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*** ***elNémo ID: 2402181553163324914Job options:ID = 2402181553163324914 JOBID = USERID = unknown PRIVAT = 0 NMODES = 10 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = -1 CUTOFF = 10 CAONLY = 0 Input data for this run:ATOM 1 N SER A 96 12.070 -18.414 32.222 1.00 29.94 N ANISOU 1 N SER A 96 3771 3012 4595 1574 -245 1007 N ATOM 2 CA SER A 96 12.232 -17.060 32.737 1.00 29.62 C ANISOU 2 CA SER A 96 3702 2999 4553 1218 -36 918 C ATOM 3 C SER A 96 11.093 -16.151 32.284 1.00 28.29 C ANISOU 3 C SER A 96 3743 2738 4269 652 312 663 C ATOM 4 O SER A 96 11.200 -15.463 31.262 1.00 28.77 O ANISOU 4 O SER A 96 3881 2675 4376 467 529 848 O ATOM 5 CB SER A 96 13.569 -16.479 32.286 1.00 30.60 C ANISOU 5 CB SER A 96 3640 3285 4702 1156 -4 1050 C ATOM 6 OG SER A 96 14.587 -17.457 32.375 1.00 32.71 O ANISOU 6 OG SER A 96 3939 3666 4822 921 -7 1117 O ATOM 7 N VAL A 97 9.999 -16.163 33.042 1.00 25.05 N ANISOU 7 N VAL A 97 3345 2491 3683 322 533 318 N ATOM 8 CA VAL A 97 8.881 -15.263 32.797 1.00 22.33 C ANISOU 8 CA VAL A 97 3026 2232 3225 59 619 22 C ATOM 9 C VAL A 97 8.449 -14.636 34.118 1.00 22.07 C ANISOU 9 C VAL A 97 2813 2482 3089 -233 380 -168 C ATOM 10 O VAL A 97 8.244 -15.348 35.106 1.00 22.30 O ANISOU 10 O VAL A 97 2756 2565 3154 -503 500 -345 O ATOM 11 CB VAL A 97 7.680 -15.985 32.135 1.00 22.67 C ANISOU 11 CB VAL A 97 3289 2127 3199 -44 824 -59 C ATOM 12 CG1 VAL A 97 6.554 -15.011 31.889 1.00 23.20 C ANISOU 12 CG1 VAL A 97 3360 2288 3169 -291 796 79 C ATOM 13 CG2 VAL A 97 8.081 -16.622 30.821 1.00 23.30 C ANISOU 13 CG2 VAL A 97 3570 2082 3200 -143 512 -279 C ATOM 14 N PRO A 98 8.330 -13.298 34.149 1.00 21.23 N ANISOU 14 N PRO A 98 2685 2543 2837 -137 390 -351 N ATOM 15 CA PRO A 98 7.876 -12.600 35.357 1.00 21.08 C ANISOU 15 CA PRO A 98 2584 2655 2769 57 645 -444 C ATOM 16 C PRO A 98 6.452 -13.003 35.738 1.00 21.56 C ANISOU 16 C PRO A 98 2609 2884 2699 -16 641 -482 C ATOM 17 O PRO A 98 5.643 -13.267 34.850 1.00 21.69 O ANISOU 17 O PRO A 98 2588 3051 2605 -173 648 -767 O ATOM 18 CB PRO A 98 7.896 -11.129 34.934 1.00 20.94 C ANISOU 18 CB PRO A 98 2538 2586 2832 136 751 -373 C ATOM 19 CG PRO A 98 8.875 -11.070 33.805 1.00 21.89 C ANISOU 19 CG PRO A 98 2797 2655 2864 172 470 -408 C ATOM 20 CD PRO A 98 8.699 -12.360 33.074 1.00 20.58 C ANISOU 20 CD PRO A 98 2630 2440 2748 -1 457 -479 C ATOM 21 N SER A 99 6.148 -13.054 37.033 1.00 21.89 N ANISOU 21 N SER A 99 2733 2807 2779 26 687 -216 N ATOM 22 CA SER A 99 4.789 -13.355 37.474 1.00 21.93 C ANISOU 22 CA SER A 99 2885 2693 2757 -3 857 13 C ATOM 23 C SER A 99 3.836 -12.237 37.051 1.00 21.54 C ANISOU 23 C SER A 99 2910 2535 2740 30 990 16 C ATOM 24 O SER A 99 4.208 -11.067 37.048 1.00 20.85 O ANISOU 24 O SER A 99 3001 2202 2720 -22 1017 -87 O ATOM 25 CB SER A 99 4.736 -13.545 38.993 1.00 22.70 C ANISOU 25 CB SER A 99 2952 2902 2770 5 838 175 C ATOM 26 OG SER A 99 3.406 -13.727 39.447 1.00 23.34 O ANISOU 26 OG SER A 99 3097 2946 2827 141 927 232 O ATOM 27 N GLN A 100 2.613 -12.603 36.681 1.00 22.28 N ANISOU 27 N GLN A 100 2971 2746 2747 8 860 40 N ATOM 28 CA GLN A 100 1.595 -11.608 36.364 1.00 24.12 C ANISOU 28 CA GLN A 100 3170 3111 2882 -177 607 151 C ATOM 29 C GLN A 100 0.409 -11.721 37.321 1.00 22.54 C ANISOU 29 C GLN A 100 2800 2992 2773 -312 472 160 C ATOM 30 O GLN A 100 -0.680 -11.208 37.053 1.00 22.09 O ANISOU 30 O GLN A 100 2493 3159 2743 -269 247 344 O ATOM 31 CB GLN A 100 1.135 -11.760 34.916 1.00 27.78 C ANISOU 31 CB GLN A 100 3813 3514 3228 -231 511 97 C ATOM 32 CG GLN A 100 0.429 -13.072 34.621 1.00 30.85 C ANISOU 32 CG GLN A 100 4351 3896 3476 -123 586 108 C ATOM 33 CD GLN A 100 0.223 -13.303 33.135 1.00 33.34 C ANISOU 33 CD GLN A 100 4704 4277 3687 -101 711 33 C ATOM 34 NE2 GLN A 100 -0.915 -12.853 32.612 1.00 33.16 N ANISOU 34 NE2 GLN A 100 4648 4258 3693 -316 371 231 N ATOM 35 OE1 GLN A 100 1.079 -13.881 32.466 1.00 34.67 O ANISOU 35 OE1 GLN A 100 4894 4549 3731 75 1115 -150 O ATOM 36 N LYS A 101 0.629 -12.389 38.449 1.00 20.97 N ANISOU 36 N LYS A 101 2598 2795 2573 -402 665 -2 N ATOM 37 CA LYS A 101 -0.450 -12.612 39.404 1.00 20.53 C ANISOU 37 CA LYS A 101 2725 2634 2442 -318 530 -115 C ATOM 38 C LYS A 101 -0.785 -11.323 40.142 1.00 19.63 C ANISOU 38 C LYS A 101 2516 2602 2340 -265 297 -9 C ATOM 39 O LYS A 101 0.094 -10.674 40.707 1.00 20.43 O ANISOU 39 O LYS A 101 2622 2625 2517 -225 277 -155 O ATOM 40 CB LYS A 101 -0.084 -13.718 40.393 1.00 22.07 C ANISOU 40 CB LYS A 101 3026 2753 2605 -307 635 -56 C ATOM 41 CG LYS A 101 -1.221 -14.086 41.330 1.00 24.94 C ANISOU 41 CG LYS A 101 3454 3035 2986 -146 648 138 C ATOM 42 CD LYS A 101 -0.877 -15.275 42.216 1.00 27.70 C ANISOU 42 CD LYS A 101 3840 3372 3311 -161 688 371 C ATOM 43 CE LYS A 101 -1.984 -15.534 43.231 1.00 29.52 C ANISOU 43 CE LYS A 101 4116 3531 3569 -208 648 631 C ATOM 44 NZ LYS A 101 -1.739 -16.765 44.035 1.00 31.24 N1+ ANISOU 44 NZ LYS A 101 4294 3744 3831 -93 626 687 N1+ ATOM 45 N THR A 102 -2.061 -10.948 40.114 1.00 17.70 N ANISOU 45 N THR A 102 2074 2433 2219 -345 244 197 N ATOM 46 CA THR A 102 -2.532 -9.758 40.816 1.00 17.74 C ANISOU 46 CA THR A 102 2072 2550 2118 -188 -95 238 C ATOM 47 C THR A 102 -2.360 -9.960 42.317 1.00 18.08 C ANISOU 47 C THR A 102 2208 2676 1987 -156 -225 372 C ATOM 48 O THR A 102 -2.677 -11.027 42.850 1.00 18.11 O ANISOU 48 O THR A 102 2398 2610 1872 -127 -69 335 O ATOM 49 CB THR A 102 -4.008 -9.450 40.476 1.00 16.94 C ANISOU 49 CB THR A 102 1839 2439 2158 3 -455 244 C ATOM 50 CG2 THR A 102 -4.525 -8.273 41.288 1.00 16.52 C ANISOU 50 CG2 THR A 102 1655 2536 2087 82 -514 93 C ATOM 51 OG1 THR A 102 -4.117 -9.143 39.080 1.00 18.08 O ANISOU 51 OG1 THR A 102 1947 2611 2314 85 -401 234 O ATOM 52 N TYR A 103 -1.851 -8.935 42.992 1.00 17.96 N ANISOU 52 N TYR A 103 2070 2825 1928 -172 -399 373 N ATOM 53 CA TYR A 103 -1.535 -9.013 44.412 1.00 18.83 C ANISOU 53 CA TYR A 103 2128 3068 1957 -181 -414 543 C ATOM 54 C TYR A 103 -1.687 -7.623 45.010 1.00 17.32 C ANISOU 54 C TYR A 103 1722 3127 1731 -135 -407 651 C ATOM 55 O TYR A 103 -0.806 -6.783 44.866 1.00 17.58 O ANISOU 55 O TYR A 103 1674 3269 1735 47 -204 781 O ATOM 56 CB TYR A 103 -0.106 -9.547 44.587 1.00 20.81 C ANISOU 56 CB TYR A 103 2596 3144 2169 -248 -586 549 C ATOM 57 CG TYR A 103 0.468 -9.476 45.985 1.00 22.20 C ANISOU 57 CG TYR A 103 2747 3216 2472 -136 -713 491 C ATOM 58 CD1 TYR A 103 -0.128 -10.150 47.041 1.00 22.82 C ANISOU 58 CD1 TYR A 103 2774 3343 2554 30 -796 457 C ATOM 59 CD2 TYR A 103 1.635 -8.762 46.238 1.00 22.48 C ANISOU 59 CD2 TYR A 103 2800 3138 2605 -247 -747 501 C ATOM 60 CE1 TYR A 103 0.411 -10.093 48.323 1.00 23.70 C ANISOU 60 CE1 TYR A 103 2845 3551 2609 -82 -669 356 C ATOM 61 CE2 TYR A 103 2.180 -8.697 47.505 1.00 23.37 C ANISOU 61 CE2 TYR A 103 2862 3286 2732 -363 -685 612 C ATOM 62 CZ TYR A 103 1.568 -9.361 48.546 1.00 24.21 C ANISOU 62 CZ TYR A 103 2879 3603 2715 -351 -577 365 C ATOM 63 OH TYR A 103 2.123 -9.296 49.806 1.00 25.24 O ANISOU 63 OH TYR A 103 2886 3786 2917 -487 -461 227 O ATOM 64 N GLN A 104 -2.818 -7.369 45.659 1.00 15.71 N ANISOU 64 N GLN A 104 1228 3137 1603 -77 -352 634 N ATOM 65 CA GLN A 104 -3.064 -6.051 46.231 1.00 17.53 C ANISOU 65 CA GLN A 104 1608 3352 1701 15 -58 741 C ATOM 66 C GLN A 104 -2.164 -5.774 47.432 1.00 16.80 C ANISOU 66 C GLN A 104 1845 3092 1445 -2 242 603 C ATOM 67 O GLN A 104 -1.776 -4.634 47.674 1.00 16.31 O ANISOU 67 O GLN A 104 2186 2869 1143 58 356 460 O ATOM 68 CB GLN A 104 -4.543 -5.868 46.587 1.00 20.81 C ANISOU 68 CB GLN A 104 1929 3816 2162 71 -155 854 C ATOM 69 CG GLN A 104 -5.440 -5.739 45.366 1.00 24.88 C ANISOU 69 CG GLN A 104 2414 4287 2751 171 -27 991 C ATOM 70 CD GLN A 104 -6.886 -5.472 45.722 1.00 28.98 C ANISOU 70 CD GLN A 104 3155 4650 3206 237 126 1081 C ATOM 71 NE2 GLN A 104 -7.757 -5.486 44.713 1.00 29.40 N ANISOU 71 NE2 GLN A 104 3302 4485 3384 209 47 1280 N ATOM 72 OE1 GLN A 104 -7.222 -5.260 46.890 1.00 31.82 O ANISOU 72 OE1 GLN A 104 3501 5087 3504 332 265 994 O ATOM 73 N GLY A 105 -1.821 -6.820 48.176 1.00 16.84 N ANISOU 73 N GLY A 105 2036 2969 1393 -224 221 623 N ATOM 74 CA GLY A 105 -0.843 -6.696 49.244 1.00 17.65 C ANISOU 74 CA GLY A 105 2301 3021 1384 -292 135 422 C ATOM 75 C GLY A 105 -1.336 -5.939 50.464 1.00 18.51 C ANISOU 75 C GLY A 105 2405 3178 1450 -487 -136 480 C ATOM 76 O GLY A 105 -2.534 -5.689 50.623 1.00 18.53 O ANISOU 76 O GLY A 105 2300 3201 1540 -465 -216 306 O ATOM 77 N SER A 106 -0.402 -5.564 51.330 1.00 18.91 N ANISOU 77 N SER A 106 2404 3292 1491 -573 -364 514 N ATOM 78 CA SER A 106 -0.750 -4.950 52.604 1.00 20.02 C ANISOU 78 CA SER A 106 2608 3406 1594 -265 -304 437 C ATOM 79 C SER A 106 -1.331 -3.551 52.471 1.00 19.23 C ANISOU 79 C SER A 106 2486 3279 1542 -316 -122 369 C ATOM 80 O SER A 106 -2.035 -3.089 53.367 1.00 18.94 O ANISOU 80 O SER A 106 2558 3095 1543 -490 -44 174 O ATOM 81 CB SER A 106 0.466 -4.905 53.524 1.00 21.60 C ANISOU 81 CB SER A 106 2905 3735 1568 -33 -496 419 C ATOM 82 OG SER A 106 0.896 -6.210 53.840 1.00 23.75 O ANISOU 82 OG SER A 106 3129 4197 1699 -82 -362 465 O ATOM 83 N TYR A 107 -1.029 -2.879 51.363 1.00 18.65 N ANISOU 83 N TYR A 107 2240 3305 1542 -319 -58 345 N ATOM 84 CA TYR A 107 -1.438 -1.492 51.187 1.00 17.91 C ANISOU 84 CA TYR A 107 2064 3147 1596 -263 -19 310 C ATOM 85 C TYR A 107 -2.637 -1.343 50.254 1.00 17.51 C ANISOU 85 C TYR A 107 2108 3123 1422 -7 -88 117 C ATOM 86 O TYR A 107 -3.048 -0.228 49.933 1.00 18.51 O ANISOU 86 O TYR A 107 2430 3236 1367 -53 -26 51 O ATOM 87 CB TYR A 107 -0.248 -0.646 50.717 1.00 18.22 C ANISOU 87 CB TYR A 107 1951 3140 1832 -359 31 209 C ATOM 88 CG TYR A 107 0.947 -0.806 51.625 1.00 19.33 C ANISOU 88 CG TYR A 107 2093 3183 2067 -385 -231 182 C ATOM 89 CD1 TYR A 107 1.033 -0.097 52.814 1.00 19.78 C ANISOU 89 CD1 TYR A 107 2101 3184 2232 -417 -228 73 C ATOM 90 CD2 TYR A 107 1.971 -1.690 51.312 1.00 20.21 C ANISOU 90 CD2 TYR A 107 2139 3293 2247 -398 -478 152 C ATOM 91 CE1 TYR A 107 2.107 -0.250 53.660 1.00 20.98 C ANISOU 91 CE1 TYR A 107 2173 3343 2457 -430 -254 33 C ATOM 92 CE2 TYR A 107 3.056 -1.853 52.155 1.00 21.51 C ANISOU 92 CE2 TYR A 107 2285 3377 2511 -445 -476 10 C ATOM 93 CZ TYR A 107 3.116 -1.129 53.328 1.00 22.06 C ANISOU 93 CZ TYR A 107 2293 3467 2622 -445 -378 -25 C ATOM 94 OH TYR A 107 4.184 -1.281 54.176 1.00 23.91 O ANISOU 94 OH TYR A 107 2519 3622 2942 -456 -379 -77 O ATOM 95 N GLY A 108 -3.206 -2.471 49.840 1.00 16.02 N ANISOU 95 N GLY A 108 1805 2914 1369 93 -117 41 N ATOM 96 CA GLY A 108 -4.372 -2.460 48.973 1.00 16.55 C ANISOU 96 CA GLY A 108 1866 3037 1385 309 -96 107 C ATOM 97 C GLY A 108 -4.079 -1.783 47.649 1.00 16.30 C ANISOU 97 C GLY A 108 1823 3100 1270 368 -174 424 C ATOM 98 O GLY A 108 -4.756 -0.834 47.264 1.00 17.22 O ANISOU 98 O GLY A 108 2002 3303 1239 388 -59 661 O ATOM 99 N PHE A 109 -3.055 -2.276 46.962 1.00 16.13 N ANISOU 99 N PHE A 109 1717 3111 1301 174 92 337 N ATOM 100 CA PHE A 109 -2.570 -1.670 45.730 1.00 15.40 C ANISOU 100 CA PHE A 109 1682 2925 1246 50 20 508 C ATOM 101 C PHE A 109 -3.470 -2.032 44.562 1.00 15.57 C ANISOU 101 C PHE A 109 1791 2740 1384 -43 52 348 C ATOM 102 O PHE A 109 -3.647 -3.210 44.263 1.00 15.44 O ANISOU 102 O PHE A 109 1895 2483 1490 76 93 480 O ATOM 103 CB PHE A 109 -1.136 -2.138 45.455 1.00 16.49 C ANISOU 103 CB PHE A 109 1953 2965 1348 0 106 469 C ATOM 104 CG PHE A 109 -0.580 -1.679 44.134 1.00 17.00 C ANISOU 104 CG PHE A 109 2140 2845 1476 -145 86 444 C ATOM 105 CD1 PHE A 109 -0.637 -0.341 43.764 1.00 18.11 C ANISOU 105 CD1 PHE A 109 2396 2920 1564 -110 247 392 C ATOM 106 CD2 PHE A 109 0.033 -2.585 43.276 1.00 16.66 C ANISOU 106 CD2 PHE A 109 2013 2772 1546 -278 123 340 C ATOM 107 CE1 PHE A 109 -0.112 0.083 42.553 1.00 18.14 C ANISOU 107 CE1 PHE A 109 2537 2803 1551 -80 380 509 C ATOM 108 CE2 PHE A 109 0.562 -2.175 42.061 1.00 16.82 C ANISOU 108 CE2 PHE A 109 2100 2696 1594 -241 275 437 C ATOM 109 CZ PHE A 109 0.491 -0.837 41.698 1.00 17.33 C ANISOU 109 CZ PHE A 109 2218 2772 1595 0 462 529 C ATOM 110 N ARG A 110 -4.037 -1.011 43.916 1.00 16.03 N ANISOU 110 N ARG A 110 1871 2830 1389 -26 -248 460 N ATOM 111 CA ARG A 110 -4.894 -1.182 42.741 1.00 16.22 C ANISOU 111 CA ARG A 110 1807 2876 1480 19 -126 398 C ATOM 112 C ARG A 110 -4.507 -0.178 41.662 1.00 14.40 C ANISOU 112 C ARG A 110 1509 2566 1397 -351 -32 336 C ATOM 113 O ARG A 110 -3.887 0.845 41.946 1.00 14.96 O ANISOU 113 O ARG A 110 1716 2568 1399 -425 -49 539 O ATOM 114 CB ARG A 110 -6.373 -0.968 43.101 1.00 19.14 C ANISOU 114 CB ARG A 110 2134 3260 1879 -88 -40 568 C ATOM 115 CG ARG A 110 -6.917 -1.865 44.187 1.00 23.15 C ANISOU 115 CG ARG A 110 2634 3721 2441 -60 123 625 C ATOM 116 CD ARG A 110 -8.266 -1.350 44.706 1.00 28.20 C ANISOU 116 CD ARG A 110 3506 4201 3008 -324 -7 685 C ATOM 117 NE ARG A 110 -8.171 0.011 45.241 1.00 32.67 N ANISOU 117 NE ARG A 110 4238 4734 3441 -567 58 856 N ATOM 118 CZ ARG A 110 -7.743 0.310 46.466 1.00 35.19 C ANISOU 118 CZ ARG A 110 4589 5010 3771 -811 13 1096 C ATOM 119 NH1 ARG A 110 -7.363 -0.656 47.294 1.00 36.02 N1+ ANISOU 119 NH1 ARG A 110 4557 5227 3902 -652 -126 1269 N1+ ATOM 120 NH2 ARG A 110 -7.695 1.575 46.868 1.00 35.61 N ANISOU 120 NH2 ARG A 110 4790 4882 3859 -1112 47 1123 N ATOM 121 N LEU A 111 -4.887 -0.467 40.423 1.00 13.52 N ANISOU 121 N LEU A 111 1379 2386 1372 -425 261 356 N ATOM 122 CA LEU A 111 -4.693 0.483 39.334 1.00 12.49 C ANISOU 122 CA LEU A 111 1224 2140 1381 -369 23 90 C ATOM 123 C LEU A 111 -6.031 1.125 38.989 1.00 13.86 C ANISOU 123 C LEU A 111 1455 2238 1571 -317 -16 55 C ATOM 124 O LEU A 111 -7.079 0.494 39.111 1.00 15.66 O ANISOU 124 O LEU A 111 1486 2714 1751 -455 67 37 O ATOM 125 CB LEU A 111 -4.106 -0.208 38.099 1.00 12.24 C ANISOU 125 CB LEU A 111 1314 1826 1510 -378 189 188 C ATOM 126 CG LEU A 111 -2.709 -0.802 38.260 1.00 12.23 C ANISOU 126 CG LEU A 111 1379 1729 1538 -168 141 86 C ATOM 127 CD1 LEU A 111 -2.233 -1.416 36.961 1.00 12.47 C ANISOU 127 CD1 LEU A 111 1627 1508 1601 -18 -24 265 C ATOM 128 CD2 LEU A 111 -1.734 0.268 38.719 1.00 11.99 C ANISOU 128 CD2 LEU A 111 1477 1668 1412 -168 98 -198 C ATOM 129 N GLY A 112 -5.992 2.383 38.575 1.00 13.65 N ANISOU 129 N GLY A 112 1669 2003 1515 -32 -14 83 N ATOM 130 CA GLY A 112 -7.176 3.060 38.082 1.00 12.53 C ANISOU 130 CA GLY A 112 1626 1815 1319 86 -55 221 C ATOM 131 C GLY A 112 -6.837 3.759 36.781 1.00 13.34 C ANISOU 131 C GLY A 112 1788 1921 1358 208 -310 70 C ATOM 132 O GLY A 112 -5.666 4.058 36.510 1.00 13.52 O ANISOU 132 O GLY A 112 1829 2043 1266 0 -489 189 O ATOM 133 N PHE A 113 -7.856 4.011 35.966 1.00 12.94 N ANISOU 133 N PHE A 113 1577 1875 1463 256 -255 -120 N ATOM 134 CA PHE A 113 -7.646 4.629 34.666 1.00 12.54 C ANISOU 134 CA PHE A 113 1588 1690 1487 376 -181 19 C ATOM 135 C PHE A 113 -8.700 5.709 34.432 1.00 14.07 C ANISOU 135 C PHE A 113 1683 1966 1698 146 -19 170 C ATOM 136 O PHE A 113 -9.765 5.699 35.061 1.00 13.84 O ANISOU 136 O PHE A 113 1285 2133 1840 231 -21 280 O ATOM 137 CB PHE A 113 -7.704 3.573 33.553 1.00 12.11 C ANISOU 137 CB PHE A 113 1567 1552 1483 384 -107 -78 C ATOM 138 CG PHE A 113 -6.781 2.398 33.771 1.00 11.64 C ANISOU 138 CG PHE A 113 1664 1482 1276 426 -328 -232 C ATOM 139 CD1 PHE A 113 -7.192 1.309 34.529 1.00 11.60 C ANISOU 139 CD1 PHE A 113 1736 1586 1084 496 -372 -185 C ATOM 140 CD2 PHE A 113 -5.513 2.382 33.205 1.00 11.67 C ANISOU 140 CD2 PHE A 113 1618 1495 1322 470 -307 -270 C ATOM 141 CE1 PHE A 113 -6.348 0.221 34.736 1.00 11.49 C ANISOU 141 CE1 PHE A 113 1751 1552 1060 834 -136 -115 C ATOM 142 CE2 PHE A 113 -4.659 1.299 33.399 1.00 12.50 C ANISOU 142 CE2 PHE A 113 1835 1447 1466 462 -122 -9 C ATOM 143 CZ PHE A 113 -5.077 0.217 34.169 1.00 13.02 C ANISOU 143 CZ PHE A 113 1900 1574 1472 618 -230 -6 C ATOM 144 N LEU A 114 -8.396 6.650 33.542 1.00 14.25 N ANISOU 144 N LEU A 114 1751 1961 1701 -49 72 -15 N ATOM 145 CA LEU A 114 -9.356 7.684 33.188 1.00 13.36 C ANISOU 145 CA LEU A 114 1605 1741 1731 59 -53 -257 C ATOM 146 C LEU A 114 -10.513 7.051 32.418 1.00 13.80 C ANISOU 146 C LEU A 114 1633 1854 1755 105 -62 -227 C ATOM 147 O LEU A 114 -10.348 6.015 31.773 1.00 14.12 O ANISOU 147 O LEU A 114 1547 1841 1976 213 -229 -269 O ATOM 148 CB LEU A 114 -8.697 8.781 32.349 1.00 13.93 C ANISOU 148 CB LEU A 114 1816 1676 1801 -62 -45 -531 C ATOM 149 CG LEU A 114 -7.601 9.648 32.967 1.00 13.33 C ANISOU 149 CG LEU A 114 1856 1431 1778 -68 79 -543 C ATOM 150 CD1 LEU A 114 -7.227 10.766 32.013 1.00 13.41 C ANISOU 150 CD1 LEU A 114 1684 1487 1922 -55 250 -592 C ATOM 151 CD2 LEU A 114 -8.051 10.226 34.301 1.00 14.64 C ANISOU 151 CD2 LEU A 114 2251 1395 1915 -74 -142 -528 C ATOM 152 N HIS A 115 -11.686 7.672 32.494 1.00 13.76 N ANISOU 152 N HIS A 115 1497 2055 1677 123 -210 -430 N ATOM 153 CA HIS A 115 -12.863 7.186 31.779 1.00 13.48 C ANISOU 153 CA HIS A 115 1551 1851 1719 -9 -271 -375 C ATOM 154 C HIS A 115 -13.070 8.075 30.557 1.00 13.08 C ANISOU 154 C HIS A 115 1481 1777 1710 3 -137 -349 C ATOM 155 O HIS A 115 -13.937 8.949 30.533 1.00 13.94 O ANISOU 155 O HIS A 115 1588 2033 1675 -210 193 -216 O ATOM 156 CB HIS A 115 -14.081 7.188 32.702 1.00 14.35 C ANISOU 156 CB HIS A 115 1747 1749 1956 -157 -407 -134 C ATOM 157 CG HIS A 115 -13.805 6.615 34.058 1.00 16.46 C ANISOU 157 CG HIS A 115 2148 1706 2399 -189 -393 -69 C ATOM 158 CD2 HIS A 115 -13.777 7.190 35.283 1.00 16.81 C ANISOU 158 CD2 HIS A 115 2221 1761 2406 -210 -639 -78 C ATOM 159 ND1 HIS A 115 -13.490 5.286 34.254 1.00 18.04 N ANISOU 159 ND1 HIS A 115 2489 1711 2655 -238 -371 59 N ATOM 160 CE1 HIS A 115 -13.290 5.069 35.543 1.00 17.93 C ANISOU 160 CE1 HIS A 115 2566 1761 2487 -187 -608 -122 C ATOM 161 NE2 HIS A 115 -13.458 6.210 36.189 1.00 17.14 N ANISOU 161 NE2 HIS A 115 2415 1715 2381 -98 -660 -47 N ATOM 162 N SER A 116 -12.250 7.829 29.541 1.00 12.75 N ANISOU 162 N SER A 116 1403 1687 1756 20 -83 -247 N ATOM 163 CA SER A 116 -12.091 8.744 28.419 1.00 12.97 C ANISOU 163 CA SER A 116 1338 1895 1696 51 -150 -57 C ATOM 164 C SER A 116 -13.037 8.539 27.248 1.00 12.39 C ANISOU 164 C SER A 116 1148 1894 1666 163 -385 -138 C ATOM 165 O SER A 116 -13.153 9.417 26.389 1.00 13.56 O ANISOU 165 O SER A 116 1254 2192 1705 34 -216 -121 O ATOM 166 CB SER A 116 -10.652 8.699 27.928 1.00 13.89 C ANISOU 166 CB SER A 116 1100 2293 1885 43 -164 135 C ATOM 167 OG SER A 116 -9.793 9.008 28.999 1.00 15.47 O ANISOU 167 OG SER A 116 1154 2599 2124 -142 71 210 O ATOM 168 N GLY A 117 -13.699 7.389 27.196 1.00 11.86 N ANISOU 168 N GLY A 117 1086 1751 1668 231 -541 -261 N ATOM 169 CA GLY A 117 -14.608 7.106 26.092 1.00 12.60 C ANISOU 169 CA GLY A 117 1540 1757 1490 72 -174 -176 C ATOM 170 C GLY A 117 -13.897 6.696 24.807 1.00 12.80 C ANISOU 170 C GLY A 117 1682 1871 1309 -117 137 -85 C ATOM 171 O GLY A 117 -12.687 6.514 24.801 1.00 13.07 O ANISOU 171 O GLY A 117 1838 1887 1242 -366 344 38 O ATOM 172 N THR A 118 -14.650 6.544 23.718 1.00 13.35 N ANISOU 172 N THR A 118 1723 2082 1266 -52 63 41 N ATOM 173 CA THR A 118 -14.071 6.081 22.450 1.00 13.67 C ANISOU 173 CA THR A 118 1507 2288 1399 -109 -115 292 C ATOM 174 C THR A 118 -14.276 7.008 21.250 1.00 14.82 C ANISOU 174 C THR A 118 1599 2490 1540 -201 -101 429 C ATOM 175 O THR A 118 -14.255 6.545 20.108 1.00 16.16 O ANISOU 175 O THR A 118 1879 2640 1620 -152 -71 357 O ATOM 176 CB THR A 118 -14.592 4.688 22.049 1.00 13.28 C ANISOU 176 CB THR A 118 1430 2208 1407 29 -268 298 C ATOM 177 CG2 THR A 118 -14.265 3.650 23.120 1.00 12.34 C ANISOU 177 CG2 THR A 118 1429 1910 1350 193 -358 199 C ATOM 178 OG1 THR A 118 -16.010 4.747 21.839 1.00 14.21 O ANISOU 178 OG1 THR A 118 1470 2516 1414 -92 -535 360 O ATOM 179 N ALA A 119 -14.473 8.303 21.491 1.00 14.45 N ANISOU 179 N ALA A 119 1500 2463 1528 -461 -115 634 N ATOM 180 CA ALA A 119 -14.526 9.262 20.384 1.00 15.44 C ANISOU 180 CA ALA A 119 1818 2634 1415 -526 -201 690 C ATOM 181 C ALA A 119 -13.217 9.224 19.606 1.00 17.57 C ANISOU 181 C ALA A 119 2268 3007 1400 -633 -267 623 C ATOM 182 O ALA A 119 -12.167 8.944 20.178 1.00 17.43 O ANISOU 182 O ALA A 119 2172 3161 1288 -513 15 625 O ATOM 183 CB ALA A 119 -14.780 10.652 20.895 1.00 15.79 C ANISOU 183 CB ALA A 119 1829 2627 1544 -519 -289 808 C ATOM 184 N LYS A 120 -13.275 9.525 18.310 1.00 20.14 N ANISOU 184 N LYS A 120 2758 3318 1576 -897 -379 552 N ATOM 185 CA LYS A 120 -12.088 9.452 17.455 1.00 23.97 C ANISOU 185 CA LYS A 120 3451 3938 1720 -829 -621 589 C ATOM 186 C LYS A 120 -10.902 10.290 17.937 1.00 25.01 C ANISOU 186 C LYS A 120 3567 3995 1941 -541 -500 724 C ATOM 187 O LYS A 120 -9.751 9.942 17.680 1.00 26.01 O ANISOU 187 O LYS A 120 3612 4186 2085 -333 -542 885 O ATOM 188 CB LYS A 120 -12.438 9.819 16.010 1.00 26.87 C ANISOU 188 CB LYS A 120 4070 4424 1716 -864 -1011 344 C ATOM 189 CG LYS A 120 -12.574 8.600 15.110 1.00 30.77 C ANISOU 189 CG LYS A 120 4730 4973 1989 -840 -983 223 C ATOM 190 CD LYS A 120 -13.208 8.917 13.757 1.00 33.04 C ANISOU 190 CD LYS A 120 5180 5364 2009 -881 -748 -21 C ATOM 191 CE LYS A 120 -13.769 7.637 13.129 1.00 34.22 C ANISOU 191 CE LYS A 120 5480 5606 1916 -902 -736 -200 C ATOM 192 NZ LYS A 120 -14.352 7.810 11.765 1.00 34.83 N1+ ANISOU 192 NZ LYS A 120 5588 5809 1838 -794 -704 -193 N1+ ATOM 193 N SER A 121 -11.185 11.382 18.637 1.00 25.05 N ANISOU 193 N SER A 121 3611 3715 2193 -456 -410 486 N ATOM 194 CA SER A 121 -10.139 12.307 19.057 1.00 26.96 C ANISOU 194 CA SER A 121 3676 