1465 O LEU A 190 10832 8466 7481 415 614 1913 ATOM 1466 CB LEU A 190 11.242 1.309 -3.012 1.00 68.91 C ANISOU 1466 CB LEU A 190 10717 8169 7296 312 572 1715 ATOM 1467 CG LEU A 190 9.868 1.374 -2.340 1.00 69.14 C ANISOU 1467 CG LEU A 190 10769 8196 7304 284 546 1636 ATOM 1468 CD1 LEU A 190 9.960 2.215 -1.076 1.00 69.43 C ANISOU 1468 CD1 LEU A 190 10843 8154 7381 285 547 1555 ATOM 1469 CD2 LEU A 190 8.803 1.927 -3.279 1.00 69.40 C ANISOU 1469 CD2 LEU A 190 10802 8262 7305 321 543 1630 ATOM 1470 N VAL A 191 13.832 0.292 -4.290 1.00 70.85 N ANISOU 1470 N VAL A 191 10899 8457 7561 334 601 1903 ATOM 1471 CA VAL A 191 15.183 0.463 -4.820 1.00 72.33 C ANISOU 1471 CA VAL A 191 11071 8630 7779 382 625 1976 ATOM 1472 C VAL A 191 15.375 -0.264 -6.168 1.00 72.92 C ANISOU 1472 C VAL A 191 11091 8792 7820 391 621 2071 ATOM 1473 O VAL A 191 15.866 0.342 -7.123 1.00 73.58 O ANISOU 1473 O VAL A 191 11154 8884 7918 461 642 2119 ATOM 1474 CB VAL A 191 16.246 -0.007 -3.780 1.00 0.00 C ATOM 1475 CG1 VAL A 191 17.675 -0.219 -4.323 1.00 0.00 C ATOM 1476 CG2 VAL A 191 16.301 0.965 -2.588 1.00 0.00 C ATOM 1477 N VAL A 192 14.919 -1.522 -6.231 1.00 72.63 N ANISOU 1477 N VAL A 192 11031 8824 7739 322 593 2095 ATOM 1478 CA VAL A 192 14.918 -2.345 -7.436 1.00 72.65 C ANISOU 1478 CA VAL A 192 10980 8917 7705 317 581 2182 ATOM 1479 C VAL A 192 14.078 -1.718 -8.571 1.00 73.07 C ANISOU 1479 C VAL A 192 11012 9010 7741 367 590 2186 ATOM 1480 O VAL A 192 14.573 -1.616 -9.691 1.00 73.93 O ANISOU 1480 O VAL A 192 11076 9162 7848 413 603 2260 ATOM 1481 CB VAL A 192 14.451 -3.796 -7.110 1.00 0.00 C ATOM 1482 CG1 VAL A 192 14.066 -4.666 -8.321 1.00 0.00 C ATOM 1483 CG2 VAL A 192 15.521 -4.536 -6.284 1.00 0.00 C ATOM 1484 N MET A 193 12.863 -1.246 -8.261 1.00 72.56 N ANISOU 1484 N MET A 193 10976 8930 7662 359 584 2109 ATOM 1485 CA MET A 193 11.992 -0.535 -9.210 1.00 72.61 C ANISOU 1485 CA MET A 193 10970 8968 7650 404 595 2104 ATOM 1486 C MET A 193 12.621 0.763 -9.717 1.00 73.54 C ANISOU 1486 C MET A 193 11090 9047 7802 500 636 2108 ATOM 1487 O MET A 193 12.627 1.024 -10.931 1.00 74.18 O ANISOU 1487 O MET A 193 11130 9182 7871 550 654 2160 ATOM 1488 CB MET A 193 10.637 -0.209 -8.578 1.00 71.85 C ANISOU 1488 CB MET A 193 10913 8850 7534 378 580 2016 ATOM 1489 CG MET A 193 9.652 -1.355 -8.563 1.00 71.13 C ANISOU 1489 CG MET A 193 10813 8814 7399 300 541 2019 ATOM 1490 SD MET A 193 8.041 -0.813 -7.970 1.00 70.81 S ANISOU 1490 SD MET A 193 10817 8745 7340 286 524 1925 ATOM 1491 CE MET A 193 8.299 -0.820 -6.199 1.00 70.03 C ANISOU 1491 CE MET A 193 10768 8562 7276 256 514 1840 ATOM 1492 N CYS A 194 13.210 1.571 -8.812 1.00 74.00 N ANISOU 1492 N CYS A 194 11196 9014 7904 525 651 2050 ATOM 1493 CA CYS A 194 13.940 2.810 -9.151 1.00 75.08 C ANISOU 1493 CA CYS A 194 11346 9097 8081 616 688 2046 ATOM 1494 C CYS A 194 15.070 2.533 -10.168 1.00 76.35 C ANISOU 1494 C CYS A 194 11458 9291 8258 659 704 2146 ATOM 1495 O CYS A 194 15.142 3.202 -11.202 1.00 77.08 O ANISOU 1495 O CYS A 194 11533 9394 8360 740 734 2169 ATOM 1496 CB CYS A 194 14.441 3.596 -7.900 1.00 0.00 C ATOM 1497 SG CYS A 194 15.164 5.237 -8.313 1.00 0.00 S ATOM 1498 N ALA A 195 15.857 1.479 -9.896 1.00 77.31 N ANISOU 1498 N ALA A 195 11559 9433 8380 607 684 2206 ATOM 1499 CA ALA A 195 16.887 0.962 -10.793 1.00 79.21 C ANISOU 1499 CA ALA A 195 11748 9714 8631 642 692 2309 ATOM 1500 C ALA A 195 16.330 0.491 -12.148 1.00 79.85 C ANISOU 1500 C ALA A 195 11763 9906 8669 653 689 2374 ATOM 1501 O ALA A 195 16.854 0.920 -13.175 1.00 81.00 O ANISOU 1501 O ALA A 195 11869 10080 8828 730 714 2429 ATOM 1502 CB ALA A 195 17.683 -0.150 -10.095 1.00 0.00 C ATOM 1503 N ILE A 196 15.262 -0.328 -12.135 1.00 80.06 N ANISOU 1503 N ILE A 196 11777 9993 8646 574 657 2366 ATOM 1504 CA ILE A 196 14.620 -0.843 -13.356 1.00 80.31 C ANISOU 1504 CA ILE A 196 11747 10131 8634 564 648 2425 ATOM 1505 C ILE A 196 14.178 0.291 -14.295 1.00 81.28 C ANISOU 1505 C ILE A 196 11853 10272 8757 648 684 2417 ATOM 1506 O ILE A 196 14.421 0.223 -15.510 1.00 81.64 O ANISOU 1506 O ILE A 196 11835 10390 8794 689 697 2494 ATOM 1507 CB ILE A 196 13.418 -1.767 -13.026 1.00 79.34 C ANISOU 1507 CB ILE A 196 11632 10050 8462 468 608 2396 ATOM 1508 CG1 ILE A 196 13.911 -3.113 -12.485 1.00 78.84 C ANISOU 1508 CG1 ILE A 196 11564 10004 8385 387 572 2428 ATOM 1509 CG2 ILE A 196 12.532 -2.007 -14.247 1.00 79.69 C ANISOU 1509 CG2 ILE A 196 11623 10189 8463 460 601 2440 ATOM 1510 CD1 ILE A 196 12.900 -3.831 -11.612 1.00 78.13 C ANISOU 1510 CD1 ILE A 196 11511 9910 8265 300 539 2365 ATOM 1511 N TYR A 197 13.530 1.321 -13.734 1.00 82.01 N ANISOU 1511 N TYR A 197 12000 10302 8856 674 701 2325 ATOM 1512 CA TYR A 197 13.046 2.435 -14.557 1.00 83.60 C ANISOU 1512 CA TYR A 197 12193 10521 9051 753 738 2309 ATOM 1513 C TYR A 197 14.195 3.222 -15.192 1.00 85.19 C ANISOU 1513 C TYR A 197 12375 10700 9293 857 779 2345 ATOM 1514 O TYR A 197 14.181 3.430 -16.404 1.00 86.71 O ANISOU 1514 O TYR A 197 12510 10963 9471 912 803 2400 ATOM 1515 CB TYR A 197 12.074 3.347 -13.786 1.00 83.12 C ANISOU 1515 CB TYR A 197 12198 10401 8982 754 742 2201 ATOM 1516 CG TYR A 197 10.669 2.781 -13.719 1.00 82.39 C ANISOU 1516 CG TYR A 197 12105 10359 8838 678 711 2181 ATOM 1517 CD1 TYR A 197 9.903 2.633 -14.875 1.00 82.68 C ANISOU 1517 CD1 TYR A 197 12091 10489 8831 678 715 2229 ATOM 1518 CD2 TYR A 197 10.108 2.384 -12.510 1.00 81.78 C ANISOU 1518 CD2 TYR A 197 12077 10235 8758 607 677 2116 ATOM 1519 CE1 TYR A 197 8.616 2.109 -14.831 1.00 82.21 C ANISOU 1519 CE1 TYR A 197 12036 10469 8727 607 683 2214 ATOM 1520 CE2 TYR A 197 8.822 1.861 -12.450 1.00 81.46 C ANISOU 1520 CE2 TYR A 197 12041 10233 8674 542 646 2098 ATOM 1521 CZ TYR A 197 8.076 1.724 -13.613 1.00 81.71 C ANISOU 1521 CZ TYR A 197 12028 10351 8664 541 648 2148 ATOM 1522 OH TYR A 197 6.805 1.196 -13.555 1.00 81.63 O ANISOU 1522 OH TYR A 197 12026 10373 8614 473 614 2134 ATOM 1523 N LEU A 198 15.205 3.599 -14.401 1.00 85.57 N ANISOU 1523 N LEU A 198 12467 10652 9393 883 786 2321 ATOM 1524 CA LEU A 198 16.429 4.212 -14.945 1.00 87.11 C ANISOU 1524 CA LEU A 198 12648 10816 9634 979 819 2363 ATOM 1525 C LEU A 198 16.949 3.427 -16.157 1.00 88.59 C ANISOU 1525 C LEU A 198 12747 11101 9810 995 818 2480 ATOM 1526 O LEU A 198 17.212 4.014 -17.236 1.00 90.00 O ANISOU 1526 O LEU A 198 12883 11316 9996 1085 853 2518 ATOM 1527 CB LEU A 198 17.530 4.313 -13.876 1.00 86.80 C ANISOU 1527 CB LEU A 198 12660 10667 9649 975 814 2345 ATOM 1528 CG LEU A 198 17.362 5.373 -12.789 1.00 86.64 C ANISOU 1528 CG LEU A 198 12724 10536 9658 987 824 2235 ATOM 1529 CD1 LEU A 198 18.222 5.048 -11.572 1.00 86.09 C ANISOU 1529 CD1 LEU A 198 12697 10381 9630 938 804 2225 ATOM 1530 CD2 LEU A 198 17.687 6.758 -13.330 1.00 87.51 C ANISOU 1530 CD2 LEU A 198 12854 10598 9797 1102 868 2204 ATOM 1531 N ASP A 199 17.039 2.091 -16.008 1.00 89.14 N ANISOU 1531 N ASP A 199 12790 11219 9860 908 777 2535 ATOM 1532 CA ASP A 199 17.389 1.145 -17.079 1.00 90.69 C ANISOU 1532 CA ASP A 199 12900 11519 10038 906 765 2647 ATOM 1533 C ASP A 199 16.451 1.239 -18.293 1.00 91.19 C ANISOU 1533 C ASP A 199 12902 11686 10057 921 778 2671 ATOM 1534 O ASP A 199 16.962 1.411 -19.398 1.00 92.17 O ANISOU 1534 O ASP A 199 12955 11878 10185 986 799 2746 ATOM 1535 CB ASP A 199 17.529 -0.339 -16.643 1.00 0.00 C ATOM 1536 CG ASP A 199 18.491 -0.638 -15.483 1.00 0.00 C ATOM 1537 OD1 ASP A 199 19.439 0.148 -15.266 1.00 0.00 O ATOM 1538 OD2 ASP A 199 18.359 -1.746 -14.923 1.00 0.00 O1- ATOM 1539 N ILE A 200 15.124 1.179 -18.077 1.00 90.81 N ANISOU 1539 N ILE A 200 12881 11653 9969 862 765 2609 ATOM 1540 CA ILE A 200 14.083 1.381 -19.099 1.00 90.93 C ANISOU 1540 CA ILE A 200 12846 11764 9939 863 775 2629 ATOM 1541 C ILE A 200 14.281 2.688 -19.880 1.00 91.72 C ANISOU 1541 C ILE A 200 12927 11868 10053 983 833 2623 ATOM 1542 O ILE A 200 14.289 2.648 -21.113 1.00 92.71 O ANISOU 1542 O ILE A 200 12974 12090 10160 1018 851 2692 ATOM 1543 CB ILE A 200 12.619 1.379 -18.537 1.00 0.00 C ATOM 1544 CG1 ILE A 200 12.215 -0.016 -18.040 1.00 0.00 C ATOM 1545 CG2 ILE A 200 11.522 1.900 -19.507 1.00 0.00 C ATOM 1546 CD1 ILE A 200 11.116 0.016 -16.972 1.00 0.00 C ATOM 1547 N PHE A 201 14.463 3.811 -19.162 1.00 92.08 N ANISOU 1547 N PHE A 201 13042 11811 10130 1044 861 2540 ATOM 1548 CA PHE A 201 14.705 5.094 -19.822 1.00 93.22 C ANISOU 1548 CA PHE A 201 13182 11945 10291 1164 918 2522 ATOM 1549 C PHE A 201 15.995 5.047 -20.628 1.00 94.72 C ANISOU 1549 C PHE A 201 13314 12154 10521 1244 938 2607 ATOM 1550 O PHE A 201 15.989 5.394 -21.826 1.00 96.44 O ANISOU 1550 O PHE A 201 13464 12450 10727 1316 973 2655 ATOM 1551 CB PHE A 201 14.766 6.245 -18.803 1.00 92.80 C ANISOU 1551 CB PHE A 201 13224 11766 10266 1204 936 2411 ATOM 1552 CG PHE A 201 13.444 6.535 -18.136 1.00 91.77 C ANISOU 1552 CG PHE A 201 13149 11623 10097 1147 923 2324 ATOM 1553 CD1 PHE A 201 12.350 6.965 -18.895 1.00 91.71 C ANISOU 1553 CD1 PHE A 201 13116 11691 10036 1162 944 2315 ATOM 1554 CD2 PHE A 201 13.291 6.391 -16.757 1.00 90.84 C ANISOU 1554 CD2 PHE A 201 13103 11418 9992 1080 890 2254 ATOM 1555 CE1 PHE A 201 11.132 7.230 -18.292 1.00 91.02 C ANISOU 1555 CE1 PHE A 201 13080 11591 9913 1111 928 2240 ATOM 1556 CE2 PHE A 201 12.072 6.657 -16.154 1.00 90.24 C ANISOU 1556 CE2 PHE A 201 13073 11331 9881 1033 875 2177 ATOM 1557 CZ PHE A 201 10.995 7.089 -16.921 1.00 90.30 C ANISOU 1557 CZ PHE A 201 13060 11411 9837 1049 893 2170 ATOM 1558 N TYR A 202 17.079 4.599 -19.976 1.00103.60 N ANISOU 1558 N TYR A 202 11362 11058 16940 2457 88 153 ATOM 1559 CA TYR A 202 18.383 4.466 -20.649 1.00103.64 C ANISOU 1559 CA TYR A 202 11412 11060 16906 2497 82 147 ATOM 1560 C TYR A 202 18.270 3.720 -21.986 1.00103.93 C ANISOU 1560 C TYR A 202 11428 11105 16954 2530 38 123 ATOM 1561 O TYR A 202 18.775 4.215 -23.014 1.00104.05 O ANISOU 1561 O TYR A 202 11449 11121 16961 2545 27 122 ATOM 1562 CB TYR A 202 19.423 3.773 -19.750 1.00103.94 C ANISOU 1562 CB TYR A 202 11502 11089 16900 2523 101 146 ATOM 1563 CG TYR A 202 20.654 3.308 -20.517 1.00104.28 C ANISOU 1563 CG TYR A 202 11585 11129 16905 2572 87 135 ATOM 1564 CD1 TYR A 202 21.563 4.229 -21.045 1.00104.49 C ANISOU 1564 CD1 TYR A 202 11641 11151 16908 2579 97 145 ATOM 1565 CD2 TYR A 202 20.891 1.949 -20.737 1.00104.53 C ANISOU 1565 CD2 TYR A 202 11625 11165 16926 2611 62 112 ATOM 1566 CE1 TYR A 202 22.675 3.807 -21.763 1.00104.83 C ANISOU 1566 CE1 TYR A 202 11721 11193 16917 2624 84 134 ATOM 1567 CE2 TYR A 202 21.999 1.518 -21.454 1.00104.79 C ANISOU 1567 CE2 TYR A 202 11694 11196 16924 2656 48 101 ATOM 1568 CZ TYR A 202 22.888 2.451 -21.970 1.00105.04 C ANISOU 1568 CZ TYR A 202 11754 11222 16932 2663 59 112 ATOM 1569 OH TYR A 202 23.996 2.040 -22.677 1.00105.83 O ANISOU 1569 OH TYR A 202 11891 11320 16997 2708 45 101 ATOM 1570 N ILE A 203 17.632 2.543 -22.022 1.00104.62 N ANISOU 1570 N ILE A 203 11491 11200 17060 2541 15 105 ATOM 1571 CA ILE A 203 17.565 1.803 -23.280 1.00105.37 C ANISOU 1571 CA ILE A 203 11563 11303 17168 2571 -27 80 ATOM 1572 C ILE A 203 16.654 2.477 -24.338 1.00105.88 C ANISOU 1572 C ILE A 203 11586 11375 17269 2553 -45 81 ATOM 1573 O ILE A 203 17.007 2.440 -25.516 1.00106.11 O ANISOU 1573 O ILE A 203 11617 11406 17290 2577 -67 72 ATOM 1574 CB ILE A 203 17.301 0.282 -23.107 1.00 0.00 C ATOM 1575 CG1 ILE A 203 17.320 -0.494 -24.446 1.00 0.00 C ATOM 1576 CG2 ILE A 203 16.044 -0.036 -22.292 1.00 0.00 C ATOM 1577 CD1 ILE A 203 17.445 -2.017 -24.288 1.00 0.00 C ATOM 1578 N ILE A 204 15.566 3.161 -23.936 1.00106.32 N ANISOU 1578 N ILE A 204 11602 11433 17362 2509 -36 93 ATOM 1579 CA ILE A 204 14.706 3.875 -24.884 1.00106.87 C ANISOU 1579 CA ILE A 204 11626 11508 17469 2488 -53 94 ATOM 1580 C ILE A 204 15.420 5.103 -25.453 1.00107.34 C ANISOU 1580 C ILE A 204 11706 11564 17513 2484 -41 108 ATOM 1581 O ILE A 204 15.399 5.325 -26.674 1.00108.10 O ANISOU 1581 O ILE A 204 11786 11665 17620 2495 -64 100 ATOM 1582 CB ILE A 204 13.339 4.277 -24.266 1.00106.70 C ANISOU 1582 CB ILE A 204 11560 11490 17490 2441 -43 104 ATOM 1583 CG1 ILE A 204 12.515 3.027 -23.914 1.00106.62 C ANISOU 1583 CG1 ILE A 204 11524 11486 17501 2445 -61 87 ATOM 1584 CG2 ILE A 204 12.530 5.128 -25.253 1.00106.58 C ANISOU 1584 CG2 ILE A 204 11502 11480 17511 2418 -57 107 ATOM 1585 CD1 ILE A 204 11.316 3.316 -23.025 1.00106.47 C ANISOU 1585 CD1 ILE A 204 11470 11467 17514 2402 -46 98 ATOM 1586 N ARG A 205 16.069 5.877 -24.586 1.00108.02 N ANISOU 1586 N ARG A 205 11828 11642 17573 2470 -4 130 ATOM 1587 CA ARG A 205 16.805 7.072 -25.042 1.00108.94 C ANISOU 1587 CA ARG A 205 11966 11753 17671 2466 9 145 ATOM 1588 C ARG A 205 17.950 6.695 -26.002 1.00110.00 C ANISOU 1588 C ARG A 205 12133 11886 17773 2513 -8 132 ATOM 1589 O ARG A 205 18.153 7.372 -27.031 1.00109.50 O ANISOU 1589 O ARG A 205 12064 11825 17713 2517 -19 133 ATOM 1590 CB ARG A 205 17.347 7.906 -23.863 1.00108.83 C ANISOU 1590 CB ARG A 205 11987 11729 17633 2444 53 169 ATOM 1591 CG ARG A 205 16.319 8.391 -22.851 1.00108.64 C ANISOU 1591 CG ARG A 205 11935 11704 17637 2397 75 184 ATOM 1592 CD ARG A 205 15.728 9.771 -23.124 1.00108.30 C ANISOU 1592 CD ARG A 205 11865 11663 17620 2359 85 202 ATOM 1593 NE ARG A 205 14.831 10.174 -22.033 1.00107.90 N ANISOU 1593 NE ARG A 205 11793 11612 17592 2317 108 216 ATOM 1594 CZ ARG A 205 13.957 11.185 -22.072 1.00107.70 C ANISOU 1594 CZ ARG A 205 11734 11589 17598 2278 115 229 ATOM 1595 NH1 ARG A 205 13.821 11.945 -23.161 1.00107.82 N ANISOU 1595 NH1 ARG A 205 11730 11606 17627 2273 102 231 ATOM 1596 NH2 ARG A 205 13.202 11.438 -21.005 1.00107.25 N1+ ANISOU 1596 NH2 ARG A 205 11660 11531 17559 2242 136 240 ATOM 1597 N ASN A 206 18.634 5.571 -25.727 1.00111.44 N ANISOU 1597 N ASN A 206 12347 12067 17926 2549 -13 118 ATOM 1598 CA ASN A 206 19.650 5.001 -26.623 1.00112.79 C ANISOU 1598 CA ASN A 206 12548 12238 18067 2596 -33 103 ATOM 1599 C ASN A 206 19.049 4.456 -27.928 1.00112.86 C ANISOU 1599 C ASN A 206 12518 12258 18104 2613 -76 81 ATOM 1600 O ASN A 206 19.601 4.754 -28.985 1.00112.93 O ANISOU 1600 O ASN A 206 12534 12269 18104 2633 -91 76 ATOM 1601 CB ASN A 206 20.503 3.934 -25.898 1.00 0.00 C ATOM 1602 CG ASN A 206 21.689 4.538 -25.141 1.00 0.00 C ATOM 1603 OD1 ASN A 206 21.595 5.603 -24.538 1.00 0.00 O ATOM 1604 ND2 ASN A 206 22.845 3.885 -25.184 1.00 0.00 N ATOM 1605 N LYS A 207 17.925 3.722 -27.878 1.00113.18 N ANISOU 1605 N LYS A 207 12516 12306 18179 2604 -95 68 ATOM 1606 CA LYS A 207 17.204 3.272 -29.078 1.00113.76 C ANISOU 1606 CA LYS A 207 12548 12390 18284 2616 -135 46 ATOM 1607 C LYS A 207 16.731 4.440 -29.963 1.00115.02 C ANISOU 1607 C LYS A 207 12675 12552 18472 2590 -140 55 ATOM 1608 O LYS A 207 16.840 4.366 -31.185 1.00115.17 O ANISOU 1608 O LYS A 207 12683 12578 18498 2610 -167 41 ATOM 1609 CB LYS A 207 16.022 2.353 -28.704 1.00 0.00 C ATOM 1610 CG LYS A 207 16.452 0.923 -28.325 1.00 0.00 C ATOM 1611 CD LYS A 207 15.300 0.043 -27.804 1.00 0.00 C ATOM 1612 CE LYS A 207 14.208 -0.248 -28.852 1.00 0.00 C ATOM 1613 NZ LYS A 207 13.197 -1.190 -28.340 1.00 0.00 N1+ ATOM 1614 N LEU A 208 16.273 5.524 -29.329 1.00116.31 N ANISOU 1614 N LEU A 208 12826 12713 18654 2546 -114 78 ATOM 1615 CA LEU A 208 15.897 6.767 -30.021 1.00116.98 C ANISOU 1615 CA LEU A 208 12887 12799 18760 2520 -112 90 ATOM 1616 C LEU A 208 17.080 7.511 -30.687 1.00118.56 C ANISOU 1616 C LEU A 208 13126 12995 18925 2540 -106 97 ATOM 1617 O LEU A 208 16.849 8.350 -31.555 1.00118.89 O ANISOU 1617 O LEU A 208 13151 13041 18979 2546 -125 91 ATOM 1618 CB LEU A 208 15.162 7.735 -29.079 1.00116.82 C ANISOU 1618 CB LEU A 208 12850 12775 18759 2470 -81 115 ATOM 1619 CG LEU A 208 13.714 7.393 -28.703 1.00116.97 C ANISOU 1619 CG LEU A 208 12820 12800 18823 2440 -88 111 ATOM 1620 CD1 LEU A 208 13.252 8.252 -27.536 1.00116.87 C ANISOU 1620 CD1 LEU A 208 12804 12782 18817 2397 -53 136 ATOM 1621 CD2 LEU A 208 12.784 7.576 -29.898 1.00116.56 C ANISOU 1621 CD2 LEU A 208 12718 12756 18812 2432 -118 101 ATOM 1622 N SER A 209 18.318 7.190 -30.290 1.00 9.10 N ATOM 1623 CA SER A 209 19.539 7.782 -30.834 1.00 28.44 C ATOM 1624 C SER A 209 19.910 7.197 -32.219 1.00 13.75 C ATOM 1625 O SER A 209 20.766 7.758 -32.906 1.00 20.17 O ATOM 1626 CB SER A 209 20.667 7.625 -29.786 1.00 0.00 C ATOM 1627 OG SER A 209 21.730 8.539 -29.981 1.00 0.00 O ATOM 1628 N LEU A 210 19.249 6.109 -32.651 1.00 23.19 N ATOM 1629 CA LEU A 210 19.480 5.398 -33.916 1.00 31.60 C ATOM 1630 C LEU A 210 18.999 6.173 -35.168 1.00 16.40 C ATOM 1631 O LEU A 210 18.333 5.610 -36.038 1.00 21.95 O ATOM 1632 CB LEU A 210 18.853 3.985 -33.830 1.00 0.00 C ATOM 1633 CG LEU A 210 19.456 3.059 -32.748 1.00 0.00 C ATOM 1634 CD1 LEU A 210 18.651 1.746 -32.645 1.00 0.00 C ATOM 1635 CD2 LEU A 210 20.961 2.797 -32.965 1.00 0.00 C ATOM 1636 N ASN A 211 19.364 7.455 -35.271 1.00 25.22 N ATOM 1637 CA ASN A 211 19.102 8.325 -36.422 1.00 20.59 C ATOM 1638 C ASN A 211 19.840 7.821 -37.678 1.00 44.95 C ATOM 1639 O ASN A 211 19.250 7.740 -38.754 1.00 26.41 O ATOM 1640 CB ASN A 211 19.520 9.772 -36.073 1.00 0.00 C ATOM 1641 CG ASN A 211 19.076 10.803 -37.114 1.00 0.00 C ATOM 1642 OD1 ASN A 211 17.960 10.750 -37.618 1.00 0.00 O ATOM 1643 ND2 ASN A 211 19.930 11.768 -37.433 1.00 0.00 N ATOM 1644 N LEU A 212 21.104 7.412 -37.486 1.00 51.33 N ATOM 1645 CA LEU A 212 22.006 6.873 -38.510 1.00 8.59 C ATOM 1646 C LEU A 212 21.470 5.602 -39.202 1.00 21.73 C ATOM 1647 O LEU A 212 21.784 5.361 -40.365 1.00 16.67 O ATOM 1648 CB LEU A 212 23.388 6.641 -37.850 1.00 0.00 C ATOM 1649 CG LEU A 212 24.534 6.187 -38.787 1.00 0.00 C ATOM 1650 CD1 LEU A 212 24.793 7.192 -39.930 1.00 0.00 C ATOM 1651 CD2 LEU A 212 25.814 5.882 -37.981 1.00 0.00 C ATOM 1652 N SER A 213 20.621 4.847 -38.499 1.00 16.15 N ATOM 1653 CA SER A 213 19.926 3.659 -38.996 1.00 7.87 C ATOM 1654 C SER A 213 18.742 4.001 -39.933 1.00 28.97 C ATOM 1655 O SER A 213 18.101 3.078 -40.436 1.00 18.78 O ATOM 1656 CB SER A 213 19.451 2.837 -37.779 1.00 0.00 C ATOM 1657 OG SER A 213 20.550 2.490 -36.944 1.00 0.00 O ATOM 1658 N ASN A 214 18.450 5.295 -40.154 1.00 9.54 N ATOM 1659 CA ASN A 214 17.359 5.843 -40.977 1.00 11.78 C ATOM 1660 C ASN A 214 15.964 5.528 -40.387 1.00 13.81 C ATOM 1661 O ASN A 214 15.040 5.085 -41.068 1.00 23.44 O ATOM 1662 CB ASN A 214 17.594 5.649 -42.513 1.00 0.00 C ATOM 1663 CG ASN A 214 16.848 4.553 -43.291 1.00 0.00 C ATOM 1664 OD1 ASN A 214 16.172 4.844 -44.274 1.00 0.00 O ATOM 1665 ND2 ASN A 214 16.974 3.292 -42.906 1.00 0.00 N ATOM 1666 N SER A 215 15.839 5.779 -39.081 1.00 3.74 N ATOM 1667 CA SER A 215 14.603 5.642 -38.317 1.00 14.07 C ATOM 1668 C SER A 215 13.691 6.855 -38.609 1.00 14.42 C ATOM 1669 O SER A 215 14.160 7.864 -39.139 1.00 11.46 O ATOM 1670 CB SER A 215 14.986 5.627 -36.818 1.00 0.00 C ATOM 1671 OG SER A 215 15.859 6.690 -36.462 1.00 0.00 O ATOM 1672 N LYS A 216 12.407 6.686 -38.273 1.00 31.02 N ATOM 1673 CA LYS A 216 11.348 7.681 -38.398 1.00 32.28 C ATOM 1674 C LYS A 216 10.172 7.226 -37.518 1.00 31.44 C ATOM 1675 O LYS A 216 10.201 7.486 -36.314 1.00 32.07 O ATOM 1676 CB LYS A 216 11.009 8.002 -39.882 1.00 0.00 C ATOM 1677 CG LYS A 216 10.839 6.787 -40.820 1.00 0.00 C ATOM 1678 CD LYS A 216 11.969 6.620 -41.849 1.00 0.00 C ATOM 1679 CE LYS A 216 11.908 5.255 -42.558 1.00 0.00 C ATOM 1680 NZ LYS A 216 12.977 5.106 -43.558 1.00 0.00 N1+ ATOM 1681 N GLU A 217 9.189 6.510 -38.087 1.00 31.02 N ATOM 1682 CA GLU A 217 7.994 6.014 -37.385 1.00 30.54 C ATOM 1683 C GLU A 217 8.311 5.072 -36.204 1.00 30.29 C ATOM 1684 O GLU A 217 7.587 5.082 -35.209 1.00 30.82 O ATOM 1685 CB GLU A 217 6.991 5.387 -38.387 1.00 0.00 C ATOM 1686 CG GLU A 217 7.340 4.008 -39.003 1.00 0.00 C ATOM 1687 CD GLU A 217 8.507 4.039 -39.991 1.00 0.00 C ATOM 1688 OE1 GLU A 217 8.302 4.545 -41.114 1.00 0.00 O ATOM 1689 OE2 GLU A 217 9.604 3.589 -39.601 1.00 0.00 O1- ATOM 1690 N THR A 218 9.425 4.336 -36.293 1.00 27.98 N ATOM 1691 CA THR A 218 10.014 3.561 -35.203 1.00 27.56 C ATOM 1692 C THR A 218 10.306 4.436 -33.964 1.00 27.51 C ATOM 1693 O THR A 218 9.966 4.039 -32.853 1.00 28.08 O ATOM 1694 CB THR A 218 11.356 2.942 -35.681 1.00 0.00 C ATOM 1695 OG1 THR A 218 12.192 3.941 -36.261 1.00 0.00 O ATOM 1696 CG2 THR A 218 11.170 1.837 -36.726 1.00 0.00 C ATOM 1697 N GLY A 219 10.853 5.643 -34.179 1.00120.42 N ANISOU 1697 N GLY A 219 16690 15973 13089 2738 2146 1120 ATOM 1698 CA GLY A 219 11.198 6.583 -33.117 1.00120.27 C ANISOU 1698 CA GLY A 219 16766 15856 13073 2772 2133 984 ATOM 1699 C GLY A 219 9.927 7.170 -32.498 1.00118.90 C ANISOU 1699 C GLY A 219 16617 15679 12880 2629 2107 1002 ATOM 1700 O GLY A 219 9.862 7.337 -31.282 1.00118.94 O ANISOU 1700 O GLY A 219 16722 15509 12959 2567 2069 952 ATOM 1701 N ALA A 220 8.882 7.399 -33.307 1.00118.08 N ANISOU 1701 N ALA A 220 16420 15768 12675 2575 2123 1078 ATOM 1702 CA ALA A 220 7.557 7.778 -32.815 1.00116.30 C ANISOU 1702 CA ALA A 220 16213 15555 12420 2445 2095 1098 ATOM 1703 C ALA A 220 6.950 6.685 -31.917 1.00113.17 C ANISOU 1703 C ALA A 220 15870 15006 12124 2300 2044 1165 ATOM 1704 O ALA A 220 6.434 7.006 -30.849 1.00112.70 O ANISOU 1704 O ALA A 220 15892 14825 12101 2234 2010 1110 ATOM 1705 CB ALA A 220 6.626 8.124 -33.986 1.00 0.00 C ATOM 1706 N PHE A 221 7.089 5.415 -32.325 1.00110.82 N ANISOU 1706 N PHE A 221 15524 14715 11867 2254 2039 1276 ATOM 1707 CA PHE A 221 6.609 4.258 -31.568 1.00108.40 C ANISOU 1707 CA PHE A 221 15258 14276 11650 2121 1989 1341 ATOM 1708 C PHE A 221 7.378 4.073 -30.245 1.00106.38 C ANISOU 1708 C PHE A 221 15115 13796 11506 2131 1964 1259 ATOM 1709 O PHE A 221 6.754 3.863 -29.204 1.00105.66 O ANISOU 1709 O PHE A 221 15085 13589 11470 2026 1920 1256 ATOM 1710 CB PHE A 221 6.656 2.983 -32.432 1.00 0.00 C ATOM 1711 CG PHE A 221 5.524 2.029 -32.096 1.00 0.00 C ATOM 1712 CD1 PHE A 221 4.322 2.079 -32.834 1.00 0.00 C ATOM 1713 CD2 PHE A 221 5.576 1.242 -30.925 1.00 0.00 C ATOM 1714 CE1 PHE A 221 3.230 1.319 -32.437 1.00 0.00 C ATOM 1715 CE2 PHE A 221 4.470 0.497 -30.540 1.00 0.00 C ATOM 1716 CZ PHE A 221 3.304 0.532 -31.294 1.00 0.00 C ATOM 1717 N TYR A 222 8.707 4.233 -30.277 1.00105.36 N ANISOU 1717 N TYR A 222 15012 13609 11409 2255 1988 1194 ATOM 1718 CA TYR A 222 9.561 4.273 -29.083 1.00103.60 C ANISOU 1718 CA TYR A 222 14900 13176 11286 2270 1963 1111 ATOM 1719 C TYR A 222 9.193 5.439 -28.139 1.00102.46 C ANISOU 1719 C TYR A 222 14836 12959 11132 2265 1948 994 ATOM 1720 O TYR A 222 9.351 5.314 -26.926 1.00102.21 O ANISOU 1720 O TYR A 222 14885 12777 11171 2188 1909 963 ATOM 1721 CB TYR A 222 11.044 4.377 -29.494 1.00 0.00 C ATOM 1722 CG TYR A 222 11.657 3.285 -30.366 1.00 0.00 C ATOM 1723 CD1 TYR A 222 11.047 2.021 -30.534 1.00 0.00 C ATOM 1724 CD2 TYR A 222 12.876 3.553 -31.029 1.00 0.00 C ATOM 1725 CE1 TYR A 222 11.633 1.056 -31.376 1.00 0.00 C ATOM 1726 CE2 TYR A 222 13.464 2.588 -31.869 1.00 0.00 C ATOM 1727 CZ TYR A 222 12.837 1.339 -32.049 1.00 0.00 C ATOM 1728 OH TYR A 222 13.390 0.402 -32.871 1.00 0.00 O ATOM 1729 N GLY A 223 8.672 6.541 -28.694 1.00102.07 N ANISOU 1729 N GLY A 223 14764 13024 10993 2349 1977 927 ATOM 1730 CA GLY A 223 8.182 7.703 -27.956 1.00101.59 C ANISOU 1730 CA GLY A 223 14772 12918 10909 2350 1964 815 ATOM 1731 C GLY A 223 6.926 7.357 -27.138 1.00 99.77 C ANISOU 1731 C GLY A 223 14548 12698 10662 2206 1931 853 ATOM 1732 O GLY A 223 6.748 7.892 -26.049 1.00 99.52 O ANISOU 1732 O GLY A 223 14594 12564 10654 2171 1904 772 ATOM 1733 N ARG A 224 6.093 6.418 -27.630 1.00 98.13 N ANISOU 1733 N ARG A 224 14260 12608 10417 2124 1929 975 ATOM 1734 CA ARG A 224 4.942 5.850 -26.912 1.00 96.08 C ANISOU 1734 CA ARG A 224 14009 12339 10158 1982 1887 1024 ATOM 1735 C ARG A 224 5.392 5.019 -25.705 1.00 93.32 C ANISOU 1735 C ARG A 224 13730 11806 9921 1896 1842 1030 ATOM 1736 O ARG A 224 4.831 5.164 -24.614 1.00 92.19 O ANISOU 1736 O ARG A 224 13643 11587 9797 1818 1804 992 ATOM 1737 CB ARG A 224 4.052 4.968 -27.821 1.00 0.00 C ATOM 1738 CG ARG A 224 3.700 5.562 -29.192 1.00 0.00 C ATOM 1739 CD ARG A 224 2.799 4.625 -30.019 1.00 0.00 C ATOM 1740 NE ARG A 224 2.725 5.011 -31.441 1.00 0.00 N ATOM 1741 CZ ARG A 224 2.134 6.082 -32.000 1.00 0.00 C ATOM 1742 NH1 ARG A 224 1.484 7.003 -31.278 1.00 0.00 N ATOM 1743 NH2 ARG A 224 2.200 6.233 -33.326 1.00 0.00 N1+ ATOM 1744 N GLU A 225 6.425 4.187 -25.920 1.00 91.93 N ANISOU 1744 N GLU A 225 13547 11568 9814 1912 1846 1076 ATOM 1745 CA GLU A 225 7.084 3.449 -24.820 1.00 89.49 C ANISOU 1745 CA GLU A 225 13305 11085 9611 1848 1808 1072 ATOM 1746 C GLU A 225 7.660 4.396 -23.759 1.00 88.26 C ANISOU 1746 C GLU A 225 13250 10785 9499 1880 1797 946 ATOM 1747 O GLU A 225 7.510 4.152 -22.546 1.00 87.57 O ANISOU 1747 O GLU A 225 13221 10587 9461 1794 1757 920 ATOM 1748 CB GLU A 225 8.186 2.506 -25.337 1.00 89.08 C ANISOU 1748 CB GLU A 225 13227 11000 9618 1875 1818 1140 ATOM 1749 CG GLU A 225 7.680 1.137 -25.772 1.00 88.87 C ANISOU 1749 CG GLU A 225 13128 11045 9591 1788 1802 1269 ATOM 1750 CD GLU A 225 7.190 0.279 -24.603 1.00 88.68 C ANISOU 1750 CD GLU A 225 13141 10932 9621 1658 1747 1289 ATOM 1751 OE1 GLU A 225 7.816 0.272 -23.521 1.00 89.16 O ANISOU 1751 OE1 GLU A 225 13275 10848 9750 1638 1726 1233 ATOM 1752 OE2 GLU A 225 6.166 -0.409 -24.764 1.00 88.55 O1- ANISOU 1752 OE2 GLU A 225 13077 10990 9574 1575 1722 1363 ATOM 1753 N PHE A 226 8.298 5.481 -24.227 1.00 87.82 N ANISOU 1753 N PHE A 226 13213 10732 9422 2003 1828 865 ATOM 1754 CA PHE A 226 8.831 6.606 -23.444 1.00 87.48 C ANISOU 1754 CA PHE A 226 13265 10559 9412 2041 1815 739 ATOM 1755 C PHE A 226 7.759 7.337 -22.619 1.00 86.60 C ANISOU 1755 C PHE A 226 13184 10465 9255 1983 1795 677 ATOM 1756 O PHE A 226 7.987 7.646 -21.449 1.00 85.62 O ANISOU 1756 O PHE A 226 13136 10211 9182 1932 1762 614 ATOM 1757 CB PHE A 226 9.703 7.497 -24.383 1.00 0.00 C ATOM 1758 CG PHE A 226 9.756 9.021 -24.330 1.00 0.00 C ATOM 1759 CD1 PHE A 226 10.631 9.651 -23.435 1.00 0.00 C ATOM 1760 CD2 PHE A 226 8.965 9.844 -25.169 1.00 0.00 C ATOM 1761 CE1 PHE A 226 10.749 11.029 -23.477 1.00 0.00 C ATOM 1762 CE2 PHE A 226 9.092 11.220 -25.176 1.00 0.00 C ATOM 1763 CZ PHE A 226 10.004 11.818 -24.336 1.00 0.00 C ATOM 1764 N LYS A 227 6.587 7.543 -23.227 1.00 86.61 N ANISOU 1764 N LYS A 227 13121 10628 9157 1989 1815 699 ATOM 1765 CA LYS A 227 5.456 8.278 -22.626 1.00 86.14 C ANISOU 1765 CA LYS A 227 13082 10604 9040 1945 1798 644 ATOM 1766 C LYS A 227 4.810 7.529 -21.470 1.00 84.75 C ANISOU 1766 C LYS A 227 12937 10353 8908 1807 1748 675 ATOM 1767 O LYS A 227 4.523 8.140 -20.444 1.00 84.38 O ANISOU 1767 O LYS A 227 12954 10235 8871 1775 1722 592 ATOM 1768 CB LYS A 227 4.381 8.615 -23.674 1.00 86.26 C ANISOU 1768 CB LYS A 227 13013 10825 8938 1966 1826 687 ATOM 1769 CG LYS A 227 3.359 9.644 -23.217 1.00 86.17 C ANISOU 1769 CG LYS A 227 13021 10863 8853 1952 1817 614 ATOM 1770 CD LYS A 227 2.230 9.773 -24.230 1.00 86.61 C ANISOU 1770 CD LYS A 227 12985 11127 8793 1949 1839 684 ATOM 1771 CE LYS A 227 1.138 10.724 -23.762 1.00 86.77 C ANISOU 1771 CE LYS A 227 13023 11206 8738 1926 1826 624 ATOM 1772 NZ LYS A 227 -0.165 10.449 -24.437 1.00 86.87 N1+ ANISOU 1772 NZ LYS A 227 12953 11394 8658 1864 1825 728 ATOM 1773 N THR A 228 4.588 6.226 -21.652 1.00 84.10 N ANISOU 1773 N THR A 228 12809 10289 8853 1729 1732 788 ATOM 1774 CA THR A 228 3.948 5.362 -20.662 1.00 83.09 C ANISOU 1774 CA THR A 228 12705 10098 8766 1603 1680 818 ATOM 1775 C THR A 228 4.866 5.116 -19.443 1.00 82.15 C ANISOU 1775 C THR A 228 12666 9804 8743 1580 1655 758 ATOM 1776 O THR A 228 4.390 5.219 -18.313 1.00 81.50 O ANISOU 1776 O THR A 228 12636 9651 8678 1519 1620 700 ATOM 1777 CB THR A 228 3.537 4.015 -21.309 1.00 0.00 C ATOM 1778 OG1 THR A 228 4.583 3.502 -22.117 1.00 0.00 O ATOM 1779 CG2 THR A 228 2.321 4.170 -22.235 1.00 0.00 C ATOM 1780 N ALA A 229 6.168 4.900 -19.682 1.00 81.98 N ANISOU 1780 N ALA A 229 12649 9717 8780 1627 1673 775 ATOM 1781 CA ALA A 229 7.224 4.744 -18.669 1.00 81.08 C ANISOU 1781 CA ALA A 229 12606 9442 8758 1608 1652 732 ATOM 1782 C ALA A 229 7.262 5.890 -17.655 1.00 80.80 C ANISOU 1782 C ALA A 229 12652 9319 8730 1613 1636 609 ATOM 1783 O ALA A 229 7.340 5.652 -16.449 1.00 79.72 O ANISOU 1783 O ALA A 229 12562 9082 8644 1536 1600 582 ATOM 1784 CB ALA A 229 8.587 4.597 -19.339 1.00 81.60 C ANISOU 1784 CB ALA A 229 12670 9463 8868 1690 1679 751 ATOM 1785 N LYS A 230 7.196 7.126 -18.154 1.00 81.49 N ANISOU 1785 N LYS A 230 12750 9449 8763 1705 1663 535 ATOM 1786 CA LYS A 230 7.150 8.310 -17.291 1.00 81.55 C ANISOU 1786 CA LYS A 230 12831 9386 8768 1716 1647 412 ATOM 1787 C LYS A 230 5.912 8.315 -16.394 1.00 79.86 C ANISOU 1787 C LYS A 230 12623 9196 8522 1620 1614 398 ATOM 1788 O LYS A 230 6.025 8.591 -15.195 1.00 79.84 O ANISOU 1788 O LYS A 230 12683 9090 8560 1569 1582 332 ATOM 1789 CB LYS A 230 7.199 9.597 -18.121 1.00 83.38 C ANISOU 1789 CB LYS A 230 13061 9683 8934 1840 1682 336 ATOM 1790 CG LYS A 230 8.537 9.855 -18.803 1.00 84.78 C ANISOU 1790 CG LYS A 230 13254 9806 9149 1951 1705 316 ATOM 1791 CD LYS A 230 8.569 11.249 -19.421 1.00 86.43 C ANISOU 1791 CD LYS A 230 13475 10069 9296 2076 1730 214 ATOM 1792 CE LYS A 230 9.802 11.475 -20.284 1.00 87.58 C ANISOU 1792 CE LYS A 230 13624 10183 9469 2202 1752 198 ATOM 1793 NZ LYS A 230 9.671 12.690 -21.139 1.00 88.66 N1+ ANISOU 1793 NZ LYS A 230 13745 10419 9524 2335 1782 113 ATOM 1794 N SER A 231 4.748 7.999 -16.969 1.00 78.29 N ANISOU 1794 N SER A 231 12358 9133 8253 1593 1618 462 ATOM 1795 CA SER A 231 3.488 7.928 -16.209 1.00 76.54 C ANISOU 1795 CA SER A 231 12138 8943 8000 1502 1581 460 ATOM 1796 C SER A 231 3.587 6.881 -15.099 1.00 74.15 C ANISOU 1796 C SER A 231 11857 8542 7772 1399 1536 488 ATOM 1797 O SER A 231 3.261 7.156 -13.940 1.00 73.19 O ANISOU 1797 O SER A 231 11783 8360 7666 1343 1502 426 ATOM 1798 CB SER A 231 2.300 7.578 -17.120 1.00 76.46 C ANISOU 1798 CB SER A 231 12050 9090 7910 1485 1588 547 ATOM 1799 OG SER A 231 2.276 8.386 -18.276 1.00 77.22 O ANISOU 1799 OG SER A 231 12108 9298 7931 1581 1634 538 ATOM 1800 N LEU A 232 4.058 5.693 -15.467 1.00 72.42 N ANISOU 1800 N LEU A 232 11602 8316 7597 1376 1537 580 ATOM 1801 CA LEU A 232 4.228 4.604 -14.503 1.00 71.04 C ANISOU 1801 CA LEU A 232 11439 8062 7490 1285 1497 611 ATOM 1802 C LEU A 232 5.288 4.922 -13.443 1.00 70.57 C ANISOU 1802 C LEU A 232 11450 7862 7500 1277 1486 536 ATOM 1803 O LEU A 232 5.136 4.522 -12.286 1.00 70.15 O ANISOU 1803 O LEU A 232 11420 7750 7482 1197 1447 517 ATOM 1804 CB LEU A 232 4.568 3.291 -15.215 1.00 70.66 C ANISOU 1804 CB LEU A 232 11334 8044 7470 1271 1502 723 ATOM 1805 CG LEU A 232 3.467 2.747 -16.133 1.00 70.49 C ANISOU 1805 CG LEU A 232 11240 8152 7388 1252 1499 812 ATOM 1806 CD1 LEU A 232 4.035 1.628 -16.992 1.00 70.51 C ANISOU 1806 CD1 LEU A 232 11188 8181 7418 1258 1512 913 ATOM 1807 CD2 LEU A 232 2.246 2.287 -15.344 1.00 69.62 C ANISOU 1807 CD2 LEU A 232 11129 8057 7266 1158 1443 821 ATOM 1808 N PHE A 233 6.346 5.656 -13.810 1.00 70.30 N ANISOU 1808 N PHE A 233 11447 7776 7486 1360 1517 494 ATOM 1809 CA PHE A 233 7.384 6.090 -12.876 1.00 69.70 C ANISOU 1809 CA PHE A 233 11445 7563 7474 1355 1504 420 ATOM 1810 C PHE A 233 6.885 7.208 -11.934 1.00 69.20 C ANISOU 1810 C PHE A 233 11432 7471 7388 1328 1479 317 ATOM 1811 O PHE A 233 7.221 7.192 -10.750 1.00 68.61 O ANISOU 1811 O PHE A 233 11395 7315 7356 1253 1445 284 ATOM 1812 CB PHE A 233 8.654 6.474 -13.662 1.00 0.00 C ATOM 1813 CG PHE A 233 9.904 6.749 -12.843 1.00 0.00 C ATOM 1814 CD1 PHE A 233 10.351 5.813 -11.885 1.00 0.00 C ATOM 1815 CD2 PHE A 233 10.712 7.869 -13.130 1.00 0.00 C ATOM 1816 CE1 PHE A 233 11.562 6.002 -11.235 1.00 0.00 C ATOM 1817 CE2 PHE A 233 11.921 8.040 -12.468 1.00 0.00 C ATOM 1818 CZ PHE A 233 12.345 7.109 -11.528 1.00 0.00 C ATOM 1819 N LEU A 234 6.034 8.121 -12.433 1.00 69.16 N ANISOU 1819 N LEU A 234 11423 7544 7310 1385 1497 268 ATOM 1820 CA LEU A 234 5.320 9.115 -11.607 1.00 68.99 C ANISOU 1820 CA LEU A 234 11443 7516 7254 1364 1475 171 ATOM 1821 C LEU A 234 4.451 8.465 -10.529 1.00 68.03 C ANISOU 1821 C LEU A 234 11314 7396 7136 1254 1431 186 ATOM 1822 O LEU A 234 4.408 8.937 -9.392 1.00 68.02 O ANISOU 1822 O LEU A 234 11361 7328 7152 1209 1401 110 ATOM 1823 CB LEU A 234 4.447 10.028 -12.480 1.00 69.35 C ANISOU 1823 CB LEU A 234 11461 7682 7203 1434 1501 144 ATOM 1824 CG LEU A 234 3.573 11.064 -11.773 1.00 69.30 C ANISOU 1824 CG LEU A 234 11488 7693 7147 1419 1481 50 ATOM 1825 CD1 LEU A 234 4.439 11.987 -10.931 1.00 69.81 C ANISOU 1825 CD1 LEU A 234 11634 7629 7258 1435 1467 -61 ATOM 1826 CD2 LEU A 234 2.755 11.843 -12.788 1.00 69.90 C ANISOU 1826 CD2 LEU A 234 11526 7908 7122 1490 1511 40 ATOM 1827 N VAL A 235 3.754 7.366 -10.876 1.00 67.22 N ANISOU 1827 N VAL A 235 11152 7371 7018 1212 1423 280 ATOM 1828 CA VAL A 235 2.948 6.648 -9.883 1.00 66.41 C ANISOU 1828 CA VAL A 235 11038 7268 6925 1113 1376 300 ATOM 1829 C VAL A 235 3.838 5.979 -8.813 1.00 66.08 C ANISOU 1829 C VAL A 235 11028 7114 6963 1054 1351 285 ATOM 1830 O VAL A 235 3.452 5.986 -7.644 1.00 66.34 O ANISOU 1830 O VAL A 235 11086 7114 7005 991 1314 234 ATOM 1831 CB VAL A 235 1.881 5.656 -10.447 1.00 0.00 C ATOM 1832 CG1 VAL A 235 1.093 6.250 -11.625 1.00 0.00 C ATOM 1833 CG2 VAL A 235 2.299 4.210 -10.772 1.00 0.00 C ATOM 1834 N LEU A 236 5.051 5.521 -9.185 1.00 65.68 N ANISOU 1834 N LEU A 236 10975 7012 6966 1075 1372 330 ATOM 1835 CA LEU A 236 6.022 5.027 -8.194 1.00 65.10 C ANISOU 1835 CA LEU A 236 10931 6838 6966 1019 1352 324 ATOM 1836 C LEU A 236 6.508 6.157 -7.286 1.00 65.02 C ANISOU 1836 C LEU A 236 10991 6737 6976 1016 1341 220 ATOM 1837 O LEU A 236 6.532 6.010 -6.054 1.00 64.84 O ANISOU 1837 O LEU A 236 10989 6667 6980 940 1307 186 ATOM 1838 CB LEU A 236 7.213 4.344 -8.878 1.00 65.54 C ANISOU 1838 CB LEU A 236 10972 6859 7072 1050 1377 396 ATOM 1839 CG LEU A 236 8.297 3.732 -7.981 1.00 65.48 C ANISOU 1839 CG LEU A 236 10985 6756 7136 992 1358 408 ATOM 1840 CD1 LEU A 236 7.713 2.659 -7.071 1.00 64.63 C ANISOU 1840 CD1 LEU A 236 10843 6677 7034 898 1320 436 ATOM 1841 CD2 LEU A 236 9.441 3.168 -8.825 1.00 65.83 C ANISOU 1841 