*** eg44_high_res ***
Job options:
ID = 2101242337025306
JOBID = eg44_high_res
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
HEADER eg44_high_res
ATOM 1 N ASN A 2 -6.812 -56.537 20.271 1.00 30.44 N
ANISOU 1 N ASN A 2 4309 2417 4838 -4 -927 -623 N
ATOM 2 CA ASN A 2 -7.365 -55.151 20.175 1.00 26.72 C
ANISOU 2 CA ASN A 2 3825 2325 4001 -167 -974 -168 C
ATOM 3 CB ASN A 2 -6.271 -54.084 20.228 1.00 23.94 C
ANISOU 3 CB ASN A 2 3951 1895 3248 -113 -954 361 C
ATOM 4 CG ASN A 2 -5.440 -54.145 21.501 1.00 23.82 C
ANISOU 4 CG ASN A 2 3893 1978 3176 -118 -900 365 C
ATOM 5 OD1 ASN A 2 -5.927 -53.811 22.586 1.00 25.21 O
ANISOU 5 OD1 ASN A 2 3853 2366 3356 11 -519 478 O
ATOM 6 ND2 ASN A 2 -4.180 -54.551 21.388 1.00 23.52 N
ANISOU 6 ND2 ASN A 2 3689 2140 3107 -675 -180 173 N
ATOM 7 C ASN A 2 -8.163 -54.999 18.879 1.00 25.65 C
ANISOU 7 C ASN A 2 3808 1933 4002 -40 -955 -100 C
ATOM 8 O ASN A 2 -7.717 -55.414 17.804 1.00 27.64 O
ANISOU 8 O ASN A 2 3633 2443 4425 134 -1035 -584 O
ATOM 9 N THR A 3 -9.341 -54.389 18.990 1.00 24.82 N
ANISOU 9 N THR A 3 3768 1721 3941 -197 -696 132 N
ATOM 10 CA ATHR A 3 -10.177 -54.102 17.836 0.50 25.70 C
ANISOU 10 CA ATHR A 3 3806 1823 4132 110 -754 163 C
ATOM 11 CA BTHR A 3 -10.175 -54.100 17.838 0.50 26.24 C
ANISOU 11 CA BTHR A 3 3914 1907 4149 109 -959 5 C
ATOM 12 CB ATHR A 3 -11.235 -55.197 17.582 0.50 25.95 C
ANISOU 12 CB ATHR A 3 3770 1570 4518 191 -639 348 C
ATOM 13 CB BTHR A 3 -11.192 -55.236 17.623 0.50 28.22 C
ANISOU 13 CB BTHR A 3 3897 2457 4367 -111 -1438 138 C
ATOM 14 OG1ATHR A 3 -12.428 -54.919 18.318 0.50 28.18 O
ANISOU 14 OG1ATHR A 3 4187 1749 4771 378 -93 838 O
ATOM 15 OG1BTHR A 3 -12.124 -54.866 16.602 0.50 31.65 O
ANISOU 15 OG1BTHR A 3 5134 2622 4267 198 -2026 -62 O
ATOM 16 CG2ATHR A 3 -10.775 -56.600 17.894 0.50 25.32 C
ANISOU 16 CG2ATHR A 3 3738 1444 4438 95 -828 241 C
ATOM 17 CG2BTHR A 3 -11.912 -55.615 18.900 0.50 29.34 C
ANISOU 17 CG2BTHR A 3 4076 2484 4587 -351 -1371 150 C
ATOM 18 C THR A 3 -10.787 -52.713 18.025 1.00 24.95 C
ANISOU 18 C THR A 3 3843 1845 3791 115 -704 166 C
ATOM 19 O THR A 3 -11.162 -52.332 19.138 1.00 24.76 O
ANISOU 19 O THR A 3 3242 2088 4077 56 -738 -13 O
ATOM 20 N PRO A 4 -10.888 -51.884 16.966 1.00 22.97 N
ANISOU 20 N PRO A 4 3004 2021 3701 171 -711 117 N
ATOM 21 CA PRO A 4 -11.486 -50.564 17.136 1.00 22.31 C
ANISOU 21 CA PRO A 4 3083 1893 3499 96 -500 301 C
ATOM 22 CB PRO A 4 -11.430 -49.952 15.732 1.00 24.64 C
ANISOU 22 CB PRO A 4 3644 2104 3611 20 -356 369 C
ATOM 23 CG PRO A 4 -10.278 -50.691 15.079 1.00 27.11 C
ANISOU 23 CG PRO A 4 3904 2733 3662 150 -286 142 C
ATOM 24 CD PRO A 4 -10.391 -52.105 15.604 1.00 25.53 C
ANISOU 24 CD PRO A 4 3235 2606 3858 271 -487 84 C
ATOM 25 C PRO A 4 -12.912 -50.687 17.657 1.00 21.29 C
ANISOU 25 C PRO A 4 3120 1821 3148 -9 -796 349 C
ATOM 26 O PRO A 4 -13.667 -51.559 17.235 1.00 22.17 O
ANISOU 26 O PRO A 4 2972 2063 3386 -115 -699 134 O
ATOM 27 N PRO A 5 -13.314 -49.814 18.600 1.00 20.64 N
ANISOU 27 N PRO A 5 2829 1771 3239 -55 -460 320 N
ATOM 28 CA PRO A 5 -14.663 -49.850 19.150 1.00 21.27 C
ANISOU 28 CA PRO A 5 2902 1888 3289 -204 -365 411 C
ATOM 29 CB PRO A 5 -14.601 -48.861 20.309 1.00 21.94 C
ANISOU 29 CB PRO A 5 3056 1727 3551 -216 -458 394 C
ATOM 30 CG PRO A 5 -13.538 -47.884 19.873 1.00 22.76 C
ANISOU 30 CG PRO A 5 3096 1910 3640 -293 -388 243 C
ATOM 31 CD PRO A 5 -12.495 -48.746 19.196 1.00 22.15 C
ANISOU 31 CD PRO A 5 3170 1883 3363 -324 -410 422 C
ATOM 32 C PRO A 5 -15.712 -49.397 18.132 1.00 20.79 C
ANISOU 32 C PRO A 5 2978 1639 3281 -122 -259 555 C
ATOM 33 O PRO A 5 -15.416 -48.572 17.263 1.00 22.45 O
ANISOU 33 O PRO A 5 3346 2115 3066 -156 -54 613 O
ATOM 34 N GLU A 6 -16.925 -49.940 18.265 1.00 22.44 N
ANISOU 34 N GLU A 6 3226 1907 3391 -438 -377 402 N
ATOM 35 CA GLU A 6 -18.077 -49.459 17.541 1.00 21.30 C
ANISOU 35 CA GLU A 6 3318 1709 3062 -416 -476 612 C
ATOM 36 CB GLU A 6 -19.317 -50.309 17.846 1.00 24.03 C
ANISOU 36 CB GLU A 6 3398 2042 3691 -371 -380 998 C
ATOM 37 CG GLU A 6 -20.591 -49.838 17.134 1.00 29.14 C
ANISOU 37 CG GLU A 6 3884 2871 4317 -224 -848 954 C
ATOM 38 CD GLU A 6 -21.381 -48.690 17.770 1.00 32.07 C
ANISOU 38 CD GLU A 6 4252 3267 4664 -12 -806 1130 C
ATOM 39 OE1 GLU A 6 -21.187 -48.392 18.979 1.00 35.62 O
ANISOU 39 OE1 GLU A 6 4494 4372 4666 -55 -1040 1204 O
ATOM 40 OE2 GLU A 6 -22.203 -48.087 17.052 1.00 34.25 O
ANISOU 40 OE2 GLU A 6 4279 4026 4709 -193 -1119 1343 O
ATOM 41 C GLU A 6 -18.343 -47.992 17.889 1.00 20.33 C
ANISOU 41 C GLU A 6 3122 1891 2710 -183 84 819 C
ATOM 42 O GLU A 6 -18.303 -47.610 19.060 1.00 22.72 O
ANISOU 42 O GLU A 6 3248 2429 2954 -207 -205 672 O
ATOM 43 N LEU A 7 -18.598 -47.187 16.848 1.00 17.43 N
ANISOU 43 N LEU A 7 2238 2123 2261 84 -130 521 N
ATOM 44 CA LEU A 7 -18.994 -45.798 16.977 1.00 17.47 C
ANISOU 44 CA LEU A 7 2302 2018 2316 -72 51 469 C
ATOM 45 CB LEU A 7 -17.927 -44.901 16.349 1.00 16.90 C
ANISOU 45 CB LEU A 7 2388 1856 2176 -76 -131 581 C
ATOM 46 CG LEU A 7 -16.533 -45.018 16.951 1.00 16.21 C
ANISOU 46 CG LEU A 7 2330 1489 2339 -38 -217 387 C
ATOM 47 CD1 LEU A 7 -15.540 -44.191 16.146 1.00 17.85 C
ANISOU 47 CD1 LEU A 7 2449 1822 2509 -189 -283 539 C
ATOM 48 CD2 LEU A 7 -16.556 -44.610 18.425 1.00 18.94 C
ANISOU 48 CD2 LEU A 7 2599 2087 2510 -109 -531 401 C
ATOM 49 C LEU A 7 -20.339 -45.581 16.272 1.00 17.96 C
ANISOU 49 C LEU A 7 2468 2124 2229 -181 -125 521 C
ATOM 50 O LEU A 7 -20.557 -46.045 15.149 1.00 20.20 O
ANISOU 50 O LEU A 7 2796 2428 2450 -180 -185 431 O
ATOM 51 N ASP A 8 -21.227 -44.839 16.939 1.00 19.39 N
ANISOU 51 N ASP A 8 2789 2156 2420 -182 64 538 N
ATOM 52 CA ASP A 8 -22.515 -44.484 16.390 1.00 19.20 C
ANISOU 52 CA ASP A 8 2689 2120 2484 -206 75 403 C
ATOM 53 CB ASP A 8 -23.458 -43.960 17.460 1.00 22.11 C
ANISOU 53 CB ASP A 8 2744 2861 2793 -45 365 660 C
ATOM 54 CG ASP A 8 -23.906 -45.000 18.468 1.00 25.90 C
ANISOU 54 CG ASP A 8 3510 3028 3301 -129 706 908 C
ATOM 55 OD1 ASP A 8 -23.728 -46.209 18.227 1.00 29.26 O
ANISOU 55 OD1 ASP A 8 3817 3084 4214 -228 841 1299 O
ATOM 56 OD2 ASP A 8 -24.461 -44.592 19.474 1.00 33.58 O
ANISOU 56 OD2 ASP A 8 5192 4776 2791 -207 811 976 O
ATOM 57 C ASP A 8 -22.340 -43.427 15.303 1.00 18.11 C
ANISOU 57 C ASP A 8 2511 2084 2284 -122 148 239 C
ATOM 58 O ASP A 8 -21.382 -42.661 15.325 1.00 18.83 O
ANISOU 58 O ASP A 8 2877 1968 2310 -329 -198 520 O
ATOM 59 N THR A 9 -23.337 -43.347 14.410 1.00 17.89 N
ANISOU 59 N THR A 9 2355 2060 2381 -252 89 373 N
ATOM 60 CA THR A 9 -23.296 -42.438 13.266 1.00 17.30 C
ANISOU 60 CA THR A 9 2426 1800 2347 -89 110 278 C
ATOM 61 CB THR A 9 -23.311 -43.208 11.945 1.00 17.94 C
ANISOU 61 CB THR A 9 2345 2034 2437 7 49 120 C
ATOM 62 OG1 THR A 9 -24.408 -44.128 11.933 1.00 18.75 O
ANISOU 62 OG1 THR A 9 2465 1903 2753 -57 -118 56 O
ATOM 63 CG2 THR A 9 -22.004 -43.938 11.731 1.00 17.75 C
ANISOU 63 CG2 THR A 9 2231 2306 2207 -67 352 -134 C
ATOM 64 C THR A 9 -24.421 -41.411 13.313 1.00 16.86 C
ANISOU 64 C THR A 9 2376 1792 2238 -59 234 200 C
ATOM 65 O THR A 9 -25.510 -41.680 13.849 1.00 18.99 O
ANISOU 65 O THR A 9 2354 2086 2773 68 175 388 O
ATOM 66 N VAL A 10 -24.125 -40.238 12.734 1.00 15.47 N
ANISOU 66 N VAL A 10 2065 1827 1983 83 83 219 N
ATOM 67 CA VAL A 10 -25.097 -39.157 12.526 1.00 15.83 C
ANISOU 67 CA VAL A 10 2247 1719 2049 60 -115 169 C
ATOM 68 CB VAL A 10 -24.887 -37.996 13.520 1.00 16.34 C
ANISOU 68 CB VAL A 10 2254 1671 2280 132 121 88 C
ATOM 69 CG1 VAL A 10 -24.990 -38.477 14.957 1.00 17.51 C
ANISOU 69 CG1 VAL A 10 2384 2041 2228 67 216 -101 C
ATOM 70 CG2 VAL A 10 -23.563 -37.289 13.280 1.00 16.66 C
ANISOU 70 CG2 VAL A 10 2248 1704 2376 152 -46 3 C
ATOM 71 C VAL A 10 -24.957 -38.667 11.079 1.00 16.74 C
ANISOU 71 C VAL A 10 2539 1782 2038 178 -12 172 C
ATOM 72 O VAL A 10 -23.959 -38.943 10.424 1.00 17.21 O
ANISOU 72 O VAL A 10 2373 2243 1923 410 -410 220 O
ATOM 73 N LEU A 11 -25.953 -37.909 10.610 1.00 17.79 N
ANISOU 73 N LEU A 11 2353 2210 2194 366 66 -21 N
ATOM 74 CA LEU A 11 -25.852 -37.241 9.300 1.00 20.14 C
ANISOU 74 CA LEU A 11 2976 2496 2180 668 -94 89 C
ATOM 75 CB LEU A 11 -27.089 -37.513 8.449 1.00 23.05 C
ANISOU 75 CB LEU A 11 2666 3032 3057 319 80 -48 C
ATOM 76 CG LEU A 11 -27.371 -38.945 8.069 1.00 23.58 C
ANISOU 76 CG LEU A 11 2844 2924 3190 19 -143 164 C
ATOM 77 CD1 LEU A 11 -28.495 -38.947 7.029 1.00 23.85 C
ANISOU 77 CD1 LEU A 11 3399 3207 2455 97 -150 -337 C
ATOM 78 CD2 LEU A 11 -26.113 -39.604 7.526 1.00 23.70 C
ANISOU 78 CD2 LEU A 11 2916 2617 3472 -276 109 295 C
ATOM 79 C LEU A 11 -25.733 -35.738 9.498 1.00 19.62 C
ANISOU 79 C LEU A 11 3074 2456 1923 860 -191 216 C
ATOM 80 O LEU A 11 -26.703 -35.103 9.875 1.00 21.78 O
ANISOU 80 O LEU A 11 3189 2864 2222 1128 -146 88 O
ATOM 81 N GLN A 12 -24.543 -35.195 9.263 1.00 17.79 N
ANISOU 81 N GLN A 12 2939 1962 1858 990 -365 50 N
ATOM 82 CA GLN A 12 -24.353 -33.752 9.299 1.00 18.16 C
ANISOU 82 CA GLN A 12 3301 1861 1737 1048 -334 193 C
ATOM 83 CB GLN A 12 -22.869 -33.418 9.150 1.00 20.95 C
ANISOU 83 CB GLN A 12 3346 2097 2514 776 -660 15 C
ATOM 84 CG GLN A 12 -22.553 -31.925 9.195 1.00 24.96 C
ANISOU 84 CG GLN A 12 4083 2083 3315 1065 -679 -28 C
ATOM 85 CD GLN A 12 -22.783 -31.357 10.571 1.00 28.26 C
ANISOU 85 CD GLN A 12 4458 2686 3593 631 -565 -476 C
ATOM 86 OE1 GLN A 12 -22.287 -31.882 11.555 1.00 33.27 O
ANISOU 86 OE1 GLN A 12 4075 4451 4114 -128 -1448 -170 O
ATOM 87 NE2 GLN A 12 -23.554 -30.276 10.644 1.00 34.41 N
ANISOU 87 NE2 GLN A 12 5249 2805 5020 867 19 -857 N
ATOM 88 C GLN A 12 -25.171 -33.140 8.159 1.00 18.35 C
ANISOU 88 C GLN A 12 3212 2159 1600 1028 -239 178 C
ATOM 89 O GLN A 12 -25.109 -33.604 7.035 1.00 19.45 O
ANISOU 89 O GLN A 12 3421 2337 1630 1056 -205 -3 O
ATOM 90 N ALA A 13 -25.972 -32.126 8.491 1.00 17.84 N
ANISOU 90 N ALA A 13 3099 1861 1816 889 -22 453 N
ATOM 91 CA ALA A 13 -26.870 -31.488 7.555 1.00 17.74 C
ANISOU 91 CA ALA A 13 2674 2107 1959 564 50 663 C
ATOM 92 CB ALA A 13 -28.270 -32.020 7.742 1.00 21.18 C
ANISOU 92 CB ALA A 13 2985 2328 2733 230 247 690 C
ATOM 93 C ALA A 13 -26.820 -29.986 7.785 1.00 17.13 C
ANISOU 93 C ALA A 13 2366 2130 2013 500 100 515 C
ATOM 94 O ALA A 13 -26.586 -29.529 8.890 1.00 18.59 O
ANISOU 94 O ALA A 13 2947 1926 2189 363 -216 341 O
ATOM 95 N PRO A 14 -27.045 -29.175 6.740 1.00 16.50 N
ANISOU 95 N PRO A 14 2554 1736 1978 490 -92 359 N
ATOM 96 CA PRO A 14 -26.991 -27.724 6.907 1.00 17.13 C
ANISOU 96 CA PRO A 14 2616 1732 2159 182 -130 437 C
ATOM 97 CB PRO A 14 -27.174 -27.169 5.493 1.00 20.68 C
ANISOU 97 CB PRO A 14 3355 2184 2318 169 -174 645 C
ATOM 98 CG PRO A 14 -27.730 -28.295 4.676 1.00 21.20 C
ANISOU 98 CG PRO A 14 3297 2313 2442 -133 -486 784 C
ATOM 99 CD PRO A 14 -27.394 -29.594 5.372 1.00 18.05 C
ANISOU 99 CD PRO A 14 2738 2071 2047 266 -139 323 C
ATOM 100 C PRO A 14 -28.122 -27.239 7.820 1.00 16.68 C
ANISOU 100 C PRO A 14 2712 1516 2109 296 -305 215 C
ATOM 101 O PRO A 14 -29.208 -27.814 7.835 1.00 15.78 O
ANISOU 101 O PRO A 14 2349 1689 1955 409 -63 -63 O
ATOM 102 N TYR A 15 -27.838 -26.176 8.568 1.00 15.75 N
ANISOU 102 N TYR A 15 2381 1761 1841 245 -293 108 N
ATOM 103 CA TYR A 15 -28.810 -25.591 9.487 1.00 17.31 C
ANISOU 103 CA TYR A 15 2335 1968 2274 308 -247 -120 C
ATOM 104 CB TYR A 15 -28.129 -24.500 10.308 1.00 17.44 C
ANISOU 104 CB TYR A 15 1851 2396 2380 102 -371 -70 C
ATOM 105 CG TYR A 15 -28.898 -23.984 11.491 1.00 18.19 C
ANISOU 105 CG TYR A 15 2052 2499 2359 324 -422 -192 C
ATOM 106 CD1 TYR A 15 -29.079 -24.764 12.624 1.00 19.65 C
ANISOU 106 CD1 TYR A 15 2289 2953 2223 408 -229 -89 C
ATOM 107 CE1 TYR A 15 -29.752 -24.280 13.739 1.00 21.35 C
ANISOU 107 CE1 TYR A 15 2498 3173 2441 442 -188 -310 C
ATOM 108 CZ TYR A 15 -30.239 -22.990 13.738 1.00 22.25 C
ANISOU 108 CZ TYR A 15 2658 3368 2425 676 -116 -539 C
ATOM 109 OH TYR A 15 -30.906 -22.491 14.828 1.00 25.35 O
ANISOU 109 OH TYR A 15 2855 3898 2876 1151 -176 -1129 O
ATOM 110 CE2 TYR A 15 -30.062 -22.199 12.616 1.00 20.82 C
ANISOU 110 CE2 TYR A 15 2690 2627 2594 675 -488 -407 C
ATOM 111 CD2 TYR A 15 -29.386 -22.691 11.514 1.00 20.33 C
ANISOU 111 CD2 TYR A 15 2596 2599 2529 492 -443 -157 C
ATOM 112 C TYR A 15 -30.022 -25.058 8.718 1.00 16.89 C
ANISOU 112 C TYR A 15 2145 1748 2522 144 -358 -300 C
ATOM 113 O TYR A 15 -31.096 -24.908 9.299 1.00 19.09 O
ANISOU 113 O TYR A 15 2048 2306 2900 267 -508 -503 O
ATOM 114 N ALA A 16 -29.860 -24.803 7.411 1.00 17.04 N
ANISOU 114 N ALA A 16 2385 1480 2608 286 -561 -76 N
ATOM 115 CA ALA A 16 -30.981 -24.441 6.525 1.00 19.79 C
ANISOU 115 CA ALA A 16 2771 1724 3025 315 -758 -108 C
ATOM 116 CB ALA A 16 -30.472 -24.311 5.109 1.00 22.21 C
ANISOU 116 CB ALA A 16 3405 1834 3200 169 -789 607 C
ATOM 117 C ALA A 16 -32.119 -25.468 6.616 1.00 20.01 C
ANISOU 117 C ALA A 16 2563 1922 3117 401 -823 -56 C
ATOM 118 O ALA A 16 -33.257 -25.112 6.408 1.00 22.38 O
ANISOU 118 O ALA A 16 2438 2033 4029 225 -889 -364 O
ATOM 119 N TYR A 17 -31.791 -26.740 6.891 1.00 16.21 N
ANISOU 119 N TYR A 17 2256 1660 2241 107 -656 -90 N
ATOM 120 CA TYR A 17 -32.795 -27.781 6.973 1.00 16.47 C
ANISOU 120 CA TYR A 17 2270 1777 2211 3 -487 -320 C
ATOM 121 CB TYR A 17 -32.233 -29.145 6.562 1.00 16.59 C
ANISOU 121 CB TYR A 17 2746 1460 2095 -39 -463 56 C
ATOM 122 CG TYR A 17 -31.968 -29.341 5.086 1.00 16.64 C
ANISOU 122 CG TYR A 17 2599 1783 1939 -24 -587 245 C
ATOM 123 CD1 TYR A 17 -32.712 -28.718 4.100 1.00 16.68 C
ANISOU 123 CD1 TYR A 17 2439 1807 2091 83 -579 279 C
ATOM 124 CE1 TYR A 17 -32.498 -28.971 2.751 1.00 17.22 C
ANISOU 124 CE1 TYR A 17 2642 1760 2139 127 -519 256 C
ATOM 125 CZ TYR A 17 -31.482 -29.815 2.356 1.00 16.42 C
ANISOU 125 CZ TYR A 17 2711 1863 1664 132 -423 217 C
ATOM 126 OH TYR A 17 -31.221 -30.085 1.033 1.00 19.14 O
ANISOU 126 OH TYR A 17 3441 2119 1710 -14 -592 135 O
ATOM 127 CE2 TYR A 17 -30.734 -30.450 3.326 1.00 17.52 C
ANISOU 127 CE2 TYR A 17 2745 2107 1802 412 -471 181 C
ATOM 128 CD2 TYR A 17 -30.983 -30.199 4.668 1.00 17.65 C
ANISOU 128 CD2 TYR A 17 2842 2157 1706 394 -760 285 C
ATOM 129 C TYR A 17 -33.414 -27.867 8.370 1.00 18.11 C
ANISOU 129 C TYR A 17 2474 2114 2290 -28 -459 -158 C
ATOM 130 O TYR A 17 -34.350 -28.668 8.569 1.00 19.67 O
ANISOU 130 O TYR A 17 2504 2323 2646 -101 -41 -271 O
ATOM 131 N ASN A 18 -32.935 -27.052 9.320 1.00 17.33 N
ANISOU 131 N ASN A 18 2033 2293 2255 214 -326 -381 N
ATOM 132 CA ASN A 18 -33.676 -26.804 10.568 1.00 17.80 C
ANISOU 132 CA ASN A 18 2265 2180 2316 121 -146 -159 C
ATOM 133 CB ASN A 18 -32.764 -26.346 11.714 1.00 17.79 C
ANISOU 133 CB ASN A 18 2511 1949 2298 277 -316 -42 C
ATOM 134 CG ASN A 18 -33.517 -26.029 12.983 1.00 18.39 C
ANISOU 134 CG ASN A 18 2873 1870 2242 257 -311 -128 C
ATOM 135 OD1 ASN A 18 -34.497 -26.702 13.322 1.00 21.41 O
ANISOU 135 OD1 ASN A 18 3204 2711 2218 50 -74 -81 O
ATOM 136 ND2 ASN A 18 -33.090 -24.979 13.677 1.00 18.53 N
ANISOU 136 ND2 ASN A 18 2964 1881 2195 345 -49 -369 N
ATOM 137 C ASN A 18 -34.762 -25.774 10.256 1.00 17.50 C
ANISOU 137 C ASN A 18 2385 2077 2187 83 -151 -89 C
ATOM 138 O ASN A 18 -34.646 -24.609 10.596 1.00 17.86 O
ANISOU 138 O ASN A 18 2291 2079 2415 4 -208 -179 O
ATOM 139 N TRP A 19 -35.791 -26.214 9.537 1.00 16.49 N
ANISOU 139 N TRP A 19 2298 1949 2018 -17 55 -191 N
ATOM 140 CA TRP A 19 -36.765 -25.308 8.971 1.00 15.39 C
ANISOU 140 CA TRP A 19 2114 1790 1942 -152 69 -143 C
ATOM 141 CB TRP A 19 -37.921 -26.060 8.312 1.00 15.75 C
ANISOU 141 CB TRP A 19 2148 1911 1926 -236 115 -52 C
ATOM 142 CG TRP A 19 -37.505 -27.019 7.256 1.00 15.58 C
ANISOU 142 CG TRP A 19 2365 1595 1958 -264 66 -44 C
ATOM 143 CD1 TRP A 19 -37.376 -28.369 7.385 1.00 15.76 C
ANISOU 143 CD1 TRP A 19 2482 1554 1952 -181 -10 -121 C
ATOM 144 NE1 TRP A 19 -37.023 -28.912 6.188 1.00 16.09 N
ANISOU 144 NE1 TRP A 19 2635 1474 2003 -73 -34 -143 N
ATOM 145 CE2 TRP A 19 -36.902 -27.923 5.252 1.00 15.34 C
ANISOU 145 CE2 TRP A 19 2178 1795 1852 -135 -191 -86 C
ATOM 146 CD2 TRP A 19 -37.195 -26.701 5.888 1.00 15.40 C
ANISOU 146 CD2 TRP A 19 2201 1711 1939 -193 58 -67 C
ATOM 147 CE3 TRP A 19 -37.165 -25.521 5.144 1.00 14.76 C
ANISOU 147 CE3 TRP A 19 1998 1705 1906 -200 -94 -185 C
ATOM 148 CZ3 TRP A 19 -36.829 -25.586 3.815 1.00 15.50 C
ANISOU 148 CZ3 TRP A 19 2005 1853 2031 -278 103 -91 C
ATOM 149 CH2 TRP A 19 -36.499 -26.801 3.216 1.00 15.68 C
ANISOU 149 CH2 TRP A 19 2125 1812 2021 -212 31 -145 C
ATOM 150 CZ2 TRP A 19 -36.531 -27.989 3.915 1.00 15.60 C
ANISOU 150 CZ2 TRP A 19 2052 1846 2029 -327 59 -193 C
ATOM 151 C TRP A 19 -37.341 -24.437 10.068 1.00 15.24 C
ANISOU 151 C TRP A 19 2168 1889 1732 -241 58 -116 C
ATOM 152 O TRP A 19 -37.785 -24.965 11.092 1.00 15.38 O
ANISOU 152 O TRP A 19 2187 1803 1853 -198 48 114 O
ATOM 153 N PRO A 20 -37.407 -23.103 9.894 1.00 13.55 N
ANISOU 153 N PRO A 20 1956 1761 1430 -226 50 227 N
ATOM 154 CA PRO A 20 -38.077 -22.275 10.890 1.00 13.78 C
ANISOU 154 CA PRO A 20 2060 1752 1423 -199 -1 139 C
ATOM 155 CB PRO A 20 -37.662 -20.836 10.539 1.00 14.14 C
ANISOU 155 CB PRO A 20 2058 1803 1511 -328 -52 39 C
ATOM 156 CG PRO A 20 -36.486 -20.998 9.637 1.00 15.49 C
ANISOU 156 CG PRO A 20 2226 2000 1658 -167 59 73 C
ATOM 157 CD PRO A 20 -36.774 -22.275 8.861 1.00 13.98 C
ANISOU 157 CD PRO A 20 1770 2132 1407 -409 89 76 C
ATOM 158 C PRO A 20 -39.592 -22.472 10.806 1.00 13.94 C
ANISOU 158 C PRO A 20 2067 1631 1595 -72 -30 17 C
ATOM 159 O PRO A 20 -40.158 -22.319 9.725 1.00 14.52 O
ANISOU 159 O PRO A 20 1862 1861 1793 -252 -177 122 O
ATOM 160 N THR A 21 -40.197 -22.825 11.940 1.00 14.90 N
ANISOU 160 N THR A 21 2118 1851 1691 -207 79 -21 N
ATOM 161 CA THR A 21 -41.625 -23.069 12.058 1.00 16.58 C
ANISOU 161 CA THR A 21 2249 2001 2047 -373 233 40 C
ATOM 162 CB THR A 21 -41.955 -24.566 12.046 1.00 18.64 C
ANISOU 162 CB THR A 21 2635 2055 2392 -517 95 -68 C
ATOM 163 OG1 THR A 21 -41.570 -25.160 13.300 1.00 20.93 O
ANISOU 163 OG1 THR A 21 2935 2489 2526 -447 125 275 O
ATOM 164 CG2 THR A 21 -41.300 -25.295 10.897 1.00 20.33 C
ANISOU 164 CG2 THR A 21 3153 2145 2425 -592 58 -118 C
ATOM 165 C THR A 21 -42.136 -22.513 13.388 1.00 15.49 C
ANISOU 165 C THR A 21 2115 1790 1979 -177 215 211 C
ATOM 166 O THR A 21 -41.364 -22.051 14.221 1.00 16.68 O
ANISOU 166 O THR A 21 2220 2064 2051 -437 300 71 O
ATOM 167 N SER A 22 -43.441 -22.624 13.606 1.00 17.02 N
ANISOU 167 N SER A 22 2227 2136 2103 -445 461 139 N
ATOM 168 CA SER A 22 -44.006 -22.164 14.853 1.00 19.05 C
ANISOU 168 CA SER A 22 2162 2773 2302 -185 532 -2 C
ATOM 169 CB SER A 22 -45.511 -22.158 14.808 1.00 21.74 C
ANISOU 169 CB SER A 22 2189 3360 2711 -374 550 29 C
ATOM 170 OG SER A 22 -45.999 -23.474 14.679 1.00 26.19 O
ANISOU 170 OG SER A 22 2884 3443 3624 -620 708 -302 O
ATOM 171 C SER A 22 -43.502 -22.992 16.043 1.00 20.11 C
ANISOU 171 C SER A 22 2507 2942 2190 -97 738 81 C
ATOM 172 O SER A 22 -43.703 -22.579 17.172 1.00 24.47 O
ANISOU 172 O SER A 22 3545 3510 2241 15 526 -157 O
ATOM 173 N LYS A 23 -42.899 -24.167 15.785 1.00 19.78 N
ANISOU 173 N LYS A 23 2795 2686 2031 -180 396 229 N
ATOM 174 CA LYS A 23 -42.425 -25.036 16.847 1.00 21.61 C
ANISOU 174 CA LYS A 23 3027 3299 1882 -133 212 193 C
ATOM 175 CB LYS A 23 -42.391 -26.491 16.388 1.00 24.42 C
ANISOU 175 CB LYS A 23 3662 3314 2301 -302 -233 106 C
ATOM 176 CG LYS A 23 -43.765 -27.102 16.165 1.00 30.91 C
ANISOU 176 CG LYS A 23 4033 4031 3679 -611 -264 76 C
ATOM 177 CD LYS A 23 -43.695 -28.562 15.796 1.00 38.33 C
ANISOU 177 CD LYS A 23 5391 4059 5113 -702 -383 11 C
ATOM 178 CE LYS A 23 -45.060 -29.175 15.601 1.00 45.35 C
ANISOU 178 CE LYS A 23 5855 5058 6318 -1145 -819 -384 C
ATOM 179 NZ LYS A 23 -44.981 -30.654 15.575 1.00 52.45 N
ANISOU 179 NZ LYS A 23 6942 5303 7681 -765 -959 -587 N
ATOM 180 C LYS A 23 -41.045 -24.607 17.355 1.00 20.18 C
ANISOU 180 C LYS A 23 2946 3120 1600 -407 341 222 C
ATOM 181 O LYS A 23 -40.671 -24.979 18.470 1.00 25.19 O
ANISOU 181 O LYS A 23 3558 3902 2110 -527 -64 572 O
ATOM 182 N ASN A 24 -40.265 -23.903 16.522 1.00 17.32 N
ANISOU 182 N ASN A 24 2564 2227 1789 -121 202 58 N
ATOM 183 CA ASN A 24 -38.879 -23.588 16.886 1.00 16.13 C
ANISOU 183 CA ASN A 24 2587 2157 1385 -69 90 268 C
ATOM 184 CB ASN A 24 -37.896 -24.494 16.149 1.00 16.83 C
ANISOU 184 CB ASN A 24 2854 1987 1553 -101 248 233 C
ATOM 185 CG ASN A 24 -37.844 -24.232 14.659 1.00 16.90 C
ANISOU 185 CG ASN A 24 2845 2137 1439 192 327 -37 C
ATOM 186 OD1 ASN A 24 -38.553 -23.384 14.159 1.00 19.55 O
ANISOU 186 OD1 ASN A 24 3052 2511 1864 278 75 211 O
ATOM 187 ND2 ASN A 24 -37.004 -24.945 13.939 1.00 19.79 N
ANISOU 187 ND2 ASN A 24 3123 2692 1703 630 458 4 N
ATOM 188 C ASN A 24 -38.518 -22.113 16.683 1.00 17.84 C
ANISOU 188 C ASN A 24 2509 2138 2130 -117 78 -47 C
ATOM 189 O ASN A 24 -37.349 -21.797 16.758 1.00 23.20 O
ANISOU 189 O ASN A 24 2584 2239 3989 -95 -176 341 O
ATOM 190 N VAL A 25 -39.496 -21.235 16.440 1.00 16.47 N
ANISOU 190 N VAL A 25 2440 1914 1904 -144 117 -228 N
ATOM 191 CA VAL A 25 -39.251 -19.809 16.304 1.00 16.63 C
ANISOU 191 CA VAL A 25 2471 1960 1886 -171 12 -355 C
ATOM 192 CB VAL A 25 -39.759 -19.280 14.953 1.00 15.47 C
ANISOU 192 CB VAL A 25 2112 1873 1893 -85 197 -287 C
ATOM 193 CG1 VAL A 25 -39.765 -17.758 14.924 1.00 16.57 C
ANISOU 193 CG1 VAL A 25 2288 1962 2044 -44 49 -1 C
ATOM 194 CG2 VAL A 25 -38.931 -19.866 13.820 1.00 15.81 C
ANISOU 194 CG2 VAL A 25 2317 1869 1819 -43 140 -390 C
ATOM 195 C VAL A 25 -39.957 -19.080 17.442 1.00 17.84 C
ANISOU 195 C VAL A 25 2688 1806 2282 18 93 -420 C
ATOM 196 O VAL A 25 -41.151 -19.308 17.695 1.00 20.68 O
ANISOU 196 O VAL A 25 2983 2341 2533 -370 362 -435 O
ATOM 197 N LYS A 26 -39.215 -18.165 18.066 1.00 18.42 N
ANISOU 197 N LYS A 26 2690 2202 2104 124 -232 -522 N
ATOM 198 CA LYS A 26 -39.800 -17.131 18.921 1.00 18.19 C
ANISOU 198 CA LYS A 26 2950 1910 2051 -59 184 -259 C
ATOM 199 CB LYS A 26 -39.368 -17.306 20.375 1.00 21.14 C
ANISOU 199 CB LYS A 26 3550 2367 2112 72 -36 -336 C
ATOM 200 CG LYS A 26 -39.859 -18.599 21.028 1.00 23.55 C
ANISOU 200 CG LYS A 26 3945 2538 2465 93 -68 79 C
ATOM 201 CD LYS A 26 -39.278 -18.817 22.399 1.00 26.52 C
ANISOU 201 CD LYS A 26 4443 3136 2497 -200 -73 332 C
ATOM 202 CE LYS A 26 -39.331 -20.267 22.809 1.00 31.07 C
ANISOU 202 CE LYS A 26 5205 3161 3439 -6 -147 563 C
ATOM 203 NZ LYS A 26 -40.567 -20.523 23.571 1.00 39.43 N
ANISOU 203 NZ LYS A 26 5507 4601 4870 311 439 391 N
ATOM 204 C LYS A 26 -39.401 -15.761 18.371 1.00 16.66 C
ANISOU 204 C LYS A 26 2563 1987 1778 8 -135 -202 C
ATOM 205 O LYS A 26 -38.369 -15.618 17.696 1.00 18.30 O
ANISOU 205 O LYS A 26 2787 2257 1907 -88 140 -455 O
ATOM 206 N ILE A 27 -40.234 -14.764 18.658 1.00 15.71 N
ANISOU 206 N ILE A 27 2232 2030 1705 -78 50 -264 N
ATOM 207 CA ILE A 27 -39.994 -13.411 18.191 1.00 15.50 C
ANISOU 207 CA ILE A 27 2170 1958 1759 -99 -81 -246 C
ATOM 208 CB ILE A 27 -41.234 -12.832 17.503 1.00 15.95 C
ANISOU 208 CB ILE A 27 2127 1823 2110 -145 -60 -144 C
ATOM 209 CG1 ILE A 27 -41.659 -13.710 16.326 1.00 16.83 C
ANISOU 209 CG1 ILE A 27 2163 2199 2032 -26 -177 -223 C
ATOM 210 CG2 ILE A 27 -40.976 -11.387 17.083 1.00 17.52 C
ANISOU 210 CG2 ILE A 27 2502 1876 2279 -157 23 -25 C
ATOM 211 CD1 ILE A 27 -40.573 -13.987 15.327 1.00 17.92 C
ANISOU 211 CD1 ILE A 27 2345 2223 2238 -169 -89 -207 C
ATOM 212 C ILE A 27 -39.560 -12.552 19.373 1.00 14.96 C
ANISOU 212 C ILE A 27 2219 1535 1930 -107 -35 -261 C
ATOM 213 O ILE A 27 -40.214 -12.545 20.439 1.00 17.35 O
ANISOU 213 O ILE A 27 2512 2241 1838 -247 63 -667 O
ATOM 214 N ALA A 28 -38.460 -11.823 19.176 1.00 15.58 N
ANISOU 214 N ALA A 28 2347 1776 1793 -241 -31 -273 N
ATOM 215 CA ALA A 28 -37.929 -10.983 20.219 1.00 15.59 C
ANISOU 215 CA ALA A 28 2504 1536 1882 -154 -293 -178 C
ATOM 216 CB ALA A 28 -36.411 -11.031 20.190 1.00 16.78 C
ANISOU 216 CB ALA A 28 2458 1751 2165 -208 -430 -203 C
ATOM 217 C ALA A 28 -38.419 -9.543 20.065 1.00 17.16 C
ANISOU 217 C ALA A 28 2738 1751 2030 135 -173 -129 C
ATOM 218 O ALA A 28 -38.428 -8.973 18.964 1.00 17.94 O
ANISOU 218 O ALA A 28 2799 1861 2153 -338 -489 53 O
ATOM 219 N SER A 29 -38.762 -8.948 21.210 1.00 17.45 N
ANISOU 219 N SER A 29 2831 1691 2106 -61 -20 -168 N
ATOM 220 CA SER A 29 -38.649 -7.507 21.376 1.00 16.27 C
ANISOU 220 CA SER A 29 2295 1629 2256 -141 -224 -208 C
ATOM 221 CB SER A 29 -39.843 -6.915 22.128 1.00 17.28 C
ANISOU 221 CB SER A 29 2284 1783 2496 -374 -27 -185 C
ATOM 222 OG SER A 29 -39.745 -5.504 22.247 1.00 16.04 O
ANISOU 222 OG SER A 29 2205 1739 2150 -243 212 -265 O
ATOM 223 C SER A 29 -37.299 -7.284 22.062 1.00 18.46 C
ANISOU 223 C SER A 29 2359 2006 2647 -270 -190 2 C
ATOM 224 O SER A 29 -36.433 -8.137 21.989 1.00 20.49 O
ANISOU 224 O SER A 29 2487 1972 3325 -211 -344 -49 O
ATOM 225 N ARG A 30 -37.100 -6.159 22.723 1.00 17.74 N
ANISOU 225 N ARG A 30 2325 1893 2520 -132 -189 -84 N
ATOM 226 CA ARG A 30 -35.744 -5.841 23.176 1.00 17.21 C
ANISOU 226 CA ARG A 30 2355 1820 2363 -204 -65 -220 C
ATOM 227 CB ARG A 30 -34.913 -5.262 22.024 1.00 19.47 C
ANISOU 227 CB ARG A 30 2688 2381 2328 -26 232 -167 C
ATOM 228 CG ARG A 30 -33.431 -5.169 22.332 1.00 20.17 C
ANISOU 228 CG ARG A 30 2818 2134 2710 91 -46 190 C
ATOM 229 CD ARG A 30 -32.618 -4.653 21.159 1.00 23.39 C
ANISOU 229 CD ARG A 30 3472 2359 3056 -245 25 593 C
ATOM 230 NE ARG A 30 -32.537 -5.698 20.164 1.00 30.70 N
ANISOU 230 NE ARG A 30 3958 4072 3631 262 -235 -163 N
ATOM 231 CZ ARG A 30 -31.516 -6.542 20.002 1.00 26.07 C
ANISOU 231 CZ ARG A 30 3665 3412 2827 83 221 670 C
ATOM 232 NH1 ARG A 30 -30.394 -6.417 20.695 1.00 30.98 N
ANISOU 232 NH1 ARG A 30 4631 3412 3727 -325 -986 184 N
ATOM 233 NH2 ARG A 30 -31.624 -7.491 19.104 1.00 34.37 N
ANISOU 233 NH2 ARG A 30 4702 4383 3973 -570 -308 -272 N
ATOM 234 C ARG A 30 -35.792 -4.805 24.289 1.00 17.49 C
ANISOU 234 C ARG A 30 2501 1921 2224 -142 -205 -229 C
ATOM 235 O ARG A 30 -36.604 -3.897 24.287 1.00 19.22 O
ANISOU 235 O ARG A 30 2997 1879 2424 58 -272 -115 O
ATOM 236 N ILE A 31 -34.907 -5.015 25.257 1.00 16.06 N
ANISOU 236 N ILE A 31 2353 1560 2187 -476 -203 -146 N
ATOM 237 CA ILE A 31 -34.492 -3.970 26.180 1.00 16.44 C
ANISOU 237 CA ILE A 31 2384 1760 2101 -398 -23 -368 C
ATOM 238 CB ILE A 31 -34.896 -4.301 27.635 1.00 19.32 C
ANISOU 238 CB ILE A 31 2424 2585 2332 -91 114 30 C
ATOM 239 CG1 ILE A 31 -34.274 -5.619 28.105 1.00 18.98 C
ANISOU 239 CG1 ILE A 31 2700 2245 2267 -269 107 -230 C
ATOM 240 CG2 ILE A 31 -36.415 -4.297 27.777 1.00 20.85 C
ANISOU 240 CG2 ILE A 31 2461 2903 2556 16 25 158 C
ATOM 241 CD1 ILE A 31 -34.514 -5.934 29.569 1.00 22.15 C
ANISOU 241 CD1 ILE A 31 3419 2696 2299 -170 149 -211 C
ATOM 242 C ILE A 31 -32.980 -3.827 26.016 1.00 17.34 C
ANISOU 242 C ILE A 31 2400 1853 2333 -327 17 -282 C
ATOM 243 O ILE A 31 -32.304 -4.726 25.536 1.00 18.96 O
ANISOU 243 O ILE A 31 2458 1907 2839 -203 -273 -307 O
ATOM 244 N GLY A 32 -32.441 -2.692 26.424 1.00 18.52 N
ANISOU 244 N GLY A 32 2508 1763 2763 -146 107 -433 N
ATOM 245 CA GLY A 32 -31.045 -2.432 26.240 1.00 18.85 C
ANISOU 245 CA GLY A 32 2594 2119 2449 -233 269 -230 C
ATOM 246 C GLY A 32 -30.588 -1.300 27.116 1.00 19.36 C
ANISOU 246 C GLY A 32 2712 2108 2537 -242 390 -432 C
ATOM 247 O GLY A 32 -31.380 -0.735 27.871 1.00 28.03 O
ANISOU 247 O GLY A 32 3018 3351 4280 -796 1121 -1535 O
ATOM 248 N ILE A 33 -29.294 -1.019 27.057 1.00 17.77 N
ANISOU 248 N ILE A 33 2788 1814 2146 -261 97 -329 N
ATOM 249 CA ILE A 33 -28.708 0.044 27.831 1.00 16.05 C
ANISOU 249 CA ILE A 33 2638 1891 1568 -222 64 -223 C
ATOM 250 CB ILE A 33 -27.254 -0.280 28.203 1.00 16.84 C
ANISOU 250 CB ILE A 33 2784 1853 1759 -290 -221 -353 C
ATOM 251 CG1 ILE A 33 -27.200 -1.547 29.076 1.00 18.78 C
ANISOU 251 CG1 ILE A 33 3031 1968 2134 7 -306 -167 C
ATOM 252 CG2 ILE A 33 -26.649 0.925 28.904 1.00 15.40 C
ANISOU 252 CG2 ILE A 33 2449 1729 1671 -364 -87 -204 C
ATOM 253 CD1 ILE A 33 -25.822 -1.917 29.613 1.00 21.48 C
ANISOU 253 CD1 ILE A 33 3185 2524 2453 399 23 -169 C
ATOM 254 C ILE A 33 -28.842 1.336 27.032 1.00 15.00 C
ANISOU 254 C ILE A 33 2458 1830 1410 -435 -94 -324 C
ATOM 255 O ILE A 33 -28.366 1.454 25.905 1.00 17.47 O
ANISOU 255 O ILE A 33 3288 1775 1571 -357 281 -228 O
ATOM 256 N PRO A 34 -29.552 2.354 27.542 1.00 14.15 N
ANISOU 256 N PRO A 34 2277 1881 1216 -299 141 25 N
ATOM 257 CA PRO A 34 -29.830 3.533 26.729 1.00 13.97 C
ANISOU 257 CA PRO A 34 2254 1665 1389 -272 -77 -99 C
ATOM 258 CB PRO A 34 -30.992 4.247 27.412 1.00 17.06 C
ANISOU 258 CB PRO A 34 2280 2206 1994 -171 153 67 C
ATOM 259 CG PRO A 34 -31.036 3.695 28.759 1.00 20.11 C
ANISOU 259 CG PRO A 34 2955 2912 1774 385 257 -165 C
ATOM 260 CD PRO A 34 -30.265 2.397 28.808 1.00 16.64 C
ANISOU 260 CD PRO A 34 2645 2290 1387 -121 341 -153 C
ATOM 261 C PRO A 34 -28.648 4.504 26.600 1.00 12.91 C
ANISOU 261 C PRO A 34 1995 1581 1326 -111 9 -216 C
ATOM 262 O PRO A 34 -27.665 4.447 27.372 1.00 14.15 O
ANISOU 262 O PRO A 34 2118 1807 1450 -145 -162 -102 O
ATOM 263 N TYR A 35 -28.806 5.400 25.627 1.00 12.87 N
ANISOU 263 N TYR A 35 1939 1687 1262 -86 -62 -150 N
ATOM 264 CA TYR A 35 -27.871 6.493 25.364 1.00 13.45 C
ANISOU 264 CA TYR A 35 1880 1768 1460 -168 114 -199 C
ATOM 265 CB TYR A 35 -27.473 6.468 23.887 1.00 14.52 C
ANISOU 265 CB TYR A 35 1985 1959 1572 -266 363 -99 C
ATOM 266 CG TYR A 35 -26.341 5.523 23.607 1.00 15.35 C
ANISOU 266 CG TYR A 35 2123 2249 1460 -37 329 -297 C
ATOM 267 CD1 TYR A 35 -26.564 4.156 23.570 1.00 16.47 C
ANISOU 267 CD1 TYR A 35 2474 2333 1448 270 414 -326 C
ATOM 268 CE1 TYR A 35 -25.527 3.266 23.374 1.00 19.53 C
ANISOU 268 CE1 TYR A 35 3083 2678 1657 734 376 -358 C
ATOM 269 CZ TYR A 35 -24.248 3.739 23.188 1.00 20.11 C
ANISOU 269 CZ TYR A 35 2785 3241 1614 1043 143 -482 C
ATOM 270 OH TYR A 35 -23.237 2.850 22.965 1.00 29.15 O
ANISOU 270 OH TYR A 35 3816 5068 2191 2328 -44 -911 O
ATOM 271 CE2 TYR A 35 -24.003 5.093 23.202 1.00 19.48 C
ANISOU 271 CE2 TYR A 35 2193 3451 1758 416 220 -1008 C
ATOM 272 CD2 TYR A 35 -25.042 5.977 23.426 1.00 16.77 C
ANISOU 272 CD2 TYR A 35 2116 2422 1831 83 341 -696 C
ATOM 273 C TYR A 35 -28.449 7.843 25.782 1.00 14.48 C
ANISOU 273 C TYR A 35 1991 1753 1756 -153 163 -108 C
ATOM 274 O TYR A 35 -27.810 8.859 25.568 1.00 14.65 O
ANISOU 274 O TYR A 35 2157 1645 1763 -113 221 43 O
ATOM 275 N SER A 36 -29.647 7.823 26.368 1.00 13.77 N
ANISOU 275 N SER A 36 1841 1389 2001 -101 107 -299 N
ATOM 276 CA SER A 36 -30.250 8.980 27.022 1.00 17.20 C
ANISOU 276 CA SER A 36 2100 2012 2422 119 299 -597 C
ATOM 277 CB SER A 36 -31.740 8.788 27.079 1.00 18.78 C
ANISOU 277 CB SER A 36 2198 2268 2668 -20 290 -885 C
ATOM 278 OG SER A 36 -32.039 7.563 27.724 1.00 19.25 O
ANISOU 278 OG SER A 36 2038 2829 2447 -284 266 -663 O
ATOM 279 C SER A 36 -29.617 9.116 28.418 1.00 16.97 C
ANISOU 279 C SER A 36 2265 1859 2321 -13 285 -693 C
ATOM 280 O SER A 36 -29.127 8.160 28.989 1.00 18.40 O
ANISOU 280 O SER A 36 2318 2164 2506 -44 75 -505 O
ATOM 281 N THR A 37 -29.695 10.310 28.996 1.00 16.67 N
ANISOU 281 N THR A 37 2090 1746 2498 -359 270 -582 N
ATOM 282 CA THR A 37 -29.037 10.668 30.270 1.00 16.70 C
ANISOU 282 CA THR A 37 2146 2112 2086 -93 230 -230 C
ATOM 283 CB THR A 37 -29.906 10.312 31.485 1.00 17.18 C
ANISOU 283 CB THR A 37 2273 2120 2134 -219 325 -220 C
ATOM 284 OG1 THR A 37 -30.081 8.905 31.691 1.00 18.06 O
ANISOU 284 OG1 THR A 37 2150 2135 2576 -197 142 -359 O
ATOM 285 CG2 THR A 37 -31.276 10.943 31.417 1.00 18.67 C
ANISOU 285 CG2 THR A 37 2586 2220 2286 -19 427 -167 C
ATOM 286 C THR A 37 -27.612 10.088 30.352 1.00 15.27 C
ANISOU 286 C THR A 37 2213 1962 1628 -58 17 -115 C
ATOM 287 O THR A 37 -27.144 9.663 31.429 1.00 17.17 O
ANISOU 287 O THR A 37 2507 2180 1837 -436 -166 266 O
ATOM 288 N PHE A 38 -26.870 10.178 29.241 1.00 14.18 N
ANISOU 288 N PHE A 38 2131 1773 1482 -177 -118 -188 N
ATOM 289 CA PHE A 38 -25.460 9.854 29.198 1.00 13.67 C
ANISOU 289 CA PHE A 38 2040 1508 1645 -289 -13 -30 C
ATOM 290 CB PHE A 38 -25.031 9.687 27.737 1.00 15.64 C
ANISOU 290 CB PHE A 38 2230 1950 1759 -175 -68 -293 C
ATOM 291 CG PHE A 38 -23.811 8.847 27.418 1.00 14.25 C
ANISOU 291 CG PHE A 38 1970 1745 1698 -338 -62 -144 C
ATOM 292 CD1 PHE A 38 -22.637 8.901 28.153 1.00 15.82 C
ANISOU 292 CD1 PHE A 38 1921 2135 1952 -252 -13 -138 C
ATOM 293 CE1 PHE A 38 -21.542 8.125 27.800 1.00 14.08 C
ANISOU 293 CE1 PHE A 38 2014 1723 1612 -319 -184 -235 C
ATOM 294 CZ PHE A 38 -21.581 7.317 26.701 1.00 15.19 C
ANISOU 294 CZ PHE A 38 2147 1828 1797 -264 -110 -305 C
ATOM 295 CD2 PHE A 38 -23.833 8.015 26.323 1.00 15.55 C
ANISOU 295 CD2 PHE A 38 2300 1675 1932 -202 -3 -256 C
ATOM 296 CE2 PHE A 38 -22.719 7.271 25.950 1.00 15.55 C
ANISOU 296 CE2 PHE A 38 2233 1994 1678 -73 -198 -361 C
ATOM 297 C PHE A 38 -24.705 10.997 29.890 1.00 13.68 C
ANISOU 297 C PHE A 38 2167 1304 1727 -245 24 4 C
ATOM 298 O PHE A 38 -24.865 12.140 29.506 1.00 16.89 O
ANISOU 298 O PHE A 38 2731 1286 2400 -196 -399 204 O
ATOM 299 N GLN A 39 -23.947 10.694 30.940 1.00 12.94 N
ANISOU 299 N GLN A 39 2002 1235 1678 -195 3 -203 N
ATOM 300 CA GLN A 39 -23.313 11.738 31.756 1.00 12.93 C
ANISOU 300 CA GLN A 39 2074 1025 1811 -183 61 -202 C
ATOM 301 CB GLN A 39 -23.086 11.234 33.177 1.00 14.43 C
ANISOU 301 CB GLN A 39 2402 1241 1840 -240 75 -141 C
ATOM 302 CG GLN A 39 -24.356 10.778 33.873 1.00 15.84 C
ANISOU 302 CG GLN A 39 2644 1449 1923 -434 241 -144 C
ATOM 303 CD GLN A 39 -25.400 11.854 33.978 1.00 21.74 C
ANISOU 303 CD GLN A 39 3314 1902 3044 -297 335 -302 C
ATOM 304 OE1 GLN A 39 -25.142 12.865 34.607 1.00 28.25 O
ANISOU 304 OE1 GLN A 39 4390 2769 3572 -9 676 -1487 O
ATOM 305 NE2 GLN A 39 -26.557 11.652 33.333 1.00 27.03 N
ANISOU 305 NE2 GLN A 39 3313 3070 3887 -547 433 -92 N
ATOM 306 C GLN A 39 -21.974 12.171 31.154 1.00 12.81 C
ANISOU 306 C GLN A 39 1990 1173 1703 -131 -52 -200 C
ATOM 307 O GLN A 39 -21.139 11.330 30.799 1.00 13.49 O
ANISOU 307 O GLN A 39 1628 1462 2035 -208 5 -315 O
ATOM 308 N THR A 40 -21.801 13.488 31.053 1.00 13.68 N
ANISOU 308 N THR A 40 1963 1146 2088 -54 37 -147 N
ATOM 309 CA THR A 40 -20.512 14.142 30.813 1.00 12.96 C
ANISOU 309 CA THR A 40 2167 945 1812 -109 15 -232 C
ATOM 310 CB THR A 40 -20.546 15.044 29.582 1.00 13.83 C
ANISOU 310 CB THR A 40 2423 1213 1616 -250 21 -218 C
ATOM 311 OG1 THR A 40 -20.724 14.251 28.396 1.00 16.73 O
ANISOU 311 OG1 THR A 40 3007 1631 1718 -272 -278 -293 O
ATOM 312 CG2 THR A 40 -19.257 15.820 29.422 1.00 15.65 C
ANISOU 312 CG2 THR A 40 2540 1383 2023 -278 95 -49 C
ATOM 313 C THR A 40 -20.169 14.881 32.105 1.00 12.99 C
ANISOU 313 C THR A 40 2087 1170 1677 -75 201 -254 C
ATOM 314 O THR A 40 -20.823 15.859 32.458 1.00 15.31 O
ANISOU 314 O THR A 40 2419 1348 2047 232 51 -355 O
ATOM 315 N ILE A 41 -19.189 14.339 32.843 1.00 12.54 N
ANISOU 315 N ILE A 41 1980 1173 1608 -115 215 -443 N
ATOM 316 CA ILE A 41 -18.873 14.796 34.185 1.00 12.66 C
ANISOU 316 CA ILE A 41 2089 1205 1516 -151 401 -435 C
ATOM 317 CB ILE A 41 -18.737 13.606 35.134 1.00 13.20 C
ANISOU 317 CB ILE A 41 2133 1286 1596 -293 328 -364 C
ATOM 318 CG1 ILE A 41 -20.002 12.739 35.070 1.00 14.00 C
ANISOU 318 CG1 ILE A 41 2033 1450 1833 -341 579 -301 C
ATOM 319 CG2 ILE A 41 -18.394 14.060 36.550 1.00 13.66 C
ANISOU 319 CG2 ILE A 41 2281 1261 1646 -356 392 -437 C
ATOM 320 CD1 ILE A 41 -19.881 11.441 35.794 1.00 15.18 C
ANISOU 320 CD1 ILE A 41 2197 1444 2127 -408 633 -238 C
ATOM 321 C ILE A 41 -17.600 15.642 34.146 1.00 13.67 C
ANISOU 321 C ILE A 41 2035 1424 1734 -166 404 -460 C
ATOM 322 O ILE A 41 -16.561 15.190 33.655 1.00 13.52 O
ANISOU 322 O ILE A 41 1675 1592 1868 -274 303 -634 O
ATOM 323 N GLN A 42 -17.724 16.875 34.639 1.00 13.15 N
ANISOU 323 N GLN A 42 1997 1239 1758 -133 83 -320 N
ATOM 324 CA GLN A 42 -16.591 17.819 34.709 1.00 13.69 C
ANISOU 324 CA GLN A 42 1805 1607 1789 -152 3 -329 C
ATOM 325 CB GLN A 42 -17.078 19.270 34.724 1.00 17.63 C
ANISOU 325 CB GLN A 42 2529 1557 2610 -201 -351 -208 C
ATOM 326 CG GLN A 42 -17.795 19.651 33.434 1.00 23.48 C
ANISOU 326 CG GLN A 42 3135 2478 3307 152 -868 -274 C
ATOM 327 CD GLN A 42 -18.204 21.103 33.423 1.00 31.12 C
ANISOU 327 CD GLN A 42 5048 2709 4066 441 -729 -132 C
ATOM 328 OE1 GLN A 42 -18.412 21.724 34.466 1.00 40.14 O
ANISOU 328 OE1 GLN A 42 6881 3395 4973 523 -578 -987 O
ATOM 329 NE2 GLN A 42 -18.334 21.650 32.225 1.00 40.72 N
ANISOU 329 NE2 GLN A 42 6556 4695 4218 699 4 579 N
ATOM 330 C GLN A 42 -15.778 17.533 35.960 1.00 12.01 C
ANISOU 330 C GLN A 42 1829 1317 1418 -182 169 -381 C
ATOM 331 O GLN A 42 -16.329 17.090 36.968 1.00 12.78 O
ANISOU 331 O GLN A 42 1885 1590 1378 -212 251 -423 O
ATOM 332 N PRO A 43 -14.464 17.806 35.945 1.00 11.81 N
ANISOU 332 N PRO A 43 1941 1271 1272 -311 140 -316 N
ATOM 333 CA PRO A 43 -13.653 17.660 37.150 1.00 12.09 C
ANISOU 333 CA PRO A 43 1763 1406 1423 -421 38 -358 C
ATOM 334 CB PRO A 43 -12.202 17.838 36.673 1.00 13.82 C
ANISOU 334 CB PRO A 43 1967 1637 1646 -417 175 -493 C
ATOM 335 CG PRO A 43 -12.332 18.605 35.378 1.00 17.41 C
ANISOU 335 CG PRO A 43 2245 2465 1905 -661 143 -213 C
ATOM 336 CD PRO A 43 -13.696 18.310 34.807 1.00 14.19 C
ANISOU 336 CD PRO A 43 2150 1706 1536 -644 155 -143 C
ATOM 337 C PRO A 43 -14.050 18.713 38.195 1.00 12.98 C
ANISOU 337 C PRO A 43 2002 1358 1572 -178 135 -323 C
ATOM 338 O PRO A 43 -14.672 19.731 37.871 1.00 13.18 O
ANISOU 338 O PRO A 43 1985 1300 1723 -88 20 -427 O
ATOM 339 N VAL A 44 -13.688 18.455 39.462 1.00 12.09 N
ANISOU 339 N VAL A 44 1851 1292 1449 -234 298 -443 N
ATOM 340 CA VAL A 44 -14.074 19.335 40.551 1.00 12.78 C
ANISOU 340 CA VAL A 44 1951 1390 1513 -243 426 -498 C
ATOM 341 CB VAL A 44 -13.885 18.669 41.922 1.00 14.18 C
ANISOU 341 CB VAL A 44 2155 1679 1552 -303 331 -331 C
ATOM 342 CG1 VAL A 44 -14.727 17.392 42.040 1.00 14.36 C
ANISOU 342 CG1 VAL A 44 2194 1711 1548 -375 369 -222 C
ATOM 343 CG2 VAL A 44 -12.425 18.414 42.243 1.00 15.37 C
ANISOU 343 CG2 VAL A 44 2276 1951 1609 -262 254 -385 C
ATOM 344 C VAL A 44 -13.328 20.674 40.504 1.00 12.86 C
ANISOU 344 C VAL A 44 1903 1520 1461 -350 290 -603 C
ATOM 345 O VAL A 44 -13.792 21.663 41.084 1.00 13.41 O
ANISOU 345 O VAL A 44 1898 1345 1849 -367 410 -608 O
ATOM 346 N SER A 45 -12.176 20.699 39.845 1.00 14.23 N
ANISOU 346 N SER A 45 2168 1594 1645 -576 566 -747 N
ATOM 347 CA SER A 45 -11.397 21.923 39.645 1.00 15.71 C
ANISOU 347 CA SER A 45 2240 1867 1859 -869 513 -720 C
ATOM 348 CB SER A 45 -10.206 22.007 40.565 1.00 16.30 C
ANISOU 348 CB SER A 45 2588 1901 1701 -1174 451 -697 C
ATOM 349 OG SER A 45 -9.270 20.957 40.326 1.00 18.57 O
ANISOU 349 OG SER A 45 2588 2327 2141 -1059 -56 -545 O
ATOM 350 C SER A 45 -10.983 21.983 38.182 1.00 14.93 C
ANISOU 350 C SER A 45 2121 1817 1732 -779 261 -667 C
ATOM 351 O SER A 45 -10.955 20.949 37.518 1.00 14.74 O
ANISOU 351 O SER A 45 2085 1810 1704 -650 137 -693 O
ATOM 352 N ASP A 46 -10.702 23.184 37.677 1.00 14.82 N
ANISOU 352 N ASP A 46 2251 1633 1745 -517 382 -637 N
ATOM 353 CA AASP A 46 -10.323 23.323 36.287 0.70 15.93 C
ANISOU 353 CA AASP A 46 2283 1893 1877 -371 322 -505 C
ATOM 354 CA BASP A 46 -10.283 23.368 36.285 0.30 15.25 C
ANISOU 354 CA BASP A 46 2132 1940 1721 -426 314 -618 C
ATOM 355 CB AASP A 46 -9.999 24.776 35.951 0.70 17.73 C
ANISOU 355 CB AASP A 46 2640 1828 2267 -446 350 -559 C
ATOM 356 CB BASP A 46 -9.856 24.816 35.991 0.30 14.86 C
ANISOU 356 CB BASP A 46 2131 1944 1571 -439 340 -694 C
ATOM 357 CG AASP A 46 -11.198 25.712 35.915 0.70 21.67 C
ANISOU 357 CG AASP A 46 2907 2203 3122 -210 211 -369 C
ATOM 358 CG BASP A 46 -9.585 25.147 34.519 0.30 15.72 C
ANISOU 358 CG BASP A 46 2062 2275 1637 -359 397 -579 C
ATOM 359 OD1AASP A 46 -12.353 25.233 35.941 0.70 25.77 O
ANISOU 359 OD1AASP A 46 3032 2962 3797 -175 160 -144 O
ATOM 360 OD1BASP A 46 -10.228 24.544 33.672 0.30 16.96 O
ANISOU 360 OD1BASP A 46 2072 2586 1784 -538 321 -452 O
ATOM 361 OD2AASP A 46 -10.956 26.940 35.856 0.70 28.34 O
ANISOU 361 OD2AASP A 46 3795 2166 4806 97 38 -268 O
ATOM 362 OD2BASP A 46 -8.756 26.053 34.228 0.30 15.42 O
ANISOU 362 OD2BASP A 46 1951 2412 1494 -678 -217 -1132 O
ATOM 363 C ASP A 46 -9.122 22.410 36.023 1.00 14.28 C
ANISOU 363 C ASP A 46 2189 1593 1644 -507 339 -570 C
ATOM 364 O ASP A 46 -8.185 22.323 36.837 1.00 15.53 O
ANISOU 364 O ASP A 46 2239 2047 1613 -480 238 -614 O
ATOM 365 N ALA A 47 -9.169 21.709 34.894 1.00 13.62 N
ANISOU 365 N ALA A 47 1863 1753 1558 -481 292 -543 N
ATOM 366 CA ALA A 47 -8.108 20.798 34.516 1.00 13.91 C
ANISOU 366 CA ALA A 47 1914 1624 1747 -472 220 -641 C
ATOM 367 CB ALA A 47 -8.440 20.157 33.192 1.00 14.51 C
ANISOU 367 CB ALA A 47 1948 1792 1771 -713 97 -591 C
ATOM 368 C ALA A 47 -6.788 21.551 34.396 1.00 13.10 C
ANISOU 368 C ALA A 47 1978 1472 1525 -534 208 -539 C
ATOM 369 O ALA A 47 -6.758 22.717 33.981 1.00 13.60 O
ANISOU 369 O ALA A 47 2019 1493 1652 -344 182 -420 O
ATOM 370 N PRO A 48 -5.649 20.910 34.720 1.00 13.28 N
ANISOU 370 N PRO A 48 2077 1477 1488 -553 362 -287 N
ATOM 371 CA PRO A 48 -4.357 21.578 34.599 1.00 13.21 C
ANISOU 371 CA PRO A 48 1959 1481 1576 -569 0 -522 C
ATOM 372 CB PRO A 48 -3.362 20.562 35.147 1.00 15.10 C
ANISOU 372 CB PRO A 48 2084 1905 1745 -458 65 -302 C
ATOM 373 CG PRO A 48 -4.087 19.213 34.980 1.00 15.47 C
ANISOU 373 CG PRO A 48 2143 1746 1986 -315 -106 -111 C
ATOM 374 CD PRO A 48 -5.547 19.535 35.215 1.00 15.21 C
ANISOU 374 CD PRO A 48 2269 1571 1939 -430 157 -218 C
ATOM 375 C PRO A 48 -4.089 21.882 33.122 1.00 12.91 C
ANISOU 375 C PRO A 48 1837 1412 1656 -692 119 -390 C
ATOM 376 O PRO A 48 -4.225 20.999 32.270 1.00 13.60 O
ANISOU 376 O PRO A 48 1877 1447 1842 -466 107 -516 O
ATOM 377 N ASN A 49 -3.710 23.122 32.817 1.00 13.13 N
ANISOU 377 N ASN A 49 2175 1289 1525 -563 182 -444 N
ATOM 378 CA ASN A 49 -3.676 23.587 31.416 1.00 13.55 C
ANISOU 378 CA ASN A 49 2124 1403 1619 -455 188 -402 C
ATOM 379 CB ASN A 49 -3.311 25.063 31.362 1.00 15.08 C
ANISOU 379 CB ASN A 49 2623 1365 1741 -532 141 -646 C
ATOM 380 CG ASN A 49 -3.450 25.642 29.973 1.00 16.07 C
ANISOU 380 CG ASN A 49 2651 1623 1829 -212 230 -559 C
ATOM 381 OD1 ASN A 49 -4.494 25.515 29.346 1.00 18.08 O
ANISOU 381 OD1 ASN A 49 3174 1776 1919 -290 -96 -310 O
ATOM 382 ND2 ASN A 49 -2.405 26.283 29.499 1.00 19.04 N
ANISOU 382 ND2 ASN A 49 3158 1719 2357 -268 894 -676 N
ATOM 383 C ASN A 49 -2.682 22.782 30.564 1.00 13.11 C
ANISOU 383 C ASN A 49 2175 1267 1538 -557 265 -370 C
ATOM 384 O ASN A 49 -2.892 22.626 29.368 1.00 13.67 O
ANISOU 384 O ASN A 49 2151 1552 1488 -449 236 -373 O
ATOM 385 N ASN A 50 -1.625 22.262 31.191 1.00 13.53 N
ANISOU 385 N ASN A 50 1857 1456 1827 -409 396 -327 N
ATOM 386 CA ASN A 50 -0.593 21.483 30.500 1.00 14.74 C
ANISOU 386 CA ASN A 50 2019 1637 1941 -237 381 -418 C
ATOM 387 CB ASN A 50 0.805 21.958 30.891 1.00 16.10 C
ANISOU 387 CB ASN A 50 1916 1764 2434 -266 389 -403 C
ATOM 388 CG ASN A 50 1.172 21.554 32.299 1.00 19.99 C
ANISOU 388 CG ASN A 50 2451 2338 2805 -374 -162 -528 C
ATOM 389 OD1 ASN A 50 0.285 21.131 33.054 1.00 22.96 O
ANISOU 389 OD1 ASN A 50 2854 2371 3498 -701 -174 -800 O
ATOM 390 ND2 ASN A 50 2.436 21.669 32.665 1.00 28.09 N
ANISOU 390 ND2 ASN A 50 2600 3427 4643 -558 -535 -475 N
ATOM 391 C ASN A 50 -0.720 19.971 30.767 1.00 13.82 C
ANISOU 391 C ASN A 50 1867 1596 1789 -184 289 -342 C
ATOM 392 O ASN A 50 0.208 19.209 30.454 1.00 15.32 O
ANISOU 392 O ASN A 50 2112 1742 1968 -72 507 -328 O
ATOM 393 N GLY A 51 -1.845 19.526 31.333 1.00 13.41 N
ANISOU 393 N GLY A 51 1985 1472 1636 -283 261 -332 N
ATOM 394 CA GLY A 51 -2.103 18.107 31.525 1.00 13.76 C
ANISOU 394 CA GLY A 51 2194 1471 1560 -331 284 -395 C
ATOM 395 C GLY A 51 -1.455 17.460 32.748 1.00 13.23 C
ANISOU 395 C GLY A 51 1958 1586 1483 -457 171 -464 C
ATOM 396 O GLY A 51 -1.685 16.277 32.982 1.00 13.60 O
ANISOU 396 O GLY A 51 2072 1449 1644 -352 -104 -532 O
ATOM 397 N AILE A 52 -0.736 18.218 33.577 0.50 12.91 N
ANISOU 397 N AILE A 52 1972 1454 1480 -361 182 -497 N
ATOM 398 N BILE A 52 -0.722 18.217 33.568 0.50 13.31 N
ANISOU 398 N BILE A 52 2015 1458 1584 -357 98 -494 N
ATOM 399 CA AILE A 52 0.006 17.649 34.703 0.50 13.94 C
ANISOU 399 CA AILE A 52 2063 1738 1494 -455 101 -538 C
ATOM 400 CA BILE A 52 -0.009 17.667 34.720 0.50 14.71 C
ANISOU 400 CA BILE A 52 2179 1776 1634 -438 -16 -530 C
ATOM 401 CB AILE A 52 1.486 18.043 34.626 0.50 14.47 C
ANISOU 401 CB AILE A 52 2028 2044 1424 -368 181 -583 C
ATOM 402 CB BILE A 52 1.461 18.091 34.742 0.50 16.32 C
ANISOU 402 CB BILE A 52 2157 2213 1830 -362 -152 -518 C
ATOM 403 CG1AILE A 52 2.189 17.297 33.491 0.50 13.88 C
ANISOU 403 CG1AILE A 52 1868 2000 1405 -455 276 -515 C
ATOM 404 CG1BILE A 52 2.114 17.919 33.382 0.50 17.55 C
ANISOU 404 CG1BILE A 52 2268 2522 1876 -354 -121 -566 C
ATOM 405 CG2AILE A 52 2.155 17.816 35.972 0.50 16.16 C
ANISOU 405 CG2AILE A 52 2142 2417 1582 -343 27 -520 C
ATOM 406 CG2BILE A 52 2.197 17.297 35.813 0.50 16.69 C
ANISOU 406 CG2BILE A 52 2049 2449 1841 -312 -272 -566 C
ATOM 407 CD1AILE A 52 3.559 17.837 33.151 0.50 13.78 C
ANISOU 407 CD1AILE A 52 1818 2164 1253 -378 391 -615 C
ATOM 408 CD1BILE A 52 2.113 16.505 32.958 0.50 18.98 C
ANISOU 408 CD1BILE A 52 2555 2604 2051 -394 -39 -713 C
ATOM 409 C AILE A 52 -0.607 18.113 36.025 0.50 14.14 C
ANISOU 409 C AILE A 52 2161 1732 1478 -489 86 -595 C
ATOM 410 C BILE A 52 -0.673 18.135 36.011 0.50 14.52 C
ANISOU 410 C BILE A 52 2229 1673 1614 -526 21 -556 C
ATOM 411 O AILE A 52 -0.497 19.294 36.371 0.50 15.49 O
ANISOU 411 O AILE A 52 2464 1792 1628 -536 141 -687 O
ATOM 412 O BILE A 52 -0.686 19.348 36.309 0.50 15.51 O
ANISOU 412 O BILE A 52 2569 1670 1652 -549 271 -536 O
ATOM 413 N GLY A 53 -1.177 17.181 36.792 1.00 14.83 N
ANISOU 413 N GLY A 53 2358 1702 1574 -491 123 -612 N
ATOM 414 CA GLY A 53 -1.767 17.510 38.077 1.00 16.23 C
ANISOU 414 CA GLY A 53 2568 1970 1629 -660 247 -713 C
ATOM 415 C GLY A 53 -2.905 16.588 38.430 1.00 15.21 C
ANISOU 415 C GLY A 53 2660 1642 1474 -619 350 -929 C
ATOM 416 O GLY A 53 -3.399 15.817 37.619 1.00 14.59 O
ANISOU 416 O GLY A 53 2246 1689 1606 -570 356 -1007 O
ATOM 417 N GLN A 54 -3.328 16.671 39.688 1.00 17.50 N
ANISOU 417 N GLN A 54 3266 1791 1589 -647 608 -752 N
ATOM 418 CA AGLN A 54 -4.404 15.820 40.160 0.70 17.66 C
ANISOU 418 CA AGLN A 54 3172 1742 1796 -493 644 -740 C
ATOM 419 CA BGLN A 54 -4.415 15.830 40.168 0.30 16.85 C
ANISOU 419 CA BGLN A 54 3076 1430 1894 -396 669 -737 C
ATOM 420 CB AGLN A 54 -4.424 15.849 41.685 0.70 19.53 C
ANISOU 420 CB AGLN A 54 3446 2162 1810 -339 809 -655 C
ATOM 421 CB BGLN A 54 -4.622 15.943 41.671 0.30 16.27 C
ANISOU 421 CB BGLN A 54 2965 1288 1927 -380 769 -693 C
ATOM 422 CG AGLN A 54 -5.279 14.773 42.313 0.70 19.65 C
ANISOU 422 CG AGLN A 54 3369 2199 1899 -21 824 -395 C
ATOM 423 CG BGLN A 54 -3.594 15.201 42.459 0.30 14.92 C
ANISOU 423 CG BGLN A 54 2831 854 1981 -256 790 -761 C
ATOM 424 CD AGLN A 54 -5.224 14.871 43.822 0.70 21.39 C
ANISOU 424 CD AGLN A 54 3685 2522 1920 348 242 -168 C
ATOM 425 CD BGLN A 54 -4.036 15.170 43.894 0.30 13.88 C
ANISOU 425 CD BGLN A 54 2619 654 2000 -171 829 -813 C
ATOM 426 OE1AGLN A 54 -5.847 15.742 44.416 0.70 21.33 O
ANISOU 426 OE1AGLN A 54 3167 2651 2285 623 175 129 O
ATOM 427 OE1BGLN A 54 -5.111 15.661 44.238 0.30 14.32 O
ANISOU 427 OE1BGLN A 54 2515 822 2102 17 576 -650 O
ATOM 428 NE2AGLN A 54 -4.462 14.000 44.473 0.70 22.43 N
ANISOU 428 NE2AGLN A 54 3821 2552 2149 486 144 -226 N
ATOM 429 NE2BGLN A 54 -3.182 14.635 44.742 0.30 15.25 N
ANISOU 429 NE2BGLN A 54 2668 789 2335 31 677 -823 N
ATOM 430 C GLN A 54 -5.708 16.268 39.500 1.00 17.33 C
ANISOU 430 C GLN A 54 3158 1310 2115 -202 820 -518 C
ATOM 431 O GLN A 54 -5.980 17.488 39.368 1.00 20.55 O
ANISOU 431 O GLN A 54 3800 1297 2709 -37 833 -560 O
ATOM 432 N ILE A 55 -6.531 15.282 39.138 1.00 14.84 N
ANISOU 432 N ILE A 55 2524 1282 1830 -18 529 -220 N
ATOM 433 CA ILE A 55 -7.824 15.494 38.518 1.00 16.06 C
ANISOU 433 CA ILE A 55 2472 1623 2006 178 664 21 C
ATOM 434 CB ILE A 55 -7.773 15.133 37.021 1.00 16.12 C
ANISOU 434 CB ILE A 55 2251 1932 1939 257 764 15 C
ATOM 435 CG1 ILE A 55 -6.762 15.983 36.239 1.00 16.52 C
ANISOU 435 CG1 ILE A 55 2123 2018 2135 270 768 -26 C
ATOM 436 CG2 ILE A 55 -9.152 15.196 36.414 1.00 17.71 C
ANISOU 436 CG2 ILE A 55 2267 2436 2023 83 801 148 C
ATOM 437 CD1 ILE A 55 -6.256 15.307 34.989 1.00 16.21 C
ANISOU 437 CD1 ILE A 55 2068 2155 1934 330 610 43 C
ATOM 438 C ILE A 55 -8.829 14.615 39.251 1.00 14.38 C
ANISOU 438 C ILE A 55 2090 1472 1901 427 560 139 C
ATOM 439 O ILE A 55 -8.607 13.428 39.357 1.00 14.67 O
ANISOU 439 O ILE A 55 2227 1328 2017 214 582 22 O
ATOM 440 N THR A 56 -9.915 15.202 39.753 1.00 14.25 N
ANISOU 440 N THR A 56 2294 1574 1543 393 650 -39 N
ATOM 441 CA THR A 56 -10.920 14.445 40.485 1.00 15.39 C
ANISOU 441 CA THR A 56 2324 1885 1636 475 658 195 C
ATOM 442 CB THR A 56 -10.956 14.797 41.975 1.00 16.61 C
ANISOU 442 CB THR A 56 2486 2253 1572 475 567 219 C
ATOM 443 OG1 THR A 56 -9.710 14.407 42.532 1.00 20.33 O
ANISOU 443 OG1 THR A 56 2576 3347 1802 763 592 581 O
ATOM 444 CG2 THR A 56 -12.075 14.107 42.722 1.00 19.05 C
ANISOU 444 CG2 THR A 56 2604 2913 1718 577 953 171 C
ATOM 445 C THR A 56 -12.303 14.667 39.876 1.00 14.02 C
ANISOU 445 C THR A 56 2181 1527 1618 538 664 19 C
ATOM 446 O THR A 56 -12.700 15.811 39.629 1.00 15.42 O
ANISOU 446 O THR A 56 2434 1583 1839 711 257 36 O
ATOM 447 N PHE A 57 -13.023 13.560 39.694 1.00 14.41 N
ANISOU 447 N PHE A 57 2245 1649 1578 534 727 1 N
ATOM 448 CA PHE A 57 -14.437 13.569 39.371 1.00 13.74 C
ANISOU 448 CA PHE A 57 2194 1382 1642 352 667 101 C
ATOM 449 CB PHE A 57 -14.748 12.661 38.179 1.00 14.48 C
ANISOU 449 CB PHE A 57 2172 1434 1893 368 634 -78 C
ATOM 450 CG PHE A 57 -13.963 13.016 36.947 1.00 14.09 C
ANISOU 450 CG PHE A 57 2229 1474 1647 141 517 -263 C
ATOM 451 CD1 PHE A 57 -14.348 14.072 36.134 1.00 13.17 C
ANISOU 451 CD1 PHE A 57 2025 1586 1393 147 347 -458 C
ATOM 452 CE1 PHE A 57 -13.586 14.430 35.041 1.00 13.66 C
ANISOU 452 CE1 PHE A 57 2300 1398 1490 -198 285 -444 C
ATOM 453 CZ PHE A 57 -12.415 13.787 34.780 1.00 14.63 C
ANISOU 453 CZ PHE A 57 2538 1502 1517 0 223 -417 C
ATOM 454 CD2 PHE A 57 -12.765 12.374 36.667 1.00 15.62 C
ANISOU 454 CD2 PHE A 57 2494 1595 1846 329 561 67 C
ATOM 455 CE2 PHE A 57 -12.011 12.743 35.572 1.00 15.58 C
ANISOU 455 CE2 PHE A 57 2544 1679 1695 216 527 -248 C
ATOM 456 C PHE A 57 -15.203 13.119 40.621 1.00 14.15 C
ANISOU 456 C PHE A 57 2150 1593 1630 427 716 101 C
ATOM 457 O PHE A 57 -14.823 12.120 41.243 1.00 16.09 O
ANISOU 457 O PHE A 57 2495 1732 1884 525 799 403 O
ATOM 458 N ASN A 58 -16.252 13.850 40.982 1.00 12.14 N
ANISOU 458 N ASN A 58 1777 1373 1461 87 530 -127 N
ATOM 459 CA ASN A 58 -17.020 13.572 42.186 1.00 12.17 C
ANISOU 459 CA ASN A 58 1913 1305 1403 -81 537 -273 C
ATOM 460 CB ASN A 58 -16.576 14.480 43.332 1.00 13.10 C
ANISOU 460 CB ASN A 58 2007 1604 1365 -100 486 -374 C
ATOM 461 CG ASN A 58 -17.327 14.237 44.625 1.00 16.42 C
ANISOU 461 CG ASN A 58 2653 2061 1522 -425 735 -408 C
ATOM 462 OD1 ASN A 58 -18.418 13.675 44.628 1.00 21.38 O
ANISOU 462 OD1 ASN A 58 3421 2897 1804 -1146 800 -583 O
ATOM 463 ND2 ASN A 58 -16.829 14.802 45.711 1.00 22.00 N
ANISOU 463 ND2 ASN A 58 3600 3057 1699 -547 442 -573 N
ATOM 464 C ASN A 58 -18.493 13.752 41.829 1.00 11.96 C
ANISOU 464 C ASN A 58 1806 1316 1420 -176 631 -293 C
ATOM 465 O ASN A 58 -18.971 14.889 41.695 1.00 15.23 O
ANISOU 465 O ASN A 58 2344 1414 2029 -155 354 -160 O
ATOM 466 N GLN A 59 -19.208 12.633 41.639 1.00 12.20 N
ANISOU 466 N GLN A 59 1923 1258 1454 -128 448 -138 N
ATOM 467 CA GLN A 59 -20.547 12.710 41.108 1.00 12.51 C
ANISOU 467 CA GLN A 59 1848 1335 1569 -196 385 -319 C
ATOM 468 CB GLN A 59 -20.524 12.845 39.591 1.00 13.81 C
ANISOU 468 CB GLN A 59 2112 1465 1670 -118 317 -78 C
ATOM 469 CG GLN A 59 -21.907 12.995 39.008 1.00 15.03 C
ANISOU 469 CG GLN A 59 2058 1913 1737 -309 315 22 C
ATOM 470 CD GLN A 59 -22.608 14.211 39.565 1.00 15.73 C
ANISOU 470 CD GLN A 59 2128 1682 2165 -335 231 81 C
ATOM 471 OE1 GLN A 59 -22.211 15.356 39.271 1.00 18.83 O
ANISOU 471 OE1 GLN A 59 2412 1825 2917 -331 333 342 O
ATOM 472 NE2 GLN A 59 -23.654 14.004 40.363 1.00 15.56 N
ANISOU 472 NE2 GLN A 59 1966 1990 1955 -315 3 265 N
ATOM 473 C GLN A 59 -21.369 11.508 41.561 1.00 12.59 C
ANISOU 473 C GLN A 59 1859 1553 1371 -212 277 -175 C
ATOM 474 O GLN A 59 -21.362 10.451 40.930 1.00 12.79 O
ANISOU 474 O GLN A 59 1852 1500 1505 12 274 -251 O
ATOM 475 N PRO A 60 -22.152 11.654 42.640 1.00 11.62 N
ANISOU 475 N PRO A 60 1773 1308 1333 -158 274 -279 N
ATOM 476 CA PRO A 60 -23.142 10.626 42.964 1.00 11.77 C
ANISOU 476 CA PRO A 60 1728 1397 1347 -96 321 -227 C
ATOM 477 CB PRO A 60 -23.904 11.228 44.147 1.00 12.39 C
ANISOU 477 CB PRO A 60 1575 1792 1340 -125 333 -313 C
ATOM 478 CG PRO A 60 -22.903 12.207 44.766 1.00 12.44 C
ANISOU 478 CG PRO A 60 1656 1595 1475 -108 445 -416 C
ATOM 479 CD PRO A 60 -22.145 12.780 43.591 1.00 12.72 C
ANISOU 479 CD PRO A 60 1842 1516 1475 -182 354 -375 C
ATOM 480 C PRO A 60 -24.076 10.373 41.785 1.00 12.26 C
ANISOU 480 C PRO A 60 1797 1400 1458 -19 226 -304 C
ATOM 481 O PRO A 60 -24.489 11.334 41.129 1.00 13.05 O
ANISOU 481 O PRO A 60 2025 1404 1529 -23 129 -276 O
ATOM 482 N LEU A 61 -24.399 9.101 41.538 1.00 13.27 N
ANISOU 482 N LEU A 61 1963 1507 1571 -113 264 -346 N
ATOM 483 CA LEU A 61 -25.266 8.721 40.433 1.00 13.76 C
ANISOU 483 CA LEU A 61 2036 1676 1515 -4 253 -451 C
ATOM 484 CB LEU A 61 -24.460 8.118 39.285 1.00 12.66 C
ANISOU 484 CB LEU A 61 1939 1273 1595 -57 294 -363 C
ATOM 485 CG LEU A 61 -23.531 9.083 38.541 1.00 13.76 C
ANISOU 485 CG LEU A 61 2309 1313 1604 -278 170 -249 C
ATOM 486 CD1 LEU A 61 -22.680 8.309 37.541 1.00 15.58 C
ANISOU 486 CD1 LEU A 61 2830 1316 1773 -216 277 -351 C
ATOM 487 CD2 LEU A 61 -24.335 10.161 37.831 1.00 16.24 C
ANISOU 487 CD2 LEU A 61 2800 1578 1792 0 62 -274 C
ATOM 488 C LEU A 61 -26.305 7.725 40.929 1.00 13.90 C
ANISOU 488 C LEU A 61 1934 1729 1617 -18 365 -657 C
ATOM 489 O LEU A 61 -25.956 6.692 41.511 1.00 13.95 O
ANISOU 489 O LEU A 61 2039 1957 1301 -358 227 -283 O
ATOM 490 N GLY A 62 -27.585 8.064 40.703 1.00 14.59 N
ANISOU 490 N GLY A 62 1989 1449 2103 -106 338 -705 N
ATOM 491 CA GLY A 62 -28.651 7.140 41.023 1.00 14.99 C
ANISOU 491 CA GLY A 62 1702 1741 2250 -42 589 -840 C
ATOM 492 C GLY A 62 -28.690 5.967 40.051 1.00 14.44 C
ANISOU 492 C GLY A 62 1767 1573 2144 -175 442 -708 C
ATOM 493 O GLY A 62 -28.082 5.988 38.983 1.00 14.72 O
ANISOU 493 O GLY A 62 1831 1859 1900 52 246 -700 O
ATOM 494 N ASN A 63 -29.407 4.917 40.452 1.00 13.50 N
ANISOU 494 N ASN A 63 1999 1573 1557 -99 537 -526 N
ATOM 495 CA ASN A 63 -29.758 3.858 39.513 1.00 12.14 C
ANISOU 495 CA ASN A 63 1905 1414 1292 10 422 -352 C
ATOM 496 CB ASN A 63 -30.767 4.395 38.497 1.00 13.82 C
ANISOU 496 CB ASN A 63 1880 1805 1565 42 324 -430 C
ATOM 497 CG ASN A 63 -32.033 4.849 39.174 1.00 15.66 C
ANISOU 497 CG ASN A 63 1946 2237 1766 175 317 -660 C
ATOM 498 OD1 ASN A 63 -32.311 6.054 39.251 1.00 23.04 O
ANISOU 498 OD1 ASN A 63 2947 2682 3122 715 -362 -936 O
ATOM 499 ND2 ASN A 63 -32.724 3.889 39.741 1.00 16.23 N
ANISOU 499 ND2 ASN A 63 1476 3030 1658 -93 413 -414 N
ATOM 500 C ASN A 63 -28.488 3.203 38.957 1.00 12.20 C
ANISOU 500 C ASN A 63 1840 1530 1265 15 318 -261 C
ATOM 501 O ASN A 63 -27.561 2.906 39.702 1.00 12.73 O
ANISOU 501 O ASN A 63 1980 1592 1263 146 280 -203 O
ATOM 502 N LEU A 64 -28.490 2.873 37.654 1.00 11.75 N
ANISOU 502 N LEU A 64 1834 1378 1251 129 268 -239 N
ATOM 503 CA LEU A 64 -27.397 2.112 37.067 1.00 11.43 C
ANISOU 503 CA LEU A 64 1773 1261 1308 109 274 -78 C
ATOM 504 CB LEU A 64 -27.956 1.083 36.099 1.00 12.32 C
ANISOU 504 CB LEU A 64 2046 1110 1524 67 296 -119 C
ATOM 505 CG LEU A 64 -28.934 0.067 36.693 1.00 13.13 C
ANISOU 505 CG LEU A 64 1971 1414 1601 -150 420 -336 C
ATOM 506 CD1 LEU A 64 -29.340 -0.967 35.653 1.00 14.44 C
ANISOU 506 CD1 LEU A 64 2301 1328 1857 -163 296 -408 C
ATOM 507 CD2 LEU A 64 -28.387 -0.606 37.940 1.00 14.11 C
ANISOU 507 CD2 LEU A 64 2314 1363 1681 -220 309 -328 C
ATOM 508 C LEU A 64 -26.405 3.029 36.350 1.00 11.74 C
ANISOU 508 C LEU A 64 1914 1206 1340 90 419 -163 C
ATOM 509 O LEU A 64 -26.787 3.954 35.640 1.00 12.11 O
ANISOU 509 O LEU A 64 1890 1380 1331 -12 358 -75 O
ATOM 510 N THR A 65 -25.126 2.714 36.535 1.00 11.97 N
ANISOU 510 N THR A 65 1920 1222 1406 -28 466 19 N
ATOM 511 CA THR A 65 -24.004 3.435 35.936 1.00 10.68 C
ANISOU 511 CA THR A 65 1605 989 1463 106 438 -90 C
ATOM 512 CB THR A 65 -23.147 4.115 37.013 1.00 12.01 C
ANISOU 512 CB THR A 65 1842 1106 1612 115 439 -165 C
ATOM 513 OG1 THR A 65 -23.935 5.115 37.662 1.00 13.74 O
ANISOU 513 OG1 THR A 65 2077 1417 1727 251 489 -359 O
ATOM 514 CG2 THR A 65 -21.863 4.705 36.451 1.00 13.32 C
ANISOU 514 CG2 THR A 65 1964 1466 1631 -114 350 -150 C
ATOM 515 C THR A 65 -23.189 2.447 35.089 1.00 11.66 C
ANISOU 515 C THR A 65 1930 1078 1422 111 479 -175 C
ATOM 516 O THR A 65 -22.875 1.338 35.511 1.00 12.91 O
ANISOU 516 O THR A 65 2326 1114 1461 110 526 -64 O
ATOM 517 N GLY A 66 -22.803 2.881 33.893 1.00 10.47 N
ANISOU 517 N GLY A 66 1633 917 1426 61 332 -66 N
ATOM 518 CA GLY A 66 -22.034 2.049 32.998 1.00 10.75 C
ANISOU 518 CA GLY A 66 1728 1073 1283 165 243 -145 C
ATOM 519 C GLY A 66 -20.771 1.500 33.643 1.00 10.50 C
ANISOU 519 C GLY A 66 1720 1048 1219 141 266 -154 C
ATOM 520 O GLY A 66 -20.045 2.190 34.359 1.00 11.24 O
ANISOU 520 O GLY A 66 1571 1288 1409 40 205 -291 O
ATOM 521 N GLY A 67 -20.469 0.235 33.331 1.00 10.61 N
ANISOU 521 N GLY A 67 1689 1140 1202 173 197 -373 N
ATOM 522 CA GLY A 67 -19.359 -0.446 33.961 1.00 10.56 C
ANISOU 522 CA GLY A 67 1675 1044 1291 136 131 -227 C
ATOM 523 C GLY A 67 -17.999 -0.096 33.383 1.00 10.53 C
ANISOU 523 C GLY A 67 1637 1094 1267 88 25 -94 C
ATOM 524 O GLY A 67 -16.982 -0.410 34.013 1.00 11.44 O
ANISOU 524 O GLY A 67 1638 1387 1320 21 -25 4 O
ATOM 525 N ALA A 68 -17.946 0.556 32.219 1.00 10.67 N
ANISOU 525 N ALA A 68 1498 1215 1338 18 4 1 N
ATOM 526 CA ALA A 68 -16.689 0.925 31.555 1.00 10.74 C
ANISOU 526 CA ALA A 68 1612 1242 1226 -26 91 -147 C
ATOM 527 CB ALA A 68 -16.426 0.073 30.335 1.00 11.11 C
ANISOU 527 CB ALA A 68 1526 1234 1459 -77 150 -306 C
ATOM 528 C ALA A 68 -16.681 2.416 31.259 1.00 11.12 C
ANISOU 528 C ALA A 68 1815 1242 1165 -174 178 -95 C
ATOM 529 O ALA A 68 -16.737 2.842 30.103 1.00 11.08 O
ANISOU 529 O ALA A 68 1739 1389 1081 -129 202 -135 O
ATOM 530 N PRO A 69 -16.574 3.271 32.299 1.00 10.85 N
ANISOU 530 N PRO A 69 1772 1104 1246 -109 202 -112 N
ATOM 531 CA PRO A 69 -16.513 4.716 32.073 1.00 11.05 C
ANISOU 531 CA PRO A 69 1797 1071 1328 -110 201 -242 C
ATOM 532 CB PRO A 69 -16.448 5.300 33.480 1.00 11.65 C
ANISOU 532 CB PRO A 69 1966 1060 1398 -136 147 -322 C
ATOM 533 CG PRO A 69 -15.891 4.191 34.325 1.00 12.45 C
ANISOU 533 CG PRO A 69 2062 1229 1440 -239 89 -129 C
ATOM 534 CD PRO A 69 -16.447 2.916 33.718 1.00 11.65 C
ANISOU 534 CD PRO A 69 2047 1013 1365 -102 214 -76 C
ATOM 535 C PRO A 69 -15.274 5.109 31.261 1.00 11.08 C
ANISOU 535 C PRO A 69 1663 1161 1383 -34 110 -130 C
ATOM 536 O PRO A 69 -14.238 4.441 31.296 1.00 11.52 O
ANISOU 536 O PRO A 69 1626 1309 1440 7 313 -123 O
ATOM 537 N ARG A 70 -15.412 6.182 30.498 1.00 10.18 N
ANISOU 537 N ARG A 70 1459 937 1470 163 179 -178 N
ATOM 538 CA ARG A 70 -14.369 6.665 29.629 1.00 10.62 C
ANISOU 538 CA ARG A 70 1508 1143 1383 16 181 -205 C
ATOM 539 CB ARG A 70 -14.832 6.663 28.176 1.00 11.34 C
ANISOU 539 CB ARG A 70 1581 1315 1410 56 182 -208 C
ATOM 540 CG ARG A 70 -15.424 5.338 27.708 1.00 11.56 C
ANISOU 540 CG ARG A 70 1545 1356 1489 -4 107 -199 C
ATOM 541 CD ARG A 70 -15.852 5.348 26.246 1.00 12.19 C
ANISOU 541 CD ARG A 70 1762 1349 1519 -76 57 -227 C
ATOM 542 NE ARG A 70 -14.728 5.314 25.330 1.00 12.32 N
ANISOU 542 NE ARG A 70 1887 1193 1601 -89 126 -105 N
ATOM 543 CZ ARG A 70 -14.136 4.208 24.874 1.00 11.72 C
ANISOU 543 CZ ARG A 70 1678 1296 1479 31 103 -97 C
ATOM 544 NH1 ARG A 70 -14.517 3.011 25.320 1.00 11.76 N
ANISOU 544 NH1 ARG A 70 1782 1340 1343 -145 -57 -180 N
ATOM 545 NH2 ARG A 70 -13.175 4.326 23.974 1.00 12.65 N
ANISOU 545 NH2 ARG A 70 1680 1605 1520 -93 67 -238 N
ATOM 546 C ARG A 70 -13.937 8.085 30.026 1.00 10.91 C
ANISOU 546 C ARG A 70 1693 1174 1278 -3 252 -214 C
ATOM 547 O ARG A 70 -14.658 8.807 30.694 1.00 11.63 O
ANISOU 547 O ARG A 70 1595 1238 1584 -190 413 -315 O
ATOM 548 N LEU A 71 -12.732 8.456 29.583 1.00 11.04 N
ANISOU 548 N LEU A 71 1672 1035 1489 34 359 -214 N
ATOM 549 CA LEU A 71 -12.216 9.786 29.723 1.00 10.94 C
ANISOU 549 CA LEU A 71 1751 1079 1327 -5 392 -252 C
ATOM 550 CB LEU A 71 -10.877 9.784 30.474 1.00 11.18 C
ANISOU 550 CB LEU A 71 1717 1071 1457 -50 445 -184 C
ATOM 551 CG LEU A 71 -10.912 9.193 31.877 1.00 12.69 C
ANISOU 551 CG LEU A 71 1975 1359 1486 -25 302 -132 C
ATOM 552 CD1 LEU A 71 -9.497 8.945 32.391 1.00 12.87 C
ANISOU 552 CD1 LEU A 71 2017 1402 1468 -75 91 -134 C
ATOM 553 CD2 LEU A 71 -11.666 10.087 32.819 1.00 12.85 C
ANISOU 553 CD2 LEU A 71 1866 1570 1447 -67 252 -207 C
ATOM 554 C LEU A 71 -12.075 10.381 28.330 1.00 10.94 C
ANISOU 554 C LEU A 71 1712 1045 1396 -50 273 -177 C
ATOM 555 O LEU A 71 -11.431 9.789 27.463 1.00 12.17 O
ANISOU 555 O LEU A 71 2090 1112 1420 -110 385 -296 O
ATOM 556 N ARG A 72 -12.638 11.584 28.171 1.00 10.70 N
ANISOU 556 N ARG A 72 1766 994 1304 -22 269 -264 N
ATOM 557 CA AARG A 72 -12.477 12.368 26.955 0.50 11.51 C
ANISOU 557 CA AARG A 72 1870 1187 1315 -128 311 -196 C
ATOM 558 CA BARG A 72 -12.474 12.366 26.958 0.50 11.40 C
ANISOU 558 CA BARG A 72 1866 1143 1323 -82 304 -207 C
ATOM 559 CB AARG A 72 -13.816 12.930 26.465 0.50 12.77 C
ANISOU 559 CB AARG A 72 1829 1529 1493 -163 272 -105 C
ATOM 560 CB BARG A 72 -13.823 12.908 26.482 0.50 12.82 C
ANISOU 560 CB BARG A 72 1869 1459 1543 -29 268 -155 C
ATOM 561 CG AARG A 72 -13.710 13.784 25.202 0.50 14.52 C
ANISOU 561 CG AARG A 72 1969 2003 1545 -230 295 71 C
ATOM 562 CG BARG A 72 -13.766 13.765 25.224 0.50 14.48 C
ANISOU 562 CG BARG A 72 2036 1856 1607 32 289 -2 C
ATOM 563 CD AARG A 72 -14.789 14.853 25.104 0.50 17.05 C
ANISOU 563 CD AARG A 72 2251 2250 1975 -110 41 165 C
ATOM 564 CD BARG A 72 -15.180 14.258 24.918 0.50 17.31 C
ANISOU 564 CD BARG A 72 2306 2223 2046 260 61 85 C
ATOM 565 NE AARG A 72 -14.885 15.592 23.849 0.50 19.64 N
ANISOU 565 NE AARG A 72 2700 2729 2031 32 139 360 N
ATOM 566 NE BARG A 72 -15.532 15.379 25.811 0.50 19.19 N
ANISOU 566 NE BARG A 72 2651 2399 2241 352 -54 -102 N
ATOM 567 CZ AARG A 72 -14.369 16.796 23.643 0.50 19.32 C
ANISOU 567 CZ AARG A 72 2566 2643 2129 255 -103 345 C
ATOM 568 CZ BARG A 72 -16.765 15.824 26.118 0.50 21.23 C
ANISOU 568 CZ BARG A 72 2859 2709 2499 602 -213 -319 C
ATOM 569 NH1AARG A 72 -13.729 17.407 24.618 0.50 22.23 N
ANISOU 569 NH1AARG A 72 2708 2884 2852 137 -75 -260 N
ATOM 570 NH1BARG A 72 -17.885 15.255 25.663 0.50 21.71 N
ANISOU 570 NH1BARG A 72 4076 2043 2129 607 -1256 -540 N
ATOM 571 NH2AARG A 72 -14.485 17.395 22.472 0.50 22.76 N
ANISOU 571 NH2AARG A 72 2961 3191 2494 705 552 885 N
ATOM 572 NH2BARG A 72 -16.853 16.894 26.874 0.50 21.60 N
ANISOU 572 NH2BARG A 72 3074 2882 2249 439 -144 -354 N
ATOM 573 C ARG A 72 -11.490 13.497 27.265 1.00 11.08 C
ANISOU 573 C ARG A 72 1875 1078 1254 -42 183 -238 C
ATOM 574 O ARG A 72 -11.787 14.362 28.098 1.00 12.17 O
ANISOU 574 O ARG A 72 2022 1051 1548 40 387 -289 O
ATOM 575 N VAL A 73 -10.342 13.478 26.596 1.00 11.51 N
ANISOU 575 N VAL A 73 2048 1043 1283 -112 234 -328 N
ATOM 576 CA VAL A 73 -9.329 14.526 26.742 1.00 12.46 C
ANISOU 576 CA VAL A 73 2081 1214 1437 -165 177 -293 C
ATOM 577 CB VAL A 73 -7.946 13.976 27.108 1.00 15.41 C
ANISOU 577 CB VAL A 73 2224 1884 1745 -71 140 27 C
ATOM 578 CG1 VAL A 73 -7.983 13.283 28.461 1.00 15.89 C
ANISOU 578 CG1 VAL A 73 2245 1910 1879 287 254 197 C
ATOM 579 CG2 VAL A 73 -7.378 13.101 26.031 1.00 16.99 C
ANISOU 579 CG2 VAL A 73 2507 1882 2064 50 83 -64 C
ATOM 580 C VAL A 73 -9.256 15.328 25.455 1.00 12.36 C
ANISOU 580 C VAL A 73 2108 1144 1444 -218 239 -306 C
ATOM 581 O VAL A 73 -9.434 14.784 24.358 1.00 13.84 O
ANISOU 581 O VAL A 73 2439 1313 1506 -494 116 -315 O
ATOM 582 N SER A 74 -9.025 16.628 25.619 1.00 12.04 N
ANISOU 582 N SER A 74 2103 1190 1279 -353 141 -325 N
ATOM 583 CA SER A 74 -8.752 17.483 24.483 1.00 12.41 C
ANISOU 583 CA SER A 74 2286 1092 1337 -360 295 -333 C
ATOM 584 CB SER A 74 -9.958 18.251 24.026 1.00 15.25 C
ANISOU 584 CB SER A 74 2258 1841 1693 -448 20 -222 C
ATOM 585 OG SER A 74 -10.374 19.163 25.017 1.00 18.30 O
ANISOU 585 OG SER A 74 2696 2428 1826 -13 91 -260 O
ATOM 586 C SER A 74 -7.601 18.409 24.849 1.00 12.64 C
ANISOU 586 C SER A 74 2369 1147 1286 -437 440 -330 C
ATOM 587 O SER A 74 -7.455 18.788 26.013 1.00 14.69 O
ANISOU 587 O SER A 74 2541 1634 1406 -597 388 -491 O
ATOM 588 N PHE A 75 -6.770 18.735 23.849 1.00 11.81 N
ANISOU 588 N PHE A 75 1979 1166 1341 -386 366 -258 N
ATOM 589 CA PHE A 75 -5.631 19.575 24.093 1.00 12.97 C
ANISOU 589 CA PHE A 75 2117 1303 1505 -452 254 -165 C
ATOM 590 CB PHE A 75 -4.575 18.870 24.944 1.00 13.09 C
ANISOU 590 CB PHE A 75 2200 1347 1423 -441 128 -165 C
ATOM 591 CG PHE A 75 -4.080 17.583 24.351 1.00 13.52 C
ANISOU 591 CG PHE A 75 2224 1586 1324 -252 111 -204 C
ATOM 592 CD1 PHE A 75 -3.027 17.564 23.460 1.00 13.69 C
ANISOU 592 CD1 PHE A 75 1967 1684 1549 -184 81 -268 C
ATOM 593 CE1 PHE A 75 -2.610 16.371 22.897 1.00 13.62 C
ANISOU 593 CE1 PHE A 75 2124 1735 1314 -116 68 -210 C
ATOM 594 CZ PHE A 75 -3.236 15.182 23.196 1.00 13.62 C
ANISOU 594 CZ PHE A 75 1923 1748 1503 -81 15 -186 C
ATOM 595 CD2 PHE A 75 -4.712 16.387 24.646 1.00 13.62 C
ANISOU 595 CD2 PHE A 75 2141 1587 1447 -225 232 -121 C
ATOM 596 CE2 PHE A 75 -4.304 15.194 24.055 1.00 13.63 C
ANISOU 596 CE2 PHE A 75 2253 1440 1483 -271 246 -98 C
ATOM 597 C PHE A 75 -5.039 19.982 22.751 1.00 12.59 C
ANISOU 597 C PHE A 75 2001 1342 1441 -397 217 -153 C
ATOM 598 O PHE A 75 -5.357 19.404 21.711 1.00 13.54 O
ANISOU 598 O PHE A 75 2000 1622 1522 -477 245 -325 O
ATOM 599 N THR A 76 -4.165 20.975 22.821 1.00 13.01 N
ANISOU 599 N THR A 76 2001 1344 1598 -439 164 -311 N
ATOM 600 CA THR A 76 -3.332 21.368 21.699 1.00 13.51 C
ANISOU 600 CA THR A 76 2032 1511 1589 -474 170 -171 C
ATOM 601 CB THR A 76 -3.501 22.863 21.400 1.00 15.14 C
ANISOU 601 CB THR A 76 2333 1498 1917 -314 230 -265 C
ATOM 602 OG1 THR A 76 -4.868 23.125 21.073 1.00 16.12 O
ANISOU 602 OG1 THR A 76 2473 1802 1849 -239 314 -113 O
ATOM 603 CG2 THR A 76 -2.613 23.328 20.273 1.00 15.91 C
ANISOU 603 CG2 THR A 76 2497 1435 2112 -319 165 102 C
ATOM 604 C THR A 76 -1.880 21.017 22.035 1.00 14.16 C
ANISOU 604 C THR A 76 2129 1638 1609 -419 261 -232 C
ATOM 605 O THR A 76 -1.403 21.334 23.138 1.00 14.45 O
ANISOU 605 O THR A 76 1839 1964 1684 -307 212 -380 O
ATOM 606 N ALA A 77 -1.198 20.355 21.085 1.00 12.76 N
ANISOU 606 N ALA A 77 1937 1346 1564 -599 229 -261 N
ATOM 607 CA ALA A 77 0.229 20.097 21.178 1.00 13.86 C
ANISOU 607 CA ALA A 77 2079 1531 1655 -536 415 -438 C
ATOM 608 CB ALA A 77 0.540 18.661 20.920 1.00 14.58 C
ANISOU 608 CB ALA A 77 2276 1458 1804 -461 598 -192 C
ATOM 609 C ALA A 77 0.950 20.982 20.173 1.00 13.76 C
ANISOU 609 C ALA A 77 1978 1708 1541 -494 306 -315 C
ATOM 610 O ALA A 77 0.581 21.019 19.009 1.00 14.80 O
ANISOU 610 O ALA A 77 2228 1755 1640 -523 72 -237 O
ATOM 611 N GLU A 78 1.985 21.677 20.649 1.00 13.88 N
ANISOU 611 N GLU A 78 2126 1675 1470 -674 379 -260 N
ATOM 612 CA GLU A 78 2.877 22.432 19.790 1.00 13.89 C
ANISOU 612 CA GLU A 78 2079 1615 1581 -620 360 -164 C
ATOM 613 CB GLU A 78 3.060 23.872 20.279 1.00 16.13 C
ANISOU 613 CB GLU A 78 2485 1597 2044 -551 568 -312 C
ATOM 614 CG GLU A 78 3.974 24.670 19.377 1.00 18.89 C
ANISOU 614 CG GLU A 78 2873 2075 2226 -705 657 -85 C
ATOM 615 CD GLU A 78 4.149 26.147 19.671 1.00 21.34 C
ANISOU 615 CD GLU A 78 3339 2129 2641 -907 713 -60 C
ATOM 616 OE1 GLU A 78 3.730 26.610 20.739 1.00 23.40 O
ANISOU 616 OE1 GLU A 78 3643 1948 3299 -608 1051 -470 O
ATOM 617 OE2 GLU A 78 4.731 26.835 18.802 1.00 28.40 O
ANISOU 617 OE2 GLU A 78 4594 2828 3366 -1508 1180 226 O
ATOM 618 C GLU A 78 4.208 21.703 19.749 1.00 14.59 C
ANISOU 618 C GLU A 78 2190 1824 1527 -552 246 -260 C
ATOM 619 O GLU A 78 4.829 21.502 20.811 1.00 15.60 O
ANISOU 619 O GLU A 78 2193 2164 1568 -370 176 -200 O
ATOM 620 N ILE A 79 4.603 21.287 18.545 1.00 14.50 N
ANISOU 620 N ILE A 79 2065 1925 1517 -520 285 -177 N
ATOM 621 CA ILE A 79 5.826 20.551 18.298 1.00 14.87 C
ANISOU 621 CA ILE A 79 1993 1820 1836 -532 261 -219 C
ATOM 622 CB ILE A 79 5.570 19.329 17.398 1.00 15.50 C
ANISOU 622 CB ILE A 79 2401 1857 1631 -584 155 -132 C
ATOM 623 CG1 ILE A 79 4.483 18.415 17.990 1.00 15.76 C
ANISOU 623 CG1 ILE A 79 2479 1663 1846 -627 149 -143 C
ATOM 624 CG2 ILE A 79 6.879 18.589 17.161 1.00 15.44 C
ANISOU 624 CG2 ILE A 79 2618 1652 1596 -415 21 -224 C
ATOM 625 CD1 ILE A 79 4.066 17.297 17.071 1.00 17.92 C
ANISOU 625 CD1 ILE A 79 3003 1653 2152 -596 -76 -171 C
ATOM 626 C ILE A 79 6.814 21.510 17.651 1.00 15.04 C
ANISOU 626 C ILE A 79 2140 1892 1683 -418 387 -87 C
ATOM 627 O ILE A 79 6.508 22.060 16.576 1.00 15.01 O
ANISOU 627 O ILE A 79 2144 1634 1924 -620 112 39 O
ATOM 628 N LYS A 80 7.964 21.700 18.306 1.00 16.54 N
ANISOU 628 N LYS A 80 1996 2164 2124 -584 494 -354 N
ATOM 629 CA LYS A 80 9.002 22.619 17.848 1.00 16.68 C
ANISOU 629 CA LYS A 80 2244 1904 2189 -623 541 -491 C
ATOM 630 CB LYS A 80 9.348 23.632 18.938 1.00 20.49 C
ANISOU 630 CB LYS A 80 2630 2537 2615 -715 412 -947 C
ATOM 631 CG LYS A 80 8.194 24.495 19.402 1.00 23.26 C
ANISOU 631 CG LYS A 80 2823 2795 3218 -477 327 -1064 C
ATOM 632 CD LYS A 80 8.560 25.327 20.604 1.00 30.68 C
ANISOU 632 CD LYS A 80 3866 3777 4011 -607 81 -1822 C
ATOM 633 CE LYS A 80 7.405 26.149 21.119 1.00 35.79 C
ANISOU 633 CE LYS A 80 4647 3983 4967 -387 42 -2337 C
ATOM 634 NZ LYS A 80 7.798 26.942 22.301 1.00 45.06 N
ANISOU 634 NZ LYS A 80 5748 6197 5172 -837 -917 -2599 N
ATOM 635 C LYS A 80 10.276 21.845 17.471 1.00 16.88 C
ANISOU 635 C LYS A 80 2006 2072 2335 -593 320 -558 C
ATOM 636 O LYS A 80 10.452 20.691 17.866 1.00 17.57 O
ANISOU 636 O LYS A 80 2108 2071 2494 -593 288 -393 O
ATOM 637 N ASN A 81 11.155 22.527 16.717 1.00 17.76 N
ANISOU 637 N ASN A 81 2246 1974 2527 -627 329 -417 N
ATOM 638 CA ASN A 81 12.482 22.057 16.282 1.00 20.18 C
ANISOU 638 CA ASN A 81 2430 2524 2709 -615 499 -524 C
ATOM 639 CB ASN A 81 13.262 21.318 17.374 1.00 19.65 C
ANISOU 639 CB ASN A 81 2077 2684 2702 -503 348 -660 C
ATOM 640 CG ASN A 81 13.483 22.140 18.626 1.00 21.75 C
ANISOU 640 CG ASN A 81 2689 2756 2816 -661 237 -729 C
ATOM 641 OD1 ASN A 81 13.421 23.369 18.587 1.00 23.49 O
ANISOU 641 OD1 ASN A 81 2591 2754 3578 -684 256 -1151 O
ATOM 642 ND2 ASN A 81 13.747 21.462 19.735 1.00 23.42 N
ANISOU 642 ND2 ASN A 81 2449 3641 2808 -484 163 -573 N
ATOM 643 C ASN A 81 12.389 21.168 15.035 1.00 18.67 C
ANISOU 643 C ASN A 81 2077 2428 2587 -711 527 -394 C
ATOM 644 O ASN A 81 13.324 20.402 14.766 1.00 20.30 O
ANISOU 644 O ASN A 81 2260 2469 2981 -477 514 -545 O
ATOM 645 N ILE A 82 11.320 21.327 14.248 1.00 18.06 N
ANISOU 645 N ILE A 82 2235 2314 2312 -608 501 -391 N
ATOM 646 CA ILE A 82 11.139 20.588 12.990 1.00 17.42 C
ANISOU 646 CA ILE A 82 2215 2008 2397 -682 498 -311 C
ATOM 647 CB ILE A 82 9.640 20.457 12.660 1.00 17.08 C
ANISOU 647 CB ILE A 82 2141 2084 2265 -676 440 -127 C
ATOM 648 CG1 ILE A 82 8.855 19.809 13.801 1.00 18.51 C
ANISOU 648 CG1 ILE A 82 2145 2484 2401 -678 517 42 C
ATOM 649 CG2 ILE A 82 9.437 19.733 11.343 1.00 17.42 C
ANISOU 649 CG2 ILE A 82 2472 1857 2289 -663 509 -139 C
ATOM 650 CD1 ILE A 82 7.349 19.860 13.648 1.00 17.73 C
ANISOU 650 CD1 ILE A 82 2100 2617 2020 -593 655 -57 C
ATOM 651 C ILE A 82 11.855 21.343 11.862 1.00 17.74 C
ANISOU 651 C ILE A 82 2138 2056 2545 -663 626 -282 C
ATOM 652 O ILE A 82 11.631 22.522 11.650 1.00 19.65 O
ANISOU 652 O ILE A 82 2517 1995 2953 -696 783 -321 O
ATOM 653 N LEU A 83 12.718 20.643 11.124 1.00 18.09 N
ANISOU 653 N LEU A 83 2214 1934 2723 -764 794 -309 N
ATOM 654 CA LEU A 83 13.422 21.258 10.008 1.00 19.73 C
ANISOU 654 CA LEU A 83 2686 2093 2717 -983 839 -238 C
ATOM 655 CB LEU A 83 14.192 20.196 9.212 1.00 21.86 C
ANISOU 655 CB LEU A 83 2825 2665 2814 -801 864 -366 C
ATOM 656 CG LEU A 83 15.078 20.728 8.084 1.00 23.32 C
ANISOU 656 CG LEU A 83 3064 2872 2922 -767 945 -187 C
ATOM 657 CD1 LEU A 83 16.239 21.520 8.634 1.00 25.64 C
ANISOU 657 CD1 LEU A 83 2946 3426 3370 -900 940 -75 C
ATOM 658 CD2 LEU A 83 15.602 19.566 7.262 1.00 23.45 C
ANISOU 658 CD2 LEU A 83 2798 3059 3052 -782 1036 -272 C
ATOM 659 C LEU A 83 12.422 21.996 9.108 1.00 19.64 C
ANISOU 659 C LEU A 83 2680 1906 2875 -889 881 -87 C
ATOM 660 O LEU A 83 11.376 21.467 8.778 1.00 20.38 O
ANISOU 660 O LEU A 83 2909 2117 2717 -872 690 42 O
ATOM 661 N ALA A 84 12.787 23.211 8.671 1.00 21.63 N
ANISOU 661 N ALA A 84 2645 2414 3158 -1068 1011 438 N
ATOM 662 CA ALA A 84 11.919 23.988 7.808 1.00 23.70 C
ANISOU 662 CA ALA A 84 3777 1925 3300 -850 979 323 C
ATOM 663 CB ALA A 84 12.558 25.320 7.501 1.00 24.38 C
ANISOU 663 CB ALA A 84 3377 2222 3663 -1010 1118 347 C
ATOM 664 C ALA A 84 11.625 23.192 6.527 1.00 24.89 C
ANISOU 664 C ALA A 84 4144 2097 3215 -1225 868 459 C
ATOM 665 O ALA A 84 12.467 22.431 6.075 1.00 27.25 O
ANISOU 665 O ALA A 84 3977 2883 3494 -1202 763 -84 O
ATOM 666 N ASP A 85 10.413 23.379 5.991 1.00 27.17 N
ANISOU 666 N ASP A 85 4323 2328 3671 -1020 734 247 N
ATOM 667 CA AASP A 85 9.940 22.773 4.727 0.50 28.45 C
ANISOU 667 CA AASP A 85 4467 2845 3494 -992 736 350 C
ATOM 668 CA BASP A 85 9.939 22.774 4.730 0.50 27.78 C
ANISOU 668 CA BASP A 85 4336 2808 3409 -868 782 422 C
ATOM 669 CB AASP A 85 10.889 23.043 3.550 0.50 30.58 C
ANISOU 669 CB AASP A 85 4672 3409 3538 -771 828 505 C
ATOM 670 CB BASP A 85 10.889 23.058 3.559 0.50 28.98 C
ANISOU 670 CB BASP A 85 4387 3221 3403 -509 796 716 C
ATOM 671 CG AASP A 85 10.251 22.789 2.190 0.50 34.26 C
ANISOU 671 CG AASP A 85 4955 4207 3854 -603 624 463 C
ATOM 672 CG BASP A 85 11.154 24.536 3.331 0.50 30.70 C
ANISOU 672 CG BASP A 85 4614 3200 3848 -181 914 939 C
ATOM 673 OD1AASP A 85 9.130 23.289 1.971 0.50 35.82 O
ANISOU 673 OD1AASP A 85 5083 4537 3990 -628 101 685 O
ATOM 674 OD1BASP A 85 10.215 25.334 3.512 0.50 35.23 O
ANISOU 674 OD1BASP A 85 4596 4567 4220 552 886 1246 O
ATOM 675 OD2AASP A 85 10.866 22.074 1.363 0.50 40.66 O
ANISOU 675 OD2AASP A 85 6297 5007 4142 -155 459 -1 O
ATOM 676 OD2BASP A 85 12.304 24.877 2.986 0.50 34.55 O
ANISOU 676 OD2BASP A 85 4618 3870 4638 -316 895 1051 O
ATOM 677 C ASP A 85 9.718 21.265 4.904 1.00 26.37 C
ANISOU 677 C ASP A 85 4648 2774 2594 -1012 931 228 C
ATOM 678 O ASP A 85 9.738 20.527 3.936 1.00 30.04 O
ANISOU 678 O ASP A 85 5620 2991 2800 -1364 910 3 O
ATOM 679 N SER A 86 9.477 20.811 6.144 1.00 22.90 N
ANISOU 679 N SER A 86 4078 2057 2563 -945 663 266 N
ATOM 680 CA SER A 86 9.148 19.401 6.388 1.00 21.47 C
ANISOU 680 CA SER A 86 3426 2023 2709 -1046 502 32 C
ATOM 681 CB SER A 86 9.414 18.983 7.811 1.00 20.75 C
ANISOU 681 CB SER A 86 3226 1846 2811 -979 432 218 C
ATOM 682 OG SER A 86 10.799 18.955 8.085 1.00 20.96 O
ANISOU 682 OG SER A 86 2929 2228 2805 -602 515 143 O
ATOM 683 C SER A 86 7.679 19.158 6.048 1.00 20.72 C
ANISOU 683 C SER A 86 3536 1936 2401 -961 100 15 C
ATOM 684 O SER A 86 6.800 19.840 6.586 1.00 21.48 O
ANISOU 684 O SER A 86 3155 2217 2787 -965 -36 -81 O
ATOM 685 N SER A 87 7.403 18.145 5.225 1.00 19.53 N
ANISOU 685 N SER A 87 3721 1750 1950 -834 153 225 N
ATOM 686 CA SER A 87 6.009 17.831 4.892 1.00 21.42 C
ANISOU 686 CA SER A 87 3628 2086 2422 -1069 147 46 C
ATOM 687 CB SER A 87 5.914 16.890 3.714 1.00 24.28 C
ANISOU 687 CB SER A 87 4238 2749 2236 -913 0 -201 C
ATOM 688 OG SER A 87 6.066 15.536 4.103 1.00 25.97 O
ANISOU 688 OG SER A 87 4554 2745 2569 -1283 472 -134 O
ATOM 689 C SER A 87 5.233 17.289 6.101 1.00 19.44 C
ANISOU 689 C SER A 87 3383 1893 2108 -619 -53 103 C
ATOM 690 O SER A 87 4.027 17.526 6.234 1.00 20.81 O
ANISOU 690 O SER A 87 3277 1868 2762 -792 -284 380 O
ATOM 691 N LEU A 88 5.932 16.532 6.955 1.00 16.64 N
ANISOU 691 N LEU A 88 2606 1648 2066 -598 189 62 N
ATOM 692 CA LEU A 88 5.363 15.782 8.097 1.00 15.96 C
ANISOU 692 CA LEU A 88 2379 1598 2084 -563 130 80 C
ATOM 693 CB LEU A 88 4.723 16.745 9.102 1.00 16.06 C
ANISOU 693 CB LEU A 88 2111 1652 2336 -480 95 -55 C
ATOM 694 CG LEU A 88 5.672 17.763 9.731 1.00 15.68 C
ANISOU 694 CG LEU A 88 1866 1706 2383 -393 108 -127 C
ATOM 695 CD1 LEU A 88 4.898 18.688 10.676 1.00 17.66 C
ANISOU 695 CD1 LEU A 88 2040 2012 2657 -217 212 -208 C
ATOM 696 CD2 LEU A 88 6.816 17.049 10.466 1.00 16.59 C
ANISOU 696 CD2 LEU A 88 1830 1751 2723 -524 -38 -163 C
ATOM 697 C LEU A 88 4.357 14.710 7.677 1.00 15.99 C
ANISOU 697 C LEU A 88 2328 1579 2166 -427 97 -92 C
ATOM 698 O LEU A 88 3.698 14.138 8.549 1.00 14.99 O
ANISOU 698 O LEU A 88 2157 1598 1941 -329 55 -222 O
ATOM 699 N LYS A 89 4.281 14.369 6.392 1.00 16.86 N
ANISOU 699 N LYS A 89 2646 1570 2188 -794 -130 89 N
ATOM 700 CA ALYS A 89 3.262 13.426 5.947 0.50 16.88 C
ANISOU 700 CA ALYS A 89 2763 1452 2196 -724 -280 179 C
ATOM 701 CA BLYS A 89 3.293 13.410 5.912 0.50 16.83 C
ANISOU 701 CA BLYS A 89 2799 1412 2183 -717 -236 118 C
ATOM 702 CB ALYS A 89 3.260 13.274 4.426 0.50 20.22 C
ANISOU 702 CB ALYS A 89 3482 1942 2257 -547 -305 426 C
ATOM 703 CB BLYS A 89 3.435 13.218 4.398 0.50 20.40 C
ANISOU 703 CB BLYS A 89 3485 1958 2307 -525 -124 163 C
ATOM 704 CG ALYS A 89 2.226 12.294 3.879 0.50 20.79 C
ANISOU 704 CG ALYS A 89 3184 2331 2382 -663 -354 626 C
ATOM 705 CG BLYS A 89 2.537 12.153 3.782 0.50 21.55 C
ANISOU 705 CG BLYS A 89 3430 2352 2406 -725 -140 148 C
ATOM 706 CD ALYS A 89 0.777 12.616 4.225 0.50 22.31 C
ANISOU 706 CD ALYS A 89 3133 2594 2747 -406 -390 740 C
ATOM 707 CD BLYS A 89 2.890 11.756 2.353 0.50 23.81 C
ANISOU 707 CD BLYS A 89 3463 2912 2671 -361 288 163 C
ATOM 708 CE ALYS A 89 -0.234 11.803 3.427 0.50 23.62 C
ANISOU 708 CE ALYS A 89 2800 3170 3002 -213 -597 689 C
ATOM 709 CE BLYS A 89 2.114 10.526 1.925 0.50 24.95 C
ANISOU 709 CE BLYS A 89 3466 3079 2932 -162 -25 -60 C
ATOM 710 NZ ALYS A 89 -0.359 12.291 2.028 0.50 23.45 N
ANISOU 710 NZ ALYS A 89 2387 3382 3139 25 -808 824 N
ATOM 711 NZ BLYS A 89 2.052 10.410 0.460 0.50 26.88 N
ANISOU 711 NZ BLYS A 89 3436 3870 2904 -103 323 267 N
ATOM 712 C LYS A 89 3.481 12.072 6.634 1.00 15.10 C
ANISOU 712 C LYS A 89 2446 1331 1958 -650 -69 63 C
ATOM 713 O LYS A 89 4.574 11.497 6.579 1.00 15.77 O
ANISOU 713 O LYS A 89 2341 2029 1619 -577 202 146 O
ATOM 714 N ASP A 90 2.402 11.566 7.250 1.00 13.54 N
ANISOU 714 N ASP A 90 2203 1120 1822 -434 -98 -232 N
ATOM 715 CA ASP A 90 2.419 10.240 7.872 1.00 12.99 C
ANISOU 715 CA ASP A 90 2040 1258 1637 -387 94 -157 C
ATOM 716 CB ASP A 90 2.554 9.146 6.812 1.00 13.68 C
ANISOU 716 CB ASP A 90 2280 1352 1564 -355 160 -200 C
ATOM 717 CG ASP A 90 1.391 9.093 5.825 1.00 14.44 C
ANISOU 717 CG ASP A 90 2187 1526 1772 -335 144 -283 C
ATOM 718 OD1 ASP A 90 0.260 9.433 6.209 1.00 14.10 O
ANISOU 718 OD1 ASP A 90 2131 1640 1585 -220 115 36 O
ATOM 719 OD2 ASP A 90 1.623 8.694 4.653 1.00 18.57 O
ANISOU 719 OD2 ASP A 90 2766 2462 1828 -266 352 -413 O
ATOM 720 C ASP A 90 3.473 10.120 8.978 1.00 12.10 C
ANISOU 720 C ASP A 90 1757 1181 1657 -253 218 -50 C
ATOM 721 O ASP A 90 3.989 9.019 9.236 1.00 12.33 O
ANISOU 721 O ASP A 90 2052 1206 1426 -212 91 -68 O
ATOM 722 N GLN A 91 3.752 11.214 9.697 1.00 12.28 N
ANISOU 722 N GLN A 91 1799 1265 1601 -217 158 -79 N
ATOM 723 CA GLN A 91 4.835 11.196 10.688 1.00 12.73 C
ANISOU 723 CA GLN A 91 1844 1479 1510 -298 121 -88 C
ATOM 724 CB GLN A 91 5.978 12.094 10.231 1.00 12.91 C
ANISOU 724 CB GLN A 91 1707 1634 1563 -246 267 -155 C
ATOM 725 CG GLN A 91 6.764 11.468 9.092 1.00 13.09 C
ANISOU 725 CG GLN A 91 1876 1341 1757 -200 412 -163 C
ATOM 726 CD GLN A 91 7.813 12.365 8.489 1.00 14.21 C
ANISOU 726 CD GLN A 91 1984 1672 1743 -196 448 49 C
ATOM 727 OE1 GLN A 91 7.545 13.532 8.220 1.00 16.35 O
ANISOU 727 OE1 GLN A 91 2479 1641 2092 -191 255 147 O
ATOM 728 NE2 GLN A 91 9.000 11.813 8.266 1.00 15.27 N
ANISOU 728 NE2 GLN A 91 2113 1699 1987 -53 311 -444 N
ATOM 729 C GLN A 91 4.410 11.600 12.109 1.00 13.03 C
ANISOU 729 C GLN A 91 1864 1484 1604 -212 197 -123 C
ATOM 730 O GLN A 91 5.216 11.413 13.031 1.00 13.45 O
ANISOU 730 O GLN A 91 2041 1610 1458 -166 148 -102 O
ATOM 731 N ILE A 92 3.197 12.118 12.319 1.00 11.63 N
ANISOU 731 N ILE A 92 1727 1353 1338 -213 -43 -99 N
ATOM 732 CA AILE A 92 2.751 12.575 13.643 0.70 13.01 C
ANISOU 732 CA AILE A 92 1934 1479 1529 -128 180 -127 C
ATOM 733 CA BILE A 92 2.762 12.562 13.651 0.30 12.31 C
ANISOU 733 CA BILE A 92 1910 1334 1432 -114 97 -96 C
ATOM 734 CB AILE A 92 2.426 14.080 13.649 0.70 14.49 C
ANISOU 734 CB AILE A 92 2250 1470 1786 -203 179 -322 C
ATOM 735 CB BILE A 92 2.534 14.088 13.707 0.30 12.45 C
ANISOU 735 CB BILE A 92 2018 1321 1391 -133 108 -145 C
ATOM 736 CG1AILE A 92 3.561 14.935 13.082 0.70 17.06 C
ANISOU 736 CG1AILE A 92 2553 1912 2016 -400 317 -281 C
ATOM 737 CG1BILE A 92 3.832 14.834 13.390 0.30 12.42 C
ANISOU 737 CG1BILE A 92 2069 1319 1331 -132 108 -99 C
ATOM 738 CG2AILE A 92 2.029 14.520 15.043 0.70 15.27 C
ANISOU 738 CG2AILE A 92 2384 1579 1839 -265 279 -318 C
ATOM 739 CG2BILE A 92 1.989 14.515 15.056 0.30 12.73 C
ANISOU 739 CG2BILE A 92 2067 1345 1424 -147 144 -151 C
ATOM 740 CD1AILE A 92 4.845 14.848 13.847 0.70 18.29 C
ANISOU 740 CD1AILE A 92 2685 2267 1994 -381 291 -375 C
ATOM 741 CD1BILE A 92 3.672 16.305 13.138 0.30 12.80 C
ANISOU 741 CD1BILE A 92 2198 1321 1343 -77 206 -90 C
ATOM 742 C ILE A 92 1.511 11.779 14.052 1.00 12.78 C
ANISOU 742 C ILE A 92 1993 1351 1511 -139 187 -185 C
ATOM 743 O ILE A 92 0.587 11.587 13.274 1.00 13.33 O
ANISOU 743 O ILE A 92 1913 1576 1575 -244 196 -27 O
ATOM 744 N GLY A 93 1.467 11.382 15.320 1.00 12.04 N
ANISOU 744 N GLY A 93 1693 1364 1518 -254 62 -79 N
ATOM 745 CA GLY A 93 0.260 10.819 15.878 1.00 11.96 C
ANISOU 745 CA GLY A 93 1692 1500 1352 -318 75 -240 C
ATOM 746 C GLY A 93 0.358 10.720 17.366 1.00 11.53 C
ANISOU 746 C GLY A 93 1599 1416 1366 -271 170 -213 C
ATOM 747 O GLY A 93 1.053 11.523 18.002 1.00 11.53 O
ANISOU 747 O GLY A 93 1676 1238 1466 -230 100 -231 O
ATOM 748 N LEU A 94 -0.343 9.737 17.912 1.00 11.14 N
ANISOU 748 N LEU A 94 1635 1169 1427 -249 131 -265 N
ATOM 749 CA LEU A 94 -0.325 9.503 19.364 1.00 11.26 C
ANISOU 749 CA LEU A 94 1705 1140 1433 -13 208 -286 C
ATOM 750 CB LEU A 94 -1.744 9.611 19.935 1.00 11.58 C
ANISOU 750 CB LEU A 94 1716 1249 1432 58 188 -273 C
ATOM 751 CG LEU A 94 -2.436 10.953 19.752 1.00 11.93 C
ANISOU 751 CG LEU A 94 1785 1240 1507 23 207 -131 C
ATOM 752 CD1 LEU A 94 -3.848 10.890 20.285 1.00 12.64 C
ANISOU 752 CD1 LEU A 94 1853 1344 1602 230 318 -62 C
ATOM 753 CD2 LEU A 94 -1.676 12.093 20.407 1.00 12.27 C
ANISOU 753 CD2 LEU A 94 1895 1249 1517 47 83 -120 C
ATOM 754 C LEU A 94 0.283 8.124 19.646 1.00 10.55 C
ANISOU 754 C LEU A 94 1645 1011 1352 -87 146 -268 C
ATOM 755 O LEU A 94 0.226 7.191 18.820 1.00 11.39 O
ANISOU 755 O LEU A 94 1858 958 1509 -150 59 -309 O
ATOM 756 N LYS A 95 0.858 7.997 20.834 1.00 10.95 N
ANISOU 756 N LYS A 95 1463 1226 1469 -189 67 -348 N
ATOM 757 CA LYS A 95 1.314 6.696 21.341 1.00 11.43 C
ANISOU 757 CA LYS A 95 1633 1272 1438 -166 113 -276 C
ATOM 758 CB LYS A 95 2.217 6.922 22.563 1.00 11.28 C
ANISOU 758 CB LYS A 95 1664 1146 1473 -224 51 -251 C
ATOM 759 CG LYS A 95 3.523 7.620 22.229 1.00 12.31 C
ANISOU 759 CG LYS A 95 1768 1483 1425 -412 32 -253 C
ATOM 760 CD LYS A 95 4.492 7.698 23.387 1.00 13.33 C
ANISOU 760 CD LYS A 95 1931 1660 1474 -386 -52 -96 C
ATOM 761 CE LYS A 95 5.816 8.301 22.978 1.00 13.36 C
ANISOU 761 CE LYS A 95 1874 1585 1617 -361 15 -292 C
ATOM 762 NZ LYS A 95 6.785 8.253 24.080 1.00 14.16 N
ANISOU 762 NZ LYS A 95 1962 1806 1612 -380 34 -339 N
ATOM 763 C LYS A 95 0.107 5.809 21.652 1.00 11.65 C
ANISOU 763 C LYS A 95 1637 1342 1446 -114 115 -165 C
ATOM 764 O LYS A 95 -1.013 6.263 21.728 1.00 12.71 O
ANISOU 764 O LYS A 95 1736 1172 1921 19 224 -105 O
ATOM 765 N SER A 96 0.372 4.514 21.818 1.00 11.08 N
ANISOU 765 N SER A 96 1581 1276 1350 -163 56 -250 N
ATOM 766 CA ASER A 96 -0.683 3.536 22.090 0.60 11.16 C
ANISOU 766 CA ASER A 96 1684 1253 1303 -138 156 -170 C
ATOM 767 CA BSER A 96 -0.695 3.547 22.084 0.40 11.81 C
ANISOU 767 CA BSER A 96 1744 1356 1387 -192 182 -199 C
ATOM 768 CB ASER A 96 -0.112 2.129 22.078 0.60 10.46 C
ANISOU 768 CB ASER A 96 1675 1193 1104 -162 151 -191 C
ATOM 769 CB BSER A 96 -0.173 2.131 22.020 0.40 13.42 C
ANISOU 769 CB BSER A 96 2052 1335 1709 -178 121 -221 C
ATOM 770 OG ASER A 96 0.658 1.871 20.902 0.60 9.59 O
ANISOU 770 OG ASER A 96 1388 1110 1145 27 124 -141 O
ATOM 771 OG BSER A 96 0.598 1.809 23.149 0.40 15.76 O
ANISOU 771 OG BSER A 96 2214 1797 1975 63 18 -199 O
ATOM 772 C SER A 96 -1.332 3.846 23.447 1.00 10.74 C
ANISOU 772 C SER A 96 1572 1200 1307 -117 97 -153 C
ATOM 773 O SER A 96 -0.628 4.033 24.434 1.00 12.18 O
ANISOU 773 O SER A 96 1666 1576 1386 -133 4 -329 O
ATOM 774 N PHE A 97 -2.666 3.845 23.492 1.00 10.49 N
ANISOU 774 N PHE A 97 1554 1334 1094 -82 64 -115 N
ATOM 775 CA PHE A 97 -3.415 4.046 24.747 1.00 9.96 C
ANISOU 775 CA PHE A 97 1515 1196 1072 1 57 -42 C
ATOM 776 CB PHE A 97 -3.331 2.812 25.660 1.00 10.34 C
ANISOU 776 CB PHE A 97 1639 1199 1091 23 -23 18 C
ATOM 777 CG PHE A 97 -3.678 1.553 24.892 1.00 10.58 C
ANISOU 777 CG PHE A 97 1716 1171 1131 48 0 -25 C
ATOM 778 CD1 PHE A 97 -4.990 1.214 24.640 1.00 11.35 C
ANISOU 778 CD1 PHE A 97 1774 1093 1443 -9 86 -53 C
ATOM 779 CE1 PHE A 97 -5.294 0.130 23.826 1.00 11.41 C
ANISOU 779 CE1 PHE A 97 1668 1052 1612 51 -102 -46 C
ATOM 780 CZ PHE A 97 -4.295 -0.649 23.316 1.00 12.28 C
ANISOU 780 CZ PHE A 97 1847 1155 1664 102 -97 -180 C
ATOM 781 CD2 PHE A 97 -2.680 0.763 24.336 1.00 10.59 C
ANISOU 781 CD2 PHE A 97 1652 1073 1297 81 -79 66 C
ATOM 782 CE2 PHE A 97 -2.997 -0.322 23.543 1.00 11.35 C
ANISOU 782 CE2 PHE A 97 1773 1098 1440 141 13 19 C
ATOM 783 C PHE A 97 -2.931 5.315 25.452 1.00 10.64 C
ANISOU 783 C PHE A 97 1535 1192 1314 -59 12 -59 C
ATOM 784 O PHE A 97 -2.501 5.285 26.610 1.00 10.90 O
ANISOU 784 O PHE A 97 1590 1246 1303 108 -8 -49 O
ATOM 785 N PRO A 98 -3.002 6.482 24.783 1.00 10.18 N
ANISOU 785 N PRO A 98 1604 1144 1120 -86 -58 -142 N
ATOM 786 CA PRO A 98 -2.371 7.695 25.306 1.00 10.08 C
ANISOU 786 CA PRO A 98 1305 1223 1302 -109 -76 -158 C
ATOM 787 CB PRO A 98 -2.536 8.698 24.169 1.00 11.34 C
ANISOU 787 CB PRO A 98 1639 1255 1412 -45 28 -152 C
ATOM 788 CG PRO A 98 -3.756 8.224 23.436 1.00 10.81 C
ANISOU 788 CG PRO A 98 1792 1099 1215 1 -20 -182 C
ATOM 789 CD PRO A 98 -3.659 6.715 23.485 1.00 10.20 C
ANISOU 789 CD PRO A 98 1678 1054 1143 -68 -98 -221 C
ATOM 790 C PRO A 98 -3.008 8.206 26.612 1.00 10.81 C
ANISOU 790 C PRO A 98 1490 1212 1403 -23 -35 -195 C
ATOM 791 O PRO A 98 -2.317 8.834 27.408 1.00 13.05 O
ANISOU 791 O PRO A 98 1799 1762 1397 -262 10 -384 O
ATOM 792 N VAL A 99 -4.292 7.904 26.848 1.00 10.41 N
ANISOU 792 N VAL A 99 1493 1197 1264 -71 102 -262 N
ATOM 793 CA VAL A 99 -4.930 8.319 28.088 1.00 10.83 C
ANISOU 793 CA VAL A 99 1628 1224 1261 -134 86 -291 C
ATOM 794 CB VAL A 99 -6.466 8.310 27.963 1.00 10.82 C
ANISOU 794 CB VAL A 99 1619 1178 1313 99 128 -147 C
ATOM 795 CG1 VAL A 99 -7.161 8.494 29.302 1.00 12.19 C
ANISOU 795 CG1 VAL A 99 1753 1481 1397 126 154 -244 C
ATOM 796 CG2 VAL A 99 -6.927 9.355 26.951 1.00 11.75 C
ANISOU 796 CG2 VAL A 99 1783 1199 1481 28 -161 -142 C
ATOM 797 C VAL A 99 -4.399 7.482 29.252 1.00 11.11 C
ANISOU 797 C VAL A 99 1580 1290 1350 -160 143 -239 C
ATOM 798 O VAL A 99 -3.970 8.028 30.267 1.00 11.39 O
ANISOU 798 O VAL A 99 1779 1354 1194 -80 180 -245 O
ATOM 799 N ASN A 100 -4.479 6.153 29.151 1.00 9.97 N
ANISOU 799 N ASN A 100 1471 1189 1125 -146 26 -158 N
ATOM 800 CA ASN A 100 -4.034 5.325 30.279 1.00 10.58 C
ANISOU 800 CA ASN A 100 1521 1175 1322 -113 -49 -112 C
ATOM 801 CB ASN A 100 -4.528 3.893 30.122 1.00 11.23 C
ANISOU 801 CB ASN A 100 1627 1231 1406 -198 -69 -100 C
ATOM 802 CG ASN A 100 -6.014 3.781 30.375 1.00 11.22 C
ANISOU 802 CG ASN A 100 1673 1363 1225 -245 33 -316 C
ATOM 803 OD1 ASN A 100 -6.429 3.775 31.545 1.00 11.66 O
ANISOU 803 OD1 ASN A 100 1695 1509 1223 -153 64 -272 O
ATOM 804 ND2 ASN A 100 -6.810 3.692 29.312 1.00 11.50 N
ANISOU 804 ND2 ASN A 100 1635 1422 1313 -19 -16 -92 N
ATOM 805 C ASN A 100 -2.514 5.444 30.483 1.00 10.41 C
ANISOU 805 C ASN A 100 1568 1204 1181 -268 23 -199 C
ATOM 806 O ASN A 100 -2.047 5.352 31.628 1.00 11.36 O
ANISOU 806 O ASN A 100 1623 1537 1155 -77 -2 -174 O
ATOM 807 N ARG A 101 -1.744 5.649 29.401 1.00 10.67 N
ANISOU 807 N ARG A 101 1469 1453 1129 -167 49 -168 N
ATOM 808 CA ARG A 101 -0.292 5.875 29.543 1.00 11.55 C
ANISOU 808 CA ARG A 101 1519 1479 1390 -276 19 -237 C
ATOM 809 CB ARG A 101 0.379 6.131 28.187 1.00 12.48 C
ANISOU 809 CB ARG A 101 1731 1629 1382 -294 56 -119 C
ATOM 810 CG ARG A 101 0.763 4.914 27.360 1.00 13.23 C
ANISOU 810 CG ARG A 101 1787 1719 1519 -368 -234 -207 C
ATOM 811 CD ARG A 101 1.543 5.301 26.094 1.00 15.80 C
ANISOU 811 CD ARG A 101 1924 2138 1941 -248 76 -39 C
ATOM 812 NE ARG A 101 2.728 6.106 26.341 1.00 16.79 N
ANISOU 812 NE ARG A 101 2074 2133 2172 -104 131 -356 N
ATOM 813 CZ ARG A 101 3.967 5.667 26.582 1.00 20.03 C
ANISOU 813 CZ ARG A 101 2282 2365 2962 -139 -168 29 C
ATOM 814 NH1 ARG A 101 4.215 4.372 26.604 1.00 19.88 N
ANISOU 814 NH1 ARG A 101 2322 2277 2954 403 303 84 N
ATOM 815 NH2 ARG A 101 4.956 6.551 26.755 1.00 21.82 N
ANISOU 815 NH2 ARG A 101 2319 2461 3509 -339 -13 99 N
ATOM 816 C ARG A 101 0.002 7.098 30.429 1.00 12.21 C
ANISOU 816 C ARG A 101 1792 1465 1380 -171 88 -282 C
ATOM 817 O ARG A 101 1.100 7.216 30.980 1.00 13.34 O
ANISOU 817 O ARG A 101 1884 1508 1676 -6 -85 -239 O
ATOM 818 N SER A 102 -0.951 8.032 30.478 1.00 11.30 N
ANISOU 818 N SER A 102 1675 1284 1333 -267 -66 -216 N
ATOM 819 CA SER A 102 -0.797 9.326 31.166 1.00 11.64 C
ANISOU 819 CA SER A 102 1883 1270 1268 -271 97 -246 C
ATOM 820 CB SER A 102 -1.532 10.395 30.404 1.00 11.03 C
