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*** ***elNémo ID: 230329183114100145Job options:ID = 230329183114100145 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:CRYST1 70.490 71.252 171.247 90.00 90.00 90.00 P 21 21 21 1 ATOM 1 N ASP A -2 -27.213 34.688 -25.596 1.00 86.86 N ATOM 2 CA ASP A -2 -27.332 35.416 -26.897 1.00 89.08 C ATOM 3 C ASP A -2 -28.798 35.782 -27.149 1.00111.40 C ATOM 4 O ASP A -2 -29.699 35.000 -26.831 1.00 90.94 O ATOM 5 CB ASP A -2 -26.770 34.561 -28.058 1.00 88.85 C ATOM 6 CG ASP A -2 -26.490 35.369 -29.333 1.00 89.45 C ATOM 7 OD1 ASP A -2 -26.042 36.532 -29.233 1.00 92.79 O ATOM 8 OD2 ASP A -2 -26.684 34.819 -30.445 1.00 67.63 O1- ATOM 9 N ASP A -1 -29.020 36.982 -27.690 1.00139.32 N ATOM 10 CA ASP A -1 -30.358 37.461 -28.085 1.00115.61 C ATOM 11 C ASP A -1 -30.772 36.954 -29.473 1.00108.76 C ATOM 12 O ASP A -1 -31.967 36.791 -29.737 1.00105.36 O ATOM 13 CB ASP A -1 -30.408 38.995 -28.082 1.00114.92 C ATOM 14 CG ASP A -1 -30.146 39.598 -26.705 1.00121.76 C ATOM 15 OD1 ASP A -1 -29.496 38.945 -25.858 1.00129.59 O ATOM 16 OD2 ASP A -1 -30.586 40.743 -26.473 1.00100.54 O1- ATOM 17 N LYS A 0 -29.785 36.730 -30.352 1.00108.62 N ATOM 18 CA LYS A 0 -29.994 36.135 -31.688 1.00 98.97 C ATOM 19 C LYS A 0 -29.648 34.617 -31.757 1.00 87.12 C ATOM 20 O LYS A 0 -29.161 34.127 -32.787 1.00114.78 O ATOM 21 CB LYS A 0 -29.207 36.936 -32.741 1.00 87.17 C ATOM 22 CG LYS A 0 -29.928 37.429 -33.950 0.00108.17 C ATOM 23 CD LYS A 0 -30.166 36.311 -34.948 0.00103.45 C ATOM 24 CE LYS A 0 -30.514 36.872 -36.317 0.00100.19 C ATOM 25 NZ LYS A 0 -30.403 35.852 -37.395 0.00 97.82 N1+ ATOM 26 N MET A 1 -29.894 33.895 -30.654 1.00 67.00 N ANISOU 26 N MET A 1 8329 7904 9224 756 565 408 N ATOM 27 CA MET A 1 -29.928 32.418 -30.617 1.00 52.50 C ANISOU 27 CA MET A 1 6447 6272 7230 729 587 305 C ATOM 28 C MET A 1 -31.370 31.970 -30.370 1.00 37.58 C ANISOU 28 C MET A 1 4553 4484 5240 821 594 158 C ATOM 29 O MET A 1 -32.098 32.613 -29.621 1.00 40.37 O ANISOU 29 O MET A 1 4968 4751 5620 865 584 79 O ATOM 30 CB MET A 1 -29.017 31.883 -29.507 1.00 51.25 C ANISOU 30 CB MET A 1 6321 6044 7108 579 546 212 C ATOM 31 CG MET A 1 -29.002 30.362 -29.355 1.00 54.72 C ANISOU 31 CG MET A 1 6710 6655 7426 539 555 118 C ATOM 32 SD MET A 1 -28.011 29.745 -27.978 1.00 69.50 S ANISOU 32 SD MET A 1 8623 8463 9322 389 520 16 S ATOM 33 CE MET A 1 -26.388 30.398 -28.390 1.00 52.72 C ANISOU 33 CE MET A 1 6487 6219 7325 290 494 178 C ATOM 34 N ASP A 2 -31.779 30.857 -30.975 1.00 32.79 N ANISOU 34 N ASP A 2 3863 4061 4536 862 592 120 N ATOM 35 CA ASP A 2 -33.178 30.413 -30.872 1.00 29.74 C ANISOU 35 CA ASP A 2 3425 3760 4114 941 582 19 C ATOM 36 C ASP A 2 -33.578 29.981 -29.455 1.00 26.17 C ANISOU 36 C ASP A 2 2975 3281 3688 872 591 -75 C ATOM 37 O ASP A 2 -32.972 29.082 -28.866 1.00 25.41 O ANISOU 37 O ASP A 2 2857 3198 3601 765 579 -107 O ATOM 38 CB ASP A 2 -33.459 29.280 -31.839 1.00 33.22 C ANISOU 38 CB ASP A 2 3757 4361 4503 1003 521 -20 C ATOM 39 CG ASP A 2 -34.912 28.867 -31.839 1.00 30.57 C ANISOU 39 CG ASP A 2 3333 4087 4196 1076 482 -101 C ATOM 40 OD1 ASP A 2 -35.707 29.468 -32.581 1.00 29.75 O ANISOU 40 OD1 ASP A 2 3217 4029 4058 1218 481 -85 O ATOM 41 OD2 ASP A 2 -35.251 27.929 -31.099 1.00 36.13 O1- ANISOU 41 OD2 ASP A 2 3960 4793 4974 993 451 -157 O1- ATOM 42 N TYR A 3 -34.617 30.626 -28.935 1.00 24.19 N ANISOU 42 N TYR A 3 2743 3018 3432 964 621 -102 N ATOM 43 CA TYR A 3 -35.121 30.365 -27.594 1.00 24.18 C ANISOU 43 CA TYR A 3 2728 3044 3414 973 654 -152 C ATOM 44 C TYR A 3 -35.491 28.913 -27.388 1.00 21.68 C ANISOU 44 C TYR A 3 2259 2844 3135 909 654 -139 C ATOM 45 O TYR A 3 -35.142 28.357 -26.371 1.00 21.42 O ANISOU 45 O TYR A 3 2212 2830 3098 852 682 -138 O ATOM 46 CB TYR A 3 -36.343 31.241 -27.293 1.00 26.72 C ANISOU 46 CB TYR A 3 3066 3389 3698 1136 689 -164 C ATOM 47 CG TYR A 3 -36.879 31.056 -25.892 1.00 30.57 C ANISOU 47 CG TYR A 3 3530 3962 4124 1212 743 -186 C ATOM 48 CD1 TYR A 3 -36.205 31.599 -24.790 1.00 32.56 C ANISOU 48 CD1 TYR A 3 3911 4146 4316 1254 727 -265 C ATOM 49 CD2 TYR A 3 -38.054 30.318 -25.655 1.00 33.09 C ANISOU 49 CD2 TYR A 3 3676 4444 4453 1267 801 -113 C ATOM 50 CE1 TYR A 3 -36.686 31.426 -23.492 1.00 35.98 C ANISOU 50 CE1 TYR A 3 4319 4713 4639 1392 784 -278 C ATOM 51 CE2 TYR A 3 -38.546 30.140 -24.361 1.00 35.89 C ANISOU 51 CE2 TYR A 3 3978 4927 4732 1375 881 -72 C ATOM 52 CZ TYR A 3 -37.862 30.693 -23.279 1.00 37.46 C ANISOU 52 CZ TYR A 3 4323 5100 4811 1459 881 -158 C ATOM 53 OH TYR A 3 -38.330 30.506 -21.989 1.00 35.67 O ANISOU 53 OH TYR A 3 4041 5054 4458 1630 967 -111 O ATOM 54 N ASP A 4 -36.190 28.310 -28.348 1.00 21.03 N ANISOU 54 N ASP A 4 2054 2829 3109 931 605 -127 N ATOM 55 CA ASP A 4 -36.649 26.921 -28.209 1.00 22.96 C ANISOU 55 CA ASP A 4 2119 3133 3471 866 558 -110 C ATOM 56 C ASP A 4 -35.489 25.949 -28.135 1.00 21.07 C ANISOU 56 C ASP A 4 1883 2862 3261 734 507 -132 C ATOM 57 O ASP A 4 -35.468 25.072 -27.287 1.00 21.83 O ANISOU 57 O ASP A 4 1890 2969 3434 655 520 -89 O ATOM 58 CB ASP A 4 -37.567 26.504 -29.376 1.00 26.84 C ANISOU 58 CB ASP A 4 2480 3667 4052 933 449 -138 C ATOM 59 CG ASP A 4 -38.905 27.224 -29.374 1.00 31.86 C ANISOU 59 CG ASP A 4 3064 4354 4689 1059 495 -102 C ATOM 60 OD1 ASP A 4 -39.235 27.997 -28.426 1.00 23.58 O ANISOU 60 OD1 ASP A 4 2070 3324 3566 1114 613 -52 O ATOM 61 OD2 ASP A 4 -39.627 27.000 -30.363 1.00 46.22 O1- ANISOU 61 OD2 ASP A 4 4785 6203 6572 1131 392 -143 O1- ATOM 62 N PHE A 5 -34.545 26.101 -29.057 1.00 20.90 N ANISOU 62 N PHE A 5 1947 2818 3175 729 455 -175 N ATOM 63 CA PHE A 5 -33.275 25.377 -29.020 1.00 19.83 C ANISOU 63 CA PHE A 5 1842 2665 3029 626 419 -195 C ATOM 64 C PHE A 5 -32.557 25.577 -27.672 1.00 19.94 C ANISOU 64 C PHE A 5 1935 2628 3012 534 506 -170 C ATOM 65 O PHE A 5 -32.189 24.615 -27.024 1.00 22.33 O ANISOU 65 O PHE A 5 2187 2938 3359 446 496 -166 O ATOM 66 CB PHE A 5 -32.441 25.838 -30.214 1.00 23.09 C ANISOU 66 CB PHE A 5 2328 3102 3342 690 390 -193 C ATOM 67 CG PHE A 5 -31.005 25.405 -30.199 1.00 24.77 C ANISOU 67 CG PHE A 5 2587 3314 3512 607 380 -184 C ATOM 68 CD1 PHE A 5 -30.631 24.159 -30.696 1.00 27.27 C ANISOU 68 CD1 PHE A 5 2835 3690 3834 611 268 -251 C ATOM 69 CD2 PHE A 5 -30.012 26.279 -29.753 1.00 22.37 C ANISOU 69 CD2 PHE A 5 2384 2938 3177 541 456 -114 C ATOM 70 CE1 PHE A 5 -29.295 23.779 -30.714 1.00 28.03 C ANISOU 70 CE1 PHE A 5 2973 3808 3871 557 265 -236 C ATOM 71 CE2 PHE A 5 -28.680 25.905 -29.773 1.00 25.27 C ANISOU 71 CE2 PHE A 5 2773 3314 3515 467 448 -87 C ATOM 72 CZ PHE A 5 -28.320 24.656 -30.259 1.00 24.16 C ANISOU 72 CZ PHE A 5 2570 3266 3342 480 367 -142 C ATOM 73 N LYS A 6 -32.424 26.819 -27.219 1.00 23.11 N ANISOU 73 N LYS A 6 2455 2974 3351 574 570 -163 N ATOM 74 CA LYS A 6 -31.712 27.104 -25.961 1.00 22.58 C ANISOU 74 CA LYS A 6 2475 2856 3247 532 608 -185 C ATOM 75 C LYS A 6 -32.365 26.437 -24.739 1.00 24.05 C ANISOU 75 C LYS A 6 2582 3129 3426 559 665 -164 C ATOM 76 O LYS A 6 -31.691 25.768 -23.959 1.00 24.72 O ANISOU 76 O LYS A 6 2663 3233 3497 495 678 -162 O ATOM 77 CB LYS A 6 -31.581 28.622 -25.749 1.00 24.18 C ANISOU 77 CB LYS A 6 2813 2949 3427 604 609 -214 C ATOM 78 CG LYS A 6 -30.746 29.050 -24.542 1.00 24.98 C ANISOU 78 CG LYS A 6 3018 2967 3504 593 586 -287 C ATOM 79 CD LYS A 6 -30.410 30.494 -24.563 0.00 27.22 C ANISOU 79 CD LYS A 6 3420 3077 3844 640 519 -327 C ATOM 80 CE LYS A 6 -29.696 30.931 -23.294 0.00 28.09 C ANISOU 80 CE LYS A 6 3633 3092 3948 670 441 -452 C ATOM 81 NZ LYS A 6 -29.365 32.383 -23.310 0.00 29.56 N1+ ANISOU 81 NZ LYS A 6 3923 3047 4263 715 317 -509 N1+ ATOM 82 N VAL A 7 -33.673 26.607 -24.572 1.00 26.59 N ANISOU 82 N VAL A 7 2824 3524 3754 668 711 -120 N ATOM 83 CA VAL A 7 -34.355 26.027 -23.397 1.00 24.75 C ANISOU 83 CA VAL A 7 2477 3415 3513 730 796 -31 C ATOM 84 C VAL A 7 -34.456 24.510 -23.453 1.00 21.37 C ANISOU 84 C VAL A 7 1862 3021 3237 612 777 71 C ATOM 85 O VAL A 7 -34.399 23.846 -22.419 1.00 20.41 O ANISOU 85 O VAL A 7 1660 2977 3117 614 845 169 O ATOM 86 CB VAL A 7 -35.719 26.693 -23.075 1.00 29.84 C ANISOU 86 CB VAL A 7 3068 4158 4111 911 867 22 C ATOM 87 CG1 VAL A 7 -35.498 28.163 -22.745 1.00 29.98 C ANISOU 87 CG1 VAL A 7 3287 4119 3984 1051 859 -102 C ATOM 88 CG2 VAL A 7 -36.759 26.508 -24.183 1.00 28.97 C ANISOU 88 CG2 VAL A 7 2825 4050 4130 902 828 68 C ATOM 89 N LYS A 8 -34.568 23.961 -24.657 1.00 20.10 N ANISOU 89 N LYS A 8 1629 2799 3208 532 668 44 N ATOM 90 CA LYS A 8 -34.533 22.516 -24.834 1.00 22.04 C ANISOU 90 CA LYS A 8 1712 3020 3643 420 583 95 C ATOM 91 C LYS A 8 -33.209 21.974 -24.324 1.00 25.12 C ANISOU 91 C LYS A 8 2180 3383 3980 323 584 69 C ATOM 92 O LYS A 8 -33.196 21.039 -23.528 1.00 25.96 O ANISOU 92 O LYS A 8 2169 3514 4180 272 612 179 O ATOM 93 CB LYS A 8 -34.757 22.147 -26.309 1.00 26.41 C ANISOU 93 CB LYS A 8 2215 3511 4308 408 414 0 C ATOM 94 CG LYS A 8 -34.582 20.680 -26.690 1.00 30.94 C ANISOU 94 CG LYS A 8 2647 4015 5095 315 249 -17 C ATOM 95 CD LYS A 8 -35.405 19.737 -25.837 1.00 40.01 C ANISOU 95 CD LYS A 8 3557 5149 6497 255 260 164 C ATOM 96 CE LYS A 8 -35.150 18.288 -26.241 1.00 44.00 C ANISOU 96 CE LYS A 8 3924 5528 7265 156 51 133 C ATOM 97 NZ LYS A 8 -35.838 17.334 -25.325 1.00 45.32 N1+ ANISOU 97 NZ LYS A 8 3829 5656 7735 74 70 372 N1+ ATOM 98 N LEU A 9 -32.095 22.577 -24.758 1.00 26.78 N ANISOU 98 N LEU A 9 2571 3549 4055 303 559 -48 N ATOM 99 CA LEU A 9 -30.760 22.101 -24.340 1.00 25.90 C ANISOU 99 CA LEU A 9 2532 3415 3892 212 551 -79 C ATOM 100 C LEU A 9 -30.501 22.304 -22.864 1.00 18.42 C ANISOU 100 C LEU A 9 1628 2521 2849 243 661 -35 C ATOM 101 O LEU A 9 -29.964 21.435 -22.212 1.00 18.99 O ANISOU 101 O LEU A 9 1660 2616 2940 185 674 7 O ATOM 102 CB LEU A 9 -29.639 22.751 -25.156 1.00 25.24 C ANISOU 102 CB LEU A 9 2594 3284 3710 191 506 -168 C ATOM 103 CG LEU A 9 -29.538 22.276 -26.597 1.00 23.96 C ANISOU 103 CG LEU A 9 2392 3127 3585 203 391 -212 C ATOM 104 CD1 LEU A 9 -28.556 23.173 -27.324 1.00 30.12 C ANISOU 104 CD1 LEU A 9 3288 3903 4252 225 399 -221 C ATOM 105 CD2 LEU A 9 -29.110 20.816 -26.700 1.00 21.84 C ANISOU 105 CD2 LEU A 9 2039 2856 3403 139 288 -239 C ATOM 106 N SER A 10 -30.900 23.448 -22.344 1.00 20.01 N ANISOU 106 N SER A 10 1913 2751 2940 365 727 -57 N ATOM 107 CA SER A 10 -30.759 23.717 -20.919 1.00 24.87 C ANISOU 107 CA SER A 10 2574 3450 3424 473 808 -48 C ATOM 108 C SER A 10 -31.507 22.696 -20.038 1.00 25.45 C ANISOU 108 C SER A 10 2460 3670 3540 524 908 138 C ATOM 109 O SER A 10 -30.994 22.288 -19.004 1.00 23.41 O ANISOU 109 O SER A 10 2203 3496 3198 565 964 178 O ATOM 110 CB SER A 10 -31.221 25.137 -20.610 1.00 30.27 C ANISOU 110 CB SER A 10 3375 4135 3992 643 822 -130 C ATOM 111 OG SER A 10 -30.731 25.513 -19.345 1.00 41.46 O ANISOU 111 OG SER A 10 4887 5610 5256 775 839 -201 O ATOM 112 N SER A 11 -32.705 22.294 -20.474 1.00 25.05 N ANISOU 112 N SER A 11 2229 3649 3639 526 926 269 N ATOM 113 CA SER A 11 -33.515 21.266 -19.806 1.00 24.88 C ANISOU 113 CA SER A 11 1963 3740 3751 547 1011 516 C ATOM 114 C SER A 11 -32.846 19.900 -19.785 1.00 24.49 C ANISOU 114 C SER A 11 1815 3624 3868 384 957 590 C ATOM 115 O SER A 11 -32.849 19.227 -18.757 1.00 29.45 O ANISOU 115 O SER A 11 2323 4360 4506 426 1058 777 O ATOM 116 CB SER A 11 -34.874 21.147 -20.508 1.00 24.36 C ANISOU 116 CB SER A 11 1709 3664 3883 547 988 625 C ATOM 117 OG SER A 11 -35.707 20.204 -19.887 1.00 24.18 O ANISOU 117 OG SER A 11 1405 3731 4051 557 1066 912 O ATOM 118 N GLU A 12 -32.293 19.489 -20.923 1.00 26.75 N ANISOU 118 N GLU A 12 2142 3748 4273 230 797 453 N ATOM 119 CA GLU A 12 -31.645 18.168 -21.063 1.00 25.15 C ANISOU 119 CA GLU A 12 1857 3456 4243 88 701 483 C ATOM 120 C GLU A 12 -30.211 18.129 -20.545 1.00 21.29 C ANISOU 120 C GLU A 12 1535 2980 3572 57 722 389 C ATOM 121 O GLU A 12 -29.667 17.043 -20.384 1.00 18.36 O ANISOU 121 O GLU A 12 1097 2565 3313 -33 674 439 O ATOM 122 CB GLU A 12 -31.637 17.699 -22.535 1.00 26.85 C ANISOU 122 CB GLU A 12 2051 3520 4632 -4 490 344 C ATOM 123 CG GLU A 12 -33.013 17.576 -23.201 1.00 36.10 C ANISOU 123 CG GLU A 12 3039 4645 6031 16 406 401 C ATOM 124 CD GLU A 12 -33.905 16.485 -22.593 1.00 50.46 C ANISOU 124 CD GLU A 12 4557 6434 8180 -34 402 661 C ATOM 125 OE1 GLU A 12 -33.409 15.358 -22.326 1.00 43.72 O ANISOU 125 OE1 GLU A 12 3612 5495 7503 -131 329 730 O ATOM 126 OE2 GLU A 12 -35.124 16.743 -22.396 1.00 58.18 O1- ANISOU 126 OE2 GLU A 12 5368 7469 9269 26 468 823 O1- ATOM 127 N ARG A 13 -29.584 19.279 -20.297 1.00 21.91 N ANISOU 127 N ARG A 13 1819 3098 3406 128 770 251 N ATOM 128 CA ARG A 13 -28.146 19.279 -20.004 1.00 26.57 C ANISOU 128 CA ARG A 13 2560 3671 3866 79 748 138 C ATOM 129 C ARG A 13 -27.882 18.659 -18.639 1.00 30.22 C ANISOU 129 C ARG A 13 2969 4246 4266 134 848 258 C ATOM 130 O ARG A 13 -28.415 19.115 -17.633 1.00 39.23 O ANISOU 130 O ARG A 13 4095 5529 5283 302 965 337 O ATOM 131 CB ARG A 13 -27.523 20.678 -20.087 1.00 24.77 C ANISOU 131 CB ARG A 13 2534 3413 3466 129 734 -28 C ATOM 132 CG ARG A 13 -25.993 20.688 -19.962 1.00 21.49 C ANISOU 132 CG ARG A 13 2243 2952 2972 53 681 -136 C ATOM 133 CD ARG A 13 -25.310 21.750 -20.837 1.00 22.95 C ANISOU 133 CD ARG A 13 2552 3029 3138 11 606 -250 C ATOM 134 NE ARG A 13 -25.997 23.030 -20.708 1.00 33.00 N ANISOU 134 NE ARG A 13 3888 4275 4375 123 620 -290 N ATOM 135 CZ ARG A 13 -26.624 23.708 -21.674 1.00 32.22 C ANISOU 135 CZ ARG A 13 3790 4123 4328 139 603 -285 C ATOM 136 NH1 ARG A 13 -26.642 23.291 -22.939 1.00 29.30 N1+ ANISOU 136 NH1 ARG A 13 3364 3738 4030 70 564 -250 N1+ ATOM 137 NH2 ARG A 13 -27.232 24.854 -21.363 1.00 32.41 N ANISOU 137 NH2 ARG A 13 3879 4120 4316 259 611 -328 N ATOM 138 N GLU A 14 -27.087 17.596 -18.637 1.00 28.26 N ANISOU 138 N GLU A 14 2688 3957 4094 23 799 279 N ATOM 139 CA GLU A 14 -26.635 16.968 -17.417 1.00 27.96 C ANISOU 139 CA GLU A 14 2613 4026 3985 74 888 391 C ATOM 140 C GLU A 14 -25.603 17.877 -16.789 1.00 26.10 C ANISOU 140 C GLU A 14 2583 3844 3491 157 898 214 C ATOM 141 O GLU A 14 -24.589 18.180 -17.413 1.00 24.33 O ANISOU 141 O GLU A 14 2488 3516 3240 55 796 45 O ATOM 142 CB GLU A 14 -26.015 15.613 -17.725 1.00 31.52 C ANISOU 142 CB GLU A 14 2985 4385 4605 -74 802 436 C ATOM 143 CG GLU A 14 -27.054 14.589 -18.149 1.00 39.04 C ANISOU 143 CG GLU A 14 3699 5251 5881 -143 750 621 C ATOM 144 CD GLU A 14 -26.454 13.334 -18.769 1.00 52.61 C ANISOU 144 CD GLU A 14 5365 6817 7808 -283 583 590 C ATOM 145 OE1 GLU A 14 -25.509 13.448 -19.586 1.00 38.40 O ANISOU 145 OE1 GLU A 14 3719 4956 5917 -335 465 369 O ATOM 146 OE2 GLU A 14 -26.957 12.231 -18.458 1.00 51.58 O1- ANISOU 146 OE2 GLU A 14 5021 6625 7951 -327 561 802 O1- ATOM 147 N ARG A 15 -25.887 18.320 -15.568 1.00 26.99 N ANISOU 147 N ARG A 15 2707 4124 3423 365 1007 261 N ATOM 148 CA ARG A 15 -24.984 19.149 -14.775 1.00 29.01 C ANISOU 148 CA ARG A 15 3143 4432 3447 494 979 71 C ATOM 149 C ARG A 15 -24.239 18.266 -13.769 1.00 26.73 C ANISOU 149 C ARG A 15 2827 4266 3064 547 1031 143 C ATOM 150 O ARG A 15 -24.849 17.398 -13.144 1.00 27.48 O ANISOU 150 O ARG A 15 2753 4505 3183 628 1161 394 O ATOM 151 CB ARG A 15 -25.775 20.222 -14.016 1.00 32.00 C ANISOU 151 CB ARG A 15 3568 4946 3645 767 1032 32 C ATOM 152 CG ARG A 15 -26.606 21.171 -14.875 1.00 38.75 C ANISOU 152 CG ARG A 15 4452 5698 4573 755 992 -28 C ATOM 153 CD ARG A 15 -27.427 22.107 -13.984 1.00 48.15 C ANISOU 153 CD ARG A 15 5678 7054 5562 1072 1047 -58 C ATOM 154 NE ARG A 15 -28.491 22.840 -14.688 1.00 50.73 N ANISOU 154 NE ARG A 15 5988 7329 5958 1092 1048 -51 N ATOM 155 CZ ARG A 15 -29.532 23.449 -14.095 1.00 60.79 C ANISOU 155 CZ ARG A 15 7235 8773 7088 1367 1124 -9 C ATOM 156 NH1 ARG A 15 -29.690 23.430 -12.767 1.00 55.42 N1+ ANISOU 156 NH1 ARG A 15 6539 8356 6164 1681 1213 39 N1+ ATOM 157 NH2 ARG A 15 -30.441 24.084 -14.834 1.00 53.29 N ANISOU 157 NH2 ARG A 15 6272 7759 6216 1361 1116 -8 N ATOM 158 N VAL A 16 -22.936 18.512 -13.601 1.00 24.38 N ANISOU 158 N VAL A 16 2675 3913 2674 509 932 -52 N ATOM 159 CA VAL A 16 -22.067 17.721 -12.697 1.00 22.04 C ANISOU 159 CA VAL A 16 2375 3727 2273 558 962 -19 C ATOM 160 C VAL A 16 -22.601 17.625 -11.269 1.00 24.14 C ANISOU 160 C VAL A 16 2581 4267 2323 874 1102 111 C ATOM 161 O VAL A 16 -22.562 16.558 -10.674 1.00 27.93 O ANISOU 161 O VAL A 16 2937 4875 2798 912 1211 324 O ATOM 162 CB VAL A 16 -20.578 18.219 -12.713 1.00 22.24 C ANISOU 162 CB VAL A 16 2569 3650 2232 489 811 -277 C ATOM 163 CG1 VAL A 16 -20.409 19.653 -12.204 1.00 26.07 C ANISOU 163 CG1 VAL A 16 3203 4120 2582 667 704 -517 C ATOM 164 CG2 VAL A 16 -19.685 17.295 -11.912 1.00 23.94 C ANISOU 164 CG2 VAL A 16 2770 3973 2352 520 838 -239 C ATOM 165 N GLU A 17 -23.115 18.737 -10.753 1.00 26.12 N ANISOU 165 N GLU A 17 2911 4616 2399 1122 1096 -5 N ATOM 166 CA GLU A 17 -23.568 18.849 -9.362 1.00 30.23 C ANISOU 166 CA GLU A 17 3400 5449 2637 1514 1213 75 C ATOM 167 C GLU A 17 -24.907 18.159 -9.054 1.00 33.83 C ANISOU 167 C GLU A 17 3613 6117 3126 1636 1439 469 C ATOM 168 O GLU A 17 -25.190 17.886 -7.890 1.00 33.98 O ANISOU 168 O GLU A 17 3545 6445 2919 1957 1585 645 O ATOM 169 CB GLU A 17 -23.608 20.330 -8.914 1.00 35.04 C ANISOU 169 CB GLU A 17 4193 6085 3037 1786 1081 -233 C ATOM 170 CG GLU A 17 -24.693 21.239 -9.530 1.00 37.99 C ANISOU 170 CG GLU A 17 4572 6384 3479 1808 1071 -256 C ATOM 171 CD GLU A 17 -24.350 21.845 -10.902 1.00 38.52 C ANISOU 171 CD GLU A 17 4731 6099 3805 1472 911 -423 C ATOM 172 OE1 GLU A 17 -23.265 21.558 -11.459 1.00 37.05 O ANISOU 172 OE1 GLU A 17 4594 5728 3756 1212 812 -507 O ATOM 173 OE2 GLU A 17 -25.182 22.613 -11.447 1.00 34.90 O1- ANISOU 173 OE2 GLU A 17 4286 5569 3406 1488 895 -448 O1- ATOM 174 N ASP A 18 -25.726 17.891 -10.074 1.00 34.11 N ANISOU 174 N ASP A 18 3521 6000 3441 1405 1463 622 N ATOM 175 CA ASP A 18 -26.930 17.042 -9.914 1.00 36.77 C ANISOU 175 CA ASP A 18 3570 6474 3925 1442 1651 1042 C ATOM 176 C ASP A 18 -26.586 15.556 -10.020 1.00 34.93 C ANISOU 176 C ASP A 18 3165 6166 3942 1227 1687 1293 C ATOM 177 O ASP A 18 -27.195 14.723 -9.347 1.00 39.01 O ANISOU 177 O ASP A 18 3437 6861 4524 1339 1859 1680 O ATOM 178 CB ASP A 18 -27.992 17.363 -10.982 1.00 37.18 C ANISOU 178 CB ASP A 18 3543 6374 4211 1290 1623 1083 C ATOM 179 CG ASP A 18 -28.468 18.812 -10.941 1.00 36.81 C ANISOU 179 CG ASP A 18 3648 6384 3955 1499 1588 865 C ATOM 180 OD1 ASP A 18 -28.598 19.387 -9.837 1.00 37.82 O ANISOU 180 OD1 ASP A 18 3829 6776 3766 1866 1659 837 O ATOM 181 OD2 ASP A 18 -28.727 19.367 -12.030 1.00 34.63 O1- ANISOU 181 OD2 ASP A 18 3437 5893 3828 1321 1479 720 O1- ATOM 182 N LEU A 19 -25.633 15.227 -10.886 1.00 29.81 N ANISOU 182 N LEU A 19 2626 5253 3447 934 1523 1094 N ATOM 183 CA LEU A 19 -25.242 13.829 -11.111 1.00 34.58 C ANISOU 183 CA LEU A 19 3092 5741 4306 726 1506 1275 C ATOM 184 C LEU A 19 -24.355 13.236 -10.023 1.00 36.43 C ANISOU 184 C LEU A 19 3339 6141 4361 858 1581 1349 C ATOM 185 O LEU A 19 -24.468 12.045 -9.737 1.00 40.55 O ANISOU 185 O LEU A 19 3661 6674 5073 810 1655 1656 O ATOM 186 CB LEU A 19 -24.578 13.651 -12.484 1.00 31.64 C ANISOU 186 CB LEU A 19 2825 5061 4134 414 1297 1037 C ATOM 187 CG LEU A 19 -25.586 13.314 -13.589 1.00 40.94 C ANISOU 187 CG LEU A 19 3849 6056 5651 243 1224 1133 C ATOM 188 CD1 LEU A 19 -26.679 14.363 -13.718 1.00 40.22 C ANISOU 188 CD1 LEU A 19 3749 6034 5499 360 1281 1129 C ATOM 189 CD2 LEU A 19 -24.881 13.126 -14.924 1.00 46.75 C ANISOU 189 CD2 LEU A 19 4696 6546 6522 13 1015 886 C ATOM 190 N PHE A 20 -23.501 14.057 -9.409 1.00 34.71 N ANISOU 190 N PHE A 20 3342 6040 3807 1033 1547 1076 N ATOM 191 CA PHE A 20 -22.443 13.569 -8.522 1.00 29.26 C ANISOU 191 CA PHE A 20 2706 5478 2933 1140 1568 1058 C ATOM 192 C PHE A 20 -22.391 14.209 -7.137 1.00 31.29 C ANISOU 192 C PHE A 20 3031 6072 2785 1566 1661 1018 C ATOM 193 O PHE A 20 -22.543 15.418 -6.991 1.00 34.43 O ANISOU 193 O PHE A 20 3577 6520 2986 1743 1593 769 O ATOM 194 CB PHE A 20 -21.102 13.722 -9.244 1.00 26.50 C ANISOU 194 CB PHE A 20 2559 4899 2610 905 1366 717 C ATOM 195 CG PHE A 20 -20.942 12.754 -10.381 1.00 22.73 C ANISOU 195 CG PHE A 20 2002 4168 2467 572 1283 785 C ATOM 196 CD1 PHE A 20 -20.615 11.430 -10.128 1.00 21.54 C ANISOU 196 CD1 PHE A 20 1725 4012 2448 505 1320 997 C ATOM 197 CD2 PHE A 20 -21.171 13.143 -11.687 1.00 21.01 C ANISOU 197 CD2 PHE A 20 1826 3728 2429 363 1158 644 C ATOM 198 CE1 PHE A 20 -20.492 10.526 -11.161 1.00 22.98 C ANISOU 198 CE1 PHE A 20 1839 3952 2941 241 1201 1024 C ATOM 199 CE2 PHE A 20 -21.051 12.233 -12.733 1.00 19.73 C ANISOU 199 CE2 PHE A 20 1593 3359 2544 122 1053 676 C ATOM 200 CZ PHE A 20 -20.719 10.926 -12.471 1.00 20.17 C ANISOU 200 CZ PHE A 20 1535 3393 2736 64 1059 849 C ATOM 201 N GLU A 21 -22.192 13.370 -6.122 1.00 36.45 N ANISOU 201 N GLU A 21 3571 6961 3319 1756 1806 1268 N ATOM 202 CA GLU A 21 -21.875 13.812 -4.768 1.00 37.51 C ANISOU 202 CA GLU A 21 3785 7445 3024 2201 1868 1197 C ATOM 203 C GLU A 21 -20.355 13.801 -4.670 1.00 36.48 C ANISOU 203 C GLU A 21 3855 7214 2792 2121 1696 870 C ATOM 204 O GLU A 21 -19.723 12.749 -4.796 1.00 32.94 O ANISOU 204 O GLU A 21 3344 6683 2489 1929 1711 999 O ATOM 205 CB GLU A 21 -22.487 12.874 -3.719 1.00 40.07 C ANISOU 205 CB GLU A 21 3847 8116 3261 2482 2141 1700 C ATOM 206 CG GLU A 21 -22.279 13.293 -2.270 1.00 43.05 C ANISOU 206 CG GLU A 21 4285 8933 3137 3035 2228 1661 C ATOM 207 CD GLU A 21 -22.853 14.668 -1.969 1.00 48.16 C ANISOU 207 CD GLU A 21 5065 9742 3491 3375 2171 1403 C ATOM 208 OE1 GLU A 21 -24.078 14.867 -2.136 1.00 49.71 O ANISOU 208 OE1 GLU A 21 5108 10023 3757 3443 2302 1644 O ATOM 209 OE2 GLU A 21 -22.073 15.557 -1.573 1.00 50.08 O1- ANISOU 209 OE2 GLU A 21 5561 10012 3456 3577 1971 949 O1- ATOM 210 N TYR A 22 -19.787 14.992 -4.499 1.00 35.99 N ANISOU 210 N TYR A 22 4024 7132 2519 2257 1509 443 N ATOM 211 CA TYR A 22 -18.353 15.185 -4.310 1.00 31.82 C ANISOU 211 CA TYR A 22 3678 6521 1892 2223 1316 106 C ATOM 212 C TYR A 22 -18.017 16.320 -3.311 1.00 35.61 C ANISOU 212 C TYR A 22 4333 7180 2017 2644 1168 -247 C ATOM 213 O TYR A 22 -16.860 16.687 -3.189 1.00 39.22 O ANISOU 213 O TYR A 22 4941 7528 2432 2617 955 -575 O ATOM 214 CB TYR A 22 -17.697 15.447 -5.681 1.00 31.04 C ANISOU 214 CB TYR A 22 3675 6018 2102 1766 1125 -111 C ATOM 215 CG TYR A 22 -18.228 16.685 -6.378 1.00 33.22 C ANISOU 215 CG TYR A 22 4039 6117 2465 1708 1006 -310 C ATOM 216 CD1 TYR A 22 -19.397 16.639 -7.140 1.00 32.60 C ANISOU 216 CD1 TYR A 22 3847 5967 2571 1579 1110 -106 C ATOM 217 CD2 TYR A 22 -17.581 17.915 -6.253 1.00 37.36 C ANISOU 217 CD2 TYR A 22 4747 6535 2912 1792 771 -698 C ATOM 218 CE1 TYR A 22 -19.902 17.781 -7.759 1.00 35.32 C ANISOU 218 CE1 TYR A 22 4273 6163 2983 1545 1008 -278 C ATOM 219 CE2 TYR A 22 -18.086 19.064 -6.861 1.00 38.30 C ANISOU 219 CE2 TYR A 22 4939 6479 3134 1751 657 -858 C ATOM 220 CZ TYR A 22 -19.246 18.992 -7.617 1.00 36.84 C ANISOU 220 CZ TYR A 22 4652 6250 3095 1631 789 -644 C ATOM 221 OH TYR A 22 -19.753 20.128 -8.223 1.00 43.67 O ANISOU 221 OH TYR A 22 5590 6950 4054 1602 682 -793 O ATOM 222 N GLU A 23 -18.993 16.846 -2.560 1.00 44.52 N ANISOU 222 N GLU A 23 5432 8592 2891 3062 1260 -188 N ATOM 223 CA GLU A 23 -18.746 17.995 -1.663 1.00 47.64 C ANISOU 223 CA GLU A 23 6008 9140 2952 3509 1064 -580 C ATOM 224 C GLU A 23 -17.767 17.588 -0.562 1.00 48.14 C ANISOU 224 C GLU A 23 6122 9443 2727 3805 1022 -684 C ATOM 225 O GLU A 23 -18.007 16.609 0.157 1.00 42.41 O ANISOU 225 O GLU A 23 5242 9047 1823 4017 1274 -325 O ATOM 226 CB GLU A 23 -20.045 18.531 -1.029 1.00 48.32 C ANISOU 226 CB GLU A 23 6037 9550 2771 3969 1193 -465 C ATOM 227 CG GLU A 23 -19.981 20.038 -0.770 0.00 53.83 C ANISOU 227 CG GLU A 23 6955 10186 3310 4257 892 -962 C ATOM 228 CD GLU A 23 -21.264 20.565 -0.148 0.00 56.69 C ANISOU 228 CD GLU A 23 7268 10895 3374 4753 1015 -861 C ATOM 229 OE1 GLU A 23 -22.363 20.193 -0.612 0.00 55.87 O ANISOU 229 OE1 GLU A 23 6983 10847 3397 4630 1267 -470 O ATOM 230 OE2 GLU A 23 -21.171 21.365 0.807 0.00 59.72 O1- ANISOU 230 OE2 GLU A 23 7793 11502 3398 5289 840 -1186 O1- ATOM 231 N GLY A 24 -16.653 18.320 -0.470 1.00 46.09 N ANISOU 231 N GLY A 24 6056 9000 2456 3802 698 -1152 N ATOM 232 CA GLY A 24 -15.613 18.050 0.529 1.00 46.93 C ANISOU 232 CA GLY A 24 6232 9298 2304 4078 596 -1330 C ATOM 233 C GLY A 24 -14.890 16.732 0.334 1.00 42.85 C ANISOU 233 C GLY A 24 5612 8757 1911 3779 746 -1066 C ATOM 234 O GLY A 24 -14.372 16.174 1.282 1.00 44.69 O ANISOU 234 O GLY A 24 5834 9269 1878 4067 794 -1033 O ATOM 235 N CYS A 25 -14.862 16.227 -0.895 1.00 39.73 N ANISOU 235 N CYS A 25 5144 8042 1908 3232 809 -886 N ATOM 236 CA CYS A 25 -14.214 14.953 -1.199 1.00 37.50 C ANISOU 236 CA CYS A 25 4767 7703 1776 2936 927 -648 C ATOM 237 C CYS A 25 -13.027 15.188 -2.124 1.00 33.61 C ANISOU 237 C CYS A 25 4380 6836 1556 2514 689 -924 C ATOM 238 O CYS A 25 -12.782 14.405 -3.039 1.00 35.17 O ANISOU 238 O CYS A 25 4505 6841 2016 2122 754 -747 O ATOM 239 CB CYS A 25 -15.211 14.005 -1.859 1.00 36.65 C ANISOU 239 CB CYS A 25 4458 7561 1905 2694 1194 -176 C ATOM 240 SG CYS A 25 -16.572 13.507 -0.801 1.00 40.50 S ANISOU 240 SG CYS A 25 4738 8504 2144 3150 1524 291 S ATOM 241 N LYS A 26 -12.283 16.263 -1.883 1.00 35.08 N ANISOU 241 N LYS A 26 4721 6919 1690 2616 396 -1350 N ATOM 242 CA LYS A 26 -11.192 16.641 -2.762 1.00 34.46 C ANISOU 242 CA LYS A 26 4706 6488 1899 2232 166 -1577 C ATOM 243 C LYS A 26 -9.991 15.773 -2.434 1.00 35.15 C ANISOU 243 C LYS A 26 4784 6637 1934 2177 151 -1578 C ATOM 244 O LYS A 26 -9.647 15.629 -1.264 1.00 45.11 O ANISOU 244 O LYS A 26 6082 8160 2899 2544 125 -1677 O ATOM 245 CB LYS A 26 -10.844 18.118 -2.597 1.00 37.02 C ANISOU 245 CB LYS A 26 5164 6641 2263 2352 -169 -2004 C ATOM 246 CG LYS A 26 -9.962 18.649 -3.722 1.00 39.05 C ANISOU 246 CG LYS A 26 5433 6499 2905 1912 -375 -2138 C ATOM 247 CD LYS A 26 -9.705 20.139 -3.604 1.00 37.27 C ANISOU 247 CD LYS A 26 5304 6047 2810 2006 -726 -2517 C ATOM 248 CE LYS A 26 -10.867 20.941 -4.125 1.00 37.69 C ANISOU 248 CE LYS A 26 5373 5990 2958 2004 -701 -2486 C ATOM 249 NZ LYS A 26 -10.737 22.344 -3.660 1.00 48.67 N1+ ANISOU 249 NZ LYS A 26 6872 7214 4408 2231 -1062 -2884 N1+ ATOM 250 N VAL A 27 -9.378 15.186 -3.457 1.00 29.32 N ANISOU 250 N VAL A 27 3997 5687 1456 1756 170 -1468 N ATOM 251 CA VAL A 27 -8.183 14.355 -3.274 1.00 28.12 C ANISOU 251 CA VAL A 27 3834 5573 1276 1673 149 -1469 C ATOM 252 C VAL A 27 -6.910 14.967 -3.864 1.00 29.55 C ANISOU 252 C VAL A 27 4061 5495 1670 1418 -114 -1728 C ATOM 253 O VAL A 27 -5.815 14.668 -3.390 1.00 27.52 O ANISOU 253 O VAL A 27 3821 5295 1340 1459 -215 -1848 O ATOM 254 CB VAL A 27 -8.396 12.910 -3.776 1.00 26.79 C ANISOU 254 CB VAL A 27 3550 5437 1190 1471 393 -1098 C ATOM 255 CG1 VAL A 27 -9.490 12.238 -2.962 1.00 31.12 C ANISOU 255 CG1 VAL A 27 4011 6264 1550 1757 643 -799 C ATOM 256 CG2 VAL A 27 -8.754 12.852 -5.248 1.00 25.93 C ANISOU 256 CG2 VAL A 27 3392 5065 1395 1085 418 -978 C ATOM 257 N GLY A 28 -7.049 15.816 -4.886 1.00 30.44 N ANISOU 257 N GLY A 28 4175 5337 2056 1166 -219 -1786 N ATOM 258 CA GLY A 28 -5.911 16.516 -5.479 1.00 29.71 C ANISOU 258 CA GLY A 28 4082 4993 2214 929 -462 -1970 C ATOM 259 C GLY A 28 -6.201 17.982 -5.774 1.00 32.16 C ANISOU 259 C GLY A 28 4428 5068 2726 910 -673 -2162 C ATOM 260 O GLY A 28 -7.327 18.360 -6.086 1.00 29.79 O ANISOU 260 O GLY A 28 4139 4739 2440 938 -584 -2086 O ATOM 261 N ARG A 29 -5.167 18.808 -5.643 1.00 40.29 N ANISOU 261 N ARG A 29 5460 5912 3935 867 -972 -2408 N ATOM 262 CA ARG A 29 -5.216 20.213 -6.020 1.00 37.27 C ANISOU 262 CA ARG A 29 5082 5232 3848 795 -1223 -2575 C ATOM 263 C ARG A 29 -3.858 20.530 -6.603 1.00 38.65 C ANISOU 263 C ARG A 29 5152 5176 4358 505 -1418 -2593 C ATOM 264 O ARG A 29 -2.851 20.297 -5.945 1.00 40.52 O ANISOU 264 O ARG A 29 5380 5463 4555 574 -1563 -2740 O ATOM 265 CB ARG A 29 -5.498 21.098 -4.810 1.00 43.30 C ANISOU 265 CB ARG A 29 5957 6016 4478 1194 -1477 -2932 C ATOM 266 CG ARG A 29 -5.481 22.609 -5.073 1.00 49.65 C ANISOU 266 CG ARG A 29 6770 6464 5632 1149 -1810 -3155 C ATOM 267 CD ARG A 29 -6.645 23.090 -5.931 1.00 55.09 C ANISOU 267 CD ARG A 29 7458 7045 6427 1039 -1669 -2986 C ATOM 268 NE ARG A 29 -6.463 24.485 -6.361 1.00 63.12 N ANISOU 268 NE ARG A 29 8452 7673 7858 923 -1985 -3139 N ATOM 269 CZ ARG A 29 -6.026 24.909 -7.557 1.00 58.22 C ANISOU 269 CZ ARG A 29 7703 6771 7646 539 -2010 -2942 C ATOM 270 NH1 ARG A 29 -5.699 24.074 -8.540 1.00 52.56 N1+ ANISOU 270 NH1 ARG A 29 6878 6128 6964 238 -1746 -2604 N1+ ATOM 271 NH2 ARG A 29 -5.915 26.218 -7.777 1.00 70.25 N ANISOU 271 NH2 ARG A 29 9197 7935 9558 482 -2320 -3079 N ATOM 272 N GLY A 30 -3.822 21.032 -7.834 1.00 36.90 N ANISOU 272 N GLY A 30 4834 4725 4461 197 -1411 -2417 N ATOM 273 CA GLY A 30 -2.553 21.381 -8.473 1.00 38.89 C ANISOU 273 CA GLY A 30 4940 4773 5063 -78 -1571 -2355 C ATOM 274 C GLY A 30 -2.722 22.140 -9.764 1.00 38.67 C ANISOU 274 C GLY A 30 4800 4509 5384 -344 -1561 -2140 C ATOM 275 O GLY A 30 -3.755 22.750 -9.997 1.00 50.12 O ANISOU 275 O GLY A 30 6306 5872 6866 -296 -1537 -2143 O ATOM 276 N THR A 31 -1.699 22.093 -10.602 1.00 42.88 N ANISOU 276 N THR A 31 5164 4964 6164 -603 -1566 -1931 N ATOM 277 CA THR A 31 -1.715 22.769 -11.897 1.00 51.57 C ANISOU 277 CA THR A 31 6120 5883 7593 -841 -1532 -1659 C ATOM 278 C THR A 31 -2.722 22.146 -12.864 1.00 41.37 C ANISOU 278 C THR A 31 4865 4760 6095 -873 -1204 -1420 C ATOM 279 O THR A 31 -3.220 22.816 -13.762 1.00 46.62 O ANISOU 279 O THR A 31 5472 5297 6945 -970 -1166 -1257 O ATOM 280 CB THR A 31 -0.312 22.762 -12.534 1.00 63.07 C ANISOU 280 CB THR A 31 7354 7285 9325 -1068 -1586 -1441 C ATOM 281 CG2 THR A 31 -0.208 23.805 -13.659 1.00 76.99 C ANISOU 281 CG2 THR A 31 8926 8809 11518 -1275 -1630 -1163 C ATOM 282 OG1 THR A 31 0.663 23.057 -11.527 1.00 58.02 O ANISOU 282 OG1 THR A 31 6682 6532 8830 -1023 -1886 -1685 O ATOM 283 N TYR A 32 -2.980 20.854 -12.695 1.00 32.61 N ANISOU 283 N TYR A 32 3837 3924 4628 -788 -989 -1395 N ATOM 284 CA TYR A 32 -4.121 20.180 -13.342 1.00 27.50 C ANISOU 284 CA TYR A 32 3251 3423 3777 -763 -730 -1249 C ATOM 285 C TYR A 32 -5.498 20.774 -12.984 1.00 28.37 C ANISOU 285 C TYR A 32 3474 3471 3835 -620 -726 -1363 C ATOM 286 O TYR A 32 -6.366 20.906 -13.847 1.00 32.56 O ANISOU 286 O TYR A 32 3996 3985 4392 -668 -601 -1219 O ATOM 287 CB TYR A 32 -4.119 18.662 -13.053 1.00 22.54 C ANISOU 287 CB TYR A 32 2676 3054 2835 -687 -553 -1219 C ATOM 288 CG TYR A 32 -3.995 18.270 -11.593 1.00 20.50 C ANISOU 288 CG TYR A 32 2516 2901 2372 -490 -614 -1435 C ATOM 289 CD1 TYR A 32 -5.118 18.197 -10.778 1.00 19.37 C ANISOU 289 CD1 TYR A 32 2485 2841 2036 -277 -553 -1533 C ATOM 290 CD2 TYR A 32 -2.745 17.964 -11.026 1.00 20.16 C ANISOU 290 CD2 TYR A 32 2441 2906 2313 -488 -724 -1521 C ATOM 291 CE1 TYR A 32 -5.015 17.850 -9.439 1.00 20.69 C ANISOU 291 CE1 TYR A 32 2729 3154 1979 -41 -591 -1700 C ATOM 292 CE2 TYR A 32 -2.634 17.609 -9.686 1.00 21.42 C ANISOU 292 CE2 TYR A 32 2691 3192 2256 -267 -778 -1718 C ATOM 293 CZ TYR A 32 -3.777 17.551 -8.896 1.00 22.87 C ANISOU 293 CZ TYR A 32 2985 3477 2227 -30 -705 -1801 C ATOM 294 OH TYR A 32 -3.698 17.216 -7.560 1.00 25.09 O ANISOU 294 OH TYR A 32 3344 3931 2256 245 -741 -1967 O ATOM 295 N GLY A 33 -5.684 21.129 -11.719 1.00 28.12 N ANISOU 295 N GLY A 33 3544 3428 3712 -416 -869 -1624 N ATOM 296 CA GLY A 33 -6.947 21.661 -11.232 1.00 31.25 C ANISOU 296 CA GLY A 33 4048 3814 4011 -220 -870 -1746 C ATOM 297 C GLY A 33 -7.369 21.017 -9.922 1.00 34.47 C ANISOU 297 C GLY A 33 4565 4457 4075 73 -818 -1896 C ATOM 298 O GLY A 33 -6.568 20.897 -9.002 1.00 43.54 O ANISOU 298 O GLY A 33 5740 5661 5144 195 -955 -2072 O ATOM 299 N HIS A 34 -8.633 20.617 -9.850 1.00 29.51 N ANISOU 299 N HIS A 34 3980 3978 3253 200 -618 -1803 N ATOM 300 CA HIS A 34 -9.252 20.101 -8.648 1.00 26.77 C ANISOU 300 CA HIS A 34 3705 3882 2586 514 -530 -1870 C ATOM 301 C HIS A 34 -9.760 18.697 -8.975 1.00 25.11 C ANISOU 301 C HIS A 34 3435 3862 2243 448 -240 -1587 C ATOM 302 O HIS A 34 -10.555 18.529 -9.895 1.00 21.03 O ANISOU 302 O HIS A 34 2872 3301 1816 311 -106 -1406 O ATOM 303 CB HIS A 34 -10.436 20.993 -8.253 1.00 29.70 C ANISOU 303 CB HIS A 34 4145 4250 2889 749 -564 -1976 C ATOM 304 CG HIS A 34 -10.096 22.451 -8.122 1.00 34.67 C ANISOU 304 CG HIS A 34 4828 4621 3722 796 -884 -2252 C ATOM 305 CD2 HIS A 34 -10.041 23.440 -9.048 1.00 33.70 C ANISOU 305 CD2 HIS A 34 4672 4199 3931 584 -1015 -2248 C ATOM 306 ND1 HIS A 34 -9.770 23.040 -6.916 1.00 39.52 N ANISOU 306 ND1 HIS A 34 5532 5258 4225 1111 -1134 -2578 N ATOM 307 CE1 HIS A 34 -9.531 24.325 -7.106 1.00 40.49 C ANISOU 307 CE1 HIS A 34 5675 5072 4638 1074 -1433 -2782 C ATOM 308 NE2 HIS A 34 -9.689 24.593 -8.390 1.00 40.58 N ANISOU 308 NE2 HIS A 34 5606 4881 4932 746 -1353 -2562 N ATOM 309 N VAL A 35 -9.309 17.696 -8.226 1.00 24.78 N ANISOU 309 N VAL A 35 3387 4016 2010 554 -165 -1554 N ATOM 310 CA VAL A 35 -9.733 16.324 -8.445 1.00 23.12 C ANISOU 310 CA VAL A 35 3107 3950 1726 499 72 -1286 C ATOM 311 C VAL A 35 -10.435 15.841 -7.195 1.00 25.68 C ANISOU 311 C VAL A 35 3435 4539 1783 826 203 -1222 C ATOM 312 O VAL A 35 -9.877 15.930 -6.097 1.00 31.24 O ANISOU 312 O VAL A 35 4193 5386 2291 1068 124 -1377 O ATOM 313 CB VAL A 35 -8.550 15.430 -8.843 1.00 22.39 C ANISOU 313 CB VAL A 35 2976 3849 1684 310 66 -1231 C ATOM 314 CG1 VAL A 35 -8.947 13.957 -8.891 1.00 22.53 C ANISOU 314 CG1 VAL A 35 2925 3995 1640 294 265 -983 C ATOM 315 CG2 VAL A 35 -8.053 15.860 -10.212 1.00 22.25 C ANISOU 315 CG2 VAL A 35 2920 3624 1911 23 -12 -1212 C ATOM 316 N TYR A 36 -11.668 15.362 -7.380 1.00 25.43 N ANISOU 316 N TYR A 36 3330 4582 1752 850 397 -982 N ATOM 317 CA TYR A 36 -12.519 14.868 -6.299 1.00 25.76 C ANISOU 317 CA TYR A 36 3319 4897 1571 1162 571 -815 C ATOM 318 C TYR A 36 -12.829 13.386 -6.509 1.00 26.20 C ANISOU 318 C TYR A 36 3236 5013 1708 1047 767 -473 C ATOM 319 O TYR A 36 -12.928 12.924 -7.656 1.00 19.85 O ANISOU 319 O TYR A 36 2376 4019 1147 751 772 -371 O ATOM 320 CB TYR A 36 -13.854 15.602 -6.274 1.00 29.65 C ANISOU 320 CB TYR A 36 3798 5427 2039 1311 632 -772 C ATOM 321 CG TYR A 36 -13.788 17.102 -6.081 1.00 33.24 C ANISOU 321 CG TYR A 36 4385 5797 2447 1454 423 -1100 C ATOM 322 CD1 TYR A 36 -13.408 17.946 -7.132 1.00 28.16 C ANISOU 322 CD1 TYR A 36 3795 4849 2057 1180 250 -1260 C ATOM 323 CD2 TYR A 36 -14.149 17.684 -4.861 1.00 30.85 C ANISOU 323 CD2 TYR A 36 4143 5723 1857 1891 390 -1236 C ATOM 324 CE1 TYR A 36 -13.368 19.319 -6.967 1.00 31.45 C ANISOU 324 CE1 TYR A 36 4313 5140 2495 1297 34 -1541 C ATOM 325 CE2 TYR A 36 -14.108 19.058 -4.688 1.00 35.98 C ANISOU 325 CE2 TYR A 36 4916 6259 2494 2041 150 -1569 C ATOM 326 CZ TYR A 36 -13.716 19.872 -5.741 1.00 36.62 C ANISOU 326 CZ TYR A 36 5042 5986 2885 1724 -35 -1718 C ATOM 327 OH TYR A 36 -13.685 21.237 -5.573 1.00 41.11 O ANISOU 327 OH TYR A 36 5719 6399 3503 1861 -297 -2031 O ATOM 328 N LYS A 37 -12.986 12.659 -5.399 1.00 23.74 N ANISOU 328 N LYS A 37 2859 4963 1200 1308 911 -296 N ATOM 329 CA LYS A 37 -13.545 11.314 -5.416 1.00 25.84 C ANISOU 329 CA LYS A 37 2952 5285 1579 1251 1105 90 C ATOM 330 C LYS A 37 -15.053 11.498 -5.344 1.00 27.40 C ANISOU 330 C LYS A 37 3029 5566 1817 1370 1256 326 C ATOM 331 O LYS A 37 -15.548 12.193 -4.457 1.00 32.11 O ANISOU 331 O LYS A 37 3647 6392 2163 1708 1309 296 O ATOM 332 CB LYS A 37 -13.026 10.522 -4.224 1.00 32.89 C ANISOU 332 CB LYS A 37 3808 6436 2252 1499 1204 217 C ATOM 333 CG LYS A 37 -13.329 9.030 -4.229 1.00 39.21 C ANISOU 333 CG LYS A 37 4422 7247 3229 1410 1369 623 C ATOM 334 CD LYS A 37 -12.845 8.399 -2.924 1.00 42.91 C ANISOU 334 CD LYS A 37 4854 8015 3434 1718 1484 764 C ATOM 335 CE LYS A 37 -13.533 7.084 -2.607 1.00 45.13 C ANISOU 335 CE LYS A 37 4894 8373 3879 1744 1700 1275 C ATOM 336 NZ LYS A 37 -13.188 6.619 -1.234 1.00 45.10 N1+ ANISOU 336 NZ LYS A 37 4843 8725 3568 2120 1847 1452 N1+ ATOM 337 N ALA A 38 -15.786 10.922 -6.288 1.00 27.83 N ANISOU 337 N ALA A 38 2955 5440 2181 1117 1302 538 N ATOM 338 CA ALA A 38 -17.223 11.202 -6.406 1.00 32.17 C ANISOU 338 CA ALA A 38 3380 6025 2818 1183 1415 741 C ATOM 339 C ALA A 38 -18.064 9.946 -6.475 1.00 31.67 C ANISOU 339 C ALA A 38 3062 5949 3022 1104 1565 1183 C ATOM 340 O ALA A 38 -17.597 8.874 -6.855 1.00 30.61 O ANISOU 340 O ALA A 38 2864 5667 3101 904 1526 1286 O ATOM 341 CB ALA A 38 -17.493 12.077 -7.627 1.00 30.41 C ANISOU 341 CB ALA A 38 3245 5552 2757 958 1276 521 C ATOM 342 N LYS A 39 -19.326 10.121 -6.127 1.00 35.93 N ANISOU 342 N LYS A 39 3446 6632 3573 1270 1717 1443 N ATOM 343 CA LYS A 39 -20.316 9.064 -6.145 1.00 44.72 C ANISOU 343 CA LYS A 39 4265 7728 4997 1210 1856 1914 C ATOM 344 C LYS A 39 -21.498 9.581 -6.969 1.00 40.91 C ANISOU 344 C LYS A 39 3705 7113 4725 1096 1836 1945 C ATOM 345 O LYS A 39 -21.802 10.764 -6.930 1.00 37.36 O ANISOU 345 O LYS A 39 3382 6755 4058 1238 1827 1737 O ATOM 346 CB LYS A 39 -20.747 8.756 -4.703 1.00 54.78 C ANISOU 346 CB LYS A 39 5369 9396 6048 1599 2110 2294 C ATOM 347 CG LYS A 39 -20.974 7.283 -4.390 1.00 61.91 C ANISOU 347 CG LYS A 39 5985 10290 7248 1541 2238 2796 C ATOM 348 CD LYS A 39 -19.666 6.516 -4.293 1.00 64.04 C ANISOU 348 CD LYS A 39 6357 10473 7504 1439 2149 2682 C ATOM 349 CE LYS A 39 -19.870 5.168 -3.619 1.00 66.57 C ANISOU 349 CE LYS A 39 6389 10870 8033 1498 2314 3220 C ATOM 350 NZ LYS A 39 -18.599 4.389 -3.501 1.00 58.61 N1+ ANISOU 350 NZ LYS A 39 5481 9782 7004 1414 2228 3114 N1+ ATOM 351 N ARG A 40 -22.154 8.690 -7.700 1.00 40.50 N ANISOU 351 N ARG A 40 3443 6835 5111 853 1806 2193 N ATOM 352 CA ARG A 40 -23.351 9.020 -8.477 1.00 42.46 C ANISOU 352 CA ARG A 40 3574 6954 5604 746 1781 2263 C ATOM 353 C ARG A 40 -24.522 9.202 -7.507 1.00 45.77 C ANISOU 353 C ARG A 40 3770 7682 5937 1041 2029 2658 C ATOM 354 O ARG A 40 -24.685 8.390 -6.603 1.00 53.70 O ANISOU 354 O ARG A 40 4559 8868 6978 1188 2202 3067 O ATOM 355 CB ARG A 40 -23.628 7.882 -9.458 1.00 51.14 C ANISOU 355 CB ARG A 40 4496 7712 7222 429 1632 2402 C ATOM 356 CG ARG A 40 -24.380 8.252 -10.719 1.00 64.54 C ANISOU 356 CG ARG A 40 6182 9171 9170 238 1476 2257 C ATOM 357 CD ARG A 40 -24.117 7.202 -11.794 1.00 77.57 C ANISOU 357 CD ARG A 40 7775 10466 11231 -44 1230 2192 C ATOM 358 NE ARG A 40 -25.192 7.115 -12.781 1.00 97.32 N ANISOU 358 NE ARG A 40 10124 12750 14102 -185 1094 2226 N ATOM 359 CZ ARG A 40 -25.323 6.149 -13.695 1.00102.88 C ANISOU 359 CZ ARG A 40 10712 13137 15241 -383 850 2212 C ATOM 360 NH1 ARG A 40 -24.440 5.151 -13.782 1.00 93.11 N1+ ANISOU 360 NH1 ARG A 40 9495 11751 14132 -472 715 2169 N1+ ATOM 361 NH2 ARG A 40 -26.355 6.179 -14.537 1.00111.68 N ANISOU 361 NH2 ARG A 40 11689 14077 16669 -474 714 2220 N ATOM 362 N LYS A 41 -25.314 10.264 -7.677 1.00 46.21 N ANISOU 362 N LYS A 41 3869 7821 5870 1151 2056 2560 N ATOM 363 CA LYS A 41 -26.420 10.597 -6.739 1.00 48.39 C ANISOU 363 CA LYS A 41 3951 8449 5987 1494 2298 2908 C ATOM 364 C LYS A 41 -27.646 9.694 -6.898 1.00 54.19 C ANISOU 364 C LYS A 41 4283 9125 7181 1389 2403 3441 C ATOM 365 O LYS A 41 -28.284 9.321 -5.905 1.00 60.81 O ANISOU 365 O LYS A 41 4854 10270 7982 1652 2648 3923 O ATOM 366 CB LYS A 41 -26.832 12.079 -6.852 1.00 46.66 C ANISOU 366 CB LYS A 41 3925 8335 5471 1672 2272 2598 C ATOM 367 CG LYS A 41 -25.958 13.006 -6.025 1.00 45.66 C ANISOU 367 CG LYS A 41 4082 8433 4832 1985 2251 2250 C ATOM 368 CD LYS A 41 -26.249 14.472 -6.288 1.00 43.69 C ANISOU 368 CD LYS A 41 4044 8188 4368 2110 2153 1888 C ATOM 369 CE LYS A 41 -25.646 15.337 -5.193 1.00 45.88 C ANISOU 369 CE LYS A 41 4533 8745 4153 2530 2135 1618 C ATOM 370 NZ LYS A 41 -25.585 16.776 -5.556 1.00 44.56 N1+ ANISOU 370 NZ LYS A 41 4622 8468 3840 2590 1947 1168 N1+ ATOM 371 N ASP A 42 -27.997 9.376 -8.142 1.00 57.18 N ANISOU 371 N ASP A 42 4604 9125 7998 1032 2209 3365 N ATOM 372 CA ASP A 42 -28.899 8.245 -8.407 1.00 64.88 C ANISOU 372 CA ASP A 42 5188 9924 9541 850 2212 3832 C ATOM 373 C ASP A 42 -28.089 6.972 -8.148 1.00 67.91 C ANISOU 373 C ASP A 42 5486 10175 10141 727 2170 3999 C ATOM 374 O ASP A 42 -27.044 6.768 -8.764 1.00 66.06 O ANISOU 374 O ASP A 42 5485 9709 9905 535 1962 3624 O ATOM 375 CB ASP A 42 -29.494 8.282 -9.830 1.00 62.74 C ANISOU 375 CB ASP A 42 4890 9280 9667 542 1967 3646 C ATOM 376 CG ASP A 42 -28.442 8.387 -10.924 1.00 60.15 C ANISOU 376 CG ASP A 42 4880 8654 9320 304 1686 3108 C ATOM 377 OD1 ASP A 42 -27.833 7.356 -11.284 1.00 51.88 O ANISOU 377 OD1 ASP A 42 3799 7363 8549 110 1527 