CD2 LEU A 236 11015 6773 7222 1037 1386 482 ATOM 1842 N PHE A 237 6.884 7.280 -7.900 1.00 65.16 N ANISOU 1842 N PHE A 237 11043 6734 6979 1099 1369 167 ATOM 1843 CA PHE A 237 7.299 8.468 -7.152 1.00 65.45 C ANISOU 1843 CA PHE A 237 11152 6685 7031 1105 1355 61 ATOM 1844 C PHE A 237 6.215 8.896 -6.166 1.00 64.91 C ANISOU 1844 C PHE A 237 11093 6645 6925 1046 1323 -3 ATOM 1845 O PHE A 237 6.500 9.123 -4.987 1.00 65.18 O ANISOU 1845 O PHE A 237 11165 6606 6992 984 1292 -56 ATOM 1846 CB PHE A 237 7.635 9.627 -8.095 1.00 66.55 C ANISOU 1846 CB PHE A 237 11319 6820 7145 1217 1387 8 ATOM 1847 CG PHE A 237 8.027 10.891 -7.382 1.00 67.63 C ANISOU 1847 CG PHE A 237 11531 6866 7296 1228 1368 -106 ATOM 1848 CD1 PHE A 237 9.289 11.018 -6.816 1.00 68.35 C ANISOU 1848 CD1 PHE A 237 11680 6822 7466 1210 1350 -127 ATOM 1849 CD2 PHE A 237 7.135 11.949 -7.266 1.00 68.28 C ANISOU 1849 CD2 PHE A 237 11630 6998 7316 1252 1365 -191 ATOM 1850 CE1 PHE A 237 9.657 12.181 -6.153 1.00 69.16 C ANISOU 1850 CE1 PHE A 237 11856 6835 7587 1215 1326 -233 ATOM 1851 CE2 PHE A 237 7.495 13.112 -6.600 1.00 69.08 C ANISOU 1851 CE2 PHE A 237 11801 7014 7431 1261 1343 -302 ATOM 1852 CZ PHE A 237 8.757 13.229 -6.042 1.00 69.39 C ANISOU 1852 CZ PHE A 237 11900 6913 7552 1241 1323 -323 ATOM 1853 N LEU A 238 4.974 8.988 -6.651 1.00 64.07 N ANISOU 1853 N LEU A 238 10947 6648 6745 1062 1328 6 ATOM 1854 CA LEU A 238 3.834 9.361 -5.804 1.00 63.13 C ANISOU 1854 CA LEU A 238 10833 6567 6583 1012 1295 -48 ATOM 1855 C LEU A 238 3.591 8.346 -4.688 1.00 61.59 C ANISOU 1855 C LEU A 238 10621 6358 6421 912 1253 -22 ATOM 1856 O LEU A 238 3.332 8.735 -3.548 1.00 61.51 O ANISOU 1856 O LEU A 238 10638 6318 6413 859 1220 -91 ATOM 1857 CB LEU A 238 2.567 9.563 -6.644 1.00 63.07 C ANISOU 1857 CB LEU A 238 10784 6685 6492 1048 1306 -25 ATOM 1858 CG LEU A 238 2.581 10.825 -7.524 1.00 63.98 C ANISOU 1858 CG LEU A 238 10917 6835 6555 1145 1342 -80 ATOM 1859 CD1 LEU A 238 1.551 10.721 -8.641 1.00 63.96 C ANISOU 1859 CD1 LEU A 238 10856 6971 6475 1182 1362 -18 ATOM 1860 CD2 LEU A 238 2.352 12.084 -6.700 1.00 64.41 C ANISOU 1860 CD2 LEU A 238 11027 6856 6588 1145 1323 -199 ATOM 1861 N PHE A 239 3.696 7.057 -5.009 1.00 60.24 N ANISOU 1861 N PHE A 239 10403 6211 6274 888 1253 71 ATOM 1862 CA PHE A 239 3.574 5.992 -4.007 1.00 58.97 C ANISOU 1862 CA PHE A 239 10219 6040 6144 801 1214 96 ATOM 1863 C PHE A 239 4.627 6.151 -2.916 1.00 58.64 C ANISOU 1863 C PHE A 239 10218 5901 6161 754 1201 50 ATOM 1864 O PHE A 239 4.292 6.202 -1.724 1.00 58.10 O ANISOU 1864 O PHE A 239 10158 5823 6093 689 1164 0 ATOM 1865 CB PHE A 239 3.708 4.614 -4.660 1.00 58.51 C ANISOU 1865 CB PHE A 239 10106 6019 6106 794 1219 203 ATOM 1866 CG PHE A 239 3.493 3.470 -3.710 1.00 57.94 C ANISOU 1866 CG PHE A 239 10004 5953 6057 715 1176 226 ATOM 1867 CD1 PHE A 239 2.217 2.966 -3.489 1.00 57.52 C ANISOU 1867 CD1 PHE A 239 9918 5968 5967 684 1137 236 ATOM 1868 CD2 PHE A 239 4.565 2.897 -3.029 1.00 57.93 C ANISOU 1868 CD2 PHE A 239 10007 5890 6113 672 1171 237 ATOM 1869 CE1 PHE A 239 2.015 1.913 -2.610 1.00 56.95 C ANISOU 1869 CE1 PHE A 239 9817 5904 5915 621 1093 248 ATOM 1870 CE2 PHE A 239 4.368 1.847 -2.145 1.00 57.27 C ANISOU 1870 CE2 PHE A 239 9890 5826 6044 603 1132 252 ATOM 1871 CZ PHE A 239 3.094 1.355 -1.934 1.00 56.68 C ANISOU 1871 CZ PHE A 239 9782 5820 5933 582 1093 253 ATOM 1872 N ALA A 240 5.892 6.242 -3.337 1.00 58.77 N ANISOU 1872 N ALA A 240 10258 5847 6224 785 1228 70 ATOM 1873 CA ALA A 240 7.025 6.401 -2.406 1.00 58.65 C ANISOU 1873 CA ALA A 240 10284 5730 6268 739 1215 40 ATOM 1874 C ALA A 240 6.893 7.659 -1.553 1.00 58.83 C ANISOU 1874 C ALA A 240 10363 5707 6282 722 1195 -67 ATOM 1875 O ALA A 240 7.089 7.618 -0.328 1.00 58.24 O ANISOU 1875 O ALA A 240 10301 5595 6230 644 1163 -101 ATOM 1876 CB ALA A 240 8.341 6.422 -3.169 1.00 59.02 C ANISOU 1876 CB ALA A 240 10353 5706 6363 789 1245 80 ATOM 1877 N LEU A 241 6.538 8.764 -2.210 1.00 59.33 N ANISOU 1877 N LEU A 241 10455 5781 6306 797 1214 -121 ATOM 1878 CA LEU A 241 6.378 10.051 -1.539 1.00 60.09 C ANISOU 1878 CA LEU A 241 10605 5837 6387 794 1196 -230 ATOM 1879 C LEU A 241 5.215 10.020 -0.543 1.00 59.46 C ANISOU 1879 C LEU A 241 10506 5817 6267 728 1160 -270 ATOM 1880 O LEU A 241 5.341 10.545 0.567 1.00 59.83 O ANISOU 1880 O LEU A 241 10587 5817 6328 673 1131 -339 ATOM 1881 CB LEU A 241 6.178 11.178 -2.562 1.00 61.13 C ANISOU 1881 CB LEU A 241 10763 5986 6476 897 1225 -278 ATOM 1882 CG LEU A 241 6.407 12.615 -2.084 1.00 62.33 C ANISOU 1882 CG LEU A 241 10984 6071 6626 916 1211 -395 ATOM 1883 CD1 LEU A 241 7.889 12.879 -1.831 1.00 63.17 C ANISOU 1883 CD1 LEU A 241 11148 6041 6811 912 1202 -410 ATOM 1884 CD2 LEU A 241 5.857 13.602 -3.103 1.00 63.04 C ANISOU 1884 CD2 LEU A 241 11079 6221 6650 1019 1238 -441 ATOM 1885 N SER A 242 4.102 9.397 -0.938 1.00 58.58 N ANISOU 1885 N SER A 242 10342 5807 6108 733 1160 -225 ATOM 1886 CA SER A 242 2.955 9.202 -0.041 1.00 57.68 C ANISOU 1886 CA SER A 242 10204 5752 5957 675 1120 -253 ATOM 1887 C SER A 242 3.287 8.292 1.146 1.00 56.78 C ANISOU 1887 C SER A 242 10072 5615 5886 585 1086 -239 ATOM 1888 O SER A 242 2.904 8.589 2.284 1.00 56.48 O ANISOU 1888 O SER A 242 10042 5578 5839 530 1051 -303 ATOM 1889 CB SER A 242 1.760 8.617 -0.812 1.00 57.29 C ANISOU 1889 CB SER A 242 10104 5807 5855 700 1120 -193 ATOM 1890 OG SER A 242 1.326 9.490 -1.850 1.00 57.89 O ANISOU 1890 OG SER A 242 10189 5926 5879 777 1149 -206 ATOM 1891 N TRP A 243 4.022 7.188 0.943 1.00 56.17 N ANISOU 1891 N TRP A 243 9964 5524 5851 571 1097 -158 ATOM 1892 CA TRP A 243 4.183 6.143 1.962 1.00 55.12 C ANISOU 1892 CA TRP A 243 9799 5395 5749 490 1067 -133 ATOM 1893 C TRP A 243 5.484 6.226 2.786 1.00 55.16 C ANISOU 1893 C TRP A 243 9832 5317 5807 431 1060 -156 ATOM 1894 O TRP A 243 5.527 5.663 3.886 1.00 54.67 O ANISOU 1894 O TRP A 243 9748 5271 5749 357 1027 -175 ATOM 1895 CB TRP A 243 4.069 4.765 1.278 1.00 54.47 C ANISOU 1895 CB TRP A 243 9660 5355 5678 496 1074 -33 ATOM 1896 CG TRP A 243 2.650 4.369 0.989 1.00 53.89 C ANISOU 1896 CG TRP A 243 9545 5372 5558 503 1049 -15 ATOM 1897 CD1 TRP A 243 1.999 4.492 -0.191 1.00 53.73 C ANISOU 1897 CD1 TRP A 243 9507 5402 5505 559 1065 31 ATOM 1898 CD2 TRP A 243 1.681 3.794 1.915 1.00 53.30 C ANISOU 1898 CD2 TRP A 243 9441 5345 5463 450 999 -44 ATOM 1899 NE1 TRP A 243 0.695 4.068 -0.054 1.00 53.10 N ANISOU 1899 NE1 TRP A 243 9393 5391 5390 540 1024 38 ATOM 1900 CE2 TRP A 243 0.443 3.614 1.223 1.00 52.97 C ANISOU 1900 CE2 TRP A 243 9370 5372 5381 478 982 -11 ATOM 1901 CE3 TRP A 243 1.727 3.399 3.273 1.00 53.27 C ANISOU 1901 CE3 TRP A 243 9431 5337 5471 382 965 -95 ATOM 1902 CZ2 TRP A 243 -0.688 3.065 1.846 1.00 52.78 C ANISOU 1902 CZ2 TRP A 243 9317 5402 5333 445 927 -29 ATOM 1903 CZ3 TRP A 243 0.602 2.835 3.905 1.00 52.98 C ANISOU 1903 CZ3 TRP A 243 9360 5365 5406 354 915 -117 ATOM 1904 CH2 TRP A 243 -0.600 2.670 3.193 1.00 52.72 C ANISOU 1904 CH2 TRP A 243 9303 5389 5337 388 895 -86 ATOM 1905 N LEU A 244 6.544 6.920 2.331 1.00 55.64 N ANISOU 1905 N LEU A 244 9940 5293 5905 463 1086 -154 ATOM 1906 CA LEU A 244 7.797 7.020 3.126 1.00 55.97 C ANISOU 1906 CA LEU A 244 10013 5247 6005 403 1076 -159 ATOM 1907 C LEU A 244 7.696 7.727 4.494 1.00 55.90 C ANISOU 1907 C LEU A 244 10029 5216 5994 329 1039 -244 ATOM 1908 O LEU A 244 8.328 7.275 5.464 1.00 55.99 O ANISOU 1908 O LEU A 244 10028 5208 6035 246 1018 -230 ATOM 1909 CB LEU A 244 8.941 7.625 2.297 1.00 56.94 C ANISOU 1909 CB LEU A 244 10190 5273 6171 460 1103 -146 ATOM 1910 CG LEU A 244 9.620 6.650 1.322 1.00 56.95 C ANISOU 1910 CG LEU A 244 10162 5274 6200 496 1132 -43 ATOM 1911 CD1 LEU A 244 10.481 7.402 0.311 1.00 57.80 C ANISOU 1911 CD1 LEU A 244 10323 5301 6337 580 1159 -43 ATOM 1912 CD2 LEU A 244 10.442 5.594 2.059 1.00 56.74 C ANISOU 1912 CD2 LEU A 244 10106 5234 6217 412 1117 19 ATOM 1913 N PRO A 245 6.920 8.828 4.582 1.00 55.98 N ANISOU 1913 N PRO A 245 10071 5233 5964 357 1031 -330 ATOM 1914 CA PRO A 245 6.726 9.505 5.874 1.00 56.37 C ANISOU 1914 CA PRO A 245 10140 5271 6006 287 994 -413 ATOM 1915 C PRO A 245 6.255 8.593 7.027 1.00 55.74 C ANISOU 1915 C PRO A 245 10000 5265 5913 203 961 -406 ATOM 1916 O PRO A 245 6.893 8.568 8.091 1.00 55.74 O ANISOU 1916 O PRO A 245 10001 5237 5940 119 938 -420 ATOM 1917 CB PRO A 245 5.673 10.570 5.546 1.00 56.52 C ANISOU 1917 CB PRO A 245 10184 5321 5969 347 994 -491 ATOM 1918 CG PRO A 245 5.940 10.911 4.125 1.00 56.72 C ANISOU 1918 CG PRO A 245 10234 5321 5995 445 1035 -465 ATOM 1919 CD PRO A 245 6.354 9.623 3.471 1.00 56.16 C ANISOU 1919 CD PRO A 245 10118 5270 5950 454 1057 -356 ATOM 1920 N LEU A 246 5.228 7.779 6.733 1.00 55.07 N ANISOU 1920 N LEU A 246 9862 5276 5786 225 956 -382 ATOM 1921 CA LEU A 246 4.629 6.774 7.603 1.00 54.53 C ANISOU 1921 CA LEU A 246 9733 5287 5699 161 921 -380 ATOM 1922 C LEU A 246 5.649 5.686 8.002 1.00 54.45 C ANISOU 1922 C LEU A 246 9685 5271 5731 101 921 -314 ATOM 1923 O LEU A 246 5.605 5.157 9.110 1.00 54.04 O ANISOU 1923 O LEU A 246 9596 5263 5674 28 891 -332 ATOM 1924 CB LEU A 246 3.407 6.155 6.883 1.00 53.77 C ANISOU 1924 CB LEU A 246 9592 5279 5556 206 912 -359 ATOM 1925 CG LEU A 246 2.402 5.450 7.825 1.00 53.22 C ANISOU 1925 CG LEU A 246 9466 5295 5458 160 865 -380 ATOM 1926 CD1 LEU A 246 1.531 6.455 8.598 1.00 53.47 C ANISOU 1926 CD1 LEU A 246 9514 5343 5457 129 833 -478 ATOM 1927 CD2 LEU A 246 1.507 4.483 7.040 1.00 52.68 C ANISOU 1927 CD2 LEU A 246 9361 5294 5360 209 854 -337 ATOM 1928 N SER A 247 6.612 5.394 7.122 1.00 54.55 N ANISOU 1928 N SER A 247 9706 5239 5781 133 954 -237 ATOM 1929 CA SER A 247 7.700 4.459 7.392 1.00 54.64 C ANISOU 1929 CA SER A 247 9691 5234 5834 78 957 -170 ATOM 1930 C SER A 247 8.773 5.139 8.277 1.00 55.48 C ANISOU 1930 C SER A 247 9839 5261 5978 8 947 -197 ATOM 1931 O SER A 247 9.251 4.520 9.230 1.00 55.46 O ANISOU 1931 O SER A 247 9801 5289 5982 -77 924 -189 ATOM 1932 CB SER A 247 8.326 3.990 6.059 1.00 0.00 C ATOM 1933 OG SER A 247 7.391 3.300 5.231 1.00 0.00 O ATOM 1934 N ILE A 248 9.109 6.419 8.018 1.00 56.35 N ANISOU 1934 N ILE A 248 10023 5275 6111 42 958 -231 ATOM 1935 CA ILE A 248 10.069 7.212 8.807 1.00 57.57 C ANISOU 1935 CA ILE A 248 10227 5341 6305 -25 939 -263 ATOM 1936 C ILE A 248 9.554 7.380 10.249 1.00 58.05 C ANISOU 1936 C ILE A 248 10260 5458 6336 -112 901 -327 ATOM 1937 O ILE A 248 10.314 7.194 11.215 1.00 58.19 O ANISOU 1937 O ILE A 248 10267 5464 6378 -208 880 -312 ATOM 1938 CB ILE A 248 10.376 8.583 8.153 1.00 58.15 C ANISOU 1938 CB ILE A 248 10387 5307 6398 36 949 -315 ATOM 1939 CG1 ILE A 248 11.179 8.383 6.856 1.00 58.20 C ANISOU 1939 CG1 ILE A 248 10419 5250 6443 112 983 -246 ATOM 1940 CG2 ILE A 248 11.164 9.490 9.103 1.00 59.00 C ANISOU 1940 CG2 ILE A 248 10549 5324 6542 -41 916 -364 ATOM 1941 CD1 ILE A 248 11.127 9.567 5.909 1.00 58.89 C ANISOU 1941 CD1 ILE A 248 10573 5272 6530 209 999 -301 ATOM 1942 N ILE A 249 8.251 7.711 10.417 1.00 58.26 N ANISOU 1942 N ILE A 249 10273 5553 6309 -81 890 -394 ATOM 1943 CA ILE A 249 7.614 7.793 11.738 1.00 58.69 C ANISOU 1943 CA ILE A 249 10292 5680 6327 -151 852 -458 ATOM 1944 C ILE A 249 7.721 6.453 12.485 1.00 58.89 C ANISOU 1944 C ILE A 249 10235 5797 6344 -218 837 -411 ATOM 1945 O ILE A 249 8.074 6.448 13.656 1.00 59.18 O ANISOU 1945 O ILE A 249 10245 5863 6374 -306 809 -440 ATOM 1946 CB ILE A 