ANISOU 820 CB SER A 102 1660 1178 1351 -330 137 -289 C
ATOM 821 OG SER A 102 -0.963 10.604 29.119 1.00 11.89 O
ANISOU 821 OG SER A 102 1920 1334 1263 -213 143 -219 O
ATOM 822 C SER A 102 -1.266 9.309 32.625 1.00 11.99 C
ANISOU 822 C SER A 102 1912 1292 1350 -171 150 -279 C
ATOM 823 O SER A 102 -1.267 10.354 33.264 1.00 13.20 O
ANISOU 823 O SER A 102 2137 1527 1348 -376 87 -496 O
ATOM 824 N ILE A 103 -1.650 8.139 33.155 1.00 11.11 N
ANISOU 824 N ILE A 103 1834 1151 1236 -189 62 -403 N
ATOM 825 CA ILE A 103 -2.221 8.064 34.506 1.00 12.13 C
ANISOU 825 CA ILE A 103 2071 1305 1232 -84 83 -383 C
ATOM 826 CB ILE A 103 -3.721 7.738 34.507 1.00 12.79 C
ANISOU 826 CB ILE A 103 2039 1472 1348 -44 40 -294 C
ATOM 827 CG1 ILE A 103 -4.520 8.696 33.621 1.00 13.17 C
ANISOU 827 CG1 ILE A 103 2211 1437 1354 -127 -90 -235 C
ATOM 828 CG2 ILE A 103 -4.247 7.707 35.929 1.00 13.26 C
ANISOU 828 CG2 ILE A 103 2145 1535 1359 -127 0 -114 C
ATOM 829 CD1 ILE A 103 -5.926 8.221 33.291 1.00 13.84 C
ANISOU 829 CD1 ILE A 103 2135 1598 1525 -89 -8 -188 C
ATOM 830 C ILE A 103 -1.439 7.056 35.326 1.00 11.77 C
ANISOU 830 C ILE A 103 1944 1361 1165 -173 7 -329 C
ATOM 831 O ILE A 103 -1.703 5.856 35.272 1.00 12.17 O
ANISOU 831 O ILE A 103 1898 1330 1393 -103 256 -276 O
ATOM 832 N PRO A 104 -0.416 7.490 36.091 1.00 12.17 N
ANISOU 832 N PRO A 104 1861 1491 1272 -182 0 -289 N
ATOM 833 CA PRO A 104 0.354 6.522 36.855 1.00 13.17 C
ANISOU 833 CA PRO A 104 1907 1513 1583 -154 -60 -206 C
ATOM 834 CB PRO A 104 1.469 7.372 37.478 1.00 15.74 C
ANISOU 834 CB PRO A 104 2302 1831 1846 -304 -411 -175 C
ATOM 835 CG PRO A 104 1.547 8.637 36.684 1.00 17.12 C
ANISOU 835 CG PRO A 104 2551 1884 2067 -141 -261 -249 C
ATOM 836 CD PRO A 104 0.201 8.822 36.045 1.00 14.52 C
ANISOU 836 CD PRO A 104 2230 1561 1725 -182 -25 -358 C
ATOM 837 C PRO A 104 -0.426 5.826 37.972 1.00 13.39 C
ANISOU 837 C PRO A 104 2026 1628 1433 -140 -66 -304 C
ATOM 838 O PRO A 104 -0.126 4.684 38.315 1.00 13.26 O
ANISOU 838 O PRO A 104 2140 1515 1384 -34 -30 -265 O
ATOM 839 N VAL A 105 -1.360 6.547 38.579 1.00 13.04 N
ANISOU 839 N VAL A 105 1880 1702 1371 -277 36 -355 N
ATOM 840 CA AVAL A 105 -2.143 5.993 39.674 0.50 12.89 C
ANISOU 840 CA AVAL A 105 1823 1642 1429 -233 23 -303 C
ATOM 841 CA BVAL A 105 -2.118 6.053 39.728 0.50 13.09 C
ANISOU 841 CA BVAL A 105 1898 1644 1430 -191 73 -281 C
ATOM 842 CB AVAL A 105 -1.467 6.203 41.047 0.50 14.29 C
ANISOU 842 CB AVAL A 105 1793 2096 1538 -264 -81 -236 C
ATOM 843 CB BVAL A 105 -1.492 6.553 41.051 0.50 14.54 C
ANISOU 843 CB BVAL A 105 2038 1990 1495 -304 -1 -270 C
ATOM 844 CG1AVAL A 105 -1.207 7.666 41.372 0.50 15.36 C
ANISOU 844 CG1AVAL A 105 2010 2217 1606 -230 -183 -388 C
ATOM 845 CG1BVAL A 105 -2.174 5.933 42.266 0.50 15.30 C
ANISOU 845 CG1BVAL A 105 2181 2302 1329 -335 -96 -270 C
ATOM 846 CG2AVAL A 105 -2.268 5.535 42.159 0.50 14.56 C
ANISOU 846 CG2AVAL A 105 1855 2150 1524 -433 -107 -309 C
ATOM 847 CG2BVAL A 105 0.023 6.403 41.147 0.50 15.21 C
ANISOU 847 CG2BVAL A 105 2114 2229 1433 -228 127 -272 C
ATOM 848 C VAL A 105 -3.545 6.593 39.606 1.00 12.26 C
ANISOU 848 C VAL A 105 1818 1532 1307 -214 22 -426 C
ATOM 849 O VAL A 105 -3.735 7.771 39.232 1.00 14.35 O
ANISOU 849 O VAL A 105 2138 1621 1692 -112 3 -285 O
ATOM 850 N ALA A 106 -4.521 5.745 39.928 1.00 12.05 N
ANISOU 850 N ALA A 106 1828 1227 1523 4 50 -234 N
ATOM 851 CA ALA A 106 -5.928 6.133 40.002 1.00 12.71 C
ANISOU 851 CA ALA A 106 1781 1623 1422 -11 107 -310 C
ATOM 852 CB ALA A 106 -6.700 5.613 38.805 1.00 14.06 C
ANISOU 852 CB ALA A 106 1881 1934 1527 139 -22 -353 C
ATOM 853 C ALA A 106 -6.514 5.548 41.283 1.00 11.99 C
ANISOU 853 C ALA A 106 1563 1492 1501 -80 203 -336 C
ATOM 854 O ALA A 106 -6.184 4.416 41.673 1.00 13.32 O
ANISOU 854 O ALA A 106 1893 1704 1462 120 269 -262 O
ATOM 855 N VAL A 107 -7.398 6.320 41.911 1.00 11.58 N
ANISOU 855 N VAL A 107 1705 1317 1378 -41 229 -270 N
ATOM 856 CA VAL A 107 -8.185 5.854 43.047 1.00 11.92 C
ANISOU 856 CA VAL A 107 1693 1435 1400 -7 186 -172 C
ATOM 857 CB VAL A 107 -7.833 6.581 44.351 1.00 14.20 C
ANISOU 857 CB VAL A 107 2016 1790 1588 -94 233 -403 C
ATOM 858 CG1 VAL A 107 -8.697 6.070 45.496 1.00 17.11 C
ANISOU 858 CG1 VAL A 107 2661 2434 1404 -156 332 -422 C
ATOM 859 CG2 VAL A 107 -6.343 6.448 44.688 1.00 16.47 C
ANISOU 859 CG2 VAL A 107 2191 2102 1962 -129 -19 -622 C
ATOM 860 C VAL A 107 -9.657 6.043 42.695 1.00 12.52 C
ANISOU 860 C VAL A 107 1741 1567 1448 160 225 -187 C
ATOM 861 O VAL A 107 -10.066 7.128 42.316 1.00 14.70 O
ANISOU 861 O VAL A 107 2006 1506 2071 98 133 52 O
ATOM 862 N ILE A 108 -10.430 4.954 42.780 1.00 12.59 N
ANISOU 862 N ILE A 108 1850 1551 1382 173 94 -197 N
ATOM 863 CA ILE A 108 -11.865 5.018 42.571 1.00 13.04 C
ANISOU 863 CA ILE A 108 1892 1558 1504 20 217 -272 C
ATOM 864 CB ILE A 108 -12.324 4.069 41.447 1.00 12.99 C
ANISOU 864 CB ILE A 108 1959 1508 1466 60 234 -213 C
ATOM 865 CG1 ILE A 108 -11.677 4.501 40.127 1.00 12.75 C
ANISOU 865 CG1 ILE A 108 1834 1406 1604 -22 260 -73 C
ATOM 866 CG2 ILE A 108 -13.850 4.032 41.369 1.00 12.38 C
ANISOU 866 CG2 ILE A 108 2009 1326 1365 47 217 -152 C
ATOM 867 CD1 ILE A 108 -12.028 3.650 38.936 1.00 13.21 C
ANISOU 867 CD1 ILE A 108 1908 1403 1707 -3 285 -200 C
ATOM 868 C ILE A 108 -12.537 4.714 43.905 1.00 12.29 C
ANISOU 868 C ILE A 108 1847 1481 1342 178 187 -337 C
ATOM 869 O ILE A 108 -12.159 3.785 44.591 1.00 13.68 O
ANISOU 869 O ILE A 108 2130 1654 1412 265 190 -221 O
ATOM 870 N ASN A 109 -13.512 5.554 44.270 1.00 12.12 N
ANISOU 870 N ASN A 109 1699 1476 1427 157 204 -185 N
ATOM 871 CA ASN A 109 -14.302 5.421 45.480 1.00 12.21 C
ANISOU 871 CA ASN A 109 1916 1576 1146 134 88 -187 C
ATOM 872 CB ASN A 109 -14.215 6.693 46.337 1.00 13.19 C
ANISOU 872 CB ASN A 109 2067 1774 1170 97 212 -378 C
ATOM 873 CG ASN A 109 -14.981 6.648 47.636 1.00 13.07 C
ANISOU 873 CG ASN A 109 2084 1636 1245 9 215 -470 C
ATOM 874 OD1 ASN A 109 -16.004 5.973 47.733 1.00 14.69 O
ANISOU 874 OD1 ASN A 109 2293 1883 1404 -205 479 -432 O
ATOM 875 ND2 ASN A 109 -14.507 7.413 48.615 1.00 16.73 N
ANISOU 875 ND2 ASN A 109 2755 1859 1740 17 -239 -744 N
ATOM 876 C ASN A 109 -15.739 5.122 45.055 1.00 11.31 C
ANISOU 876 C ASN A 109 1866 1563 868 36 221 -158 C
ATOM 877 O ASN A 109 -16.349 5.936 44.385 1.00 12.31 O
ANISOU 877 O ASN A 109 1783 1404 1489 -30 -7 20 O
ATOM 878 N MET A 110 -16.261 3.959 45.472 1.00 11.80 N
ANISOU 878 N MET A 110 1815 1491 1177 58 195 -176 N
ATOM 879 CA MET A 110 -17.656 3.621 45.328 1.00 11.76 C
ANISOU 879 CA MET A 110 1763 1484 1221 157 259 -204 C
ATOM 880 CB MET A 110 -17.856 2.374 44.457 1.00 12.20 C
ANISOU 880 CB MET A 110 1826 1502 1307 143 263 -227 C
ATOM 881 CG MET A 110 -17.513 2.630 42.998 1.00 12.52 C
ANISOU 881 CG MET A 110 1945 1500 1309 33 204 -290 C
ATOM 882 SD MET A 110 -17.859 1.212 41.969 1.00 13.63 S
ANISOU 882 SD MET A 110 2207 1590 1381 -17 230 -319 S
ATOM 883 CE MET A 110 -17.390 1.908 40.388 1.00 14.80 C
ANISOU 883 CE MET A 110 2218 1957 1446 -99 201 -241 C
ATOM 884 C MET A 110 -18.238 3.405 46.732 1.00 12.22 C
ANISOU 884 C MET A 110 1893 1515 1235 24 243 -251 C
ATOM 885 O MET A 110 -17.832 2.485 47.434 1.00 12.10 O
ANISOU 885 O MET A 110 1831 1627 1138 222 139 -313 O
ATOM 886 N ASN A 111 -19.173 4.279 47.124 1.00 12.21 N
ANISOU 886 N ASN A 111 1753 1587 1296 69 308 -180 N
ATOM 887 CA ASN A 111 -19.871 4.190 48.421 1.00 11.77 C
ANISOU 887 CA ASN A 111 1749 1459 1262 37 263 -284 C
ATOM 888 CB ASN A 111 -20.955 3.102 48.378 1.00 11.74 C
ANISOU 888 CB ASN A 111 1808 1301 1350 63 387 -216 C
ATOM 889 CG ASN A 111 -22.103 3.467 47.467 1.00 12.08 C
ANISOU 889 CG ASN A 111 1745 1353 1489 -6 366 -133 C
ATOM 890 OD1 ASN A 111 -22.190 4.626 47.042 1.00 13.18 O
ANISOU 890 OD1 ASN A 111 2051 1326 1629 -1 390 -56 O
ATOM 891 ND2 ASN A 111 -22.977 2.503 47.180 1.00 12.67 N
ANISOU 891 ND2 ASN A 111 1815 1397 1602 -97 605 -214 N
ATOM 892 C ASN A 111 -18.875 3.960 49.569 1.00 12.82 C
ANISOU 892 C ASN A 111 2009 1550 1311 198 206 -211 C
ATOM 893 O ASN A 111 -19.158 3.187 50.502 1.00 13.80 O
ANISOU 893 O ASN A 111 2490 1379 1372 128 141 -179 O
ATOM 894 N GLY A 112 -17.755 4.688 49.532 1.00 13.10 N
ANISOU 894 N GLY A 112 2034 1660 1281 156 270 -357 N
ATOM 895 CA GLY A 112 -16.790 4.703 50.608 1.00 14.05 C
ANISOU 895 CA GLY A 112 2075 2010 1253 182 207 -348 C
ATOM 896 C GLY A 112 -15.660 3.701 50.499 1.00 14.21 C
ANISOU 896 C GLY A 112 2057 2079 1260 183 34 -304 C
ATOM 897 O GLY A 112 -14.712 3.789 51.274 1.00 18.14 O
ANISOU 897 O GLY A 112 2529 2779 1582 414 -333 -389 O
ATOM 898 N LYS A 113 -15.793 2.728 49.596 1.00 13.30 N
ANISOU 898 N LYS A 113 1889 1690 1475 169 190 -227 N
ATOM 899 CA LYS A 113 -14.743 1.758 49.336 1.00 13.28 C
ANISOU 899 CA LYS A 113 1906 1713 1424 247 229 71 C
ATOM 900 CB LYS A 113 -15.338 0.428 48.879 1.00 14.03 C
ANISOU 900 CB LYS A 113 2157 1714 1457 251 116 156 C
ATOM 901 CG LYS A 113 -14.326 -0.587 48.386 1.00 16.15 C
ANISOU 901 CG LYS A 113 2359 1800 1975 319 264 91 C
ATOM 902 CD LYS A 113 -13.407 -1.074 49.479 1.00 18.10 C
ANISOU 902 CD LYS A 113 2448 2312 2114 235 88 91 C
ATOM 903 CE LYS A 113 -12.460 -2.130 48.963 1.00 21.79 C
ANISOU 903 CE LYS A 113 2854 2103 3319 303 99 -14 C
ATOM 904 NZ LYS A 113 -11.460 -2.534 49.971 1.00 26.17 N
ANISOU 904 NZ LYS A 113 3093 2557 4292 311 -210 549 N
ATOM 905 C LYS A 113 -13.800 2.310 48.264 1.00 14.01 C
ANISOU 905 C LYS A 113 2061 1805 1455 141 265 -25 C
ATOM 906 O LYS A 113 -14.234 2.639 47.178 1.00 14.88 O
ANISOU 906 O LYS A 113 2168 1917 1566 268 85 -137 O
ATOM 907 N THR A 114 -12.507 2.360 48.585 1.00 14.16 N
ANISOU 907 N THR A 114 2092 1960 1325 284 84 -197 N
ATOM 908 CA THR A 114 -11.510 2.805 47.626 1.00 13.87 C
ANISOU 908 CA THR A 114 1959 1952 1357 343 60 -50 C
ATOM 909 CB THR A 114 -10.511 3.779 48.224 1.00 15.38 C
ANISOU 909 CB THR A 114 2269 2050 1523 278 72 -294 C
ATOM 910 OG1 THR A 114 -9.741 3.086 49.205 1.00 18.89 O
ANISOU 910 OG1 THR A 114 2609 2652 1913 319 -337 -116 O
ATOM 911 CG2 THR A 114 -11.215 4.981 48.813 1.00 17.91 C
ANISOU 911 CG2 THR A 114 2548 2221 2033 197 232 -636 C
ATOM 912 C THR A 114 -10.784 1.623 46.973 1.00 14.50 C
ANISOU 912 C THR A 114 2199 1965 1343 383 127 -106 C
ATOM 913 O THR A 114 -10.496 0.597 47.589 1.00 16.88 O
ANISOU 913 O THR A 114 2625 2239 1548 624 283 20 O
ATOM 914 N PHE A 115 -10.487 1.824 45.689 1.00 12.80 N
ANISOU 914 N PHE A 115 1858 1620 1385 388 189 -27 N
ATOM 915 CA PHE A 115 -9.735 0.909 44.860 1.00 13.31 C
ANISOU 915 CA PHE A 115 1818 1680 1556 280 193 -192 C
ATOM 916 CB PHE A 115 -10.591 0.366 43.711 1.00 12.92 C
ANISOU 916 CB PHE A 115 1724 1537 1645 301 97 -82 C
ATOM 917 CG PHE A 115 -11.911 -0.242 44.117 1.00 13.31 C
ANISOU 917 CG PHE A 115 1927 1596 1531 104 209 -75 C
ATOM 918 CD1 PHE A 115 -13.044 0.529 44.247 1.00 14.43 C
ANISOU 918 CD1 PHE A 115 2234 1419 1828 173 287 -194 C
ATOM 919 CE1 PHE A 115 -14.264 -0.019 44.596 1.00 14.53 C
ANISOU 919 CE1 PHE A 115 1998 1674 1848 288 412 -600 C
ATOM 920 CZ PHE A 115 -14.369 -1.354 44.807 1.00 16.40 C
ANISOU 920 CZ PHE A 115 2225 1794 2212 -48 360 -237 C
ATOM 921 CD2 PHE A 115 -12.052 -1.606 44.272 1.00 18.06 C
ANISOU 921 CD2 PHE A 115 2371 1768 2722 170 260 35 C
ATOM 922 CE2 PHE A 115 -13.280 -2.154 44.593 1.00 19.40 C
ANISOU 922 CE2 PHE A 115 2425 1966 2977 105 510 -124 C
ATOM 923 C PHE A 115 -8.567 1.680 44.242 1.00 12.86 C
ANISOU 923 C PHE A 115 1957 1511 1417 286 174 -71 C
ATOM 924 O PHE A 115 -8.808 2.672 43.520 1.00 13.61 O
ANISOU 924 O PHE A 115 2073 1531 1566 327 16 -46 O
ATOM 925 N THR A 116 -7.338 1.277 44.568 1.00 14.01 N
ANISOU 925 N THR A 116 2072 1964 1287 179 -73 -85 N
ATOM 926 CA THR A 116 -6.149 1.939 44.075 1.00 14.13 C
ANISOU 926 CA THR A 116 1963 2041 1362 341 40 -223 C
ATOM 927 CB THR A 116 -5.176 2.245 45.221 1.00 15.26 C
ANISOU 927 CB THR A 116 2054 2358 1383 175 -30 -375 C
ATOM 928 OG1 THR A 116 -5.857 3.073 46.165 1.00 16.03 O
ANISOU 928 OG1 THR A 116 2183 2592 1313 335 -125 -438 O
ATOM 929 CG2 THR A 116 -3.925 2.958 44.749 1.00 16.68 C
ANISOU 929 CG2 THR A 116 1973 2668 1695 164 -161 -312 C
ATOM 930 C THR A 116 -5.498 1.061 43.009 1.00 13.61 C
ANISOU 930 C THR A 116 2200 1674 1297 286 48 -141 C
ATOM 931 O THR A 116 -5.227 -0.100 43.264 1.00 16.08 O
ANISOU 931 O THR A 116 2705 1742 1660 466 327 41 O
ATOM 932 N SER A 117 -5.269 1.627 41.832 1.00 13.11 N
ANISOU 932 N SER A 117 2080 1708 1193 351 131 -320 N
ATOM 933 CA SER A 117 -4.638 0.881 40.764 1.00 12.11 C
ANISOU 933 CA SER A 117 1942 1608 1050 277 166 -181 C
ATOM 934 CB SER A 117 -5.690 0.206 39.919 1.00 15.73 C
ANISOU 934 CB SER A 117 2646 1932 1396 85 60 -496 C
ATOM 935 OG SER A 117 -6.414 1.137 39.195 1.00 17.87 O
ANISOU 935 OG SER A 117 2440 2599 1750 104 -204 -426 O
ATOM 936 C SER A 117 -3.714 1.809 39.964 1.00 12.45 C
ANISOU 936 C SER A 117 1845 1581 1301 113 75 -236 C
ATOM 937 O SER A 117 -3.604 3.004 40.249 1.00 12.98 O
ANISOU 937 O SER A 117 1929 1595 1407 79 -1 -275 O
ATOM 938 N TYR A 118 -3.022 1.223 38.994 1.00 12.43 N
ANISOU 938 N TYR A 118 1869 1593 1260 75 85 -268 N
ATOM 939 CA TYR A 118 -1.895 1.862 38.289 1.00 11.82 C
ANISOU 939 CA TYR A 118 1872 1483 1135 51 36 -205 C
ATOM 940 CB TYR A 118 -0.592 1.232 38.791 1.00 13.37 C
ANISOU 940 CB TYR A 118 2071 1628 1380 146 14 -126 C
ATOM 941 CG TYR A 118 -0.471 1.350 40.291 1.00 15.08 C
ANISOU 941 CG TYR A 118 2201 2128 1398 -47 -124 44 C
ATOM 942 CD1 TYR A 118 -0.077 2.536 40.878 1.00 15.23 C
ANISOU 942 CD1 TYR A 118 2238 2166 1381 131 -260 -36 C
ATOM 943 CE1 TYR A 118 -0.037 2.684 42.254 1.00 16.41 C
ANISOU 943 CE1 TYR A 118 2409 2413 1411 3 -484 -11 C
ATOM 944 CZ TYR A 118 -0.425 1.644 43.071 1.00 17.51 C
ANISOU 944 CZ TYR A 118 2567 2728 1355 109 -208 143 C
ATOM 945 OH TYR A 118 -0.398 1.803 44.431 1.00 22.62 O
ANISOU 945 OH TYR A 118 2959 4188 1447 332 -233 -93 O
ATOM 946 CE2 TYR A 118 -0.845 0.456 42.499 1.00 18.37 C
ANISOU 946 CE2 TYR A 118 2522 2896 1560 -94 6 212 C
ATOM 947 CD2 TYR A 118 -0.868 0.319 41.129 1.00 17.51 C
ANISOU 947 CD2 TYR A 118 2668 2400 1583 -79 -47 212 C
ATOM 948 C TYR A 118 -2.117 1.736 36.784 1.00 11.27 C
ANISOU 948 C TYR A 118 1543 1619 1118 149 106 -335 C
ATOM 949 O TYR A 118 -1.579 0.831 36.148 1.00 12.32 O
ANISOU 949 O TYR A 118 1698 1683 1298 266 143 -349 O
ATOM 950 N PRO A 119 -2.927 2.629 36.170 1.00 11.63 N
ANISOU 950 N PRO A 119 1874 1376 1167 5 8 -290 N
ATOM 951 CA PRO A 119 -3.335 2.432 34.769 1.00 11.98 C
ANISOU 951 CA PRO A 119 1895 1423 1233 -37 0 -200 C
ATOM 952 CB PRO A 119 -4.233 3.644 34.507 1.00 11.20 C
ANISOU 952 CB PRO A 119 1462 1477 1314 -165 -32 -268 C
ATOM 953 CG PRO A 119 -4.824 3.923 35.874 1.00 12.02 C
ANISOU 953 CG PRO A 119 1829 1452 1284 -158 61 -227 C
ATOM 954 CD PRO A 119 -3.676 3.711 36.839 1.00 11.56 C
ANISOU 954 CD PRO A 119 1734 1524 1133 -57 173 -269 C
ATOM 955 C PRO A 119 -2.162 2.340 33.786 1.00 12.15 C
ANISOU 955 C PRO A 119 1864 1444 1307 -95 -43 -157 C
ATOM 956 O PRO A 119 -2.197 1.515 32.894 1.00 13.19 O
ANISOU 956 O PRO A 119 2227 1440 1343 -92 -39 -219 O
ATOM 957 N ALA A 120 -1.153 3.208 33.921 1.00 11.73 N
ANISOU 957 N ALA A 120 1471 1565 1418 -7 -1 -230 N
ATOM 958 CA ALA A 120 -0.046 3.178 32.948 1.00 12.59 C
ANISOU 958 CA ALA A 120 1873 1529 1381 15 189 -267 C
ATOM 959 CB ALA A 120 0.901 4.315 33.209 1.00 14.06 C
ANISOU 959 CB ALA A 120 1868 1719 1755 31 -140 -327 C
ATOM 960 C ALA A 120 0.680 1.825 33.014 1.00 13.36 C
ANISOU 960 C ALA A 120 2037 1584 1454 69 47 -158 C
ATOM 961 O ALA A 120 1.055 1.250 31.969 1.00 14.08 O
ANISOU 961 O ALA A 120 2214 1616 1517 207 91 -143 O
ATOM 962 N GLN A 121 0.886 1.307 34.243 1.00 13.01 N
ANISOU 962 N GLN A 121 2015 1558 1370 384 168 -268 N
ATOM 963 CA GLN A 121 1.537 0.024 34.417 1.00 13.77 C
ANISOU 963 CA GLN A 121 2151 1696 1386 465 88 -215 C
ATOM 964 CB GLN A 121 1.868 -0.145 35.897 1.00 15.69 C
ANISOU 964 CB GLN A 121 2531 2071 1356 405 119 -179 C
ATOM 965 CG GLN A 121 2.498 -1.485 36.268 1.00 17.57 C
ANISOU 965 CG GLN A 121 2768 2156 1750 395 -48 -151 C
ATOM 966 CD GLN A 121 2.694 -1.560 37.762 1.00 18.04 C
ANISOU 966 CD GLN A 121 2572 2553 1726 435 -27 80 C
ATOM 967 OE1 GLN A 121 1.742 -1.770 38.520 1.00 18.99 O
ANISOU 967 OE1 GLN A 121 2760 2741 1714 340 21 -210 O
ATOM 968 NE2 GLN A 121 3.924 -1.343 38.202 1.00 18.98 N
ANISOU 968 NE2 GLN A 121 2426 2674 2109 314 88 -235 N
ATOM 969 C GLN A 121 0.652 -1.095 33.853 1.00 13.58 C
ANISOU 969 C GLN A 121 2373 1664 1123 512 12 -252 C
ATOM 970 O GLN A 121 1.144 -2.031 33.192 1.00 15.18 O
ANISOU 970 O GLN A 121 2701 1524 1542 538 -34 -362 O
ATOM 971 N LEU A 122 -0.652 -1.007 34.116 1.00 13.32 N
ANISOU 971 N LEU A 122 2403 1506 1149 461 28 -402 N
ATOM 972 CA LEU A 122 -1.619 -2.027 33.699 1.00 14.35 C
ANISOU 972 CA LEU A 122 2627 1534 1291 460 -390 -325 C
ATOM 973 CB LEU A 122 -3.017 -1.732 34.250 1.00 17.73 C
ANISOU 973 CB LEU A 122 2890 2142 1704 52 219 -268 C
ATOM 974 CG LEU A 122 -3.759 -2.915 34.875 1.00 25.48 C
ANISOU 974 CG LEU A 122 3700 2823 3158 -73 227 63 C
ATOM 975 CD1 LEU A 122 -4.925 -2.423 35.730 1.00 28.00 C
ANISOU 975 CD1 LEU A 122 4073 4403 2161 -217 417 530 C
ATOM 976 CD2 LEU A 122 -4.200 -3.885 33.792 1.00 27.82 C
ANISOU 976 CD2 LEU A 122 4283 3749 2536 298 378 -293 C
ATOM 977 C LEU A 122 -1.656 -2.093 32.170 1.00 14.10 C
ANISOU 977 C LEU A 122 2615 1475 1264 340 -187 -333 C
ATOM 978 O LEU A 122 -1.590 -3.166 31.588 1.00 14.30 O
ANISOU 978 O LEU A 122 2450 1584 1399 596 -312 -491 O
ATOM 979 N ILE A 123 -1.803 -0.944 31.515 1.00 13.12 N
ANISOU 979 N ILE A 123 2421 1395 1168 148 -142 -360 N
ATOM 980 CA ILE A 123 -2.003 -0.959 30.065 1.00 12.62 C
ANISOU 980 CA ILE A 123 2207 1431 1155 106 -127 -397 C
ATOM 981 CB ILE A 123 -2.559 0.372 29.507 1.00 13.16 C
ANISOU 981 CB ILE A 123 2177 1438 1385 101 -41 -294 C
ATOM 982 CG1 ILE A 123 -3.151 0.216 28.091 1.00 13.78 C
ANISOU 982 CG1 ILE A 123 2344 1426 1462 -34 -103 -203 C
ATOM 983 CG2 ILE A 123 -1.515 1.481 29.536 1.00 13.58 C
ANISOU 983 CG2 ILE A 123 2395 1385 1377 112 -58 -367 C
ATOM 984 CD1 ILE A 123 -4.196 -0.849 27.892 1.00 14.72 C
ANISOU 984 CD1 ILE A 123 2116 1868 1606 -59 -260 -323 C
ATOM 985 C ILE A 123 -0.722 -1.405 29.355 1.00 13.06 C
ANISOU 985 C ILE A 123 2185 1493 1283 28 46 -221 C
ATOM 986 O ILE A 123 -0.806 -2.022 28.288 1.00 12.91 O
ANISOU 986 O ILE A 123 2124 1466 1313 -18 -27 -244 O
ATOM 987 N LYS A 124 0.452 -1.115 29.925 1.00 13.86 N
ANISOU 987 N LYS A 124 2217 1677 1370 294 59 -522 N
ATOM 988 CA LYS A 124 1.699 -1.539 29.266 1.00 14.78 C
ANISOU 988 CA LYS A 124 1874 2066 1672 134 -12 -375 C
ATOM 989 CB LYS A 124 2.938 -1.050 30.028 1.00 17.47 C
ANISOU 989 CB LYS A 124 1813 2514 2310 -54 -53 -434 C
ATOM 990 CG LYS A 124 4.277 -1.387 29.373 1.00 19.39 C
ANISOU 990 CG LYS A 124 2148 2658 2560 230 226 -535 C
ATOM 991 CD LYS A 124 5.492 -0.714 29.994 1.00 21.06 C
ANISOU 991 CD LYS A 124 2102 3072 2826 150 311 -503 C
ATOM 992 CE LYS A 124 6.765 -0.986 29.191 1.00 24.06 C
ANISOU 992 CE LYS A 124 2036 3522 3582 73 524 -289 C
ATOM 993 NZ LYS A 124 7.987 -0.443 29.845 1.00 28.10 N
ANISOU 993 NZ LYS A 124 2509 4146 4022 -432 597 -659 N
ATOM 994 C LYS A 124 1.734 -3.062 29.129 1.00 15.24 C
ANISOU 994 C LYS A 124 2164 2104 1520 553 36 -261 C
ATOM 995 O LYS A 124 2.301 -3.560 28.150 1.00 15.46 O
ANISOU 995 O LYS A 124 2419 1974 1479 543 207 -114 O
ATOM 996 N LEU A 125 1.200 -3.778 30.125 1.00 15.56 N
ANISOU 996 N LEU A 125 2211 2077 1624 552 109 -233 N
ATOM 997 CA LEU A 125 1.099 -5.251 30.061 1.00 16.63 C
ANISOU 997 CA LEU A 125 2666 2029 1623 526 139 80 C
ATOM 998 CB LEU A 125 0.882 -5.854 31.450 1.00 21.73 C
ANISOU 998 CB LEU A 125 3509 3082 1663 624 370 174 C
ATOM 999 CG LEU A 125 2.100 -5.960 32.325 1.00 25.80 C
ANISOU 999 CG LEU A 125 3890 3692 2219 1131 198 335 C
ATOM 1000 CD1 LEU A 125 1.670 -6.535 33.662 1.00 28.55 C
ANISOU 1000 CD1 LEU A 125 4164 4420 2261 1465 368 704 C
ATOM 1001 CD2 LEU A 125 3.155 -6.831 31.659 1.00 28.36 C
ANISOU 1001 CD2 LEU A 125 4152 4265 2358 1488 444 492 C
ATOM 1002 C LEU A 125 -0.100 -5.680 29.212 1.00 15.05 C
ANISOU 1002 C LEU A 125 2596 1345 1774 482 189 43 C
ATOM 1003 O LEU A 125 0.025 -6.551 28.346 1.00 16.31 O
ANISOU 1003 O LEU A 125 2834 1452 1911 580 265 -54 O
ATOM 1004 N HIS A 126 -1.269 -5.099 29.511 1.00 13.12 N
ANISOU 1004 N HIS A 126 2313 1296 1373 164 112 -206 N
ATOM 1005 CA HIS A 126 -2.526 -5.530 28.950 1.00 13.84 C
ANISOU 1005 CA HIS A 126 2336 1406 1514 -69 238 -217 C
ATOM 1006 CB HIS A 126 -3.663 -4.692 29.548 1.00 14.67 C
ANISOU 1006 CB HIS A 126 2644 1403 1523 44 378 -330 C
ATOM 1007 CG HIS A 126 -5.025 -5.096 29.115 1.00 15.81 C
ANISOU 1007 CG HIS A 126 2586 1698 1722 -180 392 -281 C
ATOM 1008 ND1 HIS A 126 -5.563 -6.311 29.485 1.00 17.51 N
ANISOU 1008 ND1 HIS A 126 2703 1910 2038 -411 382 -273 N
ATOM 1009 CE1 HIS A 126 -6.782 -6.423 28.980 1.00 18.18 C
ANISOU 1009 CE1 HIS A 126 2705 2199 2003 -400 450 -457 C
ATOM 1010 NE2 HIS A 126 -7.074 -5.291 28.323 1.00 17.27 N
ANISOU 1010 NE2 HIS A 126 2579 1970 2009 -311 386 -738 N
ATOM 1011 CD2 HIS A 126 -5.984 -4.457 28.390 1.00 15.36 C
ANISOU 1011 CD2 HIS A 126 2712 1350 1774 -237 380 -395 C
ATOM 1012 C HIS A 126 -2.522 -5.448 27.419 1.00 13.35 C
ANISOU 1012 C HIS A 126 2205 1409 1456 -83 324 -468 C
ATOM 1013 O HIS A 126 -3.123 -6.280 26.747 1.00 14.40 O
ANISOU 1013 O HIS A 126 2237 1359 1874 -383 330 -412 O
ATOM 1014 N GLN A 127 -1.848 -4.439 26.867 1.00 12.11 N
ANISOU 1014 N GLN A 127 2046 1332 1220 43 46 -271 N
ATOM 1015 CA GLN A 127 -1.831 -4.248 25.416 1.00 12.21 C
ANISOU 1015 CA GLN A 127 1950 1461 1226 56 29 -301 C
ATOM 1016 CB GLN A 127 -1.088 -2.960 25.060 1.00 12.91 C
ANISOU 1016 CB GLN A 127 1967 1557 1380 -11 -48 -211 C
ATOM 1017 CG GLN A 127 0.425 -3.015 25.312 1.00 13.60 C
ANISOU 1017 CG GLN A 127 1925 1598 1644 -121 -39 -364 C
ATOM 1018 CD GLN A 127 1.119 -1.687 25.120 1.00 14.91 C
ANISOU 1018 CD GLN A 127 2173 1526 1964 -139 -270 -317 C
ATOM 1019 OE1 GLN A 127 0.562 -0.789 24.458 1.00 15.77 O
ANISOU 1019 OE1 GLN A 127 2341 1638 2011 -162 -129 -51 O
ATOM 1020 NE2 GLN A 127 2.319 -1.554 25.710 1.00 15.28 N
ANISOU 1020 NE2 GLN A 127 1914 1977 1913 11 7 -450 N
ATOM 1021 C GLN A 127 -1.241 -5.459 24.686 1.00 12.53 C
ANISOU 1021 C GLN A 127 1820 1472 1466 40 166 -248 C
ATOM 1022 O GLN A 127 -1.523 -5.634 23.519 1.00 13.60 O
ANISOU 1022 O GLN A 127 2156 1414 1596 224 16 -422 O
ATOM 1023 N TYR A 128 -0.415 -6.264 25.368 1.00 12.30 N
ANISOU 1023 N TYR A 128 1831 1409 1430 46 192 -305 N
ATOM 1024 CA TYR A 128 0.264 -7.390 24.719 1.00 13.34 C
ANISOU 1024 CA TYR A 128 2186 1398 1484 134 186 -303 C
ATOM 1025 CB TYR A 128 1.654 -7.618 25.299 1.00 13.25 C
ANISOU 1025 CB TYR A 128 2156 1359 1516 314 177 -322 C
ATOM 1026 CG TYR A 128 2.629 -6.527 24.956 1.00 13.42 C
ANISOU 1026 CG TYR A 128 2015 1741 1342 243 164 -83 C
ATOM 1027 CD1 TYR A 128 3.087 -6.370 23.655 1.00 13.76 C
ANISOU 1027 CD1 TYR A 128 1972 1938 1317 266 135 -190 C
ATOM 1028 CE1 TYR A 128 3.972 -5.365 23.316 1.00 14.49 C
ANISOU 1028 CE1 TYR A 128 2024 2057 1422 335 262 0 C
ATOM 1029 CZ TYR A 128 4.447 -4.509 24.292 1.00 14.79 C
ANISOU 1029 CZ TYR A 128 2189 1994 1434 91 265 -38 C
ATOM 1030 OH TYR A 128 5.334 -3.512 23.990 1.00 17.75 O
ANISOU 1030 OH TYR A 128 2173 2429 2141 -95 35 111 O
ATOM 1031 CE2 TYR A 128 4.000 -4.650 25.597 1.00 14.40 C
ANISOU 1031 CE2 TYR A 128 1959 2117 1392 47 136 28 C
ATOM 1032 CD2 TYR A 128 3.106 -5.657 25.923 1.00 13.78 C
ANISOU 1032 CD2 TYR A 128 2138 1700 1397 161 163 -67 C
ATOM 1033 C TYR A 128 -0.506 -8.702 24.794 1.00 13.99 C
ANISOU 1033 C TYR A 128 2343 1347 1622 228 104 -158 C
ATOM 1034 O TYR A 128 -0.108 -9.641 24.125 1.00 15.65 O
ANISOU 1034 O TYR A 128 2449 1263 2232 342 -55 -338 O
ATOM 1035 N ASN A 129 -1.536 -8.831 25.619 1.00 15.51 N
ANISOU 1035 N ASN A 129 2737 1592 1562 -129 199 -213 N
ATOM 1036 CA ASN A 129 -2.177 -10.157 25.576 1.00 18.01 C
ANISOU 1036 CA ASN A 129 2793 1665 2383 -202 61 156 C
ATOM 1037 CB ASN A 129 -1.593 -11.146 26.583 1.00 19.62 C
ANISOU 1037 CB ASN A 129 3055 2212 2186 63 -20 79 C
ATOM 1038 CG ASN A 129 -2.131 -10.941 27.967 1.00 20.20 C
ANISOU 1038 CG ASN A 129 3348 2142 2185 219 83 250 C
ATOM 1039 OD1 ASN A 129 -2.457 -9.802 28.323 1.00 19.72 O
ANISOU 1039 OD1 ASN A 129 3053 1869 2570 -12 51 150 O
ATOM 1040 ND2 ASN A 129 -2.121 -12.013 28.745 1.00 18.46 N
ANISOU 1040 ND2 ASN A 129 2929 2035 2050 -76 -222 210 N
ATOM 1041 C ASN A 129 -3.696 -10.107 25.649 1.00 16.97 C
ANISOU 1041 C ASN A 129 2726 1583 2136 -60 541 291 C
ATOM 1042 O ASN A 129 -4.309 -11.150 25.726 1.00 18.50 O
ANISOU 1042 O ASN A 129 2310 1854 2862 -310 146 -192 O
ATOM 1043 N ALA A 130 -4.280 -8.940 25.442 1.00 17.11 N
ANISOU 1043 N ALA A 130 2624 1277 2598 -121 799 -54 N
ATOM 1044 CA ALA A 130 -5.690 -8.775 25.278 1.00 20.65 C
ANISOU 1044 CA ALA A 130 2799 1664 3383 -195 393 -280 C
ATOM 1045 CB ALA A 130 -6.090 -7.377 25.662 1.00 18.74 C
ANISOU 1045 CB ALA A 130 2753 1648 2717 218 52 -154 C
ATOM 1046 C ALA A 130 -6.105 -9.060 23.837 1.00 19.09 C
ANISOU 1046 C ALA A 130 2058 1696 3497 -249 470 -496 C
ATOM 1047 O ALA A 130 -5.311 -9.012 22.899 1.00 22.29 O
ANISOU 1047 O ALA A 130 2623 2428 3418 -187 848 -883 O
ATOM 1048 N ASP A 131 -7.395 -9.292 23.681 1.00 21.49 N
ANISOU 1048 N ASP A 131 1925 1670 4568 -37 350 -489 N
ATOM 1049 CA ASP A 131 -8.021 -9.428 22.402 1.00 23.96 C
ANISOU 1049 CA ASP A 131 2759 1569 4775 -91 -114 -974 C
ATOM 1050 CB ASP A 131 -9.466 -9.863 22.641 1.00 30.41 C
ANISOU 1050 CB ASP A 131 2979 2778 5797 -666 -496 -333 C
ATOM 1051 CG ASP A 131 -10.267 -10.042 21.368 1.00 34.13 C
ANISOU 1051 CG ASP A 131 3703 2957 6307 -794 -1350 -127 C
ATOM 1052 OD1 ASP A 131 -9.753 -9.672 20.298 1.00 34.87 O
ANISOU 1052 OD1 ASP A 131 3684 2582 6982 -955 -356 -963 O
ATOM 1053 OD2 ASP A 131 -11.366 -10.621 21.453 1.00 44.04 O
ANISOU 1053 OD2 ASP A 131 4970 3577 8183 -1996 -1195 565 O
ATOM 1054 C ASP A 131 -7.941 -8.102 21.646 1.00 22.84 C
ANISOU 1054 C ASP A 131 2519 1977 4180 59 68 -928 C
ATOM 1055 O ASP A 131 -8.435 -7.083 22.124 1.00 22.32 O
ANISOU 1055 O ASP A 131 2183 1747 4549 -6 -147 -1073 O
ATOM 1056 N PRO A 132 -7.289 -8.023 20.472 1.00 22.73 N
ANISOU 1056 N PRO A 132 2506 2389 3741 130 -81 -1717 N
ATOM 1057 CA PRO A 132 -7.178 -6.745 19.761 1.00 26.31 C
ANISOU 1057 CA PRO A 132 3074 2812 4110 224 321 -1293 C
ATOM 1058 CB PRO A 132 -6.359 -7.100 18.503 1.00 29.40 C
ANISOU 1058 CB PRO A 132 3568 3281 4320 419 614 -1461 C
ATOM 1059 CG PRO A 132 -5.641 -8.372 18.861 1.00 31.14 C
ANISOU 1059 CG PRO A 132 3578 3609 4645 564 918 -1425 C
ATOM 1060 CD PRO A 132 -6.553 -9.108 19.810 1.00 26.31 C
ANISOU 1060 CD PRO A 132 3128 2373 4493 384 120 -1636 C
ATOM 1061 C PRO A 132 -8.519 -6.078 19.392 1.00 23.38 C
ANISOU 1061 C PRO A 132 3109 2338 3433 -118 -370 -1453 C
ATOM 1062 O PRO A 132 -8.588 -4.852 19.278 1.00 22.90 O
ANISOU 1062 O PRO A 132 3518 2363 2818 -461 320 -1117 O
ATOM 1063 N LEU A 133 -9.592 -6.869 19.250 1.00 26.80 N
ANISOU 1063 N LEU A 133 3782 2664 3734 -556 -314 -1655 N
ATOM 1064 CA LEU A 133 -10.937 -6.288 19.039 1.00 26.53 C
ANISOU 1064 CA LEU A 133 3560 2905 3616 -522 -634 -1130 C
ATOM 1065 CB LEU A 133 -11.931 -7.407 18.720 1.00 30.98 C
ANISOU 1065 CB LEU A 133 4275 3516 3977 -720 -1507 -1404 C
ATOM 1066 CG LEU A 133 -11.522 -8.293 17.547 1.00 38.69 C
ANISOU 1066 CG LEU A 133 5477 4956 4267 -440 -1347 -1886 C
ATOM 1067 CD1 LEU A 133 -12.478 -9.467 17.365 1.00 45.45 C
ANISOU 1067 CD1 LEU A 133 6195 5188 5883 -803 -1840 -1295 C
ATOM 1068 CD2 LEU A 133 -11.424 -7.468 16.271 1.00 40.92 C
ANISOU 1068 CD2 LEU A 133 5600 5281 4664 -31 -1325 -1202 C
ATOM 1069 C LEU A 133 -11.384 -5.490 20.277 1.00 21.79 C
ANISOU 1069 C LEU A 133 2780 2272 3227 -499 -489 -503 C
ATOM 1070 O LEU A 133 -11.971 -4.395 20.161 1.00 21.36 O
ANISOU 1070 O LEU A 133 2820 2543 2751 -263 -304 -241 O
ATOM 1071 N GLU A 134 -11.119 -6.020 21.473 1.00 18.74 N
ANISOU 1071 N GLU A 134 2456 1496 3166 -281 -164 -467 N
ATOM 1072 CA GLU A 134 -11.458 -5.308 22.707 1.00 17.58 C
ANISOU 1072 CA GLU A 134 2061 1670 2946 12 -64 -174 C
ATOM 1073 CB GLU A 134 -11.318 -6.176 23.975 1.00 21.25 C
ANISOU 1073 CB GLU A 134 2518 2012 3543 -111 -70 346 C
ATOM 1074 CG GLU A 134 -12.532 -6.994 24.330 1.00 28.10 C
ANISOU 1074 CG GLU A 134 3260 3136 4281 -582 136 205 C
ATOM 1075 CD GLU A 134 -13.725 -6.217 24.854 1.00 27.58 C
ANISOU 1075 CD GLU A 134 2738 3025 4713 -471 192 845 C
ATOM 1076 OE1 GLU A 134 -13.569 -5.132 25.466 1.00 25.21 O
ANISOU 1076 OE1 GLU A 134 2303 2998 4277 194 748 789 O
ATOM 1077 OE2 GLU A 134 -14.804 -6.760 24.735 1.00 37.04 O
ANISOU 1077 OE2 GLU A 134 3528 6075 4469 -1151 -998 -178 O
ATOM 1078 C GLU A 134 -10.542 -4.085 22.832 1.00 14.95 C
ANISOU 1078 C GLU A 134 1795 1565 2318 86 206 -116 C
ATOM 1079 O GLU A 134 -10.994 -3.037 23.258 1.00 14.85 O
ANISOU 1079 O GLU A 134 1939 1475 2228 114 381 15 O
ATOM 1080 N LEU A 135 -9.268 -4.205 22.453 1.00 13.23 N
ANISOU 1080 N LEU A 135 1865 1159 2002 49 346 -201 N
ATOM 1081 CA LEU A 135 -8.346 -3.063 22.583 1.00 13.24 C
ANISOU 1081 CA LEU A 135 1861 1221 1948 25 167 -346 C
ATOM 1082 CB LEU A 135 -6.921 -3.476 22.215 1.00 12.55 C
ANISOU 1082 CB LEU A 135 1938 978 1850 31 313 -335 C
ATOM 1083 CG LEU A 135 -6.223 -4.431 23.182 1.00 12.54 C
ANISOU 1083 CG LEU A 135 1873 999 1893 62 323 -241 C
ATOM 1084 CD1 LEU A 135 -4.822 -4.790 22.673 1.00 14.94 C
ANISOU 1084 CD1 LEU A 135 1956 1428 2290 267 264 -344 C
ATOM 1085 CD2 LEU A 135 -6.155 -3.847 24.584 1.00 14.23 C
ANISOU 1085 CD2 LEU A 135 2391 1164 1848 74 189 -69 C
ATOM 1086 C LEU A 135 -8.813 -1.892 21.702 1.00 12.47 C
ANISOU 1086 C LEU A 135 1721 1505 1509 -69 3 -390 C
ATOM 1087 O LEU A 135 -8.693 -0.752 22.107 1.00 12.24 O
ANISOU 1087 O LEU A 135 1780 1361 1508 -17 142 -246 O
ATOM 1088 N ALA A 136 -9.383 -2.179 20.520 1.00 11.97 N
ANISOU 1088 N ALA A 136 1503 1589 1455 -220 62 -454 N
ATOM 1089 CA ALA A 136 -9.899 -1.112 19.662 1.00 13.38 C
ANISOU 1089 CA ALA A 136 1827 1860 1395 -224 95 -304 C
ATOM 1090 CB ALA A 136 -10.176 -1.649 18.272 1.00 14.86 C
ANISOU 1090 CB ALA A 136 1918 2331 1394 -236 -200 -183 C
ATOM 1091 C ALA A 136 -11.146 -0.437 20.267 1.00 12.80 C
ANISOU 1091 C ALA A 136 1580 1730 1550 -178 -110 -160 C
ATOM 1092 O ALA A 136 -11.418 0.723 19.983 1.00 15.40 O
ANISOU 1092 O ALA A 136 1884 1767 2199 -195 -157 27 O
ATOM 1093 N LEU A 137 -11.907 -1.156 21.077 1.00 11.74 N
ANISOU 1093 N LEU A 137 1505 1608 1347 -108 11 -243 N
ATOM 1094 CA LEU A 137 -13.023 -0.532 21.808 1.00 12.45 C
ANISOU 1094 CA LEU A 137 1627 1596 1506 -33 94 -311 C
ATOM 1095 CB LEU A 137 -13.995 -1.594 22.315 1.00 15.33 C
ANISOU 1095 CB LEU A 137 1764 1956 2105 -319 188 -340 C
ATOM 1096 CG LEU A 137 -14.711 -2.396 21.238 1.00 19.43 C
ANISOU 1096 CG LEU A 137 2174 2521 2687 -556 -272 -352 C
ATOM 1097 CD1 LEU A 137 -15.605 -3.453 21.884 1.00 21.05 C
ANISOU 1097 CD1 LEU A 137 1950 2513 3534 -577 -301 -311 C
ATOM 1098 CD2 LEU A 137 -15.494 -1.458 20.309 1.00 22.74 C
ANISOU 1098 CD2 LEU A 137 2394 3059 3187 -584 -833 -392 C
ATOM 1099 C LEU A 137 -12.519 0.276 23.003 1.00 11.98 C
ANISOU 1099 C LEU A 137 1742 1337 1472 -210 199 -202 C
ATOM 1100 O LEU A 137 -13.227 1.170 23.474 1.00 13.53 O
ANISOU 1100 O LEU A 137 1952 1493 1696 -57 244 -198 O
ATOM 1101 N LEU A 138 -11.344 -0.083 23.515 1.00 11.30 N
ANISOU 1101 N LEU A 138 1824 1204 1266 -116 287 -254 N
ATOM 1102 CA LEU A 138 -10.749 0.590 24.656 1.00 11.47 C
ANISOU 1102 CA LEU A 138 1881 1262 1214 -6 128 -169 C
ATOM 1103 CB LEU A 138 -9.647 -0.318 25.233 1.00 12.42 C
ANISOU 1103 CB LEU A 138 1899 1426 1391 111 20 -171 C
ATOM 1104 CG LEU A 138 -9.194 -0.084 26.670 1.00 12.55 C
ANISOU 1104 CG LEU A 138 1784 1465 1519 163 -104 -338 C
ATOM 1105 CD1 LEU A 138 -8.392 -1.293 27.125 1.00 14.44 C
ANISOU 1105 CD1 LEU A 138 2363 1662 1461 311 -158 -129 C
ATOM 1106 CD2 LEU A 138 -8.371 1.173 26.821 1.00 12.92 C
ANISOU 1106 CD2 LEU A 138 1827 1637 1443 3 -74 -31 C
ATOM 1107 C LEU A 138 -10.211 1.964 24.243 1.00 10.56 C
ANISOU 1107 C LEU A 138 1655 1310 1047 -28 260 -158 C
ATOM 1108 O LEU A 138 -10.468 2.966 24.938 1.00 11.49 O
ANISOU 1108 O LEU A 138 1911 1337 1116 91 181 -170 O
ATOM 1109 N SER A 139 -9.458 2.029 23.136 1.00 10.78 N
ANISOU 1109 N SER A 139 1728 1232 1135 -46 356 -213 N
ATOM 1110 CA SER A 139 -8.831 3.282 22.697 1.00 11.02 C
ANISOU 1110 CA SER A 139 1644 1376 1164 -113 289 -247 C
ATOM 1111 CB SER A 139 -7.375 3.330 23.139 1.00 11.98 C
ANISOU 1111 CB SER A 139 1737 1543 1271 -112 8 -132 C
ATOM 1112 OG SER A 139 -6.706 4.516 22.702 1.00 12.95 O
ANISOU 1112 OG SER A 139 1765 1648 1505 -242 48 -93 O
ATOM 1113 C SER A 139 -8.885 3.378 21.184 1.00 10.80 C
ANISOU 1113 C SER A 139 1505 1464 1133 18 233 -305 C
ATOM 1114 O SER A 139 -8.712 2.361 20.497 1.00 10.82 O
ANISOU 1114 O SER A 139 1675 1455 980 -121 115 -328 O
ATOM 1115 N PRO A 140 -8.964 4.613 20.632 1.00 11.61 N
ANISOU 1115 N PRO A 140 1718 1486 1206 29 305 -161 N
ATOM 1116 CA PRO A 140 -8.775 4.816 19.193 1.00 11.32 C
ANISOU 1116 CA PRO A 140 1729 1407 1165 25 200 -187 C
ATOM 1117 CB PRO A 140 -9.166 6.278 18.970 1.00 11.48 C
ANISOU 1117 CB PRO A 140 1531 1447 1383 104 300 -177 C
ATOM 1118 CG PRO A 140 -8.840 6.932 20.301 1.00 12.81 C
ANISOU 1118 CG PRO A 140 1905 1520 1441 104 149 -133 C
ATOM 1119 CD PRO A 140 -9.270 5.885 21.328 1.00 12.52 C
ANISOU 1119 CD PRO A 140 1824 1521 1411 198 339 -94 C
ATOM 1120 C PRO A 140 -7.342 4.541 18.734 1.00 10.95 C
ANISOU 1120 C PRO A 140 1625 1487 1046 -119 77 -142 C
ATOM 1121 O PRO A 140 -7.092 4.357 17.547 1.00 12.89 O
ANISOU 1121 O PRO A 140 1722 2161 1012 218 -48 -156 O
ATOM 1122 N CYS A 141 -6.407 4.545 19.698 1.00 10.25 N
ANISOU 1122 N CYS A 141 1468 1318 1107 -116 104 -194 N
ATOM 1123 CA CYS A 141 -4.993 4.318 19.416 1.00 10.35 C
ANISOU 1123 CA CYS A 141 1466 1385 1081 -96 10 -127 C
ATOM 1124 CB CYS A 141 -4.169 5.446 20.000 1.00 11.42 C
ANISOU 1124 CB CYS A 141 1602 1282 1452 -113 -56 -127 C
ATOM 1125 SG CYS A 141 -4.494 7.033 19.200 1.00 14.22 S
ANISOU 1125 SG CYS A 141 2117 1196 2089 -182 -138 1 S
ATOM 1126 C CYS A 141 -4.584 2.969 20.003 1.00 11.03 C
ANISOU 1126 C CYS A 141 1643 1245 1301 -67 88 -240 C
ATOM 1127 O CYS A 141 -3.871 2.898 20.998 1.00 12.84 O
ANISOU 1127 O CYS A 141 2025 1354 1498 -100 -195 -147 O
ATOM 1128 N SER A 142 -5.018 1.903 19.327 1.00 10.68 N
ANISOU 1128 N SER A 142 1603 1183 1270 -215 49 -146 N
ATOM 1129 CA SER A 142 -4.883 0.548 19.872 1.00 11.64 C
ANISOU 1129 CA SER A 142 1664 1184 1576 -79 300 -143 C
ATOM 1130 CB SER A 142 -6.178 -0.202 19.769 1.00 13.25 C
ANISOU 1130 CB SER A 142 1632 1486 1915 -199 457 -337 C
ATOM 1131 OG SER A 142 -6.571 -0.386 18.417 1.00 15.73 O
ANISOU 1131 OG SER A 142 2054 1878 2043 -509 322 -682 O
ATOM 1132 C SER A 142 -3.746 -0.252 19.236 1.00 11.18 C
ANISOU 1132 C SER A 142 1675 1171 1401 -32 298 -15 C
ATOM 1133 O SER A 142 -3.358 -1.270 19.785 1.00 12.21 O
ANISOU 1133 O SER A 142 1660 1206 1772 167 315 153 O
ATOM 1134 N ASP A 143 -3.211 0.207 18.105 1.00 9.85 N
ANISOU 1134 N ASP A 143 1461 1038 1244 -105 219 -86 N
ATOM 1135 CA ASP A 143 -2.087 -0.481 17.446 1.00 10.45 C
ANISOU 1135 CA ASP A 143 1485 1177 1306 -38 141 -104 C
ATOM 1136 CB ASP A 143 -1.810 0.139 16.082 1.00 11.34 C
ANISOU 1136 CB ASP A 143 1640 1350 1317 40 50 35 C
ATOM 1137 CG ASP A 143 -0.604 -0.450 15.380 1.00 11.40 C
ANISOU 1137 CG ASP A 143 1703 1421 1205 -7 103 9 C
ATOM 1138 OD1 ASP A 143 0.539 0.071 15.638 1.00 11.66 O
ANISOU 1138 OD1 ASP A 143 1660 1367 1402 -1 89 -69 O
ATOM 1139 OD2 ASP A 143 -0.791 -1.430 14.621 1.00 12.71 O
ANISOU 1139 OD2 ASP A 143 1707 1603 1517 18 50 -239 O
ATOM 1140 C ASP A 143 -0.862 -0.397 18.350 1.00 10.00 C
ANISOU 1140 C ASP A 143 1362 1211 1226 -16 188 -47 C
ATOM 1141 O ASP A 143 -0.562 0.696 18.853 1.00 11.22 O
ANISOU 1141 O ASP A 143 1749 1190 1321 -13 106 -91 O
ATOM 1142 N VAL A 144 -0.169 -1.523 18.514 1.00 10.35 N
ANISOU 1142 N VAL A 144 1532 1194 1206 -27 107 -127 N
ATOM 1143 CA VAL A 144 1.014 -1.618 19.364 1.00 10.86 C
ANISOU 1143 CA VAL A 144 1567 1247 1311 97 18 -132 C
ATOM 1144 CB VAL A 144 0.856 -2.785 20.353 1.00 11.61 C
ANISOU 1144 CB VAL A 144 1620 1375 1416 -21 60 -11 C
ATOM 1145 CG1 VAL A 144 2.142 -3.081 21.113 1.00 12.64 C
ANISOU 1145 CG1 VAL A 144 1765 1585 1452 231 153 118 C
ATOM 1146 CG2 VAL A 144 -0.294 -2.537 21.320 1.00 12.09 C
ANISOU 1146 CG2 VAL A 144 1338 1742 1511 -28 -24 189 C
ATOM 1147 C VAL A 144 2.260 -1.773 18.492 1.00 10.74 C
ANISOU 1147 C VAL A 144 1500 1145 1434 2 -4 -93 C
ATOM 1148 O VAL A 144 2.304 -2.590 17.587 1.00 11.48 O
ANISOU 1148 O VAL A 144 1709 1295 1355 21 158 -155 O
ATOM 1149 N ASP A 145 3.285 -0.967 18.793 1.00 11.04 N
ANISOU 1149 N ASP A 145 1581 1308 1303 -102 11 -182 N
ATOM 1150 CA ASP A 145 4.533 -0.953 18.015 1.00 11.08 C
ANISOU 1150 CA ASP A 145 1573 1282 1351 -116 39 -32 C
ATOM 1151 CB ASP A 145 5.507 0.063 18.576 1.00 11.33 C
ANISOU 1151 CB ASP A 145 1635 1356 1310 -94 -50 -88 C
ATOM 1152 CG ASP A 145 5.048 1.510 18.477 1.00 11.59 C
ANISOU 1152 CG ASP A 145 1611 1395 1396 -39 100 -92 C
ATOM 1153 OD1 ASP A 145 4.355 1.860 17.505 1.00 12.10 O
ANISOU 1153 OD1 ASP A 145 1512 1564 1520 -8 76 -143 O
ATOM 1154 OD2 ASP A 145 5.455 2.274 19.367 1.00 12.90 O
ANISOU 1154 OD2 ASP A 145 1980 1261 1661 3 -108 -117 O
ATOM 1155 C ASP A 145 5.212 -2.313 17.980 1.00 10.99 C
ANISOU 1155 C ASP A 145 1596 1365 1212 -102 135 -149 C
ATOM 1156 O ASP A 145 5.376 -2.990 19.004 1.00 12.13 O
ANISOU 1156 O ASP A 145 1980 1404 1223 99 163 -52 O
ATOM 1157 N GLU A 146 5.660 -2.697 16.780 1.00 10.55 N
ANISOU 1157 N GLU A 146 1496 1259 1253 40 286 -44 N
ATOM 1158 CA GLU A 146 6.399 -3.955 16.619 1.00 10.62 C
ANISOU 1158 CA GLU A 146 1431 1161 1441 -40 41 -64 C
ATOM 1159 CB GLU A 146 6.035 -4.614 15.299 1.00 11.09 C
ANISOU 1159 CB GLU A 146 1462 1356 1395 57 59 -132 C
ATOM 1160 CG GLU A 146 4.553 -4.983 15.222 1.00 12.03 C
ANISOU 1160 CG GLU A 146 1478 1455 1636 69 -49 -275 C
ATOM 1161 CD GLU A 146 3.582 -3.935 14.696 1.00 12.49 C
ANISOU 1161 CD GLU A 146 1645 1413 1684 40 -20 -162 C
ATOM 1162 OE1 GLU A 146 4.016 -2.793 14.390 1.00 12.85 O
ANISOU 1162 OE1 GLU A 146 1803 1507 1570 -94 32 -108 O
ATOM 1163 OE2 GLU A 146 2.370 -4.265 14.598 1.00 12.40 O
ANISOU 1163 OE2 GLU A 146 1677 1544 1490 150 52 -120 O
ATOM 1164 C GLU A 146 7.914 -3.744 16.709 1.00 11.49 C
ANISOU 1164 C GLU A 146 1511 1451 1403 -145 -44 -122 C
ATOM 1165 O GLU A 146 8.620 -4.656 17.131 1.00 11.81 O
ANISOU 1165 O GLU A 146 1493 1459 1534 -47 166 -23 O
ATOM 1166 N TYR A 147 8.388 -2.562 16.291 1.00 11.04 N
ANISOU 1166 N TYR A 147 1434 1390 1370 58 77 20 N
ATOM 1167 CA TYR A 147 9.816 -2.257 16.183 1.00 10.90 C
ANISOU 1167 CA TYR A 147 1451 1176 1511 -107 75 -45 C
ATOM 1168 CB TYR A 147 10.249 -2.184 14.714 1.00 11.86 C
ANISOU 1168 CB TYR A 147 1544 1472 1489 -64 63 -77 C
ATOM 1169 CG TYR A 147 9.843 -3.398 13.933 1.00 11.38 C
ANISOU 1169 CG TYR A 147 1418 1377 1529 50 112 -106 C
ATOM 1170 CD1 TYR A 147 10.488 -4.611 14.091 1.00 10.88 C
ANISOU 1170 CD1 TYR A 147 1285 1388 1460 78 140 -127 C
ATOM 1171 CE1 TYR A 147 10.046 -5.757 13.435 1.00 11.41 C
ANISOU 1171 CE1 TYR A 147 1476 1270 1589 44 -77 -2 C
ATOM 1172 CZ TYR A 147 8.940 -5.696 12.612 1.00 10.29 C
ANISOU 1172 CZ TYR A 147 1373 1361 1173 -10 101 -192 C
ATOM 1173 OH TYR A 147 8.447 -6.790 11.955 1.00 11.28 O
ANISOU 1173 OH TYR A 147 1507 1393 1385 -68 120 -265 O
ATOM 1174 CE2 TYR A 147 8.306 -4.484 12.424 1.00 11.53 C
ANISOU 1174 CE2 TYR A 147 1533 1423 1425 18 -45 -88 C
ATOM 1175 CD2 TYR A 147 8.750 -3.359 13.086 1.00 11.32 C
ANISOU 1175 CD2 TYR A 147 1672 1277 1351 97 2 22 C
ATOM 1176 C TYR A 147 10.135 -0.980 16.951 1.00 12.59 C
ANISOU 1176 C TYR A 147 1490 1409 1882 -161 281 -314 C
ATOM 1177 O TYR A 147 9.235 -0.220 17.310 1.00 15.27 O
ANISOU 1177 O TYR A 147 1718 1805 2277 143 177 -581 O
ATOM 1178 N ASN A 148 11.436 -0.724 17.118 1.00 12.71 N
ANISOU 1178 N ASN A 148 1455 1464 1910 -129 160 -338 N
ATOM 1179 CA ASN A 148 11.870 0.343 18.007 1.00 12.98 C
ANISOU 1179 CA ASN A 148 1493 1596 1840 -176 87 -399 C
ATOM 1180 CB ASN A 148 13.139 -0.030 18.768 1.00 14.10 C
ANISOU 1180 CB ASN A 148 1737 1695 1924 -122 -107 -477 C
ATOM 1181 CG ASN A 148 14.395 -0.040 17.921 1.00 14.31 C
ANISOU 1181 CG ASN A 148 1780 1763 1891 -5 -58 -383 C
ATOM 1182 OD1 ASN A 148 14.332 -0.102 16.685 1.00 14.01 O
ANISOU 1182 OD1 ASN A 148 1720 1874 1729 -17 112 -473 O
ATOM 1183 ND2 ASN A 148 15.539 -0.002 18.596 1.00 16.90 N
ANISOU 1183 ND2 ASN A 148 1829 2442 2147 -26 -146 -450 N
ATOM 1184 C ASN A 148 12.014 1.692 17.290 1.00 13.26 C
ANISOU 1184 C ASN A 148 1546 1635 1857 -62 90 -390 C
ATOM 1185 O ASN A 148 12.384 2.681 17.918 1.00 14.39 O
ANISOU 1185 O ASN A 148 1979 1666 1822 -144 -80 -387 O
ATOM 1186 N ALYS A 149 11.706 1.719 15.997 0.50 12.87 N
ANISOU 1186 N ALYS A 149 1506 1505 1876 47 -2 -399 N
ATOM 1187 N BLYS A 149 11.710 1.720 15.995 0.50 12.83 N
ANISOU 1187 N BLYS A 149 1508 1503 1862 -14 -57 -395 N
ATOM 1188 CA ALYS A 149 11.686 2.944 15.207 0.50 14.10 C
ANISOU 1188 CA ALYS A 149 1662 1627 2067 -77 13 -255 C
ATOM 1189 CA BLYS A 149 11.696 2.946 15.200 0.50 13.89 C
ANISOU 1189 CA BLYS A 149 1690 1632 1953 -172 -90 -269 C
ATOM 1190 CB ALYS A 149 12.951 3.088 14.360 0.50 16.08 C
ANISOU 1190 CB ALYS A 149 1920 1703 2487 -2 295 -213 C
ATOM 1191 CB BLYS A 149 12.968 3.096 14.359 0.50 15.36 C
ANISOU 1191 CB BLYS A 149 1908 1714 2213 -211 65 -232 C
ATOM 1192 CG ALYS A 149 14.246 3.168 15.133 0.50 18.12 C
ANISOU 1192 CG ALYS A 149 1777 2124 2982 -40 360 -144 C
ATOM 1193 CG BLYS A 149 14.260 3.143 15.141 0.50 17.39 C
ANISOU 1193 CG BLYS A 149 1838 2167 2601 -335 58 -134 C
ATOM 1194 CD ALYS A 149 15.330 3.769 14.283 0.50 20.84 C
ANISOU 1194 CD ALYS A 149 1983 2343 3592 -278 479 -62 C
ATOM 1195 CD BLYS A 149 14.345 4.328 16.068 0.50 19.05 C
ANISOU 1195 CD BLYS A 149 2028 2262 2945 -622 -149 -243 C
ATOM 1196 CE ALYS A 149 16.702 3.670 14.885 0.50 21.76 C
ANISOU 1196 CE ALYS A 149 2015 2288 3963 -102 530 -67 C
ATOM 1197 CE BLYS A 149 15.279 4.074 17.224 0.50 21.90 C
ANISOU 1197 CE BLYS A 149 2333 2769 3216 -689 -365 -340 C
ATOM 1198 NZ ALYS A 149 17.639 3.414 13.786 0.50 18.31 N
ANISOU 1198 NZ ALYS A 149 1484 1180 4293 -304 770 214 N
ATOM 1199 NZ BLYS A 149 16.670 4.308 16.803 0.50 23.92 N
ANISOU 1199 NZ BLYS A 149 2098 3144 3843 -756 -602 -447 N
ATOM 1200 C ALYS A 149 10.478 2.889 14.271 0.50 13.46 C
ANISOU 1200 C ALYS A 149 1817 1483 1812 -95 6 -308 C
ATOM 1201 C BLYS A 149 10.483 2.890 14.268 0.50 13.19 C
ANISOU 1201 C BLYS A 149 1791 1475 1745 -144 -71 -316 C
ATOM 1202 O ALYS A 149 10.028 1.802 13.877 0.50 14.90 O
ANISOU 1202 O ALYS A 149 1936 1359 2366 -40 -27 -326 O
ATOM 1203 O BLYS A 149 10.031 1.803 13.878 0.50 14.69 O
ANISOU 1203 O BLYS A 149 1915 1366 2300 -92 -75 -359 O
ATOM 1204 N ILE A 150 9.981 4.078 13.932 1.00 13.18 N
ANISOU 1204 N ILE A 150 1736 1450 1819 -126 43 -317 N
ATOM 1205 CA ILE A 150 8.898 4.270 12.983 1.00 13.15 C
ANISOU 1205 CA ILE A 150 1923 1257 1817 -66 24 -160 C
ATOM 1206 CB ILE A 150 7.647 4.817 13.701 1.00 12.42 C
ANISOU 1206 CB ILE A 150 1810 1275 1633 -213 67 -164 C
ATOM 1207 CG1 ILE A 150 7.083 3.780 14.676 1.00 12.36 C
ANISOU 1207 CG1 ILE A 150 1518 1411 1767 -347 -24 -176 C
ATOM 1208 CG2 ILE A 150 6.598 5.312 12.706 1.00 13.69 C
ANISOU 1208 CG2 ILE A 150 2068 1454 1677 -35 77 -39 C
ATOM 1209 CD1 ILE A 150 6.146 4.360 15.711 1.00 13.61 C
ANISOU 1209 CD1 ILE A 150 1623 1670 1878 -142 -17 -193 C
ATOM 1210 C ILE A 150 9.415 5.253 11.936 1.00 13.42 C
ANISOU 1210 C ILE A 150 1865 1282 1951 -107 178 -170 C
ATOM 1211 O ILE A 150 9.909 6.316 12.298 1.00 14.01 O
ANISOU 1211 O ILE A 150 2069 1485 1767 -227 115 -352 O
ATOM 1212 N LYS A 151 9.203 4.941 10.659 1.00 13.68 N
ANISOU 1212 N LYS A 151 2118 1198 1883 -337 257 -142 N
ATOM 1213 CA LYS A 151 9.628 5.806 9.572 1.00 13.75 C
ANISOU 1213 CA LYS A 151 2000 1262 1959 -309 275 -58 C
ATOM 1214 CB LYS A 151 10.905 5.294 8.906 1.00 16.07 C
ANISOU 1214 CB LYS A 151 2241 1823 2040 -324 345 -104 C
ATOM 1215 CG LYS A 151 12.116 5.176 9.816 1.00 17.82 C
ANISOU 1215 CG LYS A 151 2226 2140 2404 -70 326 159 C
ATOM 1216 CD LYS A 151 13.407 4.821 9.069 1.00 18.68 C
ANISOU 1216 CD LYS A 151 2383 2258 2457 -152 432 117 C
ATOM 1217 CE LYS A 151 13.319 3.525 8.293 1.00 20.39 C
ANISOU 1217 CE LYS A 151 2840 2345 2560 -100 435 28 C
ATOM 1218 NZ LYS A 151 14.609 3.170 7.647 1.00 22.75 N
ANISOU 1218 NZ LYS A 151 3136 2646 2861 67 476 -465 N
ATOM 1219 C LYS A 151 8.511 5.904 8.539 1.00 14.60 C
ANISOU 1219 C LYS A 151 2303 1570 1674 -320 345 -170 C
ATOM 1220 O LYS A 151 7.901 4.904 8.173 1.00 15.61 O
ANISOU 1220 O LYS A 151 2497 1586 1848 -334 102 -150 O
ATOM 1221 N ALA A 152 8.296 7.112 8.010 1.00 14.68 N
ANISOU 1221 N ALA A 152 2311 1383 1884 -320 272 -287 N
ATOM 1222 CA ALA A 152 7.252 7.304 6.997 1.00 15.67 C
ANISOU 1222 CA ALA A 152 2423 1794 1737 -276 323 18 C
ATOM 1223 CB ALA A 152 6.954 8.760 6.830 1.00 17.59 C
ANISOU 1223 CB ALA A 152 2865 1795 2022 -29 27 -150 C
ATOM 1224 C ALA A 152 7.629 6.643 5.664 1.00 16.14 C
ANISOU 1224 C ALA A 152 2665 1633 1831 -143 343 29 C
ATOM 1225 O ALA A 152 6.754 6.400 4.832 1.00 18.60 O
ANISOU 1225 O ALA A 152 2637 2222 2208 -282 245 -55 O
ATOM 1226 N VAL A 153 8.908 6.324 5.459 1.00 16.25 N
ANISOU 1226 N VAL A 153 2703 1804 1667 -307 566 56 N
ATOM 1227 CA VAL A 153 9.295 5.641 4.225 1.00 18.30 C
ANISOU 1227 CA VAL A 153 3096 2039 1814 -223 683 -81 C
ATOM 1228 CB VAL A 153 10.795 5.766 3.938 1.00 20.67 C
ANISOU 1228 CB VAL A 153 3287 2209 2357 32 1090 -250 C
ATOM 1229 CG1 VAL A 153 11.154 7.210 3.610 1.00 25.34 C
ANISOU 1229 CG1 VAL A 153 4092 2527 3006 -315 1397 -64 C
ATOM 1230 CG2 VAL A 153 11.667 5.177 5.039 1.00 21.98 C
ANISOU 1230 CG2 VAL A 153 3155 3104 2089 117 1287 -120 C
ATOM 1231 C VAL A 153 8.847 4.165 4.246 1.00 18.00 C
ANISOU 1231 C VAL A 153 3169 1989 1679 -270 515 -62 C
ATOM 1232 O VAL A 153 8.931 3.508 3.212 1.00 22.23 O
ANISOU 1232 O VAL A 153 4189 2169 2087 -116 382 -515 O
ATOM 1233 N SER A 154 8.459 3.637 5.417 1.00 16.20 N
ANISOU 1233 N SER A 154 2788 1649 1718 -217 449 -10 N
ATOM 1234 CA SER A 154 8.107 2.219 5.613 1.00 17.78 C
ANISOU 1234 CA SER A 154 2899 1762 2095 -369 176 168 C
ATOM 1235 CB SER A 154 8.716 1.706 6.901 1.00 20.21 C
ANISOU 1235 CB SER A 154 3002 2134 2541 -296 -168 483 C
ATOM 1236 OG SER A 154 10.085 1.931 6.927 1.00 25.16 O
ANISOU 1236 OG SER A 154 3080 2595 3883 -342 -369 664 O
ATOM 1237 C SER A 154 6.590 2.043 5.712 1.00 15.48 C
ANISOU 1237 C SER A 154 2735 1476 1670 -3 356 -9 C
ATOM 1238 O SER A 154 5.893 2.873 6.294 1.00 18.88 O
ANISOU 1238 O SER A 154 3311 1686 2175 25 779 -261 O
ATOM 1239 N MET A 155 6.084 0.902 5.252 1.00 14.79 N
ANISOU 1239 N MET A 155 2662 1199 1758 235 180 110 N
ATOM 1240 CA MET A 155 4.640 0.710 5.228 1.00 15.43 C
ANISOU 1240 CA MET A 155 2611 1497 1752 246 197 161 C
ATOM 1241 CB MET A 155 4.233 -0.345 4.208 1.00 17.74 C
ANISOU 1241 CB MET A 155 2799 1843 2097 367 166 -200 C
ATOM 1242 CG MET A 155 4.608 0.044 2.796 1.00 21.80 C
ANISOU 1242 CG MET A 155 3430 2787 2062 -27 37 -293 C
ATOM 1243 SD MET A 155 3.837 1.517 2.133 1.00 33.35 S
ANISOU 1243 SD MET A 155 5365 4050 3257 400 -252 729 S
ATOM 1244 CE MET A 155 2.218 1.487 2.890 1.00 35.17 C
ANISOU 1244 CE MET A 155 4664 4708 3991 122 -1154 617 C
ATOM 1245 C MET A 155 4.065 0.343 6.601 1.00 15.08 C
ANISOU 1245 C MET A 155 2581 1354 1794 134 141 176 C
ATOM 1246 O MET A 155 2.899 0.661 6.866 1.00 15.88 O
ANISOU 1246 O MET A 155 2610 1390 2033 122 124 51 O
ATOM 1247 N ASN A 156 4.851 -0.309 7.464 1.00 13.08 N
ANISOU 1247 N ASN A 156 2029 1328 1611 137 286 40 N
ATOM 1248 CA ASN A 156 4.365 -0.582 8.811 1.00 13.31 C
ANISOU 1248 CA ASN A 156 2134 1306 1615 129 259 102 C
ATOM 1249 CB ASN A 156 4.999 -1.816 9.452 1.00 13.22 C
ANISOU 1249 CB ASN A 156 2240 1139 1641 123 255 -18 C
ATOM 1250 CG ASN A 156 4.363 -2.112 10.796 1.00 13.62 C
ANISOU 1250 CG ASN A 156 2093 1464 1617 4 150 33 C
ATOM 1251 OD1 ASN A 156 3.129 -2.104 10.885 1.00 13.55 O
ANISOU 1251 OD1 ASN A 156 2014 1487 1646 -80 -116 -126 O
ATOM 1252 ND2 ASN A 156 5.174 -2.401 11.819 1.00 13.73 N
ANISOU 1252 ND2 ASN A 156 1996 1563 1656 106 101 -31 N
ATOM 1253 C ASN A 156 4.613 0.679 9.647 1.00 13.58 C
ANISOU 1253 C ASN A 156 2259 1194 1705 230 266 130 C
ATOM 1254 O ASN A 156 5.643 0.844 10.282 1.00 15.97 O
ANISOU 1254 O ASN A 156 2212 1398 2458 302 157 -15 O
ATOM 1255 N ASN A 157 3.638 1.580 9.587 1.00 11.79 N
ANISOU 1255 N ASN A 157 1729 1205 1542 41 -34 -141 N
ATOM 1256 CA ASN A 157 3.816 2.911 10.143 1.00 11.07 C
ANISOU 1256 CA ASN A 157 1673 1177 1355 39 63 -124 C
ATOM 1257 CB ASN A 157 4.243 3.902 9.056 1.00 12.26 C
ANISOU 1257 CB ASN A 157 1737 1396 1525 114 157 51 C
ATOM 1258 CG ASN A 157 4.168 5.347 9.498 1.00 11.50 C
ANISOU 1258 CG ASN A 157 1771 1406 1189 -199 184 -9 C
ATOM 1259 OD1 ASN A 157 4.090 5.595 10.706 1.00 11.38 O
ANISOU 1259 OD1 ASN A 157 1707 1422 1192 -190 217 -38 O
ATOM 1260 ND2 ASN A 157 4.196 6.278 8.537 1.00 13.06 N
ANISOU 1260 ND2 ASN A 157 1762 1587 1613 -287 363 272 N
ATOM 1261 C ASN A 157 2.497 3.332 10.769 1.00 11.38 C
ANISOU 1261 C ASN A 157 1697 1221 1404 111 109 13 C
ATOM 1262 O ASN A 157 1.559 3.687 10.054 1.00 11.12 O
ANISOU 1262 O ASN A 157 1569 1331 1322 19 122 0 O
ATOM 1263 N PRO A 158 2.389 3.325 12.111 1.00 10.74 N
ANISOU 1263 N PRO A 158 1431 1315 1333 58 130 -172 N
ATOM 1264 CA PRO A 158 1.116 3.658 12.752 1.00 11.36 C
ANISOU 1264 CA PRO A 158 1546 1419 1349 40 222 -225 C
ATOM 1265 CB PRO A 158 1.379 3.295 14.225 1.00 12.50 C
ANISOU 1265 CB PRO A 158 1869 1505 1374 103 266 -56 C
ATOM 1266 CG PRO A 158 2.847 3.535 14.398 1.00 12.60 C
ANISOU 1266 CG PRO A 158 1987 1440 1358 246 40 2 C
ATOM 1267 CD PRO A 158 3.455 3.046 13.099 1.00 11.89 C
ANISOU 1267 CD PRO A 158 1688 1473 1354 129 50 -64 C
ATOM 1268 C PRO A 158 0.734 5.135 12.596 1.00 11.35 C
ANISOU 1268 C PRO A 158 1469 1408 1434 -167 158 -17 C
ATOM 1269 O PRO A 158 -0.369 5.508 12.949 1.00 12.74 O
ANISOU 1269 O PRO A 158 1726 1479 1634 87 256 56 O
ATOM 1270 N TYR A 159 1.654 5.976 12.106 1.00 10.32 N
ANISOU 1270 N TYR A 159 1228 1365 1328 -68 187 30 N
ATOM 1271 CA TYR A 159 1.320 7.384 11.892 1.00 10.97 C
ANISOU 1271 CA TYR A 159 1492 1305 1367 -53 139 -61 C
ATOM 1272 CB TYR A 159 2.459 8.311 12.343 1.00 11.35 C
ANISOU 1272 CB TYR A 159 1456 1457 1397 -79 147 -38 C
ATOM 1273 CG TYR A 159 2.895 8.032 13.764 1.00 11.58 C
ANISOU 1273 CG TYR A 159 1541 1484 1374 -42 144 -74 C
ATOM 1274 CD1 TYR A 159 1.941 7.803 14.754 1.00 11.42 C
ANISOU 1274 CD1 TYR A 159 1683 1345 1311 -64 155 -56 C
ATOM 1275 CE1 TYR A 159 2.315 7.480 16.049 1.00 11.45 C
ANISOU 1275 CE1 TYR A 159 1619 1435 1293 -72 234 54 C
ATOM 1276 CZ TYR A 159 3.647 7.407 16.385 1.00 11.49 C
ANISOU 1276 CZ TYR A 159 1607 1330 1426 -156 120 17 C
ATOM 1277 OH TYR A 159 3.963 7.030 17.667 1.00 11.61 O
ANISOU 1277 OH TYR A 159 1732 1329 1348 -242 14 -94 O
ATOM 1278 CE2 TYR A 159 4.607 7.664 15.421 1.00 11.23 C
ANISOU 1278 CE2 TYR A 159 1449 1371 1445 -233 47 -74 C
ATOM 1279 CD2 TYR A 159 4.223 7.990 14.132 1.00 12.61 C
ANISOU 1279 CD2 TYR A 159 1629 1553 1608 -1 172 151 C
ATOM 1280 C TYR A 159 0.851 7.626 10.456 1.00 11.18 C
ANISOU 1280 C TYR A 159 1611 1209 1426 -172 10 0 C
ATOM 1281 O TYR A 159 0.582 8.774 10.096 1.00 11.80 O
ANISOU 1281 O TYR A 159 1724 1179 1578 -160 -73 23 O
ATOM 1282 N ARG A 160 0.662 6.564 9.664 1.00 11.01 N
ANISOU 1282 N ARG A 160 1565 1260 1358 -79 -87 -17 N
ATOM 1283 CA ARG A 160 -0.129 6.697 8.448 1.00 11.05 C
ANISOU 1283 CA ARG A 160 1713 1291 1192 -16 47 -45 C
ATOM 1284 CB ARG A 160 -0.321 5.347 7.761 1.00 11.99 C
ANISOU 1284 CB ARG A 160 1971 1254 1328 -45 -106 -54 C
ATOM 1285 CG ARG A 160 0.901 4.900 6.961 1.00 14.10 C
ANISOU 1285 CG ARG A 160 2412 1414 1528 13 202 63 C
ATOM 1286 CD ARG A 160 0.932 3.418 6.602 1.00 18.33 C
ANISOU 1286 CD ARG A 160 3297 1503 2163 168 -31 -167 C
ATOM 1287 NE ARG A 160 0.033 3.025 5.560 1.00 19.44 N
ANISOU 1287 NE ARG A 160 3907 1365 2114 244 -344 5 N
ATOM 1288 CZ ARG A 160 -0.258 1.769 5.155 1.00 20.24 C
ANISOU 1288 CZ ARG A 160 3871 1673 2145 86 -426 -346 C
ATOM 1289 NH1 ARG A 160 0.441 0.745 5.566 1.00 23.61 N
ANISOU 1289 NH1 ARG A 160 4890 2000 2079 446 -204 -391 N
ATOM 1290 NH2 ARG A 160 -1.291 1.561 4.342 1.00 24.80 N
ANISOU 1290 NH2 ARG A 160 3707 3005 2710 139 -329 -404 N
ATOM 1291 C ARG A 160 -1.470 7.327 8.794 1.00 11.39 C
ANISOU 1291 C ARG A 160 1574 1514 1238 -4 -73 -116 C
ATOM 1292 O ARG A 160 -2.180 6.859 9.690 1.00 13.45 O
ANISOU 1292 O ARG A 160 1627 2000 1483 86 52 79 O
ATOM 1293 N GLN A 161 -1.843 8.366 8.053 1.00 11.34 N
ANISOU 1293 N GLN A 161 1475 1567 1267 -27 49 -66 N
ATOM 1294 CA GLN A 161 -3.154 8.930 8.287 1.00 12.27 C
ANISOU 1294 CA GLN A 161 1522 1666 1473 42 59 47 C
ATOM 1295 CB GLN A 161 -3.207 10.350 7.738 1.00 15.07 C
ANISOU 1295 CB GLN A 161 1993 1681 2051 -167 -31 152 C
ATOM 1296 CG GLN A 161 -3.106 10.483 6.240 1.00 16.25 C
ANISOU 1296 CG GLN A 161 2113 1942 2116 -314 72 402 C
ATOM 1297 CD GLN A 161 -3.105 11.965 5.881 1.00 20.17 C
ANISOU 1297 CD GLN A 161 2974 1953 2736 -1137 397 704 C
ATOM 1298 OE1 GLN A 161 -2.411 12.820 6.468 1.00 24.62 O
ANISOU 1298 OE1 GLN A 161 4029 2216 3107 -850 112 446 O
ATOM 1299 NE2 GLN A 161 -3.822 12.305 4.846 1.00 23.99 N
ANISOU 1299 NE2 GLN A 161 3101 2252 3758 -959 -254 311 N
ATOM 1300 C GLN A 161 -4.259 8.018 7.731 1.00 11.23 C
ANISOU 1300 C GLN A 161 1558 1466 1241 143 53 -33 C
ATOM 1301 O GLN A 161 -3.997 7.006 7.062 1.00 11.45 O
ANISOU 1301 O GLN A 161 1434 1425 1490 113 118 -130 O
ATOM 1302 N GLY A 162 -5.511 8.388 8.002 1.00 10.62 N
ANISOU 1302 N GLY A 162 1479 1343 1212 31 -20 3 N
ATOM 1303 CA GLY A 162 -6.662 7.587 7.568 1.00 10.49 C
ANISOU 1303 CA GLY A 162 1331 1413 1238 44 83 -24 C
ATOM 1304 C GLY A 162 -6.671 7.323 6.069 1.00 11.51 C
ANISOU 1304 C GLY A 162 1731 1404 1238 -182 110 -40 C
ATOM 1305 O GLY A 162 -6.939 6.187 5.631 1.00 11.36 O
ANISOU 1305 O GLY A 162 1666 1425 1224 -211 86 -113 O
ATOM 1306 N THR A 163 -6.416 8.363 5.258 1.00 11.43 N
ANISOU 1306 N THR A 163 1584 1506 1252 -273 60 57 N
ATOM 1307 CA THR A 163 -6.434 8.175 3.805 1.00 12.54 C
ANISOU 1307 CA THR A 163 1767 1713 1283 -290 157 59 C
ATOM 1308 CB THR A 163 -6.351 9.502 3.049 1.00 13.32 C
ANISOU 1308 CB THR A 163 1778 1817 1466 -361 59 188 C
ATOM 1309 OG1 THR A 163 -5.093 10.128 3.325 1.00 14.85 O
ANISOU 1309 OG1 THR A 163 1853 1748 2040 -395 -87 175 O
ATOM 1310 CG2 THR A 163 -7.523 10.438 3.336 1.00 13.44 C
ANISOU 1310 CG2 THR A 163 1695 2040 1372 -338 34 315 C
ATOM 1311 C THR A 163 -5.294 7.261 3.328 1.00 11.99 C
ANISOU 1311 C THR A 163 1821 1619 1112 -325 47 69 C
ATOM 1312 O THR A 163 -5.296 6.848 2.150 1.00 13.13 O
ANISOU 1312 O THR A 163 1814 2064 1110 -370 -58 -49 O
ATOM 1313 N GLU A 164 -4.348 6.933 4.229 1.00 11.41 N
ANISOU 1313 N GLU A 164 1771 1491 1073 -206 75 -6 N
ATOM 1314 CA GLU A 164 -3.251 6.039 3.904 1.00 12.82 C
ANISOU 1314 CA GLU A 164 1771 1892 1206 -180 167 -181 C
ATOM 1315 CB GLU A 164 -1.920 6.663 4.309 1.00 14.27 C
ANISOU 1315 CB GLU A 164 1888 2151 1381 -312 17 -238 C
ATOM 1316 CG GLU A 164 -1.672 8.011 3.670 1.00 15.50 C
ANISOU 1316 CG GLU A 164 1938 2174 1777 -489 -89 -274 C
ATOM 1317 CD GLU A 164 -1.287 7.988 2.203 1.00 19.81 C
ANISOU 1317 CD GLU A 164 3051 2545 1930 -633 67 208 C
ATOM 1318 OE1 GLU A 164 -1.245 6.934 1.627 1.00 19.33 O
ANISOU 1318 OE1 GLU A 164 2784 3021 1538 -916 195 -265 O
ATOM 1319 OE2 GLU A 164 -0.974 9.067 1.662 1.00 28.61 O
ANISOU 1319 OE2 GLU A 164 4830 3148 2893 -1426 -40 810 O
ATOM 1320 C GLU A 164 -3.408 4.670 4.578 1.00 12.71 C
ANISOU 1320 C GLU A 164 1782 1740 1305 -238 199 -253 C
ATOM 1321 O GLU A 164 -2.492 3.852 4.527 1.00 16.49 O
ANISOU 1321 O GLU A 164 2217 2169 1880 87 523 32 O
ATOM 1322 N SER A 165 -4.551 4.427 5.238 1.00 11.93 N
ANISOU 1322 N SER A 165 1682 1502 1349 49 172 3 N
ATOM 1323 CA SER A 165 -4.748 3.228 6.091 1.00 11.62 C
ANISOU 1323 CA SER A 165 1780 1325 1310 103 90 -137 C
ATOM 1324 CB SER A 165 -4.916 3.623 7.532 1.00 12.28 C
ANISOU 1324 CB SER A 165 1844 1492 1330 -82 294 -146 C
ATOM 1325 OG SER A 165 -3.742 4.263 8.032 1.00 14.14 O
ANISOU 1325 OG SER A 165 2160 1773 1437 -169 0 -126 O
ATOM 1326 C SER A 165 -6.005 2.487 5.618 1.00 12.63 C
ANISOU 1326 C SER A 165 1836 1461 1499 119 -27 -104 C
ATOM 1327 O SER A 165 -7.102 2.979 5.754 1.00 13.49 O
ANISOU 1327 O SER A 165 1758 1446 1921 -43 87 -378 O
ATOM 1328 N ATHR A 166 -5.817 1.303 5.043 0.50 12.61 N
ANISOU 1328 N ATHR A 166 1819 1423 1549 216 55 -55 N
ATOM 1329 N BTHR A 166 -5.838 1.304 5.017 0.50 12.22 N
ANISOU 1329 N BTHR A 166 1618 1503 1520 416 -13 -80 N
ATOM 1330 CA ATHR A 166 -6.927 0.468 4.590 0.50 13.30 C
ANISOU 1330 CA ATHR A 166 2106 1410 1537 89 -21 -15 C
ATOM 1331 CA BTHR A 166 -7.010 0.494 4.596 0.50 12.71 C
ANISOU 1331 CA BTHR A 166 1778 1581 1468 380 -115 -92 C
ATOM 1332 CB ATHR A 166 -6.398 -0.625 3.662 0.50 14.18 C
ANISOU 1332 CB ATHR A 166 2432 1427 1525 92 203 89 C
ATOM 1333 CB BTHR A 166 -6.676 -0.679 3.673 0.50 12.95 C
ANISOU 1333 CB BTHR A 166 1739 1786 1396 610 4 -54 C
ATOM 1334 OG1ATHR A 166 -5.814 0.011 2.518 0.50 16.39 O
ANISOU 1334 OG1ATHR A 166 2849 1663 1714 -305 279 168 O
ATOM 1335 OG1BTHR A 166 -5.719 -1.517 4.333 0.50 13.50 O
ANISOU 1335 OG1BTHR A 166 1681 2093 1353 823 -85 -305 O
ATOM 1336 CG2ATHR A 166 -7.481 -1.573 3.219 0.50 14.10 C
ANISOU 1336 CG2ATHR A 166 2269 1534 1553 72 246 109 C
ATOM 1337 CG2BTHR A 166 -6.178 -0.205 2.324 0.50 14.02 C
ANISOU 1337 CG2BTHR A 166 1942 1994 1391 536 -9 -6 C
ATOM 1338 C ATHR A 166 -7.704 -0.095 5.790 0.50 12.18 C
ANISOU 1338 C ATHR A 166 1945 1241 1441 185 -53 -108 C
ATOM 1339 C BTHR A 166 -7.736 -0.083 5.809 0.50 12.30 C
ANISOU 1339 C BTHR A 166 1807 1357 1510 318 -76 -147 C
ATOM 1340 O ATHR A 166 -8.920 -0.286 5.727 0.50 13.05 O
ANISOU 1340 O ATHR A 166 1943 1490 1522 172 -106 -32 O
ATOM 1341 O BTHR A 166 -8.951 -0.279 5.758 0.50 13.03 O
ANISOU 1341 O BTHR A 166 1805 1582 1563 285 -135 -22 O
ATOM 1342 N ASP A 167 -6.987 -0.364 6.879 1.00 12.32 N
ANISOU 1342 N ASP A 167 1970 1352 1359 87 -135 -219 N
ATOM 1343 CA ASP A 167 -7.563 -0.931 8.104 1.00 12.89 C
ANISOU 1343 CA ASP A 167 2270 1234 1390 -6 -198 -137 C
ATOM 1344 CB ASP A 167 -6.912 -2.261 8.462 1.00 15.84 C
ANISOU 1344 CB ASP A 167 3172 1119 1726 171 -145 -371 C
ATOM 1345 CG ASP A 167 -7.472 -2.970 9.692 1.00 20.97 C
ANISOU 1345 CG ASP A 167 4014 1592 2361 -260 -77 49 C
ATOM 1346 OD1 ASP A 167 -8.298 -2.347 10.471 1.00 21.16 O
ANISOU 1346 OD1 ASP A 167 3768 1442 2826 -292 -671 -188 O
ATOM 1347 OD2 ASP A 167 -7.051 -4.153 9.883 1.00 28.08 O
ANISOU 1347 OD2 ASP A 167 5177 2044 3447 326 -335 250 O
ATOM 1348 C ASP A 167 -7.327 0.049 9.254 1.00 12.08 C
ANISOU 1348 C ASP A 167 2117 1261 1209 65 -208 -79 C
ATOM 1349 O ASP A 167 -6.163 0.230 9.697 1.00 12.54 O
ANISOU 1349 O ASP A 167 1867 1453 1443 238 44 -194 O
ATOM 1350 N SER A 168 -8.412 0.672 9.725 1.00 11.73 N
ANISOU 1350 N SER A 168 1890 1331 1234 -147 -200 -123 N
ATOM 1351 CA SER A 168 -8.318 1.710 10.728 1.00 11.83 C
ANISOU 1351 CA SER A 168 1839 1244 1408 -152 -110 -139 C
ATOM 1352 CB SER A 168 -9.674 2.264 11.062 1.00 12.31 C
ANISOU 1352 CB SER A 168 1904 1269 1502 -65 -37 -109 C
ATOM 1353 OG SER A 168 -10.487 1.275 11.671 1.00 13.55 O
ANISOU 1353 OG SER A 168 1718 1749 1680 -105 187 -18 O
ATOM 1354 C SER A 168 -7.594 1.251 12.007 1.00 11.87 C
ANISOU 1354 C SER A 168 1681 1308 1521 9 -156 -197 C
ATOM 1355 O SER A 168 -6.944 2.073 12.669 1.00 11.96 O
ANISOU 1355 O SER A 168 1820 1259 1462 -110 -192 -188 O
ATOM 1356 N ARG A 169 -7.678 -0.026 12.358 1.00 12.30 N
ANISOU 1356 N ARG A 169 1682 1415 1576 -36 -148 9 N
ATOM 1357 CA ARG A 169 -7.097 -0.468 13.652 1.00 13.84 C
ANISOU 1357 CA ARG A 169 2151 1558 1546 -10 -163 76 C
ATOM 1358 CB ARG A 169 -7.571 -1.881 14.014 1.00 19.49 C
ANISOU 1358 CB ARG A 169 3000 1906 2498 -335 -463 580 C
ATOM 1359 CG ARG A 169 -6.889 -3.012 13.277 1.00 27.09 C
ANISOU 1359 CG ARG A 169 3949 3096 3247 -146 -179 274 C
ATOM 1360 CD ARG A 169 -7.607 -4.345 13.480 1.00 35.18 C
ANISOU 1360 CD ARG A 169 5377 3567 4420 -615 319 939 C
ATOM 1361 NE ARG A 169 -6.891 -5.286 14.342 1.00 39.89 N
ANISOU 1361 NE ARG A 169 5916 5186 4055 48 772 1264 N
ATOM 1362 CZ ARG A 169 -5.941 -6.109 13.903 1.00 47.58 C
ANISOU 1362 CZ ARG A 169 6744 5941 5392 310 997 241 C
ATOM 1363 NH1 ARG A 169 -5.566 -6.064 12.631 1.00 53.00 N
ANISOU 1363 NH1 ARG A 169 7074 7267 5793 -1035 1961 -689 N
ATOM 1364 NH2 ARG A 169 -5.394 -6.985 14.725 1.00 48.81 N
ANISOU 1364 NH2 ARG A 169 5769 6795 5980 450 -192 -343 N
ATOM 1365 C ARG A 169 -5.565 -0.366 13.630 1.00 12.47 C
ANISOU 1365 C ARG A 169 2118 1356 1263 -4 -170 110 C
ATOM 1366 O ARG A 169 -4.925 -0.350 14.695 1.00 13.15 O
ANISOU 1366 O ARG A 169 2079 1709 1206 207 -194 -88 O
ATOM 1367 N MET A 170 -4.950 -0.262 12.447 1.00 11.38 N
ANISOU 1367 N MET A 170 1726 1245 1352 128 -33 -51 N
ATOM 1368 CA AMET A 170 -3.475 -0.190 12.337 0.50 11.56 C
ANISOU 1368 CA AMET A 170 1680 1207 1502 221 -8 -26 C
ATOM 1369 CA BMET A 170 -3.476 -0.195 12.352 0.50 11.42 C
ANISOU 1369 CA BMET A 170 1672 1190 1476 230 -9 -37 C
ATOM 1370 CB AMET A 170 -3.016 -0.541 10.922 0.50 13.46 C
ANISOU 1370 CB AMET A 170 2052 1475 1585 194 59 -129 C
ATOM 1371 CB BMET A 170 -2.994 -0.595 10.960 0.50 12.92 C
ANISOU 1371 CB BMET A 170 1994 1368 1545 189 25 -156 C
ATOM 1372 CG AMET A 170 -3.398 -1.928 10.495 0.50 14.66 C
ANISOU 1372 CG AMET A 170 2262 1411 1894 267 -32 -94 C
ATOM 1373 CG BMET A 170 -3.439 -1.973 10.550 0.50 13.93 C
ANISOU 1373 CG BMET A 170 2156 1294 1841 280 -62 -151 C
ATOM 1374 SD AMET A 170 -2.454 -3.131 11.438 0.50 14.76 S
ANISOU 1374 SD AMET A 170 2113 1556 1938 148 -242 -112 S
ATOM 1375 SD BMET A 170 -2.949 -3.246 11.735 0.50 13.50 S
ANISOU 1375 SD BMET A 170 2043 1201 1885 105 -158 -188 S
ATOM 1376 CE AMET A 170 -3.740 -3.734 12.537 0.50 17.13 C
ANISOU 1376 CE AMET A 170 2723 1464 2321 27 -58 127 C
ATOM 1377 CE BMET A 170 -3.230 -4.667 10.681 0.50 13.19 C
ANISOU 1377 CE BMET A 170 1999 961 2051 86 -491 -85 C
ATOM 1378 C MET A 170 -2.936 1.210 12.657 1.00 11.17 C
ANISOU 1378 C MET A 170 1504 1300 1439 131 58 -12 C
ATOM 1379 O MET A 170 -1.732 1.376 12.871 1.00 12.46 O
ANISOU 1379 O MET A 170 1530 1502 1700 249 50 -93 O
ATOM 1380 N SER A 171 -3.815 2.214 12.645 1.00 11.18 N
ANISOU 1380 N SER A 171 1436 1317 1494 55 31 -210 N
ATOM 1381 CA SER A 171 -3.384 3.613 12.669 1.00 11.22 C
ANISOU 1381 CA SER A 171 1467 1258 1537 88 20 -214 C
ATOM 1382 CB SER A 171 -4.101 4.401 11.606 1.00 11.88 C
ANISOU 1382 CB SER A 171 1613 1329 1572 -89 -64 -91 C
ATOM 1383 OG SER A 171 -3.751 5.775 11.668 1.00 11.91 O
ANISOU 1383 OG SER A 171 1804 1337 1383 -119 -237 -116 O
ATOM 1384 C SER A 171 -3.591 4.276 14.030 1.00 10.70 C
ANISOU 1384 C SER A 171 1460 1177 1425 -56 -97 -116 C
ATOM 1385 O SER A 171 -4.697 4.250 14.588 1.00 11.64 O
ANISOU 1385 O SER A 171 1604 1157 1662 -141 51 -142 O
ATOM 1386 N ARG A 172 -2.535 4.948 14.492 1.00 9.83 N
ANISOU 1386 N ARG A 172 1477 1103 1154 -53 -1 -188 N
ATOM 1387 CA ARG A 172 -2.605 5.948 15.570 1.00 9.83 C
ANISOU 1387 CA ARG A 172 1558 1079 1096 -116 126 -165 C
ATOM 1388 CB ARG A 172 -1.557 5.648 16.643 1.00 10.07 C
ANISOU 1388 CB ARG A 172 1489 1133 1204 -188 105 -281 C
ATOM 1389 CG ARG A 172 -1.593 4.232 17.191 1.00 10.69 C
ANISOU 1389 CG ARG A 172 1547 1159 1354 -198 177 -267 C
ATOM 1390 CD ARG A 172 -0.749 4.050 18.456 1.00 10.44 C
ANISOU 1390 CD ARG A 172 1489 1113 1364 -121 146 -416 C
ATOM 1391 NE ARG A 172 0.632 4.479 18.304 1.00 10.64 N
ANISOU 1391 NE ARG A 172 1562 1060 1420 -175 155 -297 N
ATOM 1392 CZ ARG A 172 1.680 3.701 18.015 1.00 10.07 C
ANISOU 1392 CZ ARG A 172 1538 993 1291 -118 27 -249 C
ATOM 1393 NH1 ARG A 172 1.520 2.395 17.784 1.00 10.70 N
ANISOU 1393 NH1 ARG A 172 1654 1048 1360 -108 -22 -407 N
ATOM 1394 NH2 ARG A 172 2.889 4.270 17.903 1.00 11.06 N
ANISOU 1394 NH2 ARG A 172 1715 1080 1406 -290 29 -71 N
ATOM 1395 C ARG A 172 -2.398 7.355 15.000 1.00 10.32 C
ANISOU 1395 C ARG A 172 1485 1237 1199 -178 47 -38 C
ATOM 1396 O ARG A 172 -2.059 8.289 15.750 1.00 11.07 O
ANISOU 1396 O ARG A 172 1646 1231 1327 -234 66 -49 O
ATOM 1397 N GLY A 173 -2.587 7.481 13.675 1.00 10.49 N
ANISOU 1397 N GLY A 173 1618 1184 1182 -168 39 -59 N
ATOM 1398 CA GLY A 173 -2.290 8.705 12.967 1.00 10.42 C
ANISOU 1398 CA GLY A 173 1408 1291 1260 -210 186 -18 C
ATOM 1399 C GLY A 173 -3.481 9.645 12.900 1.00 10.77 C
ANISOU 1399 C GLY A 173 1452 1257 1380 -152 147 -83 C
ATOM 1400 O GLY A 173 -4.557 9.367 13.428 1.00 10.73 O
ANISOU 1400 O GLY A 173 1254 1344 1478 -124 55 -41 O
ATOM 1401 N LEU A 174 -3.255 10.777 12.234 1.00 11.15 N
ANISOU 1401 N LEU A 174 1519 1289 1428 -24 139 -45 N
ATOM 1402 CA LEU A 174 -4.288 11.784 12.085 1.00 11.26 C
ANISOU 1402 CA LEU A 174 1635 1086 1556 11 67 -108 C
ATOM 1403 CB LEU A 174 -3.637 13.087 11.613 1.00 11.84 C
ANISOU 1403 CB LEU A 174 1747 1159 1591 29 180 -71 C
ATOM 1404 CG LEU A 174 -2.497 13.609 12.501 1.00 12.87 C
ANISOU 1404 CG LEU A 174 1757 1227 1905 -64 169 -139 C
ATOM 1405 CD1 LEU A 174 -1.931 14.884 11.917 1.00 15.91 C
ANISOU 1405 CD1 LEU A 174 2245 1279 2518 -282 -6 -120 C
ATOM 1406 CD2 LEU A 174 -2.939 13.782 13.945 1.00 13.94 C
ANISOU 1406 CD2 LEU A 174 2040 1264 1991 12 173 -207 C
ATOM 1407 C LEU A 174 -5.363 11.308 11.106 1.00 11.60 C
ANISOU 1407 C LEU A 174 1639 1246 1521 7 59 -69 C
ATOM 1408 O LEU A 174 -5.149 10.478 10.225 1.00 12.80 O
ANISOU 1408 O LEU A 174 1695 1672 1495 60 37 -260 O
ATOM 1409 N GLY A 175 -6.558 11.861 11.253 1.00 10.62 N
ANISOU 1409 N GLY A 175 1506 1154 1376 -140 98 -30 N
ATOM 1410 CA GLY A 175 -7.626 11.650 10.280 1.00 11.02 C
ANISOU 1410 CA GLY A 175 1529 1290 1365 -130 53 22 C
ATOM 1411 C GLY A 175 -8.047 10.203 10.131 1.00 10.93 C
ANISOU 1411 C GLY A 175 1526 1249 1375 -6 -40 -56 C
ATOM 1412 O GLY A 175 -8.422 9.777 9.036 1.00 11.67 O
ANISOU 1412 O GLY A 175 1818 1171 1445 -2 16 -191 O
ATOM 1413 N CYS A 176 -8.039 9.444 11.227 1.00 10.35 N
ANISOU 1413 N CYS A 176 1596 1208 1129 -91 -49 -209 N
ATOM 1414 CA CYS A 176 -8.379 8.028 11.152 1.00 11.28 C
ANISOU 1414 CA CYS A 176 1732 1130 1421 -38 68 -137 C
ATOM 1415 CB CYS A 176 -7.154 7.119 11.136 1.00 12.00 C
ANISOU 1415 CB CYS A 176 1741 1228 1589 -61 -29 -36 C
ATOM 1416 SG CYS A 176 -7.561 5.426 10.645 1.00 12.18 S
ANISOU 1416 SG CYS A 176 1825 1260 1541 2 76 -114 S
ATOM 1417 C CYS A 176 -9.368 7.641 12.250 1.00 10.66 C
ANISOU 1417 C CYS A 176 1652 1061 1334 52 31 -153 C
ATOM 1418 O CYS A 176 -10.579 7.485 11.946 1.00 12.31 O
ANISOU 1418 O CYS A 176 1590 1680 1406 -94 152 194 O
ATOM 1419 N ASN A 177 -8.899 7.530 13.509 1.00 10.41 N
ANISOU 1419 N ASN A 177 1427 1216 1311 -26 44 -192 N
ATOM 1420 CA ASN A 177 -9.777 7.070 14.595 1.00 10.61 C
ANISOU 1420 CA ASN A 177 1657 1104 1267 -31 30 -163 C
ATOM 1421 CB ASN A 177 -9.129 5.909 15.353 1.00 10.57 C
ANISOU 1421 CB ASN A 177 1814 970 1232 -164 -6 -80 C
ATOM 1422 CG ASN A 177 -8.836 4.740 14.434 1.00 10.01 C
ANISOU 1422 CG ASN A 177 1433 961 1406 -101 -47 -142 C
ATOM 1423 OD1 ASN A 177 -9.700 4.386 13.615 1.00 12.00 O
ANISOU 1423 OD1 ASN A 177 1447 1426 1686 -58 -179 -438 O
ATOM 1424 ND2 ASN A 177 -7.654 4.157 14.562 1.00 11.43 N
ANISOU 1424 ND2 ASN A 177 1616 1179 1546 68 -120 -20 N
ATOM 1425 C ASN A 177 -10.177 8.181 15.576 1.00 10.36 C
ANISOU 1425 C ASN A 177 1674 1070 1193 -141 42 -142 C
ATOM 1426 O ASN A 177 -11.112 7.941 16.377 1.00 11.60 O
ANISOU 1426 O ASN A 177 1892 1274 1242 -200 125 -31 O
ATOM 1427 N TYR A 178 -9.434 9.310 15.583 1.00 10.10 N
ANISOU 1427 N TYR A 178 1444 1100 1292 -131 99 -265 N
ATOM 1428 CA TYR A 178 -9.704 10.368 16.553 1.00 10.55 C
ANISOU 1428 CA TYR A 178 1593 1105 1310 -121 167 -258 C
ATOM 1429 CB TYR A 178 -8.679 10.364 17.699 1.00 10.91 C
ANISOU 1429 CB TYR A 178 1682 1181 1281 -244 146 -171 C
ATOM 1430 CG TYR A 178 -7.239 10.478 17.263 1.00 11.18 C
ANISOU 1430 CG TYR A 178 1676 1172 1399 -212 141 -183 C
ATOM 1431 CD1 TYR A 178 -6.662 11.705 16.947 1.00 10.99 C
ANISOU 1431 CD1 TYR A 178 1684 1163 1327 -242 57 -197 C
ATOM 1432 CE1 TYR A 178 -5.358 11.803 16.487 1.00 10.21 C
ANISOU 1432 CE1 TYR A 178 1621 963 1294 -236 31 -178 C
ATOM 1433 CZ TYR A 178 -4.572 10.665 16.385 1.00 10.37 C
ANISOU 1433 CZ TYR A 178 1671 1067 1201 -137 176 -265 C
ATOM 1434 OH TYR A 178 -3.270 10.759 15.952 1.00 11.64 O
ANISOU 1434 OH TYR A 178 1685 1282 1453 -297 107 -30 O
ATOM 1435 CE2 TYR A 178 -5.135 9.439 16.698 1.00 10.45 C
ANISOU 1435 CE2 TYR A 178 1583 1162 1225 -232 88 -228 C
ATOM 1436 CD2 TYR A 178 -6.454 9.360 17.120 1.00 9.96 C
ANISOU 1436 CD2 TYR A 178 1665 955 1163 -318 88 -113 C
ATOM 1437 C TYR A 178 -9.777 11.721 15.848 1.00 10.55 C
ANISOU 1437 C TYR A 178 1499 1169 1338 -70 155 -190 C
ATOM 1438 O TYR A 178 -9.152 11.949 14.800 1.00 11.23 O
ANISOU 1438 O TYR A 178 1708 1272 1286 -44 124 -172 O
ATOM 1439 N ALA A 179 -10.527 12.640 16.466 1.00 10.70 N
ANISOU 1439 N ALA A 179 1822 1046 1195 -88 178 -146 N
ATOM 1440 CA ALA A 179 -10.638 13.993 15.941 1.00 10.89 C
ANISOU 1440 CA ALA A 179 1732 1055 1351 -86 169 -153 C
ATOM 1441 CB ALA A 179 -11.794 14.690 16.626 1.00 11.36 C
ANISOU 1441 CB ALA A 179 1668 1201 1446 -62 207 -159 C
ATOM 1442 C ALA A 179 -9.340 14.778 16.149 1.00 10.83 C
ANISOU 1442 C ALA A 179 1683 1170 1259 -81 82 -142 C
ATOM 1443 O ALA A 179 -8.653 14.647 17.159 1.00 10.95 O
ANISOU 1443 O ALA A 179 1676 1135 1347 -161 73 -156 O
ATOM 1444 N TYR A 180 -9.036 15.653 15.185 1.00 10.70 N
ANISOU 1444 N TYR A 180 1651 1190 1222 -53 -17 -108 N
ATOM 1445 CA TYR A 180 -7.807 16.427 15.209 1.00 11.64 C
ANISOU 1445 CA TYR A 180 1808 1124 1489 -73 -70 -111 C
ATOM 1446 CB TYR A 180 -6.615 15.593 14.691 1.00 10.70 C
ANISOU 1446 CB TYR A 180 1651 1175 1236 -201 40 -250 C
ATOM 1447 CG TYR A 180 -6.607 15.555 13.191 1.00 11.26 C
ANISOU 1447 CG TYR A 180 1765 1231 1280 -147 61 -154 C
ATOM 1448 CD1 TYR A 180 -7.606 14.876 12.512 1.00 11.25 C
ANISOU 1448 CD1 TYR A 180 1722 1099 1451 -136 107 -108 C
ATOM 1449 CE1 TYR A 180 -7.717 14.950 11.139 1.00 12.02 C
ANISOU 1449 CE1 TYR A 180 1844 1274 1447 -55 98 -274 C
ATOM 1450 CZ TYR A 180 -6.817 15.722 10.420 1.00 12.84 C
ANISOU 1450 CZ TYR A 180 2137 1433 1307 -227 109 -240 C
ATOM 1451 OH TYR A 180 -6.987 15.856 9.066 1.00 14.02 O
ANISOU 1451 OH TYR A 180 2477 1490 1357 -226 -74 -84 O
ATOM 1452 CE2 TYR A 180 -5.787 16.389 11.076 1.00 12.50 C
ANISOU 1452 CE2 TYR A 180 2115 1382 1249 -32 1 -172 C
ATOM 1453 CD2 TYR A 180 -5.706 16.311 12.458 1.00 11.15 C
ANISOU 1453 CD2 TYR A 180 1834 1216 1186 -252 85 -342 C
ATOM 1454 C TYR A 180 -8.000 17.673 14.342 1.00 10.92 C
ANISOU 1454 C TYR A 180 1705 1095 1349 1 -36 -207 C
ATOM 1455 O TYR A 180 -8.893 17.721 13.479 1.00 11.91 O
ANISOU 1455 O TYR A 180 1590 1365 1569 -143 -77 -46 O
ATOM 1456 N TYR A 181 -7.113 18.644 14.548 1.00 11.44 N
ANISOU 1456 N TYR A 181 1910 1076 1357 -136 64 -245 N
ATOM 1457 CA TYR A 181 -7.032 19.794 13.652 1.00 12.29 C
ANISOU 1457 CA TYR A 181 2026 1153 1490 -182 -75 -145 C
ATOM 1458 CB TYR A 181 -7.998 20.907 14.056 1.00 13.73 C
ANISOU 1458 CB TYR A 181 2277 1098 1841 -199 -18 -92 C
ATOM 1459 CG TYR A 181 -7.904 22.100 13.150 1.00 15.77 C
ANISOU 1459 CG TYR A 181 2333 1468 2190 -269 203 183 C
ATOM 1460 CD1 TYR A 181 -8.273 22.008 11.825 1.00 16.30 C
ANISOU 1460 CD1 TYR A 181 2265 1621 2304 -101 -22 406 C
ATOM 1461 CE1 TYR A 181 -8.127 23.082 10.967 1.00 18.74 C
ANISOU 1461 CE1 TYR A 181 2490 1941 2686 56 127 791 C
ATOM 1462 CZ TYR A 181 -7.632 24.288 11.442 1.00 19.68 C
ANISOU 1462 CZ TYR A 181 2786 1527 3164 113 -69 824 C
ATOM 1463 OH TYR A 181 -7.468 25.375 10.608 1.00 23.81 O
ANISOU 1463 OH TYR A 181 2848 2461 3735 -312 10 1514 O
ATOM 1464 CE2 TYR A 181 -7.270 24.391 12.777 1.00 18.98 C
ANISOU 1464 CE2 TYR A 181 2664 1263 3285 -37 -118 642 C
ATOM 1465 CD2 TYR A 181 -7.392 23.288 13.610 1.00 16.84 C
ANISOU 1465 CD2 TYR A 181 2425 1309 2661 -289 -99 319 C
ATOM 1466 C TYR A 181 -5.604 20.334 13.657 1.00 11.97 C
ANISOU 1466 C TYR A 181 2003 1034 1511 -132 143 -167 C
ATOM 1467 O TYR A 181 -5.101 20.730 14.702 1.00 12.86 O
ANISOU 1467 O TYR A 181 2032 1393 1459 -209 -10 -93 O
ATOM 1468 N ILE A 182 -4.988 20.392 12.475 1.00 13.88 N
ANISOU 1468 N ILE A 182 2200 1623 1450 -381 164 -216 N
ATOM 1469 CA ILE A 182 -3.677 21.004 12.299 1.00 15.22 C
ANISOU 1469 CA ILE A 182 2152 1703 1928 -370 269 -224 C
ATOM 1470 CB ILE A 182 -2.851 20.338 11.192 1.00 19.17 C
ANISOU 1470 CB ILE A 182 2515 2303 2464 -430 719 -387 C
ATOM 1471 CG1 ILE A 182 -2.695 18.845 11.411 1.00 20.91 C
ANISOU 1471 CG1 ILE A 182 2444 2210 3290 -719 919 -518 C
ATOM 1472 CG2 ILE A 182 -1.506 21.030 11.056 1.00 18.18 C
ANISOU 1472 CG2 ILE A 182 2468 1989 2447 -381 732 -765 C
ATOM 1473 CD1 ILE A 182 -2.227 18.137 10.197 1.00 25.08 C
ANISOU 1473 CD1 ILE A 182 3224 3124 3180 -604 839 -504 C
ATOM 1474 C ILE A 182 -3.856 22.484 11.968 1.00 15.02 C
ANISOU 1474 C ILE A 182 2179 1721 1804 -518 286 -8 C
ATOM 1475 O ILE A 182 -4.512 22.834 10.986 1.00 17.68 O
ANISOU 1475 O ILE A 182 2495 2355 1864 -463 131 67 O
ATOM 1476 N HIS A 183 -3.268 23.348 12.797 1.00 15.11 N
ANISOU 1476 N HIS A 183 2392 1370 1979 -314 -102 187 N
ATOM 1477 CA HIS A 183 -3.335 24.764 12.541 1.00 16.09 C
ANISOU 1477 CA HIS A 183 2625 1441 2046 -343 231 261 C
ATOM 1478 CB HIS A 183 -2.748 25.526 13.720 1.00 17.05 C
ANISOU 1478 CB HIS A 183 2799 1427 2251 -338 240 -41 C
ATOM 1479 CG HIS A 183 -3.430 25.388 15.043 1.00 17.25 C
ANISOU 1479 CG HIS A 183 2745 1556 2251 -475 275 -120 C
ATOM 1480 ND1 HIS A 183 -4.049 24.262 15.535 1.00 19.94 N
ANISOU 1480 ND1 HIS A 183 2912 2213 2451 -542 322 351 N
ATOM 1481 CE1 HIS A 183 -4.499 24.522 16.766 1.00 16.90 C
ANISOU 1481 CE1 HIS A 183 2604 1350 2465 -701 566 769 C
ATOM 1482 NE2 HIS A 183 -4.115 25.754 17.104 1.00 22.20 N
ANISOU 1482 NE2 HIS A 183 3447 2149 2837 -636 262 318 N
ATOM 1483 CD2 HIS A 183 -3.465 26.309 16.038 1.00 16.76 C
ANISOU 1483 CD2 HIS A 183 2711 1157 2497 -574 214 -235 C
ATOM 1484 C HIS A 183 -2.550 25.110 11.283 1.00 16.55 C
ANISOU 1484 C HIS A 183 2512 1636 2140 -293 228 349 C
ATOM 1485 O HIS A 183 -1.528 24.485 10.983 1.00 17.09 O
ANISOU 1485 O HIS A 183 2459 1653 2381 -294 362 393 O
ATOM 1486 N PRO A 184 -2.952 26.150 10.532 1.00 20.96 N
ANISOU 1486 N PRO A 184 2893 2296 2772 -258 447 969 N
ATOM 1487 CA PRO A 184 -2.176 26.575 9.364 1.00 19.77 C
ANISOU 1487 CA PRO A 184 2548 2241 2721 -279 353 1011 C
ATOM 1488 CB PRO A 184 -2.860 27.888 8.968 1.00 23.79 C
ANISOU 1488 CB PRO A 184 3282 2534 3223 -76 303 1282 C
ATOM 1489 CG PRO A 184 -4.289 27.678 9.397 1.00 24.68 C
ANISOU 1489 CG PRO A 184 3212 2794 3370 105 339 1492 C
ATOM 1490 CD PRO A 184 -4.188 26.917 10.707 1.00 23.54 C
ANISOU 1490 CD PRO A 184 3225 2636 3080 77 180 1169 C
ATOM 1491 C PRO A 184 -0.698 26.805 9.697 1.00 18.77 C
ANISOU 1491 C PRO A 184 2598 1938 2593 -292 241 670 C
ATOM 1492 O PRO A 184 -0.367 27.328 10.775 1.00 20.42 O
ANISOU 1492 O PRO A 184 2819 2198 2741 -483 197 524 O
ATOM 1493 N ARG A 185 0.170 26.374 8.781 1.00 19.82 N
ANISOU 1493 N ARG A 185 3004 2252 2272 -604 310 239 N
ATOM 1494 CA ARG A 185 1.616 26.465 8.934 1.00 19.33 C
ANISOU 1494 CA ARG A 185 2829 2001 2512 -491 558 404 C
ATOM 1495 CB ARG A 185 2.278 25.143 8.535 1.00 19.50 C
ANISOU 1495 CB ARG A 185 2920 1987 2499 -562 605 364 C
ATOM 1496 CG ARG A 185 1.879 23.955 9.390 1.00 20.53 C
ANISOU 1496 CG ARG A 185 3200 2113 2485 -611 419 515 C
ATOM 1497 CD ARG A 185 2.401 22.640 8.844 1.00 21.04 C
ANISOU 1497 CD ARG A 185 2794 2281 2918 -511 297 565 C
ATOM 1498 NE ARG A 185 3.852 22.531 8.956 1.00 20.83 N
ANISOU 1498 NE ARG A 185 2656 1962 3293 -629 330 635 N
ATOM 1499 CZ ARG A 185 4.591 21.620 8.338 1.00 18.21 C
ANISOU 1499 CZ ARG A 185 2049 2281 2588 -784 96 388 C
ATOM 1500 NH1 ARG A 185 4.034 20.746 7.499 1.00 20.83 N
ANISOU 1500 NH1 ARG A 185 2875 2057 2982 -684 -208 391 N
ATOM 1501 NH2 ARG A 185 5.892 21.576 8.590 1.00 20.73 N
ANISOU 1501 NH2 ARG A 185 2157 2601 3117 -500 -270 618 N
ATOM 1502 C ARG A 185 2.132 27.593 8.045 1.00 21.67 C
ANISOU 1502 C ARG A 185 3086 2240 2905 -905 394 567 C
ATOM 1503 O ARG A 185 1.800 27.636 6.868 1.00 24.70 O
ANISOU 1503 O ARG A 185 3849 2563 2971 -651 463 765 O
ATOM 1504 N ALA A 186 2.963 28.478 8.620 1.00 21.33 N
ANISOU 1504 N ALA A 186 2895 2097 3110 -657 68 631 N
ATOM 1505 CA ALA A 186 3.518 29.604 7.863 1.00 24.90 C
ANISOU 1505 CA ALA A 186 2991 2507 3959 -867 393 879 C
ATOM 1506 CB ALA A 186 3.895 30.731 8.797 1.00 27.04 C
ANISOU 1506 CB ALA A 186 3138 2598 4537 -466 140 590 C
ATOM 1507 C ALA A 186 4.731 29.134 7.045 1.00 25.03 C
ANISOU 1507 C ALA A 186 3280 2404 3826 -783 696 1090 C
ATOM 1508 O ALA A 186 5.416 28.167 7.432 1.00 23.86 O
ANISOU 1508 O ALA A 186 3257 2467 3339 -807 595 793 O
ATOM 1509 N ALA A 187 5.015 29.834 5.934 1.00 27.77 N
ANISOU 1509 N ALA A 187 3554 3065 3929 -1243 627 1226 N
ATOM 1510 CA ALA A 187 6.218 29.545 5.184 1.00 30.75 C
ANISOU 1510 CA ALA A 187 3856 3666 4161 -1060 565 963 C
ATOM 1511 CB ALA A 187 6.331 30.452 3.980 1.00 32.88 C
ANISOU 1511 CB ALA A 187 4308 4177 4006 -1024 418 1100 C
ATOM 1512 C ALA A 187 7.427 29.708 6.118 1.00 28.54 C
ANISOU 1512 C ALA A 187 3573 3366 3902 -1016 644 939 C
ATOM 1513 O ALA A 187 7.491 30.645 6.899 1.00 30.74 O
ANISOU 1513 O ALA A 187 4019 3138 4520 -1363 844 1186 O
ATOM 1514 N GLY A 188 8.353 28.750 6.051 1.00 26.25 N
ANISOU 1514 N GLY A 188 3438 3161 3373 -1117 651 819 N
ATOM 1515 CA GLY A 188 9.594 28.758 6.813 1.00 24.58 C
ANISOU 1515 CA GLY A 188 3107 2968 3262 -982 863 551 C
ATOM 1516 C GLY A 188 9.440 28.259 8.244 1.00 23.79 C
ANISOU 1516 C GLY A 188 3111 2735 3194 -969 621 478 C
ATOM 1517 O GLY A 188 10.423 28.206 8.986 1.00 25.44 O
ANISOU 1517 O GLY A 188 3149 3197 3318 -1082 425 450 O
ATOM 1518 N SER A 189 8.225 27.884 8.647 1.00 22.82 N
ANISOU 1518 N SER A 189 3159 2506 3005 -1020 743 215 N
ATOM 1519 CA SER A 189 7.988 27.532 10.050 1.00 22.49 C
ANISOU 1519 CA SER A 189 3184 2289 3071 -700 452 507 C
ATOM 1520 CB SER A 189 6.517 27.487 10.390 1.00 22.68 C
ANISOU 1520 CB SER A 189 3236 2401 2978 -672 361 147 C
ATOM 1521 OG SER A 189 5.827 26.570 9.561 1.00 24.80 O
ANISOU 1521 OG SER A 189 3342 2662 3416 -901 546 -236 O
ATOM 1522 C SER A 189 8.683 26.206 10.398 1.00 21.46 C
ANISOU 1522 C SER A 189 3102 1921 3131 -766 798 289 C
ATOM 1523 O SER A 189 8.880 25.340 9.536 1.00 22.29 O
ANISOU 1523 O SER A 189 2802 2208 3458 -870 844 105 O
ATOM 1524 N THR A 190 9.084 26.102 11.664 1.00 20.83 N
ANISOU 1524 N THR A 190 2617 2198 3098 -442 854 182 N
ATOM 1525 CA THR A 190 9.751 24.953 12.223 1.00 19.06 C
ANISOU 1525 CA THR A 190 2253 1879 3109 -428 851 -97 C
ATOM 1526 CB THR A 190 11.149 25.351 12.714 1.00 18.98 C
ANISOU 1526 CB THR A 190 2243 1594 3374 -623 865 -272 C
ATOM 1527 OG1 THR A 190 11.036 26.387 13.704 1.00 21.84 O
ANISOU 1527 OG1 THR A 190 2954 1870 3474 -496 998 -437 O
ATOM 1528 CG2 THR A 190 12.036 25.816 11.577 1.00 21.16 C
ANISOU 1528 CG2 THR A 190 2465 1921 3651 -768 1014 -122 C
ATOM 1529 C THR A 190 8.956 24.345 13.382 1.00 18.38 C
ANISOU 1529 C THR A 190 2252 1765 2967 -495 571 14 C
ATOM 1530 O THR A 190 9.476 23.566 14.173 1.00 17.08 O
ANISOU 1530 O THR A 190 2030 1802 2654 -514 431 -261 O
ATOM 1531 N SER A 191 7.668 24.650 13.432 1.00 19.22 N
ANISOU 1531 N SER A 191 2334 1974 2994 -444 727 635 N
ATOM 1532 CA SER A 191 6.790 24.166 14.465 1.00 17.91 C
ANISOU 1532 CA SER A 191 2216 1921 2668 -330 656 378 C
ATOM 1533 CB SER A 191 6.710 25.136 15.616 1.00 19.60 C
ANISOU 1533 CB SER A 191 2829 1822 2796 -557 553 416 C
ATOM 1534 OG SER A 191 6.200 26.365 15.158 1.00 23.74 O
ANISOU 1534 OG SER A 191 3497 1991 3529 -280 383 328 O
ATOM 1535 C SER A 191 5.409 23.918 13.873 1.00 17.76 C
ANISOU 1535 C SER A 191 2425 1933 2391 -380 453 380 C
ATOM 1536 O SER A 191 5.054 24.490 12.844 1.00 20.15 O
ANISOU 1536 O SER A 191 2630 2692 2332 -649 235 545 O
ATOM 1537 N VAL A 192 4.648 23.066 14.557 1.00 15.54 N
ANISOU 1537 N VAL A 192 2176 1653 2075 -339 343 100 N
ATOM 1538 CA VAL A 192 3.254 22.806 14.186 1.00 15.49 C
ANISOU 1538 CA VAL A 192 2176 1727 1982 -284 393 143 C
ATOM 1539 CB VAL A 192 3.130 21.519 13.346 1.00 17.35 C
ANISOU 1539 CB VAL A 192 2517 1953 2121 -485 269 -39 C
ATOM 1540 CG1 VAL A 192 3.544 20.299 14.132 1.00 16.08 C
ANISOU 1540 CG1 VAL A 192 2359 2005 1743 -442 372 -104 C
ATOM 1541 CG2 VAL A 192 1.755 21.336 12.739 1.00 20.44 C
ANISOU 1541 CG2 VAL A 192 2672 2618 2474 -518 412 -21 C
ATOM 1542 C VAL A 192 2.421 22.764 15.459 1.00 14.86 C
ANISOU 1542 C VAL A 192 2298 1420 1928 -373 339 14 C
ATOM 1543 O VAL A 192 2.928 22.348 16.500 1.00 15.67 O
ANISOU 1543 O VAL A 192 2127 1991 1833 -225 310 35 O
ATOM 1544 N LYS A 193 1.159 23.185 15.343 1.00 14.44 N
ANISOU 1544 N LYS A 193 2205 1586 1692 -301 315 -18 N
ATOM 1545 CA LYS A 193 0.180 23.057 16.420 1.00 13.90 C
ANISOU 1545 CA LYS A 193 1952 1462 1866 -507 309 -49 C
ATOM 1546 CB LYS A 193 -0.424 24.397 16.829 1.00 15.43 C
ANISOU 1546 CB LYS A 193 2081 1535 2248 -454 143 -222 C
ATOM 1547 CG LYS A 193 0.494 25.260 17.679 1.00 18.23 C
ANISOU 1547 CG LYS A 193 2326 2031 2569 -399 -214 -397 C
ATOM 1548 CD LYS A 193 -0.147 26.554 18.108 1.00 20.89 C
ANISOU 1548 CD LYS A 193 2676 2242 3018 21 -368 -598 C
ATOM 1549 CE LYS A 193 0.771 27.404 18.939 1.00 25.91 C
ANISOU 1549 CE LYS A 193 2796 3061 3987 -100 -743 -807 C
ATOM 1550 NZ LYS A 193 0.171 28.729 19.230 1.00 30.27 N
ANISOU 1550 NZ LYS A 193 3456 3464 4581 318 -631 -1059 N
ATOM 1551 C LYS A 193 -0.951 22.142 15.957 1.00 14.05 C
ANISOU 1551 C LYS A 193 2010 1495 1831 -430 18 -40 C
ATOM 1552 O LYS A 193 -1.497 22.345 14.877 1.00 14.82 O
ANISOU 1552 O LYS A 193 2365 1586 1681 -351 231 61 O
ATOM 1553 N ILE A 194 -1.285 21.145 16.796 1.00 12.60 N
ANISOU 1553 N ILE A 194 1888 1388 1510 -249 24 -163 N
ATOM 1554 CA ILE A 194 -2.309 20.177 16.472 1.00 12.84 C
ANISOU 1554 CA ILE A 194 1736 1436 1703 -174 86 -131 C
ATOM 1555 CB ILE A 194 -1.705 18.807 16.104 1.00 13.89 C
ANISOU 1555 CB ILE A 194 1939 1531 1805 -58 -61 -133 C
ATOM 1556 CG1 ILE A 194 -0.611 18.964 15.048 1.00 14.94 C
ANISOU 1556 CG1 ILE A 194 1931 1768 1974 -207 6 -200 C
ATOM 1557 CG2 ILE A 194 -2.792 17.844 15.658 1.00 14.56 C
ANISOU 1557 CG2 ILE A 194 2149 1540 1840 -214 84 -62 C
ATOM 1558 CD1 ILE A 194 0.151 17.712 14.749 1.00 17.63 C
ANISOU 1558 CD1 ILE A 194 2297 1699 2701 -224 -28 -240 C
ATOM 1559 C ILE A 194 -3.253 20.057 17.662 1.00 12.59 C
ANISOU 1559 C ILE A 194 2020 1191 1569 -309 111 -20 C
ATOM 1560 O ILE A 194 -2.804 19.795 18.780 1.00 13.86 O
ANISOU 1560 O ILE A 194 2318 1418 1528 -335 10 -161 O
ATOM 1561 N ASP A 195 -4.544 20.222 17.397 1.00 11.38 N
ANISOU 1561 N ASP A 195 1931 1074 1318 -260 278 17 N
ATOM 1562 CA ASP A 195 -5.570 19.931 18.364 1.00 12.13 C
ANISOU 1562 CA ASP A 195 1869 1262 1475 -453 261 -94 C
ATOM 1563 CB ASP A 195 -6.834 20.749 18.084 1.00 12.78 C
ANISOU 1563 CB ASP A 195 1866 1465 1523 -309 283 -53 C
ATOM 1564 CG ASP A 195 -6.628 22.248 17.971 1.00 13.69 C
ANISOU 1564 CG ASP A 195 2237 1484 1481 -232 289 -39 C
ATOM 1565 OD1 ASP A 195 -5.629 22.785 18.538 1.00 15.23 O
ANISOU 1565 OD1 ASP A 195 2255 1369 2162 -165 294 -306 O
ATOM 1566 OD2 ASP A 195 -7.455 22.874 17.315 1.00 18.07 O
ANISOU 1566 OD2 ASP A 195 2633 1602 2627 -101 -195 86 O
ATOM 1567 C ASP A 195 -5.927 18.445 18.268 1.00 12.40 C
ANISOU 1567 C ASP A 195 1967 1337 1406 -558 292 -174 C
ATOM 1568 O ASP A 195 -6.026 17.904 17.165 1.00 13.13 O
ANISOU 1568 O ASP A 195 2200 1382 1403 -451 139 -139 O
ATOM 1569 N PHE A 196 -6.103 17.816 19.436 1.00 11.96 N
ANISOU 1569 N PHE A 196 1887 1361 1294 -420 288 -223 N
ATOM 1570 CA PHE A 196 -6.509 16.422 19.548 1.00 12.57 C
ANISOU 1570 CA PHE A 196 2018 1331 1424 -323 287 -125 C
ATOM 1571 CB PHE A 196 -5.370 15.606 20.169 1.00 12.77 C
ANISOU 1571 CB PHE A 196 2067 1299 1483 -369 152 -86 C
ATOM 1572 CG PHE A 196 -4.116 15.458 19.336 1.00 12.56 C
ANISOU 1572 CG PHE A 196 2015 1351 1403 -363 48 -238 C
ATOM 1573 CD1 PHE A 196 -3.975 14.399 18.452 1.00 12.50 C
ANISOU 1573 CD1 PHE A 196 2077 1325 1345 -385 126 -175 C
ATOM 1574 CE1 PHE A 196 -2.818 14.223 17.727 1.00 12.74 C
ANISOU 1574 CE1 PHE A 196 1952 1385 1501 -264 -4 -179 C
ATOM 1575 CZ PHE A 196 -1.780 15.104 17.864 1.00 13.52 C
ANISOU 1575 CZ PHE A 196 2094 1546 1495 -407 148 -221 C
ATOM 1576 CD2 PHE A 196 -3.061 16.345 19.458 1.00 12.83 C
ANISOU 1576 CD2 PHE A 196 2055 1186 1632 -285 83 -183 C
ATOM 1577 CE2 PHE A 196 -1.902 16.172 18.721 1.00 13.11 C
ANISOU 1577 CE2 PHE A 196 1923 1470 1586 -633 34 -299 C
ATOM 1578 C PHE A 196 -7.718 16.285 20.469 1.00 12.41 C
ANISOU 1578 C PHE A 196 1942 1209 1563 -351 221 -229 C
ATOM 1579 O PHE A 196 -7.833 17.042 21.453 1.00 12.89 O
ANISOU 1579 O PHE A 196 2301 1162 1432 -330 127 -185 O
ATOM 1580 N VAL A 197 -8.563 15.286 20.175 1.00 11.90 N
ANISOU 1580 N VAL A 197 1994 1218 1309 -364 126 -264 N
ATOM 1581 CA VAL A 197 -9.598 14.830 21.096 1.00 13.22 C
ANISOU 1581 CA VAL A 197 2222 1360 1440 -448 195 -159 C
ATOM 1582 CB VAL A 197 -11.001 15.268 20.687 1.00 14.25 C
ANISOU 1582 CB VAL A 197 2347 1521 1544 -267 183 -131 C
ATOM 1583 CG1 VAL A 197 -12.043 14.814 21.697 1.00 14.63 C
ANISOU 1583 CG1 VAL A 197 2079 1911 1567 -314 59 -337 C
ATOM 1584 CG2 VAL A 197 -11.059 16.767 20.476 1.00 15.78 C
ANISOU 1584 CG2 VAL A 197 2620 1559 1814 -115 196 -166 C
ATOM 1585 C VAL A 197 -9.533 13.300 21.114 1.00 12.55 C
ANISOU 1585 C VAL A 197 2056 1281 1429 -492 229 -194 C
ATOM 1586 O VAL A 197 -9.597 12.670 20.045 1.00 14.01 O
ANISOU 1586 O VAL A 197 2662 1219 1440 -259 422 -168 O
ATOM 1587 N VAL A 198 -9.427 12.711 22.308 1.00 12.18 N
ANISOU 1587 N VAL A 198 2041 1187 1398 -376 281 -232 N
ATOM 1588 CA VAL A 198 -9.392 11.257 22.469 1.00 12.46 C
ANISOU 1588 CA VAL A 198 2084 1164 1485 -259 372 -313 C
ATOM 1589 CB VAL A 198 -7.976 10.761 22.852 1.00 14.66 C
ANISOU 1589 CB VAL A 198 2290 1442 1837 54 413 -292 C
ATOM 1590 CG1 VAL A 198 -7.959 9.274 23.167 1.00 14.81 C
ANISOU 1590 CG1 VAL A 198 2392 1436 1796 50 311 -304 C
ATOM 1591 CG2 VAL A 198 -6.989 11.067 21.756 1.00 17.58 C
ANISOU 1591 CG2 VAL A 198 2436 2109 2132 158 539 -108 C
ATOM 1592 C VAL A 198 -10.388 10.845 23.549 1.00 11.51 C
ANISOU 1592 C VAL A 198 2030 977 1364 -53 353 -175 C
ATOM 1593 O VAL A 198 -10.358 11.417 24.646 1.00 12.97 O
ANISOU 1593 O VAL A 198 2259 1119 1549 -305 264 -318 O
ATOM 1594 N ASP A 199 -11.194 9.821 23.254 1.00 11.35 N
ANISOU 1594 N ASP A 199 2131 1096 1083 -128 312 -134 N
ATOM 1595 CA ASP A 199 -12.183 9.242 24.226 1.00 11.59 C
ANISOU 1595 CA ASP A 199 2234 1068 1099 91 390 -55 C
ATOM 1596 CB ASP A 199 -13.597 9.409 23.666 1.00 14.14 C
ANISOU 1596 CB ASP A 199 2198 1388 1785 62 276 68 C
ATOM 1597 CG ASP A 199 -14.755 8.925 24.496 1.00 15.08 C
ANISOU 1597 CG ASP A 199 2233 1758 1736 200 270 -90 C
ATOM 1598 OD1 ASP A 199 -14.514 8.087 25.360 1.00 17.04 O
ANISOU 1598 OD1 ASP A 199 2546 1838 2089 -44 139 167 O
ATOM 1599 OD2 ASP A 199 -15.932 9.404 24.247 1.00 18.32 O
ANISOU 1599 OD2 ASP A 199 2333 2228 2398 514 89 -93 O
ATOM 1600 C ASP A 199 -11.796 7.781 24.458 1.00 12.46 C
ANISOU 1600 C ASP A 199 2393 987 1354 25 207 -221 C
ATOM 1601 O ASP A 199 -11.974 6.976 23.546 1.00 14.59 O
ANISOU 1601 O ASP A 199 3056 1110 1375 -33 181 -268 O
ATOM 1602 N GLU A 200 -11.226 7.473 25.626 1.00 11.51 N
ANISOU 1602 N GLU A 200 1983 1022 1365 -64 115 -368 N
ATOM 1603 CA GLU A 200 -10.580 6.193 25.923 1.00 10.42 C
ANISOU 1603 CA GLU A 200 1646 1173 1140 -77 154 -312 C
ATOM 1604 CB GLU A 200 -9.062 6.420 26.009 1.00 11.72 C
ANISOU 1604 CB GLU A 200 1678 1316 1459 -153 100 -205 C
ATOM 1605 CG GLU A 200 -8.242 5.181 26.326 1.00 11.68 C
ANISOU 1605 CG GLU A 200 1742 1368 1325 -122 49 -143 C
ATOM 1606 CD GLU A 200 -6.748 5.343 26.060 1.00 11.95 C
ANISOU 1606 CD GLU A 200 1726 1406 1405 -30 89 -169 C
ATOM 1607 OE1 GLU A 200 -6.403 5.965 25.036 1.00 12.98 O
ANISOU 1607 OE1 GLU A 200 1831 1585 1515 -148 28 19 O
ATOM 1608 OE2 GLU A 200 -5.927 4.888 26.895 1.00 11.88 O
ANISOU 1608 OE2 GLU A 200 1747 1427 1339 -147 -15 -276 O
ATOM 1609 C GLU A 200 -11.137 5.645 27.245 1.00 10.50 C
ANISOU 1609 C GLU A 200 1660 1147 1181 -147 147 -229 C
ATOM 1610 O GLU A 200 -11.299 6.394 28.227 1.00 10.90 O
ANISOU 1610 O GLU A 200 1883 1105 1151 34 71 -214 O
ATOM 1611 N ALA A 201 -11.443 4.346 27.277 1.00 10.26 N
ANISOU 1611 N ALA A 201 1743 1138 1018 -136 161 -264 N
ATOM 1612 CA ALA A 201 -11.915 3.715 28.527 1.00 10.71 C
ANISOU 1612 CA ALA A 201 1737 1247 1084 -123 205 -164 C
ATOM 1613 CB ALA A 201 -12.305 2.267 28.282 1.00 11.23 C
ANISOU 1613 CB ALA A 201 1837 1271 1157 -305 315 81 C
ATOM 1614 C ALA A 201 -10.814 3.779 29.588 1.00 10.29 C
ANISOU 1614 C ALA A 201 1635 1091 1181 -132 212 -99 C
ATOM 1615 O ALA A 201 -9.659 3.516 29.297 1.00 11.07 O
ANISOU 1615 O ALA A 201 1600 1533 1074 -96 150 -156 O
ATOM 1616 N LEU A 202 -11.210 4.073 30.835 1.00 10.51 N
ANISOU 1616 N LEU A 202 1523 1239 1231 -39 196 -161 N
ATOM 1617 CA LEU A 202 -10.263 4.076 31.957 1.00 10.71 C
ANISOU 1617 CA LEU A 202 1763 1088 1218 -53 115 -109 C
ATOM 1618 CB LEU A 202 -10.856 4.880 33.116 1.00 11.11 C
ANISOU 1618 CB LEU A 202 1750 1083 1387 -89 142 -179 C
ATOM 1619 CG LEU A 202 -10.054 4.870 34.413 1.00 12.23 C
ANISOU 1619 CG LEU A 202 2027 1256 1364 89 108 -124 C
ATOM 1620 CD1 LEU A 202 -8.658 5.442 34.219 1.00 12.39 C
ANISOU 1620 CD1 LEU A 202 2130 1296 1279 23 0 -156 C
ATOM 1621 CD2 LEU A 202 -10.813 5.630 35.476 1.00 13.79 C
ANISOU 1621 CD2 LEU A 202 2097 1671 1468 71 109 -300 C
ATOM 1622 C LEU A 202 -9.989 2.640 32.398 1.00 10.48 C
ANISOU 1622 C LEU A 202 1666 1085 1232 -86 174 -103 C
ATOM 1623 O LEU A 202 -10.940 1.857 32.653 1.00 11.34 O
ANISOU 1623 O LEU A 202 1638 1261 1410 -79 167 -82 O
ATOM 1624 N VAL A 203 -8.700 2.293 32.483 1.00 10.75 N
