***    ***
Job options:
ID = 2410311535072900400
JOBID =
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
ATOM 1 N PRO A 1 -27.070 29.560 23.307 1.00 64.58 N
ANISOU 1 N PRO A 1 6986 9930 7620 2937 -2295 -2016 N
ATOM 2 CA PRO A 1 -27.302 30.181 24.607 1.00 67.49 C
ANISOU 2 CA PRO A 1 7087 10627 7929 3407 -2350 -2459 C
ATOM 3 C PRO A 1 -25.991 30.328 25.389 1.00 64.24 C
ANISOU 3 C PRO A 1 7002 9814 7591 3188 -2183 -2335 C
ATOM 4 O PRO A 1 -24.934 29.977 24.878 1.00 59.67 O
ANISOU 4 O PRO A 1 6827 8738 7107 2708 -2045 -1926 O
ATOM 5 CB PRO A 1 -28.222 29.171 25.298 1.00 68.68 C
ANISOU 5 CB PRO A 1 6483 11806 7805 3249 -1986 -2601 C
ATOM 6 CG PRO A 1 -27.728 27.838 24.789 1.00 63.64 C
ANISOU 6 CG PRO A 1 5941 11087 7151 2485 -1614 -2088 C
ATOM 7 CD PRO A 1 -27.281 28.095 23.349 1.00 62.10 C
ANISOU 7 CD PRO A 1 6295 10144 7155 2388 -1839 -1798 C
ATOM 8 N GLN A 2 -26.065 30.864 26.604 1.00 66.39 N
ANISOU 8 N GLN A 2 7069 10360 7796 3556 -2209 -2726 N
ATOM 9 CA GLN A 2 -24.899 30.921 27.475 1.00 63.99 C
ANISOU 9 CA GLN A 2 6985 9809 7518 3329 -2021 -2631 C
ATOM 10 C GLN A 2 -24.957 29.741 28.435 1.00 61.69 C
ANISOU 10 C GLN A 2 6178 10253 7008 2936 -1522 -2556 C
ATOM 11 O GLN A 2 -26.005 29.432 28.997 1.00 64.83 O
ANISOU 11 O GLN A 2 5981 11478 7174 3076 -1421 -2837 O
ATOM 12 CB GLN A 2 -24.859 32.240 28.259 1.00 68.36 C
ANISOU 12 CB GLN A 2 7692 10167 8114 3929 -2382 -3102 C
ATOM 13 CG GLN A 2 -23.570 32.481 29.047 1.00 67.03 C
ANISOU 13 CG GLN A 2 7846 9638 7983 3688 -2264 -2994 C
ATOM 14 CD GLN A 2 -23.771 33.459 30.203 1.00 73.66 C
ANISOU 14 CD GLN A 2 8595 10628 8765 4260 -2489 -3568 C
ATOM 15 OE1 GLN A 2 -24.495 33.173 31.164 1.00 76.74 O
ANISOU 15 OE1 GLN A 2 8360 11868 8931 4474 -2290 -3943 O
ATOM 16 NE2 GLN A 2 -23.128 34.619 30.113 1.00 75.54 N
ANISOU 16 NE2 GLN A 2 9462 10071 9168 4470 -2926 -3651 N
ATOM 17 N ILE A 3 -23.831 29.067 28.619 1.00 56.86 N
ANISOU 17 N ILE A 3 5787 9379 6437 2418 -1240 -2174 N
ATOM 18 CA ILE A 3 -23.817 27.960 29.574 1.00 55.12 C
ANISOU 18 CA ILE A 3 5178 9754 6012 2023 -854 -2055 C
ATOM 19 C ILE A 3 -22.669 28.004 30.597 1.00 52.03 C
ANISOU 19 C ILE A 3 4940 9212 5618 1864 -708 -1981 C
ATOM 20 O ILE A 3 -21.506 28.226 30.258 1.00 49.15 O
ANISOU 20 O ILE A 3 5032 8210 5433 1727 -742 -1763 O
ATOM 21 CB ILE A 3 -23.974 26.566 28.902 1.00 52.46 C
ANISOU 21 CB ILE A 3 4771 9521 5639 1483 -632 -1654 C
ATOM 22 CG1 ILE A 3 -22.642 25.970 28.523 1.00 48.48 C
ANISOU 22 CG1 ILE A 3 4698 8418 5304 1087 -504 -1253 C
ATOM 23 CG2 ILE A 3 -24.878 26.644 27.679 1.00 55.72 C
ANISOU 23 CG2 ILE A 3 5154 9920 6096 1616 -813 -1683 C
ATOM 24 CD1 ILE A 3 -22.781 24.588 27.964 1.00 48.12 C
ANISOU 24 CD1 ILE A 3 4621 8433 5230 622 -343 -934 C
ATOM 25 N THR A 4 -23.053 27.839 31.860 1.00 52.64 N
ANISOU 25 N THR A 4 4586 9974 5441 1876 -557 -2193 N
ATOM 26 CA THR A 4 -22.119 27.703 32.970 1.00 49.37 C
ANISOU 26 CA THR A 4 4215 9590 4953 1670 -392 -2112 C
ATOM 27 C THR A 4 -21.493 26.310 32.956 1.00 44.09 C
ANISOU 27 C THR A 4 3621 8859 4273 1057 -145 -1599 C
ATOM 28 O THR A 4 -21.907 25.434 32.200 1.00 42.62 O
ANISOU 28 O THR A 4 3411 8683 4102 791 -94 -1359 O
ATOM 29 CB THR A 4 -22.838 27.810 34.299 1.00 53.80 C
ANISOU 29 CB THR A 4 4233 11039 5169 1790 -297 -2476 C
ATOM 30 OG1 THR A 4 -23.963 26.922 34.275 1.00 56.28 O
ANISOU 30 OG1 THR A 4 4060 12105 5218 1534 -157 -2431 O
ATOM 31 CG2 THR A 4 -23.287 29.238 34.576 1.00 58.60 C
ANISOU 31 CG2 THR A 4 4779 11704 5784 2495 -580 -3093 C
ATOM 32 N LEU A 5 -20.536 26.093 33.848 1.00 40.14 N
ANISOU 32 N LEU A 5 3208 8312 3732 854 -29 -1461 N
ATOM 33 CA LEU A 5 -19.709 24.893 33.770 1.00 35.36 C
ANISOU 33 CA LEU A 5 2791 7459 3185 387 102 -1002 C
ATOM 34 C LEU A 5 -19.730 24.042 35.043 1.00 36.72 C
ANISOU 34 C LEU A 5 2715 8160 3075 16 241 -840 C
ATOM 35 O LEU A 5 -18.847 23.228 35.267 1.00 34.18 O
ANISOU 35 O LEU A 5 2599 7583 2806 -280 276 -507 O
ATOM 36 CB LEU A 5 -18.283 25.278 33.350 1.00 31.52 C
ANISOU 36 CB LEU A 5 2739 6284 2951 434 50 -884 C
ATOM 37 CG LEU A 5 -18.094 25.813 31.903 1.00 26.77 C
ANISOU 37 CG LEU A 5 2456 5132 2585 583 -92 -884 C
ATOM 38 CD1 LEU A 5 -16.711 26.453 31.694 1.00 23.04 C
ANISOU 38 CD1 LEU A 5 2339 4170 2247 579 -154 -831 C
ATOM 39 CD2 LEU A 5 -18.350 24.724 30.846 1.00 21.85 C
ANISOU 39 CD2 LEU A 5 1875 4389 2036 342 -44 -633 C
ATOM 40 N TRP A 6 -20.769 24.232 35.862 1.00 40.32 N
ANISOU 40 N TRP A 6 2713 9404 3202 35 291 -1092 N
ATOM 41 CA TRP A 6 -20.977 23.432 37.064 1.00 42.60 C
ANISOU 41 CA TRP A 6 2722 10345 3120 -421 407 -921 C