249 6.185 8.416 11.798 1.00 0.00 C ATOM 1947 CG1 ILE A 249 5.022 7.484 11.409 1.00 0.00 C ATOM 1948 CG2 ILE A 249 6.108 9.789 11.104 1.00 0.00 C ATOM 1949 CD1 ILE A 249 3.622 8.066 11.660 1.00 0.00 C ATOM 1950 N ASN A 250 7.532 5.309 11.812 1.00 58.85 N ANISOU 1950 N ASN A 250 10185 5841 6335 -176 854 -341 ATOM 1951 CA ASN A 250 7.660 3.998 12.475 1.00 58.95 C ANISOU 1951 CA ASN A 250 10117 5943 6338 -229 840 -297 ATOM 1952 C ASN A 250 9.090 3.696 12.903 1.00 59.72 C ANISOU 1952 C ASN A 250 10210 6001 6478 -308 845 -237 ATOM 1953 O ASN A 250 9.309 3.106 13.967 1.00 59.17 O ANISOU 1953 O ASN A 250 10082 6004 6394 -387 824 -232 ATOM 1954 CB ASN A 250 7.147 2.861 11.581 1.00 58.54 C ANISOU 1954 CB ASN A 250 10022 5947 6272 -162 853 -239 ATOM 1955 CG ASN A 250 5.638 2.870 11.428 1.00 57.97 C ANISOU 1955 CG ASN A 250 9933 5939 6151 -105 833 -290 ATOM 1956 OD1 ASN A 250 4.942 3.692 12.024 1.00 57.99 O ANISOU 1956 OD1 ASN A 250 9952 5953 6126 -114 810 -370 ATOM 1957 ND2 ASN A 250 5.126 1.950 10.621 1.00 57.48 N ANISOU 1957 ND2 ASN A 250 9840 5919 6080 -49 837 -241 ATOM 1958 N CYS A 251 10.051 4.091 12.068 1.00 61.25 N ANISOU 1958 N CYS A 251 10464 6086 6722 -284 872 -189 ATOM 1959 CA CYS A 251 11.477 3.955 12.395 1.00 62.65 C ANISOU 1959 CA CYS A 251 10652 6204 6947 -359 873 -127 ATOM 1960 C CYS A 251 11.871 4.837 13.574 1.00 64.03 C ANISOU 1960 C CYS A 251 10852 6345 7130 -455 842 -179 ATOM 1961 O CYS A 251 12.478 4.347 14.540 1.00 64.04 O ANISOU 1961 O CYS A 251 10808 6389 7132 -553 824 -147 ATOM 1962 CB CYS A 251 12.353 4.269 11.179 1.00 62.95 C ANISOU 1962 CB CYS A 251 10755 6124 7038 -299 903 -72 ATOM 1963 SG CYS A 251 12.195 3.062 9.847 1.00 62.50 S ANISOU 1963 SG CYS A 251 10658 6109 6977 -208 939 12 ATOM 1964 N ILE A 252 11.514 6.123 13.513 1.00 65.62 N ANISOU 1964 N ILE A 252 11120 6478 7334 -429 833 -258 ATOM 1965 CA ILE A 252 11.868 7.036 14.614 1.00 67.75 C ANISOU 1965 CA ILE A 252 11418 6709 7613 -522 799 -313 ATOM 1966 C ILE A 252 11.170 6.686 15.937 1.00 67.90 C ANISOU 1966 C ILE A 252 11361 6858 7579 -596 770 -358 ATOM 1967 O ILE A 252 11.768 6.867 16.987 1.00 69.10 O ANISOU 1967 O ILE A 252 11501 7013 7739 -703 744 -359 ATOM 1968 CB ILE A 252 11.716 8.550 14.268 1.00 68.89 C ANISOU 1968 CB ILE A 252 11656 6745 7773 -478 792 -394 ATOM 1969 CG1 ILE A 252 10.249 8.954 14.088 1.00 68.46 C ANISOU 1969 CG1 ILE A 252 11594 6757 7661 -405 794 -478 ATOM 1970 CG2 ILE A 252 12.585 8.913 13.058 1.00 69.52 C ANISOU 1970 CG2 ILE A 252 11809 6694 7909 -410 816 -351 ATOM 1971 CD1 ILE A 252 10.064 10.308 13.430 1.00 69.12 C ANISOU 1971 CD1 ILE A 252 11762 6746 7752 -334 798 -548 ATOM 1972 N ILE A 253 9.926 6.192 15.877 1.00 67.46 N ANISOU 1972 N ILE A 253 11252 6910 7470 -541 771 -391 ATOM 1973 CA ILE A 253 9.157 5.719 17.023 1.00 67.62 C ANISOU 1973 CA ILE A 253 11190 7063 7436 -600 741 -432 ATOM 1974 C ILE A 253 9.813 4.461 17.607 1.00 67.70 C ANISOU 1974 C ILE A 253 11121 7155 7444 -671 739 -358 ATOM 1975 O ILE A 253 9.928 4.359 18.826 1.00 68.08 O ANISOU 1975 O ILE A 253 11118 7278 7470 -764 713 -376 ATOM 1976 CB ILE A 253 7.666 5.530 16.619 1.00 0.00 C ATOM 1977 CG1 ILE A 253 7.055 6.927 16.379 1.00 0.00 C ATOM 1978 CG2 ILE A 253 6.824 4.770 17.663 1.00 0.00 C ATOM 1979 CD1 ILE A 253 5.727 6.975 15.626 1.00 0.00 C ATOM 1980 N TYR A 254 10.310 3.547 16.764 1.00 67.38 N ANISOU 1980 N TYR A 254 11067 7109 7423 -626 767 -275 ATOM 1981 CA TYR A 254 11.057 2.379 17.208 1.00 67.07 C ANISOU 1981 CA TYR A 254 10955 7144 7382 -686 769 -196 ATOM 1982 C TYR A 254 12.423 2.751 17.828 1.00 68.38 C ANISOU 1982 C TYR A 254 11143 7250 7587 -796 762 -148 ATOM 1983 O TYR A 254 12.656 2.461 19.000 1.00 68.66 O ANISOU 1983 O TYR A 254 11115 7376 7597 -894 741 -143 ATOM 1984 CB TYR A 254 11.183 1.355 16.061 1.00 0.00 C ATOM 1985 CG TYR A 254 11.879 0.083 16.505 1.00 0.00 C ATOM 1986 CD1 TYR A 254 11.199 -0.965 17.157 1.00 0.00 C ATOM 1987 CD2 TYR A 254 13.271 0.030 16.399 1.00 0.00 C ATOM 1988 CE1 TYR A 254 11.916 -2.049 17.698 1.00 0.00 C ATOM 1989 CE2 TYR A 254 13.996 -1.001 17.006 1.00 0.00 C ATOM 1990 CZ TYR A 254 13.322 -2.070 17.620 1.00 0.00 C ATOM 1991 OH TYR A 254 14.038 -3.115 18.128 1.00 0.00 O ATOM 1992 N PHE A 255 13.307 3.370 17.033 1.00 69.71 N ANISOU 1992 N PHE A 255 11400 7271 7816 -780 777 -112 ATOM 1993 CA PHE A 255 14.687 3.673 17.439 1.00 71.75 C ANISOU 1993 CA PHE A 255 11688 7449 8122 -880 766 -51 ATOM 1994 C PHE A 255 14.788 4.803 18.495 1.00 74.63 C ANISOU 1994 C PHE A 255 12079 7789 8487 -974 729 -115 ATOM 1995 O PHE A 255 15.809 4.846 19.183 1.00 75.06 O ANISOU 1995 O PHE A 255 12105 7864 8547 -1094 707 -74 ATOM 1996 CB PHE A 255 15.541 4.089 16.235 1.00 71.32 C ANISOU 1996 CB PHE A 255 11725 7237 8136 -824 786 3 ATOM 1997 CG PHE A 255 15.610 3.054 15.146 1.00 70.19 C ANISOU 1997 CG PHE A 255 11557 7115 7997 -741 821 75 ATOM 1998 CD1 PHE A 255 15.971 1.739 15.431 1.00 69.88 C ANISOU 1998 CD1 PHE A 255 11433 7181 7937 -782 827 151 ATOM 1999 CD2 PHE A 255 15.329 3.393 13.825 1.00 69.87 C ANISOU 1999 CD2 PHE A 255 11574 6995 7977 -622 848 68 ATOM 2000 CE1 PHE A 255 16.034 0.783 14.427 1.00 69.18 C ANISOU 2000 CE1 PHE A 255 11321 7112 7852 -707 857 216 ATOM 2001 CE2 PHE A 255 15.394 2.440 12.816 1.00 69.27 C ANISOU 2001 CE2 PHE A 255 11473 6942 7905 -549 879 136 ATOM 2002 CZ PHE A 255 15.747 1.134 13.118 1.00 68.91 C ANISOU 2002 CZ PHE A 255 11345 6994 7841 -592 883 210 ATOM 2003 N ASN A 256 13.829 5.738 18.564 1.00 48.99 N ATOM 2004 CA ASN A 256 13.985 6.965 19.362 1.00 53.05 C ATOM 2005 C ASN A 256 12.791 7.224 20.294 1.00 55.96 C ATOM 2006 O ASN A 256 12.880 8.137 21.113 1.00 57.20 O ATOM 2007 CB ASN A 256 14.221 8.231 18.486 1.00 0.00 C ATOM 2008 CG ASN A 256 15.314 8.106 17.424 1.00 0.00 C ATOM 2009 OD1 ASN A 256 15.068 7.625 16.321 1.00 0.00 O ATOM 2010 ND2 ASN A 256 16.531 8.543 17.727 1.00 0.00 N ATOM 2011 N GLY A 257 11.684 6.476 20.164 1.00 58.97 N ATOM 2012 CA GLY A 257 10.447 6.727 20.922 1.00 61.75 C ATOM 2013 C GLY A 257 9.698 7.971 20.407 1.00 62.91 C ATOM 2014 O GLY A 257 8.781 8.456 21.069 1.00 63.12 O ATOM 2015 N GLU A 258 10.103 8.514 19.253 1.00 63.82 N ATOM 2016 CA GLU A 258 9.706 9.821 18.750 1.00 64.00 C ATOM 2017 C GLU A 258 8.352 9.756 18.024 1.00 62.95 C ATOM 2018 O GLU A 258 8.308 9.802 16.800 1.00 63.27 O ATOM 2019 CB GLU A 258 10.877 10.350 17.891 1.00 0.00 C ATOM 2020 CG GLU A 258 10.710 11.778 17.315 1.00 0.00 C ATOM 2021 CD GLU A 258 11.911 12.296 16.507 1.00 0.00 C ATOM 2022 OE1 GLU A 258 12.932 11.584 16.394 1.00 0.00 O ATOM 2023 OE2 GLU A 258 11.789 13.430 15.998 1.00 0.00 O1- ATOM 2024 N VAL A 259 7.245 9.679 18.767 1.00 60.74 N ATOM 2025 CA VAL A 259 5.905 9.893 18.217 1.00 57.38 C ATOM 2026 C VAL A 259 5.785 11.396 17.883 1.00 56.09 C ATOM 2027 O VAL A 259 5.882 12.212 18.805 1.00 56.07 O ATOM 2028 CB VAL A 259 4.842 9.451 19.252 1.00 0.00 C ATOM 2029 CG1 VAL A 259 3.409 9.714 18.748 1.00 0.00 C ATOM 2030 CG2 VAL A 259 5.008 7.965 19.630 1.00 0.00 C ATOM 2031 N PRO A 260 5.645 11.782 16.596 1.00 53.78 N ATOM 2032 CA PRO A 260 5.652 13.191 16.209 1.00 51.38 C ATOM 2033 C PRO A 260 4.278 13.858 16.427 1.00 48.13 C ATOM 2034 O PRO A 260 3.320 13.236 16.886 1.00 47.73 O ATOM 2035 CD PRO A 260 5.566 10.914 15.411 1.00 0.00 C ATOM 2036 CB PRO A 260 6.054 13.149 14.730 1.00 0.00 C ATOM 2037 CG PRO A 260 5.459 11.854 14.212 1.00 0.00 C ATOM 2038 N GLN A 261 4.211 15.152 16.099 1.00 44.81 N ATOM 2039 CA GLN A 261 3.029 16.016 16.151 1.00 42.04 C ATOM 2040 C GLN A 261 2.067 15.773 14.962 1.00 39.32 C ATOM 2041 O GLN A 261 2.084 14.697 14.372 1.00 36.79 O ATOM 2042 CB GLN A 261 3.501 17.480 16.315 1.00 0.00 C ATOM 2043 CG GLN A 261 4.340 18.050 15.141 1.00 0.00 C ATOM 2044 CD GLN A 261 3.709 19.278 14.481 1.00 0.00 C ATOM 2045 OE1 GLN A 261 2.489 19.386 14.395 1.00 0.00 O ATOM 2046 NE2 GLN A 261 4.522 20.193 13.973 1.00 0.00 N ATOM 2047 N LEU A 262 1.262 16.777 14.580 1.00 81.57 N ANISOU 2047 N LEU A 262 13401 8747 8845 14 690 -1235 ATOM 2048 CA LEU A 262 0.191 16.717 13.569 1.00 81.57 C ANISOU 2048 CA LEU A 262 13433 8737 8822 117 726 -1221 ATOM 2049 C LEU A 262 0.632 16.204 12.178 1.00 80.92 C ANISOU 2049 C LEU A 262 13351 8605 8787 150 767 -1127 ATOM 2050 O LEU A 262 -0.202 15.741 11.399 1.00 80.31 O ANISOU 2050 O LEU A 262 13256 8570 8688 219 793 -1070 ATOM 2051 CB LEU A 262 -0.467 18.117 13.484 1.00 0.00 C ATOM 2052 CG LEU A 262 -1.827 18.206 12.748 1.00 0.00 C ATOM 2053 CD1 LEU A 262 -2.939 17.405 13.464 1.00 0.00 C ATOM 2054 CD2 LEU A 262 -2.227 19.679 12.509 1.00 0.00 C ATOM 2055 N VAL A 263 1.942 16.214 11.915 1.00 80.94 N ANISOU 2055 N VAL A 263 13372 8524 8856 96 769 -1105 ATOM 2056 CA VAL A 263 2.580 15.568 10.776 1.00 80.78 C ANISOU 2056 CA VAL A 263 13353 8453 8886 120 804 -1014 ATOM 2057 C VAL A 263 2.278 14.054 10.655 1.00 79.90 C ANISOU 2057 C VAL A 263 13169 8420 8769 112 810 -926 ATOM 2058 O VAL A 263 2.209 13.573 9.523 1.00 79.48 O ANISOU 2058 O VAL A 263 13105 8370 8724 169 842 -853 ATOM 2059 CB VAL A 263 4.117 15.780 10.802 1.00 0.00 C ATOM 2060 CG1 VAL A 263 4.478 17.275 10.730 1.00 0.00 C ATOM 2061 CG2 VAL A 263 4.838 15.105 11.984 1.00 0.00 C ATOM 2062 N LEU A 264 2.080 13.280 11.742 1.00 79.79 N ANISOU 2062 N LEU A 264 13102 8473 8738 43 775 -937 ATOM 2063 CA LEU A 264 1.711 11.863 11.580 1.00 78.68 C ANISOU 2063 CA LEU A 264 12892 8417 8584 41 769 -872 ATOM 2064 C LEU A 264 0.314 11.705 10.956 1.00 78.98 C ANISOU 2064 C LEU A 264 12917 8521 8569 121 773 -861 ATOM 2065 O LEU A 264 0.104 10.785 10.171 1.00 78.60 O ANISOU 2065 O LEU A 264 12838 8501 8525 157 789 -783 ATOM 2066 CB LEU A 264 1.854 10.991 12.853 1.00 0.00 C ATOM 2067 CG LEU A 264 1.507 11.560 14.243 1.00 0.00 C ATOM 2068 CD1 LEU A 264 0.130 12.226 14.336 1.00 0.00 C ATOM 2069 CD2 LEU A 264 1.599 10.449 15.293 1.00 0.00 C ATOM 2070 N TYR A 265 -0.608 12.643 11.211 1.00 80.41 N ANISOU 2070 N TYR A 265 13121 8728 8701 145 757 -935 ATOM 2071 CA TYR A 265 -1.945 12.629 10.633 1.00 80.99 C ANISOU 2071 CA TYR A 265 13183 8871 8718 211 753 -926 ATOM 2072 C TYR A 265 -1.909 13.054 9.162 1.00 79.45 C ANISOU 2072 C TYR A 265 13014 8654 8520 292 800 -876 ATOM 2073 O TYR A 265 -2.611 12.436 8.371 1.00 78.64 O ANISOU 2073 O TYR A 265 12880 8603 8396 332 805 -810 ATOM 2074 CB TYR A 265 -2.891 13.539 11.430 1.00 83.87 C ANISOU 2074 CB TYR A 265 13562 9275 9026 209 720 -1019 ATOM 2075 CG TYR A 265 -3.177 13.017 12.828 1.00 86.69 C ANISOU 2075 CG TYR A 265 13871 9709 9358 164 667 -1045 ATOM 2076 CD1 TYR A 265 -3.813 11.769 13.002 1.00 88.77 C ANISOU 2076 CD1 TYR A 265 14094 10044 9590 195 644 -1000 ATOM 2077 CD2 TYR A 265 -2.793 13.763 13.960 1.00 88.94 C ANISOU 2077 CD2 TYR A 265 14149 9995 9648 93 635 -1115 ATOM 2078 CE1 TYR A 265 -4.041 11.263 14.296 1.00 91.11 C ANISOU 2078 CE1 TYR A 265 14347 10408 9863 164 589 -1028 ATOM 2079 CE2 TYR A 265 -3.028 13.263 15.254 1.00 90.90 C ANISOU 2079 CE2 TYR A 265 14347 10321 9868 60 586 -1143 ATOM 2080 CZ TYR A 265 -3.647 12.010 15.423 1.00 93.44 C ANISOU 2080 CZ TYR A 265 14631 10710 10161 99 562 -1102 ATOM 2081 OH TYR A 265 -3.862 11.528 16.679 1.00100.76 O ANISOU 2081 OH TYR A 265 15510 11712 11060 77 506 -1135 ATOM 2082 N MET A 266 -1.045 14.008 8.769 1.00 78.96 N ANISOU 2082 N MET A 266 13005 8517 8477 318 830 -908 ATOM 2083 CA MET A 266 -0.686 14.281 7.376 1.00 78.26 C ANISOU 2083 