ATOM 1 N ASN A 3 48.872 55.475 44.218 1.00 41.21 N ANISOU 1 N ASN A 3 5286 5280 5092 -22 -74 -43 N ATOM 2 CA ASN A 3 48.591 54.003 44.268 1.00 39.21 C ANISOU 2 CA ASN A 3 5022 5109 4767 -38 -65 -41 C ATOM 3 C ASN A 3 47.724 53.498 43.082 1.00 37.49 C ANISOU 3 C ASN A 3 4795 4861 4587 -64 -23 -15 C ATOM 4 O ASN A 3 47.126 52.417 43.141 1.00 37.44 O ANISOU 4 O ASN A 3 4919 4686 4619 71 60 -72 O ATOM 5 CB ASN A 3 47.959 53.627 45.626 1.00 41.38 C ANISOU 5 CB ASN A 3 5312 5433 4974 -42 -12 75 C ATOM 6 CG ASN A 3 46.670 54.393 45.921 1.00 48.08 C ANISOU 6 CG ASN A 3 5930 6164 6173 213 47 -17 C ATOM 7 OD1 ASN A 3 46.581 55.613 45.706 1.00 52.26 O ANISOU 7 OD1 ASN A 3 6786 6322 6747 31 -14 110 O ATOM 8 ND2 ASN A 3 45.665 53.675 46.439 1.00 52.95 N ANISOU 8 ND2 ASN A 3 6357 6739 7022 -38 47 164 N ATOM 9 N VAL A 4 47.713 54.273 41.998 1.00 35.31 N ANISOU 9 N VAL A 4 4388 4697 4331 -67 -63 -91 N ATOM 10 CA VAL A 4 46.850 54.008 40.843 1.00 31.71 C ANISOU 10 CA VAL A 4 4020 4072 3955 -44 105 -190 C ATOM 11 C VAL A 4 47.719 53.476 39.706 1.00 27.77 C ANISOU 11 C VAL A 4 3483 3445 3623 -94 -10 -222 C ATOM 12 O VAL A 4 48.879 53.863 39.543 1.00 25.08 O ANISOU 12 O VAL A 4 3168 3089 3271 -77 -27 -672 O ATOM 13 CB VAL A 4 45.905 55.238 40.503 1.00 32.76 C ANISOU 13 CB VAL A 4 4359 4053 4035 -70 -15 -94 C ATOM 14 CG1 VAL A 4 46.314 56.465 41.299 1.00 38.88 C ANISOU 14 CG1 VAL A 4 5148 4766 4858 -153 -76 -102 C ATOM 15 CG2 VAL A 4 45.856 55.599 39.052 1.00 32.78 C ANISOU 15 CG2 VAL A 4 3984 4240 4228 -90 -120 -128 C ATOM 16 N PHE A 5 47.150 52.550 38.956 1.00 24.57 N ANISOU 16 N PHE A 5 3087 3042 3203 -127 -68 -48 N ATOM 17 CA PHE A 5 47.825 51.924 37.858 1.00 22.77 C ANISOU 17 CA PHE A 5 2768 2855 3026 -125 44 21 C ATOM 18 C PHE A 5 46.779 51.404 36.866 1.00 20.36 C ANISOU 18 C PHE A 5 2512 2661 2561 -18 46 0 C ATOM 19 O PHE A 5 45.572 51.501 37.117 1.00 18.18 O ANISOU 19 O PHE A 5 2408 2268 2229 101 134 -170 O ATOM 20 CB PHE A 5 48.685 50.762 38.350 1.00 22.13 C ANISOU 20 CB PHE A 5 2589 2999 2820 -103 -12 112 C ATOM 21 CG PHE A 5 47.928 49.742 39.158 1.00 21.63 C ANISOU 21 CG PHE A 5 2626 2817 2774 174 -255 210 C ATOM 22 CD1 PHE A 5 47.112 48.778 38.566 1.00 20.25 C ANISOU 22 CD1 PHE A 5 2787 2218 2688 150 -156 217 C ATOM 23 CD2 PHE A 5 48.058 49.730 40.505 1.00 22.10 C ANISOU 23 CD2 PHE A 5 3357 2882 2158 -26 23 -400 C ATOM 24 CE1 PHE A 5 46.384 47.860 39.352 1.00 20.23 C ANISOU 24 CE1 PHE A 5 2597 2626 2463 162 -202 226 C ATOM 25 CE2 PHE A 5 47.353 48.818 41.294 1.00 25.24 C ANISOU 25 CE2 PHE A 5 3557 3021 3011 -429 -89 -134 C ATOM 26 CZ PHE A 5 46.519 47.879 40.708 1.00 21.93 C ANISOU 26 CZ PHE A 5 2850 2780 2698 -256 -61 -169 C ATOM 27 N ASP A 6 47.255 50.824 35.770 1.00 19.30 N ANISOU 27 N ASP A 6 2270 2422 2640 -133 251 60 N ATOM 28 CA ASP A 6 46.409 50.174 34.764 1.00 19.59 C ANISOU 28 CA ASP A 6 2476 2422 2542 -10 73 -2 C ATOM 29 C ASP A 6 47.023 48.835 34.335 1.00 18.64 C ANISOU 29 C ASP A 6 2253 2408 2419 -68 71 38 C ATOM 30 O ASP A 6 48.092 48.438 34.812 1.00 16.78 O ANISOU 30 O ASP A 6 2297 2168 1908 -309 -195 315 O ATOM 31 CB ASP A 6 46.207 51.077 33.541 1.00 19.47 C ANISOU 31 CB ASP A 6 2488 2443 2466 -69 100 -155 C ATOM 32 CG ASP A 6 44.815 50.937 32.919 1.00 18.97 C ANISOU 32 CG ASP A 6 2318 2317 2572 -79 160 6 C ATOM 33 OD1 ASP A 6 44.083 49.958 33.228 1.00 15.50 O ANISOU 33 OD1 ASP A 6 1605 2445 1837 -152 -248 108 O ATOM 34 OD2 ASP A 6 44.451 51.786 32.089 1.00 24.72 O ANISOU 34 OD2 ASP A 6 2958 2981 3452 -287 -189 221 O ATOM 35 N TYR A 7 46.328 48.166 33.414 1.00 18.62 N ANISOU 35 N TYR A 7 2237 2445 2391 94 34 -49 N ATOM 36 CA TYR A 7 46.667 46.822 32.921 1.00 18.78 C ANISOU 36 CA TYR A 7 2396 2341 2399 28 -17 -38 C ATOM 37 C TYR A 7 48.141 46.656 32.581 1.00 17.77 C ANISOU 37 C TYR A 7 2258 2182 2310 24 -46 -139 C ATOM 38 O TYR A 7 48.775 45.687 33.029 1.00 19.79 O ANISOU 38 O TYR A 7 2403 2263 2852 65 -178 -296 O ATOM 39 CB TYR A 7 45.790 46.474 31.710 1.00 19.13 C ANISOU 39 CB TYR A 7 2368 2343 2555 35 -45 -74 C ATOM 40 CG TYR A 7 44.365 46.149 32.126 1.00 18.94 C ANISOU 40 CG TYR A 7 2359 2094 2740 0 -50 52 C ATOM 41 CD1 TYR A 7 44.054 44.930 32.750 1.00 18.84 C ANISOU 41 CD1 TYR A 7 2132 2175 2848 63 7 173 C ATOM 42 CD2 TYR A 7 43.336 47.068 31.945 1.00 17.89 C ANISOU 42 CD2 TYR A 7 2141 2198 2456 55 -10 41 C ATOM 43 CE1 TYR A 7 42.771 44.646 33.156 1.00 18.35 C ANISOU 43 CE1 TYR A 7 2299 2070 2602 27 -86 38 C ATOM 44 CE2 TYR A 7 42.054 46.774 32.328 1.00 20.83 C ANISOU 44 CE2 TYR A 7 2278 2412 3222 -31 32 60 C ATOM 45 CZ TYR A 7 41.767 45.568 32.946 1.00 21.07 C ANISOU 45 CZ TYR A 7 2320 2505 3178 59 -94 165 C ATOM 46 OH TYR A 7 40.468 45.273 33.359 1.00 20.80 O ANISOU 46 OH TYR A 7 2448 2019 3434 147 126 26 O ATOM 47 N GLU A 8 48.679 47.599 31.815 1.00 18.34 N ANISOU 47 N GLU A 8 2254 2200 2511 109 18 -93 N ATOM 48 CA GLU A 8 50.068 47.524 31.331 1.00 18.39 C ANISOU 48 CA GLU A 8 2407 2216 2362 -29 85 76 C ATOM 49 C GLU A 8 51.133 47.592 32.436 1.00 19.19 C ANISOU 49 C GLU A 8 2425 2353 2511 9 140 35 C ATOM 50 O GLU A 8 52.296 47.184 32.219 1.00 21.48 O ANISOU 50 O GLU A 8 2465 2900 2794 237 -22 169 O ATOM 51 CB GLU A 8 50.293 48.575 30.197 1.00 19.09 C ANISOU 51 CB GLU A 8 2484 2424 2342 3 -3 143 C ATOM 52 CG GLU A 8 50.466 50.015 30.650 1.00 16.06 C ANISOU 52 CG GLU A 8 2637 2167 1296 -61 10 356 C ATOM 53 CD GLU A 8 49.177 50.811 30.756 1.00 25.03 C ANISOU 53 CD GLU A 8 3167 3034 3309 98 -42 138 C ATOM 54 OE1 GLU A 8 48.087 50.184 30.827 1.00 27.68 O ANISOU 54 OE1 GLU A 8 3264 3476 3775 -64 -451 425 O ATOM 55 OE2 GLU A 8 49.262 52.083 30.792 1.00 21.93 O ANISOU 55 OE2 GLU A 8 3517 2913 1902 -271 -378 -61 O ATOM 56 N ASP A 9 50.750 48.069 33.631 1.00 17.03 N ANISOU 56 N ASP A 9 2241 2050 2177 0 98 203 N ATOM 57 CA ASP A 9 51.669 48.206 34.720 1.00 17.43 C ANISOU 57 CA ASP A 9 2173 2096 2353 -72 61 37 C ATOM 58 C ASP A 9 51.763 46.923 35.566 1.00 17.35 C ANISOU 58 C ASP A 9 2150 2205 2236 3 -19 95 C ATOM 59 O ASP A 9 52.652 46.799 36.395 1.00 18.15 O ANISOU 59 O ASP A 9 1974 2277 2643 -45 -175 198 O ATOM 60 CB ASP A 9 51.201 49.330 35.638 1.00 17.67 C ANISOU 60 CB ASP A 9 2021 2311 2379 -60 9 -74 C ATOM 61 CG ASP A 9 51.086 50.654 34.909 1.00 21.03 C ANISOU 61 CG ASP A 9 2673 2401 2915 -155 171 9 C ATOM 62 OD1 ASP A 9 52.098 51.039 34.256 1.00 18.68 O ANISOU 62 OD1 ASP A 9 2645 2353 2100 -173 360 10 O ATOM 63 OD2 ASP A 9 50.000 51.287 34.988 1.00 21.89 O ANISOU 63 OD2 ASP A 9 2519 2832 2964 -178 76 142 O ATOM 64 N ILE A 10 50.846 45.983 35.377 1.00 16.30 N ANISOU 64 N ILE A 10 2088 2006 2098 7 25 103 N ATOM 65 CA ILE A 10 50.783 44.806 36.257 1.00 17.32 C ANISOU 65 CA ILE A 10 2205 2105 2269 -49 64 37 C ATOM 66 C ILE A 10 51.407 43.558 35.640 1.00 16.31 C ANISOU 66 C ILE A 10 2148 1905 2142 -49 28 69 C ATOM 67 O ILE A 10 51.147 43.234 34.472 1.00 17.75 O ANISOU 67 O ILE A 10 2239 2158 2347 9 10 111 O ATOM 68 CB ILE A 10 49.312 44.494 36.666 1.00 17.66 C ANISOU 68 CB ILE A 10 2154 2240 2314 -79 -11 7 C ATOM 69 CG1 ILE A 10 48.707 45.627 37.501 1.00 18.85 C ANISOU 69 CG1 ILE A 10 2158 2081 2924 -174 223 0 C ATOM 70 CG2 ILE A 10 49.235 43.165 37.488 1.00 18.78 C ANISOU 70 CG2 ILE A 10 2418 2159 2557 -78 209 32 C ATOM 71 CD1 ILE A 10 49.462 45.929 38.746 1.00 22.83 C ANISOU 71 CD1 ILE A 10 2409 3125 3138 62 190 -58 C ATOM 72 N GLN A 11 52.225 42.857 36.429 1.00 16.01 N ANISOU 72 N GLN A 11 2026 2055 2002 20 -119 -105 N ATOM 73 CA GLN A 11 52.605 41.462 36.111 1.00 17.07 C ANISOU 73 CA GLN A 11 2182 2101 2201 -10 -44 -25 C ATOM 74 C GLN A 11 52.199 40.548 37.217 1.00 15.69 C ANISOU 74 C GLN A 11 1957 1956 2045 -6 -48 -76 C ATOM 75 O GLN A 11 52.450 40.835 38.397 1.00 15.79 O ANISOU 75 O GLN A 11 2351 1772 1877 -11 -311 75 O ATOM 76 CB GLN A 11 54.120 41.300 35.891 1.00 18.13 C ANISOU 76 CB GLN A 11 2276 2187 2425 -15 -148 -66 C ATOM 77 CG GLN A 11 54.645 41.911 34.624 1.00 21.51 C ANISOU 77 CG GLN A 11 2640 2874 2658 140 335 -2 C ATOM 78 CD GLN A 11 54.255 41.117 33.375 1.00 30.51 C ANISOU 78 CD GLN A 11 4162 3696 3734 -3 -204 -214 C ATOM 79 OE1 GLN A 11 54.460 39.920 33.294 1.00 34.17 O ANISOU 79 OE1 GLN A 11 5087 3813 4082 368 -249 99 O ATOM 80 NE2 GLN A 11 53.677 41.802 32.401 1.00 33.86 N ANISOU 80 NE2 GLN A 11 4510 4389 3966 56 -20 82 N ATOM 81 N LEU A 12 51.536 39.453 36.869 1.00 15.16 N ANISOU 81 N LEU A 12 1907 1836 2014 103 -77 -135 N ATOM 82 CA LEU A 12 51.200 38.424 37.868 1.00 15.88 C ANISOU 82 CA LEU A 12 1964 1998 2072 -38 16 -54 C ATOM 83 C LEU A 12 52.376 37.440 38.052 1.00 15.72 C ANISOU 83 C LEU A 12 1995 1917 2060 -4 -17 -18 C ATOM 84 O LEU A 12 53.078 37.053 37.079 1.00 17.40 O ANISOU 84 O LEU A 12 2027 2125 2457 256 -17 217 O ATOM 85 CB LEU A 12 49.910 37.660 37.450 1.00 16.27 C ANISOU 85 CB LEU A 12 1845 2093 2245 -86 9 67 C ATOM 86 CG LEU A 12 48.712 38.571 37.077 1.00 17.96 C ANISOU 86 CG LEU A 12 1992 2517 2313 24 -57 -44 C ATOM 87 CD1 LEU A 12 47.530 37.778 36.569 1.00 19.70 C ANISOU 87 CD1 LEU A 12 2160 2288 3034 -100 -77 -21 C ATOM 88 CD2 LEU A 12 48.299 39.450 38.249 1.00 16.81 C ANISOU 88 CD2 LEU A 12 1617 2300 2471 213 -220 35 C ATOM 89 N ILE A 13 52.559 37.008 39.279 1.00 17.01 N ANISOU 89 N ILE A 13 2170 2036 2253 42 90 -119 N ATOM 90 CA ILE A 13 53.659 36.189 39.665 1.00 17.96 C ANISOU 90 CA ILE A 13 2247 2176 2397 28 34 -19 C ATOM 91 C ILE A 13 53.253 34.707 39.675 1.00 19.00 C ANISOU 91 C ILE A 13 2296 2265 2655 -67 39 83 C ATOM 92 O ILE A 13 52.258 34.313 40.313 1.00 20.30 O ANISOU 92 O ILE A 13 2468 2507 2735 107 95 415 O ATOM 93 CB ILE A 13 54.207 36.590 41.023 1.00 19.01 C ANISOU 93 CB ILE A 13 2321 2167 2732 -47 -148 -53 C ATOM 94 CG1 ILE A 13 54.790 38.013 40.912 1.00 19.59 C ANISOU 94 CG1 ILE A 13 2677 2123 2641 -28 -73 276 C ATOM 95 CG2 ILE A 13 55.312 35.592 41.508 1.00 19.75 C ANISOU 95 CG2 ILE A 13 2556 2284 2660 -17 -98 -98 C ATOM 96 CD1 ILE A 13 55.144 38.618 42.211 1.00 20.35 C ANISOU 96 CD1 ILE A 13 2821 2328 2581 -101 -129 9 C ATOM 97 N PRO A 14 54.032 33.887 38.966 1.00 18.60 N ANISOU 97 N PRO A 14 2394 2301 2372 -126 -8 -100 N ATOM 98 CA PRO A 14 53.741 32.452 38.906 1.00 18.78 C ANISOU 98 CA PRO A 14 2380 2333 2422 42 -29 8 C ATOM 99 C PRO A 14 53.853 31.721 40.252 1.00 19.36 C ANISOU 99 C PRO A 14 2558 2368 2428 -6 19 93 C ATOM 100 O PRO A 14 54.685 32.072 41.114 1.00 18.63 O ANISOU 100 O PRO A 14 2764 2164 2149 -159 -82 295 O ATOM 101 CB PRO A 14 54.757 31.929 37.892 1.00 18.93 C ANISOU 101 CB PRO A 14 2451 2344 2397 89 76 -73 C ATOM 102 CG PRO A 14 55.184 33.126 37.104 1.00 20.88 C ANISOU 102 CG PRO A 14 2563 2543 2828 192 166 -181 C ATOM 103 CD PRO A 14 55.202 34.218 38.148 1.00 20.71 C ANISOU 103 CD PRO A 14 2535 2627 2705 -268 -21 -117 C ATOM 104 N ALA A 15 53.029 30.700 40.394 1.00 18.88 N ANISOU 104 N ALA A 15 2455 2342 2377 -3 103 174 N ATOM 105 CA ALA A 15 53.071 29.799 41.554 1.00 20.19 C ANISOU 105 CA ALA A 15 2668 2505 2495 24 19 67 C ATOM 106 C ALA A 15 53.362 28.366 41.048 1.00 20.31 C ANISOU 106 C ALA A 15 2749 2440 2527 89 -51 54 C ATOM 107 O ALA A 15 53.274 28.108 39.831 1.00 18.57 O ANISOU 107 O ALA A 15 2628 2176 2248 263 163 -159 O ATOM 108 CB ALA A 15 51.762 29.861 42.228 1.00 21.80 C ANISOU 108 CB ALA A 15 2908 2691 2683 116 50 225 C ATOM 109 N LYS A 16 53.688 27.438 41.953 1.00 20.94 N ANISOU 109 N LYS A 16 2762 2603 2590 -39 61 60 N ATOM 110 CA LYS A 16 54.039 26.067 41.532 1.00 21.33 C ANISOU 110 CA LYS A 16 2758 2587 2759 31 119 69 C ATOM 111 C LYS A 16 52.970 25.460 40.620 1.00 20.26 C ANISOU 111 C LYS A 16 2647 2284 2766 145 60 231 C ATOM 112 O LYS A 16 51.786 25.409 40.988 1.00 19.71 O ANISOU 112 O LYS A 16 2481 2384 2622 -140 13 224 O ATOM 113 CB LYS A 16 54.283 25.152 42.737 1.00 22.97 C ANISOU 113 CB LYS A 16 2860 2761 3104 -19 101 -44 C ATOM 114 CG LYS A 16 54.894 23.807 42.379 1.00 23.21 C ANISOU 114 CG LYS A 16 3002 2769 3046 -52 175 16 C ATOM 115 CD LYS A 16 54.981 22.979 43.612 1.00 24.98 C ANISOU 115 CD LYS A 16 3355 2990 3147 141 69 95 C ATOM 116 CE LYS A 16 55.809 21.773 43.458 1.00 29.28 C ANISOU 116 CE LYS A 16 3901 3535 3689 249 -19 -72 C ATOM 117 NZ LYS A 16 55.872 21.067 44.756 1.00 29.87 N ANISOU 117 NZ LYS A 16 4373 3184 3791 -171 101 160 N ATOM 118 N CYS A 17 53.387 24.985 39.443 1.00 20.71 N ANISOU 118 N CYS A 17 2673 2494 2701 95 112 435 N ATOM 119 CA CYS A 17 52.488 24.348 38.491 1.00 22.28 C ANISOU 119 CA CYS A 17 2865 2612 2988 0 143 146 C ATOM 120 C CYS A 17 52.110 22.971 38.979 1.00 22.34 C ANISOU 120 C CYS A 17 2884 2614 2990 7 147 174 C ATOM 121 O CYS A 17 52.996 22.176 39.325 1.00 21.11 O ANISOU 121 O CYS A 17 2674 2357 2990 -111 352 274 O ATOM 122 CB CYS A 17 53.133 24.204 37.123 1.00 21.90 C ANISOU 122 CB CYS A 17 3110 2435 2774 7 141 257 C ATOM 123 SG CYS A 17 52.070 23.634 35.787 1.00 25.86 S ANISOU 123 SG CYS A 17 3269 3112 3442 -128 -53 366 S ATOM 124 N ILE A 18 50.806 22.700 38.979 1.00 23.31 N ANISOU 124 N ILE A 18 2704 2705 3446 26 191 107 N ATOM 125 CA ILE A 18 50.240 21.414 39.495 1.00 24.28 C ANISOU 125 CA ILE A 18 3038 2826 3360 -15 147 168 C ATOM 126 C ILE A 18 49.484 20.611 38.458 1.00 24.56 C ANISOU 126 C ILE A 18 3030 2978 3323 -10 243 62 C ATOM 127 O ILE A 18 48.956 19.529 38.775 1.00 27.45 O ANISOU 127 O ILE A 18 3626 3112 3691 13 287 -85 O ATOM 128 CB ILE A 18 49.295 21.600 40.730 1.00 23.30 C ANISOU 128 CB ILE A 18 2966 2803 3084 -77 67 128 C ATOM 129 CG1 ILE A 18 48.021 22.383 40.337 1.00 21.87 C ANISOU 129 CG1 ILE A 18 2944 2403 2961 -104 139 139 C ATOM 130 CG2 ILE A 18 50.032 22.170 41.931 1.00 21.14 C ANISOU 130 CG2 ILE A 18 2663 2341 3028 -172 284 258 C ATOM 131 CD1 ILE A 18 47.066 22.645 41.477 1.00 25.35 C ANISOU 131 CD1 ILE A 18 3430 2647 3554 -35 277 135 C ATOM 132 N VAL A 19 49.449 21.089 37.219 1.00 24.48 N ANISOU 132 N VAL A 19 3050 2865 3385 97 48 124 N ATOM 133 CA VAL A 19 48.818 20.368 36.140 1.00 27.84 C ANISOU 133 CA VAL A 19 3537 3369 3672 -27 33 59 C ATOM 134 C VAL A 19 49.887 19.829 35.184 1.00 29.27 C ANISOU 134 C VAL A 19 3664 3610 3843 -11 112 27 C ATOM 135 O VAL A 19 50.983 20.393 35.053 1.00 28.29 O ANISOU 135 O VAL A 19 3578 3433 3737 2 188 23 O ATOM 136 CB VAL A 19 47.766 21.218 35.343 1.00 27.25 C ANISOU 136 CB VAL A 19 3429 3360 3563 -48 -21 -76 C ATOM 137 CG1 VAL A 19 46.633 21.680 36.260 1.00 26.70 C ANISOU 137 CG1 VAL A 19 3178 3340 3625 -19 -72 9 C ATOM 138 CG2 VAL A 19 48.426 22.412 34.622 1.00 25.28 C ANISOU 138 CG2 VAL A 19 3436 3265 2901 56 -54 -58 C ATOM 139 N ASN A 20 49.559 18.720 34.537 1.00 32.14 N ANISOU 139 N ASN A 20 4061 3979 4172 -58 29 -63 N ATOM 140 CA ASN A 20 50.420 18.129 33.520 1.00 33.79 C ANISOU 140 CA ASN A 20 4277 4248 4312 7 51 -147 C ATOM 141 C ASN A 20 50.122 18.668 32.157 1.00 34.71 C ANISOU 141 C ASN A 20 4391 4377 4421 4 -25 -116 C ATOM 142 O ASN A 20 50.919 18.489 31.241 1.00 34.40 O ANISOU 142 O ASN A 20 4438 4485 4145 227 -127 -446 O ATOM 143 CB ASN A 20 50.260 16.612 33.483 1.00 35.79 C ANISOU 143 CB ASN A 20 4544 4431 4624 31 4 -110 C ATOM 144 CG ASN A 20 51.060 15.923 34.539 1.00 41.65 C ANISOU 144 CG ASN A 20 5284 5247 5293 162 -167 48 C ATOM 145 OD1 ASN A 20 52.183 16.332 34.858 1.00 45.25 O ANISOU 145 OD1 ASN A 20 5308 5599 6284 30 -123 -8 O ATOM 146 ND2 ASN A 20 50.497 14.852 35.090 1.00 46.19 N ANISOU 146 ND2 ASN A 20 5860 5755 5936 -20 132 171 N ATOM 147 N SER A 21 48.983 19.334 32.017 1.00 35.71 N ANISOU 147 N SER A 21 4493 4461 4613 71 -7 -168 N ATOM 148 CA SER A 21 48.591 19.918 30.747 1.00 36.77 C ANISOU 148 CA SER A 21 4702 4585 4681 85 -9 -110 C ATOM 149 C SER A 21 47.553 21.010 30.942 1.00 36.55 C ANISOU 149 C SER A 21 4647 4478 4761 135 18 -120 C ATOM 150 O SER A 21 46.618 20.821 31.701 1.00 36.04 O ANISOU 150 O SER A 21 4500 4284 4907 262 156 -201 O ATOM 151 CB SER A 21 47.931 18.860 29.881 1.00 38.08 C ANISOU 151 CB SER A 21 4972 4734 4759 70 -24 -195 C ATOM 152 OG SER A 21 47.544 19.432 28.653 1.00 41.52 O ANISOU 152 OG SER A 21 5604 5063 5105 138 -237 75 O ATOM 153 N ARG A 22 47.714 22.110 30.219 1.00 37.97 N ANISOU 153 N ARG A 22 4826 4764 4835 142 26 4 N ATOM 154 CA ARG A 22 46.699 23.192 30.131 1.00 38.56 C ANISOU 154 CA ARG A 22 4901 4835 4914 128 20 -16 C ATOM 155 C ARG A 22 45.285 22.695 30.071 1.00 38.28 C ANISOU 155 C ARG A 22 4899 4835 4811 95 -95 -98 C ATOM 156 O ARG A 22 44.367 23.312 30.620 1.00 37.44 O ANISOU 156 O ARG A 22 4886 4732 4607 254 -271 -237 O ATOM 157 CB ARG A 22 46.855 23.953 28.825 1.00 38.40 C ANISOU 157 CB ARG A 22 4874 4921 4795 151 6 -14 C ATOM 158 CG ARG A 22 47.825 25.045 28.851 1.00 39.58 C ANISOU 158 CG ARG A 22 5136 4886 5014 86 46 -5 C ATOM 159 CD ARG A 22 47.474 26.066 27.816 1.00 40.57 C ANISOU 159 CD ARG A 22 5167 5136 5111 54 -33 54 C ATOM 160 NE ARG A 22 47.226 25.495 26.504 1.00 41.19 N ANISOU 160 NE ARG A 22 5484 5136 5028 86 5 -165 N ATOM 161 CZ ARG A 22 47.508 26.121 25.361 1.00 44.06 C ANISOU 161 CZ ARG A 22 5654 5517 5567 -82 4 56 C ATOM 162 NH1 ARG A 22 48.034 27.339 25.370 1.00 45.31 N ANISOU 162 NH1 ARG A 22 5748 5531 5936 -5 12 -76 N ATOM 163 NH2 ARG A 22 47.261 25.530 24.191 1.00 43.34 N ANISOU 163 NH2 ARG A 22 5568 5589 5307 -72 176 -142 N ATOM 164 N SER A 23 45.114 21.605 29.322 1.00 38.41 N ANISOU 164 N SER A 23 5013 4748 4833 117 -64 -144 N ATOM 165 CA SER A 23 43.821 20.971 29.137 1.00 38.28 C ANISOU 165 CA SER A 23 4946 4747 4851 62 0 -113 C ATOM 166 C SER A 23 43.134 20.585 30.426 1.00 37.10 C ANISOU 166 C SER A 23 4754 4440 4903 9 -16 -117 C ATOM 167 O SER A 23 41.918 20.471 30.435 1.00 38.76 O ANISOU 167 O SER A 23 4921 4559 5245 -51 -145 -329 O ATOM 168 CB SER A 23 43.976 19.742 28.236 1.00 40.30 C ANISOU 168 CB SER A 23 5254 4943 5112 -43 4 -145 C ATOM 169 OG SER A 23 44.625 20.127 27.028 1.00 44.65 O ANISOU 169 OG SER A 23 5860 5970 5135 -107 -7 -90 O ATOM 170 N GLU A 24 43.897 20.418 31.507 1.00 35.13 N ANISOU 170 N GLU A 24 4422 4166 4759 -10 -34 -144 N ATOM 171 CA GLU A 24 43.343 20.157 32.820 1.00 34.55 C ANISOU 171 CA GLU A 24 4349 4114 4663 -1 -45 -103 C ATOM 172 C GLU A 24 42.658 21.364 33.458 1.00 33.16 C ANISOU 172 C GLU A 24 4152 3920 4527 -8 -28 -14 C ATOM 173 O GLU A 24 41.962 21.195 34.439 1.00 32.76 O ANISOU 173 O GLU A 24 4336 3581 4530 136 52 -57 O ATOM 174 CB GLU A 24 44.429 19.689 33.809 1.00 36.13 C ANISOU 174 CB GLU A 24 4493 4258 4977 4 -38 -92 C ATOM 175 CG GLU A 24 44.958 18.285 33.601 1.00 36.81 C ANISOU 175 CG GLU A 24 4561 4448 4975 -25 -101 -79 C ATOM 176 CD GLU A 24 46.110 17.961 34.542 1.00 36.65 C ANISOU 176 CD GLU A 24 4609 4418 4894 0 -38 5 C ATOM 177 OE1 GLU A 24 45.894 17.943 35.786 1.00 39.64 O ANISOU 177 OE1 GLU A 24 5255 4825 4980 -212 -160 79 O ATOM 178 OE2 GLU A 24 47.224 17.732 34.028 1.00 38.66 O ANISOU 178 OE2 GLU A 24 4435 4610 5644 99 42 -32 O ATOM 179 N CYS A 25 42.876 22.575 32.944 1.00 32.46 N ANISOU 179 N CYS A 25 3884 3972 4475 79 -116 -18 N ATOM 180 CA CYS A 25 42.396 23.779 33.646 1.00 30.17 C ANISOU 180 CA CYS A 25 3628 3708 4124 14 -95 -47 C ATOM 181 C CYS A 25 40.972 24.175 33.222 1.00 29.73 C ANISOU 181 C CYS A 25 3649 3622 4023 16 -48 -39 C ATOM 182 O CYS A 25 40.666 24.238 32.041 1.00 29.80 O ANISOU 182 O CYS A 25 3451 3661 4208 58 -289 86 O ATOM 183 CB CYS A 25 43.352 24.942 33.407 1.00 28.97 C ANISOU 183 CB CYS A 25 3390 3748 3868 118 -94 41 C ATOM 184 SG CYS A 25 45.039 24.513 33.866 1.00 26.84 S ANISOU 184 SG CYS A 25 2877 2873 4446 -31 -317 -238 S ATOM 185 N ASP A 26 40.131 24.462 34.210 1.00 30.02 N ANISOU 185 N ASP A 26 3671 3526 4208 36 10 47 N ATOM 186 CA ASP A 26 38.723 24.771 33.974 1.00 28.84 C ANISOU 186 CA ASP A 26 3577 3402 3979 65 -7 -25 C ATOM 187 C ASP A 26 38.549 26.303 33.967 1.00 28.06 C ANISOU 187 C ASP A 26 3419 3281 3960 72 26 -75 C ATOM 188 O ASP A 26 38.747 26.931 35.005 1.00 28.97 O ANISOU 188 O ASP A 26 3465 2973 4568 21 -68 -309 O ATOM 189 CB ASP A 26 37.873 24.150 35.087 1.00 29.35 C ANISOU 189 CB ASP A 26 3655 3421 4075 84 26 18 C ATOM 190 CG ASP A 26 36.355 24.333 34.865 1.00 32.52 C ANISOU 190 CG ASP A 26 3816 4060 4481 25 -81 151 C ATOM 191 OD1 ASP A 26 35.903 25.299 34.207 1.00 32.98 O ANISOU 191 OD1 ASP A 26 4088 3635 4805 -112 -75 318 O ATOM 192 OD2 ASP A 26 35.599 23.485 35.363 1.00 40.07 O ANISOU 192 OD2 ASP A 26 4927 4917 5380 -260 7 406 O ATOM 193 N THR A 27 38.155 26.858 32.826 1.00 27.61 N ANISOU 193 N THR A 27 3303 3204 3981 76 50 -94 N ATOM 194 CA THR A 27 37.926 28.323 32.642 1.00 27.37 C ANISOU 194 CA THR A 27 3305 3250 3844 21 34 -22 C ATOM 195 C THR A 27 36.458 28.814 32.806 1.00 26.59 C ANISOU 195 C THR A 27 3199 3140 3764 3 11 86 C ATOM 196 O THR A 27 36.135 29.980 32.506 1.00 24.14 O ANISOU 196 O THR A 27 2950 2706 3516 54 120 -143 O ATOM 197 CB THR A 27 38.345 28.757 31.250 1.00 27.47 C ANISOU 197 CB THR A 27 3373 3300 3764 76 10 -94 C ATOM 198 OG1 THR A 27 37.510 28.116 30.277 1.00 30.70 O ANISOU 198 OG1 THR A 27 3216 3757 4692 96 -140 -205 O ATOM 199 CG2 THR A 27 39.810 28.438 30.987 1.00 23.94 C ANISOU 199 CG2 THR A 27 3069 3191 2837 142 -116 -360 C ATOM 200 N THR A 28 35.572 27.937 33.263 1.00 25.87 N ANISOU 200 N THR A 28 3110 3037 3681 -105 44 255 N ATOM 201 CA THR A 28 34.145 28.285 33.344 1.00 25.92 C ANISOU 201 CA THR A 28 3185 3141 3522 -63 -14 174 C ATOM 202 C THR A 28 33.861 29.263 34.463 1.00 26.69 C ANISOU 202 C THR A 28 3252 3227 3660 -73 -45 162 C ATOM 203 O THR A 28 34.622 29.363 35.451 1.00 26.68 O ANISOU 203 O THR A 28 2955 3053 4127 118 -316 405 O ATOM 204 CB THR A 28 33.248 27.041 33.559 1.00 25.13 C ANISOU 204 CB THR A 28 3078 3202 3266 -68 -80 145 C ATOM 205 OG1 THR A 28 33.541 26.448 34.839 1.00 25.67 O ANISOU 205 OG1 THR A 28 3384 3107 3261 156 -368 211 O ATOM 206 CG2 THR A 28 33.467 26.051 32.477 1.00 23.30 C ANISOU 206 CG2 THR A 28 2534 3023 3293 -61 -80 52 C ATOM 207 N VAL A 29 32.759 29.996 34.297 1.00 26.63 N ANISOU 207 N VAL A 29 3133 3310 3672 -110 -101 104 N ATOM 208 CA VAL A 29 32.206 30.867 35.342 1.00 26.04 C ANISOU 208 CA VAL A 29 3225 3241 3426 -119 -72 42 C ATOM 209 C VAL A 29 30.667 30.841 35.353 1.00 24.60 C ANISOU 209 C VAL A 29 3107 2980 3258 6 -70 98 C ATOM 210 O VAL A 29 30.046 30.581 34.323 1.00 26.70 O ANISOU 210 O VAL A 29 3395 3095 3655 -64 -136 140 O ATOM 211 CB VAL A 29 32.744 32.328 35.191 1.00 27.32 C ANISOU 211 CB VAL A 29 3377 3336 3666 -59 -47 47 C ATOM 212 CG1 VAL A 29 32.186 33.012 33.954 1.00 26.84 C ANISOU 212 CG1 VAL A 29 3477 3098 3622 -250 217 246 C ATOM 213 CG2 VAL A 29 32.505 33.131 36.456 1.00 27.75 C ANISOU 213 CG2 VAL A 29 3362 3375 3806 -78 -80 45 C ATOM 214 N THR A 30 30.084 31.048 36.527 1.00 24.75 N ANISOU 214 N THR A 30 3141 2865 3396 -17 -74 -63 N ATOM 215 CA THR A 30 28.619 31.151 36.729 1.00 25.08 C ANISOU 215 CA THR A 30 3131 3133 3263 -12 -123 -18 C ATOM 216 C THR A 30 28.247 32.611 37.015 1.00 25.30 C ANISOU 216 C THR A 30 3062 3198 3349 -4 -130 31 C ATOM 217 O THR A 30 28.934 33.322 37.762 1.00 26.29 O ANISOU 217 O THR A 30 2894 3228 3866 -12 -215 10 O ATOM 218 CB THR A 30 28.113 30.252 37.923 1.00 26.47 C ANISOU 218 CB THR A 30 3190 3306 3558 8 -9 -9 C ATOM 219 OG1 THR A 30 28.392 28.861 37.680 1.00 27.27 O ANISOU 219 OG1 THR A 30 3705 2972 3683 -111 -132 232 O ATOM 220 CG2 THR A 30 26.632 30.383 38.164 1.00 25.70 C ANISOU 220 CG2 THR A 30 3248 3206 3308 27 -41 -30 C ATOM 221 N LEU A 31 27.142 33.046 36.425 1.00 24.88 N ANISOU 221 N LEU A 31 2950 3219 3283 -109 -79 32 N ATOM 222 CA LEU A 31 26.567 34.356 36.665 1.00 25.19 C ANISOU 222 CA LEU A 31 3164 3086 3319 -73 -66 -27 C ATOM 223 C LEU A 31 25.074 34.137 36.827 1.00 25.34 C ANISOU 223 C LEU A 31 3235 2935 3458 -28 -62 59 C ATOM 224 O LEU A 31 24.390 33.732 35.888 1.00 26.34 O ANISOU 224 O LEU A 31 3171 3000 3836 13 -218 51 O ATOM 225 CB LEU A 31 26.858 35.307 35.493 1.00 24.37 C ANISOU 225 CB LEU A 31 3012 3086 3161 -101 -158 -13 C ATOM 226 CG LEU A 31 26.446 36.781 35.615 1.00 24.13 C ANISOU 226 CG LEU A 31 2996 3221 2948 -112 -30 -103 C ATOM 227 CD1 LEU A 31 27.284 37.484 36.709 1.00 24.69 C ANISOU 227 CD1 LEU A 31 3177 3317 2887 -260 0 -22 C ATOM 228 CD2 LEU A 31 26.551 37.547 34.265 1.00 24.10 C ANISOU 228 CD2 LEU A 31 3089 2927 3140 -76 -24 -84 C ATOM 229 N GLY A 32 24.590 34.362 38.037 1.00 28.24 N ANISOU 229 N GLY A 32 3400 3288 4041 -63 92 -75 N ATOM 230 CA GLY A 32 23.222 34.004 38.394 1.00 29.78 C ANISOU 230 CA GLY A 32 3591 3660 4061 -61 72 -22 C ATOM 231 C GLY A 32 23.034 32.509 38.264 1.00 30.24 C ANISOU 231 C GLY A 32 3762 3612 4113 -139 59 80 C ATOM 232 O GLY A 32 23.821 31.737 38.799 1.00 31.47 O ANISOU 232 O GLY A 32 3974 3757 4224 -229 30 120 O ATOM 233 N LYS A 33 22.029 32.111 37.495 1.00 32.50 N ANISOU 233 N LYS A 33 4137 3870 4339 -112 26 13 N ATOM 234 CA LYS A 33 21.614 30.695 37.395 1.00 33.45 C ANISOU 234 CA LYS A 33 4245 4032 4431 -107 28 -31 C ATOM 235 C LYS A 33 22.259 29.911 36.252 1.00 33.67 C ANISOU 235 C LYS A 33 4254 4012 4526 -106 64 -61 C ATOM 236 O LYS A 33 21.931 28.742 36.059 1.00 35.63 O ANISOU 236 O LYS A 33 4457 4163 4915 -216 64 -87 O ATOM 237 CB LYS A 33 20.096 30.630 37.226 1.00 35.56 C ANISOU 237 CB LYS A 33 4473 4269 4768 -138 21 44 C ATOM 238 CG LYS A 33 19.332 30.988 38.494 1.00 38.34 C ANISOU 238 CG LYS A 33 4815 4881 4869 -76 88 -34 C ATOM 239 CD LYS A 33 17.900 31.383 38.126 1.00 38.41 C ANISOU 239 CD LYS A 33 4737 4897 4959 20 64 -92 C ATOM 240 CE LYS A 33 17.025 31.500 39.361 1.00 41.80 C ANISOU 240 CE LYS A 33 5031 5457 5394 7 311 -95 C ATOM 241 NZ LYS A 33 15.895 32.451 39.100 1.00 47.74 N ANISOU 241 NZ LYS A 33 5558 6152 6427 311 75 48 N ATOM 242 N HIS A 34 23.169 30.529 35.499 1.00 31.70 N ANISOU 242 N HIS A 34 4004 3799 4240 -104 -17 -17 N ATOM 243 CA HIS A 34 23.767 29.871 34.363 1.00 30.10 C ANISOU 243 CA HIS A 34 3695 3682 4058 -94 -43 9 C ATOM 244 C HIS A 34 25.298 29.833 34.417 1.00 29.23 C ANISOU 244 C HIS A 34 3598 3558 3951 -54 -117 -34 C ATOM 245 O HIS A 34 25.945 30.732 34.944 1.00 25.94 O ANISOU 245 O HIS A 34 2680 3132 4044 -94 -152 82 O ATOM 246 CB HIS A 34 23.292 30.523 33.069 1.00 30.45 C ANISOU 246 CB HIS A 34 3880 3755 3935 -221 -33 1 C ATOM 247 CG HIS A 34 21.799 30.616 32.960 1.00 33.53 C ANISOU 247 CG HIS A 34 4130 4180 4430 -117 75 63 C ATOM 248 ND1 HIS A 34 21.061 31.561 33.642 1.00 37.51 N ANISOU 248 ND1 HIS A 34 4564 4581 5106 -90 -29 -38 N ATOM 249 CD2 HIS A 34 20.902 29.846 32.294 1.00 36.24 C ANISOU 249 CD2 HIS A 34 4453 4805 4510 -18 -206 -179 C ATOM 250 CE1 HIS A 34 19.779 31.382 33.388 1.00 40.36 C ANISOU 250 CE1 HIS A 34 4633 5106 5593 125 -85 -146 C ATOM 251 NE2 HIS A 34 19.654 30.348 32.574 1.00 40.29 N ANISOU 251 NE2 HIS A 34 4626 5344 5338 -25 -174 -298 N ATOM 252 N LYS A 35 25.841 28.767 33.837 1.00 29.52 N ANISOU 252 N LYS A 35 3602 3577 4034 -60 -59 -64 N ATOM 253 CA LYS A 35 27.277 28.543 33.724 1.00 29.17 C ANISOU 253 CA LYS A 35 3600 3569 3911 -71 -62 -42 C ATOM 254 C LYS A 35 27.718 28.784 32.284 1.00 28.05 C ANISOU 254 C LYS A 35 3403 3349 3905 20 -32 -97 C ATOM 255 O LYS A 35 27.028 28.372 31.325 1.00 28.40 O ANISOU 255 O LYS A 35 3450 3246 4093 -81 -123 -118 O ATOM 256 CB LYS A 35 27.587 27.118 34.158 1.00 30.10 C ANISOU 256 CB LYS A 35 3640 3657 4139 -81 -80 -6 C ATOM 257 CG LYS A 35 29.013 26.842 34.482 1.00 31.74 C ANISOU 257 CG LYS A 35 3924 3805 4329 1 -72 22 C ATOM 258 CD LYS A 35 29.097 25.572 35.330 1.00 32.01 C ANISOU 258 CD LYS A 35 4084 3915 4161 -27 -53 132 C ATOM 259 CE LYS A 35 30.459 24.935 35.248 1.00 33.33 C ANISOU 259 CE LYS A 35 4117 3949 4594 136 -51 131 C ATOM 260 NZ LYS A 35 30.579 23.971 36.386 1.00 35.88 N ANISOU 260 NZ LYS A 35 4446 4619 4565 267 0 123 N ATOM 261 N PHE A 36 28.857 29.463 32.115 1.00 26.61 N ANISOU 261 N PHE A 36 3250 3093 3768 -24 -83 -156 N ATOM 262 CA PHE A 36 29.395 29.765 30.779 1.00 25.43 C ANISOU 262 CA PHE A 36 3095 3161 3405 26 -121 -102 C ATOM 263 C PHE A 36 30.851 29.322 30.640 1.00 24.25 C ANISOU 263 C PHE A 36 2963 3084 3164 18 -94 -72 C ATOM 264 O PHE A 36 31.559 29.141 31.630 1.00 23.85 O ANISOU 264 O PHE A 36 2706 3205 3150 15 -74 -327 O ATOM 265 CB PHE A 36 29.289 31.262 30.438 1.00 24.66 C ANISOU 265 CB PHE A 36 2726 3291 3351 129 -155 -56 C ATOM 266 CG PHE A 36 27.920 31.836 30.662 1.00 22.71 C ANISOU 266 CG PHE A 36 2596 2949 3081 -14 -24 19 C ATOM 267 CD1 PHE A 36 26.954 31.774 29.656 1.00 22.57 C ANISOU 267 CD1 PHE A 36 2882 3062 2632 -106 70 173 C ATOM 268 CD2 PHE A 36 27.575 32.397 31.886 1.00 26.06 C ANISOU 268 CD2 PHE A 36 3014 3563 3324 -84 -6 -189 C ATOM 269 CE1 PHE A 36 25.665 32.294 29.870 1.00 21.70 C ANISOU 269 CE1 PHE A 36 2851 2538 2853 96 -129 -134 C ATOM 270 CE2 PHE A 36 26.290 32.912 32.105 1.00 25.85 C ANISOU 270 CE2 PHE A 36 3211 3178 3432 63 -96 47 C ATOM 271 CZ PHE A 36 25.339 32.845 31.108 1.00 21.52 C ANISOU 271 CZ PHE A 36 2873 2580 2722 -148 128 118 C ATOM 272 N LYS A 37 31.265 29.158 29.391 1.00 23.98 N ANISOU 272 N LYS A 37 2979 3196 2933 -18 -132 -128 N ATOM 273 CA LYS A 37 32.561 28.603 29.021 1.00 25.63 C ANISOU 273 CA LYS A 37 3157 3306 3273 -38 -115 -89 C ATOM 274 C LYS A 37 33.729 29.470 29.501 1.00 26.44 C ANISOU 274 C LYS A 37 3213 3241 3592 -65 -148 -84 C ATOM 275 O LYS A 37 34.753 28.932 29.930 1.00 27.27 O ANISOU 275 O LYS A 37 3157 3227 3975 -131 -289 -158 O ATOM 276 CB LYS A 37 32.672 28.481 27.484 1.00 26.67 C ANISOU 276 CB LYS A 37 3287 3487 3358 -109 -22 109 C ATOM 277 CG LYS A 37 32.021 27.247 26.888 1.00 30.71 C ANISOU 277 CG LYS A 37 3974 3973 3720 -29 -6 4 C ATOM 278 CD LYS A 37 32.407 27.096 25.419 1.00 30.05 C ANISOU 278 CD LYS A 37 4101 3811 3503 -61 -97 -190 C ATOM 279 CE LYS A 37 32.315 25.662 24.918 1.00 35.61 C ANISOU 279 CE LYS A 37 4793 4052 4682 -91 -92 -157 C ATOM 280 NZ LYS A 37 31.030 25.318 24.211 1.00 35.65 N ANISOU 280 NZ LYS A 37 4429 4639 4475 126 -53 -80 N ATOM 281 N LEU A 38 33.556 30.793 29.394 1.00 25.70 N ANISOU 281 N LEU A 38 3136 3087 3539 -88 -120 -28 N ATOM 282 CA LEU A 38 34.621 31.795 29.619 1.00 23.24 C ANISOU 282 CA LEU A 38 2871 2919 3038 9 -146 -170 C ATOM 283 C LEU A 38 34.069 32.969 30.401 1.00 22.38 C ANISOU 283 C LEU A 38 2650 2770 3081 -5 -169 -151 C ATOM 284 O LEU A 38 32.896 33.284 30.257 1.00 21.96 O ANISOU 284 O LEU A 38 2498 2793 3052 -97 -101 -102 O ATOM 285 CB LEU A 38 35.146 32.367 28.285 1.00 23.43 C ANISOU 285 CB LEU A 38 2970 2848 3081 26 -206 -96 C ATOM 286 CG LEU A 38 36.013 31.510 27.376 1.00 27.26 C ANISOU 286 CG LEU A 38 3460 3593 3303 44 58 35 C ATOM 287 CD1 LEU A 38 36.254 32.189 26.011 1.00 25.79 C ANISOU 287 CD1 LEU A 38 3453 3242 3102 57 -84 -29 C ATOM 288 CD2 LEU A 38 37.353 31.149 28.038 1.00 31.40 C ANISOU 288 CD2 LEU A 38 3809 4034 4087 -6 -187 -65 C ATOM 289 N PRO A 39 34.928 33.653 31.196 1.00 20.68 N ANISOU 289 N PRO A 39 2563 2529 2765 45 -174 -164 N ATOM 290 CA PRO A 39 34.559 34.890 31.880 1.00 20.07 C ANISOU 290 CA PRO A 39 2489 2568 2569 65 -130 -150 C ATOM 291 C PRO A 39 34.709 36.151 31.012 1.00 19.54 C ANISOU 291 C PRO A 39 2575 2526 2323 3 -94 -202 C ATOM 292 O PRO A 39 35.201 37.163 31.468 1.00 18.70 O ANISOU 292 O PRO A 39 2909 2759 1434 -69 -398 -216 O ATOM 293 CB PRO A 39 35.527 34.914 33.035 1.00 18.66 C ANISOU 293 CB PRO A 39 2557 2110 2422 28 -142 -126 C ATOM 294 CG PRO A 39 36.784 34.398 32.405 1.00 20.68 C ANISOU 294 CG PRO A 39 2581 2497 2775 -71 -244 -156 C ATOM 295 CD PRO A 39 36.323 33.278 31.505 1.00 19.99 C ANISOU 295 CD PRO A 39 2624 2443 2526 32 -121 -191 C ATOM 296 N VAL A 40 34.316 36.075 29.744 1.00 19.48 N ANISOU 296 N VAL A 40 2381 2660 2361 66 -277 -151 N ATOM 297 CA VAL A 40 34.360 37.203 28.820 1.00 22.19 C ANISOU 297 CA VAL A 40 2639 2860 2932 -33 -159 3 C ATOM 298 C VAL A 40 33.023 37.348 28.078 1.00 22.90 C ANISOU 298 C VAL A 40 2806 2929 2963 -81 -278 -18 C ATOM 299 O VAL A 40 32.284 36.364 27.875 1.00 22.54 O ANISOU 299 O VAL A 40 2787 3002 2772 -308 -208 -13 O ATOM 300 CB VAL A 40 35.438 37.081 27.683 1.00 21.82 C ANISOU 300 CB VAL A 40 2655 2861 2772 34 -93 -31 C ATOM 301 CG1 VAL A 40 36.885 36.886 28.255 1.00 20.29 C ANISOU 301 CG1 VAL A 40 2492 2832 2382 -59 65 10 C ATOM 302 CG2 VAL A 40 35.099 35.993 26.709 1.00 25.55 C ANISOU 302 CG2 VAL A 40 2878 3269 3559 -88 -374 -51 C ATOM 303 N VAL A 41 32.765 38.575 27.651 1.00 21.66 N ANISOU 303 N VAL A 41 2811 2787 2631 -24 -276 -23 N ATOM 304 CA VAL A 41 31.529 38.926 26.969 1.00 22.73 C ANISOU 304 CA VAL A 41 2847 2771 3015 -21 -192 -101 C ATOM 305 C VAL A 41 31.806 40.087 26.009 1.00 23.17 C ANISOU 305 C VAL A 41 2897 2931 2973 -29 -105 -83 C ATOM 306 O VAL A 41 32.478 41.083 26.363 1.00 22.40 O ANISOU 306 O VAL A 41 2776 2742 2991 -40 -284 -162 O ATOM 307 CB VAL A 41 30.373 39.243 27.969 1.00 21.52 C ANISOU 307 CB VAL A 41 2780 2596 2801 -70 -235 43 C ATOM 308 CG1 VAL A 41 30.694 40.435 28.853 1.00 20.31 C ANISOU 308 CG1 VAL A 41 2754 2730 2230 -13 -186 151 C ATOM 309 CG2 VAL A 41 29.031 39.453 27.211 1.00 17.92 C ANISOU 309 CG2 VAL A 41 2765 2752 1289 -9 -156 -17 C ATOM 310 N PRO A 42 31.301 39.975 24.779 1.00 23.74 N ANISOU 310 N PRO A 42 2962 2959 3097 -32 -68 -127 N ATOM 311 CA PRO A 42 31.455 41.062 23.841 1.00 24.45 C ANISOU 311 CA PRO A 42 3043 3090 3157 2 -110 -72 C ATOM 312 C PRO A 42 30.712 42.307 24.278 1.00 23.12 C ANISOU 312 C PRO A 42 2882 3028 2874 38 -169 -66 C ATOM 313 O PRO A 42 29.671 42.207 24.956 1.00 24.66 O ANISOU 313 O PRO A 42 3029 3377 2960 -54 -256 -224 O ATOM 314 CB PRO A 42 30.839 40.508 22.560 1.00 25.85 C ANISOU 314 CB PRO A 42 3258 3210 3352 89 -58 -195 C ATOM 315 CG PRO A 42 30.812 39.053 22.759 1.00 26.54 C ANISOU 315 CG PRO A 42 3502 3206 3373 -133 -50 14 C ATOM 316 CD PRO A 42 30.606 38.826 24.174 1.00 23.96 C ANISOU 316 CD PRO A 42 2775 3157 3170 -66 -140 -232 C ATOM 317 N ALA A 43 31.250 43.460 23.901 1.00 22.26 N ANISOU 317 N ALA A 43 2731 2917 2807 -26 -373 -79 N ATOM 318 CA ALA A 43 30.584 44.745 24.159 1.00 22.76 C ANISOU 318 CA ALA A 43 2841 2997 2808 37 -212 -92 C ATOM 319 C ALA A 43 29.178 44.723 23.573 1.00 23.09 C ANISOU 319 C ALA A 43 2904 3047 2822 95 -186 -142 C ATOM 320 O ALA A 43 28.979 44.288 22.405 1.00 21.48 O ANISOU 320 O ALA A 43 2806 3253 2099 235 -587 102 O ATOM 321 CB ALA A 43 31.387 45.901 23.528 1.00 21.74 C ANISOU 321 CB ALA A 43 2871 2906 2483 36 -401 -70 C ATOM 322 N ASN A 44 28.215 45.218 24.355 1.00 23.92 N ANISOU 322 N ASN A 44 3073 3228 2785 21 -173 103 N ATOM 323 CA ASN A 44 26.822 45.272 23.908 1.00 25.11 C ANISOU 323 CA ASN A 44 2997 3244 3299 -44 -141 -47 C ATOM 324 C ASN A 44 26.553 46.486 23.006 1.00 26.01 C ANISOU 324 C ASN A 44 3082 3340 3460 -43 -260 -9 C ATOM 325 O ASN A 44 25.799 47.385 23.372 1.00 28.08 O ANISOU 325 O ASN A 44 3368 3542 3758 -78 -191 -146 O ATOM 326 CB ASN A 44 25.854 45.192 25.084 1.00 24.17 C ANISOU 326 CB ASN A 44 2969 3099 3115 -11 -192 -101 C ATOM 327 CG ASN A 44 26.069 46.273 26.133 1.00 22.54 C ANISOU 327 CG ASN A 44 2554 3042 2966 -49 23 -243 C ATOM 328 OD1 ASN A 44 27.203 46.619 26.499 1.00 22.60 O ANISOU 328 OD1 ASN A 44 2787 3071 2729 47 -182 -347 O ATOM 329 ND2 ASN A 44 24.969 46.807 26.631 1.00 20.57 N ANISOU 329 ND2 ASN A 44 2744 2594 2478 -102 -221 -265 N ATOM 330 N MET A 45 27.193 46.487 21.840 1.00 27.55 N ANISOU 330 N MET A 45 3312 3592 3563 -30 -135 0 N ATOM 331 CA MET A 45 27.094 47.568 20.832 1.00 31.30 C ANISOU 331 CA MET A 45 3993 4012 3888 -3 -94 127 C ATOM 332 C MET A 45 26.910 46.973 19.451 1.00 31.35 C ANISOU 332 C MET A 45 4027 4038 3845 4 -45 59 C ATOM 333 O MET A 45 27.445 45.896 19.164 1.00 28.93 O ANISOU 333 O MET A 45 3627 4113 3252 242 -209 145 O ATOM 334 CB MET A 45 28.373 48.396 20.742 1.00 32.34 C ANISOU 334 CB MET A 45 4145 4146 3993 21 -72 204 C ATOM 335 CG MET A 45 28.869 48.968 22.014 1.00 34.33 C ANISOU 335 CG MET A 45 4484 4333 4224 -102 4 -2 C ATOM 336 SD MET A 45 30.614 49.443 21.880 1.00 37.65 S ANISOU 336 SD MET A 45 4812 4964 4526 -379 -206 154 S ATOM 337 CE MET A 45 30.605 50.778 23.074 1.00 38.65 C ANISOU 337 CE MET A 45 4891 4871 4922 -79 -28 -98 C ATOM 338 N GLN A 46 26.213 47.714 18.582 1.00 32.96 N ANISOU 338 N GLN A 46 4258 4224 4040 66 -144 69 N ATOM 339 CA GLN A 46 25.888 47.212 17.244 1.00 35.26 C ANISOU 339 CA GLN A 46 4529 4521 4345 40 -112 36 C ATOM 340 C GLN A 46 27.086 47.062 16.291 1.00 34.37 C ANISOU 340 C GLN A 46 4402 4336 4320 68 -149 110 C ATOM 341 O GLN A 46 27.011 46.344 15.301 1.00 34.24 O ANISOU 341 O GLN A 46 4502 4398 4109 163 -227 196 O ATOM 342 CB GLN A 46 24.760 48.033 16.590 1.00 36.32 C ANISOU 342 CB GLN A 46 4637 4670 4490 91 -105 43 C ATOM 343 CG GLN A 46 25.097 49.466 16.271 1.00 39.86 C ANISOU 343 CG GLN A 46 5167 4930 5048 0 -127 147 C ATOM 344 CD GLN A 46 24.293 50.025 15.080 1.00 41.11 C ANISOU 344 CD GLN A 46 5278 5234 5108 129 -149 220 C ATOM 345 OE1 GLN A 46 23.707 49.268 14.274 1.00 50.04 O ANISOU 345 OE1 GLN A 46 6472 6268 6273 -250 -214 -147 O ATOM 346 NE2 GLN A 46 24.274 51.356 14.962 1.00 45.68 N ANISOU 346 NE2 GLN A 46 5924 5411 6019 -29 -164 54 N ATOM 347 N THR A 47 28.182 47.739 16.600 1.00 34.53 N ANISOU 347 N THR A 47 4382 4296 4440 68 -155 137 N ATOM 348 CA THR A 47 29.438 47.563 15.883 1.00 34.61 C ANISOU 348 CA THR A 47 4469 4409 4272 19 -71 102 C ATOM 349 C THR A 47 30.184 46.264 16.255 1.00 34.95 C ANISOU 349 C THR A 47 4382 4477 4420 25 6 36 C ATOM 350 O THR A 47 31.157 45.905 15.596 1.00 36.52 O ANISOU 350 O THR A 47 4425 4730 4718 49 -27 10 O ATOM 351 CB THR A 47 30.362 48.761 16.163 1.00 36.26 C ANISOU 351 CB THR A 47 4620 4661 4496 -8 9 148 C ATOM 352 OG1 THR A 47 30.513 48.951 17.582 1.00 40.02 O ANISOU 352 OG1 THR A 47 5124 5188 4895 -76 -150 -81 O ATOM 353 CG2 THR A 47 29.781 50.020 15.565 1.00 36.90 C ANISOU 353 CG2 THR A 47 4619 4605 4792 36 52 102 C ATOM 354 N ILE A 48 29.722 45.565 17.298 1.00 33.48 N ANISOU 354 N ILE A 48 4110 4324 4287 36 -96 57 N ATOM 355 CA ILE A 48 30.401 44.369 17.835 1.00 32.37 C ANISOU 355 CA ILE A 48 4087 4161 4049 -31 -67 42 C ATOM 356 C ILE A 48 29.514 43.118 17.800 1.00 31.72 C ANISOU 356 C ILE A 48 4021 4194 3834 61 -134 -58 C ATOM 357 O ILE A 48 29.960 42.046 17.412 1.00 32.06 O ANISOU 357 O ILE A 48 4110 4276 3795 111 -334 -12 O ATOM 358 CB ILE A 48 30.881 44.678 19.293 1.00 31.99 C ANISOU 358 CB ILE A 48 4034 4082 4037 -60 7 51 C ATOM 359 CG1 ILE A 48 31.805 45.907 19.308 1.00 30.18 C ANISOU 359 CG1 ILE A 48 3876 4073 3515 -73 -128 -40 C ATOM 360 CG2 ILE A 48 31.550 43.474 19.962 1.00 31.94 C ANISOU 360 CG2 ILE A 48 3913 4133 4087 -54 -25 25 C ATOM 361 CD1 ILE A 48 33.115 45.740 18.556 1.00 32.09 C ANISOU 361 CD1 ILE A 48 3837 4315 4041 117 -84 -12 C ATOM 362 N ILE A 49 28.264 43.236 18.221 1.00 31.82 N ANISOU 362 N ILE A 49 4018 4206 3864 19 -200 -14 N ATOM 363 CA ILE A 49 27.368 42.083 18.274 1.00 31.51 C ANISOU 363 CA ILE A 49 3992 4055 3923 17 -108 17 C ATOM 364 C ILE A 49 26.106 42.282 17.426 1.00 32.10 C ANISOU 364 C ILE A 49 4163 4122 3909 6 -191 12 C ATOM 365 O ILE A 49 25.656 43.402 17.214 1.00 30.63 O ANISOU 365 O ILE A 49 4077 4021 3540 21 -367 7 O ATOM 366 CB ILE A 49 26.985 41.701 19.744 1.00 30.79 C ANISOU 366 CB ILE A 49 3806 3902 3988 97 -116 -24 C ATOM 367 CG1 ILE A 49 26.191 40.385 19.773 1.00 30.63 C ANISOU 367 CG1 ILE A 49 3723 3934 3979 -36 -23 120 C ATOM 368 CG2 ILE A 49 26.253 42.854 20.495 1.00 27.62 C ANISOU 368 CG2 ILE A 49 3616 3582 3297 71 -92 -27 C ATOM 369 CD1 ILE A 49 26.252 39.686 21.067 1.00 30.08 C ANISOU 369 CD1 ILE A 49 3633 4043 3751 -1 -124 24 C ATOM 370 N ASP A 50 25.567 41.168 16.935 1.00 32.74 N ANISOU 370 N ASP A 50 4264 4233 3939 -48 -178 -45 N ATOM 371 CA ASP A 50 24.272 41.163 16.265 1.00 33.96 C ANISOU 371 CA ASP A 50 4281 4382 4240 -32 -121 -13 C ATOM 372 C ASP A 50 23.539 39.858 16.574 1.00 35.00 C ANISOU 372 C ASP A 50 4434 4494 4368 -65 -144 16 C ATOM 373 O ASP A 50 24.023 39.041 17.357 1.00 34.16 O ANISOU 373 O ASP A 50 4417 4618 3942 -42 -233 -117 O ATOM 374 CB ASP A 50 24.436 41.404 14.742 1.00 33.98 C ANISOU 374 CB ASP A 50 4366 4427 4116 -36 -128 37 C ATOM 375 CG ASP A 50 25.188 40.276 14.007 1.00 36.10 C ANISOU 375 CG ASP A 50 4455 4663 4597 -80 -94 20 C ATOM 376 OD1 ASP A 50 25.343 39.148 14.524 1.00 38.58 O ANISOU 376 OD1 ASP A 50 5079 4889 4688 64 -464 122 O ATOM 377 OD2 ASP A 50 25.613 40.522 12.859 1.00 39.10 O ANISOU 377 OD2 ASP A 50 4963 5237 4656 109 -116 26 O ATOM 378 N GLU A 51 22.389 39.638 15.937 1.00 35.35 N ANISOU 378 N GLU A 51 4387 4568 4476 -3 -185 50 N ATOM 379 CA GLU A 51 21.583 38.457 16.240 1.00 34.69 C ANISOU 379 CA GLU A 51 4339 4439 4402 -24 -140 -4 C ATOM 380 C GLU A 51 22.244 37.135 15.858 1.00 34.27 C ANISOU 380 C GLU A 51 4299 4421 4298 -79 -195 -22 C ATOM 381 O GLU A 51 22.075 36.155 16.575 1.00 33.38 O ANISOU 381 O GLU A 51 4374 4189 4119 -29 -448 22 O ATOM 382 CB GLU A 51 20.201 38.548 15.597 1.00 36.41 C ANISOU 382 CB GLU A 51 4538 4628 4667 -26 -112 30 C ATOM 383 CG GLU A 51 19.365 39.725 16.098 1.00 38.32 C ANISOU 383 CG GLU A 51 4789 4841 4927 62 -128 -206 C ATOM 384 CD GLU A 51 19.652 41.032 15.348 1.00 43.48 C ANISOU 384 CD GLU A 51 5607 5550 5361 -129 -91 141 C ATOM 385 OE1 GLU A 51 20.650 41.100 14.589 1.00 44.68 O ANISOU 385 OE1 GLU A 51 5458 5967 5551 84 -232 81 O ATOM 386 OE2 GLU A 51 18.875 42.001 15.541 1.00 50.08 O ANISOU 386 OE2 GLU A 51 6205 6238 6584 109 -298 -3 O ATOM 387 N ARG A 52 22.954 37.094 14.726 1.00 34.21 N ANISOU 387 N ARG A 52 4167 4431 4397 -17 -174 -25 N ATOM 388 CA ARG A 52 23.659 35.868 14.316 1.00 33.98 C ANISOU 388 CA ARG A 52 4210 4365 4334 -38 -209 -31 C ATOM 389 C ARG A 52 24.773 35.542 15.320 1.00 32.52 C ANISOU 389 C ARG A 52 4159 4120 4077 -52 -269 33 C ATOM 390 O ARG A 52 24.921 34.399 15.736 1.00 33.21 O ANISOU 390 O ARG A 52 4225 4146 4245 -163 -512 32 O ATOM 391 CB ARG A 52 24.323 35.993 12.941 1.00 36.00 C ANISOU 391 CB ARG A 52 4576 4575 4525 -38 -33 23 C ATOM 392 CG ARG A 52 23.429 36.355 11.759 1.00 39.91 C ANISOU 392 CG ARG A 52 5064 5198 4901 -35 -234 29 C ATOM 393 CD ARG A 52 22.241 35.430 11.596 1.00 45.86 C ANISOU 393 CD ARG A 52 5680 5592 6152 -125 129 -11 C ATOM 394 NE ARG A 52 21.623 35.641 10.277 1.00 42.89 N ANISOU 394 NE ARG A 52 5340 5710 5244 -192 -349 20 N ATOM 395 CZ ARG A 52 20.354 35.390 9.966 1.00 45.82 C ANISOU 395 CZ ARG A 52 5677 5927 5804 -76 -70 -29 C ATOM 396 NH1 ARG A 52 19.509 34.907 10.878 1.00 45.14 N ANISOU 396 NH1 ARG A 52 5534 5767 5850 -2 -21 12 N ATOM 397 NH2 ARG A 52 19.934 35.636 8.718 1.00 46.94 N ANISOU 397 NH2 ARG A 52 5985 5840 6008 -114 -181 162 N ATOM 398 N ILE A 53 25.583 36.541 15.662 1.00 30.41 N ANISOU 398 N ILE A 53 3892 3912 3750 22 -141 8 N ATOM 399 CA ILE A 53 26.649 36.327 16.658 1.00 30.08 C ANISOU 399 CA ILE A 53 3789 3881 3758 -30 -74 -50 C ATOM 400 C ILE A 53 26.070 35.880 18.028 1.00 28.95 C ANISOU 400 C ILE A 53 3684 3767 3546 -74 -165 -81 C ATOM 401 O ILE A 53 26.580 34.929 18.633 1.00 30.52 O ANISOU 401 O ILE A 53 3701 3980 3913 -101 -274 -186 O ATOM 402 CB ILE A 53 27.580 37.550 16.788 1.00 30.01 C ANISOU 402 CB ILE A 53 3839 3827 3735 27 -3 -62 C ATOM 403 CG1 ILE A 53 28.376 37.740 15.492 1.00 29.50 C ANISOU 403 CG1 ILE A 53 3737 3938 3533 -184 -112 -32 C ATOM 404 CG2 ILE A 53 28.558 37.360 17.961 1.00 30.51 C ANISOU 404 CG2 ILE A 53 3814 3974 3802 12 -109 -48 C ATOM 405 CD1 ILE A 53 29.009 39.099 15.310 1.00 29.72 C ANISOU 405 CD1 ILE A 53 3984 3768 3539 -42 -120 -135 C ATOM 406 N ALA A 54 24.985 36.510 18.477 1.00 28.63 N ANISOU 406 N ALA A 54 3700 3762 3412 -59 -201 -111 N ATOM 407 CA ALA A 54 24.311 36.132 19.750 1.00 28.89 C ANISOU 407 CA ALA A 54 3672 3720 3585 -65 -113 -46 C ATOM 408 C ALA A 54 23.788 34.691 19.785 1.00 30.15 C ANISOU 408 C ALA A 54 3853 3853 3749 -67 -107 -43 C ATOM 409 O ALA A 54 23.818 33.999 20.843 1.00 28.38 O ANISOU 409 O ALA A 54 3398 3666 3716 -97 -225 -43 O ATOM 410 CB ALA A 54 23.175 37.114 20.051 1.00 28.55 C ANISOU 410 CB ALA A 54 3664 3769 3414 -66 -145 -80 C ATOM 411 N THR A 55 23.294 34.240 18.635 1.00 31.34 N ANISOU 411 N THR A 55 4017 3883 4006 -131 -143 -31 N ATOM 412 CA THR A 55 22.819 32.857 18.490 1.00 31.30 C ANISOU 412 CA THR A 55 4050 3854 3989 -57 -191 -87 C ATOM 413 C THR A 55 23.982 31.843 18.544 1.00 30.63 C ANISOU 413 C THR A 55 3985 3818 3832 -84 -255 -76 C ATOM 414 O THR A 55 23.884 30.812 19.211 1.00 29.55 O ANISOU 414 O THR A 55 3858 3660 3709 -46 -616 1 O ATOM 415 CB THR A 55 22.019 32.691 17.182 1.00 33.25 C ANISOU 415 CB THR A 55 4247 4072 4311 -37 -213 -50 C ATOM 416 OG1 THR A 55 20.966 33.676 17.133 1.00 34.95 O ANISOU 416 OG1 THR A 55 3972 4565 4740 25 -388 -241 O ATOM 417 CG2 THR A 55 21.421 31.294 17.112 1.00 31.57 C ANISOU 417 CG2 THR A 55 4118 3822 4054 -153 -177 -102 C ATOM 418 N TYR A 56 25.060 32.140 17.832 1.00 30.93 N ANISOU 418 N TYR A 56 4010 3908 3833 -53 -210 -138 N ATOM 419 CA TYR A 56 26.283 31.347 17.919 1.00 30.42 C ANISOU 419 CA TYR A 56 4024 3770 3762 -24 -159 -101 C ATOM 420 C TYR A 56 26.726 31.244 19.370 1.00 29.21 C ANISOU 420 C TYR A 56 3906 3524 3668 -71 -302 -246 C ATOM 421 O TYR A 56 27.032 30.162 19.871 1.00 29.04 O ANISOU 421 O TYR A 56 4159 3344 3528 -200 -516 -655 O ATOM 422 CB TYR A 56 27.425 31.949 17.102 1.00 33.53 C ANISOU 422 CB TYR A 56 4513 4118 4107 -281 -84 -183 C ATOM 423 CG TYR A 56 28.717 31.199 17.345 1.00 34.11 C ANISOU 423 CG TYR A 56 4180 4295 4484 54 -150 -186 C ATOM 424 CD1 TYR A 56 28.977 29.995 16.689 1.00 36.33 C ANISOU 424 CD1 TYR A 56 4491 4571 4741 71 -23 -203 C ATOM 425 CD2 TYR A 56 29.656 31.662 18.271 1.00 36.24 C ANISOU 425 CD2 TYR A 56 4523 4662 4584 99 -130 -313 C ATOM 426 CE1 TYR A 56 30.142 29.270 16.941 1.00 36.49 C ANISOU 426 CE1 TYR A 56 4467 4491 4905 124 -23 -216 C ATOM 427 CE2 TYR A 56 30.830 30.944 18.533 1.00 35.54 C ANISOU 427 CE2 TYR A 56 4255 4610 4638 114 -178 -247 C ATOM 428 CZ TYR A 56 31.068 29.749 17.850 1.00 37.86 C ANISOU 428 CZ TYR A 56 4576 4698 5111 270 -260 -182 C ATOM 429 OH TYR A 56 32.226 29.040 18.082 1.00 38.53 O ANISOU 429 OH TYR A 56 4576 4746 5314 370 -273 -317 O ATOM 430 N LEU A 57 26.767 32.381 20.050 1.00 28.11 N ANISOU 430 N LEU A 57 3681 3363 3633 68 -220 -176 N ATOM 431 CA LEU A 57 27.276 32.414 21.410 1.00 27.73 C ANISOU 431 CA LEU A 57 3612 3410 3511 40 -168 -86 C ATOM 432 C LEU A 57 26.416 31.599 22.348 1.00 26.59 C ANISOU 432 C LEU A 57 3371 3245 3486 -27 -245 -114 C ATOM 433 O LEU A 57 26.915 30.746 23.090 1.00 25.84 O ANISOU 433 O LEU A 57 2969 3226 3620 62 -594 -314 O ATOM 434 CB LEU A 57 27.448 33.885 21.901 1.00 25.88 C ANISOU 434 CB LEU A 57 3516 3245 3069 107 -139 -54 C ATOM 435 CG LEU A 57 28.605 34.609 21.194 1.00 27.97 C ANISOU 435 CG LEU A 57 3473 3353 3798 83 -190 -24 C ATOM 436 CD1 LEU A 57 28.669 36.074 21.566 1.00 29.10 C ANISOU 436 CD1 LEU A 57 3650 3643 3760 -30 -114 -229 C ATOM 437 CD2 LEU A 57 29.967 33.963 21.487 1.00 26.28 C ANISOU 437 CD2 LEU A 57 3143 3543 3298 31 26 -227 C ATOM 438 N ALA A 58 25.110 31.823 22.319 1.00 26.58 N ANISOU 438 N ALA A 58 3417 3302 3377 67 -223 -34 N ATOM 439 CA ALA A 58 24.218 31.116 23.236 1.00 28.30 C ANISOU 439 CA ALA A 58 3603 3550 3597 -8 -120 -17 C ATOM 440 C ALA A 58 24.191 29.610 22.950 1.00 28.89 C ANISOU 440 C ALA A 58 3624 3590 3760 -25 -108 -48 C ATOM 441 O ALA A 58 24.116 28.817 23.891 1.00 29.27 O ANISOU 441 O ALA A 58 3605 3403 4112 -60 -241 -126 O ATOM 442 CB ALA A 58 22.821 31.703 23.184 1.00 28.64 C ANISOU 442 CB ALA A 58 3645 3582 3655 -70 -17 -50 C ATOM 443 N GLU A 59 24.261 29.244 21.658 1.00 29.74 N ANISOU 443 N GLU A 59 3798 3610 3889 86 -61 -181 N ATOM 444 CA GLU A 59 24.292 27.827 21.210 1.00 30.77 C ANISOU 444 CA GLU A 59 3897 3834 3958 -2 -92 -74 C ATOM 445 C GLU A 59 25.508 27.045 21.680 1.00 32.50 C ANISOU 445 C GLU A 59 4101 3898 4348 51 -77 -72 C ATOM 446 O GLU A 59 25.490 25.819 21.708 1.00 33.99 O ANISOU 446 O GLU A 59 4375 3973 4565 -12 -89 -115 O ATOM 447 CB GLU A 59 24.269 27.760 19.694 1.00 28.51 C ANISOU 447 CB GLU A 59 3653 3497 3682 39 1 -173 C ATOM 448 CG GLU A 59 22.883 27.923 19.133 1.00 30.49 C ANISOU 448 CG GLU A 59 3895 4068 3622 -58 -103 16 C ATOM 449 CD GLU A 59 22.839 27.782 17.621 1.00 33.91 C ANISOU 449 CD GLU A 59 4401 4503 3980 57 -79 -61 C ATOM 450 OE1 GLU A 59 23.917 27.797 16.979 1.00 37.37 O ANISOU 450 OE1 GLU A 59 4454 5044 4700 -18 -8 -1 O ATOM 451 OE2 GLU A 59 21.703 27.656 17.088 1.00 38.10 O ANISOU 451 OE2 GLU A 59 4691 5104 4679 -126 -336 -71 O ATOM 452 N ASN A 60 26.551 27.768 22.059 1.00 32.80 N ANISOU 452 N ASN A 60 3982 4036 4442 7 -64 -28 N ATOM 453 CA ASN A 60 27.805 27.177 22.496 1.00 31.56 C ANISOU 453 CA ASN A 60 3973 3895 4122 -1 -72 -32 C ATOM 454 C ASN A 60 28.177 27.533 23.937 1.00 31.28 C ANISOU 454 C ASN A 60 3872 3864 4149 -40 -100 -93 C ATOM 455 O ASN A 60 29.310 27.314 24.342 1.00 32.51 O ANISOU 455 O ASN A 60 3974 3917 4461 83 -207 -198 O ATOM 456 CB ASN A 60 28.886 27.607 21.509 1.00 32.37 C ANISOU 456 CB ASN A 60 4016 4017 4262 82 -18 31 C ATOM 457 CG ASN A 60 28.777 26.875 20.196 1.00 35.29 C ANISOU 457 CG ASN A 60 4846 4236 4324 6 -162 9 C ATOM 458 OD1 ASN A 60 29.023 25.673 20.152 1.00 36.51 O ANISOU 458 OD1 ASN A 60 5268 4245 4360 181 -96 -311 O ATOM 459 ND2 ASN A 60 28.402 27.586 19.113 1.00 34.92 N ANISOU 459 ND2 ASN A 60 4804 4193 4268 -7 -278 -10 N ATOM 460 N ASN A 61 27.210 28.046 24.701 1.00 29.85 N ANISOU 460 N ASN A 61 3707 3623 4009 -127 -140 -106 N ATOM 461 CA ASN A 61 27.358 28.325 26.132 1.00 29.93 C ANISOU 461 CA ASN A 61 3760 3637 3975 -92 -34 -64 C ATOM 462 C ASN A 61 28.370 29.429 26.506 1.00 28.91 C ANISOU 462 C ASN A 61 3627 3489 3866 -147 -94 -50 C ATOM 463 O ASN A 61 28.989 29.370 27.589 1.00 29.08 O ANISOU 463 O ASN A 61 3688 3213 4148 -71 -172 -53 O ATOM 464 CB ASN A 61 27.669 27.054 26.933 1.00 30.98 C ANISOU 464 CB ASN A 61 3962 3760 4047 -14 -63 -52 C ATOM 465 CG ASN A 61 26.558 26.045 26.866 1.00 37.23 C ANISOU 465 CG ASN A 61 4661 4496 4986 -233 23 -60 C ATOM 466 OD1 ASN A 61 26.706 24.999 26.236 1.00 41.92 O ANISOU 466 OD1 ASN A 61 5637 4889 5400 -127 -257 -254 O ATOM 467 ND2 ASN A 61 25.436 26.345 27.512 1.00 41.19 N ANISOU 467 ND2 ASN A 61 4889 5132 5627 -94 69 -218 N ATOM 468 N TYR A 62 28.487 30.416 25.616 1.00 26.98 N ANISOU 468 N TYR A 62 3335 3340 3576 -66 -107 -65 N ATOM 469 CA TYR A 62 29.218 31.678 25.849 1.00 25.88 C ANISOU 469 CA TYR A 62 3280 3250 3301 35 -48 -168 C ATOM 470 C TYR A 62 28.178 32.736 26.244 1.00 26.08 C ANISOU 470 C TYR A 62 3375 3073 3459 58 -151 -154 C ATOM 471 O TYR A 62 27.062 32.722 25.736 1.00 26.21 O ANISOU 471 O TYR A 62 3468 2647 3843 41 -288 -275 O ATOM 472 CB TYR A 62 29.947 32.142 24.583 1.00 25.91 C ANISOU 472 CB TYR A 62 3157 3294 3393 -49 -84 -157 C ATOM 473 CG TYR A 62 31.057 31.225 24.103 1.00 25.63 C ANISOU 473 CG TYR A 62 3230 3242 3263 146 -123 -178 C ATOM 474 CD1 TYR A 62 32.277 31.193 24.759 1.00 27.86 C ANISOU 474 CD1 TYR A 62 3266 3496 3821 21 -69 -345 C ATOM 475 CD2 TYR A 62 30.884 30.407 22.971 1.00 26.71 C ANISOU 475 CD2 TYR A 62 3066 3469 3612 -34 -41 -186 C ATOM 476 CE1 TYR A 62 33.321 30.349 24.327 1.00 27.83 C ANISOU 476 CE1 TYR A 62 3325 3573 3677 177 -196 -254 C ATOM 477 CE2 TYR A 62 31.910 29.572 22.519 1.00 27.06 C ANISOU 477 CE2 TYR A 62 3370 3360 3549 99 -200 -282 C ATOM 478 CZ TYR A 62 33.143 29.553 23.206 1.00 28.64 C ANISOU 478 CZ TYR A 62 3286 3798 3796 217 -178 -367 C ATOM 479 OH TYR A 62 34.177 28.719 22.801 1.00 25.69 O ANISOU 479 OH TYR A 62 3080 3554 3126 -120 -343 -530 O ATOM 480 N PHE A 63 28.518 33.585 27.216 1.00 25.34 N ANISOU 480 N PHE A 63 3212 3097 3319 -13 -128 -248 N ATOM 481 CA PHE A 63 27.653 34.710 27.621 1.00 23.84 C ANISOU 481 CA PHE A 63 2998 3054 3006 32 -83 -122 C ATOM 482 C PHE A 63 27.616 35.769 26.510 1.00 21.87 C ANISOU 482 C PHE A 63 2790 2817 2700 10 -33 -264 C ATOM 483 O PHE A 63 28.598 35.995 25.856 1.00 20.69 O ANISOU 483 O PHE A 63 2811 2776 2274 -20 -240 -52 O ATOM 484 CB PHE A 63 28.149 35.281 28.980 1.00 24.20 C ANISOU 484 CB PHE A 63 2962 2941 3291 46 -12 -229 C ATOM 485 CG PHE A 63 27.246 36.313 29.610 1.00 24.62 C ANISOU 485 CG PHE A 63 3193 3136 3024 -98 -130 -218 C ATOM 486 CD1 PHE A 63 25.871 36.111 29.744 1.00 25.59 C ANISOU 486 CD1 PHE A 63 3453 3305 2964 -144 85 -117 C ATOM 487 CD2 PHE A 63 27.777 37.493 30.104 1.00 22.42 C ANISOU 487 CD2 PHE A 63 2749 2736 3032 -325 117 205 C ATOM 488 CE1 PHE A 63 25.058 37.062 30.301 1.00 24.21 C ANISOU 488 CE1 PHE A 63 3006 2930 3261 11 -186 89 C ATOM 489 CE2 PHE A 63 26.969 38.442 30.707 1.00 22.70 C ANISOU 489 CE2 PHE A 63 3001 2915 2709 -97 -65 35 C ATOM 490 CZ PHE A 63 25.609 38.225 30.814 1.00 25.05 C ANISOU 490 CZ PHE A 63 3140 3176 3199 52 35 41 C ATOM 491 N TYR A 64 26.451 36.371 26.269 1.00 21.51 N ANISOU 491 N TYR A 64 2678 2882 2611 -6 -125 -214 N ATOM 492 CA TYR A 64 26.346 37.543 25.416 1.00 22.04 C ANISOU 492 CA TYR A 64 2767 2849 2757 30 -110 -195 C ATOM 493 C TYR A 64 25.339 38.509 26.052 1.00 22.21 C ANISOU 493 C TYR A 64 2715 2807 2915 -22 -161 -130 C ATOM 494 O TYR A 64 24.567 38.151 26.937 1.00 23.42 O ANISOU 494 O TYR A 64 2551 2924 3422 138 -160 -247 O ATOM 495 CB TYR A 64 25.879 37.162 23.989 1.00 22.19 C ANISOU 495 CB TYR A 64 2840 2832 2756 49 -160 -267 C ATOM 496 CG TYR A 64 24.383 36.905 23.954 1.00 21.80 C ANISOU 496 CG TYR A 64 2836 2732 2714 50 22 -371 C ATOM 497 CD1 TYR A 64 23.476 37.949 23.751 1.00 23.83 C ANISOU 497 CD1 TYR A 64 3088 2996 2969 83 -351 -79 C ATOM 498 CD2 TYR A 64 23.872 35.651 24.206 1.00 18.46 C ANISOU 498 CD2 TYR A 64 2695 2984 1333 -57 -300 222 C ATOM 499 CE1 TYR A 64 22.109 37.731 23.794 1.00 22.66 C ANISOU 499 CE1 TYR A 64 2859 2910 2837 -30 -49 -112 C ATOM 500 CE2 TYR A 64 22.495 35.425 24.267 1.00 22.01 C ANISOU 500 CE2 TYR A 64 2708 2963 2689 15 -124 152 C ATOM 501 CZ TYR A 64 21.626 36.462 24.042 1.00 24.05 C ANISOU 501 CZ TYR A 64 2940 3046 3153 39 -73 -26 C ATOM 502 OH TYR A 64 20.274 36.222 24.083 1.00 25.50 O ANISOU 502 OH TYR A 64 2849 3120 3717 -36 -117 -32 O ATOM 503 N ILE A 65 25.395 39.750 25.613 1.00 22.93 N ANISOU 503 N ILE A 65 2708 2931 3070 -75 -200 -162 N ATOM 504 CA ILE A 65 24.398 40.772 25.947 1.00 23.30 C ANISOU 504 CA ILE A 65 2792 2917 3142 -22 -154 -201 C ATOM 505 C ILE A 65 24.146 41.508 24.646 1.00 22.60 C ANISOU 505 C ILE A 65 2805 2920 2863 -24 -127 -233 C ATOM 506 O ILE A 65 25.036 42.139 24.072 1.00 21.33 O ANISOU 506 O ILE A 65 2496 2716 2892 -105 -627 -551 O ATOM 507 CB ILE A 65 24.890 41.817 26.981 1.00 22.34 C ANISOU 507 CB ILE A 65 2919 2851 2715 -7 -48 -196 C ATOM 508 CG1 ILE A 65 25.225 41.178 28.330 1.00 22.56 C ANISOU 508 CG1 ILE A 65 2814 2790 2965 -4 -262 -134 C ATOM 509 CG2 ILE A 65 23.895 42.956 27.093 1.00 19.24 C ANISOU 509 CG2 ILE A 65 2116 2684 2508 -417 -82 -136 C ATOM 510 CD1 ILE A 65 26.030 42.122 29.269 1.00 23.07 C ANISOU 510 CD1 ILE A 65 2764 2720 3281 105 -160 -232 C ATOM 511 N MET A 66 22.909 41.437 24.180 1.00 25.28 N ANISOU 511 N MET A 66 3060 3247 3297 -29 -77 -106 N ATOM 512 CA MET A 66 22.530 42.094 22.955 1.00 26.26 C ANISOU 512 CA MET A 66 3171 3386 3422 15 -131 -63 C ATOM 513 C MET A 66 22.424 43.598 23.182 1.00 26.30 C ANISOU 513 C MET A 66 3052 3425 3513 -43 -151 -9 C ATOM 514 O MET A 66 22.091 44.051 24.286 1.00 25.42 O ANISOU 514 O MET A 66 2985 3174 3499 33 -398 -11 O ATOM 515 CB MET A 66 21.191 41.519 22.487 1.00 28.00 C ANISOU 515 CB MET A 66 3301 3513 3822 -60 -99 -40 C ATOM 516 CG MET A 66 20.825 41.840 21.088 1.00 34.01 C ANISOU 516 CG MET A 66 4042 4446 4431 -136 -226 63 C ATOM 517 SD MET A 66 22.039 41.552 19.825 1.00 31.20 S ANISOU 517 SD MET A 66 3133 4118 4603 503 -1120 -662 S ATOM 518 CE MET A 66 21.148 42.317 18.492 1.00 33.42 C ANISOU 518 CE MET A 66 4416 4046 4235 37 -313 72 C ATOM 519 N HIS A 67 22.714 44.352 22.128 1.00 27.19 N ANISOU 519 N HIS A 67 3256 3583 3491 3 -267 54 N ATOM 520 CA HIS A 67 22.550 45.807 22.112 1.00 28.82 C ANISOU 520 CA HIS A 67 3563 3642 3742 37 -178 -27 C ATOM 521 C HIS A 67 21.059 46.213 21.926 1.00 29.47 C ANISOU 521 C HIS A 67 3628 3746 3824 100 -171 6 C ATOM 522 O HIS A 67 20.194 45.373 21.578 1.00 28.38 O ANISOU 522 O HIS A 67 3441 3720 3622 277 -371 68 O ATOM 523 CB HIS A 67 23.404 46.424 20.983 1.00 29.63 C ANISOU 523 CB HIS A 67 3509 3703 4046 43 -67 -64 C ATOM 524 CG HIS A 67 22.953 46.045 19.599 1.00 33.72 C ANISOU 524 CG HIS A 67 4323 4371 4117 124 -71 84 C ATOM 525 ND1 HIS A 67 21.828 46.576 19.003 1.00 34.11 N ANISOU 525 ND1 HIS A 67 4297 4391 4272 131 -108 154 N ATOM 526 CD2 HIS A 67 23.458 45.158 18.711 1.00 34.59 C ANISOU 526 CD2 HIS A 67 4237 4470 4433 143 -102 -58 C ATOM 527 CE1 HIS A 67 21.670 46.042 17.806 1.00 32.70 C ANISOU 527 CE1 HIS A 67 4199 4053 4172 8 -145 72 C ATOM 528 NE2 HIS A 67 22.651 45.183 17.601 1.00 33.87 N ANISOU 528 NE2 HIS A 67 4275 4275 4319 51 -194 102 N ATOM 529 N ARG A 68 20.778 47.500 22.145 1.00 29.79 N ANISOU 529 N ARG A 68 3785 3828 3704 74 -194 7 N ATOM 530 CA ARG A 68 19.411 48.024 22.029 1.00 31.53 C ANISOU 530 CA ARG A 68 3912 3969 4096 65 -145 -75 C ATOM 531 C ARG A 68 19.285 49.084 20.924 1.00 32.34 C ANISOU 531 C ARG A 68 4058 4039 4189 -58 -268 -150 C ATOM 532 O ARG A 68 18.469 50.006 21.021 1.00 32.72 O ANISOU 532 O ARG A 68 4341 3914 4176 -26 -448 -219 O ATOM 533 CB ARG A 68 18.944 48.579 23.371 1.00 31.82 C ANISOU 533 CB ARG A 68 3919 3921 4250 26 -3 9 C ATOM 534 CG ARG A 68 19.862 49.638 23.957 1.00 30.98 C ANISOU 534 CG ARG A 68 3827 3799 4143 225 -256 -18 C ATOM 535 CD ARG A 68 19.252 50.204 25.167 1.00 31.63 C ANISOU 535 CD ARG A 68 3921 4104 3992 162 -89 51 C ATOM 536 NE ARG A 68 20.134 51.129 25.876 1.00 34.80 N ANISOU 536 NE ARG A 68 4274 4355 4594 115 -201 -99 N ATOM 537 CZ ARG A 68 19.942 52.442 26.031 1.00 34.62 C ANISOU 537 CZ ARG A 68 4235 4310 4609 -70 -102 101 C ATOM 538 NH1 ARG A 68 18.885 53.075 25.529 1.00 32.39 N ANISOU 538 NH1 ARG A 68 4089 3917 4299 0 11 145 N ATOM 539 NH2 ARG A 68 20.825 53.134 26.735 1.00 34.59 N ANISOU 539 NH2 ARG A 68 4400 4467 4274 -155 -135 -34 N ATOM 540 N PHE A 69 20.056 48.941 19.861 1.00 35.02 N ANISOU 540 N PHE A 69 4347 4462 4494 -65 -170 -93 N ATOM 541 CA PHE A 69 19.985 49.881 18.754 1.00 35.93 C ANISOU 541 CA PHE A 69 4552 4515 4582 -30 -97 26 C ATOM 542 C PHE A 69 18.667 49.784 17.972 1.00 38.37 C ANISOU 542 C PHE A 69 4792 4801 4985 -37 -144 17 C ATOM 543 O PHE A 69 18.188 50.783 17.419 1.00 40.91 O ANISOU 543 O PHE A 69 5137 5159 5246 68 -213 131 O ATOM 544 CB PHE A 69 21.144 49.681 17.793 1.00 41.27 C ANISOU 544 CB PHE A 69 4854 5408 5416 140 -116 -565 C ATOM 545 CG PHE A 69 21.271 50.788 16.782 1.00 37.85 C ANISOU 545 CG PHE A 69 4923 4761 4694 -141 -40 128 C ATOM 546 CD1 PHE A 69 21.795 52.029 17.157 1.00 42.48 C ANISOU 546 CD1 PHE A 69 5722 5213 5202 -106 -24 -52 C ATOM 547 CD2 PHE A 69 20.854 50.608 15.464 1.00 43.04 C ANISOU 547 CD2 PHE A 69 5534 5511 5306 -163 -101 54 C ATOM 548 CE1 PHE A 69 21.905 53.071 16.228 1.00 42.28 C ANISOU 548 CE1 PHE A 69 5690 5043 5330 -179 17 184 C ATOM 549 CE2 PHE A 69 20.953 51.647 14.533 1.00 41.52 C ANISOU 549 CE2 PHE A 69 5605 5178 4993 -29 -22 259 C ATOM 550 CZ PHE A 69 21.488 52.875 14.917 1.00 41.49 C ANISOU 550 CZ PHE A 69 5452 5086 5224 -41 -37 195 C ATOM 551 N GLN A 70 18.077 48.594 17.929 1.00 37.65 N ANISOU 551 N GLN A 70 4670 4757 4877 -42 -111 -86 N ATOM 552 CA GLN A 70 16.762 48.431 17.286 1.00 36.65 C ANISOU 552 CA GLN A 70 4599 4705 4620 8 -106 -22 C ATOM 553 C GLN A 70 15.770 47.934 18.296 1.00 34.75 C ANISOU 553 C GLN A 70 4314 4399 4488 17 -247 -45 C ATOM 554 O GLN A 70 15.340 46.793 18.226 1.00 34.14 O ANISOU 554 O GLN A 70 4293 4244 4433 48 -268 -106 O ATOM 555 CB GLN A 70 16.858 47.478 16.111 1.00 37.00 C ANISOU 555 CB GLN A 70 4701 4693 4661 14 -150 -92 C ATOM 556 CG GLN A 70 17.704 48.049 14.982 1.00 38.84 C ANISOU 556 CG GLN A 70 5060 4832 4865 -134 31 -19 C ATOM 557 CD GLN A 70 17.824 47.088 13.822 1.00 41.55 C ANISOU 557 CD GLN A 70 5391 5327 5067 -34 87 -139 C ATOM 558 OE1 GLN A 70 18.265 45.938 13.992 1.00 48.71 O ANISOU 558 OE1 GLN A 70 6432 5818 6256 199 -51 37 O ATOM 559 NE2 GLN A 70 17.443 47.547 12.628 1.00 47.80 N ANISOU 559 NE2 GLN A 70 6179 6171 5810 9 -235 236 N ATOM 560 N PRO A 71 15.397 48.808 19.249 1.00 32.99 N ANISOU 560 N PRO A 71 4026 4239 4266 98 -216 18 N ATOM 561 CA PRO A 71 14.695 48.381 20.427 1.00 33.40 C ANISOU 561 CA PRO A 71 4109 4227 4351 35 -173 26 C ATOM 562 C PRO A 71 13.375 47.715 20.167 1.00 32.88 C ANISOU 562 C PRO A 71 4021 4146 4323 27 -170 -7 C ATOM 563 O PRO A 71 12.907 46.977 21.029 1.00 32.26 O ANISOU 563 O PRO A 71 3595 4077 4585 16 -338 -37 O ATOM 564 CB PRO A 71 14.481 49.685 21.205 1.00 32.95 C ANISOU 564 CB PRO A 71 4074 4137 4309 40 -82 15 C ATOM 565 CG PRO A 71 14.620 50.754 20.214 1.00 31.92 C ANISOU 565 CG PRO A 71 4038 3952 4135 5 -206 -51 C ATOM 566 CD PRO A 71 15.611 50.270 19.248 1.00 33.09 C ANISOU 566 CD PRO A 71 4078 4252 4240 -6 -133 -31 C ATOM 567 N GLU A 72 12.778 47.997 19.006 1.00 33.70 N ANISOU 567 N GLU A 72 4169 4240 4392 -4 -145 -118 N ATOM 568 CA GLU A 72 11.481 47.432 18.651 1.00 35.00 C ANISOU 568 CA GLU A 72 4374 4386 4535 -12 -160 -64 C ATOM 569 C GLU A 72 11.559 45.908 18.418 1.00 34.96 C ANISOU 569 C GLU A 72 4387 4333 4560 -34 -128 -123 C ATOM 570 O GLU A 72 10.553 45.221 18.496 1.00 34.93 O ANISOU 570 O GLU A 72 4354 4339 4576 -16 -199 -204 O ATOM 571 CB GLU A 72 10.892 48.171 17.431 1.00 35.53 C ANISOU 571 CB GLU A 72 4495 4409 4595 -2 -173 -40 C ATOM 572 CG GLU A 72 11.482 47.816 16.059 1.00 38.13 C ANISOU 572 CG GLU A 72 4792 4871 4823 -48 51 -6 C ATOM 573 CD GLU A 72 12.774 48.539 15.704 1.00 39.18 C ANISOU 573 CD GLU A 72 4980 5105 4802 -162 46 -60 C ATOM 574 OE1 GLU A 72 13.318 49.286 16.558 1.00 37.19 O ANISOU 574 OE1 GLU A 72 4698 4775 4655 -171 -106 -90 O ATOM 575 OE2 GLU A 72 13.242 48.341 14.545 1.00 38.26 O ANISOU 575 OE2 GLU A 72 4953 5152 4430 213 -85 -119 O ATOM 576 N LYS A 73 12.767 45.406 18.177 1.00 35.25 N ANISOU 576 N LYS A 73 4396 4390 4607 -44 -164 -198 N ATOM 577 CA LYS A 73 13.019 43.982 17.943 1.00 35.75 C ANISOU 577 CA LYS A 73 4488 4475 4619 -9 -119 -89 C ATOM 578 C LYS A 73 13.251 43.126 19.183 1.00 34.71 C ANISOU 578 C LYS A 73 4317 4344 4527 60 -170 -105 C ATOM 579 O LYS A 73 13.336 41.911 19.064 1.00 35.32 O ANISOU 579 O LYS A 73 4207 4432 4781 52 -365 -196 O ATOM 580 CB LYS A 73 14.229 43.828 17.018 1.00 36.98 C ANISOU 580 CB LYS A 73 4531 4702 4815 -18 -57 -225 C ATOM 581 CG LYS A 73 14.017 44.434 15.642 1.00 39.01 C ANISOU 581 CG LYS A 73 4905 4847 5069 -19 -102 13 C ATOM 582 CD LYS A 73 15.270 44.319 14.791 1.00 38.60 C ANISOU 582 CD LYS A 73 4921 4880 4863 -46 -49 -48 C ATOM 583 CE LYS A 73 14.987 44.588 13.327 1.00 42.43 C ANISOU 583 CE LYS A 73 5517 5411 5191 58 9 66 C ATOM 584 NZ LYS A 73 16.210 44.413 12.475 1.00 46.24 N ANISOU 584 NZ LYS A 73 5818 6057 5694 -2 276 -16 N ATOM 585 N ARG A 74 13.349 43.736 20.359 1.00 34.01 N ANISOU 585 N ARG A 74 4250 4170 4501 116 -109 -105 N ATOM 586 CA ARG A 74 13.720 43.013 21.582 1.00 33.43 C ANISOU 586 CA ARG A 74 4174 4195 4332 42 -78 -106 C ATOM 587 C ARG A 74 12.672 42.028 22.082 1.00 33.89 C ANISOU 587 C ARG A 74 4222 4195 4457 53 -208 -155 C ATOM 588 O ARG A 74 13.017 40.962 22.587 1.00 31.80 O ANISOU 588 O ARG A 74 3970 3946 4163 39 -484 -259 O ATOM 589 CB ARG A 74 14.082 44.004 22.699 1.00 33.26 C ANISOU 589 CB ARG A 74 4126 4120 4388 97 -64 -4 C ATOM 590 CG ARG A 74 15.296 44.870 22.366 1.00 32.46 C ANISOU 590 CG ARG A 74 3990 4029 4314 59 0 -76 C ATOM 591 CD ARG A 74 15.529 45.956 23.405 1.00 32.59 C ANISOU 591 CD ARG A 74 3971 4098 4313 -32 -48 -73 C ATOM 592 NE ARG A 74 14.422 46.922 23.449 1.00 34.27 N ANISOU 592 NE ARG A 74 4077 4190 4752 74 -284 -273 N ATOM 593 CZ ARG A 74 14.274 47.883 24.357 1.00 35.33 C ANISOU 593 CZ ARG A 74 4334 4495 4591 191 -168 -112 C ATOM 594 NH1 ARG A 74 15.163 48.047 25.329 1.00 33.65 N ANISOU 594 NH1 ARG A 74 4170 4055 4557 108 -222 24 N ATOM 595 NH2 ARG A 74 13.212 48.694 24.294 1.00 32.68 N ANISOU 595 NH2 ARG A 74 4049 4045 4320 110 -178 -88 N ATOM 596 N ILE A 75 11.387 42.370 21.975 1.00 34.66 N ANISOU 596 N ILE A 75 4223 4313 4631 46 -158 -71 N ATOM 597 CA ILE A 75 10.357 41.449 22.444 1.00 34.83 C ANISOU 597 CA ILE A 75 4239 4434 4558 66 -76 -59 C ATOM 598 C ILE A 75 10.368 40.173 21.591 1.00 34.20 C ANISOU 598 C ILE A 75 4030 4351 4613 1 -192 -26 C ATOM 599 O ILE A 75 10.280 39.079 22.151 1.00 35.05 O ANISOU 599 O ILE A 75 4033 4300 4982 -139 -361 -84 O ATOM 600 CB ILE A 75 8.941 42.095 22.467 1.00 35.35 C ANISOU 600 CB ILE A 75 4232 4479 4719 85 -7 -37 C ATOM 601 CG1 ILE A 75 8.918 43.236 23.473 1.00 37.80 C ANISOU 601 CG1 ILE A 75 4635 4782 4945 125 -13 -48 C ATOM 602 CG2 ILE A 75 7.889 41.093 22.888 1.00 35.37 C ANISOU 602 CG2 ILE A 75 4338 4419 4682 72 -69 10 C ATOM 603 CD1 ILE A 75 7.856 44.262 23.178 1.00 37.59 C ANISOU 603 CD1 ILE A 75 4639 4763 4877 122 0 -20 C ATOM 604 N SER A 76 10.519 40.310 20.266 1.00 33.21 N ANISOU 604 N SER A 76 3927 4218 4472 70 -128 -53 N ATOM 605 CA SER A 76 10.590 39.133 19.386 1.00 32.77 C ANISOU 605 CA SER A 76 3918 4158 4373 102 -148 -42 C ATOM 606 C SER A 76 11.891 38.343 19.628 1.00 31.23 C ANISOU 606 C SER A 76 3818 3850 4199 48 -245 -16 C ATOM 607 O SER A 76 11.845 37.103 19.784 1.00 30.36 O ANISOU 607 O SER A 76 3743 3609 4183 57 -410 -353 O ATOM 608 CB SER A 76 10.413 39.492 17.906 1.00 34.57 C ANISOU 608 CB SER A 76 4342 4296 4495 89 -56 8 C ATOM 609 OG SER A 76 11.633 39.814 17.235 1.00 40.75 O ANISOU 609 OG SER A 76 4582 5454 5444 247 -143 -59 O ATOM 610 N PHE A 77 13.018 39.060 19.708 1.00 28.68 N ANISOU 610 N PHE A 77 3533 3577 3785 82 -209 -26 N ATOM 611 CA PHE A 77 14.310 38.450 20.071 1.00 29.35 C ANISOU 611 CA PHE A 77 3578 3669 3903 -24 -189 -79 C ATOM 612 C PHE A 77 14.181 37.569 21.311 1.00 27.83 C ANISOU 612 C PHE A 77 3211 3567 3795 -53 -380 -119 C ATOM 613 O PHE A 77 14.606 36.414 21.294 1.00 29.71 O ANISOU 613 O PHE A 77 3456 3608 4222 -8 -627 -279 O ATOM 614 CB PHE A 77 15.395 39.524 20.250 1.00 28.39 C ANISOU 614 CB PHE A 77 3329 3719 3738 133 -305 -6 C ATOM 615 CG PHE A 77 16.750 38.980 20.666 1.00 28.46 C ANISOU 615 CG PHE A 77 3517 3619 3677 92 -147 -86 C ATOM 616 CD1 PHE A 77 17.697 38.585 19.723 1.00 26.79 C ANISOU 616 CD1 PHE A 77 3152 3465 3560 3 -292 -285 C ATOM 617 CD2 PHE A 77 17.062 38.874 22.010 1.00 28.16 C ANISOU 617 CD2 PHE A 77 3533 3532 3633 211 -240 -26 C ATOM 618 CE1 PHE A 77 18.956 38.091 20.133 1.00 27.29 C ANISOU 618 CE1 PHE A 77 3743 3548 3076 174 -303 -79 C ATOM 619 CE2 PHE A 77 18.307 38.389 22.421 1.00 29.13 C ANISOU 619 CE2 PHE A 77 3445 3765 3857 61 -179 -63 C ATOM 620 CZ PHE A 77 19.237 37.999 21.505 1.00 24.16 C ANISOU 620 CZ PHE A 77 3155 3134 2888 -339 -239 -218 C ATOM 621 N ILE A 78 13.598 38.084 22.381 1.00 27.81 N ANISOU 621 N ILE A 78 3104 3523 3937 -97 -317 -46 N ATOM 622 CA ILE A 78 13.466 37.286 23.604 1.00 29.75 C ANISOU 622 CA ILE A 78 3561 3745 3995 -88 -213 -48 C ATOM 623 C ILE A 78 12.670 36.026 23.296 1.00 30.75 C ANISOU 623 C ILE A 78 3614 3767 4302 -116 -252 0 C ATOM 624 O ILE A 78 13.114 34.906 23.539 1.00 30.50 O ANISOU 624 O ILE A 78 3242 3800 4546 -292 -481 -32 O ATOM 625 CB ILE A 78 12.787 38.052 24.754 1.00 29.03 C ANISOU 625 CB ILE A 78 3485 3471 4071 -14 -170 -42 C ATOM 626 CG1 ILE A 78 13.660 39.239 25.190 1.00 30.72 C ANISOU 626 CG1 ILE A 78 3641 3927 4104 -80 -98 -106 C ATOM 627 CG2 ILE A 78 12.568 37.158 25.970 1.00 28.52 C ANISOU 627 CG2 ILE A 78 3326 3602 3907 -51 -149 -137 C ATOM 628 CD1 ILE A 78 12.850 40.469 25.534 1.00 31.48 C ANISOU 628 CD1 ILE A 78 3903 3925 4130 -86 -72 -244 C ATOM 629 N ARG A 79 11.509 36.228 22.696 1.00 31.79 N ANISOU 629 N ARG A 79 3729 3941 4409 -125 -239 -58 N ATOM 630 CA ARG A 79 10.570 35.134 22.465 1.00 32.32 C ANISOU 630 CA ARG A 79 3862 4121 4296 -75 -235 -34 C ATOM 631 C ARG A 79 11.234 34.026 21.661 1.00 30.72 C ANISOU 631 C ARG A 79 3604 3966 4099 -88 -371 -10 C ATOM 632 O ARG A 79 11.097 32.842 21.961 1.00 31.29 O ANISOU 632 O ARG A 79 3566 3985 4336 -38 -572 162 O ATOM 633 CB ARG A 79 9.333 35.687 21.740 1.00 32.22 C ANISOU 633 CB ARG A 79 3725 4304 4213 -119 -311 -22 C ATOM 634 CG ARG A 79 8.237 34.649 21.529 1.00 34.29 C ANISOU 634 CG ARG A 79 4063 4312 4653 -168 -140 -19 C ATOM 635 CD ARG A 79 6.900 35.266 21.025 1.00 36.16 C ANISOU 635 CD ARG A 79 4248 4816 4673 31 -343 29 C ATOM 636 NE ARG A 79 6.315 36.331 21.859 1.00 39.78 N ANISOU 636 NE ARG A 79 5135 4956 5021 11 -222 -103 N ATOM 637 CZ ARG A 79 6.103 37.590 21.460 1.00 41.58 C ANISOU 637 CZ ARG A 79 5427 5094 5276 -40 -15 -35 C ATOM 638 NH1 ARG A 79 6.462 38.006 20.243 1.00 43.33 N ANISOU 638 NH1 ARG A 79 5753 5693 5017 -76 -19 -119 N ATOM 639 NH2 ARG A 79 5.529 38.455 22.284 1.00 40.84 N ANISOU 639 NH2 ARG A 79 5336 5286 4893 -130 -25 -165 N ATOM 640 N ASP A 80 11.983 34.429 20.652 1.00 29.32 N ANISOU 640 N ASP A 80 3328 3861 3948 -97 -408 -119 N ATOM 641 CA ASP A 80 12.591 33.503 19.742 1.00 30.36 C ANISOU 641 CA ASP A 80 3590 3889 4057 -10 -287 -90 C ATOM 642 C ASP A 80 13.770 32.731 20.363 1.00 30.50 C ANISOU 642 C ASP A 80 3641 3802 4143 15 -338 -163 C ATOM 643 O ASP A 80 13.859 31.504 20.227 1.00 28.52 O ANISOU 643 O ASP A 80 3240 3717 3877 159 -591 -293 O ATOM 644 CB ASP A 80 12.985 34.262 18.490 1.00 28.80 C ANISOU 644 CB ASP A 80 3455 3607 3878 -8 -302 -57 C ATOM 645 CG ASP A 80 11.757 34.709 17.679 1.00 30.21 C ANISOU 645 CG ASP A 80 3837 3795 3847 97 -1 192 C ATOM 646 OD1 ASP A 80 10.615 34.477 18.146 1.00 33.90 O ANISOU 646 OD1 ASP A 80 3801 4288 4791 78 -375 -395 O ATOM 647 OD2 ASP A 80 11.941 35.280 16.590 1.00 26.26 O ANISOU 647 OD2 ASP A 80 3598 4338 2040 702 -1034 -276 O ATOM 648 N MET A 81 14.650 33.431 21.079 1.00 31.14 N ANISOU 648 N MET A 81 3644 3992 4194 42 -315 -254 N ATOM 649 CA MET A 81 15.757 32.754 21.741 1.00 31.12 C ANISOU 649 CA MET A 81 3804 3919 4101 44 -280 -110 C ATOM 650 C MET A 81 15.204 31.689 22.641 1.00 30.65 C ANISOU 650 C MET A 81 3708 3881 4055 -84 -352 -168 C ATOM 651 O MET A 81 15.643 30.531 22.558 1.00 29.73 O ANISOU 651 O MET A 81 3489 3639 4166 -272 -482 -225 O ATOM 652 CB MET A 81 16.650 33.740 22.521 1.00 30.49 C ANISOU 652 CB MET A 81 3592 3904 4085 58 -283 -48 C ATOM 653 CG MET A 81 17.434 34.697 21.623 1.00 29.12 C ANISOU 653 CG MET A 81 3677 3626 3759 -88 -417 -90 C ATOM 654 SD MET A 81 18.669 33.919 20.542 1.00 33.44 S ANISOU 654 SD MET A 81 4151 4088 4464 -140 -651 -319 S ATOM 655 CE MET A 81 20.064 33.752 21.653 1.00 31.64 C ANISOU 655 CE MET A 81 4078 3820 4123 16 -295 -55 C ATOM 656 N GLN A 82 14.215 32.056 23.456 1.00 31.90 N ANISOU 656 N GLN A 82 3897 3969 4251 -69 -360 -136 N ATOM 657 CA GLN A 82 13.755 31.218 24.548 1.00 34.40 C ANISOU 657 CA GLN A 82 4244 4339 4485 -67 -176 -18 C ATOM 658 C GLN A 82 13.025 29.988 24.020 1.00 36.74 C ANISOU 658 C GLN A 82 4580 4526 4854 -122 -164 -3 C ATOM 659 O GLN A 82 12.950 28.974 24.711 1.00 37.76 O ANISOU 659 O GLN A 82 4710 4471 5163 -250 -240 -64 O ATOM 660 CB GLN A 82 12.855 32.000 25.506 1.00 35.06 C ANISOU 660 CB GLN A 82 4371 4411 4536 -90 -196 -40 C ATOM 661 CG GLN A 82 13.543 33.188 26.214 1.00 34.60 C ANISOU 661 CG GLN A 82 4133 4419 4593 -193 -142 -122 C ATOM 662 CD GLN A 82 12.776 33.716 27.427 1.00 35.28 C ANISOU 662 CD GLN A 82 4303 4516 4586 -85 -97 1 C ATOM 663 OE1 GLN A 82 11.531 33.749 27.447 1.00 33.96 O ANISOU 663 OE1 GLN A 82 4024 4286 4592 -63 -262 -63 O ATOM 664 NE2 GLN A 82 13.521 34.148 28.453 1.00 36.40 N ANISOU 664 NE2 GLN A 82 4300 4568 4961 -264 -167 -28 N ATOM 665 N SER A 83 12.489 30.107 22.806 1.00 37.45 N ANISOU 665 N SER A 83 4747 4648 4833 -135 -134 -137 N ATOM 666 CA SER A 83 11.785 29.020 22.133 1.00 37.90 C ANISOU 666 CA SER A 83 4780 4678 4942 -77 -127 -90 C ATOM 667 C SER A 83 12.765 28.002 21.527 1.00 39.28 C ANISOU 667 C SER A 83 4910 4855 5161 -14 -52 -92 C ATOM 668 O SER A 83 12.399 26.835 21.303 1.00 40.55 O ANISOU 668 O SER A 83 5001 4874 5529 86 -121 -115 O ATOM 669 CB SER A 83 10.887 29.583 21.038 1.00 38.41 C ANISOU 669 CB SER A 83 4840 4731 5021 -79 -135 -59 C ATOM 670 OG SER A 83 11.629 29.888 19.870 1.00 40.76 O ANISOU 670 OG SER A 83 4954 5030 5502 -2 -67 -164 O ATOM 671 N ARG A 84 13.992 28.450 21.256 1.00 38.65 N ANISOU 671 N ARG A 84 4877 4784 5022 -37 -50 -55 N ATOM 672 CA ARG A 84 15.089 27.565 20.854 1.00 38.51 C ANISOU 672 CA ARG A 84 4851 4744 5035 -21 -118 -57 C ATOM 673 C ARG A 84 15.860 27.068 22.076 1.00 36.72 C ANISOU 673 C ARG A 84 4638 4500 4813 -81 -76 -83 C ATOM 674 O ARG A 84 16.920 26.456 21.942 1.00 36.53 O ANISOU 674 O ARG A 84 4762 4202 4914 -49 -307 30 O ATOM 675 CB ARG A 84 16.036 28.283 19.899 1.00 37.98 C ANISOU 675 CB ARG A 84 4781 4712 4936 58 11 -84 C ATOM 676 CG ARG A 84 15.464 28.515 18.530 1.00 43.42 C ANISOU 676 CG ARG A 84 5567 5361 5570 25 -264 -71 C ATOM 677 CD ARG A 84 16.251 29.581 17.756 1.00 44.60 C ANISOU 677 CD ARG A 84 5679 5640 5626 -49 -61 108 C ATOM 678 NE ARG A 84 17.219 29.031 16.799 1.00 51.66 N ANISOU 678 NE ARG A 84 6518 6615 6493 29 224 -108 N ATOM 679 CZ ARG A 84 17.989 29.770 15.993 1.00 51.30 C ANISOU 679 CZ ARG A 84 6479 6549 6463 -124 240 92 C ATOM 680 NH1 ARG A 84 17.922 31.106 16.033 1.00 53.95 N ANISOU 680 NH1 ARG A 84 6973 6698 6825 113 27 -23 N ATOM 681 NH2 ARG A 84 18.837 29.178 15.141 1.00 51.91 N ANISOU 681 NH2 ARG A 84 6731 6525 6467 -1 157 41 N ATOM 682 N GLY A 85 15.331 27.318 23.267 1.00 35.54 N ANISOU 682 N GLY A 85 4510 4235 4756 -184 -145 -11 N ATOM 683 CA GLY A 85 15.995 26.891 24.489 1.00 35.78 C ANISOU 683 CA GLY A 85 4498 4291 4805 -140 -138 -37 C ATOM 684 C GLY A 85 17.291 27.654 24.754 1.00 35.75 C ANISOU 684 C GLY A 85 4417 4247 4919 -124 -246 27 C ATOM 685 O GLY A 85 18.206 27.128 25.383 1.00 36.46 O ANISOU 685 O GLY A 85 4728 4056 5069 -218 -527 -37 O ATOM 686 N LEU A 86 17.370 28.890 24.265 1.00 34.48 N ANISOU 686 N LEU A 86 4211 4090 4798 -138 -219 -62 N ATOM 687 CA LEU A 86 18.575 29.705 24.434 1.00 33.05 C ANISOU 687 CA LEU A 86 4064 4061 4431 -11 -159 -82 C ATOM 688 C LEU A 86 18.289 30.864 25.413 1.00 32.59 C ANISOU 688 C LEU A 86 3990 4042 4350 -15 -146 -151 C ATOM 689 O LEU A 86 17.156 31.323 25.533 1.00 32.82 O ANISOU 689 O LEU A 86 3980 4047 4442 -50 -261 -307 O ATOM 690 CB LEU A 86 19.040 30.220 23.078 1.00 31.57 C ANISOU 690 CB LEU A 86 3726 4001 4268 84 -129 -25 C ATOM 691 CG LEU A 86 19.375 29.164 22.028 1.00 31.88 C ANISOU 691 CG LEU A 86 3890 3971 4249 130 -284 75 C ATOM 692 CD1 LEU A 86 19.836 29.806 20.727 1.00 32.26 C ANISOU 692 CD1 LEU A 86 4019 3914 4323 87 -107 -59 C ATOM 693 CD2 LEU A 86 20.476 28.210 22.557 1.00 31.15 C ANISOU 693 CD2 LEU A 86 3830 3575 4429 61 -40 13 C ATOM 694 N ILE A 87 19.327 31.301 26.124 1.00 31.46 N ANISOU 694 N ILE A 87 3915 3926 4110 -17 -159 -186 N ATOM 695 CA ILE A 87 19.240 32.441 27.035 1.00 30.66 C ANISOU 695 CA ILE A 87 3736 3859 4052 -12 -146 -37 C ATOM 696 C ILE A 87 18.946 33.703 26.247 1.00 27.65 C ANISOU 696 C ILE A 87 3234 3581 3692 -132 -214 -125 C ATOM 697 O ILE A 87 19.489 33.909 25.172 1.00 25.66 O ANISOU 697 O ILE A 87 2712 3443 3594 -378 -470 -293 O ATOM 698 CB ILE A 87 20.583 32.607 27.827 1.00 31.01 C ANISOU 698 CB ILE A 87 3935 3904 3940 -47 -164 -57 C ATOM 699 CG1 ILE A 87 20.627 31.592 28.980 1.00 31.39 C ANISOU 699 CG1 ILE A 87 3919 4044 3962 72 -202 39 C ATOM 700 CG2 ILE A 87 20.729 33.987 28.412 1.00 32.10 C ANISOU 700 CG2 ILE A 87 3991 3960 4244 -39 -151 -117 C ATOM 701 CD1 ILE A 87 21.971 31.077 29.234 1.00 32.06 C ANISOU 701 CD1 ILE A 87 4007 4161 4012 -1 -91 45 C ATOM 702 N ALA A 88 18.076 34.535 26.806 1.00 27.71 N ANISOU 702 N ALA A 88 3178 3495 3854 -134 -340 -91 N ATOM 703 CA ALA A 88 17.787 35.876 26.277 1.00 27.62 C ANISOU 703 CA ALA A 88 3250 3524 3718 -108 -131 15 C ATOM 704 C ALA A 88 18.396 36.906 27.224 1.00 25.86 C ANISOU 704 C ALA A 88 3019 3311 3493 -54 -120 -25 C ATOM 705 O ALA A 88 18.038 36.969 28.389 1.00 26.42 O ANISOU 705 O ALA A 88 2862 3440 3734 -217 -219 -163 O ATOM 706 CB ALA A 88 16.285 36.106 26.168 1.00 28.33 C ANISOU 706 CB ALA A 88 3273 3565 3926 -66 -216 160 C ATOM 707 N SER A 89 19.311 37.700 26.693 1.00 25.72 N ANISOU 707 N SER A 89 2935 3282 3555 -9 -186 -72 N ATOM 708 CA SER A 89 20.065 38.689 27.444 1.00 25.15 C ANISOU 708 CA SER A 89 3055 3199 3300 -9 -137 -69 C ATOM 709 C SER A 89 19.997 39.980 26.623 1.00 24.25 C ANISOU 709 C SER A 89 2879 3164 3170 2 -173 -44 C ATOM 710 O SER A 89 20.506 40.029 25.506 1.00 21.04 O ANISOU 710 O SER A 89 2647 2955 2392 -81 -655 -119 O ATOM 711 CB SER A 89 21.520 38.206 27.591 1.00 24.66 C ANISOU 711 CB SER A 89 2884 3153 3332 -2 -339 -144 C ATOM 712 OG SER A 89 22.391 39.164 28.227 1.00 23.96 O ANISOU 712 OG SER A 89 2539 2574 3990 -118 -436 -318 O ATOM 713 N ILE A 90 19.353 41.008 27.174 1.00 24.22 N ANISOU 713 N ILE A 90 2932 3006 3263 -111 -258 -94 N ATOM 714 CA ILE A 90 19.071 42.215 26.393 1.00 25.69 C ANISOU 714 CA ILE A 90 3188 3099 3471 -52 -137 -80 C ATOM 715 C ILE A 90 19.574 43.442 27.142 1.00 24.91 C ANISOU 715 C ILE A 90 3054 3108 3301 -120 -175 -126 C ATOM 716 O ILE A 90 19.985 43.312 28.271 1.00 26.28 O ANISOU 716 O ILE A 90 3167 3268 3548 -18 -25 -164 O ATOM 717 CB ILE A 90 17.568 42.375 26.116 1.00 24.76 C ANISOU 717 CB ILE A 90 3150 2922 3334 -111 -247 -85 C ATOM 718 CG1 ILE A 90 16.785 42.478 27.444 1.00 25.94 C ANISOU 718 CG1 ILE A 90 2938 3363 3554 -117 -169 -52 C ATOM 719 CG2 ILE A 90 17.063 41.221 25.205 1.00 24.92 C ANISOU 719 CG2 ILE A 90 3181 2847 3437 50 -275 -121 C ATOM 720 CD1 ILE A 90 15.492 43.254 27.377 1.00 26.87 C ANISOU 720 CD1 ILE A 90 3472 3293 3442 71 -122 -57 C ATOM 721 N SER A 91 19.527 44.601 26.478 1.00 26.23 N ANISOU 721 N SER A 91 3046 3252 3666 -112 -249 -77 N ATOM 722 CA SER A 91 19.868 45.893 27.068 1.00 25.83 C ANISOU 722 CA SER A 91 3171 3199 3442 -5 -76 -51 C ATOM 723 C SER A 91 18.636 46.800 27.131 1.00 26.70 C ANISOU 723 C SER A 91 3234 3442 3465 42 -46 -111 C ATOM 724 O SER A 91 17.768 46.752 26.256 1.00 26.51 O ANISOU 724 O SER A 91 3051 3248 3773 93 -75 -265 O ATOM 725 CB SER A 91 20.978 46.583 26.238 1.00 25.77 C ANISOU 725 CB SER A 91 3156 3241 3392 15 -76 -131 C ATOM 726 OG SER A 91 22.144 45.798 26.206 1.00 25.64 O ANISOU 726 OG SER A 91 2897 3352 3492 -2 -170 -48 O ATOM 727 N VAL A 92 18.562 47.619 28.175 1.00 26.61 N ANISOU 727 N VAL A 92 3178 3419 3512 -23 -89 -140 N ATOM 728 CA VAL A 92 17.525 48.653 28.294 1.00 26.92 C ANISOU 728 CA VAL A 92 3340 3437 3448 26 -69 -103 C ATOM 729 C VAL A 92 18.136 49.973 28.752 1.00 27.60 C ANISOU 729 C VAL A 92 3381 3491 3612 56 -62 -136 C ATOM 730 O VAL A 92 19.246 49.997 29.298 1.00 26.02 O ANISOU 730 O VAL A 92 3635 3311 2938 113 -498 -403 O ATOM 731 CB VAL A 92 16.410 48.260 29.286 1.00 26.52 C ANISOU 731 CB VAL A 92 3280 3418 3377 33 -23 -30 C ATOM 732 CG1 VAL A 92 15.805 46.934 28.921 1.00 28.52 C ANISOU 732 CG1 VAL A 92 3590 3655 3591 23 80 -125 C ATOM 733 CG2 VAL A 92 16.924 48.195 30.718 1.00 27.44 C ANISOU 733 CG2 VAL A 92 3350 3475 3600 89 -125 -68 C ATOM 734 N GLY A 93 17.402 51.056 28.515 1.00 28.18 N ANISOU 734 N GLY A 93 3483 3563 3659 54 -112 80 N ATOM 735 CA GLY A 93 17.747 52.388 29.003 1.00 28.93 C ANISOU 735 CA GLY A 93 3599 3591 3801 32 -129 -20 C ATOM 736 C GLY A 93 16.886 52.762 30.192 1.00 29.37 C ANISOU 736 C GLY A 93 3638 3673 3847 71 -55 10 C ATOM 737 O GLY A 93 16.364 51.883 30.916 1.00 31.21 O ANISOU 737 O GLY A 93 3800 3686 4371 244 33 -58 O ATOM 738 N VAL A 94 16.721 54.063 30.418 1.00 29.12 N ANISOU 738 N VAL A 94 3600 3702 3760 61 -166 89 N ATOM 739 CA VAL A 94 16.010 54.526 31.608 1.00 31.43 C ANISOU 739 CA VAL A 94 3868 3942 4129 78 -73 -71 C ATOM 740 C VAL A 94 14.870 55.531 31.346 1.00 33.20 C ANISOU 740 C VAL A 94 4065 4127 4422 98 -60 -72 C ATOM 741 O VAL A 94 14.233 55.988 32.299 1.00 33.22 O ANISOU 741 O VAL A 94 4112 3970 4538 160 -33 -192 O ATOM 742 CB VAL A 94 16.993 55.105 32.680 1.00 30.99 C ANISOU 742 CB VAL A 94 3872 3908 3993 137 -81 -89 C ATOM 743 CG1 VAL A 94 18.110 54.092 32.992 1.00 28.50 C ANISOU 743 CG1 VAL A 94 3496 3656 3673 -58 -324 -360 C ATOM 744 CG2 VAL A 94 17.577 56.423 32.244 1.00 31.21 C ANISOU 744 CG2 VAL A 94 3612 4077 4167 97 11 -98 C ATOM 745 N LYS A 95 14.628 55.833 30.072 1.00 33.92 N ANISOU 745 N LYS A 95 4212 4232 4443 100 -145 -18 N ATOM 746 CA LYS A 95 13.537 56.721 29.628 1.00 36.55 C ANISOU 746 CA LYS A 95 4550 4563 4772 137 -98 -19 C ATOM 747 C LYS A 95 12.128 56.124 29.802 1.00 36.92 C ANISOU 747 C LYS A 95 4518 4589 4920 123 -131 -4 C ATOM 748 O LYS A 95 11.943 54.908 29.986 1.00 34.43 O ANISOU 748 O LYS A 95 4056 4173 4850 382 -278 -128 O ATOM 749 CB LYS A 95 13.734 57.095 28.160 1.00 36.94 C ANISOU 749 CB LYS A 95 4690 4556 4788 146 -54 98 C ATOM 750 CG LYS A 95 14.747 58.211 27.911 1.00 41.84 C ANISOU 750 CG LYS A 95 5209 5296 5391 -45 47 -14 C ATOM 751 CD LYS A 95 14.866 58.541 26.403 1.00 41.16 C ANISOU 751 CD LYS A 95 5272 5256 5110 -2 13 53 C ATOM 752 CE LYS A 95 13.598 59.245 25.856 1.00 47.18 C ANISOU 752 CE LYS A 95 5921 6082 5922 138 -120 37 C ATOM 753 NZ LYS A 95 13.365 59.040 24.375 1.00 49.12 N ANISOU 753 NZ LYS A 95 6359 6516 5789 44 -138 96 N ATOM 754 N GLU A 96 11.126 57.008 29.720 1.00 38.03 N ANISOU 754 N GLU A 96 4751 4690 5008 143 -91 -20 N ATOM 755 CA GLU A 96 9.759 56.633 30.034 1.00 38.58 C ANISOU 755 CA GLU A 96 4775 4836 5048 141 -69 0 C ATOM 756 C GLU A 96 9.264 55.472 29.172 1.00 37.83 C ANISOU 756 C GLU A 96 4560 4736 5074 195 -56 33 C ATOM 757 O GLU A 96 8.578 54.581 29.679 1.00 39.57 O ANISOU 757 O GLU A 96 4639 4855 5540 195 -25 80 O ATOM 758 CB GLU A 96 8.831 57.846 29.919 1.00 39.20 C ANISOU 758 CB GLU A 96 4896 4927 5070 159 -51 -14 C ATOM 759 CG GLU A 96 7.402 57.604 30.364 1.00 39.41 C ANISOU 759 CG GLU A 96 4930 5008 5032 136 -71 13 C ATOM 760 CD GLU A 96 6.564 58.884 30.261 1.00 43.05 C ANISOU 760 CD GLU A 96 5260 5390 5704 289 17 -15 C ATOM 761 OE1 GLU A 96 6.581 59.703 31.219 1.00 49.74 O ANISOU 761 OE1 GLU A 96 6531 6281 6085 127 -73 -240 O ATOM 762 OE2 GLU A 96 5.905 59.073 29.208 1.00 50.47 O ANISOU 762 OE2 GLU A 96 6200 6690 6285 272 -272 22 O ATOM 763 N ASP A 97 9.635 55.455 27.898 1.00 35.62 N ANISOU 763 N ASP A 97 4325 4506 4704 206 -211 94 N ATOM 764 CA ASP A 97 9.262 54.346 27.026 1.00 37.06 C ANISOU 764 CA ASP A 97 4559 4646 4876 110 -145 65 C ATOM 765 C ASP A 97 9.858 52.989 27.433 1.00 36.76 C ANISOU 765 C ASP A 97 4517 4610 4838 106 -237 20 C ATOM 766 O ASP A 97 9.271 51.937 27.124 1.00 35.31 O ANISOU 766 O ASP A 97 4224 4549 4640 163 -382 59 O ATOM 767 CB ASP A 97 9.615 54.648 25.576 1.00 37.48 C ANISOU 767 CB ASP A 97 4770 4697 4771 8 -99 11 C ATOM 768 CG ASP A 97 11.081 54.940 25.385 1.00 44.31 C ANISOU 768 CG ASP A 97 5321 5738 5774 83 17 15 C ATOM 769 OD1 ASP A 97 11.810 55.119 26.396 1.00 48.74 O ANISOU 769 OD1 ASP A 97 6386 6519 5613 144 -72 -89 O ATOM 770 OD2 ASP A 97 11.514 55.020 24.216 1.00 50.54 O ANISOU 770 OD2 ASP A 97 6713 6598 5889 234 121 -20 O ATOM 771 N GLU A 98 11.004 53.006 28.130 1.00 36.09 N ANISOU 771 N GLU A 98 4330 4495 4885 83 -143 -26 N ATOM 772 CA GLU A 98 11.587 51.756 28.649 1.00 35.61 C ANISOU 772 CA GLU A 98 4361 4530 4639 35 -123 23 C ATOM 773 C GLU A 98 10.806 51.226 29.847 1.00 35.41 C ANISOU 773 C GLU A 98 4267 4529 4656 43 -120 -18 C ATOM 774 O GLU A 98 10.745 50.010 30.055 1.00 34.18 O ANISOU 774 O GLU A 98 3935 4534 4518 266 -52 66 O ATOM 775 CB GLU A 98 13.062 51.935 29.004 1.00 34.75 C ANISOU 775 CB GLU A 98 4274 4351 4579 46 -72 53 C ATOM 776 CG GLU A 98 13.932 52.322 27.846 1.00 31.24 C ANISOU 776 CG GLU A 98 3883 3847 4137 24 -155 -14 C ATOM 777 CD GLU A 98 14.124 51.222 26.823 1.00 34.71 C ANISOU 777 CD GLU A 98 4261 4140 4785 121 -196 -115 C ATOM 778 OE1 GLU A 98 15.136 50.503 26.906 1.00 32.94 O ANISOU 778 OE1 GLU A 98 3799 3858 4857 1 -392 -288 O ATOM 779 OE2 GLU A 98 13.286 51.092 25.900 1.00 37.19 O ANISOU 779 OE2 GLU A 98 4564 4386 5177 232 -411 -230 O ATOM 780 N TYR A 99 10.194 52.123 30.624 1.00 36.22 N ANISOU 780 N TYR A 99 4446 4540 4773 16 -106 -40 N ATOM 781 CA TYR A 99 9.225 51.711 31.635 1.00 37.02 C ANISOU 781 CA TYR A 99 4656 4670 4737 44 -39 -36 C ATOM 782 C TYR A 99 8.043 50.955 31.021 1.00 37.46 C ANISOU 782 C TYR A 99 4595 4739 4898 18 -17 18 C ATOM 783 O TYR A 99 7.592 49.951 31.573 1.00 36.43 O ANISOU 783 O TYR A 99 4323 4558 4960 -18 72 -16 O ATOM 784 CB TYR A 99 8.725 52.913 32.427 1.00 33.30 C ANISOU 784 CB TYR A 99 4020 4511 4119 -143 -546 -196 C ATOM 785 CG TYR A 99 9.714 53.371 33.459 1.00 36.66 C ANISOU 785 CG TYR A 99 4839 4424 4663 79 131 -223 C ATOM 786 CD1 TYR A 99 10.816 54.142 33.105 1.00 35.38 C ANISOU 786 CD1 TYR A 99 4594 4482 4366 -51 12 -50 C ATOM 787 CD2 TYR A 99 9.563 53.020 34.798 1.00 34.43 C ANISOU 787 CD2 TYR A 99 4482 4270 4327 54 -127 120 C ATOM 788 CE1 TYR A 99 11.729 54.577 34.063 1.00 35.84 C ANISOU 788 CE1 TYR A 99 4541 4503 4571 65 103 87 C ATOM 789 CE2 TYR A 99 10.490 53.444 35.764 1.00 36.58 C ANISOU 789 CE2 TYR A 99 4740 4328 4829 -72 82 -152 C ATOM 790 CZ TYR A 99 11.571 54.211 35.383 1.00 35.08 C ANISOU 790 CZ TYR A 99 4473 4441 4415 165 217 -171 C ATOM 791 OH TYR A 99 12.488 54.635 36.327 1.00 35.92 O ANISOU 791 OH TYR A 99 4460 4568 4618 242 37 -280 O ATOM 792 N GLU A 100 7.587 51.414 29.859 1.00 38.34 N ANISOU 792 N GLU A 100 4796 4854 4915 49 -88 -9 N ATOM 793 CA GLU A 100 6.456 50.788 29.166 1.00 39.05 C ANISOU 793 CA GLU A 100 4879 4924 5034 38 -69 -39 C ATOM 794 C GLU A 100 6.889 49.435 28.643 1.00 38.96 C ANISOU 794 C GLU A 100 4819 4875 5107 51 -66 6 C ATOM 795 O GLU A 100 6.129 48.467 28.710 1.00 39.37 O ANISOU 795 O GLU A 100 4628 4940 5391 133 -171 -6 O ATOM 796 CB GLU A 100 5.984 51.625 27.957 1.00 40.88 C ANISOU 796 CB GLU A 100 5211 5238 5083 26 -94 24 C ATOM 797 CG GLU A 100 5.876 53.158 28.168 1.00 46.96 C ANISOU 797 CG GLU A 100 6139 5656 6044 -52 -10 42 C ATOM 798 CD GLU A 100 4.546 53.647 28.737 1.00 54.11 C ANISOU 798 CD GLU A 100 6653 6894 7009 181 127 -22 C ATOM 799 OE1 GLU A 100 3.779 52.844 29.328 1.00 58.83 O ANISOU 799 OE1 GLU A 100 7322 7447 7582 -108 76 80 O ATOM 800 OE2 GLU A 100 4.279 54.866 28.596 1.00 57.09 O ANISOU 800 OE2 GLU A 100 7234 7025 7432 128 75 3 O ATOM 801 N PHE A 101 8.118 49.387 28.117 1.00 38.29 N ANISOU 801 N PHE A 101 4782 4827 4938 27 -26 -87 N ATOM 802 CA PHE A 101 8.683 48.186 27.480 1.00 38.43 C ANISOU 802 CA PHE A 101 4685 4897 5017 35 -55 -52 C ATOM 803 C PHE A 101 8.703 47.049 28.447 1.00 37.62 C ANISOU 803 C PHE A 101 4499 4803 4992 85 -36 -75 C ATOM 804 O PHE A 101 8.300 45.927 28.130 1.00 38.03 O ANISOU 804 O PHE A 101 4286 4966 5196 150 -158 -160 O ATOM 805 CB PHE A 101 10.093 48.486 26.949 1.00 34.66 C ANISOU 805 CB PHE A 101 4275 4056 4838 516 2 -248 C ATOM 806 CG PHE A 101 10.903 47.263 26.574 1.00 38.05 C ANISOU 806 CG PHE A 101 4807 4809 4840 -3 -119 -53 C ATOM 807 CD1 PHE A 101 10.621 46.540 25.413 1.00 38.49 C ANISOU 807 CD1 PHE A 101 5044 4677 4900 46 126 -169 C ATOM 808 CD2 PHE A 101 11.977 46.861 27.370 1.00 34.07 C ANISOU 808 CD2 PHE A 101 4273 4154 4515 -61 -126 -199 C ATOM 809 CE1 PHE A 101 11.395 45.424 25.062 1.00 38.87 C ANISOU 809 CE1 PHE A 101 4794 4820 5152 -13 -107 -24 C ATOM 810 CE2 PHE A 101 12.760 45.755 27.026 1.00 35.37 C ANISOU 810 CE2 PHE A 101 4372 4545 4522 -81 -230 16 C ATOM 811 CZ PHE A 101 12.468 45.030 25.874 1.00 36.43 C ANISOU 811 CZ PHE A 101 4762 4608 4471 162 -85 -109 C ATOM 812 N VAL A 102 9.186 47.355 29.639 1.00 37.44 N ANISOU 812 N VAL A 102 4517 4717 4991 48 40 -101 N ATOM 813 CA VAL A 102 9.240 46.422 30.728 1.00 38.76 C ANISOU 813 CA VAL A 102 4741 4861 5123 76 6 -47 C ATOM 814 C VAL A 102 7.840 45.950 31.117 1.00 40.27 C ANISOU 814 C VAL A 102 4825 5035 5439 18 -68 -36 C ATOM 815 O VAL A 102 7.612 44.750 31.328 1.00 40.55 O ANISOU 815 O VAL A 102 4750 5065 5593 66 -182 -47 O ATOM 816 CB VAL A 102 9.984 47.075 31.911 1.00 37.84 C ANISOU 816 CB VAL A 102 4595 4765 5015 43 56 -46 C ATOM 817 CG1 VAL A 102 9.763 46.328 33.227 1.00 36.92 C ANISOU 817 CG1 VAL A 102 4462 4661 4903 121 115 -98 C ATOM 818 CG2 VAL A 102 11.489 47.174 31.568 1.00 34.42 C ANISOU 818 CG2 VAL A 102 4219 4477 4379 40 -80 -56 C ATOM 819 N GLN A 103 6.897 46.889 31.198 1.00 40.82 N ANISOU 819 N GLN A 103 4887 5108 5513 11 0 -119 N ATOM 820 CA GLN A 103 5.522 46.529 31.546 1.00 42.00 C ANISOU 820 CA GLN A 103 5091 5309 5557 43 32 -14 C ATOM 821 C GLN A 103 4.946 45.612 30.468 1.00 42.65 C ANISOU 821 C GLN A 103 5149 5397 5657 57 -7 9 C ATOM 822 O GLN A 103 4.292 44.608 30.764 1.00 44.17 O ANISOU 822 O GLN A 103 5242 5489 6049 116 -47 24 O ATOM 823 CB GLN A 103 4.686 47.789 31.752 1.00 41.46 C ANISOU 823 CB GLN A 103 5031 5213 5506 14 65 7 C ATOM 824 CG GLN A 103 5.124 48.540 33.001 1.00 43.00 C ANISOU 824 CG GLN A 103 5351 5370 5615 30 -44 -38 C ATOM 825 CD GLN A 103 4.388 49.854 33.192 1.00 43.99 C ANISOU 825 CD GLN A 103 5395 5489 5829 85 39 -38 C ATOM 826 OE1 GLN A 103 3.189 49.851 33.404 1.00 48.94 O ANISOU 826 OE1 GLN A 103 5726 6452 6414 104 382 26 O ATOM 827 NE2 GLN A 103 5.099 50.977 33.101 1.00 44.09 N ANISOU 827 NE2 GLN A 103 5352 5453 5947 -14 15 -203 N ATOM 828 N GLN A 104 5.223 45.945 29.221 1.00 42.86 N ANISOU 828 N GLN A 104 5233 5449 5600 97 -12 10 N ATOM 829 CA GLN A 104 4.876 45.093 28.109 1.00 43.57 C ANISOU 829 CA GLN A 104 5355 5528 5671 46 -37 -9 C ATOM 830 C GLN A 104 5.338 43.662 28.315 1.00 44.23 C ANISOU 830 C GLN A 104 5428 5597 5781 38 -107 -49 C ATOM 831 O GLN A 104 4.594 42.718 28.084 1.00 43.90 O ANISOU 831 O GLN A 104 5153 5518 6008 78 -227 -24 O ATOM 832 CB GLN A 104 5.513 45.634 26.850 1.00 43.75 C ANISOU 832 CB GLN A 104 5458 5532 5631 5 40 -56 C ATOM 833 CG GLN A 104 4.816 45.255 25.589 1.00 44.49 C ANISOU 833 CG GLN A 104 5551 5698 5652 40 -26 -25 C ATOM 834 CD GLN A 104 5.402 45.979 24.393 1.00 46.77 C ANISOU 834 CD GLN A 104 5889 5963 5917 56 70 135 C ATOM 835 OE1 GLN A 104 6.247 46.849 24.548 1.00 52.29 O ANISOU 835 OE1 GLN A 104 6508 6647 6709 -188 -127 -68 O ATOM 836 NE2 GLN A 104 4.956 45.618 23.205 1.00 51.95 N ANISOU 836 NE2 GLN A 104 6780 6508 6449 -92 -66 -140 N ATOM 837 N LEU A 105 6.589 43.506 28.717 1.00 43.78 N ANISOU 837 N LEU A 105 5402 5570 5660 32 -124 -35 N ATOM 838 CA LEU A 105 7.171 42.191 28.858 1.00 44.90 C ANISOU 838 CA LEU A 105 5522 5692 5845 61 -99 30 C ATOM 839 C LEU A 105 6.393 41.442 29.935 1.00 45.35 C ANISOU 839 C LEU A 105 5515 5824 5891 62 -84 29 C ATOM 840 O LEU A 105 6.152 40.248 29.829 1.00 44.98 O ANISOU 840 O LEU A 105 5349 5883 5859 24 -88 12 O ATOM 841 CB LEU A 105 8.653 42.310 29.242 1.00 44.86 C ANISOU 841 CB LEU A 105 5543 5661 5837 22 -37 9 C ATOM 842 CG LEU A 105 9.644 42.623 28.120 1.00 43.27 C ANISOU 842 CG LEU A 105 5248 5584 5607 19 -81 -36 C ATOM 843 CD1 LEU A 105 11.050 42.829 28.639 1.00 40.27 C ANISOU 843 CD1 LEU A 105 5118 5085 5097 3 -65 -131 C ATOM 844 CD2 LEU A 105 9.621 41.565 27.044 1.00 42.86 C ANISOU 844 CD2 LEU A 105 5214 5397 5675 -15 -49 3 C ATOM 845 N ALA A 106 5.989 42.161 30.970 1.00 46.49 N ANISOU 845 N ALA A 106 5702 5984 5977 77 -70 30 N ATOM 846 CA ALA A 106 5.420 41.524 32.140 1.00 48.43 C ANISOU 846 CA ALA A 106 6049 6182 6169 56 -7 39 C ATOM 847 C ALA A 106 4.055 40.950 31.820 1.00 51.47 C ANISOU 847 C ALA A 106 6392 6569 6592 -1 -6 25 C ATOM 848 O ALA A 106 3.507 40.183 32.592 1.00 53.20 O ANISOU 848 O ALA A 106 6583 6830 6798 1 104 21 O ATOM 849 CB ALA A 106 5.333 42.497 33.291 1.00 48.83 C ANISOU 849 CB ALA A 106 6110 6185 6258 9 -17 14 C ATOM 850 N ALA A 107 3.521 41.335 30.667 1.00 53.46 N ANISOU 850 N ALA A 107 6619 6893 6798 -15 -36 0 N ATOM 851 CA ALA A 107 2.102 41.194 30.394 1.00 54.77 C ANISOU 851 CA ALA A 107 6852 6995 6963 17 -10 16 C ATOM 852 C ALA A 107 1.954 40.044 29.435 1.00 55.91 C ANISOU 852 C ALA A 107 6927 7130 7187 36 -37 -27 C ATOM 853 O ALA A 107 1.006 39.283 29.503 1.00 56.85 O ANISOU 853 O ALA A 107 7064 7138 7397 87 -27 -27 O ATOM 854 CB ALA A 107 1.570 42.443 29.775 1.00 55.26 C ANISOU 854 CB ALA A 107 6893 7078 7024 60 12 -17 C ATOM 855 N GLU A 108 2.930 39.919 28.546 1.00 56.20 N ANISOU 855 N GLU A 108 7022 7116 7213 48 -44 -55 N ATOM 856 CA GLU A 108 3.150 38.678 27.835 1.00 55.93 C ANISOU 856 CA GLU A 108 7021 7106 7121 22 -38 1 C ATOM 857 C GLU A 108 3.946 37.653 28.589 1.00 54.57 C ANISOU 857 C GLU A 108 6696 7028 7008 -49 -30 -50 C ATOM 858 O GLU A 108 4.326 36.639 28.032 1.00 53.66 O ANISOU 858 O GLU A 108 6320 7058 7009 -79 3 -76 O ATOM 859 CB GLU A 108 3.814 38.944 26.518 1.00 56.80 C ANISOU 859 CB GLU A 108 7141 7226 7213 -32 13 15 C ATOM 860 CG GLU A 108 3.540 40.323 25.997 1.00 56.87 C ANISOU 860 CG GLU A 108 7079 7251 7277 -4 -23 -28 C ATOM 861 CD GLU A 108 3.954 40.418 24.568 1.00 58.55 C ANISOU 861 CD GLU A 108 7479 7455 7310 -24 35 19 C ATOM 862 OE1 GLU A 108 5.120 40.110 24.303 1.00 62.28 O ANISOU 862 OE1 GLU A 108 7752 8095 7816 70 -64 134 O ATOM 863 OE2 GLU A 108 3.111 40.761 23.729 1.00 63.22 O ANISOU 863 OE2 GLU A 108 7897 8320 7801 -92 131 -35 O ATOM 864 N HIS A 109 4.184 37.902 29.862 1.00 53.45 N ANISOU 864 N HIS A 109 6577 6825 6906 -54 13 36 N ATOM 865 CA HIS A 109 4.947 36.962 30.641 1.00 52.53 C ANISOU 865 CA HIS A 109 6514 6694 6748 -53 57 -1 C ATOM 866 C HIS A 109 6.152 36.481 29.843 1.00 51.14 C ANISOU 866 C HIS A 109 6317 6426 6686 -56 -25 42 C ATOM 867 O HIS A 109 6.422 35.288 29.769 1.00 51.74 O ANISOU 867 O HIS A 109 6309 6494 6854 -127 -75 -43 O ATOM 868 CB HIS A 109 4.056 35.786 31.024 1.00 54.76 C ANISOU 868 CB HIS A 109 6915 6867 7022 -103 -43 41 C ATOM 869 CG HIS A 109 2.954 36.156 31.964 1.00 59.17 C ANISOU 869 CG HIS A 109 7378 7552 7552 -3 152 -37 C ATOM 870 ND1 HIS A 109 1.638 36.247 31.570 1.00 62.06 N ANISOU 870 ND1 HIS A 109 7588 7979 8010 95 35 -30 N ATOM 871 CD2 HIS A 109 2.978 36.488 33.275 1.00 61.85 C ANISOU 871 CD2 HIS A 109 7817 8008 7672 -16 -12 0 C ATOM 872 CE1 HIS A 109 0.897 36.605 32.601 1.00 63.03 C ANISOU 872 CE1 HIS A 109 7744 8145 8058 75 41 11 C ATOM 873 NE2 HIS A 109 1.686 36.761 33.647 1.00 63.38 N ANISOU 873 NE2 HIS A 109 7899 8193 7989 82 20 -29 N ATOM 874 N LEU A 110 6.875 37.425 29.248 1.00 48.16 N ANISOU 874 N LEU A 110 5923 6088 6287 38 -59 51 N ATOM 875 CA LEU A 110 8.261 37.212 28.885 1.00 45.84 C ANISOU 875 CA LEU A 110 5763 5770 5884 -9 -116 -2 C ATOM 876 C LEU A 110 9.216 37.747 29.943 1.00 44.02 C ANISOU 876 C LEU A 110 5477 5529 5720 4 -79 -6 C ATOM 877 O LEU A 110 9.179 38.915 30.290 1.00 44.34 O ANISOU 877 O LEU A 110 5391 5583 5871 -55 -145 -86 O ATOM 878 CB LEU A 110 8.566 37.872 27.560 1.00 45.64 C ANISOU 878 CB LEU A 110 5733 5810 5797 35 -14 -70 C ATOM 879 CG LEU A 110 7.866 37.287 26.355 1.00 45.72 C ANISOU 879 CG LEU A 110 5680 5792 5897 -30 -125 -61 C ATOM 880 CD1 LEU A 110 8.272 38.068 25.157 1.00 45.76 C ANISOU 880 CD1 LEU A 110 5619 5762 6004 -48 -39 -17 C ATOM 881 CD2 LEU A 110 8.284 35.845 26.215 1.00 46.63 C ANISOU 881 CD2 LEU A 110 5732 5842 6143 -36 -186 -25 C ATOM 882 N THR A 111 10.056 36.864 30.455 1.00 41.27 N ANISOU 882 N THR A 111 5063 5215 5403 -46 -43 -67 N ATOM 883 CA THR A 111 11.120 37.245 31.372 1.00 39.18 C ANISOU 883 CA THR A 111 4808 4919 5159 -16 97 -11 C ATOM 884 C THR A 111 12.478 36.865 30.762 1.00 36.93 C ANISOU 884 C THR A 111 4422 4540 5070 -44 54 31 C ATOM 885 O THR A 111 12.804 35.674 30.677 1.00 35.44 O ANISOU 885 O THR A 111 3964 4364 5135 -120 48 208 O ATOM 886 CB THR A 111 10.931 36.602 32.737 1.00 39.68 C ANISOU 886 CB THR A 111 4934 4950 5192 -22 43 -1 C ATOM 887 OG1 THR A 111 9.688 37.045 33.288 1.00 41.29 O ANISOU 887 OG1 THR A 111 5027 5153 5507 -76 -9 -72 O ATOM 888 CG2 THR A 111 12.035 37.012 33.678 1.00 40.48 C ANISOU 888 CG2 THR A 111 5024 5124 5232 -40 -34 38 C ATOM 889 N PRO A 112 13.256 37.882 30.301 1.00 34.58 N ANISOU 889 N PRO A 112 4175 4287 4675 25 63 13 N ATOM 890 CA PRO A 112 14.607 37.582 29.774 1.00 32.42 C ANISOU 890 CA PRO A 112 4008 4017 4293 -30 -106 -4 C ATOM 891 C PRO A 112 15.484 37.141 30.946 1.00 30.34 C ANISOU 891 C PRO A 112 3608 3770 4149 -106 -86 -107 C ATOM 892 O PRO A 112 15.272 37.600 32.057 1.00 28.74 O ANISOU 892 O PRO A 112 3182 3683 4052 -172 -121 -97 O ATOM 893 CB PRO A 112 15.070 38.906 29.127 1.00 32.42 C ANISOU 893 CB PRO A 112 3935 4171 4212 -56 -126 -104 C ATOM 894 CG PRO A 112 14.127 39.956 29.579 1.00 33.28 C ANISOU 894 CG PRO A 112 4163 4131 4350 -53 -43 0 C ATOM 895 CD PRO A 112 12.940 39.323 30.276 1.00 33.90 C ANISOU 895 CD PRO A 112 4123 4255 4502 -46 14 23 C ATOM 896 N GLU A 113 16.415 36.210 30.707 1.00 28.50 N ANISOU 896 N GLU A 113 3413 3476 3939 -247 -219 -106 N ATOM 897 CA GLU A 113 17.229 35.692 31.786 1.00 26.74 C ANISOU 897 CA GLU A 113 3307 3231 3622 -201 -91 -120 C ATOM 898 C GLU A 113 18.078 36.849 32.368 1.00 24.24 C ANISOU 898 C GLU A 113 2947 3077 3186 -149 -118 -133 C ATOM 899 O GLU A 113 18.381 36.876 33.570 1.00 24.81 O ANISOU 899 O GLU A 113 3055 3022 3347 -232 116 -201 O ATOM 900 CB GLU A 113 18.148 34.600 31.254 1.00 28.02 C ANISOU 900 CB GLU A 113 3540 3394 3712 -175 -152 -184 C ATOM 901 CG GLU A 113 17.493 33.194 31.126 1.00 26.90 C ANISOU 901 CG GLU A 113 3284 3139 3797 -153 -108 -115 C ATOM 902 CD GLU A 113 16.581 33.026 29.906 1.00 30.97 C ANISOU 902 CD GLU A 113 3953 3946 3867 3 -156 -37 C ATOM 903 OE1 GLU A 113 16.404 33.961 29.092 1.00 29.29 O ANISOU 903 OE1 GLU A 113 3509 3186 4434 -308 -289 -166 O ATOM 904 OE2 GLU A 113 16.039 31.906 29.763 1.00 37.29 O ANISOU 904 OE2 GLU A 113 4418 4548 5202 -377 -170 -61 O ATOM 905 N TYR A 114 18.486 37.740 31.476 1.00 23.52 N ANISOU 905 N TYR A 114 2826 3018 3089 -180 -181 -123 N ATOM 906 CA TYR A 114 19.398 38.857 31.768 1.00 22.61 C ANISOU 906 CA TYR A 114 2920 2894 2774 -117 -89 -94 C ATOM 907 C TYR A 114 18.920 40.175 31.159 1.00 22.91 C ANISOU 907 C TYR A 114 2712 3038 2954 41 -113 -130 C ATOM 908 O TYR A 114 18.645 40.269 29.942 1.00 20.81 O ANISOU 908 O TYR A 114 2356 2756 2791 117 -199 201 O ATOM 909 CB TYR A 114 20.836 38.560 31.281 1.00 22.60 C ANISOU 909 CB TYR A 114 2870 2964 2750 -189 -188 -193 C ATOM 910 CG TYR A 114 21.470 37.353 31.919 1.00 23.18 C ANISOU 910 CG TYR A 114 2962 2954 2888 19 22 -136 C ATOM 911 CD1 TYR A 114 22.130 37.448 33.149 1.00 22.86 C ANISOU 911 CD1 TYR A 114 2898 2951 2835 -192 -257 115 C ATOM 912 CD2 TYR A 114 21.360 36.100 31.341 1.00 26.60 C ANISOU 912 CD2 TYR A 114 2987 3168 3952 -180 -298 -140 C ATOM 913 CE1 TYR A 114 22.686 36.308 33.768 1.00 23.67 C ANISOU 913 CE1 TYR A 114 2626 3162 3206 154 -85 -152 C ATOM 914 CE2 TYR A 114 21.931 34.964 31.951 1.00 25.69 C ANISOU 914 CE2 TYR A 114 3415 2976 3369 -216 -116 144 C ATOM 915 CZ TYR A 114 22.576 35.077 33.163 1.00 26.00 C ANISOU 915 CZ TYR A 114 2942 3140 3795 -106 -239 60 C ATOM 916 OH TYR A 114 23.109 33.945 33.762 1.00 26.26 O ANISOU 916 OH TYR A 114 3205 2970 3802 -13 -20 170 O ATOM 917 N ILE A 115 18.876 41.207 32.011 1.00 23.30 N ANISOU 917 N ILE A 115 2562 2998 3290 25 5 -87 N ATOM 918 CA ILE A 115 18.676 42.567 31.526 1.00 23.11 C ANISOU 918 CA ILE A 115 2807 2919 3053 -81 -63 2 C ATOM 919 C ILE A 115 19.826 43.483 31.995 1.00 22.75 C ANISOU 919 C ILE A 115 2710 3050 2884 -38 -119 -65 C ATOM 920 O ILE A 115 20.098 43.595 33.198 1.00 21.17 O ANISOU 920 O ILE A 115 2230 3089 2725 -4 -217 -251 O ATOM 921 CB ILE A 115 17.352 43.167 32.009 1.00 23.53 C ANISOU 921 CB ILE A 115 2801 2938 3200 -39 -35 25 C ATOM 922 CG1 ILE A 115 16.162 42.298 31.597 1.00 23.87 C ANISOU 922 CG1 ILE A 115 2960 2831 3277 36 14 24 C ATOM 923 CG2 ILE A 115 17.167 44.614 31.473 1.00 24.16 C ANISOU 923 CG2 ILE A 115 2798 3078 3303 48 -64 13 C ATOM 924 CD1 ILE A 115 14.852 42.696 32.355 1.00 25.78 C ANISOU 924 CD1 ILE A 115 3004 3340 3450 -47 -30 -13 C ATOM 925 N THR A 116 20.451 44.145 31.034 1.00 20.55 N ANISOU 925 N THR A 116 2540 2839 2426 -116 -21 -65 N ATOM 926 CA THR A 116 21.497 45.142 31.280 1.00 22.07 C ANISOU 926 CA THR A 116 2788 2877 2719 -45 -48 -72 C ATOM 927 C THR A 116 20.985 46.574 31.049 1.00 20.73 C ANISOU 927 C THR A 116 2632 2688 2555 30 -69 5 C ATOM 928 O THR A 116 20.626 46.975 29.941 1.00 20.58 O ANISOU 928 O THR A 116 2556 2750 2512 91 -163 -4 O ATOM 929 CB THR A 116 22.753 44.863 30.412 1.00 19.35 C ANISOU 929 CB THR A 116 2628 2597 2126 -27 -121 -243 C ATOM 930 OG1 THR A 116 23.278 43.585 30.764 1.00 20.38 O ANISOU 930 OG1 THR A 116 2715 2707 2320 4 -488 -100 O ATOM 931 CG2 THR A 116 23.856 45.904 30.582 1.00 19.33 C ANISOU 931 CG2 THR A 116 2651 2600 2094 -18 198 -22 C ATOM 932 N ILE A 117 20.976 47.343 32.121 1.00 20.52 N ANISOU 932 N ILE A 117 2532 2815 2450 -9 -67 -51 N ATOM 933 CA ILE A 117 20.662 48.760 32.059 1.00 22.89 C ANISOU 933 CA ILE A 117 2970 2950 2777 50 -29 -91 C ATOM 934 C ILE A 117 21.935 49.490 31.624 1.00 23.37 C ANISOU 934 C ILE A 117 3051 2906 2920 17 -41 -80 C ATOM 935 O ILE A 117 22.915 49.518 32.362 1.00 23.30 O ANISOU 935 O ILE A 117 3097 2522 3231 -56 -151 -207 O ATOM 936 CB ILE A 117 20.211 49.296 33.446 1.00 21.81 C ANISOU 936 CB ILE A 117 2994 2862 2430 -63 -74 -31 C ATOM 937 CG1 ILE A 117 18.974 48.546 33.945 1.00 23.84 C ANISOU 937 CG1 ILE A 117 2968 3363 2728 118 -79 -135 C ATOM 938 CG2 ILE A 117 20.001 50.825 33.369 1.00 20.89 C ANISOU 938 CG2 ILE A 117 2672 2817 2448 177 -280 -160 C ATOM 939 CD1 ILE A 117 18.630 48.887 35.411 1.00 23.38 C ANISOU 939 CD1 ILE A 117 2854 3201 2827 49 139 -3 C ATOM 940 N ASP A 118 21.961 50.061 30.426 1.00 24.96 N ANISOU 940 N ASP A 118 3221 3067 3193 39 -80 -1 N ATOM 941 CA AASP A 118 23.218 50.509 29.847 0.50 26.06 C ANISOU 941 CA AASP A 118 3354 3254 3290 -2 22 4 C ATOM 942 C ASP A 118 23.240 52.032 29.610 1.00 26.24 C ANISOU 942 C ASP A 118 3398 3222 3349 3 -28 -51 C ATOM 943 O ASP A 118 22.716 52.496 28.638 1.00 24.45 O ANISOU 943 O ASP A 118 3529 2783 2976 -112 -211 -102 O ATOM 944 CB AASP A 118 23.551 49.587 28.625 0.50 27.89 C ANISOU 944 CB AASP A 118 3719 3408 3470 -41 44 -115 C ATOM 945 CG AASP A 118 23.720 50.315 27.293 0.50 26.07 C ANISOU 945 CG AASP A 118 3362 2978 3564 12 -72 22 C ATOM 946 OD1AASP A 118 24.835 50.742 26.986 0.50 25.19 O ANISOU 946 OD1AASP A 118 2953 2953 3662 36 -380 -164 O ATOM 947 OD2AASP A 118 22.779 50.358 26.481 0.50 26.53 O ANISOU 947 OD2AASP A 118 3165 2701 4214 97 -258 -268 O ATOM 948 N ILE A 119 23.851 52.763 30.546 1.00 27.26 N ANISOU 948 N ILE A 119 3300 3465 3590 -23 -89 10 N ATOM 949 CA ILE A 119 23.889 54.216 30.578 1.00 27.01 C ANISOU 949 CA ILE A 119 3374 3415 3471 -51 -71 36 C ATOM 950 C ILE A 119 25.361 54.678 30.824 1.00 27.05 C ANISOU 950 C ILE A 119 3295 3413 3568 -28 -76 156 C ATOM 951 O ILE A 119 26.110 54.044 31.592 1.00 26.64 O ANISOU 951 O ILE A 119 3376 3159 3585 -52 -116 286 O ATOM 952 CB ILE A 119 22.898 54.699 31.708 1.00 28.32 C ANISOU 952 CB ILE A 119 3400 3584 3775 23 -46 -26 C ATOM 953 CG1 ILE A 119 21.430 54.417 31.322 1.00 28.06 C ANISOU 953 CG1 ILE A 119 3518 3623 3520 28 -133 99 C ATOM 954 CG2 ILE A 119 23.088 56.120 32.090 1.00 28.18 C ANISOU 954 CG2 ILE A 119 3378 3420 3907 -128 -175 87 C ATOM 955 CD1 ILE A 119 21.044 54.967 29.946 1.00 31.23 C ANISOU 955 CD1 ILE A 119 4103 4029 3733 51 -124 112 C ATOM 956 N ALA A 120 25.779 55.755 30.157 1.00 25.79 N ANISOU 956 N ALA A 120 3203 3171 3425 56 -73 123 N ATOM 957 CA ALA A 120 27.165 56.227 30.260 1.00 25.05 C ANISOU 957 CA ALA A 120 3190 3114 3212 111 -79 47 C ATOM 958 C ALA A 120 27.521 56.540 31.698 1.00 24.32 C ANISOU 958 C ALA A 120 3093 3046 3101 152 -97 9 C ATOM 959 O ALA A 120 28.549 56.096 32.185 1.00 26.28 O ANISOU 959 O ALA A 120 2935 3419 3628 256 -81 -113 O ATOM 960 CB ALA A 120 27.407 57.450 29.420 1.00 25.31 C ANISOU 960 CB ALA A 120 3328 3301 2987 122 -61 88 C ATOM 961 N HIS A 121 26.677 57.319 32.363 1.00 22.77 N ANISOU 961 N HIS A 121 2795 2845 3010 39 -116 -14 N ATOM 962 CA HIS A 121 26.906 57.747 33.745 1.00 23.05 C ANISOU 962 CA HIS A 121 2924 2906 2925 89 -77 88 C ATOM 963 C HIS A 121 25.809 57.106 34.622 1.00 23.26 C ANISOU 963 C HIS A 121 2911 2915 3011 118 -25 4 C ATOM 964 O HIS A 121 24.772 57.702 34.947 1.00 22.06 O ANISOU 964 O HIS A 121 2784 3024 2572 219 62 7 O ATOM 965 CB HIS A 121 26.965 59.286 33.865 1.00 22.80 C ANISOU 965 CB HIS A 121 2819 3043 2801 -8 -104 -18 C ATOM 966 CG HIS A 121 27.364 59.762 35.228 1.00 21.32 C ANISOU 966 CG HIS A 121 2656 2649 2796 -163 -153 -51 C ATOM 967 ND1 HIS A 121 27.261 61.082 35.627 1.00 24.35 N ANISOU 967 ND1 HIS A 121 3138 3006 3107 1 -52 179 N ATOM 968 CD2 HIS A 121 27.801 59.074 36.314 1.00 15.02 C ANISOU 968 CD2 HIS A 121 1741 1787 2177 -73 373 -65 C ATOM 969 CE1 HIS A 121 27.682 61.193 36.877 1.00 18.62 C ANISOU 969 CE1 HIS A 121 2363 2184 2526 13 2 -288 C ATOM 970 NE2 HIS A 121 28.002 59.987 37.318 1.00 20.20 N ANISOU 970 NE2 HIS A 121 2468 2875 2332 -343 -187 32 N ATOM 971 N GLY A 122 26.057 55.859 34.986 1.00 21.55 N ANISOU 971 N GLY A 122 2883 2654 2648 115 -153 159 N ATOM 972 CA GLY A 122 25.016 54.997 35.527 1.00 22.32 C ANISOU 972 CA GLY A 122 2726 2878 2874 71 -40 0 C ATOM 973 C GLY A 122 24.755 55.167 37.016 1.00 23.88 C ANISOU 973 C GLY A 122 2949 3098 3026 -9 63 -86 C ATOM 974 O GLY A 122 23.752 54.644 37.517 1.00 23.95 O ANISOU 974 O GLY A 122 2923 2977 3197 -125 62 -300 O ATOM 975 N HIS A 123 25.656 55.854 37.736 1.00 23.95 N ANISOU 975 N HIS A 123 2915 3004 3178 -36 13 -75 N ATOM 976 CA HIS A 123 25.401 56.227 39.135 1.00 24.81 C ANISOU 976 CA HIS A 123 3136 3138 3152 -28 -5 19 C ATOM 977 C HIS A 123 24.383 57.389 39.104 1.00 26.13 C ANISOU 977 C HIS A 123 3387 3207 3332 2 -27 -5 C ATOM 978 O HIS A 123 24.763 58.548 39.008 1.00 26.91 O ANISOU 978 O HIS A 123 3687 3150 3386 -99 -331 -52 O ATOM 979 CB HIS A 123 26.707 56.611 39.879 1.00 23.25 C ANISOU 979 CB HIS A 123 3063 2655 3115 -16 25 96 C ATOM 980 CG HIS A 123 26.564 56.740 41.365 1.00 24.25 C ANISOU 980 CG HIS A 123 2999 2820 3391 -77 26 -135 C ATOM 981 ND1 HIS A 123 27.521 57.340 42.162 1.00 24.97 N ANISOU 981 ND1 HIS A 123 3198 3204 3085 9 -38 34 N ATOM 982 CD2 HIS A 123 25.573 56.349 42.201 1.00 23.40 C ANISOU 982 CD2 HIS A 123 3003 2839 3047 208 -33 131 C ATOM 983 CE1 HIS A 123 27.114 57.327 43.415 1.00 24.71 C ANISOU 983 CE1 HIS A 123 3059 2900 3427 30 132 -43 C ATOM 984 NE2 HIS A 123 25.940 56.723 43.466 1.00 25.21 N ANISOU 984 NE2 HIS A 123 2820 3275 3482 88 -127 -236 N ATOM 985 N SER A 124 23.091 57.054 39.115 1.00 28.21 N ANISOU 985 N SER A 124 3549 3541 3628 -45 -22 -54 N ATOM 986 CA SER A 124 21.994 58.052 39.022 1.00 28.99 C ANISOU 986 CA SER A 124 3644 3618 3750 75 -16 -46 C ATOM 987 C SER A 124 20.668 57.517 39.556 1.00 30.47 C ANISOU 987 C SER A 124 3664 3796 4117 125 -37 -119 C ATOM 988 O SER A 124 20.433 56.299 39.619 1.00 29.18 O ANISOU 988 O SER A 124 3399 3514 4174 343 41 -183 O ATOM 989 CB SER A 124 21.777 58.484 37.575 1.00 31.00 C ANISOU 989 CB SER A 124 3951 3868 3959 -40 -53 -20 C ATOM 990 OG SER A 124 21.136 57.459 36.834 1.00 33.98 O ANISOU 990 OG SER A 124 4185 4391 4335 -81 -288 -214 O ATOM 991 N ASN A 125 19.758 58.422 39.921 1.00 31.16 N ANISOU 991 N ASN A 125 3856 3797 4183 79 14 -226 N ATOM 992 CA ASN A 125 18.444 57.948 40.374 1.00 31.40 C ANISOU 992 CA ASN A 125 3906 3894 4129 140 54 -99 C ATOM 993 C ASN A 125 17.626 57.381 39.229 1.00 30.70 C ANISOU 993 C ASN A 125 3797 3708 4160 231 55 -100 C ATOM 994 O ASN A 125 16.744 56.543 39.452 1.00 32.07 O ANISOU 994 O ASN A 125 3961 3715 4508 241 82 -229 O ATOM 995 CB ASN A 125 17.709 59.037 41.141 1.00 33.26 C ANISOU 995 CB ASN A 125 4178 4048 4411 142 59 -191 C ATOM 996 CG ASN A 125 18.350 59.290 42.487 1.00 39.58 C ANISOU 996 CG ASN A 125 5256 5078 4705 99 -20 -75 C ATOM 997 OD1 ASN A 125 18.328 58.422 43.372 1.00 40.87 O ANISOU 997 OD1 ASN A 125 5424 4899 5203 252 276 50 O ATOM 998 ND2 ASN A 125 18.998 60.455 42.630 1.00 45.34 N ANISOU 998 ND2 ASN A 125 5822 5592 5814 -207 84 -127 N ATOM 999 N ALA A 126 17.962 57.806 38.006 1.00 29.89 N ANISOU 999 N ALA A 126 3815 3511 4030 300 -36 -70 N ATOM 1000 CA ALA A 126 17.349 57.265 36.789 1.00 29.92 C ANISOU 1000 CA ALA A 126 3734 3630 4002 140 -52 0 C ATOM 1001 C ALA A 126 17.596 55.768 36.707 1.00 29.34 C ANISOU 1001 C ALA A 126 3550 3603 3993 98 -125 -45 C ATOM 1002 O ALA A 126 16.682 55.007 36.459 1.00 28.50 O ANISOU 1002 O ALA A 126 3199 3643 3984 199 -391 130 O ATOM 1003 CB ALA A 126 17.916 57.935 35.568 1.00 30.67 C ANISOU 1003 CB ALA A 126 3952 3622 4076 193 -13 8 C ATOM 1004 N VAL A 127 18.842 55.358 36.952 1.00 28.80 N ANISOU 1004 N VAL A 127 3407 3616 3918 105 -93 -99 N ATOM 1005 CA VAL A 127 19.214 53.936 36.959 1.00 28.43 C ANISOU 1005 CA VAL A 127 3356 3575 3871 104 -47 -3 C ATOM 1006 C VAL A 127 18.622 53.218 38.178 1.00 28.15 C ANISOU 1006 C VAL A 127 3214 3647 3832 178 26 -41 C ATOM 1007 O VAL A 127 18.095 52.104 38.052 1.00 27.84 O ANISOU 1007 O VAL A 127 3160 3636 3781 166 155 -176 O ATOM 1008 CB VAL A 127 20.770 53.749 36.898 1.00 26.50 C ANISOU 1008 CB VAL A 127 3131 3365 3573 63 -110 30 C ATOM 1009 CG1 VAL A 127 21.177 52.265 37.169 1.00 25.18 C ANISOU 1009 CG1 VAL A 127 3004 3267 3296 -35 139 -95 C ATOM 1010 CG2 VAL A 127 21.308 54.197 35.586 1.00 24.52 C ANISOU 1010 CG2 VAL A 127 2816 3090 3409 28 -240 -149 C ATOM 1011 N ILE A 128 18.682 53.851 39.348 1.00 29.46 N ANISOU 1011 N ILE A 128 3392 3828 3973 75 -46 -62 N ATOM 1012 CA ILE A 128 18.114 53.265 40.565 1.00 30.69 C ANISOU 1012 CA ILE A 128 3755 3886 4017 76 -26 5 C ATOM 1013 C ILE A 128 16.600 52.936 40.410 1.00 30.92 C ANISOU 1013 C ILE A 128 3634 3934 4180 145 60 74 C ATOM 1014 O ILE A 128 16.145 51.838 40.758 1.00 31.21 O ANISOU 1014 O ILE A 128 3397 3933 4526 332 91 -94 O ATOM 1015 CB ILE A 128 18.407 54.163 41.816 1.00 31.14 C ANISOU 1015 CB ILE A 128 3855 3975 4001 71 -79 27 C ATOM 1016 CG1 ILE A 128 19.891 54.056 42.204 1.00 32.78 C ANISOU 1016 CG1 ILE A 128 4092 4041 4322 90 66 -114 C ATOM 1017 CG2 ILE A 128 17.514 53.781 43.003 1.00 31.53 C ANISOU 1017 CG2 ILE A 128 3800 4138 4042 -1 15 8 C ATOM 1018 CD1 ILE A 128 20.522 55.322 42.653 1.00 31.10 C ANISOU 1018 CD1 ILE A 128 3823 4077 3917 77 -82 19 C ATOM 1019 N ASN A 129 15.841 53.868 39.845 1.00 32.57 N ANISOU 1019 N ASN A 129 3869 4114 4391 91 -43 69 N ATOM 1020 CA ASN A 129 14.405 53.676 39.642 1.00 32.50 C ANISOU 1020 CA ASN A 129 3893 4151 4305 89 28 27 C ATOM 1021 C ASN A 129 14.099 52.618 38.588 1.00 33.00 C ANISOU 1021 C ASN A 129 3913 4186 4437 89 83 -10 C ATOM 1022 O ASN A 129 13.153 51.846 38.732 1.00 34.71 O ANISOU 1022 O ASN A 129 3780 4559 4846 289 237 31 O ATOM 1023 CB ASN A 129 13.740 55.013 39.261 1.00 33.28 C ANISOU 1023 CB ASN A 129 4052 4160 4430 91 -85 115 C ATOM 1024 CG ASN A 129 13.753 56.026 40.403 1.00 36.33 C ANISOU 1024 CG ASN A 129 4518 4639 4644 162 33 -13 C ATOM 1025 OD1 ASN A 129 13.801 55.660 41.589 1.00 41.38 O ANISOU 1025 OD1 ASN A 129 5079 5625 5019 213 131 57 O ATOM 1026 ND2 ASN A 129 13.719 57.306 40.054 1.00 36.67 N ANISOU 1026 ND2 ASN A 129 4777 4577 4579 11 1 -137 N ATOM 1027 N MET A 130 14.907 52.550 37.530 1.00 32.84 N ANISOU 1027 N MET A 130 3971 4226 4279 -13 -21 -6 N ATOM 1028 CA MET A 130 14.760 51.465 36.561 1.00 31.93 C ANISOU 1028 CA MET A 130 3853 4116 4160 30 32 -24 C ATOM 1029 C MET A 130 15.065 50.079 37.168 1.00 31.45 C ANISOU 1029 C MET A 130 3702 4082 4165 24 39 -130 C ATOM 1030 O MET A 130 14.358 49.101 36.890 1.00 29.24 O ANISOU 1030 O MET A 130 3177 3789 4144 128 95 -317 O ATOM 1031 CB MET A 130 15.596 51.730 35.315 1.00 32.23 C ANISOU 1031 CB MET A 130 3839 4136 4269 64 -7 -33 C ATOM 1032 CG MET A 130 15.405 50.662 34.226 1.00 31.85 C ANISOU 1032 CG MET A 130 3719 4209 4173 -15 -123 -70 C ATOM 1033 SD MET A 130 13.666 50.387 33.790 1.00 35.23 S ANISOU 1033 SD MET A 130 3413 4940 5030 -27 -122 -172 S ATOM 1034 CE MET A 130 13.446 51.734 32.642 1.00 37.28 C ANISOU 1034 CE MET A 130 4464 4847 4854 -32 -30 -89 C ATOM 1035 N ILE A 131 16.079 49.981 38.025 1.00 30.98 N ANISOU 1035 N ILE A 131 3754 4000 4017 -25 2 -56 N ATOM 1036 CA ILE A 131 16.328 48.720 38.717 1.00 31.86 C ANISOU 1036 CA ILE A 131 3892 4070 4143 -32 38 -36 C ATOM 1037 C ILE A 131 15.066 48.296 39.487 1.00 33.56 C ANISOU 1037 C ILE A 131 4022 4286 4440 -129 102 -77 C ATOM 1038 O ILE A 131 14.627 47.148 39.379 1.00 33.47 O ANISOU 1038 O ILE A 131 3905 4261 4551 -200 24 15 O ATOM 1039 CB ILE A 131 17.530 48.795 39.694 1.00 30.98 C ANISOU 1039 CB ILE A 131 3808 3945 4016 20 89 -22 C ATOM 1040 CG1 ILE A 131 18.837 48.996 38.921 1.00 28.79 C ANISOU 1040 CG1 ILE A 131 3456 3578 3904 88 43 100 C ATOM 1041 CG2 ILE A 131 17.629 47.516 40.503 1.00 30.16 C ANISOU 1041 CG2 ILE A 131 3714 3957 3789 -25 84 -12 C ATOM 1042 CD1 ILE A 131 19.981 49.516 39.757 1.00 29.44 C ANISOU 1042 CD1 ILE A 131 3658 3684 3841 89 73 -39 C ATOM 1043 N GLN A 132 14.514 49.230 40.262 1.00 34.59 N ANISOU 1043 N GLN A 132 4077 4360 4702 -67 95 -52 N ATOM 1044 CA GLN A 132 13.345 48.973 41.122 1.00 35.28 C ANISOU 1044 CA GLN A 132 4364 4531 4507 17 150 -14 C ATOM 1045 C GLN A 132 12.088 48.620 40.322 1.00 34.85 C ANISOU 1045 C GLN A 132 4153 4534 4552 101 154 7 C ATOM 1046 O GLN A 132 11.328 47.723 40.708 1.00 35.53 O ANISOU 1046 O GLN A 132 4180 4685 4633 192 112 54 O ATOM 1047 CB GLN A 132 13.117 50.170 42.043 1.00 35.75 C ANISOU 1047 CB GLN A 132 4477 4525 4580 2 132 14 C ATOM 1048 CG GLN A 132 14.156 50.233 43.160 1.00 39.21 C ANISOU 1048 CG GLN A 132 4899 4946 5051 -29 -71 -42 C ATOM 1049 CD GLN A 132 14.165 51.551 43.910 1.00 40.26 C ANISOU 1049 CD GLN A 132 5233 5092 4970 -52 116 -122 C ATOM 1050 OE1 GLN A 132 13.180 52.291 43.901 1.00 48.73 O ANISOU 1050 OE1 GLN A 132 6007 6234 6271 320 -17 -117 O ATOM 1051 NE2 GLN A 132 15.288 51.858 44.563 1.00 49.39 N ANISOU 1051 NE2 GLN A 132 5963 6652 6151 -19 -196 -74 N ATOM 1052 N HIS A 133 11.907 49.287 39.185 1.00 35.53 N ANISOU 1052 N HIS A 133 4191 4640 4669 96 130 -17 N ATOM 1053 CA HIS A 133 10.829 48.982 38.231 1.00 35.71 C ANISOU 1053 CA HIS A 133 4294 4617 4657 45 110 -79 C ATOM 1054 C HIS A 133 10.960 47.588 37.628 1.00 36.78 C ANISOU 1054 C HIS A 133 4306 4671 4995 34 77 -9 C ATOM 1055 O HIS A 133 9.975 46.832 37.560 1.00 36.71 O ANISOU 1055 O HIS A 133 3937 4857 5152 94 113 40 O ATOM 1056 CB HIS A 133 10.823 50.035 37.123 1.00 34.82 C ANISOU 1056 CB HIS A 133 4247 4470 4513 19 89 -64 C ATOM 1057 CG HIS A 133 9.759 49.854 36.086 1.00 36.51 C ANISOU 1057 CG HIS A 133 4375 4777 4720 29 97 -101 C ATOM 1058 ND1 HIS A 133 8.412 49.822 36.391 1.00 37.34 N ANISOU 1058 ND1 HIS A 133 4424 4899 4864 20 91 -108 N ATOM 1059 CD2 HIS A 133 9.839 49.767 34.736 1.00 36.51 C ANISOU 1059 CD2 HIS A 133 4466 4747 4659 31 64 42 C ATOM 1060 CE1 HIS A 133 7.714 49.689 35.276 1.00 38.12 C ANISOU 1060 CE1 HIS A 133 4602 4951 4928 58 8 -63 C ATOM 1061 NE2 HIS A 133 8.555 49.658 34.256 1.00 39.25 N ANISOU 1061 NE2 HIS A 133 4739 5083 5089 -88 94 -61 N ATOM 1062 N ILE A 134 12.172 47.245 37.173 1.00 35.87 N ANISOU 1062 N ILE A 134 4142 4643 4843 7 54 -74 N ATOM 1063 CA ILE A 134 12.427 45.922 36.618 1.00 36.44 C ANISOU 1063 CA ILE A 134 4286 4688 4872 56 78 -74 C ATOM 1064 C ILE A 134 12.160 44.822 37.635 1.00 35.60 C ANISOU 1064 C ILE A 134 4095 4647 4784 94 176 -87 C ATOM 1065 O ILE A 134 11.545 43.821 37.291 1.00 36.45 O ANISOU 1065 O ILE A 134 3998 4901 4947 92 204 -151 O ATOM 1066 CB ILE A 134 13.876 45.777 36.060 1.00 35.23 C ANISOU 1066 CB ILE A 134 4153 4544 4688 -4 134 -39 C ATOM 1067 CG1 ILE A 134 14.022 46.572 34.754 1.00 35.53 C ANISOU 1067 CG1 ILE A 134 4352 4482 4666 108 60 -32 C ATOM 1068 CG2 ILE A 134 14.201 44.308 35.802 1.00 35.48 C ANISOU 1068 CG2 ILE A 134 4048 4624 4807 48 -21 2 C ATOM 1069 CD1 ILE A 134 15.447 46.676 34.264 1.00 36.52 C ANISOU 1069 CD1 ILE A 134 4424 4654 4795 -31 40 15 C ATOM 1070 N LYS A 135 12.635 44.999 38.868 1.00 36.70 N ANISOU 1070 N LYS A 135 4245 4780 4917 75 150 -119 N ATOM 1071 CA LYS A 135 12.507 43.991 39.901 1.00 39.00 C ANISOU 1071 CA LYS A 135 4775 4940 5104 37 72 -4 C ATOM 1072 C LYS A 135 11.057 43.802 40.358 1.00 41.26 C ANISOU 1072 C LYS A 135 4993 5223 5458 30 100 31 C ATOM 1073 O LYS A 135 10.703 42.752 40.925 1.00 42.22 O ANISOU 1073 O LYS A 135 5081 5419 5540 74 229 53 O ATOM 1074 CB LYS A 135 13.379 44.346 41.109 1.00 39.25 C ANISOU 1074 CB LYS A 135 4826 4955 5129 25 69 -37 C ATOM 1075 CG LYS A 135 14.864 44.032 40.917 1.00 39.24 C ANISOU 1075 CG LYS A 135 4789 5015 5106 -24 117 -37 C ATOM 1076 CD LYS A 135 15.159 42.537 41.125 1.00 41.44 C ANISOU 1076 CD LYS A 135 5065 5251 5429 -85 130 138 C ATOM 1077 CE LYS A 135 16.468 42.060 40.467 1.00 40.73 C ANISOU 1077 CE LYS A 135 5072 5089 5311 89 110 0 C ATOM 1078 NZ LYS A 135 16.502 40.583 40.216 1.00 39.73 N ANISOU 1078 NZ LYS A 135 4639 4957 5498 -90 33 71 N ATOM 1079 N LYS A 136 10.226 44.815 40.123 1.00 42.05 N ANISOU 1079 N LYS A 136 5119 5300 5557 28 67 24 N ATOM 1080 CA LYS A 136 8.793 44.717 40.424 1.00 42.50 C ANISOU 1080 CA LYS A 136 5203 5409 5536 15 55 16 C ATOM 1081 C LYS A 136 8.040 43.920 39.352 1.00 42.65 C ANISOU 1081 C LYS A 136 5263 5422 5519 15 37 32 C ATOM 1082 O LYS A 136 7.244 43.039 39.675 1.00 43.48 O ANISOU 1082 O LYS A 136 5371 5527 5623 -46 38 60 O ATOM 1083 CB LYS A 136 8.181 46.109 40.611 1.00 43.37 C ANISOU 1083 CB LYS A 136 5346 5507 5625 19 82 4 C ATOM 1084 CG LYS A 136 8.495 46.718 41.986 1.00 45.54 C ANISOU 1084 CG LYS A 136 5673 5810 5817 -2 48 -54 C ATOM 1085 CD LYS A 136 7.598 47.918 42.344 1.00 45.70 C ANISOU 1085 CD LYS A 136 5726 5731 5908 66 60 -37 C ATOM 1086 CE LYS A 136 7.892 49.170 41.500 1.00 49.79 C ANISOU 1086 CE LYS A 136 6335 6183 6399 -51 31 60 C ATOM 1087 NZ LYS A 136 9.044 49.992 41.985 1.00 49.79 N ANISOU 1087 NZ LYS A 136 6192 6377 6347 -11 -60 -57 N ATOM 1088 N HIS A 137 8.310 44.208 38.086 1.00 41.82 N ANISOU 1088 N HIS A 137 5155 5307 5425 17 108 8 N ATOM 1089 CA HIS A 137 7.556 43.623 36.980 1.00 41.48 C ANISOU 1089 CA HIS A 137 5064 5264 5430 17 44 -25 C ATOM 1090 C HIS A 137 8.147 42.336 36.392 1.00 41.42 C ANISOU 1090 C HIS A 137 5035 5284 5419 -29 20 -94 C ATOM 1091 O HIS A 137 7.416 41.551 35.778 1.00 41.24 O ANISOU 1091 O HIS A 137 4863 5303 5503 32 44 -160 O ATOM 1092 CB HIS A 137 7.366 44.663 35.884 1.00 43.18 C ANISOU 1092 CB HIS A 137 5288 5513 5605 -52 30 35 C ATOM 1093 CG HIS A 137 6.460 45.780 36.292 1.00 47.40 C ANISOU 1093 CG HIS A 137 5914 5878 6217 149 47 -73 C ATOM 1094 ND1 HIS A 137 6.747 46.616 37.352 1.00 48.08 N ANISOU 1094 ND1 HIS A 137 6128 5946 6195 59 -18 -32 N ATOM 1095 CD2 HIS A 137 5.254 46.174 35.814 1.00 48.62 C ANISOU 1095 CD2 HIS A 137 6084 6267 6121 105 -112 -66 C ATOM 1096 CE1 HIS A 137 5.764 47.488 37.496 1.00 48.78 C ANISOU 1096 CE1 HIS A 137 6134 6056 6344 37 37 -148 C ATOM 1097 NE2 HIS A 137 4.850 47.247 36.572 1.00 47.97 N ANISOU 1097 NE2 HIS A 137 5909 6051 6264 200 -45 -20 N ATOM 1098 N LEU A 138 9.453 42.124 36.574 1.00 40.00 N ANISOU 1098 N LEU A 138 4934 5046 5217 -21 -19 -82 N ATOM 1099 CA LEU A 138 10.147 40.950 36.045 1.00 38.90 C ANISOU 1099 CA LEU A 138 4845 4971 4961 -40 7 0 C ATOM 1100 C LEU A 138 11.090 40.411 37.120 1.00 38.38 C ANISOU 1100 C LEU A 138 4787 4955 4839 -46 67 27 C ATOM 1101 O LEU A 138 12.318 40.405 36.953 1.00 37.30 O ANISOU 1101 O LEU A 138 4648 4873 4648 -44 89 68 O ATOM 1102 CB LEU A 138 10.898 41.308 34.748 1.00 37.56 C ANISOU 1102 CB LEU A 138 4718 4758 4793 -84 44 -61 C ATOM 1103 CG LEU A 138 10.063 41.905 33.603 1.00 37.16 C ANISOU 1103 CG LEU A 138 4587 4566 4965 -72 34 -12 C ATOM 1104 CD1 LEU A 138 10.928 42.527 32.546 1.00 35.93 C ANISOU 1104 CD1 LEU A 138 4286 4672 4694 78 -87 -13 C ATOM 1105 CD2 LEU A 138 9.163 40.883 32.910 1.00 37.50 C ANISOU 1105 CD2 LEU A 138 4590 4608 5050 -61 38 -107 C ATOM 1106 N PRO A 139 10.517 39.935 38.243 1.00 38.78 N ANISOU 1106 N PRO A 139 4789 5050 4896 -20 62 54 N ATOM 1107 CA PRO A 139 11.364 39.547 39.366 1.00 37.82 C ANISOU 1107 CA PRO A 139 4674 4902 4794 -22 62 46 C ATOM 1108 C PRO A 139 12.422 38.467 39.070 1.00 37.08 C ANISOU 1108 C PRO A 139 4573 4826 4689 -70 109 49 C ATOM 1109 O PRO A 139 13.434 38.396 39.776 1.00 39.99 O ANISOU 1109 O PRO A 139 4648 5284 5260 -24 229 47 O ATOM 1110 CB PRO A 139 10.353 39.017 40.398 1.00 38.87 C ANISOU 1110 CB PRO A 139 4827 4993 4947 -15 126 40 C ATOM 1111 CG PRO A 139 9.048 39.625 40.005 1.00 38.97 C ANISOU 1111 CG PRO A 139 4852 5121 4833 -56 96 109 C ATOM 1112 CD PRO A 139 9.084 39.698 38.529 1.00 38.58 C ANISOU 1112 CD PRO A 139 4806 5112 4739 -17 45 69 C ATOM 1113 N GLU A 140 12.192 37.617 38.086 1.00 35.55 N ANISOU 1113 N GLU A 140 4246 4649 4610 -120 147 135 N ATOM 1114 CA GLU A 140 13.130 36.543 37.782 1.00 35.40 C ANISOU 1114 CA GLU A 140 4301 4564 4585 -79 97 98 C ATOM 1115 C GLU A 140 14.277 36.978 36.871 1.00 34.35 C ANISOU 1115 C GLU A 140 4148 4375 4526 -76 94 130 C ATOM 1116 O GLU A 140 15.190 36.175 36.625 1.00 33.75 O ANISOU 1116 O GLU A 140 3951 4370 4499 -75 177 344 O ATOM 1117 CB GLU A 140 12.417 35.368 37.111 1.00 37.14 C ANISOU 1117 CB GLU A 140 4436 4786 4888 -15 35 0 C ATOM 1118 CG GLU A 140 11.289 34.792 37.925 1.00 41.93 C ANISOU 1118 CG GLU A 140 5171 5254 5504 -182 228 131 C ATOM 1119 CD GLU A 140 11.783 34.251 39.225 1.00 48.35 C ANISOU 1119 CD GLU A 140 6084 6330 5954 -137 -19 180 C ATOM 1120 OE1 GLU A 140 12.341 33.127 39.223 1.00 54.44 O ANISOU 1120 OE1 GLU A 140 6706 6889 7089 145 161 34 O ATOM 1121 OE2 GLU A 140 11.622 34.952 40.245 1.00 52.88 O ANISOU 1121 OE2 GLU A 140 6797 6485 6808 -120 56 -179 O ATOM 1122 N SER A 141 14.224 38.204 36.338 1.00 32.68 N ANISOU 1122 N SER A 141 3848 4187 4381 -46 57 7 N ATOM 1123 CA SER A 141 15.299 38.689 35.449 1.00 30.60 C ANISOU 1123 CA SER A 141 3708 3939 3979 -50 -28 -22 C ATOM 1124 C SER A 141 16.567 39.057 36.231 1.00 28.97 C ANISOU 1124 C SER A 141 3467 3705 3831 -67 40 -38 C ATOM 1125 O SER A 141 16.493 39.739 37.264 1.00 28.95 O ANISOU 1125 O SER A 141 3424 3677 3898 -76 105 -29 O ATOM 1126 CB SER A 141 14.842 39.893 34.630 1.00 30.58 C ANISOU 1126 CB SER A 141 3697 3890 4032 23 -38 -107 C ATOM 1127 OG SER A 141 14.048 39.513 33.526 1.00 29.54 O ANISOU 1127 OG SER A 141 3676 3744 3805 152 -81 -211 O ATOM 1128 N PHE A 142 17.726 38.607 35.736 1.00 26.39 N ANISOU 1128 N PHE A 142 3193 3280 3553 -71 -44 -80 N ATOM 1129 CA PHE A 142 19.028 38.941 36.365 1.00 26.12 C ANISOU 1129 CA PHE A 142 3228 3252 3445 -16 -21 -5 C ATOM 1130 C PHE A 142 19.457 40.322 35.824 1.00 24.35 C ANISOU 1130 C PHE A 142 2848 3151 3250 -107 64 40 C ATOM 1131 O PHE A 142 19.665 40.487 34.611 1.00 25.61 O ANISOU 1131 O PHE A 142 3112 3259 3360 -30 -201 136 O ATOM 1132 CB PHE A 142 20.072 37.861 36.077 1.00 23.22 C ANISOU 1132 CB PHE A 142 2820 3043 2960 -75 5 3 C ATOM 1133 CG PHE A 142 21.380 38.054 36.803 1.00 25.33 C ANISOU 1133 CG PHE A 142 3125 3098 3400 -70 -7 29 C ATOM 1134 CD1 PHE A 142 21.694 37.284 37.928 1.00 24.63 C ANISOU 1134 CD1 PHE A 142 2853 3200 3304 -96 -256 -16 C ATOM 1135 CD2 PHE A 142 22.309 38.982 36.338 1.00 24.71 C ANISOU 1135 CD2 PHE A 142 2928 3056 3402 24 -60 159 C ATOM 1136 CE1 PHE A 142 22.907 37.447 38.592 1.00 24.18 C ANISOU 1136 CE1 PHE A 142 2762 2879 3544 23 -37 118 C ATOM 1137 CE2 PHE A 142 23.531 39.148 36.979 1.00 23.36 C ANISOU 1137 CE2 PHE A 142 2940 2899 3033 -317 -109 40 C ATOM 1138 CZ PHE A 142 23.838 38.397 38.107 1.00 23.30 C ANISOU 1138 CZ PHE A 142 2575 2923 3354 57 128 222 C ATOM 1139 N VAL A 143 19.540 41.300 36.723 1.00 24.02 N ANISOU 1139 N VAL A 143 2744 3303 3076 -204 -124 70 N ATOM 1140 CA VAL A 143 19.748 42.709 36.363 1.00 23.12 C ANISOU 1140 CA VAL A 143 2660 3076 3046 -92 -182 14 C ATOM 1141 C VAL A 143 21.211 43.178 36.590 1.00 22.87 C ANISOU 1141 C VAL A 143 2637 3072 2978 -160 -68 26 C ATOM 1142 O VAL A 143 21.718 43.178 37.702 1.00 23.58 O ANISOU 1142 O VAL A 143 2273 3226 3459 -174 -391 -136 O ATOM 1143 CB VAL A 143 18.780 43.643 37.119 1.00 23.69 C ANISOU 1143 CB VAL A 143 2828 3200 2972 -217 -157 44 C ATOM 1144 CG1 VAL A 143 19.089 45.108 36.842 1.00 24.38 C ANISOU 1144 CG1 VAL A 143 2885 3067 3309 -112 -31 -84 C ATOM 1145 CG2 VAL A 143 17.309 43.346 36.749 1.00 24.57 C ANISOU 1145 CG2 VAL A 143 2880 3304 3152 21 17 -57 C ATOM 1146 N ILE A 144 21.828 43.629 35.518 1.00 23.41 N ANISOU 1146 N ILE A 144 2683 2917 3294 -100 4 -83 N ATOM 1147 CA ILE A 144 23.219 44.131 35.518 1.00 22.43 C ANISOU 1147 CA ILE A 144 2662 2827 3032 -70 -101 -73 C ATOM 1148 C ILE A 144 23.055 45.629 35.344 1.00 21.81 C ANISOU 1148 C ILE A 144 2738 2657 2891 -46 -160 -115 C ATOM 1149 O ILE A 144 22.364 46.070 34.439 1.00 23.05 O ANISOU 1149 O ILE A 144 3249 2931 2576 -78 -105 -29 O ATOM 1150 CB ILE A 144 23.994 43.556 34.306 1.00 22.56 C ANISOU 1150 CB ILE A 144 2756 2860 2954 47 -82 14 C ATOM 1151 CG1 ILE A 144 24.119 