ANISOU 1624 N VAL A 203 1701 1168 1215 -114 99 -30 N
ATOM 1625 CA VAL A 203 -8.238 0.984 32.930 1.00 11.10 C
ANISOU 1625 CA VAL A 203 1667 1306 1244 38 70 -16 C
ATOM 1626 CB VAL A 203 -7.123 0.469 32.008 1.00 11.96 C
ANISOU 1626 CB VAL A 203 1940 1359 1243 154 52 -133 C
ATOM 1627 CG1 VAL A 203 -6.556 -0.864 32.493 1.00 13.13 C
ANISOU 1627 CG1 VAL A 203 2092 1315 1582 44 -67 -59 C
ATOM 1628 CG2 VAL A 203 -7.627 0.351 30.573 1.00 12.36 C
ANISOU 1628 CG2 VAL A 203 1936 1323 1436 100 -164 -186 C
ATOM 1629 C VAL A 203 -7.797 1.103 34.386 1.00 11.18 C
ANISOU 1629 C VAL A 203 1597 1451 1200 144 215 -181 C
ATOM 1630 O VAL A 203 -6.642 1.416 34.684 1.00 13.14 O
ANISOU 1630 O VAL A 203 1733 1825 1433 130 144 -229 O
ATOM 1631 N ALA A 204 -8.768 0.902 35.283 1.00 11.39 N
ANISOU 1631 N ALA A 204 1520 1661 1147 5 138 -190 N
ATOM 1632 CA ALA A 204 -8.542 1.103 36.722 1.00 11.40 C
ANISOU 1632 CA ALA A 204 1671 1491 1167 34 0 -95 C
ATOM 1633 CB ALA A 204 -8.614 2.561 37.096 1.00 11.57 C
ANISOU 1633 CB ALA A 204 1561 1571 1262 -63 27 -215 C
ATOM 1634 C ALA A 204 -9.606 0.335 37.498 1.00 11.96 C
ANISOU 1634 C ALA A 204 1758 1564 1222 140 104 36 C
ATOM 1635 O ALA A 204 -10.783 0.527 37.267 1.00 12.82 O
ANISOU 1635 O ALA A 204 1773 1512 1584 -3 -36 78 O
ATOM 1636 N ASN A 205 -9.180 -0.514 38.433 1.00 12.03 N
ANISOU 1636 N ASN A 205 1812 1451 1306 145 47 70 N
ATOM 1637 CA ASN A 205 -10.137 -1.274 39.227 1.00 12.46 C
ANISOU 1637 CA ASN A 205 1933 1612 1188 233 223 -26 C
ATOM 1638 CB ASN A 205 -9.403 -2.058 40.309 1.00 13.62 C
ANISOU 1638 CB ASN A 205 2222 1701 1251 465 325 131 C
ATOM 1639 CG ASN A 205 -8.456 -3.119 39.777 1.00 15.77 C
ANISOU 1639 CG ASN A 205 2571 1716 1705 576 404 16 C
ATOM 1640 OD1 ASN A 205 -7.573 -2.805 38.974 1.00 19.12 O
ANISOU 1640 OD1 ASN A 205 2678 2428 2157 180 385 106 O
ATOM 1641 ND2 ASN A 205 -8.589 -4.335 40.280 1.00 14.88 N
ANISOU 1641 ND2 ASN A 205 2383 1695 1573 317 -157 115 N
ATOM 1642 C ASN A 205 -11.169 -0.336 39.854 1.00 11.47 C
ANISOU 1642 C ASN A 205 1781 1479 1099 135 85 -111 C
ATOM 1643 O ASN A 205 -10.793 0.701 40.389 1.00 12.66 O
ANISOU 1643 O ASN A 205 1730 1582 1497 -15 72 -258 O
ATOM 1644 N PRO A 206 -12.479 -0.666 39.805 1.00 11.98 N
ANISOU 1644 N PRO A 206 1854 1436 1259 109 203 -169 N
ATOM 1645 CA PRO A 206 -13.090 -1.905 39.339 1.00 12.40 C
ANISOU 1645 CA PRO A 206 1838 1388 1483 152 291 -130 C
ATOM 1646 CB PRO A 206 -14.213 -2.072 40.382 1.00 13.63 C
ANISOU 1646 CB PRO A 206 2033 1586 1558 159 409 3 C
ATOM 1647 CG PRO A 206 -14.714 -0.650 40.594 1.00 13.77 C
ANISOU 1647 CG PRO A 206 1989 1565 1679 206 333 87 C
ATOM 1648 CD PRO A 206 -13.438 0.157 40.554 1.00 12.49 C
ANISOU 1648 CD PRO A 206 1944 1525 1277 168 364 -14 C
ATOM 1649 C PRO A 206 -13.709 -1.816 37.932 1.00 11.75 C
ANISOU 1649 C PRO A 206 1661 1288 1512 -8 167 -190 C
ATOM 1650 O PRO A 206 -14.621 -2.570 37.605 1.00 12.29 O
ANISOU 1650 O PRO A 206 1764 1368 1535 44 91 -317 O
ATOM 1651 N THR A 207 -13.208 -0.910 37.082 1.00 11.67 N
ANISOU 1651 N THR A 207 1768 1289 1376 -31 55 -239 N
ATOM 1652 CA THR A 207 -13.829 -0.742 35.784 1.00 11.35 C
ANISOU 1652 CA THR A 207 1517 1408 1388 -76 95 -203 C
ATOM 1653 CB THR A 207 -13.278 0.415 34.949 1.00 11.80 C
ANISOU 1653 CB THR A 207 1745 1416 1319 -107 -23 -115 C
ATOM 1654 OG1 THR A 207 -11.962 0.097 34.487 1.00 12.62 O
ANISOU 1654 OG1 THR A 207 1818 1502 1474 -87 239 -89 O
ATOM 1655 CG2 THR A 207 -13.303 1.741 35.675 1.00 12.39 C
ANISOU 1655 CG2 THR A 207 1718 1375 1614 -290 -36 -187 C
ATOM 1656 C THR A 207 -13.743 -2.038 34.961 1.00 11.29 C
ANISOU 1656 C THR A 207 1561 1287 1441 -72 113 -144 C
ATOM 1657 O THR A 207 -12.821 -2.859 35.078 1.00 12.23 O
ANISOU 1657 O THR A 207 1815 1300 1528 51 44 -148 O
ATOM 1658 N GLN A 208 -14.743 -2.198 34.099 1.00 11.11 N
ANISOU 1658 N GLN A 208 1693 1221 1305 -114 116 -156 N
ATOM 1659 CA GLN A 208 -14.948 -3.419 33.329 1.00 11.64 C
ANISOU 1659 CA GLN A 208 1886 1192 1341 15 170 -195 C
ATOM 1660 CB GLN A 208 -16.434 -3.754 33.325 1.00 12.89 C
ANISOU 1660 CB GLN A 208 1943 1452 1503 -84 253 -150 C
ATOM 1661 CG GLN A 208 -16.978 -4.023 34.723 1.00 12.40 C
ANISOU 1661 CG GLN A 208 2022 1259 1429 -167 80 -64 C
ATOM 1662 CD GLN A 208 -16.354 -5.243 35.347 1.00 13.26 C
ANISOU 1662 CD GLN A 208 2048 1427 1562 -132 -60 -85 C
ATOM 1663 OE1 GLN A 208 -16.687 -6.344 34.925 1.00 14.83 O
ANISOU 1663 OE1 GLN A 208 2306 1386 1940 -295 -268 -3 O
ATOM 1664 NE2 GLN A 208 -15.451 -5.087 36.318 1.00 14.01 N
ANISOU 1664 NE2 GLN A 208 2100 1769 1452 -491 24 9 N
ATOM 1665 C GLN A 208 -14.322 -3.245 31.932 1.00 11.91 C
ANISOU 1665 C GLN A 208 1736 1580 1208 38 19 -124 C
ATOM 1666 O GLN A 208 -14.976 -3.467 30.900 1.00 12.31 O
ANISOU 1666 O GLN A 208 1843 1518 1313 9 -84 -363 O
ATOM 1667 N TYR A 209 -13.019 -2.920 31.915 1.00 13.31 N
ANISOU 1667 N TYR A 209 1895 1737 1422 -37 208 68 N
ATOM 1668 CA TYR A 209 -12.309 -2.583 30.697 1.00 13.09 C
ANISOU 1668 CA TYR A 209 1897 1787 1289 31 186 -31 C
ATOM 1669 CB TYR A 209 -10.999 -1.851 31.017 1.00 13.72 C
ANISOU 1669 CB TYR A 209 1918 1805 1489 8 281 -137 C
ATOM 1670 CG TYR A 209 -10.040 -2.657 31.853 1.00 13.99 C
ANISOU 1670 CG TYR A 209 2089 1781 1446 24 146 -111 C
ATOM 1671 CD1 TYR A 209 -9.151 -3.555 31.282 1.00 14.76 C
ANISOU 1671 CD1 TYR A 209 2034 2157 1417 -30 249 -247 C
ATOM 1672 CE1 TYR A 209 -8.308 -4.334 32.066 1.00 15.37 C
ANISOU 1672 CE1 TYR A 209 2156 2016 1667 122 204 -218 C
ATOM 1673 CZ TYR A 209 -8.323 -4.208 33.438 1.00 14.26 C
ANISOU 1673 CZ TYR A 209 1879 1892 1644 128 194 -114 C
ATOM 1674 OH TYR A 209 -7.479 -4.980 34.216 1.00 16.82 O
ANISOU 1674 OH TYR A 209 2497 2331 1559 361 75 146 O
ATOM 1675 CE2 TYR A 209 -9.184 -3.292 34.016 1.00 13.52 C
ANISOU 1675 CE2 TYR A 209 2117 1771 1249 11 142 -322 C
ATOM 1676 CD2 TYR A 209 -10.029 -2.530 33.228 1.00 14.26 C
ANISOU 1676 CD2 TYR A 209 2219 1765 1435 10 256 -168 C
ATOM 1677 C TYR A 209 -12.049 -3.808 29.800 1.00 13.82 C
ANISOU 1677 C TYR A 209 1879 1920 1450 -183 413 -187 C
ATOM 1678 O TYR A 209 -11.543 -3.661 28.660 1.00 17.59 O
ANISOU 1678 O TYR A 209 2710 2569 1403 -449 538 -354 O
ATOM 1679 N LYS A 210 -12.308 -5.020 30.300 1.00 15.31 N
ANISOU 1679 N LYS A 210 2071 1820 1926 35 526 -180 N
ATOM 1680 CA LYS A 210 -12.159 -6.234 29.496 1.00 18.78 C
ANISOU 1680 CA LYS A 210 2698 2368 2069 -25 506 -552 C
ATOM 1681 CB LYS A 210 -11.709 -7.381 30.398 1.00 20.83 C
ANISOU 1681 CB LYS A 210 2691 2347 2874 217 583 -465 C
ATOM 1682 CG LYS A 210 -10.319 -7.200 30.985 1.00 24.86 C
ANISOU 1682 CG LYS A 210 2991 2792 3660 213 237 -288 C
ATOM 1683 CD LYS A 210 -10.032 -8.053 32.221 1.00 28.02 C
ANISOU 1683 CD LYS A 210 3205 3288 4151 180 -53 -28 C
ATOM 1684 CE LYS A 210 -10.213 -9.540 32.035 1.00 27.33 C
ANISOU 1684 CE LYS A 210 3103 3268 4013 41 177 -295 C
ATOM 1685 NZ LYS A 210 -9.082 -10.155 31.315 1.00 30.65 N
ANISOU 1685 NZ LYS A 210 3398 3546 4699 218 451 -210 N
ATOM 1686 C LYS A 210 -13.454 -6.573 28.753 1.00 18.12 C
ANISOU 1686 C LYS A 210 2582 2095 2205 109 482 -633 C
ATOM 1687 O LYS A 210 -13.441 -7.495 27.914 1.00 22.68 O
ANISOU 1687 O LYS A 210 3608 2573 2435 880 72 -966 O
ATOM 1688 N ASN A 211 -14.547 -5.849 29.047 1.00 16.27 N
ANISOU 1688 N ASN A 211 2491 1769 1922 -175 687 -792 N
ATOM 1689 CA ASN A 211 -15.851 -6.128 28.507 1.00 17.56 C
ANISOU 1689 CA ASN A 211 2845 1962 1864 -292 73 -836 C
ATOM 1690 CB ASN A 211 -16.730 -6.846 29.540 1.00 21.47 C
ANISOU 1690 CB ASN A 211 2819 2590 2748 -771 59 -465 C
ATOM 1691 CG ASN A 211 -16.198 -8.189 29.999 1.00 29.12 C
ANISOU 1691 CG ASN A 211 4243 3223 3598 -200 -496 -490 C
ATOM 1692 OD1 ASN A 211 -16.534 -9.222 29.418 1.00 39.11 O
ANISOU 1692 OD1 ASN A 211 6295 3793 4772 -779 -257 -1088 O
ATOM 1693 ND2 ASN A 211 -15.406 -8.194 31.058 1.00 30.18 N
ANISOU 1693 ND2 ASN A 211 4273 3736 3456 -417 -307 -292 N
ATOM 1694 C ASN A 211 -16.538 -4.826 28.079 1.00 17.42 C
ANISOU 1694 C ASN A 211 2623 2152 1844 -283 455 -539 C
ATOM 1695 O ASN A 211 -17.603 -4.511 28.554 1.00 18.48 O
ANISOU 1695 O ASN A 211 2470 2631 1920 146 280 -332 O
ATOM 1696 N ILE A 212 -15.920 -4.086 27.151 1.00 15.60 N
ANISOU 1696 N ILE A 212 2230 1800 1898 -51 441 -408 N
ATOM 1697 CA ILE A 212 -16.397 -2.749 26.817 1.00 17.58 C
ANISOU 1697 CA ILE A 212 2866 1848 1965 -18 270 -292 C
ATOM 1698 CB ILE A 212 -15.294 -1.970 26.094 1.00 20.21 C
ANISOU 1698 CB ILE A 212 3001 2020 2658 -167 337 -264 C
ATOM 1699 CG1 ILE A 212 -14.177 -1.670 27.106 1.00 24.32 C
ANISOU 1699 CG1 ILE A 212 3129 2856 3254 -169 21 53 C
ATOM 1700 CG2 ILE A 212 -15.846 -0.698 25.464 1.00 20.25 C
ANISOU 1700 CG2 ILE A 212 3106 2118 2469 -128 492 -256 C
ATOM 1701 CD1 ILE A 212 -12.871 -1.360 26.506 1.00 26.92 C
ANISOU 1701 CD1 ILE A 212 3612 2996 3618 -477 361 312 C
ATOM 1702 C ILE A 212 -17.729 -2.785 26.054 1.00 16.26 C
ANISOU 1702 C ILE A 212 2477 1920 1779 -131 571 -36 C
ATOM 1703 O ILE A 212 -18.549 -1.870 26.190 1.00 16.93 O
ANISOU 1703 O ILE A 212 2605 2003 1821 -26 283 -283 O
ATOM 1704 N LYS A 213 -17.988 -3.816 25.256 1.00 19.59 N
ANISOU 1704 N LYS A 213 2974 2632 1834 -788 604 -115 N
ATOM 1705 CA LYS A 213 -19.245 -3.822 24.493 1.00 21.55 C
ANISOU 1705 CA LYS A 213 3246 3131 1809 -951 430 -94 C
ATOM 1706 CB LYS A 213 -19.282 -4.948 23.456 1.00 26.32 C
ANISOU 1706 CB LYS A 213 4084 3290 2626 -1200 419 -557 C
ATOM 1707 CG LYS A 213 -20.555 -4.963 22.603 1.00 34.00 C
ANISOU 1707 CG LYS A 213 4537 4550 3829 -1024 -1 -713 C
ATOM 1708 CD LYS A 213 -20.840 -6.287 21.889 1.00 42.40 C
ANISOU 1708 CD LYS A 213 6087 4834 5190 -1169 -72 -1091 C
ATOM 1709 CE LYS A 213 -22.126 -6.963 22.345 1.00 48.38 C
ANISOU 1709 CE LYS A 213 6053 5924 6404 -1416 -1 -835 C
ATOM 1710 NZ LYS A 213 -22.220 -8.367 21.877 1.00 55.64 N
ANISOU 1710 NZ LYS A 213 7032 6134 7973 -1031 -171 -917 N
ATOM 1711 C LYS A 213 -20.435 -3.965 25.444 1.00 22.07 C
ANISOU 1711 C LYS A 213 2933 3248 2204 -838 393 389 C
ATOM 1712 O LYS A 213 -21.474 -3.303 25.254 1.00 25.32 O
ANISOU 1712 O LYS A 213 3339 3801 2480 -614 -266 309 O
ATOM 1713 N ASP A 214 -20.289 -4.818 26.466 1.00 18.06 N
ANISOU 1713 N ASP A 214 2832 2389 1639 -1236 -68 -235 N
ATOM 1714 CA ASP A 214 -21.422 -5.225 27.284 1.00 17.87 C
ANISOU 1714 CA ASP A 214 2737 2600 1452 -1126 11 -297 C
ATOM 1715 CB ASP A 214 -22.019 -6.511 26.709 1.00 20.62 C
ANISOU 1715 CB ASP A 214 3446 2677 1711 -1193 226 -714 C
ATOM 1716 CG ASP A 214 -23.319 -6.970 27.336 1.00 23.74 C
ANISOU 1716 CG ASP A 214 3419 3387 2211 -1180 278 -631 C
ATOM 1717 OD1 ASP A 214 -24.085 -6.108 27.808 1.00 25.76 O
ANISOU 1717 OD1 ASP A 214 2911 4360 2517 -1033 182 -805 O
ATOM 1718 OD2 ASP A 214 -23.546 -8.193 27.362 1.00 31.25 O
ANISOU 1718 OD2 ASP A 214 4428 3798 3648 -1937 305 -524 O
ATOM 1719 C ASP A 214 -21.023 -5.434 28.748 1.00 15.96 C
ANISOU 1719 C ASP A 214 2575 2047 1441 -705 129 -184 C
ATOM 1720 O ASP A 214 -21.183 -6.512 29.325 1.00 17.44 O
ANISOU 1720 O ASP A 214 3049 1833 1744 -632 467 -304 O
ATOM 1721 N PRO A 215 -20.531 -4.384 29.422 1.00 14.18 N
ANISOU 1721 N PRO A 215 2229 1772 1386 -432 -1 -62 N
ATOM 1722 CA PRO A 215 -20.081 -4.500 30.802 1.00 12.22 C
ANISOU 1722 CA PRO A 215 2034 1360 1247 -106 115 -130 C
ATOM 1723 CB PRO A 215 -19.224 -3.251 31.011 1.00 12.94 C
ANISOU 1723 CB PRO A 215 1870 1704 1340 -249 164 -299 C
ATOM 1724 CG PRO A 215 -19.809 -2.239 30.082 1.00 13.47 C
ANISOU 1724 CG PRO A 215 1849 1531 1736 -142 261 -177 C
ATOM 1725 CD PRO A 215 -20.331 -3.021 28.899 1.00 15.26 C
ANISOU 1725 CD PRO A 215 2372 1885 1540 -343 7 123 C
ATOM 1726 C PRO A 215 -21.256 -4.511 31.778 1.00 11.57 C
ANISOU 1726 C PRO A 215 1902 1257 1236 -105 -8 -69 C
ATOM 1727 O PRO A 215 -22.267 -3.864 31.547 1.00 12.08 O
ANISOU 1727 O PRO A 215 1842 1263 1483 -121 -31 -145 O
ATOM 1728 N VAL A 216 -21.098 -5.255 32.866 1.00 11.51 N
ANISOU 1728 N VAL A 216 2044 1132 1195 49 256 -64 N
ATOM 1729 CA VAL A 216 -22.081 -5.256 33.937 1.00 11.35 C
ANISOU 1729 CA VAL A 216 1737 1151 1422 -64 198 -155 C
ATOM 1730 CB VAL A 216 -21.809 -6.371 34.964 1.00 12.65 C
ANISOU 1730 CB VAL A 216 2104 1071 1629 -2 287 -60 C
ATOM 1731 CG1 VAL A 216 -22.835 -6.344 36.082 1.00 12.75 C
ANISOU 1731 CG1 VAL A 216 2196 974 1672 284 299 -48 C
ATOM 1732 CG2 VAL A 216 -21.813 -7.734 34.299 1.00 13.39 C
ANISOU 1732 CG2 VAL A 216 2183 1198 1704 32 303 -175 C
ATOM 1733 C VAL A 216 -22.078 -3.878 34.591 1.00 10.52 C
ANISOU 1733 C VAL A 216 1728 1065 1203 61 151 -19 C
ATOM 1734 O VAL A 216 -21.035 -3.383 34.991 1.00 11.97 O
ANISOU 1734 O VAL A 216 1785 1295 1466 49 151 -131 O
ATOM 1735 N PRO A 217 -23.260 -3.242 34.746 1.00 11.91 N
ANISOU 1735 N PRO A 217 1939 1019 1567 225 113 -324 N
ATOM 1736 CA PRO A 217 -23.341 -1.920 35.359 1.00 11.78 C
ANISOU 1736 CA PRO A 217 2026 1220 1230 125 290 -418 C
ATOM 1737 CB PRO A 217 -24.786 -1.491 35.142 1.00 15.04 C
ANISOU 1737 CB PRO A 217 2212 2042 1459 502 198 -325 C
ATOM 1738 CG PRO A 217 -25.445 -2.515 34.262 1.00 17.13 C
ANISOU 1738 CG PRO A 217 2202 1729 2575 44 335 -125 C
ATOM 1739 CD PRO A 217 -24.557 -3.720 34.242 1.00 13.89 C
ANISOU 1739 CD PRO A 217 2027 1528 1723 52 208 -433 C
ATOM 1740 C PRO A 217 -23.083 -1.947 36.868 1.00 10.74 C
ANISOU 1740 C PRO A 217 1763 1082 1233 202 201 -214 C
ATOM 1741 O PRO A 217 -23.246 -2.995 37.518 1.00 11.56 O
ANISOU 1741 O PRO A 217 1765 1293 1333 -110 182 -93 O
ATOM 1742 N PHE A 218 -22.703 -0.779 37.405 1.00 10.72 N
ANISOU 1742 N PHE A 218 1829 1094 1150 28 282 -87 N
ATOM 1743 CA PHE A 218 -22.692 -0.511 38.848 1.00 11.11 C
ANISOU 1743 CA PHE A 218 1830 1165 1223 10 269 -238 C
ATOM 1744 CB PHE A 218 -21.545 0.446 39.199 1.00 11.35 C
ANISOU 1744 CB PHE A 218 1846 1091 1374 -20 311 -166 C
ATOM 1745 CG PHE A 218 -20.206 -0.181 38.894 1.00 11.94 C
ANISOU 1745 CG PHE A 218 1791 1323 1419 -44 278 -320 C
ATOM 1746 CD1 PHE A 218 -19.711 -1.174 39.740 1.00 12.53 C
ANISOU 1746 CD1 PHE A 218 1911 1484 1366 121 344 -210 C
ATOM 1747 CE1 PHE A 218 -18.493 -1.784 39.475 1.00 12.60 C
ANISOU 1747 CE1 PHE A 218 1648 1695 1443 -101 40 -313 C
ATOM 1748 CZ PHE A 218 -17.782 -1.425 38.363 1.00 13.06 C
ANISOU 1748 CZ PHE A 218 1644 1755 1563 48 301 -443 C
ATOM 1749 CD2 PHE A 218 -19.470 0.171 37.773 1.00 13.23 C
ANISOU 1749 CD2 PHE A 218 1782 1784 1458 -86 201 -136 C
ATOM 1750 CE2 PHE A 218 -18.272 -0.468 37.512 1.00 13.73 C
ANISOU 1750 CE2 PHE A 218 1983 1962 1269 12 419 -233 C
ATOM 1751 C PHE A 218 -24.043 0.056 39.262 1.00 11.24 C
ANISOU 1751 C PHE A 218 1840 1216 1212 38 303 -155 C
ATOM 1752 O PHE A 218 -24.770 0.646 38.455 1.00 13.24 O
ANISOU 1752 O PHE A 218 2175 1450 1405 142 408 173 O
ATOM 1753 N ARG A 219 -24.395 -0.147 40.534 1.00 12.00 N
ANISOU 1753 N ARG A 219 1980 1313 1266 133 449 -38 N
ATOM 1754 CA ARG A 219 -25.714 0.294 41.011 1.00 12.55 C
ANISOU 1754 CA ARG A 219 1950 1370 1446 112 323 -406 C
ATOM 1755 CB ARG A 219 -26.703 -0.856 41.198 1.00 16.00 C
ANISOU 1755 CB ARG A 219 2397 1592 2087 -23 439 -383 C
ATOM 1756 CG ARG A 219 -26.195 -2.063 41.953 1.00 16.64 C
ANISOU 1756 CG ARG A 219 2268 2143 1910 288 456 -258 C
ATOM 1757 CD ARG A 219 -26.342 -1.909 43.446 1.00 18.12 C
ANISOU 1757 CD ARG A 219 2823 2206 1853 321 115 -423 C
ATOM 1758 NE ARG A 219 -26.082 -3.143 44.145 1.00 17.94 N
ANISOU 1758 NE ARG A 219 2498 2302 2016 118 316 -173 N
ATOM 1759 CZ ARG A 219 -26.951 -4.100 44.395 1.00 16.96 C
ANISOU 1759 CZ ARG A 219 2565 2299 1577 463 631 -31 C
ATOM 1760 NH1 ARG A 219 -28.236 -3.970 44.087 1.00 19.57 N
ANISOU 1760 NH1 ARG A 219 2596 3068 1770 181 710 -145 N
ATOM 1761 NH2 ARG A 219 -26.485 -5.180 44.980 1.00 18.83 N
ANISOU 1761 NH2 ARG A 219 3353 2166 1635 647 989 236 N
ATOM 1762 C ARG A 219 -25.613 1.165 42.268 1.00 11.88 C
ANISOU 1762 C ARG A 219 1940 1246 1328 135 376 -305 C
ATOM 1763 O ARG A 219 -24.841 0.922 43.203 1.00 12.43 O
ANISOU 1763 O ARG A 219 2107 1199 1417 102 226 -175 O
ATOM 1764 N ASN A 220 -26.464 2.196 42.252 1.00 11.10 N
ANISOU 1764 N ASN A 220 1922 1075 1220 39 216 -185 N
ATOM 1765 CA ASN A 220 -26.755 3.060 43.376 1.00 11.45 C
ANISOU 1765 CA ASN A 220 1944 1077 1326 -17 324 -276 C
ATOM 1766 CB ASN A 220 -27.666 2.367 44.373 1.00 11.29 C
ANISOU 1766 CB ASN A 220 1830 1279 1179 88 318 -361 C
ATOM 1767 CG ASN A 220 -28.252 3.330 45.380 1.00 11.50 C
ANISOU 1767 CG ASN A 220 1936 1072 1359 -1 372 -416 C
ATOM 1768 OD1 ASN A 220 -28.570 4.480 45.027 1.00 13.78 O
ANISOU 1768 OD1 ASN A 220 2393 1316 1524 129 342 -289 O
ATOM 1769 ND2 ASN A 220 -28.357 2.886 46.625 1.00 12.68 N
ANISOU 1769 ND2 ASN A 220 1892 1526 1397 -142 453 -363 N
ATOM 1770 C ASN A 220 -25.487 3.614 44.059 1.00 11.38 C
ANISOU 1770 C ASN A 220 1853 1186 1285 76 322 -253 C
ATOM 1771 O ASN A 220 -25.274 3.449 45.254 1.00 12.80 O
ANISOU 1771 O ASN A 220 1991 1588 1282 -10 343 -243 O
ATOM 1772 N LEU A 221 -24.704 4.361 43.276 1.00 12.25 N
ANISOU 1772 N LEU A 221 1820 1381 1452 -155 281 -258 N
ATOM 1773 CA LEU A 221 -23.474 5.014 43.751 1.00 12.10 C
ANISOU 1773 CA LEU A 221 1847 1304 1444 -58 248 -318 C
ATOM 1774 CB LEU A 221 -22.525 5.175 42.566 1.00 12.58 C
ANISOU 1774 CB LEU A 221 1807 1370 1602 -9 273 -196 C
ATOM 1775 CG LEU A 221 -22.075 3.870 41.905 1.00 14.07 C
ANISOU 1775 CG LEU A 221 2254 1449 1640 30 208 -307 C
ATOM 1776 CD1 LEU A 221 -21.130 4.163 40.778 1.00 15.10 C
ANISOU 1776 CD1 LEU A 221 2363 1560 1811 -264 284 -308 C
ATOM 1777 CD2 LEU A 221 -21.449 2.910 42.901 1.00 14.42 C
ANISOU 1777 CD2 LEU A 221 2295 1550 1632 132 279 -317 C
ATOM 1778 C LEU A 221 -23.800 6.356 44.426 1.00 12.04 C
ANISOU 1778 C LEU A 221 1984 1227 1361 37 249 -158 C
ATOM 1779 O LEU A 221 -23.785 7.421 43.811 1.00 12.76 O
ANISOU 1779 O LEU A 221 1997 1060 1791 -19 295 -154 O
ATOM 1780 N ASN A 222 -24.049 6.294 45.731 1.00 11.78 N
ANISOU 1780 N ASN A 222 1977 1136 1363 -33 318 -292 N
ATOM 1781 CA ASN A 222 -24.215 7.493 46.547 1.00 12.48 C
ANISOU 1781 CA ASN A 222 1925 1271 1544 62 268 -411 C
ATOM 1782 CB ASN A 222 -24.596 7.174 47.989 1.00 13.41 C
ANISOU 1782 CB ASN A 222 2048 1456 1592 -87 318 -337 C
ATOM 1783 CG ASN A 222 -25.998 6.691 48.250 1.00 14.46 C
ANISOU 1783 CG ASN A 222 2009 1735 1749 21 402 -565 C
ATOM 1784 OD1 ASN A 222 -26.484 6.895 49.347 1.00 14.31 O
ANISOU 1784 OD1 ASN A 222 2069 1583 1783 9 581 -322 O
ATOM 1785 ND2 ASN A 222 -26.640 6.031 47.291 1.00 14.26 N
ANISOU 1785 ND2 ASN A 222 2038 1837 1540 -76 410 -492 N
ATOM 1786 C ASN A 222 -22.906 8.298 46.635 1.00 12.56 C
ANISOU 1786 C ASN A 222 1833 1410 1529 66 267 -208 C
ATOM 1787 O ASN A 222 -22.957 9.542 46.718 1.00 13.67 O
ANISOU 1787 O ASN A 222 2005 1450 1738 42 480 -307 O
ATOM 1788 N THR A 223 -21.762 7.592 46.670 1.00 11.39 N
ANISOU 1788 N THR A 223 1549 1348 1430 -86 262 -299 N
ATOM 1789 CA THR A 223 -20.451 8.186 46.537 1.00 12.32 C
ANISOU 1789 CA THR A 223 1749 1265 1666 -117 310 -218 C
ATOM 1790 CB THR A 223 -19.558 7.921 47.759 1.00 13.70 C
ANISOU 1790 CB THR A 223 2039 1582 1583 -75 271 -308 C
ATOM 1791 OG1 THR A 223 -20.176 8.440 48.938 1.00 15.31 O
ANISOU 1791 OG1 THR A 223 2140 2170 1505 8 257 -474 O
ATOM 1792 CG2 THR A 223 -18.186 8.528 47.608 1.00 14.24 C
ANISOU 1792 CG2 THR A 223 2194 1454 1762 -162 154 -31 C
ATOM 1793 C THR A 223 -19.786 7.571 45.304 1.00 13.01 C
ANISOU 1793 C THR A 223 1830 1603 1509 -176 231 -254 C
ATOM 1794 O THR A 223 -19.755 6.338 45.169 1.00 13.43 O
ANISOU 1794 O THR A 223 1917 1575 1609 -27 372 -297 O
ATOM 1795 N PHE A 224 -19.331 8.422 44.393 1.00 12.11 N
ANISOU 1795 N PHE A 224 1800 1346 1454 109 225 -296 N
ATOM 1796 CA PHE A 224 -18.596 7.996 43.224 1.00 11.89 C
ANISOU 1796 CA PHE A 224 1796 1272 1450 139 206 -247 C
ATOM 1797 CB PHE A 224 -19.531 7.820 42.027 1.00 11.90 C
ANISOU 1797 CB PHE A 224 1894 1332 1294 113 245 -36 C
ATOM 1798 CG PHE A 224 -18.872 7.348 40.753 1.00 13.31 C
ANISOU 1798 CG PHE A 224 2253 1417 1386 65 278 -261 C
ATOM 1799 CD1 PHE A 224 -17.854 6.402 40.772 1.00 13.49 C
ANISOU 1799 CD1 PHE A 224 2215 1463 1448 16 280 11 C
ATOM 1800 CE1 PHE A 224 -17.293 5.939 39.600 1.00 16.25 C
ANISOU 1800 CE1 PHE A 224 2660 1940 1571 45 314 -205 C
ATOM 1801 CZ PHE A 224 -17.770 6.375 38.393 1.00 15.87 C
ANISOU 1801 CZ PHE A 224 2832 1709 1487 301 378 -319 C
ATOM 1802 CD2 PHE A 224 -19.343 7.771 39.530 1.00 16.01 C
ANISOU 1802 CD2 PHE A 224 2815 1788 1479 287 238 -249 C
ATOM 1803 CE2 PHE A 224 -18.788 7.292 38.349 1.00 16.66 C
ANISOU 1803 CE2 PHE A 224 2811 2032 1484 416 334 -220 C
ATOM 1804 C PHE A 224 -17.513 9.042 42.958 1.00 12.85 C
ANISOU 1804 C PHE A 224 1874 1406 1599 74 342 -83 C
ATOM 1805 O PHE A 224 -17.829 10.157 42.535 1.00 13.21 O
ANISOU 1805 O PHE A 224 2003 1358 1657 100 168 -119 O
ATOM 1806 N LYS A 225 -16.266 8.687 43.258 1.00 13.14 N
ANISOU 1806 N LYS A 225 1839 1367 1784 31 348 -141 N
ATOM 1807 CA LYS A 225 -15.156 9.577 43.008 1.00 12.99 C
ANISOU 1807 CA LYS A 225 1773 1486 1673 35 342 -34 C
ATOM 1808 CB LYS A 225 -14.514 10.096 44.296 1.00 14.75 C
ANISOU 1808 CB LYS A 225 1986 1882 1735 -1 171 -17 C
ATOM 1809 CG LYS A 225 -15.456 10.662 45.335 1.00 17.57 C
ANISOU 1809 CG LYS A 225 2122 2486 2066 -168 291 -410 C
ATOM 1810 CD LYS A 225 -14.733 11.143 46.587 1.00 21.11 C
ANISOU 1810 CD LYS A 225 2739 3163 2117 -473 150 -566 C
ATOM 1811 CE LYS A 225 -15.700 11.615 47.645 1.00 24.78 C
ANISOU 1811 CE LYS A 225 3366 3902 2146 -714 466 -694 C
ATOM 1812 NZ LYS A 225 -14.996 12.126 48.844 1.00 28.94 N
ANISOU 1812 NZ LYS A 225 3452 4561 2982 -678 84 -999 N
ATOM 1813 C LYS A 225 -14.118 8.827 42.178 1.00 13.47 C
ANISOU 1813 C LYS A 225 1903 1460 1753 226 358 65 C
ATOM 1814 O LYS A 225 -13.842 7.659 42.427 1.00 14.12 O
ANISOU 1814 O LYS A 225 2137 1339 1888 88 395 38 O
ATOM 1815 N VAL A 226 -13.530 9.533 41.217 1.00 13.14 N
ANISOU 1815 N VAL A 226 1941 1536 1513 517 438 107 N
ATOM 1816 CA VAL A 226 -12.424 9.028 40.425 1.00 13.47 C
ANISOU 1816 CA VAL A 226 1974 1591 1552 477 522 266 C
ATOM 1817 CB VAL A 226 -12.875 8.802 38.967 1.00 14.78 C
ANISOU 1817 CB VAL A 226 2165 1819 1631 357 474 278 C
ATOM 1818 CG1 VAL A 226 -11.707 8.411 38.075 1.00 15.70 C
ANISOU 1818 CG1 VAL A 226 2330 1868 1766 299 646 210 C
ATOM 1819 CG2 VAL A 226 -13.994 7.786 38.899 1.00 15.69 C
ANISOU 1819 CG2 VAL A 226 2325 1815 1819 354 392 119 C
ATOM 1820 C VAL A 226 -11.311 10.069 40.527 1.00 13.79 C
ANISOU 1820 C VAL A 226 1906 1669 1665 489 510 113 C
ATOM 1821 O VAL A 226 -11.506 11.212 40.096 1.00 14.58 O
ANISOU 1821 O VAL A 226 2008 1723 1806 340 331 192 O
ATOM 1822 N ILE A 227 -10.202 9.676 41.153 1.00 14.40 N
ANISOU 1822 N ILE A 227 2115 1846 1508 358 378 166 N
ATOM 1823 CA ILE A 227 -9.120 10.560 41.498 1.00 15.86 C
ANISOU 1823 CA ILE A 227 2238 1956 1829 555 251 -313 C
ATOM 1824 CB ILE A 227 -8.857 10.533 43.019 1.00 20.35 C
ANISOU 1824 CB ILE A 227 2979 2813 1937 979 217 -299 C
ATOM 1825 CG1 ILE A 227 -10.134 10.839 43.814 1.00 20.83 C
ANISOU 1825 CG1 ILE A 227 2922 3216 1777 1266 15 -402 C
ATOM 1826 CG2 ILE A 227 -7.706 11.463 43.356 1.00 23.15 C
ANISOU 1826 CG2 ILE A 227 3119 3440 2236 1101 -254 -711 C
ATOM 1827 CD1 ILE A 227 -10.215 10.237 45.181 1.00 26.38 C
ANISOU 1827 CD1 ILE A 227 3894 3909 2217 817 511 -127 C
ATOM 1828 C ILE A 227 -7.887 10.106 40.713 1.00 13.09 C
ANISOU 1828 C ILE A 227 1965 1384 1623 166 125 -462 C
ATOM 1829 O ILE A 227 -7.388 8.998 40.935 1.00 14.81 O
ANISOU 1829 O ILE A 227 2139 1424 2061 172 122 -254 O
ATOM 1830 N LEU A 228 -7.422 10.948 39.787 1.00 13.14 N
ANISOU 1830 N LEU A 228 2201 1231 1558 212 -60 -359 N
ATOM 1831 CA LEU A 228 -6.350 10.604 38.867 1.00 13.64 C
ANISOU 1831 CA LEU A 228 2204 1494 1483 323 -87 -374 C
ATOM 1832 CB LEU A 228 -6.776 10.898 37.426 1.00 15.10 C
ANISOU 1832 CB LEU A 228 2262 1947 1526 483 -152 -416 C
ATOM 1833 CG LEU A 228 -8.104 10.320 36.971 1.00 16.91 C
ANISOU 1833 CG LEU A 228 2475 2015 1934 458 -315 -698 C
ATOM 1834 CD1 LEU A 228 -8.388 10.771 35.548 1.00 20.09 C
ANISOU 1834 CD1 LEU A 228 3095 2504 2033 621 -439 -563 C
ATOM 1835 CD2 LEU A 228 -8.109 8.817 37.090 1.00 16.05 C
ANISOU 1835 CD2 LEU A 228 2183 1998 1917 359 -140 -795 C
ATOM 1836 C LEU A 228 -5.106 11.441 39.161 1.00 13.84 C
ANISOU 1836 C LEU A 228 2375 1463 1417 112 113 -309 C
ATOM 1837 O LEU A 228 -5.177 12.656 39.364 1.00 15.25 O
ANISOU 1837 O LEU A 228 2519 1529 1744 135 57 -502 O
ATOM 1838 N ASP A 229 -3.958 10.785 39.119 1.00 13.26 N
ANISOU 1838 N ASP A 229 2290 1409 1338 -6 -2 -401 N
ATOM 1839 CA ASP A 229 -2.684 11.452 39.006 1.00 14.20 C
ANISOU 1839 CA ASP A 229 2213 1720 1459 -34 -28 -328 C
ATOM 1840 CB ASP A 229 -1.573 10.567 39.551 1.00 16.27 C
ANISOU 1840 CB ASP A 229 2533 1995 1653 207 -129 -402 C
ATOM 1841 CG ASP A 229 -0.163 11.101 39.381 1.00 17.58 C
ANISOU 1841 CG ASP A 229 2484 2502 1694 158 -252 -591 C
ATOM 1842 OD1 ASP A 229 0.006 12.289 39.010 1.00 21.00 O
ANISOU 1842 OD1 ASP A 229 2880 2597 2501 -42 -442 -666 O
ATOM 1843 OD2 ASP A 229 0.772 10.304 39.621 1.00 23.03 O
ANISOU 1843 OD2 ASP A 229 2715 3114 2919 536 -578 -934 O
ATOM 1844 C ASP A 229 -2.467 11.774 37.524 1.00 13.97 C
ANISOU 1844 C ASP A 229 2320 1660 1325 -115 84 -553 C
ATOM 1845 O ASP A 229 -2.054 10.910 36.765 1.00 14.94 O
ANISOU 1845 O ASP A 229 2556 1641 1477 -11 117 -489 O
ATOM 1846 N GLY A 230 -2.794 12.993 37.107 1.00 14.34 N
ANISOU 1846 N GLY A 230 2347 1525 1575 -242 121 -610 N
ATOM 1847 CA GLY A 230 -2.705 13.385 35.700 1.00 15.06 C
ANISOU 1847 CA GLY A 230 2343 1627 1750 -254 118 -403 C
ATOM 1848 C GLY A 230 -1.282 13.663 35.267 1.00 13.34 C
ANISOU 1848 C GLY A 230 2274 1311 1481 -304 61 -325 C
ATOM 1849 O GLY A 230 -0.630 14.541 35.832 1.00 13.82 O
ANISOU 1849 O GLY A 230 2387 1413 1449 -377 222 -459 O
ATOM 1850 N GLN A 231 -0.809 12.894 34.286 1.00 13.09 N
ANISOU 1850 N GLN A 231 2015 1607 1351 -383 105 -362 N
ATOM 1851 CA AGLN A 231 0.505 13.084 33.673 0.50 13.29 C
ANISOU 1851 CA AGLN A 231 2050 1480 1519 -374 65 -200 C
ATOM 1852 CA BGLN A 231 0.526 13.066 33.675 0.50 13.83 C
ANISOU 1852 CA BGLN A 231 2116 1613 1524 -422 118 -254 C
ATOM 1853 CB AGLN A 231 1.484 12.022 34.169 0.50 13.89 C
ANISOU 1853 CB AGLN A 231 1982 1515 1778 -342 37 -52 C
ATOM 1854 CB BGLN A 231 1.464 11.962 34.193 0.50 15.24 C
ANISOU 1854 CB BGLN A 231 2225 1736 1829 -312 84 -121 C
ATOM 1855 CG AGLN A 231 1.751 12.105 35.663 0.50 15.74 C
ANISOU 1855 CG AGLN A 231 2349 1754 1878 -226 -235 -219 C
ATOM 1856 CG BGLN A 231 2.975 12.113 33.963 0.50 17.78 C
ANISOU 1856 CG BGLN A 231 2367 2238 2148 -448 -65 -300 C
ATOM 1857 CD AGLN A 231 2.527 13.334 36.055 0.50 19.45 C
ANISOU 1857 CD AGLN A 231 2800 2208 2380 -632 -649 -35 C
ATOM 1858 CD BGLN A 231 3.826 10.967 34.491 0.50 17.45 C
ANISOU 1858 CD BGLN A 231 2366 2317 1946 -254 -240 -484 C
ATOM 1859 OE1AGLN A 231 3.334 13.827 35.265 0.50 23.73 O
ANISOU 1859 OE1AGLN A 231 3281 2765 2970 -1609 -642 -11 O
ATOM 1860 OE1BGLN A 231 4.126 9.958 33.791 0.50 12.61 O
ANISOU 1860 OE1BGLN A 231 1663 2187 940 -595 -497 -285 O
ATOM 1861 NE2AGLN A 231 2.300 13.826 37.275 0.50 22.76 N
ANISOU 1861 NE2AGLN A 231 4552 1781 2314 -794 -1349 -297 N
ATOM 1862 NE2BGLN A 231 4.273 11.128 35.741 0.50 20.25 N
ANISOU 1862 NE2BGLN A 231 2842 2752 2097 -332 -167 -835 N
ATOM 1863 C GLN A 231 0.333 13.045 32.151 1.00 13.91 C
ANISOU 1863 C GLN A 231 2153 1634 1498 -407 238 -353 C
ATOM 1864 O GLN A 231 0.995 12.289 31.434 1.00 14.11 O
ANISOU 1864 O GLN A 231 2107 1651 1600 -511 256 -499 O
ATOM 1865 N PHE A 232 -0.573 13.895 31.664 1.00 12.73 N
ANISOU 1865 N PHE A 232 2250 1318 1267 -425 313 -502 N
ATOM 1866 CA PHE A 232 -0.897 14.022 30.237 1.00 13.89 C
ANISOU 1866 CA PHE A 232 2481 1441 1356 -419 174 -456 C
ATOM 1867 CB PHE A 232 -2.323 14.512 30.039 1.00 14.13 C
ANISOU 1867 CB PHE A 232 2546 1337 1486 -369 12 -523 C
ATOM 1868 CG PHE A 232 -3.368 13.584 30.595 1.00 13.64 C
ANISOU 1868 CG PHE A 232 2221 1331 1627 -198 -84 -317 C
ATOM 1869 CD1 PHE A 232 -3.788 13.667 31.918 1.00 14.26 C
ANISOU 1869 CD1 PHE A 232 2395 1366 1656 -272 -137 -443 C
ATOM 1870 CE1 PHE A 232 -4.729 12.779 32.419 1.00 14.25 C
ANISOU 1870 CE1 PHE A 232 1940 1775 1699 -82 -162 -344 C
ATOM 1871 CZ PHE A 232 -5.317 11.856 31.590 1.00 13.77 C
ANISOU 1871 CZ PHE A 232 1998 1494 1740 -74 -105 -267 C
ATOM 1872 CD2 PHE A 232 -3.952 12.630 29.788 1.00 13.76 C
ANISOU 1872 CD2 PHE A 232 2392 1356 1478 -103 -3 -406 C
ATOM 1873 CE2 PHE A 232 -4.906 11.768 30.288 1.00 13.05 C
ANISOU 1873 CE2 PHE A 232 1859 1318 1782 44 -155 -501 C
ATOM 1874 C PHE A 232 0.126 14.950 29.583 1.00 16.21 C
ANISOU 1874 C PHE A 232 2701 1810 1648 -551 316 -370 C
ATOM 1875 O PHE A 232 -0.195 16.048 29.081 1.00 17.76 O
ANISOU 1875 O PHE A 232 2945 1997 1804 -541 133 -240 O
ATOM 1876 N LYS A 233 1.367 14.471 29.587 1.00 16.98 N
ANISOU 1876 N LYS A 233 2648 1732 2071 -441 706 -506 N
ATOM 1877 CA LYS A 233 2.480 15.208 29.081 1.00 17.84 C
ANISOU 1877 CA LYS A 233 2694 2123 1960 -470 692 -323 C
ATOM 1878 CB LYS A 233 3.624 15.174 30.089 1.00 20.13 C
ANISOU 1878 CB LYS A 233 2722 2848 2076 -859 458 -164 C
ATOM 1879 CG LYS A 233 4.247 13.814 30.347 1.00 20.94 C
ANISOU 1879 CG LYS A 233 2837 3011 2104 -760 56 -103 C
ATOM 1880 CD LYS A 233 5.255 13.840 31.476 1.00 27.21 C
ANISOU 1880 CD LYS A 233 3159 4175 3002 -1331 -431 390 C
ATOM 1881 CE LYS A 233 5.984 12.524 31.588 1.00 31.46 C
ANISOU 1881 CE LYS A 233 3690 4856 3408 -1014 -759 905 C
ATOM 1882 NZ LYS A 233 7.054 12.592 32.607 1.00 40.42 N
ANISOU 1882 NZ LYS A 233 4488 6604 4262 -1591 -1360 1120 N
ATOM 1883 C LYS A 233 2.941 14.631 27.754 1.00 14.74 C
ANISOU 1883 C LYS A 233 2078 1547 1974 -239 607 -204 C
ATOM 1884 O LYS A 233 2.572 13.517 27.385 1.00 14.84 O
ANISOU 1884 O LYS A 233 1940 1592 2105 -351 395 -221 O
ATOM 1885 N PRO A 234 3.749 15.386 26.989 1.00 13.36 N
ANISOU 1885 N PRO A 234 1937 1349 1787 -261 405 -171 N
ATOM 1886 CA PRO A 234 4.092 14.958 25.632 1.00 15.10 C
ANISOU 1886 CA PRO A 234 2282 1692 1762 -256 351 -254 C
ATOM 1887 CB PRO A 234 5.038 16.061 25.147 1.00 15.82 C
ANISOU 1887 CB PRO A 234 2732 1538 1740 -199 382 -24 C
ATOM 1888 CG PRO A 234 4.601 17.278 25.924 1.00 16.28 C
ANISOU 1888 CG PRO A 234 2418 1977 1791 -203 565 -190 C
ATOM 1889 CD PRO A 234 4.282 16.727 27.308 1.00 14.81 C
ANISOU 1889 CD PRO A 234 2397 1467 1763 -313 600 -359 C
ATOM 1890 C PRO A 234 4.697 13.543 25.557 1.00 13.16 C
ANISOU 1890 C PRO A 234 2095 1573 1331 -392 373 -328 C
ATOM 1891 O PRO A 234 4.330 12.763 24.672 1.00 13.03 O
ANISOU 1891 O PRO A 234 2021 1479 1450 -321 -7 -308 O
ATOM 1892 N GLU A 235 5.600 13.190 26.482 1.00 14.69 N
ANISOU 1892 N GLU A 235 2232 1679 1671 -117 296 -274 N
ATOM 1893 CA GLU A 235 6.266 11.871 26.393 1.00 14.07 C
ANISOU 1893 CA GLU A 235 1896 1774 1676 -209 70 -426 C
ATOM 1894 CB GLU A 235 7.406 11.807 27.416 1.00 16.67 C
ANISOU 1894 CB GLU A 235 1919 2296 2118 -39 -125 -127 C
ATOM 1895 CG GLU A 235 8.197 10.527 27.343 1.00 19.75 C
ANISOU 1895 CG GLU A 235 2441 2436 2625 -53 101 -230 C
ATOM 1896 CD GLU A 235 9.548 10.563 28.044 1.00 25.40 C
ANISOU 1896 CD GLU A 235 3041 3196 3411 176 -486 -421 C
ATOM 1897 OE1 GLU A 235 9.839 11.574 28.747 1.00 31.71 O
ANISOU 1897 OE1 GLU A 235 4047 3544 4454 -183 -1053 -784 O
ATOM 1898 OE2 GLU A 235 10.296 9.548 27.937 1.00 28.87 O
ANISOU 1898 OE2 GLU A 235 3656 2989 4321 426 -904 -495 O
ATOM 1899 C GLU A 235 5.249 10.733 26.577 1.00 13.69 C
ANISOU 1899 C GLU A 235 1885 1645 1669 -93 111 -271 C
ATOM 1900 O GLU A 235 5.492 9.629 26.158 1.00 14.57 O
ANISOU 1900 O GLU A 235 1953 1562 2019 -144 201 -272 O
ATOM 1901 N ASN A 236 4.131 10.988 27.262 1.00 13.09 N
ANISOU 1901 N ASN A 236 1948 1449 1576 -227 90 -324 N
ATOM 1902 CA ASN A 236 3.130 9.942 27.466 1.00 12.36 C
ANISOU 1902 CA ASN A 236 1850 1311 1535 -96 68 -106 C
ATOM 1903 CB ASN A 236 2.392 10.106 28.794 1.00 12.44 C
ANISOU 1903 CB ASN A 236 1703 1522 1502 -19 -17 -154 C
ATOM 1904 CG ASN A 236 3.307 9.768 29.962 1.00 12.53 C
ANISOU 1904 CG ASN A 236 1488 1834 1438 -37 80 -107 C
ATOM 1905 OD1 ASN A 236 4.264 8.987 29.817 1.00 15.56 O
ANISOU 1905 OD1 ASN A 236 1935 2319 1657 358 94 -297 O
ATOM 1906 ND2 ASN A 236 3.019 10.330 31.128 1.00 15.29 N
ANISOU 1906 ND2 ASN A 236 2301 1988 1517 -245 154 -324 N
ATOM 1907 C ASN A 236 2.174 9.834 26.275 1.00 13.91 C
ANISOU 1907 C ASN A 236 2296 1379 1608 -271 -38 -317 C
ATOM 1908 O ASN A 236 1.643 8.738 26.047 1.00 15.22 O
ANISOU 1908 O ASN A 236 2523 1427 1830 -467 -270 -168 O
ATOM 1909 N MET A 237 1.946 10.923 25.531 1.00 12.83 N
ANISOU 1909 N MET A 237 2141 1414 1320 -321 0 -285 N
ATOM 1910 CA MET A 237 0.854 10.942 24.547 1.00 12.80 C
ANISOU 1910 CA MET A 237 2047 1497 1317 -328 58 -408 C
ATOM 1911 CB MET A 237 -0.074 12.131 24.789 1.00 12.05 C
ANISOU 1911 CB MET A 237 1679 1570 1328 -284 33 -332 C
ATOM 1912 CG MET A 237 -0.754 12.078 26.148 1.00 13.54 C
ANISOU 1912 CG MET A 237 2118 1661 1363 -100 146 -127 C
ATOM 1913 SD MET A 237 -2.076 13.284 26.278 1.00 15.09 S
ANISOU 1913 SD MET A 237 2340 1650 1741 -40 215 -243 S
ATOM 1914 CE MET A 237 -1.202 14.835 26.040 1.00 15.63 C
ANISOU 1914 CE MET A 237 2479 1425 2032 15 218 -422 C
ATOM 1915 C MET A 237 1.337 11.025 23.089 1.00 12.34 C
ANISOU 1915 C MET A 237 1863 1512 1312 -194 49 -337 C
ATOM 1916 O MET A 237 0.666 10.462 22.234 1.00 12.15 O
ANISOU 1916 O MET A 237 1760 1462 1392 -124 4 -343 O
ATOM 1917 N ILE A 238 2.384 11.802 22.796 1.00 12.76 N
ANISOU 1917 N ILE A 238 1702 1667 1478 -108 77 -471 N
ATOM 1918 CA ILE A 238 2.702 12.242 21.431 1.00 12.42 C
ANISOU 1918 CA ILE A 238 1525 1604 1590 -394 -24 -456 C
ATOM 1919 CB ILE A 238 3.215 13.700 21.439 1.00 13.62 C
ANISOU 1919 CB ILE A 238 1840 1598 1735 -433 30 -325 C
ATOM 1920 CG1 ILE A 238 2.205 14.640 22.106 1.00 14.70 C
ANISOU 1920 CG1 ILE A 238 2044 1771 1770 -437 103 -480 C
ATOM 1921 CG2 ILE A 238 3.579 14.140 20.025 1.00 15.00 C
ANISOU 1921 CG2 ILE A 238 1978 1760 1961 -344 216 -164 C
ATOM 1922 CD1 ILE A 238 0.887 14.764 21.422 1.00 16.63 C
ANISOU 1922 CD1 ILE A 238 2194 2053 2072 -271 24 -445 C
ATOM 1923 C ILE A 238 3.733 11.306 20.787 1.00 12.35 C
ANISOU 1923 C ILE A 238 1680 1552 1459 -293 30 -311 C
ATOM 1924 O ILE A 238 4.772 11.000 21.368 1.00 12.89 O
ANISOU 1924 O ILE A 238 1625 1689 1582 -240 41 -323 O
ATOM 1925 N GLY A 239 3.419 10.871 19.567 1.00 11.63 N
ANISOU 1925 N GLY A 239 1669 1339 1409 -288 195 -304 N
ATOM 1926 CA GLY A 239 4.350 10.089 18.759 1.00 11.79 C
ANISOU 1926 CA GLY A 239 1783 1147 1546 -255 259 -301 C
ATOM 1927 C GLY A 239 4.836 10.857 17.541 1.00 11.99 C
ANISOU 1927 C GLY A 239 1703 1372 1480 -266 119 -199 C
ATOM 1928 O GLY A 239 4.046 11.498 16.848 1.00 12.92 O
ANISOU 1928 O GLY A 239 1697 1552 1659 -126 106 -60 O
ATOM 1929 N ILE A 240 6.142 10.784 17.285 1.00 12.71 N
ANISOU 1929 N ILE A 240 1853 1393 1581 -81 134 -177 N
ATOM 1930 CA ILE A 240 6.771 11.457 16.154 1.00 12.26 C
ANISOU 1930 CA ILE A 240 1781 1382 1496 -239 81 -217 C
ATOM 1931 CB ILE A 240 7.523 12.736 16.561 1.00 12.90 C
ANISOU 1931 CB ILE A 240 1780 1447 1674 -301 62 -252 C
ATOM 1932 CG1 ILE A 240 6.632 13.715 17.338 1.00 13.27 C
ANISOU 1932 CG1 ILE A 240 2011 1331 1697 -387 290 -177 C
ATOM 1933 CG2 ILE A 240 8.172 13.376 15.339 1.00 13.83 C
ANISOU 1933 CG2 ILE A 240 2022 1452 1779 -327 86 -187 C
ATOM 1934 CD1 ILE A 240 7.372 14.879 17.960 1.00 14.87 C
ANISOU 1934 CD1 ILE A 240 2314 1322 2014 -335 139 -319 C
ATOM 1935 C ILE A 240 7.701 10.446 15.482 1.00 11.77 C
ANISOU 1935 C ILE A 240 1678 1386 1407 -225 83 -154 C
ATOM 1936 O ILE A 240 8.574 9.877 16.108 1.00 13.33 O
ANISOU 1936 O ILE A 240 1672 1657 1733 -19 18 -130 O
ATOM 1937 N ALA A 241 7.485 10.213 14.183 1.00 11.47 N
ANISOU 1937 N ALA A 241 1583 1271 1501 -222 -126 -188 N
ATOM 1938 CA ALA A 241 8.325 9.291 13.445 1.00 11.82 C
ANISOU 1938 CA ALA A 241 1635 1275 1580 -241 155 -168 C
ATOM 1939 CB ALA A 241 7.909 9.256 12.004 1.00 12.46 C
ANISOU 1939 CB ALA A 241 1749 1377 1608 -143 136 -89 C
ATOM 1940 C ALA A 241 9.808 9.663 13.567 1.00 12.68 C
ANISOU 1940 C ALA A 241 1606 1468 1744 -69 246 -324 C
ATOM 1941 O ALA A 241 10.193 10.849 13.605 1.00 13.36 O
ANISOU 1941 O ALA A 241 1801 1545 1730 -176 458 -346 O
ATOM 1942 N ASP A 242 10.640 8.620 13.564 1.00 12.43 N
ANISOU 1942 N ASP A 242 1640 1202 1881 -127 321 -209 N
ATOM 1943 CA ASP A 242 12.084 8.732 13.745 1.00 14.15 C
ANISOU 1943 CA ASP A 242 1676 1553 2144 -303 259 -221 C
ATOM 1944 CB ASP A 242 12.621 7.373 14.191 1.00 14.31 C
ANISOU 1944 CB ASP A 242 1540 1581 2313 -238 116 -332 C
ATOM 1945 CG ASP A 242 12.026 6.996 15.531 1.00 17.10 C
ANISOU 1945 CG ASP A 242 2167 2046 2283 -410 -2 -238 C
ATOM 1946 OD1 ASP A 242 12.464 7.624 16.534 1.00 20.15 O
ANISOU 1946 OD1 ASP A 242 2854 2679 2122 -899 -173 -174 O
ATOM 1947 OD2 ASP A 242 11.097 6.147 15.565 1.00 14.52 O
ANISOU 1947 OD2 ASP A 242 1927 1686 1902 -198 37 -308 O
ATOM 1948 C ASP A 242 12.790 9.316 12.522 1.00 14.20 C
ANISOU 1948 C ASP A 242 1514 1788 2092 -324 288 -338 C
ATOM 1949 O ASP A 242 13.974 9.631 12.647 1.00 19.02 O
ANISOU 1949 O ASP A 242 1518 3187 2519 -645 315 -62 O
ATOM 1950 N ASP A 243 12.089 9.504 11.397 1.00 14.91 N
ANISOU 1950 N ASP A 243 1703 1871 2090 -362 277 -180 N
ATOM 1951 CA ASP A 243 12.698 10.120 10.223 1.00 15.59 C
ANISOU 1951 CA ASP A 243 1998 1736 2188 -377 303 3 C
ATOM 1952 CB ASP A 243 12.555 9.250 8.966 1.00 15.65 C
ANISOU 1952 CB ASP A 243 2181 1727 2035 -445 700 6 C
ATOM 1953 CG ASP A 243 11.154 8.983 8.440 1.00 16.09 C
ANISOU 1953 CG ASP A 243 2326 1836 1950 -545 549 -55 C
ATOM 1954 OD1 ASP A 243 10.175 9.203 9.175 1.00 15.66 O
ANISOU 1954 OD1 ASP A 243 2082 1832 2035 -233 375 116 O
ATOM 1955 OD2 ASP A 243 11.061 8.501 7.282 1.00 19.85 O
ANISOU 1955 OD2 ASP A 243 2776 2720 2043 -738 417 -206 O
ATOM 1956 C ASP A 243 12.215 11.554 9.991 1.00 16.12 C
ANISOU 1956 C ASP A 243 2083 1801 2238 -363 502 -37 C
ATOM 1957 O ASP A 243 12.607 12.148 8.966 1.00 20.11 O
ANISOU 1957 O ASP A 243 2869 2287 2484 -617 915 73 O
ATOM 1958 N VAL A 244 11.494 12.152 10.939 1.00 14.88 N
ANISOU 1958 N VAL A 244 1962 1731 1960 -610 471 -17 N
ATOM 1959 CA VAL A 244 11.311 13.611 10.898 1.00 14.98 C
ANISOU 1959 CA VAL A 244 2034 1812 1844 -424 337 -148 C
ATOM 1960 CB VAL A 244 10.255 14.097 11.906 1.00 14.74 C
ANISOU 1960 CB VAL A 244 1916 1823 1860 -294 194 -210 C
ATOM 1961 CG1 VAL A 244 10.124 15.616 11.890 1.00 14.81 C
ANISOU 1961 CG1 VAL A 244 2090 1809 1727 -157 281 -386 C
ATOM 1962 CG2 VAL A 244 8.896 13.460 11.652 1.00 14.65 C
ANISOU 1962 CG2 VAL A 244 1840 1803 1921 -199 58 -184 C
ATOM 1963 C VAL A 244 12.670 14.267 11.181 1.00 15.72 C
ANISOU 1963 C VAL A 244 2086 1865 2022 -613 577 -154 C
ATOM 1964 O VAL A 244 13.351 13.913 12.144 1.00 17.70 O
ANISOU 1964 O VAL A 244 2363 1903 2456 -370 273 -280 O
ATOM 1965 N LYS A 245 13.041 15.251 10.356 1.00 16.67 N
ANISOU 1965 N LYS A 245 2297 1985 2049 -630 492 -77 N
ATOM 1966 CA LYS A 245 14.324 15.930 10.516 1.00 19.01 C
ANISOU 1966 CA LYS A 245 2418 2206 2598 -726 460 -273 C
ATOM 1967 CB LYS A 245 14.841 16.387 9.150 1.00 21.18 C
ANISOU 1967 CB LYS A 245 2731 2449 2868 -880 972 -282 C
ATOM 1968 CG LYS A 245 15.113 15.246 8.174 1.00 25.13 C
ANISOU 1968 CG LYS A 245 3263 3083 3201 -611 1129 -621 C
ATOM 1969 CD LYS A 245 15.676 15.759 6.859 1.00 31.19 C
ANISOU 1969 CD LYS A 245 4493 3616 3738 -586 1407 -63 C
ATOM 1970 CE LYS A 245 16.008 14.682 5.846 1.00 38.84 C
ANISOU 1970 CE LYS A 245 5595 4533 4628 235 1364 -685 C
ATOM 1971 NZ LYS A 245 16.855 13.622 6.440 1.00 45.45 N
ANISOU 1971 NZ LYS A 245 5880 5729 5657 565 849 -428 N
ATOM 1972 C LYS A 245 14.191 17.103 11.496 1.00 18.23 C
ANISOU 1972 C LYS A 245 2151 2163 2612 -562 495 -184 C
ATOM 1973 O LYS A 245 13.154 17.777 11.566 1.00 17.90 O
ANISOU 1973 O LYS A 245 1946 1982 2870 -650 283 -108 O
ATOM 1974 N LEU A 246 15.287 17.347 12.220 1.00 18.68 N
ANISOU 1974 N LEU A 246 1979 2198 2918 -722 451 -233 N
ATOM 1975 CA LEU A 246 15.416 18.381 13.223 1.00 20.56 C
ANISOU 1975 CA LEU A 246 2175 2408 3226 -814 456 -436 C
ATOM 1976 CB LEU A 246 16.224 17.814 14.395 1.00 22.96 C
ANISOU 1976 CB LEU A 246 2821 2706 3196 -748 205 -521 C
ATOM 1977 CG LEU A 246 15.510 16.782 15.265 1.00 24.46 C
ANISOU 1977 CG LEU A 246 2670 3241 3381 -533 489 -221 C
ATOM 1978 CD1 LEU A 246 16.515 15.799 15.880 1.00 28.55 C
ANISOU 1978 CD1 LEU A 246 3338 3481 4028 -372 -14 -165 C
ATOM 1979 CD2 LEU A 246 14.715 17.473 16.358 1.00 23.58 C
ANISOU 1979 CD2 LEU A 246 2620 3032 3305 -585 436 -262 C
ATOM 1980 C LEU A 246 16.139 19.607 12.655 1.00 21.97 C
ANISOU 1980 C LEU A 246 2355 2622 3369 -840 753 -314 C
ATOM 1981 O LEU A 246 17.069 19.515 11.821 1.00 24.43 O
ANISOU 1981 O LEU A 246 2478 2785 4018 -1324 1047 -810 O
ATOM 1982 N VAL A 247 15.767 20.765 13.208 1.00 22.19 N
ANISOU 1982 N VAL A 247 2303 2722 3403 -1082 715 -529 N
ATOM 1983 CA AVAL A 247 16.502 21.991 12.984 0.50 24.38 C
ANISOU 1983 CA AVAL A 247 2386 2833 4043 -1133 570 -402 C
ATOM 1984 CA BVAL A 247 16.499 22.013 13.027 0.50 22.07 C
ANISOU 1984 CA BVAL A 247 2317 2463 3602 -883 757 -591 C
ATOM 1985 CB AVAL A 247 15.801 23.172 13.677 0.50 27.63 C
ANISOU 1985 CB AVAL A 247 2981 3145 4371 -869 551 -598 C
ATOM 1986 CB BVAL A 247 15.825 23.148 13.826 0.50 20.94 C
ANISOU 1986 CB BVAL A 247 2390 2229 3337 -964 774 -537 C
ATOM 1987 CG1AVAL A 247 16.095 23.219 15.159 0.50 29.08 C
ANISOU 1987 CG1AVAL A 247 3079 3444 4525 -726 253 -374 C
ATOM 1988 CG1BVAL A 247 16.734 24.346 14.057 0.50 21.37 C
ANISOU 1988 CG1BVAL A 247 2483 2245 3390 -1029 773 -371 C
ATOM 1989 CG2AVAL A 247 16.168 24.489 13.026 0.50 29.65 C
ANISOU 1989 CG2AVAL A 247 3282 3390 4593 -764 362 -250 C
ATOM 1990 CG2BVAL A 247 14.517 23.571 13.176 0.50 17.22 C
ANISOU 1990 CG2BVAL A 247 2189 1428 2923 -965 905 -607 C
ATOM 1991 C VAL A 247 17.952 21.801 13.467 1.00 25.39 C
ANISOU 1991 C VAL A 247 2471 3051 4125 -1007 522 -567 C
ATOM 1992 O VAL A 247 18.223 21.069 14.421 1.00 26.11 O
ANISOU 1992 O VAL A 247 2640 3137 4143 -782 534 -519 O
ATOM 1993 N ALA A 248 18.881 22.446 12.760 1.00 28.02 N
ANISOU 1993 N ALA A 248 2233 3445 4965 -1177 512 -308 N
ATOM 1994 CA ALA A 248 20.299 22.314 13.074 1.00 32.42 C
ANISOU 1994 CA ALA A 248 2257 4294 5766 -1201 400 -531 C
ATOM 1995 CB ALA A 248 21.115 23.153 12.129 1.00 36.13 C
ANISOU 1995 CB ALA A 248 3026 4552 6147 -1379 494 -204 C
ATOM 1996 C ALA A 248 20.541 22.706 14.537 1.00 33.88 C
ANISOU 1996 C ALA A 248 2517 4425 5929 -1387 320 -731 C
ATOM 1997 O ALA A 248 20.039 23.724 15.001 1.00 35.81 O
ANISOU 1997 O ALA A 248 3334 4885 5385 -1250 450 -1071 O
ATOM 1998 N GLY A 249 21.286 21.856 15.258 1.00 36.49 N
ANISOU 1998 N GLY A 249 2711 5040 6111 -1766 -195 -701 N
ATOM 1999 CA GLY A 249 21.731 22.115 16.635 1.00 37.02 C
ANISOU 1999 CA GLY A 249 2590 5268 6205 -1895 -235 -1109 C
ATOM 2000 C GLY A 249 20.761 21.618 17.697 1.00 37.11 C
ANISOU 2000 C GLY A 249 2463 5704 5931 -1643 -439 -1163 C
ATOM 2001 O GLY A 249 21.048 21.748 18.886 1.00 43.34 O
ANISOU 2001 O GLY A 249 3465 6694 6308 -1932 -971 -308 O
ATOM 2002 N LYS A 250 19.603 21.082 17.286 1.00 32.34 N
ANISOU 2002 N LYS A 250 1945 4917 5422 -1133 -56 -1273 N
ATOM 2003 CA LYS A 250 18.631 20.524 18.232 1.00 33.68 C
ANISOU 2003 CA LYS A 250 2373 5002 5421 -1083 46 -1218 C
ATOM 2004 CB LYS A 250 17.217 20.976 17.866 1.00 33.11 C
ANISOU 2004 CB LYS A 250 2283 4906 5388 -1102 28 -1406 C
ATOM 2005 CG LYS A 250 16.956 22.465 18.016 1.00 33.09 C
ANISOU 2005 CG LYS A 250 2092 4985 5493 -967 -349 -1709 C
ATOM 2006 CD LYS A 250 17.122 22.985 19.428 1.00 36.59 C
ANISOU 2006 CD LYS A 250 2970 5182 5747 -951 -629 -2070 C
ATOM 2007 CE LYS A 250 16.594 24.398 19.578 1.00 39.72 C
ANISOU 2007 CE LYS A 250 3851 5291 5947 -850 -924 -2478 C
ATOM 2008 NZ LYS A 250 16.743 24.901 20.965 1.00 44.35 N
ANISOU 2008 NZ LYS A 250 4712 5948 6191 -663 -1410 -2521 N
ATOM 2009 C LYS A 250 18.719 18.993 18.230 1.00 34.13 C
ANISOU 2009 C LYS A 250 2667 5093 5207 -641 381 -958 C
ATOM 2010 O LYS A 250 18.723 18.386 17.169 1.00 35.72 O
ANISOU 2010 O LYS A 250 3513 4587 5469 117 477 -1153 O
ATOM 2011 N ALA A 251 18.735 18.401 19.432 1.00 35.00 N
ANISOU 2011 N ALA A 251 2668 5477 5153 -323 -448 -779 N
ATOM 2012 CA ALA A 251 18.868 16.962 19.646 1.00 36.51 C
ANISOU 2012 CA ALA A 251 2470 5559 5839 -224 -612 -285 C
ATOM 2013 CB ALA A 251 19.536 16.728 20.977 1.00 41.38 C
ANISOU 2013 CB ALA A 251 3037 6413 6270 -630 -1236 -236 C
ATOM 2014 C ALA A 251 17.522 16.217 19.594 1.00 33.85 C
ANISOU 2014 C ALA A 251 2583 4935 5340 -291 -338 -268 C
ATOM 2015 O ALA A 251 17.494 15.046 19.261 1.00 36.02 O
ANISOU 2015 O ALA A 251 2663 4906 6117 118 398 -99 O
ATOM 2016 N ASP A 252 16.418 16.868 19.982 1.00 27.99 N
ANISOU 2016 N ASP A 252 2865 3452 4315 -420 -816 -336 N
ATOM 2017 CA ASP A 252 15.095 16.231 19.993 1.00 26.03 C
ANISOU 2017 CA ASP A 252 2194 3909 3785 16 -168 48 C
ATOM 2018 CB ASP A 252 14.835 15.371 21.257 1.00 27.94 C
ANISOU 2018 CB ASP A 252 2712 4033 3871 18 -269 280 C
ATOM 2019 CG ASP A 252 13.740 14.269 21.209 1.00 27.59 C
ANISOU 2019 CG ASP A 252 3384 3724 3373 -154 -255 360 C
ATOM 2020 OD1 ASP A 252 13.030 14.127 20.149 1.00 21.90 O
ANISOU 2020 OD1 ASP A 252 2449 2718 3151 -574 234 194 O
ATOM 2021 OD2 ASP A 252 13.529 13.541 22.280 1.00 24.60 O
ANISOU 2021 OD2 ASP A 252 2668 2554 4125 -771 -249 332 O
ATOM 2022 C ASP A 252 14.070 17.358 19.812 1.00 21.03 C
ANISOU 2022 C ASP A 252 2387 3251 2349 -311 -74 -440 C
ATOM 2023 O ASP A 252 14.387 18.552 19.903 1.00 24.25 O
ANISOU 2023 O ASP A 252 2684 3407 3122 -573 253 -892 O
ATOM 2024 N PHE A 253 12.839 16.950 19.517 1.00 19.40 N
ANISOU 2024 N PHE A 253 2211 2916 2245 -420 74 -346 N
ATOM 2025 CA PHE A 253 11.724 17.856 19.453 1.00 17.62 C
ANISOU 2025 CA PHE A 253 1932 2579 2182 -521 316 -337 C
ATOM 2026 CB PHE A 253 10.525 17.174 18.794 1.00 17.41 C
ANISOU 2026 CB PHE A 253 1925 2495 2192 -492 250 -122 C
ATOM 2027 CG PHE A 253 10.896 16.627 17.449 1.00 18.47 C
ANISOU 2027 CG PHE A 253 2192 2485 2338 -170 335 -300 C
ATOM 2028 CD1 PHE A 253 10.999 17.458 16.344 1.00 18.83 C
ANISOU 2028 CD1 PHE A 253 2463 2345 2347 -247 302 -383 C
ATOM 2029 CE1 PHE A 253 11.419 16.958 15.117 1.00 18.23 C
ANISOU 2029 CE1 PHE A 253 2541 2420 1961 -277 253 -145 C
ATOM 2030 CZ PHE A 253 11.742 15.629 14.995 1.00 17.64 C
ANISOU 2030 CZ PHE A 253 2228 2575 1896 -155 122 -473 C
ATOM 2031 CD2 PHE A 253 11.225 15.290 17.307 1.00 18.51 C
ANISOU 2031 CD2 PHE A 253 2371 2404 2257 -212 -3 -369 C
ATOM 2032 CE2 PHE A 253 11.664 14.807 16.088 1.00 18.26 C
ANISOU 2032 CE2 PHE A 253 2225 2339 2373 -89 95 -435 C
ATOM 2033 C PHE A 253 11.400 18.375 20.847 1.00 18.56 C
ANISOU 2033 C PHE A 253 2263 2816 1972 -600 -88 -347 C
ATOM 2034 O PHE A 253 11.625 17.696 21.839 1.00 20.11 O
ANISOU 2034 O PHE A 253 2761 2731 2148 -456 -151 -138 O
ATOM 2035 N GLU A 254 10.866 19.599 20.884 1.00 20.51 N
ANISOU 2035 N GLU A 254 2570 2833 2391 -425 236 -314 N
ATOM 2036 CA GLU A 254 10.327 20.204 22.112 1.00 20.93 C
ANISOU 2036 CA GLU A 254 2423 3125 2405 -250 311 -296 C
ATOM 2037 CB GLU A 254 10.977 21.564 22.361 1.00 24.49 C
ANISOU 2037 CB GLU A 254 2953 3662 2689 -659 87 -836 C
ATOM 2038 CG GLU A 254 10.470 22.294 23.598 1.00 30.97 C
ANISOU 2038 CG GLU A 254 3977 4137 3653 -440 594 -1267 C
ATOM 2039 CD GLU A 254 11.089 23.675 23.822 1.00 37.54 C
ANISOU 2039 CD GLU A 254 4738 4944 4580 -1166 838 -2082 C
ATOM 2040 OE1 GLU A 254 12.051 24.041 23.093 1.00 44.95 O
ANISOU 2040 OE1 GLU A 254 5456 6285 5336 -1716 1279 -1848 O
ATOM 2041 OE2 GLU A 254 10.594 24.400 24.708 1.00 49.04 O
ANISOU 2041 OE2 GLU A 254 6763 5962 5906 36 1508 -2373 O
ATOM 2042 C GLU A 254 8.820 20.331 21.904 1.00 19.26 C
ANISOU 2042 C GLU A 254 2329 3030 1957 -438 366 -306 C
ATOM 2043 O GLU A 254 8.381 20.916 20.913 1.00 21.33 O
ANISOU 2043 O GLU A 254 2332 3780 1990 -563 437 146 O
ATOM 2044 N VAL A 255 8.052 19.743 22.823 1.00 16.41 N
ANISOU 2044 N VAL A 255 2310 2029 1894 -314 240 -336 N
ATOM 2045 CA VAL A 255 6.608 19.689 22.675 1.00 16.59 C
ANISOU 2045 CA VAL A 255 2276 1990 2035 -388 240 -209 C
ATOM 2046 CB VAL A 255 6.122 18.260 22.425 1.00 16.99 C
ANISOU 2046 CB VAL A 255 2701 1999 1753 -447 249 13 C
ATOM 2047 CG1 VAL A 255 4.612 18.222 22.256 1.00 17.42 C
ANISOU 2047 CG1 VAL A 255 2696 2024 1895 -579 99 -2 C
ATOM 2048 CG2 VAL A 255 6.821 17.657 21.213 1.00 18.58 C
ANISOU 2048 CG2 VAL A 255 2851 2276 1932 -263 361 -110 C
ATOM 2049 C VAL A 255 5.957 20.274 23.927 1.00 15.32 C
ANISOU 2049 C VAL A 255 2008 1915 1897 -660 203 -214 C
ATOM 2050 O VAL A 255 6.384 19.985 25.045 1.00 16.31 O
ANISOU 2050 O VAL A 255 2380 1902 1915 -391 167 -150 O
ATOM 2051 N ASP A 256 4.926 21.104 23.717 1.00 16.16 N
ANISOU 2051 N ASP A 256 2042 2270 1826 -490 294 -293 N
ATOM 2052 CA AASP A 256 4.168 21.756 24.782 0.50 16.04 C
ANISOU 2052 CA AASP A 256 2011 2270 1813 -539 286 -343 C
ATOM 2053 CA BASP A 256 4.183 21.621 24.861 0.50 16.49 C
ANISOU 2053 CA BASP A 256 2069 2406 1789 -495 366 -251 C
ATOM 2054 CB AASP A 256 4.335 23.271 24.696 0.50 17.72 C
ANISOU 2054 CB AASP A 256 1955 2319 2459 -558 193 -554 C
ATOM 2055 CB BASP A 256 4.598 23.037 25.263 0.50 18.66 C
ANISOU 2055 CB BASP A 256 2453 2475 2159 -505 524 -381 C
ATOM 2056 CG AASP A 256 5.774 23.721 24.861 0.50 20.65 C
ANISOU 2056 CG AASP A 256 2116 2677 3054 -879 118 -771 C
ATOM 2057 CG BASP A 256 4.078 24.115 24.346 0.50 21.17 C
ANISOU 2057 CG BASP A 256 2802 2735 2506 -378 390 -200 C
ATOM 2058 OD1AASP A 256 6.418 23.219 25.787 0.50 25.37 O
ANISOU 2058 OD1AASP A 256 2226 3095 4315 -926 -657 -897 O
ATOM 2059 OD1BASP A 256 4.757 24.376 23.329 0.50 23.89 O
ANISOU 2059 OD1BASP A 256 3049 3341 2686 -298 637 -250 O
ATOM 2060 OD2AASP A 256 6.222 24.571 24.066 0.50 27.23 O
ANISOU 2060 OD2AASP A 256 2556 3430 4360 -1470 13 -276 O
ATOM 2061 OD2BASP A 256 3.022 24.714 24.694 0.50 21.62 O
ANISOU 2061 OD2BASP A 256 2976 2274 2962 -444 548 -496 O
ATOM 2062 C ASP A 256 2.683 21.420 24.641 1.00 15.79 C
ANISOU 2062 C ASP A 256 2143 2143 1714 -631 149 -287 C
ATOM 2063 O ASP A 256 2.152 21.552 23.539 1.00 16.87 O
ANISOU 2063 O ASP A 256 2225 2710 1473 -907 285 -285 O
ATOM 2064 N ILE A 257 2.033 21.071 25.752 1.00 15.25 N
ANISOU 2064 N ILE A 257 2205 2042 1546 -360 77 -175 N
ATOM 2065 CA ILE A 257 0.599 20.851 25.857 1.00 14.05 C
ANISOU 2065 CA ILE A 257 2127 1816 1395 -411 34 -307 C
ATOM 2066 CB ILE A 257 0.291 19.634 26.751 1.00 14.56 C
ANISOU 2066 CB ILE A 257 2182 1929 1420 -459 8 -260 C
ATOM 2067 CG1 ILE A 257 1.019 18.372 26.281 1.00 16.10 C
ANISOU 2067 CG1 ILE A 257 2208 1998 1910 -329 14 -243 C
ATOM 2068 CG2 ILE A 257 -1.210 19.414 26.890 1.00 14.74 C
ANISOU 2068 CG2 ILE A 257 2236 1942 1423 -477 49 -172 C
ATOM 2069 CD1 ILE A 257 0.686 17.937 24.867 1.00 17.07 C
ANISOU 2069 CD1 ILE A 257 2407 2051 2028 -222 -20 -366 C
ATOM 2070 C ILE A 257 -0.033 22.111 26.441 1.00 14.26 C
ANISOU 2070 C ILE A 257 1938 1805 1673 -426 240 -175 C
ATOM 2071 O ILE A 257 0.392 22.579 27.507 1.00 17.13 O
ANISOU 2071 O ILE A 257 2323 2338 1845 -479 342 -530 O
ATOM 2072 N THR A 258 -1.072 22.601 25.763 1.00 13.49 N
ANISOU 2072 N THR A 258 1930 1617 1576 -392 196 -360 N
ATOM 2073 CA THR A 258 -1.859 23.699 26.250 1.00 14.16 C
ANISOU 2073 CA THR A 258 2153 1539 1688 -436 442 -554 C
ATOM 2074 CB THR A 258 -1.476 25.027 25.575 1.00 16.44 C
ANISOU 2074 CB THR A 258 2267 1776 2203 -447 592 -312 C
ATOM 2075 OG1 THR A 258 -1.729 24.930 24.171 1.00 17.74 O
ANISOU 2075 OG1 THR A 258 2651 1948 2140 -389 536 -68 O
ATOM 2076 CG2 THR A 258 -0.027 25.420 25.803 1.00 17.57 C
ANISOU 2076 CG2 THR A 258 2464 1940 2269 -613 598 -368 C
ATOM 2077 C THR A 258 -3.346 23.404 26.039 1.00 13.99 C
ANISOU 2077 C THR A 258 2166 1354 1792 -356 368 -269 C
ATOM 2078 O THR A 258 -3.727 22.530 25.235 1.00 14.34 O
ANISOU 2078 O THR A 258 2095 1735 1618 -453 431 -427 O
ATOM 2079 N GLY A 259 -4.192 24.159 26.749 1.00 13.70 N
ANISOU 2079 N GLY A 259 2340 1169 1696 -347 246 -392 N
ATOM 2080 CA GLY A 259 -5.643 24.043 26.558 1.00 14.14 C
ANISOU 2080 CA GLY A 259 2300 1355 1714 -379 361 -343 C
ATOM 2081 C GLY A 259 -6.192 22.700 27.005 1.00 13.85 C
ANISOU 2081 C GLY A 259 2253 1264 1742 -303 260 -418 C
ATOM 2082 O GLY A 259 -7.262 22.288 26.549 1.00 14.92 O
ANISOU 2082 O GLY A 259 2223 1542 1903 -411 194 -84 O
ATOM 2083 N PHE A 260 -5.472 22.003 27.893 1.00 12.89 N
ANISOU 2083 N PHE A 260 1988 1307 1602 -520 214 -307 N
ATOM 2084 CA PHE A 260 -5.899 20.653 28.291 1.00 12.87 C
ANISOU 2084 CA PHE A 260 2149 1251 1487 -436 340 -407 C
ATOM 2085 CB PHE A 260 -4.823 19.982 29.146 1.00 13.68 C
ANISOU 2085 CB PHE A 260 1976 1562 1658 -225 415 -427 C
ATOM 2086 CG PHE A 260 -5.169 18.594 29.592 1.00 13.36 C
ANISOU 2086 CG PHE A 260 1972 1520 1581 -312 153 -458 C
ATOM 2087 CD1 PHE A 260 -4.903 17.512 28.770 1.00 13.07 C
ANISOU 2087 CD1 PHE A 260 2049 1258 1656 -429 69 -344 C
ATOM 2088 CE1 PHE A 260 -5.220 16.230 29.179 1.00 13.98 C
ANISOU 2088 CE1 PHE A 260 2376 1014 1919 -212 -20 -451 C
ATOM 2089 CZ PHE A 260 -5.851 16.020 30.374 1.00 14.31 C
ANISOU 2089 CZ PHE A 260 2149 1254 2034 -244 -6 -71 C
ATOM 2090 CD2 PHE A 260 -5.814 18.359 30.794 1.00 12.81 C
ANISOU 2090 CD2 PHE A 260 1864 1349 1654 -366 117 -462 C
ATOM 2091 CE2 PHE A 260 -6.133 17.073 31.196 1.00 14.70 C
ANISOU 2091 CE2 PHE A 260 2171 1549 1863 -389 186 -174 C
ATOM 2092 C PHE A 260 -7.252 20.692 29.018 1.00 13.03 C
ANISOU 2092 C PHE A 260 2075 1242 1633 -405 324 -295 C
ATOM 2093 O PHE A 260 -7.451 21.485 29.957 1.00 14.21 O
ANISOU 2093 O PHE A 260 2226 1600 1572 -413 344 -428 O
ATOM 2094 N LYS A 261 -8.149 19.788 28.588 1.00 11.65 N
ANISOU 2094 N LYS A 261 1915 1192 1317 -247 249 -308 N
ATOM 2095 CA LYS A 261 -9.443 19.567 29.204 1.00 12.07 C
ANISOU 2095 CA LYS A 261 1908 1215 1463 -310 259 -243 C
ATOM 2096 CB LYS A 261 -10.553 20.206 28.371 1.00 14.04 C
ANISOU 2096 CB LYS A 261 1759 1586 1988 -133 280 -184 C
ATOM 2097 CG LYS A 261 -10.468 21.723 28.250 1.00 17.15 C
ANISOU 2097 CG LYS A 261 2184 1587 2744 -178 106 -47 C
ATOM 2098 CD LYS A 261 -10.701 22.443 29.561 1.00 21.25 C
ANISOU 2098 CD LYS A 261 3013 1987 3073 -199 173 -293 C
ATOM 2099 CE LYS A 261 -10.548 23.949 29.502 1.00 26.49 C
ANISOU 2099 CE LYS A 261 3526 2045 4494 -118 498 -518 C
ATOM 2100 NZ LYS A 261 -10.615 24.558 30.864 1.00 32.85 N
ANISOU 2100 NZ LYS A 261 4342 2619 5520 160 33 -1287 N
ATOM 2101 C LYS A 261 -9.693 18.067 29.321 1.00 11.30 C
ANISOU 2101 C LYS A 261 1764 1203 1324 -207 267 -257 C
ATOM 2102 O LYS A 261 -9.222 17.275 28.483 1.00 11.91 O
ANISOU 2102 O LYS A 261 1769 1324 1433 -279 435 -321 O
ATOM 2103 N ILE A 262 -10.480 17.687 30.322 1.00 10.96 N
ANISOU 2103 N ILE A 262 1755 1122 1288 -188 330 -382 N
ATOM 2104 CA ILE A 262 -10.822 16.293 30.537 1.00 11.53 C
ANISOU 2104 CA ILE A 262 1819 1189 1370 -298 232 -354 C
ATOM 2105 CB ILE A 262 -9.753 15.572 31.376 1.00 12.24 C
ANISOU 2105 CB ILE A 262 1807 1417 1424 -313 187 -269 C
ATOM 2106 CG1 ILE A 262 -10.031 14.075 31.485 1.00 12.23 C
ANISOU 2106 CG1 ILE A 262 1574 1438 1635 -323 144 -210 C
ATOM 2107 CG2 ILE A 262 -9.616 16.215 32.741 1.00 13.32 C
ANISOU 2107 CG2 ILE A 262 1929 1676 1454 -242 107 -337 C
ATOM 2108 CD1 ILE A 262 -8.903 13.271 32.117 1.00 13.04 C
ANISOU 2108 CD1 ILE A 262 2027 1529 1396 -209 51 -61 C
ATOM 2109 C ILE A 262 -12.213 16.195 31.174 1.00 11.45 C
ANISOU 2109 C ILE A 262 1772 1257 1322 -175 254 -231 C
ATOM 2110 O ILE A 262 -12.560 16.955 32.088 1.00 13.51 O
ANISOU 2110 O ILE A 262 1962 1625 1546 -207 492 -418 O
ATOM 2111 N ASN A 263 -13.010 15.251 30.660 1.00 11.51 N
ANISOU 2111 N ASN A 263 1931 1197 1242 -190 330 -219 N
ATOM 2112 CA AASN A 263 -14.295 14.918 31.225 0.50 11.92 C
ANISOU 2112 CA AASN A 263 1862 1292 1375 -198 229 -180 C
ATOM 2113 CA BASN A 263 -14.299 14.917 31.219 0.50 11.60 C
ANISOU 2113 CA BASN A 263 1790 1276 1343 -212 276 -176 C
ATOM 2114 CB AASN A 263 -15.457 15.408 30.366 0.50 13.60 C
ANISOU 2114 CB AASN A 263 2169 1502 1494 -37 108 -19 C
ATOM 2115 CB BASN A 263 -15.453 15.435 30.360 0.50 11.43 C
ANISOU 2115 CB BASN A 263 1675 1302 1365 -209 403 0 C
ATOM 2116 CG AASN A 263 -15.586 16.908 30.246 0.50 15.24 C
ANISOU 2116 CG AASN A 263 2488 1549 1750 -15 -175 114 C
ATOM 2117 CG BASN A 263 -15.530 16.945 30.308 0.50 11.24 C
ANISOU 2117 CG BASN A 263 1560 1302 1406 -296 407 100 C
ATOM 2118 OD1AASN A 263 -16.233 17.375 29.304 0.50 18.84 O
ANISOU 2118 OD1AASN A 263 2890 2075 2194 144 -513 320 O
ATOM 2119 OD1BASN A 263 -14.835 17.579 29.498 0.50 12.90 O
ANISOU 2119 OD1BASN A 263 1487 1670 1745 -554 442 195 O
ATOM 2120 ND2AASN A 263 -15.024 17.657 31.175 0.50 16.96 N
ANISOU 2120 ND2AASN A 263 3100 1695 1647 79 -273 7 N
ATOM 2121 ND2BASN A 263 -16.306 17.517 31.206 0.50 10.60 N
ANISOU 2121 ND2BASN A 263 1441 1086 1498 -235 418 182 N
ATOM 2122 C ASN A 263 -14.412 13.394 31.330 1.00 10.99 C
ANISOU 2122 C ASN A 263 1627 1291 1254 -97 269 -167 C
ATOM 2123 O ASN A 263 -13.788 12.683 30.565 1.00 11.80 O
ANISOU 2123 O ASN A 263 1934 1136 1411 -236 521 -234 O
ATOM 2124 N MET A 264 -15.231 12.927 32.280 1.00 10.89 N
ANISOU 2124 N MET A 264 1627 1241 1268 -218 288 -222 N
ATOM 2125 CA MET A 264 -15.519 11.518 32.425 1.00 11.75 C
ANISOU 2125 CA MET A 264 1725 1295 1442 -174 274 -262 C
ATOM 2126 CB MET A 264 -15.442 11.044 33.875 1.00 12.17 C
ANISOU 2126 CB MET A 264 1829 1397 1398 -228 120 -304 C
ATOM 2127 CG MET A 264 -15.706 9.561 33.990 1.00 13.25 C
ANISOU 2127 CG MET A 264 2237 1413 1383 -207 256 -252 C
ATOM 2128 SD MET A 264 -15.277 8.851 35.586 1.00 15.03 S
ANISOU 2128 SD MET A 264 2602 1604 1504 -19 201 -7 S
ATOM 2129 CE MET A 264 -16.510 9.633 36.602 1.00 18.78 C
ANISOU 2129 CE MET A 264 3156 2211 1766 133 530 -50 C
ATOM 2130 C MET A 264 -16.921 11.281 31.860 1.00 10.67 C
ANISOU 2130 C MET A 264 1706 1082 1266 -176 266 -233 C
ATOM 2131 O MET A 264 -17.873 11.967 32.252 1.00 12.69 O
ANISOU 2131 O MET A 264 1632 1427 1762 2 75 -437 O
ATOM 2132 N LEU A 265 -17.022 10.351 30.911 1.00 10.93 N
ANISOU 2132 N LEU A 265 1739 1089 1322 -71 146 -277 N
ATOM 2133 CA LEU A 265 -18.259 10.071 30.178 1.00 11.31 C
ANISOU 2133 CA LEU A 265 1763 1148 1386 -95 84 -200 C
ATOM 2134 CB LEU A 265 -18.005 10.157 28.677 1.00 12.93 C
ANISOU 2134 CB LEU A 265 2014 1514 1383 -192 -91 -117 C
ATOM 2135 CG LEU A 265 -18.044 11.561 28.068 1.00 14.73 C
ANISOU 2135 CG LEU A 265 2633 1610 1351 -256 -21 -52 C
ATOM 2136 CD1 LEU A 265 -17.052 12.515 28.694 1.00 16.40 C
ANISOU 2136 CD1 LEU A 265 3080 1550 1599 -252 -130 -144 C
ATOM 2137 CD2 LEU A 265 -17.829 11.476 26.570 1.00 16.48 C
ANISOU 2137 CD2 LEU A 265 2988 1963 1309 -308 -6 206 C
ATOM 2138 C LEU A 265 -18.725 8.668 30.553 1.00 10.51 C
ANISOU 2138 C LEU A 265 1725 1221 1047 -196 122 -238 C
ATOM 2139 O LEU A 265 -17.963 7.701 30.415 1.00 12.33 O
ANISOU 2139 O LEU A 265 2072 1128 1483 -175 337 -276 O
ATOM 2140 N VAL A 266 -19.964 8.548 31.006 1.00 11.39 N
ANISOU 2140 N VAL A 266 1801 1101 1423 -145 316 -244 N
ATOM 2141 CA VAL A 266 -20.484 7.237 31.365 1.00 11.42 C
ANISOU 2141 CA VAL A 266 1850 1093 1394 -131 154 -134 C
ATOM 2142 CB VAL A 266 -20.017 6.831 32.781 1.00 12.44 C
ANISOU 2142 CB VAL A 266 1858 1360 1508 -146 70 -88 C
ATOM 2143 CG1 VAL A 266 -20.626 7.700 33.870 1.00 13.32 C
ANISOU 2143 CG1 VAL A 266 2150 1491 1419 -60 208 73 C
ATOM 2144 CG2 VAL A 266 -20.269 5.354 33.057 1.00 13.35 C
ANISOU 2144 CG2 VAL A 266 1925 1381 1763 -103 33 -54 C
ATOM 2145 C VAL A 266 -22.012 7.261 31.252 1.00 10.72 C
ANISOU 2145 C VAL A 266 1770 999 1303 -94 221 -190 C
ATOM 2146 O VAL A 266 -22.676 8.254 31.598 1.00 11.04 O
ANISOU 2146 O VAL A 266 1779 1024 1390 -72 155 -325 O
ATOM 2147 N GLN A 267 -22.567 6.128 30.794 1.00 11.49 N
ANISOU 2147 N GLN A 267 1781 1037 1545 -89 23 -165 N
ATOM 2148 CA GLN A 267 -24.014 5.956 30.732 1.00 12.00 C
ANISOU 2148 CA GLN A 267 1844 1309 1404 -189 -7 -142 C
ATOM 2149 CB GLN A 267 -24.361 4.703 29.938 1.00 12.83 C
ANISOU 2149 CB GLN A 267 2065 1318 1489 -180 56 -180 C
ATOM 2150 CG GLN A 267 -24.114 4.848 28.438 1.00 12.69 C
ANISOU 2150 CG GLN A 267 1959 1402 1460 -126 25 -104 C
ATOM 2151 CD GLN A 267 -23.956 3.509 27.758 1.00 11.98 C
ANISOU 2151 CD GLN A 267 1886 1460 1206 -61 52 -50 C
ATOM 2152 OE1 GLN A 267 -23.020 2.764 28.056 1.00 14.03 O
ANISOU 2152 OE1 GLN A 267 1888 1722 1718 -69 -300 13 O
ATOM 2153 NE2 GLN A 267 -24.895 3.173 26.878 1.00 13.46 N
ANISOU 2153 NE2 GLN A 267 2095 1801 1217 -379 59 -43 N
ATOM 2154 C GLN A 267 -24.576 5.883 32.153 1.00 11.85 C
ANISOU 2154 C GLN A 267 1645 1347 1511 -121 27 -140 C
ATOM 2155 O GLN A 267 -23.920 5.403 33.095 1.00 11.67 O
ANISOU 2155 O GLN A 267 1849 1190 1392 -38 -31 -145 O
ATOM 2156 N ASN A 268 -25.809 6.363 32.294 1.00 11.62 N
ANISOU 2156 N ASN A 268 1646 1313 1455 -83 115 -6 N
ATOM 2157 CA ASN A 268 -26.507 6.306 33.563 1.00 12.15 C
ANISOU 2157 CA ASN A 268 1676 1469 1469 102 164 -52 C
ATOM 2158 CB ASN A 268 -26.201 7.536 34.422 1.00 13.77 C
ANISOU 2158 CB ASN A 268 1886 1556 1787 124 -22 -149 C
ATOM 2159 CG ASN A 268 -26.957 7.566 35.731 1.00 15.12 C
ANISOU 2159 CG ASN A 268 2169 1880 1695 436 -77 -642 C
ATOM 2160 OD1 ASN A 268 -27.742 8.483 35.922 1.00 24.73 O
ANISOU 2160 OD1 ASN A 268 3905 3477 2013 2045 95 -281 O
ATOM 2161 ND2 ASN A 268 -26.674 6.668 36.653 1.00 13.86 N
ANISOU 2161 ND2 ASN A 268 1945 1481 1836 -311 185 -394 N
ATOM 2162 C ASN A 268 -27.989 6.178 33.224 1.00 11.77 C
ANISOU 2162 C ASN A 268 1655 1265 1552 0 169 -35 C
ATOM 2163 O ASN A 268 -28.484 6.932 32.396 1.00 14.74 O
ANISOU 2163 O ASN A 268 1950 1668 1981 110 78 224 O
ATOM 2164 N TRP A 269 -28.699 5.241 33.860 1.00 11.90 N
ANISOU 2164 N TRP A 269 1755 1244 1520 -7 252 -65 N
ATOM 2165 CA TRP A 269 -30.060 4.955 33.466 1.00 12.08 C
ANISOU 2165 CA TRP A 269 1774 1253 1559 85 179 -194 C
ATOM 2166 CB TRP A 269 -30.093 4.180 32.140 1.00 12.59 C
ANISOU 2166 CB TRP A 269 1776 1579 1426 -48 134 -123 C
ATOM 2167 CG TRP A 269 -29.640 2.759 32.235 1.00 12.45 C
ANISOU 2167 CG TRP A 269 1747 1546 1437 -34 174 -213 C
ATOM 2168 CD1 TRP A 269 -30.434 1.644 32.276 1.00 13.01 C
ANISOU 2168 CD1 TRP A 269 1800 1526 1615 -31 227 -200 C
ATOM 2169 NE1 TRP A 269 -29.661 0.513 32.342 1.00 12.92 N
ANISOU 2169 NE1 TRP A 269 1830 1381 1696 -125 365 -112 N
ATOM 2170 CE2 TRP A 269 -28.336 0.878 32.367 1.00 12.84 C
ANISOU 2170 CE2 TRP A 269 1833 1500 1544 -31 314 -242 C
ATOM 2171 CD2 TRP A 269 -28.283 2.284 32.284 1.00 12.52 C
ANISOU 2171 CD2 TRP A 269 1777 1527 1452 -48 196 -134 C
ATOM 2172 CE3 TRP A 269 -27.030 2.898 32.255 1.00 12.08 C
ANISOU 2172 CE3 TRP A 269 1850 1288 1450 -63 265 -86 C
ATOM 2173 CZ3 TRP A 269 -25.893 2.126 32.300 1.00 13.16 C
ANISOU 2173 CZ3 TRP A 269 1948 1515 1537 -21 186 -174 C
ATOM 2174 CH2 TRP A 269 -25.969 0.742 32.402 1.00 13.43 C
ANISOU 2174 CH2 TRP A 269 1979 1477 1644 9 256 -97 C
ATOM 2175 CZ2 TRP A 269 -27.179 0.095 32.438 1.00 12.67 C
ANISOU 2175 CZ2 TRP A 269 1863 1393 1558 -46 251 -223 C
ATOM 2176 C TRP A 269 -30.802 4.210 34.564 1.00 12.59 C
ANISOU 2176 C TRP A 269 1719 1592 1470 -136 170 -396 C
ATOM 2177 O TRP A 269 -30.190 3.599 35.441 1.00 13.25 O
ANISOU 2177 O TRP A 269 1845 1781 1408 -40 242 -252 O
ATOM 2178 N VAL A 270 -32.134 4.252 34.452 1.00 14.48 N
ANISOU 2178 N VAL A 270 1697 2037 1765 -102 298 -200 N
ATOM 2179 CA VAL A 270 -33.038 3.512 35.332 1.00 15.21 C
ANISOU 2179 CA VAL A 270 1756 2110 1912 -288 433 -353 C
ATOM 2180 CB VAL A 270 -34.412 4.194 35.405 1.00 17.39 C
ANISOU 2180 CB VAL A 270 1788 2301 2515 -301 450 -678 C
ATOM 2181 CG1 VAL A 270 -35.367 3.421 36.311 1.00 19.98 C
ANISOU 2181 CG1 VAL A 270 2209 2498 2881 -440 835 -824 C
ATOM 2182 CG2 VAL A 270 -34.281 5.635 35.850 1.00 18.32 C
ANISOU 2182 CG2 VAL A 270 1923 2221 2817 -112 429 -595 C
ATOM 2183 C VAL A 270 -33.179 2.077 34.827 1.00 15.74 C
ANISOU 2183 C VAL A 270 1973 2171 1833 -325 348 -321 C
ATOM 2184 O VAL A 270 -33.453 1.856 33.653 1.00 17.21 O
ANISOU 2184 O VAL A 270 2022 2686 1831 -314 334 -365 O
ATOM 2185 N ALA A 271 -33.064 1.116 35.755 1.00 16.52 N
ANISOU 2185 N ALA A 271 2191 2099 1986 -370 314 -221 N
ATOM 2186 CA ALA A 271 -33.218 -0.293 35.398 1.00 18.08 C
ANISOU 2186 CA ALA A 271 2251 2234 2384 -193 149 -390 C
ATOM 2187 CB ALA A 271 -33.099 -1.160 36.618 1.00 18.39 C
ANISOU 2187 CB ALA A 271 2491 2153 2341 -292 52 -297 C
ATOM 2188 C ALA A 271 -34.573 -0.491 34.728 1.00 18.32 C
ANISOU 2188 C ALA A 271 2287 2507 2164 -231 158 -521 C
ATOM 2189 O ALA A 271 -35.598 0.017 35.187 1.00 19.70 O
ANISOU 2189 O ALA A 271 2005 2342 3135 -316 172 -586 O
ATOM 2190 N PRO A 272 -34.628 -1.245 33.614 1.00 19.22 N
ANISOU 2190 N PRO A 272 2326 2345 2630 -114 255 -844 N
ATOM 2191 CA PRO A 272 -35.899 -1.535 32.959 1.00 20.60 C
ANISOU 2191 CA PRO A 272 2397 2566 2864 -232 86 -762 C
ATOM 2192 CB PRO A 272 -35.515 -2.324 31.700 1.00 23.98 C
ANISOU 2192 CB PRO A 272 2769 3281 3060 -71 -16 -1024 C
ATOM 2193 CG PRO A 272 -34.163 -2.884 32.023 1.00 27.53 C
ANISOU 2193 CG PRO A 272 2927 3621 3912 128 -107 -1367 C
ATOM 2194 CD PRO A 272 -33.491 -1.895 32.952 1.00 22.33 C
ANISOU 2194 CD PRO A 272 2175 3047 3262 298 -17 -934 C
ATOM 2195 C PRO A 272 -36.787 -2.378 33.880 1.00 20.41 C
ANISOU 2195 C PRO A 272 2386 2542 2826 -61 275 -740 C
ATOM 2196 O PRO A 272 -36.285 -3.252 34.635 1.00 19.26 O
ANISOU 2196 O PRO A 272 2332 2206 2780 -357 58 -727 O
ATOM 2197 N LEU A 273 -38.097 -2.135 33.803 1.00 21.81 N
ANISOU 2197 N LEU A 273 2607 2388 3289 202 239 -798 N
ATOM 2198 CA LEU A 273 -39.068 -2.897 34.584 1.00 24.34 C
ANISOU 2198 CA LEU A 273 3012 2747 3487 246 495 -424 C
ATOM 2199 CB LEU A 273 -40.475 -2.515 34.117 1.00 28.45 C
ANISOU 2199 CB LEU A 273 3163 3778 3867 850 676 -112 C
ATOM 2200 CG LEU A 273 -40.922 -1.091 34.439 1.00 33.53 C
ANISOU 2200 CG LEU A 273 4248 4133 4359 1140 444 -283 C
ATOM 2201 CD1 LEU A 273 -42.298 -0.824 33.839 1.00 35.96 C
ANISOU 2201 CD1 LEU A 273 3611 5210 4838 1644 871 -385 C
ATOM 2202 CD2 LEU A 273 -40.927 -0.821 35.948 1.00 34.29 C
ANISOU 2202 CD2 LEU A 273 4640 4184 4202 1009 413 -475 C
ATOM 2203 C LEU A 273 -38.861 -4.406 34.375 1.00 22.42 C
ANISOU 2203 C LEU A 273 2673 2630 3214 51 276 -506 C
ATOM 2204 O LEU A 273 -39.027 -5.188 35.294 1.00 22.70 O
ANISOU 2204 O LEU A 273 2560 3077 2985 111 243 -361 O
ATOM 2205 N GLU A 274 -38.507 -4.805 33.150 1.00 21.16 N
ANISOU 2205 N GLU A 274 2171 2717 3153 -230 130 -604 N
ATOM 2206 CA GLU A 274 -38.590 -6.208 32.752 1.00 22.50 C
ANISOU 2206 CA GLU A 274 2900 2686 2960 -132 149 -518 C
ATOM 2207 CB GLU A 274 -38.539 -6.333 31.232 1.00 22.99 C
ANISOU 2207 CB GLU A 274 2571 3166 2996 -280 -5 -687 C
ATOM 2208 CG GLU A 274 -39.688 -5.628 30.532 1.00 23.46 C
ANISOU 2208 CG GLU A 274 3085 2997 2830 -168 -82 -533 C
ATOM 2209 CD GLU A 274 -39.422 -4.221 30.019 1.00 23.72 C
ANISOU 2209 CD GLU A 274 3284 3071 2657 -65 61 -450 C
ATOM 2210 OE1 GLU A 274 -38.627 -3.523 30.626 1.00 23.50 O
ANISOU 2210 OE1 GLU A 274 2621 3422 2887 223 -401 -316 O
ATOM 2211 OE2 GLU A 274 -40.026 -3.826 29.009 1.00 25.37 O
ANISOU 2211 OE2 GLU A 274 4065 3052 2522 250 -46 -562 O
ATOM 2212 C GLU A 274 -37.489 -7.079 33.373 1.00 22.67 C
ANISOU 2212 C GLU A 274 2631 2743 3237 -365 -302 -658 C
ATOM 2213 O GLU A 274 -37.590 -8.308 33.295 1.00 26.44 O
ANISOU 2213 O GLU A 274 3524 2767 3753 -601 -225 -858 O
ATOM 2214 N ILE A 275 -36.446 -6.495 33.981 1.00 20.81 N
ANISOU 2214 N ILE A 275 2476 2777 2652 -74 -298 -686 N
ATOM 2215 CA ILE A 275 -35.416 -7.333 34.630 1.00 22.80 C
ANISOU 2215 CA ILE A 275 2786 2831 3044 143 -171 -484 C
ATOM 2216 CB ILE A 275 -33.999 -6.743 34.490 1.00 23.31 C
ANISOU 2216 CB ILE A 275 2741 3452 2663 211 -79 -217 C
ATOM 2217 CG1 ILE A 275 -33.794 -5.429 35.241 1.00 22.08 C
ANISOU 2217 CG1 ILE A 275 2556 3228 2605 -76 -19 205 C
ATOM 2218 CG2 ILE A 275 -33.628 -6.614 33.025 1.00 25.87 C
ANISOU 2218 CG2 ILE A 275 3006 3967 2856 133 123 32 C
ATOM 2219 CD1 ILE A 275 -32.345 -5.027 35.374 1.00 24.28 C
ANISOU 2219 CD1 ILE A 275 2468 3604 3153 156 -186 316 C
ATOM 2220 C ILE A 275 -35.774 -7.601 36.093 1.00 24.01 C
ANISOU 2220 C ILE A 275 2729 3152 3239 42 -177 -295 C
ATOM 2221 O ILE A 275 -35.043 -8.311 36.793 1.00 26.07 O
ANISOU 2221 O ILE A 275 2738 3348 3817 71 240 605 O
ATOM 2222 N GLY A 276 -36.883 -7.024 36.569 1.00 24.89 N
ANISOU 2222 N GLY A 276 2737 3422 3296 -89 -113 -378 N
ATOM 2223 CA GLY A 276 -37.353 -7.273 37.933 1.00 25.50 C
ANISOU 2223 CA GLY A 276 2832 3507 3350 -688 -44 -324 C
ATOM 2224 C GLY A 276 -36.308 -6.844 38.947 1.00 24.42 C
ANISOU 2224 C GLY A 276 2632 3706 2940 -489 -71 327 C
ATOM 2225 O GLY A 276 -35.552 -5.893 38.723 1.00 26.27 O
ANISOU 2225 O GLY A 276 2746 3778 3457 -543 245 262 O
ATOM 2226 N ASP A 277 -36.243 -7.581 40.049 1.00 24.81 N
ANISOU 2226 N ASP A 277 2840 3207 3377 -499 -88 591 N
ATOM 2227 CA ASP A 277 -35.425 -7.216 41.170 1.00 23.12 C
ANISOU 2227 CA ASP A 277 1623 3680 3481 -243 26 546 C
ATOM 2228 CB ASP A 277 -35.854 -7.965 42.431 1.00 28.39 C
ANISOU 2228 CB ASP A 277 2235 4944 3606 -714 283 946 C
ATOM 2229 CG ASP A 277 -37.234 -7.586 42.953 1.00 33.85 C
ANISOU 2229 CG ASP A 277 2601 5800 4456 -348 747 1477 C
ATOM 2230 OD1 ASP A 277 -37.743 -6.521 42.578 1.00 37.53 O
ANISOU 2230 OD1 ASP A 277 2901 7061 4297 601 754 1323 O
ATOM 2231 OD2 ASP A 277 -37.771 -8.345 43.761 1.00 46.78 O
ANISOU 2231 OD2 ASP A 277 4090 7873 5808 -1862 935 2309 O
ATOM 2232 C ASP A 277 -33.955 -7.505 40.854 1.00 20.79 C
ANISOU 2232 C ASP A 277 1896 2716 3284 151 175 285 C
ATOM 2233 O ASP A 277 -33.608 -8.538 40.308 1.00 27.72 O
ANISOU 2233 O ASP A 277 3232 2211 5089 11 -83 -47 O
ATOM 2234 N ILE A 278 -33.107 -6.546 41.189 1.00 18.19 N
ANISOU 2234 N ILE A 278 2104 2402 2403 201 106 350 N
ATOM 2235 CA ILE A 278 -31.681 -6.713 41.072 1.00 18.12 C
ANISOU 2235 CA ILE A 278 2136 2290 2458 76 254 255 C
ATOM 2236 CB ILE A 278 -31.010 -5.332 40.972 1.00 20.89 C
ANISOU 2236 CB ILE A 278 2560 2335 3042 -4 446 460 C
ATOM 2237 CG1 ILE A 278 -31.477 -4.612 39.702 1.00 23.46 C
ANISOU 2237 CG1 ILE A 278 2726 2753 3434 -30 573 748 C
ATOM 2238 CG2 ILE A 278 -29.494 -5.438 41.071 1.00 21.91 C
ANISOU 2238 CG2 ILE A 278 2707 2811 2805 -262 457 462 C
ATOM 2239 CD1 ILE A 278 -30.911 -3.229 39.579 1.00 25.73 C
ANISOU 2239 CD1 ILE A 278 3613 2255 3906 255 586 246 C
ATOM 2240 C ILE A 278 -31.209 -7.511 42.282 1.00 17.05 C
ANISOU 2240 C ILE A 278 2116 2169 2191 333 499 62 C
ATOM 2241 O ILE A 278 -31.663 -7.273 43.403 1.00 17.52 O
ANISOU 2241 O ILE A 278 2011 2461 2181 168 533 -81 O
ATOM 2242 N PRO A 279 -30.278 -8.470 42.102 1.00 16.28 N
ANISOU 2242 N PRO A 279 2217 2034 1931 368 262 -108 N
ATOM 2243 CA PRO A 279 -29.826 -9.287 43.218 1.00 16.37 C
ANISOU 2243 CA PRO A 279 2305 1913 2001 379 442 -37 C
ATOM 2244 CB PRO A 279 -28.772 -10.217 42.602 1.00 19.78 C
ANISOU 2244 CB PRO A 279 3109 2013 2392 662 428 -489 C
ATOM 2245 CG PRO A 279 -29.004 -10.164 41.129 1.00 22.06 C
ANISOU 2245 CG PRO A 279 3232 2691 2459 764 257 -310 C
ATOM 2246 CD PRO A 279 -29.668 -8.861 40.827 1.00 19.87 C
ANISOU 2246 CD PRO A 279 2767 2599 2182 641 461 -200 C
ATOM 2247 C PRO A 279 -29.204 -8.475 44.361 1.00 15.56 C
ANISOU 2247 C PRO A 279 2086 1703 2124 279 495 -11 C
ATOM 2248 O PRO A 279 -28.662 -7.391 44.160 1.00 16.83 O
ANISOU 2248 O PRO A 279 2187 1795 2412 245 569 182 O
ATOM 2249 N LYS A 280 -29.285 -9.041 45.561 1.00 14.97 N
ANISOU 2249 N LYS A 280 2108 1453 2124 185 615 28 N
ATOM 2250 CA LYS A 280 -28.762 -8.420 46.763 1.00 16.32 C
ANISOU 2250 CA LYS A 280 2340 1642 2217 55 772 -76 C
ATOM 2251 CB LYS A 280 -29.127 -9.270 47.985 1.00 19.39 C
ANISOU 2251 CB LYS A 280 2858 2260 2248 -264 848 100 C
ATOM 2252 CG LYS A 280 -30.622 -9.364 48.242 1.00 25.66 C
ANISOU 2252 CG LYS A 280 3073 3183 3492 109 1029 60 C
ATOM 2253 CD LYS A 280 -30.994 -10.065 49.533 1.00 30.21 C
ANISOU 2253 CD LYS A 280 3935 3918 3623 -356 1162 258 C
ATOM 2254 CE LYS A 280 -32.495 -10.137 49.738 1.00 37.73 C
ANISOU 2254 CE LYS A 280 3994 5022 5317 116 1064 -71 C
ATOM 2255 NZ LYS A 280 -33.101 -8.790 49.764 1.00 41.54 N
ANISOU 2255 NZ LYS A 280 3925 5627 6232 97 1137 -229 N
ATOM 2256 C LYS A 280 -27.247 -8.214 46.673 1.00 16.59 C
ANISOU 2256 C LYS A 280 2328 1555 2418 191 805 21 C
ATOM 2257 O LYS A 280 -26.757 -7.229 47.185 1.00 20.07 O
ANISOU 2257 O LYS A 280 2481 1744 3401 377 718 -314 O
ATOM 2258 N THR A 281 -26.507 -9.157 46.082 1.00 13.97 N
ANISOU 2258 N THR A 281 2023 1262 2020 96 465 37 N
ATOM 2259 CA THR A 281 -25.053 -9.049 45.988 1.00 14.13 C
ANISOU 2259 CA THR A 281 2144 1421 1804 125 527 -13 C
ATOM 2260 CB THR A 281 -24.328 -9.979 46.961 1.00 16.26 C
ANISOU 2260 CB THR A 281 2433 1803 1942 336 467 68 C
ATOM 2261 OG1 THR A 281 -24.815 -9.740 48.283 1.00 18.18 O
ANISOU 2261 OG1 THR A 281 2559 2304 2042 229 600 58 O
ATOM 2262 CG2 THR A 281 -22.833 -9.779 46.894 1.00 18.62 C
ANISOU 2262 CG2 THR A 281 2562 2153 2358 254 241 166 C
ATOM 2263 C THR A 281 -24.608 -9.351 44.560 1.00 13.30 C
ANISOU 2263 C THR A 281 2062 1327 1662 34 406 59 C
ATOM 2264 O THR A 281 -24.835 -10.476 44.068 1.00 17.04 O
ANISOU 2264 O THR A 281 2640 1659 2173 -220 754 -353 O
ATOM 2265 N ILE A 282 -24.007 -8.343 43.907 1.00 12.88 N
ANISOU 2265 N ILE A 282 2017 1253 1623 158 592 -71 N
ATOM 2266 CA ILE A 282 -23.503 -8.476 42.542 1.00 13.30 C
ANISOU 2266 CA ILE A 282 2151 1355 1546 214 453 -116 C
ATOM 2267 CB ILE A 282 -23.898 -7.250 41.687 1.00 13.84 C
ANISOU 2267 CB ILE A 282 2210 1610 1438 332 271 -45 C
ATOM 2268 CG1 ILE A 282 -25.413 -6.997 41.726 1.00 14.81 C
ANISOU 2268 CG1 ILE A 282 2255 1818 1554 492 138 -102 C
ATOM 2269 CG2 ILE A 282 -23.384 -7.389 40.262 1.00 14.33 C
ANISOU 2269 CG2 ILE A 282 2497 1454 1492 238 373 -179 C
ATOM 2270 CD1 ILE A 282 -25.787 -5.625 41.255 1.00 16.14 C
ANISOU 2270 CD1 ILE A 282 2519 2020 1590 845 126 -31 C
ATOM 2271 C ILE A 282 -21.982 -8.611 42.614 1.00 12.56 C
ANISOU 2271 C ILE A 282 2106 1414 1250 254 269 -179 C
ATOM 2272 O ILE A 282 -21.336 -7.913 43.371 1.00 13.05 O
ANISOU 2272 O ILE A 282 1935 1416 1607 48 430 -249 O
ATOM 2273 N ILE A 283 -21.446 -9.507 41.780 1.00 12.89 N
ANISOU 2273 N ILE A 283 1912 1515 1468 144 410 -280 N
ATOM 2274 CA ILE A 283 -20.029 -9.846 41.702 1.00 12.77 C
ANISOU 2274 CA ILE A 283 1887 1558 1407 70 344 -207 C
ATOM 2275 CB ILE A 283 -19.853 -11.361 41.798 1.00 14.08 C
ANISOU 2275 CB ILE A 283 2177 1536 1634 -13 426 -108 C
ATOM 2276 CG1 ILE A 283 -20.481 -11.900 43.084 1.00 14.98 C
ANISOU 2276 CG1 ILE A 283 2094 1832 1765 -256 388 -52 C
ATOM 2277 CG2 ILE A 283 -18.385 -11.773 41.635 1.00 15.48 C
ANISOU 2277 CG2 ILE A 283 2299 1572 2010 29 592 39 C
ATOM 2278 CD1 ILE A 283 -20.459 -13.406 43.170 1.00 16.45 C
ANISOU 2278 CD1 ILE A 283 2239 1843 2165 -88 374 126 C
ATOM 2279 C ILE A 283 -19.424 -9.298 40.413 1.00 12.28 C
ANISOU 2279 C ILE A 283 1956 1410 1297 144 203 -185 C
ATOM 2280 O ILE A 283 -20.011 -9.455 39.348 1.00 13.28 O
ANISOU 2280 O ILE A 283 1953 1722 1370 -253 91 -288 O
ATOM 2281 N TYR A 284 -18.253 -8.658 40.536 1.00 11.42 N
ANISOU 2281 N TYR A 284 1730 1464 1145 183 328 -170 N
ATOM 2282 CA TYR A 284 -17.516 -8.127 39.392 1.00 11.75 C
ANISOU 2282 CA TYR A 284 1827 1305 1331 142 413 -139 C
ATOM 2283 CB TYR A 284 -17.365 -6.607 39.473 1.00 12.33 C
ANISOU 2283 CB TYR A 284 1840 1290 1553 129 313 -23 C
ATOM 2284 CG TYR A 284 -18.671 -5.860 39.539 1.00 12.16 C
ANISOU 2284 CG TYR A 284 1861 1212 1544 190 224 -114 C
ATOM 2285 CD1 TYR A 284 -19.364 -5.765 40.734 1.00 12.78 C
ANISOU 2285 CD1 TYR A 284 2150 1253 1450 202 186 -247 C
ATOM 2286 CE1 TYR A 284 -20.592 -5.142 40.812 1.00 11.83 C
ANISOU 2286 CE1 TYR A 284 1982 1243 1268 200 227 31 C
ATOM 2287 CZ TYR A 284 -21.153 -4.568 39.682 1.00 11.98 C
ANISOU 2287 CZ TYR A 284 1982 1292 1274 186 303 48 C
ATOM 2288 OH TYR A 284 -22.369 -3.946 39.783 1.00 12.48 O
ANISOU 2288 OH TYR A 284 1963 1275 1504 153 373 -181 O
ATOM 2289 CE2 TYR A 284 -20.463 -4.615 38.481 1.00 10.88 C
ANISOU 2289 CE2 TYR A 284 1872 987 1271 146 299 -104 C
ATOM 2290 CD2 TYR A 284 -19.233 -5.270 38.412 1.00 12.15 C
ANISOU 2290 CD2 TYR A 284 1980 1177 1459 209 336 -88 C
ATOM 2291 C TYR A 284 -16.119 -8.736 39.364 1.00 12.39 C
ANISOU 2291 C TYR A 284 1906 1443 1359 130 343 -140 C
ATOM 2292 O TYR A 284 -15.424 -8.812 40.387 1.00 13.18 O
ANISOU 2292 O TYR A 284 1952 1712 1341 266 295 -148 O
ATOM 2293 N AASN A 285 -15.706 -9.146 38.164 0.50 12.38 N
ANISOU 2293 N AASN A 285 1816 1590 1296 124 244 -227 N
ATOM 2294 N BASN A 285 -15.709 -9.145 38.163 0.50 12.25 N
ANISOU 2294 N BASN A 285 1730 1621 1302 167 243 -200 N
ATOM 2295 CA AASN A 285 -14.350 -9.593 37.911 0.50 12.51 C
ANISOU 2295 CA AASN A 285 1849 1496 1408 123 282 -301 C
ATOM 2296 CA BASN A 285 -14.356 -9.586 37.909 0.50 12.61 C
ANISOU 2296 CA BASN A 285 1737 1574 1480 172 253 -225 C
ATOM 2297 CB AASN A 285 -14.305 -10.430 36.634 0.50 14.32 C
ANISOU 2297 CB AASN A 285 2085 1883 1472 139 290 -463 C
ATOM 2298 CB BASN A 285 -14.301 -10.397 36.617 0.50 14.10 C
ANISOU 2298 CB BASN A 285 1868 1949 1540 263 230 -359 C
ATOM 2299 CG AASN A 285 -13.043 -11.251 36.526 0.50 16.65 C
ANISOU 2299 CG AASN A 285 2328 2196 1799 353 291 -643 C
ATOM 2300 CG BASN A 285 -12.935 -11.001 36.417 0.50 16.60 C
ANISOU 2300 CG BASN A 285 1901 2406 1999 401 110 -486 C
ATOM 2301 OD1AASN A 285 -12.017 -10.878 37.092 0.50 20.47 O
ANISOU 2301 OD1AASN A 285 2269 2800 2707 301 305 -791 O
ATOM 2302 OD1BASN A 285 -12.411 -11.613 37.355 0.50 17.66 O
ANISOU 2302 OD1BASN A 285 1866 2222 2620 652 52 -292 O
ATOM 2303 ND2AASN A 285 -13.105 -12.345 35.781 0.50 18.38 N
ANISOU 2303 ND2AASN A 285 2702 2196 2085 69 115 -719 N
ATOM 2304 ND2BASN A 285 -12.379 -10.832 35.220 0.50 19.93 N
ANISOU 2304 ND2BASN A 285 2388 2901 2282 345 398 -443 N
ATOM 2305 C AASN A 285 -13.445 -8.350 37.826 0.50 12.04 C
ANISOU 2305 C AASN A 285 1704 1463 1406 162 176 -194 C
ATOM 2306 C BASN A 285 -13.447 -8.347 37.827 0.50 12.10 C
ANISOU 2306 C BASN A 285 1651 1506 1440 203 170 -154 C
ATOM 2307 O AASN A 285 -13.625 -7.503 36.941 0.50 13.41 O
ANISOU 2307 O AASN A 285 1927 1749 1416 158 -18 -124 O
ATOM 2308 O BASN A 285 -13.624 -7.501 36.941 0.50 13.49 O
ANISOU 2308 O BASN A 285 1886 1796 1442 190 -22 -80 O
ATOM 2309 N THR A 286 -12.483 -8.247 38.748 1.00 12.64 N
ANISOU 2309 N THR A 286 1860 1345 1598 160 19 -135 N
ATOM 2310 CA THR A 286 -11.621 -7.057 38.883 1.00 11.95 C
ANISOU 2310 CA THR A 286 1607 1533 1398 94 158 -64 C
ATOM 2311 CB THR A 286 -12.157 -6.116 39.968 1.00 12.47 C
ANISOU 2311 CB THR A 286 1752 1601 1382 113 229 -44 C
ATOM 2312 OG1 THR A 286 -12.253 -6.809 41.212 1.00 12.84 O
ANISOU 2312 OG1 THR A 286 2153 1359 1365 114 233 -43 O
ATOM 2313 CG2 THR A 286 -13.506 -5.544 39.596 1.00 12.69 C
ANISOU 2313 CG2 THR A 286 1832 1352 1637 256 306 -36 C
ATOM 2314 C THR A 286 -10.184 -7.485 39.164 1.00 13.06 C
ANISOU 2314 C THR A 286 1591 1663 1708 81 216 -149 C
ATOM 2315 O THR A 286 -9.689 -7.348 40.270 1.00 13.52 O
ANISOU 2315 O THR A 286 1921 1544 1672 95 148 -58 O
ATOM 2316 N PRO A 287 -9.487 -8.033 38.154 1.00 14.42 N
ANISOU 2316 N PRO A 287 1609 2139 1730 193 126 -426 N
ATOM 2317 CA PRO A 287 -8.155 -8.598 38.351 1.00 16.00 C
ANISOU 2317 CA PRO A 287 1679 2345 2053 196 257 -394 C
ATOM 2318 CB PRO A 287 -7.658 -8.924 36.940 1.00 18.57 C
ANISOU 2318 CB PRO A 287 1877 2983 2195 118 268 -800 C
ATOM 2319 CG PRO A 287 -8.878 -8.890 36.046 1.00 18.94 C
ANISOU 2319 CG PRO A 287 2074 2962 2159 400 214 -511 C
ATOM 2320 CD PRO A 287 -9.955 -8.107 36.758 1.00 16.34 C
ANISOU 2320 CD PRO A 287 2019 2400 1789 119 108 -581 C
ATOM 2321 C PRO A 287 -7.173 -7.617 39.001 1.00 15.13 C
ANISOU 2321 C PRO A 287 1771 2200 1776 208 250 -271 C
ATOM 2322 O PRO A 287 -7.214 -6.429 38.755 1.00 15.13 O
ANISOU 2322 O PRO A 287 1857 2198 1691 215 489 6 O
ATOM 2323 N LEU A 288 -6.272 -8.156 39.811 1.00 14.14 N
ANISOU 2323 N LEU A 288 1978 1656 1737 136 249 35 N
ATOM 2324 CA LEU A 288 -5.283 -7.366 40.526 1.00 13.94 C
ANISOU 2324 CA LEU A 288 2141 1443 1710 158 322 -172 C
ATOM 2325 CB LEU A 288 -5.300 -7.752 41.998 1.00 16.38 C
ANISOU 2325 CB LEU A 288 2600 1842 1779 239 164 -31 C
ATOM 2326 CG LEU A 288 -4.336 -6.990 42.883 1.00 20.31 C
ANISOU 2326 CG LEU A 288 3332 2279 2103 -100 52 61 C
ATOM 2327 CD1 LEU A 288 -4.722 -5.528 42.923 1.00 23.38 C
ANISOU 2327 CD1 LEU A 288 3983 2422 2478 188 153 58 C
ATOM 2328 CD2 LEU A 288 -4.321 -7.589 44.280 1.00 22.56 C
ANISOU 2328 CD2 LEU A 288 4110 2280 2180 -89 -199 163 C
ATOM 2329 C LEU A 288 -3.915 -7.625 39.915 1.00 13.13 C
ANISOU 2329 C LEU A 288 2053 1422 1512 175 189 -245 C
ATOM 2330 O LEU A 288 -3.419 -8.744 39.950 1.00 15.16 O
ANISOU 2330 O LEU A 288 2182 1564 2013 349 191 -154 O
ATOM 2331 N ILE A 289 -3.332 -6.574 39.335 1.00 13.08 N
ANISOU 2331 N ILE A 289 2230 1425 1314 249 228 -130 N
ATOM 2332 CA ILE A 289 -2.020 -6.647 38.706 1.00 14.20 C
ANISOU 2332 CA ILE A 289 2138 1711 1545 223 182 -244 C
ATOM 2333 CB ILE A 289 -2.023 -6.001 37.313 1.00 17.10 C
ANISOU 2333 CB ILE A 289 2435 2257 1805 19 471 110 C
ATOM 2334 CG1 ILE A 289 -2.823 -6.814 36.290 1.00 19.06 C
ANISOU 2334 CG1 ILE A 289 2944 2631 1666 -53 389 -41 C
ATOM 2335 CG2 ILE A 289 -0.588 -5.790 36.840 1.00 20.02 C
ANISOU 2335 CG2 ILE A 289 2626 2948 2029 -57 653 431 C
ATOM 2336 CD1 ILE A 289 -4.325 -6.786 36.470 1.00 20.45 C
ANISOU 2336 CD1 ILE A 289 3040 2859 1871 -266 431 -78 C
ATOM 2337 C ILE A 289 -1.023 -5.964 39.639 1.00 14.84 C
ANISOU 2337 C ILE A 289 2022 1714 1902 70 143 -255 C
ATOM 2338 O ILE A 289 -1.263 -4.822 40.039 1.00 17.29 O
ANISOU 2338 O ILE A 289 2242 1639 2686 110 -47 -403 O
ATOM 2339 N SER A 290 0.070 -6.663 39.973 1.00 14.44 N
ANISOU 2339 N SER A 290 1850 1771 1866 23 121 -367 N
ATOM 2340 CA ASER A 290 1.077 -6.134 40.893 0.50 15.28 C
ANISOU 2340 CA ASER A 290 2074 1910 1820 8 38 -509 C
ATOM 2341 CA BSER A 290 1.075 -6.150 40.916 0.50 15.19 C
ANISOU 2341 CA BSER A 290 2047 1897 1827 8 60 -505 C
ATOM 2342 CB ASER A 290 0.958 -6.716 42.277 0.50 18.17 C
ANISOU 2342 CB ASER A 290 2517 2595 1790 -60 61 -472 C
ATOM 2343 CB BSER A 290 0.946 -6.806 42.283 0.50 17.37 C
ANISOU 2343 CB BSER A 290 2335 2479 1784 -39 153 -489 C
ATOM 2344 OG ASER A 290 1.694 -5.868 43.150 0.50 20.91 O
ANISOU 2344 OG ASER A 290 3107 2678 2158 -334 -120 -498 O
ATOM 2345 OG BSER A 290 -0.392 -6.883 42.746 0.50 18.65 O
ANISOU 2345 OG BSER A 290 2428 2534 2123 -159 302 -435 O
ATOM 2346 C SER A 290 2.483 -6.414 40.373 1.00 15.66 C
ANISOU 2346 C SER A 290 2053 2140 1756 -2 11 -410 C
ATOM 2347 O SER A 290 2.731 -7.455 39.806 1.00 17.51 O
ANISOU 2347 O SER A 290 2190 2218 2244 -7 36 -624 O
ATOM 2348 N LEU A 291 3.401 -5.491 40.667 1.00 17.05 N
ANISOU 2348 N LEU A 291 1843 2385 2248 -64 171 -377 N
ATOM 2349 CA LEU A 291 4.824 -5.735 40.486 1.00 17.28 C
ANISOU 2349 CA LEU A 291 1856 2473 2235 -13 -7 -396 C
ATOM 2350 CB LEU A 291 5.572 -4.405 40.402 1.00 19.16 C
ANISOU 2350 CB LEU A 291 2275 2453 2552 -139 -343 -328 C
ATOM 2351 CG LEU A 291 7.080 -4.538 40.227 1.00 21.55 C
ANISOU 2351 CG LEU A 291 2379 2691 3116 -126 -217 -454 C
ATOM 2352 CD1 LEU A 291 7.435 -5.174 38.892 1.00 18.51 C
ANISOU 2352 CD1 LEU A 291 1449 2652 2931 38 -44 -246 C
ATOM 2353 CD2 LEU A 291 7.721 -3.176 40.370 1.00 23.63 C
ANISOU 2353 CD2 LEU A 291 2330 3080 3566 -503 -347 -522 C
ATOM 2354 C LEU A 291 5.321 -6.568 41.672 1.00 18.56 C
ANISOU 2354 C LEU A 291 2339 2592 2117 225 -219 -512 C
ATOM 2355 O LEU A 291 5.280 -6.118 42.800 1.00 21.16 O
ANISOU 2355 O LEU A 291 3035 2766 2238 231 -331 -693 O
ATOM 2356 N GLU A 292 5.764 -7.793 41.401 1.00 16.43 N
ANISOU 2356 N GLU A 292 1906 2481 1853 242 -75 -309 N
ATOM 2357 CA GLU A 292 6.219 -8.706 42.461 1.00 18.78 C
ANISOU 2357 CA GLU A 292 2471 2935 1729 145 39 -98 C
ATOM 2358 CB GLU A 292 5.970 -10.157 42.079 1.00 20.78 C
ANISOU 2358 CB GLU A 292 2455 3144 2294 -108 -127 -59 C
ATOM 2359 CG GLU A 292 4.503 -10.532 42.070 1.00 21.80 C
ANISOU 2359 CG GLU A 292 2403 3415 2465 -106 -386 229 C
ATOM 2360 CD GLU A 292 3.785 -10.473 43.414 1.00 23.54 C
ANISOU 2360 CD GLU A 292 2886 3411 2645 -187 -28 169 C
ATOM 2361 OE1 GLU A 292 4.449 -10.555 44.470 1.00 25.12 O
ANISOU 2361 OE1 GLU A 292 3266 3326 2950 -249 -251 283 O
ATOM 2362 OE2 GLU A 292 2.539 -10.338 43.387 1.00 25.59 O
ANISOU 2362 OE2 GLU A 292 3019 4481 2223 -199 172 102 O
ATOM 2363 C GLU A 292 7.704 -8.521 42.767 1.00 18.79 C
ANISOU 2363 C GLU A 292 2740 2636 1763 44 -155 -322 C
ATOM 2364 O GLU A 292 8.148 -8.752 43.893 1.00 21.68 O
ANISOU 2364 O GLU A 292 3001 3345 1888 -1 -207 86 O
ATOM 2365 N GLY A 293 8.488 -8.153 41.755 1.00 16.44 N
ANISOU 2365 N GLY A 293 2205 2569 1470 106 -530 -53 N
ATOM 2366 CA GLY A 293 9.895 -7.959 41.961 1.00 17.85 C
ANISOU 2366 CA GLY A 293 2226 2952 1601 -27 -488 -220 C
ATOM 2367 C GLY A 293 10.535 -7.294 40.779 1.00 17.01 C
ANISOU 2367 C GLY A 293 2088 2700 1675 162 -392 -393 C
ATOM 2368 O GLY A 293 10.017 -7.366 39.653 1.00 16.92 O
ANISOU 2368 O GLY A 293 2039 2700 1690 129 -469 -230 O
ATOM 2369 N ASN A 294 11.659 -6.638 41.051 1.00 17.73 N
ANISOU 2369 N ASN A 294 2041 3004 1692 -56 -325 -289 N
ATOM 2370 CA ASN A 294 12.403 -5.986 40.010 1.00 18.61 C
ANISOU 2370 CA ASN A 294 2187 3271 1609 -133 -454 -116 C
ATOM 2371 CB ASN A 294 11.842 -4.594 39.716 1.00 20.75 C
ANISOU 2371 CB ASN A 294 2463 3131 2288 -153 -533 -146 C
ATOM 2372 CG ASN A 294 12.002 -3.640 40.876 1.00 25.11 C
ANISOU 2372 CG ASN A 294 3418 3437 2683 36 45 -528 C
ATOM 2373 OD1 ASN A 294 11.193 -3.620 41.806 1.00 31.46 O
ANISOU 2373 OD1 ASN A 294 4944 3936 3070 217 710 -420 O
ATOM 2374 ND2 ASN A 294 13.073 -2.880 40.849 1.00 28.24 N
ANISOU 2374 ND2 ASN A 294 4086 3241 3399 -318 -185 -450 N
ATOM 2375 C ASN A 294 13.878 -5.904 40.403 1.00 17.79 C
ANISOU 2375 C ASN A 294 2131 3096 1530 -63 -380 -379 C
ATOM 2376 O ASN A 294 14.239 -5.943 41.595 1.00 21.68 O
ANISOU 2376 O ASN A 294 2493 4201 1542 -110 -456 -414 O
ATOM 2377 N ILE A 295 14.734 -5.831 39.385 1.00 18.46 N
ANISOU 2377 N ILE A 295 2097 3210 1703 -190 -349 -355 N
ATOM 2378 CA ILE A 295 16.165 -5.676 39.600 1.00 18.94 C
ANISOU 2378 CA ILE A 295 2195 3276 1724 -383 -644 -571 C
ATOM 2379 CB ILE A 295 16.849 -7.000 39.989 1.00 21.40 C
ANISOU 2379 CB ILE A 295 2461 3472 2198 -338 -794 -338 C
ATOM 2380 CG1 ILE A 295 18.269 -6.758 40.507 1.00 24.31 C
ANISOU 2380 CG1 ILE A 295 2606 4010 2620 -384 -879 -430 C
ATOM 2381 CG2 ILE A 295 16.829 -8.003 38.844 1.00 21.36 C
ANISOU 2381 CG2 ILE A 295 2455 3262 2398 10 -615 -276 C
ATOM 2382 CD1 ILE A 295 18.838 -7.895 41.292 1.00 28.04 C
ANISOU 2382 CD1 ILE A 295 3217 4142 3295 -205 -1185 -485 C
ATOM 2383 C ILE A 295 16.749 -5.085 38.317 1.00 18.54 C
ANISOU 2383 C ILE A 295 2114 3130 1797 -138 -486 -424 C
ATOM 2384 O ILE A 295 16.223 -5.368 37.222 1.00 18.66 O
ANISOU 2384 O ILE A 295 2076 3047 1966 -99 -711 -418 O
ATOM 2385 N SER A 296 17.823 -4.307 38.447 1.00 19.97 N
ANISOU 2385 N SER A 296 2107 3419 2059 -299 -546 -321 N
ATOM 2386 CA ASER A 296 18.380 -3.605 37.295 0.50 21.12 C
ANISOU 2386 CA ASER A 296 2277 3641 2104 -370 -589 -251 C
ATOM 2387 CA BSER A 296 18.383 -3.596 37.297 0.50 20.52 C
ANISOU 2387 CA BSER A 296 2244 3487 2063 -302 -533 -301 C
ATOM 2388 CB ASER A 296 17.998 -2.139 37.333 0.50 22.41 C
ANISOU 2388 CB ASER A 296 2634 3565 2317 -512 -557 -383 C
ATOM 2389 CB BSER A 296 18.056 -2.118 37.346 0.50 20.18 C
ANISOU 2389 CB BSER A 296 2198 3395 2074 -393 -398 -478 C
ATOM 2390 OG ASER A 296 18.581 -1.493 38.445 0.50 24.77 O
ANISOU 2390 OG ASER A 296 2964 3974 2474 -844 -657 -416 O
ATOM 2391 OG BSER A 296 16.676 -1.868 37.380 0.50 19.96 O
ANISOU 2391 OG BSER A 296 2125 3325 2131 -469 -137 -399 O
ATOM 2392 C SER A 296 19.900 -3.782 37.229 1.00 20.26 C
ANISOU 2392 C SER A 296 2230 3724 1741 -417 -459 -273 C
ATOM 2393 O SER A 296 20.558 -4.142 38.222 1.00 23.38 O
ANISOU 2393 O SER A 296 2177 4537 2169 -458 -711 -3 O
ATOM 2394 N SER A 297 20.454 -3.513 36.049 1.00 19.02 N
ANISOU 2394 N SER A 297 2209 3219 1796 -531 -439 -366 N
ATOM 2395 CA SER A 297 21.886 -3.451 35.878 1.00 19.67 C
ANISOU 2395 CA SER A 297 2156 3269 2047 -643 -540 -393 C
ATOM 2396 CB SER A 297 22.474 -4.807 35.602 1.00 22.21 C
ANISOU 2396 CB SER A 297 2460 3590 2388 -400 -429 -233 C
ATOM 2397 OG SER A 297 22.082 -5.256 34.313 1.00 24.13 O
ANISOU 2397 OG SER A 297 3087 3710 2371 -542 -163 -531 O
ATOM 2398 C SER A 297 22.226 -2.499 34.733 1.00 20.77 C
ANISOU 2398 C SER A 297 2261 3360 2268 -754 -338 -507 C
ATOM 2399 O SER A 297 21.389 -2.212 33.874 1.00 21.39 O
ANISOU 2399 O SER A 297 2135 3433 2557 -602 -413 -318 O
ATOM 2400 N MET A 298 23.487 -2.061 34.735 1.00 22.52 N
ANISOU 2400 N MET A 298 2480 3501 2573 -1117 -395 -687 N
ATOM 2401 CA MET A 298 24.069 -1.378 33.595 1.00 22.27 C
ANISOU 2401 CA MET A 298 2243 3626 2590 -904 -641 -331 C
ATOM 2402 CB MET A 298 25.252 -0.501 34.026 1.00 25.29 C
ANISOU 2402 CB MET A 298 2543 4162 2902 -1430 -557 -336 C
ATOM 2403 CG MET A 298 25.939 0.239 32.877 1.00 28.01 C
ANISOU 2403 CG MET A 298 2887 4251 3504 -1471 -429 51 C
ATOM 2404 SD MET A 298 24.786 1.385 32.075 1.00 31.86 S
ANISOU 2404 SD MET A 298 3527 4606 3969 -1493 -846 199 S
ATOM 2405 CE MET A 298 25.904 2.454 31.173 1.00 36.33 C
ANISOU 2405 CE MET A 298 3309 5325 5166 -973 -49 579 C
ATOM 2406 C MET A 298 24.541 -2.452 32.626 1.00 22.77 C
ANISOU 2406 C MET A 298 2319 3840 2490 -637 -704 -407 C
ATOM 2407 O MET A 298 25.444 -3.218 32.943 1.00 26.31 O
ANISOU 2407 O MET A 298 2621 4644 2729 -52 -492 -495 O
ATOM 2408 N CYS A 299 23.905 -2.496 31.457 1.00 19.68 N
ANISOU 2408 N CYS A 299 2165 3106 2206 -404 -446 -289 N
ATOM 2409 CA CYS A 299 24.188 -3.494 30.429 1.00 21.58 C
ANISOU 2409 CA CYS A 299 2633 3280 2283 -569 -293 -451 C
ATOM 2410 CB CYS A 299 22.898 -4.021 29.813 1.00 21.10 C
ANISOU 2410 CB CYS A 299 2738 3219 2059 -644 -194 -262 C
ATOM 2411 SG CYS A 299 21.894 -4.992 30.958 1.00 20.86 S
ANISOU 2411 SG CYS A 299 2474 3058 2394 -480 -293 -14 S
ATOM 2412 C CYS A 299 25.074 -2.873 29.349 1.00 20.97 C
ANISOU 2412 C CYS A 299 2353 3254 2359 -658 -335 -654 C
ATOM 2413 O CYS A 299 24.650 -1.946 28.675 1.00 22.70 O
ANISOU 2413 O CYS A 299 2207 3663 2755 -457 -198 -367 O
ATOM 2414 N LEU A 300 26.304 -3.389 29.235 1.00 21.79 N