CA MET A 266 12937 8413 8384 401 876 -864 ATOM 2084 C MET A 266 -0.113 13.045 6.659 1.00 76.43 C ANISOU 2084 C MET A 266 12676 8165 8198 408 903 -759 ATOM 2085 O MET A 266 -0.517 12.764 5.533 1.00 75.54 O ANISOU 2085 O MET A 266 12547 8087 8066 469 930 -698 ATOM 2086 CB MET A 266 0.263 15.495 7.297 1.00 0.00 C ATOM 2087 CG MET A 266 0.690 15.874 5.869 1.00 0.00 C ATOM 2088 SD MET A 266 1.733 17.352 5.790 1.00 0.00 S ATOM 2089 CE MET A 266 2.051 17.388 4.006 1.00 0.00 C ATOM 2090 N GLY A 267 0.784 12.311 7.332 1.00 75.38 N ANISOU 2090 N GLY A 267 12532 7987 8121 342 893 -737 ATOM 2091 CA GLY A 267 1.359 11.061 6.830 1.00 73.99 C ANISOU 2091 CA GLY A 267 12321 7804 7986 337 912 -639 ATOM 2092 C GLY A 267 0.273 9.991 6.645 1.00 72.29 C ANISOU 2092 C GLY A 267 12046 7680 7738 347 897 -582 ATOM 2093 O GLY A 267 0.288 9.264 5.649 1.00 72.63 O ANISOU 2093 O GLY A 267 12069 7739 7787 390 921 -504 ATOM 2094 N ILE A 268 -0.688 9.866 7.571 1.00 70.74 N ANISOU 2094 N ILE A 268 11824 7542 7509 309 852 -624 ATOM 2095 CA ILE A 268 -1.808 8.918 7.475 1.00 68.96 C ANISOU 2095 CA ILE A 268 11549 7398 7255 318 823 -581 ATOM 2096 C ILE A 268 -2.800 9.360 6.372 1.00 67.66 C ANISOU 2096 C ILE A 268 11392 7276 7039 386 833 -561 ATOM 2097 O ILE A 268 -3.236 8.521 5.579 1.00 66.76 O ANISOU 2097 O ILE A 268 11245 7201 6917 410 831 -486 ATOM 2098 CB ILE A 268 -2.475 8.767 8.876 1.00 69.00 C ANISOU 2098 CB ILE A 268 11525 7452 7240 262 767 -638 ATOM 2099 CG1 ILE A 268 -1.512 8.059 9.868 1.00 69.17 C ANISOU 2099 CG1 ILE A 268 11518 7454 7306 194 759 -632 ATOM 2100 CG2 ILE A 268 -3.824 8.012 8.843 1.00 68.64 C ANISOU 2100 CG2 ILE A 268 11438 7482 7159 282 726 -608 ATOM 2101 CD1 ILE A 268 -1.826 8.316 11.351 1.00 69.40 C ANISOU 2101 CD1 ILE A 268 11527 7522 7320 133 713 -707 ATOM 2102 N LEU A 269 -3.091 10.671 6.266 1.00 67.25 N ANISOU 2102 N LEU A 269 11381 7220 6951 415 842 -626 ATOM 2103 CA LEU A 269 -3.861 11.312 5.198 1.00 66.76 C ANISOU 2103 CA LEU A 269 11325 7205 6835 480 858 -605 ATOM 2104 C LEU A 269 -3.290 10.933 3.830 1.00 65.58 C ANISOU 2104 C LEU A 269 11176 7038 6703 534 910 -530 ATOM 2105 O LEU A 269 -4.037 10.479 2.968 1.00 64.96 O ANISOU 2105 O LEU A 269 11074 7017 6590 573 917 -467 ATOM 2106 CB LEU A 269 -3.931 12.848 5.465 1.00 0.00 C ATOM 2107 CG LEU A 269 -3.806 13.864 4.297 1.00 0.00 C ATOM 2108 CD1 LEU A 269 -4.914 13.705 3.242 1.00 0.00 C ATOM 2109 CD2 LEU A 269 -3.716 15.310 4.829 1.00 0.00 C ATOM 2110 N LEU A 270 -1.967 11.067 3.697 1.00 64.80 N ANISOU 2110 N LEU A 270 11102 6862 6656 535 944 -534 ATOM 2111 CA LEU A 270 -1.234 10.791 2.449 1.00 64.27 C ANISOU 2111 CA LEU A 270 11034 6774 6612 588 992 -463 ATOM 2112 C LEU A 270 -1.369 9.338 1.971 1.00 63.13 C ANISOU 2112 C LEU A 270 10836 6664 6485 579 989 -359 ATOM 2113 O LEU A 270 -1.558 9.097 0.772 1.00 63.24 O ANISOU 2113 O LEU A 270 10831 6715 6481 629 1016 -292 ATOM 2114 CB LEU A 270 0.254 11.142 2.595 1.00 64.72 C ANISOU 2114 CB LEU A 270 11130 6731 6729 584 1017 -486 ATOM 2115 CG LEU A 270 0.656 12.583 2.293 1.00 65.53 C ANISOU 2115 CG LEU A 270 11290 6789 6819 636 1039 -564 ATOM 2116 CD1 LEU A 270 2.008 12.920 2.907 1.00 65.80 C ANISOU 2116 CD1 LEU A 270 11369 6710 6919 604 1038 -602 ATOM 2117 CD2 LEU A 270 0.686 12.808 0.788 1.00 65.84 C ANISOU 2117 CD2 LEU A 270 11325 6857 6831 728 1084 -522 ATOM 2118 N SER A 271 -1.263 8.414 2.933 1.00 61.96 N ANISOU 2118 N SER A 271 10661 6512 6369 515 955 -348 ATOM 2119 CA SER A 271 -1.307 6.969 2.732 1.00 60.99 C ANISOU 2119 CA SER A 271 10488 6416 6267 502 945 -259 ATOM 2120 C SER A 271 -2.670 6.518 2.162 1.00 60.38 C ANISOU 2120 C SER A 271 10381 6418 6143 519 917 -218 ATOM 2121 O SER A 271 -2.712 5.848 1.134 1.00 60.40 O ANISOU 2121 O SER A 271 10355 6446 6146 545 929 -134 ATOM 2122 CB SER A 271 -0.978 6.285 4.076 1.00 0.00 C ATOM 2123 OG SER A 271 0.317 6.653 4.534 1.00 0.00 O ATOM 2124 N HIS A 272 -3.762 6.962 2.792 1.00 60.10 N ANISOU 2124 N HIS A 272 10349 6418 6066 503 874 -275 ATOM 2125 CA HIS A 272 -5.118 6.690 2.331 1.00 59.62 C ANISOU 2125 CA HIS A 272 10267 6427 5957 518 839 -239 ATOM 2126 C HIS A 272 -5.434 7.495 1.059 1.00 59.70 C ANISOU 2126 C HIS A 272 10290 6470 5923 577 879 -208 ATOM 2127 O HIS A 272 -6.099 6.987 0.158 1.00 59.41 O ANISOU 2127 O HIS A 272 10225 6482 5864 594 873 -129 ATOM 2128 CB HIS A 272 -6.100 7.056 3.459 1.00 59.69 C ANISOU 2128 CB HIS A 272 10282 6465 5931 490 782 -311 ATOM 2129 CG HIS A 272 -6.031 6.161 4.679 1.00 59.53 C ANISOU 2129 CG HIS A 272 10240 6433 5944 437 738 -345 ATOM 2130 ND1 HIS A 272 -6.746 6.412 5.839 1.00 59.94 N ANISOU 2130 ND1 HIS A 272 10303 6485 5984 404 708 -436 ATOM 2131 CD2 HIS A 272 -5.352 4.985 4.925 1.00 59.22 C ANISOU 2131 CD2 HIS A 272 10163 6390 5945 412 720 -301 ATOM 2132 CE1 HIS A 272 -6.479 5.432 6.703 1.00 59.72 C ANISOU 2132 CE1 HIS A 272 10244 6460 5986 362 674 -446 ATOM 2133 NE2 HIS A 272 -5.640 4.529 6.213 1.00 59.32 N ANISOU 2133 NE2 HIS A 272 10163 6408 5967 367 680 -367 ATOM 2134 N ALA A 273 -4.923 8.732 0.947 1.00 60.17 N ANISOU 2134 N ALA A 273 10388 6504 5969 606 918 -270 ATOM 2135 CA ALA A 273 -5.038 9.579 -0.242 1.00 60.80 C ANISOU 2135 CA ALA A 273 10478 6617 6004 671 963 -255 ATOM 2136 C ALA A 273 -4.330 9.004 -1.470 1.00 61.07 C ANISOU 2136 C ALA A 273 10488 6653 6059 707 1008 -165 ATOM 2137 O ALA A 273 -4.805 9.238 -2.580 1.00 61.57 O ANISOU 2137 O ALA A 273 10534 6783 6077 749 1028 -113 ATOM 2138 CB ALA A 273 -4.564 11.011 0.036 1.00 0.00 C ATOM 2139 N ASN A 274 -3.257 8.224 -1.277 1.00 60.93 N ANISOU 2139 N ASN A 274 10468 6573 6109 689 1021 -142 ATOM 2140 CA ASN A 274 -2.577 7.523 -2.383 1.00 60.76 C ANISOU 2140 CA ASN A 274 10420 6550 6114 721 1060 -54 ATOM 2141 C ASN A 274 -3.512 6.613 -3.207 1.00 60.86 C ANISOU 2141 C ASN A 274 10384 6639 6100 720 1042 42 ATOM 2142 O ASN A 274 -3.310 6.454 -4.415 1.00 60.81 O ANISOU 2142 O ASN A 274 10355 6666 6084 762 1079 110 ATOM 2143 CB ASN A 274 -1.387 6.712 -1.856 1.00 60.01 C ANISOU 2143 CB ASN A 274 10324 6381 6094 687 1063 -40 ATOM 2144 CG ASN A 274 -0.492 6.196 -2.965 1.00 59.79 C ANISOU 2144 CG ASN A 274 10278 6342 6096 727 1108 37 ATOM 2145 OD1 ASN A 274 -0.387 4.986 -3.178 1.00 59.17 O ANISOU 2145 OD1 ASN A 274 10161 6274 6044 705 1098 112 ATOM 2146 ND2 ASN A 274 0.152 7.107 -3.680 1.00 60.31 N ANISOU 2146 ND2 ASN A 274 10371 6387 6155 789 1154 16 ATOM 2147 N SER A 275 -4.530 6.041 -2.559 1.00 60.96 N ANISOU 2147 N SER A 275 10380 6679 6101 673 982 48 ATOM 2148 CA SER A 275 -5.555 5.249 -3.259 1.00 61.36 C ANISOU 2148 CA SER A 275 10391 6795 6125 665 950 135 ATOM 2149 C SER A 275 -6.412 6.052 -4.254 1.00 62.41 C ANISOU 2149 C SER A 275 10520 7007 6186 703 966 162 ATOM 2150 O SER A 275 -7.004 5.462 -5.163 1.00 62.68 O ANISOU 2150 O SER A 275 10518 7096 6199 703 957 253 ATOM 2151 CB SER A 275 -6.474 4.534 -2.262 1.00 61.23 C ANISOU 2151 CB SER A 275 10365 6783 6115 612 873 123 ATOM 2152 OG SER A 275 -5.743 3.629 -1.448 1.00 61.49 O ANISOU 2152 OG SER A 275 10389 6764 6208 577 857 111 ATOM 2153 N MET A 276 -6.471 7.384 -4.125 1.00 63.44 N ANISOU 2153 N MET A 276 10682 7145 6273 732 988 84 ATOM 2154 CA MET A 276 -7.257 8.227 -5.026 1.00 64.14 C ANISOU 2154 CA MET A 276 10764 7319 6284 773 1009 101 ATOM 2155 C MET A 276 -6.432 8.785 -6.200 1.00 65.17 C ANISOU 2155 C MET A 276 10884 7475 6399 840 1082 126 ATOM 2156 O MET A 276 -7.033 9.311 -7.134 1.00 65.35 O ANISOU 2156 O MET A 276 10882 7590 6358 872 1100 173 ATOM 2157 CB MET A 276 -8.013 9.284 -4.183 1.00 0.00 C ATOM 2158 CG MET A 276 -7.395 10.686 -4.051 1.00 0.00 C ATOM 2159 SD MET A 276 -8.103 11.627 -2.669 1.00 0.00 S ATOM 2160 CE MET A 276 -7.082 13.119 -2.747 1.00 0.00 C ATOM 2161 N MET A 277 -5.094 8.679 -6.163 1.00 66.30 N ANISOU 2161 N MET A 277 11046 7544 6601 863 1119 99 ATOM 2162 CA MET A 277 -4.237 9.354 -7.153 1.00 67.98 C ANISOU 2162 CA MET A 277 11261 7767 6801 939 1185 93 ATOM 2163 C MET A 277 -4.202 8.637 -8.509 1.00 68.77 C ANISOU 2163 C MET A 277 11306 7931 6889 965 1213 206 ATOM 2164 O MET A 277 -4.407 9.271 -9.565 1.00 69.43 O ANISOU 2164 O MET A 277 11368 8100 6911 1022 1251 224 ATOM 2165 CB MET A 277 -2.804 9.512 -6.610 1.00 68.13 C ANISOU 2165 CB MET A 277 11321 7674 6892 952 1207 32 ATOM 2166 CG MET A 277 -2.703 10.256 -5.283 1.00 68.40 C ANISOU 2166 CG MET A 277 11407 7639 6940 923 1181 -78 ATOM 2167 SD MET A 277 -1.003 10.557 -4.719 1.00 69.02 S ANISOU 2167 SD MET A 277 11538 7585 7100 933 1203 -143 ATOM 2168 CE MET A 277 -1.275 11.174 -3.057 1.00 68.50 C ANISOU 2168 CE MET A 277 11517 7466 7043 870 1155 -253 ATOM 2169 N ASN A 278 -3.960 7.322 -8.469 1.00 69.12 N ANISOU 2169 N ASN A 278 11326 7945 6990 922 1193 279 ATOM 2170 CA ASN A 278 -3.757 6.507 -9.679 1.00 69.74 C ANISOU 2170 CA ASN A 278 11353 8072 7071 940 1217 386 ATOM 2171 C ASN A 278 -4.815 6.747 -10.785 1.00 70.47 C ANISOU 2171 C ASN A 278 11402 8292 7081 956 1223 454 ATOM 2172 O ASN A 278 -4.444 7.129 -11.914 1.00 71.41 O ANISOU 2172 O ASN A 278 11493 8471 7165 1018 1276 483 ATOM 2173 CB ASN A 278 -3.608 5.009 -9.326 1.00 69.18 C ANISOU 2173 CB ASN A 278 11261 7957 7065 880 1179 451 ATOM 2174 CG ASN A 278 -2.249 4.666 -8.726 1.00 69.32 C ANISOU 2174 CG ASN A 278 11303 7874 7160 879 1195 417 ATOM 2175 OD1 ASN A 278 -1.293 5.438 -8.801 1.00 69.93 O ANISOU 2175 OD1 ASN A 278 11410 7908 7250 928 1238 364 ATOM 2176 ND2 ASN A 278 -2.162 3.484 -8.127 1.00 68.96 N ANISOU 2176 ND2 ASN A 278 11244 7790 7165 823 1156 449 ATOM 2177 N PRO A 279 -6.123 6.578 -10.466 1.00 70.38 N ANISOU 2177 N PRO A 279 11382 8324 7033 903 1168 478 ATOM 2178 CA PRO A 279 -7.171 6.922 -11.440 1.00 70.63 C ANISOU 2178 CA PRO A 279 11375 8479 6980 910 1169 543 ATOM 2179 C PRO A 279 -7.051 8.329 -12.018 1.00 70.92 C ANISOU 2179 C PRO A 279 11416 8585 6945 985 1226 488 ATOM 2180 O PRO A 279 -7.257 8.505 -13.218 1.00 70.57 O ANISOU 2180 O PRO A 279 11323 8646 6841 1018 1260 552 ATOM 2181 CB PRO A 279 -8.465 6.806 -10.629 1.00 70.66 C ANISOU 2181 CB PRO A 279 11393 8489 6964 845 1095 540 ATOM 2182 CG PRO A 279 -8.148 5.829 -9.565 1.00 70.02 C ANISOU 2182 CG PRO A 279 11334 8304 6966 796 1049 520 ATOM 2183 CD PRO A 279 -6.709 6.062 -9.213 1.00 70.01 C ANISOU 2183 CD PRO A 279 11359 8221 7019 834 1098 450 ATOM 2184 N ILE A 280 -6.705 9.305 -11.172 1.00 71.32 N ANISOU 2184 N ILE A 280 11519 8580 6998 1010 1234 369 ATOM 2185 CA ILE A 280 -6.589 10.700 -11.614 1.00 72.53 C ANISOU 2185 CA ILE A 280 11682 8793 7083 1085 1282 298 ATOM 2186 C ILE A 280 -5.386 10.874 -12.540 1.00 73.31 C ANISOU 2186 C ILE A 280 11767 8891 7196 1166 1347 298 ATOM 2187 O ILE A 280 -5.520 11.502 -13.597 1.00 74.20 O ANISOU 2187 O ILE A 280 11844 9113 7235 1228 1389 313 ATOM 2188 CB ILE A 280 -6.524 11.700 -10.430 1.00 72.41 C ANISOU 2188 CB ILE A 280 11730 8711 7071 1089 1267 166 ATOM 2189 CG1 ILE A 280 -7.852 11.677 -9.654 1.00 72.14 C ANISOU 2189 CG1 ILE A 280 11703 8703 7004 1021 1204 167 ATOM 2190 CG2 ILE A 280 -6.245 13.117 -10.927 1.00 73.19 C ANISOU 2190 CG2 ILE A 280 11841 8862 7105 1177 1316 84 ATOM 2191 CD1 ILE A 280 -7.810 12.372 -8.312 1.00 72.14 C ANISOU 2191 CD1 ILE A 280 11761 8626 7021 1005 1177 46 ATOM 2192 N VAL A 281 -4.229 10.322 -12.157 1.00 73.19 N ANISOU 2192 N VAL A 281 11777 8761 7270 1167 1354 282 ATOM 2193 CA VAL A 281 -3.028 10.408 -13.016 1.00 73.82 C ANISOU 2193 CA VAL A 281 11846 8829 7372 