ATOM 42 C TRP A 6 -21.244 21.973 36.709 1.00 42.85 C
ANISOU 42 C TRP A 6 2837 10356 3087 -996 408 -447 C
ATOM 43 O TRP A 6 -20.910 21.065 37.468 1.00 44.48 O
ANISOU 43 O TRP A 6 3104 10682 3115 -1471 410 -98 O
ATOM 44 CB TRP A 6 -22.120 24.024 37.878 1.00 46.65 C
ANISOU 44 CB TRP A 6 2649 11842 3235 -270 465 -1371 C
ATOM 45 CG TRP A 6 -21.844 25.439 38.211 1.00 45.08 C
ANISOU 45 CG TRP A 6 2447 11555 3126 340 388 -1877 C
ATOM 46 CD1 TRP A 6 -22.277 26.534 37.533 1.00 46.24 C
ANISOU 46 CD1 TRP A 6 2616 11492 3460 948 218 -2312 C
ATOM 47 CD2 TRP A 6 -21.054 25.921 39.298 1.00 43.20 C
ANISOU 47 CD2 TRP A 6 2244 11372 2797 396 418 -1997 C
ATOM 48 NE1 TRP A 6 -21.808 27.677 38.132 1.00 47.50 N
ANISOU 48 NE1 TRP A 6 2867 11519 3661 1380 111 -2705 N
ATOM 49 CE2 TRP A 6 -21.054 27.328 39.219 1.00 44.86 C
ANISOU 49 CE2 TRP A 6 2521 11373 3152 1043 255 -2532 C
ATOM 50 CE3 TRP A 6 -20.348 25.300 40.336 1.00 43.69 C
ANISOU 50 CE3 TRP A 6 2318 11622 2662 -45 525 -1698 C
ATOM 51 CZ2 TRP A 6 -20.377 28.131 40.141 1.00 46.54 C
ANISOU 51 CZ2 TRP A 6 2804 11567 3312 1242 218 -2799 C
ATOM 52 CZ3 TRP A 6 -19.664 26.104 41.252 1.00 43.91 C
ANISOU 52 CZ3 TRP A 6 2371 11684 2631 161 518 -1954 C
ATOM 53 CH2 TRP A 6 -19.681 27.502 41.141 1.00 44.82 C
ANISOU 53 CH2 TRP A 6 2548 11592 2890 788 376 -2507 C
ATOM 54 N GLN A 7 -21.804 21.757 35.523 1.00 41.35 N
ANISOU 54 N GLN A 7 2713 9946 3051 -955 356 -424 N
ATOM 55 CA GLN A 7 -22.004 20.426 34.988 1.00 41.00 C
ANISOU 55 CA GLN A 7 2848 9723 3006 -1456 304 -11 C
ATOM 56 C GLN A 7 -21.275 20.335 33.654 1.00 36.58 C
ANISOU 56 C GLN A 7 2742 8274 2884 -1240 222 79 C
ATOM 57 O GLN A 7 -20.936 21.356 33.060 1.00 34.53 O
ANISOU 57 O GLN A 7 2571 7696 2851 -772 212 -175 O
ATOM 58 CB GLN A 7 -23.492 20.183 34.776 1.00 44.54 C
ANISOU 58 CB GLN A 7 2879 10893 3150 -1681 326 -99 C
ATOM 59 CG GLN A 7 -24.323 20.367 36.015 1.00 51.52 C
ANISOU 59 CG GLN A 7 3191 12864 3521 -1885 429 -281 C
ATOM 60 CD GLN A 7 -24.478 19.097 36.825 1.00 58.93 C
ANISOU 60 CD GLN A 7 4123 14187 4079 -2719 408 186 C
ATOM 61 OE1 GLN A 7 -23.597 18.737 37.624 1.00 58.45 O
ANISOU 61 OE1 GLN A 7 4312 13896 4001 -2935 371 450 O
ATOM 62 NE2 GLN A 7 -25.635 18.424 36.659 1.00 62.83 N
ANISOU 62 NE2 GLN A 7 4329 15320 4223 -3237 397 302 N
ATOM 63 N ARG A 8 -20.994 19.125 33.191 1.00 35.82 N
ANISOU 63 N ARG A 8 2954 7773 2882 -1594 130 429 N
ATOM 64 CA ARG A 8 -20.424 18.936 31.818 1.00 32.87 C
ANISOU 64 CA ARG A 8 2942 6682 2863 -1410 60 457 C
ATOM 65 C ARG A 8 -21.302 19.611 30.767 1.00 31.80 C
ANISOU 65 C ARG A 8 2653 6655 2773 -1174 77 218 C
ATOM 66 O ARG A 8 -22.519 19.469 30.819 1.00 33.91 O
ANISOU 66 O ARG A 8 2610 7470 2805 -1353 86 175 O
ATOM 67 CB ARG A 8 -20.351 17.457 31.493 1.00 33.95 C
ANISOU 67 CB ARG A 8 3379 6489 3030 -1829 -88 791 C
ATOM 68 CG ARG A 8 -19.144 16.793 32.117 1.00 36.68 C
ANISOU 68 CG ARG A 8 4035 6424 3477 -1892 -204 1004 C
ATOM 69 CD ARG A 8 -19.279 15.294 32.126 1.00 44.84 C
ANISOU 69 CD ARG A 8 5384 7187 4466 -2354 -452 1347 C
ATOM 70 NE ARG A 8 -17.959 14.685 32.270 1.00 49.47 N
ANISOU 70 NE ARG A 8 6345 7175 5275 -2204 -636 1456 N
ATOM 71 CZ ARG A 8 -17.708 13.504 32.834 1.00 55.48 C
ANISOU 71 CZ ARG A 8 7440 7649 5990 -2531 -941 1779 C
ATOM 72 NH1 ARG A 8 -18.700 12.758 33.336 1.00 61.52 N
ANISOU 72 NH1 ARG A 8 8244 8677 6453 -3156 -1092 2091 N
ATOM 73 NH2 ARG A 8 -16.449 13.063 32.886 1.00 54.74 N
ANISOU 73 NH2 ARG A 8 7650 7018 6132 -2245 -1134 1790 N
ATOM 74 N PRO A 9 -20.689 20.393 29.856 1.00 29.03 N
ANISOU 74 N PRO A 9 2497 5849 2682 -796 60 64 N
ATOM 75 CA PRO A 9 -21.406 21.123 28.820 1.00 29.06 C
ANISOU 75 CA PRO A 9 2430 5867 2743 -549 9 -133 C
ATOM 76 C PRO A 9 -21.819 20.168 27.676 1.00 29.89 C
ANISOU 76 C PRO A 9 2664 5795 2900 -804 -40 23 C
ATOM 77 O PRO A 9 -21.250 20.199 26.572 1.00 26.97 O
ANISOU 77 O PRO A 9 2561 4964 2722 -714 -80 31 O
ATOM 78 CB PRO A 9 -20.391 22.190 28.379 1.00 26.30 C
ANISOU 78 CB PRO A 9 2336 5053 2606 -203 -34 -257 C
ATOM 79 CG PRO A 9 -19.053 21.549 28.578 1.00 25.31 C
ANISOU 79 CG PRO A 9 2461 4567 2590 -351 17 -73 C
ATOM 80 CD PRO A 9 -19.231 20.653 29.810 1.00 25.41 C
ANISOU 80 CD PRO A 9 2331 4890 2434 -627 62 86 C
ATOM 81 N LEU A 10 -22.799 19.319 27.975 1.00 27.90 N
ANISOU 81 N LEU A 10 2542 5107 2951 -406 170 -1251 N
ATOM 82 CA LEU A 10 -23.303 18.315 27.015 1.00 28.25 C
ANISOU 82 CA LEU A 10 2678 5006 3049 -403 137 -1017 C
ATOM 83 C LEU A 10 -24.415 18.909 26.184 1.00 28.19 C
ANISOU 83 C LEU A 10 2682 4848 3182 -234 85 -1177 C