ANISOU 2414 N LEU A 300 2107 3520 2650 -583 -261 -289 N
ATOM 2415 CA LEU A 300 27.329 -2.892 28.320 1.00 22.12 C
ANISOU 2415 CA LEU A 300 2034 3501 2869 -607 -277 -316 C
ATOM 2416 CB LEU A 300 28.689 -2.792 29.028 1.00 24.86 C
ANISOU 2416 CB LEU A 300 2221 3936 3286 -726 -561 -411 C
ATOM 2417 CG LEU A 300 28.764 -1.886 30.255 1.00 29.97 C
ANISOU 2417 CG LEU A 300 2866 4300 4218 -1184 -482 -797 C
ATOM 2418 CD1 LEU A 300 30.176 -1.859 30.834 1.00 36.06 C
ANISOU 2418 CD1 LEU A 300 3172 5298 5229 -1196 -979 -458 C
ATOM 2419 CD2 LEU A 300 28.299 -0.479 29.912 1.00 32.81 C
ANISOU 2419 CD2 LEU A 300 3598 4221 4645 -1054 -237 -816 C
ATOM 2420 C LEU A 300 27.430 -3.875 27.158 1.00 21.41 C
ANISOU 2420 C LEU A 300 2042 3553 2539 -471 -353 -148 C
ATOM 2421 O LEU A 300 27.622 -5.080 27.379 1.00 22.07 O
ANISOU 2421 O LEU A 300 2373 3502 2511 -312 -181 -63 O
ATOM 2422 N ASN A 301 27.328 -3.358 25.933 1.00 20.62 N
ANISOU 2422 N ASN A 301 1778 3509 2545 -501 -217 -244 N
ATOM 2423 CA ASN A 301 27.567 -4.158 24.757 1.00 20.03 C
ANISOU 2423 CA ASN A 301 1744 3422 2443 -644 -201 -239 C
ATOM 2424 CB ASN A 301 26.532 -3.867 23.676 1.00 19.98 C
ANISOU 2424 CB ASN A 301 1947 3513 2131 -688 -70 -120 C
ATOM 2425 CG ASN A 301 25.184 -4.486 23.979 1.00 18.65 C
ANISOU 2425 CG ASN A 301 1612 3382 2089 -470 -276 -92 C
ATOM 2426 OD1 ASN A 301 25.057 -5.354 24.847 1.00 20.44 O
ANISOU 2426 OD1 ASN A 301 1839 3497 2431 -459 -231 112 O
ATOM 2427 ND2 ASN A 301 24.167 -4.078 23.240 1.00 17.74 N
ANISOU 2427 ND2 ASN A 301 1453 2482 2805 -225 -320 -352 N
ATOM 2428 C ASN A 301 29.000 -3.929 24.267 1.00 20.95 C
ANISOU 2428 C ASN A 301 1704 3627 2627 -802 -387 -260 C
ATOM 2429 O ASN A 301 29.517 -2.800 24.268 1.00 23.91 O
ANISOU 2429 O ASN A 301 1978 3539 3565 -886 -435 -437 O
ATOM 2430 N THR A 302 29.630 -5.028 23.846 1.00 23.80 N
ANISOU 2430 N THR A 302 2136 3757 3147 -542 -249 -281 N
ATOM 2431 CA THR A 302 30.974 -5.036 23.308 1.00 25.92 C
ANISOU 2431 CA THR A 302 2248 4492 3106 -514 -141 -329 C
ATOM 2432 CB THR A 302 31.904 -5.932 24.136 1.00 26.39 C
ANISOU 2432 CB THR A 302 2067 4868 3090 -549 -394 -251 C
ATOM 2433 OG1 THR A 302 31.447 -7.277 24.044 1.00 26.28 O
ANISOU 2433 OG1 THR A 302 2287 4625 3071 -49 -368 -122 O
ATOM 2434 CG2 THR A 302 31.965 -5.521 25.591 1.00 29.11 C
ANISOU 2434 CG2 THR A 302 2653 5190 3216 -488 -286 -291 C
ATOM 2435 C THR A 302 30.988 -5.498 21.843 1.00 25.18 C
ANISOU 2435 C THR A 302 1914 4817 2833 -388 -44 43 C
ATOM 2436 O THR A 302 31.998 -5.304 21.167 1.00 30.66 O
ANISOU 2436 O THR A 302 2098 5847 3701 -435 378 202 O
ATOM 2437 N LYS A 303 29.917 -6.162 21.396 1.00 23.18 N
ANISOU 2437 N LYS A 303 1677 4539 2590 -332 81 73 N
ATOM 2438 CA LYS A 303 29.743 -6.596 20.020 1.00 24.26 C
ANISOU 2438 CA LYS A 303 2081 4411 2725 -20 -193 13 C
ATOM 2439 CB LYS A 303 29.556 -8.114 19.975 1.00 25.48 C
ANISOU 2439 CB LYS A 303 2376 4473 2832 100 -278 336 C
ATOM 2440 CG LYS A 303 30.797 -8.863 20.436 1.00 31.55 C
ANISOU 2440 CG LYS A 303 3276 5104 3607 512 -941 808 C
ATOM 2441 CD LYS A 303 30.596 -10.324 20.663 1.00 35.73 C
ANISOU 2441 CD LYS A 303 3847 5702 4025 68 -691 890 C
ATOM 2442 CE LYS A 303 30.266 -10.671 22.101 1.00 37.32 C
ANISOU 2442 CE LYS A 303 4066 6039 4072 138 -475 939 C
ATOM 2443 NZ LYS A 303 29.807 -12.078 22.232 1.00 35.00 N
ANISOU 2443 NZ LYS A 303 3334 5626 4337 490 -1378 1050 N
ATOM 2444 C LYS A 303 28.568 -5.833 19.401 1.00 21.00 C
ANISOU 2444 C LYS A 303 1554 3752 2674 -175 147 -137 C
ATOM 2445 O LYS A 303 27.676 -5.331 20.101 1.00 20.95 O
ANISOU 2445 O LYS A 303 1432 3839 2689 -57 -39 -349 O
ATOM 2446 N ASP A 304 28.579 -5.730 18.069 1.00 20.84 N
ANISOU 2446 N ASP A 304 1636 3652 2628 -201 -206 -151 N
ATOM 2447 CA ASP A 304 27.563 -4.966 17.379 1.00 19.94 C
ANISOU 2447 CA ASP A 304 1512 3378 2684 -218 -3 -133 C
ATOM 2448 CB ASP A 304 27.830 -4.875 15.878 1.00 20.62 C
ANISOU 2448 CB ASP A 304 1762 3584 2489 -209 -124 -127 C
ATOM 2449 CG ASP A 304 29.077 -4.106 15.496 1.00 22.52 C
ANISOU 2449 CG ASP A 304 1672 3944 2938 -220 38 -104 C
ATOM 2450 OD1 ASP A 304 29.406 -3.145 16.206 1.00 24.70 O
ANISOU 2450 OD1 ASP A 304 2160 4559 2666 -538 204 -417 O
ATOM 2451 OD2 ASP A 304 29.714 -4.485 14.482 1.00 26.10 O
ANISOU 2451 OD2 ASP A 304 1951 4600 3363 -271 574 -101 O
ATOM 2452 C ASP A 304 26.207 -5.619 17.590 1.00 18.72 C
ANISOU 2452 C ASP A 304 1546 3207 2357 -188 60 -235 C
ATOM 2453 O ASP A 304 26.049 -6.820 17.361 1.00 19.59 O
ANISOU 2453 O ASP A 304 1919 3116 2408 199 -85 -404 O
ATOM 2454 N PRO A 305 25.167 -4.874 18.005 1.00 17.84 N
ANISOU 2454 N PRO A 305 1560 2731 2486 -78 -58 -151 N
ATOM 2455 CA PRO A 305 23.845 -5.482 18.162 1.00 16.80 C
ANISOU 2455 CA PRO A 305 1619 2568 2197 -76 -21 34 C
ATOM 2456 CB PRO A 305 23.019 -4.363 18.817 1.00 17.07 C
ANISOU 2456 CB PRO A 305 1561 2805 2118 -53 56 -12 C
ATOM 2457 CG PRO A 305 23.699 -3.085 18.380 1.00 18.84 C
ANISOU 2457 CG PRO A 305 1781 3055 2320 -286 137 -62 C
ATOM 2458 CD PRO A 305 25.176 -3.434 18.347 1.00 17.87 C
ANISOU 2458 CD PRO A 305 1633 2928 2228 -442 -11 -171 C
ATOM 2459 C PRO A 305 23.254 -5.915 16.817 1.00 16.70 C
ANISOU 2459 C PRO A 305 1503 2612 2228 -47 -5 48 C
ATOM 2460 O PRO A 305 22.393 -6.786 16.784 1.00 15.92 O
ANISOU 2460 O PRO A 305 1546 2395 2108 -7 71 -111 O
ATOM 2461 N TYR A 306 23.742 -5.308 15.736 1.00 17.06 N
ANISOU 2461 N TYR A 306 1603 2560 2317 -298 69 -11 N
ATOM 2462 CA TYR A 306 23.311 -5.616 14.369 1.00 16.73 C
ANISOU 2462 CA TYR A 306 1430 2723 2201 102 -41 74 C
ATOM 2463 CB TYR A 306 23.264 -4.343 13.525 1.00 18.77 C
ANISOU 2463 CB TYR A 306 1914 2599 2616 -65 153 134 C
ATOM 2464 CG TYR A 306 24.557 -3.570 13.500 1.00 19.75 C
ANISOU 2464 CG TYR A 306 2027 2710 2765 -208 -11 538 C
ATOM 2465 CD1 TYR A 306 25.590 -3.927 12.647 1.00 21.81 C
ANISOU 2465 CD1 TYR A 306 2113 2798 3375 -444 140 301 C
ATOM 2466 CE1 TYR A 306 26.783 -3.228 12.632 1.00 23.29 C
ANISOU 2466 CE1 TYR A 306 2035 3267 3546 -530 314 635 C
ATOM 2467 CZ TYR A 306 26.958 -2.144 13.476 1.00 23.35 C
ANISOU 2467 CZ TYR A 306 2040 3295 3537 -1003 12 764 C
ATOM 2468 OH TYR A 306 28.132 -1.443 13.454 1.00 27.13 O
ANISOU 2468 OH TYR A 306 1893 3791 4624 -956 -138 1127 O
ATOM 2469 CE2 TYR A 306 25.944 -1.764 14.330 1.00 24.47 C
ANISOU 2469 CE2 TYR A 306 2469 3271 3557 -604 -280 539 C
ATOM 2470 CD2 TYR A 306 24.759 -2.482 14.343 1.00 22.53 C
ANISOU 2470 CD2 TYR A 306 2269 3221 3068 -421 -6 432 C
ATOM 2471 C TYR A 306 24.243 -6.635 13.704 1.00 17.06 C
ANISOU 2471 C TYR A 306 1758 2596 2126 -35 219 76 C
ATOM 2472 O TYR A 306 24.105 -6.899 12.518 1.00 19.02 O
ANISOU 2472 O TYR A 306 2234 2820 2173 -73 173 -148 O
ATOM 2473 N GLY A 307 25.180 -7.208 14.469 1.00 17.55 N
ANISOU 2473 N GLY A 307 1787 2847 2031 105 161 -146 N
ATOM 2474 CA GLY A 307 26.072 -8.263 13.945 1.00 20.08 C
ANISOU 2474 CA GLY A 307 1956 3165 2505 212 461 -125 C
ATOM 2475 C GLY A 307 25.439 -9.642 14.028 1.00 18.96 C
ANISOU 2475 C GLY A 307 2178 2842 2181 458 279 -207 C
ATOM 2476 O GLY A 307 24.240 -9.783 14.249 1.00 17.71 O
ANISOU 2476 O GLY A 307 2138 2688 1901 590 204 40 O
ATOM 2477 N ILE A 308 26.273 -10.672 13.915 1.00 19.68 N
ANISOU 2477 N ILE A 308 2015 2991 2471 480 564 -136 N
ATOM 2478 CA ILE A 308 25.842 -12.065 14.001 1.00 20.19 C
ANISOU 2478 CA ILE A 308 1966 2923 2781 603 584 -19 C
ATOM 2479 CB ILE A 308 27.079 -12.999 14.038 1.00 23.61 C
ANISOU 2479 CB ILE A 308 2641 2732 3596 977 795 -420 C
ATOM 2480 CG1 ILE A 308 27.872 -12.935 12.738 1.00 29.72 C
ANISOU 2480 CG1 ILE A 308 3515 4045 3731 1144 829 -66 C
ATOM 2481 CG2 ILE A 308 26.662 -14.422 14.361 1.00 27.04 C
ANISOU 2481 CG2 ILE A 308 3568 2982 3722 889 819 -378 C
ATOM 2482 CD1 ILE A 308 29.242 -13.553 12.829 1.00 31.52 C
ANISOU 2482 CD1 ILE A 308 3579 3726 4670 1295 848 -133 C
ATOM 2483 C ILE A 308 24.988 -12.215 15.262 1.00 18.19 C
ANISOU 2483 C ILE A 308 1891 2728 2292 619 171 18 C
ATOM 2484 O ILE A 308 25.434 -11.878 16.364 1.00 18.95 O
ANISOU 2484 O ILE A 308 2228 2772 2198 524 11 9 O
ATOM 2485 N PRO A 309 23.747 -12.731 15.170 1.00 17.36 N
ANISOU 2485 N PRO A 309 1951 2778 1863 378 -4 53 N
ATOM 2486 CA PRO A 309 22.873 -12.747 16.347 1.00 17.01 C
ANISOU 2486 CA PRO A 309 1943 2626 1892 453 65 49 C
ATOM 2487 CB PRO A 309 21.552 -13.342 15.830 1.00 17.61 C
ANISOU 2487 CB PRO A 309 1914 2686 2089 398 86 24 C
ATOM 2488 CG PRO A 309 21.569 -13.008 14.352 1.00 20.24 C
ANISOU 2488 CG PRO A 309 2354 3130 2205 308 -137 0 C
ATOM 2489 CD PRO A 309 23.024 -13.052 13.928 1.00 18.40 C
ANISOU 2489 CD PRO A 309 2302 2869 1820 325 -76 156 C
ATOM 2490 C PRO A 309 23.463 -13.534 17.518 1.00 16.11 C
ANISOU 2490 C PRO A 309 1679 2580 1861 570 101 -100 C
ATOM 2491 O PRO A 309 23.340 -13.098 18.674 1.00 16.39 O
ANISOU 2491 O PRO A 309 1877 2454 1896 366 -71 -209 O
ATOM 2492 N GLY A 310 24.093 -14.666 17.219 1.00 19.09 N
ANISOU 2492 N GLY A 310 2322 2810 2119 968 49 -1 N
ATOM 2493 CA GLY A 310 24.684 -15.504 18.263 1.00 19.94 C
ANISOU 2493 CA GLY A 310 2348 3078 2149 790 -31 100 C
ATOM 2494 C GLY A 310 25.825 -14.848 19.020 1.00 20.14 C
ANISOU 2494 C GLY A 310 2350 3263 2036 792 26 -69 C
ATOM 2495 O GLY A 310 26.217 -15.363 20.070 1.00 22.33 O
ANISOU 2495 O GLY A 310 2590 3524 2370 681 -427 23 O
ATOM 2496 N GLU A 311 26.386 -13.753 18.491 1.00 19.81 N
ANISOU 2496 N GLU A 311 2086 3356 2085 751 -14 53 N
ATOM 2497 CA AGLU A 311 27.486 -13.049 19.142 0.50 20.84 C
ANISOU 2497 CA AGLU A 311 1928 3548 2441 792 -95 -52 C
ATOM 2498 CA BGLU A 311 27.489 -13.042 19.130 0.50 20.72 C
ANISOU 2498 CA BGLU A 311 1943 3510 2420 739 -7 -29 C
ATOM 2499 CB AGLU A 311 28.566 -12.623 18.142 0.50 22.39 C
ANISOU 2499 CB AGLU A 311 1930 3778 2796 724 -23 -52 C
ATOM 2500 CB BGLU A 311 28.545 -12.579 18.116 0.50 22.57 C
ANISOU 2500 CB BGLU A 311 2089 3676 2809 660 176 -4 C
ATOM 2501 CG AGLU A 311 29.345 -13.795 17.553 0.50 24.57 C
ANISOU 2501 CG AGLU A 311 2061 4017 3256 1036 -173 -184 C
ATOM 2502 CG BGLU A 311 29.320 -13.713 17.458 0.50 24.66 C
ANISOU 2502 CG BGLU A 311 2236 3888 3242 909 198 -92 C
ATOM 2503 CD AGLU A 311 30.307 -14.529 18.480 0.50 26.50 C
ANISOU 2503 CD AGLU A 311 1833 4602 3630 1400 -244 -344 C
ATOM 2504 CD BGLU A 311 30.542 -13.307 16.631 0.50 26.68 C
ANISOU 2504 CD BGLU A 311 2403 4271 3462 1054 493 -106 C
ATOM 2505 OE1AGLU A 311 30.967 -15.481 18.014 0.50 32.29 O
ANISOU 2505 OE1AGLU A 311 3683 3794 4791 1536 -420 -476 O
ATOM 2506 OE1BGLU A 311 30.831 -12.082 16.531 0.50 28.96 O
ANISOU 2506 OE1BGLU A 311 2855 4194 3952 1600 697 -27 O
ATOM 2507 OE2AGLU A 311 30.410 -14.157 19.662 0.50 29.66 O
ANISOU 2507 OE2AGLU A 311 2360 5041 3868 1224 -153 -603 O
ATOM 2508 OE2BGLU A 311 31.220 -14.214 16.084 0.50 28.73 O
ANISOU 2508 OE2BGLU A 311 2467 4214 4235 1170 337 -176 O
ATOM 2509 C GLU A 311 26.978 -11.836 19.933 1.00 19.04 C
ANISOU 2509 C GLU A 311 1707 3412 2114 479 -107 -15 C
ATOM 2510 O GLU A 311 27.756 -11.212 20.652 1.00 20.24 O
ANISOU 2510 O GLU A 311 1899 3451 2339 325 -239 -110 O
ATOM 2511 N ARG A 312 25.686 -11.481 19.818 1.00 17.69 N
ANISOU 2511 N ARG A 312 1720 2915 2085 418 -18 -87 N
ATOM 2512 CA ARG A 312 25.179 -10.378 20.648 1.00 17.99 C
ANISOU 2512 CA ARG A 312 1807 2838 2189 273 -206 -130 C
ATOM 2513 CB ARG A 312 23.689 -10.124 20.417 1.00 16.60 C
ANISOU 2513 CB ARG A 312 1733 2683 1891 292 -16 -83 C
ATOM 2514 CG ARG A 312 23.370 -9.590 19.026 1.00 15.74 C
ANISOU 2514 CG ARG A 312 1562 2467 1951 153 -83 -54 C
ATOM 2515 CD ARG A 312 21.878 -9.357 18.832 1.00 15.35 C
ANISOU 2515 CD ARG A 312 1519 2497 1815 205 78 -128 C
ATOM 2516 NE ARG A 312 21.452 -8.203 19.609 1.00 14.91 N
ANISOU 2516 NE ARG A 312 1536 2409 1718 69 -109 -270 N
ATOM 2517 CZ ARG A 312 20.233 -7.688 19.582 1.00 14.85 C
ANISOU 2517 CZ ARG A 312 1540 2158 1944 28 -139 -259 C
ATOM 2518 NH1 ARG A 312 19.272 -8.292 18.874 1.00 13.95 N
ANISOU 2518 NH1 ARG A 312 1641 1979 1679 -64 -133 -152 N
ATOM 2519 NH2 ARG A 312 19.992 -6.581 20.277 1.00 15.39 N
ANISOU 2519 NH2 ARG A 312 1957 1996 1891 9 -34 -162 N
ATOM 2520 C ARG A 312 25.437 -10.700 22.127 1.00 17.63 C
ANISOU 2520 C ARG A 312 1724 2796 2178 334 -357 -90 C
ATOM 2521 O ARG A 312 25.258 -11.835 22.572 1.00 19.25 O
ANISOU 2521 O ARG A 312 2217 2969 2125 294 -402 242 O
ATOM 2522 N ASN A 313 25.820 -9.676 22.896 1.00 17.25 N
ANISOU 2522 N ASN A 313 1719 2836 1997 238 -312 -35 N
ATOM 2523 CA ASN A 313 26.116 -9.888 24.312 1.00 18.33 C
ANISOU 2523 CA ASN A 313 1673 3202 2086 124 -497 47 C
ATOM 2524 CB ASN A 313 26.573 -8.613 25.009 1.00 19.97 C
ANISOU 2524 CB ASN A 313 1878 3278 2431 -82 -425 55 C
ATOM 2525 CG ASN A 313 27.905 -8.116 24.477 1.00 22.25 C
ANISOU 2525 CG ASN A 313 1982 3719 2750 -348 -534 145 C
ATOM 2526 OD1 ASN A 313 27.936 -7.289 23.562 1.00 22.02 O
ANISOU 2526 OD1 ASN A 313 2204 3601 2560 -364 -774 97 O
ATOM 2527 ND2 ASN A 313 28.995 -8.612 25.040 1.00 25.46 N
ANISOU 2527 ND2 ASN A 313 1975 4256 3442 -261 -751 346 N
ATOM 2528 C ASN A 313 24.881 -10.418 25.036 1.00 18.65 C
ANISOU 2528 C ASN A 313 1692 3170 2221 -6 -580 2 C
ATOM 2529 O ASN A 313 23.781 -9.862 24.862 1.00 18.55 O
ANISOU 2529 O ASN A 313 1602 3162 2282 11 -422 16 O
ATOM 2530 N LYS A 314 25.058 -11.495 25.816 1.00 19.10 N
ANISOU 2530 N LYS A 314 1615 3307 2333 144 -355 140 N
ATOM 2531 CA LYS A 314 23.934 -12.104 26.542 1.00 19.74 C
ANISOU 2531 CA LYS A 314 2004 3258 2237 163 -180 234 C
ATOM 2532 CB LYS A 314 24.038 -13.632 26.489 1.00 20.49 C
ANISOU 2532 CB LYS A 314 2231 3194 2358 215 -269 446 C
ATOM 2533 CG LYS A 314 23.988 -14.229 25.086 1.00 23.04 C
ANISOU 2533 CG LYS A 314 2508 3403 2841 371 -127 -45 C
ATOM 2534 CD LYS A 314 24.181 -15.732 25.090 1.00 26.01 C
ANISOU 2534 CD LYS A 314 2801 3439 3641 448 -386 409 C
ATOM 2535 CE LYS A 314 23.908 -16.422 23.765 1.00 30.31 C
ANISOU 2535 CE LYS A 314 3560 4093 3860 611 -79 138 C
ATOM 2536 NZ LYS A 314 24.777 -15.923 22.672 1.00 35.89 N
ANISOU 2536 NZ LYS A 314 3925 5242 4470 464 199 306 N
ATOM 2537 C LYS A 314 23.957 -11.603 27.983 1.00 19.97 C
ANISOU 2537 C LYS A 314 1864 3539 2182 665 -222 318 C
ATOM 2538 O LYS A 314 24.803 -12.014 28.785 1.00 25.21 O
ANISOU 2538 O LYS A 314 2571 5097 1907 1151 -567 48 O
ATOM 2539 N HIS A 315 23.058 -10.667 28.287 1.00 17.45 N
ANISOU 2539 N HIS A 315 1500 3169 1961 361 -318 186 N
ATOM 2540 CA HIS A 315 22.958 -10.086 29.621 1.00 17.58 C
ANISOU 2540 CA HIS A 315 1536 3225 1919 -40 -513 128 C
ATOM 2541 CB HIS A 315 22.424 -8.662 29.521 1.00 17.98 C
ANISOU 2541 CB HIS A 315 1558 3193 2079 11 -340 -186 C
ATOM 2542 CG HIS A 315 23.290 -7.782 28.695 1.00 19.54 C
ANISOU 2542 CG HIS A 315 1869 3050 2505 88 -127 -13 C
ATOM 2543 ND1 HIS A 315 24.519 -7.350 29.153 1.00 21.18 N
ANISOU 2543 ND1 HIS A 315 2395 2989 2663 -409 -359 73 N
ATOM 2544 CE1 HIS A 315 25.072 -6.581 28.230 1.00 24.81 C
ANISOU 2544 CE1 HIS A 315 2687 3506 3230 -276 259 160 C
ATOM 2545 NE2 HIS A 315 24.219 -6.479 27.192 1.00 24.30 N
ANISOU 2545 NE2 HIS A 315 2627 3525 3079 -10 382 -4 N
ATOM 2546 CD2 HIS A 315 23.110 -7.234 27.468 1.00 20.68 C
ANISOU 2546 CD2 HIS A 315 2191 3216 2447 -5 -249 -152 C
ATOM 2547 C HIS A 315 22.062 -10.961 30.496 1.00 18.06 C
ANISOU 2547 C HIS A 315 1714 3244 1902 125 -403 229 C
ATOM 2548 O HIS A 315 21.061 -11.488 30.003 1.00 18.11 O
ANISOU 2548 O HIS A 315 1768 3364 1748 45 -271 20 O
ATOM 2549 N ILE A 316 22.391 -11.059 31.787 1.00 19.20 N
ANISOU 2549 N ILE A 316 2047 3409 1839 8 -425 95 N
ATOM 2550 CA ILE A 316 21.580 -11.839 32.711 1.00 18.98 C
ANISOU 2550 CA ILE A 316 1924 3388 1897 3 -483 44 C
ATOM 2551 CB ILE A 316 22.331 -13.094 33.203 1.00 21.85 C
ANISOU 2551 CB ILE A 316 1941 3757 2605 265 -352 300 C
ATOM 2552 CG1 ILE A 316 22.789 -13.957 32.028 1.00 22.20 C
ANISOU 2552 CG1 ILE A 316 2049 3919 2466 555 -190 498 C
ATOM 2553 CG2 ILE A 316 21.463 -13.904 34.165 1.00 22.89 C
ANISOU 2553 CG2 ILE A 316 2196 3849 2653 519 -359 595 C
ATOM 2554 CD1 ILE A 316 23.596 -15.190 32.424 1.00 26.18 C
ANISOU 2554 CD1 ILE A 316 2814 3982 3151 800 -85 658 C
ATOM 2555 C ILE A 316 21.157 -10.937 33.880 1.00 18.21 C
ANISOU 2555 C ILE A 316 1806 3233 1879 -51 -449 -69 C
ATOM 2556 O ILE A 316 22.015 -10.261 34.493 1.00 18.65 O
ANISOU 2556 O ILE A 316 2136 3169 1779 -79 -364 -316 O
ATOM 2557 N LEU A 317 19.872 -11.030 34.245 1.00 16.46 N
ANISOU 2557 N LEU A 317 1829 2983 1442 -144 -578 -111 N
ATOM 2558 CA LEU A 317 19.376 -10.459 35.488 1.00 17.02 C
ANISOU 2558 CA LEU A 317 1797 2982 1685 -184 -543 -296 C
ATOM 2559 CB LEU A 317 18.474 -9.248 35.226 1.00 17.45 C
ANISOU 2559 CB LEU A 317 1857 2842 1930 -253 -415 -346 C
ATOM 2560 CG LEU A 317 19.178 -7.959 34.820 1.00 17.74 C
ANISOU 2560 CG LEU A 317 1946 2735 2060 -252 -155 -354 C
ATOM 2561 CD1 LEU A 317 18.174 -6.910 34.347 1.00 18.91 C
ANISOU 2561 CD1 LEU A 317 2333 2694 2155 -243 -44 -197 C
ATOM 2562 CD2 LEU A 317 20.030 -7.421 35.968 1.00 19.91 C
ANISOU 2562 CD2 LEU A 317 2376 2919 2270 -500 -365 -205 C
ATOM 2563 C LEU A 317 18.599 -11.548 36.227 1.00 18.07 C
ANISOU 2563 C LEU A 317 2028 3167 1670 -84 -356 -122 C
ATOM 2564 O LEU A 317 17.822 -12.307 35.595 1.00 18.12 O
ANISOU 2564 O LEU A 317 2204 2824 1855 189 -571 -59 O
ATOM 2565 N THR A 318 18.760 -11.570 37.549 1.00 18.91 N
ANISOU 2565 N THR A 318 2147 3240 1796 201 -710 -109 N
ATOM 2566 CA THR A 318 18.012 -12.483 38.405 1.00 18.98 C
ANISOU 2566 CA THR A 318 2376 3073 1762 288 -455 -163 C
ATOM 2567 CB THR A 318 18.941 -13.559 38.977 1.00 20.65 C
ANISOU 2567 CB THR A 318 2538 3412 1892 452 -855 -335 C
ATOM 2568 OG1 THR A 318 19.642 -14.196 37.911 1.00 22.17 O
ANISOU 2568 OG1 THR A 318 2572 3667 2183 678 -406 -64 O
ATOM 2569 CG2 THR A 318 18.197 -14.598 39.788 1.00 24.02 C
ANISOU 2569 CG2 THR A 318 2974 3820 2331 349 -340 -185 C
ATOM 2570 C THR A 318 17.372 -11.698 39.548 1.00 18.63 C
ANISOU 2570 C THR A 318 2119 3036 1922 199 -397 -127 C
ATOM 2571 O THR A 318 18.062 -10.979 40.295 1.00 19.49 O
ANISOU 2571 O THR A 318 2146 2928 2329 -148 -346 -36 O
ATOM 2572 N THR A 319 16.059 -11.867 39.704 1.00 17.86 N
ANISOU 2572 N THR A 319 2105 2846 1835 174 -338 73 N
ATOM 2573 CA THR A 319 15.368 -11.214 40.811 1.00 17.94 C
ANISOU 2573 CA THR A 319 2459 2436 1919 289 -402 -89 C
ATOM 2574 CB THR A 319 13.853 -11.427 40.779 1.00 17.47 C
ANISOU 2574 CB THR A 319 2364 2526 1745 296 -275 -82 C
ATOM 2575 OG1 THR A 319 13.532 -12.796 41.021 1.00 18.15 O
ANISOU 2575 OG1 THR A 319 2322 2661 1909 -12 -415 -120 O
ATOM 2576 CG2 THR A 319 13.202 -10.988 39.487 1.00 18.20 C
ANISOU 2576 CG2 THR A 319 2330 2647 1936 136 -465 45 C
ATOM 2577 C THR A 319 15.884 -11.763 42.144 1.00 19.18 C
ANISOU 2577 C THR A 319 2295 3185 1807 42 -454 -98 C
ATOM 2578 O THR A 319 16.423 -12.868 42.205 1.00 21.12 O
ANISOU 2578 O THR A 319 2595 3578 1851 378 -766 -80 O
ATOM 2579 N HIS A 320 15.707 -10.974 43.202 1.00 19.94 N
ANISOU 2579 N HIS A 320 2727 3034 1812 -137 -302 -107 N
ATOM 2580 CA HIS A 320 15.753 -11.497 44.545 1.00 21.28 C
ANISOU 2580 CA HIS A 320 2726 3601 1757 -212 -597 -217 C
ATOM 2581 CB HIS A 320 15.663 -10.362 45.577 1.00 24.13 C
ANISOU 2581 CB HIS A 320 3638 3798 1730 -331 -440 -279 C
ATOM 2582 CG HIS A 320 16.725 -9.328 45.417 1.00 29.16 C
ANISOU 2582 CG HIS A 320 3913 4577 2588 -885 -737 -289 C
ATOM 2583 ND1 HIS A 320 18.062 -9.632 45.553 1.00 34.34 N
ANISOU 2583 ND1 HIS A 320 3855 5378 3814 -803 -553 -117 N
ATOM 2584 CE1 HIS A 320 18.783 -8.543 45.355 1.00 34.77 C
ANISOU 2584 CE1 HIS A 320 4352 5130 3727 -911 -766 -537 C
ATOM 2585 NE2 HIS A 320 17.949 -7.534 45.075 1.00 36.60 N
ANISOU 2585 NE2 HIS A 320 4670 4818 4416 -1098 -736 -413 N
ATOM 2586 CD2 HIS A 320 16.660 -8.008 45.116 1.00 34.80 C
ANISOU 2586 CD2 HIS A 320 4511 4766 3942 -872 -1015 -35 C
ATOM 2587 C HIS A 320 14.592 -12.490 44.692 1.00 19.30 C
ANISOU 2587 C HIS A 320 2271 3329 1734 125 -545 -90 C
ATOM 2588 O HIS A 320 13.677 -12.537 43.849 1.00 20.98 O
ANISOU 2588 O HIS A 320 2291 3979 1699 -73 -552 44 O
ATOM 2589 N SER A 321 14.615 -13.268 45.770 1.00 21.93 N
ANISOU 2589 N SER A 321 2521 3868 1941 81 -366 212 N
ATOM 2590 CA SER A 321 13.515 -14.166 46.055 1.00 21.50 C
ANISOU 2590 CA SER A 321 2649 3543 1975 72 -517 162 C
ATOM 2591 CB SER A 321 13.841 -15.098 47.193 1.00 25.23 C
ANISOU 2591 CB SER A 321 3271 3972 2342 197 -327 593 C
ATOM 2592 OG SER A 321 12.846 -16.106 47.322 1.00 27.86 O
ANISOU 2592 OG SER A 321 3538 3933 3112 169 -187 892 O
ATOM 2593 C SER A 321 12.254 -13.334 46.329 1.00 22.13 C
ANISOU 2593 C SER A 321 2567 3808 2033 -45 -285 -131 C
ATOM 2594 O SER A 321 12.276 -12.363 47.078 1.00 25.78 O
ANISOU 2594 O SER A 321 2931 4563 2300 46 -259 -667 O
ATOM 2595 N MET A 322 11.164 -13.714 45.674 1.00 19.85 N
ANISOU 2595 N MET A 322 2646 3258 1638 5 -326 -139 N
ATOM 2596 CA MET A 322 9.870 -13.033 45.797 1.00 19.41 C
ANISOU 2596 CA MET A 322 2844 2942 1587 159 30 -436 C
ATOM 2597 CB MET A 322 9.248 -12.744 44.423 1.00 19.36 C
ANISOU 2597 CB MET A 322 2679 2608 2068 189 -243 -30 C
ATOM 2598 CG MET A 322 10.154 -11.892 43.544 1.00 19.85 C
ANISOU 2598 CG MET A 322 2730 2969 1842 351 7 -61 C
ATOM 2599 SD MET A 322 9.542 -11.641 41.881 1.00 20.65 S
ANISOU 2599 SD MET A 322 2850 2928 2066 579 -133 17 S
ATOM 2600 CE MET A 322 9.945 -13.213 41.129 1.00 18.60 C
ANISOU 2600 CE MET A 322 2303 2676 2085 487 -139 96 C
ATOM 2601 C MET A 322 8.931 -13.929 46.609 1.00 18.82 C
ANISOU 2601 C MET A 322 2826 2708 1616 296 -126 -206 C
ATOM 2602 O MET A 322 8.549 -15.004 46.160 1.00 20.31 O
ANISOU 2602 O MET A 322 2887 2882 1947 122 -67 -263 O
ATOM 2603 N ALA A 323 8.551 -13.437 47.787 1.00 19.39 N
ANISOU 2603 N ALA A 323 2880 2943 1545 162 -60 -240 N
ATOM 2604 CA ALA A 323 7.685 -14.147 48.719 1.00 21.03 C
ANISOU 2604 CA ALA A 323 2895 3308 1786 59 -83 -250 C
ATOM 2605 CB ALA A 323 8.035 -13.791 50.141 1.00 22.68 C
ANISOU 2605 CB ALA A 323 2889 4008 1717 -54 -10 -355 C
ATOM 2606 C ALA A 323 6.235 -13.788 48.412 1.00 19.93 C
ANISOU 2606 C ALA A 323 2866 3021 1685 155 -135 -474 C
ATOM 2607 O ALA A 323 5.877 -12.622 48.419 1.00 24.85 O
ANISOU 2607 O ALA A 323 3103 3150 3187 220 -27 -785 O
ATOM 2608 N MET A 324 5.422 -14.805 48.141 1.00 20.54 N
ANISOU 2608 N MET A 324 2824 2875 2101 212 100 -488 N
ATOM 2609 CA MET A 324 4.003 -14.628 47.870 1.00 20.25 C
ANISOU 2609 CA MET A 324 2871 2820 2001 44 -21 -253 C
ATOM 2610 CB MET A 324 3.688 -15.003 46.422 1.00 19.49 C
ANISOU 2610 CB MET A 324 2739 2638 2027 -16 -371 13 C
ATOM 2611 CG MET A 324 4.371 -14.089 45.440 1.00 21.04 C
ANISOU 2611 CG MET A 324 3138 2816 2038 -165 -224 -107 C
ATOM 2612 SD MET A 324 4.161 -14.589 43.727 1.00 23.58 S
ANISOU 2612 SD MET A 324 3272 3789 1898 -7 -286 28 S
ATOM 2613 CE MET A 324 5.670 -15.506 43.501 1.00 24.43 C
ANISOU 2613 CE MET A 324 3394 3394 2494 129 -167 81 C
ATOM 2614 C MET A 324 3.204 -15.494 48.848 1.00 19.37 C
ANISOU 2614 C MET A 324 2916 2849 1595 192 -154 -199 C
ATOM 2615 O MET A 324 3.577 -16.619 49.136 1.00 21.97 O
ANISOU 2615 O MET A 324 2801 3125 2419 503 285 276 O
ATOM 2616 N ASN A 325 2.095 -14.952 49.338 1.00 18.83 N
ANISOU 2616 N ASN A 325 2679 2908 1568 191 -329 -298 N
ATOM 2617 CA ASN A 325 1.267 -15.599 50.357 1.00 20.36 C
ANISOU 2617 CA ASN A 325 3196 2841 1698 261 -104 -113 C
ATOM 2618 CB ASN A 325 0.517 -14.558 51.194 1.00 25.55 C
ANISOU 2618 CB ASN A 325 3819 3519 2367 338 113 -717 C
ATOM 2619 CG ASN A 325 1.449 -13.706 52.023 1.00 32.79 C
ANISOU 2619 CG ASN A 325 4432 4566 3458 177 -521 -933 C
ATOM 2620 OD1 ASN A 325 2.507 -14.167 52.438 1.00 40.53 O
ANISOU 2620 OD1 ASN A 325 4852 6652 3894 643 -986 -1244 O
ATOM 2621 ND2 ASN A 325 1.054 -12.474 52.299 1.00 40.83 N
ANISOU 2621 ND2 ASN A 325 6279 4820 4412 569 -261 -1030 N
ATOM 2622 C ASN A 325 0.245 -16.550 49.723 1.00 17.04 C
ANISOU 2622 C ASN A 325 2701 2492 1282 477 -42 24 C
ATOM 2623 O ASN A 325 -0.458 -17.277 50.427 1.00 21.16 O
ANISOU 2623 O ASN A 325 3284 3092 1663 216 197 213 O
ATOM 2624 N ASN A 326 0.120 -16.497 48.394 1.00 15.68 N
ANISOU 2624 N ASN A 326 2581 2076 1298 287 -175 155 N
ATOM 2625 CA ASN A 326 -0.858 -17.291 47.627 1.00 16.60 C
ANISOU 2625 CA ASN A 326 2669 2152 1483 278 -158 79 C
ATOM 2626 CB ASN A 326 -2.245 -16.671 47.733 1.00 17.18 C
ANISOU 2626 CB ASN A 326 2651 2439 1436 251 -140 -74 C
ATOM 2627 CG ASN A 326 -2.246 -15.242 47.256 1.00 18.55 C
ANISOU 2627 CG ASN A 326 2968 2388 1691 453 3 -149 C
ATOM 2628 OD1 ASN A 326 -2.157 -15.013 46.041 1.00 20.42 O
ANISOU 2628 OD1 ASN A 326 3717 2203 1835 554 -23 114 O
ATOM 2629 ND2 ASN A 326 -2.280 -14.280 48.188 1.00 18.83 N
ANISOU 2629 ND2 ASN A 326 2580 2383 2190 536 -184 -349 N
ATOM 2630 C ASN A 326 -0.330 -17.389 46.195 1.00 16.01 C
ANISOU 2630 C ASN A 326 2450 2152 1480 325 -211 47 C
ATOM 2631 O ASN A 326 0.611 -16.668 45.840 1.00 18.06 O
ANISOU 2631 O ASN A 326 2527 2700 1633 127 -120 -99 O
ATOM 2632 N VAL A 327 -0.950 -18.250 45.378 1.00 13.80 N
ANISOU 2632 N VAL A 327 2018 1892 1331 321 -70 145 N
ATOM 2633 CA VAL A 327 -0.455 -18.535 44.039 1.00 14.84 C
ANISOU 2633 CA VAL A 327 2179 2010 1447 499 -92 73 C
ATOM 2634 CB VAL A 327 -0.523 -20.040 43.759 1.00 15.44 C
ANISOU 2634 CB VAL A 327 2281 2064 1520 507 -99 3 C
ATOM 2635 CG1 VAL A 327 0.033 -20.357 42.381 1.00 16.64 C
ANISOU 2635 CG1 VAL A 327 2269 2377 1675 576 171 187 C
ATOM 2636 CG2 VAL A 327 0.204 -20.842 44.838 1.00 16.75 C
ANISOU 2636 CG2 VAL A 327 2507 2379 1478 428 -64 197 C
ATOM 2637 C VAL A 327 -1.259 -17.755 43.009 1.00 14.08 C
ANISOU 2637 C VAL A 327 2246 1669 1433 442 -8 117 C
ATOM 2638 O VAL A 327 -2.440 -18.017 42.797 1.00 15.60 O
ANISOU 2638 O VAL A 327 2398 1897 1631 500 -208 180 O
ATOM 2639 N PRO A 328 -0.639 -16.790 42.308 1.00 13.32 N
ANISOU 2639 N PRO A 328 2144 1774 1141 325 -119 124 N
ATOM 2640 CA PRO A 328 -1.336 -16.058 41.248 1.00 13.03 C
ANISOU 2640 CA PRO A 328 2122 1554 1273 297 -136 115 C
ATOM 2641 CB PRO A 328 -0.327 -15.007 40.805 1.00 14.89 C
ANISOU 2641 CB PRO A 328 2291 1819 1547 50 -84 167 C
ATOM 2642 CG PRO A 328 0.572 -14.834 42.014 1.00 15.94 C
ANISOU 2642 CG PRO A 328 2295 2002 1758 114 -242 278 C
ATOM 2643 CD PRO A 328 0.680 -16.221 42.602 1.00 15.24 C
ANISOU 2643 CD PRO A 328 2245 1944 1601 258 -63 132 C
ATOM 2644 C PRO A 328 -1.728 -16.915 40.042 1.00 12.86 C
ANISOU 2644 C PRO A 328 1993 1697 1194 254 -73 107 C
ATOM 2645 O PRO A 328 -1.141 -17.955 39.778 1.00 16.13 O
ANISOU 2645 O PRO A 328 2640 1833 1653 545 -284 -23 O
ATOM 2646 N SER A 329 -2.717 -16.415 39.310 1.00 13.10 N
ANISOU 2646 N SER A 329 2008 1757 1210 505 13 5 N
ATOM 2647 CA SER A 329 -3.171 -17.000 38.060 1.00 12.79 C
ANISOU 2647 CA SER A 329 1805 1754 1301 262 78 -43 C
ATOM 2648 CB SER A 329 -4.428 -16.312 37.626 1.00 15.28 C
ANISOU 2648 CB SER A 329 1594 2430 1781 299 22 -285 C
ATOM 2649 OG SER A 329 -4.871 -16.751 36.355 1.00 18.14 O
ANISOU 2649 OG SER A 329 2263 2509 2117 306 -104 -596 O
ATOM 2650 C SER A 329 -2.123 -16.919 36.951 1.00 12.49 C
ANISOU 2650 C SER A 329 1793 1681 1268 308 26 32 C
ATOM 2651 O SER A 329 -2.027 -17.830 36.120 1.00 13.48 O
ANISOU 2651 O SER A 329 2262 1456 1402 411 226 55 O
ATOM 2652 N MET A 330 -1.420 -15.782 36.862 1.00 12.65 N
ANISOU 2652 N MET A 330 1962 1654 1191 203 143 -143 N
ATOM 2653 CA MET A 330 -0.513 -15.577 35.758 1.00 12.33 C
ANISOU 2653 CA MET A 330 1765 1526 1394 181 227 -138 C
ATOM 2654 CB MET A 330 -1.221 -15.024 34.506 1.00 14.24 C
ANISOU 2654 CB MET A 330 1664 1851 1893 -90 -108 64 C
ATOM 2655 CG MET A 330 -0.381 -15.103 33.204 1.00 17.27 C
ANISOU 2655 CG MET A 330 1837 2574 2148 -113 27 607 C
ATOM 2656 SD MET A 330 -1.256 -14.487 31.755 1.00 19.00 S
ANISOU 2656 SD MET A 330 2520 2757 1942 -11 -143 136 S
ATOM 2657 CE MET A 330 -2.494 -15.757 31.525 1.00 18.47 C
ANISOU 2657 CE MET A 330 2476 2396 2144 -22 -222 193 C
ATOM 2658 C MET A 330 0.608 -14.641 36.205 1.00 12.48 C
ANISOU 2658 C MET A 330 1926 1452 1364 216 -10 -44 C
ATOM 2659 O MET A 330 0.426 -13.819 37.097 1.00 13.15 O
ANISOU 2659 O MET A 330 1975 1670 1352 286 29 -144 O
ATOM 2660 N PHE A 331 1.762 -14.792 35.559 1.00 12.98 N
ANISOU 2660 N PHE A 331 1980 1643 1308 63 17 -87 N
ATOM 2661 CA PHE A 331 2.911 -13.935 35.722 1.00 12.54 C
ANISOU 2661 CA PHE A 331 1827 1648 1289 130 -118 -56 C
ATOM 2662 CB PHE A 331 4.121 -14.719 36.238 1.00 14.61 C
ANISOU 2662 CB PHE A 331 1898 2097 1553 314 -88 80 C
ATOM 2663 CG PHE A 331 3.901 -15.276 37.612 1.00 16.71 C
ANISOU 2663 CG PHE A 331 2109 2612 1628 463 -139 242 C
ATOM 2664 CD1 PHE A 331 4.165 -14.519 38.740 1.00 19.12 C
ANISOU 2664 CD1 PHE A 331 2716 2906 1641 539 -47 191 C
ATOM 2665 CE1 PHE A 331 3.961 -15.040 40.004 1.00 21.21 C
ANISOU 2665 CE1 PHE A 331 3094 3290 1675 699 -145 419 C
ATOM 2666 CZ PHE A 331 3.448 -16.300 40.140 1.00 20.98 C
ANISOU 2666 CZ PHE A 331 2939 3533 1500 550 266 915 C
ATOM 2667 CD2 PHE A 331 3.414 -16.555 37.769 1.00 18.72 C
ANISOU 2667 CD2 PHE A 331 2514 2765 1834 421 -43 804 C
ATOM 2668 CE2 PHE A 331 3.166 -17.057 39.035 1.00 21.40 C
ANISOU 2668 CE2 PHE A 331 2790 3488 1852 456 -30 889 C
ATOM 2669 C PHE A 331 3.279 -13.337 34.372 1.00 12.85 C
ANISOU 2669 C PHE A 331 1740 1829 1312 91 -198 57 C
ATOM 2670 O PHE A 331 2.979 -13.934 33.318 1.00 12.54 O
ANISOU 2670 O PHE A 331 1700 1756 1306 225 -195 -1 O
ATOM 2671 N ALA A 332 3.964 -12.198 34.419 1.00 13.76 N
ANISOU 2671 N ALA A 332 1913 1916 1397 34 -149 -212 N
ATOM 2672 CA ALA A 332 4.482 -11.560 33.196 1.00 14.06 C
ANISOU 2672 CA ALA A 332 1848 1996 1496 -56 -108 -196 C
ATOM 2673 CB ALA A 332 3.623 -10.405 32.739 1.00 14.88 C
ANISOU 2673 CB ALA A 332 1851 2309 1491 37 -288 -100 C
ATOM 2674 C ALA A 332 5.904 -11.095 33.482 1.00 13.64 C
ANISOU 2674 C ALA A 332 1672 1981 1527 -25 -4 -39 C
ATOM 2675 O ALA A 332 6.143 -10.444 34.513 1.00 15.53 O
ANISOU 2675 O ALA A 332 1983 2161 1755 -108 -16 -97 O
ATOM 2676 N VAL A 333 6.816 -11.415 32.563 1.00 13.01 N
ANISOU 2676 N VAL A 333 1640 2039 1261 -187 -16 -22 N
ATOM 2677 CA VAL A 333 8.217 -11.053 32.672 1.00 13.24 C
ANISOU 2677 CA VAL A 333 1613 1888 1528 -91 -66 -196 C
ATOM 2678 CB VAL A 333 9.115 -12.304 32.612 1.00 14.04 C
ANISOU 2678 CB VAL A 333 1895 1788 1650 -23 -155 -126 C
ATOM 2679 CG1 VAL A 333 10.585 -11.957 32.736 1.00 14.31 C
ANISOU 2679 CG1 VAL A 333 1906 1757 1773 62 -41 -107 C
ATOM 2680 CG2 VAL A 333 8.694 -13.314 33.655 1.00 15.57 C
ANISOU 2680 CG2 VAL A 333 1990 1932 1993 73 -198 151 C
ATOM 2681 C VAL A 333 8.584 -10.122 31.517 1.00 13.84 C
ANISOU 2681 C VAL A 333 1663 1962 1630 -141 -179 -69 C
ATOM 2682 O VAL A 333 8.293 -10.427 30.360 1.00 15.22 O
ANISOU 2682 O VAL A 333 2173 2037 1571 16 -159 -18 O
ATOM 2683 N MET A 334 9.230 -8.994 31.835 1.00 13.79 N
ANISOU 2683 N MET A 334 1565 2115 1556 -195 -192 -217 N
ATOM 2684 CA MET A 334 9.604 -7.978 30.852 1.00 15.70 C
ANISOU 2684 CA MET A 334 1638 2317 2009 -383 142 -182 C
ATOM 2685 CB MET A 334 8.472 -6.931 30.884 1.00 21.18 C
ANISOU 2685 CB MET A 334 1907 2689 3449 -53 -480 457 C
ATOM 2686 CG MET A 334 8.590 -5.743 30.057 1.00 24.70 C
ANISOU 2686 CG MET A 334 2653 2881 3849 -104 -125 216 C
ATOM 2687 SD MET A 334 7.059 -4.816 30.234 1.00 31.91 S
ANISOU 2687 SD MET A 334 3324 2742 6058 498 646 76 S
ATOM 2688 CE MET A 334 7.266 -4.028 31.813 1.00 35.09 C
ANISOU 2688 CE MET A 334 4450 3518 5363 323 107 784 C
ATOM 2689 C MET A 334 10.931 -7.382 31.321 1.00 14.26 C
ANISOU 2689 C MET A 334 1738 2263 1417 -355 -55 111 C
ATOM 2690 O MET A 334 11.130 -7.228 32.529 1.00 17.11 O
ANISOU 2690 O MET A 334 2177 2952 1370 -659 -37 155 O
ATOM 2691 N VAL A 335 11.818 -7.036 30.389 1.00 13.55 N
ANISOU 2691 N VAL A 335 1716 2009 1421 -546 -62 -48 N
ATOM 2692 CA VAL A 335 13.057 -6.330 30.711 1.00 14.10 C
ANISOU 2692 CA VAL A 335 1741 1988 1628 -459 -165 -165 C
ATOM 2693 CB VAL A 335 14.307 -7.159 30.361 1.00 15.22 C
ANISOU 2693 CB VAL A 335 1935 2249 1599 -374 -69 -136 C
ATOM 2694 CG1 VAL A 335 15.583 -6.383 30.645 1.00 16.45 C
ANISOU 2694 CG1 VAL A 335 1962 2384 1903 -401 -123 -62 C
ATOM 2695 CG2 VAL A 335 14.316 -8.507 31.061 1.00 14.91 C
ANISOU 2695 CG2 VAL A 335 1803 2345 1517 -293 -86 -58 C
ATOM 2696 C VAL A 335 13.014 -5.002 29.940 1.00 14.25 C
ANISOU 2696 C VAL A 335 1729 2143 1540 -307 -156 -128 C
ATOM 2697 O VAL A 335 13.073 -4.995 28.696 1.00 16.34 O
ANISOU 2697 O VAL A 335 2326 2327 1555 -42 153 -214 O
ATOM 2698 N SER A 336 12.914 -3.896 30.676 1.00 15.64 N
ANISOU 2698 N SER A 336 2049 2229 1661 -323 -277 -325 N
ATOM 2699 CA ASER A 336 12.643 -2.565 30.098 0.50 15.84 C
ANISOU 2699 CA ASER A 336 2161 2193 1663 -397 -309 -355 C
ATOM 2700 CA BSER A 336 12.654 -2.574 30.077 0.50 16.65 C
ANISOU 2700 CA BSER A 336 2268 2260 1797 -452 -347 -233 C
ATOM 2701 CB ASER A 336 11.568 -1.811 30.876 0.50 16.89 C
ANISOU 2701 CB ASER A 336 2206 2497 1712 -536 -184 -579 C
ATOM 2702 CB BSER A 336 11.546 -1.829 30.791 0.50 19.23 C
ANISOU 2702 CB BSER A 336 2503 2670 2134 -448 -137 -391 C
ATOM 2703 OG ASER A 336 10.279 -2.383 30.731 0.50 16.72 O
ANISOU 2703 OG ASER A 336 2214 2230 1909 -555 -31 -568 O
ATOM 2704 OG BSER A 336 11.715 -1.927 32.180 0.50 21.50 O
ANISOU 2704 OG BSER A 336 3133 2765 2270 -426 -123 34 O
ATOM 2705 C SER A 336 13.928 -1.731 30.085 1.00 16.43 C
ANISOU 2705 C SER A 336 2165 2263 1814 -380 -431 -365 C
ATOM 2706 O SER A 336 14.661 -1.721 31.077 1.00 17.09 O
ANISOU 2706 O SER A 336 2520 2398 1574 -320 -463 -262 O
ATOM 2707 N GLN A 337 14.127 -0.974 29.001 1.00 17.05 N
ANISOU 2707 N GLN A 337 2293 2318 1866 -564 -464 -356 N
ATOM 2708 CA GLN A 337 15.100 0.097 28.986 1.00 18.02 C
ANISOU 2708 CA GLN A 337 2324 2463 2058 -629 -635 -248 C
ATOM 2709 CB GLN A 337 15.203 0.675 27.578 1.00 19.72 C
ANISOU 2709 CB GLN A 337 2746 2521 2226 -801 -636 -47 C
ATOM 2710 CG GLN A 337 16.305 1.699 27.422 1.00 22.09 C
ANISOU 2710 CG GLN A 337 3029 2877 2485 -1041 -564 30 C
ATOM 2711 CD GLN A 337 16.223 2.281 26.039 1.00 21.80 C
ANISOU 2711 CD GLN A 337 2945 2804 2533 -759 -458 125 C
ATOM 2712 OE1 GLN A 337 15.281 3.005 25.722 1.00 20.89 O
ANISOU 2712 OE1 GLN A 337 2576 2627 2732 -632 -131 -123 O
ATOM 2713 NE2 GLN A 337 17.169 1.894 25.189 1.00 25.73 N
ANISOU 2713 NE2 GLN A 337 2875 3585 3315 -963 -54 -135 N
ATOM 2714 C GLN A 337 14.631 1.163 29.982 1.00 19.09 C
ANISOU 2714 C GLN A 337 2285 2518 2448 -492 -637 -354 C
ATOM 2715 O GLN A 337 13.536 1.684 29.859 1.00 20.37 O
ANISOU 2715 O GLN A 337 2466 2640 2632 -258 -663 -287 O
ATOM 2716 N GLU A 338 15.475 1.490 30.966 1.00 19.23 N
ANISOU 2716 N GLU A 338 2313 2856 2136 -356 -541 -443 N
ATOM 2717 CA AGLU A 338 15.051 2.339 32.081 0.50 20.57 C
ANISOU 2717 CA AGLU A 338 2694 2785 2336 -303 -485 -483 C
ATOM 2718 CA BGLU A 338 15.050 2.337 32.084 0.50 21.43 C
ANISOU 2718 CA BGLU A 338 2907 2804 2432 -229 -452 -505 C
ATOM 2719 CB AGLU A 338 16.038 2.250 33.246 0.50 20.85 C
ANISOU 2719 CB AGLU A 338 2895 2898 2130 -460 -439 -504 C
ATOM 2720 CB BGLU A 338 16.052 2.276 33.239 0.50 23.31 C
ANISOU 2720 CB BGLU A 338 3358 3114 2385 -345 -564 -443 C
ATOM 2721 CG AGLU A 338 15.783 1.021 34.101 0.50 22.47 C
ANISOU 2721 CG AGLU A 338 2997 3112 2427 -583 -281 -312 C
ATOM 2722 CG BGLU A 338 15.713 3.216 34.388 0.50 26.31 C
ANISOU 2722 CG BGLU A 338 3956 3362 2676 -311 -340 -553 C
ATOM 2723 CD AGLU A 338 16.445 0.965 35.469 0.50 23.03 C
ANISOU 2723 CD AGLU A 338 2986 3269 2492 -814 -412 -621 C
ATOM 2724 CD BGLU A 338 14.462 2.859 35.172 0.50 28.82 C
ANISOU 2724 CD BGLU A 338 4001 3849 3100 -398 -267 -639 C
ATOM 2725 OE1AGLU A 338 15.754 1.170 36.471 0.50 28.10 O
ANISOU 2725 OE1AGLU A 338 3316 4234 3127 -868 170 -436 O
ATOM 2726 OE1BGLU A 338 14.033 1.707 35.075 0.50 31.91 O
ANISOU 2726 OE1BGLU A 338 4956 3774 3391 -766 58 160 O
ATOM 2727 OE2AGLU A 338 17.623 0.662 35.532 0.50 27.85 O
ANISOU 2727 OE2AGLU A 338 3398 4399 2782 -152 -686 -88 O
ATOM 2728 OE2BGLU A 338 13.921 3.750 35.862 0.50 31.27 O
ANISOU 2728 OE2BGLU A 338 3838 4590 3452 -138 8 -904 O
ATOM 2729 C GLU A 338 14.820 3.773 31.597 1.00 22.05 C
ANISOU 2729 C GLU A 338 2904 2948 2522 -168 -531 -403 C
ATOM 2730 O GLU A 338 13.847 4.421 32.019 1.00 25.99 O
ANISOU 2730 O GLU A 338 3359 3152 3361 277 -493 -260 O
ATOM 2731 N THR A 339 15.706 4.267 30.729 1.00 22.79 N
ANISOU 2731 N THR A 339 3234 2970 2455 -189 -438 -408 N
ATOM 2732 CA THR A 339 15.703 5.667 30.346 1.00 25.25 C
ANISOU 2732 CA THR A 339 3604 3060 2926 -241 -984 -255 C
ATOM 2733 CB THR A 339 16.970 6.375 30.846 1.00 28.00 C
ANISOU 2733 CB THR A 339 4231 2996 3409 -619 -1172 -480 C
ATOM 2734 OG1 THR A 339 17.083 6.141 32.248 1.00 32.53 O
ANISOU 2734 OG1 THR A 339 5204 3614 3539 -769 -1217 -292 O
ATOM 2735 CG2 THR A 339 16.951 7.865 30.578 1.00 31.08 C
ANISOU 2735 CG2 THR A 339 4388 3350 4071 -605 -1238 109 C
ATOM 2736 C THR A 339 15.591 5.790 28.831 1.00 24.80 C
ANISOU 2736 C THR A 339 3504 3058 2860 -248 -863 -474 C
ATOM 2737 O THR A 339 16.535 5.467 28.110 1.00 26.80 O
ANISOU 2737 O THR A 339 3641 3377 3162 -196 -593 -153 O
ATOM 2738 N PRO A 340 14.435 6.258 28.298 1.00 22.76 N
ANISOU 2738 N PRO A 340 3128 2799 2722 -336 -556 -416 N
ATOM 2739 CA PRO A 340 14.324 6.522 26.869 1.00 22.40 C
ANISOU 2739 CA PRO A 340 3153 2592 2764 -282 -612 -164 C
ATOM 2740 CB PRO A 340 12.902 7.075 26.718 1.00 23.19 C
ANISOU 2740 CB PRO A 340 3238 3018 2552 -150 -774 -351 C
ATOM 2741 CG PRO A 340 12.147 6.482 27.894 1.00 24.01 C
ANISOU 2741 CG PRO A 340 3282 3100 2741 79 -465 -493 C
ATOM 2742 CD PRO A 340 13.168 6.477 29.015 1.00 24.58 C
ANISOU 2742 CD PRO A 340 3410 3042 2886 -14 -622 -730 C
ATOM 2743 C PRO A 340 15.364 7.566 26.428 1.00 23.19 C
ANISOU 2743 C PRO A 340 2984 2605 3221 -447 -706 -354 C
ATOM 2744 O PRO A 340 15.584 8.539 27.143 1.00 26.08 O
ANISOU 2744 O PRO A 340 3838 2815 3253 -846 -420 -479 O
ATOM 2745 N THR A 341 15.963 7.361 25.249 1.00 23.73 N
ANISOU 2745 N THR A 341 2865 2799 3350 -242 -463 185 N
ATOM 2746 CA THR A 341 16.905 8.321 24.687 1.00 25.72 C
ANISOU 2746 CA THR A 341 2706 3431 3633 -274 -673 601 C
ATOM 2747 CB THR A 341 18.036 7.628 23.916 1.00 29.89 C
ANISOU 2747 CB THR A 341 3142 4340 3872 208 -236 716 C
ATOM 2748 OG1 THR A 341 17.488 6.831 22.872 1.00 29.40 O
ANISOU 2748 OG1 THR A 341 2885 4322 3961 56 132 511 O
ATOM 2749 CG2 THR A 341 18.895 6.762 24.812 1.00 32.37 C
ANISOU 2749 CG2 THR A 341 3549 4811 3935 148 -178 1192 C
ATOM 2750 C THR A 341 16.200 9.360 23.807 1.00 23.93 C
ANISOU 2750 C THR A 341 2950 2891 3249 -597 -580 609 C
ATOM 2751 O THR A 341 16.789 10.380 23.487 1.00 29.55 O
ANISOU 2751 O THR A 341 3691 3299 4234 -1246 -871 600 O
ATOM 2752 N LYS A 342 14.972 9.052 23.383 1.00 22.99 N
ANISOU 2752 N LYS A 342 2425 3153 3156 26 -5 437 N
ATOM 2753 CA ALYS A 342 14.124 9.935 22.601 0.30 22.56 C
ANISOU 2753 CA ALYS A 342 2532 3001 3038 -126 -43 447 C
ATOM 2754 CA BLYS A 342 14.128 9.941 22.602 0.70 23.34 C
ANISOU 2754 CA BLYS A 342 2583 3108 3175 -91 -3 434 C
ATOM 2755 CB ALYS A 342 13.997 9.392 21.174 0.30 22.64 C
ANISOU 2755 CB ALYS A 342 2642 3105 2855 45 -44 701 C
ATOM 2756 CB BLYS A 342 13.983 9.407 21.174 0.70 25.30 C
ANISOU 2756 CB BLYS A 342 3006 3515 3090 45 105 604 C
ATOM 2757 CG ALYS A 342 15.285 9.424 20.361 0.30 23.15 C
ANISOU 2757 CG ALYS A 342 2796 3261 2737 41 -14 732 C
ATOM 2758 CG BLYS A 342 15.272 9.287 20.370 0.70 28.06 C
ANISOU 2758 CG BLYS A 342 3513 3943 3203 -30 386 277 C
ATOM 2759 CD ALYS A 342 15.684 10.834 19.995 0.30 22.99 C
ANISOU 2759 CD ALYS A 342 2875 3273 2586 52 -176 861 C
ATOM 2760 CD BLYS A 342 15.023 8.585 19.055 0.70 31.77 C
ANISOU 2760 CD BLYS A 342 4185 4420 3463 -426 232 3 C
ATOM 2761 CE ALYS A 342 16.977 10.921 19.217 0.30 23.86 C
ANISOU 2761 CE ALYS A 342 3174 3475 2418 80 -39 827 C
ATOM 2762 CE BLYS A 342 15.540 9.324 17.836 0.70 31.95 C
ANISOU 2762 CE BLYS A 342 4542 4377 3220 -330 -158 134 C
ATOM 2763 NZ ALYS A 342 17.411 12.328 19.081 0.30 25.04 N
ANISOU 2763 NZ ALYS A 342 3354 3583 2574 -98 -167 773 N
ATOM 2764 NZ BLYS A 342 14.792 8.960 16.606 0.70 26.66 N
ANISOU 2764 NZ BLYS A 342 3306 3938 2885 -502 88 362 N
ATOM 2765 C LYS A 342 12.762 9.965 23.292 1.00 21.75 C
ANISOU 2765 C LYS A 342 2540 2727 2996 -134 10 173 C
ATOM 2766 O LYS A 342 12.308 8.937 23.774 1.00 27.28 O
ANISOU 2766 O LYS A 342 2810 3090 4466 -4 691 831 O
ATOM 2767 N LYS A 343 12.098 11.116 23.315 1.00 17.70 N
ANISOU 2767 N LYS A 343 2162 2310 2252 -594 -326 -82 N
ATOM 2768 CA LYS A 343 10.860 11.213 24.102 1.00 17.70 C
ANISOU 2768 CA LYS A 343 2315 2331 2077 -650 -194 -366 C
ATOM 2769 CB LYS A 343 10.601 12.658 24.532 1.00 21.06 C
ANISOU 2769 CB LYS A 343 2796 2420 2787 -485 -241 -460 C
ATOM 2770 CG LYS A 343 11.598 13.228 25.535 1.00 26.81 C
ANISOU 2770 CG LYS A 343 3562 3512 3113 -402 -693 -907 C
ATOM 2771 CD LYS A 343 11.207 14.629 25.972 1.00 32.93 C
ANISOU 2771 CD LYS A 343 4759 3948 3803 -47 -589 -1321 C
ATOM 2772 CE LYS A 343 12.187 15.283 26.920 1.00 40.95 C
ANISOU 2772 CE LYS A 343 5388 5670 4497 -439 -1352 -966 C
ATOM 2773 NZ LYS A 343 12.230 14.588 28.227 1.00 49.04 N
ANISOU 2773 NZ LYS A 343 6809 6732 5092 -308 -534 -390 N
ATOM 2774 C LYS A 343 9.631 10.704 23.332 1.00 15.25 C
ANISOU 2774 C LYS A 343 2132 1846 1817 -601 11 -261 C
ATOM 2775 O LYS A 343 8.635 10.372 23.960 1.00 15.94 O
ANISOU 2775 O LYS A 343 2211 2133 1711 -566 82 -125 O
ATOM 2776 N PHE A 344 9.683 10.668 21.993 1.00 14.92 N
ANISOU 2776 N PHE A 344 1942 1948 1778 -406 0 -373 N
ATOM 2777 CA PHE A 344 8.459 10.481 21.190 1.00 13.09 C
ANISOU 2777 CA PHE A 344 1896 1553 1521 -103 27 -308 C
ATOM 2778 CB PHE A 344 8.156 11.750 20.381 1.00 13.44 C
ANISOU 2778 CB PHE A 344 2019 1531 1557 -264 0 -231 C
ATOM 2779 CG PHE A 344 8.211 12.978 21.249 1.00 14.02 C
ANISOU 2779 CG PHE A 344 2061 1484 1782 -277 85 -267 C
ATOM 2780 CD1 PHE A 344 7.251 13.182 22.219 1.00 13.91 C
ANISOU 2780 CD1 PHE A 344 2178 1370 1735 -125 84 -178 C
ATOM 2781 CE1 PHE A 344 7.329 14.267 23.064 1.00 15.12 C
ANISOU 2781 CE1 PHE A 344 2358 1518 1868 -309 176 -301 C
ATOM 2782 CZ PHE A 344 8.388 15.153 22.976 1.00 15.60 C
ANISOU 2782 CZ PHE A 344 2185 1704 2038 -326 78 -261 C
ATOM 2783 CD2 PHE A 344 9.267 13.867 21.173 1.00 15.21 C
ANISOU 2783 CD2 PHE A 344 1901 1857 2019 -330 122 -176 C
ATOM 2784 CE2 PHE A 344 9.338 14.967 22.011 1.00 16.68 C
ANISOU 2784 CE2 PHE A 344 2164 1833 2338 -622 241 -223 C
ATOM 2785 C PHE A 344 8.534 9.231 20.317 1.00 12.90 C
ANISOU 2785 C PHE A 344 1722 1455 1724 -151 -129 -317 C
ATOM 2786 O PHE A 344 7.754 9.117 19.391 1.00 12.95 O
ANISOU 2786 O PHE A 344 1790 1470 1659 15 -135 -195 O
ATOM 2787 N ALA A 345 9.422 8.301 20.692 1.00 13.43 N
ANISOU 2787 N ALA A 345 1879 1574 1650 -46 -187 -304 N
ATOM 2788 CA ALA A 345 9.703 7.084 19.974 1.00 13.58 C
ANISOU 2788 CA ALA A 345 1798 1529 1832 -207 9 -314 C
ATOM 2789 CB ALA A 345 11.199 6.860 19.881 1.00 15.57 C
ANISOU 2789 CB ALA A 345 1878 1792 2244 -116 56 -313 C
ATOM 2790 C ALA A 345 9.040 5.898 20.666 1.00 12.98 C
ANISOU 2790 C ALA A 345 1590 1553 1786 -80 57 -250 C
ATOM 2791 O ALA A 345 8.564 6.014 21.790 1.00 14.44 O
ANISOU 2791 O ALA A 345 1968 1740 1776 -136 145 -395 O
ATOM 2792 N PRO A 346 9.020 4.718 20.026 1.00 13.27 N
ANISOU 2792 N PRO A 346 1760 1517 1763 -102 10 -250 N
ATOM 2793 CA PRO A 346 8.515 3.521 20.684 1.00 12.08 C
ANISOU 2793 CA PRO A 346 1426 1629 1535 -102 68 -161 C
ATOM 2794 CB PRO A 346 8.753 2.420 19.636 1.00 13.35 C
ANISOU 2794 CB PRO A 346 1771 1592 1708 -20 -45 -224 C
ATOM 2795 CG PRO A 346 8.693 3.165 18.314 1.00 12.72 C
ANISOU 2795 CG PRO A 346 1820 1435 1576 153 -4 -357 C
ATOM 2796 CD PRO A 346 9.434 4.449 18.633 1.00 13.10 C
ANISOU 2796 CD PRO A 346 1694 1502 1780 18 86 -144 C
ATOM 2797 C PRO A 346 9.256 3.215 21.989 1.00 13.42 C
ANISOU 2797 C PRO A 346 1723 1711 1662 0 -53 -229 C
ATOM 2798 O PRO A 346 10.467 3.443 22.094 1.00 13.62 O
ANISOU 2798 O PRO A 346 1781 1660 1734 -72 -69 -138 O
ATOM 2799 N ASP A 347 8.527 2.613 22.921 1.00 13.61 N
ANISOU 2799 N ASP A 347 1682 1721 1767 -63 -190 1 N
ATOM 2800 CA ASP A 347 9.144 2.087 24.117 1.00 13.96 C
ANISOU 2800 CA ASP A 347 1509 1970 1823 94 -311 -53 C
ATOM 2801 CB ASP A 347 8.083 1.627 25.111 1.00 15.78 C
ANISOU 2801 CB ASP A 347 1952 2128 1915 66 -92 78 C
ATOM 2802 CG ASP A 347 7.485 2.767 25.930 1.00 19.36 C
ANISOU 2802 CG ASP A 347 2268 2445 2639 321 525 22 C
ATOM 2803 OD1 ASP A 347 8.123 3.853 26.045 1.00 21.64 O
ANISOU 2803 OD1 ASP A 347 3387 2340 2496 283 580 -58 O
ATOM 2804 OD2 ASP A 347 6.493 2.517 26.550 1.00 24.73 O
ANISOU 2804 OD2 ASP A 347 2126 3511 3757 683 679 421 O
ATOM 2805 C ASP A 347 10.057 0.909 23.751 1.00 13.13 C
ANISOU 2805 C ASP A 347 1679 1758 1550 -63 -166 -204 C
ATOM 2806 O ASP A 347 9.766 0.125 22.849 1.00 15.21 O
ANISOU 2806 O ASP A 347 1920 1846 2013 115 -444 -470 O
ATOM 2807 N GLN A 348 11.180 0.809 24.449 1.00 12.94 N
ANISOU 2807 N GLN A 348 1504 1688 1724 -118 -72 -82 N
ATOM 2808 CA GLN A 348 12.176 -0.223 24.190 1.00 13.25 C
ANISOU 2808 CA GLN A 348 1571 1875 1589 12 -233 -222 C
ATOM 2809 CB GLN A 348 13.573 0.395 24.048 1.00 14.60 C
ANISOU 2809 CB GLN A 348 1580 2235 1729 22 -150 -16 C
ATOM 2810 CG GLN A 348 14.640 -0.650 23.738 1.00 15.83 C
ANISOU 2810 CG GLN A 348 1650 2453 1910 40 93 10 C
ATOM 2811 CD GLN A 348 14.580 -1.075 22.290 1.00 17.02 C
ANISOU 2811 CD GLN A 348 2004 2559 1903 34 101 82 C
ATOM 2812 OE1 GLN A 348 14.947 -0.302 21.386 1.00 18.62 O
ANISOU 2812 OE1 GLN A 348 2150 2798 2124 108 202 264 O
ATOM 2813 NE2 GLN A 348 14.122 -2.290 22.032 1.00 18.11 N
ANISOU 2813 NE2 GLN A 348 2006 2603 2272 408 201 -126 N
ATOM 2814 C GLN A 348 12.189 -1.247 25.333 1.00 13.43 C
ANISOU 2814 C GLN A 348 1722 1849 1530 -42 -262 -280 C
ATOM 2815 O GLN A 348 12.391 -0.891 26.503 1.00 14.46 O
ANISOU 2815 O GLN A 348 1930 1957 1606 -202 -337 -353 O
ATOM 2816 N LEU A 349 12.034 -2.520 24.957 1.00 13.64 N
ANISOU 2816 N LEU A 349 1740 1893 1549 40 -209 -388 N
ATOM 2817 CA LEU A 349 12.259 -3.668 25.812 1.00 13.65 C
ANISOU 2817 CA LEU A 349 1798 1894 1494 63 -212 -326 C
ATOM 2818 CB LEU A 349 11.025 -4.582 25.854 1.00 13.70 C
ANISOU 2818 CB LEU A 349 1827 1671 1707 69 -149 -371 C
ATOM 2819 CG LEU A 349 9.683 -3.922 26.170 1.00 15.09 C
ANISOU 2819 CG LEU A 349 1626 2058 2050 -155 -3 -455 C
ATOM 2820 CD1 LEU A 349 8.523 -4.906 26.053 1.00 16.32 C
ANISOU 2820 CD1 LEU A 349 1809 2033 2359 -166 63 -478 C
ATOM 2821 CD2 LEU A 349 9.683 -3.270 27.545 1.00 17.41 C
ANISOU 2821 CD2 LEU A 349 1993 2208 2413 -84 152 -838 C
ATOM 2822 C LEU A 349 13.470 -4.437 25.279 1.00 14.24 C
ANISOU 2822 C LEU A 349 1850 1895 1662 75 -254 -315 C
ATOM 2823 O LEU A 349 13.870 -4.267 24.133 1.00 16.97 O
ANISOU 2823 O LEU A 349 2455 2241 1749 559 -19 -160 O
ATOM 2824 N ALA A 350 14.055 -5.275 26.130 1.00 14.22 N
ANISOU 2824 N ALA A 350 1837 2078 1486 -51 -432 -345 N
ATOM 2825 CA ALA A 350 15.093 -6.178 25.682 1.00 14.05 C
ANISOU 2825 CA ALA A 350 1658 1973 1705 -209 -290 -262 C
ATOM 2826 CB ALA A 350 15.993 -6.567 26.828 1.00 15.34 C
ANISOU 2826 CB ALA A 350 2117 2120 1589 -194 -349 -201 C
ATOM 2827 C ALA A 350 14.461 -7.405 25.015 1.00 13.15 C
ANISOU 2827 C ALA A 350 1629 1989 1375 -123 -363 -203 C
ATOM 2828 O ALA A 350 13.300 -7.718 25.244 1.00 13.85 O
ANISOU 2828 O ALA A 350 1588 2054 1617 -104 -330 -52 O
ATOM 2829 N GLY A 351 15.257 -8.092 24.191 1.00 13.94 N
ANISOU 2829 N GLY A 351 1720 2065 1512 -197 -220 -205 N
ATOM 2830 CA GLY A 351 14.859 -9.382 23.632 1.00 13.11 C
ANISOU 2830 CA GLY A 351 1531 1889 1561 118 -283 -152 C
ATOM 2831 C GLY A 351 15.276 -10.508 24.549 1.00 13.26 C
ANISOU 2831 C GLY A 351 1570 1912 1554 183 -68 -62 C
ATOM 2832 O GLY A 351 16.467 -10.740 24.719 1.00 14.51 O
ANISOU 2832 O GLY A 351 1569 2166 1776 77 -156 -175 O
ATOM 2833 N ILE A 352 14.301 -11.190 25.144 1.00 12.81 N
ANISOU 2833 N ILE A 352 1516 1813 1536 160 -186 24 N
ATOM 2834 CA ILE A 352 14.589 -12.269 26.094 1.00 13.66 C
ANISOU 2834 CA ILE A 352 1789 1871 1529 330 -148 0 C
ATOM 2835 CB ILE A 352 13.466 -12.453 27.138 1.00 13.69 C
ANISOU 2835 CB ILE A 352 1689 1989 1522 78 -243 -41 C
ATOM 2836 CG1 ILE A 352 13.263 -11.170 27.956 1.00 13.99 C
ANISOU 2836 CG1 ILE A 352 1600 2097 1619 232 -190 -23 C
ATOM 2837 CG2 ILE A 352 13.789 -13.660 28.026 1.00 14.31 C
ANISOU 2837 CG2 ILE A 352 1931 1966 1541 238 -154 -97 C
ATOM 2838 CD1 ILE A 352 12.083 -11.202 28.911 1.00 14.34 C
ANISOU 2838 CD1 ILE A 352 1654 2132 1660 389 -183 -16 C
ATOM 2839 C ILE A 352 14.854 -13.551 25.306 1.00 13.68 C
ANISOU 2839 C ILE A 352 1850 1873 1472 207 -173 16 C
ATOM 2840 O ILE A 352 13.995 -13.997 24.550 1.00 14.77 O
ANISOU 2840 O ILE A 352 1913 1911 1789 101 -284 111 O
ATOM 2841 N ILE A 353 16.019 -14.150 25.550 1.00 14.85 N
ANISOU 2841 N ILE A 353 1878 2109 1655 300 -304 -133 N
ATOM 2842 CA ILE A 353 16.448 -15.355 24.841 1.00 15.02 C
ANISOU 2842 CA ILE A 353 1982 2169 1555 511 -250 -82 C
ATOM 2843 CB ILE A 353 17.811 -15.161 24.152 1.00 17.90 C
ANISOU 2843 CB ILE A 353 2130 2705 1965 298 11 -35 C
ATOM 2844 CG1 ILE A 353 18.960 -14.891 25.132 1.00 18.95 C
ANISOU 2844 CG1 ILE A 353 2177 3013 2008 520 -25 346 C
ATOM 2845 CG2 ILE A 353 17.717 -14.073 23.097 1.00 16.38 C
ANISOU 2845 CG2 ILE A 353 1736 2789 1698 417 115 -71 C
ATOM 2846 CD1 ILE A 353 20.314 -14.994 24.488 1.00 19.87 C
ANISOU 2846 CD1 ILE A 353 2301 3218 2030 436 127 443 C
ATOM 2847 C ILE A 353 16.466 -16.586 25.753 1.00 14.90 C
ANISOU 2847 C ILE A 353 1996 2196 1468 429 -159 -97 C
ATOM 2848 O ILE A 353 16.613 -17.714 25.251 1.00 18.09 O
ANISOU 2848 O ILE A 353 2723 2161 1986 554 -406 -152 O
ATOM 2849 N GLY A 354 16.360 -16.370 27.066 1.00 15.17 N
ANISOU 2849 N GLY A 354 2218 2038 1507 586 -245 -100 N
ATOM 2850 CA GLY A 354 16.336 -17.440 28.030 1.00 15.41 C
ANISOU 2850 CA GLY A 354 2314 2045 1494 498 -324 -78 C
ATOM 2851 C GLY A 354 15.610 -17.027 29.286 1.00 15.34 C
ANISOU 2851 C GLY A 354 1908 2132 1788 361 -211 -123 C
ATOM 2852 O GLY A 354 15.662 -15.870 29.672 1.00 14.76 O
ANISOU 2852 O GLY A 354 1935 2012 1659 273 -122 27 O
ATOM 2853 N LEU A 355 14.951 -18.000 29.922 1.00 14.86 N
ANISOU 2853 N LEU A 355 1921 1950 1775 209 -166 -364 N
ATOM 2854 CA LEU A 355 14.235 -17.775 31.151 1.00 15.88 C
ANISOU 2854 CA LEU A 355 2121 2197 1715 192 -208 -262 C
ATOM 2855 CB LEU A 355 12.763 -17.603 30.764 1.00 20.42 C
ANISOU 2855 CB LEU A 355 2009 3142 2606 112 -176 -157 C
ATOM 2856 CG LEU A 355 11.831 -17.039 31.815 1.00 21.52 C
ANISOU 2856 CG LEU A 355 2163 3192 2821 213 -463 -434 C
ATOM 2857 CD1 LEU A 355 12.242 -15.622 32.217 1.00 22.41 C
ANISOU 2857 CD1 LEU A 355 2236 3120 3157 758 -848 -935 C
ATOM 2858 CD2 LEU A 355 10.405 -17.091 31.307 1.00 18.33 C
ANISOU 2858 CD2 LEU A 355 1927 2537 2500 447 -315 39 C
ATOM 2859 C LEU A 355 14.444 -18.998 32.038 1.00 17.48 C
ANISOU 2859 C LEU A 355 2601 2371 1667 258 -75 -247 C
ATOM 2860 O LEU A 355 14.336 -20.107 31.544 1.00 19.16 O
ANISOU 2860 O LEU A 355 2868 2306 2105 -24 32 -268 O
ATOM 2861 N GLU A 356 14.742 -18.768 33.325 1.00 16.42 N
ANISOU 2861 N GLU A 356 2364 2311 1563 99 -42 -139 N
ATOM 2862 CA GLU A 356 14.797 -19.847 34.294 1.00 18.43 C
ANISOU 2862 CA GLU A 356 2792 2489 1720 130 43 46 C
ATOM 2863 CB GLU A 356 16.229 -20.231 34.669 1.00 21.95 C
ANISOU 2863 CB GLU A 356 3013 2964 2363 415 -84 58 C
ATOM 2864 CG GLU A 356 17.038 -20.693 33.488 1.00 25.17 C
ANISOU 2864 CG GLU A 356 3484 3329 2747 652 26 57 C
ATOM 2865 CD GLU A 356 18.398 -21.294 33.779 1.00 28.38 C
ANISOU 2865 CD GLU A 356 3138 3888 3757 575 306 -144 C
ATOM 2866 OE1 GLU A 356 18.671 -21.640 34.952 1.00 33.18 O
ANISOU 2866 OE1 GLU A 356 3909 4261 4435 1116 -575 217 O
ATOM 2867 OE2 GLU A 356 19.177 -21.423 32.810 1.00 34.92 O
ANISOU 2867 OE2 GLU A 356 3898 4838 4531 593 933 -772 O
ATOM 2868 C GLU A 356 14.015 -19.418 35.530 1.00 18.42 C
ANISOU 2868 C GLU A 356 3014 2242 1744 113 123 104 C
ATOM 2869 O GLU A 356 14.242 -18.329 36.069 1.00 20.75 O
ANISOU 2869 O GLU A 356 3632 2586 1663 -166 -80 -135 O
ATOM 2870 N ILE A 357 13.123 -20.302 35.984 1.00 18.14 N
ANISOU 2870 N ILE A 357 2650 2303 1938 214 124 212 N
ATOM 2871 CA ILE A 357 12.242 -20.012 37.092 1.00 18.10 C
ANISOU 2871 CA ILE A 357 2784 2369 1723 294 60 1 C
ATOM 2872 CB ILE A 357 10.755 -20.127 36.681 1.00 18.87 C
ANISOU 2872 CB ILE A 357 2788 2609 1770 261 50 -90 C
ATOM 2873 CG1 ILE A 357 10.406 -19.437 35.359 1.00 21.54 C
ANISOU 2873 CG1 ILE A 357 3710 2919 1556 406 650 -65 C
ATOM 2874 CG2 ILE A 357 9.859 -19.662 37.816 1.00 19.01 C
ANISOU 2874 CG2 ILE A 357 2642 2793 1786 236 155 52 C
ATOM 2875 CD1 ILE A 357 10.477 -17.965 35.367 1.00 22.38 C
ANISOU 2875 CD1 ILE A 357 3614 3052 1838 202 667 316 C
ATOM 2876 C ILE A 357 12.551 -20.985 38.234 1.00 18.37 C
ANISOU 2876 C ILE A 357 2762 2558 1657 417 15 68 C
ATOM 2877 O ILE A 357 12.718 -22.179 38.020 1.00 18.81 O
ANISOU 2877 O ILE A 357 2692 2531 1924 449 -128 184 O
ATOM 2878 N LYS A 358 12.622 -20.452 39.455 1.00 17.36 N
ANISOU 2878 N LYS A 358 2680 2193 1721 328 -101 142 N
ATOM 2879 CA LYS A 358 12.673 -21.249 40.668 1.00 18.77 C
ANISOU 2879 CA LYS A 358 2889 2648 1593 385 -385 153 C
ATOM 2880 CB LYS A 358 13.885 -20.851 41.519 1.00 20.55 C
ANISOU 2880 CB LYS A 358 2986 2741 2081 209 -642 265 C
ATOM 2881 CG LYS A 358 13.891 -21.406 42.942 1.00 24.00 C
ANISOU 2881 CG LYS A 358 3341 3487 2291 292 -584 614 C
ATOM 2882 CD LYS A 358 15.080 -20.916 43.733 1.00 26.44 C
ANISOU 2882 CD LYS A 358 3696 4108 2242 383 -855 237 C
ATOM 2883 CE LYS A 358 15.184 -21.516 45.119 1.00 31.00 C
ANISOU 2883 CE LYS A 358 4333 4849 2597 386 -1586 555 C
ATOM 2884 NZ LYS A 358 16.515 -21.272 45.714 1.00 33.36 N
ANISOU 2884 NZ LYS A 358 4244 5007 3423 179 -1250 65 N
ATOM 2885 C LYS A 358 11.378 -21.002 41.435 1.00 18.78 C
ANISOU 2885 C LYS A 358 2825 2535 1773 267 -347 178 C
ATOM 2886 O LYS A 358 10.988 -19.860 41.618 1.00 19.25 O
ANISOU 2886 O LYS A 358 3215 2479 1621 230 -161 -45 O
ATOM 2887 N VAL A 359 10.723 -22.088 41.860 1.00 19.16 N
ANISOU 2887 N VAL A 359 2975 2671 1633 225 -193 141 N
ATOM 2888 CA VAL A 359 9.582 -22.000 42.766 1.00 19.27 C
ANISOU 2888 CA VAL A 359 3009 2654 1658 306 -192 566 C
ATOM 2889 CB VAL A 359 8.238 -22.319 42.089 1.00 19.46 C
ANISOU 2889 CB VAL A 359 2994 2759 1640 160 -138 191 C
ATOM 2890 CG1 VAL A 359 7.104 -22.238 43.102 1.00 19.77 C
ANISOU 2890 CG1 VAL A 359 3303 2449 1758 317 -17 492 C
ATOM 2891 CG2 VAL A 359 7.951 -21.386 40.925 1.00 20.47 C
ANISOU 2891 CG2 VAL A 359 3086 2650 2041 295 -456 138 C
ATOM 2892 C VAL A 359 9.848 -22.948 43.932 1.00 19.44 C
ANISOU 2892 C VAL A 359 3061 2689 1632 564 -241 524 C
ATOM 2893 O VAL A 359 9.968 -24.146 43.723 1.00 21.42 O
ANISOU 2893 O VAL A 359 3164 2727 2247 350 -352 504 O
ATOM 2894 N ASP A 360 9.964 -22.387 45.139 1.00 20.02 N
ANISOU 2894 N ASP A 360 3198 2688 1721 635 -70 467 N
ATOM 2895 CA ASP A 360 10.270 -23.177 46.327 1.00 21.96 C
ANISOU 2895 CA ASP A 360 3196 2951 2196 899 -306 657 C
ATOM 2896 CB ASP A 360 9.051 -24.026 46.721 1.00 24.35 C
ANISOU 2896 CB ASP A 360 3702 3035 2511 629 -204 449 C
ATOM 2897 CG ASP A 360 7.816 -23.207 47.068 1.00 23.30 C
ANISOU 2897 CG ASP A 360 3664 2711 2477 402 -15 517 C
ATOM 2898 OD1 ASP A 360 7.973 -22.010 47.330 1.00 24.17 O
ANISOU 2898 OD1 ASP A 360 3647 2636 2899 452 472 377 O
ATOM 2899 OD2 ASP A 360 6.706 -23.776 47.103 1.00 26.42 O
ANISOU 2899 OD2 ASP A 360 3690 3539 2807 159 186 707 O
ATOM 2900 C ASP A 360 11.600 -23.892 46.027 1.00 24.24 C
ANISOU 2900 C ASP A 360 3413 3453 2340 1102 -190 547 C
ATOM 2901 O ASP A 360 12.553 -23.210 45.667 1.00 26.29 O
ANISOU 2901 O ASP A 360 3301 4027 2660 600 -324 541 O
ATOM 2902 N SER A 361 11.665 -25.226 46.143 1.00 26.74 N
ANISOU 2902 N SER A 361 3962 3590 2605 1164 -267 918 N
ATOM 2903 CA ASER A 361 12.934 -25.948 46.007 0.50 27.57 C
ANISOU 2903 CA ASER A 361 3816 3568 3092 1162 -273 924 C
ATOM 2904 CA BSER A 361 12.929 -25.955 46.008 0.50 27.91 C
ANISOU 2904 CA BSER A 361 3726 3871 3006 1176 -319 953 C
ATOM 2905 CB ASER A 361 12.998 -27.121 46.956 0.50 28.91 C
ANISOU 2905 CB ASER A 361 4089 3671 3222 1188 -464 1038 C
ATOM 2906 CB BSER A 361 12.969 -27.137 46.947 0.50 29.33 C
ANISOU 2906 CB BSER A 361 3916 4284 2945 1222 -575 1179 C
ATOM 2907 OG ASER A 361 12.070 -28.130 46.588 0.50 30.89 O
ANISOU 2907 OG ASER A 361 4407 3269 4058 1139 -272 919 O
ATOM 2908 OG BSER A 361 12.977 -26.711 48.302 0.50 31.79 O
ANISOU 2908 OG BSER A 361 4124 4887 3066 1170 -531 997 O
ATOM 2909 C SER A 361 13.172 -26.406 44.561 1.00 27.87 C
ANISOU 2909 C SER A 361 4079 3504 3004 1414 -314 1034 C
ATOM 2910 O SER A 361 14.192 -27.022 44.275 1.00 31.08 O
ANISOU 2910 O SER A 361 4659 4212 2936 1812 -311 431 O
ATOM 2911 N ASP A 362 12.244 -26.086 43.655 1.00 26.10 N
ANISOU 2911 N ASP A 362 3714 3385 2817 1145 -40 638 N
ATOM 2912 CA ASP A 362 12.285 -26.508 42.269 1.00 26.50 C
ANISOU 2912 CA ASP A 362 4257 2726 3083 854 228 543 C
ATOM 2913 CB ASP A 362 10.855 -26.767 41.818 1.00 27.21 C
ANISOU 2913 CB ASP A 362 4201 2938 3197 647 413 465 C
ATOM 2914 CG ASP A 362 10.693 -27.640 40.595 1.00 30.13 C
ANISOU 2914 CG ASP A 362 4758 3025 3665 802 661 85 C
ATOM 2915 OD1 ASP A 362 11.647 -27.702 39.775 1.00 34.42 O
ANISOU 2915 OD1 ASP A 362 4784 3906 4388 863 965 -168 O
ATOM 2916 OD2 ASP A 362 9.587 -28.234 40.468 1.00 31.47 O
ANISOU 2916 OD2 ASP A 362 4572 3680 3704 946 -79 -326 O
ATOM 2917 C ASP A 362 12.975 -25.430 41.422 1.00 23.12 C
ANISOU 2917 C ASP A 362 3553 2697 2534 941 39 393 C
ATOM 2918 O ASP A 362 12.430 -24.353 41.257 1.00 23.10 O
ANISOU 2918 O ASP A 362 3415 2812 2546 955 -197 434 O
ATOM 2919 N VAL A 363 14.162 -25.748 40.881 1.00 22.23 N
ANISOU 2919 N VAL A 363 3216 2893 2336 800 -253 339 N
ATOM 2920 CA VAL A 363 15.043 -24.757 40.273 1.00 23.23 C
ANISOU 2920 CA VAL A 363 3104 3353 2369 644 -260 131 C
ATOM 2921 CB VAL A 363 16.414 -24.695 40.976 1.00 27.71 C
ANISOU 2921 CB VAL A 363 3586 4293 2647 650 -684 -261 C
ATOM 2922 CG1 VAL A 363 16.265 -24.406 42.470 1.00 29.12 C
ANISOU 2922 CG1 VAL A 363 3830 4572 2659 587 -930 -208 C
ATOM 2923 CG2 VAL A 363 17.223 -25.955 40.742 1.00 31.30 C
ANISOU 2923 CG2 VAL A 363 3689 4604 3599 755 -948 -301 C
ATOM 2924 C VAL A 363 15.211 -25.044 38.776 1.00 20.77 C
ANISOU 2924 C VAL A 363 2336 3250 2305 464 -261 120 C
ATOM 2925 O VAL A 363 15.047 -26.159 38.298 1.00 23.26 O
ANISOU 2925 O VAL A 363 2833 3320 2685 518 -414 -46 O
ATOM 2926 N GLY A 364 15.550 -23.991 38.035 1.00 20.52 N
ANISOU 2926 N GLY A 364 2277 3212 2306 418 -340 51 N
ATOM 2927 CA GLY A 364 15.967 -24.103 36.645 1.00 21.81 C
ANISOU 2927 CA GLY A 364 2269 3540 2477 484 6 -280 C
ATOM 2928 C GLY A 364 14.843 -24.416 35.668 1.00 19.73 C
ANISOU 2928 C GLY A 364 1939 3054 2502 354 82 -59 C
ATOM 2929 O GLY A 364 15.102 -24.881 34.560 1.00 20.48 O
ANISOU 2929 O GLY A 364 2218 3021 2542 676 11 -99 O
ATOM 2930 N ILE A 365 13.600 -24.132 36.048 1.00 17.09 N
ANISOU 2930 N ILE A 365 1830 2899 1761 341 -95 20 N
ATOM 2931 CA ILE A 365 12.452 -24.447 35.184 1.00 15.99 C
ANISOU 2931 CA ILE A 365 1817 2465 1792 219 -77 10 C
ATOM 2932 CB ILE A 365 11.123 -24.274 35.939 1.00 17.08 C
ANISOU 2932 CB ILE A 365 1929 2665 1895 289 -8 196 C
ATOM 2933 CG1 ILE A 365 11.098 -25.060 37.252 1.00 18.71 C
ANISOU 2933 CG1 ILE A 365 2233 2942 1933 468 -62 317 C
ATOM 2934 CG2 ILE A 365 9.958 -24.648 35.033 1.00 17.60 C
ANISOU 2934 CG2 ILE A 365 1773 2652 2261 197 -65 232 C
ATOM 2935 CD1 ILE A 365 10.105 -24.537 38.249 1.00 20.11 C
ANISOU 2935 CD1 ILE A 365 2043 3467 2130 444 119 542 C
ATOM 2936 C ILE A 365 12.518 -23.545 33.942 1.00 16.34 C
ANISOU 2936 C ILE A 365 1984 2641 1582 285 -5 -30 C
ATOM 2937 O ILE A 365 12.719 -22.330 34.056 1.00 18.22 O
ANISOU 2937 O ILE A 365 2405 2738 1776 246 -63 -97 O
ATOM 2938 N PHE A 366 12.311 -24.155 32.775 1.00 15.73 N
ANISOU 2938 N PHE A 366 2054 2151 1770 373 -100 -86 N
ATOM 2939 CA PHE A 366 12.352 -23.526 31.433 1.00 16.43 C
ANISOU 2939 CA PHE A 366 2159 2364 1719 325 -34 -68 C
ATOM 2940 CB PHE A 366 11.609 -22.189 31.340 1.00 15.37 C
ANISOU 2940 CB PHE A 366 1875 2326 1637 256 -150 -68 C
ATOM 2941 CG PHE A 366 10.128 -22.227 31.634 1.00 15.59 C
ANISOU 2941 CG PHE A 366 1868 2414 1642 235 -111 -104 C
ATOM 2942 CD1 PHE A 366 9.376 -23.383 31.468 1.00 15.60 C
ANISOU 2942 CD1 PHE A 366 1890 2384 1652 226 3 -28 C
ATOM 2943 CE1 PHE A 366 8.008 -23.384 31.719 1.00 15.36 C
ANISOU 2943 CE1 PHE A 366 1955 2411 1470 303 147 -172 C
ATOM 2944 CZ PHE A 366 7.377 -22.239 32.135 1.00 15.71 C
ANISOU 2944 CZ PHE A 366 1703 2388 1877 291 -1 -55 C
ATOM 2945 CD2 PHE A 366 9.470 -21.080 32.042 1.00 16.30 C
ANISOU 2945 CD2 PHE A 366 1969 2528 1693 400 -42 0 C
ATOM 2946 CE2 PHE A 366 8.108 -21.094 32.309 1.00 16.34 C
ANISOU 2946 CE2 PHE A 366 1954 2379 1876 324 -136 6 C
ATOM 2947 C PHE A 366 13.780 -23.317 30.919 1.00 16.14 C
ANISOU 2947 C PHE A 366 1948 2304 1879 464 -211 -142 C
ATOM 2948 O PHE A 366 13.947 -22.738 29.847 1.00 17.48 O
ANISOU 2948 O PHE A 366 2330 2433 1878 355 -159 -20 O
ATOM 2949 N ARG A 367 14.798 -23.844 31.606 1.00 17.67 N
ANISOU 2949 N ARG A 367 1935 2880 1895 511 -212 -80 N
ATOM 2950 CA ARG A 367 16.183 -23.697 31.133 1.00 20.14 C
ANISOU 2950 CA ARG A 367 1981 3358 2312 415 -115 -43 C
ATOM 2951 CB ARG A 367 17.174 -24.277 32.155 1.00 23.41 C
ANISOU 2951 CB ARG A 367 2005 4098 2789 717 -339 -184 C
ATOM 2952 CG ARG A 367 17.153 -25.786 32.279 1.00 29.75 C
ANISOU 2952 CG ARG A 367 3021 4425 3858 858 -979 -329 C
ATOM 2953 CD ARG A 367 17.753 -26.322 33.578 1.00 36.84 C
ANISOU 2953 CD ARG A 367 4435 5447 4116 1038 -1550 -473 C
ATOM 2954 NE ARG A 367 19.191 -26.473 33.484 1.00 42.79 N
ANISOU 2954 NE ARG A 367 4836 6443 4979 1776 -1306 -729 N
ATOM 2955 CZ ARG A 367 19.816 -27.609 33.156 1.00 52.03 C
ANISOU 2955 CZ ARG A 367 6478 6074 7217 1582 -1441 -1292 C
ATOM 2956 NH1 ARG A 367 19.162 -28.578 32.536 1.00 61.13 N
ANISOU 2956 NH1 ARG A 367 8474 6787 7963 544 -1749 -1643 N
ATOM 2957 NH2 ARG A 367 21.090 -27.783 33.465 1.00 57.78 N
ANISOU 2957 NH2 ARG A 367 6282 7503 8169 2274 -791 -1103 N
ATOM 2958 C ARG A 367 16.374 -24.310 29.729 1.00 19.46 C
ANISOU 2958 C ARG A 367 1912 3281 2200 449 131 128 C
ATOM 2959 O ARG A 367 17.254 -23.877 29.004 1.00 21.49 O
ANISOU 2959 O ARG A 367 2402 3418 2344 287 514 -49 O
ATOM 2960 N GLU A 368 15.533 -25.268 29.317 1.00 17.92 N
ANISOU 2960 N GLU A 368 1880 2832 2096 710 61 252 N
ATOM 2961 CA GLU A 368 15.702 -25.920 28.033 1.00 21.26 C
ANISOU 2961 CA GLU A 368 2636 3254 2185 775 -175 128 C
ATOM 2962 CB GLU A 368 15.264 -27.383 28.107 1.00 22.66 C
ANISOU 2962 CB GLU A 368 3078 3426 2103 679 -139 144 C
ATOM 2963 CG GLU A 368 16.099 -28.214 29.074 1.00 27.64 C
ANISOU 2963 CG GLU A 368 3925 3992 2585 1155 -315 322 C
ATOM 2964 CD GLU A 368 17.612 -28.251 28.874 1.00 33.29 C
ANISOU 2964 CD GLU A 368 3938 5317 3392 1543 -340 456 C
ATOM 2965 OE1 GLU A 368 18.083 -28.123 27.721 1.00 35.94 O
ANISOU 2965 OE1 GLU A 368 3639 5782 4232 1785 230 893 O
ATOM 2966 OE2 GLU A 368 18.328 -28.422 29.884 1.00 39.71 O
ANISOU 2966 OE2 GLU A 368 4232 6818 4034 1440 -963 -3 O
ATOM 2967 C GLU A 368 14.951 -25.192 26.907 1.00 18.02 C
ANISOU 2967 C GLU A 368 2626 2378 1840 648 -36 -97 C
ATOM 2968 O GLU A 368 14.985 -25.647 25.748 1.00 20.93 O
ANISOU 2968 O GLU A 368 3309 2900 1741 1156 -3 -129 O
ATOM 2969 N LEU A 369 14.293 -24.062 27.208 1.00 15.86 N
ANISOU 2969 N LEU A 369 2001 2317 1707 475 -105 -159 N
ATOM 2970 CA LEU A 369 13.570 -23.325 26.164 1.00 15.01 C
ANISOU 2970 CA LEU A 369 1915 1890 1896 265 -190 -188 C
ATOM 2971 CB LEU A 369 12.361 -22.621 26.777 1.00 15.07 C
ANISOU 2971 CB LEU A 369 2014 1894 1816 261 16 -48 C
ATOM 2972 CG LEU A 369 11.303 -23.520 27.414 1.00 14.82 C
ANISOU 2972 CG LEU A 369 1949 1887 1793 149 -124 11 C
ATOM 2973 CD1 LEU A 369 10.091 -22.705 27.848 1.00 15.81 C
ANISOU 2973 CD1 LEU A 369 2071 1927 2008 308 -229 181 C
ATOM 2974 CD2 LEU A 369 10.906 -24.681 26.497 1.00 15.88 C
ANISOU 2974 CD2 LEU A 369 2137 2083 1813 202 -159 -62 C
ATOM 2975 C LEU A 369 14.477 -22.293 25.505 1.00 15.14 C
ANISOU 2975 C LEU A 369 1745 2034 1970 341 -24 -216 C
ATOM 2976 O LEU A 369 15.234 -21.585 26.171 1.00 17.79 O
ANISOU 2976 O LEU A 369 2323 2463 1971 -6 -123 -350 O
ATOM 2977 N GLU A 370 14.361 -22.193 24.182 1.00 14.59 N
ANISOU 2977 N GLU A 370 1676 1826 2040 215 -189 -154 N
ATOM 2978 CA GLU A 370 15.003 -21.124 23.431 1.00 15.49 C
ANISOU 2978 CA GLU A 370 1763 1931 2190 284 -7 41 C
ATOM 2979 CB GLU A 370 15.824 -21.657 22.262 1.00 15.89 C
ANISOU 2979 CB GLU A 370 1651 2134 2251 438 -141 7 C
ATOM 2980 CG GLU A 370 15.338 -22.930 21.593 1.00 18.30 C
ANISOU 2980 CG GLU A 370 2288 2318 2345 388 66 -158 C
ATOM 2981 CD GLU A 370 14.045 -22.865 20.808 1.00 18.36 C
ANISOU 2981 CD GLU A 370 2412 2323 2241 469 103 -93 C
ATOM 2982 OE1 GLU A 370 13.327 -21.839 20.940 1.00 17.10 O
ANISOU 2982 OE1 GLU A 370 2338 1931 2226 204 59 -137 O
ATOM 2983 OE2 GLU A 370 13.751 -23.874 20.068 1.00 20.48 O
ANISOU 2983 OE2 GLU A 370 2306 2685 2789 387 181 -577 O
ATOM 2984 C GLU A 370 13.936 -20.080 23.054 1.00 13.95 C
ANISOU 2984 C GLU A 370 1751 1614 1932 162 -28 33 C
ATOM 2985 O GLU A 370 12.756 -20.154 23.466 1.00 14.71 O
ANISOU 2985 O GLU A 370 1600 1888 2101 416 -38 6 O
ATOM 2986 N GLN A 371 14.364 -19.052 22.322 1.00 15.44 N
ANISOU 2986 N GLN A 371 1983 1825 2059 368 221 288 N
ATOM 2987 CA GLN A 371 13.533 -17.849 22.179 1.00 14.36 C
ANISOU 2987 CA GLN A 371 1837 1685 1934 301 60 97 C
ATOM 2988 CB GLN A 371 14.316 -16.748 21.456 1.00 16.28 C
ANISOU 2988 CB GLN A 371 2260 1919 2005 214 107 154 C
ATOM 2989 CG GLN A 371 13.600 -15.405 21.520 1.00 15.77 C
ANISOU 2989 CG GLN A 371 2237 1713 2042 16 -194 12 C
ATOM 2990 CD GLN A 371 14.428 -14.266 20.987 1.00 15.01 C
ANISOU 2990 CD GLN A 371 2213 1482 2008 220 -136 129 C
ATOM 2991 OE1 GLN A 371 15.017 -14.348 19.900 1.00 16.29 O
ANISOU 2991 OE1 GLN A 371 2266 1860 2062 141 -65 -17 O
ATOM 2992 NE2 GLN A 371 14.460 -13.194 21.766 1.00 14.50 N
ANISOU 2992 NE2 GLN A 371 1893 1897 1716 178 -468 -118 N
ATOM 2993 C GLN A 371 12.201 -18.162 21.481 1.00 13.78 C
ANISOU 2993 C GLN A 371 1742 1420 2070 316 181 92 C
ATOM 2994 O GLN A 371 11.149 -17.627 21.851 1.00 14.99 O
ANISOU 2994 O GLN A 371 1677 1702 2313 446 220 170 O
ATOM 2995 N GLN A 372 12.220 -19.007 20.453 1.00 14.29 N
ANISOU 2995 N GLN A 372 1787 1583 2059 400 161 95 N
ATOM 2996 CA GLN A 372 10.995 -19.361 19.743 1.00 15.08 C
ANISOU 2996 CA GLN A 372 1914 1960 1855 237 203 223 C
ATOM 2997 CB GLN A 372 11.304 -20.260 18.558 1.00 16.50 C
ANISOU 2997 CB GLN A 372 2351 1994 1921 379 189 111 C
ATOM 2998 CG GLN A 372 10.078 -20.601 17.748 1.00 20.06 C
ANISOU 2998 CG GLN A 372 2964 2480 2177 -191 158 -662 C
ATOM 2999 CD GLN A 372 9.549 -19.394 17.002 1.00 22.13 C
ANISOU 2999 CD GLN A 372 2649 3145 2612 185 -380 -695 C
ATOM 3000 OE1 GLN A 372 10.303 -18.598 16.427 1.00 27.71 O
ANISOU 3000 OE1 GLN A 372 4222 3340 2966 -287 -288 -240 O
ATOM 3001 NE2 GLN A 372 8.243 -19.233 16.999 1.00 27.58 N
ANISOU 3001 NE2 GLN A 372 2638 5069 2773 930 -534 -1575 N
ATOM 3002 C GLN A 372 10.010 -20.059 20.687 1.00 13.56 C
ANISOU 3002 C GLN A 372 1692 1710 1749 188 37 156 C
ATOM 3003 O GLN A 372 8.799 -19.810 20.629 1.00 14.62 O
ANISOU 3003 O GLN A 372 1770 1816 1969 293 139 305 O
ATOM 3004 N GLN A 373 10.518 -20.946 21.542 1.00 13.52 N
ANISOU 3004 N GLN A 373 1663 1721 1752 336 72 66 N
ATOM 3005 CA GLN A 373 9.661 -21.635 22.476 1.00 13.77 C
ANISOU 3005 CA GLN A 373 1827 1593 1809 362 46 178 C
ATOM 3006 CB GLN A 373 10.421 -22.787 23.120 1.00 13.86 C
ANISOU 3006 CB GLN A 373 1661 1598 2006 405 37 161 C
ATOM 3007 CG GLN A 373 10.714 -23.930 22.153 1.00 14.42 C
ANISOU 3007 CG GLN A 373 1815 1830 1835 247 19 51 C
ATOM 3008 CD GLN A 373 11.741 -24.878 22.722 1.00 15.40 C
ANISOU 3008 CD GLN A 373 2229 1570 2050 459 186 23 C
ATOM 3009 OE1 GLN A 373 12.824 -24.446 23.111 1.00 17.45 O
ANISOU 3009 OE1 GLN A 373 2217 1921 2491 310 154 -118 O
ATOM 3010 NE2 GLN A 373 11.401 -26.165 22.794 1.00 15.62 N
ANISOU 3010 NE2 GLN A 373 2256 1584 2095 261 495 -52 N
ATOM 3011 C GLN A 373 9.112 -20.674 23.533 1.00 12.74 C
ANISOU 3011 C GLN A 373 1547 1543 1750 426 -73 215 C
ATOM 3012 O GLN A 373 7.957 -20.828 23.965 1.00 13.34 O
ANISOU 3012 O GLN A 373 1717 1581 1770 426 178 142 O
ATOM 3013 N LEU A 374 9.912 -19.685 23.948 1.00 13.19 N
ANISOU 3013 N LEU A 374 1624 1601 1786 333 16 126 N
ATOM 3014 CA LEU A 374 9.411 -18.669 24.889 1.00 12.81 C
ANISOU 3014 CA LEU A 374 1765 1442 1659 329 -44 149 C
ATOM 3015 CB LEU A 374 10.558 -17.769 25.372 1.00 13.46 C
ANISOU 3015 CB LEU A 374 1775 1556 1782 390 -111 -10 C
ATOM 3016 CG LEU A 374 11.617 -18.459 26.225 1.00 14.51 C
ANISOU 3016 CG LEU A 374 1942 1693 1876 415 -279 -4 C
ATOM 3017 CD1 LEU A 374 12.796 -17.548 26.463 1.00 15.98 C
ANISOU 3017 CD1 LEU A 374 1988 2119 1965 258 -213 167 C
ATOM 3018 CD2 LEU A 374 11.023 -18.944 27.543 1.00 15.31 C
ANISOU 3018 CD2 LEU A 374 2160 1703 1953 343 -326 4 C
ATOM 3019 C LEU A 374 8.306 -17.820 24.249 1.00 12.16 C
ANISOU 3019 C LEU A 374 1553 1487 1577 192 -33 49 C
ATOM 3020 O LEU A 374 7.334 -17.431 24.908 1.00 12.34 O
ANISOU 3020 O LEU A 374 1762 1438 1488 35 182 -50 O
ATOM 3021 N TYR A 375 8.441 -17.551 22.953 1.00 12.52 N
ANISOU 3021 N TYR A 375 1653 1565 1536 232 82 83 N
ATOM 3022 CA TYR A 375 7.382 -16.870 22.205 1.00 12.21 C
ANISOU 3022 CA TYR A 375 1589 1575 1472 281 185 104 C
ATOM 3023 CB TYR A 375 7.856 -16.573 20.785 1.00 11.10 C
ANISOU 3023 CB TYR A 375 1463 1323 1430 248 185 -35 C
ATOM 3024 CG TYR A 375 6.796 -16.027 19.861 1.00 11.05 C
ANISOU 3024 CG TYR A 375 1553 1267 1375 133 110 68 C
ATOM 3025 CD1 TYR A 375 6.310 -14.738 20.026 1.00 12.21 C
ANISOU 3025 CD1 TYR A 375 1846 1272 1519 187 -41 88 C
ATOM 3026 CE1 TYR A 375 5.396 -14.195 19.146 1.00 13.27 C
ANISOU 3026 CE1 TYR A 375 1804 1667 1570 393 35 -11 C
ATOM 3027 CZ TYR A 375 4.909 -14.949 18.104 1.00 12.53 C
ANISOU 3027 CZ TYR A 375 1600 1858 1302 216 1 153 C
ATOM 3028 OH TYR A 375 4.009 -14.387 17.240 1.00 14.39 O
ANISOU 3028 OH TYR A 375 1709 2254 1504 330 -110 207 O
ATOM 3029 CE2 TYR A 375 5.370 -16.242 17.934 1.00 13.57 C
ANISOU 3029 CE2 TYR A 375 1873 1843 1438 147 -260 -161 C
ATOM 3030 CD2 TYR A 375 6.301 -16.770 18.812 1.00 12.63 C
ANISOU 3030 CD2 TYR A 375 1798 1442 1556 179 4 14 C
ATOM 3031 C TYR A 375 6.105 -17.721 22.173 1.00 11.71 C
ANISOU 3031 C TYR A 375 1496 1575 1376 339 49 18 C
ATOM 3032 O TYR A 375 5.004 -17.208 22.380 1.00 11.21 O
ANISOU 3032 O TYR A 375 1378 1490 1390 174 270 -115 O
ATOM 3033 N GLU A 376 6.261 -19.028 21.927 1.00 11.99 N
ANISOU 3033 N GLU A 376 1494 1503 1557 340 10 113 N
ATOM 3034 CA GLU A 376 5.091 -19.944 21.912 1.00 12.29 C
ANISOU 3034 CA GLU A 376 1761 1490 1418 213 -28 33 C
ATOM 3035 CB GLU A 376 5.548 -21.334 21.459 1.00 14.74 C
ANISOU 3035 CB GLU A 376 2088 1637 1874 357 73 -47 C
ATOM 3036 CG GLU A 376 5.945 -21.363 20.002 1.00 15.19 C
ANISOU 3036 CG GLU A 376 1866 1936 1970 268 149 -152 C
ATOM 3037 CD GLU A 376 6.633 -22.612 19.516 1.00 17.64 C
ANISOU 3037 CD GLU A 376 1952 2322 2425 547 188 -278 C
ATOM 3038 OE1 GLU A 376 6.848 -23.521 20.324 1.00 21.30 O
ANISOU 3038 OE1 GLU A 376 3112 2164 2814 662 470 -268 O
ATOM 3039 OE2 GLU A 376 6.980 -22.647 18.307 1.00 24.30 O
ANISOU 3039 OE2 GLU A 376 3094 3444 2693 1462 353 -665 O
ATOM 3040 C GLU A 376 4.433 -19.985 23.298 1.00 12.50 C
ANISOU 3040 C GLU A 376 1712 1516 1522 236 2 -8 C
ATOM 3041 O GLU A 376 3.205 -19.931 23.391 1.00 12.64 O
ANISOU 3041 O GLU A 376 1769 1399 1633 242 222 52 O
ATOM 3042 N LEU A 377 5.259 -20.045 24.363 1.00 11.24 N
ANISOU 3042 N LEU A 377 1564 1259 1444 137 56 24 N
ATOM 3043 CA LEU A 377 4.737 -20.014 25.722 1.00 11.62 C
ANISOU 3043 CA LEU A 377 1778 1253 1382 193 34 28 C
ATOM 3044 CB LEU A 377 5.912 -20.057 26.712 1.00 12.25 C
ANISOU 3044 CB LEU A 377 1848 1284 1521 249 15 43 C
ATOM 3045 CG LEU A 377 5.588 -19.740 28.174 1.00 12.64 C
ANISOU 3045 CG LEU A 377 1933 1310 1557 283 205 88 C
ATOM 3046 CD1 LEU A 377 4.581 -20.723 28.764 1.00 12.72 C
ANISOU 3046 CD1 LEU A 377 1951 1370 1511 216 158 -38 C
ATOM 3047 CD2 LEU A 377 6.865 -19.752 29.005 1.00 14.01 C
ANISOU 3047 CD2 LEU A 377 2095 1508 1718 311 80 68 C
ATOM 3048 C LEU A 377 3.904 -18.740 25.925 1.00 11.83 C
ANISOU 3048 C LEU A 377 1794 1236 1463 180 67 19 C
ATOM 3049 O LEU A 377 2.769 -18.767 26.417 1.00 12.27 O
ANISOU 3049 O LEU A 377 1808 1316 1536 216 14 -30 O
ATOM 3050 N SER A 378 4.502 -17.588 25.606 1.00 11.08 N
ANISOU 3050 N SER A 378 1430 1301 1477 162 189 -103 N
ATOM 3051 CA SER A 378 3.800 -16.336 25.858 1.00 10.60 C
ANISOU 3051 CA SER A 378 1388 1283 1355 201 143 -44 C
ATOM 3052 CB SER A 378 4.695 -15.155 25.585 1.00 11.76 C
ANISOU 3052 CB SER A 378 1654 1169 1642 205 85 24 C
ATOM 3053 OG SER A 378 4.204 -13.992 26.211 1.00 11.18 O
ANISOU 3053 OG SER A 378 1543 1373 1328 320 -68 -97 O
ATOM 3054 C SER A 378 2.496 -16.277 25.028 1.00 11.06 C
ANISOU 3054 C SER A 378 1506 1268 1429 76 70 61 C
ATOM 3055 O SER A 378 1.452 -15.830 25.521 1.00 11.21 O
ANISOU 3055 O SER A 378 1551 1315 1393 224 -163 -70 O
ATOM 3056 N SER A 379 2.570 -16.716 23.769 1.00 11.25 N
ANISOU 3056 N SER A 379 1396 1426 1452 132 148 -45 N
ATOM 3057 CA SER A 379 1.432 -16.732 22.859 1.00 11.13 C
ANISOU 3057 CA SER A 379 1461 1347 1419 148 141 61 C
ATOM 3058 CB SER A 379 1.880 -17.109 21.463 1.00 12.23 C
ANISOU 3058 CB SER A 379 1604 1678 1365 190 175 188 C
ATOM 3059 OG SER A 379 2.761 -16.125 20.940 1.00 12.80 O
ANISOU 3059 OG SER A 379 1656 1737 1470 106 158 171 O
ATOM 3060 C SER A 379 0.309 -17.642 23.369 1.00 11.03 C
ANISOU 3060 C SER A 379 1535 1385 1268 95 15 74 C
ATOM 3061 O SER A 379 -0.885 -17.333 23.199 1.00 12.21 O
ANISOU 3061 O SER A 379 1547 1512 1580 107 77 6 O
ATOM 3062 N SER A 380 0.681 -18.737 24.025 1.00 10.61 N
ANISOU 3062 N SER A 380 1346 1303 1382 167 -33 -12 N
ATOM 3063 CA SER A 380 -0.324 -19.670 24.583 1.00 11.39 C
ANISOU 3063 CA SER A 380 1619 1343 1366 88 63 118 C
ATOM 3064 CB SER A 380 0.330 -20.945 25.077 1.00 13.28 C
ANISOU 3064 CB SER A 380 1861 1576 1609 190 -125 229 C
ATOM 3065 OG SER A 380 0.989 -20.763 26.324 1.00 13.29 O
ANISOU 3065 OG SER A 380 1855 1686 1506 315 -131 224 O
ATOM 3066 C SER A 380 -1.158 -18.999 25.677 1.00 11.43 C
ANISOU 3066 C SER A 380 1543 1398 1401 151 -3 138 C
ATOM 3067 O SER A 380 -2.210 -19.491 26.010 1.00 13.79 O
ANISOU 3067 O SER A 380 1719 1623 1897 -65 270 -240 O
ATOM 3068 N ASN A 381 -0.608 -17.911 26.236 1.00 11.03 N
ANISOU 3068 N ASN A 381 1597 1313 1280 165 159 52 N
ATOM 3069 CA ASN A 381 -1.220 -17.129 27.295 1.00 11.60 C
ANISOU 3069 CA ASN A 381 1700 1604 1102 198 86 12 C
ATOM 3070 CB ASN A 381 -0.276 -17.033 28.492 1.00 11.64 C
ANISOU 3070 CB ASN A 381 1834 1554 1032 72 65 -16 C
ATOM 3071 CG ASN A 381 -0.058 -18.386 29.144 1.00 12.42 C
ANISOU 3071 CG ASN A 381 1853 1532 1333 4 -51 47 C
ATOM 3072 OD1 ASN A 381 -1.042 -19.084 29.436 1.00 13.36 O
ANISOU 3072 OD1 ASN A 381 1783 1773 1518 151 167 172 O
ATOM 3073 ND2 ASN A 381 1.191 -18.777 29.333 1.00 14.54 N
ANISOU 3073 ND2 ASN A 381 1763 2075 1685 22 12 -35 N
ATOM 3074 C ASN A 381 -1.658 -15.748 26.792 1.00 12.14 C
ANISOU 3074 C ASN A 381 1729 1589 1294 241 2 -96 C
ATOM 3075 O ASN A 381 -1.889 -14.840 27.594 1.00 14.14 O
ANISOU 3075 O ASN A 381 2224 1623 1523 368 -114 -269 O
ATOM 3076 N GLY A 382 -1.810 -15.614 25.478 1.00 10.95 N
ANISOU 3076 N GLY A 382 1745 1175 1238 192 142 -32 N
ATOM 3077 CA GLY A 382 -2.478 -14.467 24.881 1.00 12.22 C
ANISOU 3077 CA GLY A 382 1681 1454 1505 197 -30 142 C
ATOM 3078 C GLY A 382 -1.551 -13.503 24.157 1.00 12.01 C
ANISOU 3078 C GLY A 382 1624 1482 1458 135 -15 57 C
ATOM 3079 O GLY A 382 -2.076 -12.592 23.520 1.00 12.22 O
ANISOU 3079 O GLY A 382 1517 1282 1844 271 -26 -24 O
ATOM 3080 N TYR A 383 -0.215 -13.661 24.253 1.00 11.15 N
ANISOU 3080 N TYR A 383 1621 1210 1404 121 61 171 N
ATOM 3081 CA TYR A 383 0.683 -12.691 23.610 1.00 10.73 C
ANISOU 3081 CA TYR A 383 1429 1207 1439 118 1 128 C
ATOM 3082 CB TYR A 383 2.146 -13.143 23.682 1.00 10.99 C
ANISOU 3082 CB TYR A 383 1473 1215 1487 153 98 103 C
ATOM 3083 CG TYR A 383 3.105 -12.096 23.178 1.00 10.87 C
ANISOU 3083 CG TYR A 383 1533 1184 1411 101 20 137 C
ATOM 3084 CD1 TYR A 383 3.540 -11.053 23.985 1.00 11.41 C
ANISOU 3084 CD1 TYR A 383 1708 1477 1148 93 -56 100 C
ATOM 3085 CE1 TYR A 383 4.380 -10.062 23.490 1.00 11.37 C
ANISOU 3085 CE1 TYR A 383 1741 1347 1230 62 -39 -78 C
ATOM 3086 CZ TYR A 383 4.875 -10.156 22.196 1.00 10.87 C
ANISOU 3086 CZ TYR A 383 1765 1122 1240 89 53 129 C
ATOM 3087 OH TYR A 383 5.723 -9.215 21.691 1.00 11.85 O
ANISOU 3087 OH TYR A 383 1727 1398 1377 54 160 213 O
ATOM 3088 CE2 TYR A 383 4.449 -11.194 21.386 1.00 11.31 C
ANISOU 3088 CE2 TYR A 383 1682 1373 1241 138 -27 20 C
ATOM 3089 CD2 TYR A 383 3.602 -12.169 21.892 1.00 11.53 C
ANISOU 3089 CD2 TYR A 383 1677 1285 1418 32 -33 -105 C
ATOM 3090 C TYR A 383 0.268 -12.541 22.142 1.00 10.52 C
ANISOU 3090 C TYR A 383 1379 1202 1414 78 -3 105 C
ATOM 3091 O TYR A 383 0.129 -13.529 21.427 1.00 12.47 O
ANISOU 3091 O TYR A 383 1761 1520 1455 41 10 -21 O
ATOM 3092 N ASN A 384 0.146 -11.292 21.682 1.00 10.90 N
ANISOU 3092 N ASN A 384 1497 1169 1475 66 28 81 N
ATOM 3093 CA ASN A 384 -0.635 -10.973 20.489 1.00 12.10 C
ANISOU 3093 CA ASN A 384 1551 1483 1562 68 -7 106 C
ATOM 3094 CB ASN A 384 -1.879 -10.146 20.856 1.00 12.66 C
ANISOU 3094 CB ASN A 384 1637 1620 1554 216 -70 106 C
ATOM 3095 CG ASN A 384 -1.564 -8.809 21.483 1.00 12.93 C
ANISOU 3095 CG ASN A 384 1598 1748 1567 346 134 63 C
ATOM 3096 OD1 ASN A 384 -0.443 -8.299 21.330 1.00 14.94 O
ANISOU 3096 OD1 ASN A 384 1616 2053 2005 292 321 -29 O
ATOM 3097 ND2 ASN A 384 -2.554 -8.252 22.194 1.00 14.36 N
ANISOU 3097 ND2 ASN A 384 1732 2033 1689 426 393 176 N
ATOM 3098 C ASN A 384 0.173 -10.265 19.390 1.00 12.04 C
ANISOU 3098 C ASN A 384 1612 1530 1432 171 3 74 C
ATOM 3099 O ASN A 384 -0.455 -9.781 18.431 1.00 14.96 O
ANISOU 3099 O ASN A 384 1821 2095 1766 176 -259 322 O
ATOM 3100 N LYS A 385 1.508 -10.299 19.454 1.00 10.91 N
ANISOU 3100 N LYS A 385 1597 1253 1292 145 -7 -42 N
ATOM 3101 CA LYS A 385 2.343 -9.666 18.437 1.00 10.45 C
ANISOU 3101 CA LYS A 385 1458 1237 1276 178 -53 -17 C
ATOM 3102 CB LYS A 385 3.196 -8.550 19.044 1.00 11.80 C
ANISOU 3102 CB LYS A 385 1608 1257 1615 58 132 -88 C
ATOM 3103 CG LYS A 385 2.407 -7.432 19.706 1.00 12.37 C
ANISOU 3103 CG LYS A 385 1657 1359 1683 121 232 -62 C
ATOM 3104 CD LYS A 385 1.398 -6.754 18.806 1.00 12.44 C
ANISOU 3104 CD LYS A 385 1720 1314 1691 117 230 -32 C
ATOM 3105 CE LYS A 385 2.048 -6.021 17.658 1.00 12.71 C
ANISOU 3105 CE LYS A 385 1912 1410 1504 161 189 -11 C
ATOM 3106 NZ LYS A 385 1.075 -5.561 16.637 1.00 13.73 N
ANISOU 3106 NZ LYS A 385 1959 1474 1783 280 94 -66 N
ATOM 3107 C LYS A 385 3.233 -10.693 17.732 1.00 10.12 C
ANISOU 3107 C LYS A 385 1364 1220 1258 113 -9 15 C
ATOM 3108 O LYS A 385 3.474 -11.807 18.213 1.00 11.70 O
ANISOU 3108 O LYS A 385 1715 1262 1466 251 -62 10 O
ATOM 3109 N ARG A 386 3.759 -10.266 16.581 1.00 10.92 N
ANISOU 3109 N ARG A 386 1749 1050 1350 136 171 -47 N
ATOM 3110 CA ARG A 386 4.604 -11.109 15.738 1.00 10.47 C
ANISOU 3110 CA ARG A 386 1456 1122 1400 140 82 -74 C
ATOM 3111 CB ARG A 386 4.869 -10.414 14.398 1.00 10.24 C
ANISOU 3111 CB ARG A 386 1415 1184 1290 213 33 -78 C
ATOM 3112 CG ARG A 386 5.719 -9.151 14.528 1.00 11.30 C
ANISOU 3112 CG ARG A 386 1607 1351 1332 81 -171 45 C
ATOM 3113 CD ARG A 386 5.851 -8.289 13.298 1.00 10.61 C
ANISOU 3113 CD ARG A 386 1493 1257 1278 65 20 -28 C
ATOM 3114 NE ARG A 386 4.568 -7.705 12.914 1.00 11.04 N
ANISOU 3114 NE ARG A 386 1476 1404 1312 31 -2 64 N
ATOM 3115 CZ ARG A 386 4.411 -6.857 11.898 1.00 10.35 C
ANISOU 3115 CZ ARG A 386 1335 1354 1243 9 63 14 C
ATOM 3116 NH1 ARG A 386 5.472 -6.530 11.153 1.00 10.87 N
ANISOU 3116 NH1 ARG A 386 1389 1390 1351 68 237 -63 N
ATOM 3117 NH2 ARG A 386 3.204 -6.349 11.648 1.00 11.68 N
ANISOU 3117 NH2 ARG A 386 1590 1599 1245 291 -35 -36 N
ATOM 3118 C ARG A 386 5.937 -11.438 16.437 1.00 10.02 C
ANISOU 3118 C ARG A 386 1486 1005 1316 178 57 46 C
ATOM 3119 O ARG A 386 6.440 -10.723 17.327 1.00 10.95 O
ANISOU 3119 O ARG A 386 1599 1211 1348 135 51 42 O
ATOM 3120 N PHE A 387 6.568 -12.505 15.956 1.00 10.01 N
ANISOU 3120 N PHE A 387 1494 1060 1248 192 -130 -151 N
ATOM 3121 CA PHE A 387 7.825 -12.975 16.540 1.00 10.56 C
ANISOU 3121 CA PHE A 387 1401 1201 1410 214 -77 -129 C
ATOM 3122 CB PHE A 387 8.243 -14.310 15.921 1.00 10.64 C
ANISOU 3122 CB PHE A 387 1429 1198 1413 196 -4 -156 C
ATOM 3123 CG PHE A 387 9.518 -14.863 16.506 1.00 11.00 C
ANISOU 3123 CG PHE A 387 1385 1250 1545 195 28 -168 C
ATOM 3124 CD1 PHE A 387 9.599 -15.188 17.854 1.00 11.78 C
ANISOU 3124 CD1 PHE A 387 1538 1290 1648 211 -13 48 C
ATOM 3125 CE1 PHE A 387 10.769 -15.685 18.390 1.00 12.83 C
ANISOU 3125 CE1 PHE A 387 1625 1584 1663 309 -34 -58 C
ATOM 3126 CZ PHE A 387 11.855 -15.900 17.596 1.00 14.24 C
ANISOU 3126 CZ PHE A 387 1689 1731 1991 384 101 -56 C
ATOM 3127 CD2 PHE A 387 10.628 -15.068 15.713 1.00 13.03 C
ANISOU 3127 CD2 PHE A 387 1535 1672 1743 342 122 -81 C
ATOM 3128 CE2 PHE A 387 11.800 -15.570 16.258 1.00 13.99 C
ANISOU 3128 CE2 PHE A 387 1517 1958 1838 442 40 -90 C
ATOM 3129 C PHE A 387 8.961 -11.942 16.422 1.00 10.25 C
ANISOU 3129 C PHE A 387 1382 1215 1296 241 -43 -106 C
ATOM 3130 O PHE A 387 9.728 -11.806 17.353 1.00 11.96 O
ANISOU 3130 O PHE A 387 1615 1446 1481 184 -216 -206 O
ATOM 3131 N SER A 388 9.040 -11.207 15.308 1.00 10.88 N
ANISOU 3131 N SER A 388 1475 1437 1219 109 -118 -45 N
ATOM 3132 CA SER A 388 10.115 -10.215 15.119 1.00 11.26 C
ANISOU 3132 CA SER A 388 1425 1383 1470 217 -78 -118 C
ATOM 3133 CB SER A 388 10.167 -9.715 13.709 1.00 11.34 C
ANISOU 3133 CB SER A 388 1463 1403 1439 53 -11 -77 C
ATOM 3134 OG SER A 388 8.926 -9.122 13.339 1.00 12.06 O
ANISOU 3134 OG SER A 388 1398 1697 1485 166 26 29 O
ATOM 3135 C SER A 388 10.004 -9.037 16.088 1.00 12.26 C
ANISOU 3135 C SER A 388 1648 1436 1572 156 -97 -166 C
ATOM 3136 O SER A 388 10.985 -8.335 16.276 1.00 13.57 O
ANISOU 3136 O SER A 388 1794 1595 1764 -59 142 -285 O
ATOM 3137 N CYS A 389 8.816 -8.806 16.660 1.00 11.91 N
ANISOU 3137 N CYS A 389 1618 1400 1505 78 -88 -107 N
ATOM 3138 CA CYS A 389 8.663 -7.844 17.745 1.00 11.45 C
ANISOU 3138 CA CYS A 389 1680 1220 1449 44 -143 -7 C
ATOM 3139 CB CYS A 389 7.183 -7.484 17.873 1.00 11.77 C
ANISOU 3139 CB CYS A 389 1756 1245 1468 80 -81 2 C
ATOM 3140 SG CYS A 389 6.757 -6.539 19.358 1.00 13.57 S
ANISOU 3140 SG CYS A 389 2056 1569 1529 140 102 -62 S
ATOM 3141 C CYS A 389 9.239 -8.441 19.031 1.00 12.39 C
ANISOU 3141 C CYS A 389 1730 1541 1436 -18 -120 -27 C
ATOM 3142 O CYS A 389 10.206 -7.927 19.619 1.00 12.56 O
ANISOU 3142 O CYS A 389 1891 1308 1570 78 -190 -152 O
ATOM 3143 N PHE A 390 8.637 -9.562 19.431 1.00 11.09 N
ANISOU 3143 N PHE A 390 1551 1406 1254 -109 -235 -94 N
ATOM 3144 CA PHE A 390 9.019 -10.296 20.632 1.00 11.83 C
ANISOU 3144 CA PHE A 390 1582 1565 1346 -10 -142 -34 C
ATOM 3145 CB PHE A 390 8.286 -11.638 20.674 1.00 11.16 C
ANISOU 3145 CB PHE A 390 1431 1439 1369 50 -67 -110 C
ATOM 3146 CG PHE A 390 8.617 -12.500 21.861 1.00 11.69 C
ANISOU 3146 CG PHE A 390 1522 1695 1223 81 33 -88 C
ATOM 3147 CD2 PHE A 390 7.845 -12.457 23.017 1.00 10.75 C
ANISOU 3147 CD2 PHE A 390 1362 1448 1272 45 -23 -90 C
ATOM 3148 CE2 PHE A 390 8.148 -13.279 24.098 1.00 11.71 C
ANISOU 3148 CE2 PHE A 390 1590 1596 1260 66 -32 -31 C
ATOM 3149 CZ PHE A 390 9.242 -14.128 24.040 1.00 12.29 C
ANISOU 3149 CZ PHE A 390 1569 1749 1351 52 11 28 C
ATOM 3150 CD1 PHE A 390 9.678 -13.392 21.811 1.00 11.47 C
ANISOU 3150 CD1 PHE A 390 1564 1603 1191 95 191 -72 C
ATOM 3151 CE1 PHE A 390 9.997 -14.195 22.896 1.00 12.36 C
ANISOU 3151 CE1 PHE A 390 1599 1624 1470 154 10 -8 C
ATOM 3152 C PHE A 390 10.532 -10.504 20.719 1.00 11.71 C
ANISOU 3152 C PHE A 390 1537 1641 1271 -61 -107 -150 C
ATOM 3153 O PHE A 390 11.151 -10.373 21.792 1.00 12.92 O
ANISOU 3153 O PHE A 390 1702 1920 1287 -22 -201 -173 O
ATOM 3154 N SER A 391 11.147 -10.878 19.592 1.00 11.59 N
ANISOU 3154 N SER A 391 1534 1538 1328 65 -80 -67 N
ATOM 3155 CA SER A 391 12.518 -11.360 19.646 1.00 11.58 C
ANISOU 3155 CA SER A 391 1506 1632 1260 121 -128 -67 C
ATOM 3156 CB SER A 391 12.895 -12.083 18.385 1.00 12.33 C
ANISOU 3156 CB SER A 391 1647 1735 1302 130 -61 -95 C
ATOM 3157 OG SER A 391 13.020 -11.164 17.321 1.00 13.04 O
ANISOU 3157 OG SER A 391 1763 1637 1552 24 -161 102 O
ATOM 3158 C SER A 391 13.549 -10.262 19.944 1.00 12.24 C
ANISOU 3158 C SER A 391 1569 1628 1453 128 -171 -105 C
ATOM 3159 O SER A 391 14.669 -10.561 20.412 1.00 12.69 O
ANISOU 3159 O SER A 391 1560 1718 1542 64 -194 -28 O
ATOM 3160 N GLY A 392 13.229 -9.010 19.600 1.00 12.02 N
ANISOU 3160 N GLY A 392 1331 1522 1712 38 -42 -158 N
ATOM 3161 CA GLY A 392 14.214 -7.933 19.699 1.00 12.29 C
ANISOU 3161 CA GLY A 392 1267 1697 1703 -6 -186 -100 C
ATOM 3162 C GLY A 392 15.348 -8.087 18.689 1.00 12.51 C
ANISOU 3162 C GLY A 392 1436 1687 1627 46 -144 -193 C
ATOM 3163 O GLY A 392 16.388 -7.428 18.833 1.00 12.99 O
ANISOU 3163 O GLY A 392 1372 1751 1811 -2 -4 -76 O
ATOM 3164 N ALA A 393 15.170 -8.943 17.660 1.00 12.48 N
ANISOU 3164 N ALA A 393 1358 1672 1710 141 -252 -252 N
ATOM 3165 CA ALA A 393 16.209 -9.148 16.655 1.00 13.31 C
ANISOU 3165 CA ALA A 393 1724 1644 1689 18 -33 -247 C
ATOM 3166 CB ALA A 393 15.941 -10.403 15.852 1.00 12.96 C
ANISOU 3166 CB ALA A 393 1537 1623 1762 46 -87 -245 C
ATOM 3167 C ALA A 393 16.325 -7.925 15.731 1.00 12.66 C
ANISOU 3167 C ALA A 393 1446 1706 1658 -29 -24 -242 C
ATOM 3168 O ALA A 393 15.457 -7.054 15.684 1.00 12.06 O
ANISOU 3168 O ALA A 393 1406 1711 1466 -23 26 -116 O
ATOM 3169 N LEU A 394 17.431 -7.896 14.982 1.00 12.65 N
ANISOU 3169 N LEU A 394 1493 1688 1623 20 61 -97 N
ATOM 3170 CA LEU A 394 17.632 -6.897 13.937 1.00 12.90 C
ANISOU 3170 CA LEU A 394 1476 1663 1762 5 62 -54 C
ATOM 3171 CB LEU A 394 19.041 -7.038 13.369 1.00 13.88 C
ANISOU 3171 CB LEU A 394 1656 1928 1689 88 249 -188 C
ATOM 3172 CG LEU A 394 19.375 -6.153 12.172 1.00 15.22 C
ANISOU 3172 CG LEU A 394 1986 2098 1698 -133 109 -177 C
ATOM 3173 CD1 LEU A 394 19.406 -4.692 12.567 1.00 16.92 C
ANISOU 3173 CD1 LEU A 394 2086 2135 2205 -6 116 -109 C
ATOM 3174 CD2 LEU A 394 20.704 -6.618 11.556 1.00 16.13 C
ANISOU 3174 CD2 LEU A 394 2077 2183 1866 -2 162 -338 C
ATOM 3175 C LEU A 394 16.594 -7.129 12.840 1.00 12.21 C
ANISOU 3175 C LEU A 394 1445 1515 1679 -48 113 -53 C
ATOM 3176 O LEU A 394 16.582 -8.188 12.192 1.00 13.31 O
ANISOU 3176 O LEU A 394 1617 1593 1846 394 79 -187 O
ATOM 3177 N ALA A 395 15.770 -6.107 12.599 1.00 12.13 N
ANISOU 3177 N ALA A 395 1222 1610 1776 -38 -31 -140 N
ATOM 3178 CA ALA A 395 14.610 -6.214 11.720 1.00 12.19 C
ANISOU 3178 CA ALA A 395 1395 1634 1602 -85 -99 -160 C
ATOM 3179 CB ALA A 395 13.499 -5.362 12.261 1.00 11.82 C
ANISOU 3179 CB ALA A 395 1577 1374 1540 60 -156 -36 C
ATOM 3180 C ALA A 395 14.913 -5.799 10.271 1.00 12.84 C
ANISOU 3180 C ALA A 395 1633 1508 1735 -108 23 -55 C
ATOM 3181 O ALA A 395 14.182 -6.232 9.359 1.00 14.24 O
ANISOU 3181 O ALA A 395 1818 2018 1574 54 -111 -53 O
ATOM 3182 N ASN A 396 15.975 -5.013 10.043 1.00 12.88 N
ANISOU 3182 N ASN A 396 1694 1507 1692 -148 42 -87 N
ATOM 3183 CA ASN A 396 16.243 -4.448 8.723 1.00 13.51 C
ANISOU 3183 CA ASN A 396 1781 1586 1766 37 -57 78 C
ATOM 3184 CB ASN A 396 15.990 -2.940 8.710 1.00 13.73 C
ANISOU 3184 CB ASN A 396 1917 1499 1799 -60 15 210 C
ATOM 3185 CG ASN A 396 16.904 -2.134 9.606 1.00 13.21 C
ANISOU 3185 CG ASN A 396 1666 1614 1738 173 76 102 C
ATOM 3186 OD1 ASN A 396 17.446 -2.665 10.569 1.00 13.84 O
ANISOU 3186 OD1 ASN A 396 1579 1958 1720 -80 -68 73 O
ATOM 3187 ND2 ASN A 396 17.050 -0.845 9.309 1.00 16.15 N
ANISOU 3187 ND2 ASN A 396 2167 1703 2266 63 236 133 N
ATOM 3188 C ASN A 396 17.663 -4.806 8.274 1.00 14.46 C
ANISOU 3188 C ASN A 396 1827 1693 1971 34 -6 -14 C
ATOM 3189 O ASN A 396 18.492 -3.936 7.935 1.00 15.11 O
ANISOU 3189 O ASN A 396 2039 1734 1967 21 351 64 O
ATOM 3190 N GLY A 397 17.946 -6.109 8.242 1.00 14.69 N
ANISOU 3190 N GLY A 397 1666 1611 2304 -47 -32 -12 N
ATOM 3191 CA GLY A 397 19.299 -6.593 7.979 1.00 15.61 C
ANISOU 3191 CA GLY A 397 1812 1809 2308 145 95 -114 C
ATOM 3192 C GLY A 397 19.872 -6.186 6.638 1.00 15.99 C
ANISOU 3192 C GLY A 397 1900 2064 2109 235 55 -168 C
ATOM 3193 O GLY A 397 21.074 -6.053 6.539 1.00 17.11 O
ANISOU 3193 O GLY A 397 2108 2324 2069 -95 245 -181 O
ATOM 3194 N LEU A 398 19.052 -6.019 5.590 1.00 18.46 N
ANISOU 3194 N LEU A 398 1670 3026 2316 502 123 -87 N
ATOM 3195 CA LEU A 398 19.644 -5.594 4.313 1.00 21.70 C
ANISOU 3195 CA LEU A 398 2558 3461 2224 614 447 -137 C
ATOM 3196 CB LEU A 398 18.611 -5.455 3.209 1.00 25.22 C
ANISOU 3196 CB LEU A 398 2292 3994 3294 792 43 -108 C
ATOM 3197 CG LEU A 398 18.250 -6.702 2.455 1.00 26.33 C
ANISOU 3197 CG LEU A 398 1749 4386 3870 -62 -169 -180 C
ATOM 3198 CD1 LEU A 398 17.039 -6.380 1.583 1.00 26.13 C
ANISOU 3198 CD1 LEU A 398 2061 4165 3702 340 -247 -112 C
ATOM 3199 CD2 LEU A 398 19.431 -7.208 1.645 1.00 24.17 C
ANISOU 3199 CD2 LEU A 398 1813 3775 3594 -117 -435 -476 C
ATOM 3200 C LEU A 398 20.285 -4.220 4.427 1.00 24.27 C
ANISOU 3200 C LEU A 398 3481 3314 2425 843 735 12 C
ATOM 3201 O LEU A 398 21.303 -3.967 3.811 1.00 26.54 O
ANISOU 3201 O LEU A 398 4041 3548 2493 853 1262 201 O
ATOM 3202 N THR A 399 19.584 -3.313 5.111 1.00 28.83 N
ANISOU 3202 N THR A 399 4747 3332 2873 1303 1640 542 N
ATOM 3203 CA THR A 399 20.026 -1.958 5.245 1.00 32.69 C
ANISOU 3203 CA THR A 399 6034 3303 3081 1210 1786 915 C
ATOM 3204 CB THR A 399 18.985 -1.158 6.029 1.00 35.94 C
ANISOU 3204 CB THR A 399 6888 3064 3702 1884 1960 1049 C
ATOM 3205 OG1 THR A 399 17.775 -1.170 5.262 1.00 37.84 O
ANISOU 3205 OG1 THR A 399 6605 4038 3733 2574 2108 1731 O
ATOM 3206 CG2 THR A 399 19.442 0.255 6.302 1.00 42.02 C
ANISOU 3206 CG2 THR A 399 7583 3341 5041 1807 2097 660 C
ATOM 3207 C THR A 399 21.431 -1.948 5.863 1.00 32.11 C
ANISOU 3207 C THR A 399 6422 2853 2925 343 1903 591 C
ATOM 3208 O THR A 399 22.327 -1.302 5.377 1.00 38.78 O