1245 1410 286 ATOM 2194 C VAL A 281 -3.188 9.634 -14.340 1.00 73.70 C ANISOU 2194 C VAL A 281 11757 8915 7331 1256 1434 410 ATOM 2195 O VAL A 281 -2.730 10.117 -15.391 1.00 74.56 O ANISOU 2195 O VAL A 281 11836 9090 7401 1338 1485 414 ATOM 2196 CB VAL A 281 -1.705 10.044 -12.267 1.00 73.65 C ANISOU 2196 CB VAL A 281 11872 8658 7453 1241 1409 242 ATOM 2197 CG1 VAL A 281 -1.678 8.605 -11.781 1.00 72.62 C ANISOU 2197 CG1 VAL A 281 11728 8474 7391 1159 1372 318 ATOM 2198 CG2 VAL A 281 -0.487 10.320 -13.139 1.00 74.53 C ANISOU 2198 CG2 VAL A 281 11981 8753 7583 1332 1463 235 ATOM 2199 N TYR A 282 -3.858 8.474 -14.304 1.00 72.96 N ANISOU 2199 N TYR A 282 11630 8836 7254 1177 1393 507 ATOM 2200 CA TYR A 282 -4.181 7.754 -15.551 1.00 73.41 C ANISOU 2200 CA TYR A 282 11615 8998 7280 1174 1406 631 ATOM 2201 C TYR A 282 -5.001 8.628 -16.507 1.00 74.90 C ANISOU 2201 C TYR A 282 11760 9340 7356 1213 1433 650 ATOM 2202 O TYR A 282 -4.705 8.689 -17.702 1.00 75.45 O ANISOU 2202 O TYR A 282 11776 9502 7387 1268 1480 700 ATOM 2203 CB TYR A 282 -4.962 6.452 -15.298 1.00 72.42 C ANISOU 2203 CB TYR A 282 11466 8864 7183 1077 1345 725 ATOM 2204 CG TYR A 282 -4.256 5.380 -14.487 1.00 71.34 C ANISOU 2204 CG TYR A 282 11355 8603 7147 1033 1316 725 ATOM 2205 CD1 TYR A 282 -2.903 5.088 -14.675 1.00 71.48 C ANISOU 2205 CD1 TYR A 282 11377 8556 7223 1076 1355 718 ATOM 2206 CD2 TYR A 282 -4.959 4.629 -13.545 1.00 70.68 C ANISOU 2206 CD2 TYR A 282 11287 8472 7096 951 1247 736 ATOM 2207 CE1 TYR A 282 -2.273 4.100 -13.932 1.00 70.69 C ANISOU 2207 CE1 TYR A 282 11294 8354 7208 1033 1329 723 ATOM 2208 CE2 TYR A 282 -4.333 3.643 -12.797 1.00 70.18 C ANISOU 2208 CE2 TYR A 282 11239 8308 7115 914 1221 733 ATOM 2209 CZ TYR A 282 -2.995 3.380 -12.995 1.00 70.09 C ANISOU 2209 CZ TYR A 282 11230 8242 7158 952 1263 729 ATOM 2210 OH TYR A 282 -2.382 2.400 -12.252 1.00 69.84 O ANISOU 2210 OH TYR A 282 11210 8124 7202 912 1237 731 ATOM 2211 N ALA A 283 -6.021 9.299 -15.973 1.00 75.80 N ANISOU 2211 N ALA A 283 11893 9488 7416 1184 1403 612 ATOM 2212 CA ALA A 283 -6.900 10.164 -16.769 1.00 77.14 C ANISOU 2212 CA ALA A 283 12023 9813 7473 1212 1423 630 ATOM 2213 C ALA A 283 -6.146 11.323 -17.405 1.00 79.04 C ANISOU 2213 C ALA A 283 12259 10104 7665 1326 1491 551 ATOM 2214 O ALA A 283 -6.336 11.617 -18.584 1.00 79.94 O ANISOU 2214 O ALA A 283 12311 10360 7702 1372 1531 601 ATOM 2215 CB ALA A 283 -8.041 10.692 -15.912 1.00 77.02 C ANISOU 2215 CB ALA A 283 12039 9806 7416 1162 1373 591 ATOM 2216 N TYR A 284 -5.277 11.940 -16.594 1.00 80.60 N ANISOU 2216 N TYR A 284 12523 10189 7909 1372 1501 427 ATOM 2217 CA TYR A 284 -4.355 13.007 -16.969 1.00 82.80 C ANISOU 2217 CA TYR A 284 12810 10492 8155 1487 1557 336 ATOM 2218 C TYR A 284 -3.355 12.583 -18.064 1.00 84.27 C ANISOU 2218 C TYR A 284 12960 10684 8372 1553 1603 379 ATOM 2219 O TYR A 284 -3.325 13.225 -19.115 1.00 85.60 O ANISOU 2219 O TYR A 284 13083 10971 8469 1638 1651 376 ATOM 2220 CB TYR A 284 -3.723 13.583 -15.670 1.00 0.00 C ATOM 2221 CG TYR A 284 -2.359 14.267 -15.714 1.00 0.00 C ATOM 2222 CD1 TYR A 284 -1.410 13.974 -14.711 1.00 0.00 C ATOM 2223 CD2 TYR A 284 -2.026 15.193 -16.727 1.00 0.00 C ATOM 2224 CE1 TYR A 284 -0.126 14.548 -14.751 1.00 0.00 C ATOM 2225 CE2 TYR A 284 -0.737 15.761 -16.774 1.00 0.00 C ATOM 2226 CZ TYR A 284 0.218 15.426 -15.794 1.00 0.00 C ATOM 2227 OH TYR A 284 1.479 15.940 -15.851 1.00 0.00 O ATOM 2228 N LYS A 285 -2.540 11.552 -17.803 1.00 85.06 N ANISOU 2228 N LYS A 285 13077 10668 8573 1515 1588 419 ATOM 2229 CA LYS A 285 -1.437 11.188 -18.692 1.00 86.41 C ANISOU 2229 CA LYS A 285 13223 10822 8783 1582 1629 448 ATOM 2230 C LYS A 285 -1.805 10.135 -19.741 1.00 86.46 C ANISOU 2230 C LYS A 285 13146 10932 8772 1556 1640 591 ATOM 2231 O LYS A 285 -1.435 10.310 -20.906 1.00 87.35 O ANISOU 2231 O LYS A 285 13205 11138 8843 1635 1687 617 ATOM 2232 CB LYS A 285 -0.206 10.734 -17.885 1.00 0.00 C ATOM 2233 CG LYS A 285 0.516 11.888 -17.170 1.00 0.00 C ATOM 2234 CD LYS A 285 1.963 11.536 -16.792 1.00 0.00 C ATOM 2235 CE LYS A 285 2.789 12.762 -16.374 1.00 0.00 C ATOM 2236 NZ LYS A 285 4.206 12.414 -16.169 1.00 0.00 N1+ ATOM 2237 N ILE A 286 -2.452 9.036 -19.331 1.00 86.13 N ANISOU 2237 N ILE A 286 13092 10874 8760 1449 1593 680 ATOM 2238 CA ILE A 286 -2.679 7.916 -20.257 1.00 86.56 C ANISOU 2238 CA ILE A 286 13072 11005 8811 1411 1593 817 ATOM 2239 C ILE A 286 -3.903 8.178 -21.151 1.00 88.62 C ANISOU 2239 C ILE A 286 13263 11444 8961 1393 1596 892 ATOM 2240 O ILE A 286 -5.045 8.209 -20.678 1.00 88.03 O ANISOU 2240 O ILE A 286 13197 11394 8856 1320 1551 910 ATOM 2241 CB ILE A 286 -2.825 6.559 -19.530 1.00 84.90 C ANISOU 2241 CB ILE A 286 12877 10696 8685 1307 1536 879 ATOM 2242 CG1 ILE A 286 -1.616 6.319 -18.610 1.00 84.10 C ANISOU 2242 CG1 ILE A 286 12840 10428 8684 1319 1533 808 ATOM 2243 CG2 ILE A 286 -2.957 5.425 -20.546 1.00 84.79 C ANISOU 2243 CG2 ILE A 286 12788 10756 8670 1275 1535 1015 ATOM 2244 CD1 ILE A 286 -1.583 4.967 -17.927 1.00 82.95 C ANISOU 2244 CD1 ILE A 286 12703 10193 8620 1230 1483 862 ATOM 2245 N LYS A 287 -3.672 8.337 -22.462 1.00 91.38 N ANISOU 2245 N LYS A 287 13543 11920 9254 1461 1648 937 ATOM 2246 CA LYS A 287 -4.720 8.701 -23.419 1.00 93.67 C ANISOU 2246 CA LYS A 287 13752 12405 9430 1454 1662 1017 ATOM 2247 C LYS A 287 -5.838 7.649 -23.594 1.00 93.13 C ANISOU 2247 C LYS A 287 13647 12385 9353 1329 1606 1150 ATOM 2248 O LYS A 287 -6.984 8.036 -23.820 1.00 93.53 O ANISOU 2248 O LYS A 287 13670 12546 9319 1290 1588 1188 ATOM 2249 CB LYS A 287 -4.085 9.118 -24.764 1.00 0.00 C ATOM 2250 CG LYS A 287 -3.340 8.005 -25.530 1.00 0.00 C ATOM 2251 CD LYS A 287 -2.804 8.491 -26.886 1.00 0.00 C ATOM 2252 CE LYS A 287 -2.132 7.370 -27.696 1.00 0.00 C ATOM 2253 NZ LYS A 287 -1.667 7.848 -29.009 1.00 0.00 N1+ ATOM 2254 N LYS A 288 -5.518 6.349 -23.478 1.00 91.76 N ANISOU 2254 N LYS A 288 13472 12128 9264 1270 1574 1221 ATOM 2255 CA LYS A 288 -6.523 5.298 -23.685 1.00 90.51 C ANISOU 2255 CA LYS A 288 13277 12006 9106 1157 1515 1352 ATOM 2256 C LYS A 288 -7.530 5.197 -22.535 1.00 88.64 C ANISOU 2256 C LYS A 288 13098 11693 8888 1070 1441 1334 ATOM 2257 O LYS A 288 -8.674 4.797 -22.752 1.00 88.10 O ANISOU 2257 O LYS A 288 13001 11688 8784 987 1390 1428 ATOM 2258 CB LYS A 288 -5.837 3.946 -23.903 1.00 90.72 C ANISOU 2258 CB LYS A 288 13285 11964 9218 1128 1503 1422 ATOM 2259 CG LYS A 288 -5.047 3.847 -25.202 1.00 92.25 C ANISOU 2259 CG LYS A 288 13407 12257 9387 1199 1566 1472 ATOM 2260 CD LYS A 288 -3.871 2.884 -25.095 1.00 92.23 C ANISOU 2260 CD LYS A 288 13416 12142 9484 1213 1571 1477 ATOM 2261 CE LYS A 288 -3.007 2.902 -26.350 1.00 93.17 C ANISOU 2261 CE LYS A 288 13466 12356 9577 1298 1636 1513 ATOM 2262 NZ LYS A 288 -2.007 1.795 -26.364 1.00 92.62 N1+ ANISOU 2262 NZ LYS A 288 13396 12194 9599 1296 1633 1546 ATOM 2263 N PHE A 289 -7.101 5.541 -21.321 1.00 87.39 N ANISOU 2263 N PHE A 289 13019 11398 8785 1086 1430 1217 ATOM 2264 CA PHE A 289 -8.008 5.622 -20.164 1.00 86.61 C ANISOU 2264 CA PHE A 289 12976 11233 8698 1019 1364 1180 ATOM 2265 C PHE A 289 -8.927 6.851 -20.250 1.00 87.21 C ANISOU 2265 C PHE A 289 13049 11417 8670 1033 1371 1149 ATOM 2266 O PHE A 289 -10.117 6.764 -19.913 1.00 88.07 O ANISOU 2266 O PHE A 289 13163 11547 8749 959 1312 1189 ATOM 2267 CB PHE A 289 -7.220 5.647 -18.841 1.00 85.89 C ANISOU 2267 CB PHE A 289 12965 10975 8695 1032 1354 1063 ATOM 2268 CG PHE A 289 -6.751 4.288 -18.373 1.00 84.95 C ANISOU 2268 CG PHE A 289 12857 10742 8675 981 1316 1099 ATOM 2269 CD1 PHE A 289 -7.673 3.307 -18.009 1.00 84.66 C ANISOU 2269 CD1 PHE A 289 12819 10683 8664 887 1238 1168 ATOM 2270 CD2 PHE A 289 -5.393 3.996 -18.264 1.00 84.25 C ANISOU 2270 CD2 PHE A 289 12785 10569 8657 1027 1352 1061 ATOM 2271 CE1 PHE A 289 -7.250 2.058 -17.569 1.00 83.49 C ANISOU 2271 CE1 PHE A 289 12679 10438 8602 846 1201 1193 ATOM 2272 CE2 PHE A 289 -4.965 2.752 -17.820 1.00 83.49 C ANISOU 2272 CE2 PHE A 289 12696 10379 8647 980 1317 1093 ATOM 2273 CZ PHE A 289 -5.895 1.780 -17.475 1.00 82.95 C ANISOU 2273 CZ PHE A 289 12622 10298 8598 891 1243 1156 ATOM 2274 N LYS A 290 -8.402 8.005 -20.690 1.00 87.19 N ANISOU 2274 N LYS A 290 13038 11478 8612 1131 1440 1074 ATOM 2275 CA LYS A 290 -9.195 9.242 -20.714 1.00 87.03 C ANISOU 2275 CA LYS A 290 13007 11578 8483 1160 1457 1037 ATOM 2276 C LYS A 290 -10.351 9.162 -21.732 1.00 86.29 C ANISOU 2276 C LYS A 290 12838 11649 8298 1102 1439 1170 ATOM 2277 O LYS A 290 -11.477 9.533 -21.402 1.00 85.52 O ANISOU 2277 O LYS A 290 12749 11601 8144 1053 1400 1182 ATOM 2278 CB LYS A 290 -8.268 10.469 -20.836 1.00 0.00 C ATOM 2279 CG LYS A 290 -7.916 10.996 -22.236 1.00 0.00 C ATOM 2280 CD LYS A 290 -6.805 12.056 -22.165 1.00 0.00 C ATOM 2281 CE LYS A 290 -6.376 12.570 -23.547 1.00 0.00 C ATOM 2282 NZ LYS A 290 -5.293 13.563 -23.443 1.00 0.00 N1+ ATOM 2283 N GLU A 291 -10.064 8.555 -22.892 1.00 85.52 N ANISOU 2283 N GLU A 291 12667 11637 8186 1104 1466 1274 ATOM 2284 CA GLU A 291 -11.024 8.165 -23.925 1.00 85.46 C ANISOU 2284 CA GLU A 291 12581 11793 8096 1041 1449 1416 ATOM 2285 C GLU A 291 -12.160 7.269 -23.386 1.00 84.24 C ANISOU 2285 C GLU A 291 12449 11576 7983 911 1352 1507 ATOM 2286 O GLU A 291 -13.339 7.532 -23.625 1.00 85.37 O ANISOU 2286 O GLU A 291 12562 11822 8052 847 1315 1589 ATOM 2287 CB GLU A 291 -10.212 7.482 -25.051 1.00 0.00 C ATOM 2288 CG GLU A 291 -11.022 6.892 -26.230 1.00 0.00 C ATOM 2289 CD GLU A 291 -10.177 6.204 -27.316 1.00 0.00 C ATOM 2290 OE1 GLU A 291 -8.946 6.062 -27.144 1.00 0.00 O ATOM 2291 OE2 GLU A 291 -10.791 5.808 -28.329 1.00 0.00 O1- ATOM 2292 N THR A 292 -11.770 6.233 -22.638 1.00 82.44 N ANISOU 2292 N THR A 292 12272 11181 7870 876 1309 1491 ATOM 2293 CA THR A 292 -12.684 5.261 -22.039 1.00 81.36 C ANISOU 2293 CA THR A 292 12162 10966 7784 766 1212 1559 ATOM 2294 C THR A 292 -13.548 5.874 -20.926 1.00 81.39 C ANISOU 2294 C THR A 292 12229 10922 7773 738 1160 1491 ATOM 2295 O THR A 292 -14.783 5.739 -20.964 1.00 82.34 O ANISOU 2295 O THR A 292 12341 11089 7853 660 1095 1571 ATOM 2296 CB THR A 292 -11.922 4.042 -21.490 1.00 79.78 C ANISOU 2296 CB THR A 292 11994 10610 7707 747 1183 1550 ATOM 2297 OG1 THR A 292 -11.053 3.526 -22.505 1.00 79.37 O ANISOU 2297 OG1 THR A 292 11884 10603 7668 780 1234 1607 ATOM 2298 CG2 THR A 292 -12.892 2.950 -21.051 1.00 79.09 C ANISOU 2298 CG2 THR A 292 11924 10459 7667 638 1079 1630 ATOM 2299 N TYR A 293 -12.917 6.580 -19.964 1.00 80.88 N ANISOU 2299 N TYR A 293 12226 10766 7738 798 1186 1347 ATOM 2300 CA TYR A 293 -13.583 7.246 -18.832 1.00 80.54 C ANISOU 2300 CA TYR A 293 12244 10674 7683 777 1139 1270 ATOM 2301 C TYR A 293 -14.747 8.127 -19.291 1.00 82.05 C ANISOU 2301 C TYR A 293 12403 11017 7752 763 1135 1312 ATOM 2302 O TYR A 293 -15.838 8.035 -18.730 1.00 82.01 O ANISOU 2302 O TYR A 293 12423 11003 7731 697 1062 1337 ATOM 2303 CB TYR A 293 -12.603 8.134 -18.031 1.00 0.00 C ATOM 2304 CG TYR A 293 -11.457 7.473 -17.285 1.00 0.00 C ATOM 2305 CD1 TYR A 293 -10.239 8.163 -17.150 1.00 0.00 C ATOM 2306 CD2 TYR A 293 -11.591 6.204 -16.686 1.00 0.00 C ATOM 2307 CE1 TYR A 293 -9.164 7.551 -16.488 1.00 0.00 C ATOM 2308 CE2 TYR A 293 -10.535 5.641 -15.940 1.00 0.00 C ATOM 2309 CZ TYR A 293 -9.302 6.300 -15.897 1.00 0.00 C ATOM 2310 OH TYR A 293 -8.198 5.732 -15.355 1.00 0.00 O ATOM 2311 N LEU A 294 -14.498 