ATOM 84 O LEU A 10 -25.273 19.611 26.718 1.00 31.04 O
ANISOU 84 O LEU A 10 2868 5392 3535 -156 84 -1460 O
ATOM 85 CB LEU A 10 -23.840 17.076 27.745 1.00 29.68 C
ANISOU 85 CB LEU A 10 2705 5523 3048 -591 153 -840 C
ATOM 86 CG LEU A 10 -22.733 16.217 28.361 1.00 31.61 C
ANISOU 86 CG LEU A 10 2964 5838 3209 -766 142 -571 C
ATOM 87 CD1 LEU A 10 -23.336 15.275 29.406 1.00 36.30 C
ANISOU 87 CD1 LEU A 10 3353 6848 3592 -1012 119 -401 C
ATOM 88 CD2 LEU A 10 -21.986 15.440 27.281 1.00 32.97 C
ANISOU 88 CD2 LEU A 10 3345 5626 3557 -713 82 -348 C
ATOM 89 N VAL A 11 -24.396 18.647 24.884 1.00 25.63 N
ANISOU 89 N VAL A 11 2535 4220 2983 -176 31 -1021 N
ATOM 90 CA VAL A 11 -25.418 19.181 23.991 1.00 25.92 C
ANISOU 90 CA VAL A 11 2590 4104 3156 -32 -48 -1118 C
ATOM 91 C VAL A 11 -25.907 18.053 23.088 1.00 24.51 C
ANISOU 91 C VAL A 11 2474 3880 2960 -80 -60 -911 C
ATOM 92 O VAL A 11 -25.243 17.027 22.929 1.00 23.12 O
ANISOU 92 O VAL A 11 2375 3677 2734 -187 -33 -715 O
ATOM 93 CB VAL A 11 -24.893 20.380 23.100 1.00 25.83 C
ANISOU 93 CB VAL A 11 2745 3731 3338 76 -155 -1147 C
ATOM 94 CG1 VAL A 11 -24.566 21.608 23.939 1.00 30.96 C
ANISOU 94 CG1 VAL A 11 3334 4359 4070 139 -191 -1398 C
ATOM 95 CG2 VAL A 11 -23.690 19.958 22.245 1.00 26.54 C
ANISOU 95 CG2 VAL A 11 3026 3650 3406 -18 -145 -901 C
ATOM 96 N ATHR A 12 -27.074 18.246 22.501 0.50 25.02 N
ANISOU 96 N ATHR A 12 2492 3929 3087 10 -118 -979 N
ATOM 97 N BTHR A 12 -27.059 18.258 22.470 0.50 25.19 N
ANISOU 97 N BTHR A 12 2518 3941 3112 11 -120 -977 N
ATOM 98 CA ATHR A 12 -27.579 17.295 21.544 0.50 24.03 C
ANISOU 98 CA ATHR A 12 2429 3749 2953 -36 -143 -814 C
ATOM 99 CA BTHR A 12 -27.598 17.275 21.554 0.50 24.46 C
ANISOU 99 CA BTHR A 12 2480 3808 3005 -38 -143 -814 C
ATOM 100 C ATHR A 12 -26.967 17.630 20.184 0.50 23.96 C
ANISOU 100 C ATHR A 12 2617 3446 3040 5 -206 -714 C
ATOM 101 C BTHR A 12 -27.136 17.603 20.132 0.50 24.32 C
ANISOU 101 C BTHR A 12 2653 3500 3088 10 -212 -718 C
ATOM 102 O ATHR A 12 -26.779 18.808 19.842 0.50 23.99 O
ANISOU 102 O ATHR A 12 2674 3287 3152 93 -283 -772 O
ATOM 103 O BTHR A 12 -27.230 18.762 19.691 0.50 24.67 O
ANISOU 103 O BTHR A 12 2735 3391 3249 113 -303 -783 O
ATOM 104 CB ATHR A 12 -29.107 17.325 21.503 0.50 25.90 C
ANISOU 104 CB ATHR A 12 2505 4151 3184 17 -180 -919 C
ATOM 105 CB BTHR A 12 -29.122 17.236 21.634 0.50 26.38 C
ANISOU 105 CB BTHR A 12 2549 4247 3227 2 -170 -918 C
ATOM 106 OG1ATHR A 12 -29.604 17.072 22.821 0.50 26.68 O
ANISOU 106 OG1ATHR A 12 2379 4622 3137 -63 -112 -1023 O
ATOM 107 OG1BTHR A 12 -29.648 18.530 21.316 0.50 27.88 O
ANISOU 107 OG1BTHR A 12 2700 4325 3569 193 -260 -1107 O
ATOM 108 CG2ATHR A 12 -29.654 16.266 20.555 0.50 24.38 C
ANISOU 108 CG2ATHR A 12 2372 3921 2970 -61 -210 -751 C
ATOM 109 CG2BTHR A 12 -29.553 16.864 23.039 0.50 27.30 C
ANISOU 109 CG2BTHR A 12 2437 4758 3176 -106 -96 -1000 C
ATOM 110 N ILE A 13 -26.618 16.586 19.435 1.00 22.82 N
ANISOU 110 N ILE A 13 2565 3250 2857 -78 -191 -569 N
ATOM 111 CA ILE A 13 -26.111 16.755 18.079 1.00 22.53 C
ANISOU 111 CA ILE A 13 2666 3054 2842 -81 -235 -493 C
ATOM 112 C ILE A 13 -26.886 15.814 17.162 1.00 23.68 C
ANISOU 112 C ILE A 13 2813 3224 2960 -120 -262 -448 C
ATOM 113 O ILE A 13 -27.410 14.767 17.611 1.00 23.35 O
ANISOU 113 O ILE A 13 2706 3268 2898 -173 -242 -438 O
ATOM 114 CB ILE A 13 -24.591 16.490 17.936 1.00 21.37 C
ANISOU 114 CB ILE A 13 2604 2858 2656 -141 -181 -439 C
ATOM 115 CG1 ILE A 13 -24.282 14.988 18.090 1.00 19.32 C
ANISOU 115 CG1 ILE A 13 2326 2635 2380 -195 -138 -408 C
ATOM 116 CG2 ILE A 13 -23.775 17.387 18.914 1.00 21.68 C
ANISOU 116 CG2 ILE A 13 2638 2889 2710 -129 -155 -479 C
ATOM 117 CD1 ILE A 13 -22.784 14.594 17.912 1.00 22.25 C
ANISOU 117 CD1 ILE A 13 2738 2975 2741 -216 -98 -401 C
ATOM 118 N LYS A 14 -26.996 16.221 15.906 1.00 23.34 N
ANISOU 118 N LYS A 14 2836 3122 2910 -122 -329 -405 N
ATOM 119 CA LYS A 14 -27.602 15.375 14.893 1.00 24.44 C
ANISOU 119 CA LYS A 14 2979 3307 3000 -176 -355 -385 C
ATOM 120 C LYS A 14 -26.563 15.261 13.793 1.00 24.58 C
ANISOU 120 C LYS A 14 3076 3330 2934 -249 -343 -363 C
ATOM 121 O LYS A 14 -26.033 16.265 13.336 1.00 24.44 O
ANISOU 121 O LYS A 14 3105 3296 2884 -274 -386 -292 O
ATOM 122 CB LYS A 14 -28.906 15.968 14.381 1.00 25.04 C
ANISOU 122 CB LYS A 14 3004 3408 3102 -133 -458 -364 C
ATOM 123 CG LYS A 14 -29.629 15.004 13.434 1.00 26.91 C
ANISOU 123 CG LYS A 14 3228 3728 3269 -210 -481 -355 C
ATOM 124 CD LYS A 14 -30.887 15.596 12.837 1.00 29.77 C
ANISOU 124 CD LYS A 14 3526 4136 3648 -173 -598 -313 C