42.025 34.425 1.00 23.72 C ANISOU 1151 CG1 ILE A 144 2825 2966 3219 46 89 -115 C ATOM 1152 CG2 ILE A 144 25.358 44.233 34.136 1.00 21.45 C ANISOU 1152 CG2 ILE A 144 2602 2624 2922 16 -33 130 C ATOM 1153 CD1 ILE A 144 24.285 41.345 33.081 1.00 22.75 C ANISOU 1153 CD1 ILE A 144 2612 2814 3217 -79 -151 -153 C ATOM 1154 N ALA A 145 23.606 46.425 36.242 1.00 21.30 N ANISOU 1154 N ALA A 145 2563 2781 2747 23 -39 -142 N ATOM 1155 CA ALA A 145 23.414 47.877 36.153 1.00 20.26 C ANISOU 1155 CA ALA A 145 2542 2595 2561 -27 -74 -63 C ATOM 1156 C ALA A 145 24.756 48.602 36.033 1.00 20.69 C ANISOU 1156 C ALA A 145 2594 2628 2640 19 13 62 C ATOM 1157 O ALA A 145 25.719 48.290 36.747 1.00 20.85 O ANISOU 1157 O ALA A 145 2445 2556 2919 54 -70 -73 O ATOM 1158 CB ALA A 145 22.661 48.374 37.425 1.00 21.23 C ANISOU 1158 CB ALA A 145 2617 2673 2773 133 92 35 C ATOM 1159 N GLY A 146 24.776 49.647 35.216 1.00 20.74 N ANISOU 1159 N GLY A 146 2607 2829 2442 2 -11 -86 N ATOM 1160 CA GLY A 146 25.960 50.451 35.051 1.00 19.53 C ANISOU 1160 CA GLY A 146 2539 2474 2407 13 -2 -100 C ATOM 1161 C GLY A 146 25.760 51.564 34.058 1.00 20.15 C ANISOU 1161 C GLY A 146 2638 2648 2370 45 -34 -33 C ATOM 1162 O GLY A 146 24.619 51.802 33.595 1.00 20.64 O ANISOU 1162 O GLY A 146 2701 2701 2439 242 -157 149 O ATOM 1163 N ASN A 147 26.831 52.277 33.727 1.00 18.97 N ANISOU 1163 N ASN A 147 2478 2379 2351 24 11 56 N ATOM 1164 CA ASN A 147 28.192 52.005 34.155 1.00 19.59 C ANISOU 1164 CA ASN A 147 2627 2349 2466 25 5 0 C ATOM 1165 C ASN A 147 28.559 52.887 35.348 1.00 20.32 C ANISOU 1165 C ASN A 147 2711 2395 2612 104 79 -4 C ATOM 1166 O ASN A 147 28.102 54.034 35.447 1.00 20.03 O ANISOU 1166 O ASN A 147 2948 2232 2429 188 321 -58 O ATOM 1167 CB ASN A 147 29.186 52.227 32.985 1.00 19.00 C ANISOU 1167 CB ASN A 147 2570 2315 2334 -173 -29 64 C ATOM 1168 CG ASN A 147 29.389 50.983 32.097 1.00 22.43 C ANISOU 1168 CG ASN A 147 2793 2754 2973 66 15 47 C ATOM 1169 OD1 ASN A 147 28.466 50.209 31.868 1.00 24.06 O ANISOU 1169 OD1 ASN A 147 3035 2809 3298 31 22 -67 O ATOM 1170 ND2 ASN A 147 30.620 50.817 31.563 1.00 21.17 N ANISOU 1170 ND2 ASN A 147 2961 2645 2436 23 -58 12 N ATOM 1171 N VAL A 148 29.394 52.350 36.234 1.00 19.35 N ANISOU 1171 N VAL A 148 2641 2249 2462 -18 206 27 N ATOM 1172 CA VAL A 148 29.859 53.037 37.397 1.00 19.48 C ANISOU 1172 CA VAL A 148 2525 2419 2454 0 75 11 C ATOM 1173 C VAL A 148 31.382 53.025 37.507 1.00 19.06 C ANISOU 1173 C VAL A 148 2486 2464 2291 80 130 -62 C ATOM 1174 O VAL A 148 32.059 52.247 36.852 1.00 16.57 O ANISOU 1174 O VAL A 148 2378 2447 1468 93 138 -161 O ATOM 1175 CB VAL A 148 29.225 52.450 38.665 1.00 20.55 C ANISOU 1175 CB VAL A 148 2745 2649 2411 76 121 -53 C ATOM 1176 CG1 VAL A 148 27.714 52.530 38.559 1.00 22.16 C ANISOU 1176 CG1 VAL A 148 2763 2940 2715 -172 -54 -186 C ATOM 1177 CG2 VAL A 148 29.671 51.005 38.935 1.00 20.07 C ANISOU 1177 CG2 VAL A 148 2875 2569 2179 -26 185 -100 C ATOM 1178 N GLY A 149 31.909 53.871 38.384 1.00 19.64 N ANISOU 1178 N GLY A 149 2379 2543 2537 37 247 -135 N ATOM 1179 CA GLY A 149 33.339 53.977 38.558 1.00 20.51 C ANISOU 1179 CA GLY A 149 2576 2568 2646 -44 -5 -112 C ATOM 1180 C GLY A 149 33.834 54.137 39.957 1.00 20.15 C ANISOU 1180 C GLY A 149 2538 2395 2720 14 7 -93 C ATOM 1181 O GLY A 149 35.017 54.329 40.134 1.00 22.78 O ANISOU 1181 O GLY A 149 2691 2865 3096 -187 -157 -188 O ATOM 1182 N THR A 150 32.943 54.017 40.940 1.00 20.48 N ANISOU 1182 N THR A 150 2656 2322 2804 -41 11 -85 N ATOM 1183 CA THR A 150 33.286 54.172 42.319 1.00 20.09 C ANISOU 1183 CA THR A 150 2595 2432 2605 -56 -64 -49 C ATOM 1184 C THR A 150 32.617 53.102 43.186 1.00 20.76 C ANISOU 1184 C THR A 150 2670 2646 2569 -99 -27 1 C ATOM 1185 O THR A 150 31.565 52.555 42.829 1.00 19.31 O ANISOU 1185 O THR A 150 2652 2624 2061 -168 40 -36 O ATOM 1186 CB THR A 150 32.867 55.560 42.920 1.00 19.50 C ANISOU 1186 CB THR A 150 2379 2235 2793 -18 8 -75 C ATOM 1187 OG1 THR A 150 31.453 55.651 43.024 1.00 19.86 O ANISOU 1187 OG1 THR A 150 2219 2297 3027 123 305 -65 O ATOM 1188 CG2 THR A 150 33.391 56.733 42.098 1.00 16.68 C ANISOU 1188 CG2 THR A 150 2451 2074 1811 15 16 -336 C ATOM 1189 N PRO A 151 33.252 52.784 44.327 1.00 21.23 N ANISOU 1189 N PRO A 151 2811 2758 2495 -98 -92 -67 N ATOM 1190 CA PRO A 151 32.645 51.896 45.330 1.00 23.04 C ANISOU 1190 CA PRO A 151 2946 2994 2813 -105 -21 25 C ATOM 1191 C PRO A 151 31.314 52.368 45.945 1.00 23.73 C ANISOU 1191 C PRO A 151 2897 3003 3113 -1 25 -33 C ATOM 1192 O PRO A 151 30.448 51.526 46.253 1.00 24.77 O ANISOU 1192 O PRO A 151 2953 3308 3149 24 181 -181 O ATOM 1193 CB PRO A 151 33.713 51.820 46.445 1.00 23.02 C ANISOU 1193 CB PRO A 151 2952 2996 2799 -48 -91 -33 C ATOM 1194 CG PRO A 151 34.680 52.877 46.161 1.00 19.67 C ANISOU 1194 CG PRO A 151 2639 2731 2103 -122 46 -66 C ATOM 1195 CD PRO A 151 34.640 53.147 44.671 1.00 21.06 C ANISOU 1195 CD PRO A 151 2962 2764 2273 -181 -122 -161 C ATOM 1196 N GLU A 152 31.162 53.673 46.168 1.00 24.22 N ANISOU 1196 N GLU A 152 2930 3202 3068 -91 -98 -139 N ATOM 1197 CA GLU A 152 29.880 54.213 46.628 1.00 24.00 C ANISOU 1197 CA GLU A 152 2972 3082 3062 -40 -64 -49 C ATOM 1198 C GLU A 152 28.789 53.935 45.575 1.00 23.16 C ANISOU 1198 C GLU A 152 2977 2918 2901 -1 -80 -18 C ATOM 1199 O GLU A 152 27.664 53.610 45.926 1.00 23.34 O ANISOU 1199 O GLU A 152 2843 3043 2983 84 -5 -49 O ATOM 1200 CB GLU A 152 29.936 55.709 46.951 1.00 25.19 C ANISOU 1200 CB GLU A 152 3072 3382 3114 9 -46 -164 C ATOM 1201 CG GLU A 152 30.601 56.571 45.948 1.00 30.43 C ANISOU 1201 CG GLU A 152 4076 3751 3735 -4 96 -34 C ATOM 1202 CD GLU A 152 32.117 56.830 46.206 1.00 34.98 C ANISOU 1202 CD GLU A 152 4329 4558 4402 120 -181 -146 C ATOM 1203 OE1 GLU A 152 32.944 55.871 46.338 1.00 27.64 O ANISOU 1203 OE1 GLU A 152 3984 3561 2954 -16 -310 -241 O ATOM 1204 OE2 GLU A 152 32.481 58.033 46.224 1.00 42.72 O ANISOU 1204 OE2 GLU A 152 6004 4963 5265 -160 -57 32 O ATOM 1205 N ALA A 153 29.120 54.044 44.294 1.00 23.37 N ANISOU 1205 N ALA A 153 2958 2836 3085 -5 45 -4 N ATOM 1206 CA ALA A 153 28.133 53.760 43.241 1.00 22.57 C ANISOU 1206 CA ALA A 153 2812 2876 2887 -10 -14 29 C ATOM 1207 C ALA A 153 27.756 52.289 43.191 1.00 21.86 C ANISOU 1207 C ALA A 153 2732 2728 2846 -18 70 121 C ATOM 1208 O ALA A 153 26.573 51.948 43.022 1.00 22.09 O ANISOU 1208 O ALA A 153 2729 2800 2863 41 91 -76 O ATOM 1209 CB ALA A 153 28.646 54.187 41.855 1.00 21.46 C ANISOU 1209 CB ALA A 153 2565 2511 3074 -60 75 155 C ATOM 1210 N VAL A 154 28.755 51.411 43.268 1.00 21.96 N ANISOU 1210 N VAL A 154 2639 2843 2858 -72 163 126 N ATOM 1211 CA VAL A 154 28.487 49.961 43.249 1.00 22.82 C ANISOU 1211 CA VAL A 154 2874 2963 2831 0 92 55 C ATOM 1212 C VAL A 154 27.506 49.641 44.396 1.00 23.77 C ANISOU 1212 C VAL A 154 2914 3157 2958 -58 185 41 C ATOM 1213 O VAL A 154 26.479 48.975 44.194 1.00 23.49 O ANISOU 1213 O VAL A 154 2898 3147 2878 -137 492 21 O ATOM 1214 CB VAL A 154 29.792 49.122 43.367 1.00 20.62 C ANISOU 1214 CB VAL A 154 2810 2685 2338 55 176 116 C ATOM 1215 CG1 VAL A 154 29.468 47.641 43.610 1.00 21.77 C ANISOU 1215 CG1 VAL A 154 2970 2738 2564 -151 72 -246 C ATOM 1216 CG2 VAL A 154 30.670 49.284 42.100 1.00 21.55 C ANISOU 1216 CG2 VAL A 154 2329 3043 2814 113 40 210 C ATOM 1217 N ARG A 155 27.832 50.159 45.576 1.00 24.87 N ANISOU 1217 N ARG A 155 3088 3311 3047 -34 169 36 N ATOM 1218 CA ARG A 155 27.029 49.962 46.800 1.00 26.24 C ANISOU 1218 CA ARG A 155 3307 3404 3258 -13 184 12 C ATOM 1219 C ARG A 155 25.591 50.411 46.634 1.00 25.56 C ANISOU 1219 C ARG A 155 3180 3383 3147 -26 60 54 C ATOM 1220 O ARG A 155 24.659 49.675 46.968 1.00 25.33 O ANISOU 1220 O ARG A 155 3250 3207 3167 -82 1 30 O ATOM 1221 CB ARG A 155 27.613 50.785 47.935 1.00 28.36 C ANISOU 1221 CB ARG A 155 3578 3712 3485 -72 174 -75 C ATOM 1222 CG ARG A 155 28.768 50.202 48.625 1.00 35.72 C ANISOU 1222 CG ARG A 155 4504 4296 4770 117 -71 142 C ATOM 1223 CD ARG A 155 28.386 49.743 50.026 1.00 46.28 C ANISOU 1223 CD ARG A 155 6218 6032 5332 -188 200 -14 C ATOM 1224 NE ARG A 155 29.165 48.552 50.353 1.00 50.18 N ANISOU 1224 NE ARG A 155 6469 6207 6389 183 -205 48 N ATOM 1225 CZ ARG A 155 30.213 48.502 51.168 1.00 50.49 C ANISOU 1225 CZ ARG A 155 6386 6299 6496 25 -114 11 C ATOM 1226 NH1 ARG A 155 30.645 49.576 51.834 1.00 51.69 N ANISOU 1226 NH1 ARG A 155 6696 6333 6611 28 -96 -8 N ATOM 1227 NH2 ARG A 155 30.819 47.338 51.336 1.00 50.79 N ANISOU 1227 NH2 ARG A 155 6470 6353 6473 35 -95 -17 N ATOM 1228 N GLU A 156 25.425 51.629 46.126 1.00 26.67 N ANISOU 1228 N GLU A 156 3285 3351 3497 4 114 20 N ATOM 1229 CA GLU A 156 24.093 52.223 45.936 1.00 26.48 C ANISOU 1229 CA GLU A 156 3288 3376 3396 12 121 -8 C ATOM 1230 C GLU A 156 23.284 51.408 44.934 1.00 26.21 C ANISOU 1230 C GLU A 156 3256 3355 3348 16 167 39 C ATOM 1231 O GLU A 156 22.093 51.170 45.132 1.00 26.98 O ANISOU 1231 O GLU A 156 3152 3424 3674 143 320 -97 O ATOM 1232 CB GLU A 156 24.173 53.704 45.521 1.00 26.11 C ANISOU 1232 CB GLU A 156 3288 3472 3158 31 82 89 C ATOM 1233 CG GLU A 156 22.911 54.520 45.962 1.00 27.62 C ANISOU 1233 CG GLU A 156 3548 3485 3461 73 51 69 C ATOM 1234 CD GLU A 156 22.968 56.020 45.686 1.00 28.59 C ANISOU 1234 CD GLU A 156 3633 3488 3741 91 64 -63 C ATOM 1235 OE1 GLU A 156 24.031 56.528 45.287 1.00 32.83 O ANISOU 1235 OE1 GLU A 156 4037 3826 4609 -108 306 105 O ATOM 1236 OE2 GLU A 156 21.915 56.693 45.863 1.00 30.43 O ANISOU 1236 OE2 GLU A 156 3860 3894 3805 132 354 -66 O ATOM 1237 N LEU A 157 23.932 50.924 43.877 1.00 25.47 N ANISOU 1237 N LEU A 157 3148 3258 3270 2 200 0 N ATOM 1238 CA LEU A 157 23.217 50.150 42.866 1.00 25.54 C ANISOU 1238 CA LEU A 157 3143 3281 3279 21 83 -17 C ATOM 1239 C LEU A 157 22.867 48.738 43.360 1.00 24.76 C ANISOU 1239 C LEU A 157 3090 3354 2963 -81 131 40 C ATOM 1240 O LEU A 157 21.755 48.251 43.107 1.00 23.78 O ANISOU 1240 O LEU A 157 2991 3317 2726 -80 30 -54 O ATOM 1241 CB LEU A 157 24.004 50.104 41.559 1.00 25.47 C ANISOU 1241 CB LEU A 157 3259 3398 3021 43 41 -18 C ATOM 1242 CG LEU A 157 23.717 51.151 40.473 1.00 28.32 C ANISOU 1242 CG LEU A 157 3571 3643 3545 7 142 50 C ATOM 1243 CD1 LEU A 157 23.489 52.554 40.949 1.00 32.34 C ANISOU 1243 CD1 LEU A 157 4447 3874 3965 -145 108 -23 C ATOM 1244 CD2 LEU A 157 24.760 51.073 39.400 1.00 24.61 C ANISOU 1244 CD2 LEU A 157 2898 3242 3210 -83 -91 -3 C ATOM 1245 N GLU A 158 23.811 48.089 44.045 1.00 25.74 N ANISOU 1245 N GLU A 158 3163 3327 3291 -83 147 9 N ATOM 1246 CA GLU A 158 23.566 46.792 44.671 1.00 27.46 C ANISOU 1246 CA GLU A 158 3423 3480 3528 -21 53 67 C ATOM 1247 C GLU A 158 22.402 46.906 45.669 1.00 30.06 C ANISOU 1247 C GLU A 158 3671 3818 3931 -91 76 9 C ATOM 1248 O GLU A 158 21.454 46.113 45.638 1.00 30.65 O ANISOU 1248 O GLU A 158 3732 3777 4135 -212 138 81 O ATOM 1249 CB GLU A 158 24.836 46.306 45.373 1.00 27.58 C ANISOU 1249 CB GLU A 158 3375 3420 3682 -93 108 66 C ATOM 1250 CG GLU A 158 25.929 45.806 44.382 1.00 24.78 C ANISOU 1250 CG GLU A 158 3007 2971 3435 -215 70 -5 C ATOM 1251 CD GLU A 158 27.111 45.185 45.080 1.00 25.75 C ANISOU 1251 CD GLU A 158 3321 3269 3192 -104 98 82 C ATOM 1252 OE1 GLU A 158 27.124 45.190 46.346 1.00 26.93 O ANISOU 1252 OE1 GLU A 158 3406 3622 3202 -193 -305 -90 O ATOM 1253 OE2 GLU A 158 28.011 44.644 44.382 1.00 25.66 O ANISOU 1253 OE2 GLU A 158 2945 3807 2997 275 -252 40 O ATOM 1254 N ASN A 159 22.480 47.907 46.541 1.00 31.05 N ANISOU 1254 N ASN A 159 3782 3863 4152 6 59 1 N ATOM 1255 CA ASN A 159 21.428 48.182 47.495 1.00 31.52 C ANISOU 1255 CA ASN A 159 3945 4041 3990 19 130 32 C ATOM 1256 C ASN A 159 20.049 48.471 46.811 1.00 31.54 C ANISOU 1256 C ASN A 159 3932 4096 3955 -21 144 77 C ATOM 1257 O ASN A 159 19.018 48.049 47.326 1.00 33.36 O ANISOU 1257 O ASN A 159 4060 4321 4294 -65 96 175 O ATOM 1258 CB ASN A 159 21.874 49.303 48.451 1.00 33.45 C ANISOU 1258 CB ASN A 159 4090 4336 4281 -33 135 41 C ATOM 1259 CG ASN A 159 22.999 48.863 49.428 1.00 39.60 C ANISOU 1259 CG ASN A 159 5014 5064 4966 -84 -174 -136 C ATOM 1260 OD1 ASN A 159 23.334 47.669 49.544 1.00 45.84 O ANISOU 1260 OD1 ASN A 159 6201 5400 5815 265 -123 101 O ATOM 1261 ND2 ASN A 159 23.583 49.842 50.136 1.00 36.92 N ANISOU 1261 ND2 ASN A 159 4562 4824 4639 -155 68 -130 N ATOM 1262 N ALA A 160 20.018 49.119 45.637 1.00 30.92 N ANISOU 1262 N ALA A 160 3788 4013 3947 -39 78 -31 N ATOM 1263 CA ALA A 160 18.757 49.347 44.917 1.00 30.28 C ANISOU 1263 CA ALA A 160 3765 3889 3849 46 155 16 C ATOM 1264 C ALA A 160 18.136 48.059 44.383 1.00 30.62 C ANISOU 1264 C ALA A 160 3706 3948 3977 43 125 0 C ATOM 1265 O ALA A 160 16.957 48.057 44.009 1.00 32.31 O ANISOU 1265 O ALA A 160 3774 4231 4270 154 218 14 O ATOM 1266 CB ALA A 160 18.934 50.357 43.743 1.00 29.76 C ANISOU 1266 CB ALA A 160 3708 3696 3903 86 156 63 C ATOM 1267 N GLY A 161 18.918 46.978 44.326 1.00 28.70 N ANISOU 1267 N GLY A 161 3368 3759 3775 69 223 -46 N ATOM 1268 CA GLY A 161 18.449 45.691 43.827 1.00 28.45 C ANISOU 1268 CA GLY A 161 3338 3759 3711 -7 144 -5 C ATOM 1269 C GLY A 161 19.192 45.095 42.630 1.00 28.83 C ANISOU 1269 C GLY A 161 3449 3664 3840 -19 147 -44 C ATOM 1270 O GLY A 161 18.811 44.028 42.136 1.00 29.83 O ANISOU 1270 O GLY A 161 3488 3754 4089 -197 102 -64 O ATOM 1271 N ALA A 162 20.235 45.751 42.121 1.00 27.58 N ANISOU 1271 N ALA A 162 3299 3517 3663 -16 129 -50 N ATOM 1272 CA ALA A 162 20.969 45.156 40.977 1.00 26.10 C ANISOU 1272 CA ALA A 162 3103 3327 3487 -16 130 60 C ATOM 1273 C ALA A 162 21.552 43.809 41.373 1.00 24.07 C ANISOU 1273 C ALA A 162 2715 3248 3182 -115 222 46 C ATOM 1274 O ALA A 162 22.002 43.669 42.488 1.00 22.59 O ANISOU 1274 O ALA A 162 2434 3201 2946 -80 332 434 O ATOM 1275 CB ALA A 162 22.078 46.103 40.499 1.00 27.51 C ANISOU 1275 CB ALA A 162 3250 3391 3809 -14 187 -5 C ATOM 1276 N ASP A 163 21.553 42.823 40.476 1.00 23.53 N ANISOU 1276 N ASP A 163 2738 3056 3146 -83 93 15 N ATOM 1277 CA ASP A 163 22.244 41.531 40.753 1.00 23.22 C ANISOU 1277 CA ASP A 163 2728 3015 3079 -57 56 87 C ATOM 1278 C ASP A 163 23.738 41.520 40.338 1.00 21.48 C ANISOU 1278 C ASP A 163 2571 2730 2860 2 123 85 C ATOM 1279 O ASP A 163 24.492 40.599 40.672 1.00 20.50 O ANISOU 1279 O ASP A 163 2288 2646 2854 -227 215 242 O ATOM 1280 CB ASP A 163 21.513 40.386 40.073 1.00 23.99 C ANISOU 1280 CB ASP A 163 2875 3076 3164 108 -26 84 C ATOM 1281 CG ASP A 163 20.069 40.320 40.475 1.00 24.55 C ANISOU 1281 CG ASP A 163 2982 3439 2906 -166 119 231 C ATOM 1282 OD1 ASP A 163 19.829 40.053 41.687 1.00 25.39 O ANISOU 1282 OD1 ASP A 163 2467 3905 3272 -529 624 210 O ATOM 1283 OD2 ASP A 163 19.203 40.582 39.604 1.00 27.59 O ANISOU 1283 OD2 ASP A 163 2859 3882 3739 -417 -240 -104 O ATOM 1284 N ALA A 164 24.138 42.536 39.589 1.00 20.31 N ANISOU 1284 N ALA A 164 2415 2514 2785 -70 113 70 N ATOM 1285 CA ALA A 164 25.543 42.773 39.245 1.00 21.94 C ANISOU 1285 CA ALA A 164 2598 2717 3019 -31 22 51 C ATOM 1286 C ALA A 164 25.699 44.220 38.812 1.00 22.18 C ANISOU 1286 C ALA A 164 2607 2733 3086 -79 -6 185 C ATOM 1287 O ALA A 164 24.712 44.868 38.485 1.00 21.67 O ANISOU 1287 O ALA A 164 2472 2403 3355 -77 -7 350 O ATOM 1288 CB ALA A 164 25.971 41.882 38.121 1.00 21.07 C ANISOU 1288 CB ALA A 164 2496 2787 2721 -85 39 -31 C ATOM 1289 N THR A 165 26.938 44.709 38.799 1.00 22.01 N ANISOU 1289 N THR A 165 2593 2828 2939 -28 75 155 N ATOM 1290 CA THR A 165 27.236 46.046 38.295 1.00 20.74 C ANISOU 1290 CA THR A 165 2546 2605 2728 20 28 78 C ATOM 1291 C THR A 165 28.292 45.993 37.195 1.00 19.42 C ANISOU 1291 C THR A 165 2347 2486 2543 -16 98 85 C ATOM 1292 O THR A 165 29.131 45.075 37.165 1.00 18.94 O ANISOU 1292 O THR A 165 2009 2591 2594 -116 196 198 O ATOM 1293 CB THR A 165 27.694 47.033 39.389 1.00 20.96 C ANISOU 1293 CB THR A 165 2641 2712 2609 40 -43 134 C ATOM 1294 OG1 THR A 165 28.882 46.563 40.036 1.00 20.37 O ANISOU 1294 OG1 THR A 165 2594 2415 2730 -193 132 607 O ATOM 1295 CG2 THR A 165 26.585 47.261 40.409 1.00 18.97 C ANISOU 1295 CG2 THR A 165 2424 2240 2543 255 -126 134 C ATOM 1296 N LYS A 166 28.243 46.960 36.288 1.00 18.61 N ANISOU 1296 N LYS A 166 2228 2359 2482 93 -123 -79 N ATOM 1297 CA LYS A 166 29.240 47.047 35.225 1.00 18.74 C ANISOU 1297 CA LYS A 166 2398 2308 2412 -55 -59 28 C ATOM 1298 C LYS A 166 30.130 48.275 35.439 1.00 18.65 C ANISOU 1298 C LYS A 166 2514 2263 2308 -39 -111 -67 C ATOM 1299 O LYS A 166 29.633 49.414 35.522 1.00 19.58 O ANISOU 1299 O LYS A 166 2808 2219 2410 -215 70 -165 O ATOM 1300 CB LYS A 166 28.576 47.047 33.832 1.00 19.08 C ANISOU 1300 CB LYS A 166 2409 2352 2487 12 -105 -249 C ATOM 1301 CG LYS A 166 29.544 47.003 32.673 1.00 17.49 C ANISOU 1301 CG LYS A 166 2110 2015 2520 -203 -86 43 C ATOM 1302 CD LYS A 166 29.101 46.094 31.526 1.00 19.21 C ANISOU 1302 CD LYS A 166 2478 2329 2490 -102 -93 50 C ATOM 1303 CE LYS A 166 27.982 46.691 30.651 1.00 19.42 C ANISOU 1303 CE LYS A 166 2253 2481 2641 -243 -62 107 C ATOM 1304 NZ LYS A 166 28.266 48.035 30.131 1.00 20.42 N ANISOU 1304 NZ LYS A 166 2530 2759 2468 -107 -465 35 N ATOM 1305 N VAL A 167 31.429 48.018 35.533 1.00 17.92 N ANISOU 1305 N VAL A 167 2309 2189 2309 -79 111 -77 N ATOM 1306 CA VAL A 167 32.419 49.008 36.005 1.00 17.81 C ANISOU 1306 CA VAL A 167 2330 2130 2306 6 -16 -143 C ATOM 1307 C VAL A 167 33.335 49.485 34.872 1.00 17.14 C ANISOU 1307 C VAL A 167 2293 2086 2132 -80 -40 -116 C ATOM 1308 O VAL A 167 33.960 48.661 34.137 1.00 14.48 O ANISOU 1308 O VAL A 167 1989 1999 1514 -120 374 143 O ATOM 1309 CB VAL A 167 33.254 48.443 37.223 1.00 19.87 C ANISOU 1309 CB VAL A 167 2638 2238 2672 45 -20 -134 C ATOM 1310 CG1 VAL A 167 34.424 49.371 37.601 1.00 18.75 C ANISOU 1310 CG1 VAL A 167 2416 2460 2248 151 35 -320 C ATOM 1311 CG2 VAL A 167 32.387 48.215 38.400 1.00 21.14 C ANISOU 1311 CG2 VAL A 167 2846 2269 2915 71 0 -139 C ATOM 1312 N GLY A 168 33.419 50.814 34.727 1.00 17.71 N ANISOU 1312 N GLY A 168 2526 2232 1968 76 -43 39 N ATOM 1313 CA GLY A 168 34.193 51.461 33.635 1.00 18.84 C ANISOU 1313 CA GLY A 168 2442 2332 2381 -68 42 -71 C ATOM 1314 C GLY A 168 33.511 52.737 33.173 1.00 18.72 C ANISOU 1314 C GLY A 168 2427 2567 2116 -84 -4 137 C ATOM 1315 O GLY A 168 32.338 52.706 32.832 1.00 19.11 O ANISOU 1315 O GLY A 168 2544 2467 2247 -169 -53 222 O ATOM 1316 N ILE A 169 34.231 53.865 33.219 1.00 19.09 N ANISOU 1316 N ILE A 169 2446 2505 2302 -49 19 -47 N ATOM 1317 CA ILE A 169 33.732 55.157 32.773 1.00 20.99 C ANISOU 1317 CA ILE A 169 2719 2625 2632 -32 -42 -9 C ATOM 1318 C ILE A 169 34.787 55.756 31.830 1.00 22.43 C ANISOU 1318 C ILE A 169 2838 2705 2977 -32 -70 52 C ATOM 1319 O ILE A 169 35.784 56.327 32.265 1.00 20.78 O ANISOU 1319 O ILE A 169 2737 2255 2900 -62 -23 233 O ATOM 1320 CB ILE A 169 33.465 56.113 33.947 1.00 20.76 C ANISOU 1320 CB ILE A 169 2678 2380 2828 -64 24 -96 C ATOM 1321 CG1 ILE A 169 32.448 55.536 34.951 1.00 22.26 C ANISOU 1321 CG1 ILE A 169 3027 2449 2979 -67 -142 4 C ATOM 1322 CG2 ILE A 169 33.006 57.449 33.434 1.00 21.69 C ANISOU 1322 CG2 ILE A 169 2563 2792 2885 -50 -2 22 C ATOM 1323 CD1 ILE A 169 31.015 55.596 34.511 1.00 25.65 C ANISOU 1323 CD1 ILE A 169 3124 3124 3495 -57 2 48 C ATOM 1324 N GLY A 170 34.566 55.576 30.535 1.00 23.73 N ANISOU 1324 N GLY A 170 3018 3001 2995 -2 -21 7 N ATOM 1325 CA GLY A 170 35.531 55.955 29.497 1.00 25.13 C ANISOU 1325 CA GLY A 170 3145 3145 3255 -48 86 19 C ATOM 1326 C GLY A 170 36.908 55.361 29.799 1.00 25.96 C ANISOU 1326 C GLY A 170 3192 3317 3352 31 77 12 C ATOM 1327 O GLY A 170 37.858 56.106 30.077 1.00 25.00 O ANISOU 1327 O GLY A 170 3148 3178 3170 12 370 205 O ATOM 1328 N PRO A 171 37.003 54.016 29.798 1.00 26.57 N ANISOU 1328 N PRO A 171 3332 3344 3417 28 169 -48 N ATOM 1329 CA PRO A 171 38.204 53.326 30.249 1.00 28.88 C ANISOU 1329 CA PRO A 171 3661 3565 3745 32 27 20 C ATOM 1330 C PRO A 171 39.395 53.454 29.296 1.00 31.15 C ANISOU 1330 C PRO A 171 3931 3891 4012 9 35 39 C ATOM 1331 O PRO A 171 40.543 53.356 29.737 1.00 32.93 O ANISOU 1331 O PRO A 171 4101 4165 4245 -4 -198 148 O ATOM 1332 CB PRO A 171 37.757 51.867 30.333 1.00 29.22 C ANISOU 1332 CB PRO A 171 3745 3605 3749 24 63 70 C ATOM 1333 CG PRO A 171 36.684 51.746 29.339 1.00 28.94 C ANISOU 1333 CG PRO A 171 3719 3494 3783 -60 40 47 C ATOM 1334 CD PRO A 171 35.955 53.069 29.385 1.00 26.99 C ANISOU 1334 CD PRO A 171 3456 3543 3254 139 114 -258 C ATOM 1335 N GLY A 172 39.144 53.664 28.009 1.00 31.96 N ANISOU 1335 N GLY A 172 4076 3999 4065 35 -31 97 N ATOM 1336 CA GLY A 172 40.240 53.766 27.046 1.00 32.68 C ANISOU 1336 CA GLY A 172 4144 4110 4163 33 76 44 C ATOM 1337 C GLY A 172 41.118 54.992 27.248 1.00 33.76 C ANISOU 1337 C GLY A 172 4165 4316 4347 7 -24 -23 C ATOM 1338 O GLY A 172 40.653 56.051 27.685 1.00 34.04 O ANISOU 1338 O GLY A 172 4122 4299 4511 48 -107 58 O ATOM 1339 N LYS A 173 42.392 54.856 26.880 1.00 35.23 N ANISOU 1339 N LYS A 173 4336 4444 4606 49 -19 -8 N ATOM 1340 CA LYS A 173 43.411 55.873 27.188 1.00 35.88 C ANISOU 1340 CA LYS A 173 4412 4526 4694 -28 13 -24 C ATOM 1341 C LYS A 173 43.188 57.126 26.371 1.00 37.10 C ANISOU 1341 C LYS A 173 4522 4739 4834 -37 -13 -2 C ATOM 1342 O LYS A 173 43.654 58.195 26.732 1.00 39.28 O ANISOU 1342 O LYS A 173 4780 4952 5190 -7 -43 -167 O ATOM 1343 CB LYS A 173 44.829 55.381 26.875 1.00 36.59 C ANISOU 1343 CB LYS A 173 4505 4564 4831 24 -38 48 C ATOM 1344 CG LYS A 173 45.223 53.997 27.388 1.00 37.50 C ANISOU 1344 CG LYS A 173 4751 4737 4758 -69 1 42 C ATOM 1345 CD LYS A 173 45.502 53.978 28.849 1.00 35.90 C ANISOU 1345 CD LYS A 173 4506 4511 4624 47 -84 155 C ATOM 1346 CE LYS A 173 46.415 52.817 29.205 1.00 31.94 C ANISOU 1346 CE LYS A 173 3812 4078 4243 -8 106 -120 C ATOM 1347 NZ LYS A 173 46.658 52.881 30.653 1.00 29.63 N ANISOU 1347 NZ LYS A 173 3659 3722 3874 152 43 118 N ATOM 1348 N VAL A 174 42.500 57.003 25.246 1.00 37.06 N ANISOU 1348 N VAL A 174 4607 4781 4693 -57 44 4 N ATOM 1349 CA VAL A 174 42.247 58.162 24.393 1.00 36.63 C ANISOU 1349 CA VAL A 174 4556 4683 4678 -7 29 47 C ATOM 1350 C VAL A 174 40.802 58.215 23.899 1.00 35.94 C ANISOU 1350 C VAL A 174 4549 4618 4488 28 10 103 C ATOM 1351 O VAL A 174 40.523 58.703 22.804 1.00 35.93 O ANISOU 1351 O VAL A 174 4691 4573 4384 106 63 161 O ATOM 1352 CB VAL A 174 43.257 58.188 23.219 1.00 37.82 C ANISOU 1352 CB VAL A 174 4773 4816 4778 10 70 -22 C ATOM 1353 CG1 VAL A 174 44.657 58.332 23.771 1.00 39.03 C ANISOU 1353 CG1 VAL A 174 4748 5039 5041 46 110 -103 C ATOM 1354 CG2 VAL A 174 43.166 56.915 22.371 1.00 39.54 C ANISOU 1354 CG2 VAL A 174 5126 4941 4955 -16 -40 -3 C ATOM 1355 N CYS A 175 39.875 57.754 24.727 1.00 34.45 N ANISOU 1355 N CYS A 175 4359 4453 4277 28 11 142 N ATOM 1356 CA CYS A 175 38.468 57.759 24.363 1.00 33.48 C ANISOU 1356 CA CYS A 175 4288 4266 4165 -13 -2 53 C ATOM 1357 C CYS A 175 37.846 59.146 24.539 1.00 31.82 C ANISOU 1357 C CYS A 175 4067 4106 3917 -63 17 108 C ATOM 1358 O CYS A 175 38.432 60.037 25.153 1.00 29.60 O ANISOU 1358 O CYS A 175 3807 3759 3678 -6 -26 315 O ATOM 1359 CB CYS A 175 37.707 56.711 25.184 1.00 33.92 C ANISOU 1359 CB CYS A 175 4305 4265 4316 -79 -48 56 C ATOM 1360 SG CYS A 175 37.460 57.141 26.938 1.00 33.91 S ANISOU 1360 SG CYS A 175 4043 4286 4552 -119 -51 220 S ATOM 1361 N ILE A 176 36.634 59.308 24.021 1.00 32.85 N ANISOU 1361 N ILE A 176 4257 4115 4110 17 -107 -10 N ATOM 1362 CA ILE A 176 35.924 60.587 24.036 1.00 32.33 C ANISOU 1362 CA ILE A 176 4179 4047 4054 -8 -71 -42 C ATOM 1363 C ILE A 176 35.688 61.175 25.417 1.00 30.86 C ANISOU 1363 C ILE A 176 3995 3810 3919 -78 -150 -16 C ATOM 1364 O ILE A 176 35.954 62.367 25.646 1.00 30.49 O ANISOU 1364 O ILE A 176 4001 3538 4045 -64 -260 -137 O ATOM 1365 CB ILE A 176 34.531 60.448 23.334 1.00 33.99 C ANISOU 1365 CB ILE A 176 4303 4270 4342 81 -90 -20 C ATOM 1366 CG1 ILE A 176 34.728 60.099 21.863 1.00 36.80 C ANISOU 1366 CG1 ILE A 176 4727 4718 4536 148 -82 34 C ATOM 1367 CG2 ILE A 176 33.685 61.721 23.481 1.00 34.66 C ANISOU 1367 CG2 ILE A 176 4422 4344 4403 89 -27 -43 C ATOM 1368 CD1 ILE A 176 35.910 60.789 21.217 1.00 38.89 C ANISOU 1368 CD1 ILE A 176 4985 4992 4798 -46 -6 135 C ATOM 1369 N THR A 177 35.140 60.357 26.303 1.00 27.89 N ANISOU 1369 N THR A 177 3566 3452 3578 -148 -182 -36 N ATOM 1370 CA THR A 177 34.810 60.781 27.642 1.00 28.30 C ANISOU 1370 CA THR A 177 3547 3523 3680 -100 -43 42 C ATOM 1371 C THR A 177 36.016 61.405 28.346 1.00 24.70 C ANISOU 1371 C THR A 177 3261 3183 2938 -36 -63 75 C ATOM 1372 O THR A 177 35.916 62.517 28.854 1.00 21.89 O ANISOU 1372 O THR A 177 2905 2903 2510 1 41 168 O ATOM 1373 CB THR A 177 34.235 59.611 28.457 1.00 29.05 C ANISOU 1373 CB THR A 177 3658 3629 3750 -105 -59 53 C ATOM 1374 OG1 THR A 177 33.072 59.147 27.779 1.00 31.51 O ANISOU 1374 OG1 THR A 177 3667 3830 4475 -380 -36 96 O ATOM 1375 CG2 THR A 177 33.862 60.057 29.880 1.00 27.93 C ANISOU 1375 CG2 THR A 177 3613 3402 3596 -94 -37 38 C ATOM 1376 N LYS A 178 37.153 60.702 28.334 1.00 24.25 N ANISOU 1376 N LYS A 178 3317 3045 2849 -21 146 -37 N ATOM 1377 CA LYS A 178 38.399 61.193 28.934 1.00 25.65 C ANISOU 1377 CA LYS A 178 3384 3248 3112 -39 37 -10 C ATOM 1378 C LYS A 178 38.807 62.542 28.346 1.00 25.33 C ANISOU 1378 C LYS A 178 3338 3292 2992 -89 10 -18 C ATOM 1379 O LYS A 178 39.056 63.523 29.073 1.00 26.08 O ANISOU 1379 O LYS A 178 3616 3198 3092 -151 71 159 O ATOM 1380 CB LYS A 178 39.509 60.155 28.709 1.00 26.80 C ANISOU 1380 CB LYS A 178 3506 3353 3322 -134 -32 -37 C ATOM 1381 CG LYS A 178 40.823 60.455 29.334 1.00 27.94 C ANISOU 1381 CG LYS A 178 3603 3538 3472 72 -25 -97 C ATOM 1382 CD LYS A 178 41.876 59.539 28.771 1.00 29.73 C ANISOU 1382 CD LYS A 178 3722 3754 3820 146 54 -73 C ATOM 1383 CE LYS A 178 43.284 59.854 29.290 1.00 34.80 C ANISOU 1383 CE LYS A 178 4029 4623 4567 -71 -138 -28 C ATOM 1384 NZ LYS A 178 43.662 61.297 29.327 1.00 37.09 N ANISOU 1384 NZ LYS A 178 4662 4584 4846 70 133 19 N ATOM 1385 N ILE A 179 38.864 62.596 27.019 1.00 25.05 N ANISOU 1385 N ILE A 179 3244 3269 3004 -154 -49 57 N ATOM 1386 CA ILE A 179 39.329 63.782 26.355 1.00 24.90 C ANISOU 1386 CA ILE A 179 3265 3252 2942 -58 -6 22 C ATOM 1387 C ILE A 179 38.385 64.964 26.538 1.00 24.15 C ANISOU 1387 C ILE A 179 3166 3208 2799 -107 24 -9 C ATOM 1388 O ILE A 179 38.824 66.082 26.790 1.00 23.84 O ANISOU 1388 O ILE A 179 3359 3068 2630 -121 44 -273 O ATOM 1389 CB ILE A 179 39.514 63.562 24.831 1.00 25.71 C ANISOU 1389 CB ILE A 179 3464 3370 2933 -66 -11 5 C ATOM 1390 CG1 ILE A 179 40.432 62.365 24.510 1.00 29.29 C ANISOU 1390 CG1 ILE A 179 3516 3707 3907 -58 48 40 C ATOM 1391 CG2 ILE A 179 40.039 64.838 24.207 1.00 25.92 C ANISOU 1391 CG2 ILE A 179 3293 3357 3196 -26 -23 148 C ATOM 1392 CD1 ILE A 179 41.749 62.331 25.220 1.00 34.05 C ANISOU 1392 CD1 ILE A 179 4238 4404 4294 -53 -161 -75 C ATOM 1393 N LYS A 180 37.089 64.739 26.386 1.00 22.89 N ANISOU 1393 N LYS A 180 2947 2960 2788 -94 -79 2 N ATOM 1394 CA LYS A 180 36.176 65.866 26.349 1.00 23.72 C ANISOU 1394 CA LYS A 180 3079 3041 2892 -79 -32 -68 C ATOM 1395 C LYS A 180 35.715 66.362 27.734 1.00 21.71 C ANISOU 1395 C LYS A 180 2860 2818 2569 -85 -115 -87 C ATOM 1396 O LYS A 180 35.407 67.555 27.876 1.00 20.23 O ANISOU 1396 O LYS A 180 2906 2719 2061 -180 -302 23 O ATOM 1397 CB LYS A 180 34.978 65.557 25.438 1.00 26.47 C ANISOU 1397 CB LYS A 180 3338 3324 3395 92 -200 18 C ATOM 1398 CG LYS A 180 35.338 65.459 23.948 1.00 29.09 C ANISOU 1398 CG LYS A 180 3857 3949 3247 33 96 -150 C ATOM 1399 CD LYS A 180 36.280 66.610 23.512 1.00 36.28 C ANISOU 1399 CD LYS A 180 4875 4579 4330 -152 39 -9 C ATOM 1400 CE LYS A 180 36.402 66.785 21.960 1.00 37.44 C ANISOU 1400 CE LYS A 180 5060 4888 4274 0 153 220 C ATOM 1401 NZ LYS A 180 37.163 65.677 21.287 1.00 40.84 N ANISOU 1401 NZ LYS A 180 5278 5459 4781 232 8 -62 N ATOM 1402 N THR A 181 35.668 65.478 28.736 1.00 19.88 N ANISOU 1402 N THR A 181 2614 2478 2460 -39 -180 -184 N ATOM 1403 CA THR A 181 35.130 65.860 30.057 1.00 20.78 C ANISOU 1403 CA THR A 181 2647 2552 2694 -15 6 16 C ATOM 1404 C THR A 181 36.147 65.918 31.201 1.00 18.36 C ANISOU 1404 C THR A 181 2316 2185 2475 -59 33 30 C ATOM 1405 O THR A 181 35.880 66.551 32.199 1.00 19.31 O ANISOU 1405 O THR A 181 2335 2228 2773 -125 -87 142 O ATOM 1406 CB THR A 181 34.005 64.910 30.537 1.00 20.65 C ANISOU 1406 CB THR A 181 2474 2397 2973 -32 -77 -87 C ATOM 1407 OG1 THR A 181 34.567 63.669 30.989 1.00 20.61 O ANISOU 1407 OG1 THR A 181 2631 2462 2736 -211 -56 182 O ATOM 1408 CG2 THR A 181 32.978 64.690 29.446 1.00 22.49 C ANISOU 1408 CG2 THR A 181 3136 2690 2717 55 69 -71 C ATOM 1409 N GLY A 182 37.274 65.215 31.072 1.00 19.13 N ANISOU 1409 N GLY A 182 2305 2420 2542 -57 -9 111 N ATOM 1410 CA GLY A 182 38.262 65.095 32.135 1.00 18.58 C ANISOU 1410 CA GLY A 182 2404 2344 2308 -97 60 -53 C ATOM 1411 C GLY A 182 37.923 64.092 33.226 1.00 18.57 C ANISOU 1411 C GLY A 182 2267 2347 2440 -55 15 21 C ATOM 1412 O GLY A 182 38.668 63.983 34.207 1.00 17.58 O ANISOU 1412 O GLY A 182 1978 2673 2029 -96 359 -23 O ATOM 1413 N PHE A 183 36.803 63.369 33.070 1.00 17.77 N ANISOU 1413 N PHE A 183 2124 2257 2368 -146 -97 55 N ATOM 1414 CA PHE A 183 36.309 62.429 34.088 1.00 18.39 C ANISOU 1414 CA PHE A 183 2269 2328 2388 -71 -37 -5 C ATOM 1415 C PHE A 183 36.436 60.990 33.595 1.00 19.77 C ANISOU 1415 C PHE A 183 2570 2386 2555 -58 -39 3 C ATOM 1416 O PHE A 183 36.279 60.699 32.402 1.00 20.08 O ANISOU 1416 O PHE A 183 3108 2157 2363 -20 -118 313 O ATOM 1417 CB PHE A 183 34.802 62.661 34.373 1.00 17.57 C ANISOU 1417 CB PHE A 183 2356 2182 2138 -75 134 6 C ATOM 1418 CG PHE A 183 34.529 63.782 35.296 1.00 16.64 C ANISOU 1418 CG PHE A 183 1794 2245 2281 -101 7 40 C ATOM 1419 CD1 PHE A 183 34.363 63.545 36.662 1.00 17.68 C ANISOU 1419 CD1 PHE A 183 2044 2262 2410 -120 -17 52 C ATOM 1420 CD2 PHE A 183 34.489 65.084 34.822 1.00 18.67 C ANISOU 1420 CD2 PHE A 183 2601 2072 2418 -83 -57 -103 C ATOM 1421 CE1 PHE A 183 34.125 64.581 37.536 1.00 16.77 C ANISOU 1421 CE1 PHE A 183 1826 2199 2347 -118 339 -68 C ATOM 1422 CE2 PHE A 183 34.243 66.140 35.689 1.00 18.75 C ANISOU 1422 CE2 PHE A 183 2655 2023 2444 12 396 -136 C ATOM 1423 CZ PHE A 183 34.087 65.895 37.044 1.00 17.19 C ANISOU 1423 CZ PHE A 183 2530 1898 2101 322 104 30 C ATOM 1424 N GLY A 184 36.616 60.099 34.545 1.00 20.39 N ANISOU 1424 N GLY A 184 2479 2369 2898 135 -223 -33 N ATOM 1425 CA GLY A 184 36.368 58.683 34.361 1.00 21.62 C ANISOU 1425 CA GLY A 184 2596 2531 3085 56 -148 6 C ATOM 1426 C GLY A 184 37.561 57.817 34.755 1.00 20.01 C ANISOU 1426 C GLY A 184 2429 2347 2825 116 -239 95 C ATOM 1427 O GLY A 184 38.497 58.288 35.414 1.00 20.19 O ANISOU 1427 O GLY A 184 2762 2069 2836 118 -519 181 O ATOM 1428 N THR A 185 37.509 56.561 34.334 1.00 18.03 N ANISOU 1428 N THR A 185 2267 2310 2271 -62 -129 92 N ATOM 1429 CA THR A 185 38.529 55.559 34.667 1.00 19.84 C ANISOU 1429 CA THR A 185 2526 2324 2689 3 -24 56 C ATOM 1430 C THR A 185 39.613 55.386 33.610 1.00 20.03 C ANISOU 1430 C THR A 185 2601 2333 2674 -125 -22 112 C ATOM 1431 O THR A 185 40.480 54.518 33.722 1.00 19.63 O ANISOU 1431 O THR A 185 2544 2264 2649 -118 196 25 O ATOM 1432 CB THR A 185 37.873 54.191 34.933 1.00 20.44 C ANISOU 1432 CB THR A 185 2430 2392 2944 -7 -42 12 C ATOM 1433 OG1 THR A 185 37.168 53.771 33.761 1.00 17.95 O ANISOU 1433 OG1 THR A 185 2205 2019 2594 113 -80 566 O ATOM 1434 CG2 THR A 185 36.981 54.253 36.189 1.00 22.61 C ANISOU 1434 CG2 THR A 185 2572 2719 3298 57 -278 -37 C ATOM 1435 N GLY A 186 39.606 56.262 32.612 1.00 19.74 N ANISOU 1435 N GLY A 186 2655 2610 2232 -117 -107 37 N ATOM 1436 CA GLY A 186 40.568 56.165 31.504 1.00 20.80 C ANISOU 1436 CA GLY A 186 2678 2528 2694 -44 47 60 C ATOM 1437 C GLY A 186 41.979 56.353 32.008 1.00 21.05 C ANISOU 1437 C GLY A 186 2727 2614 2657 -29 44 138 C ATOM 1438 O GLY A 186 42.266 57.315 32.722 1.00 24.25 O ANISOU 1438 O GLY A 186 2932 2806 3472 -292 -112 202 O ATOM 1439 N GLY A 187 42.838 55.401 31.681 1.00 20.20 N ANISOU 1439 N GLY A 187 2629 2528 2517 -49 77 122 N ATOM 1440 CA GLY A 187 44.202 55.411 32.157 1.00 20.54 C ANISOU 1440 CA GLY A 187 2593 2474 2735 -68 162 49 C ATOM 1441 C GLY A 187 44.488 54.827 33.517 1.00 20.77 C ANISOU 1441 C GLY A 187 2597 2554 2740 -66 65 -74 C ATOM 1442 O GLY A 187 45.669 54.765 33.880 1.00 21.13 O ANISOU 1442 O GLY A 187 2546 2408 3074 -186 79 -94 O ATOM 1443 N TRP A 188 43.434 54.394 34.256 1.00 19.86 N ANISOU 1443 N TRP A 188 2482 2350 2711 25 178 -135 N ATOM 1444 CA TRP A 188 43.578 53.635 35.508 1.00 18.67 C ANISOU 1444 CA TRP A 188 2293 2198 2602 -37 140 -57 C ATOM 1445 C TRP A 188 42.456 52.584 35.732 1.00 17.74 C ANISOU 1445 C TRP A 188 2262 2061 2414 12 51 13 C ATOM 1446 O TRP A 188 42.055 52.334 36.880 1.00 14.40 O ANISOU 1446 O TRP A 188 2030 1526 1914 -75 278 -209 O ATOM 1447 CB TRP A 188 43.672 54.562 36.739 1.00 19.52 C ANISOU 1447 CB TRP A 188 2423 2423 2570 -116 27 -25 C ATOM 1448 CG TRP A 188 42.449 55.418 36.988 1.00 18.38 C ANISOU 1448 CG TRP A 188 2559 1982 2442 -103 -97 -173 C ATOM 1449 CD1 TRP A 188 41.950 56.386 36.169 1.00 19.43 C ANISOU 1449 CD1 TRP A 188 2476 2480 2422 -49 -164 -189 C ATOM 1450 CD2 TRP A 188 41.595 55.391 38.149 1.00 20.17 C ANISOU 1450 CD2 TRP A 188 2725 2139 2797 -148 80 38 C ATOM 1451 NE1 TRP A 188 40.849 56.959 36.750 1.00 20.46 N ANISOU 1451 NE1 TRP A 188 2665 2484 2623 168 -252 -12 N ATOM 1452 CE2 TRP A 188 40.588 56.351 37.947 1.00 20.42 C ANISOU 1452 CE2 TRP A 188 2739 2420 2599 -91 121 -185 C ATOM 1453 CE3 TRP A 188 41.577 54.625 39.331 1.00 20.26 C ANISOU 1453 CE3 TRP A 188 2717 2611 2371 -12 97 -7 C ATOM 1454 CZ2 TRP A 188 39.547 56.573 38.883 1.00 19.85 C ANISOU 1454 CZ2 TRP A 188 2686 2303 2553 -58 143 84 C ATOM 1455 CZ3 TRP A 188 40.563 54.853 40.263 1.00 20.28 C ANISOU 1455 CZ3 TRP A 188 2822 2321 2559 120 33 7 C ATOM 1456 CH2 TRP A 188 39.566 55.817 40.037 1.00 18.95 C ANISOU 1456 CH2 TRP A 188 2434 2342 2423 -68 -108 -217 C ATOM 1457 N GLN A 189 41.977 51.989 34.640 1.00 18.21 N ANISOU 1457 N GLN A 189 2261 2081 2574 99 165 -16 N ATOM 1458 CA GLN A 189 40.833 51.084 34.678 1.00 17.47 C ANISOU 1458 CA GLN A 189 2138 2095 2404 24 58 -24 C ATOM 1459 C GLN A 189 41.059 49.914 35.611 1.00 17.47 C ANISOU 1459 C GLN A 189 2090 2048 2500 68 37 -31 C ATOM 1460 O GLN A 189 40.155 49.571 36.410 1.00 17.00 O ANISOU 1460 O GLN A 189 1942 1961 2554 -31 13 -69 O ATOM 1461 CB GLN A 189 40.437 50.633 33.260 1.00 18.98 C ANISOU 1461 CB GLN A 189 2391 2245 2573 74 -40 22 C ATOM 1462 CG GLN A 189 39.383 49.502 33.206 1.00 20.19 C ANISOU 1462 CG GLN A 189 2515 2473 2682 -41 38 96 C ATOM 1463 CD GLN A 189 38.004 49.889 33.770 1.00 22.29 C ANISOU 1463 CD GLN A 189 2780 2771 2917 60 49 -81 C ATOM 1464 OE1 GLN A 189 37.697 51.064 33.932 1.00 23.24 O ANISOU 1464 OE1 GLN A 189 3081 2690 3058 -91 -323 -430 O ATOM 1465 NE2 GLN A 189 37.155 48.885 34.023 1.00 20.24 N ANISOU 1465 NE2 GLN A 189 2301 2693 2695 168 315 -37 N ATOM 1466 N LEU A 190 42.251 49.318 35.598 1.00 17.72 N ANISOU 1466 N LEU A 190 1931 2184 2616 -108 85 30 N ATOM 1467 CA LEU A 190 42.482 48.174 36.519 1.00 17.42 C ANISOU 1467 CA LEU A 190 2074 2093 2451 -60 27 2 C ATOM 1468 C LEU A 190 42.404 48.514 38.015 1.00 16.72 C ANISOU 1468 C LEU A 190 1959 1917 2475 -7 86 -20 C ATOM 1469 O LEU A 190 41.834 47.772 38.808 1.00 16.34 O ANISOU 1469 O LEU A 190 1792 1781 2636 183 22 -24 O ATOM 1470 CB LEU A 190 43.787 47.444 36.208 1.00 18.17 C ANISOU 1470 CB LEU A 190 2200 2090 2612 -41 -129 -111 C ATOM 1471 CG LEU A 190 43.928 46.062 36.840 1.00 18.06 C ANISOU 1471 CG LEU A 190 2106 2365 2389 -72 -4 118 C ATOM 1472 CD1 LEU A 190 42.730 45.124 36.594 1.00 18.36 C ANISOU 1472 CD1 LEU A 190 2263 2060 2651 80 49 -133 C ATOM 1473 CD2 LEU A 190 45.192 45.409 36.354 1.00 18.85 C ANISOU 1473 CD2 LEU A 190 2346 2097 2717 3 87 84 C ATOM 1474 N ALA A 191 43.015 49.631 38.404 1.00 16.76 N ANISOU 1474 N ALA A 191 2234 1911 2222 -158 -10 -54 N ATOM 1475 CA ALA A 191 42.971 50.073 39.790 1.00 17.50 C ANISOU 1475 CA ALA A 191 2270 2061 2318 -96 10 35 C ATOM 1476 C ALA A 191 41.553 50.489 40.170 1.00 16.94 C ANISOU 1476 C ALA A 191 2252 2049 2134 -185 84 10 C ATOM 1477 O ALA A 191 41.130 50.252 41.298 1.00 17.78 O ANISOU 1477 O ALA A 191 2614 2185 1954 -350 135 52 O ATOM 1478 CB ALA A 191 43.973 51.194 40.022 1.00 18.32 C ANISOU 1478 CB ALA A 191 2340 2120 2500 -115 -90 65 C ATOM 1479 N ALA A 192 40.822 51.099 39.233 1.00 16.83 N ANISOU 1479 N ALA A 192 2076 2161 2156 -165 41 -119 N ATOM 1480 CA ALA A 192 39.408 51.450 39.429 1.00 16.45 C ANISOU 1480 CA ALA A 192 2127 2166 1957 -50 38 36 C ATOM 1481 C ALA A 192 38.580 50.189 39.696 1.00 16.31 C ANISOU 1481 C ALA A 192 2032 2158 2008 54 81 71 C ATOM 1482 O ALA A 192 37.729 50.175 40.573 1.00 16.76 O ANISOU 1482 O ALA A 192 2110 2158 2098 -25 423 575 O ATOM 1483 CB ALA A 192 38.849 52.215 38.177 1.00 16.58 C ANISOU 1483 CB ALA A 192 2023 2075 2201 -1 15 86 C ATOM 1484 N LEU A 193 38.847 49.133 38.944 1.00 15.58 N ANISOU 1484 N LEU A 193 2072 2018 1827 -18 33 -73 N ATOM 1485 CA LEU A 193 38.170 47.836 39.110 1.00 16.98 C ANISOU 1485 CA LEU A 193 2173 2196 2081 0 37 82 C ATOM 1486 C LEU A 193 38.436 47.245 40.498 1.00 16.46 C ANISOU 1486 C LEU A 193 2262 2126 1865 -8 -60 85 C ATOM 1487 O LEU A 193 37.529 46.782 41.164 1.00 17.38 O ANISOU 1487 O LEU A 193 2209 2474 1921 46 -73 100 O ATOM 1488 CB LEU A 193 38.660 46.830 38.073 1.00 14.32 C ANISOU 1488 CB LEU A 193 1944 1915 1582 -113 -284 -53 C ATOM 1489 CG LEU A 193 38.174 45.389 38.228 1.00 16.03 C ANISOU 1489 CG LEU A 193 2128 2024 1938 0 -56 -15 C ATOM 1490 CD1 LEU A 193 36.638 45.299 38.170 1.00 19.18 C ANISOU 1490 CD1 LEU A 193 2423 2341 2522 -69 119 -200 C ATOM 1491 CD2 LEU A 193 38.846 44.466 37.230 1.00 16.27 C ANISOU 1491 CD2 LEU A 193 2047 2152 1981 -31 -104 31 C ATOM 1492 N ARG A 194 39.697 47.212 40.875 1.00 18.98 N ANISOU 1492 N ARG A 194 2486 2295 2430 -47 -27 102 N ATOM 1493 CA ARG A 194 40.084 46.768 42.218 1.00 20.22 C ANISOU 1493 CA ARG A 194 2635 2586 2462 16 -34 116 C ATOM 1494 C ARG A 194 39.334 47.532 43.335 1.00 20.23 C ANISOU 1494 C ARG A 194 2614 2501 2570 -19 -2 132 C ATOM 1495 O ARG A 194 38.802 46.943 44.289 1.00 19.54 O ANISOU 1495 O ARG A 194 2690 2230 2503 158 -119 409 O ATOM 1496 CB ARG A 194 41.585 46.967 42.410 1.00 20.90 C ANISOU 1496 CB ARG A 194 2803 2527 2609 -118 42 32 C ATOM 1497 CG ARG A 194 42.074 46.358 43.711 1.00 22.20 C ANISOU 1497 CG ARG A 194 3008 2728 2699 24 -131 229 C ATOM 1498 CD ARG A 194 43.344 47.017 44.247 1.00 28.25 C ANISOU 1498 CD ARG A 194 3342 4045 3345 -212 -116 -229 C ATOM 1499 NE ARG A 194 44.304 46.170 44.978 1.00 36.79 N ANISOU 1499 NE ARG A 194 4440 5108 4428 270 -489 135 N ATOM 1500 CZ ARG A 194 44.149 44.927 45.501 1.00 43.70 C ANISOU 1500 CZ ARG A 194 5475 5611 5516 -84 -110 213 C ATOM 1501 NH1 ARG A 194 43.006 44.230 45.480 1.00 47.26 N ANISOU 1501 NH1 ARG A 194 5982 5924 6051 -222 -85 182 N ATOM 1502 NH2 ARG A 194 45.197 44.351 46.102 1.00 41.98 N ANISOU 1502 NH2 ARG A 194 5390 5146 5413 228 118 187 N ATOM 1503 N TRP A 195 39.302 48.851 43.191 1.00 19.76 N ANISOU 1503 N TRP A 195 2583 2431 2492 73 -40 165 N ATOM 1504 CA TRP A 195 38.723 49.761 44.167 1.00 20.34 C ANISOU 1504 CA TRP A 195 2678 2608 2439 28 0 114 C ATOM 1505 C TRP A 195 37.225 49.497 44.359 1.00 20.04 C ANISOU 1505 C TRP A 195 2543 2570 2498 14 -52 9 C ATOM 1506 O TRP A 195 36.751 49.355 45.510 1.00 20.87 O ANISOU 1506 O TRP A 195 2540 2633 2757 -53 -69 147 O ATOM 1507 CB TRP A 195 39.011 51.197 43.709 1.00 19.88 C ANISOU 1507 CB TRP A 195 2512 2595 2445 1 -154 -60 C ATOM 1508 CG TRP A 195 38.535 52.302 44.553 1.00 20.66 C ANISOU 1508 CG TRP A 195 2624 2599 2623 -46 -72 -50 C ATOM 1509 CD1 TRP A 195 38.629 52.409 45.905 1.00 20.27 C ANISOU 1509 CD1 TRP A 195 2637 2635 2429 -32 88 -18 C ATOM 1510 CD2 TRP A 195 37.965 53.533 44.084 1.00 19.98 C ANISOU 1510 CD2 TRP A 195 2307 2673 2608 -74 -56 -28 C ATOM 1511 NE1 TRP A 195 38.140 53.637 46.318 1.00 22.52 N ANISOU 1511 NE1 TRP A 195 3058 2952 2544 25 -141 -71 N ATOM 1512 CE2 TRP A 195 37.706 54.335 45.223 1.00 22.73 C ANISOU 1512 CE2 TRP A 195 2948 2703 2985 6 56 -48 C ATOM 1513 CE3 TRP A 195 37.632 54.027 42.826 1.00 18.85 C ANISOU 1513 CE3 TRP A 195 2193 2590 2380 73 147 -86 C ATOM 1514 CZ2 TRP A 195 37.134 55.596 45.132 1.00 20.49 C ANISOU 1514 CZ2 TRP A 195 2517 2627 2639 -65 2 -60 C ATOM 1515 CZ3 TRP A 195 37.071 55.300 42.735 1.00 20.61 C ANISOU 1515 CZ3 TRP A 195 2725 2660 2444 83 -21 16 C ATOM 1516 CH2 TRP A 195 36.810 56.059 43.885 1.00 21.85 C ANISOU 1516 CH2 TRP A 195 2864 2735 2701 146 -105 22 C ATOM 1517 N CYS A 196 36.516 49.404 43.239 1.00 21.71 N ANISOU 1517 N CYS A 196 2746 2582 2917 91 -17 55 N ATOM 1518 CA CYS A 196 35.089 49.066 43.173 1.00 21.45 C ANISOU 1518 CA CYS A 196 2690 2719 2738 19 99 27 C ATOM 1519 C CYS A 196 34.803 47.652 43.670 1.00 21.55 C ANISOU 1519 C CYS A 196 2670 2741 2774 -13 170 35 C ATOM 1520 O CYS A 196 33.798 47.424 44.364 1.00 21.25 O ANISOU 1520 O CYS A 196 2826 2726 2519 16 397 214 O ATOM 1521 CB CYS A 196 34.585 49.209 41.711 1.00 20.53 C ANISOU 1521 CB CYS A 196 2550 2635 2616 31 215 -39 C ATOM 1522 SG CYS A 196 34.476 50.916 41.138 1.00 21.94 S ANISOU 1522 SG CYS A 196 2422 2849 3065 203 149 3 S ATOM 1523 N ALA A 197 35.674 46.705 43.315 1.00 21.67 N ANISOU 1523 N ALA A 197 2669 2699 2864 -6 221 -4 N ATOM 1524 CA ALA A 197 35.501 45.299 43.689 1.00 23.73 C ANISOU 1524 CA ALA A 197 3000 2895 3121 -39 161 42 C ATOM 1525 C ALA A 197 35.611 45.052 45.177 1.00 25.22 C ANISOU 1525 C ALA A 197 3253 3092 3235 5 160 35 C ATOM 1526 O ALA A 197 34.920 44.175 45.714 1.00 26.31 O ANISOU 1526 O ALA A 197 3420 3303 3271 -87 369 -15 O ATOM 1527 CB ALA A 197 36.496 44.426 42.959 1.00 24.67 C ANISOU 1527 CB ALA A 197 3237 2705 3432 -35 217 89 C ATOM 1528 N LYS A 198 36.489 45.789 45.843 1.00 25.90 N ANISOU 1528 N LYS A 198 3350 3277 3214 -41 125 50 N ATOM 1529 CA LYS A 198 36.652 45.651 47.285 1.00 29.20 C ANISOU 1529 CA LYS A 198 3766 3782 3545 -17 24 0 C ATOM 1530 C LYS A 198 35.371 46.019 48.052 1.00 30.58 C ANISOU 1530 C LYS A 198 3871 4062 3685 -26 15 87 C ATOM 1531 O LYS A 198 35.150 45.548 49.158 1.00 33.21 O ANISOU 1531 O LYS A 198 4271 4544 3802 -171 -130 117 O ATOM 1532 CB LYS A 198 37.835 46.500 47.770 1.00 30.64 C ANISOU 1532 CB LYS A 198 3995 4048 3599 -70 62 7 C ATOM 1533 CG LYS A 198 39.173 45.835 47.570 1.00 32.00 C ANISOU 1533 CG LYS A 198 3996 4129 4032 -110 -52 32 C ATOM 1534 CD LYS A 198 40.306 46.759 48.033 1.00 34.34 C ANISOU 1534 CD LYS A 198 4165 4564 4316 -142 -132 -16 C ATOM 1535 CE LYS A 198 41.687 46.072 47.930 1.00 38.46 C ANISOU 1535 CE LYS A 198 4496 5137 4977 184 -51 -94 C ATOM 1536 NZ LYS A 198 41.702 44.666 48.484 1.00 43.02 N ANISOU 1536 NZ LYS A 198 5467 5402 5476 17 -286 53 N ATOM 1537 N ALA A 199 34.537 46.865 47.465 1.00 29.30 N ANISOU 1537 N ALA A 199 3738 3873 3521 -23 30 67 N ATOM 1538 CA ALA A 199 33.291 47.268 48.078 1.00 28.80 C ANISOU 1538 CA ALA A 199 3694 3668 3577 -41 1 -6 C ATOM 1539 C ALA A 199 32.111 46.343 47.754 1.00 27.92 C ANISOU 1539 C ALA A 199 3596 3449 3561 -57 108 31 C ATOM 1540 O ALA A 199 31.060 46.479 48.356 1.00 27.79 O ANISOU 1540 O ALA A 199 3727 3235 3595 -241 289 155 O ATOM 1541 CB ALA A 199 32.964 48.672 47.631 1.00 29.28 C ANISOU 1541 CB ALA A 199 3838 3553 3735 -37 127 -50 C ATOM 1542 N ALA A 200 32.253 45.447 46.776 1.00 26.77 N ANISOU 1542 N ALA A 200 3369 3339 3462 -49 27 104 N ATOM 1543 CA ALA A 200 31.082 44.836 46.149 1.00 26.76 C ANISOU 1543 CA ALA A 200 3390 3367 3408 -39 19 92 C ATOM 1544 C ALA A 200 30.650 43.560 46.856 1.00 26.69 C ANISOU 1544 C ALA A 200 3330 3346 3462 -26 -20 126 C ATOM 1545 O ALA A 200 31.497 42.755 47.202 1.00 27.54 O ANISOU 1545 O ALA A 200 3445 3311 3707 -21 14 355 O ATOM 1546 CB ALA A 200 31.368 44.534 44.715 1.00 24.89 C ANISOU 1546 CB ALA A 200 3012 3219 3225 -54 5 77 C ATOM 1547 N SER A 201 29.338 43.398 47.065 1.00 26.42 N ANISOU 1547 N SER A 201 3383 3399 3254 -64 -3 23 N ATOM 1548 CA ASER A 201 28.769 42.140 47.534 0.50 26.50 C ANISOU 1548 CA ASER A 201 3394 3403 3269 -58 18 49 C ATOM 1549 C SER A 201 28.240 41.287 46.364 1.00 26.17 C ANISOU 1549 C SER A 201 3396 3368 3178 -103 64 81 C ATOM 1550 O SER A 201 28.042 40.077 46.499 1.00 27.87 O ANISOU 1550 O SER A 201 3867 3645 3074 -145 62 226 O ATOM 1551 CB ASER A 201 27.670 42.427 48.568 0.50 27.45 C ANISOU 1551 CB ASER A 201 3538 3572 3320 -6 48 42 C ATOM 1552 OG ASER A 201 28.217 43.039 49.742 0.50 28.63 O ANISOU 1552 OG ASER A 201 3480 3789 3608 -261 -114 155 O ATOM 1553 N LYS A 202 28.060 41.898 45.199 1.00 25.62 N ANISOU 1553 N LYS A 202 3121 3271 3341 -77 70 10 N ATOM 1554 CA LYS A 202 27.567 41.188 44.036 1.00 24.61 C ANISOU 1554 CA LYS A 202 3121 3135 3094 -107 92 84 C ATOM 1555 C LYS A 202 28.612 41.151 42.896 1.00 23.01 C ANISOU 1555 C LYS A 202 2899 2782 3061 -56 56 96 C ATOM 1556 O LYS A 202 29.559 41.926 42.933 1.00 22.66 O ANISOU 1556 O LYS A 202 2873 2718 3019 -93 283 320 O ATOM 1557 CB LYS A 202 26.275 41.859 43.599 1.00 24.62 C ANISOU 1557 CB LYS A 202 3127 2895 3333 -74 149 67 C ATOM 1558 CG LYS A 202 25.209 41.786 44.685 1.00 27.67 C ANISOU 1558 CG LYS A 202 3098 3775 3640 47 34 3 C ATOM 1559 CD LYS A 202 23.908 42.436 44.295 1.00 27.36 C ANISOU 1559 CD LYS A 202 3420 3623 3352 17 68 -76 C ATOM 1560 CE LYS A 202 22.831 42.241 45.434 1.00 28.54 C ANISOU 1560 CE LYS A 202 3339 3885 3619 -24 244 -220 C ATOM 1561 NZ LYS A 202 21.630 43.090 45.153 1.00 27.31 N ANISOU 1561 NZ LYS A 202 2941 3879 3556 -107 226 9 N ATOM 1562 N PRO A 203 28.461 40.232 41.914 1.00 21.03 N ANISOU 1562 N PRO A 203 2745 2599 2646 -77 80 181 N ATOM 1563 CA PRO A 203 29.378 40.165 40.775 1.00 22.56 C ANISOU 1563 CA PRO A 203 2841 2742 2985 -66 19 77 C ATOM 1564 C PRO A 203 29.605 41.504 40.039 1.00 19.88 C ANISOU 1564 C PRO A 203 2581 2528 2441 44 -21 168 C ATOM 1565 O PRO A 203 28.696 42.347 39.949 1.00 18.19 O ANISOU 1565 O PRO A 203 2184 2374 2353 5 -193 121 O ATOM 1566 CB PRO A 203 28.720 39.154 39.829 1.00 21.75 C ANISOU 1566 CB PRO A 203 2536 2725 3001 -143 29 -5 C ATOM 1567 CG PRO A 203 27.890 38.309 40.704 1.00 21.71 C ANISOU 1567 CG PRO A 203 3058 2657 2531 -143 87 145 C ATOM 1568 CD PRO A 203 27.424 39.177 41.837 1.00 21.94 C ANISOU 1568 CD PRO A 203 2763 2652 2918 -47 34 22 C ATOM 1569 N ILE A 204 30.829 41.672 39.562 1.00 19.24 N ANISOU 1569 N ILE A 204 2415 2420 2475 40 -154 53 N ATOM 1570 CA ILE A 204 31.204 42.792 38.718 1.00 21.26 C ANISOU 1570 CA ILE A 204 2619 2706 2750 -59 -34 48 C ATOM 1571 C ILE A 204 31.589 42.358 37.299 1.00 20.10 C ANISOU 1571 C ILE A 204 2373 2544 2716 -50 12 -18 C ATOM 1572 O ILE A 204 32.342 41.368 37.105 1.00 21.01 O ANISOU 1572 O ILE A 204 2342 2505 3133 -81 60 236 O ATOM 1573 CB ILE A 204 32.347 43.615 39.369 1.00 20.75 C ANISOU 1573 CB ILE A 204 2514 2625 2741 -130 -38 18 C ATOM 1574 CG1 ILE A 204 31.775 44.547 40.444 1.00 21.02 C ANISOU 1574 CG1 ILE A 204 2801 2841 2343 -266 165 249 C ATOM 1575 CG2 ILE A 204 33.073 44.507 38.346 1.00 18.08 C ANISOU 1575 CG2 ILE A 204 2512 2418 1940 104 -95 -151 C ATOM 1576 CD1 ILE A 204 32.806 45.094 41.335 1.00 26.16 C ANISOU 1576 CD1 ILE A 204 3353 3255 3332 -232 -108 -88 C ATOM 1577 N ILE A 205 31.033 43.078 36.318 1.00 18.79 N ANISOU 1577 N ILE A 205 2307 2372 2458 -10 125 35 N ATOM 1578 CA ILE A 205 31.471 43.011 34.917 1.00 18.80 C ANISOU 1578 CA ILE A 205 2343 2390 2408 21 46 12 C ATOM 1579 C ILE A 205 32.454 44.155 34.670 1.00 17.01 C ANISOU 1579 C ILE A 205 2234 2280 1946 69 -34 87 C ATOM 1580 O ILE A 205 32.090 45.330 34.790 1.00 17.97 O ANISOU 1580 O ILE A 205 2146 2335 2346 87 -7 83 O ATOM 1581 CB ILE A 205 30.294 43.099 33.888 1.00 17.77 C ANISOU 1581 CB ILE A 205 2337 2465 1950 51 186 88 C ATOM 1582 CG1 ILE A 205 29.224 42.038 34.176 1.00 22.04 C ANISOU 1582 CG1 ILE A 205 2948 2632 2791 -49 -176 -256 C ATOM 1583 CG2 ILE A 205 30.827 43.009 32.392 1.00 18.92 C ANISOU 1583 CG2 ILE A 205 2441 2434 2314 -188 261 -26 C ATOM 1584 CD1 ILE A 205 28.206 41.888 33.075 1.00 24.15 C ANISOU 1584 CD1 ILE A 205 2775 3126 3274 -153 -37 109 C ATOM 1585 N ALA A 206 33.706 43.814 34.379 1.00 16.54 N ANISOU 1585 N ALA A 206 2258 2264 1760 82 -65 74 N ATOM 1586 CA ALA A 206 34.758 44.812 34.114 1.00 17.93 C ANISOU 1586 CA ALA A 206 2297 2313 2201 29 -27 15 C ATOM 1587 C ALA A 206 34.658 45.243 32.666 1.00 19.24 C ANISOU 1587 C ALA A 206 2521 2427 2360 106 -12 -14 C ATOM 1588 O ALA A 206 34.746 44.413 31.775 1.00 19.89 O ANISOU 1588 O ALA A 206 2776 2233 2547 94 138 -427 O ATOM 1589 CB ALA A 206 36.102 44.221 34.353 1.00 18.77 C ANISOU 1589 CB ALA A 206 2343 2558 2230 74 -69 228 C ATOM 1590 N ASP A 207 34.457 46.529 32.413 1.00 19.63 N ANISOU 1590 N ASP A 207 2573 2329 2554 -34 -78 -36 N ATOM 1591 CA ASP A 207 34.081 46.959 31.042 1.00 18.98 C ANISOU 1591 CA ASP A 207 2477 2435 2299 70 -31 -14 C ATOM 1592 C ASP A 207 35.148 47.851 30.414 1.00 20.69 C ANISOU 1592 C ASP A 207 2765 2650 2443 58 20 2 C ATOM 1593 O ASP A 207 35.211 49.053 30.691 1.00 20.92 O ANISOU 1593 O ASP A 207 2831 2812 2303 -65 -92 12 O ATOM 1594 CB ASP A 207 32.687 47.645 31.069 1.00 19.45 C ANISOU 1594 CB ASP A 207 2470 2492 2427 -130 -44 136 C ATOM 1595 CG ASP A 207 32.165 48.048 29.674 1.00 20.16 C ANISOU 1595 CG ASP A 207 2489 2790 2380 189 -157 -220 C ATOM 1596 OD1 ASP A 207 32.785 47.721 28.628 1.00 21.18 O ANISOU 1596 OD1 ASP A 207 2697 2891 2456 -133 220 256 O ATOM 1597 OD2 ASP A 207 31.102 48.736 29.640 1.00 17.47 O ANISOU 1597 OD2 ASP A 207 2855 2718 1062 -76 -377 -20 O ATOM 1598 N GLY A 208 35.994 47.259 29.563 1.00 22.46 N ANISOU 1598 N GLY A 208 2849 2807 2877 80 80 19 N ATOM 1599 CA GLY A 208 36.861 48.044 28.677 1.00 21.84 C ANISOU 1599 CA GLY A 208 2706 2915 2675 111 100 -79 C ATOM 1600 C GLY A 208 38.303 48.179 29.162 1.00 23.56 C ANISOU 1600 C GLY A 208 2899 3076 2976 6 35 -89 C ATOM 1601 O GLY A 208 38.660 47.684 30.221 1.00 23.32 O ANISOU 1601 O GLY A 208 2644 3189 3026 -69 -153 -139 O ATOM 1602 N GLY A 209 39.128 48.828 28.346 1.00 24.76 N ANISOU 1602 N GLY A 209 3004 3151 3253 -67 80 -16 N ATOM 1603 CA GLY A 209 40.562 48.900 28.593 1.00 24.68 C ANISOU 1603 CA GLY A 209 3029 3212 3135 -37 -49 -12 C ATOM 1604 C GLY A 209 41.337 47.604 28.366 1.00 25.60 C ANISOU 1604 C GLY A 209 3203 3296 3229 -47 -78 36 C ATOM 1605 O GLY A 209 42.535 47.545 28.649 1.00 27.57 O ANISOU 1605 O GLY A 209 3326 3553 3593 -159 -224 68 O ATOM 1606 N ILE A 210 40.689 46.575 27.817 1.00 23.97 N ANISOU 1606 N ILE A 210 3134 3187 2785 -42 -35 95 N ATOM 1607 CA ILE A 210 41.348 45.301 27.589 1.00 26.01 C ANISOU 1607 CA ILE A 210 3351 3400 3130 -3 -45 13 C ATOM 1608 C ILE A 210 42.108 45.394 26.269 1.00 26.85 C ANISOU 1608 C ILE A 210 3454 3512 3233 91 26 9 C ATOM 1609 O ILE A 210 41.516 45.679 25.228 1.00 28.81 O ANISOU 1609 O ILE A 210 3697 3730 3517 158 -198 -220 O ATOM 1610 CB ILE A 210 40.322 44.141 27.520 1.00 26.21 C ANISOU 1610 CB ILE A 210 3393 3347 3217 33 55 20 C ATOM 1611 CG1 ILE A 210 39.421 44.129 28.775 1.00 25.63 C ANISOU 1611 CG1 ILE A 210 3508 3239 2990 -169 -99 226 C ATOM 1612 CG2 ILE A 210 41.011 42.830 27.274 1.00 25.30 C ANISOU 1612 CG2 ILE A 210 3312 3260 3040 90 -216 20 C ATOM 1613 CD1 ILE A 210 40.147 44.237 30.051 1.00 26.31 C ANISOU 1613 CD1 ILE A 210 3627 3358 3012 -73 -203 -91 C ATOM 1614 N ARG A 211 43.415 45.186 26.315 1.00 26.58 N ANISOU 1614 N ARG A 211 3359 3440 3297 110 -31 58 N ATOM 1615 CA ARG A 211 44.236 45.225 25.095 1.00 28.21 C ANISOU 1615 CA ARG A 211 3578 3634 3505 136 -23 45 C ATOM 1616 C ARG A 211 44.862 43.886 24.662 1.00 26.73 C ANISOU 1616 C ARG A 211 3409 3530 3216 96 1 1 C ATOM 1617 O ARG A 211 45.246 43.732 23.513 1.00 25.19 O ANISOU 1617 O ARG A 211 3372 3463 2735 350 -130 -141 O ATOM 1618 CB ARG A 211 45.317 46.271 25.276 1.00 28.96 C ANISOU 1618 CB ARG A 211 3733 3572 3697 50 -28 25 C ATOM 1619 CG ARG A 211 44.747 47.636 25.615 1.00 33.14 C ANISOU 1619 CG ARG A 211 4167 4197 4225 175 47 -125 C ATOM 1620 CD ARG A 211 45.840 48.574 26.088 1.00 37.95 C ANISOU 1620 CD ARG A 211 4953 4499 4964 39 -265 -171 C ATOM 1621 NE ARG A 211 46.777 48.916 25.025 1.00 48.48 N ANISOU 1621 NE ARG A 211 6042 6350 6026 -71 209 128 N ATOM 1622 CZ ARG A 211 47.828 49.718 25.186 1.00 52.32 C ANISOU 1622 CZ ARG A 211 6530 6719 6629 -224 79 -10 C ATOM 1623 NH1 ARG A 211 48.092 50.269 26.373 1.00 54.37 N ANISOU 1623 NH1 ARG A 211 7025 6934 6697 -116 75 -11 N ATOM 1624 NH2 ARG A 211 48.626 49.966 24.154 1.00 52.21 N ANISOU 1624 NH2 ARG A 211 6561 6672 6604 -222 -24 121 N ATOM 1625 N THR A 212 44.954 42.936 25.587 1.00 25.78 N ANISOU 1625 N THR A 212 3311 3346 3137 126 -25 -24 N ATOM 1626 CA THR A 212 45.605 41.635 25.363 1.00 24.99 C ANISOU 1626 CA THR A 212 3191 3235 3067 21 -18 -2 C ATOM 1627 C THR A 212 44.771 40.578 26.068 1.00 23.06 C ANISOU 1627 C THR A 212 2931 3024 2805 45 -64 -36 C ATOM 1628 O THR A 212 43.985 40.905 26.973 1.00 18.89 O ANISOU 1628 O THR A 212 2894 2635 1646 27 -241 -174 O ATOM 1629 CB THR A 212 47.036 41.563 25.985 1.00 24.36 C ANISOU 1629 CB THR A 212 3075 3125 3054 114 44 -17 C ATOM 1630 OG1 THR A 212 46.943 41.683 27.419 1.00 25.87 O ANISOU 1630 OG1 THR A 212 3282 3494 3054 116 -487 -80 O ATOM 1631 CG2 THR A 212 47.919 42.651 25.491 1.00 25.97 C ANISOU 1631 CG2 THR A 212 3065 3368 3433 157 110 68 C ATOM 1632 N ASN A 213 44.938 39.320 25.674 1.00 21.88 N ANISOU 1632 N ASN A 213 2774 2873 2665 98 -129 1 N ATOM 1633 CA ASN A 213 44.287 38.231 26.408 1.00 22.83 C ANISOU 1633 CA ASN A 213 2839 2917 2915 66 -19 -56 C ATOM 1634 C ASN A 213 44.779 38.121 27.858 1.00 22.00 C ANISOU 1634 C ASN A 213 2749 2733 2875 78 74 -14 C ATOM 1635 O ASN A 213 44.000 37.717 28.720 1.00 23.17 O ANISOU 1635 O ASN A 213 2773 3065 2965 1 137 64 O ATOM 1636 CB ASN A 213 44.409 36.882 25.667 1.00 23.87 C ANISOU 1636 CB ASN A 213 2921 3118 3030 33 -77 -169 C ATOM 1637 CG ASN A 213 43.642 36.854 24.348 1.00 23.43 C ANISOU 1637 CG ASN A 213 3347 3004 2549 177 -13 94 C ATOM 1638 OD1 ASN A 213 42.921 37.786 24.020 1.00 26.73 O ANISOU 1638 OD1 ASN A 213 3604 3300 3251 353 29 -235 O ATOM 1639 ND2 ASN A 213 43.777 35.748 23.602 1.00 23.92 N ANISOU 1639 ND2 ASN A 213 3317 2916 2854 -75 -123 -6 N ATOM 1640 N GLY A 214 46.034 38.520 28.143 1.00 19.66 N ANISOU 1640 N GLY A 214 2545 2397 2529 124 49 -53 N ATOM 1641 CA GLY A 214 46.540 38.533 29.509 1.00 20.57 C ANISOU 1641 CA GLY A 214 2547 2484 2783 37 53 -34 C ATOM 1642 C GLY A 214 45.780 39.480 30.413 1.00 19.79 C ANISOU 1642 C GLY A 214 2456 2416 2646 -65 -31 -29 C ATOM 1643 O GLY A 214 45.725 39.278 31.600 1.00 18.54 O ANISOU 1643 O GLY A 214 2242 2154 2648 -57 159 -6 O ATOM 1644 N ASP A 215 45.139 40.493 29.840 1.00 20.26 N ANISOU 1644 N ASP A 215 2606 2265 2825 -90 82 -107 N ATOM 1645 CA ASP A 215 44.328 41.425 30.639 1.00 19.88 C ANISOU 1645 CA ASP A 215 2542 2409 2602 -47 59 -132 C ATOM 1646 C ASP A 215 43.043 40.825 31.189 1.00 19.03 C ANISOU 1646 C ASP A 215 2610 2230 2388 -6 60 32 C ATOM 1647 O ASP A 215 42.483 41.321 32.178 1.00 19.29 O ANISOU 1647 O ASP A 215 2527 2310 2490 9 188 33 O ATOM 1648 CB ASP A 215 44.003 42.674 29.808 1.00 19.48 C ANISOU 1648 CB ASP A 215 2576 2352 2473 49 -24 -42 C ATOM 1649 CG ASP A 215 45.241 43.523 29.492 1.00 19.95 C ANISOU 1649 CG ASP A 215 2470 2574 2533 43 -142 -195 C ATOM 1650 OD1 ASP A 215 46.246 43.430 30.246 1.00 17.30 O ANISOU 1650 OD1 ASP A 215 2243 2059 2270 150 50 -421 O ATOM 1651 OD2 ASP A 215 45.203 44.294 28.486 1.00 24.90 O ANISOU 1651 OD2 ASP A 215 2913 3302 3243 -195 88 377 O ATOM 1652 N VAL A 216 42.576 39.751 30.577 1.00 19.26 N ANISOU 1652 N VAL A 216 2439 2459 2421 -70 13 6 N ATOM 1653 CA VAL A 216 41.477 38.966 31.167 1.00 19.52 C ANISOU 1653 CA VAL A 216 2523 2365 2527 -51 13 -22 C ATOM 1654 C VAL A 216 41.897 38.372 32.526 1.00 18.71 C ANISOU 1654 C VAL A 216 2333 2221 2553 -138 -38 -87 C ATOM 1655 O VAL A 216 41.197 38.558 33.526 1.00 16.40 O ANISOU 1655 O VAL A 216 2257 1673 2299 -47 52 -214 O ATOM 1656 CB VAL A 216 40.934 37.877 30.168 1.00 20.38 C ANISOU 1656 CB VAL A 216 2515 2543 2685 -58 -56 5 C ATOM 1657 CG1 VAL A 216 39.802 37.104 30.764 1.00 19.57 C ANISOU 1657 CG1 VAL A 216 2611 2411 2414 -37 299 54 C ATOM 1658 CG2 VAL A 216 40.464 38.531 28.897 1.00 20.99 C ANISOU 1658 CG2 VAL A 216 3147 2750 2076 -186 -136 -104 C ATOM 1659 N ALA A 217 43.014 37.643 32.588 1.00 18.42 N ANISOU 1659 N ALA A 217 2197 2288 2512 -123 55 -34 N ATOM 1660 CA ALA A 217 43.521 37.147 33.903 1.00 17.98 C ANISOU 1660 CA ALA A 217 2159 2183 2487 -102 81 73 C ATOM 1661 C ALA A 217 43.731 38.247 34.964 1.00 16.09 C ANISOU 1661 C ALA A 217 2037 2115 1961 100 229 237 C ATOM 1662 O ALA A 217 43.375 38.094 36.176 1.00 14.60 O ANISOU 1662 O ALA A 217 2185 1790 1572 100 230 -48 O ATOM 1663 CB ALA A 217 44.827 36.352 33.660 1.00 19.60 C ANISOU 1663 CB ALA A 217 2266 2348 2832 -37 76 -9 C ATOM 1664 N LYS A 218 44.309 39.369 34.519 1.00 17.22 N ANISOU 1664 N LYS A 218 2007 2127 2408 -46 131 31 N ATOM 1665 CA LYS A 218 44.512 40.533 35.357 1.00 16.24 C ANISOU 1665 CA LYS A 218 2121 2033 2015 -49 98 31 C ATOM 1666 C LYS A 218 43.184 41.056 35.893 1.00 17.48 C ANISOU 1666 C LYS A 218 2125 2131 2384 -19 -22 73 C ATOM 1667 O LYS A 218 43.115 41.350 37.073 1.00 15.71 O ANISOU 1667 O LYS A 218 2096 1789 2083 -129 108 87 O ATOM 1668 CB LYS A 218 45.296 41.665 34.670 1.00 14.96 C ANISOU 1668 CB LYS A 218 2008 1759 1915 -71 36 -107 C ATOM 1669 CG LYS A 218 46.686 41.275 34.194 1.00 16.81 C ANISOU 1669 CG LYS A 218 2136 1746 2505 41 -30 -39 C ATOM 1670 CD LYS A 218 47.411 42.390 33.484 1.00 15.69 C ANISOU 1670 CD LYS A 218 2055 1930 1976 -98 -105 54 C ATOM 1671 CE LYS A 218 48.701 41.911 32.863 1.00 19.15 C ANISOU 1671 CE LYS A 218 2419 2496 2358 -204 150 143 C ATOM 1672 NZ LYS A 218 49.407 42.917 31.990 1.00 22.02 N ANISOU 1672 NZ LYS A 218 2927 2416 3021 -294 166 299 N ATOM 1673 N SER A 219 42.145 41.158 35.045 1.00 18.33 N ANISOU 1673 N SER A 219 2077 2442 2443 -22 26 12 N ATOM 1674 CA SER A 219 40.802 41.584 35.526 1.00 17.46 C ANISOU 1674 CA SER A 219 2207 2121 2303 28 69 -35 C ATOM 1675 C SER A 219 40.233 40.609 36.598 1.00 16.85 C ANISOU 1675 C SER A 219 2177 2081 2143 -28 163 -89 C ATOM 1676 O SER A 219 39.682 41.042 37.609 1.00 17.17 O ANISOU 1676 O SER A 219 2294 2004 2226 72 168 -77 O ATOM 1677 CB SER A 219 39.816 41.717 34.358 1.00 18.11 C ANISOU 1677 CB SER A 219 2042 2350 2488 1 -25 97 C ATOM 1678 OG SER A 219 40.322 42.496 33.274 1.00 18.54 O ANISOU 1678 OG SER A 219 1877 2540 2624 172 -180 329 O ATOM 1679 N ILE A 220 40.428 39.304 36.389 1.00 16.68 N ANISOU 1679 N ILE A 220 2070 2107 2160 76 82 50 N ATOM 1680 CA ILE A 220 40.020 38.276 37.344 1.00 18.25 C ANISOU 1680 CA ILE A 220 2346 2152 2435 45 122 58 C ATOM 1681 C ILE A 220 40.769 38.451 38.671 1.00 17.87 C ANISOU 1681 C ILE A 220 2356 2035 2396 -24 91 67 C ATOM 1682 O ILE A 220 40.135 38.485 39.737 1.00 17.63 O ANISOU 1682 O ILE A 220 2357 1681 2659 -26 283 249 O ATOM 1683 CB ILE A 220 40.205 36.818 36.796 1.00 19.14 C ANISOU 1683 CB ILE A 220 2526 2363 2383 -176 76 65 C ATOM 1684 CG1 ILE A 220 39.316 36.569 35.548 1.00 23.12 C ANISOU 1684 CG1 ILE A 220 2682 3000 3099 -71 -112 102 C ATOM 1685 CG2 ILE A 220 39.881 35.792 37.897 1.00 18.47 C ANISOU 1685 CG2 ILE A 220 2292 2235 2489 -14 -214 195 C ATOM 1686 CD1 ILE A 220 37.817 36.709 35.814 1.00 24.73 C ANISOU 1686 CD1 ILE A 220 3028 2881 3487 7 36 -168 C ATOM 1687 N ARG A 221 42.096 38.633 38.629 1.00 17.86 N ANISOU 1687 N ARG A 221 2361 2158 2266 154 71 63 N ATOM 1688 CA ARG A 221 42.876 38.878 39.866 1.00 18.28 C ANISOU 1688 CA ARG A 221 2314 2207 2424 -2 75 55 C ATOM 1689 C ARG A 221 42.290 39.997 40.697 1.00 16.86 C ANISOU 1689 C ARG A 221 2072 2333 2001 -48 33 120 C ATOM 1690 O ARG A 221 42.171 39.853 41.924 1.00 17.48 O ANISOU 1690 O ARG A 221 2150 2662 1827 -137 -62 -13 O ATOM 1691 CB ARG A 221 44.355 39.201 39.544 1.00 18.86 C ANISOU 1691 CB ARG A 221 2176 2244 2745 118 -69 84 C ATOM 1692 CG ARG A 221 45.182 39.658 40.730 1.00 18.53 C ANISOU 1692 CG ARG A 221 2372 2387 2279 43 214 6 C ATOM 1693 CD ARG A 221 45.107 38.651 41.884 1.00 21.86 C ANISOU 1693 CD ARG A 221 2532 2551 3221 -88 4 244 C ATOM 1694 NE ARG A 221 45.930 38.984 43.027 1.00 20.04 N ANISOU 1694 NE ARG A 221 2538 2573 2502 1 244 84 N ATOM 1695 CZ ARG A 221 45.583 39.803 44.023 1.00 24.39 C ANISOU 1695 CZ ARG A 221 3160 3247 2861 32 167 -95 C ATOM 1696 NH1 ARG A 221 44.395 40.425 44.052 1.00 22.98 N ANISOU 1696 NH1 ARG A 221 3456 2824 2449 60 -129 41 N ATOM 1697 NH2 ARG A 221 46.447 39.998 45.015 1.00 25.28 N ANISOU 1697 NH2 ARG A 221 2871 3331 3401 -158 189 -64 N ATOM 1698 N PHE A 222 41.925 41.099 40.050 1.00 16.79 N ANISOU 1698 N PHE A 222 1880 2174 2322 -212 13 38 N ATOM 1699 CA PHE A 222 41.474 42.290 40.761 1.00 17.66 C ANISOU 1699 CA PHE A 222 2184 2250 2275 -84 -11 29 C ATOM 1700 C PHE A 222 39.957 42.434 40.693 1.00 19.00 C ANISOU 1700 C PHE A 222 2399 2322 2497 26 6 -12 C ATOM 1701 O PHE A 222 39.417 43.518 40.910 1.00 19.72 O ANISOU 1701 O PHE A 222 2678 2281 2532 130 77 139 O ATOM 1702 CB PHE A 222 42.147 43.541 40.192 1.00 17.47 C ANISOU 1702 CB PHE A 222 2388 2072 2177 68 130 113 C ATOM 1703 CG PHE A 222 43.621 43.616 40.472 1.00 17.95 C ANISOU 1703 CG PHE A 222 2431 2337 2053 -243 43 23 C ATOM 1704 CD1 PHE A 222 44.084 43.978 41.725 1.00 21.59 C ANISOU 1704 CD1 PHE A 222 2629 2956 2616 132 -233 -373 C ATOM 1705 CD2 PHE A 222 44.543 43.324 39.481 1.00 21.48 C ANISOU 1705 CD2 PHE A 222 2537 2683 2939 -245 -38 -76 C ATOM 1706 CE1 PHE A 222 45.440 44.048 41.986 1.00 21.05 C ANISOU 1706 CE1 PHE A 222 2442 2499 3055 -7 54 -256 C ATOM 1707 CE2 PHE A 222 45.900 43.392 39.735 1.00 19.45 C ANISOU 1707 CE2 PHE A 222 2418 2616 2354 209 -74 7 C ATOM 1708 CZ PHE A 222 46.349 43.755 40.989 1.00 17.97 C ANISOU 1708 CZ PHE A 222 2547 2190 2090 4 57 17 C ATOM 1709 N GLY A 223 39.276 41.333 40.391 1.00 17.34 N ANISOU 1709 N GLY A 223 2249 2134 2205 -19 -51 91 N ATOM 1710 CA GLY A 223 38.073 40.959 41.112 1.00 17.95 C ANISOU 1710 CA GLY A 223 2321 2236 2261 -108 20 39 C ATOM 1711 C GLY A 223 36.849 40.924 40.218 1.00 19.15 C ANISOU 1711 C GLY A 223 2328 2445 2500 -39 38 3 C ATOM 1712 O GLY A 223 35.716 40.948 40.700 1.00 20.65 O ANISOU 1712 O GLY A 223 2251 2768 2827 -100 124 -63 O ATOM 1713 N ALA A 224 37.078 40.865 38.911 1.00 19.40 N ANISOU 1713 N ALA A 224 2419 2445 2507 -102 19 41 N ATOM 1714 CA ALA A 224 35.991 40.739 37.947 1.00 18.45 C ANISOU 1714 CA ALA A 224 2262 2290 2455 -32 8 24 C ATOM 1715 C ALA A 224 35.403 39.332 37.962 1.00 19.43 C ANISOU 1715 C ALA A 224 2412 2277 2694 -50 -3 25 C ATOM 1716 O ALA A 224 36.082 38.368 38.313 1.00 19.49 O ANISOU 1716 O ALA A 224 2490 2029 2885 -126 -125 206 O ATOM 1717 CB ALA A 224 36.476 41.099 36.551 1.00 19.14 C ANISOU 1717 CB ALA A 224 2317 2307 2645 -63 -53 198 C ATOM 1718 N THR A 225 34.135 39.222 37.578 1.00 17.51 N ANISOU 1718 N THR A 225 2196 2223 2232 41 73 66 N ATOM 1719 CA THR A 225 33.532 37.927 37.286 1.00 17.46 C ANISOU 1719 CA THR A 225 2191 2384 2055 -36 -52 -29 C ATOM 1720 C THR A 225 33.357 37.726 35.785 1.00 18.08 C ANISOU 1720 C THR A 225 2255 2483 2130 41 -123 -202 C ATOM 1721 O THR A 225 33.672 36.663 35.250 1.00 19.48 O ANISOU 1721 O THR A 225 2439 2572 2388 153 -144 35 O ATOM 1722 CB THR A 225 32.175 37.790 38.001 1.00 17.90 C ANISOU 1722 CB THR A 225 2269 2448 2083 -184 -165 -158 C ATOM 1723 OG1 THR A 225 32.389 37.579 39.402 1.00 16.58 O ANISOU 1723 OG1 THR A 225 2373 2230 1695 -289 19 -69 O ATOM 1724 CG2 THR A 225 31.466 36.519 37.559 1.00 19.50 C ANISOU 1724 CG2 THR A 225 2274 2327 2806 -31 68 12 C ATOM 1725 N MET A 226 32.851 38.753 35.110 1.00 19.85 N ANISOU 1725 N MET A 226 2876 2519 2146 16 92 -79 N ATOM 1726 CA MET A 226 32.870 38.796 33.653 1.00 19.68 C ANISOU 1726 CA MET A 226 2669 2544 2264 36 3 -86 C ATOM 1727 C MET A 226 33.668 39.994 33.147 1.00 18.92 C ANISOU 1727 C MET A 226 2543 2478 2166 58 -60 -7 C ATOM 1728 O MET A 226 33.656 41.062 33.758 1.00 18.50 O ANISOU 1728 O MET A 226 2656 2166 2204 40 117 132 O ATOM 1729 CB MET A 226 31.445 38.842 33.099 1.00 22.76 C ANISOU 1729 CB MET A 226 3006 2901 2740 67 -4 -232 C ATOM 1730 CG MET A 226 31.312 38.311 31.682 1.00 26.60 C ANISOU 1730 CG MET A 226 3504 3633 2970 119 -142 -124 C ATOM 1731 SD MET A 226 31.530 36.523 31.585 1.00 28.22 S ANISOU 1731 SD MET A 226 3210 3623 3889 426 -134 -456 S ATOM 1732 CE MET A 226 29.973 35.956 32.266 1.00 34.92 C ANISOU 1732 CE MET A 226 3920 4759 4586 56 -161 142 C ATOM 1733 N VAL A 227 34.361 39.807 32.029 1.00 17.23 N ANISOU 1733 N VAL A 227 2060 2435 2048 40 -212 88 N ATOM 1734 CA VAL A 227 35.119 40.886 31.407 1.00 19.42 C ANISOU 1734 CA VAL A 227 2472 2642 2264 16 -139 0 C ATOM 1735 C VAL A 227 34.529 41.264 30.053 1.00 18.28 C ANISOU 1735 C VAL A 227 2444 2542 1958 -22 13 9 C ATOM 1736 O VAL A 227 34.531 40.462 29.119 1.00 20.34 O ANISOU 1736 O VAL A 227 2654 2830 2243 -112 -107 -187 O ATOM 1737 CB VAL A 227 36.598 40.500 31.221 1.00 19.77 C ANISOU 1737 CB VAL A 227 2626 2608 2275 83 -126 -70 C ATOM 1738 CG1 VAL A 227 37.384 41.666 30.641 1.00 18.45 C ANISOU 1738 CG1 VAL A 227 2076 2979 1953 -91 -241 -161 C ATOM 1739 CG2 VAL A 227 37.201 40.045 32.541 1.00 18.04 C ANISOU 1739 CG2 VAL A 227 2272 2392 2190 -17 -52 -254 C ATOM 1740 N MET A 228 34.023 42.489 29.954 1.00 18.12 N ANISOU 1740 N MET A 228 2337 2607 1940 -72 -110 67 N ATOM 1741 CA MET A 228 33.419 42.975 28.703 1.00 19.84 C ANISOU 1741 CA MET A 228 2572 2567 2397 12 -175 95 C ATOM 1742 C MET A 228 34.486 43.555 27.768 1.00 20.86 C ANISOU 1742 C MET A 228 2692 2716 2517 -42 -151 113 C ATOM 1743 O MET A 228 35.219 44.486 28.143 1.00 20.20 O ANISOU 1743 O MET A 228 2752 2873 2048 -239 -287 32 O ATOM 1744 CB MET A 228 32.277 43.983 28.944 1.00 18.32 C ANISOU 1744 CB MET A 228 2543 2442 1975 -52 -142 283 C ATOM 1745 CG MET A 228 31.671 44.525 27.580 1.00 16.35 C ANISOU 1745 CG MET A 228 2152 2607 1453 -153 -225 19 C ATOM 1746 SD MET A 228 30.156 45.457 27.777 1.00 20.72 S ANISOU 1746 SD MET A 228 2536 2533 2800 -10 -477 232 S ATOM 1747 CE MET A 228 29.018 44.118 28.083 1.00 21.39 C ANISOU 1747 CE MET A 228 2848 2508 2770 39 -254 6 C ATOM 1748 N ILE A 229 34.525 43.027 26.540 1.00 22.18 N ANISOU 1748 N ILE A 229 2839 2866 2721 46 -164 -71 N ATOM 1749 CA ILE A 229 35.577 43.320 25.551 1.00 24.04 C ANISOU 1749 CA ILE A 229 3066 3045 3023 18 -87 12 C ATOM 1750 C ILE A 229 35.053 43.896 24.236 1.00 25.34 C ANISOU 1750 C ILE A 229 3263 3201 3164 14 -126 -17 C ATOM 1751 O ILE A 229 34.166 43.314 23.617 1.00 25.32 O ANISOU 1751 O ILE A 229 3165 3287 3167 214 -226 -30 O ATOM 1752 CB ILE A 229 36.346 42.026 25.231 1.00 24.81 C ANISOU 1752 CB ILE A 229 3107 3265 3052 49 -108 -59 C ATOM 1753 CG1 ILE A 229 36.951 41.472 26.539 1.00 23.75 C ANISOU 1753 CG1 ILE A 229 3056 3198 2769 189 80 70 C ATOM 1754 CG2 ILE A 229 37.414 42.264 24.187 1.00 24.17 C ANISOU 1754 CG2 ILE A 229 3001 3107 3075 35 -75 77 C ATOM 1755 CD1 ILE A 229 37.819 40.217 26.388 1.00 24.18 C ANISOU 1755 CD1 ILE A 229 3201 2997 2988 51 -223 -64 C ATOM 1756 N GLY A 230 35.632 45.024 23.801 1.00 26.47 N ANISOU 1756 N GLY A 230 3397 3472 3189 16 -119 7 N ATOM 1757 CA GLY A 230 35.280 45.662 22.522 1.00 27.38 C ANISOU 1757 CA GLY A 230 3508 3515 3380 66 -43 106 C ATOM 1758 C GLY A 230 36.275 45.332 21.416 1.00 27.26 C ANISOU 1758 C GLY A 230 3588 3566 3202 81 -42 57 C ATOM 1759 O GLY A 230 36.060 44.395 20.651 1.00 28.96 O ANISOU 1759 O GLY A 230 3767 3690 3546 145 -124 108 O ATOM 1760 N SER A 231 37.384 46.069 21.383 1.00 28.64 N ANISOU 1760 N SER A 231 3774 3725 3381 78 -51 50 N ATOM 1761 CA SER A 231 38.406 45.982 20.312 1.00 30.56 C ANISOU 1761 CA SER A 231 3808 4007 3795 42 16 11 C ATOM 1762 C SER A 231 38.868 44.573 19.949 1.00 31.72 C ANISOU 1762 C SER A 231 4016 4109 3925 51 4 -37 C ATOM 1763 O SER A 231 39.059 44.268 18.774 1.00 32.95 O ANISOU 1763 O SER A 231 4134 4388 3997 96 105 -33 O ATOM 1764 CB SER A 231 39.650 46.808 20.678 1.00 31.77 C ANISOU 1764 CB SER A 231 4020 4093 3956 56 -19 -56 C ATOM 1765 OG SER A 231 40.349 46.213 21.782 1.00 38.47 O ANISOU 1765 OG SER A 231 4780 5356 4481 90 29 129 O ATOM 1766 N LEU A 232 39.095 43.725 20.942 1.00 31.93 N ANISOU 1766 N LEU A 232 3992 4129 4009 18 88 12 N ATOM 1767 CA LEU A 232 39.620 42.401 20.643 1.00 32.15 C ANISOU 1767 CA LEU A 232 4030 4121 4064 3 -13 -51 C ATOM 1768 C LEU A 232 38.605 41.580 19.849 1.00 32.02 C ANISOU 1768 C LEU A 232 3969 4086 4109 -14 -16 -102 C ATOM 1769 O LEU A 232 38.999 40.660 19.132 1.00 28.10 O ANISOU 1769 O LEU A 232 3613 3931 3131 -40 -56 -257 O ATOM 1770 CB LEU A 232 40.078 41.646 21.892 1.00 32.74 C ANISOU 1770 CB LEU A 232 3999 4359 4079 -7 32 0 C ATOM 1771 CG LEU A 232 41.433 42.033 22.523 1.00 33.50 C ANISOU 1771 CG LEU A 232 4196 4411 4120 -45 44 -66 C ATOM 1772 CD1 LEU A 232 41.541 41.356 23.877 1.00 31.68 C ANISOU 1772 CD1 LEU A 232 3727 4187 4120 196 -84 55 C ATOM 1773 CD2 LEU A 232 42.607 41.629 21.639 1.00 34.70 C ANISOU 1773 CD2 LEU A 232 4110 4566 4507 -98 -5 -84 C ATOM 1774 N PHE A 233 37.317 41.910 19.986 1.00 32.73 N ANISOU 1774 N PHE A 233 4002 4067 4365 -17 -46 -22 N ATOM 1775 CA PHE A 233 36.256 41.219 19.232 1.00 33.91 C ANISOU 1775 CA PHE A 233 4180 4375 4326 13 -68 -42 C ATOM 1776 C PHE A 233 35.861 41.947 17.962 1.00 34.13 C ANISOU 1776 C PHE A 233 4225 4446 4295 19 -37 -29 C ATOM 1777 O PHE A 233 35.066 41.427 17.176 1.00 33.05 O ANISOU 1777 O PHE A 233 4135 4384 4037 67 9 -60 O ATOM 1778 CB PHE A 233 35.003 41.046 20.099 1.00 33.97 C ANISOU 1778 CB PHE A 233 4156 4366 4383 -14 -54 -32 C ATOM 1779 CG PHE A 233 35.099 39.949 21.128 1.00 32.16 C ANISOU 1779 CG PHE A 233 3961 4069 4189 -3 -37 -26 C ATOM 1780 CD1 PHE A 233 35.375 38.650 20.753 1.00 34.58 C ANISOU 1780 CD1 PHE A 233 4430 4315 4391 107 -47 57 C ATOM 1781 CD2 PHE A 233 34.821 40.205 22.461 1.00 32.99 C ANISOU 1781 CD2 PHE A 233 4181 4142 4208 26 -115 -2 C ATOM 1782 CE1 PHE A 233 35.428 37.644 21.703 1.00 35.67 C ANISOU 1782 CE1 PHE A 233 4727 4350 4473 2 -17 55 C ATOM 1783 CE2 PHE A 233 34.874 39.211 23.411 1.00 32.47 C ANISOU 1783 CE2 PHE A 233 3985 4049 4302 31 121 -44 C ATOM 1784 CZ PHE A 233 35.170 37.924 23.042 1.00 33.17 C ANISOU 1784 CZ PHE A 233 4082 4106 4412 12 145 -141 C ATOM 1785 N ALA A 234 36.379 43.150 17.764 1.00 35.49 N ANISOU 1785 N ALA A 234 4376 4598 4508 -6 -67 -99 N ATOM 1786 CA ALA A 234 36.070 43.922 16.558 1.00 37.82 C ANISOU 1786 CA ALA A 234 4746 4876 4747 15 -52 14 C ATOM 1787 C ALA A 234 36.863 43.403 15.364 1.00 40.69 C ANISOU 1787 C ALA A 234 5100 5326 5032 74 -25 -92 C ATOM 1788 O ALA A 234 38.004 42.934 15.514 1.00 42.12 O ANISOU 1788 O ALA A 234 5263 5513 5225 136 -157 -145 O ATOM 1789 CB ALA A 234 36.349 45.389 16.766 1.00 37.83 C ANISOU 1789 CB ALA A 234 4754 4931 4686 -6 -29 -21 C ATOM 1790 N GLY A 235 36.253 43.469 14.179 1.00 41.81 N ANISOU 1790 N GLY A 235 5280 5493 5112 103 -48 -27 N ATOM 1791 CA GLY A 235 36.970 43.152 12.949 1.00 42.16 C ANISOU 1791 CA GLY A 235 5350 5525 5143 36 -5 -28 C ATOM 1792 C GLY A 235 37.156 41.680 12.638 1.00 43.62 C ANISOU 1792 C GLY A 235 5512 5634 5426 57 -36 -13 C ATOM 1793 O GLY A 235 38.170 41.299 12.032 1.00 44.86 O ANISOU 1793 O GLY A 235 5657 5807 5581 130 77 -86 O ATOM 1794 N HIS A 236 36.195 40.852 13.051 1.00 43.85 N ANISOU 1794 N HIS A 236 5524 5707 5429 -3 -40 -4 N ATOM 1795 CA HIS A 236 36.092 39.463 12.566 1.00 45.05 C ANISOU 1795 CA HIS A 236 5734 5739 5642 25 -21 -12 C ATOM 1796 C HIS A 236 35.211 39.351 11.325 1.00 46.23 C ANISOU 1796 C HIS A 236 5957 5958 5648 53 -77 -23 C ATOM 1797 O HIS A 236 34.361 40.200 11.094 1.00 45.60 O ANISOU 1797 O HIS A 236 5997 5999 5328 119 -157 -34 O ATOM 1798 CB HIS A 236 35.514 38.564 13.643 1.00 43.90 C ANISOU 1798 CB HIS A 236 5625 5656 5399 68 -117 -43 C ATOM 1799 CG HIS A 236 36.474 38.301 14.737 1.00 42.74 C ANISOU 1799 CG HIS A 236 5394 5536 5306 77 -25 -65 C ATOM 1800 ND1 HIS A 236 37.529 37.433 14.586 1.00 40.83 N ANISOU 1800 ND1 HIS A 236 5273 5273 4968 54 17 -102 N ATOM 1801 CD2 HIS A 236 36.593 38.844 15.972 1.00 39.59 C ANISOU 1801 CD2 HIS A 236 4984 5213 4843 79 45 37 C ATOM 1802 CE1 HIS A 236 38.243 37.431 15.697 1.00 41.07 C ANISOU 1802 CE1 HIS A 236 5180 5288 5135 129 41 -65 C ATOM 1803 NE2 HIS A 236 37.699 38.279 16.550 1.00 37.84 N ANISOU 1803 NE2 HIS A 236 5062 5392 3924 -91 -74 61 N ATOM 1804 N GLU A 237 35.383 38.272 10.561 1.00 48.22 N ANISOU 1804 N GLU A 237 6165 6163 5992 23 -47 -58 N ATOM 1805 CA GLU A 237 34.559 38.056 9.372 1.00 48.37 C ANISOU 1805 CA GLU A 237 6179 6158 6039 11 -77 -56 C ATOM 1806 C GLU A 237 33.077 38.202 9.732 1.00 48.97 C ANISOU 1806 C GLU A 237 6216 6261 6128 7 -55 -45 C ATOM 1807 O GLU A 237 32.333 38.914 9.050 1.00 49.24 O ANISOU 1807 O GLU A 237 6163 6308 6238 23 -99 -85 O ATOM 1808 CB GLU A 237 34.846 36.683 8.736 1.00 49.43 C ANISOU 1808 CB GLU A 237 6281 6287 6211 41 -63 -21 C ATOM 1809 CG GLU A 237 34.145 36.432 7.389 1.00 50.36 C ANISOU 1809 CG GLU A 237 6401 6517 6216 -4 23 -170 C ATOM 1810 CD GLU A 237 34.255 37.613 6.412 1.00 56.54 C ANISOU 1810 CD GLU A 237 7316 7133 7031 19 7 107 C ATOM 1811 OE1 GLU A 237 35.324 38.286 6.366 1.00 58.27 O ANISOU 1811 OE1 GLU A 237 7526 7543 7070 -103 147 -7 O ATOM 1812 OE2 GLU A 237 33.264 37.863 5.685 1.00 59.92 O ANISOU 1812 OE2 GLU A 237 7536 7759 7472 100 -72 -69 O ATOM 1813 N GLU A 238 32.682 37.583 10.845 1.00 48.81 N ANISOU 1813 N GLU A 238 6200 6205 6140 -10 -44 -13 N ATOM 1814 CA GLU A 238 31.311 37.660 11.358 1.00 49.25 C ANISOU 1814 CA GLU A 238 6259 6281 6173 -12 -57 -9 C ATOM 1815 C GLU A 238 30.884 39.034 11.868 1.00 48.52 C ANISOU 1815 C GLU A 238 6190 6219 6025 9 -69 -13 C ATOM 1816 O GLU A 238 29.699 39.288 12.032 1.00 47.87 O ANISOU 1816 O GLU A 238 6208 6212 5769 -53 -11 -50 O ATOM 1817 CB GLU A 238 31.116 36.677 12.510 1.00 49.64 C ANISOU 1817 CB GLU A 238 6309 6321 6229 -32 -28 41 C ATOM 1818 CG GLU A 238 31.338 35.231 12.141 1.00 50.68 C ANISOU 1818 CG GLU A 238 6432 6409 6415 -22 -31 -59 C ATOM 1819 CD GLU A 238 32.773 34.763 12.307 1.00 50.84 C ANISOU 1819 CD GLU A 238 6380 6441 6494 -53 -87 14 C ATOM 1820 OE1 GLU A 238 33.700 35.597 12.381 1.00 49.57 O ANISOU 1820 OE1 GLU A 238 6312 6128 6392 47 -194 42 O ATOM 1821 OE2 GLU A 238 32.972 33.538 12.355 1.00 53.13 O ANISOU 1821 OE2 GLU A 238 6701 6625 6857 57 -178 -31 O ATOM 1822 N SER A 239 31.835 39.910 12.147 1.00 49.20 N ANISOU 1822 N SER A 239 6281 6223 6189 13 -65 32 N ATOM 1823 CA SER A 239 31.488 41.188 12.737 1.00 50.38 C ANISOU 1823 CA SER A 239 6394 6405 6342 0 -7 -33 C ATOM 1824 C SER A 239 30.743 42.045 11.722 1.00 51.04 C ANISOU 1824 C SER A 239 6455 6509 6429 -6 -27 -14 C ATOM 1825 O SER A 239 30.917 41.877 10.512 1.00 49.47 O ANISOU 1825 O SER A 239 6167 6353 6276 -10 -39 7 O ATOM 1826 CB SER A 239 32.729 41.932 13.219 1.00 49.79 C ANISOU 1826 CB SER A 239 6301 6349 6268 60 -27 -5 C ATOM 1827 OG SER A 239 33.442 41.152 14.154 1.00 46.65 O ANISOU 1827 OG SER A 239 5992 6010 5723 -26 171 -21 O ATOM 1828 N PRO A 240 29.878 42.942 12.215 1.00 52.45 N ANISOU 1828 N PRO A 240 6598 6667 6663 34 -13 -37 N ATOM 1829 CA PRO A 240 29.332 44.012 11.399 1.00 54.57 C ANISOU 1829 CA PRO A 240 6908 6883 6944 59 -73 -14 C ATOM 1830 C PRO A 240 30.386 44.707 10.531 1.00 56.42 C ANISOU 1830 C PRO A 240 7114 7155 7168 15 1 -7 C ATOM 1831 O PRO A 240 31.558 44.787 10.910 1.00 56.44 O ANISOU 1831 O PRO A 240 7151 7166 7125 54 -51 -15 O ATOM 1832 CB PRO A 240 28.761 44.973 12.442 1.00 53.93 C ANISOU 1832 CB PRO A 240 6844 6806 6841 -18 -4 15 C ATOM 1833 CG PRO A 240 28.337 44.068 13.568 1.00 52.61 C ANISOU 1833 CG PRO A 240 6658 6736 6593 8 -100 -22 C ATOM 1834 CD PRO A 240 29.322 42.945 13.582 1.00 51.96 C ANISOU 1834 CD PRO A 240 6618 6576 6549 2 -10 -16 C ATOM 1835 N GLY A 241 29.956 45.195 9.370 1.00 59.16 N ANISOU 1835 N GLY A 241 7491 7508 7477 22 -39 10 N ATOM 1836 CA GLY A 241 30.832 45.910 8.438 1.00 61.19 C ANISOU 1836 CA GLY A 241 7759 7740 7749 -33 -10 99 C ATOM 1837 C GLY A 241 31.187 45.050 7.247 1.00 63.14 C ANISOU 1837 C GLY A 241 8025 8034 7928 28 -24 -1 C ATOM 1838 O GLY A 241 30.643 43.958 7.075 1.00 63.06 O ANISOU 1838 O GLY A 241 7994 8098 7866 15 -19 -10 O ATOM 1839 N GLU A 242 32.113 45.537 6.432 1.00 65.62 N ANISOU 1839 N GLU A 242 8282 8381 8267 5 7 24 N ATOM 1840 CA GLU A 242 32.539 44.813 5.239 1.00 67.96 C ANISOU 1840 CA GLU A 242 8643 8658 8520 -8 37 -24 C ATOM 1841 C GLU A 242 34.038 44.536 5.253 1.00 69.53 C ANISOU 1841 C GLU A 242 8772 8867 8778 -3 30 -7 C ATOM 1842 O GLU A 242 34.834 45.314 5.802 1.00 69.65 O ANISOU 1842 O GLU A 242 8812 8884 8767 -35 59 -35 O ATOM 1843 CB GLU A 242 32.120 45.526 3.939 1.00 68.77 C ANISOU 1843 CB GLU A 242 8705 8737 8685 -2 -8 34 C ATOM 1844 CG GLU A 242 31.905 47.038 4.013 1.00 70.40 C ANISOU 1844 CG GLU A 242 8961 8847 8941 15 -34 41 C ATOM 1845 CD GLU A 242 31.259 47.586 2.738 1.00 70.37 C ANISOU 1845 CD GLU A 242 8964 8904 8867 -2 -16 55 C ATOM 1846 OE1 GLU A 242 31.617 47.111 1.634 1.00 72.48 O ANISOU 1846 OE1 GLU A 242 9267 9210 9062 35 0 -57 O ATOM 1847 OE2 GLU A 242 30.390 48.484 2.839 1.00 73.26 O ANISOU 1847 OE2 GLU A 242 9224 9244 9365 144 14 -28 O ATOM 1848 N THR A 243 34.397 43.398 4.663 1.00 70.63 N ANISOU 1848 N THR A 243 8950 8961 8925 11 15 -18 N ATOM 1849 CA THR A 243 35.782 42.990 4.521 1.00 71.14 C ANISOU 1849 CA THR A 243 8993 9028 9009 37 2 -24 C ATOM 1850 C THR A 243 36.388 43.700 3.312 1.00 72.21 C ANISOU 1850 C THR A 243 9141 9160 9135 5 11 -8 C ATOM 1851 O THR A 243 35.741 43.828 2.269 1.00 72.95 O ANISOU 1851 O THR A 243 9217 9266 9233 6 -9 -36 O ATOM 1852 CB THR A 243 35.885 41.467 4.332 1.00 71.33 C ANISOU 1852 CB THR A 243 9045 9038 9017 21 -25 -21 C ATOM 1853 OG1 THR A 243 35.233 40.798 5.426 1.00 70.98 O ANISOU 1853 OG1 THR A 243 8924 9034 9010 0 -11 -96 O ATOM 1854 CG2 THR A 243 37.342 41.028 4.246 1.00 70.79 C ANISOU 1854 CG2 THR A 243 8960 9007 8929 1 10 5 C ATOM 1855 N ILE A 244 37.629 44.153 3.461 1.00 72.67 N ANISOU 1855 N ILE A 244 9191 9218 9200 -5 -3 -15 N ATOM 1856 CA ILE A 244 38.325 44.941 2.441 1.00 72.74 C ANISOU 1856 CA ILE A 244 9208 9224 9206 -7 11 9 C ATOM 1857 C ILE A 244 39.541 44.172 1.929 1.00 72.86 C ANISOU 1857 C ILE A 244 9202 9269 9212 1 29 9 C ATOM 1858 O ILE A 244 40.379 43.724 2.713 1.00 72.92 O ANISOU 1858 O ILE A 244 9181 9322 9201 19 59 1 O ATOM 1859 CB ILE A 244 38.765 46.308 3.022 1.00 73.03 C ANISOU 1859 CB ILE A 244 9277 9248 9220 -9 7 1 C ATOM 1860 CG1 ILE A 244 37.531 47.195 3.276 1.00 73.51 C ANISOU 1860 CG1 ILE A 244 9314 9290 9325 8 -3 -4 C ATOM 1861 CG2 ILE A 244 39.768 47.008 2.096 1.00 72.75 C ANISOU 1861 CG2 ILE A 244 9213 9202 9226 -5 3 0 C ATOM 1862 CD1 ILE A 244 37.624 48.080 4.541 1.00 73.48 C ANISOU 1862 CD1 ILE A 244 9304 9288 9324 -7 -13 -10 C ATOM 1863 N ASN A 268 44.217 36.559 -2.886 1.00 67.28 N ANISOU 1863 N ASN A 268 8552 8488 8523 -32 25 -5 N ATOM 1864 CA ASN A 268 45.257 37.549 -2.595 1.00 66.81 C ANISOU 1864 CA ASN A 268 8496 8427 8458 -9 4 -18 C ATOM 1865 C ASN A 268 44.712 38.921 -2.132 1.00 66.95 C ANISOU 1865 C ASN A 268 8529 8443 8466 -16 13 -15 C ATOM 1866 O ASN A 268 44.196 39.028 -1.012 1.00 68.05 O ANISOU 1866 O ASN A 268 8682 8623 8550 -26 59 7 O ATOM 1867 CB ASN A 268 46.228 37.701 -3.787 1.00 66.99 C ANISOU 1867 CB ASN A 268 8499 8480 8472 1 16 -36 C ATOM 1868 CG ASN A 268 45.509 37.833 -5.128 1.00 67.44 C ANISOU 1868 CG ASN A 268 8589 8538 8494 -7 15 10 C ATOM 1869 OD1 ASN A 268 44.345 38.245 -5.199 1.00 67.19 O ANISOU 1869 OD1 ASN A 268 8619 8513 8397 33 -20 10 O ATOM 1870 ND2 ASN A 268 46.211 37.491 -6.200 1.00 67.62 N ANISOU 1870 ND2 ASN A 268 8719 8438 8535 -12 19 26 N ATOM 1871 N VAL A 269 44.769 39.931 -3.013 1.00 65.99 N ANISOU 1871 N VAL A 269 8375 8358 8337 -14 -24 -32 N ATOM 1872 CA VAL A 269 45.036 41.329 -2.620 1.00 64.91 C ANISOU 1872 CA VAL A 269 8190 8265 8205 3 -22 -3 C ATOM 1873 C VAL A 269 46.437 41.318 -1.958 1.00 64.75 C ANISOU 1873 C VAL A 269 8152 8257 8192 -18 11 -31 C ATOM 1874 O VAL A 269 47.403 40.824 -2.557 1.00 66.07 O ANISOU 1874 O VAL A 269 8185 8431 8484 30 29 -20 O ATOM 1875 CB VAL A 269 43.931 41.966 -1.698 1.00 65.18 C ANISOU 1875 CB VAL A 269 8214 8258 8293 23 -2 15 C ATOM 1876 CG1 VAL A 269 44.212 43.480 -1.470 1.00 65.31 C ANISOU 1876 CG1 VAL A 269 8303 8261 8250 0 5 5 C ATOM 1877 CG2 VAL A 269 42.542 41.758 -2.295 1.00 65.28 C ANISOU 1877 CG2 VAL A 269 8205 8347 8249 -20 -6 6 C ATOM 1878 N GLU A 270 46.547 41.844 -0.740 1.00 63.40 N ANISOU 1878 N GLU A 270 7987 8094 8007 -30 -34 -23 N ATOM 1879 CA GLU A 270 47.779 41.792 0.034 1.00 62.20 C ANISOU 1879 CA GLU A 270 7891 7907 7836 -17 55 4 C ATOM 1880 C GLU A 270 47.377 41.797 1.527 1.00 61.51 C ANISOU 1880 C GLU A 270 7814 7780 7776 -55 38 23 C ATOM 1881 O GLU A 270 47.869 42.615 2.324 1.00 63.16 O ANISOU 1881 O GLU A 270 8087 7951 7957 -60 -33 -23 O ATOM 1882 CB GLU A 270 48.694 42.993 -0.295 1.00 62.15 C ANISOU 1882 CB GLU A 270 7887 7898 7829 -31 52 12 C ATOM 1883 CG GLU A 270 48.437 43.687 -1.654 1.00 62.78 C ANISOU 1883 CG GLU A 270 7992 7957 7905 0 22 22 C ATOM 1884 CD GLU A 270 48.903 45.140 -1.691 1.00 63.69 C ANISOU 1884 CD GLU A 270 8087 7980 8131 4 55 18 C ATOM 1885 OE1 GLU A 270 49.298 45.683 -0.631 1.00 67.73 O ANISOU 1885 OE1 GLU A 270 8669 8653 8410 -3 -114 -79 O ATOM 1886 OE2 GLU A 270 48.854 45.748 -2.789 1.00 66.39 O ANISOU 1886 OE2 GLU A 270 8499 8446 8280 5 83 103 O ATOM 1887 N GLY A 271 46.466 40.901 1.903 1.00 59.67 N ANISOU 1887 N GLY A 271 7579 7556 7537 -2 36 23 N ATOM 1888 CA GLY A 271 46.009 40.824 3.297 1.00 58.65 C ANISOU 1888 CA GLY A 271 7401 7422 7460 31 22 8 C ATOM 1889 C GLY A 271 44.769 41.667 3.553 1.00 57.99 C ANISOU 1889 C GLY A 271 7342 7310 7379 30 56 44 C ATOM 1890 O GLY A 271 44.722 42.848 3.179 1.00 58.50 O ANISOU 1890 O GLY A 271 7430 7331 7463 46 106 66 O ATOM 1891 N LYS A 272 43.769 41.063 4.187 1.00 57.18 N ANISOU 1891 N LYS A 272 7242 7225 7259 14 25 32 N ATOM 1892 CA LYS A 272 42.454 41.678 4.313 1.00 57.16 C ANISOU 1892 CA LYS A 272 7253 7239 7224 -1 -9 24 C ATOM 1893 C LYS A 272 42.474 42.804 5.340 1.00 57.15 C ANISOU 1893 C LYS A 272 7269 7279 7166 12 -25 -15 C ATOM 1894 O LYS A 272 43.323 42.830 6.231 1.00 57.49 O ANISOU 1894 O LYS A 272 7311 7302 7229 17 -50 -17 O ATOM 1895 CB LYS A 272 41.409 40.631 4.705 1.00 56.48 C ANISOU 1895 CB LYS A 272 7152 7184 7121 -15 6 24 C ATOM 1896 CG LYS A 272 40.926 39.770 3.549 1.00 56.89 C ANISOU 1896 CG LYS A 272 7194 7275 7146 -46 1 2 C ATOM 1897 CD LYS A 272 40.037 38.638 4.038 1.00 57.15 C ANISOU 1897 CD LYS A 272 7321 7211 7180 -8 12 -1 C ATOM 1898 CE LYS A 272 40.800 37.689 4.948 1.00 57.61 C ANISOU 1898 CE LYS A 272 7352 7247 7288 54 4 -19 C ATOM 1899 NZ LYS A 272 39.953 36.551 5.400 1.00 58.03 N ANISOU 1899 NZ LYS A 272 7439 7300 7308 11 2 28 N ATOM 1900 N LYS A 273 41.526 43.728 5.219 1.00 57.41 N ANISOU 1900 N LYS A 273 7271 7340 7199 15 -29 -11 N ATOM 1901 CA LYS A 273 41.063 44.498 6.368 1.00 58.73 C ANISOU 1901 CA LYS A 273 7477 7433 7405 17 -5 10 C ATOM 1902 C LYS A 273 39.548 44.416 6.525 1.00 59.50 C ANISOU 1902 C LYS A 273 7537 7571 7498 12 -7 20 C ATOM 1903 O LYS A 273 38.824 44.200 5.554 1.00 59.20 O ANISOU 1903 O LYS A 273 7574 7569 7348 20 -15 11 O ATOM 1904 CB LYS A 273 41.503 45.959 6.248 1.00 58.72 C ANISOU 1904 CB LYS A 273 7480 7427 7402 -10 -9 38 C ATOM 1905 CG LYS A 273 42.932 46.214 6.698 1.00 58.82 C ANISOU 1905 CG LYS A 273 7501 7426 7423 -33 38 31 C ATOM 1906 CD LYS A 273 43.933 45.688 5.683 1.00 59.73 C ANISOU 1906 CD LYS A 273 7554 7599 7540 -29 22 44 C ATOM 1907 CE LYS A 273 45.229 46.481 5.723 1.00 60.23 C ANISOU 1907 CE LYS A 273 7522 7699 7660 -12 3 4 C ATOM 1908 NZ LYS A 273 46.394 45.664 5.285 1.00 62.22 N ANISOU 1908 NZ LYS A 273 7961 7728 7951 14 61 43 N ATOM 1909 N MET A 274 39.077 44.589 7.756 1.00 61.10 N ANISOU 1909 N MET A 274 7750 7767 7698 -1 38 24 N ATOM 1910 CA MET A 274 37.653 44.494 8.053 1.00 61.21 C ANISOU 1910 CA MET A 274 7749 7789 7718 6 51 12 C ATOM 1911 C MET A 274 37.008 45.875 8.106 1.00 63.12 C ANISOU 1911 C MET A 274 8056 7954 7971 13 38 14 C ATOM 1912 O MET A 274 36.245 46.249 7.215 1.00 64.75 O ANISOU 1912 O MET A 274 8342 8144 8115 9 25 40 O ATOM 1913 CB MET A 274 37.430 43.760 9.377 1.00 61.80 C ANISOU 1913 CB MET A 274 7884 7822 7772 10 61 -10 C ATOM 1914 CG MET A 274 36.237 42.818 9.372 1.00 62.39 C ANISOU 1914 CG MET A 274 7860 7920 7922 -25 91 -6 C ATOM 1915 SD MET A 274 34.783 43.539 8.587 1.00 67.39 S ANISOU 1915 SD MET A 274 8554 8720 8330 -79 -62 94 S ATOM 1916 CE MET A 274 33.702 42.113 8.500 1.00 63.76 C ANISOU 1916 CE MET A 274 8039 8156 8029 73 -28 31 C ATOM 1917 N PHE A 275 37.319 46.628 9.156 1.00 64.10 N ANISOU 1917 N PHE A 275 8144 8094 8115 -14 13 46 N ATOM 1918 CA PHE A 275 37.332 48.084 9.078 1.00 64.41 C ANISOU 1918 CA PHE A 275 8105 8202 8166 7 4 -4 C ATOM 1919 C PHE A 275 38.624 48.656 9.653 1.00 65.43 C ANISOU 1919 C PHE A 275 8225 8374 8260 18 -26 5 C ATOM 1920 O PHE A 275 38.919 49.840 9.484 1.00 66.08 O ANISOU 1920 O PHE A 275 8260 8501 8345 15 51 24 O ATOM 1921 CB PHE A 275 36.125 48.671 9.812 1.00 67.34 C ANISOU 1921 CB PHE A 275 8776 8377 8430 -234 313 -71 C ATOM 1922 CG PHE A 275 34.948 48.948 8.920 1.00 63.63 C ANISOU 1922 CG PHE A 275 7927 8083 8164 87 -136 4 C ATOM 1923 CD1 PHE A 275 34.456 47.966 8.076 1.00 65.08 C ANISOU 1923 CD1 PHE A 275 8259 8187 8278 -26 40 58 C ATOM 1924 CD2 PHE A 275 34.335 50.189 8.924 1.00 65.42 C ANISOU 1924 CD2 PHE A 275 8310 8223 8321 -76 -54 -109 C ATOM 1925 CE1 PHE A 275 33.374 48.217 7.254 1.00 64.95 C ANISOU 1925 CE1 PHE A 275 8050 8455 8170 76 -38 169 C ATOM 1926 CE2 PHE A 275 33.253 50.447 8.105 1.00 63.02 C ANISOU 1926 CE2 PHE A 275 7871 7956 8116 147 -125 34 C ATOM 1927 CZ PHE A 275 32.772 49.459 7.268 1.00 63.48 C ANISOU 1927 CZ PHE A 275 7934 8089 8093 103 -57 58 C ATOM 1928 N VAL A 276 39.390 47.809 10.332 1.00 20.00 N ATOM 1929 CA VAL A 276 40.815 48.050 10.525 1.00 20.00 C ATOM 1930 C VAL A 276 41.569 46.745 10.756 1.00 20.00 C ATOM 1931 O VAL A 276 41.735 46.306 11.894 1.00 20.00 O ATOM 1932 CB VAL A 276 41.071 48.997 11.712 1.00 20.00 C ATOM 1933 CG1 VAL A 276 41.845 50.225 11.256 1.00 20.00 C ATOM 1934 CG2 VAL A 276 39.759 49.399 12.367 1.00 20.00 C ATOM 1935 N GLU A 277 42.022 46.129 9.669 1.00 62.70 N ANISOU 1935 N GLU A 277 7986 7904 7930 30 10 6 N ATOM 1936 CA GLU A 277 42.586 44.786 9.728 1.00 60.43 C ANISOU 1936 CA GLU A 277 7709 7627 7624 -72 9 0 C ATOM 1937 C GLU A 277 41.489 43.730 9.808 1.00 59.30 C ANISOU 1937 C GLU A 277 7591 7483 7457 -28 15 -73 C ATOM 1938 O GLU A 277 40.305 44.057 9.895 1.00 60.55 O ANISOU 1938 O GLU A 277 7711 7684 7611 -14 47 -67 O ATOM 1939 CB GLU A 277 43.531 44.654 10.925 1.00 61.07 C ANISOU 1939 CB GLU A 277 7755 7759 7687 -58 -4 4 C ATOM 1940 CG GLU A 277 44.799 43.870 10.631 1.00 63.96 C ANISOU 1940 CG GLU A 277 8072 8066 8163 76 -16 6 C ATOM 1941 CD GLU A 277 45.891 44.732 10.028 1.00 70.25 C ANISOU 1941 CD GLU A 277 8913 8992 8783 -2 234 24 C ATOM 1942 OE1 GLU A 277 47.012 44.744 10.577 1.00 74.01 O ANISOU 1942 OE1 GLU A 277 9157 9504 9458 38 27 17 O ATOM 1943 OE2 GLU A 277 45.627 45.397 9.004 1.00 72.99 O ANISOU 1943 OE2 GLU A 277 9191 9394 9145 84 -132 -35 O ATOM 1944 N HIS A 278 41.890 42.463 9.778 1.00 56.39 N ANISOU 1944 N HIS A 278 7185 7127 7114 -24 29 -24 N ATOM 1945 CA HIS A 278 40.939 41.360 9.737 1.00 54.65 C ANISOU 1945 CA HIS A 278 6965 6980 6817 32 11 28 C ATOM 1946 C HIS A 278 41.434 40.173 10.557 1.00 53.24 C ANISOU 1946 C HIS A 278 6738 6862 6628 37 9 0 C ATOM 1947 O HIS A 278 42.530 39.661 10.327 1.00 53.78 O ANISOU 1947 O HIS A 278 6773 7015 6644 78 35 25 O ATOM 1948 CB HIS A 278 40.678 40.929 8.293 1.00 53.89 C ANISOU 1948 CB HIS A 278 6857 6870 6750 -3 22 17 C ATOM 1949 CG HIS A 278 39.501 40.017 8.137 1.00 54.17 C ANISOU 1949 CG HIS A 278 6922 6893 6764 32 -2 -7 C ATOM 1950 ND1 HIS A 278 39.557 38.672 8.435 1.00 52.80 N ANISOU 1950 ND1 HIS A 278 6676 6830 6553 38 -90 18 N ATOM 1951 CD2 HIS A 278 38.237 40.256 7.715 1.00 50.83 C ANISOU 1951 CD2 HIS A 278 6580 6429 6302 -5 149 -65 C ATOM 1952 CE1 HIS A 278 38.378 38.123 8.203 1.00 51.60 C ANISOU 1952 CE1 HIS A 278 6547 6558 6499 77 47 -9 C ATOM 1953 NE2 HIS A 278 37.559 39.062 7.765 1.00 50.13 N ANISOU 1953 NE2 HIS A 278 6281 6498 6268 35 179 49 N ATOM 1954 N LYS A 279 40.620 39.740 11.514 1.00 51.54 N ANISOU 1954 N LYS A 279 6512 6601 6468 25 -29 -8 N ATOM 1955 CA LYS A 279 41.091 38.888 12.588 1.00 50.04 C ANISOU 1955 CA LYS A 279 6325 6373 6313 5 -9 -62 C ATOM 1956 C LYS A 279 40.660 37.465 12.324 1.00 49.10 C ANISOU 1956 C LYS A 279 6185 6281 6187 27 -16 -50 C ATOM 1957 O LYS A 279 40.939 36.567 13.108 1.00 48.91 O ANISOU 1957 O LYS A 279 6122 6314 6147 79 -12 -31 O ATOM 1958 CB LYS A 279 40.519 39.354 13.925 1.00 49.57 C ANISOU 1958 CB LYS A 279 6330 6271 6232 7 -4 -48 C ATOM 1959 CG LYS A 279 41.129 40.623 14.471 1.00 48.26 C ANISOU 1959 CG LYS A 279 6150 6141 6044 2 -29 19 C ATOM 1960 CD LYS A 279 40.487 40.994 15.778 1.00 47.99 C ANISOU 1960 CD LYS A 279 6021 6099 6113 38 -53 26 C ATOM 1961 CE LYS A 279 41.240 42.095 16.462 1.00 45.90 C ANISOU 1961 CE LYS A 279 5839 5869 5732 127 -95 146 C ATOM 1962 NZ LYS A 279 40.548 43.379 16.364 1.00 42.18 N ANISOU 1962 NZ LYS A 279 5335 5455 5233 31 15 -175 N ATOM 1963 N GLY A 280 39.961 37.271 11.215 1.00 48.38 N ANISOU 1963 N GLY A 280 6131 6177 6073 36 20 -22 N ATOM 1964 CA GLY A 280 39.445 35.963 10.857 1.00 47.25 C ANISOU 1964 CA GLY A 280 5985 6050 5917 37 6 -9 C ATOM 1965 C GLY A 280 38.189 35.604 11.628 1.00 46.31 C ANISOU 1965 C GLY A 280 5940 5916 5738 43 -33 -28 C ATOM 1966 O GLY A 280 37.283 36.424 11.773 1.00 46.20 O ANISOU 1966 O GLY A 280 5935 5942 5675 100 -105 -3 O ATOM 1967 N SER A 281 38.137 34.372 12.125 1.00 45.18 N ANISOU 1967 N SER A 281 5778 5813 5575 66 -37 -57 N ATOM 1968 CA SER A 281 36.896 33.806 12.639 1.00 44.58 C ANISOU 1968 CA SER A 281 5725 5720 5493 49 -40 -69 C ATOM 1969 C SER A 281 36.766 34.029 14.142 1.00 43.97 C ANISOU 1969 C SER A 281 5591 5642 5473 64 -47 -85 C ATOM 1970 O SER A 281 37.691 33.750 14.904 1.00 43.93 O ANISOU 1970 O SER A 281 5685 5613 5391 146 -140 -142 O ATOM 1971 CB SER A 281 36.815 32.312 12.319 1.00 44.37 C ANISOU 1971 CB SER A 281 5793 5656 5410 74 -55 -77 C ATOM 1972 OG SER A 281 37.135 31.529 13.455 1.00 44.93 O ANISOU 1972 OG SER A 281 5990 5585 5494 124 -95 -172 O ATOM 1973 N LEU A 282 35.610 34.535 14.560 1.00 43.21 N ANISOU 1973 N LEU A 282 5446 5586 5385 39 -103 -59 N ATOM 1974 CA LEU A 282 35.313 34.701 15.966 1.00 42.25 C ANISOU 1974 CA LEU A 282 5347 5385 5319 37 -50 -24 C ATOM 1975 C LEU A 282 35.548 33.408 16.746 1.00 40.89 C ANISOU 1975 C LEU A 282 5145 5214 5175 68 -51 -91 C ATOM 1976 O LEU A 282 36.052 33.439 17.875 1.00 38.51 O ANISOU 1976 O LEU A 282 4663 5036 4933 213 -42 -251 O ATOM 1977 CB LEU A 282 33.862 35.152 16.107 1.00 42.58 C ANISOU 1977 CB LEU A 282 5379 5457 5340 42 -157 1 C ATOM 1978 CG LEU A 282 33.194 35.112 17.467 1.00 43.70 C ANISOU 1978 CG LEU A 282 5459 5645 5500 4 -5 -38 C ATOM 1979 CD1 LEU A 282 34.015 35.878 18.501 1.00 45.34 C ANISOU 1979 CD1 LEU A 282 5723 5830 5671 -21 -162 -68 C ATOM 1980 CD2 LEU A 282 31.796 35.698 17.346 1.00 43.17 C ANISOU 1980 CD2 LEU A 282 5457 5480 5465 30 -72 -11 C ATOM 1981 N GLU A 283 35.175 32.274 16.153 1.00 39.90 N ANISOU 1981 N GLU A 283 5083 5099 4978 20 -108 -143 N ATOM 1982 CA GLU A 283 35.349 30.994 16.825 1.00 39.64 C ANISOU 1982 CA GLU A 283 5018 5106 4937 15 -67 -83 C ATOM 1983 C GLU A 283 36.820 30.710 17.173 1.00 38.18 C ANISOU 1983 C GLU A 283 4938 4829 4739 13 -25 -94 C ATOM 1984 O GLU A 283 37.114 30.172 18.252 1.00 36.94 O ANISOU 1984 O GLU A 283 4837 4707 4489 108 -229 -209 O ATOM 1985 CB GLU A 283 34.778 29.839 15.997 1.00 40.62 C ANISOU 1985 CB GLU A 283 5169 5140 5121 19 -94 -41 C ATOM 1986 CG GLU A 283 35.008 28.472 16.647 1.00 40.07 C ANISOU 1986 CG GLU A 283 5173 5068 4984 -19 -111 -63 C ATOM 1987 CD GLU A 283 34.147 27.380 16.052 1.00 43.62 C ANISOU 1987 CD GLU A 283 5530 5503 5539 -128 -104 -53 C ATOM 1988 OE1 GLU A 283 34.679 26.608 15.204 1.00 49.35 O ANISOU 1988 OE1 GLU A 283 6156 6304 6289 121 -26 -355 O ATOM 1989 OE2 GLU A 283 32.943 27.300 16.425 1.00 47.67 O ANISOU 1989 OE2 GLU A 283 5672 6249 6191 -91 85 -162 O ATOM 1990 N ASP A 284 37.740 31.049 16.269 1.00 37.05 N ANISOU 1990 N ASP A 284 4786 4701 4589 -5 -91 -70 N ATOM 1991 CA ASP A 284 39.165 30.821 16.539 1.00 36.32 C ANISOU 1991 CA ASP A 284 4708 4574 4515 31 -78 -99 C ATOM 1992 C ASP A 284 39.664 31.744 17.647 1.00 34.69 C ANISOU 1992 C ASP A 284 4503 4341 4334 92 -79 -122 C ATOM 1993 O ASP A 284 40.442 31.324 18.491 1.00 34.08 O ANISOU 1993 O ASP A 284 4561 4261 4124 108 -114 -336 O ATOM 1994 CB ASP A 284 40.023 30.989 15.291 1.00 36.35 C ANISOU 1994 CB ASP A 284 4686 4618 4505 56 -29 -29 C ATOM 1995 CG ASP A 284 39.731 29.930 14.226 1.00 40.04 C ANISOU 1995 CG ASP A 284 5154 5071 4988 -41 -1 -107 C ATOM 1996 OD1 ASP A 284 39.157 28.847 14.549 1.00 38.63 O ANISOU 1996 OD1 ASP A 284 5155 4881 4643 -15 73 -253 O ATOM 1997 OD2 ASP A 284 40.083 30.205 13.047 1.00 43.20 O ANISOU 1997 OD2 ASP A 284 5555 5893 4963 -74 -16 -131 O ATOM 1998 N THR A 285 39.185 32.981 17.652 1.00 33.63 N ANISOU 1998 N THR A 285 4331 4256 4190 60 -100 -39 N ATOM 1999 CA THR A 285 39.521 33.930 18.701 1.00 32.47 C ANISOU 1999 CA THR A 285 4160 4135 4039 55 -75 10 C ATOM 2000 C THR A 285 39.090 33.445 20.085 1.00 30.65 C ANISOU 2000 C THR A 285 3882 3872 3890 87 -16 -98 C ATOM 2001 O THR A 285 39.863 33.560 21.040 1.00 30.91 O ANISOU 2001 O THR A 285 3874 3969 3902 178 -137 -165 O ATOM 2002 CB THR A 285 38.938 35.319 18.397 1.00 31.84 C ANISOU 2002 CB THR A 285 4049 4147 3902 63 -8 41 C ATOM 2003 OG1 THR A 285 39.637 35.870 17.269 1.00 30.95 O ANISOU 2003 OG1 THR A 285 3994 4543 3221 -62 -93 15 O ATOM 2004 CG2 THR A 285 39.083 36.271 19.589 1.00 32.99 C ANISOU 2004 CG2 THR A 285 4142 4240 4149 45 -119 -10 C ATOM 2005 N LEU A 286 37.883 32.892 20.190 1.00 29.86 N ANISOU 2005 N LEU A 286 3811 3787 3746 39 -134 -160 N ATOM 2006 CA LEU A 286 37.359 32.388 21.470 1.00 30.41 C ANISOU 2006 CA LEU A 286 3798 3876 3879 20 -119 -44 C ATOM 2007 C LEU A 286 38.104 31.141 21.977 1.00 29.35 C ANISOU 2007 C LEU A 286 3643 3717 3791 76 -65 -76 C ATOM 2008 O LEU A 286 38.306 30.977 23.195 1.00 28.94 O ANISOU 2008 O LEU A 286 3612 3386 3996 178 -283 6 O ATOM 2009 CB LEU A 286 35.848 32.083 21.379 1.00 30.99 C ANISOU 2009 CB LEU A 286 3851 3965 3959 58 -127 -51 C ATOM 2010 CG LEU A 286 34.874 33.258 21.355 1.00 29.35 C ANISOU 2010 CG LEU A 286 3524 3879 3746 53 24 -92 C ATOM 2011 CD1 LEU A 286 33.470 32.819 20.810 1.00 31.60 C ANISOU 2011 CD1 LEU A 286 3856 4102 4046 11 -72 -287 C ATOM 2012 CD2 LEU A 286 34.732 33.909 22.734 1.00 28.41 C ANISOU 2012 CD2 LEU A 286 3256 3781 3757 275 -298 -55 C ATOM 2013 N ILE A 287 38.488 30.267 21.050 1.00 30.63 N ANISOU 2013 N ILE A 287 3807 3844 3987 40 -202 -74 N ATOM 2014 CA ILE A 287 39.330 29.114 21.363 1.00 30.69 C ANISOU 2014 CA ILE A 287 3837 3863 3960 31 -95 -143 C ATOM 2015 C ILE A 287 40.703 29.530 21.912 1.00 29.25 C ANISOU 2015 C ILE A 287 3703 3649 3758 89 -80 -196 C ATOM 2016 O ILE A 287 41.153 28.994 22.914 1.00 25.91 O ANISOU 2016 O ILE A 287 3398 3006 3438 146 -237 -644 O ATOM 2017 CB ILE A 287 39.516 28.223 20.131 1.00 31.52 C ANISOU 2017 CB ILE A 287 3872 4006 4096 61 -37 -132 C ATOM 2018 CG1 ILE A 287 38.214 27.477 19.854 1.00 33.67 C ANISOU 2018 CG1 ILE A 287 4219 4306 4265 55 -117 -189 C ATOM 2019 CG2 ILE A 287 40.640 27.242 20.367 1.00 31.48 C ANISOU 2019 CG2 ILE A 287 4021 3892 4046 151 -20 -59 C ATOM 2020 CD1 ILE A 287 38.215 26.701 18.569 1.00 33.27 C ANISOU 2020 CD1 ILE A 287 4298 4165 4175 29 -178 -155 C ATOM 2021 N GLU A 288 41.339 30.480 21.239 1.00 29.93 N ANISOU 2021 N GLU A 288 3791 3734 3844 46 -45 -155 N ATOM 2022 CA GLU A 288 42.625 31.013 21.673 1.00 30.23 C ANISOU 2022 CA GLU A 288 3836 3848 3801 82 -53 -133 C ATOM 2023 C GLU A 288 42.492 31.721 23.029 1.00 28.64 C ANISOU 2023 C GLU A 288 3579 3700 3600 162 -64 -51 C ATOM 2024 O GLU A 288 43.311 31.518 23.935 1.00 27.80 O ANISOU 2024 O GLU A 288 3426 3544 3592 371 -109 -280 O ATOM 2025 CB GLU A 288 43.141 31.986 20.619 1.00 30.43 C ANISOU 2025 CB GLU A 288 3788 3985 3789 62 -62 -83 C ATOM 2026 CG GLU A 288 44.507 32.514 20.883 1.00 32.94 C ANISOU 2026 CG GLU A 288 4138 4167 4208 -97 -46 -102 C ATOM 2027 CD GLU A 288 44.951 33.491 19.818 1.00 36.67 C ANISOU 2027 CD GLU A 288 4825 4602 4506 -177 12 70 C ATOM 2028 OE1 GLU A 288 44.328 34.578 19.691 1.00 45.11 O ANISOU 2028 OE1 GLU A 288 5738 5493 5908 326 114 -146 O ATOM 2029 OE2 GLU A 288 45.925 33.164 19.092 1.00 48.30 O ANISOU 2029 OE2 GLU A 288 5647 6308 6396 192 325 -4 O ATOM 2030 N MET A 289 41.449 32.533 23.192 1.00 26.24 N ANISOU 2030 N MET A 289 3280 3388 3301 140 -123 -24 N ATOM 2031 CA MET A 289 41.163 33.099 24.514 1.00 27.37 C ANISOU 2031 CA MET A 289 3378 3499 3522 77 -78 -107 C ATOM 2032 C MET A 289 41.072 32.030 25.594 1.00 25.69 C ANISOU 2032 C MET A 289 3143 3217 3397 154 -88 -175 C ATOM 2033 O MET A 289 41.570 32.200 26.705 1.00 25.13 O ANISOU 2033 O MET A 289 3114 3062 3370 137 -150 -499 O ATOM 2034 CB MET A 289 39.871 33.898 24.515 1.00 26.32 C ANISOU 2034 CB MET A 289 3311 3428 3260 110 -109 -149 C ATOM 2035 CG MET A 289 40.043 35.320 24.069 1.00 30.00 C ANISOU 2035 CG MET A 289 3551 3871 3975 -42 -44 -70 C ATOM 2036 SD MET A 289 38.461 36.191 24.113 1.00 31.02 S ANISOU 2036 SD MET A 289 3776 3930 4081 344 -196 -189 S ATOM 2037 CE MET A 289 38.961 37.798 23.544 1.00 30.23 C ANISOU 2037 CE MET A 289 3690 3802 3993 188 78 -25 C ATOM 2038 N GLU A 290 40.439 30.910 25.281 1.00 26.14 N ANISOU 2038 N GLU A 290 3210 3301 3420 24 -154 -209 N ATOM 2039 CA GLU A 290 40.300 29.868 26.275 1.00 26.37 C ANISOU 2039 CA GLU A 290 3270 3343 3405 19 -110 -106 C ATOM 2040 C GLU A 290 41.638 29.201 26.563 1.00 25.41 C ANISOU 2040 C GLU A 290 3220 3091 3341 -101 -108 -123 C ATOM 2041 O GLU A 290 41.958 28.932 27.725 1.00 24.57 O ANISOU 2041 O GLU A 290 3046 2796 3493 213 -351 140 O ATOM 2042 CB GLU A 290 39.288 28.819 25.838 1.00 26.31 C ANISOU 2042 CB GLU A 290 3297 3382 3315 -8 -32 -178 C ATOM 2043 CG GLU A 290 39.087 27.733 26.876 1.00 27.01 C ANISOU 2043 CG GLU A 290 3415 3385 3462 -61 -247 -96 C ATOM 2044 CD GLU A 290 37.948 26.790 26.538 1.00 31.10 C ANISOU 2044 CD GLU A 290 3893 3806 4115 -186 -106 -40 C ATOM 2045 OE1 GLU A 290 37.397 26.888 25.399 1.00 33.95 O ANISOU 2045 OE1 GLU A 290 4281 4423 4194 -524 -413 -444 O ATOM 2046 OE2 GLU A 290 37.628 25.954 27.420 1.00 35.28 O ANISOU 2046 OE2 GLU A 290 4760 4042 4603 -306 50 55 O ATOM 2047 N GLN A 291 42.415 28.953 25.522 1.00 25.13 N ANISOU 2047 N GLN A 291 3092 3138 3318 -91 -126 -282 N ATOM 2048 CA GLN A 291 43.739 28.367 25.700 1.00 26.35 C ANISOU 2048 CA GLN A 291 3275 3317 3419 -19 -150 -132 C ATOM 2049 C GLN A 291 44.673 29.259 26.509 1.00 25.54 C ANISOU 2049 C GLN A 291 3296 3177 3227 -36 -128 -205 C ATOM 2050 O GLN A 291 45.395 28.777 27.400 1.00 25.85 O ANISOU 2050 O GLN A 291 3367 3187 3266 -1 -157 -272 O ATOM 2051 CB GLN A 291 44.385 28.091 24.355 1.00 25.47 C ANISOU 2051 CB GLN A 291 3204 3347 3123 -34 -186 -131 C ATOM 2052 CG GLN A 291 43.743 26.884 23.671 1.00 29.97 C ANISOU 2052 CG GLN A 291 3773 3701 3912 -13 -101 -183 C ATOM 2053 CD GLN A 291 44.093 26.786 22.213 1.00 30.39 C ANISOU 2053 CD GLN A 291 3805 3998 3743 64 -157 -166 C ATOM 2054 OE1 GLN A 291 44.659 27.720 21.615 1.00 38.66 O ANISOU 2054 OE1 GLN A 291 4830 4877 4980 -211 53 -112 O ATOM 2055 NE2 GLN A 291 43.739 25.653 21.608 1.00 35.04 N ANISOU 2055 NE2 GLN A 291 4450 4191 4672 119 -104 -321 N ATOM 2056 N ASP A 292 44.669 30.544 26.172 1.00 24.44 N ANISOU 2056 N ASP A 292 3052 3175 3056 -20 -144 -169 N ATOM 2057 CA ASP A 292 45.491 31.540 26.888 1.00 23.74 C ANISOU 2057 CA ASP A 292 2942 3013 3064 -2 -67 -185 C ATOM 2058 C ASP A 292 45.106 31.625 28.339 1.00 21.96 C ANISOU 2058 C ASP A 292 2699 2704 2937 25 3 -289 C ATOM 2059 O ASP A 292 45.962 31.660 29.233 1.00 22.68 O ANISOU 2059 O ASP A 292 2628 2858 3129 157 -19 -494 O ATOM 2060 CB ASP A 292 45.402 32.906 26.212 1.00 23.44 C ANISOU 2060 CB ASP A 292 2950 2984 2973 -8 -18 -194 C ATOM 2061 CG ASP A 292 46.039 32.909 24.856 1.00 27.46 C ANISOU 2061 CG ASP A 292 3527 3538 3364 -10 17 -127 C ATOM 2062 OD1 ASP A 292 46.766 31.930 24.561 1.00 30.68 O ANISOU 2062 OD1 ASP A 292 3847 3714 4093 156 -200 -356 O ATOM 2063 OD2 ASP A 292 45.843 33.881 24.104 1.00 28.28 O ANISOU 2063 OD2 ASP A 292 3959 3658 3125 -86 -295 -142 O ATOM 2064 N LEU A 293 43.813 31.606 28.595 1.00 22.51 N ANISOU 2064 N LEU A 293 2773 2786 2993 -130 -66 -285 N ATOM 2065 CA LEU A 293 43.320 31.589 29.970 1.00 22.23 C ANISOU 2065 CA LEU A 293 2809 2816 2819 -1 -66 -189 C ATOM 2066 C LEU A 293 43.659 30.307 30.779 1.00 22.56 C ANISOU 2066 C LEU A 293 2814 2913 2844 -55 -62 -198 C ATOM 2067 O LEU A 293 43.966 30.373 31.974 1.00 19.56 O ANISOU 2067 O LEU A 293 2548 2611 2271 -117 158 -85 O ATOM 2068 CB LEU A 293 41.823 31.864 29.949 1.00 22.09 C ANISOU 2068 CB LEU A 293 2698 3159 2537 -138 -142 -117 C ATOM 2069 CG LEU A 293 41.167 32.394 31.208 1.00 23.41 C ANISOU 2069 CG LEU A 293 2702 2984 3209 47 20 -265 C ATOM 2070 CD1 LEU A 293 41.922 33.533 31.929 1.00 25.31 C ANISOU 2070 CD1 LEU A 293 2954 3280 3380 51 43 -77 C ATOM 2071 CD2 LEU A 293 39.726 32.832 30.788 1.00 24.32 C ANISOU 2071 CD2 LEU A 293 3000 2940 3300 191 -230 -153 C ATOM 2072 N GLN A 294 43.659 29.151 30.122 1.00 22.89 N ANISOU 2072 N GLN A 294 2763 2805 3127 -29 -114 -188 N ATOM 2073 CA GLN A 294 44.170 27.905 30.727 1.00 21.46 C ANISOU 2073 CA GLN A 294 2668 2735 2747 -24 -53 -83 C ATOM 2074 C GLN A 294 45.653 28.023 31.091 1.00 21.30 C ANISOU 2074 C GLN A 294 2713 2692 2687 82 -54 -46 C ATOM 2075 O GLN A 294 46.063 27.545 32.143 1.00 20.11 O ANISOU 2075 O GLN A 294 2650 2546 2442 144 -204 -221 O ATOM 2076 CB GLN A 294 43.966 26.704 29.770 1.00 20.14 C ANISOU 2076 CB GLN A 294 2501 2606 2544 123 159 -199 C ATOM 2077 CG GLN A 294 42.508 26.319 29.603 1.00 21.59 C ANISOU 2077 CG GLN A 294 2809 2681 2711 -123 15 -247 C ATOM 2078 CD GLN A 294 42.288 25.205 28.627 1.00 22.83 C ANISOU 2078 CD GLN A 294 2932 2802 2939 -84 19 -111 C ATOM 2079 OE1 GLN A 294 42.862 25.203 27.526 1.00 27.13 O ANISOU 2079 OE1 GLN A 294 3755 3520 3030 -1 -109 -477 O ATOM 2080 NE2 GLN A 294 41.446 24.240 29.016 1.00 26.75 N ANISOU 2080 NE2 GLN A 294 2882 3256 4022 -286 -97 -444 N ATOM 2081 N SER A 295 46.444 28.645 30.216 1.00 21.07 N ANISOU 2081 N SER A 295 2549 2594 2862 109 85 -197 N ATOM 2082 CA SER A 295 47.844 28.933 30.537 1.00 21.76 C ANISOU 2082 CA SER A 295 2624 2703 2940 71 -21 -29 C ATOM 2083 C SER A 295 47.998 29.805 31.762 1.00 21.26 C ANISOU 2083 C SER A 295 2523 2552 3001 94 -24 -24 C ATOM 2084 O SER A 295 48.841 29.531 32.620 1.00 21.41 O ANISOU 2084 O SER A 295 2381 2386 3367 258 -231 -68 O ATOM 2085 CB SER A 295 48.556 29.600 29.371 1.00 22.72 C ANISOU 2085 CB SER A 295 2856 2869 2907 154 4 7 C ATOM 2086 OG SER A 295 48.598 28.754 28.258 1.00 26.61 O ANISOU 2086 OG SER A 295 3533 2880 3697 54 -200 -323 O ATOM 2087 N SER A 296 47.162 30.837 31.867 1.00 22.01 N ANISOU 2087 N SER A 296 2672 2530 3160 64 -142 88 N ATOM 2088 CA SER A 296 47.100 31.698 33.048 1.00 19.48 C ANISOU 2088 CA SER A 296 2401 2377 2623 57 -42 107 C ATOM 2089 C SER A 296 46.828 30.910 34.298 1.00 18.67 C ANISOU 2089 C SER A 296 2304 2316 2472 58 -60 -5 C ATOM 2090 O SER A 296 47.528 31.079 35.244 1.00 16.31 O ANISOU 2090 O SER A 296 2256 2073 1868 -17 -153 78 O ATOM 2091 CB SER A 296 46.000 32.798 32.919 1.00 19.07 C ANISOU 2091 CB SER A 296 2290 2319 2637 23 -60 15 C ATOM 2092 OG SER A 296 46.325 33.750 31.948 1.00 18.35 O ANISOU 2092 OG SER A 296 2146 2280 2543 151 -85 28 O ATOM 2093 N ILE A 297 45.843 30.014 34.272 1.00 19.29 N ANISOU 2093 N ILE A 297 2256 2477 2594 73 13 48 N ATOM 2094 CA ILE A 297 45.539 29.146 35.434 1.00 19.28 C ANISOU 2094 CA ILE A 297 2348 2395 2581 -17 15 46 C ATOM 2095 C ILE A 297 46.734 28.238 35.749 1.00 17.71 C ANISOU 2095 C ILE A 297 2197 2101 2428 -82 26 68 C ATOM 2096 O ILE A 297 47.056 28.029 36.912 1.00 18.70 O ANISOU 2096 O ILE A 297 2195 2026 2882 -193 -137 -62 O ATOM 2097 CB ILE A 297 44.213 28.300 35.216 1.00 18.94 C ANISOU 2097 CB ILE A 297 2272 2612 2312 23 -79 36 C ATOM 2098 CG1 ILE A 297 43.018 29.252 35.046 1.00 20.54 C ANISOU 2098 CG1 ILE A 297 2517 2624 2660 -14 -79 -99 C ATOM 2099 CG2 ILE A 297 43.964 27.321 36.393 1.00 19.56 C ANISOU 2099 CG2 ILE A 297 2218 2360 2853 44 -6 1 C ATOM 2100 CD1 ILE A 297 41.771 28.600 34.528 1.00 21.96 C ANISOU 2100 CD1 ILE A 297 2520 2648 3175 -101 99 -73 C ATOM 2101 N SER A 298 47.404 27.724 34.719 1.00 17.83 N ANISOU 2101 N SER A 298 2286 2060 2427 -17 -9 46 N ATOM 2102 CA ASER A 298 48.605 26.910 34.930 0.50 19.28 C ANISOU 2102 CA ASER A 298 2413 2373 2537 22 -1 61 C ATOM 2103 C SER A 298 49.657 27.692 35.716 1.00 19.05 C ANISOU 2103 C SER A 298 2390 2306 2542 33 2 17 C ATOM 2104 O SER A 298 50.171 27.225 36.732 1.00 18.79 O ANISOU 2104 O SER A 298 2776 1954 2408 109 129 123 O ATOM 2105 CB ASER A 298 49.178 26.443 33.593 0.50 19.63 C ANISOU 2105 CB ASER A 298 2560 2274 2622 129 -55 -97 C ATOM 2106 OG ASER A 298 48.192 25.706 32.895 0.50 24.37 O ANISOU 2106 OG ASER A 298 2891 3020 3349 -95 -163 -81 O ATOM 2107 N TYR A 299 49.991 28.872 35.217 1.00 20.12 N ANISOU 2107 N TYR A 299 2411 2294 2938 82 -129 44 N ATOM 2108 CA TYR A 299 50.935 29.760 35.902 1.00 19.78 C ANISOU 2108 CA TYR A 299 2409 2453 2652 -21 -25 42 C ATOM 2109 C TYR A 299 50.498 30.176 37.285 1.00 19.03 C ANISOU 2109 C TYR A 299 2492 2226 2512 -159 -103 272 C ATOM 2110 O TYR A 299 51.349 30.417 38.097 1.00 19.33 O ANISOU 2110 O TYR A 299 2363 2576 2404 -35 -268 476 O ATOM 2111 CB TYR A 299 51.198 31.033 35.072 1.00 21.88 C ANISOU 2111 CB TYR A 299 2750 2646 2917 49 2 127 C ATOM 2112 CG TYR A 299 52.187 30.843 33.940 1.00 19.99 C ANISOU 2112 CG TYR A 299 2540 2270 2784 190 -14 104 C ATOM 2113 CD1 TYR A 299 53.524 30.566 34.218 1.00 22.41 C ANISOU 2113 CD1 TYR A 299 2538 2628 3345 49 29 -159 C ATOM 2114 CD2 TYR A 299 51.816 30.967 32.628 1.00 24.48 C ANISOU 2114 CD2 TYR A 299 2855 3333 3111 146 22 -68 C ATOM 2115 CE1 TYR A 299 54.429 30.374 33.224 1.00 20.69 C ANISOU 2115 CE1 TYR A 299 2678 2808 2374 -215 -80 213 C ATOM 2116 CE2 TYR A 299 52.752 30.780 31.586 1.00 24.02 C ANISOU 2116 CE2 TYR A 299 2921 3342 2862 -52 154 352 C ATOM 2117 CZ TYR A 299 54.060 30.481 31.908 1.00 21.40 C ANISOU 2117 CZ TYR A 299 2729 2679 2722 -41 4 166 C ATOM 2118 OH TYR A 299 55.072 30.290 30.972 1.00 25.97 O ANISOU 2118 OH TYR A 299 3323 3660 2883 181 141 279 O ATOM 2119 N ALA A 300 49.187 30.299 37.528 1.00 18.42 N ANISOU 2119 N ALA A 300 2341 2325 2332 79 156 179 N ATOM 2120 CA ALA A 300 48.660 30.657 38.866 1.00 20.74 C ANISOU 2120 CA ALA A 300 2592 2634 2652 36 -51 32 C ATOM 2121 C ALA A 300 48.770 29.531 39.889 1.00 21.11 C ANISOU 2121 C ALA A 300 2598 2650 2771 43 -2 56 C ATOM 2122 O ALA A 300 48.435 29.736 41.038 1.00 21.08 O ANISOU 2122 O ALA A 300 2633 2623 2753 302 -129 -9 O ATOM 2123 CB ALA A 300 47.210 31.120 38.782 1.00 20.31 C ANISOU 2123 CB ALA A 300 2596 2533 2586 -23 95 54 C ATOM 2124 N GLY A 301 49.220 28.346 39.476 1.00 22.32 N ANISOU 2124 N GLY A 301 2664 2722 3094 79 -6 19 N ATOM 2125 CA GLY A 301 49.379 27.226 40.424 1.00 22.12 C ANISOU 2125 CA GLY A 301 2819 2743 2840 41 -10 -10 C ATOM 2126 C GLY A 301 48.074 26.545 40.802 1.00 22.69 C ANISOU 2126 C GLY A 301 3003 2732 2886 34 40 -33 C ATOM 2127 O GLY A 301 47.966 25.931 41.867 1.00 24.55 O ANISOU 2127 O GLY A 301 3233 2944 3151 0 149 -86 O ATOM 2128 N GLY A 302 47.081 26.638 39.920 1.00 22.86 N ANISOU 2128 N GLY A 302 2907 2732 3043 -38 63 1 N ATOM 2129 CA GLY A 302 45.771 26.045 40.156 1.00 23.55 C ANISOU 2129 CA GLY A 302 2984 2975 2987 -1 43 11 C ATOM 2130 C GLY A 302 45.259 25.219 39.011 1.00 23.53 C ANISOU 2130 C GLY A 302 2860 2942 3137 -86 109 -71 C ATOM 2131 O GLY A 302 45.968 24.939 38.062 1.00 19.49 O ANISOU 2131 O GLY A 302 2594 2695 2116 -396 203 8 O ATOM 2132 N THR A 303 44.005 24.804 39.128 1.00 25.25 N ANISOU 2132 N THR A 303 2961 3057 3575 6 149 51 N ATOM 2133 CA THR A 303 43.334 24.107 38.048 1.00 25.08 C ANISOU 2133 CA THR A 303 3119 3097 3311 1 66 56 C ATOM 2134 C THR A 303 42.030 24.779 37.620 1.00 26.20 C ANISOU 2134 C THR A 303 3199 3324 3430 -76 109 -45 C ATOM 2135 O THR A 303 41.375 24.309 36.683 1.00 27.18 O ANISOU 2135 O THR A 303 3138 3585 3604 -227 -88 -358 O ATOM 2136 CB THR A 303 42.990 22.669 38.501 1.00 26.59 C ANISOU 2136 CB THR A 303 3365 3216 3522 95 90 67 C ATOM 2137 OG1 THR A 303 41.991 22.737 39.526 1.00 24.22 O ANISOU 2137 OG1 THR A 303 3226 2527 3448 -329 240 751 O ATOM 2138 CG2 THR A 303 44.248 21.986 39.087 1.00 28.08 C ANISOU 2138 CG2 THR A 303 3325 3385 3959 -30 -2 94 C ATOM 2139 N LYS A 304 41.626 25.857 38.305 1.00 26.89 N ANISOU 2139 N LYS A 304 3185 3263 3766 -23 40 20 N ATOM 2140 CA LYS A 304 40.395 26.541 37.931 1.00 26.26 C ANISOU 2140 CA LYS A 304 3218 3152 3606 39 -19 83 C ATOM 2141 C LYS A 304 40.553 28.060 38.026 1.00 25.29 C ANISOU 2141 C LYS A 304 3019 3090 3499 84 -80 -25 C ATOM 2142 O LYS A 304 41.550 28.561 38.534 1.00 22.89 O ANISOU 2142 O LYS A 304 2612 2713 3371 74 -52 -81 O ATOM 2143 CB LYS A 304 39.226 26.028 38.770 1.00 27.80 C ANISOU 2143 CB LYS A 304 3242 3426 3891 60 -123 -17 C ATOM 2144 CG LYS A 304 39.362 26.232 40.240 1.00 30.47 C ANISOU 2144 CG LYS A 304 3833 3964 3777 33 161 241 C ATOM 2145 CD LYS A 304 38.404 25.290 41.017 1.00 30.87 C ANISOU 2145 CD LYS A 304 3841 3856 4030 -75 149 204 C ATOM 2146 CE LYS A 304 38.159 25.784 42.430 1.00 37.15 C ANISOU 2146 CE LYS A 304 4815 4838 4462 77 52 -95 C ATOM 2147 NZ LYS A 304 39.231 25.442 43.423 1.00 43.32 N ANISOU 2147 NZ LYS A 304 5106 5835 5516 44 -260 136 N ATOM 2148 N LEU A 305 39.563 28.769 37.490 1.00 24.64 N ANISOU 2148 N LEU A 305 3010 3000 3352 64 -11 149 N ATOM 2149 CA LEU A 305 39.637 30.208 37.308 1.00 23.68 C ANISOU 2149 CA LEU A 305 2892 2932 3172 82 -23 72 C ATOM 2150 C LEU A 305 39.944 30.975 38.582 1.00 21.72 C ANISOU 2150 C LEU A 305 2685 2703 2864 117 -67 261 C ATOM 2151 O LEU A 305 40.768 31.909 38.597 1.00 21.30 O ANISOU 2151 O LEU A 305 2578 2788 2725 20 82 336 O ATOM 2152 CB LEU A 305 38.309 30.682 36.695 1.00 24.22 C ANISOU 2152 CB LEU A 305 2920 2963 3318 35 -83 1 C ATOM 2153 CG LEU A 305 38.325 32.060 36.074 1.00 23.60 C ANISOU 2153 CG LEU A 305 2969 2994 3001 91 -75 58 C ATOM 2154 CD1 LEU A 305 39.213 32.107 34.841 1.00 22.75 C ANISOU 2154 CD1 LEU A 305 2807 2781 3055 34 -122 190 C ATOM 2155 CD2 LEU A 305 36.872 32.458 35.792 1.00 26.16 C ANISOU 2155 CD2 LEU A 305 3239 3146 3553 105 -109 239 C ATOM 2156 N ASP A 306 39.319 30.567 39.675 1.00 21.46 N ANISOU 2156 N ASP A 306 2599 2530 3023 -8 44 108 N ATOM 2157 CA ASP A 306 39.515 31.258 40.941 1.00 22.54 C ANISOU 2157 CA ASP A 306 2827 2819 2919 15 31 91 C ATOM 2158 C ASP A 306 40.940 31.228 41.462 1.00 21.43 C ANISOU 2158 C ASP A 306 2724 2657 2760 -64 168 104 C ATOM 2159 O ASP A 306 41.313 32.051 42.320 1.00 21.92 O ANISOU 2159 O ASP A 306 2823 2559 2944 -97 173 41 O ATOM 2160 CB ASP A 306 38.524 30.750 41.992 1.00 23.19 C ANISOU 2160 CB ASP A 306 2963 2922 2927 -41 -36 101 C ATOM 2161 CG ASP A 306 37.075 31.194 41.685 1.00 30.56 C ANISOU 2161 CG ASP A 306 3481 4018 4111 99 5 104 C ATOM 2162 OD1 ASP A 306 36.873 32.114 40.845 1.00 31.89 O ANISOU 2162 OD1 ASP A 306 3789 3712 4612 158 -89 153 O ATOM 2163 OD2 ASP A 306 36.144 30.601 42.256 1.00 33.14 O ANISOU 2163 OD2 ASP A 306 4359 3804 4428 -176 256 157 O ATOM 2164 N SER A 307 41.757 30.304 40.963 1.00 20.91 N ANISOU 2164 N SER A 307 2806 2361 2775 -136 44 92 N ATOM 2165 CA SER A 307 43.167 30.294 41.356 1.00 20.34 C ANISOU 2165 CA SER A 307 2672 2513 2543 -21 -18 121 C ATOM 2166 C SER A 307 43.876 31.613 40.997 1.00 19.12 C ANISOU 2166 C SER A 307 2543 2385 2338 -34 -20 77 C ATOM 2167 O SER A 307 44.821 31.999 41.651 1.00 18.72 O ANISOU 2167 O SER A 307 2896 2387 1830 23 172 31 O ATOM 2168 CB SER A 307 43.907 29.105 40.746 1.00 19.31 C ANISOU 2168 CB SER A 307 2633 2578 2127 92 -132 54 C ATOM 2169 OG SER A 307 44.003 29.196 39.328 1.00 22.80 O ANISOU 2169 OG SER A 307 2881 3406 2373 -119 300 65 O ATOM 2170 N ILE A 308 43.446 32.262 39.920 1.00 19.73 N ANISOU 2170 N ILE A 308 2689 2422 2386 -100 -46 184 N ATOM 2171 CA ILE A 308 44.035 33.551 39.490 1.00 20.10 C ANISOU 2171 CA ILE A 308 2626 2461 2548 -86 -2 141 C ATOM 2172 C ILE A 308 43.848 34.630 40.584 1.00 20.56 C ANISOU 2172 C ILE A 308 2547 2481 2781 -43 23 167 C ATOM 2173 O ILE A 308 44.699 35.504 40.756 1.00 19.88 O ANISOU 2173 O ILE A 308 2343 2487 2721 -95 69 312 O ATOM 2174 CB ILE A 308 43.478 33.971 38.042 1.00 18.98 C ANISOU 2174 CB ILE A 308 2466 2258 2487 -106 131 170 C ATOM 2175 CG1 ILE A 308 43.833 32.905 37.017 1.00 19.78 C ANISOU 2175 CG1 ILE A 308 2656 2221 2637 -215 -16 193 C ATOM 2176 CG2 ILE A 308 44.041 35.326 37.552 1.00 19.59 C ANISOU 2176 CG2 ILE A 308 2742 2432 2268 -79 -152 135 C ATOM 2177 CD1 ILE A 308 43.163 33.041 35.692 1.00 21.32 C ANISOU 2177 CD1 ILE A 308 2987 2543 2568 18 64 202 C ATOM 2178 N ARG A 309 42.763 34.538 41.359 1.00 20.08 N ANISOU 2178 N ARG A 309 2616 2470 2540 -210 134 194 N ATOM 2179 CA ARG A 309 42.421 35.511 42.392 1.00 21.14 C ANISOU 2179 CA ARG A 309 2693 2581 2757 -58 62 103 C ATOM 2180 C ARG A 309 43.399 35.622 43.584 1.00 20.29 C ANISOU 2180 C ARG A 309 2665 2538 2505 -148 149 137 C ATOM 2181 O ARG A 309 43.366 36.596 44.295 1.00 22.81 O ANISOU 2181 O ARG A 309 2917 2975 2772 -244 66 101 O ATOM 2182 CB ARG A 309 40.991 35.247 42.923 1.00 20.89 C ANISOU 2182 CB ARG A 309 2776 2476 2683 42 97 69 C ATOM 2183 CG ARG A 309 39.914 35.304 41.813 1.00 22.14 C ANISOU 2183 CG ARG A 309 2636 2893 2883 -22 26 83 C ATOM 2184 CD ARG A 309 38.469 35.257 42.365 1.00 22.92 C ANISOU 2184 CD ARG A 309 2785 3042 2878 68 16 296 C ATOM 2185 NE ARG A 309 37.524 35.049 41.265 1.00 27.52 N ANISOU 2185 NE ARG A 309 3169 3583 3704 -242 -103 193 N ATOM 2186 CZ ARG A 309 37.144 36.005 40.405 1.00 27.45 C ANISOU 2186 CZ ARG A 309 3646 3665 3116 -16 -158 79 C ATOM 2187 NH1 ARG A 309 37.618 37.259 40.501 1.00 21.42 N ANISOU 2187 NH1 ARG A 309 2932 3501 1705 17 -144 246 N ATOM 2188 NH2 ARG A 309 36.286 35.695 39.426 1.00 28.57 N ANISOU 2188 NH2 ARG A 309 3485 3615 3753 -258 -213 124 N ATOM 2189 N THR A 310 44.256 34.651 43.810 1.00 21.65 N ANISOU 2189 N THR A 310 2578 3018 2628 -172 90 117 N ATOM 2190 CA THR A 310 45.159 34.724 44.968 1.00 23.16 C ANISOU 2190 CA THR A 310 2833 3118 2846 -24 25 156 C ATOM 2191 C THR A 310 46.637 34.729 44.633 1.00 23.29 C ANISOU 2191 C THR A 310 2741 3202 2903 -31 -28 240 C ATOM 2192 O THR A 310 47.468 34.505 45.541 1.00 25.41 O ANISOU 2192 O THR A 310 2998 3658 2998 -149 -52 368 O ATOM 2193 CB THR A 310 44.915 33.597 46.000 1.00 24.23 C ANISOU 2193 CB THR A 310 2989 3145 3070 -5 -48 232 C ATOM 2194 OG1 THR A 310 44.927 32.342 45.349 1.00 22.63 O ANISOU 2194 OG1 THR A 310 3552 3176 1869 -4 -835 188 O ATOM 2195 CG2 THR A 310 43.585 33.798 46.753 1.00 28.21 C ANISOU 2195 CG2 THR A 310 3490 4050 3178 41 134 121 C ATOM 2196 N VAL A 311 46.978 34.994 43.377 1.00 21.33 N ANISOU 2196 N VAL A 311 2622 2854 2627 -63 -100 81 N ATOM 2197 CA VAL A 311 48.371 35.188 43.030 1.00 20.68 C ANISOU 2197 CA VAL A 311 2623 2675 2560 52 -1 144 C ATOM 2198 C VAL A 311 48.903 36.547 43.500 1.00 20.52 C ANISOU 2198 C VAL A 311 2647 2717 2430 58 67 95 C ATOM 2199 O VAL A 311 48.156 37.549 43.637 1.00 19.01 O ANISOU 2199 O VAL A 311 2373 2772 2074 105 407 338 O ATOM 2200 CB VAL A 311 48.657 35.045 41.536 1.00 19.14 C ANISOU 2200 CB VAL A 311 2444 2493 2334 33 -185 48 C ATOM 2201 CG1 VAL A 311 48.365 33.620 41.066 1.00 21.01 C ANISOU 2201 CG1 VAL A 311 2896 2494 2592 -75 -104 313 C ATOM 2202 CG2 VAL A 311 47.902 36.106 40.685 1.00 17.88 C ANISOU 2202 CG2 VAL A 311 2068 2403 2323 -46 129 80 C ATOM 2203 N ASP A 312 50.211 36.605 43.702 1.00 21.24 N ANISOU 2203 N ASP A 312 2736 2813 2519 66 21 33 N ATOM 2204 CA ASP A 312 50.853 37.884 43.989 1.00 20.42 C ANISOU 2204 CA ASP A 312 2610 2553 2595 20 -1 52 C ATOM 2205 C ASP A 312 51.072 38.612 42.686 1.00 18.76 C ANISOU 2205 C ASP A 312 2317 2315 2494 49 62 12 C ATOM 2206 O ASP A 312 50.897 38.033 41.620 1.00 18.66 O ANISOU 2206 O ASP A 312 2279 2314 2495 95 -312 238 O ATOM 2207 CB ASP A 312 52.166 37.702 44.733 1.00 22.58 C ANISOU 2207 CB ASP A 312 2875 2612 3092 -29 -57 42 C ATOM 2208 CG ASP A 312 52.575 38.968 45.522 1.00 24.13 C ANISOU 2208 CG ASP A 312 3222 3236 2707 -43 27 -223 C ATOM 2209 OD1 ASP A 312 51.769 39.956 45.628 1.00 28.87 O ANISOU 2209 OD1 ASP A 312 3792 3543 3631 68 -178 392 O ATOM 2210 OD2 ASP A 312 53.718 38.970 46.026 1.00 31.50 O ANISOU 2210 OD2 ASP A 312 3748 4324 3893 225 -161 -4 O ATOM 2211 N TYR A 313 51.456 39.888 42.764 1.00 20.04 N ANISOU 2211 N TYR A 313 2588 2541 2485 134 -12 -21 N ATOM 2212 CA TYR A 313 51.683 40.680 41.563 1.00 19.48 C ANISOU 2212 CA TYR A 313 2437 2393 2570 -51 105 9 C ATOM 2213 C TYR A 313 52.731 41.748 41.844 1.00 19.45 C ANISOU 2213 C TYR A 313 2475 2401 2514 -34 66 -59 C ATOM 2214 O TYR A 313 53.103 41.979 42.976 1.00 19.29 O ANISOU 2214 O TYR A 313 2608 2342 2378 -212 118 -92 O ATOM 2215 CB TYR A 313 50.387 41.331 41.078 1.00 19.44 C ANISOU 2215 CB TYR A 313 2585 2322 2478 -168 69 20 C ATOM 2216 CG TYR A 313 49.858 42.371 42.032 1.00 20.27 C ANISOU 2216 CG TYR A 313 2565 2446 2690 138 -35 166 C ATOM 2217 CD1 TYR A 313 50.226 43.708 41.893 1.00 19.94 C ANISOU 2217 CD1 TYR A 313 2756 2311 2508 -161 -291 -474 C ATOM 2218 CD2 TYR A 313 48.996 42.036 43.044 1.00 20.84 C ANISOU 2218 CD2 TYR A 313 2795 2685 2436 239 -98 146 C ATOM 2219 CE1 TYR A 313 49.755 44.648 42.736 1.00 22.21 C ANISOU 2219 CE1 TYR A 313 2620 2757 3060 162 241 -464 C ATOM 2220 CE2 TYR A 313 48.517 43.000 43.926 1.00 21.50 C ANISOU 2220 CE2 TYR A 313 2889 2512 2768 100 52 -72 C ATOM 2221 CZ TYR A 313 48.917 44.289 43.767 1.00 23.56 C ANISOU 2221 CZ TYR A 313 3353 2601 2996 8 218 -90 C ATOM 2222 OH TYR A 313 48.454 45.274 44.607 1.00 24.04 O ANISOU 2222 OH TYR A 313 3621 3492 2019 119 -22 -606 O ATOM 2223 N VAL A 314 53.261 42.323 40.774 1.00 17.50 N ANISOU 2223 N VAL A 314 2221 2046 2382 138 97 73 N ATOM 2224 CA VAL A 314 54.127 43.484 40.898 1.00 19.38 C ANISOU 2224 CA VAL A 314 2360 2346 2658 -39 77 -21 C ATOM 2225 C VAL A 314 53.614 44.610 39.978 1.00 19.14 C ANISOU 2225 C VAL A 314 2301 2398 2570 39 -159 -25 C ATOM 2226 O VAL A 314 52.901 44.368 38.982 1.00 19.16 O ANISOU 2226 O VAL A 314 2378 2381 2521 -1 -168 -265 O ATOM 2227 CB VAL A 314 55.609 43.195 40.503 1.00 19.59 C ANISOU 2227 CB VAL A 314 2381 2237 2823 157 -37 -72 C ATOM 2228 CG1 VAL A 314 56.227 42.184 41.403 1.00 23.65 C ANISOU 2228 CG1 VAL A 314 2889 2854 3242 -55 -87 43 C ATOM 2229 CG2 VAL A 314 55.682 42.763 39.044 1.00 19.33 C ANISOU 2229 CG2 VAL A 314 2225 2455 2663 68 -105 57 C ATOM 2230 N VAL A 315 54.025 45.835 40.310 1.00 19.10 N ANISOU 2230 N VAL A 315 2506 2348 2403 -5 -240 -83 N ATOM 2231 CA VAL A 315 53.750 47.013 39.522 1.00 20.21 C ANISOU 2231 CA VAL A 315 2520 2418 2739 -21 -96 -74 C ATOM 2232 C VAL A 315 55.103 47.415 38.917 1.00 20.47 C ANISOU 2232 C VAL A 315 2630 2339 2805 -16 -92 -64 C ATOM 2233 O VAL A 315 56.023 47.795 39.641 1.00 20.64 O ANISOU 2233 O VAL A 315 2543 2467 2829 -134 -264 18 O ATOM 2234 CB VAL A 315 53.146 48.174 40.400 1.00 20.45 C ANISOU 2234 CB VAL A 315 2499 2592 2678 -14 -18 -19 C ATOM 2235 CG1 VAL A 315 52.936 49.416 39.560 1.00 19.98 C ANISOU 2235 CG1 VAL A 315 2410 2629 2550 24 -158 -92 C ATOM 2236 CG2 VAL A 315 51.843 47.729 41.095 1.00 21.48 C ANISOU 2236 CG2 VAL A 315 2508 2885 2769 196 76 -79 C ATOM 2237 N VAL A 316 55.216 47.297 37.602 1.00 19.45 N ANISOU 2237 N VAL A 316 2613 2180 2595 0 -113 151 N ATOM 2238 CA VAL A 316 56.463 47.501 36.879 1.00 21.41 C ANISOU 2238 CA VAL A 316 2603 2473 3058 5 -58 77 C ATOM 2239 C VAL A 316 56.712 49.019 36.708 1.00 23.74 C ANISOU 2239 C VAL A 316 2805 2591 3623 25 16 -56 C ATOM 2240 O VAL A 316 55.775 49.837 36.810 1.00 23.10 O ANISOU 2240 O VAL A 316 2599 2299 3875 115 -36 -204 O ATOM 2241 CB VAL A 316 56.497 46.794 35.480 1.00 21.09 C ANISOU 2241 CB VAL A 316 2658 2382 2972 -35 37 136 C ATOM 2242 CG1 VAL A 316 56.242 45.266 35.561 1.00 18.26 C ANISOU 2242 CG1 VAL A 316 2426 2185 2327 -74 329 -7 C ATOM 2243 CG2 VAL A 316 55.529 47.383 34.495 1.00 22.10 C ANISOU 2243 CG2 VAL A 316 2799 2264 3332 176 104 77 C ATOM 2244 N LYS A 317 57.969 49.372 36.442 1.00 23.96 N ANISOU 2244 N LYS A 317 2758 2807 3536 29 28 -2 N ATOM 2245 CA LYS A 317 58.382 50.782 36.353 1.00 25.33 C ANISOU 2245 CA LYS A 317 3038 2966 3619 -34 25 39 C ATOM 2246 C LYS A 317 58.010 51.339 34.982 1.00 26.84 C ANISOU 2246 C LYS A 317 3288 3217 3692 -48 85 233 C ATOM 2247 O LYS A 317 57.099 52.173 34.930 1.00 29.82 O ANISOU 2247 O LYS A 317 3458 3821 4049 38 186 524 O ATOM 2248 CB LYS A 317 59.855 50.967 36.687 1.00 24.03 C ANISOU 2248 CB LYS A 317 2997 2835 3297 137 46 52 C ATOM 2249 CG LYS A 317 60.302 52.438 36.844 1.00 25.02 C ANISOU 2249 CG LYS A 317 2843 2967 3694 -107 -52 46 C ATOM 2250 CD LYS A 317 61.717 52.540 37.401 1.00 25.21 C ANISOU 2250 CD LYS A 317 3100 3072 3404 -40 8 4 C ATOM 2251 CE LYS A 317 62.353 53.931 37.208 1.00 23.87 C ANISOU 2251 CE LYS A 317 2998 2902 3167 116 -90 55 C ATOM 2252 NZ LYS A 317 62.451 54.350 35.775 1.00 19.13 N ANISOU 2252 NZ LYS A 317 2649 1954 2664 167 177 -181 N ATOM 2253 N ASN A 318 58.645 50.888 33.895 1.00 29.50 N ANISOU 2253 N ASN A 318 3642 3529 4034 0 -26 42 N ATOM 2254 CA ASN A 318 58.239 51.258 32.512 1.00 33.18 C ANISOU 2254 CA ASN A 318 4224 4102 4280 66 -5 82 C ATOM 2255 C ASN A 318 57.302 50.249 31.884 1.00 36.43 C ANISOU 2255 C ASN A 318 4629 4472 4738 2 -70 3 C ATOM 2256 O ASN A 318 57.683 49.103 31.660 1.00 38.31 O ANISOU 2256 O ASN A 318 4761 4790 5004 85 -49 -36 O ATOM 2257 CB ASN A 318 59.427 51.322 31.553 1.00 34.90 C ANISOU 2257 CB ASN A 318 4460 4244 4555 53 -100 113 C ATOM 2258 CG ASN A 318 60.337 52.447 31.845 1.00 37.62 C ANISOU 2258 CG ASN A 318 4681 4337 5273 -39 -34 12 C ATOM 2259 OD1 ASN A 318 59.894 53.590 31.955 1.00 31.14 O ANISOU 2259 OD1 ASN A 318 3782 4007 4043 160 -96 103 O ATOM 2260 ND2 ASN A 318 61.638 52.149 31.957 1.00 41.12 N ANISOU 2260 ND2 ASN A 318 4714 5051 5856 87 -160 116 N ATOM 2261 N SER A 319 56.112 50.684 31.515 1.00 37.87 N ANISOU 2261 N SER A 319 4672 4713 5004 28 -33 -31 N ATOM 2262 CA SER A 319 55.119 49.760 30.993 1.00 40.78 C ANISOU 2262 CA SER A 319 5034 5112 5345 -11 -34 -80 C ATOM 2263 C SER A 319 54.724 49.996 29.531 1.00 43.53 C ANISOU 2263 C SER A 319 5508 5529 5502 -2 -28 -35 C ATOM 2264 O SER A 319 54.021 49.181 28.965 1.00 44.29 O ANISOU 2264 O SER A 319 5687 5560 5580 -11 18 -74 O ATOM 2265 CB SER A 319 53.893 49.806 31.897 1.00 40.83 C ANISOU 2265 CB SER A 319 5093 5135 5285 -59 -18 -44 C ATOM 2266 OG SER A 319 53.687 51.121 32.371 1.00 40.10 O ANISOU 2266 OG SER A 319 4753 5104 5378 81 106 -168 O ATOM 2267 N ILE A 320 55.185 51.092 28.926 1.00 46.77 N ANISOU 2267 N ILE A 320 5915 5928 5927 44 31 30 N ATOM 2268 CA ILE A 320 54.770 51.474 27.554 1.00 48.41 C ANISOU 2268 CA ILE A 320 6166 6159 6068 35 -1 63 C ATOM 2269 C ILE A 320 55.828 51.133 26.489 1.00 50.20 C ANISOU 2269 C ILE A 320 6373 6395 6306 24 77 41 C ATOM 2270 O ILE A 320 56.597 51.993 26.041 1.00 51.72 O ANISOU 2270 O ILE A 320 6628 6518 6504 -62 87 90 O ATOM 2271 CB ILE A 320 54.366 52.987 27.455 1.00 50.08 C ANISOU 2271 CB ILE A 320 6404 6260 6363 65 -11 21 C ATOM 2272 CG1 ILE A 320 55.413 53.896 28.115 1.00 50.82 C ANISOU 2272 CG1 ILE A 320 6423 6340 6545 -84 20 81 C ATOM 2273 CG2 ILE A 320 52.984 53.210 28.112 1.00 51.88 C ANISOU 2273 CG2 ILE A 320 6482 6614 6615 -25 21 39 C ATOM 2274 CD1 ILE A 320 55.316 55.382 27.720 1.00 51.00 C ANISOU 2274 CD1 ILE A 320 6518 6385 6474 28 -13 -4 C TER 2275 ILE A 320 ATOM 1 N ASN A 3 59.201 48.872 44.218 1.00 41.21 N ANISOU 1 N ASN B 3 5286 5280 5092 -22 -74 -43 N ATOM 2 CA ASN A 3 60.673 48.591 44.268 1.00 39.21 C ANISOU 2 CA ASN B 3 5022 5109 4767 -38 -65 -41 C ATOM 3 C ASN A 3 61.178 47.724 