3685 2881 -354 -205 329 C ATOM 195 C SER A 121 -9.335 11.847 20.286 1.00 26.44 C ANISOU 195 C SER A 121 3395 3693 2959 -355 -63 555 C ATOM 196 O SER A 121 -8.292 12.434 20.588 1.00 27.83 O ANISOU 196 O SER A 121 3596 3903 3074 -483 -186 825 O ATOM 197 CB SER A 121 -10.734 13.693 19.315 1.00 29.58 C ANISOU 197 CB SER A 121 4137 3636 3466 -456 -159 105 C ATOM 198 OG SER A 121 -11.625 13.659 20.422 1.00 31.14 O ANISOU 198 OG SER A 121 4439 3580 3813 -604 -75 48 O ATOM 199 N VAL A 122 -9.795 10.815 20.995 1.00 23.50 N ANISOU 199 N VAL A 122 2732 3306 2892 -204 279 463 N ATOM 200 CA VAL A 122 -9.058 10.356 22.180 1.00 21.88 C ANISOU 200 CA VAL A 122 2231 3273 2811 -126 381 391 C ATOM 201 C VAL A 122 -7.675 9.797 21.826 1.00 22.18 C ANISOU 201 C VAL A 122 2040 3449 2938 -326 446 632 C ATOM 202 O VAL A 122 -7.495 9.145 20.797 1.00 22.52 O ANISOU 202 O VAL A 122 1914 3505 3137 -200 324 630 O ATOM 203 CB VAL A 122 -9.853 9.332 23.039 1.00 20.78 C ANISOU 203 CB VAL A 122 2019 3165 2712 -368 513 199 C ATOM 204 CG1 VAL A 122 -11.195 9.909 23.443 1.00 20.79 C ANISOU 204 CG1 VAL A 122 2005 3112 2781 -740 497 287 C ATOM 205 CG2 VAL A 122 -10.029 8.012 22.312 1.00 20.45 C ANISOU 205 CG2 VAL A 122 2013 3203 2554 -313 608 295 C ATOM 206 N THR A 123 -6.698 10.071 22.683 1.00 21.71 N ANISOU 206 N THR A 123 1927 3401 2921 -383 605 721 N ATOM 207 CA THR A 123 -5.328 9.634 22.437 1.00 23.06 C ANISOU 207 CA THR A 123 2341 3498 2922 -279 473 750 C ATOM 208 C THR A 123 -5.002 8.434 23.301 1.00 20.81 C ANISOU 208 C THR A 123 2088 3283 2538 -388 410 641 C ATOM 209 O THR A 123 -3.985 7.767 23.115 1.00 20.49 O ANISOU 209 O THR A 123 2273 3132 2380 -317 488 647 O ATOM 210 CB THR A 123 -4.323 10.750 22.724 1.00 25.31 C ANISOU 210 CB THR A 123 2865 3766 2986 -156 441 793 C ATOM 211 CG2 THR A 123 -4.564 11.934 21.791 1.00 26.23 C ANISOU 211 CG2 THR A 123 2910 3837 3221 67 513 845 C ATOM 212 OG1 THR A 123 -4.464 11.180 24.078 1.00 25.69 O ANISOU 212 OG1 THR A 123 3170 3952 2640 -171 393 765 O ATOM 213 N CYS A 124 -5.886 8.172 24.252 1.00 19.70 N ANISOU 213 N CYS A 124 1881 3180 2425 -321 240 232 N ATOM 214 CA CYS A 124 -5.688 7.109 25.213 1.00 19.19 C ANISOU 214 CA CYS A 124 1683 3209 2399 -354 135 -73 C ATOM 215 C CYS A 124 -7.036 6.736 25.815 1.00 17.08 C ANISOU 215 C CYS A 124 1521 2685 2283 -391 107 -21 C ATOM 216 O CYS A 124 -7.763 7.608 26.291 1.00 17.81 O ANISOU 216 O CYS A 124 1408 2741 2618 -309 335 129 O ATOM 217 CB CYS A 124 -4.728 7.596 26.301 1.00 21.17 C ANISOU 217 CB CYS A 124 1721 3727 2595 -348 -46 -101 C ATOM 218 SG CYS A 124 -4.302 6.378 27.523 1.00 24.34 S ANISOU 218 SG CYS A 124 1997 4465 2786 -509 -299 -426 S ATOM 219 N THR A 125 -7.378 5.450 25.781 1.00 13.88 N ANISOU 219 N THR A 125 1398 1998 1878 -400 -262 -70 N ATOM 220 CA THR A 125 -8.622 4.982 26.400 1.00 13.33 C ANISOU 220 CA THR A 125 1505 1662 1898 -313 -449 -1 C ATOM 221 C THR A 125 -8.541 3.549 26.936 1.00 13.71 C ANISOU 221 C THR A 125 1728 1633 1848 -158 -438 20 C ATOM 222 O THR A 125 -7.981 2.661 26.289 1.00 16.51 O ANISOU 222 O THR A 125 2262 1865 2144 -12 -261 175 O ATOM 223 CB THR A 125 -9.835 5.135 25.448 1.00 13.36 C ANISOU 223 CB THR A 125 1538 1581 1957 -554 -238 175 C ATOM 224 CG2 THR A 125 -9.748 4.156 24.272 1.00 13.55 C ANISOU 224 CG2 THR A 125 1637 1619 1893 -421 -367 162 C ATOM 225 OG1 THR A 125 -11.049 4.922 26.183 1.00 13.64 O ANISOU 225 OG1 THR A 125 1597 1616 1969 -654 180 488 O ATOM 226 N TYR A 126 -9.109 3.336 28.120 1.00 12.13 N ANISOU 226 N TYR A 126 1624 1557 1428 -122 -680 -194 N ATOM 227 CA TYR A 126 -9.024 2.052 28.809 1.00 10.90 C ANISOU 227 CA TYR A 126 1590 1379 1171 -183 -615 77 C ATOM 228 C TYR A 126 -10.343 1.293 28.765 1.00 11.33 C ANISOU 228 C TYR A 126 1658 1453 1195 1 -492 280 C ATOM 229 O TYR A 126 -11.407 1.866 29.009 1.00 11.90 O ANISOU 229 O TYR A 126 1750 1603 1167 -157 -576 263 O ATOM 230 CB TYR A 126 -8.591 2.256 30.266 1.00 11.18 C ANISOU 230 CB TYR A 126 1680 1463 1107 -206 -290 57 C ATOM 231 CG TYR A 126 -8.676 1.013 31.107 1.00 11.43 C ANISOU 231 CG TYR A 126 1611 1469 1264 -189 -382 -33 C ATOM 232 CD1 TYR A 126 -7.728 0.003 30.993 1.00 11.18 C ANISOU 232 CD1 TYR A 126 1377 1527 1344 -321 -609 -23 C ATOM 233 CD2 TYR A 126 -9.702 0.850 32.035 1.00 12.16 C ANISOU 233 CD2 TYR A 126 1905 1493 1223 -43 -408 -90 C ATOM 234 CE1 TYR A 126 -7.808 -1.140 31.778 1.00 11.23 C ANISOU 234 CE1 TYR A 126 1557 1386 1323 -407 -697 44 C ATOM 235 CE2 TYR A 126 -9.790 -0.289 32.817 1.00 10.44 C ANISOU 235 CE2 TYR A 126 1763 1272 930 -156 -566 -37 C ATOM 236 CZ TYR A 126 -8.843 -1.273 32.687 1.00 11.34 C ANISOU 236 CZ TYR A 126 1852 1333 1125 -315 -529 -58 C ATOM 237 OH TYR A 126 -8.942 -2.402 33.473 1.00 13.43 O ANISOU 237 OH TYR A 126 1998 1732 1374 -384 -155 -90 O ATOM 238 N SER A 127 -10.267 0.001 28.458 1.00 11.68 N ANISOU 238 N SER A 127 1718 1523 1195 -48 -397 164 N ATOM 239 CA SER A 127 -11.437 -0.878 28.463 1.00 12.14 C ANISOU 239 CA SER A 127 1922 1512 1179 13 -417 -21 C ATOM 240 C SER A 127 -11.545 -1.719 29.744 1.00 11.74 C ANISOU 240 C SER A 127 1803 1467 1190 35 -357 127 C ATOM 241 O SER A 127 -10.753 -2.644 29.943 1.00 11.44 O ANISOU 241 O SER A 127 1793 1362 1192 330 -360 222 O ATOM 242 CB SER A 127 -11.385 -1.813 27.259 1.00 11.51 C ANISOU 242 CB SER A 127 1948 1322 1104 65 -414 -248 C ATOM 243 OG SER A 127 -12.378 -2.813 27.354 1.00 11.49 O ANISOU 243 OG SER A 127 1783 1376 1206 38 -665 -231 O ATOM 244 N PRO A 128 -12.535 -1.412 30.607 1.00 12.16 N ANISOU 244 N PRO A 128 1956 1263 1400 -148 -408 95 N ATOM 245 CA PRO A 128 -12.750 -2.223 31.814 1.00 12.27 C ANISOU 245 CA PRO A 128 1867 1207 1587 -228 -79 171 C ATOM 246 C PRO A 128 -13.078 -3.659 31.451 1.00 11.75 C ANISOU 246 C PRO A 128 1570 1201 1695 -158 -160 208 C ATOM 247 O PRO A 128 -12.540 -4.581 32.060 1.00 12.35 O ANISOU 247 O PRO A 128 1474 1332 1887 -388 -570 178 O ATOM 248 CB PRO A 128 -13.981 -1.577 32.465 1.00 12.10 C ANISOU 248 CB PRO A 128 1913 1101 1584 -35 393 192 C ATOM 249 CG PRO A 128 -14.015 -0.193 31.936 1.00 12.91 C ANISOU 249 CG PRO A 128 2007 1189 1710 145 205 205 C ATOM 250 CD PRO A 128 -13.474 -0.278 30.533 1.00 11.87 C ANISOU 250 CD PRO A 128 1977 1148 1385 131 -133 64 C ATOM 251 N ALA A 129 -13.953 -3.846 30.468 1.00 12.06 N ANISOU 251 N ALA A 129 1427 1385 1769 -91 -2 308 N ATOM 252 CA ALA A 129 -14.383 -5.187 30.082 1.00 13.71 C ANISOU 252 CA ALA A 129 1607 1740 1863 -60 -84 -12 C ATOM 253 C ALA A 129 -13.222 -6.060 29.619 1.00 13.68 C ANISOU 253 C ALA A 129 1767 1529 1904 -57 -135 62 C ATOM 254 O ALA A 129 -13.211 -7.260 29.875 1.00 14.41 O ANISOU 254 O ALA A 129 1825 1756 1894 -200 -222 585 O ATOM 255 CB ALA A 129 -15.453 -5.114 29.012 1.00 13.70 C ANISOU 255 CB ALA A 129 1764 1852 1588 -97 -310 -24 C ATOM 256 N LEU A 130 -12.253 -5.453 28.936 1.00 13.81 N ANISOU 256 N LEU A 130 1827 1516 1905 -4 -44 -122 N ATOM 257 CA LEU A 130 -11.102 -6.183 28.395 1.00 13.73 C ANISOU 257 CA LEU A 130 1811 1576 1831 -147 -18 166 C ATOM 258 C LEU A 130 -9.840 -6.046 29.252 1.00 13.38 C ANISOU 258 C LEU A 130 1626 1660 1796 92 -61 130 C ATOM 259 O LEU A 130 -8.819 -6.660 28.947 1.00 14.72 O ANISOU 259 O LEU A 130 1908 1619 2068 128 -114 28 O ATOM 260 CB LEU A 130 -10.791 -5.703 26.975 1.00 13.61 C ANISOU 260 CB LEU A 130 1922 1576 1674 -144 -61 197 C ATOM 261 CG LEU A 130 -11.910 -5.785 25.936 1.00 13.09 C ANISOU 261 CG LEU A 130 1845 1418 1709 32 -281 407 C ATOM 262 CD1 LEU A 130 -11.457 -5.131 24.653 1.00 12.75 C ANISOU 262 CD1 LEU A 130 1898 1296 1650 108 -415 645 C ATOM 263 CD2 LEU A 130 -12.288 -7.220 25.676 1.00 14.17 C ANISOU 263 CD2 LEU A 130 1894 1534 1956 -20 -201 256 C ATOM 264 N ASN A 131 -9.923 -5.251 30.319 1.00 13.33 N ANISOU 264 N ASN A 131 1590 1897 1576 -28 -104 72 N ATOM 265 CA ASN A 131 -8.746 -4.831 31.092 1.00 12.81 C ANISOU 265 CA ASN A 131 1551 1914 1401 59 25 208 C ATOM 266 C ASN A 131 -7.616 -4.444 30.148 1.00 12.42 C ANISOU 266 C ASN A 131 1644 1839 1238 -128 -77 89 C ATOM 267 O ASN A 131 -6.498 -4.951 30.234 1.00 13.51 O ANISOU 267 O ASN A 131 2085 1965 1084 -153 62 -145 O ATOM 268 CB ASN A 131 -8.287 -5.911 32.077 1.00 12.27 C ANISOU 268 CB ASN A 131 1417 1862 1384 317 -140 396 C ATOM 269 CG ASN A 131 -7.164 -5.432 32.977 1.00 13.05 C ANISOU 269 CG ASN A 131 1773 1746 1439 207 34 308 C ATOM 270 ND2 ASN A 131 -6.288 -6.346 33.369 1.00 13.06 N ANISOU 270 ND2 ASN A 131 1740 1788 1435 205 11 493 N ATOM 271 OD1 ASN A 131 -7.070 -4.244 33.290 1.00 12.94 O ANISOU 271 OD1 ASN A 131 1858 1615 1442 200 34 -30 O ATOM 272 N LYS A 132 -7.929 -3.543 29.230 1.00 12.82 N ANISOU 272 N LYS A 132 1702 1756 1414 -83 -121 19 N ATOM 273 CA LYS A 132 -7.031 -3.266 28.131 1.00 12.37 C ANISOU 273 CA LYS A 132 1805 1513 1383 111 4 -189 C ATOM 274 C LYS A 132 -6.936 -1.784 27.846 1.00 11.26 C ANISOU 274 C LYS A 132 1683 1396 1201 290 63 -240 C ATOM 275 O LYS A 132 -7.937 -1.081 27.716 1.00 10.21 O ANISOU 275 O LYS A 132 1436 1160 1283 224 -53 -83 O ATOM 276 CB LYS A 132 -7.461 -4.037 26.885 1.00 11.98 C ANISOU 276 CB LYS A 132 1713 1440 1399 92 -101 -271 C ATOM 277 CG LYS A 132 -6.585 -3.813 25.670 1.00 10.62 C ANISOU 277 CG LYS A 132 1575 1167 1293 -148 -55 -345 C ATOM 278 CD LYS A 132 -6.812 -4.911 24.647 1.00 11.34 C ANISOU 278 CD LYS A 132 1804 1238 1267 103 -185 -641 C ATOM 279 CE LYS A 132 -5.889 -4.741 23.456 1.00 12.78 C ANISOU 279 CE LYS A 132 2138 1270 1447 13 -138 -785 C ATOM 280 NZ LYS A 132 -6.008 -5.892 22.526 1.00 13.81 N1+ ANISOU 280 NZ LYS A 132 2306 1382 1560 83 16 -870 N1+ ATOM 281 N MET A 133 -5.698 -1.329 27.768 1.00 12.41 N ANISOU 281 N MET A 133 1743 1807 1165 489 87 -291 N ATOM 282 CA AMET A 133 -5.407 0.061 27.468 0.76 12.69 C ANISOU 282 CA AMET A 133 1656 1954 1212 474 -11 -419 C ATOM 283 CA BMET A 133 -5.381 0.053 27.470 0.24 13.04 C ANISOU 283 CA BMET A 133 1858 1830 1267 586 -24 -342 C ATOM 284 C MET A 133 -5.143 0.227 25.973 1.00 12.89 C ANISOU 284 C MET A 133 1763 1906 1229 512 103 -390 C ATOM 285 O MET A 133 -4.365 -0.517 25.382 1.00 13.94 O ANISOU 285 O MET A 133 1830 2094 1371 371 147 -604 O ATOM 286 CB AMET A 133 -4.194 0.534 28.271 0.76 13.48 C ANISOU 286 CB AMET A 133 1784 2131 1206 362 -203 -582 C ATOM 287 CB BMET A 133 -4.115 0.424 28.231 0.24 14.19 C ANISOU 287 CB BMET A 133 2180 1811 1399 730 -260 -346 C ATOM 288 CG AMET A 133 -3.724 1.928 27.906 0.76 16.54 C ANISOU 288 CG AMET A 133 2266 2445 1573 448 -129 -709 C ATOM 289 CG BMET A 133 -3.727 1.867 28.150 0.24 16.05 C ANISOU 289 CG BMET A 133 2612 1850 1634 933 -370 -360 C ATOM 290 SD AMET A 133 -4.956 3.201 28.243 0.76 20.03 S ANISOU 290 SD AMET A 133 2488 2915 2208 277 -192 -617 S ATOM 291 SD BMET A 133 -3.314 2.412 29.807 0.24 18.14 S ANISOU 291 SD BMET A 133 2962 1995 1937 968 -473 -339 S ATOM 292 CE AMET A 133 -4.540 3.647 29.928 0.76 21.38 C ANISOU 292 CE AMET A 133 2801 3025 2298 293 65 -625 C ATOM 293 CE BMET A 133 -4.528 3.710 30.016 0.24 18.57 C ANISOU 293 CE BMET A 133 3058 2002 1994 965 -388 -358 C ATOM 294 N PHE A 134 -5.811 1.200 25.358 1.00 11.97 N ANISOU 294 N PHE A 134 1554 1886 1108 321 -58 -37 N ATOM 295 CA PHE A 134 -5.559 1.526 23.953 1.00 11.21 C ANISOU 295 CA PHE A 134 1152 1893 1213 242 -2 129 C ATOM 296 C PHE A 134 -4.950 2.922 23.895 1.00 12.31 C ANISOU 296 C PHE A 134 1105 2111 1460 516 93 270 C ATOM 297 O PHE A 134 -5.549 3.888 24.355 1.00 11.95 O ANISOU 297 O PHE A 134 1028 1951 1563 753 32 182 O ATOM 298 CB PHE A 134 -6.851 1.487 23.130 1.00 11.82 C ANISOU 298 CB PHE A 134 1353 1876 1264 272 57 59 C ATOM 299 CG PHE A 134 -7.525 0.134 23.099 1.00 12.31 C ANISOU 299 CG PHE A 134 1607 1592 1477 444 102 -178 C ATOM 300 CD1 PHE A 134 -8.290 -0.309 24.179 1.00 12.75 C ANISOU 300 CD1 PHE A 134 1856 1376 1612 482 -6 3 C ATOM 301 CD2 PHE A 134 -7.422 -0.676 21.978 1.00 11.99 C ANISOU 301 CD2 PHE A 134 1627 1394 1536 377 80 -353 C ATOM 302 CE1 PHE A 134 -8.927 -1.545 24.146 1.00 13.27 C ANISOU 302 CE1 PHE A 134 1994 1432 1616 368 -96 -61 C ATOM 303 CE2 PHE A 134 -8.046 -1.916 21.934 1.00 12.46 C ANISOU 303 CE2 PHE A 134 1824 1439 1471 205 140 -142 C ATOM 304 CZ PHE A 134 -8.803 -2.352 23.017 1.00 12.84 C ANISOU 304 CZ PHE A 134 1900 1384 1595 257 -25 -90 C ATOM 305 N CYS A 135 -3.744 3.031 23.359 1.00 15.36 N ANISOU 305 N CYS A 135 1778 2459 1600 158 383 415 N ATOM 306 CA CYS A 135 -3.038 4.301 23.398 1.00 17.26 C ANISOU 306 CA CYS A 135 1799 2817 1943 1 464 480 C ATOM 307 C CYS A 135 -2.243 4.543 22.125 1.00 17.92 C ANISOU 307 C CYS A 135 1938 2817 2054 -218 546 635 C ATOM 308 O CYS A 135 -2.022 3.627 21.336 1.00 18.95 O ANISOU 308 O CYS A 135 1928 2879 2392 2 588 615 O ATOM 309 CB CYS A 135 -2.118 4.350 24.615 1.00 19.72 C ANISOU 309 CB CYS A 135 2068 3084 2340 101 331 464 C ATOM 310 SG CYS A 135 -0.783 3.128 24.599 1.00 20.99 S ANISOU 310 SG CYS A 135 2162 3376 2437 268 258 500 S ATOM 311 N GLN A 136 -1.822 5.787 21.932 1.00 18.61 N ANISOU 311 N GLN A 136 2274 2777 2019 -354 607 715 N ATOM 312 CA GLN A 136 -1.046 6.147 20.757 1.00 19.02 C ANISOU 312 CA GLN A 136 2216 2932 2080 -305 428 676 C ATOM 313 C GLN A 136 0.443 6.192 21.057 1.00 19.18 C ANISOU 313 C GLN A 136 2292 2999 1995 -261 225 541 C ATOM 314 O GLN A 136 0.850 6.405 22.205 1.00 19.10 O ANISOU 314 O GLN A 136 2330 3061 1865 -350 227 507 O ATOM 315 CB GLN A 136 -1.501 7.499 20.215 1.00 20.94 C ANISOU 315 CB GLN A 136 2354 3125 2477 -311 97 755 C ATOM 316 CG GLN A 136 -2.873 7.496 19.569 1.00 22.95 C ANISOU 316 CG GLN A 136 2601 3214 2906 -154 -507 871 C ATOM 317 CD GLN A 136 -3.320 8.890 19.188 1.00 25.50 C ANISOU 317 CD GLN A 136 2984 3383 3320 -35 -1050 936 C ATOM 318 NE2 GLN A 136 -4.370 8.977 18.383 1.00 28.09 N ANISOU 318 NE2 GLN A 136 3513 3672 3489 -290 -1009 844 N ATOM 319 OE1 GLN A 136 -2.726 9.879 19.614 1.00 25.91 O ANISOU 319 OE1 GLN A 136 3045 3263 3535 223 -1157 998 O ATOM 320 N LEU A 137 1.238 5.992 20.005 1.00 19.35 N ANISOU 320 N LEU A 137 2240 3100 2013 -102 107 156 N ATOM 321 CA LEU A 137 2.699 6.022 20.064 1.00 19.79 C ANISOU 321 CA LEU A 137 2240 3245 2035 28 140 -90 C ATOM 322 C LEU A 137 3.223 7.329 20.649 1.00 18.51 C ANISOU 322 C LEU A 137 2093 3092 1848 -1 11 -58 C ATOM 323 O LEU A 137 2.896 8.411 20.158 1.00 17.57 O ANISOU 323 O LEU A 137 1877 2984 1814 98 -86 126 O ATOM 324 CB LEU A 137 3.278 5.819 18.656 1.00 21.33 C ANISOU 324 CB LEU A 137 2344 3466 2296 296 426 -178 C ATOM 325 CG LEU A 137 4.766 6.096 18.424 1.00 23.42 C ANISOU 325 CG LEU A 137 2770 3727 2403 781 548 -265 C ATOM 326 CD1 LEU A 137 5.585 5.225 19.312 1.00 22.12 C ANISOU 326 CD1 LEU A 137 2380 3621 2405 1270 398 -155 C ATOM 327 CD2 LEU A 137 5.152 5.847 16.983 1.00 25.08 C ANISOU 327 CD2 LEU A 137 3094 3886 2551 830 541 -473 C ATOM 328 N ALA A 138 4.028 7.209 21.705 1.00 18.61 N ANISOU 328 N ALA A 138 2372 3021 1679 -53 -141 -72 N ATOM 329 CA ALA A 138 4.698 8.343 22.358 1.00 19.52 C ANISOU 329 CA ALA A 138 2578 3098 1742 -85 -198 16 C ATOM 330 C ALA A 138 3.780 9.350 23.068 1.00 19.40 C ANISOU 330 C ALA A 138 2651 3003 1719 -159 -174 100 C ATOM 331 O ALA A 138 4.265 10.325 23.642 1.00 20.81 O ANISOU 331 O ALA A 138 2745 2995 2165 -402 -24 4 O ATOM 332 CB ALA A 138 5.634 9.067 21.378 1.00 19.38 C ANISOU 332 CB ALA A 138 2534 3090 1738 -117 -193 -40 C ATOM 333 N LYS A 139 2.471 9.115 23.039 1.00 18.99 N ANISOU 333 N LYS A 139 2682 3017 1515 -87 -122 418 N ATOM 334 CA LYS A 139 1.515 10.020 23.681 1.00 19.05 C ANISOU 334 CA LYS A 139 2635 2891 1713 -118 -160 672 C ATOM 335 C LYS A 139 1.336 9.678 25.160 1.00 17.07 C ANISOU 335 C LYS A 139 2189 2563 1732 -55 -161 744 C ATOM 336 O LYS A 139 1.603 8.553 25.583 1.00 15.30 O ANISOU 336 O LYS A 139 1848 2486 1479 -66 -275 1037 O ATOM 337 CB LYS A 139 0.151 9.971 22.976 1.00 21.32 C ANISOU 337 CB LYS A 139 3047 3144 1909 -253 -21 904 C ATOM 338 CG LYS A 139 0.132 10.456 21.529 1.00 23.70 C ANISOU 338 CG LYS A 139 3527 3285 2192 -274 116 1040 C ATOM 339 CD LYS A 139 -0.139 11.948 21.427 1.00 26.86 C ANISOU 339 CD LYS A 139 4065 3628 2512 -406 288 1040 C ATOM 340 CE LYS A 139 -0.566 12.347 20.009 1.00 29.27 C ANISOU 340 CE LYS A 139 4531 3848 2742 -626 555 996 C ATOM 341 NZ LYS A 139 0.343 11.792 18.964 1.00 30.84 N1+ ANISOU 341 NZ LYS A 139 4866 3996 2856 -822 601 1095 N1+ ATOM 342 N THR A 140 0.870 10.655 25.935 1.00 16.91 N ANISOU 342 N THR A 140 2180 2363 1884 18 -259 443 N ATOM 343 CA THR A 140 0.639 10.468 27.362 1.00 16.74 C ANISOU 343 CA THR A 140 2077 2216 2066 241 -300 189 C ATOM 344 C THR A 140 -0.341 9.331 27.619 1.00 16.12 C ANISOU 344 C THR A 140 1876 2176 2074 356 -400 219 C ATOM 345 O THR A 140 -1.374 9.214 26.963 1.00 16.49 O ANISOU 345 O THR A 140 1750 2259 2257 243 -655 460 O ATOM 346 CB THR A 140 0.100 11.750 28.025 1.00 17.41 C ANISOU 346 CB THR A 140 2292 2122 2200 446 -346 -102 C ATOM 347 CG2 THR A 140 -0.169 11.528 29.510 1.00 17.59 C ANISOU 347 CG2 THR A 140 2419 2129 2134 521 -576 -67 C ATOM 348 OG1 THR A 140 1.060 12.799 27.876 1.00 19.02 O ANISOU 348 OG1 THR A 140 2434 2399 2393 408 -180 -116 O ATOM 349 N CYS A 141 0.009 8.491 28.583 1.00 15.79 N ANISOU 349 N CYS A 141 1802 2161 2038 485 -260 104 N ATOM 350 CA ACYS A 141 -0.841 7.385 29.003 0.39 14.90 C ANISOU 350 CA ACYS A 141 1742 1945 1975 311 -208 -48 C ATOM 351 CA BCYS A 141 -0.830 7.380 28.989 0.61 15.53 C ANISOU 351 CA BCYS A 141 1745 2091 2066 332 -265 -147 C ATOM 352 C CYS A 141 -0.974 7.402 30.513 1.00 14.29 C ANISOU 352 C CYS A 141 1723 1887 1818 248 -146 120 C ATOM 353 O CYS A 141 -0.119 6.873 31.225 1.00 12.06 O ANISOU 353 O CYS A 141 1267 1815 1500 213 -241 285 O ATOM 354 CB ACYS A 141 -0.244 6.053 28.566 0.39 15.41 C ANISOU 354 CB ACYS A 141 1818 2007 2032 160 -147 -276 C ATOM 355 CB BCYS A 141 -0.190 6.074 28.521 0.61 17.65 C ANISOU 355 CB BCYS A 141 1896 2526 2284 211 -265 -531 C ATOM 356 SG ACYS A 141 -0.046 5.884 26.804 0.39 15.76 S ANISOU 356 SG ACYS A 141 1841 2081 2066 93 -77 -428 S ATOM 357 SG BCYS A 141 -1.194 4.611 28.728 0.61 19.44 S ANISOU 357 SG BCYS A 141 1975 2927 2484 223 -287 -781 S ATOM 358 N PRO A 142 -2.045 8.034 31.017 1.00 14.31 N ANISOU 358 N PRO A 142 2086 1713 1639 293 -155 63 N ATOM 359 CA PRO A 142 -2.205 8.125 32.472 1.00 14.41 C ANISOU 359 CA PRO A 142 2250 1665 1559 319 -107 -61 C ATOM 360 C PRO A 142 -2.581 6.790 33.115 1.00 13.72 C ANISOU 360 C PRO A 142 2141 1513 1560 369 -160 -248 C ATOM 361 O PRO A 142 -3.496 6.107 32.657 1.00 13.86 O ANISOU 361 O PRO A 142 2074 1679 1515 534 -185 -224 O ATOM 362 CB PRO A 142 -3.353 9.129 32.644 1.00 16.08 C ANISOU 362 CB PRO A 142 2533 1874 1703 433 -91 -48 C ATOM 363 CG PRO A 142 -3.460 9.847 31.327 1.00 15.03 C ANISOU 363 CG PRO A 142 2433 1758 1520 502 -189 -97 C ATOM 364 CD PRO A 142 -3.058 8.829 30.301 1.00 14.22 C ANISOU 364 CD PRO A 142 2247 1722 1432 397 -175 -45 C ATOM 365 N VAL A 143 -1.858 6.430 34.169 1.00 13.55 N ANISOU 365 N VAL A 143 2057 1454 1636 305 -239 -218 N ATOM 366 CA VAL A 143 -2.189 5.271 34.982 1.00 13.81 C ANISOU 366 CA VAL A 143 2041 1382 1823 -70 -139 -260 C ATOM 367 C VAL A 143 -2.216 5.724 36.433 1.00 14.21 C ANISOU 367 C VAL A 143 2013 1417 1970 -156 -197 -309 C ATOM 368 O VAL A 143 -1.297 6.403 36.894 1.00 13.56 O ANISOU 368 O VAL A 143 2108 1203 1842 -167 -353 -762 O ATOM 369 CB VAL A 143 -1.175 4.118 34.807 1.00 13.88 C ANISOU 369 CB VAL A 143 2180 1300 1792 -77 -122 -185 C ATOM 370 CG1 VAL A 143 -1.585 2.921 35.664 1.00 12.36 C ANISOU 370 CG1 VAL A 143 1944 1093 1661 -236 -297 -211 C ATOM 371 CG2 VAL A 143 -1.074 3.704 33.348 1.00 14.16 C ANISOU 371 CG2 VAL A 143 2225 1445 1708 -195 -258 63 C ATOM 372 N GLN A 144 -3.279 5.364 37.145 1.00 14.14 N ANISOU 372 N GLN A 144 1702 1551 2120 112 110 -216 N ATOM 373 CA GLN A 144 -3.437 5.770 38.532 1.00 13.58 C ANISOU 373 CA GLN A 144 1662 1397 2099 464 89 -285 C ATOM 374 C GLN A 144 -3.049 4.654 39.483 1.00 13.79 C ANISOU 374 C GLN A 144 1505 1694 2040 401 45 -267 C ATOM 375 O GLN A 144 -3.452 3.506 39.303 1.00 14.70 O ANISOU 375 O GLN A 144 1632 1831 2123 426 -192 -133 O ATOM 376 CB GLN A 144 -4.888 6.190 38.804 1.00 13.05 C ANISOU 376 CB GLN A 144 1744 1071 2145 494 -97 -211 C ATOM 377 CG GLN A 144 -5.338 7.425 38.034 1.00 13.57 C ANISOU 377 CG GLN A 144 1983 1026 2147 486 -371 -302 C ATOM 378 CD GLN A 144 -6.823 7.629 38.115 1.00 15.44 C ANISOU 378 CD GLN A 144 2415 1249 2202 336 -769 -166 C ATOM 379 NE2 GLN A 144 -7.284 8.816 37.729 1.00 16.87 N ANISOU 379 NE2 GLN A 144 2769 1280 2359 284 -785 -27 N ATOM 380 OE1 GLN A 144 -7.555 6.733 38.533 1.00 16.85 O ANISOU 380 OE1 GLN A 144 2517 1749 2137 250 -881 -301 O ATOM 381 N LEU A 145 -2.267 5.003 40.498 1.00 12.48 N ANISOU 381 N LEU A 145 1075 1870 1797 166 35 -417 N ATOM 382 CA LEU A 145 -1.950 4.078 41.577 1.00 13.90 C ANISOU 382 CA LEU A 145 1191 2249 1841 128 71 -591 C ATOM 383 C LEU A 145 -2.867 4.374 42.765 1.00 15.49 C ANISOU 383 C LEU A 145 1751 2405 1729 161 197 -339 C ATOM 384 O LEU A 145 -2.820 5.472 43.326 1.00 16.70 O ANISOU 384 O LEU A 145 2079 2441 1826 183 130 -397 O ATOM 385 CB LEU A 145 -0.491 4.248 42.004 1.00 14.80 C ANISOU 385 CB LEU A 145 1227 2332 2066 74 -14 -866 C ATOM 386 CG LEU A 145 0.543 4.311 40.882 1.00 15.74 C ANISOU 386 CG LEU A 145 1403 2413 2164 -2 -87 -1267 C ATOM 387 CD1 LEU A 145 1.937 4.514 41.458 1.00 17.37 C ANISOU 387 CD1 LEU A 145 1527 2674 2399 40 -143 -1225 C ATOM 388 CD2 LEU A 145 0.481 3.041 40.056 1.00 16.46 C ANISOU 388 CD2 LEU A 145 1780 2352 2123 28 156 -1320 C ATOM 389 N