ATOM 125 CE LYS A 14 -31.556 14.549 11.954 1.00 32.85 C
ANISOU 125 CE LYS A 14 3899 4634 3949 -276 -611 -318 C
ATOM 126 NZ LYS A 14 -32.816 15.060 11.369 1.00 34.98 N
ANISOU 126 NZ LYS A 14 4087 4979 4224 -249 -733 -263 N
ATOM 127 N ILE A 15 -26.229 14.024 13.442 1.00 25.78 N
ANISOU 127 N ILE A 15 3224 3515 3058 -292 -298 -439 N
ATOM 128 CA ILE A 15 -25.191 13.706 12.456 1.00 27.15 C
ANISOU 128 CA ILE A 15 3413 3771 3133 -350 -264 -509 C
ATOM 129 C ILE A 15 -25.529 12.372 11.790 1.00 28.95 C
ANISOU 129 C ILE A 15 3605 4028 3366 -375 -274 -652 C
ATOM 130 O ILE A 15 -26.002 11.424 12.437 1.00 28.68 O
ANISOU 130 O ILE A 15 3557 3878 3461 -351 -297 -682 O
ATOM 131 CB ILE A 15 -23.761 13.695 13.078 1.00 27.14 C
ANISOU 131 CB ILE A 15 3415 3749 3150 -325 -192 -545 C
ATOM 132 CG1 ILE A 15 -22.715 13.368 11.998 1.00 28.93 C
ANISOU 132 CG1 ILE A 15 3601 4143 3249 -381 -150 -668 C
ATOM 133 CG2 ILE A 15 -23.690 12.745 14.281 1.00 27.16 C
ANISOU 133 CG2 ILE A 15 3392 3627 3300 -265 -178 -573 C
ATOM 134 CD1 ILE A 15 -21.262 13.459 12.455 1.00 28.26 C
ANISOU 134 CD1 ILE A 15 3488 4095 3157 -361 -83 -710 C
ATOM 135 N GLY A 16 -25.376 12.329 10.468 1.00 30.17 N
ANISOU 135 N GLY A 16 3735 4356 3372 -453 -278 -731 N
ATOM 136 CA GLY A 16 -25.717 11.135 9.697 1.00 31.21 C
ANISOU 136 CA GLY A 16 3819 4537 3502 -481 -297 -927 C
ATOM 137 C GLY A 16 -27.102 10.593 9.995 1.00 30.92 C
ANISOU 137 C GLY A 16 3792 4387 3569 -486 -369 -881 C
ATOM 138 O GLY A 16 -27.287 9.368 10.041 1.00 32.09 O
ANISOU 138 O GLY A 16 3925 4427 3842 -484 -410 -1021 O
ATOM 139 N GLY A 17 -28.075 11.493 10.159 1.00 29.28 N
ANISOU 139 N GLY A 17 3595 4205 3325 -496 -409 -696 N
ATOM 140 CA GLY A 17 -29.454 11.139 10.520 1.00 28.39 C
ANISOU 140 CA GLY A 17 3453 4055 3278 -508 -470 -639 C
ATOM 141 C GLY A 17 -29.690 10.680 11.971 1.00 26.56 C
ANISOU 141 C GLY A 17 3207 3692 3193 -476 -467 -586 C
ATOM 142 O GLY A 17 -30.814 10.337 12.332 1.00 26.97 O
ANISOU 142 O GLY A 17 3205 3773 3268 -522 -515 -534 O
ATOM 143 N GLN A 18 -28.643 10.682 12.796 1.00 24.41 N
ANISOU 143 N GLN A 18 2961 3326 2989 -426 -416 -583 N
ATOM 144 CA GLN A 18 -28.704 10.119 14.152 1.00 23.40 C
ANISOU 144 CA GLN A 18 2804 3117 2969 -445 -430 -507 C
ATOM 145 C GLN A 18 -28.580 11.208 15.193 1.00 21.73 C
ANISOU 145 C GLN A 18 2562 2971 2724 -389 -372 -425 C
ATOM 146 O GLN A 18 -27.871 12.199 14.977 1.00 21.67 O
ANISOU 146 O GLN A 18 2593 2964 2676 -319 -327 -441 O
ATOM 147 CB GLN A 18 -27.561 9.130 14.363 1.00 24.11 C
ANISOU 147 CB GLN A 18 2926 3044 3191 -438 -451 -571 C
ATOM 148 CG GLN A 18 -27.577 7.995 13.367 1.00 28.43 C
ANISOU 148 CG GLN A 18 3485 3495 3822 -464 -528 -737 C
ATOM 149 CD GLN A 18 -26.385 7.119 13.529 1.00 32.69 C
ANISOU 149 CD GLN A 18 4029 3850 4543 -403 -576 -854 C
ATOM 150 OE1 GLN A 18 -26.188 6.543 14.600 1.00 34.96 O
ANISOU 150 OE1 GLN A 18 4313 3982 4988 -429 -659 -723 O
ATOM 151 NE2 GLN A 18 -25.559 7.011 12.475 1.00 33.94 N
ANISOU 151 NE2 GLN A 18 4167 4056 4674 -329 -537 -1104 N
ATOM 152 N LEU A 19 -29.192 10.973 16.353 1.00 20.42 N
ANISOU 152 N LEU A 19 2313 2879 2568 -445 -385 -345 N
ATOM 153 CA LEU A 19 -29.157 11.943 17.444 1.00 19.59 C
ANISOU 153 CA LEU A 19 2136 2892 2417 -398 -328 -332 C
ATOM 154 C LEU A 19 -28.240 11.416 18.513 1.00 19.62 C
ANISOU 154 C LEU A 19 2134 2871 2449 -458 -314 -259 C
ATOM 155 O LEU A 19 -28.403 10.273 18.944 1.00 19.69 O
ANISOU 155 O LEU A 19 2117 2862 2502 -589 -386 -152 O
ATOM 156 CB LEU A 19 -30.555 12.155 18.051 1.00 19.59 C
ANISOU 156 CB LEU A 19 1977 3117 2347 -434 -341 -332 C
ATOM 157 CG LEU A 19 -31.666 12.515 17.067 1.00 23.70 C
ANISOU 157 CG LEU A 19 2467 3683 2854 -384 -388 -382 C
ATOM 158 CD1 LEU A 19 -33.032 12.479 17.804 1.00 24.64 C
ANISOU 158 CD1 LEU A 19 2380 4086 2896 -438 -400 -398 C
ATOM 159 CD2 LEU A 19 -31.380 13.893 16.423 1.00 25.91 C
ANISOU 159 CD2 LEU A 19 2801 3870 3174 -221 -398 -448 C
ATOM 160 N LYS A 20 -27.320 12.263 18.961 1.00 19.07 N
ANISOU 160 N LYS A 20 2084 2799 2364 -385 -248 -293 N
ATOM 161 CA LYS A 20 -26.319 11.877 19.955 1.00 20.67 C
ANISOU 161 CA LYS A 20 2275 2996 2582 -438 -238 -217 C
ATOM 162 C LYS A 20 -26.147 13.006 20.950 1.00 20.68 C
ANISOU 162 C LYS A 20 2201 3159 2496 -407 -165 -271 C
ATOM 163 O LYS A 20 -26.574 14.124 20.707 1.00 21.62 O
ANISOU 163 O LYS A 20 2308 3308 2600 -308 -140 -393 O
ATOM 164 CB LYS A 20 -24.961 11.586 19.279 1.00 20.08 C
ANISOU 164 CB LYS A 20 2305 2731 2592 -374 -236 -247 C
ATOM 165 CG LYS A 20 -24.999 10.379 18.313 1.00 23.84 C