3098 O ATOM 378 OD2 ASP A 42 -28.227 9.513 -11.421 1.00 71.98 O1- ANISOU 378 OD2 ASP A 42 6652 10171 10528 331 1626 2713 O1- ATOM 379 N GLY A 43 -28.539 6.130 -7.221 1.00 66.12 N ANISOU 379 N GLY A 43 4919 10113 10089 857 2374 4578 N ATOM 380 CA GLY A 43 -27.776 4.943 -6.843 1.00 60.83 C ANISOU 380 CA GLY A 43 4160 9346 9608 779 2358 4777 C ATOM 381 C GLY A 43 -27.907 3.814 -7.848 1.00 65.19 C ANISOU 381 C GLY A 43 4535 9393 10841 390 2077 4835 C ATOM 382 O GLY A 43 -28.367 2.728 -7.501 1.00 81.78 O ANISOU 382 O GLY A 43 6266 11395 13412 331 2119 5358 O ATOM 383 N LYS A 44 -27.497 4.065 -9.092 1.00 68.56 N ANISOU 383 N LYS A 44 5214 9502 11332 149 1775 4306 N ATOM 384 CA LYS A 44 -27.515 3.048 -10.140 1.00 68.83 C ANISOU 384 CA LYS A 44 5137 9058 11956 -170 1445 4244 C ATOM 385 C LYS A 44 -26.330 2.112 -9.898 1.00 75.95 C ANISOU 385 C LYS A 44 6122 9853 12883 -226 1363 4203 C ATOM 386 O LYS A 44 -26.534 0.937 -9.589 1.00 82.29 O ANISOU 386 O LYS A 44 6625 10487 14155 -304 1332 4615 O ATOM 387 CB LYS A 44 -27.460 3.681 -11.536 1.00 65.95 C ANISOU 387 CB LYS A 44 5021 8464 11573 -332 1167 3692 C ATOM 388 CG LYS A 44 -28.714 4.353 -12.013 0.00 71.00 C ANISOU 388 CG LYS A 44 5535 9100 12341 -336 1169 3736 C ATOM 389 CD LYS A 44 -29.587 3.456 -12.884 0.00 72.97 C ANISOU 389 CD LYS A 44 5483 8944 13298 -565 885 3875 C ATOM 390 CE LYS A 44 -30.152 2.266 -12.126 0.00 76.87 C ANISOU 390 CE LYS A 44 5531 9349 14328 -604 951 4503 C ATOM 391 NZ LYS A 44 -31.196 1.550 -12.909 0.00 79.27 N1+ ANISOU 391 NZ LYS A 44 5492 9254 15371 -813 664 4667 N1+ ATOM 392 N ASP A 45 -25.107 2.647 -10.002 1.00 74.82 N ANISOU 392 N ASP A 45 6365 9810 12255 -179 1331 3738 N ATOM 393 CA ASP A 45 -23.870 1.904 -9.675 1.00 65.08 C ANISOU 393 CA ASP A 45 5247 8543 10936 -190 1286 3668 C ATOM 394 C ASP A 45 -23.260 2.450 -8.384 1.00 61.96 C ANISOU 394 C ASP A 45 4978 8588 9975 102 1587 3737 C ATOM 395 O ASP A 45 -23.543 3.583 -8.000 1.00 66.21 O ANISOU 395 O ASP A 45 5625 9416 10117 297 1752 3649 O ATOM 396 CB ASP A 45 -22.863 1.944 -10.845 1.00 61.90 C ANISOU 396 CB ASP A 45 5154 7900 10464 -358 983 3098 C ATOM 397 CG ASP A 45 -22.175 3.301 -11.010 1.00 58.52 C ANISOU 397 CG ASP A 45 5085 7691 9458 -263 1038 2650 C ATOM 398 OD1 ASP A 45 -21.404 3.689 -10.108 1.00 57.19 O ANISOU 398 OD1 ASP A 45 5062 7798 8869 -92 1211 2613 O ATOM 399 OD2 ASP A 45 -22.379 3.963 -12.052 1.00 50.76 O1- ANISOU 399 OD2 ASP A 45 4230 6593 8464 -353 889 2336 O1- ATOM 400 N ASP A 46 -22.423 1.641 -7.733 1.00 62.88 N ANISOU 400 N ASP A 46 5086 8748 10058 151 1631 3872 N ATOM 401 CA ASP A 46 -21.727 2.029 -6.492 1.00 62.41 C ANISOU 401 CA ASP A 46 5148 9103 9461 454 1880 3913 C ATOM 402 C ASP A 46 -20.220 2.225 -6.722 1.00 55.79 C ANISOU 402 C ASP A 46 4666 8245 8287 417 1739 3412 C ATOM 403 O ASP A 46 -19.439 2.171 -5.771 1.00 54.56 O ANISOU 403 O ASP A 46 4592 8345 7794 621 1872 3441 O ATOM 404 CB ASP A 46 -21.971 0.971 -5.390 1.00 67.04 C ANISOU 404 CB ASP A 46 5411 9828 10234 600 2090 4536 C ATOM 405 CG ASP A 46 -21.913 1.556 -3.970 1.00 68.57 C ANISOU 405 CG ASP A 46 5613 10565 9875 1033 2424 4735 C ATOM 406 OD1 ASP A 46 -22.679 2.502 -3.681 1.00 70.68 O ANISOU 406 OD1 ASP A 46 5864 11092 9900 1237 2573 4769 O ATOM 407 OD2 ASP A 46 -21.119 1.062 -3.137 1.00 57.62 O1- ANISOU 407 OD2 ASP A 46 4247 9360 8285 1200 2528 4852 O1- ATOM 408 N LYS A 47 -19.815 2.466 -7.970 1.00 49.04 N ANISOU 408 N LYS A 47 4008 7113 7512 183 1476 2971 N ATOM 409 CA LYS A 47 -18.399 2.658 -8.296 1.00 51.61 C ANISOU 409 CA LYS A 47 4638 7418 7555 136 1340 2529 C ATOM 410 C LYS A 47 -17.873 4.006 -7.788 1.00 43.75 C ANISOU 410 C LYS A 47 3889 6719 6014 331 1445 2237 C ATOM 411 O LYS A 47 -18.643 4.936 -7.558 1.00 43.17 O ANISOU 411 O LYS A 47 3806 6799 5797 460 1554 2255 O ATOM 412 CB LYS A 47 -18.169 2.553 -9.813 1.00 61.49 C ANISOU 412 CB LYS A 47 6000 8332 9034 -122 1042 2182 C ATOM 413 CG LYS A 47 -18.456 1.169 -10.382 1.00 64.49 C ANISOU 413 CG LYS A 47 6178 8371 9952 -296 845 2359 C ATOM 414 CD LYS A 47 -17.871 0.954 -11.777 1.00 64.58 C ANISOU 414 CD LYS A 47 6349 8114 10073 -461 528 1952 C ATOM 415 CE LYS A 47 -18.559 1.782 -12.859 1.00 59.75 C ANISOU 415 CE LYS A 47 5790 7413 9500 -532 415 1724 C ATOM 416 NZ LYS A 47 -17.699 2.897 -13.350 1.00 61.20 N1+ ANISOU 416 NZ LYS A 47 6267 7741 9248 -504 410 1322 N1+ ATOM 417 N ASP A 48 -16.559 4.086 -7.597 1.00 36.22 N ANISOU 417 N ASP A 48 3143 5834 4784 361 1390 1969 N ATOM 418 CA ASP A 48 -15.893 5.345 -7.308 1.00 35.85 C ANISOU 418 CA ASP A 48 3338 5978 4307 496 1397 1621 C ATOM 419 C ASP A 48 -15.453 5.976 -8.615 1.00 35.60 C ANISOU 419 C ASP A 48 3483 5728 4318 273 1188 1234 C ATOM 420 O ASP A 48 -14.818 5.310 -9.456 1.00 35.15 O ANISOU 420 O ASP A 48 3460 5469 4426 84 1029 1122 O ATOM 421 CB ASP A 48 -14.658 5.128 -6.431 1.00 43.86 C ANISOU 421 CB ASP A 48 4464 7174 5026 644 1426 1534 C ATOM 422 CG ASP A 48 -14.994 4.571 -5.048 1.00 48.21 C ANISOU 422 CG ASP A 48 4850 8010 5459 932 1654 1924 C ATOM 423 OD1 ASP A 48 -16.178 4.542 -4.661 1.00 46.31 O ANISOU 423 OD1 ASP A 48 4411 7874 5311 1054 1815 2264 O ATOM 424 OD2 ASP A 48 -14.049 4.165 -4.339 1.00 59.08 O1- ANISOU 424 OD2 ASP A 48 6284 9528 6636 1057 1681 1906 O1- ATOM 425 N TYR A 49 -15.778 7.260 -8.771 1.00 28.42 N ANISOU 425 N TYR A 49 2678 4874 3248 326 1188 1043 N ATOM 426 CA TYR A 49 -15.313 8.064 -9.902 1.00 23.81 C ANISOU 426 CA TYR A 49 2257 4130 2661 159 1020 705 C ATOM 427 C TYR A 49 -14.337 9.160 -9.471 1.00 20.92 C ANISOU 427 C TYR A 49 2085 3882 1983 260 979 412 C ATOM 428 O TYR A 49 -14.326 9.583 -8.319 1.00 22.48 O ANISOU 428 O TYR A 49 2310 4293 1940 501 1069 419 O ATOM 429 CB TYR A 49 -16.509 8.696 -10.604 1.00 25.21 C ANISOU 429 CB TYR A 49 2381 4214 2983 105 1015 726 C ATOM 430 CG TYR A 49 -17.428 7.679 -11.248 1.00 35.63 C ANISOU 430 CG TYR A 49 3505 5356 4678 -29 983 958 C ATOM 431 CD1 TYR A 49 -18.469 7.091 -10.525 1.00 36.60 C ANISOU 431 CD1 TYR A 49 3402 5548 4955 65 1128 1331 C ATOM 432 CD2 TYR A 49 -17.255 7.291 -12.583 1.00 38.68 C ANISOU 432 CD2 TYR A 49 3910 5507 5281 -226 791 816 C ATOM 433 CE1 TYR A 49 -19.307 6.152 -11.106 1.00 37.30 C ANISOU 433 CE1 TYR A 49 3281 5429 5463 -74 1058 1551 C ATOM 434 CE2 TYR A 49 -18.103 6.351 -13.177 1.00 39.03 C ANISOU 434 CE2 TYR A 49 3771 5356 5704 -329 701 985 C ATOM 435 CZ TYR A 49 -19.128 5.789 -12.434 1.00 37.56 C ANISOU 435 CZ TYR A 49 3352 5194 5725 -274 823 1351 C ATOM 436 OH TYR A 49 -19.958 4.846 -12.997 1.00 36.33 O ANISOU 436 OH TYR A 49 2985 4803 6017 -391 698 1530 O ATOM 437 N ALA A 50 -13.505 9.599 -10.405 1.00 16.96 N ANISOU 437 N ALA A 50 1702 3244 1497 96 829 163 N ATOM 438 CA ALA A 50 -12.679 10.776 -10.221 1.00 16.02 C ANISOU 438 CA ALA A 50 1732 3161 1192 141 747 -105 C ATOM 439 C ALA A 50 -13.272 11.887 -11.081 1.00 16.88 C ANISOU 439 C ALA A 50 1879 3149 1388 63 690 -210 C ATOM 440 O ALA A 50 -13.508 11.689 -12.288 1.00 13.55 O ANISOU 440 O ALA A 50 1424 2581 1145 -110 640 -190 O ATOM 441 CB ALA A 50 -11.248 10.496 -10.641 1.00 16.19 C ANISOU 441 CB ALA A 50 1821 3130 1199 14 631 -249 C ATOM 442 N LEU A 51 -13.503 13.046 -10.460 1.00 16.42 N ANISOU 442 N LEU A 51 1892 3154 1194 218 682 -334 N ATOM 443 CA LEU A 51 -14.011 14.229 -11.142 1.00 16.11 C ANISOU 443 CA LEU A 51 1899 2996 1228 170 618 -444 C ATOM 444 C LEU A 51 -12.920 15.255 -11.099 1.00 15.23 C ANISOU 444 C LEU A 51 1898 2812 1075 152 460 -692 C ATOM 445 O LEU A 51 -12.537 15.678 -10.021 1.00 16.91 O ANISOU 445 O LEU A 51 2175 3122 1129 342 410 -825 O ATOM 446 CB LEU A 51 -15.236 14.797 -10.428 1.00 19.84 C ANISOU 446 CB LEU A 51 2352 3580 1608 391 709 -388 C ATOM 447 CG LEU A 51 -16.625 14.387 -10.887 1.00 21.79 C ANISOU 447 CG LEU A 51 2470 3818 1993 361 827 -159 C ATOM 448 CD1 LEU A 51 -17.653 14.936 -9.920 1.00 24.24 C ANISOU 448 CD1 LEU A 51 2754 4310 2146 644 934 -91 C ATOM 449 CD2 LEU A 51 -16.889 14.915 -12.286 1.00 26.67 C ANISOU 449 CD2 LEU A 51 3104 4232 2795 159 743 -227 C ATOM 450 N LYS A 52 -12.417 15.646 -12.262 1.00 16.49 N ANISOU 450 N LYS A 52 2067 2810 1390 -54 368 -741 N ATOM 451 CA LYS A 52 -11.440 16.714 -12.360 1.00 20.20 C ANISOU 451 CA LYS A 52 2597 3169 1910 -105 208 -920 C ATOM 452 C LYS A 52 -12.094 17.977 -12.897 1.00 28.05 C ANISOU 452 C LYS A 52 3614 4021 3024 -122 149 -971 C ATOM 453 O LYS A 52 -12.650 17.958 -14.001 1.00 26.11 O ANISOU 453 O LYS A 52 3323 3710 2889 -240 202 -857 O ATOM 454 CB LYS A 52 -10.301 16.331 -13.298 1.00 18.34 C ANISOU 454 CB LYS A 52 2320 2873 1774 -307 158 -884 C ATOM 455 CG LYS A 52 -9.291 17.458 -13.450 1.00 20.06 C ANISOU 455 CG LYS A 52 2549 2960 2114 -382 -7 -1005 C ATOM 456 CD LYS A 52 -7.942 16.988 -13.924 1.00 21.30 C ANISOU 456 CD LYS A 52 2650 3131 2313 -516 -49 -963 C ATOM 457 CE LYS A 52 -7.841 17.047 -15.424 1.00 23.06 C ANISOU 457 CE LYS A 52 2795 3307 2661 -663 -16 -808 C ATOM 458 NZ LYS A 52 -6.596 16.352 -15.819 1.00 25.52 N1+ ANISOU 458 NZ LYS A 52 3046 3701 2952 -738 -26 -745 N1+ ATOM 459 N GLN A 53 -12.004 19.070 -12.139 1.00 25.67 N ANISOU 459 N GLN A 53 3382 3666 2705 13 18 -1157 N ATOM 460 CA GLN A 53 -12.318 20.396 -12.674 1.00 23.79 C ANISOU 460 CA GLN A 53 3166 3237 2634 -25 -93 -1228 C ATOM 461 C GLN A 53 -11.037 21.012 -13.210 1.00 23.08 C ANISOU 461 C GLN A 53 3044 2966 2760 -205 -259 -1273 C ATOM 462 O GLN A 53 -10.124 21.241 -12.441 1.00 25.54 O ANISOU 462 O GLN A 53 3379 3249 3076 -154 -411 -1429 O ATOM 463 CB GLN A 53 -12.913 21.307 -11.610 1.00 20.93 C ANISOU 463 CB GLN A 53 2894 2883 2176 240 -191 -1423 C ATOM 464 CG GLN A 53 -13.470 22.579 -12.220 1.00 21.61 C ANISOU 464 CG GLN A 53 3001 2766 2445 209 -289 -1470 C ATOM 465 CD GLN A 53 -13.787 23.625 -11.186 1.00 28.47 C ANISOU 465 CD GLN A 53 3971 3596 3251 486 -468 -1728 C ATOM 466 NE2 GLN A 53 -15.072 23.967 -11.044 1.00 27.37 N ANISOU 466 NE2 GLN A 53 3866 3529 3005 664 -389 -1718 N ATOM 467 OE1 GLN A 53 -12.881 24.142 -10.527 1.00 32.06 O ANISOU 467 OE1 GLN A 53 4469 3953 3759 558 -699 -1948 O ATOM 468 N ILE A 54 -10.981 21.313 -14.507 1.00 22.71 N ANISOU 468 N ILE A 54 2925 2806 2896 -393 -236 -1122 N ATOM 469 CA ILE A 54 -9.735 21.801 -15.117 1.00 30.13 C ANISOU 469 CA ILE A 54 3782 3609 4059 -568 -355 -1072 C ATOM 470 C ILE A 54 -9.432 23.190 -14.539 1.00 31.18 C ANISOU 470 C ILE A 54 3937 3509 4402 -528 -602 -1250 C ATOM 471 O ILE A 54 -10.353 23.958 -14.297 1.00 32.90 O ANISOU 471 O ILE A 54 4223 3641 4636 -412 -651 -1347 O ATOM 472 CB ILE A 54 -9.800 21.843 -16.677 1.00 27.03 C ANISOU 472 CB ILE A 54 3288 3194 3788 -722 -255 -828 C ATOM 473 CG1 ILE A 54 -10.055 20.446 -17.244 1.00 23.55 C ANISOU 473 CG1 ILE A 54 2831 2959 3157 -727 -78 -709 C ATOM 474 CG2 ILE A 54 -8.488 22.365 -17.279 1.00 34.11 C ANISOU 474 CG2 ILE A 54 4056 3984 4919 -877 -353 -706 C ATOM 475 CD1 ILE A 54 -10.070 20.370 -18.764 1.00 23.68 C ANISOU 475 CD1 ILE A 54 2757 3009 3230 -805 2 -504 C ATOM 476 N GLU A 55 -8.148 23.480 -14.299 1.00 32.94 N ANISOU 476 N GLU A 55 4095 3623 4797 -613 -776 -1301 N ATOM 477 CA GLU A 55 -7.686 24.853 -13.985 1.00 38.56 C ANISOU 477 CA GLU A 55 4781 4038 5834 -627 -1069 -1441 C ATOM 478 C GLU A 55 -8.155 25.850 -15.033 1.00 34.31 C ANISOU 478 C GLU A 55 4170 3297 5569 -742 -1076 -1269 C ATOM 479 O GLU A 55 -8.141 25.556 -16.222 1.00 37.23 O ANISOU 479 O GLU A 55 4439 3737 5969 -883 -895 -983 O ATOM 480 CB GLU A 55 -6.142 24.957 -13.893 1.00 44.01 C ANISOU 480 CB GLU A 55 5343 4620 6759 -769 -1245 -1428 C ATOM 481 CG GLU A 55 -5.592 25.246 -12.503 1.00 51.39 C ANISOU 481 CG GLU A 55 6348 5477 7700 -609 -1526 -1771 C ATOM 482 CD GLU A 55 -6.031 26.592 -11.974 1.00 59.37 C ANISOU 482 CD GLU A 55 7421 6205 8933 -480 -1823 -2020 C ATOM 483 OE1 GLU A 55 -5.523 27.618 -12.469 1.00 79.59 O ANISOU 483 OE1 GLU A 55 9850 8444 11945 -646 -2033 -1948 O ATOM 484 OE2 GLU A 55 -6.888 26.621 -11.065 1.00 60.65 O1- ANISOU 484 OE2 GLU A 55 7749 6468 8825 -196 -1850 -2271 O1- ATOM 485 N GLY A 56 -8.543 27.034 -14.579 1.00 35.71 N ANISOU 485 N GLY A 56 4399 3230 5937 -651 -1302 -1453 N ATOM 486 CA GLY A 56 -8.982 28.105 -15.460 1.00 36.14 C ANISOU 486 CA GLY A 56 4388 3055 6288 -744 -1343 -1303 C ATOM 487 C GLY A 56 -10.445 27.966 -15.797 1.00 33.50 C ANISOU 487 C GLY A 56 4157 2859 5712 -628 -1137 -1271 C ATOM 488 O GLY A 56 -11.147 27.127 -15.223 1.00 33.96 O ANISOU 488 O GLY A 56 4329 3163 5410 -467 -992 -1377 O ATOM 489 N THR A 57 -10.893 28.823 -16.714 1.00 36.47 N ANISOU 489 N THR A 57 4472 3067 6316 -707 -1132 -1102 N ATOM 490 CA THR A 57 -12.242 28.775 -17.285 1.00 43.06 C ANISOU 490 CA THR A 57 5371 4015 6975 -628 -935 -1023 C ATOM 491 C THR A 57 -12.142 28.653 -18.797 1.00 35.70 C ANISOU 491 C THR A 57 4295 3135 6135 -795 -748 -661 C ATOM 492 O THR A 57 -11.068 28.808 -19.370 1.00 38.00 O ANISOU 492 O THR A 57 4430 3352 6656 -954 -781 -454 O ATOM 493 CB THR A 57 -13.080 30.030 -16.934 1.00 46.92 C ANISOU 493 CB THR A 57 5948 4274 7607 -491 -1115 -1194 C ATOM 494 CG2 THR A 57 -13.371 30.077 -15.446 1.00 50.98 C ANISOU 494 CG2 THR A 57 6621 4821 7929 -231 -1278 -1569 C ATOM 495 OG1 THR A 57 -12.376 31.217 -17.319 1.00 62.43 O ANISOU 495 OG1 THR A 57 7797 5882 10041 -628 -1346 -1111 O ATOM 496 N GLY A 58 -13.269 28.356 -19.426 1.00 30.92 N ANISOU 496 N GLY A 58 3731 2679 5338 -730 -555 -579 N ATOM 497 CA GLY A 58 -13.358 28.279 -20.874 1.00 30.64 C ANISOU 497 CA GLY A 58 3578 2726 5337 -812 -388 -270 C ATOM 498 C GLY A 58 -12.618 27.092 -21.460 1.00 28.32 C ANISOU 498 C GLY A 58 3200 2676 4884 -876 -240 -113 C ATOM 499 O GLY A 58 -12.379 26.089 -20.780 1.00 24.41 O ANISOU 499 O GLY A 58 2764 2324 4188 -850 -216 -251 O ATOM 500 N ILE A 59 -12.252 27.221 -22.729 1.00 27.01 N ANISOU 500 N ILE A 59 2891 2571 4802 -930 -144 186 N ATOM 501 CA ILE A 59 -11.571 26.158 -23.448 1.00 31.68 C ANISOU 501 CA ILE A 59 3396 3421 5222 -937 -12 345 C ATOM 502 C ILE A 59 -10.193 26.677 -23.795 1.00 28.14 C ANISOU 502 C ILE A 59 2758 2900 5036 -1055 -66 594 C ATOM 503 O ILE A 59 -9.983 27.256 -24.858 1.00 31.30 O ANISOU 503 O ILE A 59 3003 3314 5576 -1061 2 908 O ATOM 504 CB ILE A 59 -12.360 25.710 -24.710 1.00 36.93 C ANISOU 504 CB ILE A 59 4042 4301 5689 -822 155 486 C ATOM 505 CG1 ILE A 59 -13.789 25.284 -24.355 1.00 38.36 C ANISOU 505 CG1 ILE A 59 4375 4516 5684 -725 187 264 C ATOM 506 CG2 ILE A 59 -11.644 24.567 -25.425 1.00 41.17 C ANISOU 506 CG2 ILE A 59 4505 5117 6022 -773 253 602 C ATOM 507 CD1 ILE A 59 -13.889 24.134 -23.368 1.00 43.01 C ANISOU 507 CD1 ILE A 59 5064 5192 6088 -710 181 40 C ATOM 508 N SER A 60 -9.265 26.498 -22.864 1.00 28.22 N ANISOU 508 N SER A 60 2763 2834 5124 -1136 -189 471 N ATOM 509 CA SER A 60 -7.866 26.837 -23.091 1.00 28.79 C ANISOU 509 CA SER A 60 2632 2850 5459 -1259 -250 708 C ATOM 510 C SER A 60 -7.207 25.713 -23.876 1.00 28.93 C ANISOU 510 C SER A 60 2562 3208 5223 -1212 -75 893 C ATOM 511 O SER A 60 -7.761 24.616 -24.012 1.00 28.95 O ANISOU 511 O SER A 60 2686 3438 4874 -1097 37 762 O ATOM 512 CB SER A 60 -7.136 26.992 -21.764 1.00 27.69 C ANISOU 512 CB SER A 60 2526 2515 5478 -1340 -473 465 C ATOM 513 OG SER A 60 -6.960 25.720 -21.161 1.00 26.18 O ANISOU 513 OG SER A 60 2450 2543 4956 -1282 -415 267 O ATOM 514 N MET A 61 -6.000 25.981 -24.343 1.00 32.52 N ANISOU 514 N MET A 61 2791 3686 5880 -1291 -75 1196 N ATOM 515 CA MET A 61 -5.219 25.005 -25.089 1.00 38.22 C ANISOU 515 CA MET A 61 3406 4749 6367 -1213 77 1393 C ATOM 516 C MET A 61 -5.064 23.690 -24.356 1.00 36.41 C ANISOU 516 C MET A 61 3336 4670 5829 -1171 72 1095 C ATOM 517 O MET A 61 -5.335 22.631 -24.911 1.00 47.53 O ANISOU 517 O MET A 61 4807 6350 6902 -1026 194 1067 O ATOM 518 CB MET A 61 -3.854 25.581 -25.410 1.00 49.24 C ANISOU 518 CB MET A 61 4514 6114 8083 -1322 51 1760 C ATOM 519 CG MET A 61 -3.905 26.546 -26.570 1.00 57.35 C ANISOU 519 CG MET A 61 5321 7142 9329 -1298 149 2204 C ATOM 520 SD MET A 61 -3.774 25.670 -28.126 1.00 69.70 S ANISOU 520 SD MET A 61 6777 9239 10467 -1023 431 2528 S ATOM 521 CE MET A 61 -2.043 25.211 -28.101 1.00 65.94 C ANISOU 521 CE MET A 61 6058 8947 10049 -1068 449 2784 C ATOM 522 N SER A 62 -4.640 23.762 -23.106 1.00 36.41 N ANISOU 522 N SER A 62 3397 4485 5952 -1278 -89 864 N ATOM 523 CA SER A 62 -4.517 22.569 -22.274 1.00 38.91 C ANISOU 523 CA SER A 62 3865 4926 5994 -1234 -97 590 C ATOM 524 C SER A 62 -5.824 21.796 -22.217 1.00 33.08 C ANISOU 524 C SER A 62 3326 4284 4958 -1110 -11 383 C ATOM 525 O SER A 62 -5.838 20.575 -22.365 1.00 40.20 O ANISOU 525 O SER A 62 4287 5396 5591 -1023 68 323 O ATOM 526 CB SER A 62 -4.104 22.952 -20.850 1.00 46.68 C ANISOU 526 CB SER A 62 4907 5681 7149 -1322 -301 339 C ATOM 527 OG SER A 62 -3.091 23.936 -20.870 1.00 49.92 O ANISOU 527 OG SER A 62 5116 5901 7951 -1459 -442 516 O ATOM 528 N ALA A 63 -6.915 22.528 -21.996 1.00 33.16 N ANISOU 528 N ALA A 63 3426 4124 5050 -1100 -45 282 N ATOM 529 CA ALA A 63 -8.250 21.943 -21.871 1.00 32.72 C ANISOU 529 CA ALA A 63 3529 4129 4775 -994 24 110 C ATOM 530 C ALA A 63 -8.697 21.319 -23.191 1.00 28.58 C ANISOU 530 C ALA A 63 2969 3815 4077 -890 159 256 C ATOM 531 O ALA A 63 -9.116 20.149 -23.234 1.00 21.73 O ANISOU 531 O ALA A 63 2176 3090 2990 -806 204 149 O ATOM 532 CB ALA A 63 -9.249 23.002 -21.422 1.00 34.77 C ANISOU 532 CB ALA A 63 3865 4173 5172 -988 -44 1 C ATOM 533 N CYS A 64 -8.590 22.119 -24.250 1.00 24.07 N ANISOU 533 N CYS A 64 2272 3252 3622 -879 204 505 N ATOM 534 CA CYS A 64 -8.967 21.730 -25.600 1.00 27.11 C ANISOU 534 CA CYS A 64 2608 3856 3837 -728 315 656 C ATOM 535 C CYS A 64 -8.263 20.468 -26.056 1.00 25.15 C ANISOU 535 C CYS A 64 2331 3874 3351 -620 354 672 C ATOM 536 O CYS A 64 -8.899 19.513 -26.500 1.00 22.52 O ANISOU 536 O CYS A 64 2071 3679 2805 -479 367 555 O ATOM 537 CB CYS A 64 -8.625 22.846 -26.567 1.00 36.39 C ANISOU 537 CB CYS A 64 3609 5029 5189 -722 366 989 C ATOM 538 SG CYS A 64 -9.061 22.457 -28.260 1.00 47.38 S ANISOU 538 SG CYS A 64 4933 6744 6325 -460 501 1182 S ATOM 539 N ARG A 65 -6.948 20.458 -25.918 1.00 28.07 N ANISOU 539 N ARG A 65 2589 4299 3778 -681 347 804 N ATOM 540 CA ARG A 65 -6.148 19.309 -26.333 1.00 28.93 C ANISOU 540 CA ARG A 65 2663 4674 3656 -561 378 828 C ATOM 541 C ARG A 65 -6.310 18.085 -25.422 1.00 26.84 C ANISOU 541 C ARG A 65 2556 4395 3246 -570 313 527 C ATOM 542 O ARG A 65 -6.385 16.964 -25.907 1.00 30.80 O ANISOU 542 O ARG A 65 3099 5075 3530 -417 312 450 O ATOM 543 CB ARG A 65 -4.684 19.719 -26.514 1.00 41.37 C ANISOU 543 CB ARG A 65 4038 6332 5349 -614 403 1106 C ATOM 544 CG ARG A 65 -4.477 20.553 -27.786 1.00 44.75 C ANISOU 544 CG ARG A 65 4262 6899 5841 -511 511 1495 C ATOM 545 CD ARG A 65 -3.018 20.869 -28.056 1.00 55.44 C ANISOU 545 CD ARG A 65 5367 8376 7321 -543 557 1841 C ATOM 546 NE ARG A 65 -2.144 19.683 -28.111 1.00 63.56 N ANISOU 546 NE ARG A 65 6389 9675 8085 -422 574 1798 N ATOM 547 CZ ARG A 65 -1.858 18.947 -29.196 1.00 66.99 C ANISOU 547 CZ ARG A 65 6762 10493 8197 -131 669 1929 C ATOM 548 NH1 ARG A 65 -2.387 19.220 -30.389 1.00 94.27 N1+ ANISOU 548 NH1 ARG A 65 10155 14146 11517 99 766 2116 N1+ ATOM 549 NH2 ARG A 65 -1.032 17.903 -29.085 1.00 54.83 N ANISOU 549 NH2 ARG A 65 5230 9158 6444 -35 654 1854 N ATOM 550 N GLU A 66 -6.407 18.282 -24.115 1.00 25.54 N ANISOU 550 N GLU A 66 2478 4023 3205 -721 247 357 N ATOM 551 CA GLU A 66 -6.673 17.154 -23.222 1.00 22.18 C ANISOU 551 CA GLU A 66 2186 3593 2650 -713 210 120 C ATOM 552 C GLU A 66 -7.977 16.434 -23.584 1.00 19.03 C ANISOU 552 C GLU A 66 1876 3213 2142 -606 219 6 C ATOM 553 O GLU A 66 -8.001 15.216 -23.639 1.00 20.01 O ANISOU 553 O GLU A 66 2040 3426 2135 -527 192 -86 O ATOM 554 CB GLU A 66 -6.726 17.603 -21.765 1.00 25.67 C ANISOU 554 CB GLU A 66 2701 3841 3211 -832 147 -32 C ATOM 555 CG GLU A 66 -7.121 16.482 -20.802 1.00 30.68 C ANISOU 555 CG GLU A 66 3453 4491 3712 -798 138 -222 C ATOM 556 CD GLU A 66 -6.855 16.813 -19.353 1.00 37.62 C ANISOU 556 CD GLU A 66 4390 5264 4641 -849 78 -359 C ATOM 557 OE1 GLU A 66 -6.552 17.994 -19.045 1.00 42.12 O ANISOU 557 OE1 GLU A 66 4930 5698 5377 -914 5 -360 O ATOM 558 OE2 GLU A 66 -6.963 15.884 -18.519 1.00 28.10 O1- ANISOU 558 OE2 GLU A 66 3253 4106 3315 -805 87 -465 O1- ATOM 559 N ILE A 67 -9.041 17.197 -23.825 1.00 17.26 N ANISOU 559 N ILE A 67 1671 2886 2001 -606 238 14 N ATOM 560 CA ILE A 67 -10.327 16.649 -24.266 1.00 15.92 C ANISOU 560 CA ILE A 67 1555 2721 1773 -509 233 -73 C ATOM 561 C ILE A 67 -10.188 15.936 -25.616 1.00 14.80 C ANISOU 561 C ILE A 67 1364 2777 1481 -329 214 -28 C ATOM 562 O ILE A 67 -10.606 14.800 -25.757 1.00 16.16 O ANISOU 562 O ILE A 67 1576 2982 1582 -240 142 -158 O ATOM 563 CB ILE A 67 -11.409 17.756 -24.377 1.00 20.16 C ANISOU 563 CB ILE A 67 2105 3130 2423 -529 261 -49 C ATOM 564 CG1 ILE A 67 -11.779 18.312 -22.992 1.00 20.05 C ANISOU 564 CG1 ILE A 67 2163 2941 2515 -635 250 -152 C ATOM 565 CG2 ILE A 67 -12.686 17.227 -25.034 1.00 22.44 C ANISOU 565 CG2 ILE A 67 2417 3444 2666 -417 244 -116 C ATOM 566 CD1 ILE A 67 -12.510 19.651 -23.033 1.00 18.43 C ANISOU 566 CD1 ILE A 67 1965 2598 2438 -654 258 -121 C ATOM 567 N ALA A 68 -9.612 16.626 -26.597 1.00 15.96 N ANISOU 567 N ALA A 68 1413 3056 1594 -251 266 164 N ATOM 568 CA ALA A 68 -9.384 16.084 -27.941 1.00 16.15 C ANISOU 568 CA ALA A 68 1381 3333 1423 -6 255 227 C ATOM 569 C ALA A 68 -8.705 14.712 -27.941 1.00 16.67 C ANISOU 569 C ALA A 68 1472 3533 1330 100 175 108 C ATOM 570 O ALA A 68 -9.161 13.805 -28.626 1.00 14.26 O ANISOU 570 O ALA A 68 1200 3318 899 299 72 -27 O ATOM 571 CB ALA A 68 -8.540 17.054 -28.757 1.00 20.64 C ANISOU 571 CB ALA A 68 1799 4059 1982 55 359 531 C ATOM 572 N LEU A 69 -7.609 14.580 -27.195 1.00 15.74 N ANISOU 572 N LEU A 69 1333 3417 1229 -17 197 148 N ATOM 573 CA LEU A 69 -6.825 13.344 -27.201 1.00 15.95 C ANISOU 573 CA LEU A 69 1377 3583 1099 91 129 58 C ATOM 574 C LEU A 69 -7.491 12.242 -26.414 1.00 15.54 C ANISOU 574 C LEU A 69 1441 3368 1094 40 20 -184 C ATOM 575 O LEU A 69 -7.631 11.117 -26.906 1.00 16.81 O ANISOU 575 O LEU A 69 1636 3595 1156 212 -104 -320 O ATOM 576 CB LEU A 69 -5.391 13.586 -26.723 1.00 14.52 C ANISOU 576 CB LEU A 69 1115 3478 922 -6 190 201 C ATOM 577 CG LEU A 69 -4.617 14.390 -27.788 1.00 21.04 C ANISOU 577 CG LEU A 69 1771 4534 1690 114 290 504 C ATOM 578 CD1 LEU A 69 -3.276 14.878 -27.277 1.00 22.88 C ANISOU 578 CD1 LEU A 69 1877 4791 2025 -30 346 695 C ATOM 579 CD2 LEU A 69 -4.407 13.617 -29.086 1.00 23.65 C ANISOU 579 CD2 LEU A 69 2066 5190 1729 466 266 526 C ATOM 580 N LEU A 70 -7.949 12.569 -25.219 1.00 17.99 N ANISOU 580 N LEU A 70 1803 3465 1567 -171 52 -228 N ATOM 581 CA LEU A 70 -8.589 11.580 -24.355 1.00 20.81 C ANISOU 581 CA LEU A 70 2234 3678 1996 -224 -17 -383 C ATOM 582 C LEU A 70 -9.858 11.025 -24.981 1.00 21.50 C ANISOU 582 C LEU A 70 2335 3694 2139 -121 -118 -483 C ATOM 583 O LEU A 70 -10.231 9.891 -24.722 1.00 17.75 O ANISOU 583 O LEU A 70 1879 3134 1729 -98 -228 -591 O ATOM 584 CB LEU A 70 -8.893 12.165 -22.969 1.00 17.76 C ANISOU 584 CB LEU A 70 1884 3130 1734 -409 57 -383 C ATOM 585 CG LEU A 70 -7.698 12.392 -22.040 1.00 21.06 C ANISOU 585 CG LEU A 70 2302 3573 2127 -504 95 -358 C ATOM 586 CD1 LEU A 70 -8.156 13.056 -20.753 1.00 24.24 C ANISOU 586 CD1 LEU A 70 2750 3836 2624 -613 136 -395 C ATOM 587 CD2 LEU A 70 -6.984 11.085 -21.716 1.00 28.31 C ANISOU 587 CD2 LEU A 70 3240 4561 2955 -460 42 -419 C ATOM 588 N ARG A 71 -10.501 11.827 -25.814 1.00 18.76 N ANISOU 588 N ARG A 71 1962 3372 1794 -58 -95 -437 N ATOM 589 CA ARG A 71 -11.684 11.393 -26.509 1.00 19.58 C ANISOU 589 CA ARG A 71 2065 3419 1954 58 -212 -541 C ATOM 590 C ARG A 71 -11.398 10.296 -27.516 1.00 18.88 C ANISOU 590 C ARG A 71 1973 3454 1747 302 -391 -668 C ATOM 591 O ARG A 71 -12.283 9.532 -27.855 1.00 22.51 O ANISOU 591 O ARG A 71 2433 3809 2311 389 -564 -814 O ATOM 592 CB ARG A 71 -12.301 12.589 -27.239 1.00 24.96 C ANISOU 592 CB ARG A 71 2721 4136 2628 99 -139 -454 C ATOM 593 CG ARG A 71 -13.647 12.320 -27.876 1.00 28.54 C ANISOU 593 CG ARG A 71 3167 4516 3160 204 -255 -563 C ATOM 594 CD ARG A 71 -14.671 12.005 -26.797 1.00 27.81 C ANISOU 594 CD ARG A 71 3082 4192 3294 30 -266 -608 C ATOM 595 NE ARG A 71 -15.940 11.702 -27.403 1.00 25.31 N ANISOU 595 NE ARG A 71 2730 3792 3097 117 -397 -700 N ATOM 596 CZ ARG A 71 -16.224 10.574 -28.036 1.00 30.82 C ANISOU 596 CZ ARG A 71 3401 4458 3852 262 -623 -855 C ATOM 597 NH1 ARG A 71 -15.326 9.591 -28.158 1.00 25.48 N1+ ANISOU 597 NH1 ARG A 71 2743 3835 3104 352 -741 -940 N1+ ATOM 598 NH2 ARG A 71 -17.435 10.432 -28.559 1.00 40.31 N ANISOU 598 NH2 ARG A 71 4556 5562 5200 331 -758 -940 N ATOM 599 N GLU A 72 -10.175 10.267 -28.027 1.00 15.48 N ANISOU 599 N GLU A 72 1525 3249 1109 434 -365 -609 N ATOM 600 CA GLU A 72 -9.743 9.277 -28.990 1.00 16.88 C ANISOU 600 CA GLU A 72 1706 3596 1113 727 -537 -737 C ATOM 601 C GLU A 72 -8.974 8.086 -28.385 1.00 17.90 C ANISOU 601 C GLU A 72 1871 3693 1237 716 -636 -838 C ATOM 602 O GLU A 72 -9.117 6.963 -28.857 1.00 16.72 O ANISOU 602 O GLU A 72 1748 3528 1078 910 -864 -1032 O ATOM 603 CB GLU A 72 -8.852 9.959 -30.036 1.00 18.44 C ANISOU 603 CB GLU A 72 1837 4125 1042 947 -434 -572 C ATOM 604 CG GLU A 72 -9.492 11.141 -30.748 1.00 17.66 C ANISOU 604 CG GLU A 72 1688 4090 932 996 -330 -434 C ATOM 605 CD GLU A 72 -10.813 10.813 -31.397 1.00 18.20 C ANISOU 605 CD GLU A 72 1790 4075 1049 1148 -502 -627 C ATOM 606 OE1 GLU A 72 -10.860 9.845 -32.167 1.00 18.31 O ANISOU 606 OE1 GLU A 72 1827 4193 940 1441 -716 -825 O ATOM 607 OE2 GLU A 72 -11.804 11.522 -31.142 1.00 19.85 O1- ANISOU 607 OE2 GLU A 72 2001 4114 1426 991 -444 -596 O1- ATOM 608 N LEU A 73 -8.155 8.329 -27.365 1.00 19.00 N ANISOU 608 N LEU A 73 2010 3816 1392 510 -489 -721 N ATOM 609 CA LEU A 73 -7.255 7.290 -26.845 1.00 21.61 C ANISOU 609 CA LEU A 73 2371 4165 1677 521 -557 -788 C ATOM 610 C LEU A 73 -7.992 6.200 -26.075 1.00 21.49 C ANISOU 610 C LEU A 73 2396 3880 1890 426 -700 -925 C ATOM 611 O LEU A 73 -8.776 6.507 -25.182 1.00 19.42 O ANISOU 611 O LEU A 73 2129 3424 1824 214 -621 -870 O ATOM 612 CB LEU A 73 -6.221 7.900 -25.915 1.00 17.58 C ANISOU 612 CB LEU A 73 1840 3704 1136 328 -373 -631 C ATOM 613 CG LEU A 73 -5.276 8.887 -26.586 1.00 18.93 C ANISOU 613 CG LEU A 73 1925 4125 1143 398 -240 -438 C ATOM 614 CD1 LEU A 73 -4.695 9.804 -25.513 1.00 18.81 C ANISOU 614 CD1 LEU A 73 1878 4034 1237 134 -91 -298 C ATOM 615 CD2 LEU A 73 -4.204 8.161 -27.378 1.00 18.48 C ANISOU 615 CD2 LEU A 73 1837 4347 839 666 -304 -443 C ATOM 616 N LYS A 74 -7.712 4.944 -26.413 1.00 17.36 N ANISOU 616 N LYS A 74 1897 3352 1347 600 -911 -1082 N ATOM 617 CA LYS A 74 -8.314 3.799 -25.743 1.00 24.20 C ANISOU 617 CA LYS A 74 2770 3944 2482 520 -1073 -1178 C ATOM 618 C LYS A 74 -7.239 2.737 -25.550 1.00 19.32 C ANISOU 618 C LYS A 74 2188 3380 1774 618 -1176 -1252 C ATOM 619 O LYS A 74 -6.804 2.120 -26.514 1.00 18.08 O ANISOU 619 O LYS A 74 2055 3346 1468 898 -1369 -1409 O ATOM 620 CB LYS A 74 -9.489 3.262 -26.582 1.00 32.29 C ANISOU 620 CB LYS A 74 3771 4805 3692 661 -1336 -1347 C ATOM 621 CG LYS A 74 -10.312 2.157 -25.930 1.00 39.82 C ANISOU 621 CG LYS A 74 4680 5418 5033 549 -1521 -1393 C ATOM 622 CD LYS A 74 -11.509 1.811 -26.753 0.00 45.93 C ANISOU 622 CD LYS A 74 5403 6011 6038 663 -1790 -1548 C ATOM 623 CE LYS A 74 -12.262 0.627 -26.169 0.00 47.55 C ANISOU 623 CE LYS A 74 5521 5849 6699 553 -2012 -1563 C ATOM 624 NZ LYS A 74 -12.808 0.916 -24.814 0.00 46.39 N1+ ANISOU 624 NZ LYS A 74 5293 5566 6765 243 -1763 -1284 N1+ ATOM 625 N HIS A 75 -6.785 2.563 -24.309 1.00 13.61 N ANISOU 625 N HIS A 75 1470 2591 1109 422 -1047 -1144 N ATOM 626 CA HIS A 75 -5.827 1.499 -23.965 1.00 13.82 C ANISOU 626 CA HIS A 75 1530 2639 1081 492 -1138 -1201 C ATOM 627 C HIS A 75 -5.961 1.211 -22.456 1.00 12.74 C ANISOU 627 C HIS A 75 1378 2329 1132 255 -1021 -1069 C ATOM 628 O HIS A 75 -6.202 2.148 -21.681 1.00 10.31 O ANISOU 628 O HIS A 75 1054 2031 831 75 -803 -927 O ATOM 629 CB HIS A 75 -4.389 1.928 -24.351 1.00 13.35 C ANISOU 629 CB HIS A 75 1489 2913 672 614 -1030 -1167 C ATOM 630 CG HIS A 75 -3.346 0.868 -24.147 1.00 12.88 C ANISOU 630 CG HIS A 75 1466 2919 511 729 -1130 -1240 C ATOM 631 CD2 HIS A 75 -2.938 -0.150 -24.938 1.00 13.78 C ANISOU 631 CD2 HIS A 75 1615 3096 526 1013 -1371 -1420 C ATOM 632 ND1 HIS A 75 -2.577 0.792 -23.007 1.00 13.48 N ANISOU 632 ND1 HIS A 75 1549 3009 565 571 -990 -1138 N ATOM 633 CE1 HIS A 75 -1.747 -0.231 -23.095 1.00 12.77 C ANISOU 633 CE1 HIS A 75 1494 2981 376 730 -1122 -1233 C ATOM 634 NE2 HIS A 75 -1.937 -0.812 -24.266 1.00 15.13 N ANISOU 634 NE2 HIS A 75 1813 3312 625 1004 -1357 -1408 N ATOM 635 N PRO A 76 -5.836 -0.070 -22.038 1.00 14.46 N ANISOU 635 N PRO A 76 1596 2394 1502 282 -1175 -1112 N ATOM 636 CA PRO A 76 -6.006 -0.425 -20.616 1.00 15.10 C ANISOU 636 CA PRO A 76 1644 2336 1758 99 -1056 -946 C ATOM 637 C PRO A 76 -5.085 0.311 -19.641 1.00 14.88 C ANISOU 637 C PRO A 76 1648 2507 1497 -2 -795 -832 C ATOM 638 O PRO A 76 -5.460 0.557 -18.493 1.00 20.91 O ANISOU 638 O PRO A 76 2383 3220 2343 -136 -636 -683 O ATOM 639 CB PRO A 76 -5.687 -1.930 -20.574 1.00 17.57 C ANISOU 639 CB PRO A 76 1957 2499 2221 198 -1287 -1021 C ATOM 640 CG PRO A 76 -5.883 -2.428 -21.957 1.00 19.94 C ANISOU 640 CG PRO A 76 2275 2748 2552 416 -1591 -1255 C ATOM 641 CD PRO A 76 -5.664 -1.271 -22.888 1.00 19.56 C ANISOU 641 CD PRO A 76 2266 2968 2199 511 -1493 -1314 C ATOM 642 N ASN A 77 -3.882 0.618 -20.096 1.00 12.77 N ANISOU 642 N ASN A 77 1429 2474 949 90 -770 -898 N ATOM 643 CA ASN A 77 -2.906 1.371 -19.308 1.00 15.05 C ANISOU 643 CA ASN A 77 1732 2943 1042 4 -572 -817 C ATOM 644 C ASN A 77 -2.904 2.894 -19.414 1.00 13.07 C ANISOU 644 C ASN A 77 1463 2801 702 -85 -417 -758 C ATOM 645 O ASN A 77 -1.994 3.540 -18.890 1.00 13.47 O ANISOU 645 O ASN A 77 1510 2983 623 -143 -306 -715 O ATOM 646 CB ASN A 77 -1.505 0.797 -19.551 1.00 11.44 C ANISOU 646 CB ASN A 77 1303 2668 376 133 -629 -880 C ATOM 647 CG ASN A 77 -1.406 -0.655 -19.141 1.00 10.39 C ANISOU 647 CG ASN A 77 1193 2405 347 199 -768 -923 C ATOM 648 ND2 ASN A 77 -1.869 -0.964 -17.936 1.00 9.85 N ANISOU 648 ND2 ASN A 77 1109 2192 443 76 -691 -810 N ATOM 649 OD1 ASN A 77 -0.922 -1.492 -19.900 1.00 14.27 O ANISOU 649 OD1 ASN A 77 1713 2936 774 382 -948 -1046 O ATOM 650 N VAL A 78 -3.948 3.461 -20.012 1.00 13.65 N ANISOU 650 N VAL A 78 1516 2792 878 -102 -424 -755 N ATOM 651 CA VAL A 78 -4.127 4.904 -20.084 1.00 13.91 C ANISOU 651 CA VAL A 78 1529 2878 879 -192 -292 -690 C ATOM 652 C VAL A 78 -5.510 5.270 -19.551 1.00 15.59 C ANISOU 652 C VAL A 78 1733 2913 1279 -293 -241 -647 C ATOM 653 O VAL A 78 -6.517 4.663 -19.942 1.00 12.83 O ANISOU 653 O VAL A 78 1363 2424 1087 -258 -340 -671 O ATOM 654 CB VAL A 78 -3.984 5.395 -21.536 1.00 15.78 C ANISOU 654 CB VAL A 78 1736 3247 1014 -70 -335 -703 C ATOM 655 CG1 VAL A 78 -3.963 6.915 -21.589 1.00 15.60 C ANISOU 655 CG1 VAL A 78 1673 3271 983 -172 -199 -598 C ATOM 656 CG2 VAL A 78 -2.705 4.839 -22.155 1.00 19.86 C ANISOU 656 CG2 VAL A 78 2243 3975 1327 93 -395 -729 C ATOM 657 N ILE A 79 -5.559 6.282 -18.684 1.00 16.19 N ANISOU 657 N ILE A 79 1813 2993 1344 -398 -106 -590 N ATOM 658 CA ILE A 79 -6.810 6.689 -18.024 1.00 14.65 C ANISOU 658 CA ILE A 79 1609 2676 1283 -459 -35 -537 C ATOM 659 C ILE A 79 -7.858 7.049 -19.074 1.00 14.31 C ANISOU 659 C ILE A 79 1538 2557 1342 -444 -81 -545 C ATOM 660 O ILE A 79 -7.528 7.702 -20.063 1.00 13.90 O ANISOU 660 O ILE A 79 1486 2583 1214 -413 -98 -570 O ATOM 661 CB ILE A 79 -6.564 7.830 -17.003 1.00 15.92 C ANISOU 661 CB ILE A 79 1795 2880 1375 -516 79 -523 C ATOM 662 CG1 ILE A 79 -7.748 7.974 -16.046 1.00 21.77 C ANISOU 662 CG1 ILE A 79 2527 3549 2198 -513 161 -460 C ATOM 663 CG2 ILE A 79 -6.246 9.156 -17.687 1.00 18.65 C ANISOU 663 CG2 ILE A 79 2134 3256 1695 -558 86 -540 C ATOM 664 CD1 ILE A 79 -7.484 8.932 -14.887 1.00 20.54 C ANISOU 664 CD1 ILE A 79 2410 3453 1941 -497 235 -491 C ATOM 665 N SER A 80 -9.086 6.564 -18.874 1.00 15.02 N ANISOU 665 N SER A 80 1587 2506 1613 -454 -102 -502 N ATOM 666 CA SER A 80 -10.187 6.720 -19.822 1.00 15.33 C ANISOU 666 CA SER A 80 1588 2454 1782 -431 -175 -521 C ATOM 667 C SER A 80 -11.075 7.868 -19.410 1.00 20.01 C ANISOU 667 C SER A 80 2174 3022 2408 -491 -47 -456 C ATOM 668 O SER A 80 -11.598 7.873 -18.293 1.00 26.44 O ANISOU 668 O SER A 80 2963 3805 3278 -524 50 -363 O ATOM 669 CB SER A 80 -11.073 5.468 -19.864 1.00 17.90 C ANISOU 669 CB SER A 80 1839 2606 2358 -413 -309 -500 C ATOM 670 OG SER A 80 -10.307 4.295 -20.020 1.00 23.93 O ANISOU 670 OG SER A 80 2612 3354 3126 -350 -447 -563 O ATOM 671 N LEU A 81 -11.272 8.818 -20.321 1.00 21.62 N ANISOU 671 N LEU A 81 2390 3256 2568 -476 -48 -492 N ATOM 672 CA LEU A 81 -12.318 9.827 -20.174 1.00 19.12 C ANISOU 672 CA LEU A 81 2062 2887 2313 -510 34 -448 C ATOM 673 C LEU A 81 -13.687 9.199 -20.368 1.00 16.00 C ANISOU 673 C LEU A 81 1590 2366 2124 -498 -28 -413 C ATOM 674 O LEU A 81 -13.982 8.640 -21.410 1.00 23.96 O ANISOU 674 O LEU A 81 2566 3325 3211 -438 -176 -481 O ATOM 675 CB LEU A 81 -12.120 10.930 -21.195 1.00 20.82 C ANISOU 675 CB LEU A 81 2299 3161 2449 -489 39 -473 C ATOM 676 CG LEU A 81 -13.129 12.071 -21.171 1.00 16.88 C ANISOU 676 CG LEU A 81 1799 2605 2008 -513 110 -439 C ATOM 677 CD1 LEU A 81 -13.015 12.876 -19.883 1.00 17.40 C ANISOU 677 CD1 LEU A 81 1905 2660 2044 -565 211 -420 C ATOM 678 CD2 LEU A 81 -12.871 12.929 -22.383 1.00 14.57 C ANISOU 678 CD2 LEU A 81 1506 2373 1658 -471 98 -432 C ATOM 679 N GLN A 82 -14.509 9.272 -19.344 1.00 18.46 N ANISOU 679 N GLN A 82 1855 2632 2525 -531 71 -304 N ATOM 680 CA GLN A 82 -15.865 8.721 -19.376 1.00 21.95 C ANISOU 680 CA GLN A 82 2179 2951 3210 -535 31 -211 C ATOM 681 C GLN A 82 -16.875 9.760 -19.846 1.00 24.95 C ANISOU 681 C GLN A 82 2549 3318 3612 -526 69 -214 C ATOM 682 O GLN A 82 -17.803 9.426 -20.572 1.00 32.67 O ANISOU 682 O GLN A 82 3445 4194 4773 -515 -39 -218 O ATOM 683 CB GLN A 82 -16.269 8.273 -17.976 1.00 22.30 C ANISOU 683 CB GLN A 82 2143 3001 3330 -544 154 -24 C ATOM 684 CG GLN A 82 -15.345 7.234 -17.357 1.00 30.74 C ANISOU 684 CG GLN A 82 3211 4085 4385 -545 137 13 C ATOM 685 CD GLN A 82 -15.430 5.876 -18.027 1.00 37.07 C ANISOU 685 CD GLN A 82 3928 4721 5435 -562 -66 4 C ATOM 686 NE2 GLN A 82 -14.475 5.004 -17.716 1.00 36.50 N ANISOU 686 NE2 GLN A 82 3880 4655 5332 -553 -113 -6 N ATOM 687 OE1 GLN A 82 -16.346 5.608 -18.812 1.00 44.16 O ANISOU 687 OE1 GLN A 82 4740 5477 6562 -571 -203 -10 O ATOM 688 N LYS A 83 -16.718 11.006 -19.395 1.00 19.17 N ANISOU 688 N LYS A 83 1896 2672 2715 -522 201 -221 N ATOM 689 CA LYS A 83 -17.678 12.048 -19.693 1.00 18.11 C ANISOU 689 CA LYS A 83 1760 2525 2598 -503 247 -215 C ATOM 690 C LYS A 83 -17.049 13.401 -19.504 1.00 17.72 C ANISOU 690 C LYS A 83 1821 2537 2375 -498 318 -280 C ATOM 691 O LYS A 83 -16.068 13.539 -18.793 1.00 15.45 O ANISOU 691 O LYS A 83 1593 2303 1975 -506 348 -309 O ATOM 692 CB LYS A 83 -18.908 11.911 -18.785 1.00 22.35 C ANISOU 692 CB LYS A 83 2193 3048 3252 -478 342 -61 C ATOM 693 CG LYS A 83 -20.242 11.951 -19.517 1.00 31.88 C ANISOU 693 CG LYS A 83 3300 4171 4643 -474 291 -21 C ATOM 694 CD LYS A 83 -21.304 11.103 -18.818 1.00 47.39 C ANISOU 694 CD LYS A 83 5080 6090 6835 -474 327 190 C ATOM 695 CE LYS A 83 -22.594 11.036 -19.621 1.00 53.42 C ANISOU 695 CE LYS A 83 5718 6747 7834 -483 237 223 C ATOM 696 NZ LYS A 83 -23.717 10.486 -18.809 1.00 67.79 N1+ ANISOU 696 NZ LYS A 83 7323 8546 9887 -481 314 493 N1+ ATOM 697 N VAL A 84 -17.632 14.389 -20.165 1.00 15.59 N ANISOU 697 N VAL A 84 1568 2241 2114 -482 322 -302 N ATOM 698 CA VAL A 84 -17.196 15.766 -20.094 1.00 14.51 C ANISOU 698 CA VAL A 84 1513 2109 1890 -482 356 -348 C ATOM 699 C VAL A 84 -18.420 16.569 -19.709 1.00 18.20 C ANISOU 699 C VAL A 84 1978 2550 2388 -426 418 -324 C ATOM 700 O VAL A 84 -19.447 16.438 -20.362 1.00 16.65 O ANISOU 700 O VAL A 84 1720 2326 2280 -408 409 -286 O ATOM 701 CB VAL A 84 -16.688 16.257 -21.452 1.00 17.25 C ANISOU 701 CB VAL A 84 1870 2457 2226 -494 301 -362 C ATOM 702 CG1 VAL A 84 -16.126 17.673 -21.358 1.00 20.22 C ANISOU 702 CG1 VAL A 84 2299 2797 2587 -519 319 -366 C ATOM 703 CG2 VAL A 84 -15.622 15.314 -21.983 1.00 23.79 C ANISOU 703 CG2 VAL A 84 2683 3352 3003 -500 237 -375 C ATOM 704 N PHE A 85 -18.309 17.387 -18.658 1.00 21.42 N ANISOU 704 N PHE A 85 2449 2971 2718 -373 461 -364 N ATOM 705 CA PHE A 85 -19.349 18.346 -18.283 1.00 23.54 C ANISOU 705 CA PHE A 85 2736 3228 2980 -279 505 -369 C ATOM 706 C PHE A 85 -18.863 19.746 -18.554 1.00 24.87 C ANISOU 706 C PHE A 85 2992 3305 3152 -288 442 -463 C ATOM 707 O PHE A 85 -17.786 20.141 -18.096 1.00 30.14 O ANISOU 707 O PHE A 85 3717 3941 3795 -308 380 -543 O ATOM 708 CB PHE A 85 -19.704 18.242 -16.806 1.00 26.85 C ANISOU 708 CB PHE A 85 3157 3751 3293 -140 580 -353 C ATOM 709 CG PHE A 85 -20.282 16.923 -16.430 1.00 25.59 C ANISOU 709 CG PHE A 85 2872 3675 3176 -126 659 -192 C ATOM 710 CD1 PHE A 85 -21.600 16.638 -16.721 1.00 29.37 C ANISOU 710 CD1 PHE A 85 3233 4156 3771 -105 710 -58 C ATOM 711 CD2 PHE A 85 -19.513 15.966 -15.803 1.00 24.37 C ANISOU 711 CD2 PHE A 85 2699 3580 2981 -137 672 -154 C ATOM 712 CE1 PHE A 85 -22.153 15.413 -16.387 1.00 38.63 C ANISOU 712 CE1 PHE A 85 4249 5368 5063 -110 764 132 C ATOM 713 CE2 PHE A 85 -20.052 14.736 -15.467 1.00 29.78 C ANISOU 713 CE2 PHE A 85 3243 4311 3760 -132 736 34 C ATOM 714 CZ PHE A 85 -21.377 14.459 -15.754 1.00 35.11 C ANISOU 714 CZ PHE A 85 3780 4966 4596 -125 777 189 C ATOM 715 N LEU A 86 -19.675 20.489 -19.294 1.00 21.65 N ANISOU 715 N LEU A 86 2579 2839 2806 -272 443 -444 N ATOM 716 CA LEU A 86 -19.427 21.874 -19.561 1.00 17.70 C ANISOU 716 CA LEU A 86 2142 2223 2361 -272 380 -498 C ATOM 717 C LEU A 86 -20.428 22.661 -18.739 1.00 20.81 C ANISOU 717 C LEU A 86 2585 2609 2713 -123 393 -564 C ATOM 718 O LEU A 86 -21.610 22.634 -19.025 1.00 24.18 O ANISOU 718 O LEU A 86 2972 3076 3141 -64 458 -506 O ATOM 719 CB LEU A 86 -19.623 22.132 -21.035 1.00 17.87 C ANISOU 719 CB LEU A 86 2119 2207 2463 -326 379 -411 C ATOM 720 CG LEU A 86 -18.717 21.348 -21.984 1.00 19.92 C ANISOU 720 CG LEU A 86 2324 2525 2721 -406 366 -342 C ATOM 721 CD1 LEU A 86 -19.138 21.642 -23.419 1.00 22.59 C ANISOU 721 CD1 LEU A 86 2615 2878 3089 -378 372 -257 C ATOM 722 CD2 LEU A 86 -17.252 21.726 -21.788 1.00 18.75 C ANISOU 722 CD2 LEU A 86 2188 2332 2603 -483 313 -340 C ATOM 723 N SER A 87 -19.945 23.343 -17.708 1.00 26.03 N ANISOU 723 N SER A 87 3328 3230 3333 -36 315 -697 N ATOM 724 CA SER A 87 -20.784 24.167 -16.840 1.00 30.48 C ANISOU 724 CA SER A 87 3957 3807 3819 169 296 -799 C ATOM 725 C SER A 87 -20.897 25.583 -17.415 1.00 25.93 C ANISOU 725 C SER A 87 3434 3031 3387 163 183 -862 C ATOM 726 O SER A 87 -19.943 26.350 -17.363 1.00 20.56 O ANISOU 726 O SER A 87 2798 2179 2835 110 30 -954 O ATOM 727 CB SER A 87 -20.194 24.185 -15.430 1.00 30.32 C ANISOU 727 CB SER A 87 4004 3852 3664 324 227 -950 C ATOM 728 OG SER A 87 -20.978 24.959 -14.560 1.00 25.84 O ANISOU 728 OG SER A 87 3505 3335 2978 587 193 -1071 O ATOM 729 N HIS A 88 -22.077 25.905 -17.946 1.00 29.25 N ANISOU 729 N HIS A 88 3835 3466 3814 216 252 -797 N ATOM 730 CA HIS A 88 -22.294 27.127 -18.741 1.00 37.79 C ANISOU 730 CA HIS A 88 4945 4363 5049 193 174 -800 C ATOM 731 C HIS A 88 -22.258 28.410 -17.927 1.00 43.23 C ANISOU 731 C HIS A 88 5744 4902 5780 348 3 -994 C ATOM 732 O HIS A 88 -21.733 29.414 -18.411 1.00 50.75 O ANISOU 732 O HIS A 88 6714 5619 6950 269 -137 -1010 O ATOM 733 CB HIS A 88 -23.617 27.055 -19.515 1.00 38.40 C ANISOU 733 CB HIS A 88 4970 4516 5106 227 291 -687 C ATOM 734 CG HIS A 88 -23.538 26.234 -20.764 1.00 40.29 C ANISOU 734 CG HIS A 88 5111 4805 5393 75 369 -531 C ATOM 735 CD2 HIS A 88 -23.852 26.529 -22.046 1.00 34.10 C ANISOU 735 CD2 HIS A 88 4284 3984 4687 29 387 -430 C ATOM 736 ND1 HIS A 88 -23.087 24.932 -20.772 1.00 42.73 N ANISOU 736 ND1 HIS A 88 5356 5226 5653 -8 418 -479 N ATOM 737 CE1 HIS A 88 -23.125 24.459 -22.005 1.00 41.30 C ANISOU 737 CE1 HIS A 88 5105 5070 5516 -86 442 -380 C ATOM 738 NE2 HIS A 88 -23.586 25.408 -22.796 1.00 35.42 N ANISOU 738 NE2 HIS A 88 4370 4255 4834 -55 431 -345 N ATOM 739 N ALA A 89 -22.816 28.373 -16.712 1.00 39.82 N ANISOU 739 N ALA A 89 5371 4607 5152 590 2 -1128 N ATOM 740 CA ALA A 89 -22.836 29.541 -15.800 1.00 43.35 C ANISOU 740 CA ALA A 89 5940 4940 5592 820 -200 -1373 C ATOM 741 C ALA A 89 -21.442 30.091 -15.460 1.00 41.93 C ANISOU 741 C ALA A 89 5809 4527 5594 750 -447 -1537 C ATOM 742 O ALA A 89 -21.172 31.281 -15.659 