ANISOU 3208 O THR A 399 7660 3320 3753 -316 3019 378 O
ATOM 3209 N VAL A 400 21.602 -2.743 6.920 1.00 28.73 N
ANISOU 3209 N VAL A 400 6365 2067 2482 332 1546 14 N
ATOM 3210 CA VAL A 400 22.834 -2.839 7.679 1.00 26.82 C
ANISOU 3210 CA VAL A 400 5405 2050 2734 -1155 1445 -233 C
ATOM 3211 CB VAL A 400 22.518 -3.481 9.042 1.00 32.72 C
ANISOU 3211 CB VAL A 400 6126 3920 2386 -858 1272 -79 C
ATOM 3212 CG1 VAL A 400 23.774 -3.862 9.795 1.00 37.78 C
ANISOU 3212 CG1 VAL A 400 6063 4922 3367 -797 1171 -240 C
ATOM 3213 CG2 VAL A 400 21.622 -2.564 9.867 1.00 35.25 C
ANISOU 3213 CG2 VAL A 400 6703 3423 3267 -983 1402 -264 C
ATOM 3214 C VAL A 400 23.929 -3.600 6.897 1.00 26.42 C
ANISOU 3214 C VAL A 400 4499 2894 2644 -1065 934 -316 C
ATOM 3215 O VAL A 400 25.137 -3.335 7.074 1.00 29.63 O
ANISOU 3215 O VAL A 400 4545 3650 3061 -1418 660 -307 O
ATOM 3216 N ALA A 401 23.529 -4.519 6.011 1.00 22.42 N
ANISOU 3216 N ALA A 401 3640 2587 2291 -786 632 -42 N
ATOM 3217 CA ALA A 401 24.477 -5.346 5.238 1.00 22.52 C
ANISOU 3217 CA ALA A 401 3361 2704 2490 -818 661 -246 C
ATOM 3218 CB ALA A 401 23.803 -6.636 4.805 1.00 21.55 C
ANISOU 3218 CB ALA A 401 3217 2531 2438 -529 868 -361 C
ATOM 3219 C ALA A 401 25.005 -4.598 4.012 1.00 24.25 C
ANISOU 3219 C ALA A 401 3529 3020 2663 -651 823 -114 C
ATOM 3220 O ALA A 401 25.920 -5.070 3.367 1.00 24.36 O
ANISOU 3220 O ALA A 401 3442 2917 2897 -501 951 -50 O
ATOM 3221 N ASP A 402 24.390 -3.455 3.689 1.00 27.30 N
ANISOU 3221 N ASP A 402 4570 2954 2845 -652 1075 199 N
ATOM 3222 CA ASP A 402 24.744 -2.618 2.534 1.00 28.37 C
ANISOU 3222 CA ASP A 402 4395 3232 3149 -538 1297 412 C
ATOM 3223 CB ASP A 402 23.696 -1.513 2.395 1.00 29.52 C
ANISOU 3223 CB ASP A 402 4809 3406 2998 -170 1255 253 C
ATOM 3224 CG ASP A 402 23.828 -0.617 1.173 1.00 30.90 C
ANISOU 3224 CG ASP A 402 5021 3821 2899 14 1005 356 C
ATOM 3225 OD1 ASP A 402 24.881 -0.657 0.501 1.00 33.09 O
ANISOU 3225 OD1 ASP A 402 4597 4175 3799 5 947 -409 O
ATOM 3226 OD2 ASP A 402 22.861 0.126 0.909 1.00 34.24 O
ANISOU 3226 OD2 ASP A 402 5391 4088 3528 471 594 229 O
ATOM 3227 C ASP A 402 26.145 -2.038 2.719 1.00 28.24 C
ANISOU 3227 C ASP A 402 4594 3006 3128 -526 1488 -82 C
ATOM 3228 O ASP A 402 26.396 -1.298 3.669 1.00 30.36 O
ANISOU 3228 O ASP A 402 4633 3571 3330 -765 888 -342 O
ATOM 3229 N PRO A 403 27.098 -2.310 1.792 1.00 30.53 N
ANISOU 3229 N PRO A 403 4681 3305 3610 -1060 1973 221 N
ATOM 3230 CA PRO A 403 28.450 -1.758 1.910 1.00 31.91 C
ANISOU 3230 CA PRO A 403 4720 3452 3951 -971 1588 27 C
ATOM 3231 CB PRO A 403 29.211 -2.468 0.784 1.00 32.46 C
ANISOU 3231 CB PRO A 403 4161 3834 4337 -1033 1912 89 C
ATOM 3232 CG PRO A 403 28.146 -2.788 -0.251 1.00 32.52 C
ANISOU 3232 CG PRO A 403 4862 3672 3821 -1325 1725 73 C
ATOM 3233 CD PRO A 403 26.918 -3.121 0.576 1.00 30.92 C
ANISOU 3233 CD PRO A 403 4781 3479 3488 -1052 1617 397 C
ATOM 3234 C PRO A 403 28.511 -0.231 1.745 1.00 34.84 C
ANISOU 3234 C PRO A 403 5409 3438 4390 -1323 1333 -68 C
ATOM 3235 O PRO A 403 29.497 0.389 2.174 1.00 40.12 O
ANISOU 3235 O PRO A 403 5548 4865 4829 -1582 1117 -74 O
ATOM 3236 N ALA A 404 27.471 0.356 1.133 1.00 34.32 N
ANISOU 3236 N ALA A 404 5476 3032 4530 -1170 1547 80 N
ATOM 3237 CA ALA A 404 27.341 1.818 0.982 1.00 36.43 C
ANISOU 3237 CA ALA A 404 6120 3187 4533 -741 1692 127 C
ATOM 3238 CB ALA A 404 26.266 2.141 -0.028 1.00 39.63 C
ANISOU 3238 CB ALA A 404 7039 3739 4279 -477 1432 300 C
ATOM 3239 C ALA A 404 27.034 2.496 2.327 1.00 34.76 C
ANISOU 3239 C ALA A 404 5996 2832 4379 -1697 1524 131 C
ATOM 3240 O ALA A 404 27.147 3.708 2.428 1.00 43.09 O
ANISOU 3240 O ALA A 404 7647 2784 5941 -1288 1255 225 O
ATOM 3241 N VAL A 405 26.607 1.722 3.334 1.00 35.37 N
ANISOU 3241 N VAL A 405 5611 3583 4243 -868 2007 328 N
ATOM 3242 CA VAL A 405 26.399 2.254 4.682 1.00 33.01 C
ANISOU 3242 CA VAL A 405 4590 3503 4449 -610 1647 -79 C
ATOM 3243 CB VAL A 405 25.165 1.632 5.365 1.00 31.08 C
ANISOU 3243 CB VAL A 405 4564 2901 4343 -362 1547 137 C
ATOM 3244 CG1 VAL A 405 24.952 2.216 6.751 1.00 33.66 C
ANISOU 3244 CG1 VAL A 405 5049 3375 4363 -174 1297 -32 C
ATOM 3245 CG2 VAL A 405 23.903 1.789 4.529 1.00 30.52 C
ANISOU 3245 CG2 VAL A 405 4814 2688 4092 -596 1426 -335 C
ATOM 3246 C VAL A 405 27.668 2.001 5.502 1.00 35.21 C
ANISOU 3246 C VAL A 405 4466 3751 5158 -1483 1383 26 C
ATOM 3247 O VAL A 405 27.967 0.861 5.833 1.00 34.48 O
ANISOU 3247 O VAL A 405 3613 4399 5085 -774 1214 153 O
ATOM 3248 N ALA A 406 28.408 3.076 5.797 1.00 37.75 N
ANISOU 3248 N ALA A 406 4612 3888 5840 -1926 1006 515 N
ATOM 3249 CA ALA A 406 29.641 3.032 6.592 1.00 42.96 C
ANISOU 3249 CA ALA A 406 4082 4851 7387 -1762 805 571 C
ATOM 3250 CB ALA A 406 30.254 4.413 6.644 1.00 45.86 C
ANISOU 3250 CB ALA A 406 4918 4744 7760 -1780 627 428 C
ATOM 3251 C ALA A 406 29.340 2.518 8.003 1.00 43.92 C
ANISOU 3251 C ALA A 406 4081 5401 7204 -1474 48 980 C
ATOM 3252 O ALA A 406 28.219 2.670 8.500 1.00 43.03 O
ANISOU 3252 O ALA A 406 3984 4258 8104 -1489 100 953 O
ATOM 3253 N ALA A 407 30.358 1.941 8.651 1.00 47.42 N
ANISOU 3253 N ALA A 407 2904 6662 8449 -1531 -69 661 N
ATOM 3254 CA ALA A 407 30.238 1.281 9.978 1.00 52.08 C
ANISOU 3254 CA ALA A 407 5014 6217 8555 -1785 -1139 775 C
ATOM 3255 CB ALA A 407 31.613 0.885 10.470 1.00 53.90 C
ANISOU 3255 CB ALA A 407 5124 6402 8951 -1937 -1587 361 C
ATOM 3256 C ALA A 407 29.531 2.185 11.003 1.00 53.23 C
ANISOU 3256 C ALA A 407 6535 5155 8534 -2293 -2143 -163 C
ATOM 3257 O ALA A 407 28.663 1.717 11.748 1.00 53.07 O
ANISOU 3257 O ALA A 407 7858 4153 8153 -2186 -2698 159 O
ATOM 3258 N GLY A 408 29.908 3.471 11.044 1.00 56.47 N
ANISOU 3258 N GLY A 408 7461 5485 8510 -2808 -2315 -322 N
ATOM 3259 CA GLY A 408 29.311 4.468 11.962 1.00 50.15 C
ANISOU 3259 CA GLY A 408 7596 4181 7276 -3513 -2752 -132 C
ATOM 3260 C GLY A 408 27.810 4.619 11.756 1.00 53.64 C
ANISOU 3260 C GLY A 408 8627 5230 6524 -736 -2227 87 C
ATOM 3261 O GLY A 408 27.032 4.780 12.718 1.00 61.35 O
ANISOU 3261 O GLY A 408 11498 4882 6930 957 -1818 658 O
ATOM 3262 N ASN A 409 27.390 4.559 10.492 1.00 43.68 N
ANISOU 3262 N ASN A 409 7027 3628 5940 -1076 -1434 584 N
ATOM 3263 CA ASN A 409 26.002 4.782 10.128 1.00 40.94 C
ANISOU 3263 CA ASN A 409 6493 3400 5659 -929 -235 865 C
ATOM 3264 CB ASN A 409 25.890 5.385 8.732 1.00 42.32 C
ANISOU 3264 CB ASN A 409 6648 3455 5974 -1023 359 1458 C
ATOM 3265 CG ASN A 409 26.356 6.823 8.711 1.00 46.68 C
ANISOU 3265 CG ASN A 409 8108 3219 6408 -914 -111 1124 C
ATOM 3266 OD1 ASN A 409 26.272 7.515 9.725 1.00 50.54 O
ANISOU 3266 OD1 ASN A 409 9123 3614 6463 -649 117 1147 O
ATOM 3267 ND2 ASN A 409 26.858 7.275 7.573 1.00 52.17 N
ANISOU 3267 ND2 ASN A 409 8076 4530 7214 -1675 518 1283 N
ATOM 3268 C ASN A 409 25.188 3.486 10.227 1.00 32.73 C
ANISOU 3268 C ASN A 409 4594 3116 4725 -309 -64 597 C
ATOM 3269 O ASN A 409 23.959 3.544 10.253 1.00 30.12 O
ANISOU 3269 O ASN A 409 4736 3400 3308 6 -157 632 O
ATOM 3270 N LYS A 410 25.854 2.327 10.282 1.00 27.60 N
ANISOU 3270 N LYS A 410 3561 3002 3921 -576 354 654 N
ATOM 3271 CA LYS A 410 25.126 1.056 10.396 1.00 24.73 C
ANISOU 3271 CA LYS A 410 2492 2980 3924 -352 451 397 C
ATOM 3272 CB LYS A 410 26.066 -0.151 10.338 1.00 25.59 C
ANISOU 3272 CB LYS A 410 2295 2959 4466 -602 629 450 C
ATOM 3273 CG LYS A 410 26.600 -0.450 8.943 1.00 27.18 C
ANISOU 3273 CG LYS A 410 2383 3408 4533 -732 856 87 C
ATOM 3274 CD LYS A 410 27.451 -1.698 8.880 1.00 29.60 C
ANISOU 3274 CD LYS A 410 2720 3898 4627 -549 505 64 C
ATOM 3275 CE LYS A 410 28.254 -1.829 7.602 1.00 32.42 C
ANISOU 3275 CE LYS A 410 3088 4520 4709 -472 679 -307 C
ATOM 3276 NZ LYS A 410 27.411 -1.840 6.376 1.00 30.64 N
ANISOU 3276 NZ LYS A 410 3321 4337 3982 -625 1134 -445 N
ATOM 3277 C LYS A 410 24.298 1.053 11.677 1.00 22.60 C
ANISOU 3277 C LYS A 410 1892 3025 3667 -384 -46 204 C
ATOM 3278 O LYS A 410 23.134 0.683 11.657 1.00 22.49 O
ANISOU 3278 O LYS A 410 1734 3293 3516 -380 225 55 O
ATOM 3279 N PHE A 411 24.901 1.493 12.779 1.00 23.01 N
ANISOU 3279 N PHE A 411 2379 2822 3541 -425 -31 49 N
ATOM 3280 CA PHE A 411 24.194 1.510 14.041 1.00 22.16 C
ANISOU 3280 CA PHE A 411 2291 2826 3302 -769 -212 -35 C
ATOM 3281 CB PHE A 411 25.110 1.930 15.193 1.00 23.56 C
ANISOU 3281 CB PHE A 411 2715 2947 3289 -761 -313 -55 C
ATOM 3282 CG PHE A 411 24.337 2.026 16.478 1.00 24.02 C
ANISOU 3282 CG PHE A 411 2643 3185 3298 -657 -253 -135 C
ATOM 3283 CD1 PHE A 411 23.852 0.877 17.083 1.00 24.42 C
ANISOU 3283 CD1 PHE A 411 3377 2830 3072 -505 -221 -253 C
ATOM 3284 CE1 PHE A 411 23.088 0.956 18.232 1.00 25.16 C
ANISOU 3284 CE1 PHE A 411 3529 2966 3063 -160 -195 58 C
ATOM 3285 CZ PHE A 411 22.783 2.179 18.778 1.00 25.86 C
ANISOU 3285 CZ PHE A 411 3535 2772 3516 -284 -371 97 C
ATOM 3286 CD2 PHE A 411 23.987 3.252 17.013 1.00 25.08 C
ANISOU 3286 CD2 PHE A 411 3154 2916 3456 -579 -424 75 C
ATOM 3287 CE2 PHE A 411 23.239 3.326 18.176 1.00 27.53 C
ANISOU 3287 CE2 PHE A 411 3507 3211 3739 -400 -131 199 C
ATOM 3288 C PHE A 411 22.987 2.455 13.974 1.00 19.95 C
ANISOU 3288 C PHE A 411 2223 2460 2893 -855 25 -153 C
ATOM 3289 O PHE A 411 21.889 2.090 14.385 1.00 22.17 O
ANISOU 3289 O PHE A 411 2123 3330 2968 -1058 -222 224 O
ATOM 3290 N LYS A 412 23.199 3.666 13.450 1.00 23.67 N
ANISOU 3290 N LYS A 412 2829 2701 3462 -934 -282 149 N
ATOM 3291 CA LYS A 412 22.151 4.698 13.409 1.00 23.73 C
ANISOU 3291 CA LYS A 412 2558 2872 3585 -907 72 -42 C
ATOM 3292 CB LYS A 412 22.703 6.001 12.818 1.00 29.34 C
ANISOU 3292 CB LYS A 412 3431 2740 4976 -1303 102 -49 C
ATOM 3293 CG LYS A 412 23.703 6.706 13.728 1.00 39.61 C
ANISOU 3293 CG LYS A 412 4680 4225 6142 -1559 -417 -480 C
ATOM 3294 CD LYS A 412 24.276 8.015 13.201 1.00 46.61 C
ANISOU 3294 CD LYS A 412 5815 4632 7262 -2133 79 -245 C
ATOM 3295 CE LYS A 412 25.077 8.734 14.270 1.00 54.34 C
ANISOU 3295 CE LYS A 412 6978 5832 7834 -2074 -400 -797 C
ATOM 3296 NZ LYS A 412 25.631 10.029 13.804 1.00 57.72 N
ANISOU 3296 NZ LYS A 412 7641 5790 8496 -2286 -376 -981 N
ATOM 3297 C LYS A 412 20.932 4.197 12.617 1.00 22.94 C
ANISOU 3297 C LYS A 412 2593 2597 3525 -733 58 78 C
ATOM 3298 O LYS A 412 19.806 4.587 12.905 1.00 24.72 O
ANISOU 3298 O LYS A 412 2741 2796 3854 -524 105 -264 O
ATOM 3299 N GLU A 413 21.177 3.366 11.596 1.00 20.97 N
ANISOU 3299 N GLU A 413 2268 2353 3344 -634 38 169 N
ATOM 3300 CA GLU A 413 20.122 2.918 10.693 1.00 21.16 C
ANISOU 3300 CA GLU A 413 2263 2420 3354 -845 79 146 C
ATOM 3301 CB GLU A 413 20.655 2.779 9.277 1.00 24.05 C
ANISOU 3301 CB GLU A 413 2570 3246 3319 -1067 232 449 C
ATOM 3302 CG GLU A 413 21.150 4.118 8.752 1.00 29.84 C
ANISOU 3302 CG GLU A 413 4035 3280 4021 -1270 283 518 C
ATOM 3303 CD GLU A 413 21.442 4.201 7.270 1.00 35.34 C
ANISOU 3303 CD GLU A 413 4781 4504 4140 -1082 563 556 C
ATOM 3304 OE1 GLU A 413 20.994 3.315 6.531 1.00 41.67 O
ANISOU 3304 OE1 GLU A 413 5673 5084 5073 -1343 280 93 O
ATOM 3305 OE2 GLU A 413 22.114 5.169 6.867 1.00 45.32 O
ANISOU 3305 OE2 GLU A 413 6740 4875 5602 -1461 600 1286 O
ATOM 3306 C GLU A 413 19.459 1.619 11.165 1.00 18.72 C
ANISOU 3306 C GLU A 413 2177 2205 2729 -529 189 50 C
ATOM 3307 O GLU A 413 18.392 1.283 10.646 1.00 18.23 O
ANISOU 3307 O GLU A 413 2081 2122 2723 -458 91 108 O
ATOM 3308 N ALA A 414 20.066 0.913 12.122 1.00 16.51 N
ANISOU 3308 N ALA A 414 1784 2202 2285 -511 315 -136 N
ATOM 3309 CA ALA A 414 19.555 -0.388 12.547 1.00 15.16 C
ANISOU 3309 CA ALA A 414 1663 2033 2063 -359 218 -322 C
ATOM 3310 CB ALA A 414 20.562 -1.093 13.417 1.00 15.78 C
ANISOU 3310 CB ALA A 414 1581 2366 2048 -287 383 -231 C
ATOM 3311 C ALA A 414 18.223 -0.224 13.278 1.00 15.01 C
ANISOU 3311 C ALA A 414 1788 2070 1844 -381 218 -186 C
ATOM 3312 O ALA A 414 18.056 0.692 14.114 1.00 16.68 O
ANISOU 3312 O ALA A 414 1873 2131 2331 -336 348 -474 O
ATOM 3313 N ILE A 415 17.312 -1.162 12.992 1.00 13.40 N
ANISOU 3313 N ILE A 415 1394 1658 2038 -60 180 -144 N
ATOM 3314 CA ILE A 415 15.996 -1.221 13.635 1.00 12.81 C
ANISOU 3314 CA ILE A 415 1481 1531 1853 -134 190 -211 C
ATOM 3315 CB ILE A 415 14.861 -0.959 12.635 1.00 13.21 C
ANISOU 3315 CB ILE A 415 1605 1611 1803 -51 176 -53 C
ATOM 3316 CG1 ILE A 415 14.992 0.450 12.048 1.00 15.10 C
ANISOU 3316 CG1 ILE A 415 1764 1756 2214 -3 235 206 C
ATOM 3317 CG2 ILE A 415 13.490 -1.212 13.280 1.00 13.62 C
ANISOU 3317 CG2 ILE A 415 1538 1745 1889 125 132 43 C
ATOM 3318 CD1 ILE A 415 14.057 0.736 10.906 1.00 16.82 C
ANISOU 3318 CD1 ILE A 415 1801 2239 2348 -30 220 447 C
ATOM 3319 C ILE A 415 15.867 -2.590 14.290 1.00 12.76 C
ANISOU 3319 C ILE A 415 1468 1589 1788 -47 45 -127 C
ATOM 3320 O ILE A 415 16.191 -3.578 13.661 1.00 14.13 O
ANISOU 3320 O ILE A 415 1839 1742 1785 -90 151 -273 O
ATOM 3321 N PHE A 416 15.354 -2.614 15.523 1.00 11.58 N
ANISOU 3321 N PHE A 416 1318 1376 1703 -93 -20 -247 N
ATOM 3322 CA PHE A 416 15.192 -3.845 16.291 1.00 12.17 C
ANISOU 3322 CA PHE A 416 1513 1306 1803 95 -64 -179 C
ATOM 3323 CB PHE A 416 16.054 -3.820 17.555 1.00 12.76 C
ANISOU 3323 CB PHE A 416 1452 1651 1745 -180 -63 -266 C
ATOM 3324 CG PHE A 416 17.531 -3.809 17.238 1.00 14.36 C
ANISOU 3324 CG PHE A 416 1396 1995 2064 -186 -194 -336 C
ATOM 3325 CD1 PHE A 416 18.203 -2.616 17.037 1.00 15.61 C
ANISOU 3325 CD1 PHE A 416 1805 2017 2107 -254 -379 -214 C
ATOM 3326 CE1 PHE A 416 19.542 -2.612 16.688 1.00 16.08 C
ANISOU 3326 CE1 PHE A 416 1794 2056 2258 -419 -241 -305 C
ATOM 3327 CZ PHE A 416 20.224 -3.800 16.525 1.00 16.09 C
ANISOU 3327 CZ PHE A 416 1409 2420 2283 -290 44 -206 C
ATOM 3328 CD2 PHE A 416 18.229 -4.997 17.089 1.00 14.13 C
ANISOU 3328 CD2 PHE A 416 1406 2121 1840 -66 -155 -149 C
ATOM 3329 CE2 PHE A 416 19.575 -4.989 16.748 1.00 15.64 C
ANISOU 3329 CE2 PHE A 416 1453 2186 2303 -21 -154 -237 C
ATOM 3330 C PHE A 416 13.729 -4.061 16.673 1.00 12.85 C
ANISOU 3330 C PHE A 416 1641 1506 1733 -52 16 -27 C
ATOM 3331 O PHE A 416 12.934 -3.114 16.781 1.00 12.94 O
ANISOU 3331 O PHE A 416 1540 1491 1886 -152 221 -139 O
ATOM 3332 N GLY A 417 13.362 -5.320 16.900 1.00 12.00 N
ANISOU 3332 N GLY A 417 1518 1279 1761 144 128 -322 N
ATOM 3333 CA GLY A 417 12.079 -5.591 17.528 1.00 12.51 C
ANISOU 3333 CA GLY A 417 1544 1454 1753 211 73 -119 C
ATOM 3334 C GLY A 417 11.956 -4.851 18.851 1.00 12.78 C
ANISOU 3334 C GLY A 417 1614 1531 1710 -89 -94 -125 C
ATOM 3335 O GLY A 417 12.949 -4.628 19.557 1.00 13.58 O
ANISOU 3335 O GLY A 417 1529 1967 1663 -145 -56 38 O
ATOM 3336 N ALA A 418 10.727 -4.477 19.208 1.00 12.31 N
ANISOU 3336 N ALA A 418 1475 1747 1453 -86 -174 -162 N
ATOM 3337 CA ALA A 418 10.473 -3.750 20.453 1.00 13.63 C
ANISOU 3337 CA ALA A 418 1830 1839 1508 -94 -250 -180 C
ATOM 3338 CB ALA A 418 9.020 -3.333 20.531 1.00 15.30 C
ANISOU 3338 CB ALA A 418 1892 2370 1549 129 -258 -122 C
ATOM 3339 C ALA A 418 10.870 -4.579 21.678 1.00 13.04 C
ANISOU 3339 C ALA A 418 1748 1731 1473 -143 -183 -174 C
ATOM 3340 O ALA A 418 11.199 -3.995 22.695 1.00 15.20 O
ANISOU 3340 O ALA A 418 2406 1791 1577 -94 -331 -221 O
ATOM 3341 N GLY A 419 10.830 -5.918 21.570 1.00 12.51 N
ANISOU 3341 N GLY A 419 1752 1756 1243 6 -158 -193 N
ATOM 3342 CA GLY A 419 11.306 -6.811 22.616 1.00 12.74 C
ANISOU 3342 CA GLY A 419 1584 1789 1464 -51 -112 -88 C
ATOM 3343 C GLY A 419 10.158 -7.545 23.314 1.00 12.28 C
ANISOU 3343 C GLY A 419 1739 1551 1374 -88 -66 -116 C
ATOM 3344 O GLY A 419 9.012 -7.516 22.853 1.00 12.70 O
ANISOU 3344 O GLY A 419 1616 1780 1429 -58 86 -123 O
ATOM 3345 N SER A 420 10.508 -8.313 24.354 1.00 12.49 N
ANISOU 3345 N SER A 420 1529 1925 1290 -225 -231 -103 N
ATOM 3346 CA SER A 420 9.683 -9.423 24.846 1.00 12.50 C
ANISOU 3346 CA SER A 420 1614 1748 1385 -33 -99 -44 C
ATOM 3347 CB SER A 420 10.566 -10.580 25.271 1.00 12.17 C
ANISOU 3347 CB SER A 420 1486 1693 1443 -51 -113 46 C
ATOM 3348 OG SER A 420 11.601 -10.867 24.359 1.00 12.46 O
ANISOU 3348 OG SER A 420 1501 1679 1554 -29 -130 112 O
ATOM 3349 C SER A 420 8.788 -9.056 26.033 1.00 11.81 C
ANISOU 3349 C SER A 420 1264 1845 1378 -101 -198 -80 C
ATOM 3350 O SER A 420 9.201 -8.362 26.962 1.00 13.14 O
ANISOU 3350 O SER A 420 1717 1788 1488 -291 -43 -207 O
ATOM 3351 N VAL A 421 7.624 -9.703 26.081 1.00 11.66 N
ANISOU 3351 N VAL A 421 1406 1562 1462 -108 -214 -148 N
ATOM 3352 CA VAL A 421 6.865 -9.901 27.321 1.00 12.20 C
ANISOU 3352 CA VAL A 421 1603 1617 1413 5 -253 -105 C
ATOM 3353 CB VAL A 421 5.599 -9.028 27.437 1.00 12.62 C
ANISOU 3353 CB VAL A 421 1656 1520 1619 24 -188 -241 C
ATOM 3354 CG1 VAL A 421 4.900 -9.269 28.766 1.00 13.19 C
ANISOU 3354 CG1 VAL A 421 1628 1637 1745 264 -126 -310 C
ATOM 3355 CG2 VAL A 421 5.934 -7.567 27.229 1.00 13.25 C
ANISOU 3355 CG2 VAL A 421 1683 1515 1834 55 -335 -262 C
ATOM 3356 C VAL A 421 6.499 -11.381 27.330 1.00 12.13 C
ANISOU 3356 C VAL A 421 1616 1600 1393 70 -129 49 C
ATOM 3357 O VAL A 421 5.906 -11.883 26.359 1.00 12.57 O
ANISOU 3357 O VAL A 421 1814 1558 1404 75 -19 -51 O
ATOM 3358 N ILE A 422 6.887 -12.059 28.410 1.00 11.88 N
ANISOU 3358 N ILE A 422 1724 1606 1182 161 -97 -41 N
ATOM 3359 CA ILE A 422 6.606 -13.485 28.550 1.00 11.83 C
ANISOU 3359 CA ILE A 422 1532 1607 1356 135 -81 -12 C
ATOM 3360 CB ILE A 422 7.870 -14.305 28.842 1.00 12.18 C
ANISOU 3360 CB ILE A 422 1635 1493 1496 221 -64 -141 C
ATOM 3361 CG1 ILE A 422 8.912 -14.099 27.738 1.00 12.65 C
ANISOU 3361 CG1 ILE A 422 1769 1610 1425 477 4 28 C
ATOM 3362 CG2 ILE A 422 7.494 -15.773 29.022 1.00 12.92 C
ANISOU 3362 CG2 ILE A 422 1744 1595 1568 225 -118 92 C
ATOM 3363 CD1 ILE A 422 10.277 -14.675 28.068 1.00 13.72 C
ANISOU 3363 CD1 ILE A 422 1921 1749 1540 540 -32 106 C
ATOM 3364 C ILE A 422 5.546 -13.687 29.636 1.00 11.45 C
ANISOU 3364 C ILE A 422 1550 1552 1245 218 -121 37 C
ATOM 3365 O ILE A 422 5.813 -13.468 30.822 1.00 12.70 O
ANISOU 3365 O ILE A 422 1771 1853 1198 78 -135 198 O
ATOM 3366 N PHE A 423 4.356 -14.116 29.197 1.00 10.91 N
ANISOU 3366 N PHE A 423 1522 1503 1120 114 -20 31 N
ATOM 3367 CA PHE A 423 3.256 -14.478 30.096 1.00 11.12 C
ANISOU 3367 CA PHE A 423 1553 1535 1136 132 -78 -2 C
ATOM 3368 CB PHE A 423 1.929 -14.138 29.421 1.00 11.48 C
ANISOU 3368 CB PHE A 423 1415 1558 1388 310 78 78 C
ATOM 3369 CG PHE A 423 1.687 -12.656 29.223 1.00 11.50 C
ANISOU 3369 CG PHE A 423 1559 1424 1383 167 99 -105 C
ATOM 3370 CD1 PHE A 423 1.175 -11.878 30.250 1.00 12.90 C
ANISOU 3370 CD1 PHE A 423 1967 1649 1285 402 15 -77 C
ATOM 3371 CE1 PHE A 423 0.958 -10.525 30.073 1.00 13.17 C
ANISOU 3371 CE1 PHE A 423 2056 1590 1357 303 52 -107 C
ATOM 3372 CZ PHE A 423 1.201 -9.940 28.851 1.00 12.28 C
ANISOU 3372 CZ PHE A 423 1805 1441 1416 234 263 -139 C
ATOM 3373 CD2 PHE A 423 1.936 -12.050 28.007 1.00 12.12 C
ANISOU 3373 CD2 PHE A 423 1630 1580 1393 368 29 -99 C
ATOM 3374 CE2 PHE A 423 1.677 -10.706 27.815 1.00 12.76 C
ANISOU 3374 CE2 PHE A 423 1993 1541 1315 269 214 -108 C
ATOM 3375 C PHE A 423 3.331 -15.977 30.370 1.00 12.03 C
ANISOU 3375 C PHE A 423 1757 1559 1254 129 2 48 C
ATOM 3376 O PHE A 423 3.425 -16.775 29.430 1.00 12.66 O
ANISOU 3376 O PHE A 423 1931 1501 1375 111 -43 41 O
ATOM 3377 N PHE A 424 3.278 -16.372 31.649 1.00 11.72 N
ANISOU 3377 N PHE A 424 1891 1317 1243 262 -15 -71 N
ATOM 3378 CA PHE A 424 3.241 -17.787 32.006 1.00 12.43 C
ANISOU 3378 CA PHE A 424 1962 1406 1354 213 94 49 C
ATOM 3379 CB PHE A 424 4.643 -18.385 32.187 1.00 13.13 C
ANISOU 3379 CB PHE A 424 2019 1378 1588 340 167 92 C
ATOM 3380 CG PHE A 424 5.387 -17.986 33.432 1.00 13.89 C
ANISOU 3380 CG PHE A 424 2046 1454 1777 312 -99 192 C
ATOM 3381 CD1 PHE A 424 5.231 -18.695 34.604 1.00 15.81 C
ANISOU 3381 CD1 PHE A 424 2398 1873 1734 148 -75 227 C
ATOM 3382 CE1 PHE A 424 5.918 -18.345 35.756 1.00 16.42 C
ANISOU 3382 CE1 PHE A 424 2332 2169 1735 220 -209 284 C
ATOM 3383 CZ PHE A 424 6.740 -17.257 35.765 1.00 15.56 C
ANISOU 3383 CZ PHE A 424 2003 2355 1553 162 -270 165 C
ATOM 3384 CD2 PHE A 424 6.256 -16.907 33.441 1.00 15.38 C
ANISOU 3384 CD2 PHE A 424 2285 1780 1775 172 -35 58 C
ATOM 3385 CE2 PHE A 424 6.904 -16.525 34.608 1.00 15.67 C
ANISOU 3385 CE2 PHE A 424 2029 1959 1964 120 -263 291 C
ATOM 3386 C PHE A 424 2.386 -17.981 33.251 1.00 11.86 C
ANISOU 3386 C PHE A 424 1721 1343 1439 392 92 32 C
ATOM 3387 O PHE A 424 2.291 -17.093 34.095 1.00 13.01 O
ANISOU 3387 O PHE A 424 2058 1565 1320 400 48 -22 O
ATOM 3388 N ARG A 425 1.752 -19.158 33.308 1.00 12.79 N
ANISOU 3388 N ARG A 425 1948 1340 1570 248 164 -90 N
ATOM 3389 CA ARG A 425 0.894 -19.560 34.391 1.00 12.94 C
ANISOU 3389 CA ARG A 425 2042 1463 1410 370 45 -41 C
ATOM 3390 CB ARG A 425 -0.371 -20.221 33.847 1.00 12.71 C
ANISOU 3390 CB ARG A 425 2020 1480 1325 251 125 78 C
ATOM 3391 CG ARG A 425 -1.220 -19.333 32.956 1.00 13.69 C
ANISOU 3391 CG ARG A 425 1995 1737 1470 330 33 84 C
ATOM 3392 CD ARG A 425 -2.371 -20.134 32.352 1.00 13.92 C
ANISOU 3392 CD ARG A 425 1921 1880 1488 295 25 143 C
ATOM 3393 NE ARG A 425 -3.193 -19.383 31.426 1.00 15.36 N
ANISOU 3393 NE ARG A 425 2148 2209 1479 407 67 237 N
ATOM 3394 CZ ARG A 425 -4.230 -18.616 31.736 1.00 14.89 C
ANISOU 3394 CZ ARG A 425 1993 1864 1798 237 -208 381 C
ATOM 3395 NH1 ARG A 425 -4.599 -18.463 32.994 1.00 17.93 N
ANISOU 3395 NH1 ARG A 425 2543 2446 1822 153 192 529 N
ATOM 3396 NH2 ARG A 425 -4.896 -18.020 30.769 1.00 17.74 N
ANISOU 3396 NH2 ARG A 425 2430 2334 1977 41 -450 784 N
ATOM 3397 C ARG A 425 1.632 -20.556 35.276 1.00 12.43 C
ANISOU 3397 C ARG A 425 2075 1390 1257 315 24 -110 C
ATOM 3398 O ARG A 425 2.525 -21.274 34.817 1.00 13.26 O
ANISOU 3398 O ARG A 425 2145 1421 1472 485 36 65 O
ATOM 3399 N PRO A 426 1.201 -20.740 36.533 1.00 13.13 N
ANISOU 3399 N PRO A 426 2220 1511 1256 647 111 77 N
ATOM 3400 CA PRO A 426 1.800 -21.783 37.356 1.00 13.43 C
ANISOU 3400 CA PRO A 426 2024 1663 1414 677 82 178 C
ATOM 3401 CB PRO A 426 1.071 -21.702 38.696 1.00 16.19 C
ANISOU 3401 CB PRO A 426 2457 2296 1398 709 177 97 C
ATOM 3402 CG PRO A 426 -0.046 -20.745 38.503 1.00 16.82 C
ANISOU 3402 CG PRO A 426 2546 2234 1609 737 428 168 C
ATOM 3403 CD PRO A 426 0.204 -19.939 37.255 1.00 13.77 C
ANISOU 3403 CD PRO A 426 2205 1641 1387 729 19 -26 C
ATOM 3404 C PRO A 426 1.674 -23.174 36.719 1.00 13.04 C
ANISOU 3404 C PRO A 426 1993 1668 1292 540 109 166 C
ATOM 3405 O PRO A 426 2.614 -23.980 36.848 1.00 14.43 O
ANISOU 3405 O PRO A 426 1885 1900 1695 563 -23 242 O
ATOM 3406 N SER A 427 0.577 -23.420 35.988 1.00 13.03 N
ANISOU 3406 N SER A 427 2032 1380 1537 342 122 232 N
ATOM 3407 CA SER A 427 0.397 -24.719 35.330 1.00 13.68 C
ANISOU 3407 CA SER A 427 2236 1401 1557 80 269 278 C
ATOM 3408 CB SER A 427 -1.033 -24.907 34.827 1.00 14.82 C
ANISOU 3408 CB SER A 427 2357 1593 1679 65 256 147 C
ATOM 3409 OG SER A 427 -1.470 -23.796 34.073 1.00 16.87 O
ANISOU 3409 OG SER A 427 2720 1809 1881 145 77 301 O
ATOM 3410 C SER A 427 1.422 -24.942 34.214 1.00 13.58 C
ANISOU 3410 C SER A 427 2245 1370 1543 238 196 127 C
ATOM 3411 O SER A 427 1.748 -26.090 33.889 1.00 17.01 O
ANISOU 3411 O SER A 427 2937 1537 1989 193 535 -101 O
ATOM 3412 N ASP A 428 1.978 -23.871 33.656 1.00 12.44 N
ANISOU 3412 N ASP A 428 1977 1306 1444 412 130 241 N
ATOM 3413 CA ASP A 428 2.986 -24.007 32.591 1.00 12.97 C
ANISOU 3413 CA ASP A 428 2003 1487 1438 355 134 58 C
ATOM 3414 CB ASP A 428 3.258 -22.663 31.911 1.00 12.90 C
ANISOU 3414 CB ASP A 428 1933 1451 1515 108 -17 -17 C
ATOM 3415 CG ASP A 428 2.077 -22.150 31.096 1.00 13.55 C
ANISOU 3415 CG ASP A 428 2349 1371 1426 204 -205 -41 C
ATOM 3416 OD1 ASP A 428 1.349 -22.978 30.517 1.00 16.27 O
ANISOU 3416 OD1 ASP A 428 2486 1762 1933 60 -447 -189 O
ATOM 3417 OD2 ASP A 428 1.863 -20.931 31.090 1.00 13.57 O
ANISOU 3417 OD2 ASP A 428 2269 1390 1497 274 170 68 O
ATOM 3418 C ASP A 428 4.304 -24.574 33.126 1.00 12.80 C
ANISOU 3418 C ASP A 428 2033 1470 1359 370 162 135 C
ATOM 3419 O ASP A 428 5.137 -25.054 32.354 1.00 14.20 O
ANISOU 3419 O ASP A 428 2096 1747 1551 241 350 -34 O
ATOM 3420 N LEU A 429 4.509 -24.481 34.440 1.00 13.60 N
ANISOU 3420 N LEU A 429 1979 1824 1362 576 138 -45 N
ATOM 3421 CA LEU A 429 5.801 -24.836 35.065 1.00 15.02 C
ANISOU 3421 CA LEU A 429 2003 1990 1714 740 167 179 C
ATOM 3422 CB LEU A 429 5.920 -24.145 36.423 1.00 15.35 C
ANISOU 3422 CB LEU A 429 2022 1938 1872 726 91 -4 C
ATOM 3423 CG LEU A 429 5.946 -22.624 36.415 1.00 16.14 C
ANISOU 3423 CG LEU A 429 2284 1989 1860 757 -70 57 C
ATOM 3424 CD1 LEU A 429 5.780 -22.115 37.837 1.00 17.16 C
ANISOU 3424 CD1 LEU A 429 2312 2318 1888 620 -83 -6 C
ATOM 3425 CD2 LEU A 429 7.233 -22.114 35.792 1.00 17.38 C
ANISOU 3425 CD2 LEU A 429 2410 2070 2124 609 -35 -21 C
ATOM 3426 C LEU A 429 5.959 -26.343 35.269 1.00 15.21 C
ANISOU 3426 C LEU A 429 2013 1958 1805 592 339 247 C
ATOM 3427 O LEU A 429 7.058 -26.777 35.512 1.00 16.51 O
ANISOU 3427 O LEU A 429 2270 2125 1877 876 187 232 O
ATOM 3428 N GLY A 430 4.866 -27.118 35.212 1.00 14.77 N
ANISOU 3428 N GLY A 430 1905 2005 1702 575 299 348 N
ATOM 3429 CA GLY A 430 4.931 -28.565 35.380 1.00 16.38 C
ANISOU 3429 CA GLY A 430 2268 2072 1882 863 376 384 C
ATOM 3430 C GLY A 430 5.531 -28.974 36.719 1.00 17.13 C
ANISOU 3430 C GLY A 430 2577 2276 1654 907 613 447 C
ATOM 3431 O GLY A 430 6.321 -29.948 36.797 1.00 20.18 O
ANISOU 3431 O GLY A 430 3175 2351 2141 1117 537 318 O
ATOM 3432 N LEU A 431 5.153 -28.257 37.778 1.00 16.82 N
ANISOU 3432 N LEU A 431 2325 2466 1598 885 506 398 N
ATOM 3433 CA LEU A 431 5.779 -28.450 39.084 1.00 18.28 C
ANISOU 3433 CA LEU A 431 2563 2550 1832 934 277 484 C
ATOM 3434 CB LEU A 431 5.291 -27.389 40.071 1.00 17.04 C
ANISOU 3434 CB LEU A 431 2322 2543 1607 888 21 405 C
ATOM 3435 CG LEU A 431 5.692 -25.953 39.742 1.00 19.31 C
ANISOU 3435 CG LEU A 431 2827 2615 1893 771 313 596 C
ATOM 3436 CD1 LEU A 431 4.988 -24.993 40.685 1.00 21.79 C
ANISOU 3436 CD1 LEU A 431 3095 2848 2334 556 462 201 C
ATOM 3437 CD2 LEU A 431 7.192 -25.752 39.772 1.00 22.17 C
ANISOU 3437 CD2 LEU A 431 3152 3076 2194 476 206 470 C
ATOM 3438 C LEU A 431 5.429 -29.826 39.627 1.00 19.99 C
ANISOU 3438 C LEU A 431 2886 2412 2297 1160 291 527 C
ATOM 3439 O LEU A 431 4.290 -30.263 39.548 1.00 21.50 O
ANISOU 3439 O LEU A 431 3425 2233 2510 785 246 605 O
ATOM 3440 N LYS A 432 6.428 -30.462 40.243 1.00 24.07 N
ANISOU 3440 N LYS A 432 3420 2932 2793 1500 385 1161 N
ATOM 3441 CA LYS A 432 6.179 -31.705 40.971 1.00 26.25 C
ANISOU 3441 CA LYS A 432 4129 2905 2937 1398 857 1035 C
ATOM 3442 CB LYS A 432 7.498 -32.390 41.336 1.00 34.11 C
ANISOU 3442 CB LYS A 432 4357 4609 3993 1758 524 1167 C
ATOM 3443 CG LYS A 432 8.417 -31.663 42.310 1.00 40.96 C
ANISOU 3443 CG LYS A 432 4438 5287 5837 1825 140 542 C
ATOM 3444 CD LYS A 432 9.666 -32.464 42.672 1.00 49.77 C
ANISOU 3444 CD LYS A 432 5256 6374 7279 2560 -341 817 C
ATOM 3445 CE LYS A 432 9.338 -33.755 43.395 1.00 55.82 C
ANISOU 3445 CE LYS A 432 5886 6850 8473 1931 44 841 C
ATOM 3446 NZ LYS A 432 10.498 -34.301 44.140 1.00 60.94 N
ANISOU 3446 NZ LYS A 432 6287 7911 8956 1929 -459 730 N
ATOM 3447 C LYS A 432 5.233 -31.444 42.155 1.00 23.11 C
ANISOU 3447 C LYS A 432 3814 2483 2483 1365 484 1130 C
ATOM 3448 O LYS A 432 4.468 -32.333 42.519 1.00 24.50 O
ANISOU 3448 O LYS A 432 3967 2673 2668 1263 802 961 O
ATOM 3449 N ASP A 433 5.291 -30.245 42.755 1.00 22.31 N
ANISOU 3449 N ASP A 433 3307 2545 2625 1107 457 1209 N
ATOM 3450 CA ASP A 433 4.391 -29.897 43.850 1.00 20.09 C
ANISOU 3450 CA ASP A 433 2981 2158 2494 1148 165 977 C
ATOM 3451 CB ASP A 433 4.959 -28.770 44.713 1.00 19.80 C
ANISOU 3451 CB ASP A 433 2498 2494 2532 1173 106 767 C
ATOM 3452 CG ASP A 433 4.118 -28.472 45.944 1.00 21.69 C
ANISOU 3452 CG ASP A 433 3060 2702 2479 943 197 595 C
ATOM 3453 OD1 ASP A 433 3.020 -29.059 46.063 1.00 22.70 O
ANISOU 3453 OD1 ASP A 433 3043 3010 2570 1003 51 714 O
ATOM 3454 OD2 ASP A 433 4.573 -27.660 46.785 1.00 25.57 O
ANISOU 3454 OD2 ASP A 433 3020 3397 3295 536 -138 207 O
ATOM 3455 C ASP A 433 3.014 -29.540 43.269 1.00 20.16 C
ANISOU 3455 C ASP A 433 2685 2287 2687 958 212 697 C
ATOM 3456 O ASP A 433 2.777 -28.415 42.830 1.00 19.96 O
ANISOU 3456 O ASP A 433 2747 2442 2394 1070 34 655 O
ATOM 3457 N TYR A 434 2.099 -30.518 43.271 1.00 20.75 N
ANISOU 3457 N TYR A 434 2752 2280 2851 1031 175 668 N
ATOM 3458 CA TYR A 434 0.754 -30.370 42.688 1.00 20.26 C
ANISOU 3458 CA TYR A 434 2790 2036 2871 716 169 568 C
ATOM 3459 CB TYR A 434 0.067 -31.733 42.591 1.00 23.30 C
ANISOU 3459 CB TYR A 434 3184 2077 3591 569 94 270 C
ATOM 3460 CG TYR A 434 0.162 -32.564 43.848 1.00 26.70 C
ANISOU 3460 CG TYR A 434 3927 1851 4364 802 135 698 C
ATOM 3461 CD1 TYR A 434 -0.622 -32.276 44.958 1.00 27.91 C
ANISOU 3461 CD1 TYR A 434 3976 2206 4421 479 167 480 C
ATOM 3462 CE1 TYR A 434 -0.531 -33.019 46.121 1.00 29.93 C
ANISOU 3462 CE1 TYR A 434 4319 1954 5095 604 314 1037 C
ATOM 3463 CZ TYR A 434 0.336 -34.100 46.176 1.00 29.31 C
ANISOU 3463 CZ TYR A 434 4095 2176 4865 658 374 1154 C
ATOM 3464 OH TYR A 434 0.418 -34.841 47.317 1.00 36.88 O
ANISOU 3464 OH TYR A 434 6022 3150 4837 333 -237 1391 O
ATOM 3465 CE2 TYR A 434 1.119 -34.415 45.074 1.00 30.94 C
ANISOU 3465 CE2 TYR A 434 4709 2045 4999 759 340 616 C
ATOM 3466 CD2 TYR A 434 1.036 -33.640 43.926 1.00 28.33 C
ANISOU 3466 CD2 TYR A 434 3844 2163 4758 1001 552 486 C
ATOM 3467 C TYR A 434 -0.103 -29.394 43.511 1.00 19.86 C
ANISOU 3467 C TYR A 434 2929 2079 2536 555 -18 226 C
ATOM 3468 O TYR A 434 -1.192 -29.013 43.067 1.00 21.69 O
ANISOU 3468 O TYR A 434 3200 2228 2812 682 -350 -93 O
ATOM 3469 N ASN A 435 0.366 -28.981 44.699 1.00 17.99 N
ANISOU 3469 N ASN A 435 2488 2009 2335 513 -45 439 N
ATOM 3470 CA ASN A 435 -0.401 -28.002 45.511 1.00 18.32 C
ANISOU 3470 CA ASN A 435 2500 2131 2330 577 21 489 C
ATOM 3471 CB ASN A 435 0.033 -28.033 46.977 1.00 19.14 C
ANISOU 3471 CB ASN A 435 2569 2388 2313 376 -44 547 C
ATOM 3472 CG ASN A 435 -0.316 -29.339 47.649 1.00 23.46 C
ANISOU 3472 CG ASN A 435 3203 2480 3231 516 105 790 C
ATOM 3473 OD1 ASN A 435 -1.427 -29.830 47.474 1.00 23.84 O
ANISOU 3473 OD1 ASN A 435 3133 2450 3473 711 137 935 O
ATOM 3474 ND2 ASN A 435 0.607 -29.883 48.425 1.00 30.26 N
ANISOU 3474 ND2 ASN A 435 4119 3640 3738 997 -250 1089 N
ATOM 3475 C ASN A 435 -0.261 -26.568 44.985 1.00 17.30 C
ANISOU 3475 C ASN A 435 2456 2160 1955 562 35 411 C
ATOM 3476 O ASN A 435 -1.053 -25.701 45.372 1.00 17.59 O
ANISOU 3476 O ASN A 435 2611 1996 2075 564 31 482 O
ATOM 3477 N VAL A 436 0.746 -26.307 44.146 1.00 15.95 N
ANISOU 3477 N VAL A 436 2156 1878 2027 766 -90 445 N
ATOM 3478 CA VAL A 436 0.957 -24.984 43.595 1.00 15.65 C
ANISOU 3478 CA VAL A 436 2362 1923 1659 646 -68 348 C
ATOM 3479 CB VAL A 436 2.435 -24.729 43.246 1.00 16.08 C
ANISOU 3479 CB VAL A 436 2343 1994 1771 689 -61 435 C
ATOM 3480 CG1 VAL A 436 2.615 -23.345 42.634 1.00 16.47 C
ANISOU 3480 CG1 VAL A 436 2505 2044 1706 679 57 421 C
ATOM 3481 CG2 VAL A 436 3.342 -24.906 44.453 1.00 17.45 C
ANISOU 3481 CG2 VAL A 436 2414 2216 1998 1009 -112 554 C
ATOM 3482 C VAL A 436 0.028 -24.809 42.388 1.00 15.24 C
ANISOU 3482 C VAL A 436 2238 1824 1728 610 -86 181 C
ATOM 3483 O VAL A 436 0.347 -25.183 41.275 1.00 17.20 O
ANISOU 3483 O VAL A 436 2506 2106 1921 605 181 0 O
ATOM 3484 N MET A 437 -1.148 -24.263 42.683 1.00 14.78 N
ANISOU 3484 N MET A 437 2332 1794 1486 673 13 -111 N
ATOM 3485 CA MET A 437 -2.245 -24.105 41.731 1.00 14.26 C
ANISOU 3485 CA MET A 437 2050 1814 1550 723 84 162 C
ATOM 3486 CB MET A 437 -3.400 -25.069 42.038 1.00 16.98 C
ANISOU 3486 CB MET A 437 2455 1975 2022 540 -94 342 C
ATOM 3487 CG MET A 437 -3.043 -26.530 41.903 1.00 19.22 C
ANISOU 3487 CG MET A 437 2601 2043 2656 687 1 425 C
ATOM 3488 SD MET A 437 -4.399 -27.616 42.408 1.00 22.91 S
ANISOU 3488 SD MET A 437 3198 2233 3274 345 68 403 S
ATOM 3489 CE MET A 437 -5.497 -27.418 41.014 1.00 25.94 C
ANISOU 3489 CE MET A 437 3524 2826 3506 676 -281 119 C
ATOM 3490 C MET A 437 -2.757 -22.670 41.815 1.00 14.43 C
ANISOU 3490 C MET A 437 2230 1767 1484 649 70 -20 C
ATOM 3491 O MET A 437 -2.831 -22.093 42.905 1.00 14.90 O
ANISOU 3491 O MET A 437 2326 1898 1435 600 78 37 O
ATOM 3492 N ALA A 438 -3.192 -22.115 40.678 1.00 13.19 N
ANISOU 3492 N ALA A 438 2020 1615 1374 447 158 -126 N
ATOM 3493 CA ALA A 438 -3.796 -20.789 40.669 1.00 12.91 C
ANISOU 3493 CA ALA A 438 1762 1543 1597 346 17 44 C
ATOM 3494 CB ALA A 438 -4.354 -20.488 39.305 1.00 14.45 C
ANISOU 3494 CB ALA A 438 2027 1752 1710 460 -38 103 C
ATOM 3495 C ALA A 438 -4.892 -20.722 41.733 1.00 12.97 C
ANISOU 3495 C ALA A 438 2023 1598 1307 340 -16 102 C
ATOM 3496 O ALA A 438 -5.758 -21.607 41.799 1.00 14.01 O
ANISOU 3496 O ALA A 438 2211 1677 1433 330 93 215 O
ATOM 3497 N ASN A 439 -4.843 -19.654 42.539 1.00 13.06 N
ANISOU 3497 N ASN A 439 2092 1470 1399 310 129 117 N
ATOM 3498 CA ASN A 439 -5.820 -19.331 43.590 1.00 13.82 C
ANISOU 3498 CA ASN A 439 2219 1621 1408 249 157 33 C
ATOM 3499 CB ASN A 439 -7.250 -19.435 43.064 1.00 14.78 C
ANISOU 3499 CB ASN A 439 2302 1847 1464 333 3 -31 C
ATOM 3500 CG ASN A 439 -7.514 -18.412 41.987 1.00 15.22 C
ANISOU 3500 CG ASN A 439 2218 1939 1624 480 -46 50 C
ATOM 3501 OD1 ASN A 439 -7.035 -17.285 42.116 1.00 16.21 O
ANISOU 3501 OD1 ASN A 439 2277 2026 1855 369 67 220 O
ATOM 3502 ND2 ASN A 439 -8.277 -18.787 40.964 1.00 15.95 N
ANISOU 3502 ND2 ASN A 439 2245 1930 1884 482 -265 -40 N
ATOM 3503 C ASN A 439 -5.643 -20.191 44.849 1.00 14.99 C
ANISOU 3503 C ASN A 439 2387 1665 1642 366 134 167 C
ATOM 3504 O ASN A 439 -6.474 -20.102 45.778 1.00 16.85 O
ANISOU 3504 O ASN A 439 2854 1801 1745 373 482 430 O
ATOM 3505 N ALA A 440 -4.568 -20.986 44.922 1.00 14.37 N
ANISOU 3505 N ALA A 440 2556 1742 1161 585 163 54 N
ATOM 3506 CA ALA A 440 -4.294 -21.713 46.171 1.00 14.91 C
ANISOU 3506 CA ALA A 440 2479 1814 1370 396 137 281 C
ATOM 3507 CB ALA A 440 -3.277 -22.793 45.956 1.00 16.35 C
ANISOU 3507 CB ALA A 440 2793 1997 1421 535 92 157 C
ATOM 3508 C ALA A 440 -3.794 -20.722 47.222 1.00 15.99 C
ANISOU 3508 C ALA A 440 2528 2011 1535 498 116 15 C
ATOM 3509 O ALA A 440 -2.946 -19.864 46.922 1.00 17.38 O
ANISOU 3509 O ALA A 440 2634 2312 1655 501 388 197 O
ATOM 3510 N ASN A 441 -4.263 -20.895 48.460 1.00 17.42 N
ANISOU 3510 N ASN A 441 2779 2072 1765 498 420 142 N
ATOM 3511 CA AASN A 441 -3.819 -20.078 49.591 0.50 18.50 C
ANISOU 3511 CA AASN A 441 2796 2526 1705 559 154 119 C
ATOM 3512 CA BASN A 441 -3.834 -20.089 49.612 0.50 18.34 C
ANISOU 3512 CA BASN A 441 2815 2399 1752 475 117 208 C
ATOM 3513 CB AASN A 441 -4.898 -19.938 50.657 0.50 19.86 C
ANISOU 3513 CB AASN A 441 2965 2806 1776 580 234 -187 C
ATOM 3514 CB BASN A 441 -4.934 -19.988 50.675 0.50 19.60 C
ANISOU 3514 CB BASN A 441 2957 2570 1919 437 236 9 C
ATOM 3515 CG AASN A 441 -4.507 -18.893 51.678 0.50 23.91 C
ANISOU 3515 CG AASN A 441 3555 3467 2060 560 211 -678 C
ATOM 3516 CG BASN A 441 -5.204 -21.278 51.430 0.50 22.96 C
ANISOU 3516 CG BASN A 441 3606 2866 2251 28 210 138 C
ATOM 3517 OD1AASN A 441 -3.586 -18.106 51.435 0.50 26.89 O
ANISOU 3517 OD1AASN A 441 3518 4246 2452 602 177 -848 O
ATOM 3518 OD1BASN A 441 -4.810 -22.348 50.990 0.50 22.38 O
ANISOU 3518 OD1BASN A 441 3269 3038 2196 -61 241 76 O
ATOM 3519 ND2AASN A 441 -5.191 -18.885 52.808 0.50 27.87 N
ANISOU 3519 ND2AASN A 441 3964 4397 2228 271 408 -232 N
ATOM 3520 ND2BASN A 441 -5.845 -21.192 52.589 0.50 28.81 N
ANISOU 3520 ND2BASN A 441 3977 3997 2971 410 647 -164 N
ATOM 3521 C ASN A 441 -2.538 -20.669 50.199 1.00 19.48 C
ANISOU 3521 C ASN A 441 2730 2907 1761 595 286 313 C
ATOM 3522 O ASN A 441 -2.402 -20.809 51.398 1.00 27.65 O
ANISOU 3522 O ASN A 441 3652 4914 1937 1084 263 432 O
ATOM 3523 N LYS A 442 -1.589 -20.989 49.340 1.00 19.36 N
ANISOU 3523 N LYS A 442 2484 3076 1796 554 188 218 N
ATOM 3524 CA LYS A 442 -0.340 -21.597 49.710 1.00 19.71 C
ANISOU 3524 CA LYS A 442 2765 2590 2133 519 34 370 C
ATOM 3525 CB LYS A 442 -0.060 -22.816 48.831 1.00 20.27 C
ANISOU 3525 CB LYS A 442 3163 2427 2110 356 47 458 C
ATOM 3526 CG LYS A 442 1.282 -23.479 49.130 1.00 23.55 C
ANISOU 3526 CG LYS A 442 3349 2940 2656 573 -53 564 C
ATOM 3527 CD LYS A 442 1.604 -24.638 48.226 1.00 25.38 C
ANISOU 3527 CD LYS A 442 3904 2904 2835 771 -194 466 C
ATOM 3528 CE LYS A 442 3.058 -25.043 48.311 1.00 27.07 C
ANISOU 3528 CE LYS A 442 4090 3250 2945 1127 -427 679 C
ATOM 3529 NZ LYS A 442 3.443 -25.512 49.663 1.00 30.69 N
ANISOU 3529 NZ LYS A 442 4938 3805 2914 975 -508 760 N
ATOM 3530 C LYS A 442 0.778 -20.581 49.464 1.00 19.17 C
ANISOU 3530 C LYS A 442 2960 2635 1686 404 7 311 C
ATOM 3531 O LYS A 442 0.845 -20.013 48.375 1.00 20.47 O
ANISOU 3531 O LYS A 442 3388 2772 1615 728 176 318 O
ATOM 3532 N SER A 443 1.623 -20.358 50.481 1.00 20.56 N
ANISOU 3532 N SER A 443 3161 2996 1655 351 -177 198 N
ATOM 3533 CA ASER A 443 2.781 -19.483 50.341 0.50 21.29 C
ANISOU 3533 CA ASER A 443 3072 3133 1882 358 -175 182 C
ATOM 3534 CA BSER A 443 2.777 -19.480 50.335 0.50 22.36 C
ANISOU 3534 CA BSER A 443 3080 3312 2100 361 -100 265 C
ATOM 3535 CB ASER A 443 3.373 -19.145 51.684 0.50 21.88 C
ANISOU 3535 CB ASER A 443 3098 3233 1983 395 -160 -114 C
ATOM 3536 CB BSER A 443 3.358 -19.109 51.675 0.50 25.67 C
ANISOU 3536 CB BSER A 443 3440 3906 2406 219 -356 51 C
ATOM 3537 OG ASER A 443 2.416 -18.493 52.505 0.50 20.55 O
ANISOU 3537 OG ASER A 443 2893 3492 1422 320 -292 -213 O
ATOM 3538 OG BSER A 443 3.837 -20.250 52.359 0.50 28.18 O
ANISOU 3538 OG BSER A 443 3431 4666 2607 554 -425 363 O
ATOM 3539 C SER A 443 3.826 -20.136 49.425 1.00 21.09 C
ANISOU 3539 C SER A 443 3038 3105 1868 272 -179 306 C
ATOM 3540 O SER A 443 4.144 -21.347 49.561 1.00 23.03 O
ANISOU 3540 O SER A 443 3210 3218 2321 609 -84 402 O
ATOM 3541 N ILE A 444 4.385 -19.337 48.511 1.00 19.99 N
ANISOU 3541 N ILE A 444 2514 3112 1966 276 -121 234 N
ATOM 3542 CA ILE A 444 5.475 -19.778 47.652 1.00 18.90 C
ANISOU 3542 CA ILE A 444 2528 2818 1832 345 -137 278 C
ATOM 3543 CB ILE A 444 4.981 -20.113 46.237 1.00 20.22 C
ANISOU 3543 CB ILE A 444 2657 3135 1890 345 -171 156 C
ATOM 3544 CG1 ILE A 444 4.383 -18.896 45.512 1.00 20.59 C
ANISOU 3544 CG1 ILE A 444 2941 3134 1746 352 -180 235 C
ATOM 3545 CG2 ILE A 444 4.038 -21.302 46.281 1.00 21.37 C
ANISOU 3545 CG2 ILE A 444 2864 3363 1889 211 -436 206 C
ATOM 3546 CD1 ILE A 444 4.159 -19.089 44.028 1.00 21.84 C
ANISOU 3546 CD1 ILE A 444 3346 3182 1770 -41 -146 255 C
ATOM 3547 C ILE A 444 6.561 -18.698 47.612 1.00 19.69 C
ANISOU 3547 C ILE A 444 2508 3070 1903 341 -243 67 C
ATOM 3548 O ILE A 444 6.328 -17.533 47.942 1.00 22.77 O
ANISOU 3548 O ILE A 444 2890 3131 2630 544 23 57 O
ATOM 3549 N ASN A 445 7.766 -19.125 47.223 1.00 20.24 N
ANISOU 3549 N ASN A 445 2743 3088 1858 476 -37 35 N
ATOM 3550 CA ASN A 445 8.874 -18.216 46.927 1.00 21.01 C
ANISOU 3550 CA ASN A 445 2991 3077 1914 450 194 322 C
ATOM 3551 CB ASN A 445 10.060 -18.449 47.865 1.00 26.22 C
ANISOU 3551 CB ASN A 445 3874 3950 2136 165 -384 342 C
ATOM 3552 CG ASN A 445 9.735 -18.171 49.320 1.00 31.22 C
ANISOU 3552 CG ASN A 445 5049 4573 2240 330 -684 24 C
ATOM 3553 OD1 ASN A 445 9.336 -17.069 49.674 1.00 40.00 O
ANISOU 3553 OD1 ASN A 445 6293 5123 3781 1044 -1232 -287 O
ATOM 3554 ND2 ASN A 445 9.931 -19.160 50.175 1.00 40.54 N
ANISOU 3554 ND2 ASN A 445 5819 5428 4154 453 -935 1020 N
ATOM 3555 C ASN A 445 9.269 -18.453 45.467 1.00 20.23 C
ANISOU 3555 C ASN A 445 3125 2700 1858 570 86 338 C
ATOM 3556 O ASN A 445 9.365 -19.592 45.047 1.00 22.94 O
ANISOU 3556 O ASN A 445 4195 2703 1818 500 342 298 O
ATOM 3557 N MET A 446 9.445 -17.375 44.693 1.00 18.73 N
ANISOU 3557 N MET A 446 2829 2561 1728 524 -145 208 N
ATOM 3558 CA MET A 446 9.833 -17.477 43.294 1.00 18.80 C
ANISOU 3558 CA MET A 446 2674 2682 1785 524 -43 247 C
ATOM 3559 CB MET A 446 8.687 -17.010 42.377 1.00 19.17 C
ANISOU 3559 CB MET A 446 2420 2783 2077 654 -92 153 C
ATOM 3560 CG MET A 446 8.993 -17.057 40.884 1.00 20.81 C
ANISOU 3560 CG MET A 446 2165 3587 2155 453 -127 112 C
ATOM 3561 SD MET A 446 7.651 -16.418 39.798 1.00 22.98 S
ANISOU 3561 SD MET A 446 2728 3734 2270 545 -313 232 S
ATOM 3562 CE MET A 446 6.612 -17.864 39.873 1.00 22.34 C
ANISOU 3562 CE MET A 446 3274 3114 2098 516 -368 875 C
ATOM 3563 C MET A 446 11.057 -16.601 43.024 1.00 17.70 C
ANISOU 3563 C MET A 446 2282 2648 1793 586 -252 -7 C
ATOM 3564 O MET A 446 11.189 -15.508 43.569 1.00 19.26 O
ANISOU 3564 O MET A 446 2579 2729 2009 527 -141 87 O
ATOM 3565 N GLN A 447 11.929 -17.085 42.136 1.00 16.75 N
ANISOU 3565 N GLN A 447 2467 2409 1486 458 -163 264 N
ATOM 3566 CA GLN A 447 13.031 -16.313 41.610 1.00 16.92 C
ANISOU 3566 CA GLN A 447 2390 2430 1606 414 -219 -21 C
ATOM 3567 CB GLN A 447 14.334 -16.796 42.249 1.00 20.40 C
ANISOU 3567 CB GLN A 447 2294 2919 2536 622 -206 -51 C
ATOM 3568 CG GLN A 447 15.557 -15.938 41.940 1.00 23.75 C
ANISOU 3568 CG GLN A 447 2747 3329 2946 325 -690 609 C
ATOM 3569 CD GLN A 447 16.682 -16.265 42.903 1.00 25.60 C
ANISOU 3569 CD GLN A 447 3288 3458 2977 536 -1091 373 C
ATOM 3570 OE1 GLN A 447 17.018 -17.419 43.116 1.00 30.85 O
ANISOU 3570 OE1 GLN A 447 3959 3635 4127 679 -1657 308 O
ATOM 3571 NE2 GLN A 447 17.283 -15.253 43.505 1.00 28.12 N
ANISOU 3571 NE2 GLN A 447 3268 4236 3180 -102 -853 388 N
ATOM 3572 C GLN A 447 13.013 -16.481 40.093 1.00 18.34 C
ANISOU 3572 C GLN A 447 2725 2605 1636 305 -371 34 C
ATOM 3573 O GLN A 447 12.759 -17.582 39.592 1.00 20.41 O
ANISOU 3573 O GLN A 447 3541 2181 2032 230 88 74 O
ATOM 3574 N VAL A 448 13.268 -15.387 39.382 1.00 17.20 N
ANISOU 3574 N VAL A 448 2286 2478 1769 211 -268 -56 N
ATOM 3575 CA VAL A 448 13.252 -15.379 37.919 1.00 16.64 C
ANISOU 3575 CA VAL A 448 2290 2319 1712 231 -284 0 C
ATOM 3576 CB VAL A 448 12.103 -14.519 37.364 1.00 16.84 C
ANISOU 3576 CB VAL A 448 2242 2443 1710 322 -81 -6 C
ATOM 3577 CG1 VAL A 448 12.182 -14.384 35.839 1.00 17.23 C
ANISOU 3577 CG1 VAL A 448 2256 2594 1695 361 -395 -46 C
ATOM 3578 CG2 VAL A 448 10.764 -15.091 37.803 1.00 16.80 C
ANISOU 3578 CG2 VAL A 448 2334 2497 1550 302 -30 53 C
ATOM 3579 C VAL A 448 14.606 -14.882 37.414 1.00 16.15 C
ANISOU 3579 C VAL A 448 1931 2437 1765 320 -481 -60 C
ATOM 3580 O VAL A 448 15.063 -13.802 37.817 1.00 17.24 O
ANISOU 3580 O VAL A 448 2379 2419 1752 181 -416 -90 O
ATOM 3581 N GLN A 449 15.204 -15.667 36.514 1.00 16.48 N
ANISOU 3581 N GLN A 449 2014 2520 1728 111 -430 -125 N
ATOM 3582 CA GLN A 449 16.435 -15.326 35.808 1.00 17.34 C
ANISOU 3582 CA GLN A 449 2141 2568 1878 402 -248 73 C
ATOM 3583 CB GLN A 449 17.468 -16.449 35.926 1.00 18.89 C
ANISOU 3583 CB GLN A 449 2227 2942 2007 572 -272 31 C
ATOM 3584 CG GLN A 449 18.747 -16.160 35.159 1.00 20.64 C
ANISOU 3584 CG GLN A 449 2298 3270 2273 533 -99 -124 C
ATOM 3585 CD GLN A 449 19.599 -17.393 34.956 1.00 23.29 C
ANISOU 3585 CD GLN A 449 2446 3608 2795 983 -310 256 C
ATOM 3586 OE1 GLN A 449 19.541 -18.042 33.908 1.00 27.00 O
ANISOU 3586 OE1 GLN A 449 3529 3764 2965 1014 87 132 O
ATOM 3587 NE2 GLN A 449 20.365 -17.748 35.968 1.00 25.96 N
ANISOU 3587 NE2 GLN A 449 2277 4541 3045 815 -402 581 N
ATOM 3588 C GLN A 449 16.052 -15.122 34.340 1.00 16.50 C
ANISOU 3588 C GLN A 449 2133 2407 1728 57 -104 -23 C
ATOM 3589 O GLN A 449 15.448 -16.006 33.738 1.00 18.45 O
ANISOU 3589 O GLN A 449 3038 2071 1899 -19 -382 43 O
ATOM 3590 N ALA A 450 16.436 -13.979 33.769 1.00 15.38 N
ANISOU 3590 N ALA A 450 1971 2172 1701 154 -267 -93 N
ATOM 3591 CA ALA A 450 16.200 -13.680 32.349 1.00 15.16 C
ANISOU 3591 CA ALA A 450 1838 2338 1580 245 -240 -171 C
ATOM 3592 CB ALA A 450 15.287 -12.486 32.179 1.00 16.40 C
ANISOU 3592 CB ALA A 450 1916 2416 1898 243 -211 -53 C
ATOM 3593 C ALA A 450 17.543 -13.403 31.688 1.00 14.71 C
ANISOU 3593 C ALA A 450 1738 2093 1755 233 -335 -161 C
ATOM 3594 O ALA A 450 18.365 -12.644 32.246 1.00 15.78 O
ANISOU 3594 O ALA A 450 1631 2728 1633 -70 -198 -160 O
ATOM 3595 N THR A 451 17.749 -14.028 30.518 1.00 14.78 N
ANISOU 3595 N THR A 451 1596 2398 1621 6 -295 -130 N
ATOM 3596 CA THR A 451 18.896 -13.771 29.685 1.00 15.42 C
ANISOU 3596 CA THR A 451 1640 2577 1642 229 -304 -3 C
ATOM 3597 CB THR A 451 19.588 -15.077 29.278 1.00 15.56 C
ANISOU 3597 CB THR A 451 1648 2497 1768 319 -303 151 C
ATOM 3598 OG1 THR A 451 19.884 -15.838 30.451 1.00 17.96 O
ANISOU 3598 OG1 THR A 451 2096 2657 2069 648 -458 311 O
ATOM 3599 CG2 THR A 451 20.838 -14.846 28.466 1.00 16.65 C
ANISOU 3599 CG2 THR A 451 1470 2821 2035 698 -215 65 C
ATOM 3600 C THR A 451 18.372 -12.999 28.469 1.00 14.63 C
ANISOU 3600 C THR A 451 1754 2196 1606 309 -330 -137 C
ATOM 3601 O THR A 451 17.383 -13.412 27.856 1.00 14.73 O
ANISOU 3601 O THR A 451 1666 2285 1645 234 -313 -72 O
ATOM 3602 N PHE A 452 19.035 -11.902 28.099 1.00 14.61 N
ANISOU 3602 N PHE A 452 1683 2326 1542 236 -259 -286 N
ATOM 3603 CA PHE A 452 18.439 -10.996 27.119 1.00 14.50 C
ANISOU 3603 CA PHE A 452 1671 2268 1567 229 -255 -216 C
ATOM 3604 CB PHE A 452 17.471 -10.029 27.807 1.00 14.27 C
ANISOU 3604 CB PHE A 452 1405 2357 1659 56 -217 -215 C
ATOM 3605 CG PHE A 452 18.076 -9.187 28.896 1.00 15.46 C
ANISOU 3605 CG PHE A 452 1674 2535 1662 -3 -253 -221 C
ATOM 3606 CD1 PHE A 452 18.688 -7.984 28.592 1.00 15.91 C
ANISOU 3606 CD1 PHE A 452 1738 2596 1710 70 -388 -28 C
ATOM 3607 CE1 PHE A 452 19.208 -7.199 29.608 1.00 17.04 C
ANISOU 3607 CE1 PHE A 452 1833 2800 1840 -238 -248 -143 C
ATOM 3608 CZ PHE A 452 19.225 -7.652 30.913 1.00 18.39 C
ANISOU 3608 CZ PHE A 452 2106 2937 1942 -83 -194 -13 C
ATOM 3609 CD2 PHE A 452 18.115 -9.643 30.207 1.00 16.13 C
ANISOU 3609 CD2 PHE A 452 1935 2455 1739 -2 -293 -60 C
ATOM 3610 CE2 PHE A 452 18.646 -8.857 31.222 1.00 16.69 C
ANISOU 3610 CE2 PHE A 452 1820 2933 1587 -37 -236 -67 C
ATOM 3611 C PHE A 452 19.519 -10.237 26.347 1.00 15.56 C
ANISOU 3611 C PHE A 452 1633 2372 1905 156 -299 -71 C
ATOM 3612 O PHE A 452 20.663 -10.112 26.795 1.00 15.72 O
ANISOU 3612 O PHE A 452 1507 2398 2068 94 -131 -141 O
ATOM 3613 N VAL A 453 19.106 -9.717 25.176 1.00 14.66 N
ANISOU 3613 N VAL A 453 1362 2369 1837 18 -307 -98 N
ATOM 3614 CA VAL A 453 19.941 -8.911 24.321 1.00 16.39 C
ANISOU 3614 CA VAL A 453 1708 2515 2002 -15 3 -168 C
ATOM 3615 CB VAL A 453 20.128 -9.531 22.928 1.00 15.75 C
ANISOU 3615 CB VAL A 453 1925 2256 1804 -66 -6 -21 C
ATOM 3616 CG1 VAL A 453 20.867 -10.863 23.015 1.00 16.51 C
ANISOU 3616 CG1 VAL A 453 2103 2395 1775 0 46 -85 C
ATOM 3617 CG2 VAL A 453 18.823 -9.680 22.157 1.00 16.43 C
ANISOU 3617 CG2 VAL A 453 2035 2341 1863 -100 41 -118 C
ATOM 3618 C VAL A 453 19.362 -7.495 24.235 1.00 15.99 C
ANISOU 3618 C VAL A 453 1796 2277 2000 -308 -39 -120 C
ATOM 3619 O VAL A 453 18.127 -7.305 24.313 1.00 17.16 O
ANISOU 3619 O VAL A 453 1844 2456 2221 -361 74 -255 O
ATOM 3620 N THR A 454 20.280 -6.516 24.114 1.00 14.73 N
ANISOU 3620 N THR A 454 1505 2041 2047 -129 -22 -286 N
ATOM 3621 CA THR A 454 19.911 -5.107 24.129 1.00 15.35 C
ANISOU 3621 CA THR A 454 1865 2106 1858 -154 -140 -174 C
ATOM 3622 CB THR A 454 20.526 -4.427 25.359 1.00 16.60 C
ANISOU 3622 CB THR A 454 1927 2416 1961 -235 -391 -129 C
ATOM 3623 OG1 THR A 454 21.939 -4.635 25.266 1.00 17.52 O
ANISOU 3623 OG1 THR A 454 1852 2750 2051 -301 -424 -19 O
ATOM 3624 CG2 THR A 454 19.973 -4.984 26.652 1.00 18.41 C
ANISOU 3624 CG2 THR A 454 2161 2776 2056 -402 -388 -27 C
ATOM 3625 C THR A 454 20.403 -4.413 22.863 1.00 14.67 C
ANISOU 3625 C THR A 454 1502 2215 1855 -112 -90 -285 C
ATOM 3626 O THR A 454 21.344 -4.840 22.222 1.00 16.39 O
ANISOU 3626 O THR A 454 1739 2207 2281 5 78 -383 O
ATOM 3627 N PRO A 455 19.737 -3.322 22.448 1.00 16.45 N
ANISOU 3627 N PRO A 455 1688 2510 2049 85 -11 -84 N
ATOM 3628 CA PRO A 455 20.074 -2.679 21.178 1.00 17.43 C
ANISOU 3628 CA PRO A 455 1871 2534 2216 -118 53 -5 C
ATOM 3629 CB PRO A 455 18.732 -2.020 20.825 1.00 17.42 C
ANISOU 3629 CB PRO A 455 1947 2550 2119 -103 -115 140 C
ATOM 3630 CG PRO A 455 18.186 -1.616 22.179 1.00 18.43 C
ANISOU 3630 CG PRO A 455 2022 2607 2370 44 46 -55 C
ATOM 3631 CD PRO A 455 18.483 -2.811 23.054 1.00 17.14 C
ANISOU 3631 CD PRO A 455 1598 2810 2105 18 -26 -62 C
ATOM 3632 C PRO A 455 21.219 -1.652 21.165 1.00 17.81 C
ANISOU 3632 C PRO A 455 2011 2510 2245 -223 -117 -113 C
ATOM 3633 O PRO A 455 21.513 -1.091 20.119 1.00 20.75 O
ANISOU 3633 O PRO A 455 2477 3024 2381 -168 14 46 O
ATOM 3634 N GLU A 456 21.891 -1.427 22.294 1.00 18.75 N
ANISOU 3634 N GLU A 456 2071 2609 2442 -357 -159 -134 N
ATOM 3635 CA GLU A 456 22.933 -0.395 22.342 1.00 20.18 C
ANISOU 3635 CA GLU A 456 2275 2937 2452 -475 -7 -245 C
ATOM 3636 CB GLU A 456 23.344 -0.129 23.792 1.00 21.30 C
ANISOU 3636 CB GLU A 456 2428 3226 2439 -490 -201 -154 C
ATOM 3637 CG GLU A 456 22.402 0.823 24.506 1.00 23.44 C
ANISOU 3637 CG GLU A 456 3019 3083 2801 -453 -134 -298 C
ATOM 3638 CD GLU A 456 21.064 0.216 24.875 1.00 23.53 C
ANISOU 3638 CD GLU A 456 2880 3531 2526 -510 -179 -664 C
ATOM 3639 OE1 GLU A 456 21.029 -0.989 25.161 1.00 23.08 O
ANISOU 3639 OE1 GLU A 456 2674 3618 2478 -747 -79 -524 O
ATOM 3640 OE2 GLU A 456 20.060 0.954 24.867 1.00 26.70 O
ANISOU 3640 OE2 GLU A 456 3107 3501 3535 -503 -540 -316 O
ATOM 3641 C GLU A 456 24.148 -0.794 21.493 1.00 18.95 C
ANISOU 3641 C GLU A 456 1967 2755 2477 -454 -136 -71 C
ATOM 3642 O GLU A 456 24.485 -1.981 21.340 1.00 19.12 O
ANISOU 3642 O GLU A 456 2206 2648 2410 -426 -215 -215 O
ATOM 3643 N ALA A 457 24.794 0.231 20.927 1.00 20.44 N
ANISOU 3643 N ALA A 457 2258 2854 2652 -615 139 -134 N
ATOM 3644 CA ALA A 457 25.979 0.074 20.117 1.00 20.15 C
ANISOU 3644 CA ALA A 457 2261 3027 2367 -628 94 -129 C
ATOM 3645 CB ALA A 457 26.435 1.420 19.611 1.00 21.25 C
ANISOU 3645 CB ALA A 457 2281 3122 2669 -673 144 -46 C
ATOM 3646 C ALA A 457 27.104 -0.578 20.926 1.00 21.77 C
ANISOU 3646 C ALA A 457 2099 3314 2859 -611 118 39 C
ATOM 3647 O ALA A 457 27.209 -0.383 22.146 1.00 23.27 O
ANISOU 3647 O ALA A 457 2504 3334 3003 -721 -192 -168 O
ATOM 3648 N ALA A 458 27.972 -1.305 20.219 1.00 21.66 N
ANISOU 3648 N ALA A 458 1947 3545 2737 -576 -42 -248 N
ATOM 3649 CA ALA A 458 29.242 -1.772 20.797 1.00 22.56 C
ANISOU 3649 CA ALA A 458 1736 3791 3042 -632 128 -269 C
ATOM 3650 CB ALA A 458 30.099 -2.437 19.737 1.00 23.88 C
ANISOU 3650 CB ALA A 458 1855 3950 3268 -415 206 -390 C
ATOM 3651 C ALA A 458 29.983 -0.576 21.400 1.00 23.95 C
ANISOU 3651 C ALA A 458 2171 3750 3177 -721 -161 -255 C
ATOM 3652 O ALA A 458 30.098 0.503 20.775 1.00 26.61 O
ANISOU 3652 O ALA A 458 2554 4279 3276 -1334 -122 159 O
ATOM 3653 N GLY A 459 30.485 -0.776 22.614 1.00 24.58 N
ANISOU 3653 N GLY A 459 2256 3946 3134 -1153 -78 -51 N
ATOM 3654 CA GLY A 459 31.247 0.233 23.321 1.00 25.32 C
ANISOU 3654 CA GLY A 459 2059 4214 3344 -979 -258 -386 C
ATOM 3655 C GLY A 459 30.381 1.191 24.123 1.00 23.91 C
ANISOU 3655 C GLY A 459 2313 3780 2991 -1148 -348 -488 C
ATOM 3656 O GLY A 459 30.904 2.149 24.674 1.00 28.53 O
ANISOU 3656 O GLY A 459 2730 4387 3724 -1435 -260 -1163 O
ATOM 3657 N THR A 460 29.065 0.949 24.149 1.00 25.96 N
ANISOU 3657 N THR A 460 2270 3950 3644 -996 -268 -572 N
ATOM 3658 CA THR A 460 28.096 1.736 24.928 1.00 23.81 C
ANISOU 3658 CA THR A 460 2226 3391 3427 -1292 -172 -264 C
ATOM 3659 CB THR A 460 27.214 2.623 24.035 1.00 25.16 C
ANISOU 3659 CB THR A 460 2548 3823 3186 -1088 -247 -369 C
ATOM 3660 OG1 THR A 460 26.241 1.808 23.368 1.00 24.76 O
ANISOU 3660 OG1 THR A 460 2607 3306 3494 -1099 -124 -196 O
ATOM 3661 CG2 THR A 460 28.040 3.416 23.042 1.00 28.76 C
ANISOU 3661 CG2 THR A 460 3165 4340 3421 -1288 -270 -129 C
ATOM 3662 C THR A 460 27.227 0.784 25.754 1.00 23.11 C
ANISOU 3662 C THR A 460 2198 3379 3201 -898 68 -271 C
ATOM 3663 O THR A 460 27.256 -0.423 25.594 1.00 25.79 O
ANISOU 3663 O THR A 460 2761 3381 3656 -767 -187 -174 O
ATOM 3664 N GLY A 461 26.441 1.370 26.643 1.00 23.70 N
ANISOU 3664 N GLY A 461 2610 3532 2863 -791 267 -253 N
ATOM 3665 CA GLY A 461 25.504 0.616 27.417 1.00 24.51 C
ANISOU 3665 CA GLY A 461 2574 3609 3128 -775 91 -160 C
ATOM 3666 C GLY A 461 24.396 1.493 27.946 1.00 23.61 C
ANISOU 3666 C GLY A 461 2657 3497 2816 -744 213 -125 C
ATOM 3667 O GLY A 461 24.347 2.693 27.685 1.00 28.28 O
ANISOU 3667 O GLY A 461 3209 3357 4176 -805 550 -245 O
ATOM 3668 N ALA A 462 23.494 0.863 28.691 1.00 20.99 N
ANISOU 3668 N ALA A 462 2635 2986 2353 -735 76 -172 N
ATOM 3669 CA ALA A 462 22.373 1.536 29.301 1.00 21.64 C
ANISOU 3669 CA ALA A 462 2636 3208 2375 -639 12 -396 C
ATOM 3670 CB ALA A 462 21.335 1.854 28.261 1.00 23.30 C
ANISOU 3670 CB ALA A 462 2877 3442 2534 -586 113 27 C
ATOM 3671 C ALA A 462 21.793 0.628 30.383 1.00 20.15 C
ANISOU 3671 C ALA A 462 2607 2861 2187 -594 -192 -457 C
ATOM 3672 O ALA A 462 22.034 -0.577 30.385 1.00 19.91 O
ANISOU 3672 O ALA A 462 2166 2935 2462 -574 -260 -561 O
ATOM 3673 N HIS A 463 21.018 1.217 31.296 1.00 19.82 N
ANISOU 3673 N HIS A 463 2570 2601 2356 -709 -89 -470 N
ATOM 3674 CA HIS A 463 20.381 0.475 32.348 1.00 20.12 C
ANISOU 3674 CA HIS A 463 2494 2915 2233 -862 -324 -431 C
ATOM 3675 CB HIS A 463 20.073 1.393 33.529 1.00 22.70 C
ANISOU 3675 CB HIS A 463 2939 3515 2169 -928 -324 -684 C
ATOM 3676 CG HIS A 463 21.258 1.773 34.357 1.00 25.84 C
ANISOU 3676 CG HIS A 463 2871 4309 2635 -873 -451 -816 C
ATOM 3677 ND1 HIS A 463 21.997 2.910 34.116 1.00 29.93 N
ANISOU 3677 ND1 HIS A 463 3381 4724 3265 -1097 -319 -763 N
ATOM 3678 CE1 HIS A 463 22.961 3.015 35.012 1.00 31.05 C
ANISOU 3678 CE1 HIS A 463 3962 4459 3378 -1235 -628 -933 C
ATOM 3679 NE2 HIS A 463 22.864 1.961 35.841 1.00 31.25 N
ANISOU 3679 NE2 HIS A 463 3767 4931 3176 -1044 -523 -975 N
ATOM 3680 CD2 HIS A 463 21.815 1.175 35.427 1.00 28.91 C
ANISOU 3680 CD2 HIS A 463 3382 4854 2746 -904 -478 -722 C
ATOM 3681 C HIS A 463 19.092 -0.199 31.848 1.00 18.00 C
ANISOU 3681 C HIS A 463 2244 2954 1639 -426 -456 -555 C
ATOM 3682 O HIS A 463 18.256 0.427 31.161 1.00 18.80 O
ANISOU 3682 O HIS A 463 2188 2903 2050 -512 -578 -365 O
ATOM 3683 N TYR A 464 18.935 -1.464 32.242 1.00 18.60 N
ANISOU 3683 N TYR A 464 2172 2941 1952 -339 -560 -532 N
ATOM 3684 CA TYR A 464 17.767 -2.297 31.978 1.00 17.41 C
ANISOU 3684 CA TYR A 464 2140 2870 1604 -388 -380 -457 C
ATOM 3685 CB TYR A 464 18.057 -3.428 30.975 1.00 17.52 C
ANISOU 3685 CB TYR A 464 2192 2775 1689 -522 -508 -476 C
ATOM 3686 CG TYR A 464 18.134 -2.910 29.564 1.00 17.94 C
ANISOU 3686 CG TYR A 464 2495 2619 1700 -829 -337 -405 C
ATOM 3687 CD1 TYR A 464 19.249 -2.209 29.121 1.00 19.39 C
ANISOU 3687 CD1 TYR A 464 2372 3076 1918 -724 -190 -590 C
ATOM 3688 CE1 TYR A 464 19.291 -1.643 27.859 1.00 18.89 C
ANISOU 3688 CE1 TYR A 464 2165 2885 2125 -697 43 -252 C
ATOM 3689 CZ TYR A 464 18.194 -1.735 27.022 1.00 19.03 C
ANISOU 3689 CZ TYR A 464 2404 2741 2085 -582 -62 -315 C
ATOM 3690 OH TYR A 464 18.228 -1.163 25.787 1.00 20.94 O
ANISOU 3690 OH TYR A 464 2914 3029 2014 -704 -78 -198 O
ATOM 3691 CE2 TYR A 464 17.079 -2.430 27.441 1.00 18.26 C
ANISOU 3691 CE2 TYR A 464 2494 2523 1920 -638 -237 -190 C
ATOM 3692 CD2 TYR A 464 17.054 -3.000 28.704 1.00 17.83 C
ANISOU 3692 CD2 TYR A 464 2374 2622 1779 -687 -287 -376 C
ATOM 3693 C TYR A 464 17.246 -2.839 33.315 1.00 17.20 C
ANISOU 3693 C TYR A 464 2029 2922 1582 -325 -453 -354 C
ATOM 3694 O TYR A 464 18.021 -3.162 34.215 1.00 17.68 O
ANISOU 3694 O TYR A 464 2279 2656 1783 -110 -528 -289 O
ATOM 3695 N LYS A 465 15.921 -2.954 33.395 1.00 17.09 N
ANISOU 3695 N LYS A 465 2024 2649 1819 -366 -439 -344 N
ATOM 3696 CA ALYS A 465 15.228 -3.413 34.582 0.30 16.65 C
ANISOU 3696 CA ALYS A 465 2122 2553 1651 -223 -410 -391 C
ATOM 3697 CA BLYS A 465 15.229 -3.414 34.580 0.70 16.93 C
ANISOU 3697 CA BLYS A 465 2208 2621 1600 -253 -416 -418 C
ATOM 3698 CB ALYS A 465 14.353 -2.292 35.142 0.30 17.27 C
ANISOU 3698 CB ALYS A 465 2210 2540 1810 -190 -321 -424 C
ATOM 3699 CB BLYS A 465 14.338 -2.303 35.134 0.70 19.66 C
ANISOU 3699 CB BLYS A 465 2568 2796 2103 -65 -155 -523 C
ATOM 3700 CG ALYS A 465 13.568 -2.643 36.395 0.30 17.38 C
ANISOU 3700 CG ALYS A 465 2136 2518 1946 -225 -259 -453 C
ATOM 3701 CG BLYS A 465 13.567 -2.662 36.395 0.70 21.85 C
ANISOU 3701 CG BLYS A 465 2634 3120 2546 -210 81 -485 C
ATOM 3702 CD ALYS A 465 12.907 -1.421 36.993 0.30 18.24 C
ANISOU 3702 CD ALYS A 465 2232 2579 2118 -201 -68 -482 C
ATOM 3703 CD BLYS A 465 12.546 -1.624 36.782 0.70 25.76 C
ANISOU 3703 CD BLYS A 465 3089 3543 3153 3 687 -541 C
ATOM 3704 CE ALYS A 465 12.043 -0.692 35.982 0.30 18.24 C
ANISOU 3704 CE ALYS A 465 2201 2541 2188 -201 -50 -447 C
ATOM 3705 CE BLYS A 465 13.149 -0.350 37.322 0.70 27.53 C
ANISOU 3705 CE BLYS A 465 3371 3640 3447 -79 781 -704 C
ATOM 3706 NZ ALYS A 465 11.310 0.434 36.606 0.30 19.37 N
ANISOU 3706 NZ ALYS A 465 2547 2560 2251 -238 24 -568 N
ATOM 3707 NZ BLYS A 465 12.146 0.431 38.075 0.70 31.37 N
ANISOU 3707 NZ BLYS A 465 4092 4178 3645 402 1009 -709 N
ATOM 3708 C LYS A 465 14.361 -4.631 34.248 1.00 16.66 C
ANISOU 3708 C LYS A 465 2263 2453 1612 -235 -334 -320 C
ATOM 3709 O LYS A 465 13.438 -4.548 33.423 1.00 17.29 O
ANISOU 3709 O LYS A 465 2190 2703 1675 -264 -380 -406 O
ATOM 3710 N LEU A 466 14.674 -5.748 34.909 1.00 15.63 N
ANISOU 3710 N LEU A 466 1984 2445 1509 -247 -300 -157 N
ATOM 3711 CA LEU A 466 13.827 -6.944 34.890 1.00 15.28 C
ANISOU 3711 CA LEU A 466 1843 2370 1592 -204 -239 -158 C
ATOM 3712 CB LEU A 466 14.662 -8.170 35.281 1.00 16.25 C
ANISOU 3712 CB LEU A 466 1990 2451 1732 -151 -360 -22 C
ATOM 3713 CG LEU A 466 13.895 -9.449 35.628 1.00 15.70 C
ANISOU 3713 CG LEU A 466 1549 2641 1773 -192 -295 -55 C
ATOM 3714 CD1 LEU A 466 13.093 -9.968 34.446 1.00 16.70 C
ANISOU 3714 CD1 LEU A 466 2035 2448 1861 -163 -446 -50 C
ATOM 3715 CD2 LEU A 466 14.836 -10.532 36.130 1.00 17.50 C
ANISOU 3715 CD2 LEU A 466 1716 3020 1914 -198 -639 -30 C
ATOM 3716 C LEU A 466 12.675 -6.716 35.857 1.00 15.34 C
ANISOU 3716 C LEU A 466 1764 2435 1629 -313 -331 -177 C
ATOM 3717 O LEU A 466 12.909 -6.400 37.036 1.00 16.21 O
ANISOU 3717 O LEU A 466 1721 2823 1614 -98 -368 -184 O
ATOM 3718 N GLU A 467 11.447 -6.887 35.341 1.00 15.17 N
ANISOU 3718 N GLU A 467 1683 2390 1688 -215 -351 103 N
ATOM 3719 CA GLU A 467 10.233 -6.778 36.137 1.00 15.41 C
ANISOU 3719 CA GLU A 467 1806 2357 1690 -174 -430 -155 C
ATOM 3720 CB GLU A 467 9.372 -5.614 35.655 1.00 17.66 C
ANISOU 3720 CB GLU A 467 1970 2437 2302 -158 -674 -56 C
ATOM 3721 CG GLU A 467 9.941 -4.246 35.994 1.00 20.71 C
ANISOU 3721 CG GLU A 467 2389 2570 2907 -295 -769 107 C
ATOM 3722 CD GLU A 467 9.034 -3.099 35.586 1.00 23.50 C
ANISOU 3722 CD GLU A 467 3132 2554 3242 84 -820 -155 C
ATOM 3723 OE1 GLU A 467 8.762 -3.001 34.395 1.00 26.13 O
ANISOU 3723 OE1 GLU A 467 3540 3060 3326 -48 -892 183 O
ATOM 3724 OE2 GLU A 467 8.564 -2.321 36.480 1.00 27.50 O
ANISOU 3724 OE2 GLU A 467 3415 3384 3647 250 -366 -322 O
ATOM 3725 C GLU A 467 9.459 -8.088 36.026 1.00 14.67 C
ANISOU 3725 C GLU A 467 1844 2143 1587 15 -259 -170 C
ATOM 3726 O GLU A 467 9.297 -8.613 34.915 1.00 15.34 O
ANISOU 3726 O GLU A 467 2094 2387 1346 -39 -116 -83 O
ATOM 3727 N VAL A 468 8.971 -8.572 37.169 1.00 14.09 N
ANISOU 3727 N VAL A 468 1799 2053 1499 38 -218 -222 N
ATOM 3728 CA VAL A 468 8.051 -9.710 37.219 1.00 13.78 C
ANISOU 3728 CA VAL A 468 1741 2029 1465 177 -299 -141 C
ATOM 3729 CB VAL A 468 8.637 -10.890 38.004 1.00 14.79 C
ANISOU 3729 CB VAL A 468 1955 2044 1621 240 -245 -112 C
ATOM 3730 CG1 VAL A 468 7.641 -12.044 38.050 1.00 15.90 C
ANISOU 3730 CG1 VAL A 468 2082 2194 1764 86 -240 71 C
ATOM 3731 CG2 VAL A 468 9.962 -11.303 37.408 1.00 15.68 C
ANISOU 3731 CG2 VAL A 468 1969 2460 1528 335 -280 -142 C
ATOM 3732 C VAL A 468 6.744 -9.221 37.839 1.00 13.87 C
ANISOU 3732 C VAL A 468 1789 1966 1513 231 -180 -153 C
ATOM 3733 O VAL A 468 6.735 -8.752 38.979 1.00 16.26 O
ANISOU 3733 O VAL A 468 2165 2452 1561 357 -111 -248 O
ATOM 3734 N PHE A 469 5.669 -9.307 37.055 1.00 13.68 N
ANISOU 3734 N PHE A 469 1962 1831 1404 285 -203 -81 N
ATOM 3735 CA PHE A 469 4.331 -8.951 37.503 1.00 13.95 C
ANISOU 3735 CA PHE A 469 1821 1918 1559 278 -281 -120 C
ATOM 3736 CB PHE A 469 3.589 -8.156 36.433 1.00 14.02 C
ANISOU 3736 CB PHE A 469 1611 2034 1682 319 -393 -122 C
ATOM 3737 CG PHE A 469 4.264 -6.860 36.076 1.00 15.68 C
ANISOU 3737 CG PHE A 469 1898 2075 1985 280 -184 1 C
ATOM 3738 CD1 PHE A 469 5.236 -6.819 35.089 1.00 16.31 C
ANISOU 3738 CD1 PHE A 469 2153 1967 2077 82 -25 -22 C
ATOM 3739 CE1 PHE A 469 5.860 -5.629 34.760 1.00 18.11 C
ANISOU 3739 CE1 PHE A 469 2278 2240 2363 -55 -229 175 C
ATOM 3740 CZ PHE A 469 5.533 -4.481 35.443 1.00 19.38 C
ANISOU 3740 CZ PHE A 469 2480 2222 2658 -281 -255 -22 C
ATOM 3741 CD2 PHE A 469 3.947 -5.695 36.752 1.00 17.18 C
ANISOU 3741 CD2 PHE A 469 2430 1995 2100 277 -182 50 C
ATOM 3742 CE2 PHE A 469 4.572 -4.502 36.428 1.00 18.11 C
ANISOU 3742 CE2 PHE A 469 2459 2106 2313 90 -325 96 C
ATOM 3743 C PHE A 469 3.496 -10.198 37.781 1.00 13.62 C
ANISOU 3743 C PHE A 469 1925 1815 1434 282 -261 -99 C
ATOM 3744 O PHE A 469 3.682 -11.218 37.126 1.00 14.34 O
ANISOU 3744 O PHE A 469 2042 1802 1605 77 -112 -244 O
ATOM 3745 N SER A 470 2.605 -10.089 38.762 1.00 14.46 N
ANISOU 3745 N SER A 470 1749 1902 1841 187 -138 -496 N
ATOM 3746 CA SER A 470 1.558 -11.067 38.996 1.00 15.04 C
ANISOU 3746 CA SER A 470 1902 1918 1894 253 173 -267 C
ATOM 3747 CB SER A 470 1.463 -11.491 40.428 1.00 17.55 C
ANISOU 3747 CB SER A 470 2033 2451 2183 228 6 123 C
ATOM 3748 OG SER A 470 1.161 -10.381 41.250 1.00 19.21 O
ANISOU 3748 OG SER A 470 2738 2611 1949 546 156 300 O
ATOM 3749 C SER A 470 0.221 -10.493 38.535 1.00 13.82 C
ANISOU 3749 C SER A 470 1910 1664 1674 153 124 -179 C
ATOM 3750 O SER A 470 -0.068 -9.305 38.693 1.00 14.25 O
ANISOU 3750 O SER A 470 1873 1656 1883 24 102 -359 O
ATOM 3751 N ILE A 471 -0.618 -11.394 38.050 1.00 13.75 N
ANISOU 3751 N ILE A 471 1909 1593 1721 182 25 -258 N
ATOM 3752 CA ILE A 471 -2.007 -11.138 37.735 1.00 14.12 C
ANISOU 3752 CA ILE A 471 1837 1731 1796 166 106 -495 C
ATOM 3753 CB ILE A 471 -2.280 -11.324 36.226 1.00 17.43 C
ANISOU 3753 CB ILE A 471 2583 2179 1861 123 -105 -373 C
ATOM 3754 CG1 ILE A 471 -1.353 -10.417 35.408 1.00 19.19 C
ANISOU 3754 CG1 ILE A 471 3025 2196 2070 -78 -128 -151 C
ATOM 3755 CG2 ILE A 471 -3.744 -11.041 35.921 1.00 22.23 C
ANISOU 3755 CG2 ILE A 471 3029 3236 2180 165 -389 -577 C
ATOM 3756 CD1 ILE A 471 -0.387 -11.120 34.515 1.00 22.44 C
ANISOU 3756 CD1 ILE A 471 2969 2398 3156 1 115 29 C
ATOM 3757 C ILE A 471 -2.828 -12.099 38.591 1.00 15.31 C
ANISOU 3757 C ILE A 471 2208 1559 2048 132 92 -378 C
ATOM 3758 O ILE A 471 -2.751 -13.324 38.394 1.00 16.19 O
ANISOU 3758 O ILE A 471 2245 1530 2373 -70 582 -474 O
ATOM 3759 N ARG A 472 -3.551 -11.559 39.565 1.00 13.75 N
ANISOU 3759 N ARG A 472 2095 1243 1884 153 50 -150 N
ATOM 3760 CA ARG A 472 -4.316 -12.357 40.495 1.00 14.63 C
ANISOU 3760 CA ARG A 472 1969 1527 2062 106 197 -229 C
ATOM 3761 CB ARG A 472 -4.045 -11.954 41.941 1.00 15.17 C
ANISOU 3761 CB ARG A 472 2164 1660 1939 197 73 -131 C
ATOM 3762 CG ARG A 472 -2.696 -12.384 42.483 1.00 15.33 C
ANISOU 3762 CG ARG A 472 2276 1684 1863 303 90 -6 C
ATOM 3763 CD ARG A 472 -2.609 -11.989 43.935 1.00 16.22 C
ANISOU 3763 CD ARG A 472 2501 1738 1920 185 92 -109 C
ATOM 3764 NE ARG A 472 -1.550 -12.701 44.616 1.00 18.08 N
ANISOU 3764 NE ARG A 472 2403 2414 2052 234 -27 -120 N
ATOM 3765 CZ ARG A 472 -0.312 -12.248 44.760 1.00 20.43 C
ANISOU 3765 CZ ARG A 472 2338 2654 2770 348 -297 -34 C
ATOM 3766 NH1 ARG A 472 0.023 -11.092 44.209 1.00 22.36 N
ANISOU 3766 NH1 ARG A 472 2859 2916 2720 -81 97 -174 N
ATOM 3767 NH2 ARG A 472 0.587 -12.981 45.402 1.00 22.60 N
ANISOU 3767 NH2 ARG A 472 2791 3116 2677 575 -457 114 N
ATOM 3768 C ARG A 472 -5.818 -12.200 40.249 1.00 14.56 C
ANISOU 3768 C ARG A 472 1948 1476 2108 303 252 -189 C
ATOM 3769 O ARG A 472 -6.341 -11.123 39.951 1.00 15.79 O
ANISOU 3769 O ARG A 472 2165 1471 2360 288 311 -51 O
ATOM 3770 N ASP A 473 -6.504 -13.325 40.381 1.00 14.83 N
ANISOU 3770 N ASP A 473 2040 1409 2184 267 310 -208 N
ATOM 3771 CA ASP A 473 -7.956 -13.383 40.323 1.00 15.46 C
ANISOU 3771 CA ASP A 473 2091 1836 1945 371 215 -85 C
ATOM 3772 CB ASP A 473 -8.431 -14.824 40.184 1.00 16.01 C
ANISOU 3772 CB ASP A 473 2307 1808 1967 236 227 -62 C
ATOM 3773 CG ASP A 473 -7.946 -15.548 38.916 1.00 17.43 C
ANISOU 3773 CG ASP A 473 2606 1890 2126 423 236 -141 C
ATOM 3774 OD1 ASP A 473 -7.536 -14.871 37.933 1.00 20.35 O
ANISOU 3774 OD1 ASP A 473 3002 2239 2489 7 322 -86 O
ATOM 3775 OD2 ASP A 473 -8.008 -16.801 38.898 1.00 17.95 O
ANISOU 3775 OD2 ASP A 473 2825 1929 2066 394 -50 93 O
ATOM 3776 C ASP A 473 -8.490 -12.687 41.579 1.00 15.05 C
ANISOU 3776 C ASP A 473 2084 1739 1893 318 233 -11 C
ATOM 3777 O ASP A 473 -8.087 -12.980 42.698 1.00 16.43 O
ANISOU 3777 O ASP A 473 2520 2012 1708 357 216 -202 O
ATOM 3778 N ASN A 474 -9.376 -11.723 41.361 1.00 14.25 N
ANISOU 3778 N ASN A 474 2037 1912 1463 457 133 -112 N
ATOM 3779 CA ASN A 474 -9.801 -10.812 42.383 1.00 14.30 C
ANISOU 3779 CA ASN A 474 2086 1918 1427 318 233 -39 C
ATOM 3780 CB ASN A 474 -8.834 -9.641 42.465 1.00 15.15 C
ANISOU 3780 CB ASN A 474 2076 2023 1656 207 176 31 C
ATOM 3781 CG ASN A 474 -9.145 -8.683 43.587 1.00 15.80 C
ANISOU 3781 CG ASN A 474 2505 1803 1692 31 -272 -69 C
ATOM 3782 OD1 ASN A 474 -9.122 -9.058 44.755 1.00 18.03 O
ANISOU 3782 OD1 ASN A 474 2788 2477 1586 202 -46 -38 O
ATOM 3783 ND2 ASN A 474 -9.435 -7.445 43.223 1.00 17.67 N
ANISOU 3783 ND2 ASN A 474 3418 1591 1705 271 -462 -178 N
ATOM 3784 C ASN A 474 -11.216 -10.360 42.022 1.00 13.20 C
ANISOU 3784 C ASN A 474 2004 1649 1360 337 217 52 C
ATOM 3785 O ASN A 474 -11.460 -9.986 40.849 1.00 14.24 O
ANISOU 3785 O ASN A 474 2056 1917 1437 159 270 195 O
ATOM 3786 N LEU A 475 -12.111 -10.369 43.014 1.00 13.43 N
ANISOU 3786 N LEU A 475 2117 1564 1421 216 268 88 N
ATOM 3787 CA LEU A 475 -13.505 -10.025 42.787 1.00 12.80 C
ANISOU 3787 CA LEU A 475 2000 1190 1671 233 441 -96 C
ATOM 3788 CB LEU A 475 -14.420 -11.202 43.138 1.00 13.96 C
ANISOU 3788 CB LEU A 475 2144 1331 1827 113 235 84 C
ATOM 3789 CG LEU A 475 -14.216 -12.487 42.360 1.00 17.16 C
ANISOU 3789 CG LEU A 475 2642 1653 2224 -88 405 -246 C
ATOM 3790 CD1 LEU A 475 -15.277 -13.503 42.735 1.00 18.02 C
ANISOU 3790 CD1 LEU A 475 2853 1743 2251 -221 350 -30 C
ATOM 3791 CD2 LEU A 475 -14.151 -12.279 40.876 1.00 19.48 C
ANISOU 3791 CD2 LEU A 475 3049 2107 2242 -200 -164 -168 C
ATOM 3792 C LEU A 475 -13.912 -8.822 43.655 1.00 12.77 C
ANISOU 3792 C LEU A 475 2181 1378 1293 316 379 -86 C
ATOM 3793 O LEU A 475 -13.461 -8.660 44.801 1.00 14.59 O
ANISOU 3793 O LEU A 475 2397 1684 1459 385 209 -145 O
ATOM 3794 N THR A 476 -14.813 -8.011 43.096 1.00 12.08 N
ANISOU 3794 N THR A 476 1973 1353 1263 240 354 -60 N
ATOM 3795 CA THR A 476 -15.461 -6.917 43.803 1.00 12.90 C
ANISOU 3795 CA THR A 476 2091 1485 1322 289 365 -91 C
ATOM 3796 CB THR A 476 -15.300 -5.610 43.016 1.00 13.31 C
ANISOU 3796 CB THR A 476 2260 1359 1437 242 277 -107 C
ATOM 3797 OG1 THR A 476 -13.907 -5.300 42.960 1.00 13.82 O
ANISOU 3797 OG1 THR A 476 2137 1451 1661 140 153 -216 O
ATOM 3798 CG2 THR A 476 -16.062 -4.457 43.620 1.00 13.47 C
ANISOU 3798 CG2 THR A 476 2331 1382 1404 279 253 -139 C
ATOM 3799 C THR A 476 -16.930 -7.296 44.012 1.00 12.77 C
ANISOU 3799 C THR A 476 2012 1558 1280 363 288 -22 C
ATOM 3800 O THR A 476 -17.585 -7.847 43.113 1.00 13.92 O
ANISOU 3800 O THR A 476 2085 1842 1361 124 301 -104 O
ATOM 3801 N TYR A 477 -17.424 -7.011 45.211 1.00 12.53 N
ANISOU 3801 N TYR A 477 1953 1400 1405 408 407 -136 N
ATOM 3802 CA TYR A 477 -18.788 -7.363 45.634 1.00 12.88 C
ANISOU 3802 CA TYR A 477 2010 1495 1387 294 337 -142 C
ATOM 3803 CB TYR A 477 -18.747 -8.250 46.880 1.00 13.25 C
ANISOU 3803 CB TYR A 477 2220 1522 1292 403 501 -174 C
ATOM 3804 CG TYR A 477 -17.966 -9.519 46.700 1.00 13.86 C
ANISOU 3804 CG TYR A 477 2207 1610 1448 512 398 -79 C
ATOM 3805 CD1 TYR A 477 -16.607 -9.563 46.939 1.00 15.52 C
ANISOU 3805 CD1 TYR A 477 2278 1786 1832 565 235 77 C
ATOM 3806 CE1 TYR A 477 -15.873 -10.719 46.730 1.00 15.42 C
ANISOU 3806 CE1 TYR A 477 1898 1802 2156 464 492 23 C
ATOM 3807 CZ TYR A 477 -16.506 -11.863 46.276 1.00 15.81 C
ANISOU 3807 CZ TYR A 477 2350 1696 1960 540 329 39 C
ATOM 3808 OH TYR A 477 -15.811 -13.026 46.089 1.00 16.88 O
ANISOU 3808 OH TYR A 477 2380 1707 2324 515 518 -57 O
ATOM 3809 CE2 TYR A 477 -17.862 -11.831 46.028 1.00 15.86 C
ANISOU 3809 CE2 TYR A 477 2403 1690 1932 520 512 50 C
ATOM 3810 CD2 TYR A 477 -18.581 -10.666 46.231 1.00 14.46 C
ANISOU 3810 CD2 TYR A 477 2268 1598 1628 446 348 169 C
ATOM 3811 C TYR A 477 -19.560 -6.092 45.949 1.00 12.85 C
ANISOU 3811 C TYR A 477 1953 1674 1253 319 498 -199 C
ATOM 3812 O TYR A 477 -19.090 -5.261 46.725 1.00 14.58 O
ANISOU 3812 O TYR A 477 2351 1674 1513 484 348 -484 O
ATOM 3813 N SER A 478 -20.728 -5.950 45.326 1.00 11.90 N
ANISOU 3813 N SER A 478 1971 1361 1190 233 391 -154 N
ATOM 3814 CA SER A 478 -21.625 -4.840 45.557 1.00 12.66 C
ANISOU 3814 CA SER A 478 1923 1371 1513 198 521 -89 C
ATOM 3815 CB SER A 478 -22.052 -4.241 44.246 1.00 12.86 C
ANISOU 3815 CB SER A 478 1984 1313 1589 121 347 -57 C
ATOM 3816 OG SER A 478 -23.058 -3.241 44.417 1.00 12.54 O
ANISOU 3816 OG SER A 478 1861 1471 1432 217 425 -69 O
ATOM 3817 C SER A 478 -22.848 -5.349 46.329 1.00 13.86 C
ANISOU 3817 C SER A 478 2039 1644 1581 -17 574 -78 C
ATOM 3818 O SER A 478 -23.688 -6.054 45.749 1.00 13.72 O
ANISOU 3818 O SER A 478 1855 1718 1639 36 560 -219 O
ATOM 3819 N PHE A 479 -22.933 -4.979 47.611 1.00 13.47 N
ANISOU 3819 N PHE A 479 1956 1592 1570 40 531 -33 N
ATOM 3820 CA PHE A 479 -24.052 -5.373 48.466 1.00 14.54 C
ANISOU 3820 CA PHE A 479 2000 1792 1731 162 728 -120 C
ATOM 3821 CB PHE A 479 -23.573 -5.529 49.908 1.00 14.79 C
ANISOU 3821 CB PHE A 479 2463 1491 1664 297 703 -99 C
ATOM 3822 CG PHE A 479 -22.481 -6.559 50.078 1.00 15.51 C
ANISOU 3822 CG PHE A 479 2508 1711 1675 350 642 117 C
ATOM 3823 CD1 PHE A 479 -22.799 -7.884 50.333 1.00 17.89 C
ANISOU 3823 CD1 PHE A 479 2916 1765 2116 268 594 97 C
ATOM 3824 CE1 PHE A 479 -21.801 -8.843 50.478 1.00 18.09 C
ANISOU 3824 CE1 PHE A 479 3065 1929 1877 372 521 222 C
ATOM 3825 CZ PHE A 479 -20.480 -8.479 50.388 1.00 17.65 C
ANISOU 3825 CZ PHE A 479 2930 1996 1781 629 571 93 C
ATOM 3826 CD2 PHE A 479 -21.148 -6.211 50.013 1.00 15.97 C
ANISOU 3826 CD2 PHE A 479 2646 1882 1540 378 633 -165 C
ATOM 3827 CE2 PHE A 479 -20.156 -7.164 50.151 1.00 17.45 C
ANISOU 3827 CE2 PHE A 479 2948 1993 1689 476 644 -34 C
ATOM 3828 C PHE A 479 -25.175 -4.324 48.346 1.00 14.77 C
ANISOU 3828 C PHE A 479 2255 1511 1845 169 759 -109 C
ATOM 3829 O PHE A 479 -24.909 -3.150 48.195 1.00 14.43 O
ANISOU 3829 O PHE A 479 2293 1562 1625 159 536 35 O
ATOM 3830 N GLU A 480 -26.437 -4.755 48.441 1.00 16.67 N
ANISOU 3830 N GLU A 480 2457 1524 2351 -120 960 -30 N
ATOM 3831 CA GLU A 480 -27.533 -3.824 48.143 1.00 17.87 C
ANISOU 3831 CA GLU A 480 2398 1824 2565 -28 1130 -192 C
ATOM 3832 CB GLU A 480 -28.849 -4.534 47.840 1.00 21.75 C
ANISOU 3832 CB GLU A 480 2824 2523 2915 -243 927 -55 C
ATOM 3833 CG GLU A 480 -29.420 -5.213 49.044 1.00 19.85 C
ANISOU 3833 CG GLU A 480 2960 2377 2204 -37 1127 -426 C
ATOM 3834 CD GLU A 480 -30.812 -5.784 48.879 1.00 21.14 C
ANISOU 3834 CD GLU A 480 2730 2565 2734 234 1084 111 C
ATOM 3835 OE1 GLU A 480 -31.329 -5.867 47.735 1.00 21.55 O
ANISOU 3835 OE1 GLU A 480 2937 1970 3279 362 843 -246 O
ATOM 3836 OE2 GLU A 480 -31.378 -6.163 49.915 1.00 23.64 O
ANISOU 3836 OE2 GLU A 480 2446 3390 3143 485 1160 837 O
ATOM 3837 C GLU A 480 -27.642 -2.751 49.235 1.00 16.20 C
ANISOU 3837 C GLU A 480 2279 1654 2221 29 819 -1 C
ATOM 3838 O GLU A 480 -28.204 -1.706 48.955 1.00 16.53 O
ANISOU 3838 O GLU A 480 2529 1762 1987 188 810 -80 O
ATOM 3839 N ASP A 481 -27.101 -2.974 50.441 1.00 15.80 N
ANISOU 3839 N ASP A 481 2381 1569 2053 305 948 15 N
ATOM 3840 CA ASP A 481 -27.080 -1.919 51.475 1.00 16.91 C
ANISOU 3840 CA ASP A 481 2727 1627 2071 335 950 -12 C
ATOM 3841 CB ASP A 481 -26.752 -2.455 52.875 1.00 18.96 C
ANISOU 3841 CB ASP A 481 2969 2041 2193 418 1137 290 C
ATOM 3842 CG ASP A 481 -25.348 -3.008 53.091 1.00 19.45 C
ANISOU 3842 CG ASP A 481 3220 1990 2179 577 1054 416 C
ATOM 3843 OD1 ASP A 481 -24.471 -2.815 52.242 1.00 20.48 O
ANISOU 3843 OD1 ASP A 481 3239 2317 2223 933 1183 649 O
ATOM 3844 OD2 ASP A 481 -25.148 -3.641 54.146 1.00 25.63 O
ANISOU 3844 OD2 ASP A 481 4120 3214 2402 1101 1416 1009 O
ATOM 3845 C ASP A 481 -26.122 -0.763 51.121 1.00 16.77 C
ANISOU 3845 C ASP A 481 2650 1781 1939 266 925 -83 C
ATOM 3846 O ASP A 481 -26.108 0.236 51.836 1.00 17.71 O
ANISOU 3846 O ASP A 481 3064 1842 1821 373 870 -107 O
ATOM 3847 N GLY A 482 -25.345 -0.898 50.039 1.00 14.98 N
ANISOU 3847 N GLY A 482 2197 1605 1889 258 774 54 N
ATOM 3848 CA GLY A 482 -24.447 0.137 49.553 1.00 13.81 C
ANISOU 3848 CA GLY A 482 2242 1389 1617 154 522 -185 C
ATOM 3849 C GLY A 482 -22.986 -0.270 49.615 1.00 12.66 C
ANISOU 3849 C GLY A 482 2227 1229 1353 137 407 -13 C
ATOM 3850 O GLY A 482 -22.139 0.238 48.851 1.00 13.00 O
ANISOU 3850 O GLY A 482 2047 1551 1338 22 317 21 O
ATOM 3851 N THR A 483 -22.660 -1.188 50.528 1.00 12.81 N
ANISOU 3851 N THR A 483 2279 1234 1352 210 534 54 N
ATOM 3852 CA THR A 483 -21.272 -1.544 50.763 1.00 14.20 C
ANISOU 3852 CA THR A 483 2469 1516 1410 400 430 -67 C
ATOM 3853 CB THR A 483 -21.168 -2.526 51.935 1.00 15.18 C
ANISOU 3853 CB THR A 483 2435 1785 1546 556 461 172 C
ATOM 3854 OG1 THR A 483 -21.735 -1.883 53.072 1.00 17.00 O
ANISOU 3854 OG1 THR A 483 2540 2313 1605 720 497 45 O
ATOM 3855 CG2 THR A 483 -19.746 -2.934 52.252 1.00 15.88 C
ANISOU 3855 CG2 THR A 483 2662 2031 1341 739 297 146 C
ATOM 3856 C THR A 483 -20.640 -2.169 49.509 1.00 13.13 C
ANISOU 3856 C THR A 483 2259 1498 1231 238 397 14 C
ATOM 3857 O THR A 483 -21.272 -2.995 48.821 1.00 14.15 O
ANISOU 3857 O THR A 483 2215 1518 1641 175 290 -93 O
ATOM 3858 N PHE A 484 -19.382 -1.796 49.251 1.00 12.76 N
ANISOU 3858 N PHE A 484 2103 1587 1158 359 208 -158 N
ATOM 3859 CA PHE A 484 -18.511 -2.524 48.310 1.00 12.51 C
ANISOU 3859 CA PHE A 484 2085 1542 1124 320 234 -149 C
ATOM 3860 CB PHE A 484 -17.950 -1.616 47.206 1.00 12.21 C
ANISOU 3860 CB PHE A 484 1979 1450 1210 366 321 -192 C
ATOM 3861 CG PHE A 484 -18.949 -1.241 46.144 1.00 12.99 C
ANISOU 3861 CG PHE A 484 2082 1618 1233 323 294 -62 C
ATOM 3862 CD1 PHE A 484 -19.934 -0.294 46.373 1.00 12.45 C
ANISOU 3862 CD1 PHE A 484 1942 1660 1125 236 319 -185 C
ATOM 3863 CE1 PHE A 484 -20.827 0.052 45.380 1.00 13.13 C
ANISOU 3863 CE1 PHE A 484 1881 1650 1456 154 226 -28 C
ATOM 3864 CZ PHE A 484 -20.739 -0.525 44.144 1.00 12.71 C
ANISOU 3864 CZ PHE A 484 2018 1410 1399 -58 58 94 C
ATOM 3865 CD2 PHE A 484 -18.863 -1.805 44.882 1.00 13.84 C
ANISOU 3865 CD2 PHE A 484 2346 1661 1252 217 157 -103 C
ATOM 3866 CE2 PHE A 484 -19.779 -1.469 43.897 1.00 13.61 C
ANISOU 3866 CE2 PHE A 484 2346 1610 1215 110 232 -20 C
ATOM 3867 C PHE A 484 -17.334 -3.137 49.073 1.00 13.56 C
ANISOU 3867 C PHE A 484 2314 1547 1288 499 199 -95 C
ATOM 3868 O PHE A 484 -16.797 -2.537 50.009 1.00 14.85 O
ANISOU 3868 O PHE A 484 2277 1915 1448 287 353 -311 O
ATOM 3869 N MET A 485 -16.932 -4.339 48.644 1.00 14.64 N
ANISOU 3869 N MET A 485 2352 1654 1555 435 130 -330 N
ATOM 3870 CA MET A 485 -15.743 -5.029 49.161 1.00 15.43 C
ANISOU 3870 CA MET A 485 2574 1623 1665 595 34 -261 C
ATOM 3871 CB MET A 485 -16.128 -6.174 50.118 1.00 17.33 C
ANISOU 3871 CB MET A 485 2838 1930 1815 709 198 -3 C
ATOM 3872 CG MET A 485 -16.851 -5.716 51.386 1.00 18.60 C
ANISOU 3872 CG MET A 485 3452 1802 1813 546 199 -148 C
ATOM 3873 SD MET A 485 -17.311 -7.086 52.458 1.00 25.26 S
ANISOU 3873 SD MET A 485 4303 2903 2391 -171 -128 521 S
ATOM 3874 CE MET A 485 -15.703 -7.535 53.098 1.00 29.74 C
ANISOU 3874 CE MET A 485 4457 3922 2920 90 -432 421 C
ATOM 3875 C MET A 485 -14.979 -5.606 47.967 1.00 14.87 C
ANISOU 3875 C MET A 485 2142 1674 1831 581 35 -271 C
ATOM 3876 O MET A 485 -15.571 -5.781 46.904 1.00 15.58 O
ANISOU 3876 O MET A 485 2008 1977 1935 467 43 -417 O
ATOM 3877 N ASP A 486 -13.684 -5.883 48.127 1.00 14.58 N
ANISOU 3877 N ASP A 486 2038 1558 1943 518 14 -593 N
ATOM 3878 CA ASP A 486 -13.025 -6.722 47.155 1.00 15.84 C
ANISOU 3878 CA ASP A 486 2089 1704 2223 821 91 -503 C
ATOM 3879 CB ASP A 486 -12.326 -5.897 46.059 1.00 18.91 C
ANISOU 3879 CB ASP A 486 2518 2189 2477 647 231 -349 C
ATOM 3880 CG ASP A 486 -11.099 -5.123 46.464 1.00 26.62 C
ANISOU 3880 CG ASP A 486 2693 3541 3881 332 53 -703 C
ATOM 3881 OD1 ASP A 486 -11.027 -4.711 47.612 1.00 30.57 O
ANISOU 3881 OD1 ASP A 486 2714 3730 5171 466 107 -2306 O
ATOM 3882 OD2 ASP A 486 -10.186 -5.015 45.611 1.00 37.00 O
ANISOU 3882 OD2 ASP A 486 3752 4886 5417 -725 788 -794 O
ATOM 3883 C ASP A 486 -12.099 -7.694 47.893 1.00 16.64 C
ANISOU 3883 C ASP A 486 2564 1929 1828 924 -234 -602 C
ATOM 3884 O ASP A 486 -11.620 -7.441 49.009 1.00 20.85 O
ANISOU 3884 O ASP A 486 3297 2624 1998 1083 -625 -726 O
ATOM 3885 N ASP A 487 -11.833 -8.829 47.245 1.00 14.11 N
ANISOU 3885 N ASP A 487 2414 1677 1270 605 -40 -324 N
ATOM 3886 CA ASP A 487 -11.042 -9.866 47.858 1.00 15.34 C
ANISOU 3886 CA ASP A 487 2247 1966 1616 664 77 -84 C
ATOM 3887 CB ASP A 487 -11.835 -10.698 48.878 1.00 17.40 C
ANISOU 3887 CB ASP A 487 2674 2265 1669 617 438 -101 C
ATOM 3888 CG ASP A 487 -11.941 -10.064 50.253 1.00 23.03 C
ANISOU 3888 CG ASP A 487 3555 3195 1997 776 476 -500 C
ATOM 3889 OD1 ASP A 487 -10.894 -9.806 50.854 1.00 27.91 O
ANISOU 3889 OD1 ASP A 487 4165 4010 2429 745 -6 -360 O
ATOM 3890 OD2 ASP A 487 -13.068 -9.781 50.678 1.00 31.21 O
ANISOU 3890 OD2 ASP A 487 4083 4350 3425 607 1324 -1225 O
ATOM 3891 C ASP A 487 -10.534 -10.833 46.795 1.00 14.11 C
ANISOU 3891 C ASP A 487 2079 1772 1508 373 325 76 C
ATOM 3892 O ASP A 487 -11.231 -11.139 45.802 1.00 15.20 O
ANISOU 3892 O ASP A 487 2370 1911 1494 406 268 -85 O
ATOM 3893 N LEU A 488 -9.314 -11.336 47.035 1.00 14.46 N
ANISOU 3893 N LEU A 488 2213 1706 1574 484 215 -63 N
ATOM 3894 CA LEU A 488 -8.778 -12.405 46.253 1.00 14.52 C
ANISOU 3894 CA LEU A 488 2063 1901 1553 407 463 -186 C
ATOM 3895 CB LEU A 488 -7.373 -12.738 46.746 1.00 15.22 C
ANISOU 3895 CB LEU A 488 2322 1862 1598 466 299 -37 C
ATOM 3896 CG LEU A 488 -6.317 -11.644 46.637 1.00 16.72 C
ANISOU 3896 CG LEU A 488 2622 1789 1940 428 336 -89 C
ATOM 3897 CD1 LEU A 488 -4.979 -12.182 47.135 1.00 17.85 C
ANISOU 3897 CD1 LEU A 488 2733 2236 1811 354 167 -128 C
ATOM 3898 CD2 LEU A 488 -6.197 -11.152 45.206 1.00 16.78 C
ANISOU 3898 CD2 LEU A 488 2468 2052 1855 526 350 -90 C
ATOM 3899 C LEU A 488 -9.675 -13.634 46.411 1.00 14.66 C
ANISOU 3899 C LEU A 488 2083 1880 1605 445 179 -57 C
ATOM 3900 O LEU A 488 -10.300 -13.839 47.450 1.00 16.75 O
ANISOU 3900 O LEU A 488 2572 2210 1582 -33 265 -41 O
ATOM 3901 N THR A 489 -9.711 -14.458 45.365 1.00 15.36 N
ANISOU 3901 N THR A 489 2401 1671 1763 409 303 -123 N
ATOM 3902 CA THR A 489 -10.433 -15.721 45.360 1.00 16.54 C
ANISOU 3902 CA THR A 489 2561 1636 2087 387 60 -166 C
ATOM 3903 CB THR A 489 -11.042 -15.991 43.975 1.00 16.88 C
ANISOU 3903 CB THR A 489 2740 1514 2157 300 -181 46 C
ATOM 3904 OG1 THR A 489 -10.012 -15.961 42.970 1.00 18.82 O
ANISOU 3904 OG1 THR A 489 3134 2058 1959 291 -192 -57 O
ATOM 3905 CG2 THR A 489 -12.106 -14.975 43.616 1.00 18.21 C
ANISOU 3905 CG2 THR A 489 2692 1812 2413 337 -227 123 C
ATOM 3906 C THR A 489 -9.459 -16.826 45.756 1.00 17.05 C
ANISOU 3906 C THR A 489 2355 2057 2065 523 77 -41 C
ATOM 3907 O THR A 489 -8.757 -17.341 44.898 1.00 23.18 O
ANISOU 3907 O THR A 489 3958 2764 2083 1805 321 271 O
ATOM 3908 N LEU A 490 -9.403 -17.174 47.038 1.00 16.81 N
ANISOU 3908 N LEU A 490 2330 2003 2053 631 219 -28 N
ATOM 3909 CA LEU A 490 -8.400 -18.116 47.525 1.00 16.40 C
ANISOU 3909 CA LEU A 490 2470 1833 1928 593 222 -178 C
ATOM 3910 CB LEU A 490 -7.507 -17.434 48.568 1.00 16.41 C
ANISOU 3910 CB LEU A 490 2528 1854 1852 301 190 -15 C
ATOM 3911 CG LEU A 490 -6.690 -16.244 48.071 1.00 17.43 C
ANISOU 3911 CG LEU A 490 2764 1775 2081 268 -1 15 C
ATOM 3912 CD1 LEU A 490 -5.850 -15.660 49.209 1.00 21.96 C
ANISOU 3912 CD1 LEU A 490 3200 2652 2491 -139 -227 -129 C
ATOM 3913 CD2 LEU A 490 -5.810 -16.644 46.915 1.00 19.92 C
ANISOU 3913 CD2 LEU A 490 3177 1897 2495 461 418 194 C
ATOM 3914 C LEU A 490 -9.084 -19.324 48.157 1.00 15.83 C
ANISOU 3914 C LEU A 490 2384 2046 1582 319 163 -258 C
ATOM 3915 O LEU A 490 -10.114 -19.188 48.839 1.00 17.31 O
ANISOU 3915 O LEU A 490 2558 2096 1920 493 501 -19 O
ATOM 3916 N TYR A 491 -8.463 -20.488 47.949 1.00 15.70 N
ANISOU 3916 N TYR A 491 2364 2114 1486 459 212 -66 N
ATOM 3917 CA TYR A 491 -8.975 -21.794 48.396 1.00 15.90 C
ANISOU 3917 CA TYR A 491 2580 2037 1423 436 204 134 C
ATOM 3918 CB TYR A 491 -9.774 -22.483 47.283 1.00 16.30 C
ANISOU 3918 CB TYR A 491 2452 2075 1667 516 168 12 C
ATOM 3919 CG TYR A 491 -10.807 -21.566 46.684 1.00 17.81 C
ANISOU 3919 CG TYR A 491 2664 2047 2056 493 -118 26 C
ATOM 3920 CD1 TYR A 491 -10.465 -20.745 45.620 1.00 18.47 C
ANISOU 3920 CD1 TYR A 491 2722 2088 2207 319 -109 54 C
ATOM 3921 CE1 TYR A 491 -11.359 -19.825 45.122 1.00 20.37 C
ANISOU 3921 CE1 TYR A 491 3014 2275 2448 262 -630 -148 C
ATOM 3922 CZ TYR A 491 -12.611 -19.698 45.679 1.00 23.55 C
ANISOU 3922 CZ TYR A 491 3009 2939 2998 801 -574 -235 C
ATOM 3923 OH TYR A 491 -13.449 -18.760 45.138 1.00 27.83 O
ANISOU 3923 OH TYR A 491 4182 2832 3558 1219 -1295 -635 O
ATOM 3924 CE2 TYR A 491 -12.977 -20.513 46.734 1.00 22.18 C
ANISOU 3924 CE2 TYR A 491 2942 2867 2616 763 -299 -585 C
ATOM 3925 CD2 TYR A 491 -12.071 -21.431 47.239 1.00 19.98 C
ANISOU 3925 CD2 TYR A 491 2947 2577 2066 458 -136 -376 C
ATOM 3926 C TYR A 491 -7.784 -22.643 48.846 1.00 15.90 C
ANISOU 3926 C TYR A 491 2567 2015 1459 282 145 164 C
ATOM 3927 O TYR A 491 -6.654 -22.443 48.423 1.00 17.05 O
ANISOU 3927 O TYR A 491 2678 2034 1766 241 302 172 O
ATOM 3928 N THR A 492 -8.051 -23.655 49.672 1.00 16.95 N
ANISOU 3928 N THR A 492 2758 2035 1644 360 247 361 N
ATOM 3929 CA THR A 492 -6.993 -24.583 50.010 1.00 17.17 C
ANISOU 3929 CA THR A 492 2887 1974 1663 368 25 175 C
ATOM 3930 CB THR A 492 -7.368 -25.515 51.169 1.00 18.74 C
ANISOU 3930 CB THR A 492 3092 2227 1800 297 21 393 C
ATOM 3931 OG1 THR A 492 -8.401 -26.409 50.745 1.00 20.71 O
ANISOU 3931 OG1 THR A 492 3395 2515 1959 172 -11 237 O
ATOM 3932 CG2 THR A 492 -7.783 -24.751 52.405 1.00 20.67 C
ANISOU 3932 CG2 THR A 492 3391 2686 1775 336 -2 293 C
ATOM 3933 C THR A 492 -6.607 -25.426 48.801 1.00 17.23 C
ANISOU 3933 C THR A 492 2893 1897 1754 560 26 227 C
ATOM 3934 O THR A 492 -7.430 -25.705 47.939 1.00 16.11 O
ANISOU 3934 O THR A 492 2412 1804 1902 453 214 187 O
ATOM 3935 N PRO A 493 -5.335 -25.860 48.700 1.00 17.89 N
ANISOU 3935 N PRO A 493 2792 2075 1929 445 171 388 N
ATOM 3936 CA PRO A 493 -4.974 -26.840 47.682 1.00 18.84 C
ANISOU 3936 CA PRO A 493 3154 2027 1976 670 255 515 C
ATOM 3937 CB PRO A 493 -3.540 -27.218 48.044 1.00 19.60 C
ANISOU 3937 CB PRO A 493 2981 2072 2391 594 233 348 C
ATOM 3938 CG PRO A 493 -2.995 -25.955 48.707 1.00 20.02 C
ANISOU 3938 CG PRO A 493 2901 2108 2595 706 131 269 C
ATOM 3939 CD PRO A 493 -4.175 -25.390 49.479 1.00 18.69 C
ANISOU 3939 CD PRO A 493 2972 2228 1898 641 119 467 C
ATOM 3940 C PRO A 493 -5.929 -28.039 47.643 1.00 18.93 C
ANISOU 3940 C PRO A 493 2997 2009 2186 702 258 550 C
ATOM 3941 O PRO A 493 -6.336 -28.465 46.573 1.00 20.41 O
ANISOU 3941 O PRO A 493 3176 2378 2201 667 288 391 O
ATOM 3942 N ASP A 494 -6.298 -28.576 48.803 1.00 20.22 N
ANISOU 3942 N ASP A 494 3604 2124 1952 379 157 388 N
ATOM 3943 CA ASP A 494 -7.162 -29.744 48.846 1.00 21.65 C
ANISOU 3943 CA ASP A 494 3536 2221 2466 373 174 605 C
ATOM 3944 CB ASP A 494 -7.326 -30.269 50.273 1.00 24.32 C
ANISOU 3944 CB ASP A 494 3769 2740 2730 91 14 1057 C
ATOM 3945 CG ASP A 494 -6.108 -31.031 50.784 1.00 29.98 C
ANISOU 3945 CG ASP A 494 4457 3525 3408 686 -51 1376 C
ATOM 3946 OD1 ASP A 494 -5.183 -31.329 49.969 1.00 33.49 O
ANISOU 3946 OD1 ASP A 494 4271 3994 4459 607 222 995 O
ATOM 3947 OD2 ASP A 494 -6.093 -31.327 51.997 1.00 36.78 O
ANISOU 3947 OD2 ASP A 494 5700 4630 3644 837 -346 1898 O
ATOM 3948 C ASP A 494 -8.518 -29.427 48.219 1.00 20.65 C
ANISOU 3948 C ASP A 494 3618 1977 2249 388 174 588 C
ATOM 3949 O ASP A 494 -9.057 -30.270 47.507 1.00 23.01 O
ANISOU 3949 O ASP A 494 3975 2259 2508 300 213 523 O
ATOM 3950 N GLN A 495 -9.075 -28.230 48.472 1.00 18.90 N
ANISOU 3950 N GLN A 495 3127 2016 2038 265 228 337 N
ATOM 3951 CA AGLN A 495 -10.347 -27.852 47.844 0.50 18.52 C
ANISOU 3951 CA AGLN A 495 3058 1937 2039 232 448 513 C
ATOM 3952 CA BGLN A 495 -10.330 -27.895 47.841 0.50 18.68 C
ANISOU 3952 CA BGLN A 495 3102 1983 2012 261 406 519 C
ATOM 3953 CB AGLN A 495 -10.831 -26.465 48.296 0.50 18.82 C
ANISOU 3953 CB AGLN A 495 2917 2175 2057 360 645 430 C
ATOM 3954 CB BGLN A 495 -10.908 -26.562 48.289 0.50 18.44 C
ANISOU 3954 CB BGLN A 495 2957 2238 1808 417 519 500 C
ATOM 3955 CG AGLN A 495 -11.258 -26.343 49.765 0.50 18.77 C
ANISOU 3955 CG AGLN A 495 2706 2352 2073 450 664 501 C
ATOM 3956 CG BGLN A 495 -12.175 -26.327 47.486 0.50 18.40 C
ANISOU 3956 CG BGLN A 495 2890 2331 1769 510 546 579 C
ATOM 3957 CD AGLN A 495 -11.691 -24.946 50.177 0.50 19.43 C
ANISOU 3957 CD AGLN A 495 2534 2280 2565 321 704 463 C
ATOM 3958 CD BGLN A 495 -13.025 -25.152 47.855 0.50 18.83 C
ANISOU 3958 CD BGLN A 495 2842 2688 1625 672 553 465 C
ATOM 3959 OE1AGLN A 495 -10.903 -23.992 50.323 0.50 16.51 O
ANISOU 3959 OE1AGLN A 495 2086 2442 1744 250 837 670 O
ATOM 3960 OE1BGLN A 495 -13.766 -24.677 47.001 0.50 18.64 O
ANISOU 3960 OE1BGLN A 495 2989 2564 1529 890 737 741 O
ATOM 3961 NE2AGLN A 495 -12.988 -24.815 50.401 0.50 21.47 N
ANISOU 3961 NE2AGLN A 495 2677 2580 2900 584 862 300 N
ATOM 3962 NE2BGLN A 495 -12.937 -24.727 49.111 0.50 19.36 N
ANISOU 3962 NE2BGLN A 495 2658 3192 1504 260 385 607 N
ATOM 3963 C GLN A 495 -10.184 -27.876 46.315 1.00 18.94 C
ANISOU 3963 C GLN A 495 3170 2008 2019 239 321 354 C
ATOM 3964 O GLN A 495 -11.060 -28.377 45.589 1.00 21.44 O
ANISOU 3964 O GLN A 495 3935 2142 2068 -11 -11 416 O
ATOM 3965 N LEU A 496 -9.102 -27.275 45.824 1.00 18.11 N
ANISOU 3965 N LEU A 496 3011 1879 1989 278 232 237 N
ATOM 3966 CA LEU A 496 -8.899 -27.171 44.374 1.00 17.39 C
ANISOU 3966 CA LEU A 496 3043 1627 1937 367 -1 321 C
ATOM 3967 CB LEU A 496 -7.757 -26.197 44.109 1.00 17.78 C
ANISOU 3967 CB LEU A 496 3137 1728 1889 342 348 203 C
ATOM 3968 CG LEU A 496 -8.034 -24.761 44.568 1.00 16.89 C
ANISOU 3968 CG LEU A 496 3170 1530 1714 209 277 446 C
ATOM 3969 CD1 LEU A 496 -6.846 -23.867 44.280 1.00 17.74 C
ANISOU 3969 CD1 LEU A 496 3227 2079 1431 23 181 538 C
ATOM 3970 CD2 LEU A 496 -9.307 -24.203 43.935 1.00 18.14 C
ANISOU 3970 CD2 LEU A 496 3424 1655 1813 259 234 498 C
ATOM 3971 C LEU A 496 -8.634 -28.555 43.758 1.00 19.66 C
ANISOU 3971 C LEU A 496 3387 1653 2427 350 43 219 C
ATOM 3972 O LEU A 496 -9.202 -28.866 42.716 1.00 21.19 O
ANISOU 3972 O LEU A 496 3904 1665 2481 258 -53 193 O
ATOM 3973 N LEU A 497 -7.826 -29.394 44.418 1.00 20.79 N
ANISOU 3973 N LEU A 497 3577 1932 2389 430 -32 134 N
ATOM 3974 CA LEU A 497 -7.464 -30.721 43.881 1.00 21.49 C
ANISOU 3974 CA LEU A 497 3808 2048 2309 541 126 121 C
ATOM 3975 CB LEU A 497 -6.472 -31.408 44.826 1.00 21.58 C
ANISOU 3975 CB LEU A 497 3865 1762 2570 821 316 293 C
ATOM 3976 CG LEU A 497 -5.051 -30.852 44.778 1.00 23.50 C
ANISOU 3976 CG LEU A 497 3968 2289 2669 621 266 57 C
ATOM 3977 CD1 LEU A 497 -4.257 -31.290 45.984 1.00 26.46 C
ANISOU 3977 CD1 LEU A 497 3772 3136 3144 510 102 327 C
ATOM 3978 CD2 LEU A 497 -4.346 -31.259 43.495 1.00 25.21 C
ANISOU 3978 CD2 LEU A 497 3749 2648 3182 499 741 127 C
ATOM 3979 C LEU A 497 -8.711 -31.591 43.689 1.00 22.12 C
ANISOU 3979 C LEU A 497 4269 1760 2375 353 -107 54 C
ATOM 3980 O LEU A 497 -8.712 -32.466 42.806 1.00 25.19 O
ANISOU 3980 O LEU A 497 4722 1915 2931 406 -65 -241 O
ATOM 3981 N ARG A 498 -9.746 -31.385 44.515 1.00 21.57 N
ANISOU 3981 N ARG A 498 3614 1779 2802 97 -304 238 N
ATOM 3982 CA ARG A 498 -10.955 -32.215 44.463 1.00 24.11 C
ANISOU 3982 CA ARG A 498 3655 2106 3400 204 -380 453 C
ATOM 3983 CB ARG A 498 -11.417 -32.598 45.871 1.00 26.80 C
ANISOU 3983 CB ARG A 498 3759 2828 3594 -185 122 624 C
ATOM 3984 CG ARG A 498 -12.159 -31.542 46.673 1.00 29.78 C
ANISOU 3984 CG ARG A 498 4191 3406 3719 -87 292 698 C
ATOM 3985 CD ARG A 498 -12.510 -32.096 48.063 1.00 36.35 C
ANISOU 3985 CD ARG A 498 4839 5127 3843 -622 880 672 C
ATOM 3986 NE ARG A 498 -12.871 -31.034 48.995 1.00 40.16 N
ANISOU 3986 NE ARG A 498 4779 6396 4085 -682 1261 455 N
ATOM 3987 CZ ARG A 498 -12.093 -30.560 49.972 1.00 42.59 C
ANISOU 3987 CZ ARG A 498 5186 6914 4081 -780 1397 -1 C
ATOM 3988 NH1 ARG A 498 -10.894 -31.066 50.211 1.00 48.51 N
ANISOU 3988 NH1 ARG A 498 4170 8753 5506 -1378 1158 449 N
ATOM 3989 NH2 ARG A 498 -12.527 -29.553 50.707 1.00 46.38 N
ANISOU 3989 NH2 ARG A 498 6605 6884 4133 -620 1707 194 N
ATOM 3990 C ARG A 498 -12.076 -31.539 43.662 1.00 21.18 C
ANISOU 3990 C ARG A 498 3545 1827 2675 112 -198 371 C
ATOM 3991 O ARG A 498 -13.167 -32.109 43.540 1.00 26.01 O
ANISOU 3991 O ARG A 498 3878 2533 3470 -271 -252 578 O
ATOM 3992 N SER A 499 -11.804 -30.380 43.053 1.00 20.71 N
ANISOU 3992 N SER A 499 3550 1825 2493 75 -223 233 N
ATOM 3993 CA SER A 499 -12.818 -29.643 42.323 1.00 19.96 C
ANISOU 3993 CA SER A 499 3389 1735 2459 203 -210 7 C
ATOM 3994 CB SER A 499 -12.435 -28.207 42.142 1.00 18.96 C
ANISOU 3994 CB SER A 499 3349 1616 2238 314 -219 57 C
ATOM 3995 OG SER A 499 -12.380 -27.510 43.381 1.00 19.84 O
ANISOU 3995 OG SER A 499 3430 1925 2180 302 105 -62 O
ATOM 3996 C SER A 499 -13.058 -30.297 40.965 1.00 21.45 C
ANISOU 3996 C SER A 499 3759 1685 2703 385 -243 -133 C
ATOM 3997 O SER A 499 -12.139 -30.842 40.343 1.00 24.07 O
ANISOU 3997 O SER A 499 4648 1711 2783 729 296 -49 O
ATOM 3998 N PRO A 500 -14.302 -30.275 40.462 1.00 21.76 N
ANISOU 3998 N PRO A 500 3725 1845 2697 160 -380 92 N
ATOM 3999 CA PRO A 500 -14.604 -30.890 39.173 1.00 22.32 C
ANISOU 3999 CA PRO A 500 3888 1792 2797 223 -107 -153 C
ATOM 4000 CB PRO A 500 -16.119 -30.751 39.024 1.00 25.52 C
ANISOU 4000 CB PRO A 500 3908 2539 3248 -55 -97 102 C
