ATOM 1 N GLU A 2 30.566 6.722 -14.669 1.00 75.03 N ANISOU 1 N GLU A 2 14170 9605 4735 -4391 -766 1310 N ATOM 2 CA GLU A 2 31.564 6.241 -13.709 1.00 60.62 C ANISOU 2 CA GLU A 2 8747 10410 3875 -2837 2560 128 C ATOM 3 C GLU A 2 30.903 5.922 -12.371 1.00 48.78 C ANISOU 3 C GLU A 2 5678 8798 4059 -1140 2091 658 C ATOM 4 O GLU A 2 30.396 6.813 -11.681 1.00 56.39 O ANISOU 4 O GLU A 2 9776 8327 3321 -13 1874 1046 O ATOM 5 CB GLU A 2 32.691 7.249 -13.527 1.00 64.91 C ANISOU 5 CB GLU A 2 9659 11107 3895 -3824 3645 -144 C ATOM 6 CG GLU A 2 33.389 7.757 -14.765 1.00 76.58 C ANISOU 6 CG GLU A 2 13256 11834 4007 -5201 4934 -1036 C ATOM 7 CD GLU A 2 33.801 6.831 -15.876 1.00 82.34 C ANISOU 7 CD GLU A 2 13596 12475 5214 -5915 5693 -1989 C ATOM 8 OE1 GLU A 2 34.522 5.837 -15.626 1.00 85.12 O ANISOU 8 OE1 GLU A 2 15031 12372 4939 -5377 4967 -2771 O ATOM 9 OE2 GLU A 2 33.435 7.074 -17.056 1.00 77.25 O ANISOU 9 OE2 GLU A 2 12258 11815 5278 -6087 5044 -3150 O ATOM 10 N ALA A 3 30.911 4.640 -12.012 1.00 44.52 N ANISOU 10 N ALA A 3 5328 8512 3077 -692 1005 -21 N ATOM 11 CA ALA A 3 30.118 4.176 -10.866 1.00 37.15 C ANISOU 11 CA ALA A 3 4929 6875 2312 -118 256 94 C ATOM 12 C ALA A 3 30.782 4.575 -9.553 1.00 34.76 C ANISOU 12 C ALA A 3 3461 6800 2946 186 120 -148 C ATOM 13 O ALA A 3 31.988 4.643 -9.366 1.00 43.55 O ANISOU 13 O ALA A 3 3381 9094 4071 -291 609 -585 O ATOM 14 CB ALA A 3 29.851 2.690 -10.954 1.00 64.39 C ANISOU 14 CB ALA A 3 12657 7685 4122 -3199 -2118 694 C ATOM 15 N ILE A 4 29.935 4.882 -8.599 1.00 26.63 N ANISOU 15 N ILE A 4 2974 4884 2262 88 -352 393 N ATOM 16 CA ILE A 4 30.298 5.507 -7.366 1.00 25.38 C ANISOU 16 CA ILE A 4 3074 3923 2645 -143 -550 429 C ATOM 17 C ILE A 4 30.523 4.477 -6.284 1.00 22.52 C ANISOU 17 C ILE A 4 2639 3826 2093 -248 -108 227 C ATOM 18 O ILE A 4 29.650 3.621 -6.033 1.00 24.52 O ANISOU 18 O ILE A 4 2716 4108 2491 -448 7 73 O ATOM 19 CB ILE A 4 29.186 6.491 -6.959 1.00 27.51 C ANISOU 19 CB ILE A 4 3879 3966 2607 106 197 825 C ATOM 20 CG1 ILE A 4 29.036 7.552 -8.058 1.00 32.19 C ANISOU 20 CG1 ILE A 4 5071 4419 2740 795 51 1044 C ATOM 21 CG2 ILE A 4 29.428 7.089 -5.590 1.00 28.01 C ANISOU 21 CG2 ILE A 4 4376 3753 2515 -196 418 919 C ATOM 22 CD1 ILE A 4 27.908 8.519 -7.809 1.00 40.82 C ANISOU 22 CD1 ILE A 4 6632 5809 3070 2287 243 1078 C ATOM 23 N GLY A 5 31.696 4.606 -5.679 1.00 20.76 N ANISOU 23 N GLY A 5 2447 3529 1913 -136 125 207 N ATOM 24 CA GLY A 5 32.066 3.631 -4.672 1.00 20.45 C ANISOU 24 CA GLY A 5 2753 3742 1277 -415 59 55 C ATOM 25 C GLY A 5 31.404 3.881 -3.335 1.00 18.18 C ANISOU 25 C GLY A 5 2407 2487 2012 129 559 65 C ATOM 26 O GLY A 5 31.546 4.945 -2.716 1.00 19.77 O ANISOU 26 O GLY A 5 2857 2519 2137 -115 274 46 O ATOM 27 N VAL A 6 30.738 2.833 -2.858 1.00 18.22 N ANISOU 27 N VAL A 6 2583 2735 1606 -312 195 12 N ATOM 28 CA VAL A 6 30.083 2.861 -1.550 1.00 17.01 C ANISOU 28 CA VAL A 6 2426 2469 1569 -126 73 11 C ATOM 29 C VAL A 6 30.573 1.713 -0.695 1.00 17.24 C ANISOU 29 C VAL A 6 2160 2596 1794 -78 51 167 C ATOM 30 O VAL A 6 30.470 0.560 -1.115 1.00 18.12 O ANISOU 30 O VAL A 6 2595 2605 1685 113 26 138 O ATOM 31 CB VAL A 6 28.546 2.803 -1.717 1.00 17.54 C ANISOU 31 CB VAL A 6 2379 2594 1692 -73 64 464 C ATOM 32 CG1 VAL A 6 27.879 2.785 -0.364 1.00 18.16 C ANISOU 32 CG1 VAL A 6 2494 2634 1771 162 236 240 C ATOM 33 CG2 VAL A 6 28.075 3.995 -2.557 1.00 19.01 C ANISOU 33 CG2 VAL A 6 2648 2502 2075 68 192 514 C ATOM 34 N LEU A 7 31.110 1.998 0.479 1.00 17.67 N ANISOU 34 N LEU A 7 2144 2491 2079 263 -182 78 N ATOM 35 CA LEU A 7 31.631 0.962 1.366 1.00 15.59 C ANISOU 35 CA LEU A 7 1495 2564 1863 416 220 59 C ATOM 36 C LEU A 7 30.577 0.717 2.436 1.00 14.92 C ANISOU 36 C LEU A 7 1370 2014 2287 429 382 -120 C ATOM 37 O LEU A 7 30.257 1.580 3.240 1.00 15.61 O ANISOU 37 O LEU A 7 1713 2159 2060 288 463 -193 O ATOM 38 CB LEU A 7 32.940 1.405 1.993 1.00 16.42 C ANISOU 38 CB LEU A 7 1470 2525 2246 172 221 247 C ATOM 39 CG LEU A 7 33.605 0.443 2.981 1.00 15.38 C ANISOU 39 CG LEU A 7 1769 2431 1642 22 13 -88 C ATOM 40 CD1 LEU A 7 34.038 -0.822 2.223 1.00 18.41 C ANISOU 40 CD1 LEU A 7 2348 2562 2084 475 285 -81 C ATOM 41 CD2 LEU A 7 34.775 1.126 3.652 1.00 18.56 C ANISOU 41 CD2 LEU A 7 1722 2769 2560 -218 -174 156 C ATOM 42 N MET A 8 30.059 -0.504 2.424 1.00 16.11 N ANISOU 42 N MET A 8 2406 2135 1578 109 284 -120 N ATOM 43 CA MET A 8 29.110 -0.961 3.430 1.00 15.47 C ANISOU 43 CA MET A 8 2105 1975 1796 201 105 70 C ATOM 44 C MET A 8 29.861 -1.690 4.533 1.00 14.98 C ANISOU 44 C MET A 8 1943 1956 1792 321 197 73 C ATOM 45 O MET A 8 30.587 -2.651 4.281 1.00 16.97 O ANISOU 45 O MET A 8 2034 2289 2125 551 371 186 O ATOM 46 CB MET A 8 28.048 -1.811 2.776 1.00 16.01 C ANISOU 46 CB MET A 8 1913 2336 1834 279 188 -327 C ATOM 47 CG MET A 8 26.900 -2.190 3.637 1.00 19.64 C ANISOU 47 CG MET A 8 2449 2536 2479 -175 618 -448 C ATOM 48 SD MET A 8 25.698 -3.171 2.704 1.00 23.54 S ANISOU 48 SD MET A 8 2226 2710 4010 -234 339 -604 S ATOM 49 CE MET A 8 24.562 -3.484 4.012 1.00 23.59 C ANISOU 49 CE MET A 8 2517 2878 3570 -305 147 -101 C ATOM 50 N MET A 9 29.715 -1.268 5.771 1.00 15.81 N ANISOU 50 N MET A 9 1738 2479 1790 288 144 5 N ATOM 51 CA MET A 9 30.661 -1.707 6.798 1.00 16.10 C ANISOU 51 CA MET A 9 1641 2597 1878 227 124 176 C ATOM 52 C MET A 9 30.422 -3.091 7.335 1.00 17.62 C ANISOU 52 C MET A 9 2212 2590 1893 469 670 241 C ATOM 53 O MET A 9 31.380 -3.770 7.714 1.00 21.05 O ANISOU 53 O MET A 9 2499 2842 2657 704 624 549 O ATOM 54 CB MET A 9 30.653 -0.677 7.945 1.00 18.08 C ANISOU 54 CB MET A 9 2348 2719 1801 70 -55 180 C ATOM 55 CG MET A 9 31.178 0.677 7.527 1.00 17.16 C ANISOU 55 CG MET A 9 2312 2585 1622 266 249 78 C ATOM 56 SD MET A 9 32.798 0.661 6.756 1.00 19.26 S ANISOU 56 SD MET A 9 2186 3004 2127 -21 173 -151 S ATOM 57 CE MET A 9 33.829 0.189 8.158 1.00 22.28 C ANISOU 57 CE MET A 9 2382 3109 2976 155 -235 225 C ATOM 58 N CYS A 10 29.186 -3.539 7.378 1.00 19.04 N ANISOU 58 N CYS A 10 2393 2452 2390 313 563 628 N ATOM 59 CA CYS A 10 28.840 -4.831 7.993 1.00 21.18 C ANISOU 59 CA CYS A 10 2405 2494 3147 607 749 1054 C ATOM 60 C CYS A 10 27.524 -5.339 7.399 1.00 20.20 C ANISOU 60 C CYS A 10 2037 2050 3587 779 1185 533 C ATOM 61 O CYS A 10 26.810 -4.516 6.798 1.00 21.28 O ANISOU 61 O CYS A 10 2542 2169 3372 554 438 399 O ATOM 62 CB CYS A 10 28.790 -4.744 9.529 1.00 22.59 C ANISOU 62 CB CYS A 10 2850 2572 3164 610 950 1270 C ATOM 63 SG CYS A 10 27.646 -3.542 10.166 1.00 28.72 S ANISOU 63 SG CYS A 10 3737 3623 3553 1157 1168 731 S ATOM 64 N PRO A 11 27.167 -6.613 7.483 1.00 24.55 N ANISOU 64 N PRO A 11 2656 2085 4587 606 1094 705 N ATOM 65 CA PRO A 11 25.938 -7.097 6.817 1.00 28.22 C ANISOU 65 CA PRO A 11 2545 2242 5937 448 953 458 C ATOM 66 C PRO A 11 24.594 -6.882 7.472 1.00 27.72 C ANISOU 66 C PRO A 11 2699 2439 5394 720 1099 1831 C ATOM 67 O PRO A 11 23.894 -7.812 7.917 1.00 37.50 O ANISOU 67 O PRO A 11 4588 2462 7198 -173 2635 868 O ATOM 68 CB PRO A 11 26.177 -8.615 6.781 1.00 33.35 C ANISOU 68 CB PRO A 11 3529 2242 6899 513 605 190 C ATOM 69 CG PRO A 11 26.926 -8.844 8.060 1.00 36.65 C ANISOU 69 CG PRO A 11 4317 2347 7259 -211 283 1509 C ATOM 70 CD PRO A 11 27.920 -7.704 8.132 1.00 28.75 C ANISOU 70 CD PRO A 11 2683 2043 6197 657 998 976 C ATOM 71 N MET A 12 24.145 -5.678 7.483 1.00 20.58 N ANISOU 71 N MET A 12 2472 2248 3101 384 652 625 N ATOM 72 CA MET A 12 23.042 -5.140 8.238 1.00 17.81 C ANISOU 72 CA MET A 12 2202 2390 2174 -256 449 311 C ATOM 73 C MET A 12 21.652 -5.317 7.642 1.00 18.70 C ANISOU 73 C MET A 12 2194 2438 2471 -153 442 106 C ATOM 74 O MET A 12 20.663 -5.125 8.388 1.00 21.17 O ANISOU 74 O MET A 12 2299 2617 3126 -23 929 562 O ATOM 75 CB MET A 12 23.285 -3.625 8.448 1.00 18.52 C ANISOU 75 CB MET A 12 2373 2397 2265 -280 663 57 C ATOM 76 CG MET A 12 23.253 -2.788 7.221 1.00 19.13 C ANISOU 76 CG MET A 12 3027 2131 2109 -221 610 -107 C ATOM 77 SD MET A 12 23.919 -1.141 7.311 1.00 18.02 S ANISOU 77 SD MET A 12 2157 2058 2632 77 156 114 S ATOM 78 CE MET A 12 25.672 -1.314 7.444 1.00 18.25 C ANISOU 78 CE MET A 12 2190 2507 2237 355 327 135 C ATOM 79 N SER A 13 21.552 -5.633 6.366 1.00 19.02 N ANISOU 79 N SER A 13 2394 2243 2590 -158 162 114 N ATOM 80 CA SER A 13 20.255 -5.700 5.702 1.00 18.66 C ANISOU 80 CA SER A 13 2276 2234 2581 8 345 -110 C ATOM 81 C SER A 13 20.434 -6.253 4.299 1.00 19.25 C ANISOU 81 C SER A 13 3033 1833 2447 -172 147 87 C ATOM 82 O SER A 13 21.062 -5.591 3.474 1.00 18.98 O ANISOU 82 O SER A 13 2533 2048 2631 67 448 15 O ATOM 83 CB SER A 13 19.608 -4.316 5.583 1.00 21.28 C ANISOU 83 CB SER A 13 2534 2457 3095 292 330 -148 C ATOM 84 OG SER A 13 18.556 -4.303 4.595 1.00 20.39 O ANISOU 84 OG SER A 13 2563 2334 2850 145 396 64 O ATOM 85 N THR A 14 19.869 -7.415 4.048 1.00 19.83 N ANISOU 85 N THR A 14 2290 1919 3325 16 343 -320 N ATOM 86 CA THR A 14 19.879 -7.995 2.712 1.00 21.35 C ANISOU 86 CA THR A 14 2530 2163 3419 -30 12 -508 C ATOM 87 C THR A 14 19.303 -7.034 1.696 1.00 20.64 C ANISOU 87 C THR A 14 2384 2161 3298 -54 290 -431 C ATOM 88 O THR A 14 19.902 -6.847 0.638 1.00 21.24 O ANISOU 88 O THR A 14 2366 2534 3173 82 241 -639 O ATOM 89 CB THR A 14 19.106 -9.330 2.719 1.00 23.77 C ANISOU 89 CB THR A 14 3364 2073 3595 -144 -49 -437 C ATOM 90 OG1 THR A 14 19.816 -10.212 3.621 1.00 28.51 O ANISOU 90 OG1 THR A 14 3835 2200 4799 564 18 -106 O ATOM 91 CG2 THR A 14 19.071 -9.925 1.325 1.00 27.96 C ANISOU 91 CG2 THR A 14 4314 2135 4173 72 443 -1196 C ATOM 92 N TYR A 15 18.160 -6.446 2.014 1.00 19.88 N ANISOU 92 N TYR A 15 2314 2129 3112 -120 268 -383 N ATOM 93 CA TYR A 15 17.482 -5.537 1.100 1.00 19.00 C ANISOU 93 CA TYR A 15 2146 2178 2896 -273 -32 -667 C ATOM 94 C TYR A 15 18.353 -4.340 0.775 1.00 18.16 C ANISOU 94 C TYR A 15 1611 2317 2973 -76 -438 -178 C ATOM 95 O TYR A 15 18.504 -3.936 -0.391 1.00 20.02 O ANISOU 95 O TYR A 15 2368 2369 2869 -22 -71 -365 O ATOM 96 CB TYR A 15 16.151 -5.131 1.737 1.00 21.27 C ANISOU 96 CB TYR A 15 1977 2129 3974 -360 111 -707 C ATOM 97 CG TYR A 15 15.444 -4.019 1.018 1.00 21.29 C ANISOU 97 CG TYR A 15 1978 2443 3670 -322 16 -669 C ATOM 98 CD1 TYR A 15 14.732 -4.245 -0.131 1.00 23.71 C ANISOU 98 CD1 TYR A 15 2336 2692 3982 -324 -236 -956 C ATOM 99 CD2 TYR A 15 15.473 -2.704 1.480 1.00 20.50 C ANISOU 99 CD2 TYR A 15 2309 2339 3140 -18 -286 -430 C ATOM 100 CE1 TYR A 15 14.072 -3.263 -0.825 1.00 25.51 C ANISOU 100 CE1 TYR A 15 2335 3194 4165 -52 -677 -1147 C ATOM 101 CE2 TYR A 15 14.807 -1.702 0.798 1.00 20.95 C ANISOU 101 CE2 TYR A 15 2283 2630 3046 -180 -572 -253 C ATOM 102 CZ TYR A 15 14.107 -1.979 -0.348 1.00 22.36 C ANISOU 102 CZ TYR A 15 2459 2844 3194 -196 -592 -534 C ATOM 103 OH TYR A 15 13.443 -1.002 -1.050 1.00 25.94 O ANISOU 103 OH TYR A 15 2802 3598 3456 358 -1054 -557 O ATOM 104 N LEU A 16 18.931 -3.742 1.835 1.00 18.04 N ANISOU 104 N LEU A 16 1684 2213 2957 -171 -124 -424 N ATOM 105 CA LEU A 16 19.785 -2.586 1.570 1.00 16.86 C ANISOU 105 CA LEU A 16 1875 2066 2467 -106 -80 -247 C ATOM 106 C LEU A 16 20.989 -2.894 0.680 1.00 17.33 C ANISOU 106 C LEU A 16 2134 2171 2278 -97 37 -261 C ATOM 107 O LEU A 16 21.366 -2.091 -0.184 1.00 17.42 O ANISOU 107 O LEU A 16 2259 2375 1983 -84 -143 -207 O ATOM 108 CB LEU A 16 20.302 -1.975 2.897 1.00 16.28 C ANISOU 108 CB LEU A 16 1953 1927 2308 -166 78 -190 C ATOM 109 CG LEU A 16 21.184 -0.744 2.814 1.00 15.31 C ANISOU 109 CG LEU A 16 1579 2232 2005 -236 -30 17 C ATOM 110 CD1 LEU A 16 20.545 0.418 2.061 1.00 17.07 C ANISOU 110 CD1 LEU A 16 2199 2064 2221 -174 -33 -7 C ATOM 111 CD2 LEU A 16 21.557 -0.275 4.224 1.00 17.37 C ANISOU 111 CD2 LEU A 16 1727 2660 2213 -74 -151 -400 C ATOM 112 N GLU A 17 21.593 -4.052 0.941 1.00 17.27 N ANISOU 112 N GLU A 17 2220 2340 2000 33 234 -175 N ATOM 113 CA GLU A 17 22.721 -4.517 0.153 1.00 17.65 C ANISOU 113 CA GLU A 17 2195 1979 2533 -274 557 -163 C ATOM 114 C GLU A 17 22.272 -4.596 -1.300 1.00 21.00 C ANISOU 114 C GLU A 17 2445 3009 2526 -204 667 -784 C ATOM 115 O GLU A 17 23.013 -4.123 -2.166 1.00 21.11 O ANISOU 115 O GLU A 17 2660 3082 2279 -508 436 -770 O ATOM 116 CB GLU A 17 23.200 -5.848 0.702 1.00 22.29 C ANISOU 116 CB GLU A 17 2648 1981 3840 -21 1350 294 C ATOM 117 CG GLU A 17 24.524 -6.398 0.282 1.00 31.28 C ANISOU 117 CG GLU A 17 2464 3187 6232 478 1066 377 C ATOM 118 CD GLU A 17 24.902 -7.676 0.992 1.00 33.07 C ANISOU 118 CD GLU A 17 2533 3330 6702 384 -463 307 C ATOM 119 OE1 GLU A 17 25.666 -8.437 0.386 1.00 34.15 O ANISOU 119 OE1 GLU A 17 3894 2894 6188 508 -384 238 O ATOM 120 OE2 GLU A 17 24.470 -7.917 2.116 1.00 37.10 O ANISOU 120 OE2 GLU A 17 3482 2661 7955 1222 953 1206 O ATOM 121 N GLN A 18 21.089 -5.173 -1.543 1.00 20.46 N ANISOU 121 N GLN A 18 2756 2671 2345 -401 378 -277 N ATOM 122 CA GLN A 18 20.575 -5.342 -2.905 1.00 24.18 C ANISOU 122 CA GLN A 18 3117 3416 2654 29 37 -682 C ATOM 123 C GLN A 18 20.366 -3.985 -3.584 1.00 23.82 C ANISOU 123 C GLN A 18 3664 3326 2059 -469 -819 -942 C ATOM 124 O GLN A 18 20.703 -3.757 -4.760 1.00 26.62 O ANISOU 124 O GLN A 18 3792 4058 2266 -515 -524 -663 O ATOM 125 CB GLN A 18 19.271 -6.145 -2.906 1.00 25.68 C ANISOU 125 CB GLN A 18 3238 2965 3554 119 -628 -671 C ATOM 126 CG GLN A 18 19.408 -7.627 -2.601 1.00 30.43 C ANISOU 126 CG GLN A 18 4653 2768 4139 -14 -772 -1053 C ATOM 127 CD GLN A 18 18.082 -8.308 -2.302 1.00 31.99 C ANISOU 127 CD GLN A 18 4392 2433 5331 -341 -2176 -901 C ATOM 128 OE1 GLN A 18 17.047 -7.647 -2.064 1.00 40.66 O ANISOU 128 OE1 GLN A 18 4574 2936 7938 -236 -582 190 O ATOM 129 NE2 GLN A 18 18.067 -9.633 -2.338 1.00 39.74 N ANISOU 129 NE2 GLN A 18 6864 2375 5860 -467 -863 -857 N ATOM 130 N GLU A 19 19.800 -3.060 -2.789 1.00 22.72 N ANISOU 130 N GLU A 19 2818 3063 2753 -479 -274 -597 N ATOM 131 CA GLU A 19 19.451 -1.744 -3.333 1.00 22.47 C ANISOU 131 CA GLU A 19 2600 3515 2421 -314 -260 -190 C ATOM 132 C GLU A 19 20.684 -0.915 -3.612 1.00 21.54 C ANISOU 132 C GLU A 19 2603 3528 2055 -255 -368 146 C ATOM 133 O GLU A 19 20.694 -0.141 -4.593 1.00 24.90 O ANISOU 133 O GLU A 19 3126 3988 2346 -598 -886 462 O ATOM 134 CB GLU A 19 18.499 -1.024 -2.380 1.00 23.58 C ANISOU 134 CB GLU A 19 2896 3305 2757 -70 107 264 C ATOM 135 CG GLU A 19 17.174 -1.778 -2.228 1.00 23.38 C ANISOU 135 CG GLU A 19 2912 2833 3140 -12 241 2 C ATOM 136 CD GLU A 19 16.395 -1.834 -3.516 1.00 29.01 C ANISOU 136 CD GLU A 19 2699 4469 3853 -90 -270 602 C ATOM 137 OE1 GLU A 19 16.156 -0.735 -4.073 1.00 39.16 O ANISOU 137 OE1 GLU A 19 3592 5737 5551 -442 -833 2353 O ATOM 138 OE2 GLU A 19 16.025 -2.926 -4.005 1.00 35.64 O ANISOU 138 OE2 GLU A 19 3845 5647 4052 -919 -1026 -40 O ATOM 139 N LEU A 20 21.718 -1.085 -2.783 1.00 19.31 N ANISOU 139 N LEU A 20 2510 2572 2255 -40 -333 108 N ATOM 140 CA LEU A 20 22.968 -0.393 -3.046 1.00 20.91 C ANISOU 140 CA LEU A 20 2666 3081 2198 -370 -185 -388 C ATOM 141 C LEU A 20 23.696 -0.998 -4.225 1.00 22.87 C ANISOU 141 C LEU A 20 2921 3654 2114 -450 -96 -555 C ATOM 142 O LEU A 20 24.243 -0.236 -5.037 1.00 23.85 O ANISOU 142 O LEU A 20 3121 3735 2204 -50 -46 -239 O ATOM 143 CB LEU A 20 23.875 -0.374 -1.813 1.00 19.88 C ANISOU 143 CB LEU A 20 2445 3109 2000 -185 5 -368 C ATOM 144 CG LEU A 20 23.363 0.399 -0.591 1.00 16.69 C ANISOU 144 CG LEU A 20 2062 2316 1965 -485 265 -6 C ATOM 145 CD1 LEU A 20 24.268 0.136 0.595 1.00 18.08 C ANISOU 145 CD1 LEU A 20 2491 2425 1955 -390 33 -341 C ATOM 146 CD2 LEU A 20 23.244 1.861 -0.915 1.00 20.45 C ANISOU 146 CD2 LEU A 20 2790 2356 2624 -578 130 176 C ATOM 147 N ASP A 21 23.673 -2.315 -4.331 1.00 22.27 N ANISOU 147 N ASP A 21 2606 3753 2105 -591 379 -785 N ATOM 148 CA ASP A 21 24.353 -3.018 -5.414 1.00 23.08 C ANISOU 148 CA ASP A 21 2316 4114 2341 -469 368 -885 C ATOM 149 C ASP A 21 23.754 -2.648 -6.765 1.00 25.15 C ANISOU 149 C ASP A 21 3114 4253 2190 -744 186 -1087 C ATOM 150 O ASP A 21 24.543 -2.603 -7.710 1.00 30.48 O ANISOU 150 O ASP A 21 3788 5473 2321 -90 511 -799 O ATOM 151 CB ASP A 21 24.280 -4.531 -5.128 1.00 26.05 C ANISOU 151 CB ASP A 21 3375 3985 2539 -540 154 -1186 C ATOM 152 CG ASP A 21 25.389 -5.384 -5.687 1.00 32.98 C ANISOU 152 CG ASP A 21 3234 4106 5188 -407 93 -1778 C ATOM 153 OD1 ASP A 21 26.498 -4.928 -6.017 1.00 29.67 O ANISOU 153 OD1 ASP A 21 3428 4250 3595 -124 298 -891 O ATOM 154 OD2 ASP A 21 25.147 -6.611 -5.811 1.00 48.17 O ANISOU 154 OD2 ASP A 21 4922 4299 9081 -863 2125 -2651 O ATOM 155 N LYS A 22 22.443 -2.398 -6.846 1.00 27.10 N ANISOU 155 N LYS A 22 3101 4842 2352 -768 -274 -577 N ATOM 156 CA LYS A 22 21.745 -2.007 -8.058 1.00 31.13 C ANISOU 156 CA LYS A 22 4436 5184 2208 -342 -467 -545 C ATOM 157 C LYS A 22 22.176 -0.593 -8.481 1.00 29.31 C ANISOU 157 C LYS A 22 3981 5298 1859 -233 180 -578 C ATOM 158 O LYS A 22 22.147 -0.318 -9.687 1.00 35.95 O ANISOU 158 O LYS A 22 5557 6175 1927 -646 381 -390 O ATOM 159 CB LYS A 22 20.222 -1.902 -8.034 1.00 34.67 C ANISOU 159 CB LYS A 22 4280 6833 2062 -1277 -1429 366 C ATOM 160 CG LYS A 22 19.311 -3.043 -7.707 1.00 43.30 C ANISOU 160 CG LYS A 22 5907 7771 2775 -2632 -369 -916 C ATOM 161 CD LYS A 22 17.869 -2.541 -7.689 1.00 46.39 C ANISOU 161 CD LYS A 22 5200 9419 3007 -3304 -1029 -928 C ATOM 162 CE LYS A 22 16.898 -3.675 -7.520 1.00 50.03 C ANISOU 162 CE LYS A 22 6464 9549 2997 -3966 -531 -1740 C ATOM 163 NZ LYS A 22 15.649 -3.324 -6.773 1.00 51.00 N ANISOU 163 NZ LYS A 22 5548 9963 3866 -2904 -728 1007 N ATOM 164 N ARG A 23 22.530 0.267 -7.526 1.00 28.71 N ANISOU 164 N ARG A 23 3242 5221 2447 -308 -535 -466 N ATOM 165 CA ARG A 23 22.745 1.673 -7.833 1.00 28.22 C ANISOU 165 CA ARG A 23 3168 5103 2451 146 -702 -347 C ATOM 166 C ARG A 23 24.167 2.199 -7.907 1.00 24.90 C ANISOU 166 C ARG A 23 3232 4522 1706 244 -630 266 C ATOM 167 O ARG A 23 24.461 3.201 -8.572 1.00 33.66 O ANISOU 167 O ARG A 23 4642 5398 2748 -344 -1138 1314 O ATOM 168 CB ARG A 23 22.066 2.468 -6.699 1.00 27.74 C ANISOU 168 CB ARG A 23 3434 5013 2092 -207 -230 4 C ATOM 169 CG ARG A 23 20.549 2.431 -6.868 1.00 29.49 C ANISOU 169 CG ARG A 23 3453 5344 2408 330 -519 -164 C ATOM 170 CD ARG A 23 19.938 3.046 -5.623 1.00 31.12 C ANISOU 170 CD ARG A 23 3282 5858 2683 -334 -184 -497 C ATOM 171 NE ARG A 23 18.486 3.193 -5.758 1.00 30.45 N ANISOU 171 NE ARG A 23 3282 5579 2709 -232 -200 -153 N ATOM 172 CZ ARG A 23 17.607 2.202 -5.644 1.00 31.07 C ANISOU 172 CZ ARG A 23 3115 5625 3065 -103 635 -22 C ATOM 173 NH1 ARG A 23 18.063 0.985 -5.388 1.00 35.39 N ANISOU 173 NH1 ARG A 23 3056 5734 4657 -496 -1282 360 N ATOM 174 NH2 ARG A 23 16.304 2.446 -5.787 1.00 32.59 N ANISOU 174 NH2 ARG A 23 3270 5635 3477 -264 -200 1018 N ATOM 175 N PHE A 24 25.048 1.544 -7.182 1.00 24.72 N ANISOU 175 N PHE A 24 3244 3772 2378 263 -857 8 N ATOM 176 CA PHE A 24 26.374 2.062 -6.913 1.00 22.85 C ANISOU 176 CA PHE A 24 3157 3730 1794 169 -536 207 C ATOM 177 C PHE A 24 27.403 0.974 -7.138 1.00 21.98 C ANISOU 177 C PHE A 24 3043 3495 1814 -151 -408 -307 C ATOM 178 O PHE A 24 27.081 -0.175 -7.426 1.00 24.45 O ANISOU 178 O PHE A 24 3647 3578 2063 -539 71 -317 O ATOM 179 CB PHE A 24 26.465 2.544 -5.451 1.00 23.00 C ANISOU 179 CB PHE A 24 2713 3924 2102 177 -272 -310 C ATOM 180 CG PHE A 24 25.478 3.638 -5.096 1.00 22.84 C ANISOU 180 CG PHE A 24 2629 3503 2546 -52 169 223 C ATOM 181 CD1 PHE A 24 25.631 4.900 -5.666 1.00 27.98 C ANISOU 181 CD1 PHE A 24 3203 4157 3270 258 264 1203 C ATOM 182 CD2 PHE A 24 24.420 3.448 -4.211 1.00 21.77 C ANISOU 182 CD2 PHE A 24 3066 3499 1704 -171 146 -235 C ATOM 183 CE1 PHE A 24 24.779 5.933 -5.384 1.00 26.70 C ANISOU 183 CE1 PHE A 24 3400 3897 2848 270 265 1496 C ATOM 184 CE2 PHE A 24 23.543 4.494 -3.935 1.00 22.04 C ANISOU 184 CE2 PHE A 24 3385 3367 1622 -107 434 91 C ATOM 185 CZ PHE A 24 23.727 5.741 -4.521 1.00 24.51 C ANISOU 185 CZ PHE A 24 3485 3880 1947 45 45 862 C ATOM 186 N LYS A 25 28.667 1.307 -6.976 1.00 22.04 N ANISOU 186 N LYS A 25 2965 3564 1846 -150 -341 279 N ATOM 187 CA LYS A 25 29.720 0.292 -6.878 1.00 23.03 C ANISOU 187 CA LYS A 25 3198 3901 1650 233 142 310 C ATOM 188 C LYS A 25 29.880 -0.091 -5.408 1.00 21.07 C ANISOU 188 C LYS A 25 2657 3712 1637 4 -169 172 C ATOM 189 O LYS A 25 30.482 0.644 -4.643 1.00 21.97 O ANISOU 189 O LYS A 25 3034 3320 1995 278 -187 -73 O ATOM 190 CB LYS A 25 31.031 0.818 -7.467 1.00 27.69 C ANISOU 190 CB LYS A 25 3530 4733 2257 206 743 340 C ATOM 191 CG LYS A 25 32.174 -0.196 -7.435 1.00 34.68 C ANISOU 191 CG LYS A 25 3440 6161 3576 781 649 86 C ATOM 192 CD LYS A 25 33.414 0.272 -8.187 1.00 42.67 C ANISOU 192 CD LYS A 25 3624 7930 4657 658 1138 440 C ATOM 193 CE LYS A 25 33.932 -0.795 -9.135 1.00 55.99 C ANISOU 193 CE LYS A 25 5843 9079 6351 80 3451 -454 C ATOM 194 NZ LYS A 25 35.420 -0.893 -9.176 1.00 68.09 N ANISOU 194 NZ LYS A 25 6093 11170 8610 1499 4588 298 N ATOM 195 N LEU A 26 29.257 -1.202 -5.026 1.00 21.86 N ANISOU 195 N LEU A 26 3877 2711 1719 494 -241 116 N ATOM 196 CA LEU A 26 29.186 -1.623 -3.639 1.00 19.47 C ANISOU 196 CA LEU A 26 2653 3047 1697 535 -146 98 C ATOM 197 C LEU A 26 30.401 -2.454 -3.251 1.00 20.63 C ANISOU 197 C LEU A 26 2802 3124 1911 698 -384 -264 C ATOM 198 O LEU A 26 30.653 -3.472 -3.907 1.00 21.42 O ANISOU 198 O LEU A 26 2850 3185 2103 645 -110 -362 O ATOM 199 CB LEU A 26 27.920 -2.461 -3.359 1.00 21.45 C ANISOU 199 CB LEU A 26 2765 3258 2128 366 -139 23 C ATOM 200 CG LEU A 26 27.784 -3.026 -1.936 1.00 23.65 C ANISOU 200 CG LEU A 26 2998 4200 1787 -562 -61 -275 C ATOM 201 CD1 LEU A 26 27.683 -1.908 -0.905 1.00 24.56 C ANISOU 201 CD1 LEU A 26 3100 4071 2161 153 -435 -340 C ATOM 202 CD2 LEU A 26 26.582 -3.976 -1.820 1.00 23.42 C ANISOU 202 CD2 LEU A 26 2581 3472 2845 34 -402 433 C ATOM 203 N PHE A 27 31.056 -2.009 -2.185 1.00 19.01 N ANISOU 203 N PHE A 27 2264 2969 1990 174 -171 -57 N ATOM 204 CA PHE A 27 32.103 -2.756 -1.509 1.00 19.01 C ANISOU 204 CA PHE A 27 2333 2999 1892 438 -178 -409 C ATOM 205 C PHE A 27 31.561 -3.255 -0.171 1.00 17.92 C ANISOU 205 C PHE A 27 2117 2835 1857 640 -341 -372 C ATOM 206 O PHE A 27 30.996 -2.459 0.565 1.00 19.60 O ANISOU 206 O PHE A 27 2667 2789 1991 593 3 -378 O ATOM 207 CB PHE A 27 33.335 -1.889 -1.289 1.00 20.22 C ANISOU 207 CB PHE A 27 2430 3172 2082 321 -448 -37 C ATOM 208 CG PHE A 27 33.997 -1.396 -2.561 1.00 22.65 C ANISOU 208 CG PHE A 27 3080 3291 2234 -97 -79 -326 C ATOM 209 CD1 PHE A 27 34.728 -2.266 -3.334 1.00 23.26 C ANISOU 209 CD1 PHE A 27 3058 3591 2186 105 -160 -301 C ATOM 210 CD2 PHE A 27 33.872 -0.078 -2.952 1.00 28.05 C ANISOU 210 CD2 PHE A 27 4550 3467 2642 198 934 54 C ATOM 211 CE1 PHE A 27 35.316 -1.797 -4.484 1.00 25.54 C ANISOU 211 CE1 PHE A 27 2897 4291 2515 239 107 -79 C ATOM 212 CE2 PHE A 27 34.482 0.420 -4.101 1.00 29.75 C ANISOU 212 CE2 PHE A 27 3770 4257 3275 525 1144 586 C ATOM 213 CZ PHE A 27 35.208 -0.466 -4.865 1.00 25.22 C ANISOU 213 CZ PHE A 27 2448 4601 2533 498 226 443 C ATOM 214 N ARG A 28 31.733 -4.540 0.079 1.00 21.84 N ANISOU 214 N ARG A 28 3034 2863 2403 853 147 -176 N ATOM 215 CA ARG A 28 31.356 -5.137 1.356 1.00 21.21 C ANISOU 215 CA ARG A 28 2806 2824 2428 757 242 -201 C ATOM 216 C ARG A 28 32.589 -5.291 2.250 1.00 20.71 C ANISOU 216 C ARG A 28 2701 2725 2443 715 337 28 C ATOM 217 O ARG A 28 33.398 -6.184 2.029 1.00 23.20 O ANISOU 217 O ARG A 28 2754 3176 2885 923 310 -322 O ATOM 218 CB ARG A 28 30.645 -6.452 1.114 1.00 24.11 C ANISOU 218 CB ARG A 28 2898 2833 3428 665 10 -121 C ATOM 219 CG ARG A 28 29.401 -6.348 0.236 1.00 28.24 C ANISOU 219 CG ARG A 28 2929 2733 5069 772 -590 -165 C ATOM 220 CD ARG A 28 28.978 -7.705 -0.284 1.00 33.96 C ANISOU 220 CD ARG A 28 4788 3055 5060 246 -1471 -137 C ATOM 221 NE ARG A 28 27.744 -7.774 -1.043 1.00 34.93 N ANISOU 221 NE ARG A 28 4721 3303 5248 336 -1437 -312 N ATOM 222 CZ ARG A 28 27.472 -7.505 -2.313 1.00 36.00 C ANISOU 222 CZ ARG A 28 4636 4069 4974 565 -1419 -920 C ATOM 223 NH1 ARG A 28 28.417 -7.071 -3.146 1.00 45.12 N ANISOU 223 NH1 ARG A 28 6471 6215 4458 -523 -449 -1901 N ATOM 224 NH2 ARG A 28 26.245 -7.648 -2.817 1.00 44.44 N ANISOU 224 NH2 ARG A 28 5695 4701 6491 -208 -2740 -1536 N ATOM 225 N TYR A 29 32.726 -4.395 3.238 1.00 19.51 N ANISOU 225 N TYR A 29 2286 3030 2097 703 477 74 N ATOM 226 CA TYR A 29 33.987 -4.347 3.976 1.00 19.27 C ANISOU 226 CA TYR A 29 2081 2852 2389 596 547 197 C ATOM 227 C TYR A 29 34.269 -5.647 4.700 1.00 21.89 C ANISOU 227 C TYR A 29 2342 3287 2690 833 587 600 C ATOM 228 O TYR A 29 35.444 -6.052 4.797 1.00 21.29 O ANISOU 228 O TYR A 29 2489 3652 1948 1060 312 187 O ATOM 229 CB TYR A 29 33.935 -3.211 5.000 1.00 20.85 C ANISOU 229 CB TYR A 29 2413 3321 2189 363 511 31 C ATOM 230 CG TYR A 29 35.209 -2.869 5.724 1.00 20.39 C ANISOU 230 CG TYR A 29 2237 3266 2246 716 496 37 C ATOM 231 CD1 TYR A 29 36.365 -2.566 5.042 1.00 21.61 C ANISOU 231 CD1 TYR A 29 2250 3466 2494 667 522 265 C ATOM 232 CD2 TYR A 29 35.243 -2.832 7.094 1.00 22.11 C ANISOU 232 CD2 TYR A 29 2415 3721 2266 353 505 -285 C ATOM 233 CE1 TYR A 29 37.547 -2.242 5.683 1.00 23.57 C ANISOU 233 CE1 TYR A 29 2270 3808 2876 598 391 459 C ATOM 234 CE2 TYR A 29 36.413 -2.510 7.770 1.00 22.80 C ANISOU 234 CE2 TYR A 29 2283 3784 2596 705 412 -477 C ATOM 235 CZ TYR A 29 37.569 -2.214 7.076 1.00 24.35 C ANISOU 235 CZ TYR A 29 2269 4088 2894 507 353 -201 C ATOM 236 OH TYR A 29 38.737 -1.893 7.752 1.00 27.34 O ANISOU 236 OH TYR A 29 2369 4494 3524 451 2 28 O ATOM 237 N TRP A 30 33.241 -6.282 5.233 1.00 22.72 N ANISOU 237 N TRP A 30 2577 2943 3113 834 590 718 N ATOM 238 CA TRP A 30 33.353 -7.427 6.139 1.00 23.89 C ANISOU 238 CA TRP A 30 2859 3211 3006 842 652 815 C ATOM 239 C TRP A 30 33.769 -8.684 5.419 1.00 24.78 C ANISOU 239 C TRP A 30 3215 3021 3179 1072 508 963 C ATOM 240 O TRP A 30 34.126 -9.692 6.055 1.00 30.18 O ANISOU 240 O TRP A 30 3846 3656 3965 1683 557 1434 O ATOM 241 CB TRP A 30 32.014 -7.677 6.848 1.00 28.09 C ANISOU 241 CB TRP A 30 3192 3495 3988 930 1185 1240 C ATOM 242 CG TRP A 30 30.884 -8.150 5.980 1.00 25.91 C ANISOU 242 CG TRP A 30 2684 2793 4369 1003 1549 898 C ATOM 243 CD1 TRP A 30 30.495 -9.466 5.793 1.00 32.08 C ANISOU 243 CD1 TRP A 30 4412 2542 5234 1432 871 485 C ATOM 244 CD2 TRP A 30 29.973 -7.361 5.181 1.00 25.54 C ANISOU 244 CD2 TRP A 30 3156 2473 4075 702 1063 751 C ATOM 245 NE1 TRP A 30 29.421 -9.548 4.944 1.00 33.04 N ANISOU 245 NE1 TRP A 30 4562 2448 5545 587 713 740 N ATOM 246 CE2 TRP A 30 29.085 -8.269 4.556 1.00 28.27 C ANISOU 246 CE2 TRP A 30 3064 2467 5208 744 1042 434 C ATOM 247 CE3 TRP A 30 29.784 -5.996 4.913 1.00 25.48 C ANISOU 247 CE3 TRP A 30 3111 2370 4199 1070 934 170 C ATOM 248 CZ2 TRP A 30 28.064 -7.844 3.699 1.00 27.19 C ANISOU 248 CZ2 TRP A 30 2743 2306 5282 -79 1060 852 C ATOM 249 CZ3 TRP A 30 28.772 -5.588 4.063 1.00 24.42 C ANISOU 249 CZ3 TRP A 30 3253 1949 4078 997 798 -138 C ATOM 250 CH2 TRP A 30 27.911 -6.519 3.459 1.00 26.49 C ANISOU 250 CH2 TRP A 30 3499 2182 4382 450 816 211 C ATOM 251 N THR A 31 33.718 -8.663 4.091 1.00 25.81 N ANISOU 251 N THR A 31 3654 2954 3197 780 416 602 N ATOM 252 CA THR A 31 34.109 -9.834 3.285 1.00 29.34 C ANISOU 252 CA THR A 31 3900 3153 4095 271 1191 132 C ATOM 253 C THR A 31 35.585 -9.779 2.915 1.00 29.33 C ANISOU 253 C THR A 31 3623 2870 4652 954 709 550 C ATOM 254 O THR A 31 36.105 -10.776 2.401 1.00 36.73 O ANISOU 254 O THR A 31 4082 2849 7027 996 1122 73 O ATOM 255 CB THR A 31 33.283 -10.018 1.986 1.00 30.65 C ANISOU 255 CB THR A 31 3574 3377 4693 420 1066 -872 C ATOM 256 OG1 THR A 31 33.452 -8.899 1.097 1.00 30.10 O ANISOU 256 OG1 THR A 31 3594 3883 3960 738 179 -702 O ATOM 257 CG2 THR A 31 31.796 -10.109 2.296 1.00 37.72 C ANISOU 257 CG2 THR A 31 3437 3474 7422 602 956 -608 C ATOM 258 N GLN A 32 36.247 -8.658 3.137 1.00 25.86 N ANISOU 258 N GLN A 32 2795 3364 3668 1063 486 -37 N ATOM 259 CA GLN A 32 37.648 -8.542 2.689 1.00 26.59 C ANISOU 259 CA GLN A 32 2928 3902 3270 1173 655 -105 C ATOM 260 C GLN A 32 38.588 -9.211 3.676 1.00 27.55 C ANISOU 260 C GLN A 32 2944 4138 3387 1392 245 -709 C ATOM 261 O GLN A 32 38.645 -8.788 4.850 1.00 30.93 O ANISOU 261 O GLN A 32 4044 4266 3443 1731 150 -836 O ATOM 262 CB GLN A 32 38.025 -7.068 2.488 1.00 27.48 C ANISOU 262 CB GLN A 32 3537 4425 2479 219 411 -36 C ATOM 263 CG GLN A 32 37.265 -6.396 1.344 1.00 27.47 C ANISOU 263 CG GLN A 32 3603 4066 2769 -72 240 186 C ATOM 264 CD GLN A 32 37.802 -6.963 0.026 1.00 27.48 C ANISOU 264 CD GLN A 32 3436 4451 2554 221 266 523 C ATOM 265 OE1 GLN A 32 38.941 -7.397 -0.110 1.00 35.76 O ANISOU 265 OE1 GLN A 32 3758 5723 4105 950 -395 -1287 O ATOM 266 NE2 GLN A 32 36.993 -6.989 -0.996 1.00 28.24 N ANISOU 266 NE2 GLN A 32 3969 3938 2821 590 -119 204 N ATOM 267 N PRO A 33 39.333 -10.253 3.295 1.00 29.03 N ANISOU 267 N PRO A 33 3865 3796 3368 1580 -228 -823 N ATOM 268 CA PRO A 33 40.291 -10.854 4.232 1.00 29.70 C ANISOU 268 CA PRO A 33 4549 3549 3189 1683 -125 -440 C ATOM 269 C PRO A 33 41.471 -9.985 4.640 1.00 29.12 C ANISOU 269 C PRO A 33 4524 3865 2675 1765 -690 -132 C ATOM 270 O PRO A 33 42.094 -10.207 5.696 1.00 36.40 O ANISOU 270 O PRO A 33 5633 5492 2706 2565 -1110 -457 O ATOM 271 CB PRO A 33 40.830 -12.061 3.436 1.00 32.30 C ANISOU 271 CB PRO A 33 5053 3520 3700 1885 -6 -447 C ATOM 272 CG PRO A 33 40.622 -11.683 1.993 1.00 31.58 C ANISOU 272 CG PRO A 33 4794 3660 3545 1995 -570 -1096 C ATOM 273 CD PRO A 33 39.309 -10.950 2.003 1.00 29.15 C ANISOU 273 CD PRO A 33 3745 3758 3571 1141 -316 -1004 C ATOM 274 N ALA A 34 41.889 -8.992 3.882 1.00 28.14 N ANISOU 274 N ALA A 34 3882 3858 2950 1818 259 -511 N ATOM 275 CA ALA A 34 42.977 -8.080 4.262 1.00 28.73 C ANISOU 275 CA ALA A 34 3383 4705 2826 1747 330 -498 C ATOM 276 C ALA A 34 42.442 -6.661 4.121 1.00 23.31 C ANISOU 276 C ALA A 34 2131 4336 2390 951 162 -339 C ATOM 277 O ALA A 34 42.612 -5.919 3.171 1.00 25.15 O ANISOU 277 O ALA A 34 2237 5041 2277 835 -91 -78 O ATOM 278 CB ALA A 34 44.228 -8.355 3.439 1.00 33.06 C ANISOU 278 CB ALA A 34 2995 6900 2664 2189 -447 -2045 C ATOM 279 N GLN A 35 41.716 -6.239 5.164 1.00 22.76 N ANISOU 279 N GLN A 35 2328 4295 2023 1265 -188 -340 N ATOM 280 CA GLN A 35 40.985 -4.991 5.097 1.00 20.03 C ANISOU 280 CA GLN A 35 1889 3981 1739 832 -455 -541 C ATOM 281 C GLN A 35 41.866 -3.773 4.923 1.00 22.32 C ANISOU 281 C GLN A 35 2042 4320 2119 497 -179 -794 C ATOM 282 O GLN A 35 41.510 -2.802 4.278 1.00 24.42 O ANISOU 282 O GLN A 35 2502 3934 2844 571 243 -689 O ATOM 283 CB GLN A 35 40.131 -4.856 6.373 1.00 20.60 C ANISOU 283 CB GLN A 35 3219 2978 1629 1210 -15 80 C ATOM 284 CG GLN A 35 39.005 -5.887 6.364 1.00 25.74 C ANISOU 284 CG GLN A 35 3736 4359 1683 289 337 88 C ATOM 285 CD GLN A 35 38.189 -5.873 7.630 1.00 27.19 C ANISOU 285 CD GLN A 35 3589 5282 1460 632 127 333 C ATOM 286 OE1 GLN A 35 38.723 -5.757 8.742 1.00 31.02 O ANISOU 286 OE1 GLN A 35 4004 6238 1545 1695 -182 442 O ATOM 287 NE2 GLN A 35 36.879 -6.004 7.459 1.00 28.51 N ANISOU 287 NE2 GLN A 35 3469 5369 1992 1085 192 594 N ATOM 288 N ARG A 36 43.053 -3.736 5.527 1.00 27.13 N ANISOU 288 N ARG A 36 1631 5177 3499 699 -127 -1439 N ATOM 289 CA ARG A 36 43.822 -2.516 5.430 1.00 31.26 C ANISOU 289 CA ARG A 36 2478 6192 3209 -369 -308 -1189 C ATOM 290 C ARG A 36 44.436 -2.377 4.034 1.00 32.26 C ANISOU 290 C ARG A 36 2976 6264 3019 -601 -428 -1525 C ATOM 291 O ARG A 36 44.558 -1.260 3.519 1.00 31.31 O ANISOU 291 O ARG A 36 2681 6354 2859 -173 69 -1472 O ATOM 292 CB ARG A 36 44.905 -2.491 6.524 1.00 30.74 C ANISOU 292 CB ARG A 36 2455 6202 3024 -218 -271 -1020 C ATOM 293 CG ARG A 36 44.389 -2.743 7.933 1.00 36.01 C ANISOU 293 CG ARG A 36 4029 6900 2752 -91 245 -2155 C ATOM 294 CD ARG A 36 43.404 -1.676 8.381 1.00 38.92 C ANISOU 294 CD ARG A 36 5321 5963 3504 78 429 -1990 C ATOM 295 NE ARG A 36 43.987 -0.352 8.389 1.00 46.75 N ANISOU 295 NE ARG A 36 7426 6132 4207 -643 -24 -1008 N ATOM 296 CZ ARG A 36 44.245 0.461 9.406 1.00 47.24 C ANISOU 296 CZ ARG A 36 7981 6288 3679 -2769 -966 83 C ATOM 297 NH1 ARG A 36 44.018 0.225 10.697 1.00 24.22 N ANISOU 297 NH1 ARG A 36 2661 2685 3856 191 -783 163 N ATOM 298 NH2 ARG A 36 44.786 1.632 9.085 1.00 31.36 N ANISOU 298 NH2 ARG A 36 3939 4466 3512 759 361 555 N ATOM 299 N ASP A 37 44.807 -3.517 3.434 1.00 31.86 N ANISOU 299 N ASP A 37 2520 6529 3055 526 -949 -1317 N ATOM 300 CA ASP A 37 45.235 -3.620 2.048 1.00 32.28 C ANISOU 300 CA ASP A 37 2718 6377 3171 1026 -677 -1065 C ATOM 301 C ASP A 37 44.132 -3.110 1.124 1.00 27.30 C ANISOU 301 C ASP A 37 2239 5277 2855 811 28 -522 C ATOM 302 O ASP A 37 44.230 -2.320 0.177 1.00 27.97 O ANISOU 302 O ASP A 37 2595 4345 3689 638 351 -450 O ATOM 303 CB ASP A 37 45.597 -5.090 1.747 1.00 31.22 C ANISOU 303 CB ASP A 37 2717 6371 2775 1550 -200 -289 C ATOM 304 CG ASP A 37 46.207 -5.378 0.412 1.00 37.07 C ANISOU 304 CG ASP A 37 5098 5554 3433 1042 1231 -35 C ATOM 305 OD1 ASP A 37 47.339 -4.878 0.215 1.00 54.88 O ANISOU 305 OD1 ASP A 37 7925 5868 7058 -1213 4268 -287 O ATOM 306 OD2 ASP A 37 45.624 -6.114 -0.435 1.00 54.99 O ANISOU 306 OD2 ASP A 37 10086 6615 4192 -1246 2606 -1795 O ATOM 307 N PHE A 38 42.940 -3.600 1.461 1.00 25.14 N ANISOU 307 N PHE A 38 2346 5067 2137 793 72 -545 N ATOM 308 CA PHE A 38 41.774 -3.187 0.708 1.00 23.46 C ANISOU 308 CA PHE A 38 2329 4274 2309 505 -61 -562 C ATOM 309 C PHE A 38 41.554 -1.693 0.780 1.00 23.41 C ANISOU 309 C PHE A 38 2348 4247 2298 314 133 -636 C ATOM 310 O PHE A 38 41.260 -1.048 -0.224 1.00 23.58 O ANISOU 310 O PHE A 38 2281 4232 2447 257 458 -362 O ATOM 311 CB PHE A 38 40.562 -3.948 1.289 1.00 23.12 C ANISOU 311 CB PHE A 38 2379 4117 2290 680 -99 -130 C ATOM 312 CG PHE A 38 39.243 -3.388 0.743 1.00 21.96 C ANISOU 312 CG PHE A 38 2374 4057 1912 544 -75 71 C ATOM 313 CD1 PHE A 38 38.794 -3.764 -0.527 1.00 23.71 C ANISOU 313 CD1 PHE A 38 3148 4349 1514 747 -5 431 C ATOM 314 CD2 PHE A 38 38.471 -2.534 1.487 1.00 22.75 C ANISOU 314 CD2 PHE A 38 2368 4468 1808 802 -85 127 C ATOM 315 CE1 PHE A 38 37.603 -3.269 -1.005 1.00 24.46 C ANISOU 315 CE1 PHE A 38 2855 4547 1890 236 -288 491 C ATOM 316 CE2 PHE A 38 37.301 -1.996 1.020 1.00 23.94 C ANISOU 316 CE2 PHE A 38 2353 4120 2625 574 -421 73 C ATOM 317 CZ PHE A 38 36.879 -2.371 -0.232 1.00 24.28 C ANISOU 317 CZ PHE A 38 1905 4852 2470 116 -310 268 C ATOM 318 N LEU A 39 41.578 -1.092 1.975 1.00 23.85 N ANISOU 318 N LEU A 39 1982 4568 2513 381 122 -911 N ATOM 319 CA LEU A 39 41.362 0.362 2.019 1.00 22.91 C ANISOU 319 CA LEU A 39 1880 4500 2325 329 596 -815 C ATOM 320 C LEU A 39 42.401 1.150 1.258 1.00 26.06 C ANISOU 320 C LEU A 39 2106 5086 2707 -15 539 -635 C ATOM 321 O LEU A 39 42.138 2.166 0.623 1.00 28.08 O ANISOU 321 O LEU A 39 2869 4531 3268 -245 867 -682 O ATOM 322 CB LEU A 39 41.377 0.811 3.482 1.00 23.19 C ANISOU 322 CB LEU A 39 1864 4550 2397 265 263 -834 C ATOM 323 CG LEU A 39 40.214 0.395 4.357 1.00 21.38 C ANISOU 323 CG LEU A 39 1905 4245 1975 539 216 -802 C ATOM 324 CD1 LEU A 39 40.487 0.835 5.797 1.00 26.46 C ANISOU 324 CD1 LEU A 39 2659 5086 2308 -465 267 -1500 C ATOM 325 CD2 LEU A 39 38.904 0.964 3.824 1.00 24.63 C ANISOU 325 CD2 LEU A 39 1724 4349 3284 179 184 126 C ATOM 326 N ALA A 40 43.657 0.674 1.296 1.00 28.61 N ANISOU 326 N ALA A 40 1861 6325 2687 -70 506 -772 N ATOM 327 CA ALA A 40 44.680 1.287 0.450 1.00 31.53 C ANISOU 327 CA ALA A 40 2465 6357 3159 -524 1039 -1214 C ATOM 328 C ALA A 40 44.352 1.206 -1.053 1.00 30.94 C ANISOU 328 C ALA A 40 2615 6162 2981 -211 1448 -1193 C ATOM 329 O ALA A 40 44.486 2.205 -1.769 1.00 35.52 O ANISOU 329 O ALA A 40 2506 7297 3695 -1385 1116 -281 O ATOM 330 CB ALA A 40 46.036 0.646 0.675 1.00 40.06 C ANISOU 330 CB ALA A 40 1845 8591 4785 -824 742 -624 C ATOM 331 N LEU A 41 43.965 0.008 -1.512 1.00 31.06 N ANISOU 331 N LEU A 41 2248 6195 3358 340 696 -1439 N ATOM 332 CA LEU A 41 43.608 -0.246 -2.897 1.00 30.21 C ANISOU 332 CA LEU A 41 2850 5593 3036 81 924 -882 C ATOM 333 C LEU A 41 42.440 0.662 -3.291 1.00 30.98 C ANISOU 333 C LEU A 41 3337 5678 2758 259 912 -641 C ATOM 334 O LEU A 41 42.347 1.166 -4.407 1.00 31.94 O ANISOU 334 O LEU A 41 3149 6393 2593 -146 675 -623 O ATOM 335 CB LEU A 41 43.242 -1.713 -3.151 1.00 32.76 C ANISOU 335 CB LEU A 41 3346 5612 3487 263 1315 -1490 C ATOM 336 CG LEU A 41 44.304 -2.794 -3.285 1.00 36.38 C ANISOU 336 CG LEU A 41 3671 5583 4569 353 2153 -457 C ATOM 337 CD1 LEU A 41 43.693 -4.197 -3.314 1.00 54.62 C ANISOU 337 CD1 LEU A 41 9561 4963 6231 -260 2084 690 C ATOM 338 CD2 LEU A 41 45.158 -2.613 -4.537 1.00 46.09 C ANISOU 338 CD2 LEU A 41 5726 6501 5287 171 3694 -1726 C ATOM 339 N GLN A 42 41.490 0.899 -2.389 1.00 25.96 N ANISOU 339 N GLN A 42 2517 4933 2412 -129 348 -830 N ATOM 340 CA GLN A 42 40.285 1.627 -2.831 1.00 24.72 C ANISOU 340 CA GLN A 42 2680 4325 2389 -430 379 -202 C ATOM 341 C GLN A 42 40.206 3.056 -2.314 1.00 24.92 C ANISOU 341 C GLN A 42 2825 4325 2319 -514 731 -236 C ATOM 342 O GLN A 42 39.111 3.611 -2.383 1.00 28.50 O ANISOU 342 O GLN A 42 2804 4449 3575 -420 1189 -105 O ATOM 343 CB GLN A 42 39.019 0.894 -2.384 1.00 25.03 C ANISOU 343 CB GLN A 42 2536 4179 2797 -295 323 12 C ATOM 344 CG GLN A 42 38.922 -0.506 -2.948 1.00 30.37 C ANISOU 344 CG GLN A 42 3752 4924 2862 -1260 1508 -851 C ATOM 345 CD GLN A 42 38.903 -0.511 -4.465 1.00 28.37 C ANISOU 345 CD GLN A 42 2538 5350 2889 -106 1599 -578 C ATOM 346 OE1 GLN A 42 38.458 0.438 -5.119 1.00 34.43 O ANISOU 346 OE1 GLN A 42 3815 5290 3977 -774 -643 -646 O ATOM 347 NE2 GLN A 42 39.420 -1.620 -4.988 1.00 39.22 N ANISOU 347 NE2 GLN A 42 5622 5652 3629 301 1577 -1439 N ATOM 348 N ALA A 43 41.294 3.642 -1.815 1.00 25.65 N ANISOU 348 N ALA A 43 3129 4371 2246 -886 768 -10 N ATOM 349 CA ALA A 43 41.305 4.989 -1.246 1.00 26.96 C ANISOU 349 CA ALA A 43 3356 4427 2461 -1059 782 -89 C ATOM 350 C ALA A 43 40.739 6.030 -2.197 1.00 26.56 C ANISOU 350 C ALA A 43 3349 4392 2349 -437 1232 -297 C ATOM 351 O ALA A 43 40.041 6.973 -1.820 1.00 31.08 O ANISOU 351 O ALA A 43 3740 4767 3303 -169 1438 -690 O ATOM 352 CB ALA A 43 42.734 5.347 -0.877 1.00 29.01 C ANISOU 352 CB ALA A 43 3405 4513 3105 -1247 642 92 C ATOM 353 N GLU A 44 41.070 5.873 -3.485 1.00 26.29 N ANISOU 353 N GLU A 44 2829 4903 2257 -177 841 -284 N ATOM 354 CA GLU A 44 40.585 6.827 -4.476 1.00 27.28 C ANISOU 354 CA GLU A 44 3130 4793 2444 -244 964 -119 C ATOM 355 C GLU A 44 39.205 6.484 -5.005 1.00 28.50 C ANISOU 355 C GLU A 44 2983 5028 2819 -5 755 372 C ATOM 356 O GLU A 44 38.679 7.257 -5.814 1.00 41.21 O ANISOU 356 O GLU A 44 3895 7565 4198 -765 147 2598 O ATOM 357 CB GLU A 44 41.570 6.893 -5.652 1.00 29.15 C ANISOU 357 CB GLU A 44 3755 4326 2996 -1154 1530 -125 C ATOM 358 CG GLU A 44 42.917 7.503 -5.409 1.00 27.77 C ANISOU 358 CG GLU A 44 3419 3349 3784 -416 1530 -917 C ATOM 359 CD GLU A 44 42.979 8.992 -5.156 1.00 30.88 C ANISOU 359 CD GLU A 44 3937 3318 4479 -50 776 -994 C ATOM 360 OE1 GLU A 44 42.324 9.762 -5.893 1.00 48.33 O ANISOU 360 OE1 GLU A 44 8400 3810 6154 -672 -974 844 O ATOM 361 OE2 GLU A 44 43.692 9.415 -4.221 1.00 39.94 O ANISOU 361 OE2 GLU A 44 4109 3920 7145 -1419 -464 -1030 O ATOM 362 N SER A 45 38.597 5.369 -4.645 1.00 28.42 N ANISOU 362 N SER A 45 2711 5366 2722 -155 684 414 N ATOM 363 CA SER A 45 37.339 4.999 -5.277 1.00 30.80 C ANISOU 363 CA SER A 45 3136 6339 2229 -657 598 447 C ATOM 364 C SER A 45 36.150 5.174 -4.347 1.00 30.40 C ANISOU 364 C SER A 45 2925 5912 2715 -1016 723 249 C ATOM 365 O SER A 45 34.989 5.187 -4.745 1.00 39.64 O ANISOU 365 O SER A 45 3059 9390 2614 -823 649 1050 O ATOM 366 CB SER A 45 37.412 3.546 -5.757 1.00 32.79 C ANISOU 366 CB SER A 45 3417 6613 2431 -796 662 -63 C ATOM 367 OG SER A 45 38.575 3.295 -6.514 1.00 34.87 O ANISOU 367 OG SER A 45 4112 6753 2382 -1218 1261 -265 O ATOM 368 N ILE A 46 36.367 5.282 -3.041 1.00 24.59 N ANISOU 368 N ILE A 46 2588 4075 2679 -83 838 219 N ATOM 369 CA ILE A 46 35.214 5.230 -2.138 1.00 21.49 C ANISOU 369 CA ILE A 46 1880 3639 2644 -176 376 -45 C ATOM 370 C ILE A 46 34.760 6.629 -1.793 1.00 21.47 C ANISOU 370 C ILE A 46 2004 3397 2759 -322 353 107 C ATOM 371 O ILE A 46 35.532 7.439 -1.268 1.00 21.78 O ANISOU 371 O ILE A 46 2099 3348 2827 -403 180 392 O ATOM 372 CB ILE A 46 35.589 4.396 -0.889 1.00 21.84 C ANISOU 372 CB ILE A 46 2164 3458 2675 -23 878 99 C ATOM 373 CG1 ILE A 46 35.798 2.909 -1.190 1.00 23.78 C ANISOU 373 CG1 ILE A 46 2522 3670 2843 435 1035 -146 C ATOM 374 CG2 ILE A 46 34.534 4.609 0.181 1.00 21.54 C ANISOU 374 CG2 ILE A 46 2168 3028 2988 219 977 50 C ATOM 375 CD1 ILE A 46 36.565 2.120 -0.143 1.00 24.64 C ANISOU 375 CD1 ILE A 46 2775 3290 3297 -140 521 31 C ATOM 376 N ARG A 47 33.508 6.944 -2.092 1.00 20.32 N ANISOU 376 N ARG A 47 2071 3100 2549 -344 391 15 N ATOM 377 CA ARG A 47 32.964 8.283 -1.861 1.00 20.74 C ANISOU 377 CA ARG A 47 2564 3147 2170 -102 674 477 C ATOM 378 C ARG A 47 31.896 8.307 -0.784 1.00 18.71 C ANISOU 378 C ARG A 47 2200 2716 2193 -268 448 393 C ATOM 379 O ARG A 47 31.484 9.401 -0.386 1.00 21.04 O ANISOU 379 O ARG A 47 2437 2769 2787 -64 892 514 O ATOM 380 CB ARG A 47 32.431 8.882 -3.181 1.00 22.37 C ANISOU 380 CB ARG A 47 2263 3954 2282 31 592 533 C ATOM 381 CG ARG A 47 33.578 9.230 -4.129 1.00 24.94 C ANISOU 381 CG ARG A 47 3333 3991 2151 -279 1010 588 C ATOM 382 CD ARG A 47 33.031 9.627 -5.482 1.00 28.16 C ANISOU 382 CD ARG A 47 3517 4668 2516 -254 622 887 C ATOM 383 NE ARG A 47 32.335 10.910 -5.450 1.00 28.87 N ANISOU 383 NE ARG A 47 4190 4234 2544 -453 484 947 N ATOM 384 CZ ARG A 47 31.516 11.317 -6.410 1.00 32.13 C ANISOU 384 CZ ARG A 47 5519 4331 2359 41 538 1509 C ATOM 385 NH1 ARG A 47 31.253 10.597 -7.486 1.00 31.26 N ANISOU 385 NH1 ARG A 47 4680 4791 2406 -624 281 1620 N ATOM 386 NH2 ARG A 47 30.947 12.497 -6.262 1.00 44.36 N ANISOU 386 NH2 ARG A 47 8753 4349 3752 1044 76 1853 N ATOM 387 N ALA A 48 31.454 7.148 -0.318 1.00 20.58 N ANISOU 387 N ALA A 48 2656 2714 2450 -499 645 192 N ATOM 388 CA ALA A 48 30.434 6.998 0.717 1.00 17.97 C ANISOU 388 CA ALA A 48 2125 2358 2347 -394 394 225 C ATOM 389 C ALA A 48 30.669 5.760 1.554 1.00 16.98 C ANISOU 389 C ALA A 48 1934 2469 2047 -266 247 42 C ATOM 390 O ALA A 48 31.175 4.775 1.046 1.00 17.62 O ANISOU 390 O ALA A 48 2308 2518 1870 -101 382 183 O ATOM 391 CB ALA A 48 29.038 6.910 0.107 1.00 19.27 C ANISOU 391 CB ALA A 48 2380 2241 2701 -120 37 213 C ATOM 392 N VAL A 49 30.273 5.885 2.811 1.00 16.47 N ANISOU 392 N VAL A 49 2152 2087 2020 -463 243 -118 N ATOM 393 CA VAL A 49 30.254 4.785 3.760 1.00 15.58 C ANISOU 393 CA VAL A 49 1907 2023 1991 -210 315 -172 C ATOM 394 C VAL A 49 28.823 4.612 4.255 1.00 16.72 C ANISOU 394 C VAL A 49 1938 2195 2219 14 483 78 C ATOM 395 O VAL A 49 28.144 5.612 4.550 1.00 17.05 O ANISOU 395 O VAL A 49 2000 2075 2405 17 310 139 O ATOM 396 CB VAL A 49 31.207 5.038 4.928 1.00 15.97 C ANISOU 396 CB VAL A 49 2089 2084 1895 -142 349 -279 C ATOM 397 CG1 VAL A 49 30.880 4.094 6.085 1.00 19.29 C ANISOU 397 CG1 VAL A 49 2461 2867 2001 -147 396 77 C ATOM 398 CG2 VAL A 49 32.668 4.900 4.495 1.00 17.79 C ANISOU 398 CG2 VAL A 49 1946 2787 2027 -276 161 -100 C ATOM 399 N VAL A 50 28.376 3.362 4.321 1.00 14.73 N ANISOU 399 N VAL A 50 1467 2115 2017 128 190 30 N ATOM 400 CA VAL A 50 27.096 3.018 4.944 1.00 14.46 C ANISOU 400 CA VAL A 50 1306 2456 1731 54 -123 122 C ATOM 401 C VAL A 50 27.428 2.203 6.197 1.00 14.72 C ANISOU 401 C VAL A 50 1514 2390 1687 184 -63 44 C ATOM 402 O VAL A 50 28.088 1.162 6.129 1.00 15.35 O ANISOU 402 O VAL A 50 1655 2229 1948 163 84 78 O ATOM 403 CB VAL A 50 26.151 2.283 3.978 1.00 14.35 C ANISOU 403 CB VAL A 50 1702 2132 1618 -52 -16 63 C ATOM 404 CG1 VAL A 50 24.951 1.697 4.666 1.00 15.48 C ANISOU 404 CG1 VAL A 50 1739 2016 2127 -147 -11 198 C ATOM 405 CG2 VAL A 50 25.716 3.216 2.830 1.00 14.94 C ANISOU 405 CG2 VAL A 50 1879 2554 1242 47 -17 -7 C ATOM 406 N GLY A 51 26.984 2.695 7.357 1.00 14.99 N ANISOU 406 N GLY A 51 1987 1957 1753 75 -69 -6 N ATOM 407 CA GLY A 51 27.203 2.106 8.657 1.00 15.92 C ANISOU 407 CA GLY A 51 1780 2610 1658 339 -38 -21 C ATOM 408 C GLY A 51 25.883 1.797 9.319 1.00 16.21 C ANISOU 408 C GLY A 51 1892 2752 1515 163 65 -302 C ATOM 409 O GLY A 51 24.813 2.054 8.786 1.00 16.31 O ANISOU 409 O GLY A 51 1807 2478 1914 124 53 -190 O ATOM 410 N ASN A 52 25.996 1.277 10.527 1.00 17.49 N ANISOU 410 N ASN A 52 2115 2627 1902 453 268 110 N ATOM 411 CA ASN A 52 24.859 1.039 11.401 1.00 18.79 C ANISOU 411 CA ASN A 52 2297 2570 2274 839 701 224 C ATOM 412 C ASN A 52 25.368 1.153 12.841 1.00 21.07 C ANISOU 412 C ASN A 52 3407 2486 2112 618 753 480 C ATOM 413 O ASN A 52 26.414 1.734 13.112 1.00 24.81 O ANISOU 413 O ASN A 52 4290 3047 2091 202 204 -98 O ATOM 414 CB ASN A 52 24.177 -0.283 11.141 1.00 20.34 C ANISOU 414 CB ASN A 52 2107 2857 2763 588 397 542 C ATOM 415 CG ASN A 52 24.924 -1.487 11.676 1.00 17.77 C ANISOU 415 CG ASN A 52 2095 2586 2072 326 431 516 C ATOM 416 OD1 ASN A 52 26.117 -1.401 11.989 1.00 18.22 O ANISOU 416 OD1 ASN A 52 2289 2448 2185 382 0 240 O ATOM 417 ND2 ASN A 52 24.268 -2.612 11.773 1.00 21.06 N ANISOU 417 ND2 ASN A 52 2759 2994 2248 -246 -45 762 N ATOM 418 N SER A 53 24.658 0.597 13.811 1.00 27.38 N ANISOU 418 N SER A 53 4897 2994 2510 974 1918 445 N ATOM 419 CA SER A 53 24.985 0.885 15.219 1.00 31.55 C ANISOU 419 CA SER A 53 5868 3597 2524 -164 2251 83 C ATOM 420 C SER A 53 26.187 0.048 15.669 1.00 31.53 C ANISOU 420 C SER A 53 5637 3814 2529 -947 751 -202 C ATOM 421 O SER A 53 26.763 0.275 16.727 1.00 42.96 O ANISOU 421 O SER A 53 8894 4759 2671 -921 -195 -545 O ATOM 422 CB SER A 53 23.823 0.675 16.184 1.00 44.62 C ANISOU 422 CB SER A 53 6919 6689 3347 -215 3319 -179 C ATOM 423 OG SER A 53 23.089 -0.505 15.945 1.00 63.62 O ANISOU 423 OG SER A 53 8514 11546 4113 -4600 3586 -393 O ATOM 424 N ASN A 54 26.532 -0.914 14.807 1.00 25.26 N ANISOU 424 N ASN A 54 4032 3252 2313 -606 5 194 N ATOM 425 CA ASN A 54 27.637 -1.808 15.152 1.00 28.13 C ANISOU 425 CA ASN A 54 4139 3769 2781 -773 -710 776 C ATOM 426 C ASN A 54 28.960 -1.432 14.485 1.00 25.53 C ANISOU 426 C ASN A 54 3865 3179 2654 -394 -784 614 C ATOM 427 O ASN A 54 30.010 -1.749 15.061 1.00 30.83 O ANISOU 427 O ASN A 54 4060 4305 3349 -719 -1226 1281 O ATOM 428 CB ASN A 54 27.201 -3.236 14.851 1.00 37.12 C ANISOU 428 CB ASN A 54 4892 3144 6068 -846 -2089 2135 C ATOM 429 CG ASN A 54 26.133 -3.764 15.796 1.00 44.38 C ANISOU 429 CG ASN A 54 5742 5305 5814 -2092 -2709 3362 C ATOM 430 OD1 ASN A 54 26.292 -3.936 17.006 1.00 51.50 O ANISOU 430 OD1 ASN A 54 8526 5913 5129 -2213 -2258 1706 O ATOM 431 ND2 ASN A 54 24.952 -4.037 15.250 1.00 57.23 N ANISOU 431 ND2 ASN A 54 5738 8360 7648 -3078 -2867 3626 N ATOM 432 N ALA A 55 28.883 -0.789 13.335 1.00 22.46 N ANISOU 432 N ALA A 55 3284 2879 2369 -261 -674 195 N ATOM 433 CA ALA A 55 30.051 -0.354 12.598 1.00 21.14 C ANISOU 433 CA ALA A 55 3238 2475 2317 382 -345 -10 C ATOM 434 C ALA A 55 29.770 0.951 11.865 1.00 17.88 C ANISOU 434 C ALA A 55 2510 2337 1948 90 -482 -236 C ATOM 435 O ALA A 55 28.847 1.018 11.094 1.00 19.99 O ANISOU 435 O ALA A 55 2388 2672 2536 -307 -624 223 O ATOM 436 CB ALA A 55 30.479 -1.435 11.618 1.00 28.23 C ANISOU 436 CB ALA A 55 5487 2680 2561 1054 -148 -24 C ATOM 437 N GLY A 56 30.554 1.980 12.155 1.00 19.62 N ANISOU 437 N GLY A 56 2424 2595 2437 -3 -536 -288 N ATOM 438 CA GLY A 56 30.389 3.286 11.572 1.00 20.80 C ANISOU 438 CA GLY A 56 2266 2527 3109 -175 93 -69 C ATOM 439 C GLY A 56 31.638 3.759 10.857 1.00 19.49 C ANISOU 439 C GLY A 56 1768 2530 3109 82 -33 -480 C ATOM 440 O GLY A 56 32.158 3.090 9.992 1.00 22.49 O ANISOU 440 O GLY A 56 2702 2579 3262 207 355 -451 O ATOM 441 N ALA A 57 32.089 4.948 11.240 1.00 19.58 N ANISOU 441 N ALA A 57 1832 2430 3176 32 -42 -351 N ATOM 442 CA ALA A 57 33.228 5.577 10.604 1.00 19.56 C ANISOU 442 CA ALA A 57 1883 2892 2656 -217 -106 -715 C ATOM 443 C ALA A 57 33.959 6.397 11.667 1.00 19.81 C ANISOU 443 C ALA A 57 2051 2688 2786 -53 -268 -744 C ATOM 444 O ALA A 57 33.489 7.443 12.061 1.00 21.42 O ANISOU 444 O ALA A 57 2275 2652 3214 -45 -394 -779 O ATOM 445 CB ALA A 57 32.821 6.459 9.429 1.00 21.10 C ANISOU 445 CB ALA A 57 1998 3467 2551 -338 -4 -443 C ATOM 446 N ASP A 58 35.086 5.891 12.138 1.00 21.19 N ANISOU 446 N ASP A 58 1998 3207 2848 73 -304 -915 N ATOM 447 CA ASP A 58 35.881 6.590 13.127 1.00 20.65 C ANISOU 447 CA ASP A 58 2390 2892 2567 -101 -420 -457 C ATOM 448 C ASP A 58 36.951 7.430 12.406 1.00 21.25 C ANISOU 448 C ASP A 58 2399 2928 2748 -143 -233 -577 C ATOM 449 O ASP A 58 37.006 7.408 11.179 1.00 21.83 O ANISOU 449 O ASP A 58 2094 3399 2801 -173 299 -1196 O ATOM 450 CB ASP A 58 36.510 5.643 14.129 1.00 21.89 C ANISOU 450 CB ASP A 58 2269 3341 2709 310 -168 -255 C ATOM 451 CG ASP A 58 37.494 4.661 13.573 1.00 25.60 C ANISOU 451 CG ASP A 58 3070 3561 3097 677 305 -141 C ATOM 452 OD1 ASP A 58 37.980 4.837 12.447 1.00 26.24 O ANISOU 452 OD1 ASP A 58 2425 4740 2806 312 -69 -559 O ATOM 453 OD2 ASP A 58 37.793 3.697 14.307 1.00 28.22 O ANISOU 453 OD2 ASP A 58 2983 3494 4247 669 324 219 O ATOM 454 N ALA A 59 37.767 8.141 13.189 1.00 23.93 N ANISOU 454 N ALA A 59 2674 3409 3010 -458 -463 -545 N ATOM 455 CA ALA A 59 38.709 9.069 12.567 1.00 25.00 C ANISOU 455 CA ALA A 59 2746 3478 3276 -623 -228 -915 C ATOM 456 C ALA A 59 39.676 8.386 11.621 1.00 24.81 C ANISOU 456 C ALA A 59 2554 3776 3095 -570 -434 -1007 C ATOM 457 O ALA A 59 40.060 8.928 10.566 1.00 26.43 O ANISOU 457 O ALA A 59 3029 3774 3238 -565 -155 -937 O ATOM 458 CB ALA A 59 39.447 9.800 13.678 1.00 30.93 C ANISOU 458 CB ALA A 59 2521 5333 3899 -1129 203 -2086 C ATOM 459 N GLU A 60 40.070 7.174 12.031 1.00 25.97 N ANISOU 459 N GLU A 60 2315 4109 3444 -282 -85 -662 N ATOM 460 CA GLU A 60 41.078 6.482 11.226 1.00 25.64 C ANISOU 460 CA GLU A 60 2151 4394 3195 -223 -281 -767 C ATOM 461 C GLU A 60 40.522 6.060 9.873 1.00 23.28 C ANISOU 461 C GLU A 60 2474 3502 2870 -700 -239 -71 C ATOM 462 O GLU A 60 41.157 6.094 8.820 1.00 24.27 O ANISOU 462 O GLU A 60 2155 3905 3161 -211 -18 -526 O ATOM 463 CB GLU A 60 41.591 5.242 11.970 1.00 29.50 C ANISOU 463 CB GLU A 60 3083 5221 2904 678 -747 -867 C ATOM 464 CG GLU A 60 42.880 4.659 11.408 1.00 43.06 C ANISOU 464 CG GLU A 60 4752 5417 6190 1831 406 -1623 C ATOM 465 CD GLU A 60 43.422 3.393 11.993 1.00 46.18 C ANISOU 465 CD GLU A 60 4984 6491 6072 2113 519 -521 C ATOM 466 OE1 GLU A 60 43.035 2.823 13.051 1.00 60.73 O ANISOU 466 OE1 GLU A 60 8888 8073 6114 -4559 -2405 115 O ATOM 467 OE2 GLU A 60 44.377 2.814 11.388 1.00 60.91 O ANISOU 467 OE2 GLU A 60 5432 7206 10506 3263 -1192 -4593 O ATOM 468 N LEU A 61 39.256 5.640 9.872 1.00 21.58 N ANISOU 468 N LEU A 61 2091 3188 2920 -84 -59 -804 N ATOM 469 CA LEU A 61 38.658 5.263 8.611 1.00 20.27 C ANISOU 469 CA LEU A 61 1915 3346 2442 -233 324 -625 C ATOM 470 C LEU A 61 38.488 6.475 7.719 1.00 21.80 C ANISOU 470 C LEU A 61 2541 3004 2738 -689 0 -715 C ATOM 471 O LEU A 61 38.702 6.420 6.512 1.00 21.17 O ANISOU 471 O LEU A 61 2017 3291 2734 -548 227 -411 O ATOM 472 CB LEU A 61 37.302 4.592 8.856 1.00 19.41 C ANISOU 472 CB LEU A 61 2043 2924 2407 -212 281 -762 C ATOM 473 CG LEU A 61 36.621 4.092 7.576 1.00 20.51 C ANISOU 473 CG LEU A 61 2077 3277 2439 -272 596 -1310 C ATOM 474 CD1 LEU A 61 37.351 2.840 7.085 1.00 20.01 C ANISOU 474 CD1 LEU A 61 2576 2827 2200 39 182 -673 C ATOM 475 CD2 LEU A 61 35.132 3.847 7.753 1.00 23.22 C ANISOU 475 CD2 LEU A 61 1977 3702 3143 -274 135 -641 C ATOM 476 N ILE A 62 38.074 7.588 8.296 1.00 22.11 N ANISOU 476 N ILE A 62 2216 3334 2852 -216 -154 -698 N ATOM 477 CA ILE A 62 37.844 8.804 7.503 1.00 21.49 C ANISOU 477 CA ILE A 62 1565 3392 3207 -52 -69 -582 C ATOM 478 C ILE A 62 39.152 9.232 6.862 1.00 22.45 C ANISOU 478 C ILE A 62 1914 3363 3252 -543 114 -1033 C ATOM 479 O ILE A 62 39.157 9.591 5.685 1.00 25.19 O ANISOU 479 O ILE A 62 2187 3519 3864 -484 95 7 O ATOM 480 CB ILE A 62 37.186 9.863 8.426 1.00 23.63 C ANISOU 480 CB ILE A 62 2191 3465 3324 -74 298 -554 C ATOM 481 CG1 ILE A 62 35.782 9.461 8.855 1.00 24.39 C ANISOU 481 CG1 ILE A 62 2364 3466 3437 -526 553 -1448 C ATOM 482 CG2 ILE A 62 37.231 11.256 7.821 1.00 25.25 C ANISOU 482 CG2 ILE A 62 2129 3132 4333 -339 -229 -742 C ATOM 483 CD1 ILE A 62 35.187 10.196 10.042 1.00 21.90 C ANISOU 483 CD1 ILE A 62 2878 2573 2870 -178 517 -639 C ATOM 484 N ASP A 63 40.233 9.168 7.642 1.00 24.97 N ANISOU 484 N ASP A 63 1681 4419 3386 -685 217 -923 N ATOM 485 CA ASP A 63 41.569 9.532 7.169 1.00 24.47 C ANISOU 485 CA ASP A 63 1553 3618 4128 128 509 -263 C ATOM 486 C ASP A 63 41.991 8.591 6.060 1.00 26.82 C ANISOU 486 C ASP A 63 1760 3963 4469 -591 766 -724 C ATOM 487 O ASP A 63 42.731 8.961 5.146 1.00 31.66 O ANISOU 487 O ASP A 63 3164 4540 4325 -1454 1211 -1198 O ATOM 488 CB ASP A 63 42.590 9.506 8.317 1.00 28.01 C ANISOU 488 CB ASP A 63 1438 4496 4709 -320 211 -750 C ATOM 489 CG ASP A 63 42.627 10.693 9.249 1.00 39.88 C ANISOU 489 CG ASP A 63 4275 5446 5431 -1458 399 -1627 C ATOM 490 OD1 ASP A 63 42.164 11.808 8.876 1.00 43.38 O ANISOU 490 OD1 ASP A 63 5453 4280 6749 -1905 1610 -1753 O ATOM 491 OD2 ASP A 63 43.160 10.597 10.395 1.00 45.36 O ANISOU 491 OD2 ASP A 63 3365 8513 5358 -2133 536 -2217 O ATOM 492 N ALA A 64 41.507 7.339 6.149 1.00 25.67 N ANISOU 492 N ALA A 64 2282 3874 3597 -536 49 -395 N ATOM 493 CA ALA A 64 41.895 6.361 5.132 1.00 24.94 C ANISOU 493 CA ALA A 64 2235 3906 3334 -933 284 -361 C ATOM 494 C ALA A 64 41.131 6.478 3.821 1.00 24.16 C ANISOU 494 C ALA A 64 2510 3539 3132 -540 451 140 C ATOM 495 O ALA A 64 41.460 5.813 2.821 1.00 24.42 O ANISOU 495 O ALA A 64 2302 4130 2846 -313 605 282 O ATOM 496 CB ALA A 64 41.746 4.953 5.698 1.00 23.50 C ANISOU 496 CB ALA A 64 2581 3936 2410 -276 136 -337 C ATOM 497 N LEU A 65 40.108 7.312 3.802 1.00 24.54 N ANISOU 497 N LEU A 65 2066 3834 3426 -714 614 -161 N ATOM 498 CA LEU A 65 39.168 7.485 2.703 1.00 21.75 C ANISOU 498 CA LEU A 65 1924 3181 3158 -420 759 -621 C ATOM 499 C LEU A 65 39.130 8.952 2.277 1.00 23.14 C ANISOU 499 C LEU A 65 2118 3195 3478 -604 663 -512 C ATOM 500 O LEU A 65 38.199 9.718 2.533 1.00 24.39 O ANISOU 500 O LEU A 65 2103 3065 4098 -539 722 -312 O ATOM 501 CB LEU A 65 37.760 7.008 3.067 1.00 21.85 C ANISOU 501 CB LEU A 65 1992 3354 2958 -516 697 -263 C ATOM 502 CG LEU A 65 37.622 5.551 3.449 1.00 21.30 C ANISOU 502 CG LEU A 65 2095 3485 2512 -418 370 30 C ATOM 503 CD1 LEU A 65 36.175 5.232 3.795 1.00 22.85 C ANISOU 503 CD1 LEU A 65 2205 3227 3250 -462 573 163 C ATOM 504 CD2 LEU A 65 38.100 4.646 2.314 1.00 22.29 C ANISOU 504 CD2 LEU A 65 2497 3283 2689 -66 325 68 C ATOM 505 N PRO A 66 40.221 9.363 1.637 1.00 24.35 N ANISOU 505 N PRO A 66 2117 3670 3464 -448 635 -24 N ATOM 506 CA PRO A 66 40.371 10.796 1.343 1.00 26.87 C ANISOU 506 CA PRO A 66 1866 3755 4588 -666 793 71 C ATOM 507 C PRO A 66 39.324 11.344 0.393 1.00 27.54 C ANISOU 507 C PRO A 66 2612 3459 4392 -706 660 404 C ATOM 508 O PRO A 66 39.088 12.552 0.332 1.00 30.52 O ANISOU 508 O PRO A 66 3741 3434 4423 -559 774 454 O ATOM 509 CB PRO A 66 41.765 10.888 0.718 1.00 30.60 C ANISOU 509 CB PRO A 66 2326 3923 5377 -652 1537 -366 C ATOM 510 CG PRO A 66 42.133 9.504 0.291 1.00 28.56 C ANISOU 510 CG PRO A 66 2691 3906 4254 -836 1226 -455 C ATOM 511 CD PRO A 66 41.393 8.582 1.199 1.00 25.98 C ANISOU 511 CD PRO A 66 2244 3937 3690 -447 869 -235 C ATOM 512 N LYS A 67 38.644 10.488 -0.344 1.00 26.75 N ANISOU 512 N LYS A 67 2522 3535 4106 -521 567 462 N ATOM 513 CA LYS A 67 37.577 10.970 -1.235 1.00 26.43 C ANISOU 513 CA LYS A 67 2568 3716 3758 -316 838 588 C ATOM 514 C LYS A 67 36.202 10.820 -0.618 1.00 22.66 C ANISOU 514 C LYS A 67 2514 2671 3426 -268 755 256 C ATOM 515 O LYS A 67 35.215 10.998 -1.310 1.00 22.89 O ANISOU 515 O LYS A 67 2553 2879 3265 -386 826 650 O ATOM 516 CB LYS A 67 37.627 10.193 -2.570 1.00 29.92 C ANISOU 516 CB LYS A 67 3285 4922 3162 -657 1349 751 C ATOM 517 CG LYS A 67 38.969 10.205 -3.253 1.00 33.08 C ANISOU 517 CG LYS A 67 2653 5248 4667 -203 1132 -293 C ATOM 518 CD LYS A 67 39.558 11.617 -3.241 1.00 36.74 C ANISOU 518 CD LYS A 67 3099 6138 4720 -1369 1449 -209 C ATOM 519 CE LYS A 67 40.931 11.662 -3.903 1.00 38.30 C ANISOU 519 CE LYS A 67 3286 6727 4539 -1257 1639 -1230 C ATOM 520 NZ LYS A 67 40.749 12.351 -5.210 1.00 52.32 N ANISOU 520 NZ LYS A 67 7204 7143 5532 -2631 2639 374 N ATOM 521 N LEU A 68 36.126 10.483 0.664 1.00 22.67 N ANISOU 521 N LEU A 68 1924 3330 3361 -481 437 146 N ATOM 522 CA LEU A 68 34.863 10.324 1.383 1.00 19.40 C ANISOU 522 CA LEU A 68 1984 2646 2742 -191 377 -337 C ATOM 523 C LEU A 68 34.043 11.616 1.318 1.00 21.26 C ANISOU 523 C LEU A 68 2302 2358 3419 -351 473 402 C ATOM 524 O LEU A 68 34.585 12.667 1.649 1.00 22.66 O ANISOU 524 O LEU A 68 3213 2394 3004 -628 685 278 O ATOM 525 CB LEU A 68 35.094 9.925 2.835 1.00 21.14 C ANISOU 525 CB LEU A 68 1796 3011 3224 -432 83 445 C ATOM 526 CG LEU A 68 33.843 9.565 3.659 1.00 19.91 C ANISOU 526 CG LEU A 68 1930 2947 2687 -433 192 -194 C ATOM 527 CD1 LEU A 68 33.010 8.472 2.982 1.00 19.74 C ANISOU 527 CD1 LEU A 68 1848 2710 2941 -393 187 -50 C ATOM 528 CD2 LEU A 68 34.259 9.139 5.069 1.00 20.13 C ANISOU 528 CD2 LEU A 68 2264 2529 2855 -324 100 -93 C ATOM 529 N GLU A 69 32.763 11.492 0.952 1.00 22.17 N ANISOU 529 N GLU A 69 2224 2743 3455 -140 437 929 N ATOM 530 CA GLU A 69 31.914 12.668 0.943 1.00 20.85 C ANISOU 530 CA GLU A 69 2353 2387 3182 -379 487 718 C ATOM 531 C GLU A 69 30.729 12.593 1.897 1.00 19.73 C ANISOU 531 C GLU A 69 2477 2044 2976 -569 497 93 C ATOM 532 O GLU A 69 30.216 13.624 2.307 1.00 22.07 O ANISOU 532 O GLU A 69 2587 2132 3665 -129 256 211 O ATOM 533 CB GLU A 69 31.352 12.927 -0.458 1.00 21.67 C ANISOU 533 CB GLU A 69 2376 2718 3138 96 595 724 C ATOM 534 CG GLU A 69 32.403 13.150 -1.516 1.00 25.19 C ANISOU 534 CG GLU A 69 2767 3544 3259 -370 758 896 C ATOM 535 CD GLU A 69 31.872 13.362 -2.917 1.00 25.96 C ANISOU 535 CD GLU A 69 3090 3669 3106 -301 783 539 C ATOM 536 OE1 GLU A 69 30.668 13.572 -3.137 1.00 28.38 O ANISOU 536 OE1 GLU A 69 3236 4130 3415 -244 526 1216 O ATOM 537 OE2 GLU A 69 32.752 13.341 -3.814 1.00 31.67 O ANISOU 537 OE2 GLU A 69 3729 5028 3275 -380 1195 412 O ATOM 538 N ILE A 70 30.310 11.369 2.239 1.00 18.57 N ANISOU 538 N ILE A 70 2124 2129 2802 -441 324 316 N ATOM 539 CA ILE A 70 29.114 11.182 3.019 1.00 17.87 C ANISOU 539 CA ILE A 70 2003 2272 2514 -209 270 345 C ATOM 540 C ILE A 70 29.133 9.832 3.690 1.00 16.83 C ANISOU 540 C ILE A 70 1993 2211 2191 -247 264 220 C ATOM 541 O ILE A 70 29.558 8.823 3.110 1.00 17.53 O ANISOU 541 O ILE A 70 2147 2247 2266 -263 537 268 O ATOM 542 CB ILE A 70 27.831 11.326 2.165 1.00 18.57 C ANISOU 542 CB ILE A 70 2191 2406 2458 -174 151 346 C ATOM 543 CG1 ILE A 70 26.542 11.186 2.971 1.00 19.29 C ANISOU 543 CG1 ILE A 70 1926 2270 3133 125 226 212 C ATOM 544 CG2 ILE A 70 27.811 10.349 1.009 1.00 18.86 C ANISOU 544 CG2 ILE A 70 2106 2305 2754 -301 191 219 C ATOM 545 CD1 ILE A 70 25.275 11.577 2.251 1.00 18.93 C ANISOU 545 CD1 ILE A 70 2288 1941 2965 225 11 190 C ATOM 546 N VAL A 71 28.689 9.844 4.944 1.00 16.83 N ANISOU 546 N VAL A 71 2307 1926 2160 -340 185 -4 N ATOM 547 CA VAL A 71 28.474 8.682 5.775 1.00 15.80 C ANISOU 547 CA VAL A 71 1692 2188 2125 -147 93 260 C ATOM 548 C VAL A 71 26.956 8.657 6.033 1.00 16.24 C ANISOU 548 C VAL A 71 1716 1809 2645 -23 212 -69 C ATOM 549 O VAL A 71 26.448 9.583 6.653 1.00 16.66 O ANISOU 549 O VAL A 71 2055 1921 2352 -31 296 -69 O ATOM 550 CB VAL A 71 29.215 8.723 7.114 1.00 15.57 C ANISOU 550 CB VAL A 71 1880 1893 2142 56 97 -128 C ATOM 551 CG1 VAL A 71 28.832 7.532 8.001 1.00 17.85 C ANISOU 551 CG1 VAL A 71 2690 2164 1930 -183 -179 -6 C ATOM 552 CG2 VAL A 71 30.713 8.813 6.884 1.00 18.83 C ANISOU 552 CG2 VAL A 71 1841 2935 2378 -43 -73 -243 C ATOM 553 N SER A 72 26.322 7.616 5.503 1.00 16.29 N ANISOU 553 N SER A 72 1722 2107 2360 -214 512 -182 N ATOM 554 CA SER A 72 24.913 7.398 5.706 1.00 15.55 C ANISOU 554 CA SER A 72 1772 2025 2111 -175 299 -210 C ATOM 555 C SER A 72 24.689 6.215 6.638 1.00 14.10 C ANISOU 555 C SER A 72 1239 1964 2153 28 218 -77 C ATOM 556 O SER A 72 25.029 5.098 6.267 1.00 17.79 O ANISOU 556 O SER A 72 1940 2054 2765 64 748 -214 O ATOM 557 CB SER A 72 24.135 7.264 4.393 1.00 16.10 C ANISOU 557 CB SER A 72 1959 2152 2007 -175 337 71 C ATOM 558 OG SER A 72 24.126 8.495 3.682 1.00 18.22 O ANISOU 558 OG SER A 72 1936 2300 2688 -39 208 391 O ATOM 559 N SER A 73 24.145 6.502 7.815 1.00 15.48 N ANISOU 559 N SER A 73 1713 1892 2277 62 320 -91 N ATOM 560 CA SER A 73 23.953 5.445 8.790 1.00 15.30 C ANISOU 560 CA SER A 73 1711 2042 2059 -2 241 -167 C ATOM 561 C SER A 73 22.536 4.867 8.767 1.00 14.60 C ANISOU 561 C SER A 73 1647 1893 2006 139 374 -140 C ATOM 562 O SER A 73 21.528 5.600 8.688 1.00 15.89 O ANISOU 562 O SER A 73 1686 2075 2277 245 210 45 O ATOM 563 CB SER A 73 24.317 5.934 10.203 1.00 16.91 C ANISOU 563 CB SER A 73 1893 2347 2184 408 77 -450 C ATOM 564 OG SER A 73 24.673 4.775 10.920 1.00 19.76 O ANISOU 564 OG SER A 73 2305 2806 2395 156 58 181 O ATOM 565 N PHE A 74 22.496 3.535 8.839 1.00 14.68 N ANISOU 565 N PHE A 74 1742 1923 1915 83 188 23 N ATOM 566 CA PHE A 74 21.297 2.742 8.947 1.00 14.10 C ANISOU 566 CA PHE A 74 1714 1913 1732 87 268 -10 C ATOM 567 C PHE A 74 20.967 2.574 10.429 1.00 14.52 C ANISOU 567 C PHE A 74 1608 2076 1833 399 349 35 C ATOM 568 O PHE A 74 21.006 1.472 10.975 1.00 16.27 O ANISOU 568 O PHE A 74 2431 2082 1671 154 199 9 O ATOM 569 CB PHE A 74 21.545 1.425 8.260 1.00 13.68 C ANISOU 569 CB PHE A 74 1535 1893 1771 130 226 53 C ATOM 570 CG PHE A 74 20.417 0.416 8.115 1.00 15.14 C ANISOU 570 CG PHE A 74 1909 1956 1888 -152 -11 301 C ATOM 571 CD1 PHE A 74 19.321 0.653 7.291 1.00 13.68 C ANISOU 571 CD1 PHE A 74 1620 1785 1792 100 187 147 C ATOM 572 CD2 PHE A 74 20.499 -0.805 8.781 1.00 15.02 C ANISOU 572 CD2 PHE A 74 1759 2052 1896 -6 41 327 C ATOM 573 CE1 PHE A 74 18.378 -0.335 7.101 1.00 14.99 C ANISOU 573 CE1 PHE A 74 1740 1700 2256 154 52 72 C ATOM 574 CE2 PHE A 74 19.528 -1.783 8.623 1.00 15.76 C ANISOU 574 CE2 PHE A 74 1953 1788 2249 -1 -94 242 C ATOM 575 CZ PHE A 74 18.465 -1.549 7.758 1.00 13.82 C ANISOU 575 CZ PHE A 74 1513 1772 1965 134 267 110 C ATOM 576 N SER A 75 20.691 3.749 11.035 1.00 15.51 N ANISOU 576 N SER A 75 1806 2187 1898 535 497 26 N ATOM 577 CA SER A 75 20.442 3.832 12.462 1.00 16.57 C ANISOU 577 CA SER A 75 2350 2192 1754 142 73 -210 C ATOM 578 C SER A 75 20.024 5.250 12.811 1.00 16.63 C ANISOU 578 C SER A 75 2398 2213 1708 101 87 -226 C ATOM 579 O SER A 75 20.344 6.173 12.068 1.00 16.93 O ANISOU 579 O SER A 75 2122 2285 2024 16 124 -96 O ATOM 580 CB SER A 75 21.660 3.439 13.285 1.00 19.94 C ANISOU 580 CB SER A 75 2893 2288 2397 343 -697 -964 C ATOM 581 OG SER A 75 22.668 4.398 13.292 1.00 22.35 O ANISOU 581 OG SER A 75 2516 2878 3098 270 -250 -949 O ATOM 582 N VAL A 76 19.377 5.398 13.946 1.00 17.31 N ANISOU 582 N VAL A 76 1976 2333 2267 471 470 -15 N ATOM 583 CA VAL A 76 19.134 6.761 14.437 1.00 17.57 C ANISOU 583 CA VAL A 76 1754 2390 2533 345 612 -198 C ATOM 584 C VAL A 76 20.361 7.173 15.229 1.00 19.25 C ANISOU 584 C VAL A 76 2452 3008 1853 30 257 32 C ATOM 585 O VAL A 76 20.813 8.324 15.133 1.00 20.11 O ANISOU 585 O VAL A 76 2378 2955 2308 23 161 -232 O ATOM 586 CB VAL A 76 17.849 6.903 15.238 1.00 18.61 C ANISOU 586 CB VAL A 76 2443 2341 2285 -85 1077 -434 C ATOM 587 CG1 VAL A 76 17.856 6.050 16.488 1.00 23.17 C ANISOU 587 CG1 VAL A 76 3254 2911 2640 -729 782 -1 C ATOM 588 CG2 VAL A 76 17.637 8.345 15.683 1.00 23.77 C ANISOU 588 CG2 VAL A 76 2691 2582 3758 772 904 -634 C ATOM 589 N GLY A 77 20.953 6.236 15.985 1.00 20.57 N ANISOU 589 N GLY A 77 2595 3262 1960 262 381 56 N ATOM 590 CA GLY A 77 22.150 6.607 16.704 1.00 22.23 C ANISOU 590 CA GLY A 77 2469 3806 2172 580 257 70 C ATOM 591 C GLY A 77 23.368 6.780 15.856 1.00 21.72 C ANISOU 591 C GLY A 77 2577 3630 2046 160 213 -185 C ATOM 592 O GLY A 77 23.564 6.173 14.818 1.00 23.96 O ANISOU 592 O GLY A 77 2493 4424 2187 84 266 -520 O ATOM 593 N LEU A 78 24.247 7.649 16.344 1.00 24.98 N ANISOU 593 N LEU A 78 2723 3174 3594 341 311 -847 N ATOM 594 CA LEU A 78 25.469 7.910 15.607 1.00 22.91 C ANISOU 594 CA LEU A 78 2684 3594 2428 -200 -298 -918 C ATOM 595 C LEU A 78 26.703 7.811 16.474 1.00 23.33 C ANISOU 595 C LEU A 78 2959 2605 3298 -382 -784 -863 C ATOM 596 O LEU A 78 27.727 8.396 16.174 1.00 23.57 O ANISOU 596 O LEU A 78 2803 2926 3225 -284 -553 -1212 O ATOM 597 CB LEU A 78 25.404 9.282 14.948 1.00 27.48 C ANISOU 597 CB LEU A 78 2677 4135 3628 -388 -824 -88 C ATOM 598 CG LEU A 78 24.414 9.402 13.780 1.00 23.32 C ANISOU 598 CG LEU A 78 2402 3528 2929 380 -344 -1083 C ATOM 599 CD1 LEU A 78 24.215 10.868 13.492 1.00 28.29 C ANISOU 599 CD1 LEU A 78 2641 3632 4478 482 -789 -675 C ATOM 600 CD2 LEU A 78 24.908 8.649 12.553 1.00 27.78 C ANISOU 600 CD2 LEU A 78 2792 4196 3569 -498 975 -1352 C ATOM 601 N ASP A 79 26.623 7.028 17.541 1.00 23.44 N ANISOU 601 N ASP A 79 2503 3983 2418 430 -97 -960 N ATOM 602 CA ASP A 79 27.797 6.877 18.399 1.00 23.11 C ANISOU 602 CA ASP A 79 2254 4064 2463 199 -19 -1058 C ATOM 603 C ASP A 79 28.966 6.215 17.668 1.00 23.68 C ANISOU 603 C ASP A 79 2111 4069 2819 -63 -33 -1414 C ATOM 604 O ASP A 79 30.114 6.300 18.181 1.00 30.71 O ANISOU 604 O ASP A 79 2361 5112 4197 686 -641 -2388 O ATOM 605 CB ASP A 79 27.414 6.146 19.701 1.00 24.84 C ANISOU 605 CB ASP A 79 2725 4281 2431 572 -66 -852 C ATOM 606 CG ASP A 79 26.663 4.864 19.420 1.00 25.98 C ANISOU 606 CG ASP A 79 3036 3888 2947 624 -24 -396 C ATOM 607 OD1 ASP A 79 25.449 4.930 19.091 1.00 24.70 O ANISOU 607 OD1 ASP A 79 2818 3953 2614 290 289 -476 O ATOM 608 OD2 ASP A 79 27.332 3.810 19.505 1.00 27.87 O ANISOU 608 OD2 ASP A 79 3723 4124 2743 1018 306 -53 O ATOM 609 N LYS A 80 28.767 5.576 16.521 1.00 21.76 N ANISOU 609 N LYS A 80 2578 3381 2308 -55 157 -829 N ATOM 610 CA LYS A 80 29.893 4.898 15.867 1.00 21.54 C ANISOU 610 CA LYS A 80 2720 3193 2269 124 74 -681 C ATOM 611 C LYS A 80 30.433 5.777 14.747 1.00 18.68 C ANISOU 611 C LYS A 80 2050 3006 2044 385 -223 -668 C ATOM 612 O LYS A 80 31.322 5.380 14.013 1.00 22.40 O ANISOU 612 O LYS A 80 2512 2709 3290 194 592 -691 O ATOM 613 CB LYS A 80 29.450 3.547 15.350 1.00 22.90 C ANISOU 613 CB LYS A 80 2568 3286 2848 -78 378 -826 C ATOM 614 CG LYS A 80 28.994 2.536 16.358 1.00 26.68 C ANISOU 614 CG LYS A 80 3521 3149 3466 266 1215 -701 C ATOM 615 CD LYS A 80 30.136 1.943 17.125 1.00 35.67 C ANISOU 615 CD LYS A 80 5893 3783 3879 -63 -859 -299 C ATOM 616 CE LYS A 80 29.612 0.754 17.940 1.00 45.53 C ANISOU 616 CE LYS A 80 8906 3785 4610 -275 -535 116 C ATOM 617 NZ LYS A 80 30.666 -0.295 18.071 1.00 63.57 N ANISOU 617 NZ LYS A 80 10298 6340 7515 1048 -2681 2658 N ATOM 618 N VAL A 81 29.876 6.997 14.649 1.00 20.65 N ANISOU 618 N VAL A 81 2351 2746 2747 232 -122 -881 N ATOM 619 CA VAL A 81 30.444 7.930 13.676 1.00 20.74 C ANISOU 619 CA VAL A 81 2214 2627 3039 -27 -255 -851 C ATOM 620 C VAL A 81 31.125 9.111 14.346 1.00 21.49 C ANISOU 620 C VAL