43.082 1.00 37.49 C ANISOU 3 C ASN B 3 4795 4861 4587 -64 -23 -15 C ATOM 4 O ASN A 3 62.259 47.126 43.141 1.00 37.44 O ANISOU 4 O ASN B 3 4919 4686 4619 71 60 -72 O ATOM 5 CB ASN A 3 61.049 47.959 45.626 1.00 41.38 C ANISOU 5 CB ASN B 3 5312 5433 4974 -42 -12 75 C ATOM 6 CG ASN A 3 60.283 46.670 45.921 1.00 48.08 C ANISOU 6 CG ASN B 3 5930 6164 6173 213 47 -17 C ATOM 7 OD1 ASN A 3 59.063 46.581 45.706 1.00 52.26 O ANISOU 7 OD1 ASN B 3 6786 6322 6747 31 -14 110 O ATOM 8 ND2 ASN A 3 61.001 45.665 46.439 1.00 52.95 N ANISOU 8 ND2 ASN B 3 6357 6739 7022 -38 47 164 N ATOM 9 N VAL A 4 60.403 47.713 41.998 1.00 35.31 N ANISOU 9 N VAL B 4 4388 4697 4331 -67 -63 -91 N ATOM 10 CA VAL A 4 60.668 46.850 40.843 1.00 31.71 C ANISOU 10 CA VAL B 4 4020 4072 3955 -44 105 -190 C ATOM 11 C VAL A 4 61.200 47.719 39.706 1.00 27.77 C ANISOU 11 C VAL B 4 3483 3445 3623 -94 -10 -222 C ATOM 12 O VAL A 4 60.813 48.879 39.543 1.00 25.08 O ANISOU 12 O VAL B 4 3168 3089 3271 -77 -27 -672 O ATOM 13 CB VAL A 4 59.438 45.905 40.503 1.00 32.76 C ANISOU 13 CB VAL B 4 4359 4053 4035 -70 -15 -94 C ATOM 14 CG1 VAL A 4 58.211 46.314 41.299 1.00 38.88 C ANISOU 14 CG1 VAL B 4 5148 4766 4858 -153 -76 -102 C ATOM 15 CG2 VAL A 4 59.077 45.856 39.052 1.00 32.78 C ANISOU 15 CG2 VAL B 4 3984 4240 4228 -90 -120 -128 C ATOM 16 N PHE A 5 62.126 47.150 38.956 1.00 24.57 N ANISOU 16 N PHE B 5 3087 3042 3203 -127 -68 -48 N ATOM 17 CA PHE A 5 62.752 47.825 37.858 1.00 22.77 C ANISOU 17 CA PHE B 5 2768 2855 3026 -125 44 21 C ATOM 18 C PHE A 5 63.272 46.779 36.866 1.00 20.36 C ANISOU 18 C PHE B 5 2512 2661 2561 -18 46 0 C ATOM 19 O PHE A 5 63.175 45.572 37.117 1.00 18.18 O ANISOU 19 O PHE B 5 2408 2268 2229 101 134 -170 O ATOM 20 CB PHE A 5 63.914 48.685 38.350 1.00 22.13 C ANISOU 20 CB PHE B 5 2589 2999 2820 -103 -12 112 C ATOM 21 CG PHE A 5 64.934 47.928 39.158 1.00 21.63 C ANISOU 21 CG PHE B 5 2626 2817 2774 174 -255 210 C ATOM 22 CD1 PHE A 5 65.898 47.112 38.566 1.00 20.25 C ANISOU 22 CD1 PHE B 5 2787 2218 2688 150 -156 217 C ATOM 23 CD2 PHE A 5 64.946 48.058 40.505 1.00 22.10 C ANISOU 23 CD2 PHE B 5 3357 2882 2158 -26 23 -400 C ATOM 24 CE1 PHE A 5 66.816 46.384 39.352 1.00 20.23 C ANISOU 24 CE1 PHE B 5 2597 2626 2463 162 -202 226 C ATOM 25 CE2 PHE A 5 65.858 47.353 41.294 1.00 25.24 C ANISOU 25 CE2 PHE B 5 3557 3021 3011 -429 -89 -134 C ATOM 26 CZ PHE A 5 66.797 46.519 40.708 1.00 21.93 C ANISOU 26 CZ PHE B 5 2850 2780 2698 -256 -61 -169 C ATOM 27 N ASP A 6 63.852 47.255 35.770 1.00 19.30 N ANISOU 27 N ASP B 6 2270 2422 2640 -133 251 60 N ATOM 28 CA ASP A 6 64.502 46.409 34.764 1.00 19.59 C ANISOU 28 CA ASP B 6 2476 2422 2542 -10 73 -2 C ATOM 29 C ASP A 6 65.841 47.023 34.335 1.00 18.64 C ANISOU 29 C ASP B 6 2253 2408 2419 -68 71 38 C ATOM 30 O ASP A 6 66.238 48.092 34.812 1.00 16.78 O ANISOU 30 O ASP B 6 2297 2168 1908 -309 -195 315 O ATOM 31 CB ASP A 6 63.599 46.207 33.541 1.00 19.47 C ANISOU 31 CB ASP B 6 2488 2443 2466 -69 100 -155 C ATOM 32 CG ASP A 6 63.739 44.815 32.919 1.00 18.97 C ANISOU 32 CG ASP B 6 2318 2317 2572 -79 160 6 C ATOM 33 OD1 ASP A 6 64.718 44.083 33.228 1.00 15.50 O ANISOU 33 OD1 ASP B 6 1605 2445 1837 -152 -248 108 O ATOM 34 OD2 ASP A 6 62.890 44.451 32.089 1.00 24.72 O ANISOU 34 OD2 ASP B 6 2958 2981 3452 -287 -189 221 O ATOM 35 N TYR A 7 66.510 46.328 33.414 1.00 18.62 N ANISOU 35 N TYR B 7 2237 2445 2391 94 34 -49 N ATOM 36 CA TYR A 7 67.854 46.667 32.921 1.00 18.78 C ANISOU 36 CA TYR B 7 2396 2341 2399 28 -17 -38 C ATOM 37 C TYR A 7 68.020 48.141 32.581 1.00 17.77 C ANISOU 37 C TYR B 7 2258 2182 2310 24 -46 -139 C ATOM 38 O TYR A 7 68.989 48.775 33.029 1.00 19.79 O ANISOU 38 O TYR B 7 2403 2263 2852 65 -178 -296 O ATOM 39 CB TYR A 7 68.202 45.790 31.710 1.00 19.13 C ANISOU 39 CB TYR B 7 2368 2343 2555 35 -45 -74 C ATOM 40 CG TYR A 7 68.527 44.365 32.126 1.00 18.94 C ANISOU 40 CG TYR B 7 2359 2094 2740 0 -50 52 C ATOM 41 CD1 TYR A 7 69.746 44.054 32.750 1.00 18.84 C ANISOU 41 CD1 TYR B 7 2132 2175 2848 63 7 173 C ATOM 42 CD2 TYR A 7 67.608 43.336 31.945 1.00 17.89 C ANISOU 42 CD2 TYR B 7 2141 2198 2456 55 -10 41 C ATOM 43 CE1 TYR A 7 70.030 42.771 33.156 1.00 18.35 C ANISOU 43 CE1 TYR B 7 2299 2070 2602 27 -86 38 C ATOM 44 CE2 TYR A 7 67.902 42.054 32.328 1.00 20.83 C ANISOU 44 CE2 TYR B 7 2278 2412 3222 -31 32 60 C ATOM 45 CZ TYR A 7 69.108 41.767 32.946 1.00 21.07 C ANISOU 45 CZ TYR B 7 2320 2505 3178 59 -94 165 C ATOM 46 OH TYR A 7 69.403 40.468 33.359 1.00 20.80 O ANISOU 46 OH TYR B 7 2448 2019 3434 147 126 26 O ATOM 47 N GLU A 8 67.077 48.679 31.815 1.00 18.34 N ANISOU 47 N GLU B 8 2254 2200 2511 109 18 -93 N ATOM 48 CA GLU A 8 67.152 50.068 31.331 1.00 18.39 C ANISOU 48 CA GLU B 8 2407 2216 2362 -29 85 76 C ATOM 49 C GLU A 8 67.084 51.133 32.436 1.00 19.19 C ANISOU 49 C GLU B 8 2425 2353 2511 9 140 35 C ATOM 50 O GLU A 8 67.492 52.296 32.219 1.00 21.48 O ANISOU 50 O GLU B 8 2465 2900 2794 237 -22 169 O ATOM 51 CB GLU A 8 66.101 50.293 30.197 1.00 19.09 C ANISOU 51 CB GLU B 8 2484 2424 2342 3 -3 143 C ATOM 52 CG GLU A 8 64.661 50.466 30.650 1.00 16.06 C ANISOU 52 CG GLU B 8 2637 2167 1296 -61 10 356 C ATOM 53 CD GLU A 8 63.865 49.177 30.756 1.00 25.03 C ANISOU 53 CD GLU B 8 3167 3034 3309 98 -42 138 C ATOM 54 OE1 GLU A 8 64.492 48.087 30.827 1.00 27.68 O ANISOU 54 OE1 GLU B 8 3264 3476 3775 -64 -451 425 O ATOM 55 OE2 GLU A 8 62.593 49.262 30.792 1.00 21.93 O ANISOU 55 OE2 GLU B 8 3517 2913 1902 -271 -378 -61 O ATOM 56 N ASP A 9 66.607 50.750 33.631 1.00 17.03 N ANISOU 56 N ASP B 9 2241 2050 2177 0 98 203 N ATOM 57 CA ASP A 9 66.470 51.669 34.720 1.00 17.43 C ANISOU 57 CA ASP B 9 2173 2096 2353 -72 61 37 C ATOM 58 C ASP A 9 67.753 51.763 35.566 1.00 17.35 C ANISOU 58 C ASP B 9 2150 2205 2236 3 -19 95 C ATOM 59 O ASP A 9 67.877 52.652 36.395 1.00 18.15 O ANISOU 59 O ASP B 9 1974 2277 2643 -45 -175 198 O ATOM 60 CB ASP A 9 65.346 51.201 35.638 1.00 17.67 C ANISOU 60 CB ASP B 9 2021 2311 2379 -60 9 -74 C ATOM 61 CG ASP A 9 64.022 51.086 34.909 1.00 21.03 C ANISOU 61 CG ASP B 9 2673 2401 2915 -155 171 9 C ATOM 62 OD1 ASP A 9 63.637 52.098 34.256 1.00 18.68 O ANISOU 62 OD1 ASP B 9 2645 2353 2100 -173 360 10 O ATOM 63 OD2 ASP A 9 63.389 50.000 34.988 1.00 21.89 O ANISOU 63 OD2 ASP B 9 2519 2832 2964 -178 76 142 O ATOM 64 N ILE A 10 68.693 50.846 35.377 1.00 16.30 N ANISOU 64 N ILE B 10 2088 2006 2098 7 25 103 N ATOM 65 CA ILE A 10 69.870 50.783 36.257 1.00 17.32 C ANISOU 65 CA ILE B 10 2205 2105 2269 -49 64 37 C ATOM 66 C ILE A 10 71.118 51.407 35.640 1.00 16.31 C ANISOU 66 C ILE B 10 2148 1905 2142 -49 28 69 C ATOM 67 O ILE A 10 71.442 51.147 34.472 1.00 17.75 O ANISOU 67 O ILE B 10 2239 2158 2347 9 10 111 O ATOM 68 CB ILE A 10 70.182 49.312 36.666 1.00 17.66 C ANISOU 68 CB ILE B 10 2154 2240 2314 -79 -11 7 C ATOM 69 CG1 ILE A 10 69.049 48.707 37.501 1.00 18.85 C ANISOU 69 CG1 ILE B 10 2158 2081 2924 -174 223 0 C ATOM 70 CG2 ILE A 10 71.511 49.235 37.488 1.00 18.78 C ANISOU 70 CG2 ILE B 10 2418 2159 2557 -78 209 32 C ATOM 71 CD1 ILE A 10 68.747 49.462 38.746 1.00 22.83 C ANISOU 71 CD1 ILE B 10 2409 3125 3138 62 190 -58 C ATOM 72 N GLN A 11 71.819 52.225 36.429 1.00 16.01 N ANISOU 72 N GLN B 11 2026 2055 2002 20 -119 -105 N ATOM 73 CA GLN A 11 73.214 52.605 36.111 1.00 17.07 C ANISOU 73 CA GLN B 11 2182 2101 2201 -10 -44 -25 C ATOM 74 C GLN A 11 74.128 52.199 37.217 1.00 15.69 C ANISOU 74 C GLN B 11 1957 1956 2045 -6 -48 -76 C ATOM 75 O GLN A 11 73.841 52.450 38.397 1.00 15.79 O ANISOU 75 O GLN B 11 2351 1772 1877 -11 -311 75 O ATOM 76 CB GLN A 11 73.376 54.120 35.891 1.00 18.13 C ANISOU 76 CB GLN B 11 2276 2187 2425 -15 -148 -66 C ATOM 77 CG GLN A 11 72.765 54.645 34.624 1.00 21.51 C ANISOU 77 CG GLN B 11 2640 2874 2658 140 335 -2 C ATOM 78 CD GLN A 11 73.559 54.255 33.375 1.00 30.51 C ANISOU 78 CD GLN B 11 4162 3696 3734 -3 -204 -214 C ATOM 79 OE1 GLN A 11 74.756 54.460 33.294 1.00 34.17 O ANISOU 79 OE1 GLN B 11 5087 3813 4082 368 -249 99 O ATOM 80 NE2 GLN A 11 72.874 53.677 32.401 1.00 33.86 N ANISOU 80 NE2 GLN B 11 4510 4389 3966 56 -20 82 N ATOM 81 N LEU A 12 75.223 51.536 36.869 1.00 15.16 N ANISOU 81 N LEU B 12 1907 1836 2014 103 -77 -135 N ATOM 82 CA LEU A 12 76.252 51.200 37.868 1.00 15.88 C ANISOU 82 CA LEU B 12 1964 1998 2072 -38 16 -54 C ATOM 83 C LEU A 12 77.236 52.376 38.052 1.00 15.72 C ANISOU 83 C LEU B 12 1995 1917 2060 -4 -17 -18 C ATOM 84 O LEU A 12 77.623 53.078 37.079 1.00 17.40 O ANISOU 84 O LEU B 12 2027 2125 2457 256 -17 217 O ATOM 85 CB LEU A 12 77.016 49.910 37.450 1.00 16.27 C ANISOU 85 CB LEU B 12 1845 2093 2245 -86 9 67 C ATOM 86 CG LEU A 12 76.105 48.712 37.077 1.00 17.96 C ANISOU 86 CG LEU B 12 1992 2517 2313 24 -57 -44 C ATOM 87 CD1 LEU A 12 76.898 47.530 36.569 1.00 19.70 C ANISOU 87 CD1 LEU B 12 2160 2288 3034 -100 -77 -21 C ATOM 88 CD2 LEU A 12 75.226 48.299 38.249 1.00 16.81 C ANISOU 88 CD2 LEU B 12 1617 2300 2471 213 -220 35 C ATOM 89 N ILE A 13 77.668 52.559 39.279 1.00 17.01 N ANISOU 89 N ILE B 13 2170 2036 2253 42 90 -119 N ATOM 90 CA ILE A 13 78.487 53.659 39.665 1.00 17.96 C ANISOU 90 CA ILE B 13 2247 2176 2397 28 34 -19 C ATOM 91 C ILE A 13 79.969 53.253 39.675 1.00 19.00 C ANISOU 91 C ILE B 13 2296 2265 2655 -67 39 83 C ATOM 92 O ILE A 13 80.363 52.258 40.313 1.00 20.30 O ANISOU 92 O ILE B 13 2468 2507 2735 107 95 415 O ATOM 93 CB ILE A 13 78.086 54.207 41.023 1.00 19.01 C ANISOU 93 CB ILE B 13 2321 2167 2732 -47 -148 -53 C ATOM 94 CG1 ILE A 13 76.663 54.790 40.912 1.00 19.59 C ANISOU 94 CG1 ILE B 13 2677 2123 2641 -28 -73 276 C ATOM 95 CG2 ILE A 13 79.084 55.312 41.508 1.00 19.75 C ANISOU 95 CG2 ILE B 13 2556 2284 2660 -17 -98 -98 C ATOM 96 CD1 ILE A 13 76.058 55.144 42.211 1.00 20.35 C ANISOU 96 CD1 ILE B 13 2821 2328 2581 -101 -129 9 C ATOM 97 N PRO A 14 80.789 54.032 38.966 1.00 18.60 N ANISOU 97 N PRO B 14 2394 2301 2372 -126 -8 -100 N ATOM 98 CA PRO A 14 82.224 53.741 38.906 1.00 18.78 C ANISOU 98 CA PRO B 14 2380 2333 2422 42 -29 8 C ATOM 99 C PRO A 14 82.955 53.853 40.252 1.00 19.36 C ANISOU 99 C PRO B 14 2558 2368 2428 -6 19 93 C ATOM 100 O PRO A 14 82.604 54.685 41.114 1.00 18.63 O ANISOU 100 O PRO B 14 2764 2164 2149 -159 -82 295 O ATOM 101 CB PRO A 14 82.747 54.757 37.892 1.00 18.93 C ANISOU 101 CB PRO B 14 2451 2344 2397 89 76 -73 C ATOM 102 CG PRO A 14 81.550 55.184 37.104 1.00 20.88 C ANISOU 102 CG PRO B 14 2563 2543 2828 192 166 -181 C ATOM 103 CD PRO A 14 80.458 55.202 38.148 1.00 20.71 C ANISOU 103 CD PRO B 14 2535 2627 2705 -268 -21 -117 C ATOM 104 N ALA A 15 83.976 53.029 40.394 1.00 18.88 N ANISOU 104 N ALA B 15 2455 2342 2377 -3 103 174 N ATOM 105 CA ALA A 15 84.877 53.071 41.554 1.00 20.19 C ANISOU 105 CA ALA B 15 2668 2505 2495 24 19 67 C ATOM 106 C ALA A 15 86.310 53.362 41.048 1.00 20.31 C ANISOU 106 C ALA B 15 2749 2440 2527 89 -51 54 C ATOM 107 O ALA A 15 86.568 53.274 39.831 1.00 18.57 O ANISOU 107 O ALA B 15 2628 2176 2248 263 163 -159 O ATOM 108 CB ALA A 15 84.815 51.762 42.228 1.00 21.80 C ANISOU 108 CB ALA B 15 2908 2691 2683 116 50 225 C ATOM 109 N LYS A 16 87.238 53.688 41.953 1.00 20.94 N ANISOU 109 N LYS B 16 2762 2603 2590 -39 61 60 N ATOM 110 CA LYS A 16 88.609 54.039 41.532 1.00 21.33 C ANISOU 110 CA LYS B 16 2758 2587 2759 31 119 69 C ATOM 111 C LYS A 16 89.216 52.970 40.620 1.00 20.26 C ANISOU 111 C LYS B 16 2647 2284 2766 145 60 231 C ATOM 112 O LYS A 16 89.267 51.786 40.988 1.00 19.71 O ANISOU 112 O LYS B 16 2481 2384 2622 -140 13 224 O ATOM 113 CB LYS A 16 89.524 54.283 42.737 1.00 22.97 C ANISOU 113 CB LYS B 16 2860 2761 3104 -19 101 -44 C ATOM 114 CG LYS A 16 90.869 54.894 42.379 1.00 23.21 C ANISOU 114 CG LYS B 16 3002 2769 3046 -52 175 16 C ATOM 115 CD LYS A 16 91.697 54.981 43.612 1.00 24.98 C ANISOU 115 CD LYS B 16 3355 2990 3147 141 69 95 C ATOM 116 CE LYS A 16 92.903 55.809 43.458 1.00 29.28 C ANISOU 116 CE LYS B 16 3901 3535 3689 249 -19 -72 C ATOM 117 NZ LYS A 16 93.609 55.872 44.756 1.00 29.87 N ANISOU 117 NZ LYS B 16 4373 3184 3791 -171 101 160 N ATOM 118 N CYS A 17 89.691 53.387 39.443 1.00 20.71 N ANISOU 118 N CYS B 17 2673 2494 2701 95 112 435 N ATOM 119 CA CYS A 17 90.328 52.488 38.491 1.00 22.28 C ANISOU 119 CA CYS B 17 2865 2612 2988 0 143 146 C ATOM 120 C CYS A 17 91.705 52.110 38.979 1.00 22.34 C ANISOU 120 C CYS B 17 2884 2614 2990 7 147 174 C ATOM 121 O CYS A 17 92.500 52.996 39.325 1.00 21.11 O ANISOU 121 O CYS B 17 2674 2357 2990 -111 352 274 O ATOM 122 CB CYS A 17 90.472 53.133 37.123 1.00 21.90 C ANISOU 122 CB CYS B 17 3110 2435 2774 7 141 257 C ATOM 123 SG CYS A 17 91.042 52.070 35.787 1.00 25.86 S ANISOU 123 SG CYS B 17 3269 3112 3442 -128 -53 366 S ATOM 124 N ILE A 18 91.976 50.806 38.979 1.00 23.31 N ANISOU 124 N ILE B 18 2704 2705 3446 26 191 107 N ATOM 125 CA ILE A 18 93.262 50.240 39.495 1.00 24.28 C ANISOU 125 CA ILE B 18 3038 2826 3360 -15 147 168 C ATOM 126 C ILE A 18 94.065 49.484 38.458 1.00 24.56 C ANISOU 126 C ILE B 18 3030 2978 3323 -10 243 62 C ATOM 127 O ILE A 18 95.147 48.956 38.775 1.00 27.45 O ANISOU 127 O ILE B 18 3626 3112 3691 13 287 -85 O ATOM 128 CB ILE A 18 93.076 49.295 40.730 1.00 23.30 C ANISOU 128 CB ILE B 18 2966 2803 3084 -77 67 128 C ATOM 129 CG1 ILE A 18 92.293 48.021 40.337 1.00 21.87 C ANISOU 129 CG1 ILE B 18 2944 2403 2961 -104 139 139 C ATOM 130 CG2 ILE A 18 92.506 50.032 41.931 1.00 21.14 C ANISOU 130 CG2 ILE B 18 2663 2341 3028 -172 284 258 C ATOM 131 CD1 ILE A 18 92.031 47.066 41.477 1.00 25.35 C ANISOU 131 CD1 ILE B 18 3430 2647 3554 -35 277 135 C ATOM 132 N VAL A 19 93.587 49.449 37.219 1.00 24.48 N ANISOU 132 N VAL B 19 3050 2865 3385 97 48 124 N ATOM 133 CA VAL A 19 94.308 48.818 36.140 1.00 27.84 C ANISOU 133 CA VAL B 19 3537 3369 3672 -27 33 59 C ATOM 134 C VAL A 19 94.847 49.887 35.184 1.00 29.27 C ANISOU 134 C VAL B 19 3664 3610 3843 -11 112 27 C ATOM 135 O VAL A 19 94.283 50.983 35.053 1.00 28.29 O ANISOU 135 O VAL B 19 3578 3433 3737 2 188 23 O ATOM 136 CB VAL A 19 93.458 47.766 35.343 1.00 27.25 C ANISOU 136 CB VAL B 19 3429 3360 3563 -48 -21 -76 C ATOM 137 CG1 VAL A 19 92.996 46.633 36.260 1.00 26.70 C ANISOU 137 CG1 VAL B 19 3178 3340 3625 -19 -72 9 C ATOM 138 CG2 VAL A 19 92.264 48.426 34.622 1.00 25.28 C ANISOU 138 CG2 VAL B 19 3436 3265 2901 56 -54 -58 C ATOM 139 N ASN A 20 95.956 49.559 34.537 1.00 32.14 N ANISOU 139 N ASN B 20 4061 3979 4172 -58 29 -63 N ATOM 140 CA ASN A 20 96.547 50.420 33.520 1.00 33.79 C ANISOU 140 CA ASN B 20 4277 4248 4312 7 51 -147 C ATOM 141 C ASN A 20 96.008 50.122 32.157 1.00 34.71 C ANISOU 141 C ASN B 20 4391 4377 4421 4 -25 -116 C ATOM 142 O ASN A 20 96.187 50.919 31.241 1.00 34.40 O ANISOU 142 O ASN B 20 4438 4485 4145 227 -127 -446 O ATOM 143 CB ASN A 20 98.064 50.260 33.483 1.00 35.79 C ANISOU 143 CB ASN B 20 4544 4431 4624 31 4 -110 C ATOM 144 CG ASN A 20 98.753 51.060 34.539 1.00 41.65 C ANISOU 144 CG ASN B 20 5284 5247 5293 162 -167 48 C ATOM 145 OD1 ASN A 20 98.344 52.183 34.858 1.00 45.25 O ANISOU 145 OD1 ASN B 20 5308 5599 6284 30 -123 -8 O ATOM 146 ND2 ASN A 20 99.824 50.497 35.090 1.00 46.19 N ANISOU 146 ND2 ASN B 20 5860 5755 5936 -20 132 171 N ATOM 147 N SER A 21 95.342 48.983 32.017 1.00 35.71 N ANISOU 147 N SER B 21 4493 4461 4613 71 -7 -168 N ATOM 148 CA SER A 21 94.758 48.591 30.747 1.00 36.77 C ANISOU 148 CA SER B 21 4702 4585 4681 85 -9 -110 C ATOM 149 C SER A 21 93.666 47.553 30.942 1.00 36.55 C ANISOU 149 C SER B 21 4647 4478 4761 135 18 -120 C ATOM 150 O SER A 21 93.855 46.618 31.701 1.00 36.04 O ANISOU 150 O SER B 21 4500 4284 4907 262 156 -201 O ATOM 151 CB SER A 21 95.816 47.931 29.881 1.00 38.08 C ANISOU 151 CB SER B 21 4972 4734 4759 70 -24 -195 C ATOM 152 OG SER A 21 95.244 47.544 28.653 1.00 41.52 O ANISOU 152 OG SER B 21 5604 5063 5105 138 -237 75 O ATOM 153 N ARG A 22 92.566 47.714 30.219 1.00 37.97 N ANISOU 153 N ARG B 22 4826 4764 4835 142 26 4 N ATOM 154 CA ARG A 22 91.484 46.699 30.131 1.00 38.56 C ANISOU 154 CA ARG B 22 4901 4835 4914 128 20 -16 C ATOM 155 C ARG A 22 91.981 45.285 30.071 1.00 38.28 C ANISOU 155 C ARG B 22 4899 4835 4811 95 -95 -98 C ATOM 156 O ARG A 22 91.364 44.367 30.620 1.00 37.44 O ANISOU 156 O ARG B 22 4886 4732 4607 254 -271 -237 O ATOM 157 CB ARG A 22 90.723 46.855 28.825 1.00 38.40 C ANISOU 157 CB ARG B 22 4874 4921 4795 151 6 -14 C ATOM 158 CG ARG A 22 89.631 47.825 28.851 1.00 39.58 C ANISOU 158 CG ARG B 22 5136 4886 5014 86 46 -5 C ATOM 159 CD ARG A 22 88.610 47.474 27.816 1.00 40.57 C ANISOU 159 CD ARG B 22 5167 5136 5111 54 -33 54 C ATOM 160 NE ARG A 22 89.181 47.226 26.504 1.00 41.19 N ANISOU 160 NE ARG B 22 5484 5136 5028 86 5 -165 N ATOM 161 CZ ARG A 22 88.555 47.508 25.361 1.00 44.06 C ANISOU 161 CZ ARG B 22 5654 5517 5567 -82 4 56 C ATOM 162 NH1 ARG A 22 87.337 48.034 25.370 1.00 45.31 N ANISOU 162 NH1 ARG B 22 5748 5531 5936 -5 12 -76 N ATOM 163 NH2 ARG A 22 89.146 47.261 24.191 1.00 43.34 N ANISOU 163 NH2 ARG B 22 5568 5589 5307 -72 176 -142 N ATOM 164 N SER A 23 93.071 45.114 29.322 1.00 38.41 N ANISOU 164 N SER B 23 5013 4748 4833 117 -64 -144 N ATOM 165 CA SER A 23 93.705 43.821 29.137 1.00 38.28 C ANISOU 165 CA SER B 23 4946 4747 4851 62 0 -113 C ATOM 166 C SER A 23 94.091 43.134 30.426 1.00 37.10 C ANISOU 166 C SER B 23 4754 4440 4903 9 -16 -117 C ATOM 167 O SER A 23 94.205 41.918 30.435 1.00 38.76 O ANISOU 167 O SER B 23 4921 4559 5245 -51 -145 -329 O ATOM 168 CB SER A 23 94.934 43.976 28.236 1.00 40.30 C ANISOU 168 CB SER B 23 5254 4943 5112 -43 4 -145 C ATOM 169 OG SER A 23 94.549 44.625 27.028 1.00 44.65 O ANISOU 169 OG SER B 23 5860 5970 5135 -107 -7 -90 O ATOM 170 N GLU A 24 94.258 43.897 31.507 1.00 35.13 N ANISOU 170 N GLU B 24 4422 4166 4759 -10 -34 -144 N ATOM 171 CA GLU A 24 94.519 43.343 32.820 1.00 34.55 C ANISOU 171 CA GLU B 24 4349 4114 4663 -1 -45 -103 C ATOM 172 C GLU A 24 93.312 42.658 33.458 1.00 33.16 C ANISOU 172 C GLU B 24 4152 3920 4527 -8 -28 -14 C ATOM 173 O GLU A 24 93.481 41.962 34.439 1.00 32.76 O ANISOU 173 O GLU B 24 4336 3581 4530 136 52 -57 O ATOM 174 CB GLU A 24 94.987 44.429 33.809 1.00 36.13 C ANISOU 174 CB GLU B 24 4493 4258 4977 4 -38 -92 C ATOM 175 CG GLU A 24 96.391 44.958 33.601 1.00 36.81 C ANISOU 175 CG GLU B 24 4561 4448 4975 -25 -101 -79 C ATOM 176 CD GLU A 24 96.715 46.110 34.542 1.00 36.65 C ANISOU 176 CD GLU B 24 4609 4418 4894 0 -38 5 C ATOM 177 OE1 GLU A 24 96.733 45.894 35.786 1.00 39.64 O ANISOU 177 OE1 GLU B 24 5255 4825 4980 -212 -160 79 O ATOM 178 OE2 GLU A 24 96.944 47.224 34.028 1.00 38.66 O ANISOU 178 OE2 GLU B 24 4435 4610 5644 99 42 -32 O ATOM 179 N CYS A 25 92.101 42.876 32.944 1.00 32.46 N ANISOU 179 N CYS B 25 3884 3972 4475 79 -116 -18 N ATOM 180 CA CYS A 25 90.897 42.396 33.646 1.00 30.17 C ANISOU 180 CA CYS B 25 3628 3708 4124 14 -95 -47 C ATOM 181 C CYS A 25 90.501 40.972 33.222 1.00 29.73 C ANISOU 181 C CYS B 25 3649 3622 4023 16 -48 -39 C ATOM 182 O CYS A 25 90.438 40.666 32.041 1.00 29.80 O ANISOU 182 O CYS B 25 3451 3661 4208 58 -289 86 O ATOM 183 CB CYS A 25 89.734 43.352 33.407 1.00 28.97 C ANISOU 183 CB CYS B 25 3390 3748 3868 118 -94 41 C ATOM 184 SG CYS A 25 90.163 45.039 33.866 1.00 26.84 S ANISOU 184 SG CYS B 25 2877 2873 4446 -31 -317 -238 S ATOM 185 N ASP A 26 90.214 40.131 34.210 1.00 30.02 N ANISOU 185 N ASP B 26 3671 3526 4208 36 10 47 N ATOM 186 CA ASP A 26 89.905 38.723 33.974 1.00 28.84 C ANISOU 186 CA ASP B 26 3577 3402 3979 65 -7 -25 C ATOM 187 C ASP A 26 88.373 38.549 33.967 1.00 28.06 C ANISOU 187 C ASP B 26 3419 3281 3960 72 26 -75 C ATOM 188 O ASP A 26 87.745 38.747 35.005 1.00 28.97 O ANISOU 188 O ASP B 26 3465 2973 4568 21 -68 -309 O ATOM 189 CB ASP A 26 90.526 37.873 35.087 1.00 29.35 C ANISOU 189 CB ASP B 26 3655 3421 4075 84 26 18 C ATOM 190 CG ASP A 26 90.343 36.355 34.865 1.00 32.52 C ANISOU 190 CG ASP B 26 3816 4060 4481 25 -81 151 C ATOM 191 OD1 ASP A 26 89.377 35.903 34.207 1.00 32.98 O ANISOU 191 OD1 ASP B 26 4088 3635 4805 -112 -75 318 O ATOM 192 OD2 ASP A 26 91.191 35.599 35.363 1.00 40.07 O ANISOU 192 OD2 ASP B 26 4927 4917 5380 -260 7 406 O ATOM 193 N THR A 27 87.818 38.155 32.826 1.00 27.61 N ANISOU 193 N THR B 27 3303 3204 3981 76 50 -94 N ATOM 194 CA THR A 27 86.353 37.926 32.642 1.00 27.37 C ANISOU 194 CA THR B 27 3305 3250 3844 21 34 -22 C ATOM 195 C THR A 27 85.862 36.458 32.806 1.00 26.59 C ANISOU 195 C THR B 27 3199 3140 3764 3 11 86 C ATOM 196 O THR A 27 84.696 36.135 32.506 1.00 24.14 O ANISOU 196 O THR B 27 2950 2706 3516 54 120 -143 O ATOM 197 CB THR A 27 85.919 38.345 31.250 1.00 27.47 C ANISOU 197 CB THR B 27 3373 3300 3764 76 10 -94 C ATOM 198 OG1 THR A 27 86.560 37.510 30.277 1.00 30.70 O ANISOU 198 OG1 THR B 27 3216 3757 4692 96 -140 -205 O ATOM 199 CG2 THR A 27 86.238 39.810 30.987 1.00 23.94 C ANISOU 199 CG2 THR B 27 3069 3191 2837 142 -116 -360 C ATOM 200 N THR A 28 86.739 35.572 33.263 1.00 25.87 N ANISOU 200 N THR B 28 3110 3037 3681 -105 44 255 N ATOM 201 CA THR A 28 86.391 34.145 33.344 1.00 25.92 C ANISOU 201 CA THR B 28 3185 3141 3522 -63 -14 174 C ATOM 202 C THR A 28 85.413 33.861 34.463 1.00 26.69 C ANISOU 202 C THR B 28 3252 3227 3660 -73 -45 162 C ATOM 203 O THR A 28 85.313 34.622 35.451 1.00 26.68 O ANISOU 203 O THR B 28 2955 3053 4127 118 -316 405 O ATOM 204 CB THR A 28 87.635 33.248 33.559 1.00 25.13 C ANISOU 204 CB THR B 28 3078 3202 3266 -68 -80 145 C ATOM 205 OG1 THR A 28 88.228 33.541 34.839 1.00 25.67 O ANISOU 205 OG1 THR B 28 3384 3107 3261 156 -368 211 O ATOM 206 CG2 THR A 28 88.625 33.467 32.477 1.00 23.30 C ANISOU 206 CG2 THR B 28 2534 3023 3293 -61 -80 52 C ATOM 207 N VAL A 29 84.680 32.759 34.297 1.00 26.63 N ANISOU 207 N VAL B 29 3133 3310 3672 -110 -101 104 N ATOM 208 CA VAL A 29 83.809 32.206 35.342 1.00 26.04 C ANISOU 208 CA VAL B 29 3225 3241 3426 -119 -72 42 C ATOM 209 C VAL A 29 83.835 30.667 35.353 1.00 24.60 C ANISOU 209 C VAL B 29 3107 2980 3258 6 -70 98 C ATOM 210 O VAL A 29 84.095 30.046 34.323 1.00 26.70 O ANISOU 210 O VAL B 29 3395 3095 3655 -64 -136 140 O ATOM 211 CB VAL A 29 82.348 32.744 35.191 1.00 27.32 C ANISOU 211 CB VAL B 29 3377 3336 3666 -59 -47 47 C ATOM 212 CG1 VAL A 29 81.664 32.186 33.954 1.00 26.84 C ANISOU 212 CG1 VAL B 29 3477 3098 3622 -250 217 246 C ATOM 213 CG2 VAL A 29 81.545 32.505 36.456 1.00 27.75 C ANISOU 213 CG2 VAL B 29 3362 3375 3806 -78 -80 45 C ATOM 214 N THR A 30 83.628 30.084 36.527 1.00 24.75 N ANISOU 214 N THR B 30 3141 2865 3396 -17 -74 -63 N ATOM 215 CA THR A 30 83.525 28.619 36.729 1.00 25.08 C ANISOU 215 CA THR B 30 3131 3133 3263 -12 -123 -18 C ATOM 216 C THR A 30 82.065 28.247 37.015 1.00 25.30 C ANISOU 216 C THR B 30 3062 3198 3349 -4 -130 31 C ATOM 217 O THR A 30 81.354 28.934 37.762 1.00 26.29 O ANISOU 217 O THR B 30 2894 3228 3866 -12 -215 10 O ATOM 218 CB THR A 30 84.424 28.113 37.923 1.00 26.47 C ANISOU 218 CB THR B 30 3190 3306 3558 8 -9 -9 C ATOM 219 OG1 THR A 30 85.815 28.392 37.680 1.00 27.27 O ANISOU 219 OG1 THR B 30 3705 2972 3683 -111 -132 232 O ATOM 220 CG2 THR A 30 84.293 26.632 38.164 1.00 25.70 C ANISOU 220 CG2 THR B 30 3248 3206 3308 27 -41 -30 C ATOM 221 N LEU A 31 81.630 27.142 36.425 1.00 24.88 N ANISOU 221 N LEU B 31 2950 3219 3283 -109 -79 32 N ATOM 222 CA LEU A 31 80.320 26.567 36.665 1.00 25.19 C ANISOU 222 CA LEU B 31 3164 3086 3319 -73 -66 -27 C ATOM 223 C LEU A 31 80.539 25.074 36.827 1.00 25.34 C ANISOU 223 C LEU B 31 3235 2935 3458 -28 -62 59 C ATOM 224 O LEU A 31 80.944 24.390 35.888 1.00 26.34 O ANISOU 224 O LEU B 31 3171 3000 3836 13 -218 51 O ATOM 225 CB LEU A 31 79.369 26.858 35.493 1.00 24.37 C ANISOU 225 CB LEU B 31 3012 3086 3161 -101 -158 -13 C ATOM 226 CG LEU A 31 77.895 26.446 35.615 1.00 24.13 C ANISOU 226 CG LEU B 31 2996 3221 2948 -112 -30 -103 C ATOM 227 CD1 LEU A 31 77.192 27.284 36.709 1.00 24.69 C ANISOU 227 CD1 LEU B 31 3177 3317 2887 -260 0 -22 C ATOM 228 CD2 LEU A 31 77.129 26.551 34.265 1.00 24.10 C ANISOU 228 CD2 LEU B 31 3089 2927 3140 -76 -24 -84 C ATOM 229 N GLY A 32 80.314 24.590 38.037 1.00 28.24 N ANISOU 229 N GLY B 32 3400 3288 4041 -63 92 -75 N ATOM 230 CA GLY A 32 80.672 23.222 38.394 1.00 29.78 C ANISOU 230 CA GLY B 32 3591 3660 4061 -61 72 -22 C ATOM 231 C GLY A 32 82.167 23.034 38.264 1.00 30.24 C ANISOU 231 C GLY B 32 3762 3612 4113 -139 59 80 C ATOM 232 O GLY A 32 82.939 23.821 38.799 1.00 31.47 O ANISOU 232 O GLY B 32 3974 3757 4224 -229 30 120 O ATOM 233 N LYS A 33 82.565 22.029 37.495 1.00 32.50 N ANISOU 233 N LYS B 33 4137 3870 4339 -112 26 13 N ATOM 234 CA LYS A 33 83.981 21.614 37.395 1.00 33.45 C ANISOU 234 CA LYS B 33 4245 4032 4431 -107 28 -31 C ATOM 235 C LYS A 33 84.765 22.259 36.252 1.00 33.67 C ANISOU 235 C LYS B 33 4254 4012 4526 -106 64 -61 C ATOM 236 O LYS A 33 85.934 21.931 36.059 1.00 35.63 O ANISOU 236 O LYS B 33 4457 4163 4915 -216 64 -87 O ATOM 237 CB LYS A 33 84.046 20.096 37.226 1.00 35.56 C ANISOU 237 CB LYS B 33 4473 4269 4768 -138 21 44 C ATOM 238 CG LYS A 33 83.688 19.332 38.494 1.00 38.34 C ANISOU 238 CG LYS B 33 4815 4881 4869 -76 88 -34 C ATOM 239 CD LYS A 33 83.293 17.900 38.126 1.00 38.41 C ANISOU 239 CD LYS B 33 4737 4897 4959 20 64 -92 C ATOM 240 CE LYS A 33 83.176 17.025 39.361 1.00 41.80 C ANISOU 240 CE LYS B 33 5031 5457 5394 7 311 -95 C ATOM 241 NZ LYS A 33 82.225 15.895 39.100 1.00 47.74 N ANISOU 241 NZ LYS B 33 5558 6152 6427 311 75 48 N ATOM 242 N HIS A 34 84.147 23.169 35.499 1.00 31.70 N ANISOU 242 N HIS B 34 4004 3799 4240 -104 -17 -17 N ATOM 243 CA HIS A 34 84.805 23.767 34.363 1.00 30.10 C ANISOU 243 CA HIS B 34 3695 3682 4058 -94 -43 9 C ATOM 244 C HIS A 34 84.843 25.298 34.417 1.00 29.23 C ANISOU 244 C HIS B 34 3598 3558 3951 -54 -117 -34 C ATOM 245 O HIS A 34 83.944 25.945 34.944 1.00 25.94 O ANISOU 245 O HIS B 34 2680 3132 4044 -94 -152 82 O ATOM 246 CB HIS A 34 84.153 23.292 33.069 1.00 30.45 C ANISOU 246 CB HIS B 34 3880 3755 3935 -221 -33 1 C ATOM 247 CG HIS A 34 84.060 21.799 32.960 1.00 33.53 C ANISOU 247 CG HIS B 34 4130 4180 4430 -117 75 63 C ATOM 248 ND1 HIS A 34 83.115 21.061 33.642 1.00 37.51 N ANISOU 248 ND1 HIS B 34 4564 4581 5106 -90 -29 -38 N ATOM 249 CD2 HIS A 34 84.830 20.902 32.294 1.00 36.24 C ANISOU 249 CD2 HIS B 34 4453 4805 4510 -18 -206 -179 C ATOM 250 CE1 HIS A 34 83.294 19.779 33.388 1.00 40.36 C ANISOU 250 CE1 HIS B 34 4633 5106 5593 125 -85 -146 C ATOM 251 NE2 HIS A 34 84.328 19.654 32.574 1.00 40.29 N ANISOU 251 NE2 HIS B 34 4626 5344 5338 -25 -174 -298 N ATOM 252 N LYS A 35 85.909 25.841 33.837 1.00 29.52 N ANISOU 252 N LYS B 35 3602 3577 4034 -60 -59 -64 N ATOM 253 CA LYS A 35 86.133 27.277 33.724 1.00 29.17 C ANISOU 253 CA LYS B 35 3600 3569 3911 -71 -62 -42 C ATOM 254 C LYS A 35 85.892 27.718 32.284 1.00 28.05 C ANISOU 254 C LYS B 35 3403 3349 3905 20 -32 -97 C ATOM 255 O LYS A 35 86.304 27.028 31.325 1.00 28.40 O ANISOU 255 O LYS B 35 3450 3246 4093 -81 -123 -118 O ATOM 256 CB LYS A 35 87.558 27.587 34.158 1.00 30.10 C ANISOU 256 CB LYS B 35 3640 3657 4139 -81 -80 -6 C ATOM 257 CG LYS A 35 87.834 29.013 34.482 1.00 31.74 C ANISOU 257 CG LYS B 35 3924 3805 4329 1 -72 22 C ATOM 258 CD LYS A 35 89.104 29.097 35.330 1.00 32.01 C ANISOU 258 CD LYS B 35 4084 3915 4161 -27 -53 132 C ATOM 259 CE LYS A 35 89.741 30.459 35.248 1.00 33.33 C ANISOU 259 CE LYS B 35 4117 3949 4594 136 -51 131 C ATOM 260 NZ LYS A 35 90.705 30.579 36.386 1.00 35.88 N ANISOU 260 NZ LYS B 35 4446 4619 4565 267 0 123 N ATOM 261 N PHE A 36 85.213 28.857 32.115 1.00 26.61 N ANISOU 261 N PHE B 36 3250 3093 3768 -24 -83 -156 N ATOM 262 CA PHE A 36 84.911 29.395 30.779 1.00 25.43 C ANISOU 262 CA PHE B 36 3095 3161 3405 26 -121 -102 C ATOM 263 C PHE A 36 85.354 30.851 30.640 1.00 24.25 C ANISOU 263 C PHE B 36 2963 3084 3164 18 -94 -72 C ATOM 264 O PHE A 36 85.535 31.559 31.630 1.00 23.85 O ANISOU 264 O PHE B 36 2706 3205 3150 15 -74 -327 O ATOM 265 CB PHE A 36 83.414 29.289 30.438 1.00 24.66 C ANISOU 265 CB PHE B 36 2726 3291 3351 129 -155 -56 C ATOM 266 CG PHE A 36 82.840 27.920 30.662 1.00 22.71 C ANISOU 266 CG PHE B 36 2596 2949 3081 -14 -24 19 C ATOM 267 CD1 PHE A 36 82.902 26.954 29.656 1.00 22.57 C ANISOU 267 CD1 PHE B 36 2882 3062 2632 -106 70 173 C ATOM 268 CD2 PHE A 36 82.279 27.575 31.886 1.00 26.06 C ANISOU 268 CD2 PHE B 36 3014 3563 3324 -84 -6 -189 C ATOM 269 CE1 PHE A 36 82.382 25.665 29.870 1.00 21.70 C ANISOU 269 CE1 PHE B 36 2851 2538 2853 96 -129 -134 C ATOM 270 CE2 PHE A 36 81.764 26.290 32.105 1.00 25.85 C ANISOU 270 CE2 PHE B 36 3211 3178 3432 63 -96 47 C ATOM 271 CZ PHE A 36 81.831 25.339 31.108 1.00 21.52 C ANISOU 271 CZ PHE B 36 2873 2580 2722 -148 128 118 C ATOM 272 N LYS A 37 85.518 31.265 29.391 1.00 23.98 N ANISOU 272 N LYS B 37 2979 3196 2933 -18 -132 -128 N ATOM 273 CA LYS A 37 86.073 32.561 29.021 1.00 25.63 C ANISOU 273 CA LYS B 37 3157 3306 3273 -38 -115 -89 C ATOM 274 C LYS A 37 85.206 33.729 29.501 1.00 26.44 C ANISOU 274 C LYS B 37 3213 3241 3592 -65 -148 -84 C ATOM 275 O LYS A 37 85.744 34.753 29.930 1.00 27.27 O ANISOU 275 O LYS B 37 3157 3227 3975 -131 -289 -158 O ATOM 276 CB LYS A 37 86.195 32.672 27.484 1.00 26.67 C ANISOU 276 CB LYS B 37 3287 3487 3358 -109 -22 109 C ATOM 277 CG LYS A 37 87.429 32.021 26.888 1.00 30.71 C ANISOU 277 CG LYS B 37 3974 3973 3720 -29 -6 4 C ATOM 278 CD LYS A 37 87.580 32.407 25.419 1.00 30.05 C ANISOU 278 CD LYS B 37 4101 3811 3503 -61 -97 -190 C ATOM 279 CE LYS A 37 89.014 32.315 24.918 1.00 35.61 C ANISOU 279 CE LYS B 37 4793 4052 4682 -91 -92 -157 C ATOM 280 NZ LYS A 37 89.358 31.030 24.211 1.00 35.65 N ANISOU 280 NZ LYS B 37 4429 4639 4475 126 -53 -80 N ATOM 281 N LEU A 38 83.883 33.556 29.394 1.00 25.70 N ANISOU 281 N LEU B 38 3136 3087 3539 -88 -120 -28 N ATOM 282 CA LEU A 38 82.881 34.621 29.619 1.00 23.24 C ANISOU 282 CA LEU B 38 2871 2919 3038 9 -146 -170 C ATOM 283 C LEU A 38 81.707 34.069 30.401 1.00 22.38 C ANISOU 283 C LEU B 38 2650 2770 3081 -5 -169 -151 C ATOM 284 O LEU A 38 81.392 32.896 30.257 1.00 21.96 O ANISOU 284 O LEU B 38 2498 2793 3052 -97 -101 -102 O ATOM 285 CB LEU A 38 82.309 35.146 28.285 1.00 23.43 C ANISOU 285 CB LEU B 38 2970 2848 3081 26 -206 -96 C ATOM 286 CG LEU A 38 83.166 36.013 27.376 1.00 27.26 C ANISOU 286 CG LEU B 38 3460 3593 3303 44 58 35 C ATOM 287 CD1 LEU A 38 82.487 36.254 26.011 1.00 25.79 C ANISOU 287 CD1 LEU B 38 3453 3242 3102 57 -84 -29 C ATOM 288 CD2 LEU A 38 83.527 37.353 28.038 1.00 31.40 C ANISOU 288 CD2 LEU B 38 3809 4034 4087 -6 -187 -65 C ATOM 289 N PRO A 39 81.023 34.928 31.196 1.00 20.68 N ANISOU 289 N PRO B 39 2563 2529 2765 45 -174 -164 N ATOM 290 CA PRO A 39 79.786 34.559 31.880 1.00 20.07 C ANISOU 290 CA PRO B 39 2489 2568 2569 65 -130 -150 C ATOM 291 C PRO A 39 78.525 34.709 31.012 1.00 19.54 C ANISOU 291 C PRO B 39 2575 2526 2323 3 -94 -202 C ATOM 292 O PRO A 39 77.513 35.201 31.468 1.00 18.70 O ANISOU 292 O PRO B 39 2909 2759 1434 -69 -398 -216 O ATOM 293 CB PRO A 39 79.762 35.527 33.035 1.00 18.66 C ANISOU 293 CB PRO B 39 2557 2110 2422 28 -142 -126 C ATOM 294 CG PRO A 39 80.278 36.784 32.405 1.00 20.68 C ANISOU 294 CG PRO B 39 2581 2497 2775 -71 -244 -156 C ATOM 295 CD PRO A 39 81.398 36.323 31.505 1.00 19.99 C ANISOU 295 CD PRO B 39 2624 2443 2526 32 -121 -191 C ATOM 296 N VAL A 40 78.601 34.316 29.744 1.00 19.48 N ANISOU 296 N VAL B 40 2381 2660 2361 66 -277 -151 N ATOM 297 CA VAL A 40 77.473 34.360 28.820 1.00 22.19 C ANISOU 297 CA VAL B 40 2639 2860 2932 -33 -159 3 C ATOM 298 C VAL A 40 77.328 33.023 28.078 1.00 22.90 C ANISOU 298 C VAL B 40 2806 2929 2963 -81 -278 -18 C ATOM 299 O VAL A 40 78.312 32.284 27.875 1.00 22.54 O ANISOU 299 O VAL B 40 2787 3002 2772 -308 -208 -13 O ATOM 300 CB VAL A 40 77.595 35.438 27.683 1.00 21.82 C ANISOU 300 CB VAL B 40 2655 2861 2772 34 -93 -31 C ATOM 301 CG1 VAL A 40 77.790 36.885 28.255 1.00 20.29 C ANISOU 301 CG1 VAL B 40 2492 2832 2382 -59 65 10 C ATOM 302 CG2 VAL A 40 78.683 35.099 26.709 1.00 25.55 C ANISOU 302 CG2 VAL B 40 2878 3269 3559 -88 -374 -51 C ATOM 303 N VAL A 41 76.101 32.765 27.651 1.00 21.66 N ANISOU 303 N VAL B 41 2811 2787 2631 -24 -276 -23 N ATOM 304 CA VAL A 41 75.750 31.529 26.969 1.00 22.73 C ANISOU 304 CA VAL B 41 2847 2771 3015 -21 -192 -101 C ATOM 305 C VAL A 41 74.589 31.806 26.009 1.00 23.17 C ANISOU 305 C VAL B 41 2897 2931 2973 -29 -105 -83 C ATOM 306 O VAL A 41 73.593 32.478 26.363 1.00 22.40 O ANISOU 306 O VAL B 41 2776 2742 2991 -40 -284 -162 O ATOM 307 CB VAL A 41 75.433 30.373 27.969 1.00 21.52 C ANISOU 307 CB VAL B 41 2780 2596 2801 -70 -235 43 C ATOM 308 CG1 VAL A 41 74.241 30.694 28.853 1.00 20.31 C ANISOU 308 CG1 VAL B 41 2754 2730 2230 -13 -186 151 C ATOM 309 CG2 VAL A 41 75.223 29.031 27.211 1.00 17.92 C ANISOU 309 CG2 VAL B 41 2765 2752 1289 -9 -156 -17 C ATOM 310 N PRO A 42 74.701 31.301 24.779 1.00 23.74 N ANISOU 310 N PRO B 42 2962 2959 3097 -32 -68 -127 N ATOM 311 CA PRO A 42 73.614 31.455 23.841 1.00 24.45 C ANISOU 311 CA PRO B 42 3043 3090 3157 2 -110 -72 C ATOM 312 C PRO A 42 72.369 30.712 24.278 1.00 23.12 C ANISOU 312 C PRO B 42 2882 3028 2874 38 -169 -66 C ATOM 313 O PRO A 42 72.469 29.671 24.956 1.00 24.66 O ANISOU 313 O PRO B 42 3029 3377 2960 -54 -256 -224 O ATOM 314 CB PRO A 42 74.168 30.839 22.560 1.00 25.85 C ANISOU 314 CB PRO B 42 3258 3210 3352 89 -58 -195 C ATOM 315 CG PRO A 42 75.623 30.812 22.759 1.00 26.54 C ANISOU 315 CG PRO B 42 3502 3206 3373 -133 -50 14 C ATOM 316 CD PRO A 42 75.850 30.606 24.174 1.00 23.96 C ANISOU 316 CD PRO B 42 2775 3157 3170 -66 -140 -232 C ATOM 317 N ALA A 43 71.216 31.250 23.901 1.00 22.26 N ANISOU 317 N ALA B 43 2731 2917 2807 -26 -373 -79 N ATOM 318 CA ALA A 43 69.931 30.584 24.159 1.00 22.76 C ANISOU 318 CA ALA B 43 2841 2997 2808 37 -212 -92 C ATOM 319 C ALA A 43 69.953 29.178 23.573 1.00 23.09 C ANISOU 319 C ALA B 43 2904 3047 2822 95 -186 -142 C ATOM 320 O ALA A 43 70.388 28.979 22.405 1.00 21.48 O ANISOU 320 O ALA B 43 2806 3253 2099 235 -587 102 O ATOM 321 CB ALA A 43 68.775 31.387 23.528 1.00 21.74 C ANISOU 321 CB ALA B 43 2871 2906 2483 36 -401 -70 C ATOM 322 N ASN A 44 69.458 28.215 24.355 1.00 23.92 N ANISOU 322 N ASN B 44 3073 3228 2785 21 -173 103 N ATOM 323 CA ASN A 44 69.404 26.822 23.908 1.00 25.11 C ANISOU 323 CA ASN B 44 2997 3244 3299 -44 -141 -47 C ATOM 324 C ASN A 44 68.190 26.553 23.006 1.00 26.01 C ANISOU 324 C ASN B 44 3082 3340 3460 -43 -260 -9 C ATOM 325 O ASN A 44 67.291 25.799 23.372 1.00 28.08 O ANISOU 325 O ASN B 44 3368 3542 3758 -78 -191 -146 O ATOM 326 CB ASN A 44 69.484 25.854 25.084 1.00 24.17 C ANISOU 326 CB ASN B 44 2969 3099 3115 -11 -192 -101 C ATOM 327 CG ASN A 44 68.403 26.069 26.133 1.00 22.54 C ANISOU 327 CG ASN B 44 2554 3042 2966 -49 23 -243 C ATOM 328 OD1 ASN A 44 68.057 27.203 26.499 1.00 22.60 O ANISOU 328 OD1 ASN B 44 2787 3071 2729 47 -182 -347 O ATOM 329 ND2 ASN A 44 67.869 24.969 26.631 1.00 20.57 N ANISOU 329 ND2 ASN B 44 2744 2594 2478 -102 -221 -265 N ATOM 330 N MET A 45 68.189 27.193 21.840 1.00 27.55 N ANISOU 330 N MET B 45 3312 3592 3563 -30 -135 0 N ATOM 331 CA MET A 45 67.108 27.094 20.832 1.00 31.30 C ANISOU 331 CA MET B 45 3993 4012 3888 -3 -94 127 C ATOM 332 C MET A 45 67.703 26.910 19.451 1.00 31.35 C ANISOU 332 C MET B 45 4027 4038 3845 4 -45 59 C ATOM 333 O MET A 45 68.780 27.445 19.164 1.00 28.93 O ANISOU 333 O MET B 45 3627 4113 3252 242 -209 145 O ATOM 334 CB MET A 45 66.280 28.373 20.742 1.00 32.34 C ANISOU 334 CB MET B 45 4145 4146 3993 21 -72 204 C ATOM 335 CG MET A 45 65.708 28.869 22.014 1.00 34.33 C ANISOU 335 CG MET B 45 4484 4333 4224 -102 4 -2 C ATOM 336 SD MET A 45 65.233 30.614 21.880 1.00 37.65 S ANISOU 336 SD MET B 45 4812 4964 4526 -379 -206 154 S ATOM 337 CE MET A 45 63.898 30.605 23.074 1.00 38.65 C ANISOU 337 CE MET B 45 4891 4871 4922 -79 -28 -98 C ATOM 338 N GLN A 46 66.962 26.213 18.582 1.00 32.96 N ANISOU 338 N GLN B 46 4258 4224 4040 66 -144 69 N ATOM 339 CA GLN A 46 67.464 25.888 17.244 1.00 35.26 C ANISOU 339 CA GLN B 46 4529 4521 4345 40 -112 36 C ATOM 340 C GLN A 46 67.614 27.086 16.291 1.00 34.37 C ANISOU 340 C GLN B 46 4402 4336 4320 68 -149 110 C ATOM 341 O GLN A 46 68.332 27.011 15.301 1.00 34.24 O ANISOU 341 O GLN B 46 4502 4398 4109 163 -227 196 O ATOM 342 CB GLN A 46 66.643 24.760 16.590 1.00 36.32 C ANISOU 342 CB GLN B 46 4637 4670 4490 91 -105 43 C ATOM 343 CG GLN A 46 65.210 25.097 16.271 1.00 39.86 C ANISOU 343 CG GLN B 46 5167 4930 5048 0 -127 147 C ATOM 344 CD GLN A 46 64.651 24.293 15.080 1.00 41.11 C ANISOU 344 CD GLN B 46 5278 5234 5108 129 -149 220 C ATOM 345 OE1 GLN A 46 65.408 23.707 14.274 1.00 50.04 O ANISOU 345 OE1 GLN B 46 6472 6268 6273 -250 -214 -147 O ATOM 346 NE2 GLN A 46 63.320 24.274 14.962 1.00 45.68 N ANISOU 346 NE2 GLN B 46 5924 5411 6019 -29 -164 54 N ATOM 347 N THR A 47 66.937 28.182 16.600 1.00 34.53 N ANISOU 347 N THR B 47 4382 4296 4440 68 -155 137 N ATOM 348 CA THR A 47 67.113 29.438 15.883 1.00 34.61 C ANISOU 348 CA THR B 47 4469 4409 4272 19 -71 102 C ATOM 349 C THR A 47 68.412 30.184 16.255 1.00 34.95 C ANISOU 349 C THR B 47 4382 4477 4420 25 6 36 C ATOM 350 O THR A 47 68.771 31.157 15.596 1.00 36.52 O ANISOU 350 O THR B 47 4425 4730 4718 49 -27 10 O ATOM 351 CB THR A 47 65.915 30.362 16.163 1.00 36.26 C ANISOU 351 CB THR B 47 4620 4661 4496 -8 9 148 C ATOM 352 OG1 THR A 47 65.725 30.513 17.582 1.00 40.02 O ANISOU 352 OG1 THR B 47 5124 5188 4895 -76 -150 -81 O ATOM 353 CG2 THR A 47 64.656 29.781 15.565 1.00 36.90 C ANISOU 353 CG2 THR B 47 4619 4605 4792 36 52 102 C ATOM 354 N ILE A 48 69.111 29.722 17.298 1.00 33.48 N ANISOU 354 N ILE B 48 4110 4324 4287 36 -96 57 N ATOM 355 CA ILE A 48 70.307 30.401 17.835 1.00 32.37 C ANISOU 355 CA ILE B 48 4087 4161 4049 -31 -67 42 C ATOM 356 C ILE A 48 71.558 29.514 17.800 1.00 31.72 C ANISOU 356 C ILE B 48 4021 4194 3834 61 -134 -58 C ATOM 357 O ILE A 48 72.630 29.960 17.412 1.00 32.06 O ANISOU 357 O ILE B 48 4110 4276 3795 111 -334 -12 O ATOM 358 CB ILE A 48 69.998 30.881 19.293 1.00 31.99 C ANISOU 358 CB ILE B 48 4034 4082 4037 -60 7 51 C ATOM 359 CG1 ILE A 48 68.769 31.805 19.308 1.00 30.18 C ANISOU 359 CG1 ILE B 48 3876 4073 3515 -73 -128 -40 C ATOM 360 CG2 ILE A 48 71.202 31.550 19.962 1.00 31.94 C ANISOU 360 CG2 ILE B 48 3913 4133 4087 -54 -25 25 C ATOM 361 CD1 ILE A 48 68.936 33.115 18.556 1.00 32.09 C ANISOU 361 CD1 ILE B 48 3837 4315 4041 117 -84 -12 C ATOM 362 N ILE A 49 71.440 28.264 18.221 1.00 31.82 N ANISOU 362 N ILE B 49 4018 4206 3864 19 -200 -14 N ATOM 363 CA ILE A 49 72.593 27.368 18.274 1.00 31.51 C ANISOU 363 CA ILE B 49 3992 4055 3923 17 -108 17 C ATOM 364 C ILE A 49 72.394 26.106 17.426 1.00 32.10 C ANISOU 364 C ILE B 49 4163 4122 3909 6 -191 12 C ATOM 365 O ILE A 49 71.274 25.656 17.214 1.00 30.63 O ANISOU 365 O ILE B 49 4077 4021 3540 21 -367 7 O ATOM 366 CB ILE A 49 72.975 26.985 19.744 1.00 30.79 C ANISOU 366 CB ILE B 49 3806 3902 3988 97 -116 -24 C ATOM 367 CG1 ILE A 49 74.291 26.191 19.773 1.00 30.63 C ANISOU 367 CG1 ILE B 49 3723 3934 3979 -36 -23 120 C ATOM 368 CG2 ILE A 49 71.822 26.253 20.495 1.00 27.62 C ANISOU 368 CG2 ILE B 49 3616 3582 3297 71 -92 -27 C ATOM 369 CD1 ILE A 49 74.990 26.252 21.067 1.00 30.08 C ANISOU 369 CD1 ILE B 49 3633 4043 3751 -1 -124 24 C ATOM 370 N ASP A 50 73.508 25.567 16.935 1.00 32.74 N ANISOU 370 N ASP B 50 4264 4233 3939 -48 -178 -45 N ATOM 371 CA ASP A 50 73.513 24.272 16.265 1.00 33.96 C ANISOU 371 CA ASP B 50 4281 4382 4240 -32 -121 -13 C ATOM 372 C ASP A 50 74.818 23.539 16.574 1.00 35.00 C ANISOU 372 C ASP B 50 4434 4494 4368 -65 -144 16 C ATOM 373 O ASP A 50 75.635 24.023 17.357 1.00 34.16 O ANISOU 373 O ASP B 50 4417 4618 3942 -42 -233 -117 O ATOM 374 CB ASP A 50 73.272 24.436 14.742 1.00 33.98 C ANISOU 374 CB ASP B 50 4366 4427 4116 -36 -128 37 C ATOM 375 CG ASP A 50 74.400 25.188 14.007 1.00 36.10 C ANISOU 375 CG ASP B 50 4455 4663 4597 -80 -94 20 C ATOM 376 OD1 ASP A 50 75.528 25.343 14.524 1.00 38.58 O ANISOU 376 OD1 ASP B 50 5079 4889 4688 64 -464 122 O ATOM 377 OD2 ASP A 50 74.154 25.613 12.859 1.00 39.10 O ANISOU 377 OD2 ASP B 50 4963 5237 4656 109 -116 26 O ATOM 378 N GLU A 51 75.038 22.389 15.937 1.00 35.35 N ANISOU 378 N GLU B 51 4387 4568 4476 -3 -185 50 N ATOM 379 CA GLU A 51 76.219 21.583 16.240 1.00 34.69 C ANISOU 379 CA GLU B 51 4339 4439 4402 -24 -140 -4 C ATOM 380 C GLU A 51 77.541 22.244 15.858 1.00 34.27 C ANISOU 380 C GLU B 51 4299 4421 4298 -79 -195 -22 C ATOM 381 O GLU A 51 78.521 22.075 16.575 1.00 33.38 O ANISOU 381 O GLU B 51 4374 4189 4119 -29 -448 22 O ATOM 382 CB GLU A 51 76.128 20.201 15.597 1.00 36.41 C ANISOU 382 CB GLU B 51 4538 4628 4667 -26 -112 30 C ATOM 383 CG GLU A 51 74.951 19.365 16.098 1.00 38.32 C ANISOU 383 CG GLU B 51 4789 4841 4927 62 -128 -206 C ATOM 384 CD GLU A 51 73.644 19.652 15.348 1.00 43.48 C ANISOU 384 CD GLU B 51 5607 5550 5361 -129 -91 141 C ATOM 385 OE1 GLU A 51 73.576 20.650 14.589 1.00 44.68 O ANISOU 385 OE1 GLU B 51 5458 5967 5551 84 -232 81 O ATOM 386 OE2 GLU A 51 72.675 18.875 15.541 1.00 50.08 O ANISOU 386 OE2 GLU B 51 6205 6238 6584 109 -298 -3 O ATOM 387 N ARG A 52 77.582 22.954 14.726 1.00 34.21 N ANISOU 387 N ARG B 52 4167 4431 4397 -17 -174 -25 N ATOM 388 CA ARG A 52 78.808 23.659 14.316 1.00 33.98 C ANISOU 388 CA ARG B 52 4210 4365 4334 -38 -209 -31 C ATOM 389 C ARG A 52 79.134 24.773 15.320 1.00 32.52 C ANISOU 389 C ARG B 52 4159 4120 4077 -52 -269 33 C ATOM 390 O ARG A 52 80.277 24.921 15.736 1.00 33.21 O ANISOU 390 O ARG B 52 4225 4146 4245 -163 -512 32 O ATOM 391 CB ARG A 52 78.683 24.323 12.941 1.00 36.00 C ANISOU 391 CB ARG B 52 4576 4575 4525 -38 -33 23 C ATOM 392 CG ARG A 52 78.321 23.429 11.759 1.00 39.91 C ANISOU 392 CG ARG B 52 5064 5198 4901 -35 -234 29 C ATOM 393 CD ARG A 52 79.246 22.241 11.596 1.00 45.86 C ANISOU 393 CD ARG B 52 5680 5592 6152 -125 129 -11 C ATOM 394 NE ARG A 52 79.035 21.623 10.277 1.00 42.89 N ANISOU 394 NE ARG B 52 5340 5710 5244 -192 -349 20 N ATOM 395 CZ ARG A 52 79.286 20.354 9.966 1.00 45.82 C ANISOU 395 CZ ARG B 52 5677 5927 5804 -76 -70 -29 C ATOM 396 NH1 ARG A 52 79.769 19.509 10.878 1.00 45.14 N ANISOU 396 NH1 ARG B 52 5534 5767 5850 -2 -21 12 N ATOM 397 NH2 ARG A 52 79.040 19.934 8.718 1.00 46.94 N ANISOU 397 NH2 ARG B 52 5985 5840 6008 -114 -181 162 N ATOM 398 N ILE A 53 78.135 25.583 15.662 1.00 30.41 N ANISOU 398 N ILE B 53 3892 3912 3750 22 -141 8 N ATOM 399 CA ILE A 53 78.349 26.649 16.658 1.00 30.08 C ANISOU 399 CA ILE B 53 3789 3881 3758 -30 -74 -50 C ATOM 400 C ILE A 53 78.796 26.070 18.028 1.00 28.95 C ANISOU 400 C ILE B 53 3684 3767 3546 -74 -165 -81 C ATOM 401 O ILE A 53 79.747 26.580 18.633 1.00 30.52 O ANISOU 401 O ILE B 53 3701 3980 3913 -101 -274 -186 O ATOM 402 CB ILE A 53 77.126 27.580 16.788 1.00 30.01 C ANISOU 402 CB ILE B 53 3839 3827 3735 27 -3 -62 C ATOM 403 CG1 ILE A 53 76.936 28.376 15.492 1.00 29.50 C ANISOU 403 CG1 ILE B 53 3737 3938 3533 -184 -112 -32 C ATOM 404 CG2 ILE A 53 77.316 28.558 17.961 1.00 30.51 C ANISOU 404 CG2 ILE B 53 3814 3974 3802 12 -109 -48 C ATOM 405 CD1 ILE A 53 75.577 29.009 15.310 1.00 29.72 C ANISOU 405 CD1 ILE B 53 3984 3768 3539 -42 -120 -135 C ATOM 406 N ALA A 54 78.166 24.985 18.477 1.00 28.63 N ANISOU 406 N ALA B 54 3700 3762 3412 -59 -201 -111 N ATOM 407 CA ALA A 54 78.544 24.311 19.750 1.00 28.89 C ANISOU 407 CA ALA B 54 3672 3720 3585 -65 -113 -46 C ATOM 408 C ALA A 54 79.985 23.788 19.785 1.00 30.15 C ANISOU 408 C ALA B 54 3853 3853 3749 -67 -107 -43 C ATOM 409 O ALA A 54 80.677 23.818 20.843 1.00 28.38 O ANISOU 409 O ALA B 54 3398 3666 3716 -97 -225 -43 O ATOM 410 CB ALA A 54 77.562 23.175 20.051 1.00 28.55 C ANISOU 410 CB ALA B 54 3664 3769 3414 -66 -145 -80 C ATOM 411 N THR A 55 80.436 23.294 18.635 1.00 31.34 N ANISOU 411 N THR B 55 4017 3883 4006 -131 -143 -31 N ATOM 412 CA THR A 55 81.819 22.819 18.490 1.00 31.30 C ANISOU 412 CA THR B 55 4050 3854 3989 -57 -191 -87 C ATOM 413 C THR A 55 82.833 23.982 18.544 1.00 30.63 C ANISOU 413 C THR B 55 3985 3818 3832 -84 -255 -76 C ATOM 414 O THR A 55 83.864 23.884 19.211 1.00 29.55 O ANISOU 414 O THR B 55 3858 3660 3709 -46 -616 1 O ATOM 415 CB THR A 55 81.985 22.019 17.182 1.00 33.25 C ANISOU 415 CB THR B 55 4247 4072 4311 -37 -213 -50 C ATOM 416 OG1 THR A 55 81.000 20.966 17.133 1.00 34.95 O ANISOU 416 OG1 THR B 55 3972 4565 4740 25 -388 -241 O ATOM 417 CG2 THR A 55 83.382 21.421 17.112 1.00 31.57 C ANISOU 417 CG2 THR B 55 4118 3822 4054 -153 -177 -102 C ATOM 418 N TYR A 56 82.536 25.060 17.832 1.00 30.93 N ANISOU 418 N TYR B 56 4010 3908 3833 -53 -210 -138 N ATOM 419 CA TYR A 56 83.329 26.283 17.919 1.00 30.42 C ANISOU 419 CA TYR B 56 4024 3770 3762 -24 -159 -101 C ATOM 420 C TYR A 56 83.432 26.726 19.370 1.00 29.21 C ANISOU 420 C TYR B 56 3906 3524 3668 -71 -302 -246 C ATOM 421 O TYR A 56 84.514 27.032 19.871 1.00 29.04 O ANISOU 421 O TYR B 56 4159 3344 3528 -200 -516 -655 O ATOM 422 CB TYR A 56 82.727 27.425 17.102 1.00 33.53 C ANISOU 422 CB TYR B 56 4513 4118 4107 -281 -84 -183 C ATOM 423 CG TYR A 56 83.477 28.717 17.345 1.00 34.11 C ANISOU 423 CG TYR B 56 4180 4295 4484 54 -150 -186 C ATOM 424 CD1 TYR A 56 84.681 28.977 16.689 1.00 36.33 C ANISOU 424 CD1 TYR B 56 4491 4571 4741 71 -23 -203 C ATOM 425 CD2 TYR A 56 83.014 29.656 18.271 1.00 36.24 C ANISOU 425 CD2 TYR B 56 4523 4662 4584 99 -130 -313 C ATOM 426 CE1 TYR A 56 85.406 30.142 16.941 1.00 36.49 C ANISOU 426 CE1 TYR B 56 4467 4491 4905 124 -23 -216 C ATOM 427 CE2 TYR A 56 83.732 30.830 18.533 1.00 35.54 C ANISOU 427 CE2 TYR B 56 4255 4610 4638 114 -178 -247 C ATOM 428 CZ TYR A 56 84.927 31.068 17.850 1.00 37.86 C ANISOU 428 CZ TYR B 56 4576 4698 5111 270 -260 -182 C ATOM 429 OH TYR A 56 85.636 32.226 18.082 1.00 38.53 O ANISOU 429 OH TYR B 56 4576 4746 5314 370 -273 -317 O ATOM 430 N LEU A 57 82.295 26.767 20.050 1.00 28.11 N ANISOU 430 N LEU B 57 3681 3363 3633 68 -220 -176 N ATOM 431 CA LEU A 57 82.262 27.276 21.410 1.00 27.73 C ANISOU 431 CA LEU B 57 3612 3410 3511 40 -168 -86 C ATOM 432 C LEU A 57 83.077 26.416 22.348 1.00 26.59 C ANISOU 432 C LEU B 57 3371 3245 3486 -27 -245 -114 C ATOM 433 O LEU A 57 83.930 26.915 23.090 1.00 25.84 O ANISOU 433 O LEU B 57 2969 3226 3620 62 -594 -314 O ATOM 434 CB LEU A 57 80.791 27.448 21.901 1.00 25.88 C ANISOU 434 CB LEU B 57 3516 3245 3069 107 -139 -54 C ATOM 435 CG LEU A 57 80.067 28.605 21.194 1.00 27.97 C ANISOU 435 CG LEU B 57 3473 3353 3798 83 -190 -24 C ATOM 436 CD1 LEU A 57 78.602 28.669 21.566 1.00 29.10 C ANISOU 436 CD1 LEU B 57 3650 3643 3760 -30 -114 -229 C ATOM 437 CD2 LEU A 57 80.713 29.967 21.487 1.00 26.28 C ANISOU 437 CD2 LEU B 57 3143 3543 3298 31 26 -227 C ATOM 438 N ALA A 58 82.853 25.110 22.319 1.00 26.58 N ANISOU 438 N ALA B 58 3417 3302 3377 67 -223 -34 N ATOM 439 CA ALA A 58 83.560 24.218 23.236 1.00 28.30 C ANISOU 439 CA ALA B 58 3603 3550 3597 -8 -120 -17 C ATOM 440 C ALA A 58 85.066 24.191 22.950 1.00 28.89 C ANISOU 440 C ALA B 58 3624 3590 3760 -25 -108 -48 C ATOM 441 O ALA A 58 85.859 24.116 23.891 1.00 29.27 O ANISOU 441 O ALA B 58 3605 3403 4112 -60 -241 -126 O ATOM 442 CB ALA A 58 82.973 22.821 23.184 1.00 28.64 C ANISOU 442 CB ALA B 58 3645 3582 3655 -70 -17 -50 C ATOM 443 N GLU A 59 85.432 24.261 21.658 1.00 29.74 N ANISOU 443 N GLU B 59 3798 3610 3889 86 -61 -181 N ATOM 444 CA GLU A 59 86.849 24.292 21.210 1.00 30.77 C ANISOU 444 CA GLU B 59 3897 3834 3958 -2 -92 -74 C ATOM 445 C GLU A 59 87.631 25.508 21.680 1.00 32.50 C ANISOU 445 C GLU B 59 4101 3898 4348 51 -77 -72 C ATOM 446 O GLU A 59 88.857 25.490 21.708 1.00 33.99 O ANISOU 446 O GLU B 59 4375 3973 4565 -12 -89 -115 O ATOM 447 CB GLU A 59 86.916 24.269 19.694 1.00 28.51 C ANISOU 447 CB GLU B 59 3653 3497 3682 39 1 -173 C ATOM 448 CG GLU A 59 86.753 22.883 19.133 1.00 30.49 C ANISOU 448 CG GLU B 59 3895 4068 3622 -58 -103 16 C ATOM 449 CD GLU A 59 86.894 22.839 17.621 1.00 33.91 C ANISOU 449 CD GLU B 59 4401 4503 3980 57 -79 -61 C ATOM 450 OE1 GLU A 59 86.879 23.917 16.979 1.00 37.37 O ANISOU 450 OE1 GLU B 59 4454 5044 4700 -18 -8 -1 O ATOM 451 OE2 GLU A 59 87.020 21.703 17.088 1.00 38.10 O ANISOU 451 OE2 GLU B 59 4691 5104 4679 -126 -336 -71 O ATOM 452 N ASN A 60 86.908 26.551 22.059 1.00 32.80 N ANISOU 452 N ASN B 60 3982 4036 4442 7 -64 -28 N ATOM 453 CA ASN A 60 87.499 27.805 22.496 1.00 31.56 C ANISOU 453 CA ASN B 60 3973 3895 4122 -1 -72 -32 C ATOM 454 C ASN A 60 87.143 28.177 23.937 1.00 31.28 C ANISOU 454 C ASN B 60 3872 3864 4149 -40 -100 -93 C ATOM 455 O ASN A 60 87.362 29.310 24.342 1.00 32.51 O ANISOU 455 O ASN B 60 3974 3917 4461 83 -207 -198 O ATOM 456 CB ASN A 60 87.069 28.886 21.509 1.00 32.37 C ANISOU 456 CB ASN B 60 4016 4017 4262 82 -18 31 C ATOM 457 CG ASN A 60 87.801 28.777 20.196 1.00 35.29 C ANISOU 457 CG ASN B 60 4846 4236 4324 6 -162 9 C ATOM 458 OD1 ASN A 60 89.003 29.023 20.152 1.00 36.51 O ANISOU 458 OD1 ASN B 60 5268 4245 4360 181 -96 -311 O ATOM 459 ND2 ASN A 60 87.090 28.402 19.113 1.00 34.92 N ANISOU 459 ND2 ASN B 60 4804 4193 4268 -7 -278 -10 N ATOM 460 N ASN A 61 86.630 27.210 24.701 1.00 29.85 N ANISOU 460 N ASN B 61 3707 3623 4009 -127 -140 -106 N ATOM 461 CA ASN A 61 86.351 27.358 26.132 1.00 29.93 C ANISOU 461 CA ASN B 61 3760 3637 3975 -92 -34 -64 C ATOM 462 C ASN A 61 85.247 28.370 26.506 1.00 28.91 C ANISOU 462 C ASN B 61 3627 3489 3866 -147 -94 -50 C ATOM 463 O ASN A 61 85.306 28.989 27.589 1.00 29.08 O ANISOU 463 O ASN B 61 3688 3213 4148 -71 -172 -53 O ATOM 464 CB ASN A 61 87.622 27.669 26.933 1.00 30.98 C ANISOU 464 CB ASN B 61 3962 3760 4047 -14 -63 -52 C ATOM 465 CG ASN A 61 88.631 26.558 26.866 1.00 37.23 C ANISOU 465 CG ASN B 61 4661 4496 4986 -233 23 -60 C ATOM 466 OD1 ASN A 61 89.677 26.706 26.236 1.00 41.92 O ANISOU 466 OD1 ASN B 61 5637 4889 5400 -127 -257 -254 O ATOM 467 ND2 ASN A 61 88.331 25.436 27.512 1.00 41.19 N ANISOU 467 ND2 ASN B 61 4889 5132 5627 -94 69 -218 N ATOM 468 N TYR A 62 84.260 28.487 25.616 1.00 26.98 N ANISOU 468 N TYR B 62 3335 3340 3576 -66 -107 -65 N ATOM 469 CA TYR A 62 82.998 29.218 25.849 1.00 25.88 C ANISOU 469 CA TYR B 62 3280 3250 3301 35 -48 -168 C ATOM 470 C TYR A 62 81.940 28.178 26.244 1.00 26.08 C ANISOU 470 C TYR B 62 3375 3073 3459 58 -151 -154 C ATOM 471 O TYR A 62 81.954 27.062 25.736 1.00 26.21 O ANISOU 471 O TYR B 62 3468 2647 3843 41 -288 -275 O ATOM 472 CB TYR A 62 82.534 29.947 24.583 1.00 25.91 C ANISOU 472 CB TYR B 62 3157 3294 3393 -49 -84 -157 C ATOM 473 CG TYR A 62 83.451 31.057 24.103 1.00 25.63 C ANISOU 473 CG TYR B 62 3230 3242 3263 146 -123 -178 C ATOM 474 CD1 TYR A 62 83.483 32.277 24.759 1.00 27.86 C ANISOU 474 CD1 TYR B 62 3266 3496 3821 21 -69 -345 C ATOM 475 CD2 TYR A 62 84.269 30.884 22.971 1.00 26.71 C ANISOU 475 CD2 TYR B 62 3066 3469 3612 -34 -41 -186 C ATOM 476 CE1 TYR A 62 84.327 33.321 24.327 1.00 27.83 C ANISOU 476 CE1 TYR B 62 3325 3573 3677 177 -196 -254 C ATOM 477 CE2 TYR A 62 85.104 31.910 22.519 1.00 27.06 C ANISOU 477 CE2 TYR B 62 3370 3360 3549 99 -200 -282 C ATOM 478 CZ TYR A 62 85.123 33.143 23.206 1.00 28.64 C ANISOU 478 CZ TYR B 62 3286 3798 3796 217 -178 -367 C ATOM 479 OH TYR A 62 85.957 34.177 22.801 1.00 25.69 O ANISOU 479 OH TYR B 62 3080 3554 3126 -120 -343 -530 O ATOM 480 N PHE A 63 81.091 28.518 27.216 1.00 25.34 N ANISOU 480 N PHE B 63 3212 3097 3319 -13 -128 -248 N ATOM 481 CA PHE A 63 79.966 27.653 27.621 1.00 23.84 C ANISOU 481 CA PHE B 63 2998 3054 3006 32 -83 -122 C ATOM 482 C PHE A 63 78.907 27.616 26.510 1.00 21.87 C ANISOU 482 C PHE B 63 2790 2817 2700 10 -33 -264 C ATOM 483 O PHE A 63 78.681 28.598 25.856 1.00 20.69 O ANISOU 483 O PHE B 63 2811 2776 2274 -20 -240 -52 O ATOM 484 CB PHE A 63 79.395 28.149 28.980 1.00 24.20 C ANISOU 484 CB PHE B 63 2962 2941 3291 46 -12 -229 C ATOM 485 CG PHE A 63 78.363 27.246 29.610 1.00 24.62 C ANISOU 485 CG PHE B 63 3193 3136 3024 -98 -130 -218 C ATOM 486 CD1 PHE A 63 78.565 25.871 29.744 1.00 25.59 C ANISOU 486 CD1 PHE B 63 3453 3305 2964 -144 85 -117 C ATOM 487 CD2 PHE A 63 77.183 27.777 30.104 1.00 22.42 C ANISOU 487 CD2 PHE B 63 2749 2736 3032 -325 117 205 C ATOM 488 CE1 PHE A 63 77.614 25.058 30.301 1.00 24.21 C ANISOU 488 CE1 PHE B 63 3006 2930 3261 11 -186 89 C ATOM 489 CE2 PHE A 63 76.234 26.969 30.707 1.00 22.70 C ANISOU 489 CE2 PHE B 63 3001 2915 2709 -97 -65 35 C ATOM 490 CZ PHE A 63 76.451 25.609 30.814 1.00 25.05 C ANISOU 490 CZ PHE B 63 3140 3176 3199 52 35 41 C ATOM 491 N TYR A 64 78.305 26.451 26.269 1.00 21.51 N ANISOU 491 N TYR B 64 2678 2882 2611 -6 -125 -214 N ATOM 492 CA TYR A 64 77.133 26.346 25.416 1.00 22.04 C ANISOU 492 CA TYR B 64 2767 2849 2757 30 -110 -195 C ATOM 493 C TYR A 64 76.167 25.339 26.052 1.00 22.21 C ANISOU 493 C TYR B 64 2715 2807 2915 -22 -161 -130 C ATOM 494 O TYR A 64 76.525 24.567 26.937 1.00 23.42 O ANISOU 494 O TYR B 64 2551 2924 3422 138 -160 -247 O ATOM 495 CB TYR A 64 77.514 25.879 23.989 1.00 22.19 C ANISOU 495 CB TYR B 64 2840 2832 2756 49 -160 -267 C ATOM 496 CG TYR A 64 77.771 24.383 23.954 1.00 21.80 C ANISOU 496 CG TYR B 64 2836 2732 2714 50 22 -371 C ATOM 497 CD1 TYR A 64 76.727 23.476 23.751 1.00 23.83 C ANISOU 497 CD1 TYR B 64 3088 2996 2969 83 -351 -79 C ATOM 498 CD2 TYR A 64 79.025 23.872 24.206 1.00 18.46 C ANISOU 498 CD2 TYR B 64 2695 2984 1333 -57 -300 222 C ATOM 499 CE1 TYR A 64 76.945 22.109 23.794 1.00 22.66 C ANISOU 499 CE1 TYR B 64 2859 2910 2837 -30 -49 -112 C ATOM 500 CE2 TYR A 64 79.251 22.495 24.267 1.00 22.01 C ANISOU 500 CE2 TYR B 64 2708 2963 2689 15 -124 152 C ATOM 501 CZ TYR A 64 78.214 21.626 24.042 1.00 24.05 C ANISOU 501 CZ TYR B 64 2940 3046 3153 39 -73 -26 C ATOM 502 OH TYR A 64 78.454 20.274 24.083 1.00 25.50 O ANISOU 502 OH TYR B 64 2849 3120 3717 -36 -117 -32 O ATOM 503 N ILE A 65 74.926 25.395 25.613 1.00 22.93 N ANISOU 503 N ILE B 65 2708 2931 3070 -75 -200 -162 N ATOM 504 CA ILE A 65 73.904 24.398 25.947 1.00 23.30 C ANISOU 504 CA ILE B 65 2792 2917 3142 -22 -154 -201 C ATOM 505 C ILE A 65 73.168 24.146 24.646 1.00 22.60 C ANISOU 505 C ILE B 65 2805 2920 2863 -24 -127 -233 C ATOM 506 O ILE A 65 72.537 25.036 24.072 1.00 21.33 O ANISOU 506 O ILE B 65 2496 2716 2892 -105 -627 -551 O ATOM 507 CB ILE A 65 72.859 24.890 26.981 1.00 22.34 C ANISOU 507 CB ILE B 65 2919 2851 2715 -7 -48 -196 C ATOM 508 CG1 ILE A 65 73.498 25.225 28.330 1.00 22.56 C ANISOU 508 CG1 ILE B 65 2814 2790 2965 -4 -262 -134 C ATOM 509 CG2 ILE A 65 71.720 23.895 27.093 1.00 19.24 C ANISOU 509 CG2 ILE B 65 2116 2684 2508 -417 -82 -136 C ATOM 510 CD1 ILE A 65 72.554 26.030 29.269 1.00 23.07 C ANISOU 510 CD1 ILE B 65 2764 2720 3281 105 -160 -232 C ATOM 511 N MET A 66 73.239 22.909 24.180 1.00 25.28 N ANISOU 511 N MET B 66 3060 3247 3297 -29 -77 -106 N ATOM 512 CA MET A 66 72.582 22.530 22.955 1.00 26.26 C ANISOU 512 CA MET B 66 3171 3386 3422 15 -131 -63 C ATOM 513 C MET A 66 71.078 22.424 23.182 1.00 26.30 C ANISOU 513 C MET B 66 3052 3425 3513 -43 -151 -9 C ATOM 514 O MET A 66 70.625 22.091 24.286 1.00 25.42 O ANISOU 514 O MET B 66 2985 3174 3499 33 -398 -11 O ATOM 515 CB MET A 66 73.157 21.191 22.487 1.00 28.00 C ANISOU 515 CB MET B 66 3301 3513 3822 -60 -99 -40 C ATOM 516 CG MET A 66 72.836 20.825 21.088 1.00 34.01 C ANISOU 516 CG MET B 66 4042 4446 4431 -136 -226 63 C ATOM 517 SD MET A 66 73.124 22.039 19.825 1.00 31.20 S ANISOU 517 SD MET B 66 3133 4118 4603 503 -1120 -662 S ATOM 518 CE MET A 66 72.359 21.148 18.492 1.00 33.42 C ANISOU 518 CE MET B 66 4416 4046 4235 37 -313 72 C ATOM 519 N HIS A 67 70.324 22.714 22.128 1.00 27.19 N ANISOU 519 N HIS B 67 3256 3583 3491 3 -267 54 N ATOM 520 CA HIS A 67 68.869 22.550 22.112 1.00 28.82 C ANISOU 520 CA HIS B 67 3563 3642 3742 37 -178 -27 C ATOM 521 C HIS A 67 68.463 21.059 21.926 1.00 29.47 C ANISOU 521 C HIS B 67 3628 3746 3824 100 -171 6 C ATOM 522 O HIS A 67 69.303 20.194 21.578 1.00 28.38 O ANISOU 522 O HIS B 67 3441 3720 3622 277 -371 68 O ATOM 523 CB HIS A 67 68.252 23.404 20.983 1.00 29.63 C ANISOU 523 CB HIS B 67 3509 3703 4046 43 -67 -64 C ATOM 524 CG HIS A 67 68.631 22.953 19.599 1.00 33.72 C ANISOU 524 CG HIS B 67 4323 4371 4117 124 -71 84 C ATOM 525 ND1 HIS A 67 68.100 21.828 19.003 1.00 34.11 N ANISOU 525 ND1 HIS B 67 4297 4391 4272 131 -108 154 N ATOM 526 CD2 HIS A 67 69.518 23.458 18.711 1.00 34.59 C ANISOU 526 CD2 HIS B 67 4237 4470 4433 143 -102 -58 C ATOM 527 CE1 HIS A 67 68.634 21.670 17.806 1.00 32.70 C ANISOU 527 CE1 HIS B 67 4199 4053 4172 8 -145 72 C ATOM 528 NE2 HIS A 67 69.493 22.651 17.601 1.00 33.87 N ANISOU 528 NE2 HIS B 67 4275 4275 4319 51 -194 102 N ATOM 529 N ARG A 68 67.176 20.778 22.145 1.00 29.79 N ANISOU 529 N ARG B 68 3785 3828 3704 74 -194 7 N ATOM 530 CA ARG A 68 66.652 19.411 22.029 1.00 31.53 C ANISOU 530 CA ARG B 68 3912 3969 4096 65 -145 -75 C ATOM 531 C ARG A 68 65.592 19.285 20.924 1.00 32.34 C ANISOU 531 C ARG B 68 4058 4039 4189 -58 -268 -150 C ATOM 532 O ARG A 68 64.670 18.469 21.021 1.00 32.72 O ANISOU 532 O ARG B 68 4341 3914 4176 -26 -448 -219 O ATOM 533 CB ARG A 68 66.097 18.944 23.371 1.00 31.82 C ANISOU 533 CB ARG B 68 3919 3921 4250 26 -3 9 C ATOM 534 CG ARG A 68 65.038 19.862 23.957 1.00 30.98 C ANISOU 534 CG ARG B 68 3827 3799 4143 225 -256 -18 C ATOM 535 CD ARG A 68 64.472 19.252 25.167 1.00 31.63 C ANISOU 535 CD ARG B 68 3921 4104 3992 162 -89 51 C ATOM 536 NE ARG A 68 63.547 20.134 25.876 1.00 34.80 N ANISOU 536 NE ARG B 68 4274 4355 4594 115 -201 -99 N ATOM 537 CZ ARG A 68 62.234 19.942 26.031 1.00 34.62 C ANISOU 537 CZ ARG B 68 4235 4310 4609 -70 -102 101 C ATOM 538 NH1 ARG A 68 61.601 18.885 25.529 1.00 32.39 N ANISOU 538 NH1 ARG B 68 4089 3917 4299 0 11 145 N ATOM 539 NH2 ARG A 68 61.542 20.825 26.735 1.00 34.59 N ANISOU 539 NH2 ARG B 68 4400 4467 4274 -155 -135 -34 N ATOM 540 N PHE A 69 65.735 20.056 19.861 1.00 35.02 N ANISOU 540 N PHE B 69 4347 4462 4494 -65 -170 -93 N ATOM 541 CA PHE A 69 64.795 19.985 18.754 1.00 35.93 C ANISOU 541 CA PHE B 69 4552 4515 4582 -30 -97 26 C ATOM 542 C PHE A 69 64.892 18.667 17.972 1.00 38.37 C ANISOU 542 C PHE B 69 4792 4801 4985 -37 -144 17 C ATOM 543 O PHE A 69 63.893 18.188 17.419 1.00 40.91 O ANISOU 543 O PHE B 69 5137 5159 5246 68 -213 131 O ATOM 544 CB PHE A 69 64.995 21.144 17.793 1.00 41.27 C ANISOU 544 CB PHE B 69 4854 5408 5416 140 -116 -565 C ATOM 545 CG PHE A 69 63.888 21.271 16.782 1.00 37.85 C ANISOU 545 CG PHE B 69 4923 4761 4694 -141 -40 128 C ATOM 546 CD1 PHE A 69 62.647 21.795 17.157 1.00 42.48 C ANISOU 546 CD1 PHE B 69 5722 5213 5202 -106 -24 -52 C ATOM 547 CD2 PHE A 69 64.068 20.854 15.464 1.00 43.04 C ANISOU 547 CD2 PHE B 69 5534 5511 5306 -163 -101 54 C ATOM 548 CE1 PHE A 69 61.605 21.905 16.228 1.00 42.28 C ANISOU 548 CE1 PHE B 69 5690 5043 5330 -179 17 184 C ATOM 549 CE2 PHE A 69 63.029 20.953 14.533 1.00 41.52 C ANISOU 549 CE2 PHE B 69 5605 5178 4993 -29 -22 259 C ATOM 550 CZ PHE A 69 61.801 21.488 14.917 1.00 41.49 C ANISOU 550 CZ PHE B 69 5452 5086 5224 -41 -37 195 C ATOM 551 N GLN A 70 66.082 18.077 17.929 1.00 37.65 N ANISOU 551 N GLN B 70 4670 4757 4877 -42 -111 -86 N ATOM 552 CA GLN A 70 66.245 16.762 17.286 1.00 36.65 C ANISOU 552 CA GLN B 70 4599 4705 4620 8 -106 -22 C ATOM 553 C GLN A 70 66.742 15.770 18.296 1.00 34.75 C ANISOU 553 C GLN B 70 4314 4399 4488 17 -247 -45 C ATOM 554 O GLN A 70 67.883 15.340 18.226 1.00 34.14 O ANISOU 554 O GLN B 70 4293 4244 4433 48 -268 -106 O ATOM 555 CB GLN A 70 67.198 16.858 16.111 1.00 37.00 C ANISOU 555 CB GLN B 70 4701 4693 4661 14 -150 -92 C ATOM 556 CG GLN A 70 66.627 17.704 14.982 1.00 38.84 C ANISOU 556 CG GLN B 70 5060 4832 4865 -134 31 -19 C ATOM 557 CD GLN A 70 67.588 17.824 13.822 1.00 41.55 C ANISOU 557 CD GLN B 70 5391 5327 5067 -34 87 -139 C ATOM 558 OE1 GLN A 70 68.738 18.265 13.992 1.00 48.71 O ANISOU 558 OE1 GLN B 70 6432 5818 6256 199 -51 37 O ATOM 559 NE2 GLN A 70 67.129 17.443 12.628 1.00 47.80 N ANISOU 559 NE2 GLN B 70 6179 6171 5810 9 -235 236 N ATOM 560 N PRO A 71 65.868 15.397 19.249 1.00 32.99 N ANISOU 560 N PRO B 71 4026 4239 4266 98 -216 18 N ATOM 561 CA PRO A 71 66.295 14.695 20.427 1.00 33.40 C ANISOU 561 CA PRO B 71 4109 4227 4351 35 -173 26 C ATOM 562 C PRO A 71 66.961 13.375 20.167 1.00 32.88 C ANISOU 562 C PRO B 71 4021 4146 4323 27 -170 -7 C ATOM 563 O PRO A 71 67.699 12.907 21.029 1.00 32.26 O ANISOU 563 O PRO B 71 3595 4077 4585 16 -338 -37 O ATOM 564 CB PRO A 71 64.991 14.481 21.205 1.00 32.95 C ANISOU 564 CB PRO B 71 4074 4137 4309 40 -82 15 C ATOM 565 CG PRO A 71 63.922 14.620 20.214 1.00 31.92 C ANISOU 565 CG PRO B 71 4038 3952 4135 5 -206 -51 C ATOM 566 CD PRO A 71 64.406 15.611 19.248 1.00 33.09 C ANISOU 566 CD PRO B 71 4078 4252 4240 -6 -133 -31 C ATOM 567 N GLU A 72 66.679 12.778 19.006 1.00 33.70 N ANISOU 567 N GLU B 72 4169 4240 4392 -4 -145 -118 N ATOM 568 CA GLU A 72 67.244 11.481 18.651 1.00 35.00 C ANISOU 568 CA GLU B 72 4374 4386 4535 -12 -160 -64 C ATOM 569 C GLU A 72 68.768 11.559 18.418 1.00 34.96 C ANISOU 569 C GLU B 72 4387 4333 4560 -34 -128 -123 C ATOM 570 O GLU A 72 69.455 10.553 18.496 1.00 34.93 O ANISOU 570 O GLU B 72 4354 4339 4576 -16 -199 -204 O ATOM 571 CB GLU A 72 66.505 10.892 17.431 1.00 35.53 C ANISOU 571 CB GLU B 72 4495 4409 4595 -2 -173 -40 C ATOM 572 CG GLU A 72 66.860 11.482 16.059 1.00 38.13 C ANISOU 572 CG GLU B 72 4792 4871 4823 -48 51 -6 C ATOM 573 CD GLU A 72 66.137 12.774 15.704 1.00 39.18 C ANISOU 573 CD GLU B 72 4980 5105 4802 -162 46 -60 C ATOM 574 OE1 GLU A 72 65.390 13.318 16.558 1.00 37.19 O ANISOU 574 OE1 GLU B 72 4698 4775 4655 -171 -106 -90 O ATOM 575 OE2 GLU A 72 66.335 13.242 14.545 1.00 38.26 O ANISOU 575 OE2 GLU B 72 4953 5152 4430 213 -85 -119 O ATOM 576 N LYS A 73 69.270 12.767 18.177 1.00 35.25 N ANISOU 576 N LYS B 73 4396 4390 4607 -44 -164 -198 N ATOM 577 CA LYS A 73 70.694 13.019 17.943 1.00 35.75 C ANISOU 577 CA LYS B 73 4488 4475 4619 -9 -119 -89 C ATOM 578 C LYS A 73 71.550 13.251 19.183 1.00 34.71 C ANISOU 578 C LYS B 73 4317 4344 4527 60 -170 -105 C ATOM 579 O LYS A 73 72.765 13.336 19.064 1.00 35.32 O ANISOU 579 O LYS B 73 4207 4432 4781 52 -365 -196 O ATOM 580 CB LYS A 73 70.848 14.229 17.018 1.00 36.98 C ANISOU 580 CB LYS B 73 4531 4702 4815 -18 -57 -225 C ATOM 581 CG LYS A 73 70.242 14.017 15.642 1.00 39.01 C ANISOU 581 CG LYS B 73 4905 4847 5069 -19 -102 13 C ATOM 582 CD LYS A 73 70.357 15.270 14.791 1.00 38.60 C ANISOU 582 CD LYS B 73 4921 4880 4863 -46 -49 -48 C ATOM 583 CE LYS A 73 70.088 14.987 13.327 1.00 42.43 C ANISOU 583 CE LYS B 73 5517 5411 5191 58 9 66 C ATOM 584 NZ LYS A 73 70.263 16.210 12.475 1.00 46.24 N ANISOU 584 NZ LYS B 73 5818 6057 5694 -2 276 -16 N ATOM 585 N ARG A 74 70.940 13.349 20.359 1.00 34.01 N ANISOU 585 N ARG B 74 4250 4170 4501 116 -109 -105 N ATOM 586 CA ARG A 74 71.663 13.720 21.582 1.00 33.43 C ANISOU 586 CA ARG B 74 4174 4195 4332 42 -78 -106 C ATOM 587 C ARG A 74 72.648 12.672 22.082 1.00 33.89 C ANISOU 587 C ARG B 74 4222 4195 4457 53 -208 -155 C ATOM 588 O ARG A 74 73.714 13.017 22.587 1.00 31.80 O ANISOU 588 O ARG B 74 3970 3946 4163 39 -484 -259 O ATOM 589 CB ARG A 74 70.672 14.082 22.699 1.00 33.26 C ANISOU 589 CB ARG B 74 4126 4120 4388 97 -64 -4 C ATOM 590 CG ARG A 74 69.806 15.296 22.366 1.00 32.46 C ANISOU 590 CG ARG B 74 3990 4029 4314 59 0 -76 C ATOM 591 CD ARG A 74 68.720 15.529 23.405 1.00 32.59 C ANISOU 591 CD ARG B 74 3971 4098 4313 -32 -48 -73 C ATOM 592 NE ARG A 74 67.754 14.422 23.449 1.00 34.27 N ANISOU 592 NE ARG B 74 4077 4190 4752 74 -284 -273 N ATOM 593 CZ ARG A 74 66.793 14.274 24.357 1.00 35.33 C ANISOU 593 CZ ARG B 74 4334 4495 4591 191 -168 -112 C ATOM 594 NH1 ARG A 74 66.629 15.163 25.329 1.00 33.65 N ANISOU 594 NH1 ARG B 74 4170 4055 4557 108 -222 24 N ATOM 595 NH2 ARG A 74 65.982 13.212 24.294 1.00 32.68 N ANISOU 595 NH2 ARG B 74 4049 4045 4320 110 -178 -88 N ATOM 596 N ILE A 75 72.306 11.387 21.975 1.00 34.66 N ANISOU 596 N ILE B 75 4223 4313 4631 46 -158 -71 N ATOM 597 CA ILE A 75 73.227 10.357 22.444 1.00 34.83 C ANISOU 597 CA ILE B 75 4239 4434 4558 66 -76 -59 C ATOM 598 C ILE A 75 74.503 10.368 21.591 1.00 34.20 C ANISOU 598 C ILE B 75 4030 4351 4613 1 -192 -26 C ATOM 599 O ILE A 75 75.597 10.280 22.151 1.00 35.05 O ANISOU 599 O ILE B 75 4033 4300 4982 -139 -361 -84 O ATOM 600 CB ILE A 75 72.581 8.941 22.467 1.00 35.35 C ANISOU 600 CB ILE B 75 4232 4479 4719 85 -7 -37 C ATOM 601 CG1 ILE A 75 71.440 8.918 23.473 1.00 37.80 C ANISOU 601 CG1 ILE B 75 4635 4782 4945 125 -13 -48 C ATOM 602 CG2 ILE A 75 73.583 7.889 22.888 1.00 35.37 C ANISOU 602 CG2 ILE B 75 4338 4419 4682 72 -69 10 C ATOM 603 CD1 ILE A 75 70.414 7.856 23.178 1.00 37.59 C ANISOU 603 CD1 ILE B 75 4639 4763 4877 122 0 -20 C ATOM 604 N SER A 76 74.366 10.519 20.266 1.00 33.21 N ANISOU 604 N SER B 76 3927 4218 4472 70 -128 -53 N ATOM 605 CA SER A 76 75.543 10.590 19.386 1.00 32.77 C ANISOU 605 CA SER B 76 3918 4158 4373 102 -148 -42 C ATOM 606 C SER A 76 76.333 11.891 19.628 1.00 31.23 C ANISOU 606 C SER B 76 3818 3850 4199 48 -245 -16 C ATOM 607 O SER A 76 77.573 11.845 19.784 1.00 30.36 O ANISOU 607 O SER B 76 3743 3609 4183 57 -410 -353 O ATOM 608 CB SER A 76 75.184 10.413 17.906 1.00 34.57 C ANISOU 608 CB SER B 76 4342 4296 4495 89 -56 8 C ATOM 609 OG SER A 76 74.862 11.633 17.235 1.00 40.75 O ANISOU 609 OG SER B 76 4582 5454 5444 247 -143 -59 O ATOM 610 N PHE A 77 75.616 13.018 19.708 1.00 28.68 N ANISOU 610 N PHE B 77 3533 3577 3785 82 -209 -26 N ATOM 611 CA PHE A 77 76.226 14.310 20.071 1.00 29.35 C ANISOU 611 CA PHE B 77 3578 3669 3903 -24 -189 -79 C ATOM 612 C PHE A 77 77.107 14.181 21.311 1.00 27.83 C ANISOU 612 C PHE B 77 3211 3567 3795 -53 -380 -119 C ATOM 613 O PHE A 77 78.262 14.606 21.294 1.00 29.71 O ANISOU 613 O PHE B 77 3456 3608 4222 -8 -627 -279 O ATOM 614 CB PHE A 77 75.152 15.395 20.250 1.00 28.39 C ANISOU 614 CB PHE B 77 3329 3719 3738 133 -305 -6 C ATOM 615 CG PHE A 77 75.696 16.750 20.666 1.00 28.46 C ANISOU 615 CG PHE B 77 3517 3619 3677 92 -147 -86 C ATOM 616 CD1 PHE A 77 76.091 17.697 19.723 1.00 26.79 C ANISOU 616 CD1 PHE B 77 3152 3465 3560 3 -292 -285 C ATOM 617 CD2 PHE A 77 75.802 17.062 22.010 1.00 28.16 C ANISOU 617 CD2 PHE B 77 3533 3532 3633 211 -240 -26 C ATOM 618 CE1 PHE A 77 76.585 18.956 20.133 1.00 27.29 C ANISOU 618 CE1 PHE B 77 3743 3548 3076 174 -303 -79 C ATOM 619 CE2 PHE A 77 76.287 18.307 22.421 1.00 29.13 C ANISOU 619 CE2 PHE B 77 3445 3765 3857 61 -179 -63 C ATOM 620 CZ PHE A 77 76.677 19.237 21.505 1.00 24.16 C ANISOU 620 CZ PHE B 77 3155 3134 2888 -339 -239 -218 C ATOM 621 N ILE A 78 76.592 13.598 22.381 1.00 27.81 N ANISOU 621 N ILE B 78 3104 3523 3937 -97 -317 -46 N ATOM 622 CA ILE A 78 77.390 13.466 23.604 1.00 29.75 C ANISOU 622 CA ILE B 78 3561 3745 3995 -88 -213 -48 C ATOM 623 C ILE A 78 78.650 12.670 23.296 1.00 30.75 C ANISOU 623 C ILE B 78 3614 3767 4302 -116 -252 0 C ATOM 624 O ILE A 78 79.770 13.114 23.539 1.00 30.50 O ANISOU 624 O ILE B 78 3242 3800 4546 -292 -481 -32 O ATOM 625 CB ILE A 78 76.624 12.787 24.754 1.00 29.03 C ANISOU 625 CB ILE B 78 3485 3471 4071 -14 -170 -42 C ATOM 626 CG1 ILE A 78 75.437 13.660 25.190 1.00 30.72 C ANISOU 626 CG1 ILE B 78 3641 3927 4104 -80 -98 -106 C ATOM 627 CG2 ILE A 78 77.518 12.568 25.970 1.00 28.52 C ANISOU 627 CG2 ILE B 78 3326 3602 3907 -51 -149 -137 C ATOM 628 CD1 ILE A 78 74.207 12.850 25.534 1.00 31.48 C ANISOU 628 CD1 ILE B 78 3903 3925 4130 -86 -72 -244 C ATOM 629 N ARG A 79 78.448 11.509 22.696 1.00 31.79 N ANISOU 629 N ARG B 79 3729 3941 4409 -125 -239 -58 N ATOM 630 CA ARG A 79 79.542 10.570 22.465 1.00 32.32 C ANISOU 630 CA ARG B 79 3862 4121 4296 -75 -235 -34 C ATOM 631 C ARG A 79 80.650 11.234 21.661 1.00 30.72 C ANISOU 631 C ARG B 79 3604 3966 4099 -88 -371 -10 C ATOM 632 O ARG A 79 81.834 11.097 21.961 1.00 31.29 O ANISOU 632 O ARG B 79 3566 3985 4336 -38 -572 162 O ATOM 633 CB ARG A 79 78.989 9.333 21.740 1.00 32.22 C ANISOU 633 CB ARG B 79 3725 4304 4213 -119 -311 -22 C ATOM 634 CG ARG A 79 80.027 8.237 21.529 1.00 34.29 C ANISOU 634 CG ARG B 79 4063 4312 4653 -168 -140 -19 C ATOM 635 CD ARG A 79 79.410 6.900 21.025 1.00 36.16 C ANISOU 635 CD ARG B 79 4248 4816 4673 31 -343 29 C ATOM 636 NE ARG A 79 78.345 6.315 21.859 1.00 39.78 N ANISOU 636 NE ARG B 79 5135 4956 5021 11 -222 -103 N ATOM 637 CZ ARG A 79 77.086 6.103 21.460 1.00 41.58 C ANISOU 637 CZ ARG B 79 5427 5094 5276 -40 -15 -35 C ATOM 638 NH1 ARG A 79 76.670 6.462 20.243 1.00 43.33 N ANISOU 638 NH1 ARG B 79 5753 5693 5017 -76 -19 -119 N ATOM 639 NH2 ARG A 79 76.221 5.529 22.284 1.00 40.84 N ANISOU 639 NH2 ARG B 79 5336 5286 4893 -130 -25 -165 N ATOM 640 N ASP A 80 80.247 11.983 20.652 1.00 29.32 N ANISOU 640 N ASP B 80 3328 3861 3948 -97 -408 -119 N ATOM 641 CA ASP A 80 81.173 12.591 19.742 1.00 30.36 C ANISOU 641 CA ASP B 80 3590 3889 4057 -10 -287 -90 C ATOM 642 C ASP A 80 81.945 13.770 20.363 1.00 30.50 C ANISOU 642 C ASP B 80 3641 3802 4143 15 -338 -163 C ATOM 643 O ASP A 80 83.172 13.859 20.227 1.00 28.52 O ANISOU 643 O ASP B 80 3240 3717 3877 159 -591 -293 O ATOM 644 CB ASP A 80 80.414 12.985 18.490 1.00 28.80 C ANISOU 644 CB ASP B 80 3455 3607 3878 -8 -302 -57 C ATOM 645 CG ASP A 80 79.967 11.757 17.679 1.00 30.21 C ANISOU 645 CG ASP B 80 3837 3795 3847 97 -1 192 C ATOM 646 OD1 ASP A 80 80.199 10.615 18.146 1.00 33.90 O ANISOU 646 OD1 ASP B 80 3801 4288 4791 78 -375 -395 O ATOM 647 OD2 ASP A 80 79.396 11.941 16.590 1.00 26.26 O ANISOU 647 OD2 ASP B 80 3598 4338 2040 702 -1034 -276 O ATOM 648 N MET A 81 81.245 14.650 21.079 1.00 31.14 N ANISOU 648 N MET B 81 3644 3992 4194 42 -315 -254 N ATOM 649 CA MET A 81 81.922 15.757 21.741 1.00 31.12 C ANISOU 649 CA MET B 81 3804 3919 4101 44 -280 -110 C ATOM 650 C MET A 81 82.987 15.204 22.641 1.00 30.65 C ANISOU 650 C MET B 81 3708 3881 4055 -84 -352 -168 C ATOM 651 O MET A 81 84.145 15.643 22.558 1.00 29.73 O ANISOU 651 O MET B 81 3489 3639 4166 -272 -482 -225 O ATOM 652 CB MET A 81 80.936 16.650 22.521 1.00 30.49 C ANISOU 652 CB MET B 81 3592 3904 4085 58 -283 -48 C ATOM 653 CG MET A 81 79.979 17.434 21.623 1.00 29.12 C ANISOU 653 CG MET B 81 3677 3626 3759 -88 -417 -90 C ATOM 654 SD MET A 81 80.757 18.669 20.542 1.00 33.44 S ANISOU 654 SD MET B 81 4151 4088 4464 -140 -651 -319 S ATOM 655 CE MET A 81 80.924 20.064 21.653 1.00 31.64 C ANISOU 655 CE MET B 81 4078 3820 4123 16 -295 -55 C ATOM 656 N GLN A 82 82.620 14.215 23.456 1.00 31.90 N ANISOU 656 N GLN B 82 3897 3969 4251 -69 -360 -136 N ATOM 657 CA GLN A 82 83.458 13.755 24.548 1.00 34.40 C ANISOU 657 CA GLN B 82 4244 4339 4485 -67 -176 -18 C ATOM 658 C GLN A 82 84.688 13.025 24.020 1.00 36.74 C ANISOU 658 C GLN B 82 4580 4526 4854 -122 -164 -3 C ATOM 659 O GLN A 82 85.702 12.950 24.711 1.00 37.76 O ANISOU 659 O GLN B 82 4710 4471 5163 -250 -240 -64 O ATOM 660 CB GLN A 82 82.676 12.855 25.506 1.00 35.06 C ANISOU 660 CB GLN B 82 4371 4411 4536 -90 -196 -40 C ATOM 661 CG GLN A 82 81.488 13.543 26.214 1.00 34.60 C ANISOU 661 CG GLN B 82 4133 4419 4593 -193 -142 -122 C ATOM 662 CD GLN A 82 80.960 12.776 27.427 1.00 35.28 C ANISOU 662 CD GLN B 82 4303 4516 4586 -85 -97 1 C ATOM 663 OE1 GLN A 82 80.927 11.531 27.447 1.00 33.96 O ANISOU 663 OE1 GLN B 82 4024 4286 4592 -63 -262 -63 O ATOM 664 NE2 GLN A 82 80.528 13.521 28.453 1.00 36.40 N ANISOU 664 NE2 GLN B 82 4300 4568 4961 -264 -167 -28 N ATOM 665 N SER A 83 84.569 12.489 22.806 1.00 37.45 N ANISOU 665 N SER B 83 4747 4648 4833 -135 -134 -137 N ATOM 666 CA SER A 83 85.656 11.785 22.133 1.00 37.90 C ANISOU 666 CA SER B 83 4780 4678 4942 -77 -127 -90 C ATOM 667 C SER A 83 86.674 12.765 21.527 1.00 39.28 C ANISOU 667 C SER B 83 4910 4855 5161 -14 -52 -92 C ATOM 668 O SER A 83 87.841 12.399 21.303 1.00 40.55 O ANISOU 668 O SER B 83 5001 4874 5529 86 -121 -115 O ATOM 669 CB SER A 83 85.093 10.887 21.038 1.00 38.41 C ANISOU 669 CB SER B 83 4840 4731 5021 -79 -135 -59 C ATOM 670 OG SER A 83 84.788 11.629 19.870 1.00 40.76 O ANISOU 670 OG SER B 83 4954 5030 5502 -2 -67 -164 O ATOM 671 N ARG A 84 86.226 13.992 21.256 1.00 38.65 N ANISOU 671 N ARG B 84 4877 4784 5022 -37 -50 -55 N ATOM 672 CA ARG A 84 87.111 15.089 20.854 1.00 38.51 C ANISOU 672 CA ARG B 84 4851 4744 5035 -21 -118 -57 C ATOM 673 C ARG A 84 87.608 15.860 22.076 1.00 36.72 C ANISOU 673 C ARG B 84 4638 4500 4813 -81 -76 -83 C ATOM 674 O ARG A 84 88.220 16.920 21.942 1.00 36.53 O ANISOU 674 O ARG B 84 4762 4202 4914 -49 -307 30 O ATOM 675 CB ARG A 84 86.393 16.036 19.899 1.00 37.98 C ANISOU 675 CB ARG B 84 4781 4712 4936 58 11 -84 C ATOM 676 CG ARG A 84 86.161 15.464 18.530 1.00 43.42 C ANISOU 676 CG ARG B 84 5567 5361 5570 25 -264 -71 C ATOM 677 CD ARG A 84 85.095 16.251 17.756 1.00 44.60 C ANISOU 677 CD ARG B 84 5679 5640 5626 -49 -61 108 C ATOM 678 NE ARG A 84 85.645 17.219 16.799 1.00 51.66 N ANISOU 678 NE ARG B 84 6518 6615 6493 29 224 -108 N ATOM 679 CZ ARG A 84 84.906 17.989 15.993 1.00 51.30 C ANISOU 679 CZ ARG B 84 6479 6549 6463 -124 240 92 C ATOM 680 NH1 ARG A 84 83.570 17.922 16.033 1.00 53.95 N ANISOU 680 NH1 ARG B 84 6973 6698 6825 113 27 -23 N ATOM 681 NH2 ARG A 84 85.498 18.837 15.141 1.00 51.91 N ANISOU 681 NH2 ARG B 84 6731 6525 6467 -1 157 41 N ATOM 682 N GLY A 85 87.358 15.331 23.267 1.00 35.54 N ANISOU 682 N GLY B 85 4510 4235 4756 -184 -145 -11 N ATOM 683 CA GLY A 85 87.785 15.995 24.489 1.00 35.78 C ANISOU 683 CA GLY B 85 4498 4291 4805 -140 -138 -37 C ATOM 684 C GLY A 85 87.022 17.291 24.754 1.00 35.75 C ANISOU 684 C GLY B 85 4417 4247 4919 -124 -246 27 C ATOM 685 O GLY A 85 87.548 18.206 25.383 1.00 36.46 O ANISOU 685 O GLY B 85 4728 4056 5069 -218 -527 -37 O ATOM 686 N LEU A 86 85.786 17.370 24.265 1.00 34.48 N ANISOU 686 N LEU B 86 4211 4090 4798 -138 -219 -62 N ATOM 687 CA LEU A 86 84.971 18.575 24.434 1.00 33.05 C ANISOU 687 CA LEU B 86 4064 4061 4431 -11 -159 -82 C ATOM 688 C LEU A 86 83.812 18.289 25.413 1.00 32.59 C ANISOU 688 C LEU B 86 3990 4042 4350 -15 -146 -151 C ATOM 689 O LEU A 86 83.353 17.156 25.533 1.00 32.82 O ANISOU 689 O LEU B 86 3980 4047 4442 -50 -261 -307 O ATOM 690 CB LEU A 86 84.456 19.040 23.078 1.00 31.57 C ANISOU 690 CB LEU B 86 3726 4001 4268 84 -129 -25 C ATOM 691 CG LEU A 86 85.512 19.375 22.028 1.00 31.88 C ANISOU 691 CG LEU B 86 3890 3971 4249 130 -284 75 C ATOM 692 CD1 LEU A 86 84.870 19.836 20.727 1.00 32.26 C ANISOU 692 CD1 LEU B 86 4019 3914 4323 87 -107 -59 C ATOM 693 CD2 LEU A 86 86.466 20.476 22.557 1.00 31.15 C ANISOU 693 CD2 LEU B 86 3830 3575 4429 61 -40 13 C ATOM 694 N ILE A 87 83.375 19.327 26.124 1.00 31.46 N ANISOU 694 N ILE B 87 3915 3926 4110 -17 -159 -186 N ATOM 695 CA ILE A 87 82.235 19.240 27.035 1.00 30.66 C ANISOU 695 CA ILE B 87 3736 3859 4052 -12 -146 -37 C ATOM 696 C ILE A 87 80.973 18.946 26.247 1.00 27.65 C ANISOU 696 C ILE B 87 3234 3581 3692 -132 -214 -125 C ATOM 697 O ILE A 87 80.767 19.489 25.172 1.00 25.66 O ANISOU 697 O ILE B 87 2712 3443 3594 -378 -470 -293 O ATOM 698 CB ILE A 87 82.069 20.583 27.827 1.00 31.01 C ANISOU 698 CB ILE B 87 3935 3904 3940 -47 -164 -57 C ATOM 699 CG1 ILE A 87 83.084 20.627 28.980 1.00 31.39 C ANISOU 699 CG1 ILE B 87 3919 4044 3962 72 -202 39 C ATOM 700 CG2 ILE A 87 80.689 20.729 28.412 1.00 32.10 C ANISOU 700 CG2 ILE B 87 3991 3960 4244 -39 -151 -117 C ATOM 701 CD1 ILE A 87 83.599 21.971 29.234 1.00 32.06 C ANISOU 701 CD1 ILE B 87 4007 4161 4012 -1 -91 45 C ATOM 702 N ALA A 88 80.141 18.076 26.806 1.00 27.71 N ANISOU 702 N ALA B 88 3178 3495 3854 -134 -340 -91 N ATOM 703 CA ALA A 88 78.800 17.787 26.277 1.00 27.62 C ANISOU 703 CA ALA B 88 3250 3524 3718 -108 -131 15 C ATOM 704 C ALA A 88 77.770 18.396 27.224 1.00 25.86 C ANISOU 704 C ALA B 88 3019 3311 3493 -54 -120 -25 C ATOM 705 O ALA A 88 77.707 18.038 28.389 1.00 26.42 O ANISOU 705 O ALA B 88 2862 3440 3734 -217 -219 -163 O ATOM 706 CB ALA A 88 78.570 16.285 26.168 1.00 28.33 C ANISOU 706 CB ALA B 88 3273 3565 3926 -66 -216 160 C ATOM 707 N SER A 89 76.976 19.311 26.693 1.00 25.72 N ANISOU 707 N SER B 89 2935 3282 3555 -9 -186 -72 N ATOM 708 CA SER A 89 75.987 20.065 27.444 1.00 25.15 C ANISOU 708 CA SER B 89 3055 3199 3300 -9 -137 -69 C ATOM 709 C SER A 89 74.696 19.997 26.623 1.00 24.25 C ANISOU 709 C SER B 89 2879 3164 3170 2 -173 -44 C ATOM 710 O SER A 89 74.647 20.506 25.506 1.00 21.04 O ANISOU 710 O SER B 89 2647 2955 2392 -81 -655 -119 O ATOM 711 CB SER A 89 76.470 21.520 27.591 1.00 24.66 C ANISOU 711 CB SER B 89 2884 3153 3332 -2 -339 -144 C ATOM 712 OG SER A 89 75.512 22.391 28.227 1.00 23.96 O ANISOU 712 OG SER B 89 2539 2574 3990 -118 -436 -318 O ATOM 713 N ILE A 90 73.668 19.353 27.174 1.00 24.22 N ANISOU 713 N ILE B 90 2932 3006 3263 -111 -258 -94 N ATOM 714 CA ILE A 90 72.461 19.071 26.393 1.00 25.69 C ANISOU 714 CA ILE B 90 3188 3099 3471 -52 -137 -80 C ATOM 715 C ILE A 90 71.234 19.574 27.142 1.00 24.91 C ANISOU 715 C ILE B 90 3054 3108 3301 -120 -175 -126 C ATOM 716 O ILE A 90 71.364 19.985 28.271 1.00 26.28 O ANISOU 716 O ILE B 90 3167 3268 3548 -18 -25 -164 O ATOM 717 CB ILE A 90 72.301 17.568 26.116 1.00 24.76 C ANISOU 717 CB ILE B 90 3150 2922 3334 -111 -247 -85 C ATOM 718 CG1 ILE A 90 72.198 16.785 27.444 1.00 25.94 C ANISOU 718 CG1 ILE B 90 2938 3363 3554 -117 -169 -52 C ATOM 719 CG2 ILE A 90 73.455 17.063 25.205 1.00 24.92 C ANISOU 719 CG2 ILE B 90 3181 2847 3437 50 -275 -121 C ATOM 720 CD1 ILE A 90 71.422 15.492 27.377 1.00 26.87 C ANISOU 720 CD1 ILE B 90 3472 3293 3442 71 -122 -57 C ATOM 721 N SER A 91 70.075 19.527 26.478 1.00 26.23 N ANISOU 721 N SER B 91 3046 3252 3666 -112 -249 -77 N ATOM 722 CA SER A 91 68.783 19.868 27.068 1.00 25.83 C ANISOU 722 CA SER B 91 3171 3199 3442 -5 -76 -51 C ATOM 723 C SER A 91 67.876 18.636 27.131 1.00 26.70 C ANISOU 723 C SER B 91 3234 3442 3465 42 -46 -111 C ATOM 724 O SER A 91 67.924 17.768 26.256 1.00 26.51 O ANISOU 724 O SER B 91 3051 3248 3773 93 -75 -265 O ATOM 725 CB SER A 91 68.093 20.978 26.238 1.00 25.77 C ANISOU 725 CB SER B 91 3156 3241 3392 15 -76 -131 C ATOM 726 OG SER A 91 68.878 22.144 26.206 1.00 25.64 O ANISOU 726 OG SER B 91 2897 3352 3492 -2 -170 -48 O ATOM 727 N VAL A 92 67.057 18.562 28.175 1.00 26.61 N ANISOU 727 N VAL B 92 3178 3419 3512 -23 -89 -140 N ATOM 728 CA VAL A 92 66.023 17.525 28.294 1.00 26.92 C ANISOU 728 CA VAL B 92 3340 3437 3448 26 -69 -103 C ATOM 729 C VAL A 92 64.703 18.136 28.752 1.00 27.60 C ANISOU 729 C VAL B 92 3381 3491 3612 56 -62 -136 C ATOM 730 O VAL A 92 64.679 19.246 29.298 1.00 26.02 O ANISOU 730 O VAL B 92 3635 3311 2938 113 -498 -403 O ATOM 731 CB VAL A 92 66.416 16.410 29.286 1.00 26.52 C ANISOU 731 CB VAL B 92 3280 3418 3377 33 -23 -30 C ATOM 732 CG1 VAL A 92 67.742 15.805 28.921 1.00 28.52 C ANISOU 732 CG1 VAL B 92 3590 3655 3591 23 80 -125 C ATOM 733 CG2 VAL A 92 66.481 16.924 30.718 1.00 27.44 C ANISOU 733 CG2 VAL B 92 3350 3475 3600 89 -125 -68 C ATOM 734 N GLY A 93 63.620 17.402 28.515 1.00 28.18 N ANISOU 734 N GLY B 93 3483 3563 3659 54 -112 80 N ATOM 735 CA GLY A 93 62.288 17.747 29.003 1.00 28.93 C ANISOU 735 CA GLY B 93 3599 3591 3801 32 -129 -20 C ATOM 736 C GLY A 93 61.914 16.886 30.192 1.00 29.37 C ANISOU 736 C GLY B 93 3638 3673 3847 71 -55 10 C ATOM 737 O GLY A 93 62.793 16.364 30.916 1.00 31.21 O ANISOU 737 O GLY B 93 3800 3686 4371 244 33 -58 O ATOM 738 N VAL A 94 60.613 16.721 30.418 1.00 29.12 N ANISOU 738 N VAL B 94 3600 3702 3760 61 -166 89 N ATOM 739 CA VAL A 94 60.150 16.010 31.608 1.00 31.43 C ANISOU 739 CA VAL B 94 3868 3942 4129 78 -73 -71 C ATOM 740 C VAL A 94 59.145 14.870 31.346 1.00 33.20 C ANISOU 740 C VAL B 94 4065 4127 4422 98 -60 -72 C ATOM 741 O VAL A 94 58.688 14.233 32.299 1.00 33.22 O ANISOU 741 O VAL B 94 4112 3970 4538 160 -33 -192 O ATOM 742 CB VAL A 94 59.571 16.993 32.680 1.00 30.99 C ANISOU 742 CB VAL B 94 3872 3908 3993 137 -81 -89 C ATOM 743 CG1 VAL A 94 60.584 18.110 32.992 1.00 28.50 C ANISOU 743 CG1 VAL B 94 3496 3656 3673 -58 -324 -360 C ATOM 744 CG2 VAL A 94 58.253 17.577 32.244 1.00 31.21 C ANISOU 744 CG2 VAL B 94 3612 4077 4167 97 11 -98 C ATOM 745 N LYS A 95 58.843 14.628 30.072 1.00 33.92 N ANISOU 745 N LYS B 95 4212 4232 4443 100 -145 -18 N ATOM 746 CA LYS A 95 57.955 13.537 29.628 1.00 36.55 C ANISOU 746 CA LYS B 95 4550 4563 4772 137 -98 -19 C ATOM 747 C LYS A 95 58.552 12.128 29.802 1.00 36.92 C ANISOU 747 C LYS B 95 4518 4589 4920 123 -131 -4 C ATOM 748 O LYS A 95 59.768 11.943 29.986 1.00 34.43 O ANISOU 748 O LYS B 95 4056 4173 4850 382 -278 -128 O ATOM 749 CB LYS A 95 57.581 13.734 28.160 1.00 36.94 C ANISOU 749 CB LYS B 95 4690 4556 4788 146 -54 98 C ATOM 750 CG LYS A 95 56.465 14.747 27.911 1.00 41.84 C ANISOU 750 CG LYS B 95 5209 5296 5391 -45 47 -14 C ATOM 751 CD LYS A 95 56.135 14.866 26.403 1.00 41.16 C ANISOU 751 CD LYS B 95 5272 5256 5110 -2 13 53 C ATOM 752 CE LYS A 95 55.431 13.598 25.856 1.00 47.18 C ANISOU 752 CE LYS B 95 5921 6082 5922 138 -120 37 C ATOM 753 NZ LYS A 95 55.636 13.365 24.375 1.00 49.12 N ANISOU 753 NZ LYS B 95 6359 6516 5789 44 -138 96 N ATOM 754 N GLU A 96 57.668 11.126 29.720 1.00 38.03 N ANISOU 754 N GLU B 96 4751 4690 5008 143 -91 -20 N ATOM 755 CA GLU A 96 58.043 9.759 30.034 1.00 38.58 C ANISOU 755 CA GLU B 96 4775 4836 5048 141 -69 0 C ATOM 756 C GLU A 96 59.204 9.264 29.172 1.00 37.83 C ANISOU 756 C GLU B 96 4560 4736 5074 195 -56 33 C ATOM 757 O GLU A 96 60.095 8.578 29.679 1.00 39.57 O ANISOU 757 O GLU B 96 4639 4855 5540 195 -25 80 O ATOM 758 CB GLU A 96 56.830 8.831 29.919 1.00 39.20 C ANISOU 758 CB GLU B 96 4896 4927 5070 159 -51 -14 C ATOM 759 CG GLU A 96 57.072 7.402 30.364 1.00 39.41 C ANISOU 759 CG GLU B 96 4930 5008 5032 136 -71 13 C ATOM 760 CD GLU A 96 55.792 6.564 30.261 1.00 43.05 C ANISOU 760 CD GLU B 96 5260 5390 5704 289 17 -15 C ATOM 761 OE1 GLU A 96 54.973 6.581 31.219 1.00 49.74 O ANISOU 761 OE1 GLU B 96 6531 6281 6085 127 -73 -240 O ATOM 762 OE2 GLU A 96 55.603 5.905 29.208 1.00 50.47 O ANISOU 762 OE2 GLU B 96 6200 6690 6285 272 -272 22 O ATOM 763 N ASP A 97 59.221 9.635 27.898 1.00 35.62 N ANISOU 763 N ASP B 97 4325 4506 4704 206 -211 94 N ATOM 764 CA ASP A 97 60.330 9.262 27.026 1.00 37.06 C ANISOU 764 CA ASP B 97 4559 4646 4876 110 -145 65 C ATOM 765 C ASP A 97 61.687 9.858 27.433 1.00 36.76 C ANISOU 765 C ASP B 97 4517 4610 4838 106 -237 20 C ATOM 766 O ASP A 97 62.739 9.271 27.124 1.00 35.31 O ANISOU 766 O ASP B 97 4224 4549 4640 163 -382 59 O ATOM 767 CB ASP A 97 60.028 9.615 25.576 1.00 37.48 C ANISOU 767 CB ASP B 97 4770 4697 4771 8 -99 11 C ATOM 768 CG ASP A 97 59.736 11.081 25.385 1.00 44.31 C ANISOU 768 CG ASP B 97 5321 5738 5774 83 17 15 C ATOM 769 OD1 ASP A 97 59.557 11.810 26.396 1.00 48.74 O ANISOU 769 OD1 ASP B 97 6386 6519 5613 144 -72 -89 O ATOM 770 OD2 ASP A 97 59.656 11.514 24.216 1.00 50.54 O ANISOU 770 OD2 ASP B 97 6713 6598 5889 234 121 -20 O ATOM 771 N GLU A 98 61.670 11.004 28.130 1.00 36.09 N ANISOU 771 N GLU B 98 4330 4495 4885 83 -143 -26 N ATOM 772 CA GLU A 98 62.920 11.587 28.649 1.00 35.61 C ANISOU 772 CA GLU B 98 4361 4530 4639 35 -123 23 C ATOM 773 C GLU A 98 63.450 10.806 29.847 1.00 35.41 C ANISOU 773 C GLU B 98 4267 4529 4656 43 -120 -18 C ATOM 774 O GLU A 98 64.666 10.745 30.055 1.00 34.18 O ANISOU 774 O GLU B 98 3935 4534 4518 266 -52 66 O ATOM 775 CB GLU A 98 62.741 13.062 29.004 1.00 34.75 C ANISOU 775 CB GLU B 98 4274 4351 4579 46 -72 53 C ATOM 776 CG GLU A 98 62.354 13.932 27.846 1.00 31.24 C ANISOU 776 CG GLU B 98 3883 3847 4137 24 -155 -14 C ATOM 777 CD GLU A 98 63.454 14.124 26.823 1.00 34.71 C ANISOU 777 CD GLU B 98 4261 4140 4785 121 -196 -115 C ATOM 778 OE1 GLU A 98 64.173 15.136 26.906 1.00 32.94 O ANISOU 778 OE1 GLU B 98 3799 3858 4857 1 -392 -288 O ATOM 779 OE2 GLU A 98 63.584 13.286 25.900 1.00 37.19 O ANISOU 779 OE2 GLU B 98 4564 4386 5177 232 -411 -230 O ATOM 780 N TYR A 99 62.553 10.194 30.624 1.00 36.22 N ANISOU 780 N TYR B 99 4446 4540 4773 16 -106 -40 N ATOM 781 CA TYR A 99 62.965 9.225 31.635 1.00 37.02 C ANISOU 781 CA TYR B 99 4656 4670 4737 44 -39 -36 C ATOM 782 C TYR A 99 63.721 8.043 31.021 1.00 37.46 C ANISOU 782 C TYR B 99 4595 4739 4898 18 -17 18 C ATOM 783 O TYR A 99 64.725 7.592 31.573 1.00 36.43 O ANISOU 783 O TYR B 99 4323 4558 4960 -18 72 -16 O ATOM 784 CB TYR A 99 61.763 8.725 32.427 1.00 33.30 C ANISOU 784 CB TYR B 99 4020 4511 4119 -143 -546 -196 C ATOM 785 CG TYR A 99 61.305 9.714 33.459 1.00 36.66 C ANISOU 785 CG TYR B 99 4839 4424 4663 79 131 -223 C ATOM 786 CD1 TYR A 99 60.534 10.816 33.105 1.00 35.38 C ANISOU 786 CD1 TYR B 99 4594 4482 4366 -51 12 -50 C ATOM 787 CD2 TYR A 99 61.656 9.563 34.798 1.00 34.43 C ANISOU 787 CD2 TYR B 99 4482 4270 4327 54 -127 120 C ATOM 788 CE1 TYR A 99 60.099 11.729 34.063 1.00 35.84 C ANISOU 788 CE1 TYR B 99 4541 4503 4571 65 103 87 C ATOM 789 CE2 TYR A 99 61.232 10.490 35.764 1.00 36.58 C ANISOU 789 CE2 TYR B 99 4740 4328 4829 -72 82 -152 C ATOM 790 CZ TYR A 99 60.465 11.571 35.383 1.00 35.08 C ANISOU 790 CZ TYR B 99 4473 4441 4415 165 217 -171 C ATOM 791 OH TYR A 99 60.041 12.488 36.327 1.00 35.92 O ANISOU 791 OH TYR B 99 4460 4568 4618 242 37 -280 O ATOM 792 N GLU A 100 63.262 7.587 29.859 1.00 38.34 N ANISOU 792 N GLU B 100 4796 4854 4915 49 -88 -9 N ATOM 793 CA GLU A 100 63.888 6.456 29.166 1.00 39.05 C ANISOU 793 CA GLU B 100 4879 4924 5034 38 -69 -39 C ATOM 794 C GLU A 100 65.241 6.889 28.643 1.00 38.96 C ANISOU 794 C GLU B 100 4819 4875 5107 51 -66 6 C ATOM 795 O GLU A 100 66.209 6.129 28.710 1.00 39.37 O ANISOU 795 O GLU B 100 4628 4940 5391 133 -171 -6 O ATOM 796 CB GLU A 100 63.051 5.984 27.957 1.00 40.88 C ANISOU 796 CB GLU B 100 5211 5238 5083 26 -94 24 C ATOM 797 CG GLU A 100 61.518 5.876 28.168 1.00 46.96 C ANISOU 797 CG GLU B 100 6139 5656 6044 -52 -10 42 C ATOM 798 CD GLU A 100 61.029 4.546 28.737 1.00 54.11 C ANISOU 798 CD GLU B 100 6653 6894 7009 181 127 -22 C ATOM 799 OE1 GLU A 100 61.832 3.779 29.328 1.00 58.83 O ANISOU 799 OE1 GLU B 100 7322 7447 7582 -108 76 80 O ATOM 800 OE2 GLU A 100 59.810 4.279 28.596 1.00 57.09 O ANISOU 800 OE2 GLU B 100 7234 7025 7432 128 75 3 O ATOM 801 N PHE A 101 65.289 8.118 28.117 1.00 38.29 N ANISOU 801 N PHE B 101 4782 4827 4938 27 -26 -87 N ATOM 802 CA PHE A 101 66.490 8.683 27.480 1.00 38.43 C ANISOU 802 CA PHE B 101 4685 4897 5017 35 -55 -52 C ATOM 803 C PHE A 101 67.627 8.703 28.447 1.00 37.62 C ANISOU 803 C PHE B 101 4499 4803 4992 85 -36 -75 C ATOM 804 O PHE A 101 68.749 8.300 28.130 1.00 38.03 O ANISOU 804 O PHE B 101 4286 4966 5196 150 -158 -160 O ATOM 805 CB PHE A 101 66.190 10.093 26.949 1.00 34.66 C ANISOU 805 CB PHE B 101 4275 4056 4838 516 2 -248 C ATOM 806 CG PHE A 101 67.413 10.903 26.574 1.00 38.05 C ANISOU 806 CG PHE B 101 4807 4809 4840 -3 -119 -53 C ATOM 807 CD1 PHE A 101 68.136 10.621 25.413 1.00 38.49 C ANISOU 807 CD1 PHE B 101 5044 4677 4900 46 126 -169 C ATOM 808 CD2 PHE A 101 67.815 11.977 27.370 1.00 34.07 C ANISOU 808 CD2 PHE B 101 4273 4154 4515 -61 -126 -199 C ATOM 809 CE1 PHE A 101 69.252 11.395 25.062 1.00 38.87 C ANISOU 809 CE1 PHE B 101 4794 4820 5152 -13 -107 -24 C ATOM 810 CE2 PHE A 101 68.921 12.760 27.026 1.00 35.37 C ANISOU 810 CE2 PHE B 101 4372 4545 4522 -81 -230 16 C ATOM 811 CZ PHE A 101 69.646 12.468 25.874 1.00 36.43 C ANISOU 811 CZ PHE B 101 4762 4608 4471 162 -85 -109 C ATOM 812 N VAL A 102 67.321 9.186 29.639 1.00 37.44 N ANISOU 812 N VAL B 102 4517 4717 4991 48 40 -101 N ATOM 813 CA VAL A 102 68.254 9.240 30.728 1.00 38.76 C ANISOU 813 CA VAL B 102 4741 4861 5123 76 6 -47 C ATOM 814 C VAL A 102 68.726 7.840 31.117 1.00 40.27 C ANISOU 814 C VAL B 102 4825 5035 5439 18 -68 -36 C ATOM 815 O VAL A 102 69.926 7.612 31.328 1.00 40.55 O ANISOU 815 O VAL B 102 4750 5065 5593 66 -182 -47 O ATOM 816 CB VAL A 102 67.601 9.984 31.911 1.00 37.84 C ANISOU 816 CB VAL B 102 4595 4765 5015 43 56 -46 C ATOM 817 CG1 VAL A 102 68.348 9.763 33.227 1.00 36.92 C ANISOU 817 CG1 VAL B 102 4462 4661 4903 121 115 -98 C ATOM 818 CG2 VAL A 102 67.502 11.489 31.568 1.00 34.42 C ANISOU 818 CG2 VAL B 102 4219 4477 4379 40 -80 -56 C ATOM 819 N GLN A 103 67.787 6.897 31.198 1.00 40.82 N ANISOU 819 N GLN B 103 4887 5108 5513 11 0 -119 N ATOM 820 CA GLN A 103 68.147 5.522 31.546 1.00 42.00 C ANISOU 820 CA GLN B 103 5091 5309 5557 43 32 -14 C ATOM 821 C GLN A 103 69.064 4.946 30.468 1.00 42.65 C ANISOU 821 C GLN B 103 5149 5397 5657 57 -7 9 C ATOM 822 O GLN A 103 70.068 4.292 30.764 1.00 44.17 O ANISOU 822 O GLN B 103 5242 5489 6049 116 -47 24 O ATOM 823 CB GLN A 103 66.887 4.686 31.752 1.00 41.46 C ANISOU 823 CB GLN B 103 5031 5213 5506 14 65 7 C ATOM 824 CG GLN A 103 66.136 5.124 33.001 1.00 43.00 C ANISOU 824 CG GLN B 103 5351 5370 5615 30 -44 -38 C ATOM 825 CD GLN A 103 64.822 4.388 33.192 1.00 43.99 C ANISOU 825 CD GLN B 103 5395 5489 5829 85 39 -38 C ATOM 826 OE1 GLN A 103 64.825 3.189 33.404 1.00 48.94 O ANISOU 826 OE1 GLN B 103 5726 6452 6414 104 382 26 O ATOM 827 NE2 GLN A 103 63.699 5.099 33.101 1.00 44.09 N ANISOU 827 NE2 GLN B 103 5352 5453 5947 -14 15 -203 N ATOM 828 N GLN A 104 68.731 5.223 29.221 1.00 42.86 N ANISOU 828 N GLN B 104 5233 5449 5600 97 -12 10 N ATOM 829 CA GLN A 104 69.583 4.876 28.109 1.00 43.57 C ANISOU 829 CA GLN B 104 5355 5528 5671 46 -37 -9 C ATOM 830 C GLN A 104 71.014 5.338 28.315 1.00 44.23 C ANISOU 830 C GLN B 104 5428 5597 5781 38 -107 -49 C ATOM 831 O GLN A 104 71.958 4.594 28.084 1.00 43.90 O ANISOU 831 O GLN B 104 5153 5518 6008 78 -227 -24 O ATOM 832 CB GLN A 104 69.042 5.513 26.850 1.00 43.75 C ANISOU 832 CB GLN B 104 5458 5532 5631 5 40 -56 C ATOM 833 CG GLN A 104 69.421 4.816 25.589 1.00 44.49 C ANISOU 833 CG GLN B 104 5551 5698 5652 40 -26 -25 C ATOM 834 CD GLN A 104 68.697 5.402 24.393 1.00 46.77 C ANISOU 834 CD GLN B 104 5889 5963 5917 56 70 135 C ATOM 835 OE1 GLN A 104 67.827 6.247 24.548 1.00 52.29 O ANISOU 835 OE1 GLN B 104 6508 6647 6709 -188 -127 -68 O ATOM 836 NE2 GLN A 104 69.058 4.956 23.205 1.00 51.95 N ANISOU 836 NE2 GLN B 104 6780 6508 6449 -92 -66 -140 N ATOM 837 N LEU A 105 71.170 6.589 28.717 1.00 43.78 N ANISOU 837 N LEU B 105 5402 5570 5660 32 -124 -35 N ATOM 838 CA LEU A 105 72.485 7.171 28.858 1.00 44.90 C ANISOU 838 CA LEU B 105 5522 5692 5845 61 -99 30 C ATOM 839 C LEU A 105 73.234 6.393 29.935 1.00 45.35 C ANISOU 839 C LEU B 105 5515 5824 5891 62 -84 29 C ATOM 840 O LEU A 105 74.428 6.152 29.829 1.00 44.98 O ANISOU 840 O LEU B 105 5349 5883 5859 24 -88 12 O ATOM 841 CB LEU A 105 72.366 8.653 29.242 1.00 44.86 C ANISOU 841 CB LEU B 105 5543 5661 5837 22 -37 9 C ATOM 842 CG LEU A 105 72.053 9.644 28.120 1.00 43.27 C ANISOU 842 CG LEU B 105 5248 5584 5607 19 -81 -36 C ATOM 843 CD1 LEU A 105 71.847 11.050 28.639 1.00 40.27 C ANISOU 843 CD1 LEU B 105 5118 5085 5097 3 -65 -131 C ATOM 844 CD2 LEU A 105 73.111 9.621 27.044 1.00 42.86 C ANISOU 844 CD2 LEU B 105 5214 5397 5675 -15 -49 3 C ATOM 845 N ALA A 106 72.515 5.989 30.970 1.00 46.49 N ANISOU 845 N ALA B 106 5702 5984 5977 77 -70 30 N ATOM 846 CA ALA A 106 73.152 5.420 32.140 1.00 48.43 C ANISOU 846 CA ALA B 106 6049 6182 6169 56 -7 39 C ATOM 847 C ALA A 106 73.726 4.055 31.820 1.00 51.47 C ANISOU 847 C ALA B 106 6392 6569 6592 -1 -6 25 C ATOM 848 O ALA A 106 74.493 3.507 32.592 1.00 53.20 O ANISOU 848 O ALA B 106 6583 6830 6798 1 104 21 O ATOM 849 CB ALA A 106 72.179 5.333 33.291 1.00 48.83 C ANISOU 849 CB ALA B 106 6110 6185 6258 9 -17 14 C ATOM 850 N ALA A 107 73.341 3.521 30.667 1.00 53.46 N ANISOU 850 N ALA B 107 6619 6893 6798 -15 -36 0 N ATOM 851 CA ALA A 107 73.482 2.102 30.394 1.00 54.77 C ANISOU 851 CA ALA B 107 6852 6995 6963 17 -10 16 C ATOM 852 C ALA A 107 74.632 1.954 29.435 1.00 55.91 C ANISOU 852 C ALA B 107 6927 7130 7187 36 -37 -27 C ATOM 853 O ALA A 107 75.393 1.006 29.503 1.00 56.85 O ANISOU 853 O ALA B 107 7064 7138 7397 87 -27 -27 O ATOM 854 CB ALA A 107 72.233 1.570 29.775 1.00 55.26 C ANISOU 854 CB ALA B 107 6893 7078 7024 60 12 -17 C ATOM 855 N GLU A 108 74.757 2.930 28.546 1.00 56.20 N ANISOU 855 N GLU B 108 7022 7116 7213 48 -44 -55 N ATOM 856 CA GLU A 108 75.998 3.150 27.835 1.00 55.93 C ANISOU 856 CA GLU B 108 7021 7106 7121 22 -38 1 C ATOM 857 C GLU A 108 77.023 3.946 28.589 1.00 54.57 C ANISOU 857 C GLU B 108 6696 7028 7008 -49 -30 -50 C ATOM 858 O GLU A 108 78.037 4.326 28.032 1.00 53.66 O ANISOU 858 O GLU B 108 6320 7058 7009 -79 3 -76 O ATOM 859 CB GLU A 108 75.732 3.814 26.518 1.00 56.80 C ANISOU 859 CB GLU B 108 7141 7226 7213 -32 13 15 C ATOM 860 CG GLU A 108 74.353 3.540 25.997 1.00 56.87 C ANISOU 860 CG GLU B 108 7079 7251 7277 -4 -23 -28 C ATOM 861 CD GLU A 108 74.258 3.954 24.568 1.00 58.55 C ANISOU 861 CD GLU B 108 7479 7455 7310 -24 35 19 C ATOM 862 OE1 GLU A 108 74.566 5.120 24.303 1.00 62.28 O ANISOU 862 OE1 GLU B 108 7752 8095 7816 70 -64 134 O ATOM 863 OE2 GLU A 108 73.915 3.111 23.729 1.00 63.22 O ANISOU 863 OE2 GLU B 108 7897 8320 7801 -92 131 -35 O ATOM 864 N HIS A 109 76.774 4.184 29.862 1.00 53.45 N ANISOU 864 N HIS B 109 6577 6825 6906 -54 13 36 N ATOM 865 CA HIS A 109 77.714 4.947 30.641 1.00 52.53 C ANISOU 865 CA HIS B 109 6514 6694 6748 -53 57 -1 C ATOM 866 C HIS A 109 78.195 6.152 29.843 1.00 51.14 C ANISOU 866 C HIS B 109 6317 6426 6686 -56 -25 42 C ATOM 867 O HIS A 109 79.388 6.422 29.769 1.00 51.74 O ANISOU 867 O HIS B 109 6309 6494 6854 -127 -75 -43 O ATOM 868 CB HIS A 109 78.890 4.056 31.024 1.00 54.76 C ANISOU 868 CB HIS B 109 6915 6867 7022 -103 -43 41 C ATOM 869 CG HIS A 109 78.520 2.954 31.964 1.00 59.17 C ANISOU 869 CG HIS B 109 7378 7552 7552 -3 152 -37 C ATOM 870 ND1 HIS A 109 78.429 1.638 31.570 1.00 62.06 N ANISOU 870 ND1 HIS B 109 7588 7979 8010 95 35 -30 N ATOM 871 CD2 HIS A 109 78.188 2.978 33.275 1.00 61.85 C ANISOU 871 CD2 HIS B 109 7817 8008 7672 -16 -12 0 C ATOM 872 CE1 HIS A 109 78.071 0.897 32.601 1.00 63.03 C ANISOU 872 CE1 HIS B 109 7744 8145 8058 75 41 11 C ATOM 873 NE2 HIS A 109 77.915 1.686 33.647 1.00 63.38 N ANISOU 873 NE2 HIS B 109 7899 8193 7989 82 20 -29 N ATOM 874 N LEU A 110 77.251 6.875 29.248 1.00 48.16 N ANISOU 874 N LEU B 110 5923 6088 6287 38 -59 51 N ATOM 875 CA LEU A 110 77.464 8.261 28.885 1.00 45.84 C ANISOU 875 CA LEU B 110 5763 5770 5884 -9 -116 -2 C ATOM 876 C LEU A 110 76.929 9.216 29.943 1.00 44.02 C ANISOU 876 C LEU B 110 5477 5529 5720 4 -79 -6 C ATOM 877 O LEU A 110 75.761 9.179 30.290 1.00 44.34 O ANISOU 877 O LEU B 110 5391 5583 5871 -55 -145 -86 O ATOM 878 CB LEU A 110 76.804 8.566 27.560 1.00 45.64 C ANISOU 878 CB LEU B 110 5733 5810 5797 35 -14 -70 C ATOM 879 CG LEU A 110 77.389 7.866 26.355 1.00 45.72 C ANISOU 879 CG LEU B 110 5680 5792 5897 -30 -125 -61 C ATOM 880 CD1 LEU A 110 76.608 8.272 25.157 1.00 45.76 C ANISOU 880 CD1 LEU B 110 5619 5762 6004 -48 -39 -17 C ATOM 881 CD2 LEU A 110 78.831 8.284 26.215 1.00 46.63 C ANISOU 881 CD2 LEU B 110 5732 5842 6143 -36 -186 -25 C ATOM 882 N THR A 111 77.812 10.056 30.455 1.00 41.27 N ANISOU 882 N THR B 111 5063 5215 5403 -46 -43 -67 N ATOM 883 CA THR A 111 77.431 11.120 31.372 1.00 39.18 C ANISOU 883 CA THR B 111 4808 4919 5159 -16 97 -11 C ATOM 884 C THR A 111 77.811 12.478 30.762 1.00 36.93 C ANISOU 884 C THR B 111 4422 4540 5070 -44 54 31 C ATOM 885 O THR A 111 79.002 12.804 30.677 1.00 35.44 O ANISOU 885 O THR B 111 3964 4364 5135 -120 48 208 O ATOM 886 CB THR A 111 78.074 10.931 32.737 1.00 39.68 C ANISOU 886 CB THR B 111 4934 4950 5192 -22 43 -1 C ATOM 887 OG1 THR A 111 77.631 9.688 33.288 1.00 41.29 O ANISOU 887 OG1 THR B 111 5027 5153 5507 -76 -9 -72 O ATOM 888 CG2 THR A 111 77.664 12.035 33.678 1.00 40.48 C ANISOU 888 CG2 THR B 111 5024 5124 5232 -40 -34 38 C ATOM 889 N PRO A 112 76.794 13.256 30.301 1.00 34.58 N ANISOU 889 N PRO B 112 4175 4287 4675 25 63 13 N ATOM 890 CA PRO A 112 77.094 14.607 29.774 1.00 32.42 C ANISOU 890 CA PRO B 112 4008 4017 4293 -30 -106 -4 C ATOM 891 C PRO A 112 77.535 15.484 30.946 1.00 30.34 C ANISOU 891 C PRO B 112 3608 3770 4149 -106 -86 -107 C ATOM 892 O PRO A 112 77.076 15.272 32.057 1.00 28.74 O ANISOU 892 O PRO B 112 3182 3683 4052 -172 -121 -97 O ATOM 893 CB PRO A 112 75.770 15.070 29.127 1.00 32.42 C ANISOU 893 CB PRO B 112 3935 4171 4212 -56 -126 -104 C ATOM 894 CG PRO A 112 74.720 14.127 29.579 1.00 33.28 C ANISOU 894 CG PRO B 112 4163 4131 4350 -53 -43 0 C ATOM 895 CD PRO A 112 75.353 12.940 30.276 1.00 33.90 C ANISOU 895 CD PRO B 112 4123 4255 4502 -46 14 23 C ATOM 896 N GLU A 113 78.466 16.415 30.707 1.00 28.50 N ANISOU 896 N GLU B 113 3413 3476 3939 -247 -219 -106 N ATOM 897 CA GLU A 113 78.984 17.229 31.786 1.00 26.74 C ANISOU 897 CA GLU B 113 3307 3231 3622 -201 -91 -120 C ATOM 898 C GLU A 113 77.827 18.078 32.368 1.00 24.24 C ANISOU 898 C GLU B 113 2947 3077 3186 -149 -118 -133 C ATOM 899 O GLU A 113 77.800 18.381 33.570 1.00 24.81 O ANISOU 899 O GLU B 113 3055 3022 3347 -232 116 -201 O ATOM 900 CB GLU A 113 80.076 18.148 31.254 1.00 28.02 C ANISOU 900 CB GLU B 113 3540 3394 3712 -175 -152 -184 C ATOM 901 CG GLU A 113 81.482 17.493 31.126 1.00 26.90 C ANISOU 901 CG GLU B 113 3284 3139 3797 -153 -108 -115 C ATOM 902 CD GLU A 113 81.650 16.581 29.906 1.00 30.97 C ANISOU 902 CD GLU B 113 3953 3946 3867 3 -156 -37 C ATOM 903 OE1 GLU A 113 80.715 16.404 29.092 1.00 29.29 O ANISOU 903 OE1 GLU B 113 3509 3186 4434 -308 -289 -166 O ATOM 904 OE2 GLU A 113 82.770 16.039 29.763 1.00 37.29 O ANISOU 904 OE2 GLU B 113 4418 4548 5202 -377 -170 -61 O ATOM 905 N TYR A 114 76.936 18.486 31.476 1.00 23.52 N ANISOU 905 N TYR B 114 2826 3018 3089 -180 -181 -123 N ATOM 906 CA TYR A 114 75.819 19.398 31.768 1.00 22.61 C ANISOU 906 CA TYR B 114 2920 2894 2774 -117 -89 -94 C ATOM 907 C TYR A 114 74.501 18.920 31.159 1.00 22.91 C ANISOU 907 C TYR B 114 2712 3038 2954 41 -113 -130 C ATOM 908 O TYR A 114 74.407 18.645 29.942 1.00 20.81 O ANISOU 908 O TYR B 114 2356 2756 2791 117 -199 201 O ATOM 909 CB TYR A 114 76.116 20.836 31.281 1.00 22.60 C ANISOU 909 CB TYR B 114 2870 2964 2750 -189 -188 -193 C ATOM 910 CG TYR A 114 77.323 21.470 31.919 1.00 23.18 C ANISOU 910 CG TYR B 114 2962 2954 2888 19 22 -136 C ATOM 911 CD1 TYR A 114 77.228 22.130 33.149 1.00 22.86 C ANISOU 911 CD1 TYR B 114 2898 2951 2835 -192 -257 115 C ATOM 912 CD2 TYR A 114 78.576 21.360 31.341 1.00 26.60 C ANISOU 912 CD2 TYR B 114 2987 3168 3952 -180 -298 -140 C ATOM 913 CE1 TYR A 114 78.368 22.686 33.768 1.00 23.67 C ANISOU 913 CE1 TYR B 114 2626 3162 3206 154 -85 -152 C ATOM 914 CE2 TYR A 114 79.712 21.931 31.951 1.00 25.69 C ANISOU 914 CE2 TYR B 114 3415 2976 3369 -216 -116 144 C ATOM 915 CZ TYR A 114 79.599 22.576 33.163 1.00 26.00 C ANISOU 915 CZ TYR B 114 2942 3140 3795 -106 -239 60 C ATOM 916 OH TYR A 114 80.731 23.109 33.762 1.00 26.26 O ANISOU 916 OH TYR B 114 3205 2970 3802 -13 -20 170 O ATOM 917 N ILE A 115 73.469 18.876 32.011 1.00 23.30 N ANISOU 917 N ILE B 115 2562 2998 3290 25 5 -87 N ATOM 918 CA ILE A 115 72.109 18.676 31.526 1.00 23.11 C ANISOU 918 CA ILE B 115 2807 2919 3053 -81 -63 2 C ATOM 919 C ILE A 115 71.193 19.826 31.995 1.00 22.75 C ANISOU 919 C ILE B 115 2710 3050 2884 -38 -119 -65 C ATOM 920 O ILE A 115 71.081 20.098 33.198 1.00 21.17 O ANISOU 920 O ILE B 115 2230 3089 2725 -4 -217 -251 O ATOM 921 CB ILE A 115 71.509 17.352 32.009 1.00 23.53 C ANISOU 921 CB ILE B 115 2801 2938 3200 -39 -35 25 C ATOM 922 CG1 ILE A 115 72.378 16.162 31.597 1.00 23.87 C ANISOU 922 CG1 ILE B 115 2960 2831 3277 36 14 24 C ATOM 923 CG2 ILE A 115 70.062 17.167 31.473 1.00 24.16 C ANISOU 923 CG2 ILE B 115 2798 3078 3303 48 -64 13 C ATOM 924 CD1 ILE A 115 71.980 14.852 32.355 1.00 25.78 C ANISOU 924 CD1 ILE B 115 3004 3340 3450 -47 -30 -13 C ATOM 925 N THR A 116 70.531 20.451 31.034 1.00 20.55 N ANISOU 925 N THR B 116 2540 2839 2426 -116 -21 -65 N ATOM 926 CA THR A 116 69.534 21.497 31.280 1.00 22.07 C ANISOU 926 CA THR B 116 2788 2877 2719 -45 -48 -72 C ATOM 927 C THR A 116 68.102 20.985 31.049 1.00 20.73 C ANISOU 927 C THR B 116 2632 2688 2555 30 -69 5 C ATOM 928 O THR A 116 67.701 20.626 29.941 1.00 20.58 O ANISOU 928 O THR B 116 2556 2750 2512 91 -163 -4 O ATOM 929 CB THR A 116 69.813 22.753 30.412 1.00 19.35 C ANISOU 929 CB THR B 116 2628 2597 2126 -27 -121 -243 C ATOM 930 OG1 THR A 116 71.091 23.278 30.764 1.00 20.38 O ANISOU 930 OG1 THR B 116 2715 2707 2320 4 -488 -100 O ATOM 931 CG2 THR A 116 68.772 23.856 30.582 1.00 19.33 C ANISOU 931 CG2 THR B 116 2651 2600 2094 -18 198 -22 C ATOM 932 N ILE A 117 67.333 20.976 32.121 1.00 20.52 N ANISOU 932 N ILE B 117 2532 2815 2450 -9 -67 -51 N ATOM 933 CA ILE A 117 65.916 20.662 32.059 1.00 22.89 C ANISOU 933 CA ILE B 117 2970 2950 2777 50 -29 -91 C ATOM 934 C ILE A 117 65.186 21.935 31.624 1.00 23.37 C ANISOU 934 C ILE B 117 3051 2906 2920 17 -41 -80 C ATOM 935 O ILE A 117 65.158 22.915 32.362 1.00 23.30 O ANISOU 935 O ILE B 117 3097 2522 3231 -56 -151 -207 O ATOM 936 CB ILE A 117 65.380 20.211 33.446 1.00 21.81 C ANISOU 936 CB ILE B 117 2994 2862 2430 -63 -74 -31 C ATOM 937 CG1 ILE A 117 66.130 18.974 33.945 1.00 23.84 C ANISOU 937 CG1 ILE B 117 2968 3363 2728 118 -79 -135 C ATOM 938 CG2 ILE A 117 63.851 20.001 33.369 1.00 20.89 C ANISOU 938 CG2 ILE B 117 2672 2817 2448 177 -280 -160 C ATOM 939 CD1 ILE A 117 65.789 18.630 35.411 1.00 23.38 C ANISOU 939 CD1 ILE B 117 2854 3201 2827 49 139 -3 C ATOM 940 N ASP A 118 64.615 21.961 30.426 1.00 24.96 N ANISOU 940 N ASP B 118 3221 3067 3193 39 -80 -1 N ATOM 941 CA AASP A 118 64.167 23.218 29.847 0.50 26.06 C ANISOU 941 CA AASP B 118 3354 3254 3290 -2 22 4 C ATOM 942 C ASP A 118 62.644 23.240 29.610 1.00 26.24 C ANISOU 942 C ASP B 118 3398 3222 3349 3 -28 -51 C ATOM 943 O ASP A 118 62.180 22.716 28.638 1.00 24.45 O ANISOU 943 O ASP B 118 3529 2783 2976 -112 -211 -102 O ATOM 944 CB AASP A 118 65.089 23.551 28.625 0.50 27.89 C ANISOU 944 CB AASP B 118 3719 3408 3470 -41 44 -115 C ATOM 945 CG AASP A 118 64.361 23.720 27.293 0.50 26.07 C ANISOU 945 CG AASP B 118 3362 2978 3564 12 -72 22 C ATOM 946 OD1AASP A 118 63.934 24.835 26.986 0.50 25.19 O ANISOU 946 OD1AASP B 118 2953 2953 3662 36 -380 -164 O ATOM 947 OD2AASP A 118 64.318 22.779 26.481 0.50 26.53 O ANISOU 947 OD2AASP B 118 3165 2701 4214 97 -258 -268 O ATOM 948 N ILE A 119 61.913 23.851 30.546 1.00 27.26 N ANISOU 948 N ILE B 119 3300 3465 3590 -23 -89 10 N ATOM 949 CA ILE A 119 60.460 23.889 30.578 1.00 27.01 C ANISOU 949 CA ILE B 119 3374 3415 3471 -51 -71 36 C ATOM 950 C ILE A 119 59.998 25.361 30.824 1.00 27.05 C ANISOU 950 C ILE B 119 3295 3413 3568 -28 -76 156 C ATOM 951 O ILE A 119 60.632 26.110 31.592 1.00 26.64 O ANISOU 951 O ILE B 119 3376 3159 3585 -52 -116 286 O ATOM 952 CB ILE A 119 59.977 22.898 31.708 1.00 28.32 C ANISOU 952 CB ILE B 119 3400 3584 3775 23 -46 -26 C ATOM 953 CG1 ILE A 119 60.259 21.430 31.322 1.00 28.06 C ANISOU 953 CG1 ILE B 119 3518 3623 3520 28 -133 99 C ATOM 954 CG2 ILE A 119 58.556 23.088 32.090 1.00 28.18 C ANISOU 954 CG2 ILE B 119 3378 3420 3907 -128 -175 87 C ATOM 955 CD1 ILE A 119 59.709 21.044 29.946 1.00 31.23 C ANISOU 955 CD1 ILE B 119 4103 4029 3733 51 -124 112 C ATOM 956 N ALA A 120 58.921 25.779 30.157 1.00 25.79 N ANISOU 956 N ALA B 120 3203 3171 3425 56 -73 123 N ATOM 957 CA ALA A 120 58.449 27.165 30.260 1.00 25.05 C ANISOU 957 CA ALA B 120 3190 3114 3212 111 -79 47 C ATOM 958 C ALA A 120 58.136 27.521 31.698 1.00 24.32 C ANISOU 958 C ALA B 120 3093 3046 3101 152 -97 9 C ATOM 959 O ALA A 120 58.580 28.549 32.185 1.00 26.28 O ANISOU 959 O ALA B 120 2935 3419 3628 256 -81 -113 O ATOM 960 CB ALA A 120 57.226 27.407 29.420 1.00 25.31 C ANISOU 960 CB ALA B 120 3328 3301 2987 122 -61 88 C ATOM 961 N HIS A 121 57.357 26.677 32.363 1.00 22.77 N ANISOU 961 N HIS B 121 2795 2845 3010 39 -116 -14 N ATOM 962 CA HIS A 121 56.929 26.906 33.745 1.00 23.05 C ANISOU 962 CA HIS B 121 2924 2906 2925 89 -77 88 C ATOM 963 C HIS A 121 57.570 25.809 34.622 1.00 23.26 C ANISOU 963 C HIS B 121 2911 2915 3011 118 -25 4 C ATOM 964 O HIS A 121 56.974 24.772 34.947 1.00 22.06 O ANISOU 964 O HIS B 121 2784 3024 2572 219 62 7 O ATOM 965 CB HIS A 121 55.390 26.965 33.865 1.00 22.80 C ANISOU 965 CB HIS B 121 2819 3043 2801 -8 -104 -18 C ATOM 966 CG HIS A 121 54.914 27.364 35.228 1.00 21.32 C ANISOU 966 CG HIS B 121 2656 2649 2796 -163 -153 -51 C ATOM 967 ND1 HIS A 121 53.594 27.261 35.627 1.00 24.35 N ANISOU 967 ND1 HIS B 121 3138 3006 3107 1 -52 179 N ATOM 968 CD2 HIS A 121 55.602 27.801 36.314 1.00 15.02 C ANISOU 968 CD2 HIS B 121 1741 1787 2177 -73 373 -65 C ATOM 969 CE1 HIS A 121 53.483 27.682 36.877 1.00 18.62 C ANISOU 969 CE1 HIS B 121 2363 2184 2526 13 2 -288 C ATOM 970 NE2 HIS A 121 54.689 28.002 37.318 1.00 20.20 N ANISOU 970 NE2 HIS B 121 2468 2875 2332 -343 -187 32 N ATOM 971 N GLY A 122 58.817 26.057 34.986 1.00 21.55 N ANISOU 971 N GLY B 122 2883 2654 2648 115 -153 159 N ATOM 972 CA GLY A 122 59.679 25.016 35.527 1.00 22.32 C ANISOU 972 CA GLY B 122 2726 2878 2874 71 -40 0 C ATOM 973 C GLY A 122 59.509 24.755 37.016 1.00 23.88 C ANISOU 973 C GLY B 122 2949 3098 3026 -9 63 -86 C ATOM 974 O GLY A 122 60.032 23.752 37.517 1.00 23.95 O ANISOU 974 O GLY B 122 2923 2977 3197 -125 62 -300 O ATOM 975 N HIS A 123 58.822 25.656 37.736 1.00 23.95 N ANISOU 975 N HIS B 123 2915 3004 3178 -36 13 -75 N ATOM 976 CA HIS A 123 58.449 25.401 39.135 1.00 24.81 C ANISOU 976 CA HIS B 123 3136 3138 3152 -28 -5 19 C ATOM 977 C HIS A 123 57.287 24.383 39.104 1.00 26.13 C ANISOU 977 C HIS B 123 3387 3207 3332 2 -27 -5 C ATOM 978 O HIS A 123 56.128 24.763 39.008 1.00 26.91 O ANISOU 978 O HIS B 123 3687 3150 3386 -99 -331 -52 O ATOM 979 CB HIS A 123 58.065 26.707 39.879 1.00 23.25 C ANISOU 979 CB HIS B 123 3063 2655 3115 -16 25 96 C ATOM 980 CG HIS A 123 57.936 26.564 41.365 1.00 24.25 C ANISOU 980 CG HIS B 123 2999 2820 3391 -77 26 -135 C ATOM 981 ND1 HIS A 123 57.336 27.521 42.162 1.00 24.97 N ANISOU 981 ND1 HIS B 123 3198 3204 3085 9 -38 34 N ATOM 982 CD2 HIS A 123 58.327 25.573 42.201 1.00 23.40 C ANISOU 982 CD2 HIS B 123 3003 2839 3047 208 -33 131 C ATOM 983 CE1 HIS A 123 57.349 27.114 43.415 1.00 24.71 C ANISOU 983 CE1 HIS B 123 3059 2900 3427 30 132 -43 C ATOM 984 NE2 HIS A 123 57.953 25.940 43.466 1.00 25.21 N ANISOU 984 NE2 HIS B 123 2820 3275 3482 88 -127 -236 N ATOM 985 N SER A 124 57.622 23.091 39.115 1.00 28.21 N ANISOU 985 N SER B 124 3549 3541 3628 -45 -22 -54 N ATOM 986 CA SER A 124 56.624 21.994 39.022 1.00 28.99 C ANISOU 986 CA SER B 124 3644 3618 3750 75 -16 -46 C ATOM 987 C SER A 124 57.159 20.668 39.556 1.00 30.47 C ANISOU 987 C SER B 124 3664 3796 4117 125 -37 -119 C ATOM 988 O SER A 124 58.377 20.433 39.619 1.00 29.18 O ANISOU 988 O SER B 124 3399 3514 4174 343 41 -183 O ATOM 989 CB SER A 124 56.192 21.777 37.575 1.00 31.00 C ANISOU 989 CB SER B 124 3951 3868 3959 -40 -53 -20 C ATOM 990 OG SER A 124 57.217 21.136 36.834 1.00 33.98 O ANISOU 990 OG SER B 124 4185 4391 4335 -81 -288 -214 O ATOM 991 N ASN A 125 56.254 19.758 39.921 1.00 31.16 N ANISOU 991 N ASN B 125 3856 3797 4183 79 14 -226 N ATOM 992 CA ASN A 125 56.728 18.444 40.374 1.00 31.40 C ANISOU 992 CA ASN B 125 3906 3894 4129 140 54 -99 C ATOM 993 C ASN A 125 57.295 17.626 39.229 1.00 30.70 C ANISOU 993 C ASN B 125 3797 3708 4160 231 55 -100 C ATOM 994 O ASN A 125 58.133 16.744 39.452 1.00 32.07 O ANISOU 994 O ASN B 125 3961 3715 4508 241 82 -229 O ATOM 995 CB ASN A 125 55.639 17.709 41.141 1.00 33.26 C ANISOU 995 CB ASN B 125 4178 4048 4411 142 59 -191 C ATOM 996 CG ASN A 125 55.386 18.350 42.487 1.00 39.58 C ANISOU 996 CG ASN B 125 5256 5078 4705 99 -20 -75 C ATOM 997 OD1 ASN A 125 56.254 18.328 43.372 1.00 40.87 O ANISOU 997 OD1 ASN B 125 5424 4899 5203 252 276 50 O ATOM 998 ND2 ASN A 125 54.221 18.998 42.630 1.00 45.34 N ANISOU 998 ND2 ASN B 125 5822 5592 5814 -207 84 -127 N ATOM 999 N ALA A 126 56.870 17.962 38.006 1.00 29.89 N ANISOU 999 N ALA B 126 3815 3511 4030 300 -36 -70 N ATOM 1000 CA ALA A 126 57.411 17.349 36.789 1.00 29.92 C ANISOU 1000 CA ALA B 126 3734 3630 4002 140 -52 0 C ATOM 1001 C ALA A 126 58.908 17.596 36.707 1.00 29.34 C ANISOU 1001 C ALA B 126 3550 3603 3993 98 -125 -45 C ATOM 1002 O ALA A 126 59.669 16.682 36.459 1.00 28.50 O ANISOU 1002 O ALA B 126 3199 3643 3984 199 -391 130 O ATOM 1003 CB ALA A 126 56.741 17.916 35.568 1.00 30.67 C ANISOU 1003 CB ALA B 126 3952 3622 4076 193 -13 8 C ATOM 1004 N VAL A 127 59.318 18.842 36.952 1.00 28.80 N ANISOU 1004 N VAL B 127 3407 3616 3918 105 -93 -99 N ATOM 1005 CA VAL A 127 60.740 19.214 36.959 1.00 28.43 C ANISOU 1005 CA VAL B 127 3356 3575 3871 104 -47 -3 C ATOM 1006 C VAL A 127 61.458 18.622 38.178 1.00 28.15 C ANISOU 1006 C VAL B 127 3214 3647 3832 178 26 -41 C ATOM 1007 O VAL A 127 62.572 18.095 38.052 1.00 27.84 O ANISOU 1007 O VAL B 127 3160 3636 3781 166 155 -176 O ATOM 1008 CB VAL A 127 60.927 20.770 36.898 1.00 26.50 C ANISOU 1008 CB VAL B 127 3131 3365 3573 63 -110 30 C ATOM 1009 CG1 VAL A 127 62.411 21.177 37.169 1.00 25.18 C ANISOU 1009 CG1 VAL B 127 3004 3267 3296 -35 139 -95 C ATOM 1010 CG2 VAL A 127 60.479 21.308 35.586 1.00 24.52 C ANISOU 1010 CG2 VAL B 127 2816 3090 3409 28 -240 -149 C ATOM 1011 N ILE A 128 60.825 18.682 39.348 1.00 29.46 N ANISOU 1011 N ILE B 128 3392 3828 3973 75 -46 -62 N ATOM 1012 CA ILE A 128 61.411 18.114 40.565 1.00 30.69 C ANISOU 1012 CA ILE B 128 3755 3886 4017 76 -26 5 C ATOM 1013 C ILE A 128 61.740 16.600 40.410 1.00 30.92 C ANISOU 1013 C ILE B 128 3634 3934 4180 145 60 74 C ATOM 1014 O ILE A 128 62.838 16.145 40.758 1.00 31.21 O ANISOU 1014 O ILE B 128 3397 3933 4526 332 91 -94 O ATOM 1015 CB ILE A 128 60.513 18.407 41.816 1.00 31.14 C ANISOU 1015 CB ILE B 128 3855 3975 4001 71 -79 27 C ATOM 1016 CG1 ILE A 128 60.620 19.891 42.204 1.00 32.78 C ANISOU 1016 CG1 ILE B 128 4092 4041 4322 90 66 -114 C ATOM 1017 CG2 ILE A 128 60.895 17.514 43.003 1.00 31.53 C ANISOU 1017 CG2 ILE B 128 3800 4138 4042 -1 15 8 C ATOM 1018 CD1 ILE A 128 59.354 20.522 42.653 1.00 31.10 C ANISOU 1018 CD1 ILE B 128 3823 4077 3917 77 -82 19 C ATOM 1019 N ASN A 129 60.808 15.841 39.845 1.00 32.57 N ANISOU 1019 N ASN B 129 3869 4114 4391 91 -43 69 N ATOM 1020 CA ASN A 129 61.000 14.405 39.642 1.00 32.50 C ANISOU 1020 CA ASN B 129 3893 4151 4305 89 28 27 C ATOM 1021 C ASN A 129 62.058 14.099 38.588 1.00 33.00 C ANISOU 1021 C ASN B 129 3913 4186 4437 89 83 -10 C ATOM 1022 O ASN A 129 62.830 13.153 38.732 1.00 34.71 O ANISOU 1022 O ASN B 129 3780 4559 4846 289 237 31 O ATOM 1023 CB ASN A 129 59.663 13.740 39.261 1.00 33.28 C ANISOU 1023 CB ASN B 129 4052 4160 4430 91 -85 115 C ATOM 1024 CG ASN A 129 58.650 13.753 40.403 1.00 36.33 C ANISOU 1024 CG ASN B 129 4518 4639 4644 162 33 -13 C ATOM 1025 OD1 ASN A 129 59.016 13.801 41.589 1.00 41.38 O ANISOU 1025 OD1 ASN B 129 5079 5625 5019 213 131 57 O ATOM 1026 ND2 ASN A 129 57.370 13.719 40.054 1.00 36.67 N ANISOU 1026 ND2 ASN B 129 4777 4577 4579 11 1 -137 N ATOM 1027 N MET A 130 62.126 14.907 37.530 1.00 32.84 N ANISOU 1027 N MET B 130 3971 4226 4279 -13 -21 -6 N ATOM 1028 CA MET A 130 63.211 14.760 36.561 1.00 31.93 C ANISOU 1028 CA MET B 130 3853 4116 4160 30 32 -24 C ATOM 1029 C MET A 130 64.597 15.065 37.168 1.00 31.45 C ANISOU 1029 C MET B 130 3702 4082 4165 24 39 -130 C ATOM 1030 O MET A 130 65.575 14.358 36.890 1.00 29.24 O ANISOU 1030 O MET B 130 3177 3789 4144 128 95 -317 O ATOM 1031 CB MET A 130 62.946 15.596 35.315 1.00 32.23 C ANISOU 1031 CB MET B 130 3839 4136 4269 64 -7 -33 C ATOM 1032 CG MET A 130 64.014 15.405 34.226 1.00 31.85 C ANISOU 1032 CG MET B 130 3719 4209 4173 -15 -123 -70 C ATOM 1033 SD MET A 130 64.289 13.666 33.790 1.00 35.23 S ANISOU 1033 SD MET B 130 3413 4940 5030 -27 -122 -172 S ATOM 1034 CE MET A 130 62.942 13.446 32.642 1.00 37.28 C ANISOU 1034 CE MET B 130 4464 4847 4854 -32 -30 -89 C ATOM 1035 N ILE A 131 64.695 16.079 38.025 1.00 30.98 N ANISOU 1035 N ILE B 131 3754 4000 4017 -25 2 -56 N ATOM 1036 CA ILE A 131 65.956 16.328 38.717 1.00 31.86 C ANISOU 1036 CA ILE B 131 3892 4070 4143 -32 38 -36 C ATOM 1037 C ILE A 131 66.380 15.066 39.487 1.00 33.56 C ANISOU 1037 C ILE B 131 4022 4286 4440 -129 102 -77 C ATOM 1038 O ILE A 131 67.528 14.627 39.379 1.00 33.47 O ANISOU 1038 O ILE B 131 3905 4261 4551 -200 24 15 O ATOM 1039 CB ILE A 131 65.881 17.530 39.694 1.00 30.98 C ANISOU 1039 CB ILE B 131 3808 3945 4016 20 89 -22 C ATOM 1040 CG1 ILE A 131 65.680 18.837 38.921 1.00 28.79 C ANISOU 1040 CG1 ILE B 131 3456 3578 3904 88 43 100 C ATOM 1041 CG2 ILE A 131 67.160 17.629 40.503 1.00 30.16 C ANISOU 1041 CG2 ILE B 131 3714 3957 3789 -25 84 -12 C ATOM 1042 CD1 ILE A 131 65.160 19.981 39.757 1.00 29.44 C ANISOU 1042 CD1 ILE B 131 3658 3684 3841 89 73 -39 C ATOM 1043 N GLN A 132 65.446 14.514 40.262 1.00 34.59 N ANISOU 1043 N GLN B 132 4077 4360 4702 -67 95 -52 N ATOM 1044 CA GLN A 132 65.703 13.345 41.122 1.00 35.28 C ANISOU 1044 CA GLN B 132 4364 4531 4507 17 150 -14 C ATOM 1045 C GLN A 132 66.056 12.088 40.322 1.00 34.85 C ANISOU 1045 C GLN B 132 4153 4534 4552 101 154 7 C ATOM 1046 O GLN A 132 66.953 11.328 40.708 1.00 35.53 O ANISOU 1046 O GLN B 132 4180 4685 4633 192 112 54 O ATOM 1047 CB GLN A 132 64.506 13.117 42.043 1.00 35.75 C ANISOU 1047 CB GLN B 132 4477 4525 4580 2 132 14 C ATOM 1048 CG GLN A 132 64.443 14.156 43.160 1.00 39.21 C ANISOU 1048 CG GLN B 132 4899 4946 5051 -29 -71 -42 C ATOM 1049 CD GLN A 132 63.125 14.165 43.910 1.00 40.26 C ANISOU 1049 CD GLN B 132 5233 5092 4970 -52 116 -122 C ATOM 1050 OE1 GLN A 132 62.385 13.180 43.901 1.00 48.73 O ANISOU 1050 OE1 GLN B 132 6007 6234 6271 320 -17 -117 O ATOM 1051 NE2 GLN A 132 62.818 15.288 44.563 1.00 49.39 N ANISOU 1051 NE2 GLN B 132 5963 6652 6151 -19 -196 -74 N ATOM 1052 N HIS A 133 65.389 11.907 39.185 1.00 35.53 N ANISOU 1052 N HIS B 133 4191 4640 4669 96 130 -17 N ATOM 1053 CA HIS A 133 65.694 10.829 38.231 1.00 35.71 C ANISOU 1053 CA HIS B 133 4294 4617 4657 45 110 -79 C ATOM 1054 C HIS A 133 67.088 10.960 37.628 1.00 36.78 C ANISOU 1054 C HIS B 133 4306 4671 4995 34 77 -9 C ATOM 1055 O HIS A 133 67.844 9.975 37.560 1.00 36.71 O ANISOU 1055 O HIS B 133 3937 4857 5152 94 113 40 O ATOM 1056 CB HIS A 133 64.641 10.823 37.123 1.00 34.82 C ANISOU 1056 CB HIS B 133 4247 4470 4513 19 89 -64 C ATOM 1057 CG HIS A 133 64.822 9.759 36.086 1.00 36.51 C ANISOU 1057 CG HIS B 133 4375 4777 4720 29 97 -101 C ATOM 1058 ND1 HIS A 133 64.854 8.412 36.391 1.00 37.34 N ANISOU 1058 ND1 HIS B 133 4424 4899 4864 20 91 -108 N ATOM 1059 CD2 HIS A 133 64.909 9.839 34.736 1.00 36.51 C ANISOU 1059 CD2 HIS B 133 4466 4747 4659 31 64 42 C ATOM 1060 CE1 HIS A 133 64.987 7.714 35.276 1.00 38.12 C ANISOU 1060 CE1 HIS B 133 4602 4951 4928 58 8 -63 C ATOM 1061 NE2 HIS A 133 65.018 8.555 34.256 1.00 39.25 N ANISOU 1061 NE2 HIS B 133 4739 5083 5089 -88 94 -61 N ATOM 1062 N ILE A 134 67.431 12.172 37.173 1.00 35.87 N ANISOU 1062 N ILE B 134 4142 4643 4843 7 54 -74 N ATOM 1063 CA ILE A 134 68.754 12.427 36.618 1.00 36.44 C ANISOU 1063 CA ILE B 134 4286 4688 4872 56 78 -74 C ATOM 1064 C ILE A 134 69.854 12.160 37.635 1.00 35.60 C ANISOU 1064 C ILE B 134 4095 4647 4784 94 176 -87 C ATOM 1065 O ILE A 134 70.855 11.545 37.291 1.00 36.45 O ANISOU 1065 O ILE B 134 3998 4901 4947 92 204 -151 O ATOM 1066 CB ILE A 134 68.899 13.876 36.060 1.00 35.23 C ANISOU 1066 CB ILE B 134 4153 4544 4688 -4 134 -39 C ATOM 1067 CG1 ILE A 134 68.104 14.022 34.754 1.00 35.53 C ANISOU 1067 CG1 ILE B 134 4352 4482 4666 108 60 -32 C ATOM 1068 CG2 ILE A 134 70.368 14.201 35.802 1.00 35.48 C ANISOU 1068 CG2 ILE B 134 4048 4624 4807 48 -21 2 C ATOM 1069 CD1 ILE A 134 68.000 15.447 34.264 1.00 36.52 C ANISOU 1069 CD1 ILE B 134 4424 4654 4795 -31 40 15 C ATOM 1070 N LYS A 135 69.677 12.635 38.868 1.00 36.70 N ANISOU 1070 N LYS B 135 4245 4780 4917 75 150 -119 N ATOM 1071 CA LYS A 135 70.685 12.507 39.901 1.00 39.00 C ANISOU 1071 CA LYS B 135 4775 4940 5104 37 72 -4 C ATOM 1072 C LYS A 135 70.874 11.057 40.358 1.00 41.26 C ANISOU 1072 C LYS B 135 4993 5223 5458 30 100 31 C ATOM 1073 O LYS A 135 71.924 10.703 40.925 1.00 42.22 O ANISOU 1073 O LYS B 135 5081 5419 5540 74 229 53 O ATOM 1074 CB LYS A 135 70.330 13.379 41.109 1.00 39.25 C ANISOU 1074 CB LYS B 135 4826 4955 5129 25 69 -37 C ATOM 1075 CG LYS A 135 70.644 14.864 40.917 1.00 39.24 C ANISOU 1075 CG LYS B 135 4789 5015 5106 -24 117 -37 C ATOM 1076 CD LYS A 135 72.139 15.159 41.125 1.00 41.44 C ANISOU 1076 CD LYS B 135 5065 5251 5429 -85 130 138 C ATOM 1077 CE LYS A 135 72.616 16.468 40.467 1.00 40.73 C ANISOU 1077 CE LYS B 135 5072 5089 5311 89 110 0 C ATOM 1078 NZ LYS A 135 74.093 16.502 40.216 1.00 39.73 N ANISOU 1078 NZ LYS B 135 4639 4957 5498 -90 33 71 N ATOM 1079 N LYS A 136 69.861 10.226 40.123 1.00 42.05 N ANISOU 1079 N LYS B 136 5119 5300 5557 28 67 24 N ATOM 1080 CA LYS A 136 69.959 8.793 40.424 1.00 42.50 C ANISOU 1080 CA LYS B 136 5203 5409 5536 15 55 16 C ATOM 1081 C LYS A 136 70.756 8.040 39.352 1.00 42.65 C ANISOU 1081 C LYS B 136 5263 5422 5519 15 37 32 C ATOM 1082 O LYS A 136 71.637 7.244 39.675 1.00 43.48 O ANISOU 1082 O LYS B 136 5371 5527 5623 -46 38 60 O ATOM 1083 CB LYS A 136 68.567 8.181 40.611 1.00 43.37 C ANISOU 1083 CB LYS B 136 5346 5507 5625 19 82 4 C ATOM 1084 CG LYS A 136 67.958 8.495 41.986 1.00 45.54 C ANISOU 1084 CG LYS B 136 5673 5810 5817 -2 48 -54 C ATOM 1085 CD LYS A 136 66.758 7.598 42.344 1.00 45.70 C ANISOU 1085 CD LYS B 136 5726 5731 5908 66 60 -37 C ATOM 1086 CE LYS A 136 65.506 7.892 41.500 1.00 49.79 C ANISOU 1086 CE LYS B 136 6335 6183 6399 -51 31 60 C ATOM 1087 NZ LYS A 136 64.684 9.044 41.985 1.00 49.79 N ANISOU 1087 NZ LYS B 136 6192 6377 6347 -11 -60 -57 N ATOM 1088 N HIS A 137 70.468 8.310 38.086 1.00 41.82 N ANISOU 1088 N HIS B 137 5155 5307 5425 17 108 8 N ATOM 1089 CA HIS A 137 71.053 7.556 36.980 1.00 41.48 C ANISOU 1089 CA HIS B 137 5064 5264 5430 17 44 -25 C ATOM 1090 C HIS A 137 72.340 8.147 36.392 1.00 41.42 C ANISOU 1090 C HIS B 137 5035 5284 5419 -29 20 -94 C ATOM 1091 O HIS A 137 73.125 7.416 35.778 1.00 41.24 O ANISOU 1091 O HIS B 137 4863 5303 5503 32 44 -160 O ATOM 1092 CB HIS A 137 70.013 7.366 35.884 1.00 43.18 C ANISOU 1092 CB HIS B 137 5288 5513 5605 -52 30 35 C ATOM 1093 CG HIS A 137 68.896 6.460 36.292 1.00 47.40 C ANISOU 1093 CG HIS B 137 5914 5878 6217 149 47 -73 C ATOM 1094 ND1 HIS A 137 68.060 6.747 37.352 1.00 48.08 N ANISOU 1094 ND1 HIS B 137 6128 5946 6195 59 -18 -32 N ATOM 1095 CD2 HIS A 137 68.502 5.254 35.814 1.00 48.62 C ANISOU 1095 CD2 HIS B 137 6084 6267 6121 105 -112 -66 C ATOM 1096 CE1 HIS A 137 67.188 5.764 37.496 1.00 48.78 C ANISOU 1096 CE1 HIS B 137 6134 6056 6344 37 37 -148 C ATOM 1097 NE2 HIS A 137 67.429 4.850 36.572 1.00 47.97 N ANISOU 1097 NE2 HIS B 137 5909 6051 6264 200 -45 -20 N ATOM 1098 N LEU A 138 72.552 9.453 36.574 1.00 40.00 N ANISOU 1098 N LEU B 138 4934 5046 5217 -21 -19 -82 N ATOM 1099 CA LEU A 138 73.726 10.147 36.045 1.00 38.90 C ANISOU 1099 CA LEU B 138 4845 4971 4961 -40 7 0 C ATOM 1100 C LEU A 138 74.265 11.090 37.120 1.00 38.38 C ANISOU 1100 C LEU B 138 4787 4955 4839 -46 67 27 C ATOM 1101 O LEU A 138 74.271 12.318 36.953 1.00 37.30 O ANISOU 1101 O LEU B 138 4648 4873 4648 -44 89 68 O ATOM 1102 CB LEU A 138 73.368 10.898 34.748 1.00 37.56 C ANISOU 1102 CB LEU B 138 4718 4758 4793 -84 44 -61 C ATOM 1103 CG LEU A 138 72.771 10.063 33.603 1.00 37.16 C ANISOU 1103 CG LEU B 138 4587 4566 4965 -72 34 -12 C ATOM 1104 CD1 LEU A 138 72.149 10.928 32.546 1.00 35.93 C ANISOU 1104 CD1 LEU B 138 4286 4672 4694 78 -87 -13 C ATOM 1105 CD2 LEU A 138 73.793 9.163 32.910 1.00 37.50 C ANISOU 1105 CD2 LEU B 138 4590 4608 5050 -61 38 -107 C ATOM 1106 N PRO A 139 74.741 10.517 38.243 1.00 38.78 N ANISOU 1106 N PRO B 139 4789 5050 4896 -20 62 54 N ATOM 1107 CA PRO A 139 75.129 11.364 39.366 1.00 37.82 C ANISOU 1107 CA PRO B 139 4674 4902 4794 -22 62 46 C ATOM 1108 C PRO A 139 76.209 12.422 39.070 1.00 37.08 C ANISOU 1108 C PRO B 139 4573 4826 4689 -70 109 49 C ATOM 1109 O PRO A 139 76.280 13.434 39.776 1.00 39.99 O ANISOU 1109 O PRO B 139 4648 5284 5260 -24 229 47 O ATOM 1110 CB PRO A 139 75.659 10.353 40.398 1.00 38.87 C ANISOU 1110 CB PRO B 139 4827 4993 4947 -15 126 40 C ATOM 1111 CG PRO A 139 75.051 9.048 40.005 1.00 38.97 C ANISOU 1111 CG PRO B 139 4852 5121 4833 -56 96 109 C ATOM 1112 CD PRO A 139 74.978 9.084 38.529 1.00 38.58 C ANISOU 1112 CD PRO B 139 4806 5112 4739 -17 45 69 C ATOM 1113 N GLU A 140 77.059 12.192 38.086 1.00 35.55 N ANISOU 1113 N GLU B 140 4246 4649 4610 -120 147 135 N ATOM 1114 CA GLU A 140 78.133 13.130 37.782 1.00 35.40 C ANISOU 1114 CA GLU B 140 4301 4564 4585 -79 97 98 C ATOM 1115 C GLU A 140 77.698 14.277 36.871 1.00 34.35 C ANISOU 1115 C GLU B 140 4148 4375 4526 -76 94 130 C ATOM 1116 O GLU A 140 78.501 15.190 36.625 1.00 33.75 O ANISOU 1116 O GLU B 140 3951 4370 4499 -75 177 344 O ATOM 1117 CB GLU A 140 79.308 12.417 37.111 1.00 37.14 C ANISOU 1117 CB GLU B 140 4436 4786 4888 -15 35 0 C ATOM 1118 CG GLU A 140 79.884 11.289 37.925 1.00 41.93 C ANISOU 1118 CG GLU B 140 5171 5254 5504 -182 228 131 C ATOM 1119 CD GLU A 140 80.425 11.783 39.225 1.00 48.35 C ANISOU 1119 CD GLU B 140 6084 6330 5954 -137 -19 180 C ATOM 1120 OE1 GLU A 140 81.549 12.341 39.223 1.00 54.44 O ANISOU 1120 OE1 GLU B 140 6706 6889 7089 145 161 34 O ATOM 1121 OE2 GLU A 140 79.724 11.622 40.245 1.00 52.88 O ANISOU 1121 OE2 GLU B 140 6797 6485 6808 -120 56 -179 O ATOM 1122 N SER A 141 76.472 14.224 36.338 1.00 32.68 N ANISOU 1122 N SER B 141 3848 4187 4381 -46 57 7 N ATOM 1123 CA SER A 141 75.987 15.299 35.449 1.00 30.60 C ANISOU 1123 CA SER B 141 3708 3939 3979 -50 -28 -22 C ATOM 1124 C SER A 141 75.619 16.567 36.231 1.00 28.97 C ANISOU 1124 C SER B 141 3467 3705 3831 -67 40 -38 C ATOM 1125 O SER A 141 74.937 16.493 37.264 1.00 28.95 O ANISOU 1125 O SER B 141 3424 3677 3898 -76 105 -29 O ATOM 1126 CB SER A 141 74.783 14.842 34.630 1.00 30.58 C ANISOU 1126 CB SER B 141 3697 3890 4032 23 -38 -107 C ATOM 1127 OG SER A 141 75.163 14.048 33.526 1.00 29.54 O ANISOU 1127 OG SER B 141 3676 3744 3805 152 -81 -211 O ATOM 1128 N PHE A 142 76.069 17.726 35.736 1.00 26.39 N ANISOU 1128 N PHE B 142 3193 3280 3553 -71 -44 -80 N ATOM 1129 CA PHE A 142 75.735 19.028 36.365 1.00 26.12 C ANISOU 1129 CA PHE B 142 3228 3252 3445 -16 -21 -5 C ATOM 1130 C PHE A 142 74.354 19.457 35.824 1.00 24.35 C ANISOU 1130 C PHE B 142 2848 3151 3250 -107 64 40 C ATOM 1131 O PHE A 142 74.189 19.665 34.611 1.00 25.61 O ANISOU 1131 O PHE B 142 3112 3259 3360 -30 -201 136 O ATOM 1132 CB PHE A 142 76.815 20.072 36.077 1.00 23.22 C ANISOU 1132 CB PHE B 142 2820 3043 2960 -75 5 3 C ATOM 1133 CG PHE A 142 76.622 21.380 36.803 1.00 25.33 C ANISOU 1133 CG PHE B 142 3125 3098 3400 -70 -7 29 C ATOM 1134 CD1 PHE A 142 77.392 21.694 37.928 1.00 24.63 C ANISOU 1134 CD1 PHE B 142 2853 3200 3304 -96 -256 -16 C ATOM 1135 CD2 PHE A 142 75.694 22.309 36.338 1.00 24.71 C ANISOU 1135 CD2 PHE B 142 2928 3056 3402 24 -60 159 C ATOM 1136 CE1 PHE A 142 77.229 22.907 38.592 1.00 24.18 C ANISOU 1136 CE1 PHE B 142 2762 2879 3544 23 -37 118 C ATOM 1137 CE2 PHE A 142 75.528 23.531 36.979 1.00 23.36 C ANISOU 1137 CE2 PHE B 142 2940 2899 3033 -317 -109 40 C ATOM 1138 CZ PHE A 142 76.279 23.838 38.107 1.00 23.30 C ANISOU 1138 CZ PHE B 142 2575 2923 3354 57 128 222 C ATOM 1139 N VAL A 143 73.376 19.540 36.723 1.00 24.02 N ANISOU 1139 N VAL B 143 2744 3303 3076 -204 -124 70 N ATOM 1140 CA VAL A 143 71.967 19.748 36.363 1.00 23.12 C ANISOU 1140 CA VAL B 143 2660 3076 3046 -92 -182 14 C ATOM 1141 C VAL A 143 71.498 21.211 36.590 1.00 22.87 C ANISOU 1141 C VAL B 143 2637 3072 2978 -160 -68 26 C ATOM 1142 O VAL A 143 71.498 21.718 37.702 1.00 23.58 O ANISOU 1142 O VAL B 143 2273 3226 3459 -174 -391 -136 O ATOM 1143 CB VAL A 143 71.033 18.780 37.119 1.00 23.69 C ANISOU 1143 CB VAL B 143 2828 3200 2972 -217 -157 44 C ATOM 1144 CG1 VAL A 143 69.568 19.089 36.842 1.00 24.38 C ANISOU 1144 CG1 VAL B 143 2885 3067 3309 -112 -31 -84 C ATOM 1145 CG2 VAL A 143 71.330 17.309 36.749 1.00 24.57 C ANISOU 1145 CG2 VAL B 143 2880 3304 3152 21 17 -57 C ATOM 1146 N ILE A 144 71.047 21.828 35.518 1.00 23.41 N ANISOU 1146 N ILE B 144 2683 2917 3294 -100 4 -83 N ATOM 1147 CA ILE A 144 70.545 23.219 35.518 1.00 22.43 C ANISOU 1147 CA ILE B 144 2662 2827 3032 -70 -101 -73 C ATOM 1148 C ILE A 144 69.047 23.055 35.344 1.00 21.81 C ANISOU 1148 C ILE B 144 2738 2657 2891 -46 -160 -115 C ATOM 1149 O ILE A 144 68.606 22.364 34.439 1.00 23.05 O ANISOU 1149 O ILE B 144 3249 2931 2576 -78 -105 -29 O ATOM 1150 CB ILE A 144 71.120 23.994 34.306 1.00 22.56 C ANISOU 1150 CB ILE B 144 2756 2860 2954 47 -82 14 C ATOM 1151 CG1 ILE A 144 72.651 24.119 34.425 1.00 23.72 C ANISOU 1151 CG1 ILE B 144 2825 2966 3219 46 89 -115 C ATOM 1152 CG2 ILE A 144 70.443 25.358 34.136 1.00 21.45 C ANISOU 1152 CG2 ILE B 144 2602 2624 2922 16 -33 130 C ATOM 1153 CD1 ILE A 144 73.331 24.285 