TRP A 146 -3.703 3.406 43.138 1.00 15.32 N ANISOU 389 N TRP A 146 1876 2405 1541 204 425 220 N ATOM 390 CA TRP A 146 -4.569 3.540 44.313 1.00 15.45 C ANISOU 390 CA TRP A 146 1944 2433 1494 425 495 357 C ATOM 391 C TRP A 146 -4.086 2.618 45.424 1.00 16.54 C ANISOU 391 C TRP A 146 2344 2588 1351 422 403 412 C ATOM 392 O TRP A 146 -3.709 1.470 45.170 1.00 16.48 O ANISOU 392 O TRP A 146 2497 2594 1171 356 520 402 O ATOM 393 CB TRP A 146 -6.026 3.199 43.969 1.00 15.10 C ANISOU 393 CB TRP A 146 1710 2260 1767 386 433 570 C ATOM 394 CG TRP A 146 -6.682 4.163 43.021 1.00 15.92 C ANISOU 394 CG TRP A 146 1652 2287 2111 512 430 562 C ATOM 395 CD1 TRP A 146 -6.387 4.341 41.704 1.00 16.30 C ANISOU 395 CD1 TRP A 146 1620 2274 2298 540 337 590 C ATOM 396 CD2 TRP A 146 -7.759 5.067 43.312 1.00 17.14 C ANISOU 396 CD2 TRP A 146 1662 2540 2308 535 488 621 C ATOM 397 CE2 TRP A 146 -8.052 5.765 42.125 1.00 16.13 C ANISOU 397 CE2 TRP A 146 1454 2424 2251 581 538 753 C ATOM 398 CE3 TRP A 146 -8.500 5.355 44.465 1.00 18.00 C ANISOU 398 CE3 TRP A 146 1786 2664 2389 562 538 512 C ATOM 399 NE1 TRP A 146 -7.201 5.303 41.158 1.00 16.32 N ANISOU 399 NE1 TRP A 146 1477 2389 2337 382 347 647 N ATOM 400 CZ2 TRP A 146 -9.056 6.738 42.056 1.00 17.01 C ANISOU 400 CZ2 TRP A 146 1419 2630 2413 702 642 594 C ATOM 401 CZ3 TRP A 146 -9.494 6.319 44.393 1.00 17.77 C ANISOU 401 CZ3 TRP A 146 1627 2743 2382 834 546 471 C ATOM 402 CH2 TRP A 146 -9.761 6.999 43.201 1.00 17.45 C ANISOU 402 CH2 TRP A 146 1497 2725 2410 844 609 463 C ATOM 403 N VAL A 147 -4.091 3.129 46.653 1.00 17.40 N ANISOU 403 N VAL A 147 2461 2790 1360 393 54 470 N ATOM 404 CA VAL A 147 -3.747 2.333 47.832 1.00 18.71 C ANISOU 404 CA VAL A 147 2491 3038 1580 530 206 386 C ATOM 405 C VAL A 147 -4.723 2.625 48.974 1.00 20.64 C ANISOU 405 C VAL A 147 2605 3414 1825 398 219 63 C ATOM 406 O VAL A 147 -5.228 3.748 49.100 1.00 20.59 O ANISOU 406 O VAL A 147 2463 3482 1879 595 305 -282 O ATOM 407 CB VAL A 147 -2.293 2.597 48.320 1.00 17.87 C ANISOU 407 CB VAL A 147 2266 2899 1625 719 -9 495 C ATOM 408 CG1 VAL A 147 -1.277 2.172 47.272 1.00 17.99 C ANISOU 408 CG1 VAL A 147 2184 3006 1646 765 14 593 C ATOM 409 CG2 VAL A 147 -2.099 4.061 48.675 1.00 18.61 C ANISOU 409 CG2 VAL A 147 2265 3047 1761 421 -32 420 C ATOM 410 N ASP A 148 -4.993 1.614 49.794 1.00 21.27 N ANISOU 410 N ASP A 148 2735 3495 1850 267 240 185 N ATOM 411 CA ASP A 148 -5.829 1.799 50.978 1.00 22.43 C ANISOU 411 CA ASP A 148 2866 3692 1963 305 531 -64 C ATOM 412 C ASP A 148 -5.029 2.440 52.113 1.00 22.90 C ANISOU 412 C ASP A 148 3049 3817 1837 457 633 -12 C ATOM 413 O ASP A 148 -5.578 3.172 52.934 1.00 22.78 O ANISOU 413 O ASP A 148 3255 3860 1539 581 704 -66 O ATOM 414 CB ASP A 148 -6.414 0.466 51.453 1.00 24.91 C ANISOU 414 CB ASP A 148 3150 3842 2471 436 393 -255 C ATOM 415 CG ASP A 148 -7.337 -0.170 50.435 1.00 27.10 C ANISOU 415 CG ASP A 148 3345 4019 2931 386 436 -195 C ATOM 416 OD1 ASP A 148 -7.927 0.561 49.608 1.00 27.47 O ANISOU 416 OD1 ASP A 148 3377 4067 2995 317 317 -208 O ATOM 417 OD2 ASP A 148 -7.477 -1.413 50.468 1.00 28.54 O1- ANISOU 417 OD2 ASP A 148 3445 4228 3171 340 568 -194 O1- ATOM 418 N SER A 149 -3.732 2.149 52.149 1.00 23.68 N ANISOU 418 N SER A 149 3063 3881 2053 532 396 27 N ATOM 419 CA SER A 149 -2.825 2.700 53.148 1.00 24.52 C ANISOU 419 CA SER A 149 3027 3995 2295 316 375 230 C ATOM 420 C SER A 149 -1.537 3.156 52.468 1.00 23.26 C ANISOU 420 C SER A 149 2672 3861 2305 268 295 133 C ATOM 421 O SER A 149 -1.071 2.512 51.531 1.00 21.04 O ANISOU 421 O SER A 149 2473 3660 1859 458 205 257 O ATOM 422 CB SER A 149 -2.502 1.648 54.204 1.00 26.57 C ANISOU 422 CB SER A 149 3263 4269 2562 278 365 498 C ATOM 423 OG SER A 149 -3.581 0.754 54.369 1.00 28.88 O ANISOU 423 OG SER A 149 3683 4548 2741 540 247 571 O ATOM 424 N THR A 150 -0.964 4.259 52.948 1.00 24.55 N ANISOU 424 N THR A 150 2741 3977 2610 76 256 -153 N ATOM 425 CA THR A 150 0.270 4.808 52.378 1.00 25.42 C ANISOU 425 CA THR A 150 2713 4087 2861 -202 242 -501 C ATOM 426 C THR A 150 1.476 3.908 52.658 1.00 24.97 C ANISOU 426 C THR A 150 2485 4265 2737 -553 148 -702 C ATOM 427 O THR A 150 1.763 3.595 53.810 1.00 25.06 O ANISOU 427 O THR A 150 2311 4346 2865 -700 78 -875 O ATOM 428 CB THR A 150 0.566 6.221 52.922 1.00 27.56 C ANISOU 428 CB THR A 150 3106 4165 3200 -227 101 -529 C ATOM 429 CG2 THR A 150 1.802 6.799 52.264 1.00 27.44 C ANISOU 429 CG2 THR A 150 3204 4015 3206 -307 130 -575 C ATOM 430 OG1 THR A 150 -0.549 7.088 52.672 1.00 29.81 O ANISOU 430 OG1 THR A 150 3514 4364 3448 -314 -11 -508 O ATOM 431 N PRO A 151 2.189 3.494 51.592 1.00 24.59 N ANISOU 431 N PRO A 151 2488 4366 2491 -573 58 -717 N ATOM 432 CA PRO A 151 3.375 2.632 51.674 1.00 24.46 C ANISOU 432 CA PRO A 151 2435 4482 2376 -578 258 -654 C ATOM 433 C PRO A 151 4.564 3.380 52.276 1.00 25.48 C ANISOU 433 C PRO A 151 2590 4706 2384 -838 272 -528 C ATOM 434 O PRO A 151 4.558 4.610 52.275 1.00 26.58 O ANISOU 434 O PRO A 151 2723 4842 2535 -845 588 -708 O ATOM 435 CB PRO A 151 3.655 2.282 50.204 1.00 24.14 C ANISOU 435 CB PRO A 151 2355 4481 2336 -336 223 -747 C ATOM 436 CG PRO A 151 2.400 2.584 49.478 1.00 23.85 C ANISOU 436 CG PRO A 151 2292 4414 2356 -316 113 -718 C ATOM 437 CD PRO A 151 1.808 3.747 50.196 1.00 24.65 C ANISOU 437 CD PRO A 151 2521 4427 2416 -425 -31 -649 C ATOM 438 N PRO A 152 5.566 2.645 52.787 1.00 26.22 N ANISOU 438 N PRO A 152 2772 4872 2320 -1069 -266 -242 N ATOM 439 CA PRO A 152 6.740 3.213 53.464 1.00 26.65 C ANISOU 439 CA PRO A 152 2839 4929 2356 -1317 -698 -262 C ATOM 440 C PRO A 152 7.491 4.261 52.644 1.00 27.13 C ANISOU 440 C PRO A 152 3000 4957 2352 -1434 -694 -533 C ATOM 441 O PRO A 152 7.351 4.307 51.417 1.00 26.92 O ANISOU 441 O PRO A 152 2894 4914 2422 -1245 -796 -596 O ATOM 442 CB PRO A 152 7.647 1.994 53.657 1.00 27.28 C ANISOU 442 CB PRO A 152 2873 5028 2464 -1351 -875 -73 C ATOM 443 CG PRO A 152 6.716 0.838 53.720 1.00 27.61 C ANISOU 443 CG PRO A 152 2853 5151 2487 -1317 -824 56 C ATOM 444 CD PRO A 152 5.609 1.171 52.763 1.00 26.91 C ANISOU 444 CD PRO A 152 2840 5039 2344 -1278 -551 -52 C ATOM 445 N PRO A 153 8.290 5.101 53.326 1.00 28.53 N ANISOU 445 N PRO A 153 3465 5030 2343 -1619 -346 -696 N ATOM 446 CA PRO A 153 9.246 5.982 52.648 1.00 28.30 C ANISOU 446 CA PRO A 153 3491 4959 2301 -1496 -139 -666 C ATOM 447 C PRO A 153 10.160 5.127 51.793 1.00 26.53 C ANISOU 447 C PRO A 153 3111 4740 2229 -1356 -295 -572 C ATOM 448 O PRO A 153 10.564 4.058 52.253 1.00 28.14 O ANISOU 448 O PRO A 153 3300 5043 2350 -1220 -371 -555 O ATOM 449 CB PRO A 153 10.070 6.569 53.801 1.00 28.87 C ANISOU 449 CB PRO A 153 3602 5034 2332 -1624 -38 -796 C ATOM 450 CG PRO A 153 9.198 6.462 55.003 1.00 29.38 C ANISOU 450 CG PRO A 153 3783 5085 2296 -1708 -67 -675 C ATOM 451 CD PRO A 153 8.304 5.272 54.792 1.00 29.25 C ANISOU 451 CD PRO A 153 3679 5112 2320 -1689 -113 -653 C ATOM 452 N GLY A 154 10.469 5.564 50.577 1.00 22.91 N ANISOU 452 N GLY A 154 2565 4246 1893 -1375 -395 -419 N ATOM 453 CA GLY A 154 11.402 4.828 49.742 1.00 19.85 C ANISOU 453 CA GLY A 154 2040 3801 1701 -932 -247 -326 C ATOM 454 C GLY A 154 10.764 3.766 48.869 1.00 18.54 C ANISOU 454 C GLY A 154 1868 3493 1684 -347 -108 -135 C ATOM 455 O GLY A 154 11.460 3.067 48.137 1.00 19.07 O ANISOU 455 O GLY A 154 1845 3318 2081 230 -265 -197 O ATOM 456 N THR A 155 9.442 3.638 48.950 1.00 16.97 N ANISOU 456 N THR A 155 1614 3405 1427 -78 -365 71 N ATOM 457 CA THR A 155 8.702 2.710 48.101 1.00 15.73 C ANISOU 457 CA THR A 155 1518 3123 1335 17 -344 302 C ATOM 458 C THR A 155 8.864 3.157 46.648 1.00 16.06 C ANISOU 458 C THR A 155 1565 3125 1411 199 -106 223 C ATOM 459 O THR A 155 8.906 4.360 46.366 1.00 15.88 O ANISOU 459 O THR A 155 1499 3150 1384 84 155 274 O ATOM 460 CB THR A 155 7.193 2.684 48.467 1.00 15.73 C ANISOU 460 CB THR A 155 1551 2921 1506 -313 -305 670 C ATOM 461 CG2 THR A 155 6.404 1.793 47.518 1.00 15.24 C ANISOU 461 CG2 THR A 155 1298 2888 1605 -462 -469 762 C ATOM 462 OG1 THR A 155 7.028 2.204 49.803 1.00 17.00 O ANISOU 462 OG1 THR A 155 1598 2901 1962 -153 -374 736 O ATOM 463 N ARG A 156 8.966 2.187 45.739 1.00 15.22 N ANISOU 463 N ARG A 156 1489 2955 1338 226 -452 40 N ATOM 464 CA ARG A 156 9.069 2.447 44.304 1.00 13.98 C ANISOU 464 CA ARG A 156 1488 2609 1217 50 -361 -172 C ATOM 465 C ARG A 156 8.009 1.647 43.544 1.00 14.27 C ANISOU 465 C ARG A 156 1660 2551 1211 148 -68 -57 C ATOM 466 O ARG A 156 7.504 0.646 44.049 1.00 15.01 O ANISOU 466 O ARG A 156 1923 2608 1173 68 -115 -60 O ATOM 467 CB ARG A 156 10.469 2.078 43.798 1.00 12.90 C ANISOU 467 CB ARG A 156 1051 2305 1543 201 -475 -212 C ATOM 468 CG ARG A 156 11.496 3.191 43.957 1.00 14.14 C ANISOU 468 CG ARG A 156 1189 2426 1758 494 -486 -166 C ATOM 469 CD ARG A 156 12.823 2.692 44.510 1.00 15.58 C ANISOU 469 CD ARG A 156 1569 2403 1949 413 -407 -376 C ATOM 470 NE ARG A 156 13.508 1.696 43.678 1.00 15.74 N ANISOU 470 NE ARG A 156 1842 2359 1779 267 -408 -518 N ATOM 471 CZ ARG A 156 14.348 1.983 42.684 1.00 15.96 C ANISOU 471 CZ ARG A 156 2116 2337 1610 92 -690 -553 C ATOM 472 NH1 ARG A 156 14.591 3.241 42.355 1.00 16.14 N1+ ANISOU 472 NH1 ARG A 156 2224 2273 1635 18 -556 -582 N1+ ATOM 473 NH2 ARG A 156 14.939 1.009 42.005 1.00 16.36 N ANISOU 473 NH2 ARG A 156 2205 2485 1525 7 -921 -369 N ATOM 474 N PHE A 157 7.655 2.092 42.341 1.00 12.23 N ANISOU 474 N PHE A 157 1511 2173 964 235 55 -208 N ATOM 475 CA PHE A 157 6.804 1.273 41.484 1.00 11.74 C ANISOU 475 CA PHE A 157 1578 1946 936 376 18 -260 C ATOM 476 C PHE A 157 7.421 1.100 40.108 1.00 11.57 C ANISOU 476 C PHE A 157 1625 1839 931 196 -46 -234 C ATOM 477 O PHE A 157 7.967 2.042 39.546 1.00 12.93 O ANISOU 477 O PHE A 157 1999 2005 911 225 -207 -580 O ATOM 478 CB PHE A 157 5.369 1.801 41.403 1.00 13.03 C ANISOU 478 CB PHE A 157 1805 2002 1144 694 17 -255 C ATOM 479 CG PHE A 157 5.251 3.170 40.822 1.00 14.33 C ANISOU 479 CG PHE A 157 2060 2136 1251 927 -162 -220 C ATOM 480 CD1 PHE A 157 5.377 4.288 41.632 1.00 16.00 C ANISOU 480 CD1 PHE A 157 2432 2252 1396 999 -486 -180 C ATOM 481 CD2 PHE A 157 4.976 3.345 39.474 1.00 14.36 C ANISOU 481 CD2 PHE A 157 2034 2075 1348 1194 -151 -215 C ATOM 482 CE1 PHE A 157 5.255 5.564 41.111 1.00 16.68 C ANISOU 482 CE1 PHE A 157 2502 2378 1458 1205 -642 -148 C ATOM 483 CE2 PHE A 157 4.853 4.616 38.941 1.00 15.66 C ANISOU 483 CE2 PHE A 157 2271 2229 1449 1331 -327 -260 C ATOM 484 CZ PHE A 157 4.993 5.728 39.760 1.00 17.43 C ANISOU 484 CZ PHE A 157 2587 2390 1645 1235 -615 -86 C ATOM 485 N ARG A 158 7.322 -0.115 39.582 1.00 11.94 N ANISOU 485 N ARG A 158 1651 1745 1140 361 -272 -68 N ATOM 486 CA ARG A 158 8.039 -0.534 38.383 1.00 10.91 C ANISOU 486 CA ARG A 158 1350 1666 1128 453 -178 57 C ATOM 487 C ARG A 158 7.062 -0.997 37.295 1.00 11.69 C ANISOU 487 C ARG A 158 1435 1880 1127 282 -40 222 C ATOM 488 O ARG A 158 6.078 -1.671 37.589 1.00 12.81 O ANISOU 488 O ARG A 158 1553 2148 1165 -74 117 235 O ATOM 489 CB ARG A 158 8.973 -1.691 38.747 1.00 10.41 C ANISOU 489 CB ARG A 158 1207 1536 1212 522 -275 -16 C ATOM 490 CG ARG A 158 9.838 -2.196 37.600 1.00 11.31 C ANISOU 490 CG ARG A 158 1521 1457 1319 681 -333 -118 C ATOM 491 CD ARG A 158 10.760 -3.314 38.068 1.00 10.91 C ANISOU 491 CD ARG A 158 1285 1556 1305 462 -370 -120 C ATOM 492 NE ARG A 158 11.547 -2.897 39.227 1.00 12.07 N ANISOU 492 NE ARG A 158 1309 1823 1453 137 -264 -69 N ATOM 493 CZ ARG A 158 12.743 -2.321 39.157 1.00 12.20 C ANISOU 493 CZ ARG A 158 1266 1851 1519 108 -286 -277 C ATOM 494 NH1 ARG A 158 13.310 -2.106 37.978 1.00 11.88 N1+ ANISOU 494 NH1 ARG A 158 1135 1880 1500 169 -173 -316 N1+ ATOM 495 NH2 ARG A 158 13.375 -1.966 40.270 1.00 12.15 N ANISOU 495 NH2 ARG A 158 1327 1859 1430 61 -216 -389 N ATOM 496 N ALA A 159 7.330 -0.639 36.041 1.00 10.95 N ANISOU 496 N ALA A 159 1245 1671 1242 175 -29 65 N ATOM 497 CA ALA A 159 6.529 -1.137 34.922 1.00 9.76 C ANISOU 497 CA ALA A 159 1134 1369 1207 140 -157 -15 C ATOM 498 C ALA A 159 7.400 -1.981 34.006 1.00 11.71 C ANISOU 498 C ALA A 159 1345 1747 1357 -139 -5 -310 C ATOM 499 O ALA A 159 8.541 -1.620 33.710 1.00 12.59 O ANISOU 499 O ALA A 159 1365 2149 1271 -462 197 -192 O ATOM 500 CB ALA A 159 5.922 0.004 34.144 1.00 7.94 C ANISOU 500 CB ALA A 159 945 1042 1031 403 -407 72 C ATOM 501 N MET A 160 6.849 -3.105 33.564 1.00 11.50 N ANISOU 501 N MET A 160 1293 1517 1560 -28 -98 -485 N ATOM 502 CA MET A 160 7.544 -4.028 32.675 1.00 12.83 C ANISOU 502 CA MET A 160 1409 1658 1807 204 -161 -290 C ATOM 503 C MET A 160 6.537 -4.630 31.704 1.00 12.74 C ANISOU 503 C MET A 160 1338 1792 1712 285 -167 -267 C ATOM 504 O MET A 160 5.415 -4.957 32.093 1.00 13.40 O ANISOU 504 O MET A 160 1108 2235 1749 180 -225 -186 O ATOM 505 CB MET A 160 8.196 -5.143 33.494 1.00 14.18 C ANISOU 505 CB MET A 160 1598 1645 2146 556 -307 -331 C ATOM 506 CG MET A 160 8.853 -6.233 32.667 1.00 15.51 C ANISOU 506 CG MET A 160 1682 1703 2511 509 -433 102 C ATOM 507 SD MET A 160 9.434 -7.587 33.703 1.00 18.00 S ANISOU 507 SD MET A 160 1797 2178 2865 352 -713 244 S ATOM 508 CE MET A 160 10.573 -6.728 34.781 1.00 17.47 C ANISOU 508 CE MET A 160 1882 1945 2811 298 -992 -58 C ATOM 509 N ALA A 161 6.928 -4.777 30.443 1.00 11.83 N ANISOU 509 N ALA A 161 1346 1592 1556 406 -413 -294 N ATOM 510 CA ALA A 161 6.046 -5.383 29.453 1.00 13.05 C ANISOU 510 CA ALA A 161 1744 1520 1696 392 -176 -376 C ATOM 511 C ALA A 161 6.441 -6.834 29.184 1.00 13.51 C ANISOU 511 C ALA A 161 1673 1710 1749 251 121 -292 C ATOM 512 O ALA A 161 7.624 -7.166 29.140 1.00 13.65 O ANISOU 512 O ALA A 161 1556 1849 1782 347 217 -178 O ATOM 513 CB ALA A 161 6.053 -4.575 28.159 1.00 12.73 C ANISOU 513 CB ALA A 161 1989 1442 1405 255 -525 -525 C ATOM 514 N ILE A 162 5.443 -7.698 29.026 1.00 13.99 N ANISOU 514 N ILE A 162 1816 1806 1694 229 138 -315 N ATOM 515 CA ILE A 162 5.664 -9.066 28.568 1.00 13.28 C ANISOU 515 CA ILE A 162 1683 1754 1608 -13 93 -310 C ATOM 516 C ILE A 162 4.665 -9.384 27.458 1.00 14.12 C ANISOU 516 C ILE A 162 1667 1911 1787 -205 -24 -265 C ATOM 517 O ILE A 162 3.624 -8.733 27.352 1.00 13.43 O ANISOU 517 O ILE A 162 1561 1899 1643 -348 -391 -164 O ATOM 518 CB ILE A 162 5.532 -10.112 29.709 1.00 13.16 C ANISOU 518 CB ILE A 162 1622 1793 1587 -91 163 -154 C ATOM 519 CG1 ILE A 162 4.099 -10.189 30.231 1.00 13.64 C ANISOU 519 CG1 ILE A 162 1876 1877 1431 -240 163 36 C ATOM 520 CG2 ILE A 162 6.488 -9.810 30.844 1.00 12.50 C ANISOU 520 CG2 ILE A 162 1400 1761 1589 -3 147 -253 C ATOM 521 CD1 ILE A 162 3.864 -11.372 31.152 1.00 13.79 C ANISOU 521 CD1 ILE A 162 2074 1833 1333 -191 142 10 C ATOM 522 N TYR A 163 4.981 -10.372 26.627 1.00 14.97 N ANISOU 522 N TYR A 163 1771 1990 1927 -165 -171 -395 N ATOM 523 CA TYR A 163 4.024 -10.830 25.629 1.00 15.74 C ANISOU 523 CA TYR A 163 1753 2318 1910 -210 -273 -333 C ATOM 524 C TYR A 163 2.889 -11.608 26.281 1.00 17.90 C ANISOU 524 C TYR A 163 2054 2607 2140 -164 -333 -106 C ATOM 525 O TYR A 163 3.116 -12.435 27.163 1.00 18.96 O ANISOU 525 O TYR A 163 2258 2629 2316 -253 -201 -40 O ATOM 526 CB TYR A 163 4.712 -11.638 24.530 1.00 16.68 C ANISOU 526 CB TYR A 163 1805 2462 2068 -281 -281 -584 C ATOM 527 CG TYR A 163 5.505 -10.746 23.609 1.00 17.55 C ANISOU 527 CG TYR A 163 1885 2731 2052 -290 -71 -664 C ATOM 528 CD1 TYR A 163 4.866 -9.793 22.823 1.00 17.16 C ANISOU 528 CD1 TYR A 163 1823 2738 1959 -185 -19 -877 C ATOM 529 CD2 TYR A 163 6.889 -10.827 23.550 1.00 18.30 C ANISOU 529 CD2 TYR A 163 1907 2910 2135 -186 192 -605 C ATOM 530 CE1 TYR A 163 5.584 -8.954 21.992 1.00 17.69 C ANISOU 530 CE1 TYR A 163 1871 2917 1934 -135 71 -825 C ATOM 531 CE2 TYR A 163 7.616 -9.996 22.724 1.00 18.50 C ANISOU 531 CE2 TYR A 163 1917 3032 2080 -163 216 -663 C ATOM 532 CZ TYR A 163 6.957 -9.064 21.947 1.00 18.05 C ANISOU 532 CZ TYR A 163 1843 3023 1991 -133 144 -615 C ATOM 533 OH TYR A 163 7.667 -8.230 21.122 1.00 18.44 O ANISOU 533 OH TYR A 163 1975 3093 1937 -22 -7 -416 O ATOM 534 N LYS A 164 1.666 -11.309 25.857 1.00 18.80 N ANISOU 534 N LYS A 164 2081 2871 2190 -159 -412 -1 N ATOM 535 CA LYS A 164 0.473 -11.896 26.455 1.00 19.87 C ANISOU 535 CA LYS A 164 2220 2952 2376 -194 -269 117 C ATOM 536 C LYS A 164 0.335 -13.384 26.127 1.00 20.91 C ANISOU 536 C LYS A 164 2261 3130 2556 -135 -427 343 C ATOM 537 O LYS A 164 -0.121 -14.170 26.956 1.00 20.99 O ANISOU 537 O LYS A 164 2171 3242 2561 -74 -484 464 O ATOM 538 CB LYS A 164 -0.768 -11.124 25.994 1.00 20.78 C ANISOU 538 CB LYS A 164 2499 2940 2456 -168 75 68 C ATOM 539 CG LYS A 164 -2.079 -11.631 26.559 1.00 23.15 C ANISOU 539 CG LYS A 164 3033 3047 2714 8 328 197 C ATOM 540 CD LYS A 164 -3.242 -10.794 26.049 1.00 25.40 C ANISOU 540 CD LYS A 164 3456 3289 2907 16 420 398 C ATOM 541 CE LYS A 164 -4.559 -11.212 26.679 1.00 28.01 C ANISOU 541 CE LYS A 164 3856 3540 3245 22 393 340 C ATOM 542 NZ LYS A 164 -5.371 -12.028 25.736 1.00 29.74 N1+ ANISOU 542 NZ LYS A 164 4139 3732 3428 95 498 229 N1+ ATOM 543 N GLN A 165 0.737 -13.768 24.919 1.00 22.20 N ANISOU 543 N GLN A 165 2502 3068 2866 -178 -383 108 N ATOM 544 CA GLN A 165 0.603 -15.150 24.472 1.00 23.57 C ANISOU 544 CA GLN A 165 2910 2929 3117 -253 -475 -74 C ATOM 545 C GLN A 165 1.718 -16.003 25.045 1.00 24.17 C ANISOU 545 C GLN A 165 3264 2832 3087 -321 -548 -99 C ATOM 546 O GLN A 165 2.886 -15.630 24.977 1.00 23.27 O ANISOU 546 O GLN A 165 3163 2706 2971 -293 -455 -98 O ATOM 547 CB GLN A 165 0.635 -15.226 22.945 1.00 25.76 C ANISOU 547 CB GLN A 165 3316 3050 3421 -304 -583 -323 C ATOM 548 CG GLN A 165 -0.434 -14.405 22.258 1.00 28.17 C ANISOU 548 CG GLN A 165 3820 3241 3642 -485 -750 -515 C ATOM 549 CD GLN A 165 -0.139 -14.192 20.794 1.00 31.19 C ANISOU 549 CD GLN A 165 4399 3401 4051 -616 -775 -624 C ATOM 550 NE2 GLN A 165 -0.470 -15.180 19.973 1.00 32.84 N ANISOU 550 NE2 GLN A 165 4679 3639 4158 -714 -807 -703 N ATOM 551 OE1 GLN A 165 0.386 -13.152 20.403 1.00 32.81 O ANISOU 551 OE1 GLN A 165 4596 3551 4318 -514 -873 -660 O ATOM 552 N SER A 166 1.351 -17.157 25.593 1.00 25.98 N ANISOU 552 N SER A 166 3615 3002 3255 -247 -766 -295 N ATOM 553 CA SER A 166 2.307 -18.057 26.232 1.00 27.08 C ANISOU 553 CA SER A 166 3897 3001 3391 -95 -889 -335 C ATOM 554 C SER A 166 3.440 -18.498 25.306 1.00 27.38 C ANISOU 554 C SER A 166 3945 2976 3483 71 -778 -507 C ATOM 555 O SER A 166 4.568 -18.698 25.756 1.00 27.08 O ANISOU 555 O SER A 166 3806 3114 3371 24 -938 -569 O ATOM 556 CB SER A 166 1.590 -19.273 26.819 1.00 27.67 C ANISOU 556 CB SER A 166 4072 2961 3479 -384 -1044 -194 C ATOM 557 OG SER A 166 0.787 -19.898 25.840 1.00 29.24 O ANISOU 557 OG SER A 166 4368 3170 3571 -325 -961 -21 O ATOM 558 N GLN A 167 3.154 -18.638 24.014 1.00 27.69 N ANISOU 558 N GLN A 167 3993 2842 3687 128 -563 -624 N ATOM 559 CA GLN A 167 4.193 -19.065 23.072 1.00 28.86 C ANISOU 559 CA GLN A 167 4014 3010 3942 153 -499 -721 C ATOM 560 C GLN A 167 5.206 -17.955 22.753 1.00 27.08 C ANISOU 560 C GLN A 167 3759 2703 3829 127 -290 -1080 C ATOM 561 O GLN A 167 6.171 -18.177 22.020 1.00 27.67 O ANISOU 561 O GLN A 167 3972 2529 4013 -26 -311 -1268 O ATOM 562 CB GLN A 167 3.595 -19.659 21.786 1.00 31.42 C ANISOU 562 CB GLN A 167 4269 3375 4295 157 -560 -549 C ATOM 563 CG GLN A 167 3.032 -18.645 20.799 1.00 34.15 C ANISOU 563 CG GLN A 167 4520 3831 4623 138 -613 -434 C ATOM 564 CD GLN A 167 1.563 -18.343 21.035 1.00 36.75 C ANISOU 564 CD GLN A 167 4892 4251 4821 126 -807 -306 C ATOM 565 NE2 GLN A 167 0.887 -17.861 19.997 1.00 36.87 N ANISOU 565 NE2 GLN A 167 4925 4302 4782 100 -1046 -162 N ATOM 566 OE1 GLN A 167 1.038 -18.550 22.135 1.00 37.87 O ANISOU 566 OE1 GLN A 167 5054 4453 4883 218 -691 -353 O ATOM 567 N HIS A 168 4.993 -16.768 23.313 1.00 25.63 N ANISOU 567 N HIS A 168 3309 2865 3566 189 -239 -1244 N ATOM 568 CA HIS A 168 5.913 -15.650 23.112 1.00 23.66 C ANISOU 568 CA HIS A 168 2813 2879 3299 71 -171 -1284 C ATOM 569 C HIS A 168 6.443 -15.083 24.428 1.00 22.64 C ANISOU 569 C HIS A 168 2573 2911 3117 -115 -275 -1087 C ATOM 570 O HIS A 168 7.284 -14.185 24.421 1.00 21.72 O ANISOU 570 O HIS A 168 2343 2901 3010 -313 -293 -1017 O ATOM 571 CB HIS A 168 5.234 -14.519 22.333 1.00 23.15 C ANISOU 571 CB HIS A 168 2743 2897 3158 156 -237 -1446 C ATOM 572 CG HIS A 168 4.785 -14.907 20.960 1.00 23.06 C ANISOU 572 CG HIS A 168 2799 2877 3088 197 -396 -1624 C ATOM 573 CD2 HIS A 168 3.621 -14.679 20.309 1.00 22.80 C ANISOU 573 CD2 HIS A 168 2657 2905 3102 131 -439 -1709 C ATOM 574 ND1 HIS A 168 5.587 -15.603 20.083 1.00 23.87 N ANISOU 574 ND1 HIS A 168 2866 2977 3228 109 -498 -1600 N ATOM 575 CE1 HIS A 168 4.934 -15.796 18.951 1.00 23.47 C ANISOU 575 CE1 HIS A 168 2808 2924 3185 128 -649 -1697 C ATOM 576 NE2 HIS A 168 3.738 -15.245 19.062 1.00 23.57 N ANISOU 576 NE2 HIS A 168 2824 2908 3223 111 -671 -1712 N ATOM 577 N MET A 169 5.950 -15.604 25.550 1.00 23.13 N ANISOU 577 N MET A 169 2698 2916 3173 -35 -253 -945 N ATOM 578 CA MET A 169 6.236 -15.019 26.868 1.00 24.06 C ANISOU 578 CA MET A 169 2923 2939 3280 50 -166 -819 C ATOM 579 C MET A 169 7.719 -14.918 27.243 1.00 22.28 C ANISOU 579 C MET A 169 2683 2685 3099 259 -318 -1015 C ATOM 580 O MET A 169 8.120 -13.980 27.938 1.00 21.53 O ANISOU 580 O MET A 169 2675 2598 2907 488 -456 -1141 O ATOM 581 CB MET A 169 5.439 -15.726 27.978 1.00 26.53 C ANISOU 581 CB MET A 169 3312 3238 3528 -344 134 -427 C ATOM 582 CG MET A 169 3.940 -15.429 27.932 1.00 30.06 C ANISOU 582 CG MET A 169 4005 3570 3845 -750 288 -63 C ATOM 583 SD MET A 169 2.938 -16.091 29.282 1.00 33.33 S ANISOU 583 SD MET A 169 4681 3895 4087 -1006 546 268 S ATOM 584 CE MET A 169 3.323 -14.935 30.581 1.00 33.02 C ANISOU 584 CE MET A 169 4735 3755 4057 -915 512 230 C ATOM 585 N THR A 170 8.532 -15.865 26.779 1.00 21.99 N ANISOU 585 N THR A 170 2608 2708 3039 344 -234 -1084 N ATOM 586 CA THR A 170 9.959 -15.859 27.105 1.00 21.46 C ANISOU 586 CA THR A 170 2354 2655 3146 532 -261 -1091 C ATOM 587 C THR A 170 10.742 -14.839 26.287 1.00 21.20 C ANISOU 587 C THR A 170 2221 2894 2939 397 -156 -962 C ATOM 588 O THR A 170 11.886 -14.529 26.604 1.00 22.27 O ANISOU 588 O THR A 170 2342 3131 2989 301 -118 -896 O ATOM 589 CB THR A 170 10.606 -17.243 26.913 1.00 21.89 C ANISOU 589 CB THR A 170 2567 2439 3310 734 -334 -1249 C ATOM 590 CG2 THR A 170 9.879 -18.296 27.735 1.00 20.56 C ANISOU 590 CG2 THR A 170 2429 2131 3251 813 -295 -1168 C ATOM 591 OG1 THR A 170 10.577 -17.591 25.524 1.00 22.83 O ANISOU 591 OG1 THR A 170 2776 2444 3455 1151 -320 -1207 O ATOM 592 N GLU A 171 10.133 -14.323 25.229 1.00 20.22 N ANISOU 592 N GLU A 171 2041 2871 2771 370 -25 -893 N ATOM 593 CA GLU A 171 10.796 -13.305 24.422 1.00 21.17 C ANISOU 593 CA GLU A 171 2255 3003 2787 293 43 -823 C ATOM 594 C GLU A 171 10.726 -11.943 25.110 1.00 19.83 C ANISOU 594 C GLU A 171 1862 2907 2766 76 119 -694 C ATOM 595 O GLU A 171 9.668 -11.521 25.584 1.00 17.92 O ANISOU 595 O GLU A 171 1271 2697 2843 -33 146 -680 O ATOM 596 CB GLU A 171 10.192 -13.226 23.016 1.00 23.83 C ANISOU 596 CB GLU A 171 2836 3361 2857 331 183 -538 C ATOM 597 CG GLU A 171 10.857 -12.194 22.113 1.00 25.24 C ANISOU 597 CG GLU A 171 3235 3490 2864 196 361 -371 C ATOM 598 CD GLU A 171 10.348 -12.236 20.680 1.00 27.52 C ANISOU 598 CD GLU A 171 3730 3723 3004 68 589 -255 C ATOM 599 OE1 GLU A 171 9.910 -13.316 20.223 1.00 28.42 O ANISOU 599 OE1 GLU A 171 3974 3864 2961 81 681 -491 O ATOM 600 OE2 GLU A 171 10.383 -11.181 20.012 1.00 28.26 O1- ANISOU 600 OE2 GLU A 171 3846 3855 3038 -49 576 40 O1- ATOM 601 N VAL A 172 11.861 -11.261 25.176 1.00 18.88 N ANISOU 601 N VAL A 172 1723 2943 2506 88 184 -669 N ATOM 602 CA VAL A 172 11.909 -9.945 25.798 1.00 17.79 C ANISOU 602 CA VAL A 172 1812 2851 2094 139 -14 -371 C ATOM 603 C VAL A 172 11.234 -8.916 24.902 1.00 16.75 C ANISOU 603 C VAL A 172 1690 2866 1807 233 59 -110 C ATOM 604 O VAL A 172 11.545 -8.827 23.718 1.00 16.39 O ANISOU 604 O VAL A 172 1668 2936 1623 420 300 -106 O ATOM 605 CB VAL A 172 13.346 -9.503 26.079 1.00 17.67 C ANISOU 605 CB VAL A 172 1845 2854 2015 -14 -191 -411 C ATOM 606 CG1 VAL A 172 13.370 -8.030 26.456 1.00 16.62 C ANISOU 606 CG1 VAL A 172 1683 2669 1962 -43 -188 -594 C ATOM 607 CG2 VAL A 172 13.974 -10.369 27.176 1.00 17.56 C ANISOU 607 CG2 VAL A 172 1886 2770 2015 -39 -102 -294 C ATOM 608 N VAL A 173 10.309 -8.149 25.471 1.00 15.30 N ANISOU 608 N VAL A 173 1445 2727 1641 382 -103 -203 N ATOM 609 CA VAL A 173 9.633 -7.086 24.740 1.00 15.07 C ANISOU 609 CA VAL A 173 1443 2624 1660 344 -28 -8 C ATOM 610 C VAL A 173 10.568 -5.895 24.634 1.00 15.73 C ANISOU 610 C VAL A 173 1391 2892 1692 223 21 44 C ATOM 611 O VAL A 173 10.981 -5.330 25.649 1.00 15.93 O ANISOU 611 O VAL A 173 1640 2992 1419 -70 110 312 O ATOM 612 CB VAL A 173 8.343 -6.636 25.447 1.00 14.61 C ANISOU 612 CB VAL A 173 1461 2405 1685 521 -190 -202 C ATOM 613 CG1 VAL A 173 7.665 -5.521 24.664 1.00 13.90 C ANISOU 613 CG1 VAL A 173 1472 2302 1508 621 -439 -159 C ATOM 614 CG2 VAL A 173 7.401 -7.811 25.634 1.00 14.50 C ANISOU 614 CG2 VAL A 173 1273 2446 1792 429 -122 -220 C ATOM 615 N ARG A 174 10.894 -5.526 23.398 1.00 17.03 N ANISOU 615 N ARG A 174 1435 3168 1869 458 -157 105 N ATOM 616 CA ARG A 174 11.790 -4.411 23.113 1.00 19.48 C ANISOU 616 CA ARG A 174 1630 3637 2135 395 -9 31 C ATOM 617 C ARG A 174 11.311 -3.659 21.880 1.00 18.24 C ANISOU 617 C ARG A 174 1522 3787 1619 139 6 -51 C ATOM 618 O ARG A 174 10.472 -4.159 21.133 1.00 17.85 O ANISOU 618 O ARG A 174 1422 3932 1428 -115 -116 -99 O ATOM 619 CB ARG A 174 13.223 -4.914 22.893 1.00 23.17 C ANISOU 619 CB ARG A 174 1993 4054 2759 624 242 -168 C ATOM 620 CG ARG A 174 13.308 -6.259 22.178 1.00 27.16 C ANISOU 620 CG ARG A 174 2419 4575 3325 746 236 -316 C ATOM 621 CD ARG A 174 14.755 -6.646 21.888 1.00 31.30 C ANISOU 621 CD ARG A 174 3046 5052 3796 892 138 -414 C ATOM 622 NE ARG A 174 15.623 -6.384 23.037 1.00 36.25 N ANISOU 622 NE ARG A 174 3753 5634 4389 1002 244 -521 N ATOM 623 CZ ARG A 174 16.262 -7.320 23.740 1.00 39.38 C ANISOU 623 CZ ARG A 174 4151 6121 4692 868 297 -739 C ATOM 624 NH1 ARG A 174 16.156 -8.606 23.412 1.00 40.40 N1+ ANISOU 624 NH1 ARG A 174 4303 6200 4845 825 450 -795 N1+ ATOM 625 NH2 ARG A 174 17.023 -6.969 24.771 1.00 39.79 N ANISOU 625 NH2 ARG A 174 4134 6302 4682 792 245 -906 N ATOM 626 N ARG A 175 11.844 -2.460 21.670 1.00 18.08 N ANISOU 626 N ARG A 175 1648 3803 1420 236 5 5 N ATOM 627 CA ARG A 175 11.494 -1.683 20.489 1.00 18.81 C ANISOU 627 CA ARG A 175 1907 3773 1468 36 57 -31 C ATOM 628 C ARG A 175 12.047 -2.337 19.228 1.00 19.78 C ANISOU 628 C ARG A 175 2008 3915 1592 107 118 110 C ATOM 629 O ARG A 175 13.054 -3.046 19.277 1.00 19.87 O ANISOU 629 O ARG A 175 1999 3907 1642 -28 25 74 O ATOM 630 CB ARG A 175 12.011 -0.247 20.603 1.00 18.33 C ANISOU 630 CB ARG A 175 1812 3699 1454 -492 52 -86 C ATOM 631 CG ARG A 175 11.356 0.578 21.698 1.00 18.56 C ANISOU 631 CG ARG A 175 1864 3717 1471 -637 -39 -187 C ATOM 632 CD ARG A 175 12.037 1.922 21.820 1.00 21.23 C ANISOU 632 CD ARG A 175 2484 3929 1654 -332 -6 -306 C ATOM 633 NE ARG A 175 11.381 2.930 21.005 1.00 24.18 N ANISOU 633 NE ARG A 175 3058 4276 1853 -495 199 -518 N ATOM 634 CZ ARG A 175 11.884 4.128 20.744 1.00 24.84 C ANISOU 634 CZ ARG A 175 3070 4516 1852 -447 401 -460 C ATOM 635 NH1 ARG A 175 13.065 4.472 21.229 1.00 24.71 N1+ ANISOU 635 NH1 ARG A 175 2803 4620 1966 -98 291 -383 N1+ ATOM 636 NH2 ARG A 175 11.199 4.979 19.999 1.00 25.57 N ANISOU 636 NH2 ARG A 175 3225 4669 1823 -531 554 -485 N ATOM 637 N CYS A 176 11.369 -2.118 18.105 1.00 19.96 N ANISOU 637 N CYS A 176 2060 4046 1477 245 91 57 N ATOM 638 CA CYS A 176 11.866 -2.566 16.808 1.00 20.36 C ANISOU 638 CA CYS A 176 2019 4309 1410 628 178 172 C ATOM 639 C CYS A 176 13.130 -1.777 16.457 1.00 20.81 C ANISOU 639 C CYS A 176 2092 4456 1360 946 313 304 C ATOM 640 O CYS A 176 13.338 -0.679 16.977 1.00 20.02 O ANISOU 640 O CYS A 176 2052 4274 1281 1012 278 438 O ATOM 641 CB CYS A 176 10.794 -2.366 15.737 1.00 20.41 C ANISOU 641 CB CYS A 176 1804 4393 1559 717 17 48 C ATOM 642 SG CYS A 176 10.441 -0.634 15.370 1.00 21.83 S ANISOU 642 SG CYS A 176 2013 4708 1574 758 -170 -133 S ATOM 643 N PRO A 177 13.982 -2.338 15.582 1.00 22.66 N ANISOU 643 N PRO A 177 2144 4706 1761 900 319 346 N ATOM 644 CA PRO A 177 15.235 -1.668 15.216 1.00 22.48 C ANISOU 644 CA PRO A 177 2005 4790 1745 777 354 377 C ATOM 645 C PRO A 177 15.007 -0.243 14.721 1.00 21.87 C ANISOU 645 C PRO A 177 1839 4842 1630 488 93 203 C ATOM 646 O PRO A 177 15.790 0.636 15.064 1.00 21.53 O ANISOU 646 O PRO A 177 1727 4930 1525 327 -298 50 O ATOM 647 CB PRO A 177 15.784 -2.549 14.094 1.00 23.76 C ANISOU 647 CB PRO A 177 2106 4841 2081 867 259 420 C ATOM 648 CG PRO A 177 15.259 -3.911 14.416 1.00 23.37 C ANISOU 648 CG PRO A 177 2103 4739 2037 951 321 358 C ATOM 649 CD PRO A 177 13.875 -3.675 14.969 1.00 22.85 C ANISOU 649 CD PRO A 177 2148 4720 1815 1046 434 223 C ATOM 650 N HIS A 178 13.944 -0.025 13.947 1.00 20.55 N ANISOU 650 N HIS A 178 1561 4718 1529 507 95 38 N ATOM 651 CA HIS A 178 13.605 1.307 13.444 1.00 18.98 C ANISOU 651 CA HIS A 178 1423 4425 1363 477 -41 -103 C ATOM 652 C HIS A 178 13.428 2.334 14.557 1.00 18.97 C ANISOU 652 C HIS A 178 1318 4482 1409 195 20 -8 C ATOM 653 O HIS A 178 13.982 3.430 14.507 1.00 19.86 O ANISOU 653 O HIS A 178 1337 4665 1542 129 58 28 O ATOM 654 CB HIS A 178 12.321 1.256 12.619 1.00 18.28 C ANISOU 654 CB HIS A 178 1459 4194 1294 389 -130 -306 C ATOM 655 CG HIS A 178 11.695 2.598 12.400 1.00 18.71 C ANISOU 655 CG HIS A 178 1806 4083 1219 392 -326 -420 C ATOM 656 CD2 HIS A 178 10.484 3.088 12.757 1.00 19.38 C ANISOU 656 CD2 HIS A 178 2109 4015 1238 464 -311 -453 C ATOM 657 ND1 HIS A 178 12.335 3.614 11.724 1.00 19.11 N ANISOU 657 ND1 HIS A 178 1914 4106 1243 512 -290 -566 N ATOM 658 CE1 HIS A 178 11.546 4.674 11.676 1.00 19.65 C ANISOU 658 CE1 HIS A 178 2151 4025 1288 559 -331 -556 C ATOM 659 NE2 HIS A 178 10.416 4.380 12.295 1.00 19.11 N ANISOU 659 NE2 HIS A 178 2060 3986 1216 509 -277 -495 N ATOM 660 N HIS A 179 12.623 1.989 15.551 1.00 19.05 N ANISOU 660 N HIS A 179 1425 4467 1346 160 -131 9 N ATOM 661 CA HIS A 179 12.346 2.915 16.640 1.00 18.99 C ANISOU 661 CA HIS A 179 1467 4559 1189 32 -38 148 C ATOM 662 C HIS A 179 13.523 3.007 17.596 1.00 20.78 C ANISOU 662 C HIS A 179 1700 4934 1263 119 -35 182 C ATOM 663 O HIS A 179 13.754 4.046 18.204 1.00 21.78 O ANISOU 663 O HIS A 179 1903 4980 1391 222 -243 320 O ATOM 664 CB HIS A 179 11.055 2.537 17.363 1.00 17.65 C ANISOU 664 CB HIS A 179 1386 4250 1068 -12 5 118 C ATOM 665 CG HIS A 179 9.828 3.073 16.702 1.00 16.54 C ANISOU 665 CG HIS A 179 1158 4020 1105 70 83 227 C ATOM 666 CD2 HIS A 179 9.527 4.320 16.265 1.00 17.66 C ANISOU 666 CD2 HIS A 179 1347 3976 1388 -22 311 368 C ATOM 667 ND1 HIS A 179 8.737 2.288 16.404 1.00 14.84 N ANISOU 667 ND1 HIS A 179 922 3675 1042 -45 13 99 N ATOM 668 CE1 HIS A 179 7.815 3.026 15.814 1.00 17.72 C ANISOU 668 CE1 HIS A 179 1536 3762 1436 -133 182 204 C ATOM 669 NE2 HIS A 179 8.270 4.264 15.713 1.00 18.77 N ANISOU 669 NE2 HIS A 179 1628 3955 1548 -69 267 529 N ATOM 670 N GLU A 180 14.279 1.926 17.718 1.00 22.21 N ANISOU 670 N GLU A 180 1771 5176 1492 -24 302 125 N ATOM 671 CA GLU A 180 15.459 1.938 18.575 1.00 25.11 C ANISOU 671 CA GLU A 180 1779 5828 1933 -178 271 59 C ATOM 672 C GLU A 180 16.483 2.935 18.025 1.00 28.65 C ANISOU 672 C GLU A 180 2232 6262 2391 -334 51 -5 C ATOM 673 O GLU A 180 17.230 3.567 18.778 1.00 29.30 O ANISOU 673 O GLU A 180 2388 6370 2374 -408 197 -67 O ATOM 674 CB GLU A 180 16.051 0.532 18.652 1.00 25.93 C ANISOU 674 CB GLU A 180 1757 5966 2127 -156 40 -5 C ATOM 675 CG GLU A 180 17.327 0.424 19.463 1.00 28.28 C ANISOU 675 CG GLU A 180 2079 6209 2459 -92 5 -244 C ATOM 676 CD GLU A 180 18.007 -0.921 19.295 1.00 30.56 C ANISOU 676 CD GLU A 180 2319 6501 2792 -2 -47 -510 C ATOM 677 OE1 GLU A 180 17.310 -1.918 19.015 1.00 30.25 O ANISOU 677 OE1 GLU A 180 2421 6425 2647 82 -149 -799 O ATOM 678 OE2 GLU A 180 19.244 -0.982 19.445 1.00 33.48 O1- ANISOU 678 OE2 GLU A 180 2759 6790 3173 -12 177 -571 O1- ATOM 679 N ARG A 181 16.487 3.081 16.702 1.00 31.60 N ANISOU 679 N ARG A 181 2686 6543 2776 -565 57 78 N ATOM 680 CA ARG A 181 17.402 3.983 16.013 1.00 34.91 C ANISOU 680 CA ARG A 181 3304 6767 3194 -834 -151 58 C ATOM 681 C ARG A 181 16.786 5.349 15.734 1.00 33.79 C ANISOU 681 C ARG A 181 3242 6534 3062 -1175 -534 303 C ATOM 682 O ARG A 181 17.461 6.242 15.233 1.00 33.02 O ANISOU 682 O ARG A 181 2984 6583 2978 -1328 -704 451 O ATOM 683 CB ARG A 181 17.873 3.356 14.699 1.00 39.12 C ANISOU 683 CB ARG A 181 3918 7246 3699 -701 39 -151 C ATOM 684 CG ARG A 181 18.673 2.076 14.879 1.00 43.78 C ANISOU 684 CG ARG A 181 4682 7787 4164 -580 -48 -339 C ATOM 685 CD ARG A 181 19.496 1.773 13.634 1.00 47.79 C ANISOU 685 CD ARG A 181 5312 8206 4641 -480 -402 -429 C ATOM 686 NE ARG A 181 18.946 0.689 12.820 1.00 50.67 N ANISOU 686 NE ARG A 181 5707 8556 4989 -474 -896 -404 N ATOM 687 CZ ARG A 181 19.433 -0.550 12.809 1.00 53.09 C ANISOU 687 CZ ARG A 181 5965 8888 5318 -496 -1299 -407 C ATOM 688 NH1 ARG A 181 20.472 -0.863 13.578 1.00 53.96 N1+ ANISOU 688 NH1 ARG A 181 6022 8984 5495 -448 -1533 -405 N1+ ATOM 689 NH2 ARG A 181 18.886 -1.480 12.036 1.00 53.61 N ANISOU 689 NH2 ARG A 181 6008 9043 5318 -487 -1436 -390 N ATOM 690 N CYS A 182 15.504 5.507 16.045 1.00 34.26 N ANISOU 690 N CYS A 182 3524 6350 3143 -1289 -704 354 N ATOM 691 CA CYS A 182 14.841 6.800 15.892 1.00 35.22 C ANISOU 691 CA CYS A 182 3838 6313 3232 -1242 -893 599 C ATOM 692 C CYS A 182 15.470 7.851 16.801 1.00 35.97 C ANISOU 692 C CYS A 182 3915 6212 3541 -1348 -623 787 C ATOM 693 O CYS A 182 15.987 7.527 17.875 1.00 36.12 O ANISOU 693 O CYS A 182 3877 6379 3468 -1433 -875 836 O ATOM 694 CB CYS A 182 13.349 6.687 16.203 1.00 35.73 C ANISOU 694 CB CYS A 182 4072 6386 3117 -1057 -1201 642 C ATOM 695 SG CYS A 182 12.322 6.520 14.739 1.00 37.31 S ANISOU 695 SG CYS A 182 4548 6575 3053 -911 -1187 712 S ATOM 696 N SER A 183 15.421 9.110 16.373 1.00 35.76 N ANISOU 696 N SER A 183 3976 5899 3714 -1386 -151 889 N ATOM 697 CA SER A 183 15.964 10.206 17.168 1.00 36.41 C ANISOU 697 CA SER A 183 4266 5698 3870 -1348 265 854 C ATOM 698 C SER A 183 14.899 10.780 18.097 1.00 35.21 C ANISOU 698 C SER A 183 4314 5354 3709 -1533 258 886 C ATOM 699 O SER A 183 14.651 11.989 18.101 1.00 36.53 O ANISOU 699 O SER A 183 4562 5429 3889 -1609 268 917 O ATOM 700 CB SER A 183 16.525 11.302 16.260 1.00 38.22 C ANISOU 700 CB SER A 183 4570 5883 4068 -1163 534 785 C ATOM 701 OG SER A 183 17.572 10.805 15.445 1.00 39.49 O ANISOU 701 OG SER A 183 4772 6015 4217 -1022 696 696 O ATOM 702 N ASP A 184 14.273 9.907 18.882 1.00 31.36 N ANISOU 702 N ASP A 184 3892 4800 3224 -1682 221 1066 N ATOM 703 CA ASP A 184 13.174 10.314 19.754 1.00 29.49 C ANISOU 703 CA ASP A 184 3518 4554 3132 -1321 184 1082 C ATOM 704 C ASP A 184 13.543 10.267 21.233 1.00 28.34 C ANISOU 704 C ASP A 184 3413 4363 2992 -1175 354 1171 C ATOM 705 O ASP A 184 12.672 10.204 22.096 1.00 27.00 O ANISOU 705 O ASP A 184 3286 4311 2663 -1259 553 1113 O ATOM 706 CB ASP A 184 11.942 9.446 19.501 1.00 28.64 C ANISOU 706 CB ASP A 184 3187 4561 3134 -1170 231 1131 C ATOM 707 CG ASP A 184 12.218 7.961 19.680 1.00 28.89 C ANISOU 707 CG ASP A 184 3062 4721 3194 -983 226 1096 C ATOM 708 OD1 ASP A 184 13.213 7.596 20.340 1.00 28.34 O ANISOU 708 OD1 ASP A 184 2735 4836 3197 -1051 257 1078 O ATOM 709 OD2 ASP A 184 11.423 7.148 19.165 1.00 29.44 O1- ANISOU 709 OD2 ASP A 184 3238 4697 3252 -865 175 1180 O1- ATOM 710 N SER A 185 14.841 10.291 21.514 1.00 29.09 N ANISOU 710 N SER A 185 3586 4287 3180 -872 237 1169 N ATOM 711 CA SER A 185 15.337 10.161 22.877 1.00 28.63 C ANISOU 711 CA SER A 185 3412 4159 3308 -649 128 1103 C ATOM 712 C SER A 185 14.877 11.320 23.757 1.00 28.36 C ANISOU 712 C SER A 185 3428 3919 3429 -647 82 1062 C ATOM 713 O SER A 185 14.699 12.443 23.280 1.00 28.54 O ANISOU 713 O SER A 185 3442 3832 3571 -558 242 1118 O ATOM 714 CB SER A 185 16.863 10.068 22.873 1.00 28.81 C ANISOU 714 CB SER A 185 3184 4319 3442 -429 147 1032 C ATOM 715 OG SER A 185 17.362 9.881 24.181 1.00 29.37 O ANISOU 715 OG SER A 185 3032 4483 3645 -267 45 744 O ATOM 716 N ASP A 186 14.663 11.034 25.039 1.00 27.16 N ANISOU 716 N ASP A 186 3271 3787 3262 -701 -51 863 N ATOM 717 CA ASP A 186 14.324 12.070 26.003 1.00 25.25 C ANISOU 717 CA ASP A 186 3076 3395 3124 -697 -163 669 C ATOM 718 C ASP A 186 15.525 12.316 26.910 1.00 24.80 C ANISOU 718 C ASP A 186 3230 3033 3159 -786 -91 543 C ATOM 719 O ASP A 186 15.451 13.073 27.881 1.00 24.79 O ANISOU 719 O ASP A 186 3639 2699 3080 -760 -160 399 O ATOM 720 CB ASP A 186 13.083 11.677 26.814 1.00 25.00 C ANISOU 720 CB ASP A 186 3023 3360 3115 -615 -324 623 C ATOM 721 CG ASP A 186 13.266 10.385 27.596 1.00 24.32 C ANISOU 721 CG ASP A 186 2956 3218 3066 -739 -122 510 C ATOM 722 OD1 ASP A 186 14.282 9.686 27.410 1.00 24.53 O ANISOU 722 OD1 ASP A 186 2991 3262 3069 -633 -117 473 O ATOM 723 OD2 ASP A 186 12.372 10.068 28.403 1.00 24.20 O1- ANISOU 723 OD2 ASP A 186 2895 3209 3091 -813 -94 461 O1- ATOM 724 N GLY A 187 16.630 11.654 26.580 1.00 23.87 N ANISOU 724 N GLY A 187 2863 3045 3161 -705 -146 441 N ATOM 725 CA GLY A 187 17.878 11.819 27.303 1.00 22.65 C ANISOU 725 CA GLY A 187 2554 3125 2926 -572 -322 394 C ATOM 726 C GLY A 187 17.984 10.920 28.518 1.00 21.51 C ANISOU 726 C GLY A 187 2243 3114 2816 -611 -494 415 C ATOM 727 O GLY A 187 19.047 10.824 29.128 1.00 21.41 O ANISOU 727 O GLY A 187 2059 3214 2863 -752 -503 291 O ATOM 728 N LEU A 188 16.880 10.269 28.877 1.00 20.07 N ANISOU 728 N LEU A 188 2046 2937 2642 -845 -637 424 N ATOM 729 CA LEU A 188 16.845 9.423 30.069 1.00 19.54 C ANISOU 729 CA LEU A 188 2002 2919 2502 -603 -568 169 C ATOM 730 C LEU A 188 16.652 7.953 29.708 1.00 18.65 C ANISOU 730 C LEU A 188 1909 2866 2312 -476 -673 265 C ATOM 731 O LEU A 188 17.422 7.090 30.127 1.00 19.44 O ANISOU 731 O LEU A 188 2088 2933 2365 -744 -892 342 O ATOM 732 CB LEU A 188 15.739 9.886 31.028 1.00 19.01 C ANISOU 732 CB LEU A 188 2043 2751 2431 -411 -470 -27 C ATOM 733 CG LEU A 188 15.816 11.341 31.503 1.00 19.26 C ANISOU 733 CG LEU A 188 2285 2632 2402 -249 -479 -189 C ATOM 734 CD1 LEU A 188 14.690 11.672 32.465 1.00 19.00 C ANISOU 734 CD1 LEU A 188 2312 2480 2428 100 -287 -474 C ATOM 735 CD2 LEU A 188 17.158 11.613 32.144 1.00 19.36 C ANISOU 735 CD2 LEU A 188 2516 2536 2305 -292 -886 -190 C ATOM 736 N ALA A 189 15.621 7.677 28.917 1.00 16.91 N ANISOU 736 N ALA A 189 1630 2848 1947 -270 -678 92 N ATOM 737 CA ALA A 189 15.290 6.307 28.539 1.00 16.66 C ANISOU 737 CA ALA A 189 1544 3042 1744 -14 -366 231 C ATOM 738 C ALA A 189 16.301 5.700 27.563 1.00 16.32 C ANISOU 738 C ALA A 189 1433 3167 1602 -222 -241 247 C ATOM 739 O ALA A 189 16.755 6.371 26.626 1.00 15.91 O ANISOU 739 O ALA A 189 1577 3156 1312 -532 -441 262 O ATOM 740 CB ALA A 189 13.902 6.243 27.955 1.00 14.94 C ANISOU 740 CB ALA A 189 1244 2908 1524 399 -240 468 C ATOM 741 N PRO A 190 16.660 4.425 27.789 1.00 15.12 N ANISOU 741 N PRO A 190 1128 3014 1601 -224 -117 267 N ATOM 742 CA PRO A 190 17.491 3.666 26.850 1.00 16.37 C ANISOU 742 CA PRO A 190 1430 3218 1570 -304 -256 272 C ATOM 743 C PRO A 190 16.731 3.476 25.550 1.00 17.88 C ANISOU 743 C PRO A 190 1628 3648 1516 -411 -149 203 C ATOM 744 O PRO A 190 15.506 3.321 25.592 1.00 18.57 O ANISOU 744 O PRO A 190 1757 3822 1476 -609 -159 336 O ATOM 745 CB PRO A 190 17.679 2.317 27.557 1.00 17.01 C ANISOU 745 CB PRO A 190 1613 3222 1629 -507 -40 188 C ATOM 746 CG PRO A 190 17.459 2.611 29.008 1.00 16.20 C ANISOU 746 CG PRO A 190 1378 3168 1610 -373 -109 149 C ATOM 747 CD PRO A 190 16.397 3.671 29.025 1.00 14.91 C ANISOU 747 CD PRO A 190 1066 3016 1584 -243 -54 126 C ATOM 748 N PRO A 191 17.436 3.496 24.408 1.00 17.79 N ANISOU 748 N PRO A 191 1395 3938 1425 -548 54 270 N ATOM 749 CA PRO A 191 16.739 3.430 23.116 1.00 18.36 C ANISOU 749 CA PRO A 191 1629 3985 1361 -390 245 139 C ATOM 750 C PRO A 191 15.975 2.125 22.863 1.00 16.71 C ANISOU 750 C PRO A 191 1493 3657 1199 -296 280 103 C ATOM 751 O PRO A 191 15.052 2.142 22.061 1.00 15.77 O ANISOU 751 O PRO A 191 1313 3569 1108 -400 -47 85 O ATOM 752 CB PRO A 191 17.868 3.608 22.085 1.00 18.00 C ANISOU 752 CB PRO A 191 1532 4048 1259 -562 258 140 C ATOM 753 CG PRO A 191 19.119 3.242 22.803 1.00 18.28 C ANISOU 753 CG PRO A 191 1458 4108 1380 -584 163 65 C ATOM 754 CD PRO A 191 18.893 3.638 24.244 1.00 18.13 C ANISOU 754 CD PRO A 191 1444 4071 1372 -520 154 127 C ATOM 755 N GLN A 192 16.351 1.033 23.522 1.00 17.59 N ANISOU 755 N GLN A 192 1824 3593 1265 23 435 250 N ATOM 756 CA GLN A 192 15.678 -0.253 23.335 1.00 17.30 C ANISOU 756 CA GLN A 192 1722 3390 1461 259 353 296 C ATOM 757 C GLN A 192 14.354 -0.365 24.085 1.00 15.07 C ANISOU 757 C GLN A 192 1291 3079 1356 394 77 219 C ATOM 758 O GLN A 192 13.523 -1.215 23.758 1.00 14.16 O ANISOU 758 O GLN A 192 1041 3045 1295 335 344 82 O ATOM 759 CB GLN A 192 16.579 -1.409 23.783 1.00 20.69 C ANISOU 759 CB GLN A 192 2045 3737 2081 658 689 105 C ATOM 760 CG GLN A 192 17.683 -1.795 22.817 1.00 24.43 C ANISOU 760 CG GLN A 192 2552 4171 2560 836 896 223 C ATOM 761 CD GLN A 192 18.390 -3.075 23.242 1.00 27.90 C ANISOU 761 CD GLN A 192 3064 4653 2884 1089 1051 267 C ATOM 762 NE2 GLN A 192 19.005 -3.754 22.281 1.00 29.14 N ANISOU 762 NE2 GLN A 192 3310 4777 2985 1063 1208 468 N ATOM 763 OE1 GLN A 192 18.369 -3.456 24.417 1.00 29.46 O ANISOU 763 OE1 GLN A 192 3186 4913 3094 1227 949 153 O ATOM 764 N HIS A 193 14.170 0.482 25.095 1.00 13.09 N ANISOU 764 N HIS A 193 1135 2682 1157 407 -134 207 N ATOM 765 CA HIS A 193 13.032 0.362 26.008 1.00 11.51 C ANISOU 765 CA HIS A 193 1018 2382 975 133 -257 100 C ATOM 766 C HIS A 193 11.691 0.781 25.412 1.00 11.90 C ANISOU 766 C HIS A 193 1032 2423 1068 84 -75 225 C ATOM 767 O HIS A 193 11.540 1.899 24.918 1.00 14.20 O ANISOU 767 O HIS A 193 1173 3037 1186 -177 -196 393 O ATOM 768 CB HIS A 193 13.283 1.145 27.301 1.00 11.18 C ANISOU 768 CB HIS A 193 970 2147 1129 -77 -501 -33 C ATOM 769 CG HIS A 193 14.149 0.424 28.277 1.00 11.38 C ANISOU 769 CG HIS A 193 1216 1934 1173 -145 -506 -171 C ATOM 770 CD2 HIS A 193 15.280 -0.300 28.102 1.00 11.85 C ANISOU 770 CD2 HIS A 193 1415 1835 1254 51 -607 -76 C ATOM 771 ND1 HIS A 193 13.884 0.401 29.629 1.00 12.62 N ANISOU 771 ND1 HIS A 193 1393 1963 1441 -175 -393 -468 N ATOM 772 CE1 HIS A 193 14.817 -0.303 30.246 1.00 12.06 C ANISOU 772 CE1 HIS A 193 1377 1840 1366 55 -487 -419 C ATOM 773 NE2 HIS A 193 15.675 -0.740 29.341 1.00 11.93 N ANISOU 773 NE2 HIS A 193 1392 1856 1286 136 -639 -232 N ATOM 774 N LEU A 194 10.710 -0.113 25.490 1.00 12.59 N ANISOU 774 N LEU A 194 1339 2258 1188 194 61 162 N ATOM 775 CA LEU A 194 9.360 0.188 25.021 1.00 12.11 C ANISOU 775 CA LEU A 194 1225 2023 1353 166 -237 119 C ATOM 776 C LEU A 194 8.643 1.219 25.897 1.00 12.48 