8.896 -20.358 1.00 83.26 N ANISOU 2311 N LEU A 294 12500 11314 7819 827 1212 1319 ATOM 2312 CA LEU A 294 -15.518 9.697 -21.046 1.00 84.68 C ANISOU 2312 CA LEU A 294 12632 11671 7872 814 1217 1378 ATOM 2313 C LEU A 294 -16.661 8.834 -21.582 1.00 84.66 C ANISOU 2313 C LEU A 294 12588 11728 7849 703 1145 1545 ATOM 2314 O LEU A 294 -17.830 9.181 -21.407 1.00 85.20 O ANISOU 2314 O LEU A 294 12660 11852 7857 647 1094 1587 ATOM 2315 CB LEU A 294 -14.898 10.489 -22.205 1.00 86.17 C ANISOU 2315 CB LEU A 294 12751 12013 7973 906 1313 1367 ATOM 2316 CG LEU A 294 -13.978 11.653 -21.826 1.00 86.87 C ANISOU 2316 CG LEU A 294 12875 12079 8049 1023 1380 1202 ATOM 2317 CD1 LEU A 294 -13.153 12.097 -23.027 1.00 87.91 C ANISOU 2317 CD1 LEU A 294 12939 12336 8124 1120 1468 1197 ATOM 2318 CD2 LEU A 294 -14.784 12.818 -21.266 1.00 87.33 C ANISOU 2318 CD2 LEU A 294 12963 12191 8028 1030 1367 1131 ATOM 2319 N LEU A 295 -16.322 7.735 -22.270 1.00 84.23 N ANISOU 2319 N LEU A 295 12497 11659 7848 669 1138 1641 ATOM 2320 CA LEU A 295 -17.278 6.779 -22.832 1.00 84.25 C ANISOU 2320 CA LEU A 295 12460 11708 7841 559 1065 1805 ATOM 2321 C LEU A 295 -18.161 6.134 -21.749 1.00 83.75 C ANISOU 2321 C LEU A 295 12466 11509 7844 475 954 1813 ATOM 2322 O LEU A 295 -19.372 6.065 -21.936 1.00 84.18 O ANISOU 2322 O LEU A 295 12511 11619 7851 395 885 1908 ATOM 2323 CB LEU A 295 -16.542 5.743 -23.721 1.00 0.00 C ATOM 2324 CG LEU A 295 -17.417 4.631 -24.349 1.00 0.00 C ATOM 2325 CD1 LEU A 295 -18.538 5.199 -25.246 1.00 0.00 C ATOM 2326 CD2 LEU A 295 -16.542 3.594 -25.086 1.00 0.00 C ATOM 2327 N ILE A 296 -17.566 5.724 -20.620 1.00 83.39 N ANISOU 2327 N ILE A 296 12487 11291 7904 495 935 1713 ATOM 2328 CA ILE A 296 -18.298 5.161 -19.477 1.00 83.15 C ANISOU 2328 CA ILE A 296 12525 11129 7939 431 831 1698 ATOM 2329 C ILE A 296 -19.184 6.237 -18.834 1.00 83.92 C ANISOU 2329 C ILE A 296 12656 11260 7967 431 808 1644 ATOM 2330 O ILE A 296 -20.361 5.975 -18.537 1.00 84.10 O ANISOU 2330 O ILE A 296 12698 11273 7981 355 715 1708 ATOM 2331 CB ILE A 296 -17.343 4.522 -18.434 1.00 82.09 C ANISOU 2331 CB ILE A 296 12446 10819 7922 461 826 1591 ATOM 2332 CG1 ILE A 296 -16.634 3.303 -19.039 1.00 81.90 C ANISOU 2332 CG1 ILE A 296 12389 10760 7968 447 831 1660 ATOM 2333 CG2 ILE A 296 -18.103 4.098 -17.175 1.00 81.65 C ANISOU 2333 CG2 ILE A 296 12458 10643 7922 409 724 1555 ATOM 2334 CD1 ILE A 296 -15.364 2.902 -18.322 1.00 81.41 C ANISOU 2334 CD1 ILE A 296 12363 10569 8000 499 863 1556 ATOM 2335 N LEU A 297 -18.659 7.463 -18.709 1.00 84.77 N ANISOU 2335 N LEU A 297 12773 11408 8027 515 887 1528 ATOM 2336 CA LEU A 297 -19.426 8.646 -18.331 1.00 85.75 C ANISOU 2336 CA LEU A 297 12924 11581 8075 525 876 1469 ATOM 2337 C LEU A 297 -20.652 8.838 -19.248 1.00 87.55 C ANISOU 2337 C LEU A 297 13100 11968 8194 466 847 1600 ATOM 2338 O LEU A 297 -21.778 8.759 -18.758 1.00 87.70 O ANISOU 2338 O LEU A 297 13149 11974 8199 403 763 1636 ATOM 2339 CB LEU A 297 -18.469 9.852 -18.165 1.00 0.00 C ATOM 2340 CG LEU A 297 -19.100 11.252 -17.970 1.00 0.00 C ATOM 2341 CD1 LEU A 297 -18.373 12.073 -16.885 1.00 0.00 C ATOM 2342 CD2 LEU A 297 -19.148 12.033 -19.301 1.00 0.00 C ATOM 2343 N LYS A 298 -20.418 8.963 -20.558 1.00 89.37 N ANISOU 2343 N LYS A 298 13252 12350 8351 486 913 1675 ATOM 2344 CA LYS A 298 -21.425 9.119 -21.610 1.00 91.32 C ANISOU 2344 CA LYS A 298 13436 12775 8486 428 896 1811 ATOM 2345 C LYS A 298 -22.464 7.982 -21.669 1.00 91.45 C ANISOU 2345 C LYS A 298 13456 12750 8540 305 783 1960 ATOM 2346 O LYS A 298 -23.630 8.250 -21.953 1.00 92.42 O ANISOU 2346 O LYS A 298 13584 12924 8605 240 716 2027 ATOM 2347 CB LYS A 298 -20.690 9.317 -22.956 1.00 0.00 C ATOM 2348 CG LYS A 298 -21.591 9.552 -24.184 1.00 0.00 C ATOM 2349 CD LYS A 298 -20.778 9.797 -25.465 1.00 0.00 C ATOM 2350 CE LYS A 298 -21.671 9.998 -26.701 1.00 0.00 C ATOM 2351 NZ LYS A 298 -20.876 10.221 -27.920 1.00 0.00 N1+ ATOM 2352 N ALA A 299 -22.032 6.742 -21.422 1.00 90.87 N ANISOU 2352 N ALA A 299 13380 12581 8563 274 757 2009 ATOM 2353 CA ALA A 299 -22.890 5.565 -21.468 1.00 90.92 C ANISOU 2353 CA ALA A 299 13388 12545 8612 160 646 2152 ATOM 2354 C ALA A 299 -23.712 5.371 -20.185 1.00 90.60 C ANISOU 2354 C ALA A 299 13433 12343 8647 114 533 2115 ATOM 2355 O ALA A 299 -24.894 5.044 -20.279 1.00 91.66 O ANISOU 2355 O ALA A 299 13575 12468 8784 20 429 2231 ATOM 2356 CB ALA A 299 -22.028 4.322 -21.742 1.00 0.00 C ATOM 2357 N CYS A 300 -23.066 5.508 -19.021 1.00 90.12 N ANISOU 2357 N CYS A 300 13437 12158 8646 179 547 1958 ATOM 2358 CA CYS A 300 -23.559 4.927 -17.769 1.00 89.69 C ANISOU 2358 CA CYS A 300 13459 11951 8665 143 441 1913 ATOM 2359 C CYS A 300 -23.809 5.963 -16.663 1.00 89.63 C ANISOU 2359 C CYS A 300 13505 11924 8627 187 443 1785 ATOM 2360 O CYS A 300 -24.498 5.618 -15.704 1.00 89.48 O ANISOU 2360 O CYS A 300 13524 11867 8604 138 348 1804 ATOM 2361 CB CYS A 300 -22.567 3.877 -17.219 1.00 0.00 C ATOM 2362 SG CYS A 300 -22.299 2.523 -18.404 1.00 0.00 S ATOM 2363 N VAL A 301 -23.218 7.162 -16.750 1.00 90.27 N ANISOU 2363 N VAL A 301 13587 12025 8685 277 544 1657 ATOM 2364 CA VAL A 301 -23.078 8.057 -15.594 1.00 90.76 C ANISOU 2364 CA VAL A 301 13702 12052 8729 322 547 1520 ATOM 2365 C VAL A 301 -23.575 9.497 -15.841 1.00 93.39 C ANISOU 2365 C VAL A 301 14008 12543 8933 358 608 1501 ATOM 2366 O VAL A 301 -23.877 10.187 -14.868 1.00 93.55 O ANISOU 2366 O VAL A 301 14062 12549 8933 418 644 1368 ATOM 2367 CB VAL A 301 -21.603 7.992 -15.063 1.00 0.00 C ATOM 2368 CG1 VAL A 301 -20.897 9.313 -14.687 1.00 0.00 C ATOM 2369 CG2 VAL A 301 -21.482 6.981 -13.910 1.00 0.00 C ATOM 2370 N VAL A 302 -23.673 9.935 -17.103 1.00 96.67 N ANISOU 2370 N VAL A 302 14360 13110 9258 321 616 1633 ATOM 2371 CA VAL A 302 -24.167 11.261 -17.465 1.00 99.14 C ANISOU 2371 CA VAL A 302 14634 13596 9436 354 674 1627 ATOM 2372 C VAL A 302 -25.609 11.556 -17.014 1.00101.03 C ANISOU 2372 C VAL A 302 14903 13862 9619 299 590 1657 ATOM 2373 O VAL A 302 -26.466 10.676 -16.935 1.00100.85 O ANISOU 2373 O VAL A 302 14900 13784 9633 213 484 1757 ATOM 2374 CB VAL A 302 -24.097 11.548 -18.991 1.00 0.00 C ATOM 2375 CG1 VAL A 302 -22.685 11.960 -19.416 1.00 0.00 C ATOM 2376 CG2 VAL A 302 -24.686 10.424 -19.863 1.00 0.00 C ATOM 2377 N CYS A 303 -25.812 12.845 -16.776 1.00128.03 N ANISOU 2377 N CYS A 303 14505 21972 12167 -4848 1539 -3139 ATOM 2378 CA CYS A 303 -27.036 13.482 -16.293 1.00126.19 C ANISOU 2378 CA CYS A 303 13883 21636 12425 -4390 1852 -3271 ATOM 2379 C CYS A 303 -27.196 14.792 -17.068 1.00122.11 C ANISOU 2379 C CYS A 303 12950 21287 12158 -4036 1460 -3055 ATOM 2380 O CYS A 303 -27.235 15.882 -16.494 1.00119.34 O ANISOU 2380 O CYS A 303 12397 20906 12038 -3796 1447 -3001 ATOM 2381 CB CYS A 303 -26.939 13.721 -14.783 1.00127.99 C ANISOU 2381 CB CYS A 303 14003 21635 12991 -4256 2320 -3372 ATOM 2382 SG CYS A 303 -25.346 14.416 -14.278 1.00128.59 S ANISOU 2382 SG CYS A 303 14068 21870 12919 -4267 2103 -3238 ATOM 2383 N HIS A 304 -27.223 14.645 -18.402 1.00122.49 N ANISOU 2383 N HIS A 304 12954 21411 12173 -4090 1188 -2900 ATOM 2384 CA HIS A 304 -27.288 15.749 -19.364 1.00121.52 C ANISOU 2384 CA HIS A 304 12563 21272 12337 -3827 1073 -2704 ATOM 2385 C HIS A 304 -28.473 16.731 -19.215 1.00120.17 C ANISOU 2385 C HIS A 304 12389 20977 12290 -3586 1233 -2825 ATOM 2386 O HIS A 304 -28.265 17.907 -19.520 1.00119.55 O ANISOU 2386 O HIS A 304 12378 20778 12266 -3485 1292 -2750 ATOM 2387 CB HIS A 304 -27.191 15.244 -20.823 1.00 0.00 C ATOM 2388 CG HIS A 304 -25.866 14.677 -21.251 1.00 0.00 C ATOM 2389 ND1 HIS A 304 -24.647 15.290 -20.946 1.00 0.00 N ATOM 2390 CD2 HIS A 304 -25.618 13.546 -21.997 1.00 0.00 C ATOM 2391 CE1 HIS A 304 -23.724 14.531 -21.525 1.00 0.00 C ATOM 2392 NE2 HIS A 304 -24.244 13.484 -22.165 1.00 0.00 N ATOM 2393 N PRO A 305 -29.664 16.299 -18.719 1.00120.18 N ANISOU 2393 N PRO A 305 12403 20929 12329 -3586 1309 -2971 ATOM 2394 CA PRO A 305 -30.745 17.240 -18.407 1.00119.91 C ANISOU 2394 CA PRO A 305 12392 20734 12431 -3501 1262 -2949 ATOM 2395 C PRO A 305 -30.454 18.247 -17.282 1.00120.29 C ANISOU 2395 C PRO A 305 12475 20682 12548 -3542 1103 -2814 ATOM 2396 O PRO A 305 -31.073 19.306 -17.272 1.00120.90 O ANISOU 2396 O PRO A 305 12784 20581 12572 -3659 894 -2684 ATOM 2397 CB PRO A 305 -31.909 16.321 -18.028 1.00120.57 C ANISOU 2397 CB PRO A 305 12344 20737 12728 -3509 1369 -3039 ATOM 2398 CG PRO A 305 -31.656 15.081 -18.806 1.00120.84 C ANISOU 2398 CG PRO A 305 12465 20890 12556 -3613 1496 -3168 ATOM 2399 CD PRO A 305 -30.165 14.912 -18.766 1.00121.35 C ANISOU 2399 CD PRO A 305 12623 21082 12401 -3746 1427 -3108 TER 2400 PRO A 305 HETATM 2401 C1 UNK Z 999 0.048 2.295 9.769 1.00 0.00 C HETATM 2402 N1 UNK Z 999 -1.274 2.308 9.886 1.00 0.00 N HETATM 2403 C2 UNK Z 999 -1.757 3.111 10.938 1.00 0.00 C HETATM 2404 C3 UNK Z 999 -0.709 3.715 11.632 1.00 0.00 C HETATM 2405 S1 UNK Z 999 0.854 3.296 10.951 1.00 0.00 S HETATM 2406 N2 UNK Z 999 0.646 1.511 8.752 1.00 0.00 N HETATM 2407 C4 UNK Z 999 1.940 1.511 8.378 1.00 0.00 C HETATM 2408 O1 UNK Z 999 2.829 2.132 8.958 1.00 0.00 O HETATM 2409 C5 UNK Z 999 3.094 -1.127 5.246 1.00 0.00 C HETATM 2410 N3 UNK Z 999 4.041 -0.564 6.021 1.00 0.00 N HETATM 2411 C6 UNK Z 999 3.647 0.317 6.958 1.00 0.00 C HETATM 2412 C7 UNK Z 999 2.296 0.644 7.208 1.00 0.00 C HETATM 2413 C8 UNK Z 999 1.323 0.104 6.339 1.00 0.00 C HETATM 2414 C9 UNK Z 999 1.728 -0.816 5.358 1.00 0.00 C HETATM 2415 N4 UNK Z 999 -0.505 6.515 14.919 1.00 0.00 N HETATM 2416 C10 UNK Z 999 0.512 5.674 14.647 1.00 0.00 C HETATM 2417 C11 UNK Z 999 0.473 4.715 13.619 1.00 0.00 C HETATM 2418 C12 UNK Z 999 -0.664 4.636 12.777 1.00 0.00 C HETATM 2419 C13 UNK Z 999 -1.726 5.511 13.076 1.00 0.00 C HETATM 2420 C14 UNK Z 999 -1.612 6.406 14.158 1.00 0.00 C HETATM 2421 C15 UNK Z 999 -6.063 3.039 11.406 1.00 0.00 C HETATM 2422 C16 UNK Z 999 -5.477 2.847 10.141 1.00 0.00 C HETATM 2423 C17 UNK Z 999 -4.075 2.903 10.000 1.00 0.00 C HETATM 2424 C18 UNK Z 999 -3.231 3.129 11.116 1.00 0.00 C HETATM 2425 C19 UNK Z 999 -3.846 3.320 12.376 1.00 0.00 C HETATM 2426 C20 UNK Z 999 -5.246 3.277 12.527 1.00 0.00 C HETATM 2427 C21 UNK Z 999 -6.353 2.575 8.938 1.00 0.00 C HETATM 2428 C22 UNK Z 999 -5.868 3.482 13.894 1.00 0.00 C CONECT 572 1256 CONECT 1256 572 CONECT 2401 2402 2405 2406 CONECT 2401 2402 CONECT 2402 2401 2403 CONECT 2402 2401 CONECT 2403 2402 2404 2424 CONECT 2403 2404 CONECT 2404 2403 2405 2418 CONECT 2404 2403 CONECT 2405 2401 2404 CONECT 2406 2401 2407 CONECT 2407 2406 2408 2412 CONECT 2407 2408 CONECT 2408 2407 CONECT 2408 2407 CONECT 2409 2410 2414 CONECT 2409 2410 CONECT 2410 2409 2411 CONECT 2410 2409 CONECT 2411 2410 2412 CONECT 2411 2412 CONECT 2412 2407 2411 2413 CONECT 2412 2411 CONECT 2413 2412 2414 CONECT 2413 2414 CONECT 2414 2409 2413 CONECT 2414 2413 CONECT 2415 2416 2420 CONECT 2415 2416 CONECT 2416 2415 2417 CONECT 2416 2415 CONECT 2417 2416 2418 CONECT 2417 2418 CONECT 2418 2404 2417 2419 CONECT 2418 2417 CONECT 2419 2418 2420 CONECT 2419 2420 CONECT 2420 2415 2419 CONECT 2420 2419 CONECT 2421 2422 2426 CONECT 2421 2422 CONECT 2422 2421 2423 2427 CONECT 2422 2421 CONECT 2423 2422 2424 CONECT 2423 2424 CONECT 2424 2403 2423 2425 CONECT 2424 2423 CONECT 2425 2424 2426 CONECT 2425 2426 CONECT 2426 2421 2425 2428 CONECT 2426 2425 CONECT 2427 2422 CONECT 2428 2426 END