33.081 1.00 22.75 C ANISOU 1153 CD1 ILE B 144 2612 2814 3217 -79 -151 -153 C ATOM 1154 N ALA A 145 68.251 23.606 36.242 1.00 21.30 N ANISOU 1154 N ALA B 145 2563 2781 2747 23 -39 -142 N ATOM 1155 CA ALA A 145 66.799 23.414 36.153 1.00 20.26 C ANISOU 1155 CA ALA B 145 2542 2595 2561 -27 -74 -63 C ATOM 1156 C ALA A 145 66.074 24.756 36.033 1.00 20.69 C ANISOU 1156 C ALA B 145 2594 2628 2640 19 13 62 C ATOM 1157 O ALA A 145 66.386 25.719 36.747 1.00 20.85 O ANISOU 1157 O ALA B 145 2445 2556 2919 54 -70 -73 O ATOM 1158 CB ALA A 145 66.302 22.661 37.425 1.00 21.23 C ANISOU 1158 CB ALA B 145 2617 2673 2773 133 92 35 C ATOM 1159 N GLY A 146 65.029 24.776 35.216 1.00 20.74 N ANISOU 1159 N GLY B 146 2607 2829 2442 2 -11 -86 N ATOM 1160 CA GLY A 146 64.225 25.960 35.051 1.00 19.53 C ANISOU 1160 CA GLY B 146 2539 2474 2407 13 -2 -100 C ATOM 1161 C GLY A 146 63.112 25.760 34.058 1.00 20.15 C ANISOU 1161 C GLY B 146 2638 2648 2370 45 -34 -33 C ATOM 1162 O GLY A 146 62.874 24.619 33.595 1.00 20.64 O ANISOU 1162 O GLY B 146 2701 2701 2439 242 -157 149 O ATOM 1163 N ASN A 147 62.399 26.831 33.727 1.00 18.97 N ANISOU 1163 N ASN B 147 2478 2379 2351 24 11 56 N ATOM 1164 CA ASN A 147 62.671 28.192 34.155 1.00 19.59 C ANISOU 1164 CA ASN B 147 2627 2349 2466 25 5 0 C ATOM 1165 C ASN A 147 61.789 28.559 35.348 1.00 20.32 C ANISOU 1165 C ASN B 147 2711 2395 2612 104 79 -4 C ATOM 1166 O ASN A 147 60.642 28.102 35.447 1.00 20.03 O ANISOU 1166 O ASN B 147 2948 2232 2429 188 321 -58 O ATOM 1167 CB ASN A 147 62.449 29.186 32.985 1.00 19.00 C ANISOU 1167 CB ASN B 147 2570 2315 2334 -173 -29 64 C ATOM 1168 CG ASN A 147 63.693 29.389 32.097 1.00 22.43 C ANISOU 1168 CG ASN B 147 2793 2754 2973 66 15 47 C ATOM 1169 OD1 ASN A 147 64.467 28.466 31.868 1.00 24.06 O ANISOU 1169 OD1 ASN B 147 3035 2809 3298 31 22 -67 O ATOM 1170 ND2 ASN A 147 63.859 30.620 31.563 1.00 21.17 N ANISOU 1170 ND2 ASN B 147 2961 2645 2436 23 -58 12 N ATOM 1171 N VAL A 148 62.326 29.394 36.234 1.00 19.35 N ANISOU 1171 N VAL B 148 2641 2249 2462 -18 206 27 N ATOM 1172 CA VAL A 148 61.639 29.859 37.397 1.00 19.48 C ANISOU 1172 CA VAL B 148 2525 2419 2454 0 75 11 C ATOM 1173 C VAL A 148 61.651 31.382 37.507 1.00 19.06 C ANISOU 1173 C VAL B 148 2486 2464 2291 80 130 -62 C ATOM 1174 O VAL A 148 62.429 32.059 36.852 1.00 16.57 O ANISOU 1174 O VAL B 148 2378 2447 1468 93 138 -161 O ATOM 1175 CB VAL A 148 62.226 29.225 38.665 1.00 20.55 C ANISOU 1175 CB VAL B 148 2745 2649 2411 76 121 -53 C ATOM 1176 CG1 VAL A 148 62.146 27.714 38.559 1.00 22.16 C ANISOU 1176 CG1 VAL B 148 2763 2940 2715 -172 -54 -186 C ATOM 1177 CG2 VAL A 148 63.671 29.671 38.935 1.00 20.07 C ANISOU 1177 CG2 VAL B 148 2875 2569 2179 -26 185 -100 C ATOM 1178 N GLY A 149 60.805 31.909 38.384 1.00 19.64 N ANISOU 1178 N GLY B 149 2379 2543 2537 37 247 -135 N ATOM 1179 CA GLY A 149 60.699 33.339 38.558 1.00 20.51 C ANISOU 1179 CA GLY B 149 2576 2568 2646 -44 -5 -112 C ATOM 1180 C GLY A 149 60.539 33.834 39.957 1.00 20.15 C ANISOU 1180 C GLY B 149 2538 2395 2720 14 7 -93 C ATOM 1181 O GLY A 149 60.347 35.017 40.134 1.00 22.78 O ANISOU 1181 O GLY B 149 2691 2865 3096 -187 -157 -188 O ATOM 1182 N THR A 150 60.659 32.943 40.940 1.00 20.48 N ANISOU 1182 N THR B 150 2656 2322 2804 -41 11 -85 N ATOM 1183 CA THR A 150 60.504 33.286 42.319 1.00 20.09 C ANISOU 1183 CA THR B 150 2595 2432 2605 -56 -64 -49 C ATOM 1184 C THR A 150 61.574 32.617 43.186 1.00 20.76 C ANISOU 1184 C THR B 150 2670 2646 2569 -99 -27 1 C ATOM 1185 O THR A 150 62.121 31.565 42.829 1.00 19.31 O ANISOU 1185 O THR B 150 2652 2624 2061 -168 40 -36 O ATOM 1186 CB THR A 150 59.116 32.867 42.920 1.00 19.50 C ANISOU 1186 CB THR B 150 2379 2235 2793 -18 8 -75 C ATOM 1187 OG1 THR A 150 59.025 31.453 43.024 1.00 19.86 O ANISOU 1187 OG1 THR B 150 2219 2297 3027 123 305 -65 O ATOM 1188 CG2 THR A 150 57.943 33.391 42.098 1.00 16.68 C ANISOU 1188 CG2 THR B 150 2451 2074 1811 15 16 -336 C ATOM 1189 N PRO A 151 61.892 33.252 44.327 1.00 21.23 N ANISOU 1189 N PRO B 151 2811 2758 2495 -98 -92 -67 N ATOM 1190 CA PRO A 151 62.780 32.645 45.330 1.00 23.04 C ANISOU 1190 CA PRO B 151 2946 2994 2813 -105 -21 25 C ATOM 1191 C PRO A 151 62.308 31.314 45.945 1.00 23.73 C ANISOU 1191 C PRO B 151 2897 3003 3113 -1 25 -33 C ATOM 1192 O PRO A 151 63.150 30.448 46.253 1.00 24.77 O ANISOU 1192 O PRO B 151 2953 3308 3149 24 181 -181 O ATOM 1193 CB PRO A 151 62.856 33.713 46.445 1.00 23.02 C ANISOU 1193 CB PRO B 151 2952 2996 2799 -48 -91 -33 C ATOM 1194 CG PRO A 151 61.799 34.680 46.161 1.00 19.67 C ANISOU 1194 CG PRO B 151 2639 2731 2103 -122 46 -66 C ATOM 1195 CD PRO A 151 61.529 34.640 44.671 1.00 21.06 C ANISOU 1195 CD PRO B 151 2962 2764 2273 -181 -122 -161 C ATOM 1196 N GLU A 152 61.003 31.162 46.168 1.00 24.22 N ANISOU 1196 N GLU B 152 2930 3202 3068 -91 -98 -139 N ATOM 1197 CA GLU A 152 60.463 29.880 46.628 1.00 24.00 C ANISOU 1197 CA GLU B 152 2972 3082 3062 -40 -64 -49 C ATOM 1198 C GLU A 152 60.741 28.789 45.575 1.00 23.16 C ANISOU 1198 C GLU B 152 2977 2918 2901 -1 -80 -18 C ATOM 1199 O GLU A 152 61.066 27.664 45.926 1.00 23.34 O ANISOU 1199 O GLU B 152 2843 3043 2983 84 -5 -49 O ATOM 1200 CB GLU A 152 58.967 29.936 46.951 1.00 25.19 C ANISOU 1200 CB GLU B 152 3072 3382 3114 9 -46 -164 C ATOM 1201 CG GLU A 152 58.105 30.601 45.948 1.00 30.43 C ANISOU 1201 CG GLU B 152 4076 3751 3735 -4 96 -34 C ATOM 1202 CD GLU A 152 57.846 32.117 46.206 1.00 34.98 C ANISOU 1202 CD GLU B 152 4329 4558 4402 120 -181 -146 C ATOM 1203 OE1 GLU A 152 58.805 32.944 46.338 1.00 27.64 O ANISOU 1203 OE1 GLU B 152 3984 3561 2954 -16 -310 -241 O ATOM 1204 OE2 GLU A 152 56.643 32.481 46.224 1.00 42.72 O ANISOU 1204 OE2 GLU B 152 6004 4963 5265 -160 -57 32 O ATOM 1205 N ALA A 153 60.632 29.120 44.294 1.00 23.37 N ANISOU 1205 N ALA B 153 2958 2836 3085 -5 45 -4 N ATOM 1206 CA ALA A 153 60.916 28.133 43.241 1.00 22.57 C ANISOU 1206 CA ALA B 153 2812 2876 2887 -10 -14 29 C ATOM 1207 C ALA A 153 62.387 27.756 43.191 1.00 21.86 C ANISOU 1207 C ALA B 153 2732 2728 2846 -18 70 121 C ATOM 1208 O ALA A 153 62.728 26.573 43.022 1.00 22.09 O ANISOU 1208 O ALA B 153 2729 2800 2863 41 91 -76 O ATOM 1209 CB ALA A 153 60.489 28.646 41.855 1.00 21.46 C ANISOU 1209 CB ALA B 153 2565 2511 3074 -60 75 155 C ATOM 1210 N VAL A 154 63.265 28.755 43.268 1.00 21.96 N ANISOU 1210 N VAL B 154 2639 2843 2858 -72 163 126 N ATOM 1211 CA VAL A 154 64.715 28.487 43.249 1.00 22.82 C ANISOU 1211 CA VAL B 154 2874 2963 2831 0 92 55 C ATOM 1212 C VAL A 154 65.035 27.506 44.396 1.00 23.77 C ANISOU 1212 C VAL B 154 2914 3157 2958 -58 185 41 C ATOM 1213 O VAL A 154 65.701 26.479 44.194 1.00 23.49 O ANISOU 1213 O VAL B 154 2898 3147 2878 -137 492 21 O ATOM 1214 CB VAL A 154 65.554 29.792 43.367 1.00 20.62 C ANISOU 1214 CB VAL B 154 2810 2685 2338 55 176 116 C ATOM 1215 CG1 VAL A 154 67.035 29.468 43.610 1.00 21.77 C ANISOU 1215 CG1 VAL B 154 2970 2738 2564 -151 72 -246 C ATOM 1216 CG2 VAL A 154 65.392 30.670 42.100 1.00 21.55 C ANISOU 1216 CG2 VAL B 154 2329 3043 2814 113 40 210 C ATOM 1217 N ARG A 155 64.517 27.832 45.576 1.00 24.87 N ANISOU 1217 N ARG B 155 3088 3311 3047 -34 169 36 N ATOM 1218 CA ARG A 155 64.714 27.029 46.800 1.00 26.24 C ANISOU 1218 CA ARG B 155 3307 3404 3258 -13 184 12 C ATOM 1219 C ARG A 155 64.265 25.591 46.634 1.00 25.56 C ANISOU 1219 C ARG B 155 3180 3383 3147 -26 60 54 C ATOM 1220 O ARG A 155 65.001 24.659 46.968 1.00 25.33 O ANISOU 1220 O ARG B 155 3250 3207 3167 -82 1 30 O ATOM 1221 CB ARG A 155 63.891 27.613 47.935 1.00 28.36 C ANISOU 1221 CB ARG B 155 3578 3712 3485 -72 174 -75 C ATOM 1222 CG ARG A 155 64.474 28.768 48.625 1.00 35.72 C ANISOU 1222 CG ARG B 155 4504 4296 4770 117 -71 142 C ATOM 1223 CD ARG A 155 64.933 28.386 50.026 1.00 46.28 C ANISOU 1223 CD ARG B 155 6218 6032 5332 -188 200 -14 C ATOM 1224 NE ARG A 155 66.124 29.165 50.353 1.00 50.18 N ANISOU 1224 NE ARG B 155 6469 6207 6389 183 -205 48 N ATOM 1225 CZ ARG A 155 66.174 30.213 51.168 1.00 50.49 C ANISOU 1225 CZ ARG B 155 6386 6299 6496 25 -114 11 C ATOM 1226 NH1 ARG A 155 65.100 30.645 51.834 1.00 51.69 N ANISOU 1226 NH1 ARG B 155 6696 6333 6611 28 -96 -8 N ATOM 1227 NH2 ARG A 155 67.338 30.819 51.336 1.00 50.79 N ANISOU 1227 NH2 ARG B 155 6470 6353 6473 35 -95 -17 N ATOM 1228 N GLU A 156 63.047 25.425 46.126 1.00 26.67 N ANISOU 1228 N GLU B 156 3285 3351 3497 4 114 20 N ATOM 1229 CA GLU A 156 62.453 24.093 45.936 1.00 26.48 C ANISOU 1229 CA GLU B 156 3288 3376 3396 12 121 -8 C ATOM 1230 C GLU A 156 63.268 23.284 44.934 1.00 26.21 C ANISOU 1230 C GLU B 156 3256 3355 3348 16 167 39 C ATOM 1231 O GLU A 156 63.506 22.093 45.132 1.00 26.98 O ANISOU 1231 O GLU B 156 3152 3424 3674 143 320 -97 O ATOM 1232 CB GLU A 156 60.972 24.173 45.521 1.00 26.11 C ANISOU 1232 CB GLU B 156 3288 3472 3158 31 82 89 C ATOM 1233 CG GLU A 156 60.156 22.911 45.962 1.00 27.62 C ANISOU 1233 CG GLU B 156 3548 3485 3461 73 51 69 C ATOM 1234 CD GLU A 156 58.656 22.968 45.686 1.00 28.59 C ANISOU 1234 CD GLU B 156 3633 3488 3741 91 64 -63 C ATOM 1235 OE1 GLU A 156 58.148 24.031 45.287 1.00 32.83 O ANISOU 1235 OE1 GLU B 156 4037 3826 4609 -108 306 105 O ATOM 1236 OE2 GLU A 156 57.983 21.915 45.863 1.00 30.43 O ANISOU 1236 OE2 GLU B 156 3860 3894 3805 132 354 -66 O ATOM 1237 N LEU A 157 63.752 23.932 43.877 1.00 25.47 N ANISOU 1237 N LEU B 157 3148 3258 3270 2 200 0 N ATOM 1238 CA LEU A 157 64.526 23.217 42.866 1.00 25.54 C ANISOU 1238 CA LEU B 157 3143 3281 3279 21 83 -17 C ATOM 1239 C LEU A 157 65.938 22.867 43.360 1.00 24.76 C ANISOU 1239 C LEU B 157 3090 3354 2963 -81 131 40 C ATOM 1240 O LEU A 157 66.425 21.755 43.107 1.00 23.78 O ANISOU 1240 O LEU B 157 2991 3317 2726 -80 30 -54 O ATOM 1241 CB LEU A 157 64.572 24.004 41.559 1.00 25.47 C ANISOU 1241 CB LEU B 157 3259 3398 3021 43 41 -18 C ATOM 1242 CG LEU A 157 63.525 23.717 40.473 1.00 28.32 C ANISOU 1242 CG LEU B 157 3571 3643 3545 7 142 50 C ATOM 1243 CD1 LEU A 157 62.122 23.489 40.949 1.00 32.34 C ANISOU 1243 CD1 LEU B 157 4447 3874 3965 -145 108 -23 C ATOM 1244 CD2 LEU A 157 63.603 24.760 39.400 1.00 24.61 C ANISOU 1244 CD2 LEU B 157 2898 3242 3210 -83 -91 -3 C ATOM 1245 N GLU A 158 66.587 23.811 44.045 1.00 25.74 N ANISOU 1245 N GLU B 158 3163 3327 3291 -83 147 9 N ATOM 1246 CA GLU A 158 67.884 23.566 44.671 1.00 27.46 C ANISOU 1246 CA GLU B 158 3423 3480 3528 -21 53 67 C ATOM 1247 C GLU A 158 67.770 22.402 45.669 1.00 30.06 C ANISOU 1247 C GLU B 158 3671 3818 3931 -91 76 9 C ATOM 1248 O GLU A 158 68.563 21.454 45.638 1.00 30.65 O ANISOU 1248 O GLU B 158 3732 3777 4135 -212 138 81 O ATOM 1249 CB GLU A 158 68.370 24.836 45.373 1.00 27.58 C ANISOU 1249 CB GLU B 158 3375 3420 3682 -93 108 66 C ATOM 1250 CG GLU A 158 68.870 25.929 44.382 1.00 24.78 C ANISOU 1250 CG GLU B 158 3007 2971 3435 -215 70 -5 C ATOM 1251 CD GLU A 158 69.491 27.111 45.080 1.00 25.75 C ANISOU 1251 CD GLU B 158 3321 3269 3192 -104 98 82 C ATOM 1252 OE1 GLU A 158 69.486 27.124 46.346 1.00 26.93 O ANISOU 1252 OE1 GLU B 158 3406 3622 3202 -193 -305 -90 O ATOM 1253 OE2 GLU A 158 70.032 28.011 44.382 1.00 25.66 O ANISOU 1253 OE2 GLU B 158 2945 3807 2997 275 -252 40 O ATOM 1254 N ASN A 159 66.769 22.480 46.541 1.00 31.05 N ANISOU 1254 N ASN B 159 3782 3863 4152 6 59 1 N ATOM 1255 CA ASN A 159 66.494 21.428 47.495 1.00 31.52 C ANISOU 1255 CA ASN B 159 3945 4041 3990 19 130 32 C ATOM 1256 C ASN A 159 66.205 20.049 46.811 1.00 31.54 C ANISOU 1256 C ASN B 159 3932 4096 3955 -21 144 77 C ATOM 1257 O ASN A 159 66.627 19.018 47.326 1.00 33.36 O ANISOU 1257 O ASN B 159 4060 4321 4294 -65 96 175 O ATOM 1258 CB ASN A 159 65.373 21.874 48.451 1.00 33.45 C ANISOU 1258 CB ASN B 159 4090 4336 4281 -33 135 41 C ATOM 1259 CG ASN A 159 65.813 22.999 49.428 1.00 39.60 C ANISOU 1259 CG ASN B 159 5014 5064 4966 -84 -174 -136 C ATOM 1260 OD1 ASN A 159 67.007 23.334 49.544 1.00 45.84 O ANISOU 1260 OD1 ASN B 159 6201 5400 5815 265 -123 101 O ATOM 1261 ND2 ASN A 159 64.834 23.583 50.136 1.00 36.92 N ANISOU 1261 ND2 ASN B 159 4562 4824 4639 -155 68 -130 N ATOM 1262 N ALA A 160 65.557 20.018 45.637 1.00 30.92 N ANISOU 1262 N ALA B 160 3788 4013 3947 -39 78 -31 N ATOM 1263 CA ALA A 160 65.329 18.757 44.917 1.00 30.28 C ANISOU 1263 CA ALA B 160 3765 3889 3849 46 155 16 C ATOM 1264 C ALA A 160 66.617 18.136 44.383 1.00 30.62 C ANISOU 1264 C ALA B 160 3706 3948 3977 43 125 0 C ATOM 1265 O ALA A 160 66.619 16.957 44.009 1.00 32.31 O ANISOU 1265 O ALA B 160 3774 4231 4270 154 218 14 O ATOM 1266 CB ALA A 160 64.319 18.934 43.743 1.00 29.76 C ANISOU 1266 CB ALA B 160 3708 3696 3903 86 156 63 C ATOM 1267 N GLY A 161 67.698 18.918 44.326 1.00 28.70 N ANISOU 1267 N GLY B 161 3368 3759 3775 69 223 -46 N ATOM 1268 CA GLY A 161 68.985 18.449 43.827 1.00 28.45 C ANISOU 1268 CA GLY B 161 3338 3759 3711 -7 144 -5 C ATOM 1269 C GLY A 161 69.581 19.192 42.630 1.00 28.83 C ANISOU 1269 C GLY B 161 3449 3664 3840 -19 147 -44 C ATOM 1270 O GLY A 161 70.648 18.811 42.136 1.00 29.83 O ANISOU 1270 O GLY B 161 3488 3754 4089 -197 102 -64 O ATOM 1271 N ALA A 162 68.925 20.235 42.121 1.00 27.58 N ANISOU 1271 N ALA B 162 3299 3517 3663 -16 129 -50 N ATOM 1272 CA ALA A 162 69.520 20.969 40.977 1.00 26.10 C ANISOU 1272 CA ALA B 162 3103 3327 3487 -16 130 60 C ATOM 1273 C ALA A 162 70.867 21.552 41.373 1.00 24.07 C ANISOU 1273 C ALA B 162 2715 3248 3182 -115 222 46 C ATOM 1274 O ALA A 162 71.007 22.002 42.488 1.00 22.59 O ANISOU 1274 O ALA B 162 2434 3201 2946 -80 332 434 O ATOM 1275 CB ALA A 162 68.573 22.078 40.499 1.00 27.51 C ANISOU 1275 CB ALA B 162 3250 3391 3809 -14 187 -5 C ATOM 1276 N ASP A 163 71.853 21.553 40.476 1.00 23.53 N ANISOU 1276 N ASP B 163 2738 3056 3146 -83 93 15 N ATOM 1277 CA ASP A 163 73.145 22.244 40.753 1.00 23.22 C ANISOU 1277 CA ASP B 163 2728 3015 3079 -57 56 87 C ATOM 1278 C ASP A 163 73.156 23.738 40.338 1.00 21.48 C ANISOU 1278 C ASP B 163 2571 2730 2860 2 123 85 C ATOM 1279 O ASP A 163 74.077 24.492 40.672 1.00 20.50 O ANISOU 1279 O ASP B 163 2288 2646 2854 -227 215 242 O ATOM 1280 CB ASP A 163 74.290 21.513 40.073 1.00 23.99 C ANISOU 1280 CB ASP B 163 2875 3076 3164 108 -26 84 C ATOM 1281 CG ASP A 163 74.356 20.069 40.475 1.00 24.55 C ANISOU 1281 CG ASP B 163 2982 3439 2906 -166 119 231 C ATOM 1282 OD1 ASP A 163 74.623 19.829 41.687 1.00 25.39 O ANISOU 1282 OD1 ASP B 163 2467 3905 3272 -529 624 210 O ATOM 1283 OD2 ASP A 163 74.094 19.203 39.604 1.00 27.59 O ANISOU 1283 OD2 ASP B 163 2859 3882 3739 -417 -240 -104 O ATOM 1284 N ALA A 164 72.140 24.138 39.589 1.00 20.31 N ANISOU 1284 N ALA B 164 2415 2514 2785 -70 113 70 N ATOM 1285 CA ALA A 164 71.903 25.543 39.245 1.00 21.94 C ANISOU 1285 CA ALA B 164 2598 2717 3019 -31 22 51 C ATOM 1286 C ALA A 164 70.456 25.699 38.812 1.00 22.18 C ANISOU 1286 C ALA B 164 2607 2733 3086 -79 -6 185 C ATOM 1287 O ALA A 164 69.808 24.712 38.485 1.00 21.67 O ANISOU 1287 O ALA B 164 2472 2403 3355 -77 -7 350 O ATOM 1288 CB ALA A 164 72.794 25.971 38.121 1.00 21.07 C ANISOU 1288 CB ALA B 164 2496 2787 2721 -85 39 -31 C ATOM 1289 N THR A 165 69.967 26.938 38.799 1.00 22.01 N ANISOU 1289 N THR B 165 2593 2828 2939 -28 75 155 N ATOM 1290 CA THR A 165 68.630 27.236 38.295 1.00 20.74 C ANISOU 1290 CA THR B 165 2546 2605 2728 20 28 78 C ATOM 1291 C THR A 165 68.683 28.292 37.195 1.00 19.42 C ANISOU 1291 C THR B 165 2347 2486 2543 -16 98 85 C ATOM 1292 O THR A 165 69.601 29.131 37.165 1.00 18.94 O ANISOU 1292 O THR B 165 2009 2591 2594 -116 196 198 O ATOM 1293 CB THR A 165 67.643 27.694 39.389 1.00 20.96 C ANISOU 1293 CB THR B 165 2641 2712 2609 40 -43 134 C ATOM 1294 OG1 THR A 165 68.113 28.882 40.036 1.00 20.37 O ANISOU 1294 OG1 THR B 165 2594 2415 2730 -193 132 607 O ATOM 1295 CG2 THR A 165 67.415 26.585 40.409 1.00 18.97 C ANISOU 1295 CG2 THR B 165 2424 2240 2543 255 -126 134 C ATOM 1296 N LYS A 166 67.716 28.243 36.288 1.00 18.61 N ANISOU 1296 N LYS B 166 2228 2359 2482 93 -123 -79 N ATOM 1297 CA LYS A 166 67.629 29.240 35.225 1.00 18.74 C ANISOU 1297 CA LYS B 166 2398 2308 2412 -55 -59 28 C ATOM 1298 C LYS A 166 66.401 30.130 35.439 1.00 18.65 C ANISOU 1298 C LYS B 166 2514 2263 2308 -39 -111 -67 C ATOM 1299 O LYS A 166 65.262 29.633 35.522 1.00 19.58 O ANISOU 1299 O LYS B 166 2808 2219 2410 -215 70 -165 O ATOM 1300 CB LYS A 166 67.629 28.576 33.832 1.00 19.08 C ANISOU 1300 CB LYS B 166 2409 2352 2487 12 -105 -249 C ATOM 1301 CG LYS A 166 67.673 29.544 32.673 1.00 17.49 C ANISOU 1301 CG LYS B 166 2110 2015 2520 -203 -86 43 C ATOM 1302 CD LYS A 166 68.582 29.101 31.526 1.00 19.21 C ANISOU 1302 CD LYS B 166 2478 2329 2490 -102 -93 50 C ATOM 1303 CE LYS A 166 67.985 27.982 30.651 1.00 19.42 C ANISOU 1303 CE LYS B 166 2253 2481 2641 -243 -62 107 C ATOM 1304 NZ LYS A 166 66.641 28.266 30.131 1.00 20.42 N ANISOU 1304 NZ LYS B 166 2530 2759 2468 -107 -465 35 N ATOM 1305 N VAL A 167 66.658 31.429 35.533 1.00 17.92 N ANISOU 1305 N VAL B 167 2309 2189 2309 -79 111 -77 N ATOM 1306 CA VAL A 167 65.668 32.419 36.005 1.00 17.81 C ANISOU 1306 CA VAL B 167 2330 2130 2306 6 -16 -143 C ATOM 1307 C VAL A 167 65.191 33.335 34.872 1.00 17.14 C ANISOU 1307 C VAL B 167 2293 2086 2132 -80 -40 -116 C ATOM 1308 O VAL A 167 66.015 33.960 34.137 1.00 14.48 O ANISOU 1308 O VAL B 167 1989 1999 1514 -120 374 143 O ATOM 1309 CB VAL A 167 66.233 33.254 37.223 1.00 19.87 C ANISOU 1309 CB VAL B 167 2638 2238 2672 45 -20 -134 C ATOM 1310 CG1 VAL A 167 65.305 34.424 37.601 1.00 18.75 C ANISOU 1310 CG1 VAL B 167 2416 2460 2248 151 35 -320 C ATOM 1311 CG2 VAL A 167 66.461 32.387 38.400 1.00 21.14 C ANISOU 1311 CG2 VAL B 167 2846 2269 2915 71 0 -139 C ATOM 1312 N GLY A 168 63.862 33.419 34.727 1.00 17.71 N ANISOU 1312 N GLY B 168 2526 2232 1968 76 -43 39 N ATOM 1313 CA GLY A 168 63.215 34.193 33.635 1.00 18.84 C ANISOU 1313 CA GLY B 168 2442 2332 2381 -68 42 -71 C ATOM 1314 C GLY A 168 61.939 33.511 33.173 1.00 18.72 C ANISOU 1314 C GLY B 168 2427 2567 2116 -84 -4 137 C ATOM 1315 O GLY A 168 61.970 32.338 32.832 1.00 19.11 O ANISOU 1315 O GLY B 168 2544 2467 2247 -169 -53 222 O ATOM 1316 N ILE A 169 60.811 34.231 33.219 1.00 19.09 N ANISOU 1316 N ILE B 169 2446 2505 2302 -49 19 -47 N ATOM 1317 CA ILE A 169 59.519 33.732 32.773 1.00 20.99 C ANISOU 1317 CA ILE B 169 2719 2625 2632 -32 -42 -9 C ATOM 1318 C ILE A 169 58.920 34.787 31.830 1.00 22.43 C ANISOU 1318 C ILE B 169 2838 2705 2977 -32 -70 52 C ATOM 1319 O ILE A 169 58.349 35.784 32.265 1.00 20.78 O ANISOU 1319 O ILE B 169 2737 2255 2900 -62 -23 233 O ATOM 1320 CB ILE A 169 58.563 33.465 33.947 1.00 20.76 C ANISOU 1320 CB ILE B 169 2678 2380 2828 -64 24 -96 C ATOM 1321 CG1 ILE A 169 59.140 32.448 34.951 1.00 22.26 C ANISOU 1321 CG1 ILE B 169 3027 2449 2979 -67 -142 4 C ATOM 1322 CG2 ILE A 169 57.227 33.006 33.434 1.00 21.69 C ANISOU 1322 CG2 ILE B 169 2563 2792 2885 -50 -2 22 C ATOM 1323 CD1 ILE A 169 59.080 31.015 34.511 1.00 25.65 C ANISOU 1323 CD1 ILE B 169 3124 3124 3495 -57 2 48 C ATOM 1324 N GLY A 170 59.100 34.566 30.535 1.00 23.73 N ANISOU 1324 N GLY B 170 3018 3001 2995 -2 -21 7 N ATOM 1325 CA GLY A 170 58.721 35.531 29.497 1.00 25.13 C ANISOU 1325 CA GLY B 170 3145 3145 3255 -48 86 19 C ATOM 1326 C GLY A 170 59.315 36.908 29.799 1.00 25.96 C ANISOU 1326 C GLY B 170 3192 3317 3352 31 77 12 C ATOM 1327 O GLY A 170 58.570 37.858 30.077 1.00 25.00 O ANISOU 1327 O GLY B 170 3148 3178 3170 12 370 205 O ATOM 1328 N PRO A 171 60.660 37.003 29.798 1.00 26.57 N ANISOU 1328 N PRO B 171 3332 3344 3417 28 169 -48 N ATOM 1329 CA PRO A 171 61.350 38.204 30.249 1.00 28.88 C ANISOU 1329 CA PRO B 171 3661 3565 3745 32 27 20 C ATOM 1330 C PRO A 171 61.222 39.395 29.296 1.00 31.15 C ANISOU 1330 C PRO B 171 3931 3891 4012 9 35 39 C ATOM 1331 O PRO A 171 61.320 40.543 29.737 1.00 32.93 O ANISOU 1331 O PRO B 171 4101 4165 4245 -4 -198 148 O ATOM 1332 CB PRO A 171 62.809 37.757 30.333 1.00 29.22 C ANISOU 1332 CB PRO B 171 3745 3605 3749 24 63 70 C ATOM 1333 CG PRO A 171 62.930 36.684 29.339 1.00 28.94 C ANISOU 1333 CG PRO B 171 3719 3494 3783 -60 40 47 C ATOM 1334 CD PRO A 171 61.607 35.955 29.385 1.00 26.99 C ANISOU 1334 CD PRO B 171 3456 3543 3254 139 114 -258 C ATOM 1335 N GLY A 172 61.012 39.144 28.009 1.00 31.96 N ANISOU 1335 N GLY B 172 4076 3999 4065 35 -31 97 N ATOM 1336 CA GLY A 172 60.910 40.240 27.046 1.00 32.68 C ANISOU 1336 CA GLY B 172 4144 4110 4163 33 76 44 C ATOM 1337 C GLY A 172 59.684 41.118 27.248 1.00 33.76 C ANISOU 1337 C GLY B 172 4165 4316 4347 7 -24 -23 C ATOM 1338 O GLY A 172 58.625 40.653 27.685 1.00 34.04 O ANISOU 1338 O GLY B 172 4122 4299 4511 48 -107 58 O ATOM 1339 N LYS A 173 59.820 42.392 26.880 1.00 35.23 N ANISOU 1339 N LYS B 173 4336 4444 4606 49 -19 -8 N ATOM 1340 CA LYS A 173 58.803 43.411 27.188 1.00 35.88 C ANISOU 1340 CA LYS B 173 4412 4526 4694 -28 13 -24 C ATOM 1341 C LYS A 173 57.550 43.188 26.371 1.00 37.10 C ANISOU 1341 C LYS B 173 4522 4739 4834 -37 -13 -2 C ATOM 1342 O LYS A 173 56.481 43.654 26.732 1.00 39.28 O ANISOU 1342 O LYS B 173 4780 4952 5190 -7 -43 -167 O ATOM 1343 CB LYS A 173 59.295 44.829 26.875 1.00 36.59 C ANISOU 1343 CB LYS B 173 4505 4564 4831 24 -38 48 C ATOM 1344 CG LYS A 173 60.679 45.223 27.388 1.00 37.50 C ANISOU 1344 CG LYS B 173 4751 4737 4758 -69 1 42 C ATOM 1345 CD LYS A 173 60.698 45.502 28.849 1.00 35.90 C ANISOU 1345 CD LYS B 173 4506 4511 4624 47 -84 155 C ATOM 1346 CE LYS A 173 61.859 46.415 29.205 1.00 31.94 C ANISOU 1346 CE LYS B 173 3812 4078 4243 -8 106 -120 C ATOM 1347 NZ LYS A 173 61.795 46.658 30.653 1.00 29.63 N ANISOU 1347 NZ LYS B 173 3659 3722 3874 152 43 118 N ATOM 1348 N VAL A 174 57.673 42.500 25.246 1.00 37.06 N ANISOU 1348 N VAL B 174 4607 4781 4693 -57 44 4 N ATOM 1349 CA VAL A 174 56.514 42.247 24.393 1.00 36.63 C ANISOU 1349 CA VAL B 174 4556 4683 4678 -7 29 47 C ATOM 1350 C VAL A 174 56.461 40.802 23.899 1.00 35.94 C ANISOU 1350 C VAL B 174 4549 4618 4488 28 10 103 C ATOM 1351 O VAL A 174 55.973 40.523 22.804 1.00 35.93 O ANISOU 1351 O VAL B 174 4691 4573 4384 106 63 161 O ATOM 1352 CB VAL A 174 56.488 43.257 23.219 1.00 37.82 C ANISOU 1352 CB VAL B 174 4773 4816 4778 10 70 -22 C ATOM 1353 CG1 VAL A 174 56.344 44.657 23.771 1.00 39.03 C ANISOU 1353 CG1 VAL B 174 4748 5039 5041 46 110 -103 C ATOM 1354 CG2 VAL A 174 57.761 43.166 22.371 1.00 39.54 C ANISOU 1354 CG2 VAL B 174 5126 4941 4955 -16 -40 -3 C ATOM 1355 N CYS A 175 56.922 39.875 24.727 1.00 34.45 N ANISOU 1355 N CYS B 175 4359 4453 4277 28 11 142 N ATOM 1356 CA CYS A 175 56.917 38.468 24.363 1.00 33.48 C ANISOU 1356 CA CYS B 175 4288 4266 4165 -13 -2 53 C ATOM 1357 C CYS A 175 55.530 37.846 24.539 1.00 31.82 C ANISOU 1357 C CYS B 175 4067 4106 3917 -63 17 108 C ATOM 1358 O CYS A 175 54.639 38.432 25.153 1.00 29.60 O ANISOU 1358 O CYS B 175 3807 3759 3678 -6 -26 315 O ATOM 1359 CB CYS A 175 57.965 37.707 25.184 1.00 33.92 C ANISOU 1359 CB CYS B 175 4305 4265 4316 -79 -48 56 C ATOM 1360 SG CYS A 175 57.535 37.460 26.938 1.00 33.91 S ANISOU 1360 SG CYS B 175 4043 4286 4552 -119 -51 220 S ATOM 1361 N ILE A 176 55.368 36.634 24.021 1.00 32.85 N ANISOU 1361 N ILE B 176 4257 4115 4110 17 -107 -10 N ATOM 1362 CA ILE A 176 54.089 35.924 24.036 1.00 32.33 C ANISOU 1362 CA ILE B 176 4179 4047 4054 -8 -71 -42 C ATOM 1363 C ILE A 176 53.501 35.688 25.417 1.00 30.86 C ANISOU 1363 C ILE B 176 3995 3810 3919 -78 -150 -16 C ATOM 1364 O ILE A 176 52.309 35.954 25.646 1.00 30.49 O ANISOU 1364 O ILE B 176 4001 3538 4045 -64 -260 -137 O ATOM 1365 CB ILE A 176 54.228 34.531 23.334 1.00 33.99 C ANISOU 1365 CB ILE B 176 4303 4270 4342 81 -90 -20 C ATOM 1366 CG1 ILE A 176 54.577 34.728 21.863 1.00 36.80 C ANISOU 1366 CG1 ILE B 176 4727 4718 4536 148 -82 34 C ATOM 1367 CG2 ILE A 176 52.955 33.685 23.481 1.00 34.66 C ANISOU 1367 CG2 ILE B 176 4422 4344 4403 89 -27 -43 C ATOM 1368 CD1 ILE A 176 53.887 35.910 21.217 1.00 38.89 C ANISOU 1368 CD1 ILE B 176 4985 4992 4798 -46 -6 135 C ATOM 1369 N THR A 177 54.319 35.140 26.303 1.00 27.89 N ANISOU 1369 N THR B 177 3566 3452 3578 -148 -182 -36 N ATOM 1370 CA THR A 177 53.895 34.810 27.642 1.00 28.30 C ANISOU 1370 CA THR B 177 3547 3523 3680 -100 -43 42 C ATOM 1371 C THR A 177 53.271 36.016 28.346 1.00 24.70 C ANISOU 1371 C THR B 177 3261 3183 2938 -36 -63 75 C ATOM 1372 O THR A 177 52.159 35.916 28.854 1.00 21.89 O ANISOU 1372 O THR B 177 2905 2903 2510 1 41 168 O ATOM 1373 CB THR A 177 55.065 34.235 28.457 1.00 29.05 C ANISOU 1373 CB THR B 177 3658 3629 3750 -105 -59 53 C ATOM 1374 OG1 THR A 177 55.529 33.072 27.779 1.00 31.51 O ANISOU 1374 OG1 THR B 177 3667 3830 4475 -380 -36 96 O ATOM 1375 CG2 THR A 177 54.619 33.862 29.880 1.00 27.93 C ANISOU 1375 CG2 THR B 177 3613 3402 3596 -94 -37 38 C ATOM 1376 N LYS A 178 53.974 37.153 28.334 1.00 24.25 N ANISOU 1376 N LYS B 178 3317 3045 2849 -21 146 -37 N ATOM 1377 CA LYS A 178 53.483 38.399 28.934 1.00 25.65 C ANISOU 1377 CA LYS B 178 3384 3248 3112 -39 37 -10 C ATOM 1378 C LYS A 178 52.134 38.807 28.346 1.00 25.33 C ANISOU 1378 C LYS B 178 3338 3292 2992 -89 10 -18 C ATOM 1379 O LYS A 178 51.153 39.056 29.073 1.00 26.08 O ANISOU 1379 O LYS B 178 3616 3198 3092 -151 71 159 O ATOM 1380 CB LYS A 178 54.521 39.509 28.709 1.00 26.80 C ANISOU 1380 CB LYS B 178 3506 3353 3322 -134 -32 -37 C ATOM 1381 CG LYS A 178 54.221 40.823 29.334 1.00 27.94 C ANISOU 1381 CG LYS B 178 3603 3538 3472 72 -25 -97 C ATOM 1382 CD LYS A 178 55.137 41.876 28.771 1.00 29.73 C ANISOU 1382 CD LYS B 178 3722 3754 3820 146 54 -73 C ATOM 1383 CE LYS A 178 54.822 43.284 29.290 1.00 34.80 C ANISOU 1383 CE LYS B 178 4029 4623 4567 -71 -138 -28 C ATOM 1384 NZ LYS A 178 53.379 43.662 29.327 1.00 37.09 N ANISOU 1384 NZ LYS B 178 4662 4584 4846 70 133 19 N ATOM 1385 N ILE A 179 52.080 38.864 27.019 1.00 25.05 N ANISOU 1385 N ILE B 179 3244 3269 3004 -154 -49 57 N ATOM 1386 CA ILE A 179 50.894 39.329 26.355 1.00 24.90 C ANISOU 1386 CA ILE B 179 3265 3252 2942 -58 -6 22 C ATOM 1387 C ILE A 179 49.712 38.385 26.538 1.00 24.15 C ANISOU 1387 C ILE B 179 3166 3208 2799 -107 24 -9 C ATOM 1388 O ILE A 179 48.594 38.824 26.790 1.00 23.84 O ANISOU 1388 O ILE B 179 3359 3068 2630 -121 44 -273 O ATOM 1389 CB ILE A 179 51.114 39.514 24.831 1.00 25.71 C ANISOU 1389 CB ILE B 179 3464 3370 2933 -66 -11 5 C ATOM 1390 CG1 ILE A 179 52.311 40.432 24.510 1.00 29.29 C ANISOU 1390 CG1 ILE B 179 3516 3707 3907 -58 48 40 C ATOM 1391 CG2 ILE A 179 49.838 40.039 24.207 1.00 25.92 C ANISOU 1391 CG2 ILE B 179 3293 3357 3196 -26 -23 148 C ATOM 1392 CD1 ILE A 179 52.345 41.749 25.220 1.00 34.05 C ANISOU 1392 CD1 ILE B 179 4238 4404 4294 -53 -161 -75 C ATOM 1393 N LYS A 180 49.937 37.089 26.386 1.00 22.89 N ANISOU 1393 N LYS B 180 2947 2960 2788 -94 -79 2 N ATOM 1394 CA LYS A 180 48.810 36.176 26.349 1.00 23.72 C ANISOU 1394 CA LYS B 180 3079 3041 2892 -79 -32 -68 C ATOM 1395 C LYS A 180 48.314 35.715 27.734 1.00 21.71 C ANISOU 1395 C LYS B 180 2860 2818 2569 -85 -115 -87 C ATOM 1396 O LYS A 180 47.121 35.407 27.876 1.00 20.23 O ANISOU 1396 O LYS B 180 2906 2719 2061 -180 -302 23 O ATOM 1397 CB LYS A 180 49.119 34.978 25.438 1.00 26.47 C ANISOU 1397 CB LYS B 180 3338 3324 3395 92 -200 18 C ATOM 1398 CG LYS A 180 49.217 35.338 23.948 1.00 29.09 C ANISOU 1398 CG LYS B 180 3857 3949 3247 33 96 -150 C ATOM 1399 CD LYS A 180 48.066 36.280 23.512 1.00 36.28 C ANISOU 1399 CD LYS B 180 4875 4579 4330 -152 39 -9 C ATOM 1400 CE LYS A 180 47.891 36.402 21.960 1.00 37.44 C ANISOU 1400 CE LYS B 180 5060 4888 4274 0 153 220 C ATOM 1401 NZ LYS A 180 48.999 37.163 21.287 1.00 40.84 N ANISOU 1401 NZ LYS B 180 5278 5459 4781 232 8 -62 N ATOM 1402 N THR A 181 49.198 35.668 28.736 1.00 19.88 N ANISOU 1402 N THR B 181 2614 2478 2460 -39 -180 -184 N ATOM 1403 CA THR A 181 48.816 35.130 30.057 1.00 20.78 C ANISOU 1403 CA THR B 181 2647 2552 2694 -15 6 16 C ATOM 1404 C THR A 181 48.758 36.147 31.201 1.00 18.36 C ANISOU 1404 C THR B 181 2316 2185 2475 -59 33 30 C ATOM 1405 O THR A 181 48.125 35.880 32.199 1.00 19.31 O ANISOU 1405 O THR B 181 2335 2228 2773 -125 -87 142 O ATOM 1406 CB THR A 181 49.766 34.005 30.537 1.00 20.65 C ANISOU 1406 CB THR B 181 2474 2397 2973 -32 -77 -87 C ATOM 1407 OG1 THR A 181 51.007 34.567 30.989 1.00 20.61 O ANISOU 1407 OG1 THR B 181 2631 2462 2736 -211 -56 182 O ATOM 1408 CG2 THR A 181 49.986 32.978 29.446 1.00 22.49 C ANISOU 1408 CG2 THR B 181 3136 2690 2717 55 69 -71 C ATOM 1409 N GLY A 182 49.461 37.274 31.072 1.00 19.13 N ANISOU 1409 N GLY B 182 2305 2420 2542 -57 -9 111 N ATOM 1410 CA GLY A 182 49.581 38.262 32.135 1.00 18.58 C ANISOU 1410 CA GLY B 182 2404 2344 2308 -97 60 -53 C ATOM 1411 C GLY A 182 50.584 37.923 33.226 1.00 18.57 C ANISOU 1411 C GLY B 182 2267 2347 2440 -55 15 21 C ATOM 1412 O GLY A 182 50.693 38.668 34.207 1.00 17.58 O ANISOU 1412 O GLY B 182 1978 2673 2029 -96 359 -23 O ATOM 1413 N PHE A 183 51.307 36.803 33.070 1.00 17.77 N ANISOU 1413 N PHE B 183 2124 2257 2368 -146 -97 55 N ATOM 1414 CA PHE A 183 52.247 36.309 34.088 1.00 18.39 C ANISOU 1414 CA PHE B 183 2269 2328 2388 -71 -37 -5 C ATOM 1415 C PHE A 183 53.686 36.436 33.595 1.00 19.77 C ANISOU 1415 C PHE B 183 2570 2386 2555 -58 -39 3 C ATOM 1416 O PHE A 183 53.977 36.279 32.402 1.00 20.08 O ANISOU 1416 O PHE B 183 3108 2157 2363 -20 -118 313 O ATOM 1417 CB PHE A 183 52.015 34.802 34.373 1.00 17.57 C ANISOU 1417 CB PHE B 183 2356 2182 2138 -75 134 6 C ATOM 1418 CG PHE A 183 50.894 34.529 35.296 1.00 16.64 C ANISOU 1418 CG PHE B 183 1794 2245 2281 -101 7 40 C ATOM 1419 CD1 PHE A 183 51.131 34.363 36.662 1.00 17.68 C ANISOU 1419 CD1 PHE B 183 2044 2262 2410 -120 -17 52 C ATOM 1420 CD2 PHE A 183 49.592 34.489 34.822 1.00 18.67 C ANISOU 1420 CD2 PHE B 183 2601 2072 2418 -83 -57 -103 C ATOM 1421 CE1 PHE A 183 50.095 34.125 37.536 1.00 16.77 C ANISOU 1421 CE1 PHE B 183 1826 2199 2347 -118 339 -68 C ATOM 1422 CE2 PHE A 183 48.536 34.243 35.689 1.00 18.75 C ANISOU 1422 CE2 PHE B 183 2655 2023 2444 12 396 -136 C ATOM 1423 CZ PHE A 183 48.781 34.087 37.044 1.00 17.19 C ANISOU 1423 CZ PHE B 183 2530 1898 2101 322 104 30 C ATOM 1424 N GLY A 184 54.577 36.616 34.545 1.00 20.39 N ANISOU 1424 N GLY B 184 2479 2369 2898 135 -223 -33 N ATOM 1425 CA GLY A 184 55.993 36.368 34.361 1.00 21.62 C ANISOU 1425 CA GLY B 184 2596 2531 3085 56 -148 6 C ATOM 1426 C GLY A 184 56.859 37.561 34.755 1.00 20.01 C ANISOU 1426 C GLY B 184 2429 2347 2825 116 -239 95 C ATOM 1427 O GLY A 184 56.388 38.497 35.414 1.00 20.19 O ANISOU 1427 O GLY B 184 2762 2069 2836 118 -519 181 O ATOM 1428 N THR A 185 58.115 37.509 34.334 1.00 18.03 N ANISOU 1428 N THR B 185 2267 2310 2271 -62 -129 92 N ATOM 1429 CA THR A 185 59.117 38.529 34.667 1.00 19.84 C ANISOU 1429 CA THR B 185 2526 2324 2689 3 -24 56 C ATOM 1430 C THR A 185 59.290 39.613 33.610 1.00 20.03 C ANISOU 1430 C THR B 185 2601 2333 2674 -125 -22 112 C ATOM 1431 O THR A 185 60.158 40.480 33.722 1.00 19.63 O ANISOU 1431 O THR B 185 2544 2264 2649 -118 196 25 O ATOM 1432 CB THR A 185 60.485 37.873 34.933 1.00 20.44 C ANISOU 1432 CB THR B 185 2430 2392 2944 -7 -42 12 C ATOM 1433 OG1 THR A 185 60.905 37.168 33.761 1.00 17.95 O ANISOU 1433 OG1 THR B 185 2205 2019 2594 113 -80 566 O ATOM 1434 CG2 THR A 185 60.423 36.981 36.189 1.00 22.61 C ANISOU 1434 CG2 THR B 185 2572 2719 3298 57 -278 -37 C ATOM 1435 N GLY A 186 58.414 39.606 32.612 1.00 19.74 N ANISOU 1435 N GLY B 186 2655 2610 2232 -117 -107 37 N ATOM 1436 CA GLY A 186 58.511 40.568 31.504 1.00 20.80 C ANISOU 1436 CA GLY B 186 2678 2528 2694 -44 47 60 C ATOM 1437 C GLY A 186 58.323 41.979 32.008 1.00 21.05 C ANISOU 1437 C GLY B 186 2727 2614 2657 -29 44 138 C ATOM 1438 O GLY A 186 57.361 42.266 32.722 1.00 24.25 O ANISOU 1438 O GLY B 186 2932 2806 3472 -292 -112 202 O ATOM 1439 N GLY A 187 59.275 42.838 31.681 1.00 20.20 N ANISOU 1439 N GLY B 187 2629 2528 2517 -49 77 122 N ATOM 1440 CA GLY A 187 59.265 44.202 32.157 1.00 20.54 C ANISOU 1440 CA GLY B 187 2593 2474 2735 -68 162 49 C ATOM 1441 C GLY A 187 59.849 44.488 33.517 1.00 20.77 C ANISOU 1441 C GLY B 187 2597 2554 2740 -66 65 -74 C ATOM 1442 O GLY A 187 59.911 45.669 33.880 1.00 21.13 O ANISOU 1442 O GLY B 187 2546 2408 3074 -186 79 -94 O ATOM 1443 N TRP A 188 60.282 43.434 34.256 1.00 19.86 N ANISOU 1443 N TRP B 188 2482 2350 2711 25 178 -135 N ATOM 1444 CA TRP A 188 61.041 43.578 35.508 1.00 18.67 C ANISOU 1444 CA TRP B 188 2293 2198 2602 -37 140 -57 C ATOM 1445 C TRP A 188 62.092 42.456 35.732 1.00 17.74 C ANISOU 1445 C TRP B 188 2262 2061 2414 12 51 13 C ATOM 1446 O TRP A 188 62.342 42.055 36.880 1.00 14.40 O ANISOU 1446 O TRP B 188 2030 1526 1914 -75 278 -209 O ATOM 1447 CB TRP A 188 60.114 43.672 36.739 1.00 19.52 C ANISOU 1447 CB TRP B 188 2423 2423 2570 -116 27 -25 C ATOM 1448 CG TRP A 188 59.258 42.449 36.988 1.00 18.38 C ANISOU 1448 CG TRP B 188 2559 1982 2442 -103 -97 -173 C ATOM 1449 CD1 TRP A 188 58.290 41.950 36.169 1.00 19.43 C ANISOU 1449 CD1 TRP B 188 2476 2480 2422 -49 -164 -189 C ATOM 1450 CD2 TRP A 188 59.285 41.595 38.149 1.00 20.17 C ANISOU 1450 CD2 TRP B 188 2725 2139 2797 -148 80 38 C ATOM 1451 NE1 TRP A 188 57.717 40.849 36.750 1.00 20.46 N ANISOU 1451 NE1 TRP B 188 2665 2484 2623 168 -252 -12 N ATOM 1452 CE2 TRP A 188 58.325 40.588 37.947 1.00 20.42 C ANISOU 1452 CE2 TRP B 188 2739 2420 2599 -91 121 -185 C ATOM 1453 CE3 TRP A 188 60.051 41.577 39.331 1.00 20.26 C ANISOU 1453 CE3 TRP B 188 2717 2611 2371 -12 97 -7 C ATOM 1454 CZ2 TRP A 188 58.103 39.547 38.883 1.00 19.85 C ANISOU 1454 CZ2 TRP B 188 2686 2303 2553 -58 143 84 C ATOM 1455 CZ3 TRP A 188 59.823 40.563 40.263 1.00 20.28 C ANISOU 1455 CZ3 TRP B 188 2822 2321 2559 120 33 7 C ATOM 1456 CH2 TRP A 188 58.859 39.566 40.037 1.00 18.95 C ANISOU 1456 CH2 TRP B 188 2434 2342 2423 -68 -108 -217 C ATOM 1457 N GLN A 189 62.687 41.977 34.640 1.00 18.21 N ANISOU 1457 N GLN B 189 2261 2081 2574 99 165 -16 N ATOM 1458 CA GLN A 189 63.592 40.833 34.678 1.00 17.47 C ANISOU 1458 CA GLN B 189 2138 2095 2404 24 58 -24 C ATOM 1459 C GLN A 189 64.762 41.059 35.611 1.00 17.47 C ANISOU 1459 C GLN B 189 2090 2048 2500 68 37 -31 C ATOM 1460 O GLN A 189 65.105 40.155 36.410 1.00 17.00 O ANISOU 1460 O GLN B 189 1942 1961 2554 -31 13 -69 O ATOM 1461 CB GLN A 189 64.043 40.437 33.260 1.00 18.98 C ANISOU 1461 CB GLN B 189 2391 2245 2573 74 -40 22 C ATOM 1462 CG GLN A 189 65.174 39.383 33.206 1.00 20.19 C ANISOU 1462 CG GLN B 189 2515 2473 2682 -41 38 96 C ATOM 1463 CD GLN A 189 64.787 38.004 33.770 1.00 22.29 C ANISOU 1463 CD GLN B 189 2780 2771 2917 60 49 -81 C ATOM 1464 OE1 GLN A 189 63.612 37.697 33.932 1.00 23.24 O ANISOU 1464 OE1 GLN B 189 3081 2690 3058 -91 -323 -430 O ATOM 1465 NE2 GLN A 189 65.791 37.155 34.023 1.00 20.24 N ANISOU 1465 NE2 GLN B 189 2301 2693 2695 168 315 -37 N ATOM 1466 N LEU A 190 65.358 42.251 35.598 1.00 17.72 N ANISOU 1466 N LEU B 190 1931 2184 2616 -108 85 30 N ATOM 1467 CA LEU A 190 66.502 42.482 36.519 1.00 17.42 C ANISOU 1467 CA LEU B 190 2074 2093 2451 -60 27 2 C ATOM 1468 C LEU A 190 66.162 42.404 38.015 1.00 16.72 C ANISOU 1468 C LEU B 190 1959 1917 2475 -7 86 -20 C ATOM 1469 O LEU A 190 66.904 41.834 38.808 1.00 16.34 O ANISOU 1469 O LEU B 190 1792 1781 2636 183 22 -24 O ATOM 1470 CB LEU A 190 67.232 43.787 36.208 1.00 18.17 C ANISOU 1470 CB LEU B 190 2200 2090 2612 -41 -129 -111 C ATOM 1471 CG LEU A 190 68.614 43.928 36.840 1.00 18.06 C ANISOU 1471 CG LEU B 190 2106 2365 2389 -72 -4 118 C ATOM 1472 CD1 LEU A 190 69.552 42.730 36.594 1.00 18.36 C ANISOU 1472 CD1 LEU B 190 2263 2060 2651 80 49 -133 C ATOM 1473 CD2 LEU A 190 69.267 45.192 36.354 1.00 18.85 C ANISOU 1473 CD2 LEU B 190 2346 2097 2717 3 87 84 C ATOM 1474 N ALA A 191 65.045 43.015 38.404 1.00 16.76 N ANISOU 1474 N ALA B 191 2234 1911 2222 -158 -10 -54 N ATOM 1475 CA ALA A 191 64.603 42.971 39.790 1.00 17.50 C ANISOU 1475 CA ALA B 191 2270 2061 2318 -96 10 35 C ATOM 1476 C ALA A 191 64.187 41.553 40.170 1.00 16.94 C ANISOU 1476 C ALA B 191 2252 2049 2134 -185 84 10 C ATOM 1477 O ALA A 191 64.424 41.130 41.298 1.00 17.78 O ANISOU 1477 O ALA B 191 2614 2185 1954 -350 135 52 O ATOM 1478 CB ALA A 191 63.482 43.973 40.022 1.00 18.32 C ANISOU 1478 CB ALA B 191 2340 2120 2500 -115 -90 65 C ATOM 1479 N ALA A 192 63.577 40.822 39.233 1.00 16.83 N ANISOU 1479 N ALA B 192 2076 2161 2156 -165 41 -119 N ATOM 1480 CA ALA A 192 63.226 39.408 39.429 1.00 16.45 C ANISOU 1480 CA ALA B 192 2127 2166 1957 -50 38 36 C ATOM 1481 C ALA A 192 64.487 38.580 39.696 1.00 16.31 C ANISOU 1481 C ALA B 192 2032 2158 2008 54 81 71 C ATOM 1482 O ALA A 192 64.501 37.729 40.573 1.00 16.76 O ANISOU 1482 O ALA B 192 2110 2158 2098 -25 423 575 O ATOM 1483 CB ALA A 192 62.461 38.849 38.177 1.00 16.58 C ANISOU 1483 CB ALA B 192 2023 2075 2201 -1 15 86 C ATOM 1484 N LEU A 193 65.543 38.847 38.944 1.00 15.58 N ANISOU 1484 N LEU B 193 2072 2018 1827 -18 33 -73 N ATOM 1485 CA LEU A 193 66.840 38.170 39.110 1.00 16.98 C ANISOU 1485 CA LEU B 193 2173 2196 2081 0 37 82 C ATOM 1486 C LEU A 193 67.431 38.436 40.498 1.00 16.46 C ANISOU 1486 C LEU B 193 2262 2126 1865 -8 -60 85 C ATOM 1487 O LEU A 193 67.894 37.529 41.164 1.00 17.38 O ANISOU 1487 O LEU B 193 2209 2474 1921 46 -73 100 O ATOM 1488 CB LEU A 193 67.846 38.660 38.073 1.00 14.32 C ANISOU 1488 CB LEU B 193 1944 1915 1582 -113 -284 -53 C ATOM 1489 CG LEU A 193 69.287 38.174 38.228 1.00 16.03 C ANISOU 1489 CG LEU B 193 2128 2024 1938 0 -56 -15 C ATOM 1490 CD1 LEU A 193 69.377 36.638 38.170 1.00 19.18 C ANISOU 1490 CD1 LEU B 193 2423 2341 2522 -69 119 -200 C ATOM 1491 CD2 LEU A 193 70.210 38.846 37.230 1.00 16.27 C ANISOU 1491 CD2 LEU B 193 2047 2152 1981 -31 -104 31 C ATOM 1492 N ARG A 194 67.464 39.697 40.875 1.00 18.98 N ANISOU 1492 N ARG B 194 2486 2295 2430 -47 -27 102 N ATOM 1493 CA ARG A 194 67.908 40.084 42.218 1.00 20.22 C ANISOU 1493 CA ARG B 194 2635 2586 2462 16 -34 116 C ATOM 1494 C ARG A 194 67.144 39.334 43.335 1.00 20.23 C ANISOU 1494 C ARG B 194 2614 2501 2570 -19 -2 132 C ATOM 1495 O ARG A 194 67.733 38.802 44.289 1.00 19.54 O ANISOU 1495 O ARG B 194 2690 2230 2503 158 -119 409 O ATOM 1496 CB ARG A 194 67.709 41.585 42.410 1.00 20.90 C ANISOU 1496 CB ARG B 194 2803 2527 2609 -118 42 32 C ATOM 1497 CG ARG A 194 68.318 42.074 43.711 1.00 22.20 C ANISOU 1497 CG ARG B 194 3008 2728 2699 24 -131 229 C ATOM 1498 CD ARG A 194 67.659 43.344 44.247 1.00 28.25 C ANISOU 1498 CD ARG B 194 3342 4045 3345 -212 -116 -229 C ATOM 1499 NE ARG A 194 68.506 44.304 44.978 1.00 36.79 N ANISOU 1499 NE ARG B 194 4440 5108 4428 270 -489 135 N ATOM 1500 CZ ARG A 194 69.749 44.149 45.501 1.00 43.70 C ANISOU 1500 CZ ARG B 194 5475 5611 5516 -84 -110 213 C ATOM 1501 NH1 ARG A 194 70.446 43.006 45.480 1.00 47.26 N ANISOU 1501 NH1 ARG B 194 5982 5924 6051 -222 -85 182 N ATOM 1502 NH2 ARG A 194 70.325 45.197 46.102 1.00 41.98 N ANISOU 1502 NH2 ARG B 194 5390 5146 5413 228 118 187 N ATOM 1503 N TRP A 195 65.825 39.302 43.191 1.00 19.76 N ANISOU 1503 N TRP B 195 2583 2431 2492 73 -40 165 N ATOM 1504 CA TRP A 195 64.915 38.723 44.167 1.00 20.34 C ANISOU 1504 CA TRP B 195 2678 2608 2439 28 0 114 C ATOM 1505 C TRP A 195 65.179 37.225 44.359 1.00 20.04 C ANISOU 1505 C TRP B 195 2543 2570 2498 14 -52 9 C ATOM 1506 O TRP A 195 65.321 36.751 45.510 1.00 20.87 O ANISOU 1506 O TRP B 195 2540 2633 2757 -53 -69 147 O ATOM 1507 CB TRP A 195 63.479 39.011 43.709 1.00 19.88 C ANISOU 1507 CB TRP B 195 2512 2595 2445 1 -154 -60 C ATOM 1508 CG TRP A 195 62.374 38.535 44.553 1.00 20.66 C ANISOU 1508 CG TRP B 195 2624 2599 2623 -46 -72 -50 C ATOM 1509 CD1 TRP A 195 62.267 38.629 45.905 1.00 20.27 C ANISOU 1509 CD1 TRP B 195 2637 2635 2429 -32 88 -18 C ATOM 1510 CD2 TRP A 195 61.143 37.965 44.084 1.00 19.98 C ANISOU 1510 CD2 TRP B 195 2307 2673 2608 -74 -56 -28 C ATOM 1511 NE1 TRP A 195 61.039 38.140 46.318 1.00 22.52 N ANISOU 1511 NE1 TRP B 195 3058 2952 2544 25 -141 -71 N ATOM 1512 CE2 TRP A 195 60.341 37.706 45.223 1.00 22.73 C ANISOU 1512 CE2 TRP B 195 2948 2703 2985 6 56 -48 C ATOM 1513 CE3 TRP A 195 60.649 37.632 42.826 1.00 18.85 C ANISOU 1513 CE3 TRP B 195 2193 2590 2380 73 147 -86 C ATOM 1514 CZ2 TRP A 195 59.080 37.134 45.132 1.00 20.49 C ANISOU 1514 CZ2 TRP B 195 2517 2627 2639 -65 2 -60 C ATOM 1515 CZ3 TRP A 195 59.376 37.071 42.735 1.00 20.61 C ANISOU 1515 CZ3 TRP B 195 2725 2660 2444 83 -21 16 C ATOM 1516 CH2 TRP A 195 58.617 36.810 43.885 1.00 21.85 C ANISOU 1516 CH2 TRP B 195 2864 2735 2701 146 -105 22 C ATOM 1517 N CYS A 196 65.272 36.516 43.239 1.00 21.71 N ANISOU 1517 N CYS B 196 2746 2582 2917 91 -17 55 N ATOM 1518 CA CYS A 196 65.610 35.089 43.173 1.00 21.45 C ANISOU 1518 CA CYS B 196 2690 2719 2738 19 99 27 C ATOM 1519 C CYS A 196 67.024 34.803 43.670 1.00 21.55 C ANISOU 1519 C CYS B 196 2670 2741 2774 -13 170 35 C ATOM 1520 O CYS A 196 67.252 33.798 44.364 1.00 21.25 O ANISOU 1520 O CYS B 196 2826 2726 2519 16 397 214 O ATOM 1521 CB CYS A 196 65.467 34.585 41.711 1.00 20.53 C ANISOU 1521 CB CYS B 196 2550 2635 2616 31 215 -39 C ATOM 1522 SG CYS A 196 63.760 34.476 41.138 1.00 21.94 S ANISOU 1522 SG CYS B 196 2422 2849 3065 203 149 3 S ATOM 1523 N ALA A 197 67.971 35.674 43.315 1.00 21.67 N ANISOU 1523 N ALA B 197 2669 2699 2864 -6 221 -4 N ATOM 1524 CA ALA A 197 69.377 35.501 43.689 1.00 23.73 C ANISOU 1524 CA ALA B 197 3000 2895 3121 -39 161 42 C ATOM 1525 C ALA A 197 69.624 35.611 45.177 1.00 25.22 C ANISOU 1525 C ALA B 197 3253 3092 3235 5 160 35 C ATOM 1526 O ALA A 197 70.501 34.920 45.714 1.00 26.31 O ANISOU 1526 O ALA B 197 3420 3303 3271 -87 369 -15 O ATOM 1527 CB ALA A 197 70.250 36.496 42.959 1.00 24.67 C ANISOU 1527 CB ALA B 197 3237 2705 3432 -35 217 89 C ATOM 1528 N LYS A 198 68.887 36.489 45.843 1.00 25.90 N ANISOU 1528 N LYS B 198 3350 3277 3214 -41 125 50 N ATOM 1529 CA LYS A 198 69.025 36.652 47.285 1.00 29.20 C ANISOU 1529 CA LYS B 198 3766 3782 3545 -17 24 0 C ATOM 1530 C LYS A 198 68.657 35.371 48.052 1.00 30.58 C ANISOU 1530 C LYS B 198 3871 4062 3685 -26 15 87 C ATOM 1531 O LYS A 198 69.128 35.150 49.158 1.00 33.21 O ANISOU 1531 O LYS B 198 4271 4544 3802 -171 -130 117 O ATOM 1532 CB LYS A 198 68.176 37.835 47.770 1.00 30.64 C ANISOU 1532 CB LYS B 198 3995 4048 3599 -70 62 7 C ATOM 1533 CG LYS A 198 68.841 39.173 47.570 1.00 32.00 C ANISOU 1533 CG LYS B 198 3996 4129 4032 -110 -52 32 C ATOM 1534 CD LYS A 198 67.917 40.306 48.033 1.00 34.34 C ANISOU 1534 CD LYS B 198 4165 4564 4316 -142 -132 -16 C ATOM 1535 CE LYS A 198 68.604 41.687 47.930 1.00 38.46 C ANISOU 1535 CE LYS B 198 4496 5137 4977 184 -51 -94 C ATOM 1536 NZ LYS A 198 70.010 41.702 48.484 1.00 43.02 N ANISOU 1536 NZ LYS B 198 5467 5402 5476 17 -286 53 N ATOM 1537 N ALA A 199 67.811 34.537 47.465 1.00 29.30 N ANISOU 1537 N ALA B 199 3738 3873 3521 -23 30 67 N ATOM 1538 CA ALA A 199 67.408 33.291 48.078 1.00 28.80 C ANISOU 1538 CA ALA B 199 3694 3668 3577 -41 1 -6 C ATOM 1539 C ALA A 199 68.333 32.111 47.754 1.00 27.92 C ANISOU 1539 C ALA B 199 3596 3449 3561 -57 108 31 C ATOM 1540 O ALA A 199 68.197 31.060 48.356 1.00 27.79 O ANISOU 1540 O ALA B 199 3727 3235 3595 -241 289 155 O ATOM 1541 CB ALA A 199 66.004 32.964 47.631 1.00 29.28 C ANISOU 1541 CB ALA B 199 3838 3553 3735 -37 127 -50 C ATOM 1542 N ALA A 200 69.229 32.253 46.776 1.00 26.77 N ANISOU 1542 N ALA B 200 3369 3339 3462 -49 27 104 N ATOM 1543 CA ALA A 200 69.840 31.082 46.149 1.00 26.76 C ANISOU 1543 CA ALA B 200 3390 3367 3408 -39 19 92 C ATOM 1544 C ALA A 200 71.116 30.650 46.856 1.00 26.69 C ANISOU 1544 C ALA B 200 3330 3346 3462 -26 -20 126 C ATOM 1545 O ALA A 200 71.921 31.497 47.202 1.00 27.54 O ANISOU 1545 O ALA B 200 3445 3311 3707 -21 14 355 O ATOM 1546 CB ALA A 200 70.142 31.368 44.715 1.00 24.89 C ANISOU 1546 CB ALA B 200 3012 3219 3225 -54 5 77 C ATOM 1547 N SER A 201 71.278 29.338 47.065 1.00 26.42 N ANISOU 1547 N SER B 201 3383 3399 3254 -64 -3 23 N ATOM 1548 CA ASER A 201 72.536 28.769 47.534 0.50 26.50 C ANISOU 1548 CA ASER B 201 3394 3403 3269 -58 18 49 C ATOM 1549 C SER A 201 73.389 28.240 46.364 1.00 26.17 C ANISOU 1549 C SER B 201 3396 3368 3178 -103 64 81 C ATOM 1550 O SER A 201 74.599 28.042 46.499 1.00 27.87 O ANISOU 1550 O SER B 201 3867 3645 3074 -145 62 226 O ATOM 1551 CB ASER A 201 72.249 27.670 48.568 0.50 27.45 C ANISOU 1551 CB ASER B 201 3538 3572 3320 -6 48 42 C ATOM 1552 OG ASER A 201 71.637 28.217 49.742 0.50 28.63 O ANISOU 1552 OG ASER B 201 3480 3789 3608 -261 -114 155 O ATOM 1553 N LYS A 202 72.778 28.060 45.199 1.00 25.62 N ANISOU 1553 N LYS B 202 3121 3271 3341 -77 70 10 N ATOM 1554 CA LYS A 202 73.488 27.567 44.036 1.00 24.61 C ANISOU 1554 CA LYS B 202 3121 3135 3094 -107 92 84 C ATOM 1555 C LYS A 202 73.525 28.612 42.896 1.00 23.01 C ANISOU 1555 C LYS B 202 2899 2782 3061 -56 56 96 C ATOM 1556 O LYS A 202 72.750 29.559 42.933 1.00 22.66 O ANISOU 1556 O LYS B 202 2873 2718 3019 -93 283 320 O ATOM 1557 CB LYS A 202 72.817 26.275 43.599 1.00 24.62 C ANISOU 1557 CB LYS B 202 3127 2895 3333 -74 149 67 C ATOM 1558 CG LYS A 202 72.890 25.209 44.685 1.00 27.67 C ANISOU 1558 CG LYS B 202 3098 3775 3640 47 34 3 C ATOM 1559 CD LYS A 202 72.240 23.908 44.295 1.00 27.36 C ANISOU 1559 CD LYS B 202 3420 3623 3352 17 68 -76 C ATOM 1560 CE LYS A 202 72.435 22.831 45.434 1.00 28.54 C ANISOU 1560 CE LYS B 202 3339 3885 3619 -24 244 -220 C ATOM 1561 NZ LYS A 202 71.586 21.630 45.153 1.00 27.31 N ANISOU 1561 NZ LYS B 202 2941 3879 3556 -107 226 9 N ATOM 1562 N PRO A 203 74.444 28.461 41.914 1.00 21.03 N ANISOU 1562 N PRO B 203 2745 2599 2646 -77 80 181 N ATOM 1563 CA PRO A 203 74.511 29.378 40.775 1.00 22.56 C ANISOU 1563 CA PRO B 203 2841 2742 2985 -66 19 77 C ATOM 1564 C PRO A 203 73.172 29.605 40.039 1.00 19.88 C ANISOU 1564 C PRO B 203 2581 2528 2441 44 -21 168 C ATOM 1565 O PRO A 203 72.329 28.696 39.949 1.00 18.19 O ANISOU 1565 O PRO B 203 2184 2374 2353 5 -193 121 O ATOM 1566 CB PRO A 203 75.522 28.720 39.829 1.00 21.75 C ANISOU 1566 CB PRO B 203 2536 2725 3001 -143 29 -5 C ATOM 1567 CG PRO A 203 76.367 27.890 40.704 1.00 21.71 C ANISOU 1567 CG PRO B 203 3058 2657 2531 -143 87 145 C ATOM 1568 CD PRO A 203 75.499 27.424 41.837 1.00 21.94 C ANISOU 1568 CD PRO B 203 2763 2652 2918 -47 34 22 C ATOM 1569 N ILE A 204 73.004 30.829 39.562 1.00 19.24 N ANISOU 1569 N ILE B 204 2415 2420 2475 40 -154 53 N ATOM 1570 CA ILE A 204 71.884 31.204 38.718 1.00 21.26 C ANISOU 1570 CA ILE B 204 2619 2706 2750 -59 -34 48 C ATOM 1571 C ILE A 204 72.318 31.589 37.299 1.00 20.10 C ANISOU 1571 C ILE B 204 2373 2544 2716 -50 12 -18 C ATOM 1572 O ILE A 204 73.308 32.342 37.105 1.00 21.01 O ANISOU 1572 O ILE B 204 2342 2505 3133 -81 60 236 O ATOM 1573 CB ILE A 204 71.061 32.347 39.369 1.00 20.75 C ANISOU 1573 CB ILE B 204 2514 2625 2741 -130 -38 18 C ATOM 1574 CG1 ILE A 204 70.129 31.775 40.444 1.00 21.02 C ANISOU 1574 CG1 ILE B 204 2801 2841 2343 -266 165 249 C ATOM 1575 CG2 ILE A 204 70.169 33.073 38.346 1.00 18.08 C ANISOU 1575 CG2 ILE B 204 2512 2418 1940 104 -95 -151 C ATOM 1576 CD1 ILE A 204 69.582 32.806 41.335 1.00 26.16 C ANISOU 1576 CD1 ILE B 204 3353 3255 3332 -232 -108 -88 C ATOM 1577 N ILE A 205 71.598 31.033 36.318 1.00 18.79 N ANISOU 1577 N ILE B 205 2307 2372 2458 -10 125 35 N ATOM 1578 CA ILE A 205 71.665 31.471 34.917 1.00 18.80 C ANISOU 1578 CA ILE B 205 2343 2390 2408 21 46 12 C ATOM 1579 C ILE A 205 70.521 32.454 34.670 1.00 17.01 C ANISOU 1579 C ILE B 205 2234 2280 1946 69 -34 87 C ATOM 1580 O ILE A 205 69.346 32.090 34.790 1.00 17.97 O ANISOU 1580 O ILE B 205 2146 2335 2346 87 -7 83 O ATOM 1581 CB ILE A 205 71.577 30.294 33.888 1.00 17.77 C ANISOU 1581 CB ILE B 205 2337 2465 1950 51 186 88 C ATOM 1582 CG1 ILE A 205 72.638 29.224 34.176 1.00 22.04 C ANISOU 1582 CG1 ILE B 205 2948 2632 2791 -49 -176 -256 C ATOM 1583 CG2 ILE A 205 71.667 30.827 32.392 1.00 18.92 C ANISOU 1583 CG2 ILE B 205 2441 2434 2314 -188 261 -26 C ATOM 1584 CD1 ILE A 205 72.788 28.206 33.075 1.00 24.15 C ANISOU 1584 CD1 ILE B 205 2775 3126 3274 -153 -37 109 C ATOM 1585 N ALA A 206 70.862 33.706 34.379 1.00 16.54 N ANISOU 1585 N ALA B 206 2258 2264 1760 82 -65 74 N ATOM 1586 CA ALA A 206 69.864 34.758 34.114 1.00 17.93 C ANISOU 1586 CA ALA B 206 2297 2313 2201 29 -27 15 C ATOM 1587 C ALA A 206 69.433 34.658 32.666 1.00 19.24 C ANISOU 1587 C ALA B 206 2521 2427 2360 106 -12 -14 C ATOM 1588 O ALA A 206 70.263 34.746 31.775 1.00 19.89 O ANISOU 1588 O ALA B 206 2776 2233 2547 94 138 -427 O ATOM 1589 CB ALA A 206 70.455 36.102 34.353 1.00 18.77 C ANISOU 1589 CB ALA B 206 2343 2558 2230 74 -69 228 C ATOM 1590 N ASP A 207 68.147 34.457 32.413 1.00 19.63 N ANISOU 1590 N ASP B 207 2573 2329 2554 -34 -78 -36 N ATOM 1591 CA ASP A 207 67.717 34.081 31.042 1.00 18.98 C ANISOU 1591 CA ASP B 207 2477 2435 2299 70 -31 -14 C ATOM 1592 C ASP A 207 66.825 35.148 30.414 1.00 20.69 C ANISOU 1592 C ASP B 207 2765 2650 2443 58 20 2 C ATOM 1593 O ASP A 207 65.623 35.211 30.691 1.00 20.92 O ANISOU 1593 O ASP B 207 2831 2812 2303 -65 -92 12 O ATOM 1594 CB ASP A 207 67.031 32.687 31.069 1.00 19.45 C ANISOU 1594 CB ASP B 207 2470 2492 2427 -130 -44 136 C ATOM 1595 CG ASP A 207 66.628 32.165 29.674 1.00 20.16 C ANISOU 1595 CG ASP B 207 2489 2790 2380 189 -157 -220 C ATOM 1596 OD1 ASP A 207 66.955 32.785 28.628 1.00 21.18 O ANISOU 1596 OD1 ASP B 207 2697 2891 2456 -133 220 256 O ATOM 1597 OD2 ASP A 207 65.940 31.102 29.640 1.00 17.47 O ANISOU 1597 OD2 ASP B 207 2855 2718 1062 -76 -377 -20 O ATOM 1598 N GLY A 208 67.417 35.994 29.563 1.00 22.46 N ANISOU 1598 N GLY B 208 2849 2807 2877 80 80 19 N ATOM 1599 CA GLY A 208 66.632 36.861 28.677 1.00 21.84 C ANISOU 1599 CA GLY B 208 2706 2915 2675 111 100 -79 C ATOM 1600 C GLY A 208 66.497 38.303 29.162 1.00 23.56 C ANISOU 1600 C GLY B 208 2899 3076 2976 6 35 -89 C ATOM 1601 O GLY A 208 66.992 38.660 30.221 1.00 23.32 O ANISOU 1601 O GLY B 208 2644 3189 3026 -69 -153 -139 O ATOM 1602 N GLY A 209 65.848 39.128 28.346 1.00 24.76 N ANISOU 1602 N GLY B 209 3004 3151 3253 -67 80 -16 N ATOM 1603 CA GLY A 209 65.776 40.562 28.593 1.00 24.68 C ANISOU 1603 CA GLY B 209 3029 3212 3135 -37 -49 -12 C ATOM 1604 C GLY A 209 67.072 41.337 28.366 1.00 25.60 C ANISOU 1604 C GLY B 209 3203 3296 3229 -47 -78 36 C ATOM 1605 O GLY A 209 67.131 42.535 28.649 1.00 27.57 O ANISOU 1605 O GLY B 209 3326 3553 3593 -159 -224 68 O ATOM 1606 N ILE A 210 68.101 40.689 27.817 1.00 23.97 N ANISOU 1606 N ILE B 210 3134 3187 2785 -42 -35 95 N ATOM 1607 CA ILE A 210 69.375 41.348 27.589 1.00 26.01 C ANISOU 1607 CA ILE B 210 3351 3400 3130 -3 -45 13 C ATOM 1608 C ILE A 210 69.282 42.108 26.269 1.00 26.85 C ANISOU 1608 C ILE B 210 3454 3512 3233 91 26 9 C ATOM 1609 O ILE A 210 68.997 41.516 25.228 1.00 28.81 O ANISOU 1609 O ILE B 210 3697 3730 3517 158 -198 -220 O ATOM 1610 CB ILE A 210 70.535 40.322 27.520 1.00 26.21 C ANISOU 1610 CB ILE B 210 3393 3347 3217 33 55 20 C ATOM 1611 CG1 ILE A 210 70.547 39.421 28.775 1.00 25.63 C ANISOU 1611 CG1 ILE B 210 3508 3239 2990 -169 -99 226 C ATOM 1612 CG2 ILE A 210 71.846 41.011 27.274 1.00 25.30 C ANISOU 1612 CG2 ILE B 210 3312 3260 3040 90 -216 20 C ATOM 1613 CD1 ILE A 210 70.439 40.147 30.051 1.00 26.31 C ANISOU 1613 CD1 ILE B 210 3627 3358 3012 -73 -203 -91 C ATOM 1614 N ARG A 211 69.490 43.415 26.315 1.00 26.58 N ANISOU 1614 N ARG B 211 3359 3440 3297 110 -31 58 N ATOM 1615 CA ARG A 211 69.451 44.236 25.095 1.00 28.21 C ANISOU 1615 CA ARG B 211 3578 3634 3505 136 -23 45 C ATOM 1616 C ARG A 211 70.790 44.862 24.662 1.00 26.73 C ANISOU 1616 C ARG B 211 3409 3530 3216 96 1 1 C ATOM 1617 O ARG A 211 70.944 45.246 23.513 1.00 25.19 O ANISOU 1617 O ARG B 211 3372 3463 2735 350 -130 -141 O ATOM 1618 CB ARG A 211 68.405 45.317 25.276 1.00 28.96 C ANISOU 1618 CB ARG B 211 3733 3572 3697 50 -28 25 C ATOM 1619 CG ARG A 211 67.040 44.747 25.615 1.00 33.14 C ANISOU 1619 CG ARG B 211 4167 4197 4225 175 47 -125 C ATOM 1620 CD ARG A 211 66.102 45.840 26.088 1.00 37.95 C ANISOU 1620 CD ARG B 211 4953 4499 4964 39 -265 -171 C ATOM 1621 NE ARG A 211 65.760 46.777 25.025 1.00 48.48 N ANISOU 1621 NE ARG B 211 6042 6350 6026 -71 209 128 N ATOM 1622 CZ ARG A 211 64.958 47.828 25.186 1.00 52.32 C ANISOU 1622 CZ ARG B 211 6530 6719 6629 -224 79 -10 C ATOM 1623 NH1 ARG A 211 64.407 48.092 26.373 1.00 54.37 N ANISOU 1623 NH1 ARG B 211 7025 6934 6697 -116 75 -11 N ATOM 1624 NH2 ARG A 211 64.710 48.626 24.154 1.00 52.21 N ANISOU 1624 NH2 ARG B 211 6561 6672 6604 -222 -24 121 N ATOM 1625 N THR A 212 71.740 44.954 25.587 1.00 25.78 N ANISOU 1625 N THR B 212 3311 3346 3137 126 -25 -24 N ATOM 1626 CA THR A 212 73.041 45.605 25.363 1.00 24.99 C ANISOU 1626 CA THR B 212 3191 3235 3067 21 -18 -2 C ATOM 1627 C THR A 212 74.098 44.771 26.068 1.00 23.06 C ANISOU 1627 C THR B 212 2931 3024 2805 45 -64 -36 C ATOM 1628 O THR A 212 73.771 43.985 26.973 1.00 18.89 O ANISOU 1628 O THR B 212 2894 2635 1646 27 -241 -174 O ATOM 1629 CB THR A 212 73.113 47.036 25.985 1.00 24.36 C ANISOU 1629 CB THR B 212 3075 3125 3054 114 44 -17 C ATOM 1630 OG1 THR A 212 72.993 46.943 27.419 1.00 25.87 O ANISOU 1630 OG1 THR B 212 3282 3494 3054 116 -487 -80 O ATOM 1631 CG2 THR A 212 72.025 47.919 25.491 1.00 25.97 C ANISOU 1631 CG2 THR B 212 3065 3368 3433 157 110 68 C ATOM 1632 N ASN A 213 75.356 44.938 25.674 1.00 21.88 N ANISOU 1632 N ASN B 213 2774 2873 2665 98 -129 1 N ATOM 1633 CA ASN A 213 76.445 44.287 26.408 1.00 22.83 C ANISOU 1633 CA ASN B 213 2839 2917 2915 66 -19 -56 C ATOM 1634 C ASN A 213 76.555 44.779 27.858 1.00 22.00 C ANISOU 1634 C ASN B 213 2749 2733 2875 78 74 -14 C ATOM 1635 O ASN A 213 76.959 44.000 28.720 1.00 23.17 O ANISOU 1635 O ASN B 213 2773 3065 2965 1 137 64 O ATOM 1636 CB ASN A 213 77.794 44.409 25.667 1.00 23.87 C ANISOU 1636 CB ASN B 213 2921 3118 3030 33 -77 -169 C ATOM 1637 CG ASN A 213 77.822 43.642 24.348 1.00 23.43 C ANISOU 1637 CG ASN B 213 3347 3004 2549 177 -13 94 C ATOM 1638 OD1 ASN A 213 76.890 42.921 24.020 1.00 26.73 O ANISOU 1638 OD1 ASN B 213 3604 3300 3251 353 29 -235 O ATOM 1639 ND2 ASN A 213 78.928 43.777 23.602 1.00 23.92 N ANISOU 1639 ND2 ASN B 213 3317 2916 2854 -75 -123 -6 N ATOM 1640 N GLY A 214 76.156 46.034 28.143 1.00 19.66 N ANISOU 1640 N GLY B 214 2545 2397 2529 124 49 -53 N ATOM 1641 CA GLY A 214 76.143 46.540 29.509 1.00 20.57 C ANISOU 1641 CA GLY B 214 2547 2484 2783 37 53 -34 C ATOM 1642 C GLY A 214 75.196 45.780 30.413 1.00 19.79 C ANISOU 1642 C GLY B 214 2456 2416 2646 -65 -31 -29 C ATOM 1643 O GLY A 214 75.398 45.725 31.600 1.00 18.54 O ANISOU 1643 O GLY B 214 2242 2154 2648 -57 159 -6 O ATOM 1644 N ASP A 215 74.183 45.139 29.840 1.00 20.26 N ANISOU 1644 N ASP B 215 2606 2265 2825 -90 82 -107 N ATOM 1645 CA ASP A 215 73.251 44.328 30.639 1.00 19.88 C ANISOU 1645 CA ASP B 215 2542 2409 2602 -47 59 -132 C ATOM 1646 C ASP A 215 73.851 43.043 31.189 1.00 19.03 C ANISOU 1646 C ASP B 215 2610 2230 2388 -6 60 32 C ATOM 1647 O ASP A 215 73.355 42.483 32.178 1.00 19.29 O ANISOU 1647 O ASP B 215 2527 2310 2490 9 188 33 O ATOM 1648 CB ASP A 215 72.002 44.003 29.808 1.00 19.48 C ANISOU 1648 CB ASP B 215 2576 2352 2473 49 -24 -42 C ATOM 1649 CG ASP A 215 71.153 45.241 29.492 1.00 19.95 C ANISOU 1649 CG ASP B 215 2470 2574 2533 43 -142 -195 C ATOM 1650 OD1 ASP A 215 71.246 46.246 30.246 1.00 17.30 O ANISOU 1650 OD1 ASP B 215 2243 2059 2270 150 50 -421 O ATOM 1651 OD2 ASP A 215 70.382 45.203 28.486 1.00 24.90 O ANISOU 1651 OD2 ASP B 215 2913 3302 3243 -195 88 377 O ATOM 1652 N VAL A 216 74.925 42.576 30.577 1.00 19.26 N ANISOU 1652 N VAL B 216 2439 2459 2421 -70 13 6 N ATOM 1653 CA VAL A 216 75.710 41.477 31.167 1.00 19.52 C ANISOU 1653 CA VAL B 216 2523 2365 2527 -51 13 -22 C ATOM 1654 C VAL A 216 76.304 41.897 32.526 1.00 18.71 C ANISOU 1654 C VAL B 216 2333 2221 2553 -138 -38 -87 C ATOM 1655 O VAL A 216 76.118 41.197 33.526 1.00 16.40 O ANISOU 1655 O VAL B 216 2257 1673 2299 -47 52 -214 O ATOM 1656 CB VAL A 216 76.799 40.934 30.168 1.00 20.38 C ANISOU 1656 CB VAL B 216 2515 2543 2685 -58 -56 5 C ATOM 1657 CG1 VAL A 216 77.572 39.802 30.764 1.00 19.57 C ANISOU 1657 CG1 VAL B 216 2611 2411 2414 -37 299 54 C ATOM 1658 CG2 VAL A 216 76.145 40.464 28.897 1.00 20.99 C ANISOU 1658 CG2 VAL B 216 3147 2750 2076 -186 -136 -104 C ATOM 1659 N ALA A 217 77.033 43.014 32.588 1.00 18.42 N ANISOU 1659 N ALA B 217 2197 2288 2512 -123 55 -34 N ATOM 1660 CA ALA A 217 77.529 43.521 33.903 1.00 17.98 C ANISOU 1660 CA ALA B 217 2159 2183 2487 -102 81 73 C ATOM 1661 C ALA A 217 76.429 43.731 34.964 1.00 16.09 C ANISOU 1661 C ALA B 217 2037 2115 1961 100 229 237 C ATOM 1662 O ALA A 217 76.582 43.375 36.176 1.00 14.60 O ANISOU 1662 O ALA B 217 2185 1790 1572 100 230 -48 O ATOM 1663 CB ALA A 217 78.324 44.827 33.660 1.00 19.60 C ANISOU 1663 CB ALA B 217 2266 2348 2832 -37 76 -9 C ATOM 1664 N LYS A 218 75.307 44.309 34.519 1.00 17.22 N ANISOU 1664 N LYS B 218 2007 2127 2408 -46 131 31 N ATOM 1665 CA LYS A 218 74.143 44.512 35.357 1.00 16.24 C ANISOU 1665 CA LYS B 218 2121 2033 2015 -49 98 31 C ATOM 1666 C LYS A 218 73.620 43.184 35.893 1.00 17.48 C ANISOU 1666 C LYS B 218 2125 2131 2384 -19 -22 73 C ATOM 1667 O LYS A 218 73.326 43.115 37.073 1.00 15.71 O ANISOU 1667 O LYS B 218 2096 1789 2083 -129 108 87 O ATOM 1668 CB LYS A 218 73.011 45.296 34.670 1.00 14.96 C ANISOU 1668 CB LYS B 218 2008 1759 1915 -71 36 -107 C ATOM 1669 CG LYS A 218 73.401 46.686 34.194 1.00 16.81 C ANISOU 1669 CG LYS B 218 2136 1746 2505 41 -30 -39 C ATOM 1670 CD LYS A 218 72.286 47.411 33.484 1.00 15.69 C ANISOU 1670 CD LYS B 218 2055 1930 1976 -98 -105 54 C ATOM 1671 CE LYS A 218 72.765 48.701 32.863 1.00 19.15 C ANISOU 1671 CE LYS B 218 2419 2496 2358 -204 150 143 C ATOM 1672 NZ LYS A 218 71.759 49.407 31.990 1.00 22.02 N ANISOU 1672 NZ LYS B 218 2927 2416 3021 -294 166 299 N ATOM 1673 N SER A 219 73.518 42.145 35.045 1.00 18.33 N ANISOU 1673 N SER B 219 2077 2442 2443 -22 26 12 N ATOM 1674 CA SER A 219 73.092 40.802 35.526 1.00 17.46 C ANISOU 1674 CA SER B 219 2207 2121 2303 28 69 -35 C ATOM 1675 C SER A 219 74.067 40.233 36.598 1.00 16.85 C ANISOU 1675 C SER B 219 2177 2081 2143 -28 163 -89 C ATOM 1676 O SER A 219 73.634 39.682 37.609 1.00 17.17 O ANISOU 1676 O SER B 219 2294 2004 2226 72 168 -77 O ATOM 1677 CB SER A 219 72.959 39.816 34.358 1.00 18.11 C ANISOU 1677 CB SER B 219 2042 2350 2488 1 -25 97 C ATOM 1678 OG SER A 219 72.180 40.322 33.274 1.00 18.54 O ANISOU 1678 OG SER B 219 1877 2540 2624 172 -180 329 O ATOM 1679 N ILE A 220 75.372 40.428 36.389 1.00 16.68 N ANISOU 1679 N ILE B 220 2070 2107 2160 76 82 50 N ATOM 1680 CA ILE A 220 76.400 40.020 37.344 1.00 18.25 C ANISOU 1680 CA ILE B 220 2346 2152 2435 45 122 58 C ATOM 1681 C ILE A 220 76.225 40.769 38.671 1.00 17.87 C ANISOU 1681 C ILE B 220 2356 2035 2396 -24 91 67 C ATOM 1682 O ILE A 220 76.191 40.135 39.737 1.00 17.63 O ANISOU 1682 O ILE B 220 2357 1681 2659 -26 283 249 O ATOM 1683 CB ILE A 220 77.858 40.205 36.796 1.00 19.14 C ANISOU 1683 CB ILE B 220 2526 2363 2383 -176 76 65 C ATOM 1684 CG1 ILE A 220 78.107 39.316 35.548 1.00 23.12 C ANISOU 1684 CG1 ILE B 220 2682 3000 3099 -71 -112 102 C ATOM 1685 CG2 ILE A 220 78.884 39.881 37.897 1.00 18.47 C ANISOU 1685 CG2 ILE B 220 2292 2235 2489 -14 -214 195 C ATOM 1686 CD1 ILE A 220 77.967 37.817 35.814 1.00 24.73 C ANISOU 1686 CD1 ILE B 220 3028 2881 3487 7 36 -168 C ATOM 1687 N ARG A 221 76.043 42.096 38.629 1.00 17.86 N ANISOU 1687 N ARG B 221 2361 2158 2266 154 71 63 N ATOM 1688 CA ARG A 221 75.798 42.876 39.866 1.00 18.28 C ANISOU 1688 CA ARG B 221 2314 2207 2424 -2 75 55 C ATOM 1689 C ARG A 221 74.679 42.290 40.697 1.00 16.86 C ANISOU 1689 C ARG B 221 2072 2333 2001 -48 33 120 C ATOM 1690 O ARG A 221 74.823 42.171 41.924 1.00 17.48 O ANISOU 1690 O ARG B 221 2150 2662 1827 -137 -62 -13 O ATOM 1691 CB ARG A 221 75.475 44.355 39.544 1.00 18.86 C ANISOU 1691 CB ARG B 221 2176 2244 2745 118 -69 84 C ATOM 1692 CG ARG A 221 75.018 45.182 40.730 1.00 18.53 C ANISOU 1692 CG ARG B 221 2372 2387 2279 43 214 6 C ATOM 1693 CD ARG A 221 76.025 45.107 41.884 1.00 21.86 C ANISOU 1693 CD ARG B 221 2532 2551 3221 -88 4 244 C ATOM 1694 NE ARG A 221 75.692 45.930 43.027 1.00 20.04 N ANISOU 1694 NE ARG B 221 2538 2573 2502 1 244 84 N ATOM 1695 CZ ARG A 221 74.873 45.583 44.023 1.00 24.39 C ANISOU 1695 CZ ARG B 221 3160 3247 2861 32 167 -95 C ATOM 1696 NH1 ARG A 221 74.251 44.395 44.052 1.00 22.98 N ANISOU 1696 NH1 ARG B 221 3456 2824 2449 60 -129 41 N ATOM 1697 NH2 ARG A 221 74.678 46.447 45.015 1.00 25.28 N ANISOU 1697 NH2 ARG B 221 2871 3331 3401 -158 189 -64 N ATOM 1698 N PHE A 222 73.577 41.925 40.050 1.00 16.79 N ANISOU 1698 N PHE B 222 1880 2174 2322 -212 13 38 N ATOM 1699 CA PHE A 222 72.386 41.474 40.761 1.00 17.66 C ANISOU 1699 CA PHE B 222 2184 2250 2275 -84 -11 29 C ATOM 1700 C PHE A 222 72.242 39.957 40.693 1.00 19.00 C ANISOU 1700 C PHE B 222 2399 2322 2497 26 6 -12 C ATOM 1701 O PHE A 222 71.158 39.417 40.910 1.00 19.72 O ANISOU 1701 O PHE B 222 2678 2281 2532 130 77 139 O ATOM 1702 CB PHE A 222 71.135 42.147 40.192 1.00 17.47 C ANISOU 1702 CB PHE B 222 2388 2072 2177 68 130 113 C ATOM 1703 CG PHE A 222 71.060 43.621 40.472 1.00 17.95 C ANISOU 1703 CG PHE B 222 2431 2337 2053 -243 43 23 C ATOM 1704 CD1 PHE A 222 70.698 44.084 41.725 1.00 21.59 C ANISOU 1704 CD1 PHE B 222 2629 2956 2616 132 -233 -373 C ATOM 1705 CD2 PHE A 222 71.352 44.543 39.481 1.00 21.48 C ANISOU 1705 CD2 PHE B 222 2537 2683 2939 -245 -38 -76 C ATOM 1706 CE1 PHE A 222 70.628 45.440 41.986 1.00 21.05 C ANISOU 1706 CE1 PHE B 222 2442 2499 3055 -7 54 -256 C ATOM 1707 CE2 PHE A 222 71.284 45.900 39.735 1.00 19.45 C ANISOU 1707 CE2 PHE B 222 2418 2616 2354 209 -74 7 C ATOM 1708 CZ PHE A 222 70.921 46.349 40.989 1.00 17.97 C ANISOU 1708 CZ PHE B 222 2547 2190 2090 4 57 17 C ATOM 1709 N GLY A 223 73.343 39.276 40.391 1.00 17.34 N ANISOU 1709 N GLY B 223 2249 2134 2205 -19 -51 91 N ATOM 1710 CA GLY A 223 73.717 38.073 41.112 1.00 17.95 C ANISOU 1710 CA GLY B 223 2321 2236 2261 -108 20 39 C ATOM 1711 C GLY A 223 73.752 36.849 40.218 1.00 19.15 C ANISOU 1711 C GLY B 223 2328 2445 2500 -39 38 3 C ATOM 1712 O GLY A 223 73.728 35.716 40.700 1.00 20.65 O ANISOU 1712 O GLY B 223 2251 2768 2827 -100 124 -63 O ATOM 1713 N ALA A 224 73.811 37.078 38.911 1.00 19.40 N ANISOU 1713 N ALA B 224 2419 2445 2507 -102 19 41 N ATOM 1714 CA ALA A 224 73.937 35.991 37.947 1.00 18.45 C ANISOU 1714 CA ALA B 224 2262 2290 2455 -32 8 24 C ATOM 1715 C ALA A 224 75.344 35.403 37.962 1.00 19.43 C ANISOU 1715 C ALA B 224 2412 2277 2694 -50 -3 25 C ATOM 1716 O ALA A 224 76.308 36.082 38.313 1.00 19.49 O ANISOU 1716 O ALA B 224 2490 2029 2885 -126 -125 206 O ATOM 1717 CB ALA A 224 73.577 36.476 36.551 1.00 19.14 C ANISOU 1717 CB ALA B 224 2317 2307 2645 -63 -53 198 C ATOM 1718 N THR A 225 75.454 34.135 37.578 1.00 17.51 N ANISOU 1718 N THR B 225 2196 2223 2232 41 73 66 N ATOM 1719 CA THR A 225 76.749 33.532 37.286 1.00 17.46 C ANISOU 1719 CA THR B 225 2191 2384 2055 -36 -52 -29 C ATOM 1720 C THR A 225 76.950 33.357 35.785 1.00 18.08 C ANISOU 1720 C THR B 225 2255 2483 2130 41 -123 -202 C ATOM 1721 O THR A 225 78.013 33.672 35.250 1.00 19.48 O ANISOU 1721 O THR B 225 2439 2572 2388 153 -144 35 O ATOM 1722 CB THR A 225 76.886 32.175 38.001 1.00 17.90 C ANISOU 1722 CB THR B 225 2269 2448 2083 -184 -165 -158 C ATOM 1723 OG1 THR A 225 77.097 32.389 39.402 1.00 16.58 O ANISOU 1723 OG1 THR B 225 2373 2230 1695 -289 19 -69 O ATOM 1724 CG2 THR A 225 78.157 31.466 37.559 1.00 19.50 C ANISOU 1724 CG2 THR B 225 2274 2327 2806 -31 68 12 C ATOM 1725 N MET A 226 75.923 32.851 35.110 1.00 19.85 N ANISOU 1725 N MET B 226 2876 2519 2146 16 92 -79 N ATOM 1726 CA MET A 226 75.880 32.870 33.653 1.00 19.68 C ANISOU 1726 CA MET B 226 2669 2544 2264 36 3 -86 C ATOM 1727 C MET A 226 74.682 33.668 33.147 1.00 18.92 C ANISOU 1727 C MET B 226 2543 2478 2166 58 -60 -7 C ATOM 1728 O MET A 226 73.614 33.656 33.758 1.00 18.50 O ANISOU 1728 O MET B 226 2656 2166 2204 40 117 132 O ATOM 1729 CB MET A 226 75.834 31.445 33.099 1.00 22.76 C ANISOU 1729 CB MET B 226 3006 2901 2740 67 -4 -232 C ATOM 1730 CG MET A 226 76.365 31.312 31.682 1.00 26.60 C ANISOU 1730 CG MET B 226 3504 3633 2970 119 -142 -124 C ATOM 1731 SD MET A 226 78.153 31.530 31.585 1.00 28.22 S ANISOU 1731 SD MET B 226 3210 3623 3889 426 -134 -456 S ATOM 1732 CE MET A 226 78.720 29.973 32.266 1.00 34.92 C ANISOU 1732 CE MET B 226 3920 4759 4586 56 -161 142 C ATOM 1733 N VAL A 227 74.869 34.361 32.029 1.00 17.23 N ANISOU 1733 N VAL B 227 2060 2435 2048 40 -212 88 N ATOM 1734 CA VAL A 227 73.790 35.119 31.407 1.00 19.42 C ANISOU 1734 CA VAL B 227 2472 2642 2264 16 -139 0 C ATOM 1735 C VAL A 227 73.412 34.529 30.053 1.00 18.28 C ANISOU 1735 C VAL B 227 2444 2542 1958 -22 13 9 C ATOM 1736 O VAL A 227 74.214 34.531 29.119 1.00 20.34 O ANISOU 1736 O VAL B 227 2654 2830 2243 -112 -107 -187 O ATOM 1737 CB VAL A 227 74.176 36.598 31.221 1.00 19.77 C ANISOU 1737 CB VAL B 227 2626 2608 2275 83 -126 -70 C ATOM 1738 CG1 VAL A 227 73.010 37.384 30.641 1.00 18.45 C ANISOU 1738 CG1 VAL B 227 2076 2979 1953 -91 -241 -161 C ATOM 1739 CG2 VAL A 227 74.631 37.201 32.541 1.00 18.04 C ANISOU 1739 CG2 VAL B 227 2272 2392 2190 -17 -52 -254 C ATOM 1740 N MET A 228 72.187 34.023 29.954 1.00 18.12 N ANISOU 1740 N MET B 228 2337 2607 1940 -72 -110 67 N ATOM 1741 CA MET A 228 71.701 33.419 28.703 1.00 19.84 C ANISOU 1741 CA MET B 228 2572 2567 2397 12 -175 95 C ATOM 1742 C MET A 228 71.121 34.486 27.768 1.00 20.86 C ANISOU 1742 C MET B 228 2692 2716 2517 -42 -151 113 C ATOM 1743 O MET A 228 70.190 35.219 28.143 1.00 20.20 O ANISOU 1743 O MET B 228 2752 2873 2048 -239 -287 32 O ATOM 1744 CB MET A 228 70.693 32.277 28.944 1.00 18.32 C ANISOU 1744 CB MET B 228 2543 2442 1975 -52 -142 283 C ATOM 1745 CG MET A 228 70.151 31.671 27.580 1.00 16.35 C ANISOU 1745 CG MET B 228 2152 2607 1453 -153 -225 19 C ATOM 1746 SD MET A 228 69.219 30.156 27.777 1.00 20.72 S ANISOU 1746 SD MET B 228 2536 2533 2800 -10 -477 232 S ATOM 1747 CE MET A 228 70.558 29.018 28.083 1.00 21.39 C ANISOU 1747 CE MET B 228 2848 2508 2770 39 -254 6 C ATOM 1748 N ILE A 229 71.649 34.525 26.540 1.00 22.18 N ANISOU 1748 N ILE B 229 2839 2866 2721 46 -164 -71 N ATOM 1749 CA ILE A 229 71.356 35.577 25.551 1.00 24.04 C ANISOU 1749 CA ILE B 229 3066 3045 3023 18 -87 12 C ATOM 1750 C ILE A 229 70.780 35.053 24.236 1.00 25.34 C ANISOU 1750 C ILE B 229 3263 3201 3164 14 -126 -17 C ATOM 1751 O ILE A 229 71.362 34.166 23.617 1.00 25.32 O ANISOU 1751 O ILE B 229 3165 3287 3167 214 -226 -30 O ATOM 1752 CB ILE A 229 72.650 36.346 25.231 1.00 24.81 C ANISOU 1752 CB ILE B 229 3107 3265 3052 49 -108 -59 C ATOM 1753 CG1 ILE A 229 73.204 36.951 26.539 1.00 23.75 C ANISOU 1753 CG1 ILE B 229 3056 3198 2769 189 80 70 C ATOM 1754 CG2 ILE A 229 72.412 37.414 24.187 1.00 24.17 C ANISOU 1754 CG2 ILE B 229 3001 3107 3075 35 -75 77 C ATOM 1755 CD1 ILE A 229 74.459 37.819 26.388 1.00 24.18 C ANISOU 1755 CD1 ILE B 229 3201 2997 2988 51 -223 -64 C ATOM 1756 N GLY A 230 69.652 35.632 23.801 1.00 26.47 N ANISOU 1756 N GLY B 230 3397 3472 3189 16 -119 7 N ATOM 1757 CA GLY A 230 69.014 35.280 22.522 1.00 27.38 C ANISOU 1757 CA GLY B 230 3508 3515 3380 66 -43 106 C ATOM 1758 C GLY A 230 69.344 36.275 21.416 1.00 27.26 C ANISOU 1758 C GLY B 230 3588 3566 3202 81 -42 57 C ATOM 1759 O GLY A 230 70.281 36.060 20.651 1.00 28.96 O ANISOU 1759 O GLY B 230 3767 3690 3546 145 -124 108 O ATOM 1760 N SER A 231 68.607 37.384 21.383 1.00 28.64 N ANISOU 1760 N SER B 231 3774 3725 3381 78 -51 50 N ATOM 1761 CA SER A 231 68.694 38.406 20.312 1.00 30.56 C ANISOU 1761 CA SER B 231 3808 4007 3795 42 16 11 C ATOM 1762 C SER A 231 70.103 38.868 19.949 1.00 31.72 C ANISOU 1762 C SER B 231 4016 4109 3925 51 4 -37 C ATOM 1763 O SER A 231 70.408 39.059 18.774 1.00 32.95 O ANISOU 1763 O SER B 231 4134 4388 3997 96 105 -33 O ATOM 1764 CB SER A 231 67.868 39.650 20.678 1.00 31.77 C ANISOU 1764 CB SER B 231 4020 4093 3956 56 -19 -56 C ATOM 1765 OG SER A 231 68.463 40.349 21.782 1.00 38.47 O ANISOU 1765 OG SER B 231 4780 5356 4481 90 29 129 O ATOM 1766 N LEU A 232 70.951 39.095 20.942 1.00 31.93 N ANISOU 1766 N LEU B 232 3992 4129 4009 18 88 12 N ATOM 1767 CA LEU A 232 72.275 39.620 20.643 1.00 32.15 C ANISOU 1767 CA LEU B 232 4030 4121 4064 3 -13 -51 C ATOM 1768 C LEU A 232 73.096 38.605 19.849 1.00 32.02 C ANISOU 1768 C LEU B 232 3969 4086 4109 -14 -16 -102 C ATOM 1769 O LEU A 232 74.016 38.999 19.132 1.00 28.10 O ANISOU 1769 O LEU B 232 3613 3931 3131 -40 -56 -257 O ATOM 1770 CB LEU A 232 73.030 40.078 21.892 1.00 32.74 C ANISOU 1770 CB LEU B 232 3999 4359 4079 -7 32 0 C ATOM 1771 CG LEU A 232 72.643 41.433 22.523 1.00 33.50 C ANISOU 1771 CG LEU B 232 4196 4411 4120 -45 44 -66 C ATOM 1772 CD1 LEU A 232 73.320 41.541 23.877 1.00 31.68 C ANISOU 1772 CD1 LEU B 232 3727 4187 4120 196 -84 55 C ATOM 1773 CD2 LEU A 232 73.047 42.607 21.639 1.00 34.70 C ANISOU 1773 CD2 LEU B 232 4110 4566 4507 -98 -5 -84 C ATOM 1774 N PHE A 233 72.766 37.317 19.986 1.00 32.73 N ANISOU 1774 N PHE B 233 4002 4067 4365 -17 -46 -22 N ATOM 1775 CA PHE A 233 73.457 36.256 19.232 1.00 33.91 C ANISOU 1775 CA PHE B 233 4180 4375 4326 13 -68 -42 C ATOM 1776 C PHE A 233 72.729 35.861 17.962 1.00 34.13 C ANISOU 1776 C PHE B 233 4225 4446 4295 19 -37 -29 C ATOM 1777 O PHE A 233 73.249 35.066 17.176 1.00 33.05 O ANISOU 1777 O PHE B 233 4135 4384 4037 67 9 -60 O ATOM 1778 CB PHE A 233 73.630 35.003 20.099 1.00 33.97 C ANISOU 1778 CB PHE B 233 4156 4366 4383 -14 -54 -32 C ATOM 1779 CG PHE A 233 74.727 35.099 21.128 1.00 32.16 C ANISOU 1779 CG PHE B 233 3961 4069 4189 -3 -37 -26 C ATOM 1780 CD1 PHE A 233 76.026 35.375 20.753 1.00 34.58 C ANISOU 1780 CD1 PHE B 233 4430 4315 4391 107 -47 57 C ATOM 1781 CD2 PHE A 233 74.471 34.821 22.461 1.00 32.99 C ANISOU 1781 CD2 PHE B 233 4181 4142 4208 26 -115 -2 C ATOM 1782 CE1 PHE A 233 77.032 35.428 21.703 1.00 35.67 C ANISOU 1782 CE1 PHE B 233 4727 4350 4473 2 -17 55 C ATOM 1783 CE2 PHE A 233 75.465 34.874 23.411 1.00 32.47 C ANISOU 1783 CE2 PHE B 233 3985 4049 4302 31 121 -44 C ATOM 1784 CZ PHE A 233 76.752 35.170 23.042 1.00 33.17 C ANISOU 1784 CZ PHE B 233 4082 4106 4412 12 145 -141 C ATOM 1785 N ALA A 234 71.526 36.379 17.764 1.00 35.49 N ANISOU 1785 N ALA B 234 4376 4598 4508 -6 -67 -99 N ATOM 1786 CA ALA A 234 70.754 36.070 16.558 1.00 37.82 C ANISOU 1786 CA ALA B 234 4746 4876 4747 15 -52 14 C ATOM 1787 C ALA A 234 71.273 36.863 15.364 1.00 40.69 C ANISOU 1787 C ALA B 234 5100 5326 5032 74 -25 -92 C ATOM 1788 O ALA A 234 71.742 38.004 15.514 1.00 42.12 O ANISOU 1788 O ALA B 234 5263 5513 5225 136 -157 -145 O ATOM 1789 CB ALA A 234 69.287 36.349 16.766 1.00 37.83 C ANISOU 1789 CB ALA B 234 4754 4931 4686 -6 -29 -21 C ATOM 1790 N GLY A 235 71.207 36.253 14.179 1.00 41.81 N ANISOU 1790 N GLY B 235 5280 5493 5112 103 -48 -27 N ATOM 1791 CA GLY A 235 71.524 36.970 12.949 1.00 42.16 C ANISOU 1791 CA GLY B 235 5350 5525 5143 36 -5 -28 C ATOM 1792 C GLY A 235 72.996 37.156 12.638 1.00 43.62 C ANISOU 1792 C GLY B 235 5512 5634 5426 57 -36 -13 C ATOM 1793 O GLY A 235 73.377 38.170 12.032 1.00 44.86 O ANISOU 1793 O GLY B 235 5657 5807 5581 130 77 -86 O ATOM 1794 N HIS A 236 73.824 36.195 13.051 1.00 43.85 N ANISOU 1794 N HIS B 236 5524 5707 5429 -3 -40 -4 N ATOM 1795 CA HIS A 236 75.213 36.092 12.566 1.00 45.05 C ANISOU 1795 CA HIS B 236 5734 5739 5642 25 -21 -12 C ATOM 1796 C HIS A 236 75.325 35.211 11.325 1.00 46.23 C ANISOU 1796 C HIS B 236 5957 5958 5648 53 -77 -23 C ATOM 1797 O HIS A 236 74.476 34.361 11.094 1.00 45.60 O ANISOU 1797 O HIS B 236 5997 5999 5328 119 -157 -34 O ATOM 1798 CB HIS A 236 76.112 35.514 13.643 1.00 43.90 C ANISOU 1798 CB HIS B 236 5625 5656 5399 68 -117 -43 C ATOM 1799 CG HIS A 236 76.375 36.474 14.737 1.00 42.74 C ANISOU 1799 CG HIS B 236 5394 5536 5306 77 -25 -65 C ATOM 1800 ND1 HIS A 236 77.243 37.529 14.586 1.00 40.83 N ANISOU 1800 ND1 HIS B 236 5273 5273 4968 54 17 -102 N ATOM 1801 CD2 HIS A 236 75.832 36.593 15.972 1.00 39.59 C ANISOU 1801 CD2 HIS B 236 4984 5213 4843 79 45 37 C ATOM 1802 CE1 HIS A 236 77.245 38.243 15.697 1.00 41.07 C ANISOU 1802 CE1 HIS B 236 5180 5288 5135 129 41 -65 C ATOM 1803 NE2 HIS A 236 76.397 37.699 16.550 1.00 37.84 N ANISOU 1803 NE2 HIS B 236 5062 5392 3924 -91 -74 61 N ATOM 1804 N GLU A 237 76.404 35.383 10.561 1.00 48.22 N ANISOU 1804 N GLU B 237 6165 6163 5992 23 -47 -58 N ATOM 1805 CA GLU A 237 76.620 34.559 9.372 1.00 48.37 C ANISOU 1805 CA GLU B 237 6179 6158 6039 11 -77 -56 C ATOM 1806 C GLU A 237 76.474 33.077 9.732 1.00 48.97 C ANISOU 1806 C GLU B 237 6216 6261 6128 7 -55 -45 C ATOM 1807 O GLU A 237 75.762 32.333 9.050 1.00 49.24 O ANISOU 1807 O GLU B 237 6163 6308 6238 23 -99 -85 O ATOM 1808 CB GLU A 237 77.993 34.846 8.736 1.00 49.43 C ANISOU 1808 CB GLU B 237 6281 6287 6211 41 -63 -21 C ATOM 1809 CG GLU A 237 78.244 34.145 7.389 1.00 50.36 C ANISOU 1809 CG GLU B 237 6401 6517 6216 -4 23 -170 C ATOM 1810 CD GLU A 237 77.063 34.255 6.412 1.00 56.54 C ANISOU 1810 CD GLU B 237 7316 7133 7031 19 7 107 C ATOM 1811 OE1 GLU A 237 76.390 35.324 6.366 1.00 58.27 O ANISOU 1811 OE1 GLU B 237 7526 7543 7070 -103 147 -7 O ATOM 1812 OE2 GLU A 237 76.813 33.264 5.685 1.00 59.92 O ANISOU 1812 OE2 GLU B 237 7536 7759 7472 100 -72 -69 O ATOM 1813 N GLU A 238 77.093 32.682 10.845 1.00 48.81 N ANISOU 1813 N GLU B 238 6200 6205 6140 -10 -44 -13 N ATOM 1814 CA GLU A 238 77.016 31.311 11.358 1.00 49.25 C ANISOU 1814 CA GLU B 238 6259 6281 6173 -12 -57 -9 C ATOM 1815 C GLU A 238 75.642 30.884 11.868 1.00 48.52 C ANISOU 1815 C GLU B 238 6190 6219 6025 9 -69 -13 C ATOM 1816 O GLU A 238 75.388 29.699 12.032 1.00 47.87 O ANISOU 1816 O GLU B 238 6208 6212 5769 -53 -11 -50 O ATOM 1817 CB GLU A 238 77.999 31.116 12.510 1.00 49.64 C ANISOU 1817 CB GLU B 238 6309 6321 6229 -32 -28 41 C ATOM 1818 CG GLU A 238 79.445 31.338 12.141 1.00 50.68 C ANISOU 1818 CG GLU B 238 6432 6409 6415 -22 -31 -59 C ATOM 1819 CD GLU A 238 79.913 32.773 12.307 1.00 50.84 C ANISOU 1819 CD GLU B 238 6380 6441 6494 -53 -87 14 C ATOM 1820 OE1 GLU A 238 79.079 33.700 12.381 1.00 49.57 O ANISOU 1820 OE1 GLU B 238 6312 6128 6392 47 -194 42 O ATOM 1821 OE2 GLU A 238 81.138 32.972 12.355 1.00 53.13 O ANISOU 1821 OE2 GLU B 238 6701 6625 6857 57 -178 -31 O ATOM 1822 N SER A 239 74.766 31.835 12.147 1.00 49.20 N ANISOU 1822 N SER B 239 6281 6223 6189 13 -65 32 N ATOM 1823 CA SER A 239 73.488 31.488 12.737 1.00 50.38 C ANISOU 1823 CA SER B 239 6394 6405 6342 0 -7 -33 C ATOM 1824 C SER A 239 72.631 30.743 11.722 1.00 51.04 C ANISOU 1824 C SER B 239 6455 6509 6429 -6 -27 -14 C ATOM 1825 O SER A 239 72.799 30.917 10.512 1.00 49.47 O ANISOU 1825 O SER B 239 6167 6353 6276 -10 -39 7 O ATOM 1826 CB SER A 239 72.744 32.729 13.219 1.00 49.79 C ANISOU 1826 CB SER B 239 6301 6349 6268 60 -27 -5 C ATOM 1827 OG SER A 239 73.524 33.442 14.154 1.00 46.65 O ANISOU 1827 OG SER B 239 5992 6010 5723 -26 171 -21 O ATOM 1828 N PRO A 240 71.734 29.878 12.215 1.00 52.45 N ANISOU 1828 N PRO B 240 6598 6667 6663 34 -13 -37 N ATOM 1829 CA PRO A 240 70.664 29.332 11.399 1.00 54.57 C ANISOU 1829 CA PRO B 240 6908 6883 6944 59 -73 -14 C ATOM 1830 C PRO A 240 69.969 30.386 10.531 1.00 56.42 C ANISOU 1830 C PRO B 240 7114 7155 7168 15 1 -7 C ATOM 1831 O PRO A 240 69.889 31.558 10.910 1.00 56.44 O ANISOU 1831 O PRO B 240 7151 7166 7125 54 -51 -15 O ATOM 1832 CB PRO A 240 69.703 28.761 12.442 1.00 53.93 C ANISOU 1832 CB PRO B 240 6844 6806 6841 -18 -4 15 C ATOM 1833 CG PRO A 240 70.608 28.337 13.568 1.00 52.61 C ANISOU 1833 CG PRO B 240 6658 6736 6593 8 -100 -22 C ATOM 1834 CD PRO A 240 71.731 29.322 13.582 1.00 51.96 C ANISOU 1834 CD PRO B 240 6618 6576 6549 2 -10 -16 C ATOM 1835 N GLY A 241 69.481 29.956 9.370 1.00 59.16 N ANISOU 1835 N GLY B 241 7491 7508 7477 22 -39 10 N ATOM 1836 CA GLY A 241 68.766 30.832 8.438 1.00 61.19 C ANISOU 1836 CA GLY B 241 7759 7740 7749 -33 -10 99 C ATOM 1837 C GLY A 241 69.626 31.187 7.247 1.00 63.14 C ANISOU 1837 C GLY B 241 8025 8034 7928 28 -24 -1 C ATOM 1838 O GLY A 241 70.718 30.643 7.075 1.00 63.06 O ANISOU 1838 O GLY B 241 7994 8098 7866 15 -19 -10 O ATOM 1839 N GLU A 242 69.139 32.113 6.432 1.00 65.62 N ANISOU 1839 N GLU B 242 8282 8381 8267 5 7 24 N ATOM 1840 CA GLU A 242 69.863 32.539 5.239 1.00 67.96 C ANISOU 1840 CA GLU B 242 8643 8658 8520 -8 37 -24 C ATOM 1841 C GLU A 242 70.140 34.038 5.253 1.00 69.53 C ANISOU 1841 C GLU B 242 8772 8867 8778 -3 30 -7 C ATOM 1842 O GLU A 242 69.362 34.834 5.802 1.00 69.65 O ANISOU 1842 O GLU B 242 8812 8884 8767 -35 59 -35 O ATOM 1843 CB GLU A 242 69.150 32.120 3.939 1.00 68.77 C ANISOU 1843 CB GLU B 242 8705 8737 8685 -2 -8 34 C ATOM 1844 CG GLU A 242 67.638 31.905 4.013 1.00 70.40 C ANISOU 1844 CG GLU B 242 8961 8847 8941 15 -34 41 C ATOM 1845 CD GLU A 242 67.090 31.259 2.738 1.00 70.37 C ANISOU 1845 CD GLU B 242 8964 8904 8867 -2 -16 55 C ATOM 1846 OE1 GLU A 242 67.565 31.617 1.634 1.00 72.48 O ANISOU 1846 OE1 GLU B 242 9267 9210 9062 35 0 -57 O ATOM 1847 OE2 GLU A 242 66.192 30.390 2.839 1.00 73.26 O ANISOU 1847 OE2 GLU B 242 9224 9244 9365 144 14 -28 O ATOM 1848 N THR A 243 71.278 34.397 4.663 1.00 70.63 N ANISOU 1848 N THR B 243 8950 8961 8925 11 15 -18 N ATOM 1849 CA THR A 243 71.686 35.782 4.521 1.00 71.14 C ANISOU 1849 CA THR B 243 8993 9028 9009 37 2 -24 C ATOM 1850 C THR A 243 70.976 36.388 3.312 1.00 72.21 C ANISOU 1850 C THR B 243 9141 9160 9135 5 11 -8 C ATOM 1851 O THR A 243 70.848 35.741 2.269 1.00 72.95 O ANISOU 1851 O THR B 243 9217 9266 9233 6 -9 -36 O ATOM 1852 CB THR A 243 73.209 35.885 4.332 1.00 71.33 C ANISOU 1852 CB THR B 243 9045 9038 9017 21 -25 -21 C ATOM 1853 OG1 THR A 243 73.878 35.233 5.426 1.00 70.98 O ANISOU 1853 OG1 THR B 243 8924 9034 9010 0 -11 -96 O ATOM 1854 CG2 THR A 243 73.648 37.342 4.246 1.00 70.79 C ANISOU 1854 CG2 THR B 243 8960 9007 8929 1 10 5 C ATOM 1855 N ILE A 244 70.523 37.629 3.461 1.00 72.67 N ANISOU 1855 N ILE B 244 9191 9218 9200 -5 -3 -15 N ATOM 1856 CA ILE A 244 69.735 38.325 2.441 1.00 72.74 C ANISOU 1856 CA ILE B 244 9208 9224 9206 -7 11 9 C ATOM 1857 C ILE A 244 70.504 39.541 1.929 1.00 72.86 C ANISOU 1857 C ILE B 244 9202 9269 9212 1 29 9 C ATOM 1858 O ILE A 244 70.952 40.379 2.713 1.00 72.92 O ANISOU 1858 O ILE B 244 9181 9322 9201 19 59 1 O ATOM 1859 CB ILE A 244 68.368 38.765 3.022 1.00 73.03 C ANISOU 1859 CB ILE B 244 9277 9248 9220 -9 7 1 C ATOM 1860 CG1 ILE A 244 67.481 37.531 3.276 1.00 73.51 C ANISOU 1860 CG1 ILE B 244 9314 9290 9325 8 -3 -4 C ATOM 1861 CG2 ILE A 244 67.668 39.768 2.096 1.00 72.75 C ANISOU 1861 CG2 ILE B 244 9213 9202 9226 -5 3 0 C ATOM 1862 CD1 ILE A 244 66.596 37.624 4.541 1.00 73.48 C ANISOU 1862 CD1 ILE B 244 9304 9288 9324 -7 -13 -10 C ATOM 1863 N ASN A 268 78.117 44.217 -2.886 1.00 67.28 N ANISOU 1863 N ASN B 268 8552 8488 8523 -32 25 -5 N ATOM 1864 CA ASN A 268 77.127 45.257 -2.595 1.00 66.81 C ANISOU 1864 CA ASN B 268 8496 8427 8458 -9 4 -18 C ATOM 1865 C ASN A 268 75.755 44.712 -2.132 1.00 66.95 C ANISOU 1865 C ASN B 268 8529 8443 8466 -16 13 -15 C ATOM 1866 O ASN A 268 75.648 44.196 -1.012 1.00 68.05 O ANISOU 1866 O ASN B 268 8682 8623 8550 -26 59 7 O ATOM 1867 CB ASN A 268 76.975 46.228 -3.787 1.00 66.99 C ANISOU 1867 CB ASN B 268 8499 8480 8472 1 16 -36 C ATOM 1868 CG ASN A 268 76.843 45.509 -5.128 1.00 67.44 C ANISOU 1868 CG ASN B 268 8589 8538 8494 -7 15 10 C ATOM 1869 OD1 ASN A 268 76.431 44.345 -5.199 1.00 67.19 O ANISOU 1869 OD1 ASN B 268 8619 8513 8397 33 -20 10 O ATOM 1870 ND2 ASN A 268 77.185 46.211 -6.200 1.00 67.62 N ANISOU 1870 ND2 ASN B 268 8719 8438 8535 -12 19 26 N ATOM 1871 N VAL A 269 74.745 44.769 -3.013 1.00 65.99 N ANISOU 1871 N VAL B 269 8375 8358 8337 -14 -24 -32 N ATOM 1872 CA VAL A 269 73.347 45.036 -2.620 1.00 64.91 C ANISOU 1872 CA VAL B 269 8190 8265 8205 3 -22 -3 C ATOM 1873 C VAL A 269 73.358 46.437 -1.958 1.00 64.75 C ANISOU 1873 C VAL B 269 8152 8257 8192 -18 11 -31 C ATOM 1874 O VAL A 269 73.852 47.403 -2.557 1.00 66.07 O ANISOU 1874 O VAL B 269 8185 8431 8484 30 29 -20 O ATOM 1875 CB VAL A 269 72.710 43.931 -1.698 1.00 65.18 C ANISOU 1875 CB VAL B 269 8214 8258 8293 23 -2 15 C ATOM 1876 CG1 VAL A 269 71.196 44.212 -1.470 1.00 65.31 C ANISOU 1876 CG1 VAL B 269 8303 8261 8250 0 5 5 C ATOM 1877 CG2 VAL A 269 72.918 42.542 -2.295 1.00 65.28 C ANISOU 1877 CG2 VAL B 269 8205 8347 8249 -20 -6 6 C ATOM 1878 N GLU A 270 72.832 46.547 -0.740 1.00 63.40 N ANISOU 1878 N GLU B 270 7987 8094 8007 -30 -34 -23 N ATOM 1879 CA GLU A 270 72.884 47.779 0.034 1.00 62.20 C ANISOU 1879 CA GLU B 270 7891 7907 7836 -17 55 4 C ATOM 1880 C GLU A 270 72.879 47.377 1.527 1.00 61.51 C ANISOU 1880 C GLU B 270 7814 7780 7776 -55 38 23 C ATOM 1881 O GLU A 270 72.061 47.869 2.324 1.00 63.16 O ANISOU 1881 O GLU B 270 8087 7951 7957 -60 -33 -23 O ATOM 1882 CB GLU A 270 71.683 48.694 -0.295 1.00 62.15 C ANISOU 1882 CB GLU B 270 7887 7898 7829 -31 52 12 C ATOM 1883 CG GLU A 270 70.989 48.437 -1.654 1.00 62.78 C ANISOU 1883 CG GLU B 270 7992 7957 7905 0 22 22 C ATOM 1884 CD GLU A 270 69.536 48.903 -1.691 1.00 63.69 C ANISOU 1884 CD GLU B 270 8087 7980 8131 4 55 18 C ATOM 1885 OE1 GLU A 270 68.993 49.298 -0.631 1.00 67.73 O ANISOU 1885 OE1 GLU B 270 8669 8653 8410 -3 -114 -79 O ATOM 1886 OE2 GLU A 270 68.928 48.854 -2.789 1.00 66.39 O ANISOU 1886 OE2 GLU B 270 8499 8446 8280 5 83 103 O ATOM 1887 N GLY A 271 73.775 46.466 1.903 1.00 59.67 N ANISOU 1887 N GLY B 271 7579 7556 7537 -2 36 23 N ATOM 1888 CA GLY A 271 73.852 46.009 3.297 1.00 58.65 C ANISOU 1888 CA GLY B 271 7401 7422 7460 31 22 8 C ATOM 1889 C GLY A 271 73.009 44.769 3.553 1.00 57.99 C ANISOU 1889 C GLY B 271 7342 7310 7379 30 56 44 C ATOM 1890 O GLY A 271 71.828 44.722 3.179 1.00 58.50 O ANISOU 1890 O GLY B 271 7430 7331 7463 46 106 66 O ATOM 1891 N LYS A 272 73.613 43.769 4.187 1.00 57.18 N ANISOU 1891 N LYS B 272 7242 7225 7259 14 25 32 N ATOM 1892 CA LYS A 272 72.998 42.454 4.313 1.00 57.16 C ANISOU 1892 CA LYS B 272 7253 7239 7224 -1 -9 24 C ATOM 1893 C LYS A 272 71.872 42.474 5.340 1.00 57.15 C ANISOU 1893 C LYS B 272 7269 7279 7166 12 -25 -15 C ATOM 1894 O LYS A 272 71.846 43.323 6.231 1.00 57.49 O ANISOU 1894 O LYS B 272 7311 7302 7229 17 -50 -17 O ATOM 1895 CB LYS A 272 74.045 41.409 4.705 1.00 56.48 C ANISOU 1895 CB LYS B 272 7152 7184 7121 -15 6 24 C ATOM 1896 CG LYS A 272 74.906 40.926 3.549 1.00 56.89 C ANISOU 1896 CG LYS B 272 7194 7275 7146 -46 1 2 C ATOM 1897 CD LYS A 272 76.038 40.037 4.038 1.00 57.15 C ANISOU 1897 CD LYS B 272 7321 7211 7180 -8 12 -1 C ATOM 1898 CE LYS A 272 76.987 40.800 4.948 1.00 57.61 C ANISOU 1898 CE LYS B 272 7352 7247 7288 54 4 -19 C ATOM 1899 NZ LYS A 272 78.125 39.953 5.400 1.00 58.03 N ANISOU 1899 NZ LYS B 272 7439 7300 7308 11 2 28 N ATOM 1900 N LYS A 273 70.948 41.526 5.219 1.00 57.41 N ANISOU 1900 N LYS B 273 7271 7340 7199 15 -29 -11 N ATOM 1901 CA LYS A 273 70.178 41.063 6.368 1.00 58.73 C ANISOU 1901 CA LYS B 273 7477 7433 7405 17 -5 10 C ATOM 1902 C LYS A 273 70.260 39.548 6.525 1.00 59.50 C ANISOU 1902 C LYS B 273 7537 7571 7498 12 -7 20 C ATOM 1903 O LYS A 273 70.476 38.824 5.554 1.00 59.20 O ANISOU 1903 O LYS B 273 7574 7569 7348 20 -15 11 O ATOM 1904 CB LYS A 273 68.717 41.503 6.248 1.00 58.72 C ANISOU 1904 CB LYS B 273 7480 7427 7402 -10 -9 38 C ATOM 1905 CG LYS A 273 68.462 42.932 6.698 1.00 58.82 C ANISOU 1905 CG LYS B 273 7501 7426 7423 -33 38 31 C ATOM 1906 CD LYS A 273 68.988 43.933 5.683 1.00 59.73 C ANISOU 1906 CD LYS B 273 7554 7599 7540 -29 22 44 C ATOM 1907 CE LYS A 273 68.195 45.229 5.723 1.00 60.23 C ANISOU 1907 CE LYS B 273 7522 7699 7660 -12 3 4 C ATOM 1908 NZ LYS A 273 69.012 46.394 5.285 1.00 62.22 N ANISOU 1908 NZ LYS B 273 7961 7728 7951 14 61 43 N ATOM 1909 N MET A 274 70.087 39.077 7.756 1.00 61.10 N ANISOU 1909 N MET B 274 7750 7767 7698 -1 38 24 N ATOM 1910 CA MET A 274 70.182 37.653 8.053 1.00 61.21 C ANISOU 1910 CA MET B 274 7749 7789 7718 6 51 12 C ATOM 1911 C MET A 274 68.801 37.008 8.106 1.00 63.12 C ANISOU 1911 C MET B 274 8056 7954 7971 13 38 14 C ATOM 1912 O MET A 274 68.427 36.245 7.215 1.00 64.75 O ANISOU 1912 O MET B 274 8342 8144 8115 9 25 40 O ATOM 1913 CB MET A 274 70.916 37.430 9.377 1.00 61.80 C ANISOU 1913 CB MET B 274 7884 7822 7772 10 61 -10 C ATOM 1914 CG MET A 274 71.858 36.237 9.372 1.00 62.39 C ANISOU 1914 CG MET B 274 7860 7920 7922 -25 91 -6 C ATOM 1915 SD MET A 274 71.137 34.783 8.587 1.00 67.39 S ANISOU 1915 SD MET B 274 8554 8720 8330 -79 -62 94 S ATOM 1916 CE MET A 274 72.563 33.702 8.500 1.00 63.76 C ANISOU 1916 CE MET B 274 8039 8156 8029 73 -28 31 C ATOM 1917 N PHE A 275 68.048 37.319 9.156 1.00 64.10 N ANISOU 1917 N PHE B 275 8144 8094 8115 -14 13 46 N ATOM 1918 CA PHE A 275 66.592 37.332 9.078 1.00 64.41 C ANISOU 1918 CA PHE B 275 8105 8202 8166 7 4 -4 C ATOM 1919 C PHE A 275 66.020 38.624 9.653 1.00 65.43 C ANISOU 1919 C PHE B 275 8225 8374 8260 18 -26 5 C ATOM 1920 O PHE A 275 64.836 38.919 9.484 1.00 66.08 O ANISOU 1920 O PHE B 275 8260 8501 8345 15 51 24 O ATOM 1921 CB PHE A 275 66.005 36.125 9.812 1.00 67.34 C ANISOU 1921 CB PHE B 275 8776 8377 8430 -234 313 -71 C ATOM 1922 CG PHE A 275 65.728 34.948 8.920 1.00 63.63 C ANISOU 1922 CG PHE B 275 7927 8083 8164 87 -136 4 C ATOM 1923 CD1 PHE A 275 66.710 34.456 8.076 1.00 65.08 C ANISOU 1923 CD1 PHE B 275 8259 8187 8278 -26 40 58 C ATOM 1924 CD2 PHE A 275 64.487 34.335 8.924 1.00 65.42 C ANISOU 1924 CD2 PHE B 275 8310 8223 8321 -76 -54 -109 C ATOM 1925 CE1 PHE A 275 66.459 33.374 7.254 1.00 64.95 C ANISOU 1925 CE1 PHE B 275 8050 8455 8170 76 -38 169 C ATOM 1926 CE2 PHE A 275 64.229 33.253 8.105 1.00 63.02 C ANISOU 1926 CE2 PHE B 275 7871 7956 8116 147 -125 34 C ATOM 1927 CZ PHE A 275 65.217 32.772 7.268 1.00 63.48 C ANISOU 1927 CZ PHE B 275 7934 8089 8093 103 -57 58 C ATOM 1928 N VAL A 276 66.867 39.390 10.332 1.00 20.00 N ATOM 1929 CA VAL A 276 66.626 40.815 10.525 1.00 20.00 C ATOM 1930 C VAL A 276 67.931 41.569 10.756 1.00 20.00 C ATOM 1931 O VAL A 276 68.370 41.735 11.894 1.00 20.00 O ATOM 1932 CB VAL A 276 65.679 41.071 11.712 1.00 20.00 C ATOM 1933 CG1 VAL A 276 64.451 41.845 11.256 1.00 20.00 C ATOM 1934 CG2 VAL A 276 65.277 39.759 12.367 1.00 20.00 C ATOM 1935 N GLU A 277 68.547 42.022 9.669 1.00 62.70 N ANISOU 1935 N GLU B 277 7986 7904 7930 30 10 6 N ATOM 1936 CA GLU A 277 69.890 42.586 9.728 1.00 60.43 C ANISOU 1936 CA GLU B 277 7709 7627 7624 -72 9 0 C ATOM 1937 C GLU A 277 70.946 41.489 9.808 1.00 59.30 C ANISOU 1937 C GLU B 277 7591 7483 7457 -28 15 -73 C ATOM 1938 O GLU A 277 70.619 40.305 9.895 1.00 60.55 O ANISOU 1938 O GLU B 277 7711 7684 7611 -14 47 -67 O ATOM 1939 CB GLU A 277 70.022 43.531 10.925 1.00 61.07 C ANISOU 1939 CB GLU B 277 7755 7759 7687 -58 -4 4 C ATOM 1940 CG GLU A 277 70.806 44.799 10.631 1.00 63.96 C ANISOU 1940 CG GLU B 277 8072 8066 8163 76 -16 6 C ATOM 1941 CD GLU A 277 69.944 45.891 10.028 1.00 70.25 C ANISOU 1941 CD GLU B 277 8913 8992 8783 -2 234 24 C ATOM 1942 OE1 GLU A 277 69.932 47.012 10.577 1.00 74.01 O ANISOU 1942 OE1 GLU B 277 9157 9504 9458 38 27 17 O ATOM 1943 OE2 GLU A 277 69.279 45.627 9.004 1.00 72.99 O ANISOU 1943 OE2 GLU B 277 9191 9394 9145 84 -132 -35 O ATOM 1944 N HIS A 278 72.213 41.890 9.778 1.00 56.39 N ANISOU 1944 N HIS B 278 7185 7127 7114 -24 29 -24 N ATOM 1945 CA HIS A 278 73.316 40.939 9.737 1.00 54.65 C ANISOU 1945 CA HIS B 278 6965 6980 6817 32 11 28 C ATOM 1946 C HIS A 278 74.503 41.434 10.557 1.00 53.24 C ANISOU 1946 C HIS B 278 6738 6862 6628 37 9 0 C ATOM 1947 O HIS A 278 75.015 42.530 10.327 1.00 53.78 O ANISOU 1947 O HIS B 278 6773 7015 6644 78 35 25 O ATOM 1948 CB HIS A 278 73.747 40.678 8.293 1.00 53.89 C ANISOU 1948 CB HIS B 278 6857 6870 6750 -3 22 17 C ATOM 1949 CG HIS A 278 74.659 39.501 8.137 1.00 54.17 C ANISOU 1949 CG HIS B 278 6922 6893 6764 32 -2 -7 C ATOM 1950 ND1 HIS A 278 76.004 39.557 8.435 1.00 52.80 N ANISOU 1950 ND1 HIS B 278 6676 6830 6553 38 -90 18 N ATOM 1951 CD2 HIS A 278 74.420 38.237 7.715 1.00 50.83 C ANISOU 1951 CD2 HIS B 278 6580 6429 6302 -5 149 -65 C ATOM 1952 CE1 HIS A 278 76.553 38.378 8.203 1.00 51.60 C ANISOU 1952 CE1 HIS B 278 6547 6558 6499 77 47 -9 C ATOM 1953 NE2 HIS A 278 75.614 37.559 7.765 1.00 50.13 N ANISOU 1953 NE2 HIS B 278 6281 6498 6268 35 179 49 N ATOM 1954 N LYS A 279 74.936 40.620 11.514 1.00 51.54 N ANISOU 1954 N LYS B 279 6512 6601 6468 25 -29 -8 N ATOM 1955 CA LYS A 279 75.788 41.091 12.588 1.00 50.04 C ANISOU 1955 CA LYS B 279 6325 6373 6313 5 -9 -62 C ATOM 1956 C LYS A 279 77.211 40.660 12.324 1.00 49.10 C ANISOU 1956 C LYS B 279 6185 6281 6187 27 -16 -50 C ATOM 1957 O LYS A 279 78.109 40.939 13.108 1.00 48.91 O ANISOU 1957 O LYS B 279 6122 6314 6147 79 -12 -31 O ATOM 1958 CB LYS A 279 75.322 40.519 13.925 1.00 49.57 C ANISOU 1958 CB LYS B 279 6330 6271 6232 7 -4 -48 C ATOM 1959 CG LYS A 279 74.053 41.129 14.471 1.00 48.26 C ANISOU 1959 CG LYS B 279 6150 6141 6044 2 -29 19 C ATOM 1960 CD LYS A 279 73.682 40.487 15.778 1.00 47.99 C ANISOU 1960 CD LYS B 279 6021 6099 6113 38 -53 26 C ATOM 1961 CE LYS A 279 72.581 41.240 16.462 1.00 45.90 C ANISOU 1961 CE LYS B 279 5839 5869 5732 127 -95 146 C ATOM 1962 NZ LYS A 279 71.297 40.548 16.364 1.00 42.18 N ANISOU 1962 NZ LYS B 279 5335 5455 5233 31 15 -175 N ATOM 1963 N GLY A 280 77.405 39.961 11.215 1.00 48.38 N ANISOU 1963 N GLY B 280 6131 6177 6073 36 20 -22 N ATOM 1964 CA GLY A 280 78.713 39.445 10.857 1.00 47.25 C ANISOU 1964 CA GLY B 280 5985 6050 5917 37 6 -9 C ATOM 1965 C GLY A 280 79.072 38.189 11.628 1.00 46.31 C ANISOU 1965 C GLY B 280 5940 5916 5738 43 -33 -28 C ATOM 1966 O GLY A 280 78.252 37.283 11.773 1.00 46.20 O ANISOU 1966 O GLY B 280 5935 5942 5675 100 -105 -3 O ATOM 1967 N SER A 281 80.304 38.137 12.125 1.00 45.18 N ANISOU 1967 N SER B 281 5778 5813 5575 66 -37 -57 N ATOM 1968 CA SER A 281 80.870 36.896 12.639 1.00 44.58 C ANISOU 1968 CA SER B 281 5725 5720 5493 49 -40 -69 C ATOM 1969 C SER A 281 80.647 36.766 14.142 1.00 43.97 C ANISOU 1969 C SER B 281 5591 5642 5473 64 -47 -85 C ATOM 1970 O SER A 281 80.926 37.691 14.904 1.00 43.93 O ANISOU 1970 O SER B 281 5685 5613 5391 146 -140 -142 O ATOM 1971 CB SER A 281 82.364 36.815 12.319 1.00 44.37 C ANISOU 1971 CB SER B 281 5793 5656 5410 74 -55 -77 C ATOM 1972 OG SER A 281 83.147 37.135 13.455 1.00 44.93 O ANISOU 1972 OG SER B 281 5990 5585 5494 124 -95 -172 O ATOM 1973 N LEU A 282 80.141 35.610 14.560 1.00 43.21 N ANISOU 1973 N LEU B 282 5446 5586 5385 39 -103 -59 N ATOM 1974 CA LEU A 282 79.975 35.313 15.966 1.00 42.25 C ANISOU 1974 CA LEU B 282 5347 5385 5319 37 -50 -24 C ATOM 1975 C LEU A 282 81.268 35.548 16.746 1.00 40.89 C ANISOU 1975 C LEU B 282 5145 5214 5175 68 -51 -91 C ATOM 1976 O LEU A 282 81.237 36.052 17.875 1.00 38.51 O ANISOU 1976 O LEU B 282 4663 5036 4933 213 -42 -251 O ATOM 1977 CB LEU A 282 79.524 33.862 16.107 1.00 42.58 C ANISOU 1977 CB LEU B 282 5379 5457 5340 42 -157 1 C ATOM 1978 CG LEU A 282 79.564 33.194 17.467 1.00 43.70 C ANISOU 1978 CG LEU B 282 5459 5645 5500 4 -5 -38 C ATOM 1979 CD1 LEU A 282 78.798 34.015 18.501 1.00 45.34 C ANISOU 1979 CD1 LEU B 282 5723 5830 5671 -21 -162 -68 C ATOM 1980 CD2 LEU A 282 78.978 31.796 17.346 1.00 43.17 C ANISOU 1980 CD2 LEU B 282 5457 5480 5465 30 -72 -11 C ATOM 1981 N GLU A 283 82.402 35.175 16.153 1.00 39.90 N ANISOU 1981 N GLU B 283 5083 5099 4978 20 -108 -143 N ATOM 1982 CA GLU A 283 83.682 35.349 16.825 1.00 39.64 C ANISOU 1982 CA GLU B 283 5018 5106 4937 15 -67 -83 C ATOM 1983 C GLU A 283 83.966 36.820 17.173 1.00 38.18 C ANISOU 1983 C GLU B 283 4938 4829 4739 13 -25 -94 C ATOM 1984 O GLU A 283 84.504 37.114 18.252 1.00 36.94 O ANISOU 1984 O GLU B 283 4837 4707 4489 108 -229 -209 O ATOM 1985 CB GLU A 283 84.837 34.778 15.997 1.00 40.62 C ANISOU 1985 CB GLU B 283 5169 5140 5121 19 -94 -41 C ATOM 1986 CG GLU A 283 86.204 35.008 16.647 1.00 40.07 C ANISOU 1986 CG GLU B 283 5173 5068 4984 -19 -111 -63 C ATOM 1987 CD GLU A 283 87.296 34.147 16.052 1.00 43.62 C ANISOU 1987 CD GLU B 283 5530 5503 5539 -128 -104 -53 C ATOM 1988 OE1 GLU A 283 88.068 34.679 15.204 1.00 49.35 O ANISOU 1988 OE1 GLU B 283 6156 6304 6289 121 -26 -355 O ATOM 1989 OE2 GLU A 283 87.376 32.943 16.425 1.00 47.67 O ANISOU 1989 OE2 GLU B 283 5672 6249 6191 -91 85 -162 O ATOM 1990 N ASP A 284 83.627 37.740 16.269 1.00 37.05 N ANISOU 1990 N ASP B 284 4786 4701 4589 -5 -91 -70 N ATOM 1991 CA ASP A 284 83.855 39.165 16.539 1.00 36.32 C ANISOU 1991 CA ASP B 284 4708 4574 4515 31 -78 -99 C ATOM 1992 C ASP A 284 82.932 39.664 17.647 1.00 34.69 C ANISOU 1992 C ASP B 284 4503 4341 4334 92 -79 -122 C ATOM 1993 O ASP A 284 83.352 40.442 18.491 1.00 34.08 O ANISOU 1993 O ASP B 284 4561 4261 4124 108 -114 -336 O ATOM 1994 CB ASP A 284 83.687 40.023 15.291 1.00 36.35 C ANISOU 1994 CB ASP B 284 4686 4618 4505 56 -29 -29 C ATOM 1995 CG ASP A 284 84.746 39.731 14.226 1.00 40.04 C ANISOU 1995 CG ASP B 284 5154 5071 4988 -41 -1 -107 C ATOM 1996 OD1 ASP A 284 85.829 39.157 14.549 1.00 38.63 O ANISOU 1996 OD1 ASP B 284 5155 4881 4643 -15 73 -253 O ATOM 1997 OD2 ASP A 284 84.471 40.083 13.047 1.00 43.20 O ANISOU 1997 OD2 ASP B 284 5555 5893 4963 -74 -16 -131 O ATOM 1998 N THR A 285 81.695 39.185 17.652 1.00 33.63 N ANISOU 1998 N THR B 285 4331 4256 4190 60 -100 -39 N ATOM 1999 CA THR A 285 80.746 39.521 18.701 1.00 32.47 C ANISOU 1999 CA THR B 285 4160 4135 4039 55 -75 10 C ATOM 2000 C THR A 285 81.231 39.090 20.085 1.00 30.65 C ANISOU 2000 C THR B 285 3882 3872 3890 87 -16 -98 C ATOM 2001 O THR A 285 81.116 39.863 21.040 1.00 30.91 O ANISOU 2001 O THR B 285 3874 3969 3902 178 -137 -165 O ATOM 2002 CB THR A 285 79.357 38.938 18.397 1.00 31.84 C ANISOU 2002 CB THR B 285 4049 4147 3902 63 -8 41 C ATOM 2003 OG1 THR A 285 78.806 39.637 17.269 1.00 30.95 O ANISOU 2003 OG1 THR B 285 3994 4543 3221 -62 -93 15 O ATOM 2004 CG2 THR A 285 78.405 39.083 19.589 1.00 32.99 C ANISOU 2004 CG2 THR B 285 4142 4240 4149 45 -119 -10 C ATOM 2005 N LEU A 286 81.784 37.883 20.190 1.00 29.86 N ANISOU 2005 N LEU B 286 3811 3787 3746 39 -134 -160 N ATOM 2006 CA LEU A 286 82.288 37.359 21.470 1.00 30.41 C ANISOU 2006 CA LEU B 286 3798 3876 3879 20 -119 -44 C ATOM 2007 C LEU A 286 83.535 38.104 21.977 1.00 29.35 C ANISOU 2007 C LEU B 286 3643 3717 3791 76 -65 -76 C ATOM 2008 O LEU A 286 83.699 38.306 23.195 1.00 28.94 O ANISOU 2008 O LEU B 286 3612 3386 3996 178 -283 6 O ATOM 2009 CB LEU A 286 82.593 35.848 21.379 1.00 30.99 C ANISOU 2009 CB LEU B 286 3851 3965 3959 58 -127 -51 C ATOM 2010 CG LEU A 286 81.418 34.874 21.355 1.00 29.35 C ANISOU 2010 CG LEU B 286 3524 3879 3746 53 24 -92 C ATOM 2011 CD1 LEU A 286 81.857 33.470 20.810 1.00 31.60 C ANISOU 2011 CD1 LEU B 286 3856 4102 4046 11 -72 -287 C ATOM 2012 CD2 LEU A 286 80.767 34.732 22.734 1.00 28.41 C ANISOU 2012 CD2 LEU B 286 3256 3781 3757 275 -298 -55 C ATOM 2013 N ILE A 287 84.409 38.488 21.050 1.00 30.63 N ANISOU 2013 N ILE B 287 3807 3844 3987 40 -202 -74 N ATOM 2014 CA ILE A 287 85.562 39.330 21.363 1.00 30.69 C ANISOU 2014 CA ILE B 287 3837 3863 3960 31 -95 -143 C ATOM 2015 C ILE A 287 85.146 40.703 21.912 1.00 29.25 C ANISOU 2015 C ILE B 287 3703 3649 3758 89 -80 -196 C ATOM 2016 O ILE A 287 85.682 41.153 22.914 1.00 25.91 O ANISOU 2016 O ILE B 287 3398 3006 3438 146 -237 -644 O ATOM 2017 CB ILE A 287 86.453 39.516 20.131 1.00 31.52 C ANISOU 2017 CB ILE B 287 3872 4006 4096 61 -37 -132 C ATOM 2018 CG1 ILE A 287 87.199 38.214 19.854 1.00 33.67 C ANISOU 2018 CG1 ILE B 287 4219 4306 4265 55 -117 -189 C ATOM 2019 CG2 ILE A 287 87.434 40.640 20.367 1.00 31.48 C ANISOU 2019 CG2 ILE B 287 4021 3892 4046 151 -20 -59 C ATOM 2020 CD1 ILE A 287 87.975 38.215 18.569 1.00 33.27 C ANISOU 2020 CD1 ILE B 287 4298 4165 4175 29 -178 -155 C ATOM 2021 N GLU A 288 84.196 41.339 21.239 1.00 29.93 N ANISOU 2021 N GLU B 288 3791 3734 3844 46 -45 -155 N ATOM 2022 CA GLU A 288 83.663 42.625 21.673 1.00 30.23 C ANISOU 2022 CA GLU B 288 3836 3848 3801 82 -53 -133 C ATOM 2023 C GLU A 288 82.955 42.492 23.029 1.00 28.64 C ANISOU 2023 C GLU B 288 3579 3700 3600 162 -64 -51 C ATOM 2024 O GLU A 288 83.158 43.311 23.935 1.00 27.80 O ANISOU 2024 O GLU B 288 3426 3544 3592 371 -109 -280 O ATOM 2025 CB GLU A 288 82.690 43.141 20.619 1.00 30.43 C ANISOU 2025 CB GLU B 288 3788 3985 3789 62 -62 -83 C ATOM 2026 CG GLU A 288 82.162 44.507 20.883 1.00 32.94 C ANISOU 2026 CG GLU B 288 4138 4167 4208 -97 -46 -102 C ATOM 2027 CD GLU A 288 81.185 44.951 19.818 1.00 36.67 C ANISOU 2027 CD GLU B 288 4825 4602 4506 -177 12 70 C ATOM 2028 OE1 GLU A 288 80.098 44.328 19.691 1.00 45.11 O ANISOU 2028 OE1 GLU B 288 5738 5493 5908 326 114 -146 O ATOM 2029 OE2 GLU A 288 81.512 45.925 19.092 1.00 48.30 O ANISOU 2029 OE2 GLU B 288 5647 6308 6396 192 325 -4 O ATOM 2030 N MET A 289 82.143 41.449 23.192 1.00 26.24 N ANISOU 2030 N MET B 289 3280 3388 3301 140 -123 -24 N ATOM 2031 CA MET A 289 81.577 41.163 24.514 1.00 27.37 C ANISOU 2031 CA MET B 289 3378 3499 3522 77 -78 -107 C ATOM 2032 C MET A 289 82.646 41.072 25.594 1.00 25.69 C ANISOU 2032 C MET B 289 3143 3217 3397 154 -88 -175 C ATOM 2033 O MET A 289 82.476 41.570 26.705 1.00 25.13 O ANISOU 2033 O MET B 289 3114 3062 3370 137 -150 -499 O ATOM 2034 CB MET A 289 80.778 39.871 24.515 1.00 26.32 C ANISOU 2034 CB MET B 289 3311 3428 3260 110 -109 -149 C ATOM 2035 CG MET A 289 79.356 40.043 24.069 1.00 30.00 C ANISOU 2035 CG MET B 289 3551 3871 3975 -42 -44 -70 C ATOM 2036 SD MET A 289 78.485 38.461 24.113 1.00 31.02 S ANISOU 2036 SD MET B 289 3776 3930 4081 344 -196 -189 S ATOM 2037 CE MET A 289 76.878 38.961 23.544 1.00 30.23 C ANISOU 2037 CE MET B 289 3690 3802 3993 188 78 -25 C ATOM 2038 N GLU A 290 83.766 40.439 25.281 1.00 26.14 N ANISOU 2038 N GLU B 290 3210 3301 3420 24 -154 -209 N ATOM 2039 CA GLU A 290 84.808 40.300 26.275 1.00 26.37 C ANISOU 2039 CA GLU B 290 3270 3343 3405 19 -110 -106 C ATOM 2040 C GLU A 290 85.475 41.638 26.563 1.00 25.41 C ANISOU 2040 C GLU B 290 3220 3091 3341 -101 -108 -123 C ATOM 2041 O GLU A 290 85.744 41.958 27.725 1.00 24.57 O ANISOU 2041 O GLU B 290 3046 2796 3493 213 -351 140 O ATOM 2042 CB GLU A 290 85.857 39.288 25.838 1.00 26.31 C ANISOU 2042 CB GLU B 290 3297 3382 3315 -8 -32 -178 C ATOM 2043 CG GLU A 290 86.943 39.087 26.876 1.00 27.01 C ANISOU 2043 CG GLU B 290 3415 3385 3462 -61 -247 -96 C ATOM 2044 CD GLU A 290 87.886 37.948 26.538 1.00 31.10 C ANISOU 2044 CD GLU B 290 3893 3806 4115 -186 -106 -40 C ATOM 2045 OE1 GLU A 290 87.788 37.397 25.399 1.00 33.95 O ANISOU 2045 OE1 GLU B 290 4281 4423 4194 -524 -413 -444 O ATOM 2046 OE2 GLU A 290 88.722 37.628 27.420 1.00 35.28 O ANISOU 2046 OE2 GLU B 290 4760 4042 4603 -306 50 55 O ATOM 2047 N GLN A 291 85.723 42.415 25.522 1.00 25.13 N ANISOU 2047 N GLN B 291 3092 3138 3318 -91 -126 -282 N ATOM 2048 CA GLN A 291 86.309 43.739 25.700 1.00 26.35 C ANISOU 2048 CA GLN B 291 3275 3317 3419 -19 -150 -132 C ATOM 2049 C GLN A 291 85.417 44.673 26.509 1.00 25.54 C ANISOU 2049 C GLN B 291 3296 3177 3227 -36 -128 -205 C ATOM 2050 O GLN A 291 85.899 45.395 27.400 1.00 25.85 O ANISOU 2050 O GLN B 291 3367 3187 3266 -1 -157 -272 O ATOM 2051 CB GLN A 291 86.585 44.385 24.355 1.00 25.47 C ANISOU 2051 CB GLN B 291 3204 3347 3123 -34 -186 -131 C ATOM 2052 CG GLN A 291 87.792 43.743 23.671 1.00 29.97 C ANISOU 2052 CG GLN B 291 3773 3701 3912 -13 -101 -183 C ATOM 2053 CD GLN A 291 87.890 44.093 22.213 1.00 30.39 C ANISOU 2053 CD GLN B 291 3805 3998 3743 64 -157 -166 C ATOM 2054 OE1 GLN A 291 86.956 44.659 21.615 1.00 38.66 O ANISOU 2054 OE1 GLN B 291 4830 4877 4980 -211 53 -112 O ATOM 2055 NE2 GLN A 291 89.023 43.739 21.608 1.00 35.04 N ANISOU 2055 NE2 GLN B 291 4450 4191 4672 119 -104 -321 N ATOM 2056 N ASP A 292 84.132 44.669 26.172 1.00 24.44 N ANISOU 2056 N ASP B 292 3052 3175 3056 -20 -144 -169 N ATOM 2057 CA ASP A 292 83.136 45.491 26.888 1.00 23.74 C ANISOU 2057 CA ASP B 292 2942 3013 3064 -2 -67 -185 C ATOM 2058 C ASP A 292 83.051 45.106 28.339 1.00 21.96 C ANISOU 2058 C ASP B 292 2699 2704 2937 25 3 -289 C ATOM 2059 O ASP A 292 83.016 45.962 29.233 1.00 22.68 O ANISOU 2059 O ASP B 292 2628 2858 3129 157 -19 -494 O ATOM 2060 CB ASP A 292 81.770 45.402 26.212 1.00 23.44 C ANISOU 2060 CB ASP B 292 2950 2984 2973 -8 -18 -194 C ATOM 2061 CG ASP A 292 81.767 46.039 24.856 1.00 27.46 C ANISOU 2061 CG ASP B 292 3527 3538 3364 -10 17 -127 C ATOM 2062 OD1 ASP A 292 82.746 46.766 24.561 1.00 30.68 O ANISOU 2062 OD1 ASP B 292 3847 3714 4093 156 -200 -356 O ATOM 2063 OD2 ASP A 292 80.795 45.843 24.104 1.00 28.28 O ANISOU 2063 OD2 ASP B 292 3959 3658 3125 -86 -295 -142 O ATOM 2064 N LEU A 293 83.070 43.813 28.595 1.00 22.51 N ANISOU 2064 N LEU B 293 2773 2786 2993 -130 -66 -285 N ATOM 2065 CA LEU A 293 83.087 43.320 29.970 1.00 22.23 C ANISOU 2065 CA LEU B 293 2809 2816 2819 -1 -66 -189 C ATOM 2066 C LEU A 293 84.369 43.659 30.779 1.00 22.56 C ANISOU 2066 C LEU B 293 2814 2913 2844 -55 -62 -198 C ATOM 2067 O LEU A 293 84.303 43.966 31.974 1.00 19.56 O ANISOU 2067 O LEU B 293 2548 2611 2271 -117 158 -85 O ATOM 2068 CB LEU A 293 82.812 41.823 29.949 1.00 22.09 C ANISOU 2068 CB LEU B 293 2698 3159 2537 -138 -142 -117 C ATOM 2069 CG LEU A 293 82.282 41.167 31.208 1.00 23.41 C ANISOU 2069 CG LEU B 293 2702 2984 3209 47 20 -265 C ATOM 2070 CD1 LEU A 293 81.143 41.922 31.929 1.00 25.31 C ANISOU 2070 CD1 LEU B 293 2954 3280 3380 51 43 -77 C ATOM 2071 CD2 LEU A 293 81.844 39.726 30.788 1.00 24.32 C ANISOU 2071 CD2 LEU B 293 3000 2940 3300 191 -230 -153 C ATOM 2072 N GLN A 294 85.525 43.659 30.122 1.00 22.89 N ANISOU 2072 N GLN B 294 2763 2805 3127 -29 -114 -188 N ATOM 2073 CA GLN A 294 86.771 44.170 30.727 1.00 21.46 C ANISOU 2073 CA GLN B 294 2668 2735 2747 -24 -53 -83 C ATOM 2074 C GLN A 294 86.653 45.653 31.091 1.00 21.30 C ANISOU 2074 C GLN B 294 2713 2692 2687 82 -54 -46 C ATOM 2075 O GLN A 294 87.131 46.063 32.143 1.00 20.11 O ANISOU 2075 O GLN B 294 2650 2546 2442 144 -204 -221 O ATOM 2076 CB GLN A 294 87.972 43.966 29.770 1.00 20.14 C ANISOU 2076 CB GLN B 294 2501 2606 2544 123 159 -199 C ATOM 2077 CG GLN A 294 88.357 42.508 29.603 1.00 21.59 C ANISOU 2077 CG GLN B 294 2809 2681 2711 -123 15 -247 C ATOM 2078 CD GLN A 294 89.471 42.288 28.627 1.00 22.83 C ANISOU 2078 CD GLN B 294 2932 2802 2939 -84 19 -111 C ATOM 2079 OE1 GLN A 294 89.473 42.862 27.526 1.00 27.13 O ANISOU 2079 OE1 GLN B 294 3755 3520 3030 -1 -109 -477 O ATOM 2080 NE2 GLN A 294 90.436 41.446 29.016 1.00 26.75 N ANISOU 2080 NE2 GLN B 294 2882 3256 4022 -286 -97 -444 N ATOM 2081 N SER A 295 86.031 46.444 30.216 1.00 21.07 N ANISOU 2081 N SER B 295 2549 2594 2862 109 85 -197 N ATOM 2082 CA SER A 295 85.743 47.844 30.537 1.00 21.76 C ANISOU 2082 CA SER B 295 2624 2703 2940 71 -21 -29 C ATOM 2083 C SER A 295 84.871 47.998 31.762 1.00 21.26 C ANISOU 2083 C SER B 295 2523 2552 3001 94 -24 -24 C ATOM 2084 O SER A 295 85.145 48.841 32.620 1.00 21.41 O ANISOU 2084 O SER B 295 2381 2386 3367 258 -231 -68 O ATOM 2085 CB SER A 295 85.076 48.556 29.371 1.00 22.72 C ANISOU 2085 CB SER B 295 2856 2869 2907 154 4 7 C ATOM 2086 OG SER A 295 85.922 48.598 28.258 1.00 26.61 O ANISOU 2086 OG SER B 295 3533 2880 3697 54 -200 -323 O ATOM 2087 N SER A 296 83.839 47.162 31.867 1.00 22.01 N ANISOU 2087 N SER B 296 2672 2530 3160 64 -142 88 N ATOM 2088 CA SER A 296 82.978 47.100 33.048 1.00 19.48 C ANISOU 2088 CA SER B 296 2401 2377 2623 57 -42 107 C ATOM 2089 C SER A 296 83.766 46.828 34.298 1.00 18.67 C ANISOU 2089 C SER B 296 2304 2316 2472 58 -60 -5 C ATOM 2090 O SER A 296 83.597 47.528 35.244 1.00 16.31 O ANISOU 2090 O SER B 296 2256 2073 1868 -17 -153 78 O ATOM 2091 CB SER A 296 81.878 46.000 32.919 1.00 19.07 C ANISOU 2091 CB SER B 296 2290 2319 2637 23 -60 15 C ATOM 2092 OG SER A 296 80.926 46.325 31.948 1.00 18.35 O ANISOU 2092 OG SER B 296 2146 2280 2543 151 -85 28 O ATOM 2093 N ILE A 297 84.662 45.843 34.272 1.00 19.29 N ANISOU 2093 N ILE B 297 2256 2477 2594 73 13 48 N ATOM 2094 CA ILE A 297 85.530 45.539 35.434 1.00 19.28 C ANISOU 2094 CA ILE B 297 2348 2395 2581 -17 15 46 C ATOM 2095 C ILE A 297 86.438 46.734 35.749 1.00 17.71 C ANISOU 2095 C ILE B 297 2197 2101 2428 -82 26 68 C ATOM 2096 O ILE A 297 86.647 47.056 36.912 1.00 18.70 O ANISOU 2096 O ILE B 297 2195 2026 2882 -193 -137 -62 O ATOM 2097 CB ILE A 297 86.376 44.213 35.216 1.00 18.94 C ANISOU 2097 CB ILE B 297 2272 2612 2312 23 -79 36 C ATOM 2098 CG1 ILE A 297 85.424 43.018 35.046 1.00 20.54 C ANISOU 2098 CG1 ILE B 297 2517 2624 2660 -14 -79 -99 C ATOM 2099 CG2 ILE A 297 87.355 43.964 36.393 1.00 19.56 C ANISOU 2099 CG2 ILE B 297 2218 2360 2853 44 -6 1 C ATOM 2100 CD1 ILE A 297 86.076 41.771 34.528 1.00 21.96 C ANISOU 2100 CD1 ILE B 297 2520 2648 3175 -101 99 -73 C ATOM 2101 N SER A 298 86.952 47.404 34.719 1.00 17.83 N ANISOU 2101 N SER B 298 2286 2060 2427 -17 -9 46 N ATOM 2102 CA ASER A 298 87.766 48.605 34.930 0.50 19.28 C ANISOU 2102 CA ASER B 298 2413 2373 2537 22 -1 61 C ATOM 2103 C SER A 298 86.984 49.657 35.716 1.00 19.05 C ANISOU 2103 C SER B 298 2390 2306 2542 33 2 17 C ATOM 2104 O SER A 298 87.451 50.171 36.732 1.00 18.79 O ANISOU 2104 O SER B 298 2776 1954 2408 109 129 123 O ATOM 2105 CB ASER A 298 88.233 49.178 33.593 0.50 19.63 C ANISOU 2105 CB ASER B 298 2560 2274 2622 129 -55 -97 C ATOM 2106 OG ASER A 298 88.970 48.192 32.895 0.50 24.37 O ANISOU 2106 OG ASER B 298 2891 3020 3349 -95 -163 -81 O ATOM 2107 N TYR A 299 85.804 49.991 35.217 1.00 20.12 N ANISOU 2107 N TYR B 299 2411 2294 2938 82 -129 44 N ATOM 2108 CA TYR A 299 84.916 50.935 35.902 1.00 19.78 C ANISOU 2108 CA TYR B 299 2409 2453 2652 -21 -25 42 C ATOM 2109 C TYR A 299 84.500 50.498 37.285 1.00 19.03 C ANISOU 2109 C TYR B 299 2492 2226 2512 -159 -103 272 C ATOM 2110 O TYR A 299 84.259 51.349 38.097 1.00 19.33 O ANISOU 2110 O TYR B 299 2363 2576 2404 -35 -268 476 O ATOM 2111 CB TYR A 299 83.643 51.198 35.072 1.00 21.88 C ANISOU 2111 CB TYR B 299 2750 2646 2917 49 2 127 C ATOM 2112 CG TYR A 299 83.833 52.187 33.940 1.00 19.99 C ANISOU 2112 CG TYR B 299 2540 2270 2784 190 -14 104 C ATOM 2113 CD1 TYR A 299 84.110 53.524 34.218 1.00 22.41 C ANISOU 2113 CD1 TYR B 299 2538 2628 3345 49 29 -159 C ATOM 2114 CD2 TYR A 299 83.709 51.816 32.628 1.00 24.48 C ANISOU 2114 CD2 TYR B 299 2855 3333 3111 146 22 -68 C ATOM 2115 CE1 TYR A 299 84.302 54.429 33.224 1.00 20.69 C ANISOU 2115 CE1 TYR B 299 2678 2808 2374 -215 -80 213 C ATOM 2116 CE2 TYR A 299 83.896 52.752 31.586 1.00 24.02 C ANISOU 2116 CE2 TYR B 299 2921 3342 2862 -52 154 352 C ATOM 2117 CZ TYR A 299 84.195 54.060 31.908 1.00 21.40 C ANISOU 2117 CZ TYR B 299 2729 2679 2722 -41 4 166 C ATOM 2118 OH TYR A 299 84.386 55.072 30.972 1.00 25.97 O ANISOU 2118 OH TYR B 299 3323 3660 2883 181 141 279 O ATOM 2119 N ALA A 300 84.377 49.187 37.528 1.00 18.42 N ANISOU 2119 N ALA B 300 2341 2325 2332 79 156 179 N ATOM 2120 CA ALA A 300 84.019 48.660 38.866 1.00 20.74 C ANISOU 2120 CA ALA B 300 2592 2634 2652 36 -51 32 C ATOM 2121 C ALA A 300 85.145 48.770 39.889 1.00 21.11 C ANISOU 2121 C ALA B 300 2598 2650 2771 43 -2 56 C ATOM 2122 O ALA A 300 84.940 48.435 41.038 1.00 21.08 O ANISOU 2122 O ALA B 300 2633 2623 2753 302 -129 -9 O ATOM 2123 CB ALA A 300 83.556 47.210 38.782 1.00 20.31 C ANISOU 2123 CB ALA B 300 2596 2533 2586 -23 95 54 C ATOM 2124 N GLY A 301 86.330 49.220 39.476 1.00 22.32 N ANISOU 2124 N GLY B 301 2664 2722 3094 79 -6 19 N ATOM 2125 CA GLY A 301 87.450 49.379 40.424 1.00 22.12 C ANISOU 2125 CA GLY B 301 2819 2743 2840 41 -10 -10 C ATOM 2126 C GLY A 301 88.131 48.074 40.802 1.00 22.69 C ANISOU 2126 C GLY B 301 3003 2732 2886 34 40 -33 C ATOM 2127 O GLY A 301 88.745 47.966 41.867 1.00 24.55 O ANISOU 2127 O GLY B 301 3233 2944 3151 0 149 -86 O ATOM 2128 N GLY A 302 88.038 47.081 39.920 1.00 22.86 N ANISOU 2128 N GLY B 302 2907 2732 3043 -38 63 1 N ATOM 2129 CA GLY A 302 88.631 45.771 40.156 1.00 23.55 C ANISOU 2129 CA GLY B 302 2984 2975 2987 -1 43 11 C ATOM 2130 C GLY A 302 89.457 45.259 39.011 1.00 23.53 C ANISOU 2130 C GLY B 302 2860 2942 3137 -86 109 -71 C ATOM 2131 O GLY A 302 89.737 45.968 38.062 1.00 19.49 O ANISOU 2131 O GLY B 302 2594 2695 2116 -396 203 8 O ATOM 2132 N THR A 303 89.872 44.005 39.128 1.00 25.25 N ANISOU 2132 N THR B 303 2961 3057 3575 6 149 51 N ATOM 2133 CA THR A 303 90.569 43.334 38.048 1.00 25.08 C ANISOU 2133 CA THR B 303 3119 3097 3311 1 66 56 C ATOM 2134 C THR A 303 89.897 42.030 37.620 1.00 26.20 C ANISOU 2134 C THR B 303 3199 3324 3430 -76 109 -45 C ATOM 2135 O THR A 303 90.367 41.375 36.683 1.00 27.18 O ANISOU 2135 O THR B 303 3138 3585 3604 -227 -88 -358 O ATOM 2136 CB THR A 303 92.007 42.990 38.501 1.00 26.59 C ANISOU 2136 CB THR B 303 3365 3216 3522 95 90 67 C ATOM 2137 OG1 THR A 303 91.939 41.991 39.526 1.00 24.22 O ANISOU 2137 OG1 THR B 303 3226 2527 3448 -329 240 751 O ATOM 2138 CG2 THR A 303 92.690 44.248 39.087 1.00 28.08 C ANISOU 2138 CG2 THR B 303 3325 3385 3959 -30 -2 94 C ATOM 2139 N LYS A 304 88.819 41.626 38.305 1.00 26.89 N ANISOU 2139 N LYS B 304 3185 3263 3766 -23 40 20 N ATOM 2140 CA LYS A 304 88.135 40.395 37.931 1.00 26.26 C ANISOU 2140 CA LYS B 304 3218 3152 3606 39 -19 83 C ATOM 2141 C LYS A 304 86.616 40.553 38.026 1.00 25.29 C ANISOU 2141 C LYS B 304 3019 3090 3499 84 -80 -25 C ATOM 2142 O LYS A 304 86.115 41.550 38.534 1.00 22.89 O ANISOU 2142 O LYS B 304 2612 2713 3371 74 -52 -81 O ATOM 2143 CB LYS A 304 88.648 39.226 38.770 1.00 27.80 C ANISOU 2143 CB LYS B 304 3242 3426 3891 60 -123 -17 C ATOM 2144 CG LYS A 304 88.444 39.362 40.240 1.00 30.47 C ANISOU 2144 CG LYS B 304 3833 3964 3777 33 161 241 C ATOM 2145 CD LYS A 304 89.386 38.404 41.017 1.00 30.87 C ANISOU 2145 CD LYS B 304 3841 3856 4030 -75 149 204 C ATOM 2146 CE LYS A 304 88.892 38.159 42.430 1.00 37.15 C ANISOU 2146 CE LYS B 304 4815 4838 4462 77 52 -95 C ATOM 2147 NZ LYS A 304 89.234 39.231 43.423 1.00 43.32 N ANISOU 2147 NZ LYS B 304 5106 5835 5516 44 -260 136 N ATOM 2148 N LEU A 305 85.907 39.563 37.490 1.00 24.64 N ANISOU 2148 N LEU B 305 3010 3000 3352 64 -11 149 N ATOM 2149 CA LEU A 305 84.468 39.637 37.308 1.00 23.68 C ANISOU 2149 CA LEU B 305 2892 2932 3172 82 -23 72 C ATOM 2150 C LEU A 305 83.701 39.944 38.582 1.00 21.72 C ANISOU 2150 C LEU B 305 2685 2703 2864 117 -67 261 C ATOM 2151 O LEU A 305 82.767 40.768 38.597 1.00 21.30 O ANISOU 2151 O LEU B 305 2578 2788 2725 20 82 336 O ATOM 2152 CB LEU A 305 83.994 38.309 36.695 1.00 24.22 C ANISOU 2152 CB LEU B 305 2920 2963 3318 35 -83 1 C ATOM 2153 CG LEU A 305 82.616 38.325 36.074 1.00 23.60 C ANISOU 2153 CG LEU B 305 2969 2994 3001 91 -75 58 C ATOM 2154 CD1 LEU A 305 82.569 39.213 34.841 1.00 22.75 C ANISOU 2154 CD1 LEU B 305 2807 2781 3055 34 -122 190 C ATOM 2155 CD2 LEU A 305 82.218 36.872 35.792 1.00 26.16 C ANISOU 2155 CD2 LEU B 305 3239 3146 3553 105 -109 239 C ATOM 2156 N ASP A 306 84.109 39.319 39.675 1.00 21.46 N ANISOU 2156 N ASP B 306 2599 2530 3023 -8 44 108 N ATOM 2157 CA ASP A 306 83.418 39.515 40.941 1.00 22.54 C ANISOU 2157 CA ASP B 306 2827 2819 2919 15 31 91 C ATOM 2158 C ASP A 306 83.448 40.940 41.462 1.00 21.43 C ANISOU 2158 C ASP B 306 2724 2657 2760 -64 168 104 C ATOM 2159 O ASP A 306 82.625 41.313 42.320 1.00 21.92 O ANISOU 2159 O ASP B 306 2823 2559 2944 -97 173 41 O ATOM 2160 CB ASP A 306 83.926 38.524 41.992 1.00 23.19 C ANISOU 2160 CB ASP B 306 2963 2922 2927 -41 -36 101 C ATOM 2161 CG ASP A 306 83.482 37.075 41.685 1.00 30.56 C ANISOU 2161 CG ASP B 306 3481 4018 4111 99 5 104 C ATOM 2162 OD1 ASP A 306 82.562 36.873 40.845 1.00 31.89 O ANISOU 2162 OD1 ASP B 306 3789 3712 4612 158 -89 153 O ATOM 2163 OD2 ASP A 306 84.075 36.144 42.256 1.00 33.14 O ANISOU 2163 OD2 ASP B 306 4359 3804 4428 -176 256 157 O ATOM 2164 N SER A 307 84.372 41.757 40.963 1.00 20.91 N ANISOU 2164 N SER B 307 2806 2361 2775 -136 44 92 N ATOM 2165 CA SER A 307 84.382 43.167 41.356 1.00 20.34 C ANISOU 2165 CA SER B 307 2672 2513 2543 -21 -18 121 C ATOM 2166 C SER A 307 83.063 43.876 40.997 1.00 19.12 C ANISOU 2166 C SER B 307 2543 2385 2338 -34 -20 77 C ATOM 2167 O SER A 307 82.677 44.821 41.651 1.00 18.72 O ANISOU 2167 O SER B 307 2896 2387 1830 23 172 31 O ATOM 2168 CB SER A 307 85.571 43.907 40.746 1.00 19.31 C ANISOU 2168 CB SER B 307 2633 2578 2127 92 -132 54 C ATOM 2169 OG SER A 307 85.480 44.003 39.328 1.00 22.80 O ANISOU 2169 OG SER B 307 2881 3406 2373 -119 300 65 O ATOM 2170 N ILE A 308 82.414 43.446 39.920 1.00 19.73 N ANISOU 2170 N ILE B 308 2689 2422 2386 -100 -46 184 N ATOM 2171 CA ILE A 308 81.125 44.035 39.490 1.00 20.10 C ANISOU 2171 CA ILE B 308 2626 2461 2548 -86 -2 141 C ATOM 2172 C ILE A 308 80.046 43.848 40.584 1.00 20.56 C ANISOU 2172 C ILE B 308 2547 2481 2781 -43 23 167 C ATOM 2173 O ILE A 308 79.172 44.699 40.756 1.00 19.88 O ANISOU 2173 O ILE B 308 2343 2487 2721 -95 69 312 O ATOM 2174 CB ILE A 308 80.705 43.478 38.042 1.00 18.98 C ANISOU 2174 CB ILE B 308 2466 2258 2487 -106 131 170 C ATOM 2175 CG1 ILE A 308 81.771 43.833 37.017 1.00 19.78 C ANISOU 2175 CG1 ILE B 308 2656 2221 2637 -215 -16 193 C ATOM 2176 CG2 ILE A 308 79.350 44.041 37.552 1.00 19.59 C ANISOU 2176 CG2 ILE B 308 2742 2432 2268 -79 -152 135 C ATOM 2177 CD1 ILE A 308 81.635 43.163 35.692 1.00 21.32 C ANISOU 2177 CD1 ILE B 308 2987 2543 2568 18 64 202 C ATOM 2178 N ARG A 309 80.138 42.763 41.359 1.00 20.08 N ANISOU 2178 N ARG B 309 2616 2470 2540 -210 134 194 N ATOM 2179 CA ARG A 309 79.165 42.421 42.392 1.00 21.14 C ANISOU 2179 CA ARG B 309 2693 2581 2757 -58 62 103 C ATOM 2180 C ARG A 309 79.054 43.399 43.584 1.00 20.29 C ANISOU 2180 C ARG B 309 2665 2538 2505 -148 149 137 C ATOM 2181 O ARG A 309 78.080 43.366 44.295 1.00 22.81 O ANISOU 2181 O ARG B 309 2917 2975 2772 -244 66 101 O ATOM 2182 CB ARG A 309 79.429 40.991 42.923 1.00 20.89 C ANISOU 2182 CB ARG B 309 2776 2476 2683 42 97 69 C ATOM 2183 CG ARG A 309 79.372 39.914 41.813 1.00 22.14 C ANISOU 2183 CG ARG B 309 2636 2893 2883 -22 26 83 C ATOM 2184 CD ARG A 309 79.419 38.469 42.365 1.00 22.92 C ANISOU 2184 CD ARG B 309 2785 3042 2878 68 16 296 C ATOM 2185 NE ARG A 309 79.627 37.524 41.265 1.00 27.52 N ANISOU 2185 NE ARG B 309 3169 3583 3704 -242 -103 193 N ATOM 2186 CZ ARG A 309 78.671 37.144 40.405 1.00 27.45 C ANISOU 2186 CZ ARG B 309 3646 3665 3116 -16 -158 79 C ATOM 2187 NH1 ARG A 309 77.417 37.618 40.501 1.00 21.42 N ANISOU 2187 NH1 ARG B 309 2932 3501 1705 17 -144 246 N ATOM 2188 NH2 ARG A 309 78.981 36.286 39.426 1.00 28.57 N ANISOU 2188 NH2 ARG B 309 3485 3615 3753 -258 -213 124 N ATOM 2189 N THR A 310 80.025 44.256 43.810 1.00 21.65 N ANISOU 2189 N THR B 310 2578 3018 2628 -172 90 117 N ATOM 2190 CA THR A 310 79.952 45.159 44.968 1.00 23.16 C ANISOU 2190 CA THR B 310 2833 3118 2846 -24 25 156 C ATOM 2191 C THR A 310 79.947 46.637 44.633 1.00 23.29 C ANISOU 2191 C THR B 310 2741 3202 2903 -31 -28 240 C ATOM 2192 O THR A 310 80.171 47.468 45.541 1.00 25.41 O ANISOU 2192 O THR B 310 2998 3658 2998 -149 -52 368 O ATOM 2193 CB THR A 310 81.079 44.915 46.000 1.00 24.23 C ANISOU 2193 CB THR B 310 2989 3145 3070 -5 -48 232 C ATOM 2194 OG1 THR A 310 82.334 44.927 45.349 1.00 22.63 O ANISOU 2194 OG1 THR B 310 3552 3176 1869 -4 -835 188 O ATOM 2195 CG2 THR A 310 80.878 43.585 46.753 1.00 28.21 C ANISOU 2195 CG2 THR B 310 3490 4050 3178 41 134 121 C ATOM 2196 N VAL A 311 79.682 46.978 43.377 1.00 21.33 N ANISOU 2196 N VAL B 311 2622 2854 2627 -63 -100 81 N ATOM 2197 CA VAL A 311 79.488 48.371 43.030 1.00 20.68 C ANISOU 2197 CA VAL B 311 2623 2675 2560 52 -1 144 C ATOM 2198 C VAL A 311 78.129 48.903 43.500 1.00 20.52 C ANISOU 2198 C VAL B 311 2647 2717 2430 58 67 95 C ATOM 2199 O VAL A 311 77.127 48.156 43.637 1.00 19.01 O ANISOU 2199 O VAL B 311 2373 2772 2074 105 407 338 O ATOM 2200 CB VAL A 311 79.631 48.657 41.536 1.00 19.14 C ANISOU 2200 CB VAL B 311 2444 2493 2334 33 -185 48 C ATOM 2201 CG1 VAL A 311 81.056 48.365 41.066 1.00 21.01 C ANISOU 2201 CG1 VAL B 311 2896 2494 2592 -75 -104 313 C ATOM 2202 CG2 VAL A 311 78.570 47.902 40.685 1.00 17.88 C ANISOU 2202 CG2 VAL B 311 2068 2403 2323 -46 129 80 C ATOM 2203 N ASP A 312 78.071 50.211 43.702 1.00 21.24 N ANISOU 2203 N ASP B 312 2736 2813 2519 66 21 33 N ATOM 2204 CA ASP A 312 76.792 50.853 43.989 1.00 20.42 C ANISOU 2204 CA ASP B 312 2610 2553 2595 20 -1 52 C ATOM 2205 C ASP A 312 76.064 51.072 42.686 1.00 18.76 C ANISOU 2205 C ASP B 312 2317 2315 2494 49 62 12 C ATOM 2206 O ASP A 312 76.643 50.897 41.620 1.00 18.66 O ANISOU 2206 O ASP B 312 2279 2314 2495 95 -312 238 O ATOM 2207 CB ASP A 312 76.974 52.166 44.733 1.00 22.58 C ANISOU 2207 CB ASP B 312 2875 2612 3092 -29 -57 42 C ATOM 2208 CG ASP A 312 75.708 52.575 45.522 1.00 24.13 C ANISOU 2208 CG ASP B 312 3222 3236 2707 -43 27 -223 C ATOM 2209 OD1 ASP A 312 74.720 51.769 45.628 1.00 28.87 O ANISOU 2209 OD1 ASP B 312 3792 3543 3631 68 -178 392 O ATOM 2210 OD2 ASP A 312 75.706 53.718 46.026 1.00 31.50 O ANISOU 2210 OD2 ASP B 312 3748 4324 3893 225 -161 -4 O ATOM 2211 N TYR A 313 74.788 51.456 42.764 1.00 20.04 N ANISOU 2211 N TYR B 313 2588 2541 2485 134 -12 -21 N ATOM 2212 CA TYR A 313 73.996 51.683 41.563 1.00 19.48 C ANISOU 2212 CA TYR B 313 2437 2393 2570 -51 105 9 C ATOM 2213 C TYR A 313 72.928 52.731 41.844 1.00 19.45 C ANISOU 2213 C TYR B 313 2475 2401 2514 -34 66 -59 C ATOM 2214 O TYR A 313 72.697 53.103 42.976 1.00 19.29 O ANISOU 2214 O TYR B 313 2608 2342 2378 -212 118 -92 O ATOM 2215 CB TYR A 313 73.345 50.387 41.078 1.00 19.44 C ANISOU 2215 CB TYR B 313 2585 2322 2478 -168 69 20 C ATOM 2216 CG TYR A 313 72.305 49.858 42.032 1.00 20.27 C ANISOU 2216 CG TYR B 313 2565 2446 2690 138 -35 166 C ATOM 2217 CD1 TYR A 313 70.968 50.226 41.893 1.00 19.94 C ANISOU 2217 CD1 TYR B 313 2756 2311 2508 -161 -291 -474 C ATOM 2218 CD2 TYR A 313 72.640 48.996 43.044 1.00 20.84 C ANISOU 2218 CD2 TYR B 313 2795 2685 2436 239 -98 146 C ATOM 2219 CE1 TYR A 313 70.028 49.755 42.736 1.00 22.21 C ANISOU 2219 CE1 TYR B 313 2620 2757 3060 162 241 -464 C ATOM 2220 CE2 TYR A 313 71.676 48.517 43.926 1.00 21.50 C ANISOU 2220 CE2 TYR B 313 2889 2512 2768 100 52 -72 C ATOM 2221 CZ TYR A 313 70.387 48.917 43.767 1.00 23.56 C ANISOU 2221 CZ TYR B 313 3353 2601 2996 8 218 -90 C ATOM 2222 OH TYR A 313 69.402 48.454 44.607 1.00 24.04 O ANISOU 2222 OH TYR B 313 3621 3492 2019 119 -22 -606 O ATOM 2223 N VAL A 314 72.353 53.261 40.774 1.00 17.50 N ANISOU 2223 N VAL B 314 2221 2046 2382 138 97 73 N ATOM 2224 CA VAL A 314 71.192 54.127 40.898 1.00 19.38 C ANISOU 2224 CA VAL B 314 2360 2346 2658 -39 77 -21 C ATOM 2225 C VAL A 314 70.066 53.614 39.978 1.00 19.14 C ANISOU 2225 C VAL B 314 2301 2398 2570 39 -159 -25 C ATOM 2226 O VAL A 314 70.308 52.901 38.982 1.00 19.16 O ANISOU 2226 O VAL B 314 2378 2381 2521 -1 -168 -265 O ATOM 2227 CB VAL A 314 71.481 55.609 40.503 1.00 19.59 C ANISOU 2227 CB VAL B 314 2381 2237 2823 157 -37 -72 C ATOM 2228 CG1 VAL A 314 72.492 56.227 41.403 1.00 23.65 C ANISOU 2228 CG1 VAL B 314 2889 2854 3242 -55 -87 43 C ATOM 2229 CG2 VAL A 314 71.913 55.682 39.044 1.00 19.33 C ANISOU 2229 CG2 VAL B 314 2225 2455 2663 68 -105 57 C ATOM 2230 N VAL A 315 68.841 54.025 40.310 1.00 19.10 N ANISOU 2230 N VAL B 315 2506 2348 2403 -5 -240 -83 N ATOM 2231 CA VAL A 315 67.663 53.750 39.522 1.00 20.21 C ANISOU 2231 CA VAL B 315 2520 2418 2739 -21 -96 -74 C ATOM 2232 C VAL A 315 67.261 55.103 38.917 1.00 20.47 C ANISOU 2232 C VAL B 315 2630 2339 2805 -16 -92 -64 C ATOM 2233 O VAL A 315 66.881 56.023 39.641 1.00 20.64 O ANISOU 2233 O VAL B 315 2543 2467 2829 -134 -264 18 O ATOM 2234 CB VAL A 315 66.502 53.146 40.400 1.00 20.45 C ANISOU 2234 CB VAL B 315 2499 2592 2678 -14 -18 -19 C ATOM 2235 CG1 VAL A 315 65.260 52.936 39.560 1.00 19.98 C ANISOU 2235 CG1 VAL B 315 2410 2629 2550 24 -158 -92 C ATOM 2236 CG2 VAL A 315 66.947 51.843 41.095 1.00 21.48 C ANISOU 2236 CG2 VAL B 315 2508 2885 2769 196 76 -79 C ATOM 2237 N VAL A 316 67.379 55.216 37.602 1.00 19.45 N ANISOU 2237 N VAL B 316 2613 2180 2595 0 -113 151 N ATOM 2238 CA VAL A 316 67.175 56.463 36.879 1.00 21.41 C ANISOU 2238 CA VAL B 316 2603 2473 3058 5 -58 77 C ATOM 2239 C VAL A 316 65.657 56.712 36.708 1.00 23.74 C ANISOU 2239 C VAL B 316 2805 2591 3623 25 16 -56 C ATOM 2240 O VAL A 316 64.839 55.775 36.810 1.00 23.10 O ANISOU 2240 O VAL B 316 2599 2299 3875 115 -36 -204 O ATOM 2241 CB VAL A 316 67.882 56.497 35.480 1.00 21.09 C ANISOU 2241 CB VAL B 316 2658 2382 2972 -35 37 136 C ATOM 2242 CG1 VAL A 316 69.410 56.242 35.561 1.00 18.26 C ANISOU 2242 CG1 VAL B 316 2426 2185 2327 -74 329 -7 C ATOM 2243 CG2 VAL A 316 67.293 55.529 34.495 1.00 22.10 C ANISOU 2243 CG2 VAL B 316 2799 2264 3332 176 104 77 C ATOM 2244 N LYS A 317 65.304 57.969 36.442 1.00 23.96 N ANISOU 2244 N LYS B 317 2758 2807 3536 29 28 -2 N ATOM 2245 CA LYS A 317 63.894 58.382 36.353 1.00 25.33 C ANISOU 2245 CA LYS B 317 3038 2966 3619 -34 25 39 C ATOM 2246 C LYS A 317 63.337 58.010 34.982 1.00 26.84 C ANISOU 2246 C LYS B 317 3288 3217 3692 -48 85 233 C ATOM 2247 O LYS A 317 62.503 57.099 34.930 1.00 29.82 O ANISOU 2247 O LYS B 317 3458 3821 4049 38 186 524 O ATOM 2248 CB LYS A 317 63.709 59.855 36.687 1.00 24.03 C ANISOU 2248 CB LYS B 317 2997 2835 3297 137 46 52 C ATOM 2249 CG LYS A 317 62.238 60.302 36.844 1.00 25.02 C ANISOU 2249 CG LYS B 317 2843 2967 3694 -107 -52 46 C ATOM 2250 CD LYS A 317 62.136 61.717 37.401 1.00 25.21 C ANISOU 2250 CD LYS B 317 3100 3072 3404 -40 8 4 C ATOM 2251 CE LYS A 317 60.745 62.353 37.208 1.00 23.87 C ANISOU 2251 CE LYS B 317 2998 2902 3167 116 -90 55 C ATOM 2252 NZ LYS A 317 60.326 62.451 35.775 1.00 19.13 N ANISOU 2252 NZ LYS B 317 2649 1954 2664 167 177 -181 N ATOM 2253 N ASN A 318 63.788 58.645 33.895 1.00 29.50 N ANISOU 2253 N ASN B 318 3642 3529 4034 0 -26 42 N ATOM 2254 CA ASN A 318 63.418 58.239 32.512 1.00 33.18 C ANISOU 2254 CA ASN B 318 4224 4102 4280 66 -5 82 C ATOM 2255 C ASN A 318 64.427 57.302 31.884 1.00 36.43 C ANISOU 2255 C ASN B 318 4629 4472 4738 2 -70 3 C ATOM 2256 O ASN A 318 65.573 57.683 31.660 1.00 38.31 O ANISOU 2256 O ASN B 318 4761 4790 5004 85 -49 -36 O ATOM 2257 CB ASN A 318 63.354 59.427 31.553 1.00 34.90 C ANISOU 2257 CB ASN B 318 4460 4244 4555 53 -100 113 C ATOM 2258 CG ASN A 318 62.229 60.337 31.845 1.00 37.62 C ANISOU 2258 CG ASN B 318 4681 4337 5273 -39 -34 12 C ATOM 2259 OD1 ASN A 318 61.086 59.894 31.955 1.00 31.14 O ANISOU 2259 OD1 ASN B 318 3782 4007 4043 160 -96 103 O ATOM 2260 ND2 ASN A 318 62.527 61.638 31.957 1.00 41.12 N ANISOU 2260 ND2 ASN B 318 4714 5051 5856 87 -160 116 N ATOM 2261 N SER A 319 63.992 56.112 31.515 1.00 37.87 N ANISOU 2261 N SER B 319 4672 4713 5004 28 -33 -31 N ATOM 2262 CA SER A 319 64.916 55.119 30.993 1.00 40.78 C ANISOU 2262 CA SER B 319 5034 5112 5345 -11 -34 -80 C ATOM 2263 C SER A 319 64.680 54.724 29.531 1.00 43.53 C ANISOU 2263 C SER B 319 5508 5529 5502 -2 -28 -35 C ATOM 2264 O SER A 319 65.495 54.021 28.965 1.00 44.29 O ANISOU 2264 O SER B 319 5687 5560 5580 -11 18 -74 O ATOM 2265 CB SER A 319 64.870 53.893 31.897 1.00 40.83 C ANISOU 2265 CB SER B 319 5093 5135 5285 -59 -18 -44 C ATOM 2266 OG SER A 319 63.555 53.687 32.371 1.00 40.10 O ANISOU 2266 OG SER B 319 4753 5104 5378 81 106 -168 O ATOM 2267 N ILE A 320 63.584 55.185 28.926 1.00 46.77 N ANISOU 2267 N ILE B 320 5915 5928 5927 44 31 30 N ATOM 2268 CA ILE A 320 63.202 54.770 27.554 1.00 48.41 C ANISOU 2268 CA ILE B 320 6166 6159 6068 35 -1 63 C ATOM 2269 C ILE A 320 63.543 55.828 26.489 1.00 50.20 C ANISOU 2269 C ILE B 320 6373 6395 6306 24 77 41 C ATOM 2270 O ILE A 320 62.683 56.597 26.041 1.00 51.72 O ANISOU 2270 O ILE B 320 6628 6518 6504 -62 87 90 O ATOM 2271 CB ILE A 320 61.689 54.366 27.455 1.00 50.08 C ANISOU 2271 CB ILE B 320 6404 6260 6363 65 -11 21 C ATOM 2272 CG1 ILE A 320 60.780 55.413 28.115 1.00 50.82 C ANISOU 2272 CG1 ILE B 320 6423 6340 6545 -84 20 81 C ATOM 2273 CG2 ILE A 320 61.466 52.984 28.112 1.00 51.88 C ANISOU 2273 CG2 ILE B 320 6482 6614 6615 -25 21 39 C ATOM 2274 CD1 ILE A 320 59.294 55.316 27.720 1.00 51.00 C ANISOU 2274 CD1 ILE B 320 6518 6385 6474 28 -13 -4 C TER 2275 ILE B 320 ATOM 1 N ASN A 3 55.475 65.804 44.218 1.00 41.21 N ANISOU 1 N ASN C 3 5286 5280 5092 -22 -74 -43 N ATOM 2 CA ASN A 3 54.003 66.085 44.268 1.00 39.21 C ANISOU 2 CA ASN C 3 5022 5109 4767 -38 -65 -41 C ATOM 3 C ASN A 3 53.498 66.952 43.082 1.00 37.49 C ANISOU 3 C ASN C 3 4795 4861 4587 -64 -23 -15 C ATOM 4 O ASN A 3 52.417 67.550 43.141 1.00 37.44 O ANISOU 4 O ASN C 3 4919 4686 4619 71 60 -72 O ATOM 5 CB ASN A 3 53.627 66.717 45.626 1.00 41.38 C ANISOU 5 CB