A 81 2029 3071 3067 -32 -159 -1226 C ATOM 621 O VAL A 81 30.544 9.719 15.272 1.00 21.54 O ANISOU 621 O VAL A 81 2604 3051 2530 146 -101 -863 O ATOM 622 CB VAL A 81 29.343 8.431 12.737 1.00 21.73 C ANISOU 622 CB VAL A 81 2332 2991 2933 -375 -377 -593 C ATOM 623 CG1 VAL A 81 29.943 9.365 11.709 1.00 22.29 C ANISOU 623 CG1 VAL A 81 2824 2609 3035 259 345 -706 C ATOM 624 CG2 VAL A 81 28.692 7.214 12.081 1.00 23.33 C ANISOU 624 CG2 VAL A 81 1973 3167 3725 -202 -348 -1044 C ATOM 625 N ASP A 82 32.342 9.430 13.895 1.00 21.44 N ANISOU 625 N ASP A 82 2248 2881 3018 -191 -108 -812 N ATOM 626 CA ASP A 82 33.045 10.594 14.487 1.00 21.51 C ANISOU 626 CA ASP A 82 2428 3046 2699 -336 162 -896 C ATOM 627 C ASP A 82 32.559 11.871 13.796 1.00 24.32 C ANISOU 627 C ASP A 82 2896 2840 3505 -171 237 -941 C ATOM 628 O ASP A 82 33.056 12.277 12.755 1.00 23.37 O ANISOU 628 O ASP A 82 2905 2404 3570 -250 123 -759 O ATOM 629 CB ASP A 82 34.548 10.417 14.371 1.00 22.15 C ANISOU 629 CB ASP A 82 2389 3103 2926 -439 140 -1134 C ATOM 630 CG ASP A 82 35.328 11.470 15.130 1.00 24.44 C ANISOU 630 CG ASP A 82 2774 3060 3453 -174 -691 -1125 C ATOM 631 OD1 ASP A 82 34.749 12.552 15.387 1.00 27.13 O ANISOU 631 OD1 ASP A 82 3566 2758 3983 -172 -464 -1045 O ATOM 632 OD2 ASP A 82 36.530 11.239 15.425 1.00 30.97 O ANISOU 632 OD2 ASP A 82 2832 4868 4069 92 -943 -1851 O ATOM 633 N LEU A 83 31.533 12.444 14.401 1.00 24.36 N ANISOU 633 N LEU A 83 2604 3438 3214 5 -280 -1299 N ATOM 634 CA LEU A 83 30.877 13.618 13.839 1.00 24.02 C ANISOU 634 CA LEU A 83 2701 3168 3259 -93 164 -1211 C ATOM 635 C LEU A 83 31.854 14.788 13.769 1.00 27.89 C ANISOU 635 C LEU A 83 2917 3997 3684 -653 -299 -470 C ATOM 636 O LEU A 83 31.863 15.597 12.832 1.00 27.87 O ANISOU 636 O LEU A 83 3949 3231 3409 -282 -86 -920 O ATOM 637 CB LEU A 83 29.633 13.953 14.656 1.00 24.27 C ANISOU 637 CB LEU A 83 3196 2545 3481 -82 583 -1249 C ATOM 638 CG LEU A 83 28.532 12.896 14.630 1.00 22.18 C ANISOU 638 CG LEU A 83 3083 2622 2721 -98 492 -858 C ATOM 639 CD1 LEU A 83 27.344 13.404 15.443 1.00 27.69 C ANISOU 639 CD1 LEU A 83 3610 3483 3427 -198 1150 -1183 C ATOM 640 CD2 LEU A 83 28.126 12.483 13.208 1.00 23.03 C ANISOU 640 CD2 LEU A 83 3067 2836 2847 223 162 -877 C ATOM 641 N ILE A 84 32.696 14.863 14.799 1.00 25.39 N ANISOU 641 N ILE A 84 2849 3131 3668 -56 -263 -1093 N ATOM 642 CA ILE A 84 33.598 16.025 14.884 1.00 30.63 C ANISOU 642 CA ILE A 84 3588 3773 4278 -716 350 -2175 C ATOM 643 C ILE A 84 34.537 15.982 13.693 1.00 26.61 C ANISOU 643 C ILE A 84 3050 3265 3795 -450 -175 -1486 C ATOM 644 O ILE A 84 34.794 16.940 12.980 1.00 29.67 O ANISOU 644 O ILE A 84 3000 3378 4897 -841 -299 -1093 O ATOM 645 CB ILE A 84 34.343 16.019 16.225 1.00 36.77 C ANISOU 645 CB ILE A 84 5474 4650 3848 -2415 215 -1933 C ATOM 646 CG1 ILE A 84 33.367 16.118 17.401 1.00 44.92 C ANISOU 646 CG1 ILE A 84 6257 6455 4354 -3334 827 -2778 C ATOM 647 CG2 ILE A 84 35.378 17.126 16.255 1.00 34.03 C ANISOU 647 CG2 ILE A 84 5252 3773 3904 -1856 -251 -1217 C ATOM 648 CD1 ILE A 84 33.955 15.954 18.783 1.00 47.48 C ANISOU 648 CD1 ILE A 84 4090 9757 4194 -2421 1439 -3163 C ATOM 649 N LYS A 85 35.037 14.758 13.479 1.00 27.24 N ANISOU 649 N LYS A 85 3212 3216 3921 -559 7 -1728 N ATOM 650 CA LYS A 85 35.952 14.528 12.372 1.00 24.98 C ANISOU 650 CA LYS A 85 2804 2818 3870 -730 4 -1188 C ATOM 651 C LYS A 85 35.286 14.742 11.030 1.00 25.24 C ANISOU 651 C LYS A 85 2881 2797 3913 -1077 5 -793 C ATOM 652 O LYS A 85 35.859 15.356 10.113 1.00 25.71 O ANISOU 652 O LYS A 85 2999 2847 3922 -837 609 -1120 O ATOM 653 CB LYS A 85 36.547 13.115 12.501 1.00 25.97 C ANISOU 653 CB LYS A 85 3333 3070 3465 -426 1076 -450 C ATOM 654 CG LYS A 85 37.507 12.878 11.341 1.00 26.17 C ANISOU 654 CG LYS A 85 2219 4069 3654 -512 740 -612 C ATOM 655 CD LYS A 85 38.887 13.426 11.677 1.00 29.90 C ANISOU 655 CD LYS A 85 2267 4373 4720 -288 -152 -179 C ATOM 656 CE LYS A 85 39.953 12.651 10.897 1.00 32.68 C ANISOU 656 CE LYS A 85 1939 5294 5183 -784 222 -765 C ATOM 657 NZ LYS A 85 41.228 13.435 10.796 1.00 48.79 N ANISOU 657 NZ LYS A 85 2603 7611 8322 -2027 896 -1670 N ATOM 658 N CYS A 86 34.061 14.288 10.832 1.00 24.23 N ANISOU 658 N CYS A 86 2908 3033 3266 -1086 223 -1358 N ATOM 659 CA CYS A 86 33.330 14.501 9.582 1.00 24.70 C ANISOU 659 CA CYS A 86 3143 2684 3559 -763 -52 -1401 C ATOM 660 C CYS A 86 33.158 15.976 9.272 1.00 27.40 C ANISOU 660 C CYS A 86 3943 2697 3770 -914 -244 -1458 C ATOM 661 O CYS A 86 33.364 16.426 8.144 1.00 27.38 O ANISOU 661 O CYS A 86 2920 2753 4730 -1236 1088 -926 O ATOM 662 CB CYS A 86 31.948 13.797 9.657 1.00 23.60 C ANISOU 662 CB CYS A 86 2645 2576 3745 -270 -16 -1166 C ATOM 663 SG CYS A 86 32.095 12.009 9.478 1.00 22.16 S ANISOU 663 SG CYS A 86 2601 2453 3366 -441 198 -784 S ATOM 664 N GLU A 87 32.764 16.714 10.321 1.00 29.27 N ANISOU 664 N GLU A 87 4284 2614 4223 -841 -13 -1666 N ATOM 665 CA GLU A 87 32.584 18.158 10.148 1.00 28.61 C ANISOU 665 CA GLU A 87 4158 2724 3987 -718 -672 -1533 C ATOM 666 C GLU A 87 33.914 18.775 9.733 1.00 32.87 C ANISOU 666 C GLU A 87 4526 2887 5077 -820 -418 -668 C ATOM 667 O GLU A 87 33.967 19.587 8.802 1.00 35.54 O ANISOU 667 O GLU A 87 5384 2588 5531 -1046 -757 -530 O ATOM 668 CB GLU A 87 32.012 18.766 11.427 1.00 31.62 C ANISOU 668 CB GLU A 87 5392 2491 4133 -44 -356 -1308 C ATOM 669 CG GLU A 87 31.469 20.182 11.335 1.00 33.98 C ANISOU 669 CG GLU A 87 5546 2886 4478 475 -1688 -1524 C ATOM 670 CD GLU A 87 32.529 21.269 11.361 1.00 32.99 C ANISOU 670 CD GLU A 87 5762 2131 4642 741 -733 -1174 C ATOM 671 OE1 GLU A 87 33.655 20.980 11.841 1.00 34.51 O ANISOU 671 OE1 GLU A 87 4407 2964 5740 32 548 533 O ATOM 672 OE2 GLU A 87 32.241 22.375 10.875 1.00 35.88 O ANISOU 672 OE2 GLU A 87 7420 2720 3492 1153 -378 -766 O ATOM 673 N GLU A 88 34.975 18.404 10.449 1.00 29.08 N ANISOU 673 N GLU A 88 3834 2821 4394 -639 325 -975 N ATOM 674 CA GLU A 88 36.313 18.911 10.145 1.00 30.67 C ANISOU 674 CA GLU A 88 4362 2954 4335 -1236 211 -111 C ATOM 675 C GLU A 88 36.693 18.642 8.694 1.00 32.06 C ANISOU 675 C GLU A 88 4495 3065 4623 -1397 578 -368 C ATOM 676 O GLU A 88 37.343 19.470 8.067 1.00 37.46 O ANISOU 676 O GLU A 88 5939 4021 4271 -2631 427 -452 O ATOM 677 CB GLU A 88 37.315 18.280 11.114 1.00 40.34 C ANISOU 677 CB GLU A 88 4239 5390 5699 -2411 -763 1257 C ATOM 678 CG GLU A 88 38.725 18.068 10.625 1.00 46.74 C ANISOU 678 CG GLU A 88 4768 5500 7492 -592 -619 685 C ATOM 679 CD GLU A 88 39.558 17.177 11.533 1.00 54.69 C ANISOU 679 CD GLU A 88 5497 6443 8839 -1252 -1726 1745 C ATOM 680 OE1 GLU A 88 39.172 17.003 12.715 1.00 62.94 O ANISOU 680 OE1 GLU A 88 6457 8760 8699 -3596 -2424 2656 O ATOM 681 OE2 GLU A 88 40.591 16.663 11.036 1.00 60.05 O ANISOU 681 OE2 GLU A 88 3918 7060 11838 -1237 -2273 2231 O ATOM 682 N LYS A 89 36.314 17.509 8.112 1.00 29.30 N ANISOU 682 N LYS A 89 3627 3505 4001 -1563 -585 -77 N ATOM 683 CA LYS A 89 36.684 17.131 6.755 1.00 32.52 C ANISOU 683 CA LYS A 89 4436 3850 4070 -2282 -172 -260 C ATOM 684 C LYS A 89 35.637 17.496 5.711 1.00 31.47 C ANISOU 684 C LYS A 89 4296 4246 3417 -1769 350 -347 C ATOM 685 O LYS A 89 35.838 17.180 4.529 1.00 33.04 O ANISOU 685 O LYS A 89 4982 4258 3314 -1912 756 22 O ATOM 686 CB LYS A 89 36.892 15.608 6.637 1.00 33.49 C ANISOU 686 CB LYS A 89 3598 4125 5004 -1647 162 -686 C ATOM 687 CG LYS A 89 38.190 15.118 7.283 1.00 35.04 C ANISOU 687 CG LYS A 89 2943 4524 5849 -2259 331 -41 C ATOM 688 CD LYS A 89 39.362 15.464 6.361 1.00 36.44 C ANISOU 688 CD LYS A 89 3623 4539 5683 -2528 801 -720 C ATOM 689 CE LYS A 89 40.670 15.203 7.088 1.00 38.67 C ANISOU 689 CE LYS A 89 3053 4951 6686 -1787 1082 -1646 C ATOM 690 NZ LYS A 89 41.864 15.338 6.220 1.00 47.45 N ANISOU 690 NZ LYS A 89 3781 6345 7903 -2633 1994 -2676 N ATOM 691 N GLY A 90 34.515 18.135 6.031 1.00 30.89 N ANISOU 691 N GLY A 90 3743 4165 3827 -2370 941 261 N ATOM 692 CA GLY A 90 33.557 18.399 4.968 1.00 32.90 C ANISOU 692 CA GLY A 90 4578 3030 4894 -1785 177 188 C ATOM 693 C GLY A 90 32.759 17.167 4.576 1.00 29.56 C ANISOU 693 C GLY A 90 4552 2825 3854 -1511 305 -93 C ATOM 694 O GLY A 90 32.214 17.178 3.465 1.00 31.64 O ANISOU 694 O GLY A 90 5062 3085 3875 -869 130 -158 O ATOM 695 N VAL A 91 32.688 16.157 5.459 1.00 24.33 N ANISOU 695 N VAL A 91 3098 2317 3829 -773 370 -416 N ATOM 696 CA VAL A 91 31.937 14.951 5.186 1.00 22.01 C ANISOU 696 CA VAL A 91 2646 2249 3469 -588 337 -205 C ATOM 697 C VAL A 91 30.532 15.063 5.753 1.00 21.73 C ANISOU 697 C VAL A 91 2748 1915 3592 -352 373 -651 C ATOM 698 O VAL A 91 30.410 15.393 6.929 1.00 23.30 O ANISOU 698 O VAL A 91 2920 2498 3433 -450 415 -368 O ATOM 699 CB VAL A 91 32.688 13.727 5.745 1.00 22.45 C ANISOU 699 CB VAL A 91 2308 2388 3834 -548 487 -89 C ATOM 700 CG1 VAL A 91 31.849 12.477 5.530 1.00 19.91 C ANISOU 700 CG1 VAL A 91 2124 2301 3139 -377 -5 42 C ATOM 701 CG2 VAL A 91 34.064 13.567 5.094 1.00 28.40 C ANISOU 701 CG2 VAL A 91 2016 3822 4951 -572 448 -190 C ATOM 702 N ARG A 92 29.514 14.784 4.936 1.00 21.59 N ANISOU 702 N ARG A 92 2591 2223 3390 -335 295 112 N ATOM 703 CA ARG A 92 28.118 14.825 5.368 1.00 21.68 C ANISOU 703 CA ARG A 92 2669 2179 3392 -111 416 246 C ATOM 704 C ARG A 92 27.789 13.542 6.121 1.00 21.14 C ANISOU 704 C ARG A 92 3089 2134 2807 -156 643 2 C ATOM 705 O ARG A 92 28.356 12.471 5.847 1.00 22.84 O ANISOU 705 O ARG A 92 2541 1940 4196 -447 990 -118 O ATOM 706 CB ARG A 92 27.122 14.992 4.225 1.00 23.72 C ANISOU 706 CB ARG A 92 2619 2735 3660 -193 319 642 C ATOM 707 CG ARG A 92 27.276 16.194 3.313 1.00 25.97 C ANISOU 707 CG ARG A 92 3367 2596 3903 394 585 708 C ATOM 708 CD ARG A 92 27.320 17.522 4.050 1.00 28.46 C ANISOU 708 CD ARG A 92 3597 2584 4634 439 630 527 C ATOM 709 NE ARG A 92 26.132 17.804 4.862 1.00 30.28 N ANISOU 709 NE ARG A 92 4047 2526 4932 527 1024 512 N ATOM 710 CZ ARG A 92 24.964 18.239 4.379 1.00 27.61 C ANISOU 710 CZ ARG A 92 3801 2079 4610 376 1496 893 C ATOM 711 NH1 ARG A 92 24.774 18.448 3.070 1.00 32.63 N ANISOU 711 NH1 ARG A 92 4458 3094 4846 232 1365 1775 N ATOM 712 NH2 ARG A 92 23.976 18.455 5.234 1.00 32.54 N ANISOU 712 NH2 ARG A 92 3922 3173 5270 -77 1882 325 N ATOM 713 N VAL A 93 26.891 13.665 7.092 1.00 20.19 N ANISOU 713 N VAL A 93 2530 2149 2992 -430 415 -323 N ATOM 714 CA VAL A 93 26.417 12.505 7.846 1.00 19.53 C ANISOU 714 CA VAL A 93 2324 2198 2899 -365 608 -332 C ATOM 715 C VAL A 93 24.893 12.537 7.872 1.00 19.76 C ANISOU 715 C VAL A 93 2309 1861 3337 -104 251 105 C ATOM 716 O VAL A 93 24.314 13.586 8.186 1.00 21.72 O ANISOU 716 O VAL A 93 2549 1668 4034 -94 428 269 O ATOM 717 CB VAL A 93 26.973 12.459 9.284 1.00 19.22 C ANISOU 717 CB VAL A 93 2051 2317 2933 -286 551 -357 C ATOM 718 CG1 VAL A 93 26.522 11.166 9.982 1.00 22.14 C ANISOU 718 CG1 VAL A 93 3195 2221 2994 -441 188 -264 C ATOM 719 CG2 VAL A 93 28.485 12.598 9.375 1.00 24.66 C ANISOU 719 CG2 VAL A 93 2028 2809 4534 -83 288 -939 C ATOM 720 N THR A 94 24.298 11.392 7.537 1.00 18.16 N ANISOU 720 N THR A 94 2081 2004 2815 -96 392 -50 N ATOM 721 CA THR A 94 22.850 11.226 7.658 1.00 17.15 C ANISOU 721 CA THR A 94 1912 2119 2486 112 235 2 C ATOM 722 C THR A 94 22.526 10.020 8.526 1.00 16.21 C ANISOU 722 C THR A 94 1847 2086 2228 80 223 -89 C ATOM 723 O THR A 94 23.357 9.113 8.708 1.00 17.19 O ANISOU 723 O THR A 94 1845 1835 2850 -54 147 -157 O ATOM 724 CB THR A 94 22.151 11.086 6.288 1.00 17.95 C ANISOU 724 CB THR A 94 2541 1864 2415 -243 193 118 C ATOM 725 OG1 THR A 94 22.448 9.822 5.656 1.00 18.03 O ANISOU 725 OG1 THR A 94 2528 1876 2445 16 -30 195 O ATOM 726 CG2 THR A 94 22.608 12.199 5.324 1.00 19.43 C ANISOU 726 CG2 THR A 94 2369 2001 3011 62 353 561 C ATOM 727 N ASN A 95 21.309 10.005 9.084 1.00 16.93 N ANISOU 727 N ASN A 95 1887 2007 2539 13 256 -172 N ATOM 728 CA ASN A 95 20.830 8.923 9.928 1.00 17.09 C ANISOU 728 CA ASN A 95 1828 2089 2578 -87 320 -185 C ATOM 729 C ASN A 95 19.401 8.567 9.550 1.00 16.78 C ANISOU 729 C ASN A 95 1851 2306 2218 0 129 101 C ATOM 730 O ASN A 95 18.886 8.942 8.480 1.00 16.89 O ANISOU 730 O ASN A 95 2135 1903 2380 149 171 207 O ATOM 731 CB ASN A 95 21.025 9.257 11.421 1.00 16.35 C ANISOU 731 CB ASN A 95 1549 2058 2605 -103 122 -41 C ATOM 732 CG ASN A 95 20.099 10.386 11.868 1.00 18.98 C ANISOU 732 CG ASN A 95 2289 2397 2527 229 366 -164 C ATOM 733 OD1 ASN A 95 19.565 11.163 11.073 1.00 18.68 O ANISOU 733 OD1 ASN A 95 1918 2152 3026 140 263 -34 O ATOM 734 ND2 ASN A 95 19.877 10.438 13.202 1.00 19.89 N ANISOU 734 ND2 ASN A 95 2193 2792 2573 -390 405 -378 N ATOM 735 N THR A 96 18.732 7.806 10.407 1.00 15.33 N ANISOU 735 N THR A 96 1716 2332 1776 -119 16 -200 N ATOM 736 CA THR A 96 17.336 7.427 10.191 1.00 16.11 C ANISOU 736 CA THR A 96 1762 2466 1894 -134 30 -377 C ATOM 737 C THR A 96 16.459 7.808 11.374 1.00 19.00 C ANISOU 737 C THR A 96 1964 2796 2457 -66 441 -498 C ATOM 738 O THR A 96 16.038 6.963 12.162 1.00 20.20 O ANISOU 738 O THR A 96 2365 3246 2064 133 342 -224 O ATOM 739 CB THR A 96 17.213 5.944 9.857 1.00 15.48 C ANISOU 739 CB THR A 96 1645 2352 1885 -174 92 -151 C ATOM 740 OG1 THR A 96 17.633 5.133 10.984 1.00 18.86 O ANISOU 740 OG1 THR A 96 2299 2704 2164 -213 -303 15 O ATOM 741 CG2 THR A 96 18.099 5.535 8.693 1.00 18.53 C ANISOU 741 CG2 THR A 96 2505 1876 2658 -21 937 56 C ATOM 742 N PRO A 97 16.136 9.099 11.452 1.00 21.69 N ANISOU 742 N PRO A 97 1999 2650 3593 -413 731 -1005 N ATOM 743 CA PRO A 97 15.308 9.561 12.579 1.00 24.49 C ANISOU 743 CA PRO A 97 2176 3204 3924 -188 823 -1247 C ATOM 744 C PRO A 97 13.842 9.214 12.374 1.00 24.86 C ANISOU 744 C PRO A 97 2176 3847 3421 -227 812 -1489 C ATOM 745 O PRO A 97 13.431 9.097 11.218 1.00 23.10 O ANISOU 745 O PRO A 97 2407 3094 3276 -289 750 -520 O ATOM 746 CB PRO A 97 15.513 11.085 12.534 1.00 28.10 C ANISOU 746 CB PRO A 97 2297 3139 5242 72 1221 -1561 C ATOM 747 CG PRO A 97 15.685 11.383 11.081 1.00 29.25 C ANISOU 747 CG PRO A 97 3041 2483 5590 -278 2040 -1231 C ATOM 748 CD PRO A 97 16.427 10.183 10.525 1.00 22.56 C ANISOU 748 CD PRO A 97 1907 2348 4317 -59 804 -787 C ATOM 749 N ASP A 98 13.110 9.098 13.472 1.00 23.81 N ANISOU 749 N ASP A 98 1931 3910 3204 -32 540 -1229 N ATOM 750 CA ASP A 98 11.681 8.987 13.608 1.00 24.18 C ANISOU 750 CA ASP A 98 1956 3587 3644 -27 603 -808 C ATOM 751 C ASP A 98 11.108 7.670 13.137 1.00 28.89 C ANISOU 751 C ASP A 98 2740 4156 4082 -855 1232 -1260 C ATOM 752 O ASP A 98 10.165 7.081 13.711 1.00 23.63 O ANISOU 752 O ASP A 98 2874 2848 3255 191 752 270 O ATOM 753 CB ASP A 98 11.046 10.162 12.835 1.00 25.67 C ANISOU 753 CB ASP A 98 1944 4481 3327 -167 587 -128 C ATOM 754 CG ASP A 98 11.520 11.451 13.500 1.00 28.38 C ANISOU 754 CG ASP A 98 3039 3662 4082 -50 924 103 C ATOM 755 OD1 ASP A 98 11.229 11.571 14.719 1.00 28.98 O ANISOU 755 OD1 ASP A 98 4473 2643 3894 -383 678 179 O ATOM 756 OD2 ASP A 98 12.150 12.294 12.851 1.00 37.03 O ANISOU 756 OD2 ASP A 98 5554 3639 4875 -240 1895 433 O ATOM 757 N VAL A 99 11.669 7.113 12.101 1.00 18.34 N ANISOU 757 N VAL A 99 2111 2244 2614 234 171 435 N ATOM 758 CA VAL A 99 11.096 5.944 11.446 1.00 17.17 C ANISOU 758 CA VAL A 99 2030 2248 2245 151 400 543 C ATOM 759 C VAL A 99 11.197 4.680 12.285 1.00 17.71 C ANISOU 759 C VAL A 99 2364 2293 2071 6 362 518 C ATOM 760 O VAL A 99 10.451 3.738 11.958 1.00 18.17 O ANISOU 760 O VAL A 99 1968 2297 2639 60 90 724 O ATOM 761 CB VAL A 99 11.726 5.705 10.059 1.00 18.28 C ANISOU 761 CB VAL A 99 2546 2029 2369 398 693 706 C ATOM 762 CG1 VAL A 99 11.349 6.854 9.148 1.00 20.79 C ANISOU 762 CG1 VAL A 99 3227 2018 2655 305 650 927 C ATOM 763 CG2 VAL A 99 13.220 5.516 10.177 1.00 22.21 C ANISOU 763 CG2 VAL A 99 2565 2860 3013 660 947 601 C ATOM 764 N LEU A 100 12.028 4.597 13.308 1.00 16.31 N ANISOU 764 N LEU A 100 2349 1908 1941 243 416 181 N ATOM 765 CA LEU A 100 12.108 3.390 14.152 1.00 15.05 C ANISOU 765 CA LEU A 100 1574 2058 2088 197 399 274 C ATOM 766 C LEU A 100 11.543 3.619 15.536 1.00 14.15 C ANISOU 766 C LEU A 100 1650 1735 1992 165 254 287 C ATOM 767 O LEU A 100 11.577 2.704 16.357 1.00 14.86 O ANISOU 767 O LEU A 100 1790 1808 2050 188 198 347 O ATOM 768 CB LEU A 100 13.554 2.872 14.215 1.00 16.31 C ANISOU 768 CB LEU A 100 1551 1932 2713 148 288 -56 C ATOM 769 CG LEU A 100 14.676 3.820 14.557 1.00 16.55 C ANISOU 769 CG LEU A 100 1763 2261 2263 -89 131 -126 C ATOM 770 CD1 LEU A 100 14.687 4.350 15.981 1.00 24.83 C ANISOU 770 CD1 LEU A 100 3393 3200 2840 -840 1237 -1139 C ATOM 771 CD2 LEU A 100 16.058 3.156 14.376 1.00 21.25 C ANISOU 771 CD2 LEU A 100 1560 3554 2961 -216 657 -643 C ATOM 772 N THR A 101 11.055 4.829 15.817 1.00 14.65 N ANISOU 772 N THR A 101 1657 1686 2222 14 473 243 N ATOM 773 CA THR A 101 10.593 5.137 17.163 1.00 13.91 C ANISOU 773 CA THR A 101 1322 1917 2048 125 163 176 C ATOM 774 C THR A 101 9.537 4.183 17.705 1.00 13.82 C ANISOU 774 C THR A 101 1222 2084 1945 207 77 454 C ATOM 775 O THR A 101 9.614 3.683 18.828 1.00 15.35 O ANISOU 775 O THR A 101 2170 1725 1935 20 -234 439 O ATOM 776 CB THR A 101 10.053 6.581 17.200 1.00 15.25 C ANISOU 776 CB THR A 101 1238 1965 2592 160 392 80 C ATOM 777 OG1 THR A 101 11.127 7.448 16.830 1.00 16.54 O ANISOU 777 OG1 THR A 101 1807 1968 2509 -132 532 130 O ATOM 778 CG2 THR A 101 9.536 6.969 18.600 1.00 18.93 C ANISOU 778 CG2 THR A 101 1886 2247 3061 204 1006 -52 C ATOM 779 N ASP A 102 8.521 3.946 16.887 1.00 13.21 N ANISOU 779 N ASP A 102 1341 1793 1886 118 61 436 N ATOM 780 CA ASP A 102 7.411 3.133 17.328 1.00 13.17 C ANISOU 780 CA ASP A 102 1666 1660 1676 -116 93 132 C ATOM 781 C ASP A 102 7.818 1.694 17.602 1.00 14.20 C ANISOU 781 C ASP A 102 1757 1745 1893 90 229 256 C ATOM 782 O ASP A 102 7.439 1.094 18.612 1.00 14.14 O ANISOU 782 O ASP A 102 1630 1821 1923 97 85 339 O ATOM 783 CB ASP A 102 6.293 3.141 16.294 1.00 16.70 C ANISOU 783 CB ASP A 102 1787 2134 2424 -401 -319 712 C ATOM 784 CG ASP A 102 5.608 4.488 16.211 1.00 24.93 C ANISOU 784 CG ASP A 102 2208 2649 4614 142 -525 1349 C ATOM 785 OD1 ASP A 102 5.698 5.273 17.158 1.00 29.66 O ANISOU 785 OD1 ASP A 102 4093 3012 4167 1830 1410 1081 O ATOM 786 OD2 ASP A 102 5.005 4.687 15.150 1.00 34.88 O ANISOU 786 OD2 ASP A 102 3158 5477 4618 1371 -267 2318 O ATOM 787 N ASP A 103 8.635 1.106 16.709 1.00 13.77 N ANISOU 787 N ASP A 103 1533 1823 1874 72 38 169 N ATOM 788 CA ASP A 103 9.032 -0.286 16.961 1.00 13.66 C ANISOU 788 CA ASP A 103 1649 1728 1814 25 0 107 C ATOM 789 C ASP A 103 9.885 -0.397 18.210 1.00 12.24 C ANISOU 789 C ASP A 103 1314 1502 1837 -31 185 124 C ATOM 790 O ASP A 103 9.744 -1.395 18.945 1.00 13.48 O ANISOU 790 O ASP A 103 1608 1514 1999 -63 21 257 O ATOM 791 CB ASP A 103 9.739 -0.838 15.725 1.00 13.43 C ANISOU 791 CB ASP A 103 1559 1674 1871 -32 32 218 C ATOM 792 CG ASP A 103 8.861 -1.598 14.765 1.00 14.04 C ANISOU 792 CG ASP A 103 1838 1905 1593 18 -55 179 C ATOM 793 OD1 ASP A 103 7.889 -2.214 15.211 1.00 18.78 O ANISOU 793 OD1 ASP A 103 1504 2982 2648 -326 202 -521 O ATOM 794 OD2 ASP A 103 9.197 -1.596 13.578 1.00 22.12 O ANISOU 794 OD2 ASP A 103 4700 2023 1682 -365 504 -21 O ATOM 795 N VAL A 104 10.763 0.553 18.452 1.00 12.64 N ANISOU 795 N VAL A 104 1562 1438 1802 -39 106 139 N ATOM 796 CA VAL A 104 11.625 0.441 19.630 1.00 12.70 C ANISOU 796 CA VAL A 104 1583 1376 1864 27 60 -40 C ATOM 797 C VAL A 104 10.787 0.603 20.900 1.00 12.44 C ANISOU 797 C VAL A 104 1452 1523 1750 78 -86 94 C ATOM 798 O VAL A 104 10.935 -0.136 21.856 1.00 13.60 O ANISOU 798 O VAL A 104 1590 1749 1830 -38 -186 251 O ATOM 799 CB VAL A 104 12.769 1.442 19.560 1.00 14.48 C ANISOU 799 CB VAL A 104 1457 1756 2289 -72 30 65 C ATOM 800 CG1 VAL A 104 13.530 1.464 20.871 1.00 16.44 C ANISOU 800 CG1 VAL A 104 1571 2285 2389 -340 -193 410 C ATOM 801 CG2 VAL A 104 13.728 1.128 18.440 1.00 16.09 C ANISOU 801 CG2 VAL A 104 1584 2022 2509 50 208 227 C ATOM 802 N ALA A 105 9.871 1.589 20.888 1.00 12.66 N ANISOU 802 N ALA A 105 1538 1570 1704 168 -10 -7 N ATOM 803 CA ALA A 105 8.994 1.802 22.038 1.00 13.41 C ANISOU 803 CA ALA A 105 1687 1525 1883 118 86 75 C ATOM 804 C ALA A 105 8.075 0.591 22.271 1.00 13.16 C ANISOU 804 C ALA A 105 1827 1512 1662 94 10 220 C ATOM 805 O ALA A 105 7.855 0.162 23.405 1.00 13.20 O ANISOU 805 O ALA A 105 1567 1844 1607 57 5 151 O ATOM 806 CB ALA A 105 8.176 3.096 21.869 1.00 13.71 C ANISOU 806 CB ALA A 105 1670 1484 2055 151 114 66 C ATOM 807 N ASP A 106 7.588 -0.006 21.220 1.00 13.37 N ANISOU 807 N ASP A 106 1458 1987 1635 -170 85 226 N ATOM 808 CA ASP A 106 6.765 -1.217 21.290 1.00 12.25 C ANISOU 808 CA ASP A 106 1293 1865 1496 10 345 120 C ATOM 809 C ASP A 106 7.548 -2.333 21.980 1.00 13.28 C ANISOU 809 C ASP A 106 1448 1883 1715 -105 -6 116 C ATOM 810 O ASP A 106 6.984 -3.051 22.808 1.00 13.20 O ANISOU 810 O ASP A 106 1667 1743 1607 -83 107 60 O ATOM 811 CB ASP A 106 6.326 -1.669 19.925 1.00 13.20 C ANISOU 811 CB ASP A 106 1974 1421 1620 34 53 226 C ATOM 812 CG ASP A 106 5.237 -0.832 19.286 1.00 13.19 C ANISOU 812 CG ASP A 106 1616 1740 1657 160 93 -36 C ATOM 813 OD1 ASP A 106 4.754 0.112 19.900 1.00 15.16 O ANISOU 813 OD1 ASP A 106 1765 1862 2135 130 297 -229 O ATOM 814 OD2 ASP A 106 4.899 -1.173 18.118 1.00 15.45 O ANISOU 814 OD2 ASP A 106 1778 2370 1722 138 -45 -126 O ATOM 815 N LEU A 107 8.829 -2.453 21.629 1.00 13.39 N ANISOU 815 N LEU A 107 1362 1941 1785 -94 -91 482 N ATOM 816 CA LEU A 107 9.611 -3.526 22.198 1.00 13.39 C ANISOU 816 CA LEU A 107 1587 1634 1866 -40 -68 202 C ATOM 817 C LEU A 107 9.845 -3.301 23.685 1.00 12.68 C ANISOU 817 C LEU A 107 1584 1265 1969 479 -264 123 C ATOM 818 O LEU A 107 9.886 -4.269 24.460 1.00 13.76 O ANISOU 818 O LEU A 107 1799 1459 1971 261 11 333 O ATOM 819 CB LEU A 107 10.948 -3.713 21.457 1.00 14.20 C ANISOU 819 CB LEU A 107 1523 1750 2122 -5 -38 337 C ATOM 820 CG LEU A 107 11.675 -5.005 21.839 1.00 14.10 C ANISOU 820 CG LEU A 107 1699 1676 1981 36 129 233 C ATOM 821 CD1 LEU A 107 10.908 -6.225 21.327 1.00 16.45 C ANISOU 821 CD1 LEU A 107 1567 1825 2860 105 -116 -160 C ATOM 822 CD2 LEU A 107 13.105 -4.999 21.359 1.00 15.74 C ANISOU 822 CD2 LEU A 107 1497 2020 2464 62 12 34 C ATOM 823 N ALA A 108 9.997 -2.048 24.102 1.00 13.65 N ANISOU 823 N ALA A 108 1817 1381 1986 -14 269 103 N ATOM 824 CA ALA A 108 10.130 -1.771 25.540 1.00 13.28 C ANISOU 824 CA ALA A 108 1564 1493 1990 -66 41 41 C ATOM 825 C ALA A 108 8.926 -2.292 26.313 1.00 12.05 C ANISOU 825 C ALA A 108 1471 1461 1646 64 -98 4 C ATOM 826 O ALA A 108 9.066 -2.914 27.380 1.00 13.21 O ANISOU 826 O ALA A 108 1803 1393 1824 75 -238 239 O ATOM 827 CB ALA A 108 10.312 -0.282 25.789 1.00 14.53 C ANISOU 827 CB ALA A 108 1808 1535 2176 -196 -362 68 C ATOM 828 N ILE A 109 7.742 -2.030 25.791 1.00 12.85 N ANISOU 828 N ILE A 109 1551 1589 1741 -141 -264 156 N ATOM 829 CA ILE A 109 6.535 -2.492 26.468 1.00 12.62 C ANISOU 829 CA ILE A 109 1497 1452 1847 -241 -270 102 C ATOM 830 C ILE A 109 6.450 -4.008 26.407 1.00 12.62 C ANISOU 830 C ILE A 109 1635 1492 1670 -58 -73 143 C ATOM 831 O ILE A 109 6.099 -4.700 27.359 1.00 12.56 O ANISOU 831 O ILE A 109 1594 1468 1711 -80 -78 179 O ATOM 832 CB ILE A 109 5.267 -1.850 25.868 1.00 12.87 C ANISOU 832 CB ILE A 109 1520 1439 1931 -146 -277 121 C ATOM 833 CG1 ILE A 109 5.248 -0.329 25.865 1.00 15.06 C ANISOU 833 CG1 ILE A 109 2138 1476 2110 119 -132 -177 C ATOM 834 CG2 ILE A 109 4.017 -2.441 26.539 1.00 14.99 C ANISOU 834 CG2 ILE A 109 1544 1873 2278 213 148 152 C ATOM 835 CD1 ILE A 109 5.294 0.276 27.245 1.00 16.41 C ANISOU 835 CD1 ILE A 109 2572 1681 1982 665 -261 -69 C ATOM 836 N GLY A 110 6.807 -4.606 25.270 1.00 12.62 N ANISOU 836 N GLY A 110 1678 1548 1568 -7 -189 157 N ATOM 837 CA GLY A 110 6.836 -6.038 25.163 1.00 11.39 C ANISOU 837 CA GLY A 110 1387 1523 1415 -112 145 254 C ATOM 838 C GLY A 110 7.783 -6.709 26.137 1.00 12.75 C ANISOU 838 C GLY A 110 1798 1488 1559 -71 -246 99 C ATOM 839 O GLY A 110 7.489 -7.753 26.692 1.00 12.22 O ANISOU 839 O GLY A 110 1778 1371 1495 119 -19 54 O ATOM 840 N LEU A 111 8.955 -6.088 26.360 1.00 12.68 N ANISOU 840 N LEU A 111 1409 1503 1904 168 -9 104 N ATOM 841 CA LEU A 111 9.917 -6.576 27.348 1.00 12.35 C ANISOU 841 CA LEU A 111 1449 1512 1733 32 18 116 C ATOM 842 C LEU A 111 9.375 -6.474 28.756 1.00 12.46 C ANISOU 842 C LEU A 111 1667 1242 1824 105 121 147 C ATOM 843 O LEU A 111 9.529 -7.397 29.575 1.00 12.75 O ANISOU 843 O LEU A 111 1528 1462 1853 152 13 315 O ATOM 844 CB LEU A 111 11.238 -5.806 27.202 1.00 13.70 C ANISOU 844 CB LEU A 111 1396 1726 2083 -30 142 -263 C ATOM 845 CG LEU A 111 12.142 -6.310 26.058 1.00 12.73 C ANISOU 845 CG LEU A 111 1182 1916 1740 167 -105 34 C ATOM 846 CD1 LEU A 111 13.237 -5.275 25.744 1.00 15.30 C ANISOU 846 CD1 LEU A 111 1349 2049 2417 63 245 -43 C ATOM 847 CD2 LEU A 111 12.762 -7.650 26.404 1.00 14.87 C ANISOU 847 CD2 LEU A 111 1878 1805 1969 360 -163 -243 C ATOM 848 N ILE A 112 8.712 -5.333 29.037 1.00 12.41 N ANISOU 848 N ILE A 112 1572 1410 1734 143 -21 136 N ATOM 849 CA ILE A 112 8.116 -5.163 30.355 1.00 12.17 C ANISOU 849 CA ILE A 112 1803 1221 1600 0 -119 -112 C ATOM 850 C ILE A 112 7.139 -6.284 30.644 1.00 10.92 C ANISOU 850 C ILE A 112 1463 1289 1399 203 -176 95 C ATOM 851 O ILE A 112 7.220 -6.935 31.684 1.00 11.86 O ANISOU 851 O ILE A 112 1651 1487 1367 195 -136 104 O ATOM 852 CB ILE A 112 7.435 -3.771 30.486 1.00 12.71 C ANISOU 852 CB ILE A 112 1866 1251 1711 77 -156 -94 C ATOM 853 CG1 ILE A 112 8.467 -2.629 30.531 1.00 13.62 C ANISOU 853 CG1 ILE A 112 2182 1247 1748 -52 -1 -240 C ATOM 854 CG2 ILE A 112 6.530 -3.739 31.697 1.00 14.84 C ANISOU 854 CG2 ILE A 112 1702 1680 2257 121 91 -186 C ATOM 855 CD1 ILE A 112 7.898 -1.241 30.318 1.00 15.15 C ANISOU 855 CD1 ILE A 112 2732 1187 1839 11 -45 -240 C ATOM 856 N LEU A 113 6.193 -6.491 29.749 1.00 12.95 N ANISOU 856 N LEU A 113 1630 1720 1570 -138 -256 147 N ATOM 857 CA LEU A 113 5.199 -7.549 29.956 1.00 13.47 C ANISOU 857 CA LEU A 113 1207 1618 2294 96 161 -50 C ATOM 858 C LEU A 113 5.844 -8.935 30.006 1.00 12.48 C ANISOU 858 C LEU A 113 1339 1607 1797 6 -10 -127 C ATOM 859 O LEU A 113 5.472 -9.803 30.793 1.00 13.18 O ANISOU 859 O LEU A 113 1614 1509 1884 0 82 -133 O ATOM 860 CB LEU A 113 4.122 -7.411 28.855 1.00 13.31 C ANISOU 860 CB LEU A 113 1324 1443 2292 -61 72 34 C ATOM 861 CG LEU A 113 3.181 -6.232 29.075 1.00 13.99 C ANISOU 861 CG LEU A 113 1534 1525 2255 82 -105 -5 C ATOM 862 CD1 LEU A 113 2.493 -5.794 27.781 1.00 15.60 C ANISOU 862 CD1 LEU A 113 1771 1604 2551 -211 -558 75 C ATOM 863 CD2 LEU A 113 2.205 -6.630 30.157 1.00 16.39 C ANISOU 863 CD2 LEU A 113 2015 1705 2509 208 380 -169 C ATOM 864 N ALA A 114 6.834 -9.175 29.145 1.00 12.36 N ANISOU 864 N ALA A 114 1543 1367 1788 168 67 -56 N ATOM 865 CA ALA A 114 7.474 -10.487 29.124 1.00 12.76 C ANISOU 865 CA ALA A 114 1480 1413 1957 127 15 15 C ATOM 866 C ALA A 114 8.191 -10.806 30.428 1.00 13.89 C ANISOU 866 C ALA A 114 1516 1554 2207 169 -134 85 C ATOM 867 O ALA A 114 8.143 -11.945 30.871 1.00 13.64 O ANISOU 867 O ALA A 114 1835 1527 1821 67 -134 25 O ATOM 868 CB ALA A 114 8.413 -10.664 27.941 1.00 13.56 C ANISOU 868 CB ALA A 114 1429 1516 2209 167 134 -115 C ATOM 869 N VAL A 115 8.809 -9.785 31.021 1.00 12.33 N ANISOU 869 N VAL A 115 1428 1433 1825 87 51 237 N ATOM 870 CA VAL A 115 9.472 -9.987 32.321 1.00 13.60 C ANISOU 870 CA VAL A 115 1765 1472 1929 279 -56 47 C ATOM 871 C VAL A 115 8.446 -10.068 33.418 1.00 13.64 C ANISOU 871 C VAL A 115 2005 1550 1627 205 -40 -134 C ATOM 872 O VAL A 115 8.406 -11.097 34.129 1.00 14.60 O ANISOU 872 O VAL A 115 1790 1506 2253 323 272 42 O ATOM 873 CB VAL A 115 10.495 -8.876 32.599 1.00 14.07 C ANISOU 873 CB VAL A 115 2311 1570 1467 -5 -10 -88 C ATOM 874 CG1 VAL A 115 11.051 -9.026 34.018 1.00 14.78 C ANISOU 874 CG1 VAL A 115 1962 2042 1610 196 -72 192 C ATOM 875 CG2 VAL A 115 11.625 -8.893 31.595 1.00 14.40 C ANISOU 875 CG2 VAL A 115 1762 2114 1594 61 -212 77 C ATOM 876 N LEU A 116 7.601 -9.046 33.564 1.00 12.46 N ANISOU 876 N LEU A 116 1809 1489 1435 107 -23 225 N ATOM 877 CA LEU A 116 6.717 -9.023 34.740 1.00 11.67 C ANISOU 877 CA LEU A 116 1672 1342 1419 120 -114 80 C ATOM 878 C LEU A 116 5.725 -10.193 34.777 1.00 12.28 C ANISOU 878 C LEU A 116 1596 1354 1715 130 1 46 C ATOM 879 O LEU A 116 5.443 -10.741 35.841 1.00 14.49 O ANISOU 879 O LEU A 116 2051 1599 1855 -177 85 122 O ATOM 880 CB LEU A 116 5.946 -7.714 34.802 1.00 13.43 C ANISOU 880 CB LEU A 116 2249 1263 1591 146 41 4 C ATOM 881 CG LEU A 116 6.587 -6.549 35.564 1.00 14.27 C ANISOU 881 CG LEU A 116 2187 1465 1770 106 219 -214 C ATOM 882 CD1 LEU A 116 7.897 -6.178 34.907 1.00 15.99 C ANISOU 882 CD1 LEU A 116 1958 1917 2200 60 87 -170 C ATOM 883 CD2 LEU A 116 5.619 -5.392 35.615 1.00 15.05 C ANISOU 883 CD2 LEU A 116 2073 1297 2348 -30 300 -111 C ATOM 884 N ARG A 117 5.173 -10.563 33.610 1.00 13.41 N ANISOU 884 N ARG A 117 1711 1552 1831 69 -103 -91 N ATOM 885 CA ARG A 117 4.234 -11.653 33.470 1.00 12.55 C ANISOU 885 CA ARG A 117 1789 1509 1473 68 164 -128 C ATOM 886 C ARG A 117 4.923 -12.981 33.131 1.00 12.15 C ANISOU 886 C ARG A 117 1695 1609 1313 -9 181 -287 C ATOM 887 O ARG A 117 4.236 -13.999 32.953 1.00 14.08 O ANISOU 887 O ARG A 117 1876 1475 1998 -63 -154 -65 O ATOM 888 CB ARG A 117 3.125 -11.322 32.443 1.00 13.18 C ANISOU 888 CB ARG A 117 1703 1541 1761 -131 40 -172 C ATOM 889 CG ARG A 117 2.317 -10.066 32.809 1.00 15.02 C ANISOU 889 CG ARG A 117 1639 1700 2368 -6 144 52 C ATOM 890 CD ARG A 117 1.580 -10.156 34.146 1.00 17.01 C ANISOU 890 CD ARG A 117 1825 2221 2416 395 305 -274 C ATOM 891 NE ARG A 117 0.480 -11.116 34.028 1.00 17.53 N ANISOU 891 NE ARG A 117 2145 2053 2463 218 569 602 N ATOM 892 CZ ARG A 117 -0.707 -10.809 33.545 1.00 16.12 C ANISOU 892 CZ ARG A 117 1933 1628 2563 144 545 -324 C ATOM 893 NH1 ARG A 117 -1.023 -9.577 33.129 1.00 17.84 N ANISOU 893 NH1 ARG A 117 1865 1739 3175 247 -293 -366 N ATOM 894 NH2 ARG A 117 -1.593 -11.789 33.499 1.00 19.33 N ANISOU 894 NH2 ARG A 117 2702 2128 2512 -444 658 -445 N ATOM 895 N ARG A 118 6.229 -13.003 33.039 1.00 12.84 N ANISOU 895 N ARG A 118 1730 1361 1789 13 368 67 N ATOM 896 CA ARG A 118 7.018 -14.202 32.786 1.00 12.90 C ANISOU 896 CA ARG A 118 1797 1366 1737 176 94 180 C ATOM 897 C ARG A 118 6.512 -14.950 31.568 1.00 13.56 C ANISOU 897 C ARG A 118 1887 1489 1777 298 127 14 C ATOM 898 O ARG A 118 6.365 -16.187 31.553 1.00 14.29 O ANISOU 898 O ARG A 118 2087 1502 1840 186 43 75 O ATOM 899 CB ARG A 118 7.049 -15.128 34.015 1.00 14.70 C ANISOU 899 CB ARG A 118 2220 1608 1758 -8 102 246 C ATOM 900 CG ARG A 118 7.736 -14.582 35.244 1.00 15.84 C ANISOU 900 CG ARG A 118 2171 2088 1759 -4 67 131 C ATOM 901 CD ARG A 118 9.211 -14.344 34.955 1.00 16.92 C ANISOU 901 CD ARG A 118 1948 2439 2042 318 121 -283 C ATOM 902 NE ARG A 118 9.935 -14.232 36.217 1.00 18.94 N ANISOU 902 NE ARG A 118 2476 2264 2455 -93 -344 91 N ATOM 903 CZ ARG A 118 10.198 -13.178 36.938 1.00 18.35 C ANISOU 903 CZ ARG A 118 2234 2100 2638 169 -958 221 C ATOM 904 NH1 ARG A 118 9.806 -11.952 36.542 1.00 21.78 N ANISOU 904 NH1 ARG A 118 3498 2154 2625 371 -659 405 N ATOM 905 NH2 ARG A 118 10.869 -13.263 38.093 1.00 20.85 N ANISOU 905 NH2 ARG A 118 2546 3149 2228 -43 -737 480 N ATOM 906 N ILE A 119 6.254 -14.178 30.501 1.00 14.10 N ANISOU 906 N ILE A 119 2039 1554 1764 256 -24 19 N ATOM 907 CA ILE A 119 5.664 -14.799 29.291 1.00 13.48 C ANISOU 907 CA ILE A 119 1744 1464 1914 141 -60 27 C ATOM 908 C ILE A 119 6.570 -15.835 28.689 1.00 13.70 C ANISOU 908 C ILE A 119 1799 1346 2062 123 -94 -52 C ATOM 909 O ILE A 119 6.133 -16.938 28.284 1.00 14.70 O ANISOU 909 O ILE A 119 2247 1475 1861 40 -320 -80 O ATOM 910 CB ILE A 119 5.281 -13.702 28.281 1.00 13.00 C ANISOU 910 CB ILE A 119 1625 1407 1907 204 -134 -59 C ATOM 911 CG1 ILE A 119 4.172 -12.845 28.852 1.00 13.21 C ANISOU 911 CG1 ILE A 119 1622 1635 1761 216 -167 -106 C ATOM 912 CG2 ILE A 119 4.883 -14.251 26.920 1.00 13.72 C ANISOU 912 CG2 ILE A 119 1786 1778 1649 -76 222 37 C ATOM 913 CD1 ILE A 119 3.764 -11.670 27.999 1.00 16.16 C ANISOU 913 CD1 ILE A 119 2019 1535 2586 562 75 92 C ATOM 914 N CYS A 120 7.860 -15.559 28.602 1.00 13.91 N ANISOU 914 N CYS A 120 1778 1652 1857 175 24 -79 N ATOM 915 CA CYS A 120 8.774 -16.547 28.009 1.00 14.23 C ANISOU 915 CA CYS A 120 1939 1680 1787 304 -74 -182 C ATOM 916 C CYS A 120 8.903 -17.779 28.871 1.00 15.19 C ANISOU 916 C CYS A 120 1976 1805 1989 414 18 -87 C ATOM 917 O CYS A 120 8.939 -18.904 28.372 1.00 15.75 O ANISOU 917 O CYS A 120 1946 1653 2384 263 -139 -69 O ATOM 918 CB CYS A 120 10.151 -15.926 27.753 1.00 16.09 C ANISOU 918 CB CYS A 120 1928 1869 2315 311 170 -207 C ATOM 919 SG CYS A 120 10.187 -14.431 26.749 1.00 18.84 S ANISOU 919 SG CYS A 120 2488 2270 2400 -167 65 93 S ATOM 920 N GLU A 121 8.939 -17.576 30.194 1.00 15.29 N ANISOU 920 N GLU A 121 1965 1879 1965 208 8 89 N ATOM 921 CA GLU A 121 9.040 -18.716 31.107 1.00 15.36 C ANISOU 921 CA GLU A 121 1885 1924 2028 385 200 87 C ATOM 922 C GLU A 121 7.781 -19.568 31.044 1.00 15.05 C ANISOU 922 C GLU A 121 1924 1791 2004 360 278 36 C ATOM 923 O GLU A 121 7.855 -20.806 31.088 1.00 16.25 O ANISOU 923 O GLU A 121 2288 1769 2120 459 -16 200 O ATOM 924 CB GLU A 121 9.383 -18.217 32.523 1.00 17.43 C ANISOU 924 CB GLU A 121 2656 1875 2091 239 -231 161 C ATOM 925 CG GLU A 121 10.765 -17.561 32.593 1.00 23.20 C ANISOU 925 CG GLU A 121 2339 2459 4016 527 -873 -334 C ATOM 926 CD GLU A 121 11.906 -18.215 31.852 1.00 26.83 C ANISOU 926 CD GLU A 121 2439 2714 5040 746 -306 323 C ATOM 927 OE1 GLU A 121 12.263 -19.290 32.363 1.00 24.99 O ANISOU 927 OE1 GLU A 121 2611 2508 4376 792 -974 -145 O ATOM 928 OE2 GLU A 121 12.470 -17.692 30.818 1.00 30.18 O ANISOU 928 OE2 GLU A 121 3412 2304 5750 620 589 153 O ATOM 929 N CYS A 122 6.622 -18.952 30.978 1.00 15.62 N ANISOU 929 N CYS A 122 1896 1670 2369 280 33 -338 N ATOM 930 CA CYS A 122 5.342 -19.626 30.872 1.00 15.66 C ANISOU 930 CA CYS A 122 1982 1928 2042 118 -197 34 C ATOM 931 C CYS A 122 5.245 -20.483 29.638 1.00 14.99 C ANISOU 931 C CYS A 122 2242 1602 1850 266 -542 305 C ATOM 932 O CYS A 122 4.750 -21.613 29.627 1.00 17.39 O ANISOU 932 O CYS A 122 2464 1590 2554 169 133 6 O ATOM 933 CB CYS A 122 4.203 -18.568 30.836 1.00 15.22 C ANISOU 933 CB CYS A 122 1867 1816 2098 2 -303 65 C ATOM 934 SG CYS A 122 3.689 -17.978 32.441 1.00 17.93 S ANISOU 934 SG CYS A 122 2337 1920 2558 44 209 -141 S ATOM 935 N ASP A 123 5.686 -19.907 28.509 1.00 15.18 N ANISOU 935 N ASP A 123 2542 1298 1927 491 -366 181 N ATOM 936 CA ASP A 123 5.659 -20.618 27.229 1.00 15.10 C ANISOU 936 CA ASP A 123 2051 1639 2045 336 -41 -100 C ATOM 937 C ASP A 123 6.589 -21.803 27.308 1.00 15.74 C ANISOU 937 C ASP A 123 2047 1589 2344 309 29 -86 C ATOM 938 O ASP A 123 6.236 -22.901 26.866 1.00 16.79 O ANISOU 938 O ASP A 123 2483 1601 2296 396 -305 -56 O ATOM 939 CB ASP A 123 5.967 -19.610 26.115 1.00 15.43 C ANISOU 939 CB ASP A 123 2390 1632 1840 285 -276 -207 C ATOM 940 CG ASP A 123 5.996 -20.316 24.749 1.00 14.59 C ANISOU 940 CG ASP A 123 2044 1576 1923 379 -225 -177 C ATOM 941 OD1 ASP A 123 5.055 -20.210 23.955 1.00 15.44 O ANISOU 941 OD1 ASP A 123 2378 1791 1697 319 -371 14 O ATOM 942 OD2 ASP A 123 7.030 -20.991 24.527 1.00 18.23 O ANISOU 942 OD2 ASP A 123 2408 1976 2544 790 -261 -481 O ATOM 943 N LYS A 124 7.796 -21.690 27.857 1.00 14.99 N ANISOU 943 N LYS A 124 2210 1464 2022 420 -5 -55 N ATOM 944 CA LYS A 124 8.685 -22.838 28.023 1.00 16.01 C ANISOU 944 CA LYS A 124 2203 1591 2289 447 -41 -68 C ATOM 945 C LYS A 124 8.051 -23.902 28.915 1.00 15.84 C ANISOU 945 C LYS A 124 1942 1470 2607 641 -43 59 C ATOM 946 O LYS A 124 8.132 -25.105 28.659 1.00 18.80 O ANISOU 946 O LYS A 124 3176 1456 2512 789 -32 263 O ATOM 947 CB LYS A 124 9.991 -22.345 28.613 1.00 17.59 C ANISOU 947 CB LYS A 124 2208 1925 2549 293 -136 33 C ATOM 948 CG LYS A 124 10.942 -21.655 27.646 1.00 21.62 C ANISOU 948 CG LYS A 124 2042 3387 2788 274 41 401 C ATOM 949 CD LYS A 124 12.079 -21.015 28.388 1.00 28.71 C ANISOU 949 CD LYS A 124 1335 4730 4845 76 -848 1416 C ATOM 950 CE LYS A 124 12.198 -19.534 28.215 1.00 47.74 C ANISOU 950 CE LYS A 124 5506 4509 8124 -1746 931 -529 C ATOM 951 NZ LYS A 124 13.075 -18.974 27.164 1.00 52.24 N ANISOU 951 NZ LYS A 124 5836 2550 11462 81 3055 475 N ATOM 952 N TYR A 125 7.383 -23.460 29.972 1.00 16.97 N ANISOU 952 N TYR A 125 2125 1878 2443 666 39 189 N ATOM 953 CA TYR A 125 6.729 -24.351 30.925 1.00 17.52 C ANISOU 953 CA TYR A 125 3076 1698 1883 278 -249 -44 C ATOM 954 C TYR A 125 5.664 -25.194 30.240 1.00 18.79 C ANISOU 954 C TYR A 125 3223 1246 2672 355 -531 -52 C ATOM 955 O TYR A 125 5.546 -26.396 30.410 1.00 19.41 O ANISOU 955 O TYR A 125 3257 1381 2736 310 20 246 O ATOM 956 CB TYR A 125 6.125 -23.497 32.035 1.00 17.35 C ANISOU 956 CB TYR A 125 2850 1810 1931 281 -168 -15 C ATOM 957 CG TYR A 125 5.347 -24.108 33.152 1.00 18.20 C ANISOU 957 CG TYR A 125 3112 1668 2134 93 -37 -107 C ATOM 958 CD1 TYR A 125 6.038 -24.445 34.297 1.00 19.95 C ANISOU 958 CD1 TYR A 125 3290 1901 2390 269 44 541 C ATOM 959 CD2 TYR A 125 3.974 -24.335 33.107 1.00 18.64 C ANISOU 959 CD2 TYR A 125 3039 1786 2259 278 268 -274 C ATOM 960 CE1 TYR A 125 5.397 -25.017 35.386 1.00 20.51 C ANISOU 960 CE1 TYR A 125 3591 1587 2615 -343 52 440 C ATOM 961 CE2 TYR A 125 3.335 -24.893 34.186 1.00 20.49 C ANISOU 961 CE2 TYR A 125 3356 1636 2795 -181 165 91 C ATOM 962 CZ TYR A 125 4.031 -25.241 35.306 1.00 21.76 C ANISOU 962 CZ TYR A 125 3781 1772 2713 -780 4 313 C ATOM 963 OH TYR A 125 3.381 -25.778 36.390 1.00 24.08 O ANISOU 963 OH TYR A 125 3959 2287 2902 -506 466 367 O ATOM 964 N VAL A 126 4.822 -24.551 29.425 1.00 17.38 N ANISOU 964 N VAL A 126 3016 1336 2252 455 -331 -258 N ATOM 965 CA VAL A 126 3.798 -25.306 28.700 1.00 16.17 C ANISOU 965 CA VAL A 126 2827 1318 1998 220 -3 -145 C ATOM 966 C VAL A 126 4.447 -26.315 27.748 1.00 17.70 C ANISOU 966 C VAL A 126 2655 1442 2629 57 105 -477 C ATOM 967 O VAL A 126 4.052 -27.475 27.652 1.00 18.49 O ANISOU 967 O VAL A 126 3206 1145 2675 307 -171 -113 O ATOM 968 CB VAL A 126 2.882 -24.342 27.931 1.00 15.46 C ANISOU 968 CB VAL A 126 2362 1517 1995 37 190 96 C ATOM 969 CG1 VAL A 126 2.006 -25.125 26.964 1.00 17.21 C ANISOU 969 CG1 VAL A 126 2830 1179 2530 186 -245 -16 C ATOM 970 CG2 VAL A 126 2.061 -23.514 28.915 1.00 15.84 C ANISOU 970 CG2 VAL A 126 2225 1651 2143 96 218 33 C ATOM 971 N ARG A 127 5.416 -25.930 26.937 1.00 16.69 N ANISOU 971 N ARG A 127 2518 1875 1947 -21 -201 -575 N ATOM 972 CA ARG A 127 6.014 -26.812 25.944 1.00 16.51 C ANISOU 972 CA ARG A 127 3069 1510 1694 117 -213 -201 C ATOM 973 C ARG A 127 6.781 -27.963 26.549 1.00 18.59 C ANISOU 973 C ARG A 127 3112 1677 2275 248 -228 -83 C ATOM 974 O ARG A 127 7.011 -28.945 25.841 1.00 21.76 O ANISOU 974 O ARG A 127 3969 2067 2234 777 475 -78 O ATOM 975 CB ARG A 127 6.926 -26.014 25.027 1.00 18.39 C ANISOU 975 CB ARG A 127 2955 1798 2236 523 204 24 C ATOM 976 CG ARG A 127 6.188 -24.970 24.183 1.00 17.82 C ANISOU 976 CG ARG A 127 3211 1184 2377 400 272 -51 C ATOM 977 CD ARG A 127 7.104 -24.313 23.165 1.00 16.83 C ANISOU 977 CD ARG A 127 2540 1361 2495 286 -14 -4 C ATOM 978 NE ARG A 127 6.576 -23.046 22.706 1.00 19.80 N ANISOU 978 NE ARG A 127 3871 1449 2203 375 -139 109 N ATOM 979 CZ ARG A 127 6.211 -22.663 21.502 1.00 16.44 C ANISOU 979 CZ ARG A 127 2479 1713 2055 490 16 -116 C ATOM 980 NH1 ARG A 127 6.269 -23.465 20.438 1.00 19.67 N ANISOU 980 NH1 ARG A 127 2888 2135 2452 394 -97 -567 N ATOM 981 NH2 ARG A 127 5.747 -21.427 21.330 1.00 17.43 N ANISOU 981 NH2 ARG A 127 3055 1525 2042 240 -44 107 N ATOM 982 N ARG A 128 7.159 -27.901 27.814 1.00 19.61 N ANISOU 982 N ARG A 128 3463 1858 2131 737 -113 131 N ATOM 983 CA ARG A 128 7.809 -29.100 28.367 1.00 22.20 C ANISOU 983 CA ARG A 128 3382 2042 3012 666 -260 448 C ATOM 984 C ARG A 128 6.767 -29.997 29.050 1.00 21.33 C ANISOU 984 C ARG A 128 3728 1844 2533 966 478 133 C ATOM 985 O ARG A 128 7.131 -31.029 29.617 1.00 27.12 O ANISOU 985 O ARG A 128 3973 2137 4195 1016 611 861 O ATOM 986 CB ARG A 128 9.005 -28.715 29.197 1.00 27.97 C ANISOU 986 CB ARG A 128 3939 2698 3989 743 -1116 425 C ATOM 987 CG ARG A 128 8.839 -27.969 30.434 1.00 32.33 C ANISOU 987 CG ARG A 128 5280 3297 3707 849 -1767 368 C ATOM 988 CD ARG A 128 10.189 -27.898 31.200 1.00 31.28 C ANISOU 988 CD ARG A 128 4902 2311 4672 1143 -1717 -199 C ATOM 989 NE ARG A 128 9.842 -27.052 32.335 1.00 29.33 N ANISOU 989 NE ARG A 128 4921 2173 4052 1015 -1708 265 N ATOM 990 CZ ARG A 128 9.980 -25.732 32.366 1.00 28.21 C ANISOU 990 CZ ARG A 128 5585 2093 3040 1291 -770 498 C ATOM 991 NH1 ARG A 128 9.616 -25.078 33.462 1.00 27.76 N ANISOU 991 NH1 ARG A 128 3713 3273 3563 695 -1076 -529 N ATOM 992 NH2 ARG A 128 10.468 -25.018 31.363 1.00 28.14 N ANISOU 992 NH2 ARG A 128 3501 3334 3856 504 -830 804 N ATOM 993 N GLY A 129 5.484 -29.650 28.975 1.00 21.73 N ANISOU 993 N GLY A 129 3600 1571 3087 635 103 -126 N ATOM 994 CA GLY A 129 4.407 -30.490 29.515 1.00 21.96 C ANISOU 994 CA GLY A 129 3576 1673 3094 526 -126 -217 C ATOM 995 C GLY A 129 4.079 -30.244 30.968 1.00 24.67 C ANISOU 995 C GLY A 129 4623 1504 3245 -100 439 -253 C ATOM 996 O GLY A 129 3.269 -30.971 31.548 1.00 23.12 O ANISOU 996 O GLY A 129 3660 1736 3387 121 -182 213 O ATOM 997 N ALA A 130 4.689 -29.227 31.551 1.00 19.64 N ANISOU 997 N ALA A 130 3207 1469 2785 464 -155 132 N ATOM 998 CA ALA A 130 4.593 -29.055 33.010 1.00 19.91 C ANISOU 998 CA ALA A 130 2908 1842 2816 219 -35 189 C ATOM 999 C ALA A 130 3.209 -28.658 33.516 1.00 19.93 C ANISOU 999 C ALA A 130 2947 1838 2786 350 70 774 C ATOM 1000 O ALA A 130 2.909 -28.895 34.690 1.00 20.82 O ANISOU 1000 O ALA A 130 3176 2053 2681 356 25 626 O ATOM 1001 CB ALA A 130 5.637 -28.052 33.531 1.00 22.16 C ANISOU 1001 CB ALA A 130 2845 2076 3498 556 -875 29 C ATOM 1002 N TRP A 131 2.371 -28.068 32.673 1.00 18.86 N ANISOU 1002 N TRP A 131 2991 1603 2571 198 -192 328 N ATOM 1003 CA TRP A 131 1.048 -27.626 33.072 1.00 17.50 C ANISOU 1003 CA TRP A 131 2778 1893 1978 46 -429 146 C ATOM 1004 C TRP A 131 0.200 -28.810 33.497 1.00 19.63 C ANISOU 1004 C TRP A 131 3140 1923 2396 12 -231 337 C ATOM 1005 O TRP A 131 -0.723 -28.678 34.321 1.00 21.00 O ANISOU 1005 O TRP A 131 3258 1734 2986 -107 52 272 O ATOM 1006 CB TRP A 131 0.419 -26.779 31.956 1.00 18.94 C ANISOU 1006 CB TRP A 131 3439 1555 2203 528 -280 89 C ATOM 1007 CG TRP A 131 -0.741 -25.947 32.410 1.00 17.34 C ANISOU 1007 CG TRP A 131 2999 1528 2064 172 -150 91 C ATOM 1008 CD1 TRP A 131 -1.099 -25.601 33.676 1.00 17.85 C ANISOU 1008 CD1 TRP A 131 2376 2318 2088 -272 -241 -127 C ATOM 1009 CD2 TRP A 131 -1.714 -25.357 31.539 1.00 16.58 C ANISOU 1009 CD2 TRP A 131 2351 1898 2051 -135 -26 139 C ATOM 1010 NE1 TRP A 131 -2.245 -24.811 33.661 1.00 18.18 N ANISOU 1010 NE1 TRP A 131 2639 2142 2127 -142 109 21 N ATOM 1011 CE2 TRP A 131 -2.631 -24.657 32.346 1.00 17.18 C ANISOU 1011 CE2 TRP A 131 2705 1596 2226 -1 -136 -128 C ATOM 1012 CE3 TRP A 131 -1.849 -25.376 30.148 1.00 16.75 C ANISOU 1012 CE3 TRP A 131 2663 1637 2062 -240 -231 -56 C ATOM 1013 CZ2 TRP A 131 -3.705 -23.967 31.799 1.00 17.69 C ANISOU 1013 CZ2 TRP A 131 2227 1933 2561 -196 -86 -83 C ATOM 1014 CZ3 TRP A 131 -2.930 -24.676 29.597 1.00 17.45 C ANISOU 1014 CZ3 TRP A 131 2646 1722 2262 -276 -341 54 C ATOM 1015 CH2 TRP A 131 -3.831 -23.987 30.434 1.00 18.01 C ANISOU 1015 CH2 TRP A 131 2642 1653 2546 -217 -247 140 C ATOM 1016 N LYS A 132 0.464 -30.019 32.977 1.00 21.45 N ANISOU 1016 N LYS A 132 3204 1981 2966 -220 125 139 N ATOM 1017 CA LYS A 132 -0.302 -31.162 33.410 1.00 23.01 C ANISOU 1017 CA LYS A 132 3286 2133 3323 -419 367 -43 C ATOM 1018 C LYS A 132 -0.107 -31.473 34.890 1.00 23.38 C ANISOU 1018 C LYS A 132 3358 2092 3435 -141 565 362 C ATOM 1019 O LYS A 132 -0.906 -32.174 35.507 1.00 33.28 O ANISOU 1019 O LYS A 132 5120 3330 4193 -1564 664 766 O ATOM 1020 CB LYS A 132 0.075 -32.411 32.575 1.00 26.00 C ANISOU 1020 CB LYS A 132 3962 2068 3847 -372 508 -161 C ATOM 1021 CG LYS A 132 -0.198 -32.145 31.111 1.00 35.70 C ANISOU 1021 CG LYS A 132 7295 2803 3464 -666 1004 -284 C ATOM 1022 CD LYS A 132 -0.382 -33.421 30.315 1.00 45.28 C ANISOU 1022 CD LYS A 132 10082 3530 3593 -1588 1914 -867 C ATOM 1023 CE LYS A 132 0.645 -33.557 29.214 1.00 52.48 C ANISOU 1023 CE LYS A 132 10608 4234 5096 -1066 2851 -1380 C ATOM 1024 NZ LYS A 132 2.075 -33.465 29.620 1.00 61.04 N ANISOU 1024 NZ LYS A 132 10241 4419 8533 -1603 2940 1326 N ATOM 1025 N PHE A 133 0.942 -30.959 35.505 1.00 24.44 N ANISOU 1025 N PHE A 133 4307 1764 3215 -480 26 741 N ATOM 1026 CA PHE A 133 1.198 -31.243 36.910 1.00 27.23 C ANISOU 1026 CA PHE A 133 4853 2061 3431 10 -111 1116 C ATOM 1027 C PHE A 133 0.926 -30.095 37.834 1.00 25.54 C ANISOU 1027 C PHE A 133 4292 2331 3082 -355 -856 816 C ATOM 1028 O PHE A 133 1.122 -30.200 39.042 1.00 33.80 O ANISOU 1028 O PHE A 133 6138 3714 2989 -110 -350 1123 O ATOM 1029 CB PHE A 133 2.675 -31.691 36.994 1.00 30.79 C ANISOU 1029 CB PHE A 133 4909 2684 4104 171 -259 1271 C ATOM 1030 CG PHE A 133 2.881 -32.904 36.084 1.00 34.80 C ANISOU 1030 CG PHE A 133 5582 2823 4818 995 -323 1089 C ATOM 1031 CD1 PHE A 133 3.476 -32.749 34.839 1.00 39.13 C ANISOU 1031 CD1 PHE A 133 7618 2246 5003 935 386 837 C ATOM 1032 CD2 PHE A 133 2.469 -34.164 36.482 1.00 37.38 C ANISOU 1032 CD2 PHE A 133 6545 2695 4963 922 353 778 C ATOM 1033 CE1 PHE A 133 3.645 -33.849 34.011 1.00 43.11 C ANISOU 1033 CE1 PHE A 133 8542 2535 5301 1127 5 509 C ATOM 1034 CE2 PHE A 133 2.614 -35.258 35.662 1.00 42.49 C ANISOU 1034 CE2 PHE A 133 7362 3022 5759 1035 510 281 C ATOM 1035 CZ PHE A 133 3.190 -35.085 34.419 1.00 43.10 C ANISOU 1035 CZ PHE A 133 7998 2473 5903 1000 864 -11 C ATOM 1036 N GLY A 134 0.489 -28.946 37.348 1.00 23.97 N ANISOU 1036 N GLY A 134 3623 2118 3367 -351 -765 439 N ATOM 1037 CA GLY A 134 0.151 -27.853 38.242 1.00 26.69 C ANISOU 1037 CA GLY A 134 5002 2109 3029 -769 -445 471 C ATOM 1038 C GLY A 134 0.209 -26.543 37.475 1.00 23.30 C ANISOU 1038 C GLY A 134 4156 2238 2460 23 -438 530 C ATOM 1039 O GLY A 134 0.758 -26.494 36.385 1.00 21.99 O ANISOU 1039 O GLY A 134 3265 2562 2527 276 -597 545 O ATOM 1040 N ASP A 135 -0.296 -25.475 38.053 1.00 21.42 N ANISOU 1040 N ASP A 135 3631 2136 2371 -735 -196 350 N ATOM 1041 CA ASP A 135 -0.232 -24.159 37.523 1.00 18.71 C ANISOU 1041 CA ASP A 135 2504 2175 2428 -99 1 449 C ATOM 1042 C ASP A 135 1.122 -23.507 37.775 1.00 16.91 C ANISOU 1042 C ASP A 135 2558 1545 2322 54 -128 334 C ATOM 1043 O ASP A 135 1.867 -23.748 38.706 1.00 19.51 O ANISOU 1043 O ASP A 135 2781 2440 2191 -167 -147 484 O ATOM 1044 CB ASP A 135 -1.331 -23.294 38.162 1.00 21.23 C ANISOU 1044 CB ASP A 135 2648 3115 2305 -19 126 27 C ATOM 1045 CG ASP A 135 -2.690 -23.693 37.608 1.00 28.71 C ANISOU 1045 CG ASP A 135 2460 4990 3460 68 31 -638 C ATOM 1046 OD1 ASP A 135 -2.860 -24.265 36.528 1.00 30.14 O ANISOU 1046 OD1 ASP A 135 2706 5764 2982 -1478 294 -287 O ATOM 1047 OD2 ASP A 135 -3.616 -23.354 38.353 1.00 51.44 O ANISOU 1047 OD2 ASP A 135 2881 12099 4563 -1218 1060 -2726 O ATOM 1048 N PHE A 136 1.405 -22.571 36.859 1.00 17.21 N ANISOU 1048 N PHE A 136 2644 1319 2575 164 -116 385 N ATOM 1049 CA PHE A 136 2.558 -21.700 36.980 1.00 17.00 C ANISOU 1049 CA PHE A 136 2861 1469 2128 29 70 261 C ATOM 1050 C PHE A 136 2.401 -20.746 38.150 1.00 18.39 C ANISOU 1050 C PHE A 136 2704 2110 2174 -17 135 -44 C ATOM 1051 O PHE A 136 1.274 -20.427 38.552 1.00 16.94 O ANISOU 1051 O PHE A 136 2656 1866 1913 -76 128 193 O ATOM 1052 CB PHE A 136 2.704 -20.899 35.690 1.00 18.41 C ANISOU 1052 CB PHE A 136 2979 1939 2075 -200 15 350 C ATOM 1053 CG PHE A 136 4.035 -20.215 35.493 1.00 15.88 C ANISOU 1053 CG PHE A 136 2757 1439 1837 161 -23 254 C ATOM 1054 CD1 PHE A 136 5.090 -20.939 34.980 1.00 19.57 C ANISOU 1054 CD1 PHE A 136 2859 1753 2822 336 -40 -8 C ATOM 1055 CD2 PHE A 136 4.193 -18.864 35.789 1.00 17.46 C ANISOU 1055 CD2 PHE A 136 3309 1401 1922 -25 470 375 C ATOM 1056 CE1 PHE A 136 6.308 -20.345 34.737 1.00 21.66 C ANISOU 1056 CE1 PHE A 136 3073 2264 2894 245 555 348 C ATOM 1057 CE2 PHE A 136 5.412 -18.254 35.574 1.00 19.41 C ANISOU 1057 CE2 PHE A 136 3364 2002 2007 -412 314 -14 C ATOM 1058 CZ PHE A 136 6.461 -19.000 35.058 1.00 20.34 C ANISOU 1058 CZ PHE A 136 3191 2219 2320 -140 368 645 C ATOM 1059 N LYS A 137 3.515 -20.303 38.704 1.00 16.14 N ANISOU 1059 N LYS A 137 2632 1663 1838 430 -124 340 N ATOM 1060 CA LYS A 137 3.498 -19.358 39.811 1.00 16.13 C ANISOU 1060 CA LYS A 137 2493 1650 1984 368 -158 255 C ATOM 1061 C LYS A 137 2.795 -18.052 39.451 1.00 15.14 C ANISOU 1061 C LYS A 137 2474 1414 1865 65 -94 270 C ATOM 1062 O LYS A 137 2.674 -17.676 38.293 1.00 15.56 O ANISOU 1062 O LYS A 137 2065 1948 1901 272 -300 341 O ATOM 1063 CB LYS A 137 4.939 -19.086 40.259 1.00 18.02 C ANISOU 1063 CB LYS A 137 2596 1989 2262 253 -220 200 C ATOM 1064 CG LYS A 137 5.717 -18.276 39.243 1.00 18.33 C ANISOU 1064 CG LYS A 137 2389 2100 2475 287 -152 230 C ATOM 1065 CD LYS A 137 7.104 -17.954 39.753 1.00 21.51 C ANISOU 1065 CD LYS A 137 2507 3255 2412 -23 -221 323 C ATOM 1066 CE LYS A 137 7.985 -17.389 38.659 1.00 22.03 C ANISOU 1066 CE LYS A 137 2440 3356 2573 80 -205 547 C ATOM 1067 NZ LYS A 137 9.332 -17.071 39.229 1.00 30.10 N ANISOU 1067 NZ LYS A 137 2716 5736 2984 -963 -19 -27 N ATOM 1068 N LEU A 138 2.362 -17.336 40.486 1.00 15.05 N ANISOU 1068 N LEU A 138 2108 1562 2048 131 11 213 N ATOM 1069 CA LEU A 138 1.834 -15.980 40.280 1.00 14.50 C ANISOU 1069 CA LEU A 138 2066 1506 1939 76 21 253 C ATOM 1070 C LEU A 138 2.978 -15.034 39.942 1.00 15.04 C ANISOU 1070 C LEU A 138 2104 1755 1854 -110 -153 340 C ATOM 1071 O LEU A 138 4.094 -15.149 40.450 1.00 17.74 O ANISOU 1071 O LEU A 138 2313 1906 2522 -198 -559 589 O ATOM 1072 CB LEU A 138 1.066 -15.508 41.518 1.00 15.48 C ANISOU 1072 CB LEU A 138 2151 1541 2190 75 143 172 C ATOM 1073 CG LEU A 138 -0.038 -16.449 41.971 1.00 17.00 C ANISOU 1073 CG LEU A 138 2288 2012 2159 -21 166 556 C ATOM 1074 CD1 LEU A 138 -0.830 -15.861 43.126 1.00 22.32 C ANISOU 1074 CD1 LEU A 138 3260 2552 2668 -152 937 374 C ATOM 1075 CD2 LEU A 138 -0.959 -16.783 40.797 1.00 18.52 C ANISOU 1075 CD2 LEU A 138 2062 2480 2493 -259 -33 737 C ATOM 1076 N THR A 139 2.631 -14.085 39.075 1.00 13.60 N ANISOU 1076 N THR A 139 1606 1641 1922 63 121 257 N ATOM 1077 CA THR A 139 3.599 -13.102 38.602 1.00 13.37 C ANISOU 1077 CA THR A 139 1826 1649 1603 -19 213 87 C ATOM 1078 C THR A 139 3.210 -11.711 39.034 1.00 13.48 C ANISOU 1078 C THR A 139 1771 1626 1725 85 37 56 C ATOM 1079 O THR A 139 2.587 -11.516 40.069 1.00 14.54 O ANISOU 1079 O THR A 139 1974 1625 1926 122 242 -14 O ATOM 1080 CB THR A 139 3.809 -13.288 37.078 1.00 13.99 C ANISOU 1080 CB THR A 139 2339 1456 1520 147 76 212 C ATOM 1081 OG1 THR A 139 2.591 -12.911 36.447 1.00 17.57 O ANISOU 1081 OG1 THR A 139 2790 1854 2031 169 -397 327 O ATOM 1082 CG2 THR A 139 4.206 -14.703 36.750 1.00 17.39 C ANISOU 1082 CG2 THR A 139 3025 1533 2051 302 493 41 C ATOM 1083 N THR A 140 3.607 -10.670 38.292 1.00 15.13 N ANISOU 1083 N THR A 140 2208 1612 1928 -28 151 64 N ATOM 1084 CA THR A 140 3.529 -9.286 38.714 1.00 14.58 C ANISOU 1084 CA THR A 140 1825 1623 2092 64 65 52 C ATOM 1085 C THR A 140 2.708 -8.456 37.755 1.00 14.18 C ANISOU 1085 C THR A 140 1754 1767 1868 39 178 89 C ATOM 1086 O THR A 140 2.968 -8.466 36.564 1.00 14.49 O ANISOU 1086 O THR A 140 1770 1878 1856 -25 156 -192 O ATOM 1087 CB THR A 140 4.958 -8.713 38.773 1.00 15.18 C ANISOU 1087 CB THR A 140 1911 1623 2234 -48 -78 367 C ATOM 1088 OG1 THR A 140 5.746 -9.504 39.705 1.00 18.20 O ANISOU 1088 OG1 THR A 140 2276 2047 2593 -92 -533 446 O ATOM 1089 CG2 THR A 140 4.957 -7.294 39.251 1.00 16.69 C ANISOU 1089 CG2 THR A 140 2393 1806 2143 -207 -129 150 C ATOM 1090 N LYS A 141 1.754 -7.705 38.300 1.00 13.59 N ANISOU 1090 N LYS A 141 2062 1545 1558 134 95 66 N ATOM 1091 CA LYS A 141 0.931 -6.810 37.518 1.00 13.71 C ANISOU 1091 CA LYS A 141 1981 1630 1599 51 25 83 C ATOM 1092 C LYS A 141 1.725 -5.634 36.982 1.00 13.66 C ANISOU 1092 C LYS A 141 1984 1490 1717 -30 -169 86 C ATOM 1093 O LYS A 141 2.512 -5.025 37.729 1.00 14.65 O ANISOU 1093 O LYS A 141 2002 1812 1751 28 -133 -204 O ATOM 1094 CB LYS A 141 -0.188 -6.303 38.436 1.00 14.62 C ANISOU 1094 CB LYS A 141 1999 1622 1933 -12 49 -243 C ATOM 1095 CG LYS A 141 -1.148 -5.326 37.819 1.00 14.91 C ANISOU 1095 CG LYS A 141 2153 1584 1926 92 276 -91 C ATOM 1096 CD LYS A 141 -2.370 -5.078 38.676 1.00 17.89 C ANISOU 1096 CD LYS A 141 2543 1815 2441 362 609 -78 C ATOM 1097 CE LYS A 141 -3.446 -4.221 37.999 1.00 23.93 C ANISOU 1097 CE LYS A 141 2128 3388 3575 481 403 589 C ATOM 1098 NZ LYS A 141 -4.557 -4.030 38.997 1.00 37.57 N ANISOU 1098 NZ LYS A 141 2619 4945 6713 770 1930 160 N ATOM 1099 N PHE A 142 1.529 -5.350 35.706 1.00 12.97 N ANISOU 1099 N PHE A 142 1831 1396 1702 -189 -156 -22 N ATOM 1100 CA PHE A 142 2.120 -4.170 35.095 1.00 12.98 C ANISOU 1100 CA PHE A 142 1527 1668 1738 -14 -157 193 C ATOM 1101 C PHE A 142 1.261 -2.918 35.320 1.00 13.18 C ANISOU 1101 C PHE A 142 1518 1443 2047 -215 108 147 C ATOM 1102 O PHE A 142 1.836 -1.927 35.765 1.00 13.74 O ANISOU 1102 O PHE A 142 1756 1725 1738 -239 -182 -8 O ATOM 1103 CB PHE A 142 2.349 -4.403 33.594 1.00 13.85 C ANISOU 1103 CB PHE A 142 1894 1585 1783 -171 -74 81 C ATOM 1104 CG PHE A 142 2.820 -3.216 32.792 1.00 13.83 C ANISOU 1104 CG PHE A 142 1461 1865 1929 12 187 229 C ATOM 1105 CD1 PHE A 142 3.758 -2.307 33.305 1.00 14.51 C ANISOU 1105 CD1 PHE A 142 1595 1517 2402 51 -102 336 C ATOM 1106 CD2 PHE A 142 2.348 -2.991 31.509 1.00 15.10 C ANISOU 1106 CD2 PHE A 142 2472 1485 1780 22 86 82 C ATOM 1107 CE1 PHE A 142 4.181 -1.224 32.584 1.00 14.71 C ANISOU 1107 CE1 PHE A 142 2399 1276 1914 173 608 -28 C ATOM 1108 CE2 PHE A 142 2.801 -1.895 30.778 1.00 16.76 C ANISOU 1108 CE2 PHE A 142 2328 1562 2477 110 -3 508 C ATOM 1109 CZ PHE A 142 3.720 -1.028 31.299 1.00 15.19 C ANISOU 1109 CZ PHE A 142 2109 1575 2085 175 410 84 C ATOM 1110 N SER A 143 0.002 -2.956 34.959 1.00 13.47 N ANISOU 1110 N SER A 143 1540 1415 2162 39 98 -391 N ATOM 1111 CA SER A 143 -0.806 -1.740 35.028 1.00 14.62 C ANISOU 1111 CA SER A 143 1679 1587 2290 189 615 -346 C ATOM 1112 C SER A 143 -0.717 -1.113 36.417 1.00 13.93 C ANISOU 1112 C SER A 143 1628 1528 2135 26 652 -252 C ATOM 1113 O SER A 143 -0.813 -1.805 37.442 1.00 16.50 O ANISOU 1113 O SER A 143 2257 1688 2325 -277 351 -18 O ATOM 1114 CB SER A 143 -2.283 -2.070 34.758 1.00 18.00 C ANISOU 1114 CB SER A 143 1617 2496 2725 384 145 -501 C ATOM 1115 OG SER A 143 -2.530 -2.266 33.399 1.00 18.86 O ANISOU 1115 OG SER A 143 2395 2110 2661 -173 117 -23 O ATOM 1116 N GLY A 144 -0.459 0.186 36.399 1.00 15.66 N ANISOU 1116 N GLY A 144 2603 1650 1695 -157 219 -61 N ATOM 1117 CA GLY A 144 -0.422 0.952 37.641 1.00 14.82 C ANISOU 1117 CA GLY A 144 2208 1537 1887 97 306 -196 C ATOM 1118 C GLY A 144 0.953 1.095 38.231 1.00 16.29 C ANISOU 1118 C GLY A 144 2292 1929 1968 -153 293 -393 C ATOM 1119 O GLY A 144 1.127 1.923 39.150 1.00 18.09 O ANISOU 1119 O GLY A 144 2858 1856 2161 -304 107 -381 O ATOM 1120 N LYS A 145 1.922 0.320 37.735 1.00 16.04 N ANISOU 1120 N LYS A 145 1934 2059 2101 -317 376 -293 N ATOM 1121 CA LYS A 145 3.276 0.420 38.293 1.00 16.23 C ANISOU 1121 CA LYS A 145 2319 1638 2209 -250 -135 -208 C ATOM 1122 C LYS A 145 4.003 1.684 37.857 1.00 15.37 C ANISOU 1122 C LYS A 145 2131 1751 1957 -283 -135 -188 C ATOM 1123 O LYS A 145 3.650 2.269 36.810 1.00 16.48 O ANISOU 1123 O LYS A 145 2489 1705 2068 57 -116 -119 O ATOM 1124 CB LYS A 145 4.092 -0.819 37.887 1.00 18.66 C ANISOU 1124 CB LYS A 145 2661 1782 2647 176 -293 75 C ATOM 1125 CG LYS A 145 3.532 -2.098 38.483 1.00 24.42 C ANISOU 1125 CG LYS A 145 5367 1610 2302 -530 -1040 59 C ATOM 1126 CD LYS A 145 3.831 -2.163 39.981 1.00 32.42 C ANISOU 1126 CD LYS A 145 7667 1786 2867 -779 -2659 665 C ATOM 1127 CE LYS A 145 3.072 -3.255 40.729 1.00 39.58 C ANISOU 1127 CE LYS A 145 9985 2428 2625 -1214 -2155 1051 C ATOM 1128 NZ LYS A 145 3.070 -4.546 40.110 1.00 28.56 N ANISOU 1128 NZ LYS A 145 4587 2138 4125 -415 992 903 N ATOM 1129 N ARG A 146 4.948 2.145 38.663 1.00 15.82 N ANISOU 1129 N ARG A 146 2275 1605 2132 -211 -180 -390 N ATOM 1130 CA ARG A 146 5.695 3.381 38.382 1.00 15.39 C ANISOU 1130 CA ARG A 146 2419 1481 1946 -210 62 -607 C ATOM 1131 C ARG A 146 6.755 3.112 37.336 1.00 14.59 C ANISOU 1131 C ARG A 146 2106 1611 1827 18 -223 -373 C ATOM 1132 O ARG A 146 7.653 2.271 37.540 1.00 16.28 O ANISOU 1132 O ARG A 146 2194 2017 1975 181 -231 -54 O ATOM 1133 CB ARG A 146 6.368 3.875 39.668 1.00 19.77 C ANISOU 1133 CB ARG A 146 3079 2389 2043 -855 151 -783 C ATOM 1134 CG ARG A 146 5.398 4.176 40.789 1.00 18.26 C ANISOU 1134 CG ARG A 146 3176 1936 1824 -218 -114 -765 C ATOM 1135 CD ARG A 146 6.160 4.387 42.086 1.00 20.07 C ANISOU 1135 CD ARG A 146 3153 2523 1950 -279 -251 -666 C ATOM 1136 NE ARG A 146 6.803 3.127 42.501 1.00 20.67 N ANISOU 1136 NE ARG A 146 2707 2776 2371 -202 -205 -484 N ATOM 1137 CZ ARG A 146 7.699 3.038 43.468 1.00 23.06 C ANISOU 1137 CZ ARG A 146 3235 3077 2450 152 -492 -846 C ATOM 1138 NH1 ARG A 146 8.060 4.131 44.115 1.00 24.69 N ANISOU 1138 NH1 ARG A 146 3288 3305 2789 -310 -496 -861 N ATOM 1139 NH2 ARG A 146 8.242 1.876 43.806 1.00 22.50 N ANISOU 1139 NH2 ARG A 146 3388 3218 1944 31 -255 -354 N ATOM 1140 N VAL A 147 6.651 3.804 36.212 1.00 14.55 N ANISOU 1140 N VAL A 147 2000 1502 2027 29 -104 -194 N ATOM 1141 CA VAL A 147 7.608 3.700 35.112 1.00 14.44 C ANISOU 1141 CA VAL A 147 1965 1485 2037 75 -87 -230 C ATOM 1142 C VAL A 147 8.481 4.941 35.079 1.00 15.76 C ANISOU 1142 C VAL A 147 2055 1610 2322 1 -102 128 C ATOM 1143 O VAL A 147 7.986 6.045 34.953 1.00 16.34 O ANISOU 1143 O VAL A 147 2232 1540 2436 -23 -255 -162 O ATOM 1144 CB VAL A 147 6.910 3.470 33.768 1.00 14.64 C ANISOU 1144 CB VAL A 147 2229 1327 2009 401 -173 -87 C ATOM 1145 CG1 VAL A 147 7.948 3.487 32.631 1.00 18.15 C ANISOU 1145 CG1 VAL A 147 2489 2399 2009 20 -60 -196 C ATOM 1146 CG2 VAL A 147 6.138 2.166 33.785 1.00 17.06 C ANISOU 1146 CG2 VAL A 147 2225 1707 2551 31 -494 -135 C ATOM 1147 N GLY A 148 9.782 4.706 35.242 1.00 15.98 N ANISOU 1147 N GLY A 148 2035 1512 2527 -109 -178 -138 N ATOM 1148 CA GLY A 148 10.795 5.746 35.132 1.00 16.64 C ANISOU 1148 CA GLY A 148 2081 1702 2539 -145 435 -234 C ATOM 1149 C GLY A 148 11.526 5.618 33.791 1.00 15.90 C ANISOU 1149 C GLY A 148 2078 1748 2216 134 102 -366 C ATOM 1150 O GLY A 148 11.880 4.500 33.434 1.00 16.93 O ANISOU 1150 O GLY A 148 2425 1830 2177 356 -152 -326 O ATOM 1151 N ILE A 149 11.742 6.765 33.132 1.00 14.99 N ANISOU 1151 N ILE A 149 1786 1740 2171 -72 239 -472 N ATOM 1152 CA ILE A 149 12.395 6.740 31.846 1.00 15.46 C ANISOU 1152 CA ILE A 149 1824 1821 2229 -28 166 -394 C ATOM 1153 C ILE A 149 13.611 7.668 31.849 1.00 16.85 C ANISOU 1153 C ILE A 149 2136 2135 2130 -408 367 -546 C ATOM 1154 O ILE A 149 13.520 8.796 32.303 1.00 17.34 O ANISOU 1154 O ILE A 149 2395 1949 2245 -389 102 -349 O ATOM 1155 CB ILE A 149 11.426 7.148 30.737 1.00 17.92 C ANISOU 1155 CB ILE A 149 2085 2426 2299 133 29 -251 C ATOM 1156 CG1 ILE A 149 10.163 6.280 30.787 1.00 18.74 C ANISOU 1156 CG1 ILE A 149 2033 2602 2485 134 -263 -82 C ATOM 1157 CG2 ILE A 149 12.052 7.082 29.368 1.00 22.51 C ANISOU 1157 CG2 ILE A 149 2651 3628 2273 30 100 -74 C ATOM 1158 CD1 ILE A 149 9.052 6.776 29.932 1.00 18.78 C ANISOU 1158 CD1 ILE A 149 2388 2558 2189 304 -374 -203 C ATOM 1159 N ILE A 150 14.707 7.120 31.349 1.00 15.28 N ANISOU 1159 N ILE A 150 1852 2047 1906 -291 -79 -194 N ATOM 1160 CA ILE A 150 15.964 7.855 31.236 1.00 15.63 C ANISOU 1160 CA ILE A 150 1919 1922 2097 -242 61 -71 C ATOM 1161 C ILE A 150 16.028 8.357 29.792 1.00 17.42 C ANISOU 1161 C ILE A 150 2431 2018 2171 -280 80 49 C ATOM 1162 O ILE A 150 16.270 7.596 28.854 1.00 18.59 O ANISOU 1162 O ILE A 150 2420 2503 2140 -246 127 -165 O ATOM 1163 CB ILE A 150 17.205 7.055 31.590 1.00 16.62 C ANISOU 1163 CB ILE A 150 1809 2341 2162 -129 199 -51 C ATOM 1164 CG1 ILE A 150 17.108 6.516 33.012 1.00 19.50 C ANISOU 1164 CG1 ILE A 150 2383 2609 2416 -476 -283 365 C ATOM 1165 CG2 ILE A 150 18.440 7.900 31.379 1.00 18.59 C ANISOU 1165 CG2 ILE A 150 1895 2782 2386 -340 104 12 C ATOM 1166 CD1 ILE A 150 18.039 5.400 33.349 1.00 24.05 C ANISOU 1166 CD1 ILE A 150 2959 3370 2811 350 120 580 C ATOM 1167 N GLY A 151 15.786 9.657 29.690 1.00 18.49 N ANISOU 1167 N GLY A 151 2446 2058 2521 -230 -332 177 N ATOM 1168 CA GLY A 151 15.651 10.269 28.369 1.00 20.95 C ANISOU 1168 CA GLY A 151 3012 2353 2596 -220 -607 303 C ATOM 1169 C GLY A 151 14.185 10.497 28.032 1.00 22.14 C ANISOU 1169 C GLY A 151 3050 2412 2952 -376 -786 471 C ATOM 1170 O GLY A 151 13.383 9.574 28.143 1.00 29.26 O ANISOU 1170 O GLY A 151 3368 2351 5397 -572 -1703 707 O ATOM 1171 N LEU A 152 13.849 11.704 27.628 1.00 19.52 N ANISOU 1171 N LEU A 152 2509 2257 2650 -139 -8 142 N ATOM 1172 CA LEU A 152 12.480 12.003 27.199 1.00 18.95 C ANISOU 1172 CA LEU A 152 2333 2589 2280 -136 329 275 C ATOM 1173 C LEU A 152 12.486 12.693 25.835 1.00 18.87 C ANISOU 1173 C LEU A 152 2818 2288 2065 -327 49 43 C ATOM 1174 O LEU A 152 11.814 13.691 25.567 1.00 23.15 O ANISOU 1174 O LEU A 152 3210 2638 2946 -111 -346 346 O ATOM 1175 CB LEU A 152 11.717 12.812 28.246 1.00 19.58 C ANISOU 1175 CB LEU A 152 2663 2688 2089 40 154 231 C ATOM 1176 CG LEU A 152 10.198 12.609 28.152 1.00 21.36 C ANISOU 1176 CG LEU A 152 2552 2855 2708 322 444 352 C ATOM 1177 CD1 LEU A 152 9.805 11.235 28.636 1.00 22.26 C ANISOU 1177 CD1 LEU A 152 3005 2887 2566 -328 61 -9 C ATOM 1178 CD2 LEU A 152 9.449 13.709 28.905 1.00 20.61 C ANISOU 1178 CD2 LEU A 152 2637 2997 2198 7 278 -19 C ATOM 1179 N GLY A 153 13.265 12.104 24.934 1.00 19.80 N ANISOU 1179 N GLY A 153 2948 2608 1967 -607 74 -145 N ATOM 1180 CA GLY A 153 13.290 12.444 23.529 1.00 18.78 C ANISOU 1180 CA GLY A 153 2371 2707 2057 -342 0 -31 C ATOM 1181 C GLY A 153 12.195 11.620 22.841 1.00 16.46 C ANISOU 1181 C GLY A 153 2272 2219 1762 -328 60 418 C ATOM 1182 O GLY A 153 11.262 11.146 23.480 1.00 17.62 O ANISOU 1182 O GLY A 153 2449 2072 2173 -249 314 487 O ATOM 1183 N ARG A 154 12.348 11.407 21.543 1.00 18.21 N ANISOU 1183 N ARG A 154 2795 2266 1857 -673 237 129 N ATOM 1184 CA ARG A 154 11.314 10.748 20.775 1.00 20.51 C ANISOU 1184 CA ARG A 154 3441 2045 2308 -704 -282 105 C ATOM 1185 C ARG A 154 10.982 9.350 21.299 1.00 17.78 C ANISOU 1185 C ARG A 154 2706 1903 2148 -261 197 89 C ATOM 1186 O ARG A 154 9.805 8.962 21.454 1.00 16.63 O ANISOU 1186 O ARG A 154 2540 1885 1895 -1 170 48 O ATOM 1187 CB ARG A 154 11.784 10.653 19.316 1.00 26.20 C ANISOU 1187 CB ARG A 154 5267 2742 1947 -1720 -427 319 C ATOM 1188 CG ARG A 154 11.720 11.954 18.539 1.00 37.60 C ANISOU 1188 CG ARG A 154 8375 2974 2937 -2882 -845 873 C ATOM 1189 CD ARG A 154 12.744 11.922 17.403 1.00 57.17 C ANISOU 1189 CD ARG A 154 11068 5847 4806 -5121 1483 1404 C ATOM 1190 NE ARG A 154 12.848 13.052 16.524 1.00 67.34 N ANISOU 1190 NE ARG A 154 12982 6381 6224 -5042 1596 2293 N ATOM 1191 CZ ARG A 154 13.715 14.050 16.558 1.00 72.97 C ANISOU 1191 CZ ARG A 154 13030 6495 8201 -5157 1535 3362 C ATOM 1192 NH1 ARG A 154 14.671 14.169 17.472 1.00 71.30 N ANISOU 1192 NH1 ARG A 154 10094 5371 11624 -3273 1373 2164 N ATOM 1193 NH2 ARG A 154 13.636 14.999 15.635 1.00 93.49 N ANISOU 1193 NH2 ARG A 154 18790 6062 10672 -5274 343 4243 N ATOM 1194 N ILE A 155 12.004 8.527 21.589 1.00 19.39 N ANISOU 1194 N ILE A 155 2466 2378 2523 -150 545 300 N ATOM 1195 CA ILE A 155 11.696 7.164 22.013 1.00 18.25 C ANISOU 1195 CA ILE A 155 2252 2089 2594 45 375 81 C ATOM 1196 C ILE A 155 11.178 7.149 23.435 1.00 16.36 C ANISOU 1196 C ILE A 155 2212 1607 2398 70 114 253 C ATOM 1197 O ILE A 155 10.198 6.437 23.746 1.00 17.02 O ANISOU 1197 O ILE A 155 2230 1885 2354 -195 -92 309 O ATOM 1198 CB ILE A 155 12.914 6.239 21.781 1.00 19.97 C ANISOU 1198 CB ILE A 155 2100 2757 2732 203 503 589 C ATOM 1199 CG1 ILE A 155 13.135 5.995 20.262 1.00 23.65 C ANISOU 1199 CG1 ILE A 155 2324 3842 2822 615 937 514 C ATOM 1200 CG2 ILE A 155 12.792 4.943 22.546 1.00 20.78 C ANISOU 1200 CG2 ILE A 155 2343 2692 2860 355 45 600 C ATOM 1201 CD1 ILE A 155 14.434 5.349 19.899 1.00 26.14 C ANISOU 1201 CD1 ILE A 155 2428 3718 3788 598 963 268 C ATOM 1202 N GLY A 156 11.752 7.943 24.315 1.00 18.05 N ANISOU 1202 N GLY A 156 2285 2000 2571 -523 599 81 N ATOM 1203 CA GLY A 156 11.274 7.987 25.685 1.00 17.26 C ANISOU 1203 CA GLY A 156 2165 2114 2281 -347 132 286 C ATOM 1204 C GLY A 156 9.831 8.446 25.763 1.00 16.50 C ANISOU 1204 C GLY A 156 2361 2115 1795 -51 204 151 C ATOM 1205 O GLY A 156 9.059 7.892 26.568 1.00 15.58 O ANISOU 1205 O GLY A 156 2094 1997 1830 -133 -49 272 O ATOM 1206 N LEU A 157 9.501 9.456 24.944 1.00 16.42 N ANISOU 1206 N LEU A 157 2203 1810 2226 -355 329 274 N ATOM 1207 CA LEU A 157 8.107 9.924 24.964 1.00 16.67 C ANISOU 1207 CA LEU A 157 2353 1989 1992 -158 45 292 C ATOM 1208 C LEU A 157 7.184 8.845 24.446 1.00 15.52 C ANISOU 1208 C LEU A 157 1932 1752 2212 124 347 183 C ATOM 1209 O LEU A 157 6.069 8.708 24.972 1.00 16.79 O ANISOU 1209 O LEU A 157 2083 1870 2427 95 505 308 O ATOM 1210 CB LEU A 157 7.954 11.176 24.148 1.00 19.25 C ANISOU 1210 CB LEU A 157 3365 1726 2223 -55 34 274 C ATOM 1211 CG LEU A 157 6.905 12.234 24.423 1.00 33.77 C ANISOU 1211 CG LEU A 157 6958 2720 3153 1890 1193 333 C ATOM 1212 CD1 LEU A 157 6.844 12.675 25.886 1.00 38.61 C ANISOU 1212 CD1 LEU A 157 7704 3766 3200 3207 40 -132 C ATOM 1213 CD2 LEU A 157 7.182 13.443 23.529 1.00 51.16 C ANISOU 1213 CD2 LEU A 157 14646 1685 3109 976 -2660 533 C ATOM 1214 N ALA A 158 7.592 8.132 23.418 1.00 15.36 N ANISOU 1214 N ALA A 158 2290 1633 1913 120 311 310 N ATOM 1215 CA ALA A 158 6.746 7.068 22.871 1.00 14.64 C ANISOU 1215 CA ALA A 158 1710 1854 2000 171 331 271 C ATOM 1216 C ALA A 158 6.538 5.955 23.883 1.00 14.51 C ANISOU 1216 C ALA A 158 1554 1892 2067 -10 136 352 C ATOM 1217 O ALA A 158 5.438 5.390 23.982 1.00 14.72 O ANISOU 1217 O ALA A 158 1593 1732 2270 -82 70 63 O ATOM 1218 CB ALA A 158 7.331 6.589 21.554 1.00 15.47 C ANISOU 1218 CB ALA A 158 1962 2083 1830 -20 105 178 C ATOM 1219 N VAL A 159 7.568 5.629 24.665 1.00 14.33 N ANISOU 1219 N VAL A 159 1745 1710 1987 -129 -53 101 N ATOM 1220 CA VAL A 159 7.401 4.637 25.723 1.00 14.19 C ANISOU 1220 CA VAL A 159 1944 1462 1985 181 -11 53 C ATOM 1221 C VAL A 159 6.437 5.154 26.771 1.00 12.71 C ANISOU 1221 C VAL A 159 1728 1229 1872 145 -107 178 C ATOM 1222 O VAL A 159 5.552 4.408 27.222 1.00 13.61 O ANISOU 1222 O VAL A 159 1869 1365 1937 24 -71 184 O ATOM 1223 CB VAL A 159 8.740 4.257 26.360 1.00 13.21 C ANISOU 1223 CB VAL A 159 1714 1483 1822 -1 208 85 C ATOM 1224 CG1 VAL A 159 8.564 3.403 27.606 1.00 13.70 C ANISOU 1224 CG1 VAL A 159 1406 2072 1729 52 203 275 C ATOM 1225 