ANISOU 165 CG LYS A 20 2828 3047 3182 -384 -318 -277 C
ATOM 166 CD LYS A 20 -23.631 10.111 17.719 1.00 29.46 C
ANISOU 166 CD LYS A 20 3582 3646 3966 -301 -307 -379 C
ATOM 167 CE LYS A 20 -23.654 8.866 16.823 1.00 35.57 C
ANISOU 167 CE LYS A 20 4366 4265 4883 -287 -404 -494 C
ATOM 168 NZ LYS A 20 -24.074 7.649 17.577 1.00 39.73 N
ANISOU 168 NZ LYS A 20 4871 4637 5588 -377 -562 -362 N
ATOM 169 N GLU A 21 -25.515 12.695 22.073 1.00 21.39 N
ANISOU 169 N GLU A 21 2233 3344 2549 -496 -158 -185 N
ATOM 170 CA GLU A 21 -25.080 13.695 23.052 1.00 23.18 C
ANISOU 170 CA GLU A 21 2389 3732 2688 -481 -87 -267 C
ATOM 171 C GLU A 21 -23.585 13.849 22.902 1.00 21.22 C
ANISOU 171 C GLU A 21 2244 3326 2494 -436 -67 -246 C
ATOM 172 O GLU A 21 -22.887 12.838 22.729 1.00 21.69 O
ANISOU 172 O GLU A 21 2347 3263 2631 -471 -119 -126 O
ATOM 173 CB GLU A 21 -25.354 13.224 24.472 1.00 24.85 C
ANISOU 173 CB GLU A 21 2429 4249 2763 -661 -94 -167 C
ATOM 174 CG GLU A 21 -26.837 13.218 24.842 1.00 32.97 C
ANISOU 174 CG GLU A 21 3286 5571 3671 -738 -92 -219 C
ATOM 175 CD GLU A 21 -27.271 14.482 25.549 1.00 41.92 C
ANISOU 175 CD GLU A 21 4256 6980 4692 -661 -7 -487 C
ATOM 176 OE1 GLU A 21 -26.715 15.570 25.274 1.00 44.89 O
ANISOU 176 OE1 GLU A 21 4711 7187 5158 -490 26 -664 O
ATOM 177 OE2 GLU A 21 -28.175 14.381 26.405 1.00 47.16 O
ANISOU 177 OE2 GLU A 21 4691 8050 5179 -787 13 -535 O
ATOM 178 N ALA A 22 -23.101 15.090 22.978 1.00 20.15 N
ANISOU 178 N ALA A 22 2132 3186 2339 -361 -14 -373 N
ATOM 179 CA ALA A 22 -21.673 15.372 22.835 1.00 19.55 C
ANISOU 179 CA ALA A 22 2135 3007 2284 -343 9 -355 C
ATOM 180 C ALA A 22 -21.236 16.533 23.724 1.00 20.00 C
ANISOU 180 C ALA A 22 2149 3168 2283 -348 51 -463 C
ATOM 181 O ALA A 22 -22.049 17.411 24.059 1.00 20.66 O
ANISOU 181 O ALA A 22 2170 3322 2359 -303 51 -621 O
ATOM 182 CB ALA A 22 -21.333 15.667 21.379 1.00 18.75 C
ANISOU 182 CB ALA A 22 2162 2721 2243 -271 -3 -380 C
ATOM 183 N LEU A 23 -19.953 16.522 24.089 1.00 19.77 N
ANISOU 183 N LEU A 23 2135 3148 2229 -392 74 -408 N
ATOM 184 CA LEU A 23 -19.369 17.469 25.011 1.00 21.94 C
ANISOU 184 CA LEU A 23 2363 3535 2439 -429 107 -503 C
ATOM 185 C LEU A 23 -18.795 18.654 24.239 1.00 21.79 C
ANISOU 185 C LEU A 23 2464 3327 2487 -380 88 -581 C
ATOM 186 O LEU A 23 -17.971 18.468 23.321 1.00 22.77 O
ANISOU 186 O LEU A 23 2677 3344 2630 -386 83 -485 O
ATOM 187 CB LEU A 23 -18.257 16.751 25.804 1.00 22.77 C
ANISOU 187 CB LEU A 23 2410 3764 2478 -527 119 -361 C
ATOM 188 CG LEU A 23 -17.593 17.381 27.022 1.00 25.37 C
ANISOU 188 CG LEU A 23 2648 4300 2690 -619 154 -418 C
ATOM 189 CD1 LEU A 23 -18.544 17.410 28.221 1.00 28.96 C
ANISOU 189 CD1 LEU A 23 2929 5068 3005 -708 173 -500 C
ATOM 190 CD2 LEU A 23 -16.305 16.597 27.350 1.00 27.03 C
ANISOU 190 CD2 LEU A 23 2833 4554 2885 -686 134 -228 C
ATOM 191 N LEU A 24 -19.226 19.875 24.579 1.00 22.65 N
ANISOU 191 N LEU A 24 2560 3406 2641 -342 55 -761 N
ATOM 192 CA LEU A 24 -18.538 21.060 24.034 1.00 22.59 C
ANISOU 192 CA LEU A 24 2669 3197 2719 -349 -13 -789 C
ATOM 193 C LEU A 24 -17.164 21.168 24.696 1.00 23.46 C
ANISOU 193 C LEU A 24 2765 3410 2738 -459 34 -754 C
ATOM 194 O LEU A 24 -17.052 21.426 25.910 1.00 24.81 O
ANISOU 194 O LEU A 24 2832 3750 2847 -496 67 -882 O
ATOM 195 CB LEU A 24 -19.347 22.335 24.242 1.00 23.76 C
ANISOU 195 CB LEU A 24 2803 3211 3015 -261 -117 -1012 C
ATOM 196 CG LEU A 24 -20.783 22.348 23.704 1.00 24.16 C
ANISOU 196 CG LEU A 24 2828 3182 3172 -131 -182 -1078 C
ATOM 197 CD1 LEU A 24 -21.438 23.666 24.107 1.00 27.81 C
ANISOU 197 CD1 LEU A 24 3234 3507 3827 -10 -310 -1362 C
ATOM 198 CD2 LEU A 24 -20.803 22.186 22.225 1.00 23.54 C
ANISOU 198 CD2 LEU A 24 2888 2916 3139 -143 -251 -866 C
ATOM 199 N ASP A 25 -16.116 20.996 23.900 1.00 22.43 N
ANISOU 199 N ASP A 25 2715 3230 2578 -523 37 -599 N
ATOM 200 CA ASP A 25 -14.788 20.763 24.458 1.00 21.52 C
ANISOU 200 CA ASP A 25 2553 3264 2360 -617 93 -536 C
ATOM 201 C ASP A 25 -13.735 21.745 23.952 1.00 22.11 C
ANISOU 201 C ASP A 25 2708 3266 2427 -729 45 -496 C
ATOM 202 O ASP A 25 -13.077 21.483 22.943 1.00 20.94 O
ANISOU 202 O ASP A 25 2591 3136 2229 -777 51 -375 O
ATOM 203 CB ASP A 25 -14.359 19.323 24.155 1.00 22.16 C
ANISOU 203 CB ASP A 25 2581 3440 2398 -591 145 -402 C
ATOM 204 CG ASP A 25 -13.102 18.907 24.908 1.00 21.90 C
ANISOU 204 CG ASP A 25 2456 3577 2287 -656 180 -336 C
ATOM 205 OD1 ASP A 25 -12.439 19.791 25.469 1.00 23.62 O
ANISOU 205 OD1 ASP A 25 2668 3858 2448 -747 183 -379 O
ATOM 206 OD2 ASP A 25 -12.805 17.691 24.975 1.00 23.70 O