ASN C 3 5312 5433 4974 -42 -12 75 C ATOM 6 CG ASN A 3 54.393 68.006 45.921 1.00 48.08 C ANISOU 6 CG ASN C 3 5930 6164 6173 213 47 -17 C ATOM 7 OD1 ASN A 3 55.613 68.095 45.706 1.00 52.26 O ANISOU 7 OD1 ASN C 3 6786 6322 6747 31 -14 110 O ATOM 8 ND2 ASN A 3 53.675 69.011 46.439 1.00 52.95 N ANISOU 8 ND2 ASN C 3 6357 6739 7022 -38 47 164 N ATOM 9 N VAL A 4 54.273 66.963 41.998 1.00 35.31 N ANISOU 9 N VAL C 4 4388 4697 4331 -67 -63 -91 N ATOM 10 CA VAL A 4 54.008 67.826 40.843 1.00 31.71 C ANISOU 10 CA VAL C 4 4020 4072 3955 -44 105 -190 C ATOM 11 C VAL A 4 53.476 66.957 39.706 1.00 27.77 C ANISOU 11 C VAL C 4 3483 3445 3623 -94 -10 -222 C ATOM 12 O VAL A 4 53.863 65.797 39.543 1.00 25.08 O ANISOU 12 O VAL C 4 3168 3089 3271 -77 -27 -672 O ATOM 13 CB VAL A 4 55.238 68.771 40.503 1.00 32.76 C ANISOU 13 CB VAL C 4 4359 4053 4035 -70 -15 -94 C ATOM 14 CG1 VAL A 4 56.465 68.362 41.299 1.00 38.88 C ANISOU 14 CG1 VAL C 4 5148 4766 4858 -153 -76 -102 C ATOM 15 CG2 VAL A 4 55.599 68.820 39.052 1.00 32.78 C ANISOU 15 CG2 VAL C 4 3984 4240 4228 -90 -120 -128 C ATOM 16 N PHE A 5 52.550 67.526 38.956 1.00 24.57 N ANISOU 16 N PHE C 5 3087 3042 3203 -127 -68 -48 N ATOM 17 CA PHE A 5 51.924 66.851 37.858 1.00 22.77 C ANISOU 17 CA PHE C 5 2768 2855 3026 -125 44 21 C ATOM 18 C PHE A 5 51.404 67.897 36.866 1.00 20.36 C ANISOU 18 C PHE C 5 2512 2661 2561 -18 46 0 C ATOM 19 O PHE A 5 51.501 69.104 37.117 1.00 18.18 O ANISOU 19 O PHE C 5 2408 2268 2229 101 134 -170 O ATOM 20 CB PHE A 5 50.762 65.991 38.350 1.00 22.13 C ANISOU 20 CB PHE C 5 2589 2999 2820 -103 -12 112 C ATOM 21 CG PHE A 5 49.742 66.748 39.158 1.00 21.63 C ANISOU 21 CG PHE C 5 2626 2817 2774 174 -255 210 C ATOM 22 CD1 PHE A 5 48.778 67.564 38.566 1.00 20.25 C ANISOU 22 CD1 PHE C 5 2787 2218 2688 150 -156 217 C ATOM 23 CD2 PHE A 5 49.730 66.618 40.505 1.00 22.10 C ANISOU 23 CD2 PHE C 5 3357 2882 2158 -26 23 -400 C ATOM 24 CE1 PHE A 5 47.860 68.292 39.352 1.00 20.23 C ANISOU 24 CE1 PHE C 5 2597 2626 2463 162 -202 226 C ATOM 25 CE2 PHE A 5 48.818 67.323 41.294 1.00 25.24 C ANISOU 25 CE2 PHE C 5 3557 3021 3011 -429 -89 -134 C ATOM 26 CZ PHE A 5 47.879 68.157 40.708 1.00 21.93 C ANISOU 26 CZ PHE C 5 2850 2780 2698 -256 -61 -169 C ATOM 27 N ASP A 6 50.824 67.421 35.770 1.00 19.30 N ANISOU 27 N ASP C 6 2270 2422 2640 -133 251 60 N ATOM 28 CA ASP A 6 50.174 68.267 34.764 1.00 19.59 C ANISOU 28 CA ASP C 6 2476 2422 2542 -10 73 -2 C ATOM 29 C ASP A 6 48.835 67.653 34.335 1.00 18.64 C ANISOU 29 C ASP C 6 2253 2408 2419 -68 71 38 C ATOM 30 O ASP A 6 48.438 66.584 34.812 1.00 16.78 O ANISOU 30 O ASP C 6 2297 2168 1908 -309 -195 315 O ATOM 31 CB ASP A 6 51.077 68.469 33.541 1.00 19.47 C ANISOU 31 CB ASP C 6 2488 2443 2466 -69 100 -155 C ATOM 32 CG ASP A 6 50.937 69.861 32.919 1.00 18.97 C ANISOU 32 CG ASP C 6 2318 2317 2572 -79 160 6 C ATOM 33 OD1 ASP A 6 49.958 70.593 33.228 1.00 15.50 O ANISOU 33 OD1 ASP C 6 1605 2445 1837 -152 -248 108 O ATOM 34 OD2 ASP A 6 51.786 70.225 32.089 1.00 24.72 O ANISOU 34 OD2 ASP C 6 2958 2981 3452 -287 -189 221 O ATOM 35 N TYR A 7 48.166 68.348 33.414 1.00 18.62 N ANISOU 35 N TYR C 7 2237 2445 2391 94 34 -49 N ATOM 36 CA TYR A 7 46.822 68.009 32.921 1.00 18.78 C ANISOU 36 CA TYR C 7 2396 2341 2399 28 -17 -38 C ATOM 37 C TYR A 7 46.656 66.535 32.581 1.00 17.77 C ANISOU 37 C TYR C 7 2258 2182 2310 24 -46 -139 C ATOM 38 O TYR A 7 45.687 65.901 33.029 1.00 19.79 O ANISOU 38 O TYR C 7 2403 2263 2852 65 -178 -296 O ATOM 39 CB TYR A 7 46.474 68.886 31.710 1.00 19.13 C ANISOU 39 CB TYR C 7 2368 2343 2555 35 -45 -74 C ATOM 40 CG TYR A 7 46.149 70.311 32.126 1.00 18.94 C ANISOU 40 CG TYR C 7 2359 2094 2740 0 -50 52 C ATOM 41 CD1 TYR A 7 44.930 70.622 32.750 1.00 18.84 C ANISOU 41 CD1 TYR C 7 2132 2175 2848 63 7 173 C ATOM 42 CD2 TYR A 7 47.068 71.340 31.945 1.00 17.89 C ANISOU 42 CD2 TYR C 7 2141 2198 2456 55 -10 41 C ATOM 43 CE1 TYR A 7 44.646 71.905 33.156 1.00 18.35 C ANISOU 43 CE1 TYR C 7 2299 2070 2602 27 -86 38 C ATOM 44 CE2 TYR A 7 46.774 72.622 32.328 1.00 20.83 C ANISOU 44 CE2 TYR C 7 2278 2412 3222 -31 32 60 C ATOM 45 CZ TYR A 7 45.568 72.909 32.946 1.00 21.07 C ANISOU 45 CZ TYR C 7 2320 2505 3178 59 -94 165 C ATOM 46 OH TYR A 7 45.273 74.208 33.359 1.00 20.80 O ANISOU 46 OH TYR C 7 2448 2019 3434 147 126 26 O ATOM 47 N GLU A 8 47.599 65.997 31.815 1.00 18.34 N ANISOU 47 N GLU C 8 2254 2200 2511 109 18 -93 N ATOM 48 CA GLU A 8 47.524 64.608 31.331 1.00 18.39 C ANISOU 48 CA GLU C 8 2407 2216 2362 -29 85 76 C ATOM 49 C GLU A 8 47.592 63.543 32.436 1.00 19.19 C ANISOU 49 C GLU C 8 2425 2353 2511 9 140 35 C ATOM 50 O GLU A 8 47.184 62.380 32.219 1.00 21.48 O ANISOU 50 O GLU C 8 2465 2900 2794 237 -22 169 O ATOM 51 CB GLU A 8 48.575 64.383 30.197 1.00 19.09 C ANISOU 51 CB GLU C 8 2484 2424 2342 3 -3 143 C ATOM 52 CG GLU A 8 50.015 64.210 30.650 1.00 16.06 C ANISOU 52 CG GLU C 8 2637 2167 1296 -61 10 356 C ATOM 53 CD GLU A 8 50.811 65.499 30.756 1.00 25.03 C ANISOU 53 CD GLU C 8 3167 3034 3309 98 -42 138 C ATOM 54 OE1 GLU A 8 50.184 66.589 30.827 1.00 27.68 O ANISOU 54 OE1 GLU C 8 3264 3476 3775 -64 -451 425 O ATOM 55 OE2 GLU A 8 52.083 65.414 30.792 1.00 21.93 O ANISOU 55 OE2 GLU C 8 3517 2913 1902 -271 -378 -61 O ATOM 56 N ASP A 9 48.069 63.926 33.631 1.00 17.03 N ANISOU 56 N ASP C 9 2241 2050 2177 0 98 203 N ATOM 57 CA ASP A 9 48.206 63.007 34.720 1.00 17.43 C ANISOU 57 CA ASP C 9 2173 2096 2353 -72 61 37 C ATOM 58 C ASP A 9 46.923 62.913 35.566 1.00 17.35 C ANISOU 58 C ASP C 9 2150 2205 2236 3 -19 95 C ATOM 59 O ASP A 9 46.799 62.024 36.395 1.00 18.15 O ANISOU 59 O ASP C 9 1974 2277 2643 -45 -175 198 O ATOM 60 CB ASP A 9 49.330 63.475 35.638 1.00 17.67 C ANISOU 60 CB ASP C 9 2021 2311 2379 -60 9 -74 C ATOM 61 CG ASP A 9 50.654 63.590 34.909 1.00 21.03 C ANISOU 61 CG ASP C 9 2673 2401 2915 -155 171 9 C ATOM 62 OD1 ASP A 9 51.039 62.578 34.256 1.00 18.68 O ANISOU 62 OD1 ASP C 9 2645 2353 2100 -173 360 10 O ATOM 63 OD2 ASP A 9 51.287 64.676 34.988 1.00 21.89 O ANISOU 63 OD2 ASP C 9 2519 2832 2964 -178 76 142 O ATOM 64 N ILE A 10 45.983 63.830 35.377 1.00 16.30 N ANISOU 64 N ILE C 10 2088 2006 2098 7 25 103 N ATOM 65 CA ILE A 10 44.806 63.893 36.257 1.00 17.32 C ANISOU 65 CA ILE C 10 2205 2105 2269 -49 64 37 C ATOM 66 C ILE A 10 43.558 63.269 35.640 1.00 16.31 C ANISOU 66 C ILE C 10 2148 1905 2142 -49 28 69 C ATOM 67 O ILE A 10 43.234 63.529 34.472 1.00 17.75 O ANISOU 67 O ILE C 10 2239 2158 2347 9 10 111 O ATOM 68 CB ILE A 10 44.494 65.364 36.666 1.00 17.66 C ANISOU 68 CB ILE C 10 2154 2240 2314 -79 -11 7 C ATOM 69 CG1 ILE A 10 45.627 65.969 37.501 1.00 18.85 C ANISOU 69 CG1 ILE C 10 2158 2081 2924 -174 223 0 C ATOM 70 CG2 ILE A 10 43.165 65.441 37.488 1.00 18.78 C ANISOU 70 CG2 ILE C 10 2418 2159 2557 -78 209 32 C ATOM 71 CD1 ILE A 10 45.929 65.214 38.746 1.00 22.83 C ANISOU 71 CD1 ILE C 10 2409 3125 3138 62 190 -58 C ATOM 72 N GLN A 11 42.857 62.451 36.429 1.00 16.01 N ANISOU 72 N GLN C 11 2026 2055 2002 20 -119 -105 N ATOM 73 CA GLN A 11 41.462 62.071 36.111 1.00 17.07 C ANISOU 73 CA GLN C 11 2182 2101 2201 -10 -44 -25 C ATOM 74 C GLN A 11 40.548 62.477 37.217 1.00 15.69 C ANISOU 74 C GLN C 11 1957 1956 2045 -6 -48 -76 C ATOM 75 O GLN A 11 40.835 62.226 38.397 1.00 15.79 O ANISOU 75 O GLN C 11 2351 1772 1877 -11 -311 75 O ATOM 76 CB GLN A 11 41.300 60.556 35.891 1.00 18.13 C ANISOU 76 CB GLN C 11 2276 2187 2425 -15 -148 -66 C ATOM 77 CG GLN A 11 41.911 60.031 34.624 1.00 21.51 C ANISOU 77 CG GLN C 11 2640 2874 2658 140 335 -2 C ATOM 78 CD GLN A 11 41.117 60.421 33.375 1.00 30.51 C ANISOU 78 CD GLN C 11 4162 3696 3734 -3 -204 -214 C ATOM 79 OE1 GLN A 11 39.920 60.216 33.294 1.00 34.17 O ANISOU 79 OE1 GLN C 11 5087 3813 4082 368 -249 99 O ATOM 80 NE2 GLN A 11 41.802 60.999 32.401 1.00 33.86 N ANISOU 80 NE2 GLN C 11 4510 4389 3966 56 -20 82 N ATOM 81 N LEU A 12 39.453 63.140 36.869 1.00 15.16 N ANISOU 81 N LEU C 12 1907 1836 2014 103 -77 -135 N ATOM 82 CA LEU A 12 38.424 63.476 37.868 1.00 15.88 C ANISOU 82 CA LEU C 12 1964 1998 2072 -38 16 -54 C ATOM 83 C LEU A 12 37.440 62.300 38.052 1.00 15.72 C ANISOU 83 C LEU C 12 1995 1917 2060 -4 -17 -18 C ATOM 84 O LEU A 12 37.053 61.598 37.079 1.00 17.40 O ANISOU 84 O LEU C 12 2027 2125 2457 256 -17 217 O ATOM 85 CB LEU A 12 37.660 64.766 37.450 1.00 16.27 C ANISOU 85 CB LEU C 12 1845 2093 2245 -86 9 67 C ATOM 86 CG LEU A 12 38.571 65.964 37.077 1.00 17.96 C ANISOU 86 CG LEU C 12 1992 2517 2313 24 -57 -44 C ATOM 87 CD1 LEU A 12 37.778 67.146 36.569 1.00 19.70 C ANISOU 87 CD1 LEU C 12 2160 2288 3034 -100 -77 -21 C ATOM 88 CD2 LEU A 12 39.450 66.377 38.249 1.00 16.81 C ANISOU 88 CD2 LEU C 12 1617 2300 2471 213 -220 35 C ATOM 89 N ILE A 13 37.008 62.117 39.279 1.00 17.01 N ANISOU 89 N ILE C 13 2170 2036 2253 42 90 -119 N ATOM 90 CA ILE A 13 36.189 61.017 39.665 1.00 17.96 C ANISOU 90 CA ILE C 13 2247 2176 2397 28 34 -19 C ATOM 91 C ILE A 13 34.707 61.423 39.675 1.00 19.00 C ANISOU 91 C ILE C 13 2296 2265 2655 -67 39 83 C ATOM 92 O ILE A 13 34.313 62.418 40.313 1.00 20.30 O ANISOU 92 O ILE C 13 2468 2507 2735 107 95 415 O ATOM 93 CB ILE A 13 36.590 60.469 41.023 1.00 19.01 C ANISOU 93 CB ILE C 13 2321 2167 2732 -47 -148 -53 C ATOM 94 CG1 ILE A 13 38.013 59.886 40.912 1.00 19.59 C ANISOU 94 CG1 ILE C 13 2677 2123 2641 -28 -73 276 C ATOM 95 CG2 ILE A 13 35.592 59.364 41.508 1.00 19.75 C ANISOU 95 CG2 ILE C 13 2556 2284 2660 -17 -98 -98 C ATOM 96 CD1 ILE A 13 38.618 59.532 42.211 1.00 20.35 C ANISOU 96 CD1 ILE C 13 2821 2328 2581 -101 -129 9 C ATOM 97 N PRO A 14 33.887 60.644 38.966 1.00 18.60 N ANISOU 97 N PRO C 14 2394 2301 2372 -126 -8 -100 N ATOM 98 CA PRO A 14 32.452 60.935 38.906 1.00 18.78 C ANISOU 98 CA PRO C 14 2380 2333 2422 42 -29 8 C ATOM 99 C PRO A 14 31.721 60.823 40.252 1.00 19.36 C ANISOU 99 C PRO C 14 2558 2368 2428 -6 19 93 C ATOM 100 O PRO A 14 32.072 59.991 41.114 1.00 18.63 O ANISOU 100 O PRO C 14 2764 2164 2149 -159 -82 295 O ATOM 101 CB PRO A 14 31.929 59.919 37.892 1.00 18.93 C ANISOU 101 CB PRO C 14 2451 2344 2397 89 76 -73 C ATOM 102 CG PRO A 14 33.126 59.492 37.104 1.00 20.88 C ANISOU 102 CG PRO C 14 2563 2543 2828 192 166 -181 C ATOM 103 CD PRO A 14 34.218 59.474 38.148 1.00 20.71 C ANISOU 103 CD PRO C 14 2535 2627 2705 -268 -21 -117 C ATOM 104 N ALA A 15 30.700 61.647 40.394 1.00 18.88 N ANISOU 104 N ALA C 15 2455 2342 2377 -3 103 174 N ATOM 105 CA ALA A 15 29.799 61.605 41.554 1.00 20.19 C ANISOU 105 CA ALA C 15 2668 2505 2495 24 19 67 C ATOM 106 C ALA A 15 28.366 61.314 41.048 1.00 20.31 C ANISOU 106 C ALA C 15 2749 2440 2527 89 -51 54 C ATOM 107 O ALA A 15 28.108 61.402 39.831 1.00 18.57 O ANISOU 107 O ALA C 15 2628 2176 2248 263 163 -159 O ATOM 108 CB ALA A 15 29.861 62.914 42.228 1.00 21.80 C ANISOU 108 CB ALA C 15 2908 2691 2683 116 50 225 C ATOM 109 N LYS A 16 27.438 60.988 41.953 1.00 20.94 N ANISOU 109 N LYS C 16 2762 2603 2590 -39 61 60 N ATOM 110 CA LYS A 16 26.067 60.637 41.532 1.00 21.33 C ANISOU 110 CA LYS C 16 2758 2587 2759 31 119 69 C ATOM 111 C LYS A 16 25.460 61.706 40.620 1.00 20.26 C ANISOU 111 C LYS C 16 2647 2284 2766 145 60 231 C ATOM 112 O LYS A 16 25.409 62.890 40.988 1.00 19.71 O ANISOU 112 O LYS C 16 2481 2384 2622 -140 13 224 O ATOM 113 CB LYS A 16 25.152 60.393 42.737 1.00 22.97 C ANISOU 113 CB LYS C 16 2860 2761 3104 -19 101 -44 C ATOM 114 CG LYS A 16 23.807 59.782 42.379 1.00 23.21 C ANISOU 114 CG LYS C 16 3002 2769 3046 -52 175 16 C ATOM 115 CD LYS A 16 22.979 59.695 43.612 1.00 24.98 C ANISOU 115 CD LYS C 16 3355 2990 3147 141 69 95 C ATOM 116 CE LYS A 16 21.773 58.867 43.458 1.00 29.28 C ANISOU 116 CE LYS C 16 3901 3535 3689 249 -19 -72 C ATOM 117 NZ LYS A 16 21.067 58.804 44.756 1.00 29.87 N ANISOU 117 NZ LYS C 16 4373 3184 3791 -171 101 160 N ATOM 118 N CYS A 17 24.985 61.289 39.443 1.00 20.71 N ANISOU 118 N CYS C 17 2673 2494 2701 95 112 435 N ATOM 119 CA CYS A 17 24.348 62.188 38.491 1.00 22.28 C ANISOU 119 CA CYS C 17 2865 2612 2988 0 143 146 C ATOM 120 C CYS A 17 22.971 62.566 38.979 1.00 22.34 C ANISOU 120 C CYS C 17 2884 2614 2990 7 147 174 C ATOM 121 O CYS A 17 22.176 61.680 39.325 1.00 21.11 O ANISOU 121 O CYS C 17 2674 2357 2990 -111 352 274 O ATOM 122 CB CYS A 17 24.204 61.543 37.123 1.00 21.90 C ANISOU 122 CB CYS C 17 3110 2435 2774 7 141 257 C ATOM 123 SG CYS A 17 23.634 62.606 35.787 1.00 25.86 S ANISOU 123 SG CYS C 17 3269 3112 3442 -128 -53 366 S ATOM 124 N ILE A 18 22.700 63.870 38.979 1.00 23.31 N ANISOU 124 N ILE C 18 2704 2705 3446 26 191 107 N ATOM 125 CA ILE A 18 21.414 64.436 39.495 1.00 24.28 C ANISOU 125 CA ILE C 18 3038 2826 3360 -15 147 168 C ATOM 126 C ILE A 18 20.611 65.192 38.458 1.00 24.56 C ANISOU 126 C ILE C 18 3030 2978 3323 -10 243 62 C ATOM 127 O ILE A 18 19.529 65.720 38.775 1.00 27.45 O ANISOU 127 O ILE C 18 3626 3112 3691 13 287 -85 O ATOM 128 CB ILE A 18 21.600 65.381 40.730 1.00 23.30 C ANISOU 128 CB ILE C 18 2966 2803 3084 -77 67 128 C ATOM 129 CG1 ILE A 18 22.383 66.655 40.337 1.00 21.87 C ANISOU 129 CG1 ILE C 18 2944 2403 2961 -104 139 139 C ATOM 130 CG2 ILE A 18 22.170 64.644 41.931 1.00 21.14 C ANISOU 130 CG2 ILE C 18 2663 2341 3028 -172 284 258 C ATOM 131 CD1 ILE A 18 22.645 67.610 41.477 1.00 25.35 C ANISOU 131 CD1 ILE C 18 3430 2647 3554 -35 277 135 C ATOM 132 N VAL A 19 21.089 65.227 37.219 1.00 24.48 N ANISOU 132 N VAL C 19 3050 2865 3385 97 48 124 N ATOM 133 CA VAL A 19 20.368 65.858 36.140 1.00 27.84 C ANISOU 133 CA VAL C 19 3537 3369 3672 -27 33 59 C ATOM 134 C VAL A 19 19.829 64.789 35.184 1.00 29.27 C ANISOU 134 C VAL C 19 3664 3610 3843 -11 112 27 C ATOM 135 O VAL A 19 20.393 63.693 35.053 1.00 28.29 O ANISOU 135 O VAL C 19 3578 3433 3737 2 188 23 O ATOM 136 CB VAL A 19 21.218 66.910 35.343 1.00 27.25 C ANISOU 136 CB VAL C 19 3429 3360 3563 -48 -21 -76 C ATOM 137 CG1 VAL A 19 21.680 68.043 36.260 1.00 26.70 C ANISOU 137 CG1 VAL C 19 3178 3340 3625 -19 -72 9 C ATOM 138 CG2 VAL A 19 22.412 66.250 34.622 1.00 25.28 C ANISOU 138 CG2 VAL C 19 3436 3265 2901 56 -54 -58 C ATOM 139 N ASN A 20 18.720 65.117 34.537 1.00 32.14 N ANISOU 139 N ASN C 20 4061 3979 4172 -58 29 -63 N ATOM 140 CA ASN A 20 18.129 64.256 33.520 1.00 33.79 C ANISOU 140 CA ASN C 20 4277 4248 4312 7 51 -147 C ATOM 141 C ASN A 20 18.668 64.554 32.157 1.00 34.71 C ANISOU 141 C ASN C 20 4391 4377 4421 4 -25 -116 C ATOM 142 O ASN A 20 18.489 63.757 31.241 1.00 34.40 O ANISOU 142 O ASN C 20 4438 4485 4145 227 -127 -446 O ATOM 143 CB ASN A 20 16.612 64.416 33.483 1.00 35.79 C ANISOU 143 CB ASN C 20 4544 4431 4624 31 4 -110 C ATOM 144 CG ASN A 20 15.923 63.616 34.539 1.00 41.65 C ANISOU 144 CG ASN C 20 5284 5247 5293 162 -167 48 C ATOM 145 OD1 ASN A 20 16.332 62.493 34.858 1.00 45.25 O ANISOU 145 OD1 ASN C 20 5308 5599 6284 30 -123 -8 O ATOM 146 ND2 ASN A 20 14.852 64.179 35.090 1.00 46.19 N ANISOU 146 ND2 ASN C 20 5860 5755 5936 -20 132 171 N ATOM 147 N SER A 21 19.334 65.693 32.017 1.00 35.71 N ANISOU 147 N SER C 21 4493 4461 4613 71 -7 -168 N ATOM 148 CA SER A 21 19.918 66.085 30.747 1.00 36.77 C ANISOU 148 CA SER C 21 4702 4585 4681 85 -9 -110 C ATOM 149 C SER A 21 21.010 67.123 30.942 1.00 36.55 C ANISOU 149 C SER C 21 4647 4478 4761 135 18 -120 C ATOM 150 O SER A 21 20.821 68.058 31.701 1.00 36.04 O ANISOU 150 O SER C 21 4500 4284 4907 262 156 -201 O ATOM 151 CB SER A 21 18.860 66.745 29.881 1.00 38.08 C ANISOU 151 CB SER C 21 4972 4734 4759 70 -24 -195 C ATOM 152 OG SER A 21 19.432 67.132 28.653 1.00 41.52 O ANISOU 152 OG SER C 21 5604 5063 5105 138 -237 75 O ATOM 153 N ARG A 22 22.110 66.962 30.219 1.00 37.97 N ANISOU 153 N ARG C 22 4826 4764 4835 142 26 4 N ATOM 154 CA ARG A 22 23.192 67.977 30.131 1.00 38.56 C ANISOU 154 CA ARG C 22 4901 4835 4914 128 20 -16 C ATOM 155 C ARG A 22 22.695 69.391 30.071 1.00 38.28 C ANISOU 155 C ARG C 22 4899 4835 4811 95 -95 -98 C ATOM 156 O ARG A 22 23.312 70.309 30.620 1.00 37.44 O ANISOU 156 O ARG C 22 4886 4732 4607 254 -271 -237 O ATOM 157 CB ARG A 22 23.953 67.821 28.825 1.00 38.40 C ANISOU 157 CB ARG C 22 4874 4921 4795 151 6 -14 C ATOM 158 CG ARG A 22 25.045 66.851 28.851 1.00 39.58 C ANISOU 158 CG ARG C 22 5136 4886 5014 86 46 -5 C ATOM 159 CD ARG A 22 26.066 67.202 27.816 1.00 40.57 C ANISOU 159 CD ARG C 22 5167 5136 5111 54 -33 54 C ATOM 160 NE ARG A 22 25.495 67.450 26.504 1.00 41.19 N ANISOU 160 NE ARG C 22 5484 5136 5028 86 5 -165 N ATOM 161 CZ ARG A 22 26.121 67.168 25.361 1.00 44.06 C ANISOU 161 CZ ARG C 22 5654 5517 5567 -82 4 56 C ATOM 162 NH1 ARG A 22 27.339 66.642 25.370 1.00 45.31 N ANISOU 162 NH1 ARG C 22 5748 5531 5936 -5 12 -76 N ATOM 163 NH2 ARG A 22 25.530 67.415 24.191 1.00 43.34 N ANISOU 163 NH2 ARG C 22 5568 5589 5307 -72 176 -142 N ATOM 164 N SER A 23 21.605 69.562 29.322 1.00 38.41 N ANISOU 164 N SER C 23 5013 4748 4833 117 -64 -144 N ATOM 165 CA SER A 23 20.971 70.855 29.137 1.00 38.28 C ANISOU 165 CA SER C 23 4946 4747 4851 62 0 -113 C ATOM 166 C SER A 23 20.585 71.542 30.426 1.00 37.10 C ANISOU 166 C SER C 23 4754 4440 4903 9 -16 -117 C ATOM 167 O SER A 23 20.471 72.758 30.435 1.00 38.76 O ANISOU 167 O SER C 23 4921 4559 5245 -51 -145 -329 O ATOM 168 CB SER A 23 19.742 70.700 28.236 1.00 40.30 C ANISOU 168 CB SER C 23 5254 4943 5112 -43 4 -145 C ATOM 169 OG SER A 23 20.127 70.051 27.028 1.00 44.65 O ANISOU 169 OG SER C 23 5860 5970 5135 -107 -7 -90 O ATOM 170 N GLU A 24 20.418 70.779 31.507 1.00 35.13 N ANISOU 170 N GLU C 24 4422 4166 4759 -10 -34 -144 N ATOM 171 CA GLU A 24 20.157 71.333 32.820 1.00 34.55 C ANISOU 171 CA GLU C 24 4349 4114 4663 -1 -45 -103 C ATOM 172 C GLU A 24 21.364 72.018 33.458 1.00 33.16 C ANISOU 172 C GLU C 24 4152 3920 4527 -8 -28 -14 C ATOM 173 O GLU A 24 21.195 72.714 34.439 1.00 32.76 O ANISOU 173 O GLU C 24 4336 3581 4530 136 52 -57 O ATOM 174 CB GLU A 24 19.689 70.247 33.809 1.00 36.13 C ANISOU 174 CB GLU C 24 4493 4258 4977 4 -38 -92 C ATOM 175 CG GLU A 24 18.285 69.718 33.601 1.00 36.81 C ANISOU 175 CG GLU C 24 4561 4448 4975 -25 -101 -79 C ATOM 176 CD GLU A 24 17.961 68.566 34.542 1.00 36.65 C ANISOU 176 CD GLU C 24 4609 4418 4894 0 -38 5 C ATOM 177 OE1 GLU A 24 17.943 68.782 35.786 1.00 39.64 O ANISOU 177 OE1 GLU C 24 5255 4825 4980 -212 -160 79 O ATOM 178 OE2 GLU A 24 17.732 67.452 34.028 1.00 38.66 O ANISOU 178 OE2 GLU C 24 4435 4610 5644 99 42 -32 O ATOM 179 N CYS A 25 22.575 71.800 32.944 1.00 32.46 N ANISOU 179 N CYS C 25 3884 3972 4475 79 -116 -18 N ATOM 180 CA CYS A 25 23.779 72.280 33.646 1.00 30.17 C ANISOU 180 CA CYS C 25 3628 3708 4124 14 -95 -47 C ATOM 181 C CYS A 25 24.175 73.704 33.222 1.00 29.73 C ANISOU 181 C CYS C 25 3649 3622 4023 16 -48 -39 C ATOM 182 O CYS A 25 24.238 74.010 32.041 1.00 29.80 O ANISOU 182 O CYS C 25 3451 3661 4208 58 -289 86 O ATOM 183 CB CYS A 25 24.942 71.324 33.407 1.00 28.97 C ANISOU 183 CB CYS C 25 3390 3748 3868 118 -94 41 C ATOM 184 SG CYS A 25 24.513 69.637 33.866 1.00 26.84 S ANISOU 184 SG CYS C 25 2877 2873 4446 -31 -317 -238 S ATOM 185 N ASP A 26 24.462 74.545 34.210 1.00 30.02 N ANISOU 185 N ASP C 26 3671 3526 4208 36 10 47 N ATOM 186 CA ASP A 26 24.771 75.953 33.974 1.00 28.84 C ANISOU 186 CA ASP C 26 3577 3402 3979 65 -7 -25 C ATOM 187 C ASP A 26 26.303 76.127 33.967 1.00 28.06 C ANISOU 187 C ASP C 26 3419 3281 3960 72 26 -75 C ATOM 188 O ASP A 26 26.931 75.929 35.005 1.00 28.97 O ANISOU 188 O ASP C 26 3465 2973 4568 21 -68 -309 O ATOM 189 CB ASP A 26 24.150 76.803 35.087 1.00 29.35 C ANISOU 189 CB ASP C 26 3655 3421 4075 84 26 18 C ATOM 190 CG ASP A 26 24.333 78.321 34.865 1.00 32.52 C ANISOU 190 CG ASP C 26 3816 4060 4481 25 -81 151 C ATOM 191 OD1 ASP A 26 25.299 78.773 34.207 1.00 32.98 O ANISOU 191 OD1 ASP C 26 4088 3635 4805 -112 -75 318 O ATOM 192 OD2 ASP A 26 23.485 79.077 35.363 1.00 40.07 O ANISOU 192 OD2 ASP C 26 4927 4917 5380 -260 7 406 O ATOM 193 N THR A 27 26.858 76.521 32.826 1.00 27.61 N ANISOU 193 N THR C 27 3303 3204 3981 76 50 -94 N ATOM 194 CA THR A 27 28.323 76.750 32.642 1.00 27.37 C ANISOU 194 CA THR C 27 3305 3250 3844 21 34 -22 C ATOM 195 C THR A 27 28.814 78.218 32.806 1.00 26.59 C ANISOU 195 C THR C 27 3199 3140 3764 3 11 86 C ATOM 196 O THR A 27 29.980 78.541 32.506 1.00 24.14 O ANISOU 196 O THR C 27 2950 2706 3516 54 120 -143 O ATOM 197 CB THR A 27 28.757 76.331 31.250 1.00 27.47 C ANISOU 197 CB THR C 27 3373 3300 3764 76 10 -94 C ATOM 198 OG1 THR A 27 28.116 77.166 30.277 1.00 30.70 O ANISOU 198 OG1 THR C 27 3216 3757 4692 96 -140 -205 O ATOM 199 CG2 THR A 27 28.438 74.866 30.987 1.00 23.94 C ANISOU 199 CG2 THR C 27 3069 3191 2837 142 -116 -360 C ATOM 200 N THR A 28 27.937 79.104 33.263 1.00 25.87 N ANISOU 200 N THR C 28 3110 3037 3681 -105 44 255 N ATOM 201 CA THR A 28 28.285 80.531 33.344 1.00 25.92 C ANISOU 201 CA THR C 28 3185 3141 3522 -63 -14 174 C ATOM 202 C THR A 28 29.263 80.815 34.463 1.00 26.69 C ANISOU 202 C THR C 28 3252 3227 3660 -73 -45 162 C ATOM 203 O THR A 28 29.363 80.054 35.451 1.00 26.68 O ANISOU 203 O THR C 28 2955 3053 4127 118 -316 405 O ATOM 204 CB THR A 28 27.041 81.428 33.559 1.00 25.13 C ANISOU 204 CB THR C 28 3078 3202 3266 -68 -80 145 C ATOM 205 OG1 THR A 28 26.448 81.135 34.839 1.00 25.67 O ANISOU 205 OG1 THR C 28 3384 3107 3261 156 -368 211 O ATOM 206 CG2 THR A 28 26.051 81.209 32.477 1.00 23.30 C ANISOU 206 CG2 THR C 28 2534 3023 3293 -61 -80 52 C ATOM 207 N VAL A 29 29.996 81.917 34.297 1.00 26.63 N ANISOU 207 N VAL C 29 3133 3310 3672 -110 -101 104 N ATOM 208 CA VAL A 29 30.867 82.470 35.342 1.00 26.04 C ANISOU 208 CA VAL C 29 3225 3241 3426 -119 -72 42 C ATOM 209 C VAL A 29 30.841 84.009 35.353 1.00 24.60 C ANISOU 209 C VAL C 29 3107 2980 3258 6 -70 98 C ATOM 210 O VAL A 29 30.581 84.630 34.323 1.00 26.70 O ANISOU 210 O VAL C 29 3395 3095 3655 -64 -136 140 O ATOM 211 CB VAL A 29 32.328 81.932 35.191 1.00 27.32 C ANISOU 211 CB VAL C 29 3377 3336 3666 -59 -47 47 C ATOM 212 CG1 VAL A 29 33.012 82.490 33.954 1.00 26.84 C ANISOU 212 CG1 VAL C 29 3477 3098 3622 -250 217 246 C ATOM 213 CG2 VAL A 29 33.131 82.171 36.456 1.00 27.75 C ANISOU 213 CG2 VAL C 29 3362 3375 3806 -78 -80 45 C ATOM 214 N THR A 30 31.048 84.592 36.527 1.00 24.75 N ANISOU 214 N THR C 30 3141 2865 3396 -17 -74 -63 N ATOM 215 CA THR A 30 31.151 86.057 36.729 1.00 25.08 C ANISOU 215 CA THR C 30 3131 3133 3263 -12 -123 -18 C ATOM 216 C THR A 30 32.611 86.429 37.015 1.00 25.30 C ANISOU 216 C THR C 30 3062 3198 3349 -4 -130 31 C ATOM 217 O THR A 30 33.322 85.742 37.762 1.00 26.29 O ANISOU 217 O THR C 30 2894 3228 3866 -12 -215 10 O ATOM 218 CB THR A 30 30.252 86.563 37.923 1.00 26.47 C ANISOU 218 CB THR C 30 3190 3306 3558 8 -9 -9 C ATOM 219 OG1 THR A 30 28.861 86.284 37.680 1.00 27.27 O ANISOU 219 OG1 THR C 30 3705 2972 3683 -111 -132 232 O ATOM 220 CG2 THR A 30 30.383 88.044 38.164 1.00 25.70 C ANISOU 220 CG2 THR C 30 3248 3206 3308 27 -41 -30 C ATOM 221 N LEU A 31 33.046 87.534 36.425 1.00 24.88 N ANISOU 221 N LEU C 31 2950 3219 3283 -109 -79 32 N ATOM 222 CA LEU A 31 34.356 88.109 36.665 1.00 25.19 C ANISOU 222 CA LEU C 31 3164 3086 3319 -73 -66 -27 C ATOM 223 C LEU A 31 34.137 89.602 36.827 1.00 25.34 C ANISOU 223 C LEU C 31 3235 2935 3458 -28 -62 59 C ATOM 224 O LEU A 31 33.732 90.286 35.888 1.00 26.34 O ANISOU 224 O LEU C 31 3171 3000 3836 13 -218 51 O ATOM 225 CB LEU A 31 35.307 87.818 35.493 1.00 24.37 C ANISOU 225 CB LEU C 31 3012 3086 3161 -101 -158 -13 C ATOM 226 CG LEU A 31 36.781 88.230 35.615 1.00 24.13 C ANISOU 226 CG LEU C 31 2996 3221 2948 -112 -30 -103 C ATOM 227 CD1 LEU A 31 37.484 87.392 36.709 1.00 24.69 C ANISOU 227 CD1 LEU C 31 3177 3317 2887 -260 0 -22 C ATOM 228 CD2 LEU A 31 37.547 88.125 34.265 1.00 24.10 C ANISOU 228 CD2 LEU C 31 3089 2927 3140 -76 -24 -84 C ATOM 229 N GLY A 32 34.362 90.086 38.037 1.00 28.24 N ANISOU 229 N GLY C 32 3400 3288 4041 -63 92 -75 N ATOM 230 CA GLY A 32 34.004 91.454 38.394 1.00 29.78 C ANISOU 230 CA GLY C 32 3591 3660 4061 -61 72 -22 C ATOM 231 C GLY A 32 32.509 91.642 38.264 1.00 30.24 C ANISOU 231 C GLY C 32 3762 3612 4113 -139 59 80 C ATOM 232 O GLY A 32 31.737 90.855 38.799 1.00 31.47 O ANISOU 232 O GLY C 32 3974 3757 4224 -229 30 120 O ATOM 233 N LYS A 33 32.111 92.647 37.495 1.00 32.50 N ANISOU 233 N LYS C 33 4137 3870 4339 -112 26 13 N ATOM 234 CA LYS A 33 30.695 93.062 37.395 1.00 33.45 C ANISOU 234 CA LYS C 33 4245 4032 4431 -107 28 -31 C ATOM 235 C LYS A 33 29.911 92.417 36.252 1.00 33.67 C ANISOU 235 C LYS C 33 4254 4012 4526 -106 64 -61 C ATOM 236 O LYS A 33 28.742 92.745 36.059 1.00 35.63 O ANISOU 236 O LYS C 33 4457 4163 4915 -216 64 -87 O ATOM 237 CB LYS A 33 30.630 94.580 37.226 1.00 35.56 C ANISOU 237 CB LYS C 33 4473 4269 4768 -138 21 44 C ATOM 238 CG LYS A 33 30.988 95.344 38.494 1.00 38.34 C ANISOU 238 CG LYS C 33 4815 4881 4869 -76 88 -34 C ATOM 239 CD LYS A 33 31.383 96.776 38.126 1.00 38.41 C ANISOU 239 CD LYS C 33 4737 4897 4959 20 64 -92 C ATOM 240 CE LYS A 33 31.500 97.651 39.361 1.00 41.80 C ANISOU 240 CE LYS C 33 5031 5457 5394 7 311 -95 C ATOM 241 NZ LYS A 33 32.451 98.781 39.100 1.00 47.74 N ANISOU 241 NZ LYS C 33 5558 6152 6427 311 75 48 N ATOM 242 N HIS A 34 30.529 91.507 35.499 1.00 31.70 N ANISOU 242 N HIS C 34 4004 3799 4240 -104 -17 -17 N ATOM 243 CA HIS A 34 29.871 90.909 34.363 1.00 30.10 C ANISOU 243 CA HIS C 34 3695 3682 4058 -94 -43 9 C ATOM 244 C HIS A 34 29.833 89.378 34.417 1.00 29.23 C ANISOU 244 C HIS C 34 3598 3558 3951 -54 -117 -34 C ATOM 245 O HIS A 34 30.732 88.731 34.944 1.00 25.94 O ANISOU 245 O HIS C 34 2680 3132 4044 -94 -152 82 O ATOM 246 CB HIS A 34 30.523 91.384 33.069 1.00 30.45 C ANISOU 246 CB HIS C 34 3880 3755 3935 -221 -33 1 C ATOM 247 CG HIS A 34 30.616 92.877 32.960 1.00 33.53 C ANISOU 247 CG HIS C 34 4130 4180 4430 -117 75 63 C ATOM 248 ND1 HIS A 34 31.561 93.615 33.642 1.00 37.51 N ANISOU 248 ND1 HIS C 34 4564 4581 5106 -90 -29 -38 N ATOM 249 CD2 HIS A 34 29.846 93.774 32.294 1.00 36.24 C ANISOU 249 CD2 HIS C 34 4453 4805 4510 -18 -206 -179 C ATOM 250 CE1 HIS A 34 31.382 94.897 33.388 1.00 40.36 C ANISOU 250 CE1 HIS C 34 4633 5106 5593 125 -85 -146 C ATOM 251 NE2 HIS A 34 30.348 95.022 32.574 1.00 40.29 N ANISOU 251 NE2 HIS C 34 4626 5344 5338 -25 -174 -298 N ATOM 252 N LYS A 35 28.767 88.835 33.837 1.00 29.52 N ANISOU 252 N LYS C 35 3602 3577 4034 -60 -59 -64 N ATOM 253 CA LYS A 35 28.543 87.399 33.724 1.00 29.17 C ANISOU 253 CA LYS C 35 3600 3569 3911 -71 -62 -42 C ATOM 254 C LYS A 35 28.784 86.958 32.284 1.00 28.05 C ANISOU 254 C LYS C 35 3403 3349 3905 20 -32 -97 C ATOM 255 O LYS A 35 28.372 87.648 31.325 1.00 28.40 O ANISOU 255 O LYS C 35 3450 3246 4093 -81 -123 -118 O ATOM 256 CB LYS A 35 27.118 87.089 34.158 1.00 30.10 C ANISOU 256 CB LYS C 35 3640 3657 4139 -81 -80 -6 C ATOM 257 CG LYS A 35 26.842 85.663 34.482 1.00 31.74 C ANISOU 257 CG LYS C 35 3924 3805 4329 1 -72 22 C ATOM 258 CD LYS A 35 25.572 85.579 35.330 1.00 32.01 C ANISOU 258 CD LYS C 35 4084 3915 4161 -27 -53 132 C ATOM 259 CE LYS A 35 24.935 84.217 35.248 1.00 33.33 C ANISOU 259 CE LYS C 35 4117 3949 4594 136 -51 131 C ATOM 260 NZ LYS A 35 23.971 84.097 36.386 1.00 35.88 N ANISOU 260 NZ LYS C 35 4446 4619 4565 267 0 123 N ATOM 261 N PHE A 36 29.463 85.819 32.115 1.00 26.61 N ANISOU 261 N PHE C 36 3250 3093 3768 -24 -83 -156 N ATOM 262 CA PHE A 36 29.765 85.281 30.779 1.00 25.43 C ANISOU 262 CA PHE C 36 3095 3161 3405 26 -121 -102 C ATOM 263 C PHE A 36 29.322 83.825 30.640 1.00 24.25 C ANISOU 263 C PHE C 36 2963 3084 3164 18 -94 -72 C ATOM 264 O PHE A 36 29.141 83.117 31.630 1.00 23.85 O ANISOU 264 O PHE C 36 2706 3205 3150 15 -74 -327 O ATOM 265 CB PHE A 36 31.262 85.387 30.438 1.00 24.66 C ANISOU 265 CB PHE C 36 2726 3291 3351 129 -155 -56 C ATOM 266 CG PHE A 36 31.836 86.756 30.662 1.00 22.71 C ANISOU 266 CG PHE C 36 2596 2949 3081 -14 -24 19 C ATOM 267 CD1 PHE A 36 31.774 87.722 29.656 1.00 22.57 C ANISOU 267 CD1 PHE C 36 2882 3062 2632 -106 70 173 C ATOM 268 CD2 PHE A 36 32.397 87.101 31.886 1.00 26.06 C ANISOU 268 CD2 PHE C 36 3014 3563 3324 -84 -6 -189 C ATOM 269 CE1 PHE A 36 32.294 89.011 29.870 1.00 21.70 C ANISOU 269 CE1 PHE C 36 2851 2538 2853 96 -129 -134 C ATOM 270 CE2 PHE A 36 32.912 88.386 32.105 1.00 25.85 C ANISOU 270 CE2 PHE C 36 3211 3178 3432 63 -96 47 C ATOM 271 CZ PHE A 36 32.845 89.337 31.108 1.00 21.52 C ANISOU 271 CZ PHE C 36 2873 2580 2722 -148 128 118 C ATOM 272 N LYS A 37 29.158 83.411 29.391 1.00 23.98 N ANISOU 272 N LYS C 37 2979 3196 2933 -18 -132 -128 N ATOM 273 CA LYS A 37 28.603 82.115 29.021 1.00 25.63 C ANISOU 273 CA LYS C 37 3157 3306 3273 -38 -115 -89 C ATOM 274 C LYS A 37 29.470 80.947 29.501 1.00 26.44 C ANISOU 274 C LYS C 37 3213 3241 3592 -65 -148 -84 C ATOM 275 O LYS A 37 28.932 79.923 29.930 1.00 27.27 O ANISOU 275 O LYS C 37 3157 3227 3975 -131 -289 -158 O ATOM 276 CB LYS A 37 28.481 82.004 27.484 1.00 26.67 C ANISOU 276 CB LYS C 37 3287 3487 3358 -109 -22 109 C ATOM 277 CG LYS A 37 27.247 82.655 26.888 1.00 30.71 C ANISOU 277 CG LYS C 37 3974 3973 3720 -29 -6 4 C ATOM 278 CD LYS A 37 27.096 82.269 25.419 1.00 30.05 C ANISOU 278 CD LYS C 37 4101 3811 3503 -61 -97 -190 C ATOM 279 CE LYS A 37 25.662 82.361 24.918 1.00 35.61 C ANISOU 279 CE LYS C 37 4793 4052 4682 -91 -92 -157 C ATOM 280 NZ LYS A 37 25.318 83.646 24.211 1.00 35.65 N ANISOU 280 NZ LYS C 37 4429 4639 4475 126 -53 -80 N ATOM 281 N LEU A 38 30.793 81.120 29.394 1.00 25.70 N ANISOU 281 N LEU C 38 3136 3087 3539 -88 -120 -28 N ATOM 282 CA LEU A 38 31.795 80.055 29.619 1.00 23.24 C ANISOU 282 CA LEU C 38 2871 2919 3038 9 -146 -170 C ATOM 283 C LEU A 38 32.969 80.607 30.401 1.00 22.38 C ANISOU 283 C LEU C 38 2650 2770 3081 -5 -169 -151 C ATOM 284 O LEU A 38 33.284 81.780 30.257 1.00 21.96 O ANISOU 284 O LEU C 38 2498 2793 3052 -97 -101 -102 O ATOM 285 CB LEU A 38 32.367 79.530 28.285 1.00 23.43 C ANISOU 285 CB LEU C 38 2970 2848 3081 26 -206 -96 C ATOM 286 CG LEU A 38 31.510 78.663 27.376 1.00 27.26 C ANISOU 286 CG LEU C 38 3460 3593 3303 44 58 35 C ATOM 287 CD1 LEU A 38 32.189 78.422 26.011 1.00 25.79 C ANISOU 287 CD1 LEU C 38 3453 3242 3102 57 -84 -29 C ATOM 288 CD2 LEU A 38 31.149 77.323 28.038 1.00 31.40 C ANISOU 288 CD2 LEU C 38 3809 4034 4087 -6 -187 -65 C ATOM 289 N PRO A 39 33.653 79.748 31.196 1.00 20.68 N ANISOU 289 N PRO C 39 2563 2529 2765 45 -174 -164 N ATOM 290 CA PRO A 39 34.890 80.117 31.880 1.00 20.07 C ANISOU 290 CA PRO C 39 2489 2568 2569 65 -130 -150 C ATOM 291 C PRO A 39 36.151 79.967 31.012 1.00 19.54 C ANISOU 291 C PRO C 39 2575 2526 2323 3 -94 -202 C ATOM 292 O PRO A 39 37.163 79.475 31.468 1.00 18.70 O ANISOU 292 O PRO C 39 2909 2759 1434 -69 -398 -216 O ATOM 293 CB PRO A 39 34.914 79.149 33.035 1.00 18.66 C ANISOU 293 CB PRO C 39 2557 2110 2422 28 -142 -126 C ATOM 294 CG PRO A 39 34.398 77.892 32.405 1.00 20.68 C ANISOU 294 CG PRO C 39 2581 2497 2775 -71 -244 -156 C ATOM 295 CD PRO A 39 33.278 78.353 31.505 1.00 19.99 C ANISOU 295 CD PRO C 39 2624 2443 2526 32 -121 -191 C ATOM 296 N VAL A 40 36.075 80.360 29.744 1.00 19.48 N ANISOU 296 N VAL C 40 2381 2660 2361 66 -277 -151 N ATOM 297 CA VAL A 40 37.203 80.316 28.820 1.00 22.19 C ANISOU 297 CA VAL C 40 2639 2860 2932 -33 -159 3 C ATOM 298 C VAL A 40 37.348 81.653 28.078 1.00 22.90 C ANISOU 298 C VAL C 40 2806 2929 2963 -81 -278 -18 C ATOM 299 O VAL A 40 36.364 82.392 27.875 1.00 22.54 O ANISOU 299 O VAL C 40 2787 3002 2772 -308 -208 -13 O ATOM 300 CB VAL A 40 37.081 79.238 27.683 1.00 21.82 C ANISOU 300 CB VAL C 40 2655 2861 2772 34 -93 -31 C ATOM 301 CG1 VAL A 40 36.886 77.791 28.255 1.00 20.29 C ANISOU 301 CG1 VAL C 40 2492 2832 2382 -59 65 10 C ATOM 302 CG2 VAL A 40 35.993 79.577 26.709 1.00 25.55 C ANISOU 302 CG2 VAL C 40 2878 3269 3559 -88 -374 -51 C ATOM 303 N VAL A 41 38.575 81.911 27.651 1.00 21.66 N ANISOU 303 N VAL C 41 2811 2787 2631 -24 -276 -23 N ATOM 304 CA VAL A 41 38.926 83.147 26.969 1.00 22.73 C ANISOU 304 CA VAL C 41 2847 2771 3015 -21 -192 -101 C ATOM 305 C VAL A 41 40.087 82.870 26.009 1.00 23.17 C ANISOU 305 C VAL C 41 2897 2931 2973 -29 -105 -83 C ATOM 306 O VAL A 41 41.083 82.198 26.363 1.00 22.40 O ANISOU 306 O VAL C 41 2776 2742 2991 -40 -284 -162 O ATOM 307 CB VAL A 41 39.243 84.303 27.969 1.00 21.52 C ANISOU 307 CB VAL C 41 2780 2596 2801 -70 -235 43 C ATOM 308 CG1 VAL A 41 40.435 83.982 28.853 1.00 20.31 C ANISOU 308 CG1 VAL C 41 2754 2730 2230 -13 -186 151 C ATOM 309 CG2 VAL A 41 39.453 85.645 27.211 1.00 17.92 C ANISOU 309 CG2 VAL C 41 2765 2752 1289 -9 -156 -17 C ATOM 310 N PRO A 42 39.975 83.375 24.779 1.00 23.74 N ANISOU 310 N PRO C 42 2962 2959 3097 -32 -68 -127 N ATOM 311 CA PRO A 42 41.062 83.221 23.841 1.00 24.45 C ANISOU 311 CA PRO C 42 3043 3090 3157 2 -110 -72 C ATOM 312 C PRO A 42 42.307 83.964 24.278 1.00 23.12 C ANISOU 312 C PRO C 42 2882 3028 2874 38 -169 -66 C ATOM 313 O PRO A 42 42.207 85.005 24.956 1.00 24.66 O ANISOU 313 O PRO C 42 3029 3377 2960 -54 -256 -224 O ATOM 314 CB PRO A 42 40.508 83.837 22.560 1.00 25.85 C ANISOU 314 CB PRO C 42 3258 3210 3352 89 -58 -195 C ATOM 315 CG PRO A 42 39.053 83.864 22.759 1.00 26.54 C ANISOU 315 CG PRO C 42 3502 3206 3373 -133 -50 14 C ATOM 316 CD PRO A 42 38.826 84.070 24.174 1.00 23.96 C ANISOU 316 CD PRO C 42 2775 3157 3170 -66 -140 -232 C ATOM 317 N ALA A 43 43.460 83.426 23.901 1.00 22.26 N ANISOU 317 N ALA C 43 2731 2917 2807 -26 -373 -79 N ATOM 318 CA ALA A 43 44.745 84.092 24.159 1.00 22.76 C ANISOU 318 CA ALA C 43 2841 2997 2808 37 -212 -92 C ATOM 319 C ALA A 43 44.723 85.498 23.573 1.00 23.09 C ANISOU 319 C ALA C 43 2904 3047 2822 95 -186 -142 C ATOM 320 O ALA A 43 44.288 85.697 22.405 1.00 21.48 O ANISOU 320 O ALA C 43 2806 3253 2099 235 -587 102 O ATOM 321 CB ALA A 43 45.901 83.289 23.528 1.00 21.74 C ANISOU 321 CB ALA C 43 2871 2906 2483 36 -401 -70 C ATOM 322 N ASN A 44 45.218 86.461 24.355 1.00 23.92 N ANISOU 322 N ASN C 44 3073 3228 2785 21 -173 103 N ATOM 323 CA ASN A 44 45.272 87.854 23.908 1.00 25.11 C ANISOU 323 CA ASN C 44 2997 3244 3299 -44 -141 -47 C ATOM 324 C ASN A 44 46.486 88.123 23.006 1.00 26.01 C ANISOU 324 C ASN C 44 3082 3340 3460 -43 -260 -9 C ATOM 325 O ASN A 44 47.385 88.877 23.372 1.00 28.08 O ANISOU 325 O ASN C 44 3368 3542 3758 -78 -191 -146 O ATOM 326 CB ASN A 44 45.192 88.822 25.084 1.00 24.17 C ANISOU 326 CB ASN C 44 2969 3099 3115 -11 -192 -101 C ATOM 327 CG ASN A 44 46.273 88.607 26.133 1.00 22.54 C ANISOU 327 CG ASN C 44 2554 3042 2966 -49 23 -243 C ATOM 328 OD1 ASN A 44 46.619 87.473 26.499 1.00 22.60 O ANISOU 328 OD1 ASN C 44 2787 3071 2729 47 -182 -347 O ATOM 329 ND2 ASN A 44 46.807 89.707 26.631 1.00 20.57 N ANISOU 329 ND2 ASN C 44 2744 2594 2478 -102 -221 -265 N ATOM 330 N MET A 45 46.487 87.483 21.840 1.00 27.55 N ANISOU 330 N MET C 45 3312 3592 3563 -30 -135 0 N ATOM 331 CA MET A 45 47.568 87.582 20.832 1.00 31.30 C ANISOU 331 CA MET C 45 3993 4012 3888 -3 -94 127 C ATOM 332 C MET A 45 46.973 87.766 19.451 1.00 31.35 C ANISOU 332 C MET C 45 4027 4038 3845 4 -45 59 C ATOM 333 O MET A 45 45.896 87.231 19.164 1.00 28.93 O ANISOU 333 O MET C 45 3627 4113 3252 242 -209 145 O ATOM 334 CB MET A 45 48.396 86.303 20.742 1.00 32.34 C ANISOU 334 CB MET C 45 4145 4146 3993 21 -72 204 C ATOM 335 CG MET A 45 48.968 85.807 22.014 1.00 34.33 C ANISOU 335 CG MET C 45 4484 4333 4224 -102 4 -2 C ATOM 336 SD MET A 45 49.443 84.062 21.880 1.00 37.65 S ANISOU 336 SD MET C 45 4812 4964 4526 -379 -206 154 S ATOM 337 CE MET A 45 50.778 84.071 23.074 1.00 38.65 C ANISOU 337 CE MET C 45 4891 4871 4922 -79 -28 -98 C ATOM 338 N GLN A 46 47.714 88.463 18.582 1.00 32.96 N ANISOU 338 N GLN C 46 4258 4224 4040 66 -144 69 N ATOM 339 CA GLN A 46 47.212 88.788 17.244 1.00 35.26 C ANISOU 339 CA GLN C 46 4529 4521 4345 40 -112 36 C ATOM 340 C GLN A 46 47.062 87.590 16.291 1.00 34.37 C ANISOU 340 C GLN C 46 4402 4336 4320 68 -149 110 C ATOM 341 O GLN A 46 46.344 87.665 15.301 1.00 34.24 O ANISOU 341 O GLN C 46 4502 4398 4109 163 -227 196 O ATOM 342 CB GLN A 46 48.033 89.916 16.590 1.00 36.32 C ANISOU 342 CB GLN C 46 4637 4670 4490 91 -105 43 C ATOM 343 CG GLN A 46 49.466 89.579 16.271 1.00 39.86 C ANISOU 343 CG GLN C 46 5167 4930 5048 0 -127 147 C ATOM 344 CD GLN A 46 50.025 90.383 15.080 1.00 41.11 C ANISOU 344 CD GLN C 46 5278 5234 5108 129 -149 220 C ATOM 345 OE1 GLN A 46 49.268 90.969 14.274 1.00 50.04 O ANISOU 345 OE1 GLN C 46 6472 6268 6273 -250 -214 -147 O ATOM 346 NE2 GLN A 46 51.356 90.402 14.962 1.00 45.68 N ANISOU 346 NE2 GLN C 46 5924 5411 6019 -29 -164 54 N ATOM 347 N THR A 47 47.739 86.494 16.600 1.00 34.53 N ANISOU 347 N THR C 47 4382 4296 4440 68 -155 137 N ATOM 348 CA THR A 47 47.563 85.238 15.883 1.00 34.61 C ANISOU 348 CA THR C 47 4469 4409 4272 19 -71 102 C ATOM 349 C THR A 47 46.264 84.492 16.255 1.00 34.95 C ANISOU 349 C THR C 47 4382 4477 4420 25 6 36 C ATOM 350 O THR A 47 45.905 83.519 15.596 1.00 36.52 O ANISOU 350 O THR C 47 4425 4730 4718 49 -27 10 O ATOM 351 CB THR A 47 48.761 84.314 16.163 1.00 36.26 C ANISOU 351 CB THR C 47 4620 4661 4496 -8 9 148 C ATOM 352 OG1 THR A 47 48.951 84.163 17.582 1.00 40.02 O ANISOU 352 OG1 THR C 47 5124 5188 4895 -76 -150 -81 O ATOM 353 CG2 THR A 47 50.020 84.895 15.565 1.00 36.90 C ANISOU 353 CG2 THR C 47 4619 4605 4792 36 52 102 C ATOM 354 N ILE A 48 45.565 84.954 17.298 1.00 33.48 N ANISOU 354 N ILE C 48 4110 4324 4287 36 -96 57 N ATOM 355 CA ILE A 48 44.369 84.275 17.835 1.00 32.37 C ANISOU 355 CA ILE C 48 4087 4161 4049 -31 -67 42 C ATOM 356 C ILE A 48 43.118 85.162 17.800 1.00 31.72 C ANISOU 356 C ILE C 48 4021 4194 3834 61 -134 -58 C ATOM 357 O ILE A 48 42.046 84.716 17.412 1.00 32.06 O ANISOU 357 O ILE C 48 4110 4276 3795 111 -334 -12 O ATOM 358 CB ILE A 48 44.678 83.795 19.293 1.00 31.99 C ANISOU 358 CB ILE C 48 4034 4082 4037 -60 7 51 C ATOM 359 CG1 ILE A 48 45.907 82.871 19.308 1.00 30.18 C ANISOU 359 CG1 ILE C 48 3876 4073 3515 -73 -128 -40 C ATOM 360 CG2 ILE A 48 43.474 83.126 19.962 1.00 31.94 C ANISOU 360 CG2 ILE C 48 3913 4133 4087 -54 -25 25 C ATOM 361 CD1 ILE A 48 45.740 81.561 18.556 1.00 32.09 C ANISOU 361 CD1 ILE C 48 3837 4315 4041 117 -84 -12 C ATOM 362 N ILE A 49 43.236 86.412 18.221 1.00 31.82 N ANISOU 362 N ILE C 49 4018 4206 3864 19 -200 -14 N ATOM 363 CA ILE A 49 42.083 87.308 18.274 1.00 31.51 C ANISOU 363 CA ILE C 49 3992 4055 3923 17 -108 17 C ATOM 364 C ILE A 49 42.282 88.570 17.426 1.00 32.10 C ANISOU 364 C ILE C 49 4163 4122 3909 6 -191 12 C ATOM 365 O ILE A 49 43.402 89.020 17.214 1.00 30.63 O ANISOU 365 O ILE C 49 4077 4021 3540 21 -367 7 O ATOM 366 CB ILE A 49 41.701 87.691 19.744 1.00 30.79 C ANISOU 366 CB ILE C 49 3806 3902 3988 97 -116 -24 C ATOM 367 CG1 ILE A 49 40.385 88.485 19.773 1.00 30.63 C ANISOU 367 CG1 ILE C 49 3723 3934 3979 -36 -23 120 C ATOM 368 CG2 ILE A 49 42.854 88.423 20.495 1.00 27.62 C ANISOU 368 CG2 ILE C 49 3616 3582 3297 71 -92 -27 C ATOM 369 CD1 ILE A 49 39.686 88.424 21.067 1.00 30.08 C ANISOU 369 CD1 ILE C 49 3633 4043 3751 -1 -124 24 C ATOM 370 N ASP A 50 41.168 89.109 16.935 1.00 32.74 N ANISOU 370 N ASP C 50 4264 4233 3939 -48 -178 -45 N ATOM 371 CA ASP A 50 41.163 90.404 16.265 1.00 33.96 C ANISOU 371 CA ASP C 50 4281 4382 4240 -32 -121 -13 C ATOM 372 C ASP A 50 39.858 91.137 16.574 1.00 35.00 C ANISOU 372 C ASP C 50 4434 4494 4368 -65 -144 16 C ATOM 373 O ASP A 50 39.041 90.653 17.357 1.00 34.16 O ANISOU 373 O ASP C 50 4417 4618 3942 -42 -233 -117 O ATOM 374 CB ASP A 50 41.404 90.240 14.742 1.00 33.98 C ANISOU 374 CB ASP C 50 4366 4427 4116 -36 -128 37 C ATOM 375 CG ASP A 50 40.276 89.488 14.007 1.00 36.10 C ANISOU 375 CG ASP C 50 4455 4663 4597 -80 -94 20 C ATOM 376 OD1 ASP A 50 39.148 89.333 14.524 1.00 38.58 O ANISOU 376 OD1 ASP C 50 5079 4889 4688 64 -464 122 O ATOM 377 OD2 ASP A 50 40.522 89.063 12.859 1.00 39.10 O ANISOU 377 OD2 ASP C 50 4963 5237 4656 109 -116 26 O ATOM 378 N GLU A 51 39.638 92.287 15.937 1.00 35.35 N ANISOU 378 N GLU C 51 4387 4568 4476 -3 -185 50 N ATOM 379 CA GLU A 51 38.457 93.093 16.240 1.00 34.69 C ANISOU 379 CA GLU C 51 4339 4439 4402 -24 -140 -4 C ATOM 380 C GLU A 51 37.135 92.432 15.858 1.00 34.27 C ANISOU 380 C GLU C 51 4299 4421 4298 -79 -195 -22 C ATOM 381 O GLU A 51 36.155 92.601 16.575 1.00 33.38 O ANISOU 381 O GLU C 51 4374 4189 4119 -29 -448 22 O ATOM 382 CB GLU A 51 38.548 94.475 15.597 1.00 36.41 C ANISOU 382 CB GLU C 51 4538 4628 4667 -26 -112 30 C ATOM 383 CG GLU A 51 39.725 95.311 16.098 1.00 38.32 C ANISOU 383 CG GLU C 51 4789 4841 4927 62 -128 -206 C ATOM 384 CD GLU A 51 41.032 95.024 15.348 1.00 43.48 C ANISOU 384 CD GLU C 51 5607 5550 5361 -129 -91 141 C ATOM 385 OE1 GLU A 51 41.100 94.026 14.589 1.00 44.68 O ANISOU 385 OE1 GLU C 51 5458 5967 5551 84 -232 81 O ATOM 386 OE2 GLU A 51 42.001 95.801 15.541 1.00 50.08 O ANISOU 386 OE2 GLU C 51 6205 6238 6584 109 -298 -3 O ATOM 387 N ARG A 52 37.094 91.722 14.726 1.00 34.21 N ANISOU 387 N ARG C 52 4167 4431 4397 -17 -174 -25 N ATOM 388 CA ARG A 52 35.868 91.017 14.316 1.00 33.98 C ANISOU 388 CA ARG C 52 4210 4365 4334 -38 -209 -31 C ATOM 389 C ARG A 52 35.542 89.903 15.320 1.00 32.52 C ANISOU 389 C ARG C 52 4159 4120 4077 -52 -269 33 C ATOM 390 O ARG A 52 34.399 89.755 15.736 1.00 33.21 O ANISOU 390 O ARG C 52 4225 4146 4245 -163 -512 32 O ATOM 391 CB ARG A 52 35.993 90.353 12.941 1.00 36.00 C ANISOU 391 CB ARG C 52 4576 4575 4525 -38 -33 23 C ATOM 392 CG ARG A 52 36.355 91.247 11.759 1.00 39.91 C ANISOU 392 CG ARG C 52 5064 5198 4901 -35 -234 29 C ATOM 393 CD ARG A 52 35.430 92.435 11.596 1.00 45.86 C ANISOU 393 CD ARG C 52 5680 5592 6152 -125 129 -11 C ATOM 394 NE ARG A 52 35.641 93.053 10.277 1.00 42.89 N ANISOU 394 NE ARG C 52 5340 5710 5244 -192 -349 20 N ATOM 395 CZ ARG A 52 35.390 94.322 9.966 1.00 45.82 C ANISOU 395 CZ ARG C 52 5677 5927 5804 -76 -70 -29 C ATOM 396 NH1 ARG A 52 34.907 95.167 10.878 1.00 45.14 N ANISOU 396 NH1 ARG C 52 5534 5767 5850 -2 -21 12 N ATOM 397 NH2 ARG A 52 35.636 94.742 8.718 1.00 46.94 N ANISOU 397 NH2 ARG C 52 5985 5840 6008 -114 -181 162 N ATOM 398 N ILE A 53 36.541 89.093 15.662 1.00 30.41 N ANISOU 398 N ILE C 53 3892 3912 3750 22 -141 8 N ATOM 399 CA ILE A 53 36.327 88.027 16.658 1.00 30.08 C ANISOU 399 CA ILE C 53 3789 3881 3758 -30 -74 -50 C ATOM 400 C ILE A 53 35.880 88.606 18.028 1.00 28.95 C ANISOU 400 C ILE C 53 3684 3767 3546 -74 -165 -81 C ATOM 401 O ILE A 53 34.929 88.096 18.633 1.00 30.52 O ANISOU 401 O ILE C 53 3701 3980 3913 -101 -274 -186 O ATOM 402 CB ILE A 53 37.550 87.096 16.788 1.00 30.01 C ANISOU 402 CB ILE C 53 3839 3827 3735 27 -3 -62 C ATOM 403 CG1 ILE A 53 37.740 86.300 15.492 1.00 29.50 C ANISOU 403 CG1 ILE C 53 3737 3938 3533 -184 -112 -32 C ATOM 404 CG2 ILE A 53 37.360 86.118 17.961 1.00 30.51 C ANISOU 404 CG2 ILE C 53 3814 3974 3802 12 -109 -48 C ATOM 405 CD1 ILE A 53 39.099 85.667 15.310 1.00 29.72 C ANISOU 405 CD1 ILE C 53 3984 3768 3539 -42 -120 -135 C ATOM 406 N ALA A 54 36.510 89.691 18.477 1.00 28.63 N ANISOU 406 N ALA C 54 3700 3762 3412 -59 -201 -111 N ATOM 407 CA ALA A 54 36.132 90.365 19.750 1.00 28.89 C ANISOU 407 CA ALA C 54 3672 3720 3585 -65 -113 -46 C ATOM 408 C ALA A 54 34.691 90.888 19.785 1.00 30.15 C ANISOU 408 C ALA C 54 3853 3853 3749 -67 -107 -43 C ATOM 409 O ALA A 54 33.999 90.858 20.843 1.00 28.38 O ANISOU 409 O ALA C 54 3398 3666 3716 -97 -225 -43 O ATOM 410 CB ALA A 54 37.114 91.501 20.051 1.00 28.55 C ANISOU 410 CB ALA C 54 3664 3769 3414 -66 -145 -80 C ATOM 411 N THR A 55 34.240 91.382 18.635 1.00 31.34 N ANISOU 411 N THR C 55 4017 3883 4006 -131 -143 -31 N ATOM 412 CA THR A 55 32.857 91.857 18.490 1.00 31.30 C ANISOU 412 CA THR C 55 4050 3854 3989 -57 -191 -87 C ATOM 413 C THR A 55 31.843 90.694 18.544 1.00 30.63 C ANISOU 413 C THR C 55 3985 3818 3832 -84 -255 -76 C ATOM 414 O THR A 55 30.812 90.792 19.211 1.00 29.55 O ANISOU 414 O THR C 55 3858 3660 3709 -46 -616 1 O ATOM 415 CB THR A 55 32.691 92.657 17.182 1.00 33.25 C ANISOU 415 CB THR C 55 4247 4072 4311 -37 -213 -50 C ATOM 416 OG1 THR A 55 33.676 93.710 17.133 1.00 34.95 O ANISOU 416 OG1 THR C 55 3972 4565 4740 25 -388 -241 O ATOM 417 CG2 THR A 55 31.294 93.255 17.112 1.00 31.57 C ANISOU 417 CG2 THR C 55 4118 3822 4054 -153 -177 -102 C ATOM 418 N TYR A 56 32.140 89.616 17.832 1.00 30.93 N ANISOU 418 N TYR C 56 4010 3908 3833 -53 -210 -138 N ATOM 419 CA TYR A 56 31.347 88.393 17.919 1.00 30.42 C ANISOU 419 CA TYR C 56 4024 3770 3762 -24 -159 -101 C ATOM 420 C TYR A 56 31.244 87.950 19.370 1.00 29.21 C ANISOU 420 C TYR C 56 3906 3524 3668 -71 -302 -246 C ATOM 421 O TYR A 56 30.162 87.644 19.871 1.00 29.04 O ANISOU 421 O TYR C 56 4159 3344 3528 -200 -516 -655 O ATOM 422 CB TYR A 56 31.949 87.251 17.102 1.00 33.53 C ANISOU 422 CB TYR C 56 4513 4118 4107 -281 -84 -183 C ATOM 423 CG TYR A 56 31.199 85.959 17.345 1.00 34.11 C ANISOU 423 CG TYR C 56 4180 4295 4484 54 -150 -186 C ATOM 424 CD1 TYR A 56 29.995 85.699 16.689 1.00 36.33 C ANISOU 424 CD1 TYR C 56 4491 4571 4741 71 -23 -203 C ATOM 425 CD2 TYR A 56 31.662 85.020 18.271 1.00 36.24 C ANISOU 425 CD2 TYR C 56 4523 4662 4584 99 -130 -313 C ATOM 426 CE1 TYR A 56 29.270 84.534 16.941 1.00 36.49 C ANISOU 426 CE1 TYR C 56 4467 4491 4905 124 -23 -216 C ATOM 427 CE2 TYR A 56 30.944 83.846 18.533 1.00 35.54 C ANISOU 427 CE2 TYR C 56 4255 4610 4638 114 -178 -247 C ATOM 428 CZ TYR A 56 29.749 83.608 17.850 1.00 37.86 C ANISOU 428 CZ TYR C 56 4576 4698 5111 270 -260 -182 C ATOM 429 OH TYR A 56 29.040 82.450 18.082 1.00 38.53 O ANISOU 429 OH TYR C 56 4576 4746 5314 370 -273 -317 O ATOM 430 N LEU A 57 32.381 87.909 20.050 1.00 28.11 N ANISOU 430 N LEU C 57 3681 3363 3633 68 -220 -176 N ATOM 431 CA LEU A 57 32.414 87.400 21.410 1.00 27.73 C ANISOU 431 CA LEU C 57 3612 3410 3511 40 -168 -86 C ATOM 432 C LEU A 57 31.599 88.260 22.348 1.00 26.59 C ANISOU 432 C LEU C 57 3371 3245 3486 -27 -245 -114 C ATOM 433 O LEU A 57 30.746 87.761 23.090 1.00 25.84 O ANISOU 433 O LEU C 57 2969 3226 3620 62 -594 -314 O ATOM 434 CB LEU A 57 33.885 87.228 21.901 1.00 25.88 C ANISOU 434 CB LEU C 57 3516 3245 3069 107 -139 -54 C ATOM 435 CG LEU A 57 34.609 86.071 21.194 1.00 27.97 C ANISOU 435 CG LEU C 57 3473 3353 3798 83 -190 -24 C ATOM 436 CD1 LEU A 57 36.074 86.007 21.566 1.00 29.10 C ANISOU 436 CD1 LEU C 57 3650 3643 3760 -30 -114 -229 C ATOM 437 CD2 LEU A 57 33.963 84.709 21.487 1.00 26.28 C ANISOU 437 CD2 LEU C 57 3143 3543 3298 31 26 -227 C ATOM 438 N ALA A 58 31.823 89.566 22.319 1.00 26.58 N ANISOU 438 N ALA C 58 3417 3302 3377 67 -223 -34 N ATOM 439 CA ALA A 58 31.116 90.458 23.236 1.00 28.30 C ANISOU 439 CA ALA C 58 3603 3550 3597 -8 -120 -17 C ATOM 440 C ALA A 58 29.610 90.485 22.950 1.00 28.89 C ANISOU 440 C ALA C 58 3624 3590 3760 -25 -108 -48 C ATOM 441 O ALA A 58 28.817 90.560 23.891 1.00 29.27 O ANISOU 441 O ALA C 58 3605 3403 4112 -60 -241 -126 O ATOM 442 CB ALA A 58 31.703 91.855 23.184 1.00 28.64 C ANISOU 442 CB ALA C 58 3645 3582 3655 -70 -17 -50 C ATOM 443 N GLU A 59 29.244 90.415 21.658 1.00 29.74 N ANISOU 443 N GLU C 59 3798 3610 3889 86 -61 -181 N ATOM 444 CA GLU A 59 27.827 90.384 21.210 1.00 30.77 C ANISOU 444 CA GLU C 59 3897 3834 3958 -2 -92 -74 C ATOM 445 C GLU A 59 27.045 89.168 21.680 1.00 32.50 C ANISOU 445 C GLU C 59 4101 3898 4348 51 -77 -72 C ATOM 446 O GLU A 59 25.819 89.186 21.708 1.00 33.99 O ANISOU 446 O GLU C 59 4375 3973 4565 -12 -89 -115 O ATOM 447 CB GLU A 59 27.760 90.407 19.694 1.00 28.51 C ANISOU 447 CB GLU C 59 3653 3497 3682 39 1 -173 C ATOM 448 CG GLU A 59 27.923 91.793 19.133 1.00 30.49 C ANISOU 448 CG GLU C 59 3895 4068 3622 -58 -103 16 C ATOM 449 CD GLU A 59 27.782 91.837 17.621 1.00 33.91 C ANISOU 449 CD GLU C 59 4401 4503 3980 57 -79 -61 C ATOM 450 OE1 GLU A 59 27.797 90.759 16.979 1.00 37.37 O ANISOU 450 OE1 GLU C 59 4454 5044 4700 -18 -8 -1 O ATOM 451 OE2 GLU A 59 27.656 92.973 17.088 1.00 38.10 O ANISOU 451 OE2 GLU C 59 4691 5104 4679 -126 -336 -71 O ATOM 452 N ASN A 60 27.768 88.125 22.059 1.00 32.80 N ANISOU 452 N ASN C 60 3982 4036 4442 7 -64 -28 N ATOM 453 CA ASN A 60 27.177 86.871 22.496 1.00 31.56 C ANISOU 453 CA ASN C 60 3973 3895 4122 -1 -72 -32 C ATOM 454 C ASN A 60 27.533 86.499 23.937 1.00 31.28 C ANISOU 454 C ASN C 60 3872 3864 4149 -40 -100 -93 C ATOM 455 O ASN A 60 27.314 85.366 24.342 1.00 32.51 O ANISOU 455 O ASN C 60 3974 3917 4461 83 -207 -198 O ATOM 456 CB ASN A 60 27.607 85.790 21.509 1.00 32.37 C ANISOU 456 CB ASN C 60 4016 4017 4262 82 -18 31 C ATOM 457 CG ASN A 60 26.875 85.899 20.196 1.00 35.29 C ANISOU 457 CG ASN C 60 4846 4236 4324 6 -162 9 C ATOM 458 OD1 ASN A 60 25.673 85.653 20.152 1.00 36.51 O ANISOU 458 OD1 ASN C 60 5268 4245 4360 181 -96 -311 O ATOM 459 ND2 ASN A 60 27.586 86.274 19.113 1.00 34.92 N ANISOU 459 ND2 ASN C 60 4804 4193 4268 -7 -278 -10 N ATOM 460 N ASN A 61 28.046 87.466 24.701 1.00 29.85 N ANISOU 460 N ASN C 61 3707 3623 4009 -127 -140 -106 N ATOM 461 CA ASN A 61 28.325 87.318 26.132 1.00 29.93 C ANISOU 461 CA ASN C 61 3760 3637 3975 -92 -34 -64 C ATOM 462 C ASN A 61 29.429 86.306 26.506 1.00 28.91 C ANISOU 462 C ASN C 61 3627 3489 3866 -147 -94 -50 C ATOM 463 O ASN A 61 29.370 85.687 27.589 1.00 29.08 O ANISOU 463 O ASN C 61 3688 3213 4148 -71 -172 -53 O ATOM 464 CB ASN A 61 27.054 87.007 26.933 1.00 30.98 C ANISOU 464 CB ASN C 61 3962 3760 4047 -14 -63 -52 C ATOM 465 CG ASN A 61 26.045 88.118 26.866 1.00 37.23 C ANISOU 465 CG ASN C 61 4661 4496 4986 -233 23 -60 C ATOM 466 OD1 ASN A 61 24.999 87.970 26.236 1.00 41.92 O ANISOU 466 OD1 ASN C 61 5637 4889 5400 -127 -257 -254 O ATOM 467 ND2 ASN A 61 26.345 89.240 27.512 1.00 41.19 N ANISOU 467 ND2 ASN C 61 4889 5132 5627 -94 69 -218 N ATOM 468 N TYR A 62 30.416 86.189 25.616 1.00 26.98 N ANISOU 468 N TYR C 62 3335 3340 3576 -66 -107 -65 N ATOM 469 CA TYR A 62 31.678 85.458 25.849 1.00 25.88 C ANISOU 469 CA TYR C 62 3280 3250 3301 35 -48 -168 C ATOM 470 C TYR A 62 32.736 86.498 26.244 1.00 26.08 C ANISOU 470 C TYR C 62 3375 3073 3459 58 -151 -154 C ATOM 471 O TYR A 62 32.722 87.614 25.736 1.00 26.21 O ANISOU 471 O TYR C 62 3468 2647 3843 41 -288 -275 O ATOM 472 CB TYR A 62 32.142 84.729 24.583 1.00 25.91 C ANISOU 472 CB TYR C 62 3157 3294 3393 -49 -84 -157 C ATOM 473 CG TYR A 62 31.225 83.619 24.103 1.00 25.63 C ANISOU 473 CG TYR C 62 3230 3242 3263 146 -123 -178 C ATOM 474 CD1 TYR A 62 31.193 82.399 24.759 1.00 27.86 C ANISOU 474 CD1 TYR C 62 3266 3496 3821 21 -69 -345 C ATOM 475 CD2 TYR A 62 30.407 83.792 22.971 1.00 26.71 C ANISOU 475 CD2 TYR C 62 3066 3469 3612 -34 -41 -186 C ATOM 476 CE1 TYR A 62 30.349 81.355 24.327 1.00 27.83 C ANISOU 476 CE1 TYR C 62 3325 3573 3677 177 -196 -254 C ATOM 477 CE2 TYR A 62 29.572 82.766 22.519 1.00 27.06 C ANISOU 477 CE2 TYR C 62 3370 3360 3549 99 -200 -282 C ATOM 478 CZ TYR A 62 29.553 81.533 23.206 1.00 28.64 C ANISOU 478 CZ TYR C 62 3286 3798 3796 217 -178 -367 C ATOM 479 OH TYR A 62 28.719 80.499 22.801 1.00 25.69 O ANISOU 479 OH TYR C 62 3080 3554 3126 -120 -343 -530 O ATOM 480 N PHE A 63 33.585 86.158 27.216 1.00 25.34 N ANISOU 480 N PHE C 63 3212 3097 3319 -13 -128 -248 N ATOM 481 CA PHE A 63 34.710 87.023 27.621 1.00 23.84 C ANISOU 481 CA PHE C 63 2998 3054 3006 32 -83 -122 C ATOM 482 C PHE A 63 35.769 87.060 26.510 1.00 21.87 C ANISOU 482 C PHE C 63 2790 2817 2700 10 -33 -264 C ATOM 483 O PHE A 63 35.995 86.078 25.856 1.00 20.69 O ANISOU 483 O PHE C 63 2811 2776 2274 -20 -240 -52 O ATOM 484 CB PHE A 63 35.281 86.527 28.980 1.00 24.20 C ANISOU 484 CB PHE C 63 2962 2941 3291 46 -12 -229 C ATOM 485 CG PHE A 63 36.313 87.430 29.610 1.00 24.62 C ANISOU 485 CG PHE C 63 3193 3136 3024 -98 -130 -218 C ATOM 486 CD1 PHE A 63 36.111 88.805 29.744 1.00 25.59 C ANISOU 486 CD1 PHE C 63 3453 3305 2964 -144 85 -117 C ATOM 487 CD2 PHE A 63 37.493 86.899 30.104 1.00 22.42 C ANISOU 487 CD2 PHE C 63 2749 2736 3032 -325 117 205 C ATOM 488 CE1 PHE A 63 37.062 89.618 30.301 1.00 24.21 C ANISOU 488 CE1 PHE C 63 3006 2930 3261 11 -186 89 C ATOM 489 CE2 PHE A 63 38.442 87.707 30.707 1.00 22.70 C ANISOU 489 CE2 PHE C 63 3001 2915 2709 -97 -65 35 C ATOM 490 CZ PHE A 63 38.225 89.067 30.814 1.00 25.05 C ANISOU 490 CZ PHE C 63 3140 3176 3199 52 35 41 C ATOM 491 N TYR A 64 36.371 88.225 26.269 1.00 21.51 N ANISOU 491 N TYR C 64 2678 2882 2611 -6 -125 -214 N ATOM 492 CA TYR A 64 37.543 88.330 25.416 1.00 22.04 C ANISOU 492 CA TYR C 64 2767 2849 2757 30 -110 -195 C ATOM 493 C TYR A 64 38.509 89.337 26.052 1.00 22.21 C ANISOU 493 C TYR C 64 2715 2807 2915 -22 -161 -130 C ATOM 494 O TYR A 64 38.151 90.109 26.937 1.00 23.42 O ANISOU 494 O TYR C 64 2551 2924 3422 138 -160 -247 O ATOM 495 CB TYR A 64 37.162 88.797 23.989 1.00 22.19 C ANISOU 495 CB TYR C 64 2840 2832 2756 49 -160 -267 C ATOM 496 CG TYR A 64 36.905 90.293 23.954 1.00 21.80 C ANISOU 496 CG TYR C 64 2836 2732 2714 50 22 -371 C ATOM 497 CD1 TYR A 64 37.949 91.200 23.751 1.00 23.83 C ANISOU 497 CD1 TYR C 64 3088 2996 2969 83 -351 -79 C ATOM 498 CD2 TYR A 64 35.651 90.804 24.206 1.00 18.46 C ANISOU 498 CD2 TYR C 64 2695 2984 1333 -57 -300 222 C ATOM 499 CE1 TYR A 64 37.731 92.567 23.794 1.00 22.66 C ANISOU 499 CE1 TYR C 64 2859 2910 2837 -30 -49 -112 C ATOM 500 CE2 TYR A 64 35.425 92.181 24.267 1.00 22.01 C ANISOU 500 CE2 TYR C 64 2708 2963 2689 15 -124 152 C ATOM 501 CZ TYR A 64 36.462 93.050 24.042 1.00 24.05 C ANISOU 501 CZ TYR C 64 2940 3046 3153 39 -73 -26 C ATOM 502 OH TYR A 64 36.222 94.402 24.083 1.00 25.50 O ANISOU 502 OH TYR C 64 2849 3120 3717 -36 -117 -32 O ATOM 503 N ILE A 65 39.750 89.281 25.613 1.00 22.93 N ANISOU 503 N ILE C 65 2708 2931 3070 -75 -200 -162 N ATOM 504 CA ILE A 65 40.772 90.278 25.947 1.00 23.30 C ANISOU 504 CA ILE C 65 2792 2917 3142 -22 -154 -201 C ATOM 505 C ILE A 65 41.508 90.530 24.646 1.00 22.60 C ANISOU 505 C ILE C 65 2805 2920 2863 -24 -127 -233 C ATOM 506 O ILE A 65 42.139 89.640 24.072 1.00 21.33 O ANISOU 506 O ILE C 65 2496 2716 2892 -105 -627 -551 O ATOM 507 CB ILE A 65 41.817 89.786 26.981 1.00 22.34 C ANISOU 507 CB ILE C 65 2919 2851 2715 -7 -48 -196 C ATOM 508 CG1 ILE A 65 41.178 89.451 28.330 1.00 22.56 C ANISOU 508 CG1 ILE C 65 2814 2790 2965 -4 -262 -134 C ATOM 509 CG2 ILE A 65 42.956 90.781 27.093 1.00 19.24 C ANISOU 509 CG2 ILE C 65 2116 2684 2508 -417 -82 -136 C ATOM 510 CD1 ILE A 65 42.122 88.646 29.269 1.00 23.07 C ANISOU 510 CD1 ILE C 65 2764 2720 3281 105 -160 -232 C ATOM 511 N MET A 66 41.437 91.767 24.180 1.00 25.28 N ANISOU 511 N MET C 66 3060 3247 3297 -29 -77 -106 N ATOM 512 CA MET A 66 42.094 92.146 22.955 1.00 26.26 C ANISOU 512 CA MET C 66 3171 3386 3422 15 -131 -63 C ATOM 513 C MET A 66 43.598 92.252 23.182 1.00 26.30 C ANISOU 513 C MET C 66 3052 3425 3513 -43 -151 -9 C ATOM 514 O MET A 66 44.051 92.585 24.286 1.00 25.42 O ANISOU 514 O MET C 66 2985 3174 3499 33 -398 -11 O ATOM 515 CB MET A 66 41.519 93.485 22.487 1.00 28.00 C ANISOU 515 CB MET C 66 3301 3513 3822 -60 -99 -40 C ATOM 516 CG MET A 66 41.840 93.851 21.088 1.00 34.01 C ANISOU 516 CG MET C 66 4042 4446 4431 -136 -226 63 C ATOM 517 SD MET A 66 41.552 92.637 19.825 1.00 31.20 S ANISOU 517 SD MET C 66 3133 4118 4603 503 -1120 -662 S ATOM 518 CE MET A 66 42.317 93.528 18.492 1.00 33.42 C ANISOU 518 CE MET C 66 4416 4046 4235 37 -313 72 C ATOM 519 N HIS A 67 44.352 91.962 22.128 1.00 27.19 N ANISOU 519 N HIS C 67 3256 3583 3491 3 -267 54 N ATOM 520 CA HIS A 67 45.807 92.126 22.112 1.00 28.82 C ANISOU 520 CA HIS C 67 3563 3642 3742 37 -178 -27 C ATOM 521 C HIS A 67 46.213 93.617 21.926 1.00 29.47 C ANISOU 521 C HIS C 67 3628 3746 3824 100 -171 6 C ATOM 522 O HIS A 67 45.373 94.482 21.578 1.00 28.38 O ANISOU 522 O HIS C 67 3441 3720 3622 277 -371 68 O ATOM 523 CB HIS A 67 46.424 91.272 20.983 1.00 29.63 C ANISOU 523 CB HIS C 67 3509 3703 4046 43 -67 -64 C ATOM 524 CG HIS A 67 46.045 91.723 19.599 1.00 33.72 C ANISOU 524 CG HIS C 67 4323 4371 4117 124 -71 84 C ATOM 525 ND1 HIS A 67 46.576 92.848 19.003 1.00 34.11 N ANISOU 525 ND1 HIS C 67 4297 4391 4272 131 -108 154 N ATOM 526 CD2 HIS A 67 45.158 91.218 18.711 1.00 34.59 C ANISOU 526 CD2 HIS C 67 4237 4470 4433 143 -102 -58 C ATOM 527 CE1 HIS A 67 46.042 93.006 17.806 1.00 32.70 C ANISOU 527 CE1 HIS C 67 4199 4053 4172 8 -145 72 C ATOM 528 NE2 HIS A 67 45.183 92.025 17.601 1.00 33.87 N ANISOU 528 NE2 HIS C 67 4275 4275 4319 51 -194 102 N ATOM 529 N ARG A 68 47.500 93.898 22.145 1.00 29.79 N ANISOU 529 N ARG C 68 3785 3828 3704 74 -194 7 N ATOM 530 CA ARG A 68 48.024 95.265 22.029 1.00 31.53 C ANISOU 530 CA ARG C 68 3912 3969 4096 65 -145 -75 C ATOM 531 C ARG A 68 49.084 95.391 20.924 1.00 32.34 C ANISOU 531 C ARG C 68 4058 4039 4189 -58 -268 -150 C ATOM 532 O ARG A 68 50.006 96.207 21.021 1.00 32.72 O ANISOU 532 O ARG C 68 4341 3914 4176 -26 -448 -219 O ATOM 533 CB ARG A 68 48.579 95.732 23.371 1.00 31.82 C ANISOU 533 CB ARG C 68 3919 3921 4250 26 -3 9 C ATOM 534 CG ARG A 68 49.638 94.814 23.957 1.00 30.98 C ANISOU 534 CG ARG C 68 3827 3799 4143 225 -256 -18 C ATOM 535 CD ARG A 68 50.204 95.424 25.167 1.00 31.63 C ANISOU 535 CD ARG C 68 3921 4104 3992 162 -89 51 C ATOM 536 NE ARG A 68 51.129 94.542 25.876 1.00 34.80 N ANISOU 536 NE ARG C 68 4274 4355 4594 115 -201 -99 N ATOM 537 CZ ARG A 68 52.442 94.734 26.031 1.00 34.62 C ANISOU 537 CZ ARG C 68 4235 4310 4609 -70 -102 101 C ATOM 538 NH1 ARG A 68 53.075 95.791 25.529 1.00 32.39 N ANISOU 538 NH1 ARG C 68 4089 3917 4299 0 11 145 N ATOM 539 NH2 ARG A 68 53.134 93.851 26.735 1.00 34.59 N ANISOU 539 NH2 ARG C 68 4400 4467 4274 -155 -135 -34 N ATOM 540 N PHE A 69 48.941 94.620 19.861 1.00 35.02 N ANISOU 540 N PHE C 69 4347 4462 4494 -65 -170 -93 N ATOM 541 CA PHE A 69 49.881 94.691 18.754 1.00 35.93 C ANISOU 541 CA PHE C 69 4552 4515 4582 -30 -97 26 C ATOM 542 C PHE A 69 49.784 96.009 17.972 1.00 38.37 C ANISOU 542 C PHE C 69 4792 4801 4985 -37 -144 17 C ATOM 543 O PHE A 69 50.783 96.488 17.419 1.00 40.91 O ANISOU 543 O PHE C 69 5137 5159 5246 68 -213 131 O ATOM 544 CB PHE A 69 49.681 93.532 17.793 1.00 41.27 C ANISOU 544 CB PHE C 69 4854 5408 5416 140 -116 -565 C ATOM 545 CG PHE A 69 50.788 93.405 16.782 1.00 37.85 C ANISOU 545 CG PHE C 69 4923 4761 4694 -141 -40 128 C ATOM 546 CD1 PHE A 69 52.029 92.881 17.157 1.00 42.48 C ANISOU 546 CD1 PHE C 69 5722 5213 5202 -106 -24 -52 C ATOM 547 CD2 PHE A 69 50.608 93.822 15.464 1.00 43.04 C ANISOU 547 CD2 PHE C 69 5534 5511 5306 -163 -101 54 C ATOM 548 CE1 PHE A 69 53.071 92.771 16.228 1.00 42.28 C ANISOU 548 CE1 PHE C 69 5690 5043 5330 -179 17 184 C ATOM 549 CE2 PHE A 69 51.647 93.723 14.533 1.00 41.52 C ANISOU 549 CE2 PHE C 69 5605 5178 4993 -29 -22 259 C ATOM 550 CZ PHE A 69 52.875 93.188 14.917 1.00 41.49 C ANISOU 550 CZ PHE C 69 5452 5086 5224 -41 -37 195 C ATOM 551 N GLN A 70 48.594 96.599 17.929 1.00 37.65 N ANISOU 551 N GLN C 70 4670 4757 4877 -42 -111 -86 N ATOM 552 CA GLN A 70 48.431 97.914 17.286 1.00 36.65 C ANISOU 552 CA GLN C 70 4599 4705 4620 8 -106 -22 C ATOM 553 C GLN A 70 47.934 98.906 18.296 1.00 34.75 C ANISOU 553 C GLN C 70 4314 4399 4488 17 -247 -45 C ATOM 554 O GLN A 70 46.793 99.336 18.226 1.00 34.14 O ANISOU 554 O GLN C 70 4293 4244 4433 48 -268 -106 O ATOM 555 CB GLN A 70 47.478 97.818 16.111 1.00 37.00 C ANISOU 555 CB GLN C 70 4701 4693 4661 14 -150 -92 C ATOM 556 CG GLN A 70 48.049 96.972 14.982 1.00 38.84 C ANISOU 556 CG GLN C 70 5060 4832 4865 -134 31 -19 C ATOM 557 CD GLN A 70 47.088 96.852 13.822 1.00 41.55 C ANISOU 557 CD GLN C 70 5391 5327 5067 -34 87 -139 C ATOM 558 OE1 GLN A 70 45.938 96.411 13.992 1.00 48.71 O ANISOU 558 OE1 GLN C 70 6432 5818 6256 199 -51 37 O ATOM 559 NE2 GLN A 70 47.547 97.233 12.628 1.00 47.80 N ANISOU 559 NE2 GLN C 70 6179 6171 5810 9 -235 236 N ATOM 560 N PRO A 71 48.808 99.279 19.249 1.00 32.99 N ANISOU 560 N PRO C 71 4026 4239 4266 98 -216 18 N ATOM 561 CA PRO A 71 48.381 99.981 20.427 1.00 33.40 C ANISOU 561 CA PRO C 71 4109 4227 4351 35 -173 26 C ATOM 562 C PRO A 71 47.715 101.301 20.167 1.00 32.88 C ANISOU 562 C PRO C 71 4021 4146 4323 27 -170 -7 C ATOM 563 O PRO A 71 46.977 101.769 21.029 1.00 32.26 O ANISOU 563 O PRO C 71 3595 4077 4585 16 -338 -37 O ATOM 564 CB PRO A 71 49.685 100.195 21.205 1.00 32.95 C ANISOU 564 CB PRO C 71 4074 4137 4309 40 -82 15 C ATOM 565 CG PRO A 71 50.754 100.056 20.214 1.00 31.92 C ANISOU 565 CG PRO C 71 4038 3952 4135 5 -206 -51 C ATOM 566 CD PRO A 71 50.270 99.065 19.248 1.00 33.09 C ANISOU 566 CD PRO C 71 4078 4252 4240 -6 -133 -31 C ATOM 567 N GLU A 72 47.997 101.898 19.006 1.00 33.70 N ANISOU 567 N GLU C 72 4169 4240 4392 -4 -145 -118 N ATOM 568 CA GLU A 72 47.432 103.195 18.651 1.00 35.00 C ANISOU 568 CA GLU C 72 4374 4386 4535 -12 -160 -64 C ATOM 569 C GLU A 72 45.908 103.117 18.418 1.00 34.96 C ANISOU 569 C GLU C 72 4387 4333 4560 -34 -128 -123 C ATOM 570 O GLU A 72 45.221 104.123 18.496 1.00 34.93 O ANISOU 570 O GLU C 72 4354 4339 4576 -16 -199 -204 O ATOM 571 CB GLU A 72 48.171 103.784 17.431 1.00 35.53 C ANISOU 571 CB GLU C 72 4495 4409 4595 -2 -173 -40 C ATOM 572 CG GLU A 72 47.816 103.194 16.059 1.00 38.13 C ANISOU 572 CG GLU C 72 4792 4871 4823 -48 51 -6 C ATOM 573 CD GLU A 72 48.539 101.902 15.704 1.00 39.18 C ANISOU 573 CD GLU C 72 4980 5105 4802 -162 46 -60 C ATOM 574 OE1 GLU A 72 49.286 101.358 16.558 1.00 37.19 O ANISOU 574 OE1 GLU C 72 4698 4775 4655 -171 -106 -90 O ATOM 575 OE2 GLU A 72 48.341 101.434 14.545 1.00 38.26 O ANISOU 575 OE2 GLU C 72 4953 5152 4430 213 -85 -119 O ATOM 576 N LYS A 73 45.406 101.909 18.177 1.00 35.25 N ANISOU 576 N LYS C 73 4396 4390 4607 -44 -164 -198 N ATOM 577 CA LYS A 73 43.982 101.657 17.943 1.00 35.75 C ANISOU 577 CA LYS C 73 4488 4475 4619 -9 -119 -89 C ATOM 578 C LYS A 73 43.126 101.425 19.183 1.00 34.71 C ANISOU 578 C LYS C 73 4317 4344 4527 60 -170 -105 C ATOM 579 O LYS A 73 41.911 101.340 19.064 1.00 35.32 O ANISOU 579 O LYS C 73 4207 4432 4781 52 -365 -196 O ATOM 580 CB LYS A 73 43.828 100.447 17.018 1.00 36.98 C ANISOU 580 CB LYS C 73 4531 4702 4815 -18 -57 -225 C ATOM 581 CG LYS A 73 44.434 100.659 15.642 1.00 39.01 C ANISOU 581 CG LYS C 73 4905 4847 5069 -19 -102 13 C ATOM 582 CD LYS A 73 44.319 99.406 14.791 1.00 38.60 C ANISOU 582 CD LYS C 73 4921 4880 4863 -46 -49 -48 C ATOM 583 CE LYS A 73 44.588 99.689 13.327 1.00 42.43 C ANISOU 583 CE LYS C 73 5517 5411 5191 58 9 66 C ATOM 584 NZ LYS A 73 44.413 98.466 12.475 1.00 46.24 N ANISOU 584 NZ LYS C 73 5818 6057 5694 -2 276 -16 N ATOM 585 N ARG A 74 43.736 101.327 20.359 1.00 34.01 N ANISOU 585 N ARG C 74 4250 4170 4501 116 -109 -105 N ATOM 586 CA ARG A 74 43.013 100.956 21.582 1.00 33.43 C ANISOU 586 CA ARG C 74 4174 4195 4332 42 -78 -106 C ATOM 587 C ARG A 74 42.028 102.004 22.082 1.00 33.89 C ANISOU 587 C ARG C 74 4222 4195 4457 53 -208 -155 C ATOM 588 O ARG A 74 40.962 101.659 22.587 1.00 31.80 O ANISOU 588 O ARG C 74 3970 3946 4163 39 -484 -259 O ATOM 589 CB ARG A 74 44.004 100.594 22.699 1.00 33.26 C ANISOU 589 CB ARG C 74 4126 4120 4388 97 -64 -4 C ATOM 590 CG ARG A 74 44.870 99.380 22.366 1.00 32.46 C ANISOU 590 CG ARG C 74 3990 4029 4314 59 0 -76 C ATOM 591 CD ARG A 74 45.956 99.147 23.405 1.00 32.59 C ANISOU 591 CD ARG C 74 3971 4098 4313 -32 -48 -73 C ATOM 592 NE ARG A 74 46.922 100.254 23.449 1.00 34.27 N ANISOU 592 NE ARG C 74 4077 4190 4752 74 -284 -273 N ATOM 593 CZ ARG A 74 47.883 100.402 24.357 1.00 35.33 C ANISOU 593 CZ ARG C 74 4334 4495 4591 191 -168 -112 C ATOM 594 NH1 ARG A 74 48.047 99.513 25.329 1.00 33.65 N ANISOU 594 NH1 ARG C 74 4170 4055 4557 108 -222 24 N ATOM 595 NH2 ARG A 74 48.694 101.464 24.294 1.00 32.68 N ANISOU 595 NH2 ARG C 74 4049 4045 4320 110 -178 -88 N ATOM 596 N ILE A 75 42.370 103.289 21.975 1.00 34.66 N ANISOU 596 N ILE C 75 4223 4313 4631 46 -158 -71 N ATOM 597 CA ILE A 75 41.449 104.319 22.444 1.00 34.83 C ANISOU 597 CA ILE C 75 4239 4434 4558 66 -76 -59 C ATOM 598 C ILE A 75 40.173 104.308 21.591 1.00 34.20 C ANISOU 598 C ILE C 75 4030 4351 4613 1 -192 -26 C ATOM 599 O ILE A 75 39.079 104.396 22.151 1.00 35.05 O ANISOU 599 O ILE C 75 4033 4300 4982 -139 -361 -84 O ATOM 600 CB ILE A 75 42.095 105.735 22.467 1.00 35.35 C ANISOU 600 CB ILE C 75 4232 4479 4719 85 -7 -37 C ATOM 601 CG1 ILE A 75 43.236 105.758 23.473 1.00 37.80 C ANISOU 601 CG1 ILE C 75 4635 4782 4945 125 -13 -48 C ATOM 602 CG2 ILE A 75 41.093 106.787 22.888 1.00 35.37 C ANISOU 602 CG2 ILE C 75 4338 4419 4682 72 -69 10 C ATOM 603 CD1 ILE A 75 44.262 106.820 23.178 1.00 37.59 C ANISOU 603 CD1 ILE C 75 4639 4763 4877 122 0 -20 C ATOM 604 N SER A 76 40.310 104.157 20.266 1.00 33.21 N ANISOU 604 N SER C 76 3927 4218 4472 70 -128 -53 N ATOM 605 CA SER A 76 39.133 104.086 19.386 1.00 32.77 C ANISOU 605 CA SER C 76 3918 4158 4373 102 -148 -42 C ATOM 606 C SER A 76 38.343 102.785 19.628 1.00 31.23 C ANISOU 606 C SER C 76 3818 3850 4199 48 -245 -16 C ATOM 607 O SER A 76 37.103 102.831 19.784 1.00 30.36 O ANISOU 607 O SER C 76 3743 3609 4183 57 -410 -353 O ATOM 608 CB SER A 76 39.492 104.263 17.906 1.00 34.57 C ANISOU 608 CB SER C 76 4342 4296 4495 89 -56 8 C ATOM 609 OG SER A 76 39.814 103.043 17.235 1.00 40.75 O ANISOU 609 OG SER C 76 4582 5454 5444 247 -143 -59 O ATOM 610 N PHE A 77 39.060 101.658 19.708 1.00 28.68 N ANISOU 610 N PHE C 77 3533 3577 3785 82 -209 -26 N ATOM 611 CA PHE A 77 38.450 100.366 20.071 1.00 29.35 C ANISOU 611 CA PHE C 77 3578 3669 3903 -24 -189 -79 C ATOM 612 C PHE A 77 37.569 100.495 21.311 1.00 27.83 C ANISOU 612 C PHE C 77 3211 3567 3795 -53 -380 -119 C ATOM 613 O PHE A 77 36.414 100.070 21.294 1.00 29.71 O ANISOU 613 O PHE C 77 3456 3608 4222 -8 -627 -279 O ATOM 614 CB PHE A 77 39.524 99.281 20.250 1.00 28.39 C ANISOU 614 CB PHE C 77 3329 3719 3738 133 -305 -6 C ATOM 615 CG PHE A 77 38.980 97.926 20.666 1.00 28.46 C ANISOU 615 CG PHE C 77 3517 3619 3677 92 -147 -86 C ATOM 616 CD1 PHE A 77 38.585 96.979 19.723 1.00 26.79 C ANISOU 616 CD1 PHE C 77 3152 3465 3560 3 -292 -285 C ATOM 617 CD2 PHE A 77 38.874 97.614 22.010 1.00 28.16 C ANISOU 617 CD2 PHE C 77 3533 3532 3633 211 -240 -26 C ATOM 618 CE1 PHE A 77 38.091 95.720 20.133 1.00 27.29 C ANISOU 618 CE1 PHE C 77 3743 3548 3076 174 -303 -79 C ATOM 619 CE2 PHE A 77 38.389 96.369 22.421 1.00 29.13 C ANISOU 619 CE2 PHE C 77 3445 3765 3857 61 -179 -63 C ATOM 620 CZ PHE A 77 37.999 95.439 21.505 1.00 24.16 C ANISOU 620 CZ PHE C 77 3155 3134 2888 -339 -239 -218 C ATOM 621 N ILE A 78 38.084 101.078 22.381 1.00 27.81 N ANISOU 621 N ILE C 78 3104 3523 3937 -97 -317 -46 N ATOM 622 CA ILE A 78 37.286 101.210 23.604 1.00 29.75 C ANISOU 622 CA ILE C 78 3561 3745 3995 -88 -213 -48 C ATOM 623 C ILE A 78 36.026 102.006 23.296 1.00 30.75 C ANISOU 623 C ILE C 78 3614 3767 4302 -116 -252 0 C ATOM 624 O ILE A 78 34.906 101.562 23.539 1.00 30.50 O ANISOU 624 O ILE C 78 3242 3800 4546 -292 -481 -32 O ATOM 625 CB ILE A 78 38.052 101.889 24.754 1.00 29.03 C ANISOU 625 CB ILE C 78 3485 3471 4071 -14 -170 -42 C ATOM 626 CG1 ILE A 78 39.239 101.016 25.190 1.00 30.72 C ANISOU 626 CG1 ILE C 78 3641 3927 4104 -80 -98 -106 C ATOM 627 CG2 ILE A 78 37.158 102.108 25.970 1.00 28.52 C ANISOU 627 CG2 ILE C 78 3326 3602 3907 -51 -149 -137 C ATOM 628 CD1 ILE A 78 40.469 101.826 25.534 1.00 31.48 C ANISOU 628 CD1 ILE C 78 3903 3925 4130 -86 -72 -244 C ATOM 629 N ARG A 79 36.228 103.167 22.696 1.00 31.79 N ANISOU 629 N ARG C 79 3729 3941 4409 -125 -239 -58 N ATOM 630 CA ARG A 79 35.134 104.106 22.465 1.00 32.32 C ANISOU 630 CA ARG C 79 3862 4121 4296 -75 -235 -34 C ATOM 631 C ARG A 79 34.026 103.442 21.661 1.00 30.72 C ANISOU 631 C ARG C 79 3604 3966 4099 -88 -371 -10 C ATOM 632 O ARG A 79 32.842 103.579 21.961 1.00 31.29 O ANISOU 632 O ARG C 79 3566 3985 4336 -38 -572 162 O ATOM 633 CB ARG A 79 35.687 105.343 21.740 1.00 32.22 C ANISOU 633 CB ARG C 79 3725 4304 4213 -119 -311 -22 C ATOM 634 CG ARG A 79 34.649 106.439 21.529 1.00 34.29 C ANISOU 634 CG ARG C 79 4063 4312 4653 -168 -140 -19 C ATOM 635 CD ARG A 79 35.266 107.776 21.025 1.00 36.16 C ANISOU 635 CD ARG C 79 4248 4816 4673 31 -343 29 C ATOM 636 NE ARG A 79 36.331 108.361 21.859 1.00 39.78 N ANISOU 636 NE ARG C 79 5135 4956 5021 11 -222 -103 N ATOM 637 CZ ARG A 79 37.590 108.573 21.460 1.00 41.58 C ANISOU 637 CZ ARG C 79 5427 5094 5276 -40 -15 -35 C ATOM 638 NH1 ARG A 79 38.006 108.214 20.243 1.00 43.33 N ANISOU 638 NH1 ARG C 79 5753 5693 5017 -76 -19 -119 N ATOM 639 NH2 ARG A 79 38.455 109.147 22.284 1.00 40.84 N ANISOU 639 NH2 ARG C 79 5336 5286 4893 -130 -25 -165 N ATOM 640 N ASP A 80 34.429 102.693 20.652 1.00 29.32 N ANISOU 640 N ASP C 80 3328 3861 3948 -97 -408 -119 N ATOM 641 CA ASP A 80 33.503 102.085 19.742 1.00 30.36 C ANISOU 641 CA ASP C 80 3590 3889 4057 -10 -287 -90 C ATOM 642 C ASP A 80 32.731 100.906 20.363 1.00 30.50 C ANISOU 642 C ASP C 80 3641 3802 4143 15 -338 -163 C ATOM 643 O ASP A 80 31.504 100.817 20.227 1.00 28.52 O ANISOU 643 O ASP C 80 3240 3717 3877 159 -591 -293 O ATOM 644 CB ASP A 80 34.262 101.691 18.490 1.00 28.80 C ANISOU 644 CB ASP C 80 3455 3607 3878 -8 -302 -57 C ATOM 645 CG ASP A 80 34.709 102.919 17.679 1.00 30.21 C ANISOU 645 CG ASP C 80 3837 3795 3847 97 -1 192 C ATOM 646 OD1 ASP A 80 34.477 104.061 18.146 1.00 33.90 O ANISOU 646 OD1 ASP C 80 3801 4288 4791 78 -375 -395 O ATOM 647 OD2 ASP A 80 35.280 102.735 16.590 1.00 26.26 O ANISOU 647 OD2 ASP C 80 3598 4338 2040 702 -1034 -276 O ATOM 648 N MET A 81 33.431 100.026 21.079 1.00 31.14 N ANISOU 648 N MET C 81 3644 3992 4194 42 -315 -254 N ATOM 649 CA MET A 81 32.754 98.919 21.741 1.00 31.12 C ANISOU 649 CA MET C 81 3804 3919 4101 44 -280 -110 C ATOM 650 C MET A 81 31.689 99.472 22.641 1.00 30.65 C ANISOU 650 C MET C 81 3708 3881 4055 -84 -352 -168 C ATOM 651 O MET A 81 30.531 99.033 22.558 1.00 29.73 O ANISOU 651 O MET C 81 3489 3639 4166 -272 -482 -225 O ATOM 652 CB MET A 81 33.740 98.026 22.521 1.00 30.49 C ANISOU 652 CB MET C 81 3592 3904 4085 58 -283 -48 C ATOM 653 CG MET A 81 34.697 97.242 21.623 1.00 29.12 C ANISOU 653 CG MET C 81 3677 3626 3759 -88 -417 -90 C ATOM 654 SD MET A 81 33.919 96.007 20.542 1.00 33.44 S ANISOU 654 SD MET C 81 4151 4088 4464 -140 -651 -319 S ATOM 655 CE MET A 81 33.752 94.612 21.653 1.00 31.64 C ANISOU 655 CE MET C 81 4078 3820 4123 16 -295 -55 C ATOM 656 N GLN A 82 32.056 100.461 23.456 1.00 31.90 N ANISOU 656 N GLN C 82 3897 3969 4251 -69 -360 -136 N ATOM 657 CA GLN A 82 31.218 100.921 24.548 1.00 34.40 C ANISOU 657 CA GLN C 82 4244 4339 4485 -67 -176 -18 C ATOM 658 C GLN A 82 29.988 101.651 24.020 1.00 36.74 C ANISOU 658 C GLN C 82 4580 4526 4854 -122 -164 -3 C ATOM 659 O GLN A 82 28.974 101.726 24.711 1.00 37.76 O ANISOU 659 O GLN C 82 4710 4471 5163 -250 -240 -64 O ATOM 660 CB GLN A 82 32.000 101.821 25.506 1.00 35.06 C ANISOU 660 CB GLN C 82 4371 4411 4536 -90 -196 -40 C ATOM 661 CG GLN A 82 33.188 101.133 26.214 1.00 34.60 C ANISOU 661 CG GLN C 82 4133 4419 4593 -193 -142 -122 C ATOM 662 CD GLN A 82 33.716 101.900 27.427 1.00 35.28 C ANISOU 662 CD GLN C 82 4303 4516 4586 -85 -97 1 C ATOM 663 OE1 GLN A 82 33.749 103.145 27.447 1.00 33.96 O ANISOU 663 OE1 GLN C 82 4024 4286 4592 -63 -262 -63 O ATOM 664 NE2 GLN A 82 34.148 101.155 28.453 1.00 36.40 N ANISOU 664 NE2 GLN C 82 4300 4568 4961 -264 -167 -28 N ATOM 665 N SER A 83 30.107 102.187 22.806 1.00 37.45 N ANISOU 665 N SER C 83 4747 4648 4833 -135 -134 -137 N ATOM 666 CA SER A 83 29.020 102.891 22.133 1.00 37.90 C ANISOU 666 CA SER C 83 4780 4678 4942 -77 -127 -90 C ATOM 667 C SER A 83 28.002 101.911 21.527 1.00 39.28 C ANISOU 667 C SER C 83 4910 4855 5161 -14 -52 -92 C ATOM 668 O SER A 83 26.835 102.277 21.303 1.00 40.55 O ANISOU 668 O SER C 83 5001 4874 5529 86 -121 -115 O ATOM 669 CB SER A 83 29.583 103.789 21.038 1.00 38.41 C ANISOU 669 CB SER C 83 4840 4731 5021 -79 -135 -59 C ATOM 670 OG SER A 83 29.888 103.047 19.870 1.00 40.76 O ANISOU 670 OG SER C 83 4954 5030 5502 -2 -67 -164 O ATOM 671 N ARG A 84 28.450 100.684 21.256 1.00 38.65 N ANISOU 671 N ARG C 84 4877 4784 5022 -37 -50 -55 N ATOM 672 CA ARG A 84 27.565 99.587 20.854 1.00 38.51 C ANISOU 672 CA ARG C 84 4851 4744 5035 -21 -118 -57 C ATOM 673 C ARG A 84 27.068 98.816 22.076 1.00 36.72 C ANISOU 673 C ARG C 84 4638 4500 4813 -81 -76 -83 C ATOM 674 O ARG A 84 26.456 97.756 21.942 1.00 36.53 O ANISOU 674 O ARG C 84 4762 4202 4914 -49 -307 30 O ATOM 675 CB ARG A 84 28.283 98.640 19.899 1.00 37.98 C ANISOU 675 CB ARG C 84 4781 4712 4936 58 11 -84 C ATOM 676 CG ARG A 84 28.515 99.212 18.530 1.00 43.42 C ANISOU 676 CG ARG C 84 5567 5361 5570 25 -264 -71 C ATOM 677 CD ARG A 84 29.581 98.425 17.756 1.00 44.60 C ANISOU 677 CD ARG C 84 5679 5640 5626 -49 -61 108 C ATOM 678 NE ARG A 84 29.031 97.457 16.799 1.00 51.66 N ANISOU 678 NE ARG C 84 6518 6615 6493 29 224 -108 N ATOM 679 CZ ARG A 84 29.770 96.687 15.993 1.00 51.30 C ANISOU 679 CZ ARG C 84 6479 6549 6463 -124 240 92 C ATOM 680 NH1 ARG A 84 31.106 96.754 16.033 1.00 53.95 N ANISOU 680 NH1 ARG C 84 6973 6698 6825 113 27 -23 N ATOM 681 NH2 ARG A 84 29.178 95.839 15.141 1.00 51.91 N ANISOU 681 NH2 ARG C 84 6731 6525 6467 -1 157 41 N ATOM 682 N GLY A 85 27.318 99.345 23.267 1.00 35.54 N ANISOU 682 N GLY C 85 4510 4235 4756 -184 -145 -11 N ATOM 683 CA GLY A 85 26.891 98.681 24.489 1.00 35.78 C ANISOU 683 CA GLY C 85 4498 4291 4805 -140 -138 -37 C ATOM 684 C GLY A 85 27.654 97.385 24.754 1.00 35.75 C ANISOU 684 C GLY C 85 4417 4247 4919 -124 -246 27 C ATOM 685 O GLY A 85 27.128 96.470 25.383 1.00 36.46 O ANISOU 685 O GLY C 85 4728 4056 5069 -218 -527 -37 O ATOM 686 N LEU A 86 28.890 97.306 24.265 1.00 34.48 N ANISOU 686 N LEU C 86 4211 4090 4798 -138 -219 -62 N ATOM 687 CA LEU A 86 29.705 96.101 24.434 1.00 33.05 C ANISOU 687 CA LEU C 86 4064 4061 4431 -11 -159 -82 C ATOM 688 C LEU A 86 30.864 96.387 25.413 1.00 32.59 C ANISOU 688 C LEU C 86 3990 4042 4350 -15 -146 -151 C ATOM 689 O LEU A 86 31.323 97.520 25.533 1.00 32.82 O ANISOU 689 O LEU C 86 3980 4047 4442 -50 -261 -307 O ATOM 690 CB LEU A 86 30.220 95.636 23.078 1.00 31.57 C ANISOU 690 CB LEU C 86 3726 4001 4268 84 -129 -25 C ATOM 691 CG LEU A 86 29.164 95.301 22.028 1.00 31.88 C ANISOU 691 CG LEU C 86 3890 3971 4249 130 -284 75 C ATOM 692 CD1 LEU A 86 29.806 94.840 20.727 1.00 32.26 C ANISOU 692 CD1 LEU C 86 4019 3914 4323 87 -107 -59 C ATOM 693 CD2 LEU A 86 28.210 94.200 22.557 1.00 31.15 C ANISOU 693 CD2 LEU C 86 3830 3575 4429 61 -40 13 C ATOM 694 N ILE A 87 31.301 95.349 26.124 1.00 31.46 N ANISOU 694 N ILE C 87 3915 3926 4110 -17 -159 -186 N ATOM 695 CA ILE A 87 32.441 95.436 27.035 1.00 30.66 C ANISOU 695 CA ILE C 87 3736 3859 4052 -12 -146 -37 C ATOM 696 C ILE A 87 33.703 95.730 26.247 1.00 27.65 C ANISOU 696 C ILE C 87 3234 3581 3692 -132 -214 -125 C ATOM 697 O ILE A 87 33.909 95.187 25.172 1.00 25.66 O ANISOU 697 O ILE C 87 2712 3443 3594 -378 -470 -293 O ATOM 698 CB ILE A 87 32.607 94.093 27.827 1.00 31.01 C ANISOU 698 CB ILE C 87 3935 3904 3940 -47 -164 -57 C ATOM 699 CG1 ILE A 87 31.592 94.049 28.980 1.00 31.39 C ANISOU 699 CG1 ILE C 87 3919 4044 3962 72 -202 39 C ATOM 700 CG2 ILE A 87 33.987 93.947 28.412 1.00 32.10 C ANISOU 700 CG2 ILE C 87 3991 3960 4244 -39 -151 -117 C ATOM 701 CD1 ILE A 87 31.077 92.705 29.234 1.00 32.06 C ANISOU 701 CD1 ILE C 87 4007 4161 4012 -1 -91 45 C ATOM 702 N ALA A 88 34.535 96.600 26.806 1.00 27.71 N ANISOU 702 N ALA C 88 3178 3495 3854 -134 -340 -91 N ATOM 703 CA ALA A 88 35.876 96.889 26.277 1.00 27.62 C ANISOU 703 CA ALA C 88 3250 3524 3718 -108 -131 15 C ATOM 704 C ALA A 88 36.906 96.280 27.224 1.00 25.86 C ANISOU 704 C ALA C 88 3019 3311 3493 -54 -120 -25 C ATOM 705 O ALA A 88 36.969 96.638 28.389 1.00 26.42 O ANISOU 705 O ALA C 88 2862 3440 3734 -217 -219 -163 O ATOM 706 CB ALA A 88 36.106 98.391 26.168 1.00 28.33 C ANISOU 706 CB ALA C 88 3273 3565 3926 -66 -216 160 C ATOM 707 N SER A 89 37.700 95.365 26.693 1.00 25.72 N ANISOU 707 N SER C 89 2935 3282 3555 -9 -186 -72 N ATOM 708 CA SER A 89 38.689 94.611 27.444 1.00 25.15 C ANISOU 708 CA SER C 89 3055 3199 3300 -9 -137 -69 C ATOM 709 C SER A 89 39.980 94.679 26.623 1.00 24.25 C ANISOU 709 C SER C 89 2879 3164 3170 2 -173 -44 C ATOM 710 O SER A 89 40.029 94.170 25.506 1.00 21.04 O ANISOU 710 O SER C 89 2647 2955 2392 -81 -655 -119 O ATOM 711 CB SER A 89 38.206 93.156 27.591 1.00 24.66 C ANISOU 711 CB SER C 89 2884 3153 3332 -2 -339 -144 C ATOM 712 OG SER A 89 39.164 92.285 28.227 1.00 23.96 O ANISOU 712 OG SER C 89 2539 2574 3990 -118 -436 -318 O ATOM 713 N ILE A 90 41.008 95.323 27.174 1.00 24.22 N ANISOU 713 N ILE C 90 2932 3006 3263 -111 -258 -94 N ATOM 714 CA ILE A 90 42.215 95.605 26.393 1.00 25.69 C ANISOU 714 CA ILE C 90 3188 3099 3471 -52 -137 -80 C ATOM 715 C ILE A 90 43.442 95.102 27.142 1.00 24.91 C ANISOU 715 C ILE C 90 3054 3108 3301 -120 -175 -126 C ATOM 716 O ILE A 90 43.312 94.691 28.271 1.00 26.28 O ANISOU 716 O ILE C 90 3167 3268 3548 -18 -25 -164 O ATOM 717 CB ILE A 90 42.375 97.108 26.116 1.00 24.76 C ANISOU 717 CB ILE C 90 3150 2922 3334 -111 -247 -85 C ATOM 718 CG1 ILE A 90 42.478 97.891 27.444 1.00 25.94 C ANISOU 718 CG1 ILE C 90 2938 3363 3554 -117 -169 -52 C ATOM 719 CG2 ILE A 90 41.221 97.613 25.205 1.00 24.92 C ANISOU 719 CG2 ILE C 90 3181 2847 3437 50 -275 -121 C ATOM 720 CD1 ILE A 90 43.254 99.184 27.377 1.00 26.87 C ANISOU 720 CD1 ILE C 90 3472 3293 3442 71 -122 -57 C ATOM 721 N SER A 91 44.601 95.149 26.478 1.00 26.23 N ANISOU 721 N SER C 91 3046 3252 3666 -112 -249 -77 N ATOM 722 CA SER A 91 45.893 94.808 27.068 1.00 25.83 C ANISOU 722 CA SER C 91 3171 3199 3442 -5 -76 -51 C ATOM 723 C SER A 91 46.800 96.040 27.131 1.00 26.70 C ANISOU 723 C SER C 91 3234 3442 3465 42 -46 -111 C ATOM 724 O SER A 91 46.752 96.908 26.256 1.00 26.51 O ANISOU 724 O SER C 91 3051 3248 3773 93 -75 -265 O ATOM 725 CB SER A 91 46.583 93.698 26.238 1.00 25.77 C ANISOU 725 CB SER C 91 3156 3241 3392 15 -76 -131 C ATOM 726 OG SER A 91 45.798 92.532 26.206 1.00 25.64 O ANISOU 726 OG SER C 91 2897 3352 3492 -2 -170 -48 O ATOM 727 N VAL A 92 47.619 96.114 28.175 1.00 26.61 N ANISOU 727 N VAL C 92 3178 3419 3512 -23 -89 -140 N ATOM 728 CA VAL A 92 48.653 97.151 28.294 1.00 26.92 C ANISOU 728 CA VAL C 92 3340 3437 3448 26 -69 -103 C ATOM 729 C VAL A 92 49.973 96.540 28.752 1.00 27.60 C ANISOU 729 C VAL C 92 3381 3491 3612 56 -62 -136 C ATOM 730 O VAL A 92 49.997 95.430 29.298 1.00 26.02 O ANISOU 730 O VAL C 92 3635 3311 2938 113 -498 -403 O ATOM 731 CB VAL A 92 48.260 98.266 29.286 1.00 26.52 C ANISOU 731 CB VAL C 92 3280 3418 3377 33 -23 -30 C ATOM 732 CG1 VAL A 92 46.934 98.871 28.921 1.00 28.52 C ANISOU 732 CG1 VAL C 92 3590 3655 3591 23 80 -125 C ATOM 733 CG2 VAL A 92 48.195 97.752 30.718 1.00 27.44 C ANISOU 733 CG2 VAL C 92 3350 3475 3600 89 -125 -68 C ATOM 734 N GLY A 93 51.056 97.274 28.515 1.00 28.18 N ANISOU 734 N GLY C 93 3483 3563 3659 54 -112 80 N ATOM 735 CA GLY A 93 52.388 96.929 29.003 1.00 28.93 C ANISOU 735 CA GLY C 93 3599 3591 3801 32 -129 -20 C ATOM 736 C GLY A 93 52.762 97.790 30.192 1.00 29.37 C ANISOU 736 C GLY C 93 3638 3673 3847 71 -55 10 C ATOM 737 O GLY A 93 51.883 98.312 30.916 1.00 31.21 O ANISOU 737 O GLY C 93 3800 3686 4371 244 33 -58 O ATOM 738 N VAL A 94 54.063 97.955 30.418 1.00 29.12 N ANISOU 738 N VAL C 94 3600 3702 3760 61 -166 89 N ATOM 739 CA VAL A 94 54.526 98.666 31.608 1.00 31.43 C ANISOU 739 CA VAL C 94 3868 3942 4129 78 -73 -71 C ATOM 740 C VAL A 94 55.531 99.806 31.346 1.00 33.20 C ANISOU 740 C VAL C 94 4065 4127 4422 98 -60 -72 C ATOM 741 O VAL A 94 55.988 100.443 32.299 1.00 33.22 O ANISOU 741 O VAL C 94 4112 3970 4538 160 -33 -192 O ATOM 742 CB VAL A 94 55.105 97.683 32.680 1.00 30.99 C ANISOU 742 CB VAL C 94 3872 3908 3993 137 -81 -89 C ATOM 743 CG1 VAL A 94 54.092 96.566 32.992 1.00 28.50 C ANISOU 743 CG1 VAL C 94 3496 3656 3673 -58 -324 -360 C ATOM 744 CG2 VAL A 94 56.423 97.099 32.244 1.00 31.21 C ANISOU 744 CG2 VAL C 94 3612 4077 4167 97 11 -98 C ATOM 745 N LYS A 95 55.833 100.048 30.072 1.00 33.92 N ANISOU 745 N LYS C 95 4212 4232 4443 100 -145 -18 N ATOM 746 CA LYS A 95 56.721 101.139 29.628 1.00 36.55 C ANISOU 746 CA LYS C 95 4550 4563 4772 137 -98 -19 C ATOM 747 C LYS A 95 56.124 102.548 29.802 1.00 36.92 C ANISOU 747 C LYS C 95 4518 4589 4920 123 -131 -4 C ATOM 748 O LYS A 95 54.908 102.733 29.986 1.00 34.43 O ANISOU 748 O LYS C 95 4056 4173 4850 382 -278 -128 O ATOM 749 CB LYS A 95 57.095 100.942 28.160 1.00 36.94 C ANISOU 749 CB LYS C 95 4690 4556 4788 146 -54 98 C ATOM 750 CG LYS A 95 58.211 99.929 27.911 1.00 41.84 C ANISOU 750 CG LYS C 95 5209 5296 5391 -45 47 -14 C ATOM 751 CD LYS A 95 58.541 99.810 26.403 1.00 41.16 C ANISOU 751 CD LYS C 95 5272 5256 5110 -2 13 53 C ATOM 752 CE LYS A 95 59.245 101.078 25.856 1.00 47.18 C ANISOU 752 CE LYS C 95 5921 6082 5922 138 -120 37 C ATOM 753 NZ LYS A 95 59.040 101.311 24.375 1.00 49.12 N ANISOU 753 NZ LYS C 95 6359 6516 5789 44 -138 96 N ATOM 754 N GLU A 96 57.008 103.550 29.720 1.00 38.03 N ANISOU 754 N GLU C 96 4751 4690 5008 143 -91 -20 N ATOM 755 CA GLU A 96 56.633 104.917 30.034 1.00 38.58 C ANISOU 755 CA GLU C 96 4775 4836 5048 141 -69 0 C ATOM 756 C GLU A 96 55.472 105.412 29.172 1.00 37.83 C ANISOU 756 C GLU C 96 4560 4736 5074 195 -56 33 C ATOM 757 O GLU A 96 54.581 106.098 29.679 1.00 39.57 O ANISOU 757 O GLU C 96 4639 4855 5540 195 -25 80 O ATOM 758 CB GLU A 96 57.846 105.845 29.919 1.00 39.20 C ANISOU 758 CB GLU C 96 4896 4927 5070 159 -51 -14 C ATOM 759 CG GLU A 96 57.604 107.274 30.364 1.00 39.41 C ANISOU 759 CG GLU C 96 4930 5008 5032 136 -71 13 C ATOM 760 CD GLU A 96 58.884 108.112 30.261 1.00 43.05 C ANISOU 760 CD GLU C 96 5260 5390 5704 289 17 -15 C ATOM 761 OE1 GLU A 96 59.703 108.095 31.219 1.00 49.74 O ANISOU 761 OE1 GLU C 96 6531 6281 6085 127 -73 -240 O ATOM 762 OE2 GLU A 96 59.073 108.771 29.208 1.00 50.47 O ANISOU 762 OE2 GLU C 96 6200 6690 6285 272 -272 22 O ATOM 763 N ASP A 97 55.455 105.041 27.898 1.00 35.62 N ANISOU 763 N ASP C 97 4325 4506 4704 206 -211 94 N ATOM 764 CA ASP A 97 54.346 105.414 27.026 1.00 37.06 C ANISOU 764 CA ASP C 97 4559 4646 4876 110 -145 65 C ATOM 765 C ASP A 97 52.989 104.818 27.433 1.00 36.76 C ANISOU 765 C ASP C 97 4517 4610 4838 106 -237 20 C ATOM 766 O ASP A 97 51.937 105.405 27.124 1.00 35.31 O ANISOU 766 O ASP C 97 4224 4549 4640 163 -382 59 O ATOM 767 CB ASP A 97 54.648 105.061 25.576 1.00 37.48 C ANISOU 767 CB ASP C 97 4770 4697 4771 8 -99 11 C ATOM 768 CG ASP A 97 54.940 103.595 25.385 1.00 44.31 C ANISOU 768 CG ASP C 97 5321 5738 5774 83 17 15 C ATOM 769 OD1 ASP A 97 55.119 102.866 26.396 1.00 48.74 O ANISOU 769 OD1 ASP C 97 6386 6519 5613 144 -72 -89 O ATOM 770 OD2 ASP A 97 55.020 103.162 24.216 1.00 50.54 O ANISOU 770 OD2 ASP C 97 6713 6598 5889 234 121 -20 O ATOM 771 N GLU A 98 53.006 103.672 28.130 1.00 36.09 N ANISOU 771 N GLU C 98 4330 4495 4885 83 -143 -26 N ATOM 772 CA GLU A 98 51.756 103.089 28.649 1.00 35.61 C ANISOU 772 CA GLU C 98 4361 4530 4639 35 -123 23 C ATOM 773 C GLU A 98 51.226 103.870 29.847 1.00 35.41 C ANISOU 773 C GLU C 98 4267 4529 4656 43 -120 -18 C ATOM 774 O GLU A 98 50.010 103.931 30.055 1.00 34.18 O ANISOU 774 O GLU C 98 3935 4534 4518 266 -52 66 O ATOM 775 CB GLU A 98 51.935 101.614 29.004 1.00 34.75 C ANISOU 775 CB GLU C 98 4274 4351 4579 46 -72 53 C ATOM 776 CG GLU A 98 52.322 100.744 27.846 1.00 31.24 C ANISOU 776 CG GLU C 98 3883 3847 4137 24 -155 -14 C ATOM 777 CD GLU A 98 51.222 100.552 26.823 1.00 34.71 C ANISOU 777 CD GLU C 98 4261 4140 4785 121 -196 -115 C ATOM 778 OE1 GLU A 98 50.503 99.540 26.906 1.00 32.94 O ANISOU 778 OE1 GLU C 98 3799 3858 4857 1 -392 -288 O ATOM 779 OE2 GLU A 98 51.092 101.390 25.900 1.00 37.19 O ANISOU 779 OE2 GLU C 98 4564 4386 5177 232 -411 -230 O ATOM 780 N TYR A 99 52.123 104.482 30.624 1.00 36.22 N ANISOU 780 N TYR C 99 4446 4540 4773 16 -106 -40 N ATOM 781 CA TYR A 99 51.711 105.451 31.635 1.00 37.02 C ANISOU 781 CA TYR C 99 4656 4670 4737 44 -39 -36 C ATOM 782 C TYR A 99 50.955 106.633 31.021 1.00 37.46 C ANISOU 782 C TYR C 99 4595 4739 4898 18 -17 18 C ATOM 783 O TYR A 99 49.951 107.084 31.573 1.00 36.43 O ANISOU 783 O TYR C 99 4323 4558 4960 -18 72 -16 O ATOM 784 CB TYR A 99 52.913 105.951 32.427 1.00 33.30 C ANISOU 784 CB TYR C 99 4020 4511 4119 -143 -546 -196 C ATOM 785 CG TYR A 99 53.371 104.962 33.459 1.00 36.66 C ANISOU 785 CG TYR C 99 4839 4424 4663 79 131 -223 C ATOM 786 CD1 TYR A 99 54.142 103.860 33.105 1.00 35.38 C ANISOU 786 CD1 TYR C 99 4594 4482 4366 -51 12 -50 C ATOM 787 CD2 TYR A 99 53.020 105.113 34.798 1.00 34.43 C ANISOU 787 CD2 TYR C 99 4482 4270 4327 54 -127 120 C ATOM 788 CE1 TYR A 99 54.577 102.947 34.063 1.00 35.84 C ANISOU 788 CE1 TYR C 99 4541 4503 4571 65 103 87 C ATOM 789 CE2 TYR A 99 53.444 104.186 35.764 1.00 36.58 C ANISOU 789 CE2 TYR C 99 4740 4328 4829 -72 82 -152 C ATOM 790 CZ TYR A 99 54.211 103.105 35.383 1.00 35.08 C ANISOU 790 CZ TYR C 99 4473 4441 4415 165 217 -171 C ATOM 791 OH TYR A 99 54.635 102.188 36.327 1.00 35.92 O ANISOU 791 OH TYR C 99 4460 4568 4618 242 37 -280 O ATOM 792 N GLU A 100 51.414 107.089 29.859 1.00 38.34 N ANISOU 792 N GLU C 100 4796 4854 4915 49 -88 -9 N ATOM 793 CA GLU A 100 50.788 108.220 29.166 1.00 39.05 C ANISOU 793 CA GLU C 100 4879 4924 5034 38 -69 -39 C ATOM 794 C GLU A 100 49.435 107.787 28.643 1.00 38.96 C ANISOU 794 C GLU C 100 4819 4875 5107 51 -66 6 C ATOM 795 O GLU A 100 48.467 108.547 28.710 1.00 39.37 O ANISOU 795 O GLU C 100 4628 4940 5391 133 -171 -6 O ATOM 796 CB GLU A 100 51.625 108.692 27.957 1.00 40.88 C ANISOU 796 CB GLU C 100 5211 5238 5083 26 -94 24 C ATOM 797 CG GLU A 100 53.158 108.800 28.168 1.00 46.96 C ANISOU 797 CG GLU C 100 6139 5656 6044 -52 -10 42 C ATOM 798 CD GLU A 100 53.647 110.130 28.737 1.00 54.11 C ANISOU 798 CD GLU C 100 6653 6894 7009 181 127 -22 C ATOM 799 OE1 GLU A 100 52.844 110.897 29.328 1.00 58.83 O ANISOU 799 OE1 GLU C 100 7322 7447 7582 -108 76 80 O ATOM 800 OE2 GLU A 100 54.866 110.397 28.596 1.00 57.09 O ANISOU 800 OE2 GLU C 100 7234 7025 7432 128 75 3 O ATOM 801 N PHE A 101 49.387 106.558 28.117 1.00 38.29 N ANISOU 801 N PHE C 101 4782 4827 4938 27 -26 -87 N ATOM 802 CA PHE A 101 48.186 105.993 27.480 1.00 38.43 C ANISOU 802 CA PHE C 101 4685 4897 5017 35 -55 -52 C ATOM 803 C PHE A 101 47.049 105.973 28.447 1.00 37.62 C ANISOU 803 C PHE C 101 4499 4803 4992 85 -36 -75 C ATOM 804 O PHE A 101 45.927 106.376 28.130 1.00 38.03 O ANISOU 804 O PHE C 101 4286 4966 5196 150 -158 -160 O ATOM 805 CB PHE A 101 48.486 104.583 26.949 1.00 34.66 C ANISOU 805 CB PHE C 101 4275 4056 4838 516 2 -248 C ATOM 806 CG PHE A 101 47.263 103.773 26.574 1.00 38.05 C ANISOU 806 CG PHE C 101 4807 4809 4840 -3 -119 -53 C ATOM 807 CD1 PHE A 101 46.540 104.055 25.413 1.00 38.49 C ANISOU 807 CD1 PHE C 101 5044 4677 4900 46 126 -169 C ATOM 808 CD2 PHE A 101 46.861 102.699 27.370 1.00 34.07 C ANISOU 808 CD2 PHE C 101 4273 4154 4515 -61 -126 -199 C ATOM 809 CE1 PHE A 101 45.424 103.281 25.062 1.00 38.87 C ANISOU 809 CE1 PHE C 101 4794 4820 5152 -13 -107 -24 C ATOM 810 CE2 PHE A 101 45.755 101.916 27.026 1.00 35.37 C ANISOU 810 CE2 PHE C 101 4372 4545 4522 -81 -230 16 C ATOM 811 CZ PHE A 101 45.030 102.208 25.874 1.00 36.43 C ANISOU 811 CZ PHE C 101 4762 4608 4471 162 -85 -109 C ATOM 812 N VAL A 102 47.355 105.490 29.639 1.00 37.44 N ANISOU 812 N VAL C 102 4517 4717 4991 48 40 -101 N ATOM 813 CA VAL A 102 46.422 105.436 30.728 1.00 38.76 C ANISOU 813 CA VAL C 102 4741 4861 5123 76 6 -47 C ATOM 814 C VAL A 102 45.950 106.836 31.117 1.00 40.27 C ANISOU 814 C VAL C 102 4825 5035 5439 18 -68 -36 C ATOM 815 O VAL A 102 44.750 107.064 31.328 1.00 40.55 O ANISOU 815 O VAL C 102 4750 5065 5593 66 -182 -47 O ATOM 816 CB VAL A 102 47.075 104.692 31.911 1.00 37.84 C ANISOU 816 CB VAL C 102 4595 4765 5015 43 56 -46 C ATOM 817 CG1 VAL A 102 46.328 104.913 33.227 1.00 36.92 C ANISOU 817 CG1 VAL C 102 4462 4661 4903 121 115 -98 C ATOM 818 CG2 VAL A 102 47.174 103.187 31.568 1.00 34.42 C ANISOU 818 CG2 VAL C 102 4219 4477 4379 40 -80 -56 C ATOM 819 N GLN A 103 46.889 107.779 31.198 1.00 40.82 N ANISOU 819 N GLN C 103 4887 5108 5513 11 0 -119 N ATOM 820 CA GLN A 103 46.529 109.154 31.546 1.00 42.00 C ANISOU 820 CA GLN C 103 5091 5309 5557 43 32 -14 C ATOM 821 C GLN A 103 45.612 109.730 30.468 1.00 42.65 C ANISOU 821 C GLN C 103 5149 5397 5657 57 -7 9 C ATOM 822 O GLN A 103 44.608 110.384 30.764 1.00 44.17 O ANISOU 822 O GLN C 103 5242 5489 6049 116 -47 24 O ATOM 823 CB GLN A 103 47.789 109.990 31.752 1.00 41.46 C ANISOU 823 CB GLN C 103 5031 5213 5506 14 65 7 C ATOM 824 CG GLN A 103 48.540 109.552 33.001 1.00 43.00 C ANISOU 824 CG GLN C 103 5351 5370 5615 30 -44 -38 C ATOM 825 CD GLN A 103 49.854 110.288 33.192 1.00 43.99 C ANISOU 825 CD GLN C 103 5395 5489 5829 85 39 -38 C ATOM 826 OE1 GLN A 103 49.851 111.487 33.404 1.00 48.94 O ANISOU 826 OE1 GLN C 103 5726 6452 6414 104 382 26 O ATOM 827 NE2 GLN A 103 50.977 109.577 33.101 1.00 44.09 N ANISOU 827 NE2 GLN C 103 5352 5453 5947 -14 15 -203 N ATOM 828 N GLN A 104 45.945 109.453 29.221 1.00 42.86 N ANISOU 828 N GLN C 104 5233 5449 5600 97 -12 10 N ATOM 829 CA GLN A 104 45.093 109.800 28.109 1.00 43.57 C ANISOU 829 CA GLN C 104 5355 5528 5671 46 -37 -9 C ATOM 830 C GLN A 104 43.662 109.338 28.315 1.00 44.23 C ANISOU 830 C GLN C 104 5428 5597 5781 38 -107 -49 C ATOM 831 O GLN A 104 42.718 110.082 28.084 1.00 43.90 O ANISOU 831 O GLN C 104 5153 5518 6008 78 -227 -24 O ATOM 832 CB GLN A 104 45.634 109.163 26.850 1.00 43.75 C ANISOU 832 CB GLN C 104 5458 5532 5631 5 40 -56 C ATOM 833 CG GLN A 104 45.255 109.860 25.589 1.00 44.49 C ANISOU 833 CG GLN C 104 5551 5698 5652 40 -26 -25 C ATOM 834 CD GLN A 104 45.979 109.274 24.393 1.00 46.77 C ANISOU 834 CD GLN C 104 5889 5963 5917 56 70 135 C ATOM 835 OE1 GLN A 104 46.849 108.429 24.548 1.00 52.29 O ANISOU 835 OE1 GLN C 104 6508 6647 6709 -188 -127 -68 O ATOM 836 NE2 GLN A 104 45.618 109.720 23.205 1.00 51.95 N ANISOU 836 NE2 GLN C 104 6780 6508 6449 -92 -66 -140 N ATOM 837 N LEU A 105 43.506 108.087 28.717 1.00 43.78 N ANISOU 837 N LEU C 105 5402 5570 5660 32 -124 -35 N ATOM 838 CA LEU A 105 42.191 107.505 28.858 1.00 44.90 C ANISOU 838 CA LEU C 105 5522 5692 5845 61 -99 30 C ATOM 839 C LEU A 105 41.442 108.283 29.935 1.00 45.35 C ANISOU 839 C LEU C 105 5515 5824 5891 62 -84 29 C ATOM 840 O LEU A 105 40.248 108.524 29.829 1.00 44.98 O ANISOU 840 O LEU C 105 5349 5883 5859 24 -88 12 O ATOM 841 CB LEU A 105 42.310 106.023 29.242 1.00 44.86 C ANISOU 841 CB LEU C 105 5543 5661 5837 22 -37 9 C ATOM 842 CG LEU A 105 42.623 105.032 28.120 1.00 43.27 C ANISOU 842 CG LEU C 105 5248 5584 5607 19 -81 -36 C ATOM 843 CD1 LEU A 105 42.829 103.626 28.639 1.00 40.27 C ANISOU 843 CD1 LEU C 105 5118 5085 5097 3 -65 -131 C ATOM 844 CD2 LEU A 105 41.565 105.055 27.044 1.00 42.86 C ANISOU 844 CD2 LEU C 105 5214 5397 5675 -15 -49 3 C ATOM 845 N ALA A 106 42.161 108.687 30.970 1.00 46.49 N ANISOU 845 N ALA C 106 5702 5984 5977 77 -70 30 N ATOM 846 CA ALA A 106 41.524 109.256 32.140 1.00 48.43 C ANISOU 846 CA ALA C 106 6049 6182 6169 56 -7 39 C ATOM 847 C ALA A 106 40.950 110.621 31.820 1.00 51.47 C ANISOU 847 C ALA C 106 6392 6569 6592 -1 -6 25 C ATOM 848 O ALA A 106 40.183 111.169 32.592 1.00 53.20 O ANISOU 848 O ALA C 106 6583 6830 6798 1 104 21 O ATOM 849 CB ALA A 106 42.497 109.343 33.291 1.00 48.83 C ANISOU 849 CB ALA C 106 6110 6185 6258 9 -17 14 C ATOM 850 N ALA A 107 41.335 111.155 30.667 1.00 53.46 N ANISOU 850 N ALA C 107 6619 6893 6798 -15 -36 0 N ATOM 851 CA ALA A 107 41.194 112.574 30.394 1.00 54.77 C ANISOU 851 CA ALA C 107 6852 6995 6963 17 -10 16 C ATOM 852 C ALA A 107 40.044 112.722 29.435 1.00 55.91 C ANISOU 852 C ALA C 107 6927 7130 7187 36 -37 -27 C ATOM 853 O ALA A 107 39.283 113.670 29.503 1.00 56.85 O ANISOU 853 O ALA C 107 7064 7138 7397 87 -27 -27 O ATOM 854 CB ALA A 107 42.443 113.106 29.775 1.00 55.26 C ANISOU 854 CB ALA C 107 6893 7078 7024 60 12 -17 C ATOM 855 N GLU A 108 39.919 111.746 28.546 1.00 56.20 N ANISOU 855 N GLU C 108 7022 7116 7213 48 -44 -55 N ATOM 856 CA GLU A 108 38.678 111.526 27.835 1.00 55.93 C ANISOU 856 CA GLU C 108 7021 7106 7121 22 -38 1 C ATOM 857 C GLU A 108 37.653 110.730 28.589 1.00 54.57 C ANISOU 857 C GLU C 108 6696 7028 7008 -49 -30 -50 C ATOM 858 O GLU A 108 36.639 110.350 28.032 1.00 53.66 O ANISOU 858 O GLU C 108 6320 7058 7009 -79 3 -76 O ATOM 859 CB GLU A 108 38.944 110.862 26.518 1.00 56.80 C ANISOU 859 CB GLU C 108 7141 7226 7213 -32 13 15 C ATOM 860 CG GLU A 108 40.323 111.136 25.997 1.00 56.87 C ANISOU 860 CG GLU C 108 7079 7251 7277 -4 -23 -28 C ATOM 861 CD GLU A 108 40.418 110.722 24.568 1.00 58.55 C ANISOU 861 CD GLU C 108 7479 7455 7310 -24 35 19 C ATOM 862 OE1 GLU A 108 40.110 109.556 24.303 1.00 62.28 O ANISOU 862 OE1 GLU C 108 7752 8095 7816 70 -64 134 O ATOM 863 OE2 GLU A 108 40.761 111.565 23.729 1.00 63.22 O ANISOU 863 OE2 GLU C 108 7897 8320 7801 -92 131 -35 O ATOM 864 N HIS A 109 37.902 110.492 29.862 1.00 53.45 N ANISOU 864 N HIS C 109 6577 6825 6906 -54 13 36 N ATOM 865 CA HIS A 109 36.962 109.729 30.641 1.00 52.53 C ANISOU 865 CA HIS C 109 6514 6694 6748 -53 57 -1 C ATOM 866 C HIS A 109 36.481 108.524 29.843 1.00 51.14 C ANISOU 866 C HIS C 109 6317 6426 6686 -56 -25 42 C ATOM 867 O HIS A 109 35.288 108.254 29.769 1.00 51.74 O ANISOU 867 O HIS C 109 6309 6494 6854 -127 -75 -43 O ATOM 868 CB HIS A 109 35.786 110.620 31.024 1.00 54.76 C ANISOU 868 CB HIS C 109 6915 6867 7022 -103 -43 41 C ATOM 869 CG HIS A 109 36.156 111.722 31.964 1.00 59.17 C ANISOU 869 CG HIS C 109 7378 7552 7552 -3 152 -37 C ATOM 870 ND1 HIS A 109 36.247 113.038 31.570 1.00 62.06 N ANISOU 870 ND1 HIS C 109 7588 7979 8010 95 35 -30 N ATOM 871 CD2 HIS A 109 36.488 111.698 33.275 1.00 61.85 C ANISOU 871 CD2 HIS C 109 7817 8008 7672 -16 -12 0 C ATOM 872 CE1 HIS A 109 36.605 113.779 32.601 1.00 63.03 C ANISOU 872 CE1 HIS C 109 7744 8145 8058 75 41 11 C ATOM 873 NE2 HIS A 109 36.761 112.990 33.647 1.00 63.38 N ANISOU 873 NE2 HIS C 109 7899 8193 7989 82 20 -29 N ATOM 874 N LEU A 110 37.425 107.801 29.248 1.00 48.16 N ANISOU 874 N LEU C 110 5923 6088 6287 38 -59 51 N ATOM 875 CA LEU A 110 37.212 106.415 28.885 1.00 45.84 C ANISOU 875 CA LEU C 110 5763 5770 5884 -9 -116 -2 C ATOM 876 C LEU A 110 37.747 105.460 29.943 1.00 44.02 C ANISOU 876 C LEU C 110 5477 5529 5720 4 -79 -6 C ATOM 877 O LEU A 110 38.915 105.497 30.290 1.00 44.34 O ANISOU 877 O LEU C 110 5391 5583 5871 -55 -145 -86 O ATOM 878 CB LEU A 110 37.872 106.110 27.560 1.00 45.64 C ANISOU 878 CB LEU C 110 5733 5810 5797 35 -14 -70 C ATOM 879 CG LEU A 110 37.287 106.810 26.355 1.00 45.72 C ANISOU 879 CG LEU C 110 5680 5792 5897 -30 -125 -61 C ATOM 880 CD1 LEU A 110 38.068 106.404 25.157 1.00 45.76 C ANISOU 880 CD1 LEU C 110 5619 5762 6004 -48 -39 -17 C ATOM 881 CD2 LEU A 110 35.845 106.392 26.215 1.00 46.63 C ANISOU 881 CD2 LEU C 110 5732 5842 6143 -36 -186 -25 C ATOM 882 N THR A 111 36.864 104.620 30.455 1.00 41.27 N ANISOU 882 N THR C 111 5063 5215 5403 -46 -43 -67 N ATOM 883 CA THR A 111 37.245 103.556 31.372 1.00 39.18 C ANISOU 883 CA THR C 111 4808 4919 5159 -16 97 -11 C ATOM 884 C THR A 111 36.865 102.198 30.762 1.00 36.93 C ANISOU 884 C THR C 111 4422 4540 5070 -44 54 31 C ATOM 885 O THR A 111 35.674 101.872 30.677 1.00 35.44 O ANISOU 885 O THR C 111 3964 4364 5135 -120 48 208 O ATOM 886 CB THR A 111 36.602 103.745 32.737 1.00 39.68 C ANISOU 886 CB THR C 111 4934 4950 5192 -22 43 -1 C ATOM 887 OG1 THR A 111 37.045 104.988 33.288 1.00 41.29 O ANISOU 887 OG1 THR C 111 5027 5153 5507 -76 -9 -72 O ATOM 888 CG2 THR A 111 37.012 102.641 33.678 1.00 40.48 C ANISOU 888 CG2 THR C 111 5024 5124 5232 -40 -34 38 C ATOM 889 N PRO A 112 37.882 101.420 30.301 1.00 34.58 N ANISOU 889 N PRO C 112 4175 4287 4675 25 63 13 N ATOM 890 CA PRO A 112 37.582 100.069 29.774 1.00 32.42 C ANISOU 890 CA PRO C 112 4008 4017 4293 -30 -106 -4 C ATOM 891 C PRO A 112 37.141 99.192 30.946 1.00 30.34 C ANISOU 891 C PRO C 112 3608 3770 4149 -106 -86 -107 C ATOM 892 O PRO A 112 37.600 99.404 32.057 1.00 28.74 O ANISOU 892 O PRO C 112 3182 3683 4052 -172 -121 -97 O ATOM 893 CB PRO A 112 38.906 99.606 29.127 1.00 32.42 C ANISOU 893 CB PRO C 112 3935 4171 4212 -56 -126 -104 C ATOM 894 CG PRO A 112 39.956 100.549 29.579 1.00 33.28 C ANISOU 894 CG PRO C 112 4163 4131 4350 -53 -43 0 C ATOM 895 CD PRO A 112 39.323 101.736 30.276 1.00 33.90 C ANISOU 895 CD PRO C 112 4123 4255 4502 -46 14 23 C ATOM 896 N GLU A 113 36.210 98.261 30.707 1.00 28.50 N ANISOU 896 N GLU C 113 3413 3476 3939 -247 -219 -106 N ATOM 897 CA GLU A 113 35.692 97.447 31.786 1.00 26.74 C ANISOU 897 CA GLU C 113 3307 3231 3622 -201 -91 -120 C ATOM 898 C GLU A 113 36.849 96.598 32.368 1.00 24.24 C ANISOU 898 C GLU C 113 2947 3077 3186 -149 -118 -133 C ATOM 899 O GLU A 113 36.876 96.295 33.570 1.00 24.81 O ANISOU 899 O GLU C 113 3055 3022 3347 -232 116 -201 O ATOM 900 CB GLU A 113 34.600 96.528 31.254 1.00 28.02 C ANISOU 900 CB GLU C 113 3540 3394 3712 -175 -152 -184 C ATOM 901 CG GLU A 113 33.194 97.183 31.126 1.00 26.90 C ANISOU 901 CG GLU C 113 3284 3139 3797 -153 -108 -115 C ATOM 902 CD GLU A 113 33.026 98.095 29.906 1.00 30.97 C ANISOU 902 CD GLU C 113 3953 3946 3867 3 -156 -37 C ATOM 903 OE1 GLU A 113 33.961 98.272 29.092 1.00 29.29 O ANISOU 903 OE1 GLU C 113 3509 3186 4434 -308 -289 -166 O ATOM 904 OE2 GLU A 113 31.906 98.637 29.763 1.00 37.29 O ANISOU 904 OE2 GLU C 113 4418 4548 5202 -377 -170 -61 O ATOM 905 N TYR A 114 37.740 96.190 31.476 1.00 23.52 N ANISOU 905 N TYR C 114 2826 3018 3089 -180 -181 -123 N ATOM 906 CA TYR A 114 38.857 95.278 31.768 1.00 22.61 C ANISOU 906 CA TYR C 114 2920 2894 2774 -117 -89 -94 C ATOM 907 C TYR A 114 40.175 95.756 31.159 1.00 22.91 C ANISOU 907 C TYR C 114 2712 3038 2954 41 -113 -130 C ATOM 908 O TYR A 114 40.269 96.031 29.942 1.00 20.81 O ANISOU 908 O TYR C 114 2356 2756 2791 117 -199 201 O ATOM 909 CB TYR A 114 38.560 93.840 31.281 1.00 22.60 C ANISOU 909 CB TYR C 114 2870 2964 2750 -189 -188 -193 C ATOM 910 CG TYR A 114 37.353 93.206 31.919 1.00 23.18 C ANISOU 910 CG TYR C 114 2962 2954 2888 19 22 -136 C ATOM 911 CD1 TYR A 114 37.448 92.546 33.149 1.00 22.86 C ANISOU 911 CD1 TYR C 114 2898 2951 2835 -192 -257 115 C ATOM 912 CD2 TYR A 114 36.100 93.316 31.341 1.00 26.60 C ANISOU 912 CD2 TYR C 114 2987 3168 3952 -180 -298 -140 C ATOM 913 CE1 TYR A 114 36.308 91.990 33.768 1.00 23.67 C ANISOU 913 CE1 TYR C 114 2626 3162 3206 154 -85 -152 C ATOM 914 CE2 TYR A 114 34.964 92.745 31.951 1.00 25.69 C ANISOU 914 CE2 TYR C 114 3415 2976 3369 -216 -116 144 C ATOM 915 CZ TYR A 114 35.077 92.100 33.163 1.00 26.00 C ANISOU 915 CZ TYR C 114 2942 3140 3795 -106 -239 60 C ATOM 916 OH TYR A 114 33.945 91.567 33.762 1.00 26.26 O ANISOU 916 OH TYR C 114 3205 2970 3802 -13 -20 170 O ATOM 917 N ILE A 115 41.207 95.800 32.011 1.00 23.30 N ANISOU 917 N ILE C 115 2562 2998 3290 25 5 -87 N ATOM 918 CA ILE A 115 42.567 96.000 31.526 1.00 23.11 C ANISOU 918 CA ILE C 115 2807 2919 3053 -81 -63 2 C ATOM 919 C ILE A 115 43.483 94.850 31.995 1.00 22.75 C ANISOU 919 C ILE C 115 2710 3050 2884 -38 -119 -65 C ATOM 920 O ILE A 115 43.595 94.578 33.198 1.00 21.17 O ANISOU 920 O ILE C 115 2230 3089 2725 -4 -217 -251 O ATOM 921 CB ILE A 115 43.167 97.324 32.009 1.00 23.53 C ANISOU 921 CB ILE C 115 2801 2938 3200 -39 -35 25 C ATOM 922 CG1 ILE A 115 42.298 98.514 31.597 1.00 23.87 C ANISOU 922 CG1 ILE C 115 2960 2831 3277 36 14 24 C ATOM 923 CG2 ILE A 115 44.614 97.509 31.473 1.00 24.16 C ANISOU 923 CG2 ILE C 115 2798 3078 3303 48 -64 13 C ATOM 924 CD1 ILE A 115 42.696 99.824 32.355 1.00 25.78 C ANISOU 924 CD1 ILE C 115 3004 3340 3450 -47 -30 -13 C ATOM 925 N THR A 116 44.145 94.225 31.034 1.00 20.55 N ANISOU 925 N THR C 116 2540 2839 2426 -116 -21 -65 N ATOM 926 CA THR A 116 45.142 93.179 31.280 1.00 22.07 C ANISOU 926 CA THR C 116 2788 2877 2719 -45 -48 -72 C ATOM 927 C THR A 116 46.574 93.691 31.049 1.00 20.73 C ANISOU 927 C THR C 116 2632 2688 2555 30 -69 5 C ATOM 928 O THR A 116 46.975 94.050 29.941 1.00 20.58 O ANISOU 928 O THR C 116 2556 2750 2512 91 -163 -4 O ATOM 929 CB THR A 116 44.863 91.923 30.412 1.00 19.35 C ANISOU 929 CB THR C 116 2628 2597 2126 -27 -121 -243 C ATOM 930 OG1 THR A 116 43.585 91.398 30.764 1.00 20.38 O ANISOU 930 OG1 THR C 116 2715 2707 2320 4 -488 -100 O ATOM 931 CG2 THR A 116 45.904 90.820 30.582 1.00 19.33 C ANISOU 931 CG2 THR C 116 2651 2600 2094 -18 198 -22 C ATOM 932 N ILE A 117 47.343 93.700 32.121 1.00 20.52 N ANISOU 932 N ILE C 117 2532 2815 2450 -9 -67 -51 N ATOM 933 CA ILE A 117 48.760 94.014 32.059 1.00 22.89 C ANISOU 933 CA ILE C 117 2970 2950 2777 50 -29 -91 C ATOM 934 C ILE A 117 49.490 92.741 31.624 1.00 23.37 C ANISOU 934 C ILE C 117 3051 2906 2920 17 -41 -80 C ATOM 935 O ILE A 117 49.518 91.761 32.362 1.00 23.30 O ANISOU 935 O ILE C 117 3097 2522 3231 -56 -151 -207 O ATOM 936 CB ILE A 117 49.296 94.465 33.446 1.00 21.81 C ANISOU 936 CB ILE C 117 2994 2862 2430 -63 -74 -31 C ATOM 937 CG1 ILE A 117 48.546 95.702 33.945 1.00 23.84 C ANISOU 937 CG1 ILE C 117 2968 3363 2728 118 -79 -135 C ATOM 938 CG2 ILE A 117 50.825 94.675 33.369 1.00 20.89 C ANISOU 938 CG2 ILE C 117 2672 2817 2448 177 -280 -160 C ATOM 939 CD1 ILE A 117 48.887 96.046 35.411 1.00 23.38 C ANISOU 939 CD1 ILE C 117 2854 3201 2827 49 139 -3 C ATOM 940 N ASP A 118 50.061 92.715 30.426 1.00 24.96 N ANISOU 940 N ASP C 118 3221 3067 3193 39 -80 -1 N ATOM 941 CA AASP A 118 50.509 91.458 29.847 0.50 26.06 C ANISOU 941 CA AASP C 118 3354 3254 3290 -2 22 4 C ATOM 942 C ASP A 118 52.032 91.436 29.610 1.00 26.24 C ANISOU 942 C ASP C 118 3398 3222 3349 3 -28 -51 C ATOM 943 O ASP A 118 52.496 91.960 28.638 1.00 24.45 O ANISOU 943 O ASP C 118 3529 2783 2976 -112 -211 -102 O ATOM 944 CB AASP A 118 49.587 91.125 28.625 0.50 27.89 C ANISOU 944 CB AASP C 118 3719 3408 3470 -41 44 -115 C ATOM 945 CG AASP A 118 50.315 90.956 27.293 0.50 26.07 C ANISOU 945 CG AASP C 118 3362 2978 3564 12 -72 22 C ATOM 946 OD1AASP A 118 50.742 89.841 26.986 0.50 25.19 O ANISOU 946 OD1AASP C 118 2953 2953 3662 36 -380 -164 O ATOM 947 OD2AASP A 118 50.358 91.897 26.481 0.50 26.53 O ANISOU 947 OD2AASP C 118 3165 2701 4214 97 -258 -268 O ATOM 948 N ILE A 119 52.763 90.825 30.546 1.00 27.26 N ANISOU 948 N ILE C 119 3300 3465 3590 -23 -89 10 N ATOM 949 CA ILE A 119 54.216 90.787 30.578 1.00 27.01 C ANISOU 949 CA ILE C 119 3374 3415 3471 -51 -71 36 C ATOM 950 C ILE A 119 54.678 89.315 30.824 1.00 27.05 C ANISOU 950 C ILE C 119 3295 3413 3568 -28 -76 156 C ATOM 951 O ILE A 119 54.044 88.566 31.592 1.00 26.64 O ANISOU 951 O ILE C 119 3376 3159 3585 -52 -116 286 O ATOM 952 CB ILE A 119 54.699 91.778 31.708 1.00 28.32 C ANISOU 952 CB ILE C 119 3400 3584 3775 23 -46 -26 C ATOM 953 CG1 ILE A 119 54.417 93.246 31.322 1.00 28.06 C ANISOU 953 CG1 ILE C 119 3518 3623 3520 28 -133 99 C ATOM 954 CG2 ILE A 119 56.120 91.588 32.090 1.00 28.18 C ANISOU 954 CG2 ILE C 119 3378 3420 3907 -128 -175 87 C ATOM 955 CD1 ILE A 119 54.967 93.632 29.946 1.00 31.23 C ANISOU 955 CD1 ILE C 119 4103 4029 3733 51 -124 112 C ATOM 956 N ALA A 120 55.755 88.897 30.157 1.00 25.79 N ANISOU 956 N ALA C 120 3203 3171 3425 56 -73 123 N ATOM 957 CA ALA A 120 56.227 87.511 30.260 1.00 25.05 C ANISOU 957 CA ALA C 120 3190 3114 3212 111 -79 47 C ATOM 958 C ALA A 120 56.540 87.155 31.698 1.00 24.32 C ANISOU 958 C ALA C 120 3093 3046 3101 152 -97 9 C ATOM 959 O ALA A 120 56.096 86.127 32.185 1.00 26.28 O ANISOU 959 O ALA C 120 2935 3419 3628 256 -81 -113 O ATOM 960 CB ALA A 120 57.450 87.269 29.420 1.00 25.31 C ANISOU 960 CB ALA C 120 3328 3301 2987 122 -61 88 C ATOM 961 N HIS A 121 57.319 87.999 32.363 1.00 22.77 N ANISOU 961 N HIS C 121 2795 2845 3010 39 -116 -14 N ATOM 962 CA HIS A 121 57.747 87.770 33.745 1.00 23.05 C ANISOU 962 CA HIS C 121 2924 2906 2925 89 -77 88 C ATOM 963 C HIS A 121 57.106 88.867 34.622 1.00 23.26 C ANISOU 963 C HIS C 121 2911 2915 3011 118 -25 4 C ATOM 964 O HIS A 121 57.702 89.904 34.947 1.00 22.06 O ANISOU 964 O HIS C 121 2784 3024 2572 219 62 7 O ATOM 965 CB HIS A 121 59.286 87.711 33.865 1.00 22.80 C ANISOU 965 CB HIS C 121 2819 3043 2801 -8 -104 -18 C ATOM 966 CG HIS A 121 59.762 87.312 35.228 1.00 21.32 C ANISOU 966 CG HIS C 121 2656 2649 2796 -163 -153 -51 C ATOM 967 ND1 HIS A 121 61.082 87.415 35.627 1.00 24.35 N ANISOU 967 ND1 HIS C 121 3138 3006 3107 1 -52 179 N ATOM 968 CD2 HIS A 121 59.074 86.875 36.314 1.00 15.02 C ANISOU 968 CD2 HIS C 121 1741 1787 2177 -73 373 -65 C ATOM 969 CE1 HIS A 121 61.193 86.994 36.877 1.00 18.62 C ANISOU 969 CE1 HIS C 121 2363 2184 2526 13 2 -288 C ATOM 970 NE2 HIS A 121 59.987 86.674 37.318 1.00 20.20 N ANISOU 970 NE2 HIS C 121 2468 2875 2332 -343 -187 32 N ATOM 971 N GLY A 122 55.859 88.619 34.986 1.00 21.55 N ANISOU 971 N GLY C 122 2883 2654 2648 115 -153 159 N ATOM 972 CA GLY A 122 54.997 89.660 35.527 1.00 22.32 C ANISOU 972 CA GLY C 122 2726 2878 2874 71 -40 0 C ATOM 973 C GLY A 122 55.167 89.921 37.016 1.00 23.88 C ANISOU 973 C GLY C 122 2949 3098 3026 -9 63 -86 C ATOM 974 O GLY A 122 54.644 90.924 37.517 1.00 23.95 O ANISOU 974 O GLY C 122 2923 2977 3197 -125 62 -300 O ATOM 975 N HIS A 123 55.854 89.020 37.736 1.00 23.95 N ANISOU 975 N HIS C 123 2915 3004 3178 -36 13 -75 N ATOM 976 CA HIS A 123 56.227 89.275 39.135 1.00 24.81 C ANISOU 976 CA HIS C 123 3136 3138 3152 -28 -5 19 C ATOM 977 C HIS A 123 57.389 90.293 39.104 1.00 26.13 C ANISOU 977 C HIS C 123 3387 3207 3332 2 -27 -5 C ATOM 978 O HIS A 123 58.548 89.913 39.008 1.00 26.91 O ANISOU 978 O HIS C 123 3687 3150 3386 -99 -331 -52 O ATOM 979 CB HIS A 123 56.611 87.969 39.879 1.00 23.25 C ANISOU 979 CB HIS C 123 3063 2655 3115 -16 25 96 C ATOM 980 CG HIS A 123 56.740 88.112 41.365 1.00 24.25 C ANISOU 980 CG HIS C 123 2999 2820 3391 -77 26 -135 C ATOM 981 ND1 HIS A 123 57.340 87.155 42.162 1.00 24.97 N ANISOU 981 ND1 HIS C 123 3198 3204 3085 9 -38 34 N ATOM 982 CD2 HIS A 123 56.349 89.103 42.201 1.00 23.40 C ANISOU 982 CD2 HIS C 123 3003 2839 3047 208 -33 131 C ATOM 983 CE1 HIS A 123 57.327 87.562 43.415 1.00 24.71 C ANISOU 983 CE1 HIS C 123 3059 2900 3427 30 132 -43 C ATOM 984 NE2 HIS A 123 56.723 88.736 43.466 1.00 25.21 N ANISOU 984 NE2 HIS C 123 2820 3275 3482 88 -127 -236 N ATOM 985 N SER A 124 57.054 91.585 39.115 1.00 28.21 N ANISOU 985 N SER C 124 3549 3541 3628 -45 -22 -54 N ATOM 986 CA SER A 124 58.052 92.682 39.022 1.00 28.99 C ANISOU 986 CA SER C 124 3644 3618 3750 75 -16 -46 C ATOM 987 C SER A 124 57.517 94.008 39.556 1.00 30.47 C ANISOU 987 C SER C 124 3664 3796 4117 125 -37 -119 C ATOM 988 O SER A 124 56.299 94.243 39.619 1.00 29.18 O ANISOU 988 O SER C 124 3399 3514 4174 343 41 -183 O ATOM 989 CB SER A 124 58.484 92.899 37.575 1.00 31.00 C ANISOU 989 CB SER C 124 3951 3868 3959 -40 -53 -20 C ATOM 990 OG SER A 124 57.459 93.540 36.834 1.00 33.98 O ANISOU 990 OG SER C 124 4185 4391 4335 -81 -288 -214 O ATOM 991 N ASN A 125 58.422 94.918 39.921 1.00 31.16 N ANISOU 991 N ASN C 125 3856 3797 4183 79 14 -226 N ATOM 992 CA ASN A 125 57.948 96.232 40.374 1.00 31.40 C ANISOU 992 CA ASN C 125 3906 3894 4129 140 54 -99 C ATOM 993 C ASN A 125 57.381 97.050 39.229 1.00 30.70 C ANISOU 993 C ASN C 125 3797 3708 4160 231 55 -100 C ATOM 994 O ASN A 125 56.543 97.932 39.452 1.00 32.07 O ANISOU 994 O ASN C 125 3961 3715 4508 241 82 -229 O ATOM 995 CB ASN A 125 59.037 96.967 41.141 1.00 33.26 C ANISOU 995 CB ASN C 125 4178 4048 4411 142 59 -191 C ATOM 996 CG ASN A 125 59.290 96.326 42.487 1.00 39.58 C ANISOU 996 CG ASN C 125 5256 5078 4705 99 -20 -75 C ATOM 997 OD1 ASN A 125 58.422 96.348 43.372 1.00 40.87 O ANISOU 997 OD1 ASN C 125 5424 4899 5203 252 276 50 O ATOM 998 ND2 ASN A 125 60.455 95.678 42.630 1.00 45.34 N ANISOU 998 ND2 ASN C 125 5822 5592 5814 -207 84 -127 N ATOM 999 N ALA A 126 57.806 96.714 38.006 1.00 29.89 N ANISOU 999 N ALA C 126 3815 3511 4030 300 -36 -70 N ATOM 1000 CA ALA A 126 57.265 97.327 36.789 1.00 29.92 C ANISOU 1000 CA ALA C 126 3734 3630 4002 140 -52 0 C ATOM 1001 C ALA A 126 55.768 97.080 36.707 1.00 29.34 C ANISOU 1001 C ALA C 126 3550 3603 3993 98 -125 -45 C ATOM 1002 O ALA A 126 55.007 97.994 36.459 1.00 28.50 O ANISOU 1002 O ALA C 126 3199 3643 3984 199 -391 130 O ATOM 1003 CB ALA A 126 57.935 96.760 35.568 1.00 30.67 C ANISOU 1003 CB ALA C 126 3952 3622 4076 193 -13 8 C ATOM 1004 N VAL A 127 55.358 95.834 36.952 1.00 28.80 N ANISOU 1004 N VAL C 127 3407 3616 3918 105 -93 -99 N ATOM 1005 CA VAL A 127 53.936 95.462 36.959 1.00 28.43 C ANISOU 1005 CA VAL C 127 3356 3575 3871 104 -47 -3 C ATOM 1006 C VAL A 127 53.218 96.054 38.178 1.00 28.15 C ANISOU 1006 C VAL C 127 3214 3647 3832 178 26 -41 C ATOM 1007 O VAL A 127 52.104 96.581 38.052 1.00 27.84 O ANISOU 1007 O VAL C 127 3160 3636 3781 166 155 -176 O ATOM 1008 CB VAL A 127 53.749 93.906 36.898 1.00 26.50 C ANISOU 1008 CB VAL C 127 3131 3365 3573 63 -110 30 C ATOM 1009 CG1 VAL A 127 52.265 93.499 37.169 1.00 25.18 C ANISOU 1009 CG1 VAL C 127 3004 3267 3296 -35 139 -95 C ATOM 1010 CG2 VAL A 127 54.197 93.368 35.586 1.00 24.52 C ANISOU 1010 CG2 VAL C 127 2816 3090 3409 28 -240 -149 C ATOM 1011 N ILE A 128 53.851 95.994 39.348 1.00 29.46 N ANISOU 1011 N ILE C 128 3392 3828 3973 75 -46 -62 N ATOM 1012 CA ILE A 128 53.265 96.562 40.565 1.00 30.69 C ANISOU 1012 CA ILE C 128 3755 3886 4017 76 -26 5 C ATOM 1013 C ILE A 128 52.936 98.076 40.410 1.00 30.92 C ANISOU 1013 C ILE C 128 3634 3934 4180 145 60 74 C ATOM 1014 O ILE A 128 51.838 98.531 40.758 1.00 31.21 O ANISOU 1014 O ILE C 128 3397 3933 4526 332 91 -94 O ATOM 1015 CB ILE A 128 54.163 96.269 41.816 1.00 31.14 C ANISOU 1015 CB ILE C 128 3855 3975 4001 71 -79 27 C ATOM 1016 CG1 ILE A 128 54.056 94.785 42.204 1.00 32.78 C ANISOU 1016 CG1 ILE C 128 4092 4041 4322 90 66 -114 C ATOM 1017 CG2 ILE A 128 53.781 97.162 43.003 1.00 31.53 C ANISOU 1017 CG2 ILE C 128 3800 4138 4042 -1 15 8 C ATOM 1018 CD1 ILE A 128 55.322 94.154 42.653 1.00 31.10 C ANISOU 1018 CD1 ILE C 128 3823 4077 3917 77 -82 19 C ATOM 1019 N ASN A 129 53.868 98.835 39.845 1.00 32.57 N ANISOU 1019 N ASN C 129 3869 4114 4391 91 -43 69 N ATOM 1020 CA ASN A 129 53.676 100.271 39.642 1.00 32.50 C ANISOU 1020 CA ASN C 129 3893 4151 4305 89 28 27 C ATOM 1021 C ASN A 129 52.618 100.577 38.588 1.00 33.00 C ANISOU 1021 C ASN C 129 3913 4186 4437 89 83 -10 C ATOM 1022 O ASN A 129 51.846 101.523 38.732 1.00 34.71 O ANISOU 1022 O ASN C 129 3780 4559 4846 289 237 31 O ATOM 1023 CB ASN A 129 55.013 100.936 39.261 1.00 33.28 C ANISOU 1023 CB ASN C 129 4052 4160 4430 91 -85 115 C ATOM 1024 CG ASN A 129 56.026 100.923 40.403 1.00 36.33 C ANISOU 1024 CG ASN C 129 4518 4639 4644 162 33 -13 C ATOM 1025 OD1 ASN A 129 55.660 100.875 41.589 1.00 41.38 O ANISOU 1025 OD1 ASN C 129 5079 5625 5019 213 131 57 O ATOM 1026 ND2 ASN A 129 57.306 100.957 40.054 1.00 36.67 N ANISOU 1026 ND2 ASN C 129 4777 4577 4579 11 1 -137 N ATOM 1027 N MET A 130 52.550 99.769 37.530 1.00 32.84 N ANISOU 1027 N MET C 130 3971 4226 4279 -13 -21 -6 N ATOM 1028 CA MET A 130 51.465 99.916 36.561 1.00 31.93 C ANISOU 1028 CA MET C 130 3853 4116 4160 30 32 -24 C ATOM 1029 C MET A 130 50.079 99.611 37.168 1.00 31.45 C ANISOU 1029 C MET C 130 3702 4082 4165 24 39 -130 C ATOM 1030 O MET A 130 49.101 100.318 36.890 1.00 29.24 O ANISOU 1030 O MET C 130 3177 3789 4144 128 95 -317 O ATOM 1031 CB MET A 130 51.730 99.080 35.315 1.00 32.23 C ANISOU 1031 CB MET C 130 3839 4136 4269 64 -7 -33 C ATOM 1032 CG MET A 130 50.662 99.271 34.226 1.00 31.85 C ANISOU 1032 CG MET C 130 3719 4209 4173 -15 -123 -70 C ATOM 1033 SD MET A 130 50.387 101.010 33.790 1.00 35.23 S ANISOU 1033 SD MET C 130 3413 4940 5030 -27 -122 -172 S ATOM 1034 CE MET A 130 51.734 101.230 32.642 1.00 37.28 C ANISOU 1034 CE MET C 130 4464 4847 4854 -32 -30 -89 C ATOM 1035 N ILE A 131 49.981 98.597 38.025 1.00 30.98 N ANISOU 1035 N ILE C 131 3754 4000 4017 -25 2 -56 N ATOM 1036 CA ILE A 131 48.720 98.348 38.717 1.00 31.86 C ANISOU 1036 CA ILE C 131 3892 4070 4143 -32 38 -36 C ATOM 1037 C ILE A 131 48.296 99.610 39.487 1.00 33.56 C ANISOU 1037 C ILE C 131 4022 4286 4440 -129 102 -77 C ATOM 1038 O ILE A 131 47.148 100.049 39.379 1.00 33.47 O ANISOU 1038 O ILE C 131 3905 4261 4551 -200 24 15 O ATOM 1039 CB ILE A 131 48.795 97.146 39.694 1.00 30.98 C ANISOU 1039 CB ILE C 131 3808 3945 4016 20 89 -22 C ATOM 1040 CG1 ILE A 131 48.996 95.839 38.921 1.00 28.79 C ANISOU 1040 CG1 ILE C 131 3456 3578 3904 88 43 100 C ATOM 1041 CG2 ILE A 131 47.516 97.047 40.503 1.00 30.16 C ANISOU 1041 CG2 ILE C 131 3714 3957 3789 -25 84 -12 C ATOM 1042 CD1 ILE A 131 49.516 94.695 39.757 1.00 29.44 C ANISOU 1042 CD1 ILE C 131 3658 3684 3841 89 73 -39 C ATOM 1043 N GLN A 132 49.230 100.162 40.262 1.00 34.59 N ANISOU 1043 N GLN C 132 4077 4360 4702 -67 95 -52 N ATOM 1044 CA GLN A 132 48.973 101.331 41.122 1.00 35.28 C ANISOU 1044 CA GLN C 132 4364 4531 4507 17 150 -14 C ATOM 1045 C GLN A 132 48.620 102.588 40.322 1.00 34.85 C ANISOU 1045 C GLN C 132 4153 4534 4552 101 154 7 C ATOM 1046 O GLN A 132 47.723 103.348 40.708 1.00 35.53 O ANISOU 1046 O GLN C 132 4180 4685 4633 192 112 54 O ATOM 1047 CB GLN A 132 50.170 101.559 42.043 1.00 35.75 C ANISOU 1047 CB GLN C 132 4477 4525 4580 2 132 14 C ATOM 1048 CG GLN A 132 50.233 100.520 43.160 1.00 39.21 C ANISOU 1048 CG GLN C 132 4899 4946 5051 -29 -71 -42 C ATOM 1049 CD GLN A 132 51.551 100.511 43.910 1.00 40.26 C ANISOU 1049 CD GLN C 132 5233 5092 4970 -52 116 -122 C ATOM 1050 OE1 GLN A 132 52.291 101.496 43.901 1.00 48.73 O ANISOU 1050 OE1 GLN C 132 6007 6234 6271 320 -17 -117 O ATOM 1051 NE2 GLN A 132 51.858 99.388 44.563 1.00 49.39 N ANISOU 1051 NE2 GLN C 132 5963 6652 6151 -19 -196 -74 N ATOM 1052 N HIS A 133 49.287 102.769 39.185 1.00 35.53 N ANISOU 1052 N HIS C 133 4191 4640 4669 96 130 -17 N ATOM 1053 CA HIS A 133 48.982 103.847 38.231 1.00 35.71 C ANISOU 1053 CA HIS C 133 4294 4617 4657 45 110 -79 C ATOM 1054 C HIS A 133 47.588 103.716 37.628 1.00 36.78 C ANISOU 1054 C HIS C 133 4306 4671 4995 34 77 -9 C ATOM 1055 O HIS A 133 46.832 104.701 37.560 1.00 36.71 O ANISOU 1055 O HIS C 133 3937 4857 5152 94 113 40 O ATOM 1056 CB HIS A 133 50.035 103.853 37.123 1.00 34.82 C ANISOU 1056 CB HIS C 133 4247 4470 4513 19 89 -64 C ATOM 1057 CG HIS A 133 49.854 104.917 36.086 1.00 36.51 C ANISOU 1057 CG HIS C 133 4375 4777 4720 29 97 -101 C ATOM 1058 ND1 HIS A 133 49.822 106.264 36.391 1.00 37.34 N ANISOU 1058 ND1 HIS C 133 4424 4899 4864 20 91 -108 N ATOM 1059 CD2 HIS A 133 49.767 104.837 34.736 1.00 36.51 C ANISOU 1059 CD2 HIS C 133 4466 4747 4659 31 64 42 C ATOM 1060 CE1 HIS A 133 49.689 106.962 35.276 1.00 38.12 C ANISOU 1060 CE1 HIS C 133 4602 4951 4928 58 8 -63 C ATOM 1061 NE2 HIS A 133 49.658 106.121 34.256 1.00 39.25 N ANISOU 1061 NE2 HIS C 133 4739 5083 5089 -88 94 -61 N ATOM 1062 N ILE A 134 47.245 102.504 37.173 1.00 35.87 N ANISOU 1062 N ILE C 134 4142 4643 4843 7 54 -74 N ATOM 1063 CA ILE A 134 45.922 102.249 36.618 1.00 36.44 C ANISOU 1063 CA ILE C 134 4286 4688 4872 56 78 -74 C ATOM 1064 C ILE A 134 44.822 102.516 37.635 1.00 35.60 C ANISOU 1064 C ILE C 134 4095 4647 4784 94 176 -87 C ATOM 1065 O ILE A 134 43.821 103.131 37.291 1.00 36.45 O ANISOU 1065 O ILE C 134 3998 4901 4947 92 204 -151 O ATOM 1066 CB ILE A 134 45.777 100.800 36.060 1.00 35.23 C ANISOU 1066 CB ILE C 134 4153 4544 4688 -4 134 -39 C ATOM 1067 CG1 ILE A 134 46.572 100.654 34.754 1.00 35.53 C ANISOU 1067 CG1 ILE C 134 4352 4482 4666 108 60 -32 C ATOM 1068 CG2 ILE A 134 44.308 100.475 35.802 1.00 35.48 C ANISOU 1068 CG2 ILE C 134 4048 4624 4807 48 -21 2 C ATOM 1069 CD1 ILE A 134 46.676 99.229 34.264 1.00 36.52 C ANISOU 1069 CD1 ILE C 134 4424 4654 4795 -31 40 15 C ATOM 1070 N LYS A 135 44.999 102.041 38.868 1.00 36.70 N ANISOU 1070 N LYS C 135 4245 4780 4917 75 150 -119 N ATOM 1071 CA LYS A 135 43.991 102.169 39.901 1.00 39.00 C ANISOU 1071 CA LYS C 135 4775 4940 5104 37 72 -4 C ATOM 1072 C LYS A 135 43.802 103.619 40.358 1.00 41.26 C ANISOU 1072 C LYS C 135 4993 5223 5458 30 100 31 C ATOM 1073 O LYS A 135 42.752 103.973 40.925 1.00 42.22 O ANISOU 1073 O LYS C 135 5081 5419 5540 74 229 53 O ATOM 1074 CB LYS A 135 44.346 101.297 41.109 1.00 39.25 C ANISOU 1074 CB LYS C 135 4826 4955 5129 25 69 -37 C ATOM 1075 CG LYS A 135 44.032 99.812 40.917 1.00 39.24 C ANISOU 1075 CG LYS C 135 4789 5015 5106 -24 117 -37 C ATOM 1076 CD LYS A 135 42.537 99.517 41.125 1.00 41.44 C ANISOU 1076 CD LYS C 135 5065 5251 5429 -85 130 138 C ATOM 1077 CE LYS A 135 42.060 98.208 40.467 1.00 40.73 C ANISOU 1077 CE LYS C 135 5072 5089 5311 89 110 0 C ATOM 1078 NZ LYS A 135 40.583 98.174 40.216 1.00 39.73 N ANISOU 1078 NZ LYS C 135 4639 4957 5498 -90 33 71 N ATOM 1079 N LYS A 136 44.815 104.450 40.123 1.00 42.05 N ANISOU 1079 N LYS C 136 5119 5300 5557 28 67 24 N ATOM 1080 CA LYS A 136 44.717 105.883 40.424 1.00 42.50 C ANISOU 1080 CA LYS C 136 5203 5409 5536 15 55 16 C ATOM 1081 C LYS A 136 43.920 106.636 39.352 1.00 42.65 C ANISOU 1081 C LYS C 136 5263 5422 5519 15 37 32 C ATOM 1082 O LYS A 136 43.039 107.432 39.675 1.00 43.48 O ANISOU 1082 O LYS C 136 5371 5527 5623 -46 38 60 O ATOM 1083 CB LYS A 136 46.109 106.495 40.611 1.00 43.37 C ANISOU 1083 CB LYS C 136 5346 5507 5625 19 82 4 C ATOM 1084 CG LYS A 136 46.718 106.181 41.986 1.00 45.54 C ANISOU 1084 CG LYS C 136 5673 5810 5817 -2 48 -54 C ATOM 1085 CD LYS A 136 47.918 107.078 42.344 1.00 45.70 C ANISOU 1085 CD LYS C 136 5726 5731 5908 66 60 -37 C ATOM 1086 CE LYS A 136 49.170 106.784 41.500 1.00 49.79 C ANISOU 1086 CE LYS C 136 6335 6183 6399 -51 31 60 C ATOM 1087 NZ LYS A 136 49.992 105.632 41.985 1.00 49.79 N ANISOU 1087 NZ LYS C 136 6192 6377 6347 -11 -60 -57 N ATOM 1088 N HIS A 137 44.208 106.366 38.086 1.00 41.82 N ANISOU 1088 N HIS C 137 5155 5307 5425 17 108 8 N ATOM 1089 CA HIS A 137 43.623 107.120 36.980 1.00 41.48 C ANISOU 1089 CA HIS C 137 5064 5264 5430 17 44 -25 C ATOM 1090 C HIS A 137 42.336 106.529 36.392 1.00 41.42 C ANISOU 1090 C HIS C 137 5035 5284 5419 -29 20 -94 C ATOM 1091 O HIS A 137 41.551 107.260 35.778 1.00 41.24 O ANISOU 1091 O HIS C 137 4863 5303 5503 32 44 -160 O ATOM 1092 CB HIS A 137 44.663 107.310 35.884 1.00 43.18 C ANISOU 1092 CB HIS C 137 5288 5513 5605 -52 30 35 C ATOM 1093 CG HIS A 137 45.780 108.216 36.292 1.00 47.40 C ANISOU 1093 CG HIS C 137 5914 5878 6217 149 47 -73 C ATOM 1094 ND1 HIS A 137 46.616 107.929 37.352 1.00 48.08 N ANISOU 1094 ND1 HIS C 137 6128 5946 6195 59 -18 -32 N ATOM 1095 CD2 HIS A 137 46.174 109.422 35.814 1.00 48.62 C ANISOU 1095 CD2 HIS C 137 6084 6267 6121 105 -112 -66 C ATOM 1096 CE1 HIS A 137 47.488 108.912 37.496 1.00 48.78 C ANISOU 1096 CE1 HIS C 137 6134 6056 6344 37 37 -148 C ATOM 1097 NE2 HIS A 137 47.247 109.826 36.572 1.00 47.97 N ANISOU 1097 NE2 HIS C 137 5909 6051 6264 200 -45 -20 N ATOM 1098 N LEU A 138 42.124 105.223 36.574 1.00 40.00 N ANISOU 1098 N LEU C 138 4934 5046 5217 -21 -19 -82 N ATOM 1099 CA LEU A 138 40.950 104.529 36.045 1.00 38.90 C ANISOU 1099 CA LEU C 138 4845 4971 4961 -40 7 0 C ATOM 1100 C LEU A 138 40.411 103.586 37.120 1.00 38.38 C ANISOU 1100 C LEU C 138 4787 4955 4839 -46 67 27 C ATOM 1101 O LEU A 138 40.405 102.358 36.953 1.00 37.30 O ANISOU 1101 O LEU C 138 4648 4873 4648 -44 89 68 O ATOM 1102 CB LEU A 138 41.308 103.778 34.748 1.00 37.56 C ANISOU 1102 CB LEU C 138 4718 4758 4793 -84 44 -61 C ATOM 1103 CG LEU A 138 41.905 104.613 33.603 1.00 37.16 C ANISOU 1103 CG LEU C 138 4587 4566 4965 -72 34 -12 C ATOM 1104 CD1 LEU A 138 42.527 103.748 32.546 1.00 35.93 C ANISOU 1104 CD1 LEU C 138 4286 4672 4694 78 -87 -13 C ATOM 1105 CD2 LEU A 138 40.883 105.513 32.910 1.00 37.50 C ANISOU 1105 CD2 LEU C 138 4590 4608 5050 -61 38 -107 C ATOM 1106 N PRO A 139 39.935 104.159 38.243 1.00 38.78 N ANISOU 1106 N PRO C 139 4789 5050 4896 -20 62 54 N ATOM 1107 CA PRO A 139 39.547 103.312 39.366 1.00 37.82 C ANISOU 1107 CA PRO C 139 4674 4902 4794 -22 62 46 C ATOM 1108 C PRO A 139 38.467 102.254 39.070 1.00 37.08 C ANISOU 1108 C PRO C 139 4573 4826 4689 -70 109 49 C ATOM 1109 O PRO A 139 38.396 101.242 39.776 1.00 39.99 O ANISOU 1109 O PRO C 139 4648 5284 5260 -24 229 47 O ATOM 1110 CB PRO A 139 39.017 104.323 40.398 1.00 38.87 C ANISOU 1110 CB PRO C 139 4827 4993 4947 -15 126 40 C ATOM 1111 CG PRO A 139 39.625 105.628 40.005 1.00 38.97 C ANISOU 1111 CG PRO C 139 4852 5121 4833 -56 96 109 C ATOM 1112 CD PRO A 139 39.698 105.592 38.529 1.00 38.58 C ANISOU 1112 CD PRO C 139 4806 5112 4739 -17 45 69 C ATOM 1113 N GLU A 140 37.617 102.484 38.086 1.00 35.55 N ANISOU 1113 N GLU C 140 4246 4649 4610 -120 147 135 N ATOM 1114 CA GLU A 140 36.543 101.546 37.782 1.00 35.40 C ANISOU 1114 CA GLU C 140 4301 4564 4585 -79 97 98 C ATOM 1115 C GLU A 140 36.978 100.399 36.871 1.00 34.35 C ANISOU 1115 C GLU C 140 4148 4375 4526 -76 94 130 C ATOM 1116 O GLU A 140 36.175 99.486 36.625 1.00 33.75 O ANISOU 1116 O GLU C 140 3951 4370 4499 -75 177 344 O ATOM 1117 CB GLU A 140 35.368 102.259 37.111 1.00 37.14 C ANISOU 1117 CB GLU C 140 4436 4786 4888 -15 35 0 C ATOM 1118 CG GLU A 140 34.792 103.387 37.925 1.00 41.93 C ANISOU 1118 CG GLU C 140 5171 5254 5504 -182 228 131 C ATOM 1119 CD GLU A 140 34.251 102.893 39.225 1.00 48.35 C ANISOU 1119 CD GLU C 140 6084 6330 5954 -137 -19 180 C ATOM 1120 OE1 GLU A 140 33.127 102.335 39.223 1.00 54.44 O ANISOU 1120 OE1 GLU C 140 6706 6889 7089 145 161 34 O ATOM 1121 OE2 GLU A 140 34.952 103.054 40.245 1.00 52.88 O ANISOU 1121 OE2 GLU C 140 6797 6485 6808 -120 56 -179 O ATOM 1122 N SER A 141 38.204 100.452 36.338 1.00 32.68 N ANISOU 1122 N SER C 141 3848 4187 4381 -46 57 7 N ATOM 1123 CA SER A 141 38.689 99.377 35.449 1.00 30.60 C ANISOU 1123 CA SER C 141 3708 3939 3979 -50 -28 -22 C ATOM 1124 C SER A 141 39.057 98.109 36.231 1.00 28.97 C ANISOU 1124 C SER C 141 3467 3705 3831 -67 40 -38 C ATOM 1125 O SER A 141 39.739 98.183 37.264 1.00 28.95 O ANISOU 1125 O SER C 141 3424 3677 3898 -76 105 -29 O ATOM 1126 CB SER A 141 39.893 99.834 34.630 1.00 30.58 C ANISOU 1126 CB SER C 141 3697 3890 4032 23 -38 -107 C ATOM 1127 OG SER A 141 39.513 100.628 33.526 1.00 29.54 O ANISOU 1127 OG SER C 141 3676 3744 3805 152 -81 -211 O ATOM 1128 N PHE A 142 38.607 96.950 35.736 1.00 26.39 N ANISOU 1128 N PHE C 142 3193 3280 3553 -71 -44 -80 N ATOM 1129 CA PHE A 142 38.941 95.648 36.365 1.00 26.12 C ANISOU 1129 CA PHE C 142 3228 3252 3445 -16 -21 -5 C ATOM 1130 C PHE A 142 40.322 95.219 35.824 1.00 24.35 C ANISOU 1130 C PHE C 142 2848 3151 3250 -107 64 40 C ATOM 1131 O PHE A 142 40.487 95.011 34.611 1.00 25.61 O ANISOU 1131 O PHE C 142 3112 3259 3360 -30 -201 136 O ATOM 1132 CB PHE A 142 37.861 94.604 36.077 1.00 23.22 C ANISOU 1132 CB PHE C 142 2820 3043 2960 -75 5 3 C ATOM 1133 CG PHE A 142 38.054 93.296 36.803 1.00 25.33 C ANISOU 1133 CG PHE C 142 3125 3098 3400 -70 -7 29 C ATOM 1134 CD1 PHE A 142 37.284 92.982 37.928 1.00 24.63 C ANISOU 1134 CD1 PHE C 142 2853 3200 3304 -96 -256 -16 C ATOM 1135 CD2 PHE A 142 38.982 92.367 36.338 1.00 24.71 C ANISOU 1135 CD2 PHE C 142 2928 3056 3402 24 -60 159 C ATOM 1136 CE1 PHE A 142 37.447 91.769 38.592 1.00 24.18 C ANISOU 1136 CE1 PHE C 142 2762 2879 3544 23 -37 118 C ATOM 1137 CE2 PHE A 142 39.148 91.145 36.979 1.00 23.36 C ANISOU 1137 CE2 PHE C 142 2940 2899 3033 -317 -109 40 C ATOM 1138 CZ PHE A 142 38.397 90.838 38.107 1.00 23.30 C ANISOU 1138 CZ PHE C 142 2575 2923 3354 57 128 222 C ATOM 1139 N VAL A 143 41.300 95.136 36.723 1.00 24.02 N ANISOU 1139 N VAL C 143 2744 3303 3076 -204 -124 70 N ATOM 1140 CA VAL A 143 42.709 94.928 36.363 1.00 23.12 C ANISOU 1140 CA VAL C 143 2660 3076 3046 -92 -182 14 C ATOM 1141 C VAL A 143 43.178 93.465 36.590 1.00 22.87 C ANISOU 1141 C VAL C 143 2637 3072 2978 -160 -68 26 C ATOM 1142 O VAL A 143 43.178 92.958 37.702 1.00 23.58 O ANISOU 1142 O VAL C 143 2273 3226 3459 -174 -391 -136 O ATOM 1143 CB VAL A 143 43.643 95.896 37.119 1.00 23.69 C ANISOU 1143 CB VAL C 143 2828 3200 2972 -217 -157 44 C ATOM 1144 CG1 VAL A 143 45.108 95.587 36.842 1.00 24.38 C ANISOU 1144 CG1 VAL C 143 2885 3067 3309 -112 -31 -84 C ATOM 1145 CG2 VAL A 143 43.346 97.367 36.749 1.00 24.57 C ANISOU 1145 CG2 VAL C 143 2880 3304 3152 21 17 -57 C ATOM 1146 N ILE A 144 43.629 92.848 35.518 1.00 23.41 N ANISOU 1146 N ILE C 144 2683 2917 3294 -100 4 -83 N ATOM 1147 CA ILE A 144 44.131 91.457 35.518 1.00 22.43 C ANISOU 1147 CA ILE C 144 2662 2827 3032 -70 -101 -73 C ATOM 1148 C ILE A 144 45.629 91.621 35.344 1.00 21.81 C ANISOU 1148 C ILE C 144 2738 2657 2891 -46 -160 -115 C ATOM 1149 O ILE A 144 46.070 92.312 34.439 1.00 23.05 O ANISOU 1149 O ILE C 144 3249 2931 2576 -78 -105 -29 O ATOM 1150 CB ILE A 144 43.556 90.682 34.306 1.00 22.56 C ANISOU 1150 CB ILE C 144 2756 2860 2954 47 -82 14 C ATOM 1151 CG1 ILE A 144 42.025 