CG2 VAL A 159 9.603 3.553 25.313 1.00 15.29 C ANISOU 1225 CG2 VAL A 159 1883 2260 1668 173 254 30 C ATOM 1226 N ALA A 160 6.631 6.414 27.186 1.00 14.47 N ANISOU 1226 N ALA A 160 1858 1378 2261 35 228 3 N ATOM 1227 CA ALA A 160 5.765 7.003 28.198 1.00 15.47 C ANISOU 1227 CA ALA A 160 1954 1431 2494 357 150 -72 C ATOM 1228 C ALA A 160 4.300 6.963 27.780 1.00 15.83 C ANISOU 1228 C ALA A 160 1879 1670 2464 86 191 259 C ATOM 1229 O ALA A 160 3.415 6.628 28.586 1.00 15.78 O ANISOU 1229 O ALA A 160 2120 1612 2264 12 199 147 O ATOM 1230 CB ALA A 160 6.164 8.458 28.479 1.00 15.83 C ANISOU 1230 CB ALA A 160 2337 1649 2030 72 99 -195 C ATOM 1231 N GLU A 161 4.030 7.375 26.538 1.00 15.37 N ANISOU 1231 N GLU A 161 1765 1673 2402 60 300 268 N ATOM 1232 CA GLU A 161 2.652 7.439 26.049 1.00 14.41 C ANISOU 1232 CA GLU A 161 1739 1556 2181 193 402 128 C ATOM 1233 C GLU A 161 1.978 6.075 25.986 1.00 14.89 C ANISOU 1233 C GLU A 161 1806 1581 2272 133 279 199 C ATOM 1234 O GLU A 161 0.778 5.917 26.258 1.00 17.07 O ANISOU 1234 O GLU A 161 1781 1809 2897 108 290 151 O ATOM 1235 CB GLU A 161 2.677 8.148 24.674 1.00 16.83 C ANISOU 1235 CB GLU A 161 2304 1694 2397 222 269 385 C ATOM 1236 CG GLU A 161 3.020 9.636 24.893 1.00 20.04 C ANISOU 1236 CG GLU A 161 2469 1608 3537 218 355 498 C ATOM 1237 CD GLU A 161 3.443 10.383 23.655 1.00 22.86 C ANISOU 1237 CD GLU A 161 3142 2179 3363 -856 -339 592 C ATOM 1238 OE1 GLU A 161 3.546 9.776 22.558 1.00 25.81 O ANISOU 1238 OE1 GLU A 161 4060 2649 3098 -405 -557 673 O ATOM 1239 OE2 GLU A 161 3.708 11.626 23.778 1.00 35.40 O ANISOU 1239 OE2 GLU A 161 7166 2282 4001 -1604 -313 761 O ATOM 1240 N ARG A 162 2.745 5.039 25.643 1.00 13.96 N ANISOU 1240 N ARG A 162 1951 1497 1854 69 439 276 N ATOM 1241 CA ARG A 162 2.185 3.685 25.746 1.00 13.33 C ANISOU 1241 CA ARG A 162 1597 1529 1938 94 -62 342 C ATOM 1242 C ARG A 162 1.925 3.290 27.196 1.00 12.80 C ANISOU 1242 C ARG A 162 1494 1408 1961 50 -58 378 C ATOM 1243 O ARG A 162 0.858 2.775 27.538 1.00 14.46 O ANISOU 1243 O ARG A 162 1693 1614 2187 -137 309 -81 O ATOM 1244 CB ARG A 162 3.130 2.681 25.073 1.00 13.56 C ANISOU 1244 CB ARG A 162 1683 1501 1969 85 -76 226 C ATOM 1245 CG ARG A 162 3.100 2.756 23.553 1.00 13.27 C ANISOU 1245 CG ARG A 162 1294 1760 1989 58 -183 128 C ATOM 1246 CD ARG A 162 4.439 2.395 22.939 1.00 14.34 C ANISOU 1246 CD ARG A 162 1469 1945 2033 308 -176 -10 C ATOM 1247 NE ARG A 162 4.315 2.383 21.486 1.00 15.08 N ANISOU 1247 NE ARG A 162 2172 1575 1982 -358 116 -18 N ATOM 1248 CZ ARG A 162 4.227 3.434 20.689 1.00 14.41 C ANISOU 1248 CZ ARG A 162 1872 1681 1920 -118 40 -19 C ATOM 1249 NH1 ARG A 162 4.270 4.644 21.236 1.00 16.18 N ANISOU 1249 NH1 ARG A 162 2243 1618 2286 -331 -22 -7 N ATOM 1250 NH2 ARG A 162 4.104 3.274 19.392 1.00 18.42 N ANISOU 1250 NH2 ARG A 162 2879 2332 1787 -231 315 -14 N ATOM 1251 N ALA A 163 2.901 3.521 28.068 1.00 12.77 N ANISOU 1251 N ALA A 163 1553 1465 1834 240 -18 123 N ATOM 1252 CA ALA A 163 2.752 3.114 29.466 1.00 13.81 C ANISOU 1252 CA ALA A 163 1822 1652 1773 147 33 20 C ATOM 1253 C ALA A 163 1.627 3.879 30.144 1.00 14.35 C ANISOU 1253 C ALA A 163 2090 1456 1905 53 357 193 C ATOM 1254 O ALA A 163 0.967 3.286 31.016 1.00 14.35 O ANISOU 1254 O ALA A 163 1861 1684 1906 -206 155 150 O ATOM 1255 CB ALA A 163 4.054 3.252 30.245 1.00 15.10 C ANISOU 1255 CB ALA A 163 2207 1664 1867 96 -281 -169 C ATOM 1256 N GLU A 164 1.338 5.106 29.771 1.00 15.25 N ANISOU 1256 N GLU A 164 1738 1503 2551 21 358 263 N ATOM 1257 CA GLU A 164 0.231 5.806 30.375 1.00 15.58 C ANISOU 1257 CA GLU A 164 1918 1820 2183 218 106 -70 C ATOM 1258 C GLU A 164 -1.105 5.091 30.136 1.00 15.44 C ANISOU 1258 C GLU A 164 1678 1666 2522 434 110 -203 C ATOM 1259 O GLU A 164 -2.049 5.197 30.921 1.00 16.19 O ANISOU 1259 O GLU A 164 1983 1732 2435 198 270 -97 O ATOM 1260 CB GLU A 164 0.115 7.218 29.803 1.00 19.91 C ANISOU 1260 CB GLU A 164 2363 1607 3593 336 741 -29 C ATOM 1261 CG GLU A 164 1.054 8.248 30.325 1.00 23.24 C ANISOU 1261 CG GLU A 164 3120 1962 3747 -18 206 -17 C ATOM 1262 CD GLU A 164 0.731 9.602 29.690 1.00 20.80 C ANISOU 1262 CD GLU A 164 2562 1801 3540 -53 405 -186 C ATOM 1263 OE1 GLU A 164 1.207 9.903 28.583 1.00 25.05 O ANISOU 1263 OE1 GLU A 164 3436 2731 3351 196 318 169 O ATOM 1264 OE2 GLU A 164 -0.010 10.351 30.364 1.00 31.98 O ANISOU 1264 OE2 GLU A 164 4253 2458 5438 691 1822 -147 O ATOM 1265 N ALA A 165 -1.192 4.332 29.042 1.00 14.64 N ANISOU 1265 N ALA A 165 1789 1644 2130 308 -9 67 N ATOM 1266 CA ALA A 165 -2.457 3.632 28.707 1.00 15.06 C ANISOU 1266 CA ALA A 165 1770 2064 1889 237 121 16 C ATOM 1267 C ALA A 165 -2.670 2.410 29.586 1.00 15.52 C ANISOU 1267 C ALA A 165 1534 2048 2315 217 110 171 C ATOM 1268 O ALA A 165 -3.780 1.853 29.538 1.00 17.49 O ANISOU 1268 O ALA A 165 1809 2396 2440 -126 -159 81 O ATOM 1269 CB ALA A 165 -2.463 3.277 27.219 1.00 18.22 C ANISOU 1269 CB ALA A 165 2413 2555 1953 -29 42 -154 C ATOM 1270 N PHE A 166 -1.651 2.064 30.351 1.00 14.53 N ANISOU 1270 N PHE A 166 1534 1728 2259 35 80 104 N ATOM 1271 CA PHE A 166 -1.696 0.992 31.350 1.00 14.52 C ANISOU 1271 CA PHE A 166 1493 1811 2211 -63 -183 20 C ATOM 1272 C PHE A 166 -1.822 1.606 32.744 1.00 15.46 C ANISOU 1272 C PHE A 166 1737 1982 2157 376 -289 -2 C ATOM 1273 O PHE A 166 -1.548 0.936 33.733 1.00 16.59 O ANISOU 1273 O PHE A 166 2103 2020 2180 8 -6 208 O ATOM 1274 CB PHE A 166 -0.494 0.094 31.237 1.00 14.46 C ANISOU 1274 CB PHE A 166 1706 1687 2101 47 -244 -107 C ATOM 1275 CG PHE A 166 -0.337 -0.609 29.921 1.00 14.92 C ANISOU 1275 CG PHE A 166 1770 1797 2101 -431 -40 -172 C ATOM 1276 CD1 PHE A 166 -0.666 -1.947 29.784 1.00 13.89 C ANISOU 1276 CD1 PHE A 166 1468 1730 2080 -146 -249 -148 C ATOM 1277 CD2 PHE A 166 0.180 0.038 28.812 1.00 15.69 C ANISOU 1277 CD2 PHE A 166 1688 1877 2397 -106 341 -169 C ATOM 1278 CE1 PHE A 166 -0.540 -2.661 28.612 1.00 14.61 C ANISOU 1278 CE1 PHE A 166 1903 1664 1986 -232 -33 -72 C ATOM 1279 CE2 PHE A 166 0.304 -0.645 27.630 1.00 15.12 C ANISOU 1279 CE2 PHE A 166 1811 1602 2331 7 343 -70 C ATOM 1280 CZ PHE A 166 -0.005 -1.975 27.545 1.00 16.22 C ANISOU 1280 CZ PHE A 166 2084 1794 2283 -395 193 -77 C ATOM 1281 N ASP A 167 -2.197 2.877 32.816 1.00 15.92 N ANISOU 1281 N ASP A 167 1827 1820 2401 105 169 37 N ATOM 1282 CA ASP A 167 -2.385 3.596 34.055 1.00 16.45 C ANISOU 1282 CA ASP A 167 1818 1863 2571 -47 420 -39 C ATOM 1283 C ASP A 167 -1.100 3.725 34.853 1.00 15.54 C ANISOU 1283 C ASP A 167 1864 1751 2291 257 492 -430 C ATOM 1284 O ASP A 167 -1.180 3.924 36.064 1.00 18.07 O ANISOU 1284 O ASP A 167 2329 2283 2253 299 555 -324 O ATOM 1285 CB ASP A 167 -3.454 2.990 34.990 1.00 16.89 C ANISOU 1285 CB ASP A 167 2169 1663 2586 -205 502 -233 C ATOM 1286 CG ASP A 167 -4.851 3.102 34.417 1.00 25.54 C ANISOU 1286 CG ASP A 167 1794 3460 4451 70 793 1116 C ATOM 1287 OD1 ASP A 167 -5.118 3.918 33.503 1.00 25.80 O ANISOU 1287 OD1 ASP A 167 3075 2842 3885 516 -112 182 O ATOM 1288 OD2 ASP A 167 -5.668 2.315 34.933 1.00 44.92 O ANISOU 1288 OD2 ASP A 167 2523 6372 8173 -1489 495 3040 O ATOM 1289 N CYS A 168 0.051 3.702 34.208 1.00 14.47 N ANISOU 1289 N CYS A 168 1784 1912 1802 159 174 -109 N ATOM 1290 CA CYS A 168 1.341 3.839 34.882 1.00 15.20 C ANISOU 1290 CA CYS A 168 1859 1721 2195 33 52 -236 C ATOM 1291 C CYS A 168 1.658 5.302 35.116 1.00 15.78 C ANISOU 1291 C CYS A 168 2334 1639 2023 114 -70 -147 C ATOM 1292 O CYS A 168 1.703 6.045 34.117 1.00 17.08 O ANISOU 1292 O CYS A 168 2477 1854 2158 277 115 12 O ATOM 1293 CB CYS A 168 2.475 3.232 34.053 1.00 14.50 C ANISOU 1293 CB CYS A 168 1830 1598 2083 255 -8 75 C ATOM 1294 SG CYS A 168 2.260 1.453 33.769 1.00 16.76 S ANISOU 1294 SG CYS A 168 2141 1802 2423 110 -63 -403 S ATOM 1295 N PRO A 169 1.911 5.680 36.365 1.00 16.03 N ANISOU 1295 N PRO A 169 2323 1693 2075 65 -51 -172 N ATOM 1296 CA PRO A 169 2.480 7.021 36.580 1.00 17.95 C ANISOU 1296 CA PRO A 169 2763 1752 2305 -143 440 -477 C ATOM 1297 C PRO A 169 3.869 7.065 35.955 1.00 16.69 C ANISOU 1297 C PRO A 169 2453 1636 2251 25 83 -184 C ATOM 1298 O PRO A 169 4.645 6.118 36.125 1.00 16.89 O ANISOU 1298 O PRO A 169 2623 1550 2243 -32 -56 -225 O ATOM 1299 CB PRO A 169 2.571 7.166 38.078 1.00 18.50 C ANISOU 1299 CB PRO A 169 2484 2153 2391 -145 174 -640 C ATOM 1300 CG PRO A 169 1.902 6.016 38.683 1.00 20.99 C ANISOU 1300 CG PRO A 169 3672 2208 2097 -283 -155 -256 C ATOM 1301 CD PRO A 169 1.706 4.955 37.629 1.00 16.21 C ANISOU 1301 CD PRO A 169 2125 2031 2002 -83 -115 -149 C ATOM 1302 N ILE A 170 4.162 8.150 35.268 1.00 15.61 N ANISOU 1302 N ILE A 170 2155 1634 2143 118 38 -236 N ATOM 1303 CA ILE A 170 5.409 8.346 34.524 1.00 15.72 C ANISOU 1303 CA ILE A 170 2087 1732 2153 27 -16 -267 C ATOM 1304 C ILE A 170 6.332 9.342 35.205 1.00 16.18 C ANISOU 1304 C ILE A 170 2310 1698 2141 -39 132 -355 C ATOM 1305 O ILE A 170 5.880 10.424 35.551 1.00 18.51 O ANISOU 1305 O ILE A 170 2967 1683 2383 127 21 -421 O ATOM 1306 CB ILE A 170 5.135 8.823 33.081 1.00 16.52 C ANISOU 1306 CB ILE A 170 2198 1943 2136 149 73 -219 C ATOM 1307 CG1 ILE A 170 4.074 7.943 32.406 1.00 18.13 C ANISOU 1307 CG1 ILE A 170 2784 1653 2451 185 -585 25 C ATOM 1308 CG2 ILE A 170 6.408 8.913 32.264 1.00 19.80 C ANISOU 1308 CG2 ILE A 170 2817 1951 2756 213 710 -1 C ATOM 1309 CD1 ILE A 170 4.418 6.465 32.284 1.00 19.19 C ANISOU 1309 CD1 ILE A 170 2345 1665 3283 73 156 24 C ATOM 1310 N SER A 171 7.574 8.962 35.336 1.00 15.82 N ANISOU 1310 N SER A 171 2255 1597 2161 -211 -125 -169 N ATOM 1311 CA SER A 171 8.629 9.848 35.827 1.00 17.27 C ANISOU 1311 CA SER A 171 2486 2014 2060 -446 110 -505 C ATOM 1312 C SER A 171 9.817 9.741 34.849 1.00 16.16 C ANISOU 1312 C SER A 171 2166 1905 2067 -183 -135 -591 C ATOM 1313 O SER A 171 9.976 8.755 34.152 1.00 17.16 O ANISOU 1313 O SER A 171 2450 1668 2401 8 -167 -556 O ATOM 1314 CB SER A 171 9.065 9.448 37.228 1.00 16.73 C ANISOU 1314 CB SER A 171 2308 1911 2137 -282 34 -591 C ATOM 1315 OG SER A 171 7.965 9.541 38.116 1.00 17.83 O ANISOU 1315 OG SER A 171 2577 2136 2062 -40 154 -469 O ATOM 1316 N TYR A 172 10.645 10.800 34.850 1.00 16.64 N ANISOU 1316 N TYR A 172 2316 1857 2149 -276 70 -477 N ATOM 1317 CA TYR A 172 11.764 10.705 33.921 1.00 15.25 C ANISOU 1317 CA TYR A 172 1938 1827 2028 66 -261 -515 C ATOM 1318 C TYR A 172 12.940 11.506 34.464 1.00 15.25 C ANISOU 1318 C TYR A 172 2164 1547 2083 -12 -205 -421 C ATOM 1319 O TYR A 172 12.792 12.373 35.314 1.00 17.38 O ANISOU 1319 O TYR A 172 2538 1544 2521 -508 79 -653 O ATOM 1320 CB TYR A 172 11.368 11.173 32.516 1.00 16.71 C ANISOU 1320 CB TYR A 172 2323 2022 2005 -102 -216 -330 C ATOM 1321 CG TYR A 172 11.170 12.679 32.454 1.00 17.03 C ANISOU 1321 CG TYR A 172 2667 2089 1714 61 323 -265 C ATOM 1322 CD1 TYR A 172 12.145 13.523 31.922 1.00 19.69 C ANISOU 1322 CD1 TYR A 172 3199 2083 2201 -142 724 -344 C ATOM 1323 CD2 TYR A 172 10.016 13.275 32.925 1.00 18.35 C ANISOU 1323 CD2 TYR A 172 3049 2135 1789 226 588 -102 C ATOM 1324 CE1 TYR A 172 11.969 14.879 31.854 1.00 19.27 C ANISOU 1324 CE1 TYR A 172 3300 2076 1945 -109 245 -400 C ATOM 1325 CE2 TYR A 172 9.851 14.648 32.878 1.00 18.58 C ANISOU 1325 CE2 TYR A 172 3107 2128 1824 413 147 114 C ATOM 1326 CZ TYR A 172 10.816 15.463 32.348 1.00 19.50 C ANISOU 1326 CZ TYR A 172 3259 2068 2082 95 123 -162 C ATOM 1327 OH TYR A 172 10.611 16.835 32.324 1.00 22.74 O ANISOU 1327 OH TYR A 172 3857 2064 2718 223 168 5 O ATOM 1328 N PHE A 173 14.126 11.214 33.957 1.00 16.36 N ANISOU 1328 N PHE A 173 1942 1894 2379 -42 -215 -145 N ATOM 1329 CA PHE A 173 15.328 11.969 34.104 1.00 16.82 C ANISOU 1329 CA PHE A 173 2328 2010 2053 -371 -310 -449 C ATOM 1330 C PHE A 173 15.747 12.526 32.747 1.00 18.77 C ANISOU 1330 C PHE A 173 2560 2264 2307 -458 239 -539 C ATOM 1331 O PHE A 173 15.712 11.875 31.700 1.00 20.09 O ANISOU 1331 O PHE A 173 2953 2469 2209 -506 116 -485 O ATOM 1332 CB PHE A 173 16.467 11.096 34.660 1.00 18.03 C ANISOU 1332 CB PHE A 173 1838 2757 2256 -161 -96 -710 C ATOM 1333 CG PHE A 173 17.810 11.786 34.564 1.00 18.69 C ANISOU 1333 CG PHE A 173 2146 2500 2455 -384 216 -758 C ATOM 1334 CD1 PHE A 173 18.140 12.752 35.510 1.00 22.68 C ANISOU 1334 CD1 PHE A 173 2814 3538 2266 -1021 -65 -866 C ATOM 1335 CD2 PHE A 173 18.735 11.464 33.568 1.00 23.68 C ANISOU 1335 CD2 PHE A 173 2449 3612 2937 -527 644 -897 C ATOM 1336 CE1 PHE A 173 19.375 13.379 35.426 1.00 25.24 C ANISOU 1336 CE1 PHE A 173 3184 3712 2695 -1402 -58 -727 C ATOM 1337 CE2 PHE A 173 19.950 12.118 33.447 1.00 26.71 C ANISOU 1337 CE2 PHE A 173 2489 4105 3556 -615 800 -869 C ATOM 1338 CZ PHE A 173 20.253 13.085 34.390 1.00 26.52 C ANISOU 1338 CZ PHE A 173 2005 4125 3944 -393 -167 -804 C ATOM 1339 N SER A 174 16.196 13.745 32.721 1.00 19.44 N ANISOU 1339 N SER A 174 2436 2426 2524 -679 247 -430 N ATOM 1340 CA SER A 174 16.808 14.440 31.618 1.00 23.19 C ANISOU 1340 CA SER A 174 2669 2856 3286 -638 1209 -436 C ATOM 1341 C SER A 174 17.751 15.495 32.166 1.00 26.18 C ANISOU 1341 C SER A 174 2750 3387 3812 -1113 952 -115 C ATOM 1342 O SER A 174 17.585 15.916 33.322 1.00 26.12 O ANISOU 1342 O SER A 174 2967 2679 4279 -1059 1073 -632 O ATOM 1343 CB SER A 174 15.716 15.118 30.788 1.00 27.61 C ANISOU 1343 CB SER A 174 3984 2936 3572 -1782 94 822 C ATOM 1344 OG SER A 174 16.439 15.568 29.662 1.00 36.64 O ANISOU 1344 OG SER A 174 4954 5079 3890 -2052 762 904 O ATOM 1345 N ARG A 175 18.707 15.906 31.347 1.00 36.26 N ANISOU 1345 N ARG A 175 4065 4705 5008 -2158 2034 -596 N ATOM 1346 CA ARG A 175 19.645 16.936 31.808 1.00 39.00 C ANISOU 1346 CA ARG A 175 3718 5416 5683 -2403 2356 -1011 C ATOM 1347 C ARG A 175 18.926 18.162 32.348 1.00 38.04 C ANISOU 1347 C ARG A 175 4226 4787 5440 -2177 1344 -710 C ATOM 1348 O ARG A 175 19.267 18.756 33.381 1.00 34.09 O ANISOU 1348 O ARG A 175 5117 3381 4454 -1391 737 572 O ATOM 1349 CB ARG A 175 20.557 17.333 30.639 1.00 53.17 C ANISOU 1349 CB ARG A 175 6091 7315 6798 -4095 3792 -1467 C ATOM 1350 CG ARG A 175 21.418 18.559 31.042 1.00 65.18 C ANISOU 1350 CG ARG A 175 8672 7777 8314 -5640 4729 -1672 C ATOM 1351 CD ARG A 175 22.060 19.179 29.815 1.00 71.63 C ANISOU 1351 CD ARG A 175 9055 8443 9720 -5153 6825 -1890 C ATOM 1352 NE ARG A 175 23.048 18.260 29.245 1.00 81.93 N ANISOU 1352 NE ARG A 175 10083 10022 11023 -3696 6413 -2397 N ATOM 1353 CZ ARG A 175 24.225 18.007 29.814 1.00 88.25 C ANISOU 1353 CZ ARG A 175 10462 10936 12132 -3158 5931 -2419 C ATOM 1354 NH1 ARG A 175 24.541 18.607 30.959 1.00 92.10 N ANISOU 1354 NH1 ARG A 175 10283 10130 14583 -2333 4374 -3901 N ATOM 1355 NH2 ARG A 175 25.049 17.155 29.210 1.00 88.38 N ANISOU 1355 NH2 ARG A 175 10314 13206 10060 -2589 6641 -1786 N ATOM 1356 N SER A 176 17.891 18.535 31.610 1.00 34.85 N ANISOU 1356 N SER A 176 4898 4264 4081 -2463 1341 -505 N ATOM 1357 CA SER A 176 17.012 19.631 31.953 1.00 35.22 C ANISOU 1357 CA SER A 176 5518 4307 3559 -1846 860 30 C ATOM 1358 C SER A 176 15.565 19.199 31.991 1.00 33.09 C ANISOU 1358 C SER A 176 5372 3485 3715 -1501 1065 97 C ATOM 1359 O SER A 176 15.106 18.347 31.257 1.00 36.82 O ANISOU 1359 O SER A 176 4940 4558 4493 -1434 1103 -801 O ATOM 1360 CB SER A 176 17.192 20.781 30.934 1.00 46.90 C ANISOU 1360 CB SER A 176 7872 4266 5683 -2835 1701 702 C ATOM 1361 OG SER A 176 18.419 21.416 31.215 1.00 46.97 O ANISOU 1361 OG SER A 176 8024 3787 6035 -2314 216 1284 O ATOM 1362 N LYS A 177 14.740 19.771 32.858 1.00 30.95 N ANISOU 1362 N LYS A 177 5402 2784 3573 -681 553 539 N ATOM 1363 CA LYS A 177 13.317 19.464 32.800 1.00 30.16 C ANISOU 1363 CA LYS A 177 5469 2925 3067 -886 986 466 C ATOM 1364 C LYS A 177 12.675 19.916 31.496 1.00 28.68 C ANISOU 1364 C LYS A 177 4983 1958 3957 21 805 676 C ATOM 1365 O LYS A 177 12.926 20.980 30.897 1.00 36.05 O ANISOU 1365 O LYS A 177 6504 2346 4848 -260 771 1239 O ATOM 1366 CB LYS A 177 12.688 20.138 34.017 1.00 33.03 C ANISOU 1366 CB LYS A 177 6439 2065 4046 -632 1450 138 C ATOM 1367 CG LYS A 177 11.187 19.985 34.092 1.00 33.39 C ANISOU 1367 CG LYS A 177 6295 3047 3346 41 1304 -27 C ATOM 1368 CD LYS A 177 10.743 20.530 35.436 1.00 35.51 C ANISOU 1368 CD LYS A 177 7002 2868 3624 -306 1472 -423 C ATOM 1369 CE LYS A 177 9.233 20.408 35.574 1.00 36.92 C ANISOU 1369 CE LYS A 177 7098 3377 3554 -203 2000 -45 C ATOM 1370 NZ LYS A 177 8.863 20.993 36.907 1.00 33.45 N ANISOU 1370 NZ LYS A 177 6698 2874 3139 -384 1205 12 N ATOM 1371 N LYS A 178 11.784 19.040 31.008 1.00 30.56 N ANISOU 1371 N LYS A 178 5917 2255 3438 -105 499 235 N ATOM 1372 CA LYS A 178 10.967 19.353 29.839 1.00 35.53 C ANISOU 1372 CA LYS A 178 6270 3161 4069 67 37 469 C ATOM 1373 C LYS A 178 9.809 20.207 30.275 1.00 37.16 C ANISOU 1373 C LYS A 178 6458 2802 4860 239 -25 521 C ATOM 1374 O LYS A 178 9.044 19.783 31.142 1.00 34.65 O ANISOU 1374 O LYS A 178 5455 2854 4857 -50 -380 101 O ATOM 1375 CB LYS A 178 10.471 18.034 29.227 1.00 35.03 C ANISOU 1375 CB LYS A 178 6622 3353 3336 223 -103 244 C ATOM 1376 CG LYS A 178 11.641 17.093 28.986 1.00 39.78 C ANISOU 1376 CG LYS A 178 6635 3718 4760 122 699 -175 C ATOM 1377 CD LYS A 178 12.546 17.675 27.907 1.00 40.14 C ANISOU 1377 CD LYS A 178 6986 3300 4965 307 679 314 C ATOM 1378 CE LYS A 178 13.345 16.570 27.228 1.00 43.52 C ANISOU 1378 CE LYS A 178 6692 3838 6006 747 1504 782 C ATOM 1379 NZ LYS A 178 14.411 17.162 26.362 1.00 59.14 N ANISOU 1379 NZ LYS A 178 6586 6218 9665 130 2760 1083 N ATOM 1380 N PRO A 179 9.583 21.414 29.806 1.00 48.11 N ANISOU 1380 N PRO A 179 6185 4072 8021 654 -170 2405 N ATOM 1381 CA PRO A 179 8.447 22.168 30.364 1.00 49.43 C ANISOU 1381 CA PRO A 179 5834 4207 8741 1229 -605 3094 C ATOM 1382 C PRO A 179 7.101 21.670 29.841 1.00 53.12 C ANISOU 1382 C PRO A 179 6064 5953 8165 223 -11 2616 C ATOM 1383 O PRO A 179 6.081 21.787 30.518 1.00 60.04 O ANISOU 1383 O PRO A 179 6680 7658 8475 -1109 670 1438 O ATOM 1384 CB PRO A 179 8.729 23.591 29.891 1.00 59.11 C ANISOU 1384 CB PRO A 179 7896 3863 10700 666 1022 2359 C ATOM 1385 CG PRO A 179 10.137 23.570 29.387 1.00 61.03 C ANISOU 1385 CG PRO A 179 8206 4100 10882 355 1494 2231 C ATOM 1386 CD PRO A 179 10.327 22.181 28.806 1.00 53.19 C ANISOU 1386 CD PRO A 179 6991 3752 9468 651 389 2947 C ATOM 1387 N ASN A 180 7.095 21.107 28.660 1.00 50.46 N ANISOU 1387 N ASN A 180 5511 6345 7315 908 -210 3498 N ATOM 1388 CA ASN A 180 6.032 20.544 27.880 1.00 66.81 C ANISOU 1388 CA ASN A 180 8501 8189 8695 -827 -1266 2552 C ATOM 1389 C ASN A 180 5.183 19.441 28.490 1.00 62.27 C ANISOU 1389 C ASN A 180 8408 7182 8068 -845 -1937 1859 C ATOM 1390 O ASN A 180 4.034 19.265 28.064 1.00 73.47 O ANISOU 1390 O ASN A 180 10886 7361 9667 -2986 -4841 2404 O ATOM 1391 CB ASN A 180 6.746 19.908 26.651 1.00 71.78 C ANISOU 1391 CB ASN A 180 10201 8440 8630 -1020 -951 2237 C ATOM 1392 CG ASN A 180 8.086 19.353 27.125 1.00 71.21 C ANISOU 1392 CG ASN A 180 10690 7838 8528 149 120 2825 C ATOM 1393 OD1 ASN A 180 8.139 18.262 27.697 1.00 84.94 O ANISOU 1393 OD1 ASN A 180 12900 10116 9259 -922 -825 5258 O ATOM 1394 ND2 ASN A 180 9.136 20.129 26.883 1.00 58.49 N ANISOU 1394 ND2 ASN A 180 8788 5853 7583 2741 3075 1079 N ATOM 1395 N THR A 181 5.704 18.684 29.439 1.00 58.28 N ANISOU 1395 N THR A 181 9402 5065 7678 -997 -2760 505 N ATOM 1396 CA THR A 181 5.127 17.410 29.891 1.00 46.86 C ANISOU 1396 CA THR A 181 8221 3748 5836 -179 -1730 -1417 C ATOM 1397 C THR A 181 4.416 17.471 31.233 1.00 42.30 C ANISOU 1397 C THR A 181 7096 3228 5749 1288 -2178 -1422 C ATOM 1398 O THR A 181 4.660 18.409 31.993 1.00 55.31 O ANISOU 1398 O THR A 181 9538 4666 6812 1168 -2469 -2772 O ATOM 1399 CB THR A 181 6.288 16.384 29.871 1.00 47.35 C ANISOU 1399 CB THR A 181 7660 4401 5929 -224 -727 -2228 C ATOM 1400 OG1 THR A 181 5.846 15.086 30.229 1.00 49.66 O ANISOU 1400 OG1 THR A 181 5890 4773 8204 624 -1568 -301 O ATOM 1401 CG2 THR A 181 7.332 16.699 30.922 1.00 60.56 C ANISOU 1401 CG2 THR A 181 11495 1895 9621 1697 -4943 -2288 C ATOM 1402 N ASN A 182 3.529 16.548 31.584 1.00 43.14 N ANISOU 1402 N ASN A 182 6144 4232 6017 1662 -2222 -291 N ATOM 1403 CA ASN A 182 2.834 16.369 32.860 1.00 46.29 C ANISOU 1403 CA ASN A 182 5664 5261 6664 3076 -1545 -213 C ATOM 1404 C ASN A 182 3.460 15.226 33.659 1.00 41.93 C ANISOU 1404 C ASN A 182 5912 3747 6274 2497 -310 -303 C ATOM 1405 O ASN A 182 3.031 14.820 34.739 1.00 48.18 O ANISOU 1405 O ASN A 182 4664 7110 6532 2091 -728 690 O ATOM 1406 CB ASN A 182 1.338 16.264 32.580 1.00 55.26 C ANISOU 1406 CB ASN A 182 5909 6866 8219 1855 -1919 5 C ATOM 1407 CG ASN A 182 0.420 15.100 32.546 1.00 61.75 C ANISOU 1407 CG ASN A 182 7443 7050 8970 1075 -2848 1203 C ATOM 1408 OD1 ASN A 182 -0.577 15.017 31.779 1.00 59.74 O ANISOU 1408 OD1 ASN A 182 6441 6522 9735 1383 -2493 908 O ATOM 1409 ND2 ASN A 182 0.681 14.133 33.420 1.00 66.73 N ANISOU 1409 ND2 ASN A 182 8479 5461 11415 3373 -3256 654 N ATOM 1410 N TYR A 183 4.555 14.636 33.197 1.00 31.67 N ANISOU 1410 N TYR A 183 4404 2614 5016 1274 -1791 -1359 N ATOM 1411 CA TYR A 183 5.289 13.600 33.938 1.00 24.22 C ANISOU 1411 CA TYR A 183 3217 2178 3809 297 -664 -819 C ATOM 1412 C TYR A 183 6.176 14.174 35.042 1.00 23.68 C ANISOU 1412 C TYR A 183 2780 2256 3961 145 -594 -766 C ATOM 1413 O TYR A 183 6.498 15.351 35.042 1.00 28.55 O ANISOU 1413 O TYR A 183 3987 1954 4908 450 -1202 -1069 O ATOM 1414 CB TYR A 183 6.170 12.850 32.951 1.00 20.66 C ANISOU 1414 CB TYR A 183 2744 1684 3422 9 -460 -119 C ATOM 1415 CG TYR A 183 5.499 12.346 31.702 1.00 17.85 C ANISOU 1415 CG TYR A 183 2078 1528 3177 321 -163 9 C ATOM 1416 CD1 TYR A 183 6.145 12.324 30.473 1.00 23.17 C ANISOU 1416 CD1 TYR A 183 2802 2353 3650 -395 538 -775 C ATOM 1417 CD2 TYR A 183 4.199 11.868 31.741 1.00 18.67 C ANISOU 1417 CD2 TYR A 183 2041 1990 3064 275 -161 -9 C ATOM 1418 CE1 TYR A 183 5.518 11.860 29.337 1.00 21.98 C ANISOU 1418 CE1 TYR A 183 3060 2280 3014 -448 256 411 C ATOM 1419 CE2 TYR A 183 3.570 11.399 30.598 1.00 20.29 C ANISOU 1419 CE2 TYR A 183 2417 2305 2989 -212 -12 -99 C ATOM 1420 CZ TYR A 183 4.240 11.392 29.386 1.00 19.36 C ANISOU 1420 CZ TYR A 183 2492 1945 2918 334 -63 329 C ATOM 1421 OH TYR A 183 3.620 10.921 28.247 1.00 23.58 O ANISOU 1421 OH TYR A 183 3106 2856 2997 -49 3 -77 O ATOM 1422 N THR A 184 6.632 13.340 35.984 1.00 21.05 N ANISOU 1422 N THR A 184 2513 2389 3096 -36 128 -817 N ATOM 1423 CA THR A 184 7.393 13.772 37.166 1.00 19.86 C ANISOU 1423 CA THR A 184 2515 1890 3140 -400 126 -512 C ATOM 1424 C THR A 184 8.892 13.785 36.895 1.00 20.04 C ANISOU 1424 C THR A 184 2596 2158 2861 -481 322 -821 C ATOM 1425 O THR A 184 9.483 12.732 36.614 1.00 19.19 O ANISOU 1425 O THR A 184 2634 2123 2534 -330 165 -554 O ATOM 1426 CB THR A 184 7.097 12.866 38.392 1.00 19.86 C ANISOU 1426 CB THR A 184 2331 1962 3252 -272 221 -406 C ATOM 1427 OG1 THR A 184 5.704 12.946 38.700 1.00 24.17 O ANISOU 1427 OG1 THR A 184 2460 2587 4135 -406 647 -608 O ATOM 1428 CG2 THR A 184 7.855 13.324 39.619 1.00 22.53 C ANISOU 1428 CG2 THR A 184 2879 2628 3052 79 178 -677 C ATOM 1429 N TYR A 185 9.509 14.938 36.945 1.00 19.23 N ANISOU 1429 N TYR A 185 2538 2022 2746 -420 225 -357 N ATOM 1430 CA TYR A 185 10.907 15.123 36.659 1.00 17.93 C ANISOU 1430 CA TYR A 185 2605 1856 2351 -231 293 148 C ATOM 1431 C TYR A 185 11.780 14.840 37.884 1.00 17.50 C ANISOU 1431 C TYR A 185 2548 1980 2122 -331 353 -91 C ATOM 1432 O TYR A 185 11.509 15.331 38.970 1.00 20.14 O ANISOU 1432 O TYR A 185 3081 2262 2308 -124 495 -345 O ATOM 1433 CB TYR A 185 11.161 16.586 36.221 1.00 19.11 C ANISOU 1433 CB TYR A 185 3006 1712 2543 -268 358 -16 C ATOM 1434 CG TYR A 185 12.630 16.852 35.970 1.00 17.66 C ANISOU 1434 CG TYR A 185 2947 1657 2107 -345 261 -90 C ATOM 1435 CD1 TYR A 185 13.277 16.357 34.831 1.00 18.40 C ANISOU 1435 CD1 TYR A 185 2960 2071 1959 -69 107 -20 C ATOM 1436 CD2 TYR A 185 13.416 17.577 36.840 1.00 19.92 C ANISOU 1436 CD2 TYR A 185 3491 2027 2050 -799 419 -117 C ATOM 1437 CE1 TYR A 185 14.613 16.599 34.617 1.00 20.22 C ANISOU 1437 CE1 TYR A 185 3049 2428 2205 -228 337 -114 C ATOM 1438 CE2 TYR A 185 14.767 17.839 36.674 1.00 23.19 C ANISOU 1438 CE2 TYR A 185 3680 2106 3025 -1352 515 -673 C ATOM 1439 CZ TYR A 185 15.363 17.329 35.522 1.00 20.93 C ANISOU 1439 CZ TYR A 185 3288 1716 2949 -702 499 -109 C ATOM 1440 OH TYR A 185 16.690 17.571 35.328 1.00 25.09 O ANISOU 1440 OH TYR A 185 3582 2508 3443 -1350 681 77 O ATOM 1441 N TYR A 186 12.836 14.058 37.673 1.00 17.42 N ANISOU 1441 N TYR A 186 2699 1974 1945 -239 -192 -688 N ATOM 1442 CA TYR A 186 13.873 13.831 38.640 1.00 16.54 C ANISOU 1442 CA TYR A 186 2567 1861 1857 -523 -196 -752 C ATOM 1443 C TYR A 186 15.222 14.341 38.129 1.00 17.76 C ANISOU 1443 C TYR A 186 2655 1701 2392 -405 45 -485 C ATOM 1444 O TYR A 186 15.537 14.084 36.957 1.00 19.67 O ANISOU 1444 O TYR A 186 2666 2506 2301 -378 7 -377 O ATOM 1445 CB TYR A 186 13.949 12.317 38.914 1.00 17.53 C ANISOU 1445 CB TYR A 186 2515 1989 2157 -453 -18 -371 C ATOM 1446 CG TYR A 186 12.859 11.822 39.830 1.00 16.43 C ANISOU 1446 CG TYR A 186 2225 2036 1980 -29 -77 -287 C ATOM 1447 CD1 TYR A 186 13.030 11.715 41.190 1.00 18.86 C ANISOU 1447 CD1 TYR A 186 2605 2613 1948 -366 -124 -463 C ATOM 1448 CD2 TYR A 186 11.626 11.418 39.325 1.00 17.42 C ANISOU 1448 CD2 TYR A 186 2082 2491 2045 8 -114 -136 C ATOM 1449 CE1 TYR A 186 12.016 11.232 42.030 1.00 20.49 C ANISOU 1449 CE1 TYR A 186 3189 2741 1856 -901 -83 -466 C ATOM 1450 CE2 TYR A 186 10.601 10.959 40.130 1.00 17.77 C ANISOU 1450 CE2 TYR A 186 2427 2245 2081 -270 -88 -147 C ATOM 1451 CZ TYR A 186 10.798 10.875 41.489 1.00 17.96 C ANISOU 1451 CZ TYR A 186 2781 1943 2101 -391 -82 -23 C ATOM 1452 OH TYR A 186 9.782 10.418 42.305 1.00 19.94 O ANISOU 1452 OH TYR A 186 3110 2160 2305 -417 443 -443 O ATOM 1453 N GLY A 187 16.002 14.986 38.982 1.00 17.67 N ANISOU 1453 N GLY A 187 2424 1841 2450 -522 181 -439 N ATOM 1454 CA GLY A 187 17.280 15.534 38.596 1.00 20.45 C ANISOU 1454 CA GLY A 187 2383 2494 2892 -616 194 -168 C ATOM 1455 C GLY A 187 18.460 14.589 38.749 1.00 21.10 C ANISOU 1455 C GLY A 187 2470 2479 3068 -464 251 -1115 C ATOM 1456 O GLY A 187 19.617 14.884 38.475 1.00 24.85 O ANISOU 1456 O GLY A 187 2344 3649 3451 -449 -126 -347 O ATOM 1457 N SER A 188 18.209 13.375 39.197 1.00 24.05 N ANISOU 1457 N SER A 188 2504 2040 4593 -506 -691 -1244 N ATOM 1458 CA SER A 188 19.144 12.320 39.479 1.00 25.07 C ANISOU 1458 CA SER A 188 2752 2470 4303 -130 -914 -1586 C ATOM 1459 C SER A 188 18.614 10.993 39.005 1.00 21.76 C ANISOU 1459 C SER A 188 2509 2259 3500 103 -1172 -1178 C ATOM 1460 O SER A 188 17.432 10.722 39.231 1.00 30.07 O ANISOU 1460 O SER A 188 2391 2509 6525 37 -978 -2181 O ATOM 1461 CB SER A 188 19.214 12.260 41.004 1.00 24.82 C ANISOU 1461 CB SER A 188 2311 2853 4266 514 -1030 -2259 C ATOM 1462 OG SER A 188 19.758 11.189 41.631 1.00 29.73 O ANISOU 1462 OG SER A 188 3509 3592 4196 457 -820 -1448 O ATOM 1463 N VAL A 189 19.460 10.228 38.373 1.00 23.55 N ANISOU 1463 N VAL A 189 2883 1934 4131 205 -678 -890 N ATOM 1464 CA VAL A 189 19.112 8.885 37.945 1.00 19.20 C ANISOU 1464 CA VAL A 189 2272 1862 3161 109 -466 -489 C ATOM 1465 C VAL A 189 18.901 8.001 39.169 1.00 19.66 C ANISOU 1465 C VAL A 189 2340 2478 2652 16 -364 -647 C ATOM 1466 O VAL A 189 17.964 7.173 39.179 1.00 19.09 O ANISOU 1466 O VAL A 189 2338 2817 2097 -169 -282 -550 O ATOM 1467 CB VAL A 189 20.131 8.270 36.978 1.00 21.75 C ANISOU 1467 CB VAL A 189 3313 2178 2774 -30 24 -509 C ATOM 1468 CG1 VAL A 189 19.670 6.878 36.543 1.00 22.82 C ANISOU 1468 CG1 VAL A 189 3166 2610 2893 -116 -159 -1020 C ATOM 1469 CG2 VAL A 189 20.268 9.161 35.767 1.00 26.65 C ANISOU 1469 CG2 VAL A 189 2905 3685 3536 -194 -218 602 C ATOM 1470 N VAL A 190 19.707 8.178 40.218 1.00 21.47 N ANISOU 1470 N VAL A 190 2186 3334 2638 -204 -260 -818 N ATOM 1471 CA VAL A 190 19.498 7.342 41.405 1.00 21.93 C ANISOU 1471 CA VAL A 190 2531 3653 2147 -240 -130 -1088 C ATOM 1472 C VAL A 190 18.142 7.568 42.056 1.00 23.13 C ANISOU 1472 C VAL A 190 2520 3634 2636 -171 18 -1077 C ATOM 1473 O VAL A 190 17.424 6.664 42.460 1.00 21.91 O ANISOU 1473 O VAL A 190 2748 3804 1773 -189 -30 -902 O ATOM 1474 CB VAL A 190 20.631 7.636 42.435 1.00 23.22 C ANISOU 1474 CB VAL A 190 2653 3458 2712 -321 -478 -819 C ATOM 1475 CG1 VAL A 190 20.238 7.190 43.823 1.00 30.34 C ANISOU 1475 CG1 VAL A 190 3020 6125 2382 -1224 -612 -971 C ATOM 1476 CG2 VAL A 190 21.911 6.980 41.922 1.00 23.12 C ANISOU 1476 CG2 VAL A 190 2976 3388 2421 208 -724 -725 C ATOM 1477 N GLU A 191 17.712 8.816 42.192 1.00 23.57 N ANISOU 1477 N GLU A 191 2351 3662 2944 -206 -435 -1373 N ATOM 1478 CA GLU A 191 16.440 9.175 42.801 1.00 23.41 C ANISOU 1478 CA GLU A 191 2493 3773 2630 136 -475 -1002 C ATOM 1479 C GLU A 191 15.284 8.665 41.934 1.00 20.12 C ANISOU 1479 C GLU A 191 2238 3001 2407 319 -275 -933 C ATOM 1480 O GLU A 191 14.305 8.125 42.457 1.00 22.81 O ANISOU 1480 O GLU A 191 2736 3409 2521 -104 87 -1163 O ATOM 1481 CB GLU A 191 16.353 10.681 43.001 1.00 29.39 C ANISOU 1481 CB GLU A 191 3086 4018 4065 -81 -322 -2115 C ATOM 1482 CG GLU A 191 15.291 11.222 43.924 1.00 35.22 C ANISOU 1482 CG GLU A 191 4334 4116 4932 -485 887 -2301 C ATOM 1483 CD GLU A 191 15.161 12.740 43.815 1.00 41.77 C ANISOU 1483 CD GLU A 191 6722 3806 5341 -713 1360 -3566 C ATOM 1484 OE1 GLU A 191 15.904 13.618 43.295 1.00 52.45 O ANISOU 1484 OE1 GLU A 191 3652 3171 13107 -638 799 -3135 O ATOM 1485 OE2 GLU A 191 14.105 13.185 44.227 1.00 30.70 O ANISOU 1485 OE2 GLU A 191 5868 3424 2371 -319 -45 -1390 O ATOM 1486 N LEU A 192 15.446 8.817 40.615 1.00 21.61 N ANISOU 1486 N LEU A 192 2742 3100 2371 -399 -105 -1312 N ATOM 1487 CA LEU A 192 14.482 8.211 39.691 1.00 18.88 C ANISOU 1487 CA LEU A 192 2562 2215 2397 84 -125 -1244 C ATOM 1488 C LEU A 192 14.332 6.716 39.948 1.00 18.28 C ANISOU 1488 C LEU A 192 2273 2315 2356 108 28 -826 C ATOM 1489 O LEU A 192 13.230 6.184 40.067 1.00 18.87 O ANISOU 1489 O LEU A 192 2170 2470 2529 172 -164 -626 O ATOM 1490 CB LEU A 192 14.892 8.431 38.226 1.00 18.34 C ANISOU 1490 CB LEU A 192 2264 2377 2329 306 -611 -563 C ATOM 1491 CG LEU A 192 13.920 7.857 37.169 1.00 19.02 C ANISOU 1491 CG LEU A 192 2500 2233 2492 397 -787 -674 C ATOM 1492 CD1 LEU A 192 12.543 8.512 37.278 1.00 19.14 C ANISOU 1492 CD1 LEU A 192 2471 1733 3069 295 -1092 -737 C ATOM 1493 CD2 LEU A 192 14.514 8.025 35.782 1.00 20.55 C ANISOU 1493 CD2 LEU A 192 2893 2439 2476 -385 -768 -805 C ATOM 1494 N ALA A 193 15.456 6.011 39.968 1.00 18.38 N ANISOU 1494 N ALA A 193 2094 2405 2484 -107 -487 -348 N ATOM 1495 CA ALA A 193 15.478 4.580 40.171 1.00 18.33 C ANISOU 1495 CA ALA A 193 2351 2464 2149 222 -201 -309 C ATOM 1496 C ALA A 193 14.811 4.215 41.491 1.00 18.57 C ANISOU 1496 C ALA A 193 2700 2242 2113 -28 -75 -645 C ATOM 1497 O ALA A 193 14.057 3.249 41.545 1.00 19.23 O ANISOU 1497 O ALA A 193 2754 2173 2382 -10 -217 -356 O ATOM 1498 CB ALA A 193 16.913 4.043 40.114 1.00 20.19 C ANISOU 1498 CB ALA A 193 2389 2970 2312 411 -322 -715 C ATOM 1499 N SER A 194 15.057 4.979 42.534 1.00 20.13 N ANISOU 1499 N SER A 194 2697 2754 2197 157 -359 -884 N ATOM 1500 CA SER A 194 14.488 4.756 43.866 1.00 21.97 C ANISOU 1500 CA SER A 194 2762 3364 2222 311 -226 -890 C ATOM 1501 C SER A 194 12.971 4.835 43.898 1.00 22.11 C ANISOU 1501 C SER A 194 2704 3479 2217 -185 -441 -470 C ATOM 1502 O SER A 194 12.340 4.295 44.817 1.00 24.89 O ANISOU 1502 O SER A 194 2798 4166 2492 366 -253 124 O ATOM 1503 CB SER A 194 15.054 5.806 44.842 1.00 24.95 C ANISOU 1503 CB SER A 194 2888 4646 1947 -93 -827 -917 C ATOM 1504 OG SER A 194 16.431 5.597 45.061 1.00 31.22 O ANISOU 1504 OG SER A 194 3263 5497 3102 745 -1307 -1255 O ATOM 1505 N ASN A 195 12.452 5.539 42.902 1.00 19.51 N ANISOU 1505 N ASN A 195 2633 2816 1965 -92 -259 -746 N ATOM 1506 CA ASN A 195 11.029 5.798 42.773 1.00 19.08 C ANISOU 1506 CA ASN A 195 2579 2417 2254 -134 -162 -753 C ATOM 1507 C ASN A 195 10.379 5.159 41.531 1.00 17.32 C ANISOU 1507 C ASN A 195 2343 2189 2048 306 -204 -555 C ATOM 1508 O ASN A 195 9.313 5.591 41.099 1.00 19.38 O ANISOU 1508 O ASN A 195 2416 2391 2557 455 -343 -398 O ATOM 1509 CB ASN A 195 10.776 7.309 42.744 1.00 19.94 C ANISOU 1509 CB ASN A 195 2971 2463 2140 -56 406 -865 C ATOM 1510 CG ASN A 195 11.026 7.923 44.104 1.00 18.11 C ANISOU 1510 CG ASN A 195 2458 2432 1993 33 275 -679 C ATOM 1511 OD1 ASN A 195 10.119 7.907 44.949 1.00 22.39 O ANISOU 1511 OD1 ASN A 195 3307 3034 2168 -414 801 -742 O ATOM 1512 ND2 ASN A 195 12.208 8.437 44.314 1.00 21.58 N ANISOU 1512 ND2 ASN A 195 2684 2484 3032 -185 181 -945 N ATOM 1513 N SER A 196 11.036 4.126 41.014 1.00 16.63 N ANISOU 1513 N SER A 196 2273 2000 2047 232 -197 -489 N ATOM 1514 CA SER A 196 10.551 3.363 39.896 1.00 16.55 C ANISOU 1514 CA SER A 196 2304 1930 2053 -11 -61 -445 C ATOM 1515 C SER A 196 10.427 1.868 40.219 1.00 16.34 C ANISOU 1515 C SER A 196 2371 1977 1859 -5 -401 -217 C ATOM 1516 O SER A 196 11.311 1.298 40.867 1.00 18.75 O ANISOU 1516 O SER A 196 2325 2652 2148 266 -420 -109 O ATOM 1517 CB SER A 196 11.544 3.497 38.751 1.00 16.58 C ANISOU 1517 CB SER A 196 2268 2147 1885 -224 -243 -355 C ATOM 1518 OG SER A 196 11.634 4.828 38.297 1.00 18.87 O ANISOU 1518 OG SER A 196 2792 2204 2175 -430 -146 -275 O ATOM 1519 N ASP A 197 9.314 1.294 39.733 1.00 15.27 N ANISOU 1519 N ASP A 197 2073 1727 2001 249 -209 -194 N ATOM 1520 CA ASP A 197 9.161 -0.159 39.666 1.00 16.08 C ANISOU 1520 CA ASP A 197 2576 1833 1700 -94 -94 -227 C ATOM 1521 C ASP A 197 9.829 -0.723 38.417 1.00 15.18 C ANISOU 1521 C ASP A 197 2435 1696 1638 241 -316 -142 C ATOM 1522 O ASP A 197 10.331 -1.847 38.453 1.00 17.64 O ANISOU 1522 O ASP A 197 2618 1674 2412 353 -109 75 O ATOM 1523 CB ASP A 197 7.687 -0.565 39.706 1.00 16.77 C ANISOU 1523 CB ASP A 197 2536 2211 1625 -154 -213 -56 C ATOM 1524 CG ASP A 197 7.011 -0.045 40.957 1.00 18.21 C ANISOU 1524 CG ASP A 197 2800 2325 1794 -88 123 41 C ATOM 1525 OD1 ASP A 197 7.474 -0.393 42.070 1.00 21.27 O ANISOU 1525 OD1 ASP A 197 3415 2953 1712 393 97 -162 O ATOM 1526 OD2 ASP A 197 6.025 0.712 40.857 1.00 19.08 O ANISOU 1526 OD2 ASP A 197 2892 2238 2121 -63 38 -139 O ATOM 1527 N ILE A 198 9.838 0.049 37.347 1.00 14.53 N ANISOU 1527 N ILE A 198 2179 1609 1732 108 -130 -154 N ATOM 1528 CA ILE A 198 10.364 -0.276 36.037 1.00 15.23 C ANISOU 1528 CA ILE A 198 2104 2036 1646 -270 -148 -316 C ATOM 1529 C ILE A 198 11.190 0.921 35.594 1.00 14.14 C ANISOU 1529 C ILE A 198 2024 1723 1626 57 14 -499 C ATOM 1530 O ILE A 198 10.657 2.020 35.655 1.00 16.18 O ANISOU 1530 O ILE A 198 2285 1825 2038 311 -128 -434 O ATOM 1531 CB ILE A 198 9.230 -0.555 35.043 1.00 14.73 C ANISOU 1531 CB ILE A 198 1933 1891 1771 -5 -97 -274 C ATOM 1532 CG1 ILE A 198 8.350 -1.736 35.455 1.00 16.64 C ANISOU 1532 CG1 ILE A 198 2009 1969 2344 -197 -136 -309 C ATOM 1533 CG2 ILE A 198 9.799 -0.795 33.641 1.00 18.49 C ANISOU 1533 CG2 ILE A 198 2349 3084 1591 -168 -195 -410 C ATOM 1534 CD1 ILE A 198 6.981 -1.718 34.850 1.00 17.41 C ANISOU 1534 CD1 ILE A 198 2021 2002 2593 -145 -177 -170 C ATOM 1535 N LEU A 199 12.433 0.683 35.192 1.00 16.37 N ANISOU 1535 N LEU A 199 1888 2213 2121 159 47 16 N ATOM 1536 CA LEU A 199 13.315 1.776 34.749 1.00 15.88 C ANISOU 1536 CA LEU A 199 1964 2147 1924 130 -46 104 C ATOM 1537 C LEU A 199 13.737 1.474 33.303 1.00 16.21 C ANISOU 1537 C LEU A 199 1852 2336 1970 269 -9 25 C ATOM 1538 O LEU A 199 14.323 0.412 33.060 1.00 15.73 O ANISOU 1538 O LEU A 199 2040 2068 1867 92 -319 -58 O ATOM 1539 CB LEU A 199 14.524 1.880 35.653 1.00 15.77 C ANISOU 1539 CB LEU A 199 2102 1810 2080 238 -174 -59 C ATOM 1540 CG LEU A 199 15.489 3.050 35.445 1.00 16.26 C ANISOU 1540 CG LEU A 199 2095 2090 1993 80 -123 -132 C ATOM 1541 CD1 LEU A 199 14.831 4.366 35.777 1.00 18.58 C ANISOU 1541 CD1 LEU A 199 2299 1981 2779 -144 -440 -650 C ATOM 1542 CD2 LEU A 199 16.742 2.850 36.290 1.00 18.64 C ANISOU 1542 CD2 LEU A 199 2512 2332 2237 47 -586 -504 C ATOM 1543 N VAL A 200 13.446 2.389 32.410 1.00 15.32 N ANISOU 1543 N VAL A 200 2273 1887 1659 144 -301 -380 N ATOM 1544 CA VAL A 200 13.686 2.223 31.006 1.00 13.62 C ANISOU 1544 CA VAL A 200 1721 1719 1735 122 -168 -443 C ATOM 1545 C VAL A 200 14.803 3.119 30.496 1.00 14.66 C ANISOU 1545 C VAL A 200 1852 1664 2054 201 -286 -85 C ATOM 1546 O VAL A 200 14.692 4.332 30.624 1.00 16.21 O ANISOU 1546 O VAL A 200 2080 1746 2333 44 -126 -88 O ATOM 1547 CB VAL A 200 12.433 2.511 30.152 1.00 14.22 C ANISOU 1547 CB VAL A 200 1862 1884 1658 180 -120 -19 C ATOM 1548 CG1 VAL A 200 12.764 2.169 28.712 1.00 17.25 C ANISOU 1548 CG1 VAL A 200 2080 2842 1633 -142 -151 6 C ATOM 1549 CG2 VAL A 200 11.234 1.703 30.659 1.00 15.01 C ANISOU 1549 CG2 VAL A 200 1665 2245 1795 147 -190 -109 C ATOM 1550 N VAL A 201 15.816 2.555 29.878 1.00 15.67 N ANISOU 1550 N VAL A 201 1574 2157 2221 126 -281 -215 N ATOM 1551 CA VAL A 201 16.894 3.345 29.317 1.00 15.35 C ANISOU 1551 CA VAL A 201 1547 1980 2306 52 -454 -184 C ATOM 1552 C VAL A 201 16.481 3.711 27.914 1.00 16.91 C ANISOU 1552 C VAL A 201 1937 2223 2267 -396 -640 -161 C ATOM 1553 O VAL A 201 16.321 2.783 27.112 1.00 19.74 O ANISOU 1553 O VAL A 201 2215 2801 2484 -517 -287 -616 O ATOM 1554 CB VAL A 201 18.207 2.543 29.246 1.00 16.26 C ANISOU 1554 CB VAL A 201 1629 2040 2508 100 -216 -342 C ATOM 1555 CG1 VAL A 201 19.316 3.364 28.588 1.00 21.23 C ANISOU 1555 CG1 VAL A 201 1844 2961 3262 -46 254 -173 C ATOM 1556 CG2 VAL A 201 18.659 2.060 30.609 1.00 20.51 C ANISOU 1556 CG2 VAL A 201 1927 2721 3147 156 -773 256 C ATOM 1557 N ALA A 202 16.324 4.993 27.586 1.00 18.78 N ANISOU 1557 N ALA A 202 2740 2481 1916 -98 -52 189 N ATOM 1558 CA ALA A 202 15.860 5.430 26.292 1.00 21.34 C ANISOU 1558 CA ALA A 202 2776 3444 1887 302 21 353 C ATOM 1559 C ALA A 202 16.597 6.678 25.836 1.00 24.41 C ANISOU 1559 C ALA A 202 3181 3528 2565 468 -123 1152 C ATOM 1560 O ALA A 202 16.017 7.662 25.321 1.00 35.11 O ANISOU 1560 O ALA A 202 5015 3847 4480 836 -1355 1493 O ATOM 1561 CB ALA A 202 14.414 5.832 26.434 1.00 24.30 C ANISOU 1561 CB ALA A 202 2773 3896 2565 408 -296 -121 C ATOM 1562 N CYS A 203 17.890 6.775 26.025 1.00 22.95 N ANISOU 1562 N CYS A 203 3252 2891 2578 116 14 230 N ATOM 1563 CA CYS A 203 18.623 7.960 25.600 1.00 24.91 C ANISOU 1563 CA CYS A 203 3770 2723 2972 250 299 423 C ATOM 1564 C CYS A 203 19.746 7.561 24.653 1.00 23.18 C ANISOU 1564 C CYS A 203 3607 2305 2896 59 192 380 C ATOM 1565 O CYS A 203 20.125 6.400 24.612 1.00 22.75 O ANISOU 1565 O CYS A 203 3668 2334 2644 51 140 379 O ATOM 1566 CB CYS A 203 19.191 8.671 26.835 1.00 29.43 C ANISOU 1566 CB CYS A 203 5461 2181 3540 -188 541 -203 C ATOM 1567 SG CYS A 203 20.206 7.607 27.890 1.00 25.13 S ANISOU 1567 SG CYS A 203 3112 3853 2584 -714 405 -540 S ATOM 1568 N PRO A 204 20.281 8.508 23.889 1.00 23.87 N ANISOU 1568 N PRO A 204 4087 2295 2689 48 301 300 N ATOM 1569 CA PRO A 204 21.447 8.187 23.075 1.00 24.41 C ANISOU 1569 CA PRO A 204 4240 2611 2424 230 351 435 C ATOM 1570 C PRO A 204 22.642 7.806 23.949 1.00 22.51 C ANISOU 1570 C PRO A 204 4207 2365 1980 197 385 -45 C ATOM 1571 O PRO A 204 22.719 8.118 25.129 1.00 25.80 O ANISOU 1571 O PRO A 204 4160 3484 2157 -606 538 -496 O ATOM 1572 CB PRO A 204 21.709 9.503 22.348 1.00 27.32 C ANISOU 1572 CB PRO A 204 4726 2970 2683 412 688 758 C ATOM 1573 CG PRO A 204 20.494 10.326 22.468 1.00 30.02 C ANISOU 1573 CG PRO A 204 5678 2551 3178 819 1490 615 C ATOM 1574 CD PRO A 204 19.813 9.901 23.744 1.00 29.51 C ANISOU 1574 CD PRO A 204 5399 2523 3292 529 1327 778 C ATOM 1575 N LEU A 205 23.609 7.107 23.375 1.00 23.59 N ANISOU 1575 N LEU A 205 3885 2572 2505 -7 329 -383 N ATOM 1576 CA LEU A 205 24.863 6.759 23.983 1.00 22.08 C ANISOU 1576 CA LEU A 205 3523 2080 2786 -633 329 -483 C ATOM 1577 C LEU A 205 25.896 7.850 23.663 1.00 26.09 C ANISOU 1577 C LEU A 205 5100 2824 1989 -1733 -28 -209 C ATOM 1578 O LEU A 205 26.240 8.147 22.510 1.00 24.89 O ANISOU 1578 O LEU A 205 4656 2718 2084 -850 209 -70 O ATOM 1579 CB LEU A 205 25.392 5.417 23.452 1.00 20.74 C ANISOU 1579 CB LEU A 205 3244 2340 2295 -418 589 -278 C ATOM 1580 CG LEU A 205 26.676 4.965 24.143 1.00 22.40 C ANISOU 1580 CG LEU A 205 2855 3277 2379 -412 761 -332 C ATOM 1581 CD1 LEU A 205 26.439 4.708 25.633 1.00 24.65 C ANISOU 1581 CD1 LEU A 205 3576 3353 2439 -28 710 120 C ATOM 1582 CD2 LEU A 205 27.257 3.744 23.439 1.00 20.77 C ANISOU 1582 CD2 LEU A 205 2580 2864 2449 -536 225 -283 C ATOM 1583 N THR A 206 26.399 8.450 24.726 1.00 25.15 N ANISOU 1583 N THR A 206 4575 2653 2328 -1136 -255 -477 N ATOM 1584 CA THR A 206 27.461 9.436 24.689 1.00 26.00 C ANISOU 1584 CA THR A 206 4356 2946 2577 -1220 201 -823 C ATOM 1585 C THR A 206 28.447 9.095 25.803 1.00 30.81 C ANISOU 1585 C THR A 206 4628 3654 3425 -1799 -378 -99 C ATOM 1586 O THR A 206 28.135 8.224 26.627 1.00 27.48 O ANISOU 1586 O THR A 206 4018 3798 2625 -1233 316 -497 O ATOM 1587 CB THR A 206 26.931 10.866 24.889 1.00 26.67 C ANISOU 1587 CB THR A 206 4172 2864 3097 -1412 845 -862 C ATOM 1588 OG1 THR A 206 26.339 10.983 26.179 1.00 31.78 O ANISOU 1588 OG1 THR A 206 5482 3740 2852 -1216 761 -1258 O ATOM 1589 CG2 THR A 206 25.808 11.219 23.930 1.00 30.66 C ANISOU 1589 CG2 THR A 206 5616 2712 3320 -958 263 -202 C ATOM 1590 N PRO A 207 29.598 9.722 25.883 1.00 30.62 N ANISOU 1590 N PRO A 207 3950 4147 3537 -1354 219 -93 N ATOM 1591 CA PRO A 207 30.467 9.523 27.054 1.00 33.85 C ANISOU 1591 CA PRO A 207 4529 4627 3704 -2081 -280 -206 C ATOM 1592 C PRO A 207 29.716 9.738 28.350 1.00 32.05 C ANISOU 1592 C PRO A 207 4585 3986 3608 -1953 -378 -187 C ATOM 1593 O PRO A 207 29.842 9.037 29.330 1.00 32.38 O ANISOU 1593 O PRO A 207 4177 4156 3971 -903 242 41 O ATOM 1594 CB PRO A 207 31.520 10.642 26.890 1.00 38.19 C ANISOU 1594 CB PRO A 207 4805 5184 4521 -2460 -127 41 C ATOM 1595 CG PRO A 207 31.613 10.806 25.420 1.00 38.68 C ANISOU 1595 CG PRO A 207 5223 4975 4497 -2829 320 -383 C ATOM 1596 CD PRO A 207 30.221 10.636 24.886 1.00 32.95 C ANISOU 1596 CD PRO A 207 4947 3826 3745 -1700 440 -261 C ATOM 1597 N GLU A 208 28.885 10.771 28.331 1.00 30.73 N ANISOU 1597 N GLU A 208 4653 4136 2888 -1833 -697 122 N ATOM 1598 CA GLU A 208 28.195 11.185 29.548 1.00 33.48 C ANISOU 1598 CA GLU A 208 4909 4040 3773 -2139 -62 -381 C ATOM 1599 C GLU A 208 27.193 10.136 30.009 1.00 33.25 C ANISOU 1599 C GLU A 208 6192 4184 2258 -2745 -509 -69 C ATOM 1600 O GLU A 208 26.946 10.007 31.211 1.00 33.52 O ANISOU 1600 O GLU A 208 6721 3707 2308 -1462 -60 -324 O ATOM 1601 CB GLU A 208 27.542 12.544 29.300 1.00 39.62 C ANISOU 1601 CB GLU A 208 6742 3549 4764 -2051 263 -506 C ATOM 1602 CG GLU A 208 28.461 13.738 29.115 1.00 55.68 C ANISOU 1602 CG GLU A 208 10592 4384 6180 -3818 1632 -248 C ATOM 1603 CD GLU A 208 29.405 13.728 27.930 1.00 58.32 C ANISOU 1603 CD GLU A 208 9591 4856 7712 -3368 2193 -19 C ATOM 1604 OE1 GLU A 208 29.048 13.210 26.843 1.00 50.04 O ANISOU 1604 OE1 GLU A 208 7733 3671 7610 -556 2775 -761 O ATOM 1605 OE2 GLU A 208 30.537 14.258 28.093 1.00 63.50 O ANISOU 1605 OE2 GLU A 208 8931 4473 10724 -2509 1679 -52 O ATOM 1606 N THR A 209 26.602 9.360 29.121 1.00 29.30 N ANISOU 1606 N THR A 209 5540 3058 2536 -1762 -597 -193 N ATOM 1607 CA THR A 209 25.560 8.395 29.481 1.00 25.22 C ANISOU 1607 CA THR A 209 4456 2670 2456 -1017 -125 -806 C ATOM 1608 C THR A 209 26.124 6.983 29.497 1.00 22.78 C ANISOU 1608 C THR A 209 3822 2776 2056 -1033 -131 -483 C ATOM 1609 O THR A 209 25.394 6.017 29.688 1.00 24.73 O ANISOU 1609 O THR A 209 4092 2850 2453 -1193 -48 -152 O ATOM 1610 CB THR A 209 24.314 8.446 28.571 1.00 24.90 C ANISOU 1610 CB THR A 209 4271 2655 2534 -345 52 -979 C ATOM 1611 OG1 THR A 209 24.669 8.094 27.265 1.00 23.64 O ANISOU 1611 OG1 THR A 209 4355 2402 2226 -801 43 -489 O ATOM 1612 CG2 THR A 209 23.733 9.859 28.508 1.00 28.45 C ANISOU 1612 CG2 THR A 209 5235 2609 2966 -301 336 -519 C ATOM 1613 N THR A 210 27.424 6.852 29.278 1.00 25.41 N ANISOU 1613 N THR A 210 3856 3352 2446 -1120 83 -729 N ATOM 1614 CA THR A 210 28.058 5.549 29.393 1.00 23.13 C ANISOU 1614 CA THR A 210 3156 3329 2305 -1284 645 -373 C ATOM 1615 C THR A 210 28.014 5.091 30.851 1.00 23.00 C ANISOU 1615 C THR A 210 2564 3899 2277 -1233 606 -374 C ATOM 1616 O THR A 210 28.446 5.801 31.773 1.00 24.59 O ANISOU 1616 O THR A 210 3048 3739 2555 -940 -539 36 O ATOM 1617 CB THR A 210 29.511 5.573 28.896 1.00 27.15 C ANISOU 1617 CB THR A 210 3612 4091 2613 -1534 1333 -905 C ATOM 1618 OG1 THR A 210 29.494 5.855 27.485 1.00 28.67 O ANISOU 1618 OG1 THR A 210 4035 4125 2733 -1576 1338 -695 O ATOM 1619 CG2 THR A 210 30.206 4.233 29.055 1.00 27.17 C ANISOU 1619 CG2 THR A 210 2951 4865 2506 -1081 1019 -888 C ATOM 1620 N HIS A 211 27.523 3.904 31.108 1.00 21.68 N ANISOU 1620 N HIS A 211 2435 3584 2219 -753 -355 149 N ATOM 1621 CA HIS A 211 27.360 3.355 32.425 1.00 22.37 C ANISOU 1621 CA HIS A 211 1988 4131 2380 -337 -42 369 C ATOM 1622 C HIS A 211 26.451 4.252 33.279 1.00 22.70 C ANISOU 1622 C HIS A 211 2309 3689 2625 -551 40 141 C ATOM 1623 O HIS A 211 26.616 4.360 34.497 1.00 24.03 O ANISOU 1623 O HIS A 211 2857 3599 2674 -504 -203 -27 O ATOM 1624 CB HIS A 211 28.709 3.124 33.160 1.00 23.16 C ANISOU 1624 CB HIS A 211 2361 3985 2453 -304 -497 -81 C ATOM 1625 CG HIS A 211 29.455 1.946 32.598 1.00 23.61 C ANISOU 1625 CG HIS A 211 2187 4130 2655 -233 -560 -195 C ATOM 1626 ND1 HIS A 211 30.594 1.424 33.136 1.00 25.53 N ANISOU 1626 ND1 HIS A 211 2261 4624 2816 -46 -532 -213 N ATOM 1627 CD2 HIS A 211 29.218 1.210 31.464 1.00 24.34 C ANISOU 1627 CD2 HIS A 211 2346 3893 3009 -399 -574 -330 C ATOM 1628 CE1 HIS A 211 31.029 0.405 32.399 1.00 28.17 C ANISOU 1628 CE1 HIS A 211 2183 4383 4137 -141 -747 -649 C ATOM 1629 NE2 HIS A 211 30.229 0.243 31.371 1.00 24.68 N ANISOU 1629 NE2 HIS A 211 2449 3580 3350 -487 -397 -183 N ATOM 1630 N ILE A 212 25.472 4.910 32.641 1.00 20.98 N ANISOU 1630 N ILE A 212 2818 2554 2598 -528 -156 -320 N ATOM 1631 CA ILE A 212 24.500 5.668 33.419 1.00 20.47 C ANISOU 1631 CA ILE A 212 3225 2297 2255 -452 -191 -350 C ATOM 1632 C ILE A 212 23.747 4.752 34.372 1.00 18.75 C ANISOU 1632 C ILE A 212 2669 2486 1971 -256 -532 -226 C ATOM 1633 O ILE A 212 23.330 5.186 35.442 1.00 21.68 O ANISOU 1633 O ILE A 212 3151 2817 2268 -341 -32 -420 O ATOM 1634 CB ILE A 212 23.556 6.425 32.482 1.00 18.97 C ANISOU 1634 CB ILE A 212 2854 2512 1840 -573 53 -182 C ATOM 1635 CG1 ILE A 212 22.731 7.496 33.208 1.00 22.28 C ANISOU 1635 CG1 ILE A 212 3140 2825 2501 -214 -113 -452 C ATOM 1636 CG2 ILE A 212 22.637 5.503 31.672 1.00 21.59 C ANISOU 1636 CG2 ILE A 212 2770 2638 2794 -644 -111 -382 C ATOM 1637 CD1 ILE A 212 22.165 8.506 32.213 1.00 21.31 C ANISOU 1637 CD1 ILE A 212 2757 2816 2524 -328 -26 -396 C ATOM 1638 N ILE A 213 23.585 3.478 34.003 1.00 19.46 N ANISOU 1638 N ILE A 213 2557 2366 2473 -381 -441 -205 N ATOM 1639 CA ILE A 213 23.124 2.436 34.949 1.00 19.08 C ANISOU 1639 CA ILE A 213 2130 2714 2406 -437 -588 -40 C ATOM 1640 C ILE A 213 24.352 1.793 35.586 1.00 17.79 C ANISOU 1640 C ILE A 213 2013 2843 1902 -329 -328 -217 C ATOM 1641 O ILE A 213 24.940 0.910 34.964 1.00 21.23 O ANISOU 1641 O ILE A 213 2511 3590 1964 182 -335 -431 O ATOM 1642 CB ILE A 213 22.261 1.379 34.242 1.00 18.60 C ANISOU 1642 CB ILE A 213 1823 2953 2291 -567 -321 -89 C ATOM 1643 CG1 ILE A 213 21.140 1.995 33.405 1.00 18.69 C ANISOU 1643 CG1 ILE A 213 2002 2575 2523 -387 -467 -244 C ATOM 1644 CG2 ILE A 213 21.700 0.342 35.201 1.00 19.58 C ANISOU 1644 CG2 ILE A 213 2356 2858 2227 -561 -163 -144 C ATOM 1645 CD1 ILE A 213 20.257 2.880 34.206 1.00 22.55 C ANISOU 1645 CD1 ILE A 213 2356 3397 2815 -36 -718 -842 C ATOM 1646 N ASN A 214 24.723 2.273 36.778 1.00 20.29 N ANISOU 1646 N ASN A 214 1939 3609 2162 -128 -415 -640 N ATOM 1647 CA ASN A 214 25.834 1.732 37.530 1.00 22.09 C ANISOU 1647 CA ASN A 214 2142 3889 2361 -475 -724 -280 C ATOM 1648 C ASN A 214 25.334 0.998 38.754 1.00 22.29 C ANISOU 1648 C ASN A 214 2361 3907 2199 -742 -801 -475 C ATOM 1649 O ASN A 214 24.108 0.880 38.929 1.00 20.65 O ANISOU 1649 O ASN A 214 2340 3397 2109 -242 -579 -385 O ATOM 1650 CB ASN A 214 26.815 2.858 37.863 1.00 23.54 C ANISOU 1650 CB ASN A 214 2315 4414 2214 -852 -557 -342 C ATOM 1651 CG ASN A 214 26.138 3.941 38.683 1.00 23.17 C ANISOU 1651 CG ASN A 214 2367 3822 2614 -926 -525 -182 C ATOM 1652 OD1 ASN A 214 25.125 3.702 39.341 1.00 23.82 O ANISOU 1652 OD1 ASN A 214 2342 4104 2604 -793 -413 -303 O ATOM 1653 ND2 ASN A 214 26.705 5.137 38.637 1.00 35.76 N ANISOU 1653 ND2 ASN A 214 4393 4268 4925 -1917 475 -656 N ATOM 1654 N ARG A 215 26.286 0.510 39.556 1.00 22.42 N ANISOU 1654 N ARG A 215 2257 4076 2184 -309 -467 -314 N ATOM 1655 CA ARG A 215 25.833 -0.316 40.691 1.00 23.81 C ANISOU 1655 CA ARG A 215 1949 4873 2225 -366 -355 -73 C ATOM 1656 C ARG A 215 24.899 0.471 41.593 1.00 23.33 C ANISOU 1656 C ARG A 215 2147 4623 2093 -393 -581 -233 C ATOM 1657 O ARG A 215 23.899 -0.033 42.083 1.00 22.08 O ANISOU 1657 O ARG A 215 2227 4142 2022 -52 -339 -188 O ATOM 1658 CB ARG A 215 27.034 -0.838 41.499 1.00 27.34 C ANISOU 1658 CB ARG A 215 2325 5061 3001 -115 -481 528 C ATOM 1659 CG ARG A 215 26.649 -1.863 42.561 1.00 30.64 C ANISOU 1659 CG ARG A 215 3530 5354 2757 -412 -511 521 C ATOM 1660 CD ARG A 215 27.831 -2.254 43.406 1.00 31.18 C ANISOU 1660 CD ARG A 215 3610 4886 3352 -446 -575 958 C ATOM 1661 NE ARG A 215 27.463 -3.247 44.402 1.00 37.95 N ANISOU 1661 NE ARG A 215 5808 5093 3518 -1257 -1104 1186 N ATOM 1662 CZ ARG A 215 27.719 -4.539 44.459 1.00 36.48 C ANISOU 1662 CZ ARG A 215 4349 5340 4173 -888 -1549 1703 C ATOM 1663 NH1 ARG A 215 28.404 -5.148 43.513 1.00 39.89 N ANISOU 1663 NH1 ARG A 215 2946 6056 6155 -399 -1443 1004 N ATOM 1664 NH2 ARG A 215 27.265 -5.222 45.490 1.00 44.20 N ANISOU 1664 NH2 ARG A 215 7610 5774 3409 -2812 -2631 1664 N ATOM 1665 N GLU A 216 25.229 1.744 41.869 1.00 25.55 N ANISOU 1665 N GLU A 216 2676 5016 2016 -885 -724 -595 N ATOM 1666 CA GLU A 216 24.346 2.531 42.732 1.00 26.81 C ANISOU 1666 CA GLU A 216 3041 4869 2277 -575 -780 -661 C ATOM 1667 C GLU A 216 22.941 2.661 42.164 1.00 22.99 C ANISOU 1667 C GLU A 216 3050 3594 2090 -663 -654 -458 C ATOM 1668 O GLU A 216 21.978 2.494 42.924 1.00 21.91 O ANISOU 1668 O GLU A 216 3047 3289 1987 335 -474 -494 O ATOM 1669 CB GLU A 216 24.929 3.926 42.971 1.00 25.81 C ANISOU 1669 CB GLU A 216 2320 4893 2592 -450 -784 -499 C ATOM 1670 CG GLU A 216 24.175 4.747 43.994 1.00 30.27 C ANISOU 1670 CG GLU A 216 3128 5474 2898 -682 -733 -1358 C ATOM 1671 CD GLU A 216 24.763 6.132 44.241 1.00 34.37 C ANISOU 1671 CD GLU A 216 4249 5449 3359 -713 -2258 -1299 C ATOM 1672 OE1 GLU A 216 25.615 6.578 43.429 1.00 46.41 O ANISOU 1672 OE1 GLU A 216 6798 6227 4608 -2570 -1792 -235 O ATOM 1673 OE2 GLU A 216 24.351 6.782 45.237 1.00 51.41 O ANISOU 1673 OE2 GLU A 216 9187 6128 4217 -210 -1787 -2257 O ATOM 1674 N VAL A 217 22.810 2.933 40.887 1.00 21.27 N ANISOU 1674 N VAL A 217 2761 3147 2172 -471 -485 -249 N ATOM 1675 CA VAL A 217 21.499 2.966 40.251 1.00 19.95 C ANISOU 1675 CA VAL A 217 2670 3018 1892 -222 -291 -577 C ATOM 1676 C VAL A 217 20.802 1.620 40.359 1.00 19.23 C ANISOU 1676 C VAL A 217 2210 2904 2194 43 -627 -172 C ATOM 1677 O VAL A 217 19.609 1.542 40.655 1.00 20.05 O ANISOU 1677 O VAL A 217 2342 3070 2207 16 -323 -290 O ATOM 1678 CB VAL A 217 21.582 3.436 38.781 1.00 18.34 C ANISOU 1678 CB VAL A 217 2318 2761 1888 -168 -292 -616 C ATOM 1679 CG1 VAL A 217 20.257 3.332 38.027 1.00 20.78 C ANISOU 1679 CG1 VAL A 217 2639 2787 2470 -126 -765 -726 C ATOM 1680 CG2 VAL A 217 22.061 4.874 38.766 1.00 21.21 C ANISOU 1680 CG2 VAL A 217 2634 2873 2551 -422 -351 -514 C ATOM 1681 N ILE A 218 21.488 0.519 40.142 1.00 18.70 N ANISOU 1681 N ILE A 218 2247 2958 1898 20 -556 -234 N ATOM 1682 CA ILE A 218 20.868 -0.810 40.157 1.00 20.99 C ANISOU 1682 CA ILE A 218 2839 2958 2177 -148 -143 -562 C ATOM 1683 C ILE A 218 20.346 -1.157 41.529 1.00 20.81 C ANISOU 1683 C ILE A 218 2239 3350 2318 140 -527 273 C ATOM 1684 O ILE A 218 19.216 -1.637 41.709 1.00 20.72 O ANISOU 1684 O ILE A 218 2309 2817 2748 232 -295 73 O ATOM 1685 CB ILE A 218 21.907 -1.844 39.649 1.00 21.02 C ANISOU 1685 CB ILE A 218 2612 2906 2468 87 -487 -188 C ATOM 1686 CG1 ILE A 218 22.192 -1.716 38.158 1.00 20.02 C ANISOU 1686 CG1 ILE A 218 2186 2851 2569 -198 -70 -586 C ATOM 1687 CG2 ILE A 218 21.502 -3.257 40.064 1.00 23.03 C ANISOU 1687 CG2 ILE A 218 3103 2960 2686 -19 -611 -81 C ATOM 1688 CD1 ILE A 218 23.450 -2.447 37.712 1.00 22.08 C ANISOU 1688 CD1 ILE A 218 2722 2750 2919 454 -276 -152 C ATOM 1689 N ASP A 219 21.199 -0.885 42.539 1.00 20.85 N ANISOU 1689 N ASP A 219 2148 3416 2356 527 -474 34 N ATOM 1690 CA ASP A 219 20.742 -1.131 43.885 1.00 23.45 C ANISOU 1690 CA ASP A 219 3002 3658 2248 375 -440 -185 C ATOM 1691 C ASP A 219 19.570 -0.220 44.273 1.00 21.71 C ANISOU 1691 C ASP A 219 2699 3665 1886 122 -372 -215 C ATOM 1692 O ASP A 219 18.756 -0.679 45.070 1.00 27.79 O ANISOU 1692 O ASP A 219 2970 5351 2237 252 -178 535 O ATOM 1693 CB ASP A 219 21.874 -0.982 44.893 1.00 25.24 C ANISOU 1693 CB ASP A 219 2849 4431 2309 304 -438 -52 C ATOM 1694 CG ASP A 219 22.849 -2.135 44.937 1.00 26.57 C ANISOU 1694 CG ASP A 219 2687 4457 2953 264 -594 -224 C ATOM 1695 OD1 ASP A 219 22.521 -3.280 44.548 1.00 31.96 O ANISOU 1695 OD1 ASP A 219 4013 4350 3780 291 -872 -328 O ATOM 1696 OD2 ASP A 219 23.995 -1.951 45.358 1.00 32.77 O ANISOU 1696 OD2 ASP A 219 2920 5500 4031 136 -1244 459 O ATOM 1697 N ALA A 220 19.474 1.007 43.805 1.00 22.74 N ANISOU 1697 N ALA A 220 3072 3405 2163 234 -642 -569 N ATOM 1698 CA ALA A 220 18.327 1.859 44.139 1.00 23.48 C ANISOU 1698 CA ALA A 220 3359 3063 2500 -53 -346 -1216 C ATOM 1699 C ALA A 220 17.063 1.311 43.494 1.00 21.28 C ANISOU 1699 C ALA A 220 3003 3043 2039 161 -423 -381 C ATOM 1700 O ALA A 220 16.009 1.365 44.102 1.00 23.34 O ANISOU 1700 O ALA A 220 3156 3218 2496 505 -131 -315 O ATOM 1701 CB ALA A 220 18.580 3.287 43.716 1.00 22.91 C ANISOU 1701 CB ALA A 220 3186 3231 2290 77 -685 -842 C ATOM 1702 N LEU A 221 17.175 0.760 42.278 1.00 18.46 N ANISOU 1702 N LEU A 221 2450 2824 1739 128 -674 4 N ATOM 1703 CA LEU A 221 16.039 0.120 41.615 1.00 18.45 C ANISOU 1703 CA LEU A 221 2166 2902 1940 227 -369 -249 C ATOM 1704 C LEU A 221 15.603 -1.092 42.422 1.00 21.58 C ANISOU 1704 C LEU A 221 2546 3406 2247 -297 -929 173 C ATOM 1705 O LEU A 221 14.415 -1.325 42.679 1.00 22.15 O ANISOU 1705 O LEU A 221 2840 3092 2483 20 61 -177 O ATOM 1706 CB LEU A 221 16.427 -0.144 40.160 1.00 18.36 C ANISOU 1706 CB LEU A 221 2385 2440 2150 56 -145 -724 C ATOM 1707 CG LEU A 221 15.403 -0.793 39.242 1.00 17.64 C ANISOU 1707 CG LEU A 221 2488 2401 1812 28 -368 -80 C ATOM 1708 CD1 LEU A 221 14.142 0.048 39.202 1.00 19.28 C ANISOU 1708 CD1 LEU A 221 2860 2550 1915 306 -574 92 C ATOM 1709 CD2 LEU A 221 16.028 -0.991 37.856 1.00 19.11 C ANISOU 1709 CD2 LEU A 221 2617 3059 1585 -79 -496 68 C ATOM 1710 N GLY A 222 16.578 -1.862 42.878 1.00 21.26 N ANISOU 1710 N GLY A 222 2838 2863 2378 -128 -694 11 N ATOM 1711 CA GLY A 222 16.378 -2.855 43.878 1.00 20.42 C ANISOU 1711 CA GLY A 222 2742 2583 2432 411 144 -144 C ATOM 1712 C GLY A 222 15.714 -4.182 43.534 1.00 20.75 C ANISOU 1712 C GLY A 222 3230 2430 2224 478 -364 27 C ATOM 1713 O GLY A 222 15.362 -4.541 42.427 1.00 21.04 O ANISOU 1713 O GLY A 222 2916 3072 2007 316 85 -134 O ATOM 1714 N PRO A 223 15.587 -4.971 44.610 1.00 22.84 N ANISOU 1714 N PRO A 223 3723 2783 2173 124 -383 139 N ATOM 1715 CA PRO A 223 15.191 -6.364 44.500 1.00 23.57 C ANISOU 1715 CA PRO A 223 4152 2685 2119 210 -389 221 C ATOM 1716 C PRO A 223 13.818 -6.600 43.905 1.00 24.55 C ANISOU 1716 C PRO A 223 3856 3086 2386 -429 163 368 C ATOM 1717 O PRO A 223 13.608 -7.750 43.482 1.00 27.93 O ANISOU 1717 O PRO A 223 4968 3311 2333 -235 -771 106 O ATOM 1718 CB PRO A 223 15.159 -6.888 45.939 1.00 30.24 C ANISOU 1718 CB PRO A 223 6119 3276 2094 -537 -385 308 C ATOM 1719 CG PRO A 223 15.915 -5.898 46.739 1.00 39.79 C ANISOU 1719 CG PRO A 223 9695 3471 1953 -1851 -714 405 C ATOM 1720 CD PRO A 223 15.872 -4.583 46.006 1.00 26.59 C ANISOU 1720 CD PRO A 223 4674 3144 2283 -42 -794 103 C ATOM 1721 N LYS A 224 12.983 -5.583 43.850 1.00 23.59 N ANISOU 1721 N LYS A 224 3618 3364 1980 -358 -369 338 N ATOM 1722 CA LYS A 224 11.675 -5.737 43.243 1.00 27.36 C ANISOU 1722 CA LYS A 224 3759 4644 1992 -907 -457 754 C ATOM 1723 C LYS A 224 11.526 -4.834 42.014 1.00 25.70 C ANISOU 1723 C LYS A 224 3129 4043 2591 -583 -472 945 C ATOM 1724 O LYS A 224 10.449 -4.830 41.394 1.00 33.30 O ANISOU 1724 O LYS A 224 3271 6470 2912 -1268 -759 1729 O ATOM 1725 CB LYS A 224 10.556 -5.452 44.240 1.00 29.28 C ANISOU 1725 CB LYS A 224 3636 4991 2496 -197 -354 1107 C ATOM 1726 CG LYS A 224 10.590 -6.146 45.572 1.00 33.46 C ANISOU 1726 CG LYS A 224 4153 5539 3023 -930 229 1868 C ATOM 1727 CD LYS A 224 10.361 -7.637 45.488 1.00 38.86 C ANISOU 1727 CD LYS A 224 5110 5680 3976 -1453 391 1858 C ATOM 1728 CE LYS A 224 10.236 -8.205 46.892 1.00 50.19 C ANISOU 1728 CE LYS A 224 8356 6360 4355 -2842 -1365 2803 C ATOM 1729 NZ LYS A 224 10.899 -9.543 47.019 1.00 54.87 N ANISOU 1729 NZ LYS A 224 8807 7140 4903 -2016 -1770 2903 N ATOM 1730 N GLY A 225 12.597 -4.149 41.640 1.00 20.21 N ANISOU 1730 N GLY A 225 2994 2931 1755 -203 -199 -68 N ATOM 1731 CA GLY A 225 12.629 -3.406 40.400 1.00 18.23 C ANISOU 1731 CA GLY A 225 2412 2653 1862 247 55 -36 C ATOM 1732 C GLY A 225 13.084 -4.163 39.171 1.00 17.34 C ANISOU 1732 C GLY A 225 2401 2370 1816 134 -201 -40 C ATOM 1733 O GLY A 225 13.811 -5.161 39.258 1.00 17.89 O ANISOU 1733 O GLY A 225 2834 2173 1792 166 -88 30 O ATOM 1734 N VAL A 226 12.700 -3.694 37.973 1.00 16.46 N ANISOU 1734 N VAL A 226 2318 2152 1782 97 -170 -133 N ATOM 1735 CA VAL A 226 13.044 -4.246 36.673 1.00 15.24 C ANISOU 1735 CA VAL A 226 1935 2007 1848 185 -174 -90 C ATOM 1736 C VAL A 226 13.639 -3.169 35.788 1.00 15.17 C ANISOU 1736 C VAL A 226 2163 1795 1807 213 -54 -313 C ATOM 1737 O VAL A 226 13.064 -2.093 35.635 1.00 16.35 O ANISOU 1737 O VAL A 226 2035 1764 2413 146 -368 -187 O ATOM 1738 CB VAL A 226 11.776 -4.824 36.026 1.00 15.64 C ANISOU 1738 CB VAL A 226 2046 2120 1777 129 -186 -125 C ATOM 1739 CG1 VAL A 226 12.029 -5.251 34.602 1.00 16.76 C ANISOU 1739 CG1 VAL A 226 2050 2202 2118 283 -56 -595 C ATOM 1740 CG2 VAL A 226 11.277 -5.996 36.897 1.00 18.78 C ANISOU 1740 CG2 VAL A 226 2177 2304 2656 -87 -14 155 C ATOM 1741 N LEU A 227 14.798 -3.483 35.215 1.00 16.20 N ANISOU 1741 N LEU A 227 2072 2171 1910 211 -11 -95 N ATOM 1742 CA LEU A 227 15.521 -2.666 34.264 1.00 14.19 C ANISOU 1742 CA LEU A 227 1862 1785 1743 183 -442 7 C ATOM 1743 C LEU A 227 15.153 -3.081 32.837 1.00 14.28 C ANISOU 1743 C LEU A 227 1956 1685 1784 412 -390 -121 C ATOM 1744 O LEU A 227 15.164 -4.274 32.555 1.00 15.54 O ANISOU 1744 O LEU A 227 2405 1687 1811 255 -84 -101 O ATOM 1745 CB LEU A 227 17.042 -2.821 34.431 1.00 14.96 C ANISOU 1745 CB LEU A 227 1775 1758 2152 171 -311 -481 C ATOM 1746 CG LEU A 227 17.866 -1.935 33.481 1.00 17.70 C ANISOU 1746 CG LEU A 227 1920 2017 2787 212 -120 -59 C ATOM 1747 CD1 LEU A 227 17.704 -0.472 33.813 1.00 16.78 C ANISOU 1747 CD1 LEU A 227 2043 2042 2289 -90 -141 -119 C ATOM 1748 CD2 LEU A 227 19.322 -2.330 33.514 1.00 18.28 C ANISOU 1748 CD2 LEU A 227 1873 2369 2704 56 -218 -279 C ATOM 1749 N ILE A 228 14.811 -2.096 32.008 1.00 14.05 N ANISOU 1749 N ILE A 228 1662 1885 1792 124 -376 167 N ATOM 1750 CA ILE A 228 14.524 -2.347 30.595 1.00 13.94 C ANISOU 1750 CA ILE A 228 1759 1787 1749 221 -307 -8 C ATOM 1751 C ILE A 228 15.554 -1.586 29.764 1.00 14.50 C ANISOU 1751 C ILE A 228 1710 1939 1861 43 -282 -45 C ATOM 1752 O ILE A 228 15.598 -0.359 29.884 1.00 16.62 O ANISOU 1752 O ILE A 228 2413 1947 1954 12 310 -92 O ATOM 1753 CB ILE A 228 13.103 -1.923 30.194 1.00 13.87 C ANISOU 1753 CB ILE A 228 1662 2037 1572 174 -254 -326 C ATOM 1754 CG1 ILE A 228 12.030 -2.587 31.068 1.00 15.69 C ANISOU 1754 CG1 ILE A 228 1930 1934 2098 140 98 -223 C ATOM 1755 CG2 ILE A 228 12.831 -2.141 28.691 1.00 15.07 C ANISOU 1755 CG2 ILE A 228 2124 1935 1665 -23 -518 -201 C ATOM 1756 CD1 ILE A 228 11.898 -4.101 30.871 1.00 14.55 C ANISOU 1756 CD1 ILE A 228 1738 1875 1916 469 -167 -64 C ATOM 1757 N ASN A 229 16.386 -2.230 28.961 1.00 14.74 N ANISOU 1757 N ASN A 229 1767 1754 2080 123 -209 57 N ATOM 1758 CA ASN A 229 17.345 -1.510 28.129 1.00 14.71 C ANISOU 1758 CA ASN A 229 1729 1691 2170 172 -117 21 C ATOM 1759 C ASN A 229 17.057 -1.775 26.655 1.00 15.50 C ANISOU 1759 C ASN A 229 1685 2068 2136 235 -129 -53 C ATOM 1760 O ASN A 229 17.296 -2.872 26.165 1.00 15.48 O ANISOU 1760 O ASN A 229 1877 1819 2188 -63 -244 44 O ATOM 1761 CB ASN A 229 18.794 -1.867 28.445 1.00 15.35 C ANISOU 1761 CB ASN A 229 1764 1853 2216 120 -283 -46 C ATOM 1762 CG ASN A 229 19.766 -0.909 27.783 1.00 16.15 C ANISOU 1762 CG ASN A 229 1671 2184 2281 21 -372 -13 C ATOM 1763 OD1 ASN A 229 19.345 0.080 27.165 1.00 15.52 O ANISOU 1763 OD1 ASN A 229 1561 2275 2063 59 -95 115 O ATOM 1764 ND2 ASN A 229 21.065 -1.174 27.941 1.00 17.20 N ANISOU 1764 ND2 ASN A 229 1700 2398 2438 -25 -632 50 N ATOM 1765 N ILE A 230 16.543 -0.749 25.987 1.00 15.57 N ANISOU 1765 N ILE A 230 1946 1869 2103 122 -312 -188 N ATOM 1766 CA ILE A 230 16.377 -0.717 24.549 1.00 15.90 C ANISOU 1766 CA ILE A 230 1814 2063 2164 -42 -177 11 C ATOM 1767 C ILE A 230 17.317 0.312 23.903 1.00 18.14 C ANISOU 1767 C ILE A 230 2543 1940 2409 -517 -663 271 C ATOM 1768 O ILE A 230 17.148 0.616 22.733 1.00 19.98 O ANISOU 1768 O ILE A 230 2352 2645 2593 -583 -763 677 O ATOM 1769 CB ILE A 230 14.916 -0.487 24.132 1.00 17.85 C ANISOU 1769 CB ILE A 230 2080 2296 2407 130 -485 336 C ATOM 1770 CG1 ILE A 230 14.253 0.714 24.797 1.00 21.69 C ANISOU 1770 CG1 ILE A 230 2254 2538 3447 540 -546 120 C ATOM 1771 CG2 ILE A 230 14.184 -1.809 24.361 1.00 17.97 C ANISOU 1771 CG2 ILE A 230 1772 2576 2479 -103 -486 45 C ATOM 1772 CD1 ILE A 230 14.579 2.064 24.250 1.00 30.31 C ANISOU 1772 CD1 ILE A 230 5460 2245 3812 -59 567 -637 C ATOM 1773 N GLY A 231 18.266 0.815 24.670 1.00 17.46 N ANISOU 1773 N GLY A 231 2029 2199 2408 -241 -428 -36 N ATOM 1774 CA GLY A 231 19.206 1.830 24.226 1.00 17.19 C ANISOU 1774 CA GLY A 231 1732 1869 2930 25 -510 17 C ATOM 1775 C GLY A 231 20.380 1.200 23.528 1.00 16.01 C ANISOU 1775 C GLY A 231 1871 1981 2232 263 -518 309 C ATOM 1776 O GLY A 231 20.445 0.674 22.413 1.00 19.53 O ANISOU 1776 O GLY A 231 2504 2184 2730 -129 -593 -307 O ATOM 1777 N ARG A 232 21.514 1.097 24.157 1.00 18.13 N ANISOU 1777 N ARG A 232 1661 2842 2384 65 -275 42 N ATOM 1778 CA ARG A 232 22.793 0.557 23.919 1.00 16.48 C ANISOU 1778 CA ARG A 232 1500 2848 1916 -155 -330 -134 C ATOM 1779 C ARG A 232 23.392 -0.131 25.143 1.00 16.21 C ANISOU 1779 C ARG A 232 1710 2501 1949 -163 -356 -87 C ATOM 1780 O ARG A 232 23.252 0.225 26.295 1.00 16.34 O ANISOU 1780 O ARG A 232 1932 2384 1891 -277 -254 70 O ATOM 1781 CB ARG A 232 23.786 1.617 23.389 1.00 17.69 C ANISOU 1781 CB ARG A 232 2243 2912 1566 -240 247 -192 C ATOM 1782 CG ARG A 232 23.304 2.283 22.096 1.00 23.23 C ANISOU 1782 CG ARG A 232 3626 3116 2084 53 -202 175 C ATOM 1783 CD ARG A 232 23.622 1.407 20.878 1.00 34.48 C ANISOU 1783 CD ARG A 232 7067 4278 1757 -1980 -739 -951 C ATOM 1784 NE ARG A 232 23.473 2.137 19.623 1.00 30.44 N ANISOU 1784 NE ARG A 232 3887 5438 2240 -840 649 -105 N ATOM 1785 CZ ARG A 232 22.389 2.198 18.857 1.00 27.93 C ANISOU 1785 CZ ARG A 232 2915 4434 3263 198 973 197 C ATOM 1786 NH1 ARG A 232 21.275 1.564 19.196 1.00 41.10 N ANISOU 1786 NH1 ARG A 232 3537 3793 8287 -391 -229 2674 N ATOM 1787 NH2 ARG A 232 22.310 2.882 17.719 1.00 32.43 N ANISOU 1787 NH2 ARG A 232 4226 5583 2513 -570 391 -175 N ATOM 1788 N GLY A 233 24.117 -1.207 24.841 1.00 16.88 N ANISOU 1788 N GLY A 233 1639 2789 1984 -94 -149 -18 N ATOM 1789 CA GLY A 233 24.746 -2.013 25.835 1.00 17.71 C ANISOU 1789 CA GLY A 233 1724 2686 2318 -5 -431 -100 C ATOM 1790 C GLY A 233 25.606 -1.215 26.798 1.00 19.36 C ANISOU 1790 C GLY A 233 1846 3442 2068 -447 -276 -131 C ATOM 1791 O GLY A 233 25.432 -1.403 28.011 1.00 18.32 O ANISOU 1791 O GLY A 233 2217 2656 2086 -24 -119 -102 O ATOM 1792 N PRO A 234 26.501 -0.377 26.327 1.00 17.36 N ANISOU 1792 N PRO A 234 1746 2842 2009 -145 -229 -194 N ATOM 1793 CA PRO A 234 27.341 0.385 27.268 1.00 18.17 C ANISOU 1793 CA PRO A 234 2150 2796 1958 -335 -195 -164 C ATOM 1794 C PRO A 234 26.618 1.438 28.107 1.00 18.38 C ANISOU 1794 C PRO A 234 1995 2952 2039 -572 49 -287 C ATOM 1795 O PRO A 234 27.239 2.129 28.909 1.00 18.95 O ANISOU 1795 O PRO A 234 2314 2766 2120 -339 -288 -228 O ATOM 1796 CB PRO A 234 28.391 1.043 26.338 1.00 20.48 C ANISOU 1796 CB PRO A 234 1978 3602 2201 -592 97 -686 C ATOM 1797 CG PRO A 234 28.406 0.143 25.138 1.00 18.39 C ANISOU 1797 CG PRO A 234 1653 2986 2348 -106 -56 -613 C ATOM 1798 CD PRO A 234 26.924 -0.128 24.933 1.00 18.28 C ANISOU 1798 CD PRO A 234 1826 3121 1999 -261 -443 3 C ATOM 1799 N HIS A 235 25.315 1.608 28.006 1.00 18.80 N ANISOU 1799 N HIS A 235 2075 2730 2339 -398 -47 -26 N ATOM 1800 CA HIS A 235 24.568 2.359 28.985 1.00 18.33 C ANISOU 1800 CA HIS A 235 2038 2540 2388 -240 -107 135 C ATOM 1801 C HIS A 235 24.611 1.721 30.381 1.00 18.29 C ANISOU 1801 C HIS A 235 1953 2717 2278 -289 -100 99 C ATOM 1802 O HIS A 235 24.340 2.443 31.364 1.00 19.48 O ANISOU 1802 O HIS A 235 2082 2876 2445 -437 -188 -237 O ATOM 1803 CB HIS A 235 23.077 2.503 28.624 1.00 18.03 C ANISOU 1803 CB HIS A 235 2113 2385 2354 -315 -174 138 C ATOM 1804 CG HIS A 235 22.907 3.593 27.620 1.00 19.14 C ANISOU 1804 CG HIS A 235 2258 2388 2625 -403 -387 244 C ATOM 1805 ND1 HIS A 235 23.256 4.876 27.436 1.00 22.70 N ANISOU 1805 ND1 HIS A 235 3649 2243 2731 -457 -382 101 N ATOM 1806 CD2 HIS A 235 22.107 3.415 26.571 1.00 16.41 C ANISOU 1806 CD2 HIS A 235 1479 2379 2378 -60 89 220 C ATOM 1807 CE1 HIS A 235 22.760 5.395 26.322 1.00 19.37 C ANISOU 1807 CE1 HIS A 235 2480 2488 2391 -306 310 292 C ATOM 1808 NE2 HIS A 235 22.025 4.465 25.728 1.00 20.66 N ANISOU 1808 NE2 HIS A 235 2855 2769 2227 -266 87 361 N ATOM 1809 N VAL A 236 24.907 0.426 30.400 1.00 18.01 N ANISOU 1809 N VAL A 236 2146 2867 1829 -8 -677 -52 N ATOM 1810 CA VAL A 236 24.928 -0.307 31.662 1.00 18.24 C ANISOU 1810 CA VAL A 236 2284 2793 1852 143 -716 -140 C ATOM 1811 C VAL A 236 26.317 -0.832 31.965 1.00 18.93 C ANISOU 1811 C VAL A 236 2453 2725 2014 340 -700 -177 C ATOM 1812 O VAL A 236 26.994 -1.317 31.062 1.00 19.30 O ANISOU 1812 O VAL A 236 2256 3032 2047 3 -415 -52 O ATOM 1813 CB VAL A 236 23.951 -1.474 31.592 1.00 17.77 C ANISOU 1813 CB VAL A 236 2609 2266 1879 309 -926 65 C ATOM 1814 CG1 VAL A 236 23.879 -2.157 32.961 1.00 20.34 C ANISOU 1814 CG1 VAL A 236 2390 3409 1929 413 -611 407 C ATOM 1815 CG2 VAL A 236 22.546 -1.039 31.165 1.00 17.71 C ANISOU 1815 CG2 VAL A 236 2427 2452 1852 -60 -857 184 C ATOM 1816 N ASP A 237 