ANISOU 206 OD2 ASP A 25 2611 3860 2535 -613 180 -245 O
ATOM 207 N THR A 26 -13.542 22.849 24.673 1.00 22.10 N
ANISOU 207 N THR A 26 2718 3219 2462 -792 -8 -612 N
ATOM 208 CA THR A 26 -12.579 23.872 24.248 1.00 22.99 C
ANISOU 208 CA THR A 26 2916 3237 2583 -943 -92 -549 C
ATOM 209 C THR A 26 -11.109 23.379 24.244 1.00 22.78 C
ANISOU 209 C THR A 26 2825 3442 2387 -1063 -8 -420 C
ATOM 210 O THR A 26 -10.242 23.997 23.588 1.00 23.04 O
ANISOU 210 O THR A 26 2908 3472 2374 -1223 -64 -310 O
ATOM 211 CB THR A 26 -12.708 25.180 25.071 1.00 25.00 C
ANISOU 211 CB THR A 26 3194 3343 2961 -980 -201 -744 C
ATOM 212 OG1 THR A 26 -12.400 24.934 26.454 1.00 22.69 O
ANISOU 212 OG1 THR A 26 2770 3292 2561 -990 -102 -889 O
ATOM 213 CG2 THR A 26 -14.118 25.767 24.966 1.00 25.47 C
ANISOU 213 CG2 THR A 26 3288 3157 3233 -830 -317 -914 C
ATOM 214 N GLY A 27 -10.842 22.273 24.948 1.00 20.49 N
ANISOU 214 N GLY A 27 2411 3364 2012 -1000 100 -415 N
ATOM 215 CA GLY A 27 -9.501 21.675 24.993 1.00 21.85 C
ANISOU 215 CA GLY A 27 2483 3755 2063 -1062 161 -315 C
ATOM 216 C GLY A 27 -9.220 20.696 23.856 1.00 22.23 C
ANISOU 216 C GLY A 27 2493 3862 2091 -990 197 -237 C
ATOM 217 O GLY A 27 -8.118 20.185 23.747 1.00 22.28 O
ANISOU 217 O GLY A 27 2386 4056 2021 -1007 237 -200 O
ATOM 218 N ALA A 28 -10.223 20.435 23.014 1.00 21.20 N
ANISOU 218 N ALA A 28 2433 3592 2031 -902 179 -247 N
ATOM 219 CA ALA A 28 -10.073 19.551 21.867 1.00 21.53 C
ANISOU 219 CA ALA A 28 2429 3701 2051 -837 208 -235 C
ATOM 220 C ALA A 28 -9.888 20.390 20.589 1.00 22.96 C
ANISOU 220 C ALA A 28 2675 3911 2139 -984 170 -179 C
ATOM 221 O ALA A 28 -10.784 21.158 20.227 1.00 22.55 O
ANISOU 221 O ALA A 28 2749 3671 2146 -1023 87 -141 O
ATOM 222 CB ALA A 28 -11.338 18.685 21.729 1.00 19.69 C
ANISOU 222 CB ALA A 28 2221 3328 1932 -683 200 -270 C
ATOM 223 N ASP A 29 -8.765 20.213 19.898 1.00 24.55 N
ANISOU 223 N ASP A 29 2766 4371 2192 -1072 213 -169 N
ATOM 224 CA ASP A 29 -8.554 20.855 18.588 1.00 26.47 C
ANISOU 224 CA ASP A 29 3026 4749 2281 -1266 173 -83 C
ATOM 225 C ASP A 29 -9.599 20.374 17.581 1.00 27.37 C
ANISOU 225 C ASP A 29 3177 4805 2418 -1187 160 -112 C
ATOM 226 O ASP A 29 -10.131 21.182 16.807 1.00 28.16 O
ANISOU 226 O ASP A 29 3379 4841 2480 -1335 61 19 O
ATOM 227 CB ASP A 29 -7.157 20.515 18.030 1.00 27.83 C
ANISOU 227 CB ASP A 29 2997 5334 2244 -1364 252 -124 C
ATOM 228 CG ASP A 29 -6.034 21.050 18.885 1.00 29.91 C
ANISOU 228 CG ASP A 29 3206 5709 2448 -1484 258 -75 C
ATOM 229 OD1 ASP A 29 -6.288 21.955 19.732 1.00 30.79 O
ANISOU 229 OD1 ASP A 29 3461 5584 2653 -1560 182 9 O
ATOM 230 OD2 ASP A 29 -4.882 20.565 18.710 1.00 28.75 O
ANISOU 230 OD2 ASP A 29 2851 5909 2165 -1497 335 -153 O
ATOM 231 N ASP A 30 -9.881 19.063 17.609 1.00 26.52 N
ANISOU 231 N ASP A 30 2984 4705 2389 -968 231 -266 N
ATOM 232 CA AASP A 30 -10.735 18.372 16.629 0.50 27.22 C
ANISOU 232 CA AASP A 30 3069 4786 2487 -885 232 -344 C
ATOM 233 CA BASP A 30 -10.803 18.501 16.639 0.50 27.24 C
ANISOU 233 CA BASP A 30 3090 4771 2491 -900 223 -325 C
ATOM 234 C ASP A 30 -11.939 17.692 17.268 1.00 25.42 C
ANISOU 234 C ASP A 30 2918 4269 2472 -690 211 -385 C
ATOM 235 O ASP A 30 -11.898 17.270 18.426 1.00 25.75 O
ANISOU 235 O ASP A 30 2945 4201 2637 -586 218 -396 O
ATOM 236 CB AASP A 30 -9.953 17.281 15.866 0.50 28.66 C
ANISOU 236 CB AASP A 30 3044 5268 2580 -810 313 -551 C
ATOM 237 CB BASP A 30 -10.047 17.720 15.552 0.50 28.92 C
ANISOU 237 CB BASP A 30 3109 5335 2543 -903 296 -489 C
ATOM 238 CG AASP A 30 -8.479 17.585 15.738 0.50 30.56 C
ANISOU 238 CG AASP A 30 3121 5859 2632 -940 366 -575 C
ATOM 239 CG BASP A 30 -9.044 18.587 14.799 0.50 31.48 C
ANISOU 239 CG BASP A 30 3349 6024 2589 -1179 304 -400 C
ATOM 240 OD1AASP A 30 -8.136 18.746 15.430 0.50 34.05 O
ANISOU 240 OD1AASP A 30 3610 6431 2896 -1202 333 -395 O
ATOM 241 OD1BASP A 30 -9.433 19.620 14.201 0.50 32.66 O
ANISOU 241 OD1BASP A 30 3609 6170 2629 -1408 214 -192 O
ATOM 242 OD2AASP A 30 -7.660 16.659 15.939 0.50 31.31 O
ANISOU 242 OD2AASP A 30 3028 6095 2773 -785 418 -767 O
ATOM 243 OD2BASP A 30 -7.854 18.225 14.784 0.50 36.30 O
ANISOU 243 OD2BASP A 30 3763 6940 3088 -1182 381 -526 O
ATOM 244 N THR A 31 -12.998 17.549 16.501 1.00 25.23 N
ANISOU 244 N THR A 31 2954 4169 2464 -670 176 -391 N
ATOM 245 CA THR A 31 -14.176 16.823 16.930 1.00 23.21 C
ANISOU 245 CA THR A 31 2745 3698 2377 -518 154 -429 C
ATOM 246 C THR A 31 -13.957 15.320 16.791 1.00 24.09 C
ANISOU 246 C THR A 31 2741 3837 2574 -373 180 -589 C
ATOM 247 O THR A 31 -13.468 14.859 15.766 1.00 25.49 O