1.00 37.38 O ANISOU 742 O ALA A 89 5277 3669 5257 740 -661 -1641 O ATOM 743 CB ALA A 89 -23.574 29.193 -14.511 1.00 37.52 C ANISOU 743 CB ALA A 89 5238 4476 4544 1147 -133 -1465 C ATOM 744 N ASP A 90 -20.577 29.205 -14.961 1.00 38.06 N ANISOU 744 N ASP A 90 5295 4145 5020 696 -425 -1545 N ATOM 745 CA ASP A 90 -19.211 29.554 -14.513 1.00 35.91 C ANISOU 745 CA ASP A 90 5049 3689 4906 638 -660 -1703 C ATOM 746 C ASP A 90 -18.112 29.240 -15.541 1.00 33.83 C ANISOU 746 C ASP A 90 4675 3299 4881 299 -639 -1508 C ATOM 747 O ASP A 90 -16.930 29.485 -15.281 1.00 33.86 O ANISOU 747 O ASP A 90 4662 3145 5057 214 -822 -1591 O ATOM 748 CB ASP A 90 -18.887 28.889 -13.140 1.00 36.74 C ANISOU 748 CB ASP A 90 5207 4012 4740 859 -680 -1871 C ATOM 749 CG ASP A 90 -19.080 27.353 -13.130 1.00 33.07 C ANISOU 749 CG ASP A 90 4662 3854 4049 803 -392 -1659 C ATOM 750 OD1 ASP A 90 -19.232 26.752 -14.204 1.00 27.16 O ANISOU 750 OD1 ASP A 90 3821 3117 3383 568 -226 -1424 O ATOM 751 OD2 ASP A 90 -19.093 26.746 -12.035 1.00 31.76 O1- ANISOU 751 OD2 ASP A 90 4520 3919 3630 1019 -347 -1726 O1- ATOM 752 N ARG A 91 -18.497 28.691 -16.695 1.00 35.56 N ANISOU 752 N ARG A 91 4806 3601 5102 134 -428 -1253 N ATOM 753 CA ARG A 91 -17.558 28.355 -17.770 1.00 38.52 C ANISOU 753 CA ARG A 91 5068 3924 5644 -124 -381 -1043 C ATOM 754 C ARG A 91 -16.420 27.401 -17.306 1.00 35.65 C ANISOU 754 C ARG A 91 4674 3661 5210 -201 -380 -1059 C ATOM 755 O ARG A 91 -15.262 27.537 -17.710 1.00 34.23 O ANISOU 755 O ARG A 91 4416 3367 5222 -365 -459 -977 O ATOM 756 CB ARG A 91 -17.005 29.646 -18.408 1.00 42.13 C ANISOU 756 CB ARG A 91 5476 4074 6458 -238 -552 -980 C ATOM 757 CG ARG A 91 -18.052 30.526 -19.108 1.00 50.11 C ANISOU 757 CG ARG A 91 6497 4985 7555 -190 -528 -907 C ATOM 758 CD ARG A 91 -17.891 30.535 -20.628 1.00 58.18 C ANISOU 758 CD ARG A 91 7389 6010 8707 -354 -396 -592 C ATOM 759 NE ARG A 91 -16.531 30.947 -20.998 1.00 60.01 N ANISOU 759 NE ARG A 91 7500 6067 9235 -527 -506 -443 N ATOM 760 CZ ARG A 91 -15.874 30.599 -22.109 1.00 68.94 C ANISOU 760 CZ ARG A 91 8485 7286 10424 -658 -382 -150 C ATOM 761 NH1 ARG A 91 -16.427 29.827 -23.056 1.00 70.16 N1+ ANISOU 761 NH1 ARG A 91 8611 7692 10355 -628 -166 -3 N1+ ATOM 762 NH2 ARG A 91 -14.627 31.041 -22.281 1.00 72.80 N ANISOU 762 NH2 ARG A 91 8840 7615 11207 -800 -491 1 N ATOM 763 N LYS A 92 -16.761 26.437 -16.453 1.00 32.63 N ANISOU 763 N LYS A 92 4335 3500 4561 -74 -284 -1135 N ATOM 764 CA LYS A 92 -15.785 25.463 -15.956 1.00 30.81 C ANISOU 764 CA LYS A 92 4085 3386 4237 -121 -270 -1149 C ATOM 765 C LYS A 92 -15.961 24.173 -16.731 1.00 24.11 C ANISOU 765 C LYS A 92 3158 2715 3286 -231 -64 -948 C ATOM 766 O LYS A 92 -17.070 23.824 -17.115 1.00 24.93 O ANISOU 766 O LYS A 92 3246 2912 3315 -189 67 -862 O ATOM 767 CB LYS A 92 -15.978 25.218 -14.461 1.00 34.77 C ANISOU 767 CB LYS A 92 4672 4025 4514 123 -306 -1346 C ATOM 768 CG LYS A 92 -15.689 26.425 -13.574 1.00 38.32 C ANISOU 768 CG LYS A 92 5213 4306 5041 292 -573 -1617 C ATOM 769 CD LYS A 92 -14.192 26.644 -13.443 1.00 45.57 C ANISOU 769 CD LYS A 92 6100 5057 6157 159 -775 -1701 C ATOM 770 CE LYS A 92 -13.857 27.801 -12.511 1.00 53.72 C ANISOU 770 CE LYS A 92 7215 5885 7309 342 -1107 -2015 C ATOM 771 NZ LYS A 92 -12.378 28.006 -12.439 1.00 54.59 N1+ ANISOU 771 NZ LYS A 92 7260 5805 7677 184 -1326 -2076 N1+ ATOM 772 N VAL A 93 -14.868 23.473 -16.982 1.00 22.83 N ANISOU 772 N VAL A 93 2943 2591 3142 -361 -59 -884 N ATOM 773 CA VAL A 93 -14.951 22.161 -17.616 1.00 23.03 C ANISOU 773 CA VAL A 93 2906 2777 3066 -428 90 -740 C ATOM 774 C VAL A 93 -14.643 21.098 -16.572 1.00 22.03 C ANISOU 774 C VAL A 93 2800 2795 2775 -362 126 -797 C ATOM 775 O VAL A 93 -13.620 21.165 -15.901 1.00 19.05 O ANISOU 775 O VAL A 93 2444 2402 2391 -363 33 -893 O ATOM 776 CB VAL A 93 -13.964 22.033 -18.800 1.00 22.77 C ANISOU 776 CB VAL A 93 2787 2724 3140 -584 85 -598 C ATOM 777 CG1 VAL A 93 -14.072 20.667 -19.459 1.00 26.39 C ANISOU 777 CG1 VAL A 93 3198 3344 3484 -603 191 -502 C ATOM 778 CG2 VAL A 93 -14.223 23.115 -19.841 1.00 23.35 C ANISOU 778 CG2 VAL A 93 2818 2675 3379 -627 66 -490 C ATOM 779 N TRP A 94 -15.529 20.114 -16.453 1.00 20.80 N ANISOU 779 N TRP A 94 2618 2773 2513 -304 253 -721 N ATOM 780 CA TRP A 94 -15.277 18.953 -15.636 1.00 18.49 C ANISOU 780 CA TRP A 94 2312 2619 2096 -255 311 -704 C ATOM 781 C TRP A 94 -15.045 17.727 -16.512 1.00 19.15 C ANISOU 781 C TRP A 94 2320 2741 2215 -375 358 -582 C ATOM 782 O TRP A 94 -15.694 17.568 -17.548 1.00 19.88 O ANISOU 782 O TRP A 94 2365 2803 2385 -424 380 -505 O ATOM 783 CB TRP A 94 -16.449 18.699 -14.713 1.00 16.19 C ANISOU 783 CB TRP A 94 2011 2448 1694 -76 412 -666 C ATOM 784 CG TRP A 94 -16.718 19.770 -13.741 1.00 18.76 C ANISOU 784 CG TRP A 94 2418 2786 1925 120 357 -810 C ATOM 785 CD1 TRP A 94 -17.293 20.977 -13.993 1.00 18.20 C ANISOU 785 CD1 TRP A 94 2394 2608 1914 170 294 -889 C ATOM 786 CD2 TRP A 94 -16.472 19.727 -12.330 1.00 20.73 C ANISOU 786 CD2 TRP A 94 2714 3176 1985 341 344 -907 C ATOM 787 CE2 TRP A 94 -16.911 20.955 -11.795 1.00 25.87 C ANISOU 787 CE2 TRP A 94 3448 3798 2581 538 249 -1073 C ATOM 788 CE3 TRP A 94 -15.940 18.766 -11.464 1.00 20.21 C ANISOU 788 CE3 TRP A 94 2629 3271 1779 422 399 -871 C ATOM 789 NE1 TRP A 94 -17.393 21.702 -12.838 1.00 22.20 N ANISOU 789 NE1 TRP A 94 2983 3163 2290 411 217 -1056 N ATOM 790 CZ2 TRP A 94 -16.833 21.253 -10.417 1.00 26.81 C ANISOU 790 CZ2 TRP A 94 3639 4064 2485 847 191 -1231 C ATOM 791 CZ3 TRP A 94 -15.850 19.066 -10.093 1.00 23.72 C ANISOU 791 CZ3 TRP A 94 3136 3872 2005 716 365 -999 C ATOM 792 CH2 TRP A 94 -16.291 20.298 -9.590 1.00 24.55 C ANISOU 792 CH2 TRP A 94 3328 3962 2036 939 255 -1189 C ATOM 793 N LEU A 95 -14.132 16.859 -16.076 1.00 21.09 N ANISOU 793 N LEU A 95 2561 3055 2397 -396 352 -585 N ATOM 794 CA LEU A 95 -13.862 15.563 -16.729 1.00 23.72 C ANISOU 794 CA LEU A 95 2834 3427 2753 -470 367 -499 C ATOM 795 C LEU A 95 -14.097 14.416 -15.736 1.00 21.58 C ANISOU 795 C LEU A 95 2528 3245 2425 -399 434 -432 C ATOM 796 O LEU A 95 -13.690 14.504 -14.570 1.00 21.98 O ANISOU 796 O LEU A 95 2618 3375 2360 -307 454 -476 O ATOM 797 CB LEU A 95 -12.415 15.498 -17.241 1.00 21.74 C ANISOU 797 CB LEU A 95 2589 3179 2491 -556 296 -532 C ATOM 798 CG LEU A 95 -11.930 16.652 -18.114 1.00 20.02 C ANISOU 798 CG LEU A 95 2367 2888 2352 -623 240 -534 C ATOM 799 CD1 LEU A 95 -10.465 16.462 -18.477 1.00 21.62 C ANISOU 799 CD1 LEU A 95 2536 3133 2544 -690 191 -513 C ATOM 800 CD2 LEU A 95 -12.757 16.775 -19.376 1.00 24.27 C ANISOU 800 CD2 LEU A 95 2866 3405 2950 -625 261 -458 C ATOM 801 N LEU A 96 -14.726 13.341 -16.210 1.00 14.99 N ANISOU 801 N LEU A 96 1610 2396 1691 -428 451 -322 N ATOM 802 CA LEU A 96 -15.042 12.185 -15.386 1.00 16.93 C ANISOU 802 CA LEU A 96 1780 2694 1958 -378 512 -193 C ATOM 803 C LEU A 96 -14.129 11.017 -15.733 1.00 14.74 C ANISOU 803 C LEU A 96 1487 2401 1712 -444 441 -194 C ATOM 804 O LEU A 96 -13.995 10.680 -16.892 1.00 18.17 O ANISOU 804 O LEU A 96 1910 2764 2229 -507 342 -237 O ATOM 805 CB LEU A 96 -16.501 11.783 -15.605 1.00 17.67 C ANISOU 805 CB LEU A 96 1752 2737 2223 -367 551 -42 C ATOM 806 CG LEU A 96 -17.079 10.633 -14.790 1.00 21.14 C ANISOU 806 CG LEU A 96 2053 3209 2769 -321 626 177 C ATOM 807 CD1 LEU A 96 -17.051 10.968 -13.308 1.00 23.73 C ANISOU 807 CD1 LEU A 96 2396 3720 2901 -153 770 250 C ATOM 808 CD2 LEU A 96 -18.506 10.334 -15.249 1.00 19.96 C ANISOU 808 CD2 LEU A 96 1753 2969 2863 -344 626 329 C ATOM 809 N PHE A 97 -13.521 10.398 -14.724 1.00 14.31 N ANISOU 809 N PHE A 97 1435 2430 1573 -394 484 -153 N ATOM 810 CA PHE A 97 -12.719 9.167 -14.901 1.00 15.06 C ANISOU 810 CA PHE A 97 1509 2509 1703 -435 419 -137 C ATOM 811 C PHE A 97 -13.099 8.120 -13.867 1.00 14.52 C ANISOU 811 C PHE A 97 1345 2476 1694 -370 499 55 C ATOM 812 O PHE A 97 -13.718 8.437 -12.845 1.00 23.70 O ANISOU 812 O PHE A 97 2472 3739 2794 -260 629 171 O ATOM 813 CB PHE A 97 -11.215 9.461 -14.738 1.00 12.96 C ANISOU 813 CB PHE A 97 1340 2323 1260 -443 382 -275 C ATOM 814 CG PHE A 97 -10.734 10.691 -15.467 1.00 10.58 C ANISOU 814 CG PHE A 97 1103 2007 911 -495 331 -403 C ATOM 815 CD1 PHE A 97 -10.353 10.622 -16.781 1.00 10.60 C ANISOU 815 CD1 PHE A 97 1098 1977 954 -554 250 -438 C ATOM 816 CD2 PHE A 97 -10.629 11.912 -14.812 1.00 18.02 C ANISOU 816 CD2 PHE A 97 2099 2973 1774 -457 353 -479 C ATOM 817 CE1 PHE A 97 -9.879 11.740 -17.448 1.00 13.05 C ANISOU 817 CE1 PHE A 97 1430 2287 1242 -593 224 -488 C ATOM 818 CE2 PHE A 97 -10.164 13.050 -15.472 1.00 16.58 C ANISOU 818 CE2 PHE A 97 1946 2738 1616 -520 290 -560 C ATOM 819 CZ PHE A 97 -9.783 12.957 -16.800 1.00 15.89 C ANISOU 819 CZ PHE A 97 1826 2627 1583 -598 243 -535 C ATOM 820 N ASP A 98 -12.720 6.874 -14.124 1.00 14.42 N ANISOU 820 N ASP A 98 1285 2393 1801 -412 419 103 N ATOM 821 CA ASP A 98 -12.717 5.846 -13.084 1.00 14.42 C ANISOU 821 CA ASP A 98 1198 2433 1849 -351 493 301 C ATOM 822 C ASP A 98 -11.656 6.217 -12.023 1.00 12.82 C ANISOU 822 C ASP A 98 1095 2424 1353 -249 578 233 C ATOM 823 O ASP A 98 -10.600 6.744 -12.339 1.00 11.76 O ANISOU 823 O ASP A 98 1078 2325 1064 -280 510 28 O ATOM 824 CB ASP A 98 -12.442 4.449 -13.665 1.00 16.00 C ANISOU 824 CB ASP A 98 1335 2477 2266 -418 344 334 C ATOM 825 CG ASP A 98 -13.664 3.821 -14.351 1.00 17.86 C ANISOU 825 CG ASP A 98 1420 2500 2867 -481 238 451 C ATOM 826 OD1 ASP A 98 -14.777 4.380 -14.301 1.00 20.35 O ANISOU 826 OD1 ASP A 98 1657 2805 3269 -480 312 553 O ATOM 827 OD2 ASP A 98 -13.500 2.739 -14.946 1.00 21.69 O1- ANISOU 827 OD2 ASP A 98 1858 2816 3566 -520 55 429 O1- ATOM 828 N TYR A 99 -11.982 5.972 -10.767 1.00 15.49 N ANISOU 828 N TYR A 99 1367 2897 1622 -108 723 423 N ATOM 829 CA TYR A 99 -11.170 6.404 -9.642 1.00 16.74 C ANISOU 829 CA TYR A 99 1613 3265 1484 50 795 349 C ATOM 830 C TYR A 99 -10.061 5.383 -9.396 1.00 15.27 C ANISOU 830 C TYR A 99 1441 3100 1260 43 756 354 C ATOM 831 O TYR A 99 -10.338 4.203 -9.238 1.00 15.46 O ANISOU 831 O TYR A 99 1349 3070 1456 37 783 579 O ATOM 832 CB TYR A 99 -12.047 6.519 -8.403 1.00 18.96 C ANISOU 832 CB TYR A 99 1804 3734 1666 273 977 571 C ATOM 833 CG TYR A 99 -11.302 6.869 -7.149 1.00 22.67 C ANISOU 833 CG TYR A 99 2355 4451 1807 508 1037 492 C ATOM 834 CD1 TYR A 99 -10.741 8.138 -6.970 1.00 22.97 C ANISOU 834 CD1 TYR A 99 2547 4551 1630 582 951 184 C ATOM 835 CD2 TYR A 99 -11.163 5.938 -6.126 1.00 26.72 C ANISOU 835 CD2 TYR A 99 2781 5129 2241 676 1160 726 C ATOM 836 CE1 TYR A 99 -10.061 8.466 -5.813 1.00 25.14 C ANISOU 836 CE1 TYR A 99 2897 5041 1615 828 956 67 C ATOM 837 CE2 TYR A 99 -10.492 6.256 -4.957 1.00 29.79 C ANISOU 837 CE2 TYR A 99 3247 5774 2297 940 1203 636 C ATOM 838 CZ TYR A 99 -9.935 7.514 -4.805 1.00 32.13 C ANISOU 838 CZ TYR A 99 3707 6124 2378 1020 1086 283 C ATOM 839 OH TYR A 99 -9.280 7.807 -3.630 1.00 38.27 O ANISOU 839 OH TYR A 99 4558 7148 2837 1312 1085 159 O ATOM 840 N ALA A 100 -8.816 5.854 -9.392 1.00 17.14 N ANISOU 840 N ALA A 100 1631 2710 2174 5 1365 -240 N ATOM 841 CA ALA A 100 -7.635 5.052 -9.060 1.00 14.41 C ANISOU 841 CA ALA A 100 1418 2476 1582 -66 1263 -203 C ATOM 842 C ALA A 100 -7.253 5.297 -7.610 1.00 17.13 C ANISOU 842 C ALA A 100 1827 2972 1710 -146 1402 -328 C ATOM 843 O ALA A 100 -6.754 6.374 -7.259 1.00 16.94 O ANISOU 843 O ALA A 100 1842 2938 1658 -152 1478 -500 O ATOM 844 CB ALA A 100 -6.495 5.421 -9.965 1.00 12.86 C ANISOU 844 CB ALA A 100 1297 2208 1383 -37 1116 -207 C ATOM 845 N GLU A 101 -7.498 4.302 -6.758 1.00 19.51 N ANISOU 845 N GLU A 101 2132 3422 1858 -219 1437 -242 N ATOM 846 CA GLU A 101 -7.175 4.420 -5.328 1.00 20.19 C ANISOU 846 CA GLU A 101 2274 3711 1686 -320 1561 -334 C ATOM 847 C GLU A 101 -5.722 4.764 -5.053 1.00 17.12 C ANISOU 847 C GLU A 101 2002 3401 1101 -368 1477 -407 C ATOM 848 O GLU A 101 -5.460 5.423 -4.075 1.00 19.82 O ANISOU 848 O GLU A 101 2379 3878 1274 -442 1594 -575 O ATOM 849 CB GLU A 101 -7.548 3.147 -4.557 1.00 21.63 C ANISOU 849 CB GLU A 101 2441 4054 1724 -397 1578 -159 C ATOM 850 CG GLU A 101 -7.572 3.300 -3.037 1.00 23.88 C ANISOU 850 CG GLU A 101 2751 4591 1734 -514 1741 -241 C ATOM 851 CD GLU A 101 -8.766 4.081 -2.543 1.00 29.01 C ANISOU 851 CD GLU A 101 3311 5244 2467 -513 1986 -417 C ATOM 852 OE1 GLU A 101 -9.891 3.541 -2.582 1.00 31.65 O ANISOU 852 OE1 GLU A 101 3545 5550 2931 -496 2060 -315 O ATOM 853 OE2 GLU A 101 -8.584 5.240 -2.108 1.00 37.66 O1- ANISOU 853 OE2 GLU A 101 4425 6363 3521 -534 2115 -669 O1- ATOM 854 N HIS A 102 -4.791 4.354 -5.924 1.00 20.13 N ANISOU 854 N HIS A 102 2434 3703 1510 -334 1282 -303 N ATOM 855 CA HIS A 102 -3.344 4.497 -5.660 1.00 18.45 C ANISOU 855 CA HIS A 102 2319 3575 1117 -384 1183 -337 C ATOM 856 C HIS A 102 -2.542 5.176 -6.764 1.00 21.30 C ANISOU 856 C HIS A 102 2713 3770 1612 -317 1077 -396 C ATOM 857 O HIS A 102 -3.043 5.418 -7.862 1.00 17.71 O ANISOU 857 O HIS A 102 2209 3141 1377 -230 1051 -374 O ATOM 858 CB HIS A 102 -2.765 3.114 -5.381 1.00 16.93 C ANISOU 858 CB HIS A 102 2150 3493 790 -432 1053 -117 C ATOM 859 CG HIS A 102 -3.485 2.388 -4.287 1.00 18.60 C ANISOU 859 CG HIS A 102 2325 3880 862 -508 1149 -13 C ATOM 860 CD2 HIS A 102 -4.314 1.321 -4.312 1.00 17.86 C ANISOU 860 CD2 HIS A 102 2165 3770 849 -504 1157 170 C ATOM 861 ND1 HIS A 102 -3.433 2.803 -2.980 1.00 21.95 N ANISOU 861 ND1 HIS A 102 2774 4537 1031 -613 1267 -110 N ATOM 862 CE1 HIS A 102 -4.177 2.003 -2.237 1.00 28.55 C ANISOU 862 CE1 HIS A 102 3562 5506 1777 -670 1343 31 C ATOM 863 NE2 HIS A 102 -4.722 1.095 -3.023 1.00 27.47 N ANISOU 863 NE2 HIS A 102 3369 5209 1859 -601 1278 208 N ATOM 864 N ASP A 103 -1.289 5.490 -6.456 1.00 20.69 N ANISOU 864 N ASP A 103 2708 3766 1389 -367 1013 -460 N ATOM 865 CA ASP A 103 -0.358 6.004 -7.447 1.00 19.25 C ANISOU 865 CA ASP A 103 2559 3448 1309 -318 905 -491 C ATOM 866 C ASP A 103 1.048 5.764 -6.982 1.00 19.54 C ANISOU 866 C ASP A 103 2660 3609 1155 -388 799 -480 C ATOM 867 O ASP A 103 1.279 5.474 -5.811 1.00 26.88 O ANISOU 867 O ASP A 103 3607 4742 1863 -481 820 -480 O ATOM 868 CB ASP A 103 -0.580 7.490 -7.654 1.00 21.06 C ANISOU 868 CB ASP A 103 2770 3552 1679 -287 1019 -689 C ATOM 869 CG ASP A 103 -0.391 8.280 -6.386 1.00 27.66 C ANISOU 869 CG ASP A 103 3629 4518 2363 -381 1155 -904 C ATOM 870 OD1 ASP A 103 0.789 8.451 -5.973 1.00 24.03 O ANISOU 870 OD1 ASP A 103 3230 4159 1743 -454 1090 -970 O ATOM 871 OD2 ASP A 103 -1.413 8.729 -5.806 1.00 23.05 O1- ANISOU 871 OD2 ASP A 103 2994 3945 1821 -390 1332 -1021 O1- ATOM 872 N LEU A 104 1.998 5.918 -7.887 1.00 19.14 N ANISOU 872 N LEU A 104 2635 3454 1184 -351 684 -465 N ATOM 873 CA LEU A 104 3.373 5.600 -7.544 1.00 20.52 C ANISOU 873 CA LEU A 104 2849 3733 1213 -409 568 -431 C ATOM 874 C LEU A 104 4.072 6.604 -6.611 1.00 22.68 C ANISOU 874 C LEU A 104 3156 4129 1330 -501 616 -622 C ATOM 875 O LEU A 104 4.996 6.223 -5.896 1.00 28.17 O ANISOU 875 O LEU A 104 3868 4995 1839 -580 531 -580 O ATOM 876 CB LEU A 104 4.191 5.312 -8.792 1.00 19.63 C ANISOU 876 CB LEU A 104 2741 3482 1234 -347 440 -351 C ATOM 877 CG LEU A 104 3.826 4.041 -9.540 1.00 21.25 C ANISOU 877 CG LEU A 104 2913 3619 1543 -295 369 -173 C ATOM 878 CD1 LEU A 104 4.875 3.799 -10.619 1.00 23.34 C ANISOU 878 CD1 LEU A 104 3184 3786 1898 -260 258 -137 C ATOM 879 CD2 LEU A 104 3.732 2.822 -8.633 1.00 30.74 C ANISOU 879 CD2 LEU A 104 4093 4950 2638 -340 340 -17 C ATOM 880 N TRP A 105 3.631 7.858 -6.580 1.00 22.43 N ANISOU 880 N TRP A 105 3122 4017 1385 -498 750 -830 N ATOM 881 CA TRP A 105 4.163 8.803 -5.595 1.00 23.23 C ANISOU 881 CA TRP A 105 3244 4239 1343 -607 823 -1057 C ATOM 882 C TRP A 105 3.888 8.294 -4.168 1.00 27.21 C ANISOU 882 C TRP A 105 3753 5028 1557 -723 872 -1065 C ATOM 883 O TRP A 105 4.805 8.209 -3.349 1.00 27.41 O ANISOU 883 O TRP A 105 3800 5266 1347 -835 803 -1091 O ATOM 884 CB TRP A 105 3.567 10.191 -5.787 1.00 22.64 C ANISOU 884 CB TRP A 105 3144 3992 1466 -579 992 -1286 C ATOM 885 CG TRP A 105 4.260 11.203 -5.020 1.00 23.70 C ANISOU 885 CG TRP A 105 3295 4198 1511 -689 1059 -1545 C ATOM 886 CD1 TRP A 105 5.340 11.902 -5.416 1.00 22.02 C ANISOU 886 CD1 TRP A 105 3097 3898 1372 -707 999 -1631 C ATOM 887 CD2 TRP A 105 3.945 11.647 -3.693 1.00 24.42 C ANISOU 887 CD2 TRP A 105 3384 4478 1414 -815 1209 -1777 C ATOM 888 CE2 TRP A 105 4.881 12.634 -3.360 1.00 27.61 C ANISOU 888 CE2 TRP A 105 3802 4894 1794 -910 1227 -2016 C ATOM 889 CE3 TRP A 105 2.962 11.304 -2.760 1.00 28.94 C ANISOU 889 CE3 TRP A 105 3941 5222 1832 -867 1338 -1814 C ATOM 890 NE1 TRP A 105 5.726 12.768 -4.435 1.00 28.28 N ANISOU 890 NE1 TRP A 105 3894 4799 2053 -837 1095 -1910 N ATOM 891 CZ2 TRP A 105 4.883 13.280 -2.121 1.00 28.09 C ANISOU 891 CZ2 TRP A 105 3862 5143 1667 -1064 1366 -2314 C ATOM 892 CZ3 TRP A 105 2.947 11.952 -1.532 1.00 30.26 C ANISOU 892 CZ3 TRP A 105 4110 5584 1802 -1016 1486 -2100 C ATOM 893 CH2 TRP A 105 3.901 12.931 -1.225 1.00 34.06 C ANISOU 893 CH2 TRP A 105 4607 6083 2252 -1117 1498 -2358 C ATOM 894 N HIS A 106 2.630 7.942 -3.904 1.00 25.40 N ANISOU 894 N HIS A 106 3493 4816 1342 -700 985 -1023 N ATOM 895 CA HIS A 106 2.220 7.405 -2.605 1.00 26.19 C ANISOU 895 CA HIS A 106 3589 5193 1167 -810 1050 -1000 C ATOM 896 C HIS A 106 2.750 6.005 -2.313 1.00 25.37 C ANISOU 896 C HIS A 106 3487 5255 896 -841 882 -704 C ATOM 897 O HIS A 106 3.120 5.735 -1.185 1.00 27.15 O ANISOU 897 O HIS A 106 3721 5765 830 -968 865 -678 O ATOM 898 CB HIS A 106 0.697 7.432 -2.455 1.00 26.43 C ANISOU 898 CB HIS A 106 3571 5179 1293 -774 1233 -1034 C ATOM 899 CG HIS A 106 0.153 8.798 -2.173 1.00 30.31 C ANISOU 899 CG HIS A 106 4040 5599 1879 -791 1444 -1354 C ATOM 900 CD2 HIS A 106 0.251 9.582 -1.076 1.00 30.80 C ANISOU 900 CD2 HIS A 106 4112 5837 1755 -923 1590 -1628 C ATOM 901 ND1 HIS A 106 -0.563 9.525 -3.097 1.00 29.00 N ANISOU 901 ND1 HIS A 106 3823 5144 2053 -669 1530 -1424 N ATOM 902 CE1 HIS A 106 -0.891 10.692 -2.576 1.00 28.20 C ANISOU 902 CE1 HIS A 106 3694 5012 2010 -711 1728 -1720 C ATOM 903 NE2 HIS A 106 -0.411 10.750 -1.350 1.00 29.79 N ANISOU 903 NE2 HIS A 106 3935 5493 1892 -870 1776 -1871 N ATOM 904 N ILE A 107 2.788 5.124 -3.316 1.00 26.20 N ANISOU 904 N ILE A 107 3576 5188 1190 -734 763 -481 N ATOM 905 CA ILE A 107 3.328 3.760 -3.130 1.00 24.22 C ANISOU 905 CA ILE A 107 3306 5037 858 -749 609 -192 C ATOM 906 C ILE A 107 4.822 3.809 -2.785 1.00 23.41 C ANISOU 906 C ILE A 107 3221 5067 606 -817 463 -172 C ATOM 907 O ILE A 107 5.235 3.252 -1.770 1.00 25.47 O ANISOU 907 O ILE A 107 3465 5582 631 -917 400 -36 O ATOM 908 CB ILE A 107 3.020 2.844 -4.347 1.00 22.82 C ANISOU 908 CB ILE A 107 3098 4621 953 -625 536 -10 C ATOM 909 CG1 ILE A 107 1.600 2.286 -4.222 1.00 22.37 C ANISOU 909 CG1 ILE A 107 2998 4545 959 -605 645 72 C ATOM 910 CG2 ILE A 107 3.994 1.674 -4.475 1.00 21.05 C ANISOU 910 CG2 ILE A 107 2848 4408 743 -620 365 232 C ATOM 911 CD1 ILE A 107 1.031 1.817 -5.535 1.00 23.70 C ANISOU 911 CD1 ILE A 107 3131 4462 1411 -493 616 138 C ATOM 912 N ILE A 108 5.612 4.509 -3.594 1.00 22.19 N ANISOU 912 N ILE A 108 3089 4757 585 -772 410 -297 N ATOM 913 CA ILE A 108 7.058 4.625 -3.340 1.00 23.61 C ANISOU 913 CA ILE A 108 3269 5045 654 -835 271 -292 C ATOM 914 C ILE A 108 7.348 5.300 -1.994 1.00 27.29 C ANISOU 914 C ILE A 108 3750 5809 810 -996 311 -452 C ATOM 915 O ILE A 108 8.216 4.842 -1.258 1.00 34.50 O ANISOU 915 O ILE A 108 4637 6951 1519 -1087 182 -326 O ATOM 916 CB ILE A 108 7.798 5.324 -4.506 1.00 20.14 C ANISOU 916 CB ILE A 108 2846 4376 430 -761 230 -408 C ATOM 917 CG1 ILE A 108 7.817 4.404 -5.723 1.00 18.35 C ANISOU 917 CG1 ILE A 108 2595 3937 439 -637 153 -220 C ATOM 918 CG2 ILE A 108 9.229 5.688 -4.131 1.00 22.79 C ANISOU 918 CG2 ILE A 108 3176 4835 650 -844 116 -458 C ATOM 919 CD1 ILE A 108 8.140 5.109 -7.030 1.00 19.17 C ANISOU 919 CD1 ILE A 108 2716 3808 759 -557 156 -330 C ATOM 920 N LYS A 109 6.617 6.366 -1.674 1.00 27.25 N ANISOU 920 N LYS A 109 3773 5807 775 -1036 490 -728 N ATOM 921 CA LYS A 109 6.802 7.080 -0.408 1.00 27.79 C ANISOU 921 CA LYS A 109 3853 6160 545 -1206 561 -945 C ATOM 922 C LYS A 109 6.426 6.217 0.811 1.00 33.01 C ANISOU 922 C LYS A 109 4494 7161 886 -1318 559 -776 C ATOM 923 O LYS A 109 6.991 6.396 1.892 1.00 36.16 O ANISOU 923 O LYS A 109 4890 7885 963 -1483 523 -841 O ATOM 924 CB LYS A 109 6.028 8.412 -0.410 1.00 28.77 C ANISOU 924 CB LYS A 109 3996 6163 774 -1214 786 -1301 C ATOM 925 CG LYS A 109 6.320 9.327 0.780 1.00 32.86 C ANISOU 925 CG LYS A 109 4522 6940 1021 -1402 881 -1612 C ATOM 926 CD LYS A 109 5.816 10.712 0.610 0.00 34.73 C ANISOU 926 CD LYS A 109 4760 6982 1453 -1396 1093 -1979 C ATOM 927 CE LYS A 109 6.147 11.571 1.821 0.00 37.96 C ANISOU 927 CE LYS A 109 5173 7659 1592 -1604 1197 -2326 C ATOM 928 NZ LYS A 109 5.698 12.981 1.664 0.00 38.82 N1+ ANISOU 928 NZ LYS A 109 5265 7537 1949 -1600 1424 -2713 N1+ ATOM 929 N PHE A 110 5.484 5.288 0.646 1.00 35.23 N ANISOU 929 N PHE A 110 4755 7384 1247 -1242 593 -555 N ATOM 930 CA PHE A 110 5.153 4.317 1.709 1.00 41.25 C ANISOU 930 CA PHE A 110 5487 8448 1738 -1338 578 -320 C ATOM 931 C PHE A 110 6.305 3.340 1.948 1.00 43.72 C ANISOU 931 C PHE A 110 5758 8909 1947 -1371 341 0 C ATOM 932 O PHE A 110 6.638 3.023 3.087 1.00 49.80 O ANISOU 932 O PHE A 110 6501 10036 2384 -1518 282 118 O ATOM 933 CB PHE A 110 3.890 3.536 1.351 1.00 42.49 C ANISOU 933 CB PHE A 110 5619 8458 2069 -1240 670 -149 C ATOM 934 CG PHE A 110 3.411 2.610 2.435 1.00 44.84 C ANISOU 934 CG PHE A 110 5878 9047 2111 -1341 688 91 C ATOM 935 CD1 PHE A 110 2.737 3.111 3.546 1.00 53.00 C ANISOU 935 CD1 PHE A 110 6921 10362 2853 -1481 866 -79 C ATOM 936 CD2 PHE A 110 3.603 1.232 2.335 1.00 46.80 C ANISOU 936 CD2 PHE A 110 6072 9281 2428 -1299 545 489 C ATOM 937 CE1 PHE A 110 2.279 2.259 4.542 1.00 58.06 C ANISOU 937 CE1 PHE A 110 7524 11295 3242 -1584 891 163 C ATOM 938 CE2 PHE A 110 3.143 0.374 3.329 1.00 52.95 C ANISOU 938 CE2 PHE A 110 6805 10322 2993 -1394 565 748 C ATOM 939 CZ PHE A 110 2.482 0.889 4.433 1.00 55.38 C ANISOU 939 CZ PHE A 110 7128 10936 2976 -1539 735 595 C ATOM 940 N HIS A 111 6.905 2.866 0.863 1.00 43.15 N ANISOU 940 N HIS A 111 5667 8567 2163 -1237 208 144 N ATOM 941 CA HIS A 111 8.063 1.983 0.955 1.00 42.92 C ANISOU 941 CA HIS A 111 5575 8616 2116 -1245 -10 435 C ATOM 942 C HIS A 111 9.291 2.707 1.503 1.00 42.70 C ANISOU 942 C HIS A 111 5544 8805 1874 -1366 -117 304 C ATOM 943 O HIS A 111 10.030 2.153 2.318 1.00 48.87 O ANISOU 943 O HIS A 111 6264 9863 2443 -1464 -268 525 O ATOM 944 CB HIS A 111 8.355 1.338 -0.406 1.00 39.99 C ANISOU 944 CB HIS A 111 5179 7884 2132 -1073 -90 570 C ATOM 945 CG HIS A 111 7.459 0.178 -0.721 1.00 40.48 C ANISOU 945 CG HIS A 111 5202 7806 2372 -989 -58 812 C ATOM 946 CD2 HIS A 111 6.408 0.062 -1.565 1.00 43.72 C ANISOU 946 CD2 HIS A 111 5632 7967 3015 -886 55 755 C ATOM 947 ND1 HIS A 111 7.602 -1.055 -0.118 1.00 46.63 N ANISOU 947 ND1 HIS A 111 5900 8706 3111 -1017 -153 1169 N ATOM 948 CE1 HIS A 111 6.685 -1.882 -0.585 1.00 50.69 C ANISOU 948 CE1 HIS A 111 6389 9032 3840 -936 -89 1303 C ATOM 949 NE2 HIS A 111 5.950 -1.230 -1.467 1.00 49.59 N ANISOU 949 NE2 HIS A 111 6309 8676 3856 -859 32 1049 N ATOM 950 N ARG A 112 9.489 3.950 1.077 1.00 42.10 N ANISOU 950 N ARG A 112 5523 8610 1862 -1366 -42 -44 N ATOM 951 CA ARG A 112 10.563 4.780 1.616 1.00 44.66 C ANISOU 951 CA ARG A 112 5844 9134 1993 -1499 -117 -230 C ATOM 952 C ARG A 112 10.361 5.113 3.109 1.00 48.88 C ANISOU 952 C ARG A 112 6381 10103 2089 -1711 -66 -340 C ATOM 953 O ARG A 112 11.340 5.366 3.807 1.00 51.43 O ANISOU 953 O ARG A 112 6670 10700 2170 -1855 -190 -374 O ATOM 954 CB ARG A 112 10.749 6.061 0.786 1.00 49.05 C ANISOU 954 CB ARG A 112 6449 9428 2760 -1452 -26 -578 C ATOM 955 CG ARG A 112 12.121 6.692 0.971 1.00 52.41 C ANISOU 955 CG ARG A 112 6848 9961 3106 -1550 -152 -703 C ATOM 956 CD ARG A 112 12.297 8.010 0.244 1.00 49.83 C ANISOU 956 CD ARG A 112 6561 9382 2992 -1522 -47 -1042 C ATOM 957 NE ARG A 112 13.558 8.643 0.649 1.00 60.84 N ANISOU 957 NE ARG A 112 7920 10929 4266 -1655 -156 -1186 N ATOM 958 CZ ARG A 112 14.103 9.721 0.080 1.00 70.14 C ANISOU 958 CZ ARG A 112 9108 11915 5628 -1655 -115 -1439 C ATOM 959 NH1 ARG A 112 13.516 10.333 -0.951 1.00 78.01 N1+ ANISOU 959 NH1 ARG A 112 10146 12556 6938 -1524 29 -1560 N1+ ATOM 960 NH2 ARG A 112 15.262 10.190 0.539 1.00 66.94 N ANISOU 960 NH2 ARG A 112 8657 11680 5099 -1793 -227 -1554 N ATOM 961 N ALA A 113 9.114 5.097 3.592 1.00 50.80 N ANISOU 961 N ALA A 113 6655 10424 2223 -1739 115 -398 N ATOM 962 CA ALA A 113 8.823 5.266 5.025 1.00 58.43 C ANISOU 962 CA ALA A 113 7619 11835 2745 -1949 184 -480 C ATOM 963 C ALA A 113 9.399 4.137 5.893 1.00 67.62 C ANISOU 963 C ALA A 113 8708 13360 3623 -2049 -18 -71 C ATOM 964 O ALA A 113 9.590 4.317 7.096 1.00 76.05 O ANISOU 964 O ALA A 113 9761 14869 4267 -2258 -33 -116 O ATOM 965 CB ALA A 113 7.324 5.410 5.264 1.00 60.44 C ANISOU 965 CB ALA A 113 7909 12069 2988 -1942 437 -607 C ATOM 966 N SER A 114 9.656 2.981 5.283 1.00 67.25 N ANISOU 966 N SER A 114 8606 13129 3816 -1908 -167 328 N ATOM 967 CA SER A 114 10.469 1.928 5.889 1.00 73.57 C ANISOU 967 CA SER A 114 9307 14186 4461 -1968 -397 754 C ATOM 968 C SER A 114 11.934 2.138 5.510 1.00 66.63 C ANISOU 968 C SER A 114 8376 13261 3678 -1958 -604 760 C ATOM 969 O SER A 114 12.777 2.383 6.370 1.00 70.61 O ANISOU 969 O SER A 114 8832 14127 3868 -2126 -738 765 O ATOM 970 CB SER A 114 10.000 0.561 5.402 1.00 78.85 C ANISOU 970 CB SER A 114 9921 14634 5406 -1816 -433 1168 C ATOM 971 OG SER A 114 8.586 0.518 5.306 1.00 81.61 O ANISOU 971 OG SER A 114 10324 14871 5811 -1771 -216 1088 O ATOM 972 N VAL A 121 10.760 -2.566 4.338 1.00 64.93 N ANISOU 972 N VAL A 121 7915 12415 4341 -1524 -754 2171 N ATOM 973 CA VAL A 121 10.264 -3.307 3.168 1.00 74.30 C ANISOU 973 CA VAL A 121 9091 13151 5990 -1334 -694 2250 C ATOM 974 C VAL A 121 10.453 -2.527 1.843 1.00 72.43 C ANISOU 974 C VAL A 121 8932 12561 6026 -1210 -635 1890 C ATOM 975 O VAL A 121 9.692 -1.604 1.545 1.00 73.52 O ANISOU 975 O VAL A 121 9177 12631 6125 -1206 -473 1553 O ATOM 976 CB VAL A 121 8.772 -3.715 3.352 1.00 65.26 C ANISOU 976 CB VAL A 121 7978 11975 4842 -1329 -515 2299 C ATOM 977 CG1 VAL A 121 8.262 -4.559 2.174 1.00 54.14 C ANISOU 977 CG1 VAL A 121 6543 10123 3906 -1153 -466 2384 C ATOM 978 CG2 VAL A 121 8.590 -4.473 4.663 1.00 60.37 C ANISOU 978 CG2 VAL A 121 7278 11721 3940 -1462 -564 2676 C ATOM 979 N GLN A 122 11.470 -2.903 1.062 1.00 82.58 N ANISOU 979 N GLN A 122 10151 13629 7596 -1111 -762 1978 N ATOM 980 CA GLN A 122 11.633 -2.419 -0.323 1.00 68.63 C ANISOU 980 CA GLN A 122 8440 11509 6129 -983 -707 1710 C ATOM 981 C GLN A 122 10.599 -3.107 -1.232 1.00 69.47 C ANISOU 981 C GLN A 122 8558 11296 6540 -858 -590 1738 C ATOM 982 O GLN A 122 10.121 -4.211 -0.926 1.00 70.32 O ANISOU 982 O GLN A 122 8594 11388 6735 -845 -594 2025 O ATOM 983 CB GLN A 122 13.059 -2.676 -0.838 1.00 59.40 C ANISOU 983 CB GLN A 122 7180 10228 5161 -928 -866 1801 C ATOM 984 CG GLN A 122 14.145 -1.942 -0.095 0.00 71.77 C ANISOU 984 CG GLN A 122 8722 12084 6464 -1049 -993 1746 C ATOM 985 CD GLN A 122 15.542 -2.249 -0.609 0.00 70.98 C ANISOU 985 CD GLN A 122 8510 11865 6595 -990 -1146 1856 C ATOM 986 NE2 GLN A 122 16.516 -2.239 0.294 0.00 73.15 N ANISOU 986 NE2 GLN A 122 8689 12432 6674 -1097 -1318 2015 N ATOM 987 OE1 GLN A 122 15.746 -2.484 -1.801 0.00 68.09 O ANISOU 987 OE1 GLN A 122 8135 11164 6571 -857 -1109 1793 O ATOM 988 N LEU A 123 10.262 -2.442 -2.341 1.00 75.06 N ANISOU 988 N LEU A 123 9348 11762 7410 -776 -491 1447 N ATOM 989 CA LEU A 123 9.196 -2.891 -3.259 1.00 63.20 C ANISOU 989 CA LEU A 123 7865 9989 6158 -677 -377 1411 C ATOM 990 C LEU A 123 9.445 -4.328 -3.736 1.00 70.13 C ANISOU 990 C LEU A 123 8632 10662 7351 -598 -442 1681 C ATOM 991 O LEU A 123 10.570 -4.629 -4.172 1.00 66.22 O ANISOU 991 O LEU A 123 8073 10068 7021 -554 -545 1741 O ATOM 992 CB LEU A 123 9.100 -1.974 -4.490 1.00 57.39 C ANISOU 992 CB LEU A 123 7208 9039 5557 -604 -305 1099 C ATOM 993 CG LEU A 123 8.344 -0.641 -4.377 1.00 51.62 C ANISOU 993 CG LEU A 123 6580 8376 4659 -641 -176 811 C ATOM 994 CD1 LEU A 123 9.220 0.500 -3.872 1.00 45.36 C ANISOU 994 CD1 LEU A 123 5823 7751 3660 -723 -210 634 C ATOM 995 CD2 LEU A 123 7.768 -0.240 -5.723 1.00 67.94 C ANISOU 995 CD2 LEU A 123 8688 10178 6948 -543 -95 631 C ATOM 996 N PRO A 124 8.416 -5.216 -3.655 1.00 60.54 N ANISOU 996 N PRO A 124 7383 9371 6248 -581 -374 1835 N ATOM 997 CA PRO A 124 8.622 -6.587 -4.161 1.00 75.11 C ANISOU 997 CA PRO A 124 9112 10980 8448 -508 -416 2061 C ATOM 998 C PRO A 124 9.020 -6.627 -5.657 1.00 75.28 C ANISOU 998 C PRO A 124 9135 10696 8771 -407 -404 1864 C ATOM 999 O PRO A 124 8.544 -5.807 -6.455 1.00 41.10 O ANISOU 999 O PRO A 124 4902 6296 4417 -383 -326 1583 O ATOM 1000 CB PRO A 124 7.264 -7.269 -3.904 1.00 71.18 C ANISOU 1000 CB PRO A 124 8597 10446 8003 -521 -312 2178 C ATOM 1001 CG PRO A 124 6.664 -6.492 -2.780 1.00 59.25 C ANISOU 1001 CG PRO A 124 7156 9253 6103 -625 -258 2149 C ATOM 1002 CD PRO A 124 7.075 -5.070 -3.051 1.00 51.71 C ANISOU 1002 CD PRO A 124 6310 8374 4965 -635 -249 1820 C ATOM 1003 N ARG A 125 9.906 -7.558 -6.014 1.00 74.74 N ANISOU 1003 N ARG A 125 8950 10462 8984 -354 -477 2019 N ATOM 1004 CA ARG A 125 10.502 -7.589 -7.364 1.00 61.22 C ANISOU 1004 CA ARG A 125 7228 8502 7530 -276 -465 1825 C ATOM 1005 C ARG A 125 9.487 -7.921 -8.471 1.00 52.90 C ANISOU 1005 C ARG A 125 6202 7224 6672 -234 -349 1653 C ATOM 1006 O ARG A 125 9.542 -7.318 -9.565 1.00 34.28 O ANISOU 1006 O ARG A 125 3910 4775 4340 -205 -308 1389 O ATOM 1007 CB ARG A 125 11.749 -8.496 -7.410 1.00 66.16 C ANISOU 1007 CB ARG A 125 7702 9007 8429 -232 -557 2022 C ATOM 1008 CG ARG A 125 13.064 -7.738 -7.192 1.00 70.75 C ANISOU 1008 CG ARG A 125 8278 9728 8875 -246 -662 1990 C ATOM 1009 CD ARG A 125 13.143 -6.986 -5.863 1.00 72.79 C ANISOU 1009 CD ARG A 125 8581 10335 8739 -345 -741 2085 C ATOM 1010 NE ARG A 125 14.270 -6.042 -5.848 1.00 78.50 N ANISOU 1010 NE ARG A 125 9321 11180 9324 -371 -821 1958 N ATOM 1011 CZ ARG A 125 14.202 -4.704 -5.765 1.00 60.09 C ANISOU 1011 CZ ARG A 125 7117 9003 6712 -428 -795 1706 C ATOM 1012 NH1 ARG A 125 13.034 -4.047 -5.661 1.00 44.56 N1+ ANISOU 1012 NH1 ARG A 125 5276 7102 4555 -463 -686 1540 N1+ ATOM 1013 NH2 ARG A 125 15.347 -4.005 -5.770 1.00 39.28 N ANISOU 1013 NH2 ARG A 125 4465 6446 4011 -453 -876 1619 N ATOM 1014 N GLY A 126 8.563 -8.846 -8.167 1.00 39.42 N ANISOU 1014 N GLY A 126 4439 5449 5088 -244 -302 1812 N ATOM 1015 CA GLY A 126 7.398 -9.141 -9.025 1.00 32.58 C ANISOU 1015 CA GLY A 126 3594 4419 4366 -230 -198 1660 C ATOM 1016 C GLY A 126 6.565 -7.914 -9.405 1.00 27.12 C ANISOU 1016 C GLY A 126 3036 3829 3438 -246 -137 1405 C ATOM 1017 O GLY A 126 6.256 -7.713 -10.577 1.00 20.69 O ANISOU 1017 O GLY A 126 2253 2890 2717 -220 -94 1188 O ATOM 1018 N MET A 127 6.233 -7.092 -8.402 1.00 26.62 N ANISOU 1018 N MET A 127 3041 4000 3074 -294 -131 1435 N ATOM 1019 CA MET A 127 5.410 -5.888 -8.563 1.00 21.36 C ANISOU 1019 CA MET A 127 2481 3427 2208 -307 -60 1219 C ATOM 1020 C MET A 127 6.124 -4.827 -9.383 1.00 22.33 C ANISOU 1020 C MET A 127 2674 3531 2278 -277 -82 991 C ATOM 1021 O MET A 127 5.491 -4.169 -10.217 1.00 19.13 O ANISOU 1021 O MET A 127 2321 3069 1878 -256 -28 805 O ATOM 1022 CB MET A 127 5.028 -5.292 -7.193 1.00 29.11 C ANISOU 1022 CB MET A 127 3502 4666 2891 -376 -32 1288 C ATOM 1023 CG MET A 127 4.114 -4.071 -7.277 1.00 28.25 C ANISOU 1023 CG MET A 127 3480 4627 2626 -385 67 1064 C ATOM 1024 SD MET A 127 3.562 -3.377 -5.715 1.00 30.94 S ANISOU 1024 SD MET A 127 3859 5264 2633 -479 144 1082 S ATOM 1025 CE MET A 127 5.042 -2.528 -5.237 1.00 44.94 C ANISOU 1025 CE MET A 127 5676 7198 4199 -521 50 1011 C ATOM 1026 N VAL A 128 7.423 -4.657 -9.138 1.00 24.58 N ANISOU 1026 N VAL A 128 2950 3869 2521 -281 -165 1027 N ATOM 1027 CA VAL A 128 8.226 -3.663 -9.853 1.00 23.82 C ANISOU 1027 CA VAL A 128 2910 3757 2384 -261 -185 833 C ATOM 1028 C VAL A 128 8.258 -3.933 -11.354 1.00 19.93 C ANISOU 1028 C VAL A 128 2406 3062 2105 -208 -162 702 C ATOM 1029 O VAL A 128 8.065 -3.021 -12.162 1.00 22.43 O ANISOU 1029 O VAL A 128 2787 3360 2376 -196 -127 521 O ATOM 1030 CB VAL A 128 9.660 -3.582 -9.293 1.00 29.23 C ANISOU 1030 CB VAL A 128 3559 4533 3013 -281 -286 916 C ATOM 1031 CG1 VAL A 128 10.580 -2.756 -10.202 1.00 28.50 C ANISOU 1031 CG1 VAL A 128 3501 4380 2947 -257 -301 729 C ATOM 1032 CG2 VAL A 128 9.622 -2.962 -7.903 1.00 32.96 C ANISOU 1032 CG2 VAL A 128 4065 5262 3197 -360 -306 970 C ATOM 1033 N LYS A 129 8.492 -5.183 -11.719 1.00 22.48 N ANISOU 1033 N LYS A 129 2638 3238 2664 -185 -175 795 N ATOM 1034 CA LYS A 129 8.521 -5.573 -13.124 1.00 17.37 C ANISOU 1034 CA LYS A 129 1969 2417 2213 -155 -140 649 C ATOM 1035 C LYS A 129 7.158 -5.333 -13.746 1.00 16.82 C ANISOU 1035 C LYS A 129 1943 2332 2117 -165 -76 532 C ATOM 1036 O LYS A 129 7.074 -4.805 -14.840 1.00 21.27 O ANISOU 1036 O LYS A 129 2544 2869 2668 -160 -56 362 O ATOM 1037 CB LYS A 129 8.921 -7.043 -13.277 1.00 18.16 C ANISOU 1037 CB LYS A 129 1945 2345 2610 -137 -144 758 C ATOM 1038 CG LYS A 129 8.970 -7.558 -14.715 1.00 17.38 C ANISOU 1038 CG LYS A 129 1811 2073 2718 -126 -89 569 C ATOM 1039 CD LYS A 129 9.219 -9.059 -14.766 1.00 18.29 C ANISOU 1039 CD LYS A 129 1788 1987 3173 -112 -67 662 C ATOM 1040 CE LYS A 129 10.580 -9.432 -14.206 1.00 16.83 C ANISOU 1040 CE LYS A 129 1513 1764 3117 -77 -123 821 C ATOM 1041 NZ LYS A 129 10.969 -10.818 -14.547 1.00 18.21 N1+ ANISOU 1041 NZ LYS A 129 1535 1694 3691 -52 -80 862 N1+ ATOM 1042 N SER A 130 6.092 -5.709 -13.054 1.00 16.43 N ANISOU 1042 N SER A 130 1877 2311 2053 -184 -46 637 N ATOM 1043 CA SER A 130 4.744 -5.527 -13.609 1.00 16.29 C ANISOU 1043 CA SER A 130 1878 2279 2032 -194 10 541 C ATOM 1044 C SER A 130 4.407 -4.044 -13.818 1.00 15.77 C ANISOU 1044 C SER A 130 1901 2321 1771 -188 27 413 C ATOM 1045 O SER A 130 3.883 -3.669 -14.867 1.00 13.71 O ANISOU 1045 O SER A 130 1651 2028 1529 -182 41 289 O ATOM 1046 CB SER A 130 3.707 -6.209 -12.727 1.00 16.22 C ANISOU 1046 CB SER A 130 1822 2284 2056 -219 48 693 C ATOM 1047 OG SER A 130 4.045 -7.582 -12.571 1.00 16.22 O ANISOU 1047 OG SER A 130 1726 2155 2283 -223 36 832 O ATOM 1048 N LEU A 131 4.756 -3.201 -12.846 1.00 14.32 N ANISOU 1048 N LEU A 131 1769 2264 1410 -194 23 444 N ATOM 1049 CA LEU A 131 4.631 -1.736 -13.009 1.00 16.85 C ANISOU 1049 CA LEU A 131 2161 2651 1591 -186 49 313 C ATOM 1050 C LEU A 131 5.348 -1.237 -14.247 1.00 12.48 C ANISOU 1050 C LEU A 131 1629 2034 1078 -165 20 193 C ATOM 1051 O LEU A 131 4.744 -0.603 -15.109 1.00 19.16 O ANISOU 1051 O LEU A 131 2490 2859 1930 -151 42 108 O ATOM 1052 CB LEU A 131 5.185 -0.992 -11.788 1.00 18.68 C ANISOU 1052 CB LEU A 131 2434 3021 1641 -215 49 329 C ATOM 1053 CG LEU A 131 4.268 -1.068 -10.578 1.00 18.51 C ANISOU 1053 CG LEU A 131 2406 3114 1512 -251 110 404 C ATOM 1054 CD1 LEU A 131 4.991 -0.575 -9.346 1.00 19.52 C ANISOU 1054 CD1 LEU A 131 2565 3415 1439 -306 95 423 C ATOM 1055 CD2 LEU A 131 3.007 -0.249 -10.810 1.00 22.88 C ANISOU 1055 CD2 LEU A 131 2975 3657 2060 -236 203 297 C ATOM 1056 N LEU A 132 6.631 -1.555 -14.341 1.00 13.41 N ANISOU 1056 N LEU A 132 1736 2128 1231 -164 -30 206 N ATOM 1057 CA LEU A 132 7.404 -1.191 -15.511 1.00 15.67 C ANISOU 1057 CA LEU A 132 2034 2363 1557 -152 -45 98 C ATOM 1058 C LEU A 132 6.783 -1.682 -16.807 1.00 15.81 C ANISOU 1058 C LEU A 132 2024 2309 1673 -153 -27 27 C ATOM 1059 O LEU A 132 6.720 -0.920 -17.768 1.00 14.11 O ANISOU 1059 O LEU A 132 1837 2109 1415 -154 -21 -60 O ATOM 1060 CB LEU A 132 8.856 -1.694 -15.417 1.00 18.12 C ANISOU 1060 CB LEU A 132 2308 2644 1934 -150 -91 130 C ATOM 1061 CG LEU A 132 9.703 -1.276 -16.629 1.00 14.62 C ANISOU 1061 CG LEU A 132 1872 2159 1523 -146 -88 10 C ATOM 1062 CD1 LEU A 132 9.714 0.238 -16.813 1.00 11.71 C ANISOU 1062 CD1 LEU A 132 1575 1854 1021 -151 -75 -63 C ATOM 1063 CD2 LEU A 132 11.099 -1.827 -16.481 1.00 19.44 C ANISOU 1063 CD2 LEU A 132 2425 2731 2232 -140 -123 44 C ATOM 1064 N TYR A 133 6.339 -2.943 -16.851 1.00 19.45 N ANISOU 1064 N TYR A 133 2422 2699 2268 -163 -20 66 N ATOM 1065 CA TYR A 133 5.734 -3.468 -18.094 1.00 19.89 C ANISOU 1065 CA TYR A 133 2443 2705 2411 -187 -4 -34 C ATOM 1066 C TYR A 133 4.484 -2.670 -18.508 1.00 19.26 C ANISOU 1066 C TYR A 133 2386 2695 2238 -194 3 -63 C ATOM 1067 O TYR A 133 4.297 -2.396 -19.694 1.00 16.12 O ANISOU 1067 O TYR A 133 1986 2325 1813 -216 -6 -154 O ATOM 1068 CB TYR A 133 5.400 -4.972 -18.034 1.00 20.05 C ANISOU 1068 CB TYR A 133 2378 2614 2627 -207 14 -6 C ATOM 1069 CG TYR A 133 5.021 -5.507 -19.412 1.00 18.31 C ANISOU 1069 CG TYR A 133 2116 2353 2487 -254 32 -164 C ATOM 1070 CD1 TYR A 133 5.995 -5.788 -20.361 1.00 19.90 C ANISOU 1070 CD1 TYR A 133 2299 2516 2746 -272 48 -297 C ATOM 1071 CD2 TYR A 133 3.687 -5.650 -19.788 1.00 21.99 C ANISOU 1071 CD2 TYR A 133 2557 2845 2954 -290 36 -194 C ATOM 1072 CE1 TYR A 133 5.661 -6.239 -21.629 1.00 23.85 C ANISOU 1072 CE1 TYR A 133 2763 3018 3281 -337 72 -470 C ATOM 1073 CE2 TYR A 133 3.339 -6.098 -21.059 1.00 25.34 C ANISOU 1073 CE2 TYR A 133 2939 3272 3418 -354 41 -354 C ATOM 1074 CZ TYR A 133 4.326 -6.398 -21.973 1.00 25.67 C ANISOU 1074 CZ TYR A 133 2970 3291 3493 -383 62 -499 C ATOM 1075 OH TYR A 133 3.978 -6.833 -23.230 1.00 28.32 O ANISOU 1075 OH TYR A 133 3263 3663 3834 -468 74 -683 O ATOM 1076 N GLN A 134 3.642 -2.307 -17.543 1.00 13.09 N ANISOU 1076 N GLN A 134 1615 1951 1407 -179 23 20 N ATOM 1077 CA GLN A 134 2.398 -1.608 -17.857 1.00 17.65 C ANISOU 1077 CA GLN A 134 2186 2575 1944 -175 37 9 C ATOM 1078 C GLN A 134 2.635 -0.122 -18.201 1.00 18.44 C ANISOU 1078 C GLN A 134 2337 2725 1945 -150 35 -24 C ATOM 1079 O GLN A 134 1.956 0.451 -19.066 1.00 14.54 O ANISOU 1079 O GLN A 134 1821 2258 1444 -149 22 -39 O ATOM 1080 CB GLN A 134 1.375 -1.790 -16.748 1.00 13.38 C ANISOU 1080 CB GLN A 134 1620 2048 1414 -171 81 95 C ATOM 1081 CG GLN A 134 0.899 -3.236 -16.619 1.00 16.50 C ANISOU 1081 CG GLN A 134 1946 2380 1945 -204 87 144 C ATOM 1082 CD GLN A 134 -0.255 -3.401 -15.636 1.00 15.33 C ANISOU 1082 CD GLN A 134 1761 2256 1807 -208 142 238 C ATOM 1083 NE2 GLN A 134 -0.258 -4.502 -14.908 1.00 13.78 N ANISOU 1083 NE2 GLN A 134 1524 2016 1695 -231 159 341 N ATOM 1084 OE1 GLN A 134 -1.136 -2.537 -15.535 1.00 13.35 O ANISOU 1084 OE1 GLN A 134 1509 2058 1505 -192 176 226 O ATOM 1085 N ILE A 135 3.624 0.488 -17.568 1.00 17.60 N ANISOU 1085 N ILE A 135 2283 2628 1775 -134 42 -26 N ATOM 1086 CA ILE A 135 4.019 1.841 -17.941 1.00 12.97 C ANISOU 1086 CA ILE A 135 1736 2058 1134 -117 47 -63 C ATOM 1087 C ILE A 135 4.508 1.814 -19.392 1.00 13.51 C ANISOU 1087 C ILE A 135 1797 2129 1206 -135 8 -105 C ATOM 1088 O ILE A 135 4.090 2.646 -20.213 1.00 11.47 O ANISOU 1088 O ILE A 135 1530 1897 932 -131 1 -95 O ATOM 1089 CB ILE A 135 5.092 2.395 -16.999 1.00 9.97 C ANISOU 1089 CB ILE A 135 1405 1690 693 -116 58 -79 C ATOM 1090 CG1 ILE A 135 4.517 2.527 -15.595 1.00 11.43 C ANISOU 1090 CG1 ILE A 135 1597 1917 830 -118 106 -55 C ATOM 1091 CG2 ILE A 135 5.548 3.780 -17.442 1.00 11.43 C ANISOU 1091 CG2 ILE A 135 1620 1863 858 -105 71 -125 C ATOM 1092 CD1 ILE A 135 5.570 2.550 -14.518 1.00 13.93 C ANISOU 1092 CD1 ILE A 135 1944 2290 1060 -145 93 -55 C ATOM 1093 N LEU A 136 5.368 0.845 -19.703 1.00 9.26 N ANISOU 1093 N LEU A 136 1250 1570 699 -159 -10 -144 N ATOM 1094 CA LEU A 136 5.886 0.692 -21.071 1.00 13.20 C ANISOU 1094 CA LEU A 136 1737 2090 1187 -193 -26 -214 C ATOM 1095 C LEU A 136 4.798 0.414 -22.104 1.00 14.86 C ANISOU 1095 C LEU A 136 1904 2356 1388 -231 -46 -233 C ATOM 1096 O LEU A 136 4.878 0.895 -23.233 1.00 11.85 O ANISOU 1096 O LEU A 136 1518 2051 933 -262 -64 -255 O ATOM 1097 CB LEU A 136 6.961 -0.402 -21.147 1.00 10.43 C ANISOU 1097 CB LEU A 136 1364 1687 912 -211 -19 -274 C ATOM 1098 CG LEU A 136 8.342 -0.050 -20.614 1.00 11.45 C ANISOU 1098 CG LEU A 136 1518 1792 1041 -191 -18 -266 C ATOM 1099 CD1 LEU A 136 9.208 -1.286 -20.642 1.00 12.98 C ANISOU 1099 CD1 LEU A 136 1657 1912 1365 -198 -8 -302 C ATOM 1100 CD2 LEU A 136 9.018 1.057 -21.405 1.00 15.26 C ANISOU 1100 CD2 LEU A 136 2032 2321 1444 -201 -11 -300 C ATOM 1101 N ASP A 137 3.797 -0.371 -21.707 1.00 14.58 N ANISOU 1101 N ASP A 137 1825 2296 1418 -237 -46 -217 N ATOM 1102 CA ASP A 137 2.697 -0.740 -22.603 1.00 12.56 C ANISOU 1102 CA ASP A 137 1510 2100 1163 -285 -75 -243 C ATOM 1103 C ASP A 137 1.908 0.522 -22.925 1.00 12.29 C ANISOU 1103 C ASP A 137 1469 2140 1061 -262 -103 -155 C ATOM 