26.727 -0.751 33.221 1.00 18.70 N ANISOU 1816 N ASP A 237 2101 3040 1966 260 -569 -57 N ATOM 1817 CA ASP A 237 27.874 -1.450 33.738 1.00 19.78 C ANISOU 1817 CA ASP A 237 2039 3238 2239 108 -710 41 C ATOM 1818 C ASP A 237 27.508 -2.926 33.791 1.00 17.83 C ANISOU 1818 C ASP A 237 1610 3103 2060 360 -10 3 C ATOM 1819 O ASP A 237 27.039 -3.391 34.835 1.00 21.70 O ANISOU 1819 O ASP A 237 2356 3893 1995 11 -147 299 O ATOM 1820 CB ASP A 237 28.266 -0.953 35.129 1.00 22.58 C ANISOU 1820 CB ASP A 237 2299 3760 2519 125 -1025 -218 C ATOM 1821 CG ASP A 237 29.629 -1.426 35.606 1.00 24.97 C ANISOU 1821 CG ASP A 237 2741 3658 3088 395 -1526 -350 C ATOM 1822 OD1 ASP A 237 30.131 -2.408 35.002 1.00 29.29 O ANISOU 1822 OD1 ASP A 237 3185 4541 3405 962 -1229 -632 O ATOM 1823 OD2 ASP A 237 30.187 -0.874 36.557 1.00 28.34 O ANISOU 1823 OD2 ASP A 237 2528 5158 3080 -71 -1315 -752 O ATOM 1824 N GLU A 238 27.670 -3.636 32.671 1.00 19.51 N ANISOU 1824 N GLU A 238 1824 3458 2129 164 -271 -204 N ATOM 1825 CA GLU A 238 27.038 -4.962 32.528 1.00 19.86 C ANISOU 1825 CA GLU A 238 2054 3484 2007 131 -390 -140 C ATOM 1826 C GLU A 238 27.479 -5.985 33.568 1.00 18.98 C ANISOU 1826 C GLU A 238 1743 3355 2113 500 -30 -180 C ATOM 1827 O GLU A 238 26.600 -6.699 34.098 1.00 20.51 O ANISOU 1827 O GLU A 238 1920 3660 2214 253 -243 27 O ATOM 1828 CB GLU A 238 27.287 -5.499 31.131 1.00 20.84 C ANISOU 1828 CB GLU A 238 2179 3686 2053 -242 -196 -252 C ATOM 1829 CG GLU A 238 26.415 -6.680 30.784 1.00 19.18 C ANISOU 1829 CG GLU A 238 1945 2931 2413 292 -239 -132 C ATOM 1830 CD GLU A 238 26.517 -6.960 29.291 1.00 19.53 C ANISOU 1830 CD GLU A 238 2284 2670 2467 250 -410 -263 C ATOM 1831 OE1 GLU A 238 27.298 -7.838 28.879 1.00 20.43 O ANISOU 1831 OE1 GLU A 238 2457 2833 2471 399 -287 -202 O ATOM 1832 OE2 GLU A 238 25.826 -6.207 28.571 1.00 19.12 O ANISOU 1832 OE2 GLU A 238 2020 2877 2368 280 -321 -287 O ATOM 1833 N PRO A 239 28.749 -6.124 33.929 1.00 24.07 N ANISOU 1833 N PRO A 239 1951 4122 3074 124 -470 586 N ATOM 1834 CA PRO A 239 29.112 -7.061 34.997 1.00 22.16 C ANISOU 1834 CA PRO A 239 1941 3753 2727 357 -444 144 C ATOM 1835 C PRO A 239 28.397 -6.785 36.312 1.00 22.76 C ANISOU 1835 C PRO A 239 2057 3919 2672 -226 -451 -201 C ATOM 1836 O PRO A 239 28.037 -7.753 37.007 1.00 23.48 O ANISOU 1836 O PRO A 239 2452 4000 2471 364 -575 170 O ATOM 1837 CB PRO A 239 30.637 -6.893 35.183 1.00 24.45 C ANISOU 1837 CB PRO A 239 2013 4656 2623 192 -470 498 C ATOM 1838 CG PRO A 239 31.051 -6.440 33.801 1.00 23.60 C ANISOU 1838 CG PRO A 239 1921 4506 2541 -48 -756 536 C ATOM 1839 CD PRO A 239 29.946 -5.492 33.367 1.00 21.89 C ANISOU 1839 CD PRO A 239 1750 4284 2284 -98 -797 52 C ATOM 1840 N GLU A 240 28.149 -5.519 36.650 1.00 21.58 N ANISOU 1840 N GLU A 240 2069 3972 2159 1 -804 -109 N ATOM 1841 CA GLU A 240 27.361 -5.196 37.851 1.00 21.52 C ANISOU 1841 CA GLU A 240 2106 3637 2432 -38 -471 179 C ATOM 1842 C GLU A 240 25.888 -5.582 37.699 1.00 19.80 C ANISOU 1842 C GLU A 240 2148 2971 2404 122 -630 666 C ATOM 1843 O GLU A 240 25.215 -6.000 38.641 1.00 20.84 O ANISOU 1843 O GLU A 240 2130 3348 2441 -126 -582 462 O ATOM 1844 CB GLU A 240 27.476 -3.728 38.191 1.00 23.02 C ANISOU 1844 CB GLU A 240 2284 3848 2614 7 -1016 -340 C ATOM 1845 CG GLU A 240 28.850 -3.205 38.585 1.00 27.29 C ANISOU 1845 CG GLU A 240 2584 5086 2700 -511 -920 -856 C ATOM 1846 CD GLU A 240 29.287 -3.592 39.969 1.00 29.54 C ANISOU 1846 CD GLU A 240 2798 5399 3026 -210 -1376 -659 C ATOM 1847 OE1 GLU A 240 28.478 -4.135 40.766 1.00 27.76 O ANISOU 1847 OE1 GLU A 240 2962 4457 3129 20 -1575 -189 O ATOM 1848 OE2 GLU A 240 30.478 -3.322 40.251 1.00 36.60 O ANISOU 1848 OE2 GLU A 240 3080 6530 4295 -669 -1861 460 O ATOM 1849 N LEU A 241 25.334 -5.441 36.503 1.00 18.95 N ANISOU 1849 N LEU A 241 2180 2679 2340 274 -641 308 N ATOM 1850 CA LEU A 241 23.951 -5.890 36.272 1.00 18.52 C ANISOU 1850 CA LEU A 241 2262 2767 2008 187 -466 147 C ATOM 1851 C LEU A 241 23.819 -7.395 36.464 1.00 18.45 C ANISOU 1851 C LEU A 241 2244 2666 2100 280 -406 -21 C ATOM 1852 O LEU A 241 22.926 -7.862 37.171 1.00 18.46 O ANISOU 1852 O LEU A 241 2249 2679 2087 293 -428 104 O ATOM 1853 CB LEU A 241 23.568 -5.503 34.867 1.00 18.43 C ANISOU 1853 CB LEU A 241 2294 2703 2006 218 -575 -14 C ATOM 1854 CG LEU A 241 22.166 -5.894 34.436 1.00 19.76 C ANISOU 1854 CG LEU A 241 2448 2914 2148 -307 -585 571 C ATOM 1855 CD1 LEU A 241 21.118 -5.224 35.308 1.00 25.21 C ANISOU 1855 CD1 LEU A 241 2303 4730 2544 44 -226 628 C ATOM 1856 CD2 LEU A 241 21.866 -5.562 32.971 1.00 20.72 C ANISOU 1856 CD2 LEU A 241 2410 3241 2222 -131 -718 642 C ATOM 1857 N VAL A 242 24.721 -8.163 35.829 1.00 19.34 N ANISOU 1857 N VAL A 242 2220 3018 2110 417 -479 -65 N ATOM 1858 CA VAL A 242 24.682 -9.617 35.994 1.00 21.18 C ANISOU 1858 CA VAL A 242 2395 2928 2724 693 -348 -77 C ATOM 1859 C VAL A 242 24.816 -10.006 37.467 1.00 21.33 C ANISOU 1859 C VAL A 242 2992 2474 2640 734 -322 -191 C ATOM 1860 O VAL A 242 24.027 -10.830 37.937 1.00 23.19 O ANISOU 1860 O VAL A 242 2835 3072 2905 499 -824 331 O ATOM 1861 CB VAL A 242 25.776 -10.343 35.183 1.00 20.65 C ANISOU 1861 CB VAL A 242 2105 3049 2691 423 -316 -7 C ATOM 1862 CG1 VAL A 242 25.786 -11.858 35.418 1.00 23.77 C ANISOU 1862 CG1 VAL A 242 2488 3012 3531 804 134 -92 C ATOM 1863 CG2 VAL A 242 25.599 -10.026 33.707 1.00 22.54 C ANISOU 1863 CG2 VAL A 242 2525 3500 2538 549 -583 -361 C ATOM 1864 N SER A 243 25.784 -9.457 38.219 1.00 21.77 N ANISOU 1864 N SER A 243 2304 3166 2803 711 -460 552 N ATOM 1865 CA SER A 243 25.946 -9.775 39.629 1.00 25.05 C ANISOU 1865 CA SER A 243 1443 4795 3282 714 -939 1560 C ATOM 1866 C SER A 243 24.669 -9.498 40.413 1.00 21.20 C ANISOU 1866 C SER A 243 1882 3622 2552 377 -826 885 C ATOM 1867 O SER A 243 24.245 -10.284 41.250 1.00 25.93 O ANISOU 1867 O SER A 243 3023 3672 3158 475 -215 1088 O ATOM 1868 CB SER A 243 27.070 -8.911 40.229 1.00 27.55 C ANISOU 1868 CB SER A 243 1593 5815 3059 654 -476 292 C ATOM 1869 OG SER A 243 27.203 -9.207 41.606 1.00 37.82 O ANISOU 1869 OG SER A 243 4930 6146 3293 7 -1358 459 O ATOM 1870 N ALA A 244 24.070 -8.324 40.144 1.00 22.07 N ANISOU 1870 N ALA A 244 2422 3679 2285 555 -880 783 N ATOM 1871 CA ALA A 244 22.886 -7.904 40.867 1.00 21.47 C ANISOU 1871 CA ALA A 244 2795 2857 2505 445 -670 493 C ATOM 1872 C ALA A 244 21.729 -8.869 40.599 1.00 22.14 C ANISOU 1872 C ALA A 244 2722 2903 2787 453 -136 -82 C ATOM 1873 O ALA A 244 20.958 -9.226 41.505 1.00 22.36 O ANISOU 1873 O ALA A 244 2538 3599 2360 359 -664 382 O ATOM 1874 CB ALA A 244 22.540 -6.460 40.498 1.00 24.82 C ANISOU 1874 CB ALA A 244 3484 2812 3136 479 -1811 238 C ATOM 1875 N LEU A 245 21.600 -9.320 39.331 1.00 19.82 N ANISOU 1875 N LEU A 245 2460 2406 2663 594 -222 199 N ATOM 1876 CA LEU A 245 20.541 -10.278 39.030 1.00 19.39 C ANISOU 1876 CA LEU A 245 2446 2560 2359 459 58 214 C ATOM 1877 C LEU A 245 20.779 -11.616 39.720 1.00 21.71 C ANISOU 1877 C LEU A 245 2679 2649 2923 206 -507 449 C ATOM 1878 O LEU A 245 19.898 -12.248 40.288 1.00 26.97 O ANISOU 1878 O LEU A 245 3006 3192 4051 428 -106 1358 O ATOM 1879 CB LEU A 245 20.414 -10.468 37.519 1.00 19.34 C ANISOU 1879 CB LEU A 245 2609 2335 2404 814 66 -41 C ATOM 1880 CG LEU A 245 19.811 -9.217 36.841 1.00 18.08 C ANISOU 1880 CG LEU A 245 2014 2301 2553 259 -108 252 C ATOM 1881 CD1 LEU A 245 20.159 -9.215 35.384 1.00 20.33 C ANISOU 1881 CD1 LEU A 245 2608 2531 2584 294 63 219 C ATOM 1882 CD2 LEU A 245 18.288 -9.128 37.040 1.00 19.96 C ANISOU 1882 CD2 LEU A 245 1930 2694 2959 152 -116 510 C ATOM 1883 N VAL A 246 21.998 -12.083 39.684 1.00 24.42 N ANISOU 1883 N VAL A 246 2820 2637 3822 292 -421 880 N ATOM 1884 CA VAL A 246 22.345 -13.384 40.231 1.00 24.81 C ANISOU 1884 CA VAL A 246 3251 2674 3502 492 32 910 C ATOM 1885 C VAL A 246 22.116 -13.344 41.738 1.00 25.92 C ANISOU 1885 C VAL A 246 2912 3498 3440 856 -151 851 C ATOM 1886 O VAL A 246 21.578 -14.289 42.332 1.00 32.60 O ANISOU 1886 O VAL A 246 5773 3315 3297 723 433 915 O ATOM 1887 CB VAL A 246 23.784 -13.739 39.839 1.00 23.35 C ANISOU 1887 CB VAL A 246 3028 3112 2731 622 -511 772 C ATOM 1888 CG1 VAL A 246 24.397 -14.858 40.670 1.00 28.63 C ANISOU 1888 CG1 VAL A 246 3971 3299 3607 1062 -255 1199 C ATOM 1889 CG2 VAL A 246 23.859 -14.155 38.364 1.00 25.10 C ANISOU 1889 CG2 VAL A 246 3662 2764 3111 717 -574 115 C ATOM 1890 N GLU A 247 22.474 -12.226 42.360 1.00 27.05 N ANISOU 1890 N GLU A 247 3719 3324 3236 1096 -92 953 N ATOM 1891 CA GLU A 247 22.417 -12.160 43.822 1.00 27.21 C ANISOU 1891 CA GLU A 247 3554 3563 3222 857 -279 1008 C ATOM 1892 C GLU A 247 21.118 -11.663 44.435 1.00 26.54 C ANISOU 1892 C GLU A 247 3735 3546 2801 1013 -403 832 C ATOM 1893 O GLU A 247 21.005 -11.548 45.657 1.00 28.46 O ANISOU 1893 O GLU A 247 3890 4135 2788 620 -398 748 O ATOM 1894 CB GLU A 247 23.557 -11.263 44.320 1.00 31.69 C ANISOU 1894 CB GLU A 247 3679 4238 4124 792 -1356 1458 C ATOM 1895 CG GLU A 247 24.937 -11.767 43.955 1.00 32.10 C ANISOU 1895 CG GLU A 247 3763 3895 4538 457 -709 1447 C ATOM 1896 CD GLU A 247 26.036 -10.833 44.437 1.00 36.73 C ANISOU 1896 CD GLU A 247 3669 4885 5400 844 -1477 439 C ATOM 1897 OE1 GLU A 247 25.783 -9.687 44.881 1.00 35.16 O ANISOU 1897 OE1 GLU A 247 4059 4690 4612 785 -1921 668 O ATOM 1898 OE2 GLU A 247 27.199 -11.284 44.331 1.00 50.09 O ANISOU 1898 OE2 GLU A 247 3813 6357 8861 1422 -2260 -804 O ATOM 1899 N GLY A 248 20.124 -11.379 43.619 1.00 26.03 N ANISOU 1899 N GLY A 248 3555 3640 2696 1012 -191 863 N ATOM 1900 CA GLY A 248 18.823 -10.951 44.083 1.00 25.57 C ANISOU 1900 CA GLY A 248 3421 3644 2650 677 -223 347 C ATOM 1901 C GLY A 248 18.714 -9.478 44.389 1.00 23.63 C ANISOU 1901 C GLY A 248 2971 3703 2303 533 -402 215 C ATOM 1902 O GLY A 248 17.685 -9.050 44.935 1.00 26.84 O ANISOU 1902 O GLY A 248 3623 3587 2987 492 493 380 O ATOM 1903 N ARG A 249 19.727 -8.705 44.054 1.00 22.90 N ANISOU 1903 N ARG A 249 2828 3681 2191 695 -498 509 N ATOM 1904 CA ARG A 249 19.701 -7.279 44.365 1.00 21.80 C ANISOU 1904 CA ARG A 249 2817 3808 1658 485 -242 212 C ATOM 1905 C ARG A 249 18.889 -6.465 43.353 1.00 18.91 C ANISOU 1905 C ARG A 249 2415 3142 1628 74 -167 262 C ATOM 1906 O ARG A 249 18.483 -5.329 43.624 1.00 21.36 O ANISOU 1906 O ARG A 249 3048 3114 1953 92 -260 25 O ATOM 1907 CB ARG A 249 21.135 -6.747 44.470 1.00 24.16 C ANISOU 1907 CB ARG A 249 2960 4148 2072 424 -786 326 C ATOM 1908 CG ARG A 249 21.822 -7.121 45.796 1.00 27.35 C ANISOU 1908 CG ARG A 249 3480 4694 2217 202 -988 624 C ATOM 1909 CD ARG A 249 23.221 -6.535 45.888 1.00 31.66 C ANISOU 1909 CD ARG A 249 3466 6165 2397 -67 -1135 344 C ATOM 1910 NE ARG A 249 24.184 -7.053 44.938 1.00 30.74 N ANISOU 1910 NE ARG A 249 3352 5507 2819 243 -1015 732 N ATOM 1911 CZ ARG A 249 24.686 -6.430 43.886 1.00 26.82 C ANISOU 1911 CZ ARG A 249 3159 4441 2590 542 -1067 360 C ATOM 1912 NH1 ARG A 249 24.380 -5.194 43.510 1.00 25.24 N ANISOU 1912 NH1 ARG A 249 2862 4280 2449 600 -1528 -86 N ATOM 1913 NH2 ARG A 249 25.567 -7.128 43.160 1.00 26.22 N ANISOU 1913 NH2 ARG A 249 2760 3647 3556 96 -789 361 N ATOM 1914 N LEU A 250 18.643 -7.044 42.168 1.00 20.17 N ANISOU 1914 N LEU A 250 2632 2912 2120 175 -693 82 N ATOM 1915 CA LEU A 250 17.747 -6.478 41.160 1.00 18.55 C ANISOU 1915 CA LEU A 250 2475 2672 1902 290 -474 -3 C ATOM 1916 C LEU A 250 16.670 -7.484 40.830 1.00 17.44 C ANISOU 1916 C LEU A 250 2499 2441 1687 375 -434 -19 C ATOM 1917 O LEU A 250 16.961 -8.654 40.618 1.00 21.26 O ANISOU 1917 O LEU A 250 3082 2409 2585 396 -89 -43 O ATOM 1918 CB LEU A 250 18.505 -6.106 39.884 1.00 19.17 C ANISOU 1918 CB LEU A 250 2077 3074 2134 458 -424 118 C ATOM 1919 CG LEU A 250 17.697 -5.487 38.742 1.00 16.37 C ANISOU 1919 CG LEU A 250 2007 2457 1756 229 -385 -144 C ATOM 1920 CD1 LEU A 250 17.135 -4.153 39.181 1.00 19.97 C ANISOU 1920 CD1 LEU A 250 3044 2373 2170 487 171 294 C ATOM 1921 CD2 LEU A 250 18.539 -5.393 37.475 1.00 19.49 C ANISOU 1921 CD2 LEU A 250 2605 2465 2335 310 191 264 C ATOM 1922 N GLY A 251 15.417 -7.096 40.720 1.00 18.13 N ANISOU 1922 N GLY A 251 2459 2402 2029 193 -474 426 N ATOM 1923 CA GLY A 251 14.321 -7.994 40.506 1.00 17.48 C ANISOU 1923 CA GLY A 251 2524 2464 1652 184 -408 240 C ATOM 1924 C GLY A 251 14.260 -8.669 39.156 1.00 18.97 C ANISOU 1924 C GLY A 251 3229 2230 1750 80 -66 186 C ATOM 1925 O GLY A 251 13.878 -9.840 39.109 1.00 19.68 O ANISOU 1925 O GLY A 251 3349 2169 1958 32 -3 263 O ATOM 1926 N GLY A 252 14.633 -7.976 38.100 1.00 15.56 N ANISOU 1926 N GLY A 252 2098 2055 1760 228 -100 85 N ATOM 1927 CA GLY A 252 14.606 -8.554 36.769 1.00 16.74 C ANISOU 1927 CA GLY A 252 2305 2321 1732 9 -97 109 C ATOM 1928 C GLY A 252 15.108 -7.598 35.721 1.00 14.75 C ANISOU 1928 C GLY A 252 1777 2062 1765 215 -75 61 C ATOM 1929 O GLY A 252 15.386 -6.455 36.065 1.00 16.46 O ANISOU 1929 O GLY A 252 2133 2147 1973 119 -369 -44 O ATOM 1930 N ALA A 253 15.215 -8.074 34.494 1.00 14.09 N ANISOU 1930 N ALA A 253 1715 1910 1728 139 -128 110 N ATOM 1931 CA ALA A 253 15.725 -7.211 33.427 1.00 13.77 C ANISOU 1931 CA ALA A 253 1630 1847 1754 67 -228 183 C ATOM 1932 C ALA A 253 15.220 -7.713 32.084 1.00 14.12 C ANISOU 1932 C ALA A 253 1901 1732 1731 75 -187 165 C ATOM 1933 O ALA A 253 15.223 -8.898 31.785 1.00 15.23 O ANISOU 1933 O ALA A 253 2009 1748 2029 130 -481 174 O ATOM 1934 CB ALA A 253 17.236 -7.177 33.365 1.00 14.61 C ANISOU 1934 CB ALA A 253 1664 2202 1683 184 67 -180 C ATOM 1935 N GLY A 254 14.824 -6.792 31.220 1.00 13.82 N ANISOU 1935 N GLY A 254 1902 1670 1679 242 -240 -4 N ATOM 1936 CA GLY A 254 14.460 -7.067 29.832 1.00 12.93 C ANISOU 1936 CA GLY A 254 1739 1542 1633 154 -99 -19 C ATOM 1937 C GLY A 254 15.488 -6.314 28.965 1.00 12.65 C ANISOU 1937 C GLY A 254 1516 1471 1821 161 -156 9 C ATOM 1938 O GLY A 254 15.493 -5.084 28.994 1.00 14.41 O ANISOU 1938 O GLY A 254 1938 1474 2061 131 -17 26 O ATOM 1939 N LEU A 255 16.330 -7.046 28.255 1.00 14.02 N ANISOU 1939 N LEU A 255 1575 1686 2066 280 -46 17 N ATOM 1940 CA LEU A 255 17.501 -6.489 27.613 1.00 13.74 C ANISOU 1940 CA LEU A 255 1431 2029 1760 254 -218 -38 C ATOM 1941 C LEU A 255 17.490 -6.798 26.119 1.00 12.81 C ANISOU 1941 C LEU A 255 1482 1548 1836 85 -296 -84 C ATOM 1942 O LEU A 255 17.476 -7.971 25.766 1.00 13.97 O ANISOU 1942 O LEU A 255 1753 1486 2068 136 -97 -37 O ATOM 1943 CB LEU A 255 18.778 -7.035 28.262 1.00 15.08 C ANISOU 1943 CB LEU A 255 1633 2144 1954 144 -313 372 C ATOM 1944 CG LEU A 255 18.882 -6.865 29.789 1.00 14.84 C ANISOU 1944 CG LEU A 255 1797 1857 1986 339 -498 203 C ATOM 1945 CD1 LEU A 255 20.041 -7.673 30.352 1.00 17.15 C ANISOU 1945 CD1 LEU A 255 1665 2617 2233 757 -546 -74 C ATOM 1946 CD2 LEU A 255 18.983 -5.390 30.190 1.00 16.56 C ANISOU 1946 CD2 LEU A 255 1718 1933 2641 84 -549 93 C ATOM 1947 N ASP A 256 17.522 -5.722 25.347 1.00 13.29 N ANISOU 1947 N ASP A 256 1736 1498 1816 173 -165 -39 N ATOM 1948 CA ASP A 256 17.659 -5.848 23.880 1.00 13.34 C ANISOU 1948 CA ASP A 256 1580 1611 1879 197 -183 -77 C ATOM 1949 C ASP A 256 19.105 -5.611 23.410 1.00 13.18 C ANISOU 1949 C ASP A 256 1626 1671 1711 45 -229 55 C ATOM 1950 O ASP A 256 19.431 -5.860 22.240 1.00 15.10 O ANISOU 1950 O ASP A 256 1604 2239 1893 196 -184 -220 O ATOM 1951 CB ASP A 256 16.760 -4.883 23.141 1.00 14.41 C ANISOU 1951 CB ASP A 256 1683 1729 2065 2 -500 86 C ATOM 1952 CG ASP A 256 16.605 -5.117 21.667 1.00 15.22 C ANISOU 1952 CG ASP A 256 1718 1980 2084 -213 -521 73 C ATOM 1953 OD1 ASP A 256 16.359 -6.291 21.322 1.00 14.02 O ANISOU 1953 OD1 ASP A 256 1576 1930 1820 -88 -133 31 O ATOM 1954 OD2 ASP A 256 16.670 -4.128 20.867 1.00 14.72 O ANISOU 1954 OD2 ASP A 256 1692 1938 1964 171 -11 52 O ATOM 1955 N VAL A 257 19.939 -5.084 24.283 1.00 15.05 N ANISOU 1955 N VAL A 257 1578 2195 1947 -14 -264 -94 N ATOM 1956 CA VAL A 257 21.286 -4.622 23.912 1.00 14.99 C ANISOU 1956 CA VAL A 257 1632 2151 1913 -28 -161 -231 C ATOM 1957 C VAL A 257 22.252 -4.978 25.000 1.00 15.22 C ANISOU 1957 C VAL A 257 1398 2285 2098 39 -23 64 C ATOM 1958 O VAL A 257 21.877 -5.151 26.159 1.00 15.87 O ANISOU 1958 O VAL A 257 1707 2315 2008 153 48 138 O ATOM 1959 CB VAL A 257 21.289 -3.096 23.697 1.00 15.64 C ANISOU 1959 CB VAL A 257 1906 2201 1835 -157 -445 -72 C ATOM 1960 CG1 VAL A 257 20.447 -2.754 22.471 1.00 18.19 C ANISOU 1960 CG1 VAL A 257 2130 2516 2265 -380 -839 107 C ATOM 1961 CG2 VAL A 257 20.820 -2.348 24.951 1.00 17.13 C ANISOU 1961 CG2 VAL A 257 2329 1954 2225 11 -324 -215 C ATOM 1962 N PHE A 258 23.507 -5.233 24.582 1.00 15.74 N ANISOU 1962 N PHE A 258 1592 2234 2154 197 95 152 N ATOM 1963 CA PHE A 258 24.544 -5.774 25.468 1.00 15.92 C ANISOU 1963 CA PHE A 258 1545 2226 2280 316 112 208 C ATOM 1964 C PHE A 258 25.870 -5.094 25.156 1.00 15.62 C ANISOU 1964 C PHE A 258 1607 2399 1928 212 -10 187 C ATOM 1965 O PHE A 258 26.105 -4.673 24.038 1.00 17.82 O ANISOU 1965 O PHE A 258 1771 2985 2015 -84 87 194 O ATOM 1966 CB PHE A 258 24.701 -7.304 25.328 1.00 16.06 C ANISOU 1966 CB PHE A 258 1800 2277 2026 278 -83 218 C ATOM 1967 CG PHE A 258 23.380 -7.992 25.600 1.00 16.18 C ANISOU 1967 CG PHE A 258 1965 2194 1989 113 -49 -193 C ATOM 1968 CD1 PHE A 258 23.093 -8.406 26.890 1.00 15.89 C ANISOU 1968 CD1 PHE A 258 1416 2411 2212 460 4 207 C ATOM 1969 CD2 PHE A 258 22.451 -8.184 24.593 1.00 16.00 C ANISOU 1969 CD2 PHE A 258 2110 1983 1989 -20 -1 -367 C ATOM 1970 CE1 PHE A 258 21.845 -8.969 27.167 1.00 16.04 C ANISOU 1970 CE1 PHE A 258 1440 2389 2267 325 -88 -77 C ATOM 1971 CE2 PHE A 258 21.211 -8.703 24.863 1.00 17.01 C ANISOU 1971 CE2 PHE A 258 2065 2020 2379 3 -250 283 C ATOM 1972 CZ PHE A 258 20.922 -9.125 26.179 1.00 15.79 C ANISOU 1972 CZ PHE A 258 1626 2148 2226 315 -180 93 C ATOM 1973 N GLU A 259 26.751 -5.018 26.159 1.00 17.86 N ANISOU 1973 N GLU A 259 1834 2828 2125 170 -145 87 N ATOM 1974 CA GLU A 259 27.941 -4.162 26.058 1.00 21.60 C ANISOU 1974 CA GLU A 259 1603 3454 3148 57 -378 184 C ATOM 1975 C GLU A 259 28.888 -4.596 24.963 1.00 21.89 C ANISOU 1975 C GLU A 259 1308 3190 3820 231 -152 596 C ATOM 1976 O GLU A 259 29.516 -3.754 24.332 1.00 24.55 O ANISOU 1976 O GLU A 259 2900 3626 2803 -513 -153 430 O ATOM 1977 CB GLU A 259 28.588 -4.074 27.448 1.00 27.64 C ANISOU 1977 CB GLU A 259 2342 4767 3393 -698 -984 1016 C ATOM 1978 CG GLU A 259 29.537 -2.944 27.685 1.00 40.45 C ANISOU 1978 CG GLU A 259 4636 6343 4391 -2440 -2533 1708 C ATOM 1979 CD GLU A 259 29.894 -2.496 29.080 1.00 33.29 C ANISOU 1979 CD GLU A 259 2996 5512 4141 -1434 -985 744 C ATOM 1980 OE1 GLU A 259 29.736 -3.322 30.019 1.00 25.03 O ANISOU 1980 OE1 GLU A 259 2406 3636 3466 -136 -67 -405 O ATOM 1981 OE2 GLU A 259 30.370 -1.358 29.348 1.00 30.03 O ANISOU 1981 OE2 GLU A 259 4055 3803 3552 253 1730 -8 O ATOM 1982 N ARG A 260 28.988 -5.900 24.748 1.00 21.08 N ANISOU 1982 N ARG A 260 1847 3277 2887 250 -333 467 N ATOM 1983 CA ARG A 260 29.862 -6.495 23.754 1.00 23.40 C ANISOU 1983 CA ARG A 260 1616 3894 3381 243 -269 87 C ATOM 1984 C ARG A 260 29.037 -7.380 22.822 1.00 21.94 C ANISOU 1984 C ARG A 260 1920 3255 3161 290 -225 307 C ATOM 1985 O ARG A 260 29.448 -8.485 22.462 1.00 24.61 O ANISOU 1985 O ARG A 260 2508 3300 3541 546 -56 373 O ATOM 1986 CB ARG A 260 30.918 -7.338 24.473 1.00 26.30 C ANISOU 1986 CB ARG A 260 1896 4221 3876 636 -499 -301 C ATOM 1987 CG ARG A 260 31.757 -6.604 25.504 1.00 38.11 C ANISOU 1987 CG ARG A 260 2572 5993 5914 51 -2087 -335 C ATOM 1988 CD ARG A 260 32.788 -7.445 26.224 1.00 47.10 C ANISOU 1988 CD ARG A 260 3770 6872 7255 1042 -3022 -732 C ATOM 1989 NE ARG A 260 33.626 -8.246 25.366 1.00 57.84 N ANISOU 1989 NE ARG A 260 4541 8435 9001 2190 -1760 -387 N ATOM 1990 CZ ARG A 260 34.785 -8.811 25.565 1.00 63.52 C ANISOU 1990 CZ ARG A 260 6244 8402 9487 3545 -2347 293 C ATOM 1991 NH1 ARG A 260 35.371 -8.665 26.752 1.00 80.98 N ANISOU 1991 NH1 ARG A 260 7815 11952 11002 1673 -4409 1386 N ATOM 1992 NH2 ARG A 260 35.349 -9.508 24.583 1.00 79.80 N ANISOU 1992 NH2 ARG A 260 7790 9876 12654 4238 92 -442 N ATOM 1993 N GLU A 261 27.862 -6.949 22.407 1.00 21.78 N ANISOU 1993 N GLU A 261 1656 3288 3332 159 -128 187 N ATOM 1994 CA GLU A 261 27.013 -7.776 21.561 1.00 21.77 C ANISOU 1994 CA GLU A 261 2156 3204 2910 245 -379 395 C ATOM 1995 C GLU A 261 27.755 -8.138 20.281 1.00 24.05 C ANISOU 1995 C GLU A 261 2417 3723 2998 -437 42 398 C ATOM 1996 O GLU A 261 28.550 -7.343 19.791 1.00 26.99 O ANISOU 1996 O GLU A 261 2443 4016 3796 -385 -102 1160 O ATOM 1997 CB GLU A 261 25.682 -7.046 21.375 1.00 24.58 C ANISOU 1997 CB GLU A 261 2246 2877 4215 149 -946 -221 C ATOM 1998 CG GLU A 261 25.733 -5.670 20.809 1.00 22.56 C ANISOU 1998 CG GLU A 261 2496 2837 3241 492 -685 -500 C ATOM 1999 CD GLU A 261 24.353 -5.062 20.632 1.00 18.78 C ANISOU 1999 CD GLU A 261 2195 2624 2317 78 -448 -420 C ATOM 2000 OE1 GLU A 261 23.674 -4.760 21.628 1.00 18.37 O ANISOU 2000 OE1 GLU A 261 2153 2811 2017 5 -460 -40 O ATOM 2001 OE2 GLU A 261 24.012 -4.911 19.447 1.00 19.62 O ANISOU 2001 OE2 GLU A 261 1971 3325 2160 173 48 39 O ATOM 2002 N PRO A 262 27.556 -9.318 19.695 1.00 22.93 N ANISOU 2002 N PRO A 262 1491 3629 3591 354 182 101 N ATOM 2003 CA PRO A 262 26.522 -10.259 20.145 1.00 22.48 C ANISOU 2003 CA PRO A 262 2066 3099 3376 278 451 -168 C ATOM 2004 C PRO A 262 26.914 -11.200 21.268 1.00 23.82 C ANISOU 2004 C PRO A 262 2420 3361 3269 717 606 -125 C ATOM 2005 O PRO A 262 26.200 -12.175 21.475 1.00 22.92 O ANISOU 2005 O PRO A 262 2287 3349 3072 795 203 50 O ATOM 2006 CB PRO A 262 26.285 -11.121 18.879 1.00 24.98 C ANISOU 2006 CB PRO A 262 2177 4175 3138 -180 859 -378 C ATOM 2007 CG PRO A 262 27.698 -11.212 18.348 1.00 26.20 C ANISOU 2007 CG PRO A 262 2018 4745 3193 -244 635 -553 C ATOM 2008 CD PRO A 262 28.281 -9.816 18.503 1.00 25.77 C ANISOU 2008 CD PRO A 262 1657 4742 3391 -176 188 -176 C ATOM 2009 N GLU A 263 27.998 -10.939 21.990 1.00 23.52 N ANISOU 2009 N GLU A 263 2530 3293 3114 462 665 120 N ATOM 2010 CA GLU A 263 28.274 -11.688 23.204 1.00 24.27 C ANISOU 2010 CA GLU A 263 2681 3108 3431 619 464 216 C ATOM 2011 C GLU A 263 27.309 -11.203 24.294 1.00 22.60 C ANISOU 2011 C GLU A 263 2928 2821 2838 239 259 9 C ATOM 2012 O GLU A 263 27.137 -9.995 24.444 1.00 24.65 O ANISOU 2012 O GLU A 263 3336 2793 3237 -74 458 -315 O ATOM 2013 CB GLU A 263 29.711 -11.508 23.682 1.00 37.31 C ANISOU 2013 CB GLU A 263 2643 5816 5717 1111 -233 1153 C ATOM 2014 CG GLU A 263 30.613 -12.672 23.296 1.00 55.59 C ANISOU 2014 CG GLU A 263 3442 7843 9836 2487 282 340 C ATOM 2015 CD GLU A 263 32.036 -12.198 23.058 1.00 62.03 C ANISOU 2015 CD GLU A 263 3720 8436 11413 2087 1124 -1178 C ATOM 2016 OE1 GLU A 263 32.496 -11.254 23.745 1.00 79.84 O ANISOU 2016 OE1 GLU A 263 6244 9943 14150 304 287 -2074 O ATOM 2017 OE2 GLU A 263 32.671 -12.794 22.161 1.00 82.61 O ANISOU 2017 OE2 GLU A 263 6542 9725 15120 2317 4460 -1703 O ATOM 2018 N VAL A 264 26.676 -12.132 24.983 1.00 22.23 N ANISOU 2018 N VAL A 264 2849 2711 2885 389 201 -2 N ATOM 2019 CA VAL A 264 25.759 -12.038 26.083 1.00 19.29 C ANISOU 2019 CA VAL A 264 2447 2364 2517 323 -117 43 C ATOM 2020 C VAL A 264 26.342 -12.913 27.211 1.00 20.34 C ANISOU 2020 C VAL A 264 2243 2696 2792 625 -391 32 C ATOM 2021 O VAL A 264 26.633 -14.087 26.978 1.00 21.97 O ANISOU 2021 O VAL A 264 2353 2712 3284 792 149 215 O ATOM 2022 CB VAL A 264 24.349 -12.515 25.739 1.00 18.70 C ANISOU 2022 CB VAL A 264 2568 2622 1913 433 -373 -33 C ATOM 2023 CG1 VAL A 264 23.523 -12.448 27.021 1.00 20.05 C ANISOU 2023 CG1 VAL A 264 2855 2215 2547 64 267 429 C ATOM 2024 CG2 VAL A 264 23.754 -11.702 24.607 1.00 20.14 C ANISOU 2024 CG2 VAL A 264 2563 2813 2274 866 43 290 C ATOM 2025 N PRO A 265 26.559 -12.366 28.397 1.00 20.82 N ANISOU 2025 N PRO A 265 2231 3068 2612 315 -172 127 N ATOM 2026 CA PRO A 265 27.074 -13.189 29.490 1.00 20.58 C ANISOU 2026 CA PRO A 265 2038 3279 2501 341 50 121 C ATOM 2027 C PRO A 265 26.186 -14.405 29.715 1.00 20.05 C ANISOU 2027 C PRO A 265 1973 3025 2617 512 -226 152 C ATOM 2028 O PRO A 265 24.990 -14.318 29.959 1.00 19.04 O ANISOU 2028 O PRO A 265 2075 2779 2382 485 53 286 O ATOM 2029 CB PRO A 265 27.008 -12.241 30.691 1.00 23.73 C ANISOU 2029 CB PRO A 265 3205 3367 2445 -226 93 107 C ATOM 2030 CG PRO A 265 27.163 -10.889 30.085 1.00 24.20 C ANISOU 2030 CG PRO A 265 3509 3271 2416 178 -323 157 C ATOM 2031 CD PRO A 265 26.401 -10.951 28.786 1.00 22.95 C ANISOU 2031 CD PRO A 265 3030 2915 2775 -245 -446 -26 C ATOM 2032 N GLU A 266 26.843 -15.574 29.644 1.00 22.61 N ANISOU 2032 N GLU A 266 1995 3221 3376 714 -125 551 N ATOM 2033 CA GLU A 266 26.128 -16.843 29.690 1.00 21.39 C ANISOU 2033 CA GLU A 266 2124 3056 2949 762 -220 250 C ATOM 2034 C GLU A 266 25.473 -17.113 31.045 1.00 20.28 C ANISOU 2034 C GLU A 266 2490 2298 2917 850 -241 321 C ATOM 2035 O GLU A 266 24.524 -17.899 31.101 1.00 21.59 O ANISOU 2035 O GLU A 266 2358 3048 2799 609 -171 123 O ATOM 2036 CB GLU A 266 27.074 -17.992 29.247 1.00 27.71 C ANISOU 2036 CB GLU A 266 3390 3444 3694 1379 477 371 C ATOM 2037 CG GLU A 266 27.498 -17.842 27.792 1.00 31.28 C ANISOU 2037 CG GLU A 266 3769 4622 3495 1695 368 -16 C ATOM 2038 CD GLU A 266 28.049 -19.099 27.172 1.00 36.85 C ANISOU 2038 CD GLU A 266 6325 4147 3528 1330 336 -369 C ATOM 2039 OE1 GLU A 266 28.076 -20.147 27.860 1.00 45.36 O ANISOU 2039 OE1 GLU A 266 7297 4309 5630 1462 1054 450 O ATOM 2040 OE2 GLU A 266 28.460 -19.054 25.990 1.00 42.98 O ANISOU 2040 OE2 GLU A 266 7191 5446 3695 2247 743 -578 O ATOM 2041 N LYS A 267 25.947 -16.461 32.092 1.00 21.41 N ANISOU 2041 N LYS A 267 2535 2591 3008 620 -69 138 N ATOM 2042 CA LYS A 267 25.325 -16.618 33.401 1.00 20.87 C ANISOU 2042 CA LYS A 267 2261 2926 2741 597 -554 561 C ATOM 2043 C LYS A 267 23.878 -16.167 33.300 1.00 20.39 C ANISOU 2043 C LYS A 267 2202 2822 2724 577 -362 735 C ATOM 2044 O LYS A 267 23.023 -16.728 33.987 1.00 24.09 O ANISOU 2044 O LYS A 267 2609 3137 3409 758 177 1089 O ATOM 2045 CB LYS A 267 26.099 -15.874 34.498 1.00 21.96 C ANISOU 2045 CB LYS A 267 2246 3098 2998 471 -370 195 C ATOM 2046 CG LYS A 267 25.518 -16.068 35.884 1.00 24.82 C ANISOU 2046 CG LYS A 267 3064 3609 2759 817 -517 430 C ATOM 2047 CD LYS A 267 25.706 -17.454 36.472 1.00 25.29 C ANISOU 2047 CD LYS A 267 3085 3578 2946 782 -411 451 C ATOM 2048 CE LYS A 267 25.223 -17.539 37.908 1.00 28.47 C ANISOU 2048 CE LYS A 267 4299 3508 3009 665 -98 454 C ATOM 2049 NZ LYS A 267 25.390 -18.869 38.589 1.00 29.62 N ANISOU 2049 NZ LYS A 267 3547 4137 3571 817 -305 1086 N ATOM 2050 N LEU A 268 23.575 -15.217 32.409 1.00 17.72 N ANISOU 2050 N LEU A 268 1908 2732 2095 580 -201 316 N ATOM 2051 CA LEU A 268 22.205 -14.741 32.290 1.00 17.92 C ANISOU 2051 CA LEU A 268 2011 2507 2290 510 -538 239 C ATOM 2052 C LEU A 268 21.276 -15.815 31.744 1.00 16.71 C ANISOU 2052 C LEU A 268 1909 2225 2216 580 -234 186 C ATOM 2053 O LEU A 268 20.078 -15.731 31.998 1.00 18.42 O ANISOU 2053 O LEU A 268 1974 2324 2701 436 -4 209 O ATOM 2054 CB LEU A 268 22.176 -13.515 31.370 1.00 17.59 C ANISOU 2054 CB LEU A 268 1830 2297 2556 576 16 242 C ATOM 2055 CG LEU A 268 22.822 -12.247 31.915 1.00 18.23 C ANISOU 2055 CG LEU A 268 2180 2549 2198 433 -131 155 C ATOM 2056 CD1 LEU A 268 22.874 -11.214 30.814 1.00 22.39 C ANISOU 2056 CD1 LEU A 268 3424 2497 2585 -13 -582 352 C ATOM 2057 CD2 LEU A 268 22.116 -11.728 33.161 1.00 19.98 C ANISOU 2057 CD2 LEU A 268 1837 2722 3032 399 301 -208 C ATOM 2058 N PHE A 269 21.816 -16.793 31.024 1.00 18.76 N ANISOU 2058 N PHE A 269 2428 2246 2454 610 78 224 N ATOM 2059 CA PHE A 269 20.958 -17.769 30.331 1.00 19.48 C ANISOU 2059 CA PHE A 269 2554 1852 2994 755 5 70 C ATOM 2060 C PHE A 269 20.210 -18.632 31.310 1.00 19.39 C ANISOU 2060 C PHE A 269 1979 2159 3230 818 -94 303 C ATOM 2061 O PHE A 269 19.152 -19.163 31.013 1.00 21.56 O ANISOU 2061 O PHE A 269 2196 2565 3432 622 -323 286 O ATOM 2062 CB PHE A 269 21.786 -18.660 29.403 1.00 18.46 C ANISOU 2062 CB PHE A 269 2214 2265 2536 916 -382 171 C ATOM 2063 CG PHE A 269 22.467 -17.961 28.242 1.00 20.12 C ANISOU 2063 CG PHE A 269 2473 2270 2901 357 -84 -7 C ATOM 2064 CD1 PHE A 269 22.205 -16.634 27.912 1.00 19.13 C ANISOU 2064 CD1 PHE A 269 2293 2216 2762 79 -151 -11 C ATOM 2065 CD2 PHE A 269 23.373 -18.682 27.498 1.00 21.73 C ANISOU 2065 CD2 PHE A 269 2220 2641 3394 480 125 146 C ATOM 2066 CE1 PHE A 269 22.850 -16.038 26.847 1.00 18.40 C ANISOU 2066 CE1 PHE A 269 1843 2531 2618 306 -266 120 C ATOM 2067 CE2 PHE A 269 24.037 -18.089 26.440 1.00 22.03 C ANISOU 2067 CE2 PHE A 269 2475 2771 3123 660 43 209 C ATOM 2068 CZ PHE A 269 23.781 -16.777 26.142 1.00 20.40 C ANISOU 2068 CZ PHE A 269 2073 2568 3112 298 -54 -15 C ATOM 2069 N GLY A 270 20.747 -18.804 32.522 1.00 20.64 N ANISOU 2069 N GLY A 270 1934 2693 3214 287 -37 429 N ATOM 2070 CA GLY A 270 20.051 -19.569 33.513 1.00 20.08 C ANISOU 2070 CA GLY A 270 2074 1946 3610 794 57 704 C ATOM 2071 C GLY A 270 19.030 -18.854 34.351 1.00 18.70 C ANISOU 2071 C GLY A 270 1808 1950 3346 429 -62 485 C ATOM 2072 O GLY A 270 18.442 -19.491 35.253 1.00 21.67 O ANISOU 2072 O GLY A 270 2622 2570 3043 346 9 613 O ATOM 2073 N LEU A 271 18.804 -17.564 34.123 1.00 18.85 N ANISOU 2073 N LEU A 271 2307 2126 2728 921 -368 401 N ATOM 2074 CA LEU A 271 17.933 -16.794 34.979 1.00 17.36 C ANISOU 2074 CA LEU A 271 2042 2041 2512 618 -145 591 C ATOM 2075 C LEU A 271 16.534 -16.638 34.404 1.00 16.38 C ANISOU 2075 C LEU A 271 2061 1816 2348 494 -110 584 C ATOM 2076 O LEU A 271 16.331 -16.187 33.278 1.00 17.07 O ANISOU 2076 O LEU A 271 2221 1920 2345 345 -204 515 O ATOM 2077 CB LEU A 271 18.550 -15.418 35.190 1.00 19.01 C ANISOU 2077 CB LEU A 271 2272 2450 2500 246 33 62 C ATOM 2078 CG LEU A 271 19.964 -15.345 35.738 1.00 18.80 C ANISOU 2078 CG LEU A 271 2539 2327 2278 267 -220 359 C ATOM 2079 CD1 LEU A 271 20.359 -13.899 35.984 1.00 22.51 C ANISOU 2079 CD1 LEU A 271 2567 2329 3659 138 -566 432 C ATOM 2080 CD2 LEU A 271 20.108 -16.119 37.013 1.00 23.21 C ANISOU 2080 CD2 LEU A 271 3452 2884 2484 253 -190 725 C ATOM 2081 N GLU A 272 15.540 -17.001 35.196 1.00 18.17 N ANISOU 2081 N GLU A 272 2151 2724 2030 62 -56 -66 N ATOM 2082 CA GLU A 272 14.143 -16.897 34.809 1.00 17.36 C ANISOU 2082 CA GLU A 272 2156 2137 2303 -154 -274 -50 C ATOM 2083 C GLU A 272 13.593 -15.468 34.882 1.00 19.11 C ANISOU 2083 C GLU A 272 2427 2316 2518 77 -153 -43 C ATOM 2084 O GLU A 272 12.491 -15.263 34.321 1.00 18.80 O ANISOU 2084 O GLU A 272 2062 2384 2699 -7 103 -50 O ATOM 2085 CB GLU A 272 13.289 -17.811 35.682 1.00 20.81 C ANISOU 2085 CB GLU A 272 2335 2715 2856 -168 -193 488 C ATOM 2086 CG GLU A 272 13.242 -17.464 37.175 1.00 21.69 C ANISOU 2086 CG GLU A 272 2831 2672 2740 589 83 792 C ATOM 2087 CD GLU A 272 12.062 -16.596 37.553 1.00 22.26 C ANISOU 2087 CD GLU A 272 2775 2476 3207 642 -668 208 C ATOM 2088 OE1 GLU A 272 10.951 -16.804 37.002 1.00 22.63 O ANISOU 2088 OE1 GLU A 272 2552 3091 2956 39 -350 897 O ATOM 2089 OE2 GLU A 272 12.300 -15.673 38.368 1.00 24.56 O ANISOU 2089 OE2 GLU A 272 3327 2693 3312 -51 76 12 O ATOM 2090 N ASN A 273 14.316 -14.579 35.560 1.00 16.93 N ANISOU 2090 N ASN A 273 2477 1838 2117 78 -101 334 N ATOM 2091 CA ASN A 273 13.834 -13.201 35.692 1.00 16.58 C ANISOU 2091 CA ASN A 273 2741 1986 1573 305 -160 475 C ATOM 2092 C ASN A 273 14.452 -12.222 34.699 1.00 15.05 C ANISOU 2092 C ASN A 273 2182 1846 1691 251 -124 318 C ATOM 2093 O ASN A 273 14.413 -11.001 34.899 1.00 16.26 O ANISOU 2093 O ASN A 273 2398 1884 1894 188 -18 243 O ATOM 2094 CB ASN A 273 14.015 -12.783 37.159 1.00 17.83 C ANISOU 2094 CB ASN A 273 2842 2289 1646 245 -187 330 C ATOM 2095 CG ASN A 273 15.478 -12.786 37.549 1.00 18.54 C ANISOU 2095 CG ASN A 273 2956 1953 2136 173 -423 -55 C ATOM 2096 OD1 ASN A 273 16.278 -13.550 37.019 1.00 24.06 O ANISOU 2096 OD1 ASN A 273 3254 2869 3018 994 -771 -403 O ATOM 2097 ND2 ASN A 273 15.819 -11.923 38.493 1.00 23.04 N ANISOU 2097 ND2 ASN A 273 4104 2302 2348 -286 -680 -211 N ATOM 2098 N VAL A 274 15.010 -12.756 33.589 1.00 15.17 N ANISOU 2098 N VAL A 274 2077 1986 1700 -60 -220 110 N ATOM 2099 CA VAL A 274 15.479 -11.919 32.488 1.00 13.12 C ANISOU 2099 CA VAL A 274 1432 1974 1577 243 -253 -21 C ATOM 2100 C VAL A 274 14.791 -12.351 31.199 1.00 12.45 C ANISOU 2100 C VAL A 274 1571 1515 1646 432 -320 -175 C ATOM 2101 O VAL A 274 14.408 -13.536 31.041 1.00 14.77 O ANISOU 2101 O VAL A 274 2119 1539 1953 184 0 -184 O ATOM 2102 CB VAL A 274 17.010 -11.938 32.355 1.00 13.95 C ANISOU 2102 CB VAL A 274 1481 1885 1935 345 -383 130 C ATOM 2103 CG1 VAL A 274 17.661 -11.517 33.691 1.00 16.73 C ANISOU 2103 CG1 VAL A 274 1842 2190 2325 -114 -820 186 C ATOM 2104 CG2 VAL A 274 17.537 -13.280 31.909 1.00 15.64 C ANISOU 2104 CG2 VAL A 274 1759 1945 2240 560 -128 215 C ATOM 2105 N VAL A 275 14.707 -11.421 30.263 1.00 14.11 N ANISOU 2105 N VAL A 275 1781 1674 1905 310 -566 31 N ATOM 2106 CA VAL A 275 14.339 -11.660 28.884 1.00 12.80 C ANISOU 2106 CA VAL A 275 1424 1664 1774 262 -243 151 C ATOM 2107 C VAL A 275 15.458 -11.029 28.056 1.00 13.87 C ANISOU 2107 C VAL A 275 1294 1818 2157 153 -180 -50 C ATOM 2108 O VAL A 275 15.798 -9.872 28.301 1.00 15.19 O ANISOU 2108 O VAL A 275 1804 1808 2160 58 93 98 O ATOM 2109 CB VAL A 275 12.927 -11.116 28.524 1.00 12.44 C ANISOU 2109 CB VAL A 275 1341 1766 1617 152 -138 441 C ATOM 2110 CG1 VAL A 275 12.657 -11.276 27.036 1.00 14.56 C ANISOU 2110 CG1 VAL A 275 1915 2015 1603 125 -271 413 C ATOM 2111 CG2 VAL A 275 11.917 -11.816 29.370 1.00 14.00 C ANISOU 2111 CG2 VAL A 275 1616 1720 1982 251 265 390 C ATOM 2112 N LEU A 276 16.034 -11.800 27.154 1.00 14.49 N ANISOU 2112 N LEU A 276 1570 1888 2047 295 -46 104 N ATOM 2113 CA LEU A 276 17.212 -11.443 26.396 1.00 13.63 C ANISOU 2113 CA LEU A 276 1450 1792 1936 210 -200 38 C ATOM 2114 C LEU A 276 16.907 -11.465 24.901 1.00 14.05 C ANISOU 2114 C LEU A 276 1891 1564 1882 128 -167 31 C ATOM 2115 O LEU A 276 16.541 -12.559 24.421 1.00 15.85 O ANISOU 2115 O LEU A 276 2510 1575 1938 55 -206 79 O ATOM 2116 CB LEU A 276 18.309 -12.451 26.707 1.00 14.95 C ANISOU 2116 CB LEU A 276 1703 1972 2006 503 -99 8 C ATOM 2117 CG LEU A 276 18.563 -12.720 28.185 1.00 14.91 C ANISOU 2117 CG LEU A 276 1701 1974 1991 500 -12 131 C ATOM 2118 CD1 LEU A 276 19.533 -13.884 28.348 1.00 17.84 C ANISOU 2118 CD1 LEU A 276 2071 1973 2734 558 -152 436 C ATOM 2119 CD2 LEU A 276 19.090 -11.475 28.895 1.00 17.24 C ANISOU 2119 CD2 LEU A 276 2100 2262 2187 454 -301 -103 C ATOM 2120 N LEU A 277 17.066 -10.366 24.213 1.00 13.13 N ANISOU 2120 N LEU A 277 1713 1425 1851 279 -220 -91 N ATOM 2121 CA LEU A 277 16.771 -10.286 22.783 1.00 13.18 C ANISOU 2121 CA LEU A 277 1476 1670 1864 204 -236 12 C ATOM 2122 C LEU A 277 17.990 -9.838 21.978 1.00 13.57 C ANISOU 2122 C LEU A 277 1402 1709 2044 295 -132 -4 C ATOM 2123 O LEU A 277 18.782 -9.045 22.504 1.00 14.57 O ANISOU 2123 O LEU A 277 1415 2108 2013 137 -167 -29 O ATOM 2124 CB LEU A 277 15.613 -9.326 22.494 1.00 13.26 C ANISOU 2124 CB LEU A 277 1529 1800 1710 447 -25 -182 C ATOM 2125 CG LEU A 277 14.364 -9.567 23.343 1.00 14.44 C ANISOU 2125 CG LEU A 277 1717 1902 1867 381 121 31 C ATOM 2126 CD1 LEU A 277 13.267 -8.562 22.976 1.00 16.40 C ANISOU 2126 CD1 LEU A 277 1591 2521 2118 608 22 157 C ATOM 2127 CD2 LEU A 277 13.815 -10.955 23.193 1.00 16.82 C ANISOU 2127 CD2 LEU A 277 1956 2143 2290 61 296 -342 C ATOM 2128 N PRO A 278 18.139 -10.326 20.741 1.00 14.16 N ANISOU 2128 N PRO A 278 1140 2205 2034 74 -159 -58 N ATOM 2129 CA PRO A 278 19.356 -9.980 19.967 1.00 14.23 C ANISOU 2129 CA PRO A 278 1401 1685 2319 81 75 21 C ATOM 2130 C PRO A 278 19.285 -8.660 19.214 1.00 13.63 C ANISOU 2130 C PRO A 278 1369 1853 1956 524 100 -55 C ATOM 2131 O PRO A 278 19.407 -8.581 17.978 1.00 15.90 O ANISOU 2131 O PRO A 278 2042 2092 1908 384 5 -145 O ATOM 2132 CB PRO A 278 19.460 -11.206 19.069 1.00 15.54 C ANISOU 2132 CB PRO A 278 1581 1823 2502 185 222 -37 C ATOM 2133 CG PRO A 278 18.012 -11.567 18.827 1.00 14.36 C ANISOU 2133 CG PRO A 278 1661 1623 2174 66 193 -32 C ATOM 2134 CD PRO A 278 17.261 -11.272 20.076 1.00 13.21 C ANISOU 2134 CD PRO A 278 1344 2007 1668 57 -188 218 C ATOM 2135 N HIS A 279 19.047 -7.561 19.959 1.00 14.00 N ANISOU 2135 N HIS A 279 1446 1691 2185 436 358 -70 N ATOM 2136 CA HIS A 279 19.019 -6.219 19.405 1.00 13.48 C ANISOU 2136 CA HIS A 279 1712 1719 1692 41 -27 -120 C ATOM 2137 C HIS A 279 18.068 -6.086 18.237 1.00 12.81 C ANISOU 2137 C HIS A 279 1693 1667 1507 -32 90 -323 C ATOM 2138 O HIS A 279 18.413 -5.788 17.094 1.00 15.52 O ANISOU 2138 O HIS A 279 1796 2443 1659 98 151 67 O ATOM 2139 CB HIS A 279 20.426 -5.725 19.035 1.00 15.05 C ANISOU 2139 CB HIS A 279 1787 2120 1810 -121 -199 88 C ATOM 2140 CG HIS A 279 20.487 -4.228 19.032 1.00 14.62 C ANISOU 2140 CG HIS A 279 1570 2152 1835 -90 -3 281 C ATOM 2141 ND1 HIS A 279 21.693 -3.562 19.043 1.00 18.51 N ANISOU 2141 ND1 HIS A 279 1776 2305 2951 -303 134 -218 N ATOM 2142 CD2 HIS A 279 19.565 -3.264 19.030 1.00 16.41 C ANISOU 2142 CD2 HIS A 279 1876 2121 2239 -50 -206 236 C ATOM 2143 CE1 HIS A 279 21.496 -2.264 19.046 1.00 18.71 C ANISOU 2143 CE1 HIS A 279 2149 2277 2681 -346 -5 211 C ATOM 2144 NE2 HIS A 279 20.190 -2.041 19.034 1.00 18.65 N ANISOU 2144 NE2 HIS A 279 2139 2112 2834 -249 80 277 N ATOM 2145 N VAL A 280 16.794 -6.319 18.612 1.00 13.87 N ANISOU 2145 N VAL A 280 1654 2058 1558 166 -4 272 N ATOM 2146 CA VAL A 280 15.732 -6.384 17.617 1.00 13.99 C ANISOU 2146 CA VAL A 280 1652 1997 1665 300 -74 -237 C ATOM 2147 C VAL A 280 14.810 -5.178 17.706 1.00 13.52 C ANISOU 2147 C VAL A 280 1664 1890 1582 181 -30 44 C ATOM 2148 O VAL A 280 13.779 -5.187 17.023 1.00 14.41 O ANISOU 2148 O VAL A 280 1768 1762 1946 259 -140 99 O ATOM 2149 CB VAL A 280 14.921 -7.677 17.716 1.00 14.03 C ANISOU 2149 CB VAL A 280 1807 1900 1626 340 -120 -73 C ATOM 2150 CG1 VAL A 280 15.781 -8.908 17.551 1.00 15.94 C ANISOU 2150 CG1 VAL A 280 1439 1963 2653 183 152 -202 C ATOM 2151 CG2 VAL A 280 14.154 -7.775 19.044 1.00 14.48 C ANISOU 2151 CG2 VAL A 280 1933 1951 1617 317 -105 -111 C ATOM 2152 N GLY A 281 15.137 -4.144 18.456 1.00 14.60 N ANISOU 2152 N GLY A 281 1801 1778 1969 151 96 -81 N ATOM 2153 CA GLY A 281 14.306 -2.958 18.601 1.00 14.40 C ANISOU 2153 CA GLY A 281 1591 2087 1794 376 -110 5 C ATOM 2154 C GLY A 281 13.693 -2.425 17.327 1.00 14.13 C ANISOU 2154 C GLY A 281 1469 2289 1609 126 -49 -42 C ATOM 2155 O GLY A 281 12.502 -2.142 17.289 1.00 15.73 O ANISOU 2155 O GLY A 281 1522 2422 2033 299 38 620 O ATOM 2156 N SER A 282 14.495 -2.282 16.260 1.00 14.23 N ANISOU 2156 N SER A 282 1753 1744 1910 176 206 138 N ATOM 2157 CA SER A 282 13.972 -1.791 14.968 1.00 13.67 C ANISOU 2157 CA SER A 282 1758 1598 1838 47 266 134 C ATOM 2158 C SER A 282 13.773 -2.867 13.935 1.00 12.67 C ANISOU 2158 C SER A 282 1428 1627 1758 130 314 199 C ATOM 2159 O SER A 282 13.496 -2.555 12.774 1.00 14.97 O ANISOU 2159 O SER A 282 1930 2100 1660 -44 270 305 O ATOM 2160 CB SER A 282 14.899 -0.723 14.404 1.00 14.09 C ANISOU 2160 CB SER A 282 1363 2046 1945 -171 -45 230 C ATOM 2161 OG SER A 282 16.207 -1.185 14.210 1.00 15.77 O ANISOU 2161 OG SER A 282 1556 2290 2148 113 63 362 O ATOM 2162 N GLY A 283 13.931 -4.114 14.370 1.00 13.06 N ANISOU 2162 N GLY A 283 1416 1586 1960 250 -64 72 N ATOM 2163 CA GLY A 283 14.053 -5.241 13.486 1.00 14.18 C ANISOU 2163 CA GLY A 283 1490 1742 2157 78 160 -133 C ATOM 2164 C GLY A 283 12.787 -5.851 12.944 1.00 14.06 C ANISOU 2164 C GLY A 283 1346 1636 2360 270 214 -336 C ATOM 2165 O GLY A 283 12.576 -7.062 13.034 1.00 14.99 O ANISOU 2165 O GLY A 283 1750 1736 2208 7 -107 -144 O ATOM 2166 N THR A 284 11.926 -5.032 12.348 1.00 13.56 N ANISOU 2166 N THR A 284 1571 1618 1963 49 113 -205 N ATOM 2167 CA THR A 284 10.732 -5.484 11.673 1.00 13.86 C ANISOU 2167 CA THR A 284 1660 1795 1811 90 24 -99 C ATOM 2168 C THR A 284 10.909 -5.266 10.165 1.00 13.19 C ANISOU 2168 C THR A 284 1778 1360 1874 48 80 -101 C ATOM 2169 O THR A 284 11.677 -4.418 9.727 1.00 15.07 O ANISOU 2169 O THR A 284 1815 1755 2155 -133 -49 227 O ATOM 2170 CB THR A 284 9.451 -4.803 12.149 1.00 13.88 C ANISOU 2170 CB THR A 284 1618 1807 1851 -13 72 -33 C ATOM 2171 OG1 THR A 284 9.473 -3.411 11.834 1.00 14.76 O ANISOU 2171 OG1 THR A 284 1738 1859 2009 166 368 160 O ATOM 2172 CG2 THR A 284 9.272 -4.984 13.648 1.00 14.60 C ANISOU 2172 CG2 THR A 284 1409 2259 1880 173 65 254 C ATOM 2173 N VAL A 285 10.168 -6.086 9.417 1.00 15.18 N ANISOU 2173 N VAL A 285 1854 2107 1809 -261 -36 -152 N ATOM 2174 CA VAL A 285 10.185 -5.947 7.960 1.00 15.80 C ANISOU 2174 CA VAL A 285 1965 2213 1827 263 -125 -34 C ATOM 2175 C VAL A 285 9.853 -4.515 7.591 1.00 16.67 C ANISOU 2175 C VAL A 285 2443 2042 1848 240 -29 -236 C ATOM 2176 O VAL A 285 10.510 -3.905 6.738 1.00 18.03 O ANISOU 2176 O VAL A 285 2476 2316 2059 148 -79 72 O ATOM 2177 CB VAL A 285 9.216 -6.951 7.302 1.00 17.73 C ANISOU 2177 CB VAL A 285 2975 1961 1802 333 -803 -2 C ATOM 2178 CG1 VAL A 285 9.084 -6.635 5.827 1.00 26.89 C ANISOU 2178 CG1 VAL A 285 5271 3275 1673 282 -839 -139 C ATOM 2179 CG2 VAL A 285 9.702 -8.362 7.526 1.00 20.20 C ANISOU 2179 CG2 VAL A 285 3208 2063 2405 605 -65 -303 C ATOM 2180 N GLU A 286 8.800 -3.956 8.206 1.00 16.62 N ANISOU 2180 N GLU A 286 2038 2142 2134 225 -192 -52 N ATOM 2181 CA GLU A 286 8.323 -2.656 7.792 1.00 17.79 C ANISOU 2181 CA GLU A 286 2843 1798 2119 266 -173 -469 C ATOM 2182 C GLU A 286 9.320 -1.542 8.064 1.00 17.02 C ANISOU 2182 C GLU A 286 2356 2086 2023 269 -375 59 C ATOM 2183 O GLU A 286 9.623 -0.706 7.216 1.00 17.57 O ANISOU 2183 O GLU A 286 2145 2711 1820 137 -55 161 O ATOM 2184 CB GLU A 286 6.989 -2.329 8.495 1.00 21.11 C ANISOU 2184 CB GLU A 286 2139 2307 3575 370 -434 -443 C ATOM 2185 CG GLU A 286 5.887 -3.321 8.268 1.00 25.09 C ANISOU 2185 CG GLU A 286 2761 3165 3605 -311 -1195 140 C ATOM 2186 CD GLU A 286 5.733 -4.542 9.151 1.00 22.85 C ANISOU 2186 CD GLU A 286 2399 3928 2355 -718 -273 27 C ATOM 2187 OE1 GLU A 286 6.580 -5.089 9.858 1.00 18.53 O ANISOU 2187 OE1 GLU A 286 2087 3329 1623 -542 362 31 O ATOM 2188 OE2 GLU A 286 4.580 -5.035 9.096 1.00 26.83 O ANISOU 2188 OE2 GLU A 286 2055 4834 3304 -611 204 -218 O ATOM 2189 N THR A 287 9.851 -1.474 9.274 1.00 14.34 N ANISOU 2189 N THR A 287 1700 1888 1859 175 65 105 N ATOM 2190 CA THR A 287 10.766 -0.403 9.669 1.00 14.62 C ANISOU 2190 CA THR A 287 1735 1854 1964 193 117 10 C ATOM 2191 C THR A 287 12.104 -0.539 8.997 1.00 15.99 C ANISOU 2191 C THR A 287 2085 1821 2172 -77 558 -298 C ATOM 2192 O THR A 287 12.666 0.458 8.572 1.00 16.36 O ANISOU 2192 O THR A 287 1849 1920 2446 -14 249 40 O ATOM 2193 CB THR A 287 10.925 -0.366 11.206 1.00 13.72 C ANISOU 2193 CB THR A 287 1669 1676 1869 206 154 86 C ATOM 2194 OG1 THR A 287 9.653 0.061 11.760 1.00 16.25 O ANISOU 2194 OG1 THR A 287 1923 2003 2250 291 317 -320 O ATOM 2195 CG2 THR A 287 12.000 0.608 11.670 1.00 17.00 C ANISOU 2195 CG2 THR A 287 1982 1914 2565 121 -270 -66 C ATOM 2196 N ARG A 288 12.645 -1.748 8.880 1.00 14.80 N ANISOU 2196 N ARG A 288 1932 1900 1793 92 373 1 N ATOM 2197 CA ARG A 288 13.930 -1.842 8.188 1.00 14.79 C ANISOU 2197 CA ARG A 288 1622 2154 1844 38 141 -82 C ATOM 2198 C ARG A 288 13.856 -1.475 6.709 1.00 14.93 C ANISOU 2198 C ARG A 288 1814 2178 1682 -215 257 -338 C ATOM 2199 O ARG A 288 14.809 -0.918 6.163 1.00 15.93 O ANISOU 2199 O ARG A 288 1631 2303 2120 75 196 216 O ATOM 2200 CB ARG A 288 14.479 -3.248 8.344 1.00 16.28 C ANISOU 2200 CB ARG A 288 1879 2215 2092 208 48 -346 C ATOM 2201 CG ARG A 288 14.893 -3.564 9.783 1.00 16.22 C ANISOU 2201 CG ARG A 288 1665 2301 2197 150 196 40 C ATOM 2202 CD ARG A 288 16.128 -2.718 10.115 1.00 17.32 C ANISOU 2202 CD ARG A 288 1893 2036 2653 273 -588 519 C ATOM 2203 NE ARG A 288 16.536 -3.127 11.405 1.00 17.16 N ANISOU 2203 NE ARG A 288 1592 2241 2688 -1 -168 789 N ATOM 2204 CZ ARG A 288 17.200 -4.051 12.030 1.00 15.06 C ANISOU 2204 CZ ARG A 288 2247 1943 1533 39 200 599 C ATOM 2205 NH1 ARG A 288 17.643 -4.964 11.168 1.00 18.71 N ANISOU 2205 NH1 ARG A 288 1840 2999 2269 418 86 -227 N ATOM 2206 NH2 ARG A 288 17.469 -4.205 13.321 1.00 17.56 N ANISOU 2206 NH2 ARG A 288 2192 2762 1718 -145 -6 434 N ATOM 2207 N LYS A 289 12.713 -1.785 6.085 1.00 15.37 N ANISOU 2207 N LYS A 289 1816 2093 1931 -124 0 184 N ATOM 2208 CA LYS A 289 12.580 -1.308 4.703 1.00 15.78 C ANISOU 2208 CA LYS A 289 1837 2146 2011 -30 58 212 C ATOM 2209 C LYS A 289 12.612 0.225 4.608 1.00 15.87 C ANISOU 2209 C LYS A 289 1737 2176 2115 58 88 309 C ATOM 2210 O LYS A 289 13.290 0.805 3.735 1.00 15.92 O ANISOU 2210 O LYS A 289 1784 2198 2069 -93 114 136 O ATOM 2211 CB LYS A 289 11.298 -1.828 4.061 1.00 18.24 C ANISOU 2211 CB LYS A 289 2256 2503 2173 -113 -310 -19 C ATOM 2212 CG LYS A 289 11.144 -1.410 2.621 1.00 23.55 C ANISOU 2212 CG LYS A 289 3690 2659 2600 -646 -963 599 C ATOM 2213 CD LYS A 289 9.932 -1.934 1.928 1.00 26.71 C ANISOU 2213 CD LYS A 289 3892 3128 3129 -258 -1581 309 C ATOM 2214 CE LYS A 289 10.085 -1.919 0.403 1.00 34.20 C ANISOU 2214 CE LYS A 289 5739 4199 3056 -996 -1887 654 C ATOM 2215 NZ LYS A 289 10.427 -0.642 -0.210 1.00 29.92 N ANISOU 2215 NZ LYS A 289 3419 4468 3482 -1074 -1199 621 N ATOM 2216 N VAL A 290 11.872 0.883 5.506 1.00 16.07 N ANISOU 2216 N VAL A 290 1922 2085 2098 -28 209 258 N ATOM 2217 CA VAL A 290 11.855 2.353 5.521 1.00 15.74 C ANISOU 2217 CA VAL A 290 1561 2105 2314 154 139 544 C ATOM 2218 C VAL A 290 13.242 2.911 5.763 1.00 15.00 C ANISOU 2218 C VAL A 290 1680 1949 2069 129 86 299 C ATOM 2219 O VAL A 290 13.716 3.850 5.117 1.00 16.90 O ANISOU 2219 O VAL A 290 1822 2057 2541 -4 81 463 O ATOM 2220 CB VAL A 290 10.847 2.891 6.550 1.00 15.40 C ANISOU 2220 CB VAL A 290 1563 1943 2345 269 48 592 C ATOM 2221 CG1 VAL A 290 10.955 4.382 6.775 1.00 20.00 C ANISOU 2221 CG1 VAL A 290 2732 2051 2817 139 126 235 C ATOM 2222 CG2 VAL A 290 9.437 2.579 6.070 1.00 20.10 C ANISOU 2222 CG2 VAL A 290 1423 2845 3371 92 44 495 C ATOM 2223 N MET A 291 13.936 2.313 6.738 1.00 15.51 N ANISOU 2223 N MET A 291 1606 1993 2295 207 0 249 N ATOM 2224 CA MET A 291 15.299 2.761 7.036 1.00 14.40 C ANISOU 2224 CA MET A 291 1552 1862 2058 -1 242 316 C ATOM 2225 C MET A 291 16.228 2.604 5.829 1.00 15.54 C ANISOU 2225 C MET A 291 1839 2279 1785 -220 125 91 C ATOM 2226 O MET A 291 17.048 3.464 5.500 1.00 15.40 O ANISOU 2226 O MET A 291 1513 2222 2115 39 276 359 O ATOM 2227 CB MET A 291 15.855 1.942 8.204 1.00 14.40 C ANISOU 2227 CB MET A 291 1508 1971 1991 -57 213 327 C ATOM 2228 CG MET A 291 15.224 2.244 9.549 1.00 14.68 C ANISOU 2228 CG MET A 291 1665 1961 1953 -16 98 101 C ATOM 2229 SD MET A 291 15.709 1.106 10.857 1.00 15.99 S ANISOU 2229 SD MET A 291 1822 2251 2002 146 209 243 S ATOM 2230 CE MET A 291 17.485 1.385 10.949 1.00 15.82 C ANISOU 2230 CE MET A 291 1783 2090 2138 343 111 88 C ATOM 2231 N ALA A 292 16.113 1.452 5.140 1.00 15.80 N ANISOU 2231 N ALA A 292 1936 2289 1777 -77 60 145 N ATOM 2232 CA ALA A 292 16.995 1.185 4.022 1.00 15.24 C ANISOU 2232 CA ALA A 292 1860 1987 1943 187 106 229 C ATOM 2233 C ALA A 292 16.721 2.195 2.913 1.00 15.14 C ANISOU 2233 C ALA A 292 1885 1872 1995 350 299 242 C ATOM 2234 O ALA A 292 17.631 2.732 2.266 1.00 16.69 O ANISOU 2234 O ALA A 292 1869 2367 2105 34 43 396 O ATOM 2235 CB ALA A 292 16.777 -0.251 3.536 1.00 16.12 C ANISOU 2235 CB ALA A 292 1968 1977 2180 -169 327 246 C ATOM 2236 N ASP A 293 15.432 2.407 2.648 1.00 15.95 N ANISOU 2236 N ASP A 293 1881 2084 2097 147 160 463 N ATOM 2237 CA ASP A 293 15.054 3.344 1.567 1.00 16.50 C ANISOU 2237 CA ASP A 293 1775 2288 2206 16 76 555 C ATOM 2238 C ASP A 293 15.543 4.752 1.878 1.00 16.89 C ANISOU 2238 C ASP A 293 2006 2016 2396 367 -356 491 C ATOM 2239 O ASP A 293 15.904 5.532 0.968 1.00 18.83 O ANISOU 2239 O ASP A 293 2726 2027 2400 89 -337 505 O ATOM 2240 CB ASP A 293 13.548 3.264 1.315 1.00 17.43 C ANISOU 2240 CB ASP A 293 1864 2904 1855 67 -28 218 C ATOM 2241 CG ASP A 293 13.123 1.985 0.594 1.00 19.94 C ANISOU 2241 CG ASP A 293 2099 3146 2331 -237 16 16 C ATOM 2242 OD1 ASP A 293 13.976 1.343 -0.037 1.00 20.65 O ANISOU 2242 OD1 ASP A 293 2331 3029 2486 16 -249 -200 O ATOM 2243 OD2 ASP A 293 11.919 1.644 0.696 1.00 21.50 O ANISOU 2243 OD2 ASP A 293 2015 3458 2696 -292 -378 453 O ATOM 2244 N LEU A 294 15.567 5.099 3.169 1.00 17.28 N ANISOU 2244 N LEU A 294 2128 1997 2439 194 61 556 N ATOM 2245 CA LEU A 294 16.045 6.415 3.619 1.00 16.97 C ANISOU 2245 CA LEU A 294 2048 2269 2131 210 -290 425 C ATOM 2246 C LEU A 294 17.562 6.522 3.442 1.00 16.23 C ANISOU 2246 C LEU A 294 2104 2190 1872 143 -120 778 C ATOM 2247 O LEU A 294 18.091 7.569 3.031 1.00 17.36 O ANISOU 2247 O LEU A 294 2559 2100 1936 40 17 509 O ATOM 2248 CB LEU A 294 15.628 6.613 5.064 1.00 19.43 C ANISOU 2248 CB LEU A 294 2625 2340 2417 244 357 445 C ATOM 2249 CG LEU A 294 15.806 7.964 5.729 1.00 22.03 C ANISOU 2249 CG LEU A 294 3664 2411 2296 710 117 351 C ATOM 2250 CD1 LEU A 294 15.184 9.067 4.869 1.00 27.78 C ANISOU 2250 CD1 LEU A 294 4300 2654 3599 1353 171 723 C ATOM 2251 CD2 LEU A 294 15.223 8.008 7.141 1.00 24.00 C ANISOU 2251 CD2 LEU A 294 3270 2888 2962 828 884 113 C ATOM 2252 N VAL A 295 18.321 5.462 3.727 1.00 16.52 N ANISOU 2252 N VAL A 295 1801 1842 2632 -100 -306 287 N ATOM 2253 CA VAL A 295 19.739 5.463 3.448 1.00 15.71 C ANISOU 2253 CA VAL A 295 1993 1874 2103 7 88 209 C ATOM 2254 C VAL A 295 19.977 5.695 1.962 1.00 19.01 C ANISOU 2254 C VAL A 295 3380 1690 2152 -449 142 267 C ATOM 2255 O VAL A 295 20.731 6.552 1.494 1.00 17.56 O ANISOU 2255 O VAL A 295 2328 2049 2295 -142 -259 784 O ATOM 2256 CB VAL A 295 20.419 4.164 3.949 1.00 15.24 C ANISOU 2256 CB VAL A 295 1885 1978 1929 85 -46 13 C ATOM 2257 CG1 VAL A 295 21.805 4.054 3.366 1.00 16.83 C ANISOU 2257 CG1 VAL A 295 1864 1996 2536 12 77 -307 C ATOM 2258 CG2 VAL A 295 20.453 4.135 5.478 1.00 17.39 C ANISOU 2258 CG2 VAL A 295 2186 2511 1909 755 -309 -211 C ATOM 2259 N VAL A 296 19.300 4.920 1.128 1.00 16.85 N ANISOU 2259 N VAL A 296 2228 2091 2084 -35 53 249 N ATOM 2260 CA VAL A 296 19.457 5.051 -0.323 1.00 17.71 C ANISOU 2260 CA VAL A 296 2466 2145 2117 61 238 150 C ATOM 2261 C VAL A 296 19.049 6.440 -0.739 1.00 18.69 C ANISOU 2261 C VAL A 296 2690 2293 2117 45 340 397 C ATOM 2262 O VAL A 296 19.740 7.068 -1.543 1.00 20.11 O ANISOU 2262 O VAL A 296 2468 3060 2115 -327 -181 846 O ATOM 2263 CB VAL A 296 18.583 3.974 -1.011 1.00 17.13 C ANISOU 2263 CB VAL A 296 2244 2358 1906 49 96 297 C ATOM 2264 CG1 VAL A 296 18.516 4.276 -2.492 1.00 21.33 C ANISOU 2264 CG1 VAL A 296 2820 3373 1910 -282 143 453 C ATOM 2265 CG2 VAL A 296 19.090 2.557 -0.761 1.00 19.16 C ANISOU 2265 CG2 VAL A 296 2851 2181 2247 -23 79 -14 C ATOM 2266 N GLY A 297 17.919 6.937 -0.205 1.00 19.10 N ANISOU 2266 N GLY A 297 2452 2475 2332 270 -28 370 N ATOM 2267 CA GLY A 297 17.467 8.252 -0.643 1.00 19.70 C ANISOU 2267 CA GLY A 297 2551 2532 2402 140 -263 526 C ATOM 2268 C GLY A 297 18.428 9.367 -0.294 1.00 20.10 C ANISOU 2268 C GLY A 297 2177 2592 2868 106 -422 890 C ATOM 2269 O GLY A 297 18.630 10.316 -1.085 1.00 22.14 O ANISOU 2269 O GLY A 297 3004 2564 2846 62 -509 855 O ATOM 2270 N ASN A 298 19.079 9.285 0.863 1.00 18.63 N ANISOU 2270 N ASN A 298 2290 2240 2548 47 -152 700 N ATOM 2271 CA ASN A 298 20.113 10.263 1.211 1.00 19.43 C ANISOU 2271 CA ASN A 298 2092 2488 2804 73 -163 609 C ATOM 2272 C ASN A 298 21.282 10.182 0.247 1.00 19.22 C ANISOU 2272 C ASN A 298 2094 2327 2882 415 -133 1117 C ATOM 2273 O ASN A 298 21.784 11.219 -0.189 1.00 21.18 O ANISOU 2273 O ASN A 298 3072 2210 2766 77 382 568 O ATOM 2274 CB ASN A 298 20.595 10.058 2.645 1.00 18.76 C ANISOU 2274 CB ASN A 298 2003 2324 2800 365 -173 352 C ATOM 2275 CG ASN A 298 19.667 10.716 3.648 1.00 17.42 C ANISOU 2275 CG ASN A 298 1751 1864 3003 -54 -25 289 C ATOM 2276 OD1 ASN A 298 19.583 11.939 3.749 1.00 20.70 O ANISOU 2276 OD1 ASN A 298 2380 1840 3646 85 35 327 O ATOM 2277 ND2 ASN A 298 18.984 9.885 4.427 1.00 20.77 N ANISOU 2277 ND2 ASN A 298 2521 2237 3136 -7 146 684 N ATOM 2278 N LEU A 299 21.710 8.941 -0.072 1.00 19.81 N ANISOU 2278 N LEU A 299 2179 2268 3080 256 258 1245 N ATOM 2279 CA LEU A 299 22.874 8.818 -0.969 1.00 19.75 C ANISOU 2279 CA LEU A 299 2448 2466 2592 281 214 1046 C ATOM 2280 C LEU A 299 22.557 9.358 -2.372 1.00 22.35 C ANISOU 2280 C LEU A 299 2649 2940 2902 -4 10 1456 C ATOM 2281 O LEU A 299 23.386 10.065 -2.924 1.00 21.71 O ANISOU 2281 O LEU A 299 2703 2824 2720 86 311 1216 O ATOM 2282 CB LEU A 299 23.367 7.393 -1.034 1.00 18.52 C ANISOU 2282 CB LEU A 299 2552 2297 2186 73 28 686 C ATOM 2283 CG LEU A 299 23.963 6.814 0.257 1.00 16.87 C ANISOU 2283 CG LEU A 299 1807 2403 2201 177 299 788 C ATOM 2284 CD1 LEU A 299 24.100 5.306 0.145 1.00 22.04 C ANISOU 2284 CD1 LEU A 299 2843 2340 3192 264 -57 917 C ATOM 2285 CD2 LEU A 299 25.308 7.470 0.594 1.00 19.08 C ANISOU 2285 CD2 LEU A 299 1814 3022 2414 24 360 454 C ATOM 2286 N GLU A 300 21.380 9.009 -2.902 1.00 21.95 N ANISOU 2286 N GLU A 300 2645 2996 2700 87 24 1118 N ATOM 2287 CA GLU A 300 20.967 9.521 -4.217 1.00 23.08 C ANISOU 2287 CA GLU A 300 3001 3274 2494 572 104 833 C ATOM 2288 C GLU A 300 20.850 11.043 -4.240 1.00 25.50 C ANISOU 2288 C GLU A 300 3315 3213 3162 666 -4 1197 C ATOM 2289 O GLU A 300 21.239 11.702 -5.216 1.00 27.46 O ANISOU 2289 O GLU A 300 3218 3689 3526 266 199 1375 O ATOM 2290 CB GLU A 300 19.647 8.881 -4.633 1.00 24.13 C ANISOU 2290 CB GLU A 300 3188 3654 2325 375 -69 1002 C ATOM 2291 CG GLU A 300 19.768 7.399 -4.880 1.00 27.14 C ANISOU 2291 CG GLU A 300 4026 3760 2526 352 -878 548 C ATOM 2292 CD GLU A 300 18.558 6.778 -5.539 1.00 32.85 C ANISOU 2292 CD GLU A 300 4617 4267 3600 431 -1870 426 C ATOM 2293 OE1 GLU A 300 17.427 7.167 -5.172 1.00 39.50 O ANISOU 2293 OE1 GLU A 300 4192 4941 5877 416 -1798 1091 O ATOM 2294 OE2 GLU A 300 18.793 5.903 -6.396 1.00 38.74 O ANISOU 2294 OE2 GLU A 300 6952 4469 3299 -421 -1608 205 O ATOM 2295 N ALA A 301 20.326 11.636 -3.148 1.00 23.51 N ANISOU 2295 N ALA A 301 2976 2640 3316 316 -60 1082 N ATOM 2296 CA ALA A 301 20.255 13.095 -3.089 1.00 24.52 C ANISOU 2296 CA ALA A 301 2667 2632 4019 378 -208 1250 C ATOM 2297 C ALA A 301 21.652 13.682 -3.102 1.00 25.24 C ANISOU 2297 C ALA A 301 2978 3034 3578 -39 -173 1335 C ATOM 2298 O ALA A 301 21.926 14.575 -3.893 1.00 26.91 O ANISOU 2298 O ALA A 301 3481 3192 3551 -6 174 1370 O ATOM 2299 CB ALA A 301 19.501 13.571 -1.860 1.00 26.25 C ANISOU 2299 CB ALA A 301 2721 2625 4628 466 -51 791 C ATOM 2300 N HIS A 302 22.537 13.177 -2.240 1.00 24.47 N ANISOU 2300 N HIS A 302 2802 3260 3236 -291 -170 1132 N ATOM 2301 CA HIS A 302 23.916 13.667 -2.192 1.00 22.13 C ANISOU 2301 CA HIS A 302 2467 2378 3563 283 423 977 C ATOM 2302 C HIS A 302 24.568 13.639 -3.554 1.00 24.31 C ANISOU 2302 C HIS A 302 3119 2800 3318 268 265 1271 C ATOM 2303 O HIS A 302 25.086 14.664 -4.025 1.00 26.38 O ANISOU 2303 O HIS A 302 3692 3064 3268 -74 267 1337 O ATOM 2304 CB HIS A 302 24.743 12.852 -1.168 1.00 20.83 C ANISOU 2304 CB HIS A 302 2471 2650 2795 489 452 421 C ATOM 2305 CG HIS A 302 26.160 13.373 -1.244 1.00 23.88 C ANISOU 2305 CG HIS A 302 2554 3110 3409 264 287 580 C ATOM 2306 ND1 HIS A 302 26.543 14.540 -0.670 1.00 25.67 N ANISOU 2306 ND1 HIS A 302 2980 2994 3781 -137 639 764 N ATOM 2307 CD2 HIS A 302 27.270 12.877 -1.833 1.00 24.00 C ANISOU 2307 CD2 HIS A 302 2209 3721 3188 151 -21 450 C ATOM 2308 CE1 HIS A 302 27.817 14.771 -0.892 1.00 27.07 C ANISOU 2308 CE1 HIS A 302 2851 3125 4310 -4 551 643 C ATOM 2309 NE2 HIS A 302 28.289 13.773 -1.610 1.00 25.56 N ANISOU 2309 NE2 HIS A 302 2924 3336 3452 -337 682 690 N ATOM 2310 N PHE A 303 24.596 12.488 -4.228 1.00 24.52 N ANISOU 2310 N PHE A 303 3790 2948 2579 21 376 1411 N ATOM 2311 CA PHE A 303 25.281 12.373 -5.521 1.00 24.63 C ANISOU 2311 CA PHE A 303 3132 3529 2696 489 360 1627 C ATOM 2312 C PHE A 303 24.544 12.998 -6.678 1.00 29.55 C ANISOU 2312 C PHE A 303 3826 4736 2667 771 254 1802 C ATOM 2313 O PHE A 303 25.086 13.064 -7.790 1.00 34.33 O ANISOU 2313 O PHE A 303 5449 4962 2633 530 598 1910 O ATOM 2314 CB PHE A 303 25.565 10.886 -5.809 1.00 25.83 C ANISOU 2314 CB PHE A 303 3305 3624 2885 219 -100 863 C ATOM 2315 CG PHE A 303 26.613 10.362 -4.811 1.00 25.72 C ANISOU 2315 CG PHE A 303 2979 3373 3423 453 195 1247 C ATOM 2316 CD1 PHE A 303 27.892 10.885 -4.839 1.00 28.28 C ANISOU 2316 CD1 PHE A 303 3505 4466 2774 -467 -311 1404 C ATOM 2317 CD2 PHE A 303 26.328 9.382 -3.893 1.00 26.98 C ANISOU 2317 CD2 PHE A 303 2998 4664 2590 231 493 1394 C ATOM 2318 CE1 PHE A 303 28.882 10.469 -3.978 1.00 26.53 C ANISOU 2318 CE1 PHE A 303 3056 4111 2913 253 229 1242 C ATOM 2319 CE2 PHE A 303 27.298 8.958 -2.987 1.00 26.69 C ANISOU 2319 CE2 PHE A 303 2660 4358 3124 791 728 1474 C ATOM 2320 CZ PHE A 303 28.575 9.513 -3.019 1.00 24.56 C ANISOU 2320 CZ PHE A 303 2853 3492 2985 740 527 1062 C ATOM 2321 N SER A 304 23.322 13.491 -6.463 1.00 32.27 N ANISOU 2321 N SER A 304 4055 4659 3547 1312 -306 1636 N ATOM 2322 CA SER A 304 22.624 14.250 -7.494 1.00 36.52 C ANISOU 2322 CA SER A 304 4689 4832 4354 823 -422 2721 C ATOM 2323 C SER A 304 22.537 15.729 -7.153 1.00 40.58 C ANISOU 2323 C SER A 304 7050 4343 4027 -158 136 3583 C ATOM 2324 O SER A 304 21.912 16.510 -7.879 1.00 39.65 O ANISOU 2324 O SER A 304 6374 4623 4070 597 604 3259 O ATOM 2325 CB SER A 304 21.220 13.667 -7.727 1.00 41.40 C ANISOU 2325 CB SER A 304 5247 5601 4883 568 -1771 2090 C ATOM 2326 OG SER A 304 20.357 13.878 -6.615 1.00 48.21 O ANISOU 2326 OG SER A 304 4271 7445 6604 454 -689 3260 O ATOM 2327 N GLY A 305 23.180 16.179 -6.088 1.00 37.45 N ANISOU 2327 N GLY A 305 5052 4252 4926 326 326 2874 N ATOM 2328 CA GLY A 305 23.313 17.614 -5.815 1.00 38.38 C ANISOU 2328 CA GLY A 305 4758 4245 5581 66 904 2937 C ATOM 2329 C GLY A 305 22.063 18.189 -5.173 1.00 39.31 C ANISOU 2329 C GLY A 305 4960 4154 5821 450 976 3305 C ATOM 2330 O GLY A 305 21.939 19.428 -5.176 1.00 37.05 O ANISOU 2330 O GLY A 305 4299 4126 5653 35 4 2778 O ATOM 2331 N LYS A 306 21.225 17.279 -4.665 1.00 38.30 N ANISOU 2331 N LYS A 306 5120 3958 5473 164 1348 2309 N ATOM 2332 CA LYS A 306 19.986 17.685 -4.003 1.00 35.04 C ANISOU 2332 CA LYS A 306 4918 3424 4971 386 855 2420 C ATOM 2333 C LYS A 306 20.161 17.737 -2.489 1.00 32.70 C ANISOU 2333 C LYS A 306 4282 3079 5063 801 576 2448 C ATOM 2334 O LYS A 306 21.043 17.101 -1.920 1.00 33.51 O ANISOU 2334 O LYS A 306 3790 3063 5880 438 394 2617 O ATOM 2335 CB LYS A 306 18.872 16.719 -4.423 1.00 38.59 C ANISOU 2335 CB LYS A 306 4535 4263 5864 642 -323 2528 C ATOM 2336 CG LYS A 306 18.919 16.502 -5.934 1.00 43.86 C ANISOU 2336 CG LYS A 306 5903 4975 5789 1254 -1466 2630 C ATOM 2337 CD LYS A 306 17.568 16.133 -6.477 1.00 52.67 C ANISOU 2337 CD LYS A 306 6657 6047 7309 71 -1897 2159 C ATOM 2338 CE LYS A 306 16.901 14.983 -5.741 1.00 57.52 C ANISOU 2338 CE LYS A 306 6943 6535 8377 -128 -3022 3398 C ATOM 2339 NZ LYS A 306 15.583 14.612 -6.366 1.00 74.61 N ANISOU 2339 NZ LYS A 306 10564 8607 9178 -3584 -5343 3720 N ATOM 2340 N PRO A 307 19.343 18.514 -1.802 1.00 32.91 N ANISOU 2340 N PRO A 307 4555 2864 5087 835 -126 1722 N ATOM 2341 CA PRO A 307 19.429 18.567 -0.349 1.00 33.01 C ANISOU 2341 CA PRO A 307 4351 3141 5052 365 29 1840 C ATOM 2342 C PRO A 307 19.220 17.187 0.247 1.00 32.29 C ANISOU 2342 C PRO A 307 4648 2791 4830 492 32 1461 C ATOM 2343 O PRO A 307 18.418 16.390 -0.266 1.00 29.20 O ANISOU 2343 O PRO A 307 3397 2973 4722 793 394 1513 O ATOM 2344 CB PRO A 307 18.258 19.462 0.051 1.00 35.33 C ANISOU 2344 CB PRO A 307 5197 2581 5647 371 709 1670 C ATOM 2345 CG PRO A 307 17.943 20.262 -1.163 1.00 35.77 C ANISOU 2345 CG PRO A 307 4957 2924 5709 867 111 1422 C ATOM 2346 CD PRO A 307 18.304 19.416 -2.348 1.00 34.01 C ANISOU 2346 CD PRO A 307 4491 2830 5601 825 -754 1158 C ATOM 2347 N LEU A 308 19.952 16.954 1.332 1.00 27.39 N ANISOU 2347 N LEU A 308 3331 2326 4748 598 552 1330 N ATOM 2348 CA LEU A 308 19.855 15.626 1.954 1.00 25.21 C ANISOU 2348 CA LEU A 308 2914 2352 4313 41 265 1155 C ATOM 2349 C LEU A 308 18.519 15.460 2.649 1.00 25.40 C ANISOU 2349 C LEU A 308 2696 2326 4629 522 225 1210 C ATOM 2350 O LEU A 308 17.873 16.455 2.930 1.00 30.93 O ANISOU 2350 O LEU A 308 3606 2602 5545 855 665 1211 O ATOM 2351 CB LEU A 308 21.030 15.384 2.910 1.00 26.05 C ANISOU 2351 CB LEU A 308 2666 2712 4520 258 398 1344 C ATOM 2352 CG LEU A 308 22.422 15.479 2.258 1.00 24.47 C ANISOU 2352 CG LEU A 308 2841 2552 3906 42 446 738 C ATOM 2353 CD1 LEU A 308 23.522 15.115 3.265 1.00 26.22 C ANISOU 2353 CD1 LEU A 308 2730 3320 3912 639 554 490 C ATOM 2354 CD2 LEU A 308 22.515 14.632 0.987 1.00 27.10 C ANISOU 2354 CD2 LEU A 308 4025 2389 3881 -401 440 751 C ATOM 2355 N LEU A 309 18.133 14.214 2.920 1.00 24.80 N ANISOU 2355 N LEU A 309 3089 2552 3783 439 712 1543 N ATOM 2356 CA LEU A 309 16.839 13.986 3.543 1.00 23.10 C ANISOU 2356 CA LEU A 309 2794 2255 3730 642 679 597 C ATOM 2357 C LEU A 309 16.866 14.123 5.057 1.00 23.95 C ANISOU 2357 C LEU A 309 2606 2757 3737 419 597 441 C ATOM 2358 O LEU A 309 16.010 14.802 5.660 1.00 24.07 O ANISOU 2358 O LEU A 309 2799 2755 3590 622 336 322 O ATOM 2359 CB LEU A 309 16.364 12.586 3.114 1.00 23.91 C ANISOU 2359 CB LEU A 309 2752 2447 3886 525 541 464 C ATOM 2360 CG LEU A 309 16.261 12.368 1.603 1.00 27.52 C ANISOU 2360 CG LEU A 309 3107 3357 3993 261 -836 639 C ATOM 2361 CD1 LEU A 309 15.602 11.013 1.276 1.00 26.11 C ANISOU 2361 CD1 LEU A 309 2510 3921 3491 -336 -171 822 C ATOM 2362 CD2 LEU A 309 15.512 13.517 0.956 1.00 40.04 C ANISOU 2362 CD2 LEU A 309 5158 4018 6038 721 -2421 990 C ATOM 2363 N THR A 310 17.854 13.460 5.645 1.00 22.98 N ANISOU 2363 N THR A 310 2831 2295 3606 476 624 292 N ATOM 2364 CA THR A 310 17.998 13.442 7.090 1.00 21.63 C ANISOU 2364 CA THR A 310 2400 2220 3597 328 741 357 C ATOM 2365 C THR A 310 19.439 13.677 7.515 1.00 22.55 C ANISOU 2365 C THR A 310 2452 1955 4162 404 482 382 C ATOM 2366 O THR A 310 20.068 12.865 8.165 1.00 20.73 O ANISOU 2366 O THR A 310 2710 2024 3141 350 493 66 O ATOM 2367 CB THR A 310 17.450 12.130 7.665 1.00 22.41 C ANISOU 2367 CB THR A 310 2682 2142 3689 214 692 223 C ATOM 2368 OG1 THR A 310 17.988 11.042 6.923 1.00 21.34 O ANISOU 2368 OG1 THR A 310 3216 2185 2706 400 211 328 O ATOM 2369 CG2 THR A 310 15.931 12.077 7.499 1.00 29.02 C ANISOU 2369 CG2 THR A 310 2543 4348 4137 -225 1500 527 C ATOM 2370 N PRO A 311 19.965 14.863 7.198 1.00 23.41 N ANISOU 2370 N PRO A 311 2672 2162 4063 180 574 477 N ATOM 2371 CA PRO A 311 21.323 15.183 7.637 1.00 24.94 C ANISOU 2371 CA PRO A 311 2952 2566 3959 -130 536 -57 C ATOM 2372 C PRO A 311 21.435 15.445 9.139 1.00 23.89 C ANISOU 2372 C PRO A 311 3434 1572 4072 581 532 -460 C ATOM 2373 O PRO A 311 20.484 15.916 9.776 1.00 27.85 O ANISOU 2373 O PRO A 311 3004 2960 4616 441 308 -1150 O ATOM 2374 CB PRO A 311 21.652 16.479 6.881 1.00 29.28 C ANISOU 2374 CB PRO A 311 3746 2886 4492 -807 534 162 C ATOM 2375 CG PRO A 311 20.323 17.117 6.629 1.00 27.21 C ANISOU 2375 CG PRO A 311 4338 2031 3968 -324 647 -7 C ATOM 2376 CD PRO A 311 19.336 15.976 6.449 1.00 23.98 C ANISOU 2376 CD PRO A 311 3410 1842 3859 153 532 276 C ATOM 2377 N VAL A 312 22.623 15.129 9.640 1.00 23.85 N ANISOU 2377 N VAL A 312 3056 2300 3707 294 742 -703 N ATOM 2378 CA VAL A 312 23.010 15.517 10.977 1.00 25.11 C ANISOU 2378 CA VAL A 312 3104 2808 3629 106 913 -603 C ATOM 2379 C VAL A 312 24.207 16.462 10.963 1.00 26.84 C ANISOU 2379 C VAL A 312 3325 3000 3873 -145 658 -688 C ATOM 2380 O VAL A 312 24.235 17.401 11.793 1.00 30.46 O ANISOU 2380 O VAL A 312 3868 2729 4976 114 718 -1031 O ATOM 2381 CB VAL A 312 23.303 14.283 11.844 1.00 29.45 C ANISOU 2381 CB VAL A 312 3610 3214 4366 -269 -29 -102 C ATOM 2382 CG1 VAL A 312 23.960 14.675 13.153 1.00 31.52 C ANISOU 2382 CG1 VAL A 312 4729 3352 3895 -680 306 -144 C ATOM 2383 CG2 VAL A 312 21.979 13.530 12.057 1.00 32.94 C ANISOU 2383 CG2 VAL A 312 3279 2407 6828 230 -408 737 C ATOM 2384 N VAL A 313 25.141 16.241 10.064 1.00 28.87 N ANISOU 2384 N VAL A 313 2985 3063 4920 -143 948 -873 N ATOM 2385 CA VAL A 313 26.330 17.048 9.799 1.00 30.08 C ANISOU 2385 CA VAL A 313 3544 3068 4818 -550 941 -938 C ATOM 2386 C VAL A 313 26.483 17.357 8.321 1.00 31.04 C ANISOU 2386 C VAL A 313 4466 2291 5036 -873 374 -201 C ATOM 2387 O VAL A 313 27.028 18.432 8.034 1.00 61.71 O ANISOU 2387 O VAL A 313 13704 3404 6341 -4298 318 2 O ATOM 2388 CB VAL A 313 27.634 16.335 10.246 1.00 35.75 C ANISOU 2388 CB VAL A 313 3217 4815 5551 -1461 -358 50 C ATOM 2389 CG1 VAL A 313 28.849 17.035 9.666 1.00 45.05 C ANISOU 2389 CG1 VAL A 313 3495 6372 7249 -1484 342 863 C ATOM 2390 CG2 VAL A 313 27.634 16.271 11.761 1.00 46.23 C ANISOU 2390 CG2 VAL A 313 5174 6803 5590 -3458 -987 397 C ATOM 2391 OXT VAL A 313 26.088 16.551 7.461 1.00 25.01 O ANISOU 2391 OXT VAL A 313 3063 1834 4604 122 458 -143 O TER 2392 VAL A 313 ATOM 1 N GLU A 2 -21.104 -23.110 65.754 1.00 75.03 N ANISOU 1 N GLU B 2 14170 9605 4735 -4391 -766 1310 N ATOM 2 CA GLU A 2 -21.187 -24.215 64.794 1.00 60.62 C ANISOU 2 CA GLU B 2 8747 10410 3875 -2837 2560 128 C ATOM 3 C GLU A 2 -20.580 -23.802 63.456 1.00 48.78 C ANISOU 3 C GLU B 2 5678 8798 4059 -1140 2091 658 C ATOM 4 O GLU A 2 -21.098 -22.917 62.766 1.00 56.39 O ANISOU 4 O GLU B 2 9776 8327 3321 -13 1874 1046 O ATOM 5 CB GLU A 2 -22.623 -24.687 64.612 1.00 64.91 C ANISOU 5 CB GLU B 2 9659 11107 3895 -3824 3645 -144 C ATOM 6 CG GLU A 2 -23.412 -25.037 65.850 1.00 76.58 C ANISOU 6 CG GLU B 2 13256 11834 4007 -5201 4934 -1036 C ATOM 7 CD GLU A 2 -22.816 -25.857 66.961 1.00 82.34 C ANISOU 7 CD GLU B 2 13596 12475 5214 -5915 5693 -1989 C ATOM 8 OE1 GLU A 2 -22.316 -26.978 66.711 1.00 85.12 O ANISOU 8 OE1 GLU B 2 15031 12372 4939 -5377 4967 -2771 O ATOM 9 OE2 GLU A 2 -22.844 -25.419 68.141 1.00 77.25 O ANISOU 9 OE2 GLU B 2 12258 11815 5278 -6087 5044 -3150 O ATOM 10 N ALA A 3 -19.474 -24.450 63.097 1.00 44.52 N ANISOU 10 N ALA B 3 5328 8512 3077 -692 1005 -21 N ATOM 11 CA ALA A 3 -18.676 -23.995 61.951 1.00 37.15 C ANISOU 11 CA ALA B 3 4929 6875 2312 -118 256 94 C ATOM 12 C ALA A 3 -19.353 -24.370 60.638 1.00 34.76 C ANISOU 12 C ALA B 3 3461 6800 2946 186 120 -148 C ATOM 13 O ALA A 3 -20.015 -25.381 60.451 1.00 43.55 O ANISOU 13 O ALA B 3 3381 9094 4071 -291 609 -585 O ATOM 14 CB ALA A 3 -17.255 -24.507 62.039 1.00 64.39 C ANISOU 14 CB ALA B 3 12657 7685 4122 -3199 -2118 694 C ATOM 15 N ILE A 4 -19.195 -23.483 59.684 1.00 26.63 N ANISOU 15 N ILE B 4 2974 4884 2262 88 -352 393 N ATOM 16 CA ILE A 4 -19.918 -23.485 58.451 1.00 25.38 C ANISOU 16 CA ILE B 4 3074 3923 2645 -143 -550 429 C ATOM 17 C ILE A 4 -19.139 -24.195 57.369 1.00 22.52 C ANISOU 17 C ILE B 4 2639 3826 2093 -248 -108 227 C ATOM 18 O ILE A 4 -17.961 -23.867 57.118 1.00 24.52 O ANISOU 18 O ILE B 4 2716 4108 2491 -448 7 73 O ATOM 19 CB ILE A 4 -20.214 -22.030 58.044 1.00 27.51 C ANISOU 19 CB ILE B 4 