ANISOU 247 O THR A 31 2819 4200 2667 -372 209 -732 O
ATOM 248 CB THR A 31 -15.321 17.288 16.058 1.00 24.14 C
ANISOU 248 CB THR A 31 2952 3749 2471 -567 92 -372 C
ATOM 249 OG1 THR A 31 -15.563 18.671 16.382 1.00 21.96 O
ANISOU 249 OG1 THR A 31 2780 3353 2210 -663 13 -234 O
ATOM 250 CG2 THR A 31 -16.603 16.400 16.245 1.00 20.06 C
ANISOU 250 CG2 THR A 31 2456 3073 2094 -432 72 -428 C
ATOM 251 N VAL A 32 -14.294 14.563 17.826 1.00 22.95 N
ANISOU 251 N VAL A 32 2594 3523 2601 -266 147 -574 N
ATOM 252 CA VAL A 32 -14.085 13.115 17.786 1.00 24.29 C
ANISOU 252 CA VAL A 32 2667 3631 2933 -129 104 -698 C
ATOM 253 C VAL A 32 -15.325 12.452 18.345 1.00 23.00 C
ANISOU 253 C VAL A 32 2567 3250 2923 -94 24 -618 C
ATOM 254 O VAL A 32 -15.701 12.690 19.489 1.00 22.52 O
ANISOU 254 O VAL A 32 2538 3135 2882 -139 4 -467 O
ATOM 255 CB VAL A 32 -12.921 12.617 18.679 1.00 25.70 C
ANISOU 255 CB VAL A 32 2733 3824 3208 -64 79 -693 C
ATOM 256 CG1 VAL A 32 -12.427 11.243 18.185 1.00 26.92 C
ANISOU 256 CG1 VAL A 32 2750 3926 3553 103 5 -899 C
ATOM 257 CG2 VAL A 32 -11.816 13.613 18.731 1.00 26.32 C
ANISOU 257 CG2 VAL A 32 2769 4122 3108 -157 159 -672 C
ATOM 258 N LEU A 33 -15.915 11.581 17.539 1.00 25.80 N
ANISOU 258 N LEU A 33 2741 3295 3767 -426 -13 -530 N
ATOM 259 CA LEU A 33 -17.106 10.874 17.929 1.00 26.49 C
ANISOU 259 CA LEU A 33 2746 3119 4199 -559 -144 -453 C
ATOM 260 C LEU A 33 -16.842 9.390 18.097 1.00 29.59 C
ANISOU 260 C LEU A 33 3165 3186 4892 -541 -366 -506 C
ATOM 261 O LEU A 33 -15.985 8.820 17.404 1.00 29.43 O
ANISOU 261 O LEU A 33 3279 3128 4774 -307 -501 -804 O
ATOM 262 CB LEU A 33 -18.202 11.100 16.874 1.00 27.82 C
ANISOU 262 CB LEU A 33 2890 3260 4420 -590 -336 -578 C
ATOM 263 CG LEU A 33 -18.584 12.569 16.616 1.00 26.90 C
ANISOU 263 CG LEU A 33 2752 3388 4078 -599 -209 -513 C
ATOM 264 CD1 LEU A 33 -19.774 12.663 15.650 1.00 27.75 C
ANISOU 264 CD1 LEU A 33 2806 3445 4290 -639 -440 -598 C
ATOM 265 CD2 LEU A 33 -18.898 13.301 17.935 1.00 26.08 C
ANISOU 265 CD2 LEU A 33 2556 3365 3989 -630 1 -279 C
ATOM 266 N GLU A 34 -17.598 8.758 18.993 1.00 31.26 N
ANISOU 266 N GLU A 34 3218 3189 5469 -752 -436 -185 N
ATOM 267 CA GLU A 34 -17.475 7.328 19.194 1.00 36.85 C
ANISOU 267 CA GLU A 34 3936 3464 6603 -809 -778 -132 C
ATOM 268 C GLU A 34 -17.907 6.608 17.919 1.00 40.87 C
ANISOU 268 C GLU A 34 4574 3600 7356 -731 -1291 -512 C
ATOM 269 O GLU A 34 -18.474 7.221 16.994 1.00 40.63 O
ANISOU 269 O GLU A 34 4571 3714 7154 -686 -1327 -720 O
ATOM 270 CB GLU A 34 -18.325 6.870 20.371 1.00 38.98 C
ANISOU 270 CB GLU A 34 3913 3663 7234 -1121 -768 469 C
ATOM 271 CG GLU A 34 -18.080 7.636 21.662 1.00 38.72 C
ANISOU 271 CG GLU A 34 3774 4093 6845 -1098 -289 796 C
ATOM 272 CD GLU A 34 -19.132 7.302 22.728 1.00 46.45 C
ANISOU 272 CD GLU A 34 4367 5247 8036 -1329 -198 1464 C
ATOM 273 OE1 GLU A 34 -20.317 7.149 22.371 1.00 49.98 O
ANISOU 273 OE1 GLU A 34 4545 5653 8791 -1521 -344 1684 O
ATOM 274 OE2 GLU A 34 -18.779 7.195 23.920 1.00 49.60 O
ANISOU 274 OE2 GLU A 34 4686 5890 8268 -1309 18 1819 O
ATOM 275 N GLU A 35 -17.626 5.313 17.865 1.00 45.69 N
ANISOU 275 N GLU A 35 5295 3699 8366 -678 -1761 -631 N
ATOM 276 CA GLU A 35 -17.962 4.495 16.713 1.00 51.04 C
ANISOU 276 CA GLU A 35 6178 3914 9301 -513 -2415 -1099 C
ATOM 277 C GLU A 35 -19.363 4.789 16.147 1.00 52.22 C
ANISOU 277 C GLU A 35 6191 3987 9662 -774 -2652 -1008 C
ATOM 278 O GLU A 35 -20.365 4.765 16.859 1.00 52.55 O
ANISOU 278 O GLU A 35 5891 3949 10125 -1213 -2656 -420 O
ATOM 279 CB GLU A 35 -17.804 3.004 17.068 1.00 57.00 C
ANISOU 279 CB GLU A 35 7018 3932 10710 -552 -3053 -1067 C
ATOM 280 CG GLU A 35 -17.808 2.043 15.870 1.00 65.50 C
ANISOU 280 CG GLU A 35 8448 4431 12008 -181 -3879 -1769 C
ATOM 281 CD GLU A 35 -16.939 2.547 14.727 1.00 67.27 C
ANISOU 281 CD GLU A 35 8951 5185 11424 491 -3656 -2508 C
ATOM 282 OE1 GLU A 35 -15.731 2.812 14.942 1.00 66.36 O
ANISOU 282 OE1 GLU A 35 8850 5516 10847 820 -3184 -2600 O
ATOM 283 OE2 GLU A 35 -17.476 2.699 13.612 1.00 71.02 O
ANISOU 283 OE2 GLU A 35 9583 5696 11707 684 -3951 -2930 O
ATOM 284 N MET A 36 -19.401 5.084 14.857 1.00 53.46 N
ANISOU 284 N MET A 36 6574 4261 9476 -464 -2829 -1555 N
ATOM 285 CA MET A 36 -20.649 5.211 14.119 1.00 56.87 C
ANISOU 285 CA MET A 36 6942 4542 10125 -641 -3214 -1586 C
ATOM 286 C MET A 36 -20.326 5.064 12.643 1.00 60.55 C
ANISOU 286 C MET A 36 7799 5035 10173 -123 -3600 -2352 C
ATOM 287 O MET A 36 -19.163 5.190 12.243 1.00 60.41 O
ANISOU 287 O MET A 36 7995 5396 9563 367 -3342 -2739 O