1104 O ASP A 137 1.665 0.826 -24.106 1.00 16.77 O ANISOU 1104 O ASP A 137 2006 2811 1555 -306 -149 -157 O ATOM 1105 CB ASP A 137 1.833 -1.840 -21.959 1.00 12.25 C ANISOU 1105 CB ASP A 137 1418 1998 1240 -296 -61 -234 C ATOM 1106 CG ASP A 137 0.991 -2.624 -22.952 1.00 14.94 C ANISOU 1106 CG ASP A 137 1683 2382 1610 -374 -90 -314 C ATOM 1107 OD1 ASP A 137 0.737 -2.149 -24.061 1.00 18.16 O ANISOU 1107 OD1 ASP A 137 2074 2910 1917 -417 -136 -345 O ATOM 1108 OD2 ASP A 137 0.516 -3.726 -22.584 1.00 22.28 O1- ANISOU 1108 OD2 ASP A 137 2561 3236 2670 -399 -69 -337 O1- ATOM 1109 N GLY A 138 1.547 1.268 -21.879 1.00 11.30 N ANISOU 1109 N GLY A 138 1361 1968 966 -199 -71 -75 N ATOM 1110 CA GLY A 138 0.791 2.510 -22.041 1.00 15.98 C ANISOU 1110 CA GLY A 138 1927 2587 1559 -161 -76 13 C ATOM 1111 C GLY A 138 1.483 3.576 -22.875 1.00 15.92 C ANISOU 1111 C GLY A 138 1941 2615 1491 -159 -97 46 C ATOM 1112 O GLY A 138 0.849 4.222 -23.713 1.00 18.72 O ANISOU 1112 O GLY A 138 2240 3034 1837 -163 -140 134 O ATOM 1113 N ILE A 139 2.786 3.741 -22.653 1.00 15.47 N ANISOU 1113 N ILE A 139 1953 2524 1402 -157 -70 -5 N ATOM 1114 CA ILE A 139 3.600 4.713 -23.383 1.00 15.59 C ANISOU 1114 CA ILE A 139 1990 2562 1370 -162 -76 27 C ATOM 1115 C ILE A 139 3.799 4.324 -24.836 1.00 18.76 C ANISOU 1115 C ILE A 139 2368 3089 1672 -234 -126 14 C ATOM 1116 O ILE A 139 3.758 5.176 -25.711 1.00 27.23 O ANISOU 1116 O ILE A 139 3417 4231 2696 -248 -153 109 O ATOM 1117 CB ILE A 139 4.937 4.954 -22.648 1.00 22.14 C ANISOU 1117 CB ILE A 139 2887 3322 2204 -148 -33 -34 C ATOM 1118 CG1 ILE A 139 4.645 5.675 -21.322 1.00 36.30 C ANISOU 1118 CG1 ILE A 139 4697 5032 4064 -96 19 -25 C ATOM 1119 CG2 ILE A 139 5.933 5.760 -23.475 1.00 28.30 C ANISOU 1119 CG2 ILE A 139 3685 4125 2944 -168 -32 -15 C ATOM 1120 CD1 ILE A 139 4.054 7.073 -21.446 1.00 39.88 C ANISOU 1120 CD1 ILE A 139 5119 5439 4593 -58 47 53 C ATOM 1121 N HIS A 140 3.998 3.041 -25.090 1.00 20.09 N ANISOU 1121 N HIS A 140 2533 3288 1814 -286 -131 -101 N ATOM 1122 CA HIS A 140 4.053 2.525 -26.458 1.00 19.80 C ANISOU 1122 CA HIS A 140 2464 3391 1669 -377 -164 -161 C ATOM 1123 C HIS A 140 2.786 2.858 -27.257 1.00 16.57 C ANISOU 1123 C HIS A 140 1983 3114 1200 -412 -238 -62 C ATOM 1124 O HIS A 140 2.856 3.248 -28.431 1.00 21.25 O ANISOU 1124 O HIS A 140 2550 3864 1659 -477 -280 -17 O ATOM 1125 CB HIS A 140 4.292 1.002 -26.451 1.00 14.94 C ANISOU 1125 CB HIS A 140 1836 2746 1094 -426 -138 -329 C ATOM 1126 CG HIS A 140 4.142 0.369 -27.795 1.00 27.52 C ANISOU 1126 CG HIS A 140 3384 4491 2580 -539 -159 -441 C ATOM 1127 CD2 HIS A 140 3.136 -0.369 -28.321 1.00 33.89 C ANISOU 1127 CD2 HIS A 140 4127 5382 3369 -612 -200 -503 C ATOM 1128 ND1 HIS A 140 5.091 0.497 -28.791 1.00 31.19 N ANISOU 1128 ND1 HIS A 140 3864 5062 2925 -604 -133 -514 N ATOM 1129 CE1 HIS A 140 4.679 -0.147 -29.869 1.00 44.81 C ANISOU 1129 CE1 HIS A 140 5539 6943 4543 -718 -152 -630 C ATOM 1130 NE2 HIS A 140 3.501 -0.689 -29.607 1.00 49.44 N ANISOU 1130 NE2 HIS A 140 6076 7516 5194 -728 -198 -631 N ATOM 1131 N TYR A 141 1.636 2.724 -26.612 1.00 14.44 N ANISOU 1131 N TYR A 141 1669 2794 1023 -374 -256 -12 N ATOM 1132 CA TYR A 141 0.364 3.021 -27.270 1.00 18.26 C ANISOU 1132 CA TYR A 141 2061 3396 1482 -400 -336 99 C ATOM 1133 C TYR A 141 0.260 4.522 -27.623 1.00 16.12 C ANISOU 1133 C TYR A 141 1763 3152 1207 -354 -364 298 C ATOM 1134 O TYR A 141 -0.148 4.888 -28.722 1.00 18.03 O ANISOU 1134 O TYR A 141 1938 3560 1351 -409 -445 410 O ATOM 1135 CB TYR A 141 -0.810 2.581 -26.386 1.00 15.44 C ANISOU 1135 CB TYR A 141 1651 2956 1258 -360 -331 112 C ATOM 1136 CG TYR A 141 -2.118 3.098 -26.880 1.00 14.09 C ANISOU 1136 CG TYR A 141 1368 2879 1106 -362 -409 257 C ATOM 1137 CD1 TYR A 141 -2.739 2.504 -27.959 1.00 12.09 C ANISOU 1137 CD1 TYR A 141 1035 2806 754 -468 -503 236 C ATOM 1138 CD2 TYR A 141 -2.725 4.214 -26.290 1.00 16.52 C ANISOU 1138 CD2 TYR A 141 1635 3099 1543 -264 -389 412 C ATOM 1139 CE1 TYR A 141 -3.941 2.971 -28.432 1.00 14.11 C ANISOU 1139 CE1 TYR A 141 1167 3167 1028 -475 -594 392 C ATOM 1140 CE2 TYR A 141 -3.937 4.695 -26.768 1.00 15.10 C ANISOU 1140 CE2 TYR A 141 1325 2996 1418 -258 -464 569 C ATOM 1141 CZ TYR A 141 -4.527 4.075 -27.844 1.00 14.24 C ANISOU 1141 CZ TYR A 141 1133 3080 1196 -363 -577 573 C ATOM 1142 OH TYR A 141 -5.728 4.521 -28.335 1.00 15.24 O ANISOU 1142 OH TYR A 141 1113 3304 1376 -363 -672 747 O ATOM 1143 N LEU A 142 0.642 5.370 -26.677 1.00 14.43 N ANISOU 1143 N LEU A 142 1594 2779 1109 -261 -295 343 N ATOM 1144 CA LEU A 142 0.668 6.815 -26.897 1.00 15.48 C ANISOU 1144 CA LEU A 142 1699 2882 1301 -211 -295 517 C ATOM 1145 C LEU A 142 1.632 7.207 -28.017 1.00 15.30 C ANISOU 1145 C LEU A 142 1699 2975 1139 -273 -320 566 C ATOM 1146 O LEU A 142 1.248 7.924 -28.948 1.00 16.89 O ANISOU 1146 O LEU A 142 1827 3287 1303 -295 -385 752 O ATOM 1147 CB LEU A 142 1.038 7.529 -25.593 1.00 16.68 C ANISOU 1147 CB LEU A 142 1902 2832 1605 -120 -195 488 C ATOM 1148 CG LEU A 142 -0.011 7.413 -24.495 1.00 16.04 C ANISOU 1148 CG LEU A 142 1783 2652 1657 -60 -152 469 C ATOM 1149 CD1 LEU A 142 0.543 7.954 -23.195 1.00 26.90 C ANISOU 1149 CD1 LEU A 142 3224 3874 3122 -4 -45 385 C ATOM 1150 CD2 LEU A 142 -1.253 8.171 -24.878 1.00 18.42 C ANISOU 1150 CD2 LEU A 142 1959 2959 2081 -19 -187 643 C ATOM 1151 N HIS A 143 2.863 6.712 -27.913 1.00 13.40 N ANISOU 1151 N HIS A 143 1546 2717 828 -304 -268 414 N ATOM 1152 CA HIS A 143 3.917 6.931 -28.902 1.00 15.23 C ANISOU 1152 CA HIS A 143 1804 3059 923 -372 -264 420 C ATOM 1153 C HIS A 143 3.589 6.410 -30.281 1.00 16.47 C ANISOU 1153 C HIS A 143 1911 3466 880 -488 -337 431 C ATOM 1154 O HIS A 143 3.871 7.087 -31.273 1.00 18.95 O ANISOU 1154 O HIS A 143 2199 3921 1079 -540 -365 567 O ATOM 1155 CB HIS A 143 5.241 6.307 -28.434 1.00 17.28 C ANISOU 1155 CB HIS A 143 2148 3242 1175 -381 -188 231 C ATOM 1156 CG HIS A 143 5.894 7.057 -27.314 1.00 17.68 C ANISOU 1156 CG HIS A 143 2246 3105 1366 -300 -125 234 C ATOM 1157 CD2 HIS A 143 5.430 8.040 -26.508 1.00 12.93 C ANISOU 1157 CD2 HIS A 143 1633 2371 908 -223 -105 324 C ATOM 1158 ND1 HIS A 143 7.193 6.829 -26.926 1.00 19.33 N ANISOU 1158 ND1 HIS A 143 2512 3252 1581 -304 -70 118 N ATOM 1159 CE1 HIS A 143 7.501 7.632 -25.924 1.00 13.12 C ANISOU 1159 CE1 HIS A 143 1752 2322 913 -243 -32 135 C ATOM 1160 NE2 HIS A 143 6.448 8.375 -25.650 1.00 12.95 N ANISOU 1160 NE2 HIS A 143 1693 2252 977 -195 -42 245 N ATOM 1161 N ALA A 144 2.996 5.224 -30.367 1.00 13.03 N ANISOU 1161 N ALA A 144 1455 3099 399 -540 -367 291 N ATOM 1162 CA ALA A 144 2.543 4.723 -31.677 1.00 15.64 C ANISOU 1162 CA ALA A 144 1724 3693 525 -672 -443 276 C ATOM 1163 C ALA A 144 1.540 5.674 -32.353 1.00 17.58 C ANISOU 1163 C ALA A 144 1870 4085 725 -680 -554 548 C ATOM 1164 O ALA A 144 1.495 5.754 -33.574 1.00 21.55 O ANISOU 1164 O ALA A 144 2325 4846 1015 -793 -622 617 O ATOM 1165 CB ALA A 144 1.931 3.328 -31.542 1.00 16.55 C ANISOU 1165 CB ALA A 144 1815 3822 649 -726 -453 73 C ATOM 1166 N ASN A 145 0.743 6.380 -31.547 1.00 16.45 N ANISOU 1166 N ASN A 145 1683 3782 785 -564 -569 704 N ATOM 1167 CA ASN A 145 -0.218 7.375 -32.034 1.00 19.98 C ANISOU 1167 CA ASN A 145 2011 4309 1271 -542 -665 995 C ATOM 1168 C ASN A 145 0.368 8.786 -32.095 1.00 22.99 C ANISOU 1168 C ASN A 145 2392 4600 1742 -476 -632 1211 C ATOM 1169 O ASN A 145 -0.366 9.756 -32.201 1.00 27.33 O ANISOU 1169 O ASN A 145 2837 5120 2426 -418 -683 1469 O ATOM 1170 CB ASN A 145 -1.476 7.340 -31.137 1.00 18.52 C ANISOU 1170 CB ASN A 145 1753 3983 1300 -451 -680 1032 C ATOM 1171 CG ASN A 145 -2.372 6.172 -31.457 1.00 17.51 C ANISOU 1171 CG ASN A 145 1567 4006 1082 -539 -757 918 C ATOM 1172 ND2 ASN A 145 -2.411 5.157 -30.595 1.00 17.17 N ANISOU 1172 ND2 ASN A 145 1578 3835 1112 -526 -689 696 N ATOM 1173 OD1 ASN A 145 -3.004 6.174 -32.496 1.00 19.27 O ANISOU 1173 OD1 ASN A 145 1688 4468 1166 -630 -880 1036 O ATOM 1174 N TRP A 146 1.692 8.900 -32.040 1.00 25.90 N ANISOU 1174 N TRP A 146 2864 4913 2064 -487 -543 1113 N ATOM 1175 CA TRP A 146 2.402 10.182 -32.044 1.00 26.79 C ANISOU 1175 CA TRP A 146 2982 4915 2281 -436 -493 1285 C ATOM 1176 C TRP A 146 1.974 11.146 -30.929 1.00 20.20 C ANISOU 1176 C TRP A 146 2118 3794 1764 -294 -438 1374 C ATOM 1177 O TRP A 146 2.003 12.348 -31.099 1.00 23.32 O ANISOU 1177 O TRP A 146 2454 4104 2304 -249 -428 1594 O ATOM 1178 CB TRP A 146 2.337 10.822 -33.448 1.00 34.23 C ANISOU 1178 CB TRP A 146 3841 6102 3064 -521 -581 1557 C ATOM 1179 CG TRP A 146 3.164 10.058 -34.463 1.00 44.88 C ANISOU 1179 CG TRP A 146 5243 7715 4093 -671 -581 1424 C ATOM 1180 CD1 TRP A 146 2.701 9.198 -35.420 1.00 56.19 C ANISOU 1180 CD1 TRP A 146 6637 9452 5260 -805 -667 1364 C ATOM 1181 CD2 TRP A 146 4.597 10.076 -34.600 1.00 45.07 C ANISOU 1181 CD2 TRP A 146 5358 7724 4043 -709 -476 1307 C ATOM 1182 CE2 TRP A 146 4.926 9.208 -35.669 1.00 51.11 C ANISOU 1182 CE2 TRP A 146 6134 8787 4497 -863 -490 1176 C ATOM 1183 CE3 TRP A 146 5.631 10.751 -33.930 1.00 43.68 C ANISOU 1183 CE3 TRP A 146 5244 7316 4036 -636 -368 1290 C ATOM 1184 NE1 TRP A 146 3.753 8.688 -36.150 1.00 62.64 N ANISOU 1184 NE1 TRP A 146 7518 10442 5840 -926 -608 1203 N ATOM 1185 CZ2 TRP A 146 6.246 8.991 -36.083 1.00 56.73 C ANISOU 1185 CZ2 TRP A 146 6914 9562 5079 -936 -389 1034 C ATOM 1186 CZ3 TRP A 146 6.945 10.536 -34.338 1.00 46.39 C ANISOU 1186 CZ3 TRP A 146 5652 7724 4249 -708 -285 1167 C ATOM 1187 CH2 TRP A 146 7.240 9.661 -35.408 1.00 59.37 C ANISOU 1187 CH2 TRP A 146 7302 9659 5597 -852 -290 1044 C ATOM 1188 N VAL A 147 1.612 10.598 -29.778 1.00 19.43 N ANISOU 1188 N VAL A 147 2058 3546 1778 -233 -388 1191 N ATOM 1189 CA VAL A 147 1.235 11.382 -28.609 1.00 21.08 C ANISOU 1189 CA VAL A 147 2248 3499 2263 -115 -309 1205 C ATOM 1190 C VAL A 147 2.353 11.223 -27.583 1.00 17.79 C ANISOU 1190 C VAL A 147 1957 2933 1871 -96 -200 979 C ATOM 1191 O VAL A 147 2.630 10.117 -27.138 1.00 19.70 O ANISOU 1191 O VAL A 147 2271 3207 2006 -125 -189 782 O ATOM 1192 CB VAL A 147 -0.115 10.910 -28.000 1.00 17.97 C ANISOU 1192 CB VAL A 147 1788 3074 1968 -68 -328 1178 C ATOM 1193 CG1 VAL A 147 -0.415 11.625 -26.690 1.00 16.47 C ANISOU 1193 CG1 VAL A 147 1588 2629 2040 40 -213 1131 C ATOM 1194 CG2 VAL A 147 -1.260 11.148 -28.968 1.00 20.17 C ANISOU 1194 CG2 VAL A 147 1916 3498 2249 -84 -449 1421 C ATOM 1195 N LEU A 148 2.977 12.335 -27.212 1.00 18.49 N ANISOU 1195 N LEU A 148 2054 2856 2113 -53 -124 1020 N ATOM 1196 CA LEU A 148 3.994 12.358 -26.148 1.00 17.68 C ANISOU 1196 CA LEU A 148 2051 2614 2051 -39 -29 817 C ATOM 1197 C LEU A 148 3.331 12.678 -24.813 1.00 17.22 C ANISOU 1197 C LEU A 148 1980 2382 2179 36 49 725 C ATOM 1198 O LEU A 148 2.360 13.415 -24.786 1.00 14.29 O ANISOU 1198 O LEU A 148 1512 1925 1992 94 65 849 O ATOM 1199 CB LEU A 148 5.055 13.407 -26.475 1.00 17.17 C ANISOU 1199 CB LEU A 148 1995 2473 2058 -53 17 888 C ATOM 1200 CG LEU A 148 5.743 13.248 -27.841 1.00 19.05 C ANISOU 1200 CG LEU A 148 2235 2895 2108 -136 -39 998 C ATOM 1201 CD1 LEU A 148 6.770 14.339 -28.076 1.00 18.18 C ANISOU 1201 CD1 LEU A 148 2122 2687 2097 -149 20 1081 C ATOM 1202 CD2 LEU A 148 6.411 11.881 -27.970 1.00 25.47 C ANISOU 1202 CD2 LEU A 148 3131 3854 2692 -203 -57 803 C ATOM 1203 N HIS A 149 3.829 12.107 -23.716 1.00 15.40 N ANISOU 1203 N HIS A 149 1835 2113 1901 31 101 514 N ATOM 1204 CA HIS A 149 3.355 12.490 -22.385 1.00 14.82 C ANISOU 1204 CA HIS A 149 1759 1903 1970 80 194 402 C ATOM 1205 C HIS A 149 3.959 13.819 -21.916 1.00 16.65 C ANISOU 1205 C HIS A 149 1986 1961 2381 97 290 364 C ATOM 1206 O HIS A 149 3.240 14.660 -21.436 1.00 17.23 O ANISOU 1206 O HIS A 149 1990 1893 2662 148 371 370 O ATOM 1207 CB HIS A 149 3.668 11.419 -21.362 1.00 16.67 C ANISOU 1207 CB HIS A 149 2077 2189 2068 54 207 218 C ATOM 1208 CG HIS A 149 2.862 11.549 -20.109 1.00 17.04 C ANISOU 1208 CG HIS A 149 2108 2166 2202 89 293 123 C ATOM 1209 CD2 HIS A 149 1.755 10.897 -19.691 1.00 23.83 C ANISOU 1209 CD2 HIS A 149 2934 3064 3057 109 299 120 C ATOM 1210 ND1 HIS A 149 3.170 12.442 -19.115 1.00 16.26 N ANISOU 1210 ND1 HIS A 149 2023 1953 2204 95 399 0 N ATOM 1211 CE1 HIS A 149 2.293 12.342 -18.136 1.00 19.47 C ANISOU 1211 CE1 HIS A 149 2407 2342 2648 115 474 -82 C ATOM 1212 NE2 HIS A 149 1.416 11.414 -18.465 1.00 29.97 N ANISOU 1212 NE2 HIS A 149 3707 3760 3922 128 416 2 N ATOM 1213 N ARG A 150 5.278 13.967 -22.028 1.00 14.62 N ANISOU 1213 N ARG A 150 1791 1705 2060 49 291 308 N ATOM 1214 CA ARG A 150 6.014 15.213 -21.731 1.00 19.23 C ANISOU 1214 CA ARG A 150 2365 2127 2816 44 374 269 C ATOM 1215 C ARG A 150 6.118 15.618 -20.257 1.00 22.94 C ANISOU 1215 C ARG A 150 2861 2487 3369 40 480 43 C ATOM 1216 O ARG A 150 6.530 16.739 -19.940 1.00 27.02 O ANISOU 1216 O ARG A 150 3351 2845 4072 33 567 -18 O ATOM 1217 CB ARG A 150 5.447 16.397 -22.499 1.00 22.63 C ANISOU 1217 CB ARG A 150 2684 2428 3485 89 399 477 C ATOM 1218 CG ARG A 150 5.298 16.239 -23.990 1.00 26.42 C ANISOU 1218 CG ARG A 150 3119 3038 3882 78 296 733 C ATOM 1219 CD ARG A 150 4.629 17.498 -24.531 1.00 30.29 C ANISOU 1219 CD ARG A 150 3475 3379 4653 133 324 968 C ATOM 1220 NE ARG A 150 4.387 17.384 -25.959 1.00 39.38 N ANISOU 1220 NE ARG A 150 4568 4694 5701 111 212 1247 N ATOM 1221 CZ ARG A 150 3.325 17.857 -26.615 1.00 61.16 C ANISOU 1221 CZ ARG A 150 7194 7449 8597 158 163 1508 C ATOM 1222 NH1 ARG A 150 2.335 18.518 -25.992 1.00 54.64 N1+ ANISOU 1222 NH1 ARG A 150 6265 6429 8069 246 231 1533 N1+ ATOM 1223 NH2 ARG A 150 3.250 17.657 -27.934 1.00 73.19 N ANISOU 1223 NH2 ARG A 150 8673 9182 9953 109 45 1751 N ATOM 1224 N ASP A 151 5.771 14.711 -19.360 1.00 20.19 N ANISOU 1224 N ASP A 151 2559 2231 2881 33 477 -85 N ATOM 1225 CA ASP A 151 5.800 15.002 -17.926 1.00 21.79 C ANISOU 1225 CA ASP A 151 2786 2388 3106 10 575 -303 C ATOM 1226 C ASP A 151 5.675 13.753 -17.085 1.00 16.82 C ANISOU 1226 C ASP A 151 2218 1919 2254 -17 539 -392 C ATOM 1227 O ASP A 151 5.061 13.801 -16.025 1.00 19.06 O ANISOU 1227 O ASP A 151 2497 2205 2540 -20 621 -514 O ATOM 1228 CB ASP A 151 4.692 16.007 -17.521 1.00 29.41 C ANISOU 1228 CB ASP A 151 3662 3188 4324 63 702 -332 C ATOM 1229 CG ASP A 151 4.863 16.555 -16.089 1.00 30.73 C ANISOU 1229 CG ASP A 151 3848 3303 4527 16 834 -602 C ATOM 1230 OD1 ASP A 151 6.004 16.533 -15.582 1.00 32.40 O ANISOU 1230 OD1 ASP A 151 4127 3570 4616 -62 820 -739 O ATOM 1231 OD2 ASP A 151 3.854 16.996 -15.472 1.00 30.81 O1- ANISOU 1231 OD2 ASP A 151 3797 3229 4682 49 955 -686 O1- ATOM 1232 N LEU A 152 6.303 12.657 -17.515 1.00 18.07 N ANISOU 1232 N LEU A 152 2425 2206 2234 -41 431 -337 N ATOM 1233 CA LEU A 152 6.202 11.386 -16.795 1.00 19.70 C ANISOU 1233 CA LEU A 152 2674 2547 2264 -63 390 -378 C ATOM 1234 C LEU A 152 6.912 11.425 -15.442 1.00 20.70 C ANISOU 1234 C LEU A 152 2844 2728 2292 -125 422 -539 C ATOM 1235 O LEU A 152 8.031 11.915 -15.334 1.00 18.57 O ANISOU 1235 O LEU A 152 2594 2444 2018 -170 413 -609 O ATOM 1236 CB LEU A 152 6.752 10.244 -17.616 1.00 17.51 C ANISOU 1236 CB LEU A 152 2419 2361 1874 -74 282 -291 C ATOM 1237 CG LEU A 152 5.814 9.668 -18.650 1.00 28.89 C ANISOU 1237 CG LEU A 152 3821 3830 3327 -40 237 -164 C ATOM 1238 CD1 LEU A 152 6.590 8.654 -19.485 1.00 34.53 C ANISOU 1238 CD1 LEU A 152 4556 4623 3941 -69 155 -132 C ATOM 1239 CD2 LEU A 152 4.606 9.029 -17.978 1.00 28.50 C ANISOU 1239 CD2 LEU A 152 3750 3812 3267 -19 258 -165 C ATOM 1240 N LYS A 153 6.222 10.923 -14.421 1.00 18.28 N ANISOU 1240 N LYS A 153 2545 2501 1900 -137 458 -591 N ATOM 1241 CA LYS A 153 6.745 10.874 -13.060 1.00 20.51 C ANISOU 1241 CA LYS A 153 2861 2890 2041 -212 483 -728 C ATOM 1242 C LYS A 153 5.838 9.998 -12.202 1.00 17.59 C ANISOU 1242 C LYS A 153 2492 2637 1554 -219 506 -710 C ATOM 1243 O LYS A 153 4.710 9.704 -12.599 1.00 21.36 O ANISOU 1243 O LYS A 153 2935 3075 2107 -162 531 -629 O ATOM 1244 CB LYS A 153 6.876 12.285 -12.461 1.00 24.52 C ANISOU 1244 CB LYS A 153 3357 3317 2641 -251 599 -915 C ATOM 1245 CG LYS A 153 5.621 13.120 -12.533 1.00 31.53 C ANISOU 1245 CG LYS A 153 4188 4068 3724 -196 731 -951 C ATOM 1246 CD LYS A 153 5.844 14.497 -11.974 1.00 27.23 C ANISOU 1246 CD LYS A 153 3619 3411 3315 -239 861 -1159 C ATOM 1247 CE LYS A 153 4.604 15.330 -12.205 1.00 34.46 C ANISOU 1247 CE LYS A 153 4451 4148 4494 -164 996 -1166 C ATOM 1248 NZ LYS A 153 4.743 16.660 -11.571 1.00 41.02 N1+ ANISOU 1248 NZ LYS A 153 5244 4842 5499 -209 1153 -1402 N1+ ATOM 1249 N PRO A 154 6.316 9.569 -11.024 1.00 19.35 N ANISOU 1249 N PRO A 154 2744 3019 1590 -296 492 -769 N ATOM 1250 CA PRO A 154 5.480 8.661 -10.232 1.00 17.74 C ANISOU 1250 CA PRO A 154 2535 2939 1268 -310 513 -714 C ATOM 1251 C PRO A 154 4.051 9.142 -9.961 1.00 18.06 C ANISOU 1251 C PRO A 154 2538 2930 1393 -280 656 -775 C ATOM 1252 O PRO A 154 3.124 8.342 -10.042 1.00 20.06 O ANISOU 1252 O PRO A 154 2765 3203 1655 -246 659 -665 O ATOM 1253 CB PRO A 154 6.274 8.513 -8.935 1.00 18.98 C ANISOU 1253 CB PRO A 154 2719 3290 1202 -416 491 -784 C ATOM 1254 CG PRO A 154 7.694 8.660 -9.373 1.00 18.32 C ANISOU 1254 CG PRO A 154 2649 3186 1126 -435 385 -782 C ATOM 1255 CD PRO A 154 7.668 9.706 -10.442 1.00 16.55 C ANISOU 1255 CD PRO A 154 2416 2760 1113 -378 432 -843 C ATOM 1256 N ALA A 155 3.859 10.435 -9.709 1.00 18.71 N ANISOU 1256 N ALA A 155 2604 2929 1577 -290 779 -951 N ATOM 1257 CA ALA A 155 2.518 10.957 -9.392 1.00 18.83 C ANISOU 1257 CA ALA A 155 2562 2881 1710 -259 937 -1027 C ATOM 1258 C ALA A 155 1.510 10.893 -10.550 1.00 19.77 C ANISOU 1258 C ALA A 155 2615 2848 2050 -148 927 -875 C ATOM 1259 O ALA A 155 0.298 10.982 -10.324 1.00 21.60 O ANISOU 1259 O ALA A 155 2783 3050 2375 -113 1033 -884 O ATOM 1260 CB ALA A 155 2.624 12.374 -8.887 1.00 22.03 C ANISOU 1260 CB ALA A 155 2949 3202 2221 -296 1084 -1268 C ATOM 1261 N ASN A 156 2.020 10.759 -11.772 1.00 17.25 N ANISOU 1261 N ASN A 156 2301 2450 1803 -101 803 -741 N ATOM 1262 CA ASN A 156 1.209 10.553 -12.965 1.00 16.62 C ANISOU 1262 CA ASN A 156 2159 2280 1874 -19 754 -576 C ATOM 1263 C ASN A 156 1.028 9.085 -13.381 1.00 15.91 C ANISOU 1263 C ASN A 156 2081 2288 1675 -18 637 -428 C ATOM 1264 O ASN A 156 0.373 8.806 -14.381 1.00 22.35 O ANISOU 1264 O ASN A 156 2844 3063 2585 29 583 -306 O ATOM 1265 CB ASN A 156 1.801 11.391 -14.101 1.00 21.92 C ANISOU 1265 CB ASN A 156 2818 2823 2689 16 705 -522 C ATOM 1266 CG ASN A 156 1.619 12.895 -13.866 1.00 29.71 C ANISOU 1266 CG ASN A 156 3751 3650 3888 35 841 -636 C ATOM 1267 ND2 ASN A 156 2.492 13.704 -14.445 1.00 27.13 N ANISOU 1267 ND2 ASN A 156 3431 3224 3654 33 820 -634 N ATOM 1268 OD1 ASN A 156 0.696 13.314 -13.169 1.00 42.32 O ANISOU 1268 OD1 ASN A 156 5292 5203 5584 51 975 -729 O ATOM 1269 N ILE A 157 1.602 8.153 -12.619 1.00 15.94 N ANISOU 1269 N ILE A 157 2141 2422 1493 -77 597 -435 N ATOM 1270 CA ILE A 157 1.343 6.723 -12.773 1.00 14.35 C ANISOU 1270 CA ILE A 157 1935 2291 1226 -82 518 -310 C ATOM 1271 C ILE A 157 0.355 6.299 -11.679 1.00 15.79 C ANISOU 1271 C ILE A 157 2090 2555 1354 -105 611 -316 C ATOM 1272 O ILE A 157 0.745 6.047 -10.538 1.00 18.84 O ANISOU 1272 O ILE A 157 2513 3063 1580 -168 640 -354 O ATOM 1273 CB ILE A 157 2.638 5.872 -12.690 1.00 17.16 C ANISOU 1273 CB ILE A 157 2346 2718 1457 -124 412 -271 C ATOM 1274 CG1 ILE A 157 3.774 6.473 -13.537 1.00 18.73 C ANISOU 1274 CG1 ILE A 157 2573 2853 1690 -117 351 -301 C ATOM 1275 CG2 ILE A 157 2.368 4.426 -13.114 1.00 15.78 C ANISOU 1275 CG2 ILE A 157 2146 2557 1293 -119 338 -144 C ATOM 1276 CD1 ILE A 157 3.419 6.900 -14.946 1.00 17.43 C ANISOU 1276 CD1 ILE A 157 2374 2588 1659 -65 327 -253 C ATOM 1277 N LEU A 158 -0.925 6.246 -12.039 1.00 13.20 N ANISOU 1277 N LEU A 158 1688 2175 1153 -61 656 -268 N ATOM 1278 CA LEU A 158 -1.976 5.809 -11.131 1.00 16.60 C ANISOU 1278 CA LEU A 158 2076 2674 1558 -81 755 -260 C ATOM 1279 C LEU A 158 -2.044 4.290 -11.129 1.00 16.37 C ANISOU 1279 C LEU A 158 2044 2709 1469 -109 674 -121 C ATOM 1280 O LEU A 158 -1.686 3.644 -12.105 1.00 19.07 O ANISOU 1280 O LEU A 158 2386 3002 1857 -94 557 -45 O ATOM 1281 CB LEU A 158 -3.341 6.369 -11.554 1.00 16.90 C ANISOU 1281 CB LEU A 158 2009 2617 1794 -19 836 -257 C ATOM 1282 CG LEU A 158 -3.442 7.865 -11.861 1.00 18.68 C ANISOU 1282 CG LEU A 158 2198 2717 2181 32 911 -351 C ATOM 1283 CD1 LEU A 158 -4.890 8.258 -12.148 1.00 17.11 C ANISOU 1283 CD1 LEU A 158 1867 2432 2201 96 991 -314 C ATOM 1284 CD2 LEU A 158 -2.906 8.678 -10.696 1.00 18.76 C ANISOU 1284 CD2 LEU A 158 2259 2765 2104 -17 1038 -540 C ATOM 1285 N VAL A 159 -2.538 3.724 -10.040 1.00 15.85 N ANISOU 1285 N VAL A 159 1965 2748 1311 -156 749 -92 N ATOM 1286 CA VAL A 159 -2.758 2.289 -9.952 1.00 15.61 C ANISOU 1286 CA VAL A 159 1910 2753 1269 -183 694 59 C ATOM 1287 C VAL A 159 -4.114 2.064 -9.332 1.00 12.33 C ANISOU 1287 C VAL A 159 1419 2376 889 -196 816 88 C ATOM 1288 O VAL A 159 -4.397 2.575 -8.256 1.00 15.10 O ANISOU 1288 O VAL A 159 1775 2829 1133 -232 945 15 O ATOM 1289 CB VAL A 159 -1.680 1.586 -9.110 1.00 16.52 C ANISOU 1289 CB VAL A 159 2082 2984 1211 -246 641 130 C ATOM 1290 CG1 VAL A 159 -2.004 0.107 -8.940 1.00 16.57 C ANISOU 1290 CG1 VAL A 159 2041 3000 1255 -272 605 310 C ATOM 1291 CG2 VAL A 159 -0.329 1.756 -9.774 1.00 17.48 C ANISOU 1291 CG2 VAL A 159 2260 3058 1326 -230 523 104 C ATOM 1292 N MET A 160 -4.921 1.253 -10.001 1.00 13.27 N ANISOU 1292 N MET A 160 1464 2425 1153 -178 779 184 N ATOM 1293 CA MET A 160 -6.288 0.987 -9.563 1.00 15.58 C ANISOU 1293 CA MET A 160 1663 2737 1518 -188 889 222 C ATOM 1294 C MET A 160 -6.310 0.127 -8.300 1.00 17.08 C ANISOU 1294 C MET A 160 1862 3061 1569 -264 953 323 C ATOM 1295 O MET A 160 -5.466 -0.765 -8.113 1.00 17.01 O ANISOU 1295 O MET A 160 1894 3082 1487 -301 864 434 O ATOM 1296 CB MET A 160 -7.096 0.321 -10.683 1.00 13.40 C ANISOU 1296 CB MET A 160 1295 2356 1439 -163 814 293 C ATOM 1297 CG MET A 160 -7.304 1.186 -11.914 1.00 10.79 C ANISOU 1297 CG MET A 160 929 1934 1235 -99 753 231 C ATOM 1298 SD MET A 160 -8.316 2.640 -11.593 1.00 18.42 S ANISOU 1298 SD MET A 160 1817 2876 2306 -41 904 143 S ATOM 1299 CE MET A 160 -9.961 1.943 -11.451 1.00 14.84 C ANISOU 1299 CE MET A 160 1210 2425 2005 -52 975 225 C ATOM 1300 N GLY A 161 -7.278 0.425 -7.440 1.00 17.77 N ANISOU 1300 N GLY A 161 1897 3227 1628 -288 1114 294 N ATOM 1301 CA GLY A 161 -7.500 -0.312 -6.211 1.00 24.70 C ANISOU 1301 CA GLY A 161 2766 4260 2360 -371 1199 404 C ATOM 1302 C GLY A 161 -8.479 -1.457 -6.387 1.00 27.85 C ANISOU 1302 C GLY A 161 3063 4605 2915 -385 1206 563 C ATOM 1303 O GLY A 161 -8.664 -1.961 -7.496 1.00 26.15 O ANISOU 1303 O GLY A 161 2803 4240 2895 -346 1099 600 O ATOM 1304 N GLU A 162 -9.114 -1.855 -5.286 1.00 26.02 N ANISOU 1304 N GLU A 162 2788 4508 2590 -454 1340 647 N ATOM 1305 CA GLU A 162 -10.034 -2.988 -5.292 1.00 33.79 C ANISOU 1305 CA GLU A 162 3667 5448 3723 -484 1364 815 C ATOM 1306 C GLU A 162 -11.164 -2.710 -6.265 1.00 32.19 C ANISOU 1306 C GLU A 162 3357 5096 3778 -422 1379 735 C ATOM 1307 O GLU A 162 -11.699 -1.604 -6.279 1.00 48.81 O ANISOU 1307 O GLU A 162 5434 7203 5908 -379 1477 583 O ATOM 1308 CB GLU A 162 -10.618 -3.275 -3.889 1.00 34.45 C ANISOU 1308 CB GLU A 162 3715 5727 3646 -575 1536 912 C ATOM 1309 CG GLU A 162 -9.614 -3.749 -2.832 1.00 39.56 C ANISOU 1309 CG GLU A 162 4441 6568 4021 -660 1509 1060 C ATOM 1310 CD GLU A 162 -8.977 -5.120 -3.109 1.00 43.07 C ANISOU 1310 CD GLU A 162 4874 6922 4569 -673 1353 1310 C ATOM 1311 OE1 GLU A 162 -9.474 -5.896 -3.966 1.00 39.59 O ANISOU 1311 OE1 GLU A 162 4354 6282 4407 -642 1299 1374 O ATOM 1312 OE2 GLU A 162 -7.958 -5.429 -2.449 1.00 41.05 O1- ANISOU 1312 OE2 GLU A 162 4676 6796 4126 -722 1286 1441 O1- ATOM 1313 N GLY A 163 -11.496 -3.717 -7.074 1.00 29.24 N ANISOU 1313 N GLY A 163 2912 4592 3606 -423 1280 837 N ATOM 1314 CA GLY A 163 -12.567 -3.653 -8.066 1.00 23.01 C ANISOU 1314 CA GLY A 163 2002 3682 3058 -385 1260 789 C ATOM 1315 C GLY A 163 -12.126 -4.431 -9.286 1.00 23.89 C ANISOU 1315 C GLY A 163 2112 3661 3306 -382 1077 811 C ATOM 1316 O GLY A 163 -11.122 -5.165 -9.223 1.00 19.97 O ANISOU 1316 O GLY A 163 1687 3144 2755 -409 998 881 O ATOM 1317 N PRO A 164 -12.854 -4.279 -10.409 1.00 24.49 N ANISOU 1317 N PRO A 164 2094 3652 3560 -354 1008 748 N ATOM 1318 CA PRO A 164 -12.533 -5.026 -11.636 1.00 25.10 C ANISOU 1318 CA PRO A 164 2157 3628 3753 -374 845 732 C ATOM 1319 C PRO A 164 -11.132 -4.868 -12.223 1.00 23.29 C ANISOU 1319 C PRO A 164 2056 3376 3417 -349 725 669 C ATOM 1320 O PRO A 164 -10.700 -5.751 -12.961 1.00 21.07 O ANISOU 1320 O PRO A 164 1772 3016 3219 -385 626 660 O ATOM 1321 CB PRO A 164 -13.586 -4.554 -12.649 1.00 25.97 C ANISOU 1321 CB PRO A 164 2141 3715 4010 -352 796 668 C ATOM 1322 CG PRO A 164 -14.423 -3.528 -11.952 1.00 31.11 C ANISOU 1322 CG PRO A 164 2735 4425 4662 -303 939 660 C ATOM 1323 CD PRO A 164 -14.204 -3.692 -10.478 1.00 28.67 C ANISOU 1323 CD PRO A 164 2487 4187 4218 -330 1095 717 C ATOM 1324 N GLU A 165 -10.436 -3.775 -11.914 1.00 28.19 N ANISOU 1324 N GLU A 165 2778 4057 3877 -296 746 611 N ATOM 1325 CA GLU A 165 -9.119 -3.496 -12.516 1.00 24.55 C ANISOU 1325 CA GLU A 165 2428 3577 3322 -271 637 546 C ATOM 1326 C GLU A 165 -7.980 -3.470 -11.500 1.00 27.19 C ANISOU 1326 C GLU A 165 2877 3971 3483 -277 668 583 C ATOM 1327 O GLU A 165 -6.983 -2.729 -11.662 1.00 18.30 O ANISOU 1327 O GLU A 165 1845 2864 2245 -244 624 512 O ATOM 1328 CB GLU A 165 -9.181 -2.177 -13.267 1.00 16.81 C ANISOU 1328 CB GLU A 165 1456 2604 2328 -208 605 448 C ATOM 1329 CG GLU A 165 -10.239 -2.160 -14.335 1.00 19.22 C ANISOU 1329 CG GLU A 165 1637 2881 2787 -207 545 439 C ATOM 1330 CD GLU A 165 -10.086 -0.965 -15.239 1.00 17.42 C ANISOU 1330 CD GLU A 165 1414 2658 2548 -149 479 387 C ATOM 1331 OE1 GLU A 165 -9.229 -0.993 -16.135 1.00 17.31 O ANISOU 1331 OE1 GLU A 165 1460 2640 2476 -157 368 350 O ATOM 1332 OE2 GLU A 165 -10.814 0.003 -15.038 1.00 27.04 O1- ANISOU 1332 OE2 GLU A 165 2567 3879 3828 -97 548 391 O1- ATOM 1333 N ARG A 166 -8.123 -4.314 -10.481 1.00 23.50 N ANISOU 1333 N ARG A 166 2390 3541 2999 -327 734 711 N ATOM 1334 CA ARG A 166 -7.189 -4.388 -9.375 1.00 23.51 C ANISOU 1334 CA ARG A 166 2473 3641 2820 -351 760 789 C ATOM 1335 C ARG A 166 -5.754 -4.428 -9.876 1.00 21.74 C ANISOU 1335 C ARG A 166 2332 3375 2553 -331 637 760 C ATOM 1336 O ARG A 166 -5.423 -5.265 -10.705 1.00 29.36 O ANISOU 1336 O ARG A 166 3271 4220 3665 -333 550 775 O ATOM 1337 CB ARG A 166 -7.476 -5.630 -8.546 1.00 26.19 C ANISOU 1337 CB ARG A 166 2753 3995 3203 -416 804 986 C ATOM 1338 CG ARG A 166 -6.763 -5.646 -7.208 1.00 32.32 C ANISOU 1338 CG ARG A 166 3588 4934 3756 -458 843 1107 C ATOM 1339 CD ARG A 166 -7.190 -6.870 -6.422 1.00 32.00 C ANISOU 1339 CD ARG A 166 3469 4913 3778 -525 892 1344 C ATOM 1340 NE ARG A 166 -6.784 -6.837 -5.018 1.00 30.90 N ANISOU 1340 NE ARG A 166 3366 4990 3385 -586 947 1488 N ATOM 1341 CZ ARG A 166 -5.576 -7.141 -4.549 1.00 27.99 C ANISOU 1341 CZ ARG A 166 3044 4692 2900 -605 858 1616 C ATOM 1342 NH1 ARG A 166 -4.573 -7.519 -5.352 1.00 23.72 N1+ ANISOU 1342 NH1 ARG A 166 2519 3999 2495 -559 720 1613 N1+ ATOM 1343 NH2 ARG A 166 -5.382 -7.076 -3.238 1.00 33.79 N ANISOU 1343 NH2 ARG A 166 3796 5669 3374 -680 911 1753 N ATOM 1344 N GLY A 167 -4.935 -3.490 -9.402 1.00 20.90 N ANISOU 1344 N GLY A 167 2316 3365 2259 -317 641 696 N ATOM 1345 CA GLY A 167 -3.509 -3.459 -9.691 1.00 16.52 C ANISOU 1345 CA GLY A 167 1834 2793 1648 -303 537 678 C ATOM 1346 C GLY A 167 -3.140 -3.124 -11.121 1.00 16.31 C ANISOU 1346 C GLY A 167 1824 2653 1722 -257 450 553 C ATOM 1347 O GLY A 167 -2.085 -3.523 -11.585 1.00 21.31 O ANISOU 1347 O GLY A 167 2485 3232 2381 -252 365 555 O ATOM 1348 N ARG A 168 -3.992 -2.403 -11.833 1.00 14.40 N ANISOU 1348 N ARG A 168 1553 2381 1538 -226 472 456 N ATOM 1349 CA ARG A 168 -3.681 -2.015 -13.204 1.00 15.16 C ANISOU 1349 CA ARG A 168 1659 2407 1695 -194 387 359 C ATOM 1350 C ARG A 168 -3.197 -0.570 -13.230 1.00 14.36 C ANISOU 1350 C ARG A 168 1623 2341 1493 -154 401 266 C ATOM 1351 O ARG A 168 -3.832 0.319 -12.660 1.00 19.07 O ANISOU 1351 O ARG A 168 2209 2975 2061 -137 492 231 O ATOM 1352 CB ARG A 168 -4.904 -2.179 -14.088 1.00 20.26 C ANISOU 1352 CB ARG A 168 2210 3010 2479 -195 377 344 C ATOM 1353 CG ARG A 168 -4.651 -1.883 -15.556 1.00 24.91 C ANISOU 1353 CG ARG A 168 2796 3567 3101 -184 279 265 C ATOM 1354 CD ARG A 168 -5.911 -2.143 -16.357 1.00 26.69 C ANISOU 1354 CD ARG A 168 2910 3786 3445 -205 252 265 C ATOM 1355 NE ARG A 168 -6.067 -3.561 -16.644 1.00 29.23 N ANISOU 1355 NE ARG A 168 3177 4055 3872 -269 222 269 N ATOM 1356 CZ ARG A 168 -7.150 -4.113 -17.175 1.00 37.73 C ANISOU 1356 CZ ARG A 168 4144 5123 5067 -313 201 264 C ATOM 1357 NH1 ARG A 168 -8.236 -3.382 -17.465 1.00 36.10 N1+ ANISOU 1357 NH1 ARG A 168 3859 4968 4888 -294 199 279 N1+ ATOM 1358 NH2 ARG A 168 -7.150 -5.422 -17.408 1.00 39.96 N ANISOU 1358 NH2 ARG A 168 4381 5335 5468 -380 184 244 N ATOM 1359 N VAL A 169 -2.075 -0.347 -13.897 1.00 13.12 N ANISOU 1359 N VAL A 169 1523 2159 1304 -143 324 219 N ATOM 1360 CA VAL A 169 -1.550 0.987 -14.096 1.00 13.30 C ANISOU 1360 CA VAL A 169 1598 2189 1268 -111 330 136 C ATOM 1361 C VAL A 169 -2.511 1.783 -14.980 1.00 17.96 C ANISOU 1361 C VAL A 169 2128 2741 1953 -73 336 114 C ATOM 1362 O VAL A 169 -3.056 1.238 -15.958 1.00 18.54 O ANISOU 1362 O VAL A 169 2142 2795 2106 -81 274 141 O ATOM 1363 CB VAL A 169 -0.166 0.924 -14.756 1.00 15.78 C ANISOU 1363 CB VAL A 169 1967 2480 1547 -114 244 106 C ATOM 1364 CG1 VAL A 169 0.311 2.304 -15.204 1.00 16.91 C ANISOU 1364 CG1 VAL A 169 2149 2610 1665 -84 246 33 C ATOM 1365 CG2 VAL A 169 0.836 0.321 -13.794 1.00 19.51 C ANISOU 1365 CG2 VAL A 169 2480 2993 1940 -143 232 147 C ATOM 1366 N LYS A 170 -2.721 3.053 -14.615 1.00 14.03 N ANISOU 1366 N LYS A 170 1634 2237 1459 -38 411 64 N ATOM 1367 CA LYS A 170 -3.343 4.051 -15.492 1.00 11.80 C ANISOU 1367 CA LYS A 170 1291 1901 1291 10 407 68 C ATOM 1368 C LYS A 170 -2.457 5.305 -15.565 1.00 13.28 C ANISOU 1368 C LYS A 170 1533 2047 1465 35 425 6 C ATOM 1369 O LYS A 170 -2.307 6.041 -14.594 1.00 14.63 O ANISOU 1369 O LYS A 170 1730 2209 1619 38 526 -77 O ATOM 1370 CB LYS A 170 -4.730 4.445 -15.008 1.00 11.94 C ANISOU 1370 CB LYS A 170 1213 1902 1421 40 509 79 C ATOM 1371 CG LYS A 170 -5.706 3.299 -14.861 1.00 12.73 C ANISOU 1371 CG LYS A 170 1243 2036 1557 11 509 142 C ATOM 1372 CD LYS A 170 -6.194 2.752 -16.194 1.00 12.36 C ANISOU 1372 CD LYS A 170 1122 1986 1587 1 386 208 C ATOM 1373 CE LYS A 170 -7.392 1.830 -15.959 1.00 9.11 C ANISOU 1373 CE LYS A 170 611 1590 1258 -28 410 257 C ATOM 1374 NZ LYS A 170 -7.750 1.077 -17.180 1.00 9.90 N1+ ANISOU 1374 NZ LYS A 170 645 1710 1407 -69 284 290 N1+ ATOM 1375 N ILE A 171 -1.854 5.528 -16.723 1.00 14.64 N ANISOU 1375 N ILE A 171 1717 2202 1644 41 332 37 N ATOM 1376 CA ILE A 171 -1.103 6.733 -16.969 1.00 13.56 C ANISOU 1376 CA ILE A 171 1612 2010 1531 63 346 5 C ATOM 1377 C ILE A 171 -2.082 7.902 -17.062 1.00 14.01 C ANISOU 1377 C ILE A 171 1577 1983 1764 121 417 35 C ATOM 1378 O ILE A 171 -3.099 7.827 -17.730 1.00 11.97 O ANISOU 1378 O ILE A 171 1223 1725 1602 147 382 135 O ATOM 1379 CB ILE A 171 -0.239 6.582 -18.230 1.00 18.18 C ANISOU 1379 CB ILE A 171 2224 2616 2068 44 235 49 C ATOM 1380 CG1 ILE A 171 0.837 5.524 -17.966 1.00 15.63 C ANISOU 1380 CG1 ILE A 171 1978 2343 1618 -4 194 -2 C ATOM 1381 CG2 ILE A 171 0.427 7.909 -18.628 1.00 18.93 C ANISOU 1381 CG2 ILE A 171 2331 2643 2217 66 251 52 C ATOM 1382 CD1 ILE A 171 1.522 5.033 -19.211 1.00 23.44 C ANISOU 1382 CD1 ILE A 171 2977 3366 2562 -34 103 17 C ATOM 1383 N ALA A 172 -1.747 8.980 -16.364 1.00 20.79 N ANISOU 1383 N ALA A 172 2454 2765 2680 137 521 -57 N ATOM 1384 CA ALA A 172 -2.623 10.136 -16.195 1.00 22.45 C ANISOU 1384 CA ALA A 172 2567 2858 3105 196 630 -62 C ATOM 1385 C ALA A 172 -1.893 11.427 -16.500 1.00 18.84 C ANISOU 1385 C ALA A 172 2114 2280 2764 217 660 -84 C ATOM 1386 O ALA A 172 -0.664 11.444 -16.591 1.00 18.01 O ANISOU 1386 O ALA A 172 2100 2199 2546 175 615 -129 O ATOM 1387 CB ALA A 172 -3.146 10.176 -14.760 1.00 24.71 C ANISOU 1387 CB ALA A 172 2850 3153 3386 183 785 -206 C ATOM 1388 N ASP A 173 -2.688 12.483 -16.628 1.00 20.57 N ANISOU 1388 N ASP A 173 2218 2360 3238 281 744 -47 N ATOM 1389 CA ASP A 173 -2.278 13.880 -16.816 1.00 34.07 C ANISOU 1389 CA ASP A 173 3889 3898 5156 314 813 -60 C ATOM 1390 C ASP A 173 -1.117 14.126 -17.769 1.00 36.24 C ANISOU 1390 C ASP A 173 4220 4175 5374 290 704 31 C ATOM 1391 O ASP A 173 -0.074 14.666 -17.381 1.00 30.04 O ANISOU 1391 O ASP A 173 3504 3337 4574 253 750 -93 O ATOM 1392 CB ASP A 173 -2.028 14.573 -15.464 1.00 47.51 C ANISOU 1392 CB ASP A 173 5621 5521 6911 288 994 -314 C ATOM 1393 CG ASP A 173 -2.143 16.110 -15.551 1.00 61.69 C ANISOU 1393 CG ASP A 173 7315 7077 9049 340 1119 -341 C ATOM 1394 OD1 ASP A 173 -2.836 16.640 -16.464 1.00 46.46 O ANISOU 1394 OD1 ASP A 173 5254 5031 7366 419 1091 -136 O ATOM 1395 OD2 ASP A 173 -1.539 16.789 -14.692 1.00 68.47 O1- ANISOU 1395 OD2 ASP A 173 8213 7862 9940 295 1245 -566 O1- ATOM 1396 N MET A 174 -1.325 13.741 -19.025 1.00 32.97 N ANISOU 1396 N MET A 174 3767 3835 4924 301 563 241 N ATOM 1397 CA MET A 174 -0.344 13.969 -20.080 1.00 33.32 C ANISOU 1397 CA MET A 174 3846 3905 4908 274 466 354 C ATOM 1398 C MET A 174 -0.064 15.467 -20.161 1.00 41.70 C ANISOU 1398 C MET A 174 4845 4766 6233 312 553 389 C ATOM 1399 O MET A 174 -0.976 16.283 -19.945 1.00 41.66 O ANISOU 1399 O MET A 174 4718 4608 6501 379 644 430 O ATOM 1400 CB MET A 174 -0.853 13.451 -21.438 1.00 42.72 C ANISOU 1400 CB MET A 174 4975 5228 6030 272 317 578 C ATOM 1401 CG MET A 174 -0.843 11.936 -21.636 1.00 35.65 C ANISOU 1401 CG MET A 174 4146 4524 4876 213 219 534 C ATOM 1402 SD MET A 174 -1.695 10.985 -20.355 1.00 40.75 S ANISOU 1402 SD MET A 174 4803 5191 5489 218 286 384 S ATOM 1403 CE MET A 174 -3.397 11.158 -20.877 1.00 51.23 C ANISOU 1403 CE MET A 174 5953 6513 6997 273 258 558 C ATOM 1404 N GLY A 175 1.197 15.816 -20.431 1.00 34.07 N ANISOU 1404 N GLY A 175 3951 3784 5212 267 538 367 N ATOM 1405 CA GLY A 175 1.667 17.212 -20.511 1.00 37.82 C ANISOU 1405 CA GLY A 175 4373 4055 5942 285 623 390 C ATOM 1406 C GLY A 175 0.882 18.021 -21.514 1.00 35.31 C ANISOU 1406 C GLY A 175 3902 3638 5877 353 598 675 C ATOM 1407 O GLY A 175 1.324 18.251 -22.634 1.00 39.89 O ANISOU 1407 O GLY A 175 4460 4263 6432 336 508 888 O ATOM 1408 N PHE A 176 -0.311 18.407 -21.087 1.00 46.45 N ANISOU 1408 N PHE A 176 5194 4929 7524 426 679 686 N ATOM 1409 CA PHE A 176 -1.231 19.182 -21.870 1.00 59.02 C ANISOU 1409 CA PHE A 176 6607 6409 9411 505 661 966 C ATOM 1410 C PHE A 176 -1.037 20.609 -21.370 1.00 64.45 C ANISOU 1410 C PHE A 176 7213 6786 10491 547 834 900 C ATOM 1411 O PHE A 176 -1.243 20.854 -20.180 1.00 64.89 O ANISOU 1411 O PHE A 176 7275 6715 10664 555 996 626 O ATOM 1412 CB PHE A 176 -2.677 18.747 -21.599 1.00 66.64 C ANISOU 1412 CB PHE A 176 7468 7404 10448 564 666 995 C ATOM 1413 CG PHE A 176 -2.996 17.334 -22.023 1.00 71.43 C ANISOU 1413 CG PHE A 176 8134 8291 10714 518 512 1036 C ATOM 1414 CD1 PHE A 176 -2.699 16.884 -23.310 1.00 65.58 C ANISOU 1414 CD1 PHE A 176 7405 7743 9768 470 333 1251 C ATOM 1415 CD2 PHE A 176 -3.638 16.457 -21.140 1.00 68.94 C ANISOU 1415 CD2 PHE A 176 7852 8048 10294 513 555 857 C ATOM 1416 CE1 PHE A 176 -3.017 15.583 -23.691 1.00 75.37 C ANISOU 1416 CE1 PHE A 176 8688 9225 10722 416 207 1251 C ATOM 1417 CE2 PHE A 176 -3.957 15.160 -21.523 1.00 74.98 C ANISOU 1417 CE2 PHE A 176 8658 9041 10792 466 423 890 C ATOM 1418 CZ PHE A 176 -3.652 14.722 -22.802 1.00 66.20 C ANISOU 1418 CZ PHE A 176 7555 8102 9497 418 251 1073 C ATOM 1419 N ALA A 177 -0.601 21.555 -22.201 1.00 74.80 N ANISOU 1419 N ALA A 177 8447 7968 12004 561 817 1124 N ATOM 1420 CA ALA A 177 -0.002 21.353 -23.526 1.00 70.80 C ANISOU 1420 CA ALA A 177 7962 7632 11306 516 649 1402 C ATOM 1421 C ALA A 177 1.271 22.201 -23.535 1.00 75.54 C ANISOU 1421 C ALA A 177 8608 8083 12012 471 722 1354 C ATOM 1422 O ALA A 177 1.626 22.791 -22.496 1.00 72.46 O ANISOU 1422 O ALA A 177 8238 7486 11807 467 883 1084 O ATOM 1423 CB ALA A 177 -0.967 21.795 -24.620 1.00 62.96 C ANISOU 1423 CB ALA A 177 6779 6637 10508 582 553 1808 C ATOM 1424 N ARG A 178 1.971 22.235 -24.673 1.00 58.61 N ANISOU 1424 N ARG A 178 6477 6057 9735 423 611 1594 N ATOM 1425 CA ARG A 178 3.198 23.037 -24.814 1.00 60.50 C ANISOU 1425 CA ARG A 178 6744 6164 10081 373 673 1589 C ATOM 1426 C ARG A 178 3.187 23.748 -26.166 1.00 64.97 C ANISOU 1426 C ARG A 178 7182 6723 10781 382 597 2024 C ATOM 1427 O ARG A 178 3.072 23.084 -27.202 1.00 68.14 O ANISOU 1427 O ARG A 178 7593 7405 10892 346 441 2247 O ATOM 1428 CB ARG A 178 4.457 22.166 -24.672 1.00 49.63 C ANISOU 1428 CB ARG A 178 5555 4986 8316 270 629 1372 C ATOM 1429 CG ARG A 178 4.483 21.243 -23.453 1.00 47.27 C ANISOU 1429 CG ARG A 178 5383 4768 7810 249 662 1006 C ATOM 1430 CD ARG A 178 4.601 21.967 -22.116 1.00 51.42 C ANISOU 1430 CD ARG A 178 5907 5055 8578 254 834 708 C ATOM 1431 NE ARG A 178 3.806 21.293 -21.075 1.00 64.88 N ANISOU 1431 NE ARG A 178 7645 6817 10188 276 873 486 N ATOM 1432 CZ ARG A 178 4.218 20.300 -20.270 1.00 60.78 C ANISOU 1432 CZ ARG A 178 7261 6471 9362 218 852 242 C ATOM 1433 NH1 ARG A 178 5.458 19.809 -20.328 1.00 61.01 N1+ ANISOU 1433 NH1 ARG A 178 7403 6628 9151 139 788 164 N1+ ATOM 1434 NH2 ARG A 178 3.370 19.783 -19.381 1.00 56.04 N ANISOU 1434 NH2 ARG A 178 6670 5916 8708 240 898 90 N ATOM 1435 N LEU A 179 3.286 25.086 -26.143 1.00 52.77 N ANISOU 1435 N LEU A 179 5508 4862 9679 422 712 2142 N ATOM 1436 CA LEU A 179 3.260 25.914 -27.360 1.00 57.57 C ANISOU 1436 CA LEU A 179 5968 5425 10480 436 655 2601 C ATOM 1437 C LEU A 179 4.441 25.578 -28.303 1.00 62.03 C ANISOU 1437 C LEU A 179 6636 6234 10701 323 561 2723 C ATOM 1438 O LEU A 179 5.598 25.492 -27.855 1.00 43.17 O ANISOU 1438 O LEU A 179 4374 3822 8206 251 629 2462 O ATOM 1439 CB LEU A 179 3.272 27.407 -26.997 1.00 61.23 C ANISOU 1439 CB LEU A 179 6277 5453 11534 495 827 2655 C ATOM 1440 CG LEU A 179 2.155 27.969 -26.185 0.00 66.33 C ANISOU 1440 CG LEU A 179 6781 5809 12612 608 955 2563 C ATOM 1441 CD1 LEU A 179 2.581 29.104 -25.264 0.00 68.08 C ANISOU 1441 CD1 LEU A 179 6951 5613 13305 619 1185 2311 C ATOM 1442 CD2 LEU A 179 1.041 28.418 -27.120 0.00 68.81 C ANISOU 1442 CD2 LEU A 179 6869 6093 13183 702 864 3053 C ATOM 1443 N PHE A 180 4.123 25.366 -29.589 1.00 62.25 N ANISOU 1443 N PHE A 180 6597 6513 10542 300 408 3110 N ATOM 1444 CA PHE A 180 5.076 24.888 -30.622 1.00 56.79 C ANISOU 1444 CA PHE A 180 5993 6126 9457 182 313 3236 C ATOM 1445 C PHE A 180 5.778 23.528 -30.308 1.00 55.33 C ANISOU 1445 C PHE A 180 6020 6200 8804 100 280 2865 C ATOM 1446 O PHE A 180 6.871 23.248 -30.826 1.00 51.38 O ANISOU 1446 O PHE A 180 5607 5857 8057 4 270 2845 O ATOM 1447 CB PHE A 180 6.099 25.997 -30.946 1.00 50.88 C ANISOU 1447 CB PHE A 180 5198 5183 8951 143 406 3394 C ATOM 1448 CG PHE A 180 5.481 27.275 -31.394 0.00 56.88 C ANISOU 1448 CG PHE A 180 5737 5698 10177 216 431 3810 C ATOM 1449 CD1 PHE A 180 5.114 27.479 -32.714 0.00 58.82 C ANISOU 1449 CD1 PHE A 180 5858 6151 10340 192 297 4311 C ATOM 1450 CD2 PHE A 180 5.252 28.286 -30.476 0.00 57.67 C ANISOU 1450 CD2 PHE A 180 5739 5356 10815 304 593 3700 C ATOM 1451 CE1 PHE A 180 4.531 28.667 -33.111 0.00 62.14 C ANISOU 1451 CE1 PHE A 180 6051 6331 11226 267 313 4738 C ATOM 1452 CE2 PHE A 180 4.669 29.477 -30.866 0.00 61.08 C ANISOU 1452 CE2 PHE A 180 5944 5518 11745 382 629 4090 C ATOM 1453 CZ PHE A 180 4.308 29.668 -32.186 0.00 63.28 C ANISOU 1453 CZ PHE A 180 6091 5996 11956 370 483 4631 C ATOM 1454 N ASN A 181 5.129 22.679 -29.494 1.00 54.70 N ANISOU 1454 N ASN A 181 6005 6159 8619 139 268 2594 N ATOM 1455 CA ASN A 181 5.747 21.472 -28.908 1.00 45.67 C ANISOU 1455 CA ASN A 181 5041 5173 7138 84 264 2223 C ATOM 1456 C ASN A 181 7.127 21.766 -28.237 1.00 49.71 C ANISOU 1456 C ASN A 181 5650 5540 7697 37 377 1971 C ATOM 1457 O ASN A 181 8.043 20.934 -28.292 1.00 45.45 O ANISOU 1457 O ASN A 181 5232 5176 6862 -37 352 1802 O ATOM 1458 CB ASN A 181 5.827 20.352 -29.969 1.00 45.19 C ANISOU 1458 CB ASN A 181 5037 5495 6640 -1 124 2305 C ATOM 1459 CG ASN A 181 6.287 19.005 -29.393 1.00 47.20 C ANISOU 1459 CG ASN A 181 5448 5893 6593 -44 116 1947 C ATOM 1460 ND2 ASN A 181 7.317 18.412 -29.993 1.00 35.16 N ANISOU 1460 ND2 ASN A 181 4007 4560 4793 -138 96 1889 N ATOM 1461 OD1 ASN A 181 5.730 18.517 -28.416 1.00 55.06 O ANISOU 1461 OD1 ASN A 181 6478 6821 7620 6 136 1736 O ATOM 