C ANISOU 776 C LEU A 194 1173 1943 1627 303 -393 285 C ATOM 777 O LEU A 194 8.033 2.167 25.388 1.00 13.09 O ANISOU 777 O LEU A 194 1213 2062 1698 150 -690 462 O ATOM 778 CB LEU A 194 8.528 -1.094 24.956 1.00 11.51 C ANISOU 778 CB LEU A 194 1176 1869 1328 -8 -284 229 C ATOM 779 CG LEU A 194 7.046 -0.890 24.660 1.00 11.91 C ANISOU 779 CG LEU A 194 1347 1729 1448 -272 -475 44 C ATOM 780 CD1 LEU A 194 6.872 -0.432 23.219 1.00 12.43 C ANISOU 780 CD1 LEU A 194 1415 1773 1535 3 -457 75 C ATOM 781 CD2 LEU A 194 6.259 -2.159 24.950 1.00 12.59 C ANISOU 781 CD2 LEU A 194 1266 1909 1607 -483 -447 -91 C ATOM 782 N ILE A 195 8.703 1.021 27.210 1.00 12.71 N ANISOU 782 N ILE A 195 1187 1889 1753 462 -243 111 N ATOM 783 CA ILE A 195 7.968 1.873 28.144 1.00 12.96 C ANISOU 783 CA ILE A 195 1334 1840 1749 168 -47 142 C ATOM 784 C ILE A 195 8.841 2.985 28.743 1.00 13.99 C ANISOU 784 C ILE A 195 1337 1994 1985 -38 2 58 C ATOM 785 O ILE A 195 9.886 2.713 29.338 1.00 14.21 O ANISOU 785 O ILE A 195 1231 2250 1917 -238 -146 -270 O ATOM 786 CB ILE A 195 7.339 1.046 29.296 1.00 12.43 C ANISOU 786 CB ILE A 195 1275 1661 1786 29 102 110 C ATOM 787 CG1 ILE A 195 6.497 -0.109 28.747 1.00 12.43 C ANISOU 787 CG1 ILE A 195 1285 1740 1698 296 119 -39 C ATOM 788 CG2 ILE A 195 6.497 1.940 30.209 1.00 11.57 C ANISOU 788 CG2 ILE A 195 1256 1414 1727 206 80 39 C ATOM 789 CD1 ILE A 195 5.837 -0.959 29.836 1.00 11.96 C ANISOU 789 CD1 ILE A 195 1075 1772 1699 567 163 79 C ATOM 790 N ARG A 196 8.402 4.235 28.582 1.00 13.23 N ANISOU 790 N ARG A 196 1289 1629 2107 -281 -94 224 N ATOM 791 CA ARG A 196 9.038 5.378 29.238 1.00 13.09 C ANISOU 791 CA ARG A 196 1265 1705 2004 -270 -138 309 C ATOM 792 C ARG A 196 8.100 6.028 30.245 1.00 12.41 C ANISOU 792 C ARG A 196 1411 1435 1867 -79 -381 276 C ATOM 793 O ARG A 196 6.885 5.854 30.190 1.00 11.48 O ANISOU 793 O ARG A 196 1256 1200 1905 459 -401 270 O ATOM 794 CB ARG A 196 9.440 6.443 28.216 1.00 14.31 C ANISOU 794 CB ARG A 196 1298 2064 2077 -415 8 386 C ATOM 795 CG ARG A 196 10.440 5.994 27.191 1.00 15.20 C ANISOU 795 CG ARG A 196 1343 2275 2158 -738 -110 564 C ATOM 796 CD ARG A 196 10.864 7.157 26.319 1.00 16.69 C ANISOU 796 CD ARG A 196 1646 2446 2248 -1054 -59 594 C ATOM 797 NE ARG A 196 11.768 6.720 25.260 1.00 20.22 N ANISOU 797 NE ARG A 196 2232 2786 2663 -1082 -28 646 N ATOM 798 CZ ARG A 196 12.145 7.478 24.238 1.00 22.79 C ANISOU 798 CZ ARG A 196 2588 3158 2913 -916 -177 648 C ATOM 799 NH1 ARG A 196 11.698 8.724 24.137 1.00 23.49 N1+ ANISOU 799 NH1 ARG A 196 2747 3211 2967 -809 -315 743 N1+ ATOM 800 NH2 ARG A 196 12.967 6.984 23.318 1.00 23.80 N ANISOU 800 NH2 ARG A 196 2667 3329 3045 -701 -202 425 N ATOM 801 N VAL A 197 8.680 6.788 31.163 1.00 12.59 N ANISOU 801 N VAL A 197 1606 1327 1851 -332 -290 -31 N ATOM 802 CA VAL A 197 7.908 7.631 32.051 1.00 14.38 C ANISOU 802 CA VAL A 197 2122 1391 1952 -223 -153 -78 C ATOM 803 C VAL A 197 8.112 9.068 31.621 1.00 16.41 C ANISOU 803 C VAL A 197 2448 1499 2290 -292 37 -163 C ATOM 804 O VAL A 197 9.239 9.498 31.356 1.00 16.55 O ANISOU 804 O VAL A 197 2396 1463 2428 -73 213 -290 O ATOM 805 CB VAL A 197 8.322 7.463 33.522 1.00 12.97 C ANISOU 805 CB VAL A 197 2199 1137 1593 -193 -118 82 C ATOM 806 CG1 VAL A 197 7.759 8.598 34.359 1.00 12.90 C ANISOU 806 CG1 VAL A 197 2336 1141 1425 -351 -186 209 C ATOM 807 CG2 VAL A 197 7.833 6.138 34.051 1.00 11.82 C ANISOU 807 CG2 VAL A 197 2117 828 1547 -221 -32 -15 C ATOM 808 N GLU A 198 7.004 9.791 31.539 1.00 18.10 N ANISOU 808 N GLU A 198 2755 1657 2466 -351 -129 -5 N ATOM 809 CA GLU A 198 6.983 11.180 31.133 1.00 19.66 C ANISOU 809 CA GLU A 198 3100 1638 2733 -224 -338 283 C ATOM 810 C GLU A 198 6.935 12.081 32.372 1.00 20.07 C ANISOU 810 C GLU A 198 3251 1622 2753 -165 -339 513 C ATOM 811 O GLU A 198 6.290 11.746 33.370 1.00 20.52 O ANISOU 811 O GLU A 198 3379 1669 2747 -38 -215 353 O ATOM 812 CB GLU A 198 5.739 11.402 30.279 1.00 21.65 C ANISOU 812 CB GLU A 198 3450 1717 3061 -84 -700 335 C ATOM 813 CG GLU A 198 5.707 12.680 29.486 1.00 24.27 C ANISOU 813 CG GLU A 198 3797 1943 3481 -5 -956 516 C ATOM 814 CD GLU A 198 4.316 12.976 28.943 1.00 25.93 C ANISOU 814 CD GLU A 198 3927 2045 3878 -32 -1000 778 C ATOM 815 OE1 GLU A 198 3.618 12.036 28.502 1.00 23.41 O ANISOU 815 OE1 GLU A 198 3612 1708 3573 -474 -1148 965 O ATOM 816 OE2 GLU A 198 3.917 14.157 28.972 1.00 29.24 O1- ANISOU 816 OE2 GLU A 198 4217 2515 4380 25 -1018 696 O1- ATOM 817 N GLY A 199 7.639 13.210 32.308 1.00 20.08 N ANISOU 817 N GLY A 199 3182 1701 2747 -165 -382 700 N ATOM 818 CA GLY A 199 7.561 14.251 33.324 1.00 19.65 C ANISOU 818 CA GLY A 199 3118 1557 2792 -9 -406 654 C ATOM 819 C GLY A 199 8.006 13.910 34.736 1.00 20.01 C ANISOU 819 C GLY A 199 3037 1729 2835 221 -221 389 C ATOM 820 O GLY A 199 7.425 14.400 35.704 1.00 20.47 O ANISOU 820 O GLY A 199 3135 1786 2858 354 -220 169 O ATOM 821 N ASN A 200 9.035 13.076 34.858 1.00 19.69 N ANISOU 821 N ASN A 200 2688 1960 2833 302 -235 386 N ATOM 822 CA ASN A 200 9.582 12.707 36.161 1.00 17.87 C ANISOU 822 CA ASN A 200 2364 1827 2598 308 -357 89 C ATOM 823 C ASN A 200 11.082 12.457 36.065 1.00 17.84 C ANISOU 823 C ASN A 200 2322 1767 2688 359 -213 -68 C ATOM 824 O ASN A 200 11.514 11.437 35.541 1.00 16.75 O ANISOU 824 O ASN A 200 2017 1665 2683 737 -47 -19 O ATOM 825 CB ASN A 200 8.866 11.467 36.713 1.00 17.05 C ANISOU 825 CB ASN A 200 2151 1761 2567 249 -542 48 C ATOM 826 CG ASN A 200 9.162 11.219 38.183 1.00 17.18 C ANISOU 826 CG ASN A 200 2204 1841 2484 303 -440 -97 C ATOM 827 ND2 ASN A 200 8.204 10.631 38.882 1.00 16.24 N ANISOU 827 ND2 ASN A 200 2117 1687 2365 543 -265 57 N ATOM 828 OD1 ASN A 200 10.241 11.542 38.681 1.00 18.62 O ANISOU 828 OD1 ASN A 200 2455 2215 2404 303 -770 -116 O ATOM 829 N LEU A 201 11.867 13.387 36.595 1.00 19.35 N ANISOU 829 N LEU A 201 2473 1916 2964 205 -239 -50 N ATOM 830 CA LEU A 201 13.320 13.359 36.460 1.00 21.94 C ANISOU 830 CA LEU A 201 2877 2125 3336 -102 -423 -75 C ATOM 831 C LEU A 201 13.992 12.346 37.395 1.00 19.92 C ANISOU 831 C LEU A 201 2615 1943 3012 -260 -481 -327 C ATOM 832 O LEU A 201 15.202 12.135 37.322 1.00 20.69 O ANISOU 832 O LEU A 201 2907 1911 3042 -626 -578 -448 O ATOM 833 CB LEU A 201 13.906 14.765 36.663 1.00 25.67 C ANISOU 833 CB LEU A 201 3291 2458 4005 -391 -610 45 C ATOM 834 CG LEU A 201 13.766 15.764 35.504 1.00 30.05 C ANISOU 834 CG LEU A 201 3818 2947 4652 -514 -678 -43 C ATOM 835 CD1 LEU A 201 12.311 16.139 35.233 1.00 32.26 C ANISOU 835 CD1 LEU A 201 4104 3219 4936 -411 -728 -20 C ATOM 836 CD2 LEU A 201 14.582 17.027 35.738 1.00 30.85 C ANISOU 836 CD2 LEU A 201 3951 2971 4801 -670 -579 -176 C ATOM 837 N ARG A 202 13.205 11.709 38.257 1.00 17.87 N ANISOU 837 N ARG A 202 2213 1950 2627 -28 -126 -369 N ATOM 838 CA ARG A 202 13.735 10.687 39.156 1.00 17.53 C ANISOU 838 CA ARG A 202 2056 2100 2506 -27 5 -130 C ATOM 839 C ARG A 202 13.496 9.286 38.608 1.00 15.82 C ANISOU 839 C ARG A 202 1759 1997 2256 -174 2 105 C ATOM 840 O ARG A 202 13.721 8.286 39.290 1.00 16.90 O ANISOU 840 O ARG A 202 1795 2165 2460 -47 -81 87 O ATOM 841 CB ARG A 202 13.138 10.846 40.552 1.00 19.40 C ANISOU 841 CB ARG A 202 2433 2271 2669 16 151 -282 C ATOM 842 CG ARG A 202 13.409 12.214 41.160 1.00 22.44 C ANISOU 842 CG ARG A 202 3003 2542 2980 -242 289 -484 C ATOM 843 CD ARG A 202 12.377 12.572 42.207 1.00 26.90 C ANISOU 843 CD ARG A 202 3978 2918 3325 -452 143 -639 C ATOM 844 NE ARG A 202 12.586 11.844 43.453 1.00 30.75 N ANISOU 844 NE ARG A 202 4665 3242 3779 -660 180 -731 N ATOM 845 CZ ARG A 202 11.642 11.637 44.367 1.00 32.68 C ANISOU 845 CZ ARG A 202 4995 3481 3942 -499 303 -798 C ATOM 846 NH1 ARG A 202 10.409 12.084 44.166 1.00 32.75 N1+ ANISOU 846 NH1 ARG A 202 4986 3438 4020 -148 324 -867 N1+ ATOM 847 NH2 ARG A 202 11.927 10.961 45.472 1.00 33.67 N ANISOU 847 NH2 ARG A 202 5202 3643 3949 -652 145 -794 N ATOM 848 N VAL A 203 13.040 9.227 37.362 1.00 13.42 N ANISOU 848 N VAL A 203 1462 1711 1927 -306 0 34 N ATOM 849 CA VAL A 203 12.832 7.961 36.676 1.00 11.38 C ANISOU 849 CA VAL A 203 1361 1327 1635 -355 -312 -137 C ATOM 850 C VAL A 203 14.142 7.158 36.559 1.00 11.67 C ANISOU 850 C VAL A 203 1519 1451 1464 -247 -406 -103 C ATOM 851 O VAL A 203 15.227 7.720 36.365 1.00 11.30 O ANISOU 851 O VAL A 203 1226 1723 1345 224 -28 -240 O ATOM 852 CB VAL A 203 12.212 8.193 35.275 1.00 12.84 C ANISOU 852 CB VAL A 203 1582 1376 1920 -492 -378 -87 C ATOM 853 CG1 VAL A 203 13.174 8.947 34.376 1.00 12.52 C ANISOU 853 CG1 VAL A 203 1669 1279 1810 -536 -197 -54 C ATOM 854 CG2 VAL A 203 11.830 6.889 34.642 1.00 15.32 C ANISOU 854 CG2 VAL A 203 1846 1832 2144 -362 -320 -9 C ATOM 855 N GLU A 204 14.035 5.842 36.705 1.00 12.14 N ANISOU 855 N GLU A 204 1684 1323 1607 -41 -407 195 N ATOM 856 CA GLU A 204 15.191 4.961 36.603 1.00 11.12 C ANISOU 856 CA GLU A 204 1696 1078 1450 -140 -467 405 C ATOM 857 C GLU A 204 14.847 3.817 35.657 1.00 11.50 C ANISOU 857 C GLU A 204 1631 1210 1528 -104 -405 425 C ATOM 858 O GLU A 204 13.725 3.312 35.671 1.00 12.26 O ANISOU 858 O GLU A 204 1584 1313 1762 -554 -184 210 O ATOM 859 CB GLU A 204 15.576 4.438 37.991 1.00 11.20 C ANISOU 859 CB GLU A 204 1713 1200 1342 -212 -354 409 C ATOM 860 CG GLU A 204 16.609 3.323 38.006 1.00 12.51 C ANISOU 860 CG GLU A 204 1917 1459 1375 62 -344 397 C ATOM 861 CD GLU A 204 16.838 2.774 39.399 1.00 13.56 C ANISOU 861 CD GLU A 204 1858 1701 1593 292 -588 142 C ATOM 862 OE1 GLU A 204 16.938 3.576 40.356 1.00 14.84 O ANISOU 862 OE1 GLU A 204 2182 2014 1442 151 -989 155 O ATOM 863 OE2 GLU A 204 16.907 1.535 39.546 1.00 14.38 O1- ANISOU 863 OE2 GLU A 204 1758 1834 1873 561 -502 -75 O1- ATOM 864 N TYR A 205 15.800 3.437 34.812 1.00 11.70 N ANISOU 864 N TYR A 205 1410 1472 1564 50 -427 483 N ATOM 865 CA TYR A 205 15.595 2.341 33.866 1.00 11.83 C ANISOU 865 CA TYR A 205 1511 1554 1429 149 -422 397 C ATOM 866 C TYR A 205 16.571 1.195 34.106 1.00 12.89 C ANISOU 866 C TYR A 205 1597 1725 1575 198 -379 382 C ATOM 867 O TYR A 205 17.748 1.416 34.419 1.00 13.24 O ANISOU 867 O TYR A 205 1559 1846 1625 647 -284 384 O ATOM 868 CB TYR A 205 15.747 2.837 32.433 1.00 11.50 C ANISOU 868 CB TYR A 205 1544 1659 1166 115 -693 258 C ATOM 869 CG TYR A 205 14.697 3.824 31.999 1.00 11.62 C ANISOU 869 CG TYR A 205 1756 1666 992 111 -311 286 C ATOM 870 CD1 TYR A 205 14.873 5.187 32.193 1.00 10.81 C ANISOU 870 CD1 TYR A 205 1670 1447 991 446 -295 344 C ATOM 871 CD2 TYR A 205 13.534 3.392 31.380 1.00 9.67 C ANISOU 871 CD2 TYR A 205 1441 1486 746 159 -393 379 C ATOM 872 CE1 TYR A 205 13.912 6.091 31.788 1.00 10.24 C ANISOU 872 CE1 TYR A 205 1448 1376 1067 211 -499 455 C ATOM 873 CE2 TYR A 205 12.575 4.282 30.973 1.00 9.34 C ANISOU 873 CE2 TYR A 205 1186 1482 879 214 -448 340 C ATOM 874 CZ TYR A 205 12.765 5.625 31.181 1.00 10.49 C ANISOU 874 CZ TYR A 205 1317 1516 1152 339 -532 395 C ATOM 875 OH TYR A 205 11.798 6.505 30.769 1.00 11.56 O ANISOU 875 OH TYR A 205 1388 1451 1552 457 -621 297 O ATOM 876 N LEU A 206 16.076 -0.029 33.932 1.00 12.31 N ANISOU 876 N LEU A 206 1432 1551 1694 -99 -325 492 N ATOM 877 CA LEU A 206 16.862 -1.228 34.206 1.00 11.45 C ANISOU 877 CA LEU A 206 1215 1400 1737 -186 -391 315 C ATOM 878 C LEU A 206 16.867 -2.198 33.030 1.00 12.28 C ANISOU 878 C LEU A 206 1250 1730 1687 -160 -322 149 C ATOM 879 O LEU A 206 15.812 -2.502 32.468 1.00 12.45 O ANISOU 879 O LEU A 206 1107 1908 1715 -58 2 224 O ATOM 880 CB LEU A 206 16.314 -1.952 35.445 1.00 11.48 C ANISOU 880 CB LEU A 206 1168 1344 1850 -111 -204 214 C ATOM 881 CG LEU A 206 17.033 -3.248 35.840 1.00 12.19 C ANISOU 881 CG LEU A 206 1254 1299 2078 -163 -212 283 C ATOM 882 CD1 LEU A 206 18.445 -2.960 36.335 1.00 13.58 C ANISOU 882 CD1 LEU A 206 1329 1494 2336 -179 -425 241 C ATOM 883 CD2 LEU A 206 16.250 -4.018 36.884 1.00 10.13 C ANISOU 883 CD2 LEU A 206 1014 893 1942 46 -112 399 C ATOM 884 N ASP A 207 18.061 -2.657 32.656 1.00 12.78 N ANISOU 884 N ASP A 207 1300 1753 1805 36 -410 276 N ATOM 885 CA ASP A 207 18.222 -3.866 31.857 1.00 13.58 C ANISOU 885 CA ASP A 207 1326 1849 1986 111 -543 255 C ATOM 886 C ASP A 207 18.617 -4.942 32.847 1.00 15.14 C ANISOU 886 C ASP A 207 1403 1875 2476 376 -681 -12 C ATOM 887 O ASP A 207 19.699 -4.867 33.421 1.00 16.41 O ANISOU 887 O ASP A 207 1671 1973 2590 566 -670 -100 O ATOM 888 CB ASP A 207 19.371 -3.731 30.855 1.00 15.70 C ANISOU 888 CB ASP A 207 1593 2376 1995 -40 -339 347 C ATOM 889 CG ASP A 207 19.042 -2.841 29.665 1.00 16.90 C ANISOU 889 CG ASP A 207 1512 2963 1947 -216 -243 592 C ATOM 890 OD1 ASP A 207 17.863 -2.538 29.423 1.00 17.65 O ANISOU 890 OD1 ASP A 207 1565 3152 1989 57 -317 636 O ATOM 891 OD2 ASP A 207 19.991 -2.456 28.951 1.00 17.41 O1- ANISOU 891 OD2 ASP A 207 1437 3291 1888 -316 -102 687 O1- ATOM 892 N ASP A 208 17.760 -5.932 33.067 1.00 16.29 N ANISOU 892 N ASP A 208 1628 1742 2822 457 -758 -67 N ATOM 893 CA ASP A 208 18.093 -6.986 34.020 1.00 17.36 C ANISOU 893 CA ASP A 208 1771 1538 3286 464 -553 -110 C ATOM 894 C ASP A 208 19.290 -7.779 33.511 1.00 19.52 C ANISOU 894 C ASP A 208 1784 1897 3734 351 -530 -256 C ATOM 895 O ASP A 208 19.274 -8.288 32.397 1.00 19.45 O ANISOU 895 O ASP A 208 1590 1884 3917 342 -602 -542 O ATOM 896 CB ASP A 208 16.904 -7.919 34.258 1.00 17.26 C ANISOU 896 CB ASP A 208 2048 1285 3227 400 -449 -33 C ATOM 897 CG ASP A 208 17.067 -8.764 35.515 1.00 17.49 C ANISOU 897 CG ASP A 208 2359 1182 3106 436 -379 -122 C ATOM 898 OD1 ASP A 208 17.751 -9.814 35.463 1.00 17.49 O ANISOU 898 OD1 ASP A 208 2320 1236 3091 163 -627 -170 O ATOM 899 OD2 ASP A 208 16.504 -8.375 36.560 1.00 17.06 O1- ANISOU 899 OD2 ASP A 208 2506 995 2980 608 -167 -169 O1- ATOM 900 N ARG A 209 20.338 -7.871 34.320 1.00 21.90 N ANISOU 900 N ARG A 209 2057 2218 4045 265 -551 -277 N ATOM 901 CA ARG A 209 21.554 -8.547 33.880 1.00 25.72 C ANISOU 901 CA ARG A 209 2629 2703 4440 412 -842 -320 C ATOM 902 C ARG A 209 21.362 -10.056 33.717 1.00 24.80 C ANISOU 902 C ARG A 209 2433 2410 4579 679 -908 -647 C ATOM 903 O ARG A 209 22.122 -10.700 32.999 1.00 25.78 O ANISOU 903 O ARG A 209 2538 2445 4811 598 -759 -687 O ATOM 904 CB ARG A 209 22.703 -8.258 34.845 1.00 30.59 C ANISOU 904 CB ARG A 209 3573 3360 4691 489 -934 -103 C ATOM 905 CG ARG A 209 22.472 -8.853 36.208 1.00 35.56 C ANISOU 905 CG ARG A 209 4377 4090 5044 554 -997 24 C ATOM 906 CD ARG A 209 23.497 -8.402 37.227 1.00 39.78 C ANISOU 906 CD ARG A 209 4988 4744 5383 584 -950 215 C ATOM 907 NE ARG A 209 23.411 -9.226 38.429 1.00 43.26 N ANISOU 907 NE ARG A 209 5491 5302 5644 679 -903 433 N ATOM 908 CZ ARG A 209 22.431 -9.146 39.326 1.00 45.94 C ANISOU 908 CZ ARG A 209 5764 5712 5980 782 -779 615 C ATOM 909 NH1 ARG A 209 21.441 -8.275 39.167 1.00 47.23 N1+ ANISOU 909 NH1 ARG A 209 5945 5917 6083 894 -782 727 N1+ ATOM 910 NH2 ARG A 209 22.442 -9.942 40.388 1.00 46.85 N ANISOU 910 NH2 ARG A 209 5826 5835 6138 672 -638 622 N ATOM 911 N ASN A 210 20.348 -10.615 34.371 1.00 24.69 N ANISOU 911 N ASN A 210 2486 2380 4516 824 -972 -869 N ATOM 912 CA ASN A 210 20.093 -12.055 34.298 1.00 25.34 C ANISOU 912 CA ASN A 210 2502 2601 4525 702 -1040 -954 C ATOM 913 C ASN A 210 18.980 -12.472 33.333 1.00 24.43 C ANISOU 913 C ASN A 210 2221 2440 4621 285 -886 -1040 C ATOM 914 O ASN A 210 19.128 -13.438 32.578 1.00 24.62 O ANISOU 914 O ASN A 210 1929 2504 4922 62 -940 -1088 O ATOM 915 CB ASN A 210 19.815 -12.609 35.693 1.00 26.79 C ANISOU 915 CB ASN A 210 2821 2897 4460 941 -1196 -968 C ATOM 916 CG ASN A 210 21.032 -12.547 36.582 1.00 29.69 C ANISOU 916 CG ASN A 210 3332 3337 4612 977 -1191 -1005 C ATOM 917 ND2 ASN A 210 20.875 -11.966 37.769 1.00 31.27 N ANISOU 917 ND2 ASN A 210 3618 3487 4777 904 -1064 -983 N ATOM 918 OD1 ASN A 210 22.115 -12.998 36.198 1.00 29.57 O ANISOU 918 OD1 ASN A 210 3248 3427 4559 1210 -1372 -1019 O ATOM 919 N THR A 211 17.868 -11.744 33.367 1.00 23.86 N ANISOU 919 N THR A 211 2342 2361 4364 113 -660 -1007 N ATOM 920 CA THR A 211 16.714 -12.062 32.534 1.00 22.10 C ANISOU 920 CA THR A 211 2189 2189 4019 -10 -557 -910 C ATOM 921 C THR A 211 16.667 -11.211 31.268 1.00 22.07 C ANISOU 921 C THR A 211 2382 2293 3709 -15 -451 -810 C ATOM 922 O THR A 211 15.889 -11.500 30.358 1.00 22.93 O ANISOU 922 O THR A 211 2572 2415 3727 -90 -650 -810 O ATOM 923 CB THR A 211 15.397 -11.847 33.299 1.00 20.73 C ANISOU 923 CB THR A 211 1952 1926 4001 -175 -442 -936 C ATOM 924 CG2 THR A 211 15.439 -12.538 34.647 1.00 20.72 C ANISOU 924 CG2 THR A 211 1961 1910 4000 -371 -424 -756 C ATOM 925 OG1 THR A 211 15.193 -10.445 33.493 1.00 20.00 O ANISOU 925 OG1 THR A 211 1901 1685 4012 -131 -302 -1051 O ATOM 926 N PHE A 212 17.479 -10.156 31.238 1.00 19.78 N ANISOU 926 N PHE A 212 2097 2097 3320 -55 -83 -754 N ATOM 927 CA PHE A 212 17.553 -9.217 30.112 1.00 19.49 C ANISOU 927 CA PHE A 212 2125 2149 3133 186 148 -633 C ATOM 928 C PHE A 212 16.277 -8.416 29.884 1.00 18.13 C ANISOU 928 C PHE A 212 1828 2337 2723 -2 76 -599 C ATOM 929 O PHE A 212 16.170 -7.683 28.901 1.00 17.15 O ANISOU 929 O PHE A 212 1574 2592 2351 -185 2 -790 O ATOM 930 CB PHE A 212 17.999 -9.909 28.821 1.00 20.48 C ANISOU 930 CB PHE A 212 2407 2036 3340 340 239 -662 C ATOM 931 CG PHE A 212 19.096 -10.902 29.023 1.00 22.92 C ANISOU 931 CG PHE A 212 2705 2272 3732 439 341 -687 C ATOM 932 CD1 PHE A 212 20.304 -10.517 29.584 1.00 23.95 C ANISOU 932 CD1 PHE A 212 2726 2417 3956 640 494 -736 C ATOM 933 CD2 PHE A 212 18.919 -12.222 28.653 1.00 24.38 C ANISOU 933 CD2 PHE A 212 2873 2403 3986 707 395 -705 C ATOM 934 CE1 PHE A 212 21.319 -11.437 29.779 1.00 25.42 C ANISOU 934 CE1 PHE A 212 3057 2440 4163 518 556 -777 C ATOM 935 CE2 PHE A 212 19.922 -13.149 28.840 1.00 25.75 C ANISOU 935 CE2 PHE A 212 3010 2558 4214 646 486 -743 C ATOM 936 CZ PHE A 212 21.127 -12.757 29.405 1.00 25.97 C ANISOU 936 CZ PHE A 212 3074 2550 4246 547 498 -834 C ATOM 937 N ARG A 213 15.324 -8.544 30.805 1.00 18.04 N ANISOU 937 N ARG A 213 1906 2254 2694 -15 49 -607 N ATOM 938 CA ARG A 213 14.080 -7.775 30.748 1.00 17.37 C ANISOU 938 CA ARG A 213 1974 2079 2548 48 -88 -436 C ATOM 939 C ARG A 213 14.335 -6.281 30.969 1.00 15.32 C ANISOU 939 C ARG A 213 1715 1871 2235 -36 -4 -443 C ATOM 940 O ARG A 213 15.225 -5.885 31.735 1.00 14.01 O ANISOU 940 O ARG A 213 1299 1799 2225 -136 -179 -642 O ATOM 941 CB ARG A 213 13.063 -8.280 31.789 1.00 17.52 C ANISOU 941 CB ARG A 213 1900 1927 2831 -136 -153 -169 C ATOM 942 CG ARG A 213 12.730 -9.765 31.717 1.00 17.88 C ANISOU 942 CG ARG A 213 1985 1877 2933 -193 -23 -238 C ATOM 943 CD ARG A 213 11.613 -10.058 30.758 1.00 17.94 C ANISOU 943 CD ARG A 213 2031 1761 3026 -182 75 -124 C ATOM 944 NE ARG A 213 11.292 -11.485 30.703 1.00 17.85 N ANISOU 944 NE ARG A 213 2081 1703 2999 -282 378 175 N ATOM 945 CZ ARG A 213 10.412 -12.010 29.857 1.00 17.95 C ANISOU 945 CZ ARG A 213 2146 1829 2846 -424 730 198 C ATOM 946 NH1 ARG A 213 9.775 -11.221 29.006 1.00 17.72 N1+ ANISOU 946 NH1 ARG A 213 1948 1883 2899 -363 712 137 N1+ ATOM 947 NH2 ARG A 213 10.172 -13.316 29.857 1.00 18.57 N ANISOU 947 NH2 ARG A 213 2346 2001 2707 -550 922 476 N ATOM 948 N HIS A 214 13.548 -5.457 30.289 1.00 13.78 N ANISOU 948 N HIS A 214 1637 1745 1853 -14 295 -313 N ATOM 949 CA HIS A 214 13.592 -4.017 30.490 1.00 12.57 C ANISOU 949 CA HIS A 214 1590 1574 1611 -98 252 -185 C ATOM 950 C HIS A 214 12.500 -3.608 31.482 1.00 11.52 C ANISOU 950 C HIS A 214 1574 1400 1403 -47 138 -13 C ATOM 951 O HIS A 214 11.413 -4.188 31.507 1.00 11.26 O ANISOU 951 O HIS A 214 1395 1310 1573 -151 460 -239 O ATOM 952 CB HIS A 214 13.377 -3.290 29.161 1.00 12.43 C ANISOU 952 CB HIS A 214 1580 1664 1477 -144 263 -256 C ATOM 953 CG HIS A 214 14.345 -3.683 28.087 1.00 14.44 C ANISOU 953 CG HIS A 214 1803 1957 1728 263 345 -576 C ATOM 954 CD2 HIS A 214 15.565 -4.269 28.155 1.00 15.02 C ANISOU 954 CD2 HIS A 214 1813 2055 1839 388 620 -747 C ATOM 955 ND1 HIS A 214 14.100 -3.461 26.749 1.00 16.26 N ANISOU 955 ND1 HIS A 214 2003 2271 1905 452 212 -684 N ATOM 956 CE1 HIS A 214 15.123 -3.899 26.037 1.00 16.33 C ANISOU 956 CE1 HIS A 214 2000 2338 1867 585 314 -770 C ATOM 957 NE2 HIS A 214 16.025 -4.392 26.866 1.00 15.99 N ANISOU 957 NE2 HIS A 214 1952 2241 1885 452 530 -700 N ATOM 958 N SER A 215 12.786 -2.611 32.307 1.00 10.13 N ANISOU 958 N SER A 215 1416 1350 1084 -33 -54 141 N ATOM 959 CA SER A 215 11.757 -2.066 33.178 1.00 10.26 C ANISOU 959 CA SER A 215 1069 1579 1250 -15 -136 156 C ATOM 960 C SER A 215 12.076 -0.641 33.552 1.00 10.49 C ANISOU 960 C SER A 215 1185 1629 1172 129 95 132 C ATOM 961 O SER A 215 13.221 -0.206 33.459 1.00 12.31 O ANISOU 961 O SER A 215 1585 1740 1353 235 395 -182 O ATOM 962 CB SER A 215 11.581 -2.924 34.432 1.00 9.76 C ANISOU 962 CB SER A 215 759 1573 1377 -317 -191 242 C ATOM 963 OG SER A 215 12.775 -2.999 35.191 1.00 10.76 O ANISOU 963 OG SER A 215 856 1662 1570 -327 -490 596 O ATOM 964 N VAL A 216 11.055 0.082 33.986 1.00 10.39 N ANISOU 964 N VAL A 216 1166 1794 987 141 -98 -7 N ATOM 965 CA VAL A 216 11.223 1.476 34.359 1.00 10.65 C ANISOU 965 CA VAL A 216 1301 1818 926 157 -158 -149 C ATOM 966 C VAL A 216 10.628 1.709 35.742 1.00 11.36 C ANISOU 966 C VAL A 216 1471 2045 803 38 -468 -67 C ATOM 967 O VAL A 216 9.469 1.374 35.994 1.00 11.51 O ANISOU 967 O VAL A 216 1550 2205 618 58 -250 6 O ATOM 968 CB VAL A 216 10.571 2.414 33.327 1.00 11.60 C ANISOU 968 CB VAL A 216 1479 1920 1008 200 -201 -380 C ATOM 969 CG1 VAL A 216 9.123 1.990 33.023 1.00 11.14 C ANISOU 969 CG1 