ATOM 4001 CG PRO A 500 -16.510 -29.677 39.990 1.00 27.61 C
ANISOU 4001 CG PRO A 500 3972 3097 3421 252 -493 -215 C
ATOM 4002 CD PRO A 500 -15.486 -29.697 41.103 1.00 24.79 C
ANISOU 4002 CD PRO A 500 3819 2547 3052 273 -328 -94 C
ATOM 4003 C PRO A 500 -13.907 -30.191 38.002 1.00 19.64 C
ANISOU 4003 C PRO A 500 3025 1452 2985 494 -77 -124 C
ATOM 4004 O PRO A 500 -13.743 -28.960 38.051 1.00 19.57 O
ANISOU 4004 O PRO A 500 3214 1431 2788 422 345 -256 O
ATOM 4005 N LEU A 501 -13.521 -30.968 36.975 1.00 20.44 N
ANISOU 4005 N LEU A 501 3129 1365 3270 396 -235 -408 N
ATOM 4006 CA LEU A 501 -12.899 -30.395 35.804 1.00 22.24 C
ANISOU 4006 CA LEU A 501 2880 2504 3065 730 10 -682 C
ATOM 4007 CB LEU A 501 -12.315 -31.475 34.886 1.00 25.30 C
ANISOU 4007 CB LEU A 501 3488 2651 3472 668 -215 -1173 C
ATOM 4008 CG LEU A 501 -11.234 -32.363 35.478 1.00 27.19 C
ANISOU 4008 CG LEU A 501 4020 2514 3796 807 -381 -846 C
ATOM 4009 CD1 LEU A 501 -10.850 -33.456 34.498 1.00 29.84 C
ANISOU 4009 CD1 LEU A 501 3982 3132 4221 1154 -476 -1177 C
ATOM 4010 CD2 LEU A 501 -10.026 -31.537 35.857 1.00 26.83 C
ANISOU 4010 CD2 LEU A 501 3564 2507 4121 1102 -312 -740 C
ATOM 4011 C LEU A 501 -13.948 -29.619 35.011 1.00 20.94 C
ANISOU 4011 C LEU A 501 2440 2648 2867 736 52 -813 C
ATOM 4012 O LEU A 501 -15.106 -30.042 34.924 1.00 24.36 O
ANISOU 4012 O LEU A 501 2647 3535 3071 271 -5 -492 O
ATOM 4013 N LYS A 502 -13.498 -28.526 34.400 1.00 21.18 N
ANISOU 4013 N LYS A 502 2253 3251 2541 726 -61 -541 N
ATOM 4014 CA LYS A 502 -14.264 -27.784 33.421 1.00 21.31 C
ANISOU 4014 CA LYS A 502 2212 3418 2464 701 -130 -563 C
ATOM 4015 CB LYS A 502 -14.512 -26.343 33.866 1.00 24.07 C
ANISOU 4015 CB LYS A 502 2762 3675 2708 1043 -135 -530 C
ATOM 4016 CG LYS A 502 -15.189 -25.482 32.799 1.00 27.34 C
ANISOU 4016 CG LYS A 502 3580 4023 2786 1212 -148 -254 C
ATOM 4017 CD LYS A 502 -15.455 -24.066 33.223 1.00 30.72 C
ANISOU 4017 CD LYS A 502 4254 4246 3171 1409 -225 -436 C
ATOM 4018 CE LYS A 502 -16.089 -23.225 32.138 1.00 31.02 C
ANISOU 4018 CE LYS A 502 4224 3787 3775 1985 -50 -381 C
ATOM 4019 NZ LYS A 502 -15.109 -22.840 31.105 1.00 35.51 N
ANISOU 4019 NZ LYS A 502 4786 4377 4328 1045 -144 117 N
ATOM 4020 C LYS A 502 -13.448 -27.842 32.125 1.00 20.47 C
ANISOU 4020 C LYS A 502 2194 3268 2316 454 -108 -555 C
ATOM 4021 O LYS A 502 -12.404 -27.171 32.021 1.00 21.79 O
ANISOU 4021 O LYS A 502 2104 3498 2677 515 14 -781 O
ATOM 4022 N LEU A 503 -13.914 -28.664 31.167 1.00 19.45 N
ANISOU 4022 N LEU A 503 2306 2956 2126 532 215 -670 N
ATOM 4023 CA LEU A 503 -13.155 -28.938 29.961 1.00 21.96 C
ANISOU 4023 CA LEU A 503 2571 3427 2346 451 456 -785 C
ATOM 4024 CB LEU A 503 -13.268 -30.424 29.624 1.00 22.25 C
ANISOU 4024 CB LEU A 503 2464 3310 2679 263 404 -565 C
ATOM 4025 CG LEU A 503 -12.609 -31.363 30.620 1.00 24.33 C
ANISOU 4025 CG LEU A 503 2696 3447 3102 305 -52 -576 C
ATOM 4026 CD1 LEU A 503 -13.169 -32.765 30.517 1.00 24.95 C
ANISOU 4026 CD1 LEU A 503 2485 3634 3361 221 -106 -500 C
ATOM 4027 CD2 LEU A 503 -11.123 -31.391 30.394 1.00 27.77 C
ANISOU 4027 CD2 LEU A 503 2866 3773 3909 381 97 -378 C
ATOM 4028 C LEU A 503 -13.635 -28.084 28.776 1.00 24.91 C
ANISOU 4028 C LEU A 503 3646 3392 2424 570 376 -686 C
ATOM 4029 O LEU A 503 -12.952 -28.058 27.728 1.00 26.78 O
ANISOU 4029 O LEU A 503 4497 3401 2277 449 584 -468 O
ATOM 4030 N THR A 504 -14.780 -27.408 28.937 1.00 28.43 N
ANISOU 4030 N THR A 504 4104 3809 2890 928 280 -501 N
ATOM 4031 CA THR A 504 -15.352 -26.542 27.884 1.00 34.60 C
ANISOU 4031 CA THR A 504 5136 4696 3314 1322 -401 -471 C
ATOM 4032 CB THR A 504 -16.754 -27.022 27.514 1.00 38.12 C
ANISOU 4032 CB THR A 504 4662 5561 4259 1365 -209 -388 C
ATOM 4033 OG1 THR A 504 -17.559 -26.900 28.689 1.00 44.12 O
ANISOU 4033 OG1 THR A 504 4584 7337 4840 1742 153 179 O
ATOM 4034 CG2 THR A 504 -16.739 -28.440 26.993 1.00 38.51 C
ANISOU 4034 CG2 THR A 504 4597 5324 4709 719 -699 -110 C
ATOM 4035 C THR A 504 -15.370 -25.082 28.342 1.00 45.76 C
ANISOU 4035 C THR A 504 7069 4795 5522 1300 -162 -1057 C
ATOM 4036 O THR A 504 -14.589 -24.705 29.226 1.00 53.37 O
ANISOU 4036 O THR A 504 9215 5028 6033 1778 -1153 -815 O
ATOM 4037 N LYS A 509 -25.468 -21.473 29.948 1.00 46.82 N
ANISOU 4037 N LYS A 509 8200 2603 6984 646 156 -1665 N
ATOM 4038 CA LYS A 509 -25.014 -20.217 29.314 1.00 42.27 C
ANISOU 4038 CA LYS A 509 7347 3507 5203 942 -394 -1096 C
ATOM 4039 CB LYS A 509 -25.733 -19.975 27.979 1.00 47.31 C
ANISOU 4039 CB LYS A 509 8042 3627 6305 1772 -938 -991 C
ATOM 4040 CG LYS A 509 -25.236 -20.814 26.808 1.00 54.37 C
ANISOU 4040 CG LYS A 509 8770 5640 6245 856 -756 -1791 C
ATOM 4041 CD LYS A 509 -26.300 -21.146 25.771 1.00 60.74 C
ANISOU 4041 CD LYS A 509 8854 6719 7503 162 -1281 -1357 C
ATOM 4042 CE LYS A 509 -25.727 -21.367 24.382 1.00 62.06 C
ANISOU 4042 CE LYS A 509 8362 7187 8029 6 -939 -1782 C
ATOM 4043 NZ LYS A 509 -26.386 -22.484 23.664 1.00 63.03 N
ANISOU 4043 NZ LYS A 509 7836 6745 9367 -608 -1158 -1148 N
ATOM 4044 C LYS A 509 -25.226 -19.040 30.274 1.00 32.05 C
ANISOU 4044 C LYS A 509 5108 3314 3753 1073 -562 -396 C
ATOM 4045 O LYS A 509 -24.516 -18.040 30.192 1.00 33.71 O
ANISOU 4045 O LYS A 509 5382 3318 4107 1230 667 665 O
ATOM 4046 N LEU A 510 -26.144 -19.178 31.231 1.00 29.39 N
ANISOU 4046 N LEU A 510 3899 3283 3981 695 -928 -636 N
ATOM 4047 CA LEU A 510 -26.281 -18.149 32.264 1.00 26.22 C
ANISOU 4047 CA LEU A 510 3451 2819 3692 594 -745 -535 C
ATOM 4048 CB LEU A 510 -27.679 -18.183 32.897 1.00 29.23 C
ANISOU 4048 CB LEU A 510 3914 3288 3903 199 -481 -83 C
ATOM 4049 CG LEU A 510 -28.840 -17.751 32.004 1.00 31.47 C
ANISOU 4049 CG LEU A 510 3904 3342 4711 324 -596 47 C
ATOM 4050 CD1 LEU A 510 -30.127 -17.637 32.807 1.00 35.83 C
ANISOU 4050 CD1 LEU A 510 4482 4227 4902 -30 -337 228 C
ATOM 4051 CD2 LEU A 510 -28.558 -16.428 31.301 1.00 29.25 C
ANISOU 4051 CD2 LEU A 510 3323 3156 4634 369 -811 -43 C
ATOM 4052 C LEU A 510 -25.201 -18.309 33.348 1.00 22.60 C
ANISOU 4052 C LEU A 510 3673 2299 2615 1116 -131 -284 C
ATOM 4053 O LEU A 510 -24.957 -17.373 34.140 1.00 23.71 O
ANISOU 4053 O LEU A 510 3715 2191 3101 960 -248 -410 O
ATOM 4054 N MET A 511 -24.560 -19.476 33.407 1.00 24.81 N
ANISOU 4054 N MET A 511 3906 2524 2995 1292 -165 -454 N
ATOM 4055 CA AMET A 511 -23.526 -19.688 34.394 0.50 25.48 C
ANISOU 4055 CA AMET A 511 3962 2760 2958 1294 -170 -735 C
ATOM 4056 CA BMET A 511 -23.501 -19.730 34.377 0.50 24.64 C
ANISOU 4056 CA BMET A 511 4026 2553 2781 1494 -34 -858 C
ATOM 4057 CB AMET A 511 -23.333 -21.188 34.642 0.50 28.31 C
ANISOU 4057 CB AMET A 511 4490 2781 3483 1115 -325 -606 C
ATOM 4058 CB BMET A 511 -23.202 -21.232 34.514 0.50 27.97 C
ANISOU 4058 CB BMET A 511 4956 2476 3194 1578 178 -1193 C
ATOM 4059 CG AMET A 511 -24.625 -21.893 35.145 0.50 32.09 C
ANISOU 4059 CG AMET A 511 4730 3197 4266 654 -593 -289 C
ATOM 4060 CG BMET A 511 -23.638 -21.859 35.849 0.50 33.03 C
ANISOU 4060 CG BMET A 511 5787 2898 3862 1099 167 -640 C
ATOM 4061 SD AMET A 511 -25.362 -21.254 36.718 0.50 33.48 S
ANISOU 4061 SD AMET A 511 5078 2914 4727 -293 -378 -646 S
ATOM 4062 SD BMET A 511 -22.732 -21.262 37.311 0.50 37.25 S
ANISOU 4062 SD BMET A 511 6746 3124 4283 1361 -79 -1039 S
ATOM 4063 CE AMET A 511 -26.686 -20.225 36.084 0.50 31.97 C
ANISOU 4063 CE AMET A 511 4702 2928 4517 -671 -517 -383 C
ATOM 4064 CE BMET A 511 -21.032 -21.456 36.787 0.50 31.21 C
ANISOU 4064 CE BMET A 511 6135 2334 3386 1400 -85 -309 C
ATOM 4065 C MET A 511 -22.254 -18.988 33.897 1.00 24.44 C
ANISOU 4065 C MET A 511 3879 2861 2544 1543 -159 -780 C
ATOM 4066 O MET A 511 -21.927 -19.009 32.700 1.00 30.64 O
ANISOU 4066 O MET A 511 4006 4834 2799 1160 28 -1133 O
ATOM 4067 N ARG A 512 -21.580 -18.311 34.815 1.00 24.16 N
ANISOU 4067 N ARG A 512 3754 3138 2285 1361 -65 -556 N
ATOM 4068 CA ARG A 512 -20.366 -17.585 34.558 1.00 23.75 C
ANISOU 4068 CA ARG A 512 3622 3433 1967 1508 -270 -131 C
ATOM 4069 CB ARG A 512 -20.536 -16.129 35.005 1.00 25.56 C
ANISOU 4069 CB ARG A 512 3887 3489 2336 1115 -465 -284 C
ATOM 4070 CG ARG A 512 -21.633 -15.374 34.266 1.00 24.95 C
ANISOU 4070 CG ARG A 512 3729 3234 2514 924 -520 -390 C
ATOM 4071 CD ARG A 512 -22.006 -14.106 35.011 1.00 25.83 C
ANISOU 4071 CD ARG A 512 3459 3757 2597 898 -506 -837 C
ATOM 4072 NE ARG A 512 -22.736 -13.123 34.222 1.00 22.87 N
ANISOU 4072 NE ARG A 512 3188 3050 2449 311 -226 -585 N
ATOM 4073 CZ ARG A 512 -22.165 -12.219 33.424 1.00 22.47 C
ANISOU 4073 CZ ARG A 512 2869 3463 2204 476 -39 -629 C
ATOM 4074 NH1 ARG A 512 -20.876 -12.301 33.158 1.00 24.64 N
ANISOU 4074 NH1 ARG A 512 2623 3712 3027 627 -175 -1466 N
ATOM 4075 NH2 ARG A 512 -22.876 -11.231 32.910 1.00 22.02 N
ANISOU 4075 NH2 ARG A 512 3251 2810 2303 517 -131 -825 N
ATOM 4076 C ARG A 512 -19.243 -18.281 35.335 1.00 23.79 C
ANISOU 4076 C ARG A 512 3105 3982 1952 1220 -294 -221 C
ATOM 4077 O ARG A 512 -19.420 -18.667 36.485 1.00 30.32 O
ANISOU 4077 O ARG A 512 3494 5810 2214 1909 397 278 O
ATOM 4078 N VAL A 513 -18.101 -18.471 34.694 1.00 19.56 N
ANISOU 4078 N VAL A 513 2796 2537 2099 377 -218 -119 N
ATOM 4079 CA VAL A 513 -16.942 -18.964 35.414 1.00 19.62 C
ANISOU 4079 CA VAL A 513 2765 2512 2178 326 -181 -229 C
ATOM 4080 CB VAL A 513 -16.428 -20.295 34.839 1.00 20.77 C
ANISOU 4080 CB VAL A 513 3030 2517 2343 308 -247 -353 C
ATOM 4081 CG1 VAL A 513 -15.179 -20.771 35.556 1.00 21.81 C
ANISOU 4081 CG1 VAL A 513 3153 2627 2507 351 -318 -436 C
ATOM 4082 CG2 VAL A 513 -17.517 -21.368 34.901 1.00 22.09 C
ANISOU 4082 CG2 VAL A 513 2986 2733 2672 246 -106 -650 C
ATOM 4083 C VAL A 513 -15.899 -17.854 35.365 1.00 19.14 C
ANISOU 4083 C VAL A 513 2960 2384 1927 244 150 -80 C
ATOM 4084 O VAL A 513 -15.549 -17.394 34.285 1.00 23.54 O
ANISOU 4084 O VAL A 513 3444 3460 2038 -297 32 258 O
ATOM 4085 N MET A 514 -15.463 -17.412 36.539 1.00 16.95 N
ANISOU 4085 N MET A 514 2601 2023 1814 279 240 49 N
ATOM 4086 CA MET A 514 -14.473 -16.365 36.667 1.00 17.48 C
ANISOU 4086 CA MET A 514 2368 2038 2235 348 297 63 C
ATOM 4087 CB MET A 514 -14.953 -15.263 37.607 1.00 18.12 C
ANISOU 4087 CB MET A 514 2661 2049 2172 141 171 -50 C
ATOM 4088 CG MET A 514 -16.150 -14.522 37.068 1.00 18.45 C
ANISOU 4088 CG MET A 514 2821 2087 2102 230 349 40 C
ATOM 4089 SD MET A 514 -16.612 -13.188 38.173 1.00 19.35 S
ANISOU 4089 SD MET A 514 2887 1911 2553 246 116 -26 S
ATOM 4090 CE MET A 514 -17.999 -12.488 37.281 1.00 20.99 C
ANISOU 4090 CE MET A 514 2782 2361 2830 114 55 269 C
ATOM 4091 C MET A 514 -13.152 -16.956 37.170 1.00 18.46 C
ANISOU 4091 C MET A 514 2405 1793 2815 414 220 45 C
ATOM 4092 O MET A 514 -13.081 -18.063 37.659 1.00 19.88 O
ANISOU 4092 O MET A 514 2292 2430 2829 588 252 761 O
ATOM 4093 N GLY A 515 -12.083 -16.199 36.970 1.00 23.39 N
ANISOU 4093 N GLY A 515 2691 2220 3977 218 93 27 N
ATOM 4094 CA GLY A 515 -10.799 -16.575 37.479 1.00 23.85 C
ANISOU 4094 CA GLY A 515 2607 2643 3811 193 134 -387 C
ATOM 4095 C GLY A 515 -10.013 -17.336 36.443 1.00 22.92 C
ANISOU 4095 C GLY A 515 2679 2778 3251 248 170 -78 C
ATOM 4096 O GLY A 515 -9.775 -16.836 35.377 1.00 31.62 O
ANISOU 4096 O GLY A 515 4190 4193 3629 438 -87 329 O
ATOM 4097 N GLY A 516 -9.576 -18.543 36.814 1.00 22.26 N
ANISOU 4097 N GLY A 516 3131 2765 2561 391 722 -308 N
ATOM 4098 CA GLY A 516 -8.744 -19.391 36.000 1.00 19.51 C
ANISOU 4098 CA GLY A 516 2195 2568 2649 85 799 15 C
ATOM 4099 C GLY A 516 -7.279 -19.068 36.195 1.00 18.78 C
ANISOU 4099 C GLY A 516 2115 2314 2706 422 485 -211 C
ATOM 4100 O GLY A 516 -6.434 -19.711 35.573 1.00 19.67 O
ANISOU 4100 O GLY A 516 2167 2327 2980 161 684 -604 O
ATOM 4101 OXT GLY A 516 -6.956 -18.160 36.986 1.00 21.20 O
ANISOU 4101 OXT GLY A 516 2685 2687 2682 -40 182 -118 O
TER 4102 GLY A 516
HETATM12270 O4 SO4 A 601 2.510 -8.114 14.976 1.00 12.91 O
ANISOU12270 O4 SO4 A 601 1681 1544 1678 156 189 17 O
HETATM12271 S SO4 A 601 1.231 -8.457 14.280 1.00 12.82 S
ANISOU12271 S SO4 A 601 1676 1417 1775 82 153 123 S
HETATM12272 O1 SO4 A 601 0.989 -9.890 14.285 1.00 14.08 O
ANISOU12272 O1 SO4 A 601 1986 1394 1967 -92 -109 96 O
HETATM12273 O2 SO4 A 601 1.257 -7.966 12.882 1.00 12.85 O
ANISOU12273 O2 SO4 A 601 1862 1356 1663 26 -1 179 O
HETATM12274 O3 SO4 A 601 0.154 -7.772 15.001 1.00 13.55 O
ANISOU12274 O3 SO4 A 601 1629 1802 1715 174 176 -81 O
HETATM12275 O4 SO4 A 602 14.488 -27.568 32.390 0.70 19.20 O
ANISOU12275 O4 SO4 A 602 1805 2868 2619 324 -180 -525 O
HETATM12276 S SO4 A 602 13.170 -27.553 31.673 0.70 17.21 S
ANISOU12276 S SO4 A 602 1814 2214 2509 251 -184 -168 S
HETATM12277 O1 SO4 A 602 13.292 -26.653 30.500 0.70 18.22 O
ANISOU12277 O1 SO4 A 602 2277 2452 2193 -40 15 -205 O
HETATM12278 O2 SO4 A 602 12.889 -28.935 31.157 0.70 20.91 O
ANISOU12278 O2 SO4 A 602 2369 2388 3185 76 -502 -353 O
HETATM12279 O3 SO4 A 602 12.082 -27.012 32.576 0.70 14.93 O
ANISOU12279 O3 SO4 A 602 1656 1470 2545 514 -217 168 O
HETATM12280 O4 SO4 A 603 15.552 0.238 7.115 1.00 35.64 O
ANISOU12280 O4 SO4 A 603 5751 2327 5462 -217 -2223 -198 O
HETATM12281 S SO4 A 603 14.286 -0.256 6.526 1.00 29.97 S
ANISOU12281 S SO4 A 603 4577 2991 3818 555 -1157 -114 S
HETATM12282 O1 SO4 A 603 14.562 -1.422 5.668 1.00 28.87 O
ANISOU12282 O1 SO4 A 603 4288 2872 3807 50 -423 -261 O
HETATM12283 O2 SO4 A 603 13.690 0.856 5.795 1.00 29.52 O
ANISOU12283 O2 SO4 A 603 4286 3404 3523 831 -412 302 O
HETATM12284 O3 SO4 A 603 13.325 -0.753 7.565 1.00 36.93 O
ANISOU12284 O3 SO4 A 603 5873 3728 4429 142 -484 -419 O
HETATM12285 O4 SO4 A 604 -3.028 13.719 2.391 1.00 26.76 O
ANISOU12285 O4 SO4 A 604 4213 3121 2831 -204 275 -365 O
HETATM12286 S SO4 A 604 -3.694 13.439 1.094 1.00 30.54 S
ANISOU12286 S SO4 A 604 4963 3941 2700 1461 -96 -408 S
HETATM12287 O1 SO4 A 604 -2.925 12.765 0.046 1.00 31.85 O
ANISOU12287 O1 SO4 A 604 4769 3916 3415 295 755 -762 O
HETATM12288 O2 SO4 A 604 -4.198 14.683 0.487 1.00 34.33 O
ANISOU12288 O2 SO4 A 604 6036 4872 2132 2120 652 559 O
HETATM12289 O3 SO4 A 604 -4.799 12.469 1.498 1.00 37.58 O
ANISOU12289 O3 SO4 A 604 5708 5278 3293 645 -234 603 O
HETATM12290 O4 SO4 A 605 -27.177 -2.650 22.440 0.50 23.46 O
ANISOU12290 O4 SO4 A 605 3153 1743 4017 -12 -207 276 O
HETATM12291 S SO4 A 605 -28.210 -3.699 22.364 0.50 23.25 S
ANISOU12291 S SO4 A 605 3133 2410 3288 -211 -235 41 S
HETATM12292 O1 SO4 A 605 -27.986 -4.690 21.260 0.50 25.01 O
ANISOU12292 O1 SO4 A 605 3650 2280 3571 -24 141 26 O
HETATM12293 O2 SO4 A 605 -29.515 -3.033 22.155 0.50 20.93 O
ANISOU12293 O2 SO4 A 605 2720 1896 3335 -359 -318 205 O
HETATM12294 O3 SO4 A 605 -28.221 -4.430 23.659 0.50 21.76 O
ANISOU12294 O3 SO4 A 605 3353 2106 2808 -246 -55 -204 O
HETATM12295 O4 SO4 A 606 19.359 4.591 32.291 1.00 44.17 O
ANISOU12295 O4 SO4 A 606 4934 5027 6819 -1213 -2573 1817 O
HETATM12296 S SO4 A 606 20.752 4.996 31.891 1.00 41.53 S
ANISOU12296 S SO4 A 606 4438 5037 6303 -509 -2034 661 S
HETATM12297 O1 SO4 A 606 20.769 6.235 31.126 1.00 43.47 O
ANISOU12297 O1 SO4 A 606 6002 4790 5723 -1610 -1808 656 O
HETATM12298 O2 SO4 A 606 21.196 3.922 30.998 1.00 47.69 O
ANISOU12298 O2 SO4 A 606 5515 6210 6395 38 -291 512 O
HETATM12299 O3 SO4 A 606 21.574 5.112 33.100 1.00 47.65 O
ANISOU12299 O3 SO4 A 606 4347 6932 6825 -1096 -2177 608 O
HETATM12300 O4 SO4 A 607 28.493 -10.895 26.811 0.70 30.59 O
ANISOU12300 O4 SO4 A 607 2986 5164 3472 187 -234 557 O
HETATM12301 S SO4 A 607 28.778 -12.248 26.266 0.70 31.11 S
ANISOU12301 S SO4 A 607 2579 5712 3529 371 -531 159 S
HETATM12302 O1 SO4 A 607 29.708 -12.067 25.129 0.70 34.54 O
ANISOU12302 O1 SO4 A 607 2648 6072 4403 220 -90 419 O
HETATM12303 O2 SO4 A 607 27.539 -12.945 25.778 0.70 23.26 O
ANISOU12303 O2 SO4 A 607 2005 4082 2749 864 -375 499 O
HETATM12304 O3 SO4 A 607 29.445 -13.080 27.281 0.70 35.20 O
ANISOU12304 O3 SO4 A 607 3468 6019 3886 484 -591 518 O
HETATM12305 O4 SO4 A 608 -0.144 -1.687 4.057 1.00 35.57 O
ANISOU12305 O4 SO4 A 608 5338 3598 4577 161 -1396 -1707 O
HETATM12306 S SO4 A 608 -0.924 -1.818 2.762 1.00 28.02 S
ANISOU12306 S SO4 A 608 3588 3612 3445 163 -144 -946 S
HETATM12307 O1 SO4 A 608 -0.143 -0.842 1.931 1.00 48.90 O
ANISOU12307 O1 SO4 A 608 6872 5924 5781 -1232 -148 302 O
HETATM12308 O2 SO4 A 608 -0.755 -3.180 2.123 1.00 33.82 O
ANISOU12308 O2 SO4 A 608 4148 3963 4738 1445 -212 -1258 O
HETATM12309 O3 SO4 A 608 -2.355 -1.267 2.793 1.00 38.89 O
ANISOU12309 O3 SO4 A 608 4253 4718 5804 1080 -1222 -121 O
HETATM12310 O3 GOL A 609 3.124 0.788 21.052 1.00 14.64 O
ANISOU12310 O3 GOL A 609 2226 1731 1603 -201 236 -458 O
HETATM12311 C3 GOL A 609 3.618 0.691 22.428 1.00 19.10 C
ANISOU12311 C3 GOL A 609 2554 2710 1991 -382 39 -298 C
HETATM12312 C2 GOL A 609 4.549 1.877 22.824 1.00 18.18 C
ANISOU12312 C2 GOL A 609 2188 2316 2402 -82 247 -150 C
HETATM12313 O2 GOL A 609 5.759 1.908 22.013 1.00 15.33 O
ANISOU12313 O2 GOL A 609 1872 1995 1958 -125 199 -184 O
HETATM12314 C1 GOL A 609 3.764 3.228 22.824 1.00 19.98 C
ANISOU12314 C1 GOL A 609 2073 2416 3099 110 12 22 C
HETATM12315 O1 GOL A 609 3.199 3.721 21.526 1.00 16.89 O
ANISOU12315 O1 GOL A 609 1635 1917 2865 79 -53 -92 O
HETATM12316 O3 GOL A 610 -3.944 -7.235 31.548 1.00 24.51 O
ANISOU12316 O3 GOL A 610 3650 2653 3009 -319 565 -461 O
HETATM12317 C3 GOL A 610 -4.720 -7.596 32.689 1.00 27.11 C
ANISOU12317 C3 GOL A 610 4219 3390 2690 -498 317 -119 C
HETATM12318 C2 GOL A 610 -5.431 -8.928 32.429 1.00 24.51 C
ANISOU12318 C2 GOL A 610 3929 3053 2330 -87 259 -281 C
HETATM12319 O2 GOL A 610 -6.293 -8.789 31.295 1.00 28.00 O
ANISOU12319 O2 GOL A 610 3506 4066 3064 457 -39 -69 O
HETATM12320 C1 GOL A 610 -6.271 -9.263 33.652 1.00 24.71 C
ANISOU12320 C1 GOL A 610 3763 3220 2403 180 480 -536 C
HETATM12321 O1 GOL A 610 -7.099 -10.403 33.397 1.00 30.43 O
ANISOU12321 O1 GOL A 610 3993 3773 3793 -224 674 -1040 O
HETATM12322 O3 GOL A 611 18.684 -16.372 20.599 1.00 37.77 O
ANISOU12322 O3 GOL A 611 5600 4148 4601 1388 953 158 O
HETATM12323 C3 GOL A 611 18.566 -15.796 19.292 1.00 31.18 C
ANISOU12323 C3 GOL A 611 3112 4975 3757 21 833 249 C
HETATM12324 C2 GOL A 611 19.735 -14.834 18.994 1.00 24.47 C
ANISOU12324 C2 GOL A 611 2754 3192 3348 464 452 -50 C
HETATM12325 O2 GOL A 611 21.017 -15.486 18.901 1.00 23.78 O
ANISOU12325 O2 GOL A 611 2585 3579 2868 454 277 156 O
HETATM12326 C1 GOL A 611 19.886 -13.683 20.006 1.00 20.62 C
ANISOU12326 C1 GOL A 611 2085 3456 2292 216 359 276 C
HETATM12327 O1 GOL A 611 20.711 -12.645 19.388 1.00 17.77 O
ANISOU12327 O1 GOL A 611 1821 2678 2253 265 -145 73 O
HETATM12437 O HOH A 701 -12.845 18.668 25.853 1.00 27.33 O
ANISOU12437 O HOH A 701 3653 3565 3164 -285 418 -191 O
HETATM12438 O HOH A 702 -1.128 -7.939 44.756 1.00 42.63 O
ANISOU12438 O HOH A 702 5053 5508 5634 1894 2466 2887 O
HETATM12439 O HOH A 703 -3.278 0.598 3.952 1.00 31.82 O
ANISOU12439 O HOH A 703 2474 3920 5696 227 226 -1067 O
HETATM12440 O HOH A 704 -32.274 -1.249 29.960 1.00 29.10 O
ANISOU12440 O HOH A 704 3659 3350 4045 -29 -340 -74 O
HETATM12441 O HOH A 705 2.903 -3.702 42.800 1.00 38.25 O
ANISOU12441 O HOH A 705 4586 4034 5910 -80 1877 -1752 O
HETATM12442 O HOH A 706 -8.175 24.048 32.209 1.00 34.67 O
ANISOU12442 O HOH A 706 4187 5311 3672 -1901 -1510 2273 O
HETATM12443 O HOH A 707 27.106 -9.729 28.525 1.00 43.99 O
ANISOU12443 O HOH A 707 4884 6156 5673 452 -2093 76 O
HETATM12444 O HOH A 708 -29.848 -32.016 0.355 1.00 24.67 O
ANISOU12444 O HOH A 708 2820 3672 2879 66 -304 -599 O
HETATM12445 O HOH A 709 5.669 -2.567 21.671 1.00 17.53 O
ANISOU12445 O HOH A 709 2370 2832 1457 -333 -205 -117 O
HETATM12446 O HOH A 710 20.810 5.964 28.750 1.00 45.16 O
ANISOU12446 O HOH A 710 5768 6897 4492 -994 -461 -2138 O
HETATM12447 O HOH A 712 10.333 -4.032 32.675 1.00 25.91 O
ANISOU12447 O HOH A 712 3404 3515 2925 -241 -51 112 O
HETATM12448 O HOH A 713 6.435 -20.793 16.694 1.00 38.56 O
ANISOU12448 O HOH A 713 6303 5178 3167 -280 1008 180 O
HETATM12449 O HOH A 714 -3.627 26.441 23.167 1.00 41.31 O
ANISOU12449 O HOH A 714 4881 4618 6195 963 -1379 -786 O
HETATM12450 O HOH A 715 -2.138 -9.087 31.124 1.00 27.45 O
ANISOU12450 O HOH A 715 3372 4391 2667 732 72 -306 O
HETATM12451 O HOH A 716 -27.541 -2.718 25.483 1.00 23.49 O
ANISOU12451 O HOH A 716 3060 2398 3468 -92 678 -671 O
HETATM12452 O HOH A 717 2.064 26.088 22.866 1.00 24.12 O
ANISOU12452 O HOH A 717 3447 2113 3605 -735 1162 -436 O
HETATM12453 O HOH A 718 -6.948 15.737 46.724 1.00 22.20 O
ANISOU12453 O HOH A 718 3426 2356 2652 47 377 -419 O
HETATM12454 O HOH A 719 3.954 8.014 3.918 1.00 31.11 O
ANISOU12454 O HOH A 719 3315 5758 2747 1311 477 -1137 O
HETATM12455 O HOH A 720 2.243 24.002 28.452 1.00 46.60 O
ANISOU12455 O HOH A 720 6347 5659 5699 -4345 -2413 -477 O
HETATM12456 O HOH A 721 -16.346 11.856 23.478 1.00 27.43 O
ANISOU12456 O HOH A 721 4113 3491 2817 -32 149 -34 O
HETATM12457 O HOH A 723 5.785 14.904 34.611 1.00 36.28 O
ANISOU12457 O HOH A 723 5080 5136 3566 -21 633 -324 O
HETATM12458 O HOH A 724 -9.896 -11.395 38.462 1.00 24.87 O
ANISOU12458 O HOH A 724 2796 4727 1926 1111 245 -207 O
HETATM12459 O HOH A 725 6.329 -1.520 25.343 1.00 27.36 O
ANISOU12459 O HOH A 725 3331 3483 3582 -511 -505 -815 O
HETATM12460 O HOH A 726 8.056 26.350 4.284 1.00 40.70 O
ANISOU12460 O HOH A 726 5337 5835 4291 -1298 580 -1361 O
HETATM12461 O HOH A 727 -46.897 -24.191 17.043 1.00 56.62 O
ANISOU12461 O HOH A 727 7664 6709 7140 -1260 2580 -180 O
HETATM12462 O HOH A 728 -9.809 -14.469 49.974 1.00 45.17 O
ANISOU12462 O HOH A 728 4688 7978 4495 1165 477 1333 O
HETATM12463 O HOH A 729 8.744 15.568 7.086 1.00 18.51 O
ANISOU12463 O HOH A 729 2643 1942 2448 -550 401 84 O
HETATM12464 O HOH A 730 -5.204 -9.504 29.095 1.00 33.71 O
ANISOU12464 O HOH A 730 4740 5236 2832 1953 802 316 O
HETATM12465 O HOH A 731 2.600 -0.557 14.191 1.00 13.00 O
ANISOU12465 O HOH A 731 1781 1520 1638 34 84 -225 O
HETATM12466 O HOH A 732 10.116 7.544 23.869 1.00 21.70 O
ANISOU12466 O HOH A 732 2569 2872 2802 -121 -142 -264 O
HETATM12467 O HOH A 733 -23.805 13.807 36.241 1.00 46.52 O
ANISOU12467 O HOH A 733 4152 6037 7485 -420 -1633 2834 O
HETATM12468 O HOH A 734 -18.011 8.311 25.296 1.00 18.40 O
ANISOU12468 O HOH A 734 3146 1951 1893 58 -243 -265 O
HETATM12469 O HOH A 735 -5.135 19.951 39.174 1.00 25.81 O
ANISOU12469 O HOH A 735 4642 2654 2507 -619 452 28 O
HETATM12470 O HOH A 738 -1.009 -5.691 20.911 1.00 26.89 O
ANISOU12470 O HOH A 738 4930 2368 2918 22 1858 -279 O
HETATM12471 O HOH A 739 -33.786 -6.042 51.097 1.00 23.48 O
ANISOU12471 O HOH A 739 3080 2490 3350 -47 408 -83 O
HETATM12472 O HOH A 741 6.671 -26.223 46.288 1.00 26.22 O
ANISOU12472 O HOH A 741 3812 3287 2861 672 -594 383 O
HETATM12473 O HOH A 742 -27.439 -3.852 18.854 1.00 25.31 O
ANISOU12473 O HOH A 742 2865 2266 4484 -805 -767 523 O
HETATM12474 O HOH A 743 7.554 5.834 27.741 1.00 26.02 O
ANISOU12474 O HOH A 743 2579 4070 3236 267 -241 -1158 O
HETATM12475 O HOH A 744 -40.168 -1.345 28.390 1.00 29.11 O
ANISOU12475 O HOH A 744 3954 3806 3298 342 -1119 -581 O
HETATM12476 O HOH A 745 18.843 4.230 27.679 1.00 30.80 O
ANISOU12476 O HOH A 745 3884 3437 4378 129 -172 19 O
HETATM12477 O HOH A 746 19.751 18.608 14.779 1.00 42.21 O
ANISOU12477 O HOH A 746 1784 6078 8176 -954 -123 -111 O
HETATM12478 O HOH A 747 -33.789 -6.665 47.124 1.00 29.35 O
ANISOU12478 O HOH A 747 3193 3852 4107 -134 976 -305 O
HETATM12479 O HOH A 748 3.303 10.963 39.196 1.00 31.61 O
ANISOU12479 O HOH A 748 3571 4405 4034 -784 -554 -1730 O
HETATM12480 O HOH A 749 -35.946 -28.832 13.153 1.00 38.54 O
ANISOU12480 O HOH A 749 3669 4136 6838 -336 206 993 O
HETATM12481 O HOH A 750 21.965 -18.784 32.900 1.00 44.53 O
ANISOU12481 O HOH A 750 6810 5581 4526 1704 276 1210 O
HETATM12482 O HOH A 751 29.096 -6.692 13.050 1.00 37.69 O
ANISOU12482 O HOH A 751 5794 5213 3310 -1527 424 -551 O
HETATM12483 O HOH A 752 -17.380 -8.764 35.823 1.00 16.82 O
ANISOU12483 O HOH A 752 3314 1349 1727 -9 -374 11 O
HETATM12484 O HOH A 753 -26.897 -0.107 24.335 1.00 19.38 O
ANISOU12484 O HOH A 753 2892 2282 2189 -156 246 62 O
HETATM12485 O HOH A 754 -1.024 -24.094 31.511 1.00 26.95 O
ANISOU12485 O HOH A 754 5384 2968 1885 -1241 -844 362 O
HETATM12486 O HOH A 755 6.407 -7.510 23.578 1.00 14.12 O
ANISOU12486 O HOH A 755 1611 1908 1845 -95 -140 -275 O
HETATM12487 O HOH A 756 17.912 -20.007 25.813 1.00 31.93 O
ANISOU12487 O HOH A 756 4001 3651 4480 879 255 -404 O
HETATM12488 O HOH A 757 2.681 18.655 4.254 1.00 29.38 O
ANISOU12488 O HOH A 757 3384 4091 3687 -118 240 1008 O
HETATM12489 O HOH A 758 -4.250 -3.722 19.338 1.00 28.63 O
ANISOU12489 O HOH A 758 4719 1534 4624 -624 147 -236 O
HETATM12490 O HOH A 759 22.940 -7.746 33.727 1.00 31.08 O
ANISOU12490 O HOH A 759 3248 3825 4735 601 1141 168 O
HETATM12491 O HOH A 760 20.531 -16.702 38.402 1.00 36.52 O
ANISOU12491 O HOH A 760 5332 5312 3231 1531 -1407 -338 O
HETATM12492 O HOH A 761 -3.723 -19.815 35.573 1.00 14.04 O
ANISOU12492 O HOH A 761 2234 1738 1360 203 122 71 O
HETATM12493 O HOH A 762 -13.217 -13.096 46.579 1.00 21.90 O
ANISOU12493 O HOH A 762 2526 2403 3390 371 509 22 O
HETATM12494 O HOH A 763 -13.303 -3.871 17.890 1.00 35.79 O
ANISOU12494 O HOH A 763 4387 5699 3510 -949 -1598 534 O
HETATM12495 O HOH A 764 -39.593 -10.061 33.121 1.00 40.99 O
ANISOU12495 O HOH A 764 6897 4870 3805 -1304 -8 858 O
HETATM12496 O HOH A 765 5.060 29.329 19.280 1.00 54.49 O
ANISOU12496 O HOH A 765 8417 5498 6788 -1231 2796 -841 O
HETATM12497 O HOH A 766 -15.900 -2.370 52.507 1.00 22.76 O
ANISOU12497 O HOH A 766 3863 2937 1846 70 -377 -562 O
HETATM12498 O HOH A 767 7.907 -0.938 32.839 1.00 25.32 O
ANISOU12498 O HOH A 767 3237 3193 3187 473 -122 -116 O
HETATM12499 O HOH A 769 13.050 28.724 8.546 1.00 36.87 O
ANISOU12499 O HOH A 769 4006 3471 6533 -1581 1934 -679 O
HETATM12500 O HOH A 770 1.733 13.639 10.315 1.00 16.44 O
ANISOU12500 O HOH A 770 1977 2099 2169 -71 -33 346 O
HETATM12501 O HOH A 771 30.709 0.952 18.005 1.00 47.09 O
ANISOU12501 O HOH A 771 4735 5297 7859 -1292 -1564 1711 O
HETATM12502 O HOH A 772 -45.456 -21.013 18.402 1.00 31.33 O
ANISOU12502 O HOH A 772 4729 3825 3350 -808 24 -152 O
HETATM12503 O HOH A 773 6.580 6.928 18.312 1.00 13.17 O
ANISOU12503 O HOH A 773 1744 1533 1726 -104 -113 -479 O
HETATM12504 O HOH A 774 -8.864 21.483 24.558 1.00 21.83 O
ANISOU12504 O HOH A 774 3686 1925 2682 92 -629 -572 O
HETATM12505 O HOH A 776 0.675 21.698 36.073 1.00 25.10 O
ANISOU12505 O HOH A 776 3951 2689 2896 -972 736 -564 O
HETATM12506 O HOH A 777 20.002 3.507 25.349 1.00 36.21 O
ANISOU12506 O HOH A 777 6016 2995 4745 12 201 -542 O
HETATM12507 O HOH A 779 -9.430 -5.095 27.097 1.00 21.56 O
ANISOU12507 O HOH A 779 3009 2185 2995 -678 -231 256 O
HETATM12508 O HOH A 780 18.038 -17.373 31.663 1.00 22.56 O
ANISOU12508 O HOH A 780 2113 3405 3051 472 -648 588 O
HETATM12509 O HOH A 781 -9.676 14.561 45.242 1.00 23.79 O
ANISOU12509 O HOH A 781 3066 4086 1888 -311 424 239 O
HETATM12510 O HOH A 782 -10.789 -21.865 51.861 1.00 37.57 O
ANISOU12510 O HOH A 782 4904 5168 4200 460 1554 -660 O
HETATM12511 O HOH A 783 -4.610 5.038 47.529 1.00 26.87 O
ANISOU12511 O HOH A 783 4204 3695 2308 -1155 -659 -398 O
HETATM12512 O HOH A 784 14.153 25.219 16.820 1.00 35.36 O
ANISOU12512 O HOH A 784 4800 3638 4995 -1332 -282 12 O
HETATM12513 O HOH A 785 15.241 13.675 24.308 1.00 38.33 O
ANISOU12513 O HOH A 785 4196 5960 4403 -2118 -899 907 O
HETATM12514 O HOH A 786 22.019 -13.050 37.704 1.00 37.30 O
ANISOU12514 O HOH A 786 4021 6428 3721 -155 109 90 O
HETATM12515 O HOH A 787 5.341 4.861 20.026 1.00 14.24 O
ANISOU12515 O HOH A 787 1987 1576 1846 -7 -206 -50 O
HETATM12516 O HOH A 788 -20.935 2.826 52.449 1.00 21.55 O
ANISOU12516 O HOH A 788 2163 3877 2147 668 580 402 O
HETATM12517 O HOH A 789 11.181 1.104 9.268 1.00 25.23 O
ANISOU12517 O HOH A 789 3157 3211 3217 -1150 -937 767 O
HETATM12518 O HOH A 790 -20.390 15.051 45.812 1.00 37.50 O
ANISOU12518 O HOH A 790 2909 4279 7059 -320 608 -2787 O
HETATM12519 O HOH A 791 -22.014 -9.871 25.938 1.00 38.45 O
ANISOU12519 O HOH A 791 4981 3801 5824 -800 650 -9 O
HETATM12520 O HOH A 792 -14.597 -47.635 14.869 1.00 22.32 O
ANISOU12520 O HOH A 792 3028 2709 2742 309 -361 414 O
HETATM12521 O HOH A 793 1.549 -28.352 35.354 1.00 26.02 O
ANISOU12521 O HOH A 793 2912 2580 4391 719 382 311 O
HETATM12522 O HOH A 794 12.786 3.156 20.525 1.00 22.88 O
ANISOU12522 O HOH A 794 1747 4337 2607 522 -44 -1507 O
HETATM12523 O HOH A 795 -23.066 13.363 27.560 1.00 18.58 O
ANISOU12523 O HOH A 795 2767 2102 2188 154 221 -424 O
HETATM12524 O HOH A 796 22.131 -4.568 1.248 1.00 23.34 O
ANISOU12524 O HOH A 796 3207 3070 2588 -410 912 -345 O
HETATM12525 O HOH A 797 -20.916 18.456 31.772 1.00 38.37 O
ANISOU12525 O HOH A 797 6465 2330 5784 771 428 1185 O
HETATM12526 O HOH A 798 21.921 -17.633 30.423 1.00 27.61 O
ANISOU12526 O HOH A 798 2403 4060 4024 1008 264 756 O
HETATM12527 O HOH A 799 7.182 -0.470 22.385 1.00 21.79 O
ANISOU12527 O HOH A 799 2227 2429 3621 -176 -327 -242 O
HETATM12528 O HOH A 800 -1.781 -2.957 41.922 1.00 37.48 O
ANISOU12528 O HOH A 800 5485 4541 4213 -750 473 -2065 O
HETATM12529 O HOH A 801 5.782 24.011 10.299 1.00 22.66 O
ANISOU12529 O HOH A 801 2850 3244 2517 -1072 369 -248 O
HETATM12530 O HOH A 802 29.627 -6.412 28.478 1.00 44.77 O
ANISOU12530 O HOH A 802 4866 7146 4998 939 -1983 -1001 O
HETATM12531 O HOH A 803 24.969 -7.279 10.006 1.00 29.47 O
ANISOU12531 O HOH A 803 5230 3177 2789 -1059 1087 -458 O
HETATM12532 O HOH A 805 -23.105 -1.789 46.681 1.00 12.72 O
ANISOU12532 O HOH A 805 2021 1432 1380 302 447 -267 O
HETATM12533 O HOH A 806 -2.517 -31.459 49.335 1.00 34.55 O
ANISOU12533 O HOH A 806 4739 3722 4665 -208 1216 1121 O
HETATM12534 O HOH A 807 0.696 1.717 25.678 1.00 21.42 O
ANISOU12534 O HOH A 807 3455 1731 2951 89 -662 92 O
HETATM12535 O HOH A 808 -0.120 -22.110 28.482 1.00 26.20 O
ANISOU12535 O HOH A 808 3968 3521 2462 -1535 -1344 1212 O
HETATM12536 O HOH A 809 -1.712 28.791 12.548 1.00 35.10 O
ANISOU12536 O HOH A 809 5113 2836 5387 -765 1715 -1 O
HETATM12537 O HOH A 810 15.389 -2.264 39.804 1.00 36.18 O
ANISOU12537 O HOH A 810 5233 4732 3778 185 -259 -1498 O
HETATM12538 O HOH A 811 -1.311 -9.291 41.809 1.00 16.74 O
ANISOU12538 O HOH A 811 2387 2027 1946 97 9 41 O
HETATM12539 O HOH A 812 14.005 -11.249 48.724 1.00 46.56 O
ANISOU12539 O HOH A 812 3648 9037 5003 -1183 -638 -2138 O
HETATM12540 O HOH A 813 11.588 5.098 23.950 1.00 18.41 O
ANISOU12540 O HOH A 813 2472 2284 2236 -428 -245 -445 O
HETATM12541 O HOH A 814 9.821 -9.029 45.906 1.00 46.78 O
ANISOU12541 O HOH A 814 8002 6145 3625 2712 -2205 -1757 O
HETATM12542 O HOH A 815 -37.591 -2.137 22.453 1.00 14.59 O
ANISOU12542 O HOH A 815 1692 2047 1803 -255 64 -308 O
HETATM12543 O HOH A 816 8.418 25.327 6.771 1.00 31.91 O
ANISOU12543 O HOH A 816 5577 2830 3714 -434 1372 -282 O
HETATM12544 O HOH A 817 10.060 0.391 11.426 1.00 22.05 O
ANISOU12544 O HOH A 817 2886 2212 3278 -580 623 -1207 O
HETATM12545 O HOH A 818 11.753 -7.899 27.692 1.00 13.69 O
ANISOU12545 O HOH A 818 1808 1799 1594 -59 -248 -76 O
HETATM12546 O HOH A 819 19.040 -11.050 17.938 1.00 14.75 O
ANISOU12546 O HOH A 819 2124 1639 1838 208 -99 -120 O
HETATM12547 O HOH A 820 -16.671 2.341 27.406 1.00 20.29 O
ANISOU12547 O HOH A 820 4799 1552 1358 -1012 107 -53 O
HETATM12548 O HOH A 821 8.804 13.675 30.015 1.00 36.45 O
ANISOU12548 O HOH A 821 5764 3428 4656 364 -1857 -1063 O
HETATM12549 O HOH A 822 -35.309 -31.199 8.848 1.00 37.70 O
ANISOU12549 O HOH A 822 4967 3330 6027 -1276 -1160 484 O
HETATM12550 O HOH A 823 -24.229 -11.963 49.739 1.00 33.54 O
ANISOU12550 O HOH A 823 6033 3023 3688 131 486 1153 O
HETATM12551 O HOH A 824 2.790 18.757 29.676 1.00 17.98 O
ANISOU12551 O HOH A 824 2521 2204 2104 130 361 -253 O
HETATM12552 O HOH A 825 11.337 -27.171 28.719 1.00 17.33 O
ANISOU12552 O HOH A 825 2396 2018 2167 504 41 -20 O
HETATM12553 O HOH A 826 19.827 0.639 18.740 1.00 35.89 O
ANISOU12553 O HOH A 826 5343 4002 4290 540 223 67 O
HETATM12554 O HOH A 827 -10.010 21.911 16.980 1.00 23.12 O
ANISOU12554 O HOH A 827 2575 2587 3622 -38 224 523 O
HETATM12555 O HOH A 828 -4.635 -12.038 22.773 1.00 21.29 O
ANISOU12555 O HOH A 828 2188 2942 2958 333 -383 -55 O
HETATM12556 O HOH A 829 14.979 23.183 5.286 1.00 35.59 O
ANISOU12556 O HOH A 829 5087 4103 4330 -1192 1850 635 O
HETATM12557 O HOH A 830 1.001 -2.970 12.662 1.00 16.59 O
ANISOU12557 O HOH A 830 2500 1893 1911 417 265 -88 O
HETATM12558 O HOH A 831 -8.231 4.577 50.831 1.00 47.19 O
ANISOU12558 O HOH A 831 6618 5262 6049 208 -2516 -1564 O
HETATM12559 O HOH A 832 -32.547 1.446 38.643 1.00 26.66 O
ANISOU12559 O HOH A 832 5073 3052 2002 -2305 624 -734 O
HETATM12560 O HOH A 833 -8.463 2.086 40.707 1.00 14.80 O
ANISOU12560 O HOH A 833 1980 2024 1617 65 -50 -322 O
HETATM12561 O HOH A 834 4.795 0.530 26.189 1.00 26.01 O
ANISOU12561 O HOH A 834 3270 3329 3281 853 626 724 O
HETATM12562 O HOH A 835 -37.245 0.334 37.262 1.00 37.31 O
ANISOU12562 O HOH A 835 6373 3594 4207 -866 2734 -442 O
HETATM12563 O HOH A 836 30.774 3.129 20.854 1.00 45.27 O
ANISOU12563 O HOH A 836 5770 5630 5799 76 2093 -513 O
HETATM12564 O HOH A 837 -6.748 -14.947 44.016 1.00 19.93 O
ANISOU12564 O HOH A 837 3627 1808 2135 603 629 -72 O
HETATM12565 O HOH A 838 2.074 -2.586 41.095 1.00 28.45 O
ANISOU12565 O HOH A 838 5765 2978 2063 -1004 -605 276 O
HETATM12566 O HOH A 839 -11.816 11.702 18.888 1.00 14.24 O
ANISOU12566 O HOH A 839 2110 1544 1754 -326 604 -290 O
HETATM12567 O HOH A 840 -12.334 4.618 14.276 1.00 12.35 O
ANISOU12567 O HOH A 840 1629 1349 1715 184 -186 -76 O
HETATM12568 O HOH A 841 11.443 -6.187 9.286 1.00 14.24 O
ANISOU12568 O HOH A 841 1973 1581 1854 -45 106 5 O
HETATM12569 O HOH A 842 12.804 19.818 4.982 1.00 36.88 O
ANISOU12569 O HOH A 842 4159 4340 5512 437 179 -777 O
HETATM12570 O HOH A 843 -23.774 17.571 38.896 1.00 38.45 O
ANISOU12570 O HOH A 843 4476 3965 6167 1056 1404 1526 O
HETATM12571 O HOH A 844 7.191 5.492 24.084 1.00 16.31 O
ANISOU12571 O HOH A 844 2324 1795 2075 134 326 -109 O
HETATM12572 O HOH A 845 -7.151 24.133 30.022 1.00 24.58 O
ANISOU12572 O HOH A 845 2874 2319 4144 -238 -216 -1118 O
HETATM12573 O HOH A 846 -0.660 11.075 10.870 1.00 12.38 O
ANISOU12573 O HOH A 846 1718 1497 1487 -76 19 98 O
HETATM12574 O HOH A 847 -30.497 -5.884 23.876 1.00 34.08 O
ANISOU12574 O HOH A 847 3128 7143 2676 -1020 -226 -743 O
HETATM12575 O HOH A 848 -14.902 -17.699 47.083 1.00 31.82 O
ANISOU12575 O HOH A 848 6104 2782 3204 2105 -1221 -588 O
HETATM12576 O HOH A 849 23.072 -2.443 26.424 1.00 25.19 O
ANISOU12576 O HOH A 849 3790 2877 2902 -1512 -562 -519 O
HETATM12577 O HOH A 850 -9.894 -0.096 50.174 1.00 22.05 O
ANISOU12577 O HOH A 850 2846 3374 2155 425 -133 118 O
HETATM12578 O HOH A 851 13.196 -18.177 45.512 1.00 32.37 O
ANISOU12578 O HOH A 851 4204 5066 3026 996 249 929 O
HETATM12579 O HOH A 852 11.660 -28.259 34.972 1.00 24.30 O
ANISOU12579 O HOH A 852 2615 3460 3155 554 -455 884 O
HETATM12580 O HOH A 853 -22.228 11.455 48.422 1.00 33.57 O
ANISOU12580 O HOH A 853 2661 5383 4709 786 -705 -3335 O
HETATM12581 O HOH A 854 -17.033 16.102 39.434 1.00 15.67 O
ANISOU12581 O HOH A 854 2800 1556 1596 15 233 10 O
HETATM12582 O HOH A 855 -40.361 -27.566 13.492 1.00 29.86 O
ANISOU12582 O HOH A 855 4116 3755 3475 176 617 1096 O
HETATM12583 O HOH A 856 0.341 23.928 22.735 1.00 19.53 O
ANISOU12583 O HOH A 856 3099 2234 2087 -572 403 -140 O
HETATM12584 O HOH A 857 -3.670 13.816 47.283 1.00 21.27 O
ANISOU12584 O HOH A 857 3726 2030 2324 -283 -339 -425 O
HETATM12585 O HOH A 859 -26.966 12.416 41.515 1.00 21.86 O
ANISOU12585 O HOH A 859 2154 2465 3688 157 821 468 O
HETATM12586 O HOH A 860 27.230 -13.819 22.981 1.00 36.18 O
ANISOU12586 O HOH A 860 3513 5909 4325 1851 372 -94 O
HETATM12587 O HOH A 861 -7.591 25.572 17.997 1.00 30.99 O
ANISOU12587 O HOH A 861 4363 2155 5254 597 -62 -536 O
HETATM12588 O HOH A 862 14.482 22.842 22.179 1.00 42.27 O
ANISOU12588 O HOH A 862 5212 6513 4335 -1703 -135 -1787 O
HETATM12589 O HOH A 863 -32.105 7.442 30.475 1.00 21.72 O
ANISOU12589 O HOH A 863 2390 3442 2417 -218 365 -592 O
HETATM12590 O HOH A 864 -38.237 -27.620 11.699 1.00 23.24 O
ANISOU12590 O HOH A 864 3101 2213 3513 -340 454 416 O
HETATM12591 O HOH A 865 -21.024 3.862 29.629 1.00 14.14 O
ANISOU12591 O HOH A 865 1942 1288 2140 -89 -36 -107 O
HETATM12592 O HOH A 866 -5.099 -14.766 34.391 1.00 35.48 O
ANISOU12592 O HOH A 866 3607 6501 3374 -250 -232 1389 O
HETATM12593 O HOH A 867 13.112 -8.196 14.572 1.00 13.29 O
ANISOU12593 O HOH A 867 1544 1723 1781 83 72 -82 O
HETATM12594 O HOH A 869 2.691 -11.135 46.432 1.00 35.21 O
ANISOU12594 O HOH A 869 3172 6257 3948 -742 -259 688 O
HETATM12595 O HOH A 870 13.777 11.594 16.397 1.00 38.65 O
ANISOU12595 O HOH A 870 6478 3798 4409 744 -1783 -640 O
HETATM12596 O HOH A 871 9.159 -28.421 36.251 1.00 25.78 O
ANISOU12596 O HOH A 871 2276 3642 3876 1080 278 1578 O
HETATM12597 O HOH A 872 1.304 3.125 36.562 1.00 19.41 O
ANISOU12597 O HOH A 872 3343 1928 2102 -72 435 -39 O
HETATM12598 O HOH A 873 -27.203 0.445 47.544 1.00 15.54 O
ANISOU12598 O HOH A 873 2160 1878 1865 83 366 -82 O
HETATM12599 O HOH A 874 -34.763 2.516 41.125 1.00 39.38 O
ANISOU12599 O HOH A 874 5575 4550 4836 -2224 3024 -2438 O
HETATM12600 O HOH A 875 -22.106 -47.912 13.941 1.00 27.10 O
ANISOU12600 O HOH A 875 4399 2571 3324 -767 -820 -25 O
HETATM12601 O HOH A 877 3.753 -2.750 33.146 1.00 23.02 O
ANISOU12601 O HOH A 877 2761 3015 2969 529 107 -1001 O
HETATM12602 O HOH A 878 2.344 2.751 30.079 1.00 21.04 O
ANISOU12602 O HOH A 878 3575 2191 2226 65 579 -131 O
HETATM12603 O HOH A 879 21.800 -8.893 15.067 1.00 17.26 O
ANISOU12603 O HOH A 879 1957 2462 2139 -244 -96 33 O
HETATM12604 O HOH A 880 -0.795 -2.392 37.733 1.00 29.48 O
ANISOU12604 O HOH A 880 2309 3668 5221 -573 1092 -2408 O
HETATM12605 O HOH A 881 23.527 -13.706 21.531 1.00 23.19 O
ANISOU12605 O HOH A 881 3174 2672 2962 408 175 35 O
HETATM12606 O HOH A 882 16.619 3.189 9.634 1.00 26.22 O
ANISOU12606 O HOH A 882 2582 2820 4558 -348 -676 736 O
HETATM12607 O HOH A 883 -10.720 2.052 17.663 1.00 19.53 O
ANISOU12607 O HOH A 883 2525 2805 2089 -601 -72 159 O
HETATM12608 O HOH A 884 7.900 2.407 10.176 1.00 20.08 O
ANISOU12608 O HOH A 884 2797 1535 3297 -250 -413 -232 O
HETATM12609 O HOH A 885 3.438 26.457 15.767 1.00 38.22 O
ANISOU12609 O HOH A 885 4325 4424 5772 -785 1947 1101 O
HETATM12610 O HOH A 886 18.232 2.943 30.142 1.00 21.51 O
ANISOU12610 O HOH A 886 2638 2381 3153 -822 -475 -79 O
HETATM12611 O HOH A 887 -26.961 6.575 29.363 1.00 16.10 O
ANISOU12611 O HOH A 887 2546 1844 1724 229 302 -151 O
HETATM12612 O HOH A 888 -13.367 16.556 27.391 1.00 24.64 O
ANISOU12612 O HOH A 888 4285 2097 2979 976 12 -293 O
HETATM12613 O HOH A 889 -2.301 -22.116 36.105 1.00 14.24 O
ANISOU12613 O HOH A 889 1723 2033 1651 224 134 308 O
HETATM12614 O HOH A 890 -19.489 11.239 45.248 1.00 15.94 O
ANISOU12614 O HOH A 890 2331 1607 2117 157 760 -149 O
HETATM12615 O HOH A 891 -26.277 -41.716 16.530 1.00 31.31 O
ANISOU12615 O HOH A 891 3442 5072 3381 590 750 1480 O
HETATM12616 O HOH A 892 9.979 -1.357 38.846 1.00 44.47 O
ANISOU12616 O HOH A 892 5531 4965 6398 -1757 2779 -1541 O
HETATM12617 O HOH A 893 1.687 -27.387 40.354 1.00 18.84 O
ANISOU12617 O HOH A 893 2657 2246 2254 503 200 164 O
HETATM12618 O HOH A 894 2.202 7.704 33.448 1.00 19.48 O
ANISOU12618 O HOH A 894 2691 2861 1847 -458 -189 -570 O
HETATM12619 O HOH A 895 23.027 -7.398 24.064 1.00 18.11 O
ANISOU12619 O HOH A 895 1543 3237 2098 91 -192 150 O
HETATM12620 O HOH A 896 21.265 -17.060 16.597 1.00 25.03 O
ANISOU12620 O HOH A 896 3420 2747 3340 287 -198 -141 O
HETATM12621 O HOH A 897 12.678 25.209 20.512 1.00 41.36 O
ANISOU12621 O HOH A 897 6406 4886 4420 -279 -548 -2236 O
HETATM12622 O HOH A 898 -20.713 0.541 53.830 1.00 25.82 O
ANISOU12622 O HOH A 898 4293 3077 2440 575 -422 -99 O
HETATM12623 O HOH A 899 11.445 16.235 8.182 1.00 20.29 O
ANISOU12623 O HOH A 899 2472 2525 2712 -709 101 212 O
HETATM12624 O HOH A 900 -1.733 -15.540 21.188 1.00 18.72 O
ANISOU12624 O HOH A 900 2634 2253 2225 -45 -357 -238 O
HETATM12625 O HOH A 901 -33.273 -8.680 45.144 1.00 31.85 O
ANISOU12625 O HOH A 901 3791 4218 4092 -600 461 1181 O
HETATM12626 O HOH A 902 7.558 -0.574 11.725 1.00 17.51 O
ANISOU12626 O HOH A 902 2191 1703 2755 -136 79 317 O
HETATM12627 O HOH A 903 -36.100 -3.568 37.423 1.00 30.62 O
ANISOU12627 O HOH A 903 5309 3283 3040 -934 1033 -351 O
HETATM12628 O HOH A 904 -8.105 -4.669 36.876 1.00 19.14 O
ANISOU12628 O HOH A 904 3331 2118 1821 257 -127 -13 O
HETATM12629 O HOH A 905 -2.554 -7.986 18.121 1.00 32.78 O
ANISOU12629 O HOH A 905 4749 4014 3692 1831 1179 821 O
HETATM12630 O HOH A 906 -6.622 21.541 41.018 1.00 18.07 O
ANISOU12630 O HOH A 906 3223 2020 1623 -881 -2 -108 O
HETATM12631 O HOH A 907 -9.341 -4.153 50.463 1.00 55.34 O
ANISOU12631 O HOH A 907 8434 4643 7950 1627 1523 1851 O
HETATM12632 O HOH A 908 17.181 -26.675 24.518 1.00 41.83 O
ANISOU12632 O HOH A 908 3733 5902 6256 199 251 -2023 O
HETATM12633 O HOH A 909 -7.391 1.760 47.990 1.00 21.44 O
ANISOU12633 O HOH A 909 2900 3366 1877 148 323 18 O
HETATM12634 O HOH A 910 -25.188 4.388 40.050 1.00 14.16 O
ANISOU12634 O HOH A 910 2160 1519 1700 73 452 7 O
HETATM12635 O HOH A 911 6.239 -26.181 49.760 1.00 42.07 O
ANISOU12635 O HOH A 911 4856 6923 4204 2326 -193 175 O
HETATM12636 O HOH A 912 -15.988 21.728 42.673 1.00 26.59 O
ANISOU12636 O HOH A 912 2730 4460 2910 -59 907 -671 O
HETATM12637 O HOH A 913 -27.565 11.396 26.674 1.00 17.32 O
ANISOU12637 O HOH A 913 2583 1989 2008 -57 270 -139 O
HETATM12638 O HOH A 914 -18.934 0.577 27.477 1.00 16.65 O
ANISOU12638 O HOH A 914 3020 1653 1651 -115 177 -67 O
HETATM12639 O HOH A 915 6.785 11.943 5.049 1.00 28.89 O
ANISOU12639 O HOH A 915 3817 4412 2746 -1058 1128 -60 O
HETATM12640 O HOH A 916 15.938 12.920 12.178 1.00 44.56 O
ANISOU12640 O HOH A 916 3702 5199 8031 602 1414 2755 O
HETATM12641 O HOH A 917 9.128 -4.931 43.331 1.00 41.67 O
ANISOU12641 O HOH A 917 6477 3926 5429 1113 -577 -481 O
HETATM12642 O HOH A 918 4.375 5.154 5.811 1.00 17.13 O
ANISOU12642 O HOH A 918 2513 2241 1753 29 247 -248 O
HETATM12643 O HOH A 919 15.329 -20.616 28.769 1.00 20.35 O
ANISOU12643 O HOH A 919 2781 2707 2244 -285 606 -271 O
HETATM12644 O HOH A 920 -27.865 9.980 38.248 1.00 28.38 O
ANISOU12644 O HOH A 920 4754 3650 2377 995 -125 154 O
HETATM12645 O HOH A 921 -12.018 -20.350 50.462 1.00 33.81 O
ANISOU12645 O HOH A 921 5121 4779 2944 -724 780 74 O
HETATM12646 O HOH A 922 17.788 0.870 16.909 1.00 29.56 O
ANISOU12646 O HOH A 922 3314 3923 3992 -840 808 -409 O
HETATM12647 O HOH A 923 -32.414 -8.270 37.403 1.00 25.00 O
ANISOU12647 O HOH A 923 2519 3549 3428 143 411 780 O
HETATM12648 O HOH A 924 6.734 -10.715 45.990 1.00 32.09 O
ANISOU12648 O HOH A 924 3834 5455 2904 977 532 126 O
HETATM12649 O HOH A 925 27.701 -1.247 17.313 1.00 24.14 O
ANISOU12649 O HOH A 925 2148 3939 3083 -787 302 -21 O
HETATM12650 O HOH A 926 8.982 7.722 26.429 1.00 26.67 O
ANISOU12650 O HOH A 926 2970 3621 3540 -48 -428 -412 O
HETATM12651 O HOH A 927 10.284 10.193 5.278 1.00 38.63 O
ANISOU12651 O HOH A 927 7737 4234 2704 1129 1209 -31 O
HETATM12652 O HOH A 928 3.823 -23.210 51.527 1.00 30.57 O
ANISOU12652 O HOH A 928 4393 3963 3258 310 -243 408 O
HETATM12653 O HOH A 929 14.669 -5.471 21.782 1.00 17.16 O
ANISOU12653 O HOH A 929 2050 2593 1875 254 -86 -391 O
HETATM12654 O HOH A 930 17.199 -18.563 22.540 1.00 27.41 O
ANISOU12654 O HOH A 930 2899 2310 5203 100 173 -119 O
HETATM12655 O HOH A 931 -22.673 -2.071 41.827 1.00 12.49 O
ANISOU12655 O HOH A 931 1738 1473 1534 229 379 -184 O
HETATM12656 O HOH A 932 -4.987 -15.626 41.267 1.00 16.29 O
ANISOU12656 O HOH A 932 2311 2014 1864 680 353 -37 O
HETATM12657 O HOH A 933 26.004 -5.905 33.458 1.00 41.21 O
ANISOU12657 O HOH A 933 4681 5829 5147 -1038 -328 -7 O
HETATM12658 O HOH A 934 -5.503 22.290 37.536 1.00 15.23 O
ANISOU12658 O HOH A 934 2263 1560 1963 -356 225 -419 O
HETATM12659 O HOH A 935 -19.788 16.637 38.892 1.00 21.57 O
ANISOU12659 O HOH A 935 3252 2008 2935 155 410 31 O
HETATM12660 O HOH A 936 -17.466 -28.678 35.267 1.00 43.55 O
ANISOU12660 O HOH A 936 4222 6455 5868 1533 563 811 O
HETATM12661 O HOH A 937 25.988 -6.954 21.532 1.00 20.67 O
ANISOU12661 O HOH A 937 1805 3445 2600 270 -193 61 O
HETATM12662 O HOH A 938 -7.188 10.219 13.861 1.00 10.96 O
ANISOU12662 O HOH A 938 1497 1663 1002 -8 102 -165 O
HETATM12663 O HOH A 939 27.974 -2.635 33.948 1.00 44.33 O
ANISOU12663 O HOH A 939 4021 6742 6079 -1574 -1644 211 O
HETATM12664 O HOH A 940 -2.761 15.333 5.413 1.00 24.49 O
ANISOU12664 O HOH A 940 2462 1890 4951 -83 -442 -185 O
HETATM12665 O HOH A 941 8.604 7.105 16.397 1.00 13.58 O
ANISOU12665 O HOH A 941 2021 1479 1660 -141 65 -130 O
HETATM12666 O HOH A 942 -6.808 -34.522 42.233 1.00 35.91 O
ANISOU12666 O HOH A 942 6688 3328 3628 645 501 354 O
HETATM12667 O HOH A 943 -7.696 -7.848 46.821 1.00 32.45 O
ANISOU12667 O HOH A 943 7021 3190 2117 -1609 -1130 351 O
HETATM12668 O HOH A 944 15.174 -27.751 35.041 1.00 42.05 O
ANISOU12668 O HOH A 944 5408 4102 6468 992 -2433 91 O
HETATM12669 O HOH A 945 15.259 5.294 5.913 1.00 33.07 O
ANISOU12669 O HOH A 945 4075 4990 3497 -589 466 977 O
HETATM12670 O HOH A 946 6.191 -0.788 36.407 1.00 25.34 O
ANISOU12670 O HOH A 946 3308 3120 3199 22 111 -454 O
HETATM12671 O HOH A 947 2.793 -26.664 37.717 1.00 17.00 O
ANISOU12671 O HOH A 947 2620 2034 1804 733 125 349 O
HETATM12672 O HOH A 948 -0.326 4.246 45.575 1.00 37.34 O
ANISOU12672 O HOH A 948 6001 4998 3186 -1397 -469 -1326 O
HETATM12673 O HOH A 950 -18.602 -6.716 32.911 1.00 16.43 O
ANISOU12673 O HOH A 950 2140 1943 2158 177 -198 -230 O
HETATM12674 O HOH A 951 -13.636 1.715 31.809 1.00 13.41 O
ANISOU12674 O HOH A 951 1847 1303 1945 -281 173 -89 O
HETATM12675 O HOH A 952 4.810 0.799 14.998 1.00 13.63 O
ANISOU12675 O HOH A 952 2044 1579 1552 -118 82 79 O
HETATM12676 O HOH A 953 -4.449 -3.626 3.071 1.00 35.57 O
ANISOU12676 O HOH A 953 3807 6728 2979 2378 -988 -1140 O
HETATM12677 O HOH A 954 -15.695 1.917 22.220 1.00 30.06 O
ANISOU12677 O HOH A 954 4621 3285 3513 719 -1107 -932 O
HETATM12678 O HOH A 955 -8.226 -32.988 47.740 1.00 37.73 O
ANISOU12678 O HOH A 955 5834 2878 5621 401 742 394 O
HETATM12679 O HOH A 956 -11.582 17.759 12.670 1.00 13.83 O
ANISOU12679 O HOH A 956 2077 1343 1834 134 -211 -67 O
HETATM12680 O HOH A 957 7.683 -28.398 42.597 1.00 24.88 O
ANISOU12680 O HOH A 957 2750 3927 2775 318 -70 563 O
HETATM12681 O HOH A 958 0.582 24.471 12.843 1.00 21.89 O
ANISOU12681 O HOH A 958 2692 3588 2036 -317 549 651 O
HETATM12682 O HOH A 959 -12.118 19.706 31.763 1.00 16.85 O
ANISOU12682 O HOH A 959 2796 1573 2030 -45 590 -501 O
HETATM12683 O HOH A 960 24.375 3.913 25.184 1.00 43.54 O
ANISOU12683 O HOH A 960 3976 7783 4784 -421 -394 257 O
HETATM12684 O HOH A 961 0.191 1.273 9.495 1.00 24.03 O
ANISOU12684 O HOH A 961 3410 3253 2464 -1976 -1017 1085 O
HETATM12685 O HOH A 962 -18.482 0.466 50.867 1.00 15.05 O
ANISOU12685 O HOH A 962 2566 1459 1692 174 488 -204 O
HETATM12686 O HOH A 963 10.815 25.406 16.306 1.00 27.09 O
ANISOU12686 O HOH A 963 4379 2397 3513 -1211 201 -989 O
HETATM12687 O HOH A 964 11.215 13.116 6.723 1.00 33.71 O
ANISOU12687 O HOH A 964 3599 3321 5886 -324 1831 1079 O
HETATM12688 O HOH A 965 13.371 -28.095 37.267 1.00 37.14 O
ANISOU12688 O HOH A 965 3974 4990 5147 844 -666 -217 O
HETATM12689 O HOH A 966 12.624 12.124 14.200 1.00 24.19 O
ANISOU12689 O HOH A 966 3442 2202 3546 -395 750 -561 O
HETATM12690 O HOH A 967 -33.833 3.106 31.223 1.00 29.47 O
ANISOU12690 O HOH A 967 4116 3726 3354 78 43 -564 O
HETATM12691 O HOH A 968 -24.922 0.307 45.974 1.00 18.10 O
ANISOU12691 O HOH A 968 2347 2999 1529 539 579 427 O
HETATM12692 O HOH A 969 -1.732 -0.068 45.946 1.00 38.57 O
ANISOU12692 O HOH A 969 4435 7416 2801 -80 367 801 O
HETATM12693 O HOH A 970 -0.447 -25.218 38.602 1.00 17.72 O
ANISOU12693 O HOH A 970 2554 2339 1837 687 527 230 O
HETATM12694 O HOH A 971 1.375 -14.067 18.922 1.00 27.50 O
ANISOU12694 O HOH A 971 2910 4713 2823 -708 554 -1064 O
HETATM12695 O HOH A 972 -6.248 -3.041 17.878 1.00 38.12 O
ANISOU12695 O HOH A 972 5106 3319 6059 268 -1788 -2460 O
HETATM12696 O HOH A 973 3.426 31.940 5.304 1.00 49.47 O
ANISOU12696 O HOH A 973 7542 3095 8160 -49 -693 2488 O
HETATM12697 O HOH A 974 -5.400 25.782 20.349 1.00 39.55 O
ANISOU12697 O HOH A 974 4584 4144 6296 -590 546 -769 O
HETATM12698 O HOH A 975 8.720 22.437 8.979 1.00 22.52 O
ANISOU12698 O HOH A 975 2674 2075 3808 -765 455 -144 O
HETATM12699 O HOH A 976 30.571 -7.091 16.590 1.00 30.07 O
ANISOU12699 O HOH A 976 2882 4304 4239 714 1175 417 O
HETATM12700 O HOH A 977 -30.811 -5.059 45.032 1.00 23.71 O
ANISOU12700 O HOH A 977 2936 2376 3696 204 675 -397 O
HETATM12701 O HOH A 979 0.631 0.091 12.019 1.00 13.22 O
ANISOU12701 O HOH A 979 2239 1372 1409 138 151 -102 O
HETATM12702 O HOH A 980 -6.470 19.587 10.190 1.00 13.85 O
ANISOU12702 O HOH A 980 2051 1640 1568 -154 31 -301 O
HETATM12703 O HOH A 981 10.983 10.003 17.611 1.00 22.93 O
ANISOU12703 O HOH A 981 2044 3801 2865 95 -523 -1086 O
HETATM12704 O HOH A 982 -27.308 13.510 29.607 1.00 32.27 O
ANISOU12704 O HOH A 982 4231 3366 4663 978 866 -352 O
HETATM12705 O HOH A 983 -22.751 -1.111 31.947 1.00 12.70 O
ANISOU12705 O HOH A 983 1777 1292 1755 -48 174 -379 O
HETATM12706 O HOH A 984 -45.104 -23.004 11.308 1.00 30.33 O
ANISOU12706 O HOH A 984 3323 5443 2758 541 -276 -812 O
HETATM12707 O HOH A 985 4.619 -24.979 21.391 1.00 32.19 O
ANISOU12707 O HOH A 985 4461 2804 4964 514 412 201 O
HETATM12708 O HOH A 986 -34.166 -4.352 42.683 1.00 29.60 O
ANISOU12708 O HOH A 986 3391 2864 4991 652 -286 -1229 O
HETATM12709 O HOH A 987 -4.843 1.970 16.349 1.00 12.33 O
ANISOU12709 O HOH A 987 1846 1539 1299 -37 74 -107 O
HETATM12710 O HOH A 988 3.308 5.552 30.319 1.00 22.77 O
ANISOU12710 O HOH A 988 2336 3344 2968 666 159 -846 O
HETATM12711 O HOH A 989 -2.450 18.274 41.871 1.00 21.82 O
ANISOU12711 O HOH A 989 3680 2026 2582 222 -489 -698 O
HETATM12712 O HOH A 990 26.923 -9.557 17.194 1.00 20.71 O
ANISOU12712 O HOH A 990 1695 3225 2948 418 199 -35 O
HETATM12713 O HOH A 991 1.663 -20.805 21.120 1.00 24.85 O
ANISOU12713 O HOH A 991 3183 2798 3458 -247 -418 -154 O
HETATM12714 O HOH A 992 -11.269 -3.963 37.194 1.00 17.83 O
ANISOU12714 O HOH A 992 2554 2192 2027 240 552 319 O
HETATM12715 O HOH A 993 16.679 -11.982 18.966 1.00 15.55 O
ANISOU12715 O HOH A 993 1776 1997 2135 287 64 12 O
HETATM12716 O HOH A 994 3.137 -28.439 49.154 1.00 37.23 O
ANISOU12716 O HOH A 994 6308 4179 3657 733 127 1533 O
HETATM12717 O HOH A 995 14.557 13.136 17.904 1.00 38.14 O
ANISOU12717 O HOH A 995 4750 4501 5241 -266 909 155 O
HETATM12718 O HOH A 996 -37.258 1.874 33.612 1.00 37.19 O
ANISOU12718 O HOH A 996 4912 3898 5318 789 -1393 -1209 O
HETATM12719 O HOH A 997 27.230 5.830 5.321 1.00 46.46 O
ANISOU12719 O HOH A 997 7764 3243 6645 -598 1716 216 O
HETATM12720 O HOH A 998 -8.789 19.661 20.782 1.00 19.98 O
ANISOU12720 O HOH A 998 3331 1668 2589 141 842 258 O
HETATM12721 O HOH A 999 20.955 -0.833 -0.875 1.00 40.89 O
ANISOU12721 O HOH A 999 4476 5771 5286 -1313 -357 417 O
HETATM12722 O HOH A1000 -13.821 -6.181 32.464 1.00 25.17 O
ANISOU12722 O HOH A1000 4367 2053 3141 469 544 -175 O
HETATM12723 O HOH A1001 3.102 21.550 35.426 1.00 35.92 O
ANISOU12723 O HOH A1001 3921 4422 5305 -670 446 -314 O
HETATM12724 O HOH A1002 29.513 -9.616 16.368 1.00 28.99 O
ANISOU12724 O HOH A1002 1920 4606 4486 359 1226 358 O
HETATM12725 O HOH A1003 17.346 -29.105 25.017 1.00 39.97 O
ANISOU12725 O HOH A1003 3165 7512 4509 -565 -486 -1697 O
HETATM12726 O HOH A1005 1.169 -12.232 15.910 1.00 24.98 O
ANISOU12726 O HOH A1005 2851 3339 3301 -597 -343 323 O
HETATM12727 O HOH A1006 16.426 -21.300 38.782 1.00 29.75 O
ANISOU12727 O HOH A1006 2869 4604 3830 -434 -95 -792 O
HETATM12728 O HOH A1007 -25.006 -3.583 26.585 1.00 30.87 O
ANISOU12728 O HOH A1007 3445 3262 5019 -624 777 -496 O
HETATM12729 O HOH A1008 11.383 2.694 28.376 1.00 30.98 O
ANISOU12729 O HOH A1008 3384 4965 3418 14 76 -280 O
HETATM12730 O HOH A1009 -18.334 -49.041 21.445 1.00 32.77 O
ANISOU12730 O HOH A1009 5554 2761 4134 -252 -333 909 O
HETATM12731 O HOH A1010 13.637 7.828 6.148 1.00 33.21 O
ANISOU12731 O HOH A1010 3634 4441 4543 -967 1848 -1720 O
HETATM12732 O HOH A1011 -1.978 -4.018 14.877 1.00 28.43 O
ANISOU12732 O HOH A1011 4549 3420 2833 -1212 -1226 860 O
HETATM12733 O HOH A1012 13.911 -13.061 15.389 1.00 14.90 O
ANISOU12733 O HOH A1012 2077 1498 2083 -216 184 -318 O
HETATM12734 O HOH A1013 24.175 3.040 21.793 1.00 24.70 O
ANISOU12734 O HOH A1013 3226 2843 3314 -496 -370 -380 O
HETATM12735 O HOH A1015 11.529 11.500 19.987 1.00 18.36 O
ANISOU12735 O HOH A1015 2207 2903 1863 -190 -126 -237 O
HETATM12736 O HOH A1016 -5.789 -2.534 42.071 1.00 40.73 O
ANISOU12736 O HOH A1016 10018 2192 3264 171 63 -174 O
HETATM12737 O HOH A1017 -11.392 -1.637 6.333 1.00 19.65 O
ANISOU12737 O HOH A1017 3311 1585 2570 -247 1089 -672 O
HETATM12738 O HOH A1018 -21.429 -9.108 30.640 1.00 29.19 O
ANISOU12738 O HOH A1018 4302 3164 3625 -459 -166 -637 O
HETATM12739 O HOH A1019 -1.189 -4.038 17.461 1.00 13.38 O
ANISOU12739 O HOH A1019 1599 1288 2195 77 -33 -394 O
HETATM12740 O HOH A1021 -14.918 -53.567 18.786 1.00 46.87 O
ANISOU12740 O HOH A1021 7518 2844 7447 -1152 871 484 O
HETATM12741 O HOH A1022 -37.928 -9.921 40.314 1.00 44.96 O
ANISOU12741 O HOH A1022 4545 5583 6952 -1760 39 1751 O
HETATM12742 O HOH A1023 23.678 -16.404 14.932 1.00 21.50 O
ANISOU12742 O HOH A1023 2742 2683 2741 466 -10 -345 O
HETATM12743 O HOH A1024 -11.626 9.016 20.534 1.00 19.16 O
ANISOU12743 O HOH A1024 2567 2847 1866 18 -11 -731 O
HETATM12744 O HOH A1025 -12.299 -5.759 34.451 1.00 38.97 O
ANISOU12744 O HOH A1025 2353 3687 8767 173 -666 -3452 O
HETATM12745 O HOH A1026 15.325 -14.872 17.093 1.00 17.60 O
ANISOU12745 O HOH A1026 2124 2631 1930 330 199 -171 O
HETATM12746 O HOH A1027 14.086 -8.582 42.933 1.00 28.61 O
ANISOU12746 O HOH A1027 4998 3460 2412 1086 -713 -392 O
HETATM12747 O HOH A1028 23.279 -6.829 21.329 1.00 17.36 O
ANISOU12747 O HOH A1028 1739 2709 2144 -356 -141 -55 O
HETATM12748 O HOH A1029 -17.293 20.491 38.613 1.00 41.03 O
ANISOU12748 O HOH A1029 4101 7812 3674 2660 498 -534 O
HETATM12749 O HOH A1030 -8.521 -12.656 36.360 1.00 44.08 O
ANISOU12749 O HOH A1030 9107 4290 3350 2639 1830 922 O
HETATM12750 O HOH A1031 20.732 0.476 2.883 1.00 36.65 O
ANISOU12750 O HOH A1031 5657 3572 4696 72 1384 825 O
HETATM12751 O HOH A1032 -4.052 -15.127 43.800 1.00 19.42 O
ANISOU12751 O HOH A1032 3224 2247 1908 58 275 5 O
HETATM12752 O HOH A1033 -31.611 8.303 34.048 1.00 27.57 O
ANISOU12752 O HOH A1033 3602 3318 3556 -41 724 -544 O
HETATM12753 O HOH A1034 -40.309 -7.384 44.186 1.00 43.80 O
ANISOU12753 O HOH A1034 3718 3844 9080 -208 1853 -2108 O
HETATM12754 O HOH A1035 -0.432 -18.637 52.883 1.00 38.44 O
ANISOU12754 O HOH A1035 6673 5506 2424 12 408 287 O
HETATM12755 O HOH A1036 -22.588 0.248 29.397 1.00 15.08 O
ANISOU12755 O HOH A1036 1934 1659 2134 -62 215 54 O
HETATM12756 O HOH A1037 -13.174 5.851 52.276 1.00 46.37 O
ANISOU12756 O HOH A1037 7593 6656 3369 -3067 -2303 -478 O
HETATM12757 O HOH A1038 -8.910 18.174 10.658 1.00 14.43 O
ANISOU12757 O HOH A1038 2241 1345 1895 71 121 1 O
HETATM12758 O HOH A1039 -18.364 6.921 27.672 1.00 15.06 O
ANISOU12758 O HOH A1039 2350 1396 1974 144 186 -219 O
HETATM12759 O HOH A1040 -0.417 12.793 8.615 1.00 22.17 O
ANISOU12759 O HOH A1040 3333 2408 2681 -1086 -528 738 O
HETATM12760 O HOH A1041 3.392 28.627 11.521 1.00 27.87 O
ANISOU12760 O HOH A1041 3792 3390 3404 -274 713 487 O
HETATM12761 O HOH A1042 6.403 33.150 7.110 1.00 44.62 O
ANISOU12761 O HOH A1042 6339 3122 7491 108 -678 1562 O
HETATM12762 O HOH A1043 1.773 -29.786 38.158 1.00 38.77 O
ANISOU12762 O HOH A1043 4093 4946 5690 -275 194 341 O
HETATM12763 O HOH A1044 30.439 -0.949 26.436 1.00 38.53 O
ANISOU12763 O HOH A1044 4445 6600 3593 -1913 -1162 559 O
HETATM12764 O HOH A1045 29.082 -9.826 13.577 1.00 29.46 O
ANISOU12764 O HOH A1045 2213 5014 3963 55 744 -52 O
HETATM12765 O HOH A1046 5.525 14.415 1.609 1.00 54.09 O
ANISOU12765 O HOH A1046 11430 5363 3757 -1226 316 -152 O
HETATM12766 O HOH A1047 17.949 24.098 10.458 1.00 32.70 O
ANISOU12766 O HOH A1047 2882 3337 6203 -858 1502 615 O
HETATM12767 O HOH A1048 -21.097 1.746 26.151 1.00 27.71 O
ANISOU12767 O HOH A1048 3696 3869 2961 257 727 -1005 O
HETATM12768 O HOH A1049 -7.166 28.041 11.455 1.00 37.88 O
ANISOU12768 O HOH A1049 3822 3019 7550 60 972 1066 O
HETATM12769 O HOH A1050 17.318 -5.772 21.072 1.00 22.95 O
ANISOU12769 O HOH A1050 1790 2047 4882 -234 989 -469 O
HETATM12770 O HOH A1051 16.774 -29.402 32.211 1.00 47.23 O
ANISOU12770 O HOH A1051 5884 6612 5447 2674 -519 916 O
HETATM12771 O HOH A1052 2.824 26.178 12.405 1.00 29.40 O
ANISOU12771 O HOH A1052 4535 3165 3470 -823 -78 285 O
HETATM12772 O HOH A1053 -8.175 -10.593 49.651 1.00 24.94 O
ANISOU12772 O HOH A1053 4304 3008 2161 984 -437 -766 O
HETATM12773 O HOH A1054 6.409 20.002 27.928 1.00 32.06 O
ANISOU12773 O HOH A1054 2805 5155 4220 -416 -120 -1736 O
HETATM12774 O HOH A1055 -24.045 15.240 31.651 1.00 33.38 O
ANISOU12774 O HOH A1055 3159 1984 7540 266 65 -787 O
HETATM12775 O HOH A1056 -14.061 -33.806 37.175 1.00 41.09 O
ANISOU12775 O HOH A1056 6954 2496 6163 -530 730 -668 O
HETATM12776 O HOH A1057 -32.499 -6.752 16.191 1.00 38.34 O
ANISOU12776 O HOH A1057 7091 3055 4421 541 -1590 -817 O
HETATM12777 O HOH A1058 -9.431 -2.028 47.249 1.00 28.34 O
ANISOU12777 O HOH A1058 3949 3281 3537 17 981 -359 O
HETATM12778 O HOH A1059 -10.003 -11.779 34.101 1.00 47.33 O
ANISOU12778 O HOH A1059 3685 7758 6537 668 2901 -1170 O
HETATM12779 O HOH A1060 -18.187 -18.079 31.933 1.00 42.16 O
ANISOU12779 O HOH A1060 5060 8040 2919 1188 -228 648 O
HETATM12780 O HOH A1061 25.229 -18.128 20.932 1.00 42.64 O
ANISOU12780 O HOH A1061 7967 4847 3388 622 377 -93 O
HETATM12781 O HOH A1062 -6.077 7.064 14.348 1.00 10.90 O
ANISOU12781 O HOH A1062 1562 1256 1323 -77 -118 -61 O
HETATM12782 O HOH A1063 10.207 0.332 27.994 1.00 21.14 O
ANISOU12782 O HOH A1063 2772 2916 2343 205 345 -425 O
HETATM12783 O HOH A1064 -11.312 11.355 12.946 1.00 15.07 O
ANISOU12783 O HOH A1064 2607 1595 1522 -19 -136 -30 O
HETATM12784 O HOH A1065 3.540 26.031 27.374 1.00 47.66 O
ANISOU12784 O HOH A1065 7305 7722 3080 -1889 972 -1747 O
HETATM12785 O HOH A1066 17.542 15.554 11.718 1.00 30.08 O
ANISOU12785 O HOH A1066 2596 3851 4981 -172 635 -815 O
HETATM12786 O HOH A1067 3.736 20.751 28.114 1.00 17.93 O
ANISOU12786 O HOH A1067 2495 2586 1729 -691 -168 -227 O
HETATM12787 O HOH A1068 1.295 -12.219 48.532 1.00 30.42 O
ANISOU12787 O HOH A1068 3714 5262 2579 1685 -322 145 O
HETATM12788 O HOH A1069 -10.285 0.912 14.544 1.00 28.07 O
ANISOU12788 O HOH A1069 4839 3160 2663 680 1177 658 O
HETATM12789 O HOH A1070 21.680 -6.622 39.000 1.00 37.55 O
ANISOU12789 O HOH A1070 3635 7156 3475 938 -481 180 O
HETATM12790 O HOH A1071 -1.507 -11.455 48.099 1.00 21.52 O
ANISOU12790 O HOH A1071 3458 2308 2407 24 -204 -191 O
HETATM12791 O HOH A1072 -26.435 -7.978 50.115 1.00 21.96 O
ANISOU12791 O HOH A1072 3014 1916 3411 463 -154 -371 O
HETATM12792 O HOH A1073 -7.166 -1.146 46.098 1.00 25.23 O
ANISOU12792 O HOH A1073 3159 3163 3264 768 349 1451 O
HETATM12793 O HOH A1074 9.311 18.313 25.080 1.00 24.26 O
ANISOU12793 O HOH A1074 2991 3052 3172 -30 -527 299 O
HETATM12794 O HOH A1075 -9.106 24.588 26.068 1.00 34.27 O
ANISOU12794 O HOH A1075 4436 3675 4909 908 -699 65 O
HETATM12795 O HOH A1076 -3.062 -1.709 38.988 1.00 21.93 O
ANISOU12795 O HOH A1076 2402 1590 4338 59 792 -777 O
HETATM12796 O HOH A1077 -20.164 17.551 36.106 1.00 20.11 O
ANISOU12796 O HOH A1077 2333 2371 2934 217 552 -548 O
HETATM12797 O HOH A1078 -4.847 -3.879 39.452 1.00 17.62 O
ANISOU12797 O HOH A1078 2390 1644 2658 75 -120 -12 O
HETATM12798 O HOH A1079 27.040 -5.633 30.955 1.00 30.35 O
ANISOU12798 O HOH A1079 2961 4994 3577 158 -428 102 O
HETATM12799 O HOH A1080 -4.770 9.151 42.335 1.00 23.69 O
ANISOU12799 O HOH A1080 2407 3157 3435 423 543 401 O
HETATM12800 O HOH A1081 15.894 -18.181 45.751 1.00 46.05 O
ANISOU12800 O HOH A1081 3954 7699 5844 931 -917 -1058 O
HETATM12801 O HOH A1082 19.342 -10.086 15.325 1.00 14.69 O
ANISOU12801 O HOH A1082 1776 1898 1907 152 67 -17 O
HETATM12802 O HOH A1083 8.577 -31.101 35.176 1.00 31.99 O
ANISOU12802 O HOH A1083 4400 4939 2815 -1898 53 -808 O
HETATM12803 O HOH A1084 -39.009 -0.607 31.469 1.00 38.04 O
ANISOU12803 O HOH A1084 3614 6070 4770 90 -182 1484 O
HETATM12804 O HOH A1085 -12.050 3.248 21.321 1.00 16.76 O
ANISOU12804 O HOH A1085 2292 2059 2017 -44 690 -139 O
HETATM12805 O HOH A1086 7.129 2.602 29.513 1.00 26.87 O
ANISOU12805 O HOH A1086 3280 3422 3508 -447 414 187 O
HETATM12806 O HOH A1087 21.825 -20.402 36.263 1.00 45.15 O
ANISOU12806 O HOH A1087 4832 5509 6812 915 -1580 1182 O
HETATM12807 O HOH A1088 12.203 3.143 25.948 1.00 23.74 O
ANISOU12807 O HOH A1088 3973 2339 2706 -533 -751 -659 O
HETATM12808 O HOH A1089 -10.418 -4.493 42.597 1.00 26.02 O
ANISOU12808 O HOH A1089 5050 2459 2376 -730 888 -491 O
HETATM12809 O HOH A1090 -24.724 16.183 41.966 1.00 32.43 O
ANISOU12809 O HOH A1090 7106 1843 3370 433 2634 83 O
HETATM12810 O HOH A1091 -13.979 21.647 35.798 1.00 29.61 O
ANISOU12810 O HOH A1091 4103 2828 4320 -354 -13 47 O
HETATM12811 O HOH A1092 -10.123 -54.020 21.698 1.00 39.52 O
ANISOU12811 O HOH A1092 5798 5076 4140 791 -251 1515 O
HETATM12812 O HOH A1093 4.651 -0.846 41.071 1.00 30.12 O
ANISOU12812 O HOH A1093 3415 3474 4552 -350 -511 -478 O
HETATM12813 O HOH A1094 14.927 11.910 7.519 1.00 46.71 O
ANISOU12813 O HOH A1094 7483 3015 7249 -321 3927 -1235 O
HETATM12814 O HOH A1095 6.266 -17.028 50.825 1.00 28.41 O
ANISOU12814 O HOH A1095 4280 3974 2538 -167 -572 116 O
HETATM12815 O HOH A1096 14.842 -28.660 40.998 1.00 35.03 O
ANISOU12815 O HOH A1096 4344 3227 5738 1082 603 406 O
HETATM12816 O HOH A1097 -2.176 1.757 8.211 1.00 19.24 O
ANISOU12816 O HOH A1097 2469 2346 2494 -415 -356 340 O
HETATM12817 O HOH A1098 -11.808 21.771 33.531 1.00 20.08 O
ANISOU12817 O HOH A1098 2648 2389 2590 388 -650 -1069 O
HETATM12818 O HOH A1099 7.543 -25.811 43.615 1.00 27.15 O
ANISOU12818 O HOH A1099 3821 3649 2842 517 -874 663 O
HETATM12819 O HOH A1100 -4.968 -28.189 51.425 1.00 24.69 O
ANISOU12819 O HOH A1100 3691 2967 2720 530 -553 714 O
HETATM12820 O HOH A1101 -22.360 -1.721 22.915 1.00 28.55 O
ANISOU12820 O HOH A1101 3948 3926 2973 548 -81 490 O
HETATM12821 O HOH A1102 -24.570 0.558 25.550 1.00 19.20 O
ANISOU12821 O HOH A1102 3033 1873 2389 362 -245 -627 O
HETATM12822 O HOH A1103 1.730 -8.218 45.297 1.00 41.63 O
ANISOU12822 O HOH A1103 5886 5130 4802 -757 -374 -361 O
HETATM12823 O HOH A1105 20.908 -9.926 38.670 1.00 26.52 O
ANISOU12823 O HOH A1105 1972 5648 2453 -830 -653 291 O
HETATM12824 O HOH A1106 -24.977 -25.385 8.731 1.00 27.60 O
ANISOU12824 O HOH A1106 2867 3540 4078 394 -122 -79 O
HETATM12825 O HOH A1107 33.355 -3.008 22.678 1.00 51.10 O
ANISOU12825 O HOH A1107 3679 4683 11053 -683 -1209 -340 O
HETATM12826 O HOH A1108 -27.352 -11.992 45.575 1.00 26.46 O
ANISOU12826 O HOH A1108 3165 1864 5025 -121 -566 -107 O
HETATM12827 O HOH A1109 13.332 -19.080 15.909 1.00 22.73 O
ANISOU12827 O HOH A1109 4403 2078 2155 805 612 228 O
HETATM12828 O HOH A1110 -7.545 21.954 22.063 1.00 26.72 O
ANISOU12828 O HOH A1110 4397 2273 3479 172 -699 -353 O
HETATM12829 O HOH A1111 -21.193 16.342 43.140 1.00 45.42 O
ANISOU12829 O HOH A1111 5114 3909 8233 -1614 759 -383 O
HETATM12830 O HOH A1112 14.888 -19.436 19.117 1.00 26.66 O
ANISOU12830 O HOH A1112 3761 3230 3138 716 896 274 O
HETATM12831 O HOH A1113 11.982 -6.186 43.963 1.00 32.04 O
ANISOU12831 O HOH A1113 3853 6026 2293 -1431 -167 -205 O
HETATM12832 O HOH A1114 -18.531 -48.759 14.277 1.00 33.50 O
ANISOU12832 O HOH A1114 5454 3583 3688 772 -491 1041 O
HETATM12833 O HOH A1115 -29.759 -1.472 43.260 1.00 21.07 O
ANISOU12833 O HOH A1115 2733 2335 2936 239 922 -61 O
HETATM12834 O HOH A1116 -12.033 -16.769 48.467 1.00 35.07 O
ANISOU12834 O HOH A1116 3209 5497 4619 1328 1237 -159 O
HETATM12835 O HOH A1117 -3.994 -0.073 7.116 1.00 19.74 O
ANISOU12835 O HOH A1117 2090 2167 3243 145 -311 271 O
HETATM12836 O HOH A1118 -25.360 -45.519 14.955 1.00 25.96 O
ANISOU12836 O HOH A1118 3063 3644 3154 -679 49 547 O
HETATM12837 O HOH A1119 2.364 29.514 20.911 1.00 43.33 O
ANISOU12837 O HOH A1119 7923 3877 4663 -954 -910 -1131 O
HETATM12838 O HOH A1120 -26.743 -5.641 51.711 1.00 29.28 O
ANISOU12838 O HOH A1120 5640 1987 3495 1244 3022 902 O
HETATM12839 O HOH A1121 9.456 -10.722 48.555 1.00 35.61 O
ANISOU12839 O HOH A1121 4534 4783 4210 -1297 685 -1271 O
HETATM12840 O HOH A1122 -11.830 1.683 51.458 1.00 25.50 O
ANISOU12840 O HOH A1122 3147 4915 1626 -470 -257 85 O
HETATM12841 O HOH A1124 15.706 -18.783 38.739 1.00 28.71 O
ANISOU12841 O HOH A1124 4070 4320 2517 -848 -397 212 O
HETATM12842 O HOH A1125 -5.138 -12.643 32.799 1.00 34.47 O
ANISOU12842 O HOH A1125 4628 4048 4419 3 1087 -1194 O
HETATM12843 O HOH A1126 -33.356 5.564 32.039 1.00 24.55 O
ANISOU12843 O HOH A1126 2160 3669 3497 131 26 843 O
HETATM12844 O HOH A1127 25.790 -14.791 29.388 1.00 44.29 O
ANISOU12844 O HOH A1127 5178 8314 3336 2282 77 656 O
HETATM12845 O HOH A1128 -28.849 13.728 32.498 1.00 47.75 O
ANISOU12845 O HOH A1128 3088 5320 9734 -192 -485 -2538 O
HETATM12846 O HOH A1129 -19.956 1.245 30.083 1.00 11.86 O
ANISOU12846 O HOH A1129 1823 1277 1406 -44 39 39 O
HETATM12847 O HOH A1130 -14.159 -28.463 45.796 1.00 55.64 O
ANISOU12847 O HOH A1130 6760 7942 6438 -3326 5323 -348 O
HETATM12848 O HOH A1131 -7.400 -17.258 33.361 1.00 30.67 O
ANISOU12848 O HOH A1131 3482 4256 3916 891 134 -244 O
HETATM12849 O HOH A1132 1.397 -16.795 18.108 1.00 37.26 O
ANISOU12849 O HOH A1132 6122 5733 2300 1461 965 465 O
HETATM12850 O HOH A1133 -14.154 20.517 30.077 1.00 26.95 O
ANISOU12850 O HOH A1133 2890 2753 4596 -512 -700 -272 O
HETATM12851 O HOH A1134 -34.755 -0.931 27.471 1.00 28.33 O
ANISOU12851 O HOH A1134 3515 3023 4225 636 86 -579 O
HETATM12852 O HOH A1135 27.417 4.209 27.231 1.00 41.20 O
ANISOU12852 O HOH A1135 4632 4187 6835 -1626 990 -2172 O
HETATM12853 O HOH A1136 -23.118 -1.393 27.033 1.00 20.40 O
ANISOU12853 O HOH A1136 2727 2538 2482 215 -46 -95 O
HETATM12854 O HOH A1137 2.662 1.811 27.480 1.00 19.70 O
ANISOU12854 O HOH A1137 2493 2977 2012 422 -107 -465 O
HETATM12855 O HOH A1138 -2.967 15.183 8.255 1.00 29.42 O
ANISOU12855 O HOH A1138 4746 2824 3605 348 1029 717 O
HETATM12856 O HOH A1139 -3.134 -14.921 51.092 1.00 38.83 O
ANISOU12856 O HOH A1139 3511 8657 2583 -433 323 -1012 O
HETATM12857 O HOH A1140 -11.745 8.716 48.447 1.00 29.81 O
ANISOU12857 O HOH A1140 3362 3517 4446 -991 -477 -904 O
HETATM12858 O HOH A1141 15.354 24.673 9.512 1.00 27.22 O
ANISOU12858 O HOH A1141 2966 3355 4021 -1562 1026 -292 O
HETATM12859 O HOH A1142 -14.720 24.143 39.490 1.00 36.23 O
ANISOU12859 O HOH A1142 4876 2410 6477 -401 -1872 -126 O
HETATM12860 O HOH A1143 -30.752 -11.753 45.685 1.00 30.35 O
ANISOU12860 O HOH A1143 5281 2981 3268 -465 35 192 O
HETATM12861 O HOH A1144 -8.601 -6.913 49.146 1.00 47.70 O
ANISOU12861 O HOH A1144 3739 9449 4933 -60 559 -2726 O
HETATM12862 O HOH A1145 -2.897 -11.603 31.741 1.00 29.13 O
ANISOU12862 O HOH A1145 5192 3435 2441 612 618 82 O
HETATM12863 O HOH A1146 -8.411 19.143 37.647 1.00 19.23 O
ANISOU12863 O HOH A1146 2543 2749 2014 -95 700 -243 O
HETATM12864 O HOH A1147 -10.440 -3.554 8.429 1.00 42.69 O
ANISOU12864 O HOH A1147 7948 3145 5124 947 1012 509 O
HETATM12865 O HOH A1148 7.389 -0.094 14.588 1.00 18.06 O
ANISOU12865 O HOH A1148 1774 1927 3159 304 -213 -104 O
HETATM12866 O HOH A1149 21.528 -0.836 38.174 1.00 43.53 O
ANISOU12866 O HOH A1149 4373 5449 6715 -1601 1232 -2091 O
HETATM12867 O HOH A1150 -3.309 27.841 27.043 1.00 43.67 O
ANISOU12867 O HOH A1150 9932 2859 3800 1586 1977 764 O
HETATM12868 O HOH A1151 -11.023 15.017 12.799 1.00 12.82 O
ANISOU12868 O HOH A1151 1869 1576 1425 -153 -166 -137 O
HETATM12869 O HOH A1152 -7.814 -3.354 44.059 1.00 36.05 O
ANISOU12869 O HOH A1152 4416 4981 4299 275 -168 -903 O
HETATM12870 O HOH A1153 -47.682 -23.639 11.897 1.00 38.24 O
ANISOU12870 O HOH A1153 5009 5277 4243 -452 349 -254 O
HETATM12871 O HOH A1154 16.132 -29.242 38.935 1.00 50.36 O
ANISOU12871 O HOH A1154 5403 8334 5397 479 2034 2109 O
HETATM12872 O HOH A1155 -11.716 11.448 48.526 1.00 33.32 O
ANISOU12872 O HOH A1155 6056 3484 3120 -1024 -534 53 O
HETATM12873 O HOH A1156 -22.594 16.018 35.136 1.00 37.16 O
ANISOU12873 O HOH A1156 3692 4171 6252 142 994 -833 O
HETATM12874 O HOH A1157 -18.551 -9.544 32.013 1.00 50.26 O
ANISOU12874 O HOH A1157 10454 6158 2482 -367 919 -1484 O
HETATM12875 O HOH A1158 31.210 -8.642 27.578 1.00 46.21 O
ANISOU12875 O HOH A1158 4103 8356 5098 1576 -897 -352 O
HETATM12876 O HOH A1159 -14.037 16.402 45.640 1.00 43.72 O
ANISOU12876 O HOH A1159 3667 10411 2531 -43 221 -420 O
HETATM12877 O HOH A1160 -23.510 -28.850 7.721 1.00 33.31 O
ANISOU12877 O HOH A1160 3634 4081 4939 -303 593 125 O
HETATM12878 O HOH A1161 -37.655 -6.593 46.072 1.00 33.99 O
ANISOU12878 O HOH A1161 5581 3451 3881 -379 419 -650 O
HETATM12879 O HOH A1162 -35.682 -6.593 49.346 1.00 25.27 O
ANISOU12879 O HOH A1162 3089 2816 3694 408 -24 -81 O
HETATM12880 O HOH A1163 2.351 -14.055 14.477 1.00 29.48 O
ANISOU12880 O HOH A1163 2597 5355 3246 -107 -499 -1090 O
HETATM12881 O HOH A1164 -13.286 -14.391 48.943 1.00 35.29 O
ANISOU12881 O HOH A1164 4708 3514 5182 536 853 380 O
HETATM12882 O HOH A1165 17.920 -19.895 30.071 1.00 28.00 O
ANISOU12882 O HOH A1165 3417 3621 3600 -5 -538 194 O
HETATM12883 O HOH A1166 21.335 -2.052 40.531 1.00 51.46 O
ANISOU12883 O HOH A1166 7528 8049 3975 -1406 -1979 1241 O
HETATM12884 O HOH A1167 -7.820 -4.452 48.714 1.00 50.51 O
ANISOU12884 O HOH A1167 5810 8021 5360 275 1134 1683 O
HETATM12885 O HOH A1169 3.029 -18.914 18.938 1.00 34.36 O
ANISOU12885 O HOH A1169 4951 4390 3713 1027 467 -962 O
HETATM12886 O HOH A1170 16.385 10.806 10.577 1.00 55.01 O
ANISOU12886 O HOH A1170 3920 4712 12267 -582 726 1591 O
HETATM12887 O HOH A1171 -20.880 20.106 36.085 1.00 44.97 O
ANISOU12887 O HOH A1171 6376 3010 7697 1111 2845 -217 O
HETATM12888 O HOH A1172 0.570 28.271 22.646 1.00 29.49 O
ANISOU12888 O HOH A1172 4533 3061 3609 -658 -32 -905 O
HETATM12889 O HOH A1173 0.211 24.744 32.837 1.00 34.73 O
ANISOU12889 O HOH A1173 5269 3462 4464 -846 -1201 601 O
HETATM12890 O HOH A1174 -6.011 27.747 13.919 1.00 43.17 O
ANISOU12890 O HOH A1174 7996 3877 4528 -488 1071 -1139 O
HETATM12891 O HOH A1175 -6.896 -5.185 46.283 1.00 37.90 O
ANISOU12891 O HOH A1175 5769 4371 4259 -174 30 -246 O
HETATM12892 O HOH A1176 27.595 -16.895 16.923 1.00 40.79 O
ANISOU12892 O HOH A1176 4148 5549 5799 1824 575 -648 O
HETATM12893 O HOH A1177 -10.533 4.146 52.607 1.00 47.07 O
ANISOU12893 O HOH A1177 6093 6989 4801 -269 -494 -333 O
HETATM12894 O HOH A1178 -6.735 27.599 16.362 1.00 37.61 O
ANISOU12894 O HOH A1178 4952 3290 6046 -1040 580 70 O
HETATM12895 O HOH A1179 -25.989 14.742 37.586 1.00 55.95 O
ANISOU12895 O HOH A1179 3783 13269 4203 1765 117 -254 O
HETATM12896 O HOH A1180 1.070 -1.230 45.419 1.00 50.45 O
ANISOU12896 O HOH A1180 8214 6398 4555 1679 -739 85 O
HETATM12897 O HOH A1181 -19.006 4.275 27.838 1.00 29.47 O
ANISOU12897 O HOH A1181 2408 1448 7339 -174 1242 -898 O
HETATM12898 O HOH A1182 13.647 -10.341 12.805 1.00 14.58 O
ANISOU12898 O HOH A1182 1924 2166 1447 280 -95 171 O
HETATM12899 O HOH A1183 -29.877 12.335 34.619 1.00 45.34 O
ANISOU12899 O HOH A1183 6593 5494 5140 1826 -965 -1564 O
HETATM12900 O HOH A1184 -12.164 4.444 17.006 1.00 31.52 O
ANISOU12900 O HOH A1184 4852 4875 2248 194 190 1043 O
HETATM12901 O HOH A1185 -12.004 7.966 51.237 1.00 39.55 O
ANISOU12901 O HOH A1185 6203 5142 3682 -215 -1048 -698 O
HETATM12902 O HOH A1186 -13.650 0.829 53.153 1.00 45.14 O
ANISOU12902 O HOH A1186 5663 9108 2378 -1616 316 1173 O
HETATM12903 O HOH A1188 27.964 -7.769 30.090 1.00 53.42 O
ANISOU12903 O HOH A1188 4974 6835 8485 -1129 -770 2052 O
HETATM12904 O HOH A1189 -31.414 2.229 42.896 1.00 21.78 O
ANISOU12904 O HOH A1189 2863 2318 3094 -428 947 -602 O
HETATM12905 O HOH A1190 17.707 -1.918 1.608 1.00 46.28 O
ANISOU12905 O HOH A1190 4605 6844 6133 84 1166 115 O
HETATM12906 O HOH A1191 -14.367 16.846 18.562 1.00 28.41 O
ANISOU12906 O HOH A1191 2250 4535 4007 -106 251 1219 O
HETATM12907 O HOH A1192 -30.145 0.453 41.217 1.00 24.91 O
ANISOU12907 O HOH A1192 3548 2758 3155 655 1079 170 O
HETATM12908 O HOH A1193 4.557 1.820 33.374 1.00 36.95 O
ANISOU12908 O HOH A1193 4403 3776 5860 404 1483 722 O
HETATM12909 O HOH A1194 -8.297 26.293 28.036 1.00 35.45 O
ANISOU12909 O HOH A1194 3872 4514 5083 -165 -289 -887 O
HETATM12910 O HOH A1195 -14.509 -21.313 49.945 1.00 33.33 O
ANISOU12910 O HOH A1195 4150 4477 4034 632 238 41 O
HETATM12911 O HOH A1196 -2.512 -9.366 46.513 1.00 26.24 O
ANISOU12911 O HOH A1196 4725 2943 2302 156 -244 51 O
HETATM12912 O HOH A1197 -34.844 -2.172 39.529 1.00 37.43 O
ANISOU12912 O HOH A1197 5566 4514 4140 -128 1180 189 O
HETATM12913 O HOH A1198 21.364 -18.387 23.124 1.00 47.10 O
ANISOU12913 O HOH A1198 4882 3446 9564 509 782 246 O
HETATM12914 O HOH A1199 -7.526 13.103 46.629 1.00 40.12 O
ANISOU12914 O HOH A1199 4771 5645 4826 46 690 -1513 O
HETATM12915 O HOH A1200 -16.456 0.467 52.768 1.00 31.73 O
ANISOU12915 O HOH A1200 5435 4002 2615 494 -552 26 O
HETATM12916 O HOH A1201 -8.274 -34.920 45.806 1.00 41.90 O
ANISOU12916 O HOH A1201 6136 3351 6433 595 361 512 O
HETATM12917 O HOH A1202 3.865 3.592 35.477 1.00 27.28 O
ANISOU12917 O HOH A1202 2387 4505 3471 -132 -15 462 O
HETATM12918 O HOH A1203 -17.384 -10.655 33.842 1.00 39.60 O
ANISOU12918 O HOH A1203 6619 3050 5375 -1228 847 -1814 O
HETATM12919 O HOH A1204 3.992 6.084 34.485 1.00 29.14 O
ANISOU12919 O HOH A1204 3224 3944 3904 735 -98 -948 O
HETATM12920 O HOH A1206 -27.770 12.756 37.855 1.00 52.33 O
ANISOU12920 O HOH A1206 6850 7824 5206 2081 2320 1381 O
HETATM12921 O HOH A1207 -32.162 -2.979 43.731 1.00 25.19 O
ANISOU12921 O HOH A1207 3476 2914 3179 475 -56 -874 O
HETATM12922 O HOH A1208 -14.048 20.823 27.117 1.00 41.57 O
ANISOU12922 O HOH A1208 4998 4349 6445 -103 199 338 O
HETATM12923 O HOH A1209 6.555 26.755 1.650 1.00 48.70 O
ANISOU12923 O HOH A1209 4834 8291 5378 -548 1766 124 O
HETATM12924 O HOH A1210 -44.345 -10.388 -15.252 1.00 35.65 O
ANISOU12924 O HOH A1210 4212 4315 5017 -1572 -581 1400 O
HETATM12925 O HOH A1211 -11.589 13.478 46.985 1.00 33.14 O
ANISOU12925 O HOH A1211 4580 2987 5023 -237 623 452 O
HETATM12926 O HOH A1212 -9.212 23.802 20.986 1.00 46.78 O
ANISOU12926 O HOH A1212 5489 6101 6182 1684 788 1857 O
HETATM12927 O HOH A1213 28.407 1.262 16.471 1.00 30.13 O
ANISOU12927 O HOH A1213 3237 4012 4198 -771 314 463 O
HETATM12928 O HOH A1214 5.374 7.267 36.568 1.00 41.13 O
ANISOU12928 O HOH A1214 3332 6710 5583 60 -399 -1191 O
HETATM12929 O HOH A1215 -38.700 2.806 35.897 1.00 49.82 O
ANISOU12929 O HOH A1215 5513 5514 7901 810 -1716 -2636 O
HETATM12930 O HOH A1216 9.487 4.209 30.011 1.00 41.02 O
ANISOU12930 O HOH A1216 4923 5389 5271 189 711 621 O
HETATM12931 O HOH A1217 5.371 -0.739 33.774 1.00 25.09 O
ANISOU12931 O HOH A1217 3653 3224 2657 -77 149 -235 O
HETATM12932 O HOH A1218 -2.639 -5.660 19.078 1.00 26.86 O
ANISOU12932 O HOH A1218 3163 3327 3715 -50 1019 508 O
HETATM12933 O HOH A1219 25.770 -18.048 15.315 1.00 42.81 O
ANISOU12933 O HOH A1219 4018 3791 8454 1350 223 -1278 O
HETATM12934 O HOH A1220 -1.244 -17.229 19.060 1.00 27.30 O
ANISOU12934 O HOH A1220 4336 3016 3017 102 -555 -454 O
HETATM12935 O HOH A1222 16.172 24.891 6.809 1.00 37.40 O
ANISOU12935 O HOH A1222 4159 6141 3909 -1556 578 913 O
HETATM12936 O HOH A1223 30.430 -2.837 10.365 1.00 48.53 O
ANISOU12936 O HOH A1223 4238 6315 7884 -384 -1496 511 O
HETATM12937 O HOH A1224 -36.654 0.021 26.579 1.00 52.87 O
ANISOU12937 O HOH A1224 7697 8783 3607 1217 4087 121 O
HETATM12938 O HOH A1225 5.475 29.739 12.763 1.00 40.48 O
ANISOU12938 O HOH A1225 5861 4326 5191 -1809 603 -477 O
HETATM12939 O HOH A1226 6.149 30.823 23.296 1.00 44.00 O
ANISOU12939 O HOH A1226 8845 4459 3414 -6 284 142 O
HETATM12940 O HOH A1228 -5.107 -12.306 20.126 1.00 34.07 O
ANISOU12940 O HOH A1228 3703 5442 3799 -1018 -557 26 O
HETATM12941 O HOH A1230 25.524 4.976 20.376 1.00 34.72 O
ANISOU12941 O HOH A1230 4638 3092 5460 -838 641 -142 O
HETATM12942 O HOH A1231 4.850 3.137 31.091 1.00 36.66 O
ANISOU12942 O HOH A1231 5584 4880 3464 -1419 833 -1641 O
HETATM12943 O HOH A1232 15.100 -17.675 17.031 1.00 24.76 O
ANISOU12943 O HOH A1232 3343 3548 2515 350 -40 21 O
HETATM12944 O HOH A1233 29.227 -4.988 8.934 1.00 42.23 O
ANISOU12944 O HOH A1233 3266 7010 5768 -1623 -179 -21 O
HETATM12945 O HOH A1234 -6.503 6.321 49.180 1.00 43.27 O
ANISOU12945 O HOH A1234 7957 4854 3627 180 112 -1402 O
HETATM12946 O HOH A1236 -4.335 -15.250 20.835 1.00 39.41 O
ANISOU12946 O HOH A1236 3259 5189 6525 60 -1060 -1031 O
HETATM12947 O HOH A1237 -4.874 -1.487 47.445 1.00 44.71 O
ANISOU12947 O HOH A1237 5291 7123 4572 1297 171 2059 O
HETATM12948 O HOH A1238 19.561 15.909 13.482 1.00 40.99 O
ANISOU12948 O HOH A1238 2745 6973 5853 -106 -93 -99 O
HETATM12949 O HOH A1239 26.053 6.133 24.730 1.00 47.16 O
ANISOU12949 O HOH A1239 7538 3986 6394 -118 823 -665 O
HETATM12950 O HOH A1240 31.811 -5.047 29.190 1.00 48.76 O
ANISOU12950 O HOH A1240 4408 9782 4335 467 -683 -1281 O
HETATM12951 O HOH A1241 18.172 -21.450 41.334 1.00 41.39 O
ANISOU12951 O HOH A1241 6103 5645 3978 968 -458 352 O
HETATM12952 O HOH A1242 -8.469 25.612 23.734 1.00 49.02 O
ANISOU12952 O HOH A1242 10802 3204 4620 255 -1182 466 O
HETATM12953 O HOH A1243 21.750 4.155 22.058 1.00 41.10 O
ANISOU12953 O HOH A1243 5185 5720 4711 444 1165 327 O
HETATM12954 O HOH A1244 -2.651 6.438 46.079 1.00 34.91 O
ANISOU12954 O HOH A1244 5124 5685 2454 -551 -300 -163 O
HETATM12955 O HOH A1245 17.819 -14.367 15.837 1.00 21.80 O
ANISOU12955 O HOH A1245 2791 2720 2770 -110 -218 97 O
HETATM12956 O HOH A1246 18.979 -16.658 14.956 1.00 23.76 O
ANISOU12956 O HOH A1246 2746 2921 3361 266 683 440 O
HETATM12957 O HOH A1249 14.958 27.321 10.145 1.00 38.32 O
ANISOU12957 O HOH A1249 3842 3273 7444 -1568 1335 -370 O
HETATM12958 O HOH A1250 24.302 -17.174 29.076 1.00 38.60 O
ANISOU12958 O HOH A1250 4513 5081 5072 797 412 780 O
HETATM12959 O HOH A1251 -17.102 -3.291 54.816 1.00 36.67 O
ANISOU12959 O HOH A1251 4957 6580 2395 -511 -535 499 O
HETATM12960 O HOH A1252 -5.510 -9.806 49.984 1.00 34.37 O
ANISOU12960 O HOH A1252 3923 6029 3108 -191 127 -679 O
HETATM12961 O HOH A1253 -3.719 8.732 44.638 1.00 37.58 O
ANISOU12961 O HOH A1253 4304 6629 3342 -2444 8 -1259 O
HETATM12962 O HOH A1254 -4.789 -8.417 47.646 1.00 26.65 O
ANISOU12962 O HOH A1254 5147 2583 2395 -370 282 -304 O
ATOM 4103 N ASN B 2 -21.507 -7.191 56.267 1.00 31.38 N
ANISOU 4103 N ASN B 2 5571 3062 3288 865 -83 76 N
ATOM 4104 CA ASN B 2 -21.503 -7.929 54.995 1.00 25.72 C
ANISOU 4104 CA ASN B 2 4583 2409 2778 728 357 319 C
ATOM 4105 CB ASN B 2 -21.610 -6.998 53.792 1.00 22.67 C
ANISOU 4105 CB ASN B 2 3887 2724 2003 689 936 12 C
ATOM 4106 CG ASN B 2 -22.897 -6.197 53.757 1.00 22.91 C
ANISOU 4106 CG ASN B 2 4108 2584 2013 792 1165 77 C
ATOM 4107 OD1 ASN B 2 -23.962 -6.735 53.477 1.00 28.94 O
ANISOU 4107 OD1 ASN B 2 4839 3013 3144 464 1068 -434 O
ATOM 4108 ND2 ASN B 2 -22.801 -4.910 54.006 1.00 24.61 N
ANISOU 4108 ND2 ASN B 2 4738 2321 2291 943 680 299 N
ATOM 4109 C ASN B 2 -20.222 -8.759 54.864 1.00 26.04 C
ANISOU 4109 C ASN B 2 4747 2611 2534 749 106 -81 C
ATOM 4110 O ASN B 2 -19.134 -8.330 55.234 1.00 25.74 O
ANISOU 4110 O ASN B 2 4911 2410 2458 519 79 106 O
ATOM 4111 N THR B 3 -20.369 -9.938 54.262 1.00 26.08 N
ANISOU 4111 N THR B 3 5091 2624 2191 631 268 -66 N
ATOM 4112 CA ATHR B 3 -19.250 -10.816 53.981 0.50 26.20 C
ANISOU 4112 CA ATHR B 3 4995 2845 2113 763 211 -29 C
ATOM 4113 CA BTHR B 3 -19.251 -10.827 53.982 0.50 25.64 C
ANISOU 4113 CA BTHR B 3 5148 2687 1907 646 425 23 C
ATOM 4114 CB ATHR B 3 -19.097 -11.847 55.107 0.50 28.61 C
ANISOU 4114 CB ATHR B 3 5087 2920 2862 1277 -19 191 C
ATOM 4115 CB BTHR B 3 -19.116 -11.950 55.021 0.50 26.00 C
ANISOU 4115 CB BTHR B 3 5818 2690 1371 727 300 -323 C
ATOM 4116 OG1ATHR B 3 -18.113 -12.814 54.739 0.50 29.48 O
ANISOU 4116 OG1ATHR B 3 4657 3872 2670 1662 -175 -12 O
ATOM 4117 OG1BTHR B 3 -20.033 -12.998 54.707 0.50 29.91 O
ANISOU 4117 OG1BTHR B 3 5895 3450 2017 284 728 -306 O
ATOM 4118 CG2ATHR B 3 -20.407 -12.515 55.463 0.50 29.35 C
ANISOU 4118 CG2ATHR B 3 5312 3074 2765 1084 10 285 C
ATOM 4119 CG2BTHR B 3 -19.354 -11.483 56.435 0.50 23.99 C
ANISOU 4119 CG2BTHR B 3 5706 2210 1198 660 305 -109 C
ATOM 4120 C THR B 3 -19.439 -11.392 52.579 1.00 24.88 C
ANISOU 4120 C THR B 3 4784 2558 2108 638 128 45 C
ATOM 4121 O THR B 3 -20.557 -11.716 52.174 1.00 24.19 O
ANISOU 4121 O THR B 3 4458 2683 2050 511 468 137 O
ATOM 4122 N PRO B 4 -18.365 -11.515 51.775 1.00 22.24 N
ANISOU 4122 N PRO B 4 4687 1933 1828 434 283 274 N
ATOM 4123 CA PRO B 4 -18.505 -12.093 50.444 1.00 21.72 C
ANISOU 4123 CA PRO B 4 4427 1936 1888 119 105 274 C
ATOM 4124 CB PRO B 4 -17.071 -12.134 49.906 1.00 23.25 C
ANISOU 4124 CB PRO B 4 4306 2100 2424 401 95 53 C
ATOM 4125 CG PRO B 4 -16.412 -10.985 50.647 1.00 26.42 C
ANISOU 4125 CG PRO B 4 4863 2617 2558 168 -12 -6 C
ATOM 4126 CD PRO B 4 -16.990 -11.075 52.042 1.00 25.55 C
ANISOU 4126 CD PRO B 4 4742 2529 2435 230 30 -30 C
ATOM 4127 C PRO B 4 -19.098 -13.491 50.533 1.00 21.21 C
ANISOU 4127 C PRO B 4 4223 1885 1949 205 335 249 C
ATOM 4128 O PRO B 4 -18.745 -14.279 51.418 1.00 23.08 O
ANISOU 4128 O PRO B 4 4809 1931 2028 538 363 292 O
ATOM 4129 N PRO B 5 -20.013 -13.837 49.609 1.00 19.44 N
ANISOU 4129 N PRO B 5 3803 1803 1779 326 411 156 N
ATOM 4130 CA PRO B 5 -20.607 -15.170 49.604 1.00 20.22 C
ANISOU 4130 CA PRO B 5 3483 2058 2142 151 403 91 C
ATOM 4131 CB PRO B 5 -21.718 -15.038 48.558 1.00 21.93 C
ANISOU 4131 CB PRO B 5 3648 2313 2368 167 232 215 C
ATOM 4132 CG PRO B 5 -21.166 -14.007 47.596 1.00 21.08 C
ANISOU 4132 CG PRO B 5 3439 2144 2425 77 47 311 C
ATOM 4133 CD PRO B 5 -20.496 -12.995 48.501 1.00 19.60 C
ANISOU 4133 CD PRO B 5 3477 1824 2144 169 316 296 C
ATOM 4134 C PRO B 5 -19.606 -16.252 49.176 1.00 19.98 C
ANISOU 4134 C PRO B 5 3416 2073 2101 116 648 33 C
ATOM 4135 O PRO B 5 -18.700 -15.986 48.399 1.00 20.85 O
ANISOU 4135 O PRO B 5 3303 2251 2365 432 767 135 O
ATOM 4136 N GLU B 6 -19.814 -17.462 49.681 1.00 19.87 N
ANISOU 4136 N GLU B 6 3481 2163 1905 403 653 224 N
ATOM 4137 CA GLU B 6 -19.095 -18.641 49.244 1.00 21.24 C
ANISOU 4137 CA GLU B 6 3787 2100 2182 444 851 194 C
ATOM 4138 CB GLU B 6 -19.519 -19.866 50.069 1.00 24.23 C
ANISOU 4138 CB GLU B 6 4397 2440 2369 497 1221 452 C
ATOM 4139 CG GLU B 6 -18.889 -21.189 49.620 1.00 26.41 C
ANISOU 4139 CG GLU B 6 4781 2752 2499 764 1334 565 C
ATOM 4140 CD GLU B 6 -19.519 -21.932 48.434 1.00 29.33 C
ANISOU 4140 CD GLU B 6 4858 3188 3095 497 1044 518 C
ATOM 4141 OE1 GLU B 6 -20.681 -21.659 48.077 1.00 32.87 O
ANISOU 4141 OE1 GLU B 6 4915 3830 3743 1053 691 375 O
ATOM 4142 OE2 GLU B 6 -18.831 -22.797 47.858 1.00 33.31 O
ANISOU 4142 OE2 GLU B 6 5397 3689 3571 874 1406 637 O
ATOM 4143 C GLU B 6 -19.388 -18.881 47.766 1.00 21.15 C
ANISOU 4143 C GLU B 6 3333 2423 2279 444 841 74 C
ATOM 4144 O GLU B 6 -20.553 -18.773 47.311 1.00 21.22 O
ANISOU 4144 O GLU B 6 3204 2235 2622 457 894 144 O
ATOM 4145 N LEU B 7 -18.321 -19.186 47.024 1.00 17.79 N
ANISOU 4145 N LEU B 7 2855 1630 2272 462 587 238 N
ATOM 4146 CA LEU B 7 -18.407 -19.582 45.616 1.00 16.84 C
ANISOU 4146 CA LEU B 7 2733 1541 2120 263 610 180 C
ATOM 4147 CB LEU B 7 -17.662 -18.558 44.751 1.00 15.83 C
ANISOU 4147 CB LEU B 7 2656 1465 1894 327 480 192 C
ATOM 4148 CG LEU B 7 -18.191 -17.124 44.859 1.00 16.47 C
ANISOU 4148 CG LEU B 7 2596 1539 2122 443 538 286 C
ATOM 4149 CD1 LEU B 7 -17.333 -16.152 44.069 1.00 16.99 C
ANISOU 4149 CD1 LEU B 7 2508 1692 2256 386 696 164 C
ATOM 4150 CD2 LEU B 7 -19.636 -17.040 44.391 1.00 17.52 C
ANISOU 4150 CD2 LEU B 7 2557 1812 2286 228 555 461 C
ATOM 4151 C LEU B 7 -17.777 -20.964 45.442 1.00 17.37 C
ANISOU 4151 C LEU B 7 2752 1509 2336 182 632 179 C
ATOM 4152 O LEU B 7 -16.706 -21.252 45.986 1.00 19.40 O
ANISOU 4152 O LEU B 7 2717 1984 2668 455 723 169 O
ATOM 4153 N ASP B 8 -18.444 -21.795 44.639 1.00 18.06 N
ANISOU 4153 N ASP B 8 2802 1671 2387 176 753 -89 N
ATOM 4154 CA ASP B 8 -17.922 -23.116 44.313 1.00 18.05 C
ANISOU 4154 CA ASP B 8 2579 1851 2428 289 658 -266 C
ATOM 4155 CB ASP B 8 -18.999 -24.002 43.710 1.00 21.94 C
ANISOU 4155 CB ASP B 8 2968 2313 3054 -55 537 -457 C
ATOM 4156 CG ASP B 8 -20.128 -24.392 44.647 1.00 25.62 C
ANISOU 4156 CG ASP B 8 3404 2816 3513 -570 740 -388 C
ATOM 4157 OD1 ASP B 8 -20.015 -24.218 45.870 1.00 27.80 O
ANISOU 4157 OD1 ASP B 8 4283 2800 3477 -691 1307 -291 O
ATOM 4158 OD2 ASP B 8 -21.118 -24.900 44.117 1.00 33.93 O
ANISOU 4158 OD2 ASP B 8 2924 4691 5276 -630 519 -192 O
ATOM 4159 C ASP B 8 -16.767 -22.977 43.324 1.00 17.13 C
ANISOU 4159 C ASP B 8 2456 1791 2259 125 451 -116 C
ATOM 4160 O ASP B 8 -16.672 -21.991 42.594 1.00 17.51 O
ANISOU 4160 O ASP B 8 2556 1823 2272 232 726 -79 O
ATOM 4161 N THR B 9 -15.900 -23.988 43.305 1.00 17.29 N
ANISOU 4161 N THR B 9 2648 1791 2128 222 390 -179 N
ATOM 4162 CA THR B 9 -14.710 -23.985 42.450 1.00 17.08 C
ANISOU 4162 CA THR B 9 2718 1853 1917 239 402 -270 C
ATOM 4163 CB THR B 9 -13.429 -24.071 43.283 1.00 17.52 C
ANISOU 4163 CB THR B 9 2532 1982 2141 440 402 -48 C
ATOM 4164 OG1 THR B 9 -13.517 -25.166 44.203 1.00 18.66 O
ANISOU 4164 OG1 THR B 9 2983 2041 2065 378 232 -41 O
ATOM 4165 CG2 THR B 9 -13.188 -22.799 44.064 1.00 17.74 C
ANISOU 4165 CG2 THR B 9 2681 2122 1935 348 119 81 C
ATOM 4166 C THR B 9 -14.760 -25.126 41.428 1.00 17.39 C
ANISOU 4166 C THR B 9 2792 1816 1997 247 378 -277 C
ATOM 4167 O THR B 9 -15.355 -26.194 41.655 1.00 18.52 O
ANISOU 4167 O THR B 9 2923 2013 2100 249 284 -93 O
ATOM 4168 N VAL B 10 -14.120 -24.859 40.288 1.00 15.87 N
ANISOU 4168 N VAL B 10 2460 1518 2049 479 356 -191 N
ATOM 4169 CA VAL B 10 -13.866 -25.826 39.229 1.00 15.73 C
ANISOU 4169 CA VAL B 10 2240 1646 2087 241 165 -396 C
ATOM 4170 CB VAL B 10 -14.767 -25.574 38.018 1.00 16.24 C
ANISOU 4170 CB VAL B 10 2369 1711 2088 365 196 -280 C
ATOM 4171 CG1 VAL B 10 -16.240 -25.647 38.408 1.00 18.69 C
ANISOU 4171 CG1 VAL B 10 2447 2300 2353 100 188 -140 C
ATOM 4172 CG2 VAL B 10 -14.449 -24.255 37.329 1.00 17.05 C
ANISOU 4172 CG2 VAL B 10 2572 1944 1961 299 438 -161 C
ATOM 4173 C VAL B 10 -12.391 -25.746 38.826 1.00 15.79 C
ANISOU 4173 C VAL B 10 2076 1790 2132 343 46 -376 C
ATOM 4174 O VAL B 10 -11.706 -24.796 39.183 1.00 16.64 O
ANISOU 4174 O VAL B 10 2271 1687 2363 272 396 -441 O
ATOM 4175 N LEU B 11 -11.914 -26.762 38.103 1.00 17.13 N
ANISOU 4175 N LEU B 11 2461 1869 2177 138 -26 -626 N
ATOM 4176 CA LEU B 11 -10.572 -26.750 37.517 1.00 19.09 C
ANISOU 4176 CA LEU B 11 2404 2404 2444 309 -170 -538 C
ATOM 4177 CB LEU B 11 -9.841 -28.052 37.842 1.00 23.34 C
ANISOU 4177 CB LEU B 11 3224 2444 3199 535 -202 -670 C
ATOM 4178 CG LEU B 11 -9.512 -28.298 39.297 1.00 24.09 C
ANISOU 4178 CG LEU B 11 3431 2360 3359 481 -73 -26 C
ATOM 4179 CD1 LEU B 11 -8.556 -29.471 39.393 1.00 25.60 C
ANISOU 4179 CD1 LEU B 11 3227 2682 3817 479 -679 504 C
ATOM 4180 CD2 LEU B 11 -8.918 -27.059 39.941 1.00 24.07 C
ANISOU 4180 CD2 LEU B 11 3421 2499 3225 73 -444 373 C
ATOM 4181 C LEU B 11 -10.685 -26.611 36.002 1.00 18.62 C
ANISOU 4181 C LEU B 11 1988 2797 2288 440 -182 -904 C
ATOM 4182 O LEU B 11 -11.072 -27.560 35.333 1.00 22.72 O
ANISOU 4182 O LEU B 11 2639 2990 3003 324 -302 -1245 O
ATOM 4183 N GLN B 12 -10.341 -25.437 35.490 1.00 18.84 N
ANISOU 4183 N GLN B 12 2216 2868 2072 437 27 -1039 N
ATOM 4184 CA GLN B 12 -10.322 -25.218 34.045 1.00 18.73 C
ANISOU 4184 CA GLN B 12 2087 3009 2017 611 -2 -1101 C
ATOM 4185 CB GLN B 12 -10.100 -23.744 33.724 1.00 21.65 C
ANISOU 4185 CB GLN B 12 2771 3083 2372 756 10 -859 C
ATOM 4186 CG GLN B 12 -10.059 -23.418 32.243 1.00 24.62 C
ANISOU 4186 CG GLN B 12 3383 3540 2432 688 15 -1050 C
ATOM 4187 CD GLN B 12 -11.412 -23.585 31.596 1.00 28.49 C
ANISOU 4187 CD GLN B 12 3894 4185 2747 484 -407 -624 C
ATOM 4188 OE1 GLN B 12 -12.414 -23.059 32.074 1.00 33.95 O
ANISOU 4188 OE1 GLN B 12 4178 4844 3876 1119 -156 18 O
ATOM 4189 NE2 GLN B 12 -11.446 -24.330 30.496 1.00 36.19 N
ANISOU 4189 NE2 GLN B 12 5559 5135 3054 569 -813 -1040 N
ATOM 4190 C GLN B 12 -9.192 -26.090 33.481 1.00 18.23 C
ANISOU 4190 C GLN B 12 2136 2639 2152 434 286 -929 C
ATOM 4191 O GLN B 12 -8.088 -26.074 34.003 1.00 19.29 O
ANISOU 4191 O GLN B 12 2062 2606 2660 562 191 -837 O
ATOM 4192 N ALA B 13 -9.497 -26.856 32.433 1.00 18.28 N
ANISOU 4192 N ALA B 13 2026 2621 2297 156 399 -955 N
ATOM 4193 CA ALA B 13 -8.548 -27.771 31.844 1.00 17.87 C
ANISOU 4193 CA ALA B 13 2225 2455 2107 178 491 -769 C
ATOM 4194 CB ALA B 13 -8.814 -29.179 32.331 1.00 20.41 C
ANISOU 4194 CB ALA B 13 2871 2649 2233 112 313 -539 C
ATOM 4195 C ALA B 13 -8.694 -27.695 30.330 1.00 17.16 C
ANISOU 4195 C ALA B 13 2222 2229 2069 188 310 -797 C
ATOM 4196 O ALA B 13 -9.786 -27.423 29.823 1.00 19.44 O
ANISOU 4196 O ALA B 13 2254 2612 2517 400 356 -508 O
ATOM 4197 N PRO B 14 -7.618 -27.942 29.564 1.00 17.63 N
ANISOU 4197 N PRO B 14 2387 2253 2059 285 377 -730 N
ATOM 4198 CA PRO B 14 -7.733 -27.888 28.114 1.00 18.49 C
ANISOU 4198 CA PRO B 14 2621 2292 2109 276 403 -581 C
ATOM 4199 CB PRO B 14 -6.305 -28.127 27.609 1.00 21.77 C
ANISOU 4199 CB PRO B 14 2521 2920 2831 48 430 -475 C
ATOM 4200 CG PRO B 14 -5.556 -28.743 28.778 1.00 21.60 C
ANISOU 4200 CG PRO B 14 2574 2946 2685 421 852 -200 C
ATOM 4201 CD PRO B 14 -6.291 -28.342 30.041 1.00 19.35 C
ANISOU 4201 CD PRO B 14 2410 2544 2395 210 494 -473 C
ATOM 4202 C PRO B 14 -8.674 -28.977 27.586 1.00 16.89 C
ANISOU 4202 C PRO B 14 2209 2277 1929 347 267 -382 C
ATOM 4203 O PRO B 14 -8.743 -30.084 28.144 1.00 16.67 O
ANISOU 4203 O PRO B 14 2293 2142 1898 312 124 -465 O
ATOM 4204 N TYR B 15 -9.376 -28.661 26.503 1.00 16.90 N