90.557 34.425 1.00 23.72 C ANISOU 1151 CG1 ILE C 144 2825 2966 3219 46 89 -115 C ATOM 1152 CG2 ILE A 144 44.233 89.318 34.136 1.00 21.45 C ANISOU 1152 CG2 ILE C 144 2602 2624 2922 16 -33 130 C ATOM 1153 CD1 ILE A 144 41.345 90.391 33.081 1.00 22.75 C ANISOU 1153 CD1 ILE C 144 2612 2814 3217 -79 -151 -153 C ATOM 1154 N ALA A 145 46.425 91.070 36.242 1.00 21.30 N ANISOU 1154 N ALA C 145 2563 2781 2747 23 -39 -142 N ATOM 1155 CA ALA A 145 47.877 91.262 36.153 1.00 20.26 C ANISOU 1155 CA ALA C 145 2542 2595 2561 -27 -74 -63 C ATOM 1156 C ALA A 145 48.602 89.920 36.033 1.00 20.69 C ANISOU 1156 C ALA C 145 2594 2628 2640 19 13 62 C ATOM 1157 O ALA A 145 48.290 88.957 36.747 1.00 20.85 O ANISOU 1157 O ALA C 145 2445 2556 2919 54 -70 -73 O ATOM 1158 CB ALA A 145 48.374 92.015 37.425 1.00 21.23 C ANISOU 1158 CB ALA C 145 2617 2673 2773 133 92 35 C ATOM 1159 N GLY A 146 49.647 89.900 35.216 1.00 20.74 N ANISOU 1159 N GLY C 146 2607 2829 2442 2 -11 -86 N ATOM 1160 CA GLY A 146 50.451 88.716 35.051 1.00 19.53 C ANISOU 1160 CA GLY C 146 2539 2474 2407 13 -2 -100 C ATOM 1161 C GLY A 146 51.564 88.916 34.058 1.00 20.15 C ANISOU 1161 C GLY C 146 2638 2648 2370 45 -34 -33 C ATOM 1162 O GLY A 146 51.802 90.057 33.595 1.00 20.64 O ANISOU 1162 O GLY C 146 2701 2701 2439 242 -157 149 O ATOM 1163 N ASN A 147 52.277 87.845 33.727 1.00 18.97 N ANISOU 1163 N ASN C 147 2478 2379 2351 24 11 56 N ATOM 1164 CA ASN A 147 52.005 86.484 34.155 1.00 19.59 C ANISOU 1164 CA ASN C 147 2627 2349 2466 25 5 0 C ATOM 1165 C ASN A 147 52.887 86.117 35.348 1.00 20.32 C ANISOU 1165 C ASN C 147 2711 2395 2612 104 79 -4 C ATOM 1166 O ASN A 147 54.034 86.574 35.447 1.00 20.03 O ANISOU 1166 O ASN C 147 2948 2232 2429 188 321 -58 O ATOM 1167 CB ASN A 147 52.227 85.490 32.985 1.00 19.00 C ANISOU 1167 CB ASN C 147 2570 2315 2334 -173 -29 64 C ATOM 1168 CG ASN A 147 50.983 85.287 32.097 1.00 22.43 C ANISOU 1168 CG ASN C 147 2793 2754 2973 66 15 47 C ATOM 1169 OD1 ASN A 147 50.209 86.210 31.868 1.00 24.06 O ANISOU 1169 OD1 ASN C 147 3035 2809 3298 31 22 -67 O ATOM 1170 ND2 ASN A 147 50.817 84.056 31.563 1.00 21.17 N ANISOU 1170 ND2 ASN C 147 2961 2645 2436 23 -58 12 N ATOM 1171 N VAL A 148 52.350 85.282 36.234 1.00 19.35 N ANISOU 1171 N VAL C 148 2641 2249 2462 -18 206 27 N ATOM 1172 CA VAL A 148 53.037 84.817 37.397 1.00 19.48 C ANISOU 1172 CA VAL C 148 2525 2419 2454 0 75 11 C ATOM 1173 C VAL A 148 53.025 83.294 37.507 1.00 19.06 C ANISOU 1173 C VAL C 148 2486 2464 2291 80 130 -62 C ATOM 1174 O VAL A 148 52.247 82.617 36.852 1.00 16.57 O ANISOU 1174 O VAL C 148 2378 2447 1468 93 138 -161 O ATOM 1175 CB VAL A 148 52.450 85.451 38.665 1.00 20.55 C ANISOU 1175 CB VAL C 148 2745 2649 2411 76 121 -53 C ATOM 1176 CG1 VAL A 148 52.530 86.962 38.559 1.00 22.16 C ANISOU 1176 CG1 VAL C 148 2763 2940 2715 -172 -54 -186 C ATOM 1177 CG2 VAL A 148 51.005 85.005 38.935 1.00 20.07 C ANISOU 1177 CG2 VAL C 148 2875 2569 2179 -26 185 -100 C ATOM 1178 N GLY A 149 53.871 82.767 38.384 1.00 19.64 N ANISOU 1178 N GLY C 149 2379 2543 2537 37 247 -135 N ATOM 1179 CA GLY A 149 53.977 81.337 38.558 1.00 20.51 C ANISOU 1179 CA GLY C 149 2576 2568 2646 -44 -5 -112 C ATOM 1180 C GLY A 149 54.137 80.842 39.957 1.00 20.15 C ANISOU 1180 C GLY C 149 2538 2395 2720 14 7 -93 C ATOM 1181 O GLY A 149 54.329 79.659 40.134 1.00 22.78 O ANISOU 1181 O GLY C 149 2691 2865 3096 -187 -157 -188 O ATOM 1182 N THR A 150 54.017 81.733 40.940 1.00 20.48 N ANISOU 1182 N THR C 150 2656 2322 2804 -41 11 -85 N ATOM 1183 CA THR A 150 54.172 81.390 42.319 1.00 20.09 C ANISOU 1183 CA THR C 150 2595 2432 2605 -56 -64 -49 C ATOM 1184 C THR A 150 53.102 82.059 43.186 1.00 20.76 C ANISOU 1184 C THR C 150 2670 2646 2569 -99 -27 1 C ATOM 1185 O THR A 150 52.555 83.111 42.829 1.00 19.31 O ANISOU 1185 O THR C 150 2652 2624 2061 -168 40 -36 O ATOM 1186 CB THR A 150 55.560 81.809 42.920 1.00 19.50 C ANISOU 1186 CB THR C 150 2379 2235 2793 -18 8 -75 C ATOM 1187 OG1 THR A 150 55.651 83.223 43.024 1.00 19.86 O ANISOU 1187 OG1 THR C 150 2219 2297 3027 123 305 -65 O ATOM 1188 CG2 THR A 150 56.733 81.285 42.098 1.00 16.68 C ANISOU 1188 CG2 THR C 150 2451 2074 1811 15 16 -336 C ATOM 1189 N PRO A 151 52.784 81.424 44.327 1.00 21.23 N ANISOU 1189 N PRO C 151 2811 2758 2495 -98 -92 -67 N ATOM 1190 CA PRO A 151 51.896 82.031 45.330 1.00 23.04 C ANISOU 1190 CA PRO C 151 2946 2994 2813 -105 -21 25 C ATOM 1191 C PRO A 151 52.368 83.362 45.945 1.00 23.73 C ANISOU 1191 C PRO C 151 2897 3003 3113 -1 25 -33 C ATOM 1192 O PRO A 151 51.526 84.228 46.253 1.00 24.77 O ANISOU 1192 O PRO C 151 2953 3308 3149 24 181 -181 O ATOM 1193 CB PRO A 151 51.820 80.963 46.445 1.00 23.02 C ANISOU 1193 CB PRO C 151 2952 2996 2799 -48 -91 -33 C ATOM 1194 CG PRO A 151 52.877 79.996 46.161 1.00 19.67 C ANISOU 1194 CG PRO C 151 2639 2731 2103 -122 46 -66 C ATOM 1195 CD PRO A 151 53.147 80.036 44.671 1.00 21.06 C ANISOU 1195 CD PRO C 151 2962 2764 2273 -181 -122 -161 C ATOM 1196 N GLU A 152 53.673 83.514 46.168 1.00 24.22 N ANISOU 1196 N GLU C 152 2930 3202 3068 -91 -98 -139 N ATOM 1197 CA GLU A 152 54.213 84.796 46.628 1.00 24.00 C ANISOU 1197 CA GLU C 152 2972 3082 3062 -40 -64 -49 C ATOM 1198 C GLU A 152 53.935 85.887 45.575 1.00 23.16 C ANISOU 1198 C GLU C 152 2977 2918 2901 -1 -80 -18 C ATOM 1199 O GLU A 152 53.610 87.012 45.926 1.00 23.34 O ANISOU 1199 O GLU C 152 2843 3043 2983 84 -5 -49 O ATOM 1200 CB GLU A 152 55.709 84.740 46.951 1.00 25.19 C ANISOU 1200 CB GLU C 152 3072 3382 3114 9 -46 -164 C ATOM 1201 CG GLU A 152 56.571 84.075 45.948 1.00 30.43 C ANISOU 1201 CG GLU C 152 4076 3751 3735 -4 96 -34 C ATOM 1202 CD GLU A 152 56.830 82.559 46.206 1.00 34.98 C ANISOU 1202 CD GLU C 152 4329 4558 4402 120 -181 -146 C ATOM 1203 OE1 GLU A 152 55.871 81.732 46.338 1.00 27.64 O ANISOU 1203 OE1 GLU C 152 3984 3561 2954 -16 -310 -241 O ATOM 1204 OE2 GLU A 152 58.033 82.195 46.224 1.00 42.72 O ANISOU 1204 OE2 GLU C 152 6004 4963 5265 -160 -57 32 O ATOM 1205 N ALA A 153 54.044 85.556 44.294 1.00 23.37 N ANISOU 1205 N ALA C 153 2958 2836 3085 -5 45 -4 N ATOM 1206 CA ALA A 153 53.760 86.543 43.241 1.00 22.57 C ANISOU 1206 CA ALA C 153 2812 2876 2887 -10 -14 29 C ATOM 1207 C ALA A 153 52.289 86.920 43.191 1.00 21.86 C ANISOU 1207 C ALA C 153 2732 2728 2846 -18 70 121 C ATOM 1208 O ALA A 153 51.948 88.103 43.022 1.00 22.09 O ANISOU 1208 O ALA C 153 2729 2800 2863 41 91 -76 O ATOM 1209 CB ALA A 153 54.187 86.030 41.855 1.00 21.46 C ANISOU 1209 CB ALA C 153 2565 2511 3074 -60 75 155 C ATOM 1210 N VAL A 154 51.411 85.921 43.268 1.00 21.96 N ANISOU 1210 N VAL C 154 2639 2843 2858 -72 163 126 N ATOM 1211 CA VAL A 154 49.961 86.189 43.249 1.00 22.82 C ANISOU 1211 CA VAL C 154 2874 2963 2831 0 92 55 C ATOM 1212 C VAL A 154 49.641 87.170 44.396 1.00 23.77 C ANISOU 1212 C VAL C 154 2914 3157 2958 -58 185 41 C ATOM 1213 O VAL A 154 48.975 88.197 44.194 1.00 23.49 O ANISOU 1213 O VAL C 154 2898 3147 2878 -137 492 21 O ATOM 1214 CB VAL A 154 49.122 84.884 43.367 1.00 20.62 C ANISOU 1214 CB VAL C 154 2810 2685 2338 55 176 116 C ATOM 1215 CG1 VAL A 154 47.641 85.208 43.610 1.00 21.77 C ANISOU 1215 CG1 VAL C 154 2970 2738 2564 -151 72 -246 C ATOM 1216 CG2 VAL A 154 49.284 84.006 42.100 1.00 21.55 C ANISOU 1216 CG2 VAL C 154 2329 3043 2814 113 40 210 C ATOM 1217 N ARG A 155 50.159 86.844 45.576 1.00 24.87 N ANISOU 1217 N ARG C 155 3088 3311 3047 -34 169 36 N ATOM 1218 CA ARG A 155 49.962 87.647 46.800 1.00 26.24 C ANISOU 1218 CA ARG C 155 3307 3404 3258 -13 184 12 C ATOM 1219 C ARG A 155 50.411 89.085 46.634 1.00 25.56 C ANISOU 1219 C ARG C 155 3180 3383 3147 -26 60 54 C ATOM 1220 O ARG A 155 49.675 90.017 46.968 1.00 25.33 O ANISOU 1220 O ARG C 155 3250 3207 3167 -82 1 30 O ATOM 1221 CB ARG A 155 50.785 87.063 47.935 1.00 28.36 C ANISOU 1221 CB ARG C 155 3578 3712 3485 -72 174 -75 C ATOM 1222 CG ARG A 155 50.202 85.908 48.625 1.00 35.72 C ANISOU 1222 CG ARG C 155 4504 4296 4770 117 -71 142 C ATOM 1223 CD ARG A 155 49.743 86.290 50.026 1.00 46.28 C ANISOU 1223 CD ARG C 155 6218 6032 5332 -188 200 -14 C ATOM 1224 NE ARG A 155 48.552 85.511 50.353 1.00 50.18 N ANISOU 1224 NE ARG C 155 6469 6207 6389 183 -205 48 N ATOM 1225 CZ ARG A 155 48.502 84.463 51.168 1.00 50.49 C ANISOU 1225 CZ ARG C 155 6386 6299 6496 25 -114 11 C ATOM 1226 NH1 ARG A 155 49.576 84.031 51.834 1.00 51.69 N ANISOU 1226 NH1 ARG C 155 6696 6333 6611 28 -96 -8 N ATOM 1227 NH2 ARG A 155 47.338 83.857 51.336 1.00 50.79 N ANISOU 1227 NH2 ARG C 155 6470 6353 6473 35 -95 -17 N ATOM 1228 N GLU A 156 51.629 89.251 46.126 1.00 26.67 N ANISOU 1228 N GLU C 156 3285 3351 3497 4 114 20 N ATOM 1229 CA GLU A 156 52.223 90.583 45.936 1.00 26.48 C ANISOU 1229 CA GLU C 156 3288 3376 3396 12 121 -8 C ATOM 1230 C GLU A 156 51.408 91.392 44.934 1.00 26.21 C ANISOU 1230 C GLU C 156 3256 3355 3348 16 167 39 C ATOM 1231 O GLU A 156 51.170 92.583 45.132 1.00 26.98 O ANISOU 1231 O GLU C 156 3152 3424 3674 143 320 -97 O ATOM 1232 CB GLU A 156 53.704 90.503 45.521 1.00 26.11 C ANISOU 1232 CB GLU C 156 3288 3472 3158 31 82 89 C ATOM 1233 CG GLU A 156 54.520 91.765 45.962 1.00 27.62 C ANISOU 1233 CG GLU C 156 3548 3485 3461 73 51 69 C ATOM 1234 CD GLU A 156 56.020 91.708 45.686 1.00 28.59 C ANISOU 1234 CD GLU C 156 3633 3488 3741 91 64 -63 C ATOM 1235 OE1 GLU A 156 56.528 90.645 45.287 1.00 32.83 O ANISOU 1235 OE1 GLU C 156 4037 3826 4609 -108 306 105 O ATOM 1236 OE2 GLU A 156 56.693 92.761 45.863 1.00 30.43 O ANISOU 1236 OE2 GLU C 156 3860 3894 3805 132 354 -66 O ATOM 1237 N LEU A 157 50.924 90.744 43.877 1.00 25.47 N ANISOU 1237 N LEU C 157 3148 3258 3270 2 200 0 N ATOM 1238 CA LEU A 157 50.150 91.459 42.866 1.00 25.54 C ANISOU 1238 CA LEU C 157 3143 3281 3279 21 83 -17 C ATOM 1239 C LEU A 157 48.738 91.809 43.360 1.00 24.76 C ANISOU 1239 C LEU C 157 3090 3354 2963 -81 131 40 C ATOM 1240 O LEU A 157 48.251 92.921 43.107 1.00 23.78 O ANISOU 1240 O LEU C 157 2991 3317 2726 -80 30 -54 O ATOM 1241 CB LEU A 157 50.104 90.672 41.559 1.00 25.47 C ANISOU 1241 CB LEU C 157 3259 3398 3021 43 41 -18 C ATOM 1242 CG LEU A 157 51.151 90.959 40.473 1.00 28.32 C ANISOU 1242 CG LEU C 157 3571 3643 3545 7 142 50 C ATOM 1243 CD1 LEU A 157 52.554 91.187 40.949 1.00 32.34 C ANISOU 1243 CD1 LEU C 157 4447 3874 3965 -145 108 -23 C ATOM 1244 CD2 LEU A 157 51.073 89.916 39.400 1.00 24.61 C ANISOU 1244 CD2 LEU C 157 2898 3242 3210 -83 -91 -3 C ATOM 1245 N GLU A 158 48.089 90.865 44.045 1.00 25.74 N ANISOU 1245 N GLU C 158 3163 3327 3291 -83 147 9 N ATOM 1246 CA GLU A 158 46.792 91.110 44.671 1.00 27.46 C ANISOU 1246 CA GLU C 158 3423 3480 3528 -21 53 67 C ATOM 1247 C GLU A 158 46.906 92.274 45.669 1.00 30.06 C ANISOU 1247 C GLU C 158 3671 3818 3931 -91 76 9 C ATOM 1248 O GLU A 158 46.113 93.222 45.638 1.00 30.65 O ANISOU 1248 O GLU C 158 3732 3777 4135 -212 138 81 O ATOM 1249 CB GLU A 158 46.306 89.840 45.373 1.00 27.58 C ANISOU 1249 CB GLU C 158 3375 3420 3682 -93 108 66 C ATOM 1250 CG GLU A 158 45.806 88.747 44.382 1.00 24.78 C ANISOU 1250 CG GLU C 158 3007 2971 3435 -215 70 -5 C ATOM 1251 CD GLU A 158 45.185 87.565 45.080 1.00 25.75 C ANISOU 1251 CD GLU C 158 3321 3269 3192 -104 98 82 C ATOM 1252 OE1 GLU A 158 45.190 87.552 46.346 1.00 26.93 O ANISOU 1252 OE1 GLU C 158 3406 3622 3202 -193 -305 -90 O ATOM 1253 OE2 GLU A 158 44.644 86.665 44.382 1.00 25.66 O ANISOU 1253 OE2 GLU C 158 2945 3807 2997 275 -252 40 O ATOM 1254 N ASN A 159 47.907 92.196 46.541 1.00 31.05 N ANISOU 1254 N ASN C 159 3782 3863 4152 6 59 1 N ATOM 1255 CA ASN A 159 48.182 93.248 47.495 1.00 31.52 C ANISOU 1255 CA ASN C 159 3945 4041 3990 19 130 32 C ATOM 1256 C ASN A 159 48.471 94.627 46.811 1.00 31.54 C ANISOU 1256 C ASN C 159 3932 4096 3955 -21 144 77 C ATOM 1257 O ASN A 159 48.049 95.658 47.326 1.00 33.36 O ANISOU 1257 O ASN C 159 4060 4321 4294 -65 96 175 O ATOM 1258 CB ASN A 159 49.303 92.802 48.451 1.00 33.45 C ANISOU 1258 CB ASN C 159 4090 4336 4281 -33 135 41 C ATOM 1259 CG ASN A 159 48.863 91.677 49.428 1.00 39.60 C ANISOU 1259 CG ASN C 159 5014 5064 4966 -84 -174 -136 C ATOM 1260 OD1 ASN A 159 47.669 91.342 49.544 1.00 45.84 O ANISOU 1260 OD1 ASN C 159 6201 5400 5815 265 -123 101 O ATOM 1261 ND2 ASN A 159 49.842 91.093 50.136 1.00 36.92 N ANISOU 1261 ND2 ASN C 159 4562 4824 4639 -155 68 -130 N ATOM 1262 N ALA A 160 49.119 94.658 45.637 1.00 30.92 N ANISOU 1262 N ALA C 160 3788 4013 3947 -39 78 -31 N ATOM 1263 CA ALA A 160 49.347 95.919 44.917 1.00 30.28 C ANISOU 1263 CA ALA C 160 3765 3889 3849 46 155 16 C ATOM 1264 C ALA A 160 48.059 96.540 44.383 1.00 30.62 C ANISOU 1264 C ALA C 160 3706 3948 3977 43 125 0 C ATOM 1265 O ALA A 160 48.057 97.719 44.009 1.00 32.31 O ANISOU 1265 O ALA C 160 3774 4231 4270 154 218 14 O ATOM 1266 CB ALA A 160 50.357 95.742 43.743 1.00 29.76 C ANISOU 1266 CB ALA C 160 3708 3696 3903 86 156 63 C ATOM 1267 N GLY A 161 46.978 95.758 44.326 1.00 28.70 N ANISOU 1267 N GLY C 161 3368 3759 3775 69 223 -46 N ATOM 1268 CA GLY A 161 45.691 96.227 43.827 1.00 28.45 C ANISOU 1268 CA GLY C 161 3338 3759 3711 -7 144 -5 C ATOM 1269 C GLY A 161 45.095 95.484 42.630 1.00 28.83 C ANISOU 1269 C GLY C 161 3449 3664 3840 -19 147 -44 C ATOM 1270 O GLY A 161 44.028 95.865 42.136 1.00 29.83 O ANISOU 1270 O GLY C 161 3488 3754 4089 -197 102 -64 O ATOM 1271 N ALA A 162 45.751 94.441 42.121 1.00 27.58 N ANISOU 1271 N ALA C 162 3299 3517 3663 -16 129 -50 N ATOM 1272 CA ALA A 162 45.156 93.707 40.977 1.00 26.10 C ANISOU 1272 CA ALA C 162 3103 3327 3487 -16 130 60 C ATOM 1273 C ALA A 162 43.809 93.124 41.373 1.00 24.07 C ANISOU 1273 C ALA C 162 2715 3248 3182 -115 222 46 C ATOM 1274 O ALA A 162 43.669 92.674 42.488 1.00 22.59 O ANISOU 1274 O ALA C 162 2434 3201 2946 -80 332 434 O ATOM 1275 CB ALA A 162 46.103 92.598 40.499 1.00 27.51 C ANISOU 1275 CB ALA C 162 3250 3391 3809 -14 187 -5 C ATOM 1276 N ASP A 163 42.823 93.123 40.476 1.00 23.53 N ANISOU 1276 N ASP C 163 2738 3056 3146 -83 93 15 N ATOM 1277 CA ASP A 163 41.531 92.432 40.753 1.00 23.22 C ANISOU 1277 CA ASP C 163 2728 3015 3079 -57 56 87 C ATOM 1278 C ASP A 163 41.520 90.938 40.338 1.00 21.48 C ANISOU 1278 C ASP C 163 2571 2730 2860 2 123 85 C ATOM 1279 O ASP A 163 40.599 90.184 40.672 1.00 20.50 O ANISOU 1279 O ASP C 163 2288 2646 2854 -227 215 242 O ATOM 1280 CB ASP A 163 40.386 93.163 40.073 1.00 23.99 C ANISOU 1280 CB ASP C 163 2875 3076 3164 108 -26 84 C ATOM 1281 CG ASP A 163 40.320 94.607 40.475 1.00 24.55 C ANISOU 1281 CG ASP C 163 2982 3439 2906 -166 119 231 C ATOM 1282 OD1 ASP A 163 40.053 94.847 41.687 1.00 25.39 O ANISOU 1282 OD1 ASP C 163 2467 3905 3272 -529 624 210 O ATOM 1283 OD2 ASP A 163 40.582 95.473 39.604 1.00 27.59 O ANISOU 1283 OD2 ASP C 163 2859 3882 3739 -417 -240 -104 O ATOM 1284 N ALA A 164 42.536 90.538 39.589 1.00 20.31 N ANISOU 1284 N ALA C 164 2415 2514 2785 -70 113 70 N ATOM 1285 CA ALA A 164 42.773 89.133 39.245 1.00 21.94 C ANISOU 1285 CA ALA C 164 2598 2717 3019 -31 22 51 C ATOM 1286 C ALA A 164 44.220 88.977 38.812 1.00 22.18 C ANISOU 1286 C ALA C 164 2607 2733 3086 -79 -6 185 C ATOM 1287 O ALA A 164 44.868 89.964 38.485 1.00 21.67 O ANISOU 1287 O ALA C 164 2472 2403 3355 -77 -7 350 O ATOM 1288 CB ALA A 164 41.882 88.705 38.121 1.00 21.07 C ANISOU 1288 CB ALA C 164 2496 2787 2721 -85 39 -31 C ATOM 1289 N THR A 165 44.709 87.738 38.799 1.00 22.01 N ANISOU 1289 N THR C 165 2593 2828 2939 -28 75 155 N ATOM 1290 CA THR A 165 46.046 87.440 38.295 1.00 20.74 C ANISOU 1290 CA THR C 165 2546 2605 2728 20 28 78 C ATOM 1291 C THR A 165 45.993 86.384 37.195 1.00 19.42 C ANISOU 1291 C THR C 165 2347 2486 2543 -16 98 85 C ATOM 1292 O THR A 165 45.075 85.545 37.165 1.00 18.94 O ANISOU 1292 O THR C 165 2009 2591 2594 -116 196 198 O ATOM 1293 CB THR A 165 47.033 86.982 39.389 1.00 20.96 C ANISOU 1293 CB THR C 165 2641 2712 2609 40 -43 134 C ATOM 1294 OG1 THR A 165 46.563 85.794 40.036 1.00 20.37 O ANISOU 1294 OG1 THR C 165 2594 2415 2730 -193 132 607 O ATOM 1295 CG2 THR A 165 47.261 88.091 40.409 1.00 18.97 C ANISOU 1295 CG2 THR C 165 2424 2240 2543 255 -126 134 C ATOM 1296 N LYS A 166 46.960 86.433 36.288 1.00 18.61 N ANISOU 1296 N LYS C 166 2228 2359 2482 93 -123 -79 N ATOM 1297 CA LYS A 166 47.047 85.436 35.225 1.00 18.74 C ANISOU 1297 CA LYS C 166 2398 2308 2412 -55 -59 28 C ATOM 1298 C LYS A 166 48.275 84.546 35.439 1.00 18.65 C ANISOU 1298 C LYS C 166 2514 2263 2308 -39 -111 -67 C ATOM 1299 O LYS A 166 49.414 85.043 35.522 1.00 19.58 O ANISOU 1299 O LYS C 166 2808 2219 2410 -215 70 -165 O ATOM 1300 CB LYS A 166 47.047 86.100 33.832 1.00 19.08 C ANISOU 1300 CB LYS C 166 2409 2352 2487 12 -105 -249 C ATOM 1301 CG LYS A 166 47.003 85.132 32.673 1.00 17.49 C ANISOU 1301 CG LYS C 166 2110 2015 2520 -203 -86 43 C ATOM 1302 CD LYS A 166 46.094 85.575 31.526 1.00 19.21 C ANISOU 1302 CD LYS C 166 2478 2329 2490 -102 -93 50 C ATOM 1303 CE LYS A 166 46.691 86.694 30.651 1.00 19.42 C ANISOU 1303 CE LYS C 166 2253 2481 2641 -243 -62 107 C ATOM 1304 NZ LYS A 166 48.035 86.410 30.131 1.00 20.42 N ANISOU 1304 NZ LYS C 166 2530 2759 2468 -107 -465 35 N ATOM 1305 N VAL A 167 48.018 83.247 35.533 1.00 17.92 N ANISOU 1305 N VAL C 167 2309 2189 2309 -79 111 -77 N ATOM 1306 CA VAL A 167 49.008 82.257 36.005 1.00 17.81 C ANISOU 1306 CA VAL C 167 2330 2130 2306 6 -16 -143 C ATOM 1307 C VAL A 167 49.485 81.341 34.872 1.00 17.14 C ANISOU 1307 C VAL C 167 2293 2086 2132 -80 -40 -116 C ATOM 1308 O VAL A 167 48.661 80.716 34.137 1.00 14.48 O ANISOU 1308 O VAL C 167 1989 1999 1514 -120 374 143 O ATOM 1309 CB VAL A 167 48.443 81.422 37.223 1.00 19.87 C ANISOU 1309 CB VAL C 167 2638 2238 2672 45 -20 -134 C ATOM 1310 CG1 VAL A 167 49.371 80.252 37.601 1.00 18.75 C ANISOU 1310 CG1 VAL C 167 2416 2460 2248 151 35 -320 C ATOM 1311 CG2 VAL A 167 48.215 82.289 38.400 1.00 21.14 C ANISOU 1311 CG2 VAL C 167 2846 2269 2915 71 0 -139 C ATOM 1312 N GLY A 168 50.814 81.257 34.727 1.00 17.71 N ANISOU 1312 N GLY C 168 2526 2232 1968 76 -43 39 N ATOM 1313 CA GLY A 168 51.461 80.483 33.635 1.00 18.84 C ANISOU 1313 CA GLY C 168 2442 2332 2381 -68 42 -71 C ATOM 1314 C GLY A 168 52.737 81.165 33.173 1.00 18.72 C ANISOU 1314 C GLY C 168 2427 2567 2116 -84 -4 137 C ATOM 1315 O GLY A 168 52.706 82.338 32.832 1.00 19.11 O ANISOU 1315 O GLY C 168 2544 2467 2247 -169 -53 222 O ATOM 1316 N ILE A 169 53.865 80.445 33.219 1.00 19.09 N ANISOU 1316 N ILE C 169 2446 2505 2302 -49 19 -47 N ATOM 1317 CA ILE A 169 55.157 80.944 32.773 1.00 20.99 C ANISOU 1317 CA ILE C 169 2719 2625 2632 -32 -42 -9 C ATOM 1318 C ILE A 169 55.756 79.889 31.830 1.00 22.43 C ANISOU 1318 C ILE C 169 2838 2705 2977 -32 -70 52 C ATOM 1319 O ILE A 169 56.327 78.892 32.265 1.00 20.78 O ANISOU 1319 O ILE C 169 2737 2255 2900 -62 -23 233 O ATOM 1320 CB ILE A 169 56.113 81.211 33.947 1.00 20.76 C ANISOU 1320 CB ILE C 169 2678 2380 2828 -64 24 -96 C ATOM 1321 CG1 ILE A 169 55.536 82.228 34.951 1.00 22.26 C ANISOU 1321 CG1 ILE C 169 3027 2449 2979 -67 -142 4 C ATOM 1322 CG2 ILE A 169 57.449 81.670 33.434 1.00 21.69 C ANISOU 1322 CG2 ILE C 169 2563 2792 2885 -50 -2 22 C ATOM 1323 CD1 ILE A 169 55.596 83.661 34.511 1.00 25.65 C ANISOU 1323 CD1 ILE C 169 3124 3124 3495 -57 2 48 C ATOM 1324 N GLY A 170 55.576 80.110 30.535 1.00 23.73 N ANISOU 1324 N GLY C 170 3018 3001 2995 -2 -21 7 N ATOM 1325 CA GLY A 170 55.955 79.145 29.497 1.00 25.13 C ANISOU 1325 CA GLY C 170 3145 3145 3255 -48 86 19 C ATOM 1326 C GLY A 170 55.361 77.768 29.799 1.00 25.96 C ANISOU 1326 C GLY C 170 3192 3317 3352 31 77 12 C ATOM 1327 O GLY A 170 56.106 76.818 30.077 1.00 25.00 O ANISOU 1327 O GLY C 170 3148 3178 3170 12 370 205 O ATOM 1328 N PRO A 171 54.016 77.673 29.798 1.00 26.57 N ANISOU 1328 N PRO C 171 3332 3344 3417 28 169 -48 N ATOM 1329 CA PRO A 171 53.326 76.472 30.249 1.00 28.88 C ANISOU 1329 CA PRO C 171 3661 3565 3745 32 27 20 C ATOM 1330 C PRO A 171 53.454 75.281 29.296 1.00 31.15 C ANISOU 1330 C PRO C 171 3931 3891 4012 9 35 39 C ATOM 1331 O PRO A 171 53.356 74.133 29.737 1.00 32.93 O ANISOU 1331 O PRO C 171 4101 4165 4245 -4 -198 148 O ATOM 1332 CB PRO A 171 51.867 76.919 30.333 1.00 29.22 C ANISOU 1332 CB PRO C 171 3745 3605 3749 24 63 70 C ATOM 1333 CG PRO A 171 51.746 77.992 29.339 1.00 28.94 C ANISOU 1333 CG PRO C 171 3719 3494 3783 -60 40 47 C ATOM 1334 CD PRO A 171 53.069 78.721 29.385 1.00 26.99 C ANISOU 1334 CD PRO C 171 3456 3543 3254 139 114 -258 C ATOM 1335 N GLY A 172 53.664 75.532 28.009 1.00 31.96 N ANISOU 1335 N GLY C 172 4076 3999 4065 35 -31 97 N ATOM 1336 CA GLY A 172 53.766 74.436 27.046 1.00 32.68 C ANISOU 1336 CA GLY C 172 4144 4110 4163 33 76 44 C ATOM 1337 C GLY A 172 54.992 73.558 27.248 1.00 33.76 C ANISOU 1337 C GLY C 172 4165 4316 4347 7 -24 -23 C ATOM 1338 O GLY A 172 56.051 74.023 27.685 1.00 34.04 O ANISOU 1338 O GLY C 172 4122 4299 4511 48 -107 58 O ATOM 1339 N LYS A 173 54.856 72.284 26.880 1.00 35.23 N ANISOU 1339 N LYS C 173 4336 4444 4606 49 -19 -8 N ATOM 1340 CA LYS A 173 55.873 71.265 27.188 1.00 35.88 C ANISOU 1340 CA LYS C 173 4412 4526 4694 -28 13 -24 C ATOM 1341 C LYS A 173 57.126 71.488 26.371 1.00 37.10 C ANISOU 1341 C LYS C 173 4522 4739 4834 -37 -13 -2 C ATOM 1342 O LYS A 173 58.195 71.022 26.732 1.00 39.28 O ANISOU 1342 O LYS C 173 4780 4952 5190 -7 -43 -167 O ATOM 1343 CB LYS A 173 55.381 69.847 26.875 1.00 36.59 C ANISOU 1343 CB LYS C 173 4505 4564 4831 24 -38 48 C ATOM 1344 CG LYS A 173 53.997 69.453 27.388 1.00 37.50 C ANISOU 1344 CG LYS C 173 4751 4737 4758 -69 1 42 C ATOM 1345 CD LYS A 173 53.978 69.174 28.849 1.00 35.90 C ANISOU 1345 CD LYS C 173 4506 4511 4624 47 -84 155 C ATOM 1346 CE LYS A 173 52.817 68.261 29.205 1.00 31.94 C ANISOU 1346 CE LYS C 173 3812 4078 4243 -8 106 -120 C ATOM 1347 NZ LYS A 173 52.881 68.018 30.653 1.00 29.63 N ANISOU 1347 NZ LYS C 173 3659 3722 3874 152 43 118 N ATOM 1348 N VAL A 174 57.003 72.176 25.246 1.00 37.06 N ANISOU 1348 N VAL C 174 4607 4781 4693 -57 44 4 N ATOM 1349 CA VAL A 174 58.162 72.429 24.393 1.00 36.63 C ANISOU 1349 CA VAL C 174 4556 4683 4678 -7 29 47 C ATOM 1350 C VAL A 174 58.215 73.874 23.899 1.00 35.94 C ANISOU 1350 C VAL C 174 4549 4618 4488 28 10 103 C ATOM 1351 O VAL A 174 58.703 74.153 22.804 1.00 35.93 O ANISOU 1351 O VAL C 174 4691 4573 4384 106 63 161 O ATOM 1352 CB VAL A 174 58.188 71.419 23.219 1.00 37.82 C ANISOU 1352 CB VAL C 174 4773 4816 4778 10 70 -22 C ATOM 1353 CG1 VAL A 174 58.332 70.019 23.771 1.00 39.03 C ANISOU 1353 CG1 VAL C 174 4748 5039 5041 46 110 -103 C ATOM 1354 CG2 VAL A 174 56.915 71.510 22.371 1.00 39.54 C ANISOU 1354 CG2 VAL C 174 5126 4941 4955 -16 -40 -3 C ATOM 1355 N CYS A 175 57.754 74.801 24.727 1.00 34.45 N ANISOU 1355 N CYS C 175 4359 4453 4277 28 11 142 N ATOM 1356 CA CYS A 175 57.759 76.208 24.363 1.00 33.48 C ANISOU 1356 CA CYS C 175 4288 4266 4165 -13 -2 53 C ATOM 1357 C CYS A 175 59.146 76.830 24.539 1.00 31.82 C ANISOU 1357 C CYS C 175 4067 4106 3917 -63 17 108 C ATOM 1358 O CYS A 175 60.037 76.244 25.153 1.00 29.60 O ANISOU 1358 O CYS C 175 3807 3759 3678 -6 -26 315 O ATOM 1359 CB CYS A 175 56.711 76.969 25.184 1.00 33.92 C ANISOU 1359 CB CYS C 175 4305 4265 4316 -79 -48 56 C ATOM 1360 SG CYS A 175 57.141 77.216 26.938 1.00 33.91 S ANISOU 1360 SG CYS C 175 4043 4286 4552 -119 -51 220 S ATOM 1361 N ILE A 176 59.308 78.042 24.021 1.00 32.85 N ANISOU 1361 N ILE C 176 4257 4115 4110 17 -107 -10 N ATOM 1362 CA ILE A 176 60.587 78.752 24.036 1.00 32.33 C ANISOU 1362 CA ILE C 176 4179 4047 4054 -8 -71 -42 C ATOM 1363 C ILE A 176 61.175 78.988 25.417 1.00 30.86 C ANISOU 1363 C ILE C 176 3995 3810 3919 -78 -150 -16 C ATOM 1364 O ILE A 176 62.367 78.722 25.646 1.00 30.49 O ANISOU 1364 O ILE C 176 4001 3538 4045 -64 -260 -137 O ATOM 1365 CB ILE A 176 60.448 80.145 23.334 1.00 33.99 C ANISOU 1365 CB ILE C 176 4303 4270 4342 81 -90 -20 C ATOM 1366 CG1 ILE A 176 60.099 79.948 21.863 1.00 36.80 C ANISOU 1366 CG1 ILE C 176 4727 4718 4536 148 -82 34 C ATOM 1367 CG2 ILE A 176 61.721 80.991 23.481 1.00 34.66 C ANISOU 1367 CG2 ILE C 176 4422 4344 4403 89 -27 -43 C ATOM 1368 CD1 ILE A 176 60.789 78.766 21.217 1.00 38.89 C ANISOU 1368 CD1 ILE C 176 4985 4992 4798 -46 -6 135 C ATOM 1369 N THR A 177 60.357 79.536 26.303 1.00 27.89 N ANISOU 1369 N THR C 177 3566 3452 3578 -148 -182 -36 N ATOM 1370 CA THR A 177 60.781 79.866 27.642 1.00 28.30 C ANISOU 1370 CA THR C 177 3547 3523 3680 -100 -43 42 C ATOM 1371 C THR A 177 61.405 78.660 28.346 1.00 24.70 C ANISOU 1371 C THR C 177 3261 3183 2938 -36 -63 75 C ATOM 1372 O THR A 177 62.517 78.760 28.854 1.00 21.89 O ANISOU 1372 O THR C 177 2905 2903 2510 1 41 168 O ATOM 1373 CB THR A 177 59.611 80.441 28.457 1.00 29.05 C ANISOU 1373 CB THR C 177 3658 3629 3750 -105 -59 53 C ATOM 1374 OG1 THR A 177 59.147 81.604 27.779 1.00 31.51 O ANISOU 1374 OG1 THR C 177 3667 3830 4475 -380 -36 96 O ATOM 1375 CG2 THR A 177 60.057 80.814 29.880 1.00 27.93 C ANISOU 1375 CG2 THR C 177 3613 3402 3596 -94 -37 38 C ATOM 1376 N LYS A 178 60.702 77.523 28.334 1.00 24.25 N ANISOU 1376 N LYS C 178 3317 3045 2849 -21 146 -37 N ATOM 1377 CA LYS A 178 61.193 76.277 28.934 1.00 25.65 C ANISOU 1377 CA LYS C 178 3384 3248 3112 -39 37 -10 C ATOM 1378 C LYS A 178 62.542 75.869 28.346 1.00 25.33 C ANISOU 1378 C LYS C 178 3338 3292 2992 -89 10 -18 C ATOM 1379 O LYS A 178 63.523 75.620 29.073 1.00 26.08 O ANISOU 1379 O LYS C 178 3616 3198 3092 -151 71 159 O ATOM 1380 CB LYS A 178 60.155 75.167 28.709 1.00 26.80 C ANISOU 1380 CB LYS C 178 3506 3353 3322 -134 -32 -37 C ATOM 1381 CG LYS A 178 60.455 73.853 29.334 1.00 27.94 C ANISOU 1381 CG LYS C 178 3603 3538 3472 72 -25 -97 C ATOM 1382 CD LYS A 178 59.539 72.800 28.771 1.00 29.73 C ANISOU 1382 CD LYS C 178 3722 3754 3820 146 54 -73 C ATOM 1383 CE LYS A 178 59.854 71.392 29.290 1.00 34.80 C ANISOU 1383 CE LYS C 178 4029 4623 4567 -71 -138 -28 C ATOM 1384 NZ LYS A 178 61.297 71.014 29.327 1.00 37.09 N ANISOU 1384 NZ LYS C 178 4662 4584 4846 70 133 19 N ATOM 1385 N ILE A 179 62.596 75.812 27.019 1.00 25.05 N ANISOU 1385 N ILE C 179 3244 3269 3004 -154 -49 57 N ATOM 1386 CA ILE A 179 63.782 75.347 26.355 1.00 24.90 C ANISOU 1386 CA ILE C 179 3265 3252 2942 -58 -6 22 C ATOM 1387 C ILE A 179 64.964 76.291 26.538 1.00 24.15 C ANISOU 1387 C ILE C 179 3166 3208 2799 -107 24 -9 C ATOM 1388 O ILE A 179 66.082 75.852 26.790 1.00 23.84 O ANISOU 1388 O ILE C 179 3359 3068 2630 -121 44 -273 O ATOM 1389 CB ILE A 179 63.562 75.162 24.831 1.00 25.71 C ANISOU 1389 CB ILE C 179 3464 3370 2933 -66 -11 5 C ATOM 1390 CG1 ILE A 179 62.365 74.244 24.510 1.00 29.29 C ANISOU 1390 CG1 ILE C 179 3516 3707 3907 -58 48 40 C ATOM 1391 CG2 ILE A 179 64.838 74.637 24.207 1.00 25.92 C ANISOU 1391 CG2 ILE C 179 3293 3357 3196 -26 -23 148 C ATOM 1392 CD1 ILE A 179 62.331 72.927 25.220 1.00 34.05 C ANISOU 1392 CD1 ILE C 179 4238 4404 4294 -53 -161 -75 C ATOM 1393 N LYS A 180 64.739 77.587 26.386 1.00 22.89 N ANISOU 1393 N LYS C 180 2947 2960 2788 -94 -79 2 N ATOM 1394 CA LYS A 180 65.866 78.500 26.349 1.00 23.72 C ANISOU 1394 CA LYS C 180 3079 3041 2892 -79 -32 -68 C ATOM 1395 C LYS A 180 66.362 78.961 27.734 1.00 21.71 C ANISOU 1395 C LYS C 180 2860 2818 2569 -85 -115 -87 C ATOM 1396 O LYS A 180 67.555 79.269 27.876 1.00 20.23 O ANISOU 1396 O LYS C 180 2906 2719 2061 -180 -302 23 O ATOM 1397 CB LYS A 180 65.557 79.698 25.438 1.00 26.47 C ANISOU 1397 CB LYS C 180 3338 3324 3395 92 -200 18 C ATOM 1398 CG LYS A 180 65.459 79.338 23.948 1.00 29.09 C ANISOU 1398 CG LYS C 180 3857 3949 3247 33 96 -150 C ATOM 1399 CD LYS A 180 66.610 78.396 23.512 1.00 36.28 C ANISOU 1399 CD LYS C 180 4875 4579 4330 -152 39 -9 C ATOM 1400 CE LYS A 180 66.785 78.274 21.960 1.00 37.44 C ANISOU 1400 CE LYS C 180 5060 4888 4274 0 153 220 C ATOM 1401 NZ LYS A 180 65.677 77.513 21.287 1.00 40.84 N ANISOU 1401 NZ LYS C 180 5278 5459 4781 232 8 -62 N ATOM 1402 N THR A 181 65.478 79.008 28.736 1.00 19.88 N ANISOU 1402 N THR C 181 2614 2478 2460 -39 -180 -184 N ATOM 1403 CA THR A 181 65.860 79.546 30.057 1.00 20.78 C ANISOU 1403 CA THR C 181 2647 2552 2694 -15 6 16 C ATOM 1404 C THR A 181 65.918 78.529 31.201 1.00 18.36 C ANISOU 1404 C THR C 181 2316 2185 2475 -59 33 30 C ATOM 1405 O THR A 181 66.551 78.796 32.199 1.00 19.31 O ANISOU 1405 O THR C 181 2335 2228 2773 -125 -87 142 O ATOM 1406 CB THR A 181 64.910 80.671 30.537 1.00 20.65 C ANISOU 1406 CB THR C 181 2474 2397 2973 -32 -77 -87 C ATOM 1407 OG1 THR A 181 63.669 80.109 30.989 1.00 20.61 O ANISOU 1407 OG1 THR C 181 2631 2462 2736 -211 -56 182 O ATOM 1408 CG2 THR A 181 64.690 81.698 29.446 1.00 22.49 C ANISOU 1408 CG2 THR C 181 3136 2690 2717 55 69 -71 C ATOM 1409 N GLY A 182 65.215 77.402 31.072 1.00 19.13 N ANISOU 1409 N GLY C 182 2305 2420 2542 -57 -9 111 N ATOM 1410 CA GLY A 182 65.095 76.414 32.135 1.00 18.58 C ANISOU 1410 CA GLY C 182 2404 2344 2308 -97 60 -53 C ATOM 1411 C GLY A 182 64.092 76.753 33.226 1.00 18.57 C ANISOU 1411 C GLY C 182 2267 2347 2440 -55 15 21 C ATOM 1412 O GLY A 182 63.983 76.008 34.207 1.00 17.58 O ANISOU 1412 O GLY C 182 1978 2673 2029 -96 359 -23 O ATOM 1413 N PHE A 183 63.369 77.873 33.070 1.00 17.77 N ANISOU 1413 N PHE C 183 2124 2257 2368 -146 -97 55 N ATOM 1414 CA PHE A 183 62.429 78.367 34.088 1.00 18.39 C ANISOU 1414 CA PHE C 183 2269 2328 2388 -71 -37 -5 C ATOM 1415 C PHE A 183 60.990 78.240 33.595 1.00 19.77 C ANISOU 1415 C PHE C 183 2570 2386 2555 -58 -39 3 C ATOM 1416 O PHE A 183 60.699 78.397 32.402 1.00 20.08 O ANISOU 1416 O PHE C 183 3108 2157 2363 -20 -118 313 O ATOM 1417 CB PHE A 183 62.661 79.874 34.373 1.00 17.57 C ANISOU 1417 CB PHE C 183 2356 2182 2138 -75 134 6 C ATOM 1418 CG PHE A 183 63.782 80.147 35.296 1.00 16.64 C ANISOU 1418 CG PHE C 183 1794 2245 2281 -101 7 40 C ATOM 1419 CD1 PHE A 183 63.545 80.313 36.662 1.00 17.68 C ANISOU 1419 CD1 PHE C 183 2044 2262 2410 -120 -17 52 C ATOM 1420 CD2 PHE A 183 65.084 80.187 34.822 1.00 18.67 C ANISOU 1420 CD2 PHE C 183 2601 2072 2418 -83 -57 -103 C ATOM 1421 CE1 PHE A 183 64.581 80.551 37.536 1.00 16.77 C ANISOU 1421 CE1 PHE C 183 1826 2199 2347 -118 339 -68 C ATOM 1422 CE2 PHE A 183 66.140 80.433 35.689 1.00 18.75 C ANISOU 1422 CE2 PHE C 183 2655 2023 2444 12 396 -136 C ATOM 1423 CZ PHE A 183 65.895 80.589 37.044 1.00 17.19 C ANISOU 1423 CZ PHE C 183 2530 1898 2101 322 104 30 C ATOM 1424 N GLY A 184 60.099 78.060 34.545 1.00 20.39 N ANISOU 1424 N GLY C 184 2479 2369 2898 135 -223 -33 N ATOM 1425 CA GLY A 184 58.683 78.308 34.361 1.00 21.62 C ANISOU 1425 CA GLY C 184 2596 2531 3085 56 -148 6 C ATOM 1426 C GLY A 184 57.817 77.115 34.755 1.00 20.01 C ANISOU 1426 C GLY C 184 2429 2347 2825 116 -239 95 C ATOM 1427 O GLY A 184 58.288 76.179 35.414 1.00 20.19 O ANISOU 1427 O GLY C 184 2762 2069 2836 118 -519 181 O ATOM 1428 N THR A 185 56.561 77.167 34.334 1.00 18.03 N ANISOU 1428 N THR C 185 2267 2310 2271 -62 -129 92 N ATOM 1429 CA THR A 185 55.559 76.147 34.667 1.00 19.84 C ANISOU 1429 CA THR C 185 2526 2324 2689 3 -24 56 C ATOM 1430 C THR A 185 55.386 75.063 33.610 1.00 20.03 C ANISOU 1430 C THR C 185 2601 2333 2674 -125 -22 112 C ATOM 1431 O THR A 185 54.518 74.196 33.722 1.00 19.63 O ANISOU 1431 O THR C 185 2544 2264 2649 -118 196 25 O ATOM 1432 CB THR A 185 54.191 76.803 34.933 1.00 20.44 C ANISOU 1432 CB THR C 185 2430 2392 2944 -7 -42 12 C ATOM 1433 OG1 THR A 185 53.771 77.508 33.761 1.00 17.95 O ANISOU 1433 OG1 THR C 185 2205 2019 2594 113 -80 566 O ATOM 1434 CG2 THR A 185 54.253 77.695 36.189 1.00 22.61 C ANISOU 1434 CG2 THR C 185 2572 2719 3298 57 -278 -37 C ATOM 1435 N GLY A 186 56.262 75.070 32.612 1.00 19.74 N ANISOU 1435 N GLY C 186 2655 2610 2232 -117 -107 37 N ATOM 1436 CA GLY A 186 56.165 74.108 31.504 1.00 20.80 C ANISOU 1436 CA GLY C 186 2678 2528 2694 -44 47 60 C ATOM 1437 C GLY A 186 56.353 72.697 32.008 1.00 21.05 C ANISOU 1437 C GLY C 186 2727 2614 2657 -29 44 138 C ATOM 1438 O GLY A 186 57.315 72.410 32.722 1.00 24.25 O ANISOU 1438 O GLY C 186 2932 2806 3472 -292 -112 202 O ATOM 1439 N GLY A 187 55.401 71.838 31.681 1.00 20.20 N ANISOU 1439 N GLY C 187 2629 2528 2517 -49 77 122 N ATOM 1440 CA GLY A 187 55.411 70.474 32.157 1.00 20.54 C ANISOU 1440 CA GLY C 187 2593 2474 2735 -68 162 49 C ATOM 1441 C GLY A 187 54.827 70.188 33.517 1.00 20.77 C ANISOU 1441 C GLY C 187 2597 2554 2740 -66 65 -74 C ATOM 1442 O GLY A 187 54.765 69.007 33.880 1.00 21.13 O ANISOU 1442 O GLY C 187 2546 2408 3074 -186 79 -94 O ATOM 1443 N TRP A 188 54.394 71.242 34.256 1.00 19.86 N ANISOU 1443 N TRP C 188 2482 2350 2711 25 178 -135 N ATOM 1444 CA TRP A 188 53.635 71.098 35.508 1.00 18.67 C ANISOU 1444 CA TRP C 188 2293 2198 2602 -37 140 -57 C ATOM 1445 C TRP A 188 52.584 72.220 35.732 1.00 17.74 C ANISOU 1445 C TRP C 188 2262 2061 2414 12 51 13 C ATOM 1446 O TRP A 188 52.334 72.621 36.880 1.00 14.40 O ANISOU 1446 O TRP C 188 2030 1526 1914 -75 278 -209 O ATOM 1447 CB TRP A 188 54.562 71.004 36.739 1.00 19.52 C ANISOU 1447 CB TRP C 188 2423 2423 2570 -116 27 -25 C ATOM 1448 CG TRP A 188 55.418 72.227 36.988 1.00 18.38 C ANISOU 1448 CG TRP C 188 2559 1982 2442 -103 -97 -173 C ATOM 1449 CD1 TRP A 188 56.386 72.726 36.169 1.00 19.43 C ANISOU 1449 CD1 TRP C 188 2476 2480 2422 -49 -164 -189 C ATOM 1450 CD2 TRP A 188 55.391 73.081 38.149 1.00 20.17 C ANISOU 1450 CD2 TRP C 188 2725 2139 2797 -148 80 38 C ATOM 1451 NE1 TRP A 188 56.959 73.827 36.750 1.00 20.46 N ANISOU 1451 NE1 TRP C 188 2665 2484 2623 168 -252 -12 N ATOM 1452 CE2 TRP A 188 56.351 74.088 37.947 1.00 20.42 C ANISOU 1452 CE2 TRP C 188 2739 2420 2599 -91 121 -185 C ATOM 1453 CE3 TRP A 188 54.625 73.099 39.331 1.00 20.26 C ANISOU 1453 CE3 TRP C 188 2717 2611 2371 -12 97 -7 C ATOM 1454 CZ2 TRP A 188 56.573 75.129 38.883 1.00 19.85 C ANISOU 1454 CZ2 TRP C 188 2686 2303 2553 -58 143 84 C ATOM 1455 CZ3 TRP A 188 54.853 74.113 40.263 1.00 20.28 C ANISOU 1455 CZ3 TRP C 188 2822 2321 2559 120 33 7 C ATOM 1456 CH2 TRP A 188 55.817 75.110 40.037 1.00 18.95 C ANISOU 1456 CH2 TRP C 188 2434 2342 2423 -68 -108 -217 C ATOM 1457 N GLN A 189 51.989 72.699 34.640 1.00 18.21 N ANISOU 1457 N GLN C 189 2261 2081 2574 99 165 -16 N ATOM 1458 CA GLN A 189 51.084 73.843 34.678 1.00 17.47 C ANISOU 1458 CA GLN C 189 2138 2095 2404 24 58 -24 C ATOM 1459 C GLN A 189 49.914 73.617 35.611 1.00 17.47 C ANISOU 1459 C GLN C 189 2090 2048 2500 68 37 -31 C ATOM 1460 O GLN A 189 49.571 74.521 36.410 1.00 17.00 O ANISOU 1460 O GLN C 189 1942 1961 2554 -31 13 -69 O ATOM 1461 CB GLN A 189 50.633 74.239 33.260 1.00 18.98 C ANISOU 1461 CB GLN C 189 2391 2245 2573 74 -40 22 C ATOM 1462 CG GLN A 189 49.502 75.293 33.206 1.00 20.19 C ANISOU 1462 CG GLN C 189 2515 2473 2682 -41 38 96 C ATOM 1463 CD GLN A 189 49.889 76.672 33.770 1.00 22.29 C ANISOU 1463 CD GLN C 189 2780 2771 2917 60 49 -81 C ATOM 1464 OE1 GLN A 189 51.064 76.979 33.932 1.00 23.24 O ANISOU 1464 OE1 GLN C 189 3081 2690 3058 -91 -323 -430 O ATOM 1465 NE2 GLN A 189 48.885 77.521 34.023 1.00 20.24 N ANISOU 1465 NE2 GLN C 189 2301 2693 2695 168 315 -37 N ATOM 1466 N LEU A 190 49.318 72.425 35.598 1.00 17.72 N ANISOU 1466 N LEU C 190 1931 2184 2616 -108 85 30 N ATOM 1467 CA LEU A 190 48.174 72.194 36.519 1.00 17.42 C ANISOU 1467 CA LEU C 190 2074 2093 2451 -60 27 2 C ATOM 1468 C LEU A 190 48.514 72.272 38.015 1.00 16.72 C ANISOU 1468 C LEU C 190 1959 1917 2475 -7 86 -20 C ATOM 1469 O LEU A 190 47.772 72.842 38.808 1.00 16.34 O ANISOU 1469 O LEU C 190 1792 1781 2636 183 22 -24 O ATOM 1470 CB LEU A 190 47.444 70.889 36.208 1.00 18.17 C ANISOU 1470 CB LEU C 190 2200 2090 2612 -41 -129 -111 C ATOM 1471 CG LEU A 190 46.062 70.748 36.840 1.00 18.06 C ANISOU 1471 CG LEU C 190 2106 2365 2389 -72 -4 118 C ATOM 1472 CD1 LEU A 190 45.124 71.946 36.594 1.00 18.36 C ANISOU 1472 CD1 LEU C 190 2263 2060 2651 80 49 -133 C ATOM 1473 CD2 LEU A 190 45.409 69.484 36.354 1.00 18.85 C ANISOU 1473 CD2 LEU C 190 2346 2097 2717 3 87 84 C ATOM 1474 N ALA A 191 49.631 71.661 38.404 1.00 16.76 N ANISOU 1474 N ALA C 191 2234 1911 2222 -158 -10 -54 N ATOM 1475 CA ALA A 191 50.073 71.705 39.790 1.00 17.50 C ANISOU 1475 CA ALA C 191 2270 2061 2318 -96 10 35 C ATOM 1476 C ALA A 191 50.489 73.123 40.170 1.00 16.94 C ANISOU 1476 C ALA C 191 2252 2049 2134 -185 84 10 C ATOM 1477 O ALA A 191 50.252 73.546 41.298 1.00 17.78 O ANISOU 1477 O ALA C 191 2614 2185 1954 -350 135 52 O ATOM 1478 CB ALA A 191 51.194 70.703 40.022 1.00 18.32 C ANISOU 1478 CB ALA C 191 2340 2120 2500 -115 -90 65 C ATOM 1479 N ALA A 192 51.099 73.854 39.233 1.00 16.83 N ANISOU 1479 N ALA C 192 2076 2161 2156 -165 41 -119 N ATOM 1480 CA ALA A 192 51.450 75.268 39.429 1.00 16.45 C ANISOU 1480 CA ALA C 192 2127 2166 1957 -50 38 36 C ATOM 1481 C ALA A 192 50.189 76.096 39.696 1.00 16.31 C ANISOU 1481 C ALA C 192 2032 2158 2008 54 81 71 C ATOM 1482 O ALA A 192 50.175 76.947 40.573 1.00 16.76 O ANISOU 1482 O ALA C 192 2110 2158 2098 -25 423 575 O ATOM 1483 CB ALA A 192 52.215 75.827 38.177 1.00 16.58 C ANISOU 1483 CB ALA C 192 2023 2075 2201 -1 15 86 C ATOM 1484 N LEU A 193 49.133 75.829 38.944 1.00 15.58 N ANISOU 1484 N LEU C 193 2072 2018 1827 -18 33 -73 N ATOM 1485 CA LEU A 193 47.836 76.506 39.110 1.00 16.98 C ANISOU 1485 CA LEU C 193 2173 2196 2081 0 37 82 C ATOM 1486 C LEU A 193 47.245 76.240 40.498 1.00 16.46 C ANISOU 1486 C LEU C 193 2262 2126 1865 -8 -60 85 C ATOM 1487 O LEU A 193 46.782 77.147 41.164 1.00 17.38 O ANISOU 1487 O LEU C 193 2209 2474 1921 46 -73 100 O ATOM 1488 CB LEU A 193 46.830 76.016 38.073 1.00 14.32 C ANISOU 1488 CB LEU C 193 1944 1915 1582 -113 -284 -53 C ATOM 1489 CG LEU A 193 45.389 76.502 38.228 1.00 16.03 C ANISOU 1489 CG LEU C 193 2128 2024 1938 0 -56 -15 C ATOM 1490 CD1 LEU A 193 45.299 78.038 38.170 1.00 19.18 C ANISOU 1490 CD1 LEU C 193 2423 2341 2522 -69 119 -200 C ATOM 1491 CD2 LEU A 193 44.466 75.830 37.230 1.00 16.27 C ANISOU 1491 CD2 LEU C 193 2047 2152 1981 -31 -104 31 C ATOM 1492 N ARG A 194 47.212 74.979 40.875 1.00 18.98 N ANISOU 1492 N ARG C 194 2486 2295 2430 -47 -27 102 N ATOM 1493 CA ARG A 194 46.768 74.592 42.218 1.00 20.22 C ANISOU 1493 CA ARG C 194 2635 2586 2462 16 -34 116 C ATOM 1494 C ARG A 194 47.532 75.342 43.335 1.00 20.23 C ANISOU 1494 C ARG C 194 2614 2501 2570 -19 -2 132 C ATOM 1495 O ARG A 194 46.943 75.874 44.289 1.00 19.54 O ANISOU 1495 O ARG C 194 2690 2230 2503 158 -119 409 O ATOM 1496 CB ARG A 194 46.967 73.091 42.410 1.00 20.90 C ANISOU 1496 CB ARG C 194 2803 2527 2609 -118 42 32 C ATOM 1497 CG ARG A 194 46.358 72.602 43.711 1.00 22.20 C ANISOU 1497 CG ARG C 194 3008 2728 2699 24 -131 229 C ATOM 1498 CD ARG A 194 47.017 71.332 44.247 1.00 28.25 C ANISOU 1498 CD ARG C 194 3342 4045 3345 -212 -116 -229 C ATOM 1499 NE ARG A 194 46.170 70.372 44.978 1.00 36.79 N ANISOU 1499 NE ARG C 194 4440 5108 4428 270 -489 135 N ATOM 1500 CZ ARG A 194 44.927 70.527 45.501 1.00 43.70 C ANISOU 1500 CZ ARG C 194 5475 5611 5516 -84 -110 213 C ATOM 1501 NH1 ARG A 194 44.230 71.670 45.480 1.00 47.26 N ANISOU 1501 NH1 ARG C 194 5982 5924 6051 -222 -85 182 N ATOM 1502 NH2 ARG A 194 44.351 69.479 46.102 1.00 41.98 N ANISOU 1502 NH2 ARG C 194 5390 5146 5413 228 118 187 N ATOM 1503 N TRP A 195 48.851 75.374 43.191 1.00 19.76 N ANISOU 1503 N TRP C 195 2583 2431 2492 73 -40 165 N ATOM 1504 CA TRP A 195 49.761 75.953 44.167 1.00 20.34 C ANISOU 1504 CA TRP C 195 2678 2608 2439 28 0 114 C ATOM 1505 C TRP A 195 49.497 77.451 44.359 1.00 20.04 C ANISOU 1505 C TRP C 195 2543 2570 2498 14 -52 9 C ATOM 1506 O TRP A 195 49.355 77.925 45.510 1.00 20.87 O ANISOU 1506 O TRP C 195 2540 2633 2757 -53 -69 147 O ATOM 1507 CB TRP A 195 51.197 75.665 43.709 1.00 19.88 C ANISOU 1507 CB TRP C 195 2512 2595 2445 1 -154 -60 C ATOM 1508 CG TRP A 195 52.302 76.141 44.553 1.00 20.66 C ANISOU 1508 CG TRP C 195 2624 2599 2623 -46 -72 -50 C ATOM 1509 CD1 TRP A 195 52.409 76.047 45.905 1.00 20.27 C ANISOU 1509 CD1 TRP C 195 2637 2635 2429 -32 88 -18 C ATOM 1510 CD2 TRP A 195 53.533 76.711 44.084 1.00 19.98 C ANISOU 1510 CD2 TRP C 195 2307 2673 2608 -74 -56 -28 C ATOM 1511 NE1 TRP A 195 53.637 76.536 46.318 1.00 22.52 N ANISOU 1511 NE1 TRP C 195 3058 2952 2544 25 -141 -71 N ATOM 1512 CE2 TRP A 195 54.335 76.970 45.223 1.00 22.73 C ANISOU 1512 CE2 TRP C 195 2948 2703 2985 6 56 -48 C ATOM 1513 CE3 TRP A 195 54.027 77.044 42.826 1.00 18.85 C ANISOU 1513 CE3 TRP C 195 2193 2590 2380 73 147 -86 C ATOM 1514 CZ2 TRP A 195 55.596 77.542 45.132 1.00 20.49 C ANISOU 1514 CZ2 TRP C 195 2517 2627 2639 -65 2 -60 C ATOM 1515 CZ3 TRP A 195 55.300 77.605 42.735 1.00 20.61 C ANISOU 1515 CZ3 TRP C 195 2725 2660 2444 83 -21 16 C ATOM 1516 CH2 TRP A 195 56.059 77.866 43.885 1.00 21.85 C ANISOU 1516 CH2 TRP C 195 2864 2735 2701 146 -105 22 C ATOM 1517 N CYS A 196 49.404 78.160 43.239 1.00 21.71 N ANISOU 1517 N CYS C 196 2746 2582 2917 91 -17 55 N ATOM 1518 CA CYS A 196 49.066 79.587 43.173 1.00 21.45 C ANISOU 1518 CA CYS C 196 2690 2719 2738 19 99 27 C ATOM 1519 C CYS A 196 47.652 79.873 43.670 1.00 21.55 C ANISOU 1519 C CYS C 196 2670 2741 2774 -13 170 35 C ATOM 1520 O CYS A 196 47.424 80.878 44.364 1.00 21.25 O ANISOU 1520 O CYS C 196 2826 2726 2519 16 397 214 O ATOM 1521 CB CYS A 196 49.209 80.091 41.711 1.00 20.53 C ANISOU 1521 CB CYS C 196 2550 2635 2616 31 215 -39 C ATOM 1522 SG CYS A 196 50.916 80.200 41.138 1.00 21.94 S ANISOU 1522 SG CYS C 196 2422 2849 3065 203 149 3 S ATOM 1523 N ALA A 197 46.705 79.002 43.315 1.00 21.67 N ANISOU 1523 N ALA C 197 2669 2699 2864 -6 221 -4 N ATOM 1524 CA ALA A 197 45.299 79.175 43.689 1.00 23.73 C ANISOU 1524 CA ALA C 197 3000 2895 3121 -39 161 42 C ATOM 1525 C ALA A 197 45.052 79.065 45.177 1.00 25.22 C ANISOU 1525 C ALA C 197 3253 3092 3235 5 160 35 C ATOM 1526 O ALA A 197 44.175 79.756 45.714 1.00 26.31 O ANISOU 1526 O ALA C 197 3420 3303 3271 -87 369 -15 O ATOM 1527 CB ALA A 197 44.426 78.180 42.959 1.00 24.67 C ANISOU 1527 CB ALA C 197 3237 2705 3432 -35 217 89 C ATOM 1528 N LYS A 198 45.789 78.187 45.843 1.00 25.90 N ANISOU 1528 N LYS C 198 3350 3277 3214 -41 125 50 N ATOM 1529 CA LYS A 198 45.651 78.024 47.285 1.00 29.20 C ANISOU 1529 CA LYS C 198 3766 3782 3545 -17 24 0 C ATOM 1530 C LYS A 198 46.019 79.305 48.052 1.00 30.58 C ANISOU 1530 C LYS C 198 3871 4062 3685 -26 15 87 C ATOM 1531 O LYS A 198 45.548 79.526 49.158 1.00 33.21 O ANISOU 1531 O LYS C 198 4271 4544 3802 -171 -130 117 O ATOM 1532 CB LYS A 198 46.500 76.841 47.770 1.00 30.64 C ANISOU 1532 CB LYS C 198 3995 4048 3599 -70 62 7 C ATOM 1533 CG LYS A 198 45.835 75.503 47.570 1.00 32.00 C ANISOU 1533 CG LYS C 198 3996 4129 4032 -110 -52 32 C ATOM 1534 CD LYS A 198 46.759 74.370 48.033 1.00 34.34 C ANISOU 1534 CD LYS C 198 4165 4564 4316 -142 -132 -16 C ATOM 1535 CE LYS A 198 46.072 72.989 47.930 1.00 38.46 C ANISOU 1535 CE LYS C 198 4496 5137 4977 184 -51 -94 C ATOM 1536 NZ LYS A 198 44.666 72.974 48.484 1.00 43.02 N ANISOU 1536 NZ LYS C 198 5467 5402 5476 17 -286 53 N ATOM 1537 N ALA A 199 46.865 80.139 47.465 1.00 29.30 N ANISOU 1537 N ALA C 199 3738 3873 3521 -23 30 67 N ATOM 1538 CA ALA A 199 47.268 81.385 48.078 1.00 28.80 C ANISOU 1538 CA ALA C 199 3694 3668 3577 -41 1 -6 C ATOM 1539 C ALA A 199 46.343 82.565 47.754 1.00 27.92 C ANISOU 1539 C ALA C 199 3596 3449 3561 -57 108 31 C ATOM 1540 O ALA A 199 46.479 83.616 48.356 1.00 27.79 O ANISOU 1540 O ALA C 199 3727 3235 3595 -241 289 155 O ATOM 1541 CB ALA A 199 48.672 81.712 47.631 1.00 29.28 C ANISOU 1541 CB ALA C 199 3838 3553 3735 -37 127 -50 C ATOM 1542 N ALA A 200 45.447 82.423 46.776 1.00 26.77 N ANISOU 1542 N ALA C 200 3369 3339 3462 -49 27 104 N ATOM 1543 CA ALA A 200 44.836 83.594 46.149 1.00 26.76 C ANISOU 1543 CA ALA C 200 3390 3367 3408 -39 19 92 C ATOM 1544 C ALA A 200 43.560 84.026 46.856 1.00 26.69 C ANISOU 1544 C ALA C 200 3330 3346 3462 -26 -20 126 C ATOM 1545 O ALA A 200 42.755 83.179 47.202 1.00 27.54 O ANISOU 1545 O ALA C 200 3445 3311 3707 -21 14 355 O ATOM 1546 CB ALA A 200 44.534 83.308 44.715 1.00 24.89 C ANISOU 1546 CB ALA C 200 3012 3219 3225 -54 5 77 C ATOM 1547 N SER A 201 43.398 85.338 47.065 1.00 26.42 N ANISOU 1547 N SER C 201 3383 3399 3254 -64 -3 23 N ATOM 1548 CA ASER A 201 42.140 85.907 47.534 0.50 26.50 C ANISOU 1548 CA ASER C 201 3394 3403 3269 -58 18 49 C ATOM 1549 C SER A 201 41.287 86.436 46.364 1.00 26.17 C ANISOU 1549 C SER C 201 3396 3368 3178 -103 64 81 C ATOM 1550 O SER A 201 40.077 86.634 46.499 1.00 27.87 O ANISOU 1550 O SER C 201 3867 3645 3074 -145 62 226 O ATOM 1551 CB ASER A 201 42.427 87.006 48.568 0.50 27.45 C ANISOU 1551 CB ASER C 201 3538 3572 3320 -6 48 42 C ATOM 1552 OG ASER A 201 43.039 86.459 49.742 0.50 28.63 O ANISOU 1552 OG ASER C 201 3480 3789 3608 -261 -114 155 O ATOM 1553 N LYS A 202 41.898 86.616 45.199 1.00 25.62 N ANISOU 1553 N LYS C 202 3121 3271 3341 -77 70 10 N ATOM 1554 CA LYS A 202 41.188 87.109 44.036 1.00 24.61 C ANISOU 1554 CA LYS C 202 3121 3135 3094 -107 92 84 C ATOM 1555 C LYS A 202 41.151 86.064 42.896 1.00 23.01 C ANISOU 1555 C LYS C 202 2899 2782 3061 -56 56 96 C ATOM 1556 O LYS A 202 41.926 85.117 42.933 1.00 22.66 O ANISOU 1556 O LYS C 202 2873 2718 3019 -93 283 320 O ATOM 1557 CB LYS A 202 41.859 88.401 43.599 1.00 24.62 C ANISOU 1557 CB LYS C 202 3127 2895 3333 -74 149 67 C ATOM 1558 CG LYS A 202 41.786 89.467 44.685 1.00 27.67 C ANISOU 1558 CG LYS C 202 3098 3775 3640 47 34 3 C ATOM 1559 CD LYS A 202 42.436 90.768 44.295 1.00 27.36 C ANISOU 1559 CD LYS C 202 3420 3623 3352 17 68 -76 C ATOM 1560 CE LYS A 202 42.241 91.845 45.434 1.00 28.54 C ANISOU 1560 CE LYS C 202 3339 3885 3619 -24 244 -220 C ATOM 1561 NZ LYS A 202 43.090 93.046 45.153 1.00 27.31 N ANISOU 1561 NZ LYS C 202 2941 3879 3556 -107 226 9 N ATOM 1562 N PRO A 203 40.232 86.215 41.914 1.00 21.03 N ANISOU 1562 N PRO C 203 2745 2599 2646 -77 80 181 N ATOM 1563 CA PRO A 203 40.165 85.298 40.775 1.00 22.56 C ANISOU 1563 CA PRO C 203 2841 2742 2985 -66 19 77 C ATOM 1564 C PRO A 203 41.504 85.071 40.039 1.00 19.88 C ANISOU 1564 C PRO C 203 2581 2528 2441 44 -21 168 C ATOM 1565 O PRO A 203 42.347 85.980 39.949 1.00 18.19 O ANISOU 1565 O PRO C 203 2184 2374 2353 5 -193 121 O ATOM 1566 CB PRO A 203 39.154 85.956 39.829 1.00 21.75 C ANISOU 1566 CB PRO C 203 2536 2725 3001 -143 29 -5 C ATOM 1567 CG PRO A 203 38.309 86.786 40.704 1.00 21.71 C ANISOU 1567 CG PRO C 203 3058 2657 2531 -143 87 145 C ATOM 1568 CD PRO A 203 39.177 87.252 41.837 1.00 21.94 C ANISOU 1568 CD PRO C 203 2763 2652 2918 -47 34 22 C ATOM 1569 N ILE A 204 41.672 83.847 39.562 1.00 19.24 N ANISOU 1569 N ILE C 204 2415 2420 2475 40 -154 53 N ATOM 1570 CA ILE A 204 42.792 83.472 38.718 1.00 21.26 C ANISOU 1570 CA ILE C 204 2619 2706 2750 -59 -34 48 C ATOM 1571 C ILE A 204 42.358 83.087 37.299 1.00 20.10 C ANISOU 1571 C ILE C 204 2373 2544 2716 -50 12 -18 C ATOM 1572 O ILE A 204 41.368 82.334 37.105 1.00 21.01 O ANISOU 1572 O ILE C 204 2342 2505 3133 -81 60 236 O ATOM 1573 CB ILE A 204 43.615 82.329 39.369 1.00 20.75 C ANISOU 1573 CB ILE C 204 2514 2625 2741 -130 -38 18 C ATOM 1574 CG1 ILE A 204 44.547 82.901 40.444 1.00 21.02 C ANISOU 1574 CG1 ILE C 204 2801 2841 2343 -266 165 249 C ATOM 1575 CG2 ILE A 204 44.507 81.603 38.346 1.00 18.08 C ANISOU 1575 CG2 ILE C 204 2512 2418 1940 104 -95 -151 C ATOM 1576 CD1 ILE A 204 45.094 81.870 41.335 1.00 26.16 C ANISOU 1576 CD1 ILE C 204 3353 3255 3332 -232 -108 -88 C ATOM 1577 N ILE A 205 43.078 83.643 36.318 1.00 18.79 N ANISOU 1577 N ILE C 205 2307 2372 2458 -10 125 35 N ATOM 1578 CA ILE A 205 43.011 83.205 34.917 1.00 18.80 C ANISOU 1578 CA ILE C 205 2343 2390 2408 21 46 12 C ATOM 1579 C ILE A 205 44.155 82.222 34.670 1.00 17.01 C ANISOU 1579 C ILE C 205 2234 2280 1946 69 -34 87 C ATOM 1580 O ILE A 205 45.330 82.586 34.790 1.00 17.97 O ANISOU 1580 O ILE C 205 2146 2335 2346 87 -7 83 O ATOM 1581 CB ILE A 205 43.099 84.382 33.888 1.00 17.77 C ANISOU 1581 CB ILE C 205 2337 2465 1950 51 186 88 C ATOM 1582 CG1 ILE A 205 42.038 85.452 34.176 1.00 22.04 C ANISOU 1582 CG1 ILE C 205 2948 2632 2791 -49 -176 -256 C ATOM 1583 CG2 ILE A 205 43.009 83.849 32.392 1.00 18.92 C ANISOU 1583 CG2 ILE C 205 2441 2434 2314 -188 261 -26 C ATOM 1584 CD1 ILE A 205 41.888 86.470 33.075 1.00 24.15 C ANISOU 1584 CD1 ILE C 205 2775 3126 3274 -153 -37 109 C ATOM 1585 N ALA A 206 43.814 80.970 34.379 1.00 16.54 N ANISOU 1585 N ALA C 206 2258 2264 1760 82 -65 74 N ATOM 1586 CA ALA A 206 44.812 79.918 34.114 1.00 17.93 C ANISOU 1586 CA ALA C 206 2297 2313 2201 29 -27 15 C ATOM 1587 C ALA A 206 45.243 80.018 32.666 1.00 19.24 C ANISOU 1587 C ALA C 206 2521 2427 2360 106 -12 -14 C ATOM 1588 O ALA A 206 44.413 79.930 31.775 1.00 19.89 O ANISOU 1588 O ALA C 206 2776 2233 2547 94 138 -427 O ATOM 1589 CB ALA A 206 44.221 78.574 34.353 1.00 18.77 C ANISOU 1589 CB ALA C 206 2343 2558 2230 74 -69 228 C ATOM 1590 N ASP A 207 46.529 80.219 32.413 1.00 19.63 N ANISOU 1590 N ASP C 207 2573 2329 2554 -34 -78 -36 N ATOM 1591 CA ASP A 207 46.959 80.595 31.042 1.00 18.98 C ANISOU 1591 CA ASP C 207 2477 2435 2299 70 -31 -14 C ATOM 1592 C ASP A 207 47.851 79.528 30.414 1.00 20.69 C ANISOU 1592 C ASP C 207 2765 2650 2443 58 20 2 C ATOM 1593 O ASP A 207 49.053 79.465 30.691 1.00 20.92 O ANISOU 1593 O ASP C 207 2831 2812 2303 -65 -92 12 O ATOM 1594 CB ASP A 207 47.645 81.989 31.069 1.00 19.45 C ANISOU 1594 CB ASP C 207 2470 2492 2427 -130 -44 136 C ATOM 1595 CG ASP A 207 48.048 82.511 29.674 1.00 20.16 C ANISOU 1595 CG ASP C 207 2489 2790 2380 189 -157 -220 C ATOM 1596 OD1 ASP A 207 47.721 81.891 28.628 1.00 21.18 O ANISOU 1596 OD1 ASP C 207 2697 2891 2456 -133 220 256 O ATOM 1597 OD2 ASP A 207 48.736 83.574 29.640 1.00 17.47 O ANISOU 1597 OD2 ASP C 207 2855 2718 1062 -76 -377 -20 O ATOM 1598 N GLY A 208 47.259 78.682 29.563 1.00 22.46 N ANISOU 1598 N GLY C 208 2849 2807 2877 80 80 19 N ATOM 1599 CA GLY A 208 48.044 77.815 28.677 1.00 21.84 C ANISOU 1599 CA GLY C 208 2706 2915 2675 111 100 -79 C ATOM 1600 C GLY A 208 48.179 76.373 29.162 1.00 23.56 C ANISOU 1600 C GLY C 208 2899 3076 2976 6 35 -89 C ATOM 1601 O GLY A 208 47.684 76.016 30.221 1.00 23.32 O ANISOU 1601 O GLY C 208 2644 3189 3026 -69 -153 -139 O ATOM 1602 N GLY A 209 48.828 75.548 28.346 1.00 24.76 N ANISOU 1602 N GLY C 209 3004 3151 3253 -67 80 -16 N ATOM 1603 CA GLY A 209 48.900 74.114 28.593 1.00 24.68 C ANISOU 1603 CA GLY C 209 3029 3212 3135 -37 -49 -12 C ATOM 1604 C GLY A 209 47.604 73.339 28.366 1.00 25.60 C ANISOU 1604 C GLY C 209 3203 3296 3229 -47 -78 36 C ATOM 1605 O GLY A 209 47.545 72.141 28.649 1.00 27.57 O ANISOU 1605 O GLY C 209 3326 3553 3593 -159 -224 68 O ATOM 1606 N ILE A 210 46.575 73.987 27.817 1.00 23.97 N ANISOU 1606 N ILE C 210 3134 3187 2785 -42 -35 95 N ATOM 1607 CA ILE A 210 45.301 73.328 27.589 1.00 26.01 C ANISOU 1607 CA ILE C 210 3351 3400 3130 -3 -45 13 C ATOM 1608 C ILE A 210 45.394 72.568 26.269 1.00 26.85 C ANISOU 1608 C ILE C 210 3454 3512 3233 91 26 9 C ATOM 1609 O ILE A 210 45.679 73.160 25.228 1.00 28.81 O ANISOU 1609 O ILE C 210 3697 3730 3517 158 -198 -220 O ATOM 1610 CB ILE A 210 44.141 74.354 27.520 1.00 26.21 C ANISOU 1610 CB ILE C 210 3393 3347 3217 33 55 20 C ATOM 1611 CG1 ILE A 210 44.129 75.255 28.775 1.00 25.63 C ANISOU 1611 CG1 ILE C 210 3508 3239 2990 -169 -99 226 C ATOM 1612 CG2 ILE A 210 42.830 73.665 27.274 1.00 25.30 C ANISOU 1612 CG2 ILE C 210 3312 3260 3040 90 -216 20 C ATOM 1613 CD1 ILE A 210 44.237 74.529 30.051 1.00 26.31 C ANISOU 1613 CD1 ILE C 210 3627 3358 3012 -73 -203 -91 C ATOM 1614 N ARG A 211 45.186 71.261 26.315 1.00 26.58 N ANISOU 1614 N ARG C 211 3359 3440 3297 110 -31 58 N ATOM 1615 CA ARG A 211 45.225 70.440 25.095 1.00 28.21 C ANISOU 1615 CA ARG C 211 3578 3634 3505 136 -23 45 C ATOM 1616 C ARG A 211 43.886 69.814 24.662 1.00 26.73 C ANISOU 1616 C ARG C 211 3409 3530 3216 96 1 1 C ATOM 1617 O ARG A 211 43.732 69.430 23.513 1.00 25.19 O ANISOU 1617 O ARG C 211 3372 3463 2735 350 -130 -141 O ATOM 1618 CB ARG A 211 46.271 69.359 25.276 1.00 28.96 C ANISOU 1618 CB ARG C 211 3733 3572 3697 50 -28 25 C ATOM 1619 CG ARG A 211 47.636 69.929 25.615 1.00 33.14 C ANISOU 1619 CG ARG C 211 4167 4197 4225 175 47 -125 C ATOM 1620 CD ARG A 211 48.574 68.836 26.088 1.00 37.95 C ANISOU 1620 CD ARG C 211 4953 4499 4964 39 -265 -171 C ATOM 1621 NE ARG A 211 48.916 67.899 25.025 1.00 48.48 N ANISOU 1621 NE ARG C 211 6042 6350 6026 -71 209 128 N ATOM 1622 CZ ARG A 211 49.718 66.848 25.186 1.00 52.32 C ANISOU 1622 CZ ARG C 211 6530 6719 6629 -224 79 -10 C ATOM 1623 NH1 ARG A 211 50.269 66.584 26.373 1.00 54.37 N ANISOU 1623 NH1 ARG C 211 7025 6934 6697 -116 75 -11 N ATOM 1624 NH2 ARG A 211 49.966 66.050 24.154 1.00 52.21 N ANISOU 1624 NH2 ARG C 211 6561 6672 6604 -222 -24 121 N ATOM 1625 N THR A 212 42.936 69.722 25.587 1.00 25.78 N ANISOU 1625 N THR C 212 3311 3346 3137 126 -25 -24 N ATOM 1626 CA THR A 212 41.635 69.071 25.363 1.00 24.99 C ANISOU 1626 CA THR C 212 3191 3235 3067 21 -18 -2 C ATOM 1627 C THR A 212 40.578 69.905 26.068 1.00 23.06 C ANISOU 1627 C THR C 212 2931 3024 2805 45 -64 -36 C ATOM 1628 O THR A 212 40.905 70.691 26.973 1.00 18.89 O ANISOU 1628 O THR C 212 2894 2635 1646 27 -241 -174 O ATOM 1629 CB THR A 212 41.563 67.640 25.985 1.00 24.36 C ANISOU 1629 CB THR C 212 3075 3125 3054 114 44 -17 C ATOM 1630 OG1 THR A 212 41.683 67.733 27.419 1.00 25.87 O ANISOU 1630 OG1 THR C 212 3282 3494 3054 116 -487 -80 O ATOM 1631 CG2 THR A 212 42.651 66.757 25.491 1.00 25.97 C ANISOU 1631 CG2 THR C 212 3065 3368 3433 157 110 68 C ATOM 1632 N ASN A 213 39.320 69.738 25.674 1.00 21.88 N ANISOU 1632 N ASN C 213 2774 2873 2665 98 -129 1 N ATOM 1633 CA ASN A 213 38.231 70.389 26.408 1.00 22.83 C ANISOU 1633 CA ASN C 213 2839 2917 2915 66 -19 -56 C ATOM 1634 C ASN A 213 38.121 69.897 27.858 1.00 22.00 C ANISOU 1634 C ASN C 213 2749 2733 2875 78 74 -14 C ATOM 1635 O ASN A 213 37.717 70.676 28.720 1.00 23.17 O ANISOU 1635 O ASN C 213 2773 3065 2965 1 137 64 O ATOM 1636 CB ASN A 213 36.882 70.267 25.667 1.00 23.87 C ANISOU 1636 CB ASN C 213 2921 3118 3030 33 -77 -169 C ATOM 1637 CG ASN A 213 36.854 71.034 24.348 1.00 23.43 C ANISOU 1637 CG ASN C 213 3347 3004 2549 177 -13 94 C ATOM 1638 OD1 ASN A 213 37.786 71.755 24.020 1.00 26.73 O ANISOU 1638 OD1 ASN C 213 3604 3300 3251 353 29 -235 O ATOM 1639 ND2 ASN A 213 35.748 70.899 23.602 1.00 23.92 N ANISOU 1639 ND2 ASN C 213 3317 2916 2854 -75 -123 -6 N ATOM 1640 N GLY A 214 38.520 68.642 28.143 1.00 19.66 N ANISOU 1640 N GLY C 214 2545 2397 2529 124 49 -53 N ATOM 1641 CA GLY A 214 38.533 68.136 29.509 1.00 20.57 C ANISOU 1641 CA GLY C 214 2547 2484 2783 37 53 -34 C ATOM 1642 C GLY A 214 39.480 68.896 30.413 1.00 19.79 C ANISOU 1642 C GLY C 214 2456 2416 2646 -65 -31 -29 C ATOM 1643 O GLY A 214 39.278 68.951 31.600 1.00 18.54 O ANISOU 1643 O GLY C 214 2242 2154 2648 -57 159 -6 O ATOM 1644 N ASP A 215 40.493 69.537 29.840 1.00 20.26 N ANISOU 1644 N ASP C 215 2606 2265 2825 -90 82 -107 N ATOM 1645 CA ASP A 215 41.425 70.348 30.639 1.00 19.88 C ANISOU 1645 CA ASP C 215 2542 2409 2602 -47 59 -132 C ATOM 1646 C ASP A 215 40.825 71.633 31.189 1.00 19.03 C ANISOU 1646 C ASP C 215 2610 2230 2388 -6 60 32 C ATOM 1647 O ASP A 215 41.321 72.193 32.178 1.00 19.29 O ANISOU 1647 O ASP C 215 2527 2310 2490 9 188 33 O ATOM 1648 CB ASP A 215 42.674 70.673 29.808 1.00 19.48 C ANISOU 1648 CB ASP C 215 2576 2352 2473 49 -24 -42 C ATOM 1649 CG ASP A 215 43.523 69.435 29.492 1.00 19.95 C ANISOU 1649 CG ASP C 215 2470 2574 2533 43 -142 -195 C ATOM 1650 OD1 ASP A 215 43.430 68.430 30.246 1.00 17.30 O ANISOU 1650 OD1 ASP C 215 2243 2059 2270 150 50 -421 O ATOM 1651 OD2 ASP A 215 44.294 69.473 28.486 1.00 24.90 O ANISOU 1651 OD2 ASP C 215 2913 3302 3243 -195 88 377 O ATOM 1652 N VAL A 216 39.751 72.100 30.577 1.00 19.26 N ANISOU 1652 N VAL C 216 2439 2459 2421 -70 13 6 N ATOM 1653 CA VAL A 216 38.966 73.199 31.167 1.00 19.52 C ANISOU 1653 CA VAL C 216 2523 2365 2527 -51 13 -22 C ATOM 1654 C VAL A 216 38.372 72.779 32.526 1.00 18.71 C ANISOU 1654 C VAL C 216 2333 2221 2553 -138 -38 -87 C ATOM 1655 O VAL A 216 38.558 73.479 33.526 1.00 16.40 O ANISOU 1655 O VAL C 216 2257 1673 2299 -47 52 -214 O ATOM 1656 CB VAL A 216 37.877 73.742 30.168 1.00 20.38 C ANISOU 1656 CB VAL C 216 2515 2543 2685 -58 -56 5 C ATOM 1657 CG1 VAL A 216 37.104 74.874 30.764 1.00 19.57 C ANISOU 1657 CG1 VAL C 216 2611 2411 2414 -37 299 54 C ATOM 1658 CG2 VAL A 216 38.531 74.212 28.897 1.00 20.99 C ANISOU 1658 CG2 VAL C 216 3147 2750 2076 -186 -136 -104 C ATOM 1659 N ALA A 217 37.643 71.662 32.588 1.00 18.42 N ANISOU 1659 N ALA C 217 2197 2288 2512 -123 55 -34 N ATOM 1660 CA ALA A 217 37.147 71.155 33.903 1.00 17.98 C ANISOU 1660 CA ALA C 217 2159 2183 2487 -102 81 73 C ATOM 1661 C ALA A 217 38.247 70.945 34.964 1.00 16.09 C ANISOU 1661 C ALA C 217 2037 2115 1961 100 229 237 C ATOM 1662 O ALA A 217 38.094 71.301 36.176 1.00 14.60 O ANISOU 1662 O ALA C 217 2185 1790 1572 100 230 -48 O ATOM 1663 CB ALA A 217 36.352 69.849 33.660 1.00 19.60 C ANISOU 1663 CB ALA C 217 2266 2348 2832 -37 76 -9 C ATOM 1664 N LYS A 218 39.369 70.367 34.519 1.00 17.22 N ANISOU 1664 N LYS C 218 2007 2127 2408 -46 131 31 N ATOM 1665 CA LYS A 218 40.533 70.164 35.357 1.00 16.24 C ANISOU 1665 CA LYS C 218 2121 2033 2015 -49 98 31 C ATOM 1666 C LYS A 218 41.056 71.492 35.893 1.00 17.48 C ANISOU 1666 C LYS C 218 2125 2131 2384 -19 -22 73 C ATOM 1667 O LYS A 218 41.350 71.561 37.073 1.00 15.71 O ANISOU 1667 O LYS C 218 2096 1789 2083 -129 108 87 O ATOM 1668 CB LYS A 218 41.665 69.380 34.670 1.00 14.96 C ANISOU 1668 CB LYS C 218 2008 1759 1915 -71 36 -107 C ATOM 1669 CG LYS A 218 41.275 67.990 34.194 1.00 16.81 C ANISOU 1669 CG LYS C 218 2136 1746 2505 41 -30 -39 C ATOM 1670 CD LYS A 218 42.390 67.265 33.484 1.00 15.69 C ANISOU 1670 CD LYS C 218 2055 1930 1976 -98 -105 54 C ATOM 1671 CE LYS A 218 41.911 65.975 32.863 1.00 19.15 C ANISOU 1671 CE LYS C 218 2419 2496 2358 -204 150 143 C ATOM 1672 NZ LYS A 218 42.917 65.269 31.990 1.00 22.02 N ANISOU 1672 NZ LYS C 218 2927 2416 3021 -294 166 299 N ATOM 1673 N SER A 219 41.158 72.531 35.045 1.00 18.33 N ANISOU 1673 N SER C 219 2077 2442 2443 -22 26 12 N ATOM 1674 CA SER A 219 41.584 73.874 35.526 1.00 17.46 C ANISOU 1674 CA SER C 219 2207 2121 2303 28 69 -35 C ATOM 1675 C SER A 219 40.609 74.443 36.598 1.00 16.85 C ANISOU 1675 C SER C 219 2177 2081 2143 -28 163 -89 C ATOM 1676 O SER A 219 41.042 74.994 37.609 1.00 17.17 O ANISOU 1676 O SER C 219 2294 2004 2226 72 168 -77 O ATOM 1677 CB SER A 219 41.717 74.860 34.358 1.00 18.11 C ANISOU 1677 CB SER C 219 2042 2350 2488 1 -25 97 C ATOM 1678 OG SER A 219 42.496 74.354 33.274 1.00 18.54 O ANISOU 1678 OG SER C 219 1877 2540 2624 172 -180 329 O ATOM 1679 N ILE A 220 39.304 74.248 36.389 1.00 16.68 N ANISOU 1679 N ILE C 220 2070 2107 2160 76 82 50 N ATOM 1680 CA ILE A 220 38.276 74.656 37.344 1.00 18.25 C ANISOU 1680 CA ILE C 220 2346 2152 2435 45 122 58 C ATOM 1681 C ILE A 220 38.451 73.907 38.671 1.00 17.87 C ANISOU 1681 C ILE C 220 2356 2035 2396 -24 91 67 C ATOM 1682 O ILE A 220 38.485 74.541 39.737 1.00 17.63 O ANISOU 1682 O ILE C 220 2357 1681 2659 -26 283 249 O ATOM 1683 CB ILE A 220 36.818 74.471 36.796 1.00 19.14 C ANISOU 1683 CB ILE C 220 2526 2363 2383 -176 76 65 C ATOM 1684 CG1 ILE A 220 36.569 75.360 35.548 1.00 23.12 C ANISOU 1684 CG1 ILE C 220 2682 3000 3099 -71 -112 102 C ATOM 1685 CG2 ILE A 220 35.792 74.795 37.897 1.00 18.47 C ANISOU 1685 CG2 ILE C 220 2292 2235 2489 -14 -214 195 C ATOM 1686 CD1 ILE A 220 36.709 76.859 35.814 1.00 24.73 C ANISOU 1686 CD1 ILE C 220 3028 2881 3487 7 36 -168 C ATOM 1687 N ARG A 221 38.633 72.580 38.629 1.00 17.86 N ANISOU 1687 N ARG C 221 2361 2158 2266 154 71 63 N ATOM 1688 CA ARG A 221 38.878 71.800 39.866 1.00 18.28 C ANISOU 1688 CA ARG C 221 2314 2207 2424 -2 75 55 C ATOM 1689 C ARG A 221 39.997 72.386 40.697 1.00 16.86 C ANISOU 1689 C ARG C 221 2072 2333 2001 -48 33 120 C ATOM 1690 O ARG A 221 39.853 72.505 41.924 1.00 17.48 O ANISOU 1690 O ARG C 221 2150 2662 1827 -137 -62 -13 O ATOM 1691 CB ARG A 221 39.201 70.321 39.544 1.00 18.86 C ANISOU 1691 CB ARG C 221 2176 2244 2745 118 -69 84 C ATOM 1692 CG ARG A 221 39.658 69.494 40.730 1.00 18.53 C ANISOU 1692 CG ARG C 221 2372 2387 2279 43 214 6 C ATOM 1693 CD ARG A 221 38.651 69.569 41.884 1.00 21.86 C ANISOU 1693 CD ARG C 221 2532 2551 3221 -88 4 244 C ATOM 1694 NE ARG A 221 38.984 68.746 43.027 1.00 20.04 N ANISOU 1694 NE ARG C 221 2538 2573 2502 1 244 84 N ATOM 1695 CZ ARG A 221 39.803 69.093 44.023 1.00 24.39 C ANISOU 1695 CZ ARG C 221 3160 3247 2861 32 167 -95 C ATOM 1696 NH1 ARG A 221 40.425 70.281 44.052 1.00 22.98 N ANISOU 1696 NH1 ARG C 221 3456 2824 2449 60 -129 41 N ATOM 1697 NH2 ARG A 221 39.998 68.229 45.015 1.00 25.28 N ANISOU 1697 NH2 ARG C 221 2871 3331 3401 -158 189 -64 N ATOM 1698 N PHE A 222 41.099 72.751 40.050 1.00 16.79 N ANISOU 1698 N PHE C 222 1880 2174 2322 -212 13 38 N ATOM 1699 CA PHE A 222 42.290 73.202 40.761 1.00 17.66 C ANISOU 1699 CA PHE C 222 2184 2250 2275 -84 -11 29 C ATOM 1700 C PHE A 222 42.434 74.719 40.693 1.00 19.00 C ANISOU 1700 C PHE C 222 2399 2322 2497 26 6 -12 C ATOM 1701 O PHE A 222 43.518 75.259 40.910 1.00 19.72 O ANISOU 1701 O PHE C 222 2678 2281 2532 130 77 139 O ATOM 1702 CB PHE A 222 43.541 72.529 40.192 1.00 17.47 C ANISOU 1702 CB PHE C 222 2388 2072 2177 68 130 113 C ATOM 1703 CG PHE A 222 43.616 71.055 40.472 1.00 17.95 C ANISOU 1703 CG PHE C 222 2431 2337 2053 -243 43 23 C ATOM 1704 CD1 PHE A 222 43.978 70.592 41.725 1.00 21.59 C ANISOU 1704 CD1 PHE C 222 2629 2956 2616 132 -233 -373 C ATOM 1705 CD2 PHE A 222 43.324 70.133 39.481 1.00 21.48 C ANISOU 1705 CD2 PHE C 222 2537 2683 2939 -245 -38 -76 C ATOM 1706 CE1 PHE A 222 44.048 69.236 41.986 1.00 21.05 C ANISOU 1706 CE1 PHE C 222 2442 2499 3055 -7 54 -256 C ATOM 1707 CE2 PHE A 222 43.392 68.776 39.735 1.00 19.45 C ANISOU 1707 CE2 PHE C 222 2418 2616 2354 209 -74 7 C ATOM 1708 CZ PHE A 222 43.755 68.327 40.989 1.00 17.97 C ANISOU 1708 CZ PHE C 222 2547 2190 2090 4 57 17 C ATOM 1709 N GLY A 223 41.333 75.400 40.391 1.00 17.34 N ANISOU 1709 N GLY C 223 2249 2134 2205 -19 -51 91 N ATOM 1710 CA GLY A 223 40.959 76.603 41.112 1.00 17.95 C ANISOU 1710 CA GLY C 223 2321 2236 2261 -108 20 39 C ATOM 1711 C GLY A 223 40.924 77.827 40.218 1.00 19.15 C ANISOU 1711 C GLY C 223 2328 2445 2500 -39 38 3 C ATOM 1712 O GLY A 223 40.948 78.960 40.700 1.00 20.65 O ANISOU 1712 O GLY C 223 2251 2768 2827 -100 124 -63 O ATOM 1713 N ALA A 224 40.865 77.598 38.911 1.00 19.40 N ANISOU 1713 N ALA C 224 2419 2445 2507 -102 19 41 N ATOM 1714 CA ALA A 224 40.739 78.685 37.947 1.00 18.45 C ANISOU 1714 CA ALA C 224 2262 2290 2455 -32 8 24 C ATOM 1715 C ALA A 224 39.332 79.273 37.962 1.00 19.43 C ANISOU 1715 C ALA C 224 2412 2277 2694 -50 -3 25 C ATOM 1716 O ALA A 224 38.368 78.594 38.313 1.00 19.49 O ANISOU 1716 O ALA C 224 2490 2029 2885 -126 -125 206 O ATOM 1717 CB ALA A 224 41.099 78.200 36.551 1.00 19.14 C ANISOU 1717 CB ALA C 224 2317 2307 2645 -63 -53 198 C ATOM 1718 N THR A 225 39.222 80.541 37.578 1.00 17.51 N ANISOU 1718 N THR C 225 2196 2223 2232 41 73 66 N ATOM 1719 CA THR A 225 37.927 81.144 37.286 1.00 17.46 C ANISOU 1719 CA THR C 225 2191 2384 2055 -36 -52 -29 C ATOM 1720 C THR A 225 37.726 81.319 35.785 1.00 18.08 C ANISOU 1720 C THR C 225 2255 2483 2130 41 -123 -202 C ATOM 1721 O THR A 225 36.663 81.004 35.250 1.00 19.48 O ANISOU 1721 O THR C 225 2439 2572 2388 153 -144 35 O ATOM 1722 CB THR A 225 37.790 82.501 38.001 1.00 17.90 C ANISOU 1722 CB THR C 225 2269 2448 2083 -184 -165 -158 C ATOM 1723 OG1 THR A 225 37.579 82.287 39.402 1.00 16.58 O ANISOU 1723 OG1 THR C 225 2373 2230 1695 -289 19 -69 O ATOM 1724 CG2 THR A 225 36.519 83.210 37.559 1.00 19.50 C ANISOU 1724 CG2 THR C 225 2274 2327 2806 -31 68 12 C ATOM 1725 N MET A 226 38.753 81.825 35.110 1.00 19.85 N ANISOU 1725 N MET C 226 2876 2519 2146 16 92 -79 N ATOM 1726 CA MET A 226 38.796 81.806 33.653 1.00 19.68 C ANISOU 1726 CA MET C 226 2669 2544 2264 36 3 -86 C ATOM 1727 C MET A 226 39.994 81.008 33.147 1.00 18.92 C ANISOU 1727 C MET C 226 2543 2478 2166 58 -60 -7 C ATOM 1728 O MET A 226 41.062 81.020 33.758 1.00 18.50 O ANISOU 1728 O MET C 226 2656 2166 2204 40 117 132 O ATOM 1729 CB MET A 226 38.842 83.231 33.099 1.00 22.76 C ANISOU 1729 CB MET C 226 3006 2901 2740 67 -4 -232 C ATOM 1730 CG MET A 226 38.311 83.364 31.682 1.00 26.60 C ANISOU 1730 CG MET C 226 3504 3633 2970 119 -142 -124 C ATOM 1731 SD MET A 226 36.523 83.146 31.585 1.00 28.22 S ANISOU 1731 SD MET C 226 3210 3623 3889 426 -134 -456 S ATOM 1732 CE MET A 226 35.956 84.703 32.266 1.00 34.92 C ANISOU 1732 CE MET C 226 3920 4759 4586 56 -161 142 C ATOM 1733 N VAL A 227 39.807 80.315 32.029 1.00 17.23 N ANISOU 1733 N VAL C 227 2060 2435 2048 40 -212 88 N ATOM 1734 CA VAL A 227 40.886 79.557 31.407 1.00 19.42 C ANISOU 1734 CA VAL C 227 2472 2642 2264 16 -139 0 C ATOM 1735 C VAL A 227 41.264 80.147 30.053 1.00 18.28 C ANISOU 1735 C VAL C 227 2444 2542 1958 -22 13 9 C ATOM 1736 O VAL A 227 40.462 80.145 29.119 1.00 20.34 O ANISOU 1736 O VAL C 227 2654 2830 2243 -112 -107 -187 O ATOM 1737 CB VAL A 227 40.500 78.078 31.221 1.00 19.77 C ANISOU 1737 CB VAL C 227 2626 2608 2275 83 -126 -70 C ATOM 1738 CG1 VAL A 227 41.666 77.292 30.641 1.00 18.45 C ANISOU 1738 CG1 VAL C 227 2076 2979 1953 -91 -241 -161 C ATOM 1739 CG2 VAL A 227 40.045 77.475 32.541 1.00 18.04 C ANISOU 1739 CG2 VAL C 227 2272 2392 2190 -17 -52 -254 C ATOM 1740 N MET A 228 42.489 80.653 29.954 1.00 18.12 N ANISOU 1740 N MET C 228 2337 2607 1940 -72 -110 67 N ATOM 1741 CA MET A 228 42.975 81.257 28.703 1.00 19.84 C ANISOU 1741 CA MET C 228 2572 2567 2397 12 -175 95 C ATOM 1742 C MET A 228 43.555 80.190 27.768 1.00 20.86 C ANISOU 1742 C MET C 228 2692 2716 2517 -42 -151 113 C ATOM 1743 O MET A 228 44.486 79.457 28.143 1.00 20.20 O ANISOU 1743 O MET C 228 2752 2873 2048 -239 -287 32 O ATOM 1744 CB MET A 228 43.983 82.399 28.944 1.00 18.32 C ANISOU 1744 CB MET C 228 2543 2442 1975 -52 -142 283 C ATOM 1745 CG MET A 228 44.525 83.005 27.580 1.00 16.35 C ANISOU 1745 CG MET C 228 2152 2607 1453 -153 -225 19 C ATOM 1746 SD MET A 228 45.457 84.520 27.777 1.00 20.72 S ANISOU 1746 SD MET C 228 2536 2533 2800 -10 -477 232 S ATOM 1747 CE MET A 228 44.118 85.658 28.083 1.00 21.39 C ANISOU 1747 CE MET C 228 2848 2508 2770 39 -254 6 C ATOM 1748 N ILE A 229 43.027 80.151 26.540 1.00 22.18 N ANISOU 1748 N ILE C 229 2839 2866 2721 46 -164 -71 N ATOM 1749 CA ILE A 229 43.320 79.099 25.551 1.00 24.04 C ANISOU 1749 CA ILE C 229 3066 3045 3023 18 -87 12 C ATOM 1750 C ILE A 229 43.896 79.623 24.236 1.00 25.34 C ANISOU 1750 C ILE C 229 3263 3201 3164 14 -126 -17 C ATOM 1751 O ILE A 229 43.314 80.510 23.617 1.00 25.32 O ANISOU 1751 O ILE C 229 3165 3287 3167 214 -226 -30 O ATOM 1752 CB ILE A 229 42.026 78.330 25.231 1.00 24.81 C ANISOU 1752 CB ILE C 229 3107 3265 3052 49 -108 -59 C ATOM 1753 CG1 ILE A 229 41.472 77.725 26.539 1.00 23.75 C ANISOU 1753 CG1 ILE C 229 3056 3198 2769 189 80 70 C ATOM 1754 CG2 ILE A 229 42.264 77.262 24.187 1.00 24.17 C ANISOU 1754 CG2 ILE C 229 3001 3107 3075 35 -75 77 C ATOM 1755 CD1 ILE A 229 40.217 76.857 26.388 1.00 24.18 C ANISOU 1755 CD1 ILE C 229 3201 2997 2988 51 -223 -64 C ATOM 1756 N GLY A 230 45.024 79.044 23.801 1.00 26.47 N ANISOU 1756 N GLY C 230 3397 3472 3189 16 -119 7 N ATOM 1757 CA GLY A 230 45.662 79.396 22.522 1.00 27.38 C ANISOU 1757 CA GLY C 230 3508 3515 3380 66 -43 106 C ATOM 1758 C GLY A 230 45.332 78.401 21.416 1.00 27.26 C ANISOU 1758 C GLY C 230 3588 3566 3202 81 -42 57 C ATOM 1759 O GLY A 230 44.395 78.616 20.651 1.00 28.96 O ANISOU 1759 O GLY C 230 3767 3690 3546 145 -124 108 O ATOM 1760 N SER A 231 46.069 77.292 21.383 1.00 28.64 N ANISOU 1760 N SER C 231 3774 3725 3381 78 -51 50 N ATOM 1761 CA SER A 231 45.982 76.270 20.312 1.00 30.56 C ANISOU 1761 CA SER C 231 3808 4007 3795 42 16 11 C ATOM 1762 C SER A 231 44.573 75.808 19.949 1.00 31.72 C ANISOU 1762 C SER C 231 4016 4109 3925 51 4 -37 C ATOM 1763 O SER A 231 44.268 75.617 18.774 1.00 32.95 O ANISOU 1763 O SER C 231 4134 4388 3997 96 105 -33 O ATOM 1764 CB SER A 231 46.808 75.026 20.678 1.00 31.77 C ANISOU 1764 CB SER C 231 4020 4093 3956 56 -19 -56 C ATOM 1765 OG SER A 231 46.213 74.327 21.782 1.00 38.47 O ANISOU 1765 OG SER C 231 4780 5356 4481 90 29 129 O ATOM 1766 N LEU A 232 43.725 75.581 20.942 1.00 31.93 N ANISOU 1766 N LEU C 232 3992 4129 4009 18 88 12 N ATOM 1767 CA LEU A 232 42.401 75.056 20.643 1.00 32.15 C ANISOU 1767 CA LEU C 232 4030 4121 4064 3 -13 -51 C ATOM 1768 C LEU A 232 41.580 76.071 19.849 1.00 32.02 C ANISOU 1768 C LEU C 232 3969 4086 4109 -14 -16 -102 C ATOM 1769 O LEU A 232 40.660 75.677 19.132 1.00 28.10 O ANISOU 1769 O LEU C 232 3613 3931 3131 -40 -56 -257 O ATOM 1770 CB LEU A 232 41.646 74.598 21.892 1.00 32.74 C ANISOU 1770 CB LEU C 232 3999 4359 4079 -7 32 0 C ATOM 1771 CG LEU A 232 42.033 73.243 22.523 1.00 33.50 C ANISOU 1771 CG LEU C 232 4196 4411 4120 -45 44 -66 C ATOM 1772 CD1 LEU A 232 41.356 73.135 23.877 1.00 31.68 C ANISOU 1772 CD1 LEU C 232 3727 4187 4120 196 -84 55 C ATOM 1773 CD2 LEU A 232 41.629 72.069 21.639 1.00 34.70 C ANISOU 1773 CD2 LEU C 232 4110 4566 4507 -98 -5 -84 C ATOM 1774 N PHE A 233 41.910 77.359 19.986 1.00 32.73 N ANISOU 1774 N PHE C 233 4002 4067 4365 -17 -46 -22 N ATOM 1775 CA PHE A 233 41.219 78.420 19.232 1.00 33.91 C ANISOU 1775 CA PHE C 233 4180 4375 4326 13 -68 -42 C ATOM 1776 C PHE A 233 41.947 78.815 17.962 1.00 34.13 C ANISOU 1776 C PHE C 233 4225 4446 4295 19 -37 -29 C ATOM 1777 O PHE A 233 41.427 79.610 17.176 1.00 33.05 O ANISOU 1777 O PHE C 233 4135 4384 4037 67 9 -60 O ATOM 1778 CB PHE A 233 41.046 79.673 20.099 1.00 33.97 C ANISOU 1778 CB PHE C 233 4156 4366 4383 -14 -54 -32 C ATOM 1779 CG PHE A 233 39.949 79.577 21.128 1.00 32.16 C ANISOU 1779 CG PHE C 233 3961 4069 4189 -3 -37 -26 C ATOM 1780 CD1 PHE A 233 38.650 79.301 20.753 1.00 34.58 C ANISOU 1780 CD1 PHE C 233 4430 4315 4391 107 -47 57 C ATOM 1781 CD2 PHE A 233 40.205 79.855 22.461 1.00 32.99 C ANISOU 1781 CD2 PHE C 233 4181 4142 4208 26 -115 -2 C ATOM 1782 CE1 PHE A 233 37.644 79.248 21.703 1.00 35.67 C ANISOU 1782 CE1 PHE C 233 4727 4350 4473 2 -17 55 C ATOM 1783 CE2 PHE A 233 39.211 79.802 23.411 1.00 32.47 C ANISOU 1783 CE2 PHE C 233 3985 4049 4302 31 121 -44 C ATOM 1784 CZ PHE A 233 37.924 79.506 23.042 1.00 33.17 C ANISOU 1784 CZ PHE C 233 4082 4106 4412 12 145 -141 C ATOM 1785 N ALA A 234 43.150 78.297 17.764 1.00 35.49 N ANISOU 1785 N ALA C 234 4376 4598 4508 -6 -67 -99 N ATOM 1786 CA ALA A 234 43.922 78.606 16.558 1.00 37.82 C ANISOU 1786 CA ALA C 234 4746 4876 4747 15 -52 14 C ATOM 1787 C ALA A 234 43.403 77.813 15.364 1.00 40.69 C ANISOU 1787 C ALA C 234 5100 5326 5032 74 -25 -92 C ATOM 1788 O ALA A 234 42.934 76.672 15.514 1.00 42.12 O ANISOU 1788 O ALA C 234 5263 5513 5225 136 -157 -145 O ATOM 1789 CB ALA A 234 45.389 78.327 16.766 1.00 37.83 C ANISOU 1789 CB ALA C 234 4754 4931 4686 -6 -29 -21 C ATOM 1790 N GLY A 235 43.469 78.423 14.179 1.00 41.81 N ANISOU 1790 N GLY C 235 5280 5493 5112 103 -48 -27 N ATOM 1791 CA GLY A 235 43.152 77.706 12.949 1.00 42.16 C ANISOU 1791 CA GLY C 235 5350 5525 5143 36 -5 -28 C ATOM 1792 C GLY A 235 41.680 77.520 12.638 1.00 43.62 C ANISOU 1792 C GLY C 235 5512 5634 5426 57 -36 -13 C ATOM 1793 O GLY A 235 41.299 76.506 12.032 1.00 44.86 O ANISOU 1793 O GLY C 235 5657 5807 5581 130 77 -86 O ATOM 1794 N HIS A 236 40.852 78.481 13.051 1.00 43.85 N ANISOU 1794 N HIS C 236 5524 5707 5429 -3 -40 -4 N ATOM 1795 CA HIS A 236 39.463 78.584 12.566 1.00 45.05 C ANISOU 1795 CA HIS C 236 5734 5739 5642 25 -21 -12 C ATOM 1796 C HIS A 236 39.351 79.465 11.325 1.00 46.23 C ANISOU 1796 C HIS C 236 5957 5958 5648 53 -77 -23 C ATOM 1797 O HIS A 236 40.200 80.315 11.094 1.00 45.60 O ANISOU 1797 O HIS C 236 5997 5999 5328 119 -157 -34 O ATOM 1798 CB HIS A 236 38.564 79.162 13.643 1.00 43.90 C ANISOU 1798 CB HIS C 236 5625 5656 5399 68 -117 -43 C ATOM 1799 CG HIS A 236 38.301 78.202 14.737 1.00 42.74 C ANISOU 1799 CG HIS C 236 5394 5536 5306 77 -25 -65 C ATOM 1800 ND1 HIS A 236 37.433 77.147 14.586 1.00 40.83 N ANISOU 1800 ND1 HIS C 236 5273 5273 4968 54 17 -102 N ATOM 1801 CD2 HIS A 236 38.844 78.083 15.972 1.00 39.59 C ANISOU 1801 CD2 HIS C 236 4984 5213 4843 79 45 37 C ATOM 1802 CE1 HIS A 236 37.431 76.433 15.697 1.00 41.07 C ANISOU 1802 CE1 HIS C 236 5180 5288 5135 129 41 -65 C ATOM 1803 NE2 HIS A 236 38.279 76.977 16.550 1.00 37.84 N ANISOU 1803 NE2 HIS C 236 5062 5392 3924 -91 -74 61 N ATOM 1804 N GLU A 237 38.272 79.293 10.561 1.00 48.22 N ANISOU 1804 N GLU C 237 6165 6163 5992 23 -47 -58 N ATOM 1805 CA GLU A 237 38.056 80.117 9.372 1.00 48.37 C ANISOU 1805 CA GLU C 237 6179 6158 6039 11 -77 -56 C ATOM 1806 C GLU A 237 38.202 81.599 9.732 1.00 48.97 C ANISOU 1806 C GLU C 237 6216 6261 6128 7 -55 -45 C ATOM 1807 O GLU A 237 38.914 82.343 9.050 1.00 49.24 O ANISOU 1807 O GLU C 237 6163 6308 6238 23 -99 -85 O ATOM 1808 CB GLU A 237 36.683 79.830 8.736 1.00 49.43 C ANISOU 1808 CB GLU C 237 6281 6287 6211 41 -63 -21 C ATOM 1809 CG GLU A 237 36.432 80.531 7.389 1.00 50.36 C ANISOU 1809 CG GLU C 237 6401 6517 6216 -4 23 -170 C ATOM 1810 CD GLU A 237 37.613 80.421 6.412 1.00 56.54 C ANISOU 1810 CD GLU C 237 7316 7133 7031 19 7 107 C ATOM 1811 OE1 GLU A 237 38.286 79.352 6.366 1.00 58.27 O ANISOU 1811 OE1 GLU C 237 7526 7543 7070 -103 147 -7 O ATOM 1812 OE2 GLU A 237 37.863 81.412 5.685 1.00 59.92 O ANISOU 1812 OE2 GLU C 237 7536 7759 7472 100 -72 -69 O ATOM 1813 N GLU A 238 37.583 81.994 10.845 1.00 48.81 N ANISOU 1813 N GLU C 238 6200 6205 6140 -10 -44 -13 N ATOM 1814 CA GLU A 238 37.660 83.365 11.358 1.00 49.25 C ANISOU 1814 CA GLU C 238 6259 6281 6173 -12 -57 -9 C ATOM 1815 C GLU A 238 39.034 83.792 11.868 1.00 48.52 C ANISOU 1815 C GLU C 238 6190 6219 6025 9 -69 -13 C ATOM 1816 O GLU A 238 39.288 84.977 12.032 1.00 47.87 O ANISOU 1816 O GLU C 238 6208 6212 5769 -53 -11 -50 O ATOM 1817 CB GLU A 238 36.677 83.560 12.510 1.00 49.64 C ANISOU 1817 CB GLU C 238 6309 6321 6229 -32 -28 41 C ATOM 1818 CG GLU A 238 35.231 83.338 12.141 1.00 50.68 C ANISOU 1818 CG GLU C 238 6432 6409 6415 -22 -31 -59 C ATOM 1819 CD GLU A 238 34.763 81.903 12.307 1.00 50.84 C ANISOU 1819 CD GLU C 238 6380 6441 6494 -53 -87 14 C ATOM 1820 OE1 GLU A 238 35.597 80.976 12.381 1.00 49.57 O ANISOU 1820 OE1 GLU C 238 6312 6128 6392 47 -194 42 O ATOM 1821 OE2 GLU A 238 33.538 81.704 12.355 1.00 53.13 O ANISOU 1821 OE2 GLU C 238 6701 6625 6857 57 -178 -31 O ATOM 1822 N SER A 239 39.910 82.841 12.147 1.00 49.20 N ANISOU 1822 N SER C 239 6281 6223 6189 13 -65 32 N ATOM 1823 CA SER A 239 41.188 83.188 12.737 1.00 50.38 C ANISOU 1823 CA SER C 239 6394 6405 6342 0 -7 -33 C ATOM 1824 C SER A 239 42.045 83.933 11.722 1.00 51.04 C ANISOU 1824 C SER C 239 6455 6509 6429 -6 -27 -14 C ATOM 1825 O SER A 239 41.877 83.759 10.512 1.00 49.47 O ANISOU 1825 O SER C 239 6167 6353 6276 -10 -39 7 O ATOM 1826 CB SER A 239 41.932 81.947 13.219 1.00 49.79 C ANISOU 1826 CB SER C 239 6301 6349 6268 60 -27 -5 C ATOM 1827 OG SER A 239 41.152 81.234 14.154 1.00 46.65 O ANISOU 1827 OG SER C 239 5992 6010 5723 -26 171 -21 O ATOM 1828 N PRO A 240 42.942 84.798 12.215 1.00 52.45 N ANISOU 1828 N PRO C 240 6598 6667 6663 34 -13 -37 N ATOM 1829 CA PRO A 240 44.012 85.344 11.399 1.00 54.57 C ANISOU 1829 CA PRO C 240 6908 6883 6944 59 -73 -14 C ATOM 1830 C PRO A 240 44.707 84.290 10.531 1.00 56.42 C ANISOU 1830 C PRO C 240 7114 7155 7168 15 1 -7 C ATOM 1831 O PRO A 240 44.787 83.118 10.910 1.00 56.44 O ANISOU 1831 O PRO C 240 7151 7166 7125 54 -51 -15 O ATOM 1832 CB PRO A 240 44.973 85.915 12.442 1.00 53.93 C ANISOU 1832 CB PRO C 240 6844 6806 6841 -18 -4 15 C ATOM 1833 CG PRO A 240 44.068 86.339 13.568 1.00 52.61 C ANISOU 1833 CG PRO C 240 6658 6736 6593 8 -100 -22 C ATOM 1834 CD PRO A 240 42.945 85.354 13.582 1.00 51.96 C ANISOU 1834 CD PRO C 240 6618 6576 6549 2 -10 -16 C ATOM 1835 N GLY A 241 45.195 84.720 9.370 1.00 59.16 N ANISOU 1835 N GLY C 241 7491 7508 7477 22 -39 10 N ATOM 1836 CA GLY A 241 45.910 83.844 8.438 1.00 61.19 C ANISOU 1836 CA GLY C 241 7759 7740 7749 -33 -10 99 C ATOM 1837 C GLY A 241 45.050 83.489 7.247 1.00 63.14 C ANISOU 1837 C GLY C 241 8025 8034 7928 28 -24 -1 C ATOM 1838 O GLY A 241 43.958 84.033 7.075 1.00 63.06 O ANISOU 1838 O GLY C 241 7994 8098 7866 15 -19 -10 O ATOM 1839 N GLU A 242 45.537 82.563 6.432 1.00 65.62 N ANISOU 1839 N GLU C 242 8282 8381 8267 5 7 24 N ATOM 1840 CA GLU A 242 44.813 82.137 5.239 1.00 67.96 C ANISOU 1840 CA GLU C 242 8643 8658 8520 -8 37 -24 C ATOM 1841 C GLU A 242 44.536 80.638 5.253 1.00 69.53 C ANISOU 1841 C GLU C 242 8772 8867 8778 -3 30 -7 C ATOM 1842 O GLU A 242 45.314 79.842 5.802 1.00 69.65 O ANISOU 1842 O GLU C 242 8812 8884 8767 -35 59 -35 O ATOM 1843 CB GLU A 242 45.526 82.556 3.939 1.00 68.77 C ANISOU 1843 CB GLU C 242 8705 8737 8685 -2 -8 34 C ATOM 1844 CG GLU A 242 47.038 82.771 4.013 1.00 70.40 C ANISOU 1844 CG GLU C 242 8961 8847 8941 15 -34 41 C ATOM 1845 CD GLU A 242 47.586 83.417 2.738 1.00 70.37 C ANISOU 1845 CD GLU C 242 8964 8904 8867 -2 -16 55 C ATOM 1846 OE1 GLU A 242 47.111 83.059 1.634 1.00 72.48 O ANISOU 1846 OE1 GLU C 242 9267 9210 9062 35 0 -57 O ATOM 1847 OE2 GLU A 242 48.484 84.286 2.839 1.00 73.26 O ANISOU 1847 OE2 GLU C 242 9224 9244 9365 144 14 -28 O ATOM 1848 N THR A 243 43.398 80.279 4.663 1.00 70.63 N ANISOU 1848 N THR C 243 8950 8961 8925 11 15 -18 N ATOM 1849 CA THR A 243 42.990 78.894 4.521 1.00 71.14 C ANISOU 1849 CA THR C 243 8993 9028 9009 37 2 -24 C ATOM 1850 C THR A 243 43.700 78.288 3.312 1.00 72.21 C ANISOU 1850 C THR C 243 9141 9160 9135 5 11 -8 C ATOM 1851 O THR A 243 43.828 78.935 2.269 1.00 72.95 O ANISOU 1851 O THR C 243 9217 9266 9233 6 -9 -36 O ATOM 1852 CB THR A 243 41.467 78.791 4.332 1.00 71.33 C ANISOU 1852 CB THR C 243 9045 9038 9017 21 -25 -21 C ATOM 1853 OG1 THR A 243 40.798 79.443 5.426 1.00 70.98 O ANISOU 1853 OG1 THR C 243 8924 9034 9010 0 -11 -96 O ATOM 1854 CG2 THR A 243 41.028 77.334 4.246 1.00 70.79 C ANISOU 1854 CG2 THR C 243 8960 9007 8929 1 10 5 C ATOM 1855 N ILE A 244 44.153 77.047 3.461 1.00 72.67 N ANISOU 1855 N ILE C 244 9191 9218 9200 -5 -3 -15 N ATOM 1856 CA ILE A 244 44.941 76.351 2.441 1.00 72.74 C ANISOU 1856 CA ILE C 244 9208 9224 9206 -7 11 9 C ATOM 1857 C ILE A 244 44.172 75.135 1.929 1.00 72.86 C ANISOU 1857 C ILE C 244 9202 9269 9212 1 29 9 C ATOM 1858 O ILE A 244 43.724 74.297 2.713 1.00 72.92 O ANISOU 1858 O ILE C 244 9181 9322 9201 19 59 1 O ATOM 1859 CB ILE A 244 46.308 75.911 3.022 1.00 73.03 C ANISOU 1859 CB ILE C 244 9277 9248 9220 -9 7 1 C ATOM 1860 CG1 ILE A 244 47.195 77.145 3.276 1.00 73.51 C ANISOU 1860 CG1 ILE C 244 9314 9290 9325 8 -3 -4 C ATOM 1861 CG2 ILE A 244 47.008 74.908 2.096 1.00 72.75 C ANISOU 1861 CG2 ILE C 244 9213 9202 9226 -5 3 0 C ATOM 1862 CD1 ILE A 244 48.080 77.052 4.541 1.00 73.48 C ANISOU 1862 CD1 ILE C 244 9304 9288 9324 -7 -13 -10 C ATOM 1863 N ASN A 268 36.559 70.459 -2.886 1.00 67.28 N ANISOU 1863 N ASN C 268 8552 8488 8523 -32 25 -5 N ATOM 1864 CA ASN A 268 37.549 69.419 -2.595 1.00 66.81 C ANISOU 1864 CA ASN C 268 8496 8427 8458 -9 4 -18 C ATOM 1865 C ASN A 268 38.921 69.964 -2.132 1.00 66.95 C ANISOU 1865 C ASN C 268 8529 8443 8466 -16 13 -15 C ATOM 1866 O ASN A 268 39.028 70.480 -1.012 1.00 68.05 O ANISOU 1866 O ASN C 268 8682 8623 8550 -26 59 7 O ATOM 1867 CB ASN A 268 37.701 68.448 -3.787 1.00 66.99 C ANISOU 1867 CB ASN C 268 8499 8480 8472 1 16 -36 C ATOM 1868 CG ASN A 268 37.833 69.167 -5.128 1.00 67.44 C ANISOU 1868 CG ASN C 268 8589 8538 8494 -7 15 10 C ATOM 1869 OD1 ASN A 268 38.245 70.331 -5.199 1.00 67.19 O ANISOU 1869 OD1 ASN C 268 8619 8513 8397 33 -20 10 O ATOM 1870 ND2 ASN A 268 37.491 68.465 -6.200 1.00 67.62 N ANISOU 1870 ND2 ASN C 268 8719 8438 8535 -12 19 26 N ATOM 1871 N VAL A 269 39.931 69.907 -3.013 1.00 65.99 N ANISOU 1871 N VAL C 269 8375 8358 8337 -14 -24 -32 N ATOM 1872 CA VAL A 269 41.329 69.640 -2.620 1.00 64.91 C ANISOU 1872 CA VAL C 269 8190 8265 8205 3 -22 -3 C ATOM 1873 C VAL A 269 41.318 68.239 -1.958 1.00 64.75 C ANISOU 1873 C VAL C 269 8152 8257 8192 -18 11 -31 C ATOM 1874 O VAL A 269 40.824 67.273 -2.557 1.00 66.07 O ANISOU 1874 O VAL C 269 8185 8431 8484 30 29 -20 O ATOM 1875 CB VAL A 269 41.966 70.745 -1.698 1.00 65.18 C ANISOU 1875 CB VAL C 269 8214 8258 8293 23 -2 15 C ATOM 1876 CG1 VAL A 269 43.480 70.464 -1.470 1.00 65.31 C ANISOU 1876 CG1 VAL C 269 8303 8261 8250 0 5 5 C ATOM 1877 CG2 VAL A 269 41.758 72.134 -2.295 1.00 65.28 C ANISOU 1877 CG2 VAL C 269 8205 8347 8249 -20 -6 6 C ATOM 1878 N GLU A 270 41.844 68.129 -0.740 1.00 63.40 N ANISOU 1878 N GLU C 270 7987 8094 8007 -30 -34 -23 N ATOM 1879 CA GLU A 270 41.792 66.897 0.034 1.00 62.20 C ANISOU 1879 CA GLU C 270 7891 7907 7836 -17 55 4 C ATOM 1880 C GLU A 270 41.797 67.299 1.527 1.00 61.51 C ANISOU 1880 C GLU C 270 7814 7780 7776 -55 38 23 C ATOM 1881 O GLU A 270 42.615 66.807 2.324 1.00 63.16 O ANISOU 1881 O GLU C 270 8087 7951 7957 -60 -33 -23 O ATOM 1882 CB GLU A 270 42.993 65.982 -0.295 1.00 62.15 C ANISOU 1882 CB GLU C 270 7887 7898 7829 -31 52 12 C ATOM 1883 CG GLU A 270 43.687 66.239 -1.654 1.00 62.78 C ANISOU 1883 CG GLU C 270 7992 7957 7905 0 22 22 C ATOM 1884 CD GLU A 270 45.140 65.773 -1.691 1.00 63.69 C ANISOU 1884 CD GLU C 270 8087 7980 8131 4 55 18 C ATOM 1885 OE1 GLU A 270 45.683 65.378 -0.631 1.00 67.73 O ANISOU 1885 OE1 GLU C 270 8669 8653 8410 -3 -114 -79 O ATOM 1886 OE2 GLU A 270 45.748 65.822 -2.789 1.00 66.39 O ANISOU 1886 OE2 GLU C 270 8499 8446 8280 5 83 103 O ATOM 1887 N GLY A 271 40.901 68.210 1.903 1.00 59.67 N ANISOU 1887 N GLY C 271 7579 7556 7537 -2 36 23 N ATOM 1888 CA GLY A 271 40.824 68.667 3.297 1.00 58.65 C ANISOU 1888 CA GLY C 271 7401 7422 7460 31 22 8 C ATOM 1889 C GLY A 271 41.667 69.907 3.553 1.00 57.99 C ANISOU 1889 C GLY C 271 7342 7310 7379 30 56 44 C ATOM 1890 O GLY A 271 42.848 69.954 3.179 1.00 58.50 O ANISOU 1890 O GLY C 271 7430 7331 7463 46 106 66 O ATOM 1891 N LYS A 272 41.063 70.907 4.187 1.00 57.18 N ANISOU 1891 N LYS C 272 7242 7225 7259 14 25 32 N ATOM 1892 CA LYS A 272 41.678 72.222 4.313 1.00 57.16 C ANISOU 1892 CA LYS C 272 7253 7239 7224 -1 -9 24 C ATOM 1893 C LYS A 272 42.804 72.202 5.340 1.00 57.15 C ANISOU 1893 C LYS C 272 7269 7279 7166 12 -25 -15 C ATOM 1894 O LYS A 272 42.830 71.353 6.231 1.00 57.49 O ANISOU 1894 O LYS C 272 7311 7302 7229 17 -50 -17 O ATOM 1895 CB LYS A 272 40.631 73.267 4.705 1.00 56.48 C ANISOU 1895 CB LYS C 272 7152 7184 7121 -15 6 24 C ATOM 1896 CG LYS A 272 39.770 73.750 3.549 1.00 56.89 C ANISOU 1896 CG LYS C 272 7194 7275 7146 -46 1 2 C ATOM 1897 CD LYS A 272 38.638 74.639 4.038 1.00 57.15 C ANISOU 1897 CD LYS C 272 7321 7211 7180 -8 12 -1 C ATOM 1898 CE LYS A 272 37.689 73.876 4.948 1.00 57.61 C ANISOU 1898 CE LYS C 272 7352 7247 7288 54 4 -19 C ATOM 1899 NZ LYS A 272 36.551 74.723 5.400 1.00 58.03 N ANISOU 1899 NZ LYS C 272 7439 7300 7308 11 2 28 N ATOM 1900 N LYS A 273 43.728 73.150 5.219 1.00 57.41 N ANISOU 1900 N LYS C 273 7271 7340 7199 15 -29 -11 N ATOM 1901 CA LYS A 273 44.498 73.613 6.368 1.00 58.73 C ANISOU 1901 CA LYS C 273 7477 7433 7405 17 -5 10 C ATOM 1902 C LYS A 273 44.416 75.128 6.525 1.00 59.50 C ANISOU 1902 C LYS C 273 7537 7571 7498 12 -7 20 C ATOM 1903 O LYS A 273 44.200 75.852 5.554 1.00 59.20 O ANISOU 1903 O LYS C 273 7574 7569 7348 20 -15 11 O ATOM 1904 CB LYS A 273 45.959 73.173 6.248 1.00 58.72 C ANISOU 1904 CB LYS C 273 7480 7427 7402 -10 -9 38 C ATOM 1905 CG LYS A 273 46.214 71.744 6.698 1.00 58.82 C ANISOU 1905 CG LYS C 273 7501 7426 7423 -33 38 31 C ATOM 1906 CD LYS A 273 45.688 70.743 5.683 1.00 59.73 C ANISOU 1906 CD LYS C 273 7554 7599 7540 -29 22 44 C ATOM 1907 CE LYS A 273 46.481 69.447 5.723 1.00 60.23 C ANISOU 1907 CE LYS C 273 7522 7699 7660 -12 3 4 C ATOM 1908 NZ LYS A 273 45.664 68.282 5.285 1.00 62.22 N ANISOU 1908 NZ LYS C 273 7961 7728 7951 14 61 43 N ATOM 1909 N MET A 274 44.589 75.599 7.756 1.00 61.10 N ANISOU 1909 N MET C 274 7750 7767 7698 -1 38 24 N ATOM 1910 CA MET A 274 44.494 77.023 8.053 1.00 61.21 C ANISOU 1910 CA MET C 274 7749 7789 7718 6 51 12 C ATOM 1911 C MET A 274 45.875 77.668 8.106 1.00 63.12 C ANISOU 1911 C MET C 274 8056 7954 7971 13 38 14 C ATOM 1912 O MET A 274 46.249 78.431 7.215 1.00 64.75 O ANISOU 1912 O MET C 274 8342 8144 8115 9 25 40 O ATOM 1913 CB MET A 274 43.760 77.246 9.377 1.00 61.80 C ANISOU 1913 CB MET C 274 7884 7822 7772 10 61 -10 C ATOM 1914 CG MET A 274 42.818 78.439 9.372 1.00 62.39 C ANISOU 1914 CG MET C 274 7860 7920 7922 -25 91 -6 C ATOM 1915 SD MET A 274 43.539 79.893 8.587 1.00 67.39 S ANISOU 1915 SD MET C 274 8554 8720 8330 -79 -62 94 S ATOM 1916 CE MET A 274 42.113 80.974 8.500 1.00 63.76 C ANISOU 1916 CE MET C 274 8039 8156 8029 73 -28 31 C ATOM 1917 N PHE A 275 46.628 77.357 9.156 1.00 64.10 N ANISOU 1917 N PHE C 275 8144 8094 8115 -14 13 46 N ATOM 1918 CA PHE A 275 48.084 77.344 9.078 1.00 64.41 C ANISOU 1918 CA PHE C 275 8105 8202 8166 7 4 -4 C ATOM 1919 C PHE A 275 48.656 76.052 9.653 1.00 65.43 C ANISOU 1919 C PHE C 275 8225 8374 8260 18 -26 5 C ATOM 1920 O PHE A 275 49.840 75.757 9.484 1.00 66.08 O ANISOU 1920 O PHE C 275 8260 8501 8345 15 51 24 O ATOM 1921 CB PHE A 275 48.671 78.551 9.812 1.00 67.34 C ANISOU 1921 CB PHE C 275 8776 8377 8430 -234 313 -71 C ATOM 1922 CG PHE A 275 48.948 79.728 8.920 1.00 63.63 C ANISOU 1922 CG PHE C 275 7927 8083 8164 87 -136 4 C ATOM 1923 CD1 PHE A 275 47.966 80.220 8.076 1.00 65.08 C ANISOU 1923 CD1 PHE C 275 8259 8187 8278 -26 40 58 C ATOM 1924 CD2 PHE A 275 50.189 80.341 8.924 1.00 65.42 C ANISOU 1924 CD2 PHE C 275 8310 8223 8321 -76 -54 -109 C ATOM 1925 CE1 PHE A 275 48.217 81.302 7.254 1.00 64.95 C ANISOU 1925 CE1 PHE C 275 8050 8455 8170 76 -38 169 C ATOM 1926 CE2 PHE A 275 50.447 81.423 8.105 1.00 63.02 C ANISOU 1926 CE2 PHE C 275 7871 7956 8116 147 -125 34 C ATOM 1927 CZ PHE A 275 49.459 81.904 7.268 1.00 63.48 C ANISOU 1927 CZ PHE C 275 7934 8089 8093 103 -57 58 C ATOM 1928 N VAL A 276 47.809 75.286 10.332 1.00 20.00 N ATOM 1929 CA VAL A 276 48.050 73.861 10.525 1.00 20.00 C ATOM 1930 C VAL A 276 46.745 73.107 10.756 1.00 20.00 C ATOM 1931 O VAL A 276 46.306 72.941 11.894 1.00 20.00 O ATOM 1932 CB VAL A 276 48.997 73.605 11.712 1.00 20.00 C ATOM 1933 CG1 VAL A 276 50.225 72.831 11.256 1.00 20.00 C ATOM 1934 CG2 VAL A 276 49.399 74.917 12.367 1.00 20.00 C ATOM 1935 N GLU A 277 46.129 72.654 9.669 1.00 62.70 N ANISOU 1935 N GLU C 277 7986 7904 7930 30 10 6 N ATOM 1936 CA GLU A 277 44.786 72.090 9.728 1.00 60.43 C ANISOU 1936 CA GLU C 277 7709 7627 7624 -72 9 0 C ATOM 1937 C GLU A 277 43.730 73.187 9.808 1.00 59.30 C ANISOU 1937 C GLU C 277 7591 7483 7457 -28 15 -73 C ATOM 1938 O GLU A 277 44.057 74.371 9.895 1.00 60.55 O ANISOU 1938 O GLU C 277 7711 7684 7611 -14 47 -67 O ATOM 1939 CB GLU A 277 44.654 71.145 10.925 1.00 61.07 C ANISOU 1939 CB GLU C 277 7755 7759 7687 -58 -4 4 C ATOM 1940 CG GLU A 277 43.870 69.877 10.631 1.00 63.96 C ANISOU 1940 CG GLU C 277 8072 8066 8163 76 -16 6 C ATOM 1941 CD GLU A 277 44.732 68.785 10.028 1.00 70.25 C ANISOU 1941 CD GLU C 277 8913 8992 8783 -2 234 24 C ATOM 1942 OE1 GLU A 277 44.744 67.664 10.577 1.00 74.01 O ANISOU 1942 OE1 GLU C 277 9157 9504 9458 38 27 17 O ATOM 1943 OE2 GLU A 277 45.397 69.049 9.004 1.00 72.99 O ANISOU 1943 OE2 GLU C 277 9191 9394 9145 84 -132 -35 O ATOM 1944 N HIS A 278 42.463 72.786 9.778 1.00 56.39 N ANISOU 1944 N HIS C 278 7185 7127 7114 -24 29 -24 N ATOM 1945 CA HIS A 278 41.360 73.737 9.737 1.00 54.65 C ANISOU 1945 CA HIS C 278 6965 6980 6817 32 11 28 C ATOM 1946 C HIS A 278 40.173 73.242 10.557 1.00 53.24 C ANISOU 1946 C HIS C 278 6738 6862 6628 37 9 0 C ATOM 1947 O HIS A 278 39.661 72.146 10.327 1.00 53.78 O ANISOU 1947 O HIS C 278 6773 7015 6644 78 35 25 O ATOM 1948 CB HIS A 278 40.929 73.998 8.293 1.00 53.89 C ANISOU 1948 CB HIS C 278 6857 6870 6750 -3 22 17 C ATOM 1949 CG HIS A 278 40.017 75.175 8.137 1.00 54.17 C ANISOU 1949 CG HIS C 278 6922 6893 6764 32 -2 -7 C ATOM 1950 ND1 HIS A 278 38.672 75.119 8.435 1.00 52.80 N ANISOU 1950 ND1 HIS C 278 6676 6830 6553 38 -90 18 N ATOM 1951 CD2 HIS A 278 40.256 76.439 7.715 1.00 50.83 C ANISOU 1951 CD2 HIS C 278 6580 6429 6302 -5 149 -65 C ATOM 1952 CE1 HIS A 278 38.123 76.298 8.203 1.00 51.60 C ANISOU 1952 CE1 HIS C 278 6547 6558 6499 77 47 -9 C ATOM 1953 NE2 HIS A 278 39.062 77.117 7.765 1.00 50.13 N ANISOU 1953 NE2 HIS C 278 6281 6498 6268 35 179 49 N ATOM 1954 N LYS A 279 39.740 74.056 11.514 1.00 51.54 N ANISOU 1954 N LYS C 279 6512 6601 6468 25 -29 -8 N ATOM 1955 CA LYS A 279 38.888 73.585 12.588 1.00 50.04 C ANISOU 1955 CA LYS C 279 6325 6373 6313 5 -9 -62 C ATOM 1956 C LYS A 279 37.465 74.016 12.324 1.00 49.10 C ANISOU 1956 C LYS C 279 6185 6281 6187 27 -16 -50 C ATOM 1957 O LYS A 279 36.567 73.737 13.108 1.00 48.91 O ANISOU 1957 O LYS C 279 6122 6314 6147 79 -12 -31 O ATOM 1958 CB LYS A 279 39.354 74.157 13.925 1.00 49.57 C ANISOU 1958 CB LYS C 279 6330 6271 6232 7 -4 -48 C ATOM 1959 CG LYS A 279 40.623 73.547 14.471 1.00 48.26 C ANISOU 1959 CG LYS C 279 6150 6141 6044 2 -29 19 C ATOM 1960 CD LYS A 279 40.994 74.189 15.778 1.00 47.99 C ANISOU 1960 CD LYS C 279 6021 6099 6113 38 -53 26 C ATOM 1961 CE LYS A 279 42.095 73.436 16.462 1.00 45.90 C ANISOU 1961 CE LYS C 279 5839 5869 5732 127 -95 146 C ATOM 1962 NZ LYS A 279 43.379 74.128 16.364 1.00 42.18 N ANISOU 1962 NZ LYS C 279 5335 5455 5233 31 15 -175 N ATOM 1963 N GLY A 280 37.271 74.715 11.215 1.00 48.38 N ANISOU 1963 N GLY C 280 6131 6177 6073 36 20 -22 N ATOM 1964 CA GLY A 280 35.963 75.231 10.857 1.00 47.25 C ANISOU 1964 CA GLY C 280 5985 6050 5917 37 6 -9 C ATOM 1965 C GLY A 280 35.604 76.487 11.628 1.00 46.31 C ANISOU 1965 C GLY C 280 5940 5916 5738 43 -33 -28 C ATOM 1966 O GLY A 280 36.424 77.393 11.773 1.00 46.20 O ANISOU 1966 O GLY C 280 5935 5942 5675 100 -105 -3 O ATOM 1967 N SER A 281 34.372 76.539 12.125 1.00 45.18 N ANISOU 1967 N SER C 281 5778 5813 5575 66 -37 -57 N ATOM 1968 CA SER A 281 33.806 77.780 12.639 1.00 44.58 C ANISOU 1968 CA SER C 281 5725 5720 5493 49 -40 -69 C ATOM 1969 C SER A 281 34.029 77.910 14.142 1.00 43.97 C ANISOU 1969 C SER C 281 5591 5642 5473 64 -47 -85 C ATOM 1970 O SER A 281 33.750 76.985 14.904 1.00 43.93 O ANISOU 1970 O SER C 281 5685 5613 5391 146 -140 -142 O ATOM 1971 CB SER A 281 32.312 77.861 12.319 1.00 44.37 C ANISOU 1971 CB SER C 281 5793 5656 5410 74 -55 -77 C ATOM 1972 OG SER A 281 31.529 77.541 13.455 1.00 44.93 O ANISOU 1972 OG SER C 281 5990 5585 5494 124 -95 -172 O ATOM 1973 N LEU A 282 34.535 79.066 14.560 1.00 43.21 N ANISOU 1973 N LEU C 282 5446 5586 5385 39 -103 -59 N ATOM 1974 CA LEU A 282 34.701 79.363 15.966 1.00 42.25 C ANISOU 1974 CA LEU C 282 5347 5385 5319 37 -50 -24 C ATOM 1975 C LEU A 282 33.408 79.128 16.746 1.00 40.89 C ANISOU 1975 C LEU C 282 5145 5214 5175 68 -51 -91 C ATOM 1976 O LEU A 282 33.439 78.624 17.875 1.00 38.51 O ANISOU 1976 O LEU C 282 4663 5036 4933 213 -42 -251 O ATOM 1977 CB LEU A 282 35.152 80.814 16.107 1.00 42.58 C ANISOU 1977 CB LEU C 282 5379 5457 5340 42 -157 1 C ATOM 1978 CG LEU A 282 35.112 81.482 17.467 1.00 43.70 C ANISOU 1978 CG LEU C 282 5459 5645 5500 4 -5 -38 C ATOM 1979 CD1 LEU A 282 35.878 80.661 18.501 1.00 45.34 C ANISOU 1979 CD1 LEU C 282 5723 5830 5671 -21 -162 -68 C ATOM 1980 CD2 LEU A 282 35.698 82.880 17.346 1.00 43.17 C ANISOU 1980 CD2 LEU C 282 5457 5480 5465 30 -72 -11 C ATOM 1981 N GLU A 283 32.274 79.501 16.153 1.00 39.90 N ANISOU 1981 N GLU C 283 5083 5099 4978 20 -108 -143 N ATOM 1982 CA GLU A 283 30.994 79.327 16.825 1.00 39.64 C ANISOU 1982 CA GLU C 283 5018 5106 4937 15 -67 -83 C ATOM 1983 C GLU A 283 30.710 77.856 17.173 1.00 38.18 C ANISOU 1983 C GLU C 283 4938 4829 4739 13 -25 -94 C ATOM 1984 O GLU A 283 30.172 77.562 18.252 1.00 36.94 O ANISOU 1984 O GLU C 283 4837 4707 4489 108 -229 -209 O ATOM 1985 CB GLU A 283 29.839 79.898 15.997 1.00 40.62 C ANISOU 1985 CB GLU C 283 5169 5140 5121 19 -94 -41 C ATOM 1986 CG GLU A 283 28.472 79.668 16.647 1.00 40.07 C ANISOU 1986 CG GLU C 283 5173 5068 4984 -19 -111 -63 C ATOM 1987 CD GLU A 283 27.380 80.529 16.052 1.00 43.62 C ANISOU 1987 CD GLU C 283 5530 5503 5539 -128 -104 -53 C ATOM 1988 OE1 GLU A 283 26.608 79.997 15.204 1.00 49.35 O ANISOU 1988 OE1 GLU C 283 6156 6304 6289 121 -26 -355 O ATOM 1989 OE2 GLU A 283 27.300 81.733 16.425 1.00 47.67 O ANISOU 1989 OE2 GLU C 283 5672 6249 6191 -91 85 -162 O ATOM 1990 N ASP A 284 31.049 76.936 16.269 1.00 37.05 N ANISOU 1990 N ASP C 284 4786 4701 4589 -5 -91 -70 N ATOM 1991 CA ASP A 284 30.821 75.511 16.539 1.00 36.32 C ANISOU 1991 CA ASP C 284 4708 4574 4515 31 -78 -99 C ATOM 1992 C ASP A 284 31.744 75.012 17.647 1.00 34.69 C ANISOU 1992 C ASP C 284 4503 4341 4334 92 -79 -122 C ATOM 1993 O ASP A 284 31.324 74.234 18.491 1.00 34.08 O ANISOU 1993 O ASP C 284 4561 4261 4124 108 -114 -336 O ATOM 1994 CB ASP A 284 30.989 74.653 15.291 1.00 36.35 C ANISOU 1994 CB ASP C 284 4686 4618 4505 56 -29 -29 C ATOM 1995 CG ASP A 284 29.930 74.945 14.226 1.00 40.04 C ANISOU 1995 CG ASP C 284 5154 5071 4988 -41 -1 -107 C ATOM 1996 OD1 ASP A 284 28.847 75.519 14.549 1.00 38.63 O ANISOU 1996 OD1 ASP C 284 5155 4881 4643 -15 73 -253 O ATOM 1997 OD2 ASP A 284 30.205 74.593 13.047 1.00 43.20 O ANISOU 1997 OD2 ASP C 284 5555 5893 4963 -74 -16 -131 O ATOM 1998 N THR A 285 32.981 75.491 17.652 1.00 33.63 N ANISOU 1998 N THR C 285 4331 4256 4190 60 -100 -39 N ATOM 1999 CA THR A 285 33.930 75.155 18.701 1.00 32.47 C ANISOU 1999 CA THR C 285 4160 4135 4039 55 -75 10 C ATOM 2000 C THR A 285 33.445 75.586 20.085 1.00 30.65 C ANISOU 2000 C THR C 285 3882 3872 3890 87 -16 -98 C ATOM 2001 O THR A 285 33.560 74.813 21.040 1.00 30.91 O ANISOU 2001 O THR C 285 3874 3969 3902 178 -137 -165 O ATOM 2002 CB THR A 285 35.319 75.738 18.397 1.00 31.84 C ANISOU 2002 CB THR C 285 4049 4147 3902 63 -8 41 C ATOM 2003 OG1 THR A 285 35.870 75.039 17.269 1.00 30.95 O ANISOU 2003 OG1 THR C 285 3994 4543 3221 -62 -93 15 O ATOM 2004 CG2 THR A 285 36.271 75.593 19.589 1.00 32.99 C ANISOU 2004 CG2 THR C 285 4142 4240 4149 45 -119 -10 C ATOM 2005 N LEU A 286 32.892 76.793 20.190 1.00 29.86 N ANISOU 2005 N LEU C 286 3811 3787 3746 39 -134 -160 N ATOM 2006 CA LEU A 286 32.388 77.317 21.470 1.00 30.41 C ANISOU 2006 CA LEU C 286 3798 3876 3879 20 -119 -44 C ATOM 2007 C LEU A 286 31.141 76.572 21.977 1.00 29.35 C ANISOU 2007 C LEU C 286 3643 3717 3791 76 -65 -76 C ATOM 2008 O LEU A 286 30.977 76.370 23.195 1.00 28.94 O ANISOU 2008 O LEU C 286 3612 3386 3996 178 -283 6 O ATOM 2009 CB LEU A 286 32.083 78.828 21.379 1.00 30.99 C ANISOU 2009 CB LEU C 286 3851 3965 3959 58 -127 -51 C ATOM 2010 CG LEU A 286 33.258 79.802 21.355 1.00 29.35 C ANISOU 2010 CG LEU C 286 3524 3879 3746 53 24 -92 C ATOM 2011 CD1 LEU A 286 32.819 81.206 20.810 1.00 31.60 C ANISOU 2011 CD1 LEU C 286 3856 4102 4046 11 -72 -287 C ATOM 2012 CD2 LEU A 286 33.909 79.944 22.734 1.00 28.41 C ANISOU 2012 CD2 LEU C 286 3256 3781 3757 275 -298 -55 C ATOM 2013 N ILE A 287 30.267 76.188 21.050 1.00 30.63 N ANISOU 2013 N ILE C 287 3807 3844 3987 40 -202 -74 N ATOM 2014 CA ILE A 287 29.114 75.346 21.363 1.00 30.69 C ANISOU 2014 CA ILE C 287 3837 3863 3960 31 -95 -143 C ATOM 2015 C ILE A 287 29.530 73.973 21.912 1.00 29.25 C ANISOU 2015 C ILE C 287 3703 3649 3758 89 -80 -196 C ATOM 2016 O ILE A 287 28.994 73.523 22.914 1.00 25.91 O ANISOU 2016 O ILE C 287 3398 3006 3438 146 -237 -644 O ATOM 2017 CB ILE A 287 28.223 75.160 20.131 1.00 31.52 C ANISOU 2017 CB ILE C 287 3872 4006 4096 61 -37 -132 C ATOM 2018 CG1 ILE A 287 27.477 76.462 19.854 1.00 33.67 C ANISOU 2018 CG1 ILE C 287 4219 4306 4265 55 -117 -189 C ATOM 2019 CG2 ILE A 287 27.242 74.036 20.367 1.00 31.48 C ANISOU 2019 CG2 ILE C 287 4021 3892 4046 151 -20 -59 C ATOM 2020 CD1 ILE A 287 26.701 76.461 18.569 1.00 33.27 C ANISOU 2020 CD1 ILE C 287 4298 4165 4175 29 -178 -155 C ATOM 2021 N GLU A 288 30.480 73.337 21.239 1.00 29.93 N ANISOU 2021 N GLU C 288 3791 3734 3844 46 -45 -155 N ATOM 2022 CA GLU A 288 31.013 72.051 21.673 1.00 30.23 C ANISOU 2022 CA GLU C 288 3836 3848 3801 82 -53 -133 C ATOM 2023 C GLU A 288 31.721 72.184 23.029 1.00 28.64 C ANISOU 2023 C GLU C 288 3579 3700 3600 162 -64 -51 C ATOM 2024 O GLU A 288 31.518 71.365 23.935 1.00 27.80 O ANISOU 2024 O GLU C 288 3426 3544 3592 371 -109 -280 O ATOM 2025 CB GLU A 288 31.986 71.535 20.619 1.00 30.43 C ANISOU 2025 CB GLU C 288 3788 3985 3789 62 -62 -83 C ATOM 2026 CG GLU A 288 32.514 70.169 20.883 1.00 32.94 C ANISOU 2026 CG GLU C 288 4138 4167 4208 -97 -46 -102 C ATOM 2027 CD GLU A 288 33.491 69.725 19.818 1.00 36.67 C ANISOU 2027 CD GLU C 288 4825 4602 4506 -177 12 70 C ATOM 2028 OE1 GLU A 288 34.578 70.348 19.691 1.00 45.11 O ANISOU 2028 OE1 GLU C 288 5738 5493 5908 326 114 -146 O ATOM 2029 OE2 GLU A 288 33.164 68.751 19.092 1.00 48.30 O ANISOU 2029 OE2 GLU C 288 5647 6308 6396 192 325 -4 O ATOM 2030 N MET A 289 32.533 73.227 23.192 1.00 26.24 N ANISOU 2030 N MET C 289 3280 3388 3301 140 -123 -24 N ATOM 2031 CA MET A 289 33.099 73.513 24.514 1.00 27.37 C ANISOU 2031 CA MET C 289 3378 3499 3522 77 -78 -107 C ATOM 2032 C MET A 289 32.030 73.604 25.594 1.00 25.69 C ANISOU 2032 C MET C 289 3143 3217 3397 154 -88 -175 C ATOM 2033 O MET A 289 32.200 73.106 26.705 1.00 25.13 O ANISOU 2033 O MET C 289 3114 3062 3370 137 -150 -499 O ATOM 2034 CB MET A 289 33.898 74.805 24.515 1.00 26.32 C ANISOU 2034 CB MET C 289 3311 3428 3260 110 -109 -149 C ATOM 2035 CG MET A 289 35.320 74.633 24.069 1.00 30.00 C ANISOU 2035 CG MET C 289 3551 3871 3975 -42 -44 -70 C ATOM 2036 SD MET A 289 36.191 76.215 24.113 1.00 31.02 S ANISOU 2036 SD MET C 289 3776 3930 4081 344 -196 -189 S ATOM 2037 CE MET A 289 37.798 75.715 23.544 1.00 30.23 C ANISOU 2037 CE MET C 289 3690 3802 3993 188 78 -25 C ATOM 2038 N GLU A 290 30.910 74.237 25.281 1.00 26.14 N ANISOU 2038 N GLU C 290 3210 3301 3420 24 -154 -209 N ATOM 2039 CA GLU A 290 29.868 74.376 26.275 1.00 26.37 C ANISOU 2039 CA GLU C 290 3270 3343 3405 19 -110 -106 C ATOM 2040 C GLU A 290 29.201 73.038 26.563 1.00 25.41 C ANISOU 2040 C GLU C 290 3220 3091 3341 -101 -108 -123 C ATOM 2041 O GLU A 290 28.932 72.718 27.725 1.00 24.57 O ANISOU 2041 O GLU C 290 3046 2796 3493 213 -351 140 O ATOM 2042 CB GLU A 290 28.819 75.388 25.838 1.00 26.31 C ANISOU 2042 CB GLU C 290 3297 3382 3315 -8 -32 -178 C ATOM 2043 CG GLU A 290 27.733 75.589 26.876 1.00 27.01 C ANISOU 2043 CG GLU C 290 3415 3385 3462 -61 -247 -96 C ATOM 2044 CD GLU A 290 26.790 76.728 26.538 1.00 31.10 C ANISOU 2044 CD GLU C 290 3893 3806 4115 -186 -106 -40 C ATOM 2045 OE1 GLU A 290 26.888 77.279 25.399 1.00 33.95 O ANISOU 2045 OE1 GLU C 290 4281 4423 4194 -524 -413 -444 O ATOM 2046 OE2 GLU A 290 25.954 77.048 27.420 1.00 35.28 O ANISOU 2046 OE2 GLU C 290 4760 4042 4603 -306 50 55 O ATOM 2047 N GLN A 291 28.953 72.261 25.522 1.00 25.13 N ANISOU 2047 N GLN C 291 3092 3138 3318 -91 -126 -282 N ATOM 2048 CA GLN A 291 28.367 70.937 25.700 1.00 26.35 C ANISOU 2048 CA GLN C 291 3275 3317 3419 -19 -150 -132 C ATOM 2049 C GLN A 291 29.259 70.003 26.509 1.00 25.54 C ANISOU 2049 C GLN C 291 3296 3177 3227 -36 -128 -205 C ATOM 2050 O GLN A 291 28.777 69.281 27.400 1.00 25.85 O ANISOU 2050 O GLN C 291 3367 3187 3266 -1 -157 -272 O ATOM 2051 CB GLN A 291 28.091 70.291 24.355 1.00 25.47 C ANISOU 2051 CB GLN C 291 3204 3347 3123 -34 -186 -131 C ATOM 2052 CG GLN A 291 26.884 70.933 23.671 1.00 29.97 C ANISOU 2052 CG GLN C 291 3773 3701 3912 -13 -101 -183 C ATOM 2053 CD GLN A 291 26.786 70.583 22.213 1.00 30.39 C ANISOU 2053 CD GLN C 291 3805 3998 3743 64 -157 -166 C ATOM 2054 OE1 GLN A 291 27.720 70.017 21.615 1.00 38.66 O ANISOU 2054 OE1 GLN C 291 4830 4877 4980 -211 53 -112 O ATOM 2055 NE2 GLN A 291 25.653 70.937 21.608 1.00 35.04 N ANISOU 2055 NE2 GLN C 291 4450 4191 4672 119 -104 -321 N ATOM 2056 N ASP A 292 30.544 70.007 26.172 1.00 24.44 N ANISOU 2056 N ASP C 292 3052 3175 3056 -20 -144 -169 N ATOM 2057 CA ASP A 292 31.540 69.185 26.888 1.00 23.74 C ANISOU 2057 CA ASP C 292 2942 3013 3064 -2 -67 -185 C ATOM 2058 C ASP A 292 31.625 69.570 28.339 1.00 21.96 C ANISOU 2058 C ASP C 292 2699 2704 2937 25 3 -289 C ATOM 2059 O ASP A 292 31.660 68.714 29.233 1.00 22.68 O ANISOU 2059 O ASP C 292 2628 2858 3129 157 -19 -494 O ATOM 2060 CB ASP A 292 32.906 69.274 26.212 1.00 23.44 C ANISOU 2060 CB ASP C 292 2950 2984 2973 -8 -18 -194 C ATOM 2061 CG ASP A 292 32.909 68.637 24.856 1.00 27.46 C ANISOU 2061 CG ASP C 292 3527 3538 3364 -10 17 -127 C ATOM 2062 OD1 ASP A 292 31.930 67.910 24.561 1.00 30.68 O ANISOU 2062 OD1 ASP C 292 3847 3714 4093 156 -200 -356 O ATOM 2063 OD2 ASP A 292 33.881 68.833 24.104 1.00 28.28 O ANISOU 2063 OD2 ASP C 292 3959 3658 3125 -86 -295 -142 O ATOM 2064 N LEU A 293 31.606 70.863 28.595 1.00 22.51 N ANISOU 2064 N LEU C 293 2773 2786 2993 -130 -66 -285 N ATOM 2065 CA LEU A 293 31.589 71.356 29.970 1.00 22.23 C ANISOU 2065 CA LEU C 293 2809 2816 2819 -1 -66 -189 C ATOM 2066 C LEU A 293 30.307 71.017 30.779 1.00 22.56 C ANISOU 2066 C LEU C 293 2814 2913 2844 -55 -62 -198 C ATOM 2067 O LEU A 293 30.373 70.710 31.974 1.00 19.56 O ANISOU 2067 O LEU C 293 2548 2611 2271 -117 158 -85 O ATOM 2068 CB LEU A 293 31.864 72.853 29.949 1.00 22.09 C ANISOU 2068 CB LEU C 293 2698 3159 2537 -138 -142 -117 C ATOM 2069 CG LEU A 293 32.394 73.509 31.208 1.00 23.41 C ANISOU 2069 CG LEU C 293 2702 2984 3209 47 20 -265 C ATOM 2070 CD1 LEU A 293 33.533 72.754 31.929 1.00 25.31 C ANISOU 2070 CD1 LEU C 293 2954 3280 3380 51 43 -77 C ATOM 2071 CD2 LEU A 293 32.832 74.950 30.788 1.00 24.32 C ANISOU 2071 CD2 LEU C 293 3000 2940 3300 191 -230 -153 C ATOM 2072 N GLN A 294 29.151 71.017 30.122 1.00 22.89 N ANISOU 2072 N GLN C 294 2763 2805 3127 -29 -114 -188 N ATOM 2073 CA GLN A 294 27.905 70.506 30.727 1.00 21.46 C ANISOU 2073 CA GLN C 294 2668 2735 2747 -24 -53 -83 C ATOM 2074 C GLN A 294 28.023 69.023 31.091 1.00 21.30 C ANISOU 2074 C GLN C 294 2713 2692 2687 82 -54 -46 C ATOM 2075 O GLN A 294 27.545 68.613 32.143 1.00 20.11 O ANISOU 2075 O GLN C 294 2650 2546 2442 144 -204 -221 O ATOM 2076 CB GLN A 294 26.704 70.710 29.770 1.00 20.14 C ANISOU 2076 CB GLN C 294 2501 2606 2544 123 159 -199 C ATOM 2077 CG GLN A 294 26.319 72.168 29.603 1.00 21.59 C ANISOU 2077 CG GLN C 294 2809 2681 2711 -123 15 -247 C ATOM 2078 CD GLN A 294 25.205 72.388 28.627 1.00 22.83 C ANISOU 2078 CD GLN C 294 2932 2802 2939 -84 19 -111 C ATOM 2079 OE1 GLN A 294 25.203 71.814 27.526 1.00 27.13 O ANISOU 2079 OE1 GLN C 294 3755 3520 3030 -1 -109 -477 O ATOM 2080 NE2 GLN A 294 24.240 73.230 29.016 1.00 26.75 N ANISOU 2080 NE2 GLN C 294 2882 3256 4022 -286 -97 -444 N ATOM 2081 N SER A 295 28.645 68.232 30.216 1.00 21.07 N ANISOU 2081 N SER C 295 2549 2594 2862 109 85 -197 N ATOM 2082 CA SER A 295 28.933 66.832 30.537 1.00 21.76 C ANISOU 2082 CA SER C 295 2624 2703 2940 71 -21 -29 C ATOM 2083 C SER A 295 29.805 66.678 31.762 1.00 21.26 C ANISOU 2083 C SER C 295 2523 2552 3001 94 -24 -24 C ATOM 2084 O SER A 295 29.531 65.835 32.620 1.00 21.41 O ANISOU 2084 O SER C 295 2381 2386 3367 258 -231 -68 O ATOM 2085 CB SER A 295 29.600 66.120 29.371 1.00 22.72 C ANISOU 2085 CB SER C 295 2856 2869 2907 154 4 7 C ATOM 2086 OG SER A 295 28.754 66.078 28.258 1.00 26.61 O ANISOU 2086 OG SER C 295 3533 2880 3697 54 -200 -323 O ATOM 2087 N SER A 296 30.837 67.514 31.867 1.00 22.01 N ANISOU 2087 N SER C 296 2672 2530 3160 64 -142 88 N ATOM 2088 CA SER A 296 31.698 67.576 33.048 1.00 19.48 C ANISOU 2088 CA SER C 296 2401 2377 2623 57 -42 107 C ATOM 2089 C SER A 296 30.910 67.848 34.298 1.00 18.67 C ANISOU 2089 C SER C 296 2304 2316 2472 58 -60 -5 C ATOM 2090 O SER A 296 31.079 67.148 35.244 1.00 16.31 O ANISOU 2090 O SER C 296 2256 2073 1868 -17 -153 78 O ATOM 2091 CB SER A 296 32.798 68.676 32.919 1.00 19.07 C ANISOU 2091 CB SER C 296 2290 2319 2637 23 -60 15 C ATOM 2092 OG SER A 296 33.750 68.351 31.948 1.00 18.35 O ANISOU 2092 OG SER C 296 2146 2280 2543 151 -85 28 O ATOM 2093 N ILE A 297 30.014 68.833 34.272 1.00 19.29 N ANISOU 2093 N ILE C 297 2256 2477 2594 73 13 48 N ATOM 2094 CA ILE A 297 29.146 69.137 35.434 1.00 19.28 C ANISOU 2094 CA ILE C 297 2348 2395 2581 -17 15 46 C ATOM 2095 C ILE A 297 28.238 67.942 35.749 1.00 17.71 C ANISOU 2095 C ILE C 297 2197 2101 2428 -82 26 68 C ATOM 2096 O ILE A 297 28.029 67.620 36.912 1.00 18.70 O ANISOU 2096 O ILE C 297 2195 2026 2882 -193 -137 -62 O ATOM 2097 CB ILE A 297 28.300 70.463 35.216 1.00 18.94 C ANISOU 2097 CB ILE C 297 2272 2612 2312 23 -79 36 C ATOM 2098 CG1 ILE A 297 29.252 71.658 35.046 1.00 20.54 C ANISOU 2098 CG1 ILE C 297 2517 2624 2660 -14 -79 -99 C ATOM 2099 CG2 ILE A 297 27.321 70.712 36.393 1.00 19.56 C ANISOU 2099 CG2 ILE C 297 2218 2360 2853 44 -6 1 C ATOM 2100 CD1 ILE A 297 28.600 72.905 34.528 1.00 21.96 C ANISOU 2100 CD1 ILE C 297 2520 2648 3175 -101 99 -73 C ATOM 2101 N SER A 298 27.724 67.272 34.719 1.00 17.83 N ANISOU 2101 N SER C 298 2286 2060 2427 -17 -9 46 N ATOM 2102 CA ASER A 298 26.910 66.071 34.930 0.50 19.28 C ANISOU 2102 CA ASER C 298 2413 2373 2537 22 -1 61 C ATOM 2103 C SER A 298 27.692 65.019 35.716 1.00 19.05 C ANISOU 2103 C SER C 298 2390 2306 2542 33 2 17 C ATOM 2104 O SER A 298 27.225 64.505 36.732 1.00 18.79 O ANISOU 2104 O SER C 298 2776 1954 2408 109 129 123 O ATOM 2105 CB ASER A 298 26.443 65.498 33.593 0.50 19.63 C ANISOU 2105 CB ASER C 298 2560 2274 2622 129 -55 -97 C ATOM 2106 OG ASER A 298 25.706 66.484 32.895 0.50 24.37 O ANISOU 2106 OG ASER C 298 2891 3020 3349 -95 -163 -81 O ATOM 2107 N TYR A 299 28.872 64.685 35.217 1.00 20.12 N ANISOU 2107 N TYR C 299 2411 2294 2938 82 -129 44 N ATOM 2108 CA TYR A 299 29.760 63.741 35.902 1.00 19.78 C ANISOU 2108 CA TYR C 299 2409 2453 2652 -21 -25 42 C ATOM 2109 C TYR A 299 30.176 64.178 37.285 1.00 19.03 C ANISOU 2109 C TYR C 299 2492 2226 2512 -159 -103 272 C ATOM 2110 O TYR A 299 30.417 63.327 38.097 1.00 19.33 O ANISOU 2110 O TYR C 299 2363 2576 2404 -35 -268 476 O ATOM 2111 CB TYR A 299 31.033 63.478 35.072 1.00 21.88 C ANISOU 2111 CB TYR C 299 2750 2646 2917 49 2 127 C ATOM 2112 CG TYR A 299 30.843 62.489 33.940 1.00 19.99 C ANISOU 2112 CG TYR C 299 2540 2270 2784 190 -14 104 C ATOM 2113 CD1 TYR A 299 30.566 61.152 34.218 1.00 22.41 C ANISOU 2113 CD1 TYR C 299 2538 2628 3345 49 29 -159 C ATOM 2114 CD2 TYR A 299 30.967 62.860 32.628 1.00 24.48 C ANISOU 2114 CD2 TYR C 299 2855 3333 3111 146 22 -68 C ATOM 2115 CE1 TYR A 299 30.374 60.247 33.224 1.00 20.69 C ANISOU 2115 CE1 TYR C 299 2678 2808 2374 -215 -80 213 C ATOM 2116 CE2 TYR A 299 30.780 61.924 31.586 1.00 24.02 C ANISOU 2116 CE2 TYR C 299 2921 3342 2862 -52 154 352 C ATOM 2117 CZ TYR A 299 30.481 60.616 31.908 1.00 21.40 C ANISOU 2117 CZ TYR C 299 2729 2679 2722 -41 4 166 C ATOM 2118 OH TYR A 299 30.290 59.604 30.972 1.00 25.97 O ANISOU 2118 OH TYR C 299 3323 3660 2883 181 141 279 O ATOM 2119 N ALA A 300 30.299 65.489 37.528 1.00 18.42 N ANISOU 2119 N ALA C 300 2341 2325 2332 79 156 179 N ATOM 2120 CA ALA A 300 30.657 66.016 38.866 1.00 20.74 C ANISOU 2120 CA ALA C 300 2592 2634 2652 36 -51 32 C ATOM 2121 C ALA A 300 29.531 65.906 39.889 1.00 21.11 C ANISOU 2121 C ALA C 300 2598 2650 2771 43 -2 56 C ATOM 2122 O ALA A 300 29.736 66.241 41.038 1.00 21.08 O ANISOU 2122 O ALA C 300 2633 2623 2753 302 -129 -9 O ATOM 2123 CB ALA A 300 31.120 67.466 38.782 1.00 20.31 C ANISOU 2123 CB ALA C 300 2596 2533 2586 -23 95 54 C ATOM 2124 N GLY A 301 28.346 65.456 39.476 1.00 22.32 N ANISOU 2124 N GLY C 301 2664 2722 3094 79 -6 19 N ATOM 2125 CA GLY A 301 27.226 65.297 40.424 1.00 22.12 C ANISOU 2125 CA GLY C 301 2819 2743 2840 41 -10 -10 C ATOM 2126 C GLY A 301 26.545 66.602 40.802 1.00 22.69 C ANISOU 2126 C GLY C 301 3003 2732 2886 34 40 -33 C ATOM 2127 O GLY A 301 25.931 66.710 41.867 1.00 24.55 O ANISOU 2127 O GLY C 301 3233 2944 3151 0 149 -86 O ATOM 2128 N GLY A 302 26.638 67.595 39.920 1.00 22.86 N ANISOU 2128 N GLY C 302 2907 2732 3043 -38 63 1 N ATOM 2129 CA GLY A 302 26.045 68.905 40.156 1.00 23.55 C ANISOU 2129 CA GLY C 302 2984 2975 2987 -1 43 11 C ATOM 2130 C GLY A 302 25.219 69.417 39.011 1.00 23.53 C ANISOU 2130 C GLY C 302 2860 2942 3137 -86 109 -71 C ATOM 2131 O GLY A 302 24.939 68.708 38.062 1.00 19.49 O ANISOU 2131 O GLY C 302 2594 2695 2116 -396 203 8 O ATOM 2132 N THR A 303 24.804 70.671 39.128 1.00 25.25 N ANISOU 2132 N THR C 303 2961 3057 3575 6 149 51 N ATOM 2133 CA THR A 303 24.107 71.342 38.048 1.00 25.08 C ANISOU 2133 CA THR C 303 3119 3097 3311 1 66 56 C ATOM 2134 C THR A 303 24.779 72.646 37.620 1.00 26.20 C ANISOU 2134 C THR C 303 3199 3324 3430 -76 109 -45 C ATOM 2135 O THR A 303 24.309 73.301 36.683 1.00 27.18 O ANISOU 2135 O THR C 303 3138 3585 3604 -227 -88 -358 O ATOM 2136 CB THR A 303 22.669 71.686 38.501 1.00 26.59 C ANISOU 2136 CB THR C 303 3365 3216 3522 95 90 67 C ATOM 2137 OG1 THR A 303 22.737 72.685 39.526 1.00 24.22 O ANISOU 2137 OG1 THR C 303 3226 2527 3448 -329 240 751 O ATOM 2138 CG2 THR A 303 21.986 70.428 39.087 1.00 28.08 C ANISOU 2138 CG2 THR C 303 3325 3385 3959 -30 -2 94 C ATOM 2139 N LYS A 304 25.857 73.050 38.305 1.00 26.89 N ANISOU 2139 N LYS C 304 3185 3263 3766 -23 40 20 N ATOM 2140 CA LYS A 304 26.541 74.281 37.931 1.00 26.26 C ANISOU 2140 CA LYS C 304 3218 3152 3606 39 -19 83 C ATOM 2141 C LYS A 304 28.060 74.123 38.026 1.00 25.29 C ANISOU 2141 C LYS C 304 3019 3090 3499 84 -80 -25 C ATOM 2142 O LYS A 304 28.561 73.126 38.534 1.00 22.89 O ANISOU 2142 O LYS C 304 2612 2713 3371 74 -52 -81 O ATOM 2143 CB LYS A 304 26.028 75.450 38.770 1.00 27.80 C ANISOU 2143 CB LYS C 304 3242 3426 3891 60 -123 -17 C ATOM 2144 CG LYS A 304 26.232 75.314 40.240 1.00 30.47 C ANISOU 2144 CG LYS C 304 3833 3964 3777 33 161 241 C ATOM 2145 CD LYS A 304 25.290 76.272 41.017 1.00 30.87 C ANISOU 2145 CD LYS C 304 3841 3856 4030 -75 149 204 C ATOM 2146 CE LYS A 304 25.784 76.517 42.430 1.00 37.15 C ANISOU 2146 CE LYS C 304 4815 4838 4462 77 52 -95 C ATOM 2147 NZ LYS A 304 25.442 75.445 43.423 1.00 43.32 N ANISOU 2147 NZ LYS C 304 5106 5835 5516 44 -260 136 N ATOM 2148 N LEU A 305 28.769 75.113 37.490 1.00 24.64 N ANISOU 2148 N LEU C 305 3010 3000 3352 64 -11 149 N ATOM 2149 CA LEU A 305 30.208 75.039 37.308 1.00 23.68 C ANISOU 2149 CA LEU C 305 2892 2932 3172 82 -23 72 C ATOM 2150 C LEU A 305 30.975 74.732 38.582 1.00 21.72 C ANISOU 2150 C LEU C 305 2685 2703 2864 117 -67 261 C ATOM 2151 O LEU A 305 31.909 73.908 38.597 1.00 21.30 O ANISOU 2151 O LEU C 305 2578 2788 2725 20 82 336 O ATOM 2152 CB LEU A 305 30.682 76.367 36.695 1.00 24.22 C ANISOU 2152 CB LEU C 305 2920 2963 3318 35 -83 1 C ATOM 2153 CG LEU A 305 32.060 76.351 36.074 1.00 23.60 C ANISOU 2153 CG LEU C 305 2969 2994 3001 91 -75 58 C ATOM 2154 CD1 LEU A 305 32.107 75.463 34.841 1.00 22.75 C ANISOU 2154 CD1 LEU C 305 2807 2781 3055 34 -122 190 C ATOM 2155 CD2 LEU A 305 32.458 77.804 35.792 1.00 26.16 C ANISOU 2155 CD2 LEU C 305 3239 3146 3553 105 -109 239 C ATOM 2156 N ASP A 306 30.567 75.357 39.675 1.00 21.46 N ANISOU 2156 N ASP C 306 2599 2530 3023 -8 44 108 N ATOM 2157 CA ASP A 306 31.258 75.161 40.941 1.00 22.54 C ANISOU 2157 CA ASP C 306 2827 2819 2919 15 31 91 C ATOM 2158 C ASP A 306 31.228 73.736 41.462 1.00 21.43 C ANISOU 2158 C ASP C 306 2724 2657 2760 -64 168 104 C ATOM 2159 O ASP A 306 32.051 73.363 42.320 1.00 21.92 O ANISOU 2159 O ASP C 306 2823 2559 2944 -97 173 41 O ATOM 2160 CB ASP A 306 30.750 76.152 41.992 1.00 23.19 C ANISOU 2160 CB ASP C 306 2963 2922 2927 -41 -36 101 C ATOM 2161 CG ASP A 306 31.194 77.601 41.685 1.00 30.56 C ANISOU 2161 CG ASP C 306 3481 4018 4111 99 5 104 C ATOM 2162 OD1 ASP A 306 32.114 77.803 40.845 1.00 31.89 O ANISOU 2162 OD1 ASP C 306 3789 3712 4612 158 -89 153 O ATOM 2163 OD2 ASP A 306 30.601 78.532 42.256 1.00 33.14 O ANISOU 2163 OD2 ASP C 306 4359 3804 4428 -176 256 157 O ATOM 2164 N SER A 307 30.304 72.919 40.963 1.00 20.91 N ANISOU 2164 N SER C 307 2806 2361 2775 -136 44 92 N ATOM 2165 CA SER A 307 30.294 71.509 41.356 1.00 20.34 C ANISOU 2165 CA SER C 307 2672 2513 2543 -21 -18 121 C ATOM 2166 C SER A 307 31.613 70.800 40.997 1.00 19.12 C ANISOU 2166 C SER C 307 2543 2385 2338 -34 -20 77 C ATOM 2167 O SER A 307 31.999 69.855 41.651 1.00 18.72 O ANISOU 2167 O SER C 307 2896 2387 1830 23 172 31 O ATOM 2168 CB SER A 307 29.105 70.769 40.746 1.00 19.31 C ANISOU 2168 CB SER C 307 2633 2578 2127 92 -132 54 C ATOM 2169 OG SER A 307 29.196 70.673 39.328 1.00 22.80 O ANISOU 2169 OG SER C 307 2881 3406 2373 -119 300 65 O ATOM 2170 N ILE A 308 32.262 71.230 39.920 1.00 19.73 N ANISOU 2170 N ILE C 308 2689 2422 2386 -100 -46 184 N ATOM 2171 CA ILE A 308 33.551 70.641 39.490 1.00 20.10 C ANISOU 2171 CA ILE C 308 2626 2461 2548 -86 -2 141 C ATOM 2172 C ILE A 308 34.630 70.828 40.584 1.00 20.56 C ANISOU 2172 C ILE C 308 2547 2481 2781 -43 23 167 C ATOM 2173 O ILE A 308 35.504 69.977 40.756 1.00 19.88 O ANISOU 2173 O ILE C 308 2343 2487 2721 -95 69 312 O ATOM 2174 CB ILE A 308 33.971 71.198 38.042 1.00 18.98 C ANISOU 2174 CB ILE C 308 2466 2258 2487 -106 131 170 C ATOM 2175 CG1 ILE A 308 32.905 70.843 37.017 1.00 19.78 C ANISOU 2175 CG1 ILE C 308 2656 2221 2637 -215 -16 193 C ATOM 2176 CG2 ILE A 308 35.326 70.635 37.552 1.00 19.59 C ANISOU 2176 CG2 ILE C 308 2742 2432 2268 -79 -152 135 C ATOM 2177 CD1 ILE A 308 33.041 71.513 35.692 1.00 21.32 C ANISOU 2177 CD1 ILE C 308 2987 2543 2568 18 64 202 C ATOM 2178 N ARG A 309 34.538 71.913 41.359 1.00 20.08 N ANISOU 2178 N ARG C 309 2616 2470 2540 -210 134 194 N ATOM 2179 CA ARG A 309 35.511 72.255 42.392 1.00 21.14 C ANISOU 2179 CA ARG C 309 2693 2581 2757 -58 62 103 C ATOM 2180 C ARG A 309 35.622 71.277 43.584 1.00 20.29 C ANISOU 2180 C ARG C 309 2665 2538 2505 -148 149 137 C ATOM 2181 O ARG A 309 36.596 71.310 44.295 1.00 22.81 O ANISOU 2181 O ARG C 309 2917 2975 2772 -244 66 101 O ATOM 2182 CB ARG A 309 35.247 73.685 42.923 1.00 20.89 C ANISOU 2182 CB ARG C 309 2776 2476 2683 42 97 69 C ATOM 2183 CG ARG A 309 35.304 74.762 41.813 1.00 22.14 C ANISOU 2183 CG ARG C 309 2636 2893 2883 -22 26 83 C ATOM 2184 CD ARG A 309 35.257 76.207 42.365 1.00 22.92 C ANISOU 2184 CD ARG C 309 2785 3042 2878 68 16 296 C ATOM 2185 NE ARG A 309 35.049 77.152 41.265 1.00 27.52 N ANISOU 2185 NE ARG C 309 3169 3583 3704 -242 -103 193 N ATOM 2186 CZ ARG A 309 36.005 77.532 40.405 1.00 27.45 C ANISOU 2186 CZ ARG C 309 3646 3665 3116 -16 -158 79 C ATOM 2187 NH1 ARG A 309 37.259 77.058 40.501 1.00 21.42 N ANISOU 2187 NH1 ARG C 309 2932 3501 1705 17 -144 246 N ATOM 2188 NH2 ARG A 309 35.695 78.390 39.426 1.00 28.57 N ANISOU 2188 NH2 ARG C 309 3485 3615 3753 -258 -213 124 N ATOM 2189 N THR A 310 34.651 70.420 43.810 1.00 21.65 N ANISOU 2189 N THR C 310 2578 3018 2628 -172 90 117 N ATOM 2190 CA THR A 310 34.724 69.517 44.968 1.00 23.16 C ANISOU 2190 CA THR C 310 2833 3118 2846 -24 25 156 C ATOM 2191 C THR A 310 34.729 68.039 44.633 1.00 23.29 C ANISOU 2191 C THR C 310 2741 3202 2903 -31 -28 240 C ATOM 2192 O THR A 310 34.505 67.208 45.541 1.00 25.41 O ANISOU 2192 O THR C 310 2998 3658 2998 -149 -52 368 O ATOM 2193 CB THR A 310 33.597 69.761 46.000 1.00 24.23 C ANISOU 2193 CB THR C 310 2989 3145 3070 -5 -48 232 C ATOM 2194 OG1 THR A 310 32.342 69.749 45.349 1.00 22.63 O ANISOU 2194 OG1 THR C 310 3552 3176 1869 -4 -835 188 O ATOM 2195 CG2 THR A 310 33.798 71.091 46.753 1.00 28.21 C ANISOU 2195 CG2 THR C 310 3490 4050 3178 41 134 121 C ATOM 2196 N VAL A 311 34.994 67.698 43.377 1.00 21.33 N ANISOU 2196 N VAL C 311 2622 2854 2627 -63 -100 81 N ATOM 2197 CA VAL A 311 35.188 66.305 43.030 1.00 20.68 C ANISOU 2197 CA VAL C 311 2623 2675 2560 52 -1 144 C ATOM 2198 C VAL A 311 36.547 65.773 43.500 1.00 20.52 C ANISOU 2198 C VAL C 311 2647 2717 2430 58 67 95 C ATOM 2199 O VAL A 311 37.549 66.520 43.637 1.00 19.01 O ANISOU 2199 O VAL C 311 2373 2772 2074 105 407 338 O ATOM 2200 CB VAL A 311 35.045 66.019 41.536 1.00 19.14 C ANISOU 2200 CB VAL C 311 2444 2493 2334 33 -185 48 C ATOM 2201 CG1 VAL A 311 33.620 66.311 41.066 1.00 21.01 C ANISOU 2201 CG1 VAL C 311 2896 2494 2592 -75 -104 313 C ATOM 2202 CG2 VAL A 311 36.106 66.774 40.685 1.00 17.88 C ANISOU 2202 CG2 VAL C 311 2068 2403 2323 -46 129 80 C ATOM 2203 N ASP A 312 36.605 64.465 43.702 1.00 21.24 N ANISOU 2203 N ASP C 312 2736 2813 2519 66 21 33 N ATOM 2204 CA ASP A 312 37.884 63.823 43.989 1.00 20.42 C ANISOU 2204 CA ASP C 312 2610 2553 2595 20 -1 52 C ATOM 2205 C ASP A 312 38.612 63.604 42.686 1.00 18.76 C ANISOU 2205 C ASP C 312 2317 2315 2494 49 62 12 C ATOM 2206 O ASP A 312 38.033 63.779 41.620 1.00 18.66 O ANISOU 2206 O ASP C 312 2279 2314 2495 95 -312 238 O ATOM 2207 CB ASP A 312 37.702 62.510 44.733 1.00 22.58 C ANISOU 2207 CB ASP C 312 2875 2612 3092 -29 -57 42 C ATOM 2208 CG ASP A 312 38.968 62.101 45.522 1.00 24.13 C ANISOU 2208 CG ASP C 312 3222 3236 2707 -43 27 -223 C ATOM 2209 OD1 ASP A 312 39.956 62.907 45.628 1.00 28.87 O ANISOU 2209 OD1 ASP C 312 3792 3543 3631 68 -178 392 O ATOM 2210 OD2 ASP A 312 38.970 60.958 46.026 1.00 31.50 O ANISOU 2210 OD2 ASP C 312 3748 4324 3893 225 -161 -4 O ATOM 2211 N TYR A 313 39.888 63.220 42.764 1.00 20.04 N ANISOU 2211 N TYR C 313 2588 2541 2485 134 -12 -21 N ATOM 2212 CA TYR A 313 40.680 62.993 41.563 1.00 19.48 C ANISOU 2212 CA TYR C 313 2437 2393 2570 -51 105 9 C ATOM 2213 C TYR A 313 41.748 61.945 41.844 1.00 19.45 C ANISOU 2213 C TYR C 313 2475 2401 2514 -34 66 -59 C ATOM 2214 O TYR A 313 41.979 61.573 42.976 1.00 19.29 O ANISOU 2214 O TYR C 313 2608 2342 2378 -212 118 -92 O ATOM 2215 CB TYR A 313 41.331 64.289 41.078 1.00 19.44 C ANISOU 2215 CB TYR C 313 2585 2322 2478 -168 69 20 C ATOM 2216 CG TYR A 313 42.371 64.818 42.032 1.00 20.27 C ANISOU 2216 CG TYR C 313 2565 2446 2690 138 -35 166 C ATOM 2217 CD1 TYR A 313 43.708 64.450 41.893 1.00 19.94 C ANISOU 2217 CD1 TYR C 313 2756 2311 2508 -161 -291 -474 C ATOM 2218 CD2 TYR A 313 42.036 65.680 43.044 1.00 20.84 C ANISOU 2218 CD2 TYR C 313 2795 2685 2436 239 -98 146 C ATOM 2219 CE1 TYR A 313 44.648 64.921 42.736 1.00 22.21 C ANISOU 2219 CE1 TYR C 313 2620 2757 3060 162 241 -464 C ATOM 2220 CE2 TYR A 313 43.000 66.159 43.926 1.00 21.50 C ANISOU 2220 CE2 TYR C 313 2889 2512 2768 100 52 -72 C ATOM 2221 CZ TYR A 313 44.289 65.759 43.767 1.00 23.56 C ANISOU 2221 CZ TYR C 313 3353 2601 2996 8 218 -90 C ATOM 2222 OH TYR A 313 45.274 66.222 44.607 1.00 24.04 O ANISOU 2222 OH TYR C 313 3621 3492 2019 119 -22 -606 O ATOM 2223 N VAL A 314 42.323 61.415 40.774 1.00 17.50 N ANISOU 2223 N VAL C 314 2221 2046 2382 138 97 73 N ATOM 2224 CA VAL A 314 43.484 60.549 40.898 1.00 19.38 C ANISOU 2224 CA VAL C 314 2360 2346 2658 -39 77 -21 C ATOM 2225 C VAL A 314 44.610 61.062 39.978 1.00 19.14 C ANISOU 2225 C VAL C 314 2301 2398 2570 39 -159 -25 C ATOM 2226 O VAL A 314 44.368 61.775 38.982 1.00 19.16 O ANISOU 2226 O VAL C 314 2378 2381 2521 -1 -168 -265 O ATOM 2227 CB VAL A 314 43.195 59.067 40.503 1.00 19.59 C ANISOU 2227 CB VAL C 314 2381 2237 2823 157 -37 -72 C ATOM 2228 CG1 VAL A 314 42.184 58.449 41.403 1.00 23.65 C ANISOU 2228 CG1 VAL C 314 2889 2854 3242 -55 -87 43 C ATOM 2229 CG2 VAL A 314 42.763 58.994 39.044 1.00 19.33 C ANISOU 2229 CG2 VAL C 314 2225 2455 2663 68 -105 57 C ATOM 2230 N VAL A 315 45.835 60.651 40.310 1.00 19.10 N ANISOU 2230 N VAL C 315 2506 2348 2403 -5 -240 -83 N ATOM 2231 CA VAL A 315 47.013 60.926 39.522 1.00 20.21 C ANISOU 2231 CA VAL C 315 2520 2418 2739 -21 -96 -74 C ATOM 2232 C VAL A 315 47.415 59.573 38.917 1.00 20.47 C ANISOU 2232 C VAL C 315 2630 2339 2805 -16 -92 -64 C ATOM 2233 O VAL A 315 47.795 58.653 39.641 1.00 20.64 O ANISOU 2233 O VAL C 315 2543 2467 2829 -134 -264 18 O ATOM 2234 CB VAL A 315 48.174 61.530 40.400 1.00 20.45 C ANISOU 2234 CB VAL C 315 2499 2592 2678 -14 -18 -19 C ATOM 2235 CG1 VAL A 315 49.416 61.740 39.560 1.00 19.98 C ANISOU 2235 CG1 VAL C 315 2410 2629 2550 24 -158 -92 C ATOM 2236 CG2 VAL A 315 47.729 62.833 41.095 1.00 21.48 C ANISOU 2236 CG2 VAL C 315 2508 2885 2769 196 76 -79 C ATOM 2237 N VAL A 316 47.297 59.460 37.602 1.00 19.45 N ANISOU 2237 N VAL C 316 2613 2180 2595 0 -113 151 N ATOM 2238 CA VAL A 316 47.501 58.213 36.879 1.00 21.41 C ANISOU 2238 CA VAL C 316 2603 2473 3058 5 -58 77 C ATOM 2239 C VAL A 316 49.019 57.964 36.708 1.00 23.74 C ANISOU 2239 C VAL C 316 2805 2591 3623 25 16 -56 C ATOM 2240 O VAL A 316 49.837 58.901 36.810 1.00 23.10 O ANISOU 2240 O VAL C 316 2599 2299 3875 115 -36 -204 O ATOM 2241 CB VAL A 316 46.794 58.179 35.480 1.00 21.09 C ANISOU 2241 CB VAL C 316 2658 2382 2972 -35 37 136 C ATOM 2242 CG1 VAL A 316 45.266 58.434 35.561 1.00 18.26 C ANISOU 2242 CG1 VAL C 316 2426 2185 2327 -74 329 -7 C ATOM 2243 CG2 VAL A 316 47.383 59.147 34.495 1.00 22.10 C ANISOU 2243 CG2 VAL C 316 2799 2264 3332 176 104 77 C ATOM 2244 N LYS A 317 49.372 56.707 36.442 1.00 23.96 N ANISOU 2244 N LYS C 317 2758 2807 3536 29 28 -2 N ATOM 2245 CA LYS A 317 50.782 56.294 36.353 1.00 25.33 C ANISOU 2245 CA LYS C 317 3038 2966 3619 -34 25 39 C ATOM 2246 C LYS A 317 51.339 56.666 34.982 1.00 26.84 C ANISOU 2246 C LYS C 317 3288 3217 3692 -48 85 233 C ATOM 2247 O LYS A 317 52.173 57.577 34.930 1.00 29.82 O ANISOU 2247 O LYS C 317 3458 3821 4049 38 186 524 O ATOM 2248 CB LYS A 317 50.967 54.821 36.687 1.00 24.03 C ANISOU 2248 CB LYS C 317 2997 2835 3297 137 46 52 C ATOM 2249 CG LYS A 317 52.438 54.374 36.844 1.00 25.02 C ANISOU 2249 CG LYS C 317 2843 2967 3694 -107 -52 46 C ATOM 2250 CD LYS A 317 52.540 52.959 37.401 1.00 25.21 C ANISOU 2250 CD LYS C 317 3100 3072 3404 -40 8 4 C ATOM 2251 CE LYS A 317 53.931 52.323 37.208 1.00 23.87 C ANISOU 2251 CE LYS C 317 2998 2902 3167 116 -90 55 C ATOM 2252 NZ LYS A 317 54.350 52.225 35.775 1.00 19.13 N ANISOU 2252 NZ LYS C 317 2649 1954 2664 167 177 -181 N ATOM 2253 N ASN A 318 50.888 56.031 33.895 1.00 29.50 N ANISOU 2253 N ASN C 318 3642 3529 4034 0 -26 42 N ATOM 2254 CA ASN A 318 51.258 56.437 32.512 1.00 33.18 C ANISOU 2254 CA ASN C 318 4224 4102 4280 66 -5 82 C ATOM 2255 C ASN A 318 50.249 57.374 31.884 1.00 36.43 C ANISOU 2255 C ASN C 318 4629 4472 4738 2 -70 3 C ATOM 2256 O ASN A 318 49.103 56.993 31.660 1.00 38.31 O ANISOU 2256 O ASN C 318 4761 4790 5004 85 -49 -36 O ATOM 2257 CB ASN A 318 51.322 55.249 31.553 1.00 34.90 C ANISOU 2257 CB ASN C 318 4460 4244 4555 53 -100 113 C ATOM 2258 CG ASN A 318 52.447 54.339 31.845 1.00 37.62 C ANISOU 2258 CG ASN C 318 4681 4337 5273 -39 -34 12 C ATOM 2259 OD1 ASN A 318 53.590 54.782 31.955 1.00 31.14 O ANISOU 2259 OD1 ASN C 318 3782 4007 4043 160 -96 103 O ATOM 2260 ND2 ASN A 318 52.149 53.038 31.957 1.00 41.12 N ANISOU 2260 ND2 ASN C 318 4714 5051 5856 87 -160 116 N ATOM 2261 N SER A 319 50.684 58.564 31.515 1.00 37.87 N ANISOU 2261 N SER C 319 4672 4713 5004 28 -33 -31 N ATOM 2262 CA SER A 319 49.760 59.557 30.993 1.00 40.78 C ANISOU 2262 CA SER C 319 5034 5112 5345 -11 -34 -80 C ATOM 2263 C SER A 319 49.996 59.952 29.531 1.00 43.53 C ANISOU 2263 C SER C 319 5508 5529 5502 -2 -28 -35 C ATOM 2264 O SER A 319 49.181 60.655 28.965 1.00 44.29 O ANISOU 2264 O SER C 319 5687 5560 5580 -11 18 -74 O ATOM 2265 CB SER A 319 49.806 60.783 31.897 1.00 40.83 C ANISOU 2265 CB SER C 319 5093 5135 5285 -59 -18 -44 C ATOM 2266 OG SER A 319 51.121 60.989 32.371 1.00 40.10 O ANISOU 2266 OG SER C 319 4753 5104 5378 81 106 -168 O ATOM 2267 N ILE A 320 51.092 59.491 28.926 1.00 46.77 N ANISOU 2267 N ILE C 320 5915 5928 5927 44 31 30 N ATOM 2268 CA ILE A 320 51.474 59.906 27.554 1.00 48.41 C ANISOU 2268 CA ILE C 320 6166 6159 6068 35 -1 63 C ATOM 2269 C ILE A 320 51.133 58.848 26.489 1.00 50.20 C ANISOU 2269 C ILE C 320 6373 6395 6306 24 77 41 C ATOM 2270 O ILE A 320 51.993 58.079 26.041 1.00 51.72 O ANISOU 2270 O ILE C 320 6628 6518 6504 -62 87 90 O ATOM 2271 CB ILE A 320 52.987 60.310 27.455 1.00 50.08 C ANISOU 2271 CB ILE C 320 6404 6260 6363 65 -11 21 C ATOM 2272 CG1 ILE A 320 53.896 59.263 28.115 1.00 50.82 C ANISOU 2272 CG1 ILE C 320 6423 6340 6545 -84 20 81 C ATOM 2273 CG2 ILE A 320 53.210 61.692 28.112 1.00 51.88 C ANISOU 2273 CG2 ILE C 320 6482 6614 6615 -25 21 39 C ATOM 2274 CD1 ILE A 320 55.382 59.360 27.720 1.00 51.00 C ANISOU 2274 CD1 ILE C 320 6518 6385 6474 28 -13 -4 C TER 2275 ILE C 320 ATOM 1 N ASN A 3 65.804 59.201 44.218 1.00 41.21 N ANISOU 1 N ASN D 3 5286 5280 5092 -22 -74 -43 N ATOM 2 CA ASN A 3 66.085 60.673 44.268 1.00 39.21 C ANISOU 2 CA ASN D 3 5022 5109 4767 -38 -65 -41 C ATOM 3 C ASN A 3 66.952 61.178 