VAL A 216 1329 2001 905 105 -522 -267 C ATOM 970 CG2 VAL A 216 10.633 3.824 33.816 1.00 11.74 C ANISOU 970 CG2 VAL A 216 1581 1745 1136 350 35 -472 C ATOM 971 N VAL A 217 11.424 2.269 36.645 1.00 11.99 N ANISOU 971 N VAL A 217 1470 2106 981 160 -623 -120 N ATOM 972 CA VAL A 217 11.018 2.363 38.043 1.00 13.08 C ANISOU 972 CA VAL A 217 1687 2093 1189 427 -334 3 C ATOM 973 C VAL A 217 11.040 3.819 38.518 1.00 13.89 C ANISOU 973 C VAL A 217 1761 2180 1339 506 -241 -33 C ATOM 974 O VAL A 217 11.863 4.619 38.061 1.00 14.80 O ANISOU 974 O VAL A 217 1920 2291 1412 384 -22 -240 O ATOM 975 CB VAL A 217 11.876 1.412 38.946 1.00 12.19 C ANISOU 975 CB VAL A 217 1578 2008 1046 632 -344 167 C ATOM 976 CG1 VAL A 217 13.331 1.850 38.978 1.00 11.14 C ANISOU 976 CG1 VAL A 217 1334 1650 1247 697 -204 361 C ATOM 977 CG2 VAL A 217 11.298 1.308 40.353 1.00 10.82 C ANISOU 977 CG2 VAL A 217 1321 2082 707 583 -180 108 C ATOM 978 N VAL A 218 10.117 4.155 39.416 1.00 12.91 N ANISOU 978 N VAL A 218 1407 2135 1365 719 -231 199 N ATOM 979 CA VAL A 218 9.895 5.530 39.843 1.00 13.83 C ANISOU 979 CA VAL A 218 1745 2199 1311 309 -279 219 C ATOM 980 C VAL A 218 9.627 5.551 41.354 1.00 14.14 C ANISOU 980 C VAL A 218 1742 2132 1499 8 -367 143 C ATOM 981 O VAL A 218 8.959 4.658 41.865 1.00 13.07 O ANISOU 981 O VAL A 218 1793 1866 1307 35 -408 548 O ATOM 982 CB VAL A 218 8.672 6.125 39.093 1.00 14.35 C ANISOU 982 CB VAL A 218 2114 2285 1051 468 -358 500 C ATOM 983 CG1 VAL A 218 8.255 7.446 39.693 1.00 16.45 C ANISOU 983 CG1 VAL A 218 2439 2281 1529 752 -506 603 C ATOM 984 CG2 VAL A 218 8.956 6.290 37.600 1.00 14.31 C ANISOU 984 CG2 VAL A 218 1990 2568 879 385 -392 236 C ATOM 985 N PRO A 219 10.165 6.554 42.079 1.00 16.44 N ANISOU 985 N PRO A 219 1973 2471 1803 -12 -296 -308 N ATOM 986 CA PRO A 219 9.839 6.716 43.505 1.00 16.27 C ANISOU 986 CA PRO A 219 1784 2652 1744 -130 -413 -385 C ATOM 987 C PRO A 219 8.344 6.942 43.703 1.00 17.35 C ANISOU 987 C PRO A 219 2036 2820 1735 -52 -303 -244 C ATOM 988 O PRO A 219 7.785 7.811 43.030 1.00 17.05 O ANISOU 988 O PRO A 219 2031 2784 1664 -92 -350 -196 O ATOM 989 CB PRO A 219 10.568 8.005 43.885 1.00 16.99 C ANISOU 989 CB PRO A 219 1897 2687 1873 -262 -384 -570 C ATOM 990 CG PRO A 219 11.653 8.152 42.883 1.00 18.08 C ANISOU 990 CG PRO A 219 2254 2761 1854 -343 -460 -617 C ATOM 991 CD PRO A 219 11.123 7.573 41.609 1.00 17.49 C ANISOU 991 CD PRO A 219 2095 2655 1896 -379 -497 -674 C ATOM 992 N TYR A 220 7.709 6.190 44.599 1.00 17.37 N ANISOU 992 N TYR A 220 1967 3021 1613 47 -107 -188 N ATOM 993 CA TYR A 220 6.299 6.422 44.910 1.00 17.77 C ANISOU 993 CA TYR A 220 2105 3034 1613 154 300 -397 C ATOM 994 C TYR A 220 6.155 7.707 45.699 1.00 19.46 C ANISOU 994 C TYR A 220 2292 3177 1923 231 333 -545 C ATOM 995 O TYR A 220 6.897 7.942 46.647 1.00 20.21 O ANISOU 995 O TYR A 220 2342 3252 2083 354 418 -511 O ATOM 996 CB TYR A 220 5.705 5.267 45.723 1.00 17.08 C ANISOU 996 CB TYR A 220 2151 2897 1440 174 371 -483 C ATOM 997 CG TYR A 220 4.283 5.530 46.188 1.00 17.44 C ANISOU 997 CG TYR A 220 2355 2866 1407 315 478 -419 C ATOM 998 CD1 TYR A 220 3.202 5.298 45.348 1.00 17.33 C ANISOU 998 CD1 TYR A 220 2109 2967 1509 313 562 -259 C ATOM 999 CD2 TYR A 220 4.026 6.004 47.463 1.00 18.12 C ANISOU 999 CD2 TYR A 220 2522 2837 1528 464 557 -563 C ATOM 1000 CE1 TYR A 220 1.909 5.538 45.761 1.00 17.77 C ANISOU 1000 CE1 TYR A 220 2358 2906 1487 316 634 -335 C ATOM 1001 CE2 TYR A 220 2.735 6.243 47.888 1.00 17.44 C ANISOU 1001 CE2 TYR A 220 2261 2921 1444 489 631 -506 C ATOM 1002 CZ TYR A 220 1.682 6.009 47.034 1.00 17.56 C ANISOU 1002 CZ TYR A 220 2342 3030 1300 351 445 -520 C ATOM 1003 OH TYR A 220 0.398 6.251 47.454 1.00 18.38 O ANISOU 1003 OH TYR A 220 2522 3354 1106 490 117 -601 O ATOM 1004 N GLU A 221 5.201 8.541 45.304 1.00 22.25 N ANISOU 1004 N GLU A 221 2790 3413 2251 265 251 -852 N ATOM 1005 CA GLU A 221 4.821 9.695 46.104 1.00 25.83 C ANISOU 1005 CA GLU A 221 3323 3825 2665 385 145 -1149 C ATOM 1006 C GLU A 221 3.336 9.585 46.409 1.00 26.13 C ANISOU 1006 C GLU A 221 3332 3811 2787 610 163 -1097 C ATOM 1007 O GLU A 221 2.534 9.307 45.514 1.00 25.43 O ANISOU 1007 O GLU A 221 3151 3735 2778 626 188 -1255 O ATOM 1008 CB GLU A 221 5.137 11.010 45.380 1.00 29.88 C ANISOU 1008 CB GLU A 221 3963 4254 3137 442 183 -1408 C ATOM 1009 CG GLU A 221 6.628 11.286 45.177 1.00 34.34 C ANISOU 1009 CG GLU A 221 4610 4831 3608 475 337 -1550 C ATOM 1010 CD GLU A 221 7.359 11.639 46.469 1.00 38.81 C ANISOU 1010 CD GLU A 221 5143 5470 4132 572 703 -1530 C ATOM 1011 OE1 GLU A 221 6.722 12.191 47.394 1.00 40.72 O ANISOU 1011 OE1 GLU A 221 5437 5760 4274 618 898 -1577 O ATOM 1012 OE2 GLU A 221 8.580 11.369 46.559 1.00 39.84 O1- ANISOU 1012 OE2 GLU A 221 5156 5652 4331 466 718 -1505 O1- ATOM 1013 N PRO A 222 2.962 9.779 47.683 1.00 26.77 N ANISOU 1013 N PRO A 222 3403 3792 2977 656 42 -1046 N ATOM 1014 CA PRO A 222 1.549 9.685 48.065 1.00 27.48 C ANISOU 1014 CA PRO A 222 3473 3773 3197 803 87 -997 C ATOM 1015 C PRO A 222 0.774 10.829 47.427 1.00 28.20 C ANISOU 1015 C PRO A 222 3456 3767 3492 995 249 -1033 C ATOM 1016 O PRO A 222 1.397 11.825 47.057 1.00 28.55 O ANISOU 1016 O PRO A 222 3488 3665 3694 1050 371 -851 O ATOM 1017 CB PRO A 222 1.590 9.846 49.589 1.00 27.39 C ANISOU 1017 CB PRO A 222 3471 3798 3136 640 -40 -1065 C ATOM 1018 CG PRO A 222 2.846 10.618 49.852 1.00 26.93 C ANISOU 1018 CG PRO A 222 3352 3819 3059 456 -290 -1051 C ATOM 1019 CD PRO A 222 3.825 10.136 48.824 1.00 26.60 C ANISOU 1019 CD PRO A 222 3308 3815 2985 426 -190 -1043 C ATOM 1020 N PRO A 223 -0.555 10.688 47.275 1.00 28.70 N ANISOU 1020 N PRO A 223 3515 3871 3518 965 331 -1322 N ATOM 1021 CA PRO A 223 -1.312 11.773 46.638 1.00 29.54 C ANISOU 1021 CA PRO A 223 3505 3920 3800 1190 362 -1322 C ATOM 1022 C PRO A 223 -1.336 13.011 47.522 1.00 32.07 C ANISOU 1022 C PRO A 223 3782 4141 4261 1313 266 -1093 C ATOM 1023 O PRO A 223 -1.106 12.894 48.728 1.00 32.04 O ANISOU 1023 O PRO A 223 3914 4016 4243 1349 36 -1169 O ATOM 1024 CB PRO A 223 -2.731 11.202 46.526 1.00 28.40 C ANISOU 1024 CB PRO A 223 3319 3830 3643 1148 502 -1477 C ATOM 1025 CG PRO A 223 -2.597 9.724 46.734 1.00 28.23 C ANISOU 1025 CG PRO A 223 3293 3882 3551 1012 524 -1429 C ATOM 1026 CD PRO A 223 -1.408 9.540 47.627 1.00 28.14 C ANISOU 1026 CD PRO A 223 3417 3871 3402 891 385 -1493 C ATOM 1027 N GLU A 224 -1.610 14.173 46.933 1.00 34.79 N ANISOU 1027 N GLU A 224 4105 4459 4655 1232 462 -966 N ATOM 1028 CA GLU A 224 -1.899 15.372 47.709 1.00 36.55 C ANISOU 1028 CA GLU A 224 4374 4584 4929 1355 535 -1038 C ATOM 1029 C GLU A 224 -3.011 14.996 48.680 1.00 37.50 C ANISOU 1029 C GLU A 224 4344 4815 5090 1583 589 -1276 C ATOM 1030 O GLU A 224 -3.823 14.119 48.383 1.00 38.39 O ANISOU 1030 O GLU A 224 4432 4978 5174 1618 615 -1395 O ATOM 1031 CB GLU A 224 -2.374 16.495 46.787 1.00 37.57 C ANISOU 1031 CB GLU A 224 4572 4587 5116 1343 443 -863 C ATOM 1032 CG GLU A 224 -1.608 17.810 46.898 1.00 38.72 C ANISOU 1032 CG GLU A 224 4806 4665 5240 1367 293 -777 C ATOM 1033 CD GLU A 224 -2.225 18.891 46.028 1.00 38.92 C ANISOU 1033 CD GLU A 224 4920 4619 5249 1372 91 -668 C ATOM 1034 OE1 GLU A 224 -3.030 18.535 45.143 1.00 38.95 O ANISOU 1034 OE1 GLU A 224 4879 4695 5226 1408 -18 -544 O ATOM 1035 OE2 GLU A 224 -1.920 20.086 46.228 1.00 38.93 O1- ANISOU 1035 OE2 GLU A 224 5025 4491 5275 1250 78 -693 O1- ATOM 1036 N VAL A 225 -3.042 15.638 49.842 1.00 37.89 N ANISOU 1036 N VAL A 225 4401 4867 5127 1686 609 -1327 N ATOM 1037 CA VAL A 225 -4.011 15.286 50.880 1.00 38.49 C ANISOU 1037 CA VAL A 225 4590 4853 5183 1702 452 -1350 C ATOM 1038 C VAL A 225 -5.460 15.332 50.372 1.00 39.48 C ANISOU 1038 C VAL A 225 4629 5030 5341 1892 473 -1351 C ATOM 1039 O VAL A 225 -6.302 14.523 50.775 1.00 40.92 O ANISOU 1039 O VAL A 225 4816 5269 5464 1705 335 -1300 O ATOM 1040 CB VAL A 225 -3.812 16.160 52.132 1.00 37.27 C ANISOU 1040 CB VAL A 225 4608 4522 5029 1656 301 -1454 C ATOM 1041 CG1 VAL A 225 -4.941 15.963 53.135 1.00 35.91 C ANISOU 1041 CG1 VAL A 225 4450 4342 4853 1673 352 -1397 C ATOM 1042 CG2 VAL A 225 -2.471 15.840 52.765 1.00 37.56 C ANISOU 1042 CG2 VAL A 225 4756 4471 5043 1519 246 -1537 C ATOM 1043 N GLY A 226 -5.733 16.252 49.455 1.00 38.47 N ANISOU 1043 N GLY A 226 4471 4830 5316 2265 518 -1453 N ATOM 1044 CA GLY A 226 -7.057 16.353 48.870 1.00 38.33 C ANISOU 1044 CA GLY A 226 4433 4702 5427 2162 660 -1492 C ATOM 1045 C GLY A 226 -7.292 15.420 47.692 1.00 38.74 C ANISOU 1045 C GLY A 226 4386 4789 5545 2037 718 -1428 C ATOM 1046 O GLY A 226 -8.361 15.459 47.081 1.00 39.02 O ANISOU 1046 O GLY A 226 4332 4877 5615 2107 741 -1506 O ATOM 1047 N SER A 227 -6.302 14.582 47.377 1.00 37.97 N ANISOU 1047 N SER A 227 4226 4647 5555 1856 800 -1286 N ATOM 1048 CA SER A 227 -6.385 13.678 46.225 1.00 37.48 C ANISOU 1048 CA SER A 227 4189 4608 5442 1521 854 -1036 C ATOM 1049 C SER A 227 -6.530 12.203 46.611 1.00 36.04 C ANISOU 1049 C SER A 227 3952 4437 5302 1333 896 -891 C ATOM 1050 O SER A 227 -6.181 11.804 47.724 1.00 36.44 O ANISOU 1050 O SER A 227 4035 4379 5430 1277 714 -690 O ATOM 1051 CB SER A 227 -5.181 13.872 45.303 1.00 38.71 C ANISOU 1051 CB SER A 227 4481 4716 5511 1361 745 -892 C ATOM 1052 OG SER A 227 -5.222 15.150 44.702 1.00 39.74 O ANISOU 1052 OG SER A 227 4680 4820 5598 1308 712 -829 O ATOM 1053 N ASP A 228 -7.042 11.406 45.677 1.00 33.98 N ANISOU 1053 N ASP A 228 3581 4318 5013 1205 1102 -955 N ATOM 1054 CA ASP A 228 -7.357 10.004 45.933 1.00 33.28 C ANISOU 1054 CA ASP A 228 3487 4365 4792 969 1192 -829 C ATOM 1055 C ASP A 228 -6.251 9.054 45.485 1.00 29.84 C ANISOU 1055 C ASP A 228 3107 4122 4107 652 1019 -639 C ATOM 1056 O ASP A 228 -6.105 7.960 46.029 1.00 29.39 O ANISOU 1056 O ASP A 228 3097 4019 4052 473 1245 -622 O ATOM 1057 CB ASP A 228 -8.660 9.613 45.225 1.00 36.61 C ANISOU 1057 CB ASP A 228 3819 4743 5349 856 1204 -835 C ATOM 1058 CG ASP A 228 -9.893 10.210 45.876 1.00 41.31 C ANISOU 1058 CG ASP A 228 4497 5210 5988 515 954 -841 C ATOM 1059 OD1 ASP A 228 -9.766 11.230 46.588 1.00 42.87 O ANISOU 1059 OD1 ASP A 228 4789 5329 6171 246 901 -835 O ATOM 1060 OD2 ASP A 228 -10.998 9.653 45.666 1.00 42.81 O1- ANISOU 1060 OD2 ASP A 228 4608 5414 6245 545 817 -890 O1- ATOM 1061 N CYS A 229 -5.478 9.467 44.486 1.00 26.78 N ANISOU 1061 N CYS A 229 2772 3895 3507 536 587 -588 N ATOM 1062 CA CYS A 229 -4.490 8.577 43.890 1.00 23.48 C ANISOU 1062 CA CYS A 229 2329 3512 3082 158 288 -545 C ATOM 1063 C CYS A 229 -3.305 9.332 43.317 1.00 21.45 C ANISOU 1063 C CYS A 229 2065 3386 2697 -213 284 -407 C ATOM 1064 O CYS A 229 -3.302 10.562 43.245 1.00 21.39 O ANISOU 1064 O CYS A 229 1959 3440 2729 -449 293 -203 O ATOM 1065 CB CYS A 229 -5.128 7.738 42.783 1.00 22.41 C ANISOU 1065 CB CYS A 229 2330 3258 2927 84 115 -691 C ATOM 1066 SG CYS A 229 -5.853 8.734 41.470 1.00 22.82 S ANISOU 1066 SG CYS A 229 2522 3179 2969 -59 189 -835 S ATOM 1067 N THR A 230 -2.300 8.570 42.908 1.00 20.09 N ANISOU 1067 N THR A 230 1979 3312 2343 -391 44 -536 N ATOM 1068 CA THR A 230 -1.120 9.117 42.269 1.00 19.65 C ANISOU 1068 CA THR A 230 2039 3327 2100 -430 61 -551 C ATOM 1069 C THR A 230 -1.180 8.773 40.790 1.00 18.97 C ANISOU 1069 C THR A 230 2152 2916 2141 -510 -16 -697 C ATOM 1070 O THR A 230 -1.361 7.611 40.426 1.00 18.63 O ANISOU 1070 O THR A 230 2359 2680 2041 -709 -117 -660 O ATOM 1071 CB THR A 230 0.152 8.521 42.881 1.00 19.06 C ANISOU 1071 CB THR A 230 1688 3568 1988 -393 -224 -447 C ATOM 1072 CG2 THR A 230 1.384 9.043 42.167 1.00 19.63 C ANISOU 1072 CG2 THR A 230 1811 3516 2132 -727 -462 -446 C ATOM 1073 OG1 THR A 230 0.218 8.873 44.267 1.00 20.85 O ANISOU 1073 OG1 THR A 230 1909 3834 2179 -37 -264 -175 O ATOM 1074 N THR A 231 -1.036 9.782 39.937 1.00 18.39 N ANISOU 1074 N THR A 231 2036 2637 2314 -431 9 -692 N ATOM 1075 CA THR A 231 -1.052 9.558 38.497 1.00 18.67 C ANISOU 1075 CA THR A 231 1837 2722 2533 -432 23 -661 C ATOM 1076 C THR A 231 0.365 9.549 37.935 1.00 19.25 C ANISOU 1076 C THR A 231 1874 2782 2660 -474 143 -593 C ATOM 1077 O THR A 231 1.169 10.448 38.210 1.00 19.40 O ANISOU 1077 O THR A 231 1697 2873 2799 -541 336 -542 O ATOM 1078 CB THR A 231 -1.894 10.618 37.770 1.00 19.94 C ANISOU 1078 CB THR A 231 2028 2886 2660 -357 142 -646 C ATOM 1079 CG2 THR A 231 -1.982 10.311 36.270 1.00 19.77 C ANISOU 1079 CG2 THR A 231 2031 2862 2619 -296 141 -530 C ATOM 1080 OG1 THR A 231 -3.211 10.637 38.331 1.00 20.92 O ANISOU 1080 OG1 THR A 231 2117 3079 2754 -187 179 -678 O ATOM 1081 N ILE A 232 0.667 8.514 37.161 1.00 18.76 N ANISOU 1081 N ILE A 232 1811 2800 2516 -427 -116 -564 N ATOM 1082 CA ILE A 232 1.937 8.412 36.460 1.00 18.94 C ANISOU 1082 CA ILE A 232 1972 2779 2444 -340 -371 -346 C ATOM 1083 C ILE A 232 1.636 8.487 34.966 1.00 17.26 C ANISOU 1083 C ILE A 232 1832 2406 2322 -355 -502 -250 C ATOM 1084 O ILE A 232 0.595 8.004 34.518 1.00 18.18 O ANISOU 1084 O ILE A 232 1977 2483 2449 -269 -643 -181 O ATOM 1085 CB ILE A 232 2.689 7.106 36.847 1.00 20.40 C ANISOU 1085 CB ILE A 232 2166 2938 2646 -77 -491 -192 C ATOM 1086 CG1 ILE A 232 4.052 7.025 36.166 1.00 21.13 C ANISOU 1086 CG1 ILE A 232 2229 3189 2611 15 -480 -243 C ATOM 1087 CG2 ILE A 232 1.865 5.883 36.522 1.00 21.32 C ANISOU 1087 CG2 ILE A 232 2399 2938 2762 54 -630 8 C ATOM 1088 CD1 ILE A 232 5.035 8.025 36.698 1.00 23.02 C ANISOU 1088 CD1 ILE A 232 2515 3505 2727 191 -385 -262 C ATOM 1089 N HIS A 233 2.516 9.132 34.209 1.00 14.61 N ANISOU 1089 N HIS A 233 1467 1976 2107 -370 -178 -228 N ATOM 1090 CA HIS A 233 2.326 9.268 32.770 1.00 14.21 C ANISOU 1090 CA HIS A 233 1638 1729 2033 -102 -259 -63 C ATOM 1091 C HIS A 233 3.317 8.390 32.022 1.00 13.01 C ANISOU 1091 C HIS A 233 1539 1743 1661 -13 -319 70 C ATOM 1092 O HIS A 233 4.502 8.708 31.948 1.00 12.79 O ANISOU 1092 O HIS A 233 1206 1886 1767 194 -91 -51 O ATOM 1093 CB HIS A 233 2.502 10.726 32.328 1.00 14.90 C ANISOU 1093 CB HIS A 233 1982 1407 2271 165 -300 -79 C ATOM 1094 CG HIS A 233 1.350 11.613 32.685 1.00 17.00 C ANISOU 1094 CG HIS A 233 2315 1475 2670 337 31 105 C ATOM 1095 CD2 HIS A 233 0.116 11.328 33.163 1.00 16.88 C ANISOU 1095 CD2 HIS A 233 2233 1382 2798 504 87 153 C ATOM 1096 ND1 HIS A 233 1.398 12.984 32.543 1.00 18.86 N ANISOU 1096 ND1 HIS A 233 2615 1739 2814 581 232 63 N ATOM 1097 CE1 HIS A 233 0.244 13.504 32.926 1.00 18.86 C ANISOU 1097 CE1 HIS A 233 2558 1748 2858 441 122 174 C ATOM 1098 NE2 HIS A 233 -0.551 12.520 33.306 1.00 17.36 N ANISOU 1098 NE2 HIS A 233 2318 1443 2837 197 42 240 N ATOM 1099 N TYR A 234 2.835 7.284 31.472 1.00 11.44 N ANISOU 1099 N TYR A 234 1329 1733 1287 -174 -592 346 N ATOM 1100 CA TYR A 234 3.686 6.431 30.659 1.00 11.19 C ANISOU 1100 CA TYR A 234 1274 1715 1265 -32 -409 319 C ATOM 1101 C TYR A 234 3.614 6.817 29.183 1.00 12.11 C ANISOU 1101 C TYR A 234 1430 1953 1220 65 -205 204 C ATOM 1102 O TYR A 234 2.605 7.368 28.728 1.00 11.31 O ANISOU 1102 O TYR A 234 1283 2079 935 418 120 -81 O ATOM 1103 CB TYR A 234 3.291 4.964 30.828 1.00 10.80 C ANISOU 1103 CB TYR A 234 1228 1534 1342 -76 -518 529 C ATOM 1104 CG TYR A 234 3.628 4.388 32.174 1.00 12.15 C ANISOU 1104 CG TYR A 234 1438 1557 1620 -186 -197 667 C ATOM 1105 CD1 TYR A 234 4.950 4.224 32.572 1.00 12.54 C ANISOU 1105 CD1 TYR A 234 1471 1489 1803 -209 -271 596 C ATOM 1106 CD2 TYR A 234 2.627 4.003 33.052 1.00 12.92 C ANISOU 1106 CD2 TYR A 234 1288 1819 1802 -382 -281 737 C ATOM 1107 CE1 TYR A 234 5.264 3.692 33.819 1.00 11.91 C ANISOU 1107 CE1 TYR A 234 1336 1441 1747 -40 -339 649 C ATOM 1108 CE2 TYR A 234 2.931 3.461 34.293 1.00 13.18 C ANISOU 1108 CE2 TYR A 234 1335 1942 1729 -196 -317 578 C ATOM 1109 CZ TYR A 234 4.248 3.314 34.670 1.00 12.41 C ANISOU 1109 CZ TYR A 234 1376 1699 1641 46 -386 669 C ATOM 1110 OH TYR A 234 4.536 2.784 35.902 1.00 12.33 O ANISOU 1110 OH TYR A 234 1415 1815 1454 -99 -430 525 O ATOM 1111 N ASN A 235 4.695 6.533 28.455 1.00 12.44 N ANISOU 1111 N ASN A 235 1307 2133 1288 -179 -249 167 N ATOM 1112 CA ASN A 235 4.723 6.602 26.996 1.00 13.62 C ANISOU 1112 CA ASN A 235 1510 2236 1428 -251 -706 108 C ATOM 1113 C ASN A 235 5.155 5.246 26.450 1.00 13.11 C ANISOU 1113 C ASN A 235 1363 2149 1469 -184 -644 395 C ATOM 1114 O ASN A 235 6.135 4.670 26.914 1.00 13.83 O ANISOU 1114 O ASN A 235 1492 2133 1630 -103 -517 482 O ATOM 1115 CB ASN A 235 5.706 7.670 26.485 1.00 15.15 C ANISOU 1115 CB ASN A 235 1680 2389 1686 -560 -699 126 C ATOM 1116 CG ASN A 235 5.431 9.067 27.032 1.00 17.86 C ANISOU 1116 CG ASN A 235 1920 2580 2287 -919 -860 300 C ATOM 1117 ND2 ASN A 235 4.164 9.403 27.219 1.00 18.28 N ANISOU 1117 ND2 ASN A 235 2056 2642 2248 -570 -897 401 N ATOM 1118 OD1 ASN A 235 6.362 9.834 27.279 1.00 20.29 O ANISOU 1118 OD1 ASN A 235 2130 2694 2887 -1071 -604 444 O ATOM 1119 N TYR A 236 4.418 4.738 25.472 1.00 12.91 N ANISOU 1119 N TYR A 236 1429 2156 1319 -405 -213 503 N ATOM 1120 CA TYR A 236 4.785 3.509 24.787 1.00 11.89 C ANISOU 1120 CA TYR A 236 1238 1993 1287 -267 110 652 C ATOM 1121 C TYR A 236 5.411 3.886 23.448 1.00 13.35 C ANISOU 1121 C TYR A 236 1320 2323 1430 -7 -73 718 C ATOM 1122 O TYR A 236 4.789 4.571 22.626 1.00 13.77 O ANISOU 1122 O TYR A 236 1469 2326 1439 356 -169 897 O ATOM 1123 CB TYR A 236 3.561 2.609 24.608 1.00 11.69 C ANISOU 1123 CB TYR A 236 1254 1878 1309 -153 109 308 C ATOM 1124 CG TYR A 236 3.082 1.998 25.908 1.00 11.97 C ANISOU 1124 CG TYR A 236 1372 1932 1242 -576 -97 214 C ATOM 1125 CD1 TYR A 236 2.292 2.727 26.789 1.00 12.44 C ANISOU 1125 CD1 TYR A 236 1294 1964 1467 -866 25 188 C ATOM 1126 CD2 TYR A 236 3.427 0.699 26.260 1.00 10.72 C ANISOU 1126 CD2 TYR A 236 1250 1764 1058 -744 -413 439 C ATOM 1127 CE1 TYR A 236 1.863 2.183 27.993 1.00 12.68 C ANISOU 1127 CE1 TYR A 236 1287 1963 1567 -867 -4 326 C ATOM 1128 CE2 TYR A 236 2.998 0.145 27.456 1.00 12.18 C ANISOU 1128 CE2 TYR A 236 1431 1926 1271 -696 -276 657 C ATOM 1129 CZ TYR A 236 2.214 0.893 28.319 1.00 12.15 C ANISOU 1129 CZ TYR A 236 1293 2025 1298 -561 -48 767 C ATOM 1130 OH TYR A 236 1.780 0.355 29.511 1.00 13.68 O ANISOU 1130 OH TYR A 236 1443 2523 1231 -377 -35 732 O ATOM 1131 N MET A 237 6.650 3.449 23.240 1.00 14.51 N ANISOU 1131 N MET A 237 1503 2478 1533 -322 140 400 N ATOM 1132 CA MET A 237 7.489 4.008 22.180 1.00 14.32 C ANISOU 1132 CA MET A 237 1353 2628 1461 -409 100 210 C ATOM 1133 C MET A 237 7.566 3.169 20.904 1.00 14.70 C ANISOU 1133 C MET A 237 1373 2888 1325 -219 -120 90 C ATOM 1134 O MET A 237 8.392 3.442 20.038 1.00 13.89 O ANISOU 1134 O MET A 237 1116 2842 1320 -383 -81 294 O ATOM 1135 CB MET A 237 8.893 4.291 22.712 1.00 14.47 C ANISOU 1135 CB MET A 237 1258 2536 1704 -817 -204 103 C ATOM 1136 CG MET A 237 8.917 5.280 23.857 1.00 16.19 C ANISOU 1136 CG MET A 237 1693 2463 1995 -676 -133 12 C ATOM 1137 SD MET A 237 8.049 6.826 23.510 1.00 18.10 S ANISOU 1137 SD MET A 237 2195 2284 2396 -645 -168 -141 S ATOM 1138 CE MET A 237 9.022 7.456 22.148 1.00 19.07 C ANISOU 1138 CE MET A 237 2350 2302 2595 -634 -275 -108 C ATOM 1139 N CYS A 238 6.699 2.164 20.803 1.00 15.39 N ANISOU 1139 N CYS A 238 1545 3011 1291 -49 -269 -159 N ATOM 1140 CA CYS A 238 6.488 1.399 19.570 1.00 16.87 C ANISOU 1140 CA CYS A 238 1719 3308 1384 -175 -89 -184 C ATOM 1141 C CYS A 238 4.997 1.135 19.398 1.00 15.34 C ANISOU 1141 C CYS A 238 1589 3103 1136 -414 266 -282 C ATOM 1142 O CYS A 238 4.267 1.010 20.382 1.00 14.95 O ANISOU 1142 O CYS A 238 1789 2917 976 -418 293 -531 O ATOM 1143 CB CYS A 238 7.198 0.045 19.643 1.00 18.98 C ANISOU 1143 CB CYS A 238 1866 3945 1399 -79 110 -281 C ATOM 1144 SG CYS A 238 8.816 -0.065 18.899 1.00 20.34 S ANISOU 1144 SG CYS A 238 2103 4443 1181 149 30 -40 S ATOM 1145 N ASN A 239 4.550 1.037 18.151 1.00 15.98 N ANISOU 1145 N ASN A 239 1714 3244 1115 -409 430 -118 N ATOM 1146 CA ASN A 239 3.189 0.588 17.858 1.00 17.32 C ANISOU 1146 CA ASN A 239 2022 3388 1169 -218 433 101 C ATOM 1147 C ASN A 239 3.066 -0.931 17.958 1.00 16.50 C ANISOU 1147 C ASN A 239 1986 3358 926 -169 195 82 C ATOM 1148 O ASN A 239 4.043 -1.648 17.747 1.00 16.22 O ANISOU 1148 O ASN A 239 1965 3349 850 -108 20 -144 O ATOM 1149 CB ASN A 239 2.743 1.061 16.466 1.00 18.65 C ANISOU 1149 CB ASN A 239 2301 3463 1324 -34 423 211 C ATOM 1150 CG ASN A 239 2.134 2.444 16.488 1.00 20.11 C ANISOU 1150 CG ASN A 239 2532 3708 1402 -38 612 398 C ATOM 1151 ND2 ASN A 239 2.518 3.271 15.525 1.00 19.91 N ANISOU 1151 ND2 ASN A 239 2623 3664 1279 18 643 493 N ATOM 1152 OD1 ASN A 239 1.334 2.773 17.368 1.00 21.69 O ANISOU 1152 OD1 ASN A 239 2701 3893 1646 -40 449 140 O ATOM 1153 N SER A 240 1.869 -1.418 18.271 1.00 16.40 N ANISOU 1153 N SER A 240 2057 3195 978 -268 358 284 N ATOM 1154 CA SER A 240 1.639 -2.859 18.312 1.00 17.03 C ANISOU 1154 CA SER A 240 1904 3401 1163 -335 356 -72 C ATOM 1155 C SER A 240 1.948 -3.480 16.956 1.00 19.13 C ANISOU 1155 C SER A 240 2071 3704 1492 -349 348 -223 C ATOM 1156 O SER A 240 2.350 -4.636 16.876 1.00 20.36 O ANISOU 1156 O SER A 240 2144 3786 1804 -306 298 -247 O ATOM 1157 CB SER A 240 0.202 -3.184 18.727 1.00 16.78 C ANISOU 1157 CB SER A 240 1885 3193 1298 -250 374 -83 C ATOM 1158 OG SER A 240 0.016 -2.991 20.109 1.00 15.83 O ANISOU 1158 OG SER A 240 1808 2881 1324 -155 348 -234 O ATOM 1159 N SER A 241 1.785 -2.686 15.902 1.00 19.42 N ANISOU 1159 N SER A 241 2084 3968 1326 -301 16 -204 N ATOM 1160 CA SER A 241 1.943 -3.153 14.527 1.00 21.75 C ANISOU 1160 CA SER A 241 2491 4314 1458 -184 165 -199 C ATOM 1161 C SER