ANISOU 4204 N TYR B 15 2443 2049 1926 293 224 -383 N
ATOM 4205 CA TYR B 15 -10.284 -29.603 25.862 1.00 16.51 C
ANISOU 4205 CA TYR B 15 2539 1896 1837 188 69 -153 C
ATOM 4206 CB TYR B 15 -11.024 -28.886 24.737 1.00 16.95 C
ANISOU 4206 CB TYR B 15 2527 1668 2245 237 135 163 C
ATOM 4207 CG TYR B 15 -12.198 -29.614 24.139 1.00 17.85 C
ANISOU 4207 CG TYR B 15 2730 1655 2397 442 -170 -87 C
ATOM 4208 CD1 TYR B 15 -13.375 -29.752 24.853 1.00 20.72 C
ANISOU 4208 CD1 TYR B 15 2913 2138 2819 301 53 0 C
ATOM 4209 CE1 TYR B 15 -14.482 -30.385 24.313 1.00 22.14 C
ANISOU 4209 CE1 TYR B 15 2686 2416 3308 411 58 -324 C
ATOM 4210 CZ TYR B 15 -14.435 -30.866 23.021 1.00 22.49 C
ANISOU 4210 CZ TYR B 15 3112 2099 3333 309 -410 -415 C
ATOM 4211 OH TYR B 15 -15.532 -31.475 22.472 1.00 26.35 O
ANISOU 4211 OH TYR B 15 3146 2356 4508 209 -550 -618 O
ATOM 4212 CE2 TYR B 15 -13.286 -30.685 22.273 1.00 22.22 C
ANISOU 4212 CE2 TYR B 15 3172 2159 3110 453 -349 -469 C
ATOM 4213 CD2 TYR B 15 -12.172 -30.085 22.840 1.00 20.96 C
ANISOU 4213 CD2 TYR B 15 3319 2060 2586 323 -132 -304 C
ATOM 4214 C TYR B 15 -9.526 -30.829 25.337 1.00 17.53 C
ANISOU 4214 C TYR B 15 2841 2011 1808 331 -168 -269 C
ATOM 4215 O TYR B 15 -10.143 -31.883 25.172 1.00 18.89 O
ANISOU 4215 O TYR B 15 3017 1970 2190 269 -487 -258 O
ATOM 4216 N ALA B 16 -8.202 -30.715 25.160 1.00 18.25 N
ANISOU 4216 N ALA B 16 3046 1943 1943 373 58 -327 N
ATOM 4217 CA ALA B 16 -7.350 -31.854 24.818 1.00 20.26 C
ANISOU 4217 CA ALA B 16 3195 2382 2118 757 6 -163 C
ATOM 4218 CB ALA B 16 -5.903 -31.409 24.786 1.00 20.34 C
ANISOU 4218 CB ALA B 16 3323 2055 2348 748 378 -92 C
ATOM 4219 C ALA B 16 -7.525 -33.004 25.825 1.00 19.82 C
ANISOU 4219 C ALA B 16 3313 1969 2246 294 289 -354 C
ATOM 4220 O ALA B 16 -7.345 -34.157 25.463 1.00 22.57 O
ANISOU 4220 O ALA B 16 4314 2129 2130 988 -12 -180 O
ATOM 4221 N TYR B 17 -7.842 -32.691 27.094 1.00 17.01 N
ANISOU 4221 N TYR B 17 2714 1720 2029 487 -3 -162 N
ATOM 4222 CA TYR B 17 -8.001 -33.709 28.117 1.00 16.86 C
ANISOU 4222 CA TYR B 17 2525 2060 1818 414 -51 -140 C
ATOM 4223 CB TYR B 17 -7.644 -33.144 29.493 1.00 17.39 C
ANISOU 4223 CB TYR B 17 2365 2493 1747 474 -116 44 C
ATOM 4224 CG TYR B 17 -6.177 -32.957 29.777 1.00 16.43 C
ANISOU 4224 CG TYR B 17 2156 2213 1871 493 195 -52 C
ATOM 4225 CD1 TYR B 17 -5.212 -33.788 29.254 1.00 18.05 C
ANISOU 4225 CD1 TYR B 17 2331 2615 1911 483 344 -294 C
ATOM 4226 CE1 TYR B 17 -3.871 -33.623 29.558 1.00 17.72 C
ANISOU 4226 CE1 TYR B 17 2029 2589 2113 833 611 -318 C
ATOM 4227 CZ TYR B 17 -3.463 -32.632 30.429 1.00 17.52 C
ANISOU 4227 CZ TYR B 17 2000 2819 1838 758 432 -232 C
ATOM 4228 OH TYR B 17 -2.136 -32.484 30.770 1.00 19.61 O
ANISOU 4228 OH TYR B 17 1971 3232 2247 852 388 -23 O
ATOM 4229 CE2 TYR B 17 -4.424 -31.805 30.980 1.00 16.89 C
ANISOU 4229 CE2 TYR B 17 1928 2195 2295 604 187 -423 C
ATOM 4230 CD2 TYR B 17 -5.759 -31.982 30.661 1.00 17.72 C
ANISOU 4230 CD2 TYR B 17 1946 2383 2403 481 195 -371 C
ATOM 4231 C TYR B 17 -9.429 -34.268 28.135 1.00 16.95 C
ANISOU 4231 C TYR B 17 2741 1891 1808 279 -313 -42 C
ATOM 4232 O TYR B 17 -9.720 -35.181 28.924 1.00 18.37 O
ANISOU 4232 O TYR B 17 2964 1958 2056 117 -209 95 O
ATOM 4233 N ASN B 18 -10.317 -33.748 27.273 1.00 17.82 N
ANISOU 4233 N ASN B 18 2764 1688 2319 350 -549 -232 N
ATOM 4234 CA ASN B 18 -11.597 -34.423 26.989 1.00 17.82 C
ANISOU 4234 CA ASN B 18 2827 1762 2181 301 -399 -122 C
ATOM 4235 CB ASN B 18 -12.674 -33.458 26.477 1.00 18.55 C
ANISOU 4235 CB ASN B 18 2886 1785 2375 357 -494 -76 C
ATOM 4236 CG ASN B 18 -13.973 -34.160 26.120 1.00 20.18 C
ANISOU 4236 CG ASN B 18 2994 2157 2517 296 -475 -200 C
ATOM 4237 OD1 ASN B 18 -14.381 -35.110 26.804 1.00 21.62 O
ANISOU 4237 OD1 ASN B 18 2938 2070 3204 503 -58 -115 O
ATOM 4238 ND2 ASN B 18 -14.618 -33.706 25.057 1.00 18.47 N
ANISOU 4238 ND2 ASN B 18 2578 2105 2333 562 -176 -263 N
ATOM 4239 C ASN B 18 -11.282 -35.521 25.973 1.00 16.13 C
ANISOU 4239 C ASN B 18 2681 1475 1973 271 -278 107 C
ATOM 4240 O ASN B 18 -11.576 -35.402 24.794 1.00 18.11 O
ANISOU 4240 O ASN B 18 2920 2000 1960 295 -362 116 O
ATOM 4241 N TRP B 19 -10.661 -36.589 26.462 1.00 15.45 N
ANISOU 4241 N TRP B 19 2454 1475 1939 218 -291 72 N
ATOM 4242 CA TRP B 19 -10.109 -37.606 25.585 1.00 15.02 C
ANISOU 4242 CA TRP B 19 2150 1771 1785 64 -180 22 C
ATOM 4243 CB TRP B 19 -9.551 -38.776 26.390 1.00 15.55 C
ANISOU 4243 CB TRP B 19 2068 1826 2011 131 -39 138 C
ATOM 4244 CG TRP B 19 -8.507 -38.416 27.393 1.00 15.88 C
ANISOU 4244 CG TRP B 19 2135 2004 1892 153 -103 183 C
ATOM 4245 CD1 TRP B 19 -8.684 -38.275 28.739 1.00 16.71 C
ANISOU 4245 CD1 TRP B 19 2257 2146 1947 -72 251 117 C
ATOM 4246 NE1 TRP B 19 -7.494 -37.975 29.347 1.00 17.61 N
ANISOU 4246 NE1 TRP B 19 2343 2560 1787 81 148 159 N
ATOM 4247 CE2 TRP B 19 -6.514 -37.883 28.388 1.00 15.63 C
ANISOU 4247 CE2 TRP B 19 2070 2107 1761 108 97 85 C
ATOM 4248 CD2 TRP B 19 -7.121 -38.131 27.139 1.00 14.55 C
ANISOU 4248 CD2 TRP B 19 2118 1658 1751 193 3 209 C
ATOM 4249 CE3 TRP B 19 -6.325 -38.154 25.998 1.00 15.10 C
ANISOU 4249 CE3 TRP B 19 2168 1934 1635 102 -130 188 C
ATOM 4250 CZ3 TRP B 19 -4.991 -37.853 26.096 1.00 15.16 C
ANISOU 4250 CZ3 TRP B 19 2056 1973 1732 169 59 120 C
ATOM 4251 CH2 TRP B 19 -4.416 -37.607 27.337 1.00 16.32 C
ANISOU 4251 CH2 TRP B 19 1925 2358 1915 138 -219 267 C
ATOM 4252 CZ2 TRP B 19 -5.160 -37.590 28.496 1.00 16.59 C
ANISOU 4252 CZ2 TRP B 19 2228 2480 1594 78 -293 203 C
ATOM 4253 C TRP B 19 -11.202 -38.128 24.668 1.00 14.11 C
ANISOU 4253 C TRP B 19 1884 1700 1778 187 -203 264 C
ATOM 4254 O TRP B 19 -12.269 -38.516 25.141 1.00 14.87 O
ANISOU 4254 O TRP B 19 1997 1769 1883 -117 39 64 O
ATOM 4255 N PRO B 20 -10.976 -38.192 23.345 1.00 14.47 N
ANISOU 4255 N PRO B 20 1889 1745 1863 36 78 278 N
ATOM 4256 CA PRO B 20 -11.957 -38.818 22.466 1.00 14.85 C
ANISOU 4256 CA PRO B 20 2021 1750 1869 13 -13 256 C
ATOM 4257 CB PRO B 20 -11.490 -38.430 21.056 1.00 15.18 C
ANISOU 4257 CB PRO B 20 2214 1751 1803 77 3 159 C
ATOM 4258 CG PRO B 20 -10.505 -37.318 21.271 1.00 15.26 C
ANISOU 4258 CG PRO B 20 2072 1674 2051 190 -76 256 C
ATOM 4259 CD PRO B 20 -9.839 -37.634 22.591 1.00 14.37 C
ANISOU 4259 CD PRO B 20 1916 1610 1931 108 88 368 C
ATOM 4260 C PRO B 20 -11.950 -40.335 22.662 1.00 15.05 C
ANISOU 4260 C PRO B 20 2077 1787 1852 207 115 416 C
ATOM 4261 O PRO B 20 -10.890 -40.960 22.596 1.00 14.53 O
ANISOU 4261 O PRO B 20 2117 1592 1810 244 61 271 O
ATOM 4262 N THR B 21 -13.131 -40.882 22.955 1.00 14.67 N
ANISOU 4262 N THR B 21 2084 1582 1908 153 2 319 N
ATOM 4263 CA THR B 21 -13.338 -42.311 23.185 1.00 15.43 C
ANISOU 4263 CA THR B 21 2218 1676 1968 49 71 369 C
ATOM 4264 CB THR B 21 -13.416 -42.639 24.678 1.00 17.58 C
ANISOU 4264 CB THR B 21 2668 2034 1977 37 41 365 C
ATOM 4265 OG1 THR B 21 -14.676 -42.190 25.194 1.00 19.32 O
ANISOU 4265 OG1 THR B 21 2817 2359 2163 -94 394 266 O
ATOM 4266 CG2 THR B 21 -12.269 -42.060 25.481 1.00 18.00 C
ANISOU 4266 CG2 THR B 21 2678 2190 1971 160 -71 304 C
ATOM 4267 C THR B 21 -14.658 -42.747 22.550 1.00 15.54 C
ANISOU 4267 C THR B 21 2379 1696 1827 -19 17 336 C
ATOM 4268 O THR B 21 -15.414 -41.951 22.054 1.00 15.31 O
ANISOU 4268 O THR B 21 2019 1829 1967 -67 -134 350 O
ATOM 4269 N SER B 22 -14.942 -44.047 22.659 1.00 17.39 N
ANISOU 4269 N SER B 22 2530 1642 2432 -101 -86 454 N
ATOM 4270 CA SER B 22 -16.190 -44.579 22.164 1.00 19.77 C
ANISOU 4270 CA SER B 22 2637 2166 2708 -219 -2 383 C
ATOM 4271 CB SER B 22 -16.177 -46.075 22.176 1.00 23.41 C
ANISOU 4271 CB SER B 22 3139 2158 3594 -183 14 177 C
ATOM 4272 OG SER B 22 -16.159 -46.568 23.499 1.00 25.68 O
ANISOU 4272 OG SER B 22 3601 1975 4180 -446 -328 833 O
ATOM 4273 C SER B 22 -17.385 -44.024 22.943 1.00 20.48 C
ANISOU 4273 C SER B 22 2540 2440 2798 -217 -50 356 C
ATOM 4274 O SER B 22 -18.509 -44.171 22.477 1.00 22.07 O
ANISOU 4274 O SER B 22 2803 2749 2832 -208 -415 290 O
ATOM 4275 N LYS B 23 -17.150 -43.415 24.110 1.00 18.97 N
ANISOU 4275 N LYS B 23 2574 2104 2530 -257 -1 639 N
ATOM 4276 CA LYS B 23 -18.244 -42.874 24.926 1.00 21.59 C
ANISOU 4276 CA LYS B 23 2836 2621 2745 47 181 603 C
ATOM 4277 CB LYS B 23 -17.844 -42.815 26.403 1.00 24.67 C
ANISOU 4277 CB LYS B 23 3477 3178 2718 344 411 680 C
ATOM 4278 CG LYS B 23 -17.678 -44.163 27.074 1.00 29.75 C
ANISOU 4278 CG LYS B 23 4126 3695 3483 427 315 1283 C
ATOM 4279 CD LYS B 23 -17.180 -44.040 28.486 1.00 36.58 C
ANISOU 4279 CD LYS B 23 5185 4993 3720 570 8 1221 C
ATOM 4280 CE LYS B 23 -17.120 -45.383 29.184 1.00 44.15 C
ANISOU 4280 CE LYS B 23 6362 5571 4839 504 -265 1879 C
ATOM 4281 NZ LYS B 23 -16.751 -45.240 30.613 1.00 51.00 N
ANISOU 4281 NZ LYS B 23 6858 7209 5308 513 -729 1358 N
ATOM 4282 C LYS B 23 -18.661 -41.474 24.461 1.00 19.37 C
ANISOU 4282 C LYS B 23 1994 2769 2594 -23 132 631 C
ATOM 4283 O LYS B 23 -19.786 -41.061 24.757 1.00 25.08 O
ANISOU 4283 O LYS B 23 2391 3300 3838 248 502 550 O
ATOM 4284 N ASN B 24 -17.775 -40.745 23.772 1.00 17.82 N
ANISOU 4284 N ASN B 24 2091 2255 2421 -37 112 447 N
ATOM 4285 CA ASN B 24 -18.058 -39.353 23.447 1.00 16.30 C
ANISOU 4285 CA ASN B 24 1760 2281 2152 187 -9 193 C
ATOM 4286 CB ASN B 24 -17.316 -38.380 24.372 1.00 16.24 C
ANISOU 4286 CB ASN B 24 1931 2510 1727 42 141 103 C
ATOM 4287 CG ASN B 24 -15.807 -38.413 24.219 1.00 16.56 C
ANISOU 4287 CG ASN B 24 1858 2653 1779 198 -141 -17 C
ATOM 4288 OD1 ASN B 24 -15.292 -39.129 23.389 1.00 18.30 O
ANISOU 4288 OD1 ASN B 24 1825 2636 2491 66 45 -297 O
ATOM 4289 ND2 ASN B 24 -15.092 -37.605 24.985 1.00 20.85 N
ANISOU 4289 ND2 ASN B 24 2360 3298 2264 74 -107 -540 N
ATOM 4290 C ASN B 24 -17.769 -39.002 21.981 1.00 17.77 C
ANISOU 4290 C ASN B 24 2625 2161 1962 160 -173 -32 C
ATOM 4291 O ASN B 24 -17.770 -37.841 21.667 1.00 22.98 O
ANISOU 4291 O ASN B 24 3733 2486 2511 454 240 506 O
ATOM 4292 N VAL B 25 -17.514 -39.982 21.105 1.00 16.46 N
ANISOU 4292 N VAL B 25 2505 1989 1758 79 -277 141 N
ATOM 4293 CA VAL B 25 -17.295 -39.733 19.693 1.00 16.80 C
ANISOU 4293 CA VAL B 25 2594 1985 1805 -24 -376 278 C
ATOM 4294 CB VAL B 25 -15.942 -40.278 19.217 1.00 16.69 C
ANISOU 4294 CB VAL B 25 2570 1921 1850 -15 -294 254 C
ATOM 4295 CG1 VAL B 25 -15.820 -40.214 17.694 1.00 18.26 C
ANISOU 4295 CG1 VAL B 25 2982 2006 1950 28 -238 382 C
ATOM 4296 CG2 VAL B 25 -14.790 -39.538 19.873 1.00 17.63 C
ANISOU 4296 CG2 VAL B 25 2587 2147 1963 -236 -300 262 C
ATOM 4297 C VAL B 25 -18.414 -40.394 18.891 1.00 16.94 C
ANISOU 4297 C VAL B 25 2564 2069 1802 -170 -297 235 C
ATOM 4298 O VAL B 25 -18.726 -41.557 19.104 1.00 19.35 O
ANISOU 4298 O VAL B 25 2794 2347 2211 -358 -21 592 O
ATOM 4299 N LYS B 26 -18.987 -39.626 17.960 1.00 16.27 N
ANISOU 4299 N LYS B 26 2315 2057 1808 47 -215 132 N
ATOM 4300 CA LYS B 26 -19.820 -40.150 16.884 1.00 16.31 C
ANISOU 4300 CA LYS B 26 2061 2317 1818 -205 -163 201 C
ATOM 4301 CB LYS B 26 -21.258 -39.622 16.993 1.00 20.27 C
ANISOU 4301 CB LYS B 26 2312 3183 2206 53 -187 61 C
ATOM 4302 CG LYS B 26 -21.975 -40.039 18.269 1.00 22.53 C
ANISOU 4302 CG LYS B 26 2433 3875 2251 -46 -56 180 C
ATOM 4303 CD LYS B 26 -23.424 -39.633 18.379 1.00 27.59 C
ANISOU 4303 CD LYS B 26 2752 4713 3017 110 171 509 C
ATOM 4304 CE LYS B 26 -23.985 -40.086 19.709 1.00 32.03 C
ANISOU 4304 CE LYS B 26 3625 5569 2976 -74 473 199 C
ATOM 4305 NZ LYS B 26 -25.341 -39.553 19.947 1.00 40.58 N
ANISOU 4305 NZ LYS B 26 4013 6747 4656 18 438 128 N
ATOM 4306 C LYS B 26 -19.193 -39.764 15.539 1.00 16.89 C
ANISOU 4306 C LYS B 26 2354 2198 1865 42 -131 184 C
ATOM 4307 O LYS B 26 -18.444 -38.785 15.440 1.00 18.13 O
ANISOU 4307 O LYS B 26 2453 2366 2067 -23 -152 436 O
ATOM 4308 N ILE B 27 -19.501 -40.559 14.514 1.00 15.67 N
ANISOU 4308 N ILE B 27 2553 1622 1777 202 -202 403 N
ATOM 4309 CA ILE B 27 -18.988 -40.324 13.168 1.00 15.18 C
ANISOU 4309 CA ILE B 27 2282 1663 1822 157 -142 355 C
ATOM 4310 CB ILE B 27 -18.328 -41.570 12.589 1.00 16.24 C
ANISOU 4310 CB ILE B 27 2120 1828 2222 415 -162 415 C
ATOM 4311 CG1 ILE B 27 -17.207 -42.070 13.509 1.00 18.16 C
ANISOU 4311 CG1 ILE B 27 2541 2238 2119 547 -341 365 C
ATOM 4312 CG2 ILE B 27 -17.829 -41.304 11.183 1.00 18.54 C
ANISOU 4312 CG2 ILE B 27 2613 2165 2263 522 -80 258 C
ATOM 4313 CD1 ILE B 27 -16.146 -41.017 13.822 1.00 19.25 C
ANISOU 4313 CD1 ILE B 27 2232 2488 2595 490 -98 534 C
ATOM 4314 C ILE B 27 -20.110 -39.809 12.274 1.00 14.70 C
ANISOU 4314 C ILE B 27 2197 1543 1845 252 -120 276 C
ATOM 4315 O ILE B 27 -21.172 -40.400 12.217 1.00 16.49 O
ANISOU 4315 O ILE B 27 2303 1696 2265 125 -401 154 O
ATOM 4316 N ALA B 28 -19.833 -38.694 11.579 1.00 14.27 N
ANISOU 4316 N ALA B 28 1881 1750 1789 109 -134 318 N
ATOM 4317 CA ALA B 28 -20.814 -38.121 10.668 1.00 15.29 C
ANISOU 4317 CA ALA B 28 2105 1944 1759 388 -86 381 C
ATOM 4318 CB ALA B 28 -20.752 -36.606 10.731 1.00 15.37 C
ANISOU 4318 CB ALA B 28 2019 1931 1887 237 -167 479 C
ATOM 4319 C ALA B 28 -20.605 -38.599 9.229 1.00 15.10 C
ANISOU 4319 C ALA B 28 2160 1709 1865 299 18 257 C
ATOM 4320 O ALA B 28 -19.493 -38.649 8.734 1.00 17.09 O
ANISOU 4320 O ALA B 28 2262 2559 1673 809 64 370 O
ATOM 4321 N SER B 29 -21.721 -38.904 8.565 1.00 15.36 N
ANISOU 4321 N SER B 29 2273 1843 1718 275 -17 318 N
ATOM 4322 CA SER B 29 -21.830 -38.767 7.104 1.00 14.77 C
ANISOU 4322 CA SER B 29 2299 1611 1703 92 -18 326 C
ATOM 4323 CB SER B 29 -22.576 -39.922 6.471 1.00 15.28 C
ANISOU 4323 CB SER B 29 2277 1720 1808 159 -170 322 C
ATOM 4324 OG SER B 29 -22.625 -39.823 5.047 1.00 15.01 O
ANISOU 4324 OG SER B 29 2193 1773 1737 -39 -106 275 O
ATOM 4325 C SER B 29 -22.448 -37.390 6.851 1.00 15.78 C
ANISOU 4325 C SER B 29 2461 1702 1831 246 -106 116 C
ATOM 4326 O SER B 29 -22.400 -36.532 7.726 1.00 17.53 O
ANISOU 4326 O SER B 29 3239 1472 1950 340 -210 187 O
ATOM 4327 N ARG B 30 -22.980 -37.148 5.665 1.00 15.16 N
ANISOU 4327 N ARG B 30 2351 1526 1881 62 -169 62 N
ATOM 4328 CA ARG B 30 -23.388 -35.803 5.324 1.00 15.36 C
ANISOU 4328 CA ARG B 30 2253 1817 1764 393 -43 302 C
ATOM 4329 CB ARG B 30 -22.179 -35.006 4.846 1.00 16.42 C
ANISOU 4329 CB ARG B 30 2205 2190 1841 331 -103 218 C
ATOM 4330 CG ARG B 30 -22.421 -33.518 4.717 1.00 17.14 C
ANISOU 4330 CG ARG B 30 2534 2199 1777 275 74 270 C
ATOM 4331 CD ARG B 30 -21.174 -32.807 4.263 1.00 19.14 C
ANISOU 4331 CD ARG B 30 2619 2368 2284 354 502 413 C
ATOM 4332 NE ARG B 30 -20.213 -32.762 5.355 1.00 27.83 N
ANISOU 4332 NE ARG B 30 3597 3076 3900 506 -181 6 N
ATOM 4333 CZ ARG B 30 -20.016 -31.721 6.154 1.00 23.39 C
ANISOU 4333 CZ ARG B 30 2878 2210 3796 264 593 -114 C
ATOM 4334 NH1 ARG B 30 -20.698 -30.606 6.011 1.00 33.22 N
ANISOU 4334 NH1 ARG B 30 4069 3742 4808 1433 -69 1639 N
ATOM 4335 NH2 ARG B 30 -19.103 -31.787 7.084 1.00 31.73 N
ANISOU 4335 NH2 ARG B 30 4171 3547 4336 201 -41 925 N
ATOM 4336 C ARG B 30 -24.455 -35.793 4.234 1.00 15.11 C
ANISOU 4336 C ARG B 30 2168 1789 1784 234 13 162 C
ATOM 4337 O ARG B 30 -24.422 -36.594 3.317 1.00 15.07 O
ANISOU 4337 O ARG B 30 2214 1681 1830 131 -22 156 O
ATOM 4338 N ILE B 31 -25.390 -34.846 4.377 1.00 14.40 N
ANISOU 4338 N ILE B 31 2129 1756 1587 247 137 299 N
ATOM 4339 CA ILE B 31 -26.232 -34.386 3.279 1.00 15.12 C
ANISOU 4339 CA ILE B 31 2163 1801 1778 141 -56 259 C
ATOM 4340 CB ILE B 31 -27.713 -34.737 3.515 1.00 17.92 C
ANISOU 4340 CB ILE B 31 2326 2178 2305 -6 15 508 C
ATOM 4341 CG1 ILE B 31 -28.258 -34.104 4.796 1.00 18.98 C
ANISOU 4341 CG1 ILE B 31 2505 2393 2311 115 -56 603 C
ATOM 4342 CG2 ILE B 31 -27.914 -36.243 3.469 1.00 20.35 C
ANISOU 4342 CG2 ILE B 31 2781 2324 2625 -315 137 599 C
ATOM 4343 CD1 ILE B 31 -29.763 -34.249 4.959 1.00 20.77 C
ANISOU 4343 CD1 ILE B 31 2680 2717 2492 -71 13 632 C
ATOM 4344 C ILE B 31 -25.993 -32.887 3.140 1.00 16.02 C
ANISOU 4344 C ILE B 31 2374 1900 1812 -9 -171 286 C
ATOM 4345 O ILE B 31 -25.559 -32.253 4.074 1.00 16.19 O
ANISOU 4345 O ILE B 31 2498 1858 1795 10 -245 201 O
ATOM 4346 N GLY B 32 -26.308 -32.324 1.970 1.00 16.25 N
ANISOU 4346 N GLY B 32 2321 1774 2076 -167 -243 402 N
ATOM 4347 CA GLY B 32 -26.040 -30.942 1.741 1.00 15.84 C
ANISOU 4347 CA GLY B 32 2459 1761 1797 -248 -295 398 C
ATOM 4348 C GLY B 32 -26.777 -30.452 0.528 1.00 16.08 C
ANISOU 4348 C GLY B 32 2462 1762 1886 -225 -402 418 C
ATOM 4349 O GLY B 32 -27.470 -31.229 -0.152 1.00 20.55 O
ANISOU 4349 O GLY B 32 3331 1855 2622 -722 -746 495 O
ATOM 4350 N ILE B 33 -26.675 -29.152 0.279 1.00 15.64 N
ANISOU 4350 N ILE B 33 2349 1753 1841 -94 -332 275 N
ATOM 4351 CA ILE B 33 -27.361 -28.549 -0.837 1.00 15.05 C
ANISOU 4351 CA ILE B 33 1942 2002 1775 -12 -280 258 C
ATOM 4352 CB ILE B 33 -27.704 -27.081 -0.531 1.00 16.07 C
ANISOU 4352 CB ILE B 33 2095 2018 1989 120 -346 267 C
ATOM 4353 CG1 ILE B 33 -28.648 -26.965 0.668 1.00 19.18 C
ANISOU 4353 CG1 ILE B 33 2681 2461 2143 379 -222 140 C
ATOM 4354 CG2 ILE B 33 -28.243 -26.404 -1.783 1.00 15.24 C
ANISOU 4354 CG2 ILE B 33 1917 1951 1921 83 -276 280 C
ATOM 4355 CD1 ILE B 33 -29.070 -25.546 0.991 1.00 20.44 C
ANISOU 4355 CD1 ILE B 33 2960 2519 2287 90 -345 -220 C
ATOM 4356 C ILE B 33 -26.462 -28.698 -2.064 1.00 14.42 C
ANISOU 4356 C ILE B 33 1795 1825 1860 -133 -227 286 C
ATOM 4357 O ILE B 33 -25.324 -28.257 -2.074 1.00 16.00 O
ANISOU 4357 O ILE B 33 1763 2098 2215 -141 -192 310 O
ATOM 4358 N PRO B 34 -26.942 -29.334 -3.143 1.00 13.09 N
ANISOU 4358 N PRO B 34 1682 1523 1768 -47 -149 304 N
ATOM 4359 CA PRO B 34 -26.066 -29.625 -4.260 1.00 13.34 C
ANISOU 4359 CA PRO B 34 1774 1640 1652 -48 -119 315 C
ATOM 4360 CB PRO B 34 -26.783 -30.722 -5.049 1.00 16.69 C
ANISOU 4360 CB PRO B 34 2209 1869 2263 -301 -83 124 C
ATOM 4361 CG PRO B 34 -28.198 -30.629 -4.641 1.00 18.72 C
ANISOU 4361 CG PRO B 34 2053 2645 2415 -295 -319 -299 C
ATOM 4362 CD PRO B 34 -28.268 -29.947 -3.289 1.00 14.24 C
ANISOU 4362 CD PRO B 34 1508 2054 1848 -13 -135 224 C
ATOM 4363 C PRO B 34 -25.789 -28.441 -5.195 1.00 12.68 C
ANISOU 4363 C PRO B 34 1607 1552 1657 9 -157 315 C
ATOM 4364 O PRO B 34 -26.518 -27.448 -5.191 1.00 12.24 O
ANISOU 4364 O PRO B 34 1509 1431 1707 -65 -182 50 O
ATOM 4365 N TYR B 35 -24.743 -28.629 -6.007 1.00 12.31 N
ANISOU 4365 N TYR B 35 1562 1358 1755 18 -120 294 N
ATOM 4366 CA TYR B 35 -24.369 -27.698 -7.063 1.00 12.64 C
ANISOU 4366 CA TYR B 35 1889 1202 1709 -9 -214 284 C
ATOM 4367 CB TYR B 35 -22.888 -27.345 -6.948 1.00 12.67 C
ANISOU 4367 CB TYR B 35 1862 1307 1644 21 -195 167 C
ATOM 4368 CG TYR B 35 -22.624 -26.243 -5.966 1.00 13.88 C
ANISOU 4368 CG TYR B 35 1625 1537 2111 -17 -399 4 C
ATOM 4369 CD1 TYR B 35 -22.716 -26.434 -4.598 1.00 15.30 C
ANISOU 4369 CD1 TYR B 35 1602 2066 2142 -299 -371 -369 C
ATOM 4370 CE1 TYR B 35 -22.500 -25.382 -3.725 1.00 17.23 C
ANISOU 4370 CE1 TYR B 35 1822 2653 2069 49 -463 -743 C
ATOM 4371 CZ TYR B 35 -22.187 -24.132 -4.224 1.00 18.41 C
ANISOU 4371 CZ TYR B 35 1938 2289 2767 79 -668 -1012 C
ATOM 4372 OH TYR B 35 -21.917 -23.047 -3.447 1.00 29.59 O
ANISOU 4372 OH TYR B 35 2861 3715 4667 443 -884 -2694 O
ATOM 4373 CE2 TYR B 35 -22.039 -23.950 -5.571 1.00 18.56 C
ANISOU 4373 CE2 TYR B 35 2350 1656 3044 84 -970 -99 C
ATOM 4374 CD2 TYR B 35 -22.299 -24.989 -6.432 1.00 16.76 C
ANISOU 4374 CD2 TYR B 35 2196 1586 2586 3 -678 93 C
ATOM 4375 C TYR B 35 -24.714 -28.247 -8.453 1.00 13.43 C
ANISOU 4375 C TYR B 35 1937 1351 1812 -282 -131 232 C
ATOM 4376 O TYR B 35 -24.409 -27.587 -9.449 1.00 14.31 O
ANISOU 4376 O TYR B 35 2230 1550 1658 -330 -320 283 O
ATOM 4377 N SER B 36 -25.324 -29.434 -8.497 1.00 11.89 N
ANISOU 4377 N SER B 36 1869 1231 1417 -259 -340 326 N
ATOM 4378 CA SER B 36 -25.970 -29.969 -9.696 1.00 14.17 C
ANISOU 4378 CA SER B 36 2286 1392 1703 -415 -353 107 C
ATOM 4379 CB SER B 36 -26.142 -31.449 -9.543 1.00 16.11 C
ANISOU 4379 CB SER B 36 2673 1422 2024 -396 -453 -200 C
ATOM 4380 OG SER B 36 -26.859 -31.754 -8.374 1.00 17.25 O
ANISOU 4380 OG SER B 36 2442 1776 2334 -330 -563 235 O
ATOM 4381 C SER B 36 -27.301 -29.239 -9.892 1.00 15.95 C
ANISOU 4381 C SER B 36 2353 1710 1997 -406 -371 81 C
ATOM 4382 O SER B 36 -27.908 -28.725 -8.944 1.00 17.31 O
ANISOU 4382 O SER B 36 2483 2001 2092 21 -141 289 O
ATOM 4383 N THR B 37 -27.817 -29.275 -11.112 1.00 16.67 N
ANISOU 4383 N THR B 37 2586 1817 1929 -214 -347 277 N
ATOM 4384 CA THR B 37 -29.010 -28.543 -11.528 1.00 16.36 C
ANISOU 4384 CA THR B 37 2411 1508 2297 -32 -84 207 C
ATOM 4385 CB THR B 37 -30.310 -29.322 -11.276 1.00 16.99 C
ANISOU 4385 CB THR B 37 2342 1781 2330 -165 -244 -184 C
ATOM 4386 OG1 THR B 37 -30.570 -29.549 -9.888 1.00 18.21 O
ANISOU 4386 OG1 THR B 37 2491 1945 2481 -84 68 141 O
ATOM 4387 CG2 THR B 37 -30.302 -30.659 -11.964 1.00 18.04 C
ANISOU 4387 CG2 THR B 37 2636 1935 2283 -344 119 -391 C
ATOM 4388 C THR B 37 -29.038 -27.124 -10.934 1.00 14.82 C
ANISOU 4388 C THR B 37 1865 1694 2069 -65 -151 19 C
ATOM 4389 O THR B 37 -30.114 -26.597 -10.557 1.00 15.90 O
ANISOU 4389 O THR B 37 2106 1715 2217 13 303 234 O
ATOM 4390 N PHE B 38 -27.894 -26.445 -10.998 1.00 13.70 N
ANISOU 4390 N PHE B 38 1842 1565 1798 -4 -421 54 N
ATOM 4391 CA PHE B 38 -27.791 -25.044 -10.667 1.00 13.81 C
ANISOU 4391 CA PHE B 38 2030 1481 1734 -115 -200 175 C
ATOM 4392 CB PHE B 38 -26.322 -24.690 -10.393 1.00 13.95 C
ANISOU 4392 CB PHE B 38 1956 1671 1670 -24 -308 230 C
ATOM 4393 CG PHE B 38 -26.021 -23.489 -9.513 1.00 12.15 C
ANISOU 4393 CG PHE B 38 1685 1483 1448 1 -116 313 C
ATOM 4394 CD1 PHE B 38 -26.699 -22.282 -9.618 1.00 13.38 C
ANISOU 4394 CD1 PHE B 38 1836 1460 1789 -77 -198 176 C
ATOM 4395 CE1 PHE B 38 -26.357 -21.206 -8.820 1.00 12.96 C
ANISOU 4395 CE1 PHE B 38 1830 1518 1572 -27 -256 200 C
ATOM 4396 CZ PHE B 38 -25.337 -21.310 -7.906 1.00 14.67 C
ANISOU 4396 CZ PHE B 38 2113 1618 1841 182 -504 170 C
ATOM 4397 CD2 PHE B 38 -24.992 -23.568 -8.592 1.00 14.01 C
ANISOU 4397 CD2 PHE B 38 2022 1537 1762 -59 -408 76 C
ATOM 4398 CE2 PHE B 38 -24.667 -22.499 -7.773 1.00 14.37 C
ANISOU 4398 CE2 PHE B 38 2001 1614 1843 90 -721 49 C
ATOM 4399 C PHE B 38 -28.358 -24.246 -11.849 1.00 13.53 C
ANISOU 4399 C PHE B 38 1982 1449 1708 -47 -195 123 C
ATOM 4400 O PHE B 38 -27.891 -24.405 -12.961 1.00 15.35 O
ANISOU 4400 O PHE B 38 2463 1714 1654 263 28 182 O
ATOM 4401 N GLN B 39 -29.386 -23.437 -11.626 1.00 11.72 N
ANISOU 4401 N GLN B 39 1874 1156 1420 -199 -195 80 N
ATOM 4402 CA GLN B 39 -30.109 -22.779 -12.726 1.00 12.96 C
ANISOU 4402 CA GLN B 39 1938 1366 1620 -111 -193 278 C
ATOM 4403 CB GLN B 39 -31.561 -22.498 -12.333 1.00 13.51 C
ANISOU 4403 CB GLN B 39 1740 1549 1843 -267 -355 359 C
ATOM 4404 CG GLN B 39 -32.333 -23.735 -11.924 1.00 13.83 C
ANISOU 4404 CG GLN B 39 1951 1544 1759 -426 -534 328 C
ATOM 4405 CD GLN B 39 -32.378 -24.788 -13.006 1.00 16.56 C
ANISOU 4405 CD GLN B 39 2331 1786 2172 -388 -735 116 C
ATOM 4406 OE1 GLN B 39 -32.878 -24.525 -14.091 1.00 23.66 O
ANISOU 4406 OE1 GLN B 39 3542 3007 2438 -699 -1299 99 O
ATOM 4407 NE2 GLN B 39 -31.820 -25.963 -12.717 1.00 21.57 N
ANISOU 4407 NE2 GLN B 39 3075 2043 3076 -264 -383 292 N
ATOM 4408 C GLN B 39 -29.442 -21.461 -13.108 1.00 11.38 C
ANISOU 4408 C GLN B 39 1769 1286 1266 -81 -278 108 C
ATOM 4409 O GLN B 39 -29.098 -20.650 -12.242 1.00 11.96 O
ANISOU 4409 O GLN B 39 1964 1268 1310 -163 -213 57 O
ATOM 4410 N THR B 40 -29.214 -21.292 -14.415 1.00 12.12 N
ANISOU 4410 N THR B 40 2023 1294 1287 -124 -177 108 N
ATOM 4411 CA THR B 40 -28.890 -20.022 -15.020 1.00 12.39 C
ANISOU 4411 CA THR B 40 2180 1440 1087 27 -207 282 C
ATOM 4412 CB THR B 40 -27.595 -20.090 -15.843 1.00 13.26 C
ANISOU 4412 CB THR B 40 2090 1584 1363 5 -282 392 C
ATOM 4413 OG1 THR B 40 -26.477 -20.360 -14.990 1.00 15.26 O
ANISOU 4413 OG1 THR B 40 1869 2247 1682 268 -243 157 O
ATOM 4414 CG2 THR B 40 -27.339 -18.797 -16.590 1.00 14.38 C
ANISOU 4414 CG2 THR B 40 2209 1602 1651 71 -112 481 C
ATOM 4415 C THR B 40 -30.115 -19.615 -15.842 1.00 13.25 C
ANISOU 4415 C THR B 40 2027 1564 1441 -5 -199 263 C
ATOM 4416 O THR B 40 -30.432 -20.251 -16.855 1.00 15.66 O
ANISOU 4416 O THR B 40 2538 1745 1664 97 -428 -14 O
ATOM 4417 N ILE B 41 -30.831 -18.603 -15.362 1.00 12.10 N
ANISOU 4417 N ILE B 41 1808 1252 1535 -160 -268 250 N
ATOM 4418 CA ILE B 41 -32.137 -18.224 -15.899 1.00 12.36 C
ANISOU 4418 CA ILE B 41 1775 1384 1536 -247 -392 167 C
ATOM 4419 CB ILE B 41 -33.136 -18.037 -14.749 1.00 12.57 C
ANISOU 4419 CB ILE B 41 1744 1451 1581 -354 -390 124 C
ATOM 4420 CG1 ILE B 41 -33.229 -19.306 -13.906 1.00 13.82 C
ANISOU 4420 CG1 ILE B 41 1882 1558 1808 -565 -364 146 C
ATOM 4421 CG2 ILE B 41 -34.490 -17.625 -15.292 1.00 12.86 C
ANISOU 4421 CG2 ILE B 41 1703 1387 1794 -317 -194 266 C
ATOM 4422 CD1 ILE B 41 -33.977 -19.120 -12.618 1.00 13.90 C
ANISOU 4422 CD1 ILE B 41 1781 1696 1803 -488 -368 186 C
ATOM 4423 C ILE B 41 -31.974 -16.948 -16.722 1.00 12.02 C
ANISOU 4423 C ILE B 41 1714 1327 1526 -34 -406 165 C
ATOM 4424 O ILE B 41 -31.485 -15.915 -16.229 1.00 13.57 O
ANISOU 4424 O ILE B 41 2102 1403 1648 -318 -688 391 O
ATOM 4425 N GLN B 42 -32.369 -17.044 -17.985 1.00 12.63 N
ANISOU 4425 N GLN B 42 1887 1430 1482 134 -399 192 N
ATOM 4426 CA AGLN B 42 -32.340 -15.921 -18.909 0.50 13.98 C
ANISOU 4426 CA AGLN B 42 2061 1475 1773 81 -347 293 C
ATOM 4427 CA BGLN B 42 -32.352 -15.942 -18.931 0.50 14.06 C
ANISOU 4427 CA BGLN B 42 2138 1500 1702 147 -360 303 C
ATOM 4428 CB AGLN B 42 -32.243 -16.405 -20.356 0.50 16.16 C
ANISOU 4428 CB AGLN B 42 2377 1879 1883 229 -232 156 C
ATOM 4429 CB BGLN B 42 -32.362 -16.461 -20.375 0.50 16.00 C
ANISOU 4429 CB BGLN B 42 2517 1862 1697 368 -293 278 C
ATOM 4430 CG AGLN B 42 -30.872 -16.996 -20.653 0.50 18.22 C
ANISOU 4430 CG AGLN B 42 2321 2372 2227 257 -190 15 C
ATOM 4431 CG BGLN B 42 -31.298 -17.517 -20.697 0.50 17.84 C
ANISOU 4431 CG BGLN B 42 2754 2239 1785 624 -255 197 C
ATOM 4432 CD AGLN B 42 -30.723 -17.572 -22.037 0.50 22.36 C
ANISOU 4432 CD AGLN B 42 2857 3069 2567 304 -56 -399 C
ATOM 4433 CD BGLN B 42 -29.910 -16.928 -20.775 0.50 20.76 C
ANISOU 4433 CD BGLN B 42 3042 2782 2063 390 -346 317 C
ATOM 4434 OE1AGLN B 42 -31.691 -17.929 -22.692 0.50 25.13 O
ANISOU 4434 OE1AGLN B 42 3087 3918 2542 591 -372 -469 O
ATOM 4435 OE1BGLN B 42 -29.742 -15.820 -21.282 0.50 24.21 O
ANISOU 4435 OE1BGLN B 42 3867 2911 2420 409 -259 391 O
ATOM 4436 NE2AGLN B 42 -29.483 -17.683 -22.476 0.50 24.80 N
ANISOU 4436 NE2AGLN B 42 3086 3199 3137 44 364 -290 N
ATOM 4437 NE2BGLN B 42 -28.917 -17.646 -20.240 0.50 23.91 N
ANISOU 4437 NE2BGLN B 42 4194 3064 1825 1042 -568 278 N
ATOM 4438 C GLN B 42 -33.603 -15.099 -18.709 1.00 13.43 C
ANISOU 4438 C GLN B 42 2015 1417 1670 53 -341 266 C
ATOM 4439 O GLN B 42 -34.658 -15.629 -18.329 1.00 13.97 O
ANISOU 4439 O GLN B 42 1967 1704 1634 -72 -419 71 O
ATOM 4440 N PRO B 43 -33.547 -13.782 -18.984 1.00 12.19 N
ANISOU 4440 N PRO B 43 1681 1341 1606 -7 -298 228 N
ATOM 4441 CA PRO B 43 -34.752 -12.968 -18.935 1.00 12.08 C
ANISOU 4441 CA PRO B 43 1611 1427 1551 -20 -456 310 C
ATOM 4442 CB PRO B 43 -34.233 -11.539 -19.081 1.00 14.74 C
ANISOU 4442 CB PRO B 43 2192 1356 2051 -26 -374 160 C
ATOM 4443 CG PRO B 43 -32.893 -11.660 -19.691 1.00 17.83 C
ANISOU 4443 CG PRO B 43 2371 1782 2619 -93 -165 551 C
ATOM 4444 CD PRO B 43 -32.357 -13.032 -19.395 1.00 15.24 C
ANISOU 4444 CD PRO B 43 1946 1698 2144 -129 -367 367 C
ATOM 4445 C PRO B 43 -35.727 -13.334 -20.062 1.00 12.08 C
ANISOU 4445 C PRO B 43 1801 1352 1437 -217 -414 292 C
ATOM 4446 O PRO B 43 -35.352 -14.004 -21.033 1.00 13.98 O
ANISOU 4446 O PRO B 43 1767 1872 1670 36 -372 69 O
ATOM 4447 N VAL B 44 -36.976 -12.910 -19.905 1.00 12.50 N
ANISOU 4447 N VAL B 44 1857 1470 1419 -195 -655 209 N
ATOM 4448 CA VAL B 44 -38.040 -13.269 -20.869 1.00 12.18 C
ANISOU 4448 CA VAL B 44 1656 1498 1474 -124 -620 233 C
ATOM 4449 CB VAL B 44 -39.428 -12.897 -20.325 1.00 14.12 C
ANISOU 4449 CB VAL B 44 1936 1764 1664 -147 -399 380 C
ATOM 4450 CG1 VAL B 44 -39.710 -13.615 -19.008 1.00 14.31 C
ANISOU 4450 CG1 VAL B 44 1864 1850 1719 -390 -220 351 C
ATOM 4451 CG2 VAL B 44 -39.621 -11.397 -20.213 1.00 14.73 C
ANISOU 4451 CG2 VAL B 44 1974 1856 1767 134 -517 217 C
ATOM 4452 C VAL B 44 -37.813 -12.635 -22.250 1.00 13.19 C
ANISOU 4452 C VAL B 44 1861 1533 1616 -212 -560 308 C
ATOM 4453 O VAL B 44 -38.397 -13.063 -23.242 1.00 14.35 O
ANISOU 4453 O VAL B 44 2172 1672 1606 -310 -596 255 O
ATOM 4454 N SER B 45 -37.031 -11.571 -22.305 1.00 12.72 N
ANISOU 4454 N SER B 45 1934 1564 1333 -284 -787 330 N
ATOM 4455 CA SER B 45 -36.789 -10.807 -23.500 1.00 13.71 C
ANISOU 4455 CA SER B 45 2196 1509 1503 -289 -512 348 C
ATOM 4456 CB SER B 45 -37.817 -9.714 -23.656 1.00 14.37 C
ANISOU 4456 CB SER B 45 2381 1416 1664 -258 -561 442 C
ATOM 4457 OG SER B 45 -37.812 -8.874 -22.499 1.00 15.33 O
ANISOU 4457 OG SER B 45 2535 1534 1753 -156 -578 263 O
ATOM 4458 C SER B 45 -35.374 -10.250 -23.417 1.00 13.25 C
ANISOU 4458 C SER B 45 2116 1541 1376 -212 -460 345 C
ATOM 4459 O SER B 45 -34.770 -10.203 -22.336 1.00 14.39 O
ANISOU 4459 O SER B 45 2067 1913 1487 -362 -580 465 O
ATOM 4460 N ASP B 46 -34.839 -9.836 -24.571 1.00 13.89 N
ANISOU 4460 N ASP B 46 2174 1731 1371 -123 -355 372 N
ATOM 4461 CA AASP B 46 -33.457 -9.427 -24.655 0.70 14.99 C
ANISOU 4461 CA AASP B 46 2148 1676 1867 -59 -411 133 C
ATOM 4462 CA BASP B 46 -33.459 -9.396 -24.692 0.30 14.16 C
ANISOU 4462 CA BASP B 46 2036 1688 1656 31 -357 222 C
ATOM 4463 CB AASP B 46 -33.060 -9.092 -26.096 0.70 17.07 C
ANISOU 4463 CB AASP B 46 2654 1795 2036 18 -370 439 C
ATOM 4464 CB BASP B 46 -33.133 -8.961 -26.126 0.30 14.69 C
ANISOU 4464 CB BASP B 46 2033 1790 1758 197 -305 399 C
ATOM 4465 CG AASP B 46 -32.965 -10.300 -27.025 0.70 21.14 C
ANISOU 4465 CG AASP B 46 3239 2249 2542 -34 -331 3 C
ATOM 4466 CG BASP B 46 -31.660 -8.688 -26.403 0.30 15.12 C
ANISOU 4466 CG BASP B 46 2041 1916 1788 325 -199 385 C
ATOM 4467 OD1AASP B 46 -32.860 -11.434 -26.509 0.70 26.31 O
ANISOU 4467 OD1AASP B 46 4462 2519 3015 84 71 218 O
ATOM 4468 OD1BASP B 46 -30.828 -9.348 -25.774 0.30 15.72 O
ANISOU 4468 OD1BASP B 46 1741 2117 2115 326 -237 358 O
ATOM 4469 OD2AASP B 46 -32.967 -10.096 -28.255 0.70 26.49 O
ANISOU 4469 OD2AASP B 46 3841 3295 2927 226 -609 771 O
ATOM 4470 OD2BASP B 46 -31.359 -7.809 -27.261 0.30 17.27 O
ANISOU 4470 OD2BASP B 46 2077 2429 2053 758 -169 936 O
ATOM 4471 C ASP B 46 -33.215 -8.241 -23.719 1.00 13.86 C
ANISOU 4471 C ASP B 46 1878 1785 1603 -27 -228 166 C
ATOM 4472 O ASP B 46 -33.933 -7.243 -23.734 1.00 16.25 O
ANISOU 4472 O ASP B 46 2350 1719 2105 96 -320 187 O
ATOM 4473 N ALA B 47 -32.158 -8.362 -22.926 1.00 14.20 N
ANISOU 4473 N ALA B 47 2146 1507 1740 -142 -539 156 N
ATOM 4474 CA ALA B 47 -31.768 -7.308 -21.991 1.00 15.38 C
ANISOU 4474 CA ALA B 47 2311 1589 1943 -265 -477 133 C
ATOM 4475 CB ALA B 47 -30.583 -7.749 -21.171 1.00 16.78 C
ANISOU 4475 CB ALA B 47 2485 2167 1721 -509 -639 470 C
ATOM 4476 C ALA B 47 -31.417 -6.042 -22.766 1.00 14.78 C
ANISOU 4476 C ALA B 47 2202 1548 1865 -164 -502 176 C
ATOM 4477 O ALA B 47 -30.837 -6.094 -23.845 1.00 14.92 O
ANISOU 4477 O ALA B 47 2088 1621 1958 -143 -497 158 O
ATOM 4478 N PRO B 48 -31.667 -4.857 -22.174 1.00 16.67 N
ANISOU 4478 N PRO B 48 2300 1565 2466 -259 -252 153 N
ATOM 4479 CA PRO B 48 -31.286 -3.601 -22.809 1.00 15.75 C
ANISOU 4479 CA PRO B 48 2183 1405 2394 2 -616 177 C
ATOM 4480 CB PRO B 48 -31.830 -2.545 -21.844 1.00 18.03 C
ANISOU 4480 CB PRO B 48 2425 1508 2917 430 -636 66 C
ATOM 4481 CG PRO B 48 -32.006 -3.256 -20.540 1.00 24.09 C
ANISOU 4481 CG PRO B 48 3712 2060 3380 -57 51 -49 C
ATOM 4482 CD PRO B 48 -32.310 -4.682 -20.865 1.00 19.19 C
ANISOU 4482 CD PRO B 48 2787 1944 2558 -88 -222 -6 C
ATOM 4483 C PRO B 48 -29.761 -3.523 -22.927 1.00 14.80 C
ANISOU 4483 C PRO B 48 2219 1531 1871 -44 -570 209 C
ATOM 4484 O PRO B 48 -29.059 -3.767 -21.968 1.00 15.26 O
ANISOU 4484 O PRO B 48 2261 1698 1837 29 -560 352 O
ATOM 4485 N ASN B 49 -29.281 -3.135 -24.113 1.00 14.70 N
ANISOU 4485 N ASN B 49 2109 1702 1770 -65 -646 365 N
ATOM 4486 CA ASN B 49 -27.863 -3.150 -24.441 1.00 15.80 C
ANISOU 4486 CA ASN B 49 2288 1983 1730 -168 -559 240 C
ATOM 4487 CB ASN B 49 -27.636 -2.710 -25.885 1.00 19.85 C
ANISOU 4487 CB ASN B 49 2860 3149 1530 -323 -544 130 C
ATOM 4488 CG ASN B 49 -26.195 -2.816 -26.332 1.00 22.01 C
ANISOU 4488 CG ASN B 49 3190 3321 1848 157 -785 303 C
ATOM 4489 OD1 ASN B 49 -25.613 -3.884 -26.270 1.00 29.55 O
ANISOU 4489 OD1 ASN B 49 3761 4221 3244 1219 -1503 -389 O
ATOM 4490 ND2 ASN B 49 -25.613 -1.714 -26.803 1.00 28.01 N
ANISOU 4490 ND2 ASN B 49 4505 3783 2353 -411 -315 329 N
ATOM 4491 C ASN B 49 -27.051 -2.244 -23.497 1.00 13.35 C
ANISOU 4491 C ASN B 49 1891 1814 1368 9 -647 541 C
ATOM 4492 O ASN B 49 -25.889 -2.532 -23.229 1.00 12.52 O
ANISOU 4492 O ASN B 49 1938 1363 1454 -111 -565 517 O
ATOM 4493 N ASN B 50 -27.660 -1.182 -22.977 1.00 14.04 N
ANISOU 4493 N ASN B 50 2009 1798 1527 -135 -525 393 N
ATOM 4494 CA ASN B 50 -26.992 -0.242 -22.100 1.00 13.40 C
ANISOU 4494 CA ASN B 50 2060 1590 1441 -41 -445 413 C
ATOM 4495 CB ASN B 50 -27.157 1.205 -22.563 1.00 14.15 C
ANISOU 4495 CB ASN B 50 2080 1541 1752 -167 -254 484 C
ATOM 4496 CG ASN B 50 -28.563 1.708 -22.358 1.00 15.34 C
ANISOU 4496 CG ASN B 50 2276 1544 2008 156 -471 521 C
ATOM 4497 OD1 ASN B 50 -29.471 0.904 -22.077 1.00 15.57 O
ANISOU 4497 OD1 ASN B 50 2162 1825 1928 125 -198 535 O
ATOM 4498 ND2 ASN B 50 -28.731 3.023 -22.514 1.00 17.09 N
ANISOU 4498 ND2 ASN B 50 2866 1469 2158 -71 -737 411 N
ATOM 4499 C ASN B 50 -27.469 -0.369 -20.651 1.00 13.31 C
ANISOU 4499 C ASN B 50 1781 1737 1538 -56 -373 290 C
ATOM 4500 O ASN B 50 -27.179 0.503 -19.824 1.00 13.72 O
ANISOU 4500 O ASN B 50 2117 1623 1472 -12 -375 210 O
ATOM 4501 N GLY B 51 -28.152 -1.457 -20.316 1.00 12.58 N
ANISOU 4501 N GLY B 51 1741 1622 1415 157 -344 327 N
ATOM 4502 CA GLY B 51 -28.551 -1.714 -18.928 1.00 13.51 C
ANISOU 4502 CA GLY B 51 1884 1799 1450 163 -342 405 C
ATOM 4503 C GLY B 51 -29.761 -0.933 -18.410 1.00 11.98 C
ANISOU 4503 C GLY B 51 1777 1461 1312 62 -394 387 C
ATOM 4504 O GLY B 51 -30.076 -1.060 -17.221 1.00 12.04 O
ANISOU 4504 O GLY B 51 1619 1501 1452 -18 -209 398 O
ATOM 4505 N ILE B 52 -30.461 -0.176 -19.271 1.00 12.60 N
ANISOU 4505 N ILE B 52 1753 1639 1394 121 -424 375 N
ATOM 4506 CA ILE B 52 -31.581 0.654 -18.817 1.00 12.59 C
ANISOU 4506 CA ILE B 52 1646 1489 1646 54 -444 231 C
ATOM 4507 CB ILE B 52 -31.430 2.108 -19.282 1.00 14.20 C
ANISOU 4507 CB ILE B 52 1997 1687 1710 4 -193 442 C
ATOM 4508 CG1 ILE B 52 -30.073 2.689 -18.922 1.00 16.32 C
ANISOU 4508 CG1 ILE B 52 2008 1944 2248 136 -275 302 C
ATOM 4509 CG2 ILE B 52 -32.563 2.947 -18.716 1.00 15.23 C
ANISOU 4509 CG2 ILE B 52 2264 1441 2081 103 -186 417 C
ATOM 4510 CD1 ILE B 52 -29.776 2.690 -17.484 1.00 16.95 C
ANISOU 4510 CD1 ILE B 52 2590 1749 2100 -102 -187 467 C
ATOM 4511 C ILE B 52 -32.918 0.102 -19.319 1.00 13.24 C
ANISOU 4511 C ILE B 52 1790 1447 1792 -63 -451 252 C
ATOM 4512 O ILE B 52 -33.148 0.080 -20.523 1.00 14.14 O
ANISOU 4512 O ILE B 52 1777 1746 1847 -35 -485 246 O
ATOM 4513 N GLY B 53 -33.784 -0.305 -18.384 1.00 12.55 N
ANISOU 4513 N GLY B 53 1812 1362 1594 87 -475 222 N
ATOM 4514 CA GLY B 53 -35.115 -0.746 -18.715 1.00 12.90 C
ANISOU 4514 CA GLY B 53 1885 1453 1561 56 -433 93 C
ATOM 4515 C GLY B 53 -35.614 -1.847 -17.815 1.00 12.14 C
ANISOU 4515 C GLY B 53 1724 1555 1331 119 -552 133 C
ATOM 4516 O GLY B 53 -34.852 -2.461 -17.072 1.00 13.12 O
ANISOU 4516 O GLY B 53 1706 1663 1615 140 -602 324 O
ATOM 4517 N GLN B 54 -36.917 -2.125 -17.887 1.00 11.76 N
ANISOU 4517 N GLN B 54 1655 1316 1495 166 -473 242 N
ATOM 4518 CA GLN B 54 -37.476 -3.271 -17.168 1.00 12.08 C
ANISOU 4518 CA GLN B 54 1644 1404 1541 64 -415 263 C
ATOM 4519 CB GLN B 54 -38.998 -3.298 -17.323 1.00 11.70 C
ANISOU 4519 CB GLN B 54 1633 1382 1428 96 -413 333 C
ATOM 4520 CG GLN B 54 -39.678 -4.217 -16.339 1.00 12.78 C
ANISOU 4520 CG GLN B 54 1767 1778 1309 95 -249 388 C
ATOM 4521 CD GLN B 54 -41.183 -4.162 -16.429 1.00 13.83 C
ANISOU 4521 CD GLN B 54 1737 1909 1607 228 -87 208 C
ATOM 4522 OE1 GLN B 54 -41.787 -4.729 -17.332 1.00 17.76 O
ANISOU 4522 OE1 GLN B 54 2101 2277 2368 249 -434 -192 O
ATOM 4523 NE2 GLN B 54 -41.812 -3.463 -15.497 1.00 17.10 N
ANISOU 4523 NE2 GLN B 54 2143 2143 2211 504 -40 -204 N
ATOM 4524 C GLN B 54 -36.848 -4.573 -17.666 1.00 12.30 C
ANISOU 4524 C GLN B 54 1750 1482 1439 168 -402 333 C
ATOM 4525 O GLN B 54 -36.616 -4.762 -18.864 1.00 13.21 O
ANISOU 4525 O GLN B 54 1986 1668 1365 -39 -504 317 O
ATOM 4526 N ILE B 55 -36.570 -5.466 -16.707 1.00 11.46 N
ANISOU 4526 N ILE B 55 1757 1409 1188 50 -464 204 N
ATOM 4527 CA ILE B 55 -36.004 -6.794 -16.965 1.00 12.38 C
ANISOU 4527 CA ILE B 55 1821 1357 1525 8 -328 194 C
ATOM 4528 CB ILE B 55 -34.529 -6.868 -16.542 1.00 11.87 C
ANISOU 4528 CB ILE B 55 1747 1146 1615 -21 -310 77 C
ATOM 4529 CG1 ILE B 55 -33.651 -5.868 -17.306 1.00 12.21 C
ANISOU 4529 CG1 ILE B 55 1814 1191 1631 17 -235 69 C
ATOM 4530 CG2 ILE B 55 -33.999 -8.292 -16.630 1.00 12.70 C
ANISOU 4530 CG2 ILE B 55 2004 1064 1755 -104 -219 121 C
ATOM 4531 CD1 ILE B 55 -32.362 -5.495 -16.588 1.00 13.27 C
ANISOU 4531 CD1 ILE B 55 1919 1255 1867 79 -470 198 C
ATOM 4532 C ILE B 55 -36.838 -7.789 -16.150 1.00 11.28 C
ANISOU 4532 C ILE B 55 1604 1323 1356 -39 -423 128 C
ATOM 4533 O ILE B 55 -37.015 -7.571 -14.975 1.00 12.58 O
ANISOU 4533 O ILE B 55 1882 1569 1329 -16 -294 213 O
ATOM 4534 N THR B 56 -37.309 -8.865 -16.785 1.00 10.79 N
ANISOU 4534 N THR B 56 1512 1333 1255 -111 -336 100 N
ATOM 4535 CA THR B 56 -38.164 -9.840 -16.115 1.00 11.22 C
ANISOU 4535 CA THR B 56 1563 1185 1515 -49 -296 229 C
ATOM 4536 CB THR B 56 -39.603 -9.814 -16.647 1.00 12.79 C
ANISOU 4536 CB THR B 56 1571 1462 1827 -50 -291 208 C
ATOM 4537 OG1 THR B 56 -40.170 -8.525 -16.444 1.00 13.42 O
ANISOU 4537 OG1 THR B 56 1491 1717 1890 195 -299 157 O
ATOM 4538 CG2 THR B 56 -40.480 -10.862 -16.002 1.00 13.92 C
ANISOU 4538 CG2 THR B 56 1548 1496 2243 -62 -200 164 C
ATOM 4539 C THR B 56 -37.614 -11.262 -16.268 1.00 11.51 C
ANISOU 4539 C THR B 56 1682 1253 1437 -21 -334 207 C
ATOM 4540 O THR B 56 -37.257 -11.694 -17.374 1.00 12.79 O
ANISOU 4540 O THR B 56 1963 1386 1510 -75 -283 160 O
ATOM 4541 N PHE B 57 -37.560 -11.964 -15.135 1.00 11.20 N
ANISOU 4541 N PHE B 57 1670 1162 1421 -89 -362 182 N
ATOM 4542 CA PHE B 57 -37.323 -13.401 -15.111 1.00 11.55 C
ANISOU 4542 CA PHE B 57 1737 1175 1474 -71 -269 248 C
ATOM 4543 CB PHE B 57 -36.222 -13.763 -14.102 1.00 12.06 C
ANISOU 4543 CB PHE B 57 1845 1274 1463 -179 -380 281 C
ATOM 4544 CG PHE B 57 -34.911 -13.074 -14.365 1.00 11.77 C
ANISOU 4544 CG PHE B 57 1620 1486 1363 -95 -380 196 C
ATOM 4545 CD1 PHE B 57 -34.010 -13.593 -15.281 1.00 12.61 C
ANISOU 4545 CD1 PHE B 57 1779 1658 1351 8 -426 288 C
ATOM 4546 CE1 PHE B 57 -32.843 -12.918 -15.566 1.00 12.80 C
ANISOU 4546 CE1 PHE B 57 1721 1682 1459 -19 -428 334 C
ATOM 4547 CZ PHE B 57 -32.543 -11.732 -14.934 1.00 13.08 C
ANISOU 4547 CZ PHE B 57 1762 1517 1688 -212 -349 394 C
ATOM 4548 CD2 PHE B 57 -34.619 -11.858 -13.758 1.00 12.45 C
ANISOU 4548 CD2 PHE B 57 1650 1494 1585 -221 -210 171 C
ATOM 4549 CE2 PHE B 57 -33.433 -11.191 -14.036 1.00 13.73 C
ANISOU 4549 CE2 PHE B 57 1831 1692 1691 -442 -335 214 C
ATOM 4550 C PHE B 57 -38.637 -14.086 -14.753 1.00 12.23 C
ANISOU 4550 C PHE B 57 1730 1389 1526 -115 -326 223 C
ATOM 4551 O PHE B 57 -39.325 -13.654 -13.818 1.00 13.52 O
ANISOU 4551 O PHE B 57 2032 1294 1809 -137 -74 95 O
ATOM 4552 N ASN B 58 -38.979 -15.138 -15.505 1.00 12.28 N
ANISOU 4552 N ASN B 58 1599 1382 1683 -163 -269 190 N
ATOM 4553 CA ASN B 58 -40.207 -15.874 -15.296 1.00 13.11 C
ANISOU 4553 CA ASN B 58 1644 1509 1827 -265 -290 259 C
ATOM 4554 CB ASN B 58 -41.297 -15.426 -16.272 1.00 13.77 C
ANISOU 4554 CB ASN B 58 1605 1608 2019 -254 -339 254 C
ATOM 4555 CG ASN B 58 -42.592 -16.196 -16.161 1.00 14.93 C
ANISOU 4555 CG ASN B 58 1440 2012 2218 -288 -552 534 C
ATOM 4556 OD1 ASN B 58 -42.660 -17.226 -15.492 1.00 17.02 O
ANISOU 4556 OD1 ASN B 58 2112 2221 2130 -749 -539 546 O
ATOM 4557 ND2 ASN B 58 -43.597 -15.759 -16.910 1.00 21.50 N
ANISOU 4557 ND2 ASN B 58 1915 2688 3565 -119 -1203 733 N
ATOM 4558 C ASN B 58 -39.875 -17.352 -15.420 1.00 12.97 C
ANISOU 4558 C ASN B 58 1816 1452 1657 -322 -293 237 C
ATOM 4559 O ASN B 58 -39.688 -17.841 -16.535 1.00 14.88 O
ANISOU 4559 O ASN B 58 2288 1598 1765 -398 -174 141 O
ATOM 4560 N GLN B 59 -39.733 -18.037 -14.274 1.00 12.12 N
ANISOU 4560 N GLN B 59 1893 1208 1504 -326 -302 39 N
ATOM 4561 CA GLN B 59 -39.246 -19.414 -14.327 1.00 12.13 C
ANISOU 4561 CA GLN B 59 1798 1317 1491 -251 -198 144 C
ATOM 4562 CB GLN B 59 -37.724 -19.427 -14.364 1.00 13.75 C
ANISOU 4562 CB GLN B 59 1824 1596 1801 -340 -196 138 C
ATOM 4563 CG GLN B 59 -37.174 -20.843 -14.477 1.00 14.42 C
ANISOU 4563 CG GLN B 59 1929 1577 1972 -231 -110 183 C
ATOM 4564 CD GLN B 59 -37.712 -21.535 -15.707 1.00 14.39 C
ANISOU 4564 CD GLN B 59 2380 1388 1697 -270 143 177 C
ATOM 4565 OE1 GLN B 59 -37.372 -21.158 -16.820 1.00 18.52 O
ANISOU 4565 OE1 GLN B 59 3053 2069 1913 -449 406 350 O
ATOM 4566 NE2 GLN B 59 -38.578 -22.523 -15.520 1.00 15.36 N
ANISOU 4566 NE2 GLN B 59 2667 1266 1900 -415 -45 254 N
ATOM 4567 C GLN B 59 -39.752 -20.197 -13.119 1.00 12.83 C
ANISOU 4567 C GLN B 59 1836 1511 1527 -318 -264 214 C
ATOM 4568 O GLN B 59 -39.134 -20.216 -12.040 1.00 12.61 O
ANISOU 4568 O GLN B 59 1739 1444 1605 -197 -318 41 O
ATOM 4569 N PRO B 60 -40.876 -20.907 -13.269 1.00 12.26 N
ANISOU 4569 N PRO B 60 1654 1557 1446 -242 -321 142 N
ATOM 4570 CA PRO B 60 -41.296 -21.860 -12.244 1.00 12.52 C
ANISOU 4570 CA PRO B 60 1788 1527 1439 -243 -400 122 C
ATOM 4571 CB PRO B 60 -42.494 -22.558 -12.883 1.00 13.57 C
ANISOU 4571 CB PRO B 60 1776 1550 1827 -399 -432 200 C
ATOM 4572 CG PRO B 60 -43.028 -21.530 -13.861 1.00 13.94 C
ANISOU 4572 CG PRO B 60 1755 1825 1716 -395 -552 197 C
ATOM 4573 CD PRO B 60 -41.783 -20.904 -14.427 1.00 13.86 C
ANISOU 4573 CD PRO B 60 1741 1940 1583 -289 -442 249 C
ATOM 4574 C PRO B 60 -40.174 -22.853 -11.943 1.00 12.23 C
ANISOU 4574 C PRO B 60 1680 1493 1472 -299 -490 -26 C
ATOM 4575 O PRO B 60 -39.500 -23.298 -12.860 1.00 12.89 O
ANISOU 4575 O PRO B 60 1829 1606 1462 -145 -161 229 O
ATOM 4576 N LEU B 61 -40.032 -23.208 -10.666 1.00 12.48 N
ANISOU 4576 N LEU B 61 1829 1466 1447 -227 -245 5 N
ATOM 4577 CA LEU B 61 -38.988 -24.145 -10.225 1.00 12.67 C
ANISOU 4577 CA LEU B 61 1780 1411 1622 -258 -244 2 C
ATOM 4578 CB LEU B 61 -37.830 -23.398 -9.576 1.00 13.44 C
ANISOU 4578 CB LEU B 61 1709 1685 1709 -289 -314 182 C
ATOM 4579 CG LEU B 61 -36.963 -22.553 -10.507 1.00 14.26 C
ANISOU 4579 CG LEU B 61 1797 1868 1750 -266 -170 217 C
ATOM 4580 CD1 LEU B 61 -35.955 -21.747 -9.710 1.00 14.51 C
ANISOU 4580 CD1 LEU B 61 1657 1933 1923 -391 -229 446 C
ATOM 4581 CD2 LEU B 61 -36.273 -23.401 -11.553 1.00 14.88 C
ANISOU 4581 CD2 LEU B 61 1581 2320 1751 -184 -180 201 C
ATOM 4582 C LEU B 61 -39.613 -25.126 -9.240 1.00 12.86 C
ANISOU 4582 C LEU B 61 1677 1585 1621 -221 -328 180 C
ATOM 4583 O LEU B 61 -40.212 -24.719 -8.240 1.00 14.68 O
ANISOU 4583 O LEU B 61 2108 1729 1741 -181 -64 312 O
ATOM 4584 N GLY B 62 -39.473 -26.427 -9.533 1.00 13.83 N
ANISOU 4584 N GLY B 62 2002 1637 1616 -391 -484 109 N
ATOM 4585 CA GLY B 62 -40.044 -27.442 -8.648 1.00 15.22 C
ANISOU 4585 CA GLY B 62 2048 1769 1964 -467 -610 291 C
ATOM 4586 C GLY B 62 -39.181 -27.660 -7.423 1.00 13.79 C
ANISOU 4586 C GLY B 62 2150 1388 1699 -732 -525 176 C
ATOM 4587 O GLY B 62 -38.022 -27.221 -7.366 1.00 13.84 O
ANISOU 4587 O GLY B 62 1920 1616 1722 -602 -601 222 O
ATOM 4588 N ASN B 63 -39.748 -28.333 -6.426 1.00 12.59 N
ANISOU 4588 N ASN B 63 1808 1372 1602 -382 -412 206 N
ATOM 4589 CA ASN B 63 -38.966 -28.796 -5.280 1.00 12.45 C
ANISOU 4589 CA ASN B 63 1851 1277 1599 -275 -414 178 C
ATOM 4590 CB ASN B 63 -38.092 -29.977 -5.702 1.00 13.10 C
ANISOU 4590 CB ASN B 63 1936 1291 1750 -414 -363 -27 C
ATOM 4591 CG ASN B 63 -38.960 -31.150 -6.102 1.00 14.41 C
ANISOU 4591 CG ASN B 63 2105 1527 1842 -691 -297 31 C
ATOM 4592 OD1 ASN B 63 -39.481 -31.869 -5.241 1.00 14.36 O
ANISOU 4592 OD1 ASN B 63 2014 1526 1913 -449 -244 169 O
ATOM 4593 ND2 ASN B 63 -39.149 -31.339 -7.399 1.00 16.25 N
ANISOU 4593 ND2 ASN B 63 2469 1782 1920 -488 -473 -96 N
ATOM 4594 C ASN B 63 -38.284 -27.590 -4.611 1.00 11.75 C
ANISOU 4594 C ASN B 63 1629 1352 1480 -236 -413 235 C
ATOM 4595 O ASN B 63 -38.976 -26.620 -4.337 1.00 12.45 O
ANISOU 4595 O ASN B 63 1694 1371 1664 -192 -311 97 O
ATOM 4596 N LEU B 64 -36.996 -27.694 -4.254 1.00 10.70 N
ANISOU 4596 N LEU B 64 1519 1062 1482 -161 -256 210 N
ATOM 4597 CA LEU B 64 -36.363 -26.661 -3.451 1.00 11.70 C
ANISOU 4597 CA LEU B 64 1721 1205 1518 -324 -116 76 C
ATOM 4598 CB LEU B 64 -35.499 -27.291 -2.366 1.00 11.45 C
ANISOU 4598 CB LEU B 64 1470 1313 1568 -276 -53 32 C
ATOM 4599 CG LEU B 64 -36.211 -28.212 -1.386 1.00 11.62 C
ANISOU 4599 CG LEU B 64 1655 1240 1518 -211 -130 148 C
ATOM 4600 CD1 LEU B 64 -35.240 -28.702 -0.321 1.00 13.06 C
ANISOU 4600 CD1 LEU B 64 1688 1409 1863 -228 -233 243 C
ATOM 4601 CD2 LEU B 64 -37.432 -27.550 -0.762 1.00 13.37 C
ANISOU 4601 CD2 LEU B 64 1686 1661 1731 -206 -32 169 C
ATOM 4602 C LEU B 64 -35.525 -25.716 -4.316 1.00 10.88 C
ANISOU 4602 C LEU B 64 1450 1360 1323 -217 -61 29 C
ATOM 4603 O LEU B 64 -34.804 -26.132 -5.222 1.00 12.14 O
ANISOU 4603 O LEU B 64 1737 1496 1377 -258 80 57 O
ATOM 4604 N THR B 65 -35.596 -24.428 -3.975 1.00 11.01 N
ANISOU 4604 N THR B 65 1610 1293 1277 -257 39 87 N
ATOM 4605 CA THR B 65 -34.877 -23.351 -4.646 1.00 10.71 C
ANISOU 4605 CA THR B 65 1462 1285 1323 -262 69 3 C
ATOM 4606 CB THR B 65 -35.854 -22.422 -5.394 1.00 11.52 C
ANISOU 4606 CB THR B 65 1654 1314 1408 -339 -73 100 C
ATOM 4607 OG1 THR B 65 -36.465 -23.174 -6.449 1.00 13.66 O
ANISOU 4607 OG1 THR B 65 2137 1539 1515 -429 -302 103 O
ATOM 4608 CG2 THR B 65 -35.167 -21.215 -5.986 1.00 12.75 C
ANISOU 4608 CG2 THR B 65 1736 1323 1784 -281 -182 293 C
ATOM 4609 C THR B 65 -34.034 -22.600 -3.609 1.00 10.71 C
ANISOU 4609 C THR B 65 1510 1244 1315 -312 33 105 C
ATOM 4610 O THR B 65 -34.494 -22.305 -2.508 1.00 11.88 O
ANISOU 4610 O THR B 65 1585 1503 1423 -139 4 -206 O
ATOM 4611 N GLY B 66 -32.805 -22.252 -3.996 1.00 10.23 N
ANISOU 4611 N GLY B 66 1405 1267 1213 -205 -31 108 N
ATOM 4612 CA GLY B 66 -31.924 -21.497 -3.113 1.00 10.72 C
ANISOU 4612 CA GLY B 66 1511 1178 1381 -310 -64 149 C
ATOM 4613 C GLY B 66 -32.563 -20.228 -2.575 1.00 11.32 C
ANISOU 4613 C GLY B 66 1597 1351 1351 -196 -206 60 C
ATOM 4614 O GLY B 66 -33.207 -19.462 -3.302 1.00 11.16 O
ANISOU 4614 O GLY B 66 1368 1352 1520 -150 -125 113 O
ATOM 4615 N GLY B 67 -32.299 -19.951 -1.287 1.00 10.48 N
ANISOU 4615 N GLY B 67 1440 1182 1358 -36 -318 48 N
ATOM 4616 CA GLY B 67 -32.888 -18.784 -0.635 1.00 10.53 C
ANISOU 4616 CA GLY B 67 1316 1323 1362 -30 -309 -34 C
ATOM 4617 C GLY B 67 -32.239 -17.467 -0.980 1.00 10.59 C
ANISOU 4617 C GLY B 67 1484 1329 1210 -7 -268 39 C
ATOM 4618 O GLY B 67 -32.834 -16.421 -0.668 1.00 11.84 O
ANISOU 4618 O GLY B 67 1441 1448 1610 -58 -10 -123 O
ATOM 4619 N ALA B 68 -31.036 -17.490 -1.545 1.00 10.50 N
ANISOU 4619 N ALA B 68 1486 1107 1396 -124 -226 -55 N
ATOM 4620 CA ALA B 68 -30.294 -16.252 -1.879 1.00 10.80 C
ANISOU 4620 CA ALA B 68 1548 1172 1384 -148 -197 75 C
ATOM 4621 CB ALA B 68 -29.097 -16.070 -0.968 1.00 10.63 C
ANISOU 4621 CB ALA B 68 1599 1125 1313 -309 -124 103 C
ATOM 4622 C ALA B 68 -29.921 -16.249 -3.354 1.00 10.55 C
ANISOU 4622 C ALA B 68 1393 1208 1408 -216 -215 10 C
ATOM 4623 O ALA B 68 -28.751 -16.369 -3.727 1.00 11.16 O
ANISOU 4623 O ALA B 68 1466 1342 1429 -51 -158 73 O
ATOM 4624 N PRO B 69 -30.905 -16.076 -4.258 1.00 10.49 N
ANISOU 4624 N PRO B 69 1452 1289 1243 -65 -189 15 N
ATOM 4625 CA PRO B 69 -30.602 -16.008 -5.693 1.00 10.05 C
ANISOU 4625 CA PRO B 69 1337 1193 1287 -49 -143 14 C
ATOM 4626 CB PRO B 69 -31.972 -15.871 -6.354 1.00 10.95 C
ANISOU 4626 CB PRO B 69 1536 1406 1217 -163 -357 55 C
ATOM 4627 CG PRO B 69 -32.838 -15.271 -5.267 1.00 12.26 C
ANISOU 4627 CG PRO B 69 1676 1479 1502 -6 -366 -107 C
ATOM 4628 CD PRO B 69 -32.332 -15.887 -3.976 1.00 11.24 C
ANISOU 4628 CD PRO B 69 1502 1381 1386 23 -296 -207 C
ATOM 4629 C PRO B 69 -29.703 -14.815 -6.022 1.00 10.26 C
ANISOU 4629 C PRO B 69 1303 1284 1310 -98 -143 41 C
ATOM 4630 O PRO B 69 -29.735 -13.774 -5.337 1.00 10.95 O
ANISOU 4630 O PRO B 69 1686 1072 1402 -177 3 134 O
ATOM 4631 N ARG B 70 -28.892 -14.991 -7.058 1.00 9.50 N
ANISOU 4631 N ARG B 70 1317 1131 1161 -185 -182 67 N
ATOM 4632 CA ARG B 70 -27.941 -13.961 -7.467 1.00 9.66 C
ANISOU 4632 CA ARG B 70 1464 984 1222 -188 -236 94 C
ATOM 4633 CB ARG B 70 -26.512 -14.504 -7.379 1.00 10.36 C
ANISOU 4633 CB ARG B 70 1546 1052 1338 -55 -189 103 C
ATOM 4634 CG ARG B 70 -26.148 -15.089 -6.027 1.00 10.47 C
ANISOU 4634 CG ARG B 70 1547 1009 1422 -34 -188 154 C
ATOM 4635 CD ARG B 70 -24.727 -15.597 -5.941 1.00 11.14 C
ANISOU 4635 CD ARG B 70 1535 1159 1536 -92 -182 231 C
ATOM 4636 NE ARG B 70 -23.759 -14.536 -5.841 1.00 11.29 N
ANISOU 4636 NE ARG B 70 1464 1309 1515 -148 -206 294 N
ATOM 4637 CZ ARG B 70 -23.339 -13.989 -4.696 1.00 11.04 C
ANISOU 4637 CZ ARG B 70 1589 1116 1489 -88 -110 229 C
ATOM 4638 NH1 ARG B 70 -23.893 -14.345 -3.532 1.00 11.83 N
ANISOU 4638 NH1 ARG B 70 1686 1296 1510 75 -80 279 N
ATOM 4639 NH2 ARG B 70 -22.369 -13.081 -4.743 1.00 11.67 N
ANISOU 4639 NH2 ARG B 70 1553 1074 1806 -54 -356 259 N
ATOM 4640 C ARG B 70 -28.226 -13.499 -8.898 1.00 10.01 C
ANISOU 4640 C ARG B 70 1503 1010 1288 -111 -280 144 C
ATOM 4641 O ARG B 70 -28.912 -14.178 -9.662 1.00 10.92 O
ANISOU 4641 O ARG B 70 1834 1080 1233 -144 -401 194 O
ATOM 4642 N LEU B 71 -27.701 -12.307 -9.224 1.00 10.07 N
ANISOU 4642 N LEU B 71 1578 1087 1159 -219 -359 80 N
ATOM 4643 CA LEU B 71 -27.722 -11.792 -10.567 1.00 10.50 C
ANISOU 4643 CA LEU B 71 1483 1283 1221 -168 -243 173 C
ATOM 4644 CB LEU B 71 -28.377 -10.410 -10.587 1.00 11.39 C
ANISOU 4644 CB LEU B 71 1570 1330 1428 -155 -269 141 C
ATOM 4645 CG LEU B 71 -29.845 -10.369 -10.138 1.00 11.26 C
ANISOU 4645 CG LEU B 71 1580 1363 1333 -118 -227 147 C
ATOM 4646 CD1 LEU B 71 -30.299 -8.923 -9.965 1.00 12.00 C
ANISOU 4646 CD1 LEU B 71 1768 1348 1442 -224 -399 -30 C
ATOM 4647 CD2 LEU B 71 -30.763 -11.099 -11.130 1.00 12.95 C
ANISOU 4647 CD2 LEU B 71 1507 1690 1723 -177 -276 145 C
ATOM 4648 C LEU B 71 -26.290 -11.732 -11.084 1.00 10.43 C
ANISOU 4648 C LEU B 71 1465 1290 1207 -152 -236 17 C
ATOM 4649 O LEU B 71 -25.413 -11.177 -10.411 1.00 10.74 O
ANISOU 4649 O LEU B 71 1579 1393 1107 -292 -194 43 O
ATOM 4650 N ARG B 72 -26.072 -12.316 -12.272 1.00 10.58 N
ANISOU 4650 N ARG B 72 1530 1206 1283 -124 -339 -80 N
ATOM 4651 CA ARG B 72 -24.812 -12.213 -12.978 1.00 11.33 C
ANISOU 4651 CA ARG B 72 1593 1370 1340 -282 -340 130 C
ATOM 4652 CB ARG B 72 -24.374 -13.576 -13.510 1.00 13.85 C
ANISOU 4652 CB ARG B 72 1828 1577 1857 -81 -137 31 C
ATOM 4653 CG ARG B 72 -23.077 -13.568 -14.317 1.00 15.77 C
ANISOU 4653 CG ARG B 72 1630 2015 2346 -46 -131 16 C
ATOM 4654 CD ARG B 72 -22.930 -14.833 -15.142 1.00 22.92 C
ANISOU 4654 CD ARG B 72 2796 2189 3722 50 461 -385 C
ATOM 4655 NE ARG B 72 -21.534 -15.189 -15.294 1.00 32.37 N
ANISOU 4655 NE ARG B 72 3011 3961 5327 -434 425 -989 N
ATOM 4656 CZ ARG B 72 -20.818 -15.004 -16.383 1.00 38.74 C
ANISOU 4656 CZ ARG B 72 4366 5143 5208 -54 634 -1059 C
ATOM 4657 NH1 ARG B 72 -21.308 -14.269 -17.370 1.00 45.58 N
ANISOU 4657 NH1 ARG B 72 6894 3932 6490 -315 -1098 -1529 N
ATOM 4658 NH2 ARG B 72 -19.606 -15.538 -16.469 1.00 39.47 N
ANISOU 4658 NH2 ARG B 72 3978 5028 5990 305 316 -2907 N
ATOM 4659 C ARG B 72 -24.983 -11.210 -14.114 1.00 10.68 C
ANISOU 4659 C ARG B 72 1430 1421 1205 -178 -283 67 C
ATOM 4660 O ARG B 72 -25.788 -11.435 -15.023 1.00 12.09 O
ANISOU 4660 O ARG B 72 1848 1418 1325 -249 -491 75 O
ATOM 4661 N VAL B 73 -24.238 -10.098 -14.026 1.00 10.39 N
ANISOU 4661 N VAL B 73 1375 1449 1122 -147 -281 32 N
ATOM 4662 CA VAL B 73 -24.302 -9.067 -15.064 1.00 11.97 C
ANISOU 4662 CA VAL B 73 1552 1663 1331 -245 -267 260 C
ATOM 4663 CB VAL B 73 -24.649 -7.675 -14.520 1.00 15.65 C
ANISOU 4663 CB VAL B 73 1925 2068 1954 -17 -211 -121 C
ATOM 4664 CG1 VAL B 73 -26.026 -7.667 -13.875 1.00 16.34 C
ANISOU 4664 CG1 VAL B 73 2214 1669 2325 -259 74 -171 C
ATOM 4665 CG2 VAL B 73 -23.574 -7.142 -13.603 1.00 17.04 C
ANISOU 4665 CG2 VAL B 73 2439 2016 2017 15 -279 -311 C
ATOM 4666 C VAL B 73 -22.953 -9.045 -15.770 1.00 11.89 C
ANISOU 4666 C VAL B 73 1558 1552 1406 -78 -241 353 C
ATOM 4667 O VAL B 73 -21.896 -9.228 -15.139 1.00 13.35 O
ANISOU 4667 O VAL B 73 1599 2007 1466 -170 -332 546 O
ATOM 4668 N SER B 74 -23.007 -8.826 -17.075 1.00 12.00 N
ANISOU 4668 N SER B 74 1523 1644 1393 -103 -233 346 N
ATOM 4669 CA SER B 74 -21.801 -8.625 -17.859 1.00 11.76 C
ANISOU 4669 CA SER B 74 1521 1547 1399 -189 -215 473 C
ATOM 4670 CB SER B 74 -21.371 -9.834 -18.604 1.00 14.32 C
ANISOU 4670 CB SER B 74 2122 1452 1867 -170 -157 595 C
ATOM 4671 OG SER B 74 -22.324 -10.220 -19.560 1.00 18.52 O
ANISOU 4671 OG SER B 74 2484 1980 2573 153 -427 -10 O
ATOM 4672 C SER B 74 -22.049 -7.442 -18.789 1.00 11.53 C
ANISOU 4672 C SER B 74 1598 1404 1378 -213 -122 417 C
ATOM 4673 O SER B 74 -23.173 -7.245 -19.263 1.00 14.41 O
ANISOU 4673 O SER B 74 1905 1776 1793 -313 -455 402 O
ATOM 4674 N PHE B 75 -20.979 -6.678 -19.045 1.00 11.30 N
ANISOU 4674 N PHE B 75 1569 1391 1331 -201 -167 334 N
ATOM 4675 CA PHE B 75 -21.085 -5.520 -19.899 1.00 11.69 C
ANISOU 4675 CA PHE B 75 1647 1501 1290 -42 -213 340 C
ATOM 4676 CB PHE B 75 -21.940 -4.434 -19.237 1.00 11.42 C
ANISOU 4676 CB PHE B 75 1569 1430 1337 -93 -90 277 C
ATOM 4677 CG PHE B 75 -21.412 -3.968 -17.902 1.00 12.23 C
ANISOU 4677 CG PHE B 75 1565 1565 1516 2 -241 184 C
ATOM 4678 CD1 PHE B 75 -20.483 -2.950 -17.823 1.00 12.68 C
ANISOU 4678 CD1 PHE B 75 1685 1627 1504 -76 -13 138 C
ATOM 4679 CE1 PHE B 75 -19.967 -2.549 -16.603 1.00 14.04 C
ANISOU 4679 CE1 PHE B 75 1854 1780 1700 -86 -160 42 C
ATOM 4680 CZ PHE B 75 -20.378 -3.142 -15.450 1.00 14.38 C
ANISOU 4680 CZ PHE B 75 2046 1703 1713 -174 -30 -52 C
ATOM 4681 CD2 PHE B 75 -21.803 -4.585 -16.723 1.00 12.78 C
ANISOU 4681 CD2 PHE B 75 1769 1595 1491 -249 -67 17 C
ATOM 4682 CE2 PHE B 75 -21.289 -4.173 -15.498 1.00 12.83 C
ANISOU 4682 CE2 PHE B 75 1871 1595 1407 -139 -1 33 C
ATOM 4683 C PHE B 75 -19.692 -4.989 -20.192 1.00 12.26 C
ANISOU 4683 C PHE B 75 1876 1439 1340 -192 -189 262 C
ATOM 4684 O PHE B 75 -18.730 -5.362 -19.557 1.00 13.02 O
ANISOU 4684 O PHE B 75 1870 1562 1513 -230 -212 455 O
ATOM 4685 N THR B 76 -19.642 -4.088 -21.165 1.00 11.95 N
ANISOU 4685 N THR B 76 1863 1326 1350 -177 -218 260 N
ATOM 4686 CA THR B 76 -18.472 -3.313 -21.487 1.00 12.55 C
ANISOU 4686 CA THR B 76 1760 1480 1527 -155 -177 266 C
ATOM 4687 CB THR B 76 -18.082 -3.478 -22.960 1.00 13.02 C
ANISOU 4687 CB THR B 76 2026 1405 1513 86 -240 319 C
ATOM 4688 OG1 THR B 76 -17.856 -4.865 -23.237 1.00 14.89 O
ANISOU 4688 OG1 THR B 76 2303 1496 1858 105 -33 105 O
ATOM 4689 CG2 THR B 76 -16.879 -2.640 -23.325 1.00 15.08 C
ANISOU 4689 CG2 THR B 76 2350 1803 1576 -95 -95 232 C
ATOM 4690 C THR B 76 -18.765 -1.857 -21.130 1.00 11.46 C
ANISOU 4690 C THR B 76 1549 1556 1249 23 -108 382 C
ATOM 4691 O THR B 76 -19.809 -1.316 -21.513 1.00 12.69 O
ANISOU 4691 O THR B 76 1727 1441 1652 61 -411 358 O
ATOM 4692 N ALA B 77 -17.830 -1.211 -20.412 1.00 12.30 N
ANISOU 4692 N ALA B 77 1829 1401 1441 57 -231 330 N
ATOM 4693 CA ALA B 77 -17.871 0.216 -20.166 1.00 12.64 C
ANISOU 4693 CA ALA B 77 1849 1416 1535 35 -197 264 C
ATOM 4694 CB ALA B 77 -17.692 0.486 -18.709 1.00 13.38 C
ANISOU 4694 CB ALA B 77 1744 1854 1485 -39 -290 182 C
ATOM 4695 C ALA B 77 -16.774 0.890 -20.970 1.00 12.67 C
ANISOU 4695 C ALA B 77 1956 1171 1685 -83 -185 198 C
ATOM 4696 O ALA B 77 -15.635 0.473 -20.913 1.00 13.74 O
ANISOU 4696 O ALA B 77 2077 1572 1571 57 77 369 O
ATOM 4697 N GLU B 78 -17.150 1.931 -21.709 1.00 12.28 N
ANISOU 4697 N GLU B 78 1750 1377 1540 -195 -198 365 N
ATOM 4698 CA GLU B 78 -16.192 2.793 -22.406 1.00 13.17 C
ANISOU 4698 CA GLU B 78 2079 1333 1589 -219 -134 402 C
ATOM 4699 CB GLU B 78 -16.599 3.013 -23.863 1.00 14.46 C
ANISOU 4699 CB GLU B 78 2346 1519 1629 -431 -335 425 C
ATOM 4700 CG GLU B 78 -15.597 3.887 -24.604 1.00 17.09 C
ANISOU 4700 CG GLU B 78 2730 1854 1908 -568 -108 572 C
ATOM 4701 CD GLU B 78 -15.833 4.104 -26.074 1.00 20.40 C
ANISOU 4701 CD GLU B 78 3165 2599 1985 -1037 -118 842 C
ATOM 4702 OE1 GLU B 78 -16.886 3.725 -26.558 1.00 25.70 O
ANISOU 4702 OE1 GLU B 78 3707 3808 2249 -1516 -548 888 O
ATOM 4703 OE2 GLU B 78 -14.957 4.687 -26.729 1.00 27.64 O
ANISOU 4703 OE2 GLU B 78 3942 4054 2504 -1256 622 961 O
ATOM 4704 C GLU B 78 -16.135 4.117 -21.650 1.00 13.43 C
ANISOU 4704 C GLU B 78 1897 1555 1649 -303 -185 249 C
ATOM 4705 O GLU B 78 -17.169 4.775 -21.528 1.00 13.84 O
ANISOU 4705 O GLU B 78 1838 1506 1914 -216 -256 302 O
ATOM 4706 N ILE B 79 -14.944 4.446 -21.145 1.00 12.67 N
ANISOU 4706 N ILE B 79 1792 1464 1557 -203 -138 250 N
ATOM 4707 CA ILE B 79 -14.682 5.656 -20.404 1.00 12.82 C
ANISOU 4707 CA ILE B 79 1863 1419 1587 -242 -83 315 C
ATOM 4708 CB ILE B 79 -13.879 5.369 -19.132 1.00 13.58 C
ANISOU 4708 CB ILE B 79 1908 1665 1586 -220 -91 335 C
ATOM 4709 CG1 ILE B 79 -14.557 4.312 -18.249 1.00 14.56 C
ANISOU 4709 CG1 ILE B 79 2049 1968 1515 -149 4 480 C
ATOM 4710 CG2 ILE B 79 -13.607 6.657 -18.376 1.00 15.74 C
ANISOU 4710 CG2 ILE B 79 2368 1913 1698 -40 -137 145 C
ATOM 4711 CD1 ILE B 79 -13.694 3.829 -17.134 1.00 17.79 C
ANISOU 4711 CD1 ILE B 79 2429 2555 1773 -3 -159 558 C
ATOM 4712 C ILE B 79 -13.925 6.617 -21.319 1.00 13.72 C
ANISOU 4712 C ILE B 79 1984 1605 1622 -332 -180 463 C
ATOM 4713 O ILE B 79 -12.847 6.255 -21.827 1.00 14.60 O
ANISOU 4713 O ILE B 79 2105 1790 1652 -406 -45 445 O
ATOM 4714 N LYS B 80 -14.530 7.793 -21.537 1.00 14.06 N
ANISOU 4714 N LYS B 80 2098 1562 1680 -209 56 313 N
ATOM 4715 CA LYS B 80 -13.976 8.811 -22.423 1.00 15.55 C
ANISOU 4715 CA LYS B 80 2714 1473 1721 -277 -236 485 C
ATOM 4716 CB LYS B 80 -14.989 9.187 -23.511 1.00 18.53 C
ANISOU 4716 CB LYS B 80 3157 1807 2074 -249 -549 706 C
ATOM 4717 CG LYS B 80 -15.502 8.040 -24.363 1.00 21.31 C
ANISOU 4717 CG LYS B 80 3696 2043 2357 -261 -672 543 C
ATOM 4718 CD LYS B 80 -16.623 8.476 -25.263 1.00 26.75 C
ANISOU 4718 CD LYS B 80 4004 3019 3139 -167 -1106 680 C
ATOM 4719 CE LYS B 80 -17.401 7.331 -25.861 1.00 30.23 C
ANISOU 4719 CE LYS B 80 4477 3360 3646 -322 -1414 1049 C
ATOM 4720 NZ LYS B 80 -18.653 7.834 -26.479 1.00 36.55 N
ANISOU 4720 NZ LYS B 80 4196 4696 4994 -194 -1547 1193 N
ATOM 4721 C LYS B 80 -13.590 10.071 -21.643 1.00 15.47 C
ANISOU 4721 C LYS B 80 2732 1426 1718 -163 -185 484 C
ATOM 4722 O LYS B 80 -14.027 10.278 -20.508 1.00 16.48 O
ANISOU 4722 O LYS B 80 2719 1735 1807 -287 77 249 O
ATOM 4723 N ASN B 81 -12.767 10.895 -22.295 1.00 15.99 N
ANISOU 4723 N ASN B 81 2774 1410 1889 -172 -156 535 N
ATOM 4724 CA ASN B 81 -12.298 12.216 -21.808 1.00 17.43 C
ANISOU 4724 CA ASN B 81 2870 1351 2400 -312 -256 553 C
ATOM 4725 CB ASN B 81 -13.393 13.042 -21.127 1.00 18.41 C
ANISOU 4725 CB ASN B 81 2942 1582 2468 -129 -323 609 C
ATOM 4726 CG ASN B 81 -14.595 13.317 -22.006 1.00 18.79 C
ANISOU 4726 CG ASN B 81 2846 1651 2642 170 -226 699 C
ATOM 4727 OD1 ASN B 81 -14.500 13.246 -23.225 1.00 21.15 O
ANISOU 4727 OD1 ASN B 81 3468 1896 2669 56 -306 562 O
ATOM 4728 ND2 ASN B 81 -15.732 13.625 -21.387 1.00 18.99 N
ANISOU 4728 ND2 ASN B 81 2932 1616 2668 357 -223 400 N
ATOM 4729 C ASN B 81 -11.107 12.071 -20.843 1.00 17.16 C
ANISOU 4729 C ASN B 81 2962 1442 2115 -302 -145 582 C
ATOM 4730 O ASN B 81 -10.840 12.987 -20.056 1.00 19.00 O
ANISOU 4730 O ASN B 81 3294 1460 2464 -401 -185 427 O
ATOM 4731 N ILE B 82 -10.362 10.966 -20.951 1.00 16.08 N
ANISOU 4731 N ILE B 82 2853 1371 1886 -374 -145 395 N
ATOM 4732 CA ILE B 82 -9.163 10.714 -20.162 1.00 16.12 C
ANISOU 4732 CA ILE B 82 2752 1626 1744 -466 -54 532 C
ATOM 4733 CB ILE B 82 -8.923 9.193 -20.015 1.00 15.73 C
ANISOU 4733 CB ILE B 82 2588 1566 1819 -621 -87 636 C
ATOM 4734 CG1 ILE B 82 -10.142 8.476 -19.424 1.00 16.43 C
ANISOU 4734 CG1 ILE B 82 2581 1537 2124 -547 -115 942 C
ATOM 4735 CG2 ILE B 82 -7.662 8.928 -19.208 1.00 16.20 C
ANISOU 4735 CG2 ILE B 82 2525 1610 2017 -466 22 418 C
ATOM 4736 CD1 ILE B 82 -10.030 6.962 -19.505 1.00 17.37 C
ANISOU 4736 CD1 ILE B 82 2595 1658 2345 -291 -68 724 C
ATOM 4737 C ILE B 82 -7.964 11.380 -20.834 1.00 17.53 C
ANISOU 4737 C ILE B 82 2920 1846 1894 -592 -36 639 C
ATOM 4738 O ILE B 82 -7.700 11.154 -22.010 1.00 18.63 O
ANISOU 4738 O ILE B 82 3073 2142 1862 -881 -66 645 O
ATOM 4739 N LEU B 83 -7.223 12.192 -20.076 1.00 18.71 N
ANISOU 4739 N LEU B 83 3113 2325 1670 -861 30 707 N
ATOM 4740 CA LEU B 83 -6.046 12.860 -20.622 1.00 19.08 C
ANISOU 4740 CA LEU B 83 3160 2309 1780 -833 219 698 C
ATOM 4741 CB LEU B 83 -5.272 13.569 -19.512 1.00 20.56 C
ANISOU 4741 CB LEU B 83 3217 2511 2084 -888 187 535 C
ATOM 4742 CG LEU B 83 -4.069 14.395 -19.971 1.00 23.73 C
ANISOU 4742 CG LEU B 83 3781 3068 2165 -1309 253 656 C
ATOM 4743 CD1 LEU B 83 -4.498 15.593 -20.799 1.00 24.50 C
ANISOU 4743 CD1 LEU B 83 4101 2678 2530 -1286 455 626 C
ATOM 4744 CD2 LEU B 83 -3.253 14.851 -18.780 1.00 23.82 C
ANISOU 4744 CD2 LEU B 83 3865 2691 2495 -1324 -46 599 C
ATOM 4745 C LEU B 83 -5.159 11.823 -21.322 1.00 18.51 C
ANISOU 4745 C LEU B 83 2940 2423 1668 -860 195 636 C
ATOM 4746 O LEU B 83 -4.903 10.767 -20.770 1.00 18.26 O
ANISOU 4746 O LEU B 83 2742 2305 1888 -832 305 630 O
ATOM 4747 N ALA B 84 -4.655 12.155 -22.514 1.00 19.73 N
ANISOU 4747 N ALA B 84 3144 2600 1751 -883 397 622 N
ATOM 4748 CA ALA B 84 -3.786 11.246 -23.235 1.00 22.28 C
ANISOU 4748 CA ALA B 84 3350 2931 2182 -626 650 799 C
ATOM 4749 CB ALA B 84 -3.361 11.861 -24.545 1.00 23.43 C
ANISOU 4749 CB ALA B 84 3624 3426 1852 -623 715 548 C
ATOM 4750 C ALA B 84 -2.577 10.882 -22.362 1.00 23.39 C
ANISOU 4750 C ALA B 84 3387 3398 2101 -531 718 889 C
ATOM 4751 O ALA B 84 -2.119 11.692 -21.546 1.00 22.81 O
ANISOU 4751 O ALA B 84 2766 3169 2730 -400 496 943 O
ATOM 4752 N ASP B 85 -2.092 9.645 -22.525 1.00 24.94 N
ANISOU 4752 N ASP B 85 3432 3780 2263 -263 909 615 N
ATOM 4753 CA ASP B 85 -0.878 9.120 -21.854 1.00 27.29 C
ANISOU 4753 CA ASP B 85 3174 4345 2848 -452 965 803 C
ATOM 4754 CB ASP B 85 0.345 10.021 -22.083 1.00 32.13 C
ANISOU 4754 CB ASP B 85 3441 4783 3984 -861 678 945 C
ATOM 4755 CG ASP B 85 0.649 10.262 -23.555 1.00 40.15 C
ANISOU 4755 CG ASP B 85 4733 6181 4338 -1078 1262 387 C
ATOM 4756 OD1 ASP B 85 0.466 9.315 -24.356 1.00 48.17 O
ANISOU 4756 OD1 ASP B 85 5618 6371 6313 -799 1377 -575 O
ATOM 4757 OD2 ASP B 85 1.043 11.405 -23.898 1.00 55.62 O
ANISOU 4757 OD2 ASP B 85 7510 6590 7033 -1866 1343 387 O
ATOM 4758 C ASP B 85 -1.147 8.877 -20.369 1.00 24.36 C
ANISOU 4758 C ASP B 85 2737 3843 2676 -159 359 986 C
ATOM 4759 O ASP B 85 -0.218 8.846 -19.583 1.00 28.29 O
ANISOU 4759 O ASP B 85 2576 5084 3089 -458 285 827 O
ATOM 4760 N SER B 86 -2.424 8.705 -19.991 1.00 20.74 N
ANISOU 4760 N SER B 86 2708 3001 2170 -306 254 720 N
ATOM 4761 CA SER B 86 -2.755 8.383 -18.593 1.00 18.62 C
ANISOU 4761 CA SER B 86 2481 2564 2027 -63 119 685 C
ATOM 4762 CB SER B 86 -4.189 8.701 -18.266 1.00 17.88 C
ANISOU 4762 CB SER B 86 2487 2402 1903 -22 127 629 C
ATOM 4763 OG SER B 86 -4.405 10.100 -18.249 1.00 19.49 O
ANISOU 4763 OG SER B 86 2950 2213 2241 -324 179 700 O
ATOM 4764 C SER B 86 -2.492 6.895 -18.338 1.00 18.51 C
ANISOU 4764 C SER B 86 2453 2580 1998 -33 182 822 C
ATOM 4765 O SER B 86 -3.005 6.038 -19.058 1.00 20.56 O
ANISOU 4765 O SER B 86 3121 2571 2120 155 -109 692 O
ATOM 4766 N SER B 87 -1.741 6.583 -17.278 1.00 19.64 N
ANISOU 4766 N SER B 87 2534 2930 1998 -74 187 652 N
ATOM 4767 CA SER B 87 -1.493 5.182 -16.931 1.00 18.38 C
ANISOU 4767 CA SER B 87 2177 2831 1973 118 394 679 C
ATOM 4768 CB SER B 87 -0.401 5.061 -15.907 1.00 21.25 C
ANISOU 4768 CB SER B 87 2373 3091 2610 -239 -18 804 C
ATOM 4769 OG SER B 87 -0.892 5.262 -14.592 1.00 24.20 O
ANISOU 4769 OG SER B 87 2541 4020 2630 -295 98 1030 O
ATOM 4770 C SER B 87 -2.776 4.466 -16.471 1.00 17.57 C
ANISOU 4770 C SER B 87 2211 2700 1764 52 312 445 C
ATOM 4771 O SER B 87 -2.960 3.271 -16.719 1.00 18.97 O
ANISOU 4771 O SER B 87 2673 2710 1825 103 406 525 O
ATOM 4772 N LEU B 88 -3.632 5.200 -15.765 1.00 16.94 N
ANISOU 4772 N LEU B 88 2284 2434 1715 82 267 415 N
ATOM 4773 CA LEU B 88 -4.858 4.693 -15.089 1.00 15.34 C
ANISOU 4773 CA LEU B 88 2323 1968 1535 21 200 354 C
ATOM 4774 CB LEU B 88 -5.813 4.104 -16.133 1.00 14.54 C
ANISOU 4774 CB LEU B 88 2086 1868 1570 72 144 335 C
ATOM 4775 CG LEU B 88 -6.339 5.102 -17.158 1.00 16.59 C
ANISOU 4775 CG LEU B 88 2634 1986 1681 26 -32 416 C
ATOM 4776 CD1 LEU B 88 -7.270 4.406 -18.138 1.00 18.21 C
ANISOU 4776 CD1 LEU B 88 3251 1896 1770 -123 -83 211 C
ATOM 4777 CD2 LEU B 88 -7.070 6.264 -16.483 1.00 17.09 C
ANISOU 4777 CD2 LEU B 88 2686 1865 1943 39 -28 540 C
ATOM 4778 C LEU B 88 -4.548 3.664 -13.987 1.00 15.98 C
ANISOU 4778 C LEU B 88 2355 2218 1496 162 221 408 C
ATOM 4779 O LEU B 88 -5.468 3.035 -13.484 1.00 15.56 O
ANISOU 4779 O LEU B 88 2414 1976 1522 81 163 366 O
ATOM 4780 N LYS B 89 -3.289 3.538 -13.571 1.00 16.77 N
ANISOU 4780 N LYS B 89 2290 2247 1833 158 449 564 N
ATOM 4781 CA ALYS B 89 -2.944 2.514 -12.599 0.50 16.64 C
ANISOU 4781 CA ALYS B 89 2254 2260 1805 257 458 533 C
ATOM 4782 CA BLYS B 89 -2.878 2.562 -12.558 0.50 16.66 C
ANISOU 4782 CA BLYS B 89 2183 2355 1792 211 432 554 C
ATOM 4783 CB ALYS B 89 -1.436 2.431 -12.365 0.50 18.95 C
ANISOU 4783 CB ALYS B 89 2313 2657 2229 253 436 508 C
ATOM 4784 CB BLYS B 89 -1.389 2.752 -12.245 0.50 19.54 C
ANISOU 4784 CB BLYS B 89 2236 2914 2271 99 448 475 C
ATOM 4785 CG ALYS B 89 -1.006 1.338 -11.390 0.50 20.21 C
ANISOU 4785 CG ALYS B 89 2673 2423 2583 341 579 532 C
ATOM 4786 CG BLYS B 89 -0.799 1.980 -11.068 0.50 20.37 C
ANISOU 4786 CG BLYS B 89 2299 2952 2486 327 535 517 C
ATOM 4787 CD ALYS B 89 -1.438 -0.077 -11.752 0.50 21.14 C
ANISOU 4787 CD ALYS B 89 2708 2406 2918 224 469 603 C
ATOM 4788 CD BLYS B 89 0.703 2.191 -10.908 0.50 21.99 C
ANISOU 4788 CD BLYS B 89 2344 3149 2859 119 641 375 C
ATOM 4789 CE ALYS B 89 -0.754 -1.132 -10.903 0.50 22.33 C
ANISOU 4789 CE ALYS B 89 2973 1924 3585 420 389 298 C
ATOM 4790 CE BLYS B 89 1.270 1.631 -9.620 0.50 22.91 C
ANISOU 4790 CE BLYS B 89 2372 3546 2785 -19 651 387 C
ATOM 4791 NZ ALYS B 89 0.643 -1.339 -11.357 0.50 21.70 N
ANISOU 4791 NZ ALYS B 89 2769 1559 3913 459 275 155 N
ATOM 4792 NZ BLYS B 89 0.726 0.290 -9.320 0.50 26.40 N
ANISOU 4792 NZ BLYS B 89 2982 3560 3487 184 676 336 N
ATOM 4793 C LYS B 89 -3.689 2.761 -11.282 1.00 15.17 C
ANISOU 4793 C LYS B 89 2161 2048 1552 78 248 535 C
ATOM 4794 O LYS B 89 -3.607 3.829 -10.702 1.00 15.09 O
ANISOU 4794 O LYS B 89 1885 1999 1847 -165 15 544 O
ATOM 4795 N ASP B 90 -4.403 1.717 -10.828 1.00 13.28 N
ANISOU 4795 N ASP B 90 1841 1799 1405 100 132 344 N
ATOM 4796 CA ASP B 90 -5.096 1.733 -9.546 1.00 11.56 C
ANISOU 4796 CA ASP B 90 1682 1380 1329 108 43 300 C
ATOM 4797 CB ASP B 90 -4.089 1.805 -8.396 1.00 11.93 C
ANISOU 4797 CB ASP B 90 1441 1675 1416 -2 145 287 C
ATOM 4798 CG ASP B 90 -3.179 0.598 -8.303 1.00 13.01 C
ANISOU 4798 CG ASP B 90 1710 1718 1512 84 122 67 C
ATOM 4799 OD1 ASP B 90 -3.622 -0.506 -8.660 1.00 13.80 O
ANISOU 4799 OD1 ASP B 90 1811 1638 1792 -14 196 28 O
ATOM 4800 OD2 ASP B 90 -2.002 0.775 -7.847 1.00 18.21 O
ANISOU 4800 OD2 ASP B 90 1810 2190 2918 81 -236 98 O
ATOM 4801 C ASP B 90 -6.148 2.849 -9.483 1.00 11.37 C
ANISOU 4801 C ASP B 90 1753 1378 1187 64 126 288 C
ATOM 4802 O ASP B 90 -6.447 3.369 -8.392 1.00 12.18 O
ANISOU 4802 O ASP B 90 2068 1449 1108 28 183 257 O
ATOM 4803 N GLN B 91 -6.796 3.142 -10.619 1.00 11.28 N
ANISOU 4803 N GLN B 91 1773 1377 1136 -77 27 207 N
ATOM 4804 CA GLN B 91 -7.720 4.274 -10.655 1.00 11.70 C
ANISOU 4804 CA GLN B 91 1770 1340 1333 -79 -2 134 C
ATOM 4805 CB GLN B 91 -7.150 5.399 -11.520 1.00 11.72 C
ANISOU 4805 CB GLN B 91 1726 1273 1452 -91 64 148 C
ATOM 4806 CG GLN B 91 -6.003 6.121 -10.834 1.00 12.19 C
ANISOU 4806 CG GLN B 91 1735 1435 1462 -164 122 220 C
ATOM 4807 CD GLN B 91 -5.317 7.146 -11.688 1.00 12.91 C
ANISOU 4807 CD GLN B 91 1718 1496 1688 -310 223 139 C
ATOM 4808 OE1 GLN B 91 -4.967 6.865 -12.837 1.00 15.16 O
ANISOU 4808 OE1 GLN B 91 2132 1987 1639 -377 249 113 O
ATOM 4809 NE2 GLN B 91 -5.047 8.305 -11.106 1.00 13.83 N
ANISOU 4809 NE2 GLN B 91 1922 1553 1779 -390 -22 135 N
ATOM 4810 C GLN B 91 -9.142 3.933 -11.134 1.00 11.58 C
ANISOU 4810 C GLN B 91 1808 1268 1322 -99 -122 115 C
ATOM 4811 O GLN B 91 -10.033 4.773 -11.000 1.00 12.87 O
ANISOU 4811 O GLN B 91 1866 1377 1647 -130 -99 114 O
ATOM 4812 N ILE B 92 -9.381 2.733 -11.661 1.00 11.35 N
ANISOU 4812 N ILE B 92 1756 1231 1325 -78 -141 199 N
ATOM 4813 CA AILE B 92 -10.676 2.342 -12.221 0.70 12.05 C
ANISOU 4813 CA AILE B 92 1829 1497 1252 -118 -169 92 C
ATOM 4814 CA BILE B 92 -10.692 2.363 -12.199 0.30 11.68 C
ANISOU 4814 CA BILE B 92 1771 1431 1236 -67 -121 80 C
ATOM 4815 CB AILE B 92 -10.582 2.030 -13.729 0.70 13.99 C
ANISOU 4815 CB AILE B 92 2170 1800 1343 -295 -53 50 C
ATOM 4816 CB BILE B 92 -10.649 2.164 -13.728 0.30 12.49 C
ANISOU 4816 CB BILE B 92 1950 1548 1245 -147 -55 142 C
ATOM 4817 CG1AILE B 92 -9.912 3.155 -14.524 0.70 15.68 C
ANISOU 4817 CG1AILE B 92 2179 2031 1748 -366 -34 222 C
ATOM 4818 CG1BILE B 92 -10.224 3.465 -14.413 0.30 12.74 C
ANISOU 4818 CG1BILE B 92 1962 1566 1310 -77 -29 210 C
ATOM 4819 CG2AILE B 92 -11.976 1.702 -14.251 0.70 15.35 C
ANISOU 4819 CG2AILE B 92 2339 1899 1593 -400 -120 -23 C
ATOM 4820 CG2BILE B 92 -11.994 1.676 -14.246 0.30 13.09 C
ANISOU 4820 CG2BILE B 92 2030 1589 1353 -194 -76 98 C
ATOM 4821 CD1AILE B 92 -10.627 4.466 -14.479 0.70 16.60 C
ANISOU 4821 CD1AILE B 92 2316 2164 1828 -232 -11 399 C
ATOM 4822 CD1BILE B 92 -10.084 3.360 -15.897 0.30 13.40 C
ANISOU 4822 CD1BILE B 92 2116 1699 1277 -96 -45 330 C
ATOM 4823 C ILE B 92 -11.200 1.119 -11.474 1.00 10.98 C
ANISOU 4823 C ILE B 92 1608 1402 1159 -49 -60 -21 C
ATOM 4824 O ILE B 92 -10.455 0.162 -11.233 1.00 12.03 O
ANISOU 4824 O ILE B 92 1531 1453 1588 19 -76 21 O
ATOM 4825 N GLY B 93 -12.486 1.142 -11.131 1.00 10.68 N
ANISOU 4825 N GLY B 93 1583 1221 1254 -124 -50 20 N
ATOM 4826 CA GLY B 93 -13.142 -0.038 -10.622 1.00 10.69 C
ANISOU 4826 CA GLY B 93 1621 1202 1236 -132 -143 50 C
ATOM 4827 C GLY B 93 -14.641 0.151 -10.602 1.00 10.48 C
ANISOU 4827 C GLY B 93 1633 1102 1247 -21 -75 165 C
ATOM 4828 O GLY B 93 -15.195 0.868 -11.461 1.00 11.33 O
ANISOU 4828 O GLY B 93 1764 1197 1342 112 -48 258 O
ATOM 4829 N LEU B 94 -15.305 -0.511 -9.655 1.00 10.34 N
ANISOU 4829 N LEU B 94 1643 1097 1189 -34 -110 124 N
ATOM 4830 CA LEU B 94 -16.743 -0.425 -9.519 1.00 10.63 C
ANISOU 4830 CA LEU B 94 1594 1306 1138 -143 -118 53 C
ATOM 4831 CB LEU B 94 -17.394 -1.804 -9.673 1.00 10.76 C
ANISOU 4831 CB LEU B 94 1690 1180 1215 -25 -170 129 C
ATOM 4832 CG LEU B 94 -17.132 -2.512 -11.015 1.00 10.70 C
ANISOU 4832 CG LEU B 94 1515 1263 1287 -68 -314 -53 C
ATOM 4833 CD1 LEU B 94 -17.753 -3.897 -11.002 1.00 12.02 C
ANISOU 4833 CD1 LEU B 94 1678 1375 1514 -138 -299 -26 C
ATOM 4834 CD2 LEU B 94 -17.679 -1.707 -12.188 1.00 10.78 C
ANISOU 4834 CD2 LEU B 94 1340 1315 1441 -157 -330 -8 C
ATOM 4835 C LEU B 94 -17.091 0.185 -8.158 1.00 9.91 C
ANISOU 4835 C LEU B 94 1465 1187 1110 -200 -208 39 C
ATOM 4836 O LEU B 94 -16.319 0.093 -7.174 1.00 9.92 O
ANISOU 4836 O LEU B 94 1486 1275 1008 -157 -206 -23 O
ATOM 4837 N LYS B 95 -18.255 0.828 -8.105 1.00 10.91 N
ANISOU 4837 N LYS B 95 1720 1310 1112 -15 -227 92 N
ATOM 4838 CA LYS B 95 -18.825 1.290 -6.860 1.00 10.18 C
ANISOU 4838 CA LYS B 95 1658 1173 1035 -113 -106 135 C
ATOM 4839 CB LYS B 95 -19.954 2.278 -7.127 1.00 10.55 C
ANISOU 4839 CB LYS B 95 1784 1184 1037 -47 -128 -3 C
ATOM 4840 CG LYS B 95 -19.480 3.562 -7.796 1.00 11.86 C
ANISOU 4840 CG LYS B 95 1744 1374 1386 -60 46 173 C
ATOM 4841 CD LYS B 95 -20.589 4.585 -7.955 1.00 12.31 C
ANISOU 4841 CD LYS B 95 1840 1385 1450 26 -102 292 C
ATOM 4842 CE LYS B 95 -20.095 5.906 -8.489 1.00 12.29 C
ANISOU 4842 CE LYS B 95 1701 1415 1552 -62 -74 251 C
ATOM 4843 NZ LYS B 95 -21.168 6.926 -8.526 1.00 12.73 N
ANISOU 4843 NZ LYS B 95 1997 1268 1572 -11 -91 131 N
ATOM 4844 C LYS B 95 -19.244 0.100 -5.996 1.00 10.58 C
ANISOU 4844 C LYS B 95 1642 1219 1156 -134 -13 149 C
ATOM 4845 O LYS B 95 -19.351 -1.018 -6.465 1.00 11.55 O
ANISOU 4845 O LYS B 95 1904 1302 1180 -239 -147 121 O
ATOM 4846 N SER B 96 -19.459 0.358 -4.701 1.00 9.90 N
ANISOU 4846 N SER B 96 1693 956 1109 -111 -140 137 N
ATOM 4847 CA ASER B 96 -19.858 -0.711 -3.782 0.50 10.39 C
ANISOU 4847 CA ASER B 96 1622 1104 1220 -175 -129 207 C
ATOM 4848 CA BSER B 96 -19.860 -0.690 -3.764 0.50 9.82 C
ANISOU 4848 CA BSER B 96 1559 1033 1139 -138 -146 169 C
ATOM 4849 CB ASER B 96 -19.857 -0.208 -2.365 0.50 11.73 C
ANISOU 4849 CB ASER B 96 1830 1472 1154 -189 -138 215 C
ATOM 4850 CB BSER B 96 -19.897 -0.118 -2.350 0.50 9.37 C
ANISOU 4850 CB BSER B 96 1394 1125 1040 -196 -224 210 C
ATOM 4851 OG ASER B 96 -20.962 0.616 -2.106 0.50 14.13 O
ANISOU 4851 OG ASER B 96 2073 1563 1730 -68 -80 31 O
ATOM 4852 OG BSER B 96 -18.691 0.591 -1.983 0.50 8.54 O
ANISOU 4852 OG BSER B 96 1413 829 1004 -167 -161 90 O
ATOM 4853 C SER B 96 -21.235 -1.259 -4.169 1.00 9.96 C
ANISOU 4853 C SER B 96 1487 1035 1260 -63 -108 235 C
ATOM 4854 O SER B 96 -22.156 -0.514 -4.440 1.00 11.73 O
ANISOU 4854 O SER B 96 1516 1240 1699 16 -237 249 O
ATOM 4855 N PHE B 97 -21.355 -2.591 -4.201 1.00 10.21 N
ANISOU 4855 N PHE B 97 1464 999 1415 75 -137 92 N
ATOM 4856 CA PHE B 97 -22.631 -3.288 -4.481 1.00 9.67 C
ANISOU 4856 CA PHE B 97 1443 1044 1187 -4 -119 148 C
ATOM 4857 CB PHE B 97 -23.607 -3.143 -3.309 1.00 10.55 C
ANISOU 4857 CB PHE B 97 1443 1231 1333 62 -93 23 C
ATOM 4858 CG PHE B 97 -22.948 -3.546 -2.010 1.00 10.63 C
ANISOU 4858 CG PHE B 97 1566 1212 1258 7 -67 46 C
ATOM 4859 CD1 PHE B 97 -22.787 -4.873 -1.666 1.00 11.20 C
ANISOU 4859 CD1 PHE B 97 1775 1169 1309 -101 -112 -63 C
ATOM 4860 CE1 PHE B 97 -22.079 -5.240 -0.541 1.00 12.21 C
ANISOU 4860 CE1 PHE B 97 1818 1319 1500 -56 -149 81 C
ATOM 4861 CZ PHE B 97 -21.530 -4.285 0.262 1.00 12.21 C
ANISOU 4861 CZ PHE B 97 1909 1412 1318 -34 -100 -29 C
ATOM 4862 CD2 PHE B 97 -22.404 -2.586 -1.171 1.00 10.68 C
ANISOU 4862 CD2 PHE B 97 1422 1265 1371 -19 5 -19 C
ATOM 4863 CE2 PHE B 97 -21.688 -2.957 -0.047 1.00 11.44 C
ANISOU 4863 CE2 PHE B 97 1566 1375 1403 -12 -102 -47 C
ATOM 4864 C PHE B 97 -23.228 -2.756 -5.790 1.00 9.75 C
ANISOU 4864 C PHE B 97 1415 1122 1166 -112 -158 152 C
ATOM 4865 O PHE B 97 -24.363 -2.272 -5.828 1.00 11.15 O
ANISOU 4865 O PHE B 97 1476 1477 1282 -114 -194 -50 O
ATOM 4866 N PRO B 98 -22.492 -2.852 -6.915 1.00 9.82 N
ANISOU 4866 N PRO B 98 1362 1187 1182 4 -154 225 N
ATOM 4867 CA PRO B 98 -22.914 -2.196 -8.149 1.00 9.72 C
ANISOU 4867 CA PRO B 98 1483 1141 1069 -3 -129 112 C
ATOM 4868 CB PRO B 98 -21.739 -2.385 -9.104 1.00 10.01 C
ANISOU 4868 CB PRO B 98 1359 1288 1155 -191 -76 98 C
ATOM 4869 CG PRO B 98 -21.063 -3.640 -8.573 1.00 10.69 C
ANISOU 4869 CG PRO B 98 1509 1236 1316 -143 -28 56 C
ATOM 4870 CD PRO B 98 -21.214 -3.564 -7.063 1.00 10.01 C
ANISOU 4870 CD PRO B 98 1471 979 1353 -81 -42 -14 C
ATOM 4871 C PRO B 98 -24.199 -2.763 -8.760 1.00 10.56 C
ANISOU 4871 C PRO B 98 1529 1332 1151 -65 -185 165 C
ATOM 4872 O PRO B 98 -24.911 -2.043 -9.433 1.00 11.24 O
ANISOU 4872 O PRO B 98 1588 1151 1529 57 -313 63 O
ATOM 4873 N VAL B 99 -24.522 -4.028 -8.474 1.00 10.14 N
ANISOU 4873 N VAL B 99 1431 1320 1101 -16 -192 219 N
ATOM 4874 CA VAL B 99 -25.748 -4.598 -9.000 1.00 10.41 C
ANISOU 4874 CA VAL B 99 1486 1234 1233 0 -101 119 C
ATOM 4875 CB VAL B 99 -25.709 -6.132 -8.991 1.00 10.46 C
ANISOU 4875 CB VAL B 99 1600 1193 1178 -1 -12 125 C
ATOM 4876 CG1 VAL B 99 -27.083 -6.746 -9.265 1.00 12.41 C
ANISOU 4876 CG1 VAL B 99 1816 1409 1489 -64 -216 -5 C
ATOM 4877 CG2 VAL B 99 -24.674 -6.638 -9.963 1.00 11.76 C
ANISOU 4877 CG2 VAL B 99 1640 1517 1308 -14 15 62 C
ATOM 4878 C VAL B 99 -26.951 -4.027 -8.234 1.00 10.62 C
ANISOU 4878 C VAL B 99 1334 1326 1374 18 -132 162 C
ATOM 4879 O VAL B 99 -27.890 -3.509 -8.851 1.00 10.55 O
ANISOU 4879 O VAL B 99 1540 1181 1285 37 -258 116 O
ATOM 4880 N ASN B 100 -26.931 -4.116 -6.898 1.00 9.86 N
ANISOU 4880 N ASN B 100 1297 1105 1341 27 -195 168 N
ATOM 4881 CA ASN B 100 -28.078 -3.601 -6.143 1.00 10.73 C
ANISOU 4881 CA ASN B 100 1348 1246 1480 86 -140 198 C
ATOM 4882 CB ASN B 100 -28.052 -4.111 -4.703 1.00 10.72 C
ANISOU 4882 CB ASN B 100 1396 1232 1444 19 -138 158 C
ATOM 4883 CG ASN B 100 -28.393 -5.583 -4.627 1.00 11.18 C
ANISOU 4883 CG ASN B 100 1504 1193 1550 54 -239 100 C
ATOM 4884 OD1 ASN B 100 -29.577 -5.932 -4.693 1.00 11.59 O
ANISOU 4884 OD1 ASN B 100 1581 1239 1582 10 -249 248 O
ATOM 4885 ND2 ASN B 100 -27.383 -6.436 -4.495 1.00 11.05 N
ANISOU 4885 ND2 ASN B 100 1690 1150 1356 101 -346 272 N
ATOM 4886 C ASN B 100 -28.189 -2.082 -6.274 1.00 10.65 C
ANISOU 4886 C ASN B 100 1366 1210 1470 26 -199 173 C
ATOM 4887 O ASN B 100 -29.314 -1.551 -6.236 1.00 10.87 O
ANISOU 4887 O ASN B 100 1432 1169 1526 22 -131 89 O
ATOM 4888 N ARG B 101 -27.059 -1.355 -6.385 1.00 10.58 N
ANISOU 4888 N ARG B 101 1351 1153 1514 109 -271 215 N
ATOM 4889 CA AARG B 101 -27.110 0.112 -6.608 0.50 10.87 C
ANISOU 4889 CA AARG B 101 1557 1148 1421 27 -215 146 C
ATOM 4890 CA BARG B 101 -27.123 0.108 -6.605 0.50 11.47 C
ANISOU 4890 CA BARG B 101 1683 1167 1508 67 -271 151 C
ATOM 4891 CB AARG B 101 -25.707 0.711 -6.757 0.50 10.83 C
ANISOU 4891 CB AARG B 101 1579 1125 1411 -29 -196 155 C
ATOM 4892 CB BARG B 101 -25.728 0.711 -6.772 0.50 12.88 C
ANISOU 4892 CB BARG B 101 1794 1273 1825 -50 -197 119 C
ATOM 4893 CG AARG B 101 -24.965 1.027 -5.460 0.50 11.31 C
ANISOU 4893 CG AARG B 101 1575 1340 1380 -43 -157 187 C
ATOM 4894 CG BARG B 101 -24.975 1.001 -5.485 0.50 15.23 C
ANISOU 4894 CG BARG B 101 2103 1759 1922 -25 -265 65 C
ATOM 4895 CD AARG B 101 -23.633 1.771 -5.709 0.50 10.29 C
ANISOU 4895 CD AARG B 101 1477 1184 1246 -36 -289 110 C
ATOM 4896 CD BARG B 101 -23.697 1.735 -5.882 0.50 16.30 C
ANISOU 4896 CD BARG B 101 2100 1816 2275 -136 -300 -69 C
ATOM 4897 NE AARG B 101 -23.729 2.956 -6.560 0.50 10.06 N
ANISOU 4897 NE AARG B 101 1467 1211 1144 -42 -108 127 N
ATOM 4898 NE BARG B 101 -22.886 2.006 -4.729 0.50 18.60 N
ANISOU 4898 NE BARG B 101 2565 2125 2376 -27 -454 -148 N
ATOM 4899 CZ AARG B 101 -23.929 4.205 -6.138 0.50 11.33 C
ANISOU 4899 CZ AARG B 101 1702 1273 1326 31 -188 144 C
ATOM 4900 CZ BARG B 101 -22.913 3.134 -4.053 0.50 19.73 C
ANISOU 4900 CZ BARG B 101 2911 2087 2496 -210 -576 -197 C
ATOM 4901 NH1AARG B 101 -23.946 5.202 -7.014 0.50 12.34 N
ANISOU 4901 NH1AARG B 101 1978 1152 1556 15 -283 177 N
ATOM 4902 NH1BARG B 101 -22.295 3.188 -2.890 0.50 20.44 N
ANISOU 4902 NH1BARG B 101 2762 2417 2587 -200 -624 202 N
ATOM 4903 NH2AARG B 101 -24.136 4.457 -4.862 0.50 11.98 N
ANISOU 4903 NH2AARG B 101 1822 1365 1363 131 -366 -91 N
ATOM 4904 NH2BARG B 101 -23.555 4.191 -4.518 0.50 19.46 N
ANISOU 4904 NH2BARG B 101 2510 1990 2893 -103 -512 -435 N
ATOM 4905 C ARG B 101 -27.901 0.458 -7.875 1.00 11.27 C
ANISOU 4905 C ARG B 101 1503 1344 1433 49 -192 111 C
ATOM 4906 O ARG B 101 -28.368 1.579 -8.003 1.00 12.05 O
ANISOU 4906 O ARG B 101 1749 1297 1531 18 -262 81 O
ATOM 4907 N SER B 102 -27.961 -0.486 -8.818 1.00 10.23 N
ANISOU 4907 N SER B 102 1501 1104 1280 -8 -279 257 N
ATOM 4908 CA SER B 102 -28.544 -0.271 -10.153 1.00 10.42 C
ANISOU 4908 CA SER B 102 1509 1214 1234 -20 -254 191 C
ATOM 4909 CB SER B 102 -27.762 -1.054 -11.179 1.00 10.81 C
ANISOU 4909 CB SER B 102 1587 1330 1188 63 -295 122 C
ATOM 4910 OG SER B 102 -26.445 -0.563 -11.317 1.00 12.20 O
ANISOU 4910 OG SER B 102 1679 1505 1449 -40 -209 243 O
ATOM 4911 C SER B 102 -30.025 -0.649 -10.230 1.00 10.57 C
ANISOU 4911 C SER B 102 1519 1174 1323 -61 -264 208 C
ATOM 4912 O SER B 102 -30.605 -0.639 -11.326 1.00 12.14 O
ANISOU 4912 O SER B 102 1591 1742 1277 126 -138 166 O
ATOM 4913 N ILE B 103 -30.648 -1.019 -9.098 1.00 11.35 N
ANISOU 4913 N ILE B 103 1619 1453 1240 -188 -298 231 N
ATOM 4914 CA ILE B 103 -32.028 -1.530 -9.119 1.00 10.94 C
ANISOU 4914 CA ILE B 103 1637 1197 1321 -71 -170 126 C
ATOM 4915 CB ILE B 103 -32.112 -3.029 -8.814 1.00 11.12 C
ANISOU 4915 CB ILE B 103 1695 1277 1251 -142 -108 231 C
ATOM 4916 CG1 ILE B 103 -31.213 -3.864 -9.732 1.00 11.12 C
ANISOU 4916 CG1 ILE B 103 1541 1268 1413 -254 -139 50 C
ATOM 4917 CG2 ILE B 103 -33.579 -3.462 -8.894 1.00 11.52 C
ANISOU 4917 CG2 ILE B 103 1719 1289 1366 -166 -205 176 C
ATOM 4918 CD1 ILE B 103 -30.985 -5.287 -9.242 1.00 12.66 C
ANISOU 4918 CD1 ILE B 103 1617 1449 1744 -162 -395 93 C
ATOM 4919 C ILE B 103 -32.865 -0.709 -8.141 1.00 11.37 C
ANISOU 4919 C ILE B 103 1616 1267 1437 20 -81 194 C
ATOM 4920 O ILE B 103 -32.894 -0.973 -6.946 1.00 12.62 O
ANISOU 4920 O ILE B 103 1904 1464 1426 77 -121 182 O
ATOM 4921 N PRO B 104 -33.552 0.352 -8.607 1.00 11.63 N
ANISOU 4921 N PRO B 104 1539 1344 1535 105 -91 172 N
ATOM 4922 CA PRO B 104 -34.315 1.160 -7.661 1.00 12.57 C
ANISOU 4922 CA PRO B 104 1658 1438 1677 98 -52 57 C
ATOM 4923 CB PRO B 104 -34.827 2.325 -8.519 1.00 14.72 C
ANISOU 4923 CB PRO B 104 2214 1305 2074 82 190 321 C
ATOM 4924 CG PRO B 104 -34.005 2.334 -9.763 1.00 14.33 C
ANISOU 4924 CG PRO B 104 2319 1558 1567 248 -94 213 C
ATOM 4925 CD PRO B 104 -33.403 0.981 -9.932 1.00 11.85 C
ANISOU 4925 CD PRO B 104 1493 1506 1500 149 -132 155 C
ATOM 4926 C PRO B 104 -35.526 0.445 -7.041 1.00 12.48 C
ANISOU 4926 C PRO B 104 1762 1220 1757 82 -118 105 C
ATOM 4927 O PRO B 104 -35.911 0.738 -5.936 1.00 13.04 O
ANISOU 4927 O PRO B 104 1833 1350 1772 37 -223 0 O
ATOM 4928 N VAL B 105 -36.135 -0.452 -7.813 1.00 12.09 N
ANISOU 4928 N VAL B 105 1684 1208 1701 20 -208 172 N
ATOM 4929 CA AVAL B 105 -37.295 -1.188 -7.373 0.50 11.59 C
ANISOU 4929 CA AVAL B 105 1398 1286 1719 168 -317 203 C
ATOM 4930 CA BVAL B 105 -37.347 -1.162 -7.460 0.50 12.43 C
ANISOU 4930 CA BVAL B 105 1557 1278 1887 135 -202 133 C
ATOM 4931 CB AVAL B 105 -38.617 -0.440 -7.643 0.50 12.71 C
ANISOU 4931 CB AVAL B 105 1426 1606 1797 144 -528 397 C
ATOM 4932 CB BVAL B 105 -38.576 -0.485 -8.088 0.50 14.47 C
ANISOU 4932 CB BVAL B 105 1810 1559 2127 216 -412 158 C
ATOM 4933 CG1AVAL B 105 -38.832 -0.132 -9.115 0.50 13.28 C
ANISOU 4933 CG1AVAL B 105 1633 1665 1747 204 -393 402 C
ATOM 4934 CG1BVAL B 105 -39.866 -1.160 -7.651 0.50 15.19 C
ANISOU 4934 CG1BVAL B 105 1908 1499 2361 255 -223 240 C
ATOM 4935 CG2AVAL B 105 -39.784 -1.196 -7.048 0.50 12.35 C
ANISOU 4935 CG2AVAL B 105 1096 1797 1797 252 -611 415 C
ATOM 4936 CG2BVAL B 105 -38.617 1.005 -7.812 0.50 16.59 C
ANISOU 4936 CG2BVAL B 105 2126 1607 2569 372 -386 93 C
ATOM 4937 C VAL B 105 -37.247 -2.587 -8.006 1.00 11.45 C
ANISOU 4937 C VAL B 105 1498 1256 1593 64 -364 223 C
ATOM 4938 O VAL B 105 -36.832 -2.764 -9.153 1.00 12.99 O
ANISOU 4938 O VAL B 105 2021 1291 1624 103 -362 194 O
ATOM 4939 N ALA B 106 -37.640 -3.570 -7.185 1.00 11.56 N
ANISOU 4939 N ALA B 106 1580 1287 1525 -97 -120 78 N
ATOM 4940 CA ALA B 106 -37.778 -4.945 -7.594 1.00 11.46 C
ANISOU 4940 CA ALA B 106 1570 1319 1465 -65 -128 35 C
ATOM 4941 CB ALA B 106 -36.658 -5.783 -7.036 1.00 12.51 C
ANISOU 4941 CB ALA B 106 1412 1522 1818 -19 -132 -5 C
ATOM 4942 C ALA B 106 -39.123 -5.465 -7.099 1.00 12.08 C
ANISOU 4942 C ALA B 106 1520 1414 1656 -128 -324 32 C
ATOM 4943 O ALA B 106 -39.569 -5.150 -5.982 1.00 12.86 O
ANISOU 4943 O ALA B 106 1573 1592 1721 -200 -201 12 O
ATOM 4944 N VAL B 107 -39.730 -6.294 -7.934 1.00 11.91 N
ANISOU 4944 N VAL B 107 1599 1384 1540 -217 -335 118 N
ATOM 4945 CA VAL B 107 -40.930 -7.045 -7.546 1.00 13.02 C
ANISOU 4945 CA VAL B 107 1696 1473 1777 -222 -152 144 C
ATOM 4946 CB VAL B 107 -42.157 -6.635 -8.378 1.00 15.76 C
ANISOU 4946 CB VAL B 107 1758 1968 2259 -171 -351 108 C
ATOM 4947 CG1 VAL B 107 -43.378 -7.415 -7.917 1.00 16.85 C
ANISOU 4947 CG1 VAL B 107 1358 2690 2354 -159 -350 107 C
ATOM 4948 CG2 VAL B 107 -42.424 -5.143 -8.277 1.00 17.54 C
ANISOU 4948 CG2 VAL B 107 2183 2078 2402 232 -484 229 C
ATOM 4949 C VAL B 107 -40.626 -8.528 -7.713 1.00 12.59 C
ANISOU 4949 C VAL B 107 1668 1494 1621 -203 -66 -1 C
ATOM 4950 O VAL B 107 -40.244 -8.946 -8.789 1.00 15.12 O
ANISOU 4950 O VAL B 107 2541 1468 1733 -16 119 -30 O
ATOM 4951 N ILE B 108 -40.842 -9.288 -6.642 1.00 12.56 N
ANISOU 4951 N ILE B 108 1632 1426 1711 -141 -107 54 N
ATOM 4952 CA ILE B 108 -40.729 -10.730 -6.683 1.00 12.86 C
ANISOU 4952 CA ILE B 108 1631 1438 1815 -177 -10 58 C
ATOM 4953 CB ILE B 108 -39.713 -11.246 -5.644 1.00 12.89 C
ANISOU 4953 CB ILE B 108 1531 1499 1865 -63 84 71 C
ATOM 4954 CG1 ILE B 108 -38.320 -10.686 -5.936 1.00 14.67 C
ANISOU 4954 CG1 ILE B 108 1710 1719 2143 -140 240 32 C
ATOM 4955 CG2 ILE B 108 -39.741 -12.783 -5.604 1.00 13.66 C
ANISOU 4955 CG2 ILE B 108 1775 1546 1867 -131 -47 233 C
ATOM 4956 CD1 ILE B 108 -37.248 -11.139 -5.005 1.00 15.05 C
ANISOU 4956 CD1 ILE B 108 1732 1643 2342 101 291 -42 C
ATOM 4957 C ILE B 108 -42.131 -11.309 -6.454 1.00 13.30 C
ANISOU 4957 C ILE B 108 1623 1567 1861 -248 -148 115 C
ATOM 4958 O ILE B 108 -42.839 -10.912 -5.543 1.00 14.27 O
ANISOU 4958 O ILE B 108 1591 1874 1954 -281 -82 67 O
ATOM 4959 N ASN B 109 -42.513 -12.252 -7.318 1.00 12.87 N
ANISOU 4959 N ASN B 109 1485 1569 1833 -295 -178 155 N
ATOM 4960 CA ASN B 109 -43.771 -12.981 -7.244 1.00 13.35 C
ANISOU 4960 CA ASN B 109 1422 1524 2127 -204 -253 81 C
ATOM 4961 CB ASN B 109 -44.552 -12.825 -8.553 1.00 14.29 C
ANISOU 4961 CB ASN B 109 1566 1674 2186 -58 -352 111 C
ATOM 4962 CG ASN B 109 -45.902 -13.503 -8.574 1.00 13.73 C
ANISOU 4962 CG ASN B 109 1715 1464 2036 -218 -299 118 C
ATOM 4963 OD1 ASN B 109 -46.102 -14.519 -7.914 1.00 15.55 O
ANISOU 4963 OD1 ASN B 109 1862 1965 2081 -491 -290 440 O
ATOM 4964 ND2 ASN B 109 -46.798 -12.964 -9.390 1.00 17.76 N
ANISOU 4964 ND2 ASN B 109 1920 2283 2544 176 -430 205 N
ATOM 4965 C ASN B 109 -43.450 -14.438 -6.942 1.00 12.76 C
ANISOU 4965 C ASN B 109 1131 1608 2109 -80 -63 146 C
ATOM 4966 O ASN B 109 -42.775 -15.076 -7.743 1.00 13.17 O
ANISOU 4966 O ASN B 109 1692 1305 2005 -300 175 74 O
ATOM 4967 N MET B 110 -43.928 -14.930 -5.796 1.00 12.19 N
ANISOU 4967 N MET B 110 1334 1445 1853 -173 -98 -65 N
ATOM 4968 CA MET B 110 -43.889 -16.355 -5.479 1.00 12.41 C
ANISOU 4968 CA MET B 110 1301 1525 1886 -124 -145 -5 C
ATOM 4969 CB MET B 110 -43.092 -16.661 -4.210 1.00 12.66 C
ANISOU 4969 CB MET B 110 1479 1563 1767 -170 -144 -109 C
ATOM 4970 CG MET B 110 -41.605 -16.310 -4.345 1.00 13.06 C
ANISOU 4970 CG MET B 110 1449 1670 1843 -60 -199 150 C
ATOM 4971 SD MET B 110 -40.705 -16.721 -2.846 1.00 14.06 S
ANISOU 4971 SD MET B 110 1843 1736 1762 -295 -223 44 S
ATOM 4972 CE MET B 110 -39.029 -16.408 -3.407 1.00 14.90 C
ANISOU 4972 CE MET B 110 1573 2077 2009 -74 -421 222 C
ATOM 4973 C MET B 110 -45.331 -16.844 -5.329 1.00 12.13 C
ANISOU 4973 C MET B 110 1265 1476 1866 -176 -202 28 C
ATOM 4974 O MET B 110 -46.060 -16.396 -4.431 1.00 12.97 O
ANISOU 4974 O MET B 110 1302 1718 1909 -138 -134 32 O
ATOM 4975 N ASN B 111 -45.752 -17.735 -6.240 1.00 13.02 N
ANISOU 4975 N ASN B 111 1446 1618 1880 -250 -32 -33 N
ATOM 4976 CA ASN B 111 -47.077 -18.358 -6.166 1.00 13.69 C
ANISOU 4976 CA ASN B 111 1510 1711 1977 -288 -92 107 C
ATOM 4977 CB ASN B 111 -47.143 -19.449 -5.083 1.00 14.25 C
ANISOU 4977 CB ASN B 111 1784 1635 1994 -366 1 105 C
ATOM 4978 CG ASN B 111 -46.288 -20.646 -5.429 1.00 13.67 C
ANISOU 4978 CG ASN B 111 1649 1621 1921 -532 63 38 C
ATOM 4979 OD1 ASN B 111 -45.805 -20.750 -6.573 1.00 14.32 O
ANISOU 4979 OD1 ASN B 111 2062 1425 1952 -378 146 234 O
ATOM 4980 ND2 ASN B 111 -46.073 -21.523 -4.439 1.00 13.18 N
ANISOU 4980 ND2 ASN B 111 1631 1634 1740 -461 49 -103 N
ATOM 4981 C ASN B 111 -48.194 -17.309 -6.008 1.00 14.07 C
ANISOU 4981 C ASN B 111 1566 1668 2112 -252 -238 -52 C
ATOM 4982 O ASN B 111 -49.178 -17.542 -5.302 1.00 16.24 O
ANISOU 4982 O ASN B 111 1869 1908 2392 -202 -106 91 O
ATOM 4983 N GLY B 112 -48.063 -16.189 -6.719 1.00 13.19 N
ANISOU 4983 N GLY B 112 1235 1637 2137 -294 -356 -51 N
ATOM 4984 CA GLY B 112 -49.080 -15.154 -6.786 1.00 15.75 C
ANISOU 4984 CA GLY B 112 1499 2058 2426 -65 -407 -120 C
ATOM 4985 C GLY B 112 -48.960 -14.059 -5.743 1.00 15.19 C
ANISOU 4985 C GLY B 112 1489 1780 2500 -99 -415 16 C
ATOM 4986 O GLY B 112 -49.702 -13.101 -5.817 1.00 19.05 O
ANISOU 4986 O GLY B 112 1946 2194 3097 353 -537 4 O
ATOM 4987 N LYS B 113 -48.074 -14.224 -4.754 1.00 14.30 N
ANISOU 4987 N LYS B 113 1307 1859 2266 -256 -275 -84 N
ATOM 4988 CA LYS B 113 -47.824 -13.206 -3.754 1.00 14.84 C
ANISOU 4988 CA LYS B 113 1548 1921 2169 -187 -5 -87 C
ATOM 4989 CB LYS B 113 -47.435 -13.831 -2.412 1.00 15.83 C
ANISOU 4989 CB LYS B 113 1883 2157 1972 -251 128 -147 C
ATOM 4990 CG LYS B 113 -46.954 -12.827 -1.361 1.00 16.30 C
ANISOU 4990 CG LYS B 113 2106 1980 2105 -358 166 -156 C
ATOM 4991 CD LYS B 113 -48.000 -11.852 -0.920 1.00 21.07 C
ANISOU 4991 CD LYS B 113 2961 2482 2563 -77 542 -143 C
ATOM 4992 CE LYS B 113 -47.445 -10.926 0.145 1.00 22.98 C
ANISOU 4992 CE LYS B 113 3839 2410 2481 34 398 -183 C
ATOM 4993 NZ LYS B 113 -48.429 -9.887 0.520 1.00 29.68 N
ANISOU 4993 NZ LYS B 113 4641 3392 3241 411 1029 -648 N
ATOM 4994 C LYS B 113 -46.685 -12.322 -4.259 1.00 15.09 C
ANISOU 4994 C LYS B 113 1563 1999 2171 -254 -153 8 C
ATOM 4995 O LYS B 113 -45.609 -12.822 -4.554 1.00 14.42 O
ANISOU 4995 O LYS B 113 1613 1868 1997 -150 -213 73 O
ATOM 4996 N THR B 114 -46.940 -11.012 -4.324 1.00 15.17 N
ANISOU 4996 N THR B 114 1513 1921 2330 -244 18 -32 N
ATOM 4997 CA THR B 114 -45.901 -10.083 -4.740 1.00 14.57 C
ANISOU 4997 CA THR B 114 1630 1686 2217 -218 -120 48 C
ATOM 4998 CB THR B 114 -46.398 -9.046 -5.740 1.00 16.63 C
ANISOU 4998 CB THR B 114 1816 2056 2444 1 -320 168 C