1462 N SER A 182 7.238 22.941 -27.591 1.00 59.90 N ANISOU 1462 N SER A 182 6872 6506 9381 79 504 1939 N ATOM 1463 CA SER A 182 8.514 23.489 -27.042 1.00 72.17 C ANISOU 1463 CA SER A 182 8478 7894 11049 24 612 1741 C ATOM 1464 C SER A 182 8.520 23.632 -25.488 1.00 78.04 C ANISOU 1464 C SER A 182 9266 8438 11949 45 727 1353 C ATOM 1465 O SER A 182 7.538 24.123 -24.906 1.00 69.81 O ANISOU 1465 O SER A 182 8143 7210 11173 121 797 1321 O ATOM 1466 CB SER A 182 8.820 24.863 -27.679 1.00 68.44 C ANISOU 1466 CB SER A 182 7874 7204 10926 23 678 2028 C ATOM 1467 OG SER A 182 10.150 25.306 -27.411 1.00 56.68 O ANISOU 1467 OG SER A 182 6429 5605 9503 -53 762 1878 O ATOM 1468 N PRO A 183 9.623 23.203 -24.817 1.00 65.05 N ANISOU 1468 N PRO A 183 7738 6844 10133 -29 749 1060 N ATOM 1469 CA PRO A 183 9.813 23.525 -23.388 1.00 73.56 C ANISOU 1469 CA PRO A 183 8846 7751 11354 -41 861 705 C ATOM 1470 C PRO A 183 10.360 24.950 -23.075 1.00 85.18 C ANISOU 1470 C PRO A 183 10232 8905 13229 -69 1002 648 C ATOM 1471 O PRO A 183 10.304 25.363 -21.909 1.00 80.04 O ANISOU 1471 O PRO A 183 9579 8095 12737 -82 1112 349 O ATOM 1472 CB PRO A 183 10.811 22.456 -22.927 1.00 64.62 C ANISOU 1472 CB PRO A 183 7852 6835 9866 -118 798 470 C ATOM 1473 CG PRO A 183 11.610 22.138 -24.148 1.00 54.64 C ANISOU 1473 CG PRO A 183 6603 5729 8427 -163 719 681 C ATOM 1474 CD PRO A 183 10.691 22.309 -25.322 1.00 50.33 C ANISOU 1474 CD PRO A 183 5975 5226 7920 -109 667 1033 C ATOM 1475 N LEU A 184 10.850 25.686 -24.087 1.00 79.61 N ANISOU 1475 N LEU A 184 9449 8112 12687 -87 1007 925 N ATOM 1476 CA LEU A 184 11.492 27.010 -23.897 1.00 71.56 C ANISOU 1476 CA LEU A 184 8341 6781 12069 -126 1142 892 C ATOM 1477 C LEU A 184 10.512 28.187 -24.009 1.00 73.13 C ANISOU 1477 C LEU A 184 8370 6656 12761 -40 1247 1073 C ATOM 1478 O LEU A 184 9.294 28.035 -23.859 1.00 71.71 O ANISOU 1478 O LEU A 184 8144 6463 12641 51 1242 1122 O ATOM 1479 CB LEU A 184 12.631 27.206 -24.911 1.00 61.47 C ANISOU 1479 CB LEU A 184 7057 5566 10732 -200 1107 1107 C ATOM 1480 CG LEU A 184 13.588 26.033 -25.165 1.00 61.06 C ANISOU 1480 CG LEU A 184 7140 5841 10220 -273 999 1024 C ATOM 1481 CD1 LEU A 184 14.710 26.448 -26.106 1.00 61.67 C ANISOU 1481 CD1 LEU A 184 7183 5932 10317 -351 1009 1222 C ATOM 1482 CD2 LEU A 184 14.162 25.476 -23.870 1.00 66.58 C ANISOU 1482 CD2 LEU A 184 7940 6589 10767 -324 1009 598 C ATOM 1483 N VAL A 195 8.387 22.772 -10.211 1.00 67.08 N ANISOU 1483 N VAL A 195 8372 7345 9770 -584 1657 -2492 N ATOM 1484 CA VAL A 195 9.779 22.916 -9.745 1.00 80.57 C ANISOU 1484 CA VAL A 195 10123 9163 11326 -731 1593 -2670 C ATOM 1485 C VAL A 195 10.589 21.587 -9.788 1.00 84.05 C ANISOU 1485 C VAL A 195 10662 9919 11353 -760 1364 -2505 C ATOM 1486 O VAL A 195 11.819 21.622 -9.669 1.00 85.31 O ANISOU 1486 O VAL A 195 10841 10160 11413 -858 1275 -2567 O ATOM 1487 CB VAL A 195 9.831 23.587 -8.337 1.00 77.45 C ANISOU 1487 CB VAL A 195 9711 8814 10901 -888 1756 -3119 C ATOM 1488 CG1 VAL A 195 11.256 23.934 -7.910 1.00 72.29 C ANISOU 1488 CG1 VAL A 195 9072 8244 10149 -1052 1696 -3319 C ATOM 1489 CG2 VAL A 195 8.990 24.860 -8.326 1.00 76.34 C ANISOU 1489 CG2 VAL A 195 9456 8327 11223 -848 2005 -3290 C ATOM 1490 N THR A 196 9.918 20.437 -9.969 1.00 67.73 N ANISOU 1490 N THR A 196 8642 8011 9080 -677 1274 -2295 N ATOM 1491 CA THR A 196 10.590 19.118 -10.148 1.00 69.73 C ANISOU 1491 CA THR A 196 8969 8513 9014 -680 1069 -2103 C ATOM 1492 C THR A 196 11.424 18.975 -11.442 1.00 54.69 C ANISOU 1492 C THR A 196 7061 6525 7192 -625 946 -1861 C ATOM 1493 O THR A 196 10.873 18.982 -12.536 1.00 71.60 O ANISOU 1493 O THR A 196 9179 8532 9493 -512 942 -1641 O ATOM 1494 CB THR A 196 9.580 17.921 -10.061 1.00 65.90 C ANISOU 1494 CB THR A 196 8520 8183 8337 -605 1023 -1942 C ATOM 1495 CG2 THR A 196 8.528 17.913 -11.200 1.00 61.43 C ANISOU 1495 CG2 THR A 196 7913 7438 7988 -454 1045 -1710 C ATOM 1496 OG1 THR A 196 10.290 16.676 -10.093 1.00 44.48 O ANISOU 1496 OG1 THR A 196 5861 5688 5350 -621 843 -1790 O ATOM 1497 N PHE A 197 12.743 18.831 -11.313 1.00 43.22 N ANISOU 1497 N PHE A 197 5625 5174 5622 -712 846 -1900 N ATOM 1498 CA PHE A 197 13.603 18.491 -12.462 1.00 33.25 C ANISOU 1498 CA PHE A 197 4361 3884 4388 -670 730 -1679 C ATOM 1499 C PHE A 197 14.164 17.052 -12.444 1.00 26.05 C ANISOU 1499 C PHE A 197 3494 3209 3196 -669 564 -1542 C ATOM 1500 O PHE A 197 14.962 16.685 -13.305 1.00 24.42 O ANISOU 1500 O PHE A 197 3281 3000 2998 -646 479 -1394 O ATOM 1501 CB PHE A 197 14.749 19.495 -12.585 1.00 36.31 C ANISOU 1501 CB PHE A 197 4704 4152 4941 -756 754 -1791 C ATOM 1502 CG PHE A 197 14.300 20.915 -12.767 1.00 46.79 C ANISOU 1502 CG PHE A 197 5968 5197 6615 -750 921 -1891 C ATOM 1503 CD1 PHE A 197 13.894 21.376 -14.008 1.00 48.24 C ANISOU 1503 CD1 PHE A 197 6109 5169 7050 -646 960 -1663 C ATOM 1504 CD2 PHE A 197 14.304 21.802 -11.700 1.00 61.91 C ANISOU 1504 CD2 PHE A 197 7852 7056 8613 -857 1043 -2212 C ATOM 1505 CE1 PHE A 197 13.488 22.690 -14.183 1.00 55.62 C ANISOU 1505 CE1 PHE A 197 6964 5819 8351 -633 1113 -1718 C ATOM 1506 CE2 PHE A 197 13.902 23.125 -11.868 1.00 69.94 C ANISOU 1506 CE2 PHE A 197 8793 7773 10009 -849 1214 -2314 C ATOM 1507 CZ PHE A 197 13.493 23.570 -13.112 1.00 56.72 C ANISOU 1507 CZ PHE A 197 7068 5863 8620 -729 1248 -2050 C ATOM 1508 N TRP A 198 13.715 16.208 -11.521 1.00 22.21 N ANISOU 1508 N TRP A 198 3042 2916 2481 -688 528 -1576 N ATOM 1509 CA TRP A 198 14.370 14.900 -11.317 1.00 24.03 C ANISOU 1509 CA TRP A 198 3292 3357 2481 -701 374 -1456 C ATOM 1510 C TRP A 198 14.184 13.859 -12.432 1.00 20.99 C ANISOU 1510 C TRP A 198 2917 2954 2102 -591 300 -1205 C ATOM 1511 O TRP A 198 14.933 12.888 -12.489 1.00 25.85 O ANISOU 1511 O TRP A 198 3528 3684 2611 -595 186 -1105 O ATOM 1512 CB TRP A 198 13.917 14.241 -10.012 1.00 25.90 C ANISOU 1512 CB TRP A 198 3553 3816 2473 -757 355 -1521 C ATOM 1513 CG TRP A 198 13.909 15.098 -8.807 1.00 28.34 C ANISOU 1513 CG TRP A 198 3855 4200 2712 -883 440 -1792 C ATOM 1514 CD1 TRP A 198 14.589 16.260 -8.608 1.00 31.69 C ANISOU 1514 CD1 TRP A 198 4248 4542 3249 -975 496 -2004 C ATOM 1515 CD2 TRP A 198 13.182 14.844 -7.608 1.00 32.70 C ANISOU 1515 CD2 TRP A 198 4427 4938 3058 -946 488 -1900 C ATOM 1516 CE2 TRP A 198 13.462 15.901 -6.721 1.00 36.08 C ANISOU 1516 CE2 TRP A 198 4838 5404 3467 -1083 578 -2203 C ATOM 1517 CE3 TRP A 198 12.315 13.823 -7.198 1.00 34.03 C ANISOU 1517 CE3 TRP A 198 4622 5250 3058 -909 472 -1774 C ATOM 1518 NE1 TRP A 198 14.320 16.754 -7.363 1.00 34.94 N ANISOU 1518 NE1 TRP A 198 4660 5079 3536 -1097 580 -2265 N ATOM 1519 CZ2 TRP A 198 12.896 15.980 -5.446 1.00 43.51 C ANISOU 1519 CZ2 TRP A 198 5790 6542 4199 -1189 660 -2398 C ATOM 1520 CZ3 TRP A 198 11.759 13.888 -5.927 1.00 42.48 C ANISOU 1520 CZ3 TRP A 198 5703 6513 3926 -1007 549 -1934 C ATOM 1521 CH2 TRP A 198 12.047 14.968 -5.066 1.00 45.60 C ANISOU 1521 CH2 TRP A 198 6083 6962 4280 -1149 645 -2250 C ATOM 1522 N TYR A 199 13.176 14.035 -13.284 1.00 22.83 N ANISOU 1522 N TYR A 199 3154 3054 2467 -499 365 -1111 N ATOM 1523 CA TYR A 199 12.819 13.034 -14.298 1.00 15.44 C ANISOU 1523 CA TYR A 199 2226 2126 1514 -412 304 -908 C ATOM 1524 C TYR A 199 13.091 13.527 -15.710 1.00 12.40 C ANISOU 1524 C TYR A 199 1818 1609 1283 -371 315 -799 C ATOM 1525 O TYR A 199 12.722 12.860 -16.670 1.00 22.92 O ANISOU 1525 O TYR A 199 3152 2952 2604 -313 279 -653 O ATOM 1526 CB TYR A 199 11.347 12.644 -14.107 1.00 18.46 C ANISOU 1526 CB TYR A 199 2621 2520 1875 -354 348 -866 C ATOM 1527 CG TYR A 199 11.073 12.186 -12.681 1.00 19.56 C ANISOU 1527 CG TYR A 199 2778 2810 1842 -409 351 -963 C ATOM 1528 CD1 TYR A 199 10.740 13.100 -11.681 1.00 22.95 C ANISOU 1528 CD1 TYR A 199 3205 3239 2276 -468 456 -1155 C ATOM 1529 CD2 TYR A 199 11.198 10.843 -12.322 1.00 16.67 C ANISOU 1529 CD2 TYR A 199 2425 2596 1313 -411 257 -863 C ATOM 1530 CE1 TYR A 199 10.514 12.680 -10.363 1.00 27.29 C ANISOU 1530 CE1 TYR A 199 3772 3973 2625 -538 464 -1245 C ATOM 1531 CE2 TYR A 199 10.977 10.412 -11.018 1.00 13.91 C ANISOU 1531 CE2 TYR A 199 2085 2411 787 -471 254 -912 C ATOM 1532 CZ TYR A 199 10.640 11.328 -10.035 1.00 20.29 C ANISOU 1532 CZ TYR A 199 2899 3256 1554 -540 355 -1103 C ATOM 1533 OH TYR A 199 10.425 10.897 -8.737 1.00 18.54 O ANISOU 1533 OH TYR A 199 2687 3240 1118 -617 357 -1151 O ATOM 1534 N ARG A 200 13.768 14.673 -15.822 1.00 13.52 N ANISOU 1534 N ARG A 200 1934 1641 1561 -414 364 -873 N ATOM 1535 CA ARG A 200 14.031 15.329 -17.100 1.00 17.03 C ANISOU 1535 CA ARG A 200 2348 1960 2164 -388 391 -754 C ATOM 1536 C ARG A 200 15.361 14.882 -17.666 1.00 17.10 C ANISOU 1536 C ARG A 200 2348 2031 2120 -423 322 -708 C ATOM 1537 O ARG A 200 16.384 14.954 -16.987 1.00 20.61 O ANISOU 1537 O ARG A 200 2780 2517 2534 -493 293 -821 O ATOM 1538 CB ARG A 200 14.025 16.858 -16.959 1.00 19.68 C ANISOU 1538 CB ARG A 200 2641 2107 2728 -416 500 -841 C ATOM 1539 CG ARG A 200 12.620 17.405 -16.814 1.00 32.11 C ANISOU 1539 CG ARG A 200 4195 3571 4435 -357 591 -837 C ATOM 1540 CD ARG A 200 12.554 18.755 -16.134 1.00 42.72 C ANISOU 1540 CD ARG A 200 5493 4736 6002 -399 720 -1017 C ATOM 1541 NE ARG A 200 12.835 19.869 -17.047 1.00 56.32 N ANISOU 1541 NE ARG A 200 7150 6251 7998 -388 779 -910 N ATOM 1542 CZ ARG A 200 12.182 21.040 -17.084 1.00 63.92 C ANISOU 1542 CZ ARG A 200 8039 6982 9266 -359 905 -921 C ATOM 1543 NH1 ARG A 200 11.140 21.313 -16.280 1.00 42.55 N1+ ANISOU 1543 NH1 ARG A 200 5312 4211 6645 -333 1002 -1058 N1+ ATOM 1544 NH2 ARG A 200 12.567 21.958 -17.968 1.00 77.57 N ANISOU 1544 NH2 ARG A 200 9701 8531 11239 -354 944 -778 N ATOM 1545 N ALA A 201 15.313 14.454 -18.927 1.00 14.85 N ANISOU 1545 N ALA A 201 2057 1759 1825 -380 301 -546 N ATOM 1546 CA ALA A 201 16.454 14.011 -19.695 1.00 11.00 C ANISOU 1546 CA ALA A 201 1552 1325 1302 -406 264 -495 C ATOM 1547 C ALA A 201 17.559 15.063 -19.828 1.00 13.15 C ANISOU 1547 C ALA A 201 1782 1508 1707 -469 306 -533 C ATOM 1548 O ALA A 201 17.266 16.269 -19.913 1.00 15.43 O ANISOU 1548 O ALA A 201 2049 1655 2158 -477 379 -527 O ATOM 1549 CB ALA A 201 15.979 13.612 -21.078 1.00 14.56 C ANISOU 1549 CB ALA A 201 2002 1811 1720 -364 264 -335 C ATOM 1550 N PRO A 202 18.828 14.618 -19.892 1.00 8.31 N ANISOU 1550 N PRO A 202 1140 959 1057 -512 266 -562 N ATOM 1551 CA PRO A 202 19.899 15.608 -20.008 1.00 11.07 C ANISOU 1551 CA PRO A 202 1439 1224 1544 -581 306 -601 C ATOM 1552 C PRO A 202 19.695 16.594 -21.146 1.00 11.26 C ANISOU 1552 C PRO A 202 1441 1130 1708 -576 391 -463 C ATOM 1553 O PRO A 202 20.012 17.769 -20.972 1.00 16.55 O ANISOU 1553 O PRO A 202 2072 1660 2555 -622 452 -502 O ATOM 1554 CB PRO A 202 21.175 14.782 -20.211 1.00 11.04 C ANISOU 1554 CB PRO A 202 1393 1320 1482 -610 254 -607 C ATOM 1555 CG PRO A 202 20.749 13.370 -20.370 1.00 12.71 C ANISOU 1555 CG PRO A 202 1632 1647 1549 -549 199 -559 C ATOM 1556 CD PRO A 202 19.289 13.240 -20.100 1.00 9.68 C ANISOU 1556 CD PRO A 202 1310 1260 1107 -494 199 -537 C ATOM 1557 N GLU A 203 19.148 16.140 -22.275 1.00 9.97 N ANISOU 1557 N GLU A 203 1292 1026 1471 -528 394 -302 N ATOM 1558 CA GLU A 203 18.997 17.013 -23.438 1.00 13.61 C ANISOU 1558 CA GLU A 203 1720 1418 2035 -533 459 -123 C ATOM 1559 C GLU A 203 18.047 18.201 -23.194 1.00 16.26 C ANISOU 1559 C GLU A 203 2037 1578 2562 -506 514 -74 C ATOM 1560 O GLU A 203 18.324 19.294 -23.660 1.00 16.74 O ANISOU 1560 O GLU A 203 2044 1507 2810 -534 581 24 O ATOM 1561 CB GLU A 203 18.631 16.224 -24.707 1.00 18.04 C ANISOU 1561 CB GLU A 203 2293 2128 2432 -510 441 30 C ATOM 1562 CG GLU A 203 17.265 15.528 -24.724 1.00 19.32 C ANISOU 1562 CG GLU A 203 2497 2362 2482 -445 392 68 C ATOM 1563 CD GLU A 203 17.288 14.090 -24.213 1.00 16.52 C ANISOU 1563 CD GLU A 203 2181 2124 1971 -426 330 -61 C ATOM 1564 OE1 GLU A 203 18.226 13.691 -23.471 1.00 12.34 O ANISOU 1564 OE1 GLU A 203 1648 1600 1442 -450 311 -193 O ATOM 1565 OE2 GLU A 203 16.339 13.364 -24.538 1.00 10.60 O1- ANISOU 1565 OE2 GLU A 203 1455 1457 1117 -390 296 -19 O1- ATOM 1566 N LEU A 204 16.974 18.011 -22.427 1.00 12.96 N ANISOU 1566 N LEU A 204 1651 1144 2128 -454 498 -143 N ATOM 1567 CA LEU A 204 16.144 19.144 -21.994 1.00 15.28 C ANISOU 1567 CA LEU A 204 1912 1247 2647 -429 571 -149 C ATOM 1568 C LEU A 204 16.946 20.159 -21.165 1.00 20.46 C ANISOU 1568 C LEU A 204 2532 1745 3498 -501 640 -327 C ATOM 1569 O LEU A 204 16.926 21.383 -21.421 1.00 20.63 O ANISOU 1569 O LEU A 204 2487 1563 3787 -513 728 -268 O ATOM 1570 CB LEU A 204 14.963 18.652 -21.169 1.00 18.58 C ANISOU 1570 CB LEU A 204 2366 1696 2996 -373 554 -237 C ATOM 1571 CG LEU A 204 13.844 17.998 -21.962 1.00 23.07 C ANISOU 1571 CG LEU A 204 2944 2360 3463 -301 507 -55 C ATOM 1572 CD1 LEU A 204 12.887 17.265 -21.034 1.00 21.59 C ANISOU 1572 CD1 LEU A 204 2796 2234 3175 -260 485 -169 C ATOM 1573 CD2 LEU A 204 13.106 19.069 -22.741 1.00 28.01 C ANISOU 1573 CD2 LEU A 204 3493 2841 4309 -260 560 153 C ATOM 1574 N LEU A 205 17.692 19.635 -20.202 1.00 17.65 N ANISOU 1574 N LEU A 205 2207 1484 3016 -557 595 -536 N ATOM 1575 CA LEU A 205 18.559 20.463 -19.377 1.00 21.67 C ANISOU 1575 CA LEU A 205 2679 1893 3663 -649 639 -736 C ATOM 1576 C LEU A 205 19.624 21.160 -20.219 1.00 23.03 C ANISOU 1576 C LEU A 205 2787 1971 3992 -703 677 -638 C ATOM 1577 O LEU A 205 20.080 22.239 -19.847 1.00 21.50 O ANISOU 1577 O LEU A 205 2537 1608 4023 -772 752 -749 O ATOM 1578 CB LEU A 205 19.188 19.632 -18.252 1.00 25.13 C ANISOU 1578 CB LEU A 205 3150 2507 3891 -706 552 -936 C ATOM 1579 CG LEU A 205 18.193 18.985 -17.266 1.00 23.25 C ANISOU 1579 CG LEU A 205 2969 2373 3492 -673 524 -1038 C ATOM 1580 CD1 LEU A 205 18.882 17.953 -16.390 1.00 26.01 C ANISOU 1580 CD1 LEU A 205 3340 2937 3606 -722 412 -1139 C ATOM 1581 CD2 LEU A 205 17.521 20.035 -16.402 1.00 23.75 C ANISOU 1581 CD2 LEU A 205 3015 2294 3715 -703 632 -1222 C ATOM 1582 N LEU A 206 20.001 20.568 -21.360 1.00 20.91 N ANISOU 1582 N LEU A 206 2522 1811 3614 -681 640 -441 N ATOM 1583 CA LEU A 206 20.919 21.244 -22.292 1.00 21.91 C ANISOU 1583 CA LEU A 206 2583 1863 3881 -733 694 -310 C ATOM 1584 C LEU A 206 20.256 22.141 -23.366 1.00 21.91 C ANISOU 1584 C LEU A 206 2538 1726 4062 -696 769 -47 C ATOM 1585 O LEU A 206 20.932 22.626 -24.285 1.00 19.75 O ANISOU 1585 O LEU A 206 2210 1419 3876 -738 815 116 O ATOM 1586 CB LEU A 206 21.922 20.241 -22.875 1.00 20.79 C ANISOU 1586 CB LEU A 206 2445 1913 3543 -756 637 -271 C ATOM 1587 CG LEU A 206 22.875 19.732 -21.774 1.00 21.40 C ANISOU 1587 CG LEU A 206 2515 2066 3549 -813 572 -502 C ATOM 1588 CD1 LEU A 206 23.725 18.592 -22.284 1.00 19.64 C ANISOU 1588 CD1 LEU A 206 2283 2019 3161 -813 519 -466 C ATOM 1589 CD2 LEU A 206 23.779 20.835 -21.238 1.00 21.80 C ANISOU 1589 CD2 LEU A 206 2493 1972 3818 -914 620 -633 C ATOM 1590 N GLY A 207 18.956 22.406 -23.204 1.00 23.42 N ANISOU 1590 N GLY A 207 2736 1834 4327 -623 786 2 N ATOM 1591 CA GLY A 207 18.242 23.379 -24.034 1.00 22.04 C ANISOU 1591 CA GLY A 207 2493 1500 4383 -583 852 261 C ATOM 1592 C GLY A 207 17.636 22.821 -25.306 1.00 19.97 C ANISOU 1592 C GLY A 207 2239 1408 3940 -533 796 554 C ATOM 1593 O GLY A 207 17.419 23.578 -26.250 1.00 20.78 O ANISOU 1593 O GLY A 207 2269 1437 4191 -527 833 832 O ATOM 1594 N ALA A 208 17.332 21.520 -25.323 1.00 17.16 N ANISOU 1594 N ALA A 208 1962 1284 3276 -504 706 500 N ATOM 1595 CA ALA A 208 16.586 20.900 -26.420 1.00 19.46 C ANISOU 1595 CA ALA A 208 2262 1758 3374 -466 646 727 C ATOM 1596 C ALA A 208 15.284 21.651 -26.623 1.00 20.67 C ANISOU 1596 C ALA A 208 2353 1784 3715 -396 659 922 C ATOM 1597 O ALA A 208 14.595 21.992 -25.641 1.00 21.10 O ANISOU 1597 O ALA A 208 2400 1679 3937 -346 690 788 O ATOM 1598 CB ALA A 208 16.278 19.436 -26.118 1.00 19.11 C ANISOU 1598 CB ALA A 208 2302 1919 3040 -441 561 582 C ATOM 1599 N ARG A 209 14.958 21.897 -27.891 1.00 22.17 N ANISOU 1599 N ARG A 209 2489 2059 3877 -398 639 1239 N ATOM 1600 CA ARG A 209 13.871 22.811 -28.272 1.00 30.36 C ANISOU 1600 CA ARG A 209 3425 2959 5151 -337 650 1507 C ATOM 1601 C ARG A 209 12.524 22.126 -28.557 1.00 34.80 C ANISOU 1601 C ARG A 209 3989 3675 5559 -273 556 1610 C ATOM 1602 O ARG A 209 11.555 22.821 -28.871 1.00 43.66 O ANISOU 1602 O ARG A 209 5011 4696 6883 -215 551 1849 O ATOM 1603 CB ARG A 209 14.308 23.650 -29.488 1.00 32.29 C ANISOU 1603 CB ARG A 209 3580 3200 5488 -387 677 1852 C ATOM 1604 CG ARG A 209 15.582 24.413 -29.316 0.00 32.85 C ANISOU 1604 CG ARG A 209 3627 3105 5748 -456 776 1790 C ATOM 1605 CD ARG A 209 15.879 25.265 -30.540 0.00 35.28 C ANISOU 1605 CD ARG A 209 3834 3410 6163 -504 808 2178 C ATOM 1606 NE ARG A 209 17.144 25.984 -30.417 0.00 36.04 N ANISOU 1606 NE ARG A 209 3898 3345 6452 -581 910 2124 N ATOM 1607 CZ ARG A 209 17.267 27.189 -29.868 0.00 37.60 C ANISOU 1607 CZ ARG A 209 4008 3193 7084 -573 1011 2115 C ATOM 1608 NH1 ARG A 209 16.200 27.814 -29.390 0.00 38.55 N1+ ANISOU 1608 NH1 ARG A 209 4063 3083 7503 -485 1034 2154 N1+ ATOM 1609 NH2 ARG A 209 18.456 27.768 -29.798 0.00 38.49 N ANISOU 1609 NH2 ARG A 209 4089 3179 7356 -658 1098 2055 N ATOM 1610 N HIS A 210 12.462 20.789 -28.450 1.00 33.28 N ANISOU 1610 N HIS A 210 3892 3711 5042 -283 482 1441 N ATOM 1611 CA HIS A 210 11.240 20.020 -28.691 1.00 28.39 C ANISOU 1611 CA HIS A 210 3274 3249 4263 -238 391 1503 C ATOM 1612 C HIS A 210 11.177 18.785 -27.798 1.00 26.74 C ANISOU 1612 C HIS A 210 3168 3126 3866 -226 361 1196 C ATOM 1613 O HIS A 210 12.205 18.194 -27.487 1.00 23.36 O ANISOU 1613 O HIS A 210 2813 2755 3309 -274 374 1001 O ATOM 1614 CB HIS A 210 11.150 19.549 -30.157 1.00 36.89 C ANISOU 1614 CB HIS A 210 4331 4615 5070 -297 308 1741 C ATOM 1615 CG HIS A 210 11.165 20.656 -31.168 1.00 49.98 C ANISOU 1615 CG HIS A 210 5880 6250 6860 -321 318 2106 C ATOM 1616 CD2 HIS A 210 12.029 20.931 -32.175 1.00 55.51 C ANISOU 1616 CD2 HIS A 210 6560 7076 7454 -409 336 2280 C ATOM 1617 ND1 HIS A 210 10.194 21.636 -31.219 1.00 62.07 N ANISOU 1617 ND1 HIS A 210 7290 7613 8681 -249 314 2359 N ATOM 1618 CE1 HIS A 210 10.465 22.473 -32.204 1.00 59.02 C ANISOU 1618 CE1 HIS A 210 6812 7243 8369 -290 320 2695 C ATOM 1619 NE2 HIS A 210 11.572 22.067 -32.802 1.00 55.83 N ANISOU 1619 NE2 HIS A 210 6473 7029 7712 -393 335 2654 N ATOM 1620 N TYR A 211 9.965 18.381 -27.408 1.00 27.85 N ANISOU 1620 N TYR A 211 3299 3278 4004 -163 320 1177 N ATOM 1621 CA TYR A 211 9.772 17.093 -26.746 1.00 22.12 C ANISOU 1621 CA TYR A 211 2658 2665 3081 -158 280 947 C ATOM 1622 C TYR A 211 9.829 15.959 -27.761 1.00 21.37 C ANISOU 1622 C TYR A 211 2592 2841 2686 -213 196 989 C ATOM 1623 O TYR A 211 9.468 16.128 -28.929 1.00 21.64 O ANISOU 1623 O TYR A 211 2571 3008 2644 -242 148 1215 O ATOM 1624 CB TYR A 211 8.450 17.044 -25.993 1.00 27.28 C ANISOU 1624 CB TYR A 211 3282 3240 3841 -82 278 912 C ATOM 1625 CG TYR A 211 8.400 17.939 -24.778 1.00 33.73 C ANISOU 1625 CG TYR A 211 4084 3810 4924 -41 383 772 C ATOM 1626 CD1 TYR A 211 8.812 17.474 -23.526 1.00 31.35 C ANISOU 1626 CD1 TYR A 211 3860 3486 4563 -55 420 491 C ATOM 1627 CD2 TYR A 211 7.919 19.253 -24.872 1.00 42.71 C ANISOU 1627 CD2 TYR A 211 5115 4737 6377 6 450 921 C ATOM 1628 CE1 TYR A 211 8.760 18.288 -22.395 1.00 35.84 C ANISOU 1628 CE1 TYR A 211 4414 3862 5341 -40 524 328 C ATOM 1629 CE2 TYR A 211 7.863 20.077 -23.754 1.00 42.14 C ANISOU 1629 CE2 TYR A 211 5020 4429 6564 31 569 747 C ATOM 1630 CZ TYR A 211 8.283 19.593 -22.519 1.00 42.99 C ANISOU 1630 CZ TYR A 211 5217 4549 6568 1 607 435 C ATOM 1631 OH TYR A 211 8.213 20.418 -21.418 1.00 45.87 O ANISOU 1631 OH TYR A 211 5557 4711 7160 5 732 235 O ATOM 1632 N THR A 212 10.273 14.797 -27.295 1.00 20.08 N ANISOU 1632 N THR A 212 2507 2761 2360 -234 183 768 N ATOM 1633 CA THR A 212 10.509 13.636 -28.148 1.00 19.57 C ANISOU 1633 CA THR A 212 2471 2923 2042 -296 133 735 C ATOM 1634 C THR A 212 10.094 12.385 -27.400 1.00 17.95 C ANISOU 1634 C THR A 212 2313 2750 1758 -273 103 546 C ATOM 1635 O THR A 212 9.952 12.385 -26.171 1.00 15.96 O ANISOU 1635 O THR A 212 2087 2367 1611 -224 126 429 O ATOM 1636 CB THR A 212 12.014 13.457 -28.451 1.00 17.83 C ANISOU 1636 CB THR A 212 2283 2745 1747 -361 180 646 C ATOM 1637 CG2 THR A 212 12.598 14.697 -29.113 1.00 19.23 C ANISOU 1637 CG2 THR A 212 2413 2877 2017 -393 226 829 C ATOM 1638 OG1 THR A 212 12.707 13.206 -27.221 1.00 14.73 O ANISOU 1638 OG1 THR A 212 1936 2228 1433 -337 212 442 O ATOM 1639 N LYS A 213 9.990 11.299 -28.141 1.00 16.44 N ANISOU 1639 N LYS A 213 2129 2738 1378 -323 61 506 N ATOM 1640 CA LYS A 213 9.690 10.016 -27.541 1.00 14.48 C ANISOU 1640 CA LYS A 213 1915 2511 1076 -312 39 336 C ATOM 1641 C LYS A 213 10.777 9.628 -26.547 1.00 12.55 C ANISOU 1641 C LYS A 213 1717 2167 883 -299 82 167 C ATOM 1642 O LYS A 213 10.477 9.176 -25.448 1.00 14.34 O ANISOU 1642 O LYS A 213 1966 2321 1162 -257 76 78 O ATOM 1643 CB LYS A 213 9.511 8.965 -28.626 1.00 17.82 C ANISOU 1643 CB LYS A 213 2325 3133 1313 -385 4 299 C ATOM 1644 CG LYS A 213 8.267 9.227 -29.465 1.00 21.75 C ANISOU 1644 CG LYS A 213 2763 3759 1742 -404 -66 466 C ATOM 1645 CD LYS A 213 8.043 8.154 -30.509 1.00 26.49 C ANISOU 1645 CD LYS A 213 3346 4581 2137 -500 -103 391 C ATOM 1646 CE LYS A 213 6.804 8.470 -31.333 1.00 28.85 C ANISOU 1646 CE LYS A 213 3570 5037 2353 -531 -195 577 C ATOM 1647 NZ LYS A 213 6.616 7.496 -32.448 1.00 30.74 N1+ ANISOU 1647 NZ LYS A 213 3788 5534 2360 -654 -233 486 N1+ ATOM 1648 N ALA A 214 12.033 9.859 -26.918 1.00 12.52 N ANISOU 1648 N ALA A 214 1718 2171 866 -340 123 141 N ATOM 1649 CA ALA A 214 13.176 9.534 -26.058 1.00 13.40 C ANISOU 1649 CA ALA A 214 1852 2205 1034 -336 150 2 C ATOM 1650 C ALA A 214 13.154 10.231 -24.675 1.00 15.40 C ANISOU 1650 C ALA A 214 2122 2313 1416 -290 156 -30 C ATOM 1651 O ALA A 214 13.697 9.689 -23.708 1.00 16.17 O ANISOU 1651 O ALA A 214 2235 2379 1529 -283 146 -141 O ATOM 1652 CB ALA A 214 14.474 9.862 -26.788 1.00 13.36 C ANISOU 1652 CB ALA A 214 1829 2233 1013 -391 200 2 C ATOM 1653 N ILE A 215 12.577 11.430 -24.598 1.00 11.62 N ANISOU 1653 N ILE A 215 1629 1752 1034 -268 176 65 N ATOM 1654 CA ILE A 215 12.469 12.165 -23.333 1.00 14.42 C ANISOU 1654 CA ILE A 215 1992 1971 1514 -240 204 -1 C ATOM 1655 C ILE A 215 11.519 11.433 -22.365 1.00 21.17 C ANISOU 1655 C ILE A 215 2869 2838 2336 -201 179 -71 C ATOM 1656 O ILE A 215 11.806 11.309 -21.170 1.00 17.97 O ANISOU 1656 O ILE A 215 2487 2406 1936 -204 185 -186 O ATOM 1657 CB ILE A 215 12.059 13.632 -23.576 1.00 14.00 C ANISOU 1657 CB ILE A 215 1899 1797 1624 -224 253 112 C ATOM 1658 CG1 ILE A 215 13.251 14.394 -24.171 1.00 16.73 C ANISOU 1658 CG1 ILE A 215 2223 2106 2029 -275 290 156 C ATOM 1659 CG2 ILE A 215 11.639 14.324 -22.298 1.00 15.94 C ANISOU 1659 CG2 ILE A 215 2144 1905 2008 -197 302 9 C ATOM 1660 CD1 ILE A 215 12.894 15.701 -24.843 1.00 14.97 C ANISOU 1660 CD1 ILE A 215 1940 1779 1968 -266 333 339 C ATOM 1661 N ASP A 216 10.402 10.943 -22.886 1.00 15.48 N ANISOU 1661 N ASP A 216 2134 2177 1570 -176 150 7 N ATOM 1662 CA ASP A 216 9.513 10.116 -22.101 1.00 10.95 C ANISOU 1662 CA ASP A 216 1572 1625 963 -147 131 -45 C ATOM 1663 C ASP A 216 10.232 8.875 -21.606 1.00 10.20 C ANISOU 1663 C ASP A 216 1506 1586 783 -168 101 -143 C ATOM 1664 O ASP A 216 10.112 8.500 -20.433 1.00 13.82 O ANISOU 1664 O ASP A 216 1982 2036 1235 -158 100 -207 O ATOM 1665 CB ASP A 216 8.270 9.712 -22.919 1.00 13.91 C ANISOU 1665 CB ASP A 216 1911 2068 1306 -131 94 57 C ATOM 1666 CG ASP A 216 7.264 10.840 -23.058 1.00 14.71 C ANISOU 1666 CG ASP A 216 1960 2097 1533 -89 118 173 C ATOM 1667 OD1 ASP A 216 7.395 11.896 -22.400 1.00 19.22 O ANISOU 1667 OD1 ASP A 216 2524 2540 2239 -66 181 151 O ATOM 1668 OD2 ASP A 216 6.316 10.672 -23.840 1.00 21.55 O1- ANISOU 1668 OD2 ASP A 216 2776 3031 2380 -82 74 287 O1- ATOM 1669 N ILE A 217 11.001 8.252 -22.491 1.00 11.19 N ANISOU 1669 N ILE A 217 1625 1773 853 -201 82 -149 N ATOM 1670 CA ILE A 217 11.713 7.015 -22.148 1.00 9.24 C ANISOU 1670 CA ILE A 217 1380 1555 578 -213 61 -227 C ATOM 1671 C ILE A 217 12.703 7.247 -21.013 1.00 10.46 C ANISOU 1671 C ILE A 217 1542 1667 764 -218 58 -283 C ATOM 1672 O ILE A 217 12.812 6.400 -20.129 1.00 14.68 O ANISOU 1672 O ILE A 217 2073 2214 1290 -212 28 -309 O ATOM 1673 CB ILE A 217 12.440 6.403 -23.367 1.00 10.04 C ANISOU 1673 CB ILE A 217 1458 1716 641 -253 69 -252 C ATOM 1674 CG1 ILE A 217 11.449 6.057 -24.495 1.00 11.10 C ANISOU 1674 CG1 ILE A 217 1577 1936 703 -273 60 -216 C ATOM 1675 CG2 ILE A 217 13.253 5.180 -22.961 1.00 8.39 C ANISOU 1675 CG2 ILE A 217 1226 1494 467 -255 61 -331 C ATOM 1676 CD1 ILE A 217 10.253 5.217 -24.079 1.00 13.00 C ANISOU 1676 CD1 ILE A 217 1812 2180 948 -251 28 -221 C ATOM 1677 N TRP A 218 13.392 8.387 -21.019 1.00 8.87 N ANISOU 1677 N TRP A 218 1343 1425 603 -238 85 -292 N ATOM 1678 CA TRP A 218 14.259 8.766 -19.886 1.00 9.24 C ANISOU 1678 CA TRP A 218 1389 1449 671 -261 76 -361 C ATOM 1679 C TRP A 218 13.510 8.804 -18.562 1.00 9.85 C ANISOU 1679 C TRP A 218 1489 1535 718 -252 70 -398 C ATOM 1680 O TRP A 218 13.968 8.269 -17.552 1.00 15.13 O ANISOU 1680 O TRP A 218 2153 2257 1339 -272 29 -432 O ATOM 1681 CB TRP A 218 14.944 10.120 -20.125 1.00 8.41 C ANISOU 1681 CB TRP A 218 1276 1278 641 -293 118 -377 C ATOM 1682 CG TRP A 218 15.823 10.503 -18.993 1.00 10.88 C ANISOU 1682 CG TRP A 218 1580 1586 968 -335 103 -472 C ATOM 1683 CD1 TRP A 218 15.450 11.178 -17.870 1.00 11.63 C ANISOU 1683 CD1 TRP A 218 1691 1661 1066 -355 120 -554 C ATOM 1684 CD2 TRP A 218 17.228 10.249 -18.855 1.00 12.43 C ANISOU 1684 CD2 TRP A 218 1736 1812 1174 -376 67 -507 C ATOM 1685 CE2 TRP A 218 17.632 10.804 -17.623 1.00 12.19 C ANISOU 1685 CE2 TRP A 218 1699 1795 1136 -425 46 -602 C ATOM 1686 CE3 TRP A 218 18.183 9.608 -19.649 1.00 13.53 C ANISOU 1686 CE3 TRP A 218 1833 1974 1334 -380 57 -479 C ATOM 1687 NE1 TRP A 218 16.526 11.360 -17.045 1.00 13.92 N ANISOU 1687 NE1 TRP A 218 1959 1987 1342 -417 87 -642 N ATOM 1688 CZ2 TRP A 218 18.941 10.731 -17.164 1.00 12.56 C ANISOU 1688 CZ2 TRP A 218 1695 1886 1192 -479 -6 -647 C ATOM 1689 CZ3 TRP A 218 19.489 9.541 -19.196 1.00 12.14 C ANISOU 1689 CZ3 TRP A 218 1601 1818 1195 -420 20 -522 C ATOM 1690 CH2 TRP A 218 19.856 10.106 -17.962 1.00 14.81 C ANISOU 1690 CH2 TRP A 218 1930 2177 1522 -469 -22 -594 C ATOM 1691 N ALA A 219 12.352 9.439 -18.558 1.00 14.57 N ANISOU 1691 N ALA A 219 2100 2090 1343 -226 114 -382 N ATOM 1692 CA ALA A 219 11.559 9.504 -17.345 1.00 11.60 C ANISOU 1692 CA ALA A 219 1740 1730 937 -223 135 -432 C ATOM 1693 C ALA A 219 11.220 8.112 -16.874 1.00 13.90 C ANISOU 1693 C ALA A 219 2033 2105 1143 -212 86 -396 C ATOM 1694 O ALA A 219 11.203 7.875 -15.669 1.00 20.78 O ANISOU 1694 O ALA A 219 2913 3040 1942 -238 77 -432 O ATOM 1695 CB ALA A 219 10.294 10.294 -17.578 1.00 15.85 C ANISOU 1695 CB ALA A 219 2271 2196 1557 -185 200 -408 C ATOM 1696 N ILE A 220 10.949 7.190 -17.806 1.00 13.72 N ANISOU 1696 N ILE A 220 1996 2089 1127 -186 58 -325 N ATOM 1697 CA ILE A 220 10.572 5.815 -17.413 1.00 14.61 C ANISOU 1697 CA ILE A 220 2096 2249 1207 -177 22 -285 C ATOM 1698 C ILE A 220 11.731 5.089 -16.732 1.00 11.67 C ANISOU 1698 C ILE A 220 1703 1915 815 -201 -32 -280 C ATOM 1699 O ILE A 220 11.521 4.387 -15.743 1.00 11.66 O ANISOU 1699 O ILE A 220 1692 1966 772 -207 -58 -238 O ATOM 1700 CB ILE A 220 10.023 4.982 -18.587 1.00 8.60 C ANISOU 1700 CB ILE A 220 1313 1477 478 -159 12 -244 C ATOM 1701 CG1 ILE A 220 8.652 5.517 -18.990 1.00 10.16 C ANISOU 1701 CG1 ILE A 220 1509 1664 686 -136 42 -213 C ATOM 1702 CG2 ILE A 220 9.875 3.519 -18.183 1.00 10.22 C ANISOU 1702 CG2 ILE A 220 1489 1694 698 -156 -17 -213 C ATOM 1703 CD1 ILE A 220 8.189 5.029 -20.350 1.00 13.00 C ANISOU 1703 CD1 ILE A 220 1842 2046 1051 -142 23 -184 C ATOM 1704 N GLY A 221 12.938 5.253 -17.258 1.00 9.35 N ANISOU 1704 N GLY A 221 1391 1605 558 -216 -48 -305 N ATOM 1705 CA GLY A 221 14.130 4.750 -16.578 1.00 12.08 C ANISOU 1705 CA GLY A 221 1695 1986 908 -238 -105 -290 C ATOM 1706 C GLY A 221 14.278 5.292 -15.163 1.00 14.35 C ANISOU 1706 C GLY A 221 1995 2357 1101 -281 -133 -311 C ATOM 1707 O GLY A 221 14.576 4.533 -14.242 1.00 23.34 O ANISOU 1707 O GLY A 221 3098 3572 2197 -297 -194 -243 O ATOM 1708 N CYS A 222 14.050 6.597 -14.991 1.00 13.32 N ANISOU 1708 N CYS A 222 1904 2215 941 -307 -83 -402 N ATOM 1709 CA CYS A 222 14.097 7.238 -13.672 1.00 14.33 C ANISOU 1709 CA CYS A 222 2046 2432 966 -368 -84 -475 C ATOM 1710 C CYS A 222 13.122 6.545 -12.723 1.00 16.98 C ANISOU 1710 C CYS A 222 2393 2860 1198 -369 -86 -423 C ATOM 1711 O CYS A 222 13.487 6.149 -11.619 1.00 15.74 O ANISOU 1711 O CYS A 222 2217 2839 926 -421 -143 -392 O ATOM 1712 CB CYS A 222 13.755 8.727 -13.771 1.00 15.45 C ANISOU 1712 CB CYS A 222 2220 2501 1149 -386 4 -602 C ATOM 1713 SG CYS A 222 14.950 9.729 -14.694 1.00 17.40 S ANISOU 1713 SG CYS A 222 2445 2646 1521 -407 16 -654 S ATOM 1714 N ILE A 223 11.896 6.353 -13.196 1.00 15.04 N ANISOU 1714 N ILE A 223 2168 2553 993 -316 -28 -394 N ATOM 1715 CA ILE A 223 10.855 5.711 -12.406 1.00 13.49 C ANISOU 1715 CA ILE A 223 1976 2428 720 -315 -10 -339 C ATOM 1716 C ILE A 223 11.264 4.289 -12.010 1.00 11.44 C ANISOU 1716 C ILE A 223 1673 2236 439 -317 -96 -192 C ATOM 1717 O ILE A 223 11.133 3.894 -10.855 1.00 16.01 O ANISOU 1717 O ILE A 223 2241 2945 896 -360 -119 -134 O ATOM 1718 CB ILE A 223 9.510 5.710 -13.156 1.00 12.21 C ANISOU 1718 CB ILE A 223 1822 2175 640 -256 57 -323 C ATOM 1719 CG1 ILE A 223 8.992 7.141 -13.284 1.00 14.24 C ANISOU 1719 CG1 ILE A 223 2100 2367 943 -252 147 -438 C ATOM 1720 CG2 ILE A 223 8.486 4.873 -12.412 1.00 14.74 C ANISOU 1720 CG2 ILE A 223 2133 2563 904 -256 75 -249 C ATOM 1721 CD1 ILE A 223 7.898 7.304 -14.320 1.00 19.90 C ANISOU 1721 CD1 ILE A 223 2802 2983 1774 -189 189 -396 C ATOM 1722 N PHE A 224 11.766 3.545 -12.980 1.00 9.79 N ANISOU 1722 N PHE A 224 1429 1936 354 -274 -135 -132 N ATOM 1723 CA PHE A 224 12.218 2.174 -12.783 1.00 12.59 C ANISOU 1723 CA PHE A 224 1719 2298 767 -263 -203 7 C ATOM 1724 C PHE A 224 13.306 2.119 -11.735 1.00 15.42 C ANISOU 1724 C PHE A 224 2035 2779 1044 -314 -288 67 C ATOM 1725 O PHE A 224 13.252 1.278 -10.850 1.00 23.90 O ANISOU 1725 O PHE A 224 3065 3938 2077 -331 -339 213 O ATOM 1726 CB PHE A 224 12.683 1.599 -14.135 1.00 13.81 C ANISOU 1726 CB PHE A 224 1837 2319 1090 -217 -201 -2 C ATOM 1727 CG PHE A 224 13.156 0.165 -14.105 1.00 12.88 C ANISOU 1727 CG PHE A 224 1632 2153 1107 -195 -247 118 C ATOM 1728 CD1 PHE A 224 12.514 -0.809 -13.352 1.00 17.32 C ANISOU 1728 CD1 PHE A 224 2160 2734 1686 -193 -263 255 C ATOM 1729 CD2 PHE A 224 14.221 -0.227 -14.916 1.00 17.23 C ANISOU 1729 CD2 PHE A 224 2124 2619 1803 -176 -257 94 C ATOM 1730 CE1 PHE A 224 12.949 -2.127 -13.376 1.00 16.03 C ANISOU 1730 CE1 PHE A 224 1899 2487 1705 -168 -295 378 C ATOM 1731 CE2 PHE A 224 14.649 -1.541 -14.946 1.00 16.60 C ANISOU 1731 CE2 PHE A 224 1945 2458 1905 -148 -279 191 C ATOM 1732 CZ PHE A 224 14.018 -2.488 -14.168 1.00 15.28 C ANISOU 1732 CZ PHE A 224 1739 2290 1778 -142 -301 340 C ATOM 1733 N ALA A 225 14.258 3.044 -11.792 1.00 14.24 N ANISOU 1733 N ALA A 225 1892 2652 867 -347 -307 -31 N ATOM 1734 CA ALA A 225 15.287 3.112 -10.752 1.00 14.81 C ANISOU 1734 CA ALA A 225 1916 2871 842 -415 -401 13 C ATOM 1735 C ALA A 225 14.691 3.431 -9.367 1.00 15.04 C ANISOU 1735 C ALA A 225 1976 3093 646 -493 -402 8 C ATOM 1736 O ALA A 225 15.120 2.879 -8.334 1.00 23.99 O ANISOU 1736 O ALA A 225 3054 4393 1668 -547 -495 141 O ATOM 1737 CB ALA A 225 16.365 4.124 -11.137 1.00 14.03 C ANISOU 1737 CB ALA A 225 1812 2750 770 -446 -411 -116 C ATOM 1738 N GLU A 226 13.716 4.330 -9.347 1.00 15.19 N ANISOU 1738 N GLU A 226 2072 3097 601 -504 -295 -140 N ATOM 1739 CA GLU A 226 13.027 4.712 -8.114 1.00 15.21 C ANISOU 1739 CA GLU A 226 2108 3275 397 -582 -254 -193 C ATOM 1740 C GLU A 226 12.239 3.539 -7.538 1.00 18.38 C ANISOU 1740 C GLU A 226 2487 3755 741 -571 -266 -4 C ATOM 1741 O GLU A 226 12.255 3.343 -6.331 1.00 21.51 O ANISOU 1741 O GLU A 226 2866 4368 938 -656 -302 60 O ATOM 1742 CB GLU A 226 12.153 5.953 -8.346 1.00 16.92 C ANISOU 1742 CB GLU A 226 2391 3410 628 -581 -114 -404 C ATOM 1743 CG GLU A 226 11.746 6.678 -7.064 1.00 20.62 C ANISOU 1743 CG GLU A 226 2886 4060 891 -687 -48 -549 C ATOM 1744 CD GLU A 226 11.102 8.051 -7.281 1.00 25.30 C ANISOU 1744 CD GLU A 226 3519 4536 1558 -688 101 -785 C ATOM 1745 OE1 GLU A 226 11.236 8.640 -8.372 1.00 21.03 O ANISOU 1745 OE1 GLU A 226 2984 3792 1214 -622 129 -831 O ATOM 1746 OE2 GLU A 226 10.464 8.562 -6.337 1.00 32.89 O1- ANISOU 1746 OE2 GLU A 226 4498 5611 2389 -759 198 -924 O1- ATOM 1747 N LEU A 227 11.629 2.706 -8.388 1.00 18.68 N ANISOU 1747 N LEU A 227 2513 3633 950 -481 -242 95 N ATOM 1748 CA LEU A 227 10.963 1.460 -7.909 1.00 21.00 C ANISOU 1748 CA LEU A 227 2768 3969 1243 -470 -256 298 C ATOM 1749 C LEU A 227 11.913 0.418 -7.297 1.00 20.59 C ANISOU 1749 C LEU A 227 2625 4009 1189 -492 -386 528 C ATOM 1750 O LEU A 227 11.571 -0.259 -6.335 1.00 29.80 O ANISOU 1750 O LEU A 227 3756 5317 2250 -534 -412 703 O ATOM 1751 CB LEU A 227 10.152 0.810 -9.036 1.00 17.80 C ANISOU 1751 CB LEU A 227 2359 3358 1048 -380 -203 325 C ATOM 1752 CG LEU A 227 8.965 1.622 -9.571 1.00 19.22 C ANISOU 1752 CG LEU A 227 2600 3461 1242 -353 -87 170 C ATOM 1753 CD1 LEU A 227 8.403 0.958 -10.805 1.00 19.43 C ANISOU 1753 CD1 LEU A 227 2606 3310 1465 -281 -69 196 C ATOM 1754 CD2 LEU A 227 7.859 1.800 -8.541 1.00 22.72 C ANISOU 1754 CD2 LEU A 227 3062 4032 1539 -398 -6 168 C ATOM 1755 N LEU A 228 13.101 0.285 -7.862 1.00 26.20 N ANISOU 1755 N LEU A 228 3283 4639 2031 -463 -465 544 N ATOM 1756 CA LEU A 228 14.061 -0.711 -7.394 1.00 26.92 C ANISOU 1756 CA LEU A 228 3260 4783 2185 -468 -591 777 C ATOM 1757 C LEU A 228 14.754 -0.337 -6.072 1.00 25.34 C ANISOU 1757 C LEU A 228 3028 4866 1732 -579 -695 844 C ATOM 1758 O LEU A 228 15.130 -1.213 -5.317 1.00 34.34 O ANISOU 1758 O LEU A 228 4072 6123 2853 -604 -799 1101 O ATOM 1759 CB LEU A 228 15.115 -0.939 -8.472 1.00 27.79 C ANISOU 1759 CB LEU A 228 3310 4709 2540 -401 -624 752 C ATOM 1760 CG LEU A 228 14.618 -1.497 -9.805 1.00 32.28 C ANISOU 1760 CG LEU A 228 3885 5026 3352 -309 -537 695 C ATOM 1761 CD1 LEU A 228 15.726 -1.363 -10.836 1.00 37.02 C ANISOU 1761 CD1 LEU A 228 4445 5497 4126 -270 -545 602 C ATOM 1762 CD2 LEU A 228 14.183 -2.951 -9.694 1.00 37.72 C ANISOU 1762 CD2 LEU A 228 4492 5626 4216 -269 -543 903 C ATOM 1763 N THR A 229 14.929 0.957 -5.823 1.00 23.95 N ANISOU 1763 N THR A 229 2922 4800 1377 -652 -669 617 N ATOM 1764 CA THR A 229 15.692 1.491 -4.683 1.00 25.66 C ANISOU 1764 CA THR A 229 3110 5297 1341 -781 -766 608 C ATOM 1765 C THR A 229 14.842 2.207 -3.625 1.00 29.48 C ANISOU 1765 C THR A 229 3671 6014 1516 -895 -691 477 C ATOM 1766 O THR A 229 15.254 2.303 -2.455 1.00 35.05 O ANISOU 1766 O THR A 229 4340 7019 1958 -1024 -777 529 O ATOM 1767 CB THR A 229 16.733 2.531 -5.178 1.00 28.82 C ANISOU 1767 CB THR A 229 3515 5647 1789 -803 -788 399 C ATOM 1768 CG2 THR A 229 17.628 1.940 -6.265 1.00 27.59 C ANISOU 1768 CG2 THR A 229 3280 5271 1932 -699 -838 490 C ATOM 1769 OG1 THR A 229 16.067 3.698 -5.700 1.00 32.25 O ANISOU 1769 OG1 THR A 229 4061 5969 2225 -798 -641 116 O ATOM 1770 N SER A 230 13.689 2.735 -4.063 1.00 26.29 N ANISOU 1770 N SER A 230 3361 5480 1146 -855 -528 298 N ATOM 1771 CA SER A 230 12.779 3.600 -3.281 1.00 29.03 C ANISOU 1771 CA SER A 230 3784 5980 1268 -946 -403 99 C ATOM 1772 C SER A 230 13.286 5.040 -3.163 1.00 32.09 C ANISOU 1772 C SER A 230 4210 6405 1577 -1028 -363 -211 C ATOM 1773 O SER A 230 12.669 5.852 -2.476 1.00 32.20 O ANISOU 1773 O SER A 230 4272 6541 1420 -1117 -248 -420 O ATOM 1774 CB SER A 230 12.423 3.000 -1.910 1.00 33.94 C ANISOU 1774 CB SER A 230 4376 6916 1604 -1054 -435 265 C ATOM 1775 OG SER A 230 12.031 1.635 -2.037 1.00 35.20 O ANISOU 1775 OG SER A 230 4482 7011 1882 -977 -475 576 O ATOM 1776 N GLU A 231 14.366 5.359 -3.885 1.00 34.14 N ANISOU 1776 N GLU A 231 4442 6537 1991 -998 -436 -253 N ATOM 1777 CA GLU A 231 14.997 6.673 -3.877 1.00 35.57 C ANISOU 1777 CA GLU A 231 4643 6719 2154 -1075 -409 -526 C ATOM 1778 C GLU A 231 14.893 7.222 -5.294 1.00 30.06 C ANISOU 1778 C GLU A 231 3981 5692 1751 -955 -323 -626 C ATOM 1779 O GLU A 231 15.101 6.456 -6.241 1.00 26.98 O ANISOU 1779 O GLU A 231 3564 5139 1548 -844 -370 -458 O ATOM 1780 CB GLU A 231 16.489 6.545 -3.546 1.00 43.92 C ANISOU 1780 CB GLU A 231 5614 7919 3154 -1149 -585 -453 C ATOM 1781 CG GLU A 231 16.848 5.712 -2.317 1.00 60.54 C ANISOU 1781 CG GLU A 231 7646 10358 5000 -1251 -732 -237 C ATOM 1782 CD GLU A 231 16.747 6.463 -1.007 1.00 64.41 C ANISOU 1782 CD GLU A 231 8155 11175 5142 -1442 -714 -429 C ATOM 1783 OE1 GLU A 231 16.022 7.482 -0.949 1.00 62.54 O ANISOU 1783 OE1 GLU A 231 8000 10888 4875 -1481 -543 -729 O ATOM 1784 OE2 GLU A 231 17.399 6.016 -0.031 1.00 70.72 O1- ANISOU 1784 OE2 GLU A 231 8876 12290 5705 -1560 -870 -276 O1- ATOM 1785 N PRO A 232 14.617 8.536 -5.463 1.00 24.78 N ANISOU 1785 N PRO A 232 3358 4923 1133 -984 -196 -893 N ATOM 1786 CA PRO A 232 14.704 9.085 -6.809 1.00 22.69 C ANISOU 1786 CA PRO A 232 3109 4373 1139 -884 -139 -944 C ATOM 1787 C PRO A 232 16.176 9.175 -7.248 1.00 28.06 C ANISOU 1787 C PRO A 232 3733 5024 1903 -902 -251 -920 C ATOM 1788 O PRO A 232 16.995 9.809 -6.574 1.00 22.25 O ANISOU 1788 O PRO A 232 2969 4415 1072 -1020 -294 -1053 O ATOM 1789 CB PRO A 232 14.060 10.476 -6.688 1.00 22.19 C ANISOU 1789 CB PRO A 232 3088 4221 1124 -922 25 -1213 C ATOM 1790 CG PRO A 232 13.566 10.579 -5.284 1.00 25.94 C ANISOU 1790 CG PRO A 232 3575 4938 1345 -1041 70 -1332 C ATOM 1791 CD PRO A 232 14.383 9.609 -4.488 1.00 26.41 C ANISOU 1791 CD PRO A 232 3590 5266 1178 -1117 -102 -1163 C ATOM 1792 N ILE A 233 16.493 8.512 -8.356 1.00 28.68 N ANISOU 1792 N ILE A 233 3789 4950 2158 -794 -292 -762 N ATOM 1793 CA ILE A 233 17.881 8.366 -8.808 1.00 25.85 C ANISOU 1793 CA ILE A 233 3361 4568 1895 -798 -393 -707 C ATOM 1794 C ILE A 233 18.587 9.714 -9.027 1.00 23.98 C ANISOU 1794 C ILE A 233 3119 4259 1733 -864 -351 -909 C ATOM 1795 O ILE A 233 19.778 9.842 -8.752 1.00 24.49 O ANISOU 1795 O ILE A 233 3115 4405 1787 -935 -445 -925 O ATOM 1796 CB ILE A 233 17.976 7.464 -10.071 1.00 20.86 C ANISOU 1796 CB ILE A 233 2706 3767 1452 -672 -402 -544 C ATOM 1797 CG1 ILE A 233 19.428 7.198 -10.453 1.00 21.14 C ANISOU 1797 CG1 ILE A 233 2650 3789 1592 -676 -494 -484 C ATOM 1798 CG2 ILE A 233 17.229 8.074 -11.246 1.00 25.80 C ANISOU 1798 CG2 ILE A 233 3395 4191 2218 -599 -276 -616 C ATOM 1799 CD1 ILE A 233 19.603 5.991 -11.345 1.00 20.37 C ANISOU 1799 CD1 ILE A 233 2504 3585 1651 -574 -514 -321 C ATOM 1800 N PHE A 234 17.851 10.712 -9.502 1.00 22.72 N ANISOU 1800 N PHE A 234 3019 3942 1673 -843 -212 -1050 N ATOM 1801 CA PHE A 234 18.413 12.032 -9.747 1.00 20.75 C ANISOU 1801 CA PHE A 234 2758 3583 1542 -902 -151 -1232 C ATOM 1802 C PHE A 234 17.845 13.099 -8.818 1.00 22.14 C ANISOU 1802 C PHE A 234 2964 3796 1652 -999 -49 -1476 C ATOM 1803 O PHE A 234 17.686 14.255 -9.212 1.00 23.28 O ANISOU 1803 O PHE A 234 3116 3761 1969 -1007 68 -1623 O ATOM 1804 CB PHE A 234 18.229 12.381 -11.223 1.00 20.34 C ANISOU 1804 CB PHE A 234 2721 3287 1718 -800 -71 -1173 C ATOM 1805 CG PHE A 234 18.869 11.387 -12.149 1.00 17.39 C ANISOU 1805 CG PHE A 234 2312 2889 1405 -725 -147 -985 C ATOM 1806 CD1 PHE A 234 20.221 11.072 -12.030 1.00 20.03 C ANISOU 1806 CD1 PHE A 234 2570 3298 1744 -771 -250 -953 C ATOM 1807 CD2 PHE A 234 18.136 10.773 -13.119 1.00 13.27 C ANISOU 1807 CD2 PHE A 234 1821 2277 945 -619 -112 -858 C ATOM 1808 CE1 PHE A 234 20.804 10.150 -12.871 1.00 20.84 C ANISOU 1808 CE1 PHE A 234 2626 3364 1930 -702 -296 -804 C ATOM 1809 CE2 PHE A 234 18.714 9.850 -13.959 1.00 17.57 C ANISOU 1809 CE2 PHE A 234 2327 2800 1549 -564 -161 -728 C ATOM 1810 CZ PHE A 234 20.047 9.536 -13.838 1.00 17.43 C ANISOU 1810 CZ PHE A 234 2232 2837 1555 -601 -243 -705 C ATOM 1811 N HIS A 235 17.602 12.716 -7.564 1.00 25.54 N ANISOU 1811 N HIS A 235 3400 4466 1839 -1084 -89 -1519 N ATOM 1812 CA HIS A 235 17.166 13.647 -6.526 1.00 26.75 C ANISOU 1812 CA HIS A 235 3571 4708 1885 -1207 11 -1789 C ATOM 1813 C HIS A 235 18.109 14.827 -6.457 1.00 26.69 C ANISOU 1813 C HIS A 235 3521 4640 1979 -1318 32 -2015 C ATOM 1814 O HIS A 235 19.322 14.652 -6.518 1.00 35.70 O ANISOU 1814 O HIS A 235 4604 5851 3111 -1366 -98 -1962 O ATOM 1815 CB HIS A 235 17.135 12.965 -5.159 1.00 31.73 C ANISOU 1815 CB HIS A 235 4195 5679 2182 -1317 -74 -1778 C ATOM 1816 CG HIS A 235 16.878 13.915 -4.034 1.00 51.94 C ANISOU 1816 