3879 3966 2607 106 197 825 C ATOM 20 CG1 ILE A 4 -21.058 -21.370 59.143 1.00 32.19 C ANISOU 20 CG1 ILE B 4 5071 4419 2740 795 51 1044 C ATOM 21 CG2 ILE A 4 -20.853 -21.941 56.675 1.00 28.01 C ANISOU 21 CG2 ILE B 4 4376 3753 2515 -196 418 919 C ATOM 22 CD1 ILE A 4 -21.332 -19.910 58.894 1.00 40.82 C ANISOU 22 CD1 ILE B 4 6632 5809 3070 2287 243 1078 C ATOM 23 N GLY A 5 -19.837 -25.147 56.764 1.00 20.76 N ANISOU 23 N GLY B 5 2447 3529 1913 -136 125 207 N ATOM 24 CA GLY A 5 -19.178 -25.954 55.757 1.00 20.45 C ANISOU 24 CA GLY B 5 2753 3742 1277 -415 59 55 C ATOM 25 C GLY A 5 -19.063 -25.256 54.420 1.00 18.18 C ANISOU 25 C GLY B 5 2407 2487 2012 129 559 65 C ATOM 26 O GLY A 5 -20.055 -24.847 53.801 1.00 19.77 O ANISOU 26 O GLY B 5 2857 2519 2137 -115 274 46 O ATOM 27 N VAL A 6 -17.822 -25.203 53.943 1.00 18.22 N ANISOU 27 N VAL B 6 2583 2735 1606 -312 195 12 N ATOM 28 CA VAL A 6 -17.519 -24.622 52.635 1.00 17.01 C ANISOU 28 CA VAL B 6 2426 2469 1569 -126 73 11 C ATOM 29 C VAL A 6 -16.770 -25.620 51.780 1.00 17.24 C ANISOU 29 C VAL B 6 2160 2596 1794 -78 51 167 C ATOM 30 O VAL A 6 -15.720 -26.108 52.200 1.00 18.12 O ANISOU 30 O VAL B 6 2595 2605 1685 113 26 138 O ATOM 31 CB VAL A 6 -16.700 -23.320 52.802 1.00 17.54 C ANISOU 31 CB VAL B 6 2379 2594 1692 -73 64 464 C ATOM 32 CG1 VAL A 6 -16.351 -22.751 51.449 1.00 18.16 C ANISOU 32 CG1 VAL B 6 2494 2634 1771 162 236 240 C ATOM 33 CG2 VAL A 6 -17.497 -22.316 53.642 1.00 19.01 C ANISOU 33 CG2 VAL B 6 2648 2502 2075 68 192 514 C ATOM 34 N LEU A 7 -17.285 -25.943 50.606 1.00 17.67 N ANISOU 34 N LEU B 7 2144 2491 2079 263 -182 78 N ATOM 35 CA LEU A 7 -16.649 -26.912 49.719 1.00 15.59 C ANISOU 35 CA LEU B 7 1495 2564 1863 416 220 59 C ATOM 36 C LEU A 7 -15.909 -26.122 48.649 1.00 14.92 C ANISOU 36 C LEU B 7 1370 2014 2287 429 382 -120 C ATOM 37 O LEU A 7 -16.497 -25.413 47.845 1.00 15.61 O ANISOU 37 O LEU B 7 1713 2159 2060 288 463 -193 O ATOM 38 CB LEU A 7 -17.687 -27.824 49.092 1.00 16.42 C ANISOU 38 CB LEU B 7 1470 2525 2246 172 221 247 C ATOM 39 CG LEU A 7 -17.186 -28.881 48.104 1.00 15.38 C ANISOU 39 CG LEU B 7 1769 2431 1642 22 13 -88 C ATOM 40 CD1 LEU A 7 -16.307 -29.889 48.862 1.00 18.41 C ANISOU 40 CD1 LEU B 7 2348 2562 2084 475 285 -81 C ATOM 41 CD2 LEU A 7 -18.363 -29.553 47.433 1.00 18.56 C ANISOU 41 CD2 LEU B 7 1722 2769 2560 -218 -174 156 C ATOM 42 N MET A 8 -14.593 -26.284 48.661 1.00 16.11 N ANISOU 42 N MET B 8 2406 2135 1578 109 284 -120 N ATOM 43 CA MET A 8 -13.723 -25.690 47.655 1.00 15.47 C ANISOU 43 CA MET B 8 2105 1975 1796 201 105 70 C ATOM 44 C MET A 8 -13.467 -26.705 46.552 1.00 14.98 C ANISOU 44 C MET B 8 1943 1956 1792 321 197 73 C ATOM 45 O MET A 8 -12.998 -27.815 46.804 1.00 16.97 O ANISOU 45 O MET B 8 2034 2289 2125 551 371 186 O ATOM 46 CB MET A 8 -12.456 -25.196 48.309 1.00 16.01 C ANISOU 46 CB MET B 8 1913 2336 1834 279 188 -327 C ATOM 47 CG MET A 8 -11.553 -24.391 47.448 1.00 19.64 C ANISOU 47 CG MET B 8 2449 2536 2479 -175 618 -448 C ATOM 48 SD MET A 8 -10.103 -23.841 48.381 1.00 23.54 S ANISOU 48 SD MET B 8 2226 2710 4010 -234 339 -604 S ATOM 49 CE MET A 8 -9.264 -23.013 47.073 1.00 23.59 C ANISOU 49 CE MET B 8 2517 2878 3570 -305 147 -101 C ATOM 50 N MET A 9 -13.759 -26.368 45.314 1.00 15.81 N ANISOU 50 N MET B 9 1738 2479 1790 288 144 5 N ATOM 51 CA MET A 9 -13.852 -27.407 44.287 1.00 16.10 C ANISOU 51 CA MET B 9 1641 2597 1878 227 124 176 C ATOM 52 C MET A 9 -12.534 -27.892 43.750 1.00 17.62 C ANISOU 52 C MET B 9 2212 2590 1893 469 670 241 C ATOM 53 O MET A 9 -12.425 -29.061 43.371 1.00 21.05 O ANISOU 53 O MET B 9 2499 2842 2657 704 624 549 O ATOM 54 CB MET A 9 -14.740 -26.885 43.140 1.00 18.08 C ANISOU 54 CB MET B 9 2348 2719 1801 70 -55 180 C ATOM 55 CG MET A 9 -16.175 -26.662 43.558 1.00 17.16 C ANISOU 55 CG MET B 9 2312 2585 1622 266 249 78 C ATOM 56 SD MET A 9 -16.971 -28.073 44.329 1.00 19.26 S ANISOU 56 SD MET B 9 2186 3004 2127 -21 173 -151 S ATOM 57 CE MET A 9 -17.078 -29.202 42.927 1.00 22.28 C ANISOU 57 CE MET B 9 2382 3109 2976 155 -235 225 C ATOM 58 N CYS A 10 -11.528 -27.045 43.707 1.00 19.04 N ANISOU 58 N CYS B 10 2393 2452 2390 313 563 628 N ATOM 59 CA CYS A 10 -10.236 -27.392 43.092 1.00 21.18 C ANISOU 59 CA CYS B 10 2405 2494 3147 607 749 1054 C ATOM 60 C CYS A 10 -9.138 -26.506 43.686 1.00 20.20 C ANISOU 60 C CYS B 10 2037 2050 3587 779 1185 533 C ATOM 61 O CYS A 10 -9.494 -25.476 44.287 1.00 21.28 O ANISOU 61 O CYS B 10 2542 2169 3372 554 438 399 O ATOM 62 CB CYS A 10 -10.287 -27.305 41.556 1.00 22.59 C ANISOU 62 CB CYS B 10 2850 2572 3164 610 950 1270 C ATOM 63 SG CYS A 10 -10.756 -25.713 40.919 1.00 28.72 S ANISOU 63 SG CYS B 10 3737 3623 3553 1157 1168 731 S ATOM 64 N PRO A 11 -7.856 -26.834 43.602 1.00 24.55 N ANISOU 64 N PRO B 11 2656 2085 4587 606 1094 705 N ATOM 65 CA PRO A 11 -6.823 -26.011 44.268 1.00 28.22 C ANISOU 65 CA PRO B 11 2545 2242 5937 448 953 458 C ATOM 66 C PRO A 11 -6.337 -24.740 43.613 1.00 27.72 C ANISOU 66 C PRO B 11 2699 2439 5394 720 1099 1831 C ATOM 67 O PRO A 11 -5.182 -24.599 43.168 1.00 37.50 O ANISOU 67 O PRO B 11 4588 2462 7198 -173 2635 868 O ATOM 68 CB PRO A 11 -5.628 -26.977 44.304 1.00 33.35 C ANISOU 68 CB PRO B 11 3529 2242 6899 513 605 190 C ATOM 69 CG PRO A 11 -5.804 -27.741 43.025 1.00 36.65 C ANISOU 69 CG PRO B 11 4317 2347 7259 -211 283 1509 C ATOM 70 CD PRO A 11 -7.288 -28.031 42.953 1.00 28.75 C ANISOU 70 CD PRO B 11 2683 2043 6197 657 998 976 C ATOM 71 N MET A 12 -7.155 -23.749 43.602 1.00 20.58 N ANISOU 71 N MET B 12 2472 2248 3101 384 652 625 N ATOM 72 CA MET A 12 -7.070 -22.525 42.847 1.00 17.81 C ANISOU 72 CA MET B 12 2202 2390 2174 -256 449 311 C ATOM 73 C MET A 12 -6.221 -21.410 43.443 1.00 18.70 C ANISOU 73 C MET B 12 2194 2438 2471 -153 442 106 C ATOM 74 O MET A 12 -5.893 -20.457 42.697 1.00 21.17 O ANISOU 74 O MET B 12 2299 2617 3126 -23 929 562 O ATOM 75 CB MET A 12 -8.503 -21.978 42.637 1.00 18.52 C ANISOU 75 CB MET B 12 2373 2397 2265 -280 663 57 C ATOM 76 CG MET A 12 -9.212 -21.532 43.864 1.00 19.13 C ANISOU 76 CG MET B 12 3027 2131 2109 -221 610 -107 C ATOM 77 SD MET A 12 -10.971 -21.285 43.774 1.00 18.02 S ANISOU 77 SD MET B 12 2157 2058 2632 77 156 114 S ATOM 78 CE MET A 12 -11.698 -22.890 43.641 1.00 18.25 C ANISOU 78 CE MET B 12 2190 2507 2237 355 327 135 C ATOM 79 N SER A 13 -5.898 -21.481 44.719 1.00 19.02 N ANISOU 79 N SER B 13 2394 2243 2590 -158 162 114 N ATOM 80 CA SER A 13 -5.191 -20.391 45.383 1.00 18.66 C ANISOU 80 CA SER B 13 2276 2234 2581 8 345 -110 C ATOM 81 C SER A 13 -4.802 -20.823 46.786 1.00 19.25 C ANISOU 81 C SER B 13 3033 1833 2447 -172 147 87 C ATOM 82 O SER A 13 -5.689 -21.036 47.611 1.00 18.98 O ANISOU 82 O SER B 13 2533 2048 2631 67 448 15 O ATOM 83 CB SER A 13 -6.066 -19.139 45.502 1.00 21.28 C ANISOU 83 CB SER B 13 2534 2457 3095 292 330 -148 C ATOM 84 OG SER A 13 -5.551 -18.221 46.490 1.00 20.39 O ANISOU 84 OG SER B 13 2563 2334 2850 145 396 64 O ATOM 85 N THR A 14 -3.513 -20.915 47.037 1.00 19.83 N ANISOU 85 N THR B 14 2290 1919 3325 16 343 -320 N ATOM 86 CA THR A 14 -3.016 -21.213 48.373 1.00 21.35 C ANISOU 86 CA THR B 14 2530 2163 3419 -30 12 -508 C ATOM 87 C THR A 14 -3.560 -20.234 49.389 1.00 20.64 C ANISOU 87 C THR B 14 2384 2161 3298 -54 290 -431 C ATOM 88 O THR A 14 -4.021 -20.659 50.447 1.00 21.24 O ANISOU 88 O THR B 14 2366 2534 3173 82 241 -639 O ATOM 89 CB THR A 14 -1.473 -21.211 48.366 1.00 23.77 C ANISOU 89 CB THR B 14 3364 2073 3595 -144 -49 -437 C ATOM 90 OG1 THR A 14 -1.064 -22.267 47.464 1.00 28.51 O ANISOU 90 OG1 THR B 14 3835 2200 4799 564 18 -106 O ATOM 91 CG2 THR A 14 -0.940 -21.478 49.760 1.00 27.96 C ANISOU 91 CG2 THR B 14 4314 2135 4173 72 443 -1196 C ATOM 92 N TYR A 15 -3.498 -18.950 49.071 1.00 19.88 N ANISOU 92 N TYR B 15 2314 2129 3112 -120 268 -383 N ATOM 93 CA TYR A 15 -3.946 -17.908 49.985 1.00 19.00 C ANISOU 93 CA TYR B 15 2146 2178 2896 -273 -32 -667 C ATOM 94 C TYR A 15 -5.418 -18.064 50.310 1.00 18.16 C ANISOU 94 C TYR B 15 1611 2317 2973 -76 -438 -178 C ATOM 95 O TYR A 15 -5.843 -17.993 51.476 1.00 20.02 O ANISOU 95 O TYR B 15 2368 2369 2869 -22 -71 -365 O ATOM 96 CB TYR A 15 -3.632 -16.553 49.348 1.00 21.27 C ANISOU 96 CB TYR B 15 1977 2129 3974 -360 111 -707 C ATOM 97 CG TYR A 15 -4.241 -15.384 50.067 1.00 21.29 C ANISOU 97 CG TYR B 15 1978 2443 3670 -322 16 -669 C ATOM 98 CD1 TYR A 15 -3.690 -14.881 51.216 1.00 23.71 C ANISOU 98 CD1 TYR B 15 2336 2692 3982 -324 -236 -956 C ATOM 99 CD2 TYR A 15 -5.395 -14.752 49.605 1.00 20.50 C ANISOU 99 CD2 TYR B 15 2309 2339 3140 -18 -286 -430 C ATOM 100 CE1 TYR A 15 -4.210 -13.818 51.910 1.00 25.51 C ANISOU 100 CE1 TYR B 15 2335 3194 4165 -52 -677 -1147 C ATOM 101 CE2 TYR A 15 -5.930 -13.674 50.287 1.00 20.95 C ANISOU 101 CE2 TYR B 15 2283 2630 3046 -180 -572 -253 C ATOM 102 CZ TYR A 15 -5.340 -13.207 51.433 1.00 22.36 C ANISOU 102 CZ TYR B 15 2459 2844 3194 -196 -592 -534 C ATOM 103 OH TYR A 15 -5.854 -12.143 52.135 1.00 25.94 O ANISOU 103 OH TYR B 15 2802 3598 3456 358 -1054 -557 O ATOM 104 N LEU A 16 -6.225 -18.266 49.250 1.00 18.04 N ANISOU 104 N LEU B 16 1684 2213 2957 -171 -124 -424 N ATOM 105 CA LEU A 16 -7.653 -18.427 49.515 1.00 16.86 C ANISOU 105 CA LEU B 16 1875 2066 2467 -106 -80 -247 C ATOM 106 C LEU A 16 -7.988 -19.624 50.405 1.00 17.33 C ANISOU 106 C LEU B 16 2134 2171 2278 -97 37 -261 C ATOM 107 O LEU A 16 -8.872 -19.549 51.269 1.00 17.42 O ANISOU 107 O LEU B 16 2259 2375 1983 -84 -143 -207 O ATOM 108 CB LEU A 16 -8.441 -18.570 48.188 1.00 16.28 C ANISOU 108 CB LEU B 16 1953 1927 2308 -166 78 -190 C ATOM 109 CG LEU A 16 -9.948 -18.718 48.271 1.00 15.31 C ANISOU 109 CG LEU B 16 1579 2232 2005 -236 -30 17 C ATOM 110 CD1 LEU A 16 -10.634 -17.583 49.024 1.00 17.07 C ANISOU 110 CD1 LEU B 16 2199 2064 2221 -174 -33 -7 C ATOM 111 CD2 LEU A 16 -10.540 -18.806 46.861 1.00 17.37 C ANISOU 111 CD2 LEU B 16 1727 2660 2213 -74 -151 -400 C ATOM 112 N GLU A 17 -7.287 -20.726 50.144 1.00 17.27 N ANISOU 112 N GLU B 17 2220 2340 2000 33 234 -175 N ATOM 113 CA GLU A 17 -7.449 -21.935 50.932 1.00 17.65 C ANISOU 113 CA GLU B 17 2195 1979 2533 -274 557 -163 C ATOM 114 C GLU A 17 -7.156 -21.586 52.385 1.00 21.00 C ANISOU 114 C GLU B 17 2445 3009 2526 -204 667 -784 C ATOM 115 O GLU A 17 -7.936 -21.991 53.251 1.00 21.11 O ANISOU 115 O GLU B 17 2660 3082 2279 -508 436 -770 O ATOM 116 CB GLU A 17 -6.535 -23.016 50.383 1.00 22.29 C ANISOU 116 CB GLU B 17 2648 1981 3840 -21 1350 294 C ATOM 117 CG GLU A 17 -6.721 -24.437 50.803 1.00 31.28 C ANISOU 117 CG GLU B 17 2464 3187 6232 478 1066 377 C ATOM 118 CD GLU A 17 -5.803 -25.404 50.093 1.00 33.07 C ANISOU 118 CD GLU B 17 2533 3330 6702 384 -463 307 C ATOM 119 OE1 GLU A 17 -5.526 -26.446 50.699 1.00 34.15 O ANISOU 119 OE1 GLU B 17 3894 2894 6188 508 -384 238 O ATOM 120 OE2 GLU A 17 -5.379 -25.150 48.969 1.00 37.10 O ANISOU 120 OE2 GLU B 17 3482 2661 7955 1222 953 1206 O ATOM 121 N GLN A 18 -6.065 -20.850 52.628 1.00 20.46 N ANISOU 121 N GLN B 18 2756 2671 2345 -401 378 -277 N ATOM 122 CA GLN A 18 -5.661 -20.489 53.990 1.00 24.18 C ANISOU 122 CA GLN B 18 3117 3416 2654 29 37 -682 C ATOM 123 C GLN A 18 -6.732 -19.630 54.669 1.00 23.82 C ANISOU 123 C GLN B 18 3664 3326 2059 -469 -819 -942 C ATOM 124 O GLN A 18 -7.098 -19.808 55.845 1.00 26.62 O ANISOU 124 O GLN B 18 3792 4058 2266 -515 -524 -663 O ATOM 125 CB GLN A 18 -4.314 -19.762 53.991 1.00 25.68 C ANISOU 125 CB GLN B 18 3238 2965 3554 119 -628 -671 C ATOM 126 CG GLN A 18 -3.099 -20.621 53.686 1.00 30.43 C ANISOU 126 CG GLN B 18 4653 2768 4139 -14 -772 -1053 C ATOM 127 CD GLN A 18 -1.846 -19.813 53.387 1.00 31.99 C ANISOU 127 CD GLN B 18 4392 2433 5331 -341 -2176 -901 C ATOM 128 OE1 GLN A 18 -1.901 -18.587 53.149 1.00 40.66 O ANISOU 128 OE1 GLN B 18 4574 2936 7938 -236 -582 190 O ATOM 129 NE2 GLN A 18 -0.691 -20.463 53.423 1.00 39.74 N ANISOU 129 NE2 GLN B 18 6864 2375 5860 -467 -863 -857 N ATOM 130 N GLU A 19 -7.250 -18.677 53.874 1.00 22.72 N ANISOU 130 N GLU B 19 2818 3063 2753 -479 -274 -597 N ATOM 131 CA GLU A 19 -8.215 -17.717 54.418 1.00 22.47 C ANISOU 131 CA GLU B 19 2600 3515 2421 -314 -260 -190 C ATOM 132 C GLU A 19 -9.550 -18.370 54.697 1.00 21.54 C ANISOU 132 C GLU B 19 2603 3528 2055 -255 -368 146 C ATOM 133 O GLU A 19 -10.225 -17.992 55.678 1.00 24.90 O ANISOU 133 O GLU B 19 3126 3988 2346 -598 -886 462 O ATOM 134 CB GLU A 19 -8.363 -16.533 53.465 1.00 23.58 C ANISOU 134 CB GLU B 19 2896 3305 2757 -70 107 264 C ATOM 135 CG GLU A 19 -7.047 -15.762 53.313 1.00 23.38 C ANISOU 135 CG GLU B 19 2912 2833 3140 -12 241 2 C ATOM 136 CD GLU A 19 -6.609 -15.115 54.601 1.00 29.01 C ANISOU 136 CD GLU B 19 2699 4469 3853 -90 -270 602 C ATOM 137 OE1 GLU A 19 -7.441 -14.359 55.158 1.00 39.16 O ANISOU 137 OE1 GLU B 19 3592 5737 5551 -442 -833 2353 O ATOM 138 OE2 GLU A 19 -5.479 -15.341 55.090 1.00 35.64 O ANISOU 138 OE2 GLU B 19 3845 5647 4052 -919 -1026 -40 O ATOM 139 N LEU A 20 -9.919 -19.351 53.868 1.00 19.31 N ANISOU 139 N LEU B 20 2510 2572 2255 -40 -333 108 N ATOM 140 CA LEU A 20 -11.144 -20.087 54.131 1.00 20.91 C ANISOU 140 CA LEU B 20 2666 3081 2198 -370 -185 -388 C ATOM 141 C LEU A 20 -10.984 -21.020 55.310 1.00 22.87 C ANISOU 141 C LEU B 20 2921 3654 2114 -450 -96 -555 C ATOM 142 O LEU A 20 -11.917 -21.113 56.122 1.00 23.85 O ANISOU 142 O LEU B 20 3121 3735 2204 -50 -46 -239 O ATOM 143 CB LEU A 20 -11.614 -20.863 52.898 1.00 19.88 C ANISOU 143 CB LEU B 20 2445 3109 2000 -185 5 -368 C ATOM 144 CG LEU A 20 -12.027 -20.033 51.676 1.00 16.69 C ANISOU 144 CG LEU B 20 2062 2316 1965 -485 265 -6 C ATOM 145 CD1 LEU A 20 -12.252 -20.949 50.490 1.00 18.08 C ANISOU 145 CD1 LEU B 20 2491 2425 1955 -390 33 -341 C ATOM 146 CD2 LEU A 20 -13.234 -19.199 52.000 1.00 20.45 C ANISOU 146 CD2 LEU B 20 2790 2356 2624 -578 130 176 C ATOM 147 N ASP A 21 -9.832 -21.659 55.416 1.00 22.27 N ANISOU 147 N ASP B 21 2606 3753 2105 -591 379 -785 N ATOM 148 CA ASP A 21 -9.563 -22.599 56.499 1.00 23.08 C ANISOU 148 CA ASP B 21 2316 4114 2341 -469 368 -885 C ATOM 149 C ASP A 21 -9.584 -21.896 57.850 1.00 25.15 C ANISOU 149 C ASP B 21 3114 4253 2190 -744 186 -1087 C ATOM 150 O ASP A 21 -10.017 -22.556 58.795 1.00 30.48 O ANISOU 150 O ASP B 21 3788 5473 2321 -90 511 -799 O ATOM 151 CB ASP A 21 -8.216 -23.293 56.213 1.00 26.05 C ANISOU 151 CB ASP B 21 3375 3985 2539 -540 154 -1186 C ATOM 152 CG ASP A 21 -8.032 -24.680 56.772 1.00 32.98 C ANISOU 152 CG ASP B 21 3234 4106 5188 -407 93 -1778 C ATOM 153 OD1 ASP A 21 -8.981 -25.412 57.102 1.00 29.67 O ANISOU 153 OD1 ASP B 21 3428 4250 3595 -124 298 -891 O ATOM 154 OD2 ASP A 21 -6.848 -25.083 56.896 1.00 48.17 O ANISOU 154 OD2 ASP B 21 4922 4299 9081 -863 2125 -2651 O ATOM 155 N LYS A 22 -9.145 -20.635 57.931 1.00 27.10 N ANISOU 155 N LYS B 22 3101 4842 2352 -768 -274 -577 N ATOM 156 CA LYS A 22 -9.134 -19.835 59.143 1.00 31.13 C ANISOU 156 CA LYS B 22 4436 5184 2208 -342 -467 -545 C ATOM 157 C LYS A 22 -10.574 -19.501 59.566 1.00 29.31 C ANISOU 157 C LYS B 22 3981 5298 1859 -233 180 -578 C ATOM 158 O LYS A 22 -10.798 -19.339 60.772 1.00 35.95 O ANISOU 158 O LYS B 22 5557 6175 1927 -646 381 -390 O ATOM 159 CB LYS A 22 -8.464 -18.464 59.119 1.00 34.67 C ANISOU 159 CB LYS B 22 4280 6833 2062 -1277 -1429 366 C ATOM 160 CG LYS A 22 -7.020 -18.245 58.792 1.00 43.30 C ANISOU 160 CG LYS B 22 5907 7771 2775 -2632 -369 -916 C ATOM 161 CD LYS A 22 -6.734 -16.745 58.774 1.00 46.39 C ANISOU 161 CD LYS B 22 5200 9419 3007 -3304 -1029 -928 C ATOM 162 CE LYS A 22 -5.266 -16.472 58.605 1.00 50.03 C ANISOU 162 CE LYS B 22 6464 9549 2997 -3966 -531 -1740 C ATOM 163 NZ LYS A 22 -4.946 -15.214 57.858 1.00 51.00 N ANISOU 163 NZ LYS B 22 5548 9963 3866 -2904 -728 1007 N ATOM 164 N ARG A 23 -11.496 -19.378 58.611 1.00 28.71 N ANISOU 164 N ARG B 23 3242 5221 2447 -308 -535 -466 N ATOM 165 CA ARG A 23 -12.821 -18.861 58.918 1.00 28.22 C ANISOU 165 CA ARG B 23 3168 5103 2451 146 -702 -347 C ATOM 166 C ARG A 23 -13.988 -19.830 58.992 1.00 24.90 C ANISOU 166 C ARG B 23 3232 4522 1706 244 -630 266 C ATOM 167 O ARG A 23 -15.003 -19.583 59.657 1.00 33.66 O ANISOU 167 O ARG B 23 4642 5398 2748 -344 -1138 1314 O ATOM 168 CB ARG A 23 -13.170 -17.876 57.784 1.00 27.74 C ANISOU 168 CB ARG B 23 3434 5013 2092 -207 -230 4 C ATOM 169 CG ARG A 23 -12.380 -16.580 57.953 1.00 29.49 C ANISOU 169 CG ARG B 23 3453 5344 2408 330 -519 -164 C ATOM 170 CD ARG A 23 -12.607 -15.744 56.708 1.00 31.12 C ANISOU 170 CD ARG B 23 3282 5858 2683 -334 -184 -497 C ATOM 171 NE ARG A 23 -12.008 -14.413 56.843 1.00 30.45 N ANISOU 171 NE ARG B 23 3282 5579 2709 -232 -200 -153 N ATOM 172 CZ ARG A 23 -10.710 -14.147 56.729 1.00 31.07 C ANISOU 172 CZ ARG B 23 3115 5625 3065 -103 635 -22 C ATOM 173 NH1 ARG A 23 -9.885 -15.151 56.473 1.00 35.39 N ANISOU 173 NH1 ARG B 23 3056 5734 4657 -496 -1282 360 N ATOM 174 NH2 ARG A 23 -10.270 -12.897 56.872 1.00 32.59 N ANISOU 174 NH2 ARG B 23 3270 5635 3477 -264 -200 1018 N ATOM 175 N PHE A 24 -13.861 -20.920 58.267 1.00 24.72 N ANISOU 175 N PHE B 24 3244 3772 2378 263 -857 8 N ATOM 176 CA PHE A 24 -14.973 -21.810 57.998 1.00 22.85 C ANISOU 176 CA PHE B 24 3157 3730 1794 169 -536 207 C ATOM 177 C PHE A 24 -14.545 -23.245 58.223 1.00 21.98 C ANISOU 177 C PHE B 24 3043 3495 1814 -151 -408 -307 C ATOM 178 O PHE A 24 -13.389 -23.540 58.511 1.00 24.45 O ANISOU 178 O PHE B 24 3647 3578 2063 -539 71 -317 O ATOM 179 CB PHE A 24 -15.436 -21.647 56.536 1.00 23.00 C ANISOU 179 CB PHE B 24 2713 3924 2102 177 -272 -310 C ATOM 180 CG PHE A 24 -15.890 -20.246 56.181 1.00 22.84 C ANISOU 180 CG PHE B 24 2629 3503 2546 -52 169 223 C ATOM 181 CD1 PHE A 24 -17.059 -19.747 56.751 1.00 27.98 C ANISOU 181 CD1 PHE B 24 3203 4157 3270 258 264 1203 C ATOM 182 CD2 PHE A 24 -15.196 -19.424 55.296 1.00 21.77 C ANISOU 182 CD2 PHE B 24 3066 3499 1704 -171 146 -235 C ATOM 183 CE1 PHE A 24 -17.528 -18.493 56.469 1.00 26.70 C ANISOU 183 CE1 PHE B 24 3400 3897 2848 270 265 1496 C ATOM 184 CE2 PHE A 24 -15.663 -18.142 55.020 1.00 22.04 C ANISOU 184 CE2 PHE B 24 3385 3367 1622 -107 434 91 C ATOM 185 CZ PHE A 24 -16.835 -17.678 55.606 1.00 24.51 C ANISOU 185 CZ PHE B 24 3485 3880 1947 45 45 862 C ATOM 186 N LYS A 25 -15.465 -24.173 58.061 1.00 22.04 N ANISOU 186 N LYS B 25 2965 3564 1846 -150 -341 279 N ATOM 187 CA LYS A 25 -15.113 -25.592 57.963 1.00 23.03 C ANISOU 187 CA LYS B 25 3198 3901 1650 233 142 310 C ATOM 188 C LYS A 25 -14.861 -25.922 56.493 1.00 21.07 C ANISOU 188 C LYS B 25 2657 3712 1637 4 -169 172 C ATOM 189 O LYS A 25 -15.799 -26.076 55.728 1.00 21.97 O ANISOU 189 O LYS B 25 3034 3320 1995 278 -187 -73 O ATOM 190 CB LYS A 25 -16.224 -26.465 58.552 1.00 27.69 C ANISOU 190 CB LYS B 25 3530 4733 2257 206 743 340 C ATOM 191 CG LYS A 25 -15.917 -27.961 58.520 1.00 34.68 C ANISOU 191 CG LYS B 25 3440 6161 3576 781 649 86 C ATOM 192 CD LYS A 25 -16.943 -28.801 59.272 1.00 42.67 C ANISOU 192 CD LYS B 25 3624 7930 4657 658 1138 440 C ATOM 193 CE LYS A 25 -16.278 -29.783 60.220 1.00 55.99 C ANISOU 193 CE LYS B 25 5843 9079 6351 80 3451 -454 C ATOM 194 NZ LYS A 25 -16.937 -31.121 60.261 1.00 68.09 N ANISOU 194 NZ LYS B 25 6093 11170 8610 1499 4588 298 N ATOM 195 N LEU A 26 -13.588 -25.938 56.111 1.00 21.86 N ANISOU 195 N LEU B 26 3877 2711 1719 494 -241 116 N ATOM 196 CA LEU A 26 -13.187 -26.087 54.724 1.00 19.47 C ANISOU 196 CA LEU B 26 2653 3047 1697 535 -146 98 C ATOM 197 C LEU A 26 -13.075 -27.555 54.336 1.00 20.63 C ANISOU 197 C LEU B 26 2802 3124 1911 698 -384 -264 C ATOM 198 O LEU A 26 -12.320 -28.282 54.992 1.00 21.42 O ANISOU 198 O LEU B 26 2850 3185 2103 645 -110 -362 O ATOM 199 CB LEU A 26 -11.829 -25.410 54.444 1.00 21.45 C ANISOU 199 CB LEU B 26 2765 3258 2128 366 -139 23 C ATOM 200 CG LEU A 26 -11.271 -25.575 53.021 1.00 23.65 C ANISOU 200 CG LEU B 26 2998 4200 1787 -562 -61 -275 C ATOM 201 CD1 LEU A 26 -12.189 -24.928 51.990 1.00 24.56 C ANISOU 201 CD1 LEU B 26 3100 4071 2161 153 -435 -340 C ATOM 202 CD2 LEU A 26 -9.848 -25.009 52.905 1.00 23.42 C ANISOU 202 CD2 LEU B 26 2581 3472 2845 34 -402 433 C ATOM 203 N PHE A 27 -13.788 -27.900 53.270 1.00 19.01 N ANISOU 203 N PHE B 27 2264 2969 1990 174 -171 -57 N ATOM 204 CA PHE A 27 -13.665 -29.180 52.594 1.00 19.01 C ANISOU 204 CA PHE B 27 2333 2999 1892 438 -178 -409 C ATOM 205 C PHE A 27 -12.962 -28.960 51.256 1.00 17.92 C ANISOU 205 C PHE B 27 2117 2835 1857 640 -341 -372 C ATOM 206 O PHE A 27 -13.368 -28.073 50.520 1.00 19.60 O ANISOU 206 O PHE B 27 2667 2789 1991 593 3 -378 O ATOM 207 CB PHE A 27 -15.032 -29.813 52.374 1.00 20.22 C ANISOU 207 CB PHE B 27 2430 3172 2082 321 -448 -37 C ATOM 208 CG PHE A 27 -15.790 -30.140 53.646 1.00 22.65 C ANISOU 208 CG PHE B 27 3080 3291 2234 -97 -79 -326 C ATOM 209 CD1 PHE A 27 -15.402 -31.208 54.419 1.00 23.26 C ANISOU 209 CD1 PHE B 27 3058 3591 2186 105 -160 -301 C ATOM 210 CD2 PHE A 27 -16.868 -29.373 54.037 1.00 28.05 C ANISOU 210 CD2 PHE B 27 4550 3467 2642 198 934 54 C ATOM 211 CE1 PHE A 27 -16.102 -31.483 55.569 1.00 25.54 C ANISOU 211 CE1 PHE B 27 2897 4291 2515 239 107 -79 C ATOM 212 CE2 PHE A 27 -17.605 -29.652 55.186 1.00 29.75 C ANISOU 212 CE2 PHE B 27 3770 4257 3275 525 1144 586 C ATOM 213 CZ PHE A 27 -17.200 -30.724 55.950 1.00 25.22 C ANISOU 213 CZ PHE B 27 2448 4601 2533 498 226 443 C ATOM 214 N ARG A 28 -11.935 -29.752 51.006 1.00 21.84 N ANISOU 214 N ARG B 28 3034 2863 2403 853 147 -176 N ATOM 215 CA ARG A 28 -11.229 -29.724 49.729 1.00 21.21 C ANISOU 215 CA ARG B 28 2806 2824 2428 757 242 -201 C ATOM 216 C ARG A 28 -11.712 -30.868 48.835 1.00 20.71 C ANISOU 216 C ARG B 28 2701 2725 2443 715 337 28 C ATOM 217 O ARG A 28 -11.344 -32.016 49.056 1.00 23.20 O ANISOU 217 O ARG B 28 2754 3176 2885 923 310 -322 O ATOM 218 CB ARG A 28 -9.735 -29.765 49.971 1.00 24.11 C ANISOU 218 CB ARG B 28 2898 2833 3428 665 10 -121 C ATOM 219 CG ARG A 28 -9.203 -28.636 50.849 1.00 28.24 C ANISOU 219 CG ARG B 28 2929 2733 5069 772 -590 -165 C ATOM 220 CD ARG A 28 -7.816 -28.948 51.369 1.00 33.96 C ANISOU 220 CD ARG B 28 4788 3055 5060 246 -1471 -137 C ATOM 221 NE ARG A 28 -7.140 -27.914 52.128 1.00 34.93 N ANISOU 221 NE ARG B 28 4721 3303 5248 336 -1437 -312 N ATOM 222 CZ ARG A 28 -7.236 -27.544 53.398 1.00 36.00 C ANISOU 222 CZ ARG B 28 4636 4069 4974 565 -1419 -920 C ATOM 223 NH1 ARG A 28 -8.085 -28.145 54.231 1.00 45.12 N ANISOU 223 NH1 ARG B 28 6471 6215 4458 -523 -449 -1901 N ATOM 224 NH2 ARG A 28 -6.499 -26.553 53.902 1.00 44.44 N ANISOU 224 NH2 ARG B 28 5695 4701 6491 -208 -2740 -1536 N ATOM 225 N TYR A 29 -12.557 -30.539 47.847 1.00 19.51 N ANISOU 225 N TYR B 29 2286 3030 2097 703 477 74 N ATOM 226 CA TYR A 29 -13.229 -31.607 47.109 1.00 19.27 C ANISOU 226 CA TYR B 29 2081 2852 2389 596 547 197 C ATOM 227 C TYR A 29 -12.244 -32.501 46.385 1.00 21.89 C ANISOU 227 C TYR B 29 2342 3287 2690 833 587 600 C ATOM 228 O TYR A 29 -12.481 -33.721 46.288 1.00 21.29 O ANISOU 228 O TYR B 29 2489 3652 1948 1060 312 187 O ATOM 229 CB TYR A 29 -14.187 -30.994 46.085 1.00 20.85 C ANISOU 229 CB TYR B 29 2413 3321 2189 363 511 31 C ATOM 230 CG TYR A 29 -15.120 -31.926 45.361 1.00 20.39 C ANISOU 230 CG TYR B 29 2237 3266 2246 716 496 37 C ATOM 231 CD1 TYR A 29 -15.960 -32.776 46.043 1.00 21.61 C ANISOU 231 CD1 TYR B 29 2250 3466 2494 667 522 265 C ATOM 232 CD2 TYR A 29 -15.169 -31.937 43.991 1.00 22.11 C ANISOU 232 CD2 TYR B 29 2415 3721 2266 353 505 -285 C ATOM 233 CE1 TYR A 29 -16.832 -33.638 45.402 1.00 23.57 C ANISOU 233 CE1 TYR B 29 2270 3808 2876 598 391 459 C ATOM 234 CE2 TYR A 29 -16.033 -32.790 43.315 1.00 22.80 C ANISOU 234 CE2 TYR B 29 2283 3784 2596 705 412 -477 C ATOM 235 CZ TYR A 29 -16.867 -33.643 44.009 1.00 24.35 C ANISOU 235 CZ TYR B 29 2269 4088 2894 507 353 -201 C ATOM 236 OH TYR A 29 -17.729 -34.494 43.333 1.00 27.34 O ANISOU 236 OH TYR B 29 2369 4494 3524 451 2 28 O ATOM 237 N TRP A 30 -11.180 -31.929 45.852 1.00 22.72 N ANISOU 237 N TRP B 30 2577 2943 3113 834 590 718 N ATOM 238 CA TRP A 30 -10.245 -32.598 44.946 1.00 23.89 C ANISOU 238 CA TRP B 30 2859 3211 3006 842 652 815 C ATOM 239 C TRP A 30 -9.364 -33.587 45.666 1.00 24.78 C ANISOU 239 C TRP B 30 3215 3021 3179 1072 508 963 C ATOM 240 O TRP A 30 -8.669 -34.400 45.030 1.00 30.18 O ANISOU 240 O TRP B 30 3846 3656 3965 1683 557 1434 O ATOM 241 CB TRP A 30 -9.359 -31.563 44.237 1.00 28.09 C ANISOU 241 CB TRP B 30 3192 3495 3988 930 1185 1240 C ATOM 242 CG TRP A 30 -8.384 -30.821 45.105 1.00 25.91 C ANISOU 242 CG TRP B 30 2684 2793 4369 1003 1549 898 C ATOM 243 CD1 TRP A 30 -7.050 -31.142 45.292 1.00 32.08 C ANISOU 243 CD1 TRP B 30 4412 2542 5234 1432 871 485 C ATOM 244 CD2 TRP A 30 -8.612 -29.638 45.904 1.00 25.54 C ANISOU 244 CD2 TRP B 30 3156 2473 4075 702 1063 751 C ATOM 245 NE1 TRP A 30 -6.442 -30.253 46.141 1.00 33.04 N ANISOU 245 NE1 TRP B 30 4562 2448 5545 587 713 740 N ATOM 246 CE2 TRP A 30 -7.381 -29.323 46.529 1.00 28.27 C ANISOU 246 CE2 TRP B 30 3064 2467 5208 744 1042 434 C ATOM 247 CE3 TRP A 30 -9.699 -28.792 46.172 1.00 25.48 C ANISOU 247 CE3 TRP B 30 3111 2370 4199 1070 934 170 C ATOM 248 CZ2 TRP A 30 -7.239 -28.226 47.386 1.00 27.19 C ANISOU 248 CZ2 TRP B 30 2743 2306 5282 -79 1060 852 C ATOM 249 CZ3 TRP A 30 -9.547 -27.711 47.022 1.00 24.42 C ANISOU 249 CZ3 TRP B 30 3253 1949 4078 997 798 -138 C ATOM 250 CH2 TRP A 30 -8.310 -27.431 47.626 1.00 26.49 C ANISOU 250 CH2 TRP B 30 3499 2182 4382 450 816 211 C ATOM 251 N THR A 31 -9.357 -33.532 46.994 1.00 25.81 N ANISOU 251 N THR B 31 3654 2954 3197 780 416 602 N ATOM 252 CA THR A 31 -8.538 -34.456 47.800 1.00 29.34 C ANISOU 252 CA THR B 31 3900 3153 4095 271 1191 132 C ATOM 253 C THR A 31 -9.324 -35.707 48.170 1.00 29.33 C ANISOU 253 C THR B 31 3623 2870 4652 954 709 550 C ATOM 254 O THR A 31 -8.720 -36.656 48.684 1.00 36.73 O ANISOU 254 O THR B 31 4082 2849 7027 996 1122 73 O ATOM 255 CB THR A 31 -7.966 -33.833 49.099 1.00 30.65 C ANISOU 255 CB THR B 31 3574 3377 4693 420 1066 -872 C ATOM 256 OG1 THR A 31 -9.019 -33.420 49.988 1.00 30.10 O ANISOU 256 OG1 THR B 31 3594 3883 3960 738 179 -702 O ATOM 257 CG2 THR A 31 -7.143 -32.591 48.789 1.00 37.72 C ANISOU 257 CG2 THR B 31 3437 3474 7422 602 956 -608 C ATOM 258 N GLN A 32 -10.625 -35.720 47.948 1.00 25.86 N ANISOU 258 N GLN B 32 2795 3364 3668 1063 486 -37 N ATOM 259 CA GLN A 32 -11.426 -36.875 48.396 1.00 26.59 C ANISOU 259 CA GLN B 32 2928 3902 3270 1173 655 -105 C ATOM 260 C GLN A 32 -11.317 -38.024 47.409 1.00 27.55 C ANISOU 260 C GLN B 32 2944 4138 3387 1392 245 -709 C ATOM 261 O GLN A 32 -11.712 -37.862 46.235 1.00 30.93 O ANISOU 261 O GLN B 32 4044 4266 3443 1731 150 -836 O ATOM 262 CB GLN A 32 -12.891 -36.465 48.597 1.00 27.48 C ANISOU 262 CB GLN B 32 3537 4425 2479 219 411 -36 C ATOM 263 CG GLN A 32 -13.093 -35.470 49.741 1.00 27.47 C ANISOU 263 CG GLN B 32 3603 4066 2769 -72 240 186 C ATOM 264 CD GLN A 32 -12.871 -36.219 51.059 1.00 27.48 C ANISOU 264 CD GLN B 32 3436 4451 2554 221 266 523 C ATOM 265 OE1 GLN A 32 -13.065 -37.422 51.195 1.00 35.76 O ANISOU 265 OE1 GLN B 32 3758 5723 4105 950 -395 -1287 O ATOM 266 NE2 GLN A 32 -12.444 -35.531 52.081 1.00 28.24 N ANISOU 266 NE2 GLN B 32 3969 3938 2821 590 -119 204 N ATOM 267 N PRO A 33 -10.787 -39.190 47.790 1.00 29.03 N ANISOU 267 N PRO B 33 3865 3796 3368 1580 -228 -823 N ATOM 268 CA PRO A 33 -10.746 -40.320 46.853 1.00 29.70 C ANISOU 268 CA PRO B 33 4549 3549 3189 1683 -125 -440 C ATOM 269 C PRO A 33 -12.088 -40.907 46.445 1.00 29.12 C ANISOU 269 C PRO B 33 4524 3865 2675 1765 -690 -132 C ATOM 270 O PRO A 33 -12.207 -41.558 45.389 1.00 36.40 O ANISOU 270 O PRO B 33 5633 5492 2706 2565 -1110 -457 O ATOM 271 CB PRO A 33 -9.970 -41.390 47.649 1.00 32.30 C ANISOU 271 CB PRO B 33 5053 3520 3700 1885 -6 -447 C ATOM 272 CG PRO A 33 -10.193 -41.021 49.092 1.00 31.58 C ANISOU 272 CG PRO B 33 4794 3660 3545 1995 -570 -1096 C ATOM 273 CD PRO A 33 -10.172 -39.518 49.082 1.00 29.15 C ANISOU 273 CD PRO B 33 3745 3758 3571 1141 -316 -1004 C ATOM 274 N ALA A 34 -13.157 -40.773 47.203 1.00 28.14 N ANISOU 274 N ALA B 34 3882 3858 2950 1818 259 -511 N ATOM 275 CA ALA A 34 -14.491 -41.259 46.823 1.00 28.73 C ANISOU 275 CA ALA B 34 3383 4705 2826 1747 330 -498 C ATOM 276 C ALA A 34 -15.452 -40.086 46.964 1.00 23.31 C ANISOU 276 C ALA B 34 2131 4336 2390 951 162 -339 C ATOM 277 O ALA A 34 -16.180 -39.863 47.914 1.00 25.15 O ANISOU 277 O ALA B 34 2237 5041 2277 835 -91 -78 O ATOM 278 CB ALA A 34 -14.878 -42.480 47.646 1.00 33.06 C ANISOU 278 CB ALA B 34 2995 6900 2664 2189 -447 -2045 C ATOM 279 N GLN A 35 -15.455 -39.247 45.921 1.00 22.76 N ANISOU 279 N GLN B 35 2328 4295 2023 1265 -188 -340 N ATOM 280 CA GLN A 35 -16.170 -37.990 45.988 1.00 20.03 C ANISOU 280 CA GLN B 35 1889 3981 1739 832 -455 -541 C ATOM 281 C GLN A 35 -17.665 -38.144 46.162 1.00 22.32 C ANISOU 281 C GLN B 35 2042 4320 2119 497 -179 -794 C ATOM 282 O GLN A 35 -18.328 -37.350 46.807 1.00 24.42 O ANISOU 282 O GLN B 35 2502 3934 2844 571 243 -689 O ATOM 283 CB GLN A 35 -15.860 -37.182 44.712 1.00 20.60 C ANISOU 283 CB GLN B 35 3219 2978 1629 1210 -15 80 C ATOM 284 CG GLN A 35 -14.404 -36.723 44.721 1.00 25.74 C ANISOU 284 CG GLN B 35 3736 4359 1683 289 337 88 C ATOM 285 CD GLN A 35 -14.008 -36.009 43.455 1.00 27.19 C ANISOU 285 CD GLN B 35 3589 5282 1460 632 127 333 C ATOM 286 OE1 GLN A 35 -14.376 -36.414 42.343 1.00 31.02 O ANISOU 286 OE1 GLN B 35 4004 6238 1545 1695 -182 442 O ATOM 287 NE2 GLN A 35 -13.240 -34.940 43.626 1.00 28.51 N ANISOU 287 NE2 GLN B 35 3469 5369 1992 1085 192 594 N ATOM 288 N ARG A 36 -18.291 -39.153 45.558 1.00 27.13 N ANISOU 288 N ARG B 36 1631 5177 3499 699 -127 -1439 N ATOM 289 CA ARG A 36 -19.732 -39.209 45.655 1.00 31.26 C ANISOU 289 CA ARG B 36 2478 6192 3209 -369 -308 -1189 C ATOM 290 C ARG A 36 -20.159 -39.671 47.051 1.00 32.26 C ANISOU 290 C ARG B 36 2976 6264 3019 -601 -428 -1525 C ATOM 291 O ARG A 36 -21.188 -39.218 47.566 1.00 31.31 O ANISOU 291 O ARG B 36 2681 6354 2859 -173 69 -1472 O ATOM 292 CB ARG A 36 -20.295 -40.134 44.561 1.00 30.74 C ANISOU 292 CB ARG B 36 2455 6202 3024 -218 -271 -1020 C ATOM 293 CG ARG A 36 -19.819 -39.813 43.152 1.00 36.01 C ANISOU 293 CG ARG B 36 4029 6900 2752 -91 245 -2155 C ATOM 294 CD ARG A 36 -20.251 -38.427 42.704 1.00 38.92 C ANISOU 294 CD ARG B 36 5321 5963 3504 78 429 -1990 C ATOM 295 NE ARG A 36 -21.689 -38.270 42.696 1.00 46.75 N ANISOU 295 NE ARG B 36 7426 6132 4207 -643 -24 -1008 N ATOM 296 CZ ARG A 36 -22.522 -38.087 41.679 1.00 47.24 C ANISOU 296 CZ ARG B 36 7981 6288 3679 -2769 -966 83 C ATOM 297 NH1 ARG A 36 -22.204 -38.008 40.388 1.00 24.22 N ANISOU 297 NH1 ARG B 36 2661 2685 3856 191 -783 163 N ATOM 298 NH2 ARG A 36 -23.806 -37.970 42.000 1.00 31.36 N ANISOU 298 NH2 ARG B 36 3939 4466 3512 759 361 555 N ATOM 299 N ASP A 37 -19.358 -40.562 47.651 1.00 31.86 N ANISOU 299 N ASP B 37 2520 6529 3055 526 -949 -1317 N ATOM 300 CA ASP A 37 -19.482 -40.985 49.037 1.00 32.28 C ANISOU 300 CA ASP B 37 2718 6377 3171 1026 -677 -1065 C ATOM 301 C ASP A 37 -19.373 -39.774 49.961 1.00 27.30 C ANISOU 301 C ASP B 37 2239 5277 2855 811 28 -522 C ATOM 302 O ASP A 37 -20.106 -39.464 50.908 1.00 27.97 O ANISOU 302 O ASP B 37 2595 4345 3689 638 351 -450 O ATOM 303 CB ASP A 37 -18.390 -42.033 49.338 1.00 31.22 C ANISOU 303 CB ASP B 37 2717 6371 2775 1550 -200 -289 C ATOM 304 CG ASP A 37 -18.446 -42.705 50.673 1.00 37.07 C ANISOU 304 CG ASP B 37 5098 5554 3433 1042 1231 -35 C ATOM 305 OD1 ASP A 37 -19.445 -43.436 50.870 1.00 54.88 O ANISOU 305 OD1 ASP B 37 7925 5868 7058 -1213 4268 -287 O ATOM 306 OD2 ASP A 37 -17.517 -42.569 51.520 1.00 54.99 O ANISOU 306 OD2 ASP B 37 10086 6615 4192 -1246 2606 -1795 O ATOM 307 N PHE A 38 -18.352 -38.987 49.624 1.00 25.14 N ANISOU 307 N PHE B 38 2346 5067 2137 793 72 -545 N ATOM 308 CA PHE A 38 -18.127 -37.771 50.377 1.00 23.46 C ANISOU 308 CA PHE B 38 2329 4274 2309 505 -61 -562 C ATOM 309 C PHE A 38 -19.311 -36.833 50.305 1.00 23.41 C ANISOU 309 C PHE B 38 2348 4247 2298 314 133 -636 C ATOM 310 O PHE A 38 -19.722 -36.256 51.309 1.00 23.58 O ANISOU 310 O PHE B 38 2281 4232 2447 257 458 -362 O ATOM 311 CB PHE A 38 -16.862 -37.102 49.796 1.00 23.12 C ANISOU 311 CB PHE B 38 2379 4117 2290 680 -99 -130 C ATOM 312 CG PHE A 38 -16.687 -35.679 50.342 1.00 21.96 C ANISOU 312 CG PHE B 38 2374 4057 1912 544 -75 71 C ATOM 313 CD1 PHE A 38 -16.137 -35.479 51.612 1.00 23.71 C ANISOU 313 CD1 PHE B 38 3148 4349 1514 747 -5 431 C ATOM 314 CD2 PHE A 38 -17.041 -34.584 49.598 1.00 22.75 C ANISOU 314 CD2 PHE B 38 2368 4468 1808 802 -85 127 C ATOM 315 CE1 PHE A 38 -15.970 -34.200 52.090 1.00 24.46 C ANISOU 315 CE1 PHE B 38 2855 4547 1890 236 -288 491 C ATOM 316 CE2 PHE A 38 -16.922 -33.302 50.065 1.00 23.94 C ANISOU 316 CE2 PHE B 38 2353 4120 2625 574 -421 73 C ATOM 317 CZ PHE A 38 -16.386 -33.124 51.317 1.00 24.28 C ANISOU 317 CZ PHE B 38 1905 4852 2470 116 -310 268 C ATOM 318 N LEU A 39 -19.843 -36.554 49.110 1.00 23.85 N ANISOU 318 N LEU B 39 1982 4568 2513 381 122 -911 N ATOM 319 CA LEU A 39 -20.995 -35.640 49.066 1.00 22.91 C ANISOU 319 CA LEU B 39 1880 4500 2325 329 596 -815 C ATOM 320 C LEU A 39 -22.196 -36.145 49.827 1.00 26.06 C ANISOU 320 C LEU B 39 2106 5086 2707 -15 539 -635 C ATOM 321 O LEU A 39 -22.945 -35.410 50.462 1.00 28.08 O ANISOU 321 O LEU B 39 2869 4531 3268 -245 867 -682 O ATOM 322 CB LEU A 39 -21.391 -35.428 47.603 1.00 23.19 C ANISOU 322 CB LEU B 39 1864 4550 2397 265 263 -834 C ATOM 323 CG LEU A 39 -20.449 -34.629 46.728 1.00 21.38 C ANISOU 323 CG LEU B 39 1905 4245 1975 539 216 -802 C ATOM 324 CD1 LEU A 39 -20.967 -34.645 45.288 1.00 26.46 C ANISOU 324 CD1 LEU B 39 2659 5086 2308 -465 267 -1500 C ATOM 325 CD2 LEU A 39 -20.287 -33.210 47.261 1.00 24.63 C ANISOU 325 CD2 LEU B 39 1724 4349 3284 179 184 126 C ATOM 326 N ALA A 40 -22.412 -37.471 49.789 1.00 28.61 N ANISOU 326 N ALA B 40 1861 6325 2687 -70 506 -772 N ATOM 327 CA ALA A 40 -23.455 -38.051 50.635 1.00 31.53 C ANISOU 327 CA ALA B 40 2465 6357 3159 -524 1039 -1214 C ATOM 328 C ALA A 40 -23.220 -37.807 52.138 1.00 30.94 C ANISOU 328 C ALA B 40 2615 6162 2981 -211 1448 -1193 C ATOM 329 O ALA A 40 -24.153 -37.424 52.854 1.00 35.52 O ANISOU 329 O ALA B 40 2506 7297 3695 -1385 1116 -281 O ATOM 330 CB ALA A 40 -23.577 -39.545 50.410 1.00 40.06 C ANISOU 330 CB ALA B 40 1845 8591 4785 -824 742 -624 C ATOM 331 N LEU A 41 -21.989 -38.071 52.597 1.00 31.06 N ANISOU 331 N LEU B 41 2248 6195 3358 340 696 -1439 N ATOM 332 CA LEU A 41 -21.591 -37.889 53.982 1.00 30.21 C ANISOU 332 CA LEU B 41 2850 5593 3036 81 924 -882 C ATOM 333 C LEU A 41 -21.793 -36.423 54.376 1.00 30.98 C ANISOU 333 C LEU B 41 3337 5678 2758 259 912 -641 C ATOM 334 O LEU A 41 -22.183 -36.091 55.492 1.00 31.94 O ANISOU 334 O LEU B 41 3149 6393 2593 -146 675 -623 O ATOM 335 CB LEU A 41 -20.137 -38.305 54.236 1.00 32.76 C ANISOU 335 CB LEU B 41 3346 5612 3487 263 1315 -1490 C ATOM 336 CG LEU A 41 -19.732 -39.765 54.370 1.00 36.38 C ANISOU 336 CG LEU B 41 3671 5583 4569 353 2153 -457 C ATOM 337 CD1 LEU A 41 -18.212 -39.938 54.399 1.00 54.62 C ANISOU 337 CD1 LEU B 41 9561 4963 6231 -260 2084 690 C ATOM 338 CD2 LEU A 41 -20.316 -40.414 55.622 1.00 46.09 C ANISOU 338 CD2 LEU B 41 5726 6501 5287 171 3694 -1726 C ATOM 339 N GLN A 42 -21.524 -35.482 53.474 1.00 25.96 N ANISOU 339 N GLN B 42 2517 4933 2412 -129 348 -830 N ATOM 340 CA GLN A 42 -21.552 -34.074 53.916 1.00 24.72 C ANISOU 340 CA GLN B 42 2680 4325 2389 -430 379 -202 C ATOM 341 C GLN A 42 -22.750 -33.291 53.399 1.00 24.92 C ANISOU 341 C GLN B 42 2825 4325 2319 -514 731 -236 C ATOM 342 O GLN A 42 -22.683 -32.066 53.468 1.00 28.50 O ANISOU 342 O GLN B 42 2804 4449 3575 -420 1189 -105 O ATOM 343 CB GLN A 42 -20.284 -33.344 53.469 1.00 25.03 C ANISOU 343 CB GLN B 42 2536 4179 2797 -295 323 12 C ATOM 344 CG GLN A 42 -19.023 -33.960 54.033 1.00 30.37 C ANISOU 344 CG GLN B 42 3752 4924 2862 -1260 1508 -851 C ATOM 345 CD GLN A 42 -19.009 -33.946 55.550 1.00 28.37 C ANISOU 345 CD GLN B 42 2538 5350 2889 -106 1599 -578 C ATOM 346 OE1 GLN A 42 -19.608 -33.087 56.204 1.00 34.43 O ANISOU 346 OE1 GLN B 42 3815 5290 3977 -774 -643 -646 O ATOM 347 NE2 GLN A 42 -18.307 -34.949 56.073 1.00 39.22 N ANISOU 347 NE2 GLN B 42 5622 5652 3629 301 1577 -1439 N ATOM 348 N ALA A 43 -23.801 -33.941 52.900 1.00 25.65 N ANISOU 348 N ALA B 43 3129 4371 2246 -886 768 -10 N ATOM 349 CA ALA A 43 -24.973 -33.277 52.331 1.00 26.96 C ANISOU 349 CA ALA B 43 3356 4427 2461 -1059 782 -89 C ATOM 350 C ALA A 43 -25.592 -32.266 53.282 1.00 26.56 C ANISOU 350 C ALA B 43 3349 4392 2349 -437 1232 -297 C ATOM 351 O ALA A 43 -26.059 -31.190 52.905 1.00 31.08 O ANISOU 351 O ALA B 43 3740 4767 3303 -169 1438 -690 O ATOM 352 CB ALA A 43 -25.998 -34.335 51.962 1.00 29.01 C ANISOU 352 CB ALA B 43 3405 4513 3105 -1247 642 92 C ATOM 353 N GLU A 44 -25.621 -32.631 54.570 1.00 26.29 N ANISOU 353 N GLU B 44 2829 4903 2257 -177 841 -284 N ATOM 354 CA GLU A 44 -26.205 -31.734 55.561 1.00 27.28 C ANISOU 354 CA GLU B 44 3130 4793 2444 -244 964 -119 C ATOM 355 C GLU A 44 -25.218 -30.711 56.090 1.00 28.50 C ANISOU 355 C GLU B 44 2983 5028 2819 -5 755 372 C ATOM 356 O GLU A 44 -25.624 -29.868 56.899 1.00 41.21 O ANISOU 356 O GLU B 44 3895 7565 4198 -765 147 2598 O ATOM 357 CB GLU A 44 -26.755 -32.554 56.737 1.00 29.15 C ANISOU 357 CB GLU B 44 3755 4326 2996 -1154 1530 -125 C ATOM 358 CG GLU A 44 -27.956 -33.416 56.494 1.00 27.77 C ANISOU 358 CG GLU B 44 3419 3349 3784 -416 1530 -917 C ATOM 359 CD GLU A 44 -29.277 -32.725 56.241 1.00 30.88 C ANISOU 359 CD GLU B 44 3937 3318 4479 -50 776 -994 C ATOM 360 OE1 GLU A 44 -29.616 -31.773 56.978 1.00 48.33 O ANISOU 360 OE1 GLU B 44 8400 3810 6154 -672 -974 844 O ATOM 361 OE2 GLU A 44 -30.000 -33.131 55.306 1.00 39.94 O ANISOU 361 OE2 GLU B 44 4109 3920 7145 -1419 -464 -1030 O ATOM 362 N SER A 45 -23.948 -30.741 55.730 1.00 28.42 N ANISOU 362 N SER B 45 2711 5366 2722 -155 684 414 N ATOM 363 CA SER A 45 -22.999 -29.837 56.362 1.00 30.80 C ANISOU 363 CA SER B 45 3136 6339 2229 -657 598 447 C ATOM 364 C SER A 45 -22.556 -28.720 55.432 1.00 30.40 C ANISOU 364 C SER B 45 2925 5912 2715 -1016 723 249 C ATOM 365 O SER A 45 -21.987 -27.708 55.830 1.00 39.64 O ANISOU 365 O SER B 45 3059 9390 2614 -823 649 1050 O ATOM 366 CB SER A 45 -21.777 -30.627 56.842 1.00 32.79 C ANISOU 366 CB SER B 45 3417 6613 2431 -796 662 -63 C ATOM 367 OG SER A 45 -22.141 -31.759 57.599 1.00 34.87 O ANISOU 367 OG SER B 45 4112 6753 2382 -1218 1261 -265 O ATOM 368 N ILE A 46 -22.758 -28.854 54.126 1.00 24.59 N ANISOU 368 N ILE B 46 2588 4075 2679 -83 838 219 N ATOM 369 CA ILE A 46 -22.136 -27.881 53.223 1.00 21.49 C ANISOU 369 CA ILE B 46 1880 3639 2644 -176 376 -45 C ATOM 370 C ILE A 46 -23.121 -26.789 52.878 1.00 21.47 C ANISOU 370 C ILE B 46 2004 3397 2759 -322 353 107 C ATOM 371 O ILE A 46 -24.208 -27.052 52.353 1.00 21.78 O ANISOU 371 O ILE B 46 2099 3348 2827 -403 180 392 O ATOM 372 CB ILE A 46 -21.602 -28.623 51.974 1.00 21.84 C ANISOU 372 CB ILE B 46 2164 3458 2675 -23 878 99 C ATOM 373 CG1 ILE A 46 -20.418 -29.547 52.275 1.00 23.78 C ANISOU 373 CG1 ILE B 46 2522 3670 2843 435 1035 -146 C ATOM 374 CG2 ILE A 46 -21.259 -27.603 50.904 1.00 21.54 C ANISOU 374 CG2 ILE B 46 2168 3028 2988 219 977 50 C ATOM 375 CD1 ILE A 46 -20.118 -30.606 51.228 1.00 24.64 C ANISOU 375 CD1 ILE B 46 2775 3290 3297 -140 521 31 C ATOM 376 N ARG A 47 -22.768 -25.547 53.177 1.00 20.32 N ANISOU 376 N ARG B 47 2071 3100 2549 -344 391 15 N ATOM 377 CA ARG A 47 -23.655 -24.406 52.946 1.00 20.74 C ANISOU 377 CA ARG B 47 2564 3147 2170 -102 674 477 C ATOM 378 C ARG A 47 -23.142 -23.469 51.869 1.00 18.71 C ANISOU 378 C ARG B 47 2200 2716 2193 -268 448 393 C ATOM 379 O ARG A 47 -23.883 -22.565 51.471 1.00 21.04 O ANISOU 379 O ARG B 47 2437 2769 2787 -64 892 514 O ATOM 380 CB ARG A 47 -23.908 -23.645 54.266 1.00 22.37 C ANISOU 380 CB ARG B 47 2263 3954 2282 31 592 533 C ATOM 381 CG ARG A 47 -24.782 -24.464 55.214 1.00 24.94 C ANISOU 381 CG ARG B 47 3333 3991 2151 -279 1010 588 C ATOM 382 CD ARG A 47 -24.853 -23.792 56.567 1.00 28.16 C ANISOU 382 CD ARG B 47 3517 4668 2516 -254 622 887 C ATOM 383 NE ARG A 47 -25.616 -22.548 56.535 1.00 28.87 N ANISOU 383 NE ARG B 47 4190 4234 2544 -453 484 947 N ATOM 384 CZ ARG A 47 -25.559 -21.635 57.495 1.00 32.13 C ANISOU 384 CZ ARG B 47 5519 4331 2359 41 538 1509 C ATOM 385 NH1 ARG A 47 -24.804 -21.767 58.571 1.00 31.26 N ANISOU 385 NH1 ARG B 47 4680 4791 2406 -624 281 1620 N ATOM 386 NH2 ARG A 47 -26.296 -20.552 57.347 1.00 44.36 N ANISOU 386 NH2 ARG B 47 8753 4349 3752 1044 76 1853 N ATOM 387 N ALA A 48 -21.917 -23.666 51.403 1.00 20.58 N ANISOU 387 N ALA B 48 2656 2714 2450 -499 645 192 N ATOM 388 CA ALA A 48 -21.277 -22.858 50.368 1.00 17.97 C ANISOU 388 CA ALA B 48 2125 2358 2347 -394 394 225 C ATOM 389 C ALA A 48 -20.323 -23.680 49.531 1.00 16.98 C ANISOU 389 C ALA B 48 1934 2469 2047 -266 247 42 C ATOM 390 O ALA A 48 -19.723 -24.611 50.039 1.00 17.62 O ANISOU 390 O ALA B 48 2308 2518 1870 -101 382 183 O ATOM 391 CB ALA A 48 -20.503 -21.693 50.978 1.00 19.27 C ANISOU 391 CB ALA B 48 2380 2241 2701 -120 37 213 C ATOM 392 N VAL A 49 -20.233 -23.275 48.274 1.00 16.47 N ANISOU 392 N VAL B 49 2152 2087 2020 -463 243 -118 N ATOM 393 CA VAL A 49 -19.271 -23.808 47.325 1.00 15.58 C ANISOU 393 CA VAL B 49 1907 2023 1991 -210 315 -172 C ATOM 394 C VAL A 49 -18.406 -22.655 46.830 1.00 16.72 C ANISOU 394 C VAL B 49 1938 2195 2219 14 483 78 C ATOM 395 O VAL A 49 -18.932 -21.567 46.535 1.00 17.05 O ANISOU 395 O VAL B 49 2000 2075 2405 17 310 139 O ATOM 396 CB VAL A 49 -19.967 -24.507 46.157 1.00 15.97 C ANISOU 396 CB VAL B 49 2089 2084 1895 -142 349 -279 C ATOM 397 CG1 VAL A 49 -18.985 -24.696 45.000 1.00 19.29 C ANISOU 397 CG1 VAL B 49 2461 2867 2001 -147 396 77 C ATOM 398 CG2 VAL A 49 -20.578 -25.841 46.590 1.00 17.79 C ANISOU 398 CG2 VAL B 49 1946 2787 2027 -276 161 -100 C ATOM 399 N VAL A 50 -17.100 -22.893 46.764 1.00 14.73 N ANISOU 399 N VAL B 50 1467 2115 2017 128 190 30 N ATOM 400 CA VAL A 50 -16.162 -21.957 46.141 1.00 14.46 C ANISOU 400 CA VAL B 50 1306 2456 1731 54 -123 122 C ATOM 401 C VAL A 50 -15.622 -22.652 44.888 1.00 14.72 C ANISOU 401 C VAL B 50 1514 2390 1687 184 -63 44 C ATOM 402 O VAL A 50 -15.050 -23.744 44.956 1.00 15.35 O ANISOU 402 O VAL B 50 1655 2229 1948 163 84 78 O ATOM 403 CB VAL A 50 -15.053 -21.506 47.107 1.00 14.35 C ANISOU 403 CB VAL B 50 1702 2132 1618 -52 -16 63 C ATOM 404 CG1 VAL A 50 -13.945 -20.760 46.419 1.00 15.48 C ANISOU 404 CG1 VAL B 50 1739 2016 2127 -147 -11 198 C ATOM 405 CG2 VAL A 50 -15.643 -20.663 48.255 1.00 14.94 C ANISOU 405 CG2 VAL B 50 1879 2554 1242 47 -17 -7 C ATOM 406 N GLY A 51 -15.826 -22.021 43.728 1.00 14.99 N ANISOU 406 N GLY B 51 1987 1957 1753 75 -69 -6 N ATOM 407 CA GLY A 51 -15.425 -22.505 42.428 1.00 15.92 C ANISOU 407 CA GLY B 51 1780 2610 1658 339 -38 -21 C ATOM 408 C GLY A 51 -14.498 -21.517 41.766 1.00 16.21 C ANISOU 408 C GLY B 51 1892 2752 1515 163 65 -302 C ATOM 409 O GLY A 51 -14.185 -20.462 42.299 1.00 16.31 O ANISOU 409 O GLY B 51 1807 2478 1914 124 53 -190 O ATOM 410 N ASN A 52 -14.104 -21.875 40.558 1.00 17.49 N ANISOU 410 N ASN B 52 2115 2627 1902 453 268 110 N ATOM 411 CA ASN A 52 -13.329 -21.009 39.684 1.00 18.79 C ANISOU 411 CA ASN B 52 2297 2570 2274 839 701 224 C ATOM 412 C ASN A 52 -13.683 -21.393 38.244 1.00 21.07 C ANISOU 412 C ASN B 52 3407 2486 2112 618 753 480 C ATOM 413 O ASN A 52 -14.709 -22.008 37.973 1.00 24.81 O ANISOU 413 O ASN B 52 4290 3047 2091 202 204 -98 O ATOM 414 CB ASN A 52 -11.843 -21.079 39.944 1.00 20.34 C ANISOU 414 CB ASN B 52 2107 2857 2763 588 397 542 C ATOM 415 CG ASN A 52 -11.174 -22.328 39.409 1.00 17.77 C ANISOU 415 CG ASN B 52 2095 2586 2072 326 431 516 C ATOM 416 OD1 ASN A 52 -11.845 -23.318 39.096 1.00 18.22 O ANISOU 416 OD1 ASN B 52 2289 2448 2185 382 0 240 O ATOM 417 ND2 ASN A 52 -9.872 -22.323 39.312 1.00 21.06 N ANISOU 417 ND2 ASN B 52 2759 2994 2248 -246 -45 762 N ATOM 418 N SER A 53 -12.846 -21.056 37.274 1.00 27.38 N ANISOU 418 N SER B 53 4897 2994 2510 974 1918 445 N ATOM 419 CA SER A 53 -13.259 -21.195 35.866 1.00 31.55 C ANISOU 419 CA SER B 53 5868 3597 2524 -164 2251 83 C ATOM 420 C SER A 53 -13.135 -22.655 35.416 1.00 31.53 C ANISOU 420 C SER B 53 5637 3814 2529 -947 751 -202 C ATOM 421 O SER A 53 -13.620 -23.040 34.358 1.00 42.96 O ANISOU 421 O SER B 53 8894 4759 2671 -921 -195 -545 O ATOM 422 CB SER A 53 -12.496 -20.294 34.901 1.00 44.62 C ANISOU 422 CB SER B 53 6919 6689 3347 -215 3319 -179 C ATOM 423 OG SER A 53 -11.107 -20.248 35.140 1.00 63.62 O ANISOU 423 OG SER B 53 8514 11546 4113 -4600 3586 -393 O ATOM 424 N ASN A 54 -12.474 -23.434 36.278 1.00 25.26 N ANISOU 424 N ASN B 54 4032 3252 2313 -606 5 194 N ATOM 425 CA ASN A 54 -12.253 -24.838 35.933 1.00 28.13 C ANISOU 425 CA ASN B 54 4139 3769 2781 -773 -710 776 C ATOM 426 C ASN A 54 -13.240 -25.796 36.600 1.00 25.53 C ANISOU 426 C ASN B 54 3865 3179 2654 -394 -784 614 C ATOM 427 O ASN A 54 -13.490 -26.864 36.024 1.00 30.83 O ANISOU 427 O ASN B 54 4060 4305 3349 -719 -1226 1281 O ATOM 428 CB ASN A 54 -10.798 -25.175 36.234 1.00 37.12 C ANISOU 428 CB ASN B 54 4892 3144 6068 -846 -2089 2135 C ATOM 429 CG ASN A 54 -9.807 -24.514 35.289 1.00 44.38 C ANISOU 429 CG ASN B 54 5742 5305 5814 -2092 -2709 3362 C ATOM 430 OD1 ASN A 54 -9.737 -24.738 34.079 1.00 51.50 O ANISOU 430 OD1 ASN B 54 8526 5913 5129 -2213 -2258 1706 O ATOM 431 ND2 ASN A 54 -8.980 -23.628 35.835 1.00 57.23 N ANISOU 431 ND2 ASN B 54 5738 8360 7648 -3078 -2867 3626 N ATOM 432 N ALA A 55 -13.758 -25.408 37.750 1.00 22.46 N ANISOU 432 N ALA B 55 3284 2879 2369 -261 -674 195 N ATOM 433 CA ALA A 55 -14.719 -26.202 38.487 1.00 21.14 C ANISOU 433 CA ALA B 55 3238 2475 2317 382 -345 -10 C ATOM 434 C ALA A 55 -15.709 -25.306 39.220 1.00 17.88 C ANISOU 434 C ALA B 55 2510 2337 1948 90 -482 -236 C ATOM 435 O ALA A 55 -15.305 -24.473 39.991 1.00 19.99 O ANISOU 435 O ALA B 55 2388 2672 2536 -307 -624 223 O ATOM 436 CB ALA A 55 -13.997 -27.113 39.467 1.00 28.23 C ANISOU 436 CB ALA B 55 5487 2680 2561 1054 -148 -24 C ATOM 437 N GLY A 56 -16.992 -25.471 38.930 1.00 19.62 N ANISOU 437 N GLY B 56 2424 2595 2437 -3 -536 -288 N ATOM 438 CA GLY A 56 -18.040 -24.675 39.513 1.00 20.80 C ANISOU 438 CA GLY B 56 2266 2527 3109 -175 93 -69 C ATOM 439 C GLY A 56 -19.074 -25.520 40.228 1.00 19.49 C ANISOU 439 C GLY B 56 1768 2530 3109 82 -33 -480 C ATOM 440 O GLY A 56 -18.755 -26.305 41.093 1.00 22.49 O ANISOU 440 O GLY B 56 2702 2579 3262 207 355 -451 O ATOM 441 N ALA A 57 -20.330 -25.316 39.845 1.00 19.58 N ANISOU 441 N ALA B 57 1832 2430 3176 32 -42 -351 N ATOM 442 CA ALA A 57 -21.444 -25.988 40.481 1.00 19.56 C ANISOU 442 CA ALA B 57 1883 2892 2656 -217 -106 -715 C ATOM 443 C ALA A 57 -22.519 -26.211 39.418 1.00 19.81 C ANISOU 443 C ALA B 57 2051 2688 2786 -53 -268 -744 C ATOM 444 O ALA A 57 -23.190 -25.281 39.024 1.00 21.42 O ANISOU 444 O ALA B 57 2275 2652 3214 -45 -394 -779 O ATOM 445 CB ALA A 57 -22.004 -25.194 41.656 1.00 21.10 C ANISOU 445 CB ALA B 57 1998 3467 2551 -338 -4 -443 C ATOM 446 N ASP A 58 -22.645 -27.440 38.947 1.00 21.19 N ANISOU 446 N ASP B 58 1998 3207 2848 73 -304 -915 N ATOM 447 CA ASP A 58 -23.648 -27.779 37.958 1.00 20.65 C ANISOU 447 CA ASP B 58 2390 2892 2567 -101 -420 -457 C ATOM 448 C ASP A 58 -24.910 -28.285 38.679 1.00 21.25 C ANISOU 448 C ASP B 58 2399 2928 2748 -143 -233 -577 C ATOM 449 O ASP A 58 -24.919 -28.344 39.906 1.00 21.83 O ANISOU 449 O ASP B 58 2094 3399 2801 -173 299 -1196 O ATOM 450 CB ASP A 58 -23.142 -28.797 36.956 1.00 21.89 C ANISOU 450 CB ASP B 58 2269 3341 2709 310 -168 -255 C ATOM 451 CG ASP A 58 -22.784 -30.140 37.512 1.00 25.60 C ANISOU 451 CG ASP B 58 3070 3561 3097 677 305 -141 C ATOM 452 OD1 ASP A 58 -23.179 -30.473 38.638 1.00 26.24 O ANISOU 452 OD1 ASP B 58 2425 4740 2806 312 -69 -559 O ATOM 453 OD2 ASP A 58 -22.098 -30.881 36.778 1.00 28.22 O ANISOU 453 OD2 ASP B 58 2983 3494 4247 669 324 219 O ATOM 454 N ALA A 59 -25.934 -28.637 37.896 1.00 23.93 N ANISOU 454 N ALA B 59 2674 3409 3010 -458 -463 -545 N ATOM 455 CA ALA A 59 -27.208 -28.988 38.518 1.00 25.00 C ANISOU 455 CA ALA B 59 2746 3478 3276 -623 -228 -915 C ATOM 456 C ALA A 59 -27.100 -30.167 39.464 1.00 24.81 C ANISOU 456 C ALA B 59 2554 3776 3095 -570 -434 -1007 C ATOM 457 O ALA A 59 -27.762 -30.229 40.519 1.00 26.43 O ANISOU 457 O ALA B 59 3029 3774 3238 -565 -155 -937 O ATOM 458 CB ALA A 59 -28.211 -29.262 37.407 1.00 30.93 C ANISOU 458 CB ALA B 59 2521 5333 3899 -1129 203 -2086 C ATOM 459 N GLU A 60 -26.248 -31.115 39.054 1.00 25.97 N ANISOU 459 N GLU B 60 2315 4109 3444 -282 -85 -662 N ATOM 460 CA GLU A 60 -26.153 -32.334 39.859 1.00 25.64 C ANISOU 460 CA GLU B 60 2151 4394 3195 -223 -281 -767 C ATOM 461 C GLU A 60 -25.509 -32.063 41.212 1.00 23.28 C ANISOU 461 C GLU B 60 2474 3502 2870 -700 -239 -71 C ATOM 462 O GLU A 60 -25.856 -32.596 42.265 1.00 24.27 O ANISOU 462 O GLU B 60 2155 3905 3161 -211 -18 -526 O ATOM 463 CB GLU A 60 -25.335 -33.398 39.115 1.00 29.50 C ANISOU 463 CB GLU B 60 3083 5221 2904 678 -747 -867 C ATOM 464 CG GLU A 60 -25.475 -34.806 39.677 1.00 43.06 C ANISOU 464 CG GLU B 60 4752 5417 6190 1831 406 -1623 C ATOM 465 CD GLU A 60 -24.649 -35.908 39.092 1.00 46.18 C ANISOU 465 CD GLU B 60 4984 6491 6072 2113 519 -521 C ATOM 466 OE1 GLU A 60 -23.962 -35.858 38.034 1.00 60.73 O ANISOU 466 OE1 GLU B 60 8888 8073 6114 -4559 -2405 115 O ATOM 467 OE2 GLU A 60 -24.625 -37.025 39.697 1.00 60.91 O ANISOU 467 OE2 GLU B 60 5432 7206 10506 3263 -1192 -4593 O ATOM 468 N LEU A 61 -24.512 -31.177 41.213 1.00 21.58 N ANISOU 468 N LEU B 61 2091 3188 2920 -84 -59 -804 N ATOM 469 CA LEU A 61 -23.887 -30.847 42.474 1.00 20.27 C ANISOU 469 CA LEU B 61 1915 3346 2442 -233 324 -625 C ATOM 470 C LEU A 61 -24.852 -30.094 43.366 1.00 21.80 C ANISOU 470 C LEU B 61 2541 3004 2738 -689 0 -715 C ATOM 471 O LEU A 61 -24.911 -30.307 44.573 1.00 21.17 O ANISOU 471 O LEU B 61 2017 3291 2734 -548 227 -411 O ATOM 472 CB LEU A 61 -22.628 -30.008 42.229 1.00 19.41 C ANISOU 472 CB LEU B 61 2043 2924 2407 -212 281 -762 C ATOM 473 CG LEU A 61 -21.854 -29.669 43.509 1.00 20.51 C ANISOU 473 CG LEU B 61 2077 3277 2439 -272 596 -1310 C ATOM 474 CD1 LEU A 61 -21.135 -30.927 44.000 1.00 20.01 C ANISOU 474 CD1 LEU B 61 2576 2827 2200 39 182 -673 C ATOM 475 CD2 LEU A 61 -20.898 -28.502 43.332 1.00 23.22 C ANISOU 475 CD2 LEU B 61 1977 3702 3143 -274 135 -641 C ATOM 476 N ILE A 62 -25.608 -29.179 42.789 1.00 22.11 N ANISOU 476 N ILE B 62 2216 3334 2852 -216 -154 -698 N ATOM 477 CA ILE A 62 -26.546 -28.372 43.582 1.00 21.49 C ANISOU 477 CA ILE B 62 1565 3392 3207 -52 -69 -582 C ATOM 478 C ILE A 62 -27.571 -29.291 44.223 1.00 22.45 C ANISOU 478 C ILE B 62 1914 3363 3252 -543 114 -1033 C ATOM 479 O ILE A 62 -27.885 -29.115 45.400 1.00 25.19 O ANISOU 479 O ILE B 62 2187 3519 3864 -484 95 7 O ATOM 480 CB ILE A 62 -27.135 -27.273 42.659 1.00 23.63 C ANISOU 480 CB ILE B 62 2191 3465 3324 -74 298 -554 C ATOM 481 CG1 ILE A 62 -26.084 -26.258 42.230 1.00 24.39 C ANISOU 481 CG1 ILE B 62 2364 3466 3437 -526 553 -1448 C ATOM 482 CG2 ILE A 62 -28.363 -26.615 43.264 1.00 25.25 C ANISOU 482 CG2 ILE B 62 2129 3132 4333 -339 -229 -742 C ATOM 483 CD1 ILE A 62 -26.423 -25.375 41.043 1.00 21.90 C ANISOU 483 CD1 ILE B 62 2878 2573 2870 -178 517 -639 C ATOM 484 N ASP A 63 -28.056 -30.259 43.443 1.00 24.97 N ANISOU 484 N ASP B 63 1681 4419 3386 -685 217 -923 N ATOM 485 CA ASP A 63 -29.039 -31.234 43.916 1.00 24.47 C ANISOU 485 CA ASP B 63 1553 3618 4128 128 509 -263 C ATOM 486 C ASP A 63 -28.436 -32.070 45.025 1.00 26.82 C ANISOU 486 C ASP B 63 1760 3963 4469 -591 766 -724 C ATOM 487 O ASP A 63 -29.126 -32.526 45.939 1.00 31.66 O ANISOU 487 O ASP B 63 3164 4540 4325 -1454 1211 -1198 O ATOM 488 CB ASP A 63 -29.527 -32.131 42.768 1.00 28.01 C ANISOU 488 CB ASP B 63 1438 4496 4709 -320 211 -750 C ATOM 489 CG ASP A 63 -30.574 -31.570 41.836 1.00 39.88 C ANISOU 489 CG ASP B 63 4275 5446 5431 -1458 399 -1627 C ATOM 490 OD1 ASP A 63 -31.308 -30.611 42.209 1.00 43.38 O ANISOU 490 OD1 ASP B 63 5453 4280 6749 -1905 1610 -1753 O ATOM 491 OD2 ASP A 63 -30.757 -32.079 40.690 1.00 45.36 O ANISOU 491 OD2 ASP B 63 3365 8513 5358 -2133 536 -2217 O ATOM 492 N ALA A 64 -27.109 -32.277 44.936 1.00 25.67 N ANISOU 492 N ALA B 64 2282 3874 3597 -536 49 -395 N ATOM 493 CA ALA A 64 -26.456 -33.102 45.953 1.00 24.94 C ANISOU 493 CA ALA B 64 2235 3906 3334 -933 284 -361 C ATOM 494 C ALA A 64 -26.176 -32.381 47.264 1.00 24.16 C ANISOU 494 C ALA B 64 2510 3539 3132 -540 451 140 C ATOM 495 O ALA A 64 -25.764 -32.999 48.264 1.00 24.42 O ANISOU 495 O ALA B 64 2302 4130 2846 -313 605 282 O ATOM 496 CB ALA A 64 -25.162 -33.677 45.387 1.00 23.50 C ANISOU 496 CB ALA B 64 2581 3936 2410 -276 136 -337 C ATOM 497 N LEU A 65 -26.386 -31.079 47.283 1.00 24.54 N ANISOU 497 N LEU B 65 2066 3834 3426 -714 614 -161 N ATOM 498 CA LEU A 65 -26.066 -30.178 48.382 1.00 21.75 C ANISOU 498 CA LEU B 65 1924 3181 3158 -420 759 -621 C ATOM 499 C LEU A 65 -27.318 -29.412 48.808 1.00 23.14 C ANISOU 499 C LEU B 65 2118 3195 3478 -604 663 -512 C ATOM 500 O LEU A 65 -27.516 -28.222 48.552 1.00 24.39 O ANISOU 500 O LEU B 65 2103 3065 4098 -539 722 -312 O ATOM 501 CB LEU A 65 -24.949 -29.197 48.018 1.00 21.85 C ANISOU 501 CB LEU B 65 1992 3354 2958 -516 697 -263 C ATOM 502 CG LEU A 65 -23.618 -29.806 47.636 1.00 21.30 C ANISOU 502 CG LEU B 65 2095 3485 2512 -418 370 30 C ATOM 503 CD1 LEU A 65 -22.619 -28.712 47.290 1.00 22.85 C ANISOU 503 CD1 LEU B 65 2205 3227 3250 -462 573 163 C ATOM 504 CD2 LEU A 65 -23.074 -30.673 48.771 1.00 22.29 C ANISOU 504 CD2 LEU B 65 2497 3283 2689 -66 325 68 C ATOM 505 N PRO A 66 -28.219 -30.151 49.448 1.00 24.35 N ANISOU 505 N PRO B 66 2117 3670 3464 -448 635 -24 N ATOM 506 CA PRO A 66 -29.535 -29.564 49.742 1.00 26.87 C ANISOU 506 CA PRO B 66 1866 3755 4588 -666 793 71 C ATOM 507 C PRO A 66 -29.486 -28.384 50.692 1.00 27.54 C ANISOU 507 C PRO B 66 2612 3459 4392 -706 660 404 C ATOM 508 O PRO A 66 -30.414 -27.575 50.753 1.00 30.52 O ANISOU 508 O PRO B 66 3741 3434 4423 -559 774 454 O ATOM 509 CB PRO A 66 -30.312 -30.726 50.367 1.00 30.60 C ANISOU 509 CB PRO B 66 2326 3923 5377 -652 1537 -366 C ATOM 510 CG PRO A 66 -29.297 -31.736 50.794 1.00 28.56 C ANISOU 510 CG PRO B 66 2691 3906 4254 -836 1226 -455 C ATOM 511 CD PRO A 66 -28.129 -31.556 49.886 1.00 25.98 C ANISOU 511 CD PRO B 66 2244 3937 3690 -447 869 -235 C ATOM 512 N LYS A 67 -28.405 -28.223 51.429 1.00 26.75 N ANISOU 512 N LYS B 67 2522 3535 4106 -521 567 462 N ATOM 513 CA LYS A 67 -28.289 -27.058 52.320 1.00 26.43 C ANISOU 513 CA LYS B 67 2568 3716 3758 -316 838 588 C ATOM 514 C LYS A 67 -27.471 -25.942 51.703 1.00 22.66 C ANISOU 514 C LYS B 67 2514 2671 3426 -268 755 256 C ATOM 515 O LYS A 67 -27.132 -24.998 52.395 1.00 22.89 O ANISOU 515 O LYS B 67 2553 2879 3265 -386 826 650 O ATOM 516 CB LYS A 67 -27.641 -27.489 53.655 1.00 29.92 C ANISOU 516 CB LYS B 67 3285 4922 3162 -657 1349 751 C ATOM 517 CG LYS A 67 -28.322 -28.646 54.338 1.00 33.08 C ANISOU 517 CG LYS B 67 2653 5248 4667 -203 1132 -293 C ATOM 518 CD LYS A 67 -29.840 -28.450 54.326 1.00 36.74 C ANISOU 518 CD LYS B 67 3099 6138 4720 -1369 1449 -209 C ATOM 519 CE LYS A 67 -30.565 -29.616 54.988 1.00 38.30 C ANISOU 519 CE LYS B 67 3286 6727 4539 -1257 1639 -1230 C ATOM 520 NZ LYS A 67 -31.071 -29.114 56.295 1.00 52.32 N ANISOU 520 NZ LYS B 67 7204 7143 5532 -2631 2639 374 N ATOM 521 N LEU A 68 -27.142 -26.045 50.421 1.00 22.67 N ANISOU 521 N LEU B 68 1924 3330 3361 -481 437 146 N ATOM 522 CA LEU A 68 -26.372 -25.030 49.702 1.00 19.40 C ANISOU 522 CA LEU B 68 1984 2646 2742 -191 377 -337 C ATOM 523 C LEU A 68 -27.081 -23.674 49.767 1.00 21.26 C ANISOU 523 C LEU B 68 2302 2358 3419 -351 473 402 C ATOM 524 O LEU A 68 -28.262 -23.618 49.436 1.00 22.66 O ANISOU 524 O LEU B 68 3213 2394 3004 -628 685 278 O ATOM 525 CB LEU A 68 -26.142 -25.430 48.250 1.00 21.14 C ANISOU 525 CB LEU B 68 1796 3011 3224 -432 83 445 C ATOM 526 CG LEU A 68 -25.205 -24.526 47.426 1.00 19.91 C ANISOU 526 CG LEU B 68 1930 2947 2687 -433 192 -194 C ATOM 527 CD1 LEU A 68 -23.842 -24.352 48.103 1.00 19.74 C ANISOU 527 CD1 LEU B 68 1848 2710 2941 -393 187 -50 C ATOM 528 CD2 LEU A 68 -25.044 -25.100 46.016 1.00 20.13 C ANISOU 528 CD2 LEU B 68 2264 2529 2855 -324 100 -93 C ATOM 529 N GLU A 69 -26.334 -22.628 50.133 1.00 22.17 N ANISOU 529 N GLU B 69 2224 2743 3455 -140 437 929 N ATOM 530 CA GLU A 69 -26.928 -21.304 50.142 1.00 20.85 C ANISOU 530 CA GLU B 69 2353 2387 3182 -379 487 718 C ATOM 531 C GLU A 69 -26.270 -20.316 49.188 1.00 19.73 C ANISOU 531 C GLU B 69 2477 2044 2976 -569 497 93 C ATOM 532 O GLU A 69 -26.907 -19.356 48.778 1.00 22.07 O ANISOU 532 O GLU B 69 2587 2132 3665 -129 256 211 O ATOM 533 CB GLU A 69 -26.871 -20.688 51.543 1.00 21.67 C ANISOU 533 CB GLU B 69 2376 2718 3138 96 595 724 C ATOM 534 CG GLU A 69 -27.590 -21.487 52.601 1.00 25.19 C ANISOU 534 CG GLU B 69 2767 3544 3259 -370 758 896 C ATOM 535 CD GLU A 69 -27.508 -20.921 54.002 1.00 25.96 C ANISOU 535 CD GLU B 69 3090 3669 3106 -301 783 539 C ATOM 536 OE1 GLU A 69 -27.088 -19.773 54.222 1.00 28.38 O ANISOU 536 OE1 GLU B 69 3236 4130 3415 -244 526 1216 O ATOM 537 OE2 GLU A 69 -27.930 -21.694 54.899 1.00 31.67 O ANISOU 537 OE2 GLU B 69 3729 5028 3275 -380 1195 412 O ATOM 538 N ILE A 70 -25.001 -20.565 48.846 1.00 18.57 N ANISOU 538 N ILE B 70 2124 2129 2802 -441 324 316 N ATOM 539 CA ILE A 70 -24.241 -19.622 48.066 1.00 17.87 C ANISOU 539 CA ILE B 70 2003 2272 2514 -209 270 345 C ATOM 540 C ILE A 70 -23.081 -20.314 47.395 1.00 16.83 C ANISOU 540 C ILE B 70 1993 2211 2191 -247 264 220 C ATOM 541 O ILE A 70 -22.420 -21.186 47.975 1.00 17.53 O ANISOU 541 O ILE B 70 2147 2247 2266 -263 537 268 O ATOM 542 CB ILE A 70 -23.724 -18.439 48.920 1.00 18.57 C ANISOU 542 CB ILE B 70 2191 2406 2458 -174 151 346 C ATOM 543 CG1 ILE A 70 -22.958 -17.393 48.114 1.00 19.29 C ANISOU 543 CG1 ILE B 70 1926 2270 3133 125 226 212 C ATOM 544 CG2 ILE A 70 -22.868 -18.911 50.076 1.00 18.86 C ANISOU 544 CG2 ILE B 70 2106 2305 2754 -301 191 219 C ATOM 545 CD1 ILE A 70 -22.663 -16.100 48.834 1.00 18.93 C ANISOU 545 CD1 ILE B 70 2288 1941 2965 225 11 190 C ATOM 546 N VAL A 71 -22.870 -19.923 46.141 1.00 16.83 N ANISOU 546 N VAL B 71 2307 1926 2160 -340 185 -4 N ATOM 547 CA VAL A 71 -21.756 -20.318 45.310 1.00 15.80 C ANISOU 547 CA VAL B 71 1692 2188 2125 -147 93 260 C ATOM 548 C VAL A 71 -20.975 -19.016 45.052 1.00 16.24 C ANISOU 548 C VAL B 71 1716 1809 2645 -23 212 -69 C ATOM 549 O VAL A 71 -21.523 -18.113 44.432 1.00 16.66 O ANISOU 549 O VAL B 71 2055 1921 2352 -31 296 -69 O ATOM 550 CB VAL A 71 -22.162 -20.939 43.971 1.00 15.57 C ANISOU 550 CB VAL B 71 1880 1893 2142 56 97 -128 C ATOM 551 CG1 VAL A 71 -20.939 -21.203 43.084 1.00 17.85 C ANISOU 551 CG1 VAL B 71 2690 2164 1930 -183 -179 -6 C ATOM 552 CG2 VAL A 71 -22.989 -22.192 44.201 1.00 18.83 C ANISOU 552 CG2 VAL B 71 1841 2935 2378 -43 -73 -243 C ATOM 553 N SER A 72 -19.757 -18.988 45.582 1.00 16.29 N ANISOU 553 N SER B 72 1722 2107 2360 -214 512 -182 N ATOM 554 CA SER A 72 -18.863 -17.876 45.379 1.00 15.55 C ANISOU 554 CA SER B 72 1772 2025 2111 -175 299 -210 C ATOM 555 C SER A 72 -17.727 -18.274 44.447 1.00 14.10 C ANISOU 555 C SER B 72 1239 1964 2153 28 218 -77 C ATOM 556 O SER A 72 -16.929 -19.127 44.818 1.00 17.79 O ANISOU 556 O SER B 72 1940 2054 2765 64 748 -214 O ATOM 557 CB SER A 72 -18.358 -17.270 46.692 1.00 16.10 C ANISOU 557 CB SER B 72 1959 2152 2007 -175 337 71 C ATOM 558 OG SER A 72 -19.420 -16.646 47.403 1.00 18.22 O ANISOU 558 OG SER B 72 1936 2300 2688 -39 208 391 O ATOM 559 N SER A 73 -17.703 -17.659 43.270 1.00 15.48 N ANISOU 559 N SER B 73 1713 1892 2277 62 320 -91 N ATOM 560 CA SER A 73 -16.692 -18.021 42.295 1.00 15.30 C ANISOU 560 CA SER B 73 1711 2042 2059 -2 241 -167 C ATOM 561 C SER A 73 -15.483 -17.083 42.318 1.00 14.60 C ANISOU 561 C SER B 73 1647 1893 2006 139 374 -140 C ATOM 562 O SER A 73 -15.614 -15.844 42.397 1.00 15.89 O ANISOU 562 O SER B 73 1686 2075 2277 245 210 45 O ATOM 563 CB SER A 73 -17.297 -18.092 40.882 1.00 16.91 C ANISOU 563 CB SER B 73 1893 2347 2184 408 77 -450 C ATOM 564 OG SER A 73 -16.472 -18.980 40.165 1.00 19.76 O ANISOU 564 OG SER B 73 2305 2806 2395 156 58 181 O ATOM 565 N PHE A 74 -14.309 -17.715 42.246 1.00 14.68 N ANISOU 565 N PHE B 74 1742 1923 1915 83 188 23 N ATOM 566 CA PHE A 74 -13.023 -17.073 42.138 1.00 14.10 C ANISOU 566 CA PHE B 74 1714 1913 1732 87 268 -10 C ATOM 567 C PHE A 74 -12.713 -16.871 40.656 1.00 14.52 C ANISOU 567 C PHE B 74 1608 2076 1833 399 349 35 C ATOM 568 O PHE A 74 -11.778 -17.456 40.110 1.00 16.27 O ANISOU 568 O PHE B 74 2431 2082 1671 154 199 9 O ATOM 569 CB PHE A 74 -12.007 -17.946 42.825 1.00 13.68 C ANISOU 569 CB PHE B 74 1535 1893 1771 130 226 53 C ATOM 570 CG PHE A 74 -10.569 -17.474 42.970 1.00 15.14 C ANISOU 570 CG PHE B 74 1909 1956 1888 -152 -11 301 C ATOM 571 CD1 PHE A 74 -10.226 -16.406 43.794 1.00 13.68 C ANISOU 571 CD1 PHE B 74 1620 1785 1792 100 187 147 C ATOM 572 CD2 PHE A 74 -9.552 -18.155 42.304 1.00 15.02 C ANISOU 572 CD2 PHE B 74 1759 2052 1896 -6 41 327 C ATOM 573 CE1 PHE A 74 -8.899 -16.083 43.984 1.00 14.99 C ANISOU 573 CE1 PHE B 74 1740 1700 2256 154 52 72 C ATOM 574 CE2 PHE A 74 -8.220 -17.803 42.462 1.00 15.76 C ANISOU 574 CE2 PHE B 74 1953 1788 2249 -1 -94 242 C ATOM 575 CZ PHE A 74 -7.891 -16.766 43.327 1.00 13.82 C ANISOU 575 CZ PHE B 74 1513 1772 1965 134 267 110 C ATOM 576 N SER A 75 -13.592 -16.044 40.050 1.00 15.51 N ANISOU 576 N SER B 75 1806 2187 1898 535 497 26 N ATOM 577 CA SER A 75 -13.540 -15.787 38.623 1.00 16.57 C ANISOU 577 CA SER B 75 2350 2192 1754 142 73 -210 C ATOM 578 C SER A 75 -14.559 -14.716 38.274 1.00 16.63 C ANISOU 578 C SER B 75 2398 2213 1708 101 87 -226 C ATOM 579 O SER A 75 -15.518 -14.532 39.017 1.00 16.93 O ANISOU 579 O SER B 75 2122 2285 2024 16 124 -96 O ATOM 580 CB SER A 75 -13.808 -17.039 37.800 1.00 19.94 C ANISOU 580 CB SER B 75 2893 2288 2397 343 -697 -964 C ATOM 581 OG SER A 75 -15.143 -17.432 37.793 1.00 22.35 O ANISOU 581 OG SER B 75 2516 2878 3098 270 -250 -949 O ATOM 582 N VAL A 76 -14.363 -14.082 37.139 1.00 17.31 N ANISOU 582 N VAL B 76 1976 2333 2267 471 470 -15 N ATOM 583 CA VAL A 76 -15.422 -13.190 36.648 1.00 17.57 C ANISOU 583 CA VAL B 76 1754 2390 2533 345 612 -198 C ATOM 584 C VAL A 76 -16.392 -14.047 35.856 1.00 19.25 C ANISOU 584 C VAL B 76 2452 3008 1853 30 257 32 C ATOM 585 O VAL A 76 -17.615 -13.863 35.952 1.00 20.11 O ANISOU 585 O VAL B 76 2378 2955 2308 23 161 -232 O ATOM 586 CB VAL A 76 -14.903 -12.006 35.847 1.00 18.61 C ANISOU 586 CB VAL B 76 2443 2341 2285 -85 1077 -434 C ATOM 587 CG1 VAL A 76 -14.167 -12.439 34.597 1.00 23.17 C ANISOU 587 CG1 VAL B 76 3254 2911 2640 -729 782 -1 C ATOM 588 CG2 VAL A 76 -16.045 -11.102 35.402 1.00 23.77 C ANISOU 588 CG2 VAL B 76 2691 2582 3758 772 904 -634 C ATOM 589 N GLY A 77 -15.877 -15.028 35.100 1.00 20.57 N ANISOU 589 N GLY B 77 2595 3262 1960 262 381 56 N ATOM 590 CA GLY A 77 -16.797 -15.879 34.381 1.00 22.23 C ANISOU 590 CA GLY B 77 2469 3806 2172 580 257 70 C ATOM 591 C GLY A 77 -17.556 -16.847 35.229 1.00 21.72 C ANISOU 591 C GLY B 77 2577 3630 2046 160 213 -185 C ATOM 592 O GLY A 77 -17.128 -17.321 36.267 1.00 23.96 O ANISOU 592 O GLY B 77 2493 4424 2187 84 266 -520 O ATOM 593 N LEU A 78 -18.748 -17.174 34.741 1.00 24.98 N ANISOU 593 N LEU B 78 2723 3174 3594 341 311 -847 N ATOM 594 CA LEU A 78 -19.585 -18.102 35.478 1.00 22.91 C ANISOU 594 CA LEU B 78 2684 3594 2428 -200 -298 -918 C ATOM 595 C LEU A 78 -20.116 -19.220 34.611 1.00 23.33 C ANISOU 595 C LEU B 78 2959 2605 3298 -382 -784 -863 C ATOM 596 O LEU A 78 -21.135 -19.814 34.911 1.00 23.57 O ANISOU 596 O LEU B 78 2803 2926 3225 -284 -553 -1212 O ATOM 597 CB LEU A 78 -20.740 -17.360 36.137 1.00 27.48 C ANISOU 597 CB LEU B 78 2677 4135 3628 -388 -824 -88 C ATOM 598 CG LEU A 78 -20.349 -16.442 37.305 1.00 23.32 C ANISOU 598 CG LEU B 78 2402 3528 2929 380 -344 -1083 C ATOM 599 CD1 LEU A 78 -21.519 -15.537 37.593 1.00 28.29 C ANISOU 599 CD1 LEU B 78 2641 3632 4478 482 -789 -675 C ATOM 600 CD2 LEU A 78 -19.944 -17.246 38.532 1.00 27.78 C ANISOU 600 CD2 LEU B 78 2792 4196 3569 -498 975 -1352 C ATOM 601 N ASP A 79 -19.398 -19.542 33.544 1.00 23.44 N ANISOU 601 N ASP B 79 2503 3983 2418 430 -97 -960 N ATOM 602 CA ASP A 79 -19.854 -20.634 32.686 1.00 23.11 C ANISOU 602 CA ASP B 79 2254 4064 2463 199 -19 -1058 C ATOM 603 C ASP A 79 -19.865 -21.978 33.417 1.00 23.68 C ANISOU 603 C ASP B 79 2111 4069 2819 -63 -33 -1414 C ATOM 604 O ASP A 79 -20.513 -22.929 32.904 1.00 30.71 O ANISOU 604 O ASP B 79 2361 5112 4197 686 -641 -2388 O ATOM 605 CB ASP A 79 -19.030 -20.668 31.384 1.00 24.84 C ANISOU 605 CB ASP B 79 2725 4281 2431 572 -66 -852 C ATOM 606 CG ASP A 79 -17.544 -20.659 31.665 1.00 25.98 C ANISOU 606 CG ASP B 79 3036 3888 2947 624 -24 -396 C ATOM 607 OD1 ASP A 79 -16.994 -19.574 31.994 1.00 24.70 O ANISOU 607 OD1 ASP B 79 2818 3953 2614 290 289 -476 O ATOM 608 OD2 ASP A 79 -16.966 -21.765 31.580 1.00 27.87 O ANISOU 608 OD2 ASP B 79 3723 4124 2743 1018 306 -53 O ATOM 609 N LYS A 80 -19.212 -22.125 34.564 1.00 21.76 N ANISOU 609 N LYS B 80 2578 3381 2308 -55 157 -829 N ATOM 610 CA LYS A 80 -19.188 -23.439 35.218 1.00 21.54 C ANISOU 610 CA LYS B 80 2720 3193 2269 124 74 -681 C ATOM 611 C LYS A 80 -20.220 -23.467 36.338 1.00 18.68 C ANISOU 611 C LYS B 80 2050 3006 2044 385 -223 -668 C ATOM 612 O LYS A 80 -20.320 -24.436 37.072 1.00 22.40 O ANISOU 612 O LYS B 80 2512 2709 3290 194 592 -691 O ATOM 613 CB LYS A 80 -17.797 -23.731 35.735 1.00 22.90 C ANISOU 613 CB LYS B 80 2568 3286 2848 -78 378 -826 C ATOM 614 CG LYS A 80 -16.693 -23.842 34.727 1.00 26.68 C ANISOU 614 CG LYS B 80 3521 3149 3466 266 1215 -701 C ATOM 615 CD LYS A 80 -16.751 -25.127 33.960 1.00 35.67 C ANISOU 615 CD LYS B 80 5893 3783 3879 -63 -859 -299 C ATOM 616 CE LYS A 80 -15.459 -25.268 33.145 1.00 45.53 C ANISOU 616 CE LYS B 80 8906 3785 4610 -275 -535 116 C ATOM 617 NZ LYS A 80 -15.078 -26.705 33.014 1.00 63.57 N ANISOU 617 NZ LYS B 80 10298 6340 7515 1048 -2681 2658 N ATOM 618 N VAL A 81 -20.998 -22.375 36.436 1.00 20.65 N ANISOU 618 N VAL B 81 2351 2746 2747 232 -122 -881 N ATOM 619 CA VAL A 81 -22.090 -22.400 37.409 1.00 20.74 C ANISOU 619 CA VAL B 81 2214 2627 3039 -27 -255 -851 C ATOM 620 C VAL A 81 -23.453 -22.400 36.739 1.00 21.49 C ANISOU 620 C VAL B 81 2029 3071 3067 -32 -159 -1226 C ATOM 621 O VAL A 81 -23.689 -21.592 35.813 1.00 21.54 O ANISOU 621 O VAL B 81 2604 3051 2530 146 -101 -863 O ATOM 622 CB VAL A 81 -21.973 -21.196 38.348 1.00 21.73 C ANISOU 622 CB VAL B 81 2332 2991 2933 -375 -377 -593 C ATOM 623 CG1 VAL A 81 -23.082 -21.249 