43.082 1.00 37.49 C ANISOU 3 C ASN D 3 4795 4861 4587 -64 -23 -15 C ATOM 4 O ASN A 3 67.550 62.259 43.141 1.00 37.44 O ANISOU 4 O ASN D 3 4919 4686 4619 71 60 -72 O ATOM 5 CB ASN A 3 66.717 61.049 45.626 1.00 41.38 C ANISOU 5 CB ASN D 3 5312 5433 4974 -42 -12 75 C ATOM 6 CG ASN A 3 68.006 60.283 45.921 1.00 48.08 C ANISOU 6 CG ASN D 3 5930 6164 6173 213 47 -17 C ATOM 7 OD1 ASN A 3 68.095 59.063 45.706 1.00 52.26 O ANISOU 7 OD1 ASN D 3 6786 6322 6747 31 -14 110 O ATOM 8 ND2 ASN A 3 69.011 61.001 46.439 1.00 52.95 N ANISOU 8 ND2 ASN D 3 6357 6739 7022 -38 47 164 N ATOM 9 N VAL A 4 66.963 60.403 41.998 1.00 35.31 N ANISOU 9 N VAL D 4 4388 4697 4331 -67 -63 -91 N ATOM 10 CA VAL A 4 67.826 60.668 40.843 1.00 31.71 C ANISOU 10 CA VAL D 4 4020 4072 3955 -44 105 -190 C ATOM 11 C VAL A 4 66.957 61.200 39.706 1.00 27.77 C ANISOU 11 C VAL D 4 3483 3445 3623 -94 -10 -222 C ATOM 12 O VAL A 4 65.797 60.813 39.543 1.00 25.08 O ANISOU 12 O VAL D 4 3168 3089 3271 -77 -27 -672 O ATOM 13 CB VAL A 4 68.771 59.438 40.503 1.00 32.76 C ANISOU 13 CB VAL D 4 4359 4053 4035 -70 -15 -94 C ATOM 14 CG1 VAL A 4 68.362 58.211 41.299 1.00 38.88 C ANISOU 14 CG1 VAL D 4 5148 4766 4858 -153 -76 -102 C ATOM 15 CG2 VAL A 4 68.820 59.077 39.052 1.00 32.78 C ANISOU 15 CG2 VAL D 4 3984 4240 4228 -90 -120 -128 C ATOM 16 N PHE A 5 67.526 62.126 38.956 1.00 24.57 N ANISOU 16 N PHE D 5 3087 3042 3203 -127 -68 -48 N ATOM 17 CA PHE A 5 66.851 62.752 37.858 1.00 22.77 C ANISOU 17 CA PHE D 5 2768 2855 3026 -125 44 21 C ATOM 18 C PHE A 5 67.897 63.272 36.866 1.00 20.36 C ANISOU 18 C PHE D 5 2512 2661 2561 -18 46 0 C ATOM 19 O PHE A 5 69.104 63.175 37.117 1.00 18.18 O ANISOU 19 O PHE D 5 2408 2268 2229 101 134 -170 O ATOM 20 CB PHE A 5 65.991 63.914 38.350 1.00 22.13 C ANISOU 20 CB PHE D 5 2589 2999 2820 -103 -12 112 C ATOM 21 CG PHE A 5 66.748 64.934 39.158 1.00 21.63 C ANISOU 21 CG PHE D 5 2626 2817 2774 174 -255 210 C ATOM 22 CD1 PHE A 5 67.564 65.898 38.566 1.00 20.25 C ANISOU 22 CD1 PHE D 5 2787 2218 2688 150 -156 217 C ATOM 23 CD2 PHE A 5 66.618 64.946 40.505 1.00 22.10 C ANISOU 23 CD2 PHE D 5 3357 2882 2158 -26 23 -400 C ATOM 24 CE1 PHE A 5 68.292 66.816 39.352 1.00 20.23 C ANISOU 24 CE1 PHE D 5 2597 2626 2463 162 -202 226 C ATOM 25 CE2 PHE A 5 67.323 65.858 41.294 1.00 25.24 C ANISOU 25 CE2 PHE D 5 3557 3021 3011 -429 -89 -134 C ATOM 26 CZ PHE A 5 68.157 66.797 40.708 1.00 21.93 C ANISOU 26 CZ PHE D 5 2850 2780 2698 -256 -61 -169 C ATOM 27 N ASP A 6 67.421 63.852 35.770 1.00 19.30 N ANISOU 27 N ASP D 6 2270 2422 2640 -133 251 60 N ATOM 28 CA ASP A 6 68.267 64.502 34.764 1.00 19.59 C ANISOU 28 CA ASP D 6 2476 2422 2542 -10 73 -2 C ATOM 29 C ASP A 6 67.653 65.841 34.335 1.00 18.64 C ANISOU 29 C ASP D 6 2253 2408 2419 -68 71 38 C ATOM 30 O ASP A 6 66.584 66.238 34.812 1.00 16.78 O ANISOU 30 O ASP D 6 2297 2168 1908 -309 -195 315 O ATOM 31 CB ASP A 6 68.469 63.599 33.541 1.00 19.47 C ANISOU 31 CB ASP D 6 2488 2443 2466 -69 100 -155 C ATOM 32 CG ASP A 6 69.861 63.739 32.919 1.00 18.97 C ANISOU 32 CG ASP D 6 2318 2317 2572 -79 160 6 C ATOM 33 OD1 ASP A 6 70.593 64.718 33.228 1.00 15.50 O ANISOU 33 OD1 ASP D 6 1605 2445 1837 -152 -248 108 O ATOM 34 OD2 ASP A 6 70.225 62.890 32.089 1.00 24.72 O ANISOU 34 OD2 ASP D 6 2958 2981 3452 -287 -189 221 O ATOM 35 N TYR A 7 68.348 66.510 33.414 1.00 18.62 N ANISOU 35 N TYR D 7 2237 2445 2391 94 34 -49 N ATOM 36 CA TYR A 7 68.009 67.854 32.921 1.00 18.78 C ANISOU 36 CA TYR D 7 2396 2341 2399 28 -17 -38 C ATOM 37 C TYR A 7 66.535 68.020 32.581 1.00 17.77 C ANISOU 37 C TYR D 7 2258 2182 2310 24 -46 -139 C ATOM 38 O TYR A 7 65.901 68.989 33.029 1.00 19.79 O ANISOU 38 O TYR D 7 2403 2263 2852 65 -178 -296 O ATOM 39 CB TYR A 7 68.886 68.202 31.710 1.00 19.13 C ANISOU 39 CB TYR D 7 2368 2343 2555 35 -45 -74 C ATOM 40 CG TYR A 7 70.311 68.527 32.126 1.00 18.94 C ANISOU 40 CG TYR D 7 2359 2094 2740 0 -50 52 C ATOM 41 CD1 TYR A 7 70.622 69.746 32.750 1.00 18.84 C ANISOU 41 CD1 TYR D 7 2132 2175 2848 63 7 173 C ATOM 42 CD2 TYR A 7 71.340 67.608 31.945 1.00 17.89 C ANISOU 42 CD2 TYR D 7 2141 2198 2456 55 -10 41 C ATOM 43 CE1 TYR A 7 71.905 70.030 33.156 1.00 18.35 C ANISOU 43 CE1 TYR D 7 2299 2070 2602 27 -86 38 C ATOM 44 CE2 TYR A 7 72.622 67.902 32.328 1.00 20.83 C ANISOU 44 CE2 TYR D 7 2278 2412 3222 -31 32 60 C ATOM 45 CZ TYR A 7 72.909 69.108 32.946 1.00 21.07 C ANISOU 45 CZ TYR D 7 2320 2505 3178 59 -94 165 C ATOM 46 OH TYR A 7 74.208 69.403 33.359 1.00 20.80 O ANISOU 46 OH TYR D 7 2448 2019 3434 147 126 26 O ATOM 47 N GLU A 8 65.997 67.077 31.815 1.00 18.34 N ANISOU 47 N GLU D 8 2254 2200 2511 109 18 -93 N ATOM 48 CA GLU A 8 64.608 67.152 31.331 1.00 18.39 C ANISOU 48 CA GLU D 8 2407 2216 2362 -29 85 76 C ATOM 49 C GLU A 8 63.543 67.084 32.436 1.00 19.19 C ANISOU 49 C GLU D 8 2425 2353 2511 9 140 35 C ATOM 50 O GLU A 8 62.380 67.492 32.219 1.00 21.48 O ANISOU 50 O GLU D 8 2465 2900 2794 237 -22 169 O ATOM 51 CB GLU A 8 64.383 66.101 30.197 1.00 19.09 C ANISOU 51 CB GLU D 8 2484 2424 2342 3 -3 143 C ATOM 52 CG GLU A 8 64.210 64.661 30.650 1.00 16.06 C ANISOU 52 CG GLU D 8 2637 2167 1296 -61 10 356 C ATOM 53 CD GLU A 8 65.499 63.865 30.756 1.00 25.03 C ANISOU 53 CD GLU D 8 3167 3034 3309 98 -42 138 C ATOM 54 OE1 GLU A 8 66.589 64.492 30.827 1.00 27.68 O ANISOU 54 OE1 GLU D 8 3264 3476 3775 -64 -451 425 O ATOM 55 OE2 GLU A 8 65.414 62.593 30.792 1.00 21.93 O ANISOU 55 OE2 GLU D 8 3517 2913 1902 -271 -378 -61 O ATOM 56 N ASP A 9 63.926 66.607 33.631 1.00 17.03 N ANISOU 56 N ASP D 9 2241 2050 2177 0 98 203 N ATOM 57 CA ASP A 9 63.007 66.470 34.720 1.00 17.43 C ANISOU 57 CA ASP D 9 2173 2096 2353 -72 61 37 C ATOM 58 C ASP A 9 62.913 67.753 35.566 1.00 17.35 C ANISOU 58 C ASP D 9 2150 2205 2236 3 -19 95 C ATOM 59 O ASP A 9 62.024 67.877 36.395 1.00 18.15 O ANISOU 59 O ASP D 9 1974 2277 2643 -45 -175 198 O ATOM 60 CB ASP A 9 63.475 65.346 35.638 1.00 17.67 C ANISOU 60 CB ASP D 9 2021 2311 2379 -60 9 -74 C ATOM 61 CG ASP A 9 63.590 64.022 34.909 1.00 21.03 C ANISOU 61 CG ASP D 9 2673 2401 2915 -155 171 9 C ATOM 62 OD1 ASP A 9 62.578 63.637 34.256 1.00 18.68 O ANISOU 62 OD1 ASP D 9 2645 2353 2100 -173 360 10 O ATOM 63 OD2 ASP A 9 64.676 63.389 34.988 1.00 21.89 O ANISOU 63 OD2 ASP D 9 2519 2832 2964 -178 76 142 O ATOM 64 N ILE A 10 63.830 68.693 35.377 1.00 16.30 N ANISOU 64 N ILE D 10 2088 2006 2098 7 25 103 N ATOM 65 CA ILE A 10 63.893 69.870 36.257 1.00 17.32 C ANISOU 65 CA ILE D 10 2205 2105 2269 -49 64 37 C ATOM 66 C ILE A 10 63.269 71.118 35.640 1.00 16.31 C ANISOU 66 C ILE D 10 2148 1905 2142 -49 28 69 C ATOM 67 O ILE A 10 63.529 71.442 34.472 1.00 17.75 O ANISOU 67 O ILE D 10 2239 2158 2347 9 10 111 O ATOM 68 CB ILE A 10 65.364 70.182 36.666 1.00 17.66 C ANISOU 68 CB ILE D 10 2154 2240 2314 -79 -11 7 C ATOM 69 CG1 ILE A 10 65.969 69.049 37.501 1.00 18.85 C ANISOU 69 CG1 ILE D 10 2158 2081 2924 -174 223 0 C ATOM 70 CG2 ILE A 10 65.441 71.511 37.488 1.00 18.78 C ANISOU 70 CG2 ILE D 10 2418 2159 2557 -78 209 32 C ATOM 71 CD1 ILE A 10 65.214 68.747 38.746 1.00 22.83 C ANISOU 71 CD1 ILE D 10 2409 3125 3138 62 190 -58 C ATOM 72 N GLN A 11 62.451 71.819 36.429 1.00 16.01 N ANISOU 72 N GLN D 11 2026 2055 2002 20 -119 -105 N ATOM 73 CA GLN A 11 62.071 73.214 36.111 1.00 17.07 C ANISOU 73 CA GLN D 11 2182 2101 2201 -10 -44 -25 C ATOM 74 C GLN A 11 62.477 74.128 37.217 1.00 15.69 C ANISOU 74 C GLN D 11 1957 1956 2045 -6 -48 -76 C ATOM 75 O GLN A 11 62.226 73.841 38.397 1.00 15.79 O ANISOU 75 O GLN D 11 2351 1772 1877 -11 -311 75 O ATOM 76 CB GLN A 11 60.556 73.376 35.891 1.00 18.13 C ANISOU 76 CB GLN D 11 2276 2187 2425 -15 -148 -66 C ATOM 77 CG GLN A 11 60.031 72.765 34.624 1.00 21.51 C ANISOU 77 CG GLN D 11 2640 2874 2658 140 335 -2 C ATOM 78 CD GLN A 11 60.421 73.559 33.375 1.00 30.51 C ANISOU 78 CD GLN D 11 4162 3696 3734 -3 -204 -214 C ATOM 79 OE1 GLN A 11 60.216 74.756 33.294 1.00 34.17 O ANISOU 79 OE1 GLN D 11 5087 3813 4082 368 -249 99 O ATOM 80 NE2 GLN A 11 60.999 72.874 32.401 1.00 33.86 N ANISOU 80 NE2 GLN D 11 4510 4389 3966 56 -20 82 N ATOM 81 N LEU A 12 63.140 75.223 36.869 1.00 15.16 N ANISOU 81 N LEU D 12 1907 1836 2014 103 -77 -135 N ATOM 82 CA LEU A 12 63.476 76.252 37.868 1.00 15.88 C ANISOU 82 CA LEU D 12 1964 1998 2072 -38 16 -54 C ATOM 83 C LEU A 12 62.300 77.236 38.052 1.00 15.72 C ANISOU 83 C LEU D 12 1995 1917 2060 -4 -17 -18 C ATOM 84 O LEU A 12 61.598 77.623 37.079 1.00 17.40 O ANISOU 84 O LEU D 12 2027 2125 2457 256 -17 217 O ATOM 85 CB LEU A 12 64.766 77.016 37.450 1.00 16.27 C ANISOU 85 CB LEU D 12 1845 2093 2245 -86 9 67 C ATOM 86 CG LEU A 12 65.964 76.105 37.077 1.00 17.96 C ANISOU 86 CG LEU D 12 1992 2517 2313 24 -57 -44 C ATOM 87 CD1 LEU A 12 67.146 76.898 36.569 1.00 19.70 C ANISOU 87 CD1 LEU D 12 2160 2288 3034 -100 -77 -21 C ATOM 88 CD2 LEU A 12 66.377 75.226 38.249 1.00 16.81 C ANISOU 88 CD2 LEU D 12 1617 2300 2471 213 -220 35 C ATOM 89 N ILE A 13 62.117 77.668 39.279 1.00 17.01 N ANISOU 89 N ILE D 13 2170 2036 2253 42 90 -119 N ATOM 90 CA ILE A 13 61.017 78.487 39.665 1.00 17.96 C ANISOU 90 CA ILE D 13 2247 2176 2397 28 34 -19 C ATOM 91 C ILE A 13 61.423 79.969 39.675 1.00 19.00 C ANISOU 91 C ILE D 13 2296 2265 2655 -67 39 83 C ATOM 92 O ILE A 13 62.418 80.363 40.313 1.00 20.30 O ANISOU 92 O ILE D 13 2468 2507 2735 107 95 415 O ATOM 93 CB ILE A 13 60.469 78.086 41.023 1.00 19.01 C ANISOU 93 CB ILE D 13 2321 2167 2732 -47 -148 -53 C ATOM 94 CG1 ILE A 13 59.886 76.663 40.912 1.00 19.59 C ANISOU 94 CG1 ILE D 13 2677 2123 2641 -28 -73 276 C ATOM 95 CG2 ILE A 13 59.364 79.084 41.508 1.00 19.75 C ANISOU 95 CG2 ILE D 13 2556 2284 2660 -17 -98 -98 C ATOM 96 CD1 ILE A 13 59.532 76.058 42.211 1.00 20.35 C ANISOU 96 CD1 ILE D 13 2821 2328 2581 -101 -129 9 C ATOM 97 N PRO A 14 60.644 80.789 38.966 1.00 18.60 N ANISOU 97 N PRO D 14 2394 2301 2372 -126 -8 -100 N ATOM 98 CA PRO A 14 60.935 82.224 38.906 1.00 18.78 C ANISOU 98 CA PRO D 14 2380 2333 2422 42 -29 8 C ATOM 99 C PRO A 14 60.823 82.955 40.252 1.00 19.36 C ANISOU 99 C PRO D 14 2558 2368 2428 -6 19 93 C ATOM 100 O PRO A 14 59.991 82.604 41.114 1.00 18.63 O ANISOU 100 O PRO D 14 2764 2164 2149 -159 -82 295 O ATOM 101 CB PRO A 14 59.919 82.747 37.892 1.00 18.93 C ANISOU 101 CB PRO D 14 2451 2344 2397 89 76 -73 C ATOM 102 CG PRO A 14 59.492 81.550 37.104 1.00 20.88 C ANISOU 102 CG PRO D 14 2563 2543 2828 192 166 -181 C ATOM 103 CD PRO A 14 59.474 80.458 38.148 1.00 20.71 C ANISOU 103 CD PRO D 14 2535 2627 2705 -268 -21 -117 C ATOM 104 N ALA A 15 61.647 83.976 40.394 1.00 18.88 N ANISOU 104 N ALA D 15 2455 2342 2377 -3 103 174 N ATOM 105 CA ALA A 15 61.605 84.877 41.554 1.00 20.19 C ANISOU 105 CA ALA D 15 2668 2505 2495 24 19 67 C ATOM 106 C ALA A 15 61.314 86.310 41.048 1.00 20.31 C ANISOU 106 C ALA D 15 2749 2440 2527 89 -51 54 C ATOM 107 O ALA A 15 61.402 86.568 39.831 1.00 18.57 O ANISOU 107 O ALA D 15 2628 2176 2248 263 163 -159 O ATOM 108 CB ALA A 15 62.914 84.815 42.228 1.00 21.80 C ANISOU 108 CB ALA D 15 2908 2691 2683 116 50 225 C ATOM 109 N LYS A 16 60.988 87.238 41.953 1.00 20.94 N ANISOU 109 N LYS D 16 2762 2603 2590 -39 61 60 N ATOM 110 CA LYS A 16 60.637 88.609 41.532 1.00 21.33 C ANISOU 110 CA LYS D 16 2758 2587 2759 31 119 69 C ATOM 111 C LYS A 16 61.706 89.216 40.620 1.00 20.26 C ANISOU 111 C LYS D 16 2647 2284 2766 145 60 231 C ATOM 112 O LYS A 16 62.890 89.267 40.988 1.00 19.71 O ANISOU 112 O LYS D 16 2481 2384 2622 -140 13 224 O ATOM 113 CB LYS A 16 60.393 89.524 42.737 1.00 22.97 C ANISOU 113 CB LYS D 16 2860 2761 3104 -19 101 -44 C ATOM 114 CG LYS A 16 59.782 90.869 42.379 1.00 23.21 C ANISOU 114 CG LYS D 16 3002 2769 3046 -52 175 16 C ATOM 115 CD LYS A 16 59.695 91.697 43.612 1.00 24.98 C ANISOU 115 CD LYS D 16 3355 2990 3147 141 69 95 C ATOM 116 CE LYS A 16 58.867 92.903 43.458 1.00 29.28 C ANISOU 116 CE LYS D 16 3901 3535 3689 249 -19 -72 C ATOM 117 NZ LYS A 16 58.804 93.609 44.756 1.00 29.87 N ANISOU 117 NZ LYS D 16 4373 3184 3791 -171 101 160 N ATOM 118 N CYS A 17 61.289 89.691 39.443 1.00 20.71 N ANISOU 118 N CYS D 17 2673 2494 2701 95 112 435 N ATOM 119 CA CYS A 17 62.188 90.328 38.491 1.00 22.28 C ANISOU 119 CA CYS D 17 2865 2612 2988 0 143 146 C ATOM 120 C CYS A 17 62.566 91.705 38.979 1.00 22.34 C ANISOU 120 C CYS D 17 2884 2614 2990 7 147 174 C ATOM 121 O CYS A 17 61.680 92.500 39.325 1.00 21.11 O ANISOU 121 O CYS D 17 2674 2357 2990 -111 352 274 O ATOM 122 CB CYS A 17 61.543 90.472 37.123 1.00 21.90 C ANISOU 122 CB CYS D 17 3110 2435 2774 7 141 257 C ATOM 123 SG CYS A 17 62.606 91.042 35.787 1.00 25.86 S ANISOU 123 SG CYS D 17 3269 3112 3442 -128 -53 366 S ATOM 124 N ILE A 18 63.870 91.976 38.979 1.00 23.31 N ANISOU 124 N ILE D 18 2704 2705 3446 26 191 107 N ATOM 125 CA ILE A 18 64.436 93.262 39.495 1.00 24.28 C ANISOU 125 CA ILE D 18 3038 2826 3360 -15 147 168 C ATOM 126 C ILE A 18 65.192 94.065 38.458 1.00 24.56 C ANISOU 126 C ILE D 18 3030 2978 3323 -10 243 62 C ATOM 127 O ILE A 18 65.720 95.147 38.775 1.00 27.45 O ANISOU 127 O ILE D 18 3626 3112 3691 13 287 -85 O ATOM 128 CB ILE A 18 65.381 93.076 40.730 1.00 23.30 C ANISOU 128 CB ILE D 18 2966 2803 3084 -77 67 128 C ATOM 129 CG1 ILE A 18 66.655 92.293 40.337 1.00 21.87 C ANISOU 129 CG1 ILE D 18 2944 2403 2961 -104 139 139 C ATOM 130 CG2 ILE A 18 64.644 92.506 41.931 1.00 21.14 C ANISOU 130 CG2 ILE D 18 2663 2341 3028 -172 284 258 C ATOM 131 CD1 ILE A 18 67.610 92.031 41.477 1.00 25.35 C ANISOU 131 CD1 ILE D 18 3430 2647 3554 -35 277 135 C ATOM 132 N VAL A 19 65.227 93.587 37.219 1.00 24.48 N ANISOU 132 N VAL D 19 3050 2865 3385 97 48 124 N ATOM 133 CA VAL A 19 65.858 94.308 36.140 1.00 27.84 C ANISOU 133 CA VAL D 19 3537 3369 3672 -27 33 59 C ATOM 134 C VAL A 19 64.789 94.847 35.184 1.00 29.27 C ANISOU 134 C VAL D 19 3664 3610 3843 -11 112 27 C ATOM 135 O VAL A 19 63.693 94.283 35.053 1.00 28.29 O ANISOU 135 O VAL D 19 3578 3433 3737 2 188 23 O ATOM 136 CB VAL A 19 66.910 93.458 35.343 1.00 27.25 C ANISOU 136 CB VAL D 19 3429 3360 3563 -48 -21 -76 C ATOM 137 CG1 VAL A 19 68.043 92.996 36.260 1.00 26.70 C ANISOU 137 CG1 VAL D 19 3178 3340 3625 -19 -72 9 C ATOM 138 CG2 VAL A 19 66.250 92.264 34.622 1.00 25.28 C ANISOU 138 CG2 VAL D 19 3436 3265 2901 56 -54 -58 C ATOM 139 N ASN A 20 65.117 95.956 34.537 1.00 32.14 N ANISOU 139 N ASN D 20 4061 3979 4172 -58 29 -63 N ATOM 140 CA ASN A 20 64.256 96.547 33.520 1.00 33.79 C ANISOU 140 CA ASN D 20 4277 4248 4312 7 51 -147 C ATOM 141 C ASN A 20 64.554 96.008 32.157 1.00 34.71 C ANISOU 141 C ASN D 20 4391 4377 4421 4 -25 -116 C ATOM 142 O ASN A 20 63.757 96.187 31.241 1.00 34.40 O ANISOU 142 O ASN D 20 4438 4485 4145 227 -127 -446 O ATOM 143 CB ASN A 20 64.416 98.064 33.483 1.00 35.79 C ANISOU 143 CB ASN D 20 4544 4431 4624 31 4 -110 C ATOM 144 CG ASN A 20 63.616 98.753 34.539 1.00 41.65 C ANISOU 144 CG ASN D 20 5284 5247 5293 162 -167 48 C ATOM 145 OD1 ASN A 20 62.493 98.344 34.858 1.00 45.25 O ANISOU 145 OD1 ASN D 20 5308 5599 6284 30 -123 -8 O ATOM 146 ND2 ASN A 20 64.179 99.824 35.090 1.00 46.19 N ANISOU 146 ND2 ASN D 20 5860 5755 5936 -20 132 171 N ATOM 147 N SER A 21 65.693 95.342 32.017 1.00 35.71 N ANISOU 147 N SER D 21 4493 4461 4613 71 -7 -168 N ATOM 148 CA SER A 21 66.085 94.758 30.747 1.00 36.77 C ANISOU 148 CA SER D 21 4702 4585 4681 85 -9 -110 C ATOM 149 C SER A 21 67.123 93.666 30.942 1.00 36.55 C ANISOU 149 C SER D 21 4647 4478 4761 135 18 -120 C ATOM 150 O SER A 21 68.058 93.855 31.701 1.00 36.04 O ANISOU 150 O SER D 21 4500 4284 4907 262 156 -201 O ATOM 151 CB SER A 21 66.745 95.816 29.881 1.00 38.08 C ANISOU 151 CB SER D 21 4972 4734 4759 70 -24 -195 C ATOM 152 OG SER A 21 67.132 95.244 28.653 1.00 41.52 O ANISOU 152 OG SER D 21 5604 5063 5105 138 -237 75 O ATOM 153 N ARG A 22 66.962 92.566 30.219 1.00 37.97 N ANISOU 153 N ARG D 22 4826 4764 4835 142 26 4 N ATOM 154 CA ARG A 22 67.977 91.484 30.131 1.00 38.56 C ANISOU 154 CA ARG D 22 4901 4835 4914 128 20 -16 C ATOM 155 C ARG A 22 69.391 91.981 30.071 1.00 38.28 C ANISOU 155 C ARG D 22 4899 4835 4811 95 -95 -98 C ATOM 156 O ARG A 22 70.309 91.364 30.620 1.00 37.44 O ANISOU 156 O ARG D 22 4886 4732 4607 254 -271 -237 O ATOM 157 CB ARG A 22 67.821 90.723 28.825 1.00 38.40 C ANISOU 157 CB ARG D 22 4874 4921 4795 151 6 -14 C ATOM 158 CG ARG A 22 66.851 89.631 28.851 1.00 39.58 C ANISOU 158 CG ARG D 22 5136 4886 5014 86 46 -5 C ATOM 159 CD ARG A 22 67.202 88.610 27.816 1.00 40.57 C ANISOU 159 CD ARG D 22 5167 5136 5111 54 -33 54 C ATOM 160 NE ARG A 22 67.450 89.181 26.504 1.00 41.19 N ANISOU 160 NE ARG D 22 5484 5136 5028 86 5 -165 N ATOM 161 CZ ARG A 22 67.168 88.555 25.361 1.00 44.06 C ANISOU 161 CZ ARG D 22 5654 5517 5567 -82 4 56 C ATOM 162 NH1 ARG A 22 66.642 87.337 25.370 1.00 45.31 N ANISOU 162 NH1 ARG D 22 5748 5531 5936 -5 12 -76 N ATOM 163 NH2 ARG A 22 67.415 89.146 24.191 1.00 43.34 N ANISOU 163 NH2 ARG D 22 5568 5589 5307 -72 176 -142 N ATOM 164 N SER A 23 69.562 93.071 29.322 1.00 38.41 N ANISOU 164 N SER D 23 5013 4748 4833 117 -64 -144 N ATOM 165 CA SER A 23 70.855 93.705 29.137 1.00 38.28 C ANISOU 165 CA SER D 23 4946 4747 4851 62 0 -113 C ATOM 166 C SER A 23 71.542 94.091 30.426 1.00 37.10 C ANISOU 166 C SER D 23 4754 4440 4903 9 -16 -117 C ATOM 167 O SER A 23 72.758 94.205 30.435 1.00 38.76 O ANISOU 167 O SER D 23 4921 4559 5245 -51 -145 -329 O ATOM 168 CB SER A 23 70.700 94.934 28.236 1.00 40.30 C ANISOU 168 CB SER D 23 5254 4943 5112 -43 4 -145 C ATOM 169 OG SER A 23 70.051 94.549 27.028 1.00 44.65 O ANISOU 169 OG SER D 23 5860 5970 5135 -107 -7 -90 O ATOM 170 N GLU A 24 70.779 94.258 31.507 1.00 35.13 N ANISOU 170 N GLU D 24 4422 4166 4759 -10 -34 -144 N ATOM 171 CA GLU A 24 71.333 94.519 32.820 1.00 34.55 C ANISOU 171 CA GLU D 24 4349 4114 4663 -1 -45 -103 C ATOM 172 C GLU A 24 72.018 93.312 33.458 1.00 33.16 C ANISOU 172 C GLU D 24 4152 3920 4527 -8 -28 -14 C ATOM 173 O GLU A 24 72.714 93.481 34.439 1.00 32.76 O ANISOU 173 O GLU D 24 4336 3581 4530 136 52 -57 O ATOM 174 CB GLU A 24 70.247 94.987 33.809 1.00 36.13 C ANISOU 174 CB GLU D 24 4493 4258 4977 4 -38 -92 C ATOM 175 CG GLU A 24 69.718 96.391 33.601 1.00 36.81 C ANISOU 175 CG GLU D 24 4561 4448 4975 -25 -101 -79 C ATOM 176 CD GLU A 24 68.566 96.715 34.542 1.00 36.65 C ANISOU 176 CD GLU D 24 4609 4418 4894 0 -38 5 C ATOM 177 OE1 GLU A 24 68.782 96.733 35.786 1.00 39.64 O ANISOU 177 OE1 GLU D 24 5255 4825 4980 -212 -160 79 O ATOM 178 OE2 GLU A 24 67.452 96.944 34.028 1.00 38.66 O ANISOU 178 OE2 GLU D 24 4435 4610 5644 99 42 -32 O ATOM 179 N CYS A 25 71.800 92.101 32.944 1.00 32.46 N ANISOU 179 N CYS D 25 3884 3972 4475 79 -116 -18 N ATOM 180 CA CYS A 25 72.280 90.897 33.646 1.00 30.17 C ANISOU 180 CA CYS D 25 3628 3708 4124 14 -95 -47 C ATOM 181 C CYS A 25 73.704 90.501 33.222 1.00 29.73 C ANISOU 181 C CYS D 25 3649 3622 4023 16 -48 -39 C ATOM 182 O CYS A 25 74.010 90.438 32.041 1.00 29.80 O ANISOU 182 O CYS D 25 3451 3661 4208 58 -289 86 O ATOM 183 CB CYS A 25 71.324 89.734 33.407 1.00 28.97 C ANISOU 183 CB CYS D 25 3390 3748 3868 118 -94 41 C ATOM 184 SG CYS A 25 69.637 90.163 33.866 1.00 26.84 S ANISOU 184 SG CYS D 25 2877 2873 4446 -31 -317 -238 S ATOM 185 N ASP A 26 74.545 90.214 34.210 1.00 30.02 N ANISOU 185 N ASP D 26 3671 3526 4208 36 10 47 N ATOM 186 CA ASP A 26 75.953 89.905 33.974 1.00 28.84 C ANISOU 186 CA ASP D 26 3577 3402 3979 65 -7 -25 C ATOM 187 C ASP A 26 76.127 88.373 33.967 1.00 28.06 C ANISOU 187 C ASP D 26 3419 3281 3960 72 26 -75 C ATOM 188 O ASP A 26 75.929 87.745 35.005 1.00 28.97 O ANISOU 188 O ASP D 26 3465 2973 4568 21 -68 -309 O ATOM 189 CB ASP A 26 76.803 90.526 35.087 1.00 29.35 C ANISOU 189 CB ASP D 26 3655 3421 4075 84 26 18 C ATOM 190 CG ASP A 26 78.321 90.343 34.865 1.00 32.52 C ANISOU 190 CG ASP D 26 3816 4060 4481 25 -81 151 C ATOM 191 OD1 ASP A 26 78.773 89.377 34.207 1.00 32.98 O ANISOU 191 OD1 ASP D 26 4088 3635 4805 -112 -75 318 O ATOM 192 OD2 ASP A 26 79.077 91.191 35.363 1.00 40.07 O ANISOU 192 OD2 ASP D 26 4927 4917 5380 -260 7 406 O ATOM 193 N THR A 27 76.521 87.818 32.826 1.00 27.61 N ANISOU 193 N THR D 27 3303 3204 3981 76 50 -94 N ATOM 194 CA THR A 27 76.750 86.353 32.642 1.00 27.37 C ANISOU 194 CA THR D 27 3305 3250 3844 21 34 -22 C ATOM 195 C THR A 27 78.218 85.862 32.806 1.00 26.59 C ANISOU 195 C THR D 27 3199 3140 3764 3 11 86 C ATOM 196 O THR A 27 78.541 84.696 32.506 1.00 24.14 O ANISOU 196 O THR D 27 2950 2706 3516 54 120 -143 O ATOM 197 CB THR A 27 76.331 85.919 31.250 1.00 27.47 C ANISOU 197 CB THR D 27 3373 3300 3764 76 10 -94 C ATOM 198 OG1 THR A 27 77.166 86.560 30.277 1.00 30.70 O ANISOU 198 OG1 THR D 27 3216 3757 4692 96 -140 -205 O ATOM 199 CG2 THR A 27 74.866 86.238 30.987 1.00 23.94 C ANISOU 199 CG2 THR D 27 3069 3191 2837 142 -116 -360 C ATOM 200 N THR A 28 79.104 86.739 33.263 1.00 25.87 N ANISOU 200 N THR D 28 3110 3037 3681 -105 44 255 N ATOM 201 CA THR A 28 80.531 86.391 33.344 1.00 25.92 C ANISOU 201 CA THR D 28 3185 3141 3522 -63 -14 174 C ATOM 202 C THR A 28 80.815 85.413 34.463 1.00 26.69 C ANISOU 202 C THR D 28 3252 3227 3660 -73 -45 162 C ATOM 203 O THR A 28 80.054 85.313 35.451 1.00 26.68 O ANISOU 203 O THR D 28 2955 3053 4127 118 -316 405 O ATOM 204 CB THR A 28 81.428 87.635 33.559 1.00 25.13 C ANISOU 204 CB THR D 28 3078 3202 3266 -68 -80 145 C ATOM 205 OG1 THR A 28 81.135 88.228 34.839 1.00 25.67 O ANISOU 205 OG1 THR D 28 3384 3107 3261 156 -368 211 O ATOM 206 CG2 THR A 28 81.209 88.625 32.477 1.00 23.30 C ANISOU 206 CG2 THR D 28 2534 3023 3293 -61 -80 52 C ATOM 207 N VAL A 29 81.917 84.680 34.297 1.00 26.63 N ANISOU 207 N VAL D 29 3133 3310 3672 -110 -101 104 N ATOM 208 CA VAL A 29 82.470 83.809 35.342 1.00 26.04 C ANISOU 208 CA VAL D 29 3225 3241 3426 -119 -72 42 C ATOM 209 C VAL A 29 84.009 83.835 35.353 1.00 24.60 C ANISOU 209 C VAL D 29 3107 2980 3258 6 -70 98 C ATOM 210 O VAL A 29 84.630 84.095 34.323 1.00 26.70 O ANISOU 210 O VAL D 29 3395 3095 3655 -64 -136 140 O ATOM 211 CB VAL A 29 81.932 82.348 35.191 1.00 27.32 C ANISOU 211 CB VAL D 29 3377 3336 3666 -59 -47 47 C ATOM 212 CG1 VAL A 29 82.490 81.664 33.954 1.00 26.84 C ANISOU 212 CG1 VAL D 29 3477 3098 3622 -250 217 246 C ATOM 213 CG2 VAL A 29 82.171 81.545 36.456 1.00 27.75 C ANISOU 213 CG2 VAL D 29 3362 3375 3806 -78 -80 45 C ATOM 214 N THR A 30 84.592 83.628 36.527 1.00 24.75 N ANISOU 214 N THR D 30 3141 2865 3396 -17 -74 -63 N ATOM 215 CA THR A 30 86.057 83.525 36.729 1.00 25.08 C ANISOU 215 CA THR D 30 3131 3133 3263 -12 -123 -18 C ATOM 216 C THR A 30 86.429 82.065 37.015 1.00 25.30 C ANISOU 216 C THR D 30 3062 3198 3349 -4 -130 31 C ATOM 217 O THR A 30 85.742 81.354 37.762 1.00 26.29 O ANISOU 217 O THR D 30 2894 3228 3866 -12 -215 10 O ATOM 218 CB THR A 30 86.563 84.424 37.923 1.00 26.47 C ANISOU 218 CB THR D 30 3190 3306 3558 8 -9 -9 C ATOM 219 OG1 THR A 30 86.284 85.815 37.680 1.00 27.27 O ANISOU 219 OG1 THR D 30 3705 2972 3683 -111 -132 232 O ATOM 220 CG2 THR A 30 88.044 84.293 38.164 1.00 25.70 C ANISOU 220 CG2 THR D 30 3248 3206 3308 27 -41 -30 C ATOM 221 N LEU A 31 87.534 81.630 36.425 1.00 24.88 N ANISOU 221 N LEU D 31 2950 3219 3283 -109 -79 32 N ATOM 222 CA LEU A 31 88.109 80.320 36.665 1.00 25.19 C ANISOU 222 CA LEU D 31 3164 3086 3319 -73 -66 -27 C ATOM 223 C LEU A 31 89.602 80.539 36.827 1.00 25.34 C ANISOU 223 C LEU D 31 3235 2935 3458 -28 -62 59 C ATOM 224 O LEU A 31 90.286 80.944 35.888 1.00 26.34 O ANISOU 224 O LEU D 31 3171 3000 3836 13 -218 51 O ATOM 225 CB LEU A 31 87.818 79.369 35.493 1.00 24.37 C ANISOU 225 CB LEU D 31 3012 3086 3161 -101 -158 -13 C ATOM 226 CG LEU A 31 88.230 77.895 35.615 1.00 24.13 C ANISOU 226 CG LEU D 31 2996 3221 2948 -112 -30 -103 C ATOM 227 CD1 LEU A 31 87.392 77.192 36.709 1.00 24.69 C ANISOU 227 CD1 LEU D 31 3177 3317 2887 -260 0 -22 C ATOM 228 CD2 LEU A 31 88.125 77.129 34.265 1.00 24.10 C ANISOU 228 CD2 LEU D 31 3089 2927 3140 -76 -24 -84 C ATOM 229 N GLY A 32 90.086 80.314 38.037 1.00 28.24 N ANISOU 229 N GLY D 32 3400 3288 4041 -63 92 -75 N ATOM 230 CA GLY A 32 91.454 80.672 38.394 1.00 29.78 C ANISOU 230 CA GLY D 32 3591 3660 4061 -61 72 -22 C ATOM 231 C GLY A 32 91.642 82.167 38.264 1.00 30.24 C ANISOU 231 C GLY D 32 3762 3612 4113 -139 59 80 C ATOM 232 O GLY A 32 90.855 82.939 38.799 1.00 31.47 O ANISOU 232 O GLY D 32 3974 3757 4224 -229 30 120 O ATOM 233 N LYS A 33 92.647 82.565 37.495 1.00 32.50 N ANISOU 233 N LYS D 33 4137 3870 4339 -112 26 13 N ATOM 234 CA LYS A 33 93.062 83.981 37.395 1.00 33.45 C ANISOU 234 CA LYS D 33 4245 4032 4431 -107 28 -31 C ATOM 235 C LYS A 33 92.417 84.765 36.252 1.00 33.67 C ANISOU 235 C LYS D 33 4254 4012 4526 -106 64 -61 C ATOM 236 O LYS A 33 92.745 85.934 36.059 1.00 35.63 O ANISOU 236 O LYS D 33 4457 4163 4915 -216 64 -87 O ATOM 237 CB LYS A 33 94.580 84.046 37.226 1.00 35.56 C ANISOU 237 CB LYS D 33 4473 4269 4768 -138 21 44 C ATOM 238 CG LYS A 33 95.344 83.688 38.494 1.00 38.34 C ANISOU 238 CG LYS D 33 4815 4881 4869 -76 88 -34 C ATOM 239 CD LYS A 33 96.776 83.293 38.126 1.00 38.41 C ANISOU 239 CD LYS D 33 4737 4897 4959 20 64 -92 C ATOM 240 CE LYS A 33 97.651 83.176 39.361 1.00 41.80 C ANISOU 240 CE LYS D 33 5031 5457 5394 7 311 -95 C ATOM 241 NZ LYS A 33 98.781 82.225 39.100 1.00 47.74 N ANISOU 241 NZ LYS D 33 5558 6152 6427 311 75 48 N ATOM 242 N HIS A 34 91.507 84.147 35.499 1.00 31.70 N ANISOU 242 N HIS D 34 4004 3799 4240 -104 -17 -17 N ATOM 243 CA HIS A 34 90.909 84.805 34.363 1.00 30.10 C ANISOU 243 CA HIS D 34 3695 3682 4058 -94 -43 9 C ATOM 244 C HIS A 34 89.378 84.843 34.417 1.00 29.23 C ANISOU 244 C HIS D 34 3598 3558 3951 -54 -117 -34 C ATOM 245 O HIS A 34 88.731 83.944 34.944 1.00 25.94 O ANISOU 245 O HIS D 34 2680 3132 4044 -94 -152 82 O ATOM 246 CB HIS A 34 91.384 84.153 33.069 1.00 30.45 C ANISOU 246 CB HIS D 34 3880 3755 3935 -221 -33 1 C ATOM 247 CG HIS A 34 92.877 84.060 32.960 1.00 33.53 C ANISOU 247 CG HIS D 34 4130 4180 4430 -117 75 63 C ATOM 248 ND1 HIS A 34 93.615 83.115 33.642 1.00 37.51 N ANISOU 248 ND1 HIS D 34 4564 4581 5106 -90 -29 -38 N ATOM 249 CD2 HIS A 34 93.774 84.830 32.294 1.00 36.24 C ANISOU 249 CD2 HIS D 34 4453 4805 4510 -18 -206 -179 C ATOM 250 CE1 HIS A 34 94.897 83.294 33.388 1.00 40.36 C ANISOU 250 CE1 HIS D 34 4633 5106 5593 125 -85 -146 C ATOM 251 NE2 HIS A 34 95.022 84.328 32.574 1.00 40.29 N ANISOU 251 NE2 HIS D 34 4626 5344 5338 -25 -174 -298 N ATOM 252 N LYS A 35 88.835 85.909 33.837 1.00 29.52 N ANISOU 252 N LYS D 35 3602 3577 4034 -60 -59 -64 N ATOM 253 CA LYS A 35 87.399 86.133 33.724 1.00 29.17 C ANISOU 253 CA LYS D 35 3600 3569 3911 -71 -62 -42 C ATOM 254 C LYS A 35 86.958 85.892 32.284 1.00 28.05 C ANISOU 254 C LYS D 35 3403 3349 3905 20 -32 -97 C ATOM 255 O LYS A 35 87.648 86.304 31.325 1.00 28.40 O ANISOU 255 O LYS D 35 3450 3246 4093 -81 -123 -118 O ATOM 256 CB LYS A 35 87.089 87.558 34.158 1.00 30.10 C ANISOU 256 CB LYS D 35 3640 3657 4139 -81 -80 -6 C ATOM 257 CG LYS A 35 85.663 87.834 34.482 1.00 31.74 C ANISOU 257 CG LYS D 35 3924 3805 4329 1 -72 22 C ATOM 258 CD LYS A 35 85.579 89.104 35.330 1.00 32.01 C ANISOU 258 CD LYS D 35 4084 3915 4161 -27 -53 132 C ATOM 259 CE LYS A 35 84.217 89.741 35.248 1.00 33.33 C ANISOU 259 CE LYS D 35 4117 3949 4594 136 -51 131 C ATOM 260 NZ LYS A 35 84.097 90.705 36.386 1.00 35.88 N ANISOU 260 NZ LYS D 35 4446 4619 4565 267 0 123 N ATOM 261 N PHE A 36 85.819 85.213 32.115 1.00 26.61 N ANISOU 261 N PHE D 36 3250 3093 3768 -24 -83 -156 N ATOM 262 CA PHE A 36 85.281 84.911 30.779 1.00 25.43 C ANISOU 262 CA PHE D 36 3095 3161 3405 26 -121 -102 C ATOM 263 C PHE A 36 83.825 85.354 30.640 1.00 24.25 C ANISOU 263 C PHE D 36 2963 3084 3164 18 -94 -72 C ATOM 264 O PHE A 36 83.117 85.535 31.630 1.00 23.85 O ANISOU 264 O PHE D 36 2706 3205 3150 15 -74 -327 O ATOM 265 CB PHE A 36 85.387 83.414 30.438 1.00 24.66 C ANISOU 265 CB PHE D 36 2726 3291 3351 129 -155 -56 C ATOM 266 CG PHE A 36 86.756 82.840 30.662 1.00 22.71 C ANISOU 266 CG PHE D 36 2596 2949 3081 -14 -24 19 C ATOM 267 CD1 PHE A 36 87.722 82.902 29.656 1.00 22.57 C ANISOU 267 CD1 PHE D 36 2882 3062 2632 -106 70 173 C ATOM 268 CD2 PHE A 36 87.101 82.279 31.886 1.00 26.06 C ANISOU 268 CD2 PHE D 36 3014 3563 3324 -84 -6 -189 C ATOM 269 CE1 PHE A 36 89.011 82.382 29.870 1.00 21.70 C ANISOU 269 CE1 PHE D 36 2851 2538 2853 96 -129 -134 C ATOM 270 CE2 PHE A 36 88.386 81.764 32.105 1.00 25.85 C ANISOU 270 CE2 PHE D 36 3211 3178 3432 63 -96 47 C ATOM 271 CZ PHE A 36 89.337 81.831 31.108 1.00 21.52 C ANISOU 271 CZ PHE D 36 2873 2580 2722 -148 128 118 C ATOM 272 N LYS A 37 83.411 85.518 29.391 1.00 23.98 N ANISOU 272 N LYS D 37 2979 3196 2933 -18 -132 -128 N ATOM 273 CA LYS A 37 82.115 86.073 29.021 1.00 25.63 C ANISOU 273 CA LYS D 37 3157 3306 3273 -38 -115 -89 C ATOM 274 C LYS A 37 80.947 85.206 29.501 1.00 26.44 C ANISOU 274 C LYS D 37 3213 3241 3592 -65 -148 -84 C ATOM 275 O LYS A 37 79.923 85.744 29.930 1.00 27.27 O ANISOU 275 O LYS D 37 3157 3227 3975 -131 -289 -158 O ATOM 276 CB LYS A 37 82.004 86.195 27.484 1.00 26.67 C ANISOU 276 CB LYS D 37 3287 3487 3358 -109 -22 109 C ATOM 277 CG LYS A 37 82.655 87.429 26.888 1.00 30.71 C ANISOU 277 CG LYS D 37 3974 3973 3720 -29 -6 4 C ATOM 278 CD LYS A 37 82.269 87.580 25.419 1.00 30.05 C ANISOU 278 CD LYS D 37 4101 3811 3503 -61 -97 -190 C ATOM 279 CE LYS A 37 82.361 89.014 24.918 1.00 35.61 C ANISOU 279 CE LYS D 37 4793 4052 4682 -91 -92 -157 C ATOM 280 NZ LYS A 37 83.646 89.358 24.211 1.00 35.65 N ANISOU 280 NZ LYS D 37 4429 4639 4475 126 -53 -80 N ATOM 281 N LEU A 38 81.120 83.883 29.394 1.00 25.70 N ANISOU 281 N LEU D 38 3136 3087 3539 -88 -120 -28 N ATOM 282 CA LEU A 38 80.055 82.881 29.619 1.00 23.24 C ANISOU 282 CA LEU D 38 2871 2919 3038 9 -146 -170 C ATOM 283 C LEU A 38 80.607 81.707 30.401 1.00 22.38 C ANISOU 283 C LEU D 38 2650 2770 3081 -5 -169 -151 C ATOM 284 O LEU A 38 81.780 81.392 30.257 1.00 21.96 O ANISOU 284 O LEU D 38 2498 2793 3052 -97 -101 -102 O ATOM 285 CB LEU A 38 79.530 82.309 28.285 1.00 23.43 C ANISOU 285 CB LEU D 38 2970 2848 3081 26 -206 -96 C ATOM 286 CG LEU A 38 78.663 83.166 27.376 1.00 27.26 C ANISOU 286 CG LEU D 38 3460 3593 3303 44 58 35 C ATOM 287 CD1 LEU A 38 78.422 82.487 26.011 1.00 25.79 C ANISOU 287 CD1 LEU D 38 3453 3242 3102 57 -84 -29 C ATOM 288 CD2 LEU A 38 77.323 83.527 28.038 1.00 31.40 C ANISOU 288 CD2 LEU D 38 3809 4034 4087 -6 -187 -65 C ATOM 289 N PRO A 39 79.748 81.023 31.196 1.00 20.68 N ANISOU 289 N PRO D 39 2563 2529 2765 45 -174 -164 N ATOM 290 CA PRO A 39 80.117 79.786 31.880 1.00 20.07 C ANISOU 290 CA PRO D 39 2489 2568 2569 65 -130 -150 C ATOM 291 C PRO A 39 79.967 78.525 31.012 1.00 19.54 C ANISOU 291 C PRO D 39 2575 2526 2323 3 -94 -202 C ATOM 292 O PRO A 39 79.475 77.513 31.468 1.00 18.70 O ANISOU 292 O PRO D 39 2909 2759 1434 -69 -398 -216 O ATOM 293 CB PRO A 39 79.149 79.762 33.035 1.00 18.66 C ANISOU 293 CB PRO D 39 2557 2110 2422 28 -142 -126 C ATOM 294 CG PRO A 39 77.892 80.278 32.405 1.00 20.68 C ANISOU 294 CG PRO D 39 2581 2497 2775 -71 -244 -156 C ATOM 295 CD PRO A 39 78.353 81.398 31.505 1.00 19.99 C ANISOU 295 CD PRO D 39 2624 2443 2526 32 -121 -191 C ATOM 296 N VAL A 40 80.360 78.601 29.744 1.00 19.48 N ANISOU 296 N VAL D 40 2381 2660 2361 66 -277 -151 N ATOM 297 CA VAL A 40 80.316 77.473 28.820 1.00 22.19 C ANISOU 297 CA VAL D 40 2639 2860 2932 -33 -159 3 C ATOM 298 C VAL A 40 81.653 77.328 28.078 1.00 22.90 C ANISOU 298 C VAL D 40 2806 2929 2963 -81 -278 -18 C ATOM 299 O VAL A 40 82.392 78.312 27.875 1.00 22.54 O ANISOU 299 O VAL D 40 2787 3002 2772 -308 -208 -13 O ATOM 300 CB VAL A 40 79.238 77.595 27.683 1.00 21.82 C ANISOU 300 CB VAL D 40 2655 2861 2772 34 -93 -31 C ATOM 301 CG1 VAL A 40 77.791 77.790 28.255 1.00 20.29 C ANISOU 301 CG1 VAL D 40 2492 2832 2382 -59 65 10 C ATOM 302 CG2 VAL A 40 79.577 78.683 26.709 1.00 25.55 C ANISOU 302 CG2 VAL D 40 2878 3269 3559 -88 -374 -51 C ATOM 303 N VAL A 41 81.911 76.101 27.651 1.00 21.66 N ANISOU 303 N VAL D 41 2811 2787 2631 -24 -276 -23 N ATOM 304 CA VAL A 41 83.147 75.750 26.969 1.00 22.73 C ANISOU 304 CA VAL D 41 2847 2771 3015 -21 -192 -101 C ATOM 305 C VAL A 41 82.870 74.589 26.009 1.00 23.17 C ANISOU 305 C VAL D 41 2897 2931 2973 -29 -105 -83 C ATOM 306 O VAL A 41 82.198 73.593 26.363 1.00 22.40 O ANISOU 306 O VAL D 41 2776 2742 2991 -40 -284 -162 O ATOM 307 CB VAL A 41 84.303 75.433 27.969 1.00 21.52 C ANISOU 307 CB VAL D 41 2780 2596 2801 -70 -235 43 C ATOM 308 CG1 VAL A 41 83.982 74.241 28.853 1.00 20.31 C ANISOU 308 CG1 VAL D 41 2754 2730 2230 -13 -186 151 C ATOM 309 CG2 VAL A 41 85.645 75.223 27.211 1.00 17.92 C ANISOU 309 CG2 VAL D 41 2765 2752 1289 -9 -156 -17 C ATOM 310 N PRO A 42 83.375 74.701 24.779 1.00 23.74 N ANISOU 310 N PRO D 42 2962 2959 3097 -32 -68 -127 N ATOM 311 CA PRO A 42 83.221 73.614 23.841 1.00 24.45 C ANISOU 311 CA PRO D 42 3043 3090 3157 2 -110 -72 C ATOM 312 C PRO A 42 83.964 72.369 24.278 1.00 23.12 C ANISOU 312 C PRO D 42 2882 3028 2874 38 -169 -66 C ATOM 313 O PRO A 42 85.005 72.469 24.956 1.00 24.66 O ANISOU 313 O PRO D 42 3029 3377 2960 -54 -256 -224 O ATOM 314 CB PRO A 42 83.837 74.168 22.560 1.00 25.85 C ANISOU 314 CB PRO D 42 3258 3210 3352 89 -58 -195 C ATOM 315 CG PRO A 42 83.864 75.623 22.759 1.00 26.54 C ANISOU 315 CG PRO D 42 3502 3206 3373 -133 -50 14 C ATOM 316 CD PRO A 42 84.070 75.850 24.174 1.00 23.96 C ANISOU 316 CD PRO D 42 2775 3157 3170 -66 -140 -232 C ATOM 317 N ALA A 43 83.426 71.216 23.901 1.00 22.26 N ANISOU 317 N ALA D 43 2731 2917 2807 -26 -373 -79 N ATOM 318 CA ALA A 43 84.092 69.931 24.159 1.00 22.76 C ANISOU 318 CA ALA D 43 2841 2997 2808 37 -212 -92 C ATOM 319 C ALA A 43 85.498 69.953 23.573 1.00 23.09 C ANISOU 319 C ALA D 43 2904 3047 2822 95 -186 -142 C ATOM 320 O ALA A 43 85.697 70.388 22.405 1.00 21.48 O ANISOU 320 O ALA D 43 2806 3253 2099 235 -587 102 O ATOM 321 CB ALA A 43 83.289 68.775 23.528 1.00 21.74 C ANISOU 321 CB ALA D 43 2871 2906 2483 36 -401 -70 C ATOM 322 N ASN A 44 86.461 69.458 24.355 1.00 23.92 N ANISOU 322 N ASN D 44 3073 3228 2785 21 -173 103 N ATOM 323 CA ASN A 44 87.854 69.404 23.908 1.00 25.11 C ANISOU 323 CA ASN D 44 2997 3244 3299 -44 -141 -47 C ATOM 324 C ASN A 44 88.123 68.190 23.006 1.00 26.01 C ANISOU 324 C ASN D 44 3082 3340 3460 -43 -260 -9 C ATOM 325 O ASN A 44 88.877 67.291 23.372 1.00 28.08 O ANISOU 325 O ASN D 44 3368 3542 3758 -78 -191 -146 O ATOM 326 CB ASN A 44 88.822 69.484 25.084 1.00 24.17 C ANISOU 326 CB ASN D 44 2969 3099 3115 -11 -192 -101 C ATOM 327 CG ASN A 44 88.607 68.403 26.133 1.00 22.54 C ANISOU 327 CG ASN D 44 2554 3042 2966 -49 23 -243 C ATOM 328 OD1 ASN A 44 87.473 68.057 26.499 1.00 22.60 O ANISOU 328 OD1 ASN D 44 2787 3071 2729 47 -182 -347 O ATOM 329 ND2 ASN A 44 89.707 67.869 26.631 1.00 20.57 N ANISOU 329 ND2 ASN D 44 2744 2594 2478 -102 -221 -265 N ATOM 330 N MET A 45 87.483 68.189 21.840 1.00 27.55 N ANISOU 330 N MET D 45 3312 3592 3563 -30 -135 0 N ATOM 331 CA MET A 45 87.582 67.108 20.832 1.00 31.30 C ANISOU 331 CA MET D 45 3993 4012 3888 -3 -94 127 C ATOM 332 C MET A 45 87.766 67.703 19.451 1.00 31.35 C ANISOU 332 C MET D 45 4027 4038 3845 4 -45 59 C ATOM 333 O MET A 45 87.231 68.780 19.164 1.00 28.93 O ANISOU 333 O MET D 45 3627 4113 3252 242 -209 145 O ATOM 334 CB MET A 45 86.303 66.280 20.742 1.00 32.34 C ANISOU 334 CB MET D 45 4145 4146 3993 21 -72 204 C ATOM 335 CG MET A 45 85.807 65.708 22.014 1.00 34.33 C ANISOU 335 CG MET D 45 4484 4333 4224 -102 4 -2 C ATOM 336 SD MET A 45 84.062 65.233 21.880 1.00 37.65 S ANISOU 336 SD MET D 45 4812 4964 4526 -379 -206 154 S ATOM 337 CE MET A 45 84.071 63.898 23.074 1.00 38.65 C ANISOU 337 CE MET D 45 4891 4871 4922 -79 -28 -98 C ATOM 338 N GLN A 46 88.463 66.962 18.582 1.00 32.96 N ANISOU 338 N GLN D 46 4258 4224 4040 66 -144 69 N ATOM 339 CA GLN A 46 88.788 67.464 17.244 1.00 35.26 C ANISOU 339 CA GLN D 46 4529 4521 4345 40 -112 36 C ATOM 340 C GLN A 46 87.590 67.614 16.291 1.00 34.37 C ANISOU 340 C GLN D 46 4402 4336 4320 68 -149 110 C ATOM 341 O GLN A 46 87.665 68.332 15.301 1.00 34.24 O ANISOU 341 O GLN D 46 4502 4398 4109 163 -227 196 O ATOM 342 CB GLN A 46 89.916 66.643 16.590 1.00 36.32 C ANISOU 342 CB GLN D 46 4637 4670 4490 91 -105 43 C ATOM 343 CG GLN A 46 89.579 65.210 16.271 1.00 39.86 C ANISOU 343 CG GLN D 46 5167 4930 5048 0 -127 147 C ATOM 344 CD GLN A 46 90.383 64.651 15.080 1.00 41.11 C ANISOU 344 CD GLN D 46 5278 5234 5108 129 -149 220 C ATOM 345 OE1 GLN A 46 90.969 65.408 14.274 1.00 50.04 O ANISOU 345 OE1 GLN D 46 6472 6268 6273 -250 -214 -147 O ATOM 346 NE2 GLN A 46 90.402 63.320 14.962 1.00 45.68 N ANISOU 346 NE2 GLN D 46 5924 5411 6019 -29 -164 54 N ATOM 347 N THR A 47 86.494 66.937 16.600 1.00 34.53 N ANISOU 347 N THR D 47 4382 4296 4440 68 -155 137 N ATOM 348 CA THR A 47 85.238 67.113 15.883 1.00 34.61 C ANISOU 348 CA THR D 47 4469 4409 4272 19 -71 102 C ATOM 349 C THR A 47 84.492 68.412 16.255 1.00 34.95 C ANISOU 349 C THR D 47 4382 4477 4420 25 6 36 C ATOM 350 O THR A 47 83.519 68.771 15.596 1.00 36.52 O ANISOU 350 O THR D 47 4425 4730 4718 49 -27 10 O ATOM 351 CB THR A 47 84.314 65.915 16.163 1.00 36.26 C ANISOU 351 CB THR D 47 4620 4661 4496 -8 9 148 C ATOM 352 OG1 THR A 47 84.163 65.725 17.582 1.00 40.02 O ANISOU 352 OG1 THR D 47 5124 5188 4895 -76 -150 -81 O ATOM 353 CG2 THR A 47 84.895 64.656 15.565 1.00 36.90 C ANISOU 353 CG2 THR D 47 4619 4605 4792 36 52 102 C ATOM 354 N ILE A 48 84.954 69.111 17.298 1.00 33.48 N ANISOU 354 N ILE D 48 4110 4324 4287 36 -96 57 N ATOM 355 CA ILE A 48 84.275 70.307 17.835 1.00 32.37 C ANISOU 355 CA ILE D 48 4087 4161 4049 -31 -67 42 C ATOM 356 C ILE A 48 85.162 71.558 17.800 1.00 31.72 C ANISOU 356 C ILE D 48 4021 4194 3834 61 -134 -58 C ATOM 357 O ILE A 48 84.716 72.630 17.412 1.00 32.06 O ANISOU 357 O ILE D 48 4110 4276 3795 111 -334 -12 O ATOM 358 CB ILE A 48 83.795 69.998 19.293 1.00 31.99 C ANISOU 358 CB ILE D 48 4034 4082 4037 -60 7 51 C ATOM 359 CG1 ILE A 48 82.871 68.769 19.308 1.00 30.18 C ANISOU 359 CG1 ILE D 48 3876 4073 3515 -73 -128 -40 C ATOM 360 CG2 ILE A 48 83.126 71.202 19.962 1.00 31.94 C ANISOU 360 CG2 ILE D 48 3913 4133 4087 -54 -25 25 C ATOM 361 CD1 ILE A 48 81.561 68.936 18.556 1.00 32.09 C ANISOU 361 CD1 ILE D 48 3837 4315 4041 117 -84 -12 C ATOM 362 N ILE A 49 86.412 71.440 18.221 1.00 31.82 N ANISOU 362 N ILE D 49 4018 4206 3864 19 -200 -14 N ATOM 363 CA ILE A 49 87.308 72.593 18.274 1.00 31.51 C ANISOU 363 CA ILE D 49 3992 4055 3923 17 -108 17 C ATOM 364 C ILE A 49 88.570 72.394 17.426 1.00 32.10 C ANISOU 364 C ILE D 49 4163 4122 3909 6 -191 12 C ATOM 365 O ILE A 49 89.020 71.274 17.214 1.00 30.63 O ANISOU 365 O ILE D 49 4077 4021 3540 21 -367 7 O ATOM 366 CB ILE A 49 87.691 72.975 19.744 1.00 30.79 C ANISOU 366 CB ILE D 49 3806 3902 3988 97 -116 -24 C ATOM 367 CG1 ILE A 49 88.485 74.291 19.773 1.00 30.63 C ANISOU 367 CG1 ILE D 49 3723 3934 3979 -36 -23 120 C ATOM 368 CG2 ILE A 49 88.423 71.822 20.495 1.00 27.62 C ANISOU 368 CG2 ILE D 49 3616 3582 3297 71 -92 -27 C ATOM 369 CD1 ILE A 49 88.424 74.990 21.067 1.00 30.08 C ANISOU 369 CD1 ILE D 49 3633 4043 3751 -1 -124 24 C ATOM 370 N ASP A 50 89.109 73.508 16.935 1.00 32.74 N ANISOU 370 N ASP D 50 4264 4233 3939 -48 -178 -45 N ATOM 371 CA ASP A 50 90.404 73.513 16.265 1.00 33.96 C ANISOU 371 CA ASP D 50 4281 4382 4240 -32 -121 -13 C ATOM 372 C ASP A 50 91.137 74.818 16.574 1.00 35.00 C ANISOU 372 C ASP D 50 4434 4494 4368 -65 -144 16 C ATOM 373 O ASP A 50 90.653 75.635 17.357 1.00 34.16 O ANISOU 373 O ASP D 50 4417 4618 3942 -42 -233 -117 O ATOM 374 CB ASP A 50 90.240 73.272 14.742 1.00 33.98 C ANISOU 374 CB ASP D 50 4366 4427 4116 -36 -128 37 C ATOM 375 CG ASP A 50 89.488 74.400 14.007 1.00 36.10 C ANISOU 375 CG ASP D 50 4455 4663 4597 -80 -94 20 C ATOM 376 OD1 ASP A 50 89.333 75.528 14.524 1.00 38.58 O ANISOU 376 OD1 ASP D 50 5079 4889 4688 64 -464 122 O ATOM 377 OD2 ASP A 50 89.063 74.154 12.859 1.00 39.10 O ANISOU 377 OD2 ASP D 50 4963 5237 4656 109 -116 26 O ATOM 378 N GLU A 51 92.287 75.038 15.937 1.00 35.35 N ANISOU 378 N GLU D 51 4387 4568 4476 -3 -185 50 N ATOM 379 CA GLU A 51 93.093 76.219 16.240 1.00 34.69 C ANISOU 379 CA GLU D 51 4339 4439 4402 -24 -140 -4 C ATOM 380 C GLU A 51 92.432 77.541 15.858 1.00 34.27 C ANISOU 380 C GLU D 51 4299 4421 4298 -79 -195 -22 C ATOM 381 O GLU A 51 92.601 78.521 16.575 1.00 33.38 O ANISOU 381 O GLU D 51 4374 4189 4119 -29 -448 22 O ATOM 382 CB GLU A 51 94.475 76.128 15.597 1.00 36.41 C ANISOU 382 CB GLU D 51 4538 4628 4667 -26 -112 30 C ATOM 383 CG GLU A 51 95.311 74.951 16.098 1.00 38.32 C ANISOU 383 CG GLU D 51 4789 4841 4927 62 -128 -206 C ATOM 384 CD GLU A 51 95.024 73.644 15.348 1.00 43.48 C ANISOU 384 CD GLU D 51 5607 5550 5361 -129 -91 141 C ATOM 385 OE1 GLU A 51 94.026 73.576 14.589 1.00 44.68 O ANISOU 385 OE1 GLU D 51 5458 5967 5551 84 -232 81 O ATOM 386 OE2 GLU A 51 95.801 72.675 15.541 1.00 50.08 O ANISOU 386 OE2 GLU D 51 6205 6238 6584 109 -298 -3 O ATOM 387 N ARG A 52 91.722 77.582 14.726 1.00 34.21 N ANISOU 387 N ARG D 52 4167 4431 4397 -17 -174 -25 N ATOM 388 CA ARG A 52 91.017 78.808 14.316 1.00 33.98 C ANISOU 388 CA ARG D 52 4210 4365 4334 -38 -209 -31 C ATOM 389 C ARG A 52 89.903 79.134 15.320 1.00 32.52 C ANISOU 389 C ARG D 52 4159 4120 4077 -52 -269 33 C ATOM 390 O ARG A 52 89.755 80.277 15.736 1.00 33.21 O ANISOU 390 O ARG D 52 4225 4146 4245 -163 -512 32 O ATOM 391 CB ARG A 52 90.353 78.683 12.941 1.00 36.00 C ANISOU 391 CB ARG D 52 4576 4575 4525 -38 -33 23 C ATOM 392 CG ARG A 52 91.247 78.321 11.759 1.00 39.91 C ANISOU 392 CG ARG D 52 5064 5198 4901 -35 -234 29 C ATOM 393 CD ARG A 52 92.435 79.246 11.596 1.00 45.86 C ANISOU 393 CD ARG D 52 5680 5592 6152 -125 129 -11 C ATOM 394 NE ARG A 52 93.053 79.035 10.277 1.00 42.89 N ANISOU 394 NE ARG D 52 5340 5710 5244 -192 -349 20 N ATOM 395 CZ ARG A 52 94.322 79.286 9.966 1.00 45.82 C ANISOU 395 CZ ARG D 52 5677 5927 5804 -76 -70 -29 C ATOM 396 NH1 ARG A 52 95.167 79.769 10.878 1.00 45.14 N ANISOU 396 NH1 ARG D 52 5534 5767 5850 -2 -21 12 N ATOM 397 NH2 ARG A 52 94.742 79.040 8.718 1.00 46.94 N ANISOU 397 NH2 ARG D 52 5985 5840 6008 -114 -181 162 N ATOM 398 N ILE A 53 89.093 78.135 15.662 1.00 30.41 N ANISOU 398 N ILE D 53 3892 3912 3750 22 -141 8 N ATOM 399 CA ILE A 53 88.027 78.349 16.658 1.00 30.08 C ANISOU 399 CA ILE D 53 3789 3881 3758 -30 -74 -50 C ATOM 400 C ILE A 53 88.606 78.796 18.028 1.00 28.95 C ANISOU 400 C ILE D 53 3684 3767 3546 -74 -165 -81 C ATOM 401 O ILE A 53 88.096 79.747 18.633 1.00 30.52 O ANISOU 401 O ILE D 53 3701 3980 3913 -101 -274 -186 O ATOM 402 CB ILE A 53 87.096 77.126 16.788 1.00 30.01 C ANISOU 402 CB ILE D 53 3839 3827 3735 27 -3 -62 C ATOM 403 CG1 ILE A 53 86.300 76.936 15.492 1.00 29.50 C ANISOU 403 CG1 ILE D 53 3737 3938 3533 -184 -112 -32 C ATOM 404 CG2 ILE A 53 86.118 77.316 17.961 1.00 30.51 C ANISOU 404 CG2 ILE D 53 3814 3974 3802 12 -109 -48 C ATOM 405 CD1 ILE A 53 85.667 75.577 15.310 1.00 29.72 C ANISOU 405 CD1 ILE D 53 3984 3768 3539 -42 -120 -135 C ATOM 406 N ALA A 54 89.691 78.166 18.477 1.00 28.63 N ANISOU 406 N ALA D 54 3700 3762 3412 -59 -201 -111 N ATOM 407 CA ALA A 54 90.365 78.544 19.750 1.00 28.89 C ANISOU 407 CA ALA D 54 3672 3720 3585 -65 -113 -46 C ATOM 408 C ALA A 54 90.888 79.985 19.785 1.00 30.15 C ANISOU 408 C ALA D 54 3853 3853 3749 -67 -107 -43 C ATOM 409 O ALA A 54 90.858 80.677 20.843 1.00 28.38 O ANISOU 409 O ALA D 54 3398 3666 3716 -97 -225 -43 O ATOM 410 CB ALA A 54 91.501 77.562 20.051 1.00 28.55 C ANISOU 410 CB ALA D 54 3664 3769 3414 -66 -145 -80 C ATOM 411 N THR A 55 91.382 80.436 18.635 1.00 31.34 N ANISOU 411 N THR D 55 4017 3883 4006 -131 -143 -31 N ATOM 412 CA THR A 55 91.857 81.819 18.490 1.00 31.30 C ANISOU 412 CA THR D 55 4050 3854 3989 -57 -191 -87 C ATOM 413 C THR A 55 90.694 82.833 18.544 1.00 30.63 C ANISOU 413 C THR D 55 3985 3818 3832 -84 -255 -76 C ATOM 414 O THR A 55 90.792 83.864 19.211 1.00 29.55 O ANISOU 414 O THR D 55 3858 3660 3709 -46 -616 1 O ATOM 415 CB THR A 55 92.657 81.985 17.182 1.00 33.25 C ANISOU 415 CB THR D 55 4247 4072 4311 -37 -213 -50 C ATOM 416 OG1 THR A 55 93.710 81.000 17.133 1.00 34.95 O ANISOU 416 OG1 THR D 55 3972 4565 4740 25 -388 -241 O ATOM 417 CG2 THR A 55 93.255 83.382 17.112 1.00 31.57 C ANISOU 417 CG2 THR D 55 4118 3822 4054 -153 -177 -102 C ATOM 418 N TYR A 56 89.616 82.536 17.832 1.00 30.93 N ANISOU 418 N TYR D 56 4010 3908 3833 -53 -210 -138 N ATOM 419 CA TYR A 56 88.393 83.329 17.919 1.00 30.42 C ANISOU 419 CA TYR D 56 4024 3770 3762 -24 -159 -101 C ATOM 420 C TYR A 56 87.950 83.432 19.370 1.00 29.21 C ANISOU 420 C TYR D 56 3906 3524 3668 -71 -302 -246 C ATOM 421 O TYR A 56 87.644 84.514 19.871 1.00 29.04 O ANISOU 421 O TYR D 56 4159 3344 3528 -200 -516 -655 O ATOM 422 CB TYR A 56 87.251 82.727 17.102 1.00 33.53 C ANISOU 422 CB TYR D 56 4513 4118 4107 -281 -84 -183 C ATOM 423 CG TYR A 56 85.959 83.477 17.345 1.00 34.11 C ANISOU 423 CG TYR D 56 4180 4295 4484 54 -150 -186 C ATOM 424 CD1 TYR A 56 85.699 84.681 16.689 1.00 36.33 C ANISOU 424 CD1 TYR D 56 4491 4571 4741 71 -23 -203 C ATOM 425 CD2 TYR A 56 85.020 83.014 18.271 1.00 36.24 C ANISOU 425 CD2 TYR D 56 4523 4662 4584 99 -130 -313 C ATOM 426 CE1 TYR A 56 84.534 85.406 16.941 1.00 36.49 C ANISOU 426 CE1 TYR D 56 4467 4491 4905 124 -23 -216 C ATOM 427 CE2 TYR A 56 83.846 83.732 18.533 1.00 35.54 C ANISOU 427 CE2 TYR D 56 4255 4610 4638 114 -178 -247 C ATOM 428 CZ TYR A 56 83.608 84.927 17.850 1.00 37.86 C ANISOU 428 CZ TYR D 56 4576 4698 5111 270 -260 -182 C ATOM 429 OH TYR A 56 82.450 85.636 18.082 1.00 38.53 O ANISOU 429 OH TYR D 56 4576 4746 5314 370 -273 -317 O ATOM 430 N LEU A 57 87.909 82.295 20.050 1.00 28.11 N ANISOU 430 N LEU D 57 3681 3363 3633 68 -220 -176 N ATOM 431 CA LEU A 57 87.400 82.262 21.410 1.00 27.73 C ANISOU 431 CA LEU D 57 3612 3410 3511 40 -168 -86 C ATOM 432 C LEU A 57 88.260 83.077 22.348 1.00 26.59 C ANISOU 432 C LEU D 57 3371 3245 3486 -27 -245 -114 C ATOM 433 O LEU A 57 87.761 83.930 23.090 1.00 25.84 O ANISOU 433 O LEU D 57 2969 3226 3620 62 -594 -314 O ATOM 434 CB LEU A 57 87.228 80.791 21.901 1.00 25.88 C ANISOU 434 CB LEU D 57 3516 3245 3069 107 -139 -54 C ATOM 435 CG LEU A 57 86.071 80.067 21.194 1.00 27.97 C ANISOU 435 CG LEU D 57 3473 3353 3798 83 -190 -24 C ATOM 436 CD1 LEU A 57 86.007 78.602 21.566 1.00 29.10 C ANISOU 436 CD1 LEU D 57 3650 3643 3760 -30 -114 -229 C ATOM 437 CD2 LEU A 57 84.709 80.713 21.487 1.00 26.28 C ANISOU 437 CD2 LEU D 57 3143 3543 3298 31 26 -227 C ATOM 438 N ALA A 58 89.566 82.853 22.319 1.00 26.58 N ANISOU 438 N ALA D 58 3417 3302 3377 67 -223 -34 N ATOM 439 CA ALA A 58 90.458 83.560 23.236 1.00 28.30 C ANISOU 439 CA ALA D 58 3603 3550 3597 -8 -120 -17 C ATOM 440 C ALA A 58 90.485 85.066 22.950 1.00 28.89 C ANISOU 440 C ALA D 58 3624 3590 3760 -25 -108 -48 C ATOM 441 O ALA A 58 90.560 85.859 23.891 1.00 29.27 O ANISOU 441 O ALA D 58 3605 3403 4112 -60 -241 -126 O ATOM 442 CB ALA A 58 91.855 82.973 23.184 1.00 28.64 C ANISOU 442 CB ALA D 58 3645 3582 3655 -70 -17 -50 C ATOM 443 N GLU A 59 90.415 85.432 21.658 1.00 29.74 N ANISOU 443 N GLU D 59 3798 3610 3889 86 -61 -181 N ATOM 444 CA GLU A 59 90.384 86.849 21.210 1.00 30.77 C ANISOU 444 CA GLU D 59 3897 3834 3958 -2 -92 -74 C ATOM 445 C GLU A 59 89.168 87.631 21.680 1.00 32.50 C ANISOU 445 C GLU D 59 4101 3898 4348 51 -77 -72 C ATOM 446 O GLU A 59 89.186 88.857 21.708 1.00 33.99 O ANISOU 446 O GLU D 59 4375 3973 4565 -12 -89 -115 O ATOM 447 CB GLU A 59 90.407 86.916 19.694 1.00 28.51 C ANISOU 447 CB GLU D 59 3653 3497 3682 39 1 -173 C ATOM 448 CG GLU A 59 91.793 86.753 19.133 1.00 30.49 C ANISOU 448 CG GLU D 59 3895 4068 3622 -58 -103 16 C ATOM 449 CD GLU A 59 91.837 86.894 17.621 1.00 33.91 C ANISOU 449 CD GLU D 59 4401 4503 3980 57 -79 -61 C ATOM 450 OE1 GLU A 59 90.759 86.879 16.979 1.00 37.37 O ANISOU 450 OE1 GLU D 59 4454 5044 4700 -18 -8 -1 O ATOM 451 OE2 GLU A 59 92.973 87.020 17.088 1.00 38.10 O ANISOU 451 OE2 GLU D 59 4691 5104 4679 -126 -336 -71 O ATOM 452 N ASN A 60 88.125 86.908 22.059 1.00 32.80 N ANISOU 452 N ASN D 60 3982 4036 4442 7 -64 -28 N ATOM 453 CA ASN A 60 86.871 87.499 22.496 1.00 31.56 C ANISOU 453 CA ASN D 60 3973 3895 4122 -1 -72 -32 C ATOM 454 C ASN A 60 86.499 87.143 23.937 1.00 31.28 C ANISOU 454 C ASN D 60 3872 3864 4149 -40 -100 -93 C ATOM 455 O ASN A 60 85.366 87.362 24.342 1.00 32.51 O ANISOU 455 O ASN D 60 3974 3917 4461 83 -207 -198 O ATOM 456 CB ASN A 60 85.790 87.069 21.509 1.00 32.37 C ANISOU 456 CB ASN D 60 4016 4017 4262 82 -18 31 C ATOM 457 CG ASN A 60 85.899 87.801 20.196 1.00 35.29 C ANISOU 457 CG ASN D 60 4846 4236 4324 6 -162 9 C ATOM 458 OD1 ASN A 60 85.653 89.003 20.152 1.00 36.51 O ANISOU 458 OD1 ASN D 60 5268 4245 4360 181 -96 -311 O ATOM 459 ND2 ASN A 60 86.274 87.090 19.113 1.00 34.92 N ANISOU 459 ND2 ASN D 60 4804 4193 4268 -7 -278 -10 N ATOM 460 N ASN A 61 87.466 86.630 24.701 1.00 29.85 N ANISOU 460 N ASN D 61 3707 3623 4009 -127 -140 -106 N ATOM 461 CA ASN A 61 87.318 86.351 26.132 1.00 29.93 C ANISOU 461 CA ASN D 61 3760 3637 3975 -92 -34 -64 C ATOM 462 C ASN A 61 86.306 85.247 26.506 1.00 28.91 C ANISOU 462 C ASN D 61 3627 3489 3866 -147 -94 -50 C ATOM 463 O ASN A 61 85.687 85.306 27.589 1.00 29.08 O ANISOU 463 O ASN D 61 3688 3213 4148 -71 -172 -53 O ATOM 464 CB ASN A 61 87.007 87.622 26.933 1.00 30.98 C ANISOU 464 CB ASN D 61 3962 3760 4047 -14 -63 -52 C ATOM 465 CG ASN A 61 88.118 88.631 26.866 1.00 37.23 C ANISOU 465 CG ASN D 61 4661 4496 4986 -233 23 -60 C ATOM 466 OD1 ASN A 61 87.970 89.677 26.236 1.00 41.92 O ANISOU 466 OD1 ASN D 61 5637 4889 5400 -127 -257 -254 O ATOM 467 ND2 ASN A 61 89.240 88.331 27.512 1.00 41.19 N ANISOU 467 ND2 ASN D 61 4889 5132 5627 -94 69 -218 N ATOM 468 N TYR A 62 86.189 84.260 25.616 1.00 26.98 N ANISOU 468 N TYR D 62 3335 3340 3576 -66 -107 -65 N ATOM 469 CA TYR A 62 85.458 82.998 25.849 1.00 25.88 C ANISOU 469 CA TYR D 62 3280 3250 3301 35 -48 -168 C ATOM 470 C TYR A 62 86.498 81.940 26.244 1.00 26.08 C ANISOU 470 C TYR D 62 3375 3073 3459 58 -151 -154 C ATOM 471 O TYR A 62 87.614 81.954 25.736 1.00 26.21 O ANISOU 471 O TYR D 62 3468 2647 3843 41 -288 -275 O ATOM 472 CB TYR A 62 84.729 82.534 24.583 1.00 25.91 C ANISOU 472 CB TYR D 62 3157 3294 3393 -49 -84 -157 C ATOM 473 CG TYR A 62 83.619 83.451 24.103 1.00 25.63 C ANISOU 473 CG TYR D 62 3230 3242 3263 146 -123 -178 C ATOM 474 CD1 TYR A 62 82.399 83.483 24.759 1.00 27.86 C ANISOU 474 CD1 TYR D 62 3266 3496 3821 21 -69 -345 C ATOM 475 CD2 TYR A 62 83.792 84.269 22.971 1.00 26.71 C ANISOU 475 CD2 TYR D 62 3066 3469 3612 -34 -41 -186 C ATOM 476 CE1 TYR A 62 81.355 84.327 24.327 1.00 27.83 C ANISOU 476 CE1 TYR D 62 3325 3573 3677 177 -196 -254 C ATOM 477 CE2 TYR A 62 82.766 85.104 22.519 1.00 27.06 C ANISOU 477 CE2 TYR D 62 3370 3360 3549 99 -200 -282 C ATOM 478 CZ TYR A 62 81.533 85.123 23.206 1.00 28.64 C ANISOU 478 CZ TYR D 62 3286 3798 3796 217 -178 -367 C ATOM 479 OH TYR A 62 80.499 85.957 22.801 1.00 25.69 O ANISOU 479 OH TYR D 62 3080 3554 3126 -120 -343 -530 O ATOM 480 N PHE A 63 86.158 81.091 27.216 1.00 25.34 N ANISOU 480 N PHE D 63 3212 3097 3319 -13 -128 -248 N ATOM 481 CA PHE A 63 87.023 79.966 27.621 1.00 23.84 C ANISOU 481 CA PHE D 63 2998 3054 3006 32 -83 -122 C ATOM 482 C PHE A 63 87.060 78.907 26.510 1.00 21.87 C ANISOU 482 C PHE D 63 2790 2817 2700 10 -33 -264 C ATOM 483 O PHE A 63 86.078 78.681 25.856 1.00 20.69 O ANISOU 483 O PHE D 63 2811 2776 2274 -20 -240 -52 O ATOM 484 CB PHE A 63 86.527 79.395 28.980 1.00 24.20 C ANISOU 484 CB PHE D 63 2962 2941 3291 46 -12 -229 C ATOM 485 CG PHE A 63 87.430 78.363 29.610 1.00 24.62 C ANISOU 485 CG PHE D 63 3193 3136 3024 -98 -130 -218 C ATOM 486 CD1 PHE A 63 88.805 78.565 29.744 1.00 25.59 C ANISOU 486 CD1 PHE D 63 3453 3305 2964 -144 85 -117 C ATOM 487 CD2 PHE A 63 86.899 77.183 30.104 1.00 22.42 C ANISOU 487 CD2 PHE D 63 2749 2736 3032 -325 117 205 C ATOM 488 CE1 PHE A 63 89.618 77.614 30.301 1.00 24.21 C ANISOU 488 CE1 PHE D 63 3006 2930 3261 11 -186 89 C ATOM 489 CE2 PHE A 63 87.707 76.234 30.707 1.00 22.70 C ANISOU 489 CE2 PHE D 63 3001 2915 2709 -97 -65 35 C ATOM 490 CZ PHE A 63 89.067 76.451 30.814 1.00 25.05 C ANISOU 490 CZ PHE D 63 3140 3176 3199 52 35 41 C ATOM 491 N TYR A 64 88.225 78.305 26.269 1.00 21.51 N ANISOU 491 N TYR D 64 2678 2882 2611 -6 -125 -214 N ATOM 492 CA TYR A 64 88.330 77.133 25.416 1.00 22.04 C ANISOU 492 CA TYR D 64 2767 2849 2757 30 -110 -195 C ATOM 493 C TYR A 64 89.337 76.167 26.052 1.00 22.21 C ANISOU 493 C TYR D 64 2715 2807 2915 -22 -161 -130 C ATOM 494 O TYR A 64 90.109 76.525 26.937 1.00 23.42 O ANISOU 494 O TYR D 64 2551 2924 3422 138 -160 -247 O ATOM 495 CB TYR A 64 88.797 77.514 23.989 1.00 22.19 C ANISOU 495 CB TYR D 64 2840 2832 2756 49 -160 -267 C ATOM 496 CG TYR A 64 90.293 77.771 23.954 1.00 21.80 C ANISOU 496 CG TYR D 64 2836 2732 2714 50 22 -371 C ATOM 497 CD1 TYR A 64 91.200 76.727 23.751 1.00 23.83 C ANISOU 497 CD1 TYR D 64 3088 2996 2969 83 -351 -79 C ATOM 498 CD2 TYR A 64 90.804 79.025 24.206 1.00 18.46 C ANISOU 498 CD2 TYR D 64 2695 2984 1333 -57 -300 222 C ATOM 499 CE1 TYR A 64 92.567 76.945 23.794 1.00 22.66 C ANISOU 499 CE1 TYR D 64 2859 2910 2837 -30 -49 -112 C ATOM 500 CE2 TYR A 64 92.181 79.251 24.267 1.00 22.01 C ANISOU 500 CE2 TYR D 64 2708 2963 2689 15 -124 152 C ATOM 501 CZ TYR A 64 93.050 78.214 24.042 1.00 24.05 C ANISOU 501 CZ TYR D 64 2940 3046 3153 39 -73 -26 C ATOM 502 OH TYR A 64 94.402 78.454 24.083 1.00 25.50 O ANISOU 502 OH TYR D 64 2849 3120 3717 -36 -117 -32 O ATOM 503 N ILE A 65 89.281 74.926 25.613 1.00 22.93 N ANISOU 503 N ILE D 65 2708 2931 3070 -75 -200 -162 N ATOM 504 CA ILE A 65 90.278 73.904 25.947 1.00 23.30 C ANISOU 504 CA ILE D 65 2792 2917 3142 -22 -154 -201 C ATOM 505 C ILE A 65 90.530 73.168 24.646 1.00 22.60 C ANISOU 505 C ILE D 65 2805 2920 2863 -24 -127 -233 C ATOM 506 O ILE A 65 89.640 72.537 24.072 1.00 21.33 O ANISOU 506 O ILE D 65 2496 2716 2892 -105 -627 -551 O ATOM 507 CB ILE A 65 89.786 72.859 26.981 1.00 22.34 C ANISOU 507 CB ILE D 65 2919 2851 2715 -7 -48 -196 C ATOM 508 CG1 ILE A 65 89.451 73.498 28.330 1.00 22.56 C ANISOU 508 CG1 ILE D 65 2814 2790 2965 -4 -262 -134 C ATOM 509 CG2 ILE A 65 90.781 71.720 27.093 1.00 19.24 C ANISOU 509 CG2 ILE D 65 2116 2684 2508 -417 -82 -136 C ATOM 510 CD1 ILE A 65 88.646 72.554 29.269 1.00 23.07 C ANISOU 510 CD1 ILE D 65 2764 2720 3281 105 -160 -232 C ATOM 511 N MET A 66 91.767 73.239 24.180 1.00 25.28 N ANISOU 511 N MET D 66 3060 3247 3297 -29 -77 -106 N ATOM 512 CA MET A 66 92.146 72.582 22.955 1.00 26.26 C ANISOU 512 CA MET D 66 3171 3386 3422 15 -131 -63 C ATOM 513 C MET A 66 92.252 71.078 23.182 1.00 26.30 C ANISOU 513 C MET D 66 3052 3425 3513 -43 -151 -9 C ATOM 514 O MET A 66 92.585 70.625 24.286 1.00 25.42 O ANISOU 514 O MET D 66 2985 3174 3499 33 -398 -11 O ATOM 515 CB MET A 66 93.485 73.157 22.487 1.00 28.00 C ANISOU 515 CB MET D 66 3301 3513 3822 -60 -99 -40 C ATOM 516 CG MET A 66 93.851 72.836 21.088 1.00 34.01 C ANISOU 516 CG MET D 66 4042 4446 4431 -136 -226 63 C ATOM 517 SD MET A 66 92.637 73.124 19.825 1.00 31.20 S ANISOU 517 SD MET D 66 3133 4118 4603 503 -1120 -662 S ATOM 518 CE MET A 66 93.528 72.359 18.492 1.00 33.42 C ANISOU 518 CE MET D 66 4416 4046 4235 37 -313 72 C ATOM 519 N HIS A 67 91.962 70.324 22.128 1.00 27.19 N ANISOU 519 N HIS D 67 3256 3583 3491 3 -267 54 N ATOM 520 CA HIS A 67 92.126 68.869 22.112 1.00 28.82 C ANISOU 520 CA HIS D 67 3563 3642 3742 37 -178 -27 C ATOM 521 C HIS A 67 93.617 68.463 21.926 1.00 29.47 C ANISOU 521 C HIS D 67 3628 3746 3824 100 -171 6 C ATOM 522 O HIS A 67 94.482 69.303 21.578 1.00 28.38 O ANISOU 522 O HIS D 67 3441 3720 3622 277 -371 68 O ATOM 523 CB HIS A 67 91.272 68.252 20.983 1.00 29.63 C ANISOU 523 CB HIS D 67 3509 3703 4046 43 -67 -64 C ATOM 524 CG HIS A 67 91.723 68.631 19.599 1.00 33.72 C ANISOU 524 CG HIS D 67 4323 4371 4117 124 -71 84 C ATOM 525 ND1 HIS A 67 92.848 68.100 19.003 1.00 34.11 N ANISOU 525 ND1 HIS D 67 4297 4391 4272 131 -108 154 N ATOM 526 CD2 HIS A 67 91.218 69.518 18.711 1.00 34.59 C ANISOU 526 CD2 HIS D 67 4237 4470 4433 143 -102 -58 C ATOM 527 CE1 HIS A 67 93.006 68.634 17.806 1.00 32.70 C ANISOU 527 CE1 HIS D 67 4199 4053 4172 8 -145 72 C ATOM 528 NE2 HIS A 67 92.025 69.493 17.601 1.00 33.87 N ANISOU 528 NE2 HIS D 67 4275 4275 4319 51 -194 102 N ATOM 529 N ARG A 68 93.898 67.176 22.145 1.00 29.79 N ANISOU 529 N ARG D 68 3785 3828 3704 74 -194 7 N ATOM 530 CA ARG A 68 95.265 66.652 22.029 1.00 31.53 C ANISOU 530 CA ARG D 68 3912 3969 4096 65 -145 -75 C ATOM 531 C ARG A 68 95.391 65.592 20.924 1.00 32.34 C ANISOU 531 C ARG D 68 4058 4039 4189 -58 -268 -150 C ATOM 532 O ARG A 68 96.207 64.670 21.021 1.00 32.72 O ANISOU 532 O ARG D 68 4341 3914 4176 -26 -448 -219 O ATOM 533 CB ARG A 68 95.732 66.097 23.371 1.00 31.82 C ANISOU 533 CB ARG D 68 3919 3921 4250 26 -3 9 C ATOM 534 CG ARG A 68 94.814 65.038 23.957 1.00 30.98 C ANISOU 534 CG ARG D 68 3827 3799 4143 225 -256 -18 C ATOM 535 CD ARG A 68 95.424 64.472 25.167 1.00 31.63 C ANISOU 535 CD ARG D 68 3921 4104 3992 162 -89 51 C ATOM 536 NE ARG A 68 94.542 63.547 25.876 1.00 34.80 N ANISOU 536 NE ARG D 68 4274 4355 4594 115 -201 -99 N ATOM 537 CZ ARG A 68 94.734 62.234 26.031 1.00 34.62 C ANISOU 537 CZ ARG D 68 4235 4310 4609 -70 -102 101 C ATOM 538 NH1 ARG A 68 95.791 61.601 25.529 1.00 32.39 N ANISOU 538 NH1 ARG D 68 4089 3917 4299 0 11 145 N ATOM 539 NH2 ARG A 68 93.851 61.542 26.735 1.00 34.59 N ANISOU 539 NH2 ARG D 68 4400 4467 4274 -155 -135 -34 N ATOM 540 N PHE A 69 94.620 65.735 19.861 1.00 35.02 N ANISOU 540 N PHE D 69 4347 4462 4494 -65 -170 -93 N ATOM 541 CA PHE A 69 94.691 64.795 18.754 1.00 35.93 C ANISOU 541 CA PHE D 69 4552 4515 4582 -30 -97 26 C ATOM 542 C PHE A 69 96.009 64.892 17.972 1.00 38.37 C ANISOU 542 C PHE D 69 4792 4801 4985 -37 -144 17 C ATOM 543 O PHE A 69 96.488 63.893 17.419 1.00 40.91 O ANISOU 543 O PHE D 69 5137 5159 5246 68 -213 131 O ATOM 544 CB PHE A 69 93.532 64.995 17.793 1.00 41.27 C ANISOU 544 CB PHE D 69 4854 5408 5416 140 -116 -565 C ATOM 545 CG PHE A 69 93.405 63.888 16.782 1.00 37.85 C ANISOU 545 CG PHE D 69 4923 4761 4694 -141 -40 128 C ATOM 546 CD1 PHE A 69 92.881 62.647 17.157 1.00 42.48 C ANISOU 546 CD1 PHE D 69 5722 5213 5202 -106 -24 -52 C ATOM 547 CD2 PHE A 69 93.822 64.068 15.464 1.00 43.04 C ANISOU 547 CD2 PHE D 69 5534 5511 5306 -163 -101 54 C ATOM 548 CE1 PHE A 69 92.771 61.605 16.228 1.00 42.28 C ANISOU 548 CE1 PHE D 69 5690 5043 5330 -179 17 184 C ATOM 549 CE2 PHE A 69 93.723 63.029 14.533 1.00 41.52 C ANISOU 549 CE2 PHE D 69 5605 5178 4993 -29 -22 259 C ATOM 550 CZ PHE A 69 93.188 61.801 14.917 1.00 41.49 C ANISOU 550 CZ PHE D 69 5452 5086 5224 -41 -37 195 C ATOM 551 N GLN A 70 96.599 66.082 17.929 1.00 37.65 N ANISOU 551 N GLN D 70 4670 4757 4877 -42 -111 -86 N ATOM 552 CA GLN A 70 97.914 66.245 17.286 1.00 36.65 C ANISOU 552 CA GLN D 70 4599 4705 4620 8 -106 -22 C ATOM 553 C GLN A 70 98.906 66.742 18.296 1.00 34.75 C ANISOU 553 C GLN D 70 4314 4399 4488 17 -247 -45 C ATOM 554 O GLN A 70 99.336 67.883 18.226 1.00 34.14 O ANISOU 554 O GLN D 70 4293 4244 4433 48 -268 -106 O ATOM 555 CB GLN A 70 97.818 67.198 16.111 1.00 37.00 C ANISOU 555 CB GLN D 70 4701 4693 4661 14 -150 -92 C ATOM 556 CG GLN A 70 96.972 66.627 14.982 1.00 38.84 C ANISOU 556 CG GLN D 70 5060 4832 4865 -134 31 -19 C ATOM 557 CD GLN A 70 96.852 67.588 13.822 1.00 41.55 C ANISOU 557 CD GLN D 70 5391 5327 5067 -34 87 -139 C ATOM 558 OE1 GLN A 70 96.411 68.738 13.992 1.00 48.71 O ANISOU 558 OE1 GLN D 70 6432 5818 6256 199 -51 37 O ATOM 559 NE2 GLN A 70 97.233 67.129 12.628 1.00 47.80 N ANISOU 559 NE2 GLN D 70 6179 6171 5810 9 -235 236 N ATOM 560 N PRO A 71 99.279 65.868 19.249 1.00 32.99 N ANISOU 560 N PRO D 71 4026 4239 4266 98 -216 18 N ATOM 561 CA PRO A 71 99.981 66.295 20.427 1.00 33.40 C ANISOU 561 CA PRO D 71 4109 4227 4351 35 -173 26 C ATOM 562 C PRO A 71 101.301 66.961 20.167 1.00 32.88 C ANISOU 562 C PRO D 71 4021 4146 4323 27 -170 -7 C ATOM 563 O PRO A 71 101.769 67.699 21.029 1.00 32.26 O ANISOU 563 O PRO D 71 3595 4077 4585 16 -338 -37 O ATOM 564 CB PRO A 71 100.195 64.991 21.205 1.00 32.95 C ANISOU 564 CB PRO D 71 4074 4137 4309 40 -82 15 C ATOM 565 CG PRO A 71 100.056 63.922 20.214 1.00 31.92 C ANISOU 565 CG PRO D 71 4038 3952 4135 5 -206 -51 C ATOM 566 CD PRO A 71 99.065 64.406 19.248 1.00 33.09 C ANISOU 566 CD PRO D 71 4078 4252 4240 -6 -133 -31 C ATOM 567 N GLU A 72 101.898 66.679 19.006 1.00 33.70 N ANISOU 567 N GLU D 72 4169 4240 4392 -4 -145 -118 N ATOM 568 CA GLU A 72 103.195 67.244 18.651 1.00 35.00 C ANISOU 568 CA GLU D 72 4374 4386 4535 -12 -160 -64 C ATOM 569 C GLU A 72 103.117 68.768 18.418 1.00 34.96 C ANISOU 569 C GLU D 72 4387 4333 4560 -34 -128 -123 C ATOM 570 O GLU A 72 104.123 69.455 18.496 1.00 34.93 O ANISOU 570 O GLU D 72 4354 4339 4576 -16 -199 -204 O ATOM 571 CB GLU A 72 103.784 66.505 17.431 1.00 35.53 C ANISOU 571 CB GLU D 72 4495 4409 4595 -2 -173 -40 C ATOM 572 CG GLU A 72 103.194 66.860 16.059 1.00 38.13 C ANISOU 572 CG GLU D 72 4792 4871 4823 -48 51 -6 C ATOM 573 CD GLU A 72 101.902 66.137 15.704 1.00 39.18 C ANISOU 573 CD GLU D 72 4980 5105 4802 -162 46 -60 C ATOM 574 OE1 GLU A 72 101.358 65.390 16.558 1.00 37.19 O ANISOU 574 OE1 GLU D 72 4698 4775 4655 -171 -106 -90 O ATOM 575 OE2 GLU A 72 101.434 66.335 14.545 1.00 38.26 O ANISOU 575 OE2 GLU D 72 4953 5152 4430 213 -85 -119 O ATOM 576 N LYS A 73 101.909 69.270 18.177 1.00 35.25 N ANISOU 576 N LYS D 73 4396 4390 4607 -44 -164 -198 N ATOM 577 CA LYS A 73 101.657 70.694 17.943 1.00 35.75 C ANISOU 577 CA LYS D 73 4488 4475 4619 -9 -119 -89 C ATOM 578 C LYS A 73 101.425 71.550 19.183 1.00 34.71 C ANISOU 578 C LYS D 73 4317 4344 4527 60 -170 -105 C ATOM 579 O LYS A 73 101.340 72.765 19.064 1.00 35.32 O ANISOU 579 O LYS D 73 4207 4432 4781 52 -365 -196 O ATOM 580 CB LYS A 73 100.447 70.848 17.018 1.00 36.98 C ANISOU 580 CB LYS D 73 4531 4702 4815 -18 -57 -225 C ATOM 581 CG LYS A 73 100.659 70.242 15.642 1.00 39.01 C ANISOU 581 CG LYS D 73 4905 4847 5069 -19 -102 13 C ATOM 582 CD LYS A 73 99.406 70.357 14.791 1.00 38.60 C ANISOU 582 CD LYS D 73 4921 4880 4863 -46 -49 -48 C ATOM 583 CE LYS A 73 99.689 70.088 13.327 1.00 42.43 C ANISOU 583 CE LYS D 73 5517 5411 5191 58 9 66 C ATOM 584 NZ LYS A 73 98.466 70.263 12.475 1.00 46.24 N ANISOU 584 NZ LYS D 73 5818 6057 5694 -2 276 -16 N ATOM 585 N ARG A 74 101.327 70.940 20.359 1.00 34.01 N ANISOU 585 N ARG D 74 4250 4170 4501 116 -109 -105 N ATOM 586 CA ARG A 74 100.956 71.663 21.582 1.00 33.43 C ANISOU 586 CA ARG D 74 4174 4195 4332 42 -78 -106 C ATOM 587 C ARG A 74 102.004 72.648 22.082 1.00 33.89 C ANISOU 587 C ARG D 74 4222 4195 4457 53 -208 -155 C ATOM 588 O ARG A 74 101.659 73.714 22.587 1.00 31.80 O ANISOU 588 O ARG D 74 3970 3946 4163 39 -484 -259 O ATOM 589 CB ARG A 74 100.594 70.672 22.699 1.00 33.26 C ANISOU 589 CB ARG D 74 4126 4120 4388 97 -64 -4 C ATOM 590 CG ARG A 74 99.380 69.806 22.366 1.00 32.46 C ANISOU 590 CG ARG D 74 3990 4029 4314 59 0 -76 C ATOM 591 CD ARG A 74 99.147 68.720 23.405 1.00 32.59 C ANISOU 591 CD ARG D 74 3971 4098 4313 -32 -48 -73 C ATOM 592 NE ARG A 74 100.254 67.754 23.449 1.00 34.27 N ANISOU 592 NE ARG D 74 4077 4190 4752 74 -284 -273 N ATOM 593 CZ ARG A 74 100.402 66.793 24.357 1.00 35.33 C ANISOU 593 CZ ARG D 74 4334 4495 4591 191 -168 -112 C ATOM 594 NH1 ARG A 74 99.513 66.629 25.329 1.00 33.65 N ANISOU 594 NH1 ARG D 74 4170 4055 4557 108 -222 24 N ATOM 595 NH2 ARG A 74 101.464 65.982 24.294 1.00 32.68 N ANISOU 595 NH2 ARG D 74 4049 4045 4320 110 -178 -88 N ATOM 596 N ILE A 75 103.289 72.306 21.975 1.00 34.66 N ANISOU 596 N ILE D 75 4223 4313 4631 46 -158 -71 N ATOM 597 CA ILE A 75 104.319 73.227 22.444 1.00 34.83 C ANISOU 597 CA ILE D 75 4239 4434 4558 66 -76 -59 C ATOM 598 C ILE A 75 104.308 74.503 21.591 1.00 34.20 C ANISOU 598 C ILE D 75 4030 4351 4613 1 -192 -26 C ATOM 599 O ILE A 75 104.396 75.597 22.151 1.00 35.05 O ANISOU 599 O ILE D 75 4033 4300 4982 -139 -361 -84 O ATOM 600 CB ILE A 75 105.735 72.581 22.467 1.00 35.35 C ANISOU 600 CB ILE D 75 4232 4479 4719 85 -7 -37 C ATOM 601 CG1 ILE A 75 105.758 71.440 23.473 1.00 37.80 C ANISOU 601 CG1 ILE D 75 4635 4782 4945 125 -13 -48 C ATOM 602 CG2 ILE A 75 106.787 73.583 22.888 1.00 35.37 C ANISOU 602 CG2 ILE D 75 4338 4419 4682 72 -69 10 C ATOM 603 CD1 ILE A 75 106.820 70.414 23.178 1.00 37.59 C ANISOU 603 CD1 ILE D 75 4639 4763 4877 122 0 -20 C ATOM 604 N SER A 76 104.157 74.366 20.266 1.00 33.21 N ANISOU 604 N SER D 76 3927 4218 4472 70 -128 -53 N ATOM 605 CA SER A 76 104.086 75.543 19.386 1.00 32.77 C ANISOU 605 CA SER D 76 3918 4158 4373 102 -148 -42 C ATOM 606 C SER A 76 102.785 76.333 19.628 1.00 31.23 C ANISOU 606 C SER D 76 3818 3850 4199 48 -245 -16 C ATOM 607 O SER A 76 102.831 77.573 19.784 1.00 30.36 O ANISOU 607 O SER D 76 3743 3609 4183 57 -410 -353 O ATOM 608 CB SER A 76 104.263 75.184 17.906 1.00 34.57 C ANISOU 608 CB SER D 76 4342 4296 4495 89 -56 8 C ATOM 609 OG SER A 76 103.043 74.862 17.235 1.00 40.75 O ANISOU 609 OG SER D 76 4582 5454 5444 247 -143 -59 O ATOM 610 N PHE A 77 101.658 75.616 19.708 1.00 28.68 N ANISOU 610 N PHE D 77 3533 3577 3785 82 -209 -26 N ATOM 611 CA PHE A 77 100.366 76.226 20.071 1.00 29.35 C ANISOU 611 CA PHE D 77 3578 3669 3903 -24 -189 -79 C ATOM 612 C PHE A 77 100.495 77.107 21.311 1.00 27.83 C ANISOU 612 C PHE D 77 3211 3567 3795 -53 -380 -119 C ATOM 613 O PHE A 77 100.070 78.262 21.294 1.00 29.71 O ANISOU 613 O PHE D 77 3456 3608 4222 -8 -627 -279 O ATOM 614 CB PHE A 77 99.281 75.152 20.250 1.00 28.39 C ANISOU 614 CB PHE D 77 3329 3719 3738 133 -305 -6 C ATOM 615 CG PHE A 77 97.926 75.696 20.666 1.00 28.46 C ANISOU 615 CG PHE D 77 3517 3619 3677 92 -147 -86 C ATOM 616 CD1 PHE A 77 96.979 76.091 19.723 1.00 26.79 C ANISOU 616 CD1 PHE D 77 3152 3465 3560 3 -292 -285 C ATOM 617 CD2 PHE A 77 97.614 75.802 22.010 1.00 28.16 C ANISOU 617 CD2 PHE D 77 3533 3532 3633 211 -240 -26 C ATOM 618 CE1 PHE A 77 95.720 76.585 20.133 1.00 27.29 C ANISOU 618 CE1 PHE D 77 3743 3548 3076 174 -303 -79 C ATOM 619 CE2 PHE A 77 96.369 76.287 22.421 1.00 29.13 C ANISOU 619 CE2 PHE D 77 3445 3765 3857 61 -179 -63 C ATOM 620 CZ PHE A 77 95.439 76.677 21.505 1.00 24.16 C ANISOU 620 CZ PHE D 77 3155 3134 2888 -339 -239 -218 C ATOM 621 N ILE A 78 101.078 76.592 22.381 1.00 27.81 N ANISOU 621 N ILE D 78 3104 3523 3937 -97 -317 -46 N ATOM 622 CA ILE A 78 101.210 77.390 23.604 1.00 29.75 C ANISOU 622 CA ILE D 78 3561 3745 3995 -88 -213 -48 C ATOM 623 C ILE A 78 102.006 78.650 23.296 1.00 30.75 C ANISOU 623 C ILE D 78 3614 3767 4302 -116 -252 0 C ATOM 624 O ILE A 78 101.562 79.770 23.539 1.00 30.50 O ANISOU 624 O ILE D 78 3242 3800 4546 -292 -481 -32 O ATOM 625 CB ILE A 78 101.889 76.624 24.754 1.00 29.03 C ANISOU 625 CB ILE D 78 3485 3471 4071 -14 -170 -42 C ATOM 626 CG1 ILE A 78 101.016 75.437 25.190 1.00 30.72 C ANISOU 626 CG1 ILE D 78 3641 3927 4104 -80 -98 -106 C ATOM 627 CG2 ILE A 78 102.108 77.518 25.970 1.00 28.52 C ANISOU 627 CG2 ILE D 78 3326 3602 3907 -51 -149 -137 C ATOM 628 CD1 ILE A 78 101.826 74.207 25.534 1.00 31.48 C ANISOU 628 CD1 ILE D 78 3903 3925 4130 -86 -72 -244 C ATOM 629 N ARG A 79 103.167 78.448 22.696 1.00 31.79 N ANISOU 629 N ARG D 79 3729 3941 4409 -125 -239 -58 N ATOM 630 CA ARG A 79 104.106 79.542 22.465 1.00 32.32 C ANISOU 630 CA ARG D 79 3862 4121 4296 -75 -235 -34 C ATOM 631 C ARG A 79 103.442 80.650 21.661 1.00 30.72 C ANISOU 631 C ARG D 79 3604 3966 4099 -88 -371 -10 C ATOM 632 O ARG A 79 103.579 81.834 21.961 1.00 31.29 O ANISOU 632 O ARG D 79 3566 3985 4336 -38 -572 162 O ATOM 633 CB ARG A 79 105.343 78.989 21.740 1.00 32.22 C ANISOU 633 CB ARG D 79 3725 4304 4213 -119 -311 -22 C ATOM 634 CG ARG A 79 106.439 80.027 21.529 1.00 34.29 C ANISOU 634 CG ARG D 79 4063 4312 4653 -168 -140 -19 C ATOM 635 CD ARG A 79 107.776 79.410 21.025 1.00 36.16 C ANISOU 635 CD ARG D 79 4248 4816 4673 31 -343 29 C ATOM 636 NE ARG A 79 108.361 78.345 21.859 1.00 39.78 N ANISOU 636 NE ARG D 79 5135 4956 5021 11 -222 -103 N ATOM 637 CZ ARG A 79 108.573 77.086 21.460 1.00 41.58 C ANISOU 637 CZ ARG D 79 5427 5094 5276 -40 -15 -35 C ATOM 638 NH1 ARG A 79 108.214 76.670 20.243 1.00 43.33 N ANISOU 638 NH1 ARG D 79 5753 5693 5017 -76 -19 -119 N ATOM 639 NH2 ARG A 79 109.147 76.221 22.284 1.00 40.84 N ANISOU 639 NH2 ARG D 79 5336 5286 4893 -130 -25 -165 N ATOM 640 N ASP A 80 102.693 80.247 20.652 1.00 29.32 N ANISOU 640 N ASP D 80 3328 3861 3948 -97 -408 -119 N ATOM 641 CA ASP A 80 102.085 81.173 19.742 1.00 30.36 C ANISOU 641 CA ASP D 80 3590 3889 4057 -10 -287 -90 C ATOM 642 C ASP A 80 100.906 81.945 20.363 1.00 30.50 C ANISOU 642 C ASP D 80 3641 3802 4143 15 -338 -163 C ATOM 643 O ASP A 80 100.817 83.172 20.227 1.00 28.52 O ANISOU 643 O ASP D 80 3240 3717 3877 159 -591 -293 O ATOM 644 CB ASP A 80 101.691 80.414 18.490 1.00 28.80 C ANISOU 644 CB ASP D 80 3455 3607 3878 -8 -302 -57 C ATOM 645 CG ASP A 80 102.919 79.967 17.679 1.00 30.21 C ANISOU 645 CG ASP D 80 3837 3795 3847 97 -1 192 C ATOM 646 OD1 ASP A 80 104.061 80.199 18.146 1.00 33.90 O ANISOU 646 OD1 ASP D 80 3801 4288 4791 78 -375 -395 O ATOM 647 OD2 ASP A 80 102.735 79.396 16.590 1.00 26.26 O ANISOU 647 OD2 ASP D 80 3598 4338 2040 702 -1034 -276 O ATOM 648 N MET A 81 100.026 81.245 21.079 1.00 31.14 N ANISOU 648 N MET D 81 3644 3992 4194 42 -315 -254 N ATOM 649 CA MET A 81 98.919 81.922 21.741 1.00 31.12 C ANISOU 649 CA MET D 81 3804 3919 4101 44 -280 -110 C ATOM 650 C MET A 81 99.472 82.987 22.641 1.00 30.65 C ANISOU 650 C MET D 81 3708 3881 4055 -84 -352 -168 C ATOM 651 O MET A 81 99.033 84.145 22.558 1.00 29.73 O ANISOU 651 O MET D 81 3489 3639 4166 -272 -482 -225 O ATOM 652 CB MET A 81 98.026 80.936 22.521 1.00 30.49 C ANISOU 652 CB MET D 81 3592 3904 4085 58 -283 -48 C ATOM 653 CG MET A 81 97.242 79.979 21.623 1.00 29.12 C ANISOU 653 CG MET D 81 3677 3626 3759 -88 -417 -90 C ATOM 654 SD MET A 81 96.007 80.757 20.542 1.00 33.44 S ANISOU 654 SD MET D 81 4151 4088 4464 -140 -651 -319 S ATOM 655 CE MET A 81 94.612 80.924 21.653 1.00 31.64 C ANISOU 655 CE MET D 81 4078 3820 4123 16 -295 -55 C ATOM 656 N GLN A 82 100.461 82.620 23.456 1.00 31.90 N ANISOU 656 N GLN D 82 3897 3969 4251 -69 -360 -136 N ATOM 657 CA GLN A 82 100.921 83.458 24.548 1.00 34.40 C ANISOU 657 CA GLN D 82 4244 4339 4485 -67 -176 -18 C ATOM 658 C GLN A 82 101.651 84.688 24.020 1.00 36.74 C ANISOU 658 C GLN D 82 4580 4526 4854 -122 -164 -3 C ATOM 659 O GLN A 82 101.726 85.702 24.711 1.00 37.76 O ANISOU 659 O GLN D 82 4710 4471 5163 -250 -240 -64 O ATOM 660 CB GLN A 82 101.821 82.676 25.506 1.00 35.06 C ANISOU 660 CB GLN D 82 4371 4411 4536 -90 -196 -40 C ATOM 661 CG GLN A 82 101.133 81.488 26.214 1.00 34.60 C ANISOU 661 CG GLN D 82 4133 4419 4593 -193 -142 -122 C ATOM 662 CD GLN A 82 101.900 80.960 27.427 1.00 35.28 C ANISOU 662 CD GLN D 82 4303 4516 4586 -85 -97 1 C ATOM 663 OE1 GLN A 82 103.145 80.927 27.447 1.00 33.96 O ANISOU 663 OE1 GLN D 82 4024 4286 4592 -63 -262 -63 O ATOM 664 NE2 GLN A 82 101.155 80.528 28.453 1.00 36.40 N ANISOU 664 NE2 GLN D 82 4300 4568 4961 -264 -167 -28 N ATOM 665 N SER A 83 102.187 84.569 22.806 1.00 37.45 N ANISOU 665 N SER D 83 4747 4648 4833 -135 -134 -137 N ATOM 666 CA SER A 83 102.891 85.656 22.133 1.00 37.90 C ANISOU 666 CA SER D 83 4780 4678 4942 -77 -127 -90 C ATOM 667 C SER A 83 101.911 86.674 21.527 1.00 39.28 C ANISOU 667 C SER D 83 4910 4855 5161 -14 -52 -92 C ATOM 668 O SER A 83 102.277 87.841 21.303 1.00 40.55 O ANISOU 668 O SER D 83 5001 4874 5529 86 -121 -115 O ATOM 669 CB SER A 83 103.789 85.093 21.038 1.00 38.41 C ANISOU 669 CB SER D 83 4840 4731 5021 -79 -135 -59 C ATOM 670 OG SER A 83 103.047 84.788 19.870 1.00 40.76 O ANISOU 670 OG SER D 83 4954 5030 5502 -2 -67 -164 O ATOM 671 N ARG A 84 100.684 86.226 21.256 1.00 38.65 N ANISOU 671 N ARG D 84 4877 4784 5022 -37 -50 -55 N ATOM 672 CA ARG A 84 99.587 87.111 20.854 1.00 38.51 C ANISOU 672 CA ARG D 84 4851 4744 5035 -21 -118 -57 C ATOM 673 C ARG A 84 98.816 87.608 22.076 1.00 36.72 C ANISOU 673 C ARG D 84 4638 4500 4813 -81 -76 -83 C ATOM 674 O ARG A 84 97.756 88.220 21.942 1.00 36.53 O ANISOU 674 O ARG D 84 4762 4202 4914 -49 -307 30 O ATOM 675 CB ARG A 84 98.640 86.393 19.899 1.00 37.98 C ANISOU 675 CB ARG D 84 4781 4712 4936 58 11 -84 C ATOM 676 CG ARG A 84 99.212 86.161 18.530 1.00 43.42 C ANISOU 676 CG ARG D 84 5567 5361 5570 25 -264 -71 C ATOM 677 CD ARG A 84 98.425 85.095 17.756 1.00 44.60 C ANISOU 677 CD ARG D 84 5679 5640 5626 -49 -61 108 C ATOM 678 NE ARG A 84 97.457 85.645 16.799 1.00 51.66 N ANISOU 678 NE ARG D 84 6518 6615 6493 29 224 -108 N ATOM 679 CZ ARG A 84 96.687 84.906 15.993 1.00 51.30 C ANISOU 679 CZ ARG D 84 6479 6549 6463 -124 240 92 C ATOM 680 NH1 ARG A 84 96.754 83.570 16.033 1.00 53.95 N ANISOU 680 NH1 ARG D 84 6973 6698 6825 113 27 -23 N ATOM 681 NH2 ARG A 84 95.839 85.498 15.141 1.00 51.91 N ANISOU 681 NH2 ARG D 84 6731 6525 6467 -1 157 41 N ATOM 682 N GLY A 85 99.345 87.358 23.267 1.00 35.54 N ANISOU 682 N GLY D 85 4510 4235 4756 -184 -145 -11 N ATOM 683 CA GLY A 85 98.681 87.785 24.489 1.00 35.78 C ANISOU 683 CA GLY D 85 4498 4291 4805 -140 -138 -37 C ATOM 684 C GLY A 85 97.385 87.022 24.754 1.00 35.75 C ANISOU 684 C GLY D 85 4417 4247 4919 -124 -246 27 C ATOM 685 O GLY A 85 96.470 87.548 25.383 1.00 36.46 O ANISOU 685 O GLY D 85 4728 4056 5069 -218 -527 -37 O ATOM 686 N LEU A 86 97.306 85.786 24.265 1.00 34.48 N ANISOU 686 N LEU D 86 4211 4090 4798 -138 -219 -62 N ATOM 687 CA LEU A 86 96.101 84.971 24.434 1.00 33.05 C ANISOU 687 CA LEU D 86 4064 4061 4431 -11 -159 -82 C ATOM 688 C LEU A 86 96.387 83.812 25.413 1.00 32.59 C ANISOU 688 C LEU D 86 3990 4042 4350 -15 -146 -151 C ATOM 689 O LEU A 86 97.520 83.353 25.533 1.00 32.82 O ANISOU 689 O LEU D 86 3980 4047 4442 -50 -261 -307 O ATOM 690 CB LEU A 86 95.636 84.456 23.078 1.00 31.57 C ANISOU 690 CB LEU D 86 3726 4001 4268 84 -129 -25 C ATOM 691 CG LEU A 86 95.301 85.512 22.028 1.00 31.88 C ANISOU 691 CG LEU D 86 3890 3971 4249 130 -284 75 C ATOM 692 CD1 LEU A 86 94.840 84.870 20.727 1.00 32.26 C ANISOU 692 CD1 LEU D 86 4019 3914 4323 87 -107 -59 C ATOM 693 CD2 LEU A 86 94.200 86.466 22.557 1.00 31.15 C ANISOU 693 CD2 LEU D 86 3830 3575 4429 61 -40 13 C ATOM 694 N ILE A 87 95.349 83.375 26.124 1.00 31.46 N ANISOU 694 N ILE D 87 3915 3926 4110 -17 -159 -186 N ATOM 695 CA ILE A 87 95.436 82.235 27.035 1.00 30.66 C ANISOU 695 CA ILE D 87 3736 3859 4052 -12 -146 -37 C ATOM 696 C ILE A 87 95.730 80.973 26.247 1.00 27.65 C ANISOU 696 C ILE D 87 3234 3581 3692 -132 -214 -125 C ATOM 697 O ILE A 87 95.187 80.767 25.172 1.00 25.66 O ANISOU 697 O ILE D 87 2712 3443 3594 -378 -470 -293 O ATOM 698 CB ILE A 87 94.093 82.069 27.827 1.00 31.01 C ANISOU 698 CB ILE D 87 3935 3904 3940 -47 -164 -57 C ATOM 699 CG1 ILE A 87 94.049 83.084 28.980 1.00 31.39 C ANISOU 699 CG1 ILE D 87 3919 4044 3962 72 -202 39 C ATOM 700 CG2 ILE A 87 93.947 80.689 28.412 1.00 32.10 C ANISOU 700 CG2 ILE D 87 3991 3960 4244 -39 -151 -117 C ATOM 701 CD1 ILE A 87 92.705 83.599 29.234 1.00 32.06 C ANISOU 701 CD1 ILE D 87 4007 4161 4012 -1 -91 45 C ATOM 702 N ALA A 88 96.600 80.141 26.806 1.00 27.71 N ANISOU 702 N ALA D 88 3178 3495 3854 -134 -340 -91 N ATOM 703 CA ALA A 88 96.889 78.800 26.277 1.00 27.62 C ANISOU 703 CA ALA D 88 3250 3524 3718 -108 -131 15 C ATOM 704 C ALA A 88 96.280 77.770 27.224 1.00 25.86 C ANISOU 704 C ALA D 88 3019 3311 3493 -54 -120 -25 C ATOM 705 O ALA A 88 96.638 77.707 28.389 1.00 26.42 O ANISOU 705 O ALA D 88 2862 3440 3734 -217 -219 -163 O ATOM 706 CB ALA A 88 98.391 78.570 26.168 1.00 28.33 C ANISOU 706 CB ALA D 88 3273 3565 3926 -66 -216 160 C ATOM 707 N SER A 89 95.365 76.976 26.693 1.00 25.72 N ANISOU 707 N SER D 89 2935 3282 3555 -9 -186 -72 N ATOM 708 CA SER A 89 94.611 75.987 27.444 1.00 25.15 C ANISOU 708 CA SER D 89 3055 3199 3300 -9 -137 -69 C ATOM 709 C SER A 89 94.679 74.696 26.623 1.00 24.25 C ANISOU 709 C SER D 89 2879 3164 3170 2 -173 -44 C ATOM 710 O SER A 89 94.170 74.647 25.506 1.00 21.04 O ANISOU 710 O SER D 89 2647 2955 2392 -81 -655 -119 O ATOM 711 CB SER A 89 93.156 76.470 27.591 1.00 24.66 C ANISOU 711 CB SER D 89 2884 3153 3332 -2 -339 -144 C ATOM 712 OG SER A 89 92.285 75.512 28.227 1.00 23.96 O ANISOU 712 OG SER D 89 2539 2574 3990 -118 -436 -318 O ATOM 713 N ILE A 90 95.323 73.668 27.174 1.00 24.22 N ANISOU 713 N ILE D 90 2932 3006 3263 -111 -258 -94 N ATOM 714 CA ILE A 90 95.605 72.461 26.393 1.00 25.69 C ANISOU 714 CA ILE D 90 3188 3099 3471 -52 -137 -80 C ATOM 715 C ILE A 90 95.102 71.234 27.142 1.00 24.91 C ANISOU 715 C ILE D 90 3054 3108 3301 -120 -175 -126 C ATOM 716 O ILE A 90 94.691 71.364 28.271 1.00 26.28 O ANISOU 716 O ILE D 90 3167 3268 3548 -18 -25 -164 O ATOM 717 CB ILE A 90 97.108 72.301 26.116 1.00 24.76 C ANISOU 717 CB ILE D 90 3150 2922 3334 -111 -247 -85 C ATOM 718 CG1 ILE A 90 97.891 72.198 27.444 1.00 25.94 C ANISOU 718 CG1 ILE D 90 2938 3363 3554 -117 -169 -52 C ATOM 719 CG2 ILE A 90 97.613 73.455 25.205 1.00 24.92 C ANISOU 719 CG2 ILE D 90 3181 2847 3437 50 -275 -121 C ATOM 720 CD1 ILE A 90 99.184 71.422 27.377 1.00 26.87 C ANISOU 720 CD1 ILE D 90 3472 3293 3442 71 -122 -57 C ATOM 721 N SER A 91 95.149 70.075 26.478 1.00 26.23 N ANISOU 721 N SER D 91 3046 3252 3666 -112 -249 -77 N ATOM 722 CA SER A 91 94.808 68.783 27.068 1.00 25.83 C ANISOU 722 CA SER D 91 3171 3199 3442 -5 -76 -51 C ATOM 723 C SER A 91 96.040 67.876 27.131 1.00 26.70 C ANISOU 723 C SER D 91 3234 3442 3465 42 -46 -111 C ATOM 724 O SER A 91 96.908 67.924 26.256 1.00 26.51 O ANISOU 724 O SER D 91 3051 3248 3773 93 -75 -265 O ATOM 725 CB SER A 91 93.698 68.093 26.238 1.00 25.77 C ANISOU 725 CB SER D 91 3156 3241 3392 15 -76 -131 C ATOM 726 OG SER A 91 92.532 68.878 26.206 1.00 25.64 O ANISOU 726 OG SER D 91 2897 3352 3492 -2 -170 -48 O ATOM 727 N VAL A 92 96.114 67.057 28.175 1.00 26.61 N ANISOU 727 N VAL D 92 3178 3419 3512 -23 -89 -140 N ATOM 728 CA VAL A 92 97.151 66.023 28.294 1.00 26.92 C ANISOU 728 CA VAL D 92 3340 3437 3448 26 -69 -103 C ATOM 729 C VAL A 92 96.540 64.703 28.752 1.00 27.60 C ANISOU 729 C VAL D 92 3381 3491 3612 56 -62 -136 C ATOM 730 O VAL A 92 95.430 64.679 29.298 1.00 26.02 O ANISOU 730 O VAL D 92 3635 3311 2938 113 -498 -403 O ATOM 731 CB VAL A 92 98.266 66.416 29.286 1.00 26.52 C ANISOU 731 CB VAL D 92 3280 3418 3377 33 -23 -30 C ATOM 732 CG1 VAL A 92 98.871 67.742 28.921 1.00 28.52 C ANISOU 732 CG1 VAL D 92 3590 3655 3591 23 80 -125 C ATOM 733 CG2 VAL A 92 97.752 66.481 30.718 1.00 27.44 C ANISOU 733 CG2 VAL D 92 3350 3475 3600 89 -125 -68 C ATOM 734 N GLY A 93 97.274 63.620 28.515 1.00 28.18 N ANISOU 734 N GLY D 93 3483 3563 3659 54 -112 80 N ATOM 735 CA GLY A 93 96.929 62.288 29.003 1.00 28.93 C ANISOU 735 CA GLY D 93 3599 3591 3801 32 -129 -20 C ATOM 736 C GLY A 93 97.790 61.914 30.192 1.00 29.37 C ANISOU 736 C GLY D 93 3638 3673 3847 71 -55 10 C ATOM 737 O GLY A 93 98.312 62.793 30.916 1.00 31.21 O ANISOU 737 O GLY D 93 3800 3686 4371 244 33 -58 O ATOM 738 N VAL A 94 97.955 60.613 30.418 1.00 29.12 N ANISOU 738 N VAL D 94 3600 3702 3760 61 -166 89 N ATOM 739 CA VAL A 94 98.666 60.150 31.608 1.00 31.43 C ANISOU 739 CA VAL D 94 3868 3942 4129 78 -73 -71 C ATOM 740 C VAL A 94 99.806 59.145 31.346 1.00 33.20 C ANISOU 740 C VAL D 94 4065 4127 4422 98 -60 -72 C ATOM 741 O VAL A 94 100.443 58.688 32.299 1.00 33.22 O ANISOU 741 O VAL D 94 4112 3970 4538 160 -33 -192 O ATOM 742 CB VAL A 94 97.683 59.571 32.680 1.00 30.99 C ANISOU 742 CB VAL D 94 3872 3908 3993 137 -81 -89 C ATOM 743 CG1 VAL A 94 96.566 60.584 32.992 1.00 28.50 C ANISOU 743 CG1 VAL D 94 3496 3656 3673 -58 -324 -360 C ATOM 744 CG2 VAL A 94 97.099 58.253 32.244 1.00 31.21 C ANISOU 744 CG2 VAL D 94 3612 4077 4167 97 11 -98 C ATOM 745 N LYS A 95 100.048 58.843 30.072 1.00 33.92 N ANISOU 745 N LYS D 95 4212 4232 4443 100 -145 -18 N ATOM 746 CA LYS A 95 101.139 57.955 29.628 1.00 36.55 C ANISOU 746 CA LYS D 95 4550 4563 4772 137 -98 -19 C ATOM 747 C LYS A 95 102.548 58.552 29.802 1.00 36.92 C ANISOU 747 C LYS D 95 4518 4589 4920 123 -131 -4 C ATOM 748 O LYS A 95 102.733 59.768 29.986 1.00 34.43 O ANISOU 748 O LYS D 95 4056 4173 4850 382 -278 -128 O ATOM 749 CB LYS A 95 100.942 57.581 28.160 1.00 36.94 C ANISOU 749 CB LYS D 95 4690 4556 4788 146 -54 98 C ATOM 750 CG LYS A 95 99.929 56.465 27.911 1.00 41.84 C ANISOU 750 CG LYS D 95 5209 5296 5391 -45 47 -14 C ATOM 751 CD LYS A 95 99.810 56.135 26.403 1.00 41.16 C ANISOU 751 CD LYS D 95 5272 5256 5110 -2 13 53 C ATOM 752 CE LYS A 95 101.078 55.431 25.856 1.00 47.18 C ANISOU 752 CE LYS D 95 5921 6082 5922 138 -120 37 C ATOM 753 NZ LYS A 95 101.311 55.636 24.375 1.00 49.12 N ANISOU 753 NZ LYS D 95 6359 6516 5789 44 -138 96 N ATOM 754 N GLU A 96 103.550 57.668 29.720 1.00 38.03 N ANISOU 754 N GLU D 96 4751 4690 5008 143 -91 -20 N ATOM 755 CA GLU A 96 104.917 58.043 30.034 1.00 38.58 C ANISOU 755 CA GLU D 96 4775 4836 5048 141 -69 0 C ATOM 756 C GLU A 96 105.412 59.204 29.172 1.00 37.83 C ANISOU 756 C GLU D 96 4560 4736 5074 195 -56 33 C ATOM 757 O GLU A 96 106.098 60.095 29.679 1.00 39.57 O ANISOU 757 O GLU D 96 4639 4855 5540 195 -25 80 O ATOM 758 CB GLU A 96 105.845 56.830 29.919 1.00 39.20 C ANISOU 758 CB GLU D 96 4896 4927 5070 159 -51 -14 C ATOM 759 CG GLU A 96 107.274 57.072 30.364 1.00 39.41 C ANISOU 759 CG GLU D 96 4930 5008 5032 136 -71 13 C ATOM 760 CD GLU A 96 108.112 55.792 30.261 1.00 43.05 C ANISOU 760 CD GLU D 96 5260 5390 5704 289 17 -15 C ATOM 761 OE1 GLU A 96 108.095 54.973 31.219 1.00 49.74 O ANISOU 761 OE1 GLU D 96 6531 6281 6085 127 -73 -240 O ATOM 762 OE2 GLU A 96 108.771 55.603 29.208 1.00 50.47 O ANISOU 762 OE2 GLU D 96 6200 6690 6285 272 -272 22 O ATOM 763 N ASP A 97 105.041 59.221 27.898 1.00 35.62 N ANISOU 763 N ASP D 97 4325 4506 4704 206 -211 94 N ATOM 764 CA ASP A 97 105.414 60.330 27.026 1.00 37.06 C ANISOU 764 CA ASP D 97 4559 4646 4876 110 -145 65 C ATOM 765 C ASP A 97 104.818 61.687 27.433 1.00 36.76 C ANISOU 765 C ASP D 97 4517 4610 4838 106 -237 20 C ATOM 766 O ASP A 97 105.405 62.739 27.124 1.00 35.31 O ANISOU 766 O ASP D 97 4224 4549 4640 163 -382 59 O ATOM 767 CB ASP A 97 105.061 60.028 25.576 1.00 37.48 C ANISOU 767 CB ASP D 97 4770 4697 4771 8 -99 11 C ATOM 768 CG ASP A 97 103.595 59.736 25.385 1.00 44.31 C ANISOU 768 CG ASP D 97 5321 5738 5774 83 17 15 C ATOM 769 OD1 ASP A 97 102.866 59.557 26.396 1.00 48.74 O ANISOU 769 OD1 ASP D 97 6386 6519 5613 144 -72 -89 O ATOM 770 OD2 ASP A 97 103.162 59.656 24.216 1.00 50.54 O ANISOU 770 OD2 ASP D 97 6713 6598 5889 234 121 -20 O ATOM 771 N GLU A 98 103.672 61.670 28.130 1.00 36.09 N ANISOU 771 N GLU D 98 4330 4495 4885 83 -143 -26 N ATOM 772 CA GLU A 98 103.089 62.920 28.649 1.00 35.61 C ANISOU 772 CA GLU D 98 4361 4530 4639 35 -123 23 C ATOM 773 C GLU A 98 103.870 63.450 29.847 1.00 35.41 C ANISOU 773 C GLU D 98 4267 4529 4656 43 -120 -18 C ATOM 774 O GLU A 98 103.931 64.666 30.055 1.00 34.18 O ANISOU 774 O GLU D 98 3935 4534 4518 266 -52 66 O ATOM 775 CB GLU A 98 101.614 62.741 29.004 1.00 34.75 C ANISOU 775 CB GLU D 98 4274 4351 4579 46 -72 53 C ATOM 776 CG GLU A 98 100.744 62.354 27.846 1.00 31.24 C ANISOU 776 CG GLU D 98 3883 3847 4137 24 -155 -14 C ATOM 777 CD GLU A 98 100.552 63.454 26.823 1.00 34.71 C ANISOU 777 CD GLU D 98 4261 4140 4785 121 -196 -115 C ATOM 778 OE1 GLU A 98 99.540 64.173 26.906 1.00 32.94 O ANISOU 778 OE1 GLU D 98 3799 3858 4857 1 -392 -288 O ATOM 779 OE2 GLU A 98 101.390 63.584 25.900 1.00 37.19 O ANISOU 779 OE2 GLU D 98 4564 4386 5177 232 -411 -230 O ATOM 780 N TYR A 99 104.482 62.553 30.624 1.00 36.22 N ANISOU 780 N TYR D 99 4446 4540 4773 16 -106 -40 N ATOM 781 CA TYR A 99 105.451 62.965 31.635 1.00 37.02 C ANISOU 781 CA TYR D 99 4656 4670 4737 44 -39 -36 C ATOM 782 C TYR A 99 106.633 63.721 31.021 1.00 37.46 C ANISOU 782 C TYR D 99 4595 4739 4898 18 -17 18 C ATOM 783 O TYR A 99 107.084 64.725 31.573 1.00 36.43 O ANISOU 783 O TYR D 99 4323 4558 4960 -18 72 -16 O ATOM 784 CB TYR A 99 105.951 61.763 32.427 1.00 33.30 C ANISOU 784 CB TYR D 99 4020 4511 4119 -143 -546 -196 C ATOM 785 CG TYR A 99 104.962 61.305 33.459 1.00 36.66 C ANISOU 785 CG TYR D 99 4839 4424 4663 79 131 -223 C ATOM 786 CD1 TYR A 99 103.860 60.534 33.105 1.00 35.38 C ANISOU 786 CD1 TYR D 99 4594 4482 4366 -51 12 -50 C ATOM 787 CD2 TYR A 99 105.113 61.656 34.798 1.00 34.43 C ANISOU 787 CD2 TYR D 99 4482 4270 4327 54 -127 120 C ATOM 788 CE1 TYR A 99 102.947 60.099 34.063 1.00 35.84 C ANISOU 788 CE1 TYR D 99 4541 4503 4571 65 103 87 C ATOM 789 CE2 TYR A 99 104.186 61.232 35.764 1.00 36.58 C ANISOU 789 CE2 TYR D 99 4740 4328 4829 -72 82 -152 C ATOM 790 CZ TYR A 99 103.105 60.465 35.383 1.00 35.08 C ANISOU 790 CZ TYR D 99 4473 4441 4415 165 217 -171 C ATOM 791 OH TYR A 99 102.188 60.041 36.327 1.00 35.92 O ANISOU 791 OH TYR D 99 4460 4568 4618 242 37 -280 O ATOM 792 N GLU A 100 107.089 63.262 29.859 1.00 38.34 N ANISOU 792 N GLU D 100 4796 4854 4915 49 -88 -9 N ATOM 793 CA GLU A 100 108.220 63.888 29.166 1.00 39.05 C ANISOU 793 CA GLU D 100 4879 4924 5034 38 -69 -39 C ATOM 794 C GLU A 100 107.787 65.241 28.643 1.00 38.96 C ANISOU 794 C GLU D 100 4819 4875 5107 51 -66 6 C ATOM 795 O GLU A 100 108.547 66.209 28.710 1.00 39.37 O ANISOU 795 O GLU D 100 4628 4940 5391 133 -171 -6 O ATOM 796 CB GLU A 100 108.692 63.051 27.957 1.00 40.88 C ANISOU 796 CB GLU D 100 5211 5238 5083 26 -94 24 C ATOM 797 CG GLU A 100 108.800 61.518 28.168 1.00 46.96 C ANISOU 797 CG GLU D 100 6139 5656 6044 -52 -10 42 C ATOM 798 CD GLU A 100 110.130 61.029 28.737 1.00 54.11 C ANISOU 798 CD GLU D 100 6653 6894 7009 181 127 -22 C ATOM 799 OE1 GLU A 100 110.897 61.832 29.328 1.00 58.83 O ANISOU 799 OE1 GLU D 100 7322 7447 7582 -108 76 80 O ATOM 800 OE2 GLU A 100 110.397 59.810 28.596 1.00 57.09 O ANISOU 800 OE2 GLU D 100 7234 7025 7432 128 75 3 O ATOM 801 N PHE A 101 106.558 65.289 28.117 1.00 38.29 N ANISOU 801 N PHE D 101 4782 4827 4938 27 -26 -87 N ATOM 802 CA PHE A 101 105.993 66.490 27.480 1.00 38.43 C ANISOU 802 CA PHE D 101 4685 4897 5017 35 -55 -52 C ATOM 803 C PHE A 101 105.973 67.627 28.447 1.00 37.62 C ANISOU 803 C PHE D 101 4499 4803 4992 85 -36 -75 C ATOM 804 O PHE A 101 106.376 68.749 28.130 1.00 38.03 O ANISOU 804 O PHE D 101 4286 4966 5196 150 -158 -160 O ATOM 805 CB PHE A 101 104.583 66.190 26.949 1.00 34.66 C ANISOU 805 CB PHE D 101 4275 4056 4838 516 2 -248 C ATOM 806 CG PHE A 101 103.773 67.413 26.574 1.00 38.05 C ANISOU 806 CG PHE D 101 4807 4809 4840 -3 -119 -53 C ATOM 807 CD1 PHE A 101 104.055 68.136 25.413 1.00 38.49 C ANISOU 807 CD1 PHE D 101 5044 4677 4900 46 126 -169 C ATOM 808 CD2 PHE A 101 102.699 67.815 27.370 1.00 34.07 C ANISOU 808 CD2 PHE D 101 4273 4154 4515 -61 -126 -199 C ATOM 809 CE1 PHE A 101 103.281 69.252 25.062 1.00 38.87 C ANISOU 809 CE1 PHE D 101 4794 4820 5152 -13 -107 -24 C ATOM 810 CE2 PHE A 101 101.916 68.921 27.026 1.00 35.37 C ANISOU 810 CE2 PHE D 101 4372 4545 4522 -81 -230 16 C ATOM 811 CZ PHE A 101 102.208 69.646 25.874 1.00 36.43 C ANISOU 811 CZ PHE D 101 4762 4608 4471 162 -85 -109 C ATOM 812 N VAL A 102 105.490 67.321 29.639 1.00 37.44 N ANISOU 812 N VAL D 102 4517 4717 4991 48 40 -101 N ATOM 813 CA VAL A 102 105.436 68.254 30.728 1.00 38.76 C ANISOU 813 CA VAL D 102 4741 4861 5123 76 6 -47 C ATOM 814 C VAL A 102 106.836 68.726 31.117 1.00 40.27 C ANISOU 814 C VAL D 102 4825 5035 5439 18 -68 -36 C ATOM 815 O VAL A 102 107.064 69.926 31.328 1.00 40.55 O ANISOU 815 O VAL D 102 4750 5065 5593 66 -182 -47 O ATOM 816 CB VAL A 102 104.692 67.601 31.911 1.00 37.84 C ANISOU 816 CB VAL D 102 4595 4765 5015 43 56 -46 C ATOM 817 CG1 VAL A 102 104.913 68.348 33.227 1.00 36.92 C ANISOU 817 CG1 VAL D 102 4462 4661 4903 121 115 -98 C ATOM 818 CG2 VAL A 102 103.187 67.502 31.568 1.00 34.42 C ANISOU 818 CG2 VAL D 102 4219 4477 4379 40 -80 -56 C ATOM 819 N GLN A 103 107.779 67.787 31.198 1.00 40.82 N ANISOU 819 N GLN D 103 4887 5108 5513 11 0 -119 N ATOM 820 CA GLN A 103 109.154 68.147 31.546 1.00 42.00 C ANISOU 820 CA GLN D 103 5091 5309 5557 43 32 -14 C ATOM 821 C GLN A 103 109.730 69.064 30.468 1.00 42.65 C ANISOU 821 C GLN D 103 5149 5397 5657 57 -7 9 C ATOM 822 O GLN A 103 110.384 70.068 30.764 1.00 44.17 O ANISOU 822 O GLN D 103 5242 5489 6049 116 -47 24 O ATOM 823 CB GLN A 103 109.990 66.887 31.752 1.00 41.46 C ANISOU 823 CB GLN D 103 5031 5213 5506 14 65 7 C ATOM 824 CG GLN A 103 109.552 66.136 33.001 1.00 43.00 C ANISOU 824 CG GLN D 103 5351 5370 5615 30 -44 -38 C ATOM 825 CD GLN A 103 110.288 64.822 33.192 1.00 43.99 C ANISOU 825 CD GLN D 103 5395 5489 5829 85 39 -38 C ATOM 826 OE1 GLN A 103 111.487 64.825 33.404 1.00 48.94 O ANISOU 826 OE1 GLN D 103 5726 6452 6414 104 382 26 O ATOM 827 NE2 GLN A 103 109.577 63.699 33.101 1.00 44.09 N ANISOU 827 NE2 GLN D 103 5352 5453 5947 -14 15 -203 N ATOM 828 N GLN A 104 109.453 68.731 29.221 1.00 42.86 N ANISOU 828 N GLN D 104 5233 5449 5600 97 -12 10 N ATOM 829 CA GLN A 104 109.800 69.583 28.109 1.00 43.57 C ANISOU 829 CA GLN D 104 5355 5528 5671 46 -37 -9 C ATOM 830 C GLN A 104 109.338 71.014 28.315 1.00 44.23 C ANISOU 830 C GLN D 104 5428 5597 5781 38 -107 -49 C ATOM 831 O GLN A 104 110.082 71.958 28.084 1.00 43.90 O ANISOU 831 O GLN D 104 5153 5518 6008 78 -227 -24 O ATOM 832 CB GLN A 104 109.163 69.042 26.850 1.00 43.75 C ANISOU 832 CB GLN D 104 5458 5532 5631 5 40 -56 C ATOM 833 CG GLN A 104 109.860 69.421 25.589 1.00 44.49 C ANISOU 833 CG GLN D 104 5551 5698 5652 40 -26 -25 C ATOM 834 CD GLN A 104 109.274 68.697 24.393 1.00 46.77 C ANISOU 834 CD GLN D 104 5889 5963 5917 56 70 135 C ATOM 835 OE1 GLN A 104 108.429 67.827 24.548 1.00 52.29 O ANISOU 835 OE1 GLN D 104 6508 6647 6709 -188 -127 -68 O ATOM 836 NE2 GLN A 104 109.720 69.058 23.205 1.00 51.95 N ANISOU 836 NE2 GLN D 104 6780 6508 6449 -92 -66 -140 N ATOM 837 N LEU A 105 108.087 71.170 28.717 1.00 43.78 N ANISOU 837 N LEU D 105 5402 5570 5660 32 -124 -35 N ATOM 838 CA LEU A 105 107.505 72.485 28.858 1.00 44.90 C ANISOU 838 CA LEU D 105 5522 5692 5845 61 -99 30 C ATOM 839 C LEU A 105 108.283 73.234 29.935 1.00 45.35 C ANISOU 839 C LEU D 105 5515 5824 5891 62 -84 29 C ATOM 840 O LEU A 105 108.524 74.428 29.829 1.00 44.98 O ANISOU 840 O LEU D 105 5349 5883 5859 24 -88 12 O ATOM 841 CB LEU A 105 106.023 72.366 29.242 1.00 44.86 C ANISOU 841 CB LEU D 105 5543 5661 5837 22 -37 9 C ATOM 842 CG LEU A 105 105.032 72.053 28.120 1.00 43.27 C ANISOU 842 CG LEU D 105 5248 5584 5607 19 -81 -36 C ATOM 843 CD1 LEU A 105 103.626 71.847 28.639 1.00 40.27 C ANISOU 843 CD1 LEU D 105 5118 5085 5097 3 -65 -131 C ATOM 844 CD2 LEU A 105 105.055 73.111 27.044 1.00 42.86 C ANISOU 844 CD2 LEU D 105 5214 5397 5675 -15 -49 3 C ATOM 845 N ALA A 106 108.687 72.515 30.970 1.00 46.49 N ANISOU 845 N ALA D 106 5702 5984 5977 77 -70 30 N ATOM 846 CA ALA A 106 109.256 73.152 32.140 1.00 48.43 C ANISOU 846 CA ALA D 106 6049 6182 6169 56 -7 39 C ATOM 847 C ALA A 106 110.621 73.726 31.820 1.00 51.47 C ANISOU 847 C ALA D 106 6392 6569 6592 -1 -6 25 C ATOM 848 O ALA A 106 111.169 74.493 32.592 1.00 53.20 O ANISOU 848 O ALA D 106 6583 6830 6798 1 104 21 O ATOM 849 CB ALA A 106 109.343 72.179 33.291 1.00 48.83 C ANISOU 849 CB ALA D 106 6110 6185 6258 9 -17 14 C ATOM 850 N ALA A 107 111.155 73.341 30.667 1.00 53.46 N ANISOU 850 N ALA D 107 6619 6893 6798 -15 -36 0 N ATOM 851 CA ALA A 107 112.574 73.482 30.394 1.00 54.77 C ANISOU 851 CA ALA D 107 6852 6995 6963 17 -10 16 C ATOM 852 C ALA A 107 112.722 74.632 29.435 1.00 55.91 C ANISOU 852 C ALA D 107 6927 7130 7187 36 -37 -27 C ATOM 853 O ALA A 107 113.670 75.393 29.503 1.00 56.85 O ANISOU 853 O ALA D 107 7064 7138 7397 87 -27 -27 O ATOM 854 CB ALA A 107 113.106 72.233 29.775 1.00 55.26 C ANISOU 854 CB ALA D 107 6893 7078 7024 60 12 -17 C ATOM 855 N GLU A 108 111.746 74.757 28.546 1.00 56.20 N ANISOU 855 N GLU D 108 7022 7116 7213 48 -44 -55 N ATOM 856 CA GLU A 108 111.526 75.998 27.835 1.00 55.93 C ANISOU 856 CA GLU D 108 7021 7106 7121 22 -38 1 C ATOM 857 C GLU A 108 110.730 77.023 28.589 1.00 54.57 C ANISOU 857 C GLU D 108 6696 7028 7008 -49 -30 -50 C ATOM 858 O GLU A 108 110.350 78.037 28.032 1.00 53.66 O ANISOU 858 O GLU D 108 6320 7058 7009 -79 3 -76 O ATOM 859 CB GLU A 108 110.862 75.732 26.518 1.00 56.80 C ANISOU 859 CB GLU D 108 7141 7226 7213 -32 13 15 C ATOM 860 CG GLU A 108 111.136 74.353 25.997 1.00 56.87 C ANISOU 860 CG GLU D 108 7079 7251 7277 -4 -23 -28 C ATOM 861 CD GLU A 108 110.722 74.258 24.568 1.00 58.55 C ANISOU 861 CD GLU D 108 7479 7455 7310 -24 35 19 C ATOM 862 OE1 GLU A 108 109.556 74.566 24.303 1.00 62.28 O ANISOU 862 OE1 GLU D 108 7752 8095 7816 70 -64 134 O ATOM 863 OE2 GLU A 108 111.565 73.915 23.729 1.00 63.22 O ANISOU 863 OE2 GLU D 108 7897 8320 7801 -92 131 -35 O ATOM 864 N HIS A 109 110.492 76.774 29.862 1.00 53.45 N ANISOU 864 N HIS D 109 6577 6825 6906 -54 13 36 N ATOM 865 CA HIS A 109 109.729 77.714 30.641 1.00 52.53 C ANISOU 865 CA HIS D 109 6514 6694 6748 -53 57 -1 C ATOM 866 C HIS A 109 108.524 78.195 29.843 1.00 51.14 C ANISOU 866 C HIS D 109 6317 6426 6686 -56 -25 42 C ATOM 867 O HIS A 109 108.254 79.388 29.769 1.00 51.74 O ANISOU 867 O HIS D 109 6309 6494 6854 -127 -75 -43 O ATOM 868 CB HIS A 109 110.620 78.890 31.024 1.00 54.76 C ANISOU 868 CB HIS D 109 6915 6867 7022 -103 -43 41 C ATOM 869 CG HIS A 109 111.722 78.520 31.964 1.00 59.17 C ANISOU 869 CG HIS D 109 7378 7552 7552 -3 152 -37 C ATOM 870 ND1 HIS A 109 113.038 78.429 31.570 1.00 62.06 N ANISOU 870 ND1 HIS D 109 7588 7979 8010 95 35 -30 N ATOM 871 CD2 HIS A 109 111.698 78.188 33.275 1.00 61.85 C ANISOU 871 CD2 HIS D 109 7817 8008 7672 -16 -12 0 C ATOM 872 CE1 HIS A 109 113.779 78.071 32.601 1.00 63.03 C ANISOU 872 CE1 HIS D 109 7744 8145 8058 75 41 11 C ATOM 873 NE2 HIS A 109 112.990 77.915 33.647 1.00 63.38 N ANISOU 873 NE2 HIS D 109 7899 8193 7989 82 20 -29 N ATOM 874 N LEU A 110 107.801 77.251 29.248 1.00 48.16 N ANISOU 874 N LEU D 110 5923 6088 6287 38 -59 51 N ATOM 875 CA LEU A 110 106.415 77.464 28.885 1.00 45.84 C ANISOU 875 CA LEU D 110 5763 5770 5884 -9 -116 -2 C ATOM 876 C LEU A 110 105.460 76.929 29.943 1.00 44.02 C ANISOU 876 C LEU D 110 5477 5529 5720 4 -79 -6 C ATOM 877 O LEU A 110 105.497 75.761 30.290 1.00 44.34 O ANISOU 877 O LEU D 110 5391 5583 5871 -55 -145 -86 O ATOM 878 CB LEU A 110 106.110 76.804 27.560 1.00 45.64 C ANISOU 878 CB LEU D 110 5733 5810 5797 35 -14 -70 C ATOM 879 CG LEU A 110 106.810 77.389 26.355 1.00 45.72 C ANISOU 879 CG LEU D 110 5680 5792 5897 -30 -125 -61 C ATOM 880 CD1 LEU A 110 106.404 76.608 25.157 1.00 45.76 C ANISOU 880 CD1 LEU D 110 5619 5762 6004 -48 -39 -17 C ATOM 881 CD2 LEU A 110 106.392 78.831 26.215 1.00 46.63 C ANISOU 881 CD2 LEU D 110 5732 5842 6143 -36 -186 -25 C ATOM 882 N THR A 111 104.620 77.812 30.455 1.00 41.27 N ANISOU 882 N THR D 111 5063 5215 5403 -46 -43 -67 N ATOM 883 CA THR A 111 103.556 77.431 31.372 1.00 39.18 C ANISOU 883 CA THR D 111 4808 4919 5159 -16 97 -11 C ATOM 884 C THR A 111 102.198 77.811 30.762 1.00 36.93 C ANISOU 884 C THR D 111 4422 4540 5070 -44 54 31 C ATOM 885 O THR A 111 101.872 79.002 30.677 1.00 35.44 O ANISOU 885 O THR D 111 3964 4364 5135 -120 48 208 O ATOM 886 CB THR A 111 103.745 78.074 32.737 1.00 39.68 C ANISOU 886 CB THR D 111 4934 4950 5192 -22 43 -1 C ATOM 887 OG1 THR A 111 104.988 77.631 33.288 1.00 41.29 O ANISOU 887 OG1 THR D 111 5027 5153 5507 -76 -9 -72 O ATOM 888 CG2 THR A 111 102.641 77.664 33.678 1.00 40.48 C ANISOU 888 CG2 THR D 111 5024 5124 5232 -40 -34 38 C ATOM 889 N PRO A 112 101.420 76.794 30.301 1.00 34.58 N ANISOU 889 N PRO D 112 4175 4287 4675 25 63 13 N ATOM 890 CA PRO A 112 100.069 77.094 29.774 1.00 32.42 C ANISOU 890 CA PRO D 112 4008 4017 4293 -30 -106 -4 C ATOM 891 C PRO A 112 99.192 77.535 30.946 1.00 30.34 C ANISOU 891 C PRO D 112 3608 3770 4149 -106 -86 -107 C ATOM 892 O PRO A 112 99.404 77.076 32.057 1.00 28.74 O ANISOU 892 O PRO D 112 3182 3683 4052 -172 -121 -97 O ATOM 893 CB PRO A 112 99.606 75.770 29.127 1.00 32.42 C ANISOU 893 CB PRO D 112 3935 4171 4212 -56 -126 -104 C ATOM 894 CG PRO A 112 100.549 74.720 29.579 1.00 33.28 C ANISOU 894 CG PRO D 112 4163 4131 4350 -53 -43 0 C ATOM 895 CD PRO A 112 101.736 75.353 30.276 1.00 33.90 C ANISOU 895 CD PRO D 112 4123 4255 4502 -46 14 23 C ATOM 896 N GLU A 113 98.261 78.466 30.707 1.00 28.50 N ANISOU 896 N GLU D 113 3413 3476 3939 -247 -219 -106 N ATOM 897 CA GLU A 113 97.447 78.984 31.786 1.00 26.74 C ANISOU 897 CA GLU D 113 3307 3231 3622 -201 -91 -120 C ATOM 898 C GLU A 113 96.598 77.827 32.368 1.00 24.24 C ANISOU 898 C GLU D 113 2947 3077 3186 -149 -118 -133 C ATOM 899 O GLU A 113 96.295 77.800 33.570 1.00 24.81 O ANISOU 899 O GLU D 113 3055 3022 3347 -232 116 -201 O ATOM 900 CB GLU A 113 96.528 80.076 31.254 1.00 28.02 C ANISOU 900 CB GLU D 113 3540 3394 3712 -175 -152 -184 C ATOM 901 CG GLU A 113 97.183 81.482 31.126 1.00 26.90 C ANISOU 901 CG GLU D 113 3284 3139 3797 -153 -108 -115 C ATOM 902 CD GLU A 113 98.095 81.650 29.906 1.00 30.97 C ANISOU 902 CD GLU D 113 3953 3946 3867 3 -156 -37 C ATOM 903 OE1 GLU A 113 98.272 80.715 29.092 1.00 29.29 O ANISOU 903 OE1 GLU D 113 3509 3186 4434 -308 -289 -166 O ATOM 904 OE2 GLU A 113 98.637 82.770 29.763 1.00 37.29 O ANISOU 904 OE2 GLU D 113 4418 4548 5202 -377 -170 -61 O ATOM 905 N TYR A 114 96.190 76.936 31.476 1.00 23.52 N ANISOU 905 N TYR D 114 2826 3018 3089 -180 -181 -123 N ATOM 906 CA TYR A 114 95.278 75.819 31.768 1.00 22.61 C ANISOU 906 CA TYR D 114 2920 2894 2774 -117 -89 -94 C ATOM 907 C TYR A 114 95.756 74.501 31.159 1.00 22.91 C ANISOU 907 C TYR D 114 2712 3038 2954 41 -113 -130 C ATOM 908 O TYR A 114 96.031 74.407 29.942 1.00 20.81 O ANISOU 908 O TYR D 114 2356 2756 2791 117 -199 201 O ATOM 909 CB TYR A 114 93.840 76.116 31.281 1.00 22.60 C ANISOU 909 CB TYR D 114 2870 2964 2750 -189 -188 -193 C ATOM 910 CG TYR A 114 93.206 77.323 31.919 1.00 23.18 C ANISOU 910 CG TYR D 114 2962 2954 2888 19 22 -136 C ATOM 911 CD1 TYR A 114 92.546 77.228 33.149 1.00 22.86 C ANISOU 911 CD1 TYR D 114 2898 2951 2835 -192 -257 115 C ATOM 912 CD2 TYR A 114 93.316 78.576 31.341 1.00 26.60 C ANISOU 912 CD2 TYR D 114 2987 3168 3952 -180 -298 -140 C ATOM 913 CE1 TYR A 114 91.990 78.368 33.768 1.00 23.67 C ANISOU 913 CE1 TYR D 114 2626 3162 3206 154 -85 -152 C ATOM 914 CE2 TYR A 114 92.745 79.712 31.951 1.00 25.69 C ANISOU 914 CE2 TYR D 114 3415 2976 3369 -216 -116 144 C ATOM 915 CZ TYR A 114 92.100 79.599 33.163 1.00 26.00 C ANISOU 915 CZ TYR D 114 2942 3140 3795 -106 -239 60 C ATOM 916 OH TYR A 114 91.567 80.731 33.762 1.00 26.26 O ANISOU 916 OH TYR D 114 3205 2970 3802 -13 -20 170 O ATOM 917 N ILE A 115 95.800 73.469 32.011 1.00 23.30 N ANISOU 917 N ILE D 115 2562 2998 3290 25 5 -87 N ATOM 918 CA ILE A 115 96.000 72.109 31.526 1.00 23.11 C ANISOU 918 CA ILE D 115 2807 2919 3053 -81 -63 2 C ATOM 919 C ILE A 115 94.850 71.193 31.995 1.00 22.75 C ANISOU 919 C ILE D 115 2710 3050 2884 -38 -119 -65 C ATOM 920 O ILE A 115 94.578 71.081 33.198 1.00 21.17 O ANISOU 920 O ILE D 115 2230 3089 2725 -4 -217 -251 O ATOM 921 CB ILE A 115 97.324 71.509 32.009 1.00 23.53 C ANISOU 921 CB ILE D 115 2801 2938 3200 -39 -35 25 C ATOM 922 CG1 ILE A 115 98.514 72.378 31.597 1.00 23.87 C ANISOU 922 CG1 ILE D 115 2960 2831 3277 36 14 24 C ATOM 923 CG2 ILE A 115 97.509 70.062 31.473 1.00 24.16 C ANISOU 923 CG2 ILE D 115 2798 3078 3303 48 -64 13 C ATOM 924 CD1 ILE A 115 99.824 71.980 32.355 1.00 25.78 C ANISOU 924 CD1 ILE D 115 3004 3340 3450 -47 -30 -13 C ATOM 925 N THR A 116 94.225 70.531 31.034 1.00 20.55 N ANISOU 925 N THR D 116 2540 2839 2426 -116 -21 -65 N ATOM 926 CA THR A 116 93.179 69.534 31.280 1.00 22.07 C ANISOU 926 CA THR D 116 2788 2877 2719 -45 -48 -72 C ATOM 927 C THR A 116 93.691 68.102 31.049 1.00 20.73 C ANISOU 927 C THR D 116 2632 2688 2555 30 -69 5 C ATOM 928 O THR A 116 94.050 67.701 29.941 1.00 20.58 O ANISOU 928 O THR D 116 2556 2750 2512 91 -163 -4 O ATOM 929 CB THR A 116 91.923 69.813 30.412 1.00 19.35 C ANISOU 929 CB THR D 116 2628 2597 2126 -27 -121 -243 C ATOM 930 OG1 THR A 116 91.398 71.091 30.764 1.00 20.38 O ANISOU 930 OG1 THR D 116 2715 2707 2320 4 -488 -100 O ATOM 931 CG2 THR A 116 90.820 68.772 30.582 1.00 19.33 C ANISOU 931 CG2 THR D 116 2651 2600 2094 -18 198 -22 C ATOM 932 N ILE A 117 93.700 67.333 32.121 1.00 20.52 N ANISOU 932 N ILE D 117 2532 2815 2450 -9 -67 -51 N ATOM 933 CA ILE A 117 94.014 65.916 32.059 1.00 22.89 C ANISOU 933 CA ILE D 117 2970 2950 2777 50 -29 -91 C ATOM 934 C ILE A 117 92.741 65.186 31.624 1.00 23.37 C ANISOU 934 C ILE D 117 3051 2906 2920 17 -41 -80 C ATOM 935 O ILE A 117 91.761 65.158 32.362 1.00 23.30 O ANISOU 935 O ILE D 117 3097 2522 3231 -56 -151 -207 O ATOM 936 CB ILE A 117 94.465 65.380 33.446 1.00 21.81 C ANISOU 936 CB ILE D 117 2994 2862 2430 -63 -74 -31 C ATOM 937 CG1 ILE A 117 95.702 66.130 33.945 1.00 23.84 C ANISOU 937 CG1 ILE D 117 2968 3363 2728 118 -79 -135 C ATOM 938 CG2 ILE A 117 94.675 63.851 33.369 1.00 20.89 C ANISOU 938 CG2 ILE D 117 2672 2817 2448 177 -280 -160 C ATOM 939 CD1 ILE A 117 96.046 65.789 35.411 1.00 23.38 C ANISOU 939 CD1 ILE D 117 2854 3201 2827 49 139 -3 C ATOM 940 N ASP A 118 92.715 64.615 30.426 1.00 24.96 N ANISOU 940 N ASP D 118 3221 3067 3193 39 -80 -1 N ATOM 941 CA AASP A 118 91.458 64.167 29.847 0.50 26.06 C ANISOU 941 CA AASP D 118 3354 3254 3290 -2 22 4 C ATOM 942 C ASP A 118 91.436 62.644 29.610 1.00 26.24 C ANISOU 942 C ASP D 118 3398 3222 3349 3 -28 -51 C ATOM 943 O ASP A 118 91.960 62.180 28.638 1.00 24.45 O ANISOU 943 O ASP D 118 3529 2783 2976 -112 -211 -102 O ATOM 944 CB AASP A 118 91.125 65.089 28.625 0.50 27.89 C ANISOU 944 CB AASP D 118 3719 3408 3470 -41 44 -115 C ATOM 945 CG AASP A 118 90.956 64.361 27.293 0.50 26.07 C ANISOU 945 CG AASP D 118 3362 2978 3564 12 -72 22 C ATOM 946 OD1AASP A 118 89.841 63.934 26.986 0.50 25.19 O ANISOU 946 OD1AASP D 118 2953 2953 3662 36 -380 -164 O ATOM 947 OD2AASP A 118 91.897 64.318 26.481 0.50 26.53 O ANISOU 947 OD2AASP D 118 3165 2701 4214 97 -258 -268 O ATOM 948 N ILE A 119 90.825 61.913 30.546 1.00 27.26 N ANISOU 948 N ILE D 119 3300 3465 3590 -23 -89 10 N ATOM 949 CA ILE A 119 90.787 60.460 30.578 1.00 27.01 C ANISOU 949 CA ILE D 119 3374 3415 3471 -51 -71 36 C ATOM 950 C ILE A 119 89.315 59.998 30.824 1.00 27.05 C ANISOU 950 C ILE D 119 3295 3413 3568 -28 -76 156 C ATOM 951 O ILE A 119 88.566 60.632 31.592 1.00 26.64 O ANISOU 951 O ILE D 119 3376 3159 3585 -52 -116 286 O ATOM 952 CB ILE A 119 91.778 59.977 31.708 1.00 28.32 C ANISOU 952 CB ILE D 119 3400 3584 3775 23 -46 -26 C ATOM 953 CG1 ILE A 119 93.246 60.259 31.322 1.00 28.06 C ANISOU 953 CG1 ILE D 119 3518 3623 3520 28 -133 99 C ATOM 954 CG2 ILE A 119 91.588 58.556 32.090 1.00 28.18 C ANISOU 954 CG2 ILE D 119 3378 3420 3907 -128 -175 87 C ATOM 955 CD1 ILE A 119 93.632 59.709 29.946 1.00 31.23 C ANISOU 955 CD1 ILE D 119 4103 4029 3733 51 -124 112 C ATOM 956 N ALA A 120 88.897 58.921 30.157 1.00 25.79 N ANISOU 956 N ALA D 120 3203 3171 3425 56 -73 123 N ATOM 957 CA ALA A 120 87.511 58.449 30.260 1.00 25.05 C ANISOU 957 CA ALA D 120 3190 3114 3212 111 -79 47 C ATOM 958 C ALA A 120 87.155 58.136 31.698 1.00 24.32 C ANISOU 958 C ALA D 120 3093 3046 3101 152 -97 9 C ATOM 959 O ALA A 120 86.127 58.580 32.185 1.00 26.28 O ANISOU 959 O ALA D 120 2935 3419 3628 256 -81 -113 O ATOM 960 CB ALA A 120 87.269 57.226 29.420 1.00 25.31 C ANISOU 960 CB ALA D 120 3328 3301 2987 122 -61 88 C ATOM 961 N HIS A 121 87.999 57.357 32.363 1.00 22.77 N ANISOU 961 N HIS D 121 2795 2845 3010 39 -116 -14 N ATOM 962 CA HIS A 121 87.770 56.929 33.745 1.00 23.05 C ANISOU 962 CA HIS D 121 2924 2906 2925 89 -77 88 C ATOM 963 C HIS A 121 88.867 57.570 34.622 1.00 23.26 C ANISOU 963 C HIS D 121 2911 2915 3011 118 -25 4 C ATOM 964 O HIS A 121 89.904 56.974 34.947 1.00 22.06 O ANISOU 964 O HIS D 121 2784 3024 2572 219 62 7 O ATOM 965 CB HIS A 121 87.711 55.390 33.865 1.00 22.80 C ANISOU 965 CB HIS D 121 2819 3043 2801 -8 -104 -18 C ATOM 966 CG HIS A 121 87.312 54.914 35.228 1.00 21.32 C ANISOU 966 CG HIS D 121 2656 2649 2796 -163 -153 -51 C ATOM 967 ND1 HIS A 121 87.415 53.594 35.627 1.00 24.35 N ANISOU 967 ND1 HIS D 121 3138 3006 3107 1 -52 179 N ATOM 968 CD2 HIS A 121 86.875 55.602 36.314 1.00 15.02 C ANISOU 968 CD2 HIS D 121 1741 1787 2177 -73 373 -65 C ATOM 969 CE1 HIS A 121 86.994 53.483 36.877 1.00 18.62 C ANISOU 969 CE1 HIS D 121 2363 2184 2526 13 2 -288 C ATOM 970 NE2 HIS A 121 86.674 54.689 37.318 1.00 20.20 N ANISOU 970 NE2 HIS D 121 2468 2875 2332 -343 -187 32 N ATOM 971 N GLY A 122 88.619 58.817 34.986 1.00 21.55 N ANISOU 971 N GLY D 122 2883 2654 2648 115 -153 159 N ATOM 972 CA GLY A 122 89.660 59.679 35.527 1.00 22.32 C ANISOU 972 CA GLY D 122 2726 2878 2874 71 -40 0 C ATOM 973 C GLY A 122 89.921 59.509 37.016 1.00 23.88 C ANISOU 973 C GLY D 122 2949 3098 3026 -9 63 -86 C ATOM 974 O GLY A 122 90.924 60.032 37.517 1.00 23.95 O ANISOU 974 O GLY D 122 2923 2977 3197 -125 62 -300 O ATOM 975 N HIS A 123 89.020 58.822 37.736 1.00 23.95 N ANISOU 975 N HIS D 123 2915 3004 3178 -36 13 -75 N ATOM 976 CA HIS A 123 89.275 58.449 39.135 1.00 24.81 C ANISOU 976 CA HIS D 123 3136 3138 3152 -28 -5 19 C ATOM 977 C HIS A 123 90.293 57.287 39.104 1.00 26.13 C ANISOU 977 C HIS D 123 3387 3207 3332 2 -27 -5 C ATOM 978 O HIS A 123 89.913 56.128 39.008 1.00 26.91 O ANISOU 978 O HIS D 123 3687 3150 3386 -99 -331 -52 O ATOM 979 CB HIS A 123 87.969 58.065 39.879 1.00 23.25 C ANISOU 979 CB HIS D 123 3063 2655 3115 -16 25 96 C ATOM 980 CG HIS A 123 88.112 57.936 41.365 1.00 24.25 C ANISOU 980 CG HIS D 123 2999 2820 3391 -77 26 -135 C ATOM 981 ND1 HIS A 123 87.155 57.336 42.162 1.00 24.97 N ANISOU 981 ND1 HIS D 123 3198 3204 3085 9 -38 34 N ATOM 982 CD2 HIS A 123 89.103 58.327 42.201 1.00 23.40 C ANISOU 982 CD2 HIS D 123 3003 2839 3047 208 -33 131 C ATOM 983 CE1 HIS A 123 87.562 57.349 43.415 1.00 24.71 C ANISOU 983 CE1 HIS D 123 3059 2900 3427 30 132 -43 C ATOM 984 NE2 HIS A 123 88.736 57.953 43.466 1.00 25.21 N ANISOU 984 NE2 HIS D 123 2820 3275 3482 88 -127 -236 N ATOM 985 N SER A 124 91.585 57.622 39.115 1.00 28.21 N ANISOU 985 N SER D 124 3549 3541 3628 -45 -22 -54 N ATOM 986 CA SER A 124 92.682 56.624 39.022 1.00 28.99 C ANISOU 986 CA SER D 124 3644 3618 3750 75 -16 -46 C ATOM 987 C SER A 124 94.008 57.159 39.556 1.00 30.47 C ANISOU 987 C SER D 124 3664 3796 4117 125 -37 -119 C ATOM 988 O SER A 124 94.243 58.377 39.619 1.00 29.18 O ANISOU 988 O SER D 124 3399 3514 4174 343 41 -183 O ATOM 989 CB SER A 124 92.899 56.192 37.575 1.00 31.00 C ANISOU 989 CB SER D 124 3951 3868 3959 -40 -53 -20 C ATOM 990 OG SER A 124 93.540 57.217 36.834 1.00 33.98 O ANISOU 990 OG SER D 124 4185 4391 4335 -81 -288 -214 O ATOM 991 N ASN A 125 94.918 56.254 39.921 1.00 31.16 N ANISOU 991 N ASN D 125 3856 3797 4183 79 14 -226 N ATOM 992 CA ASN A 125 96.232 56.728 40.374 1.00 31.40 C ANISOU 992 CA ASN D 125 3906 3894 4129 140 54 -99 C ATOM 993 C ASN A 125 97.050 57.295 39.229 1.00 30.70 C ANISOU 993 C ASN D 125 3797 3708 4160 231 55 -100 C ATOM 994 O ASN A 125 97.932 58.133 39.452 1.00 32.07 O ANISOU 994 O ASN D 125 3961 3715 4508 241 82 -229 O ATOM 995 CB ASN A 125 96.967 55.639 41.141 1.00 33.26 C ANISOU 995 CB ASN D 125 4178 4048 4411 142 59 -191 C ATOM 996 CG ASN A 125 96.326 55.386 42.487 1.00 39.58 C ANISOU 996 CG ASN D 125 5256 5078 4705 99 -20 -75 C ATOM 997 OD1 ASN A 125 96.348 56.254 43.372 1.00 40.87 O ANISOU 997 OD1 ASN D 125 5424 4899 5203 252 276 50 O ATOM 998 ND2 ASN A 125 95.678 54.221 42.630 1.00 45.34 N ANISOU 998 ND2 ASN D 125 5822 5592 5814 -207 84 -127 N ATOM 999 N ALA A 126 96.714 56.870 38.006 1.00 29.89 N ANISOU 999 N ALA D 126 3815 3511 4030 300 -36 -70 N ATOM 1000 CA ALA A 126 97.327 57.411 36.789 1.00 29.92 C ANISOU 1000 CA ALA D 126 3734 3630 4002 140 -52 0 C ATOM 1001 C ALA A 126 97.080 58.908 36.707 1.00 29.34 C ANISOU 1001 C ALA D 126 3550 3603 3993 98 -125 -45 C ATOM 1002 O ALA A 126 97.994 59.669 36.459 1.00 28.50 O ANISOU 1002 O ALA D 126 3199 3643 3984 199 -391 130 O ATOM 1003 CB ALA A 126 96.760 56.741 35.568 1.00 30.67 C ANISOU 1003 CB ALA D 126 3952 3622 4076 193 -13 8 C ATOM 1004 N VAL A 127 95.834 59.318 36.952 1.00 28.80 N ANISOU 1004 N VAL D 127 3407 3616 3918 105 -93 -99 N ATOM 1005 CA VAL A 127 95.462 60.740 36.959 1.00 28.43 C ANISOU 1005 CA VAL D 127 3356 3575 3871 104 -47 -3 C ATOM 1006 C VAL A 127 96.054 61.458 38.178 1.00 28.15 C ANISOU 1006 C VAL D 127 3214 3647 3832 178 26 -41 C ATOM 1007 O VAL A 127 96.581 62.572 38.052 1.00 27.84 O ANISOU 1007 O VAL D 127 3160 3636 3781 166 155 -176 O ATOM 1008 CB VAL A 127 93.906 60.927 36.898 1.00 26.50 C ANISOU 1008 CB VAL D 127 3131 3365 3573 63 -110 30 C ATOM 1009 CG1 VAL A 127 93.499 62.411 37.169 1.00 25.18 C ANISOU 1009 CG1 VAL D 127 3004 3267 3296 -35 139 -95 C ATOM 1010 CG2 VAL A 127 93.368 60.479 35.586 1.00 24.52 C ANISOU 1010 CG2 VAL D 127 2816 3090 3409 28 -240 -149 C ATOM 1011 N ILE A 128 95.994 60.825 39.348 1.00 29.46 N ANISOU 1011 N ILE D 128 3392 3828 3973 75 -46 -62 N ATOM 1012 CA ILE A 128 96.562 61.411 40.565 1.00 30.69 C ANISOU 1012 CA ILE D 128 3755 3886 4017 76 -26 5 C ATOM 1013 C ILE A 128 98.076 61.740 40.410 1.00 30.92 C ANISOU 1013 C ILE D 128 3634 3934 4180 145 60 74 C ATOM 1014 O ILE A 128 98.531 62.838 40.758 1.00 31.21 O ANISOU 1014 O ILE D 128 3397 3933 4526 332 91 -94 O ATOM 1015 CB ILE A 128 96.269 60.513 41.816 1.00 31.14 C ANISOU 1015 CB ILE D 128 3855 3975 4001 71 -79 27 C ATOM 1016 CG1 ILE A 128 94.785 60.620 42.204 1.00 32.78 C ANISOU 1016 CG1 ILE D 128 4092 4041 4322 90 66 -114 C ATOM 1017 CG2 ILE A 128 97.162 60.895 43.003 1.00 31.53 C ANISOU 1017 CG2 ILE D 128 3800 4138 4042 -1 15 8 C ATOM 1018 CD1 ILE A 128 94.154 59.354 42.653 1.00 31.10 C ANISOU 1018 CD1 ILE D 128 3823 4077 3917 77 -82 19 C ATOM 1019 N ASN A 129 98.835 60.808 39.845 1.00 32.57 N ANISOU 1019 N ASN D 129 3869 4114 4391 91 -43 69 N ATOM 1020 CA ASN A 129 100.271 61.000 39.642 1.00 32.50 C ANISOU 1020 CA ASN D 129 3893 4151 4305 89 28 27 C ATOM 1021 C ASN A 129 100.577 62.058 38.588 1.00 33.00 C ANISOU 1021 C ASN D 129 3913 4186 4437 89 83 -10 C ATOM 1022 O ASN A 129 101.523 62.830 38.732 1.00 34.71 O ANISOU 1022 O ASN D 129 3780 4559 4846 289 237 31 O ATOM 1023 CB ASN A 129 100.936 59.663 39.261 1.00 33.28 C ANISOU 1023 CB ASN D 129 4052 4160 4430 91 -85 115 C ATOM 1024 CG ASN A 129 100.923 58.650 40.403 1.00 36.33 C ANISOU 1024 CG ASN D 129 4518 4639 4644 162 33 -13 C ATOM 1025 OD1 ASN A 129 100.875 59.016 41.589 1.00 41.38 O ANISOU 1025 OD1 ASN D 129 5079 5625 5019 213 131 57 O ATOM 1026 ND2 ASN A 129 100.957 57.370 40.054 1.00 36.67 N ANISOU 1026 ND2 ASN D 129 4777 4577 4579 11 1 -137 N ATOM 1027 N MET A 130 99.769 62.126 37.530 1.00 32.84 N ANISOU 1027 N MET D 130 3971 4226 4279 -13 -21 -6 N ATOM 1028 CA MET A 130 99.916 63.211 36.561 1.00 31.93 C ANISOU 1028 CA MET D 130 3853 4116 4160 30 32 -24 C ATOM 1029 C MET A 130 99.611 64.597 37.168 1.00 31.45 C ANISOU 1029 C MET D 130 3702 4082 4165 24 39 -130 C ATOM 1030 O MET A 130 100.318 65.575 36.890 1.00 29.24 O ANISOU 1030 O MET D 130 3177 3789 4144 128 95 -317 O ATOM 1031 CB MET A 130 99.080 62.946 35.315 1.00 32.23 C ANISOU 1031 CB MET D 130 3839 4136 4269 64 -7 -33 C ATOM 1032 CG MET A 130 99.271 64.014 34.226 1.00 31.85 C ANISOU 1032 CG MET D 130 3719 4209 4173 -15 -123 -70 C ATOM 1033 SD MET A 130 101.010 64.289 33.790 1.00 35.23 S ANISOU 1033 SD MET D 130 3413 4940 5030 -27 -122 -172 S ATOM 1034 CE MET A 130 101.230 62.942 32.642 1.00 37.28 C ANISOU 1034 CE MET D 130 4464 4847 4854 -32 -30 -89 C ATOM 1035 N ILE A 131 98.597 64.695 38.025 1.00 30.98 N ANISOU 1035 N ILE D 131 3754 4000 4017 -25 2 -56 N ATOM 1036 CA ILE A 131 98.348 65.956 38.717 1.00 31.86 C ANISOU 1036 CA ILE D 131 3892 4070 4143 -32 38 -36 C ATOM 1037 C ILE A 131 99.610 66.380 39.487 1.00 33.56 C ANISOU 1037 C ILE D 131 4022 4286 4440 -129 102 -77 C ATOM 1038 O ILE A 131 100.049 67.528 39.379 1.00 33.47 O ANISOU 1038 O ILE D 131 3905 4261 4551 -200 24 15 O ATOM 1039 CB ILE A 131 97.146 65.881 39.694 1.00 30.98 C ANISOU 1039 CB ILE D 131 3808 3945 4016 20 89 -22 C ATOM 1040 CG1 ILE A 131 95.839 65.680 38.921 1.00 28.79 C ANISOU 1040 CG1 ILE D 131 3456 3578 3904 88 43 100 C ATOM 1041 CG2 ILE A 131 97.047 67.160 40.503 1.00 30.16 C ANISOU 1041 CG2 ILE D 131 3714 3957 3789 -25 84 -12 C ATOM 1042 CD1 ILE A 131 94.695 65.160 39.757 1.00 29.44 C ANISOU 1042 CD1 ILE D 131 3658 3684 3841 89 73 -39 C ATOM 1043 N GLN A 132 100.162 65.446 40.262 1.00 34.59 N ANISOU 1043 N GLN D 132 4077 4360 4702 -67 95 -52 N ATOM 1044 CA GLN A 132 101.331 65.703 41.122 1.00 35.28 C ANISOU 1044 CA GLN D 132 4364 4531 4507 17 150 -14 C ATOM 1045 C GLN A 132 102.588 66.056 40.322 1.00 34.85 C ANISOU 1045 C GLN D 132 4153 4534 4552 101 154 7 C ATOM 1046 O GLN A 132 103.348 66.953 40.708 1.00 35.53 O ANISOU 1046 O GLN D 132 4180 4685 4633 192 112 54 O ATOM 1047 CB GLN A 132 101.559 64.506 42.043 1.00 35.75 C ANISOU 1047 CB GLN D 132 4477 4525 4580 2 132 14 C ATOM 1048 CG GLN A 132 100.520 64.443 43.160 1.00 39.21 C ANISOU 1048 CG GLN D 132 4899 4946 5051 -29 -71 -42 C ATOM 1049 CD GLN A 132 100.511 63.125 43.910 1.00 40.26 C ANISOU 1049 CD GLN D 132 5233 5092 4970 -52 116 -122 C ATOM 1050 OE1 GLN A 132 101.496 62.385 43.901 1.00 48.73 O ANISOU 1050 OE1 GLN D 132 6007 6234 6271 320 -17 -117 O ATOM 1051 NE2 GLN A 132 99.388 62.818 44.563 1.00 49.39 N ANISOU 1051 NE2 GLN D 132 5963 6652 6151 -19 -196 -74 N ATOM 1052 N HIS A 133 102.769 65.389 39.185 1.00 35.53 N ANISOU 1052 N HIS D 133 4191 4640 4669 96 130 -17 N ATOM 1053 CA HIS A 133 103.847 65.694 38.231 1.00 35.71 C ANISOU 1053 CA HIS D 133 4294 4617 4657 45 110 -79 C ATOM 1054 C HIS A 133 103.716 67.088 37.628 1.00 36.78 C ANISOU 1054 C HIS D 133 4306 4671 4995 34 77 -9 C ATOM 1055 O HIS A 133 104.701 67.844 37.560 1.00 36.71 O ANISOU 1055 O HIS D 133 3937 4857 5152 94 113 40 O ATOM 1056 CB HIS A 133 103.853 64.641 37.123 1.00 34.82 C ANISOU 1056 CB HIS D 133 4247 4470 4513 19 89 -64 C ATOM 1057 CG HIS A 133 104.917 64.822 36.086 1.00 36.51 C ANISOU 1057 CG HIS D 133 4375 4777 4720 29 97 -101 C ATOM 1058 ND1 HIS A 133 106.264 64.854 36.391 1.00 37.34 N ANISOU 1058 ND1 HIS D 133 4424 4899 4864 20 91 -108 N ATOM 1059 CD2 HIS A 133 104.837 64.909 34.736 1.00 36.51 C ANISOU 1059 CD2 HIS D 133 4466 4747 4659 31 64 42 C ATOM 1060 CE1 HIS A 133 106.962 64.987 35.276 1.00 38.12 C ANISOU 1060 CE1 HIS D 133 4602 4951 4928 58 8 -63 C ATOM 1061 NE2 HIS A 133 106.121 65.018 34.256 1.00 39.25 N ANISOU 1061 NE2 HIS D 133 4739 5083 5089 -88 94 -61 N ATOM 1062 N ILE A 134 102.504 67.431 37.173 1.00 35.87 N ANISOU 1062 N ILE D 134 4142 4643 4843 7 54 -74 N ATOM 1063 CA ILE A 134 102.249 68.754 36.618 1.00 36.44 C ANISOU 1063 CA ILE D 134 4286 4688 4872 56 78 -74 C ATOM 1064 C ILE A 134 102.516 69.854 37.635 1.00 35.60 C ANISOU 1064 C ILE D 134 4095 4647 4784 94 176 -87 C ATOM 1065 O ILE A 134 103.131 70.855 37.291 1.00 36.45 O ANISOU 1065 O ILE D 134 3998 4901 4947 92 204 -151 O ATOM 1066 CB ILE A 134 100.800 68.899 36.060 1.00 35.23 C ANISOU 1066 CB ILE D 134 4153 4544 4688 -4 134 -39 C ATOM 1067 CG1 ILE A 134 100.654 68.104 34.754 1.00 35.53 C ANISOU 1067 CG1 ILE D 134 4352 4482 4666 108 60 -32 C ATOM 1068 CG2 ILE A 134 100.475 70.368 35.802 1.00 35.48 C ANISOU 1068 CG2 ILE D 134 4048 4624 4807 48 -21 2 C ATOM 1069 CD1 ILE A 134 99.229 68.000 34.264 1.00 36.52 C ANISOU 1069 CD1 ILE D 134 4424 4654 4795 -31 40 15 C ATOM 1070 N LYS A 135 102.041 69.677 38.868 1.00 36.70 N ANISOU 1070 N LYS D 135 4245 4780 4917 75 150 -119 N ATOM 1071 CA LYS A 135 102.169 70.685 39.901 1.00 39.00 C ANISOU 1071 CA LYS D 135 4775 4940 5104 37 72 -4 C ATOM 1072 C LYS A 135 103.619 70.874 40.358 1.00 41.26 C ANISOU 1072 C LYS D 135 4993 5223 5458 30 100 31 C ATOM 1073 O LYS A 135 103.973 71.924 40.925 1.00 42.22 O ANISOU 1073 O LYS D 135 5081 5419 5540 74 229 53 O ATOM 1074 CB LYS A 135 101.297 70.330 41.109 1.00 39.25 C ANISOU 1074 CB LYS D 135 4826 4955 5129 25 69 -37 C ATOM 1075 CG LYS A 135 99.812 70.644 40.917 1.00 39.24 C ANISOU 1075 CG LYS D 135 4789 5015 5106 -24 117 -37 C ATOM 1076 CD LYS A 135 99.517 72.139 41.125 1.00 41.44 C ANISOU 1076 CD LYS D 135 5065 5251 5429 -85 130 138 C ATOM 1077 CE LYS A 135 98.208 72.616 40.467 1.00 40.73 C ANISOU 1077 CE LYS D 135 5072 5089 5311 89 110 0 C ATOM 1078 NZ LYS A 135 98.174 74.093 40.216 1.00 39.73 N ANISOU 1078 NZ LYS D 135 4639 4957 5498 -90 33 71 N ATOM 1079 N LYS A 136 104.450 69.861 40.123 1.00 42.05 N ANISOU 1079 N LYS D 136 5119 5300 5557 28 67 24 N ATOM 1080 CA LYS A 136 105.883 69.959 40.424 1.00 42.50 C ANISOU 1080 CA LYS D 136 5203 5409 5536 15 55 16 C ATOM 1081 C LYS A 136 106.636 70.756 39.352 1.00 42.65 C ANISOU 1081 C LYS D 136 5263 5422 5519 15 37 32 C ATOM 1082 O LYS A 136 107.432 71.637 39.675 1.00 43.48 O ANISOU 1082 O LYS D 136 5371 5527 5623 -46 38 60 O ATOM 1083 CB LYS A 136 106.495 68.567 40.611 1.00 43.37 C ANISOU 1083 CB LYS D 136 5346 5507 5625 19 82 4 C ATOM 1084 CG LYS A 136 106.181 67.958 41.986 1.00 45.54 C ANISOU 1084 CG LYS D 136 5673 5810 5817 -2 48 -54 C ATOM 1085 CD LYS A 136 107.078 66.758 42.344 1.00 45.70 C ANISOU 1085 CD LYS D 136 5726 5731 5908 66 60 -37 C ATOM 1086 CE LYS A 136 106.784 65.506 41.500 1.00 49.79 C ANISOU 1086 CE LYS D 136 6335 6183 6399 -51 31 60 C ATOM 1087 NZ LYS A 136 105.632 64.684 41.985 1.00 49.79 N ANISOU 1087 NZ LYS D 136 6192 6377 6347 -11 -60 -57 N ATOM 1088 N HIS A 137 106.366 70.468 38.086 1.00 41.82 N ANISOU 1088 N HIS D 137 5155 5307 5425 17 108 8 N ATOM 1089 CA HIS A 137 107.120 71.053 36.980 1.00 41.48 C ANISOU 1089 CA HIS D 137 5064 5264 5430 17 44 -25 C ATOM 1090 C HIS A 137 106.529 72.340 36.392 1.00 41.42 C ANISOU 1090 C HIS D 137 5035 5284 5419 -29 20 -94 C ATOM 1091 O HIS A 137 107.260 73.125 35.778 1.00 41.24 O ANISOU 1091 O HIS D 137 4863 5303 5503 32 44 -160 O ATOM 1092 CB HIS A 137 107.310 70.013 35.884 1.00 43.18 C ANISOU 1092 CB HIS D 137 5288 5513 5605 -52 30 35 C ATOM 1093 CG HIS A 137 108.216 68.896 36.292 1.00 47.40 C ANISOU 1093 CG HIS D 137 5914 5878 6217 149 47 -73 C ATOM 1094 ND1 HIS A 137 107.929 68.060 37.352 1.00 48.08 N ANISOU 1094 ND1 HIS D 137 6128 5946 6195 59 -18 -32 N ATOM 1095 CD2 HIS A 137 109.422 68.502 35.814 1.00 48.62 C ANISOU 1095 CD2 HIS D 137 6084 6267 6121 105 -112 -66 C ATOM 1096 CE1 HIS A 137 108.912 67.188 37.496 1.00 48.78 C ANISOU 1096 CE1 HIS D 137 6134 6056 6344 37 37 -148 C ATOM 1097 NE2 HIS A 137 109.826 67.429 36.572 1.00 47.97 N ANISOU 1097 NE2 HIS D 137 5909 6051 6264 200 -45 -20 N ATOM 1098 N LEU A 138 105.223 72.552 36.574 1.00 40.00 N ANISOU 1098 N LEU D 138 4934 5046 5217 -21 -19 -82 N ATOM 1099 CA LEU A 138 104.529 73.726 36.045 1.00 38.90 C ANISOU 1099 CA LEU D 138 4845 4971 4961 -40 7 0 C ATOM 1100 C LEU A 138 103.586 74.265 37.120 1.00 38.38 C ANISOU 1100 C LEU D 138 4787 4955 4839 -46 67 27 C ATOM 1101 O LEU A 138 102.358 74.271 36.953 1.00 37.30 O ANISOU 1101 O LEU D 138 4648 4873 4648 -44 89 68 O ATOM 1102 CB LEU A 138 103.778 73.368 34.748 1.00 37.56 C ANISOU 1102 CB LEU D 138 4718 4758 4793 -84 44 -61 C ATOM 1103 CG LEU A 138 104.613 72.771 33.603 1.00 37.16 C ANISOU 1103 CG LEU D 138 4587 4566 4965 -72 34 -12 C ATOM 1104 CD1 LEU A 138 103.748 72.149 32.546 1.00 35.93 C ANISOU 1104 CD1 LEU D 138 4286 4672 4694 78 -87 -13 C ATOM 1105 CD2 LEU A 138 105.513 73.793 32.910 1.00 37.50 C ANISOU 1105 CD2 LEU D 138 4590 4608 5050 -61 38 -107 C ATOM 1106 N PRO A 139 104.159 74.741 38.243 1.00 38.78 N ANISOU 1106 N PRO D 139 4789 5050 4896 -20 62 54 N ATOM 1107 CA PRO A 139 103.312 75.129 39.366 1.00 37.82 C ANISOU 1107 CA PRO D 139 4674 4902 4794 -22 62 46 C ATOM 1108 C PRO A 139 102.254 76.209 39.070 1.00 37.08 C ANISOU 1108 C PRO D 139 4573 4826 4689 -70 109 49 C ATOM 1109 O PRO A 139 101.242 76.280 39.776 1.00 39.99 O ANISOU 1109 O PRO D 139 4648 5284 5260 -24 229 47 O ATOM 1110 CB PRO A 139 104.323 75.659 40.398 1.00 38.87 C ANISOU 1110 CB PRO D 139 4827 4993 4947 -15 126 40 C ATOM 1111 CG PRO A 139 105.628 75.051 40.005 1.00 38.97 C ANISOU 1111 CG PRO D 139 4852 5121 4833 -56 96 109 C ATOM 1112 CD PRO A 139 105.592 74.978 38.529 1.00 38.58 C ANISOU 1112 CD PRO D 139 4806 5112 4739 -17 45 69 C ATOM 1113 N GLU A 140 102.484 77.059 38.086 1.00 35.55 N ANISOU 1113 N GLU D 140 4246 4649 4610 -120 147 135 N ATOM 1114 CA GLU A 140 101.546 78.133 37.782 1.00 35.40 C ANISOU 1114 CA GLU D 140 4301 4564 4585 -79 97 98 C ATOM 1115 C GLU A 140 100.399 77.698 36.871 1.00 34.35 C ANISOU 1115 C GLU D 140 4148 4375 4526 -76 94 130 C ATOM 1116 O GLU A 140 99.486 78.501 36.625 1.00 33.75 O ANISOU 1116 O GLU D 140 3951 4370 4499 -75 177 344 O ATOM 1117 CB GLU A 140 102.259 79.308 37.111 1.00 37.14 C ANISOU 1117 CB GLU D 140 4436 4786 4888 -15 35 0 C ATOM 1118 CG GLU A 140 103.387 79.884 37.925 1.00 41.93 C ANISOU 1118 CG GLU D 140 5171 5254 5504 -182 228 131 C ATOM 1119 CD GLU A 140 102.893 80.425 39.225 1.00 48.35 C ANISOU 1119 CD GLU D 140 6084 6330 5954 -137 -19 180 C ATOM 1120 OE1 GLU A 140 102.335 81.549 39.223 1.00 54.44 O ANISOU 1120 OE1 GLU D 140 6706 6889 7089 145 161 34 O ATOM 1121 OE2 GLU A 140 103.054 79.724 40.245 1.00 52.88 O ANISOU 1121 OE2 GLU D 140 6797 6485 6808 -120 56 -179 O ATOM 1122 N SER A 141 100.452 76.472 36.338 1.00 32.68 N ANISOU 1122 N SER D 141 3848 4187 4381 -46 57 7 N ATOM 1123 CA SER A 141 99.377 75.987 35.449 1.00 30.60 C ANISOU 1123 CA SER D 141 3708 3939 3979 -50 -28 -22 C ATOM 1124 C SER A 141 98.109 75.619 36.231 1.00 28.97 C ANISOU 1124 C SER D 141 3467 3705 3831 -67 40 -38 C ATOM 1125 O SER A 141 98.183 74.937 37.264 1.00 28.95 O ANISOU 1125 O SER D 141 3424 3677 3898 -76 105 -29 O ATOM 1126 CB SER A 141 99.834 74.783 34.630 1.00 30.58 C ANISOU 1126 CB SER D 141 3697 3890 4032 23 -38 -107 C ATOM 1127 OG SER A 141 100.628 75.163 33.526 1.00 29.54 O ANISOU 1127 OG SER D 141 3676 3744 3805 152 -81 -211 O ATOM 1128 N PHE A 142 96.950 76.069 35.736 1.00 26.39 N ANISOU 1128 N PHE D 142 3193 3280 3553 -71 -44 -80 N ATOM 1129 CA PHE A 142 95.648 75.735 36.365 1.00 26.12 C ANISOU 1129 CA PHE D 142 3228 3252 3445 -16 -21 -5 C ATOM 1130 C PHE A 142 95.219 74.354 35.824 1.00 24.35 C ANISOU 1130 C PHE D 142 2848 3151 3250 -107 64 40 C ATOM 1131 O PHE A 142 95.011 74.189 34.611 1.00 25.61 O ANISOU 1131 O PHE D 142 3112 3259 3360 -30 -201 136 O ATOM 1132 CB PHE A 142 94.604 76.815 36.077 1.00 23.22 C ANISOU 1132 CB PHE D 142 2820 3043 2960 -75 5 3 C ATOM 1133 CG PHE A 142 93.296 76.622 36.803 1.00 25.33 C ANISOU 1133 CG PHE D 142 3125 3098 3400 -70 -7 29 C ATOM 1134 CD1 PHE A 142 92.982 77.392 37.928 1.00 24.63 C ANISOU 1134 CD1 PHE D 142 2853 3200 3304 -96 -256 -16 C ATOM 1135 CD2 PHE A 142 92.367 75.694 36.338 1.00 24.71 C ANISOU 1135 CD2 PHE D 142 2928 3056 3402 24 -60 159 C ATOM 1136 CE1 PHE A 142 91.769 77.229 38.592 1.00 24.18 C ANISOU 1136 CE1 PHE D 142 2762 2879 3544 23 -37 118 C ATOM 1137 CE2 PHE A 142 91.145 75.528 36.979 1.00 23.36 C ANISOU 1137 CE2 PHE D 142 2940 2899 3033 -317 -109 40 C ATOM 1138 CZ PHE A 142 90.838 76.279 38.107 1.00 23.30 C ANISOU 1138 CZ PHE D 142 2575 2923 3354 57 128 222 C ATOM 1139 N VAL A 143 95.136 73.376 36.723 1.00 24.02 N ANISOU 1139 N VAL D 143 2744 3303 3076 -204 -124 70 N ATOM 1140 CA VAL A 143 94.928 71.967 36.363 1.00 23.12 C ANISOU 1140 CA VAL D 143 2660 3076 3046 -92 -182 14 C ATOM 1141 C VAL A 143 93.465 71.498 36.590 1.00 22.87 C ANISOU 1141 C VAL D 143 2637 3072 2978 -160 -68 26 C ATOM 1142 O VAL A 143 92.958 71.498 37.702 1.00 23.58 O ANISOU 1142 O VAL D 143 2273 3226 3459 -174 -391 -136 O ATOM 1143 CB VAL A 143 95.896 71.033 37.119 1.00 23.69 C ANISOU 1143 CB VAL D 143 2828 3200 2972 -217 -157 44 C ATOM 1144 CG1 VAL A 143 95.587 69.568 36.842 1.00 24.38 C ANISOU 1144 CG1 VAL D 143 2885 3067 3309 -112 -31 -84 C ATOM 1145 CG2 VAL A 143 97.367 71.330 36.749 1.00 24.57 C ANISOU 1145 CG2 VAL D 143 2880 3304 3152 21 17 -57 C ATOM 1146 N ILE A 144 92.848 71.047 35.518 1.00 23.41 N ANISOU 1146 N ILE D 144 2683 2917 3294 -100 4 -83 N ATOM 1147 CA ILE A 144 91.457 70.545 35.518 1.00 22.43 C ANISOU 1147 CA ILE D 144 2662 2827 3032 -70 -101 -73 C ATOM 1148 C ILE A 144 91.621 69.047 35.344 1.00 21.81 C ANISOU 1148 C ILE D 144 2738 2657 2891 -46 -160 -115 C ATOM 1149 O ILE A 144 