CG HIS A 235 6764 8381 4591 -1479 27 -2095 C ATOM 1817 CD2 HIS A 235 15.746 14.547 -3.642 1.00 58.08 C ANISOU 1817 CD2 HIS A 235 7583 9114 5371 -1496 213 -2298 C ATOM 1818 ND1 HIS A 235 17.881 14.382 -3.211 1.00 64.84 N ANISOU 1818 ND1 HIS A 235 8347 10218 6072 -1656 -50 -2269 N ATOM 1819 CE1 HIS A 235 17.370 15.228 -2.335 1.00 75.02 C ANISOU 1819 CE1 HIS A 235 9655 11597 7253 -1786 87 -2583 C ATOM 1820 NE2 HIS A 235 16.077 15.346 -2.575 1.00 74.16 N ANISOU 1820 NE2 HIS A 235 9600 11332 7247 -1688 256 -2607 N ATOM 1821 N CYS A 236 17.550 16.019 -6.305 1.00 28.48 N ANISOU 1821 N CYS A 236 3764 4729 2328 -1360 201 -2270 N ATOM 1822 CA CYS A 236 18.329 17.252 -6.250 1.00 31.55 C ANISOU 1822 CA CYS A 236 4106 5015 2868 -1472 253 -2515 C ATOM 1823 C CYS A 236 17.527 18.362 -5.556 1.00 37.09 C ANISOU 1823 C CYS A 236 4818 5652 3624 -1556 450 -2847 C ATOM 1824 O CYS A 236 16.313 18.253 -5.442 1.00 43.73 O ANISOU 1824 O CYS A 236 5699 6455 4459 -1487 563 -2847 O ATOM 1825 CB CYS A 236 18.688 17.664 -7.676 1.00 30.11 C ANISOU 1825 CB CYS A 236 3904 4527 3010 -1360 281 -2387 C ATOM 1826 SG CYS A 236 19.821 19.043 -7.759 1.00 37.48 S ANISOU 1826 SG CYS A 236 4762 5311 4168 -1490 327 -2623 S ATOM 1827 N ARG A 237 18.200 19.430 -5.121 1.00 43.38 N ANISOU 1827 N ARG A 237 5565 6418 4499 -1706 503 -3140 N ATOM 1828 CA ARG A 237 17.563 20.557 -4.392 1.00 55.15 C ANISOU 1828 CA ARG A 237 7047 7837 6071 -1812 710 -3518 C ATOM 1829 C ARG A 237 16.608 21.396 -5.265 1.00 67.00 C ANISOU 1829 C ARG A 237 8543 8934 7978 -1674 914 -3528 C ATOM 1830 O ARG A 237 16.454 21.127 -6.455 1.00 75.99 O ANISOU 1830 O ARG A 237 9690 9876 9305 -1507 883 -3234 O ATOM 1831 CB ARG A 237 18.645 21.480 -3.795 1.00 63.30 C ANISOU 1831 CB ARG A 237 8012 8918 7120 -2020 706 -3838 C ATOM 1832 CG ARG A 237 19.202 22.423 -5.023 0.00 63.55 C ANISOU 1832 CG ARG A 237 7989 8541 7616 -1950 769 -3799 C ATOM 1833 CD ARG A 237 20.405 23.211 -4.566 0.00 66.17 C ANISOU 1833 CD ARG A 237 8242 8910 7988 -2148 739 -4069 C ATOM 1834 NE ARG A 237 20.648 24.377 -5.412 0.00 66.33 N ANISOU 1834 NE ARG A 237 8203 8528 8469 -2122 874 -4136 N ATOM 1835 CZ ARG A 237 20.034 25.547 -5.262 0.00 68.15 C ANISOU 1835 CZ ARG A 237 8401 8493 8999 -2158 1104 -4420 C ATOM 1836 NH1 ARG A 237 19.138 25.709 -4.298 0.00 69.70 N1+ ANISOU 1836 NH1 ARG A 237 8622 8792 9069 -2225 1235 -4692 N1+ ATOM 1837 NH2 ARG A 237 20.315 26.555 -6.077 0.00 68.63 N ANISOU 1837 NH2 ARG A 237 8393 8178 9504 -2130 1213 -4427 N ATOM 1838 N GLN A 238 15.977 22.413 -4.670 1.00 78.65 N ANISOU 1838 N GLN A 238 9993 10296 9595 -1750 1125 -3866 N ATOM 1839 CA GLN A 238 15.080 23.334 -5.403 1.00 85.67 C ANISOU 1839 CA GLN A 238 10846 10782 10923 -1627 1331 -3886 C ATOM 1840 C GLN A 238 15.792 24.138 -6.506 0.00 83.57 C ANISOU 1840 C GLN A 238 10520 10187 11046 -1579 1338 -3789 C ATOM 1841 O GLN A 238 16.488 25.123 -6.245 0.00 72.07 O ANISOU 1841 O GLN A 238 9001 8614 9768 -1711 1408 -4052 O ATOM 1842 CB GLN A 238 14.382 24.291 -4.429 0.00 89.97 C ANISOU 1842 CB GLN A 238 11352 11267 11564 -1739 1572 -4314 C ATOM 1843 CG GLN A 238 13.306 25.166 -5.037 0.00 97.20 C ANISOU 1843 CG GLN A 238 12210 11777 12947 -1603 1796 -4328 C ATOM 1844 CD GLN A 238 12.486 25.920 -4.004 0.00 99.82 C ANISOU 1844 CD GLN A 238 12499 12073 13356 -1702 2052 -4754 C ATOM 1845 NE2 GLN A 238 11.232 26.200 -4.340 0.00 99.30 N ANISOU 1845 NE2 GLN A 238 12392 11765 13573 -1556 2223 -4700 N ATOM 1846 OE1 GLN A 238 12.973 26.253 -2.923 0.00102.05 O ANISOU 1846 OE1 GLN A 238 12774 12552 13448 -1912 2098 -5136 O ATOM 1847 N PRO A 246 15.573 26.518 -18.470 1.00 60.27 N ANISOU 1847 N PRO A 246 7221 5481 10198 -605 1287 -945 N ATOM 1848 CA PRO A 246 15.933 25.172 -18.936 1.00 67.11 C ANISOU 1848 CA PRO A 246 8182 6662 10654 -587 1124 -807 C ATOM 1849 C PRO A 246 17.192 24.609 -18.247 1.00 62.40 C ANISOU 1849 C PRO A 246 7641 6251 9816 -700 1047 -1030 C ATOM 1850 O PRO A 246 17.080 23.644 -17.470 1.00 55.51 O ANISOU 1850 O PRO A 246 6844 5596 8650 -709 969 -1172 O ATOM 1851 CB PRO A 246 16.138 25.357 -20.453 1.00 56.76 C ANISOU 1851 CB PRO A 246 6826 5316 9423 -545 1096 -432 C ATOM 1852 CG PRO A 246 16.324 26.837 -20.664 1.00 65.64 C ANISOU 1852 CG PRO A 246 7832 6112 10995 -573 1231 -389 C ATOM 1853 CD PRO A 246 16.069 27.570 -19.370 1.00 65.01 C ANISOU 1853 CD PRO A 246 7719 5841 11140 -618 1355 -745 C ATOM 1854 N TYR A 247 18.353 25.223 -18.520 1.00 46.39 N ANISOU 1854 N TYR A 247 5563 4135 7930 -786 1068 -1042 N ATOM 1855 CA TYR A 247 19.645 24.825 -17.943 1.00 42.09 C ANISOU 1855 CA TYR A 247 5036 3745 7210 -900 993 -1230 C ATOM 1856 C TYR A 247 19.653 24.961 -16.430 1.00 40.52 C ANISOU 1856 C TYR A 247 4850 3589 6956 -992 1013 -1601 C ATOM 1857 O TYR A 247 19.570 26.066 -15.925 1.00 44.20 O ANISOU 1857 O TYR A 247 5255 3842 7697 -1055 1139 -1797 O ATOM 1858 CB TYR A 247 20.776 25.668 -18.544 1.00 38.30 C ANISOU 1858 CB TYR A 247 4472 3115 6964 -978 1040 -1171 C ATOM 1859 CG TYR A 247 22.164 25.303 -18.062 1.00 40.30 C ANISOU 1859 CG TYR A 247 4719 3522 7072 -1095 958 -1336 C ATOM 1860 CD1 TYR A 247 22.882 24.247 -18.643 1.00 41.02 C ANISOU 1860 CD1 TYR A 247 4838 3832 6915 -1078 844 -1188 C ATOM 1861 CD2 TYR A 247 22.770 26.015 -17.034 1.00 40.35 C ANISOU 1861 CD2 TYR A 247 4675 3455 7202 -1229 998 -1649 C ATOM 1862 CE1 TYR A 247 24.159 23.911 -18.201 1.00 30.60 C ANISOU 1862 CE1 TYR A 247 3486 2644 5495 -1177 766 -1320 C ATOM 1863 CE2 TYR A 247 24.038 25.686 -16.585 1.00 39.69 C ANISOU 1863 CE2 TYR A 247 4565 3527 6986 -1342 906 -1784 C ATOM 1864 CZ TYR A 247 24.728 24.632 -17.163 1.00 35.36 C ANISOU 1864 CZ TYR A 247 4035 3187 6212 -1309 787 -1606 C ATOM 1865 OH TYR A 247 25.996 24.343 -16.717 1.00 28.54 O ANISOU 1865 OH TYR A 247 3121 2464 5260 -1415 696 -1725 O ATOM 1866 N HIS A 248 19.722 23.827 -15.731 1.00 38.73 N ANISOU 1866 N HIS A 248 4697 3641 6378 -1003 895 -1689 N ATOM 1867 CA HIS A 248 19.847 23.778 -14.280 1.00 44.29 C ANISOU 1867 CA HIS A 248 5417 4474 6939 -1112 884 -2016 C ATOM 1868 C HIS A 248 21.160 23.044 -13.953 1.00 35.29 C ANISOU 1868 C HIS A 248 4276 3571 5563 -1201 733 -2055 C ATOM 1869 O HIS A 248 21.299 21.871 -14.246 1.00 26.70 O ANISOU 1869 O HIS A 248 3231 2674 4241 -1140 612 -1884 O ATOM 1870 CB HIS A 248 18.635 23.061 -13.674 1.00 58.92 C ANISOU 1870 CB HIS A 248 7341 6461 8585 -1043 876 -2044 C ATOM 1871 CG HIS A 248 18.411 23.359 -12.219 1.00 95.26 C ANISOU 1871 CG HIS A 248 11948 11144 13104 -1156 931 -2391 C ATOM 1872 CD2 HIS A 248 17.351 23.909 -11.579 1.00127.46 C ANISOU 1872 CD2 HIS A 248 16022 15125 17283 -1153 1073 -2576 C ATOM 1873 ND1 HIS A 248 19.338 23.069 -11.238 1.00 88.31 N ANISOU 1873 ND1 HIS A 248 11067 10490 11996 -1299 838 -2593 N ATOM 1874 CE1 HIS A 248 18.864 23.439 -10.062 1.00112.79 C ANISOU 1874 CE1 HIS A 248 14171 13651 15032 -1393 919 -2894 C ATOM 1875 NE2 HIS A 248 17.660 23.950 -10.240 1.00137.66 N ANISOU 1875 NE2 HIS A 248 17320 16598 18386 -1305 1074 -2902 N ATOM 1876 N HIS A 249 22.115 23.752 -13.354 1.00 38.46 N ANISOU 1876 N HIS A 249 4612 3946 6054 -1349 745 -2282 N ATOM 1877 CA HIS A 249 23.465 23.231 -13.117 1.00 36.32 C ANISOU 1877 CA HIS A 249 4305 3870 5627 -1442 604 -2305 C ATOM 1878 C HIS A 249 23.483 22.027 -12.178 1.00 37.05 C ANISOU 1878 C HIS A 249 4443 4292 5342 -1461 453 -2343 C ATOM 1879 O HIS A 249 24.080 20.991 -12.501 1.00 30.70 O ANISOU 1879 O HIS A 249 3637 3649 4380 -1419 321 -2162 O ATOM 1880 CB HIS A 249 24.366 24.326 -12.532 1.00 38.35 C ANISOU 1880 CB HIS A 249 4471 4037 6065 -1616 650 -2580 C ATOM 1881 CG HIS A 249 25.740 23.847 -12.171 1.00 41.19 C ANISOU 1881 CG HIS A 249 4769 4609 6270 -1726 496 -2620 C ATOM 1882 CD2 HIS A 249 26.892 23.825 -12.880 1.00 40.57 C ANISOU 1882 CD2 HIS A 249 4616 4506 6293 -1746 447 -2491 C ATOM 1883 ND1 HIS A 249 26.037 23.288 -10.947 1.00 43.21 N ANISOU 1883 ND1 HIS A 249 5026 5160 6233 -1831 368 -2792 N ATOM 1884 CE1 HIS A 249 27.314 22.953 -10.913 1.00 42.78 C ANISOU 1884 CE1 HIS A 249 4889 5243 6123 -1907 236 -2759 C ATOM 1885 NE2 HIS A 249 27.855 23.267 -12.074 1.00 45.68 N ANISOU 1885 NE2 HIS A 249 5210 5412 6734 -1855 288 -2589 N ATOM 1886 N ASP A 250 22.858 22.189 -11.009 1.00 32.45 N ANISOU 1886 N ASP A 250 3889 3805 4634 -1531 483 -2580 N ATOM 1887 CA ASP A 250 22.865 21.149 -9.971 1.00 31.58 C ANISOU 1887 CA ASP A 250 3812 4029 4158 -1576 344 -2617 C ATOM 1888 C ASP A 250 22.160 19.876 -10.371 1.00 27.81 C ANISOU 1888 C ASP A 250 3405 3654 3505 -1422 277 -2347 C ATOM 1889 O ASP A 250 22.536 18.804 -9.912 1.00 28.89 O ANISOU 1889 O ASP A 250 3542 4038 3395 -1431 128 -2256 O ATOM 1890 CB ASP A 250 22.258 21.665 -8.665 1.00 36.56 C ANISOU 1890 CB ASP A 250 4460 4754 4678 -1697 419 -2938 C ATOM 1891 CG ASP A 250 23.171 22.638 -7.933 1.00 41.74 C ANISOU 1891 CG ASP A 250 5034 5426 5399 -1902 434 -3259 C ATOM 1892 OD1 ASP A 250 24.343 22.820 -8.341 1.00 35.83 O ANISOU 1892 OD1 ASP A 250 4211 4644 4760 -1954 361 -3216 O ATOM 1893 OD2 ASP A 250 22.709 23.211 -6.926 1.00 52.91 O1- ANISOU 1893 OD2 ASP A 250 6453 6897 6753 -2022 526 -3571 O1- ATOM 1894 N GLN A 251 21.141 19.989 -11.217 1.00 26.18 N ANISOU 1894 N GLN A 251 3246 3257 3443 -1286 382 -2212 N ATOM 1895 CA GLN A 251 20.443 18.833 -11.709 1.00 22.53 C ANISOU 1895 CA GLN A 251 2844 2871 2847 -1147 327 -1969 C ATOM 1896 C GLN A 251 21.379 18.037 -12.627 1.00 23.06 C ANISOU 1896 C GLN A 251 2882 2976 2903 -1095 219 -1746 C ATOM 1897 O GLN A 251 21.443 16.799 -12.548 1.00 21.72 O ANISOU 1897 O GLN A 251 2727 2975 2549 -1048 108 -1610 O ATOM 1898 CB GLN A 251 19.161 19.250 -12.438 1.00 22.05 C ANISOU 1898 CB GLN A 251 2819 2602 2959 -1029 460 -1884 C ATOM 1899 CG GLN A 251 18.307 18.065 -12.895 1.00 19.36 C ANISOU 1899 CG GLN A 251 2535 2346 2476 -901 408 -1663 C ATOM 1900 CD GLN A 251 17.831 17.194 -11.739 1.00 20.38 C ANISOU 1900 CD GLN A 251 2704 2704 2335 -926 349 -1725 C ATOM 1901 NE2 GLN A 251 18.460 16.047 -11.559 1.00 24.91 N ANISOU 1901 NE2 GLN A 251 3277 3471 2719 -930 206 -1613 N ATOM 1902 OE1 GLN A 251 16.913 17.561 -11.007 1.00 23.21 O ANISOU 1902 OE1 GLN A 251 3084 3064 2671 -945 439 -1867 O ATOM 1903 N LEU A 252 22.109 18.754 -13.480 1.00 22.16 N ANISOU 1903 N LEU A 252 2717 2699 3004 -1108 264 -1713 N ATOM 1904 CA LEU A 252 23.134 18.137 -14.322 1.00 23.28 C ANISOU 1904 CA LEU A 252 2815 2877 3155 -1082 188 -1544 C ATOM 1905 C LEU A 252 24.273 17.518 -13.489 1.00 21.29 C ANISOU 1905 C LEU A 252 2499 2834 2756 -1171 43 -1602 C ATOM 1906 O LEU A 252 24.667 16.379 -13.722 1.00 22.78 O ANISOU 1906 O LEU A 252 2670 3141 2846 -1116 -54 -1451 O ATOM 1907 CB LEU A 252 23.688 19.144 -15.342 1.00 22.24 C ANISOU 1907 CB LEU A 252 2631 2536 3283 -1097 282 -1500 C ATOM 1908 CG LEU A 252 22.778 19.511 -16.524 1.00 21.14 C ANISOU 1908 CG LEU A 252 2528 2222 3283 -992 391 -1326 C ATOM 1909 CD1 LEU A 252 23.322 20.739 -17.247 1.00 25.51 C ANISOU 1909 CD1 LEU A 252 3015 2564 4112 -1038 493 -1301 C ATOM 1910 CD2 LEU A 252 22.654 18.364 -17.508 1.00 19.77 C ANISOU 1910 CD2 LEU A 252 2385 2144 2984 -890 341 -1104 C ATOM 1911 N ASP A 253 24.791 18.259 -12.517 1.00 24.13 N ANISOU 1911 N ASP A 253 2812 3240 3116 -1312 28 -1822 N ATOM 1912 CA ASP A 253 25.760 17.704 -11.569 1.00 26.20 C ANISOU 1912 CA ASP A 253 3004 3743 3209 -1413 -130 -1875 C ATOM 1913 C ASP A 253 25.320 16.357 -10.949 1.00 28.28 C ANISOU 1913 C ASP A 253 3301 4233 3212 -1359 -249 -1750 C ATOM 1914 O ASP A 253 26.138 15.459 -10.757 1.00 25.34 O ANISOU 1914 O ASP A 253 2856 4015 2756 -1363 -389 -1631 O ATOM 1915 CB ASP A 253 25.998 18.694 -10.445 1.00 29.96 C ANISOU 1915 CB ASP A 253 3446 4276 3661 -1587 -120 -2169 C ATOM 1916 CG ASP A 253 26.960 18.171 -9.411 1.00 35.18 C ANISOU 1916 CG ASP A 253 4023 5227 4117 -1711 -302 -2215 C ATOM 1917 OD1 ASP A 253 28.008 17.626 -9.798 1.00 37.38 O ANISOU 1917 OD1 ASP A 253 4212 5554 4437 -1697 -408 -2068 O ATOM 1918 OD2 ASP A 253 26.669 18.309 -8.211 1.00 42.39 O1- ANISOU 1918 OD2 ASP A 253 4949 6330 4827 -1827 -337 -2395 O1- ATOM 1919 N ARG A 254 24.036 16.237 -10.615 1.00 26.20 N ANISOU 1919 N ARG A 254 3131 3978 2844 -1311 -187 -1771 N ATOM 1920 CA ARG A 254 23.512 15.007 -10.017 1.00 27.62 C ANISOU 1920 CA ARG A 254 3343 4357 2795 -1265 -281 -1644 C ATOM 1921 C ARG A 254 23.484 13.870 -11.027 1.00 22.35 C ANISOU 1921 C ARG A 254 2678 3635 2179 -1117 -314 -1385 C ATOM 1922 O ARG A 254 23.843 12.750 -10.697 1.00 27.05 O ANISOU 1922 O ARG A 254 3229 4380 2669 -1096 -437 -1241 O ATOM 1923 CB ARG A 254 22.113 15.232 -9.427 1.00 33.64 C ANISOU 1923 CB ARG A 254 4197 5133 3451 -1258 -185 -1745 C ATOM 1924 CG ARG A 254 21.399 13.964 -8.948 1.00 38.45 C ANISOU 1924 CG ARG A 254 4844 5914 3851 -1197 -255 -1585 C ATOM 1925 CD ARG A 254 22.121 13.237 -7.809 1.00 36.89 C ANISOU 1925 CD ARG A 254 4583 6017 3418 -1297 -425 -1542 C ATOM 1926 NE ARG A 254 21.420 12.013 -7.430 1.00 34.85 N ANISOU 1926 NE ARG A 254 4351 5892 2998 -1232 -482 -1350 N ATOM 1927 CZ ARG A 254 21.824 11.129 -6.517 1.00 36.21 C ANISOU 1927 CZ ARG A 254 4465 6323 2970 -1288 -633 -1220 C ATOM 1928 NH1 ARG A 254 22.950 11.294 -5.845 1.00 42.54 N1+ ANISOU 1928 NH1 ARG A 254 5174 7308 3681 -1415 -764 -1259 N1+ ATOM 1929 NH2 ARG A 254 21.084 10.052 -6.280 1.00 39.12 N ANISOU 1929 NH2 ARG A 254 4857 6768 3237 -1218 -660 -1029 N ATOM 1930 N ILE A 255 23.067 14.153 -12.255 1.00 19.12 N ANISOU 1930 N ILE A 255 2308 3016 1940 -1022 -203 -1323 N ATOM 1931 CA ILE A 255 23.084 13.144 -13.310 1.00 15.07 C ANISOU 1931 CA ILE A 255 1793 2457 1477 -903 -216 -1120 C ATOM 1932 C ILE A 255 24.499 12.600 -13.516 1.00 16.37 C ANISOU 1932 C ILE A 255 1848 2676 1696 -922 -310 -1046 C ATOM 1933 O ILE A 255 24.691 11.398 -13.621 1.00 18.47 O ANISOU 1933 O ILE A 255 2077 3008 1934 -859 -381 -906 O ATOM 1934 CB ILE A 255 22.510 13.692 -14.633 1.00 18.45 C ANISOU 1934 CB ILE A 255 2268 2686 2057 -828 -86 -1073 C ATOM 1935 CG1 ILE A 255 21.003 13.981 -14.485 1.00 23.17 C ANISOU 1935 CG1 ILE A 255 2953 3231 2618 -782 -6 -1098 C ATOM 1936 CG2 ILE A 255 22.720 12.695 -15.778 1.00 18.05 C ANISOU 1936 CG2 ILE A 255 2201 2616 2041 -737 -93 -906 C ATOM 1937 CD1 ILE A 255 20.398 14.890 -15.546 1.00 18.92 C ANISOU 1937 CD1 ILE A 255 2441 2501 2247 -736 117 -1065 C ATOM 1938 N PHE A 256 25.486 13.483 -13.558 1.00 19.11 N ANISOU 1938 N PHE A 256 2128 2984 2149 -1009 -303 -1144 N ATOM 1939 CA PHE A 256 26.873 13.064 -13.762 1.00 20.99 C ANISOU 1939 CA PHE A 256 2242 3266 2467 -1031 -383 -1082 C ATOM 1940 C PHE A 256 27.465 12.332 -12.555 1.00 23.46 C ANISOU 1940 C PHE A 256 2469 3797 2647 -1089 -555 -1051 C ATOM 1941 O PHE A 256 28.264 11.406 -12.746 1.00 26.98 O ANISOU 1941 O PHE A 256 2811 4287 3152 -1048 -635 -914 O ATOM 1942 CB PHE A 256 27.757 14.252 -14.149 1.00 22.24 C ANISOU 1942 CB PHE A 256 2341 3318 2791 -1118 -324 -1190 C ATOM 1943 CG PHE A 256 27.273 15.015 -15.358 1.00 23.13 C ANISOU 1943 CG PHE A 256 2515 3225 3046 -1070 -164 -1173 C ATOM 1944 CD1 PHE A 256 26.667 14.374 -16.445 1.00 23.43 C ANISOU 1944 CD1 PHE A 256 2608 3205 3089 -952 -99 -1027 C ATOM 1945 CD2 PHE A 256 27.456 16.386 -15.422 1.00 21.80 C ANISOU 1945 CD2 PHE A 256 2337 2928 3017 -1154 -79 -1297 C ATOM 1946 CE1 PHE A 256 26.235 15.109 -17.540 1.00 20.71 C ANISOU 1946 CE1 PHE A 256 2308 2710 2852 -923 31 -984 C ATOM 1947 CE2 PHE A 256 27.044 17.109 -16.519 1.00 20.84 C ANISOU 1947 CE2 PHE A 256 2253 2622 3042 -1113 60 -1238 C ATOM 1948 CZ PHE A 256 26.434 16.473 -17.578 1.00 21.07 C ANISOU 1948 CZ PHE A 256 2337 2627 3042 -999 107 -1069 C ATOM 1949 N ASN A 257 27.097 12.727 -11.329 1.00 22.56 N ANISOU 1949 N ASN A 257 2384 3827 2361 -1187 -608 -1170 N ATOM 1950 CA ASN A 257 27.489 11.963 -10.127 1.00 26.13 C ANISOU 1950 CA ASN A 257 2760 4535 2634 -1248 -783 -1102 C ATOM 1951 C ASN A 257 26.932 10.534 -10.128 1.00 24.98 C ANISOU 1951 C ASN A 257 2627 4439 2427 -1129 -834 -878 C ATOM 1952 O ASN A 257 27.561 9.641 -9.580 1.00 28.51 O ANISOU 1952 O ASN A 257 2964 5034 2835 -1136 -980 -723 O ATOM 1953 CB ASN A 257 27.079 12.672 -8.830 1.00 29.64 C ANISOU 1953 CB ASN A 257 3244 5155 2862 -1393 -810 -1292 C ATOM 1954 CG ASN A 257 27.986 13.840 -8.494 1.00 38.49 C ANISOU 1954 CG ASN A 257 4294 6297 4032 -1550 -822 -1509 C ATOM 1955 ND2 ASN A 257 27.399 15.011 -8.261 1.00 42.65 N ANISOU 1955 ND2 ASN A 257 4898 6746 4560 -1629 -696 -1757 N ATOM 1956 OD1 ASN A 257 29.205 13.691 -8.442 1.00 49.80 O ANISOU 1956 OD1 ASN A 257 5592 7802 5526 -1603 -937 -1459 O ATOM 1957 N VAL A 258 25.777 10.319 -10.757 1.00 21.87 N ANISOU 1957 N VAL A 258 2349 3914 2048 -1025 -717 -849 N ATOM 1958 CA VAL A 258 25.238 8.970 -10.932 1.00 23.03 C ANISOU 1958 CA VAL A 258 2502 4064 2187 -911 -743 -651 C ATOM 1959 C VAL A 258 25.834 8.274 -12.149 1.00 20.91 C ANISOU 1959 C VAL A 258 2166 3642 2135 -808 -710 -540 C ATOM 1960 O VAL A 258 26.340 7.158 -12.036 1.00 19.01 O ANISOU 1960 O VAL A 258 1823 3440 1958 -762 -797 -379 O ATOM 1961 CB VAL A 258 23.706 8.975 -11.064 1.00 18.89 C ANISOU 1961 CB VAL A 258 2116 3478 1584 -853 -636 -675 C ATOM 1962 CG1 VAL A 258 23.167 7.563 -11.256 1.00 17.39 C ANISOU 1962 CG1 VAL A 258 1921 3278 1408 -747 -660 -481 C ATOM 1963 CG2 VAL A 258 23.076 9.586 -9.821 1.00 21.22 C ANISOU 1963 CG2 VAL A 258 2468 3931 1665 -955 -645 -800 C ATOM 1964 N MET A 259 25.741 8.928 -13.303 1.00 18.26 N ANISOU 1964 N MET A 259 1882 3138 1918 -777 -578 -623 N ATOM 1965 CA MET A 259 26.010 8.296 -14.599 1.00 17.35 C ANISOU 1965 CA MET A 259 1734 2889 1968 -685 -505 -549 C ATOM 1966 C MET A 259 27.461 8.388 -15.067 1.00 22.43 C ANISOU 1966 C MET A 259 2245 3502 2775 -709 -515 -549 C ATOM 1967 O MET A 259 27.872 7.629 -15.937 1.00 23.10 O ANISOU 1967 O MET A 259 2267 3511 2999 -641 -468 -487 O ATOM 1968 CB MET A 259 25.131 8.942 -15.679 1.00 19.89 C ANISOU 1968 CB MET A 259 2172 3077 2306 -648 -357 -611 C ATOM 1969 CG MET A 259 23.621 8.855 -15.453 1.00 17.94 C ANISOU 1969 CG MET A 259 2046 2833 1939 -609 -324 -608 C ATOM 1970 SD MET A 259 22.976 7.175 -15.383 1.00 22.76 S ANISOU 1970 SD MET A 259 2648 3472 2526 -519 -366 -467 S ATOM 1971 CE MET A 259 23.359 6.556 -17.008 1.00 12.28 C ANISOU 1971 CE MET A 259 1282 2023 1359 -452 -273 -443 C ATOM 1972 N GLY A 260 28.239 9.299 -14.498 1.00 20.07 N ANISOU 1972 N GLY A 260 1893 3261 2471 -813 -567 -634 N ATOM 1973 CA GLY A 260 29.508 9.703 -15.101 1.00 24.95 C ANISOU 1973 CA GLY A 260 2397 3823 3258 -848 -542 -663 C ATOM 1974 C GLY A 260 29.282 10.797 -16.140 1.00 21.75 C ANISOU 1974 C GLY A 260 2072 3276 2917 -863 -385 -755 C ATOM 1975 O GLY A 260 28.155 11.126 -16.483 1.00 18.77 O ANISOU 1975 O GLY A 260 1825 2838 2470 -829 -302 -776 O ATOM 1976 N PHE A 261 30.370 11.385 -16.602 1.00 20.22 N ANISOU 1976 N PHE A 261 1784 3035 2864 -917 -349 -793 N ATOM 1977 CA PHE A 261 30.330 12.430 -17.611 1.00 24.12 C ANISOU 1977 CA PHE A 261 2325 3397 3442 -941 -202 -842 C ATOM 1978 C PHE A 261 30.440 11.741 -18.962 1.00 22.15 C ANISOU 1978 C PHE A 261 2062 3091 3263 -860 -93 -756 C ATOM 1979 O PHE A 261 31.337 10.911 -19.146 1.00 22.02 O ANISOU 1979 O PHE A 261 1922 3101 3341 -835 -114 -714 O ATOM 1980 CB PHE A 261 31.492 13.412 -17.403 1.00 25.79 C ANISOU 1980 CB PHE A 261 2429 3591 3780 -1057 -212 -926 C ATOM 1981 CG PHE A 261 31.268 14.753 -18.031 1.00 24.59 C ANISOU 1981 CG PHE A 261 2333 3298 3712 -1108 -80 -983 C ATOM 1982 CD1 PHE A 261 30.590 15.738 -17.354 1.00 27.41 C ANISOU 1982 CD1 PHE A 261 2766 3613 4035 -1168 -74 -1096 C ATOM 1983 CD2 PHE A 261 31.732 15.022 -19.306 1.00 27.57 C ANISOU 1983 CD2 PHE A 261 2677 3583 4215 -1098 50 -917 C ATOM 1984 CE1 PHE A 261 30.382 16.976 -17.934 1.00 30.36 C ANISOU 1984 CE1 PHE A 261 3172 3825 4540 -1208 54 -1127 C ATOM 1985 CE2 PHE A 261 31.538 16.256 -19.890 1.00 25.75 C ANISOU 1985 CE2 PHE A 261 2484 3220 4081 -1146 168 -926 C ATOM 1986 CZ PHE A 261 30.856 17.235 -19.204 1.00 28.05 C ANISOU 1986 CZ PHE A 261 2841 3439 4377 -1196 168 -1022 C ATOM 1987 N PRO A 262 29.530 12.055 -19.909 1.00 22.39 N ANISOU 1987 N PRO A 262 2205 3052 3250 -823 25 -731 N ATOM 1988 CA PRO A 262 29.534 11.332 -21.194 1.00 21.50 C ANISOU 1988 CA PRO A 262 2086 2927 3154 -764 129 -671 C ATOM 1989 C PRO A 262 30.778 11.656 -21.989 1.00 23.93 C ANISOU 1989 C PRO A 262 2281 3210 3601 -812 217 -674 C ATOM 1990 O PRO A 262 31.148 12.813 -22.085 1.00 25.15 O ANISOU 1990 O PRO A 262 2424 3312 3821 -887 258 -690 O ATOM 1991 CB PRO A 262 28.294 11.867 -21.917 1.00 16.01 C ANISOU 1991 CB PRO A 262 1527 2194 2362 -743 213 -635 C ATOM 1992 CG PRO A 262 28.065 13.204 -21.330 1.00 19.94 C ANISOU 1992 CG PRO A 262 2063 2626 2887 -804 203 -672 C ATOM 1993 CD PRO A 262 28.596 13.192 -19.923 1.00 21.07 C ANISOU 1993 CD PRO A 262 2149 2814 3042 -849 78 -759 C ATOM 1994 N ALA A 263 31.443 10.632 -22.503 1.00 25.40 N ANISOU 1994 N ALA A 263 2372 3422 3859 -774 255 -665 N ATOM 1995 CA ALA A 263 32.572 10.821 -23.404 1.00 27.32 C ANISOU 1995 CA ALA A 263 2502 3650 4229 -816 371 -674 C ATOM 1996 C ALA A 263 32.031 11.298 -24.735 1.00 24.97 C ANISOU 1996 C ALA A 263 2294 3353 3842 -833 525 -639 C ATOM 1997 O ALA A 263 30.830 11.138 -25.020 1.00 24.32 O ANISOU 1997 O ALA A 263 2337 3290 3612 -794 531 -611 O ATOM 1998 CB ALA A 263 33.341 9.518 -23.580 1.00 29.70 C ANISOU 1998 CB ALA A 263 2666 3969 4650 -762 387 -690 C ATOM 1999 N ASP A 264 32.917 11.881 -25.542 1.00 26.13 N ANISOU 1999 N ASP A 264 2364 3493 4073 -899 643 -628 N ATOM 2000 CA ASP A 264 32.590 12.306 -26.921 1.00 27.72 C ANISOU 2000 CA ASP A 264 2622 3733 4179 -934 799 -566 C ATOM 2001 C ASP A 264 31.886 11.185 -27.686 1.00 25.58 C ANISOU 2001 C ASP A 264 2406 3550 3763 -880 856 -591 C ATOM 2002 O ASP A 264 30.823 11.410 -28.264 1.00 21.15 O ANISOU 2002 O ASP A 264 1961 3036 3038 -880 880 -529 O ATOM 2003 CB ASP A 264 33.858 12.725 -27.689 1.00 34.03 C ANISOU 2003 CB ASP A 264 3293 4540 5097 -1011 934 -559 C ATOM 2004 CG ASP A 264 34.539 13.976 -27.107 1.00 40.40 C ANISOU 2004 CG ASP A 264 4040 5251 6059 -1087 899 -535 C ATOM 2005 OD1 ASP A 264 33.905 14.723 -26.320 1.00 27.76 O ANISOU 2005 OD1 ASP A 264 2517 3578 4453 -1093 802 -522 O ATOM 2006 OD2 ASP A 264 35.723 14.210 -27.450 1.00 48.01 O1- ANISOU 2006 OD2 ASP A 264 4868 6208 7164 -1148 982 -544 O1- ATOM 2007 N LYS A 265 32.470 9.981 -27.632 1.00 30.94 N ANISOU 2007 N LYS A 265 2987 4242 4528 -837 871 -683 N ATOM 2008 CA LYS A 265 31.929 8.764 -28.290 1.00 28.14 C ANISOU 2008 CA LYS A 265 2657 3948 4088 -792 937 -754 C ATOM 2009 C LYS A 265 30.524 8.325 -27.816 1.00 25.04 C ANISOU 2009 C LYS A 265 2395 3555 3563 -730 828 -736 C ATOM 2010 O LYS A 265 29.780 7.776 -28.603 1.00 17.71 O ANISOU 2010 O LYS A 265 1528 2697 2502 -728 892 -771 O ATOM 2011 CB LYS A 265 32.913 7.584 -28.152 1.00 25.88 C ANISOU 2011 CB LYS A 265 2209 3623 4001 -750 974 -857 C ATOM 2012 CG LYS A 265 32.639 6.413 -29.039 0.00 28.40 C ANISOU 2012 CG LYS A 265 2516 3987 4289 -730 1101 -974 C ATOM 2013 CD LYS A 265 33.806 5.439 -29.077 0.00 29.84 C ANISOU 2013 CD LYS A 265 2503 4104 4729 -698 1186 -1079 C ATOM 2014 CE LYS A 265 33.547 4.300 -30.050 0.00 30.58 C ANISOU 2014 CE LYS A 265 2577 4231 4811 -694 1348 -1242 C ATOM 2015 NZ LYS A 265 34.703 3.366 -30.140 0.00 32.23 N1+ ANISOU 2015 NZ LYS A 265 2574 4350 5321 -659 1461 -1359 N1+ ATOM 2016 N ASP A 266 30.172 8.577 -26.552 1.00 24.17 N ANISOU 2016 N ASP A 266 2321 3381 3480 -694 671 -692 N ATOM 2017 CA ASP A 266 28.843 8.226 -25.997 1.00 28.34 C ANISOU 2017 CA ASP A 266 2966 3909 3894 -638 573 -669 C ATOM 2018 C ASP A 266 27.690 9.125 -26.482 1.00 30.03 C ANISOU 2018 C ASP A 266 3316 4156 3938 -662 587 -595 C ATOM 2019 O ASP A 266 26.542 8.670 -26.558 1.00 29.66 O ANISOU 2019 O ASP A 266 3354 4138 3777 -626 559 -587 O ATOM 2020 CB ASP A 266 28.853 8.263 -24.450 1.00 28.97 C ANISOU 2020 CB ASP A 266 3035 3938 4034 -607 411 -647 C ATOM 2021 CG ASP A 266 29.916 7.346 -23.828 1.00 40.98 C ANISOU 2021 CG ASP A 266 4405 5436 5731 -577 359 -670 C ATOM 2022 OD1 ASP A 266 30.215 6.282 -24.425 1.00 44.61 O ANISOU 2022 OD1 ASP A 266 4789 5884 6277 -541 437 -716 O ATOM 2023 OD2 ASP A 266 30.441 7.692 -22.735 1.00 34.39 O1- ANISOU 2023 OD2 ASP A 266 3515 4596 4957 -594 241 -644 O1- ATOM 2024 N TRP A 267 27.986 10.394 -26.774 1.00 24.93 N ANISOU 2024 N TRP A 267 2675 3493 3302 -723 628 -530 N ATOM 2025 CA TRP A 267 26.966 11.356 -27.217 1.00 23.53 C ANISOU 2025 CA TRP A 267 2598 3323 3018 -742 641 -422 C ATOM 2026 C TRP A 267 27.604 12.373 -28.173 1.00 26.21 C ANISOU 2026 C TRP A 267 2899 3678 3382 -822 752 -336 C ATOM 2027 O TRP A 267 27.937 13.487 -27.779 1.00 26.92 O ANISOU 2027 O TRP A 267 2970 3671 3586 -857 745 -287 O ATOM 2028 CB TRP A 267 26.353 12.033 -25.981 1.00 20.12 C ANISOU 2028 CB TRP A 267 2221 2795 2630 -716 532 -409 C ATOM 2029 CG TRP A 267 25.134 12.867 -26.213 1.00 19.56 C ANISOU 2029 CG TRP A 267 2238 2698 2495 -708 532 -306 C ATOM 2030 CD1 TRP A 267 24.519 13.142 -27.407 1.00 21.26 C ANISOU 2030 CD1 TRP A 267 2487 2982 2610 -725 597 -186 C ATOM 2031 CD2 TRP A 267 24.380 13.560 -25.208 1.00 18.63 C ANISOU 2031 CD2 TRP A 267 2171 2484 2422 -685 466 -308 C ATOM 2032 CE2 TRP A 267 23.322 14.231 -25.864 1.00 17.92 C ANISOU 2032 CE2 TRP A 267 2134 2382 2295 -675 499 -178 C ATOM 2033 CE3 TRP A 267 24.506 13.693 -23.821 1.00 16.34 C ANISOU 2033 CE3 TRP A 267 1878 2133 2196 -681 387 -409 C ATOM 2034 NE1 TRP A 267 23.419 13.944 -27.199 1.00 19.77 N ANISOU 2034 NE1 TRP A 267 2355 2728 2427 -701 565 -91 N ATOM 2035 CZ2 TRP A 267 22.396 15.025 -25.177 1.00 19.98 C ANISOU 2035 CZ2 TRP A 267 2435 2535 2620 -649 471 -158 C ATOM 2036 CZ3 TRP A 267 23.585 14.477 -23.140 1.00 17.81 C ANISOU 2036 CZ3 TRP A 267 2118 2238 2409 -670 367 -414 C ATOM 2037 CH2 TRP A 267 22.537 15.127 -23.818 1.00 17.29 C ANISOU 2037 CH2 TRP A 267 2097 2128 2345 -647 416 -295 C ATOM 2038 N GLU A 268 27.771 11.970 -29.433 1.00 37.60 N ANISOU 2038 N GLU A 268 4324 5247 4717 -861 864 -323 N ATOM 2039 CA GLU A 268 28.482 12.778 -30.452 1.00 39.37 C ANISOU 2039 CA GLU A 268 4496 5523 4941 -949 990 -230 C ATOM 2040 C GLU A 268 27.839 14.126 -30.806 1.00 35.05 C ANISOU 2040 C GLU A 268 3998 4946 4373 -984 993 -28 C ATOM 2041 O GLU A 268 28.556 15.101 -31.040 1.00 47.87 O ANISOU 2041 O GLU A 268 5564 6515 6109 -1047 1059 61 O ATOM 2042 CB GLU A 268 28.709 11.965 -31.732 1.00 40.80 C ANISOU 2042 CB GLU A 268 4649 5885 4967 -997 1119 -280 C ATOM 2043 CG GLU A 268 29.749 10.865 -31.563 1.00 46.84 C ANISOU 2043 CG GLU A 268 5312 6642 5842 -980 1173 -469 C ATOM 2044 CD GLU A 268 30.120 10.169 -32.861 1.00 51.25 C ANISOU 2044 CD GLU A 268 5824 7372 6277 -1045 1341 -557 C ATOM 2045 OE1 GLU A 268 30.207 10.840 -33.910 1.00 46.61 O ANISOU 2045 OE1 GLU A 268 5240 6917 5552 -1138 1446 -452 O ATOM 2046 OE2 GLU A 268 30.346 8.940 -32.824 1.00 54.66 O1- ANISOU 2046 OE2 GLU A 268 6206 7806 6757 -1010 1376 -734 O1- ATOM 2047 N ASP A 269 26.506 14.171 -30.831 1.00 36.61 N ANISOU 2047 N ASP A 269 4284 5165 4459 -943 925 52 N ATOM 2048 CA ASP A 269 25.741 15.405 -31.107 1.00 40.07 C ANISOU 2048 CA ASP A 269 4754 5553 4918 -957 917 265 C ATOM 2049 C ASP A 269 25.530 16.316 -29.898 1.00 35.13 C ANISOU 2049 C ASP A 269 4137 4704 4507 -918 848 261 C ATOM 2050 O ASP A 269 24.747 17.259 -29.982 1.00 42.65 O ANISOU 2050 O ASP A 269 5109 5575 5521 -909 839 418 O ATOM 2051 CB ASP A 269 24.353 15.062 -31.690 1.00 46.47 C ANISOU 2051 CB ASP A 269 5636 6491 5530 -931 870 362 C ATOM 2052 CG ASP A 269 24.424 14.506 -33.099 1.00 54.73 C ANISOU 2052 CG ASP A 269 6669 7788 6336 -1006 951 404 C ATOM 2053 OD1 ASP A 269 25.277 14.972 -33.887 1.00 44.37 O ANISOU 2053 OD1 ASP A 269 5300 6548 5012 -1090 1058 486 O ATOM 2054 OD2 ASP A 269 23.596 13.620 -33.418 1.00 52.12 O1- ANISOU 2054 OD2 ASP A 269 6385 7594 5826 -992 911 349 O1- ATOM 2055 N ILE A 270 26.204 16.054 -28.779 1.00 28.48 N ANISOU 2055 N ILE A 270 3270 3767 3783 -900 803 83 N ATOM 2056 CA ILE A 270 26.094 16.915 -27.595 1.00 26.72 C ANISOU 2056 CA ILE A 270 3049 3360 3743 -890 748 33 C ATOM 2057 C ILE A 270 26.569 18.343 -27.927 1.00 27.70 C ANISOU 2057 C ILE A 270 3114 3352 4060 -959 830 155 C ATOM 2058 O ILE A 270 25.975 19.308 -27.457 1.00 28.88 O ANISOU 2058 O ILE A 270 3275 3344 4355 -950 823 195 O ATOM 2059 CB ILE A 270 26.820 16.300 -26.353 1.00 25.21 C ANISOU 2059 CB ILE A 270 2828 3145 3604 -880 671 -174 C ATOM 2060 CG1 ILE A 270 26.285 16.915 -25.059 1.00 26.92 C ANISOU 2060 CG1 ILE A 270 3078 3236 3915 -866 598 -260 C ATOM 2061 CG2 ILE A 270 28.347 16.387 -26.469 1.00 25.93 C ANISOU 2061 CG2 ILE A 270 2809 3235 3807 -949 719 -226 C ATOM 2062 CD1 ILE A 270 26.908 16.379 -23.785 1.00 28.21 C ANISOU 2062 CD1 ILE A 270 3210 3418 4092 -873 503 -437 C ATOM 2063 N LYS A 271 27.601 18.444 -28.772 1.00 29.08 N ANISOU 2063 N LYS A 271 3216 3586 4247 -1029 921 215 N ATOM 2064 CA LYS A 271 28.093 19.708 -29.326 1.00 33.14 C ANISOU 2064 CA LYS A 271 3661 3997 4934 -1105 1017 374 C ATOM 2065 C LYS A 271 27.022 20.548 -30.036 1.00 35.80 C ANISOU 2065 C LYS A 271 4026 4295 5281 -1094 1045 630 C ATOM 2066 O LYS A 271 27.122 21.769 -30.044 1.00 40.06 O ANISOU 2066 O LYS A 271 4512 4657 6051 -1132 1098 752 O ATOM 2067 CB LYS A 271 29.250 19.441 -30.300 1.00 32.42 C ANISOU 2067 CB LYS A 271 3493 4035 4789 -1181 1124 414 C ATOM 2068 CG LYS A 271 30.541 19.022 -29.653 0.00 34.81 C ANISOU 2068 CG LYS A 271 3715 4319 5194 -1210 1119 214 C ATOM 2069 CD LYS A 271 31.600 18.700 -30.695 0.00 35.90 C ANISOU 2069 CD LYS A 271 3768 4591 5282 -1278 1246 250 C ATOM 2070 CE LYS A 271 32.895 18.238 -30.046 0.00 35.97 C ANISOU 2070 CE LYS A 271 3670 4575 5422 -1298 1236 61 C ATOM 2071 NZ LYS A 271 33.496 19.295 -29.187 0.00 36.64 N1+ ANISOU 2071 NZ LYS A 271 3684 4469 5767 -1353 1205 23 N1+ ATOM 2072 N LYS A 272 26.022 19.899 -30.637 1.00 40.78 N ANISOU 2072 N LYS A 272 4724 5087 5685 -1046 1008 719 N ATOM 2073 CA LYS A 272 24.876 20.595 -31.266 1.00 40.85 C ANISOU 2073 CA LYS A 272 4746 5083 5692 -1026 1005 982 C ATOM 2074 C LYS A 272 23.874 21.235 -30.288 1.00 38.25 C ANISOU 2074 C LYS A 272 4441 4534 5557 -951 945 964 C ATOM 2075 O LYS A 272 23.062 22.057 -30.708 1.00 39.54 O ANISOU 2075 O LYS A 272 4580 4620 5824 -932 956 1198 O ATOM 2076 CB LYS A 272 24.108 19.654 -32.219 1.00 40.40 C ANISOU 2076 CB LYS A 272 4741 5296 5313 -1013 972 1067 C ATOM 2077 CG LYS A 272 24.889 19.243 -33.462 1.00 48.41 C ANISOU 2077 CG LYS A 272 5722 6550 6123 -1107 1062 1136 C ATOM 2078 CD LYS A 272 23.987 18.612 -34.520 1.00 54.53 C ANISOU 2078 CD LYS A 272 6535 7599 6586 -1123 1035 1257 C ATOM 2079 CE LYS A 272 24.771 18.165 -35.750 1.00 52.19 C ANISOU 2079 CE LYS A 272 6204 7572 6055 -1235 1144 1282 C ATOM 2080 NZ LYS A 272 23.890 17.558 -36.782 0.00 54.92 N1+ ANISOU 2080 NZ LYS A 272 6582 8215 6069 -1275 1114 1373 N1+ ATOM 2081 N MET A 273 23.918 20.868 -29.006 1.00 34.09 N ANISOU 2081 N MET A 273 3950 3919 5085 -911 888 698 N ATOM 2082 CA MET A 273 22.968 21.402 -28.017 1.00 31.19 C ANISOU 2082 CA MET A 273 3606 3365 4879 -850 851 635 C ATOM 2083 C MET A 273 23.245 22.874 -27.714 1.00 30.12 C ANISOU 2083 C MET A 273 3393 2960 5092 -890 929 680 C ATOM 2084 O MET A 273 24.411 23.263 -27.615 1.00 26.70 O ANISOU 2084 O MET A 273 2903 2464 4780 -969 981 612 O ATOM 2085 CB MET A 273 23.032 20.607 -26.711 1.00 28.98 C ANISOU 2085 CB MET A 273 3380 3100 4533 -820 775 339 C ATOM 2086 CG MET A 273 22.702 19.135 -26.860 1.00 26.54 C ANISOU 2086 CG MET A 273 3137 3010 3939 -773 702 281 C ATOM 2087 SD MET A 273 21.068 18.832 -27.558 1.00 26.24 S ANISOU 2087 SD MET A 273 3149 3064 3757 -700 664 464 S ATOM 2088 CE MET A 273 20.078 19.421 -26.205 1.00 35.81 C ANISOU 2088 CE MET A 273 4382 4076 5148 -637 639 354 C ATOM 2089 N PRO A 274 22.187 23.699 -27.564 1.00 31.44 N ANISOU 2089 N PRO A 274 3542 2951 5451 -839 947 789 N ATOM 2090 CA PRO A 274 22.423 25.157 -27.410 1.00 33.49 C ANISOU 2090 CA PRO A 274 3707 2919 6098 -880 1045 853 C ATOM 2091 C PRO A 274 23.225 25.551 -26.169 1.00 31.29 C ANISOU 2091 C PRO A 274 3409 2478 6002 -941 1072 531 C ATOM 2092 O PRO A 274 24.038 26.498 -26.225 1.00 30.17 O ANISOU 2092 O PRO A 274 3179 2160 6123 -1022 1155 545 O ATOM 2093 CB PRO A 274 21.009 25.747 -27.343 1.00 33.33 C ANISOU 2093 CB PRO A 274 3669 2746 6249 -793 1052 990 C ATOM 2094 CG PRO A 274 20.141 24.732 -27.992 1.00 36.57 C ANISOU 2094 CG PRO A 274 4144 3414 6336 -727 960 1126 C ATOM 2095 CD PRO A 274 20.744 23.393 -27.659 1.00 30.76 C ANISOU 2095 CD PRO A 274 3499 2913 5277 -746 891 888 C ATOM 2096 N GLU A 275 23.016 24.799 -25.085 1.00 31.13 N ANISOU 2096 N GLU A 275 3461 2537 5830 -916 997 253 N ATOM 2097 CA GLU A 275 23.733 25.011 -23.823 1.00 33.12 C ANISOU 2097 CA GLU A 275 3698 2708 6177 -988 994 -72 C ATOM 2098 C GLU A 275 25.051 24.223 -23.693 1.00 31.08 C ANISOU 2098 C GLU A 275 3436 2632 5741 -1056 935 -196 C ATOM 2099 O GLU A 275 25.596 24.124 -22.585 1.00 31.89 O ANISOU 2099 O GLU A 275 3532 2744 5841 -1113 891 -461 O ATOM 2100 CB GLU A 275 22.815 24.694 -22.623 1.00 27.89 C ANISOU 2100 CB GLU A 275 3102 2051 5445 -941 949 -299 C ATOM 2101 CG GLU A 275 21.552 25.547 -22.551 1.00 32.20 C ANISOU 2101 CG GLU A 275 3627 2383 6224 -877 1026 -231 C ATOM 2102 CD GLU A 275 21.816 27.024 -22.292 1.00 36.62 C ANISOU 2102 CD GLU A 275 4084 2625 7205 -943 1154 -293 C ATOM 2103 OE1 GLU A 275 22.899 27.375 -21.783 1.00 42.13 O ANISOU 2103 OE1 GLU A 275 4741 3274 7992 -1054 1173 -490 O ATOM 2104 OE2 GLU A 275 20.928 27.851 -22.596 1.00 49.54 O1- ANISOU 2104 OE2 GLU A 275 5665 4045 9111 -886 1237 -144 O1- ATOM 2105 N HIS A 276 25.588 23.697 -24.798 1.00 24.80 N ANISOU 2105 N HIS A 276 2631 1985 4808 -1057 937 -10 N ATOM 2106 CA HIS A 276 26.809 22.901 -24.713 1.00 23.58 C ANISOU 2106 CA HIS A 276 2454 1989 4517 -1108 893 -122 C ATOM 2107 C HIS A 276 28.007 23.719 -24.241 1.00 23.31 C ANISOU 2107 C HIS A 276 2318 1822 4716 -1223 933 -253 C ATOM 2108 O HIS A 276 28.745 23.257 -23.386 1.00 23.85 O ANISOU 2108 O HIS A 276 2365 1968 4728 -1267 859 -462 O ATOM 2109 CB HIS A 276 27.151 22.197 -26.028 1.00 20.75 C ANISOU 2109 CB HIS A 276 2093 1813 3979 -1097 918 73 C ATOM 2110 CG HIS A 276 28.411 21.398 -25.955 1.00 19.28 C ANISOU 2110 CG HIS A 276 1860 1762 3705 -1141 893 -45 C ATOM 2111 CD2 HIS A 276 28.656 20.168 -25.448 1.00 17.41 C ANISOU 2111 CD2 HIS A 276 1645 1677 3291 -1106 803 -189 C ATOM 2112 ND1 HIS A 276 29.627 21.885 -26.394 1.00 19.88 N ANISOU 2112 ND1 HIS A 276 1833 1802 3919 -1231 969 -12 N ATOM 2113 CE1 HIS A 276 30.562 20.977 -26.180 1.00 19.94 C ANISOU 2113 CE1 HIS A 276 1798 1939 3837 -1245 927 -137 C ATOM 2114 NE2 HIS A 276 30.001 19.929 -25.600 1.00 20.43 N ANISOU 2114 NE2 HIS A 276 1934 2112 3719 -1168 824 -239 N ATOM 2115 N SER A 277 28.217 24.906 -24.792 1.00 24.54 N ANISOU 2115 N SER A 277 2400 1785 5138 -1277 1043 -118 N ATOM 2116 CA SER A 277 29.383 25.702 -24.387 1.00 31.50 C ANISOU 2116 CA SER A 277 3172 2530 6265 -1400 1089 -248 C ATOM 2117 C SER A 277 29.304 26.181 -22.927 1.00 30.48 C ANISOU 2117 C SER A 277 3036 2279 6267 -1453 1052 -563 C ATOM 2118 O SER A 277 30.337 26.336 -22.278 1.00 29.92 O ANISOU 2118 O SER A 277 2890 2208 6269 -1559 1024 -760 O ATOM 2119 CB SER A 277 29.646 26.850 -25.359 1.00 32.99 C ANISOU 2119 CB SER A 277 3272 2530 6732 -1452 1226 -8 C ATOM 2120 OG SER A 277 30.399 26.341 -26.453 1.00 36.90 O ANISOU 2120 OG SER A 277 3737 3197 7085 -1470 1258 177 O ATOM 2121 N THR A 278 28.087 26.366 -22.420 1.00 25.84 N ANISOU 2121 N THR A 278 2516 1612 5688 -1388 1051 -617 N ATOM 2122 CA THR A 278 27.857 26.609 -20.997 1.00 27.65 C ANISOU 2122 CA THR A 278 2759 1792 5957 -1436 1016 -942 C ATOM 2123 C THR A 278 28.270 25.407 -20.122 1.00 25.74 C ANISOU 2123 C THR A 278 2560 1826 5393 -1447 865 -1129 C ATOM 2124 O THR A 278 28.905 25.597 -19.078 1.00 28.04 O ANISOU 2124 O THR A 278 2805 2143 5706 -1556 817 -1391 O ATOM 2125 CB THR A 278 26.385 27.039 -20.744 1.00 29.56 C ANISOU 2125 CB THR A 278 3056 1891 6286 -1353 1072 -940 C ATOM 2126 CG2 THR A 278 26.050 27.137 -19.239 1.00 28.81 C ANISOU 2126 CG2 THR A 278 2986 1797 6164 -1405 1046 -1301 C ATOM 2127 OG1 THR A 278 26.180 28.326 -21.346 1.00 30.94 O ANISOU 2127 OG1 THR A 278 3149 1764 6843 -1366 1214 -795 O ATOM 2128 N LEU A 279 27.906 24.196 -20.550 1.00 22.61 N ANISOU 2128 N LEU A 279 2241 1635 4716 -1343 789 -989 N ATOM 2129 CA LEU A 279 28.344 22.931 -19.919 1.00 19.93 C ANISOU 2129 CA LEU A 279 1924 1548 4099 -1336 648 -1091 C ATOM 2130 C LEU A 279 29.845 22.769 -19.826 1.00 21.81 C ANISOU 2130 C LEU A 279 2055 1864 4368 -1430 600 -1153 C ATOM 2131 O LEU A 279 30.350 22.292 -18.826 1.00 28.64 O ANISOU 2131 O LEU A 279 2892 2868 5122 -1483 485 -1321 O ATOM 2132 CB LEU A 279 27.791 21.734 -20.688 1.00 18.28 C ANISOU 2132 CB LEU A 279 1791 1496 3658 -1211 610 -900 C ATOM 2133 CG LEU A 279 28.007 20.310 -20.155 1.00 17.05 C ANISOU 2133 CG LEU A 279 1659 1570 3248 -1174 477 -955 C ATOM 2134 CD1 LEU A 279 27.215 20.038 -18.896 1.00 19.21 C ANISOU 2134 CD1 LEU A 279 1998 1908 3392 -1163 400 -1111 C ATOM 2135 CD2 LEU A 279 27.627 19.308 -21.218 1.00 14.20 C ANISOU 2135 CD2 LEU A 279 1347 1312 2737 -1072 484 -765 C ATOM 2136 N MET A 280 30.559 23.170 -20.868 1.00 25.67 N ANISOU 2136 N MET A 280 2473 2276 5006 -1457 687 -1003 N ATOM 2137 CA MET A 280 32.011 23.109 -20.869 1.00 25.78 C ANISOU 2137 CA MET A 280 2364 2342 5091 -1549 662 -1052 C ATOM 2138 C MET A 280 32.607 24.136 -19.913 1.00 30.61 C ANISOU 2138 C MET A 280 2888 2836 5908 -1695 657 -1282 C ATOM 2139 O MET A 280 33.623 23.873 -19.264 1.00 36.01 O ANISOU 2139 O MET A 280 3480 3632 6572 -1781 562 -1419 O ATOM 2140 CB MET A 280 32.572 23.350 -22.268 1.00 27.10 C ANISOU 2140 CB MET A 280 2473 2456 5368 -1551 782 -829 C ATOM 2141 CG MET A 280 32.090 22.396 -23.341 1.00 26.23 C ANISOU 2141 CG MET A 280 2434 2480 5051 -1437 804 -622 C ATOM 2142 SD MET A 280 32.648 20.704 -23.119 1.00 28.00 S ANISOU 2142 SD MET A 280 2645 2956 5036 -1381 687 -680 S ATOM 2143 CE MET A 280 31.291 19.922 -22.271 1.00 24.60 C ANISOU 2143 CE MET A 280 2354 2609 4385 -1279 573 -748 C ATOM 2144 N LYS A 281 31.999 25.315 -19.845 1.00 33.83 N ANISOU 2144 N LYS A 281 3308 3014 6532 -1728 763 -1326 N ATOM 2145 CA LYS A 281 32.462 26.371 -18.942 1.00 35.07 C ANISOU 2145 CA LYS A 281 3381 3032 6914 -1879 783 -1586 C ATOM 2146 C LYS A 281 32.340 25.917 -17.489 1.00 38.07 C ANISOU 2146 C LYS A 281 3789 3590 7085 -1932 645 -1866 C ATOM 2147 O LYS A 281 33.252 26.128 -16.707 1.00 44.42 O ANISOU 2147 O LYS A 281 4498 4461 7920 -2072 574 -2074 O ATOM 2148 CB LYS A 281 31.656 27.649 -19.182 1.00 35.99 C ANISOU 2148 CB LYS A 281 3504 2839 7331 -1883 942 -1571 C ATOM 2149 CG LYS A 281 32.044 28.858 -18.347 1.00 40.30 C ANISOU 2149 CG LYS A 281 3956 3185 8172 -2045 1003 -1860 C ATOM 2150 CD LYS A 281 31.107 30.030 -18.619 1.00 45.00 C ANISOU 2150 CD LYS A 281 4552 3446 9101 -2020 1174 -1823 C ATOM 2151 CE LYS A 281 29.778 29.895 -17.885 1.00 49.08 C ANISOU 2151 CE LYS A 281 5175 3970 9504 -1946 1172 -1960 C ATOM 2152 NZ LYS A 281 28.665 30.618 -18.565 1.00 53.60 N1+ ANISOU 2152 NZ LYS A 281 5761 4268 10336 -1841 1318 -1763 N1+ ATOM 2153 N ASP A 282 31.229 25.261 -17.153 1.00 39.68 N ANISOU 2153 N ASP A 282 4117 3897 7064 -1827 601 -1856 N ATOM 2154 CA ASP A 282 30.895 24.962 -15.758 1.00 40.90 C ANISOU 2154 CA ASP A 282 4308 4214 7017 -1881 498 -2110 C ATOM 2155 C ASP A 282 31.407 23.613 -15.270 1.00 37.66 C ANISOU 2155 C ASP A 282 3894 4119 6297 -1864 312 -2081 C ATOM 2156 O ASP A 282 31.520 23.438 -14.071 1.00 38.91 O ANISOU 2156 O ASP A 282 4039 4449 6296 -1956 204 -2283 O ATOM 2157 CB ASP A 282 29.363 25.033 -15.530 1.00 36.86 C ANISOU 2157 CB ASP A 282 3920 3639 6446 -1788 563 -2128 C ATOM 2158 CG ASP A 282 28.782 26.457 -15.693 1.00 38.22 C ANISOU 2158 CG ASP A 282 4072 3483 6965 -1818 745 -2211 C ATOM 2159 OD1 ASP A 282 29.509 27.459 -15.542 1.00 47.12 O ANISOU 2159 OD1 ASP A 282 5098 4450 8356 -1951 811 -2362 O ATOM 2160 OD2 ASP A 282 27.572 26.578 -15.966 1.00 39.15 O1- ANISOU 2160 OD2 ASP A 282 4265 3491 7119 -1708 826 -2121 O1- ATOM 2161 N PHE A 283 31.693 22.669 -16.171 1.00 33.36 N ANISOU 2161 N PHE A 283 3350 3652 5672 -1754 280 -1833 N ATOM 2162 CA PHE A 283 31.998 21.279 -15.775 1.00 36.87 C ANISOU 2162 CA PHE A 283 3789 4359 5861 -1705 118 -1770 C ATOM 2163 C PHE A 283 33.290 20.691 -16.354 1.00 33.53 C ANISOU 2163 C PHE A 283 3243 4009 5490 -1707 68 -1647 C ATOM 2164 O PHE A 283 33.646 20.944 -17.500 1.00 32.57 O ANISOU 2164 O PHE A 283 3089 