A 241 3.366 -2.994 13.972 1.00 23.25 C ANISOU 1161 C SER A 241 2657 4629 1548 -123 265 -229 C ATOM 1162 O SER A 241 3.595 -3.195 12.776 1.00 24.88 O ANISOU 1162 O SER A 241 3002 4859 1592 -222 384 -214 O ATOM 1163 CB SER A 241 0.965 -2.409 13.623 1.00 23.45 C ANISOU 1163 CB SER A 241 2990 4319 1600 -34 75 -207 C ATOM 1164 OG SER A 241 1.219 -1.020 13.667 1.00 24.68 O ANISOU 1164 OG SER A 241 3201 4462 1716 126 -2 -244 O ATOM 1165 N CYS A 242 4.321 -2.641 14.828 1.00 22.61 N ANISOU 1165 N CYS A 242 2336 4649 1607 33 284 -96 N ATOM 1166 CA CYS A 242 5.695 -2.423 14.365 1.00 22.44 C ANISOU 1166 CA CYS A 242 2220 4686 1619 166 350 24 C ATOM 1167 C CYS A 242 6.360 -3.694 13.836 1.00 24.00 C ANISOU 1167 C CYS A 242 2666 4747 1708 404 577 133 C ATOM 1168 O CYS A 242 6.523 -4.671 14.574 1.00 25.22 O ANISOU 1168 O CYS A 242 3020 4706 1855 383 808 125 O ATOM 1169 CB CYS A 242 6.554 -1.815 15.471 1.00 20.81 C ANISOU 1169 CB CYS A 242 1733 4673 1500 -102 101 200 C ATOM 1170 SG CYS A 242 6.517 -0.023 15.515 1.00 20.62 S ANISOU 1170 SG CYS A 242 1696 4708 1430 -266 15 556 S ATOM 1171 N MET A 243 6.748 -3.669 12.560 1.00 23.55 N ANISOU 1171 N MET A 243 2631 4728 1588 470 390 139 N ATOM 1172 CA MET A 243 7.492 -4.770 11.962 1.00 23.26 C ANISOU 1172 CA MET A 243 2687 4630 1522 478 312 193 C ATOM 1173 C MET A 243 8.851 -4.884 12.645 1.00 23.03 C ANISOU 1173 C MET A 243 2732 4549 1468 664 427 26 C ATOM 1174 O MET A 243 9.571 -3.891 12.781 1.00 23.38 O ANISOU 1174 O MET A 243 2765 4669 1450 730 419 51 O ATOM 1175 CB MET A 243 7.690 -4.537 10.463 1.00 24.59 C ANISOU 1175 CB MET A 243 2910 4686 1748 294 143 513 C ATOM 1176 CG MET A 243 6.412 -4.219 9.699 1.00 26.32 C ANISOU 1176 CG MET A 243 3279 4759 1964 -5 30 686 C ATOM 1177 SD MET A 243 6.714 -4.064 7.928 1.00 28.25 S ANISOU 1177 SD MET A 243 3620 4841 2272 77 -184 795 S ATOM 1178 CE MET A 243 7.242 -5.731 7.532 1.00 29.01 C ANISOU 1178 CE MET A 243 3752 4934 2338 103 -188 913 C ATOM 1179 N GLY A 244 9.195 -6.090 13.088 1.00 22.84 N ANISOU 1179 N GLY A 244 2846 4259 1574 887 517 -276 N ATOM 1180 CA GLY A 244 10.476 -6.317 13.734 1.00 23.64 C ANISOU 1180 CA GLY A 244 3148 4055 1779 711 434 -449 C ATOM 1181 C GLY A 244 10.466 -6.052 15.230 1.00 24.74 C ANISOU 1181 C GLY A 244 3353 4022 2026 408 404 -347 C ATOM 1182 O GLY A 244 11.454 -6.301 15.922 1.00 25.88 O ANISOU 1182 O GLY A 244 3670 4006 2156 373 135 -447 O ATOM 1183 N GLY A 245 9.353 -5.531 15.735 1.00 24.20 N ANISOU 1183 N GLY A 245 3179 4011 2004 60 788 -403 N ATOM 1184 CA GLY A 245 9.211 -5.312 17.161 1.00 24.72 C ANISOU 1184 CA GLY A 245 3192 4032 2167 -29 885 -570 C ATOM 1185 C GLY A 245 8.151 -6.231 17.737 1.00 24.69 C ANISOU 1185 C GLY A 245 3280 3969 2132 248 993 -738 C ATOM 1186 O GLY A 245 8.265 -7.457 17.649 1.00 24.64 O ANISOU 1186 O GLY A 245 3327 3799 2237 583 1082 -964 O ATOM 1187 N MET A 246 7.110 -5.642 18.318 1.00 23.19 N ANISOU 1187 N MET A 246 3136 3877 1798 184 800 -969 N ATOM 1188 CA MET A 246 5.987 -6.429 18.817 1.00 22.10 C ANISOU 1188 CA MET A 246 2919 3838 1640 -14 537 -1064 C ATOM 1189 C MET A 246 5.324 -7.231 17.701 1.00 23.79 C ANISOU 1189 C MET A 246 3281 3931 1827 -190 339 -1278 C ATOM 1190 O MET A 246 4.744 -8.286 17.953 1.00 24.15 O ANISOU 1190 O MET A 246 3391 3929 1857 -118 214 -1341 O ATOM 1191 CB MET A 246 4.978 -5.541 19.543 1.00 20.89 C ANISOU 1191 CB MET A 246 2568 3791 1580 -142 318 -943 C ATOM 1192 CG MET A 246 5.485 -5.070 20.893 1.00 19.76 C ANISOU 1192 CG MET A 246 2403 3824 1279 -228 296 -663 C ATOM 1193 SD MET A 246 4.397 -3.912 21.727 1.00 19.50 S ANISOU 1193 SD MET A 246 2324 3866 1221 -116 125 -390 S ATOM 1194 CE MET A 246 4.720 -2.402 20.814 1.00 20.71 C ANISOU 1194 CE MET A 246 2628 3901 1341 -58 106 -188 C ATOM 1195 N ASN A 247 5.418 -6.723 16.474 1.00 25.14 N ANISOU 1195 N ASN A 247 3686 4019 1846 -295 5 -1360 N ATOM 1196 CA ASN A 247 5.071 -7.500 15.285 1.00 27.16 C ANISOU 1196 CA ASN A 247 4383 4134 1802 -171 -137 -1287 C ATOM 1197 C ASN A 247 3.630 -8.010 15.336 1.00 26.34 C ANISOU 1197 C ASN A 247 4336 3968 1704 -240 -316 -1205 C ATOM 1198 O ASN A 247 3.364 -9.172 15.022 1.00 26.81 O ANISOU 1198 O ASN A 247 4433 3954 1799 -358 -282 -1247 O ATOM 1199 CB ASN A 247 6.055 -8.667 15.136 1.00 30.40 C ANISOU 1199 CB ASN A 247 5123 4359 2069 236 -114 -1360 C ATOM 1200 CG ASN A 247 6.012 -9.307 13.765 1.00 34.51 C ANISOU 1200 CG ASN A 247 5886 4629 2597 702 -45 -1367 C ATOM 1201 ND2 ASN A 247 6.529 -10.529 13.669 1.00 35.21 N ANISOU 1201 ND2 ASN A 247 5945 4541 2892 913 124 -1425 N ATOM 1202 OD1 ASN A 247 5.525 -8.714 12.802 1.00 36.10 O ANISOU 1202 OD1 ASN A 247 6273 4856 2587 906 -186 -1405 O ATOM 1203 N ARG A 248 2.724 -7.129 15.761 1.00 25.64 N ANISOU 1203 N ARG A 248 4202 3836 1704 -119 -364 -1178 N ATOM 1204 CA ARG A 248 1.290 -7.418 15.893 1.00 27.29 C ANISOU 1204 CA ARG A 248 4294 4064 2012 -49 -330 -1069 C ATOM 1205 C ARG A 248 0.927 -8.307 17.104 1.00 26.37 C ANISOU 1205 C ARG A 248 3937 3962 2119 71 -537 -946 C ATOM 1206 O ARG A 248 -0.226 -8.695 17.271 1.00 26.71 O ANISOU 1206 O ARG A 248 3819 4032 2299 -20 -497 -831 O ATOM 1207 CB ARG A 248 0.707 -7.958 14.575 1.00 30.18 C ANISOU 1207 CB ARG A 248 4729 4392 2345 -73 -97 -1145 C ATOM 1208 CG ARG A 248 0.939 -7.028 13.385 1.00 33.70 C ANISOU 1208 CG ARG A 248 5304 4703 2797 47 -6 -1073 C ATOM 1209 CD ARG A 248 0.741 -7.731 12.039 1.00 37.74 C ANISOU 1209 CD ARG A 248 5782 5168 3390 147 56 -789 C ATOM 1210 NE ARG A 248 1.588 -8.917 11.899 1.00 40.64 N ANISOU 1210 NE ARG A 248 6087 5526 3827 274 276 -588 N ATOM 1211 CZ ARG A 248 2.871 -8.891 11.545 1.00 42.34 C ANISOU 1211 CZ ARG A 248 6219 5725 4144 207 278 -440 C ATOM 1212 NH1 ARG A 248 3.471 -7.736 11.294 1.00 43.12 N1+ ANISOU 1212 NH1 ARG A 248 6299 5825 4261 -6 218 -399 N1+ ATOM 1213 NH2 ARG A 248 3.558 -10.023 11.446 1.00 42.45 N ANISOU 1213 NH2 ARG A 248 6158 5722 4249 368 304 -459 N ATOM 1214 N ARG A 249 1.904 -8.604 17.958 1.00 24.55 N ANISOU 1214 N ARG A 249 3725 3747 1855 223 -517 -1068 N ATOM 1215 CA ARG A 249 1.652 -9.433 19.137 1.00 22.90 C ANISOU 1215 CA ARG A 249 3360 3510 1830 244 -434 -998 C ATOM 1216 C ARG A 249 1.181 -8.594 20.325 1.00 21.61 C ANISOU 1216 C ARG A 249 2925 3443 1842 112 -392 -820 C ATOM 1217 O ARG A 249 1.793 -7.577 20.651 1.00 22.06 O ANISOU 1217 O ARG A 249 2919 3680 1784 17 -371 -801 O ATOM 1218 CB ARG A 249 2.908 -10.220 19.522 1.00 22.11 C ANISOU 1218 CB ARG A 249 3231 3386 1784 305 -461 -922 C ATOM 1219 CG ARG A 249 3.375 -11.198 18.458 1.00 22.22 C ANISOU 1219 CG ARG A 249 3233 3358 1851 323 -298 -933 C ATOM 1220 CD ARG A 249 4.749 -11.752 18.774 1.00 21.99 C ANISOU 1220 CD ARG A 249 3301 3301 1752 110 -246 -1054 C ATOM 1221 NE ARG A 249 5.790 -10.728 18.718 1.00 21.66 N ANISOU 1221 NE ARG A 249 3485 3104 1640 -34 -109 -1216 N ATOM 1222 CZ ARG A 249 7.080 -10.959 18.942 1.00 21.48 C ANISOU 1222 CZ ARG A 249 3468 2976 1715 -18 56 -1256 C ATOM 1223 NH1 ARG A 249 7.492 -12.181 19.238 1.00 20.96 N1+ ANISOU 1223 NH1 ARG A 249 3456 2776 1732 157 158 -1228 N1+ ATOM 1224 NH2 ARG A 249 7.957 -9.968 18.870 1.00 21.74 N ANISOU 1224 NH2 ARG A 249 3370 3073 1819 -184 137 -1308 N ATOM 1225 N PRO A 250 0.082 -9.017 20.973 1.00 20.31 N ANISOU 1225 N PRO A 250 2553 3217 1944 -90 -352 -758 N ATOM 1226 CA PRO A 250 -0.428 -8.338 22.173 1.00 19.54 C ANISOU 1226 CA PRO A 250 2309 3058 2056 -321 -220 -805 C ATOM 1227 C PRO A 250 0.552 -8.438 23.342 1.00 18.14 C ANISOU 1227 C PRO A 250 2125 2773 1996 -444 -209 -642 C ATOM 1228 O PRO A 250 1.229 -9.458 23.489 1.00 18.29 O ANISOU 1228 O PRO A 250 2138 2858 1953 -700 -364 -375 O ATOM 1229 CB PRO A 250 -1.710 -9.119 22.503 1.00 19.88 C ANISOU 1229 CB PRO A 250 2351 2985 2216 -357 -29 -914 C ATOM 1230 CG PRO A 250 -1.562 -10.438 21.790 1.00 20.79 C ANISOU 1230 CG PRO A 250 2526 3090 2284 -303 -35 -843 C ATOM 1231 CD PRO A 250 -0.804 -10.113 20.543 1.00 20.54 C ANISOU 1231 CD PRO A 250 2617 3117 2070 -226 -223 -817 C ATOM 1232 N ILE A 251 0.621 -7.385 24.154 1.00 16.85 N ANISOU 1232 N ILE A 251 1962 2516 1924 -292 -211 -704 N ATOM 1233 CA ILE A 251 1.480 -7.357 25.331 1.00 15.43 C ANISOU 1233 CA ILE A 251 1852 2179 1833 67 -99 -672 C ATOM 1234 C ILE A 251 0.675 -7.000 26.580 1.00 14.97 C ANISOU 1234 C ILE A 251 1864 2149 1676 -98 -141 -512 C ATOM 1235 O ILE A 251 -0.421 -6.439 26.486 1.00 14.38 O ANISOU 1235 O ILE A 251 1855 2173 1437 -394 -214 -472 O ATOM 1236 CB ILE A 251 2.621 -6.323 25.189 1.00 15.18 C ANISOU 1236 CB ILE A 251 1814 1851 2103 443 98 -628 C ATOM 1237 CG1 ILE A 251 2.054 -4.916 24.982 1.00 15.10 C ANISOU 1237 CG1 ILE A 251 1801 1670 2267 379 29 -519 C ATOM 1238 CG2 ILE A 251 3.578 -6.699 24.056 1.00 14.92 C ANISOU 1238 CG2 ILE A 251 1824 1774 2071 553 280 -642 C ATOM 1239 CD1 ILE A 251 3.027 -3.798 25.305 1.00 14.80 C ANISOU 1239 CD1 ILE A 251 1797 1546 2281 353 158 -370 C ATOM 1240 N LEU A 252 1.235 -7.326 27.743 1.00 15.03 N ANISOU 1240 N LEU A 252 1762 2195 1754 -111 -318 -476 N ATOM 1241 CA LEU A 252 0.714 -6.864 29.025 1.00 15.46 C ANISOU 1241 CA LEU A 252 1871 2078 1924 89 -197 -372 C ATOM 1242 C LEU A 252 1.748 -5.943 29.638 1.00 14.20 C ANISOU 1242 C LEU A 252 1772 1955 1668 339 -315 -429 C ATOM 1243 O LEU A 252 2.949 -6.135 29.441 1.00 14.73 O ANISOU 1243 O LEU A 252 1817 1932 1848 496 -599 -558 O ATOM 1244 CB LEU A 252 0.506 -8.025 29.992 1.00 17.64 C ANISOU 1244 CB LEU A 252 2089 2354 2260 127 164 -77 C ATOM 1245 CG LEU A 252 -0.198 -9.294 29.535 1.00 21.36 C ANISOU 1245 CG LEU A 252 2555 2748 2814 303 295 524 C ATOM 1246 CD1 LEU A 252 -0.237 -10.280 30.687 1.00 23.26 C ANISOU 1246 CD1 LEU A 252 2901 2897 3039 438 353 669 C ATOM 1247 CD2 LEU A 252 -1.602 -8.990 29.033 1.00 22.67 C ANISOU 1247 CD2 LEU A 252 2586 2949 3079 328 286 594 C ATOM 1248 N THR A 253 1.287 -4.947 30.384 1.00 12.32 N ANISOU 1248 N THR A 253 1576 1809 1297 521 0 -333 N ATOM 1249 CA THR A 253 2.176 -4.176 31.239 1.00 12.81 C ANISOU 1249 CA THR A 253 1631 1934 1304 458 -143 -116 C ATOM 1250 C THR A 253 1.930 -4.649 32.662 1.00 13.83 C ANISOU 1250 C THR A 253 1642 2147 1466 291 -26 12 C ATOM 1251 O THR A 253 0.780 -4.694 33.108 1.00 14.19 O ANISOU 1251 O THR A 253 1905 2133 1352 113 23 212 O ATOM 1252 CB THR A 253 1.894 -2.669 31.131 1.00 13.26 C ANISOU 1252 CB THR A 253 1823 1897 1320 387 -314 65 C ATOM 1253 CG2 THR A 253 2.749 -1.876 32.117 1.00 13.02 C ANISOU 1253 CG2 THR A 253 1877 1982 1088 310 -447 202 C ATOM 1254 OG1 THR A 253 2.168 -2.227 29.794 1.00 15.13 O ANISOU 1254 OG1 THR A 253 2089 2167 1491 481 -255 -31 O ATOM 1255 N ILE A 254 3.001 -5.024 33.362 1.00 12.47 N ANISOU 1255 N ILE A 254 1338 2023 1376 199 42 -33 N ATOM 1256 CA ILE A 254 2.918 -5.409 34.768 1.00 11.70 C ANISOU 1256 CA ILE A 254 1509 1705 1232 66 -18 -58 C ATOM 1257 C ILE A 254 3.474 -4.278 35.632 1.00 11.48 C ANISOU 1257 C ILE A 254 1474 1742 1144 -100 109 -64 C ATOM 1258 O ILE A 254 4.619 -3.848 35.445 1.00 10.63 O ANISOU 1258 O ILE A 254 1359 1761 918 3 144 -102 O ATOM 1259 CB ILE A 254 3.705 -6.707 35.055 1.00 13.08 C ANISOU 1259 CB ILE A 254 1815 1865 1289 -207 -26 -71 C ATOM 1260 CG1 ILE A 254 3.192 -7.854 34.181 1.00 14.39 C ANISOU 1260 CG1 ILE A 254 2273 1944 1251 63 111 -75 C ATOM 1261 CG2 ILE A 254 3.599 -7.091 36.528 1.00 12.29 C ANISOU 1261 CG2 ILE A 254 1603 1811 1257 -204 -247 -134 C ATOM 1262 CD1 ILE A 254 4.107 -9.068 34.156 1.00 15.19 C ANISOU 1262 CD1 ILE A 254 2576 1955 1239 93 31 -102 C ATOM 1263 N ILE A 255 2.657 -3.793 36.567 1.00 10.75 N ANISOU 1263 N ILE A 255 1408 1640 1038 -263 249 -41 N ATOM 1264 CA ILE A 255 3.085 -2.763 37.512 1.00 10.92 C ANISOU 1264 CA ILE A 255 1575 1608 967 -317 17 200 C ATOM 1265 C ILE A 255 3.290 -3.403 38.881 1.00 11.75 C ANISOU 1265 C ILE A 255 1707 1684 1073 -553 247 319 C ATOM 1266 O ILE A 255 2.347 -3.919 39.483 1.00 12.12 O ANISOU 1266 O ILE A 255 1951 1559 1096 -601 269 437 O ATOM 1267 CB ILE A 255 2.056 -1.617 37.651 1.00 11.45 C ANISOU 1267 CB ILE A 255 2027 1370 955 -514 -187 323 C ATOM 1268 CG1 ILE A 255 1.589 -1.109 36.280 1.00 14.66 C ANISOU 1268 CG1 ILE A 255 2472 1785 1312 -802 -116 308 C ATOM 1269 CG2 ILE A 255 2.619 -0.484 38.515 1.00 8.76 C ANISOU 1269 CG2 ILE A 255 1727 921 681 -398 -162 283 C ATOM 1270 CD1 ILE A 255 2.609 -0.268 35.529 1.00 16.40 C ANISOU 1270 CD1 ILE A 255 2576 2083 1572 -1021 -443 207 C ATOM 1271 N THR A 256 4.527 -3.373 39.370 1.00 12.11 N ANISOU 1271 N THR A 256 1650 1809 1141 -642 349 383 N ATOM 1272 CA THR A 256 4.821 -3.885 40.704 1.00 13.80 C ANISOU 1272 CA THR A 256 1999 1829 1416 -464 204 174 C ATOM 1273 C THR A 256 5.130 -2.741 41.661 1.00 15.03 C ANISOU 1273 C THR A 256 2230 2045 1437 -337 118 242 C ATOM 1274 O THR A 256 5.795 -1.767 41.294 1.00 16.11 O ANISOU 1274 O THR A 256 2688 2138 1294 -653 193 156 O ATOM 1275 CB THR A 256 5.988 -4.889 40.705 1.00 15.05 C ANISOU 1275 CB THR A 256 2146 1704 1868 -448 273 -47 C ATOM 1276 CG2 THR A 256 5.587 -6.188 40.038 1.00 15.29 C ANISOU 1276 CG2 THR A 256 2148 1620 2041 -422 243 -280 C ATOM 1277 OG1 THR A 256 7.101 -4.332 40.003 1.00 16.48 O ANISOU 1277 OG1 THR A 256 2449 1773 2041 -507 356 -43 O ATOM 1278 N LEU A 257 4.620 -2.863 42.879 1.00 14.83 N ANISOU 1278 N LEU A 257 2133 2191 1310 155 -227 190 N ATOM 1279 CA LEU A 257 4.956 -1.964 43.963 1.00 14.17 C ANISOU 1279 CA LEU A 257 1809 2261 1313 332 -240 29 C ATOM 1280 C LEU A 257 6.045 -2.670 44.769 1.00 14.85 C ANISOU 1280 C LEU A 257 1641 2559 1441 279 -38 -124 C ATOM 1281 O LEU A 257 5.913 -3.846 45.113 1.00 15.49 O ANISOU 1281 O LEU A 257 1687 2713 1486 506 -266 -380 O ATOM 1282 CB LEU A 257 3.719 -1.716 44.826 1.00 13.87 C ANISOU 1282 CB LEU A 257 1713 2208 1349 446 -85 150 C ATOM 1283 CG LEU A 257 3.782 -0.598 45.867 1.00 14.62 C ANISOU 1283 CG LEU A 257 1884 2275 1397 199 304 160 C ATOM 1284 CD1 LEU A 257 3.908 0.748 45.183 1.00 14.30 C ANISOU 1284 CD1 LEU A 257 1896 2160 1378 276 518 399 C ATOM 1285 CD2 LEU A 257 2.555 -0.615 46.769 1.00 15.00 C ANISOU 1285 CD2 LEU A 257 1851 2374 1476 -208 476 242 C ATOM 1286 N GLU A 258 7.137 -1.973 45.050 1.00 15.85 N ANISOU 1286 N GLU A 258 1761 2830 1431 361 -39 -76 N ATOM 1287 CA GLU A 258 8.238 -2.601 45.767 1.00 16.41 C ANISOU 1287 CA GLU A 258 1637 3081 1518 146 58 171 C ATOM 1288 C GLU A 258 8.813 -1.680 46.835 1.00 17.52 C ANISOU 1288 C GLU A 258 1804 3334 1519 -49 165 292 C ATOM 1289 O GLU A 258 8.687 -0.455 46.739 1.00 19.28 O ANISOU 1289 O GLU A 258 2044 3716 1565 -234 83 257 O ATOM 1290 CB GLU A 258 9.323 -3.061 44.789 1.00 17.23 C ANISOU 1290 CB GLU A 258 1853 3185 1509 20 131 453 C ATOM 1291 CG GLU A 258 9.879 -1.960 43.917 1.00 18.27 C ANISOU 1291 CG GLU A 258 1915 3292 1736 207 361 509 C ATOM 1292 CD GLU A 258 10.949 -2.446 42.964 1.00 19.47 C ANISOU 1292 CD GLU A 258 2210 3359 1830 545 579 362 C ATOM 1293 OE1 GLU A 258 10.638 -3.286 42.095 1.00 20.19 O ANISOU 1293 OE1 GLU A 258 2340 3372 1961 794 624 299 O ATOM 1294 OE2 GLU A 258 12.105 -1.990 43.087 1.00 19.78 O1- ANISOU 1294 OE2 GLU A 258 2247 3433 1834 477 1048 357 O1- ATOM 1295 N ASP A 259 9.431 -2.262 47.859 1.00 16.73 N ANISOU 1295 N ASP A 259 1636 3309 1410 -242 172 423 N ATOM 1296 CA ASP A 259 10.028 -1.444 48.912 1.00 17.83 C ANISOU 1296 CA ASP A 259 1879 3298 1596 -185 -124 378 C ATOM 1297 C ASP A 259 11.401 -0.934 48.482 1.00 18.15 C ANISOU 1297 C ASP A 259 1997 3392 1507 -23 -219 135 C ATOM 1298 O ASP A 259 11.852 -1.234 47.376 1.00 17.16 O ANISOU 1298 O ASP A 259 2027 3362 1131 59 -328 -467 O ATOM 1299 CB ASP A 259 10.074 -2.180 50.266 1.00 18.25 C ANISOU 1299 CB ASP A 259 1996 3161 1778 -119 -428 309 C ATOM 1300 CG ASP A 259 11.057 -3.346 50.292 1.00 19.28 C ANISOU 1300 CG ASP A 259 2308 2993 2025 -160 -469 91 C ATOM 1301 OD1 ASP A 259 11.846 -3.529 49.345 1.00 18.42 O ANISOU 1301 OD1 ASP A 259 1978 2899 2121 -1 -478 -18 O ATOM 1302 OD2 ASP A 259 11.051 -4.082 51.300 1.00 20.80 O1- ANISOU 1302 OD2 ASP A 259 2611 3021 2270 -359 -314 95 O1- ATOM 1303 N SER A 260 12.065 -0.173 49.346 1.00 19.17 N ANISOU 1303 N SER A 260 2094 3512 1677 178 -306 248 N ATOM 1304 CA SER A 260 13.360 0.410 48.999 1.00 20.52 C ANISOU 1304 CA SER A 260 2063 3558 2174 335 -234 220 C ATOM 1305 C SER A 260 14.431 -0.644 48.695 1.00 21.36 C ANISOU 1305 C SER A 260 1969 3613 2533 408 32 11 C ATOM 1306 O SER A 260 15.432 -0.341 48.041 1.00 22.45 O ANISOU 1306 O SER A 260 1979 3661 2891 433 254 -276 O ATOM 1307 CB SER A 260 13.845 1.358 50.100 1.00 20.90 C ANISOU 1307 CB SER A 260 2116 3645 2181 497 -375 398 C ATOM 1308 OG SER A 260 14.022 0.676 51.327 1.00 21.47 O ANISOU 1308 OG SER A 260 2036 3800 2323 494 -275 528 O ATOM 1309 N SER A 261 14.215 -1.871 49.167 1.00 20.60 N ANISOU 1309 N SER A 261 1890 3479 2457 451 -93 207 N ATOM 1310 CA SER A 261 15.138 -2.979 48.913 1.00 20.86 C ANISOU 1310 CA SER A 261 1914 3532 2478 479 3 273 C ATOM 1311 C SER A 261 14.703 -3.831 47.722 1.00 20.07 C ANISOU 1311 C SER A 261 1783 3480 2363 497 290 341 C ATOM 1312 O SER A 261 15.356 -4.817 47.386 1.00 20.16 O ANISOU 1312 O SER A 261 1774 3393 2493 705 248 265 O ATOM 1313 CB SER A 261 15.265 -3.869 50.149 1.00 22.38 C ANISOU 1313 CB SER A 261 2122 3694 2688 636 -54 229 C ATOM 1314 OG SER A 261 15.908 -3.190 51.209 1.00 24.27 O ANISOU 1314 OG SER A 261 2381 3935 2906 622 -3 340 O ATOM 1315 N GLY A 262 13.589 -3.461 47.099 1.00 19.50 N ANISOU 1315 N GLY A 262 1718 3399 2293 291 209 462 N ATOM 1316 CA GLY A 262 13.115 -4.176 45.929 1.00 19.87 C ANISOU 1316 CA GLY A 262 1839 3283 2427 244 243 390 C ATOM 1317 C GLY A 262 12.187 -5.335 46.249 1.00 20.80 C ANISOU 1317 C GLY A 262 2154 3189 2560 352 10 363 C ATOM 1318 O GLY A 262 11.789 -6.076 45.349 1.00 22.15 O ANISOU 1318 O GLY A 262 2475 3244 2698 481 142 236 O ATOM 1319 N ASN A 263 11.839 -5.498 47.523 1.00 19.79 N ANISOU 1319 N ASN A 263 2002 3082 2435 177 -140 593 N ATOM 1320 CA ASN A 263 10.887 -6.533 47.923 1.00 20.11 C ANISOU 1320 CA ASN A 263 1971 3139 2532 448 -413 679 C ATOM 1321 C ASN A 263 9.489 -6.248 47.373 1.00 18.73 C ANISOU 1321 C ASN A 263 1687 2945 2485 393 -422 669 C ATOM 1322 O ASN A 263 9.038 -5.105 47.382 1.00 17.61 O ANISOU 1322 O ASN A 263 1244 2982 2467 485 -361 799 O ATOM 1323 CB ASN A 263 10.817 -6.652 49.450 1.00 20.98 C ANISOU 1323 CB ASN A 263 2103 3209 2659 587 -760 693 C ATOM 1324 CG ASN A 263 12.143 -7.059 50.076 1.00 21.85 C ANISOU 1324 CG ASN A 263 2154 3274 2875 761 -696 616 C ATOM 1325 ND2 ASN A 263 12.552 -6.332 51.108 1.00 21.70 N ANISOU 1325 ND2 ASN A 263 2183 3336 2725 771 -670 749 N ATOM 1326 OD1 ASN A 263 12.790 -8.013 49.639 1.00 22.62 O ANISOU 1326 OD1 ASN A 263 2254 3224 3116 945 -769 583 O ATOM 1327 N LEU A 264 8.800 -7.292 46.918 1.00 18.24 N ANISOU 1327 N LEU A 264 1884 2662 2386 295 -362 482 N ATOM 1328 CA LEU A 264 7.451 -7.148 46.360 1.00 18.35 C ANISOU 1328 CA LEU A 264 2352 2340 2281 142 -318 306 C ATOM 1329 C LEU A 264 6.424 -6.715 47.406 1.00 17.43 C ANISOU 1329 C LEU A 264 2253 2243 2127 -103 -208 386 C ATOM 1330 O LEU A 264 6.323 -7.326 48.467 1.00 19.62 O ANISOU 1330 O LEU A 264 2571 2646 2239 -55 -162 174 O ATOM 1331 CB LEU A 264 7.005 -8.468 45.731 1.00 19.25 C ANISOU 1331 CB LEU A 264 2779 2060 2473 192 -213 180 C ATOM 1332 CG LEU A 264 5.599 -8.523 45.144 1.00 20.38 C ANISOU 1332 CG LEU A 264 3078 1982 2685 155 142 57 C ATOM 1333 CD1 LEU A 264 5.520 -7.710 43.858 1.00 20.59 C ANISOU 1333 CD1 LEU A 264 3270 1883 2669 345 100 -58 C ATOM 1334 CD2 LEU A 264 5.201 -9.963 44.889 1.00 21.73 C ANISOU 1334 CD2 LEU A 264 3192 2204 2859 -11 334 161 C ATOM 1335 N LEU A 265 5.661 -5.669 47.095 1.00 15.14 N ANISOU 1335 N LEU A 265 1970 1835 1950 -119 -223 585 N ATOM 1336 CA LEU A 265 4.608 -5.169 47.985 1.00 13.63 C ANISOU 1336 CA LEU A 265 1854 1680 1644 -247 -143 552 C ATOM 1337 C LEU A 265 3.221 -5.282 47.352 1.00 14.33 C ANISOU 1337 C LEU A 265 2039 1784 1624 -151 17 625 C ATOM 1338 O LEU A 265 2.212 -5.308 48.055 1.00 15.06 O ANISOU 1338 O LEU A 265 2116 2027 1579 -225 155 587 O ATOM 1339 CB LEU A 265 4.853 -3.705 48.349 1.00 12.79 C ANISOU 1339 CB LEU A 265 1809 1613 1439 -220 -184 431 C ATOM 1340 CG LEU A 265 6.087 -3.297 49.144 1.00 11.90 C ANISOU 1340 CG LEU A 265 1845 1364 1313 -449 -276 395 C ATOM 1341 CD1 LEU A 265 6.080 -1.777 49.334 1.00 10.93 C ANISOU 1341 CD1 LEU A 265 1715 1127 1312 -513 -113 563 C ATOM 1342 CD2 LEU A 265 6.136 -4.011 50.483 1.00 13.04 C ANISOU 1342 CD2 LEU A 265 2073 1404 1480 -283 -60 464 C ATOM 1343 N GLY A 266 3.179 -5.317 46.022 1.00 13.04 N ANISOU 1343 N GLY A 266 1876 1622 1457 -157 -47 675 N ATOM 1344 CA GLY A 266 1.930 -5.386 45.285 1.00 12.20 C ANISOU 1344 CA GLY A 266 1557 1619 1458 -151 -180 759 C ATOM 1345 C GLY A 266 2.188 -5.598 43.805 1.00 12.44 C ANISOU 1345 C GLY A 266 1550 1666 1511 -297 -283 920 C ATOM 1346 O GLY A 266 3.288 -5.328 43.328 1.00 13.12 O ANISOU 1346 O GLY A 266 1580 1814 1591 -409 -228 971 O ATOM 1347 N ARG A 267 1.186 -6.101 43.086 1.00 13.22 N ANISOU 1347 N ARG A 267 1742 1806 1474 15 -392 860 N ATOM 1348 CA ARG A 267 1.282 -6.279 41.638 1.00 12.59 C ANISOU 1348 CA ARG A 267 1558 1802 1423 -150 -462 696 C ATOM 1349 C ARG A 267 -0.086 -6.154 40.971 1.00 13.44 C ANISOU 1349 C ARG A 267 1784 1933 1390 -537 -473 609 C ATOM 1350 O ARG A 267 -1.090 -6.657 41.486 1.00 13.77 O ANISOU 1350 O ARG A 267 1769 2013 1449 -929 -393 673 O ATOM 1351 CB ARG A 267 1.890 -7.636 41.283 1.00 12.81 C ANISOU 1351 CB ARG A 267 1633 1629 1606 53 -422 557 C ATOM 1352 CG ARG A 267 2.091 -7.835 