92.312 68.606 34.439 1.00 23.05 O ANISOU 1149 O ILE D 144 3249 2931 2576 -78 -105 -29 O ATOM 1150 CB ILE A 144 90.682 71.120 34.306 1.00 22.56 C ANISOU 1150 CB ILE D 144 2756 2860 2954 47 -82 14 C ATOM 1151 CG1 ILE A 144 90.557 72.651 34.425 1.00 23.72 C ANISOU 1151 CG1 ILE D 144 2825 2966 3219 46 89 -115 C ATOM 1152 CG2 ILE A 144 89.318 70.443 34.136 1.00 21.45 C ANISOU 1152 CG2 ILE D 144 2602 2624 2922 16 -33 130 C ATOM 1153 CD1 ILE A 144 90.391 73.331 33.081 1.00 22.75 C ANISOU 1153 CD1 ILE D 144 2612 2814 3217 -79 -151 -153 C ATOM 1154 N ALA A 145 91.070 68.251 36.242 1.00 21.30 N ANISOU 1154 N ALA D 145 2563 2781 2747 23 -39 -142 N ATOM 1155 CA ALA A 145 91.262 66.799 36.153 1.00 20.26 C ANISOU 1155 CA ALA D 145 2542 2595 2561 -27 -74 -63 C ATOM 1156 C ALA A 145 89.920 66.074 36.033 1.00 20.69 C ANISOU 1156 C ALA D 145 2594 2628 2640 19 13 62 C ATOM 1157 O ALA A 145 88.957 66.386 36.747 1.00 20.85 O ANISOU 1157 O ALA D 145 2445 2556 2919 54 -70 -73 O ATOM 1158 CB ALA A 145 92.015 66.302 37.425 1.00 21.23 C ANISOU 1158 CB ALA D 145 2617 2673 2773 133 92 35 C ATOM 1159 N GLY A 146 89.900 65.029 35.216 1.00 20.74 N ANISOU 1159 N GLY D 146 2607 2829 2442 2 -11 -86 N ATOM 1160 CA GLY A 146 88.716 64.225 35.051 1.00 19.53 C ANISOU 1160 CA GLY D 146 2539 2474 2407 13 -2 -100 C ATOM 1161 C GLY A 146 88.916 63.112 34.058 1.00 20.15 C ANISOU 1161 C GLY D 146 2638 2648 2370 45 -34 -33 C ATOM 1162 O GLY A 146 90.057 62.874 33.595 1.00 20.64 O ANISOU 1162 O GLY D 146 2701 2701 2439 242 -157 149 O ATOM 1163 N ASN A 147 87.845 62.399 33.727 1.00 18.97 N ANISOU 1163 N ASN D 147 2478 2379 2351 24 11 56 N ATOM 1164 CA ASN A 147 86.484 62.671 34.155 1.00 19.59 C ANISOU 1164 CA ASN D 147 2627 2349 2466 25 5 0 C ATOM 1165 C ASN A 147 86.117 61.789 35.348 1.00 20.32 C ANISOU 1165 C ASN D 147 2711 2395 2612 104 79 -4 C ATOM 1166 O ASN A 147 86.574 60.642 35.447 1.00 20.03 O ANISOU 1166 O ASN D 147 2948 2232 2429 188 321 -58 O ATOM 1167 CB ASN A 147 85.490 62.449 32.985 1.00 19.00 C ANISOU 1167 CB ASN D 147 2570 2315 2334 -173 -29 64 C ATOM 1168 CG ASN A 147 85.287 63.693 32.097 1.00 22.43 C ANISOU 1168 CG ASN D 147 2793 2754 2973 66 15 47 C ATOM 1169 OD1 ASN A 147 86.210 64.467 31.868 1.00 24.06 O ANISOU 1169 OD1 ASN D 147 3035 2809 3298 31 22 -67 O ATOM 1170 ND2 ASN A 147 84.056 63.859 31.563 1.00 21.17 N ANISOU 1170 ND2 ASN D 147 2961 2645 2436 23 -58 12 N ATOM 1171 N VAL A 148 85.282 62.326 36.234 1.00 19.35 N ANISOU 1171 N VAL D 148 2641 2249 2462 -18 206 27 N ATOM 1172 CA VAL A 148 84.817 61.639 37.397 1.00 19.48 C ANISOU 1172 CA VAL D 148 2525 2419 2454 0 75 11 C ATOM 1173 C VAL A 148 83.294 61.651 37.507 1.00 19.06 C ANISOU 1173 C VAL D 148 2486 2464 2291 80 130 -62 C ATOM 1174 O VAL A 148 82.617 62.429 36.852 1.00 16.57 O ANISOU 1174 O VAL D 148 2378 2447 1468 93 138 -161 O ATOM 1175 CB VAL A 148 85.451 62.226 38.665 1.00 20.55 C ANISOU 1175 CB VAL D 148 2745 2649 2411 76 121 -53 C ATOM 1176 CG1 VAL A 148 86.962 62.146 38.559 1.00 22.16 C ANISOU 1176 CG1 VAL D 148 2763 2940 2715 -172 -54 -186 C ATOM 1177 CG2 VAL A 148 85.005 63.671 38.935 1.00 20.07 C ANISOU 1177 CG2 VAL D 148 2875 2569 2179 -26 185 -100 C ATOM 1178 N GLY A 149 82.767 60.805 38.384 1.00 19.64 N ANISOU 1178 N GLY D 149 2379 2543 2537 37 247 -135 N ATOM 1179 CA GLY A 149 81.337 60.699 38.558 1.00 20.51 C ANISOU 1179 CA GLY D 149 2576 2568 2646 -44 -5 -112 C ATOM 1180 C GLY A 149 80.842 60.539 39.957 1.00 20.15 C ANISOU 1180 C GLY D 149 2538 2395 2720 14 7 -93 C ATOM 1181 O GLY A 149 79.659 60.347 40.134 1.00 22.78 O ANISOU 1181 O GLY D 149 2691 2865 3096 -187 -157 -188 O ATOM 1182 N THR A 150 81.733 60.659 40.940 1.00 20.48 N ANISOU 1182 N THR D 150 2656 2322 2804 -41 11 -85 N ATOM 1183 CA THR A 150 81.390 60.504 42.319 1.00 20.09 C ANISOU 1183 CA THR D 150 2595 2432 2605 -56 -64 -49 C ATOM 1184 C THR A 150 82.059 61.574 43.186 1.00 20.76 C ANISOU 1184 C THR D 150 2670 2646 2569 -99 -27 1 C ATOM 1185 O THR A 150 83.111 62.121 42.829 1.00 19.31 O ANISOU 1185 O THR D 150 2652 2624 2061 -168 40 -36 O ATOM 1186 CB THR A 150 81.809 59.116 42.920 1.00 19.50 C ANISOU 1186 CB THR D 150 2379 2235 2793 -18 8 -75 C ATOM 1187 OG1 THR A 150 83.223 59.025 43.024 1.00 19.86 O ANISOU 1187 OG1 THR D 150 2219 2297 3027 123 305 -65 O ATOM 1188 CG2 THR A 150 81.285 57.943 42.098 1.00 16.68 C ANISOU 1188 CG2 THR D 150 2451 2074 1811 15 16 -336 C ATOM 1189 N PRO A 151 81.424 61.892 44.327 1.00 21.23 N ANISOU 1189 N PRO D 151 2811 2758 2495 -98 -92 -67 N ATOM 1190 CA PRO A 151 82.031 62.780 45.330 1.00 23.04 C ANISOU 1190 CA PRO D 151 2946 2994 2813 -105 -21 25 C ATOM 1191 C PRO A 151 83.362 62.308 45.945 1.00 23.73 C ANISOU 1191 C PRO D 151 2897 3003 3113 -1 25 -33 C ATOM 1192 O PRO A 151 84.228 63.150 46.253 1.00 24.77 O ANISOU 1192 O PRO D 151 2953 3308 3149 24 181 -181 O ATOM 1193 CB PRO A 151 80.963 62.856 46.445 1.00 23.02 C ANISOU 1193 CB PRO D 151 2952 2996 2799 -48 -91 -33 C ATOM 1194 CG PRO A 151 79.996 61.799 46.161 1.00 19.67 C ANISOU 1194 CG PRO D 151 2639 2731 2103 -122 46 -66 C ATOM 1195 CD PRO A 151 80.036 61.529 44.671 1.00 21.06 C ANISOU 1195 CD PRO D 151 2962 2764 2273 -181 -122 -161 C ATOM 1196 N GLU A 152 83.514 61.003 46.168 1.00 24.22 N ANISOU 1196 N GLU D 152 2930 3202 3068 -91 -98 -139 N ATOM 1197 CA GLU A 152 84.796 60.463 46.628 1.00 24.00 C ANISOU 1197 CA GLU D 152 2972 3082 3062 -40 -64 -49 C ATOM 1198 C GLU A 152 85.887 60.741 45.575 1.00 23.16 C ANISOU 1198 C GLU D 152 2977 2918 2901 -1 -80 -18 C ATOM 1199 O GLU A 152 87.012 61.066 45.926 1.00 23.34 O ANISOU 1199 O GLU D 152 2843 3043 2983 84 -5 -49 O ATOM 1200 CB GLU A 152 84.740 58.967 46.951 1.00 25.19 C ANISOU 1200 CB GLU D 152 3072 3382 3114 9 -46 -164 C ATOM 1201 CG GLU A 152 84.075 58.105 45.948 1.00 30.43 C ANISOU 1201 CG GLU D 152 4076 3751 3735 -4 96 -34 C ATOM 1202 CD GLU A 152 82.559 57.846 46.206 1.00 34.98 C ANISOU 1202 CD GLU D 152 4329 4558 4402 120 -181 -146 C ATOM 1203 OE1 GLU A 152 81.732 58.805 46.338 1.00 27.64 O ANISOU 1203 OE1 GLU D 152 3984 3561 2954 -16 -310 -241 O ATOM 1204 OE2 GLU A 152 82.195 56.643 46.224 1.00 42.72 O ANISOU 1204 OE2 GLU D 152 6004 4963 5265 -160 -57 32 O ATOM 1205 N ALA A 153 85.556 60.632 44.294 1.00 23.37 N ANISOU 1205 N ALA D 153 2958 2836 3085 -5 45 -4 N ATOM 1206 CA ALA A 153 86.543 60.916 43.241 1.00 22.57 C ANISOU 1206 CA ALA D 153 2812 2876 2887 -10 -14 29 C ATOM 1207 C ALA A 153 86.920 62.387 43.191 1.00 21.86 C ANISOU 1207 C ALA D 153 2732 2728 2846 -18 70 121 C ATOM 1208 O ALA A 153 88.103 62.728 43.022 1.00 22.09 O ANISOU 1208 O ALA D 153 2729 2800 2863 41 91 -76 O ATOM 1209 CB ALA A 153 86.030 60.489 41.855 1.00 21.46 C ANISOU 1209 CB ALA D 153 2565 2511 3074 -60 75 155 C ATOM 1210 N VAL A 154 85.921 63.265 43.268 1.00 21.96 N ANISOU 1210 N VAL D 154 2639 2843 2858 -72 163 126 N ATOM 1211 CA VAL A 154 86.189 64.715 43.249 1.00 22.82 C ANISOU 1211 CA VAL D 154 2874 2963 2831 0 92 55 C ATOM 1212 C VAL A 154 87.170 65.035 44.396 1.00 23.77 C ANISOU 1212 C VAL D 154 2914 3157 2958 -58 185 41 C ATOM 1213 O VAL A 154 88.197 65.701 44.194 1.00 23.49 O ANISOU 1213 O VAL D 154 2898 3147 2878 -137 492 21 O ATOM 1214 CB VAL A 154 84.884 65.554 43.367 1.00 20.62 C ANISOU 1214 CB VAL D 154 2810 2685 2338 55 176 116 C ATOM 1215 CG1 VAL A 154 85.208 67.035 43.610 1.00 21.77 C ANISOU 1215 CG1 VAL D 154 2970 2738 2564 -151 72 -246 C ATOM 1216 CG2 VAL A 154 84.006 65.392 42.100 1.00 21.55 C ANISOU 1216 CG2 VAL D 154 2329 3043 2814 113 40 210 C ATOM 1217 N ARG A 155 86.844 64.517 45.576 1.00 24.87 N ANISOU 1217 N ARG D 155 3088 3311 3047 -34 169 36 N ATOM 1218 CA ARG A 155 87.647 64.714 46.800 1.00 26.24 C ANISOU 1218 CA ARG D 155 3307 3404 3258 -13 184 12 C ATOM 1219 C ARG A 155 89.085 64.265 46.634 1.00 25.56 C ANISOU 1219 C ARG D 155 3180 3383 3147 -26 60 54 C ATOM 1220 O ARG A 155 90.017 65.001 46.968 1.00 25.33 O ANISOU 1220 O ARG D 155 3250 3207 3167 -82 1 30 O ATOM 1221 CB ARG A 155 87.063 63.891 47.935 1.00 28.36 C ANISOU 1221 CB ARG D 155 3578 3712 3485 -72 174 -75 C ATOM 1222 CG ARG A 155 85.908 64.474 48.625 1.00 35.72 C ANISOU 1222 CG ARG D 155 4504 4296 4770 117 -71 142 C ATOM 1223 CD ARG A 155 86.290 64.933 50.026 1.00 46.28 C ANISOU 1223 CD ARG D 155 6218 6032 5332 -188 200 -14 C ATOM 1224 NE ARG A 155 85.511 66.124 50.353 1.00 50.18 N ANISOU 1224 NE ARG D 155 6469 6207 6389 183 -205 48 N ATOM 1225 CZ ARG A 155 84.463 66.174 51.168 1.00 50.49 C ANISOU 1225 CZ ARG D 155 6386 6299 6496 25 -114 11 C ATOM 1226 NH1 ARG A 155 84.031 65.100 51.834 1.00 51.69 N ANISOU 1226 NH1 ARG D 155 6696 6333 6611 28 -96 -8 N ATOM 1227 NH2 ARG A 155 83.857 67.338 51.336 1.00 50.79 N ANISOU 1227 NH2 ARG D 155 6470 6353 6473 35 -95 -17 N ATOM 1228 N GLU A 156 89.251 63.047 46.126 1.00 26.67 N ANISOU 1228 N GLU D 156 3285 3351 3497 4 114 20 N ATOM 1229 CA GLU A 156 90.583 62.453 45.936 1.00 26.48 C ANISOU 1229 CA GLU D 156 3288 3376 3396 12 121 -8 C ATOM 1230 C GLU A 156 91.392 63.268 44.934 1.00 26.21 C ANISOU 1230 C GLU D 156 3256 3355 3348 16 167 39 C ATOM 1231 O GLU A 156 92.583 63.506 45.132 1.00 26.98 O ANISOU 1231 O GLU D 156 3152 3424 3674 143 320 -97 O ATOM 1232 CB GLU A 156 90.503 60.972 45.521 1.00 26.11 C ANISOU 1232 CB GLU D 156 3288 3472 3158 31 82 89 C ATOM 1233 CG GLU A 156 91.765 60.156 45.962 1.00 27.62 C ANISOU 1233 CG GLU D 156 3548 3485 3461 73 51 69 C ATOM 1234 CD GLU A 156 91.708 58.656 45.686 1.00 28.59 C ANISOU 1234 CD GLU D 156 3633 3488 3741 91 64 -63 C ATOM 1235 OE1 GLU A 156 90.645 58.148 45.287 1.00 32.83 O ANISOU 1235 OE1 GLU D 156 4037 3826 4609 -108 306 105 O ATOM 1236 OE2 GLU A 156 92.761 57.983 45.863 1.00 30.43 O ANISOU 1236 OE2 GLU D 156 3860 3894 3805 132 354 -66 O ATOM 1237 N LEU A 157 90.744 63.752 43.877 1.00 25.47 N ANISOU 1237 N LEU D 157 3148 3258 3270 2 200 0 N ATOM 1238 CA LEU A 157 91.459 64.526 42.866 1.00 25.54 C ANISOU 1238 CA LEU D 157 3143 3281 3279 21 83 -17 C ATOM 1239 C LEU A 157 91.809 65.938 43.360 1.00 24.76 C ANISOU 1239 C LEU D 157 3090 3354 2963 -81 131 40 C ATOM 1240 O LEU A 157 92.921 66.425 43.107 1.00 23.78 O ANISOU 1240 O LEU D 157 2991 3317 2726 -80 30 -54 O ATOM 1241 CB LEU A 157 90.672 64.572 41.559 1.00 25.47 C ANISOU 1241 CB LEU D 157 3259 3398 3021 43 41 -18 C ATOM 1242 CG LEU A 157 90.959 63.525 40.473 1.00 28.32 C ANISOU 1242 CG LEU D 157 3571 3643 3545 7 142 50 C ATOM 1243 CD1 LEU A 157 91.187 62.122 40.949 1.00 32.34 C ANISOU 1243 CD1 LEU D 157 4447 3874 3965 -145 108 -23 C ATOM 1244 CD2 LEU A 157 89.916 63.603 39.400 1.00 24.61 C ANISOU 1244 CD2 LEU D 157 2898 3242 3210 -83 -91 -3 C ATOM 1245 N GLU A 158 90.865 66.587 44.045 1.00 25.74 N ANISOU 1245 N GLU D 158 3163 3327 3291 -83 147 9 N ATOM 1246 CA GLU A 158 91.110 67.884 44.671 1.00 27.46 C ANISOU 1246 CA GLU D 158 3423 3480 3528 -21 53 67 C ATOM 1247 C GLU A 158 92.274 67.770 45.669 1.00 30.06 C ANISOU 1247 C GLU D 158 3671 3818 3931 -91 76 9 C ATOM 1248 O GLU A 158 93.222 68.563 45.638 1.00 30.65 O ANISOU 1248 O GLU D 158 3732 3777 4135 -212 138 81 O ATOM 1249 CB GLU A 158 89.840 68.370 45.373 1.00 27.58 C ANISOU 1249 CB GLU D 158 3375 3420 3682 -93 108 66 C ATOM 1250 CG GLU A 158 88.747 68.870 44.382 1.00 24.78 C ANISOU 1250 CG GLU D 158 3007 2971 3435 -215 70 -5 C ATOM 1251 CD GLU A 158 87.565 69.491 45.080 1.00 25.75 C ANISOU 1251 CD GLU D 158 3321 3269 3192 -104 98 82 C ATOM 1252 OE1 GLU A 158 87.552 69.486 46.346 1.00 26.93 O ANISOU 1252 OE1 GLU D 158 3406 3622 3202 -193 -305 -90 O ATOM 1253 OE2 GLU A 158 86.665 70.032 44.382 1.00 25.66 O ANISOU 1253 OE2 GLU D 158 2945 3807 2997 275 -252 40 O ATOM 1254 N ASN A 159 92.196 66.769 46.541 1.00 31.05 N ANISOU 1254 N ASN D 159 3782 3863 4152 6 59 1 N ATOM 1255 CA ASN A 159 93.248 66.494 47.495 1.00 31.52 C ANISOU 1255 CA ASN D 159 3945 4041 3990 19 130 32 C ATOM 1256 C ASN A 159 94.627 66.205 46.811 1.00 31.54 C ANISOU 1256 C ASN D 159 3932 4096 3955 -21 144 77 C ATOM 1257 O ASN A 159 95.658 66.627 47.326 1.00 33.36 O ANISOU 1257 O ASN D 159 4060 4321 4294 -65 96 175 O ATOM 1258 CB ASN A 159 92.802 65.373 48.451 1.00 33.45 C ANISOU 1258 CB ASN D 159 4090 4336 4281 -33 135 41 C ATOM 1259 CG ASN A 159 91.677 65.813 49.428 1.00 39.60 C ANISOU 1259 CG ASN D 159 5014 5064 4966 -84 -174 -136 C ATOM 1260 OD1 ASN A 159 91.342 67.007 49.544 1.00 45.84 O ANISOU 1260 OD1 ASN D 159 6201 5400 5815 265 -123 101 O ATOM 1261 ND2 ASN A 159 91.093 64.834 50.136 1.00 36.92 N ANISOU 1261 ND2 ASN D 159 4562 4824 4639 -155 68 -130 N ATOM 1262 N ALA A 160 94.658 65.557 45.637 1.00 30.92 N ANISOU 1262 N ALA D 160 3788 4013 3947 -39 78 -31 N ATOM 1263 CA ALA A 160 95.919 65.329 44.917 1.00 30.28 C ANISOU 1263 CA ALA D 160 3765 3889 3849 46 155 16 C ATOM 1264 C ALA A 160 96.540 66.617 44.383 1.00 30.62 C ANISOU 1264 C ALA D 160 3706 3948 3977 43 125 0 C ATOM 1265 O ALA A 160 97.719 66.619 44.009 1.00 32.31 O ANISOU 1265 O ALA D 160 3774 4231 4270 154 218 14 O ATOM 1266 CB ALA A 160 95.742 64.319 43.743 1.00 29.76 C ANISOU 1266 CB ALA D 160 3708 3696 3903 86 156 63 C ATOM 1267 N GLY A 161 95.758 67.698 44.326 1.00 28.70 N ANISOU 1267 N GLY D 161 3368 3759 3775 69 223 -46 N ATOM 1268 CA GLY A 161 96.227 68.985 43.827 1.00 28.45 C ANISOU 1268 CA GLY D 161 3338 3759 3711 -7 144 -5 C ATOM 1269 C GLY A 161 95.484 69.581 42.630 1.00 28.83 C ANISOU 1269 C GLY D 161 3449 3664 3840 -19 147 -44 C ATOM 1270 O GLY A 161 95.865 70.648 42.136 1.00 29.83 O ANISOU 1270 O GLY D 161 3488 3754 4089 -197 102 -64 O ATOM 1271 N ALA A 162 94.441 68.925 42.121 1.00 27.58 N ANISOU 1271 N ALA D 162 3299 3517 3663 -16 129 -50 N ATOM 1272 CA ALA A 162 93.707 69.520 40.977 1.00 26.10 C ANISOU 1272 CA ALA D 162 3103 3327 3487 -16 130 60 C ATOM 1273 C ALA A 162 93.124 70.867 41.373 1.00 24.07 C ANISOU 1273 C ALA D 162 2715 3248 3182 -115 222 46 C ATOM 1274 O ALA A 162 92.674 71.007 42.488 1.00 22.59 O ANISOU 1274 O ALA D 162 2434 3201 2946 -80 332 434 O ATOM 1275 CB ALA A 162 92.598 68.573 40.499 1.00 27.51 C ANISOU 1275 CB ALA D 162 3250 3391 3809 -14 187 -5 C ATOM 1276 N ASP A 163 93.123 71.853 40.476 1.00 23.53 N ANISOU 1276 N ASP D 163 2738 3056 3146 -83 93 15 N ATOM 1277 CA ASP A 163 92.432 73.145 40.753 1.00 23.22 C ANISOU 1277 CA ASP D 163 2728 3015 3079 -57 56 87 C ATOM 1278 C ASP A 163 90.938 73.156 40.338 1.00 21.48 C ANISOU 1278 C ASP D 163 2571 2730 2860 2 123 85 C ATOM 1279 O ASP A 163 90.184 74.077 40.672 1.00 20.50 O ANISOU 1279 O ASP D 163 2288 2646 2854 -227 215 242 O ATOM 1280 CB ASP A 163 93.163 74.290 40.073 1.00 23.99 C ANISOU 1280 CB ASP D 163 2875 3076 3164 108 -26 84 C ATOM 1281 CG ASP A 163 94.607 74.356 40.475 1.00 24.55 C ANISOU 1281 CG ASP D 163 2982 3439 2906 -166 119 231 C ATOM 1282 OD1 ASP A 163 94.847 74.623 41.687 1.00 25.39 O ANISOU 1282 OD1 ASP D 163 2467 3905 3272 -529 624 210 O ATOM 1283 OD2 ASP A 163 95.473 74.094 39.604 1.00 27.59 O ANISOU 1283 OD2 ASP D 163 2859 3882 3739 -417 -240 -104 O ATOM 1284 N ALA A 164 90.538 72.140 39.589 1.00 20.31 N ANISOU 1284 N ALA D 164 2415 2514 2785 -70 113 70 N ATOM 1285 CA ALA A 164 89.133 71.903 39.245 1.00 21.94 C ANISOU 1285 CA ALA D 164 2598 2717 3019 -31 22 51 C ATOM 1286 C ALA A 164 88.977 70.456 38.812 1.00 22.18 C ANISOU 1286 C ALA D 164 2607 2733 3086 -79 -6 185 C ATOM 1287 O ALA A 164 89.964 69.808 38.485 1.00 21.67 O ANISOU 1287 O ALA D 164 2472 2403 3355 -77 -7 350 O ATOM 1288 CB ALA A 164 88.705 72.794 38.121 1.00 21.07 C ANISOU 1288 CB ALA D 164 2496 2787 2721 -85 39 -31 C ATOM 1289 N THR A 165 87.738 69.967 38.799 1.00 22.01 N ANISOU 1289 N THR D 165 2593 2828 2939 -28 75 155 N ATOM 1290 CA THR A 165 87.440 68.630 38.295 1.00 20.74 C ANISOU 1290 CA THR D 165 2546 2605 2728 20 28 78 C ATOM 1291 C THR A 165 86.384 68.683 37.195 1.00 19.42 C ANISOU 1291 C THR D 165 2347 2486 2543 -16 98 85 C ATOM 1292 O THR A 165 85.545 69.601 37.165 1.00 18.94 O ANISOU 1292 O THR D 165 2009 2591 2594 -116 196 198 O ATOM 1293 CB THR A 165 86.982 67.643 39.389 1.00 20.96 C ANISOU 1293 CB THR D 165 2641 2712 2609 40 -43 134 C ATOM 1294 OG1 THR A 165 85.794 68.113 40.036 1.00 20.37 O ANISOU 1294 OG1 THR D 165 2594 2415 2730 -193 132 607 O ATOM 1295 CG2 THR A 165 88.091 67.415 40.409 1.00 18.97 C ANISOU 1295 CG2 THR D 165 2424 2240 2543 255 -126 134 C ATOM 1296 N LYS A 166 86.433 67.716 36.288 1.00 18.61 N ANISOU 1296 N LYS D 166 2228 2359 2482 93 -123 -79 N ATOM 1297 CA LYS A 166 85.436 67.629 35.225 1.00 18.74 C ANISOU 1297 CA LYS D 166 2398 2308 2412 -55 -59 28 C ATOM 1298 C LYS A 166 84.546 66.401 35.439 1.00 18.65 C ANISOU 1298 C LYS D 166 2514 2263 2308 -39 -111 -67 C ATOM 1299 O LYS A 166 85.043 65.262 35.522 1.00 19.58 O ANISOU 1299 O LYS D 166 2808 2219 2410 -215 70 -165 O ATOM 1300 CB LYS A 166 86.100 67.629 33.832 1.00 19.08 C ANISOU 1300 CB LYS D 166 2409 2352 2487 12 -105 -249 C ATOM 1301 CG LYS A 166 85.132 67.673 32.673 1.00 17.49 C ANISOU 1301 CG LYS D 166 2110 2015 2520 -203 -86 43 C ATOM 1302 CD LYS A 166 85.575 68.582 31.526 1.00 19.21 C ANISOU 1302 CD LYS D 166 2478 2329 2490 -102 -93 50 C ATOM 1303 CE LYS A 166 86.694 67.985 30.651 1.00 19.42 C ANISOU 1303 CE LYS D 166 2253 2481 2641 -243 -62 107 C ATOM 1304 NZ LYS A 166 86.410 66.641 30.131 1.00 20.42 N ANISOU 1304 NZ LYS D 166 2530 2759 2468 -107 -465 35 N ATOM 1305 N VAL A 167 83.247 66.658 35.533 1.00 17.92 N ANISOU 1305 N VAL D 167 2309 2189 2309 -79 111 -77 N ATOM 1306 CA VAL A 167 82.257 65.668 36.005 1.00 17.81 C ANISOU 1306 CA VAL D 167 2330 2130 2306 6 -16 -143 C ATOM 1307 C VAL A 167 81.341 65.191 34.872 1.00 17.14 C ANISOU 1307 C VAL D 167 2293 2086 2132 -80 -40 -116 C ATOM 1308 O VAL A 167 80.716 66.015 34.137 1.00 14.48 O ANISOU 1308 O VAL D 167 1989 1999 1514 -120 374 143 O ATOM 1309 CB VAL A 167 81.422 66.233 37.223 1.00 19.87 C ANISOU 1309 CB VAL D 167 2638 2238 2672 45 -20 -134 C ATOM 1310 CG1 VAL A 167 80.252 65.305 37.601 1.00 18.75 C ANISOU 1310 CG1 VAL D 167 2416 2460 2248 151 35 -320 C ATOM 1311 CG2 VAL A 167 82.289 66.461 38.400 1.00 21.14 C ANISOU 1311 CG2 VAL D 167 2846 2269 2915 71 0 -139 C ATOM 1312 N GLY A 168 81.257 63.862 34.727 1.00 17.71 N ANISOU 1312 N GLY D 168 2526 2232 1968 76 -43 39 N ATOM 1313 CA GLY A 168 80.483 63.215 33.635 1.00 18.84 C ANISOU 1313 CA GLY D 168 2442 2332 2381 -68 42 -71 C ATOM 1314 C GLY A 168 81.165 61.939 33.173 1.00 18.72 C ANISOU 1314 C GLY D 168 2427 2567 2116 -84 -4 137 C ATOM 1315 O GLY A 168 82.338 61.970 32.832 1.00 19.11 O ANISOU 1315 O GLY D 168 2544 2467 2247 -169 -53 222 O ATOM 1316 N ILE A 169 80.445 60.811 33.219 1.00 19.09 N ANISOU 1316 N ILE D 169 2446 2505 2302 -49 19 -47 N ATOM 1317 CA ILE A 169 80.944 59.519 32.773 1.00 20.99 C ANISOU 1317 CA ILE D 169 2719 2625 2632 -32 -42 -9 C ATOM 1318 C ILE A 169 79.889 58.920 31.830 1.00 22.43 C ANISOU 1318 C ILE D 169 2838 2705 2977 -32 -70 52 C ATOM 1319 O ILE A 169 78.892 58.349 32.265 1.00 20.78 O ANISOU 1319 O ILE D 169 2737 2255 2900 -62 -23 233 O ATOM 1320 CB ILE A 169 81.211 58.563 33.947 1.00 20.76 C ANISOU 1320 CB ILE D 169 2678 2380 2828 -64 24 -96 C ATOM 1321 CG1 ILE A 169 82.228 59.140 34.951 1.00 22.26 C ANISOU 1321 CG1 ILE D 169 3027 2449 2979 -67 -142 4 C ATOM 1322 CG2 ILE A 169 81.670 57.227 33.434 1.00 21.69 C ANISOU 1322 CG2 ILE D 169 2563 2792 2885 -50 -2 22 C ATOM 1323 CD1 ILE A 169 83.661 59.080 34.511 1.00 25.65 C ANISOU 1323 CD1 ILE D 169 3124 3124 3495 -57 2 48 C ATOM 1324 N GLY A 170 80.110 59.100 30.535 1.00 23.73 N ANISOU 1324 N GLY D 170 3018 3001 2995 -2 -21 7 N ATOM 1325 CA GLY A 170 79.145 58.721 29.497 1.00 25.13 C ANISOU 1325 CA GLY D 170 3145 3145 3255 -48 86 19 C ATOM 1326 C GLY A 170 77.768 59.315 29.799 1.00 25.96 C ANISOU 1326 C GLY D 170 3192 3317 3352 31 77 12 C ATOM 1327 O GLY A 170 76.818 58.570 30.077 1.00 25.00 O ANISOU 1327 O GLY D 170 3148 3178 3170 12 370 205 O ATOM 1328 N PRO A 171 77.673 60.660 29.798 1.00 26.57 N ANISOU 1328 N PRO D 171 3332 3344 3417 28 169 -48 N ATOM 1329 CA PRO A 171 76.472 61.350 30.249 1.00 28.88 C ANISOU 1329 CA PRO D 171 3661 3565 3745 32 27 20 C ATOM 1330 C PRO A 171 75.281 61.222 29.296 1.00 31.15 C ANISOU 1330 C PRO D 171 3931 3891 4012 9 35 39 C ATOM 1331 O PRO A 171 74.133 61.320 29.737 1.00 32.93 O ANISOU 1331 O PRO D 171 4101 4165 4245 -4 -198 148 O ATOM 1332 CB PRO A 171 76.919 62.809 30.333 1.00 29.22 C ANISOU 1332 CB PRO D 171 3745 3605 3749 24 63 70 C ATOM 1333 CG PRO A 171 77.992 62.930 29.339 1.00 28.94 C ANISOU 1333 CG PRO D 171 3719 3494 3783 -60 40 47 C ATOM 1334 CD PRO A 171 78.721 61.607 29.385 1.00 26.99 C ANISOU 1334 CD PRO D 171 3456 3543 3254 139 114 -258 C ATOM 1335 N GLY A 172 75.532 61.012 28.009 1.00 31.96 N ANISOU 1335 N GLY D 172 4076 3999 4065 35 -31 97 N ATOM 1336 CA GLY A 172 74.436 60.910 27.046 1.00 32.68 C ANISOU 1336 CA GLY D 172 4144 4110 4163 33 76 44 C ATOM 1337 C GLY A 172 73.558 59.684 27.248 1.00 33.76 C ANISOU 1337 C GLY D 172 4165 4316 4347 7 -24 -23 C ATOM 1338 O GLY A 172 74.023 58.625 27.685 1.00 34.04 O ANISOU 1338 O GLY D 172 4122 4299 4511 48 -107 58 O ATOM 1339 N LYS A 173 72.284 59.820 26.880 1.00 35.23 N ANISOU 1339 N LYS D 173 4336 4444 4606 49 -19 -8 N ATOM 1340 CA LYS A 173 71.265 58.803 27.188 1.00 35.88 C ANISOU 1340 CA LYS D 173 4412 4526 4694 -28 13 -24 C ATOM 1341 C LYS A 173 71.488 57.550 26.371 1.00 37.10 C ANISOU 1341 C LYS D 173 4522 4739 4834 -37 -13 -2 C ATOM 1342 O LYS A 173 71.022 56.481 26.732 1.00 39.28 O ANISOU 1342 O LYS D 173 4780 4952 5190 -7 -43 -167 O ATOM 1343 CB LYS A 173 69.847 59.295 26.875 1.00 36.59 C ANISOU 1343 CB LYS D 173 4505 4564 4831 24 -38 48 C ATOM 1344 CG LYS A 173 69.453 60.679 27.388 1.00 37.50 C ANISOU 1344 CG LYS D 173 4751 4737 4758 -69 1 42 C ATOM 1345 CD LYS A 173 69.174 60.698 28.849 1.00 35.90 C ANISOU 1345 CD LYS D 173 4506 4511 4624 47 -84 155 C ATOM 1346 CE LYS A 173 68.261 61.859 29.205 1.00 31.94 C ANISOU 1346 CE LYS D 173 3812 4078 4243 -8 106 -120 C ATOM 1347 NZ LYS A 173 68.018 61.795 30.653 1.00 29.63 N ANISOU 1347 NZ LYS D 173 3659 3722 3874 152 43 118 N ATOM 1348 N VAL A 174 72.176 57.673 25.246 1.00 37.06 N ANISOU 1348 N VAL D 174 4607 4781 4693 -57 44 4 N ATOM 1349 CA VAL A 174 72.429 56.514 24.393 1.00 36.63 C ANISOU 1349 CA VAL D 174 4556 4683 4678 -7 29 47 C ATOM 1350 C VAL A 174 73.874 56.461 23.899 1.00 35.94 C ANISOU 1350 C VAL D 174 4549 4618 4488 28 10 103 C ATOM 1351 O VAL A 174 74.153 55.973 22.804 1.00 35.93 O ANISOU 1351 O VAL D 174 4691 4573 4384 106 63 161 O ATOM 1352 CB VAL A 174 71.419 56.488 23.219 1.00 37.82 C ANISOU 1352 CB VAL D 174 4773 4816 4778 10 70 -22 C ATOM 1353 CG1 VAL A 174 70.019 56.344 23.771 1.00 39.03 C ANISOU 1353 CG1 VAL D 174 4748 5039 5041 46 110 -103 C ATOM 1354 CG2 VAL A 174 71.510 57.761 22.371 1.00 39.54 C ANISOU 1354 CG2 VAL D 174 5126 4941 4955 -16 -40 -3 C ATOM 1355 N CYS A 175 74.801 56.922 24.727 1.00 34.45 N ANISOU 1355 N CYS D 175 4359 4453 4277 28 11 142 N ATOM 1356 CA CYS A 175 76.208 56.917 24.363 1.00 33.48 C ANISOU 1356 CA CYS D 175 4288 4266 4165 -13 -2 53 C ATOM 1357 C CYS A 175 76.830 55.530 24.539 1.00 31.82 C ANISOU 1357 C CYS D 175 4067 4106 3917 -63 17 108 C ATOM 1358 O CYS A 175 76.244 54.639 25.153 1.00 29.60 O ANISOU 1358 O CYS D 175 3807 3759 3678 -6 -26 315 O ATOM 1359 CB CYS A 175 76.969 57.965 25.184 1.00 33.92 C ANISOU 1359 CB CYS D 175 4305 4265 4316 -79 -48 56 C ATOM 1360 SG CYS A 175 77.216 57.535 26.938 1.00 33.91 S ANISOU 1360 SG CYS D 175 4043 4286 4552 -119 -51 220 S ATOM 1361 N ILE A 176 78.042 55.368 24.021 1.00 32.85 N ANISOU 1361 N ILE D 176 4257 4115 4110 17 -107 -10 N ATOM 1362 CA ILE A 176 78.752 54.089 24.036 1.00 32.33 C ANISOU 1362 CA ILE D 176 4179 4047 4054 -8 -71 -42 C ATOM 1363 C ILE A 176 78.988 53.501 25.417 1.00 30.86 C ANISOU 1363 C ILE D 176 3995 3810 3919 -78 -150 -16 C ATOM 1364 O ILE A 176 78.722 52.309 25.646 1.00 30.49 O ANISOU 1364 O ILE D 176 4001 3538 4045 -64 -260 -137 O ATOM 1365 CB ILE A 176 80.145 54.228 23.334 1.00 33.99 C ANISOU 1365 CB ILE D 176 4303 4270 4342 81 -90 -20 C ATOM 1366 CG1 ILE A 176 79.948 54.577 21.863 1.00 36.80 C ANISOU 1366 CG1 ILE D 176 4727 4718 4536 148 -82 34 C ATOM 1367 CG2 ILE A 176 80.991 52.955 23.481 1.00 34.66 C ANISOU 1367 CG2 ILE D 176 4422 4344 4403 89 -27 -43 C ATOM 1368 CD1 ILE A 176 78.766 53.887 21.217 1.00 38.89 C ANISOU 1368 CD1 ILE D 176 4985 4992 4798 -46 -6 135 C ATOM 1369 N THR A 177 79.536 54.319 26.303 1.00 27.89 N ANISOU 1369 N THR D 177 3566 3452 3578 -148 -182 -36 N ATOM 1370 CA THR A 177 79.866 53.895 27.642 1.00 28.30 C ANISOU 1370 CA THR D 177 3547 3523 3680 -100 -43 42 C ATOM 1371 C THR A 177 78.660 53.271 28.346 1.00 24.70 C ANISOU 1371 C THR D 177 3261 3183 2938 -36 -63 75 C ATOM 1372 O THR A 177 78.760 52.159 28.854 1.00 21.89 O ANISOU 1372 O THR D 177 2905 2903 2510 1 41 168 O ATOM 1373 CB THR A 177 80.441 55.065 28.457 1.00 29.05 C ANISOU 1373 CB THR D 177 3658 3629 3750 -105 -59 53 C ATOM 1374 OG1 THR A 177 81.604 55.529 27.779 1.00 31.51 O ANISOU 1374 OG1 THR D 177 3667 3830 4475 -380 -36 96 O ATOM 1375 CG2 THR A 177 80.814 54.619 29.880 1.00 27.93 C ANISOU 1375 CG2 THR D 177 3613 3402 3596 -94 -37 38 C ATOM 1376 N LYS A 178 77.523 53.974 28.334 1.00 24.25 N ANISOU 1376 N LYS D 178 3317 3045 2849 -21 146 -37 N ATOM 1377 CA LYS A 178 76.277 53.483 28.934 1.00 25.65 C ANISOU 1377 CA LYS D 178 3384 3248 3112 -39 37 -10 C ATOM 1378 C LYS A 178 75.869 52.134 28.346 1.00 25.33 C ANISOU 1378 C LYS D 178 3338 3292 2992 -89 10 -18 C ATOM 1379 O LYS A 178 75.620 51.153 29.073 1.00 26.08 O ANISOU 1379 O LYS D 178 3616 3198 3092 -151 71 159 O ATOM 1380 CB LYS A 178 75.167 54.521 28.709 1.00 26.80 C ANISOU 1380 CB LYS D 178 3506 3353 3322 -134 -32 -37 C ATOM 1381 CG LYS A 178 73.853 54.221 29.334 1.00 27.94 C ANISOU 1381 CG LYS D 178 3603 3538 3472 72 -25 -97 C ATOM 1382 CD LYS A 178 72.800 55.137 28.771 1.00 29.73 C ANISOU 1382 CD LYS D 178 3722 3754 3820 146 54 -73 C ATOM 1383 CE LYS A 178 71.392 54.822 29.290 1.00 34.80 C ANISOU 1383 CE LYS D 178 4029 4623 4567 -71 -138 -28 C ATOM 1384 NZ LYS A 178 71.014 53.379 29.327 1.00 37.09 N ANISOU 1384 NZ LYS D 178 4662 4584 4846 70 133 19 N ATOM 1385 N ILE A 179 75.812 52.080 27.019 1.00 25.05 N ANISOU 1385 N ILE D 179 3244 3269 3004 -154 -49 57 N ATOM 1386 CA ILE A 179 75.347 50.894 26.355 1.00 24.90 C ANISOU 1386 CA ILE D 179 3265 3252 2942 -58 -6 22 C ATOM 1387 C ILE A 179 76.291 49.712 26.538 1.00 24.15 C ANISOU 1387 C ILE D 179 3166 3208 2799 -107 24 -9 C ATOM 1388 O ILE A 179 75.852 48.594 26.790 1.00 23.84 O ANISOU 1388 O ILE D 179 3359 3068 2630 -121 44 -273 O ATOM 1389 CB ILE A 179 75.162 51.114 24.831 1.00 25.71 C ANISOU 1389 CB ILE D 179 3464 3370 2933 -66 -11 5 C ATOM 1390 CG1 ILE A 179 74.244 52.311 24.510 1.00 29.29 C ANISOU 1390 CG1 ILE D 179 3516 3707 3907 -58 48 40 C ATOM 1391 CG2 ILE A 179 74.637 49.838 24.207 1.00 25.92 C ANISOU 1391 CG2 ILE D 179 3293 3357 3196 -26 -23 148 C ATOM 1392 CD1 ILE A 179 72.927 52.345 25.220 1.00 34.05 C ANISOU 1392 CD1 ILE D 179 4238 4404 4294 -53 -161 -75 C ATOM 1393 N LYS A 180 77.587 49.937 26.386 1.00 22.89 N ANISOU 1393 N LYS D 180 2947 2960 2788 -94 -79 2 N ATOM 1394 CA LYS A 180 78.500 48.810 26.349 1.00 23.72 C ANISOU 1394 CA LYS D 180 3079 3041 2892 -79 -32 -68 C ATOM 1395 C LYS A 180 78.961 48.314 27.734 1.00 21.71 C ANISOU 1395 C LYS D 180 2860 2818 2569 -85 -115 -87 C ATOM 1396 O LYS A 180 79.269 47.121 27.876 1.00 20.23 O ANISOU 1396 O LYS D 180 2906 2719 2061 -180 -302 23 O ATOM 1397 CB LYS A 180 79.698 49.119 25.438 1.00 26.47 C ANISOU 1397 CB LYS D 180 3338 3324 3395 92 -200 18 C ATOM 1398 CG LYS A 180 79.338 49.217 23.948 1.00 29.09 C ANISOU 1398 CG LYS D 180 3857 3949 3247 33 96 -150 C ATOM 1399 CD LYS A 180 78.396 48.066 23.512 1.00 36.28 C ANISOU 1399 CD LYS D 180 4875 4579 4330 -152 39 -9 C ATOM 1400 CE LYS A 180 78.274 47.891 21.960 1.00 37.44 C ANISOU 1400 CE LYS D 180 5060 4888 4274 0 153 220 C ATOM 1401 NZ LYS A 180 77.513 48.999 21.287 1.00 40.84 N ANISOU 1401 NZ LYS D 180 5278 5459 4781 232 8 -62 N ATOM 1402 N THR A 181 79.008 49.198 28.736 1.00 19.88 N ANISOU 1402 N THR D 181 2614 2478 2460 -39 -180 -184 N ATOM 1403 CA THR A 181 79.546 48.816 30.057 1.00 20.78 C ANISOU 1403 CA THR D 181 2647 2552 2694 -15 6 16 C ATOM 1404 C THR A 181 78.529 48.758 31.201 1.00 18.36 C ANISOU 1404 C THR D 181 2316 2185 2475 -59 33 30 C ATOM 1405 O THR A 181 78.796 48.125 32.199 1.00 19.31 O ANISOU 1405 O THR D 181 2335 2228 2773 -125 -87 142 O ATOM 1406 CB THR A 181 80.671 49.766 30.537 1.00 20.65 C ANISOU 1406 CB THR D 181 2474 2397 2973 -32 -77 -87 C ATOM 1407 OG1 THR A 181 80.109 51.007 30.989 1.00 20.61 O ANISOU 1407 OG1 THR D 181 2631 2462 2736 -211 -56 182 O ATOM 1408 CG2 THR A 181 81.698 49.986 29.446 1.00 22.49 C ANISOU 1408 CG2 THR D 181 3136 2690 2717 55 69 -71 C ATOM 1409 N GLY A 182 77.402 49.461 31.072 1.00 19.13 N ANISOU 1409 N GLY D 182 2305 2420 2542 -57 -9 111 N ATOM 1410 CA GLY A 182 76.414 49.581 32.135 1.00 18.58 C ANISOU 1410 CA GLY D 182 2404 2344 2308 -97 60 -53 C ATOM 1411 C GLY A 182 76.753 50.584 33.226 1.00 18.57 C ANISOU 1411 C GLY D 182 2267 2347 2440 -55 15 21 C ATOM 1412 O GLY A 182 76.008 50.693 34.207 1.00 17.58 O ANISOU 1412 O GLY D 182 1978 2673 2029 -96 359 -23 O ATOM 1413 N PHE A 183 77.873 51.307 33.070 1.00 17.77 N ANISOU 1413 N PHE D 183 2124 2257 2368 -146 -97 55 N ATOM 1414 CA PHE A 183 78.367 52.247 34.088 1.00 18.39 C ANISOU 1414 CA PHE D 183 2269 2328 2388 -71 -37 -5 C ATOM 1415 C PHE A 183 78.240 53.686 33.595 1.00 19.77 C ANISOU 1415 C PHE D 183 2570 2386 2555 -58 -39 3 C ATOM 1416 O PHE A 183 78.397 53.977 32.402 1.00 20.08 O ANISOU 1416 O PHE D 183 3108 2157 2363 -20 -118 313 O ATOM 1417 CB PHE A 183 79.874 52.015 34.373 1.00 17.57 C ANISOU 1417 CB PHE D 183 2356 2182 2138 -75 134 6 C ATOM 1418 CG PHE A 183 80.147 50.894 35.296 1.00 16.64 C ANISOU 1418 CG PHE D 183 1794 2245 2281 -101 7 40 C ATOM 1419 CD1 PHE A 183 80.313 51.131 36.662 1.00 17.68 C ANISOU 1419 CD1 PHE D 183 2044 2262 2410 -120 -17 52 C ATOM 1420 CD2 PHE A 183 80.187 49.592 34.822 1.00 18.67 C ANISOU 1420 CD2 PHE D 183 2601 2072 2418 -83 -57 -103 C ATOM 1421 CE1 PHE A 183 80.551 50.095 37.536 1.00 16.77 C ANISOU 1421 CE1 PHE D 183 1826 2199 2347 -118 339 -68 C ATOM 1422 CE2 PHE A 183 80.433 48.536 35.689 1.00 18.75 C ANISOU 1422 CE2 PHE D 183 2655 2023 2444 12 396 -136 C ATOM 1423 CZ PHE A 183 80.589 48.781 37.044 1.00 17.19 C ANISOU 1423 CZ PHE D 183 2530 1898 2101 322 104 30 C ATOM 1424 N GLY A 184 78.060 54.577 34.545 1.00 20.39 N ANISOU 1424 N GLY D 184 2479 2369 2898 135 -223 -33 N ATOM 1425 CA GLY A 184 78.308 55.993 34.361 1.00 21.62 C ANISOU 1425 CA GLY D 184 2596 2531 3085 56 -148 6 C ATOM 1426 C GLY A 184 77.115 56.859 34.755 1.00 20.01 C ANISOU 1426 C GLY D 184 2429 2347 2825 116 -239 95 C ATOM 1427 O GLY A 184 76.179 56.388 35.414 1.00 20.19 O ANISOU 1427 O GLY D 184 2762 2069 2836 118 -519 181 O ATOM 1428 N THR A 185 77.167 58.115 34.334 1.00 18.03 N ANISOU 1428 N THR D 185 2267 2310 2271 -62 -129 92 N ATOM 1429 CA THR A 185 76.147 59.117 34.667 1.00 19.84 C ANISOU 1429 CA THR D 185 2526 2324 2689 3 -24 56 C ATOM 1430 C THR A 185 75.063 59.290 33.610 1.00 20.03 C ANISOU 1430 C THR D 185 2601 2333 2674 -125 -22 112 C ATOM 1431 O THR A 185 74.196 60.158 33.722 1.00 19.63 O ANISOU 1431 O THR D 185 2544 2264 2649 -118 196 25 O ATOM 1432 CB THR A 185 76.803 60.485 34.933 1.00 20.44 C ANISOU 1432 CB THR D 185 2430 2392 2944 -7 -42 12 C ATOM 1433 OG1 THR A 185 77.508 60.905 33.761 1.00 17.95 O ANISOU 1433 OG1 THR D 185 2205 2019 2594 113 -80 566 O ATOM 1434 CG2 THR A 185 77.695 60.423 36.189 1.00 22.61 C ANISOU 1434 CG2 THR D 185 2572 2719 3298 57 -278 -37 C ATOM 1435 N GLY A 186 75.070 58.414 32.612 1.00 19.74 N ANISOU 1435 N GLY D 186 2655 2610 2232 -117 -107 37 N ATOM 1436 CA GLY A 186 74.108 58.511 31.504 1.00 20.80 C ANISOU 1436 CA GLY D 186 2678 2528 2694 -44 47 60 C ATOM 1437 C GLY A 186 72.697 58.323 32.008 1.00 21.05 C ANISOU 1437 C GLY D 186 2727 2614 2657 -29 44 138 C ATOM 1438 O GLY A 186 72.410 57.361 32.722 1.00 24.25 O ANISOU 1438 O GLY D 186 2932 2806 3472 -292 -112 202 O ATOM 1439 N GLY A 187 71.838 59.275 31.681 1.00 20.20 N ANISOU 1439 N GLY D 187 2629 2528 2517 -49 77 122 N ATOM 1440 CA GLY A 187 70.474 59.265 32.157 1.00 20.54 C ANISOU 1440 CA GLY D 187 2593 2474 2735 -68 162 49 C ATOM 1441 C GLY A 187 70.188 59.849 33.517 1.00 20.77 C ANISOU 1441 C GLY D 187 2597 2554 2740 -66 65 -74 C ATOM 1442 O GLY A 187 69.007 59.911 33.880 1.00 21.13 O ANISOU 1442 O GLY D 187 2546 2408 3074 -186 79 -94 O ATOM 1443 N TRP A 188 71.242 60.282 34.256 1.00 19.86 N ANISOU 1443 N TRP D 188 2482 2350 2711 25 178 -135 N ATOM 1444 CA TRP A 188 71.098 61.041 35.508 1.00 18.67 C ANISOU 1444 CA TRP D 188 2293 2198 2602 -37 140 -57 C ATOM 1445 C TRP A 188 72.220 62.092 35.732 1.00 17.74 C ANISOU 1445 C TRP D 188 2262 2061 2414 12 51 13 C ATOM 1446 O TRP A 188 72.621 62.342 36.880 1.00 14.40 O ANISOU 1446 O TRP D 188 2030 1526 1914 -75 278 -209 O ATOM 1447 CB TRP A 188 71.004 60.114 36.739 1.00 19.52 C ANISOU 1447 CB TRP D 188 2423 2423 2570 -116 27 -25 C ATOM 1448 CG TRP A 188 72.227 59.258 36.988 1.00 18.38 C ANISOU 1448 CG TRP D 188 2559 1982 2442 -103 -97 -173 C ATOM 1449 CD1 TRP A 188 72.726 58.290 36.169 1.00 19.43 C ANISOU 1449 CD1 TRP D 188 2476 2480 2422 -49 -164 -189 C ATOM 1450 CD2 TRP A 188 73.081 59.285 38.149 1.00 20.17 C ANISOU 1450 CD2 TRP D 188 2725 2139 2797 -148 80 38 C ATOM 1451 NE1 TRP A 188 73.827 57.717 36.750 1.00 20.46 N ANISOU 1451 NE1 TRP D 188 2665 2484 2623 168 -252 -12 N ATOM 1452 CE2 TRP A 188 74.088 58.325 37.947 1.00 20.42 C ANISOU 1452 CE2 TRP D 188 2739 2420 2599 -91 121 -185 C ATOM 1453 CE3 TRP A 188 73.099 60.051 39.331 1.00 20.26 C ANISOU 1453 CE3 TRP D 188 2717 2611 2371 -12 97 -7 C ATOM 1454 CZ2 TRP A 188 75.129 58.103 38.883 1.00 19.85 C ANISOU 1454 CZ2 TRP D 188 2686 2303 2553 -58 143 84 C ATOM 1455 CZ3 TRP A 188 74.113 59.823 40.263 1.00 20.28 C ANISOU 1455 CZ3 TRP D 188 2822 2321 2559 120 33 7 C ATOM 1456 CH2 TRP A 188 75.110 58.859 40.037 1.00 18.95 C ANISOU 1456 CH2 TRP D 188 2434 2342 2423 -68 -108 -217 C ATOM 1457 N GLN A 189 72.699 62.687 34.640 1.00 18.21 N ANISOU 1457 N GLN D 189 2261 2081 2574 99 165 -16 N ATOM 1458 CA GLN A 189 73.843 63.592 34.678 1.00 17.47 C ANISOU 1458 CA GLN D 189 2138 2095 2404 24 58 -24 C ATOM 1459 C GLN A 189 73.617 64.762 35.611 1.00 17.47 C ANISOU 1459 C GLN D 189 2090 2048 2500 68 37 -31 C ATOM 1460 O GLN A 189 74.521 65.105 36.410 1.00 17.00 O ANISOU 1460 O GLN D 189 1942 1961 2554 -31 13 -69 O ATOM 1461 CB GLN A 189 74.239 64.043 33.260 1.00 18.98 C ANISOU 1461 CB GLN D 189 2391 2245 2573 74 -40 22 C ATOM 1462 CG GLN A 189 75.293 65.174 33.206 1.00 20.19 C ANISOU 1462 CG GLN D 189 2515 2473 2682 -41 38 96 C ATOM 1463 CD GLN A 189 76.672 64.787 33.770 1.00 22.29 C ANISOU 1463 CD GLN D 189 2780 2771 2917 60 49 -81 C ATOM 1464 OE1 GLN A 189 76.979 63.612 33.932 1.00 23.24 O ANISOU 1464 OE1 GLN D 189 3081 2690 3058 -91 -323 -430 O ATOM 1465 NE2 GLN A 189 77.521 65.791 34.023 1.00 20.24 N ANISOU 1465 NE2 GLN D 189 2301 2693 2695 168 315 -37 N ATOM 1466 N LEU A 190 72.425 65.358 35.598 1.00 17.72 N ANISOU 1466 N LEU D 190 1931 2184 2616 -108 85 30 N ATOM 1467 CA LEU A 190 72.194 66.502 36.519 1.00 17.42 C ANISOU 1467 CA LEU D 190 2074 2093 2451 -60 27 2 C ATOM 1468 C LEU A 190 72.272 66.162 38.015 1.00 16.72 C ANISOU 1468 C LEU D 190 1959 1917 2475 -7 86 -20 C ATOM 1469 O LEU A 190 72.842 66.904 38.808 1.00 16.34 O ANISOU 1469 O LEU D 190 1792 1781 2636 183 22 -24 O ATOM 1470 CB LEU A 190 70.889 67.232 36.208 1.00 18.17 C ANISOU 1470 CB LEU D 190 2200 2090 2612 -41 -129 -111 C ATOM 1471 CG LEU A 190 70.748 68.614 36.840 1.00 18.06 C ANISOU 1471 CG LEU D 190 2106 2365 2389 -72 -4 118 C ATOM 1472 CD1 LEU A 190 71.946 69.552 36.594 1.00 18.36 C ANISOU 1472 CD1 LEU D 190 2263 2060 2651 80 49 -133 C ATOM 1473 CD2 LEU A 190 69.484 69.267 36.354 1.00 18.85 C ANISOU 1473 CD2 LEU D 190 2346 2097 2717 3 87 84 C ATOM 1474 N ALA A 191 71.661 65.045 38.404 1.00 16.76 N ANISOU 1474 N ALA D 191 2234 1911 2222 -158 -10 -54 N ATOM 1475 CA ALA A 191 71.705 64.603 39.790 1.00 17.50 C ANISOU 1475 CA ALA D 191 2270 2061 2318 -96 10 35 C ATOM 1476 C ALA A 191 73.123 64.187 40.170 1.00 16.94 C ANISOU 1476 C ALA D 191 2252 2049 2134 -185 84 10 C ATOM 1477 O ALA A 191 73.546 64.424 41.298 1.00 17.78 O ANISOU 1477 O ALA D 191 2614 2185 1954 -350 135 52 O ATOM 1478 CB ALA A 191 70.703 63.482 40.022 1.00 18.32 C ANISOU 1478 CB ALA D 191 2340 2120 2500 -115 -90 65 C ATOM 1479 N ALA A 192 73.854 63.577 39.233 1.00 16.83 N ANISOU 1479 N ALA D 192 2076 2161 2156 -165 41 -119 N ATOM 1480 CA ALA A 192 75.268 63.226 39.429 1.00 16.45 C ANISOU 1480 CA ALA D 192 2127 2166 1957 -50 38 36 C ATOM 1481 C ALA A 192 76.096 64.487 39.696 1.00 16.31 C ANISOU 1481 C ALA D 192 2032 2158 2008 54 81 71 C ATOM 1482 O ALA A 192 76.947 64.501 40.573 1.00 16.76 O ANISOU 1482 O ALA D 192 2110 2158 2098 -25 423 575 O ATOM 1483 CB ALA A 192 75.827 62.461 38.177 1.00 16.58 C ANISOU 1483 CB ALA D 192 2023 2075 2201 -1 15 86 C ATOM 1484 N LEU A 193 75.829 65.543 38.944 1.00 15.58 N ANISOU 1484 N LEU D 193 2072 2018 1827 -18 33 -73 N ATOM 1485 CA LEU A 193 76.506 66.840 39.110 1.00 16.98 C ANISOU 1485 CA LEU D 193 2173 2196 2081 0 37 82 C ATOM 1486 C LEU A 193 76.240 67.431 40.498 1.00 16.46 C ANISOU 1486 C LEU D 193 2262 2126 1865 -8 -60 85 C ATOM 1487 O LEU A 193 77.147 67.894 41.164 1.00 17.38 O ANISOU 1487 O LEU D 193 2209 2474 1921 46 -73 100 O ATOM 1488 CB LEU A 193 76.016 67.846 38.073 1.00 14.32 C ANISOU 1488 CB LEU D 193 1944 1915 1582 -113 -284 -53 C ATOM 1489 CG LEU A 193 76.502 69.287 38.228 1.00 16.03 C ANISOU 1489 CG LEU D 193 2128 2024 1938 0 -56 -15 C ATOM 1490 CD1 LEU A 193 78.038 69.377 38.170 1.00 19.18 C ANISOU 1490 CD1 LEU D 193 2423 2341 2522 -69 119 -200 C ATOM 1491 CD2 LEU A 193 75.830 70.210 37.230 1.00 16.27 C ANISOU 1491 CD2 LEU D 193 2047 2152 1981 -31 -104 31 C ATOM 1492 N ARG A 194 74.979 67.464 40.875 1.00 18.98 N ANISOU 1492 N ARG D 194 2486 2295 2430 -47 -27 102 N ATOM 1493 CA ARG A 194 74.592 67.908 42.218 1.00 20.22 C ANISOU 1493 CA ARG D 194 2635 2586 2462 16 -34 116 C ATOM 1494 C ARG A 194 75.342 67.144 43.335 1.00 20.23 C ANISOU 1494 C ARG D 194 2614 2501 2570 -19 -2 132 C ATOM 1495 O ARG A 194 75.874 67.733 44.289 1.00 19.54 O ANISOU 1495 O ARG D 194 2690 2230 2503 158 -119 409 O ATOM 1496 CB ARG A 194 73.091 67.709 42.410 1.00 20.90 C ANISOU 1496 CB ARG D 194 2803 2527 2609 -118 42 32 C ATOM 1497 CG ARG A 194 72.602 68.318 43.711 1.00 22.20 C ANISOU 1497 CG ARG D 194 3008 2728 2699 24 -131 229 C ATOM 1498 CD ARG A 194 71.332 67.659 44.247 1.00 28.25 C ANISOU 1498 CD ARG D 194 3342 4045 3345 -212 -116 -229 C ATOM 1499 NE ARG A 194 70.372 68.506 44.978 1.00 36.79 N ANISOU 1499 NE ARG D 194 4440 5108 4428 270 -489 135 N ATOM 1500 CZ ARG A 194 70.527 69.749 45.501 1.00 43.70 C ANISOU 1500 CZ ARG D 194 5475 5611 5516 -84 -110 213 C ATOM 1501 NH1 ARG A 194 71.670 70.446 45.480 1.00 47.26 N ANISOU 1501 NH1 ARG D 194 5982 5924 6051 -222 -85 182 N ATOM 1502 NH2 ARG A 194 69.479 70.325 46.102 1.00 41.98 N ANISOU 1502 NH2 ARG D 194 5390 5146 5413 228 118 187 N ATOM 1503 N TRP A 195 75.374 65.825 43.191 1.00 19.76 N ANISOU 1503 N TRP D 195 2583 2431 2492 73 -40 165 N ATOM 1504 CA TRP A 195 75.953 64.915 44.167 1.00 20.34 C ANISOU 1504 CA TRP D 195 2678 2608 2439 28 0 114 C ATOM 1505 C TRP A 195 77.451 65.179 44.359 1.00 20.04 C ANISOU 1505 C TRP D 195 2543 2570 2498 14 -52 9 C ATOM 1506 O TRP A 195 77.925 65.321 45.510 1.00 20.87 O ANISOU 1506 O TRP D 195 2540 2633 2757 -53 -69 147 O ATOM 1507 CB TRP A 195 75.665 63.479 43.709 1.00 19.88 C ANISOU 1507 CB TRP D 195 2512 2595 2445 1 -154 -60 C ATOM 1508 CG TRP A 195 76.141 62.374 44.553 1.00 20.66 C ANISOU 1508 CG TRP D 195 2624 2599 2623 -46 -72 -50 C ATOM 1509 CD1 TRP A 195 76.047 62.267 45.905 1.00 20.27 C ANISOU 1509 CD1 TRP D 195 2637 2635 2429 -32 88 -18 C ATOM 1510 CD2 TRP A 195 76.711 61.143 44.084 1.00 19.98 C ANISOU 1510 CD2 TRP D 195 2307 2673 2608 -74 -56 -28 C ATOM 1511 NE1 TRP A 195 76.536 61.039 46.318 1.00 22.52 N ANISOU 1511 NE1 TRP D 195 3058 2952 2544 25 -141 -71 N ATOM 1512 CE2 TRP A 195 76.970 60.341 45.223 1.00 22.73 C ANISOU 1512 CE2 TRP D 195 2948 2703 2985 6 56 -48 C ATOM 1513 CE3 TRP A 195 77.044 60.649 42.826 1.00 18.85 C ANISOU 1513 CE3 TRP D 195 2193 2590 2380 73 147 -86 C ATOM 1514 CZ2 TRP A 195 77.542 59.080 45.132 1.00 20.49 C ANISOU 1514 CZ2 TRP D 195 2517 2627 2639 -65 2 -60 C ATOM 1515 CZ3 TRP A 195 77.605 59.376 42.735 1.00 20.61 C ANISOU 1515 CZ3 TRP D 195 2725 2660 2444 83 -21 16 C ATOM 1516 CH2 TRP A 195 77.866 58.617 43.885 1.00 21.85 C ANISOU 1516 CH2 TRP D 195 2864 2735 2701 146 -105 22 C ATOM 1517 N CYS A 196 78.160 65.272 43.239 1.00 21.71 N ANISOU 1517 N CYS D 196 2746 2582 2917 91 -17 55 N ATOM 1518 CA CYS A 196 79.587 65.610 43.173 1.00 21.45 C ANISOU 1518 CA CYS D 196 2690 2719 2738 19 99 27 C ATOM 1519 C CYS A 196 79.873 67.024 43.670 1.00 21.55 C ANISOU 1519 C CYS D 196 2670 2741 2774 -13 170 35 C ATOM 1520 O CYS A 196 80.878 67.252 44.364 1.00 21.25 O ANISOU 1520 O CYS D 196 2826 2726 2519 16 397 214 O ATOM 1521 CB CYS A 196 80.091 65.467 41.711 1.00 20.53 C ANISOU 1521 CB CYS D 196 2550 2635 2616 31 215 -39 C ATOM 1522 SG CYS A 196 80.200 63.760 41.138 1.00 21.94 S ANISOU 1522 SG CYS D 196 2422 2849 3065 203 149 3 S ATOM 1523 N ALA A 197 79.002 67.971 43.315 1.00 21.67 N ANISOU 1523 N ALA D 197 2669 2699 2864 -6 221 -4 N ATOM 1524 CA ALA A 197 79.175 69.377 43.689 1.00 23.73 C ANISOU 1524 CA ALA D 197 3000 2895 3121 -39 161 42 C ATOM 1525 C ALA A 197 79.065 69.624 45.177 1.00 25.22 C ANISOU 1525 C ALA D 197 3253 3092 3235 5 160 35 C ATOM 1526 O ALA A 197 79.756 70.501 45.714 1.00 26.31 O ANISOU 1526 O ALA D 197 3420 3303 3271 -87 369 -15 O ATOM 1527 CB ALA A 197 78.180 70.250 42.959 1.00 24.67 C ANISOU 1527 CB ALA D 197 3237 2705 3432 -35 217 89 C ATOM 1528 N LYS A 198 78.187 68.887 45.843 1.00 25.90 N ANISOU 1528 N LYS D 198 3350 3277 3214 -41 125 50 N ATOM 1529 CA LYS A 198 78.024 69.025 47.285 1.00 29.20 C ANISOU 1529 CA LYS D 198 3766 3782 3545 -17 24 0 C ATOM 1530 C LYS A 198 79.305 68.657 48.052 1.00 30.58 C ANISOU 1530 C LYS D 198 3871 4062 3685 -26 15 87 C ATOM 1531 O LYS A 198 79.526 69.128 49.158 1.00 33.21 O ANISOU 1531 O LYS D 198 4271 4544 3802 -171 -130 117 O ATOM 1532 CB LYS A 198 76.841 68.176 47.770 1.00 30.64 C ANISOU 1532 CB LYS D 198 3995 4048 3599 -70 62 7 C ATOM 1533 CG LYS A 198 75.503 68.841 47.570 1.00 32.00 C ANISOU 1533 CG LYS D 198 3996 4129 4032 -110 -52 32 C ATOM 1534 CD LYS A 198 74.370 67.917 48.033 1.00 34.34 C ANISOU 1534 CD LYS D 198 4165 4564 4316 -142 -132 -16 C ATOM 1535 CE LYS A 198 72.989 68.604 47.930 1.00 38.46 C ANISOU 1535 CE LYS D 198 4496 5137 4977 184 -51 -94 C ATOM 1536 NZ LYS A 198 72.974 70.010 48.484 1.00 43.02 N ANISOU 1536 NZ LYS D 198 5467 5402 5476 17 -286 53 N ATOM 1537 N ALA A 199 80.139 67.811 47.465 1.00 29.30 N ANISOU 1537 N ALA D 199 3738 3873 3521 -23 30 67 N ATOM 1538 CA ALA A 199 81.385 67.408 48.078 1.00 28.80 C ANISOU 1538 CA ALA D 199 3694 3668 3577 -41 1 -6 C ATOM 1539 C ALA A 199 82.565 68.333 47.754 1.00 27.92 C ANISOU 1539 C ALA D 199 3596 3449 3561 -57 108 31 C ATOM 1540 O ALA A 199 83.616 68.197 48.356 1.00 27.79 O ANISOU 1540 O ALA D 199 3727 3235 3595 -241 289 155 O ATOM 1541 CB ALA A 199 81.712 66.004 47.631 1.00 29.28 C ANISOU 1541 CB ALA D 199 3838 3553 3735 -37 127 -50 C ATOM 1542 N ALA A 200 82.423 69.229 46.776 1.00 26.77 N ANISOU 1542 N ALA D 200 3369 3339 3462 -49 27 104 N ATOM 1543 CA ALA A 200 83.594 69.840 46.149 1.00 26.76 C ANISOU 1543 CA ALA D 200 3390 3367 3408 -39 19 92 C ATOM 1544 C ALA A 200 84.026 71.116 46.856 1.00 26.69 C ANISOU 1544 C ALA D 200 3330 3346 3462 -26 -20 126 C ATOM 1545 O ALA A 200 83.179 71.921 47.202 1.00 27.54 O ANISOU 1545 O ALA D 200 3445 3311 3707 -21 14 355 O ATOM 1546 CB ALA A 200 83.308 70.142 44.715 1.00 24.89 C ANISOU 1546 CB ALA D 200 3012 3219 3225 -54 5 77 C ATOM 1547 N SER A 201 85.338 71.278 47.065 1.00 26.42 N ANISOU 1547 N SER D 201 3383 3399 3254 -64 -3 23 N ATOM 1548 CA ASER A 201 85.907 72.536 47.534 0.50 26.50 C ANISOU 1548 CA ASER D 201 3394 3403 3269 -58 18 49 C ATOM 1549 C SER A 201 86.436 73.389 46.364 1.00 26.17 C ANISOU 1549 C SER D 201 3396 3368 3178 -103 64 81 C ATOM 1550 O SER A 201 86.634 74.599 46.499 1.00 27.87 O ANISOU 1550 O SER D 201 3867 3645 3074 -145 62 226 O ATOM 1551 CB ASER A 201 87.006 72.249 48.568 0.50 27.45 C ANISOU 1551 CB ASER D 201 3538 3572 3320 -6 48 42 C ATOM 1552 OG ASER A 201 86.459 71.637 49.742 0.50 28.63 O ANISOU 1552 OG ASER D 201 3480 3789 3608 -261 -114 155 O ATOM 1553 N LYS A 202 86.616 72.778 45.199 1.00 25.62 N ANISOU 1553 N LYS D 202 3121 3271 3341 -77 70 10 N ATOM 1554 CA LYS A 202 87.109 73.488 44.036 1.00 24.61 C ANISOU 1554 CA LYS D 202 3121 3135 3094 -107 92 84 C ATOM 1555 C LYS A 202 86.064 73.525 42.896 1.00 23.01 C ANISOU 1555 C LYS D 202 2899 2782 3061 -56 56 96 C ATOM 1556 O LYS A 202 85.117 72.750 42.933 1.00 22.66 O ANISOU 1556 O LYS D 202 2873 2718 3019 -93 283 320 O ATOM 1557 CB LYS A 202 88.401 72.817 43.599 1.00 24.62 C ANISOU 1557 CB LYS D 202 3127 2895 3333 -74 149 67 C ATOM 1558 CG LYS A 202 89.467 72.890 44.685 1.00 27.67 C ANISOU 1558 CG LYS D 202 3098 3775 3640 47 34 3 C ATOM 1559 CD LYS A 202 90.768 72.240 44.295 1.00 27.36 C ANISOU 1559 CD LYS D 202 3420 3623 3352 17 68 -76 C ATOM 1560 CE LYS A 202 91.845 72.435 45.434 1.00 28.54 C ANISOU 1560 CE LYS D 202 3339 3885 3619 -24 244 -220 C ATOM 1561 NZ LYS A 202 93.046 71.586 45.153 1.00 27.31 N ANISOU 1561 NZ LYS D 202 2941 3879 3556 -107 226 9 N ATOM 1562 N PRO A 203 86.215 74.444 41.914 1.00 21.03 N ANISOU 1562 N PRO D 203 2745 2599 2646 -77 80 181 N ATOM 1563 CA PRO A 203 85.298 74.511 40.775 1.00 22.56 C ANISOU 1563 CA PRO D 203 2841 2742 2985 -66 19 77 C ATOM 1564 C PRO A 203 85.071 73.172 40.039 1.00 19.88 C ANISOU 1564 C PRO D 203 2581 2528 2441 44 -21 168 C ATOM 1565 O PRO A 203 85.980 72.329 39.949 1.00 18.19 O ANISOU 1565 O PRO D 203 2184 2374 2353 5 -193 121 O ATOM 1566 CB PRO A 203 85.956 75.522 39.829 1.00 21.75 C ANISOU 1566 CB PRO D 203 2536 2725 3001 -143 29 -5 C ATOM 1567 CG PRO A 203 86.786 76.367 40.704 1.00 21.71 C ANISOU 1567 CG PRO D 203 3058 2657 2531 -143 87 145 C ATOM 1568 CD PRO A 203 87.252 75.499 41.837 1.00 21.94 C ANISOU 1568 CD PRO D 203 2763 2652 2918 -47 34 22 C ATOM 1569 N ILE A 204 83.847 73.004 39.562 1.00 19.24 N ANISOU 1569 N ILE D 204 2415 2420 2475 40 -154 53 N ATOM 1570 CA ILE A 204 83.472 71.884 38.718 1.00 21.26 C ANISOU 1570 CA ILE D 204 2619 2706 2750 -59 -34 48 C ATOM 1571 C ILE A 204 83.087 72.318 37.299 1.00 20.10 C ANISOU 1571 C ILE D 204 2373 2544 2716 -50 12 -18 C ATOM 1572 O ILE A 204 82.334 73.308 37.105 1.00 21.01 O ANISOU 1572 O ILE D 204 2342 2505 3133 -81 60 236 O ATOM 1573 CB ILE A 204 82.329 71.061 39.369 1.00 20.75 C ANISOU 1573 CB ILE D 204 2514 2625 2741 -130 -38 18 C ATOM 1574 CG1 ILE A 204 82.901 70.129 40.444 1.00 21.02 C ANISOU 1574 CG1 ILE D 204 2801 2841 2343 -266 165 249 C ATOM 1575 CG2 ILE A 204 81.603 70.169 38.346 1.00 18.08 C ANISOU 1575 CG2 ILE D 204 2512 2418 1940 104 -95 -151 C ATOM 1576 CD1 ILE A 204 81.870 69.582 41.335 1.00 26.16 C ANISOU 1576 CD1 ILE D 204 3353 3255 3332 -232 -108 -88 C ATOM 1577 N ILE A 205 83.643 71.598 36.318 1.00 18.79 N ANISOU 1577 N ILE D 205 2307 2372 2458 -10 125 35 N ATOM 1578 CA ILE A 205 83.205 71.665 34.917 1.00 18.80 C ANISOU 1578 CA ILE D 205 2343 2390 2408 21 46 12 C ATOM 1579 C ILE A 205 82.222 70.521 34.670 1.00 17.01 C ANISOU 1579 C ILE D 205 2234 2280 1946 69 -34 87 C ATOM 1580 O ILE A 205 82.586 69.346 34.790 1.00 17.97 O ANISOU 1580 O ILE D 205 2146 2335 2346 87 -7 83 O ATOM 1581 CB ILE A 205 84.382 71.577 33.888 1.00 17.77 C ANISOU 1581 CB ILE D 205 2337 2465 1950 51 186 88 C ATOM 1582 CG1 ILE A 205 85.452 72.638 34.176 1.00 22.04 C ANISOU 1582 CG1 ILE D 205 2948 2632 2791 -49 -176 -256 C ATOM 1583 CG2 ILE A 205 83.849 71.667 32.392 1.00 18.92 C ANISOU 1583 CG2 ILE D 205 2441 2434 2314 -188 261 -26 C ATOM 1584 CD1 ILE A 205 86.470 72.788 33.075 1.00 24.15 C ANISOU 1584 CD1 ILE D 205 2775 3126 3274 -153 -37 109 C ATOM 1585 N ALA A 206 80.970 70.862 34.379 1.00 16.54 N ANISOU 1585 N ALA D 206 2258 2264 1760 82 -65 74 N ATOM 1586 CA ALA A 206 79.918 69.864 34.114 1.00 17.93 C ANISOU 1586 CA ALA D 206 2297 2313 2201 29 -27 15 C ATOM 1587 C ALA A 206 80.018 69.433 32.666 1.00 19.24 C ANISOU 1587 C ALA D 206 2521 2427 2360 106 -12 -14 C ATOM 1588 O ALA A 206 79.930 70.263 31.775 1.00 19.89 O ANISOU 1588 O ALA D 206 2776 2233 2547 94 138 -427 O ATOM 1589 CB ALA A 206 78.574 70.455 34.353 1.00 18.77 C ANISOU 1589 CB ALA D 206 2343 2558 2230 74 -69 228 C ATOM 1590 N ASP A 207 80.219 68.147 32.413 1.00 19.63 N ANISOU 1590 N ASP D 207 2573 2329 2554 -34 -78 -36 N ATOM 1591 CA ASP A 207 80.595 67.717 31.042 1.00 18.98 C ANISOU 1591 CA ASP D 207 2477 2435 2299 70 -31 -14 C ATOM 1592 C ASP A 207 79.528 66.825 30.414 1.00 20.69 C ANISOU 1592 C ASP D 207 2765 2650 2443 58 20 2 C ATOM 1593 O ASP A 207 79.465 65.623 30.691 1.00 20.92 O ANISOU 1593 O ASP D 207 2831 2812 2303 -65 -92 12 O ATOM 1594 CB ASP A 207 81.989 67.031 31.069 1.00 19.45 C ANISOU 1594 CB ASP D 207 2470 2492 2427 -130 -44 136 C ATOM 1595 CG ASP A 207 82.511 66.628 29.674 1.00 20.16 C ANISOU 1595 CG ASP D 207 2489 2790 2380 189 -157 -220 C ATOM 1596 OD1 ASP A 207 81.891 66.955 28.628 1.00 21.18 O ANISOU 1596 OD1 ASP D 207 2697 2891 2456 -133 220 256 O ATOM 1597 OD2 ASP A 207 83.574 65.940 29.640 1.00 17.47 O ANISOU 1597 OD2 ASP D 207 2855 2718 1062 -76 -377 -20 O ATOM 1598 N GLY A 208 78.682 67.417 29.563 1.00 22.46 N ANISOU 1598 N GLY D 208 2849 2807 2877 80 80 19 N ATOM 1599 CA GLY A 208 77.815 66.632 28.677 1.00 21.84 C ANISOU 1599 CA GLY D 208 2706 2915 2675 111 100 -79 C ATOM 1600 C GLY A 208 76.373 66.497 29.162 1.00 23.56 C ANISOU 1600 C GLY D 208 2899 3076 2976 6 35 -89 C ATOM 1601 O GLY A 208 76.016 66.992 30.221 1.00 23.32 O ANISOU 1601 O GLY D 208 2644 3189 3026 -69 -153 -139 O ATOM 1602 N GLY A 209 75.548 65.848 28.346 1.00 24.76 N ANISOU 1602 N GLY D 209 3004 3151 3253 -67 80 -16 N ATOM 1603 CA GLY A 209 74.114 65.776 28.593 1.00 24.68 C ANISOU 1603 CA GLY D 209 3029 3212 3135 -37 -49 -12 C ATOM 1604 C GLY A 209 73.339 67.072 28.366 1.00 25.60 C ANISOU 1604 C GLY D 209 3203 3296 3229 -47 -78 36 C ATOM 1605 O GLY A 209 72.141 67.131 28.649 1.00 27.57 O ANISOU 1605 O GLY D 209 3326 3553 3593 -159 -224 68 O ATOM 1606 N ILE A 210 73.987 68.101 27.817 1.00 23.97 N ANISOU 1606 N ILE D 210 3134 3187 2785 -42 -35 95 N ATOM 1607 CA ILE A 210 73.328 69.375 27.589 1.00 26.01 C ANISOU 1607 CA ILE D 210 3351 3400 3130 -3 -45 13 C ATOM 1608 C ILE A 210 72.568 69.282 26.269 1.00 26.85 C ANISOU 1608 C ILE D 210 3454 3512 3233 91 26 9 C ATOM 1609 O ILE A 210 73.160 68.997 25.228 1.00 28.81 O ANISOU 1609 O ILE D 210 3697 3730 3517 158 -198 -220 O ATOM 1610 CB ILE A 210 74.354 70.535 27.520 1.00 26.21 C ANISOU 1610 CB ILE D 210 3393 3347 3217 33 55 20 C ATOM 1611 CG1 ILE A 210 75.255 70.547 28.775 1.00 25.63 C ANISOU 1611 CG1 ILE D 210 3508 3239 2990 -169 -99 226 C ATOM 1612 CG2 ILE A 210 73.665 71.846 27.274 1.00 25.30 C ANISOU 1612 CG2 ILE D 210 3312 3260 3040 90 -216 20 C ATOM 1613 CD1 ILE A 210 74.529 70.439 30.051 1.00 26.31 C ANISOU 1613 CD1 ILE D 210 3627 3358 3012 -73 -203 -91 C ATOM 1614 N ARG A 211 71.261 69.490 26.315 1.00 26.58 N ANISOU 1614 N ARG D 211 3359 3440 3297 110 -31 58 N ATOM 1615 CA ARG A 211 70.440 69.451 25.095 1.00 28.21 C ANISOU 1615 CA ARG D 211 3578 3634 3505 136 -23 45 C ATOM 1616 C ARG A 211 69.814 70.790 24.662 1.00 26.73 C ANISOU 1616 C ARG D 211 3409 3530 3216 96 1 1 C ATOM 1617 O ARG A 211 69.430 70.944 23.513 1.00 25.19 O ANISOU 1617 O ARG D 211 3372 3463 2735 350 -130 -141 O ATOM 1618 CB ARG A 211 69.359 68.405 25.276 1.00 28.96 C ANISOU 1618 CB ARG D 211 3733 3572 3697 50 -28 25 C ATOM 1619 CG ARG A 211 69.929 67.040 25.615 1.00 33.14 C ANISOU 1619 CG ARG D 211 4167 4197 4225 175 47 -125 C ATOM 1620 CD ARG A 211 68.836 66.102 26.088 1.00 37.95 C ANISOU 1620 CD ARG D 211 4953 4499 4964 39 -265 -171 C ATOM 1621 NE ARG A 211 67.899 65.760 25.025 1.00 48.48 N ANISOU 1621 NE ARG D 211 6042 6350 6026 -71 209 128 N ATOM 1622 CZ ARG A 211 66.848 64.958 25.186 1.00 52.32 C ANISOU 1622 CZ ARG D 211 6530 6719 6629 -224 79 -10 C ATOM 1623 NH1 ARG A 211 66.584 64.407 26.373 1.00 54.37 N ANISOU 1623 NH1 ARG D 211 7025 6934 6697 -116 75 -11 N ATOM 1624 NH2 ARG A 211 66.050 64.710 24.154 1.00 52.21 N ANISOU 1624 NH2 ARG D 211 6561 6672 6604 -222 -24 121 N ATOM 1625 N THR A 212 69.722 71.740 25.587 1.00 25.78 N ANISOU 1625 N THR D 212 3311 3346 3137 126 -25 -24 N ATOM 1626 CA THR A 212 69.071 73.041 25.363 1.00 24.99 C ANISOU 1626 CA THR D 212 3191 3235 3067 21 -18 -2 C ATOM 1627 C THR A 212 69.905 74.098 26.068 1.00 23.06 C ANISOU 1627 C THR D 212 2931 3024 2805 45 -64 -36 C ATOM 1628 O THR A 212 70.691 73.771 26.973 1.00 18.89 O ANISOU 1628 O THR D 212 2894 2635 1646 27 -241 -174 O ATOM 1629 CB THR A 212 67.640 73.113 25.985 1.00 24.36 C ANISOU 1629 CB THR D 212 3075 3125 3054 114 44 -17 C ATOM 1630 OG1 THR A 212 67.733 72.993 27.419 1.00 25.87 O ANISOU 1630 OG1 THR D 212 3282 3494 3054 116 -487 -80 O ATOM 1631 CG2 THR A 212 66.757 72.025 25.491 1.00 25.97 C ANISOU 1631 CG2 THR D 212 3065 3368 3433 157 110 68 C ATOM 1632 N ASN A 213 69.738 75.356 25.674 1.00 21.88 N ANISOU 1632 N ASN D 213 2774 2873 2665 98 -129 1 N ATOM 1633 CA ASN A 213 70.389 76.445 26.408 1.00 22.83 C ANISOU 1633 CA ASN D 213 2839 2917 2915 66 -19 -56 C ATOM 1634 C ASN A 213 69.897 76.555 27.858 1.00 22.00 C ANISOU 1634 C ASN D 213 2749 2733 2875 78 74 -14 C ATOM 1635 O ASN A 213 70.676 76.959 28.720 1.00 23.17 O ANISOU 1635 O ASN D 213 2773 3065 2965 1 137 64 O ATOM 1636 CB ASN A 213 70.267 77.794 25.667 1.00 23.87 C ANISOU 1636 CB ASN D 213 2921 3118 3030 33 -77 -169 C ATOM 1637 CG ASN A 213 71.034 77.822 24.348 1.00 23.43 C ANISOU 1637 CG ASN D 213 3347 3004 2549 177 -13 94 C ATOM 1638 OD1 ASN A 213 71.755 76.890 24.020 1.00 26.73 O ANISOU 1638 OD1 ASN D 213 3604 3300 3251 353 29 -235 O ATOM 1639 ND2 ASN A 213 70.899 78.928 23.602 1.00 23.92 N ANISOU 1639 ND2 ASN D 213 3317 2916 2854 -75 -123 -6 N ATOM 1640 N GLY A 214 68.642 76.156 28.143 1.00 19.66 N ANISOU 1640 N GLY D 214 2545 2397 2529 124 49 -53 N ATOM 1641 CA GLY A 214 68.136 76.143 29.509 1.00 20.57 C ANISOU 1641 CA GLY D 214 2547 2484 2783 37 53 -34 C ATOM 1642 C GLY A 214 68.896 75.196 30.413 1.00 19.79 C ANISOU 1642 C GLY D 214 2456 2416 2646 -65 -31 -29 C ATOM 1643 O GLY A 214 68.951 75.398 31.600 1.00 18.54 O ANISOU 1643 O GLY D 214 2242 2154 2648 -57 159 -6 O ATOM 1644 N ASP A 215 69.537 74.183 29.840 1.00 20.26 N ANISOU 1644 N ASP D 215 2606 2265 2825 -90 82 -107 N ATOM 1645 CA ASP A 215 70.348 73.251 30.639 1.00 19.88 C ANISOU 1645 CA ASP D 215 2542 2409 2602 -47 59 -132 C ATOM 1646 C ASP A 215 71.633 73.851 31.189 1.00 19.03 C ANISOU 1646 C ASP D 215 2610 2230 2388 -6 60 32 C ATOM 1647 O ASP A 215 72.193 73.355 32.178 1.00 19.29 O ANISOU 1647 O ASP D 215 2527 2310 2490 9 188 33 O ATOM 1648 CB ASP A 215 70.673 72.002 29.808 1.00 19.48 C ANISOU 1648 CB ASP D 215 2576 2352 2473 49 -24 -42 C ATOM 1649 CG ASP A 215 69.435 71.153 29.492 1.00 19.95 C ANISOU 1649 CG ASP D 215 2470 2574 2533 43 -142 -195 C ATOM 1650 OD1 ASP A 215 68.430 71.246 30.246 1.00 17.30 O ANISOU 1650 OD1 ASP D 215 2243 2059 2270 150 50 -421 O ATOM 1651 OD2 ASP A 215 69.473 70.382 28.486 1.00 24.90 O ANISOU 1651 OD2 ASP D 215 2913 3302 3243 -195 88 377 O ATOM 1652 N VAL A 216 72.100 74.925 30.577 1.00 19.26 N ANISOU 1652 N VAL D 216 2439 2459 2421 -70 13 6 N ATOM 1653 CA VAL A 216 73.199 75.710 31.167 1.00 19.52 C ANISOU 1653 CA VAL D 216 2523 2365 2527 -51 13 -22 C ATOM 1654 C VAL A 216 72.779 76.304 32.526 1.00 18.71 C ANISOU 1654 C VAL D 216 2333 2221 2553 -138 -38 -87 C ATOM 1655 O VAL A 216 73.479 76.118 33.526 1.00 16.40 O ANISOU 1655 O VAL D 216 2257 1673 2299 -47 52 -214 O ATOM 1656 CB VAL A 216 73.742 76.799 30.168 1.00 20.38 C ANISOU 1656 CB VAL D 216 2515 2543 2685 -58 -56 5 C ATOM 1657 CG1 VAL A 216 74.874 77.572 30.764 1.00 19.57 C ANISOU 1657 CG1 VAL D 216 2611 2411 2414 -37 299 54 C ATOM 1658 CG2 VAL A 216 74.212 76.145 28.897 1.00 20.99 C ANISOU 1658 CG2 VAL D 216 3147 2750 2076 -186 -136 -104 C ATOM 1659 N ALA A 217 71.662 77.033 32.588 1.00 18.42 N ANISOU 1659 N ALA D 217 2197 2288 2512 -123 55 -34 N ATOM 1660 CA ALA A 217 71.155 77.529 33.903 1.00 17.98 C ANISOU 1660 CA ALA D 217 2159 2183 2487 -102 81 73 C ATOM 1661 C ALA A 217 70.945 76.429 34.964 1.00 16.09 C ANISOU 1661 C ALA D 217 2037 2115 1961 100 229 237 C ATOM 1662 O ALA A 217 71.301 76.582 36.176 1.00 14.60 O ANISOU 1662 O ALA D 217 2185 1790 1572 100 230 -48 O ATOM 1663 CB ALA A 217 69.849 78.324 33.660 1.00 19.60 C ANISOU 1663 CB ALA D 217 2266 2348 2832 -37 76 -9 C ATOM 1664 N LYS A 218 70.367 75.307 34.519 1.00 17.22 N ANISOU 1664 N LYS D 218 2007 2127 2408 -46 131 31 N ATOM 1665 CA LYS A 218 70.164 74.143 35.357 1.00 16.24 C ANISOU 1665 CA LYS D 218 2121 2033 2015 -49 98 31 C ATOM 1666 C LYS A 218 71.492 73.620 35.893 1.00 17.48 C ANISOU 1666 C LYS D 218 2125 2131 2384 -19 -22 73 C ATOM 1667 O LYS A 218 71.561 73.326 37.073 1.00 15.71 O ANISOU 1667 O LYS D 218 2096 1789 2083 -129 108 87 O ATOM 1668 CB LYS A 218 69.380 73.011 34.670 1.00 14.96 C ANISOU 1668 CB LYS D 218 2008 1759 1915 -71 36 -107 C ATOM 1669 CG LYS A 218 67.990 73.401 34.194 1.00 16.81 C ANISOU 1669 CG LYS D 218 2136 1746 2505 41 -30 -39 C ATOM 1670 CD LYS A 218 67.265 72.286 33.484 1.00 15.69 C ANISOU 1670 CD LYS D 218 2055 1930 1976 -98 -105 54 C ATOM 1671 CE LYS A 218 65.975 72.765 32.863 1.00 19.15 C ANISOU 1671 CE LYS D 218 2419 2496 2358 -204 150 143 C ATOM 1672 NZ LYS A 218 65.269 71.759 31.990 1.00 22.02 N ANISOU 1672 NZ LYS D 218 2927 2416 3021 -294 166 299 N ATOM 1673 N SER A 219 72.531 73.518 35.045 1.00 18.33 N ANISOU 1673 N SER D 219 2077 2442 2443 -22 26 12 N ATOM 1674 CA SER A 219 73.874 73.092 35.526 1.00 17.46 C ANISOU 1674 CA SER D 219 2207 2121 2303 28 69 -35 C ATOM 1675 C SER A 219 74.443 74.067 36.598 1.00 16.85 C ANISOU 1675 C SER D 219 2177 2081 2143 -28 163 -89 C ATOM 1676 O SER A 219 74.994 73.634 37.609 1.00 17.17 O ANISOU 1676 O SER D 219 2294 2004 2226 72 168 -77 O ATOM 1677 CB SER A 219 74.860 72.959 34.358 1.00 18.11 C ANISOU 1677 CB SER D 219 2042 2350 2488 1 -25 97 C ATOM 1678 OG SER A 219 74.354 72.180 33.274 1.00 18.54 O ANISOU 1678 OG SER D 219 1877 2540 2624 172 -180 329 O ATOM 1679 N ILE A 220 74.248 75.372 36.389 1.00 16.68 N ANISOU 1679 N ILE D 220 2070 2107 2160 76 82 50 N ATOM 1680 CA ILE A 220 74.656 76.400 37.344 1.00 18.25 C ANISOU 1680 CA ILE D 220 2346 2152 2435 45 122 58 C ATOM 1681 C ILE A 220 73.907 76.225 38.671 1.00 17.87 C ANISOU 1681 C ILE D 220 2356 2035 2396 -24 91 67 C ATOM 1682 O ILE A 220 74.541 76.191 39.737 1.00 17.63 O ANISOU 1682 O ILE D 220 2357 1681 2659 -26 283 249 O ATOM 1683 CB ILE A 220 74.471 77.858 36.796 1.00 19.14 C ANISOU 1683 CB ILE D 220 2526 2363 2383 -176 76 65 C ATOM 1684 CG1 ILE A 220 75.360 78.107 35.548 1.00 23.12 C ANISOU 1684 CG1 ILE D 220 2682 3000 3099 -71 -112 102 C ATOM 1685 CG2 ILE A 220 74.795 78.884 37.897 1.00 18.47 C ANISOU 1685 CG2 ILE D 220 2292 2235 2489 -14 -214 195 C ATOM 1686 CD1 ILE A 220 76.859 77.967 35.814 1.00 24.73 C ANISOU 1686 CD1 ILE D 220 3028 2881 3487 7 36 -168 C ATOM 1687 N ARG A 221 72.580 76.043 38.629 1.00 17.86 N ANISOU 1687 N ARG D 221 2361 2158 2266 154 71 63 N ATOM 1688 CA ARG A 221 71.800 75.798 39.866 1.00 18.28 C ANISOU 1688 CA ARG D 221 2314 2207 2424 -2 75 55 C ATOM 1689 C ARG A 221 72.386 74.679 40.697 1.00 16.86 C ANISOU 1689 C ARG D 221 2072 2333 2001 -48 33 120 C ATOM 1690 O ARG A 221 72.505 74.823 41.924 1.00 17.48 O ANISOU 1690 O ARG D 221 2150 2662 1827 -137 -62 -13 O ATOM 1691 CB ARG A 221 70.321 75.475 39.544 1.00 18.86 C ANISOU 1691 CB ARG D 221 2176 2244 2745 118 -69 84 C ATOM 1692 CG ARG A 221 69.494 75.018 40.730 1.00 18.53 C ANISOU 1692 CG ARG D 221 2372 2387 2279 43 214 6 C ATOM 1693 CD ARG A 221 69.569 76.025 41.884 1.00 21.86 C ANISOU 1693 CD ARG D 221 2532 2551 3221 -88 4 244 C ATOM 1694 NE ARG A 221 68.746 75.692 43.027 1.00 20.04 N ANISOU 1694 NE ARG D 221 2538 2573 2502 1 244 84 N ATOM 1695 CZ ARG A 221 69.093 74.873 44.023 1.00 24.39 C ANISOU 1695 CZ ARG D 221 3160 3247 2861 32 167 -95 C ATOM 1696 NH1 ARG A 221 70.281 74.251 44.052 1.00 22.98 N ANISOU 1696 NH1 ARG D 221 3456 2824 2449 60 -129 41 N ATOM 1697 NH2 ARG A 221 68.229 74.678 45.015 1.00 25.28 N ANISOU 1697 NH2 ARG D 221 2871 3331 3401 -158 189 -64 N ATOM 1698 N PHE A 222 72.751 73.577 40.050 1.00 16.79 N ANISOU 1698 N PHE D 222 1880 2174 2322 -212 13 38 N ATOM 1699 CA PHE A 222 73.202 72.386 40.761 1.00 17.66 C ANISOU 1699 CA PHE D 222 2184 2250 2275 -84 -11 29 C ATOM 1700 C PHE A 222 74.719 72.242 40.693 1.00 19.00 C ANISOU 1700 C PHE D 222 2399 2322 2497 26 6 -12 C ATOM 1701 O PHE A 222 75.259 71.158 40.910 1.00 19.72 O ANISOU 1701 O PHE D 222 2678 2281 2532 130 77 139 O ATOM 1702 CB PHE A 222 72.529 71.135 40.192 1.00 17.47 C ANISOU 1702 CB PHE D 222 2388 2072 2177 68 130 113 C ATOM 1703 CG PHE A 222 71.055 71.060 40.472 1.00 17.95 C ANISOU 1703 CG PHE D 222 2431 2337 2053 -243 43 23 C ATOM 1704 CD1 PHE A 222 70.592 70.698 41.725 1.00 21.59 C ANISOU 1704 CD1 PHE D 222 2629 2956 2616 132 -233 -373 C ATOM 1705 CD2 PHE A 222 70.133 71.352 39.481 1.00 21.48 C ANISOU 1705 CD2 PHE D 222 2537 2683 2939 -245 -38 -76 C ATOM 1706 CE1 PHE A 222 69.236 70.628 41.986 1.00 21.05 C ANISOU 1706 CE1 PHE D 222 2442 2499 3055 -7 54 -256 C ATOM 1707 CE2 PHE A 222 68.776 71.284 39.735 1.00 19.45 C ANISOU 1707 CE2 PHE D 222 2418 2616 2354 209 -74 7 C ATOM 1708 CZ PHE A 222 68.327 70.921 40.989 1.00 17.97 C ANISOU 1708 CZ PHE D 222 2547 2190 2090 4 57 17 C ATOM 1709 N GLY A 223 75.400 73.343 40.391 1.00 17.34 N ANISOU 1709 N GLY D 223 2249 2134 2205 -19 -51 91 N ATOM 1710 CA GLY A 223 76.603 73.717 41.112 1.00 17.95 C ANISOU 1710 CA GLY D 223 2321 2236 2261 -108 20 39 C ATOM 1711 C GLY A 223 77.827 73.752 40.218 1.00 19.15 C ANISOU 1711 C GLY D 223 2328 2445 2500 -39 38 3 C ATOM 1712 O GLY A 223 78.960 73.728 40.700 1.00 20.65 O ANISOU 1712 O GLY D 223 2251 2768 2827 -100 124 -63 O ATOM 1713 N ALA A 224 77.598 73.811 38.911 1.00 19.40 N ANISOU 1713 N ALA D 224 2419 2445 2507 -102 19 41 N ATOM 1714 CA ALA A 224 78.685 73.937 37.947 1.00 18.45 C ANISOU 1714 CA ALA D 224 2262 2290 2455 -32 8 24 C ATOM 1715 C ALA A 224 79.273 75.344 37.962 1.00 19.43 C ANISOU 1715 C ALA D 224 2412 2277 2694 -50 -3 25 C ATOM 1716 O ALA A 224 78.594 76.308 38.313 1.00 19.49 O ANISOU 1716 O ALA D 224 2490 2029 2885 -126 -125 206 O ATOM 1717 CB ALA A 224 78.200 73.577 36.551 1.00 19.14 C ANISOU 1717 CB ALA D 224 2317 2307 2645 -63 -53 198 C ATOM 1718 N THR A 225 80.541 75.454 37.578 1.00 17.51 N ANISOU 1718 N THR D 225 2196 2223 2232 41 73 66 N ATOM 1719 CA THR A 225 81.144 76.749 37.286 1.00 17.46 C ANISOU 1719 CA THR D 225 2191 2384 2055 -36 -52 -29 C ATOM 1720 C THR A 225 81.319 76.950 35.785 1.00 18.08 C ANISOU 1720 C THR D 225 2255 2483 2130 41 -123 -202 C ATOM 1721 O THR A 225 81.004 78.013 35.250 1.00 19.48 O ANISOU 1721 O THR D 225 2439 2572 2388 153 -144 35 O ATOM 1722 CB THR A 225 82.501 76.886 38.001 1.00 17.90 C ANISOU 1722 CB THR D 225 2269 2448 2083 -184 -165 -158 C ATOM 1723 OG1 THR A 225 82.287 77.097 39.402 1.00 16.58 O ANISOU 1723 OG1 THR D 225 2373 2230 1695 -289 19 -69 O ATOM 1724 CG2 THR A 225 83.210 78.157 37.559 1.00 19.50 C ANISOU 1724 CG2 THR D 225 2274 2327 2806 -31 68 12 C ATOM 1725 N MET A 226 81.825 75.923 35.110 1.00 19.85 N ANISOU 1725 N MET D 226 2876 2519 2146 16 92 -79 N ATOM 1726 CA MET A 226 81.806 75.880 33.653 1.00 19.68 C ANISOU 1726 CA MET D 226 2669 2544 2264 36 3 -86 C ATOM 1727 C MET A 226 81.008 74.682 33.147 1.00 18.92 C ANISOU 1727 C MET D 226 2543 2478 2166 58 -60 -7 C ATOM 1728 O MET A 226 81.020 73.614 33.758 1.00 18.50 O ANISOU 1728 O MET D 226 2656 2166 2204 40 117 132 O ATOM 1729 CB MET A 226 83.231 75.834 33.099 1.00 22.76 C ANISOU 1729 CB MET D 226 3006 2901 2740 67 -4 -232 C ATOM 1730 CG MET A 226 83.364 76.365 31.682 1.00 26.60 C ANISOU 1730 CG MET D 226 3504 3633 2970 119 -142 -124 C ATOM 1731 SD MET A 226 83.146 78.153 31.585 1.00 28.22 S ANISOU 1731 SD MET D 226 3210 3623 3889 426 -134 -456 S ATOM 1732 CE MET A 226 84.703 78.720 32.266 1.00 34.92 C ANISOU 1732 CE MET D 226 3920 4759 4586 56 -161 142 C ATOM 1733 N VAL A 227 80.315 74.869 32.029 1.00 17.23 N ANISOU 1733 N VAL D 227 2060 2435 2048 40 -212 88 N ATOM 1734 CA VAL A 227 79.557 73.790 31.407 1.00 19.42 C ANISOU 1734 CA VAL D 227 2472 2642 2264 16 -139 0 C ATOM 1735 C VAL A 227 80.147 73.412 30.053 1.00 18.28 C ANISOU 1735 C VAL D 227 2444 2542 1958 -22 13 9 C ATOM 1736 O VAL A 227 80.145 74.214 29.119 1.00 20.34 O ANISOU 1736 O VAL D 227 2654 2830 2243 -112 -107 -187 O ATOM 1737 CB VAL A 227 78.078 74.176 31.221 1.00 19.77 C ANISOU 1737 CB VAL D 227 2626 2608 2275 83 -126 -70 C ATOM 1738 CG1 VAL A 227 77.292 73.010 30.641 1.00 18.45 C ANISOU 1738 CG1 VAL D 227 2076 2979 1953 -91 -241 -161 C ATOM 1739 CG2 VAL A 227 77.475 74.631 32.541 1.00 18.04 C ANISOU 1739 CG2 VAL D 227 2272 2392 2190 -17 -52 -254 C ATOM 1740 N MET A 228 80.653 72.187 29.954 1.00 18.12 N ANISOU 1740 N MET D 228 2337 2607 1940 -72 -110 67 N ATOM 1741 CA MET A 228 81.257 71.701 28.703 1.00 19.84 C ANISOU 1741 CA MET D 228 2572 2567 2397 12 -175 95 C ATOM 1742 C MET A 228 80.190 71.121 27.768 1.00 20.86 C ANISOU 1742 C MET D 228 2692 2716 2517 -42 -151 113 C ATOM 1743 O MET A 228 79.457 70.190 28.143 1.00 20.20 O ANISOU 1743 O MET D 228 2752 2873 2048 -239 -287 32 O ATOM 1744 CB MET A 228 82.399 70.693 28.944 1.00 18.32 C ANISOU 1744 CB MET D 228 2543 2442 1975 -52 -142 283 C ATOM 1745 CG MET A 228 83.005 70.151 27.580 1.00 16.35 C ANISOU 1745 CG MET D 228 2152 2607 1453 -153 -225 19 C ATOM 1746 SD MET A 228 84.520 69.219 27.777 1.00 20.72 S ANISOU 1746 SD MET D 228 2536 2533 2800 -10 -477 232 S ATOM 1747 CE MET A 228 85.658 70.558 28.083 1.00 21.39 C ANISOU 1747 CE MET D 228 2848 2508 2770 39 -254 6 C ATOM 1748 N ILE A 229 80.151 71.649 26.540 1.00 22.18 N ANISOU 1748 N ILE D 229 2839 2866 2721 46 -164 -71 N ATOM 1749 CA ILE A 229 79.099 71.356 25.551 1.00 24.04 C ANISOU 1749 CA ILE D 229 3066 3045 3023 18 -87 12 C ATOM 1750 C ILE A 229 79.623 70.780 24.236 1.00 25.34 C ANISOU 1750 C ILE D 229 3263 3201 3164 14 -126 -17 C ATOM 1751 O ILE A 229 80.510 71.362 23.617 1.00 25.32 O ANISOU 1751 O ILE D 229 3165 3287 3167 214 -226 -30 O ATOM 1752 CB ILE A 229 78.330 72.650 25.231 1.00 24.81 C ANISOU 1752 CB ILE D 229 3107 3265 3052 49 -108 -59 C ATOM 1753 CG1 ILE A 229 77.725 73.204 26.539 1.00 23.75 C ANISOU 1753 CG1 ILE D 229 3056 3198 2769 189 80 70 C ATOM 1754 CG2 ILE A 229 77.262 72.412 24.187 1.00 24.17 C ANISOU 1754 CG2 ILE D 229 3001 3107 3075 35 -75 77 C ATOM 1755 CD1 ILE A 229 76.857 74.459 26.388 1.00 24.18 C ANISOU 1755 CD1 ILE D 229 3201 2997 2988 51 -223 -64 C ATOM 1756 N GLY A 230 79.044 69.652 23.801 1.00 26.47 N ANISOU 1756 N GLY D 230 3397 3472 3189 16 -119 7 N ATOM 1757 CA GLY A 230 79.396 69.014 22.522 1.00 27.38 C ANISOU 1757 CA GLY D 230 3508 3515 3380 66 -43 106 C ATOM 1758 C GLY A 230 78.401 69.344 21.416 1.00 27.26 C ANISOU 1758 C GLY D 230 3588 3566 3202 81 -42 57 C ATOM 1759 O GLY A 230 78.616 70.281 20.651 1.00 28.96 O ANISOU 1759 O GLY D 230 3767 3690 3546 145 -124 108 O ATOM 1760 N SER A 231 77.292 68.607 21.383 1.00 28.64 N ANISOU 1760 N SER D 231 3774 3725 3381 78 -51 50 N ATOM 1761 CA SER A 231 76.270 68.694 20.312 1.00 30.56 C ANISOU 1761 CA SER D 231 3808 4007 3795 42 16 11 C ATOM 1762 C SER A 231 75.808 70.103 19.949 1.00 31.72 C ANISOU 1762 C SER D 231 4016 4109 3925 51 4 -37 C ATOM 1763 O SER A 231 75.617 70.408 18.774 1.00 32.95 O ANISOU 1763 O SER D 231 4134 4388 3997 96 105 -33 O ATOM 1764 CB SER A 231 75.026 67.868 20.678 1.00 31.77 C ANISOU 1764 CB SER D 231 4020 4093 3956 56 -19 -56 C ATOM 1765 OG SER A 231 74.327 68.463 21.782 1.00 38.47 O ANISOU 1765 OG SER D 231 4780 5356 4481 90 29 129 O ATOM 1766 N LEU A 232 75.581 70.951 20.942 1.00 31.93 N ANISOU 1766 N LEU D 232 3992 4129 4009 18 88 12 N ATOM 1767 CA LEU A 232 75.056 72.275 20.643 1.00 32.15 C ANISOU 1767 CA LEU D 232 4030 4121 4064 3 -13 -51 C ATOM 1768 C LEU A 232 76.071 73.096 19.849 1.00 32.02 C ANISOU 1768 C LEU D 232 3969 4086 4109 -14 -16 -102 C ATOM 1769 O LEU A 232 75.677 74.016 19.132 1.00 28.10 O ANISOU 1769 O LEU D 232 3613 3931 3131 -40 -56 -257 O ATOM 1770 CB LEU A 232 74.598 73.030 21.892 1.00 32.74 C ANISOU 1770 CB LEU D 232 3999 4359 4079 -7 32 0 C ATOM 1771 CG LEU A 232 73.243 72.643 22.523 1.00 33.50 C ANISOU 1771 CG LEU D 232 4196 4411 4120 -45 44 -66 C ATOM 1772 CD1 LEU A 232 73.135 73.320 23.877 1.00 31.68 C ANISOU 1772 CD1 LEU D 232 3727 4187 4120 196 -84 55 C ATOM 1773 CD2 LEU A 232 72.069 73.047 21.639 1.00 34.70 C ANISOU 1773 CD2 LEU D 232 4110 4566 4507 -98 -5 -84 C ATOM 1774 N PHE A 233 77.359 72.766 19.986 1.00 32.73 N ANISOU 1774 N PHE D 233 4002 4067 4365 -17 -46 -22 N ATOM 1775 CA PHE A 233 78.420 73.457 19.232 1.00 33.91 C ANISOU 1775 CA PHE D 233 4180 4375 4326 13 -68 -42 C ATOM 1776 C PHE A 233 78.815 72.729 17.962 1.00 34.13 C ANISOU 1776 C PHE D 233 4225 4446 4295 19 -37 -29 C ATOM 1777 O PHE A 233 79.610 73.249 17.176 1.00 33.05 O ANISOU 1777 O PHE D 233 4135 4384 4037 67 9 -60 O ATOM 1778 CB PHE A 233 79.673 73.630 20.099 1.00 33.97 C ANISOU 1778 CB PHE D 233 4156 4366 4383 -14 -54 -32 C ATOM 1779 CG PHE A 233 79.577 74.727 21.128 1.00 32.16 C ANISOU 1779 CG PHE D 233 3961 4069 4189 -3 -37 -26 C ATOM 1780 CD1 PHE A 233 79.301 76.026 20.753 1.00 34.58 C ANISOU 1780 CD1 PHE D 233 4430 4315 4391 107 -47 57 C ATOM 1781 CD2 PHE A 233 79.855 74.471 22.461 1.00 32.99 C ANISOU 1781 CD2 PHE D 233 4181 4142 4208 26 -115 -2 C ATOM 1782 CE1 PHE A 233 79.248 77.032 21.703 1.00 35.67 C ANISOU 1782 CE1 PHE D 233 4727 4350 4473 2 -17 55 C ATOM 1783 CE2 PHE A 233 79.802 75.465 23.411 1.00 32.47 C ANISOU 1783 CE2 PHE D 233 3985 4049 4302 31 121 -44 C ATOM 1784 CZ PHE A 233 79.506 76.752 23.042 1.00 33.17 C ANISOU 1784 CZ PHE D 233 4082 4106 4412 12 145 -141 C ATOM 1785 N ALA A 234 78.297 71.526 17.764 1.00 35.49 N ANISOU 1785 N ALA D 234 4376 4598 4508 -6 -67 -99 N ATOM 1786 CA ALA A 234 78.606 70.754 16.558 1.00 37.82 C ANISOU 1786 CA ALA D 234 4746 4876 4747 15 -52 14 C ATOM 1787 C ALA A 234 77.813 71.273 15.364 1.00 40.69 C ANISOU 1787 C ALA D 234 5100 5326 5032 74 -25 -92 C ATOM 1788 O ALA A 234 76.672 71.742 15.514 1.00 42.12 O ANISOU 1788 O ALA D 234 5263 5513 5225 136 -157 -145 O ATOM 1789 CB ALA A 234 78.327 69.287 16.766 1.00 37.83 C ANISOU 1789 CB ALA D 234 4754 4931 4686 -6 -29 -21 C ATOM 1790 N GLY A 235 78.423 71.207 14.179 1.00 41.81 N ANISOU 1790 N GLY D 235 5280 5493 5112 103 -48 -27 N ATOM 1791 CA GLY A 235 77.706 71.524 12.949 1.00 42.16 C ANISOU 1791 CA GLY D 235 5350 5525 5143 36 -5 -28 C ATOM 1792 C GLY A 235 77.520 72.996 12.638 1.00 43.62 C ANISOU 1792 C GLY D 235 5512 5634 5426 57 -36 -13 C ATOM 1793 O GLY A 235 76.506 73.377 12.032 1.00 44.86 O ANISOU 1793 O GLY D 235 5657 5807 5581 130 77 -86 O ATOM 1794 N HIS A 236 78.481 73.824 13.051 1.00 43.85 N ANISOU 1794 N HIS D 236 5524 5707 5429 -3 -40 -4 N ATOM 1795 CA HIS A 236 78.584 75.213 12.566 1.00 45.05 C ANISOU 1795 CA HIS D 236 5734 5739 5642 25 -21 -12 C ATOM 1796 C HIS A 236 79.465 75.325 11.325 1.00 46.23 C ANISOU 1796 C HIS D 236 5957 5958 5648 53 -77 -23 C ATOM 1797 O HIS A 236 80.315 74.476 11.094 1.00 45.60 O ANISOU 1797 O HIS D 236 5997 5999 5328 119 -157 -34 O ATOM 1798 CB HIS A 236 79.162 76.112 13.643 1.00 43.90 C ANISOU 1798 CB HIS D 236 5625 5656 5399 68 -117 -43 C ATOM 1799 CG HIS A 236 78.202 76.375 14.737 1.00 42.74 C ANISOU 1799 CG HIS D 236 5394 5536 5306 77 -25 -65 C ATOM 1800 ND1 HIS A 236 77.147 77.243 14.586 1.00 40.83 N ANISOU 1800 ND1 HIS D 236 5273 5273 4968 54 17 -102 N ATOM 1801 CD2 HIS A 236 78.083 75.832 15.972 1.00 39.59 C ANISOU 1801 CD2 HIS D 236 4984 5213 4843 79 45 37 C ATOM 1802 CE1 HIS A 236 76.433 77.245 15.697 1.00 41.07 C ANISOU 1802 CE1 HIS D 236 5180 5288 5135 129 41 -65 C ATOM 1803 NE2 HIS A 236 76.977 76.397 16.550 1.00 37.84 N ANISOU 1803 NE2 HIS D 236 5062 5392 3924 -91 -74 61 N ATOM 1804 N GLU A 237 79.293 76.404 10.561 1.00 48.22 N ANISOU 1804 N GLU D 237 6165 6163 5992 23 -47 -58 N ATOM 1805 CA GLU A 237 80.117 76.620 9.372 1.00 48.37 C ANISOU 1805 CA GLU D 237 6179 6158 6039 11 -77 -56 C ATOM 1806 C GLU A 237 81.599 76.474 9.732 1.00 48.97 C ANISOU 1806 C GLU D 237 6216 6261 6128 7 -55 -45 C ATOM 1807 O GLU A 237 82.343 75.762 9.050 1.00 49.24 O ANISOU 1807 O GLU D 237 6163 6308 6238 23 -99 -85 O ATOM 1808 CB GLU A 237 79.830 77.993 8.736 1.00 49.43 C ANISOU 1808 CB GLU D 237 6281 6287 6211 41 -63 -21 C ATOM 1809 CG GLU A 237 80.531 78.244 7.389 1.00 50.36 C ANISOU 1809 CG GLU D 237 6401 6517 6216 -4 23 -170 C ATOM 1810 CD GLU A 237 80.421 77.063 6.412 1.00 56.54 C ANISOU 1810 CD GLU D 237 7316 7133 7031 19 7 107 C ATOM 1811 OE1 GLU A 237 79.352 76.390 6.366 1.00 58.27 O ANISOU 1811 OE1 GLU D 237 7526 7543 7070 -103 147 -7 O ATOM 1812 OE2 GLU A 237 81.412 76.813 5.685 1.00 59.92 O ANISOU 1812 OE2 GLU D 237 7536 7759 7472 100 -72 -69 O ATOM 1813 N GLU A 238 81.994 77.093 10.845 1.00 48.81 N ANISOU 1813 N GLU D 238 6200 6205 6140 -10 -44 -13 N ATOM 1814 CA GLU A 238 83.365 77.016 11.358 1.00 49.25 C ANISOU 1814 CA GLU D 238 6259 6281 6173 -12 -57 -9 C ATOM 1815 C GLU A 238 83.792 75.642 11.868 1.00 48.52 C ANISOU 1815 C GLU D 238 6190 6219 6025 9 -69 -13 C ATOM 1816 O GLU A 238 84.977 75.388 12.032 1.00 47.87 O ANISOU 1816 O GLU D 238 6208 6212 5769 -53 -11 -50 O ATOM 1817 CB GLU A 238 83.560 77.999 12.510 1.00 49.64 C ANISOU 1817 CB GLU D 238 6309 6321 6229 -32 -28 41 C ATOM 1818 CG GLU A 238 83.338 79.445 12.141 1.00 50.68 C ANISOU 1818 CG GLU D 238 6432 6409 6415 -22 -31 -59 C ATOM 1819 CD GLU A 238 81.903 79.913 12.307 1.00 50.84 C ANISOU 1819 CD GLU D 238 6380 6441 6494 -53 -87 14 C ATOM 1820 OE1 GLU A 238 80.976 79.079 12.381 1.00 49.57 O ANISOU 1820 OE1 GLU D 238 6312 6128 6392 47 -194 42 O ATOM 1821 OE2 GLU A 238 81.704 81.138 12.355 1.00 53.13 O ANISOU 1821 OE2 GLU D 238 6701 6625 6857 57 -178 -31 O ATOM 1822 N SER A 239 82.841 74.766 12.147 1.00 49.20 N ANISOU 1822 N SER D 239 6281 6223 6189 13 -65 32 N ATOM 1823 CA SER A 239 83.188 73.488 12.737 1.00 50.38 C ANISOU 1823 CA SER D 239 6394 6405 6342 0 -7 -33 C ATOM 1824 C SER A 239 83.933 72.631 11.722 1.00 51.04 C ANISOU 1824 C SER D 239 6455 6509 6429 -6 -27 -14 C ATOM 1825 O SER A 239 83.759 72.799 10.512 1.00 49.47 O ANISOU 1825 O SER D 239 6167 6353 6276 -10 -39 7 O ATOM 1826 CB SER A 239 81.947 72.744 13.219 1.00 49.79 C ANISOU 1826 CB SER D 239 6301 6349 6268 60 -27 -5 C ATOM 1827 OG SER A 239 81.234 73.524 14.154 1.00 46.65 O ANISOU 1827 OG SER D 239 5992 6010 5723 -26 171 -21 O ATOM 1828 N PRO A 240 84.798 71.734 12.215 1.00 52.45 N ANISOU 1828 N PRO D 240 6598 6667 6663 34 -13 -37 N ATOM 1829 CA PRO A 240 85.344 70.664 11.399 1.00 54.57 C ANISOU 1829 CA PRO D 240 6908 6883 6944 59 -73 -14 C ATOM 1830 C PRO A 240 84.290 69.969 10.531 1.00 56.42 C ANISOU 1830 C PRO D 240 7114 7155 7168 15 1 -7 C ATOM 1831 O PRO A 240 83.118 69.889 10.910 1.00 56.44 O ANISOU 1831 O PRO D 240 7151 7166 7125 54 -51 -15 O ATOM 1832 CB PRO A 240 85.915 69.703 12.442 1.00 53.93 C ANISOU 1832 CB PRO D 240 6844 6806 6841 -18 -4 15 C ATOM 1833 CG PRO A 240 86.339 70.608 13.568 1.00 52.61 C ANISOU 1833 CG PRO D 240 6658 6736 6593 8 -100 -22 C ATOM 1834 CD PRO A 240 85.354 71.731 13.582 1.00 51.96 C ANISOU 1834 CD PRO D 240 6618 6576 6549 2 -10 -16 C ATOM 1835 N GLY A 241 84.720 69.481 9.370 1.00 59.16 N ANISOU 1835 N GLY D 241 7491 7508 7477 22 -39 10 N ATOM 1836 CA GLY A 241 83.844 68.766 8.438 1.00 61.19 C ANISOU 1836 CA GLY D 241 7759 7740 7749 -33 -10 99 C ATOM 1837 C GLY A 241 83.489 69.626 7.247 1.00 63.14 C ANISOU 1837 C GLY D 241 8025 8034 7928 28 -24 -1 C ATOM 1838 O GLY A 241 84.033 70.718 7.075 1.00 63.06 O ANISOU 1838 O GLY D 241 7994 8098 7866 15 -19 -10 O ATOM 1839 N GLU A 242 82.563 69.139 6.432 1.00 65.62 N ANISOU 1839 N GLU D 242 8282 8381 8267 5 7 24 N ATOM 1840 CA GLU A 242 82.137 69.863 5.239 1.00 67.96 C ANISOU 1840 CA GLU D 242 8643 8658 8520 -8 37 -24 C ATOM 1841 C GLU A 242 80.638 70.140 5.253 1.00 69.53 C ANISOU 1841 C GLU D 242 8772 8867 8778 -3 30 -7 C ATOM 1842 O GLU A 242 79.842 69.362 5.802 1.00 69.65 O ANISOU 1842 O GLU D 242 8812 8884 8767 -35 59 -35 O ATOM 1843 CB GLU A 242 82.556 69.150 3.939 1.00 68.77 C ANISOU 1843 CB GLU D 242 8705 8737 8685 -2 -8 34 C ATOM 1844 CG GLU A 242 82.771 67.638 4.013 1.00 70.40 C ANISOU 1844 CG GLU D 242 8961 8847 8941 15 -34 41 C ATOM 1845 CD GLU A 242 83.417 67.090 2.738 1.00 70.37 C ANISOU 1845 CD GLU D 242 8964 8904 8867 -2 -16 55 C ATOM 1846 OE1 GLU A 242 83.059 67.565 1.634 1.00 72.48 O ANISOU 1846 OE1 GLU D 242 9267 9210 9062 35 0 -57 O ATOM 1847 OE2 GLU A 242 84.286 66.192 2.839 1.00 73.26 O ANISOU 1847 OE2 GLU D 242 9224 9244 9365 144 14 -28 O ATOM 1848 N THR A 243 80.279 71.278 4.663 1.00 70.63 N ANISOU 1848 N THR D 243 8950 8961 8925 11 15 -18 N ATOM 1849 CA THR A 243 78.894 71.686 4.521 1.00 71.14 C ANISOU 1849 CA THR D 243 8993 9028 9009 37 2 -24 C ATOM 1850 C THR A 243 78.288 70.976 3.312 1.00 72.21 C ANISOU 1850 C THR D 243 9141 9160 9135 5 11 -8 C ATOM 1851 O THR A 243 78.935 70.848 2.269 1.00 72.95 O ANISOU 1851 O THR D 243 9217 9266 9233 6 -9 -36 O ATOM 1852 CB THR A 243 78.791 73.209 4.332 1.00 71.33 C ANISOU 1852 CB THR D 243 9045 9038 9017 21 -25 -21 C ATOM 1853 OG1 THR A 243 79.443 73.878 5.426 1.00 70.98 O ANISOU 1853 OG1 THR D 243 8924 9034 9010 0 -11 -96 O ATOM 1854 CG2 THR A 243 77.334 73.648 4.246 1.00 70.79 C ANISOU 1854 CG2 THR D 243 8960 9007 8929 1 10 5 C ATOM 1855 N ILE A 244 77.047 70.523 3.461 1.00 72.67 N ANISOU 1855 N ILE D 244 9191 9218 9200 -5 -3 -15 N ATOM 1856 CA ILE A 244 76.351 69.735 2.441 1.00 72.74 C ANISOU 1856 CA ILE D 244 9208 9224 9206 -7 11 9 C ATOM 1857 C ILE A 244 75.135 70.504 1.929 1.00 72.86 C ANISOU 1857 C ILE D 244 9202 9269 9212 1 29 9 C ATOM 1858 O ILE A 244 74.297 70.952 2.713 1.00 72.92 O ANISOU 1858 O ILE D 244 9181 9322 9201 19 59 1 O ATOM 1859 CB ILE A 244 75.911 68.368 3.022 1.00 73.03 C ANISOU 1859 CB ILE D 244 9277 9248 9220 -9 7 1 C ATOM 1860 CG1 ILE A 244 77.145 67.481 3.276 1.00 73.51 C ANISOU 1860 CG1 ILE D 244 9314 9290 9325 8 -3 -4 C ATOM 1861 CG2 ILE A 244 74.908 67.668 2.096 1.00 72.75 C ANISOU 1861 CG2 ILE D 244 9213 9202 9226 -5 3 0 C ATOM 1862 CD1 ILE A 244 77.052 66.596 4.541 1.00 73.48 C ANISOU 1862 CD1 ILE D 244 9304 9288 9324 -7 -13 -10 C ATOM 1863 N ASN A 268 70.459 78.117 -2.886 1.00 67.28 N ANISOU 1863 N ASN D 268 8552 8488 8523 -32 25 -5 N ATOM 1864 CA ASN A 268 69.419 77.127 -2.595 1.00 66.81 C ANISOU 1864 CA ASN D 268 8496 8427 8458 -9 4 -18 C ATOM 1865 C ASN A 268 69.964 75.755 -2.132 1.00 66.95 C ANISOU 1865 C ASN D 268 8529 8443 8466 -16 13 -15 C ATOM 1866 O ASN A 268 70.480 75.648 -1.012 1.00 68.05 O ANISOU 1866 O ASN D 268 8682 8623 8550 -26 59 7 O ATOM 1867 CB ASN A 268 68.448 76.975 -3.787 1.00 66.99 C ANISOU 1867 CB ASN D 268 8499 8480 8472 1 16 -36 C ATOM 1868 CG ASN A 268 69.167 76.843 -5.128 1.00 67.44 C ANISOU 1868 CG ASN D 268 8589 8538 8494 -7 15 10 C ATOM 1869 OD1 ASN A 268 70.331 76.431 -5.199 1.00 67.19 O ANISOU 1869 OD1 ASN D 268 8619 8513 8397 33 -20 10 O ATOM 1870 ND2 ASN A 268 68.465 77.185 -6.200 1.00 67.62 N ANISOU 1870 ND2 ASN D 268 8719 8438 8535 -12 19 26 N ATOM 1871 N VAL A 269 69.907 74.745 -3.013 1.00 65.99 N ANISOU 1871 N VAL D 269 8375 8358 8337 -14 -24 -32 N ATOM 1872 CA VAL A 269 69.640 73.347 -2.620 1.00 64.91 C ANISOU 1872 CA VAL D 269 8190 8265 8205 3 -22 -3 C ATOM 1873 C VAL A 269 68.239 73.358 -1.958 1.00 64.75 C ANISOU 1873 C VAL D 269 8152 8257 8192 -18 11 -31 C ATOM 1874 O VAL A 269 67.273 73.852 -2.557 1.00 66.07 O ANISOU 1874 O VAL D 269 8185 8431 8484 30 29 -20 O ATOM 1875 CB VAL A 269 70.745 72.710 -1.698 1.00 65.18 C ANISOU 1875 CB VAL D 269 8214 8258 8293 23 -2 15 C ATOM 1876 CG1 VAL A 269 70.464 71.196 -1.470 1.00 65.31 C ANISOU 1876 CG1 VAL D 269 8303 8261 8250 0 5 5 C ATOM 1877 CG2 VAL A 269 72.134 72.918 -2.295 1.00 65.28 C ANISOU 1877 CG2 VAL D 269 8205 8347 8249 -20 -6 6 C ATOM 1878 N GLU A 270 68.129 72.832 -0.740 1.00 63.40 N ANISOU 1878 N GLU D 270 7987 8094 8007 -30 -34 -23 N ATOM 1879 CA GLU A 270 66.897 72.884 0.034 1.00 62.20 C ANISOU 1879 CA GLU D 270 7891 7907 7836 -17 55 4 C ATOM 1880 C GLU A 270 67.299 72.879 1.527 1.00 61.51 C ANISOU 1880 C GLU D 270 7814 7780 7776 -55 38 23 C ATOM 1881 O GLU A 270 66.807 72.061 2.324 1.00 63.16 O ANISOU 1881 O GLU D 270 8087 7951 7957 -60 -33 -23 O ATOM 1882 CB GLU A 270 65.982 71.683 -0.295 1.00 62.15 C ANISOU 1882 CB GLU D 270 7887 7898 7829 -31 52 12 C ATOM 1883 CG GLU A 270 66.239 70.989 -1.654 1.00 62.78 C ANISOU 1883 CG GLU D 270 7992 7957 7905 0 22 22 C ATOM 1884 CD GLU A 270 65.773 69.536 -1.691 1.00 63.69 C ANISOU 1884 CD GLU D 270 8087 7980 8131 4 55 18 C ATOM 1885 OE1 GLU A 270 65.378 68.993 -0.631 1.00 67.73 O ANISOU 1885 OE1 GLU D 270 8669 8653 8410 -3 -114 -79 O ATOM 1886 OE2 GLU A 270 65.822 68.928 -2.789 1.00 66.39 O ANISOU 1886 OE2 GLU D 270 8499 8446 8280 5 83 103 O ATOM 1887 N GLY A 271 68.210 73.775 1.903 1.00 59.67 N ANISOU 1887 N GLY D 271 7579 7556 7537 -2 36 23 N ATOM 1888 CA GLY A 271 68.667 73.852 3.297 1.00 58.65 C ANISOU 1888 CA GLY D 271 7401 7422 7460 31 22 8 C ATOM 1889 C GLY A 271 69.907 73.009 3.553 1.00 57.99 C ANISOU 1889 C GLY D 271 7342 7310 7379 30 56 44 C ATOM 1890 O GLY A 271 69.954 71.828 3.179 1.00 58.50 O ANISOU 1890 O GLY D 271 7430 7331 7463 46 106 66 O ATOM 1891 N LYS A 272 70.907 73.613 4.187 1.00 57.18 N ANISOU 1891 N LYS D 272 7242 7225 7259 14 25 32 N ATOM 1892 CA LYS A 272 72.222 72.998 4.313 1.00 57.16 C ANISOU 1892 CA LYS D 272 7253 7239 7224 -1 -9 24 C ATOM 1893 C LYS A 272 72.202 71.872 5.340 1.00 57.15 C ANISOU 1893 C LYS D 272 7269 7279 7166 12 -25 -15 C ATOM 1894 O LYS A 272 71.353 71.846 6.231 1.00 57.49 O ANISOU 1894 O LYS D 272 7311 7302 7229 17 -50 -17 O ATOM 1895 CB LYS A 272 73.267 74.045 4.705 1.00 56.48 C ANISOU 1895 CB LYS D 272 7152 7184 7121 -15 6 24 C ATOM 1896 CG LYS A 272 73.750 74.906 3.549 1.00 56.89 C ANISOU 1896 CG LYS D 272 7194 7275 7146 -46 1 2 C ATOM 1897 CD LYS A 272 74.639 76.038 4.038 1.00 57.15 C ANISOU 1897 CD LYS D 272 7321 7211 7180 -8 12 -1 C ATOM 1898 CE LYS A 272 73.876 76.987 4.948 1.00 57.61 C ANISOU 1898 CE LYS D 272 7352 7247 7288 54 4 -19 C ATOM 1899 NZ LYS A 272 74.723 78.125 5.400 1.00 58.03 N ANISOU 1899 NZ LYS D 272 7439 7300 7308 11 2 28 N ATOM 1900 N LYS A 273 73.150 70.948 5.219 1.00 57.41 N ANISOU 1900 N LYS D 273 7271 7340 7199 15 -29 -11 N ATOM 1901 CA LYS A 273 73.613 70.178 6.368 1.00 58.73 C ANISOU 1901 CA LYS D 273 7477 7433 7405 17 -5 10 C ATOM 1902 C LYS A 273 75.128 70.260 6.525 1.00 59.50 C ANISOU 1902 C LYS D 273 7537 7571 7498 12 -7 20 C ATOM 1903 O LYS A 273 75.852 70.476 5.554 1.00 59.20 O ANISOU 1903 O LYS D 273 7574 7569 7348 20 -15 11 O ATOM 1904 CB LYS A 273 73.173 68.717 6.248 1.00 58.72 C ANISOU 1904 CB LYS D 273 7480 7427 7402 -10 -9 38 C ATOM 1905 CG LYS A 273 71.744 68.462 6.698 1.00 58.82 C ANISOU 1905 CG LYS D 273 7501 7426 7423 -33 38 31 C ATOM 1906 CD LYS A 273 70.743 68.988 5.683 1.00 59.73 C ANISOU 1906 CD LYS D 273 7554 7599 7540 -29 22 44 C ATOM 1907 CE LYS A 273 69.447 68.195 5.723 1.00 60.23 C ANISOU 1907 CE LYS D 273 7522 7699 7660 -12 3 4 C ATOM 1908 NZ LYS A 273 68.282 69.012 5.285 1.00 62.22 N ANISOU 1908 NZ LYS D 273 7961 7728 7951 14 61 43 N ATOM 1909 N MET A 274 75.599 70.087 7.756 1.00 61.10 N ANISOU 1909 N MET D 274 7750 7767 7698 -1 38 24 N ATOM 1910 CA MET A 274 77.023 70.182 8.053 1.00 61.21 C ANISOU 1910 CA MET D 274 7749 7789 7718 6 51 12 C ATOM 1911 C MET A 274 77.668 68.801 8.106 1.00 63.12 C ANISOU 1911 C MET D 274 8056 7954 7971 13 38 14 C ATOM 1912 O MET A 274 78.431 68.427 7.215 1.00 64.75 O ANISOU 1912 O MET D 274 8342 8144 8115 9 25 40 O ATOM 1913 CB MET A 274 77.246 70.916 9.377 1.00 61.80 C ANISOU 1913 CB MET D 274 7884 7822 7772 10 61 -10 C ATOM 1914 CG MET A 274 78.439 71.858 9.372 1.00 62.39 C ANISOU 1914 CG MET D 274 7860 7920 7922 -25 91 -6 C ATOM 1915 SD MET A 274 79.893 71.137 8.587 1.00 67.39 S ANISOU 1915 SD MET D 274 8554 8720 8330 -79 -62 94 S ATOM 1916 CE MET A 274 80.974 72.563 8.500 1.00 63.76 C ANISOU 1916 CE MET D 274 8039 8156 8029 73 -28 31 C ATOM 1917 N PHE A 275 77.357 68.048 9.156 1.00 64.10 N ANISOU 1917 N PHE D 275 8144 8094 8115 -14 13 46 N ATOM 1918 CA PHE A 275 77.344 66.592 9.078 1.00 64.41 C ANISOU 1918 CA PHE D 275 8105 8202 8166 7 4 -4 C ATOM 1919 C PHE A 275 76.052 66.020 9.653 1.00 65.43 C ANISOU 1919 C PHE D 275 8225 8374 8260 18 -26 5 C ATOM 1920 O PHE A 275 75.757 64.836 9.484 1.00 66.08 O ANISOU 1920 O PHE D 275 8260 8501 8345 15 51 24 O ATOM 1921 CB PHE A 275 78.551 66.005 9.812 1.00 67.34 C ANISOU 1921 CB PHE D 275 8776 8377 8430 -234 313 -71 C ATOM 1922 CG PHE A 275 79.728 65.728 8.920 1.00 63.63 C ANISOU 1922 CG PHE D 275 7927 8083 8164 87 -136 4 C ATOM 1923 CD1 PHE A 275 80.220 66.710 8.076 1.00 65.08 C ANISOU 1923 CD1 PHE D 275 8259 8187 8278 -26 40 58 C ATOM 1924 CD2 PHE A 275 80.341 64.487 8.924 1.00 65.42 C ANISOU 1924 CD2 PHE D 275 8310 8223 8321 -76 -54 -109 C ATOM 1925 CE1 PHE A 275 81.302 66.459 7.254 1.00 64.95 C ANISOU 1925 CE1 PHE D 275 8050 8455 8170 76 -38 169 C ATOM 1926 CE2 PHE A 275 81.423 64.229 8.105 1.00 63.02 C ANISOU 1926 CE2 PHE D 275 7871 7956 8116 147 -125 34 C ATOM 1927 CZ PHE A 275 81.904 65.217 7.268 1.00 63.48 C ANISOU 1927 CZ PHE D 275 7934 8089 8093 103 -57 58 C ATOM 1928 N VAL A 276 75.286 66.867 10.332 1.00 20.00 N ATOM 1929 CA VAL A 276 73.861 66.626 10.525 1.00 20.00 C ATOM 1930 C VAL A 276 73.107 67.931 10.756 1.00 20.00 C ATOM 1931 O VAL A 276 72.941 68.370 11.894 1.00 20.00 O ATOM 1932 CB VAL A 276 73.605 65.679 11.712 1.00 20.00 C ATOM 1933 CG1 VAL A 276 72.831 64.451 11.256 1.00 20.00 C ATOM 1934 CG2 VAL A 276 74.917 65.277 12.367 1.00 20.00 C ATOM 1935 N GLU A 277 72.654 68.547 9.669 1.00 62.70 N ANISOU 1935 N GLU D 277 7986 7904 7930 30 10 6 N ATOM 1936 CA GLU A 277 72.090 69.890 9.728 1.00 60.43 C ANISOU 1936 CA GLU D 277 7709 7627 7624 -72 9 0 C ATOM 1937 C GLU A 277 73.187 70.946 9.808 1.00 59.30 C ANISOU 1937 C GLU D 277 7591 7483 7457 -28 15 -73 C ATOM 1938 O GLU A 277 74.371 70.619 9.895 1.00 60.55 O ANISOU 1938 O GLU D 277 7711 7684 7611 -14 47 -67 O ATOM 1939 CB GLU A 277 71.145 70.022 10.925 1.00 61.07 C ANISOU 1939 CB GLU D 277 7755 7759 7687 -58 -4 4 C ATOM 1940 CG GLU A 277 69.877 70.806 10.631 1.00 63.96 C ANISOU 1940 CG GLU D 277 8072 8066 8163 76 -16 6 C ATOM 1941 CD GLU A 277 68.785 69.944 10.028 1.00 70.25 C ANISOU 1941 CD GLU D 277 8913 8992 8783 -2 234 24 C ATOM 1942 OE1 GLU A 277 67.664 69.932 10.577 1.00 74.01 O ANISOU 1942 OE1 GLU D 277 9157 9504 9458 38 27 17 O ATOM 1943 OE2 GLU A 277 69.049 69.279 9.004 1.00 72.99 O ANISOU 1943 OE2 GLU D 277 9191 9394 9145 84 -132 -35 O ATOM 1944 N HIS A 278 72.786 72.213 9.778 1.00 56.39 N ANISOU 1944 N HIS D 278 7185 7127 7114 -24 29 -24 N ATOM 1945 CA HIS A 278 73.737 73.316 9.737 1.00 54.65 C ANISOU 1945 CA HIS D 278 6965 6980 6817 32 11 28 C ATOM 1946 C HIS A 278 73.242 74.503 10.557 1.00 53.24 C ANISOU 1946 C HIS D 278 6738 6862 6628 37 9 0 C ATOM 1947 O HIS A 278 72.146 75.015 10.327 1.00 53.78 O ANISOU 1947 O HIS D 278 6773 7015 6644 78 35 25 O ATOM 1948 CB HIS A 278 73.998 73.747 8.293 1.00 53.89 C ANISOU 1948 CB HIS D 278 6857 6870 6750 -3 22 17 C ATOM 1949 CG HIS A 278 75.175 74.659 8.137 1.00 54.17 C ANISOU 1949 CG HIS D 278 6922 6893 6764 32 -2 -7 C ATOM 1950 ND1 HIS A 278 75.119 76.004 8.435 1.00 52.80 N ANISOU 1950 ND1 HIS D 278 6676 6830 6553 38 -90 18 N ATOM 1951 CD2 HIS A 278 76.439 74.420 7.715 1.00 50.83 C ANISOU 1951 CD2 HIS D 278 6580 6429 6302 -5 149 -65 C ATOM 1952 CE1 HIS A 278 76.298 76.553 8.203 1.00 51.60 C ANISOU 1952 CE1 HIS D 278 6547 6558 6499 77 47 -9 C ATOM 1953 NE2 HIS A 278 77.117 75.614 7.765 1.00 50.13 N ANISOU 1953 NE2 HIS D 278 6281 6498 6268 35 179 49 N ATOM 1954 N LYS A 279 74.056 74.936 11.514 1.00 51.54 N ANISOU 1954 N LYS D 279 6512 6601 6468 25 -29 -8 N ATOM 1955 CA LYS A 279 73.585 75.788 12.588 1.00 50.04 C ANISOU 1955 CA LYS D 279 6325 6373 6313 5 -9 -62 C ATOM 1956 C LYS A 279 74.016 77.211 12.324 1.00 49.10 C ANISOU 1956 C LYS D 279 6185 6281 6187 27 -16 -50 C ATOM 1957 O LYS A 279 73.737 78.109 13.108 1.00 48.91 O ANISOU 1957 O LYS D 279 6122 6314 6147 79 -12 -31 O ATOM 1958 CB LYS A 279 74.157 75.322 13.925 1.00 49.57 C ANISOU 1958 CB LYS D 279 6330 6271 6232 7 -4 -48 C ATOM 1959 CG LYS A 279 73.547 74.053 14.471 1.00 48.26 C ANISOU 1959 CG LYS D 279 6150 6141 6044 2 -29 19 C ATOM 1960 CD LYS A 279 74.189 73.682 15.778 1.00 47.99 C ANISOU 1960 CD LYS D 279 6021 6099 6113 38 -53 26 C ATOM 1961 CE LYS A 279 73.436 72.581 16.462 1.00 45.90 C ANISOU 1961 CE LYS D 279 5839 5869 5732 127 -95 146 C ATOM 1962 NZ LYS A 279 74.128 71.297 16.364 1.00 42.18 N ANISOU 1962 NZ LYS D 279 5335 5455 5233 31 15 -175 N ATOM 1963 N GLY A 280 74.715 77.405 11.215 1.00 48.38 N ANISOU 1963 N GLY D 280 6131 6177 6073 36 20 -22 N ATOM 1964 CA GLY A 280 75.231 78.713 10.857 1.00 47.25 C ANISOU 1964 CA GLY D 280 5985 6050 5917 37 6 -9 C ATOM 1965 C GLY A 280 76.487 79.072 11.628 1.00 46.31 C ANISOU 1965 C GLY D 280 5940 5916 5738 43 -33 -28 C ATOM 1966 O GLY A 280 77.393 78.252 11.773 1.00 46.20 O ANISOU 1966 O GLY D 280 5935 5942 5675 100 -105 -3 O ATOM 1967 N SER A 281 76.539 80.304 12.125 1.00 45.18 N ANISOU 1967 N SER D 281 5778 5813 5575 66 -37 -57 N ATOM 1968 CA SER A 281 77.780 80.870 12.639 1.00 44.58 C ANISOU 1968 CA SER D 281 5725 5720 5493 49 -40 -69 C ATOM 1969 C SER A 281 77.910 80.647 14.142 1.00 43.97 C ANISOU 1969 C SER D 281 5591 5642 5473 64 -47 -85 C ATOM 1970 O SER A 281 76.985 80.926 14.904 1.00 43.93 O ANISOU 1970 O SER D 281 5685 5613 5391 146 -140 -142 O ATOM 1971 CB SER A 281 77.861 82.364 12.319 1.00 44.37 C ANISOU 1971 CB SER D 281 5793 5656 5410 74 -55 -77 C ATOM 1972 OG SER A 281 77.541 83.147 13.455 1.00 44.93 O ANISOU 1972 OG SER D 281 5990 5585 5494 124 -95 -172 O ATOM 1973 N LEU A 282 79.066 80.141 14.560 1.00 43.21 N ANISOU 1973 N LEU D 282 5446 5586 5385 39 -103 -59 N ATOM 1974 CA LEU A 282 79.363 79.975 15.966 1.00 42.25 C ANISOU 1974 CA LEU D 282 5347 5385 5319 37 -50 -24 C ATOM 1975 C LEU A 282 79.128 81.268 16.746 1.00 40.89 C ANISOU 1975 C LEU D 282 5145 5214 5175 68 -51 -91 C ATOM 1976 O LEU A 282 78.624 81.237 17.875 1.00 38.51 O ANISOU 1976 O LEU D 282 4663 5036 4933 213 -42 -251 O ATOM 1977 CB LEU A 282 80.814 79.524 16.107 1.00 42.58 C ANISOU 1977 CB LEU D 282 5379 5457 5340 42 -157 1 C ATOM 1978 CG LEU A 282 81.482 79.564 17.467 1.00 43.70 C ANISOU 1978 CG LEU D 282 5459 5645 5500 4 -5 -38 C ATOM 1979 CD1 LEU A 282 80.661 78.798 18.501 1.00 45.34 C ANISOU 1979 CD1 LEU D 282 5723 5830 5671 -21 -162 -68 C ATOM 1980 CD2 LEU A 282 82.880 78.978 17.346 1.00 43.17 C ANISOU 1980 CD2 LEU D 282 5457 5480 5465 30 -72 -11 C ATOM 1981 N GLU A 283 79.501 82.402 16.153 1.00 39.90 N ANISOU 1981 N GLU D 283 5083 5099 4978 20 -108 -143 N ATOM 1982 CA GLU A 283 79.327 83.682 16.825 1.00 39.64 C ANISOU 1982 CA GLU D 283 5018 5106 4937 15 -67 -83 C ATOM 1983 C GLU A 283 77.856 83.966 17.173 1.00 38.18 C ANISOU 1983 C GLU D 283 4938 4829 4739 13 -25 -94 C ATOM 1984 O GLU A 283 77.562 84.504 18.252 1.00 36.94 O ANISOU 1984 O GLU D 283 4837 4707 4489 108 -229 -209 O ATOM 1985 CB GLU A 283 79.898 84.837 15.997 1.00 40.62 C ANISOU 1985 CB GLU D 283 5169 5140 5121 19 -94 -41 C ATOM 1986 CG GLU A 283 79.668 86.204 16.647 1.00 40.07 C ANISOU 1986 CG GLU D 283 5173 5068 4984 -19 -111 -63 C ATOM 1987 CD GLU A 283 80.529 87.296 16.052 1.00 43.62 C ANISOU 1987 CD GLU D 283 5530 5503 5539 -128 -104 -53 C ATOM 1988 OE1 GLU A 283 79.997 88.068 15.204 1.00 49.35 O ANISOU 1988 OE1 GLU D 283 6156 6304 6289 121 -26 -355 O ATOM 1989 OE2 GLU A 283 81.733 87.376 16.425 1.00 47.67 O ANISOU 1989 OE2 GLU D 283 5672 6249 6191 -91 85 -162 O ATOM 1990 N ASP A 284 76.936 83.627 16.269 1.00 37.05 N ANISOU 1990 N ASP D 284 4786 4701 4589 -5 -91 -70 N ATOM 1991 CA ASP A 284 75.511 83.855 16.539 1.00 36.32 C ANISOU 1991 CA ASP D 284 4708 4574 4515 31 -78 -99 C ATOM 1992 C ASP A 284 75.012 82.932 17.647 1.00 34.69 C ANISOU 1992 C ASP D 284 4503 4341 4334 92 -79 -122 C ATOM 1993 O ASP A 284 74.234 83.352 18.491 1.00 34.08 O ANISOU 1993 O ASP D 284 4561 4261 4124 108 -114 -336 O ATOM 1994 CB ASP A 284 74.653 83.687 15.291 1.00 36.35 C ANISOU 1994 CB ASP D 284 4686 4618 4505 56 -29 -29 C ATOM 1995 CG ASP A 284 74.945 84.746 14.226 1.00 40.04 C ANISOU 1995 CG ASP D 284 5154 5071 4988 -41 -1 -107 C ATOM 1996 OD1 ASP A 284 75.519 85.829 14.549 1.00 38.63 O ANISOU 1996 OD1 ASP D 284 5155 4881 4643 -15 73 -253 O ATOM 1997 OD2 ASP A 284 74.593 84.471 13.047 1.00 43.20 O ANISOU 1997 OD2 ASP D 284 5555 5893 4963 -74 -16 -131 O ATOM 1998 N THR A 285 75.491 81.695 17.652 1.00 33.63 N ANISOU 1998 N THR D 285 4331 4256 4190 60 -100 -39 N ATOM 1999 CA THR A 285 75.155 80.746 18.701 1.00 32.47 C ANISOU 1999 CA THR D 285 4160 4135 4039 55 -75 10 C ATOM 2000 C THR A 285 75.586 81.231 20.085 1.00 30.65 C ANISOU 2000 C THR D 285 3882 3872 3890 87 -16 -98 C ATOM 2001 O THR A 285 74.813 81.116 21.040 1.00 30.91 O ANISOU 2001 O THR D 285 3874 3969 3902 178 -137 -165 O ATOM 2002 CB THR A 285 75.738 79.357 18.397 1.00 31.84 C ANISOU 2002 CB THR D 285 4049 4147 3902 63 -8 41 C ATOM 2003 OG1 THR A 285 75.039 78.806 17.269 1.00 30.95 O ANISOU 2003 OG1 THR D 285 3994 4543 3221 -62 -93 15 O ATOM 2004 CG2 THR A 285 75.593 78.405 19.589 1.00 32.99 C ANISOU 2004 CG2 THR D 285 4142 4240 4149 45 -119 -10 C ATOM 2005 N LEU A 286 76.793 81.784 20.190 1.00 29.86 N ANISOU 2005 N LEU D 286 3811 3787 3746 39 -134 -160 N ATOM 2006 CA LEU A 286 77.317 82.288 21.470 1.00 30.41 C ANISOU 2006 CA LEU D 286 3798 3876 3879 20 -119 -44 C ATOM 2007 C LEU A 286 76.572 83.535 21.977 1.00 29.35 C ANISOU 2007 C LEU D 286 3643 3717 3791 76 -65 -76 C ATOM 2008 O LEU A 286 76.370 83.699 23.195 1.00 28.94 O ANISOU 2008 O LEU D 286 3612 3386 3996 178 -283 6 O ATOM 2009 CB LEU A 286 78.828 82.593 21.379 1.00 30.99 C ANISOU 2009 CB LEU D 286 3851 3965 3959 58 -127 -51 C ATOM 2010 CG LEU A 286 79.802 81.418 21.355 1.00 29.35 C ANISOU 2010 CG LEU D 286 3524 3879 3746 53 24 -92 C ATOM 2011 CD1 LEU A 286 81.206 81.857 20.810 1.00 31.60 C ANISOU 2011 CD1 LEU D 286 3856 4102 4046 11 -72 -287 C ATOM 2012 CD2 LEU A 286 79.944 80.767 22.734 1.00 28.41 C ANISOU 2012 CD2 LEU D 286 3256 3781 3757 275 -298 -55 C ATOM 2013 N ILE A 287 76.188 84.409 21.050 1.00 30.63 N ANISOU 2013 N ILE D 287 3807 3844 3987 40 -202 -74 N ATOM 2014 CA ILE A 287 75.346 85.562 21.363 1.00 30.69 C ANISOU 2014 CA ILE D 287 3837 3863 3960 31 -95 -143 C ATOM 2015 C ILE A 287 73.973 85.146 21.912 1.00 29.25 C ANISOU 2015 C ILE D 287 3703 3649 3758 89 -80 -196 C ATOM 2016 O ILE A 287 73.523 85.682 22.914 1.00 25.91 O ANISOU 2016 O ILE D 287 3398 3006 3438 146 -237 -644 O ATOM 2017 CB ILE A 287 75.160 86.453 20.131 1.00 31.52 C ANISOU 2017 CB ILE D 287 3872 4006 4096 61 -37 -132 C ATOM 2018 CG1 ILE A 287 76.462 87.199 19.854 1.00 33.67 C ANISOU 2018 CG1 ILE D 287 4219 4306 4265 55 -117 -189 C ATOM 2019 CG2 ILE A 287 74.036 87.434 20.367 1.00 31.48 C ANISOU 2019 CG2 ILE D 287 4021 3892 4046 151 -20 -59 C ATOM 2020 CD1 ILE A 287 76.461 87.975 18.569 1.00 33.27 C ANISOU 2020 CD1 ILE D 287 4298 4165 4175 29 -178 -155 C ATOM 2021 N GLU A 288 73.337 84.196 21.239 1.00 29.93 N ANISOU 2021 N GLU D 288 3791 3734 3844 46 -45 -155 N ATOM 2022 CA GLU A 288 72.051 83.663 21.673 1.00 30.23 C ANISOU 2022 CA GLU D 288 3836 3848 3801 82 -53 -133 C ATOM 2023 C GLU A 288 72.184 82.955 23.029 1.00 28.64 C ANISOU 2023 C GLU D 288 3579 3700 3600 162 -64 -51 C ATOM 2024 O GLU A 288 71.365 83.158 23.935 1.00 27.80 O ANISOU 2024 O GLU D 288 3426 3544 3592 371 -109 -280 O ATOM 2025 CB GLU A 288 71.535 82.690 20.619 1.00 30.43 C ANISOU 2025 CB GLU D 288 3788 3985 3789 62 -62 -83 C ATOM 2026 CG GLU A 288 70.169 82.162 20.883 1.00 32.94 C ANISOU 2026 CG GLU D 288 4138 4167 4208 -97 -46 -102 C ATOM 2027 CD GLU A 288 69.725 81.185 19.818 1.00 36.67 C ANISOU 2027 CD GLU D 288 4825 4602 4506 -177 12 70 C ATOM 2028 OE1 GLU A 288 70.348 80.098 19.691 1.00 45.11 O ANISOU 2028 OE1 GLU D 288 5738 5493 5908 326 114 -146 O ATOM 2029 OE2 GLU A 288 68.751 81.512 19.092 1.00 48.30 O ANISOU 2029 OE2 GLU D 288 5647 6308 6396 192 325 -4 O ATOM 2030 N MET A 289 73.227 82.143 23.192 1.00 26.24 N ANISOU 2030 N MET D 289 3280 3388 3301 140 -123 -24 N ATOM 2031 CA MET A 289 73.513 81.577 24.514 1.00 27.37 C ANISOU 2031 CA MET D 289 3378 3499 3522 77 -78 -107 C ATOM 2032 C MET A 289 73.604 82.646 25.594 1.00 25.69 C ANISOU 2032 C MET D 289 3143 3217 3397 154 -88 -175 C ATOM 2033 O MET A 289 73.106 82.476 26.705 1.00 25.13 O ANISOU 2033 O MET D 289 3114 3062 3370 137 -150 -499 O ATOM 2034 CB MET A 289 74.805 80.778 24.515 1.00 26.32 C ANISOU 2034 CB MET D 289 3311 3428 3260 110 -109 -149 C ATOM 2035 CG MET A 289 74.633 79.356 24.069 1.00 30.00 C ANISOU 2035 CG MET D 289 3551 3871 3975 -42 -44 -70 C ATOM 2036 SD MET A 289 76.215 78.485 24.113 1.00 31.02 S ANISOU 2036 SD MET D 289 3776 3930 4081 344 -196 -189 S ATOM 2037 CE MET A 289 75.715 76.878 23.544 1.00 30.23 C ANISOU 2037 CE MET D 289 3690 3802 3993 188 78 -25 C ATOM 2038 N GLU A 290 74.237 83.766 25.281 1.00 26.14 N ANISOU 2038 N GLU D 290 3210 3301 3420 24 -154 -209 N ATOM 2039 CA GLU A 290 74.376 84.808 26.275 1.00 26.37 C ANISOU 2039 CA GLU D 290 3270 3343 3405 19 -110 -106 C ATOM 2040 C GLU A 290 73.038 85.475 26.563 1.00 25.41 C ANISOU 2040 C GLU D 290 3220 3091 3341 -101 -108 -123 C ATOM 2041 O GLU A 290 72.718 85.744 27.725 1.00 24.57 O ANISOU 2041 O GLU D 290 3046 2796 3493 213 -351 140 O ATOM 2042 CB GLU A 290 75.388 85.857 25.838 1.00 26.31 C ANISOU 2042 CB GLU D 290 3297 3382 3315 -8 -32 -178 C ATOM 2043 CG GLU A 290 75.589 86.943 26.876 1.00 27.01 C ANISOU 2043 CG GLU D 290 3415 3385 3462 -61 -247 -96 C ATOM 2044 CD GLU A 290 76.728 87.886 26.538 1.00 31.10 C ANISOU 2044 CD GLU D 290 3893 3806 4115 -186 -106 -40 C ATOM 2045 OE1 GLU A 290 77.279 87.788 25.399 1.00 33.95 O ANISOU 2045 OE1 GLU D 290 4281 4423 4194 -524 -413 -444 O ATOM 2046 OE2 GLU A 290 77.048 88.722 27.420 1.00 35.28 O ANISOU 2046 OE2 GLU D 290 4760 4042 4603 -306 50 55 O ATOM 2047 N GLN A 291 72.261 85.723 25.522 1.00 25.13 N ANISOU 2047 N GLN D 291 3092 3138 3318 -91 -126 -282 N ATOM 2048 CA GLN A 291 70.937 86.309 25.700 1.00 26.35 C ANISOU 2048 CA GLN D 291 3275 3317 3419 -19 -150 -132 C ATOM 2049 C GLN A 291 70.003 85.417 26.509 1.00 25.54 C ANISOU 2049 C GLN D 291 3296 3177 3227 -36 -128 -205 C ATOM 2050 O GLN A 291 69.281 85.899 27.400 1.00 25.85 O ANISOU 2050 O GLN D 291 3367 3187 3266 -1 -157 -272 O ATOM 2051 CB GLN A 291 70.291 86.585 24.355 1.00 25.47 C ANISOU 2051 CB GLN D 291 3204 3347 3123 -34 -186 -131 C ATOM 2052 CG GLN A 291 70.933 87.792 23.671 1.00 29.97 C ANISOU 2052 CG GLN D 291 3773 3701 3912 -13 -101 -183 C ATOM 2053 CD GLN A 291 70.583 87.890 22.213 1.00 30.39 C ANISOU 2053 CD GLN D 291 3805 3998 3743 64 -157 -166 C ATOM 2054 OE1 GLN A 291 70.017 86.956 21.615 1.00 38.66 O ANISOU 2054 OE1 GLN D 291 4830 4877 4980 -211 53 -112 O ATOM 2055 NE2 GLN A 291 70.937 89.023 21.608 1.00 35.04 N ANISOU 2055 NE2 GLN D 291 4450 4191 4672 119 -104 -321 N ATOM 2056 N ASP A 292 70.007 84.132 26.172 1.00 24.44 N ANISOU 2056 N ASP D 292 3052 3175 3056 -20 -144 -169 N ATOM 2057 CA ASP A 292 69.185 83.136 26.888 1.00 23.74 C ANISOU 2057 CA ASP D 292 2942 3013 3064 -2 -67 -185 C ATOM 2058 C ASP A 292 69.570 83.051 28.339 1.00 21.96 C ANISOU 2058 C ASP D 292 2699 2704 2937 25 3 -289 C ATOM 2059 O ASP A 292 68.714 83.016 29.233 1.00 22.68 O ANISOU 2059 O ASP D 292 2628 2858 3129 157 -19 -494 O ATOM 2060 CB ASP A 292 69.274 81.770 26.212 1.00 23.44 C ANISOU 2060 CB ASP D 292 2950 2984 2973 -8 -18 -194 C ATOM 2061 CG ASP A 292 68.637 81.767 24.856 1.00 27.46 C ANISOU 2061 CG ASP D 292 3527 3538 3364 -10 17 -127 C ATOM 2062 OD1 ASP A 292 67.910 82.746 24.561 1.00 30.68 O ANISOU 2062 OD1 ASP D 292 3847 3714 4093 156 -200 -356 O ATOM 2063 OD2 ASP A 292 68.833 80.795 24.104 1.00 28.28 O ANISOU 2063 OD2 ASP D 292 3959 3658 3125 -86 -295 -142 O ATOM 2064 N LEU A 293 70.863 83.070 28.595 1.00 22.51 N ANISOU 2064 N LEU D 293 2773 2786 2993 -130 -66 -285 N ATOM 2065 CA LEU A 293 71.356 83.087 29.970 1.00 22.23 C ANISOU 2065 CA LEU D 293 2809 2816 2819 -1 -66 -189 C ATOM 2066 C LEU A 293 71.017 84.369 30.779 1.00 22.56 C ANISOU 2066 C LEU D 293 2814 2913 2844 -55 -62 -198 C ATOM 2067 O LEU A 293 70.710 84.303 31.974 1.00 19.56 O ANISOU 2067 O LEU D 293 2548 2611 2271 -117 158 -85 O ATOM 2068 CB LEU A 293 72.853 82.812 29.949 1.00 22.09 C ANISOU 2068 CB LEU D 293 2698 3159 2537 -138 -142 -117 C ATOM 2069 CG LEU A 293 73.509 82.282 31.208 1.00 23.41 C ANISOU 2069 CG LEU D 293 2702 2984 3209 47 20 -265 C ATOM 2070 CD1 LEU A 293 72.754 81.143 31.929 1.00 25.31 C ANISOU 2070 CD1 LEU D 293 2954 3280 3380 51 43 -77 C ATOM 2071 CD2 LEU A 293 74.950 81.844 30.788 1.00 24.32 C ANISOU 2071 CD2 LEU D 293 3000 2940 3300 191 -230 -153 C ATOM 2072 N GLN A 294 71.017 85.525 30.122 1.00 22.89 N ANISOU 2072 N GLN D 294 2763 2805 3127 -29 -114 -188 N ATOM 2073 CA GLN A 294 70.506 86.771 30.727 1.00 21.46 C ANISOU 2073 CA GLN D 294 2668 2735 2747 -24 -53 -83 C ATOM 2074 C GLN A 294 69.023 86.653 31.091 1.00 21.30 C ANISOU 2074 C GLN D 294 2713 2692 2687 82 -54 -46 C ATOM 2075 O GLN A 294 68.613 87.131 32.143 1.00 20.11 O ANISOU 2075 O GLN D 294 2650 2546 2442 144 -204 -221 O ATOM 2076 CB GLN A 294 70.710 87.972 29.770 1.00 20.14 C ANISOU 2076 CB GLN D 294 2501 2606 2544 123 159 -199 C ATOM 2077 CG GLN A 294 72.168 88.357 29.603 1.00 21.59 C ANISOU 2077 CG GLN D 294 2809 2681 2711 -123 15 -247 C ATOM 2078 CD GLN A 294 72.388 89.471 28.627 1.00 22.83 C ANISOU 2078 CD GLN D 294 2932 2802 2939 -84 19 -111 C ATOM 2079 OE1 GLN A 294 71.814 89.473 27.526 1.00 27.13 O ANISOU 2079 OE1 GLN D 294 3755 3520 3030 -1 -109 -477 O ATOM 2080 NE2 GLN A 294 73.230 90.436 29.016 1.00 26.75 N ANISOU 2080 NE2 GLN D 294 2882 3256 4022 -286 -97 -444 N ATOM 2081 N SER A 295 68.232 86.031 30.216 1.00 21.07 N ANISOU 2081 N SER D 295 2549 2594 2862 109 85 -197 N ATOM 2082 CA SER A 295 66.832 85.743 30.537 1.00 21.76 C ANISOU 2082 CA SER D 295 2624 2703 2940 71 -21 -29 C ATOM 2083 C SER A 295 66.678 84.871 31.762 1.00 21.26 C ANISOU 2083 C SER D 295 2523 2552 3001 94 -24 -24 C ATOM 2084 O SER A 295 65.835 85.145 32.620 1.00 21.41 O ANISOU 2084 O SER D 295 2381 2386 3367 258 -231 -68 O ATOM 2085 CB SER A 295 66.120 85.076 29.371 1.00 22.72 C ANISOU 2085 CB SER D 295 2856 2869 2907 154 4 7 C ATOM 2086 OG SER A 295 66.078 85.922 28.258 1.00 26.61 O ANISOU 2086 OG SER D 295 3533 2880 3697 54 -200 -323 O ATOM 2087 N SER A 296 67.514 83.839 31.867 1.00 22.01 N ANISOU 2087 N SER D 296 2672 2530 3160 64 -142 88 N ATOM 2088 CA SER A 296 67.576 82.978 33.048 1.00 19.48 C ANISOU 2088 CA SER D 296 2401 2377 2623 57 -42 107 C ATOM 2089 C SER A 296 67.848 83.766 34.298 1.00 18.67 C ANISOU 2089 C SER D 296 2304 2316 2472 58 -60 -5 C ATOM 2090 O SER A 296 67.148 83.597 35.244 1.00 16.31 O ANISOU 2090 O SER D 296 2256 2073 1868 -17 -153 78 O ATOM 2091 CB SER A 296 68.676 81.878 32.919 1.00 19.07 C ANISOU 2091 CB SER D 296 2290 2319 2637 23 -60 15 C ATOM 2092 OG SER A 296 68.351 80.926 31.948 1.00 18.35 O ANISOU 2092 OG SER D 296 2146 2280 2543 151 -85 28 O ATOM 2093 N ILE A 297 68.833 84.662 34.272 1.00 19.29 N ANISOU 2093 N ILE D 297 2256 2477 2594 73 13 48 N ATOM 2094 CA ILE A 297 69.137 85.530 35.434 1.00 19.28 C ANISOU 2094 CA ILE D 297 2348 2395 2581 -17 15 46 C ATOM 2095 C ILE A 297 67.942 86.438 35.749 1.00 17.71 C ANISOU 2095 C ILE D 297 2197 2101 2428 -82 26 68 C ATOM 2096 O ILE A 297 67.620 86.647 36.912 1.00 18.70 O ANISOU 2096 O ILE D 297 2195 2026 2882 -193 -137 -62 O ATOM 2097 CB ILE A 297 70.463 86.376 35.216 1.00 18.94 C ANISOU 2097 CB ILE D 297 2272 2612 2312 23 -79 36 C ATOM 2098 CG1 ILE A 297 71.658 85.424 35.046 1.00 20.54 C ANISOU 2098 CG1 ILE D 297 2517 2624 2660 -14 -79 -99 C ATOM 2099 CG2 ILE A 297 70.712 87.355 36.393 1.00 19.56 C ANISOU 2099 CG2 ILE D 297 2218 2360 2853 44 -6 1 C ATOM 2100 CD1 ILE A 297 72.905 86.076 34.528 1.00 21.96 C ANISOU 2100 CD1 ILE D 297 2520 2648 3175 -101 99 -73 C ATOM 2101 N SER A 298 67.272 86.952 34.719 1.00 17.83 N ANISOU 2101 N SER D 298 2286 2060 2427 -17 -9 46 N ATOM 2102 CA ASER A 298 66.071 87.766 34.930 0.50 19.28 C ANISOU 2102 CA ASER D 298 2413 2373 2537 22 -1 61 C ATOM 2103 C SER A 298 65.019 86.984 35.716 1.00 19.05 C ANISOU 2103 C SER D 298 2390 2306 2542 33 2 17 C ATOM 2104 O SER A 298 64.505 87.451 36.732 1.00 18.79 O ANISOU 2104 O SER D 298 2776 1954 2408 109 129 123 O ATOM 2105 CB ASER A 298 65.498 88.233 33.593 0.50 19.63 C ANISOU 2105 CB ASER D 298 2560 2274 2622 129 -55 -97 C ATOM 2106 OG ASER A 298 66.484 88.970 32.895 0.50 24.37 O ANISOU 2106 OG ASER D 298 2891 3020 3349 -95 -163 -81 O ATOM 2107 N TYR A 299 64.685 85.804 35.217 1.00 20.12 N ANISOU 2107 N TYR D 299 2411 2294 2938 82 -129 44 N ATOM 2108 CA TYR A 299 63.741 84.916 35.902 1.00 19.78 C ANISOU 2108 CA TYR D 299 2409 2453 2652 -21 -25 42 C ATOM 2109 C TYR A 299 64.178 84.500 37.285 1.00 19.03 C ANISOU 2109 C TYR D 299 2492 2226 2512 -159 -103 272 C ATOM 2110 O TYR A 299 63.327 84.259 38.097 1.00 19.33 O ANISOU 2110 O TYR D 299 2363 2576 2404 -35 -268 476 O ATOM 2111 CB TYR A 299 63.478 83.643 35.072 1.00 21.88 C ANISOU 2111 CB TYR D 299 2750 2646 2917 49 2 127 C ATOM 2112 CG TYR A 299 62.489 83.833 33.940 1.00 19.99 C ANISOU 2112 CG TYR D 299 2540 2270 2784 190 -14 104 C ATOM 2113 CD1 TYR A 299 61.152 84.110 34.218 1.00 22.41 C ANISOU 2113 CD1 TYR D 299 2538 2628 3345 49 29 -159 C ATOM 2114 CD2 TYR A 299 62.860 83.709 32.628 1.00 24.48 C ANISOU 2114 CD2 TYR D 299 2855 3333 3111 146 22 -68 C ATOM 2115 CE1 TYR A 299 60.247 84.302 33.224 1.00 20.69 C ANISOU 2115 CE1 TYR D 299 2678 2808 2374 -215 -80 213 C ATOM 2116 CE2 TYR A 299 61.924 83.896 31.586 1.00 24.02 C ANISOU 2116 CE2 TYR D 299 2921 3342 2862 -52 154 352 C ATOM 2117 CZ TYR A 299 60.616 84.195 31.908 1.00 21.40 C ANISOU 2117 CZ TYR D 299 2729 2679 2722 -41 4 166 C ATOM 2118 OH TYR A 299 59.604 84.386 30.972 1.00 25.97 O ANISOU 2118 OH TYR D 299 3323 3660 2883 181 141 279 O ATOM 2119 N ALA A 300 65.489 84.377 37.528 1.00 18.42 N ANISOU 2119 N ALA D 300 2341 2325 2332 79 156 179 N ATOM 2120 CA ALA A 300 66.016 84.019 38.866 1.00 20.74 C ANISOU 2120 CA ALA D 300 2592 2634 2652 36 -51 32 C ATOM 2121 C ALA A 300 65.906 85.145 39.889 1.00 21.11 C ANISOU 2121 C ALA D 300 2598 2650 2771 43 -2 56 C ATOM 2122 O ALA A 300 66.241 84.940 41.038 1.00 21.08 O ANISOU 2122 O ALA D 300 2633 2623 2753 302 -129 -9 O ATOM 2123 CB ALA A 300 67.466 83.556 38.782 1.00 20.31 C ANISOU 2123 CB ALA D 300 2596 2533 2586 -23 95 54 C ATOM 2124 N GLY A 301 65.456 86.330 39.476 1.00 22.32 N ANISOU 2124 N GLY D 301 2664 2722 3094 79 -6 19 N ATOM 2125 CA GLY A 301 65.297 87.450 40.424 1.00 22.12 C ANISOU 2125 CA GLY D 301 2819 2743 2840 41 -10 -10 C ATOM 2126 C GLY A 301 66.602 88.131 40.802 1.00 22.69 C ANISOU 2126 C GLY D 301 3003 2732 2886 34 40 -33 C ATOM 2127 O GLY A 301 66.710 88.745 41.867 1.00 24.55 O ANISOU 2127 O GLY D 301 3233 2944 3151 0 149 -86 O ATOM 2128 N GLY A 302 67.595 88.038 39.920 1.00 22.86 N ANISOU 2128 N GLY D 302 2907 2732 3043 -38 63 1 N ATOM 2129 CA GLY A 302 68.905 88.631 40.156 1.00 23.55 C ANISOU 2129 CA GLY D 302 2984 2975 2987 -1 43 11 C ATOM 2130 C GLY A 302 69.417 89.457 39.011 1.00 23.53 C ANISOU 2130 C GLY D 302 2860 2942 3137 -86 109 -71 C ATOM 2131 O GLY A 302 68.708 89.737 38.062 1.00 19.49 O ANISOU 2131 O GLY D 302 2594 2695 2116 -396 203 8 O ATOM 2132 N THR A 303 70.671 89.872 39.128 1.00 25.25 N ANISOU 2132 N THR D 303 2961 3057 3575 6 149 51 N ATOM 2133 CA THR A 303 71.342 90.569 38.048 1.00 25.08 C ANISOU 2133 CA THR D 303 3119 3097 3311 1 66 56 C ATOM 2134 C THR A 303 72.646 89.897 37.620 1.00 26.20 C ANISOU 2134 C THR D 303 3199 3324 3430 -76 109 -45 C ATOM 2135 O THR A 303 73.301 90.367 36.683 1.00 27.18 O ANISOU 2135 O THR D 303 3138 3585 3604 -227 -88 -358 O ATOM 2136 CB THR A 303 71.686 92.007 38.501 1.00 26.59 C ANISOU 2136 CB THR D 303 3365 3216 3522 95 90 67 C ATOM 2137 OG1 THR A 303 72.685 91.939 39.526 1.00 24.22 O ANISOU 2137 OG1 THR D 303 3226 2527 3448 -329 240 751 O ATOM 2138 CG2 THR A 303 70.428 92.690 39.087 1.00 28.08 C ANISOU 2138 CG2 THR D 303 3325 3385 3959 -30 -2 94 C ATOM 2139 N LYS A 304 73.050 88.819 38.305 1.00 26.89 N ANISOU 2139 N LYS D 304 3185 3263 3766 -23 40 20 N ATOM 2140 CA LYS A 304 74.281 88.135 37.931 1.00 26.26 C ANISOU 2140 CA LYS D 304 3218 3152 3606 39 -19 83 C ATOM 2141 C LYS A 304 74.123 86.616 38.026 1.00 25.29 C ANISOU 2141 C LYS D 304 3019 3090 3499 84 -80 -25 C ATOM 2142 O LYS A 304 73.126 86.115 38.534 1.00 22.89 O ANISOU 2142 O LYS D 304 2612 2713 3371 74 -52 -81 O ATOM 2143 CB LYS A 304 75.450 88.648 38.770 1.00 27.80 C ANISOU 2143 CB LYS D 304 3242 3426 3891 60 -123 -17 C ATOM 2144 CG LYS A 304 75.314 88.444 40.240 1.00 30.47 C ANISOU 2144 CG LYS D 304 3833 3964 3777 33 161 241 C ATOM 2145 CD LYS A 304 76.272 89.386 41.017 1.00 30.87 C ANISOU 2145 CD LYS D 304 3841 3856 4030 -75 149 204 C ATOM 2146 CE LYS A 304 76.517 88.892 42.430 1.00 37.15 C ANISOU 2146 CE LYS D 304 4815 4838 4462 77 52 -95 C ATOM 2147 NZ LYS A 304 75.445 89.234 43.423 1.00 43.32 N ANISOU 2147 NZ LYS D 304 5106 5835 5516 44 -260 136 N ATOM 2148 N LEU A 305 75.113 85.907 37.490 1.00 24.64 N ANISOU 2148 N LEU D 305 3010 3000 3352 64 -11 149 N ATOM 2149 CA LEU A 305 75.039 84.468 37.308 1.00 23.68 C ANISOU 2149 CA LEU D 305 2892 2932 3172 82 -23 72 C ATOM 2150 C LEU A 305 74.732 83.701 38.582 1.00 21.72 C ANISOU 2150 C LEU D 305 2685 2703 2864 117 -67 261 C ATOM 2151 O LEU A 305 73.908 82.767 38.597 1.00 21.30 O ANISOU 2151 O LEU D 305 2578 2788 2725 20 82 336 O ATOM 2152 CB LEU A 305 76.367 83.994 36.695 1.00 24.22 C ANISOU 2152 CB LEU D 305 2920 2963 3318 35 -83 1 C ATOM 2153 CG LEU A 305 76.351 82.616 36.074 1.00 23.60 C ANISOU 2153 CG LEU D 305 2969 2994 3001 91 -75 58 C ATOM 2154 CD1 LEU A 305 75.463 82.569 34.841 1.00 22.75 C ANISOU 2154 CD1 LEU D 305 2807 2781 3055 34 -122 190 C ATOM 2155 CD2 LEU A 305 77.804 82.218 35.792 1.00 26.16 C ANISOU 2155 CD2 LEU D 305 3239 3146 3553 105 -109 239 C ATOM 2156 N ASP A 306 75.357 84.109 39.675 1.00 21.46 N ANISOU 2156 N ASP D 306 2599 2530 3023 -8 44 108 N ATOM 2157 CA ASP A 306 75.161 83.418 40.941 1.00 22.54 C ANISOU 2157 CA ASP D 306 2827 2819 2919 15 31 91 C ATOM 2158 C ASP A 306 73.736 83.448 41.462 1.00 21.43 C ANISOU 2158 C ASP D 306 2724 2657 2760 -64 168 104 C ATOM 2159 O ASP A 306 73.363 82.625 42.320 1.00 21.92 O ANISOU 2159 O ASP D 306 2823 2559 2944 -97 173 41 O ATOM 2160 CB ASP A 306 76.152 83.926 41.992 1.00 23.19 C ANISOU 2160 CB ASP D 306 2963 2922 2927 -41 -36 101 C ATOM 2161 CG ASP A 306 77.601 83.482 41.685 1.00 30.56 C ANISOU 2161 CG ASP D 306 3481 4018 4111 99 5 104 C ATOM 2162 OD1 ASP A 306 77.803 82.562 40.845 1.00 31.89 O ANISOU 2162 OD1 ASP D 306 3789 3712 4612 158 -89 153 O ATOM 2163 OD2 ASP A 306 78.532 84.075 42.256 1.00 33.14 O ANISOU 2163 OD2 ASP D 306 4359 3804 4428 -176 256 157 O ATOM 2164 N SER A 307 72.919 84.372 40.963 1.00 20.91 N ANISOU 2164 N SER D 307 2806 2361 2775 -136 44 92 N ATOM 2165 CA SER A 307 71.509 84.382 41.356 1.00 20.34 C ANISOU 2165 CA SER D 307 2672 2513 2543 -21 -18 121 C ATOM 2166 C SER A 307 70.800 83.063 40.997 1.00 19.12 C ANISOU 2166 C SER D 307 2543 2385 2338 -34 -20 77 C ATOM 2167 O SER A 307 69.855 82.677 41.651 1.00 18.72 O ANISOU 2167 O SER D 307 2896 2387 1830 23 172 31 O ATOM 2168 CB SER A 307 70.769 85.571 40.746 1.00 19.31 C ANISOU 2168 CB SER D 307 2633 2578 2127 92 -132 54 C ATOM 2169 OG SER A 307 70.673 85.480 39.328 1.00 22.80 O ANISOU 2169 OG SER D 307 2881 3406 2373 -119 300 65 O ATOM 2170 N ILE A 308 71.230 82.414 39.920 1.00 19.73 N ANISOU 2170 N ILE D 308 2689 2422 2386 -100 -46 184 N ATOM 2171 CA ILE A 308 70.641 81.125 39.490 1.00 20.10 C ANISOU 2171 CA ILE D 308 2626 2461 2548 -86 -2 141 C ATOM 2172 C ILE A 308 70.828 80.046 40.584 1.00 20.56 C ANISOU 2172 C ILE D 308 2547 2481 2781 -43 23 167 C ATOM 2173 O ILE A 308 69.977 79.172 40.756 1.00 19.88 O ANISOU 2173 O ILE D 308 2343 2487 2721 -95 69 312 O ATOM 2174 CB ILE A 308 71.198 80.705 38.042 1.00 18.98 C ANISOU 2174 CB ILE D 308 2466 2258 2487 -106 131 170 C ATOM 2175 CG1 ILE A 308 70.843 81.771 37.017 1.00 19.78 C ANISOU 2175 CG1 ILE D 308 2656 2221 2637 -215 -16 193 C ATOM 2176 CG2 ILE A 308 70.635 79.350 37.552 1.00 19.59 C ANISOU 2176 CG2 ILE D 308 2742 2432 2268 -79 -152 135 C ATOM 2177 CD1 ILE A 308 71.513 81.635 35.692 1.00 21.32 C ANISOU 2177 CD1 ILE D 308 2987 2543 2568 18 64 202 C ATOM 2178 N ARG A 309 71.913 80.138 41.359 1.00 20.08 N ANISOU 2178 N ARG D 309 2616 2470 2540 -210 134 194 N ATOM 2179 CA ARG A 309 72.255 79.165 42.392 1.00 21.14 C ANISOU 2179 CA ARG D 309 2693 2581 2757 -58 62 103 C ATOM 2180 C ARG A 309 71.277 79.054 43.584 1.00 20.29 C ANISOU 2180 C ARG D 309 2665 2538 2505 -148 149 137 C ATOM 2181 O ARG A 309 71.310 78.080 44.295 1.00 22.81 O ANISOU 2181 O ARG D 309 2917 2975 2772 -244 66 101 O ATOM 2182 CB ARG A 309 73.685 79.429 42.923 1.00 20.89 C ANISOU 2182 CB ARG D 309 2776 2476 2683 42 97 69 C ATOM 2183 CG ARG A 309 74.762 79.372 41.813 1.00 22.14 C ANISOU 2183 CG ARG D 309 2636 2893 2883 -22 26 83 C ATOM 2184 CD ARG A 309 76.207 79.419 42.365 1.00 22.92 C ANISOU 2184 CD ARG D 309 2785 3042 2878 68 16 296 C ATOM 2185 NE ARG A 309 77.152 79.627 41.265 1.00 27.52 N ANISOU 2185 NE ARG D 309 3169 3583 3704 -242 -103 193 N ATOM 2186 CZ ARG A 309 77.532 78.671 40.405 1.00 27.45 C ANISOU 2186 CZ ARG D 309 3646 3665 3116 -16 -158 79 C ATOM 2187 NH1 ARG A 309 77.058 77.417 40.501 1.00 21.42 N ANISOU 2187 NH1 ARG D 309 2932 3501 1705 17 -144 246 N ATOM 2188 NH2 ARG A 309 78.390 78.981 39.426 1.00 28.57 N ANISOU 2188 NH2 ARG D 309 3485 3615 3753 -258 -213 124 N ATOM 2189 N THR A 310 70.420 80.025 43.810 1.00 21.65 N ANISOU 2189 N THR D 310 2578 3018 2628 -172 90 117 N ATOM 2190 CA THR A 310 69.517 79.952 44.968 1.00 23.16 C ANISOU 2190 CA THR D 310 2833 3118 2846 -24 25 156 C ATOM 2191 C THR A 310 68.039 79.947 44.633 1.00 23.29 C ANISOU 2191 C THR D 310 2741 3202 2903 -31 -28 240 C ATOM 2192 O THR A 310 67.208 80.171 45.541 1.00 25.41 O ANISOU 2192 O THR D 310 2998 3658 2998 -149 -52 368 O ATOM 2193 CB THR A 310 69.761 81.079 46.000 1.00 24.23 C ANISOU 2193 CB THR D 310 2989 3145 3070 -5 -48 232 C ATOM 2194 OG1 THR A 310 69.749 82.334 45.349 1.00 22.63 O ANISOU 2194 OG1 THR D 310 3552 3176 1869 -4 -835 188 O ATOM 2195 CG2 THR A 310 71.091 80.878 46.753 1.00 28.21 C ANISOU 2195 CG2 THR D 310 3490 4050 3178 41 134 121 C ATOM 2196 N VAL A 311 67.698 79.682 43.377 1.00 21.33 N ANISOU 2196 N VAL D 311 2622 2854 2627 -63 -100 81 N ATOM 2197 CA VAL A 311 66.305 79.488 43.030 1.00 20.68 C ANISOU 2197 CA VAL D 311 2623 2675 2560 52 -1 144 C ATOM 2198 C VAL A 311 65.773 78.129 43.500 1.00 20.52 C ANISOU 2198 C VAL D 311 2647 2717 2430 58 67 95 C ATOM 2199 O VAL A 311 66.520 77.127 43.637 1.00 19.01 O ANISOU 2199 O VAL D 311 2373 2772 2074 105 407 338 O ATOM 2200 CB VAL A 311 66.019 79.631 41.536 1.00 19.14 C ANISOU 2200 CB VAL D 311 2444 2493 2334 33 -185 48 C ATOM 2201 CG1 VAL A 311 66.311 81.056 41.066 1.00 21.01 C ANISOU 2201 CG1 VAL D 311 2896 2494 2592 -75 -104 313 C ATOM 2202 CG2 VAL A 311 66.774 78.570 40.685 1.00 17.88 C ANISOU 2202 CG2 VAL D 311 2068 2403 2323 -46 129 80 C ATOM 2203 N ASP A 312 64.465 78.071 43.702 1.00 21.24 N ANISOU 2203 N ASP D 312 2736 2813 2519 66 21 33 N ATOM 2204 CA ASP A 312 63.823 76.792 43.989 1.00 20.42 C ANISOU 2204 CA ASP D 312 2610 2553 2595 20 -1 52 C ATOM 2205 C ASP A 312 63.604 76.064 42.686 1.00 18.76 C ANISOU 2205 C ASP D 312 2317 2315 2494 49 62 12 C ATOM 2206 O ASP A 312 63.779 76.643 41.620 1.00 18.66 O ANISOU 2206 O ASP D 312 2279 2314 2495 95 -312 238 O ATOM 2207 CB ASP A 312 62.510 76.974 44.733 1.00 22.58 C ANISOU 2207 CB ASP D 312 2875 2612 3092 -29 -57 42 C ATOM 2208 CG ASP A 312 62.101 75.708 45.522 1.00 24.13 C ANISOU 2208 CG ASP D 312 3222 3236 2707 -43 27 -223 C ATOM 2209 OD1 ASP A 312 62.907 74.720 45.628 1.00 28.87 O ANISOU 2209 OD1 ASP D 312 3792 3543 3631 68 -178 392 O ATOM 2210 OD2 ASP A 312 60.958 75.706 46.026 1.00 31.50 O ANISOU 2210 OD2 ASP D 312 3748 4324 3893 225 -161 -4 O ATOM 2211 N TYR A 313 63.220 74.788 42.764 1.00 20.04 N ANISOU 2211 N TYR D 313 2588 2541 2485 134 -12 -21 N ATOM 2212 CA TYR A 313 62.993 73.996 41.563 1.00 19.48 C ANISOU 2212 CA TYR D 313 2437 2393 2570 -51 105 9 C ATOM 2213 C TYR A 313 61.945 72.928 41.844 1.00 19.45 C ANISOU 2213 C TYR D 313 2475 2401 2514 -34 66 -59 C ATOM 2214 O TYR A 313 61.573 72.697 42.976 1.00 19.29 O ANISOU 2214 O TYR D 313 2608 2342 2378 -212 118 -92 O ATOM 2215 CB TYR A 313 64.289 73.345 41.078 1.00 19.44 C ANISOU 2215 CB TYR D 313 2585 2322 2478 -168 69 20 C ATOM 2216 CG TYR A 313 64.818 72.305 42.032 1.00 20.27 C ANISOU 2216 CG TYR D 313 2565 2446 2690 138 -35 166 C ATOM 2217 CD1 TYR A 313 64.450 70.968 41.893 1.00 19.94 C ANISOU 2217 CD1 TYR D 313 2756 2311 2508 -161 -291 -474 C ATOM 2218 CD2 TYR A 313 65.680 72.640 43.044 1.00 20.84 C ANISOU 2218 CD2 TYR D 313 2795 2685 2436 239 -98 146 C ATOM 2219 CE1 TYR A 313 64.921 70.028 42.736 1.00 22.21 C ANISOU 2219 CE1 TYR D 313 2620 2757 3060 162 241 -464 C ATOM 2220 CE2 TYR A 313 66.159 71.676 43.926 1.00 21.50 C ANISOU 2220 CE2 TYR D 313 2889 2512 2768 100 52 -72 C ATOM 2221 CZ TYR A 313 65.759 70.387 43.767 1.00 23.56 C ANISOU 2221 CZ TYR D 313 3353 2601 2996 8 218 -90 C ATOM 2222 OH TYR A 313 66.222 69.402 44.607 1.00 24.04 O ANISOU 2222 OH TYR D 313 3621 3492 2019 119 -22 -606 O ATOM 2223 N VAL A 314 61.415 72.353 40.774 1.00 17.50 N ANISOU 2223 N VAL D 314 2221 2046 2382 138 97 73 N ATOM 2224 CA VAL A 314 60.549 71.192 40.898 1.00 19.38 C ANISOU 2224 CA VAL D 314 2360 2346 2658 -39 77 -21 C ATOM 2225 C VAL A 314 61.062 70.066 39.978 1.00 19.14 C ANISOU 2225 C VAL D 314 2301 2398 2570 39 -159 -25 C ATOM 2226 O VAL A 314 61.775 70.308 38.982 1.00 19.16 O ANISOU 2226 O VAL D 314 2378 2381 2521 -1 -168 -265 O ATOM 2227 CB VAL A 314 59.067 71.481 40.503 1.00 19.59 C ANISOU 2227 CB VAL D 314 2381 2237 2823 157 -37 -72 C ATOM 2228 CG1 VAL A 314 58.449 72.492 41.403 1.00 23.65 C ANISOU 2228 CG1 VAL D 314 2889 2854 3242 -55 -87 43 C ATOM 2229 CG2 VAL A 314 58.994 71.913 39.044 1.00 19.33 C ANISOU 2229 CG2 VAL D 314 2225 2455 2663 68 -105 57 C ATOM 2230 N VAL A 315 60.651 68.841 40.310 1.00 19.10 N ANISOU 2230 N VAL D 315 2506 2348 2403 -5 -240 -83 N ATOM 2231 CA VAL A 315 60.926 67.663 39.522 1.00 20.21 C ANISOU 2231 CA VAL D 315 2520 2418 2739 -21 -96 -74 C ATOM 2232 C VAL A 315 59.573 67.261 38.917 1.00 20.47 C ANISOU 2232 C VAL D 315 2630 2339 2805 -16 -92 -64 C ATOM 2233 O VAL A 315 58.653 66.881 39.641 1.00 20.64 O ANISOU 2233 O VAL D 315 2543 2467 2829 -134 -264 18 O ATOM 2234 CB VAL A 315 61.530 66.502 40.400 1.00 20.45 C ANISOU 2234 CB VAL D 315 2499 2592 2678 -14 -18 -19 C ATOM 2235 CG1 VAL A 315 61.740 65.260 39.560 1.00 19.98 C ANISOU 2235 CG1 VAL D 315 2410 2629 2550 24 -158 -92 C ATOM 2236 CG2 VAL A 315 62.833 66.947 41.095 1.00 21.48 C ANISOU 2236 CG2 VAL D 315 2508 2885 2769 196 76 -79 C ATOM 2237 N VAL A 316 59.460 67.379 37.602 1.00 19.45 N ANISOU 2237 N VAL D 316 2613 2180 2595 0 -113 151 N ATOM 2238 CA VAL A 316 58.213 67.175 36.879 1.00 21.41 C ANISOU 2238 CA VAL D 316 2603 2473 3058 5 -58 77 C ATOM 2239 C VAL A 316 57.964 65.657 36.708 1.00 23.74 C ANISOU 2239 C VAL D 316 2805 2591 3623 25 16 -56 C ATOM 2240 O VAL A 316 58.901 64.839 36.810 1.00 23.10 O ANISOU 2240 O VAL D 316 2599 2299 3875 115 -36 -204 O ATOM 2241 CB VAL A 316 58.179 67.882 35.480 1.00 21.09 C ANISOU 2241 CB VAL D 316 2658 2382 2972 -35 37 136 C ATOM 2242 CG1 VAL A 316 58.434 69.410 35.561 1.00 18.26 C ANISOU 2242 CG1 VAL D 316 2426 2185 2327 -74 329 -7 C ATOM 2243 CG2 VAL A 316 59.147 67.293 34.495 1.00 22.10 C ANISOU 2243 CG2 VAL D 316 2799 2264 3332 176 104 77 C ATOM 2244 N LYS A 317 56.707 65.304 36.442 1.00 23.96 N ANISOU 2244 N LYS D 317 2758 2807 3536 29 28 -2 N ATOM 2245 CA LYS A 317 56.294 63.894 36.353 1.00 25.33 C ANISOU 2245 CA LYS D 317 3038 2966 3619 -34 25 39 C ATOM 2246 C LYS A 317 56.666 63.337 34.982 1.00 26.84 C ANISOU 2246 C LYS D 317 3288 3217 3692 -48 85 233 C ATOM 2247 O LYS A 317 57.577 62.503 34.930 1.00 29.82 O ANISOU 2247 O LYS D 317 3458 3821 4049 38 186 524 O ATOM 2248 CB LYS A 317 54.821 63.709 36.687 1.00 24.03 C ANISOU 2248 CB LYS D 317 2997 2835 3297 137 46 52 C ATOM 2249 CG LYS A 317 54.374 62.238 36.844 1.00 25.02 C ANISOU 2249 CG LYS D 317 2843 2967 3694 -107 -52 46 C ATOM 2250 CD LYS A 317 52.959 62.136 37.401 1.00 25.21 C ANISOU 2250 CD LYS D 317 3100 3072 3404 -40 8 4 C ATOM 2251 CE LYS A 317 52.323 60.745 37.208 1.00 23.87 C ANISOU 2251 CE LYS D 317 2998 2902 3167 116 -90 55 C ATOM 2252 NZ LYS A 317 52.225 60.326 35.775 1.00 19.13 N ANISOU 2252 NZ LYS D 317 2649 1954 2664 167 177 -181 N ATOM 2253 N ASN A 318 56.031 63.788 33.895 1.00 29.50 N ANISOU 2253 N ASN D 318 3642 3529 4034 0 -26 42 N ATOM 2254 CA ASN A 318 56.437 63.418 32.512 1.00 33.18 C ANISOU 2254 CA ASN D 318 4224 4102 4280 66 -5 82 C ATOM 2255 C ASN A 318 57.374 64.427 31.884 1.00 36.43 C ANISOU 2255 C ASN D 318 4629 4472 4738 2 -70 3 C ATOM 2256 O ASN A 318 56.993 65.573 31.660 1.00 38.31 O ANISOU 2256 O ASN D 318 4761 4790 5004 85 -49 -36 O ATOM 2257 CB ASN A 318 55.249 63.354 31.553 1.00 34.90 C ANISOU 2257 CB ASN D 318 4460 4244 4555 53 -100 113 C ATOM 2258 CG ASN A 318 54.339 62.229 31.845 1.00 37.62 C ANISOU 2258 CG ASN D 318 4681 4337 5273 -39 -34 12 C ATOM 2259 OD1 ASN A 318 54.782 61.086 31.955 1.00 31.14 O ANISOU 2259 OD1 ASN D 318 3782 4007 4043 160 -96 103 O ATOM 2260 ND2 ASN A 318 53.038 62.527 31.957 1.00 41.12 N ANISOU 2260 ND2 ASN D 318 4714 5051 5856 87 -160 116 N ATOM 2261 N SER A 319 58.564 63.992 31.515 1.00 37.87 N ANISOU 2261 N SER D 319 4672 4713 5004 28 -33 -31 N ATOM 2262 CA SER A 319 59.557 64.916 30.993 1.00 40.78 C ANISOU 2262 CA SER D 319 5034 5112 5345 -11 -34 -80 C ATOM 2263 C SER A 319 59.952 64.680 29.531 1.00 43.53 C ANISOU 2263 C SER D 319 5508 5529 5502 -2 -28 -35 C ATOM 2264 O SER A 319 60.655 65.495 28.965 1.00 44.29 O ANISOU 2264 O SER D 319 5687 5560 5580 -11 18 -74 O ATOM 2265 CB SER A 319 60.783 64.870 31.897 1.00 40.83 C ANISOU 2265 CB SER D 319 5093 5135 5285 -59 -18 -44 C ATOM 2266 OG SER A 319 60.989 63.555 32.371 1.00 40.10 O ANISOU 2266 OG SER D 319 4753 5104 5378 81 106 -168 O ATOM 2267 N ILE A 320 59.491 63.584 28.926 1.00 46.77 N ANISOU 2267 N ILE D 320 5915 5928 5927 44 31 30 N ATOM 2268 CA ILE A 320 59.906 63.202 27.554 1.00 48.41 C ANISOU 2268 CA ILE D 320 6166 6159 6068 35 -1 63 C ATOM 2269 C ILE A 320 58.848 63.543 26.489 1.00 50.20 C ANISOU 2269 C ILE D 320 6373 6395 6306 24 77 41 C ATOM 2270 O ILE A 320 58.079 62.683 26.041 1.00 51.72 O ANISOU 2270 O ILE D 320 6628 6518 6504 -62 87 90 O ATOM 2271 CB ILE A 320 60.310 61.689 27.455 1.00 50.08 C ANISOU 2271 CB ILE D 320 6404 6260 6363 65 -11 21 C ATOM 2272 CG1 ILE A 320 59.263 60.780 28.115 1.00 50.82 C ANISOU 2272 CG1 ILE D 320 6423 6340 6545 -84 20 81 C ATOM 2273 CG2 ILE A 320 61.692 61.466 28.112 1.00 51.88 C ANISOU 2273 CG2 ILE D 320 6482 6614 6615 -25 21 39 C ATOM 2274 CD1 ILE A 320 59.360 59.294 27.720 1.00 51.00 C ANISOU 2274 CD1 ILE D 320 6518 6385 6474 28 -13 -4 C TER 2275 ILE D 320 END