ATOM 4999 OG1 THR B 114 -47.373 -8.233 -5.093 1.00 18.72 O
ANISOU 4999 OG1 THR B 114 1872 2153 3087 258 -247 292 O
ATOM 5000 CG2 THR B 114 -47.007 -9.669 -6.969 1.00 16.69 C
ANISOU 5000 CG2 THR B 114 1755 2046 2537 -151 -588 369 C
ATOM 5001 C THR B 114 -45.269 -9.392 -3.530 1.00 13.85 C
ANISOU 5001 C THR B 114 1481 1677 2103 -160 -113 36 C
ATOM 5002 O THR B 114 -45.926 -9.035 -2.537 1.00 17.05 O
ANISOU 5002 O THR B 114 1639 2187 2651 -294 278 -360 O
ATOM 5003 N PHE B 115 -43.969 -9.187 -3.658 1.00 13.23 N
ANISOU 5003 N PHE B 115 1465 1617 1944 56 -17 71 N
ATOM 5004 CA PHE B 115 -43.151 -8.474 -2.688 1.00 13.05 C
ANISOU 5004 CA PHE B 115 1573 1574 1808 -104 9 53 C
ATOM 5005 CB PHE B 115 -42.085 -9.401 -2.093 1.00 13.71 C
ANISOU 5005 CB PHE B 115 1762 1655 1792 -93 -96 76 C
ATOM 5006 CG PHE B 115 -42.580 -10.687 -1.492 1.00 14.82 C
ANISOU 5006 CG PHE B 115 2173 1576 1882 -188 -188 0 C
ATOM 5007 CD1 PHE B 115 -42.747 -11.828 -2.264 1.00 14.37 C
ANISOU 5007 CD1 PHE B 115 2082 1531 1846 -146 -285 64 C
ATOM 5008 CE1 PHE B 115 -43.185 -13.015 -1.703 1.00 14.80 C
ANISOU 5008 CE1 PHE B 115 2008 1739 1874 -111 -417 149 C
ATOM 5009 CZ PHE B 115 -43.426 -13.080 -0.369 1.00 16.90 C
ANISOU 5009 CZ PHE B 115 2412 1968 2040 -349 -175 344 C
ATOM 5010 CD2 PHE B 115 -42.786 -10.793 -0.132 1.00 19.75 C
ANISOU 5010 CD2 PHE B 115 3343 2069 2090 -428 2 -89 C
ATOM 5011 CE2 PHE B 115 -43.202 -11.991 0.422 1.00 20.39 C
ANISOU 5011 CE2 PHE B 115 3504 2205 2036 -407 59 119 C
ATOM 5012 C PHE B 115 -42.437 -7.348 -3.439 1.00 12.29 C
ANISOU 5012 C PHE B 115 1618 1380 1671 -11 -125 83 C
ATOM 5013 O PHE B 115 -41.670 -7.633 -4.375 1.00 13.37 O
ANISOU 5013 O PHE B 115 1952 1485 1643 -118 50 -26 O
ATOM 5014 N THR B 116 -42.717 -6.103 -3.054 1.00 12.63 N
ANISOU 5014 N THR B 116 1633 1423 1742 -98 102 -36 N
ATOM 5015 CA THR B 116 -42.102 -4.938 -3.681 1.00 12.58 C
ANISOU 5015 CA THR B 116 1408 1439 1933 -57 -23 53 C
ATOM 5016 CB THR B 116 -43.160 -3.901 -4.078 1.00 14.85 C
ANISOU 5016 CB THR B 116 1606 1620 2414 92 -55 144 C
ATOM 5017 OG1 THR B 116 -44.090 -4.526 -4.973 1.00 17.53 O
ANISOU 5017 OG1 THR B 116 1819 2066 2774 121 -121 -72 O
ATOM 5018 CG2 THR B 116 -42.532 -2.692 -4.731 1.00 16.92 C
ANISOU 5018 CG2 THR B 116 1962 1699 2767 -74 -178 232 C
ATOM 5019 C THR B 116 -41.076 -4.357 -2.714 1.00 13.49 C
ANISOU 5019 C THR B 116 1632 1495 1996 -183 -10 2 C
ATOM 5020 O THR B 116 -41.402 -4.077 -1.553 1.00 16.63 O
ANISOU 5020 O THR B 116 2075 2081 2159 -383 47 -333 O
ATOM 5021 N SER B 117 -39.843 -4.225 -3.194 1.00 12.45 N
ANISOU 5021 N SER B 117 1533 1452 1742 -164 -135 -62 N
ATOM 5022 CA ASER B 117 -38.805 -3.652 -2.371 0.50 11.82 C
ANISOU 5022 CA ASER B 117 1403 1363 1724 -32 -169 0 C
ATOM 5023 CA BSER B 117 -38.678 -3.795 -2.414 0.50 12.87 C
ANISOU 5023 CA BSER B 117 1562 1547 1780 -206 -145 -30 C
ATOM 5024 CB ASER B 117 -38.077 -4.738 -1.625 0.50 11.29 C
ANISOU 5024 CB ASER B 117 1300 1324 1662 1 -122 -15 C
ATOM 5025 CB BSER B 117 -37.743 -4.940 -2.078 0.50 14.16 C
ANISOU 5025 CB BSER B 117 1808 1713 1857 -27 -261 -115 C
ATOM 5026 OG ASER B 117 -37.352 -5.539 -2.520 0.50 11.74 O
ANISOU 5026 OG ASER B 117 1094 1373 1993 317 -132 50 O
ATOM 5027 OG BSER B 117 -38.376 -5.985 -1.385 0.50 17.36 O
ANISOU 5027 OG BSER B 117 2324 1924 2347 -113 -77 -69 O
ATOM 5028 C SER B 117 -37.887 -2.776 -3.228 1.00 11.57 C
ANISOU 5028 C SER B 117 1497 1217 1680 -86 -307 43 C
ATOM 5029 O SER B 117 -38.090 -2.655 -4.443 1.00 11.93 O
ANISOU 5029 O SER B 117 1654 1145 1732 149 -214 30 O
ATOM 5030 N TYR B 118 -36.903 -2.149 -2.565 1.00 11.49 N
ANISOU 5030 N TYR B 118 1397 1223 1742 -116 -209 29 N
ATOM 5031 CA TYR B 118 -36.120 -1.058 -3.151 1.00 11.16 C
ANISOU 5031 CA TYR B 118 1425 1279 1534 -67 -148 105 C
ATOM 5032 CB TYR B 118 -36.591 0.269 -2.548 1.00 12.03 C
ANISOU 5032 CB TYR B 118 1531 1384 1654 118 -103 92 C
ATOM 5033 CG TYR B 118 -38.072 0.467 -2.730 1.00 13.87 C
ANISOU 5033 CG TYR B 118 1612 1506 2150 312 -95 -51 C
ATOM 5034 CD1 TYR B 118 -38.617 0.841 -3.942 1.00 15.27 C
ANISOU 5034 CD1 TYR B 118 1714 1867 2217 300 -50 47 C
ATOM 5035 CE1 TYR B 118 -39.986 0.964 -4.111 1.00 17.51 C
ANISOU 5035 CE1 TYR B 118 1732 2215 2703 550 -132 27 C
ATOM 5036 CZ TYR B 118 -40.848 0.649 -3.072 1.00 18.98 C
ANISOU 5036 CZ TYR B 118 1774 2470 2965 348 -54 -125 C
ATOM 5037 OH TYR B 118 -42.208 0.737 -3.241 1.00 23.80 O
ANISOU 5037 OH TYR B 118 1882 2813 4348 440 -222 -301 O
ATOM 5038 CE2 TYR B 118 -40.321 0.206 -1.878 1.00 18.65 C
ANISOU 5038 CE2 TYR B 118 1781 2407 2896 161 256 84 C
ATOM 5039 CD2 TYR B 118 -38.946 0.124 -1.720 1.00 17.01 C
ANISOU 5039 CD2 TYR B 118 1845 1982 2637 257 126 237 C
ATOM 5040 C TYR B 118 -34.635 -1.353 -2.939 1.00 11.50 C
ANISOU 5040 C TYR B 118 1528 1215 1626 -9 -237 156 C
ATOM 5041 O TYR B 118 -34.019 -0.863 -1.972 1.00 12.44 O
ANISOU 5041 O TYR B 118 1826 1271 1629 -62 -292 104 O
ATOM 5042 N PRO B 119 -34.021 -2.192 -3.803 1.00 11.11 N
ANISOU 5042 N PRO B 119 1319 1383 1518 -168 -204 105 N
ATOM 5043 CA PRO B 119 -32.674 -2.679 -3.532 1.00 11.17 C
ANISOU 5043 CA PRO B 119 1512 1323 1406 83 -165 199 C
ATOM 5044 CB PRO B 119 -32.392 -3.558 -4.741 1.00 10.84 C
ANISOU 5044 CB PRO B 119 1425 1230 1463 191 -196 200 C
ATOM 5045 CG PRO B 119 -33.752 -4.093 -5.122 1.00 11.29 C
ANISOU 5045 CG PRO B 119 1473 1360 1456 89 -161 128 C
ATOM 5046 CD PRO B 119 -34.662 -2.895 -4.941 1.00 11.35 C
ANISOU 5046 CD PRO B 119 1537 1298 1476 62 -255 65 C
ATOM 5047 C PRO B 119 -31.625 -1.568 -3.350 1.00 11.41 C
ANISOU 5047 C PRO B 119 1496 1272 1565 164 -163 84 C
ATOM 5048 O PRO B 119 -30.798 -1.661 -2.459 1.00 11.94 O
ANISOU 5048 O PRO B 119 1574 1503 1458 33 -169 84 O
ATOM 5049 N ALA B 120 -31.654 -0.540 -4.216 1.00 10.68 N
ANISOU 5049 N ALA B 120 1214 1283 1560 233 -207 106 N
ATOM 5050 CA ALA B 120 -30.639 0.508 -4.101 1.00 12.08 C
ANISOU 5050 CA ALA B 120 1487 1371 1732 86 -246 -24 C
ATOM 5051 CB ALA B 120 -30.763 1.472 -5.243 1.00 13.22 C
ANISOU 5051 CB ALA B 120 1990 1162 1869 -23 -266 10 C
ATOM 5052 C ALA B 120 -30.727 1.222 -2.743 1.00 12.64 C
ANISOU 5052 C ALA B 120 1659 1424 1718 212 -246 22 C
ATOM 5053 O ALA B 120 -29.701 1.526 -2.124 1.00 14.72 O
ANISOU 5053 O ALA B 120 1789 2008 1792 53 -250 -215 O
ATOM 5054 N GLN B 121 -31.949 1.500 -2.307 1.00 13.14 N
ANISOU 5054 N GLN B 121 1628 1600 1764 44 -253 -199 N
ATOM 5055 CA GLN B 121 -32.185 2.164 -1.032 1.00 13.50 C
ANISOU 5055 CA GLN B 121 1687 1623 1818 196 -259 -322 C
ATOM 5056 CB GLN B 121 -33.666 2.540 -0.912 1.00 14.86 C
ANISOU 5056 CB GLN B 121 1766 1775 2104 303 -221 -316 C
ATOM 5057 CG GLN B 121 -34.059 3.204 0.390 1.00 16.00 C
ANISOU 5057 CG GLN B 121 2130 1987 1961 329 -124 -118 C
ATOM 5058 CD GLN B 121 -35.527 3.521 0.378 1.00 16.14 C
ANISOU 5058 CD GLN B 121 2106 1865 2159 355 40 -417 C
ATOM 5059 OE1 GLN B 121 -36.364 2.633 0.533 1.00 17.88 O
ANISOU 5059 OE1 GLN B 121 1798 2094 2901 234 -98 -248 O
ATOM 5060 NE2 GLN B 121 -35.847 4.789 0.192 1.00 18.01 N
ANISOU 5060 NE2 GLN B 121 2600 1955 2288 640 -88 -367 N
ATOM 5061 C GLN B 121 -31.734 1.243 0.112 1.00 13.74 C
ANISOU 5061 C GLN B 121 1470 1904 1846 246 -289 -234 C
ATOM 5062 O GLN B 121 -31.118 1.704 1.084 1.00 15.60 O
ANISOU 5062 O GLN B 121 1973 2147 1807 185 -226 -535 O
ATOM 5063 N LEU B 122 -32.092 -0.055 0.011 1.00 13.50 N
ANISOU 5063 N LEU B 122 1691 1850 1589 193 -245 -179 N
ATOM 5064 CA ALEU B 122 -31.797 -1.057 1.052 0.50 14.90 C
ANISOU 5064 CA ALEU B 122 1764 2266 1630 319 -145 -18 C
ATOM 5065 CA BLEU B 122 -31.791 -1.011 1.065 0.50 14.45 C
ANISOU 5065 CA BLEU B 122 1781 2101 1607 264 -115 -71 C
ATOM 5066 CB ALEU B 122 -32.355 -2.439 0.681 0.50 16.47 C
ANISOU 5066 CB ALEU B 122 1794 2442 2019 142 -151 115 C
ATOM 5067 CB BLEU B 122 -32.458 -2.350 0.751 0.50 15.89 C
ANISOU 5067 CB BLEU B 122 1959 2186 1891 101 -42 21 C
ATOM 5068 CG ALEU B 122 -33.844 -2.746 0.871 0.50 17.32 C
ANISOU 5068 CG ALEU B 122 1692 2760 2128 433 -94 152 C
ATOM 5069 CG BLEU B 122 -32.929 -3.133 1.968 0.50 16.93 C
ANISOU 5069 CG BLEU B 122 2373 2093 1964 268 76 29 C
ATOM 5070 CD1ALEU B 122 -34.229 -4.058 0.182 0.50 19.09 C
ANISOU 5070 CD1ALEU B 122 2079 2592 2582 450 231 286 C
ATOM 5071 CD1BLEU B 122 -33.833 -4.282 1.579 0.50 16.36 C
ANISOU 5071 CD1BLEU B 122 2268 1950 1998 333 24 160 C
ATOM 5072 CD2ALEU B 122 -34.219 -2.834 2.338 0.50 18.66 C
ANISOU 5072 CD2ALEU B 122 1998 3051 2038 254 -241 31 C
ATOM 5073 CD2BLEU B 122 -31.750 -3.595 2.777 0.50 18.40 C
ANISOU 5073 CD2BLEU B 122 2219 2418 2353 64 -22 75 C
ATOM 5074 C LEU B 122 -30.272 -1.157 1.213 1.00 13.87 C
ANISOU 5074 C LEU B 122 1724 2081 1462 243 -89 65 C
ATOM 5075 O LEU B 122 -29.735 -1.093 2.328 1.00 14.12 O
ANISOU 5075 O LEU B 122 1476 2274 1611 102 -149 -177 O
ATOM 5076 N ILE B 123 -29.565 -1.337 0.099 1.00 12.57 N
ANISOU 5076 N ILE B 123 1329 1971 1474 95 -148 -132 N
ATOM 5077 CA ILE B 123 -28.120 -1.618 0.201 1.00 12.27 C
ANISOU 5077 CA ILE B 123 1346 1816 1498 214 -32 27 C
ATOM 5078 CB ILE B 123 -27.522 -2.201 -1.105 1.00 12.84 C
ANISOU 5078 CB ILE B 123 1456 1798 1623 118 31 -93 C
ATOM 5079 CG1 ILE B 123 -26.168 -2.867 -0.860 1.00 13.56 C
ANISOU 5079 CG1 ILE B 123 1583 1990 1576 232 149 -30 C
ATOM 5080 CG2 ILE B 123 -27.430 -1.159 -2.210 1.00 14.21 C
ANISOU 5080 CG2 ILE B 123 1706 2112 1580 182 94 -50 C
ATOM 5081 CD1 ILE B 123 -26.147 -3.953 0.213 1.00 14.60 C
ANISOU 5081 CD1 ILE B 123 1748 1931 1869 347 279 -24 C
ATOM 5082 C ILE B 123 -27.358 -0.385 0.698 1.00 13.56 C
ANISOU 5082 C ILE B 123 1390 2047 1713 195 28 -206 C
ATOM 5083 O ILE B 123 -26.342 -0.530 1.380 1.00 13.38 O
ANISOU 5083 O ILE B 123 1568 1913 1601 138 11 -53 O
ATOM 5084 N LYS B 124 -27.822 0.814 0.355 1.00 14.70 N
ANISOU 5084 N LYS B 124 1768 2009 1808 165 -356 -61 N
ATOM 5085 CA LYS B 124 -27.123 2.039 0.793 1.00 15.87 C
ANISOU 5085 CA LYS B 124 1901 1968 2159 103 -353 -95 C
ATOM 5086 CB LYS B 124 -27.765 3.331 0.264 1.00 19.08 C
ANISOU 5086 CB LYS B 124 2552 2030 2667 -43 -626 314 C
ATOM 5087 CG LYS B 124 -27.067 4.631 0.691 1.00 21.02 C
ANISOU 5087 CG LYS B 124 2814 2362 2810 -183 -582 5 C
ATOM 5088 CD LYS B 124 -27.635 5.924 0.102 1.00 24.53 C
ANISOU 5088 CD LYS B 124 3177 2251 3889 -123 -445 59 C
ATOM 5089 CE LYS B 124 -26.771 7.141 0.439 1.00 24.97 C
ANISOU 5089 CE LYS B 124 3731 2235 3518 -225 -393 -182 C
ATOM 5090 NZ LYS B 124 -27.311 8.424 -0.091 1.00 29.49 N
ANISOU 5090 NZ LYS B 124 4558 2585 4061 -366 -766 211 N
ATOM 5091 C LYS B 124 -27.075 2.085 2.321 1.00 15.68 C
ANISOU 5091 C LYS B 124 1974 1753 2228 277 -336 -210 C
ATOM 5092 O LYS B 124 -26.100 2.602 2.886 1.00 16.69 O
ANISOU 5092 O LYS B 124 1941 1980 2421 156 -195 -564 O
ATOM 5093 N LEU B 125 -28.136 1.606 2.980 1.00 15.13 N
ANISOU 5093 N LEU B 125 1745 1783 2220 257 -265 -325 N
ATOM 5094 CA ALEU B 125 -28.182 1.561 4.436 0.50 16.88 C
ANISOU 5094 CA ALEU B 125 2099 2150 2162 184 -154 -488 C
ATOM 5095 CA BLEU B 125 -28.187 1.544 4.454 0.50 16.79 C
ANISOU 5095 CA BLEU B 125 1937 2242 2197 261 -35 -502 C
ATOM 5096 CB ALEU B 125 -29.661 1.585 4.813 0.50 17.82 C
ANISOU 5096 CB ALEU B 125 2176 2240 2355 64 -194 -541 C
ATOM 5097 CB BLEU B 125 -29.622 1.432 4.963 0.50 18.84 C
ANISOU 5097 CB BLEU B 125 2041 2529 2586 186 78 -561 C
ATOM 5098 CG ALEU B 125 -29.991 1.706 6.278 0.50 18.11 C
ANISOU 5098 CG ALEU B 125 2457 2234 2187 177 -334 -367 C
ATOM 5099 CG BLEU B 125 -30.407 2.715 5.021 0.50 19.42 C
ANISOU 5099 CG BLEU B 125 2090 2714 2573 385 224 -525 C
ATOM 5100 CD1ALEU B 125 -29.472 3.021 6.809 0.50 17.86 C
ANISOU 5100 CD1ALEU B 125 2460 2282 2043 56 -363 -274 C
ATOM 5101 CD1BLEU B 125 -31.823 2.393 5.416 0.50 19.94 C
ANISOU 5101 CD1BLEU B 125 2061 2796 2717 383 236 -716 C
ATOM 5102 CD2ALEU B 125 -31.492 1.577 6.476 0.50 18.34 C
ANISOU 5102 CD2ALEU B 125 2475 2514 1979 106 -216 -364 C
ATOM 5103 CD2BLEU B 125 -29.758 3.632 6.026 0.50 19.63 C
ANISOU 5103 CD2BLEU B 125 1951 2684 2823 566 164 -667 C
ATOM 5104 C LEU B 125 -27.456 0.314 4.966 1.00 14.75 C
ANISOU 5104 C LEU B 125 1702 2079 1822 48 -24 -452 C
ATOM 5105 O LEU B 125 -26.649 0.415 5.895 1.00 15.52 O
ANISOU 5105 O LEU B 125 1672 2388 1837 -12 -106 -510 O
ATOM 5106 N HIS B 126 -27.793 -0.854 4.387 1.00 13.90 N
ANISOU 5106 N HIS B 126 1574 2159 1547 0 -120 -330 N
ATOM 5107 CA HIS B 126 -27.323 -2.141 4.868 1.00 13.83 C
ANISOU 5107 CA HIS B 126 1689 2098 1468 -176 -125 -80 C
ATOM 5108 CB HIS B 126 -27.916 -3.248 3.995 1.00 14.67 C
ANISOU 5108 CB HIS B 126 1842 2046 1684 -161 -357 39 C
ATOM 5109 CG HIS B 126 -27.589 -4.631 4.422 1.00 14.42 C
ANISOU 5109 CG HIS B 126 1784 2027 1667 -279 -301 161 C
ATOM 5110 ND1 HIS B 126 -28.039 -5.132 5.615 1.00 17.40 N
ANISOU 5110 ND1 HIS B 126 2096 2303 2212 -299 -37 538 N
ATOM 5111 CE1 HIS B 126 -27.624 -6.379 5.740 1.00 18.44 C
ANISOU 5111 CE1 HIS B 126 2647 2052 2306 -374 -117 369 C
ATOM 5112 NE2 HIS B 126 -26.936 -6.714 4.622 1.00 17.03 N
ANISOU 5112 NE2 HIS B 126 2028 2175 2265 -538 -393 201 N
ATOM 5113 CD2 HIS B 126 -26.910 -5.624 3.801 1.00 15.29 C
ANISOU 5113 CD2 HIS B 126 1912 2046 1849 -405 -310 56 C
ATOM 5114 C HIS B 126 -25.797 -2.215 4.880 1.00 13.16 C
ANISOU 5114 C HIS B 126 1755 1754 1490 -43 -230 136 C
ATOM 5115 O HIS B 126 -25.206 -2.849 5.724 1.00 14.35 O
ANISOU 5115 O HIS B 126 1792 2058 1602 -239 -407 388 O
ATOM 5116 N GLN B 127 -25.147 -1.574 3.909 1.00 11.85 N
ANISOU 5116 N GLN B 127 1535 1510 1456 99 -104 83 N
ATOM 5117 CA GLN B 127 -23.698 -1.659 3.798 1.00 11.96 C
ANISOU 5117 CA GLN B 127 1503 1540 1500 19 -235 19 C
ATOM 5118 CB GLN B 127 -23.218 -0.971 2.521 1.00 12.96 C
ANISOU 5118 CB GLN B 127 1633 1709 1580 -12 -92 64 C
ATOM 5119 CG GLN B 127 -23.367 0.547 2.547 1.00 13.08 C
ANISOU 5119 CG GLN B 127 1809 1633 1528 -25 -1 44 C
ATOM 5120 CD GLN B 127 -23.043 1.235 1.247 1.00 15.03 C
ANISOU 5120 CD GLN B 127 2199 1931 1578 69 -60 98 C
ATOM 5121 OE1 GLN B 127 -22.365 0.667 0.396 1.00 15.26 O
ANISOU 5121 OE1 GLN B 127 2328 1757 1713 0 129 179 O
ATOM 5122 NE2 GLN B 127 -23.532 2.463 1.085 1.00 16.24 N
ANISOU 5122 NE2 GLN B 127 2503 1683 1983 -188 -558 162 N
ATOM 5123 C GLN B 127 -22.997 -1.104 5.040 1.00 12.61 C
ANISOU 5123 C GLN B 127 1694 1465 1631 -134 -214 -25 C
ATOM 5124 O GLN B 127 -21.859 -1.467 5.279 1.00 13.04 O
ANISOU 5124 O GLN B 127 1874 1485 1593 47 -449 -4 O
ATOM 5125 N TYR B 128 -23.676 -0.237 5.793 1.00 12.21 N
ANISOU 5125 N TYR B 128 1457 1732 1449 -168 -114 -32 N
ATOM 5126 CA TYR B 128 -23.045 0.418 6.958 1.00 13.14 C
ANISOU 5126 CA TYR B 128 1657 1850 1483 -148 -107 -147 C
ATOM 5127 CB TYR B 128 -23.552 1.844 7.147 1.00 13.59 C
ANISOU 5127 CB TYR B 128 1693 1975 1496 -108 45 -287 C
ATOM 5128 CG TYR B 128 -23.090 2.784 6.072 1.00 13.58 C
ANISOU 5128 CG TYR B 128 1880 1726 1551 -45 77 -352 C
ATOM 5129 CD1 TYR B 128 -21.762 3.170 5.995 1.00 14.13 C
ANISOU 5129 CD1 TYR B 128 1937 1901 1528 -19 6 -383 C
ATOM 5130 CE1 TYR B 128 -21.330 4.037 5.009 1.00 13.22 C
ANISOU 5130 CE1 TYR B 128 1732 1615 1674 -38 70 -401 C
ATOM 5131 CZ TYR B 128 -22.239 4.554 4.098 1.00 14.54 C
ANISOU 5131 CZ TYR B 128 1866 1680 1975 45 -4 -216 C
ATOM 5132 OH TYR B 128 -21.837 5.422 3.115 1.00 16.89 O
ANISOU 5132 OH TYR B 128 2030 2095 2291 29 249 66 O
ATOM 5133 CE2 TYR B 128 -23.567 4.187 4.174 1.00 15.05 C
ANISOU 5133 CE2 TYR B 128 1987 1690 2041 -42 156 -140 C
ATOM 5134 CD2 TYR B 128 -23.982 3.295 5.143 1.00 13.93 C
ANISOU 5134 CD2 TYR B 128 1819 1648 1822 -141 -9 -263 C
ATOM 5135 C TYR B 128 -23.228 -0.333 8.265 1.00 14.28 C
ANISOU 5135 C TYR B 128 1748 2156 1519 79 -5 -132 C
ATOM 5136 O TYR B 128 -22.588 0.026 9.247 1.00 15.85 O
ANISOU 5136 O TYR B 128 2269 2206 1546 203 -237 -376 O
ATOM 5137 N ASN B 129 -24.124 -1.307 8.345 1.00 15.95 N
ANISOU 5137 N ASN B 129 1903 2335 1820 -193 28 275 N
ATOM 5138 CA ASN B 129 -24.176 -1.972 9.669 1.00 16.32 C
ANISOU 5138 CA ASN B 129 2013 2365 1823 -141 377 305 C
ATOM 5139 CB ASN B 129 -25.203 -1.380 10.624 1.00 18.15 C
ANISOU 5139 CB ASN B 129 2137 2401 2356 -8 438 227 C
ATOM 5140 CG ASN B 129 -26.593 -1.829 10.311 1.00 18.30 C
ANISOU 5140 CG ASN B 129 2501 2285 2166 -167 262 59 C
ATOM 5141 OD1 ASN B 129 -26.900 -2.118 9.144 1.00 20.46 O
ANISOU 5141 OD1 ASN B 129 3221 2460 2091 305 199 -78 O
ATOM 5142 ND2 ASN B 129 -27.430 -1.808 11.340 1.00 18.22 N
ANISOU 5142 ND2 ASN B 129 2718 2033 2168 387 483 413 N
ATOM 5143 C ASN B 129 -24.312 -3.487 9.595 1.00 15.89 C
ANISOU 5143 C ASN B 129 2023 2371 1643 -261 418 44 C
ATOM 5144 O ASN B 129 -24.480 -4.106 10.635 1.00 18.42 O
ANISOU 5144 O ASN B 129 3030 1966 2001 -177 217 370 O
ATOM 5145 N ALA B 130 -24.055 -4.067 8.433 1.00 16.64 N
ANISOU 5145 N ALA B 130 2679 2229 1413 -596 134 22 N
ATOM 5146 CA ALA B 130 -24.004 -5.493 8.274 1.00 18.56 C
ANISOU 5146 CA ALA B 130 3146 2265 1641 -798 69 176 C
ATOM 5147 CB ALA B 130 -24.336 -5.845 6.849 1.00 18.84 C
ANISOU 5147 CB ALA B 130 2982 2328 1846 -766 -347 148 C
ATOM 5148 C ALA B 130 -22.617 -6.008 8.639 1.00 19.10 C
ANISOU 5148 C ALA B 130 3740 2057 1458 -477 -169 306 C
ATOM 5149 O ALA B 130 -21.641 -5.277 8.721 1.00 21.68 O
ANISOU 5149 O ALA B 130 3561 2181 2493 -545 -592 143 O
ATOM 5150 N ASP B 131 -22.554 -7.314 8.845 1.00 21.69 N
ANISOU 5150 N ASP B 131 4608 2116 1515 -482 -230 134 N
ATOM 5151 CA ASP B 131 -21.324 -8.005 9.051 1.00 22.65 C
ANISOU 5151 CA ASP B 131 4774 2221 1609 29 -567 194 C
ATOM 5152 CB ASP B 131 -21.669 -9.430 9.462 1.00 26.49 C
ANISOU 5152 CB ASP B 131 5710 2192 2161 391 -76 322 C
ATOM 5153 CG ASP B 131 -20.445 -10.285 9.724 1.00 31.15 C
ANISOU 5153 CG ASP B 131 6424 2636 2772 1206 -344 1095 C
ATOM 5154 OD1 ASP B 131 -19.319 -9.826 9.438 1.00 32.91 O
ANISOU 5154 OD1 ASP B 131 6905 3169 2427 1013 243 761 O
ATOM 5155 OD2 ASP B 131 -20.634 -11.389 10.236 1.00 40.98 O
ANISOU 5155 OD2 ASP B 131 8608 2684 4278 908 344 1104 O
ATOM 5156 C ASP B 131 -20.482 -7.940 7.774 1.00 21.81 C
ANISOU 5156 C ASP B 131 4286 2137 1864 46 -821 134 C
ATOM 5157 O ASP B 131 -20.908 -8.405 6.741 1.00 20.06 O
ANISOU 5157 O ASP B 131 4065 1838 1719 -92 -747 182 O
ATOM 5158 N PRO B 132 -19.264 -7.353 7.771 1.00 23.53 N
ANISOU 5158 N PRO B 132 4124 2499 2315 -66 -1347 -82 N
ATOM 5159 CA PRO B 132 -18.464 -7.282 6.542 1.00 23.89 C
ANISOU 5159 CA PRO B 132 3664 2603 2808 111 -1002 -60 C
ATOM 5160 CB PRO B 132 -17.182 -6.571 6.998 1.00 29.16 C
ANISOU 5160 CB PRO B 132 4212 3331 3536 -117 -1204 -455 C
ATOM 5161 CG PRO B 132 -17.608 -5.782 8.219 1.00 31.15 C
ANISOU 5161 CG PRO B 132 4733 3867 3235 -527 -1381 -573 C
ATOM 5162 CD PRO B 132 -18.636 -6.654 8.901 1.00 25.70 C
ANISOU 5162 CD PRO B 132 4548 2920 2295 188 -1474 -281 C
ATOM 5163 C PRO B 132 -18.147 -8.646 5.896 1.00 21.09 C
ANISOU 5163 C PRO B 132 3263 2479 2269 247 -1002 320 C
ATOM 5164 O PRO B 132 -17.969 -8.717 4.664 1.00 21.51 O
ANISOU 5164 O PRO B 132 2776 3092 2303 -333 -1031 303 O
ATOM 5165 N LEU B 133 -18.116 -9.729 6.694 1.00 23.29 N
ANISOU 5165 N LEU B 133 3639 2856 2353 165 -1296 586 N
ATOM 5166 CA LEU B 133 -17.909 -11.065 6.129 1.00 24.15 C
ANISOU 5166 CA LEU B 133 3716 2937 2523 523 -953 580 C
ATOM 5167 CB LEU B 133 -17.701 -12.073 7.265 1.00 30.06 C
ANISOU 5167 CB LEU B 133 4673 3857 2890 871 -1017 1030 C
ATOM 5168 CG LEU B 133 -16.575 -11.715 8.229 1.00 38.63 C
ANISOU 5168 CG LEU B 133 4815 5199 4663 1170 -1699 895 C
ATOM 5169 CD1 LEU B 133 -16.521 -12.699 9.390 1.00 44.12 C
ANISOU 5169 CD1 LEU B 133 6566 4841 5354 1268 -1583 1107 C
ATOM 5170 CD2 LEU B 133 -15.244 -11.649 7.487 1.00 41.61 C
ANISOU 5170 CD2 LEU B 133 4540 5679 5589 1403 -1344 510 C
ATOM 5171 C LEU B 133 -19.110 -11.464 5.255 1.00 20.30 C
ANISOU 5171 C LEU B 133 3048 2282 2381 121 -339 584 C
ATOM 5172 O LEU B 133 -18.959 -12.079 4.169 1.00 21.44 O
ANISOU 5172 O LEU B 133 3239 2157 2750 444 -33 224 O
ATOM 5173 N GLU B 134 -20.319 -11.156 5.720 1.00 18.03 N
ANISOU 5173 N GLU B 134 3098 2055 1696 17 -326 538 N
ATOM 5174 CA AGLU B 134 -21.504 -11.405 4.957 0.50 16.29 C
ANISOU 5174 CA AGLU B 134 2657 1627 1903 -266 1 194 C
ATOM 5175 CA BGLU B 134 -21.525 -11.430 4.932 0.50 17.14 C
ANISOU 5175 CA BGLU B 134 2757 1741 2012 -241 -117 286 C
ATOM 5176 CB AGLU B 134 -22.706 -11.150 5.862 0.50 17.43 C
ANISOU 5176 CB AGLU B 134 2891 1743 1986 -296 254 230 C
ATOM 5177 CB BGLU B 134 -22.835 -11.221 5.708 0.50 19.36 C
ANISOU 5177 CB BGLU B 134 2920 2147 2288 -225 71 273 C
ATOM 5178 CG AGLU B 134 -23.981 -11.586 5.237 0.50 17.79 C
ANISOU 5178 CG AGLU B 134 2797 1771 2188 -252 248 20 C
ATOM 5179 CG BGLU B 134 -23.325 -12.419 6.495 0.50 20.80 C
ANISOU 5179 CG BGLU B 134 2950 2073 2880 -293 -89 361 C
ATOM 5180 CD AGLU B 134 -24.051 -13.087 5.118 0.50 19.13 C
ANISOU 5180 CD AGLU B 134 2838 1742 2686 -207 115 194 C
ATOM 5181 CD BGLU B 134 -23.871 -13.613 5.729 0.50 21.28 C
ANISOU 5181 CD BGLU B 134 2893 2062 3130 -347 -215 466 C
ATOM 5182 OE1AGLU B 134 -23.282 -13.784 5.844 0.50 20.16 O
ANISOU 5182 OE1AGLU B 134 2979 1349 3329 -245 51 492 O
ATOM 5183 OE1BGLU B 134 -24.332 -13.480 4.549 0.50 22.49 O
ANISOU 5183 OE1BGLU B 134 2656 2647 3240 -613 -771 -382 O
ATOM 5184 OE2AGLU B 134 -24.879 -13.552 4.310 0.50 22.96 O
ANISOU 5184 OE2AGLU B 134 3428 2351 2943 -576 13 -350 O
ATOM 5185 OE2BGLU B 134 -23.895 -14.678 6.352 0.50 22.98 O
ANISOU 5185 OE2BGLU B 134 2953 1407 4370 6 -141 334 O
ATOM 5186 C GLU B 134 -21.551 -10.510 3.707 1.00 14.39 C
ANISOU 5186 C GLU B 134 2208 1317 1939 -390 -65 119 C
ATOM 5187 O GLU B 134 -21.943 -10.931 2.633 1.00 14.25 O
ANISOU 5187 O GLU B 134 2097 1553 1763 -330 -25 154 O
ATOM 5188 N LEU B 135 -21.129 -9.246 3.850 1.00 12.55 N
ANISOU 5188 N LEU B 135 1972 1291 1504 -213 -210 49 N
ATOM 5189 CA LEU B 135 -21.158 -8.335 2.701 1.00 12.59 C
ANISOU 5189 CA LEU B 135 1905 1385 1493 -198 -219 109 C
ATOM 5190 CB LEU B 135 -20.769 -6.925 3.142 1.00 12.83 C
ANISOU 5190 CB LEU B 135 1862 1427 1585 -259 -269 112 C
ATOM 5191 CG LEU B 135 -21.763 -6.187 4.038 1.00 13.98 C
ANISOU 5191 CG LEU B 135 2141 1581 1588 -226 -134 35 C
ATOM 5192 CD1 LEU B 135 -21.218 -4.806 4.439 1.00 15.93 C
ANISOU 5192 CD1 LEU B 135 2570 1572 1910 -123 -209 -37 C
ATOM 5193 CD2 LEU B 135 -23.116 -6.062 3.365 1.00 14.26 C
ANISOU 5193 CD2 LEU B 135 2188 1477 1750 -59 -41 -24 C
ATOM 5194 C LEU B 135 -20.239 -8.848 1.586 1.00 12.22 C
ANISOU 5194 C LEU B 135 1705 1367 1571 -62 -340 78 C
ATOM 5195 O LEU B 135 -20.571 -8.686 0.420 1.00 11.73 O
ANISOU 5195 O LEU B 135 1697 1309 1451 -153 -197 116 O
ATOM 5196 N ALA B 136 -19.104 -9.475 1.939 1.00 11.92 N
ANISOU 5196 N ALA B 136 1815 1120 1595 -54 -431 66 N
ATOM 5197 CA ALA B 136 -18.204 -10.035 0.931 1.00 13.14 C
ANISOU 5197 CA ALA B 136 1770 1417 1805 -128 -312 57 C
ATOM 5198 CB ALA B 136 -16.876 -10.395 1.540 1.00 14.70 C
ANISOU 5198 CB ALA B 136 1798 1606 2178 4 -356 -111 C
ATOM 5199 C ALA B 136 -18.837 -11.230 0.205 1.00 11.69 C
ANISOU 5199 C ALA B 136 1644 1066 1730 49 -106 95 C
ATOM 5200 O ALA B 136 -18.487 -11.508 -0.934 1.00 14.24 O
ANISOU 5200 O ALA B 136 2127 1402 1879 40 38 28 O
ATOM 5201 N LEU B 137 -19.740 -11.962 0.867 1.00 11.87 N
ANISOU 5201 N LEU B 137 1630 1371 1507 7 -101 118 N
ATOM 5202 CA LEU B 137 -20.472 -13.037 0.193 1.00 12.50 C
ANISOU 5202 CA LEU B 137 1916 1284 1550 38 -165 76 C
ATOM 5203 CB LEU B 137 -21.073 -14.009 1.207 1.00 14.06 C
ANISOU 5203 CB LEU B 137 2454 1130 1757 -42 -250 139 C
ATOM 5204 CG LEU B 137 -20.059 -14.745 2.075 1.00 18.14 C
ANISOU 5204 CG LEU B 137 2948 1606 2337 261 -419 352 C
ATOM 5205 CD1 LEU B 137 -20.794 -15.637 3.062 1.00 19.75 C
ANISOU 5205 CD1 LEU B 137 3314 1851 2338 175 -392 524 C
ATOM 5206 CD2 LEU B 137 -19.076 -15.535 1.209 1.00 22.45 C
ANISOU 5206 CD2 LEU B 137 3461 2515 2551 739 -427 362 C
ATOM 5207 C LEU B 137 -21.588 -12.464 -0.691 1.00 11.05 C
ANISOU 5207 C LEU B 137 1610 1082 1506 -100 -66 94 C
ATOM 5208 O LEU B 137 -22.032 -13.114 -1.617 1.00 12.89 O
ANISOU 5208 O LEU B 137 1838 1322 1737 -28 -282 -71 O
ATOM 5209 N LEU B 138 -22.062 -11.270 -0.351 1.00 10.51 N
ANISOU 5209 N LEU B 138 1503 1187 1303 -40 -45 72 N
ATOM 5210 CA LEU B 138 -23.147 -10.603 -1.093 1.00 10.62 C
ANISOU 5210 CA LEU B 138 1441 1191 1401 -72 -9 133 C
ATOM 5211 CB LEU B 138 -23.714 -9.495 -0.208 1.00 11.63 C
ANISOU 5211 CB LEU B 138 1699 1247 1470 -48 -156 4 C
ATOM 5212 CG LEU B 138 -25.107 -8.963 -0.517 1.00 12.48 C
ANISOU 5212 CG LEU B 138 1762 1379 1600 40 -91 36 C
ATOM 5213 CD1 LEU B 138 -25.608 -8.144 0.664 1.00 13.55 C
ANISOU 5213 CD1 LEU B 138 1716 1924 1509 107 48 64 C
ATOM 5214 CD2 LEU B 138 -25.151 -8.121 -1.780 1.00 13.18 C
ANISOU 5214 CD2 LEU B 138 1873 1521 1611 -76 82 51 C
ATOM 5215 C LEU B 138 -22.618 -10.082 -2.432 1.00 9.93 C
ANISOU 5215 C LEU B 138 1411 1069 1291 -51 -98 80 C
ATOM 5216 O LEU B 138 -23.266 -10.303 -3.472 1.00 10.79 O
ANISOU 5216 O LEU B 138 1290 1547 1262 47 -74 132 O
ATOM 5217 N SER B 139 -21.462 -9.411 -2.434 1.00 10.54 N
ANISOU 5217 N SER B 139 1463 1219 1319 -67 -230 112 N
ATOM 5218 CA SER B 139 -20.925 -8.786 -3.650 1.00 11.16 C
ANISOU 5218 CA SER B 139 1487 1252 1499 -65 -49 32 C
ATOM 5219 CB SER B 139 -21.284 -7.315 -3.701 1.00 11.63 C
ANISOU 5219 CB SER B 139 1375 1321 1721 29 -90 69 C
ATOM 5220 OG SER B 139 -20.730 -6.661 -4.852 1.00 12.81 O
ANISOU 5220 OG SER B 139 1674 1215 1979 72 46 314 O
ATOM 5221 C SER B 139 -19.413 -8.926 -3.644 1.00 10.56 C
ANISOU 5221 C SER B 139 1437 1174 1401 89 -66 70 C
ATOM 5222 O SER B 139 -18.781 -8.785 -2.586 1.00 10.97 O
ANISOU 5222 O SER B 139 1416 1392 1358 -26 -49 127 O
ATOM 5223 N PRO B 140 -18.778 -9.036 -4.829 1.00 10.10 N
ANISOU 5223 N PRO B 140 1420 1164 1252 127 -158 32 N
ATOM 5224 CA PRO B 140 -17.323 -8.915 -4.934 1.00 10.07 C
ANISOU 5224 CA PRO B 140 1453 1041 1330 180 -106 116 C
ATOM 5225 CB PRO B 140 -17.026 -9.308 -6.389 1.00 10.68 C
ANISOU 5225 CB PRO B 140 1654 1057 1346 72 24 154 C
ATOM 5226 CG PRO B 140 -18.307 -8.920 -7.109 1.00 11.37 C
ANISOU 5226 CG PRO B 140 1688 1394 1238 30 -38 -32 C
ATOM 5227 CD PRO B 140 -19.409 -9.306 -6.137 1.00 10.71 C
ANISOU 5227 CD PRO B 140 1396 1383 1290 60 -114 3 C
ATOM 5228 C PRO B 140 -16.811 -7.506 -4.612 1.00 10.69 C
ANISOU 5228 C PRO B 140 1389 1168 1502 56 -70 69 C
ATOM 5229 O PRO B 140 -15.632 -7.331 -4.343 1.00 13.16 O
ANISOU 5229 O PRO B 140 1488 1280 2232 180 -176 -382 O
ATOM 5230 N CYS B 141 -17.719 -6.514 -4.665 1.00 10.57 N
ANISOU 5230 N CYS B 141 1303 1156 1555 3 -181 99 N
ATOM 5231 CA CYS B 141 -17.373 -5.105 -4.411 1.00 10.64 C
ANISOU 5231 CA CYS B 141 1496 1196 1349 65 -176 40 C
ATOM 5232 CB CYS B 141 -17.874 -4.263 -5.572 1.00 11.06 C
ANISOU 5232 CB CYS B 141 1746 1149 1307 162 -208 -74 C
ATOM 5233 SG CYS B 141 -16.972 -4.601 -7.101 1.00 13.90 S
ANISOU 5233 SG CYS B 141 2249 1565 1467 219 148 119 S
ATOM 5234 C CYS B 141 -18.017 -4.675 -3.092 1.00 10.44 C
ANISOU 5234 C CYS B 141 1421 1228 1318 -69 -204 28 C
ATOM 5235 O CYS B 141 -19.002 -3.938 -3.081 1.00 12.41 O
ANISOU 5235 O CYS B 141 1635 1794 1283 206 -132 186 O
ATOM 5236 N SER B 142 -17.447 -5.159 -1.989 1.00 10.40 N
ANISOU 5236 N SER B 142 1505 1122 1323 67 -72 168 N
ATOM 5237 CA SER B 142 -18.065 -5.003 -0.662 1.00 10.96 C
ANISOU 5237 CA SER B 142 1721 1155 1287 -162 -71 87 C
ATOM 5238 CB SER B 142 -18.049 -6.312 0.080 1.00 12.87 C
ANISOU 5238 CB SER B 142 2112 1139 1638 -520 -106 132 C
ATOM 5239 OG SER B 142 -16.735 -6.770 0.307 1.00 15.15 O
ANISOU 5239 OG SER B 142 2380 1625 1749 -383 -430 338 O
ATOM 5240 C SER B 142 -17.406 -3.910 0.182 1.00 10.60 C
ANISOU 5240 C SER B 142 1599 1120 1307 -118 34 40 C
ATOM 5241 O SER B 142 -17.990 -3.490 1.187 1.00 12.65 O
ANISOU 5241 O SER B 142 1780 1468 1556 -374 261 -290 O
ATOM 5242 N ASP B 143 -16.216 -3.430 -0.203 1.00 9.92 N
ANISOU 5242 N ASP B 143 1559 1096 1114 -7 67 -31 N
ATOM 5243 CA ASP B 143 -15.539 -2.361 0.554 1.00 10.79 C
ANISOU 5243 CA ASP B 143 1749 1041 1309 -71 12 35 C
ATOM 5244 CB ASP B 143 -14.128 -2.150 0.013 1.00 10.95 C
ANISOU 5244 CB ASP B 143 1635 1095 1428 -91 -94 -28 C
ATOM 5245 CG ASP B 143 -13.395 -0.990 0.635 1.00 10.90 C
ANISOU 5245 CG ASP B 143 1693 1101 1346 -135 -117 68 C
ATOM 5246 OD1 ASP B 143 -12.741 -1.207 1.660 1.00 12.37 O
ANISOU 5246 OD1 ASP B 143 2026 1304 1370 -136 -233 91 O
ATOM 5247 OD2 ASP B 143 -13.541 0.140 0.089 1.00 11.50 O
ANISOU 5247 OD2 ASP B 143 1840 1144 1385 -85 2 178 O
ATOM 5248 C ASP B 143 -16.363 -1.074 0.408 1.00 10.67 C
ANISOU 5248 C ASP B 143 1618 1103 1330 -74 -93 -125 C
ATOM 5249 O ASP B 143 -16.802 -0.744 -0.707 1.00 10.90 O
ANISOU 5249 O ASP B 143 1539 1291 1310 -142 -82 -75 O
ATOM 5250 N VAL B 144 -16.562 -0.381 1.534 1.00 9.71 N
ANISOU 5250 N VAL B 144 1532 1001 1154 -87 -66 28 N
ATOM 5251 CA VAL B 144 -17.346 0.847 1.606 1.00 10.23 C
ANISOU 5251 CA VAL B 144 1467 1157 1264 -19 -107 48 C
ATOM 5252 CB VAL B 144 -18.414 0.743 2.705 1.00 11.54 C
ANISOU 5252 CB VAL B 144 1482 1273 1628 -163 70 56 C
ATOM 5253 CG1 VAL B 144 -19.090 2.076 2.962 1.00 13.09 C
ANISOU 5253 CG1 VAL B 144 1720 1314 1939 -160 158 145 C
ATOM 5254 CG2 VAL B 144 -19.421 -0.359 2.385 1.00 12.37 C
ANISOU 5254 CG2 VAL B 144 1432 1343 1923 -125 157 62 C
ATOM 5255 C VAL B 144 -16.399 2.031 1.798 1.00 10.63 C
ANISOU 5255 C VAL B 144 1679 1097 1263 -60 -11 67 C
ATOM 5256 O VAL B 144 -15.531 2.014 2.668 1.00 11.09 O
ANISOU 5256 O VAL B 144 1601 1165 1446 58 -99 66 O
ATOM 5257 N ASP B 145 -16.607 3.078 0.978 1.00 10.33 N
ANISOU 5257 N ASP B 145 1529 1119 1276 -109 -65 100 N
ATOM 5258 CA ASP B 145 -15.728 4.252 1.028 1.00 10.77 C
ANISOU 5258 CA ASP B 145 1725 1021 1346 -113 -79 -16 C
ATOM 5259 CB ASP B 145 -16.163 5.287 -0.004 1.00 11.11 C
ANISOU 5259 CB ASP B 145 1751 1109 1358 -123 -216 35 C
ATOM 5260 CG ASP B 145 -16.021 4.840 -1.442 1.00 11.26 C
ANISOU 5260 CG ASP B 145 1688 1226 1364 -42 -132 98 C
ATOM 5261 OD1 ASP B 145 -15.071 4.085 -1.730 1.00 11.93 O
ANISOU 5261 OD1 ASP B 145 1723 1269 1540 -95 -23 234 O
ATOM 5262 OD2 ASP B 145 -16.837 5.322 -2.268 1.00 11.98 O
ANISOU 5262 OD2 ASP B 145 1663 1549 1339 62 -138 74 O
ATOM 5263 C ASP B 145 -15.744 4.932 2.397 1.00 10.33 C
ANISOU 5263 C ASP B 145 1502 1139 1284 -49 -168 41 C
ATOM 5264 O ASP B 145 -16.808 5.155 3.002 1.00 11.93 O
ANISOU 5264 O ASP B 145 1594 1460 1476 -12 -97 -141 O
ATOM 5265 N GLU B 146 -14.549 5.346 2.832 1.00 10.39 N
ANISOU 5265 N GLU B 146 1600 1082 1266 -196 -140 -114 N
ATOM 5266 CA GLU B 146 -14.420 6.069 4.085 1.00 10.77 C
ANISOU 5266 CA GLU B 146 1679 1210 1202 -165 -5 -139 C
ATOM 5267 CB GLU B 146 -13.164 5.626 4.835 1.00 11.63 C
ANISOU 5267 CB GLU B 146 1820 1303 1293 -167 -98 -2 C
ATOM 5268 CG GLU B 146 -13.161 4.151 5.214 1.00 12.37 C
ANISOU 5268 CG GLU B 146 1961 1386 1353 -73 20 143 C
ATOM 5269 CD GLU B 146 -12.616 3.173 4.196 1.00 13.02 C
ANISOU 5269 CD GLU B 146 1961 1361 1624 47 0 115 C
ATOM 5270 OE1 GLU B 146 -12.241 3.618 3.073 1.00 13.08 O
ANISOU 5270 OE1 GLU B 146 1943 1457 1568 -102 -38 -68 O
ATOM 5271 OE2 GLU B 146 -12.651 1.960 4.523 1.00 12.71 O
ANISOU 5271 OE2 GLU B 146 1733 1305 1791 146 -68 5 O
ATOM 5272 C GLU B 146 -14.412 7.578 3.892 1.00 11.57 C
ANISOU 5272 C GLU B 146 1904 1271 1219 -80 -65 -147 C
ATOM 5273 O GLU B 146 -14.857 8.308 4.801 1.00 11.02 O
ANISOU 5273 O GLU B 146 1972 1094 1118 -33 81 -4 O
ATOM 5274 N TYR B 147 -13.897 8.039 2.751 1.00 10.17 N
ANISOU 5274 N TYR B 147 1604 933 1327 -105 -61 -27 N
ATOM 5275 CA TYR B 147 -13.683 9.458 2.466 1.00 11.20 C
ANISOU 5275 CA TYR B 147 1775 906 1573 24 -196 24 C
ATOM 5276 CB TYR B 147 -12.188 9.818 2.478 1.00 11.72 C
ANISOU 5276 CB TYR B 147 1913 947 1591 -34 -90 130 C
ATOM 5277 CG TYR B 147 -11.517 9.343 3.738 1.00 10.96 C
ANISOU 5277 CG TYR B 147 1730 947 1484 -25 -103 -10 C
ATOM 5278 CD1 TYR B 147 -11.700 10.003 4.940 1.00 11.10 C
ANISOU 5278 CD1 TYR B 147 1770 1038 1409 -109 -245 -41 C
ATOM 5279 CE1 TYR B 147 -11.133 9.538 6.118 1.00 10.16 C
ANISOU 5279 CE1 TYR B 147 1561 1160 1140 -109 -117 -143 C
ATOM 5280 CZ TYR B 147 -10.381 8.379 6.106 1.00 10.37 C
ANISOU 5280 CZ TYR B 147 1698 977 1262 -156 -171 -120 C
ATOM 5281 OH TYR B 147 -9.795 7.855 7.229 1.00 11.49 O
ANISOU 5281 OH TYR B 147 1834 1307 1225 48 -45 -49 O
ATOM 5282 CE2 TYR B 147 -10.162 7.734 4.907 1.00 10.84 C
ANISOU 5282 CE2 TYR B 147 1710 1069 1338 -39 -26 -101 C
ATOM 5283 CD2 TYR B 147 -10.709 8.216 3.731 1.00 10.82 C
ANISOU 5283 CD2 TYR B 147 1755 1003 1352 -16 74 -10 C
ATOM 5284 C TYR B 147 -14.382 9.819 1.162 1.00 11.57 C
ANISOU 5284 C TYR B 147 1981 1088 1325 -36 -137 -111 C
ATOM 5285 O TYR B 147 -14.755 8.959 0.367 1.00 14.15 O
ANISOU 5285 O TYR B 147 2599 1050 1726 -118 -512 -125 O
ATOM 5286 N ASN B 148 -14.494 11.130 0.925 1.00 11.80 N
ANISOU 5286 N ASN B 148 1923 1080 1480 -88 -449 -35 N
ATOM 5287 CA ASN B 148 -15.280 11.624 -0.205 1.00 12.50 C
ANISOU 5287 CA ASN B 148 2079 1249 1422 85 -327 76 C
ATOM 5288 CB ASN B 148 -15.990 12.927 0.152 1.00 13.69 C
ANISOU 5288 CB ASN B 148 2050 1327 1823 173 -373 -79 C
ATOM 5289 CG ASN B 148 -15.083 14.139 0.218 1.00 13.56 C
ANISOU 5289 CG ASN B 148 2243 1245 1663 91 -376 -100 C
ATOM 5290 OD1 ASN B 148 -13.866 14.017 0.355 1.00 13.68 O
ANISOU 5290 OD1 ASN B 148 2301 1458 1435 142 -228 143 O
ATOM 5291 ND2 ASN B 148 -15.672 15.330 0.130 1.00 15.84 N
ANISOU 5291 ND2 ASN B 148 2592 1275 2149 183 -337 -99 N
ATOM 5292 C ASN B 148 -14.472 11.737 -1.500 1.00 12.43 C
ANISOU 5292 C ASN B 148 2111 1141 1469 -39 -290 39 C
ATOM 5293 O ASN B 148 -15.026 12.148 -2.524 1.00 14.28 O
ANISOU 5293 O ASN B 148 2366 1518 1541 42 -348 172 O
ATOM 5294 N ALYS B 149 -13.189 11.377 -1.444 0.50 12.04 N
ANISOU 5294 N ALYS B 149 2150 1178 1246 -42 -176 75 N
ATOM 5295 N BLYS B 149 -13.183 11.395 -1.446 0.50 12.36 N
ANISOU 5295 N BLYS B 149 2137 1290 1268 47 -80 109 N
ATOM 5296 CA ALYS B 149 -12.335 11.320 -2.619 0.50 12.32 C
ANISOU 5296 CA ALYS B 149 2217 1134 1328 -82 -84 82 C
ATOM 5297 CA BLYS B 149 -12.324 11.351 -2.628 0.50 12.80 C
ANISOU 5297 CA BLYS B 149 2134 1325 1401 103 32 131 C
ATOM 5298 CB ALYS B 149 -11.415 12.537 -2.685 0.50 14.86 C
ANISOU 5298 CB ALYS B 149 2694 1414 1537 -414 -81 61 C
ATOM 5299 CB BLYS B 149 -11.416 12.583 -2.712 0.50 15.10 C
ANISOU 5299 CB BLYS B 149 2413 1652 1671 -130 122 160 C
ATOM 5300 CG ALYS B 149 -12.145 13.855 -2.870 0.50 16.99 C
ANISOU 5300 CG ALYS B 149 3245 1326 1883 -402 33 67 C
ATOM 5301 CG BLYS B 149 -12.134 13.929 -2.752 0.50 17.46 C
ANISOU 5301 CG BLYS B 149 2761 1776 2095 27 415 190 C
ATOM 5302 CD ALYS B 149 -11.189 14.917 -3.321 0.50 19.24 C
ANISOU 5302 CD ALYS B 149 3885 1527 1898 -769 -70 180 C
ATOM 5303 CD BLYS B 149 -12.893 14.224 -4.028 0.50 18.48 C
ANISOU 5303 CD BLYS B 149 3023 1963 2033 -26 459 272 C
ATOM 5304 CE ALYS B 149 -11.733 16.324 -3.246 0.50 20.84 C
ANISOU 5304 CE ALYS B 149 4220 1726 1972 -635 69 -10 C
ATOM 5305 CE BLYS B 149 -13.446 15.648 -4.082 0.50 22.51 C
ANISOU 5305 CE BLYS B 149 3394 2454 2705 507 349 489 C
ATOM 5306 NZ ALYS B 149 -10.628 17.256 -2.969 0.50 18.52 N
ANISOU 5306 NZ ALYS B 149 4509 1342 1184 -947 351 201 N
ATOM 5307 NZ BLYS B 149 -14.446 15.847 -5.157 0.50 25.00 N
ANISOU 5307 NZ BLYS B 149 4022 2730 2747 261 311 728 N
ATOM 5308 C ALYS B 149 -11.471 10.065 -2.531 0.50 12.57 C
ANISOU 5308 C ALYS B 149 2105 1290 1378 -22 -104 109 C
ATOM 5309 C BLYS B 149 -11.467 10.086 -2.535 0.50 12.70 C
ANISOU 5309 C BLYS B 149 2046 1366 1410 79 -32 142 C
ATOM 5310 O ALYS B 149 -11.170 9.596 -1.430 0.50 14.21 O
ANISOU 5310 O ALYS B 149 2377 1828 1191 91 -46 73 O
ATOM 5311 O BLYS B 149 -11.184 9.616 -1.424 0.50 14.40 O
ANISOU 5311 O BLYS B 149 2360 1912 1199 215 61 97 O
ATOM 5312 N ILE B 150 -11.108 9.553 -3.703 1.00 12.07 N
ANISOU 5312 N ILE B 150 1955 1309 1319 -90 -51 147 N
ATOM 5313 CA ILE B 150 -10.199 8.412 -3.847 1.00 12.02 C
ANISOU 5313 CA ILE B 150 1866 1263 1435 -104 -115 184 C
ATOM 5314 CB ILE B 150 -10.948 7.203 -4.445 1.00 12.10 C
ANISOU 5314 CB ILE B 150 1797 1243 1557 -51 13 138 C
ATOM 5315 CG1 ILE B 150 -11.998 6.686 -3.466 1.00 12.71 C
ANISOU 5315 CG1 ILE B 150 1854 1321 1653 28 53 193 C
ATOM 5316 CG2 ILE B 150 -9.982 6.113 -4.858 1.00 13.00 C
ANISOU 5316 CG2 ILE B 150 1988 1161 1787 -18 3 170 C
ATOM 5317 CD1 ILE B 150 -13.042 5.802 -4.105 1.00 12.27 C
ANISOU 5317 CD1 ILE B 150 1895 1367 1398 25 -124 213 C
ATOM 5318 C ILE B 150 -9.081 8.870 -4.774 1.00 13.03 C
ANISOU 5318 C ILE B 150 2030 1590 1331 -202 -8 59 C
ATOM 5319 O ILE B 150 -9.356 9.415 -5.849 1.00 13.72 O
ANISOU 5319 O ILE B 150 2117 1704 1390 -208 85 253 O
ATOM 5320 N LYS B 151 -7.841 8.587 -4.392 1.00 13.37 N
ANISOU 5320 N LYS B 151 2030 1716 1334 -196 -34 375 N
ATOM 5321 CA LYS B 151 -6.674 8.971 -5.197 1.00 13.58 C
ANISOU 5321 CA LYS B 151 2021 1747 1392 -175 83 336 C
ATOM 5322 CB LYS B 151 -5.953 10.199 -4.611 1.00 15.61 C
ANISOU 5322 CB LYS B 151 2329 1854 1747 -253 38 364 C
ATOM 5323 CG LYS B 151 -6.821 11.452 -4.503 1.00 17.22 C
ANISOU 5323 CG LYS B 151 2638 1762 2143 -205 162 197 C
ATOM 5324 CD LYS B 151 -6.056 12.713 -4.125 1.00 17.12 C
ANISOU 5324 CD LYS B 151 2512 1842 2150 -169 354 177 C
ATOM 5325 CE LYS B 151 -5.335 12.621 -2.796 1.00 18.69 C
ANISOU 5325 CE LYS B 151 2619 2274 2205 -505 322 273 C
ATOM 5326 NZ LYS B 151 -4.705 13.910 -2.423 1.00 22.91 N
ANISOU 5326 NZ LYS B 151 3454 2458 2789 -473 295 -82 N
ATOM 5327 C LYS B 151 -5.693 7.804 -5.230 1.00 13.68 C
ANISOU 5327 C LYS B 151 1884 1754 1559 -319 93 242 C
ATOM 5328 O LYS B 151 -5.421 7.172 -4.211 1.00 15.16 O
ANISOU 5328 O LYS B 151 1824 2289 1646 -89 43 428 O
ATOM 5329 N ALA B 152 -5.117 7.563 -6.406 1.00 13.33 N
ANISOU 5329 N ALA B 152 1728 2005 1329 -200 -77 215 N
ATOM 5330 CA ALA B 152 -4.137 6.465 -6.549 1.00 15.53 C
ANISOU 5330 CA ALA B 152 2109 2011 1778 -188 169 93 C
ATOM 5331 CB ALA B 152 -3.905 6.175 -8.004 1.00 18.14 C
ANISOU 5331 CB ALA B 152 2449 2522 1920 35 -111 -323 C
ATOM 5332 C ALA B 152 -2.835 6.761 -5.795 1.00 16.09 C
ANISOU 5332 C ALA B 152 2073 2271 1768 -183 277 5 C
ATOM 5333 O ALA B 152 -2.082 5.860 -5.527 1.00 18.36 O
ANISOU 5333 O ALA B 152 2638 2511 1827 65 94 253 O
ATOM 5334 N VAL B 153 -2.575 8.024 -5.454 1.00 16.41 N
ANISOU 5334 N VAL B 153 1971 2447 1816 -493 88 -180 N
ATOM 5335 CA VAL B 153 -1.344 8.329 -4.682 1.00 18.75 C
ANISOU 5335 CA VAL B 153 2426 2820 1878 -676 -79 -30 C
ATOM 5336 CB VAL B 153 -0.964 9.819 -4.767 1.00 21.29 C
ANISOU 5336 CB VAL B 153 2715 2924 2449 -874 65 -145 C
ATOM 5337 CG1 VAL B 153 -0.556 10.191 -6.189 1.00 25.67 C
ANISOU 5337 CG1 VAL B 153 3240 3612 2899 -795 437 211 C
ATOM 5338 CG2 VAL B 153 -2.065 10.747 -4.232 1.00 21.49 C
ANISOU 5338 CG2 VAL B 153 2595 2901 2668 -1078 234 -79 C
ATOM 5339 C VAL B 153 -1.499 7.880 -3.224 1.00 17.94 C
ANISOU 5339 C VAL B 153 2070 2879 1866 -575 -20 23 C
ATOM 5340 O VAL B 153 -0.485 7.878 -2.510 1.00 22.71 O
ANISOU 5340 O VAL B 153 2382 3880 2366 -599 -421 111 O
ATOM 5341 N SER B 154 -2.733 7.555 -2.781 1.00 16.91 N
ANISOU 5341 N SER B 154 2189 2666 1567 -462 222 83 N
ATOM 5342 CA SER B 154 -3.024 7.220 -1.376 1.00 18.46 C
ANISOU 5342 CA SER B 154 2499 2917 1596 -297 82 280 C
ATOM 5343 CB SER B 154 -4.288 7.887 -0.910 1.00 21.82 C
ANISOU 5343 CB SER B 154 3157 2993 2139 10 444 193 C
ATOM 5344 OG SER B 154 -4.246 9.271 -1.148 1.00 26.36 O
ANISOU 5344 OG SER B 154 4382 3149 2483 8 1003 271 O
ATOM 5345 C SER B 154 -3.187 5.714 -1.212 1.00 15.89 C
ANISOU 5345 C SER B 154 1912 2804 1321 -208 -34 -70 C
ATOM 5346 O SER B 154 -3.741 5.042 -2.089 1.00 18.61 O
ANISOU 5346 O SER B 154 2386 3204 1481 -301 -275 -146 O
ATOM 5347 N MET B 155 -2.780 5.186 -0.056 1.00 14.30 N
ANISOU 5347 N MET B 155 1838 2354 1239 -203 177 -88 N
ATOM 5348 CA MET B 155 -2.831 3.744 0.121 1.00 15.82 C
ANISOU 5348 CA MET B 155 2037 2289 1682 -60 196 -217 C
ATOM 5349 CB MET B 155 -1.870 3.289 1.217 1.00 18.52 C
ANISOU 5349 CB MET B 155 2321 2784 1930 -40 41 -89 C
ATOM 5350 CG MET B 155 -0.434 3.629 0.929 1.00 22.16 C
ANISOU 5350 CG MET B 155 2322 3340 2758 -129 -299 -124 C
ATOM 5351 SD MET B 155 0.252 2.804 -0.512 1.00 32.99 S
ANISOU 5351 SD MET B 155 3867 4688 3977 444 571 -147 S
ATOM 5352 CE MET B 155 -0.611 1.231 -0.574 1.00 32.94 C
ANISOU 5352 CE MET B 155 3894 4085 4535 1098 1376 -796 C
ATOM 5353 C MET B 155 -4.248 3.222 0.417 1.00 14.73 C
ANISOU 5353 C MET B 155 2035 2220 1341 -69 199 -311 C
ATOM 5354 O MET B 155 -4.553 2.079 0.086 1.00 16.46 O
ANISOU 5354 O MET B 155 2230 2222 1799 -213 276 -300 O
ATOM 5355 N ASN B 156 -5.112 4.029 1.028 1.00 12.74 N
ANISOU 5355 N ASN B 156 1733 1999 1107 -192 166 -257 N
ATOM 5356 CA ASN B 156 -6.502 3.604 1.210 1.00 13.64 C
ANISOU 5356 CA ASN B 156 1925 1869 1388 -228 142 -178 C
ATOM 5357 CB ASN B 156 -7.188 4.266 2.403 1.00 12.57 C
ANISOU 5357 CB ASN B 156 1706 1741 1329 -169 197 -78 C
ATOM 5358 CG ASN B 156 -8.584 3.721 2.636 1.00 13.64 C
ANISOU 5358 CG ASN B 156 1756 1721 1703 -266 308 -172 C
ATOM 5359 OD1 ASN B 156 -8.790 2.509 2.575 1.00 13.39 O
ANISOU 5359 OD1 ASN B 156 1722 1693 1673 -98 -190 -103 O
ATOM 5360 ND2 ASN B 156 -9.546 4.589 2.873 1.00 14.49 N
ANISOU 5360 ND2 ASN B 156 2140 1720 1644 -182 288 -201 N
ATOM 5361 C ASN B 156 -7.254 3.919 -0.084 1.00 13.82 C
ANISOU 5361 C ASN B 156 2165 1787 1297 -74 107 -297 C
ATOM 5362 O ASN B 156 -7.780 5.003 -0.277 1.00 16.49 O
ANISOU 5362 O ASN B 156 2791 1873 1598 146 78 -289 O
ATOM 5363 N ASN B 157 -7.231 2.962 -0.995 1.00 11.57 N
ANISOU 5363 N ASN B 157 1815 1400 1181 46 134 -111 N
ATOM 5364 CA ASN B 157 -7.692 3.180 -2.351 1.00 11.45 C
ANISOU 5364 CA ASN B 157 1711 1360 1279 -122 47 4 C
ATOM 5365 CB ASN B 157 -6.520 3.527 -3.277 1.00 12.33 C
ANISOU 5365 CB ASN B 157 1839 1418 1426 9 173 81 C
ATOM 5366 CG ASN B 157 -6.895 3.510 -4.735 1.00 11.28 C
ANISOU 5366 CG ASN B 157 1657 1164 1464 -72 91 -57 C
ATOM 5367 OD1 ASN B 157 -8.102 3.505 -5.058 1.00 11.76 O
ANISOU 5367 OD1 ASN B 157 1720 1214 1534 -156 -18 111 O
ATOM 5368 ND2 ASN B 157 -5.874 3.492 -5.607 1.00 11.72 N
ANISOU 5368 ND2 ASN B 157 1638 1365 1448 10 77 165 N
ATOM 5369 C ASN B 157 -8.383 1.904 -2.819 1.00 11.29 C
ANISOU 5369 C ASN B 157 1542 1362 1384 -51 -39 -65 C
ATOM 5370 O ASN B 157 -7.713 0.918 -3.146 1.00 11.67 O
ANISOU 5370 O ASN B 157 1503 1620 1309 93 -70 -28 O
ATOM 5371 N PRO B 158 -9.725 1.878 -2.887 1.00 10.39 N
ANISOU 5371 N PRO B 158 1481 1089 1378 -95 -87 -48 N
ATOM 5372 CA PRO B 158 -10.421 0.654 -3.265 1.00 11.22 C
ANISOU 5372 CA PRO B 158 1598 1113 1550 -230 -88 52 C
ATOM 5373 CB PRO B 158 -11.896 0.969 -3.004 1.00 11.79 C
ANISOU 5373 CB PRO B 158 1646 1474 1358 -220 -16 -55 C
ATOM 5374 CG PRO B 158 -11.977 2.434 -3.233 1.00 13.08 C
ANISOU 5374 CG PRO B 158 1724 1504 1742 -36 -110 -133 C
ATOM 5375 CD PRO B 158 -10.669 2.988 -2.648 1.00 11.60 C
ANISOU 5375 CD PRO B 158 1503 1300 1605 24 -96 -76 C
ATOM 5376 C PRO B 158 -10.208 0.277 -4.734 1.00 10.84 C
ANISOU 5376 C PRO B 158 1533 1057 1526 -186 -31 142 C
ATOM 5377 O PRO B 158 -10.612 -0.814 -5.150 1.00 12.07 O
ANISOU 5377 O PRO B 158 1846 1211 1528 -363 -69 -10 O
ATOM 5378 N TYR B 159 -9.621 1.175 -5.535 1.00 10.03 N
ANISOU 5378 N TYR B 159 1561 795 1455 -130 14 64 N
ATOM 5379 CA TYR B 159 -9.337 0.830 -6.932 1.00 10.74 C
ANISOU 5379 CA TYR B 159 1660 1052 1367 -33 -99 -71 C
ATOM 5380 CB TYR B 159 -9.686 1.976 -7.889 1.00 10.62 C
ANISOU 5380 CB TYR B 159 1656 1164 1213 -146 16 12 C
ATOM 5381 CG TYR B 159 -11.097 2.475 -7.701 1.00 10.43 C
ANISOU 5381 CG TYR B 159 1558 1131 1274 -246 -64 32 C
ATOM 5382 CD1 TYR B 159 -12.145 1.583 -7.536 1.00 10.34 C
ANISOU 5382 CD1 TYR B 159 1437 1134 1356 -231 -187 124 C
ATOM 5383 CE1 TYR B 159 -13.432 2.023 -7.274 1.00 10.89 C
ANISOU 5383 CE1 TYR B 159 1590 1222 1325 -147 -66 -5 C
ATOM 5384 CZ TYR B 159 -13.709 3.374 -7.216 1.00 10.94 C
ANISOU 5384 CZ TYR B 159 1505 1263 1386 -106 -186 95 C
ATOM 5385 OH TYR B 159 -14.990 3.756 -6.919 1.00 10.71 O
ANISOU 5385 OH TYR B 159 1600 1396 1074 -17 -64 147 O
ATOM 5386 CE2 TYR B 159 -12.679 4.281 -7.429 1.00 11.12 C
ANISOU 5386 CE2 TYR B 159 1756 1082 1384 -97 15 142 C
ATOM 5387 CD2 TYR B 159 -11.393 3.834 -7.650 1.00 10.95 C
ANISOU 5387 CD2 TYR B 159 1669 1134 1357 -201 29 122 C
ATOM 5388 C TYR B 159 -7.918 0.282 -7.101 1.00 10.98 C
ANISOU 5388 C TYR B 159 1609 1085 1475 -119 -25 23 C
ATOM 5389 O TYR B 159 -7.520 -0.000 -8.229 1.00 12.01 O
ANISOU 5389 O TYR B 159 1708 1396 1458 120 66 68 O
ATOM 5390 N ARG B 160 -7.199 0.048 -6.002 1.00 11.15 N
ANISOU 5390 N ARG B 160 1752 1078 1405 14 68 50 N
ATOM 5391 CA ARG B 160 -6.016 -0.805 -6.070 1.00 11.42 C
ANISOU 5391 CA ARG B 160 1724 1196 1419 95 80 32 C
ATOM 5392 CB ARG B 160 -5.430 -1.046 -4.677 1.00 12.86 C
ANISOU 5392 CB ARG B 160 1809 1500 1574 280 -3 60 C
ATOM 5393 CG ARG B 160 -4.599 0.117 -4.171 1.00 15.85 C
ANISOU 5393 CG ARG B 160 2008 2187 1825 41 -88 -82 C
ATOM 5394 CD ARG B 160 -4.315 0.106 -2.674 1.00 19.73 C
ANISOU 5394 CD ARG B 160 2722 2978 1793 343 -15 -131 C
ATOM 5395 NE ARG B 160 -3.326 -0.834 -2.247 1.00 23.61 N
ANISOU 5395 NE ARG B 160 2935 3993 2043 838 -141 -45 N
ATOM 5396 CZ ARG B 160 -3.024 -1.159 -0.968 1.00 23.31 C
ANISOU 5396 CZ ARG B 160 3035 3550 2271 1177 -508 180 C
ATOM 5397 NH1 ARG B 160 -3.544 -0.508 0.040 1.00 28.40 N
ANISOU 5397 NH1 ARG B 160 3297 5107 2385 1099 -134 -1 N
ATOM 5398 NH2 ARG B 160 -2.246 -2.206 -0.717 1.00 26.09 N
ANISOU 5398 NH2 ARG B 160 3258 3475 3179 1089 -781 -41 N
ATOM 5399 C ARG B 160 -6.405 -2.129 -6.726 1.00 11.93 C
ANISOU 5399 C ARG B 160 1683 1291 1555 -22 -10 69 C
ATOM 5400 O ARG B 160 -7.361 -2.791 -6.320 1.00 13.45 O
ANISOU 5400 O ARG B 160 1737 1302 2069 -23 108 -35 O
ATOM 5401 N GLN B 161 -5.636 -2.530 -7.729 1.00 11.28 N
ANISOU 5401 N GLN B 161 1519 1093 1672 -2 -58 38 N
ATOM 5402 CA GLN B 161 -5.882 -3.822 -8.321 1.00 11.84 C
ANISOU 5402 CA GLN B 161 1670 1177 1649 26 -93 -9 C
ATOM 5403 CB GLN B 161 -5.245 -3.900 -9.702 1.00 15.30 C
ANISOU 5403 CB GLN B 161 2456 1492 1864 -87 171 -47 C
ATOM 5404 CG GLN B 161 -3.752 -3.833 -9.745 1.00 16.48 C
ANISOU 5404 CG GLN B 161 2541 1746 1972 -139 158 149 C
ATOM 5405 CD GLN B 161 -3.322 -3.867 -11.207 1.00 20.68 C
ANISOU 5405 CD GLN B 161 2896 2733 2228 -290 814 1044 C
ATOM 5406 OE1 GLN B 161 -3.812 -3.111 -12.076 1.00 23.99 O
ANISOU 5406 OE1 GLN B 161 3197 3572 2345 -295 182 807 O
ATOM 5407 NE2 GLN B 161 -2.321 -4.644 -11.498 1.00 24.00 N
ANISOU 5407 NE2 GLN B 161 4206 2487 2423 165 1040 862 N
ATOM 5408 C GLN B 161 -5.422 -4.944 -7.380 1.00 11.70 C
ANISOU 5408 C GLN B 161 1593 1265 1585 106 -15 17 C
ATOM 5409 O GLN B 161 -4.819 -4.724 -6.321 1.00 12.77 O
ANISOU 5409 O GLN B 161 1591 1573 1685 61 -176 3 O
ATOM 5410 N GLY B 162 -5.754 -6.171 -7.767 1.00 10.93 N
ANISOU 5410 N GLY B 162 1545 1223 1382 124 -86 39 N
ATOM 5411 CA GLY B 162 -5.412 -7.351 -6.961 1.00 11.08 C
ANISOU 5411 CA GLY B 162 1530 1181 1499 71 80 157 C
ATOM 5412 C GLY B 162 -3.938 -7.435 -6.602 1.00 11.70 C
ANISOU 5412 C GLY B 162 1593 1235 1616 -30 51 36 C
ATOM 5413 O GLY B 162 -3.575 -7.724 -5.450 1.00 12.10 O
ANISOU 5413 O GLY B 162 1656 1267 1673 61 50 83 O
ATOM 5414 N THR B 163 -3.061 -7.221 -7.586 1.00 11.49 N
ANISOU 5414 N THR B 163 1521 1248 1594 100 54 277 N
ATOM 5415 CA THR B 163 -1.613 -7.316 -7.323 1.00 12.69 C
ANISOU 5415 CA THR B 163 1537 1594 1687 67 31 182 C
ATOM 5416 CB THR B 163 -0.773 -7.252 -8.601 1.00 13.51 C
ANISOU 5416 CB THR B 163 1740 1651 1742 87 173 234 C
ATOM 5417 OG1 THR B 163 -0.991 -5.983 -9.220 1.00 14.87 O
ANISOU 5417 OG1 THR B 163 2121 1704 1822 103 165 374 O
ATOM 5418 CG2 THR B 163 -1.070 -8.363 -9.581 1.00 14.65 C
ANISOU 5418 CG2 THR B 163 1841 1839 1885 136 216 48 C
ATOM 5419 C THR B 163 -1.130 -6.210 -6.368 1.00 12.37 C
ANISOU 5419 C THR B 163 1385 1400 1915 91 -24 202 C
ATOM 5420 O THR B 163 0.012 -6.279 -5.894 1.00 12.93 O
ANISOU 5420 O THR B 163 1352 1599 1962 -21 -33 142 O
ATOM 5421 N GLU B 164 -1.996 -5.230 -6.071 1.00 11.98 N
ANISOU 5421 N GLU B 164 1336 1335 1878 137 -95 194 N
ATOM 5422 CA GLU B 164 -1.685 -4.152 -5.143 1.00 12.47 C
ANISOU 5422 CA GLU B 164 1438 1350 1950 -10 -48 184 C
ATOM 5423 CB GLU B 164 -2.012 -2.796 -5.797 1.00 14.46 C
ANISOU 5423 CB GLU B 164 1581 1483 2430 180 -282 292 C
ATOM 5424 CG GLU B 164 -1.289 -2.554 -7.098 1.00 16.38 C
ANISOU 5424 CG GLU B 164 2272 1538 2414 -194 -364 363 C
ATOM 5425 CD GLU B 164 0.189 -2.290 -7.033 1.00 20.13 C
ANISOU 5425 CD GLU B 164 2215 2956 2477 131 274 869 C
ATOM 5426 OE1 GLU B 164 0.727 -2.251 -5.927 1.00 19.47 O
ANISOU 5426 OE1 GLU B 164 1627 2886 2883 -235 -311 1146 O
ATOM 5427 OE2 GLU B 164 0.800 -2.137 -8.147 1.00 26.82 O
ANISOU 5427 OE2 GLU B 164 3088 4128 2973 527 1067 1041 O
ATOM 5428 C GLU B 164 -2.448 -4.283 -3.831 1.00 13.09 C
ANISOU 5428 C GLU B 164 1557 1364 2052 -121 -13 -64 C
ATOM 5429 O GLU B 164 -2.343 -3.395 -2.976 1.00 15.20 O
ANISOU 5429 O GLU B 164 1940 1677 2158 -242 150 -274 O
ATOM 5430 N SER B 165 -3.191 -5.381 -3.644 1.00 11.40 N
ANISOU 5430 N SER B 165 1474 1199 1656 39 -2 -30 N
ATOM 5431 CA SER B 165 -4.090 -5.550 -2.505 1.00 12.22 C
ANISOU 5431 CA SER B 165 1672 1409 1562 -44 -44 66 C
ATOM 5432 CB SER B 165 -5.513 -5.623 -2.968 1.00 12.68 C
ANISOU 5432 CB SER B 165 1692 1626 1497 -113 -6 154 C
ATOM 5433 OG SER B 165 -5.939 -4.448 -3.642 1.00 13.11 O
ANISOU 5433 OG SER B 165 1615 1652 1713 -38 -99 185 O
ATOM 5434 C SER B 165 -3.723 -6.820 -1.726 1.00 11.93 C
ANISOU 5434 C SER B 165 1620 1531 1378 207 -284 -86 C
ATOM 5435 O SER B 165 -3.848 -7.921 -2.247 1.00 13.78 O
ANISOU 5435 O SER B 165 2209 1491 1534 1 -431 -40 O
ATOM 5436 N THR B 166 -3.272 -6.669 -0.489 1.00 11.62 N
ANISOU 5436 N THR B 166 1490 1441 1484 222 -392 -276 N
ATOM 5437 CA ATHR B 166 -2.934 -7.854 0.329 0.50 10.92 C
ANISOU 5437 CA ATHR B 166 1406 1355 1387 352 -151 -316 C
ATOM 5438 CA BTHR B 166 -2.932 -7.828 0.332 0.50 12.85 C
ANISOU 5438 CA BTHR B 166 1722 1584 1576 184 -135 -69 C
ATOM 5439 CB ATHR B 166 -2.083 -7.566 1.571 0.50 10.10 C
ANISOU 5439 CB ATHR B 166 1096 1285 1453 522 -86 -442 C
ATOM 5440 CB BTHR B 166 -1.992 -7.387 1.459 0.50 16.42 C
ANISOU 5440 CB BTHR B 166 1914 2345 1979 -8 -347 -124 C
ATOM 5441 OG1ATHR B 166 -2.761 -6.563 2.332 0.50 9.27 O
ANISOU 5441 OG1ATHR B 166 993 1246 1281 449 -172 -493 O
ATOM 5442 OG1BTHR B 166 -0.871 -6.696 0.886 0.50 18.62 O
ANISOU 5442 OG1BTHR B 166 2099 2692 2282 -277 -415 -27 O
ATOM 5443 CG2ATHR B 166 -0.650 -7.186 1.253 0.50 10.61 C
ANISOU 5443 CG2ATHR B 166 988 1397 1645 545 -212 -432 C
ATOM 5444 CG2BTHR B 166 -1.479 -8.547 2.276 0.50 19.22 C
ANISOU 5444 CG2BTHR B 166 2264 2555 2483 131 -241 91 C
ATOM 5445 C THR B 166 -4.201 -8.555 0.802 1.00 12.14 C
ANISOU 5445 C THR B 166 1571 1561 1477 203 -229 -246 C
ATOM 5446 O THR B 166 -4.181 -9.771 1.014 1.00 12.47 O
ANISOU 5446 O THR B 166 1512 1509 1716 262 -97 -189 O
ATOM 5447 N ASP B 167 -5.264 -7.789 1.019 1.00 11.88 N
ANISOU 5447 N ASP B 167 1451 1742 1320 130 -164 -108 N
ATOM 5448 CA ASP B 167 -6.540 -8.316 1.516 1.00 12.36 C
ANISOU 5448 CA ASP B 167 1391 1942 1362 220 -118 -8 C
ATOM 5449 CB ASP B 167 -6.938 -7.674 2.844 1.00 15.58 C
ANISOU 5449 CB ASP B 167 1968 2644 1305 437 -130 -37 C
ATOM 5450 CG ASP B 167 -8.239 -8.191 3.454 1.00 20.62 C
ANISOU 5450 CG ASP B 167 2370 3600 1861 140 128 108 C
ATOM 5451 OD1 ASP B 167 -9.026 -8.954 2.759 1.00 20.20 O
ANISOU 5451 OD1 ASP B 167 2764 3028 1883 534 181 144 O
ATOM 5452 OD2 ASP B 167 -8.477 -7.828 4.637 1.00 27.73 O
ANISOU 5452 OD2 ASP B 167 3611 4724 2198 500 -58 -485 O
ATOM 5453 C ASP B 167 -7.611 -8.009 0.477 1.00 12.05 C
ANISOU 5453 C ASP B 167 1599 1631 1346 277 -218 -109 C
ATOM 5454 O ASP B 167 -7.980 -6.827 0.276 1.00 12.18 O
ANISOU 5454 O ASP B 167 1622 1447 1557 278 -147 -363 O
ATOM 5455 N SER B 168 -8.096 -9.054 -0.207 1.00 11.53 N
ANISOU 5455 N SER B 168 1417 1415 1549 106 -164 126 N
ATOM 5456 CA SER B 168 -9.037 -8.870 -1.296 1.00 11.17 C
ANISOU 5456 CA SER B 168 1568 1369 1306 95 -118 98 C
ATOM 5457 CB SER B 168 -9.426 -10.181 -1.901 1.00 10.87 C
ANISOU 5457 CB SER B 168 1551 1224 1354 213 -132 44 C
ATOM 5458 OG SER B 168 -10.089 -11.020 -0.979 1.00 13.22 O
ANISOU 5458 OG SER B 168 1846 1439 1737 -19 1 88 O
ATOM 5459 C SER B 168 -10.283 -8.105 -0.912 1.00 10.64 C
ANISOU 5459 C SER B 168 1549 1158 1334 124 -241 198 C
ATOM 5460 O SER B 168 -10.862 -7.420 -1.772 1.00 10.91 O
ANISOU 5460 O SER B 168 1526 1225 1393 245 -421 94 O
ATOM 5461 N ARG B 169 -10.730 -8.197 0.343 1.00 11.96 N
ANISOU 5461 N ARG B 169 1687 1405 1450 304 -50 186 N
ATOM 5462 CA AARG B 169 -12.014 -7.571 0.717 0.50 13.50 C
ANISOU 5462 CA AARG B 169 1717 1622 1790 317 74 208 C
ATOM 5463 CA BARG B 169 -11.997 -7.560 0.765 0.50 13.60 C
ANISOU 5463 CA BARG B 169 1682 1647 1836 301 122 169 C
ATOM 5464 CB AARG B 169 -12.456 -8.058 2.102 0.50 17.30 C
ANISOU 5464 CB AARG B 169 2254 2160 2157 258 365 555 C
ATOM 5465 CB BARG B 169 -12.341 -7.870 2.227 0.50 16.78 C
ANISOU 5465 CB BARG B 169 1859 2352 2164 365 635 319 C
ATOM 5466 CG AARG B 169 -13.621 -7.300 2.722 0.50 21.91 C
ANISOU 5466 CG AARG B 169 2783 2595 2946 617 434 402 C
ATOM 5467 CG BARG B 169 -12.467 -9.351 2.533 0.50 21.07 C
ANISOU 5467 CG BARG B 169 2521 2437 3047 424 698 218 C
ATOM 5468 CD AARG B 169 -13.875 -7.738 4.158 0.50 25.73 C
ANISOU 5468 CD AARG B 169 3354 3271 3148 295 563 628 C
ATOM 5469 CD BARG B 169 -12.534 -9.672 4.015 0.50 24.85 C
ANISOU 5469 CD BARG B 169 3269 3128 3043 205 647 120 C
ATOM 5470 NE AARG B 169 -12.655 -7.732 4.945 0.50 29.38 N
ANISOU 5470 NE AARG B 169 3615 3770 3777 327 276 494 N
ATOM 5471 NE BARG B 169 -11.611 -8.891 4.832 0.50 30.16 N
ANISOU 5471 NE BARG B 169 3773 4079 3604 147 171 -10 N
ATOM 5472 CZ AARG B 169 -12.189 -6.694 5.625 0.50 30.47 C
ANISOU 5472 CZ AARG B 169 3673 4411 3491 288 254 225 C
ATOM 5473 CZ BARG B 169 -10.742 -9.392 5.697 0.50 28.46 C
ANISOU 5473 CZ BARG B 169 2814 4082 3917 163 112 -389 C
ATOM 5474 NH1AARG B 169 -10.913 -6.661 5.976 0.50 31.79 N
ANISOU 5474 NH1AARG B 169 3178 5181 3720 -858 1079 515 N
ATOM 5475 NH1BARG B 169 -10.108 -8.580 6.523 0.50 34.86 N
ANISOU 5475 NH1BARG B 169 4041 4682 4521 -556 39 -648 N
ATOM 5476 NH2AARG B 169 -12.982 -5.681 5.913 0.50 30.53 N
ANISOU 5476 NH2AARG B 169 3184 5451 2965 317 1501 -173 N
ATOM 5477 NH2BARG B 169 -10.517 -10.692 5.747 0.50 33.39 N
ANISOU 5477 NH2BARG B 169 4166 4041 4478 -198 210 -602 N
ATOM 5478 C ARG B 169 -11.918 -6.035 0.622 1.00 12.77 C
ANISOU 5478 C ARG B 169 1620 1594 1638 204 113 -12 C
ATOM 5479 O ARG B 169 -12.944 -5.364 0.548 1.00 13.86 O
ANISOU 5479 O ARG B 169 1718 1767 1778 328 -50 33 O
ATOM 5480 N MET B 170 -10.690 -5.482 0.602 1.00 11.78 N
ANISOU 5480 N MET B 170 1576 1367 1530 235 -89 -42 N
ATOM 5481 CA AMET B 170 -10.515 -4.020 0.580 0.50 12.19 C
ANISOU 5481 CA AMET B 170 1728 1382 1521 71 -121 -207 C
ATOM 5482 CA BMET B 170 -10.478 -4.019 0.575 0.50 12.04 C
ANISOU 5482 CA BMET B 170 1671 1372 1530 117 -101 -234 C
ATOM 5483 CB AMET B 170 -9.127 -3.623 1.085 0.50 13.44 C
ANISOU 5483 CB AMET B 170 1937 1652 1515 90 -341 -273 C
ATOM 5484 CB BMET B 170 -9.051 -3.643 0.996 0.50 13.41 C
ANISOU 5484 CB BMET B 170 1793 1618 1682 183 -265 -376 C
ATOM 5485 CG AMET B 170 -8.870 -4.098 2.487 0.50 14.97 C
ANISOU 5485 CG AMET B 170 2302 1754 1631 226 -295 -107 C
ATOM 5486 CG BMET B 170 -8.718 -4.045 2.392 0.50 14.41 C
ANISOU 5486 CG BMET B 170 2040 1713 1722 378 -134 -296 C
ATOM 5487 SD AMET B 170 -10.128 -3.536 3.680 0.50 15.39 S
ANISOU 5487 SD AMET B 170 2439 1865 1543 55 -199 107 S
ATOM 5488 SD BMET B 170 -9.688 -3.112 3.584 0.50 14.77 S
ANISOU 5488 SD BMET B 170 2105 1691 1815 341 -153 -397 S
ATOM 5489 CE AMET B 170 -9.194 -3.954 5.148 0.50 15.11 C
ANISOU 5489 CE AMET B 170 2609 1747 1383 486 -130 -14 C
ATOM 5490 CE BMET B 170 -10.830 -4.404 4.079 0.50 15.95 C
ANISOU 5490 CE BMET B 170 2191 2164 1704 267 280 -349 C
ATOM 5491 C MET B 170 -10.698 -3.444 -0.829 1.00 11.24 C
ANISOU 5491 C MET B 170 1629 1188 1451 52 -210 -314 C
ATOM 5492 O MET B 170 -10.837 -2.214 -0.992 1.00 12.62 O
ANISOU 5492 O MET B 170 1916 1243 1635 128 -52 -293 O
ATOM 5493 N SER B 171 -10.693 -4.303 -1.854 1.00 10.52 N
ANISOU 5493 N SER B 171 1754 1001 1242 55 -80 -119 N
ATOM 5494 CA SER B 171 -10.603 -3.838 -3.240 1.00 10.40 C
ANISOU 5494 CA SER B 171 1623 1086 1239 17 -198 -110 C
ATOM 5495 CB SER B 171 -9.531 -4.613 -3.984 1.00 11.88 C
ANISOU 5495 CB SER B 171 1630 1502 1381 205 -160 -51 C
ATOM 5496 OG SER B 171 -9.497 -4.250 -5.366 1.00 13.01 O
ANISOU 5496 OG SER B 171 1724 1759 1458 46 -62 107 O
ATOM 5497 C SER B 171 -11.930 -3.975 -3.995 1.00 10.04 C
ANISOU 5497 C SER B 171 1535 1009 1271 66 -156 -40 C
ATOM 5498 O SER B 171 -12.531 -5.063 -4.021 1.00 11.02 O
ANISOU 5498 O SER B 171 1754 1057 1375 -54 -347 108 O
ATOM 5499 N ARG B 172 -12.302 -2.894 -4.707 1.00 9.44 N
ANISOU 5499 N ARG B 172 1464 1013 1107 9 -126 -70 N
ATOM 5500 CA ARG B 172 -13.314 -2.916 -5.760 1.00 9.66 C
ANISOU 5500 CA ARG B 172 1415 1104 1151 -94 -108 46 C
ATOM 5501 CB ARG B 172 -14.349 -1.821 -5.532 1.00 9.50 C
ANISOU 5501 CB ARG B 172 1339 1091 1180 -167 -121 5 C
ATOM 5502 CG ARG B 172 -14.989 -1.838 -4.148 1.00 9.65 C
ANISOU 5502 CG ARG B 172 1283 1210 1172 -139 -130 101 C
ATOM 5503 CD ARG B 172 -16.229 -0.942 -4.038 1.00 9.76 C
ANISOU 5503 CD ARG B 172 1461 1188 1059 -69 -102 38 C
ATOM 5504 NE ARG B 172 -15.971 0.450 -4.437 1.00 9.81 N
ANISOU 5504 NE ARG B 172 1569 1206 950 -31 -140 152 N
ATOM 5505 CZ ARG B 172 -15.651 1.464 -3.630 1.00 10.20 C
ANISOU 5505 CZ ARG B 172 1561 1096 1217 -24 -168 155 C
ATOM 5506 NH1 ARG B 172 -15.514 1.262 -2.325 1.00 10.33 N
ANISOU 5506 NH1 ARG B 172 1446 1296 1181 -25 -49 161 N
ATOM 5507 NH2 ARG B 172 -15.423 2.665 -4.169 1.00 10.42 N
ANISOU 5507 NH2 ARG B 172 1566 1093 1300 -24 -102 223 N
ATOM 5508 C ARG B 172 -12.640 -2.725 -7.128 1.00 9.41 C
ANISOU 5508 C ARG B 172 1321 1082 1172 -59 -63 56 C
ATOM 5509 O ARG B 172 -13.325 -2.354 -8.111 1.00 10.31 O
ANISOU 5509 O ARG B 172 1471 1182 1263 -38 -173 43 O
ATOM 5510 N GLY B 173 -11.318 -2.973 -7.184 1.00 9.78 N
ANISOU 5510 N GLY B 173 1415 1149 1149 14 -124 70 N
ATOM 5511 CA GLY B 173 -10.512 -2.719 -8.358 1.00 10.38 C
ANISOU 5511 CA GLY B 173 1353 1296 1295 -47 -67 12 C
ATOM 5512 C GLY B 173 -10.455 -3.911 -9.296 1.00 10.20 C
ANISOU 5512 C GLY B 173 1351 1228 1294 -67 -43 52 C
ATOM 5513 O GLY B 173 -11.066 -4.953 -9.073 1.00 10.02 O
ANISOU 5513 O GLY B 173 1466 1241 1099 -168 -108 -11 O
ATOM 5514 N LEU B 174 -9.690 -3.734 -10.372 1.00 10.45 N
ANISOU 5514 N LEU B 174 1570 1135 1265 -93 26 26 N
ATOM 5515 CA LEU B 174 -9.549 -4.743 -11.389 1.00 10.45 C
ANISOU 5515 CA LEU B 174 1583 1182 1206 7 -37 47 C
ATOM 5516 CB LEU B 174 -8.994 -4.118 -12.659 1.00 11.69 C
ANISOU 5516 CB LEU B 174 1689 1358 1394 -79 119 82 C
ATOM 5517 CG LEU B 174 -9.782 -2.928 -13.205 1.00 12.19 C
ANISOU 5517 CG LEU B 174 1888 1391 1351 -51 12 143 C
ATOM 5518 CD1 LEU B 174 -9.118 -2.344 -14.435 1.00 14.66 C
ANISOU 5518 CD1 LEU B 174 2207 1794 1570 -243 73 263 C
ATOM 5519 CD2 LEU B 174 -11.229 -3.296 -13.479 1.00 12.77 C
ANISOU 5519 CD2 LEU B 174 1924 1431 1494 112 11 232 C
ATOM 5520 C LEU B 174 -8.653 -5.871 -10.862 1.00 10.69 C
ANISOU 5520 C LEU B 174 1448 1317 1297 57 -41 89 C
ATOM 5521 O LEU B 174 -7.805 -5.686 -10.005 1.00 12.58 O
ANISOU 5521 O LEU B 174 1757 1285 1737 28 -321 -66 O
ATOM 5522 N GLY B 175 -8.841 -7.065 -11.414 1.00 11.04 N
ANISOU 5522 N GLY B 175 1434 1341 1417 10 -47 79 N
ATOM 5523 CA GLY B 175 -7.934 -8.152 -11.161 1.00 11.47 C
ANISOU 5523 CA GLY B 175 1575 1371 1412 79 -36 50 C
ATOM 5524 C GLY B 175 -7.906 -8.623 -9.723 1.00 10.92 C
ANISOU 5524 C GLY B 175 1487 1251 1408 122 -93 35 C
ATOM 5525 O GLY B 175 -6.841 -9.038 -9.254 1.00 10.86 O
ANISOU 5525 O GLY B 175 1463 1277 1384 107 -15 194 O
ATOM 5526 N CYS B 176 -9.059 -8.563 -9.025 1.00 10.48 N
ANISOU 5526 N CYS B 176 1329 1337 1314 125 -190 143 N
ATOM 5527 CA CYS B 176 -9.066 -8.910 -7.605 1.00 10.03 C
ANISOU 5527 CA CYS B 176 1403 1014 1394 137 -99 152 C
ATOM 5528 CB CYS B 176 -9.041 -7.673 -6.708 1.00 9.83 C
ANISOU 5528 CB CYS B 176 1446 820 1469 -54 -185 228 C
ATOM 5529 SG CYS B 176 -8.695 -8.095 -4.986 1.00 12.08 S
ANISOU 5529 SG CYS B 176 1780 1418 1392 -28 -123 14 S
ATOM 5530 C CYS B 176 -10.247 -9.840 -7.300 1.00 10.47 C
ANISOU 5530 C CYS B 176 1479 1134 1363 50 -121 96 C
ATOM 5531 O CYS B 176 -10.021 -11.035 -7.121 1.00 11.32 O
ANISOU 5531 O CYS B 176 1520 1213 1565 109 74 207 O
ATOM 5532 N ASN B 177 -11.475 -9.303 -7.250 1.00 10.28 N
ANISOU 5532 N ASN B 177 1495 1010 1398 -10 14 118 N
ATOM 5533 CA ASN B 177 -12.644 -10.117 -6.872 1.00 9.06 C
ANISOU 5533 CA ASN B 177 1395 1019 1025 54 -95 129 C
ATOM 5534 CB ASN B 177 -13.439 -9.425 -5.763 1.00 10.26 C
ANISOU 5534 CB ASN B 177 1668 1067 1161 119 -24 -47 C
ATOM 5535 CG ASN B 177 -12.595 -9.199 -4.531 1.00 10.61 C
ANISOU 5535 CG ASN B 177 1657 1093 1278 100 -122 54 C
ATOM 5536 OD1 ASN B 177 -11.837 -10.089 -4.135 1.00 11.92 O
ANISOU 5536 OD1 ASN B 177 1991 1038 1499 145 -349 -10 O
ATOM 5537 ND2 ASN B 177 -12.709 -8.015 -3.935 1.00 11.26 N
ANISOU 5537 ND2 ASN B 177 1716 1045 1515 155 -56 1 N
ATOM 5538 C ASN B 177 -13.575 -10.458 -8.038 1.00 9.96 C
ANISOU 5538 C ASN B 177 1661 1000 1123 28 -258 195 C
ATOM 5539 O ASN B 177 -14.386 -11.366 -7.878 1.00 10.52 O
ANISOU 5539 O ASN B 177 1618 1175 1203 -15 -89 70 O
ATOM 5540 N TYR B 178 -13.500 -9.712 -9.150 1.00 9.72 N
ANISOU 5540 N TYR B 178 1574 1060 1058 -131 -267 179 N
ATOM 5541 CA TYR B 178 -14.415 -9.936 -10.280 1.00 9.49 C
ANISOU 5541 CA TYR B 178 1531 1014 1059 -165 -251 147 C
ATOM 5542 CB TYR B 178 -15.487 -8.848 -10.364 1.00 10.38 C
ANISOU 5542 CB TYR B 178 1568 1184 1189 -60 -154 151 C
ATOM 5543 CG TYR B 178 -14.966 -7.430 -10.437 1.00 10.42 C
ANISOU 5543 CG TYR B 178 1570 1149 1237 9 -164 147 C
ATOM 5544 CD1 TYR B 178 -14.528 -6.865 -11.625 1.00 10.40 C
ANISOU 5544 CD1 TYR B 178 1591 1260 1100 59 -237 47 C
ATOM 5545 CE1 TYR B 178 -14.001 -5.591 -11.672 1.00 11.29 C
ANISOU 5545 CE1 TYR B 178 1779 1295 1215 49 -218 -33 C
ATOM 5546 CZ TYR B 178 -13.923 -4.825 -10.525 1.00 10.32 C
ANISOU 5546 CZ TYR B 178 1728 1000 1193 -79 -249 30 C
ATOM 5547 OH TYR B 178 -13.412 -3.544 -10.597 1.00 10.46 O
ANISOU 5547 OH TYR B 178 1707 920 1345 24 -61 182 O
ATOM 5548 CE2 TYR B 178 -14.331 -5.381 -9.326 1.00 10.64 C
ANISOU 5548 CE2 TYR B 178 1672 1011 1360 -11 6 -8 C
ATOM 5549 CD2 TYR B 178 -14.852 -6.661 -9.295 1.00 9.92 C
ANISOU 5549 CD2 TYR B 178 1554 1017 1196 16 -53 148 C
ATOM 5550 C TYR B 178 -13.618 -10.048 -11.579 1.00 10.03 C
ANISOU 5550 C TYR B 178 1530 1212 1069 128 -267 126 C
ATOM 5551 O TYR B 178 -12.531 -9.475 -11.727 1.00 10.98 O
ANISOU 5551 O TYR B 178 1696 1296 1178 62 -132 47 O
ATOM 5552 N ALA B 179 -14.210 -10.759 -12.538 1.00 10.31 N
ANISOU 5552 N ALA B 179 1549 1201 1164 104 -68 -95 N
ATOM 5553 CA ALA B 179 -13.602 -10.905 -13.863 1.00 10.71 C
ANISOU 5553 CA ALA B 179 1696 1363 1008 150 -210 -2 C
ATOM 5554 CB ALA B 179 -14.316 -12.017 -14.605 1.00 11.53 C
ANISOU 5554 CB ALA B 179 1847 1336 1197 180 -227 -87 C
ATOM 5555 C ALA B 179 -13.687 -9.591 -14.647 1.00 10.76 C
ANISOU 5555 C ALA B 179 1512 1290 1284 21 -106 0 C
ATOM 5556 O ALA B 179 -14.682 -8.841 -14.574 1.00 10.80 O
ANISOU 5556 O ALA B 179 1386 1443 1273 2 -34 156 O
ATOM 5557 N TYR B 180 -12.655 -9.334 -15.448 1.00 10.03 N
ANISOU 5557 N TYR B 180 1459 1123 1227 142 -67 -60 N
ATOM 5558 CA TYR B 180 -12.591 -8.095 -16.224 1.00 10.93 C
ANISOU 5558 CA TYR B 180 1571 1331 1251 50 -68 56 C
ATOM 5559 CB TYR B 180 -12.081 -6.922 -15.358 1.00 11.22 C
ANISOU 5559 CB TYR B 180 1617 1460 1186 32 -142 -51 C
ATOM 5560 CG TYR B 180 -10.584 -6.968 -15.224 1.00 11.10 C
ANISOU 5560 CG TYR B 180 1557 1566 1093 69 -110 0 C
ATOM 5561 CD1 TYR B 180 -9.998 -7.997 -14.495 1.00 11.32 C
ANISOU 5561 CD1 TYR B 180 1647 1506 1145 50 -183 -68 C
ATOM 5562 CE1 TYR B 180 -8.630 -8.195 -14.491 1.00 11.63 C
ANISOU 5562 CE1 TYR B 180 1584 1664 1170 94 -184 0 C
ATOM 5563 CZ TYR B 180 -7.812 -7.346 -15.219 1.00 12.08 C
ANISOU 5563 CZ TYR B 180 1604 1706 1277 -24 -271 39 C
ATOM 5564 OH TYR B 180 -6.455 -7.570 -15.264 1.00 13.51 O
ANISOU 5564 OH TYR B 180 1601 1978 1553 -9 -140 169 O
ATOM 5565 CE2 TYR B 180 -8.372 -6.283 -15.907 1.00 11.76 C
ANISOU 5565 CE2 TYR B 180 1638 1578 1252 -38 -74 73 C
ATOM 5566 CD2 TYR B 180 -9.749 -6.112 -15.924 1.00 11.80 C
ANISOU 5566 CD2 TYR B 180 1699 1556 1229 -9 -231 -23 C
ATOM 5567 C TYR B 180 -11.645 -8.322 -17.407 1.00 11.30 C
ANISOU 5567 C TYR B 180 1680 1392 1221 17 -74 86 C
ATOM 5568 O TYR B 180 -10.813 -9.237 -17.406 1.00 11.94 O
ANISOU 5568 O TYR B 180 1782 1480 1273 130 10 127 O
ATOM 5569 N TYR B 181 -11.741 -7.424 -18.397 1.00 10.74 N
ANISOU 5569 N TYR B 181 1687 1216 1174 95 -59 33 N
ATOM 5570 CA TYR B 181 -10.789 -7.382 -19.476 1.00 11.23 C
ANISOU 5570 CA TYR B 181 1623 1334 1309 55 97 -25 C
ATOM 5571 CB TYR B 181 -11.149 -8.352 -20.612 1.00 12.74 C
ANISOU 5571 CB TYR B 181 1857 1654 1326 -44 79 -71 C
ATOM 5572 CG TYR B 181 -10.170 -8.286 -21.747 1.00 14.40 C
ANISOU 5572 CG TYR B 181 2182 1795 1493 -223 323 -127 C
ATOM 5573 CD1 TYR B 181 -8.873 -8.720 -21.583 1.00 15.91 C
ANISOU 5573 CD1 TYR B 181 2279 2162 1603 -149 636 -188 C
ATOM 5574 CE1 TYR B 181 -7.955 -8.651 -22.621 1.00 18.70 C
ANISOU 5574 CE1 TYR B 181 2531 2432 2142 -268 1042 -182 C
ATOM 5575 CZ TYR B 181 -8.329 -8.114 -23.837 1.00 20.54 C
ANISOU 5575 CZ TYR B 181 3090 2681 2032 -129 1067 -332 C
ATOM 5576 OH TYR B 181 -7.411 -8.001 -24.857 1.00 25.47 O
ANISOU 5576 OH TYR B 181 4263 2483 2931 58 2027 34 O
ATOM 5577 CE2 TYR B 181 -9.628 -7.676 -24.018 1.00 17.70 C
ANISOU 5577 CE2 TYR B 181 3041 1970 1713 -289 766 -100 C
ATOM 5578 CD2 TYR B 181 -10.536 -7.756 -22.972 1.00 15.80 C
ANISOU 5578 CD2 TYR B 181 2629 1918 1456 -108 481 -108 C
ATOM 5579 C TYR B 181 -10.675 -5.966 -20.024 1.00 12.14 C
ANISOU 5579 C TYR B 181 1844 1402 1365 81 40 9 C
ATOM 5580 O TYR B 181 -11.661 -5.407 -20.498 1.00 11.98 O
ANISOU 5580 O TYR B 181 1671 1568 1312 54 163 101 O
ATOM 5581 N ILE B 182 -9.459 -5.416 -19.993 1.00 13.31 N
ANISOU 5581 N ILE B 182 1856 1587 1614 85 49 382 N
ATOM 5582 CA ILE B 182 -9.162 -4.102 -20.588 1.00 14.22 C
ANISOU 5582 CA ILE B 182 2199 1584 1618 -230 83 336 C
ATOM 5583 CB ILE B 182 -8.036 -3.369 -19.860 1.00 18.26 C
ANISOU 5583 CB ILE B 182 2949 1890 2099 -615 -135 478 C
ATOM 5584 CG1 ILE B 182 -8.366 -3.209 -18.385 1.00 20.06 C
ANISOU 5584 CG1 ILE B 182 3500 2169 1950 -817 -243 431 C
ATOM 5585 CG2 ILE B 182 -7.801 -2.023 -20.529 1.00 17.38 C
ANISOU 5585 CG2 ILE B 182 2947 1969 1686 -664 -515 569 C
ATOM 5586 CD1 ILE B 182 -7.194 -2.826 -17.557 1.00 22.85 C
ANISOU 5586 CD1 ILE B 182 3182 2809 2691 -608 -302 375 C
ATOM 5587 C ILE B 182 -8.767 -4.320 -22.055 1.00 14.21 C
ANISOU 5587 C ILE B 182 2242 1537 1618 -103 173 440 C
ATOM 5588 O ILE B 182 -7.807 -5.024 -22.359 1.00 17.12 O
ANISOU 5588 O ILE B 182 2300 1855 2349 66 332 602 O
ATOM 5589 N HIS B 183 -9.501 -3.686 -22.958 1.00 14.25 N
ANISOU 5589 N HIS B 183 2127 1837 1449 19 326 460 N
ATOM 5590 CA HIS B 183 -9.182 -3.770 -24.356 1.00 15.81 C
ANISOU 5590 CA HIS B 183 2377 2090 1540 -61 392 158 C
ATOM 5591 CB HIS B 183 -10.294 -3.170 -25.215 1.00 15.31 C
ANISOU 5591 CB HIS B 183 2450 2004 1363 -79 349 347 C
ATOM 5592 CG HIS B 183 -11.653 -3.780 -25.086 1.00 15.40 C
ANISOU 5592 CG HIS B 183 2383 2164 1304 -156 80 258 C
ATOM 5593 ND1 HIS B 183 -12.572 -3.694 -26.117 1.00 18.52 N
ANISOU 5593 ND1 HIS B 183 2317 2803 1916 -242 -238 211 N
ATOM 5594 CE1 HIS B 183 -13.706 -4.258 -25.720 1.00 17.99 C
ANISOU 5594 CE1 HIS B 183 2682 2460 1691 -319 -208 318 C
ATOM 5595 NE2 HIS B 183 -13.530 -4.745 -24.471 1.00 16.98 N
ANISOU 5595 NE2 HIS B 183 2551 2256 1643 -52 -182 213 N
ATOM 5596 CD2 HIS B 183 -12.261 -4.431 -24.068 1.00 15.53 C
ANISOU 5596 CD2 HIS B 183 2298 2246 1356 -147 148 238 C
ATOM 5597 C HIS B 183 -7.887 -3.021 -24.633 1.00 16.04 C
ANISOU 5597 C HIS B 183 2428 1911 1756 -21 577 222 C
ATOM 5598 O HIS B 183 -7.590 -2.016 -23.989 1.00 16.58 O
ANISOU 5598 O HIS B 183 2397 1964 1937 -235 523 283 O
ATOM 5599 N PRO B 184 -7.084 -3.469 -25.620 1.00 18.19 N
ANISOU 5599 N PRO B 184 3066 1888 1958 -257 983 -31 N
ATOM 5600 CA PRO B 184 -5.858 -2.755 -25.976 1.00 19.42 C
ANISOU 5600 CA PRO B 184 3010 2127 2241 -298 870 100 C
ATOM 5601 CB PRO B 184 -5.404 -3.467 -27.258 1.00 21.92 C
ANISOU 5601 CB PRO B 184 3302 2418 2605 -322 1106 -185 C
ATOM 5602 CG PRO B 184 -5.916 -4.871 -27.069 1.00 23.24 C
ANISOU 5602 CG PRO B 184 3501 2373 2955 -292 1262 -363 C
ATOM 5603 CD PRO B 184 -7.271 -4.693 -26.411 1.00 21.61 C
ANISOU 5603 CD PRO B 184 3420 2355 2437 -524 1078 -418 C
ATOM 5604 C PRO B 184 -6.091 -1.256 -26.218 1.00 19.26 C
ANISOU 5604 C PRO B 184 3001 2119 2195 -300 668 318 C
ATOM 5605 O PRO B 184 -7.096 -0.870 -26.815 1.00 19.59 O
ANISOU 5605 O PRO B 184 3105 2352 1987 -446 476 261 O
ATOM 5606 N ARG B 185 -5.151 -0.437 -25.734 1.00 19.39 N
ANISOU 5606 N ARG B 185 3100 2202 2065 -165 509 401 N
ATOM 5607 CA ARG B 185 -5.231 1.012 -25.832 1.00 19.29 C
ANISOU 5607 CA ARG B 185 2898 2239 2191 -184 611 610 C
ATOM 5608 CB ARG B 185 -4.879 1.655 -24.488 1.00 19.47 C
ANISOU 5608 CB ARG B 185 2868 2308 2219 -60 532 563 C
ATOM 5609 CG ARG B 185 -5.837 1.292 -23.359 1.00 18.91 C
ANISOU 5609 CG ARG B 185 2843 2142 2197 179 502 854 C
ATOM 5610 CD ARG B 185 -5.335 1.753 -21.993 1.00 19.13 C
ANISOU 5610 CD ARG B 185 2962 2008 2298 113 399 738 C
ATOM 5611 NE ARG B 185 -5.373 3.208 -21.882 1.00 19.65 N
ANISOU 5611 NE ARG B 185 3389 2023 2052 185 475 712 N
ATOM 5612 CZ ARG B 185 -4.783 3.929 -20.935 1.00 19.04 C
ANISOU 5612 CZ ARG B 185 3396 1905 1932 74 474 893 C
ATOM 5613 NH1 ARG B 185 -4.036 3.319 -20.023 1.00 20.61 N
ANISOU 5613 NH1 ARG B 185 3149 2259 2420 343 420 812 N
ATOM 5614 NH2 ARG B 185 -4.986 5.248 -20.891 1.00 21.04 N
ANISOU 5614 NH2 ARG B 185 3523 1995 2475 349 577 665 N
ATOM 5615 C ARG B 185 -4.254 1.495 -26.903 1.00 21.06 C
ANISOU 5615 C ARG B 185 3538 2418 2044 -375 812 426 C
ATOM 5616 O ARG B 185 -3.097 1.087 -26.907 1.00 23.74 O
ANISOU 5616 O ARG B 185 3549 3054 2416 -160 912 757 O
ATOM 5617 N ALA B 186 -4.735 2.362 -27.793 1.00 22.94 N
ANISOU 5617 N ALA B 186 3912 2489 2315 -190 968 685 N
ATOM 5618 CA ALA B 186 -3.900 2.900 -28.876 1.00 25.01 C
ANISOU 5618 CA ALA B 186 4238 2806 2457 -508 1093 738 C
ATOM 5619 CB ALA B 186 -4.767 3.354 -30.030 1.00 25.43 C
ANISOU 5619 CB ALA B 186 4717 2604 2338 -560 824 733 C
ATOM 5620 C ALA B 186 -3.046 4.059 -28.354 1.00 24.93 C
ANISOU 5620 C ALA B 186 3964 2811 2696 -398 1263 762 C
ATOM 5621 O ALA B 186 -3.435 4.750 -27.415 1.00 24.60 O
ANISOU 5621 O ALA B 186 4288 2535 2522 -568 986 779 O
ATOM 5622 N ALA B 187 -1.884 4.277 -28.971 1.00 26.72 N
ANISOU 5622 N ALA B 187 4018 2974 3159 -362 1358 1170 N
ATOM 5623 CA ALA B 187 -1.075 5.440 -28.642 1.00 28.01 C
ANISOU 5623 CA ALA B 187 3743 3119 3778 -386 1490 1129 C
ATOM 5624 CB ALA B 187 0.172 5.470 -29.493 1.00 30.96 C
ANISOU 5624 CB ALA B 187 3964 3560 4237 -510 1820 979 C
ATOM 5625 C ALA B 187 -1.931 6.697 -28.838 1.00 25.89 C
ANISOU 5625 C ALA B 187 3647 2844 3344 -586 1600 1030 C
ATOM 5626 O ALA B 187 -2.649 6.814 -29.834 1.00 28.38 O
ANISOU 5626 O ALA B 187 4620 2913 3249 -176 1252 996 O
ATOM 5627 N GLY B 188 -1.866 7.607 -27.863 1.00 27.48 N
ANISOU 5627 N GLY B 188 3766 2735 3940 -706 1150 738 N
ATOM 5628 CA GLY B 188 -2.570 8.883 -27.904 1.00 26.90 C
ANISOU 5628 CA GLY B 188 3850 2667 3701 -686 1029 699 C
ATOM 5629 C GLY B 188 -4.039 8.806 -27.513 1.00 24.38 C
ANISOU 5629 C GLY B 188 3714 2535 3013 -598 736 555 C
ATOM 5630 O GLY B 188 -4.733 9.824 -27.507 1.00 24.19 O
ANISOU 5630 O GLY B 188 3432 2729 3030 -335 613 592 O
ATOM 5631 N SER B 189 -4.530 7.614 -27.189 1.00 22.07 N
ANISOU 5631 N SER B 189 3425 2439 2519 -522 776 532 N
ATOM 5632 CA SER B 189 -5.973 7.442 -26.919 1.00 21.03 C
ANISOU 5632 CA SER B 189 3349 2289 2352 -381 638 284 C
ATOM 5633 CB SER B 189 -6.370 5.999 -26.851 1.00 20.65 C
ANISOU 5633 CB SER B 189 3471 2346 2027 -503 737 171 C
ATOM 5634 OG SER B 189 -5.593 5.276 -25.900 1.00 24.79 O
ANISOU 5634 OG SER B 189 3538 3119 2761 -454 169 602 O
ATOM 5635 C SER B 189 -6.369 8.155 -25.624 1.00 19.87 C
ANISOU 5635 C SER B 189 3254 2280 2014 -480 313 366 C
ATOM 5636 O SER B 189 -5.554 8.319 -24.688 1.00 20.34 O
ANISOU 5636 O SER B 189 3216 2497 2013 -579 238 526 O
ATOM 5637 N THR B 190 -7.632 8.585 -25.601 1.00 19.74 N
ANISOU 5637 N THR B 190 3136 2375 1989 -741 451 227 N
ATOM 5638 CA THR B 190 -8.229 9.313 -24.489 1.00 18.18 C
ANISOU 5638 CA THR B 190 3052 2142 1713 -474 243 422 C
ATOM 5639 CB THR B 190 -8.628 10.725 -24.916 1.00 19.57 C
ANISOU 5639 CB THR B 190 3475 2001 1958 -654 4 390 C
ATOM 5640 OG1 THR B 190 -9.544 10.619 -26.012 1.00 20.23 O
ANISOU 5640 OG1 THR B 190 3355 2387 1941 -659 13 534 O
ATOM 5641 CG2 THR B 190 -7.418 11.550 -25.297 1.00 20.83 C
ANISOU 5641 CG2 THR B 190 3413 2272 2229 -432 422 592 C
ATOM 5642 C THR B 190 -9.446 8.563 -23.949 1.00 17.65 C
ANISOU 5642 C THR B 190 2879 1872 1953 -377 196 333 C
ATOM 5643 O THR B 190 -10.240 9.119 -23.197 1.00 16.34 O
ANISOU 5643 O THR B 190 2541 1880 1788 -259 -90 417 O
ATOM 5644 N SER B 191 -9.531 7.272 -24.274 1.00 17.79 N
ANISOU 5644 N SER B 191 2938 1877 1942 -473 608 212 N
ATOM 5645 CA SER B 191 -10.628 6.435 -23.839 1.00 16.88 C
ANISOU 5645 CA SER B 191 2526 1831 2055 -251 528 329 C
ATOM 5646 CB SER B 191 -11.740 6.422 -24.833 1.00 19.41 C
ANISOU 5646 CB SER B 191 3079 2154 2141 -566 448 325 C
ATOM 5647 OG SER B 191 -11.290 5.874 -26.041 1.00 23.69 O
ANISOU 5647 OG SER B 191 3997 2705 2299 -132 333 78 O
ATOM 5648 C SER B 191 -10.107 5.028 -23.566 1.00 17.49 C
ANISOU 5648 C SER B 191 2384 1987 2274 -168 536 366 C
ATOM 5649 O SER B 191 -9.067 4.654 -24.075 1.00 19.32 O
ANISOU 5649 O SER B 191 2380 2084 2874 -182 656 316 O
ATOM 5650 N VAL B 192 -10.856 4.284 -22.751 1.00 14.91 N
ANISOU 5650 N VAL B 192 1939 1704 2021 -129 384 201 N
ATOM 5651 CA AVAL B 192 -10.572 2.889 -22.475 0.50 15.03 C
ANISOU 5651 CA AVAL B 192 1939 1736 2035 -63 342 240 C
ATOM 5652 CA BVAL B 192 -10.574 2.893 -22.478 0.50 14.34 C
ANISOU 5652 CA BVAL B 192 1994 1682 1770 -104 330 226 C
ATOM 5653 CB AVAL B 192 -9.789 2.677 -21.158 0.50 17.17 C
ANISOU 5653 CB AVAL B 192 2016 2307 2198 -4 296 224 C
ATOM 5654 CB BVAL B 192 -9.804 2.728 -21.153 0.50 15.21 C
ANISOU 5654 CB BVAL B 192 2072 1947 1758 -129 361 218 C
ATOM 5655 CG1AVAL B 192 -8.437 3.361 -21.167 0.50 19.05 C
ANISOU 5655 CG1AVAL B 192 2013 2568 2657 38 309 241 C
ATOM 5656 CG1BVAL B 192 -10.622 3.141 -19.944 0.50 15.11 C
ANISOU 5656 CG1BVAL B 192 2014 1902 1823 -100 352 128 C
ATOM 5657 CG2AVAL B 192 -10.541 3.089 -19.903 0.50 16.40 C
ANISOU 5657 CG2AVAL B 192 1646 2253 2331 -39 299 133 C
ATOM 5658 CG2BVAL B 192 -9.289 1.315 -20.969 0.50 14.86 C
ANISOU 5658 CG2BVAL B 192 2213 1905 1528 -115 345 184 C
ATOM 5659 C VAL B 192 -11.900 2.128 -22.486 1.00 14.49 C
ANISOU 5659 C VAL B 192 2022 1633 1849 -85 417 244 C
ATOM 5660 O VAL B 192 -12.941 2.668 -22.099 1.00 14.24 O
ANISOU 5660 O VAL B 192 2105 1378 1926 -69 311 145 O
ATOM 5661 N LYS B 193 -11.839 0.871 -22.932 1.00 13.72 N
ANISOU 5661 N LYS B 193 2050 1542 1618 -155 435 292 N
ATOM 5662 CA LYS B 193 -12.980 -0.061 -22.873 1.00 13.67 C
ANISOU 5662 CA LYS B 193 2010 1608 1574 -192 212 361 C
ATOM 5663 CB LYS B 193 -13.321 -0.644 -24.245 1.00 16.44 C
ANISOU 5663 CB LYS B 193 2766 1792 1688 -47 76 270 C
ATOM 5664 CG LYS B 193 -14.074 0.321 -25.131 1.00 19.24 C
ANISOU 5664 CG LYS B 193 3298 2081 1931 173 -314 96 C
ATOM 5665 CD LYS B 193 -14.506 -0.264 -26.452 1.00 22.60 C
ANISOU 5665 CD LYS B 193 4026 2624 1935 246 -603 -125 C
ATOM 5666 CE LYS B 193 -15.263 0.713 -27.306 1.00 27.89 C
ANISOU 5666 CE LYS B 193 4726 3031 2840 417 -1026 -167 C
ATOM 5667 NZ LYS B 193 -15.695 0.074 -28.567 1.00 34.96 N
ANISOU 5667 NZ LYS B 193 5468 4510 3302 294 -1517 -712 N
ATOM 5668 C LYS B 193 -12.614 -1.214 -21.940 1.00 13.38 C
ANISOU 5668 C LYS B 193 1888 1677 1518 -67 104 292 C
ATOM 5669 O LYS B 193 -11.548 -1.802 -22.087 1.00 13.64 O
ANISOU 5669 O LYS B 193 1845 1646 1691 -137 175 224 O
ATOM 5670 N ILE B 194 -13.526 -1.509 -20.998 1.00 12.02 N
ANISOU 5670 N ILE B 194 1786 1487 1293 -79 -37 284 N
ATOM 5671 CA ILE B 194 -13.297 -2.549 -20.018 1.00 12.65 C
ANISOU 5671 CA ILE B 194 1922 1488 1394 -81 -123 279 C
ATOM 5672 CB ILE B 194 -12.986 -1.963 -18.630 1.00 12.91 C
ANISOU 5672 CB ILE B 194 1841 1600 1464 -16 -306 139 C
ATOM 5673 CG1 ILE B 194 -11.900 -0.892 -18.716 1.00 15.15 C
ANISOU 5673 CG1 ILE B 194 2124 1860 1771 -164 -371 238 C
ATOM 5674 CG2 ILE B 194 -12.639 -3.085 -17.665 1.00 12.32 C
ANISOU 5674 CG2 ILE B 194 1677 1525 1479 -124 -394 59 C
ATOM 5675 CD1 ILE B 194 -11.539 -0.207 -17.423 1.00 18.22 C
ANISOU 5675 CD1 ILE B 194 2811 2192 1917 -59 -408 37 C
ATOM 5676 C ILE B 194 -14.540 -3.428 -19.964 1.00 12.04 C
ANISOU 5676 C ILE B 194 1863 1398 1313 -51 -108 310 C
ATOM 5677 O ILE B 194 -15.656 -2.924 -19.740 1.00 12.71 O
ANISOU 5677 O ILE B 194 1807 1506 1515 -124 -56 342 O
ATOM 5678 N ASP B 195 -14.320 -4.742 -20.121 1.00 11.33 N
ANISOU 5678 N ASP B 195 1636 1360 1310 -19 55 245 N
ATOM 5679 CA ASP B 195 -15.373 -5.718 -19.902 1.00 11.42 C
ANISOU 5679 CA ASP B 195 1691 1346 1301 -78 -151 230 C
ATOM 5680 CB ASP B 195 -15.113 -6.990 -20.711 1.00 12.65 C
ANISOU 5680 CB ASP B 195 1944 1325 1538 -99 -118 166 C
ATOM 5681 CG ASP B 195 -14.877 -6.787 -22.187 1.00 14.80 C
ANISOU 5681 CG ASP B 195 2277 1779 1565 23 -8 34 C
ATOM 5682 OD1 ASP B 195 -15.346 -5.749 -22.733 1.00 14.40 O
ANISOU 5682 OD1 ASP B 195 2244 1799 1427 -98 -142 48 O
ATOM 5683 OD2 ASP B 195 -14.253 -7.672 -22.771 1.00 16.57 O
ANISOU 5683 OD2 ASP B 195 2780 1942 1571 251 74 36 O
ATOM 5684 C ASP B 195 -15.402 -6.062 -18.412 1.00 13.04 C
ANISOU 5684 C ASP B 195 1808 1803 1343 -24 -91 336 C
ATOM 5685 O ASP B 195 -14.341 -6.211 -17.800 1.00 13.12 O
ANISOU 5685 O ASP B 195 1768 1703 1511 -112 -140 283 O
ATOM 5686 N PHE B 196 -16.605 -6.227 -17.864 1.00 12.32 N
ANISOU 5686 N PHE B 196 1823 1784 1070 -47 -215 216 N
ATOM 5687 CA PHE B 196 -16.813 -6.621 -16.472 1.00 11.36 C
ANISOU 5687 CA PHE B 196 1736 1427 1153 -19 -154 252 C
ATOM 5688 CB PHE B 196 -17.431 -5.460 -15.683 1.00 11.63 C
ANISOU 5688 CB PHE B 196 1656 1461 1300 -25 -48 193 C
ATOM 5689 CG PHE B 196 -16.561 -4.246 -15.478 1.00 11.50 C
ANISOU 5689 CG PHE B 196 1611 1475 1280 6 -260 246 C
ATOM 5690 CD1 PHE B 196 -16.558 -3.205 -16.390 1.00 12.92 C
ANISOU 5690 CD1 PHE B 196 1829 1537 1539 -67 -306 386 C
ATOM 5691 CE1 PHE B 196 -15.791 -2.062 -16.167 1.00 12.10 C
ANISOU 5691 CE1 PHE B 196 1804 1298 1492 112 -129 444 C
ATOM 5692 CZ PHE B 196 -14.991 -1.987 -15.053 1.00 12.41 C
ANISOU 5692 CZ PHE B 196 1937 1144 1631 89 -152 351 C
ATOM 5693 CD2 PHE B 196 -15.747 -4.140 -14.360 1.00 10.80 C
ANISOU 5693 CD2 PHE B 196 1547 1343 1214 60 -236 358 C
ATOM 5694 CE2 PHE B 196 -14.984 -3.006 -14.149 1.00 11.43 C
ANISOU 5694 CE2 PHE B 196 1786 1339 1217 27 -173 289 C
ATOM 5695 C PHE B 196 -17.813 -7.777 -16.399 1.00 11.69 C
ANISOU 5695 C PHE B 196 1531 1523 1384 25 -197 224 C
ATOM 5696 O PHE B 196 -18.782 -7.835 -17.195 1.00 12.68 O
ANISOU 5696 O PHE B 196 1706 1664 1446 -108 -329 231 O
ATOM 5697 N VAL B 197 -17.639 -8.626 -15.378 1.00 12.12 N
ANISOU 5697 N VAL B 197 1646 1605 1352 -128 -354 227 N
ATOM 5698 CA VAL B 197 -18.664 -9.595 -14.976 1.00 11.62 C
ANISOU 5698 CA VAL B 197 1682 1475 1259 -65 -215 224 C
ATOM 5699 CB VAL B 197 -18.302 -11.041 -15.392 1.00 13.45 C
ANISOU 5699 CB VAL B 197 1831 1579 1698 -87 -243 22 C
ATOM 5700 CG1 VAL B 197 -19.405 -12.013 -15.011 1.00 13.36 C
ANISOU 5700 CG1 VAL B 197 1897 1341 1837 -128 -597 53 C
ATOM 5701 CG2 VAL B 197 -17.976 -11.127 -16.880 1.00 15.59 C
ANISOU 5701 CG2 VAL B 197 2262 1970 1688 30 -298 144 C
ATOM 5702 C VAL B 197 -18.772 -9.526 -13.459 1.00 11.45 C
ANISOU 5702 C VAL B 197 1560 1525 1266 -213 -172 224 C
ATOM 5703 O VAL B 197 -17.754 -9.660 -12.786 1.00 13.22 O
ANISOU 5703 O VAL B 197 1723 2050 1248 -136 -276 229 O
ATOM 5704 N VAL B 198 -19.996 -9.369 -12.957 1.00 11.10 N
ANISOU 5704 N VAL B 198 1428 1545 1242 -254 -262 92 N
ATOM 5705 CA VAL B 198 -20.250 -9.317 -11.508 1.00 11.27 C
ANISOU 5705 CA VAL B 198 1520 1511 1250 -213 -211 38 C
ATOM 5706 CB VAL B 198 -20.592 -7.890 -11.044 1.00 12.98 C
ANISOU 5706 CB VAL B 198 1802 1508 1619 -269 -304 -47 C
ATOM 5707 CG1 VAL B 198 -20.981 -7.873 -9.580 1.00 13.91 C
ANISOU 5707 CG1 VAL B 198 2037 1543 1704 -34 -241 -161 C
ATOM 5708 CG2 VAL B 198 -19.453 -6.927 -11.319 1.00 16.38 C
ANISOU 5708 CG2 VAL B 198 2414 1541 2268 -573 -237 -86 C
ATOM 5709 C VAL B 198 -21.408 -10.257 -11.185 1.00 10.84 C
ANISOU 5709 C VAL B 198 1459 1477 1180 -86 -89 11 C
ATOM 5710 O VAL B 198 -22.462 -10.191 -11.833 1.00 11.89 O
ANISOU 5710 O VAL B 198 1628 1604 1285 -287 -249 313 O
ATOM 5711 N ASP B 199 -21.197 -11.120 -10.175 1.00 11.18 N
ANISOU 5711 N ASP B 199 1439 1609 1198 -37 -136 95 N
ATOM 5712 CA ASP B 199 -22.249 -12.074 -9.674 1.00 11.85 C
ANISOU 5712 CA ASP B 199 1518 1590 1393 -34 -144 47 C
ATOM 5713 CB ASP B 199 -21.741 -13.509 -9.833 1.00 12.50 C
ANISOU 5713 CB ASP B 199 1921 1573 1253 -82 13 -8 C
ATOM 5714 CG ASP B 199 -22.673 -14.618 -9.400 1.00 14.15 C
ANISOU 5714 CG ASP B 199 1931 1568 1875 -157 -102 -69 C
ATOM 5715 OD1 ASP B 199 -23.585 -14.341 -8.615 1.00 14.65 O
ANISOU 5715 OD1 ASP B 199 1848 1858 1859 121 -295 48 O
ATOM 5716 OD2 ASP B 199 -22.451 -15.798 -9.855 1.00 15.57 O
ANISOU 5716 OD2 ASP B 199 2060 1841 2011 -100 -241 -466 O
ATOM 5717 C ASP B 199 -22.562 -11.682 -8.224 1.00 11.51 C
ANISOU 5717 C ASP B 199 1357 1639 1377 -89 -234 16 C
ATOM 5718 O ASP B 199 -21.737 -11.916 -7.365 1.00 12.82 O
ANISOU 5718 O ASP B 199 1622 1991 1257 227 -225 40 O
ATOM 5719 N GLU B 200 -23.709 -11.033 -7.999 1.00 9.72 N
ANISOU 5719 N GLU B 200 1490 1171 1031 -21 -312 66 N
ATOM 5720 CA GLU B 200 -24.066 -10.372 -6.754 1.00 9.87 C
ANISOU 5720 CA GLU B 200 1464 1175 1109 50 -260 52 C
ATOM 5721 CB GLU B 200 -24.043 -8.856 -6.966 1.00 10.82 C
ANISOU 5721 CB GLU B 200 1560 1183 1368 85 -158 118 C
ATOM 5722 CG GLU B 200 -24.380 -8.015 -5.758 1.00 11.58 C
ANISOU 5722 CG GLU B 200 1717 1240 1442 70 -199 90 C
ATOM 5723 CD GLU B 200 -24.012 -6.540 -5.900 1.00 11.70 C
ANISOU 5723 CD GLU B 200 1610 1360 1473 -76 -57 234 C
ATOM 5724 OE1 GLU B 200 -22.928 -6.244 -6.456 1.00 12.50 O
ANISOU 5724 OE1 GLU B 200 1658 1448 1643 -202 64 -70 O
ATOM 5725 OE2 GLU B 200 -24.838 -5.689 -5.495 1.00 11.57 O
ANISOU 5725 OE2 GLU B 200 1618 1246 1530 -87 -232 140 O
ATOM 5726 C GLU B 200 -25.434 -10.866 -6.288 1.00 9.88 C
ANISOU 5726 C GLU B 200 1490 1101 1160 48 -245 85 C
ATOM 5727 O GLU B 200 -26.365 -10.991 -7.091 1.00 10.75 O
ANISOU 5727 O GLU B 200 1554 1307 1222 59 -325 28 O
ATOM 5728 N ALA B 201 -25.560 -11.173 -4.993 1.00 10.40 N
ANISOU 5728 N ALA B 201 1588 1129 1231 -22 -142 108 N
ATOM 5729 CA ALA B 201 -26.869 -11.565 -4.443 1.00 10.54 C
ANISOU 5729 CA ALA B 201 1526 1148 1330 -36 -161 189 C
ATOM 5730 CB ALA B 201 -26.724 -11.959 -2.987 1.00 11.58 C
ANISOU 5730 CB ALA B 201 1809 1180 1409 12 -20 378 C
ATOM 5731 C ALA B 201 -27.861 -10.414 -4.583 1.00 10.59 C
ANISOU 5731 C ALA B 201 1480 1197 1346 -79 -158 210 C
ATOM 5732 O ALA B 201 -27.515 -9.275 -4.315 1.00 10.84 O
ANISOU 5732 O ALA B 201 1309 1139 1669 -98 -233 140 O
ATOM 5733 N LEU B 202 -29.095 -10.740 -4.960 1.00 10.15 N
ANISOU 5733 N LEU B 202 1431 1135 1289 -26 -244 177 N
ATOM 5734 CA LEU B 202 -30.160 -9.726 -5.052 1.00 10.52 C
ANISOU 5734 CA LEU B 202 1331 1381 1284 23 -294 291 C
ATOM 5735 CB LEU B 202 -31.296 -10.283 -5.915 1.00 11.94 C
ANISOU 5735 CB LEU B 202 1511 1574 1450 -32 -422 220 C
ATOM 5736 CG LEU B 202 -32.551 -9.403 -5.996 1.00 12.42 C
ANISOU 5736 CG LEU B 202 1725 1592 1399 124 -417 89 C
ATOM 5737 CD1 LEU B 202 -32.247 -8.022 -6.549 1.00 13.15 C
ANISOU 5737 CD1 LEU B 202 1770 1616 1608 209 -392 157 C
ATOM 5738 CD2 LEU B 202 -33.629 -10.084 -6.814 1.00 13.45 C
ANISOU 5738 CD2 LEU B 202 1595 1953 1560 105 -421 3 C
ATOM 5739 C LEU B 202 -30.672 -9.430 -3.634 1.00 10.42 C
ANISOU 5739 C LEU B 202 1441 1244 1271 -61 -314 94 C
ATOM 5740 O LEU B 202 -31.023 -10.359 -2.889 1.00 11.73 O
ANISOU 5740 O LEU B 202 1813 1281 1361 -37 -174 155 O
ATOM 5741 N VAL B 203 -30.730 -8.148 -3.282 1.00 10.96 N
ANISOU 5741 N VAL B 203 1551 1261 1351 2 -193 86 N
ATOM 5742 CA VAL B 203 -31.223 -7.657 -1.996 1.00 11.37 C
ANISOU 5742 CA VAL B 203 1502 1326 1491 -38 -154 59 C
ATOM 5743 CB VAL B 203 -30.274 -6.596 -1.416 1.00 11.78 C
ANISOU 5743 CB VAL B 203 1604 1186 1686 37 -195 -12 C
ATOM 5744 CG1 VAL B 203 -30.807 -6.004 -0.119 1.00 12.90 C
ANISOU 5744 CG1 VAL B 203 1747 1468 1686 66 -103 55 C
ATOM 5745 CG2 VAL B 203 -28.882 -7.180 -1.230 1.00 12.35 C
ANISOU 5745 CG2 VAL B 203 1563 1562 1567 8 -262 7 C
ATOM 5746 C VAL B 203 -32.651 -7.146 -2.195 1.00 11.10 C
ANISOU 5746 C VAL B 203 1481 1100 1636 -55 -126 -56 C
ATOM 5747 O VAL B 203 -32.892 -5.981 -2.482 1.00 12.81 O
ANISOU 5747 O VAL B 203 1725 1166 1976 -55 -122 113 O
ATOM 5748 N ALA B 204 -33.604 -8.062 -2.039 1.00 11.05 N
ANISOU 5748 N ALA B 204 1476 1043 1680 -11 -93 134 N
ATOM 5749 CA ALA B 204 -35.015 -7.782 -2.325 1.00 11.06 C
ANISOU 5749 CA ALA B 204 1450 1165 1585 57 -137 166 C
ATOM 5750 CB ALA B 204 -35.303 -7.824 -3.822 1.00 11.72 C
ANISOU 5750 CB ALA B 204 1582 1237 1634 81 -218 255 C
ATOM 5751 C ALA B 204 -35.880 -8.802 -1.606 1.00 11.43 C
ANISOU 5751 C ALA B 204 1402 1319 1619 -59 -42 -11 C
ATOM 5752 O ALA B 204 -35.686 -10.008 -1.818 1.00 12.39 O
ANISOU 5752 O ALA B 204 1652 1257 1796 -51 160 164 O
ATOM 5753 N ASN B 205 -36.832 -8.342 -0.798 1.00 12.36 N
ANISOU 5753 N ASN B 205 1264 1554 1877 -165 40 -12 N
ATOM 5754 CA ASN B 205 -37.691 -9.274 -0.058 1.00 12.75 C
ANISOU 5754 CA ASN B 205 1331 1595 1918 -372 6 -193 C
ATOM 5755 CB ASN B 205 -38.792 -8.532 0.704 1.00 14.29 C
ANISOU 5755 CB ASN B 205 1562 2141 1725 -391 207 -327 C
ATOM 5756 CG ASN B 205 -38.280 -7.552 1.740 1.00 18.71 C
ANISOU 5756 CG ASN B 205 2318 2675 2113 -567 156 -727 C
ATOM 5757 OD1 ASN B 205 -37.428 -6.711 1.429 1.00 22.68 O
ANISOU 5757 OD1 ASN B 205 3227 2802 2587 -748 114 -114 O
ATOM 5758 ND2 ASN B 205 -38.822 -7.602 2.935 1.00 16.69 N
ANISOU 5758 ND2 ASN B 205 2073 2233 2032 53 104 -379 N
ATOM 5759 C ASN B 205 -38.315 -10.264 -1.048 1.00 12.10 C
ANISOU 5759 C ASN B 205 1415 1693 1486 -212 119 -227 C
ATOM 5760 O ASN B 205 -38.781 -9.868 -2.102 1.00 12.81 O
ANISOU 5760 O ASN B 205 1505 1715 1647 -91 -210 -204 O
ATOM 5761 N PRO B 206 -38.329 -11.571 -0.733 1.00 12.15 N
ANISOU 5761 N PRO B 206 1446 1515 1652 -69 -238 -197 N
ATOM 5762 CA PRO B 206 -37.973 -12.220 0.519 1.00 12.82 C
ANISOU 5762 CA PRO B 206 1488 1703 1680 -249 -165 -155 C
ATOM 5763 CB PRO B 206 -39.082 -13.302 0.630 1.00 13.97 C
ANISOU 5763 CB PRO B 206 1589 1765 1951 -291 -220 -188 C
ATOM 5764 CG PRO B 206 -39.246 -13.766 -0.797 1.00 13.68 C
ANISOU 5764 CG PRO B 206 1604 1579 2013 -348 -231 -319 C
ATOM 5765 CD PRO B 206 -39.119 -12.479 -1.588 1.00 13.66 C
ANISOU 5765 CD PRO B 206 1590 1723 1875 -186 -502 -156 C
ATOM 5766 C PRO B 206 -36.595 -12.888 0.506 1.00 11.80 C
ANISOU 5766 C PRO B 206 1459 1373 1649 -284 -93 -101 C
ATOM 5767 O PRO B 206 -36.359 -13.827 1.268 1.00 13.27 O
ANISOU 5767 O PRO B 206 1887 1428 1727 -206 -184 -101 O
ATOM 5768 N THR B 207 -35.684 -12.435 -0.364 1.00 11.30 N
ANISOU 5768 N THR B 207 1389 1482 1422 19 -41 -47 N
ATOM 5769 CA THR B 207 -34.405 -13.133 -0.474 1.00 11.99 C
ANISOU 5769 CA THR B 207 1533 1395 1626 102 -80 -77 C
ATOM 5770 CB THR B 207 -33.487 -12.597 -1.582 1.00 11.72 C
ANISOU 5770 CB THR B 207 1343 1322 1785 54 -24 -151 C
ATOM 5771 OG1 THR B 207 -33.002 -11.298 -1.213 1.00 12.58 O
ANISOU 5771 OG1 THR B 207 1821 1346 1612 -116 -203 -9 O
ATOM 5772 CG2 THR B 207 -34.137 -12.566 -2.948 1.00 13.36 C
ANISOU 5772 CG2 THR B 207 1670 1454 1952 122 -216 -217 C
ATOM 5773 C THR B 207 -33.643 -13.092 0.855 1.00 11.60 C
ANISOU 5773 C THR B 207 1401 1417 1586 30 -41 -62 C
ATOM 5774 O THR B 207 -33.760 -12.149 1.680 1.00 12.32 O
ANISOU 5774 O THR B 207 1655 1248 1778 33 33 -32 O
ATOM 5775 N GLN B 208 -32.857 -14.139 1.069 1.00 11.50 N
ANISOU 5775 N GLN B 208 1558 1412 1399 111 18 -73 N
ATOM 5776 CA GLN B 208 -32.156 -14.374 2.322 1.00 12.10 C
ANISOU 5776 CA GLN B 208 1639 1459 1500 72 -8 137 C
ATOM 5777 CB GLN B 208 -32.254 -15.858 2.668 1.00 12.12 C
ANISOU 5777 CB GLN B 208 1597 1407 1598 -33 -48 73 C
ATOM 5778 CG GLN B 208 -33.690 -16.327 2.873 1.00 12.49 C
ANISOU 5778 CG GLN B 208 1638 1418 1687 -51 -27 180 C
ATOM 5779 CD GLN B 208 -34.325 -15.652 4.061 1.00 13.62 C
ANISOU 5779 CD GLN B 208 1797 1594 1783 181 14 130 C
ATOM 5780 OE1 GLN B 208 -33.973 -16.015 5.177 1.00 15.68 O
ANISOU 5780 OE1 GLN B 208 2234 1940 1782 198 92 247 O
ATOM 5781 NE2 GLN B 208 -35.258 -14.703 3.857 1.00 13.32 N
ANISOU 5781 NE2 GLN B 208 1688 1270 2100 -131 -185 301 N
ATOM 5782 C GLN B 208 -30.726 -13.825 2.234 1.00 11.74 C
ANISOU 5782 C GLN B 208 1514 1480 1467 170 -196 120 C
ATOM 5783 O GLN B 208 -29.738 -14.520 2.507 1.00 12.37 O
ANISOU 5783 O GLN B 208 1286 1530 1883 75 -252 109 O
ATOM 5784 N TYR B 209 -30.632 -12.523 1.953 1.00 13.07 N
ANISOU 5784 N TYR B 209 1537 1474 1954 96 -12 188 N
ATOM 5785 CA TYR B 209 -29.348 -11.859 1.663 1.00 13.47 C
ANISOU 5785 CA TYR B 209 1490 1642 1983 -51 -145 70 C
ATOM 5786 CB TYR B 209 -29.578 -10.539 0.918 1.00 14.13 C
ANISOU 5786 CB TYR B 209 1512 1795 2061 -171 -50 268 C
ATOM 5787 CG TYR B 209 -30.406 -9.542 1.677 1.00 13.54 C
ANISOU 5787 CG TYR B 209 1632 1557 1954 -217 -7 202 C
ATOM 5788 CD1 TYR B 209 -29.836 -8.671 2.597 1.00 13.29 C
ANISOU 5788 CD1 TYR B 209 1239 1649 2162 -102 -91 80 C
ATOM 5789 CE1 TYR B 209 -30.619 -7.801 3.345 1.00 14.67 C
ANISOU 5789 CE1 TYR B 209 1557 1787 2229 -46 23 37 C
ATOM 5790 CZ TYR B 209 -31.989 -7.754 3.143 1.00 14.82 C
ANISOU 5790 CZ TYR B 209 1546 1606 2479 -49 193 -14 C
ATOM 5791 OH TYR B 209 -32.761 -6.892 3.877 1.00 16.04 O
ANISOU 5791 OH TYR B 209 1600 1930 2561 250 139 -168 O
ATOM 5792 CE2 TYR B 209 -32.563 -8.578 2.196 1.00 13.67 C | 