3762 5524 -1677 180 -1512 O ATOM 2165 CB PHE A 283 30.874 20.337 -16.219 1.00 34.45 C ANISOU 2165 CB PHE A 283 3610 4099 5380 -1541 125 -1601 C ATOM 2166 CG PHE A 283 29.577 20.519 -15.490 1.00 34.14 C ANISOU 2166 CG PHE A 283 3684 4057 5232 -1520 141 -1706 C ATOM 2167 CD1 PHE A 283 29.315 19.805 -14.328 1.00 30.57 C ANISOU 2167 CD1 PHE A 283 3258 3817 4540 -1539 13 -1797 C ATOM 2168 CD2 PHE A 283 28.582 21.349 -16.005 1.00 37.85 C ANISOU 2168 CD2 PHE A 283 4223 4318 5840 -1474 286 -1685 C ATOM 2169 CE1 PHE A 283 28.096 19.935 -13.677 1.00 35.02 C ANISOU 2169 CE1 PHE A 283 3923 4391 4995 -1521 45 -1893 C ATOM 2170 CE2 PHE A 283 27.361 21.485 -15.357 1.00 35.66 C ANISOU 2170 CE2 PHE A 283 4036 4031 5484 -1446 315 -1781 C ATOM 2171 CZ PHE A 283 27.121 20.777 -14.192 1.00 36.21 C ANISOU 2171 CZ PHE A 283 4137 4318 5303 -1472 201 -1898 C ATOM 2172 N ARG A 284 33.931 19.833 -15.569 1.00 34.28 N ANISOU 2172 N ARG A 284 3263 4320 5444 -1735 -98 -1673 N ATOM 2173 CA ARG A 284 35.099 19.082 -16.008 1.00 38.15 C ANISOU 2173 CA ARG A 284 3618 4892 5987 -1716 -156 -1550 C ATOM 2174 C ARG A 284 34.839 17.586 -15.881 1.00 31.69 C ANISOU 2174 C ARG A 284 2822 4237 4983 -1593 -260 -1410 C ATOM 2175 O ARG A 284 34.412 17.115 -14.832 1.00 29.62 O ANISOU 2175 O ARG A 284 2592 4128 4534 -1602 -388 -1454 O ATOM 2176 CB ARG A 284 36.326 19.483 -15.177 1.00 45.07 C ANISOU 2176 CB ARG A 284 4327 5860 6939 -1878 -272 -1691 C ATOM 2177 CG ARG A 284 36.833 20.885 -15.474 1.00 53.67 C ANISOU 2177 CG ARG A 284 5355 6760 8277 -2006 -155 -1815 C ATOM 2178 CD ARG A 284 37.925 21.334 -14.505 1.00 72.57 C ANISOU 2178 CD ARG A 284 7585 9261 10726 -2191 -283 -1999 C ATOM 2179 NE ARG A 284 38.981 20.327 -14.325 1.00 96.77 N ANISOU 2179 NE ARG A 284 10495 12521 13754 -2181 -439 -1890 N ATOM 2180 CZ ARG A 284 39.952 20.033 -15.202 1.00111.28 C ANISOU 2180 CZ ARG A 284 12202 14310 15769 -2145 -394 -1750 C ATOM 2181 NH1 ARG A 284 40.051 20.663 -16.379 1.00 82.24 N1+ ANISOU 2181 NH1 ARG A 284 8536 10417 12295 -2124 -196 -1688 N1+ ATOM 2182 NH2 ARG A 284 40.847 19.084 -14.899 1.00120.98 N ANISOU 2182 NH2 ARG A 284 13272 15714 16980 -2131 -545 -1658 N ATOM 2183 N ARG A 285 35.119 16.856 -16.956 1.00 32.37 N ANISOU 2183 N ARG A 285 2880 4289 5132 -1488 -194 -1248 N ATOM 2184 CA ARG A 285 35.059 15.392 -16.989 1.00 39.01 C ANISOU 2184 CA ARG A 285 3704 5242 5874 -1371 -268 -1116 C ATOM 2185 C ARG A 285 35.624 14.711 -15.740 1.00 40.85 C ANISOU 2185 C ARG A 285 3824 5667 6029 -1412 -476 -1121 C ATOM 2186 O ARG A 285 34.984 13.805 -15.166 1.00 38.29 O ANISOU 2186 O ARG A 285 3551 5450 5546 -1345 -569 -1053 O ATOM 2187 CB ARG A 285 35.813 14.878 -18.231 1.00 47.58 C ANISOU 2187 CB ARG A 285 4700 6269 7110 -1308 -162 -1004 C ATOM 2188 CG ARG A 285 36.070 13.365 -18.266 1.00 54.28 C ANISOU 2188 CG ARG A 285 5472 7204 7947 -1202 -227 -894 C ATOM 2189 CD ARG A 285 36.639 12.867 -19.595 1.00 55.74 C ANISOU 2189 CD ARG A 285 5586 7321 8272 -1139 -76 -825 C ATOM 2190 NE ARG A 285 35.973 13.476 -20.747 1.00 61.94 N ANISOU 2190 NE ARG A 285 6502 8009 9025 -1128 104 -817 N ATOM 2191 CZ ARG A 285 34.731 13.209 -21.156 1.00 64.54 C ANISOU 2191 CZ ARG A 285 6992 8324 9205 -1054 156 -783 C ATOM 2192 NH1 ARG A 285 33.969 12.306 -20.521 1.00 53.09 N1+ ANISOU 2192 NH1 ARG A 285 5604 6935 7632 -979 56 -764 N1+ ATOM 2193 NH2 ARG A 285 34.242 13.855 -22.217 1.00 57.92 N ANISOU 2193 NH2 ARG A 285 6244 7418 8344 -1060 305 -750 N ATOM 2194 N ASN A 286 36.828 15.140 -15.350 1.00 40.56 N ANISOU 2194 N ASN A 286 3623 5680 6110 -1527 -551 -1180 N ATOM 2195 CA ASN A 286 37.584 14.491 -14.269 1.00 45.36 C ANISOU 2195 CA ASN A 286 4076 6492 6668 -1576 -765 -1145 C ATOM 2196 C ASN A 286 36.911 14.497 -12.890 1.00 37.22 C ANISOU 2196 C ASN A 286 3114 5647 5382 -1646 -916 -1217 C ATOM 2197 O ASN A 286 37.222 13.663 -12.041 1.00 39.05 O ANISOU 2197 O ASN A 286 3248 6075 5515 -1651 -1099 -1116 O ATOM 2198 CB ASN A 286 39.021 15.047 -14.182 1.00 61.15 C ANISOU 2198 CB ASN A 286 5869 8510 8854 -1701 -815 -1202 C ATOM 2199 CG ASN A 286 39.936 14.433 -15.235 1.00 72.60 C ANISOU 2199 CG ASN A 286 7177 9873 10535 -1614 -732 -1068 C ATOM 2200 ND2 ASN A 286 40.769 13.477 -14.821 1.00 66.65 N ANISOU 2200 ND2 ASN A 286 6234 9242 9850 -1586 -878 -946 N ATOM 2201 OD1 ASN A 286 39.870 14.790 -16.415 1.00 73.11 O ANISOU 2201 OD1 ASN A 286 7294 9768 10716 -1573 -534 -1066 O ATOM 2202 N THR A 287 35.984 15.415 -12.674 1.00 32.69 N ANISOU 2202 N THR A 287 2697 5015 4708 -1700 -834 -1377 N ATOM 2203 CA THR A 287 35.189 15.424 -11.456 1.00 35.21 C ANISOU 2203 CA THR A 287 3102 5507 4770 -1762 -934 -1466 C ATOM 2204 C THR A 287 34.407 14.114 -11.255 1.00 33.81 C ANISOU 2204 C THR A 287 2991 5427 4429 -1627 -996 -1278 C ATOM 2205 O THR A 287 34.257 13.659 -10.121 1.00 29.80 O ANISOU 2205 O THR A 287 2463 5147 3712 -1680 -1151 -1255 O ATOM 2206 CB THR A 287 34.213 16.610 -11.478 1.00 39.28 C ANISOU 2206 CB THR A 287 3774 5881 5267 -1812 -782 -1671 C ATOM 2207 CG2 THR A 287 33.637 16.891 -10.082 1.00 43.23 C ANISOU 2207 CG2 THR A 287 4327 6581 5517 -1934 -870 -1845 C ATOM 2208 OG1 THR A 287 34.909 17.767 -11.960 1.00 42.63 O ANISOU 2208 OG1 THR A 287 4135 6143 5920 -1907 -685 -1802 O ATOM 2209 N TYR A 288 33.937 13.511 -12.350 1.00 28.99 N ANISOU 2209 N TYR A 288 2448 4655 3912 -1466 -874 -1144 N ATOM 2210 CA TYR A 288 33.044 12.340 -12.288 1.00 28.98 C ANISOU 2210 CA TYR A 288 2525 4697 3790 -1337 -898 -989 C ATOM 2211 C TYR A 288 33.728 11.020 -12.723 1.00 31.29 C ANISOU 2211 C TYR A 288 2682 4991 4217 -1227 -952 -778 C ATOM 2212 O TYR A 288 33.067 10.113 -13.244 1.00 25.14 O ANISOU 2212 O TYR A 288 1963 4142 3446 -1097 -895 -664 O ATOM 2213 CB TYR A 288 31.782 12.633 -13.132 1.00 27.14 C ANISOU 2213 CB TYR A 288 2478 4288 3546 -1248 -717 -1022 C ATOM 2214 CG TYR A 288 31.180 13.990 -12.817 1.00 25.99 C ANISOU 2214 CG TYR A 288 2435 4088 3351 -1345 -637 -1226 C ATOM 2215 CD1 TYR A 288 30.387 14.171 -11.689 1.00 28.09 C ANISOU 2215 CD1 TYR A 288 2777 4485 3410 -1407 -689 -1326 C ATOM 2216 CD2 TYR A 288 31.429 15.099 -13.624 1.00 26.24 C ANISOU 2216 CD2 TYR A 288 2474 3935 3563 -1381 -500 -1317 C ATOM 2217 CE1 TYR A 288 29.854 15.413 -11.374 1.00 27.75 C ANISOU 2217 CE1 TYR A 288 2811 4374 3360 -1497 -596 -1542 C ATOM 2218 CE2 TYR A 288 30.902 16.350 -13.313 1.00 25.58 C ANISOU 2218 CE2 TYR A 288 2461 3767 3491 -1467 -417 -1503 C ATOM 2219 CZ TYR A 288 30.117 16.504 -12.186 1.00 28.50 C ANISOU 2219 CZ TYR A 288 2902 4253 3674 -1523 -460 -1630 C ATOM 2220 OH TYR A 288 29.592 17.738 -11.846 1.00 27.79 O ANISOU 2220 OH TYR A 288 2868 4063 3629 -1611 -358 -1845 O ATOM 2221 N THR A 289 35.042 10.906 -12.488 1.00 37.40 N ANISOU 2221 N THR A 289 3258 5837 5115 -1282 -1060 -734 N ATOM 2222 CA THR A 289 35.846 9.786 -13.021 1.00 33.96 C ANISOU 2222 CA THR A 289 2659 5357 4887 -1177 -1080 -556 C ATOM 2223 C THR A 289 35.534 8.411 -12.414 1.00 30.06 C ANISOU 2223 C THR A 289 2117 4961 4344 -1088 -1204 -348 C ATOM 2224 O THR A 289 35.602 7.418 -13.118 1.00 28.36 O ANISOU 2224 O THR A 289 1848 4626 4301 -959 -1139 -230 O ATOM 2225 CB THR A 289 37.361 10.026 -12.843 1.00 43.74 C ANISOU 2225 CB THR A 289 3669 6654 6297 -1262 -1174 -549 C ATOM 2226 CG2 THR A 289 38.177 9.162 -13.822 1.00 44.77 C ANISOU 2226 CG2 THR A 289 3642 6651 6716 -1145 -1096 -427 C ATOM 2227 OG1 THR A 289 37.662 11.402 -13.069 1.00 44.47 O ANISOU 2227 OG1 THR A 289 3792 6691 6413 -1383 -1096 -745 O ATOM 2228 N ASN A 290 35.241 8.349 -11.115 1.00 32.18 N ANISOU 2228 N ASN A 290 2389 5447 4390 -1166 -1377 -305 N ATOM 2229 CA ASN A 290 34.854 7.082 -10.459 1.00 37.29 C ANISOU 2229 CA ASN A 290 2994 6198 4976 -1091 -1498 -76 C ATOM 2230 C ASN A 290 33.331 6.990 -10.256 1.00 38.40 C ANISOU 2230 C ASN A 290 3354 6341 4895 -1057 -1431 -105 C ATOM 2231 O ASN A 290 32.869 6.417 -9.262 1.00 45.83 O ANISOU 2231 O ASN A 290 4296 7458 5661 -1074 -1557 29 O ATOM 2232 CB ASN A 290 35.612 6.897 -9.119 1.00 41.31 C ANISOU 2232 CB ASN A 290 3328 6991 5378 -1203 -1755 57 C ATOM 2233 CG ASN A 290 37.124 6.676 -9.305 1.00 48.47 C ANISOU 2233 CG ASN A 290 3972 7892 6554 -1207 -1844 156 C ATOM 2234 ND2 ASN A 290 37.495 5.690 -10.130 1.00 40.11 N ANISOU 2234 ND2 ASN A 290 2800 6642 5800 -1054 -1771 303 N ATOM 2235 OD1 ASN A 290 37.948 7.380 -8.699 1.00 49.63 O ANISOU 2235 OD1 ASN A 290 4007 8205 6644 -1354 -1973 88 O ATOM 2236 N CYS A 291 32.569 7.538 -11.215 1.00 33.64 N ANISOU 2236 N CYS A 291 2921 5552 4308 -1011 -1233 -260 N ATOM 2237 CA CYS A 291 31.095 7.588 -11.178 1.00 28.35 C ANISOU 2237 CA CYS A 291 2454 4856 3461 -977 -1146 -310 C ATOM 2238 C CYS A 291 30.516 6.864 -12.384 1.00 28.62 C ANISOU 2238 C CYS A 291 2550 4683 3643 -829 -997 -257 C ATOM 2239 O CYS A 291 30.903 7.162 -13.524 1.00 25.10 O ANISOU 2239 O CYS A 291 2097 4081 3360 -795 -869 -329 O ATOM 2240 CB CYS A 291 30.576 9.035 -11.215 1.00 25.54 C ANISOU 2240 CB CYS A 291 2242 4471 2990 -1068 -1046 -551 C ATOM 2241 SG CYS A 291 31.119 10.122 -9.884 1.00 24.25 S ANISOU 2241 SG CYS A 291 2031 4534 2647 -1274 -1175 -715 S ATOM 2242 N SER A 292 29.576 5.951 -12.123 1.00 24.53 N ANISOU 2242 N SER A 292 2090 4177 3053 -757 -1009 -142 N ATOM 2243 CA SER A 292 28.896 5.166 -13.166 1.00 23.72 C ANISOU 2243 CA SER A 292 2045 3898 3069 -632 -877 -106 C ATOM 2244 C SER A 292 27.575 4.573 -12.640 1.00 19.73 C ANISOU 2244 C SER A 292 1646 3435 2414 -595 -888 -31 C ATOM 2245 O SER A 292 27.422 4.348 -11.431 1.00 19.93 O ANISOU 2245 O SER A 292 1649 3633 2290 -644 -1018 69 O ATOM 2246 CB SER A 292 29.792 4.019 -13.625 1.00 22.70 C ANISOU 2246 CB SER A 292 1738 3680 3206 -548 -890 29 C ATOM 2247 OG SER A 292 29.874 3.029 -12.613 1.00 24.75 O ANISOU 2247 OG SER A 292 1889 4040 3473 -530 -1041 240 O ATOM 2248 N LEU A 293 26.630 4.325 -13.540 1.00 17.16 N ANISOU 2248 N LEU A 293 1429 2972 2118 -520 -754 -74 N ATOM 2249 CA LEU A 293 25.362 3.691 -13.140 1.00 19.27 C ANISOU 2249 CA LEU A 293 1784 3261 2278 -481 -753 -1 C ATOM 2250 C LEU A 293 25.582 2.375 -12.384 1.00 23.43 C ANISOU 2250 C LEU A 293 2185 3839 2878 -443 -869 223 C ATOM 2251 O LEU A 293 24.857 2.087 -11.423 1.00 27.46 O ANISOU 2251 O LEU A 293 2732 4470 3231 -465 -936 322 O ATOM 2252 CB LEU A 293 24.449 3.451 -14.341 1.00 17.30 C ANISOU 2252 CB LEU A 293 1631 2853 2089 -406 -604 -68 C ATOM 2253 CG LEU A 293 23.002 3.020 -14.020 1.00 19.94 C ANISOU 2253 CG LEU A 293 2069 3200 2308 -377 -585 -27 C ATOM 2254 CD1 LEU A 293 22.276 3.986 -13.078 1.00 20.74 C ANISOU 2254 CD1 LEU A 293 2275 3432 2173 -450 -608 -89 C ATOM 2255 CD2 LEU A 293 22.200 2.855 -15.303 1.00 17.14 C ANISOU 2255 CD2 LEU A 293 1791 2707 2013 -320 -450 -105 C ATOM 2256 N ILE A 294 26.595 1.608 -12.793 1.00 19.41 N ANISOU 2256 N ILE A 294 1515 3240 2620 -390 -888 313 N ATOM 2257 CA ILE A 294 26.981 0.383 -12.089 1.00 25.27 C ANISOU 2257 CA ILE A 294 2096 4007 3498 -349 -1005 560 C ATOM 2258 C ILE A 294 27.222 0.631 -10.594 1.00 28.89 C ANISOU 2258 C ILE A 294 2508 4724 3745 -444 -1192 700 C ATOM 2259 O ILE A 294 26.637 -0.055 -9.747 1.00 27.59 O ANISOU 2259 O ILE A 294 2333 4653 3495 -443 -1270 885 O ATOM 2260 CB ILE A 294 28.231 -0.282 -12.729 1.00 25.35 C ANISOU 2260 CB ILE A 294 1909 3876 3847 -285 -992 616 C ATOM 2261 CG1 ILE A 294 27.849 -0.917 -14.082 1.00 23.03 C ANISOU 2261 CG1 ILE A 294 1642 3347 3762 -195 -804 505 C ATOM 2262 CG2 ILE A 294 28.848 -1.339 -11.801 1.00 27.15 C ANISOU 2262 CG2 ILE A 294 1929 4153 4232 -257 -1150 909 C ATOM 2263 CD1 ILE A 294 29.031 -1.392 -14.908 1.00 19.99 C ANISOU 2263 CD1 ILE A 294 1081 2812 3703 -142 -734 478 C ATOM 2264 N LYS A 295 28.073 1.607 -10.280 1.00 31.24 N ANISOU 2264 N LYS A 295 2772 5148 3951 -537 -1262 609 N ATOM 2265 CA LYS A 295 28.463 1.867 -8.889 1.00 30.14 C ANISOU 2265 CA LYS A 295 2565 5288 3597 -652 -1451 717 C ATOM 2266 C LYS A 295 27.329 2.474 -8.085 1.00 28.43 C ANISOU 2266 C LYS A 295 2519 5244 3037 -739 -1445 629 C ATOM 2267 O LYS A 295 27.158 2.129 -6.917 1.00 31.67 O ANISOU 2267 O LYS A 295 2892 5884 3257 -805 -1577 793 O ATOM 2268 CB LYS A 295 29.722 2.727 -8.805 1.00 34.98 C ANISOU 2268 CB LYS A 295 3078 5986 4227 -742 -1526 621 C ATOM 2269 CG LYS A 295 30.933 2.018 -9.388 1.00 46.16 C ANISOU 2269 CG LYS A 295 4281 7267 5991 -662 -1552 748 C ATOM 2270 CD LYS A 295 32.235 2.771 -9.163 1.00 55.28 C ANISOU 2270 CD LYS A 295 5301 8531 7172 -758 -1653 691 C ATOM 2271 CE LYS A 295 33.413 1.992 -9.734 1.00 59.36 C ANISOU 2271 CE LYS A 295 5584 8904 8066 -668 -1667 830 C ATOM 2272 NZ LYS A 295 34.725 2.606 -9.392 1.00 62.23 N1+ ANISOU 2272 NZ LYS A 295 5779 9395 8470 -765 -1793 817 N1+ ATOM 2273 N TYR A 296 26.538 3.355 -8.693 1.00 25.79 N ANISOU 2273 N TYR A 296 2363 4810 2627 -742 -1289 385 N ATOM 2274 CA TYR A 296 25.310 3.821 -8.023 1.00 24.93 C ANISOU 2274 CA TYR A 296 2409 4821 2243 -802 -1248 297 C ATOM 2275 C TYR A 296 24.389 2.649 -7.616 1.00 25.24 C ANISOU 2275 C TYR A 296 2457 4882 2250 -740 -1262 512 C ATOM 2276 O TYR A 296 24.036 2.520 -6.441 1.00 30.26 O ANISOU 2276 O TYR A 296 3094 5753 2650 -821 -1350 611 O ATOM 2277 CB TYR A 296 24.515 4.813 -8.884 1.00 21.78 C ANISOU 2277 CB TYR A 296 2175 4259 1840 -784 -1066 44 C ATOM 2278 CG TYR A 296 23.269 5.280 -8.175 1.00 21.50 C ANISOU 2278 CG TYR A 296 2274 4332 1562 -838 -1012 -50 C ATOM 2279 CD1 TYR A 296 23.347 6.222 -7.131 1.00 22.51 C ANISOU 2279 CD1 TYR A 296 2426 4672 1455 -984 -1053 -195 C ATOM 2280 CD2 TYR A 296 22.030 4.742 -8.487 1.00 20.72 C ANISOU 2280 CD2 TYR A 296 2264 4139 1471 -755 -919 -2 C ATOM 2281 CE1 TYR A 296 22.218 6.631 -6.449 1.00 23.30 C ANISOU 2281 CE1 TYR A 296 2636 4875 1342 -1039 -983 -300 C ATOM 2282 CE2 TYR A 296 20.881 5.143 -7.812 1.00 22.04 C ANISOU 2282 CE2 TYR A 296 2537 4404 1431 -802 -859 -84 C ATOM 2283 CZ TYR A 296 20.974 6.085 -6.797 1.00 26.87 C ANISOU 2283 CZ TYR A 296 3172 5218 1819 -941 -883 -235 C ATOM 2284 OH TYR A 296 19.831 6.478 -6.127 1.00 33.04 O ANISOU 2284 OH TYR A 296 4049 6096 2408 -990 -799 -339 O ATOM 2285 N MET A 297 24.027 1.798 -8.576 1.00 23.43 N ANISOU 2285 N MET A 297 2226 4420 2255 -611 -1172 580 N ATOM 2286 CA MET A 297 23.044 0.729 -8.319 1.00 25.39 C ANISOU 2286 CA MET A 297 2490 4645 2512 -552 -1157 756 C ATOM 2287 C MET A 297 23.532 -0.361 -7.364 1.00 28.21 C ANISOU 2287 C MET A 297 2684 5131 2903 -557 -1318 1080 C ATOM 2288 O MET A 297 22.718 -0.945 -6.657 1.00 24.95 O ANISOU 2288 O MET A 297 2290 4811 2378 -567 -1339 1238 O ATOM 2289 CB MET A 297 22.554 0.101 -9.621 1.00 23.65 C ANISOU 2289 CB MET A 297 2299 4144 2544 -430 -1018 716 C ATOM 2290 CG MET A 297 21.811 1.071 -10.527 1.00 25.11 C ANISOU 2290 CG MET A 297 2645 4228 2669 -424 -868 456 C ATOM 2291 SD MET A 297 20.347 1.830 -9.803 1.00 32.70 S ANISOU 2291 SD MET A 297 3771 5320 3333 -486 -814 357 S ATOM 2292 CE MET A 297 19.326 0.391 -9.507 1.00 35.74 C ANISOU 2292 CE MET A 297 4135 5672 3771 -425 -811 574 C ATOM 2293 N GLU A 298 24.843 -0.612 -7.333 1.00 35.62 N ANISOU 2293 N GLU A 298 3452 6080 4004 -553 -1430 1193 N ATOM 2294 CA GLU A 298 25.447 -1.558 -6.378 1.00 36.94 C ANISOU 2294 CA GLU A 298 3430 6388 4217 -565 -1609 1538 C ATOM 2295 C GLU A 298 25.336 -1.085 -4.933 1.00 44.67 C ANISOU 2295 C GLU A 298 4425 7745 4803 -717 -1752 1617 C ATOM 2296 O GLU A 298 25.208 -1.911 -4.025 1.00 48.61 O ANISOU 2296 O GLU A 298 4831 8400 5239 -737 -1870 1925 O ATOM 2297 CB GLU A 298 26.929 -1.783 -6.677 1.00 46.11 C ANISOU 2297 CB GLU A 298 4389 7485 5646 -532 -1699 1624 C ATOM 2298 CG GLU A 298 27.225 -2.798 -7.764 1.00 50.38 C ANISOU 2298 CG GLU A 298 4820 7692 6630 -381 -1600 1684 C ATOM 2299 CD GLU A 298 28.724 -2.995 -7.988 1.00 50.71 C ANISOU 2299 CD GLU A 298 4639 7679 6951 -351 -1682 1770 C ATOM 2300 OE1 GLU A 298 29.495 -2.013 -7.823 1.00 39.28 O ANISOU 2300 OE1 GLU A 298 3179 6377 5369 -440 -1749 1645 O ATOM 2301 OE2 GLU A 298 29.125 -4.137 -8.333 1.00 46.44 O1- ANISOU 2301 OE2 GLU A 298 3922 6934 6787 -240 -1669 1954 O1- ATOM 2302 N LYS A 299 25.422 0.227 -4.717 1.00 43.10 N ANISOU 2302 N LYS A 299 4329 7696 4350 -834 -1740 1343 N ATOM 2303 CA LYS A 299 25.209 0.810 -3.381 1.00 50.42 C ANISOU 2303 CA LYS A 299 5294 8997 4866 -1004 -1841 1332 C ATOM 2304 C LYS A 299 23.759 0.662 -2.883 1.00 45.34 C ANISOU 2304 C LYS A 299 4795 8435 3999 -1023 -1747 1335 C ATOM 2305 O LYS A 299 23.516 0.708 -1.684 1.00 48.48 O ANISOU 2305 O LYS A 299 5188 9158 4073 -1152 -1836 1427 O ATOM 2306 CB LYS A 299 25.615 2.290 -3.362 1.00 55.95 C ANISOU 2306 CB LYS A 299 6069 9790 5401 -1125 -1816 985 C ATOM 2307 CG LYS A 299 27.108 2.519 -3.504 1.00 60.87 C ANISOU 2307 CG LYS A 299 6528 10434 6167 -1156 -1944 1000 C ATOM 2308 CD LYS A 299 27.442 3.983 -3.727 1.00 60.56 C ANISOU 2308 CD LYS A 299 6567 10399 6043 -1258 -1878 633 C ATOM 2309 CE LYS A 299 28.935 4.225 -3.556 1.00 67.24 C ANISOU 2309 CE LYS A 299 7229 11351 6967 -1332 -2039 665 C ATOM 2310 NZ LYS A 299 29.365 5.472 -4.240 1.00 77.26 N1+ ANISOU 2310 NZ LYS A 299 8554 12481 8319 -1376 -1934 334 N1+ ATOM 2311 N HIS A 300 22.815 0.508 -3.811 1.00 35.14 N ANISOU 2311 N HIS A 300 3619 6864 2868 -907 -1568 1229 N ATOM 2312 CA HIS A 300 21.418 0.244 -3.499 1.00 36.96 C ANISOU 2312 CA HIS A 300 3965 7120 2959 -901 -1467 1248 C ATOM 2313 C HIS A 300 21.043 -1.221 -3.713 1.00 37.31 C ANISOU 2313 C HIS A 300 3929 7006 3242 -784 -1470 1556 C ATOM 2314 O HIS A 300 19.884 -1.543 -3.918 1.00 38.06 O ANISOU 2314 O HIS A 300 4113 6998 3348 -737 -1350 1545 O ATOM 2315 CB HIS A 300 20.533 1.213 -4.299 1.00 35.36 C ANISOU 2315 CB HIS A 300 3942 6743 2751 -873 -1270 905 C ATOM 2316 CG HIS A 300 20.767 2.645 -3.930 1.00 43.19 C ANISOU 2316 CG HIS A 300 5005 7883 3521 -1000 -1251 611 C ATOM 2317 CD2 HIS A 300 21.489 3.619 -4.532 1.00 48.48 C ANISOU 2317 CD2 HIS A 300 5686 8456 4279 -1016 -1226 384 C ATOM 2318 ND1 HIS A 300 20.291 3.195 -2.758 1.00 52.08 N ANISOU 2318 ND1 HIS A 300 6184 9302 4301 -1145 -1255 524 N ATOM 2319 CE1 HIS A 300 20.683 4.454 -2.670 1.00 51.67 C ANISOU 2319 CE1 HIS A 300 6174 9307 4150 -1243 -1226 232 C ATOM 2320 NE2 HIS A 300 21.411 4.737 -3.734 1.00 47.53 N ANISOU 2320 NE2 HIS A 300 5624 8542 3893 -1165 -1212 155 N ATOM 2321 N LYS A 301 22.041 -2.102 -3.630 1.00 50.48 N ANISOU 2321 N LYS A 301 5409 8650 5120 -742 -1608 1834 N ATOM 2322 CA LYS A 301 21.867 -3.562 -3.596 1.00 48.82 C ANISOU 2322 CA LYS A 301 5073 8312 5163 -649 -1638 2179 C ATOM 2323 C LYS A 301 21.058 -4.138 -4.769 1.00 42.10 C ANISOU 2323 C LYS A 301 4285 7099 4612 -514 -1460 2086 C ATOM 2324 O LYS A 301 20.200 -5.006 -4.595 1.00 47.65 O ANISOU 2324 O LYS A 301 4983 7737 5385 -478 -1417 2259 O ATOM 2325 CB LYS A 301 21.329 -3.990 -2.219 1.00 47.98 C ANISOU 2325 CB LYS A 301 4942 8516 4774 -747 -1733 2461 C ATOM 2326 CG LYS A 301 22.257 -3.603 -1.063 1.00 47.75 C ANISOU 2326 CG LYS A 301 4811 8876 4457 -893 -1939 2597 C ATOM 2327 CD LYS A 301 21.750 -4.180 0.237 0.00 54.51 C ANISOU 2327 CD LYS A 301 5621 10050 5040 -991 -2034 2925 C ATOM 2328 CE LYS A 301 22.642 -3.774 1.400 0.00 57.43 C ANISOU 2328 CE LYS A 301 5888 10859 5074 -1161 -2250 3054 C ATOM 2329 NZ LYS A 301 22.566 -2.315 1.688 0.00 56.90 N1+ ANISOU 2329 NZ LYS A 301 5975 11018 4627 -1310 -2204 2635 N1+ ATOM 2330 N VAL A 302 21.368 -3.633 -5.962 1.00 40.87 N ANISOU 2330 N VAL A 302 4180 6725 4623 -452 -1359 1813 N ATOM 2331 CA VAL A 302 20.840 -4.123 -7.240 1.00 37.31 C ANISOU 2331 CA VAL A 302 3769 5948 4459 -338 -1201 1690 C ATOM 2332 C VAL A 302 22.046 -4.581 -8.046 1.00 39.43 C ANISOU 2332 C VAL A 302 3887 6015 5080 -259 -1214 1706 C ATOM 2333 O VAL A 302 23.014 -3.830 -8.187 1.00 39.59 O ANISOU 2333 O VAL A 302 3881 6097 5066 -290 -1259 1595 O ATOM 2334 CB VAL A 302 20.120 -3.002 -8.003 1.00 38.17 C ANISOU 2334 CB VAL A 302 4072 6010 4420 -351 -1060 1340 C ATOM 2335 CG1 VAL A 302 19.668 -3.460 -9.387 1.00 32.87 C ANISOU 2335 CG1 VAL A 302 3431 5045 4013 -253 -914 1206 C ATOM 2336 CG2 VAL A 302 18.924 -2.513 -7.201 1.00 40.71 C ANISOU 2336 CG2 VAL A 302 4527 6516 4425 -426 -1029 1304 C ATOM 2337 N LYS A 303 21.984 -5.802 -8.575 1.00 38.53 N ANISOU 2337 N LYS A 303 3665 5654 5321 -161 -1160 1829 N ATOM 2338 CA LYS A 303 23.154 -6.447 -9.180 1.00 38.71 C ANISOU 2338 CA LYS A 303 3501 5481 5728 -83 -1166 1886 C ATOM 2339 C LYS A 303 23.392 -5.930 -10.613 1.00 34.73 C ANISOU 2339 C LYS A 303 3067 4796 5332 -46 -1014 1544 C ATOM 2340 O LYS A 303 22.452 -5.870 -11.404 1.00 30.74 O ANISOU 2340 O LYS A 303 2695 4180 4806 -30 -875 1348 O ATOM 2341 CB LYS A 303 22.980 -7.974 -9.192 1.00 43.08 C ANISOU 2341 CB LYS A 303 3896 5813 6661 3 -1145 2131 C ATOM 2342 CG LYS A 303 22.787 -8.615 -7.821 1.00 42.11 C ANISOU 2342 CG LYS A 303 3674 5855 6471 -29 -1294 2531 C ATOM 2343 CD LYS A 303 23.980 -8.577 -6.994 0.00 50.47 C ANISOU 2343 CD LYS A 303 4561 7091 7525 -58 -1484 2781 C ATOM 2344 CE LYS A 303 23.801 -9.368 -5.708 0.00 53.30 C ANISOU 2344 CE LYS A 303 4794 7610 7849 -88 -1634 3228 C ATOM 2345 NZ LYS A 303 22.751 -8.784 -4.828 0.00 52.88 N1+ ANISOU 2345 NZ LYS A 303 4921 7858 7312 -203 -1659 3227 N1+ ATOM 2346 N PRO A 304 24.642 -5.565 -10.956 1.00 35.66 N ANISOU 2346 N PRO A 304 3086 4900 5562 -41 -1041 1483 N ATOM 2347 CA PRO A 304 24.929 -5.077 -12.309 1.00 38.02 C ANISOU 2347 CA PRO A 304 3442 5054 5951 -17 -891 1181 C ATOM 2348 C PRO A 304 24.907 -6.138 -13.420 1.00 35.86 C ANISOU 2348 C PRO A 304 3085 4488 6051 71 -737 1102 C ATOM 2349 O PRO A 304 24.863 -5.780 -14.601 1.00 39.80 O ANISOU 2349 O PRO A 304 3660 4895 6566 75 -592 835 O ATOM 2350 CB PRO A 304 26.331 -4.465 -12.171 1.00 43.05 C ANISOU 2350 CB PRO A 304 3966 5777 6612 -46 -977 1182 C ATOM 2351 CG PRO A 304 26.951 -5.233 -11.067 1.00 50.47 C ANISOU 2351 CG PRO A 304 4707 6791 7678 -35 -1149 1521 C ATOM 2352 CD PRO A 304 25.828 -5.448 -10.091 1.00 45.85 C ANISOU 2352 CD PRO A 304 4215 6348 6856 -74 -1217 1683 C ATOM 2353 N ASP A 305 24.953 -7.416 -13.058 1.00 37.03 N ANISOU 2353 N ASP A 305 3071 4499 6502 134 -761 1327 N ATOM 2354 CA ASP A 305 24.759 -8.490 -14.039 1.00 38.41 C ANISOU 2354 CA ASP A 305 3168 4381 7044 206 -598 1226 C ATOM 2355 C ASP A 305 23.285 -8.935 -14.149 1.00 36.82 C ANISOU 2355 C ASP A 305 3093 4123 6774 198 -525 1187 C ATOM 2356 O ASP A 305 22.979 -9.853 -14.907 1.00 37.24 O ANISOU 2356 O ASP A 305 3089 3943 7117 239 -390 1087 O ATOM 2357 CB ASP A 305 25.723 -9.675 -13.803 1.00 48.89 C ANISOU 2357 CB ASP A 305 4214 5515 8847 288 -625 1453 C ATOM 2358 CG ASP A 305 25.633 -10.267 -12.407 1.00 73.35 C ANISOU 2358 CG ASP A 305 7200 8699 11972 295 -804 1867 C ATOM 2359 OD1 ASP A 305 25.006 -9.651 -11.520 1.00101.00 O ANISOU 2359 OD1 ASP A 305 10838 12456 15080 223 -920 1969 O ATOM 2360 OD2 ASP A 305 26.211 -11.357 -12.196 1.00 84.82 O1- ANISOU 2360 OD2 ASP A 305 8414 9963 13851 371 -823 2097 O1- ATOM 2361 N SER A 306 22.371 -8.278 -13.432 1.00 27.51 N ANISOU 2361 N SER A 306 2077 3152 5223 138 -600 1239 N ATOM 2362 CA SER A 306 20.949 -8.573 -13.569 1.00 25.01 C ANISOU 2362 CA SER A 306 1882 2798 4825 125 -528 1185 C ATOM 2363 C SER A 306 20.382 -8.007 -14.871 1.00 25.09 C ANISOU 2363 C SER A 306 2041 2766 4726 103 -383 839 C ATOM 2364 O SER A 306 20.841 -6.976 -15.378 1.00 21.25 O ANISOU 2364 O SER A 306 1632 2372 4070 75 -366 666 O ATOM 2365 CB SER A 306 20.145 -8.020 -12.381 1.00 25.49 C ANISOU 2365 CB SER A 306 2057 3102 4526 64 -637 1341 C ATOM 2366 OG SER A 306 20.009 -6.602 -12.441 1.00 23.49 O ANISOU 2366 OG SER A 306 1971 3041 3911 4 -646 1156 O ATOM 2367 N LYS A 307 19.351 -8.682 -15.375 1.00 23.67 N ANISOU 2367 N LYS A 307 1894 2458 4641 108 -286 757 N ATOM 2368 CA LYS A 307 18.598 -8.234 -16.542 1.00 19.86 C ANISOU 2368 CA LYS A 307 1547 1970 4027 73 -169 466 C ATOM 2369 C LYS A 307 17.856 -6.940 -16.244 1.00 18.13 C ANISOU 2369 C LYS A 307 1514 1972 3401 23 -218 426 C ATOM 2370 O LYS A 307 17.666 -6.109 -17.125 1.00 17.14 O ANISOU 2370 O LYS A 307 1495 1901 3115 -7 -159 221 O ATOM 2371 CB LYS A 307 17.612 -9.326 -16.981 1.00 23.52 C ANISOU 2371 CB LYS A 307 1982 2263 4690 76 -76 412 C ATOM 2372 CG LYS A 307 18.325 -10.564 -17.507 1.00 25.08 C ANISOU 2372 CG LYS A 307 1991 2201 5335 120 17 373 C ATOM 2373 CD LYS A 307 17.375 -11.568 -18.138 1.00 25.91 C ANISOU 2373 CD LYS A 307 2070 2128 5646 103 133 241 C ATOM 2374 CE LYS A 307 18.119 -12.562 -19.019 1.00 25.51 C ANISOU 2374 CE LYS A 307 1854 1825 6016 126 274 69 C ATOM 2375 NZ LYS A 307 18.274 -13.870 -18.357 1.00 32.12 N1+ ANISOU 2375 NZ LYS A 307 2496 2416 7294 184 277 290 N1+ ATOM 2376 N ALA A 308 17.418 -6.787 -14.999 1.00 20.95 N ANISOU 2376 N ALA A 308 1900 2455 3604 9 -318 630 N ATOM 2377 CA ALA A 308 16.920 -5.509 -14.497 1.00 18.04 C ANISOU 2377 CA ALA A 308 1680 2295 2878 -39 -364 600 C ATOM 2378 C ALA A 308 17.885 -4.381 -14.787 1.00 13.19 C ANISOU 2378 C ALA A 308 1100 1768 2145 -59 -382 482 C ATOM 2379 O ALA A 308 17.508 -3.380 -15.389 1.00 12.71 O ANISOU 2379 O ALA A 308 1157 1759 1913 -85 -333 313 O ATOM 2380 CB ALA A 308 16.668 -5.593 -13.002 1.00 23.03 C ANISOU 2380 CB ALA A 308 2299 3073 3378 -63 -469 841 C ATOM 2381 N PHE A 309 19.135 -4.546 -14.377 1.00 16.00 N ANISOU 2381 N PHE A 309 1338 2131 2612 -48 -454 587 N ATOM 2382 CA PHE A 309 20.125 -3.485 -14.524 1.00 14.32 C ANISOU 2382 CA PHE A 309 1138 2003 2299 -76 -481 493 C ATOM 2383 C PHE A 309 20.389 -3.178 -15.995 1.00 18.34 C ANISOU 2383 C PHE A 309 1676 2410 2884 -67 -358 266 C ATOM 2384 O PHE A 309 20.341 -2.025 -16.416 1.00 17.24 O ANISOU 2384 O PHE A 309 1640 2344 2566 -104 -329 131 O ATOM 2385 CB PHE A 309 21.442 -3.841 -13.858 1.00 18.04 C ANISOU 2385 CB PHE A 309 1447 2497 2912 -66 -587 659 C ATOM 2386 CG PHE A 309 22.489 -2.799 -14.065 1.00 23.43 C ANISOU 2386 CG PHE A 309 2126 3253 3522 -102 -609 552 C ATOM 2387 CD1 PHE A 309 22.567 -1.701 -13.218 1.00 24.23 C ANISOU 2387 CD1 PHE A 309 2298 3554 3354 -176 -697 550 C ATOM 2388 CD2 PHE A 309 23.347 -2.864 -15.153 1.00 21.85 C ANISOU 2388 CD2 PHE A 309 1856 2926 3520 -73 -522 425 C ATOM 2389 CE1 PHE A 309 23.511 -0.707 -13.431 1.00 23.09 C ANISOU 2389 CE1 PHE A 309 2145 3461 3165 -219 -710 438 C ATOM 2390 CE2 PHE A 309 24.286 -1.867 -15.371 1.00 21.79 C ANISOU 2390 CE2 PHE A 309 1844 2984 3453 -113 -532 329 C ATOM 2391 CZ PHE A 309 24.367 -0.790 -14.509 1.00 19.96 C ANISOU 2391 CZ PHE A 309 1676 2932 2975 -185 -630 341 C ATOM 2392 N HIS A 310 20.678 -4.217 -16.773 1.00 20.87 N ANISOU 2392 N HIS A 310 1894 2560 3477 -23 -278 225 N ATOM 2393 CA HIS A 310 20.936 -4.038 -18.197 1.00 16.80 C ANISOU 2393 CA HIS A 310 1395 1974 3016 -30 -148 1 C ATOM 2394 C HIS A 310 19.769 -3.320 -18.922 1.00 17.09 C ANISOU 2394 C HIS A 310 1597 2078 2819 -70 -86 -145 C ATOM 2395 O HIS A 310 20.019 -2.504 -19.818 1.00 14.18 O ANISOU 2395 O HIS A 310 1284 1755 2350 -102 -25 -284 O ATOM 2396 CB HIS A 310 21.315 -5.367 -18.864 1.00 18.48 C ANISOU 2396 CB HIS A 310 1462 1991 3567 11 -51 -51 C ATOM 2397 CG HIS A 310 22.692 -5.855 -18.504 1.00 23.06 C ANISOU 2397 CG HIS A 310 1858 2491 4415 55 -84 55 C ATOM 2398 CD2 HIS A 310 23.109 -6.785 -17.608 1.00 22.86 C ANISOU 2398 CD2 HIS A 310 1675 2378 4633 106 -162 280 C ATOM 2399 ND1 HIS A 310 23.833 -5.378 -19.112 1.00 25.80 N ANISOU 2399 ND1 HIS A 310 2147 2841 4816 47 -33 -53 N ATOM 2400 CE1 HIS A 310 24.890 -5.984 -18.601 1.00 23.94 C ANISOU 2400 CE1 HIS A 310 1723 2522 4852 95 -82 88 C ATOM 2401 NE2 HIS A 310 24.475 -6.848 -17.692 1.00 26.68 N ANISOU 2401 NE2 HIS A 310 2003 2813 5322 134 -165 301 N ATOM 2402 N LEU A 311 18.520 -3.592 -18.524 1.00 13.26 N ANISOU 2402 N LEU A 311 1177 1606 2254 -71 -106 -91 N ATOM 2403 CA LEU A 311 17.370 -2.890 -19.107 1.00 12.52 C ANISOU 2403 CA LEU A 311 1218 1582 1954 -104 -66 -195 C ATOM 2404 C LEU A 311 17.388 -1.434 -18.647 1.00 14.81 C ANISOU 2404 C LEU A 311 1605 2005 2016 -130 -116 -179 C ATOM 2405 O LEU A 311 17.242 -0.511 -19.466 1.00 13.19 O ANISOU 2405 O LEU A 311 1473 1844 1695 -157 -70 -283 O ATOM 2406 CB LEU A 311 16.019 -3.554 -18.756 1.00 11.25 C ANISOU 2406 CB LEU A 311 1085 1398 1791 -99 -71 -138 C ATOM 2407 CG LEU A 311 14.747 -2.787 -19.185 1.00 12.16 C ANISOU 2407 CG LEU A 311 1321 1596 1702 -128 -49 -209 C ATOM 2408 CD1 LEU A 311 14.773 -2.468 -20.669 1.00 18.62 C ANISOU 2408 CD1 LEU A 311 2166 2428 2483 -161 27 -381 C ATOM 2409 CD2 LEU A 311 13.448 -3.520 -18.874 1.00 13.26 C ANISOU 2409 CD2 LEU A 311 1465 1706 1868 -126 -48 -158 C ATOM 2410 N LEU A 312 17.562 -1.236 -17.340 1.00 17.38 N ANISOU 2410 N LEU A 312 1923 2398 2282 -131 -207 -48 N ATOM 2411 CA LEU A 312 17.651 0.106 -16.759 1.00 16.53 C ANISOU 2411 CA LEU A 312 1892 2408 1982 -168 -248 -61 C ATOM 2412 C LEU A 312 18.679 0.971 -17.493 1.00 20.09 C ANISOU 2412 C LEU A 312 2336 2855 2441 -190 -217 -162 C ATOM 2413 O LEU A 312 18.420 2.145 -17.745 1.00 15.39 O ANISOU 2413 O LEU A 312 1823 2300 1725 -218 -190 -233 O ATOM 2414 CB LEU A 312 18.012 0.043 -15.265 1.00 19.10 C ANISOU 2414 CB LEU A 312 2177 2832 2248 -187 -354 78 C ATOM 2415 CG LEU A 312 18.207 1.393 -14.529 1.00 26.31 C ANISOU 2415 CG LEU A 312 3152 3876 2969 -247 -393 29 C ATOM 2416 CD1 LEU A 312 16.958 2.265 -14.632 1.00 22.64 C ANISOU 2416 CD1 LEU A 312 2808 3430 2362 -260 -327 -62 C ATOM 2417 CD2 LEU A 312 18.600 1.199 -13.070 1.00 21.44 C ANISOU 2417 CD2 LEU A 312 2483 3401 2264 -288 -506 160 C ATOM 2418 N GLN A 313 19.831 0.384 -17.832 1.00 17.40 N ANISOU 2418 N GLN A 313 1886 2457 2270 -175 -213 -159 N ATOM 2419 CA GLN A 313 20.946 1.130 -18.433 1.00 17.32 C ANISOU 2419 CA GLN A 313 1847 2448 2286 -200 -182 -239 C ATOM 2420 C GLN A 313 20.626 1.599 -19.849 1.00 17.14 C ANISOU 2420 C GLN A 313 1887 2404 2221 -216 -69 -366 C ATOM 2421 O GLN A 313 21.052 2.685 -20.278 1.00 19.56 O ANISOU 2421 O GLN A 313 2226 2743 2463 -252 -39 -417 O ATOM 2422 CB GLN A 313 22.212 0.270 -18.441 1.00 18.26 C ANISOU 2422 CB GLN A 313 1809 2501 2627 -174 -194 -199 C ATOM 2423 CG GLN A 313 23.462 0.944 -18.998 1.00 21.68 C ANISOU 2423 CG GLN A 313 2186 2936 3114 -201 -158 -273 C ATOM 2424 CD GLN A 313 24.730 0.180 -18.643 1.00 27.95 C ANISOU 2424 CD GLN A 313 2801 3680 4137 -173 -201 -196 C ATOM 2425 NE2 GLN A 313 24.770 -1.119 -18.972 1.00 23.80 N ANISOU 2425 NE2 GLN A 313 2177 3035 3830 -118 -151 -180 N ATOM 2426 OE1 GLN A 313 25.656 0.746 -18.055 1.00 42.33 O ANISOU 2426 OE1 GLN A 313 4560 5564 5959 -203 -279 -152 O ATOM 2427 N LYS A 314 19.903 0.760 -20.575 1.00 15.92 N ANISOU 2427 N LYS A 314 1739 2204 2106 -198 -8 -410 N ATOM 2428 CA LYS A 314 19.439 1.112 -21.909 1.00 16.19 C ANISOU 2428 CA LYS A 314 1831 2263 2058 -229 84 -515 C ATOM 2429 C LYS A 314 18.394 2.223 -21.861 1.00 16.75 C ANISOU 2429 C LYS A 314 2018 2402 1945 -246 64 -486 C ATOM 2430 O LYS A 314 18.402 3.134 -22.703 1.00 21.04 O ANISOU 2430 O LYS A 314 2602 2989 2404 -280 110 -517 O ATOM 2431 CB LYS A 314 18.896 -0.116 -22.596 1.00 17.51 C ANISOU 2431 CB LYS A 314 1964 2379 2309 -222 144 -588 C ATOM 2432 CG LYS A 314 19.978 -1.145 -22.858 1.00 14.79 C ANISOU 2432 CG LYS A 314 1488 1940 2193 -206 201 -647 C ATOM 2433 CD LYS A 314 19.384 -2.492 -23.219 1.00 11.17 C ANISOU 2433 CD LYS A 314 979 1391 1874 -197 256 -719 C ATOM 2434 CE LYS A 314 20.481 -3.474 -23.564 1.00 9.58 C ANISOU 2434 CE LYS A 314 629 1067 1944 -178 340 -802 C ATOM 2435 NZ LYS A 314 19.906 -4.744 -24.036 1.00 13.13 N1+ ANISOU 2435 NZ LYS A 314 1023 1410 2556 -183 419 -914 N1+ ATOM 2436 N LEU A 315 17.527 2.180 -20.856 1.00 14.81 N ANISOU 2436 N LEU A 315 1812 2163 1652 -224 1 -415 N ATOM 2437 CA LEU A 315 16.590 3.293 -20.621 1.00 16.80 C ANISOU 2437 CA LEU A 315 2154 2459 1772 -233 -10 -391 C ATOM 2438 C LEU A 315 17.307 4.612 -20.220 1.00 18.48 C ANISOU 2438 C LEU A 315 2384 2687 1953 -260 -20 -395 C ATOM 2439 O LEU A 315 16.959 5.686 -20.705 1.00 15.06 O ANISOU 2439 O LEU A 315 1996 2255 1469 -276 15 -402 O ATOM 2440 CB LEU A 315 15.574 2.905 -19.548 1.00 11.86 C ANISOU 2440 CB LEU A 315 1553 1842 1112 -210 -56 -329 C ATOM 2441 CG LEU A 315 14.608 1.784 -19.906 1.00 15.40 C ANISOU 2441 CG LEU A 315 1990 2265 1597 -192 -42 -323 C ATOM 2442 CD1 LEU A 315 13.816 1.405 -18.682 1.00 15.20 C ANISOU 2442 CD1 LEU A 315 1975 2253 1549 -175 -84 -241 C ATOM 2443 CD2 LEU A 315 13.657 2.201 -21.016 1.00 15.75 C ANISOU 2443 CD2 LEU A 315 2077 2337 1571 -207 0 -363 C ATOM 2444 N LEU A 316 18.314 4.514 -19.360 1.00 8.74 N ANISOU 2444 N LEU A 316 1098 1459 765 -269 -71 -384 N ATOM 2445 CA LEU A 316 19.053 5.670 -18.908 1.00 14.00 C ANISOU 2445 CA LEU A 316 1765 2140 1413 -311 -86 -411 C ATOM 2446 C LEU A 316 20.310 5.910 -19.732 1.00 17.71 C ANISOU 2446 C LEU A 316 2175 2586 1968 -334 -48 -445 C ATOM 2447 O LEU A 316 21.395 6.085 -19.205 1.00 25.18 O ANISOU 2447 O LEU A 316 3057 3544 2967 -361 -89 -452 O ATOM 2448 CB LEU A 316 19.371 5.527 -17.424 1.00 14.02 C ANISOU 2448 CB LEU A 316 1740 2204 1382 -330 -177 -381 C ATOM 2449 CG LEU A 316 18.134 5.589 -16.529 1.00 16.39 C ANISOU 2449 CG LEU A 316 2106 2550 1570 -326 -192 -363 C ATOM 2450 CD1 LEU A 316 18.561 5.384 -15.085 1.00 17.24 C ANISOU 2450 CD1 LEU A 316 2177 2765 1609 -366 -284 -325 C ATOM 2451 CD2 LEU A 316 17.361 6.902 -16.673 1.00 14.88 C ANISOU 2451 CD2 LEU A 316 1992 2333 1330 -343 -127 -434 C ATOM 2452 N THR A 317 20.135 5.958 -21.042 1.00 14.68 N ANISOU 2452 N THR A 317 1806 2187 1586 -334 32 -465 N ATOM 2453 CA THR A 317 21.207 6.292 -21.962 1.00 15.88 C ANISOU 2453 CA THR A 317 1908 2332 1796 -367 96 -498 C ATOM 2454 C THR A 317 21.171 7.798 -22.173 1.00 15.47 C ANISOU 2454 C THR A 317 1900 2268 1710 -407 127 -485 C ATOM 2455 O THR A 317 20.114 8.404 -22.367 1.00 15.21 O ANISOU 2455 O THR A 317 1936 2230 1613 -400 141 -449 O ATOM 2456 CB THR A 317 21.039 5.529 -23.290 1.00 15.10 C ANISOU 2456 CB THR A 317 1795 2252 1689 -366 178 -534 C ATOM 2457 CG2 THR A 317 22.071 5.956 -24.286 1.00 12.98 C ANISOU 2457 CG2 THR A 317 1479 2002 1450 -412 264 -568 C ATOM 2458 OG1 THR A 317 21.139 4.111 -23.035 1.00 11.49 O ANISOU 2458 OG1 THR A 317 1278 1766 1322 -329 162 -561 O ATOM 2459 N MET A 318 22.348 8.395 -22.162 1.00 18.55 N ANISOU 2459 N MET A 318 2233 2639 2174 -448 141 -506 N ATOM 2460 CA MET A 318 22.466 9.846 -22.138 1.00 19.51 C ANISOU 2460 CA MET A 318 2377 2719 2318 -494 168 -498 C ATOM 2461 C MET A 318 22.089 10.470 -23.470 1.00 16.23 C ANISOU 2461 C MET A 318 1990 2302 1875 -509 257 -432 C ATOM 2462 O MET A 318 21.387 11.467 -23.512 1.00 17.73 O ANISOU 2462 O MET A 318 2224 2446 2068 -514 274 -381 O ATOM 2463 CB MET A 318 23.898 10.230 -21.798 1.00 28.34 C ANISOU 2463 CB MET A 318 3409 3820 3538 -544 158 -540 C ATOM 2464 CG MET A 318 24.344 9.786 -20.416 1.00 35.37 C ANISOU 2464 CG MET A 318 4255 4743 4442 -548 48 -580 C ATOM 2465 SD MET A 318 23.734 10.877 -19.128 1.00 37.41 S ANISOU 2465 SD MET A 318 4573 4992 4648 -591 -1 -639 S ATOM 2466 CE MET A 318 24.852 12.242 -19.382 1.00 26.56 C ANISOU 2466 CE MET A 318 3140 3547 3405 -679 50 -694 C ATOM 2467 N ASP A 319 22.576 9.879 -24.554 1.00 18.93 N ANISOU 2467 N ASP A 319 2295 2702 2197 -523 318 -431 N ATOM 2468 CA ASP A 319 22.347 10.396 -25.891 1.00 17.68 C ANISOU 2468 CA ASP A 319 2150 2592 1974 -558 401 -354 C ATOM 2469 C ASP A 319 20.971 9.899 -26.309 1.00 18.51 C ANISOU 2469 C ASP A 319 2317 2761 1955 -527 381 -316 C ATOM 2470 O ASP A 319 20.773 8.689 -26.409 1.00 16.19 O ANISOU 2470 O ASP A 319 2018 2516 1618 -506 371 -387 O ATOM 2471 CB ASP A 319 23.422 9.880 -26.856 1.00 18.21 C ANISOU 2471 CB ASP A 319 2148 2729 2043 -601 487 -398 C ATOM 2472 CG ASP A 319 23.198 10.311 -28.307 1.00 14.94 C ANISOU 2472 CG ASP A 319 1745 2420 1511 -658 577 -312 C ATOM 2473 OD1 ASP A 319 22.118 10.822 -28.657 1.00 15.82 O ANISOU 2473 OD1 ASP A 319 1913 2563 1535 -656 555 -202 O ATOM 2474 OD2 ASP A 319 24.121 10.122 -29.119 1.00 16.24 O1- ANISOU 2474 OD2 ASP A 319 1850 2652 1668 -711 670 -347 O1- ATOM 2475 N PRO A 320 20.031 10.827 -26.583 1.00 20.53 N ANISOU 2475 N PRO A 320 2615 3006 2178 -526 377 -200 N ATOM 2476 CA PRO A 320 18.668 10.387 -26.872 1.00 21.07 C ANISOU 2476 CA PRO A 320 2727 3136 2143 -496 342 -157 C ATOM 2477 C PRO A 320 18.548 9.427 -28.059 1.00 19.69 C ANISOU 2477 C PRO A 320 2541 3114 1827 -534 374 -185 C ATOM 2478 O PRO A 320 17.678 8.559 -28.028 1.00 22.77 O ANISOU 2478 O PRO A 320 2951 3547 2154 -511 336 -226 O ATOM 2479 CB PRO A 320 17.917 11.700 -27.139 1.00 21.78 C ANISOU 2479 CB PRO A 320 2828 3184 2262 -495 345 2 C ATOM 2480 CG PRO A 320 18.967 12.714 -27.477 1.00 19.26 C ANISOU 2480 CG PRO A 320 2470 2816 2032 -545 408 58 C ATOM 2481 CD PRO A 320 20.153 12.300 -26.655 1.00 19.42 C ANISOU 2481 CD PRO A 320 2466 2784 2128 -551 408 -95 C ATOM 2482 N ILE A 321 19.406 9.562 -29.074 1.00 20.59 N ANISOU 2482 N ILE A 321 2618 3314 1892 -600 453 -178 N ATOM 2483 CA ILE A 321 19.365 8.636 -30.230 1.00 22.06 C ANISOU 2483 CA ILE A 321 2787 3669 1925 -659 506 -249 C ATOM 2484 C ILE A 321 19.815 7.194 -29.893 1.00 22.16 C ANISOU 2484 C ILE A 321 2769 3653 1997 -638 526 -449 C ATOM 2485 O ILE A 321 19.496 6.274 -30.645 1.00 18.43 O ANISOU 2485 O ILE A 321 2287 3291 1426 -678 563 -549 O ATOM 2486 CB ILE A 321 20.101 9.170 -31.499 1.00 24.86 C ANISOU 2486 CB ILE A 321 3107 4161 2179 -753 604 -189 C ATOM 2487 CG1 ILE A 321 21.615 9.264 -31.311 1.00 36.05 C ANISOU 2487 CG1 ILE A 321 4466 5506 3724 -768 684 -265 C ATOM 2488 CG2 ILE A 321 19.534 10.526 -31.937 1.00 24.91 C ANISOU 2488 CG2 ILE A 321 3127 4197 2142 -774 580 53 C ATOM 2489 CD1 ILE A 321 22.389 9.387 -32.612 1.00 36.46 C ANISOU 2489 CD1 ILE A 321 4472 5722 3660 -871 810 -261 C ATOM 2490 N LYS A 322 20.536 7.011 -28.777 1.00 19.67 N ANISOU 2490 N LYS A 322 2428 3195 1851 -583 501 -501 N ATOM 2491 CA LYS A 322 20.966 5.687 -28.281 1.00 22.05 C ANISOU 2491 CA LYS A 322 2678 3434 2264 -547 504 -640 C ATOM 2492 C LYS A 322 20.104 5.105 -27.132 1.00 19.24 C ANISOU 2492 C LYS A 322 2354 2995 1963 -475 403 -630 C ATOM 2493 O LYS A 322 20.473 4.104 -26.509 1.00 23.97 O ANISOU 2493 O LYS A 322 2900 3518 2687 -437 389 -695 O ATOM 2494 CB LYS A 322 22.448 5.740 -27.853 1.00 16.57 C ANISOU 2494 CB LYS A 322 1903 2664 1729 -542 536 -679 C ATOM 2495 CG LYS A 322 23.399 5.983 -29.002 1.00 19.22 C ANISOU 2495 CG LYS A 322 2185 3081 2037 -615 663 -722 C ATOM 2496 CD LYS A 322 24.828 6.225 -28.542 1.00 21.87 C ANISOU 2496 CD LYS A 322 2429 3336 2543 -611 687 -738 C ATOM 2497 CE LYS A 322 25.743 6.376 -29.752 1.00 31.34 C ANISOU 2497 CE LYS A 322 3567 4627 3716 -689 838 -791 C ATOM 2498 NZ LYS A 322 27.192 6.398 -29.393 1.00 38.15 N1+ ANISOU 2498 NZ LYS A 322 4311 5411 4774 -686 876 -829 N1+ ATOM 2499 N ARG A 323 18.962 5.725 -26.860 1.00 17.47 N ANISOU 2499 N ARG A 323 2200 2780 1657 -458 340 -534 N ATOM 2500 CA ARG A 323 18.024 5.242 -25.843 1.00 13.14 C ANISOU 2500 CA ARG A 323 1682 2174 1135 -401 261 -518 C ATOM 2501 C ARG A 323 17.119 4.245 -26.567 1.00 13.56 C ANISOU 2501 C ARG A 323 1737 2293 1123 -418 275 -576 C ATOM 2502 O ARG A 323 16.760 4.496 -27.731 1.00 13.95 O ANISOU 2502 O ARG A 323 1797 2459 1045 -475 312 -573 O ATOM 2503 CB ARG A 323 17.235 6.434 -25.295 1.00 13.98 C ANISOU 2503 CB ARG A 323 1847 2258 1207 -381 213 -410 C ATOM 2504 CG ARG A 323 16.927 6.380 -23.818 1.00 18.94 C ANISOU 2504 CG ARG A 323 2494 2812 1892 -333 147 -402 C ATOM 2505 CD ARG A 323 16.442 7.738 -23.320 1.00 16.67 C ANISOU 2505 CD ARG A 323 2247 2484 1604 -327 137 -339 C ATOM 2506 NE ARG A 323 17.539 8.696 -23.177 1.00 13.44 N ANISOU 2506 NE ARG A 323 1817 2032 1257 -358 160 -347 N ATOM 2507 CZ ARG A 323 17.431 10.023 -23.275 1.00 12.33 C ANISOU 2507 CZ ARG A 323 1688 1840 1156 -374 189 -297 C ATOM 2508 NH1 ARG A 323 16.261 10.604 -23.539 1.00 11.23 N1+ ANISOU 2508 NH1 ARG A 323 1575 1684 1007 -352 197 -218 N1+ ATOM 2509 NH2 ARG A 323 18.523 10.781 -23.150 1.00 12.77 N ANISOU 2509 NH2 ARG A 323 1713 1850 1290 -413 214 -320 N ATOM 2510 N ILE A 324 16.782 3.109 -25.956 1.00 14.09 N ANISOU 2510 N ILE A 324 1783 2298 1273 -382 249 -627 N ATOM 2511 CA ILE A 324 15.812 2.201 -26.630 1.00 22.29 C ANISOU 2511 CA ILE A 324 2819 3388 2263 -410 262 -696 C ATOM 2512 C ILE A 324 14.402 2.785 -26.604 1.00 14.25 C ANISOU 2512 C ILE A 324 1856 2425 1132 -405 200 -597 C ATOM 2513 O ILE A 324 14.097 3.677 -25.829 1.00 17.32 O ANISOU 2513 O ILE A 324 2284 2776 1522 -364 154 -489 O ATOM 2514 CB ILE A 324 15.819 0.709 -26.156 1.00 25.90 C ANISOU 2514 CB ILE A 324 3217 3744 2880 -383 271 -783 C ATOM 2515 CG1 ILE A 324 15.472 0.551 -24.681 1.00 32.43 C ANISOU 2515 CG1 ILE A 324 4053 4474 3793 -313 190 -676 C ATOM 2516 CG2 ILE A 324 17.157 