39.376 1.00 22.29 C ANISOU 623 CG1 VAL B 81 2824 2609 3035 259 345 -706 C ATOM 624 CG2 VAL A 81 -20.593 -21.241 39.004 1.00 23.33 C ANISOU 624 CG2 VAL B 81 1973 3167 3725 -202 -348 -1044 C ATOM 625 N ASP A 82 -24.338 -23.294 37.190 1.00 21.44 N ANISOU 625 N ASP B 82 2248 2881 3018 -191 -108 -812 N ATOM 626 CA ASP A 82 -25.697 -23.321 36.598 1.00 21.51 C ANISOU 626 CA ASP B 82 2428 3046 2699 -336 162 -896 C ATOM 627 C ASP A 82 -26.560 -22.261 37.289 1.00 24.32 C ANISOU 627 C ASP B 82 2896 2840 3505 -171 237 -941 C ATOM 628 O ASP A 82 -27.160 -22.489 38.330 1.00 23.37 O ANISOU 628 O ASP B 82 2905 2404 3570 -250 123 -759 O ATOM 629 CB ASP A 82 -26.295 -24.711 36.714 1.00 22.15 C ANISOU 629 CB ASP B 82 2389 3103 2926 -439 140 -1134 C ATOM 630 CG ASP A 82 -27.597 -24.860 35.955 1.00 24.44 C ANISOU 630 CG ASP B 82 2774 3060 3453 -174 -691 -1125 C ATOM 631 OD1 ASP A 82 -28.245 -23.818 35.698 1.00 27.13 O ANISOU 631 OD1 ASP B 82 3566 2758 3983 -172 -464 -1045 O ATOM 632 OD2 ASP A 82 -27.998 -26.016 35.660 1.00 30.97 O ANISOU 632 OD2 ASP B 82 2832 4868 4069 92 -943 -1851 O ATOM 633 N LEU A 83 -26.543 -21.086 36.684 1.00 24.36 N ANISOU 633 N LEU B 83 2604 3438 3214 5 -280 -1299 N ATOM 634 CA LEU A 83 -27.232 -19.931 37.246 1.00 24.02 C ANISOU 634 CA LEU B 83 2701 3168 3259 -93 164 -1211 C ATOM 635 C LEU A 83 -28.734 -20.192 37.316 1.00 27.89 C ANISOU 635 C LEU B 83 2917 3997 3684 -653 -299 -470 C ATOM 636 O LEU A 83 -29.439 -19.796 38.253 1.00 27.87 O ANISOU 636 O LEU B 83 3949 3231 3409 -282 -86 -920 O ATOM 637 CB LEU A 83 -26.900 -18.686 36.429 1.00 24.27 C ANISOU 637 CB LEU B 83 3196 2545 3481 -82 583 -1249 C ATOM 638 CG LEU A 83 -25.434 -18.261 36.455 1.00 22.18 C ANISOU 638 CG LEU B 83 3083 2622 2721 -98 492 -858 C ATOM 639 CD1 LEU A 83 -25.280 -16.979 35.642 1.00 27.69 C ANISOU 639 CD1 LEU B 83 3610 3483 3427 -198 1150 -1183 C ATOM 640 CD2 LEU A 83 -24.874 -18.116 37.877 1.00 23.03 C ANISOU 640 CD2 LEU B 83 3067 2836 2847 223 162 -877 C ATOM 641 N ILE A 84 -29.220 -20.884 36.286 1.00 25.39 N ANISOU 641 N ILE B 84 2849 3131 3668 -56 -263 -1093 N ATOM 642 CA ILE A 84 -30.677 -21.084 36.201 1.00 30.63 C ANISOU 642 CA ILE B 84 3588 3773 4278 -716 350 -2175 C ATOM 643 C ILE A 84 -31.109 -21.919 37.392 1.00 26.61 C ANISOU 643 C ILE B 84 3050 3265 3795 -450 -175 -1486 C ATOM 644 O ILE A 84 -32.067 -21.662 38.105 1.00 29.67 O ANISOU 644 O ILE B 84 3000 3378 4897 -841 -299 -1093 O ATOM 645 CB ILE A 84 -31.044 -21.732 34.860 1.00 36.77 C ANISOU 645 CB ILE B 84 5474 4650 3848 -2415 215 -1933 C ATOM 646 CG1 ILE A 84 -30.642 -20.838 33.684 1.00 44.92 C ANISOU 646 CG1 ILE B 84 6257 6455 4354 -3334 827 -2778 C ATOM 647 CG2 ILE A 84 -32.521 -22.075 34.830 1.00 34.03 C ANISOU 647 CG2 ILE B 84 5252 3773 3904 -1856 -251 -1217 C ATOM 648 CD1 ILE A 84 -30.794 -21.429 32.302 1.00 47.48 C ANISOU 648 CD1 ILE B 84 4090 9757 4194 -2421 1439 -3163 C ATOM 649 N LYS A 85 -30.299 -22.964 37.606 1.00 27.24 N ANISOU 649 N LYS B 85 3212 3216 3921 -559 7 -1728 N ATOM 650 CA LYS A 85 -30.558 -23.871 38.713 1.00 24.98 C ANISOU 650 CA LYS B 85 2804 2818 3870 -730 4 -1188 C ATOM 651 C LYS A 85 -30.410 -23.188 40.055 1.00 25.24 C ANISOU 651 C LYS B 85 2881 2797 3913 -1077 5 -793 C ATOM 652 O LYS A 85 -31.228 -23.377 40.972 1.00 25.71 O ANISOU 652 O LYS B 85 2999 2847 3922 -837 609 -1120 O ATOM 653 CB LYS A 85 -29.631 -25.093 38.584 1.00 25.97 C ANISOU 653 CB LYS B 85 3333 3070 3465 -426 1076 -450 C ATOM 654 CG LYS A 85 -29.906 -26.043 39.744 1.00 26.17 C ANISOU 654 CG LYS B 85 2219 4069 3654 -512 740 -612 C ATOM 655 CD LYS A 85 -31.071 -26.964 39.408 1.00 29.90 C ANISOU 655 CD LYS B 85 2267 4373 4720 -288 -152 -179 C ATOM 656 CE LYS A 85 -30.933 -28.275 40.188 1.00 32.68 C ANISOU 656 CE LYS B 85 1939 5294 5183 -784 222 -765 C ATOM 657 NZ LYS A 85 -32.249 -28.987 40.289 1.00 48.79 N ANISOU 657 NZ LYS B 85 2603 7611 8322 -2027 896 -1670 N ATOM 658 N CYS A 86 -29.404 -22.354 40.253 1.00 24.23 N ANISOU 658 N CYS B 86 2908 3033 3266 -1086 223 -1358 N ATOM 659 CA CYS A 86 -29.223 -21.614 41.503 1.00 24.70 C ANISOU 659 CA CYS B 86 3143 2684 3559 -763 -52 -1401 C ATOM 660 C CYS A 86 -30.415 -20.728 41.813 1.00 27.40 C ANISOU 660 C CYS B 86 3943 2697 3770 -914 -244 -1458 C ATOM 661 O CYS A 86 -30.907 -20.681 42.941 1.00 27.38 O ANISOU 661 O CYS B 86 2920 2753 4730 -1236 1088 -926 O ATOM 662 CB CYS A 86 -27.923 -20.769 41.428 1.00 23.60 C ANISOU 662 CB CYS B 86 2645 2576 3745 -270 -16 -1166 C ATOM 663 SG CYS A 86 -26.448 -21.791 41.607 1.00 22.16 S ANISOU 663 SG CYS B 86 2601 2453 3366 -441 198 -784 S ATOM 664 N GLU A 87 -30.857 -20.017 40.764 1.00 29.27 N ANISOU 664 N GLU B 87 4284 2614 4223 -841 -13 -1666 N ATOM 665 CA GLU A 87 -32.017 -19.140 40.937 1.00 28.61 C ANISOU 665 CA GLU B 87 4158 2724 3987 -718 -672 -1533 C ATOM 666 C GLU A 87 -33.217 -19.983 41.352 1.00 32.87 C ANISOU 666 C GLU B 87 4526 2887 5077 -820 -418 -668 C ATOM 667 O GLU A 87 -33.946 -19.623 42.283 1.00 35.54 O ANISOU 667 O GLU B 87 5384 2588 5531 -1046 -757 -530 O ATOM 668 CB GLU A 87 -32.258 -18.340 39.658 1.00 31.62 C ANISOU 668 CB GLU B 87 5392 2491 4133 -44 -356 -1308 C ATOM 669 CG GLU A 87 -33.213 -17.162 39.750 1.00 33.98 C ANISOU 669 CG GLU B 87 5546 2886 4478 475 -1688 -1524 C ATOM 670 CD GLU A 87 -34.684 -17.536 39.724 1.00 32.99 C ANISOU 670 CD GLU B 87 5762 2131 4642 741 -733 -1174 C ATOM 671 OE1 GLU A 87 -34.997 -18.656 39.244 1.00 34.51 O ANISOU 671 OE1 GLU B 87 4407 2964 5740 32 548 533 O ATOM 672 OE2 GLU A 87 -35.498 -16.734 40.210 1.00 35.88 O ANISOU 672 OE2 GLU B 87 7420 2720 3492 1153 -378 -766 O ATOM 673 N GLU A 88 -33.426 -21.087 40.636 1.00 29.08 N ANISOU 673 N GLU B 88 3834 2821 4394 -639 325 -975 N ATOM 674 CA GLU A 88 -34.534 -21.992 40.940 1.00 30.67 C ANISOU 674 CA GLU B 88 4362 2954 4335 -1236 211 -111 C ATOM 675 C GLU A 88 -34.491 -22.456 42.391 1.00 32.06 C ANISOU 675 C GLU B 88 4495 3065 4623 -1397 578 -368 C ATOM 676 O GLU A 88 -35.533 -22.605 43.018 1.00 37.46 O ANISOU 676 O GLU B 88 5939 4021 4271 -2631 427 -452 O ATOM 677 CB GLU A 88 -34.488 -23.176 39.971 1.00 40.34 C ANISOU 677 CB GLU B 88 4239 5390 5699 -2411 -763 1257 C ATOM 678 CG GLU A 88 -35.010 -24.503 40.460 1.00 46.74 C ANISOU 678 CG GLU B 88 4768 5500 7492 -592 -619 685 C ATOM 679 CD GLU A 88 -34.655 -25.670 39.552 1.00 54.69 C ANISOU 679 CD GLU B 88 5497 6443 8839 -1252 -1726 1745 C ATOM 680 OE1 GLU A 88 -34.311 -25.422 38.370 1.00 62.94 O ANISOU 680 OE1 GLU B 88 6457 8760 8699 -3596 -2424 2656 O ATOM 681 OE2 GLU A 88 -34.726 -26.821 40.049 1.00 60.05 O ANISOU 681 OE2 GLU B 88 3918 7060 11838 -1237 -2273 2231 O ATOM 682 N LYS A 89 -33.320 -22.694 42.973 1.00 29.30 N ANISOU 682 N LYS B 89 3627 3505 4001 -1563 -585 -77 N ATOM 683 CA LYS A 89 -33.178 -23.204 44.330 1.00 32.52 C ANISOU 683 CA LYS B 89 4436 3850 4070 -2282 -172 -260 C ATOM 684 C LYS A 89 -32.970 -22.115 45.374 1.00 31.47 C ANISOU 684 C LYS B 89 4296 4246 3417 -1769 350 -347 C ATOM 685 O LYS A 89 -32.797 -22.447 46.556 1.00 33.04 O ANISOU 685 O LYS B 89 4982 4258 3314 -1912 756 22 O ATOM 686 CB LYS A 89 -31.963 -24.145 44.448 1.00 33.49 C ANISOU 686 CB LYS B 89 3598 4125 5004 -1647 162 -686 C ATOM 687 CG LYS A 89 -32.188 -25.515 43.802 1.00 35.04 C ANISOU 687 CG LYS B 89 2943 4524 5849 -2259 331 -41 C ATOM 688 CD LYS A 89 -33.073 -26.356 44.724 1.00 36.44 C ANISOU 688 CD LYS B 89 3623 4539 5683 -2528 801 -720 C ATOM 689 CE LYS A 89 -33.501 -27.620 43.997 1.00 38.67 C ANISOU 689 CE LYS B 89 3053 4951 6686 -1787 1082 -1646 C ATOM 690 NZ LYS A 89 -34.215 -28.586 44.865 1.00 47.45 N ANISOU 690 NZ LYS B 89 3781 6345 7903 -2633 1994 -2676 N ATOM 691 N GLY A 90 -32.963 -20.823 45.054 1.00 30.89 N ANISOU 691 N GLY B 90 3743 4165 3827 -2370 941 261 N ATOM 692 CA GLY A 90 -32.712 -19.862 46.117 1.00 32.90 C ANISOU 692 CA GLY B 90 4578 3030 4894 -1785 177 188 C ATOM 693 C GLY A 90 -31.247 -19.787 46.509 1.00 29.56 C ANISOU 693 C GLY B 90 4552 2825 3854 -1511 305 -93 C ATOM 694 O GLY A 90 -30.984 -19.309 47.620 1.00 31.64 O ANISOU 694 O GLY B 90 5062 3085 3875 -869 130 -158 O ATOM 695 N VAL A 91 -30.336 -20.230 45.626 1.00 24.33 N ANISOU 695 N VAL B 91 3098 2317 3829 -773 370 -416 N ATOM 696 CA VAL A 91 -28.916 -20.183 45.899 1.00 22.01 C ANISOU 696 CA VAL B 91 2646 2249 3469 -588 337 -205 C ATOM 697 C VAL A 91 -28.311 -18.910 45.332 1.00 21.73 C ANISOU 697 C VAL B 91 2748 1915 3592 -352 373 -651 C ATOM 698 O VAL A 91 -28.536 -18.639 44.156 1.00 23.30 O ANISOU 698 O VAL B 91 2920 2498 3433 -450 415 -368 O ATOM 699 CB VAL A 91 -28.232 -21.445 45.340 1.00 22.45 C ANISOU 699 CB VAL B 91 2308 2388 3834 -548 487 -89 C ATOM 700 CG1 VAL A 91 -26.730 -21.344 45.555 1.00 19.91 C ANISOU 700 CG1 VAL B 91 2124 2301 3139 -377 -5 42 C ATOM 701 CG2 VAL A 91 -28.781 -22.717 45.991 1.00 28.40 C ANISOU 701 CG2 VAL B 91 2016 3822 4951 -572 448 -190 C ATOM 702 N ARG A 92 -27.560 -18.168 46.149 1.00 21.59 N ANISOU 702 N ARG B 92 2591 2223 3390 -335 295 112 N ATOM 703 CA ARG A 92 -26.898 -16.938 45.717 1.00 21.68 C ANISOU 703 CA ARG B 92 2669 2179 3392 -111 416 246 C ATOM 704 C ARG A 92 -25.622 -17.295 44.964 1.00 21.14 C ANISOU 704 C ARG B 92 3089 2134 2807 -156 643 2 C ATOM 705 O ARG A 92 -24.978 -18.322 45.238 1.00 22.84 O ANISOU 705 O ARG B 92 2541 1940 4196 -447 990 -118 O ATOM 706 CB ARG A 92 -26.544 -15.992 46.860 1.00 23.72 C ANISOU 706 CB ARG B 92 2619 2735 3660 -193 319 642 C ATOM 707 CG ARG A 92 -27.662 -15.525 47.772 1.00 25.97 C ANISOU 707 CG ARG B 92 3367 2596 3903 394 585 708 C ATOM 708 CD ARG A 92 -28.834 -14.899 47.035 1.00 28.46 C ANISOU 708 CD ARG B 92 3597 2584 4634 439 630 527 C ATOM 709 NE ARG A 92 -28.485 -13.729 46.223 1.00 30.28 N ANISOU 709 NE ARG B 92 4047 2526 4932 527 1024 512 N ATOM 710 CZ ARG A 92 -28.277 -12.500 46.706 1.00 27.61 C ANISOU 710 CZ ARG B 92 3801 2079 4610 376 1496 893 C ATOM 711 NH1 ARG A 92 -28.363 -12.231 48.015 1.00 32.63 N ANISOU 711 NH1 ARG B 92 4458 3094 4846 232 1365 1775 N ATOM 712 NH2 ARG A 92 -27.970 -11.536 45.851 1.00 32.54 N ANISOU 712 NH2 ARG B 92 3922 3173 5270 -77 1882 325 N ATOM 713 N VAL A 93 -25.280 -16.456 43.993 1.00 20.19 N ANISOU 713 N VAL B 93 2530 2149 2992 -430 415 -323 N ATOM 714 CA VAL A 93 -24.038 -16.625 43.239 1.00 19.53 C ANISOU 714 CA VAL B 93 2324 2198 2899 -365 608 -332 C ATOM 715 C VAL A 93 -23.304 -15.289 43.213 1.00 19.76 C ANISOU 715 C VAL B 93 2309 1861 3337 -104 251 105 C ATOM 716 O VAL A 93 -23.923 -14.264 42.899 1.00 21.72 O ANISOU 716 O VAL B 93 2549 1668 4034 -94 428 269 O ATOM 717 CB VAL A 93 -24.276 -17.130 41.801 1.00 19.22 C ANISOU 717 CB VAL B 93 2051 2317 2933 -286 551 -357 C ATOM 718 CG1 VAL A 93 -22.931 -17.386 41.103 1.00 22.14 C ANISOU 718 CG1 VAL B 93 3195 2221 2994 -441 188 -264 C ATOM 719 CG2 VAL A 93 -25.153 -18.370 41.710 1.00 24.66 C ANISOU 719 CG2 VAL B 93 2028 2809 4534 -83 288 -939 C ATOM 720 N THR A 94 -22.015 -15.347 43.548 1.00 18.16 N ANISOU 720 N THR B 94 2081 2004 2815 -96 392 -50 N ATOM 721 CA THR A 94 -21.147 -14.176 43.427 1.00 17.15 C ANISOU 721 CA THR B 94 1912 2119 2486 112 235 2 C ATOM 722 C THR A 94 -19.941 -14.498 42.559 1.00 16.21 C ANISOU 722 C THR B 94 1847 2086 2228 80 223 -89 C ATOM 723 O THR A 94 -19.571 -15.671 42.377 1.00 17.19 O ANISOU 723 O THR B 94 1845 1835 2850 -54 147 -157 O ATOM 724 CB THR A 94 -20.676 -13.640 44.797 1.00 17.95 C ANISOU 724 CB THR B 94 2541 1864 2415 -243 193 118 C ATOM 725 OG1 THR A 94 -19.730 -14.530 45.429 1.00 18.03 O ANISOU 725 OG1 THR B 94 2528 1876 2445 16 -30 195 O ATOM 726 CG2 THR A 94 -21.869 -13.480 45.761 1.00 19.43 C ANISOU 726 CG2 THR B 94 2369 2001 3011 62 353 561 C ATOM 727 N ASN A 95 -19.319 -13.452 42.001 1.00 16.93 N ANISOU 727 N ASN B 95 1887 2007 2539 13 256 -172 N ATOM 728 CA ASN A 95 -18.143 -13.578 41.157 1.00 17.09 C ANISOU 728 CA ASN B 95 1828 2089 2578 -87 320 -185 C ATOM 729 C ASN A 95 -17.120 -12.518 41.535 1.00 16.78 C ANISOU 729 C ASN B 95 1851 2306 2218 0 129 101 C ATOM 730 O ASN A 95 -17.187 -11.885 42.605 1.00 16.89 O ANISOU 730 O ASN B 95 2135 1903 2380 149 171 207 O ATOM 731 CB ASN A 95 -18.529 -13.580 39.664 1.00 16.35 C ANISOU 731 CB ASN B 95 1549 2058 2605 -103 122 -41 C ATOM 732 CG ASN A 95 -19.044 -12.213 39.217 1.00 18.98 C ANISOU 732 CG ASN B 95 2289 2397 2527 229 366 -164 C ATOM 733 OD1 ASN A 95 -19.450 -11.362 40.012 1.00 18.68 O ANISOU 733 OD1 ASN B 95 1918 2152 3026 140 263 -34 O ATOM 734 ND2 ASN A 95 -18.978 -11.995 37.883 1.00 19.89 N ANISOU 734 ND2 ASN B 95 2193 2792 2573 -390 405 -378 N ATOM 735 N THR A 96 -16.126 -12.319 40.678 1.00 15.33 N ANISOU 735 N THR B 96 1716 2332 1776 -119 16 -200 N ATOM 736 CA THR A 96 -15.100 -11.300 40.894 1.00 16.11 C ANISOU 736 CA THR B 96 1762 2466 1894 -134 30 -377 C ATOM 737 C THR A 96 -14.991 -10.350 39.711 1.00 19.00 C ANISOU 737 C THR B 96 1964 2796 2457 -66 441 -498 C ATOM 738 O THR A 96 -14.049 -10.408 38.923 1.00 20.20 O ANISOU 738 O THR B 96 2365 3246 2064 133 342 -224 O ATOM 739 CB THR A 96 -13.754 -11.935 41.228 1.00 15.48 C ANISOU 739 CB THR B 96 1645 2352 1885 -174 92 -151 C ATOM 740 OG1 THR A 96 -13.262 -12.704 40.101 1.00 18.86 O ANISOU 740 OG1 THR B 96 2299 2704 2164 -213 -303 15 O ATOM 741 CG2 THR A 96 -13.843 -12.907 42.392 1.00 18.53 C ANISOU 741 CG2 THR B 96 2505 1876 2658 -21 937 56 C ATOM 742 N PRO A 97 -15.948 -9.425 39.633 1.00 21.69 N ANISOU 742 N PRO B 97 1999 2650 3593 -413 731 -1005 N ATOM 743 CA PRO A 97 -15.934 -8.477 38.506 1.00 24.49 C ANISOU 743 CA PRO B 97 2176 3204 3924 -188 823 -1247 C ATOM 744 C PRO A 97 -14.901 -7.381 38.711 1.00 24.86 C ANISOU 744 C PRO B 97 2176 3847 3421 -227 812 -1489 C ATOM 745 O PRO A 97 -14.594 -7.083 39.867 1.00 23.10 O ANISOU 745 O PRO B 97 2407 3094 3276 -289 750 -520 O ATOM 746 CB PRO A 97 -17.356 -7.892 38.551 1.00 28.10 C ANISOU 746 CB PRO B 97 2297 3139 5242 72 1221 -1561 C ATOM 747 CG PRO A 97 -17.700 -7.892 40.004 1.00 29.25 C ANISOU 747 CG PRO B 97 3041 2483 5590 -278 2040 -1231 C ATOM 748 CD PRO A 97 -17.032 -9.135 40.560 1.00 22.56 C ANISOU 748 CD PRO B 97 1907 2348 4317 -59 804 -787 C ATOM 749 N ASP A 98 -14.434 -6.805 37.613 1.00 23.81 N ANISOU 749 N ASP B 98 1931 3910 3204 -32 540 -1229 N ATOM 750 CA ASP A 98 -13.623 -5.623 37.477 1.00 24.18 C ANISOU 750 CA ASP B 98 1956 3587 3644 -27 603 -808 C ATOM 751 C ASP A 98 -12.196 -5.785 37.948 1.00 28.89 C ANISOU 751 C ASP B 98 2740 4156 4082 -855 1232 -1260 C ATOM 752 O ASP A 98 -11.215 -5.263 37.374 1.00 23.63 O ANISOU 752 O ASP B 98 2874 2848 3255 191 752 270 O ATOM 753 CB ASP A 98 -14.324 -4.485 38.250 1.00 25.67 C ANISOU 753 CB ASP B 98 1944 4481 3327 -167 587 -128 C ATOM 754 CG ASP A 98 -15.677 -4.251 37.585 1.00 28.38 C ANISOU 754 CG ASP B 98 3039 3662 4082 -50 924 103 C ATOM 755 OD1 ASP A 98 -15.635 -3.939 36.366 1.00 28.98 O ANISOU 755 OD1 ASP B 98 4473 2643 3894 -383 678 179 O ATOM 756 OD2 ASP A 98 -16.722 -4.375 38.234 1.00 37.03 O ANISOU 756 OD2 ASP B 98 5554 3639 4875 -240 1895 433 O ATOM 757 N VAL A 99 -11.995 -6.549 38.984 1.00 18.34 N ANISOU 757 N VAL B 99 2111 2244 2614 234 171 435 N ATOM 758 CA VAL A 99 -10.696 -6.637 39.639 1.00 17.17 C ANISOU 758 CA VAL B 99 2030 2248 2245 151 400 543 C ATOM 759 C VAL A 99 -9.651 -7.357 38.800 1.00 17.71 C ANISOU 759 C VAL B 99 2364 2293 2071 6 362 518 C ATOM 760 O VAL A 99 -8.463 -7.182 39.127 1.00 18.17 O ANISOU 760 O VAL B 99 1968 2297 2639 60 90 724 O ATOM 761 CB VAL A 99 -10.804 -7.303 41.026 1.00 18.28 C ANISOU 761 CB VAL B 99 2546 2029 2369 398 693 706 C ATOM 762 CG1 VAL A 99 -11.610 -6.402 41.937 1.00 20.79 C ANISOU 762 CG1 VAL B 99 3227 2018 2655 305 650 927 C ATOM 763 CG2 VAL A 99 -11.387 -8.691 40.908 1.00 22.21 C ANISOU 763 CG2 VAL B 99 2565 2860 3013 660 947 601 C ATOM 764 N LEU A 100 -9.995 -8.118 37.777 1.00 16.31 N ANISOU 764 N LEU B 100 2349 1908 1941 243 416 181 N ATOM 765 CA LEU A 100 -8.990 -8.791 36.933 1.00 15.05 C ANISOU 765 CA LEU B 100 1574 2058 2088 197 399 274 C ATOM 766 C LEU A 100 -8.906 -8.187 35.549 1.00 14.15 C ANISOU 766 C LEU B 100 1650 1735 1992 165 254 287 C ATOM 767 O LEU A 100 -8.130 -8.674 34.728 1.00 14.86 O ANISOU 767 O LEU B 100 1790 1808 2050 188 198 347 O ATOM 768 CB LEU A 100 -9.264 -10.302 36.870 1.00 16.31 C ANISOU 768 CB LEU B 100 1551 1932 2713 148 288 -56 C ATOM 769 CG LEU A 100 -10.646 -10.800 36.528 1.00 16.55 C ANISOU 769 CG LEU B 100 1763 2261 2263 -89 131 -126 C ATOM 770 CD1 LEU A 100 -11.111 -10.544 35.104 1.00 24.83 C ANISOU 770 CD1 LEU B 100 3393 3200 2840 -840 1237 -1139 C ATOM 771 CD2 LEU A 100 -10.762 -12.329 36.709 1.00 21.25 C ANISOU 771 CD2 LEU B 100 1560 3554 2961 -216 657 -643 C ATOM 772 N THR A 101 -9.710 -7.159 35.268 1.00 14.65 N ANISOU 772 N THR B 101 1657 1686 2222 14 473 243 N ATOM 773 CA THR A 101 -9.745 -6.605 33.922 1.00 13.91 C ANISOU 773 CA THR B 101 1322 1917 2048 125 163 176 C ATOM 774 C THR A 101 -8.391 -6.168 33.380 1.00 13.82 C ANISOU 774 C THR B 101 1222 2084 1945 207 77 454 C ATOM 775 O THR A 101 -7.997 -6.484 32.257 1.00 15.35 O ANISOU 775 O THR B 101 2170 1725 1935 20 -234 439 O ATOM 776 CB THR A 101 -10.726 -5.416 33.885 1.00 15.25 C ANISOU 776 CB THR B 101 1238 1965 2592 160 392 80 C ATOM 777 OG1 THR A 101 -12.014 -5.912 34.255 1.00 16.54 O ANISOU 777 OG1 THR B 101 1807 1968 2509 -132 532 130 O ATOM 778 CG2 THR A 101 -10.803 -4.774 32.485 1.00 18.93 C ANISOU 778 CG2 THR B 101 1886 2247 3061 204 1006 -52 C ATOM 779 N ASP A 102 -7.678 -5.406 34.198 1.00 13.21 N ANISOU 779 N ASP B 102 1341 1793 1886 118 61 436 N ATOM 780 CA ASP A 102 -6.419 -4.852 33.757 1.00 13.17 C ANISOU 780 CA ASP B 102 1666 1660 1676 -116 93 132 C ATOM 781 C ASP A 102 -5.376 -5.924 33.483 1.00 14.20 C ANISOU 781 C ASP B 102 1757 1745 1893 90 229 256 C ATOM 782 O ASP A 102 -4.667 -5.895 32.473 1.00 14.14 O ANISOU 782 O ASP B 102 1630 1821 1923 97 85 339 O ATOM 783 CB ASP A 102 -5.867 -3.879 34.791 1.00 16.70 C ANISOU 783 CB ASP B 102 1787 2134 2424 -401 -319 712 C ATOM 784 CG ASP A 102 -6.691 -2.613 34.874 1.00 24.93 C ANISOU 784 CG ASP B 102 2208 2649 4614 142 -525 1349 C ATOM 785 OD1 ASP A 102 -7.416 -2.298 33.927 1.00 29.66 O ANISOU 785 OD1 ASP B 102 4093 3012 4167 1830 1410 1081 O ATOM 786 OD2 ASP A 102 -6.562 -1.991 35.935 1.00 34.88 O ANISOU 786 OD2 ASP B 102 3158 5477 4618 1371 -267 2318 O ATOM 787 N ASP A 103 -5.275 -6.925 34.376 1.00 13.77 N ANISOU 787 N ASP B 103 1533 1823 1874 72 38 169 N ATOM 788 CA ASP A 103 -4.268 -7.965 34.124 1.00 13.66 C ANISOU 788 CA ASP B 103 1649 1728 1814 25 0 107 C ATOM 789 C ASP A 103 -4.599 -8.759 32.875 1.00 12.24 C ANISOU 789 C ASP B 103 1314 1502 1837 -31 185 124 C ATOM 790 O ASP A 103 -3.664 -9.136 32.140 1.00 13.48 O ANISOU 790 O ASP B 103 1608 1514 1999 -63 21 257 O ATOM 791 CB ASP A 103 -4.144 -8.853 35.360 1.00 13.43 C ANISOU 791 CB ASP B 103 1559 1674 1871 -32 32 218 C ATOM 792 CG ASP A 103 -3.047 -8.473 36.320 1.00 14.04 C ANISOU 792 CG ASP B 103 1838 1905 1593 18 -55 179 C ATOM 793 OD1 ASP A 103 -2.027 -7.939 35.874 1.00 18.78 O ANISOU 793 OD1 ASP B 103 1504 2982 2648 -326 202 -521 O ATOM 794 OD2 ASP A 103 -3.216 -8.763 37.507 1.00 22.12 O ANISOU 794 OD2 ASP B 103 4700 2023 1682 -365 504 -21 O ATOM 795 N VAL A 104 -5.860 -9.045 32.633 1.00 12.64 N ANISOU 795 N VAL B 104 1562 1438 1802 -39 106 139 N ATOM 796 CA VAL A 104 -6.194 -9.847 31.455 1.00 12.70 C ANISOU 796 CA VAL B 104 1583 1376 1864 27 60 -40 C ATOM 797 C VAL A 104 -5.916 -9.040 30.185 1.00 12.44 C ANISOU 797 C VAL B 104 1452 1523 1750 78 -86 94 C ATOM 798 O VAL A 104 -5.350 -9.538 29.229 1.00 13.60 O ANISOU 798 O VAL B 104 1590 1749 1830 -38 -186 251 O ATOM 799 CB VAL A 104 -7.633 -10.337 31.525 1.00 14.48 C ANISOU 799 CB VAL B 104 1457 1756 2289 -72 30 65 C ATOM 800 CG1 VAL A 104 -8.033 -10.985 30.214 1.00 16.44 C ANISOU 800 CG1 VAL B 104 1571 2285 2389 -340 -193 410 C ATOM 801 CG2 VAL A 104 -7.841 -11.325 32.645 1.00 16.09 C ANISOU 801 CG2 VAL B 104 1584 2022 2509 50 208 227 C ATOM 802 N ALA A 105 -6.312 -7.754 30.197 1.00 12.66 N ANISOU 802 N ALA B 105 1538 1570 1704 168 -10 -7 N ATOM 803 CA ALA A 105 -6.058 -6.888 29.047 1.00 13.41 C ANISOU 803 CA ALA B 105 1687 1525 1883 118 86 75 C ATOM 804 C ALA A 105 -4.549 -6.698 28.814 1.00 13.16 C ANISOU 804 C ALA B 105 1827 1512 1662 94 10 220 C ATOM 805 O ALA A 105 -4.068 -6.722 27.680 1.00 13.20 O ANISOU 805 O ALA B 105 1567 1844 1607 57 5 151 O ATOM 806 CB ALA A 105 -6.769 -5.533 29.216 1.00 13.71 C ANISOU 806 CB ALA B 105 1670 1484 2055 151 114 66 C ATOM 807 N ASP A 106 -3.789 -6.574 29.865 1.00 13.37 N ANISOU 807 N ASP B 106 1458 1987 1635 -170 85 226 N ATOM 808 CA ASP A 106 -2.329 -6.467 29.795 1.00 12.25 C ANISOU 808 CA ASP B 106 1293 1865 1496 10 345 120 C ATOM 809 C ASP A 106 -1.754 -7.703 29.105 1.00 13.28 C ANISOU 809 C ASP B 106 1448 1883 1715 -105 -6 116 C ATOM 810 O ASP A 106 -0.850 -7.574 28.277 1.00 13.20 O ANISOU 810 O ASP B 106 1667 1743 1607 -83 107 60 O ATOM 811 CB ASP A 106 -1.718 -6.313 31.160 1.00 13.20 C ANISOU 811 CB ASP B 106 1974 1421 1620 34 53 226 C ATOM 812 CG ASP A 106 -1.898 -4.951 31.799 1.00 13.19 C ANISOU 812 CG ASP B 106 1616 1740 1657 160 93 -36 C ATOM 813 OD1 ASP A 106 -2.474 -4.061 31.185 1.00 15.16 O ANISOU 813 OD1 ASP B 106 1765 1862 2135 130 297 -229 O ATOM 814 OD2 ASP A 106 -1.434 -4.829 32.967 1.00 15.45 O ANISOU 814 OD2 ASP B 106 1778 2370 1722 138 -45 -126 O ATOM 815 N LEU A 107 -2.290 -8.873 29.456 1.00 13.39 N ANISOU 815 N LEU B 107 1362 1941 1785 -94 -91 482 N ATOM 816 CA LEU A 107 -1.752 -10.086 28.887 1.00 13.39 C ANISOU 816 CA LEU B 107 1587 1634 1866 -40 -68 202 C ATOM 817 C LEU A 107 -2.064 -10.177 27.400 1.00 12.68 C ANISOU 817 C LEU B 107 1584 1265 1969 479 -264 123 C ATOM 818 O LEU A 107 -1.246 -10.696 26.625 1.00 13.76 O ANISOU 818 O LEU B 107 1799 1459 1971 261 11 333 O ATOM 819 CB LEU A 107 -2.258 -11.338 29.628 1.00 14.20 C ANISOU 819 CB LEU B 107 1523 1750 2122 -5 -38 337 C ATOM 820 CG LEU A 107 -1.503 -12.613 29.246 1.00 14.10 C ANISOU 820 CG LEU B 107 1699 1676 1981 36 129 233 C ATOM 821 CD1 LEU A 107 -0.063 -12.559 29.758 1.00 16.45 C ANISOU 821 CD1 LEU B 107 1567 1825 2860 105 -116 -160 C ATOM 822 CD2 LEU A 107 -2.223 -13.849 29.726 1.00 15.74 C ANISOU 822 CD2 LEU B 107 1497 2020 2464 62 12 34 C ATOM 823 N ALA A 108 -3.225 -9.682 26.983 1.00 13.65 N ANISOU 823 N ALA B 108 1817 1381 1986 -14 269 103 N ATOM 824 CA ALA A 108 -3.531 -9.658 25.545 1.00 13.28 C ANISOU 824 CA ALA B 108 1564 1493 1990 -66 41 41 C ATOM 825 C ALA A 108 -2.478 -8.876 24.772 1.00 12.05 C ANISOU 825 C ALA B 108 1471 1461 1646 64 -98 4 C ATOM 826 O ALA A 108 -2.009 -9.308 23.705 1.00 13.21 O ANISOU 826 O ALA B 108 1803 1393 1824 75 -238 239 O ATOM 827 CB ALA A 108 -4.912 -9.071 25.296 1.00 14.53 C ANISOU 827 CB ALA B 108 1808 1535 2176 -196 -362 68 C ATOM 828 N ILE A 109 -2.113 -7.720 25.294 1.00 12.85 N ANISOU 828 N ILE B 109 1551 1589 1741 -141 -264 156 N ATOM 829 CA ILE A 109 -1.109 -6.905 24.617 1.00 12.62 C ANISOU 829 CA ILE B 109 1497 1452 1847 -241 -270 102 C ATOM 830 C ILE A 109 0.246 -7.590 24.678 1.00 12.62 C ANISOU 830 C ILE B 109 1635 1492 1670 -58 -73 143 C ATOM 831 O ILE A 109 1.021 -7.632 23.726 1.00 12.56 O ANISOU 831 O ILE B 109 1594 1468 1711 -80 -78 179 O ATOM 832 CB ILE A 109 -1.031 -5.486 25.217 1.00 12.87 C ANISOU 832 CB ILE B 109 1520 1439 1931 -146 -277 121 C ATOM 833 CG1 ILE A 109 -2.339 -4.709 25.220 1.00 15.06 C ANISOU 833 CG1 ILE B 109 2138 1476 2110 119 -132 -177 C ATOM 834 CG2 ILE A 109 0.105 -4.699 24.546 1.00 14.99 C ANISOU 834 CG2 ILE B 109 1544 1873 2278 213 148 152 C ATOM 835 CD1 ILE A 109 -2.886 -4.447 23.840 1.00 16.41 C ANISOU 835 CD1 ILE B 109 2572 1681 1982 665 -261 -69 C ATOM 836 N GLY A 110 0.585 -8.198 25.815 1.00 12.62 N ANISOU 836 N GLY B 110 1678 1548 1568 -7 -189 157 N ATOM 837 CA GLY A 110 1.811 -8.939 25.922 1.00 11.39 C ANISOU 837 CA GLY B 110 1387 1523 1415 -112 145 254 C ATOM 838 C GLY A 110 1.919 -10.095 24.948 1.00 12.75 C ANISOU 838 C GLY B 110 1798 1488 1559 -71 -246 99 C ATOM 839 O GLY A 110 2.970 -10.362 24.393 1.00 12.22 O ANISOU 839 O GLY B 110 1778 1371 1495 119 -19 54 O ATOM 840 N LEU A 111 0.795 -10.799 24.725 1.00 12.68 N ANISOU 840 N LEU B 111 1409 1503 1904 168 -9 104 N ATOM 841 CA LEU A 111 0.736 -11.876 23.737 1.00 12.35 C ANISOU 841 CA LEU B 111 1449 1512 1733 32 18 116 C ATOM 842 C LEU A 111 0.919 -11.356 22.329 1.00 12.46 C ANISOU 842 C LEU B 111 1667 1242 1824 105 121 147 C ATOM 843 O LEU A 111 1.641 -11.951 21.510 1.00 12.75 O ANISOU 843 O LEU B 111 1528 1462 1853 152 13 315 O ATOM 844 CB LEU A 111 -0.591 -12.635 23.883 1.00 13.70 C ANISOU 844 CB LEU B 111 1396 1726 2083 -30 142 -263 C ATOM 845 CG LEU A 111 -0.606 -13.670 25.027 1.00 12.73 C ANISOU 845 CG LEU B 111 1182 1916 1740 167 -105 34 C ATOM 846 CD1 LEU A 111 -2.050 -14.101 25.341 1.00 15.30 C ANISOU 846 CD1 LEU B 111 1349 2049 2417 63 245 -43 C ATOM 847 CD2 LEU A 111 0.244 -14.877 24.681 1.00 14.87 C ANISOU 847 CD2 LEU B 111 1878 1805 1969 360 -163 -243 C ATOM 848 N ILE A 112 0.263 -10.211 22.048 1.00 12.41 N ANISOU 848 N ILE B 112 1572 1410 1734 143 -21 136 N ATOM 849 CA ILE A 112 0.413 -9.610 20.730 1.00 12.17 C ANISOU 849 CA ILE B 112 1803 1221 1600 0 -119 -112 C ATOM 850 C ILE A 112 1.873 -9.325 20.441 1.00 10.92 C ANISOU 850 C ILE B 112 1463 1289 1399 203 -176 95 C ATOM 851 O ILE A 112 2.396 -9.720 19.401 1.00 11.86 O ANISOU 851 O ILE B 112 1651 1487 1367 195 -136 104 O ATOM 852 CB ILE A 112 -0.452 -8.324 20.599 1.00 12.71 C ANISOU 852 CB ILE B 112 1866 1251 1711 77 -156 -94 C ATOM 853 CG1 ILE A 112 -1.957 -8.647 20.554 1.00 13.62 C ANISOU 853 CG1 ILE B 112 2182 1247 1748 -52 -1 -240 C ATOM 854 CG2 ILE A 112 -0.027 -7.525 19.388 1.00 14.84 C ANISOU 854 CG2 ILE B 112 1702 1680 2257 121 91 -186 C ATOM 855 CD1 ILE A 112 -2.874 -7.460 20.767 1.00 15.15 C ANISOU 855 CD1 ILE B 112 2732 1187 1839 11 -45 -240 C ATOM 856 N LEU A 113 2.525 -8.609 21.336 1.00 12.95 N ANISOU 856 N LEU B 113 1630 1720 1570 -138 -256 147 N ATOM 857 CA LEU A 113 3.938 -8.277 21.129 1.00 13.47 C ANISOU 857 CA LEU B 113 1207 1618 2294 96 161 -50 C ATOM 858 C LEU A 113 4.816 -9.529 21.079 1.00 12.48 C ANISOU 858 C LEU B 113 1339 1607 1797 6 -10 -127 C ATOM 859 O LEU A 113 5.754 -9.640 20.292 1.00 13.18 O ANISOU 859 O LEU B 113 1614 1509 1884 0 82 -133 O ATOM 860 CB LEU A 113 4.357 -7.275 22.230 1.00 13.31 C ANISOU 860 CB LEU B 113 1324 1443 2292 -61 72 34 C ATOM 861 CG LEU A 113 3.807 -5.871 22.010 1.00 13.99 C ANISOU 861 CG LEU B 113 1534 1525 2255 82 -105 -5 C ATOM 862 CD1 LEU A 113 3.771 -5.056 23.304 1.00 15.60 C ANISOU 862 CD1 LEU B 113 1771 1604 2551 -211 -558 75 C ATOM 863 CD2 LEU A 113 4.639 -5.225 20.928 1.00 16.39 C ANISOU 863 CD2 LEU B 113 2015 1705 2509 208 380 -169 C ATOM 864 N ALA A 114 4.529 -10.506 21.940 1.00 12.36 N ANISOU 864 N ALA B 114 1543 1367 1788 168 67 -56 N ATOM 865 CA ALA A 114 5.345 -11.716 21.961 1.00 12.76 C ANISOU 865 CA ALA B 114 1480 1413 1957 127 15 15 C ATOM 866 C ALA A 114 5.263 -12.497 20.657 1.00 13.89 C ANISOU 866 C ALA B 114 1516 1554 2207 169 -134 85 C ATOM 867 O ALA A 114 6.273 -13.025 20.214 1.00 13.64 O ANISOU 867 O ALA B 114 1835 1527 1821 67 -134 25 O ATOM 868 CB ALA A 114 5.029 -12.618 23.144 1.00 13.56 C ANISOU 868 CB ALA B 114 1429 1516 2209 167 134 -115 C ATOM 869 N VAL A 115 4.070 -12.521 20.064 1.00 12.33 N ANISOU 869 N VAL B 115 1428 1433 1825 87 51 237 N ATOM 870 CA VAL A 115 3.913 -13.196 18.764 1.00 13.60 C ANISOU 870 CA VAL B 115 1765 1472 1929 279 -56 47 C ATOM 871 C VAL A 115 4.496 -12.348 17.667 1.00 13.64 C ANISOU 871 C VAL B 115 2005 1550 1627 205 -40 -134 C ATOM 872 O VAL A 115 5.407 -12.828 16.956 1.00 14.60 O ANISOU 872 O VAL B 115 1790 1506 2253 323 272 42 O ATOM 873 CB VAL A 115 2.439 -13.527 18.486 1.00 14.07 C ANISOU 873 CB VAL B 115 2311 1570 1467 -5 -10 -88 C ATOM 874 CG1 VAL A 115 2.291 -14.083 17.067 1.00 14.78 C ANISOU 874 CG1 VAL B 115 1962 2042 1610 196 -72 192 C ATOM 875 CG2 VAL A 115 1.889 -14.514 19.490 1.00 14.40 C ANISOU 875 CG2 VAL B 115 1762 2114 1594 61 -212 77 C ATOM 876 N LEU A 116 4.034 -11.106 17.521 1.00 12.46 N ANISOU 876 N LEU B 116 1809 1489 1435 107 -23 225 N ATOM 877 CA LEU A 116 4.456 -10.329 16.345 1.00 11.67 C ANISOU 877 CA LEU B 116 1672 1342 1419 120 -114 80 C ATOM 878 C LEU A 116 5.965 -10.054 16.308 1.00 12.28 C ANISOU 878 C LEU B 116 1596 1354 1715 130 1 46 C ATOM 879 O LEU A 116 6.580 -10.084 15.244 1.00 14.49 O ANISOU 879 O LEU B 116 2051 1599 1855 -177 85 122 O ATOM 880 CB LEU A 116 3.708 -9.006 16.283 1.00 13.43 C ANISOU 880 CB LEU B 116 2249 1263 1591 146 41 4 C ATOM 881 CG LEU A 116 2.378 -8.979 15.521 1.00 14.27 C ANISOU 881 CG LEU B 116 2187 1465 1770 106 219 -214 C ATOM 882 CD1 LEU A 116 1.402 -9.928 16.178 1.00 15.99 C ANISOU 882 CD1 LEU B 116 1958 1917 2200 60 87 -170 C ATOM 883 CD2 LEU A 116 1.860 -7.562 15.470 1.00 15.05 C ANISOU 883 CD2 LEU B 116 2073 1297 2348 -30 300 -111 C ATOM 884 N ARG A 117 6.561 -9.761 17.475 1.00 13.41 N ANISOU 884 N ARG B 117 1711 1552 1831 69 -103 -91 N ATOM 885 CA ARG A 117 7.975 -9.493 17.615 1.00 12.55 C ANISOU 885 CA ARG B 117 1789 1509 1473 68 164 -128 C ATOM 886 C ARG A 117 8.780 -10.754 17.954 1.00 12.15 C ANISOU 886 C ARG B 117 1695 1609 1313 -9 181 -287 C ATOM 887 O ARG A 117 10.005 -10.668 18.132 1.00 14.08 O ANISOU 887 O ARG B 117 1876 1475 1998 -63 -154 -65 O ATOM 888 CB ARG A 117 8.243 -8.367 18.642 1.00 13.18 C ANISOU 888 CB ARG B 117 1703 1541 1761 -131 40 -172 C ATOM 889 CG ARG A 117 7.559 -7.040 18.276 1.00 15.02 C ANISOU 889 CG ARG B 117 1639 1700 2368 -6 144 52 C ATOM 890 CD ARG A 117 8.005 -6.446 16.939 1.00 17.01 C ANISOU 890 CD ARG B 117 1825 2221 2416 395 305 -274 C ATOM 891 NE ARG A 117 9.387 -5.974 17.057 1.00 17.53 N ANISOU 891 NE ARG B 117 2145 2053 2463 218 569 602 N ATOM 892 CZ ARG A 117 9.714 -4.792 17.540 1.00 16.12 C ANISOU 892 CZ ARG B 117 1933 1628 2563 144 545 -324 C ATOM 893 NH1 ARG A 117 8.805 -3.903 17.956 1.00 17.84 N ANISOU 893 NH1 ARG B 117 1865 1739 3175 247 -293 -366 N ATOM 894 NH2 ARG A 117 11.006 -4.515 17.586 1.00 19.33 N ANISOU 894 NH2 ARG B 117 2702 2128 2512 -444 658 -445 N ATOM 895 N ARG A 118 8.146 -11.896 18.046 1.00 12.84 N ANISOU 895 N ARG B 118 1730 1361 1789 13 368 67 N ATOM 896 CA ARG A 118 8.790 -13.179 18.299 1.00 12.90 C ANISOU 896 CA ARG B 118 1797 1366 1737 176 94 180 C ATOM 897 C ARG A 118 9.691 -13.115 19.517 1.00 13.56 C ANISOU 897 C ARG B 118 1887 1489 1777 298 127 14 C ATOM 898 O ARG A 118 10.836 -13.606 19.532 1.00 14.29 O ANISOU 898 O ARG B 118 2087 1502 1840 186 43 75 O ATOM 899 CB ARG A 118 9.577 -13.669 17.070 1.00 14.70 C ANISOU 899 CB ARG B 118 2220 1608 1758 -8 102 246 C ATOM 900 CG ARG A 118 8.760 -13.991 15.841 1.00 15.84 C ANISOU 900 CG ARG B 118 2171 2088 1759 -4 67 131 C ATOM 901 CD ARG A 118 7.817 -15.149 16.130 1.00 16.92 C ANISOU 901 CD ARG B 118 1948 2439 2042 318 121 -283 C ATOM 902 NE ARG A 118 7.358 -15.720 14.868 1.00 18.94 N ANISOU 902 NE ARG B 118 2476 2264 2455 -93 -344 91 N ATOM 903 CZ ARG A 118 6.313 -15.421 14.147 1.00 18.35 C ANISOU 903 CZ ARG B 118 2234 2100 2638 169 -958 221 C ATOM 904 NH1 ARG A 118 5.448 -14.468 14.543 1.00 21.78 N ANISOU 904 NH1 ARG B 118 3498 2154 2625 371 -659 405 N ATOM 905 NH2 ARG A 118 6.052 -16.044 12.992 1.00 20.85 N ANISOU 905 NH2 ARG B 118 2546 3149 2228 -43 -737 480 N ATOM 906 N ILE A 119 9.152 -12.505 20.584 1.00 14.10 N ANISOU 906 N ILE B 119 2039 1554 1764 256 -24 19 N ATOM 907 CA ILE A 119 9.984 -12.305 21.794 1.00 13.48 C ANISOU 907 CA ILE B 119 1744 1464 1914 141 -60 27 C ATOM 908 C ILE A 119 10.429 -13.607 22.396 1.00 13.70 C ANISOU 908 C ILE B 119 1799 1346 2062 123 -94 -52 C ATOM 909 O ILE A 119 11.602 -13.780 22.801 1.00 14.70 O ANISOU 909 O ILE B 119 2247 1475 1861 40 -320 -80 O ATOM 910 CB ILE A 119 9.226 -11.424 22.804 1.00 13.00 C ANISOU 910 CB ILE B 119 1625 1407 1907 204 -134 -59 C ATOM 911 CG1 ILE A 119 9.038 -10.036 22.233 1.00 13.21 C ANISOU 911 CG1 ILE B 119 1622 1635 1761 216 -167 -106 C ATOM 912 CG2 ILE A 119 9.900 -11.354 24.165 1.00 13.72 C ANISOU 912 CG2 ILE B 119 1786 1778 1649 -76 222 37 C ATOM 913 CD1 ILE A 119 8.225 -9.095 23.086 1.00 16.16 C ANISOU 913 CD1 ILE B 119 2019 1535 2586 562 75 92 C ATOM 914 N CYS A 120 9.544 -14.586 22.483 1.00 13.91 N ANISOU 914 N CYS B 120 1778 1652 1857 175 24 -79 N ATOM 915 CA CYS A 120 9.943 -15.872 23.076 1.00 14.23 C ANISOU 915 CA CYS B 120 1939 1680 1787 304 -74 -182 C ATOM 916 C CYS A 120 10.946 -16.600 22.214 1.00 15.19 C ANISOU 916 C CYS B 120 1976 1805 1989 414 18 -87 C ATOM 917 O CYS A 120 11.902 -17.193 22.713 1.00 15.75 O ANISOU 917 O CYS B 120 1946 1653 2384 263 -139 -69 O ATOM 918 CB CYS A 120 8.717 -16.754 23.332 1.00 16.09 C ANISOU 918 CB CYS B 120 1928 1869 2315 311 170 -207 C ATOM 919 SG CYS A 120 7.404 -16.038 24.336 1.00 18.84 S ANISOU 919 SG CYS B 120 2488 2270 2400 -167 65 93 S ATOM 920 N GLU A 121 10.752 -16.529 20.891 1.00 15.29 N ANISOU 920 N GLU B 121 1965 1879 1965 208 8 89 N ATOM 921 CA GLU A 121 11.689 -17.187 19.978 1.00 15.36 C ANISOU 921 CA GLU B 121 1885 1924 2028 385 200 87 C ATOM 922 C GLU A 121 13.056 -16.523 20.041 1.00 15.05 C ANISOU 922 C GLU B 121 1924 1791 2004 360 278 36 C ATOM 923 O GLU A 121 14.091 -17.206 19.997 1.00 16.25 O ANISOU 923 O GLU B 121 2288 1769 2120 459 -16 200 O ATOM 924 CB GLU A 121 11.085 -17.234 18.562 1.00 17.43 C ANISOU 924 CB GLU B 121 2656 1875 2091 239 -231 161 C ATOM 925 CG GLU A 121 9.826 -18.103 18.492 1.00 23.20 C ANISOU 925 CG GLU B 121 2339 2459 4016 527 -873 -334 C ATOM 926 CD GLU A 121 9.822 -19.418 19.233 1.00 26.83 C ANISOU 926 CD GLU B 121 2439 2714 5040 746 -306 323 C ATOM 927 OE1 GLU A 121 10.574 -20.265 18.722 1.00 24.99 O ANISOU 927 OE1 GLU B 121 2611 2508 4376 792 -974 -145 O ATOM 928 OE2 GLU A 121 9.087 -19.645 20.267 1.00 30.18 O ANISOU 928 OE2 GLU B 121 3412 2304 5750 620 589 153 O ATOM 929 N CYS A 122 13.102 -15.211 20.107 1.00 15.62 N ANISOU 929 N CYS B 122 1896 1670 2369 280 33 -338 N ATOM 930 CA CYS A 122 14.326 -14.439 20.213 1.00 15.66 C ANISOU 930 CA CYS B 122 1982 1928 2042 118 -197 34 C ATOM 931 C CYS A 122 15.116 -14.784 21.447 1.00 14.99 C ANISOU 931 C CYS B 122 2242 1602 1850 266 -542 305 C ATOM 932 O CYS A 122 16.342 -14.920 21.458 1.00 17.39 O ANISOU 932 O CYS B 122 2464 1590 2554 169 133 6 O ATOM 933 CB CYS A 122 13.979 -12.924 20.249 1.00 15.22 C ANISOU 933 CB CYS B 122 1867 1816 2098 2 -303 65 C ATOM 934 SG CYS A 122 13.725 -12.184 18.644 1.00 17.93 S ANISOU 934 SG CYS B 122 2337 1920 2558 44 209 -141 S ATOM 935 N ASP A 123 14.397 -14.878 22.576 1.00 15.18 N ANISOU 935 N ASP B 123 2542 1298 1927 491 -366 181 N ATOM 936 CA ASP A 123 15.026 -15.210 23.856 1.00 15.10 C ANISOU 936 CA ASP B 123 2051 1639 2045 336 -41 -100 C ATOM 937 C ASP A 123 15.587 -16.608 23.777 1.00 15.74 C ANISOU 937 C ASP B 123 2047 1589 2344 309 29 -86 C ATOM 938 O ASP A 123 16.715 -16.851 24.219 1.00 16.79 O ANISOU 938 O ASP B 123 2483 1601 2296 396 -305 -56 O ATOM 939 CB ASP A 123 13.999 -14.973 24.970 1.00 15.43 C ANISOU 939 CB ASP B 123 2390 1632 1840 285 -276 -207 C ATOM 940 CG ASP A 123 14.596 -15.351 26.336 1.00 14.59 C ANISOU 940 CG ASP B 123 2044 1576 1923 379 -225 -177 C ATOM 941 OD1 ASP A 123 14.975 -14.483 27.130 1.00 15.44 O ANISOU 941 OD1 ASP B 123 2378 1791 1697 319 -371 14 O ATOM 942 OD2 ASP A 123 14.664 -16.584 26.558 1.00 18.23 O ANISOU 942 OD2 ASP B 123 2408 1976 2544 790 -261 -481 O ATOM 943 N LYS A 124 14.886 -17.597 23.228 1.00 14.99 N ANISOU 943 N LYS B 124 2210 1464 2022 420 -5 -55 N ATOM 944 CA LYS A 124 15.436 -18.940 23.062 1.00 16.01 C ANISOU 944 CA LYS B 124 2203 1591 2289 447 -41 -68 C ATOM 945 C LYS A 124 16.674 -18.923 22.170 1.00 15.84 C ANISOU 945 C LYS B 124 1942 1470 2607 641 -43 59 C ATOM 946 O LYS A 124 17.676 -19.595 22.426 1.00 18.80 O ANISOU 946 O LYS B 124 3176 1456 2512 789 -32 263 O ATOM 947 CB LYS A 124 14.356 -19.825 22.472 1.00 17.59 C ANISOU 947 CB LYS B 124 2208 1925 2549 293 -136 33 C ATOM 948 CG LYS A 124 13.283 -20.304 23.439 1.00 21.62 C ANISOU 948 CG LYS B 124 2042 3387 2788 274 41 401 C ATOM 949 CD LYS A 124 12.160 -20.968 22.697 1.00 28.71 C ANISOU 949 CD LYS B 124 1335 4730 4845 76 -848 1416 C ATOM 950 CE LYS A 124 10.818 -20.331 22.870 1.00 47.74 C ANISOU 950 CE LYS B 124 5506 4509 8124 -1746 931 -529 C ATOM 951 NZ LYS A 124 9.894 -20.810 23.921 1.00 52.24 N ANISOU 951 NZ LYS B 124 5836 2550 11462 81 3055 475 N ATOM 952 N TYR A 125 16.625 -18.124 21.113 1.00 16.97 N ANISOU 952 N TYR B 125 2125 1878 2443 666 39 189 N ATOM 953 CA TYR A 125 17.724 -18.003 20.160 1.00 17.52 C ANISOU 953 CA TYR B 125 3076 1698 1883 278 -249 -44 C ATOM 954 C TYR A 125 18.987 -17.502 20.845 1.00 18.79 C ANISOU 954 C TYR B 125 3223 1246 2672 355 -531 -52 C ATOM 955 O TYR A 125 20.087 -18.001 20.675 1.00 19.41 O ANISOU 955 O TYR B 125 3257 1381 2736 310 20 246 O ATOM 956 CB TYR A 125 17.286 -17.053 19.050 1.00 17.35 C ANISOU 956 CB TYR B 125 2850 1810 1931 281 -168 -15 C ATOM 957 CG TYR A 125 18.205 -16.685 17.933 1.00 18.20 C ANISOU 957 CG TYR B 125 3112 1668 2134 93 -37 -107 C ATOM 958 CD1 TYR A 125 18.151 -17.452 16.788 1.00 19.95 C ANISOU 958 CD1 TYR B 125 3290 1901 2390 269 44 541 C ATOM 959 CD2 TYR A 125 19.088 -15.609 17.978 1.00 18.64 C ANISOU 959 CD2 TYR B 125 3039 1786 2259 278 268 -274 C ATOM 960 CE1 TYR A 125 18.967 -17.182 15.699 1.00 20.51 C ANISOU 960 CE1 TYR B 125 3591 1587 2615 -343 52 440 C ATOM 961 CE2 TYR A 125 19.890 -15.335 16.899 1.00 20.49 C ANISOU 961 CE2 TYR B 125 3356 1636 2795 -181 165 91 C ATOM 962 CZ TYR A 125 19.844 -16.111 15.779 1.00 21.76 C ANISOU 962 CZ TYR B 125 3781 1772 2713 -780 4 313 C ATOM 963 OH TYR A 125 20.634 -15.817 14.695 1.00 24.08 O ANISOU 963 OH TYR B 125 3959 2287 2902 -506 466 367 O ATOM 964 N VAL A 126 18.851 -16.451 21.660 1.00 17.38 N ANISOU 964 N VAL B 126 3016 1336 2252 455 -331 -258 N ATOM 965 CA VAL A 126 20.017 -15.942 22.385 1.00 16.17 C ANISOU 965 CA VAL B 126 2827 1318 1998 220 -3 -145 C ATOM 966 C VAL A 126 20.566 -17.009 23.337 1.00 17.70 C ANISOU 966 C VAL B 126 2655 1442 2629 57 105 -477 C ATOM 967 O VAL A 126 21.768 -17.247 23.433 1.00 18.49 O ANISOU 967 O VAL B 126 3206 1145 2675 307 -171 -113 O ATOM 968 CB VAL A 126 19.640 -14.667 23.154 1.00 15.46 C ANISOU 968 CB VAL B 126 2362 1517 1995 37 190 96 C ATOM 969 CG1 VAL A 126 20.756 -14.300 24.121 1.00 17.21 C ANISOU 969 CG1 VAL B 126 2830 1179 2530 186 -245 -16 C ATOM 970 CG2 VAL A 126 19.333 -13.542 22.170 1.00 15.84 C ANISOU 970 CG2 VAL B 126 2225 1651 2143 96 218 33 C ATOM 971 N ARG A 127 19.748 -17.655 24.148 1.00 16.69 N ANISOU 971 N ARG B 127 2518 1875 1947 -21 -201 -575 N ATOM 972 CA ARG A 127 20.213 -18.614 25.141 1.00 16.51 C ANISOU 972 CA ARG B 127 3069 1510 1694 117 -213 -201 C ATOM 973 C ARG A 127 20.826 -19.854 24.536 1.00 18.59 C ANISOU 973 C ARG B 127 3112 1677 2275 248 -228 -83 C ATOM 974 O ARG A 127 21.562 -20.544 25.244 1.00 21.76 O ANISOU 974 O ARG B 127 3969 2067 2234 777 475 -78 O ATOM 975 CB ARG A 127 19.066 -19.005 26.058 1.00 18.39 C ANISOU 975 CB ARG B 127 2955 1798 2236 523 204 24 C ATOM 976 CG ARG A 127 18.531 -17.844 26.902 1.00 17.82 C ANISOU 976 CG ARG B 127 3211 1184 2377 400 272 -51 C ATOM 977 CD ARG A 127 17.504 -18.309 27.920 1.00 16.83 C ANISOU 977 CD ARG B 127 2540 1361 2495 286 -14 -4 C ATOM 978 NE ARG A 127 16.670 -17.218 28.379 1.00 19.80 N ANISOU 978 NE ARG B 127 3871 1449 2203 375 -139 109 N ATOM 979 CZ ARG A 127 16.521 -16.710 29.583 1.00 16.44 C ANISOU 979 CZ ARG B 127 2479 1713 2055 490 16 -116 C ATOM 980 NH1 ARG A 127 17.187 -17.162 30.647 1.00 19.67 N ANISOU 980 NH1 ARG B 127 2888 2135 2452 394 -97 -567 N ATOM 981 NH2 ARG A 127 15.683 -15.691 29.755 1.00 17.43 N ANISOU 981 NH2 ARG B 127 3055 1525 2042 240 -44 107 N ATOM 982 N ARG A 128 20.583 -20.150 23.271 1.00 19.61 N ANISOU 982 N ARG B 128 3463 1858 2131 737 -113 131 N ATOM 983 CA ARG A 128 21.297 -21.313 22.718 1.00 22.20 C ANISOU 983 CA ARG B 128 3382 2042 3012 666 -260 448 C ATOM 984 C ARG A 128 22.595 -20.859 22.035 1.00 21.33 C ANISOU 984 C ARG B 128 3728 1844 2533 966 478 133 C ATOM 985 O ARG A 128 23.306 -21.690 21.468 1.00 27.12 O ANISOU 985 O ARG B 128 3973 2137 4195 1016 611 861 O ATOM 986 CB ARG A 128 20.365 -22.156 21.888 1.00 27.97 C ANISOU 986 CB ARG B 128 3939 2698 3989 743 -1116 425 C ATOM 987 CG ARG A 128 19.802 -21.639 20.651 1.00 32.33 C ANISOU 987 CG ARG B 128 5280 3297 3707 849 -1767 368 C ATOM 988 CD ARG A 128 19.066 -22.773 19.885 1.00 31.28 C ANISOU 988 CD ARG B 128 4902 2311 4672 1143 -1717 -199 C ATOM 989 NE ARG A 128 18.507 -22.049 18.750 1.00 29.33 N ANISOU 989 NE ARG B 128 4921 2173 4052 1015 -1708 265 N ATOM 990 CZ ARG A 128 17.295 -21.509 18.719 1.00 28.21 C ANISOU 990 CZ ARG B 128 5585 2093 3040 1291 -770 498 C ATOM 991 NH1 ARG A 128 16.910 -20.867 17.623 1.00 27.76 N ANISOU 991 NH1 ARG B 128 3713 3273 3563 695 -1076 -529 N ATOM 992 NH2 ARG A 128 16.432 -21.575 19.722 1.00 28.14 N ANISOU 992 NH2 ARG B 128 3501 3334 3856 504 -830 804 N ATOM 993 N GLY A 129 22.936 -19.574 22.110 1.00 21.73 N ANISOU 993 N GLY B 129 3600 1571 3087 635 103 -126 N ATOM 994 CA GLY A 129 24.202 -19.062 21.570 1.00 21.96 C ANISOU 994 CA GLY B 129 3576 1673 3094 526 -126 -217 C ATOM 995 C GLY A 129 24.153 -18.655 20.117 1.00 24.67 C ANISOU 995 C GLY B 129 4623 1504 3245 -100 439 -253 C ATOM 996 O GLY A 129 25.187 -18.317 19.537 1.00 23.12 O ANISOU 996 O GLY B 129 3660 1736 3387 121 -182 213 O ATOM 997 N ALA A 130 22.967 -18.674 19.534 1.00 19.64 N ANISOU 997 N ALA B 130 3207 1469 2785 464 -155 132 N ATOM 998 CA ALA A 130 22.866 -18.505 18.075 1.00 19.91 C ANISOU 998 CA ALA B 130 2908 1842 2816 219 -35 189 C ATOM 999 C ALA A 130 23.214 -17.108 17.569 1.00 19.93 C ANISOU 999 C ALA B 130 2947 1838 2786 350 70 774 C ATOM 1000 O ALA A 130 23.569 -16.967 16.395 1.00 20.82 O ANISOU 1000 O ALA B 130 3176 2053 2681 356 25 626 O ATOM 1001 CB ALA A 130 21.475 -18.908 17.554 1.00 22.16 C ANISOU 1001 CB ALA B 130 2845 2076 3498 556 -875 29 C ATOM 1002 N TRP A 131 23.122 -16.087 18.412 1.00 18.86 N ANISOU 1002 N TRP B 131 2991 1603 2571 198 -192 328 N ATOM 1003 CA TRP A 131 23.401 -14.721 18.013 1.00 17.50 C ANISOU 1003 CA TRP B 131 2778 1893 1978 46 -429 146 C ATOM 1004 C TRP A 131 24.850 -14.578 17.588 1.00 19.63 C ANISOU 1004 C TRP B 131 3140 1923 2396 12 -231 337 C ATOM 1005 O TRP A 131 25.197 -13.713 16.764 1.00 21.00 O ANISOU 1005 O TRP B 131 3258 1734 2986 -107 52 272 O ATOM 1006 CB TRP A 131 22.982 -13.752 19.129 1.00 18.94 C ANISOU 1006 CB TRP B 131 3439 1555 2203 528 -280 89 C ATOM 1007 CG TRP A 131 22.841 -12.332 18.675 1.00 17.34 C ANISOU 1007 CG TRP B 131 2999 1528 2064 172 -150 91 C ATOM 1008 CD1 TRP A 131 22.721 -11.849 17.409 1.00 17.85 C ANISOU 1008 CD1 TRP B 131 2376 2318 2088 -272 -241 -127 C ATOM 1009 CD2 TRP A 131 22.817 -11.194 19.546 1.00 16.58 C ANISOU 1009 CD2 TRP B 131 2351 1898 2051 -135 -26 139 C ATOM 1010 NE1 TRP A 131 22.609 -10.461 17.424 1.00 18.18 N ANISOU 1010 NE1 TRP B 131 2639 2142 2127 -142 109 21 N ATOM 1011 CE2 TRP A 131 22.669 -10.050 18.739 1.00 17.18 C ANISOU 1011 CE2 TRP B 131 2705 1596 2226 -1 -136 -128 C ATOM 1012 CE3 TRP A 131 22.901 -11.087 20.937 1.00 16.75 C ANISOU 1012 CE3 TRP B 131 2663 1637 2062 -240 -231 -56 C ATOM 1013 CZ2 TRP A 131 22.609 -8.775 19.286 1.00 17.69 C ANISOU 1013 CZ2 TRP B 131 2227 1933 2561 -196 -86 -83 C ATOM 1014 CZ3 TRP A 131 22.835 -9.801 21.488 1.00 17.45 C ANISOU 1014 CZ3 TRP B 131 2646 1722 2262 -276 -341 54 C ATOM 1015 CH2 TRP A 131 22.689 -8.676 20.651 1.00 18.01 C ANISOU 1015 CH2 TRP B 131 2642 1653 2546 -217 -247 140 C ATOM 1016 N LYS A 132 25.765 -15.411 18.108 1.00 21.45 N ANISOU 1016 N LYS B 132 3204 1981 2966 -220 125 139 N ATOM 1017 CA LYS A 132 27.138 -15.319 17.675 1.00 23.01 C ANISOU 1017 CA LYS B 132 3286 2133 3323 -419 367 -43 C ATOM 1018 C LYS A 132 27.310 -15.644 16.195 1.00 23.38 C ANISOU 1018 C LYS B 132 3358 2092 3435 -141 565 362 C ATOM 1019 O LYS A 132 28.316 -15.302 15.578 1.00 33.28 O ANISOU 1019 O LYS B 132 5120 3330 4193 -1564 664 766 O ATOM 1020 CB LYS A 132 28.031 -16.270 18.510 1.00 26.00 C ANISOU 1020 CB LYS B 132 3962 2068 3847 -372 508 -161 C ATOM 1021 CG LYS A 132 27.937 -15.901 19.974 1.00 35.70 C ANISOU 1021 CG LYS B 132 7295 2803 3464 -666 1004 -284 C ATOM 1022 CD LYS A 132 29.134 -16.380 20.770 1.00 45.28 C ANISOU 1022 CD LYS B 132 10082 3530 3593 -1588 1914 -867 C ATOM 1023 CE LYS A 132 28.739 -17.337 21.871 1.00 52.48 C ANISOU 1023 CE LYS B 132 10608 4234 5096 -1066 2851 -1380 C ATOM 1024 NZ LYS A 132 27.944 -18.529 21.465 1.00 61.04 N ANISOU 1024 NZ LYS B 132 10241 4419 8533 -1603 2940 1326 N ATOM 1025 N PHE A 133 26.340 -16.295 15.580 1.00 24.44 N ANISOU 1025 N PHE B 133 4307 1764 3215 -480 26 741 N ATOM 1026 CA PHE A 133 26.458 -16.659 14.175 1.00 27.23 C ANISOU 1026 CA PHE B 133 4853 2061 3431 10 -111 1116 C ATOM 1027 C PHE A 133 25.600 -15.849 13.251 1.00 25.54 C ANISOU 1027 C PHE B 133 4292 2331 3082 -355 -856 816 C ATOM 1028 O PHE A 133 25.593 -16.072 12.043 1.00 33.80 O ANISOU 1028 O PHE B 133 6138 3714 2989 -110 -350 1123 O ATOM 1029 CB PHE A 133 26.108 -18.162 14.091 1.00 30.79 C ANISOU 1029 CB PHE B 133 4909 2684 4104 171 -259 1271 C ATOM 1030 CG PHE A 133 27.055 -18.947 15.001 1.00 34.80 C ANISOU 1030 CG PHE B 133 5582 2823 4818 995 -323 1089 C ATOM 1031 CD1 PHE A 133 26.623 -19.385 16.246 1.00 39.13 C ANISOU 1031 CD1 PHE B 133 7618 2246 5003 935 386 837 C ATOM 1032 CD2 PHE A 133 28.352 -19.220 14.603 1.00 37.38 C ANISOU 1032 CD2 PHE B 133 6545 2695 4963 922 353 778 C ATOM 1033 CE1 PHE A 133 27.492 -20.081 17.074 1.00 43.11 C ANISOU 1033 CE1 PHE B 133 8542 2535 5301 1127 5 509 C ATOM 1034 CE2 PHE A 133 29.227 -19.893 15.423 1.00 42.49 C ANISOU 1034 CE2 PHE B 133 7362 3022 5759 1035 510 281 C ATOM 1035 CZ PHE A 133 28.790 -20.305 16.666 1.00 43.10 C ANISOU 1035 CZ PHE B 133 7998 2473 5903 1000 864 -11 C ATOM 1036 N GLY A 134 24.823 -14.896 13.737 1.00 23.97 N ANISOU 1036 N GLY B 134 3623 2118 3367 -351 -765 439 N ATOM 1037 CA GLY A 134 24.046 -14.057 12.843 1.00 26.69 C ANISOU 1037 CA GLY B 134 5002 2109 3029 -769 -445 471 C ATOM 1038 C GLY A 134 22.882 -13.452 13.610 1.00 23.30 C ANISOU 1038 C GLY B 134 4156 2238 2460 23 -438 530 C ATOM 1039 O GLY A 134 22.565 -13.903 14.700 1.00 21.99 O ANISOU 1039 O GLY B 134 3265 2562 2527 276 -597 545 O ATOM 1040 N ASP A 135 22.210 -12.481 13.032 1.00 21.42 N ANISOU 1040 N ASP B 135 3631 2136 2371 -735 -196 350 N ATOM 1041 CA ASP A 135 21.038 -11.879 13.562 1.00 18.71 C ANISOU 1041 CA ASP B 135 2504 2175 2428 -99 1 449 C ATOM 1042 C ASP A 135 19.797 -12.725 13.310 1.00 16.91 C ANISOU 1042 C ASP B 135 2558 1545 2322 54 -128 334 C ATOM 1043 O ASP A 135 19.633 -13.491 12.379 1.00 19.51 O ANISOU 1043 O ASP B 135 2781 2440 2191 -167 -147 484 O ATOM 1044 CB ASP A 135 20.839 -10.494 12.923 1.00 21.23 C ANISOU 1044 CB ASP B 135 2648 3115 2305 -19 126 27 C ATOM 1045 CG ASP A 135 21.864 -9.517 13.477 1.00 28.71 C ANISOU 1045 CG ASP B 135 2460 4990 3460 68 31 -638 C ATOM 1046 OD1 ASP A 135 22.444 -9.656 14.557 1.00 30.14 O ANISOU 1046 OD1 ASP B 135 2706 5764 2982 -1478 294 -287 O ATOM 1047 OD2 ASP A 135 22.033 -8.545 12.732 1.00 51.44 O ANISOU 1047 OD2 ASP B 135 2881 12099 4563 -1218 1060 -2726 O ATOM 1048 N PHE A 136 18.845 -12.502 14.226 1.00 17.21 N ANISOU 1048 N PHE B 136 2644 1319 2575 164 -116 385 N ATOM 1049 CA PHE A 136 17.514 -13.065 14.105 1.00 17.00 C ANISOU 1049 CA PHE B 136 2861 1469 2128 29 70 261 C ATOM 1050 C PHE A 136 16.766 -12.452 12.935 1.00 18.39 C ANISOU 1050 C PHE B 136 2704 2110 2174 -17 135 -44 C ATOM 1051 O PHE A 136 17.053 -11.317 12.533 1.00 16.94 O ANISOU 1051 O PHE B 136 2656 1866 1913 -76 128 193 O ATOM 1052 CB PHE A 136 16.747 -12.791 15.395 1.00 18.41 C ANISOU 1052 CB PHE B 136 2979 1939 2075 -200 15 350 C ATOM 1053 CG PHE A 136 15.489 -13.602 15.592 1.00 15.88 C ANISOU 1053 CG PHE B 136 2757 1439 1837 161 -23 254 C ATOM 1054 CD1 PHE A 136 15.589 -14.878 16.105 1.00 19.57 C ANISOU 1054 CD1 PHE B 136 2859 1753 2822 336 -40 -8 C ATOM 1055 CD2 PHE A 136 14.240 -13.063 15.296 1.00 17.46 C ANISOU 1055 CD2 PHE B 136 3309 1401 1922 -25 470 375 C ATOM 1056 CE1 PHE A 136 14.465 -15.635 16.348 1.00 21.66 C ANISOU 1056 CE1 PHE B 136 3073 2264 2894 245 555 348 C ATOM 1057 CE2 PHE A 136 13.102 -13.814 15.511 1.00 19.41 C ANISOU 1057 CE2 PHE B 136 3364 2002 2007 -412 314 -14 C ATOM 1058 CZ PHE A 136 13.224 -15.095 16.027 1.00 20.34 C ANISOU 1058 CZ PHE B 136 3191 2219 2320 -140 368 645 C ATOM 1059 N LYS A 137 15.825 -13.196 12.381 1.00 16.14 N ANISOU 1059 N LYS B 137 2632 1663 1838 430 -124 340 N ATOM 1060 CA LYS A 137 15.016 -12.708 11.274 1.00 16.13 C ANISOU 1060 CA LYS B 137 2493 1650 1984 368 -158 255 C ATOM 1061 C LYS A 137 14.236 -11.447 11.634 1.00 15.14 C ANISOU 1061 C LYS B 137 2474 1414 1865 65 -94 270 C ATOM 1062 O LYS A 137 13.971 -11.154 12.792 1.00 15.56 O ANISOU 1062 O LYS B 137 2065 1948 1901 272 -300 341 O ATOM 1063 CB LYS A 137 14.059 -13.820 10.826 1.00 18.02 C ANISOU 1063 CB LYS B 137 2596 1989 2262 253 -220 200 C ATOM 1064 CG LYS A 137 12.969 -14.089 11.842 1.00 18.33 C ANISOU 1064 CG LYS B 137 2389 2100 2475 287 -152 230 C ATOM 1065 CD LYS A 137 11.997 -15.129 11.332 1.00 21.51 C ANISOU 1065 CD LYS B 137 2507 3255 2412 -23 -221 323 C ATOM 1066 CE LYS A 137 11.067 -15.610 12.426 1.00 22.03 C ANISOU 1066 CE LYS B 137 2440 3356 2573 80 -205 547 C ATOM 1067 NZ LYS A 137 10.118 -16.617 11.856 1.00 30.10 N ANISOU 1067 NZ LYS B 137 2716 5736 2984 -963 -19 -27 N ATOM 1068 N LEU A 138 13.832 -10.714 10.599 1.00 15.05 N ANISOU 1068 N LEU B 138 2108 1562 2048 131 11 213 N ATOM 1069 CA LEU A 138 12.922 -9.578 10.805 1.00 14.50 C ANISOU 1069 CA LEU B 138 2066 1506 1939 76 21 253 C ATOM 1070 C LEU A 138 11.531 -10.096 11.143 1.00 15.04 C ANISOU 1070 C LEU B 138 2104 1755 1854 -110 -153 340 C ATOM 1071 O LEU A 138 11.072 -11.120 10.635 1.00 17.74 O ANISOU 1071 O LEU B 138 2313 1906 2522 -198 -559 589 O ATOM 1072 CB LEU A 138 12.897 -8.677 9.567 1.00 15.48 C ANISOU 1072 CB LEU B 138 2151 1541 2190 75 143 172 C ATOM 1073 CG LEU A 138 14.264 -8.192 9.114 1.00 17.00 C ANISOU 1073 CG LEU B 138 2288 2012 2159 -21 166 556 C ATOM 1074 CD1 LEU A 138 14.151 -7.212 7.959 1.00 22.32 C ANISOU 1074 CD1 LEU B 138 3260 2552 2668 -152 937 374 C ATOM 1075 CD2 LEU A 138 15.014 -7.561 10.288 1.00 18.52 C ANISOU 1075 CD2 LEU B 138 2062 2480 2493 -259 -33 737 C ATOM 1076 N THR A 139 10.882 -9.321 12.010 1.00 13.60 N ANISOU 1076 N THR B 139 1606 1641 1922 63 121 257 N ATOM 1077 CA THR A 139 9.547 -9.668 12.483 1.00 13.37 C ANISOU 1077 CA THR B 139 1826 1649 1603 -19 213 87 C ATOM 1078 C THR A 139 8.537 -8.635 12.051 1.00 13.48 C ANISOU 1078 C THR B 139 1771 1626 1725 85 37 56 C ATOM 1079 O THR A 139 8.680 -7.998 11.016 1.00 14.54 O ANISOU 1079 O THR B 139 1974 1625 1926 122 242 -14 O ATOM 1080 CB THR A 139 9.603 -9.943 14.007 1.00 13.99 C ANISOU 1080 CB THR B 139 2339 1456 1520 147 76 212 C ATOM 1081 OG1 THR A 139 9.886 -8.699 14.638 1.00 17.57 O ANISOU 1081 OG1 THR B 139 2790 1854 2031 169 -397 327 O ATOM 1082 CG2 THR A 139 10.630 -10.994 14.335 1.00 17.39 C ANISOU 1082 CG2 THR B 139 3025 1533 2051 302 493 41 C ATOM 1083 N THR A 140 7.437 -8.459 12.793 1.00 15.13 N ANISOU 1083 N THR B 140 2208 1612 1928 -28 151 64 N ATOM 1084 CA THR A 140 6.277 -7.699 12.371 1.00 14.58 C ANISOU 1084 CA THR B 140 1825 1623 2092 64 65 52 C ATOM 1085 C THR A 140 5.969 -6.573 13.330 1.00 14.18 C ANISOU 1085 C THR B 140 1754 1767 1868 39 178 89 C ATOM 1086 O THR A 140 5.848 -6.803 14.521 1.00 14.49 O ANISOU 1086 O THR B 140 1770 1878 1856 -25 156 -192 O ATOM 1087 CB THR A 140 5.067 -8.650 12.312 1.00 15.18 C ANISOU 1087 CB THR B 140 1911 1623 2234 -48 -78 367 C ATOM 1088 OG1 THR A 140 5.358 -9.728 11.380 1.00 18.20 O ANISOU 1088 OG1 THR B 140 2276 2047 2593 -92 -533 446 O ATOM 1089 CG2 THR A 140 3.838 -7.940 11.834 1.00 16.69 C ANISOU 1089 CG2 THR B 140 2393 1806 2143 -207 -129 150 C ATOM 1090 N LYS A 141 5.796 -5.371 12.785 1.00 13.59 N ANISOU 1090 N LYS B 141 2062 1545 1558 134 95 66 N ATOM 1091 CA LYS A 141 5.432 -4.211 13.567 1.00 13.71 C ANISOU 1091 CA LYS B 141 1981 1630 1599 51 25 83 C ATOM 1092 C LYS A 141 4.017 -4.311 14.103 1.00 13.66 C ANISOU 1092 C LYS B 141 1984 1490 1717 -30 -169 86 C ATOM 1093 O LYS A 141 3.096 -4.688 13.356 1.00 14.65 O ANISOU 1093 O LYS B 141 2002 1812 1751 28 -133 -204 O ATOM 1094 CB LYS A 141 5.553 -2.989 12.649 1.00 14.62 C ANISOU 1094 CB LYS B 141 1999 1622 1933 -12 49 -243 C ATOM 1095 CG LYS A 141 5.186 -1.669 13.266 1.00 14.91 C ANISOU 1095 CG LYS B 141 2153 1584 1926 92 276 -91 C ATOM 1096 CD LYS A 141 5.583 -0.487 12.409 1.00 17.89 C ANISOU 1096 CD LYS B 141 2543 1815 2441 362 609 -78 C ATOM 1097 CE LYS A 141 5.378 0.874 13.086 1.00 23.93 C ANISOU 1097 CE LYS B 141 2128 3388 3575 481 403 589 C ATOM 1098 NZ LYS A 141 5.769 1.931 12.088 1.00 37.57 N ANISOU 1098 NZ LYS B 141 2619 4945 6713 770 1930 160 N ATOM 1099 N PHE A 142 3.869 -3.999 15.379 1.00 12.97 N ANISOU 1099 N PHE B 142 1831 1396 1702 -189 -156 -22 N ATOM 1100 CA PHE A 142 2.551 -3.921 15.990 1.00 12.98 C ANISOU 1100 CA PHE B 142 1527 1668 1738 -14 -157 193 C ATOM 1101 C PHE A 142 1.897 -2.551 15.765 1.00 13.18 C ANISOU 1101 C PHE B 142 1518 1443 2047 -215 108 147 C ATOM 1102 O PHE A 142 0.751 -2.554 15.320 1.00 13.74 O ANISOU 1102 O PHE B 142 1756 1725 1738 -239 -182 -8 O ATOM 1103 CB PHE A 142 2.639 -4.236 17.491 1.00 13.85 C ANISOU 1103 CB PHE B 142 1894 1585 1783 -171 -74 81 C ATOM 1104 CG PHE A 142 1.375 -4.050 18.293 1.00 13.83 C ANISOU 1104 CG PHE B 142 1461 1865 1929 12 187 229 C ATOM 1105 CD1 PHE A 142 0.119 -4.408 17.780 1.00 14.51 C ANISOU 1105 CD1 PHE B 142 1595 1517 2402 51 -102 336 C ATOM 1106 CD2 PHE A 142 1.416 -3.529 19.576 1.00 15.10 C ANISOU 1106 CD2 PHE B 142 2472 1485 1780 22 86 82 C ATOM 1107 CE1 PHE A 142 -1.030 -4.233 18.501 1.00 14.71 C ANISOU 1107 CE1 PHE B 142 2399 1276 1914 173 608 -28 C ATOM 1108 CE2 PHE A 142 0.241 -3.373 20.307 1.00 16.76 C ANISOU 1108 CE2 PHE B 142 2328 1562 2477 110 -3 508 C ATOM 1109 CZ PHE A 142 -0.970 -3.736 19.786 1.00 15.19 C ANISOU 1109 CZ PHE B 142 2109 1575 2085 175 410 84 C ATOM 1110 N SER A 143 2.559 -1.480 16.126 1.00 13.47 N ANISOU 1110 N SER B 143 1540 1415 2162 39 98 -391 N ATOM 1111 CA SER A 143 1.910 -0.172 16.057 1.00 14.62 C ANISOU 1111 CA SER B 143 1679 1587 2290 189 615 -346 C ATOM 1112 C SER A 143 1.322 0.064 14.668 1.00 13.93 C ANISOU 1112 C SER B 143 1628 1528 2135 26 652 -252 C ATOM 1113 O SER A 143 1.970 -0.198 13.643 1.00 16.50 O ANISOU 1113 O SER B 143 2257 1688 2325 -277 351 -18 O ATOM 1114 CB SER A 143 2.934 0.942 16.327 1.00 18.00 C ANISOU 1114 CB SER B 143 1617 2496 2725 384 145 -501 C ATOM 1115 OG SER A 143 3.227 1.058 17.686 1.00 18.86 O ANISOU 1115 OG SER B 143 2395 2110 2661 -173 117 -23 O ATOM 1116 N GLY A 144 0.068 0.491 14.686 1.00 15.66 N ANISOU 1116 N GLY B 144 2603 1650 1695 -157 219 -61 N ATOM 1117 CA GLY A 144 -0.613 0.841 13.444 1.00 14.82 C ANISOU 1117 CA GLY B 144 2208 1537 1887 97 306 -196 C ATOM 1118 C GLY A 144 -1.425 -0.278 12.854 1.00 16.29 C ANISOU 1118 C GLY B 144 2292 1929 1968 -153 293 -393 C ATOM 1119 O GLY A 144 -2.229 -0.015 11.935 1.00 18.09 O ANISOU 1119 O GLY B 144 2858 1856 2161 -304 107 -381 O ATOM 1120 N LYS A 145 -1.238 -1.504 13.350 1.00 16.04 N ANISOU 1120 N LYS B 145 1934 2059 2101 -317 376 -293 N ATOM 1121 CA LYS A 145 -2.002 -2.627 12.792 1.00 16.23 C ANISOU 1121 CA LYS B 145 2319 1638 2209 -250 -135 -208 C ATOM 1122 C LYS A 145 -3.460 -2.625 13.228 1.00 15.37 C ANISOU 1122 C LYS B 145 2131 1751 1957 -283 -135 -188 C ATOM 1123 O LYS A 145 -3.790 -2.026 14.275 1.00 16.48 O ANISOU 1123 O LYS B 145 2489 1705 2068 57 -116 -119 O ATOM 1124 CB LYS A 145 -1.337 -3.953 13.198 1.00 18.66 C ANISOU 1124 CB LYS B 145 2661 1782 2647 176 -293 75 C ATOM 1125 CG LYS A 145 0.051 -4.108 12.602 1.00 24.42 C ANISOU 1125 CG LYS B 145 5367 1610 2302 -530 -1040 59 C ATOM 1126 CD LYS A 145 -0.042 -4.399 11.104 1.00 32.42 C ANISOU 1126 CD LYS B 145 7667 1786 2867 -779 -2659 665 C ATOM 1127 CE LYS A 145 1.283 -4.288 10.356 1.00 39.58 C ANISOU 1127 CE LYS B 145 9985 2428 2625 -1214 -2155 1051 C ATOM 1128 NZ LYS A 145 2.402 -4.932 10.975 1.00 28.56 N ANISOU 1128 NZ LYS B 145 4587 2138 4125 -415 992 903 N ATOM 1129 N ARG A 146 -4.332 -3.213 12.422 1.00 15.82 N ANISOU 1129 N ARG B 146 2275 1605 2132 -211 -180 -390 N ATOM 1130 CA ARG A 146 -5.776 -3.242 12.703 1.00 15.39 C ANISOU 1130 CA ARG B 146 2419 1481 1946 -210 62 -607 C ATOM 1131 C ARG A 146 -6.073 -4.294 13.749 1.00 14.59 C ANISOU 1131 C ARG B 146 2106 1611 1827 18 -223 -373 C ATOM 1132 O ARG A 146 -5.793 -5.492 13.545 1.00 16.28 O ANISOU 1132 O ARG B 146 2194 2017 1975 181 -231 -54 O ATOM 1133 CB ARG A 146 -6.540 -3.577 11.417 1.00 19.77 C ANISOU 1133 CB ARG B 146 3079 2389 2043 -855 151 -783 C ATOM 1134 CG ARG A 146 -6.316 -2.587 10.296 1.00 18.26 C ANISOU 1134 CG ARG B 146 3176 1936 1824 -218 -114 -765 C ATOM 1135 CD ARG A 146 -6.879 -3.141 8.999 1.00 20.07 C ANISOU 1135 CD ARG B 146 3153 2523 1950 -279 -251 -666 C ATOM 1136 NE ARG A 146 -6.110 -4.328 8.584 1.00 20.67 N ANISOU 1136 NE ARG B 146 2707 2776 2371 -202 -205 -484 N ATOM 1137 CZ ARG A 146 -6.480 -5.149 7.617 1.00 23.06 C ANISOU 1137 CZ ARG B 146 3235 3077 2450 152 -492 -846 C ATOM 1138 NH1 ARG A 146 -7.608 -4.915 6.970 1.00 24.69 N ANISOU 1138 NH1 ARG B 146 3288 3305 2789 -310 -496 -861 N ATOM 1139 NH2 ARG A 146 -5.746 -6.200 7.279 1.00 22.50 N ANISOU 1139 NH2 ARG B 146 3388 3218 1944 31 -255 -354 N ATOM 1140 N VAL A 147 -6.620 -3.858 14.873 1.00 14.55 N ANISOU 1140 N VAL B 147 2000 1502 2027 29 -104 -194 N ATOM 1141 CA VAL A 147 -7.008 -4.739 15.973 1.00 14.44 C ANISOU 1141 CA VAL B 147 1965 1485 2037 75 -87 -230 C ATOM 1142 C VAL A 147 -8.520 -4.874 16.006 1.00 15.76 C ANISOU 1142 C VAL B 147 2055 1610 2322 1 -102 128 C ATOM 1143 O VAL A 147 -9.228 -3.894 16.132 1.00 16.34 O ANISOU 1143 O VAL B 147 2232 1540 2436 -23 -255 -162 O ATOM 1144 CB VAL A 147 -6.460 -4.249 17.317 1.00 14.64 C ANISOU 1144 CB VAL B 147 2229 1327 2009 401 -173 -87 C ATOM 1145 CG1 VAL A 147 -6.994 -5.140 18.454 1.00 18.15 C ANISOU 1145 CG1 VAL B 147 2489 2399 2009 20 -60 -196 C ATOM 1146 CG2 VAL A 147 -4.945 -4.233 17.300 1.00 17.06 C ANISOU 1146 CG2 VAL B 147 2225 1707 2551 31 -494 -135 C ATOM 1147 N GLY A 148 -8.967 -6.118 15.843 1.00 15.98 N ANISOU 1147 N GLY B 148 2035 1512 2527 -109 -178 -138 N ATOM 1148 CA GLY A 148 -10.374 -6.476 15.953 1.00 16.64 C ANISOU 1148 CA GLY B 148 2081 1702 2539 -145 435 -234 C ATOM 1149 C GLY A 148 -10.628 -7.173 17.294 1.00 15.90 C ANISOU 1149 C GLY B 148 2078 1748 2216 134 102 -366 C ATOM 1150 O GLY A 148 -9.837 -8.038 17.651 1.00 16.93 O ANISOU 1150 O GLY B 148 2425 1830 2177 356 -152 -326 O ATOM 1151 N ILE A 149 -11.730 -6.786 17.953 1.00 14.99 N ANISOU 1151 N ILE B 149 1786 1740 2171 -72 239 -472 N ATOM 1152 CA ILE A 149 -12.034 -7.364 19.239 1.00 15.46 C ANISOU 1152 CA ILE B 149 1824 1821 2229 -28 166 -394 C ATOM 1153 C ILE A 149 -13.446 -7.953 19.236 1.00 16.85 C ANISOU 1153 C ILE B 149 2136 2135 2130 -408 367 -546 C ATOM 1154 O ILE A 149 -14.378 -7.311 18.782 1.00 17.34 O ANISOU 1154 O ILE B 149 2395 1949 2245 -389 102 -349 O ATOM 1155 CB ILE A 149 -11.903 -6.321 20.348 1.00 17.92 C ANISOU 1155 CB ILE B 149 2085 2426 2299 133 29 -251 C ATOM 1156 CG1 ILE A 149 -10.520 -5.661 20.298 1.00 18.74 C ANISOU 1156 CG1 ILE B 149 2033 2602 2485 134 -263 -82 C ATOM 1157 CG2 ILE A 149 -12.159 -6.896 21.717 1.00 22.51 C ANISOU 1157 CG2 ILE B 149 2651 3628 2273 30 100 -74 C ATOM 1158 CD1 ILE A 149 -10.394 -4.451 21.153 1.00 18.78 C ANISOU 1158 CD1 ILE B 149 2388 2558 2189 304 -374 -203 C ATOM 1159 N ILE A 150 -13.520 -9.177 19.736 1.00 15.28 N ANISOU 1159 N ILE B 150 1852 2047 1906 -291 -79 -194 N ATOM 1160 CA ILE A 150 -14.785 -9.898 19.849 1.00 15.63 C ANISOU 1160 CA ILE B 150 1919 1922 2097 -242 61 -71 C ATOM 1161 C ILE A 150 -15.251 -9.702 21.293 1.00 17.42 C ANISOU 1161 C ILE B 150 2431 2018 2171 -280 80 49 C ATOM 1162 O ILE A 150 -14.713 -10.292 22.231 1.00 18.59 O ANISOU 1162 O ILE B 150 2420 2503 2140 -246 127 -165 O ATOM 1163 CB ILE A 150 -14.712 -11.372 19.495 1.00 16.62 C ANISOU 1163 CB ILE B 150 1809 2341 2162 -129 199 -51 C ATOM 1164 CG1 ILE A 150 -14.197 -11.558 18.073 1.00 19.50 C ANISOU 1164 CG1 ILE B 150 2383 2609 2416 -476 -283 365 C ATOM 1165 CG2 ILE A 150 -16.062 -12.020 19.706 1.00 18.59 C ANISOU 1165 CG2 ILE B 150 1895 2782 2386 -340 104 12 C ATOM 1166 CD1 ILE A 150 -13.696 -12.922 17.736 1.00 24.05 C ANISOU 1166 CD1 ILE B 150 2959 3370 2811 350 120 580 C ATOM 1167 N GLY A 151 -16.256 -8.843 21.395 1.00 18.49 N ANISOU 1167 N GLY B 151 2446 2058 2521 -230 -332 177 N ATOM 1168 CA GLY A 151 -16.719 -8.420 22.716 1.00 20.95 C ANISOU 1168 CA GLY B 151 3012 2353 2596 -220 -607 303 C ATOM 1169 C GLY A 151 -16.183 -7.036 23.053 1.00 22.14 C ANISOU 1169 C GLY B 151 3050 2412 2952 -376 -786 471 C ATOM 1170 O GLY A 151 -14.983 -6.803 22.942 1.00 29.26 O ANISOU 1170 O GLY B 151 3368 2351 5397 -572 -1703 707 O ATOM 1171 N LEU A 152 -17.060 -6.142 23.457 1.00 19.52 N ANISOU 1171 N LEU B 152 2509 2257 2650 -139 -8 142 N ATOM 1172 CA LEU A 152 -16.635 -4.806 23.886 1.00 18.95 C ANISOU 1172 CA LEU B 152 2333 2589 2280 -136 329 275 C ATOM 1173 C LEU A 152 -17.235 -4.467 25.250 1.00 18.87 C ANISOU 1173 C LEU B 152 2818 2288 2065 -327 49 43 C ATOM 1174 O LEU A 152 -17.764 -3.386 25.518 1.00 23.15 O ANISOU 1174 O LEU B 152 3210 2638 2946 -111 -346 346 O ATOM 1175 CB LEU A 152 -16.954 -3.741 22.839 1.00 19.58 C ANISOU 1175 CB LEU B 152 2663 2688 2089 40 154 231 C ATOM 1176 CG LEU A 152 -16.019 -2.527 22.933 1.00 21.36 C ANISOU 1176 CG LEU B 152 2552 2855 2708 322 444 352 C ATOM 1177 CD1 LEU A 152 -14.632 -2.874 22.449 1.00 22.26 C ANISOU 1177 CD1 LEU B 152 3005 2887 2566 -328 61 -9 C ATOM 1178 CD2 LEU A 152 -16.597 -1.329 22.180 1.00 20.61 C ANISOU 1178 CD2 LEU B 152 2637 2997 2198 7 278 -19 C ATOM 1179 N GLY A 153 -17.115 -5.436 26.151 1.00 19.80 N ANISOU 1179 N GLY B 153 2948 2608 1967 -607 74 -145 N ATOM 1180 CA GLY A 153 -17.422 -5.287 27.556 1.00 18.78 C ANISOU 1180 CA GLY B 153 2371 2707 2057 -342 0 -31 C ATOM 1181 C GLY A 153 -16.161 -4.751 28.244 1.00 16.46 C ANISOU 1181 C GLY B 153 2272 2219 1762 -328 60 418 C ATOM 1182 O GLY A 153 -15.284 -4.180 27.605 1.00 17.62 O ANISOU 1182 O GLY B 153 2449 2072 2173 -249 314 487 O ATOM 1183 N ARG A 154 -16.053 -4.990 29.542 1.00 18.21 N ANISOU 1183 N ARG B 154 2795 2266 1857 -673 237 129 N ATOM 1184 CA ARG A 154 -14.965 -4.424 30.310 1.00 20.51 C ANISOU 1184 CA ARG B 154 3441 2045 2308 -704 -282 105 C ATOM 1185 C ARG A 154 -13.588 -4.836 29.786 1.00 17.78 C ANISOU 1185 C ARG B 154 2706 1903 2148 -261 197 89 C ATOM 1186 O ARG A 154 -12.664 -4.010 29.631 1.00 16.63 O ANISOU 1186 O ARG B 154 2540 1885 1895 -1 170 48 O ATOM 1187 CB ARG A 154 -15.118 -4.879 31.769 1.00 26.20 C ANISOU 1187 CB ARG B 154 5267 2742 1947 -1720 -427 319 C ATOM 1188 CG ARG A 154 -16.212 -4.173 32.546 1.00 37.60 C ANISOU 1188 CG ARG B 154 8375 2974 2937 -2882 -845 873 C ATOM 1189 CD ARG A 154 -16.697 -5.076 33.682 1.00 57.17 C ANISOU 1189 CD ARG B 154 11068 5847 4806 -5121 1483 1404 C ATOM 1190 NE ARG A 154 -17.727 -4.601 34.561 1.00 67.34 N ANISOU 1190 NE ARG B 154 12982 6381 6224 -5042 1596 2293 N ATOM 1191 CZ ARG A 154 -19.025 -4.853 34.527 1.00 72.97 C ANISOU 1191 CZ ARG B 154 13030 6495 8201 -5157 1535 3362 C ATOM 1192 NH1 ARG A 154 -19.606 -5.621 33.613 1.00 71.30 N ANISOU 1192 NH1 ARG B 154 10094 5371 11624 -3273 1373 2164 N ATOM 1193 NH2 ARG A 154 -19.808 -4.310 35.450 1.00 93.49 N ANISOU 1193 NH2 ARG B 154 18790 6062 10672 -5274 343 4243 N ATOM 1194 N ILE A 155 -13.387 -6.132 29.496 1.00 19.39 N ANISOU 1194 N ILE B 155 2466 2378 2523 -150 545 300 N ATOM 1195 CA ILE A 155 -12.052 -6.547 29.072 1.00 18.25 C ANISOU 1195 CA ILE B 155 2252 2089 2594 45 375 81 C ATOM 1196 C ILE A 155 -11.780 -6.106 27.650 1.00 16.36 C ANISOU 1196 C ILE B 155 2212 1607 2398 70 114 253 C ATOM 1197 O ILE A 155 -10.674 -5.613 27.339 1.00 17.02 O ANISOU 1197 O ILE B 155 2230 1885 2354 -195 -92 309 O ATOM 1198 CB ILE A 155 -11.860 -8.064 29.304 1.00 19.97 C ANISOU 1198 CB ILE B 155 2100 2757 2732 203 503 589 C ATOM 1199 CG1 ILE A 155 -11.759 -8.378 30.823 1.00 23.65 C ANISOU 1199 CG1 ILE B 155 2324 3842 2822 615 937 514 C ATOM 1200 CG2 ILE A 155 -10.677 -8.607 28.539 1.00 20.78 C ANISOU 1200 CG2 ILE B 155 2343 2692 2860 355 45 600 C ATOM 1201 CD1 ILE A 155 -11.849 -9.826 31.186 1.00 26.14 C ANISOU 1201 CD1 ILE B 155 2428 3718 3788 598 963 268 C ATOM 1202 N GLY A 156 -12.755 -6.206 26.770 1.00 18.05 N ANISOU 1202 N GLY B 156 2285 2000 2571 -523 599 81 N ATOM 1203 CA GLY A 156 -12.554 -5.770 25.400 1.00 17.26 C ANISOU 1203 CA GLY B 156 2165 2114 2281 -347 132 286 C ATOM 1204 C GLY A 156 -12.230 -4.291 25.322 1.00 16.50 C ANISOU 1204 C GLY B 156 2361 2115 1795 -51 204 151 C ATOM 1205 O GLY A 156 -11.364 -3.899 24.517 1.00 15.58 O ANISOU 1205 O GLY B 156 2094 1997 1830 -133 -49 272 O ATOM 1206 N LEU A 157 -12.940 -3.500 26.141 1.00 16.42 N ANISOU 1206 N LEU B 157 2203 1810 2226 -355 329 274 N ATOM 1207 CA LEU A 157 -12.648 -2.059 26.121 1.00 16.67 C ANISOU 1207 CA LEU B 157 2353 1989 1992 -158 45 292 C ATOM 1208 C LEU A 157 -11.252 -1.799 26.639 1.00 15.52 C ANISOU 1208 C LEU B 157 1932 1752 2212 124 347 183 C ATOM 1209 O LEU A 157 -10.576 -0.902 26.113 1.00 16.79 O ANISOU 1209 O LEU B 157 2083 1870 2427 95 505 308 O ATOM 1210 CB LEU A 157 -13.656 -1.300 26.937 1.00 19.25 C ANISOU 1210 CB LEU B 157 3365 1726 2223 -55 34 274 C ATOM 1211 CG LEU A 157 -14.047 0.137 26.662 1.00 33.77 C ANISOU 1211 CG LEU B 157 6958 2720 3153 1890 1193 333 C ATOM 1212 CD1 LEU A 157 -14.399 0.410 25.199 1.00 38.61 C ANISOU 1212 CD1 LEU B 157 7704 3766 3200 3207 40 -132 C ATOM 1213 CD2 LEU A 157 -15.233 0.502 27.556 1.00 51.16 C ANISOU 1213 CD2 LEU B 157 14646 1685 3109 976 -2660 533 C ATOM 1214 N ALA A 158 -10.839 -2.509 27.667 1.00 15.36 N ANISOU 1214 N ALA B 158 2290 1633 1913 120 311 310 N ATOM 1215 CA ALA A 158 -9.494 -2.308 28.214 1.00 14.64 C ANISOU 1215 CA ALA B 158 1710 1854 2000 171 331 271 C ATOM 1216 C ALA A 158 -8.426 -2.685 27.202 1.00 14.51 C ANISOU 1216 C ALA B 158 1554 1892 2067 -10 136 352 C ATOM 1217 O ALA A 158 -7.387 -2.014 27.103 1.00 14.72 O ANISOU 1217 O ALA B 158 1593 1732 2270 -82 70 63 O ATOM 1218 CB ALA A 158 -9.372 -3.054 29.531 1.00 15.47 C ANISOU 1218 CB ALA B 158 1962 2083 1830 -20 105 178 C ATOM 1219 N VAL A 159 -8.659 -3.740 26.420 1.00 14.33 N ANISOU 1219 N VAL B 159 1745 1710 1987 -129 -53 101 N ATOM 1220 CA VAL A 159 -7.716 -4.091 25.362 1.00 14.19 C ANISOU 1220 CA VAL B 159 1944 1462 1985 181 -11 53 C ATOM 