39.777 1.00 14.10 C ANISOU 1352 CG ARG A 267 2165 1418 1774 345 -285 521 C ATOM 1353 CD ARG A 267 2.538 -9.251 39.417 1.00 15.59 C ANISOU 1353 CD ARG A 267 2512 1481 1929 419 -140 250 C ATOM 1354 NE ARG A 267 3.774 -9.648 40.089 1.00 16.35 N ANISOU 1354 NE ARG A 267 2684 1421 2106 475 -18 94 N ATOM 1355 CZ ARG A 267 3.844 -10.485 41.123 1.00 17.38 C ANISOU 1355 CZ ARG A 267 2977 1383 2245 541 -193 64 C ATOM 1356 NH1 ARG A 267 2.743 -11.025 41.627 1.00 17.48 N1+ ANISOU 1356 NH1 ARG A 267 3114 1325 2203 335 -196 29 N1+ ATOM 1357 NH2 ARG A 267 5.022 -10.780 41.656 1.00 18.06 N ANISOU 1357 NH2 ARG A 267 3179 1382 2302 716 -419 279 N ATOM 1358 N ASN A 268 -0.114 -5.459 39.837 1.00 12.62 N ANISOU 1358 N ASN A 268 1648 2075 1072 -450 -478 635 N ATOM 1359 CA ASN A 268 -1.282 -5.412 38.972 1.00 14.68 C ANISOU 1359 CA ASN A 268 2060 2392 1125 -504 -212 333 C ATOM 1360 C ASN A 268 -0.820 -5.408 37.525 1.00 14.60 C ANISOU 1360 C ASN A 268 1953 2467 1126 -523 -314 396 C ATOM 1361 O ASN A 268 0.360 -5.165 37.235 1.00 16.33 O ANISOU 1361 O ASN A 268 2271 2814 1120 -581 -171 552 O ATOM 1362 CB ASN A 268 -2.127 -4.168 39.244 1.00 16.86 C ANISOU 1362 CB ASN A 268 2254 2712 1439 -325 -86 236 C ATOM 1363 CG ASN A 268 -2.997 -4.307 40.474 1.00 20.07 C ANISOU 1363 CG ASN A 268 2669 2955 2002 -323 -14 7 C ATOM 1364 ND2 ASN A 268 -2.624 -3.612 41.548 1.00 20.45 N ANISOU 1364 ND2 ASN A 268 2961 2844 1967 -149 39 -131 N ATOM 1365 OD1 ASN A 268 -4.004 -5.021 40.459 1.00 21.23 O ANISOU 1365 OD1 ASN A 268 2537 3191 2341 -364 19 -100 O ATOM 1366 N SER A 269 -1.743 -5.668 36.612 1.00 13.22 N ANISOU 1366 N SER A 269 1741 2110 1171 -360 -502 182 N ATOM 1367 CA SER A 269 -1.397 -5.700 35.200 1.00 12.63 C ANISOU 1367 CA SER A 269 1760 1828 1213 54 -517 78 C ATOM 1368 C SER A 269 -2.581 -5.328 34.311 1.00 11.74 C ANISOU 1368 C SER A 269 1579 1601 1279 183 -284 113 C ATOM 1369 O SER A 269 -3.732 -5.386 34.732 1.00 12.50 O ANISOU 1369 O SER A 269 1544 1774 1431 369 -322 268 O ATOM 1370 CB SER A 269 -0.859 -7.074 34.817 1.00 13.12 C ANISOU 1370 CB SER A 269 2005 1681 1300 146 -411 -102 C ATOM 1371 OG SER A 269 -1.827 -8.075 35.045 1.00 14.48 O ANISOU 1371 OG SER A 269 2491 1602 1407 336 -234 -257 O ATOM 1372 N PHE A 270 -2.274 -4.937 33.081 1.00 10.42 N ANISOU 1372 N PHE A 270 1389 1445 1126 175 -26 -236 N ATOM 1373 CA PHE A 270 -3.283 -4.616 32.083 1.00 9.97 C ANISOU 1373 CA PHE A 270 1501 1228 1057 -71 177 -202 C ATOM 1374 C PHE A 270 -2.714 -4.878 30.687 1.00 11.61 C ANISOU 1374 C PHE A 270 1733 1468 1209 -172 37 -297 C ATOM 1375 O PHE A 270 -1.503 -4.764 30.459 1.00 11.88 O ANISOU 1375 O PHE A 270 1595 1636 1282 -193 161 -485 O ATOM 1376 CB PHE A 270 -3.792 -3.171 32.241 1.00 9.26 C ANISOU 1376 CB PHE A 270 1442 1050 1027 -77 -3 7 C ATOM 1377 CG PHE A 270 -2.713 -2.117 32.142 1.00 9.80 C ANISOU 1377 CG PHE A 270 1476 1070 1178 32 141 0 C ATOM 1378 CD1 PHE A 270 -2.037 -1.691 33.275 1.00 11.04 C ANISOU 1378 CD1 PHE A 270 1652 1186 1355 -78 227 -249 C ATOM 1379 CD2 PHE A 270 -2.391 -1.538 30.914 1.00 9.77 C ANISOU 1379 CD2 PHE A 270 1341 1107 1264 124 292 126 C ATOM 1380 CE1 PHE A 270 -1.050 -0.727 33.189 1.00 11.34 C ANISOU 1380 CE1 PHE A 270 1780 1124 1407 -112 237 -421 C ATOM 1381 CE2 PHE A 270 -1.409 -0.571 30.828 1.00 10.75 C ANISOU 1381 CE2 PHE A 270 1647 1084 1355 37 217 -86 C ATOM 1382 CZ PHE A 270 -0.740 -0.163 31.968 1.00 11.04 C ANISOU 1382 CZ PHE A 270 1566 1238 1390 -161 340 -234 C ATOM 1383 N GLU A 271 -3.579 -5.270 29.762 1.00 11.90 N ANISOU 1383 N GLU A 271 1700 1539 1284 -27 -316 -177 N ATOM 1384 CA GLU A 271 -3.131 -5.494 28.397 1.00 12.90 C ANISOU 1384 CA GLU A 271 1865 1757 1280 59 -380 -292 C ATOM 1385 C GLU A 271 -2.977 -4.131 27.723 1.00 13.22 C ANISOU 1385 C GLU A 271 1918 1858 1248 -8 -359 -155 C ATOM 1386 O GLU A 271 -3.613 -3.162 28.128 1.00 13.39 O ANISOU 1386 O GLU A 271 1961 2010 1116 -33 -406 -50 O ATOM 1387 CB GLU A 271 -4.124 -6.380 27.644 1.00 14.48 C ANISOU 1387 CB GLU A 271 1965 1913 1623 -20 -430 -460 C ATOM 1388 CG GLU A 271 -3.642 -6.836 26.278 1.00 17.41 C ANISOU 1388 CG GLU A 271 2274 2236 2104 -32 -757 -583 C ATOM 1389 CD GLU A 271 -4.662 -7.700 25.577 1.00 20.53 C ANISOU 1389 CD GLU A 271 2638 2616 2545 -49 -591 -658 C ATOM 1390 OE1 GLU A 271 -5.553 -8.226 26.281 1.00 21.94 O ANISOU 1390 OE1 GLU A 271 2562 2973 2803 -201 -374 -688 O ATOM 1391 OE2 GLU A 271 -4.578 -7.849 24.332 1.00 21.71 O1- ANISOU 1391 OE2 GLU A 271 2960 2679 2610 116 -702 -792 O1- ATOM 1392 N VAL A 272 -2.101 -4.038 26.728 1.00 14.70 N ANISOU 1392 N VAL A 272 2152 1955 1479 6 -263 -40 N ATOM 1393 CA VAL A 272 -1.923 -2.787 25.997 1.00 14.48 C ANISOU 1393 CA VAL A 272 2099 1985 1420 -162 -132 -199 C ATOM 1394 C VAL A 272 -1.908 -3.026 24.492 1.00 14.62 C ANISOU 1394 C VAL A 272 1997 2032 1526 -194 225 -278 C ATOM 1395 O VAL A 272 -1.292 -3.975 24.008 1.00 14.31 O ANISOU 1395 O VAL A 272 2006 1858 1574 -84 656 -440 O ATOM 1396 CB VAL A 272 -0.615 -2.059 26.391 1.00 14.46 C ANISOU 1396 CB VAL A 272 2022 2051 1422 -396 -464 -427 C ATOM 1397 CG1 VAL A 272 -0.570 -0.659 25.782 1.00 14.81 C ANISOU 1397 CG1 VAL A 272 1962 2254 1412 -393 -531 -490 C ATOM 1398 CG2 VAL A 272 -0.485 -1.975 27.882 1.00 14.95 C ANISOU 1398 CG2 VAL A 272 1990 2108 1582 -530 -671 -591 C ATOM 1399 N ARG A 273 -2.612 -2.163 23.769 1.00 12.40 N ANISOU 1399 N ARG A 273 1579 1902 1230 57 -52 -95 N ATOM 1400 CA ARG A 273 -2.477 -2.056 22.328 1.00 13.60 C ANISOU 1400 CA ARG A 273 1674 2145 1349 360 74 -267 C ATOM 1401 C ARG A 273 -2.061 -0.629 22.014 1.00 12.87 C ANISOU 1401 C ARG A 273 1558 2073 1260 451 335 -32 C ATOM 1402 O ARG A 273 -2.763 0.319 22.372 1.00 13.10 O ANISOU 1402 O ARG A 273 1841 1770 1368 512 649 145 O ATOM 1403 CB ARG A 273 -3.805 -2.379 21.641 1.00 15.08 C ANISOU 1403 CB ARG A 273 1962 2405 1365 463 -42 -471 C ATOM 1404 CG ARG A 273 -3.842 -2.088 20.153 1.00 16.54 C ANISOU 1404 CG ARG A 273 2135 2678 1471 551 -15 -386 C ATOM 1405 CD ARG A 273 -5.188 -2.486 19.551 1.00 18.61 C ANISOU 1405 CD ARG A 273 2477 3011 1584 575 -84 -486 C ATOM 1406 NE ARG A 273 -5.294 -2.118 18.143 1.00 22.74 N ANISOU 1406 NE ARG A 273 3075 3460 2104 687 -85 -509 N ATOM 1407 CZ ARG A 273 -4.757 -2.821 17.153 1.00 26.15 C ANISOU 1407 CZ ARG A 273 3593 3780 2562 788 -360 -611 C ATOM 1408 NH1 ARG A 273 -4.070 -3.919 17.430 1.00 28.14 N1+ ANISOU 1408 NH1 ARG A 273 4081 3938 2674 674 -578 -829 N1+ ATOM 1409 NH2 ARG A 273 -4.892 -2.427 15.891 1.00 27.24 N ANISOU 1409 NH2 ARG A 273 3479 4061 2812 738 -329 -526 N ATOM 1410 N VAL A 274 -0.911 -0.467 21.372 1.00 13.18 N ANISOU 1410 N VAL A 274 1403 2398 1205 467 82 -112 N ATOM 1411 CA VAL A 274 -0.481 0.853 20.930 1.00 13.86 C ANISOU 1411 CA VAL A 274 1448 2785 1033 223 1 -66 C ATOM 1412 C VAL A 274 -0.872 0.997 19.457 1.00 14.80 C ANISOU 1412 C VAL A 274 1494 2986 1141 -32 -373 4 C ATOM 1413 O VAL A 274 -0.404 0.243 18.608 1.00 14.01 O ANISOU 1413 O VAL A 274 1434 2930 958 -145 -391 2 O ATOM 1414 CB VAL A 274 1.033 1.068 21.123 1.00 15.31 C ANISOU 1414 CB VAL A 274 1831 2907 1079 210 -157 -297 C ATOM 1415 CG1 VAL A 274 1.386 2.534 20.916 1.00 16.22 C ANISOU 1415 CG1 VAL A 274 2061 2963 1138 366 -332 -473 C ATOM 1416 CG2 VAL A 274 1.459 0.620 22.514 1.00 14.53 C ANISOU 1416 CG2 VAL A 274 1735 2884 902 246 290 -324 C ATOM 1417 N CYS A 275 -1.750 1.955 19.170 1.00 16.65 N ANISOU 1417 N CYS A 275 1662 3215 1451 -76 -385 32 N ATOM 1418 CA CYS A 275 -2.357 2.077 17.843 1.00 17.77 C ANISOU 1418 CA CYS A 275 1773 3488 1491 85 -182 -121 C ATOM 1419 C CYS A 275 -2.660 3.521 17.443 1.00 18.63 C ANISOU 1419 C CYS A 275 1962 3641 1474 173 49 4 C ATOM 1420 O CYS A 275 -2.639 4.431 18.277 1.00 18.80 O ANISOU 1420 O CYS A 275 1959 3679 1505 217 156 125 O ATOM 1421 CB CYS A 275 -3.640 1.236 17.768 1.00 18.52 C ANISOU 1421 CB CYS A 275 1711 3722 1605 142 -195 -258 C ATOM 1422 SG CYS A 275 -4.845 1.570 19.090 1.00 19.87 S ANISOU 1422 SG CYS A 275 1564 4066 1918 393 23 -351 S ATOM 1423 N ALA A 276 -2.967 3.717 16.165 1.00 18.85 N ANISOU 1423 N ALA A 276 2073 3687 1400 438 386 123 N ATOM 1424 CA ALA A 276 -3.265 5.044 15.651 1.00 19.67 C ANISOU 1424 CA ALA A 276 2131 3890 1452 487 337 212 C ATOM 1425 C ALA A 276 -4.619 5.581 16.110 1.00 20.33 C ANISOU 1425 C ALA A 276 2100 4066 1560 135 154 357 C ATOM 1426 O ALA A 276 -4.762 6.782 16.329 1.00 20.75 O ANISOU 1426 O ALA A 276 2268 4074 1541 -5 155 389 O ATOM 1427 CB ALA A 276 -3.188 5.057 14.135 1.00 20.08 C ANISOU 1427 CB ALA A 276 2203 3981 1447 688 361 132 C ATOM 1428 N CYS A 277 -5.614 4.704 16.248 1.00 19.70 N ANISOU 1428 N CYS A 277 1706 4037 1742 -60 -220 456 N ATOM 1429 CA ACYS A 277 -6.962 5.124 16.630 0.58 20.37 C ANISOU 1429 CA ACYS A 277 1791 4097 1851 -129 -390 506 C ATOM 1430 CA BCYS A 277 -6.951 5.145 16.648 0.42 19.97 C ANISOU 1430 CA BCYS A 277 1633 4012 1941 50 -350 462 C ATOM 1431 C CYS A 277 -7.492 4.355 17.834 1.00 18.73 C ANISOU 1431 C CYS A 277 1540 3843 1732 -36 -324 282 C ATOM 1432 O CYS A 277 -8.309 3.453 17.668 1.00 19.96 O ANISOU 1432 O CYS A 277 1726 4142 1716 -103 -388 55 O ATOM 1433 CB ACYS A 277 -7.924 4.920 15.459 0.58 22.18 C ANISOU 1433 CB ACYS A 277 2006 4417 2005 -299 -611 708 C ATOM 1434 CB BCYS A 277 -7.927 5.071 15.472 0.42 21.13 C ANISOU 1434 CB BCYS A 277 1567 4169 2294 235 -502 602 C ATOM 1435 SG ACYS A 277 -7.480 5.799 13.951 0.58 24.38 S ANISOU 1435 SG ACYS A 277 2401 4709 2153 -385 -942 838 S ATOM 1436 SG BCYS A 277 -9.330 6.205 15.626 0.42 22.61 S ANISOU 1436 SG BCYS A 277 1709 4251 2632 452 -733 690 S ATOM 1437 N PRO A 278 -7.030 4.702 19.045 1.00 15.56 N ANISOU 1437 N PRO A 278 1182 3230 1499 96 -392 13 N ATOM 1438 CA PRO A 278 -7.443 4.004 20.270 1.00 15.16 C ANISOU 1438 CA PRO A 278 1194 3046 1521 -133 -314 -60 C ATOM 1439 C PRO A 278 -8.961 3.888 20.454 1.00 15.49 C ANISOU 1439 C PRO A 278 1395 2875 1615 76 -512 -284 C ATOM 1440 O PRO A 278 -9.438 2.821 20.841 1.00 14.45 O ANISOU 1440 O PRO A 278 1560 2404 1528 -24 -375 -279 O ATOM 1441 CB PRO A 278 -6.873 4.887 21.378 1.00 14.57 C ANISOU 1441 CB PRO A 278 1224 2940 1371 -504 -421 -119 C ATOM 1442 CG PRO A 278 -5.667 5.502 20.779 1.00 15.20 C ANISOU 1442 CG PRO A 278 1332 3013 1432 -375 -443 -45 C ATOM 1443 CD PRO A 278 -6.031 5.748 19.323 1.00 14.64 C ANISOU 1443 CD PRO A 278 1295 2980 1286 -23 -539 139 C ATOM 1444 N GLY A 279 -9.700 4.967 20.202 1.00 15.65 N ANISOU 1444 N GLY A 279 1358 3007 1581 364 -640 -427 N ATOM 1445 CA GLY A 279 -11.140 4.955 20.384 1.00 16.28 C ANISOU 1445 CA GLY A 279 1452 3303 1430 502 -499 -555 C ATOM 1446 C GLY A 279 -11.824 3.972 19.452 1.00 16.85 C ANISOU 1446 C GLY A 279 1577 3458 1369 588 -328 -532 C ATOM 1447 O GLY A 279 -12.644 3.159 19.885 1.00 16.44 O ANISOU 1447 O GLY A 279 1594 3398 1254 698 124 -522 O ATOM 1448 N ARG A 280 -11.479 4.050 18.170 1.00 18.21 N ANISOU 1448 N ARG A 280 1983 3678 1259 303 -510 -477 N ATOM 1449 CA ARG A 280 -12.016 3.143 17.159 1.00 20.38 C ANISOU 1449 CA ARG A 280 2552 3936 1254 216 -584 -343 C ATOM 1450 C ARG A 280 -11.687 1.694 17.482 1.00 17.87 C ANISOU 1450 C ARG A 280 2163 3531 1097 116 -466 -309 C ATOM 1451 O ARG A 280 -12.556 0.827 17.442 1.00 16.90 O ANISOU 1451 O ARG A 280 1963 3319 1139 15 -508 -389 O ATOM 1452 CB ARG A 280 -11.447 3.493 15.782 1.00 24.96 C ANISOU 1452 CB ARG A 280 3574 4469 1441 65 -527 -312 C ATOM 1453 CG ARG A 280 -11.977 2.647 14.634 1.00 30.17 C ANISOU 1453 CG ARG A 280 4593 5002 1867 -31 -269 -258 C ATOM 1454 CD ARG A 280 -11.176 2.893 13.355 1.00 35.68 C ANISOU 1454 CD ARG A 280 5475 5521 2562 -41 -161 -313 C ATOM 1455 NE ARG A 280 -9.785 2.467 13.510 1.00 40.21 N ANISOU 1455 NE ARG A 280 6265 5929 3083 69 -182 -328 N ATOM 1456 CZ ARG A 280 -9.335 1.256 13.195 1.00 42.79 C ANISOU 1456 CZ ARG A 280 6688 6211 3360 186 -396 -225 C ATOM 1457 NH1 ARG A 280 -10.166 0.345 12.703 1.00 43.94 N1+ ANISOU 1457 NH1 ARG A 280 6928 6293 3474 219 -415 -157 N1+ ATOM 1458 NH2 ARG A 280 -8.055 0.953 13.371 1.00 43.05 N ANISOU 1458 NH2 ARG A 280 6655 6340 3362 208 -610 -135 N ATOM 1459 N ASP A 281 -10.423 1.437 17.804 1.00 17.42 N ANISOU 1459 N ASP A 281 2208 3445 966 252 -161 -403 N ATOM 1460 CA ASP A 281 -9.980 0.074 18.060 1.00 17.06 C ANISOU 1460 CA ASP A 281 2150 3306 1025 342 -293 -500 C ATOM 1461 C ASP A 281 -10.618 -0.524 19.309 1.00 17.04 C ANISOU 1461 C ASP A 281 2155 2860 1458 -40 -326 -643 C ATOM 1462 O ASP A 281 -10.977 -1.696 19.305 1.00 19.47 O ANISOU 1462 O ASP A 281 2512 3043 1843 -124 -431 -970 O ATOM 1463 CB ASP A 281 -8.451 -0.013 18.108 1.00 18.77 C ANISOU 1463 CB ASP A 281 2217 3735 1181 584 -361 -364 C ATOM 1464 CG ASP A 281 -7.820 0.053 16.724 1.00 20.79 C ANISOU 1464 CG ASP A 281 2257 4053 1588 650 -633 -276 C ATOM 1465 OD1 ASP A 281 -8.573 0.074 15.726 1.00 21.07 O ANISOU 1465 OD1 ASP A 281 2225 4052 1730 944 -672 91 O ATOM 1466 OD2 ASP A 281 -6.573 0.071 16.633 1.00 22.05 O1- ANISOU 1466 OD2 ASP A 281 2337 4211 1832 519 -727 -398 O1- ATOM 1467 N ARG A 282 -10.770 0.278 20.365 1.00 14.51 N ANISOU 1467 N ARG A 282 1847 2533 1132 -22 -208 -446 N ATOM 1468 CA ARG A 282 -11.460 -0.175 21.568 1.00 12.51 C ANISOU 1468 CA ARG A 282 1510 2174 1068 25 68 -628 C ATOM 1469 C ARG A 282 -12.905 -0.535 21.271 1.00 15.05 C ANISOU 1469 C ARG A 282 1787 2566 1367 236 -222 -482 C ATOM 1470 O ARG A 282 -13.371 -1.620 21.628 1.00 15.66 O ANISOU 1470 O ARG A 282 1813 2748 1390 269 -662 -423 O ATOM 1471 CB ARG A 282 -11.421 0.886 22.670 1.00 10.42 C ANISOU 1471 CB ARG A 282 1340 1747 871 -30 414 -466 C ATOM 1472 CG ARG A 282 -12.297 0.514 23.864 1.00 10.64 C ANISOU 1472 CG ARG A 282 1407 1727 908 -162 604 -175 C ATOM 1473 CD ARG A 282 -12.218 1.503 25.022 1.00 11.86 C ANISOU 1473 CD ARG A 282 1546 1866 1094 -298 298 -203 C ATOM 1474 NE ARG A 282 -13.291 1.239 25.981 1.00 11.86 N ANISOU 1474 NE ARG A 282 1548 1981 978 -53 48 -302 N ATOM 1475 CZ ARG A 282 -13.740 2.099 26.889 1.00 11.09 C ANISOU 1475 CZ ARG A 282 1281 1928 1007 193 78 -369 C ATOM 1476 NH1 ARG A 282 -13.200 3.301 26.999 1.00 11.53 N1+ ANISOU 1476 NH1 ARG A 282 1186 1832 1363 392 -207 -521 N1+ ATOM 1477 NH2 ARG A 282 -14.731 1.742 27.692 1.00 11.69 N ANISOU 1477 NH2 ARG A 282 1319 2093 1028 214 322 -231 N ATOM 1478 N ARG A 283 -13.612 0.378 20.615 1.00 15.95 N ANISOU 1478 N ARG A 283 1857 2701 1504 162 -289 -267 N ATOM 1479 CA ARG A 283 -15.024 0.170 20.295 1.00 16.61 C ANISOU 1479 CA ARG A 283 1581 3036 1695 -84 -77 -121 C ATOM 1480 C ARG A 283 -15.195 -1.093 19.454 1.00 18.56 C ANISOU 1480 C ARG A 283 1828 3328 1898 -316 194 -123 C ATOM 1481 O ARG A 283 -16.113 -1.882 19.683 1.00 19.49 O ANISOU 1481 O ARG A 283 2138 3366 1900 -264 330 304 O ATOM 1482 CB ARG A 283 -15.608 1.396 19.569 1.00 16.74 C ANISOU 1482 CB ARG A 283 1456 3184 1722 28 -30 110 C ATOM 1483 CG ARG A 283 -17.138 1.469 19.578 1.00 17.23 C ANISOU 1483 CG ARG A 283 1739 3208 1598 64 -55 165 C ATOM 1484 CD ARG A 283 -17.677 2.660 18.789 1.00 16.22 C ANISOU 1484 CD ARG A 283 1807 3020 1335 17 -377 199 C ATOM 1485 NE ARG A 283 -17.271 3.954 19.343 1.00 15.50 N ANISOU 1485 NE ARG A 283 1837 2934 1117 -159 -610 111 N ATOM 1486 CZ ARG A 283 -17.642 5.133 18.845 1.00 14.79 C ANISOU 1486 CZ ARG A 283 1748 2709 1162 -147 -505 -17 C ATOM 1487 NH1 ARG A 283 -18.431 5.184 17.787 1.00 14.21 N1+ ANISOU 1487 NH1 ARG A 283 1784 2541 1073 -199 -682 23 N1+ ATOM 1488 NH2 ARG A 283 -17.226 6.261 19.404 1.00 15.08 N ANISOU 1488 NH2 ARG A 283 1815 2710 1203 -135 -7 82 N ATOM 1489 N THR A 284 -14.289 -1.295 18.498 1.00 19.56 N ANISOU 1489 N THR A 284 2006 3446 1981 -615 70 -461 N ATOM 1490 CA THR A 284 -14.337 -2.474 17.637 1.00 19.92 C ANISOU 1490 CA THR A 284 2193 3414 1963 -673 71 -784 C ATOM 1491 C THR A 284 -14.079 -3.769 18.413 1.00 20.25 C ANISOU 1491 C THR A 284 2085 3351 2258 -527 -35 -1334 C ATOM 1492 O THR A 284 -14.770 -4.764 18.211 1.00 20.44 O ANISOU 1492 O THR A 284 2205 3179 2383 -532 -135 -1467 O ATOM 1493 CB THR A 284 -13.357 -2.349 16.443 1.00 21.83 C ANISOU 1493 CB THR A 284 2778 3484 2032 -945 -189 -516 C ATOM 1494 CG2 THR A 284 -13.271 -3.649 15.673 1.00 22.16 C ANISOU 1494 CG2 THR A 284 2971 3469 1981 -973 -86 -570 C ATOM 1495 OG1 THR A 284 -13.816 -1.321 15.559 1.00 22.23 O ANISOU 1495 OG1 THR A 284 2956 3518 1972 -1250 -354 -158 O ATOM 1496 N GLU A 285 -13.099 -3.755 19.309 1.00 22.05 N ANISOU 1496 N GLU A 285 2340 3613 2425 -436 -150 -1476 N ATOM 1497 CA GLU A 285 -12.741 -4.966 20.040 1.00 24.58 C ANISOU 1497 CA GLU A 285 2703 3939 2699 -436 -284 -1430 C ATOM 1498 C GLU A 285 -13.829 -5.356 21.026 1.00 27.00 C ANISOU 1498 C GLU A 285 3030 4100 3129 -378 -745 -1312 C ATOM 1499 O GLU A 285 -14.027 -6.533 21.311 1.00 29.71 O ANISOU 1499 O GLU A 285 3548 4239 3502 -344 -733 -1214 O ATOM 1500 CB GLU A 285 -11.391 -4.810 20.750 1.00 25.66 C ANISOU 1500 CB GLU A 285 2807 4220 2724 -283 -267 -1664 C ATOM 1501 CG GLU A 285 -10.203 -4.720 19.802 1.00 28.06 C ANISOU 1501 CG GLU A 285 3100 4565 2997 13 -405 -1808 C ATOM 1502 CD GLU A 285 -8.873 -5.034 20.468 1.00 30.01 C ANISOU 1502 CD GLU A 285 3376 4883 3143 47 -202 -1886 C ATOM 1503 OE1 GLU A 285 -7.828 -4.866 19.796 1.00 30.85 O ANISOU 1503 OE1 GLU A 285 3334 4925 3462 -67 -89 -1865 O ATOM 1504 OE2 GLU A 285 -8.869 -5.462 21.646 1.00 29.28 O1- ANISOU 1504 OE2 GLU A 285 3483 4998 2646 209 -225 -1957 O1- ATOM 1505 N GLU A 286 -14.539 -4.360 21.541 1.00 26.23 N ANISOU 1505 N GLU A 286 2730 4181 3055 -400 -1168 -1174 N ATOM 1506 CA GLU A 286 -15.633 -4.609 22.470 1.00 25.85 C ANISOU 1506 CA GLU A 286 2540 4261 3020 -826 -1023 -961 C ATOM 1507 C GLU A 286 -16.905 -5.073 21.751 1.00 30.48 C ANISOU 1507 C GLU A 286 3238 4792 3552 -1083 -807 -1017 C ATOM 1508 O GLU A 286 -17.810 -5.634 22.373 1.00 31.19 O ANISOU 1508 O GLU A 286 3327 4894 3629 -1175 -798 -1010 O ATOM 1509 CB GLU A 286 -15.904 -3.362 23.319 1.00 22.80 C ANISOU 1509 CB GLU A 286 2120 3846 2696 -770 -746 -763 C ATOM 1510 CG GLU A 286 -14.726 -2.972 24.214 1.00 21.36 C ANISOU 1510 CG GLU A 286 1981 3565 2569 -622 -535 -554 C ATOM 1511 CD GLU A 286 -14.976 -1.696 24.993 1.00 20.04 C ANISOU 1511 CD GLU A 286 1653 3386 2574 -496 -427 -145 C ATOM 1512 OE1 GLU A 286 -15.903 -0.944 24.629 1.00 20.42 O ANISOU 1512 OE1 GLU A 286 1591 3494 2674 -303 -72 2 O ATOM 1513 OE2 GLU A 286 -14.248 -1.443 25.974 1.00 18.48 O1- ANISOU 1513 OE2 GLU A 286 1448 3155 2421 -334 -554 19 O1- ATOM 1514 N GLU A 287 -16.965 -4.843 20.443 1.00 33.64 N ANISOU 1514 N GLU A 287 3697 5210 3875 -1211 -695 -1098 N ATOM 1515 CA GLU A 287 -18.087 -5.296 19.624 1.00 37.55 C ANISOU 1515 CA GLU A 287 4198 5685 4384 -1123 -669 -1049 C ATOM 1516 C GLU A 287 -18.248 -6.815 19.715 1.00 39.41 C ANISOU 1516 C GLU A 287 4633 5584 4756 -1110 -364 -1130 C ATOM 1517 O GLU A 287 -19.353 -7.341 19.593 1.00 39.97 O ANISOU 1517 O GLU A 287 4692 5627 4869 -1006 -309 -1145 O ATOM 1518 CB GLU A 287 -17.860 -4.874 18.171 1.00 40.27 C ANISOU 1518 CB GLU A 287 4422 6258 4623 -1069 -815 -974 C ATOM 1519 CG GLU A 287 -19.116 -4.552 17.382 1.00 43.73 C ANISOU 1519 CG GLU A 287 4862 6826 4929 -1076 -778 -980 C ATOM 1520 CD GLU A 287 -18.816 -3.769 16.110 1.00 46.25 C ANISOU 1520 CD GLU A 287 5074 7285 5212 -1119 -835 -1121 C ATOM 1521 OE1 GLU A 287 -17.642 -3.383 15.908 1.00 46.66 O ANISOU 1521 OE1 GLU A 287 4997 7426 5306 -1288 -979 -1141 O ATOM 1522 OE2 GLU A 287 -19.752 -3.537 15.312 1.00 47.32 O1- ANISOU 1522 OE2 GLU A 287 5197 7449 5332 -938 -687 -1182 O1- ATOM 1523 N ASN A 288 -17.139 -7.514 19.944 1.00 41.43 N ANISOU 1523 N ASN A 288 5198 5502 5042 -1188 -4 -1137 N ATOM 1524 CA ASN A 288 -17.136 -8.976 20.024 1.00 43.35 C ANISOU 1524 CA ASN A 288 5579 5509 5382 -1210 246 -1191 C ATOM 1525 C ASN A 288 -17.746 -9.543 21.311 1.00 42.05 C ANISOU 1525 C ASN A 288 5437 5177 5363 -1373 445 -1176 C ATOM 1526 O ASN A 288 -17.948 -10.754 21.426 1.00 41.76 O ANISOU 1526 O ASN A 288 5431 4974 5460 -1272 420 -1180 O ATOM 1527 CB ASN A 288 -15.712 -9.520 19.859 1.00 46.10 C ANISOU 1527 CB ASN A 288 5981 5773 5762 -1098 119 -1258 C ATOM 1528 CG ASN A 288 -15.091 -9.148 18.521 1.00 48.55 C ANISOU 1528 CG ASN A 288 6299 5978 6169 -1011 -168 -1418 C ATOM 1529 ND2 ASN A 288 -15.665 -9.662 17.432 1.00 49.14 N ANISOU 1529 ND2 ASN A 288 6400 6011 6261 -1098 -289 -1525 N ATOM 1530 OD1 ASN A 288 -14.097 -8.418 18.467 1.00 49.22 O ANISOU 1530 OD1 ASN A 288 6366 6013 6321 -909 -358 -1474 O ATOM 1531 N LEU A 289 -18.032 -8.670 22.274 1.00 40.10 N ANISOU 1531 N LEU A 289 5193 4923 5119 -1593 646 -1204 N ATOM 1532 CA LEU A 289 -18.534 -9.100 23.577 1.00 38.19 C ANISOU 1532 CA LEU A 289 4938 4667 4906 -1730 766 -1121 C ATOM 1533 C LEU A 289 -20.055 -9.288 23.585 1.00 38.37 C ANISOU 1533 C LEU A 289 5089 4552 4938 -1921 799 -974 C ATOM 1534 O LEU A 289 -20.752 -8.955 22.623 1.00 37.52 O ANISOU 1534 O LEU A 289 5222 4392 4642 -1922 607 -1099 O ATOM 1535 CB LEU A 289 -18.105 -8.108 24.665 1.00 35.81 C ANISOU 1535 CB LEU A 289 4494 4463 4650 -1756 753 -1109 C ATOM 1536 CG LEU A 289 -16.603 -7.825 24.760 1.00 34.32 C ANISOU 1536 CG LEU A 289 4235 4283 4523 -1841 820 -1157 C ATOM 1537 CD1 LEU A 289 -16.289 -6.803 25.843 1.00 33.54 C ANISOU 1537 CD1 LEU A 289 4081 4265 4399 -1747 891 -1267 C ATOM 1538 CD2 LEU A 289 -15.824 -9.112 24.998 1.00 33.88 C ANISOU 1538 CD2 LEU A 289 4128 4233 4510 -1841 865 -1127 C END If you find results from this site helpful for your research, please cite one of our papers:
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