0.043 -26.501 1.00 43.93 C ANISOU 2516 CG2 ILE A 324 5416 5974 5303 -394 355 -898 C ATOM 2517 CD1 ILE A 324 15.255 -0.906 -24.295 1.00 36.73 C ANISOU 2517 CD1 ILE A 324 4534 4918 4502 -292 196 -717 C ATOM 2518 N THR A 325 13.564 2.274 -27.487 1.00 16.21 N ANISOU 2518 N THR A 325 2098 2769 1293 -456 207 -648 N ATOM 2519 CA THR A 325 12.182 2.723 -27.624 1.00 16.72 C ANISOU 2519 CA THR A 325 2189 2901 1262 -458 144 -552 C ATOM 2520 C THR A 325 11.381 1.947 -26.631 1.00 16.38 C ANISOU 2520 C THR A 325 2142 2762 1320 -409 105 -555 C ATOM 2521 O THR A 325 11.884 1.001 -26.023 1.00 16.32 O ANISOU 2521 O THR A 325 2107 2653 1442 -385 125 -625 O ATOM 2522 CB THR A 325 11.631 2.436 -29.045 1.00 21.65 C ANISOU 2522 CB THR A 325 2791 3706 1730 -555 154 -608 C ATOM 2523 CG2 THR A 325 12.486 3.131 -30.108 1.00 27.70 C ANISOU 2523 CG2 THR A 325 3554 4600 2369 -621 207 -597 C ATOM 2524 OG1 THR A 325 11.647 1.029 -29.313 1.00 16.52 O ANISOU 2524 OG1 THR A 325 2098 3045 1132 -597 197 -796 O ATOM 2525 N SER A 326 10.124 2.332 -26.482 1.00 16.76 N ANISOU 2525 N SER A 326 2203 2840 1323 -394 52 -464 N ATOM 2526 CA SER A 326 9.207 1.600 -25.643 1.00 16.53 C ANISOU 2526 CA SER A 326 2163 2741 1375 -360 23 -459 C ATOM 2527 C SER A 326 9.028 0.156 -26.150 1.00 15.73 C ANISOU 2527 C SER A 326 2011 2642 1322 -413 46 -600 C ATOM 2528 O SER A 326 9.059 -0.780 -25.354 1.00 19.42 O ANISOU 2528 O SER A 326 2455 2994 1929 -384 56 -627 O ATOM 2529 CB SER A 326 7.850 2.334 -25.522 1.00 24.13 C ANISOU 2529 CB SER A 326 3131 3745 2294 -339 -26 -340 C ATOM 2530 OG SER A 326 7.378 2.846 -26.767 1.00 19.35 O ANISOU 2530 OG SER A 326 2504 3281 1566 -394 -53 -298 O ATOM 2531 N GLU A 327 8.879 -0.032 -27.457 1.00 17.64 N ANISOU 2531 N GLU A 327 2229 3017 1455 -500 59 -690 N ATOM 2532 CA GLU A 327 8.617 -1.372 -27.979 1.00 20.52 C ANISOU 2532 CA GLU A 327 2539 3384 1874 -568 93 -863 C ATOM 2533 C GLU A 327 9.809 -2.304 -27.726 1.00 18.18 C ANISOU 2533 C GLU A 327 2208 2949 1750 -555 175 -991 C ATOM 2534 O GLU A 327 9.621 -3.457 -27.344 1.00 16.94 O ANISOU 2534 O GLU A 327 2000 2669 1768 -551 200 -1068 O ATOM 2535 CB GLU A 327 8.225 -1.355 -29.464 1.00 26.73 C ANISOU 2535 CB GLU A 327 3301 4383 2470 -688 91 -957 C ATOM 2536 CG GLU A 327 7.660 -2.697 -29.944 1.00 47.07 C ANISOU 2536 CG GLU A 327 5814 6968 5103 -776 117 -1158 C ATOM 2537 CD GLU A 327 7.070 -2.649 -31.353 1.00 72.47 C ANISOU 2537 CD GLU A 327 9001 10443 8090 -917 92 -1249 C ATOM 2538 OE1 GLU A 327 7.846 -2.544 -32.330 1.00 68.50 O ANISOU 2538 OE1 GLU A 327 8497 10080 7448 -999 153 -1361 O ATOM 2539 OE2 GLU A 327 5.825 -2.739 -31.493 1.00 74.30 O1- ANISOU 2539 OE2 GLU A 327 9202 10758 8272 -955 11 -1211 O1- ATOM 2540 N GLN A 328 11.025 -1.807 -27.911 1.00 13.74 N ANISOU 2540 N GLN A 328 1658 2393 1168 -545 219 -999 N ATOM 2541 CA GLN A 328 12.215 -2.633 -27.671 1.00 17.02 C ANISOU 2541 CA GLN A 328 2019 2672 1776 -524 297 -1104 C ATOM 2542 C GLN A 328 12.339 -3.029 -26.206 1.00 18.75 C ANISOU 2542 C GLN A 328 2223 2713 2188 -428 258 -985 C ATOM 2543 O GLN A 328 12.699 -4.156 -25.893 1.00 19.31 O ANISOU 2543 O GLN A 328 2219 2642 2476 -411 300 -1046 O ATOM 2544 CB GLN A 328 13.469 -1.906 -28.120 1.00 18.54 C ANISOU 2544 CB GLN A 328 2219 2915 1908 -532 347 -1116 C ATOM 2545 CG GLN A 328 13.601 -1.786 -29.624 1.00 19.42 C ANISOU 2545 CG GLN A 328 2323 3210 1844 -645 417 -1257 C ATOM 2546 CD GLN A 328 14.772 -0.890 -30.032 1.00 32.99 C ANISOU 2546 CD GLN A 328 4053 4993 3488 -655 467 -1227 C ATOM 2547 NE2 GLN A 328 15.541 -1.339 -31.021 1.00 40.74 N ANISOU 2547 NE2 GLN A 328 4985 6044 4452 -734 587 -1413 N ATOM 2548 OE1 GLN A 328 14.978 0.208 -29.476 1.00 25.21 O ANISOU 2548 OE1 GLN A 328 3116 3996 2469 -600 410 -1051 O ATOM 2549 N ALA A 329 12.003 -2.104 -25.315 1.00 17.49 N ANISOU 2549 N ALA A 329 2124 2567 1953 -372 181 -811 N ATOM 2550 CA ALA A 329 12.014 -2.375 -23.885 1.00 19.10 C ANISOU 2550 CA ALA A 329 2320 2659 2277 -300 136 -685 C ATOM 2551 C ALA A 329 10.996 -3.437 -23.491 1.00 17.98 C ANISOU 2551 C ALA A 329 2141 2445 2245 -300 127 -675 C ATOM 2552 O ALA A 329 11.284 -4.265 -22.632 1.00 23.06 O ANISOU 2552 O ALA A 329 2730 2967 3063 -261 124 -613 O ATOM 2553 CB ALA A 329 11.774 -1.100 -23.095 1.00 20.12 C ANISOU 2553 CB ALA A 329 2523 2843 2279 -263 76 -546 C ATOM 2554 N MET A 330 9.836 -3.447 -24.130 1.00 15.14 N ANISOU 2554 N MET A 330 1795 2159 1799 -347 120 -722 N ATOM 2555 CA MET A 330 8.831 -4.494 -23.855 1.00 23.03 C ANISOU 2555 CA MET A 330 2746 3085 2919 -361 119 -730 C ATOM 2556 C MET A 330 9.309 -5.879 -24.292 1.00 18.91 C ANISOU 2556 C MET A 330 2130 2435 2618 -395 194 -881 C ATOM 2557 O MET A 330 8.916 -6.872 -23.690 1.00 16.67 O ANISOU 2557 O MET A 330 1787 2020 2528 -382 203 -845 O ATOM 2558 CB MET A 330 7.469 -4.177 -24.495 1.00 19.03 C ANISOU 2558 CB MET A 330 2257 2699 2276 -413 86 -752 C ATOM 2559 CG MET A 330 6.752 -3.010 -23.844 1.00 23.88 C ANISOU 2559 CG MET A 330 2931 3382 2761 -365 28 -589 C ATOM 2560 SD MET A 330 5.252 -2.492 -24.699 1.00 25.26 S ANISOU 2560 SD MET A 330 3098 3704 2796 -417 -21 -582 S ATOM 2561 CE MET A 330 4.225 -3.953 -24.505 1.00 27.08 C ANISOU 2561 CE MET A 330 3248 3853 3189 -459 -12 -643 C ATOM 2562 N GLN A 331 10.160 -5.925 -25.321 1.00 17.80 N ANISOU 2562 N GLN A 331 1970 2329 2464 -441 259 -1048 N ATOM 2563 CA GLN A 331 10.740 -7.171 -25.827 1.00 17.50 C ANISOU 2563 CA GLN A 331 1832 2159 2660 -477 359 -1234 C ATOM 2564 C GLN A 331 11.938 -7.659 -25.020 1.00 16.34 C ANISOU 2564 C GLN A 331 1616 1833 2760 -396 387 -1155 C ATOM 2565 O GLN A 331 12.478 -8.720 -25.319 1.00 15.87 O ANISOU 2565 O GLN A 331 1450 1620 2959 -408 480 -1290 O ATOM 2566 CB GLN A 331 11.185 -7.019 -27.302 1.00 21.09 C ANISOU 2566 CB GLN A 331 2284 2746 2985 -573 439 -1469 C ATOM 2567 CG GLN A 331 10.095 -6.702 -28.324 1.00 21.72 C ANISOU 2567 CG GLN A 331 2400 3033 2820 -680 411 -1567 C ATOM 2568 CD GLN A 331 8.833 -7.466 -28.062 1.00 30.30 C ANISOU 2568 CD GLN A 331 3450 4061 4001 -708 378 -1577 C ATOM 2569 NE2 GLN A 331 8.846 -8.753 -28.387 1.00 32.05 N ANISOU 2569 NE2 GLN A 331 3576 4150 4451 -766 469 -1783 N ATOM 2570 OE1 GLN A 331 7.862 -6.921 -27.524 1.00 48.46 O ANISOU 2570 OE1 GLN A 331 5795 6415 6201 -676 283 -1404 O ATOM 2571 N ASP A 332 12.355 -6.903 -24.008 1.00 18.95 N ANISOU 2571 N ASP A 332 1991 2182 3025 -320 309 -945 N ATOM 2572 CA ASP A 332 13.586 -7.186 -23.278 1.00 16.08 C ANISOU 2572 CA ASP A 332 1558 1700 2854 -252 310 -847 C ATOM 2573 C ASP A 332 13.459 -8.512 -22.542 1.00 15.74 C ANISOU 2573 C ASP A 332 1402 1455 3125 -216 321 -761 C ATOM 2574 O ASP A 332 12.373 -8.825 -22.039 1.00 15.74 O ANISOU 2574 O ASP A 332 1417 1440 3123 -220 284 -673 O ATOM 2575 CB ASP A 332 13.869 -6.060 -22.269 1.00 19.43 C ANISOU 2575 CB ASP A 332 2056 2221 3106 -201 208 -645 C ATOM 2576 CG ASP A 332 15.273 -6.125 -21.717 1.00 16.74 C ANISOU 2576 CG ASP A 332 1640 1813 2906 -151 195 -563 C ATOM 2577 OD1 ASP A 332 15.510 -6.869 -20.752 1.00 21.95 O ANISOU 2577 OD1 ASP A 332 2216 2366 3757 -104 156 -407 O ATOM 2578 OD2 ASP A 332 16.152 -5.488 -22.302 1.00 23.91 O1- ANISOU 2578 OD2 ASP A 332 2556 2777 3750 -164 226 -646 O1- ATOM 2579 N PRO A 333 14.552 -9.290 -22.465 1.00 11.90 N ANISOU 2579 N PRO A 333 788 805 2930 -178 375 -769 N ATOM 2580 CA PRO A 333 14.435 -10.571 -21.789 1.00 16.34 C ANISOU 2580 CA PRO A 333 1223 1151 3834 -140 389 -657 C ATOM 2581 C PRO A 333 14.163 -10.496 -20.275 1.00 21.82 C ANISOU 2581 C PRO A 333 1925 1863 4502 -84 264 -326 C ATOM 2582 O PRO A 333 13.800 -11.522 -19.673 1.00 24.67 O ANISOU 2582 O PRO A 333 2190 2068 5113 -64 266 -191 O ATOM 2583 CB PRO A 333 15.774 -11.263 -22.084 1.00 20.41 C ANISOU 2583 CB PRO A 333 1585 1491 4678 -104 476 -728 C ATOM 2584 CG PRO A 333 16.723 -10.173 -22.437 1.00 18.50 C ANISOU 2584 CG PRO A 333 1401 1401 4226 -102 464 -777 C ATOM 2585 CD PRO A 333 15.869 -9.119 -23.093 1.00 16.33 C ANISOU 2585 CD PRO A 333 1296 1352 3558 -173 445 -891 C ATOM 2586 N TYR A 334 14.321 -9.316 -19.670 1.00 14.92 N ANISOU 2586 N TYR A 334 1155 1178 3335 -70 166 -203 N ATOM 2587 CA TYR A 334 13.873 -9.083 -18.286 1.00 18.11 C ANISOU 2587 CA TYR A 334 1592 1664 3623 -46 57 65 C ATOM 2588 C TYR A 334 12.426 -9.563 -18.025 1.00 17.40 C ANISOU 2588 C TYR A 334 1528 1556 3528 -73 66 111 C ATOM 2589 O TYR A 334 12.133 -10.170 -16.990 1.00 22.86 O ANISOU 2589 O TYR A 334 2162 2203 4320 -54 25 338 O ATOM 2590 CB TYR A 334 14.029 -7.590 -17.953 1.00 17.28 C ANISOU 2590 CB TYR A 334 1617 1778 3172 -55 -15 85 C ATOM 2591 CG TYR A 334 13.520 -7.153 -16.606 1.00 16.31 C ANISOU 2591 CG TYR A 334 1547 1785 2866 -54 -107 297 C ATOM 2592 CD1 TYR A 334 13.987 -7.750 -15.427 1.00 22.42 C ANISOU 2592 CD1 TYR A 334 2227 2544 3745 -29 -179 546 C ATOM 2593 CD2 TYR A 334 12.596 -6.121 -16.498 1.00 15.84 C ANISOU 2593 CD2 TYR A 334 1618 1873 2526 -83 -117 252 C ATOM 2594 CE1 TYR A 334 13.524 -7.344 -14.176 1.00 21.17 C ANISOU 2594 CE1 TYR A 334 2118 2548 3378 -48 -255 728 C ATOM 2595 CE2 TYR A 334 12.133 -5.697 -15.257 1.00 20.79 C ANISOU 2595 CE2 TYR A 334 2289 2629 2979 -92 -177 410 C ATOM 2596 CZ TYR A 334 12.599 -6.308 -14.097 1.00 22.83 C ANISOU 2596 CZ TYR A 334 2466 2903 3304 -83 -243 638 C ATOM 2597 OH TYR A 334 12.128 -5.887 -12.877 1.00 19.42 O ANISOU 2597 OH TYR A 334 2079 2637 2662 -112 -292 778 O ATOM 2598 N PHE A 335 11.548 -9.315 -18.983 1.00 14.60 N ANISOU 2598 N PHE A 335 1244 1243 3062 -124 118 -92 N ATOM 2599 CA PHE A 335 10.137 -9.709 -18.888 1.00 16.76 C ANISOU 2599 CA PHE A 335 1533 1506 3331 -158 130 -80 C ATOM 2600 C PHE A 335 9.848 -11.181 -19.171 1.00 18.27 C ANISOU 2600 C PHE A 335 1593 1474 3874 -177 205 -126 C ATOM 2601 O PHE A 335 8.721 -11.637 -18.915 1.00 20.66 O ANISOU 2601 O PHE A 335 1885 1746 4219 -207 212 -78 O ATOM 2602 CB PHE A 335 9.280 -8.793 -19.781 1.00 14.59 C ANISOU 2602 CB PHE A 335 1367 1384 2792 -209 136 -254 C ATOM 2603 CG PHE A 335 9.346 -7.353 -19.362 1.00 15.29 C ANISOU 2603 CG PHE A 335 1572 1658 2581 -189 72 -184 C ATOM 2604 CD1 PHE A 335 8.868 -6.963 -18.106 1.00 12.91 C ANISOU 2604 CD1 PHE A 335 1308 1430 2166 -166 19 9 C ATOM 2605 CD2 PHE A 335 9.941 -6.383 -20.180 1.00 17.06 C ANISOU 2605 CD2 PHE A 335 1857 1978 2647 -199 76 -310 C ATOM 2606 CE1 PHE A 335 8.959 -5.635 -17.693 1.00 11.87 C ANISOU 2606 CE1 PHE A 335 1272 1449 1789 -154 -22 39 C ATOM 2607 CE2 PHE A 335 10.025 -5.050 -19.760 1.00 10.51 C ANISOU 2607 CE2 PHE A 335 1120 1284 1589 -182 27 -247 C ATOM 2608 CZ PHE A 335 9.538 -4.679 -18.520 1.00 8.84 C ANISOU 2608 CZ PHE A 335 943 1129 1288 -160 -18 -88 C ATOM 2609 N LEU A 336 10.839 -11.910 -19.691 1.00 18.23 N ANISOU 2609 N LEU A 336 1481 1304 4143 -164 272 -228 N ATOM 2610 CA LEU A 336 10.793 -13.378 -19.810 1.00 22.19 C ANISOU 2610 CA LEU A 336 1827 1539 5067 -170 358 -255 C ATOM 2611 C LEU A 336 11.458 -14.169 -18.641 1.00 25.32 C ANISOU 2611 C LEU A 336 2088 1769 5764 -95 324 57 C ATOM 2612 O LEU A 336 11.269 -15.388 -18.515 1.00 27.46 O ANISOU 2612 O LEU A 336 2219 1800 6415 -92 386 109 O ATOM 2613 CB LEU A 336 11.461 -13.798 -21.128 1.00 27.28 C ANISOU 2613 CB LEU A 336 2405 2075 5883 -207 480 -581 C ATOM 2614 CG LEU A 336 11.008 -13.132 -22.431 1.00 28.01 C ANISOU 2614 CG LEU A 336 2602 2346 5693 -297 519 -891 C ATOM 2615 CD1 LEU A 336 11.685 -13.796 -23.626 1.00 28.33 C ANISOU 2615 CD1 LEU A 336 2550 2269 5946 -349 664 -1214 C ATOM 2616 CD2 LEU A 336 9.497 -13.190 -22.585 1.00 29.79 C ANISOU 2616 CD2 LEU A 336 2878 2642 5798 -368 497 -934 C ATOM 2617 N GLU A 337 12.273 -13.495 -17.832 1.00 21.25 N ANISOU 2617 N GLU A 337 1598 1377 5099 -40 226 265 N ATOM 2618 CA GLU A 337 12.866 -14.079 -16.622 1.00 19.92 C ANISOU 2618 CA GLU A 337 1307 1127 5136 22 157 613 C ATOM 2619 C GLU A 337 11.794 -14.179 -15.537 1.00 21.56 C ANISOU 2619 C GLU A 337 1549 1418 5223 3 94 871 C ATOM 2620 O GLU A 337 10.984 -13.269 -15.374 1.00 24.19 O ANISOU 2620 O GLU A 337 2032 1965 5194 -34 58 835 O ATOM 2621 CB GLU A 337 13.994 -13.161 -16.145 1.00 18.91 C ANISOU 2621 CB GLU A 337 1209 1168 4806 60 58 720 C ATOM 2622 CG GLU A 337 14.914 -13.675 -15.061 1.00 20.61 C ANISOU 2622 CG GLU A 337 1276 1333 5223 118 -30 1062 C ATOM 2623 CD GLU A 337 15.999 -12.662 -14.733 1.00 20.99 C ANISOU 2623 CD GLU A 337 1360 1573 5042 135 -129 1108 C ATOM 2624 OE1 GLU A 337 15.666 -11.518 -14.310 1.00 20.76 O ANISOU 2624 OE1 GLU A 337 1487 1803 4597 97 -203 1107 O ATOM 2625 OE2 GLU A 337 17.190 -12.996 -14.907 1.00 20.79 O1- ANISOU 2625 OE2 GLU A 337 1196 1432 5270 183 -126 1133 O1- ATOM 2626 N ASP A 338 11.786 -15.280 -14.799 1.00 27.56 N ANISOU 2626 N ASP A 338 2159 2008 6305 29 91 1139 N ATOM 2627 CA ASP A 338 10.940 -15.421 -13.608 1.00 31.41 C ANISOU 2627 CA ASP A 338 2658 2595 6682 10 29 1447 C ATOM 2628 C ASP A 338 11.184 -14.251 -12.615 1.00 31.32 C ANISOU 2628 C ASP A 338 2763 2913 6223 5 -98 1615 C ATOM 2629 O ASP A 338 12.332 -13.864 -12.397 1.00 24.49 O ANISOU 2629 O ASP A 338 1872 2119 5314 39 -170 1677 O ATOM 2630 CB ASP A 338 11.258 -16.753 -12.935 1.00 34.89 C ANISOU 2630 CB ASP A 338 2890 2802 7564 47 30 1769 C ATOM 2631 CG ASP A 338 10.394 -17.015 -11.738 1.00 41.70 C ANISOU 2631 CG ASP A 338 3747 3765 8333 16 -19 2108 C ATOM 2632 OD1 ASP A 338 9.168 -17.152 -11.908 1.00 45.54 O ANISOU 2632 OD1 ASP A 338 4286 4237 8778 -36 46 2019 O ATOM 2633 OD2 ASP A 338 10.942 -17.085 -10.625 1.00 50.54 O1- ANISOU 2633 OD2 ASP A 338 4799 4995 9410 37 -125 2471 O1- ATOM 2634 N PRO A 339 10.118 -13.659 -12.049 1.00 29.88 N ANISOU 2634 N PRO A 339 2702 2933 5719 -43 -116 1658 N ATOM 2635 CA PRO A 339 8.679 -13.866 -12.244 1.00 32.52 C ANISOU 2635 CA PRO A 339 3082 3241 6034 -90 -42 1579 C ATOM 2636 C PRO A 339 8.167 -13.091 -13.441 1.00 24.95 C ANISOU 2636 C PRO A 339 2247 2322 4912 -114 13 1207 C ATOM 2637 O PRO A 339 8.689 -12.024 -13.735 1.00 28.31 O ANISOU 2637 O PRO A 339 2772 2894 5089 -105 -23 1070 O ATOM 2638 CB PRO A 339 8.073 -13.284 -10.966 1.00 29.74 C ANISOU 2638 CB PRO A 339 2804 3152 5344 -125 -99 1804 C ATOM 2639 CG PRO A 339 8.988 -12.139 -10.645 1.00 32.02 C ANISOU 2639 CG PRO A 339 3179 3663 5323 -115 -185 1778 C ATOM 2640 CD PRO A 339 10.370 -12.538 -11.121 1.00 29.61 C ANISOU 2640 CD PRO A 339 2771 3206 5273 -61 -216 1768 C ATOM 2641 N LEU A 340 7.153 -13.612 -14.117 1.00 27.11 N ANISOU 2641 N LEU A 340 2503 2474 5322 -152 92 1059 N ATOM 2642 CA LEU A 340 6.516 -12.885 -15.220 1.00 29.26 C ANISOU 2642 CA LEU A 340 2882 2822 5415 -189 127 744 C ATOM 2643 C LEU A 340 5.734 -11.702 -14.693 1.00 27.27 C ANISOU 2643 C LEU A 340 2761 2818 4781 -203 88 777 C ATOM 2644 O LEU A 340 5.173 -11.787 -13.601 1.00 35.64 O ANISOU 2644 O LEU A 340 3816 3953 5773 -211 75 998 O ATOM 2645 CB LEU A 340 5.520 -13.774 -15.973 1.00 36.67 C ANISOU 2645 CB LEU A 340 3752 3596 6586 -244 207 594 C ATOM 2646 CG LEU A 340 5.995 -15.069 -16.648 1.00 45.07 C ANISOU 2646 CG LEU A 340 4669 4371 8086 -253 286 486 C ATOM 2647 CD1 LEU A 340 4.913 -15.560 -17.602 1.00 52.05 C ANISOU 2647 CD1 LEU A 340 5524 5172 9079 -337 358 237 C ATOM 2648 CD2 LEU A 340 7.312 -14.897 -17.388 1.00 43.47 C ANISOU 2648 CD2 LEU A 340 4457 4126 7935 -221 300 318 C ATOM 2649 N PRO A 341 5.643 -10.611 -15.473 1.00 23.22 N ANISOU 2649 N PRO A 341 2356 2431 4035 -210 81 562 N ATOM 2650 CA PRO A 341 4.691 -9.579 -15.099 1.00 21.93 C ANISOU 2650 CA PRO A 341 2291 2453 3588 -223 70 568 C ATOM 2651 C PRO A 341 3.260 -10.085 -15.062 1.00 22.08 C ANISOU 2651 C PRO A 341 2270 2437 3680 -264 115 585 C ATOM 2652 O PRO A 341 2.935 -11.024 -15.783 1.00 26.01 O ANISOU 2652 O PRO A 341 2687 2780 4414 -296 153 491 O ATOM 2653 CB PRO A 341 4.830 -8.556 -16.213 1.00 25.55 C ANISOU 2653 CB PRO A 341 2833 2991 3885 -225 62 336 C ATOM 2654 CG PRO A 341 5.392 -9.314 -17.349 1.00 28.46 C ANISOU 2654 CG PRO A 341 3138 3215 4461 -241 92 171 C ATOM 2655 CD PRO A 341 6.335 -10.265 -16.718 1.00 25.16 C ANISOU 2655 CD PRO A 341 2628 2657 4276 -210 93 318 C ATOM 2656 N THR A 342 2.428 -9.450 -14.231 1.00 25.12 N ANISOU 2656 N THR A 342 2704 2967 3872 -269 120 685 N ATOM 2657 CA THR A 342 1.003 -9.784 -14.094 1.00 21.37 C ANISOU 2657 CA THR A 342 2188 2486 3447 -307 168 714 C ATOM 2658 C THR A 342 0.139 -8.566 -14.358 1.00 17.32 C ANISOU 2658 C THR A 342 1749 2120 2713 -307 175 600 C ATOM 2659 O THR A 342 0.579 -7.451 -14.167 1.00 21.07 O ANISOU 2659 O THR A 342 2310 2716 2980 -276 154 569 O ATOM 2660 CB THR A 342 0.677 -10.304 -12.668 1.00 29.69 C ANISOU 2660 CB THR A 342 3197 3570 4511 -319 194 986 C ATOM 2661 CG2 THR A 342 1.263 -11.685 -12.447 1.00 28.98 C ANISOU 2661 CG2 THR A 342 2995 3295 4720 -322 194 1143 C ATOM 2662 OG1 THR A 342 1.218 -9.415 -11.680 1.00 22.55 O ANISOU 2662 OG1 THR A 342 2372 2854 3343 -300 167 1086 O ATOM 2663 N SER A 343 -1.102 -8.805 -14.774 1.00 21.10 N ANISOU 2663 N SER A 343 2176 2575 3267 -342 205 547 N ATOM 2664 CA SER A 343 -2.118 -7.767 -15.026 1.00 22.31 C ANISOU 2664 CA SER A 343 2359 2846 3272 -339 215 470 C ATOM 2665 C SER A 343 -2.465 -6.983 -13.781 1.00 21.49 C ANISOU 2665 C SER A 343 2299 2872 2994 -316 262 588 C ATOM 2666 O SER A 343 -2.784 -5.803 -13.867 1.00 23.99 O ANISOU 2666 O SER A 343 2664 3286 3166 -290 272 516 O ATOM 2667 CB SER A 343 -3.421 -8.418 -15.507 1.00 27.53 C ANISOU 2667 CB SER A 343 2921 3451 4088 -392 237 434 C ATOM 2668 OG SER A 343 -3.195 -9.175 -16.669 1.00 44.90 O ANISOU 2668 OG SER A 343 5071 5545 6443 -437 205 287 O ATOM 2669 N ASP A 344 -2.474 -7.694 -12.650 1.00 21.45 N ANISOU 2669 N ASP A 344 2261 2867 3023 -336 301 770 N ATOM 2670 CA ASP A 344 -2.614 -7.139 -11.309 1.00 23.09 C ANISOU 2670 CA ASP A 344 2507 3227 3039 -337 354 891 C ATOM 2671 C ASP A 344 -1.212 -7.010 -10.774 1.00 21.66 C ANISOU 2671 C ASP A 344 2384 3099 2747 -323 301 956 C ATOM 2672 O ASP A 344 -0.567 -7.997 -10.466 1.00 25.73 O ANISOU 2672 O ASP A 344 2852 3547 3377 -334 268 1103 O ATOM 2673 CB ASP A 344 -3.446 -8.073 -10.398 1.00 22.72 C ANISOU 2673 CB ASP A 344 2376 3178 3077 -384 424 1082 C ATOM 2674 CG ASP A 344 -3.719 -7.486 -9.004 1.00 22.11 C ANISOU 2674 CG ASP A 344 2334 3302 2766 -407 500 1190 C ATOM 2675 OD1 ASP A 344 -3.006 -6.586 -8.530 1.00 24.58 O ANISOU 2675 OD1 ASP A 344 2731 3748 2860 -396 487 1147 O ATOM 2676 OD2 ASP A 344 -4.667 -7.946 -8.356 1.00 33.10 O1- ANISOU 2676 OD2 ASP A 344 3661 4726 4189 -448 583 1310 O1- ATOM 2677 N VAL A 345 -0.756 -5.774 -10.692 1.00 19.61 N ANISOU 2677 N VAL A 345 2212 2950 2289 -300 292 848 N ATOM 2678 CA VAL A 345 0.532 -5.387 -10.107 1.00 16.35 C ANISOU 2678 CA VAL A 345 1857 2628 1729 -297 240 884 C ATOM 2679 C VAL A 345 0.743 -5.918 -8.669 1.00 17.84 C ANISOU 2679 C VAL A 345 2019 2945 1812 -345 248 1108 C ATOM 2680 O VAL A 345 1.879 -6.222 -8.268 1.00 18.42 O ANISOU 2680 O VAL A 345 2088 3051 1859 -350 173 1218 O ATOM 2681 CB VAL A 345 0.640 -3.828 -10.270 1.00 17.85 C ANISOU 2681 CB VAL A 345 2133 2906 1742 -277 258 699 C ATOM 2682 CG1 VAL A 345 1.391 -3.093 -9.189 1.00 18.85 C ANISOU 2682 CG1 VAL A 345 2318 3202 1642 -306 257 710 C ATOM 2683 CG2 VAL A 345 1.190 -3.504 -11.653 1.00 18.09 C ANISOU 2683 CG2 VAL A 345 2186 2824 1864 -235 200 555 C ATOM 2684 N PHE A 346 -0.342 -6.044 -7.906 1.00 20.04 N ANISOU 2684 N PHE A 346 2271 3310 2034 -385 336 1190 N ATOM 2685 CA PHE A 346 -0.290 -6.600 -6.536 1.00 24.07 C ANISOU 2685 CA PHE A 346 2748 3975 2423 -447 353 1431 C ATOM 2686 C PHE A 346 -0.331 -8.138 -6.447 1.00 26.78 C ANISOU 2686 C PHE A 346 2982 4187 3007 -459 328 1682 C ATOM 2687 O PHE A 346 -0.188 -8.693 -5.348 1.00 27.55 O ANISOU 2687 O PHE A 346 3036 4409 3022 -512 326 1936 O ATOM 2688 CB PHE A 346 -1.414 -5.999 -5.681 1.00 26.41 C ANISOU 2688 CB PHE A 346 3059 4445 2531 -496 483 1403 C ATOM 2689 CG PHE A 346 -1.470 -4.486 -5.719 1.00 25.60 C ANISOU 2689 CG PHE A 346 3042 4439 2245 -484 533 1149 C ATOM 2690 CD1 PHE A 346 -0.417 -3.721 -5.225 1.00 25.24 C ANISOU 2690 CD1 PHE A 346 3067 4538 1986 -508 488 1084 C ATOM 2691 CD2 PHE A 346 -2.575 -3.830 -6.248 1.00 27.79 C ANISOU 2691 CD2 PHE A 346 3314 4651 2593 -452 627 980 C ATOM 2692 CE1 PHE A 346 -0.463 -2.335 -5.267 1.00 27.70 C ANISOU 2692 CE1 PHE A 346 3446 4904 2174 -501 547 840 C ATOM 2693 CE2 PHE A 346 -2.632 -2.441 -6.280 1.00 28.45 C ANISOU 2693 CE2 PHE A 346 3457 4789 2564 -434 684 761 C ATOM 2694 CZ PHE A 346 -1.575 -1.692 -5.791 1.00 26.08 C ANISOU 2694 CZ PHE A 346 3231 4610 2068 -460 651 683 C ATOM 2695 N ALA A 347 -0.542 -8.806 -7.589 1.00 30.68 N ANISOU 2695 N ALA A 347 3423 4438 3796 -421 315 1612 N ATOM 2696 CA ALA A 347 -0.384 -10.265 -7.753 1.00 40.83 C ANISOU 2696 CA ALA A 347 4594 5528 5391 -424 292 1796 C ATOM 2697 C ALA A 347 -1.311 -11.098 -6.857 1.00 54.90 C ANISOU 2697 C ALA A 347 6290 7334 7235 -481 366 2043 C ATOM 2698 O ALA A 347 -0.901 -12.119 -6.300 1.00 59.07 O ANISOU 2698 O ALA A 347 6729 7808 7909 -499 340 2316 O ATOM 2699 CB ALA A 347 1.076 -10.660 -7.530 1.00 43.66 C ANISOU 2699 CB ALA A 347 4929 5863 5796 -402 192 1935 C ATOM 2700 N GLY A 348 -2.553 -10.642 -6.697 1.00 67.10 N ANISOU 2700 N GLY A 348 7849 8964 8683 -510 463 1964 N ATOM 2701 CA GLY A 348 -3.506 -11.273 -5.776 1.00 57.80 C ANISOU 2701 CA GLY A 348 6594 7848 7520 -574 554 2188 C ATOM 2702 C GLY A 348 -3.258 -11.089 -4.276 1.00 60.43 C ANISOU 2702 C GLY A 348 6946 8462 7552 -634 576 2422 C ATOM 2703 O GLY A 348 -4.092 -11.508 -3.474 1.00 66.50 O ANISOU 2703 O GLY A 348 7656 9322 8290 -698 668 2605 O ATOM 2704 N CYS A 349 -2.136 -10.468 -3.890 1.00 52.92 N ANISOU 2704 N CYS A 349 6070 7668 6369 -628 494 2414 N ATOM 2705 CA CYS A 349 -1.796 -10.232 -2.477 1.00 54.99 C ANISOU 2705 CA CYS A 349 6352 8245 6298 -706 495 2614 C ATOM 2706 C CYS A 349 -2.596 -9.032 -1.954 1.00 62.97 C ANISOU 2706 C CYS A 349 7444 9490 6990 -751 620 2408 C ATOM 2707 O CYS A 349 -3.020 -8.176 -2.744 1.00 54.07 O ANISOU 2707 O CYS A 349 6374 8278 5893 -699 663 2105 O ATOM 2708 CB CYS A 349 -0.288 -9.960 -2.312 1.00 46.57 C ANISOU 2708 CB CYS A 349 5322 7264 5106 -692 352 2650 C ATOM 2709 SG CYS A 349 0.808 -11.125 -3.166 1.00 48.55 S ANISOU 2709 SG CYS A 349 5475 7197 5775 -612 218 2795 S ATOM 2710 N GLN A 350 -2.802 -8.975 -0.634 1.00 65.33 N ANISOU 2710 N GLN A 350 7739 10087 6997 -852 683 2576 N ATOM 2711 CA GLN A 350 -3.483 -7.838 0.014 1.00 56.94 C ANISOU 2711 CA GLN A 350 6744 9272 5619 -911 825 2367 C ATOM 2712 C GLN A 350 -2.715 -6.523 -0.234 1.00 60.40 C ANISOU 2712 C GLN A 350 7294 9779 5875 -885 783 2059 C ATOM 2713 O GLN A 350 -1.484 -6.533 -0.317 1.00 53.53 O ANISOU 2713 O GLN A 350 6450 8921 4969 -872 637 2104 O ATOM 2714 CB GLN A 350 -3.643 -8.090 1.517 1.00 54.55 C ANISOU 2714 CB GLN A 350 6413 9317 4996 -1046 891 2613 C ATOM 2715 CG GLN A 350 -4.602 -9.195 1.854 0.00 61.29 C ANISOU 2715 CG GLN A 350 7155 10126 6005 -1086 978 2896 C ATOM 2716 CD GLN A 350 -4.884 -9.299 3.342 0.00 64.25 C ANISOU 2716 CD GLN A 350 7507 10889 6017 -1233 1072 3118 C ATOM 2717 NE2 GLN A 350 -6.091 -9.734 3.683 0.00 65.60 N ANISOU 2717 NE2 GLN A 350 7605 11076 6244 -1281 1231 3222 N ATOM 2718 OE1 GLN A 350 -4.028 -8.998 4.176 0.00 65.47 O ANISOU 2718 OE1 GLN A 350 7701 11342 5834 -1314 1001 3198 O ATOM 2719 N ILE A 351 -3.454 -5.418 -0.392 1.00 58.78 N ANISOU 2719 N ILE A 351 7139 9594 5600 -873 914 1755 N ATOM 2720 CA ILE A 351 -2.883 -4.079 -0.654 1.00 46.37 C ANISOU 2720 CA ILE A 351 5662 8054 3903 -848 904 1444 C ATOM 2721 C ILE A 351 -2.653 -3.376 0.698 1.00 49.62 C ANISOU 2721 C ILE A 351 6119 8830 3907 -977 980 1382 C ATOM 2722 O ILE A 351 -3.628 -3.066 1.393 1.00 47.80 O ANISOU 2722 O ILE A 351 5872 8751 3541 -1042 1158 1311 O ATOM 2723 CB ILE A 351 -3.829 -3.208 -1.523 1.00 40.42 C ANISOU 2723 CB ILE A 351 4917 7118 3324 -768 1014 1158 C ATOM 2724 CG1 ILE A 351 -4.091 -3.849 -2.891 1.00 38.60 C ANISOU 2724 CG1 ILE A 351 4639 6572 3454 -664 934 1194 C ATOM 2725 CG2 ILE A 351 -3.240 -1.831 -1.755 1.00 39.28 C ANISOU 2725 CG2 ILE A 351 4855 6986 3084 -746 1015 866 C ATOM 2726 CD1 ILE A 351 -5.277 -3.262 -3.632 1.00 32.71 C ANISOU 2726 CD1 ILE A 351 3859 5682 2886 -603 1037 1007 C ATOM 2727 N PRO A 352 -1.375 -3.125 1.078 1.00 44.18 N ANISOU 2727 N PRO A 352 5475 8293 3017 -1023 852 1395 N ATOM 2728 CA PRO A 352 -1.088 -2.521 2.381 1.00 50.33 C ANISOU 2728 CA PRO A 352 6289 9454 3380 -1171 907 1332 C ATOM 2729 C PRO A 352 -1.086 -0.986 2.375 1.00 49.12 C ANISOU 2729 C PRO A 352 6212 9341 3111 -1187 1016 911 C ATOM 2730 O PRO A 352 -1.000 -0.365 3.443 1.00 44.36 O ANISOU 2730 O PRO A 352 5636 9053 2166 -1323 1102 779 O ATOM 2731 CB PRO A 352 0.309 -3.055 2.688 1.00 50.70 C ANISOU 2731 CB PRO A 352 6326 9624 3314 -1210 693 1566 C ATOM 2732 CG PRO A 352 0.961 -3.146 1.351 1.00 44.71 C ANISOU 2732 CG PRO A 352 5576 8518 2895 -1066 562 1521 C ATOM 2733 CD PRO A 352 -0.126 -3.431 0.351 1.00 41.90 C ANISOU 2733 CD PRO A 352 5194 7850 2875 -955 652 1470 C ATOM 2734 N TYR A 353 -1.210 -0.388 1.190 1.00 45.39 N ANISOU 2734 N TYR A 353 5762 8555 2927 -1058 1021 703 N ATOM 2735 CA TYR A 353 -1.056 1.054 1.025 1.00 41.55 C ANISOU 2735 CA TYR A 353 5334 8041 2412 -1054 1102 333 C ATOM 2736 C TYR A 353 -2.335 1.730 1.471 1.00 35.95 C ANISOU 2736 C TYR A 353 4603 7380 1675 -1084 1350 122 C ATOM 2737 O TYR A 353 -3.413 1.281 1.105 1.00 33.20 O ANISOU 2737 O TYR A 353 4197 6893 1523 -1020 1430 204 O ATOM 2738 CB TYR A 353 -0.737 1.411 -0.437 1.00 43.48 C ANISOU 2738 CB TYR A 353 5596 7938 2985 -906 1013 237 C ATOM 2739 CG TYR A 353 0.417 0.606 -0.965 1.00 39.48 C ANISOU 2739 CG TYR A 353 5091 7355 2553 -867 794 450 C ATOM 2740 CD1 TYR A 353 1.713 0.845 -0.519 1.00 38.64 C ANISOU 2740 CD1 TYR A 353 5018 7408 2256 -935 674 445 C ATOM 2741 CD2 TYR A 353 0.208 -0.441 -1.856 1.00 38.51 C ANISOU 2741 CD2 TYR A 353 4922 7012 2699 -773 712 653 C ATOM 2742 CE1 TYR A 353 2.775 0.087 -0.980 1.00 36.21 C ANISOU 2742 CE1 TYR A 353 4691 7022 2045 -894 483 646 C ATOM 2743 CE2 TYR A 353 1.262 -1.207 -2.321 1.00 39.78 C ANISOU 2743 CE2 TYR A 353 5069 7089 2958 -737 535 830 C ATOM 2744 CZ TYR A 353 2.540 -0.938 -1.879 1.00 35.76 C ANISOU 2744 CZ TYR A 353 4586 6725 2275 -792 424 834 C ATOM 2745 OH TYR A 353 3.567 -1.715 -2.321 1.00 26.52 O ANISOU 2745 OH TYR A 353 3381 5462 1232 -751 260 1015 O ATOM 2746 N PRO A 354 -2.225 2.801 2.275 1.00 39.65 N ANISOU 2746 N PRO A 354 5107 8046 1913 -1188 1479 -164 N ATOM 2747 CA PRO A 354 -3.450 3.483 2.710 1.00 38.62 C ANISOU 2747 CA PRO A 354 4941 7945 1788 -1215 1744 -396 C ATOM 2748 C PRO A 354 -4.210 4.146 1.554 1.00 39.73 C ANISOU 2748 C PRO A 354 5045 7715 2336 -1055 1822 -555 C ATOM 2749 O PRO A 354 -3.613 4.521 0.524 1.00 40.29 O ANISOU 2749 O PRO A 354 5142 7547 2619 -952 1696 -595 O ATOM 2750 CB PRO A 354 -2.938 4.542 3.688 1.00 40.83 C ANISOU 2750 CB PRO A 354 5267 8484 1763 -1363 1848 -710 C ATOM 2751 CG PRO A 354 -1.520 4.785 3.293 1.00 42.13 C ANISOU 2751 CG PRO A 354 5491 8611 1906 -1356 1636 -720 C ATOM 2752 CD PRO A 354 -1.006 3.476 2.772 1.00 41.84 C ANISOU 2752 CD PRO A 354 5444 8506 1946 -1287 1401 -318 C ATOM 2753 N LYS A 355 -5.519 4.266 1.738 1.00 39.16 N ANISOU 2753 N LYS A 355 4899 7612 2367 -1040 2027 -622 N ATOM 2754 CA LYS A 355 -6.397 4.965 0.807 1.00 44.32 C ANISOU 2754 CA LYS A 355 5488 7954 3398 -903 2125 -767 C ATOM 2755 C LYS A 355 -6.091 6.473 0.845 1.00 46.76 C ANISOU 2755 C LYS A 355 5817 8191 3759 -906 2240 -1132 C ATOM 2756 O LYS A 355 -5.442 6.961 1.775 1.00 52.41 O ANISOU 2756 O LYS A 355 6588 9136 4191 -1038 2296 -1316 O ATOM 2757 CB LYS A 355 -7.883 4.714 1.168 1.00 49.40 C ANISOU 2757 CB LYS A 355 6026 8616 4127 -903 2333 -750 C ATOM 2758 CG LYS A 355 -8.375 3.271 1.020 1.00 43.10 C ANISOU 2758 CG LYS A 355 5183 7829 3363 -890 2244 -400 C ATOM 2759 CD LYS A 355 -9.848 3.151 1.287 0.00 47.84 C ANISOU 2759 CD LYS A 355 5666 8421 4089 -885 2456 -407 C ATOM 2760 CE LYS A 355 -10.327 1.715 1.149 0.00 47.27 C ANISOU 2760 CE LYS A 355 5540 8347 4073 -885 2372 -65 C ATOM 2761 NZ LYS A 355 -11.783 1.581 1.432 0.00 48.83 N1+ ANISOU 2761 NZ LYS A 355 5610 8543 4400 -888 2584 -65 N1+ ATOM 2762 N ARG A 356 -6.579 7.205 -0.154 1.00 48.81 N ANISOU 2762 N ARG A 356 6019 8138 4388 -768 2277 -1229 N ATOM 2763 CA ARG A 356 -6.318 8.651 -0.263 1.00 47.94 C ANISOU 2763 CA ARG A 356 5907 7890 4417 -751 2386 -1547 C ATOM 2764 C ARG A 356 -7.008 9.400 0.867 1.00 50.08 C ANISOU 2764 C ARG A 356 6128 8298 4601 -850 2687 -1853 C ATOM 2765 O ARG A 356 -8.191 9.169 1.138 1.00 43.84 O ANISOU 2765 O ARG A 356 5247 7521 3892 -835 2852 -1836 O ATOM 2766 CB ARG A 356 -6.820 9.226 -1.597 1.00 47.11 C ANISOU 2766 CB ARG A 356 5724 7420 4756 -577 2363 -1528 C ATOM 2767 CG ARG A 356 -6.311 8.503 -2.830 1.00 43.56 C ANISOU 2767 CG ARG A 356 5307 6832 4410 -482 2092 -1248 C ATOM 2768 CD ARG A 356 -6.648 9.247 -4.118 1.00 38.77 C ANISOU 2768 CD ARG A 356 4629 5912 4190 -336 2061 -1244 C ATOM 2769 NE ARG A 356 -6.102 8.531 -5.268 1.00 24.11 N ANISOU 2769 NE ARG A 356 2810 3969 2381 -270 1812 -1003 N ATOM 2770 CZ ARG A 356 -4.817 8.513 -5.594 1.00 23.18 C ANISOU 2770 CZ ARG A 356 2790 3862 2157 -289 1653 -981 C ATOM 2771 NH1 ARG A 356 -3.922 9.205 -4.890 1.00 26.33 N1+ ANISOU 2771 NH1 ARG A 356 3256 4348 2402 -371 1698 -1174 N1+ ATOM 2772 NH2 ARG A 356 -4.415 7.818 -6.652 1.00 24.93 N ANISOU 2772 NH2 ARG A 356 3031 4008 2432 -233 1454 -780 N ATOM 2773 N GLU A 357 -6.263 10.282 1.525 1.00 51.92 N ANISOU 2773 N GLU A 357 6413 8640 4675 -958 2765 -2147 N ATOM 2774 CA GLU A 357 -6.858 11.214 2.478 1.00 58.94 C ANISOU 2774 CA GLU A 357 7245 9611 5536 -1051 3077 -2520 C ATOM 2775 C GLU A 357 -7.542 12.337 1.691 1.00 53.93 C ANISOU 2775 C GLU A 357 6499 8582 5410 -902 3225 -2695 C ATOM 2776 O GLU A 357 -7.023 12.785 0.670 1.00 59.14 O ANISOU 2776 O GLU A 357 7167 8976 6328 -791 3081 -2641 O ATOM 2777 CB GLU A 357 -5.794 11.791 3.439 1.00 68.42 C ANISOU 2777 CB GLU A 357 8533 11070 6395 -1238 3108 -2804 C ATOM 2778 CG GLU A 357 -5.415 10.876 4.604 1.00 69.50 C ANISOU 2778 CG GLU A 357 8739 11677 5992 -1429 3058 -2698 C ATOM 2779 CD GLU A 357 -6.456 10.866 5.715 1.00 83.58 C ANISOU 2779 CD GLU A 357 10461 13707 7589 -1548 3351 -2863 C ATOM 2780 OE1 GLU A 357 -6.563 11.872 6.456 1.00 91.38 O ANISOU 2780 OE1 GLU A 357 11426 14782 8513 -1664 3598 -3286 O ATOM 2781 OE2 GLU A 357 -7.163 9.847 5.861 1.00 83.77 O1- ANISOU 2781 OE2 GLU A 357 10454 13840 7534 -1535 3346 -2582 O1- ATOM 2782 N PHE A 358 -8.709 12.768 2.163 1.00 60.66 N ANISOU 2782 N PHE A 358 7234 9401 6413 -900 3512 -2883 N ATOM 2783 CA PHE A 358 -9.370 13.985 1.663 1.00 60.61 C ANISOU 2783 CA PHE A 358 7093 9036 6900 -780 3704 -3100 C ATOM 2784 C PHE A 358 -8.678 15.244 2.184 1.00 69.67 C ANISOU 2784 C PHE A 358 8261 10151 8060 -876 3858 -3522 C ATOM 2785 O PHE A 358 -7.919 15.180 3.155 1.00 84.28 O ANISOU 2785 O PHE A 358 10215 12319 9490 -1064 3872 -3700 O ATOM 2786 CB PHE A 358 -10.838 14.027 2.088 1.00 59.11 C ANISOU 2786 CB PHE A 358 6750 8826 6882 -754 3985 -3185 C ATOM 2787 CG PHE A 358 -11.653 12.863 1.599 1.00 57.39 C ANISOU 2787 CG PHE A 358 6484 8620 6702 -667 3865 -2803 C ATOM 2788 CD1 PHE A 358 -11.665 12.522 0.252 1.00 49.22 C ANISOU 2788 CD1 PHE A 358 5428 7341 5934 -504 3614 -2485 C ATOM 2789 CD2 PHE A 358 -12.434 12.121 2.482 1.00 63.23 C ANISOU 2789 CD2 PHE A 358 7191 9621 7214 -759 4013 -2771 C ATOM 2790 CE1 PHE A 358 -12.420 11.456 -0.203 1.00 48.48 C ANISOU 2790 CE1 PHE A 358 5280 7257 5884 -441 3507 -2166 C ATOM 2791 CE2 PHE A 358 -13.197 11.049 2.029 1.00 60.19 C ANISOU 2791 CE2 PHE A 358 6749 9227 6894 -687 3909 -2427 C ATOM 2792 CZ PHE A 358 -13.189 10.716 0.684 1.00 55.23 C ANISOU 2792 CZ PHE A 358 6099 8346 6541 -529 3654 -2137 C ATOM 2793 N LEU A 359 -8.949 16.385 1.546 1.00 71.19 N ANISOU 2793 N LEU A 359 8343 9963 8744 -755 3972 -3673 N ATOM 2794 CA LEU A 359 -8.360 17.680 1.946 1.00 80.31 C ANISOU 2794 CA LEU A 359 9490 11010 10014 -834 4142 -4093 C ATOM 2795 C LEU A 359 -9.353 18.582 2.699 1.00 72.85 C ANISOU 2795 C LEU A 359 8395 9977 9310 -867 4549 -4498 C ATOM 2796 O LEU A 359 -10.245 19.190 2.109 1.00 66.54 O ANISOU 2796 O LEU A 359 7427 8823 9032 -707 4687 -4493 O ATOM 2797 CB LEU A 359 -7.773 18.411 0.725 1.00 78.28 C ANISOU 2797 CB LEU A 359 9212 10370 10160 -692 3988 -3990 C ATOM 2798 CG LEU A 359 -6.837 17.637 -0.217 1.00 67.14 C ANISOU 2798 CG LEU A 359 7925 8985 8602 -636 3607 -3602 C ATOM 2799 CD1 LEU A 359 -6.102 18.611 -1.130 1.00 68.23 C ANISOU 2799 CD1 LEU A 359 8047 8795 9084 -555 3525 -3617 C ATOM 2800 CD2 LEU A 359 -5.828 16.763 0.513 1.00 68.63 C ANISOU 2800 CD2 LEU A 359 8282 9579 8214 -807 3442 -3570 C TER HETATM 2801 C1 C1I A1360 2.219 17.791 -2.715 1.00 58.72 C HETATM 2802 N2 C1I A1360 2.814 16.463 -2.538 1.00 61.20 N HETATM 2803 C3 C1I A1360 2.275 15.857 -1.319 1.00 56.81 C HETATM 2804 C4 C1I A1360 2.576 15.607 -3.704 1.00 58.33 C HETATM 2805 C6 C1I A1360 1.077 15.447 -3.875 1.00 58.16 C HETATM 2806 C7 C1I A1360 0.693 14.622 -5.096 1.00 55.61 C HETATM 2807 C8 C1I A1360 0.740 13.106 -4.880 1.00 53.37 C HETATM 2808 C9 C1I A1360 -0.363 12.607 -5.857 1.00 51.78 C HETATM 2809 C10 C1I A1360 -1.068 13.874 -6.371 1.00 50.40 C HETATM 2810 O11 C1I A1360 -0.700 14.881 -5.410 1.00 55.78 O HETATM 2811 C12 C1I A1360 -0.406 14.324 -7.677 1.00 50.38 C HETATM 2812 C13 C1I A1360 0.962 14.790 -7.534 1.00 50.76 C HETATM 2813 C14 C1I A1360 1.535 14.960 -6.307 1.00 53.74 C HETATM 2814 C15 C1I A1360 2.953 15.428 -6.181 1.00 56.95 C HETATM 2815 O17 C1I A1360 3.290 16.212 -7.318 1.00 57.06 O HETATM 2816 C18 C1I A1360 3.168 16.279 -4.940 1.00 59.42 C HETATM 2817 O20 C1I A1360 4.566 16.447 -4.747 1.00 63.53 O HETATM 2818 C21 C1I A1360 -1.028 14.305 -8.830 1.00 47.12 C HETATM 2819 C22 C1I A1360 -2.445 13.841 -9.008 1.00 45.18 C HETATM 2820 C23 C1I A1360 -2.967 13.074 -7.818 1.00 46.47 C HETATM 2821 C24 C1I A1360 -2.447 11.639 -7.852 1.00 45.98 C HETATM 2822 C25 C1I A1360 -4.465 13.078 -7.571 1.00 46.41 C HETATM 2823 C26 C1I A1360 -4.588 12.511 -6.140 1.00 45.08 C HETATM 2824 C27 C1I A1360 -3.275 12.925 -5.436 1.00 46.17 C HETATM 2825 C28 C1I A1360 -2.566 13.778 -6.494 1.00 48.05 C HETATM 2826 C29 C1I A1360 -5.274 12.320 -8.592 1.00 45.90 C HETATM 2827 C30 C1I A1360 -5.929 11.176 -8.271 1.00 45.23 C HETATM 2828 C31 C1I A1360 -6.685 10.521 -9.246 1.00 46.57 C HETATM 2829 C32 C1I A1360 -7.378 9.334 -8.988 1.00 47.01 C HETATM 2830 N33 C1I A1360 -8.075 8.765 -9.933 1.00 47.24 N HETATM 2831 C34 C1I A1360 -8.160 9.249 -11.152 1.00 45.48 C HETATM 2832 C35 C1I A1360 -7.528 10.394 -11.498 1.00 45.86 C HETATM 2833 C36 C1I A1360 -6.764 11.068 -10.542 1.00 44.29 C HETATM 2834 C37 C1I A1360 -6.086 12.251 -10.834 1.00 46.06 C HETATM 2835 C38 C1I A1360 -5.363 12.856 -9.865 1.00 42.75 C HETATM 2836 C FMT A1361 6.561 -10.735 -5.914 1.00 67.97 C HETATM 2837 O1 FMT A1361 7.781 -10.707 -6.014 1.00 59.88 O HETATM 2838 O2 FMT A1361 5.889 -9.585 -5.901 1.00 59.21 O HETATM 2839 C FMT A1362 -8.062 -0.350 -2.055 1.00 78.50 C HETATM 2840 O1 FMT A1362 -6.872 -0.541 -2.281 1.00 56.67 O HETATM 2841 O2 FMT A1362 -8.852 0.104 -3.036 1.00 59.91 O HETATM 2842 C FMT A1363 -6.260 12.802 -16.185 1.00 55.77 C HETATM 2843 O1 FMT A1363 -5.904 13.309 -15.124 1.00 52.55 O HETATM 2844 O2 FMT A1363 -5.617 13.116 -17.318 1.00 45.36 O HETATM 2845 O HOH A2001 -37.956 23.667 -26.870 1.00 39.47 O HETATM 2846 O HOH A2002 -32.348 17.128 -16.863 1.00 56.53 O HETATM 2847 O HOH A2003 -25.705 17.445 -22.002 1.00 46.78 O HETATM 2848 O HOH A2004 -23.057 18.682 -19.734 1.00 42.76 O HETATM 2849 O HOH A2005 -22.027 20.710 -15.009 1.00 37.81 O HETATM 2850 O HOH A2006 -21.714 17.779 -4.378 1.00 49.43 O HETATM 2851 O HOH A2007 -13.234 22.749 -3.206 1.00 55.68 O HETATM 2852 O HOH A2008 -14.781 23.097 -7.705 1.00 54.48 O HETATM 2853 O HOH A2009 -21.307 5.954 -7.555 1.00 58.27 O HETATM 2854 O HOH A2010 11.531 6.342 -28.136 1.00 42.50 O HETATM 2855 O HOH A2011 10.000 14.704 -18.878 1.00 34.76 O HETATM 2856 O HOH A2012 -11.073 25.319 -12.106 1.00 53.53 O HETATM 2857 O HOH A2013 -12.416 24.457 -16.093 1.00 43.74 O HETATM 2858 O HOH A2014 -10.827 25.073 -18.520 1.00 45.74 O HETATM 2859 O HOH A2015 -12.736 29.397 -24.176 1.00 45.25 O HETATM 2860 O HOH A2016 -11.296 14.238 -30.597 1.00 31.33 O HETATM 2861 O HOH A2017 -8.983 8.178 -22.811 1.00 51.61 O HETATM 2862 O HOH A2018 -13.113 7.137 -29.581 1.00 45.12 O HETATM 2863 O HOH A2019 -15.864 6.905 -30.354 1.00 56.28 O HETATM 2864 O HOH A2020 -11.487 11.140 -34.552 1.00 26.16 O HETATM 2865 O HOH A2021 -8.422 8.807 -33.232 1.00 34.32 O HETATM 2866 O HOH A2022 -7.710 4.606 -22.517 1.00 32.46 O HETATM 2867 O HOH A2023 -8.268 2.552 -19.188 1.00 31.91 O HETATM 2868 O HOH A2024 -9.440 4.687 -16.330 1.00 35.09 O HETATM 2869 O HOH A2025 -21.245 30.292 -21.824 1.00 55.06 O HETATM 2870 O HOH A2026 -8.750 5.213 -13.512 1.00 32.75 O HETATM 2871 O HOH A2027 -10.931 2.355 -16.294 1.00 50.00 O HETATM 2872 O HOH A2028 -13.348 0.045 -13.567 1.00 45.92 O HETATM 2873 O HOH A2029 -9.334 2.434 -7.818 1.00 29.72 O HETATM 2874 O HOH A2030 -1.113 4.892 -3.099 1.00 38.46 O HETATM 2875 O HOH A2031 8.276 14.271 -5.333 1.00 34.75 O HETATM 2876 O HOH A2032 12.395 -7.010 -10.574 1.00 43.44 O HETATM 2877 O HOH A2033 13.231 -11.176 -12.907 1.00 40.17 O HETATM 2878 O HOH A2034 8.940 4.686 -27.627 1.00 31.22 O HETATM 2879 O HOH A2035 1.594 14.984 -28.324 1.00 47.32 O HETATM 2880 O HOH A2036 2.118 20.643 -29.026 1.00 52.74 O HETATM 2881 O HOH A2037 8.097 13.155 -19.832 1.00 43.48 O HETATM 2882 O HOH A2038 6.032 12.126 -8.944 1.00 38.51 O HETATM 2883 O HOH A2039 -10.519 -1.688 -9.887 1.00 43.96 O HETATM 2884 O HOH A2040 -10.827 -6.645 -6.401 1.00 46.88 O HETATM 2885 O HOH A2041 -6.874 -6.636 -12.819 1.00 44.27 O HETATM 2886 O HOH A2042 11.079 16.176 -13.817 1.00 41.12 O HETATM 2887 O HOH A2043 15.076 11.009 -10.513 1.00 36.61 O HETATM 2888 O HOH A2044 12.528 13.354 -19.436 1.00 29.50 O HETATM 2889 O HOH A2045 8.398 11.855 -7.485 1.00 37.55 O HETATM 2890 O HOH A2046 15.343 13.948 -26.975 1.00 31.75 O HETATM 2891 O HOH A2047 8.453 13.902 -24.179 1.00 43.71 O HETATM 2892 O HOH A2048 10.260 11.417 -31.103 1.00 33.08 O HETATM 2893 O HOH A2049 12.936 10.259 -29.653 1.00 39.01 O HETATM 2894 O HOH A2050 13.703 8.608 -10.111 1.00 33.85 O HETATM 2895 O HOH A2051 17.324 5.240 -7.596 1.00 51.47 O HETATM 2896 O HOH A2052 27.966 6.855 -9.514 1.00 35.45 O HETATM 2897 O HOH A2053 27.793 9.092 -18.916 1.00 50.41 O HETATM 2898 O HOH A2054 27.191 5.030 -16.368 1.00 29.00 O HETATM 2899 O HOH A2055 24.852 7.788 -24.464 1.00 36.81 O HETATM 2900 O HOH A2056 24.673 11.815 -31.223 1.00 40.24 O HETATM 2901 O HOH A2057 35.526 23.918 -17.039 1.00 65.89 O HETATM 2902 O HOH A2058 33.703 19.937 -12.831 1.00 45.63 O HETATM 2903 O HOH A2059 31.217 20.070 -10.865 1.00 41.04 O HETATM 2904 O HOH A2060 27.689 6.421 -6.549 1.00 45.99 O HETATM 2905 O HOH A2061 16.566 -8.940 -13.098 1.00 42.30 O HETATM 2906 O HOH A2062 18.114 -7.234 -19.762 1.00 32.87 O HETATM 2907 O HOH A2063 23.704 4.528 -19.952 1.00 41.61 O HETATM 2908 O HOH A2064 20.134 1.780 -25.127 1.00 33.72 O HETATM 2909 O HOH A2065 25.093 6.797 -21.662 1.00 34.92 O HETATM 2910 O HOH A2066 15.749 6.888 -28.667 1.00 39.13 O HETATM 2911 O HOH A2067 15.381 -4.943 -25.132 1.00 40.81 O HETATM 2912 O HOH A2068 -1.805 -11.917 -14.617 1.00 55.68 O HETATM 2913 O HOH A2069 -3.392 -10.779 -12.314 1.00 44.20 O HETATM 2914 O HOH A2070 3.953 -8.050 -4.073 1.00 46.51 O CONECT 2801 2802 CONECT 2802 2801 2803 2804 CONECT 2803 2802 CONECT 2804 2802 2805 2816 CONECT 2805 2804 2806 CONECT 2806 2805 2807 2810 2813 CONECT 2807 2806 2808 CONECT 2808 2807 2809 CONECT 2809 2808 2810 2811 2825 CONECT 2810 2806 2809 CONECT 2811 2809 2812 2818 CONECT 2812 2811 2813 CONECT 2813 2806 2812 2814 CONECT 2814 2813 2815 2816 CONECT 2815 2814 CONECT 2816 2804 2814 2817 CONECT 2817 2816 CONECT 2818 2811 2819 CONECT 2819 2818 2820 CONECT 2820 2819 2821 2822 2825 CONECT 2821 2820 CONECT 2822 2820 2823 2826 CONECT 2823 2822 2824 CONECT 2824 2823 2825 CONECT 2825 2809 2820 2824 CONECT 2826 2822 2827 2835 CONECT 2827 2826 2828 CONECT 2828 2827 2829 2833 CONECT 2829 2828 2830 CONECT 2830 2829 2831 CONECT 2831 2830 2832 CONECT 2832 2831 2833 CONECT 2833 2828 2832 2834 CONECT 2834 2833 2835 CONECT 2835 2826 2834 CONECT 2836 2837 2838 CONECT 2837 2836 CONECT 2838 2836 CONECT 2839 2840 2841 CONECT 2840 2839 CONECT 2841 2839 CONECT 2842 2843 2844 CONECT 2843 2842 CONECT 2844 2842 END If you find results from this site helpful for your research, please cite one of our papers:
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