1221 C VAL A 159 -7.682 -2.998 24.314 1.00 12.71 C ANISOU 1221 C VAL B 159 1728 1229 1872 145 -107 178 C ATOM 1222 O VAL A 159 -6.593 -2.604 23.863 1.00 13.61 O ANISOU 1222 O VAL B 159 1869 1365 1937 24 -71 184 O ATOM 1223 CB VAL A 159 -8.057 -5.441 24.725 1.00 13.21 C ANISOU 1223 CB VAL B 159 1714 1483 1822 -1 208 85 C ATOM 1224 CG1 VAL A 159 -7.229 -5.715 23.479 1.00 13.70 C ANISOU 1224 CG1 VAL B 159 1406 2072 1729 52 203 275 C ATOM 1225 CG2 VAL A 159 -7.878 -6.540 25.772 1.00 15.29 C ANISOU 1225 CG2 VAL B 159 1883 2260 1668 173 254 30 C ATOM 1226 N ALA A 160 -8.870 -2.536 23.899 1.00 14.47 N ANISOU 1226 N ALA B 160 1858 1378 2261 35 228 3 N ATOM 1227 CA ALA A 160 -8.947 -1.491 22.887 1.00 15.47 C ANISOU 1227 CA ALA B 160 1954 1431 2494 357 150 -72 C ATOM 1228 C ALA A 160 -8.180 -0.242 23.305 1.00 15.83 C ANISOU 1228 C ALA B 160 1879 1670 2464 86 191 259 C ATOM 1229 O ALA A 160 -7.448 0.357 22.499 1.00 15.78 O ANISOU 1229 O ALA B 160 2120 1612 2264 12 199 147 O ATOM 1230 CB ALA A 160 -10.407 -1.109 22.606 1.00 15.83 C ANISOU 1230 CB ALA B 160 2337 1649 2030 72 99 -195 C ATOM 1231 N GLU A 161 -8.402 0.197 24.547 1.00 15.37 N ANISOU 1231 N GLU B 161 1765 1673 2402 60 300 268 N ATOM 1232 CA GLU A 161 -7.768 1.423 25.036 1.00 14.41 C ANISOU 1232 CA GLU B 161 1739 1556 2181 193 402 128 C ATOM 1233 C GLU A 161 -6.250 1.325 25.099 1.00 14.89 C ANISOU 1233 C GLU B 161 1806 1581 2272 133 279 199 C ATOM 1234 O GLU A 161 -5.513 2.285 24.827 1.00 17.07 O ANISOU 1234 O GLU B 161 1781 1809 2897 108 290 151 O ATOM 1235 CB GLU A 161 -8.395 1.756 26.411 1.00 16.83 C ANISOU 1235 CB GLU B 161 2304 1694 2397 222 269 385 C ATOM 1236 CG GLU A 161 -9.855 2.203 26.192 1.00 20.04 C ANISOU 1236 CG GLU B 161 2469 1608 3537 218 355 498 C ATOM 1237 CD GLU A 161 -10.713 2.210 27.430 1.00 22.86 C ANISOU 1237 CD GLU B 161 3142 2179 3363 -856 -339 592 C ATOM 1238 OE1 GLU A 161 -10.239 1.817 28.527 1.00 25.81 O ANISOU 1238 OE1 GLU B 161 4060 2649 3098 -405 -557 673 O ATOM 1239 OE2 GLU A 161 -11.922 2.602 27.307 1.00 35.40 O ANISOU 1239 OE2 GLU B 161 7166 2282 4001 -1604 -313 761 O ATOM 1240 N ARG A 162 -5.736 0.142 25.442 1.00 13.96 N ANISOU 1240 N ARG B 162 1951 1497 1854 69 439 276 N ATOM 1241 CA ARG A 162 -4.284 -0.050 25.339 1.00 13.33 C ANISOU 1241 CA ARG B 162 1597 1529 1938 94 -62 342 C ATOM 1242 C ARG A 162 -3.812 -0.022 23.889 1.00 12.80 C ANISOU 1242 C ARG B 162 1494 1408 1961 50 -58 378 C ATOM 1243 O ARG A 162 -2.832 0.644 23.547 1.00 14.46 O ANISOU 1243 O ARG B 162 1693 1614 2187 -137 309 -81 O ATOM 1244 CB ARG A 162 -3.887 -1.370 26.012 1.00 13.56 C ANISOU 1244 CB ARG B 162 1683 1501 1969 85 -76 226 C ATOM 1245 CG ARG A 162 -3.937 -1.307 27.532 1.00 13.27 C ANISOU 1245 CG ARG B 162 1294 1760 1989 58 -183 128 C ATOM 1246 CD ARG A 162 -4.294 -2.647 28.146 1.00 14.34 C ANISOU 1246 CD ARG B 162 1469 1945 2033 308 -176 -10 C ATOM 1247 NE ARG A 162 -4.221 -2.545 29.599 1.00 15.08 N ANISOU 1247 NE ARG B 162 2172 1575 1982 -358 116 -18 N ATOM 1248 CZ ARG A 162 -5.087 -1.944 30.396 1.00 14.41 C ANISOU 1248 CZ ARG B 162 1872 1681 1920 -118 40 -19 C ATOM 1249 NH1 ARG A 162 -6.157 -1.376 29.849 1.00 16.18 N ANISOU 1249 NH1 ARG B 162 2243 1618 2286 -331 -22 -7 N ATOM 1250 NH2 ARG A 162 -4.887 -1.917 31.693 1.00 18.42 N ANISOU 1250 NH2 ARG B 162 2879 2332 1787 -231 315 -14 N ATOM 1251 N ALA A 163 -4.500 -0.752 23.017 1.00 12.77 N ANISOU 1251 N ALA B 163 1553 1465 1834 240 -18 123 N ATOM 1252 CA ALA A 163 -4.073 -0.826 21.619 1.00 13.81 C ANISOU 1252 CA ALA B 163 1822 1652 1773 147 33 20 C ATOM 1253 C ALA A 163 -4.173 0.530 20.941 1.00 14.35 C ANISOU 1253 C ALA B 163 2090 1456 1905 53 357 193 C ATOM 1254 O ALA A 163 -3.329 0.806 20.069 1.00 14.35 O ANISOU 1254 O ALA B 163 1861 1684 1906 -206 155 150 O ATOM 1255 CB ALA A 163 -4.843 -1.885 20.840 1.00 15.10 C ANISOU 1255 CB ALA B 163 2207 1664 1867 96 -281 -169 C ATOM 1256 N GLU A 164 -5.091 1.394 21.314 1.00 15.25 N ANISOU 1256 N GLU B 164 1738 1503 2551 21 358 263 N ATOM 1257 CA GLU A 164 -5.144 2.703 20.710 1.00 15.58 C ANISOU 1257 CA GLU B 164 1918 1820 2183 218 106 -70 C ATOM 1258 C GLU A 164 -3.856 3.502 20.949 1.00 15.44 C ANISOU 1258 C GLU B 164 1678 1666 2522 434 110 -203 C ATOM 1259 O GLU A 164 -3.476 4.373 20.164 1.00 16.19 O ANISOU 1259 O GLU B 164 1983 1732 2435 198 270 -97 O ATOM 1260 CB GLU A 164 -6.308 3.509 21.282 1.00 19.91 C ANISOU 1260 CB GLU B 164 2363 1607 3593 336 741 -29 C ATOM 1261 CG GLU A 164 -7.670 3.211 20.760 1.00 23.24 C ANISOU 1261 CG GLU B 164 3120 1962 3747 -18 206 -17 C ATOM 1262 CD GLU A 164 -8.681 4.168 21.395 1.00 20.80 C ANISOU 1262 CD GLU B 164 2562 1801 3540 -53 405 -186 C ATOM 1263 OE1 GLU A 164 -9.180 3.906 22.502 1.00 25.05 O ANISOU 1263 OE1 GLU B 164 3436 2731 3351 196 318 169 O ATOM 1264 OE2 GLU A 164 -8.959 5.184 20.721 1.00 31.98 O ANISOU 1264 OE2 GLU B 164 4253 2458 5438 691 1822 -147 O ATOM 1265 N ALA A 165 -3.156 3.198 22.043 1.00 14.64 N ANISOU 1265 N ALA B 165 1789 1644 2130 308 -9 67 N ATOM 1266 CA ALA A 165 -1.917 3.944 22.378 1.00 15.06 C ANISOU 1266 CA ALA B 165 1770 2064 1889 237 121 16 C ATOM 1267 C ALA A 165 -0.752 3.517 21.499 1.00 15.52 C ANISOU 1267 C ALA B 165 1534 2048 2315 217 110 171 C ATOM 1268 O ALA A 165 0.285 4.200 21.547 1.00 17.49 O ANISOU 1268 O ALA B 165 1809 2396 2440 -126 -159 81 O ATOM 1269 CB ALA A 165 -1.606 3.772 23.866 1.00 18.22 C ANISOU 1269 CB ALA B 165 2413 2555 1953 -29 42 -154 C ATOM 1270 N PHE A 166 -0.962 2.462 20.734 1.00 14.53 N ANISOU 1270 N PHE B 166 1534 1728 2259 35 80 104 N ATOM 1271 CA PHE A 166 -0.011 1.965 19.735 1.00 14.52 C ANISOU 1271 CA PHE B 166 1493 1811 2211 -63 -183 20 C ATOM 1272 C PHE A 166 -0.480 2.381 18.341 1.00 15.46 C ANISOU 1272 C PHE B 166 1737 1982 2157 376 -289 -2 C ATOM 1273 O PHE A 166 -0.037 1.809 17.352 1.00 16.59 O ANISOU 1273 O PHE B 166 2103 2020 2180 8 -6 208 O ATOM 1274 CB PHE A 166 0.166 0.475 19.848 1.00 14.46 C ANISOU 1274 CB PHE B 166 1706 1687 2101 47 -244 -107 C ATOM 1275 CG PHE A 166 0.696 -0.013 21.164 1.00 14.92 C ANISOU 1275 CG PHE B 166 1770 1797 2101 -431 -40 -172 C ATOM 1276 CD1 PHE A 166 2.019 -0.397 21.301 1.00 13.89 C ANISOU 1276 CD1 PHE B 166 1468 1730 2080 -146 -249 -148 C ATOM 1277 CD2 PHE A 166 -0.123 -0.137 22.273 1.00 15.69 C ANISOU 1277 CD2 PHE B 166 1688 1877 2397 -106 341 -169 C ATOM 1278 CE1 PHE A 166 2.574 -0.863 22.473 1.00 14.61 C ANISOU 1278 CE1 PHE B 166 1903 1664 1986 -232 -33 -72 C ATOM 1279 CE2 PHE A 166 0.407 -0.586 23.455 1.00 15.12 C ANISOU 1279 CE2 PHE B 166 1811 1602 2331 7 343 -70 C ATOM 1280 CZ PHE A 166 1.713 -0.983 23.540 1.00 16.22 C ANISOU 1280 CZ PHE B 166 2084 1794 2283 -395 193 -77 C ATOM 1281 N ASP A 167 -1.393 3.341 18.269 1.00 15.92 N ANISOU 1281 N ASP B 167 1827 1820 2401 105 169 37 N ATOM 1282 CA ASP A 167 -1.922 3.863 17.030 1.00 16.45 C ANISOU 1282 CA ASP B 167 1818 1863 2571 -47 420 -39 C ATOM 1283 C ASP A 167 -2.676 2.815 16.232 1.00 15.54 C ANISOU 1283 C ASP B 167 1864 1751 2291 257 492 -430 C ATOM 1284 O ASP A 167 -2.808 2.984 15.021 1.00 18.07 O ANISOU 1284 O ASP B 167 2329 2283 2253 299 555 -324 O ATOM 1285 CB ASP A 167 -0.862 4.486 16.095 1.00 16.89 C ANISOU 1285 CB ASP B 167 2169 1663 2586 -205 502 -233 C ATOM 1286 CG ASP A 167 -0.261 5.752 16.668 1.00 25.54 C ANISOU 1286 CG ASP B 167 1794 3460 4451 70 793 1116 C ATOM 1287 OD1 ASP A 167 -0.834 6.391 17.582 1.00 25.80 O ANISOU 1287 OD1 ASP B 167 3075 2842 3885 516 -112 182 O ATOM 1288 OD2 ASP A 167 0.829 6.066 16.152 1.00 44.92 O ANISOU 1288 OD2 ASP B 167 2523 6372 8173 -1489 495 3040 O ATOM 1289 N CYS A 168 -3.232 1.807 16.877 1.00 14.47 N ANISOU 1289 N CYS B 168 1784 1912 1802 159 174 -109 N ATOM 1290 CA CYS A 168 -3.995 0.758 16.203 1.00 15.20 C ANISOU 1290 CA CYS B 168 1859 1721 2195 33 52 -236 C ATOM 1291 C CYS A 168 -5.421 1.215 15.969 1.00 15.78 C ANISOU 1291 C CYS B 168 2334 1639 2023 114 -70 -147 C ATOM 1292 O CYS A 168 -6.087 1.548 16.968 1.00 17.08 O ANISOU 1292 O CYS B 168 2477 1854 2158 277 115 12 O ATOM 1293 CB CYS A 168 -4.036 -0.527 17.032 1.00 14.50 C ANISOU 1293 CB CYS B 168 1830 1598 2083 255 -8 75 C ATOM 1294 SG CYS A 168 -2.388 -1.231 17.316 1.00 16.76 S ANISOU 1294 SG CYS B 168 2141 1802 2423 110 -63 -403 S ATOM 1295 N PRO A 169 -5.875 1.185 14.720 1.00 16.03 N ANISOU 1295 N PRO B 169 2323 1693 2075 65 -51 -172 N ATOM 1296 CA PRO A 169 -7.320 1.363 14.505 1.00 17.95 C ANISOU 1296 CA PRO B 169 2763 1752 2305 -143 440 -477 C ATOM 1297 C PRO A 169 -8.053 0.182 15.130 1.00 16.69 C ANISOU 1297 C PRO B 169 2453 1636 2251 25 83 -184 C ATOM 1298 O PRO A 169 -7.621 -0.964 14.960 1.00 16.89 O ANISOU 1298 O PRO B 169 2623 1550 2243 -32 -56 -225 O ATOM 1299 CB PRO A 169 -7.491 1.356 13.007 1.00 18.50 C ANISOU 1299 CB PRO B 169 2484 2153 2391 -145 174 -640 C ATOM 1300 CG PRO A 169 -6.161 1.361 12.402 1.00 20.99 C ANISOU 1300 CG PRO B 169 3672 2208 2097 -283 -155 -256 C ATOM 1301 CD PRO A 169 -5.144 1.000 13.456 1.00 16.21 C ANISOU 1301 CD PRO B 169 2125 2031 2002 -83 -115 -149 C ATOM 1302 N ILE A 170 -9.139 0.471 15.817 1.00 15.61 N ANISOU 1302 N ILE B 170 2155 1634 2143 118 38 -236 N ATOM 1303 CA ILE A 170 -9.932 -0.511 16.561 1.00 15.72 C ANISOU 1303 CA ILE B 170 2087 1732 2153 27 -16 -267 C ATOM 1304 C ILE A 170 -11.256 -0.813 15.880 1.00 16.18 C ANISOU 1304 C ILE B 170 2310 1698 2141 -39 132 -355 C ATOM 1305 O ILE A 170 -11.967 0.120 15.534 1.00 18.51 O ANISOU 1305 O ILE B 170 2967 1683 2383 127 21 -421 O ATOM 1306 CB ILE A 170 -10.208 -0.036 18.004 1.00 16.52 C ANISOU 1306 CB ILE B 170 2198 1943 2136 149 73 -219 C ATOM 1307 CG1 ILE A 170 -8.916 0.443 18.679 1.00 18.13 C ANISOU 1307 CG1 ILE B 170 2784 1653 2451 185 -585 25 C ATOM 1308 CG2 ILE A 170 -10.923 -1.093 18.821 1.00 19.80 C ANISOU 1308 CG2 ILE B 170 2817 1951 2756 213 710 -1 C ATOM 1309 CD1 ILE A 170 -7.808 -0.594 18.801 1.00 19.19 C ANISOU 1309 CD1 ILE B 170 2345 1665 3283 73 156 24 C ATOM 1310 N SER A 171 -11.548 -2.078 15.749 1.00 15.82 N ANISOU 1310 N SER B 171 2255 1597 2161 -211 -125 -169 N ATOM 1311 CA SER A 171 -12.843 -2.549 15.258 1.00 17.27 C ANISOU 1311 CA SER B 171 2486 2014 2060 -446 110 -505 C ATOM 1312 C SER A 171 -13.344 -3.631 16.236 1.00 16.16 C ANISOU 1312 C SER B 171 2166 1905 2067 -183 -135 -591 C ATOM 1313 O SER A 171 -12.570 -4.262 16.933 1.00 17.16 O ANISOU 1313 O SER B 171 2450 1668 2401 8 -167 -556 O ATOM 1314 CB SER A 171 -12.715 -3.127 13.857 1.00 16.73 C ANISOU 1314 CB SER B 171 2308 1911 2137 -282 34 -591 C ATOM 1315 OG SER A 171 -12.245 -2.127 12.969 1.00 17.83 O ANISOU 1315 OG SER B 171 2577 2136 2062 -40 154 -469 O ATOM 1316 N TYR A 172 -14.676 -3.819 16.235 1.00 16.64 N ANISOU 1316 N TYR B 172 2316 1857 2149 -276 70 -477 N ATOM 1317 CA TYR A 172 -15.153 -4.835 17.164 1.00 15.25 C ANISOU 1317 CA TYR B 172 1938 1827 2028 66 -261 -515 C ATOM 1318 C TYR A 172 -16.434 -5.453 16.621 1.00 15.25 C ANISOU 1318 C TYR B 172 2164 1547 2083 -12 -205 -421 C ATOM 1319 O TYR A 172 -17.111 -4.892 15.771 1.00 17.38 O ANISOU 1319 O TYR B 172 2538 1544 2521 -508 79 -653 O ATOM 1320 CB TYR A 172 -15.360 -4.258 18.569 1.00 16.71 C ANISOU 1320 CB TYR B 172 2323 2022 2005 -102 -216 -330 C ATOM 1321 CG TYR A 172 -16.565 -3.334 18.631 1.00 17.03 C ANISOU 1321 CG TYR B 172 2667 2089 1714 61 323 -265 C ATOM 1322 CD1 TYR A 172 -17.784 -3.756 19.163 1.00 19.69 C ANISOU 1322 CD1 TYR B 172 3199 2083 2201 -142 724 -344 C ATOM 1323 CD2 TYR A 172 -16.504 -2.037 18.160 1.00 18.35 C ANISOU 1323 CD2 TYR B 172 3049 2135 1789 226 588 -102 C ATOM 1324 CE1 TYR A 172 -18.870 -2.926 19.231 1.00 19.27 C ANISOU 1324 CE1 TYR B 172 3300 2076 1945 -109 245 -400 C ATOM 1325 CE2 TYR A 172 -17.611 -1.207 18.207 1.00 18.58 C ANISOU 1325 CE2 TYR B 172 3107 2128 1824 413 147 114 C ATOM 1326 CZ TYR A 172 -18.799 -1.635 18.737 1.00 19.50 C ANISOU 1326 CZ TYR B 172 3259 2068 2082 95 123 -162 C ATOM 1327 OH TYR A 172 -19.885 -0.772 18.761 1.00 22.74 O ANISOU 1327 OH TYR B 172 3857 2064 2718 223 168 5 O ATOM 1328 N PHE A 173 -16.775 -6.626 17.128 1.00 16.36 N ANISOU 1328 N PHE B 173 1942 1894 2379 -42 -215 -145 N ATOM 1329 CA PHE A 173 -18.029 -7.290 16.981 1.00 16.82 C ANISOU 1329 CA PHE B 173 2328 2010 2053 -371 -310 -449 C ATOM 1330 C PHE A 173 -18.721 -7.374 18.338 1.00 18.77 C ANISOU 1330 C PHE B 173 2560 2264 2307 -458 239 -539 C ATOM 1331 O PHE A 173 -18.140 -7.669 19.385 1.00 20.09 O ANISOU 1331 O PHE B 173 2953 2469 2209 -506 116 -485 O ATOM 1332 CB PHE A 173 -17.843 -8.713 16.425 1.00 18.03 C ANISOU 1332 CB PHE B 173 1838 2757 2256 -161 -96 -710 C ATOM 1333 CG PHE A 173 -19.112 -9.531 16.521 1.00 18.69 C ANISOU 1333 CG PHE B 173 2146 2500 2455 -384 216 -758 C ATOM 1334 CD1 PHE A 173 -20.114 -9.334 15.575 1.00 22.68 C ANISOU 1334 CD1 PHE B 173 2814 3538 2266 -1021 -65 -866 C ATOM 1335 CD2 PHE A 173 -19.296 -10.493 17.517 1.00 23.68 C ANISOU 1335 CD2 PHE B 173 2449 3612 2937 -527 644 -897 C ATOM 1336 CE1 PHE A 173 -21.274 -10.090 15.659 1.00 25.24 C ANISOU 1336 CE1 PHE B 173 3184 3712 2695 -1402 -58 -727 C ATOM 1337 CE2 PHE A 173 -20.469 -11.218 17.638 1.00 26.71 C ANISOU 1337 CE2 PHE B 173 2489 4105 3556 -615 800 -869 C ATOM 1338 CZ PHE A 173 -21.458 -10.997 16.695 1.00 26.52 C ANISOU 1338 CZ PHE B 173 2005 4125 3944 -393 -167 -804 C ATOM 1339 N SER A 174 -20.002 -7.154 18.364 1.00 19.44 N ANISOU 1339 N SER B 174 2436 2426 2524 -679 247 -430 N ATOM 1340 CA SER A 174 -20.909 -7.336 19.467 1.00 23.19 C ANISOU 1340 CA SER B 174 2669 2856 3286 -638 1209 -436 C ATOM 1341 C SER A 174 -22.295 -7.625 18.919 1.00 26.18 C ANISOU 1341 C SER B 174 2750 3387 3812 -1113 952 -115 C ATOM 1342 O SER A 174 -22.576 -7.271 17.763 1.00 26.12 O ANISOU 1342 O SER B 174 2967 2679 4279 -1059 1073 -632 O ATOM 1343 CB SER A 174 -20.951 -6.051 20.297 1.00 27.61 C ANISOU 1343 CB SER B 174 3984 2936 3572 -1782 94 822 C ATOM 1344 OG SER A 174 -21.702 -6.453 21.423 1.00 36.64 O ANISOU 1344 OG SER B 174 4954 5079 3890 -2052 762 904 O ATOM 1345 N ARG A 175 -23.128 -8.248 19.738 1.00 36.26 N ANISOU 1345 N ARG B 175 4065 4705 5008 -2158 2034 -596 N ATOM 1346 CA ARG A 175 -24.489 -8.545 19.277 1.00 39.00 C ANISOU 1346 CA ARG B 175 3718 5416 5683 -2403 2356 -1011 C ATOM 1347 C ARG A 175 -25.192 -7.309 18.737 1.00 38.04 C ANISOU 1347 C ARG B 175 4226 4787 5440 -2177 1344 -710 C ATOM 1348 O ARG A 175 -25.877 -7.308 17.704 1.00 34.09 O ANISOU 1348 O ARG B 175 5117 3381 4454 -1391 737 572 O ATOM 1349 CB ARG A 175 -25.289 -9.136 20.446 1.00 53.17 C ANISOU 1349 CB ARG B 175 6091 7315 6798 -4095 3792 -1467 C ATOM 1350 CG ARG A 175 -26.782 -9.269 20.043 1.00 65.18 C ANISOU 1350 CG ARG B 175 8672 7777 8314 -5640 4729 -1672 C ATOM 1351 CD ARG A 175 -27.639 -9.515 21.270 1.00 71.63 C ANISOU 1351 CD ARG B 175 9055 8443 9720 -5153 6825 -1890 C ATOM 1352 NE ARG A 175 -27.338 -10.830 21.840 1.00 81.93 N ANISOU 1352 NE ARG B 175 10083 10022 11023 -3696 6413 -2397 N ATOM 1353 CZ ARG A 175 -27.707 -11.976 21.271 1.00 88.25 C ANISOU 1353 CZ ARG B 175 10462 10936 12132 -3158 5931 -2419 C ATOM 1354 NH1 ARG A 175 -28.385 -11.950 20.126 1.00 92.10 N ANISOU 1354 NH1 ARG B 175 10283 10130 14583 -2333 4374 -3901 N ATOM 1355 NH2 ARG A 175 -27.381 -13.116 21.875 1.00 88.38 N ANISOU 1355 NH2 ARG B 175 10314 13206 10060 -2589 6641 -1786 N ATOM 1356 N SER A 176 -24.997 -6.227 19.475 1.00 34.85 N ANISOU 1356 N SER B 176 4898 4264 4081 -2463 1341 -505 N ATOM 1357 CA SER A 176 -25.507 -4.917 19.132 1.00 35.22 C ANISOU 1357 CA SER B 176 5518 4307 3559 -1846 860 30 C ATOM 1358 C SER A 176 -24.409 -3.880 19.094 1.00 33.09 C ANISOU 1358 C SER B 176 5372 3485 3715 -1501 1065 97 C ATOM 1359 O SER A 176 -23.442 -3.909 19.828 1.00 36.82 O ANISOU 1359 O SER B 176 4940 4558 4493 -1434 1103 -801 O ATOM 1360 CB SER A 176 -26.593 -4.498 20.151 1.00 46.90 C ANISOU 1360 CB SER B 176 7872 4266 5683 -2835 1701 702 C ATOM 1361 OG SER A 176 -27.756 -5.243 19.870 1.00 46.97 O ANISOU 1361 OG SER B 176 8024 3787 6035 -2314 216 1284 O ATOM 1362 N LYS A 177 -24.492 -2.880 18.227 1.00 30.95 N ANISOU 1362 N LYS B 177 5402 2784 3573 -681 553 539 N ATOM 1363 CA LYS A 177 -23.515 -1.801 18.285 1.00 30.16 C ANISOU 1363 CA LYS B 177 5469 2925 3067 -886 986 466 C ATOM 1364 C LYS A 177 -23.585 -1.019 19.589 1.00 28.68 C ANISOU 1364 C LYS B 177 4983 1958 3957 21 805 676 C ATOM 1365 O LYS A 177 -24.632 -0.704 20.188 1.00 36.05 O ANISOU 1365 O LYS B 177 6504 2346 4848 -260 771 1239 O ATOM 1366 CB LYS A 177 -23.784 -0.919 17.068 1.00 33.03 C ANISOU 1366 CB LYS B 177 6439 2065 4046 -632 1450 138 C ATOM 1367 CG LYS A 177 -22.901 0.304 16.993 1.00 33.39 C ANISOU 1367 CG LYS B 177 6295 3047 3346 41 1304 -27 C ATOM 1368 CD LYS A 177 -23.151 0.961 15.649 1.00 35.51 C ANISOU 1368 CD LYS B 177 7002 2868 3624 -306 1472 -423 C ATOM 1369 CE LYS A 177 -22.290 2.208 15.511 1.00 36.92 C ANISOU 1369 CE LYS B 177 7098 3377 3554 -203 2000 -45 C ATOM 1370 NZ LYS A 177 -22.612 2.821 14.178 1.00 33.45 N ANISOU 1370 NZ LYS B 177 6698 2874 3139 -384 1205 12 N ATOM 1371 N LYS A 178 -22.381 -0.685 20.077 1.00 30.56 N ANISOU 1371 N LYS B 178 5917 2255 3438 -105 499 235 N ATOM 1372 CA LYS A 178 -22.244 0.179 21.246 1.00 35.53 C ANISOU 1372 CA LYS B 178 6270 3161 4069 67 37 469 C ATOM 1373 C LYS A 178 -22.404 1.609 20.810 1.00 37.16 C ANISOU 1373 C LYS B 178 6458 2802 4860 239 -25 521 C ATOM 1374 O LYS A 178 -21.655 2.059 19.943 1.00 34.65 O ANISOU 1374 O LYS B 178 5455 2854 4857 -50 -380 101 O ATOM 1375 CB LYS A 178 -20.853 -0.051 21.858 1.00 35.03 C ANISOU 1375 CB LYS B 178 6622 3353 3336 223 -103 244 C ATOM 1376 CG LYS A 178 -20.623 -1.535 22.099 1.00 39.78 C ANISOU 1376 CG LYS B 178 6635 3718 4760 122 699 -175 C ATOM 1377 CD LYS A 178 -21.580 -2.028 23.178 1.00 40.14 C ANISOU 1377 CD LYS B 178 6986 3300 4965 307 679 314 C ATOM 1378 CE LYS A 178 -21.023 -3.272 23.857 1.00 43.52 C ANISOU 1378 CE LYS B 178 6692 3838 6006 747 1504 782 C ATOM 1379 NZ LYS A 178 -22.068 -3.899 24.723 1.00 59.14 N ANISOU 1379 NZ LYS B 178 6586 6218 9665 130 2760 1083 N ATOM 1380 N PRO A 179 -23.337 2.408 21.279 1.00 48.11 N ANISOU 1380 N PRO B 179 6185 4072 8021 654 -170 2405 N ATOM 1381 CA PRO A 179 -23.422 3.769 20.721 1.00 49.43 C ANISOU 1381 CA PRO B 179 5834 4207 8741 1229 -605 3094 C ATOM 1382 C PRO A 179 -22.317 4.685 21.244 1.00 53.12 C ANISOU 1382 C PRO B 179 6064 5953 8165 223 -11 2616 C ATOM 1383 O PRO A 179 -21.909 5.627 20.567 1.00 60.04 O ANISOU 1383 O PRO B 179 6680 7658 8475 -1109 670 1438 O ATOM 1384 CB PRO A 179 -24.795 4.236 21.194 1.00 59.11 C ANISOU 1384 CB PRO B 179 7896 3863 10700 666 1022 2359 C ATOM 1385 CG PRO A 179 -25.481 3.006 21.698 1.00 61.03 C ANISOU 1385 CG PRO B 179 8206 4100 10882 355 1494 2231 C ATOM 1386 CD PRO A 179 -24.373 2.147 22.279 1.00 53.19 C ANISOU 1386 CD PRO B 179 6991 3752 9468 651 389 2947 C ATOM 1387 N ASN A 180 -21.827 4.409 22.425 1.00 50.46 N ANISOU 1387 N ASN B 180 5511 6345 7315 908 -210 3498 N ATOM 1388 CA ASN A 180 -20.808 5.048 23.205 1.00 66.81 C ANISOU 1388 CA ASN B 180 8501 8189 8695 -827 -1266 2552 C ATOM 1389 C ASN A 180 -19.428 5.232 22.595 1.00 62.27 C ANISOU 1389 C ASN B 180 8408 7182 8068 -845 -1937 1859 C ATOM 1390 O ASN A 180 -18.701 6.139 23.021 1.00 73.47 O ANISOU 1390 O ASN B 180 10886 7361 9667 -2986 -4841 2404 O ATOM 1391 CB ASN A 180 -20.614 4.112 24.434 1.00 71.78 C ANISOU 1391 CB ASN B 180 10201 8440 8630 -1020 -951 2237 C ATOM 1392 CG ASN A 180 -20.803 2.674 23.960 1.00 71.21 C ANISOU 1392 CG ASN B 180 10690 7838 8528 149 120 2825 C ATOM 1393 OD1 ASN A 180 -19.885 2.082 23.388 1.00 84.94 O ANISOU 1393 OD1 ASN B 180 12900 10116 9259 -922 -825 5258 O ATOM 1394 ND2 ASN A 180 -22.000 2.153 24.202 1.00 58.49 N ANISOU 1394 ND2 ASN B 180 8788 5853 7583 2741 3075 1079 N ATOM 1395 N THR A 181 -19.033 4.402 21.646 1.00 58.28 N ANISOU 1395 N THR B 181 9402 5065 7678 -997 -2760 505 N ATOM 1396 CA THR A 181 -17.641 4.265 21.194 1.00 46.86 C ANISOU 1396 CA THR B 181 8221 3748 5836 -179 -1730 -1417 C ATOM 1397 C THR A 181 -17.338 4.911 19.852 1.00 42.30 C ANISOU 1397 C THR B 181 7096 3228 5749 1288 -2178 -1422 C ATOM 1398 O THR A 181 -18.273 5.169 19.092 1.00 55.31 O ANISOU 1398 O THR B 181 9538 4666 6812 1168 -2469 -2772 O ATOM 1399 CB THR A 181 -17.333 2.746 21.214 1.00 47.35 C ANISOU 1399 CB THR B 181 7660 4401 5929 -224 -727 -2228 C ATOM 1400 OG1 THR A 181 -15.988 2.480 20.856 1.00 49.66 O ANISOU 1400 OG1 THR B 181 5890 4773 8204 624 -1568 -301 O ATOM 1401 CG2 THR A 181 -18.128 2.000 20.163 1.00 60.56 C ANISOU 1401 CG2 THR B 181 11495 1895 9621 1697 -4943 -2288 C ATOM 1402 N ASN A 182 -16.095 5.218 19.501 1.00 43.14 N ANISOU 1402 N ASN B 182 6144 4232 6017 1662 -2222 -291 N ATOM 1403 CA ASN A 182 -15.593 5.730 18.225 1.00 46.29 C ANISOU 1403 CA ASN B 182 5664 5261 6664 3076 -1545 -213 C ATOM 1404 C ASN A 182 -14.916 4.617 17.426 1.00 41.93 C ANISOU 1404 C ASN B 182 5912 3747 6274 2497 -310 -303 C ATOM 1405 O ASN A 182 -14.350 4.785 16.346 1.00 48.18 O ANISOU 1405 O ASN B 182 4664 7110 6532 2091 -728 690 O ATOM 1406 CB ASN A 182 -14.754 6.973 18.505 1.00 55.26 C ANISOU 1406 CB ASN B 182 5909 6866 8219 1855 -1919 5 C ATOM 1407 CG ASN A 182 -13.287 7.186 18.539 1.00 61.75 C ANISOU 1407 CG ASN B 182 7443 7050 8970 1075 -2848 1203 C ATOM 1408 OD1 ASN A 182 -12.717 8.008 19.306 1.00 59.74 O ANISOU 1408 OD1 ASN B 182 6441 6522 9735 1383 -2493 908 O ATOM 1409 ND2 ASN A 182 -12.580 6.477 17.665 1.00 66.73 N ANISOU 1409 ND2 ASN B 182 8479 5461 11415 3373 -3256 654 N ATOM 1410 N TYR A 183 -14.953 3.373 17.888 1.00 31.67 N ANISOU 1410 N TYR B 183 4404 2614 5016 1274 -1791 -1359 N ATOM 1411 CA TYR A 183 -14.422 2.220 17.147 1.00 24.22 C ANISOU 1411 CA TYR B 183 3217 2178 3809 297 -664 -819 C ATOM 1412 C TYR A 183 -15.363 1.738 16.043 1.00 23.68 C ANISOU 1412 C TYR B 183 2780 2256 3961 145 -594 -766 C ATOM 1413 O TYR A 183 -16.543 2.048 16.043 1.00 28.55 O ANISOU 1413 O TYR B 183 3987 1954 4908 450 -1202 -1069 O ATOM 1414 CB TYR A 183 -14.213 1.082 18.134 1.00 20.66 C ANISOU 1414 CB TYR B 183 2744 1684 3422 9 -460 -119 C ATOM 1415 CG TYR A 183 -13.441 1.411 19.383 1.00 17.85 C ANISOU 1415 CG TYR B 183 2078 1528 3177 321 -163 9 C ATOM 1416 CD1 TYR A 183 -13.745 0.840 20.612 1.00 23.17 C ANISOU 1416 CD1 TYR B 183 2802 2353 3650 -395 538 -775 C ATOM 1417 CD2 TYR A 183 -12.377 2.298 19.344 1.00 18.67 C ANISOU 1417 CD2 TYR B 183 2041 1990 3064 275 -161 -9 C ATOM 1418 CE1 TYR A 183 -13.030 1.151 21.748 1.00 21.98 C ANISOU 1418 CE1 TYR B 183 3060 2280 3014 -448 256 411 C ATOM 1419 CE2 TYR A 183 -11.657 2.608 20.487 1.00 20.29 C ANISOU 1419 CE2 TYR B 183 2417 2305 2989 -212 -12 -99 C ATOM 1420 CZ TYR A 183 -11.986 2.024 21.699 1.00 19.36 C ANISOU 1420 CZ TYR B 183 2492 1945 2918 334 -63 329 C ATOM 1421 OH TYR A 183 -11.268 2.325 22.838 1.00 23.58 O ANISOU 1421 OH TYR B 183 3106 2856 2997 -49 3 -77 O ATOM 1422 N THR A 184 -14.869 0.927 15.101 1.00 21.05 N ANISOU 1422 N THR B 184 2513 2389 3096 -36 128 -817 N ATOM 1423 CA THR A 184 -15.623 0.483 13.919 1.00 19.86 C ANISOU 1423 CA THR B 184 2515 1890 3140 -400 126 -512 C ATOM 1424 C THR A 184 -16.384 -0.808 14.190 1.00 20.04 C ANISOU 1424 C THR B 184 2596 2158 2861 -481 322 -821 C ATOM 1425 O THR A 184 -15.768 -1.847 14.471 1.00 19.19 O ANISOU 1425 O THR B 184 2634 2123 2534 -330 165 -554 O ATOM 1426 CB THR A 184 -14.691 0.287 12.693 1.00 19.86 C ANISOU 1426 CB THR B 184 2331 1962 3252 -272 221 -406 C ATOM 1427 OG1 THR A 184 -14.064 1.533 12.385 1.00 24.17 O ANISOU 1427 OG1 THR B 184 2460 2587 4135 -406 647 -608 O ATOM 1428 CG2 THR A 184 -15.466 -0.141 11.466 1.00 22.53 C ANISOU 1428 CG2 THR B 184 2879 2628 3052 79 178 -677 C ATOM 1429 N TYR A 185 -17.691 -0.766 14.140 1.00 19.23 N ANISOU 1429 N TYR B 185 2538 2022 2746 -420 225 -357 N ATOM 1430 CA TYR A 185 -18.550 -1.884 14.426 1.00 17.93 C ANISOU 1430 CA TYR B 185 2605 1856 2351 -231 293 148 C ATOM 1431 C TYR A 185 -18.742 -2.782 13.201 1.00 17.50 C ANISOU 1431 C TYR B 185 2548 1980 2122 -331 353 -91 C ATOM 1432 O TYR A 185 -19.032 -2.302 12.115 1.00 20.14 O ANISOU 1432 O TYR B 185 3081 2262 2308 -124 495 -345 O ATOM 1433 CB TYR A 185 -19.944 -1.373 14.864 1.00 19.11 C ANISOU 1433 CB TYR B 185 3006 1712 2543 -268 358 -16 C ATOM 1434 CG TYR A 185 -20.909 -2.512 15.115 1.00 17.66 C ANISOU 1434 CG TYR B 185 2947 1657 2107 -345 261 -90 C ATOM 1435 CD1 TYR A 185 -20.804 -3.320 16.254 1.00 18.40 C ANISOU 1435 CD1 TYR B 185 2960 2071 1959 -69 107 -20 C ATOM 1436 CD2 TYR A 185 -21.930 -2.830 14.245 1.00 19.92 C ANISOU 1436 CD2 TYR B 185 3491 2027 2050 -799 419 -117 C ATOM 1437 CE1 TYR A 185 -21.682 -4.356 16.468 1.00 20.22 C ANISOU 1437 CE1 TYR B 185 3049 2428 2205 -228 337 -114 C ATOM 1438 CE2 TYR A 185 -22.833 -3.869 14.411 1.00 23.19 C ANISOU 1438 CE2 TYR B 185 3680 2106 3025 -1352 515 -673 C ATOM 1439 CZ TYR A 185 -22.689 -4.640 15.563 1.00 20.93 C ANISOU 1439 CZ TYR B 185 3288 1716 2949 -702 499 -109 C ATOM 1440 OH TYR A 185 -23.562 -5.668 15.757 1.00 25.09 O ANISOU 1440 OH TYR B 185 3582 2508 3443 -1350 681 77 O ATOM 1441 N TYR A 186 -18.593 -4.087 13.412 1.00 17.42 N ANISOU 1441 N TYR B 186 2699 1974 1945 -239 -192 -688 N ATOM 1442 CA TYR A 186 -18.914 -5.099 12.445 1.00 16.54 C ANISOU 1442 CA TYR B 186 2567 1861 1857 -523 -196 -752 C ATOM 1443 C TYR A 186 -20.031 -6.012 12.956 1.00 17.76 C ANISOU 1443 C TYR B 186 2655 1701 2392 -405 45 -485 C ATOM 1444 O TYR A 186 -19.966 -6.413 14.128 1.00 19.67 O ANISOU 1444 O TYR B 186 2666 2506 2301 -378 7 -377 O ATOM 1445 CB TYR A 186 -17.641 -5.922 12.171 1.00 17.53 C ANISOU 1445 CB TYR B 186 2515 1989 2157 -453 -18 -371 C ATOM 1446 CG TYR A 186 -16.668 -5.225 11.255 1.00 16.43 C ANISOU 1446 CG TYR B 186 2225 2036 1980 -29 -77 -287 C ATOM 1447 CD1 TYR A 186 -16.660 -5.427 9.895 1.00 18.86 C ANISOU 1447 CD1 TYR B 186 2605 2613 1948 -366 -124 -463 C ATOM 1448 CD2 TYR A 186 -15.701 -4.359 11.760 1.00 17.42 C ANISOU 1448 CD2 TYR B 186 2082 2491 2045 8 -114 -136 C ATOM 1449 CE1 TYR A 186 -15.735 -4.790 9.055 1.00 20.49 C ANISOU 1449 CE1 TYR B 186 3189 2741 1856 -901 -83 -466 C ATOM 1450 CE2 TYR A 186 -14.791 -3.701 10.955 1.00 17.77 C ANISOU 1450 CE2 TYR B 186 2427 2245 2081 -270 -88 -147 C ATOM 1451 CZ TYR A 186 -14.817 -3.914 9.596 1.00 17.96 C ANISOU 1451 CZ TYR B 186 2781 1943 2101 -391 -82 -23 C ATOM 1452 OH TYR A 186 -13.913 -3.262 8.780 1.00 19.94 O ANISOU 1452 OH TYR B 186 3110 2160 2305 -417 443 -443 O ATOM 1453 N GLY A 187 -20.979 -6.365 12.103 1.00 17.67 N ANISOU 1453 N GLY B 187 2424 1841 2450 -522 181 -439 N ATOM 1454 CA GLY A 187 -22.093 -7.198 12.489 1.00 20.45 C ANISOU 1454 CA GLY B 187 2383 2494 2892 -616 194 -168 C ATOM 1455 C GLY A 187 -21.864 -8.692 12.336 1.00 21.10 C ANISOU 1455 C GLY B 187 2470 2479 3068 -464 251 -1115 C ATOM 1456 O GLY A 187 -22.698 -9.547 12.610 1.00 24.85 O ANISOU 1456 O GLY B 187 2344 3649 3451 -449 -126 -347 O ATOM 1457 N SER A 188 -20.688 -9.082 11.888 1.00 24.05 N ANISOU 1457 N SER B 188 2504 2040 4593 -506 -691 -1244 N ATOM 1458 CA SER A 188 -20.241 -10.419 11.606 1.00 25.07 C ANISOU 1458 CA SER B 188 2752 2470 4303 -130 -914 -1586 C ATOM 1459 C SER A 188 -18.827 -10.624 12.080 1.00 21.76 C ANISOU 1459 C SER B 188 2509 2259 3500 103 -1172 -1178 C ATOM 1460 O SER A 188 -18.002 -9.736 11.854 1.00 30.07 O ANISOU 1460 O SER B 188 2391 2509 6525 37 -978 -2181 O ATOM 1461 CB SER A 188 -20.224 -10.510 10.081 1.00 24.82 C ANISOU 1461 CB SER B 188 2311 2853 4266 514 -1030 -2259 C ATOM 1462 OG SER A 188 -19.569 -11.516 9.454 1.00 29.73 O ANISOU 1462 OG SER B 188 3509 3592 4196 457 -820 -1448 O ATOM 1463 N VAL A 189 -18.588 -11.739 12.712 1.00 23.55 N ANISOU 1463 N VAL B 189 2883 1934 4131 205 -678 -890 N ATOM 1464 CA VAL A 189 -17.251 -12.109 13.140 1.00 19.20 C ANISOU 1464 CA VAL B 189 2272 1862 3161 109 -466 -489 C ATOM 1465 C VAL A 189 -16.380 -12.368 11.916 1.00 19.66 C ANISOU 1465 C VAL B 189 2340 2478 2652 16 -364 -647 C ATOM 1466 O VAL A 189 -15.194 -11.971 11.906 1.00 19.09 O ANISOU 1466 O VAL B 189 2338 2817 2097 -169 -282 -550 O ATOM 1467 CB VAL A 189 -17.228 -13.299 14.107 1.00 21.75 C ANISOU 1467 CB VAL B 189 3313 2178 2774 -30 24 -509 C ATOM 1468 CG1 VAL A 189 -15.792 -13.596 14.542 1.00 22.82 C ANISOU 1468 CG1 VAL B 189 3166 2610 2893 -116 -159 -1020 C ATOM 1469 CG2 VAL A 189 -18.068 -12.972 15.318 1.00 26.65 C ANISOU 1469 CG2 VAL B 189 2905 3685 3536 -194 -218 602 C ATOM 1470 N VAL A 190 -16.936 -12.978 10.867 1.00 21.47 N ANISOU 1470 N VAL B 190 2186 3334 2638 -204 -260 -818 N ATOM 1471 CA VAL A 190 -16.107 -13.215 9.680 1.00 21.93 C ANISOU 1471 CA VAL B 190 2531 3653 2147 -240 -130 -1088 C ATOM 1472 C VAL A 190 -15.625 -11.927 9.029 1.00 23.13 C ANISOU 1472 C VAL B 190 2520 3634 2636 -171 18 -1077 C ATOM 1473 O VAL A 190 -14.483 -11.758 8.625 1.00 21.91 O ANISOU 1473 O VAL B 190 2748 3804 1773 -189 -30 -902 O ATOM 1474 CB VAL A 190 -16.928 -14.049 8.650 1.00 23.22 C ANISOU 1474 CB VAL B 190 2653 3458 2712 -321 -478 -819 C ATOM 1475 CG1 VAL A 190 -16.346 -13.932 7.262 1.00 30.34 C ANISOU 1475 CG1 VAL B 190 3020 6125 2382 -1224 -612 -971 C ATOM 1476 CG2 VAL A 190 -17.000 -15.485 9.163 1.00 23.12 C ANISOU 1476 CG2 VAL B 190 2976 3388 2421 208 -724 -725 C ATOM 1477 N GLU A 191 -16.491 -10.931 8.893 1.00 23.57 N ANISOU 1477 N GLU B 191 2351 3662 2944 -206 -435 -1373 N ATOM 1478 CA GLU A 191 -16.166 -9.650 8.284 1.00 23.41 C ANISOU 1478 CA GLU B 191 2493 3773 2630 136 -475 -1002 C ATOM 1479 C GLU A 191 -15.146 -8.904 9.151 1.00 20.12 C ANISOU 1479 C GLU B 191 2238 3001 2407 319 -275 -933 C ATOM 1480 O GLU A 191 -14.189 -8.326 8.628 1.00 22.81 O ANISOU 1480 O GLU B 191 2736 3409 2521 -104 87 -1163 O ATOM 1481 CB GLU A 191 -17.427 -8.822 8.084 1.00 29.39 C ANISOU 1481 CB GLU B 191 3086 4018 4065 -81 -322 -2115 C ATOM 1482 CG GLU A 191 -17.364 -7.631 7.161 1.00 35.22 C ANISOU 1482 CG GLU B 191 4334 4116 4932 -485 887 -2301 C ATOM 1483 CD GLU A 191 -18.614 -6.760 7.270 1.00 41.77 C ANISOU 1483 CD GLU B 191 6722 3806 5341 -713 1360 -3566 C ATOM 1484 OE1 GLU A 191 -19.746 -6.964 7.790 1.00 52.45 O ANISOU 1484 OE1 GLU B 191 3652 3171 13107 -638 799 -3135 O ATOM 1485 OE2 GLU A 191 -18.471 -5.623 6.858 1.00 30.70 O ANISOU 1485 OE2 GLU B 191 5868 3424 2371 -319 -45 -1390 O ATOM 1486 N LEU A 192 -15.359 -8.968 10.470 1.00 21.61 N ANISOU 1486 N LEU B 192 2742 3100 2371 -399 -105 -1312 N ATOM 1487 CA LEU A 192 -14.352 -8.436 11.394 1.00 18.88 C ANISOU 1487 CA LEU B 192 2562 2215 2397 84 -125 -1244 C ATOM 1488 C LEU A 192 -12.982 -9.054 11.137 1.00 18.28 C ANISOU 1488 C LEU B 192 2273 2315 2356 108 28 -826 C ATOM 1489 O LEU A 192 -11.970 -8.366 11.018 1.00 18.87 O ANISOU 1489 O LEU B 192 2170 2470 2529 172 -164 -626 O ATOM 1490 CB LEU A 192 -14.747 -8.681 12.859 1.00 18.34 C ANISOU 1490 CB LEU B 192 2264 2377 2329 306 -611 -563 C ATOM 1491 CG LEU A 192 -13.764 -8.127 13.916 1.00 19.02 C ANISOU 1491 CG LEU B 192 2500 2233 2492 397 -787 -674 C ATOM 1492 CD1 LEU A 192 -13.643 -6.607 13.807 1.00 19.14 C ANISOU 1492 CD1 LEU B 192 2471 1733 3069 295 -1092 -737 C ATOM 1493 CD2 LEU A 192 -14.207 -8.557 15.303 1.00 20.55 C ANISOU 1493 CD2 LEU B 192 2893 2439 2476 -385 -768 -805 C ATOM 1494 N ALA A 193 -12.934 -10.380 11.117 1.00 18.38 N ANISOU 1494 N ALA B 193 2094 2405 2484 -107 -487 -348 N ATOM 1495 CA ALA A 193 -11.705 -11.114 10.914 1.00 18.33 C ANISOU 1495 CA ALA B 193 2351 2464 2149 222 -201 -309 C ATOM 1496 C ALA A 193 -11.056 -10.719 9.594 1.00 18.57 C ANISOU 1496 C ALA B 193 2700 2242 2113 -28 -75 -645 C ATOM 1497 O ALA A 193 -9.842 -10.549 9.540 1.00 19.23 O ANISOU 1497 O ALA B 193 2754 2173 2382 -10 -217 -356 O ATOM 1498 CB ALA A 193 -11.958 -12.626 10.971 1.00 20.19 C ANISOU 1498 CB ALA B 193 2389 2970 2312 411 -322 -715 C ATOM 1499 N SER A 194 -11.840 -10.550 8.551 1.00 20.13 N ANISOU 1499 N SER B 194 2697 2754 2197 157 -359 -884 N ATOM 1500 CA SER A 194 -11.363 -10.169 7.219 1.00 21.97 C ANISOU 1500 CA SER B 194 2762 3364 2222 311 -226 -890 C ATOM 1501 C SER A 194 -10.673 -8.816 7.187 1.00 22.11 C ANISOU 1501 C SER B 194 2704 3479 2217 -185 -441 -470 C ATOM 1502 O SER A 194 -9.890 -8.539 6.268 1.00 24.89 O ANISOU 1502 O SER B 194 2798 4166 2492 366 -253 124 O ATOM 1503 CB SER A 194 -12.555 -10.134 6.243 1.00 24.95 C ANISOU 1503 CB SER B 194 2888 4646 1947 -93 -827 -917 C ATOM 1504 OG SER A 194 -13.063 -11.431 6.024 1.00 31.22 O ANISOU 1504 OG SER B 194 3263 5497 3102 745 -1307 -1255 O ATOM 1505 N ASN A 195 -11.023 -8.014 8.183 1.00 19.51 N ANISOU 1505 N ASN B 195 2633 2816 1965 -92 -259 -746 N ATOM 1506 CA ASN A 195 -10.536 -6.652 8.312 1.00 19.08 C ANISOU 1506 CA ASN B 195 2579 2417 2254 -134 -162 -753 C ATOM 1507 C ASN A 195 -9.657 -6.409 9.554 1.00 17.32 C ANISOU 1507 C ASN B 195 2343 2189 2048 306 -204 -555 C ATOM 1508 O ASN A 195 -9.498 -5.270 9.986 1.00 19.38 O ANISOU 1508 O ASN B 195 2416 2391 2557 455 -343 -398 O ATOM 1509 CB ASN A 195 -11.718 -5.678 8.341 1.00 19.94 C ANISOU 1509 CB ASN B 195 2971 2463 2140 -56 406 -865 C ATOM 1510 CG ASN A 195 -12.375 -5.587 6.981 1.00 18.11 C ANISOU 1510 CG ASN B 195 2458 2432 1993 33 275 -679 C ATOM 1511 OD1 ASN A 195 -11.907 -4.810 6.136 1.00 22.39 O ANISOU 1511 OD1 ASN B 195 3307 3034 2168 -414 801 -742 O ATOM 1512 ND2 ASN A 195 -13.411 -6.354 6.771 1.00 21.58 N ANISOU 1512 ND2 ASN B 195 2684 2484 3032 -185 181 -945 N ATOM 1513 N SER A 196 -9.091 -7.494 10.071 1.00 16.63 N ANISOU 1513 N SER B 196 2273 2000 2047 232 -197 -489 N ATOM 1514 CA SER A 196 -8.188 -7.456 11.189 1.00 16.55 C ANISOU 1514 CA SER B 196 2304 1930 2053 -11 -61 -445 C ATOM 1515 C SER A 196 -6.831 -8.096 10.866 1.00 16.34 C ANISOU 1515 C SER B 196 2371 1977 1859 -5 -401 -217 C ATOM 1516 O SER A 196 -6.780 -9.147 10.218 1.00 18.75 O ANISOU 1516 O SER B 196 2325 2652 2148 266 -420 -109 O ATOM 1517 CB SER A 196 -8.800 -8.249 12.334 1.00 16.58 C ANISOU 1517 CB SER B 196 2268 2147 1885 -224 -243 -355 C ATOM 1518 OG SER A 196 -9.998 -7.661 12.788 1.00 18.87 O ANISOU 1518 OG SER B 196 2792 2204 2175 -430 -146 -275 O ATOM 1519 N ASP A 197 -5.778 -7.419 11.352 1.00 15.27 N ANISOU 1519 N ASP B 197 2073 1727 2001 249 -209 -194 N ATOM 1520 CA ASP A 197 -4.443 -8.013 11.419 1.00 16.08 C ANISOU 1520 CA ASP B 197 2576 1833 1700 -94 -94 -227 C ATOM 1521 C ASP A 197 -4.288 -8.874 12.668 1.00 15.18 C ANISOU 1521 C ASP B 197 2435 1696 1638 241 -316 -142 C ATOM 1522 O ASP A 197 -3.566 -9.870 12.632 1.00 17.64 O ANISOU 1522 O ASP B 197 2618 1674 2412 353 -109 75 O ATOM 1523 CB ASP A 197 -3.354 -6.940 11.379 1.00 16.77 C ANISOU 1523 CB ASP B 197 2536 2211 1625 -154 -213 -56 C ATOM 1524 CG ASP A 197 -3.467 -6.094 10.128 1.00 18.21 C ANISOU 1524 CG ASP B 197 2800 2325 1794 -88 123 41 C ATOM 1525 OD1 ASP A 197 -3.397 -6.669 9.015 1.00 21.27 O ANISOU 1525 OD1 ASP B 197 3415 2953 1712 393 97 -162 O ATOM 1526 OD2 ASP A 197 -3.629 -4.862 10.228 1.00 19.08 O ANISOU 1526 OD2 ASP B 197 2892 2238 2121 -63 38 -139 O ATOM 1527 N ILE A 198 -4.961 -8.495 13.738 1.00 14.53 N ANISOU 1527 N ILE B 198 2179 1609 1732 108 -130 -154 N ATOM 1528 CA ILE A 198 -4.943 -9.113 15.048 1.00 15.23 C ANISOU 1528 CA ILE B 198 2104 2036 1646 -270 -148 -316 C ATOM 1529 C ILE A 198 -6.393 -9.230 15.491 1.00 14.14 C ANISOU 1529 C ILE B 198 2024 1723 1626 57 14 -499 C ATOM 1530 O ILE A 198 -7.078 -8.219 15.430 1.00 16.18 O ANISOU 1530 O ILE B 198 2285 1825 2038 311 -128 -434 O ATOM 1531 CB ILE A 198 -4.134 -8.271 16.042 1.00 14.73 C ANISOU 1531 CB ILE B 198 1933 1891 1771 -5 -97 -274 C ATOM 1532 CG1 ILE A 198 -2.672 -8.099 15.630 1.00 16.64 C ANISOU 1532 CG1 ILE B 198 2009 1969 2344 -197 -136 -309 C ATOM 1533 CG2 ILE A 198 -4.211 -8.884 17.444 1.00 18.49 C ANISOU 1533 CG2 ILE B 198 2349 3084 1591 -168 -195 -410 C ATOM 1534 CD1 ILE A 198 -2.003 -6.905 16.235 1.00 17.41 C ANISOU 1534 CD1 ILE B 198 2021 2002 2593 -145 -177 -170 C ATOM 1535 N LEU A 199 -6.808 -10.426 15.893 1.00 16.37 N ANISOU 1535 N LEU B 199 1888 2213 2121 159 47 16 N ATOM 1536 CA LEU A 199 -8.196 -10.643 16.336 1.00 15.88 C ANISOU 1536 CA LEU B 199 1964 2147 1924 130 -46 104 C ATOM 1537 C LEU A 199 -8.145 -11.160 17.782 1.00 16.21 C ANISOU 1537 C LEU B 199 1852 2336 1970 269 -9 25 C ATOM 1538 O LEU A 199 -7.518 -12.198 18.025 1.00 15.73 O ANISOU 1538 O LEU B 199 2040 2068 1867 92 -319 -58 O ATOM 1539 CB LEU A 199 -8.890 -11.638 15.432 1.00 15.77 C ANISOU 1539 CB LEU B 199 2102 1810 2080 238 -174 -59 C ATOM 1540 CG LEU A 199 -10.386 -11.889 15.640 1.00 16.26 C ANISOU 1540 CG LEU B 199 2095 2090 1993 80 -123 -132 C ATOM 1541 CD1 LEU A 199 -11.197 -10.661 15.308 1.00 18.58 C ANISOU 1541 CD1 LEU B 199 2299 1981 2779 -144 -440 -650 C ATOM 1542 CD2 LEU A 199 -10.839 -13.074 14.795 1.00 18.64 C ANISOU 1542 CD2 LEU B 199 2512 2332 2237 47 -586 -504 C ATOM 1543 N VAL A 200 -8.792 -10.450 18.675 1.00 15.32 N ANISOU 1543 N VAL B 200 2273 1887 1659 144 -301 -380 N ATOM 1544 CA VAL A 200 -8.768 -10.741 20.079 1.00 13.62 C ANISOU 1544 CA VAL B 200 1721 1719 1735 122 -168 -443 C ATOM 1545 C VAL A 200 -10.103 -11.260 20.589 1.00 14.66 C ANISOU 1545 C VAL B 200 1852 1664 2054 201 -286 -85 C ATOM 1546 O VAL A 200 -11.098 -10.558 20.461 1.00 16.21 O ANISOU 1546 O VAL B 200 2080 1746 2333 44 -126 -88 O ATOM 1547 CB VAL A 200 -8.391 -9.512 20.933 1.00 14.22 C ANISOU 1547 CB VAL B 200 1862 1884 1658 180 -120 -19 C ATOM 1548 CG1 VAL A 200 -8.260 -9.969 22.373 1.00 17.25 C ANISOU 1548 CG1 VAL B 200 2080 2842 1633 -142 -151 6 C ATOM 1549 CG2 VAL A 200 -7.092 -8.877 20.426 1.00 15.01 C ANISOU 1549 CG2 VAL B 200 1665 2245 1795 147 -190 -109 C ATOM 1550 N VAL A 201 -10.121 -12.420 21.207 1.00 15.67 N ANISOU 1550 N VAL B 201 1574 2157 2221 126 -281 -215 N ATOM 1551 CA VAL A 201 -11.344 -12.958 21.768 1.00 15.35 C ANISOU 1551 CA VAL B 201 1547 1980 2306 52 -454 -184 C ATOM 1552 C VAL A 201 -11.454 -12.417 23.171 1.00 16.91 C ANISOU 1552 C VAL B 201 1937 2223 2267 -396 -640 -161 C ATOM 1553 O VAL A 201 -10.571 -12.743 23.973 1.00 19.74 O ANISOU 1553 O VAL B 201 2215 2801 2484 -517 -287 -616 O ATOM 1554 CB VAL A 201 -11.306 -14.496 21.839 1.00 16.26 C ANISOU 1554 CB VAL B 201 1629 2040 2508 100 -216 -342 C ATOM 1555 CG1 VAL A 201 -12.571 -15.046 22.497 1.00 21.23 C ANISOU 1555 CG1 VAL B 201 1844 2961 3262 -46 254 -173 C ATOM 1556 CG2 VAL A 201 -11.114 -15.129 20.476 1.00 20.51 C ANISOU 1556 CG2 VAL B 201 1927 2721 3147 156 -773 256 C ATOM 1557 N ALA A 202 -12.486 -11.640 23.499 1.00 18.78 N ANISOU 1557 N ALA B 202 2740 2481 1916 -98 -52 189 N ATOM 1558 CA ALA A 202 -12.633 -11.020 24.793 1.00 21.34 C ANISOU 1558 CA ALA B 202 2776 3444 1887 302 21 353 C ATOM 1559 C ALA A 202 -14.082 -11.034 25.249 1.00 24.41 C ANISOU 1559 C ALA B 202 3181 3528 2565 468 -123 1152 C ATOM 1560 O ALA A 202 -14.644 -10.040 25.764 1.00 35.11 O ANISOU 1560 O ALA B 202 5015 3847 4480 836 -1355 1493 O ATOM 1561 CB ALA A 202 -12.258 -9.567 24.651 1.00 24.30 C ANISOU 1561 CB ALA B 202 2773 3896 2565 408 -296 -121 C ATOM 1562 N CYS A 203 -14.812 -12.106 25.060 1.00 22.95 N ANISOU 1562 N CYS B 203 3252 2891 2578 116 14 230 N ATOM 1563 CA CYS A 203 -16.205 -12.148 25.485 1.00 24.91 C ANISOU 1563 CA CYS B 203 3770 2723 2972 250 299 423 C ATOM 1564 C CYS A 203 -16.421 -13.320 26.432 1.00 23.18 C ANISOU 1564 C CYS B 203 3607 2305 2896 59 192 380 C ATOM 1565 O CYS A 203 -15.605 -14.229 26.473 1.00 22.75 O ANISOU 1565 O CYS B 203 3668 2334 2644 51 140 379 O ATOM 1566 CB CYS A 203 -17.105 -12.284 24.250 1.00 29.43 C ANISOU 1566 CB CYS B 203 5461 2181 3540 -188 541 -203 C ATOM 1567 SG CYS A 203 -16.691 -13.695 23.195 1.00 25.13 S ANISOU 1567 SG CYS B 203 3112 3853 2584 -714 405 -540 S ATOM 1568 N PRO A 204 -17.509 -13.310 27.196 1.00 23.87 N ANISOU 1568 N PRO B 204 4087 2295 2689 48 301 300 N ATOM 1569 CA PRO A 204 -17.814 -14.480 28.010 1.00 24.41 C ANISOU 1569 CA PRO B 204 4240 2611 2424 230 351 435 C ATOM 1570 C PRO A 204 -18.081 -15.706 27.136 1.00 22.51 C ANISOU 1570 C PRO B 204 4207 2365 1980 197 385 -45 C ATOM 1571 O PRO A 204 -18.390 -15.616 25.956 1.00 25.80 O ANISOU 1571 O PRO B 204 4160 3484 2157 -606 538 -496 O ATOM 1572 CB PRO A 204 -19.084 -14.049 28.737 1.00 27.32 C ANISOU 1572 CB PRO B 204 4726 2970 2683 412 688 758 C ATOM 1573 CG PRO A 204 -19.190 -12.585 28.617 1.00 30.02 C ANISOU 1573 CG PRO B 204 5678 2551 3178 819 1490 615 C ATOM 1574 CD PRO A 204 -18.481 -12.208 27.341 1.00 29.51 C ANISOU 1574 CD PRO B 204 5399 2523 3292 529 1327 778 C ATOM 1575 N LEU A 205 -17.959 -16.892 27.710 1.00 23.59 N ANISOU 1575 N LEU B 205 3885 2572 2505 -7 329 -383 N ATOM 1576 CA LEU A 205 -18.285 -18.152 27.102 1.00 22.08 C ANISOU 1576 CA LEU B 205 3523 2080 2786 -633 329 -483 C ATOM 1577 C LEU A 205 -19.746 -18.502 27.422 1.00 26.09 C ANISOU 1577 C LEU B 205 5100 2824 1989 -1733 -28 -209 C ATOM 1578 O LEU A 205 -20.175 -18.651 28.575 1.00 24.89 O ANISOU 1578 O LEU B 205 4656 2718 2084 -850 209 -70 O ATOM 1579 CB LEU A 205 -17.387 -19.282 27.633 1.00 20.74 C ANISOU 1579 CB LEU B 205 3244 2340 2295 -418 589 -278 C ATOM 1580 CG LEU A 205 -17.638 -20.620 26.942 1.00 22.40 C ANISOU 1580 CG LEU B 205 2855 3277 2379 -412 761 -332 C ATOM 1581 CD1 LEU A 205 -17.297 -20.543 25.452 1.00 24.65 C ANISOU 1581 CD1 LEU B 205 3576 3353 2439 -28 710 120 C ATOM 1582 CD2 LEU A 205 -16.871 -21.733 27.646 1.00 20.77 C ANISOU 1582 CD2 LEU B 205 2580 2864 2449 -536 225 -283 C ATOM 1583 N THR A 206 -20.517 -18.637 26.359 1.00 25.15 N ANISOU 1583 N THR B 206 4575 2653 2328 -1136 -255 -477 N ATOM 1584 CA THR A 206 -21.902 -19.064 26.396 1.00 26.00 C ANISOU 1584 CA THR B 206 4356 2946 2577 -1220 201 -823 C ATOM 1585 C THR A 206 -22.100 -20.088 25.282 1.00 30.81 C ANISOU 1585 C THR B 206 4628 3654 3425 -1799 -378 -99 C ATOM 1586 O THR A 206 -21.190 -20.254 24.458 1.00 27.48 O ANISOU 1586 O THR B 206 4018 3798 2625 -1233 316 -497 O ATOM 1587 CB THR A 206 -22.876 -17.890 26.196 1.00 26.67 C ANISOU 1587 CB THR B 206 4172 2864 3097 -1412 845 -862 C ATOM 1588 OG1 THR A 206 -22.681 -17.319 24.906 1.00 31.78 O ANISOU 1588 OG1 THR B 206 5482 3740 2852 -1216 761 -1258 O ATOM 1589 CG2 THR A 206 -22.620 -16.741 27.155 1.00 30.66 C ANISOU 1589 CG2 THR B 206 5616 2712 3320 -958 263 -202 C ATOM 1590 N PRO A 207 -23.218 -20.772 25.202 1.00 30.62 N ANISOU 1590 N PRO B 207 3950 4147 3537 -1354 219 -93 N ATOM 1591 CA PRO A 207 -23.481 -21.624 24.031 1.00 33.85 C ANISOU 1591 CA PRO B 207 4529 4627 3704 -2081 -280 -206 C ATOM 1592 C PRO A 207 -23.291 -20.866 22.735 1.00 32.05 C ANISOU 1592 C PRO B 207 4585 3986 3608 -1953 -378 -187 C ATOM 1593 O PRO A 207 -22.747 -21.325 21.755 1.00 32.38 O ANISOU 1593 O PRO B 207 4177 4156 3971 -903 242 41 O ATOM 1594 CB PRO A 207 -24.976 -21.976 24.195 1.00 38.19 C ANISOU 1594 CB PRO B 207 4805 5184 4521 -2460 -127 41 C ATOM 1595 CG PRO A 207 -25.165 -21.975 25.665 1.00 38.68 C ANISOU 1595 CG PRO B 207 5223 4975 4497 -2829 320 -383 C ATOM 1596 CD PRO A 207 -24.322 -20.854 26.199 1.00 32.95 C ANISOU 1596 CD PRO B 207 4947 3826 3745 -1700 440 -261 C ATOM 1597 N GLU A 208 -23.770 -19.630 22.754 1.00 30.73 N ANISOU 1597 N GLU B 208 4653 4136 2888 -1833 -697 122 N ATOM 1598 CA GLU A 208 -23.784 -18.825 21.537 1.00 33.48 C ANISOU 1598 CA GLU B 208 4909 4040 3773 -2139 -62 -381 C ATOM 1599 C GLU A 208 -22.375 -18.482 21.076 1.00 33.25 C ANISOU 1599 C GLU B 208 6192 4184 2258 -2745 -509 -69 C ATOM 1600 O GLU A 208 -22.139 -18.332 19.874 1.00 33.52 O ANISOU 1600 O GLU B 208 6721 3707 2308 -1462 -60 -324 O ATOM 1601 CB GLU A 208 -24.634 -17.580 21.785 1.00 39.62 C ANISOU 1601 CB GLU B 208 6742 3549 4764 -2051 263 -506 C ATOM 1602 CG GLU A 208 -26.128 -17.779 21.970 1.00 55.68 C ANISOU 1602 CG GLU B 208 10592 4384 6180 -3818 1632 -248 C ATOM 1603 CD GLU A 208 -26.591 -18.601 23.155 1.00 58.32 C ANISOU 1603 CD GLU B 208 9591 4856 7712 -3368 2193 -19 C ATOM 1604 OE1 GLU A 208 -25.964 -18.551 24.242 1.00 50.04 O ANISOU 1604 OE1 GLU B 208 7733 3671 7610 -556 2775 -761 O ATOM 1605 OE2 GLU A 208 -27.616 -19.317 22.992 1.00 63.50 O ANISOU 1605 OE2 GLU B 208 8931 4473 10724 -2509 1679 -52 O ATOM 1606 N THR A 209 -21.407 -18.358 21.964 1.00 29.30 N ANISOU 1606 N THR B 209 5540 3058 2536 -1762 -597 -193 N ATOM 1607 CA THR A 209 -20.050 -17.938 21.604 1.00 25.22 C ANISOU 1607 CA THR B 209 4456 2670 2456 -1017 -125 -806 C ATOM 1608 C THR A 209 -19.109 -19.133 21.588 1.00 22.78 C ANISOU 1608 C THR B 209 3822 2776 2056 -1033 -131 -483 C ATOM 1609 O THR A 209 -17.908 -18.983 21.397 1.00 24.73 O ANISOU 1609 O THR B 209 4092 2850 2453 -1193 -48 -152 O ATOM 1610 CB THR A 209 -19.471 -16.834 22.514 1.00 24.90 C ANISOU 1610 CB THR B 209 4271 2655 2534 -345 52 -979 C ATOM 1611 OG1 THR A 209 -19.344 -17.317 23.820 1.00 23.64 O ANISOU 1611 OG1 THR B 209 4355 2402 2226 -801 43 -489 O ATOM 1612 CG2 THR A 209 -20.405 -15.624 22.577 1.00 28.45 C ANISOU 1612 CG2 THR B 209 5235 2609 2966 -301 336 -519 C ATOM 1613 N THR A 210 -19.646 -20.324 21.807 1.00 25.41 N ANISOU 1613 N THR B 210 3856 3352 2446 -1120 83 -729 N ATOM 1614 CA THR A 210 -18.835 -21.524 21.692 1.00 23.13 C ANISOU 1614 CA THR B 210 3156 3329 2305 -1284 645 -373 C ATOM 1615 C THR A 210 -18.416 -21.715 20.234 1.00 23.00 C ANISOU 1615 C THR B 210 2564 3899 2277 -1233 606 -374 C ATOM 1616 O THR A 210 -19.247 -21.734 19.312 1.00 24.59 O ANISOU 1616 O THR B 210 3048 3739 2555 -940 -539 36 O ATOM 1617 CB THR A 210 -19.582 -22.771 22.189 1.00 27.15 C ANISOU 1617 CB THR B 210 3612 4091 2613 -1534 1333 -905 C ATOM 1618 OG1 THR A 210 -19.818 -22.615 23.600 1.00 28.67 O ANISOU 1618 OG1 THR B 210 4035 4125 2733 -1576 1338 -695 O ATOM 1619 CG2 THR A 210 -18.769 -24.043 22.030 1.00 27.17 C ANISOU 1619 CG2 THR B 210 2951 4865 2506 -1081 1019 -888 C ATOM 1620 N HIS A 211 -17.142 -21.884 19.977 1.00 21.68 N ANISOU 1620 N HIS B 211 2435 3584 2219 -753 -355 149 N ATOM 1621 CA HIS A 211 -16.586 -22.017 18.660 1.00 22.37 C ANISOU 1621 CA HIS B 211 1988 4131 2380 -337 -42 369 C ATOM 1622 C HIS A 211 -16.908 -20.781 17.806 1.00 22.70 C ANISOU 1622 C HIS B 211 2309 3689 2625 -551 40 141 C ATOM 1623 O HIS A 211 -17.084 -20.870 16.588 1.00 24.03 O ANISOU 1623 O HIS B 211 2857 3599 2674 -504 -203 -27 O ATOM 1624 CB HIS A 211 -17.060 -23.301 17.925 1.00 23.16 C ANISOU 1624 CB HIS B 211 2361 3985 2453 -304 -497 -81 C ATOM 1625 CG HIS A 211 -16.413 -24.536 18.487 1.00 23.61 C ANISOU 1625 CG HIS B 211 2187 4130 2655 -233 -560 -195 C ATOM 1626 ND1 HIS A 211 -16.530 -25.783 17.949 1.00 25.53 N ANISOU 1626 ND1 HIS B 211 2261 4624 2816 -46 -532 -213 N ATOM 1627 CD2 HIS A 211 -15.657 -24.699 19.621 1.00 24.34 C ANISOU 1627 CD2 HIS B 211 2346 3893 3009 -399 -574 -330 C ATOM 1628 CE1 HIS A 211 -15.865 -26.669 18.686 1.00 28.17 C ANISOU 1628 CE1 HIS B 211 2183 4383 4137 -141 -747 -649 C ATOM 1629 NE2 HIS A 211 -15.325 -26.058 19.714 1.00 24.68 N ANISOU 1629 NE2 HIS B 211 2449 3580 3350 -487 -397 -183 N ATOM 1630 N ILE A 212 -16.988 -19.604 18.444 1.00 20.98 N ANISOU 1630 N ILE B 212 2818 2554 2598 -528 -156 -320 N ATOM 1631 CA ILE A 212 -17.159 -18.384 17.666 1.00 20.47 C ANISOU 1631 CA ILE B 212 3225 2297 2255 -452 -191 -350 C ATOM 1632 C ILE A 212 -15.989 -18.190 16.713 1.00 18.75 C ANISOU 1632 C ILE B 212 2669 2486 1971 -256 -532 -226 C ATOM 1633 O ILE A 212 -16.156 -17.611 15.643 1.00 21.68 O ANISOU 1633 O ILE B 212 3151 2817 2268 -341 -32 -420 O ATOM 1634 CB ILE A 212 -17.342 -17.188 18.603 1.00 18.97 C ANISOU 1634 CB ILE B 212 2854 2512 1840 -573 53 -182 C ATOM 1635 CG1 ILE A 212 -17.857 -15.938 17.877 1.00 22.28 C ANISOU 1635 CG1 ILE B 212 3140 2825 2501 -214 -113 -452 C ATOM 1636 CG2 ILE A 212 -16.084 -16.853 19.413 1.00 21.59 C ANISOU 1636 CG2 ILE B 212 2770 2638 2794 -644 -111 -382 C ATOM 1637 CD1 ILE A 212 -18.449 -14.942 18.872 1.00 21.31 C ANISOU 1637 CD1 ILE B 212 2757 2816 2524 -328 -26 -396 C ATOM 1638 N ILE A 213 -14.805 -18.686 17.082 1.00 19.46 N ANISOU 1638 N ILE B 213 2557 2366 2473 -381 -441 -205 N ATOM 1639 CA ILE A 213 -13.672 -18.808 16.136 1.00 19.08 C ANISOU 1639 CA ILE B 213 2130 2714 2406 -437 -588 -40 C ATOM 1640 C ILE A 213 -13.729 -20.193 15.499 1.00 17.79 C ANISOU 1640 C ILE B 213 2013 2843 1902 -329 -328 -217 C ATOM 1641 O ILE A 213 -13.258 -21.144 16.121 1.00 21.23 O ANISOU 1641 O ILE B 213 2511 3590 1964 182 -335 -431 O ATOM 1642 CB ILE A 213 -12.325 -18.589 16.843 1.00 18.60 C ANISOU 1642 CB ILE B 213 1823 2953 2291 -567 -321 -89 C ATOM 1643 CG1 ILE A 213 -12.298 -17.310 17.680 1.00 18.69 C ANISOU 1643 CG1 ILE B 213 2002 2575 2523 -387 -467 -244 C ATOM 1644 CG2 ILE A 213 -11.146 -18.622 15.884 1.00 19.58 C ANISOU 1644 CG2 ILE B 213 2356 2858 2227 -561 -163 -144 C ATOM 1645 CD1 ILE A 213 -12.623 -16.103 16.879 1.00 22.55 C ANISOU 1645 CD1 ILE B 213 2356 3397 2815 -36 -718 -842 C ATOM 1646 N ASN A 214 -14.330 -20.274 14.307 1.00 20.29 N ANISOU 1646 N ASN B 214 1939 3609 2162 -128 -415 -640 N ATOM 1647 CA ASN A 214 -14.417 -21.507 13.555 1.00 22.09 C ANISOU 1647 CA ASN B 214 2142 3889 2361 -475 -724 -280 C ATOM 1648 C ASN A 214 -13.531 -21.441 12.331 1.00 22.29 C ANISOU 1648 C ASN B 214 2361 3907 2199 -742 -801 -475 C ATOM 1649 O ASN A 214 -12.816 -20.438 12.156 1.00 20.65 O ANISOU 1649 O ASN B 214 2340 3397 2109 -242 -579 -385 O ATOM 1650 CB ASN A 214 -15.883 -21.793 13.222 1.00 23.54 C ANISOU 1650 CB ASN B 214 2315 4414 2214 -852 -557 -342 C ATOM 1651 CG ASN A 214 -16.482 -20.666 12.402 1.00 23.17 C ANISOU 1651 CG ASN B 214 2367 3822 2614 -926 -525 -182 C ATOM 1652 OD1 ASN A 214 -15.769 -19.908 11.744 1.00 23.82 O ANISOU 1652 OD1 ASN B 214 2342 4104 2604 -793 -413 -303 O ATOM 1653 ND2 ASN A 214 -17.801 -20.559 12.448 1.00 35.76 N ANISOU 1653 ND2 ASN B 214 4393 4268 4925 -1917 475 -656 N ATOM 1654 N ARG A 215 -13.585 -22.509 11.529 1.00 22.42 N ANISOU 1654 N ARG B 215 2257 4076 2184 -309 -467 -314 N ATOM 1655 CA ARG A 215 -12.643 -22.530 10.394 1.00 23.81 C ANISOU 1655 CA ARG B 215 1949 4873 2225 -366 -355 -73 C ATOM 1656 C ARG A 215 -12.857 -21.328 9.492 1.00 23.33 C ANISOU 1656 C ARG B 215 2147 4623 2093 -393 -581 -233 C ATOM 1657 O ARG A 215 -11.921 -20.714 9.002 1.00 22.08 O ANISOU 1657 O ARG B 215 2227 4142 2022 -52 -339 -188 O ATOM 1658 CB ARG A 215 -12.791 -23.831 9.586 1.00 27.34 C ANISOU 1658 CB ARG B 215 2325 5061 3001 -115 -481 528 C ATOM 1659 CG ARG A 215 -11.711 -24.010 8.524 1.00 30.64 C ANISOU 1659 CG ARG B 215 3530 5354 2757 -412 -511 521 C ATOM 1660 CD ARG A 215 -11.963 -25.229 7.679 1.00 31.18 C ANISOU 1660 CD ARG B 215 3610 4886 3352 -446 -575 958 C ATOM 1661 NE ARG A 215 -10.920 -25.407 6.683 1.00 37.95 N ANISOU 1661 NE ARG B 215 5808 5093 3518 -1257 -1104 1186 N ATOM 1662 CZ ARG A 215 -9.929 -26.275 6.626 1.00 36.48 C ANISOU 1662 CZ ARG B 215 4349 5340 4173 -888 -1549 1703 C ATOM 1663 NH1 ARG A 215 -9.744 -27.173 7.572 1.00 39.89 N ANISOU 1663 NH1 ARG B 215 2946 6056 6155 -399 -1443 1004 N ATOM 1664 NH2 ARG A 215 -9.110 -26.223 5.595 1.00 44.20 N ANISOU 1664 NH2 ARG B 215 7610 5774 3409 -2812 -2631 1664 N ATOM 1665 N GLU A 216 -14.125 -20.977 9.216 1.00 25.55 N ANISOU 1665 N GLU B 216 2676 5016 2016 -885 -724 -595 N ATOM 1666 CA GLU A 216 -14.365 -19.819 8.353 1.00 26.81 C ANISOU 1666 CA GLU B 216 3041 4869 2277 -575 -780 -661 C ATOM 1667 C GLU A 216 -13.775 -18.537 8.921 1.00 22.99 C ANISOU 1667 C GLU B 216 3050 3594 2090 -663 -654 -458 C ATOM 1668 O GLU A 216 -13.149 -17.787 8.161 1.00 21.91 O ANISOU 1668 O GLU B 216 3047 3289 1987 335 -474 -494 O ATOM 1669 CB GLU A 216 -15.865 -19.626 8.114 1.00 25.81 C ANISOU 1669 CB GLU B 216 2320 4893 2592 -450 -784 -499 C ATOM 1670 CG GLU A 216 -16.199 -18.563 7.091 1.00 30.27 C ANISOU 1670 CG GLU B 216 3128 5474 2898 -682 -733 -1358 C ATOM 1671 CD GLU A 216 -17.692 -18.379 6.844 1.00 34.37 C ANISOU 1671 CD GLU B 216 4249 5449 3359 -713 -2258 -1299 C ATOM 1672 OE1 GLU A 216 -18.504 -18.894 7.656 1.00 46.41 O ANISOU 1672 OE1 GLU B 216 6798 6227 4608 -2570 -1792 -235 O ATOM 1673 OE2 GLU A 216 -18.049 -17.698 5.848 1.00 51.41 O ANISOU 1673 OE2 GLU B 216 9187 6128 4217 -210 -1787 -2257 O ATOM 1674 N VAL A 217 -13.945 -18.288 10.198 1.00 21.27 N ANISOU 1674 N VAL B 217 2761 3147 2172 -471 -485 -249 N ATOM 1675 CA VAL A 217 -13.318 -17.136 10.834 1.00 19.95 C ANISOU 1675 CA VAL B 217 2670 3018 1892 -222 -291 -577 C ATOM 1676 C VAL A 217 -11.804 -17.205 10.726 1.00 19.23 C ANISOU 1676 C VAL B 217 2210 2904 2194 43 -627 -172 C ATOM 1677 O VAL A 217 -11.140 -16.211 10.430 1.00 20.05 O ANISOU 1677 O VAL B 217 2342 3070 2207 16 -323 -290 O ATOM 1678 CB VAL A 217 -13.767 -16.973 12.304 1.00 18.34 C ANISOU 1678 CB VAL B 217 2318 2761 1888 -168 -292 -616 C ATOM 1679 CG1 VAL A 217 -13.014 -15.877 13.058 1.00 20.78 C ANISOU 1679 CG1 VAL B 217 2639 2787 2470 -126 -765 -726 C ATOM 1680 CG2 VAL A 217 -15.251 -16.668 12.319 1.00 21.21 C ANISOU 1680 CG2 VAL B 217 2634 2873 2551 -422 -351 -514 C ATOM 1681 N ILE A 218 -11.193 -18.350 10.943 1.00 18.70 N ANISOU 1681 N ILE B 218 2247 2958 1898 20 -556 -234 N ATOM 1682 CA ILE A 218 -9.733 -18.477 10.928 1.00 20.99 C ANISOU 1682 CA ILE B 218 2839 2958 2177 -148 -143 -562 C ATOM 1683 C ILE A 218 -9.171 -18.199 9.556 1.00 20.81 C ANISOU 1683 C ILE B 218 2239 3350 2318 140 -527 273 C ATOM 1684 O ILE A 218 -8.190 -17.460 9.376 1.00 20.72 O ANISOU 1684 O ILE B 218 2309 2817 2748 232 -295 73 O ATOM 1685 CB ILE A 218 -9.357 -19.894 11.436 1.00 21.02 C ANISOU 1685 CB ILE B 218 2612 2906 2468 87 -487 -188 C ATOM 1686 CG1 ILE A 218 -9.610 -20.077 12.927 1.00 20.02 C ANISOU 1686 CG1 ILE B 218 2186 2851 2569 -198 -70 -586 C ATOM 1687 CG2 ILE A 218 -7.930 -20.250 11.021 1.00 23.03 C ANISOU 1687 CG2 ILE B 218 3103 2960 2686 -19 -611 -81 C ATOM 1688 CD1 ILE A 218 -9.606 -21.532 13.373 1.00 22.08 C ANISOU 1688 CD1 ILE B 218 2722 2750 2919 454 -276 -152 C ATOM 1689 N ASP A 219 -9.833 -18.801 8.546 1.00 20.85 N ANISOU 1689 N ASP B 219 2148 3416 2356 527 -474 34 N ATOM 1690 CA ASP A 219 -9.392 -18.529 7.200 1.00 23.45 C ANISOU 1690 CA ASP B 219 3002 3658 2248 375 -440 -185 C ATOM 1691 C ASP A 219 -9.594 -17.058 6.812 1.00 21.71 C ANISOU 1691 C ASP B 219 2699 3665 1886 122 -372 -215 C ATOM 1692 O ASP A 219 -8.790 -16.583 6.015 1.00 27.79 O ANISOU 1692 O ASP B 219 2970 5351 2237 252 -178 535 O ATOM 1693 CB ASP A 219 -10.087 -19.434 6.192 1.00 25.24 C ANISOU 1693 CB ASP B 219 2849 4431 2309 304 -438 -52 C ATOM 1694 CG ASP A 219 -9.576 -20.855 6.148 1.00 26.57 C ANISOU 1694 CG ASP B 219 2687 4457 2953 264 -594 -224 C ATOM 1695 OD1 ASP A 219 -8.420 -21.144 6.537 1.00 31.96 O ANISOU 1695 OD1 ASP B 219 4013 4350 3780 291 -872 -328 O ATOM 1696 OD2 ASP A 219 -10.308 -21.756 5.727 1.00 32.77 O ANISOU 1696 OD2 ASP B 219 2920 5500 4031 136 -1244 459 O ATOM 1697 N ALA A 220 -10.609 -16.361 7.280 1.00 22.74 N ANISOU 1697 N ALA B 220 3072 3405 2163 234 -642 -569 N ATOM 1698 CA ALA A 220 -10.773 -14.942 6.946 1.00 23.48 C ANISOU 1698 CA ALA B 220 3359 3063 2500 -53 -346 -1216 C ATOM 1699 C ALA A 220 -9.667 -14.121 7.591 1.00 21.28 C ANISOU 1699 C ALA B 220 3003 3043 2039 161 -423 -381 C ATOM 1700 O ALA A 220 -9.187 -13.182 6.983 1.00 23.34 O ANISOU 1700 O ALA B 220 3156 3218 2496 505 -131 -315 O ATOM 1701 CB ALA A 220 -12.137 -14.447 7.369 1.00 22.91 C ANISOU 1701 CB ALA B 220 3186 3231 2290 77 -685 -842 C ATOM 1702 N LEU A 221 -9.246 -14.494 8.807 1.00 18.46 N ANISOU 1702 N LEU B 221 2450 2824 1739 128 -674 4 N ATOM 1703 CA LEU A 221 -8.123 -13.830 9.470 1.00 18.45 C ANISOU 1703 CA LEU B 221 2166 2902 1940 227 -369 -249 C ATOM 1704 C LEU A 221 -6.856 -14.059 8.663 1.00 21.58 C ANISOU 1704 C LEU B 221 2546 3406 2247 -297 -929 173 C ATOM 1705 O LEU A 221 -6.060 -13.146 8.406 1.00 22.15 O ANISOU 1705 O LEU B 221 2840 3092 2483 20 61 -177 O ATOM 1706 CB LEU A 221 -8.089 -14.298 10.925 1.00 18.36 C ANISOU 1706 CB LEU B 221 2385 2440 2150 56 -145 -724 C ATOM 1707 CG LEU A 221 -7.015 -13.736 11.843 1.00 17.64 C ANISOU 1707 CG LEU B 221 2488 2401 1812 28 -368 -80 C ATOM 1708 CD1 LEU A 221 -7.113 -12.223 11.883 1.00 19.28 C ANISOU 1708 CD1 LEU B 221 2860 2550 1915 306 -574 92 C ATOM 1709 CD2 LEU A 221 -7.156 -14.376 13.229 1.00 19.11 C ANISOU 1709 CD2 LEU B 221 2617 3059 1585 -79 -496 68 C ATOM 1710 N GLY A 222 -6.676 -15.288 8.207 1.00 21.26 N ANISOU 1710 N GLY B 222 2838 2863 2378 -128 -694 11 N ATOM 1711 CA GLY A 222 -5.716 -15.611 7.207 1.00 20.42 C ANISOU 1711 CA GLY B 222 2742 2583 2432 411 144 -144 C ATOM 1712 C GLY A 222 -4.235 -15.700 7.551 1.00 20.75 C ANISOU 1712 C GLY B 222 3230 2430 2224 478 -364 27 C ATOM 1713 O GLY A 222 -3.748 -15.574 8.658 1.00 21.04 O ANISOU 1713 O GLY B 222 2916 3072 2007 316 85 -134 O ATOM 1714 N PRO A 223 -3.488 -15.984 6.475 1.00 22.84 N ANISOU 1714 N PRO B 223 3723 2783 2173 124 -383 139 N ATOM 1715 CA PRO A 223 -2.084 -16.338 6.585 1.00 23.57 C ANISOU 1715 CA PRO B 223 4152 2685 2119 210 -389 221 C ATOM 1716 C PRO A 223 -1.193 -15.267 7.180 1.00 24.55 C ANISOU 1716 C PRO B 223 3856 3086 2386 -429 163 368 C ATOM 1717 O PRO A 223 -0.092 -15.660 7.603 1.00 27.93 O ANISOU 1717 O PRO B 223 4968 3311 2333 -235 -771 106 O ATOM 1718 CB PRO A 223 -1.614 -16.572 5.146 1.00 30.24 C ANISOU 1718 CB PRO B 223 6119 3276 2094 -537 -385 308 C ATOM 1719 CG PRO A 223 -2.850 -16.732 4.346 1.00 39.79 C ANISOU 1719 CG PRO B 223 9695 3471 1953 -1851 -714 405 C ATOM 1720 CD PRO A 223 -3.967 -16.037 5.079 1.00 26.59 C ANISOU 1720 CD PRO B 223 4674 3144 2283 -42 -794 103 C ATOM 1721 N LYS A 224 -1.656 -14.035 7.235 1.00 23.59 N ANISOU 1721 N LYS B 224 3618 3364 1980 -358 -369 338 N ATOM 1722 CA LYS A 224 -0.869 -12.979 7.842 1.00 27.36 C ANISOU 1722 CA LYS B 224 3759 4644 1992 -907 -457 754 C ATOM 1723 C LYS A 224 -1.577 -12.399 9.071 1.00 25.70 C ANISOU 1723 C LYS B 224 3129 4043 2591 -583 -472 945 C ATOM 1724 O LYS A 224 -1.042 -11.464 9.691 1.00 33.30 O ANISOU 1724 O LYS B 224 3271 6470 2912 -1268 -759 1729 O ATOM 1725 CB LYS A 224 -0.556 -11.868 6.845 1.00 29.28 C ANISOU 1725 CB LYS B 224 3636 4991 2496 -197 -354 1107 C ATOM 1726 CG LYS A 224 0.028 -12.244 5.513 1.00 33.46 C ANISOU 1726 CG LYS B 224 4153 5539 3023 -930 229 1868 C ATOM 1727 CD LYS A 224 1.433 -12.791 5.597 1.00 38.86 C ANISOU 1727 CD LYS B 224 5110 5680 3976 -1453 391 1858 C ATOM 1728 CE LYS A 224 1.988 -12.967 4.193 1.00 50.19 C ANISOU 1728 CE LYS B 224 8356 6360 4355 -2842 -1365 2803 C ATOM 1729 NZ LYS A 224 2.815 -14.210 4.066 1.00 54.87 N ANISOU 1729 NZ LYS B 224 8807 7140 4903 -2016 -1770 2903 N ATOM 1730 N GLY A 225 -2.705 -12.984 9.445 1.00 20.21 N ANISOU 1730 N GLY B 225 2994 2931 1755 -203 -199 -68 N ATOM 1731 CA GLY A 225 -3.365 -12.640 10.685 1.00 18.23 C ANISOU 1731 CA GLY B 225 2412 2653 1862 247 55 -36 C ATOM 1732 C GLY A 225 -2.937 -13.413 11.914 1.00 17.34 C ANISOU 1732 C GLY B 225 2401 2370 1816 134 -201 -40 C ATOM 1733 O GLY A 225 -2.436 -14.541 11.827 1.00 17.89 O ANISOU 1733 O GLY B 225 2834 2173 1792 166 -88 30 O ATOM 1734 N VAL A 226 -3.151 -12.846 13.112 1.00 16.46 N ANISOU 1734 N VAL B 226 2318 2152 1782 97 -170 -133 N ATOM 1735 CA VAL A 226 -2.845 -13.419 14.412 1.00 15.24 C ANISOU 1735 CA VAL B 226 1935 2007 1848 185 -174 -90 C ATOM 1736 C VAL A 226 -4.075 -13.396 15.297 1.00 15.17 C ANISOU 1736 C VAL B 226 2163 1795 1807 213 -54 -313 C ATOM 1737 O VAL A 226 -4.719 -12.360 15.450 1.00 16.35 O ANISOU 1737 O VAL B 226 2035 1764 2413 146 -368 -187 O ATOM 1738 CB VAL A 226 -1.710 -12.610 15.059 1.00 15.64 C ANISOU 1738 CB VAL B 226 2046 2120 1777 129 -186 -125 C ATOM 1739 CG1 VAL A 226 -1.467 -13.043 16.483 1.00 16.76 C ANISOU 1739 CG1 VAL B 226 2050 2202 2118 283 -56 -595 C ATOM 1740 CG2 VAL A 226 -0.446 -12.764 14.188 1.00 18.78 C ANISOU 1740 CG2 VAL B 226 2177 2304 2656 -87 -14 155 C ATOM 1741 N LEU A 227 -4.383 -14.557 15.870 1.00 16.20 N ANISOU 1741 N LEU B 227 2072 2171 1910 211 -11 -95 N ATOM 1742 CA LEU A 227 -5.452 -14.775 16.821 1.00 14.19 C ANISOU 1742 CA LEU B 227 1862 1785 1743 183 -442 7 C ATOM 1743 C LEU A 227 -4.908 -14.663 18.248 1.00 14.28 C ANISOU 1743 C LEU B 227 1956 1685 1784 412 -390 -121 C ATOM 1744 O LEU A 227 -3.881 -15.269 18.530 1.00 15.54 O ANISOU 1744 O LEU B 227 2405 1687 1811 255 -84 -101 O ATOM 1745 CB LEU A 227 -6.078 -16.169 16.654 1.00 14.96 C ANISOU 1745 CB LEU B 227 1775 1758 2152 171 -311 -481 C ATOM 1746 CG LEU A 227 -7.257 -16.440 17.604 1.00 17.70 C ANISOU 1746 CG LEU B 227 1920 2017 2787 212 -120 -59 C ATOM 1747 CD1 LEU A 227 -8.443 -15.568 17.272 1.00 16.78 C ANISOU 1747 CD1 LEU B 227 2043 2042 2289 -90 -141 -119 C ATOM 1748 CD2 LEU A 227 -7.643 -17.898 17.571 1.00 18.28 C ANISOU 1748 CD2 LEU B 227 1873 2369 2704 56 -218 -279 C ATOM 1749 N ILE A 228 -5.590 -13.875 19.077 1.00 14.05 N ANISOU 1749 N ILE B 228 1662 1885 1792 124 -376 167 N ATOM 1750 CA ILE A 228 -5.229 -13.752 20.490 1.00 13.94 C ANISOU 1750 CA ILE B 228 1759 1787 1749 221 -307 -8 C ATOM 1751 C ILE A 228 -6.403 -14.263 21.321 1.00 14.50 C ANISOU 1751 C ILE B 228 1710 1939 1861 43 -282 -45 C ATOM 1752 O ILE A 228 -7.488 -13.688 21.201 1.00 16.62 O ANISOU 1752 O ILE B 228 2413 1947 1954 12 310 -92 O ATOM 1753 CB ILE A 228 -4.886 -12.309 20.891 1.00 13.87 C ANISOU 1753 CB ILE B 228 1662 2037 1572 174 -254 -326 C ATOM 1754 CG1 ILE A 228 -3.775 -11.712 20.017 1.00 15.69 C ANISOU 1754 CG1 ILE B 228 1930 1934 2098 140 98 -223 C ATOM 1755 CG2 ILE A 228 -4.561 -12.182 22.394 1.00 15.07 C ANISOU 1755 CG2 ILE B 228 2124 1935 1665 -23 -518 -201 C ATOM 1756 CD1 ILE A 228 -2.397 -12.354 20.214 1.00 14.55 C ANISOU 1756 CD1 ILE B 228 1738 1875 1916 469 -167 -64 C ATOM 1757 N ASN A 229 -6.262 -15.306 22.124 1.00 14.74 N ANISOU 1757 N ASN B 229 1767 1754 2080 123 -209 57 N ATOM 1758 CA ASN A 229 -7.365 -15.776 22.956 1.00 14.71 C ANISOU 1758 CA ASN B 229 1729 1691 2170 172 -117 21 C ATOM 1759 C ASN A 229 -6.991 -15.659 24.430 1.00 15.50 C ANISOU 1759 C ASN B 229 1685 2068 2136 235 -129 -53 C ATOM 1760 O ASN A 229 -6.161 -16.415 24.920 1.00 15.48 O ANISOU 1760 O ASN B 229 1877 1819 2188 -63 -244 44 O ATOM 1761 CB ASN A 229 -7.780 -17.210 22.640 1.00 15.35 C ANISOU 1761 CB ASN B 229 1764 1853 2216 120 -283 -46 C ATOM 1762 CG ASN A 229 -9.096 -17.572 23.302 1.00 16.15 C ANISOU 1762 CG ASN B 229 1671 2184 2281 21 -372 -13 C ATOM 1763 OD1 ASN A 229 -9.742 -16.713 23.920 1.00 15.52 O ANISOU 1763 OD1 ASN B 229 1561 2275 2063 59 -95 115 O ATOM 1764 ND2 ASN A 229 -9.516 -18.830 23.144 1.00 17.20 N ANISOU 1764 ND2 ASN B 229 1700 2398 2438 -25 -632 50 N ATOM 1765 N ILE A 230 -7.623 -14.701 25.098 1.00 15.57 N ANISOU 1765 N ILE B 230 1946 1869 2103 122 -312 -188 N ATOM 1766 CA ILE A 230 -7.568 -14.541 26.536 1.00 15.90 C ANISOU 1766 CA ILE B 230 1814 2063 2164 -42 -177 11 C ATOM 1767 C ILE A 230 -8.929 -14.841 27.182 1.00 18.14 C ANISOU 1767 C ILE B 230 2543 1940 2409 -517 -663 271 C ATOM 1768 O ILE A 230 -9.107 -14.543 28.352 1.00 19.98 O ANISOU 1768 O ILE B 230 2352 2645 2593 -583 -763 677 O ATOM 1769 CB ILE A 230 -7.036 -13.161 26.953 1.00 17.85 C ANISOU 1769 CB ILE B 230 2080 2296 2407 130 -485 336 C ATOM 1770 CG1 ILE A 230 -7.745 -11.986 26.288 1.00 21.69 C ANISOU 1770 CG1 ILE B 230 2254 2538 3447 540 -546 120 C ATOM 1771 CG2 ILE A 230 -5.525 -13.188 26.724 1.00 17.97 C ANISOU 1771 CG2 ILE B 230 1772 2576 2479 -103 -486 45 C ATOM 1772 CD1 ILE A 230 -9.077 -11.594 26.835 1.00 30.31 C ANISOU 1772 CD1 ILE B 230 5460 2245 3812 -59 567 -637 C ATOM 1773 N GLY A 231 -9.839 -15.411 26.415 1.00 17.46 N ANISOU 1773 N GLY B 231 2029 2199 2408 -241 -428 -36 N ATOM 1774 CA GLY A 231 -11.188 -15.718 26.859 1.00 17.19 C ANISOU 1774 CA GLY B 231 1732 1869 2930 25 -510 17 C ATOM 1775 C GLY A 231 -11.229 -17.050 27.557 1.00 16.01 C ANISOU 1775 C GLY B 231 1871 1981 2232 263 -518 309 C ATOM 1776 O GLY A 231 -10.806 -17.369 28.672 1.00 19.53 O ANISOU 1776 O GLY B 231 2504 2184 2730 -129 -593 -307 O ATOM 1777 N ARG A 232 -11.707 -18.083 26.928 1.00 18.13 N ANISOU 1777 N ARG B 232 1661 2842 2384 65 -275 42 N ATOM 1778 CA ARG A 232 -11.879 -19.461 27.166 1.00 16.48 C ANISOU 1778 CA ARG B 232 1500 2848 1916 -155 -330 -134 C ATOM 1779 C ARG A 232 -11.583 -20.324 25.942 1.00 16.21 C ANISOU 1779 C ARG B 232 1710 2501 1949 -163 -356 -87 C ATOM 1780 O ARG A 232 -11.821 -20.024 24.790 1.00 16.34 O ANISOU 1780 O ARG B 232 1932 2384 1891 -277 -254 70 O ATOM 1781 CB ARG A 232 -13.293 -19.791 27.696 1.00 17.69 C ANISOU 1781 CB ARG B 232 2243 2912 1566 -240 247 -192 C ATOM 1782 CG ARG A 232 -13.629 -19.040 28.989 1.00 23.23 C ANISOU 1782 CG ARG B 232 3626 3116 2084 53 -202 175 C ATOM 1783 CD ARG A 232 -13.029 -19.754 30.207 1.00 34.48 C ANISOU 1783 CD ARG B 232 7067 4278 1757 -1980 -739 -951 C ATOM 1784 NE ARG A 232 -13.587 -19.260 31.462 1.00 30.44 N ANISOU 1784 NE ARG B 232 3887 5438 2240 -840 649 -105 N ATOM 1785 CZ ARG A 232 -13.098 -18.290 32.228 1.00 27.93 C ANISOU 1785 CZ ARG B 232 2915 4434 3263 198 973 197 C ATOM 1786 NH1 ARG A 232 -11.992 -17.643 31.889 1.00 41.10 N ANISOU 1786 NH1 ARG B 232 3537 3793 8287 -391 -229 2674 N ATOM 1787 NH2 ARG A 232 -13.651 -17.880 33.366 1.00 32.43 N ANISOU 1787 NH2 ARG B 232 4226 5583 2513 -570 391 -175 N ATOM 1788 N GLY A 233 -11.013 -21.489 26.244 1.00 16.88 N ANISOU 1788 N GLY B 233 1639 2789 1984 -94 -149 -18 N ATOM 1789 CA GLY A 233 -10.630 -22.437 25.250 1.00 17.71 C ANISOU 1789 CA GLY B 233 1724 2686 2318 -5 -431 -100 C ATOM 1790 C GLY A 233 -11.751 -22.783 24.287 1.00 19.36 C ANISOU 1790 C GLY B 233 1846 3442 2068 -447 -276 -131 C ATOM 1791 O GLY A 233 -11.501 -22.726 23.074 1.00 18.32 O ANISOU 1791 O GLY B 233 2217 2656 2086 -24 -119 -102 O ATOM 1792 N PRO A 234 -12.924 -23.139 24.758 1.00 17.36 N ANISOU 1792 N PRO B 234 1746 2842 2009 -145 -229 -194 N ATOM 1793 CA PRO A 234 -14.004 -23.485 23.817 1.00 18.17 C ANISOU 1793 CA PRO B 234 2150 2796 1958 -335 -195 -164 C ATOM 1794 C PRO A 234 -14.554 -22.333 22.978 1.00 18.38 C ANISOU 1794 C PRO B 234 1995 2952 2039 -572 49 -287 C ATOM 1795 O PRO A 234 -15.463 -22.525 22.176 1.00 18.95 O ANISOU 1795 O PRO B 234 2314 2766 2120 -339 -288 -228 O ATOM 1796 CB PRO A 234 -15.099 -24.066 24.747 1.00 20.48 C ANISOU 1796 CB PRO B 234 1978 3602 2201 -592 97 -686 C ATOM 1797 CG PRO A 234 -14.327 -24.529 25.947 1.00 18.39 C ANISOU 1797 CG PRO B 234 1653 2986 2348 -106 -56 -613 C ATOM 1798 CD PRO A 234 -13.351 -23.381 26.152 1.00 18.28 C ANISOU 1798 CD PRO B 234 1826 3121 1999 -261 -443 3 C ATOM 1799 N HIS A 235 -14.050 -21.119 23.079 1.00 18.80 N ANISOU 1799 N HIS B 235 2075 2730 2339 -398 -47 -26 N ATOM 1800 CA HIS A 235 -14.327 -20.097 22.100 1.00 18.33 C ANISOU 1800 CA HIS B 235 2038 2540 2388 -240 -107 135 C ATOM 1801 C HIS A 235 -13.796 -20.453 20.704 1.00 18.29 C ANISOU 1801 C HIS B 235 1953 2717 2278 -289 -100 99 C ATOM 1802 O HIS A 235 -14.286 -19.858 19.721 1.00 19.48 O ANISOU 1802 O HIS B 235 2082 2876 2445 -437 -188 -237 O ATOM 1803 CB HIS A 235 -13.706 -18.734 22.461 1.00 18.03 C ANISOU 1803 CB HIS B 235 2113 2385 2354 -315 -174 138 C ATOM 1804 CG HIS A 235 -14.565 -18.042 23.465 1.00 19.14 C ANISOU 1804 CG HIS B 235 2258 2388 2625 -403 -387 244 C ATOM 1805 ND1 HIS A 235 -15.851 -17.702 23.649 1.00 22.70 N ANISOU 1805 ND1 HIS B 235 3649 2243 2731 -457 -382 101 N ATOM 1806 CD2 HIS A 235 -14.011 -17.438 24.514 1.00 16.41 C ANISOU 1806 CD2 HIS B 235 1479 2379 2378 -60 89 220 C ATOM 1807 CE1 HIS A 235 -16.052 -17.013 24.763 1.00 19.37 C ANISOU 1807 CE1 HIS B 235 2480 2488 2391 -306 310 292 C ATOM 1808 NE2 HIS A 235 -14.879 -16.842 25.357 1.00 20.66 N ANISOU 1808 NE2 HIS B 235 2855 2769 2227 -266 87 361 N ATOM 1809 N VAL A 236 -12.822 -21.357 20.685 1.00 18.01 N ANISOU 1809 N VAL B 236 2146 2867 1829 -8 -677 -52 N ATOM 1810 CA VAL A 236 -12.198 -21.742 19.423 1.00 18.24 C ANISOU 1810 CA VAL B 236 2284 2793 1852 143 -716 -140 C ATOM 1811 C VAL A 236 -12.438 -23.207 19.120 1.00 18.93 C ANISOU 1811 C VAL B 236 2453 2725 2014 340 -700 -177 C ATOM 1812 O VAL A 236 -12.356 -24.036 20.023 1.00 19.30 O ANISOU 1812 O VAL B 236 2256 3032 2047 3 -415 -52 O ATOM 1813 CB VAL A 236 -10.699 -21.479 19.493 1.00 17.77 C ANISOU 1813 CB VAL B 236 2609 2266 1879 309 -926 65 C ATOM 1814 CG1 VAL A 236 -10.071 -21.758 18.124 1.00 20.34 C ANISOU 1814 CG1 VAL B 236 2390 3409 1929 413 -611 407 C ATOM 1815 CG2 VAL A 236 -10.373 -20.045 19.920 1.00 17.71 C ANISOU 1815 CG2 VAL B 236 2427 2452 1852 -60 -857 184 C ATOM 1816 N ASP A 237 -12.713 -23.522 17.864 1.00 18.70 N ANISOU 1816 N ASP B 237 2101 3040 1966 260 -569 -57 N ATOM 1817 CA ASP A 237 -12.681 -24.865 17.347 1.00 19.78 C ANISOU 1817 CA ASP B 237 2039 3238 2239 108 -710 41 C ATOM 1818 C ASP A 237 -11.220 -25.286 17.294 1.00 17.83 C ANISOU 1818 C ASP B 237 1610 3103 2060 360 -10 3 C ATOM 1819 O ASP A 237 -10.583 -25.112 16.250 1.00 21.70 O ANISOU 1819 O ASP B 237 2356 3893 1995 11 -147 299 O ATOM 1820 CB ASP A 237 -13.308 -24.956 15.956 1.00 22.58 C ANISOU 1820 CB ASP B 237 2299 3760 2519 125 -1025 -218 C ATOM 1821 CG ASP A 237 -13.580 -26.372 15.479 1.00 24.97 C ANISOU 1821 CG ASP B 237 2741 3658 3088 395 -1526 -350 C ATOM 1822 OD1 ASP A 237 -12.980 -27.298 16.083 1.00 29.29 O ANISOU 1822 OD1 ASP B 237 3185 4541 3405 962 -1229 -632 O ATOM 1823 OD2 ASP A 237 -14.337 -26.580 14.528 1.00 28.34 O ANISOU 1823 OD2 ASP B 237 2528 5158 3080 -71 -1315 -752 O ATOM 1824 N GLU A 238 -10.686 -25.781 18.414 1.00 19.51 N ANISOU 1824 N GLU B 238 1824 3458 2129 164 -271 -204 N ATOM 1825 CA GLU A 238 -9.222 -25.897 18.557 1.00 19.86 C ANISOU 1825 CA GLU B 238 2054 3484 2007 131 -390 -140 C ATOM 1826 C GLU A 238 -8.556 -26.790 17.517 1.00 18.98 C ANISOU 1826 C GLU B 238 1743 3355 2113 500 -30 -180 C ATOM 1827 O GLU A 238 -7.499 -26.386 16.987 1.00 20.51 O ANISOU 1827 O GLU B 238 1920 3660 2214 253 -243 27 O ATOM 1828 CB GLU A 238 -8.881 -26.381 19.954 1.00 20.84 C ANISOU 1828 CB GLU B 238 2179 3686 2053 -242 -196 -252 C ATOM 1829 CG GLU A 238 -7.422 -26.216 20.301 1.00 19.18 C ANISOU 1829 CG GLU B 238 1945 2931 2413 292 -239 -132 C ATOM 1830 CD GLU A 238 -7.231 -26.444 21.794 1.00 19.53 C ANISOU 1830 CD GLU B 238 2284 2670 2467 250 -410 -263 C ATOM 1831 OE1 GLU A 238 -6.861 -27.560 22.206 1.00 20.43 O ANISOU 1831 OE1 GLU B 238 2457 2833 2471 399 -287 -202 O ATOM 1832 OE2 GLU A 238 -7.538 -25.469 22.514 1.00 19.12 O ANISOU 1832 OE2 GLU B 238 2020 2877 2368 280 -321 -287 O ATOM 1833 N PRO A 239 -9.071 -27.959 17.156 1.00 24.07 N ANISOU 1833 N PRO B 239 1951 4122 3074 124 -470 586 N ATOM 1834 CA PRO A 239 -8.441 -28.742 16.088 1.00 22.16 C ANISOU 1834 CA PRO B 239 1941 3753 2727 357 -444 144 C ATOM 1835 C PRO A 239 -8.323 -27.985 14.773 1.00 22.76 C ANISOU 1835 C PRO B 239 2057 3919 2672 -226 -451 -201 C ATOM 1836 O PRO A 239 -7.304 -28.157 14.078 1.00 23.48 O ANISOU 1836 O PRO B 239 2452 4000 2471 364 -575 170 O ATOM 1837 CB PRO A 239 -9.349 -29.979 15.902 1.00 24.45 C ANISOU 1837 CB PRO B 239 2013 4656 2623 192 -470 498 C ATOM 1838 CG PRO A 239 -9.948 -30.111 17.284 1.00 23.60 C ANISOU 1838 CG PRO B 239 1921 4506 2541 -48 -756 536 C ATOM 1839 CD PRO A 239 -10.217 -28.680 17.718 1.00 21.89 C ANISOU 1839 CD PRO B 239 1750 4284 2284 -98 -797 52 C ATOM 1840 N GLU A 240 -9.295 -27.137 14.435 1.00 21.58 N ANISOU 1840 N GLU B 240 2069 3972 2159 1 -804 -109 N ATOM 1841 CA GLU A 240 -9.181 -26.293 13.234 1.00 21.52 C ANISOU 1841 CA GLU B 240 2106 3637 2432 -38 -471 179 C ATOM 1842 C GLU A 240 -8.110 -25.211 13.386 1.00 19.80 C ANISOU 1842 C GLU B 240 2148 2971 2404 122 -630 666 C ATOM 1843 O GLU A 240 -7.411 -24.837 12.444 1.00 20.84 O ANISOU 1843 O GLU B 240 2130 3348 2441 -126 -582 462 O ATOM 1844 CB GLU A 240 -10.509 -25.659 12.894 1.00 23.02 C ANISOU 1844 CB GLU B 240 2284 3848 2614 7 -1016 -340 C ATOM 1845 CG GLU A 240 -11.649 -26.587 12.500 1.00 27.29 C ANISOU 1845 CG GLU B 240 2584 5086 2700 -511 -920 -856 C ATOM 1846 CD GLU A 240 -11.533 -27.159 11.116 1.00 29.54 C ANISOU 1846 CD GLU B 240 2798 5399 3026 -210 -1376 -659 C ATOM 1847 OE1 GLU A 240 -10.658 -26.730 10.319 1.00 27.76 O ANISOU 1847 OE1 GLU B 240 2962 4457 3129 20 -1575 -189 O ATOM 1848 OE2 GLU A 240 -12.362 -28.056 10.834 1.00 36.60 O ANISOU 1848 OE2 GLU B 240 3080 6530 4295 -669 -1861 460 O ATOM 1849 N LEU A 241 -7.955 -24.660 14.582 1.00 18.95 N ANISOU 1849 N LEU B 241 2180 2679 2340 274 -641 308 N ATOM 1850 CA LEU A 241 -6.875 -23.687 14.813 1.00 18.52 C ANISOU 1850 CA LEU B 241 2262 2767 2008 187 -466 147 C ATOM 1851 C LEU A 241 -5.505 -24.325 14.621 1.00 18.45 C ANISOU 1851 C LEU B 241 2244 2666 2100 280 -406 -21 C ATOM 1852 O LEU A 241 -4.654 -23.785 13.914 1.00 18.46 O ANISOU 1852 O LEU B 241 2249 2679 2087 293 -428 104 O ATOM 1853 CB LEU A 241 -7.018 -23.162 16.218 1.00 18.43 C ANISOU 1853 CB LEU B 241 2294 2703 2006 218 -575 -14 C ATOM 1854 CG LEU A 241 -5.979 -22.143 16.649 1.00 19.76 C ANISOU 1854 CG LEU B 241 2448 2914 2148 -307 -585 571 C ATOM 1855 CD1 LEU A 241 -6.035 -20.901 15.777 1.00 25.21 C ANISOU 1855 CD1 LEU B 241 2303 4730 2544 44 -226 628 C ATOM 1856 CD2 LEU A 241 -6.116 -21.718 18.114 1.00 20.72 C ANISOU 1856 CD2 LEU B 241 2410 3241 2222 -131 -718 642 C ATOM 1857 N VAL A 242 -5.291 -25.491 15.256 1.00 19.34 N ANISOU 1857 N VAL B 242 2220 3018 2110 417 -479 -65 N ATOM 1858 CA VAL A 242 -4.012 -26.184 15.091 1.00 21.18 C ANISOU 1858 CA VAL B 242 2395 2928 2724 693 -348 -77 C ATOM 1859 C VAL A 242 -3.743 -26.494 13.618 1.00 21.33 C ANISOU 1859 C VAL B 242 2992 2474 2640 734 -322 -191 C ATOM 1860 O VAL A 242 -2.634 -26.223 13.148 1.00 23.19 O ANISOU 1860 O VAL B 242 2835 3072 2905 499 -824 331 O ATOM 1861 CB VAL A 242 -3.931 -27.494 15.902 1.00 20.65 C ANISOU 1861 CB VAL B 242 2105 3049 2691 423 -316 -7 C ATOM 1862 CG1 VAL A 242 -2.624 -28.260 15.667 1.00 23.77 C ANISOU 1862 CG1 VAL B 242 2488 3012 3531 804 134 -92 C ATOM 1863 CG2 VAL A 242 -4.117 -27.182 17.378 1.00 22.54 C ANISOU 1863 CG2 VAL B 242 2525 3500 2538 549 -583 -361 C ATOM 1864 N SER A 243 -4.702 -27.058 12.866 1.00 21.77 N ANISOU 1864 N SER B 243 2304 3166 2803 711 -460 552 N ATOM 1865 CA SER A 243 -4.508 -27.357 11.456 1.00 25.05 C ANISOU 1865 CA SER B 243 1443 4795 3282 714 -939 1560 C ATOM 1866 C SER A 243 -4.109 -26.113 10.672 1.00 21.20 C ANISOU 1866 C SER B 243 1882 3622 2552 377 -826 885 C ATOM 1867 O SER A 243 -3.216 -26.139 9.835 1.00 25.93 O ANISOU 1867 O SER B 243 3023 3672 3158 475 -215 1088 O ATOM 1868 CB SER A 243 -5.818 -27.899 10.856 1.00 27.55 C ANISOU 1868 CB SER B 243 1593 5815 3059 654 -476 292 C ATOM 1869 OG SER A 243 -5.628 -28.162 9.479 1.00 37.82 O ANISOU 1869 OG SER B 243 4930 6146 3293 7 -1358 459 O ATOM 1870 N ALA A 244 -4.826 -25.007 10.941 1.00 22.07 N ANISOU 1870 N ALA B 244 2422 3679 2285 555 -880 783 N ATOM 1871 CA ALA A 244 -4.598 -23.772 10.218 1.00 21.47 C ANISOU 1871 CA ALA B 244 2795 2857 2505 445 -670 493 C ATOM 1872 C ALA A 244 -3.184 -23.252 10.486 1.00 22.14 C ANISOU 1872 C ALA B 244 2722 2903 2787 453 -136 -82 C ATOM 1873 O ALA A 244 -2.489 -22.763 9.580 1.00 22.36 O ANISOU 1873 O ALA B 244 2538 3599 2360 359 -664 382 O ATOM 1874 CB ALA A 244 -5.675 -22.750 10.587 1.00 24.82 C ANISOU 1874 CB ALA B 244 3484 2812 3136 479 -1811 238 C ATOM 1875 N LEU A 245 -2.729 -23.366 11.754 1.00 19.82 N ANISOU 1875 N LEU B 245 2460 2406 2663 594 -222 199 N ATOM 1876 CA LEU A 245 -1.369 -22.928 12.055 1.00 19.39 C ANISOU 1876 CA LEU B 245 2446 2560 2359 459 58 214 C ATOM 1877 C LEU A 245 -0.330 -23.803 11.365 1.00 21.71 C ANISOU 1877 C LEU B 245 2679 2649 2923 206 -507 449 C ATOM 1878 O LEU A 245 0.658 -23.356 10.797 1.00 26.97 O ANISOU 1878 O LEU B 245 3006 3192 4051 428 -106 1358 O ATOM 1879 CB LEU A 245 -1.141 -22.913 13.566 1.00 19.34 C ANISOU 1879 CB LEU B 245 2609 2335 2404 814 66 -41 C ATOM 1880 CG LEU A 245 -1.923 -21.765 14.244 1.00 18.08 C ANISOU 1880 CG LEU B 245 2014 2301 2553 259 -108 252 C ATOM 1881 CD1 LEU A 245 -2.099 -22.066 15.701 1.00 20.33 C ANISOU 1881 CD1 LEU B 245 2608 2531 2584 294 63 219 C ATOM 1882 CD2 LEU A 245 -1.239 -20.402 14.045 1.00 19.96 C ANISOU 1882 CD2 LEU B 245 1930 2694 2959 152 -116 510 C ATOM 1883 N VAL A 246 -0.535 -25.092 11.401 1.00 24.42 N ANISOU 1883 N VAL B 246 2820 2637 3822 292 -421 880 N ATOM 1884 CA VAL A 246 0.418 -26.043 10.854 1.00 24.81 C ANISOU 1884 CA VAL B 246 3251 2674 3502 492 32 910 C ATOM 1885 C VAL A 246 0.498 -25.825 9.347 1.00 25.92 C ANISOU 1885 C VAL B 246 2912 3498 3440 856 -151 851 C ATOM 1886 O VAL A 246 1.586 -25.832 8.753 1.00 32.60 O ANISOU 1886 O VAL B 246 5773 3315 3297 723 433 915 O ATOM 1887 CB VAL A 246 0.006 -27.467 11.246 1.00 23.35 C ANISOU 1887 CB VAL B 246 3028 3112 2731 622 -511 772 C ATOM 1888 CG1 VAL A 246 0.669 -28.557 10.415 1.00 28.63 C ANISOU 1888 CG1 VAL B 246 3971 3299 3607 1062 -255 1199 C ATOM 1889 CG2 VAL A 246 0.329 -27.740 12.721 1.00 25.10 C ANISOU 1889 CG2 VAL B 246 3662 2764 3111 717 -574 115 C ATOM 1890 N GLU A 247 -0.649 -25.576 8.725 1.00 27.05 N ANISOU 1890 N GLU B 247 3719 3324 3236 1096 -92 953 N ATOM 1891 CA GLU A 247 -0.678 -25.494 7.263 1.00 27.21 C ANISOU 1891 CA GLU B 247 3554 3563 3222 857 -279 1008 C ATOM 1892 C GLU A 247 -0.459 -24.120 6.650 1.00 26.54 C ANISOU 1892 C GLU B 247 3735 3546 2801 1013 -403 832 C ATOM 1893 O GLU A 247 -0.502 -23.965 5.428 1.00 28.46 O ANISOU 1893 O GLU B 247 3890 4135 2788 620 -398 748 O ATOM 1894 CB GLU A 247 -2.024 -26.032 6.765 1.00 31.69 C ANISOU 1894 CB GLU B 247 3679 4238 4124 792 -1356 1458 C ATOM 1895 CG GLU A 247 -2.278 -27.480 7.130 1.00 32.10 C ANISOU 1895 CG GLU B 247 3763 3895 4538 457 -709 1447 C ATOM 1896 CD GLU A 247 -3.636 -27.964 6.648 1.00 36.73 C ANISOU 1896 CD GLU B 247 3669 4885 5400 844 -1477 439 C ATOM 1897 OE1 GLU A 247 -4.502 -27.172 6.204 1.00 35.16 O ANISOU 1897 OE1 GLU B 247 4059 4690 4612 785 -1921 668 O ATOM 1898 OE2 GLU A 247 -3.827 -29.197 6.754 1.00 50.09 O ANISOU 1898 OE2 GLU B 247 3813 6357 8861 1422 -2260 -804 O ATOM 1899 N GLY A 248 -0.207 -23.117 7.466 1.00 26.03 N ANISOU 1899 N GLY B 248 3555 3640 2696 1012 -191 863 N ATOM 1900 CA GLY A 248 0.072 -21.777 7.002 1.00 25.57 C ANISOU 1900 CA GLY B 248 3421 3644 2650 677 -223 347 C ATOM 1901 C GLY A 248 -1.149 -20.946 6.696 1.00 23.63 C ANISOU 1901 C GLY B 248 2971 3703 2303 533 -402 215 C ATOM 1902 O GLY A 248 -1.005 -19.841 6.150 1.00 26.84 O ANISOU 1902 O GLY B 248 3623 3587 2987 492 493 380 O ATOM 1903 N ARG A 249 -2.325 -21.437 7.031 1.00 22.90 N ANISOU 1903 N ARG B 249 2828 3681 2191 695 -498 509 N ATOM 1904 CA ARG A 249 -3.547 -20.701 6.720 1.00 21.80 C ANISOU 1904 CA ARG B 249 2817 3808 1658 485 -242 212 C ATOM 1905 C ARG A 249 -3.846 -19.591 7.732 1.00 18.91 C ANISOU 1905 C ARG B 249 2415 3142 1628 74 -167 262 C ATOM 1906 O ARG A 249 -4.626 -18.671 7.461 1.00 21.36 O ANISOU 1906 O ARG B 249 3048 3114 1953 92 -260 25 O ATOM 1907 CB ARG A 249 -4.724 -21.677 6.615 1.00 24.16 C ANISOU 1907 CB ARG B 249 2960 4148 2072 424 -786 326 C ATOM 1908 CG ARG A 249 -4.744 -22.459 5.289 1.00 27.35 C ANISOU 1908 CG ARG B 249 3480 4694 2217 202 -988 624 C ATOM 1909 CD ARG A 249 -5.951 -23.377 5.197 1.00 31.66 C ANISOU 1909 CD ARG B 249 3466 6165 2397 -67 -1135 344 C ATOM 1910 NE ARG A 249 -5.984 -24.470 6.147 1.00 30.74 N ANISOU 1910 NE ARG B 249 3352 5507 2819 243 -1015 732 N ATOM 1911 CZ ARG A 249 -6.774 -24.594 7.199 1.00 26.82 C ANISOU 1911 CZ ARG B 249 3159 4441 2590 542 -1067 360 C ATOM 1912 NH1 ARG A 249 -7.692 -23.711 7.575 1.00 25.24 N ANISOU 1912 NH1 ARG B 249 2862 4280 2449 600 -1528 -86 N ATOM 1913 NH2 ARG A 249 -6.610 -25.706 7.925 1.00 26.22 N ANISOU 1913 NH2 ARG B 249 2760 3647 3556 96 -789 361 N ATOM 1914 N LEU A 250 -3.221 -19.667 8.917 1.00 20.17 N ANISOU 1914 N LEU B 250 2632 2912 2120 175 -693 82 N ATOM 1915 CA LEU A 250 -3.263 -18.608 9.925 1.00 18.55 C ANISOU 1915 CA LEU B 250 2475 2672 1902 290 -474 -3 C ATOM 1916 C LEU A 250 -1.854 -18.179 10.255 1.00 17.44 C ANISOU 1916 C LEU B 250 2499 2441 1687 375 -434 -19 C ATOM 1917 O LEU A 250 -0.986 -19.016 10.467 1.00 21.26 O ANISOU 1917 O LEU B 250 3082 2409 2585 396 -89 -43 O ATOM 1918 CB LEU A 250 -3.965 -19.079 11.201 1.00 19.17 C ANISOU 1918 CB LEU B 250 2077 3074 2134 458 -424 118 C ATOM 1919 CG LEU A 250 -4.097 -18.070 12.343 1.00 16.37 C ANISOU 1919 CG LEU B 250 2007 2457 1756 229 -385 -144 C ATOM 1920 CD1 LEU A 250 -4.971 -16.916 11.904 1.00 19.97 C ANISOU 1920 CD1 LEU B 250 3044 2373 2170 487 171 294 C ATOM 1921 CD2 LEU A 250 -4.599 -18.752 13.610 1.00 19.49 C ANISOU 1921 CD2 LEU B 250 2605 2465 2335 310 191 264 C ATOM 1922 N GLY A 251 -1.563 -16.900 10.365 1.00 18.13 N ANISOU 1922 N GLY B 251 2459 2402 2029 193 -474 426 N ATOM 1923 CA GLY A 251 -0.238 -16.399 10.579 1.00 17.48 C ANISOU 1923 CA GLY B 251 2524 2464 1652 184 -408 240 C ATOM 1924 C GLY A 251 0.378 -16.684 11.929 1.00 18.97 C ANISOU 1924 C GLY B 251 3229 2230 1750 80 -66 186 C ATOM 1925 O GLY A 251 1.583 -16.939 11.976 1.00 19.68 O ANISOU 1925 O GLY B 251 3349 2169 1958 32 -3 263 O ATOM 1926 N GLY A 252 -0.409 -16.661 12.985 1.00 15.56 N ANISOU 1926 N GLY B 252 2098 2055 1760 228 -100 85 N ATOM 1927 CA GLY A 252 0.105 -16.926 14.316 1.00 16.74 C ANISOU 1927 CA GLY B 252 2305 2321 1732 9 -97 109 C ATOM 1928 C GLY A 252 -0.974 -16.883 15.364 1.00 14.75 C ANISOU 1928 C GLY B 252 1777 2062 1765 215 -75 61 C ATOM 1929 O GLY A 252 -2.103 -16.552 15.020 1.00 16.46 O ANISOU 1929 O GLY B 252 2133 2147 1973 119 -369 -44 O ATOM 1930 N ALA A 253 -0.615 -17.214 16.591 1.00 14.09 N ANISOU 1930 N ALA B 253 1715 1910 1728 139 -128 110 N ATOM 1931 CA ALA A 253 -1.618 -17.224 17.658 1.00 13.77 C ANISOU 1931 CA ALA B 253 1630 1847 1754 67 -228 183 C ATOM 1932 C ALA A 253 -0.930 -17.037 19.001 1.00 14.12 C ANISOU 1932 C ALA B 253 1901 1732 1731 75 -187 165 C ATOM 1933 O ALA A 253 0.094 -17.632 19.300 1.00 15.23 O ANISOU 1933 O ALA B 253 2009 1748 2029 130 -481 174 O ATOM 1934 CB ALA A 253 -2.403 -18.515 17.720 1.00 14.61 C ANISOU 1934 CB ALA B 253 1664 2202 1683 184 67 -180 C ATOM 1935 N GLY A 254 -1.530 -16.234 19.865 1.00 13.82 N ANISOU 1935 N GLY B 254 1902 1670 1679 242 -240 -4 N ATOM 1936 CA GLY A 254 -1.110 -16.056 21.253 1.00 12.93 C ANISOU 1936 CA GLY B 254 1739 1542 1633 154 -99 -19 C ATOM 1937 C GLY A 254 -2.276 -16.570 22.120 1.00 12.65 C ANISOU 1937 C GLY B 254 1516 1471 1821 161 -156 9 C ATOM 1938 O GLY A 254 -3.344 -15.959 22.091 1.00 14.41 O ANISOU 1938 O GLY B 254 1938 1474 2061 131 -17 26 O ATOM 1939 N LEU A 255 -2.063 -17.665 22.830 1.00 14.02 N ANISOU 1939 N LEU B 255 1575 1686 2066 280 -46 17 N ATOM 1940 CA LEU A 255 -3.131 -18.401 23.472 1.00 13.74 C ANISOU 1940 CA LEU B 255 1431 2029 1760 254 -218 -38 C ATOM 1941 C LEU A 255 -2.858 -18.546 24.966 1.00 12.81 C ANISOU 1941 C LEU B 255 1482 1548 1836 85 -296 -84 C ATOM 1942 O LEU A 255 -1.835 -19.120 25.319 1.00 13.97 O ANISOU 1942 O LEU B 255 1753 1486 2068 136 -97 -37 O ATOM 1943 CB LEU A 255 -3.297 -19.780 22.823 1.00 15.08 C ANISOU 1943 CB LEU B 255 1633 2144 1954 144 -313 372 C ATOM 1944 CG LEU A 255 -3.496 -19.785 21.296 1.00 14.84 C ANISOU 1944 CG LEU B 255 1797 1857 1986 339 -498 203 C ATOM 1945 CD1 LEU A 255 -3.375 -21.192 20.733 1.00 17.15 C ANISOU 1945 CD1 LEU B 255 1665 2617 2233 757 -546 -74 C ATOM 1946 CD2 LEU A 255 -4.824 -19.135 20.895 1.00 16.56 C ANISOU 1946 CD2 LEU B 255 1718 1933 2641 84 -549 93 C ATOM 1947 N ASP A 256 -3.806 -18.035 25.738 1.00 13.29 N ANISOU 1947 N ASP B 256 1736 1498 1816 173 -165 -39 N ATOM 1948 CA ASP A 256 -3.765 -18.217 27.205 1.00 13.34 C ANISOU 1948 CA ASP B 256 1580 1611 1879 197 -183 -77 C ATOM 1949 C ASP A 256 -4.693 -19.351 27.675 1.00 13.18 C ANISOU 1949 C ASP B 256 1626 1671 1711 45 -229 55 C ATOM 1950 O ASP A 256 -4.641 -19.758 28.845 1.00 15.10 O ANISOU 1950 O ASP B 256 1604 2239 1893 196 -184 -220 O ATOM 1951 CB ASP A 256 -4.151 -16.956 27.944 1.00 14.41 C ANISOU 1951 CB ASP B 256 1683 1729 2065 2 -500 86 C ATOM 1952 CG ASP A 256 -3.871 -16.939 29.418 1.00 15.22 C ANISOU 1952 CG ASP B 256 1718 1980 2084 -213 -521 73 C ATOM 1953 OD1 ASP A 256 -2.731 -17.313 29.763 1.00 14.02 O ANISOU 1953 OD1 ASP B 256 1576 1930 1820 -88 -133 31 O ATOM 1954 OD2 ASP A 256 -4.760 -16.501 30.218 1.00 14.72 O ANISOU 1954 OD2 ASP B 256 1692 1938 1964 171 -11 52 O ATOM 1955 N VAL A 257 -5.567 -19.810 26.802 1.00 15.05 N ANISOU 1955 N VAL B 257 1578 2195 1947 -14 -264 -94 N ATOM 1956 CA VAL A 257 -6.640 -20.745 27.173 1.00 14.99 C ANISOU 1956 CA VAL B 257 1632 2151 1913 -28 -161 -231 C ATOM 1957 C VAL A 257 -6.815 -21.760 26.085 1.00 15.22 C ANISOU 1957 C VAL B 257 1398 2285 2098 39 -23 64 C ATOM 1958 O VAL A 257 -6.478 -21.522 24.926 1.00 15.87 O ANISOU 1958 O VAL B 257 1707 2315 2008 153 48 138 O ATOM 1959 CB VAL A 257 -7.963 -19.985 27.388 1.00 15.64 C ANISOU 1959 CB VAL B 257 1906 2201 1835 -157 -445 -72 C ATOM 1960 CG1 VAL A 257 -7.838 -19.085 28.614 1.00 18.19 C ANISOU 1960 CG1 VAL B 257 2130 2516 2265 -380 -839 107 C ATOM 1961 CG2 VAL A 257 -8.377 -19.205 26.134 1.00 17.13 C ANISOU 1961 CG2 VAL B 257 2329 1954 2225 11 -324 -215 C ATOM 1962 N PHE A 258 -7.222 -22.974 26.503 1.00 15.74 N ANISOU 1962 N PHE B 258 1592 2234 2154 197 95 152 N ATOM 1963 CA PHE A 258 -7.272 -24.143 25.617 1.00 15.92 C ANISOU 1963 CA PHE B 258 1545 2226 2280 316 112 208 C ATOM 1964 C PHE A 258 -8.523 -24.951 25.929 1.00 15.62 C ANISOU 1964 C PHE B 258 1607 2399 1928 212 -10 187 C ATOM 1965 O PHE A 258 -9.006 -24.944 27.047 1.00 17.82 O ANISOU 1965 O PHE B 258 1771 2985 2015 -84 87 194 O ATOM 1966 CB PHE A 258 -6.025 -25.044 25.757 1.00 16.06 C ANISOU 1966 CB PHE B 258 1800 2277 2026 278 -83 218 C ATOM 1967 CG PHE A 258 -4.769 -24.244 25.485 1.00 16.18 C ANISOU 1967 CG PHE B 258 1965 2194 1989 113 -49 -193 C ATOM 1968 CD1 PHE A 258 -4.267 -24.202 24.195 1.00 15.89 C ANISOU 1968 CD1 PHE B 258 1416 2411 2212 460 4 207 C ATOM 1969 CD2 PHE A 258 -4.138 -23.535 26.492 1.00 16.00 C ANISOU 1969 CD2 PHE B 258 2110 1983 1989 -20 -1 -367 C ATOM 1970 CE1 PHE A 258 -3.155 -23.403 23.918 1.00 16.04 C ANISOU 1970 CE1 PHE B 258 1440 2389 2267 325 -88 -77 C ATOM 1971 CE2 PHE A 258 -3.068 -22.721 26.222 1.00 17.01 C ANISOU 1971 CE2 PHE B 258 2065 2020 2379 3 -250 283 C ATOM 1972 CZ PHE A 258 -2.559 -22.681 24.906 1.00 15.79 C ANISOU 1972 CZ PHE B 258 1626 2148 2226 315 -180 93 C ATOM 1973 N GLU A 259 -9.030 -25.676 24.926 1.00 17.86 N ANISOU 1973 N GLU B 259 1834 2828 2125 170 -145 87 N ATOM 1974 CA GLU A 259 -10.366 -26.279 25.027 1.00 21.60 C ANISOU 1974 CA GLU B 259 1603 3454 3148 57 -378 184 C ATOM 1975 C GLU A 259 -10.464 -27.316 26.122 1.00 21.89 C ANISOU 1975 C GLU B 259 1308 3190 3820 231 -152 596 C ATOM 1976 O GLU A 259 -11.507 -27.439 26.753 1.00 24.55 O ANISOU 1976 O GLU B 259 2900 3626 2803 -513 -153 430 O ATOM 1977 CB GLU A 259 -10.766 -26.795 23.637 1.00 27.64 C ANISOU 1977 CB GLU B 259 2342 4767 3393 -698 -984 1016 C ATOM 1978 CG GLU A 259 -12.219 -27.052 23.400 1.00 40.45 C ANISOU 1978 CG GLU B 259 4636 6343 4391 -2440 -2533 1708 C ATOM 1979 CD GLU A 259 -12.785 -27.137 22.005 1.00 33.29 C ANISOU 1979 CD GLU B 259 2996 5512 4141 -1434 -985 744 C ATOM 1980 OE1 GLU A 259 -11.991 -27.413 21.066 1.00 25.03 O ANISOU 1980 OE1 GLU B 259 2406 3636 3466 -136 -67 -405 O ATOM 1981 OE2 GLU A 259 -14.009 -26.980 21.737 1.00 30.03 O ANISOU 1981 OE2 GLU B 259 4055 3803 3552 253 1730 -8 O ATOM 1982 N ARG A 260 -9.384 -28.054 26.337 1.00 21.08 N ANISOU 1982 N ARG B 260 1847 3277 2887 250 -333 467 N ATOM 1983 CA ARG A 260 -9.306 -29.109 27.331 1.00 23.40 C ANISOU 1983 CA ARG B 260 1616 3894 3381 243 -269 87 C ATOM 1984 C ARG A 260 -8.127 -28.837 28.263 1.00 21.94 C ANISOU 1984 C ARG B 260 1920 3255 3161 290 -225 307 C ATOM 1985 O ARG A 260 -7.376 -29.745 28.623 1.00 24.61 O ANISOU 1985 O ARG B 260 2508 3300 3541 546 -56 373 O ATOM 1986 CB ARG A 260 -9.104 -30.445 26.612 1.00 26.30 C ANISOU 1986 CB ARG B 260 1896 4221 3876 636 -499 -301 C ATOM 1987 CG ARG A 260 -10.159 -30.804 25.581 1.00 38.11 C ANISOU 1987 CG ARG B 260 2572 5993 5914 51 -2087 -335 C ATOM 1988 CD ARG A 260 -9.946 -32.118 24.861 1.00 47.10 C ANISOU 1988 CD ARG B 260 3770 6872 7255 1042 -3022 -732 C ATOM 1989 NE ARG A 260 -9.672 -33.244 25.719 1.00 57.84 N ANISOU 1989 NE ARG B 260 4541 8435 9001 2190 -1760 -387 N ATOM 1990 CZ ARG A 260 -9.762 -34.530 25.520 1.00 63.52 C ANISOU 1990 CZ ARG B 260 6244 8402 9487 3545 -2347 293 C ATOM 1991 NH1 ARG A 260 -10.181 -34.965 24.333 1.00 80.98 N ANISOU 1991 NH1 ARG B 260 7815 11952 11002 1673 -4409 1386 N ATOM 1992 NH2 ARG A 260 -9.440 -35.367 26.502 1.00 79.80 N ANISOU 1992 NH2 ARG B 260 7790 9876 12654 4238 92 -442 N ATOM 1993 N GLU A 261 -7.913 -27.604 28.678 1.00 21.78 N ANISOU 1993 N GLU B 261 1656 3288 3332 159 -128 187 N ATOM 1994 CA GLU A 261 -6.772 -27.282 29.524 1.00 21.77 C ANISOU 1994 CA GLU B 261 2156 3204 2910 245 -379 395 C ATOM 1995 C GLU A 261 -6.830 -28.106 30.804 1.00 24.05 C ANISOU 1995 C GLU B 261 2417 3723 2998 -437 42 398 C ATOM 1996 O GLU A 261 -7.916 -28.397 31.294 1.00 26.99 O ANISOU 1996 O GLU B 261 2443 4016 3796 -385 -102 1160 O ATOM 1997 CB GLU A 261 -6.739 -25.764 29.710 1.00 24.58 C ANISOU 1997 CB GLU B 261 2246 2877 4215 149 -946 -221 C ATOM 1998 CG GLU A 261 -7.956 -25.120 30.276 1.00 22.56 C ANISOU 1998 CG GLU B 261 2496 2837 3241 492 -685 -500 C ATOM 1999 CD GLU A 261 -7.793 -23.621 30.453 1.00 18.78 C ANISOU 1999 CD GLU B 261 2195 2624 2317 78 -448 -420 C ATOM 2000 OE1 GLU A 261 -7.715 -22.882 29.457 1.00 18.37 O ANISOU 2000 OE1 GLU B 261 2153 2811 2017 5 -460 -40 O ATOM 2001 OE2 GLU A 261 -7.753 -23.250 31.638 1.00 19.62 O ANISOU 2001 OE2 GLU B 261 1971 3325 2160 173 48 39 O ATOM 2002 N PRO A 262 -5.708 -28.523 31.390 1.00 22.93 N ANISOU 2002 N PRO B 262 1491 3629 3591 354 182 101 N ATOM 2003 CA PRO A 262 -4.376 -28.098 30.940 1.00 22.48 C ANISOU 2003 CA PRO B 262 2066 3099 3376 278 451 -168 C ATOM 2004 C PRO A 262 -3.758 -28.908 29.817 1.00 23.82 C ANISOU 2004 C PRO B 262 2420 3361 3269 717 606 -125 C ATOM 2005 O PRO A 262 -2.556 -28.777 29.610 1.00 22.92 O ANISOU 2005 O PRO B 262 2287 3349 3072 795 203 50 O ATOM 2006 CB PRO A 262 -3.511 -28.324 32.206 1.00 24.98 C ANISOU 2006 CB PRO B 262 2177 4175 3138 -180 859 -378 C ATOM 2007 CG PRO A 262 -4.139 -29.593 32.737 1.00 26.20 C ANISOU 2007 CG PRO B 262 2018 4745 3193 -244 635 -553 C ATOM 2008 CD PRO A 262 -5.640 -29.400 32.582 1.00 25.77 C ANISOU 2008 CD PRO B 262 1657 4742 3391 -176 188 -176 C ATOM 2009 N GLU A 263 -4.526 -29.716 29.095 1.00 23.52 N ANISOU 2009 N GLU B 263 2530 3293 3114 462 665 120 N ATOM 2010 CA GLU A 263 -4.015 -30.330 27.881 1.00 24.27 C ANISOU 2010 CA GLU B 263 2681 3108 3431 619 464 216 C ATOM 2011 C GLU A 263 -3.952 -29.252 26.791 1.00 22.60 C ANISOU 2011 C GLU B 263 2928 2821 2838 239 259 9 C ATOM 2012 O GLU A 263 -4.913 -28.499 26.641 1.00 24.65 O ANISOU 2012 O GLU B 263 3336 2793 3237 -74 458 -315 O ATOM 2013 CB GLU A 263 -4.889 -31.484 27.403 1.00 37.31 C ANISOU 2013 CB GLU B 263 2643 5816 5717 1111 -233 1153 C ATOM 2014 CG GLU A 263 -4.332 -32.848 27.789 1.00 55.59 C ANISOU 2014 CG GLU B 263 3442 7843 9836 2487 282 340 C ATOM 2015 CD GLU A 263 -5.454 -33.843 28.027 1.00 62.03 C ANISOU 2015 CD GLU B 263 3720 8436 11413 2087 1124 -1178 C ATOM 2016 OE1 GLU A 263 -6.502 -33.769 27.340 1.00 79.84 O ANISOU 2016 OE1 GLU B 263 6244 9943 14150 304 287 -2074 O ATOM 2017 OE2 GLU A 263 -5.256 -34.691 28.924 1.00 82.61 O ANISOU 2017 OE2 GLU B 263 6542 9725 15120 2317 4460 -1703 O ATOM 2018 N VAL A 264 -2.831 -29.168 26.102 1.00 22.23 N ANISOU 2018 N VAL B 264 2849 2711 2885 389 201 -2 N ATOM 2019 CA VAL A 264 -2.454 -28.327 25.002 1.00 19.29 C ANISOU 2019 CA VAL B 264 2447 2364 2517 323 -117 43 C ATOM 2020 C VAL A 264 -1.988 -29.269 23.874 1.00 20.34 C ANISOU 2020 C VAL B 264 2243 2696 2792 625 -391 32 C ATOM 2021 O VAL A 264 -1.117 -30.108 24.107 1.00 21.97 O ANISOU 2021 O VAL B 264 2353 2712 3284 792 149 215 O ATOM 2022 CB VAL A 264 -1.336 -27.344 25.346 1.00 18.70 C ANISOU 2022 CB VAL B 264 2568 2622 1913 433 -373 -33 C ATOM 2023 CG1 VAL A 264 -0.981 -26.596 24.064 1.00 20.05 C ANISOU 2023 CG1 VAL B 264 2855 2215 2547 64 267 429 C ATOM 2024 CG2 VAL A 264 -1.743 -26.423 26.478 1.00 20.14 C ANISOU 2024 CG2 VAL B 264 2563 2813 2274 866 43 290 C ATOM 2025 N PRO A 265 -2.570 -29.184 22.688 1.00 20.82 N ANISOU 2025 N PRO B 265 2231 3068 2612 315 -172 127 N ATOM 2026 CA PRO A 265 -2.115 -30.041 21.595 1.00 20.58 C ANISOU 2026 CA PRO B 265 2038 3279 2501 341 50 121 C ATOM 2027 C PRO A 265 -0.618 -29.880 21.370 1.00 20.05 C ANISOU 2027 C PRO B 265 1973 3025 2617 512 -226 152 C ATOM 2028 O PRO A 265 -0.095 -28.801 21.126 1.00 19.04 O ANISOU 2028 O PRO B 265 2075 2779 2382 485 53 286 O ATOM 2029 CB PRO A 265 -2.903 -29.510 20.394 1.00 23.73 C ANISOU 2029 CB PRO B 265 3205 3367 2445 -226 93 107 C ATOM 2030 CG PRO A 265 -4.151 -28.968 21.000 1.00 24.20 C ANISOU 2030 CG PRO B 265 3509 3271 2416 178 -323 157 C ATOM 2031 CD PRO A 265 -3.717 -28.339 22.299 1.00 22.95 C ANISOU 2031 CD PRO B 265 3030 2915 2775 -245 -446 -26 C ATOM 2032 N GLU A 266 0.066 -31.034 21.441 1.00 22.61 N ANISOU 2032 N GLU B 266 1995 3221 3376 714 -125 551 N ATOM 2033 CA GLU A 266 1.522 -31.049 21.395 1.00 21.39 C ANISOU 2033 CA GLU B 266 2124 3056 2949 762 -220 250 C ATOM 2034 C GLU A 266 2.084 -30.617 20.040 1.00 20.28 C ANISOU 2034 C GLU B 266 2490 2298 2917 850 -241 321 C ATOM 2035 O GLU A 266 3.239 -30.188 19.984 1.00 21.59 O ANISOU 2035 O GLU B 266 2358 3048 2799 609 -171 123 O ATOM 2036 CB GLU A 266 2.045 -32.443 21.838 1.00 27.71 C ANISOU 2036 CB GLU B 266 3390 3444 3694 1379 477 371 C ATOM 2037 CG GLU A 266 1.703 -32.735 23.293 1.00 31.28 C ANISOU 2037 CG GLU B 266 3769 4622 3495 1695 368 -16 C ATOM 2038 CD GLU A 266 2.516 -33.841 23.913 1.00 36.85 C ANISOU 2038 CD GLU B 266 6325 4147 3528 1330 336 -369 C ATOM 2039 OE1 GLU A 266 3.410 -34.388 23.225 1.00 45.36 O ANISOU 2039 OE1 GLU B 266 7297 4309 5630 1462 1054 450 O ATOM 2040 OE2 GLU A 266 2.271 -34.174 25.095 1.00 42.98 O ANISOU 2040 OE2 GLU B 266 7191 5446 3695 2247 743 -578 O ATOM 2041 N LYS A 267 1.282 -30.701 18.993 1.00 21.41 N ANISOU 2041 N LYS B 267 2535 2591 3008 620 -69 138 N ATOM 2042 CA LYS A 267 1.729 -30.241 17.684 1.00 20.87 C ANISOU 2042 CA LYS B 267 2261 2926 2741 597 -554 561 C ATOM 2043 C LYS A 267 2.062 -28.762 17.785 1.00 20.39 C ANISOU 2043 C LYS B 267 2202 2822 2724 577 -362 735 C ATOM 2044 O LYS A 267 2.975 -28.302 17.098 1.00 24.09 O ANISOU 2044 O LYS B 267 2609 3137 3409 758 177 1089 O ATOM 2045 CB LYS A 267 0.698 -30.539 16.587 1.00 21.96 C ANISOU 2045 CB LYS B 267 2246 3098 2998 471 -370 195 C ATOM 2046 CG LYS A 267 1.156 -30.133 15.201 1.00 24.82 C ANISOU 2046 CG LYS B 267 3064 3609 2759 817 -517 430 C ATOM 2047 CD LYS A 267 2.263 -30.989 14.613 1.00 25.29 C ANISOU 2047 CD LYS B 267 3085 3578 2946 782 -411 451 C ATOM 2048 CE LYS A 267 2.578 -30.613 13.177 1.00 28.47 C ANISOU 2048 CE LYS B 267 4299 3508 3009 665 -98 454 C ATOM 2049 NZ LYS A 267 3.646 -31.423 12.496 1.00 29.62 N ANISOU 2049 NZ LYS B 267 3547 4137 3571 817 -305 1086 N ATOM 2050 N LEU A 268 1.391 -28.025 18.676 1.00 17.72 N ANISOU 2050 N LEU B 268 1908 2732 2095 580 -201 316 N ATOM 2051 CA LEU A 268 1.664 -26.601 18.795 1.00 17.92 C ANISOU 2051 CA LEU B 268 2011 2507 2290 510 -538 239 C ATOM 2052 C LEU A 268 3.058 -26.333 19.341 1.00 16.71 C ANISOU 2052 C LEU B 268 1909 2225 2216 580 -234 186 C ATOM 2053 O LEU A 268 3.584 -25.254 19.087 1.00 18.42 O ANISOU 2053 O LEU B 268 1974 2324 2701 436 -4 209 O ATOM 2054 CB LEU A 268 0.616 -25.962 19.715 1.00 17.59 C ANISOU 2054 CB LEU B 268 1830 2297 2556 576 16 242 C ATOM 2055 CG LEU A 268 -0.805 -25.888 19.170 1.00 18.23 C ANISOU 2055 CG LEU B 268 2180 2549 2198 433 -131 155 C ATOM 2056 CD1 LEU A 268 -1.725 -25.416 20.271 1.00 22.39 C ANISOU 2056 CD1 LEU B 268 3424 2497 2585 -13 -582 352 C ATOM 2057 CD2 LEU A 268 -0.901 -25.017 17.924 1.00 19.98 C ANISOU 2057 CD2 LEU B 268 1837 2722 3032 399 301 -208 C ATOM 2058 N PHE A 269 3.635 -27.290 20.061 1.00 18.76 N ANISOU 2058 N PHE B 269 2428 2246 2454 610 78 224 N ATOM 2059 CA PHE A 269 4.909 -27.035 20.754 1.00 19.48 C ANISOU 2059 CA PHE B 269 2554 1852 2994 755 5 70 C ATOM 2060 C PHE A 269 6.031 -26.818 19.775 1.00 19.39 C ANISOU 2060 C PHE B 269 1979 2159 3230 818 -94 303 C ATOM 2061 O PHE A 269 7.020 -26.168 20.072 1.00 21.56 O ANISOU 2061 O PHE B 269 2196 2565 3432 622 -323 286 O ATOM 2062 CB PHE A 269 5.267 -28.197 21.682 1.00 18.46 C ANISOU 2062 CB PHE B 269 2214 2265 2536 916 -382 171 C ATOM 2063 CG PHE A 269 4.321 -28.437 22.843 1.00 20.12 C ANISOU 2063 CG PHE B 269 2473 2270 2901 357 -84 -7 C ATOM 2064 CD1 PHE A 269 3.303 -27.547 23.173 1.00 19.13 C ANISOU 2064 CD1 PHE B 269 2293 2216 2762 79 -151 -11 C ATOM 2065 CD2 PHE A 269 4.493 -29.583 23.587 1.00 21.73 C ANISOU 2065 CD2 PHE B 269 2220 2641 3394 480 125 146 C ATOM 2066 CE1 PHE A 269 2.464 -27.808 24.238 1.00 18.40 C ANISOU 2066 CE1 PHE B 269 1843 2531 2618 306 -266 120 C ATOM 2067 CE2 PHE A 269 3.647 -29.861 24.645 1.00 22.03 C ANISOU 2067 CE2 PHE B 269 2475 2771 3123 660 43 209 C ATOM 2068 CZ PHE A 269 2.639 -28.983 24.943 1.00 20.40 C ANISOU 2068 CZ PHE B 269 2073 2568 3112 298 -54 -15 C ATOM 2069 N GLY A 270 5.911 -27.369 18.563 1.00 20.64 N ANISOU 2069 N GLY B 270 1934 2693 3214 287 -37 429 N ATOM 2070 CA GLY A 270 6.922 -27.149 17.572 1.00 20.08 C ANISOU 2070 CA GLY B 270 2074 1946 3610 794 57 704 C ATOM 2071 C GLY A 270 6.813 -25.907 16.734 1.00 18.70 C ANISOU 2071 C GLY B 270 1808 1950 3346 429 -62 485 C ATOM 2072 O GLY A 270 7.659 -25.717 15.832 1.00 21.67 O ANISOU 2072 O GLY B 270 2622 2570 3043 346 9 613 O ATOM 2073 N LEU A 271 5.809 -25.067 16.962 1.00 18.85 N ANISOU 2073 N LEU B 271 2307 2126 2728 921 -368 401 N ATOM 2074 CA LEU A 271 5.578 -23.927 16.106 1.00 17.36 C ANISOU 2074 CA LEU B 271 2042 2041 2512 618 -145 591 C ATOM 2075 C LEU A 271 6.142 -22.638 16.681 1.00 16.38 C ANISOU 2075 C LEU B 271 2061 1816 2348 494 -110 584 C ATOM 2076 O LEU A 271 5.853 -22.237 17.807 1.00 17.07 O ANISOU 2076 O LEU B 271 2221 1920 2345 345 -204 515 O ATOM 2077 CB LEU A 271 4.077 -23.774 15.895 1.00 19.01 C ANISOU 2077 CB LEU B 271 2272 2450 2500 246 33 62 C ATOM 2078 CG LEU A 271 3.307 -24.962 15.347 1.00 18.80 C ANISOU 2078 CG LEU B 271 2539 2327 2278 267 -220 359 C ATOM 2079 CD1 LEU A 271 1.857 -24.581 15.101 1.00 22.51 C ANISOU 2079 CD1 LEU B 271 2567 2329 3659 138 -566 432 C ATOM 2080 CD2 LEU A 271 3.905 -25.474 14.072 1.00 23.21 C ANISOU 2080 CD2 LEU B 271 3452 2884 2484 253 -190 725 C ATOM 2081 N GLU A 272 6.953 -21.959 15.889 1.00 18.17 N ANISOU 2081 N GLU B 272 2151 2724 2030 62 -56 -66 N ATOM 2082 CA GLU A 272 7.562 -20.697 16.276 1.00 17.36 C ANISOU 2082 CA GLU B 272 2156 2137 2303 -154 -274 -50 C ATOM 2083 C GLU A 272 6.599 -19.506 16.203 1.00 19.11 C ANISOU 2083 C GLU B 272 2427 2316 2518 77 -153 -43 C ATOM 2084 O GLU A 272 6.973 -18.449 16.764 1.00 18.80 O ANISOU 2084 O GLU B 272 2062 2384 2699 -7 103 -50 O ATOM 2085 CB GLU A 272 8.780 -20.414 15.403 1.00 20.81 C ANISOU 2085 CB GLU B 272 2335 2715 2856 -168 -193 488 C ATOM 2086 CG GLU A 272 8.503 -20.200 13.910 1.00 21.69 C ANISOU 2086 CG GLU B 272 2831 2672 2740 589 83 792 C ATOM 2087 CD GLU A 272 8.342 -18.744 13.532 1.00 22.26 C ANISOU 2087 CD GLU B 272 2775 2476 3207 642 -668 208 C ATOM 2088 OE1 GLU A 272 9.077 -17.886 14.083 1.00 22.63 O ANISOU 2088 OE1 GLU B 272 2552 3091 2956 39 -350 897 O ATOM 2089 OE2 GLU A 272 7.423 -18.489 12.717 1.00 24.56 O ANISOU 2089 OE2 GLU B 272 3327 2693 3312 -51 76 12 O ATOM 2090 N ASN A 273 5.468 -19.688 15.525 1.00 16.93 N ANISOU 2090 N ASN B 273 2477 1838 2117 78 -101 334 N ATOM 2091 CA ASN A 273 4.515 -18.581 15.393 1.00 16.58 C ANISOU 2091 CA ASN B 273 2741 1986 1573 305 -160 475 C ATOM 2092 C ASN A 273 3.359 -18.627 16.386 1.00 15.05 C ANISOU 2092 C ASN B 273 2182 1846 1691 251 -124 318 C ATOM 2093 O ASN A 273 2.321 -17.983 16.186 1.00 16.26 O ANISOU 2093 O ASN B 273 2398 1884 1894 188 -18 243 O ATOM 2094 CB ASN A 273 4.063 -18.529 13.926 1.00 17.83 C ANISOU 2094 CB ASN B 273 2842 2289 1646 245 -187 330 C ATOM 2095 CG ASN A 273 3.334 -19.797 13.536 1.00 18.54 C ANISOU 2095 CG ASN B 273 2956 1953 2136 173 -423 -55 C ATOM 2096 OD1 ASN A 273 3.596 -20.872 14.066 1.00 24.06 O ANISOU 2096 OD1 ASN B 273 3254 2869 3018 994 -771 -403 O ATOM 2097 ND2 ASN A 273 2.416 -19.661 12.592 1.00 23.04 N ANISOU 2097 ND2 ASN B 273 4104 2302 2348 -286 -680 -211 N ATOM 2098 N VAL A 274 3.542 -19.377 17.496 1.00 15.17 N ANISOU 2098 N VAL B 274 2077 1986 1700 -60 -220 110 N ATOM 2099 CA VAL A 274 2.583 -19.365 18.597 1.00 13.12 C ANISOU 2099 CA VAL B 274 1432 1974 1577 243 -253 -21 C ATOM 2100 C VAL A 274 3.301 -18.985 19.886 1.00 12.45 C ANISOU 2100 C VAL B 274 1571 1515 1646 432 -320 -175 C ATOM 2101 O VAL A 274 4.519 -19.246 20.044 1.00 14.77 O ANISOU 2101 O VAL B 274 2119 1539 1953 184 0 -184 O ATOM 2102 CB VAL A 274 1.834 -20.700 18.730 1.00 13.95 C ANISOU 2102 CB VAL B 274 1481 1885 1935 345 -383 130 C ATOM 2103 CG1 VAL A 274 1.144 -21.053 17.394 1.00 16.73 C ANISOU 2103 CG1 VAL B 274 1842 2190 2325 -114 -820 186 C ATOM 2104 CG2 VAL A 274 2.732 -21.827 19.176 1.00 15.64 C ANISOU 2104 CG2 VAL B 274 1759 1945 2240 560 -128 215 C ATOM 2105 N VAL A 275 2.537 -18.447 20.822 1.00 14.11 N ANISOU 2105 N VAL B 275 1781 1674 1905 310 -566 31 N ATOM 2106 CA VAL A 275 2.928 -18.248 22.201 1.00 12.80 C ANISOU 2106 CA VAL B 275 1424 1664 1774 262 -243 151 C ATOM 2107 C VAL A 275 1.822 -18.902 23.029 1.00 13.87 C ANISOU 2107 C VAL B 275 1294 1818 2157 153 -180 -50 C ATOM 2108 O VAL A 275 0.650 -18.617 22.784 1.00 15.19 O ANISOU 2108 O VAL B 275 1804 1808 2160 58 93 98 O ATOM 2109 CB VAL A 275 3.163 -16.753 22.561 1.00 12.44 C ANISOU 2109 CB VAL B 275 1341 1766 1617 152 -138 441 C ATOM 2110 CG1 VAL A 275 3.437 -16.599 24.049 1.00 14.56 C ANISOU 2110 CG1 VAL B 275 1915 2015 1603 125 -271 413 C ATOM 2111 CG2 VAL A 275 4.274 -16.228 21.715 1.00 14.00 C ANISOU 2111 CG2 VAL B 275 1616 1720 1982 251 265 390 C ATOM 2112 N LEU A 276 2.202 -19.786 23.931 1.00 14.49 N ANISOU 2112 N LEU B 276 1570 1888 2047 295 -46 104 N ATOM 2113 CA LEU A 276 1.304 -20.628 24.689 1.00 13.63 C ANISOU 2113 CA LEU B 276 1450 1792 1936 210 -200 38 C ATOM 2114 C LEU A 276 1.475 -20.374 26.184 1.00 14.05 C ANISOU 2114 C LEU B 276 1891 1564 1882 128 -167 31 C ATOM 2115 O LEU A 276 2.606 -20.604 26.664 1.00 15.85 O ANISOU 2115 O LEU B 276 2510 1575 1938 55 -206 79 O ATOM 2116 CB LEU A 276 1.628 -22.082 24.378 1.00 14.95 C ANISOU 2116 CB LEU B 276 1703 1972 2006 503 -99 8 C ATOM 2117 CG LEU A 276 1.734 -22.436 22.900 1.00 14.91 C ANISOU 2117 CG LEU B 276 1701 1974 1991 500 -12 131 C ATOM 2118 CD1 LEU A 276 2.257 -23.858 22.737 1.00 17.84 C ANISOU 2118 CD1 LEU B 276 2071 1973 2734 558 -152 436 C ATOM 2119 CD2 LEU A 276 0.393 -22.270 22.190 1.00 17.24 C ANISOU 2119 CD2 LEU B 276 2100 2262 2187 454 -301 -103 C ATOM 2120 N LEU A 277 0.444 -19.963 26.872 1.00 13.13 N ANISOU 2120 N LEU B 277 1713 1425 1851 279 -220 -91 N ATOM 2121 CA LEU A 277 0.522 -19.667 28.302 1.00 13.18 C ANISOU 2121 CA LEU B 277 1476 1670 1864 204 -236 12 C ATOM 2122 C LEU A 277 -0.475 -20.499 29.107 1.00 13.57 C ANISOU 2122 C LEU B 277 1402 1709 2044 295 -132 -4 C ATOM 2123 O LEU A 277 -1.558 -20.788 28.581 1.00 14.57 O ANISOU 2123 O LEU B 277 1415 2108 2013 137 -167 -29 O ATOM 2124 CB LEU A 277 0.270 -18.184 28.591 1.00 13.26 C ANISOU 2124 CB LEU B 277 1529 1800 1710 447 -25 -182 C ATOM 2125 CG LEU A 277 1.103 -17.223 27.742 1.00 14.44 C ANISOU 2125 CG LEU B 277 1717 1902 1867 381 121 31 C ATOM 2126 CD1 LEU A 277 0.781 -15.771 28.109 1.00 16.40 C ANISOU 2126 CD1 LEU B 277 1591 2521 2118 608 22 157 C ATOM 2127 CD2 LEU A 277 2.580 -17.442 27.892 1.00 16.82 C ANISOU 2127 CD2 LEU B 277 1956 2143 2290 61 296 -342 C ATOM 2128 N PRO A 278 -0.127 -20.872 30.344 1.00 14.16 N ANISOU 2128 N PRO B 278 1140 2205 2034 74 -159 -58 N ATOM 2129 CA PRO A 278 -1.035 -21.753 31.118 1.00 14.23 C ANISOU 2129 CA PRO B 278 1401 1685 2319 81 75 21 C ATOM 2130 C PRO A 278 -2.143 -21.031 31.871 1.00 13.63 C ANISOU 2130 C PRO B 278 1369 1853 1956 524 100 -55 C ATOM 2131 O PRO A 278 -2.272 -21.097 33.107 1.00 15.90 O ANISOU 2131 O PRO B 278 2042 2092 1908 384 5 -145 O ATOM 2132 CB PRO A 278 -0.025 -22.456 32.016 1.00 15.54 C ANISOU 2132 CB PRO B 278 1581 1823 2502 185 222 -37 C ATOM 2133 CG PRO A 278 1.011 -21.382 32.258 1.00 14.36 C ANISOU 2133 CG PRO B 278 1661 1623 2174 66 193 -32 C ATOM 2134 CD PRO A 278 1.131 -20.584 31.009 1.00 13.21 C ANISOU 2134 CD PRO B 278 1344 2007 1668 57 -188 218 C ATOM 2135 N HIS A 279 -2.975 -20.276 31.126 1.00 14.00 N ANISOU 2135 N HIS B 279 1446 1691 2185 436 358 -70 N ATOM 2136 CA HIS A 279 -4.124 -19.580 31.680 1.00 13.48 C ANISOU 2136 CA HIS B 279 1712 1719 1692 41 -27 -120 C ATOM 2137 C HIS A 279 -3.763 -18.690 32.848 1.00 12.81 C ANISOU 2137 C HIS B 279 1693 1667 1507 -32 90 -323 C ATOM 2138 O HIS A 279 -4.194 -18.840 33.991 1.00 15.52 O ANISOU 2138 O HIS B 279 1796 2443 1659 98 151 67 O ATOM 2139 CB HIS A 279 -5.255 -20.552 32.050 1.00 15.05 C ANISOU 2139 CB HIS B 279 1787 2120 1810 -121 -199 88 C ATOM 2140 CG HIS A 279 -6.582 -19.856 32.053 1.00 14.62 C ANISOU 2140 CG HIS B 279 1570 2152 1835 -90 -3 281 C ATOM 2141 ND1 HIS A 279 -7.762 -20.568 32.042 1.00 18.51 N ANISOU 2141 ND1 HIS B 279 1776 2305 2951 -303 134 -218 N ATOM 2142 CD2 HIS A 279 -6.956 -18.576 32.055 1.00 16.41 C ANISOU 2142 CD2 HIS B 279 1876 2121 2239 -50 -206 236 C ATOM 2143 CE1 HIS A 279 -8.787 -19.748 32.039 1.00 18.71 C ANISOU 2143 CE1 HIS B 279 2149 2277 2681 -346 -5 211 C ATOM 2144 NE2 HIS A 279 -8.327 -18.506 32.051 1.00 18.65 N ANISOU 2144 NE2 HIS B 279 2139 2112 2834 -249 80 277 N ATOM 2145 N VAL A 280 -2.925 -17.704 32.473 1.00 13.87 N ANISOU 2145 N VAL B 280 1654 2058 1558 166 -4 272 N ATOM 2146 CA VAL A 280 -2.337 -16.816 33.468 1.00 13.99 C ANISOU 2146 CA VAL B 280 1652 1997 1665 300 -74 -237 C ATOM 2147 C VAL A 280 -2.921 -15.415 33.379 1.00 13.52 C ANISOU 2147 C VAL B 280 1664 1890 1582 181 -30 44 C ATOM 2148 O VAL A 280 -2.397 -14.526 34.062 1.00 14.41 O ANISOU 2148 O VAL B 280 1768 1762 1946 259 -140 99 O ATOM 2149 CB VAL A 280 -0.812 -16.760 33.369 1.00 14.03 C ANISOU 2149 CB VAL B 280 1807 1900 1626 340 -120 -73 C ATOM 2150 CG1 VAL A 280 -0.176 -18.121 33.534 1.00 15.94 C ANISOU 2150 CG1 VAL B 280 1439 1963 2653 183 152 -202 C ATOM 2151 CG2 VAL A 280 -0.344 -16.145 32.041 1.00 14.48 C ANISOU 2151 CG2 VAL B 280 1933 1951 1617 317 -105 -111 C ATOM 2152 N GLY A 281 -3.980 -15.181 32.629 1.00 14.60 N ANISOU 2152 N GLY B 281 1801 1778 1969 151 96 -81 N ATOM 2153 CA GLY A 281 -4.591 -13.868 32.484 1.00 14.40 C ANISOU 2153 CA GLY B 281 1591 2087 1794 376 -110 5 C ATOM 2154 C GLY A 281 -4.746 -13.071 33.758 1.00 14.13 C ANISOU 2154 C GLY B 281 1469 2289 1609 126 -49 -42 C ATOM 2155 O GLY A 281 -4.396 -11.898 33.796 1.00 15.73 O ANISOU 2155 O GLY B 281 1522 2422 2033 299 38 620 O ATOM 2156 N SER A 282 -5.271 -13.694 34.825 1.00 14.23 N ANISOU 2156 N SER B 282 1753 1744 1910 176 206 138 N ATOM 2157 CA SER A 282 -5.435 -12.996 36.117 1.00 13.67 C ANISOU 2157 CA SER B 282 1758 1598 1838 47 266 134 C ATOM 2158 C SER A 282 -4.404 -13.361 37.150 1.00 12.67 C ANISOU 2158 C SER B 282 1428 1627 1758 130 314 199 C ATOM 2159 O SER A 282 -4.535 -12.965 38.311 1.00 14.97 O ANISOU 2159 O SER B 282 1930 2100 1660 -44 270 305 O ATOM 2160 CB SER A 282 -6.823 -13.264 36.681 1.00 14.09 C ANISOU 2160 CB SER B 282 1363 2046 1945 -171 -45 230 C ATOM 2161 OG SER A 282 -7.077 -14.628 36.875 1.00 15.77 O ANISOU 2161 OG SER B 282 1556 2290 2148 113 63 362 O ATOM 2162 N GLY A 283 -3.403 -14.122 36.715 1.00 13.06 N ANISOU 2162 N GLY B 283 1416 1586 1960 250 -64 72 N ATOM 2163 CA GLY A 283 -2.488 -14.791 37.599 1.00 14.18 C ANISOU 2163 CA GLY B 283 1490 1742 2157 78 160 -133 C ATOM 2164 C GLY A 283 -1.326 -13.999 38.141 1.00 14.06 C ANISOU 2164 C GLY B 283 1346 1636 2360 270 214 -336 C ATOM 2165 O GLY A 283 -0.172 -14.422 38.051 1.00 14.99 O ANISOU 2165 O GLY B 283 1750 1736 2208 7 -107 -144 O ATOM 2166 N THR A 284 -1.605 -12.844 38.737 1.00 13.56 N ANISOU 2166 N THR B 284 1571 1618 1963 49 113 -205 N ATOM 2167 CA THR A 284 -0.617 -12.036 39.412 1.00 13.86 C ANISOU 2167 CA THR B 284 1660 1795 1811 90 24 -99 C ATOM 2168 C THR A 284 -0.894 -12.080 40.920 1.00 13.19 C ANISOU 2168 C THR B 284 1778 1360 1874 48 80 -101 C ATOM 2169 O THR A 284 -2.012 -12.322 41.358 1.00 15.07 O ANISOU 2169 O THR B 284 1815 1755 2155 -133 -49 227 O ATOM 2170 CB THR A 284 -0.566 -10.586 38.936 1.00 13.88 C ANISOU 2170 CB THR B 284 1618 1807 1851 -13 72 -33 C ATOM 2171 OG1 THR A 284 -1.782 -9.909 39.251 1.00 14.76 O ANISOU 2171 OG1 THR B 284 1738 1859 2009 166 368 160 O ATOM 2172 CG2 THR A 284 -0.320 -10.522 37.437 1.00 14.60 C ANISOU 2172 CG2 THR B 284 1409 2259 1880 173 65 254 C ATOM 2173 N VAL A 285 0.187 -11.849 41.668 1.00 15.18 N ANISOU 2173 N VAL B 285 1854 2107 1809 -261 -36 -152 N ATOM 2174 CA VAL A 285 0.058 -11.794 43.125 1.00 15.80 C ANISOU 2174 CA VAL B 285 1965 2213 1827 263 -125 -34 C ATOM 2175 C VAL A 285 -1.016 -10.790 43.494 1.00 16.67 C ANISOU 2175 C VAL B 285 2443 2042 1848 240 -29 -236 C ATOM 2176 O VAL A 285 -1.873 -11.054 44.347 1.00 18.03 O ANISOU 2176 O VAL B 285 2476 2316 2059 148 -79 72 O ATOM 2177 CB VAL A 285 1.412 -11.457 43.783 1.00 17.73 C ANISOU 2177 CB VAL B 285 2975 1961 1802 333 -803 -2 C ATOM 2178 CG1 VAL A 285 1.204 -11.184 45.258 1.00 26.89 C ANISOU 2178 CG1 VAL B 285 5271 3275 1673 282 -839 -139 C ATOM 2179 CG2 VAL A 285 2.391 -12.583 43.559 1.00 20.20 C ANISOU 2179 CG2 VAL B 285 3208 2063 2405 605 -65 -303 C ATOM 2180 N GLU A 286 -0.974 -9.599 42.879 1.00 16.62 N ANISOU 2180 N GLU B 286 2038 2142 2134 225 -192 -52 N ATOM 2181 CA GLU A 286 -1.861 -8.536 43.293 1.00 17.79 C ANISOU 2181 CA GLU B 286 2843 1798 2119 266 -173 -469 C ATOM 2182 C GLU A 286 -3.325 -8.842 43.021 1.00 17.02 C ANISOU 2182 C GLU B 286 2356 2086 2023 269 -375 59 C ATOM 2183 O GLU A 286 -4.200 -8.687 43.869 1.00 17.57 O ANISOU 2183 O GLU B 286 2145 2711 1820 137 -55 161 O ATOM 2184 CB GLU A 286 -1.478 -7.217 42.590 1.00 21.11 C ANISOU 2184 CB GLU B 286 2139 2307 3575 370 -434 -443 C ATOM 2185 CG GLU A 286 -0.067 -6.759 42.817 1.00 25.09 C ANISOU 2185 CG GLU B 286 2761 3165 3605 -311 -1195 140 C ATOM 2186 CD GLU A 286 1.067 -7.236 41.934 1.00 22.85 C ANISOU 2186 CD GLU B 286 2399 3928 2355 -718 -273 27 C ATOM 2187 OE1 GLU A 286 1.117 -8.243 41.227 1.00 18.53 O ANISOU 2187 OE1 GLU B 286 2087 3329 1623 -542 362 31 O ATOM 2188 OE2 GLU A 286 2.070 -6.484 41.989 1.00 26.83 O ANISOU 2188 OE2 GLU B 286 2055 4834 3304 -611 204 -218 O ATOM 2189 N THR A 287 -3.649 -9.268 41.811 1.00 14.34 N ANISOU 2189 N THR B 287 1700 1888 1859 175 65 105 N ATOM 2190 CA THR A 287 -5.034 -9.525 41.416 1.00 14.62 C ANISOU 2190 CA THR B 287 1735 1854 1964 193 117 10 C ATOM 2191 C THR A 287 -5.585 -10.752 42.088 1.00 15.99 C ANISOU 2191 C THR B 287 2085 1821 2172 -77 558 -298 C ATOM 2192 O THR A 287 -6.730 -10.740 42.513 1.00 16.36 O ANISOU 2192 O THR B 287 1849 1920 2446 -14 249 40 O ATOM 2193 CB THR A 287 -5.146 -9.644 39.879 1.00 13.72 C ANISOU 2193 CB THR B 287 1669 1676 1869 206 154 86 C ATOM 2194 OG1 THR A 287 -4.879 -8.329 39.325 1.00 16.25 O ANISOU 2194 OG1 THR B 287 1923 2003 2250 291 317 -320 O ATOM 2195 CG2 THR A 287 -6.527 -10.088 39.415 1.00 17.00 C ANISOU 2195 CG2 THR B 287 1982 1914 2565 121 -270 -66 C ATOM 2196 N ARG A 288 -4.809 -11.825 42.205 1.00 14.80 N ANISOU 2196 N ARG B 288 1932 1900 1793 92 373 1 N ATOM 2197 CA ARG A 288 -5.370 -12.985 42.897 1.00 14.79 C ANISOU 2197 CA ARG B 288 1622 2154 1844 38 141 -82 C ATOM 2198 C ARG A 288 -5.651 -12.737 44.376 1.00 14.93 C ANISOU 2198 C ARG B 288 1814 2178 1682 -215 257 -338 C ATOM 2199 O ARG A 288 -6.609 -13.284 44.922 1.00 15.93 O ANISOU 2199 O ARG B 288 1631 2303 2120 75 196 216 O ATOM 2200 CB ARG A 288 -4.427 -14.163 42.741 1.00 16.28 C ANISOU 2200 CB ARG B 288 1879 2215 2092 208 48 -346 C ATOM 2201 CG ARG A 288 -4.360 -14.680 41.302 1.00 16.22 C ANISOU 2201 CG ARG B 288 1665 2301 2197 150 196 40 C ATOM 2202 CD ARG A 288 -5.710 -15.326 40.970 1.00 17.32 C ANISOU 2202 CD ARG B 288 1893 2036 2653 273 -588 519 C ATOM 2203 NE ARG A 288 -5.560 -15.884 39.680 1.00 17.16 N ANISOU 2203 NE ARG B 288 1592 2241 2688 -1 -168 789 N ATOM 2204 CZ ARG A 288 -5.092 -16.921 39.055 1.00 15.06 C ANISOU 2204 CZ ARG B 288 2247 1943 1533 39 200 599 C ATOM 2205 NH1 ARG A 288 -4.523 -17.761 39.917 1.00 18.71 N ANISOU 2205 NH1 ARG B 288 1840 2999 2269 418 86 -227 N ATOM 2206 NH2 ARG A 288 -5.093 -17.231 37.764 1.00 17.56 N ANISOU 2206 NH2 ARG B 288 2192 2762 1718 -145 -6 434 N ATOM 2207 N LYS A 289 -4.811 -11.902 45.000 1.00 15.37 N ANISOU 2207 N LYS B 289 1816 2093 1931 -124 0 184 N ATOM 2208 CA LYS A 289 -5.157 -11.549 46.382 1.00 15.78 C ANISOU 2208 CA LYS B 289 1837 2146 2011 -30 58 212 C ATOM 2209 C LYS A 289 -6.501 -10.810 46.477 1.00 15.87 C ANISOU 2209 C LYS B 289 1737 2176 2115 58 88 309 C ATOM 2210 O LYS A 289 -7.342 -11.107 47.350 1.00 15.92 O ANISOU 2210 O LYS B 289 1784 2198 2069 -93 114 136 O ATOM 2211 CB LYS A 289 -4.066 -10.698 47.024 1.00 18.24 C ANISOU 2211 CB LYS B 289 2256 2503 2173 -113 -310 -19 C ATOM 2212 CG LYS A 289 -4.351 -10.356 48.464 1.00 23.55 C ANISOU 2212 CG LYS B 289 3690 2659 2600 -646 -963 599 C ATOM 2213 CD LYS A 289 -3.291 -9.568 49.157 1.00 26.71 C ANISOU 2213 CD LYS B 289 3892 3128 3129 -258 -1581 309 C ATOM 2214 CE LYS A 289 -3.381 -9.693 50.682 1.00 34.20 C ANISOU 2214 CE LYS B 289 5739 4199 3056 -996 -1887 654 C ATOM 2215 NZ LYS A 289 -4.658 -9.351 51.295 1.00 29.92 N ANISOU 2215 NZ LYS B 289 3419 4468 3482 -1074 -1199 621 N ATOM 2216 N VAL A 290 -6.701 -9.840 45.579 1.00 16.07 N ANISOU 2216 N VAL B 290 1922 2085 2098 -28 209 258 N ATOM 2217 CA VAL A 290 -7.965 -9.090 45.564 1.00 15.74 C ANISOU 2217 CA VAL B 290 1561 2105 2314 154 139 544 C ATOM 2218 C VAL A 290 -9.142 -10.012 45.322 1.00 15.00 C ANISOU 2218 C VAL B 290 1680 1949 2069 129 86 299 C ATOM 2219 O VAL A 290 -10.192 -9.953 45.968 1.00 16.90 O ANISOU 2219 O VAL B 290 1822 2057 2541 -4 81 463 O ATOM 2220 CB VAL A 290 -7.927 -7.948 44.535 1.00 15.40 C ANISOU 2220 CB VAL B 290 1563 1943 2345 269 48 592 C ATOM 2221 CG1 VAL A 290 -9.272 -7.296 44.310 1.00 20.00 C ANISOU 2221 CG1 VAL B 290 2732 2051 2817 139 126 235 C ATOM 2222 CG2 VAL A 290 -6.952 -6.883 45.015 1.00 20.10 C ANISOU 2222 CG2 VAL B 290 1423 2845 3371 92 44 495 C ATOM 2223 N MET A 291 -8.971 -10.912 44.347 1.00 15.51 N ANISOU 2223 N MET B 291 1606 1993 2295 207 0 249 N ATOM 2224 CA MET A 291 -10.041 -11.869 44.049 1.00 14.40 C ANISOU 2224 CA MET B 291 1552 1862 2058 -1 242 316 C ATOM 2225 C MET A 291 -10.369 -12.752 45.256 1.00 15.54 C ANISOU 2225 C MET B 291 1839 2279 1785 -220 125 91 C ATOM 2226 O MET A 291 -11.524 -13.032 45.585 1.00 15.40 O ANISOU 2226 O MET B 291 1513 2222 2115 39 276 359 O ATOM 2227 CB MET A 291 -9.609 -12.760 42.881 1.00 14.40 C ANISOU 2227 CB MET B 291 1508 1971 1991 -57 213 327 C ATOM 2228 CG MET A 291 -9.555 -12.062 41.536 1.00 14.68 C ANISOU 2228 CG MET B 291 1665 1961 1953 -16 98 101 C ATOM 2229 SD MET A 291 -8.812 -13.051 40.228 1.00 15.99 S ANISOU 2229 SD MET B 291 1822 2251 2002 146 209 243 S ATOM 2230 CE MET A 291 -9.942 -14.450 40.136 1.00 15.82 C ANISOU 2230 CE MET B 291 1783 2090 2138 343 111 88 C ATOM 2231 N ALA A 292 -9.314 -13.228 45.945 1.00 15.80 N ANISOU 2231 N ALA B 292 1936 2289 1777 -77 60 145 N ATOM 2232 CA ALA A 292 -9.524 -14.126 47.063 1.00 15.24 C ANISOU 2232 CA ALA B 292 1860 1987 1943 187 106 229 C ATOM 2233 C ALA A 292 -10.261 -13.383 48.172 1.00 15.14 C ANISOU 2233 C ALA B 292 1885 1872 1995 350 299 242 C ATOM 2234 O ALA A 292 -11.181 -13.903 48.819 1.00 16.69 O ANISOU 2234 O ALA B 292 1869 2367 2105 34 43 396 O ATOM 2235 CB ALA A 292 -8.171 -14.655 47.549 1.00 16.12 C ANISOU 2235 CB ALA B 292 1968 1977 2180 -169 327 246 C ATOM 2236 N ASP A 293 -9.801 -12.161 48.437 1.00 15.95 N ANISOU 2236 N ASP B 293 1881 2084 2097 147 160 463 N ATOM 2237 CA ASP A 293 -10.423 -11.365 49.518 1.00 16.50 C ANISOU 2237 CA ASP B 293 1775 2288 2206 16 76 555 C ATOM 2238 C ASP A 293 -11.887 -11.085 49.207 1.00 16.89 C ANISOU 2238 C ASP B 293 2006 2016 2396 367 -356 491 C ATOM 2239 O ASP A 293 -12.743 -11.007 50.117 1.00 18.83 O ANISOU 2239 O ASP B 293 2726 2027 2400 89 -337 505 O ATOM 2240 CB ASP A 293 -9.601 -10.101 49.770 1.00 17.43 C ANISOU 2240 CB ASP B 293 1864 2904 1855 67 -28 218 C ATOM 2241 CG ASP A 293 -8.281 -10.372 50.491 1.00 19.94 C ANISOU 2241 CG ASP B 293 2099 3146 2331 -237 16 16 C ATOM 2242 OD1 ASP A 293 -8.151 -11.432 51.122 1.00 20.65 O ANISOU 2242 OD1 ASP B 293 2331 3029 2486 16 -249 -200 O ATOM 2243 OD2 ASP A 293 -7.383 -9.500 50.389 1.00 21.50 O ANISOU 2243 OD2 ASP B 293 2015 3458 2696 -292 -378 453 O ATOM 2244 N LEU A 294 -12.199 -10.932 47.916 1.00 17.28 N ANISOU 2244 N LEU B 294 2128 1997 2439 194 61 556 N ATOM 2245 CA LEU A 294 -13.578 -10.688 47.466 1.00 16.97 C ANISOU 2245 CA LEU B 294 2048 2269 2131 210 -290 425 C ATOM 2246 C LEU A 294 -14.429 -11.948 47.643 1.00 16.23 C ANISOU 2246 C LEU B 294 2104 2190 1872 143 -120 778 C ATOM 2247 O LEU A 294 -15.600 -11.883 48.054 1.00 17.36 O ANISOU 2247 O LEU B 294 2559 2100 1936 40 17 509 O ATOM 2248 CB LEU A 294 -13.541 -10.228 46.021 1.00 19.43 C ANISOU 2248 CB LEU B 294 2625 2340 2417 244 357 445 C ATOM 2249 CG LEU A 294 -14.800 -9.706 45.356 1.00 22.03 C ANISOU 2249 CG LEU B 294 3664 2411 2296 710 117 351 C ATOM 2250 CD1 LEU A 294 -15.444 -8.616 46.216 1.00 27.78 C ANISOU 2250 CD1 LEU B 294 4300 2654 3599 1353 171 723 C ATOM 2251 CD2 LEU A 294 -14.547 -9.179 43.944 1.00 24.00 C ANISOU 2251 CD2 LEU B 294 3270 2888 2962 828 884 113 C ATOM 2252 N VAL A 295 -13.891 -13.135 47.358 1.00 16.52 N ANISOU 2252 N VAL B 295 1801 1842 2632 -100 -306 287 N ATOM 2253 CA VAL A 295 -14.601 -14.363 47.637 1.00 15.71 C ANISOU 2253 CA VAL B 295 1993 1874 2103 7 88 209 C ATOM 2254 C VAL A 295 -14.921 -14.453 49.123 1.00 19.01 C ANISOU 2254 C VAL B 295 3380 1690 2152 -449 142 267 C ATOM 2255 O VAL A 295 -16.040 -14.678 49.591 1.00 17.56 O ANISOU 2255 O VAL B 295 2328 2049 2295 -142 -259 784 O ATOM 2256 CB VAL A 295 -13.816 -15.601 47.136 1.00 15.24 C ANISOU 2256 CB VAL B 295 1885 1978 1929 85 -46 13 C ATOM 2257 CG1 VAL A 295 -14.413 -16.857 47.719 1.00 16.83 C ANISOU 2257 CG1 VAL B 295 1864 1996 2536 12 77 -307 C ATOM 2258 CG2 VAL A 295 -13.808 -15.645 45.607 1.00 17.39 C ANISOU 2258 CG2 VAL B 295 2186 2511 1909 755 -309 -211 C ATOM 2259 N VAL A 296 -13.911 -14.254 49.957 1.00 16.85 N ANISOU 2259 N VAL B 296 2228 2091 2084 -35 53 249 N ATOM 2260 CA VAL A 296 -14.103 -14.325 51.408 1.00 17.71 C ANISOU 2260 CA VAL B 296 2466 2145 2117 61 238 150 C ATOM 2261 C VAL A 296 -15.102 -13.277 51.824 1.00 18.69 C ANISOU 2261 C VAL B 296 2690 2293 2117 45 340 397 C ATOM 2262 O VAL A 296 -15.991 -13.561 52.628 1.00 20.11 O ANISOU 2262 O VAL B 296 2468 3060 2115 -327 -181 846 O ATOM 2263 CB VAL A 296 -12.733 -14.106 52.096 1.00 17.13 C ANISOU 2263 CB VAL B 296 2244 2358 1906 49 96 297 C ATOM 2264 CG1 VAL A 296 -12.961 -13.897 53.577 1.00 21.33 C ANISOU 2264 CG1 VAL B 296 2820 3373 1910 -282 143 453 C ATOM 2265 CG2 VAL A 296 -11.759 -15.254 51.846 1.00 19.16 C ANISOU 2265 CG2 VAL B 296 2851 2181 2247 -23 79 -14 C ATOM 2266 N GLY A 297 -14.967 -12.050 51.290 1.00 19.10 N ANISOU 2266 N GLY B 297 2452 2475 2332 270 -28 370 N ATOM 2267 CA GLY A 297 -15.880 -11.001 51.728 1.00 19.70 C ANISOU 2267 CA GLY B 297 2551 2532 2402 140 -263 526 C ATOM 2268 C GLY A 297 -17.326 -11.276 51.379 1.00 20.10 C ANISOU 2268 C GLY B 297 2177 2592 2868 106 -422 890 C ATOM 2269 O GLY A 297 -18.249 -10.976 52.170 1.00 22.14 O ANISOU 2269 O GLY B 297 3004 2564 2846 62 -509 855 O ATOM 2270 N ASN A 298 -17.581 -11.880 50.222 1.00 18.63 N ANISOU 2270 N ASN B 298 2290 2240 2548 47 -152 700 N ATOM 2271 CA ASN A 298 -18.945 -12.287 49.874 1.00 19.43 C ANISOU 2271 CA ASN B 298 2092 2488 2804 73 -163 609 C ATOM 2272 C ASN A 298 -19.459 -13.340 50.838 1.00 19.22 C ANISOU 2272 C ASN B 298 2094 2327 2882 415 -133 1117 C ATOM 2273 O ASN A 298 -20.608 -13.256 51.274 1.00 21.18 O ANISOU 2273 O ASN B 298 3072 2210 2766 77 382 568 O ATOM 2274 CB ASN A 298 -19.008 -12.807 48.440 1.00 18.76 C ANISOU 2274 CB ASN B 298 2003 2324 2800 365 -173 352 C ATOM 2275 CG ASN A 298 -19.114 -11.674 47.437 1.00 17.42 C ANISOU 2275 CG ASN B 298 1751 1864 3003 -54 -25 289 C ATOM 2276 OD1 ASN A 298 -20.131 -10.990 47.336 1.00 20.70 O ANISOU 2276 OD1 ASN B 298 2380 1840 3646 85 35 327 O ATOM 2277 ND2 ASN A 298 -18.053 -11.498 46.658 1.00 20.77 N ANISOU 2277 ND2 ASN B 298 2521 2237 3136 -7 146 684 N ATOM 2278 N LEU A 299 -18.598 -14.331 51.157 1.00 19.81 N ANISOU 2278 N LEU B 299 2179 2268 3080 256 258 1245 N ATOM 2279 CA LEU A 299 -19.074 -15.400 52.054 1.00 19.75 C ANISOU 2279 CA LEU B 299 2448 2466 2592 281 214 1046 C ATOM 2280 C LEU A 299 -19.383 -14.856 53.457 1.00 22.35 C ANISOU 2280 C LEU B 299 2649 2940 2902 -4 10 1456 C ATOM 2281 O LEU A 299 -20.410 -15.220 54.009 1.00 21.71 O ANISOU 2281 O LEU B 299 2703 2824 2720 86 311 1216 O ATOM 2282 CB LEU A 299 -18.086 -16.540 52.119 1.00 18.52 C ANISOU 2282 CB LEU B 299 2552 2297 2186 73 28 686 C ATOM 2283 CG LEU A 299 -17.883 -17.346 50.828 1.00 16.87 C ANISOU 2283 CG LEU B 299 1807 2403 2201 177 299 788 C ATOM 2284 CD1 LEU A 299 -16.645 -18.218 50.940 1.00 22.04 C ANISOU 2284 CD1 LEU B 299 2843 2340 3192 264 -57 917 C ATOM 2285 CD2 LEU A 299 -19.123 -18.182 50.491 1.00 19.08 C ANISOU 2285 CD2 LEU B 299 1814 3022 2414 24 360 454 C ATOM 2286 N GLU A 300 -18.492 -14.011 53.987 1.00 21.95 N ANISOU 2286 N GLU B 300 2645 2996 2700 87 24 1118 N ATOM 2287 CA GLU A 300 -18.729 -13.397 55.302 1.00 23.08 C ANISOU 2287 CA GLU B 300 3001 3274 2494 572 104 833 C ATOM 2288 C GLU A 300 -19.989 -12.535 55.325 1.00 25.50 C ANISOU 2288 C GLU B 300 3315 3213 3162 666 -4 1197 C ATOM 2289 O GLU A 300 -20.754 -12.543 56.301 1.00 27.46 O ANISOU 2289 O GLU B 300 3218 3689 3526 266 199 1375 O ATOM 2290 CB GLU A 300 -17.515 -12.574 55.718 1.00 24.13 C ANISOU 2290 CB GLU B 300 3188 3654 2325 375 -69 1002 C ATOM 2291 CG GLU A 300 -16.292 -13.420 55.965 1.00 27.14 C ANISOU 2291 CG GLU B 300 4026 3760 2526 352 -878 548 C ATOM 2292 CD GLU A 300 -15.149 -12.683 56.624 1.00 32.85 C ANISOU 2292 CD GLU B 300 4617 4267 3600 431 -1870 426 C ATOM 2293 OE1 GLU A 300 -14.920 -11.509 56.257 1.00 39.50 O ANISOU 2293 OE1 GLU B 300 4192 4941 5877 416 -1798 1091 O ATOM 2294 OE2 GLU A 300 -14.509 -13.324 57.481 1.00 38.74 O ANISOU 2294 OE2 GLU B 300 6952 4469 3299 -421 -1608 205 O ATOM 2295 N ALA A 301 -20.240 -11.785 54.233 1.00 23.51 N ANISOU 2295 N ALA B 301 2976 2640 3316 316 -60 1082 N ATOM 2296 CA ALA A 301 -21.468 -10.994 54.174 1.00 24.52 C ANISOU 2296 CA ALA B 301 2667 2632 4019 378 -208 1250 C ATOM 2297 C ALA A 301 -22.675 -11.910 54.187 1.00 25.24 C ANISOU 2297 C ALA B 301 2978 3034 3578 -39 -173 1335 C ATOM 2298 O ALA A 301 -23.585 -11.701 54.978 1.00 26.91 O ANISOU 2298 O ALA B 301 3481 3192 3551 -6 174 1370 O ATOM 2299 CB ALA A 301 -21.503 -10.103 52.945 1.00 26.25 C ANISOU 2299 CB ALA B 301 2721 2625 4628 466 -51 791 C ATOM 2300 N HIS A 302 -22.680 -12.929 53.325 1.00 24.47 N ANISOU 2300 N HIS B 302 2802 3260 3236 -291 -170 1132 N ATOM 2301 CA HIS A 302 -23.794 -13.878 53.277 1.00 22.13 C ANISOU 2301 CA HIS B 302 2467 2378 3563 283 423 977 C ATOM 2302 C HIS A 302 -24.096 -14.457 54.639 1.00 24.31 C ANISOU 2302 C HIS B 302 3119 2800 3318 268 265 1271 C ATOM 2303 O HIS A 302 -25.242 -14.393 55.110 1.00 26.38 O ANISOU 2303 O HIS B 302 3692 3064 3268 -74 267 1337 O ATOM 2304 CB HIS A 302 -23.502 -15.002 52.253 1.00 20.83 C ANISOU 2304 CB HIS B 302 2471 2650 2795 489 452 421 C ATOM 2305 CG HIS A 302 -24.661 -15.969 52.329 1.00 23.88 C ANISOU 2305 CG HIS B 302 2554 3110 3409 264 287 580 C ATOM 2306 ND1 HIS A 302 -25.864 -15.717 51.755 1.00 25.67 N ANISOU 2306 ND1 HIS B 302 2980 2994 3781 -137 639 764 N ATOM 2307 CD2 HIS A 302 -24.787 -17.178 52.918 1.00 24.00 C ANISOU 2307 CD2 HIS B 302 2209 3721 3188 151 -21 450 C ATOM 2308 CE1 HIS A 302 -26.701 -16.705 51.977 1.00 27.07 C ANISOU 2308 CE1 HIS B 302 2851 3125 4310 -4 551 643 C ATOM 2309 NE2 HIS A 302 -26.072 -17.612 52.695 1.00 25.56 N ANISOU 2309 NE2 HIS B 302 2924 3336 3452 -337 682 690 N ATOM 2310 N PHE A 303 -23.113 -15.057 55.313 1.00 24.52 N ANISOU 2310 N PHE B 303 3790 2948 2579 21 376 1411 N ATOM 2311 CA PHE A 303 -23.356 -15.707 56.606 1.00 24.63 C ANISOU 2311 CA PHE B 303 3132 3529 2696 489 360 1627 C ATOM 2312 C PHE A 303 -23.529 -14.757 57.763 1.00 29.55 C ANISOU 2312 C PHE B 303 3826 4736 2667 771 254 1802 C ATOM 2313 O PHE A 303 -23.857 -15.193 58.875 1.00 34.33 O ANISOU 2313 O PHE B 303 5449 4962 2633 530 598 1910 O ATOM 2314 CB PHE A 303 -22.210 -16.697 56.894 1.00 25.83 C ANISOU 2314 CB PHE B 303 3305 3624 2885 219 -100 863 C ATOM 2315 CG PHE A 303 -22.280 -17.867 55.896 1.00 25.72 C ANISOU 2315 CG PHE B 303 2979 3373 3423 453 195 1247 C ATOM 2316 CD1 PHE A 303 -23.373 -18.713 55.924 1.00 28.28 C ANISOU 2316 CD1 PHE B 303 3505 4466 2774 -467 -311 1404 C ATOM 2317 CD2 PHE A 303 -21.289 -18.110 54.978 1.00 26.98 C ANISOU 2317 CD2 PHE B 303 2998 4664 2590 231 493 1394 C ATOM 2318 CE1 PHE A 303 -23.507 -19.778 55.063 1.00 26.53 C ANISOU 2318 CE1 PHE B 303 3056 4111 2913 253 229 1242 C ATOM 2319 CE2 PHE A 303 -21.407 -19.162 54.072 1.00 26.69 C ANISOU 2319 CE2 PHE B 303 2660 4358 3124 791 728 1474 C ATOM 2320 CZ PHE A 303 -22.526 -19.990 54.104 1.00 24.56 C ANISOU 2320 CZ PHE B 303 2853 3492 2985 740 527 1062 C ATOM 2321 N SER A 304 -23.345 -13.452 57.548 1.00 32.27 N ANISOU 2321 N SER B 304 4055 4659 3547 1312 -306 1636 N ATOM 2322 CA SER A 304 -23.653 -12.468 58.579 1.00 36.52 C ANISOU 2322 CA SER B 304 4689 4832 4354 823 -422 2721 C ATOM 2323 C SER A 304 -24.890 -11.653 58.238 1.00 40.58 C ANISOU 2323 C SER B 304 7050 4343 4027 -158 136 3583 C ATOM 2324 O SER A 304 -25.254 -10.721 58.964 1.00 39.65 O ANISOU 2324 O SER B 304 6374 4623 4070 597 604 3259 O ATOM 2325 CB SER A 304 -22.446 -11.544 58.812 1.00 41.40 C ANISOU 2325 CB SER B 304 5247 5601 4883 568 -1771 2090 C ATOM 2326 OG SER A 304 -22.197 -10.691 57.700 1.00 48.21 O ANISOU 2326 OG SER B 304 4271 7445 6604 454 -689 3260 O ATOM 2327 N GLY A 305 -25.601 -11.985 57.173 1.00 37.45 N ANISOU 2327 N GLY B 305 5052 4252 4926 326 326 2874 N ATOM 2328 CA GLY A 305 -26.911 -11.383 56.900 1.00 38.38 C ANISOU 2328 CA GLY B 305 4758 4245 5581 66 904 2937 C ATOM 2329 C GLY A 305 -26.784 -10.013 56.258 1.00 39.31 C ANISOU 2329 C GLY B 305 4960 4154 5821 450 976 3305 C ATOM 2330 O GLY A 305 -27.795 -9.286 56.261 1.00 37.05 O ANISOU 2330 O GLY B 305 4299 4126 5653 35 4 2778 O ATOM 2331 N LYS A 306 -25.577 -9.742 55.750 1.00 38.30 N ANISOU 2331 N LYS B 306 5120 3958 5473 164 1348 2309 N ATOM 2332 CA LYS A 306 -25.309 -8.466 55.088 1.00 35.04 C ANISOU 2332 CA LYS B 306 4918 3424 4971 386 855 2420 C ATOM 2333 C LYS A 306 -25.441 -8.591 53.574 1.00 32.70 C ANISOU 2333 C LYS B 306 4282 3079 5063 801 576 2448 C ATOM 2334 O LYS A 306 -25.331 -9.673 53.005 1.00 33.51 O ANISOU 2334 O LYS B 306 3790 3063 5880 438 394 2617 O ATOM 2335 CB LYS A 306 -23.915 -7.984 55.508 1.00 38.59 C ANISOU 2335 CB LYS B 306 4535 4263 5864 642 -323 2528 C ATOM 2336 CG LYS A 306 -23.751 -8.133 57.019 1.00 43.86 C ANISOU 2336 CG LYS B 306 5903 4975 5789 1254 -1466 2630 C ATOM 2337 CD LYS A 306 -22.756 -7.148 57.562 1.00 52.67 C ANISOU 2337 CD LYS B 306 6657 6047 7309 71 -1897 2159 C ATOM 2338 CE LYS A 306 -21.426 -7.145 56.826 1.00 57.52 C ANISOU 2338 CE LYS B 306 6943 6535 8377 -128 -3022 3398 C ATOM 2339 NZ LYS A 306 -20.446 -6.189 57.451 1.00 74.61 N ANISOU 2339 NZ LYS B 306 10564 8607 9178 -3584 -5343 3720 N ATOM 2340 N PRO A 307 -25.705 -7.495 52.887 1.00 32.91 N ANISOU 2340 N PRO B 307 4555 2864 5087 835 -126 1722 N ATOM 2341 CA PRO A 307 -25.794 -7.543 51.434 1.00 33.01 C ANISOU 2341 CA PRO B 307 4351 3141 5052 365 29 1840 C ATOM 2342 C PRO A 307 -24.494 -8.051 50.838 1.00 32.29 C ANISOU 2342 C PRO B 307 4648 2791 4830 492 32 1461 C ATOM 2343 O PRO A 307 -23.403 -7.755 51.351 1.00 29.20 O ANISOU 2343 O PRO B 307 3397 2973 4722 793 394 1513 O ATOM 2344 CB PRO A 307 -25.984 -6.081 51.034 1.00 35.33 C ANISOU 2344 CB PRO B 307 5197 2581 5647 371 709 1670 C ATOM 2345 CG PRO A 307 -26.519 -5.408 52.248 1.00 35.77 C ANISOU 2345 CG PRO B 307 4957 2924 5709 867 111 1422 C ATOM 2346 CD PRO A 307 -25.967 -6.144 53.433 1.00 34.01 C ANISOU 2346 CD PRO B 307 4491 2830 5601 825 -754 1158 C ATOM 2347 N LEU A 308 -24.659 -8.802 49.753 1.00 27.39 N ANISOU 2347 N LEU B 308 3331 2326 4748 598 552 1330 N ATOM 2348 CA LEU A 308 -23.460 -9.382 49.131 1.00 25.21 C ANISOU 2348 CA LEU B 308 2914 2352 4313 41 265 1155 C ATOM 2349 C LEU A 308 -22.648 -8.308 48.436 1.00 25.40 C ANISOU 2349 C LEU B 308 2696 2326 4629 522 225 1210 C ATOM 2350 O LEU A 308 -23.187 -7.251 48.155 1.00 30.93 O ANISOU 2350 O LEU B 308 3606 2602 5545 855 665 1211 O ATOM 2351 CB LEU A 308 -23.838 -10.521 48.175 1.00 26.05 C ANISOU 2351 CB LEU B 308 2666 2712 4520 258 398 1344 C ATOM 2352 CG LEU A 308 -24.616 -11.679 48.827 1.00 24.47 C ANISOU 2352 CG LEU B 308 2841 2552 3906 42 446 738 C ATOM 2353 CD1 LEU A 308 -24.851 -12.813 47.820 1.00 26.22 C ANISOU 2353 CD1 LEU B 308 2730 3320 3912 639 554 490 C ATOM 2354 CD2 LEU A 308 -23.929 -12.183 50.098 1.00 27.10 C ANISOU 2354 CD2 LEU B 308 4025 2389 3881 -401 440 751 C ATOM 2355 N LEU A 309 -21.376 -8.597 48.165 1.00 24.80 N ANISOU 2355 N LEU B 309 3089 2552 3783 439 712 1543 N ATOM 2356 CA LEU A 309 -20.532 -7.590 47.542 1.00 23.10 C ANISOU 2356 CA LEU B 309 2794 2255 3730 642 679 597 C ATOM 2357 C LEU A 309 -20.664 -7.545 46.028 1.00 23.95 C ANISOU 2357 C LEU B 309 2606 2757 3737 419 597 441 C ATOM 2358 O LEU A 309 -20.824 -6.464 45.425 1.00 24.07 O ANISOU 2358 O LEU B 309 2799 2755 3590 622 336 322 O ATOM 2359 CB LEU A 309 -19.082 -7.879 47.971 1.00 23.91 C ANISOU 2359 CB LEU B 309 2752 2447 3886 525 541 464 C ATOM 2360 CG LEU A 309 -18.841 -7.898 49.482 1.00 27.52 C ANISOU 2360 CG LEU B 309 3107 3357 3993 261 -836 639 C ATOM 2361 CD1 LEU A 309 -17.339 -8.005 49.809 1.00 26.11 C ANISOU 2361 CD1 LEU B 309 2510 3921 3491 -336 -171 822 C ATOM 2362 CD2 LEU A 309 -19.462 -6.675 50.129 1.00 40.04 C ANISOU 2362 CD2 LEU B 309 5158 4018 6038 721 -2421 990 C ATOM 2363 N THR A 310 -20.584 -8.732 45.440 1.00 22.98 N ANISOU 2363 N THR B 310 2831 2295 3606 476 624 292 N ATOM 2364 CA THR A 310 -20.640 -8.866 43.995 1.00 21.63 C ANISOU 2364 CA THR B 310 2400 2220 3597 328 741 357 C ATOM 2365 C THR A 310 -21.564 -9.996 43.570 1.00 22.55 C ANISOU 2365 C THR B 310 2452 1955 4162 404 482 382 C ATOM 2366 O THR A 310 -21.175 -10.947 42.920 1.00 20.73 O ANISOU 2366 O THR B 310 2710 2024 3141 350 493 66 O ATOM 2367 CB THR A 310 -19.230 -9.047 43.420 1.00 22.41 C ANISOU 2367 CB THR B 310 2682 2142 3689 214 692 223 C ATOM 2368 OG1 THR A 310 -18.557 -10.057 44.162 1.00 21.34 O ANISOU 2368 OG1 THR B 310 3216 2185 2706 400 211 328 O ATOM 2369 CG2 THR A 310 -18.424 -7.758 43.586 1.00 29.02 C ANISOU 2369 CG2 THR B 310 2543 4348 4137 -225 1500 527 C ATOM 2370 N PRO A 311 -22.854 -9.859 43.887 1.00 23.41 N ANISOU 2370 N PRO B 311 2672 2162 4063 180 574 477 N ATOM 2371 CA PRO A 311 -23.810 -10.875 43.448 1.00 24.94 C ANISOU 2371 CA PRO B 311 2952 2566 3959 -130 536 -57 C ATOM 2372 C PRO A 311 -24.093 -10.841 41.946 1.00 23.89 C ANISOU 2372 C PRO B 311 3434 1572 4072 581 532 -460 C ATOM 2373 O PRO A 311 -24.026 -9.782 41.309 1.00 27.85 O ANISOU 2373 O PRO B 311 3004 2960 4616 441 308 -1150 O ATOM 2374 CB PRO A 311 -25.097 -10.512 44.204 1.00 29.28 C ANISOU 2374 CB PRO B 311 3746 2886 4492 -807 534 162 C ATOM 2375 CG PRO A 311 -24.985 -9.042 44.456 1.00 27.21 C ANISOU 2375 CG PRO B 311 4338 2031 3968 -324 647 -7 C ATOM 2376 CD PRO A 311 -23.504 -8.757 44.636 1.00 23.98 C ANISOU 2376 CD PRO B 311 3410 1842 3859 153 532 276 C ATOM 2377 N VAL A 312 -24.414 -12.028 41.445 1.00 23.85 N ANISOU 2377 N VAL B 312 3056 2300 3707 294 742 -703 N ATOM 2378 CA VAL A 312 -24.943 -12.169 40.108 1.00 25.11 C ANISOU 2378 CA VAL B 312 3104 2808 3629 106 913 -603 C ATOM 2379 C VAL A 312 -26.360 -12.733 40.122 1.00 26.84 C ANISOU 2379 C VAL B 312 3325 3000 3873 -145 658 -688 C ATOM 2380 O VAL A 312 -27.187 -12.288 39.292 1.00 30.46 O ANISOU 2380 O VAL B 312 3868 2729 4976 114 718 -1031 O ATOM 2381 CB VAL A 312 -24.021 -13.039 39.241 1.00 29.45 C ANISOU 2381 CB VAL B 312 3610 3214 4366 -269 -29 -102 C ATOM 2382 CG1 VAL A 312 -24.689 -13.412 37.932 1.00 31.52 C ANISOU 2382 CG1 VAL B 312 4729 3352 3895 -680 306 -144 C ATOM 2383 CG2 VAL A 312 -22.707 -12.269 39.028 1.00 32.94 C ANISOU 2383 CG2 VAL B 312 3279 2407 6828 230 -408 737 C ATOM 2384 N VAL A 313 -26.636 -13.652 41.021 1.00 28.87 N ANISOU 2384 N VAL B 313 2985 3063 4920 -143 948 -873 N ATOM 2385 CA VAL A 313 -27.929 -14.278 41.286 1.00 30.08 C ANISOU 2385 CA VAL B 313 3544 3068 4818 -550 941 -938 C ATOM 2386 C VAL A 313 -28.273 -14.256 42.764 1.00 31.04 C ANISOU 2386 C VAL B 313 4466 2291 5036 -873 374 -201 C ATOM 2387 O VAL A 313 -29.477 -14.191 43.051 1.00 61.71 O ANISOU 2387 O VAL B 313 13704 3404 6341 -4298 318 2 O ATOM 2388 CB VAL A 313 -27.964 -15.764 40.839 1.00 35.75 C ANISOU 2388 CB VAL B 313 3217 4815 5551 -1461 -358 50 C ATOM 2389 CG1 VAL A 313 -29.177 -16.466 41.419 1.00 45.05 C ANISOU 2389 CG1 VAL B 313 3495 6372 7249 -1484 342 863 C ATOM 2390 CG2 VAL A 313 -27.908 -15.796 39.324 1.00 46.23 C ANISOU 2390 CG2 VAL B 313 5174 6803 5590 -3458 -987 397 C ATOM 2391 OXT VAL A 313 -27.378 -14.317 43.624 1.00 25.01 O ANISOU 2391 OXT VAL B 313 3063 1834 4604 122 458 -143 O TER 2392 VAL B 313 END