ATOM 288 CB MET A 36 -21.308 6.566 14.392 1.00 52.09 C
ANISOU 288 CB MET A 36 6046 4483 9264 -867 -2640 -1190 C
ATOM 289 CG MET A 36 -20.508 7.770 13.916 1.00 47.26 C
ANISOU 289 CG MET A 36 5577 4497 7883 -556 -2109 -1417 C
ATOM 290 SD MET A 36 -21.376 9.327 14.151 1.00 43.65 S
ANISOU 290 SD MET A 36 4851 4482 7250 -766 -1667 -1037 S
ATOM 291 CE MET A 36 -22.924 8.971 13.303 1.00 46.95 C
ANISOU 291 CE MET A 36 5149 4587 8103 -951 -2270 -1069 C
ATOM 292 N ASN A 37 -21.340 4.786 11.834 1.00 65.61 N
ANISOU 292 N ASN A 37 8501 5342 11087 -193 -4230 -2548 N
ATOM 293 CA ASN A 37 -21.153 4.814 10.398 1.00 69.65 C
ANISOU 293 CA ASN A 37 9385 6032 11048 352 -4565 -3270 C
ATOM 294 C ASN A 37 -21.377 6.218 9.881 1.00 65.78 C
ANISOU 294 C ASN A 37 8776 6278 9937 353 -4012 -3127 C
ATOM 295 O ASN A 37 -22.485 6.767 9.956 1.00 65.03 O
ANISOU 295 O ASN A 37 8431 6154 10123 -52 -4030 -2761 O
ATOM 296 CB ASN A 37 -22.053 3.807 9.666 1.00 77.28 C
ANISOU 296 CB ASN A 37 10564 6234 12566 357 -5666 -3661 C
ATOM 297 CG ASN A 37 -21.643 3.600 8.206 1.00 82.80 C
ANISOU 297 CG ASN A 37 11761 7125 12573 1134 -6109 -4581 C
ATOM 298 OD1 ASN A 37 -20.704 4.245 7.710 1.00 80.58 O
ANISOU 298 OD1 ASN A 37 11585 7670 11363 1649 -5505 -4821 O
ATOM 299 ND2 ASN A 37 -22.352 2.691 7.510 1.00 90.52 N
ANISOU 299 ND2 ASN A 37 13025 7374 13995 1239 -7216 -5066 N
ATOM 300 N LEU A 38 -20.296 6.816 9.400 1.00 64.35 N
ANISOU 300 N LEU A 38 8721 6782 8947 801 -3522 -3336 N
ATOM 301 CA LEU A 38 -20.406 7.990 8.569 1.00 63.16 C
ANISOU 301 CA LEU A 38 8540 7292 8166 905 -3210 -3278 C
ATOM 302 C LEU A 38 -20.227 7.543 7.135 1.00 70.09 C
ANISOU 302 C LEU A 38 9772 8391 8466 1540 -3680 -3960 C
ATOM 303 O LEU A 38 -19.319 6.760 6.823 1.00 74.11 O
ANISOU 303 O LEU A 38 10517 8983 8660 2112 -3823 -4458 O
ATOM 304 CB LEU A 38 -19.393 9.068 8.941 1.00 58.16 C
ANISOU 304 CB LEU A 38 7727 7331 7039 911 -2410 -2893 C
ATOM 305 CG LEU A 38 -19.749 9.949 10.134 1.00 51.79 C
ANISOU 305 CG LEU A 38 6619 6455 6604 370 -1975 -2272 C
ATOM 306 CD1 LEU A 38 -18.764 11.085 10.223 1.00 50.35 C
ANISOU 306 CD1 LEU A 38 6328 6867 5936 410 -1408 -1963 C
ATOM 307 CD2 LEU A 38 -21.156 10.502 10.029 1.00 50.92 C
ANISOU 307 CD2 LEU A 38 6367 6178 6801 42 -2158 -2062 C
ATOM 308 N PRO A 39 -21.097 8.033 6.248 1.00 72.27 N
ANISOU 308 N PRO A 39 10096 8808 8557 1520 -3948 -4018 N
ATOM 309 CA PRO A 39 -20.985 7.520 4.899 1.00 79.75 C
ANISOU 309 CA PRO A 39 11426 9976 8898 2199 -4483 -4730 C
ATOM 310 C PRO A 39 -19.866 8.278 4.189 1.00 80.10 C
ANISOU 310 C PRO A 39 11445 11134 7855 2720 -3850 -4691 C
ATOM 311 O PRO A 39 -19.555 9.419 4.574 1.00 74.72 O
ANISOU 311 O PRO A 39 10438 10920 7031 2373 -3158 -4022 O
ATOM 312 CB PRO A 39 -22.363 7.807 4.289 1.00 81.54 C
ANISOU 312 CB PRO A 39 11669 9954 9361 1924 -5016 -4713 C
ATOM 313 CG PRO A 39 -22.982 8.878 5.136 1.00 74.22 C
ANISOU 313 CG PRO A 39 10300 9030 8871 1214 -4491 -3911 C
ATOM 314 CD PRO A 39 -22.133 9.077 6.374 1.00 68.98 C
ANISOU 314 CD PRO A 39 9408 8429 8372 1001 -3794 -3497 C
ATOM 315 N GLY A 40 -19.234 7.626 3.213 1.00 87.03 N
ANISOU 315 N GLY A 40 12634 12435 7997 3569 -4120 -5371 N
ATOM 316 CA GLY A 40 -18.242 8.290 2.370 1.00 89.25 C
ANISOU 316 CA GLY A 40 12810 13962 7137 4141 -3547 -5264 C
ATOM 317 C GLY A 40 -16.793 7.887 2.573 1.00 90.51 C
ANISOU 317 C GLY A 40 12872 14667 6850 4701 -3096 -5379 C
ATOM 318 O GLY A 40 -16.494 6.876 3.224 1.00 91.29 O
ANISOU 318 O GLY A 40 13118 14120 7449 4831 -3363 -5771 O
ATOM 319 N ARG A 41 -15.895 8.688 1.998 1.00 91.43 N
ANISOU 319 N ARG A 41 12690 16002 6048 5020 -2439 -4959 N
ATOM 320 CA ARG A 41 -14.455 8.462 2.112 1.00 93.14 C
ANISOU 320 CA ARG A 41 12664 16966 5757 5562 -1915 -4912 C
ATOM 321 C ARG A 41 -13.892 8.963 3.444 1.00 84.25 C
ANISOU 321 C ARG A 41 11144 15557 5311 4828 -1369 -4169 C
ATOM 322 O ARG A 41 -14.372 9.981 4.018 1.00 77.39 O
ANISOU 322 O ARG A 41 10064 14416 4927 3980 -1148 -3463 O
ATOM 323 CB ARG A 41 -13.702 9.103 0.948 1.00 99.94 C
ANISOU 323 CB ARG A 41 13245 19374 5352 6191 -1430 -4614 C
ATOM 324 CG ARG A 41 -13.911 10.612 0.821 1.00 96.91 C
ANISOU 324 CG ARG A 41 12457 19475 4889 5464 -980 -3547 C
ATOM 325 CD ARG A 41 -13.528 11.069 -0.608 1.00106.63 C
ANISOU 325 CD ARG A 41 13511 22200 4803 6150 -741 -3333 C
ATOM 326 NE ARG A 41 -12.979 12.430 -0.570 1.00105.19 N
ANISOU 326 NE ARG A 41 12707 22774 4485 5572 -109 -2066 N
ATOM 327 CZ ARG A 41 -12.495 13.105 -1.630 1.00112.82 C
ANISOU 327 CZ ARG A 41 13294 25158 4413 5918 253 -1425 C
ATOM 328 NH1 ARG A 41 -12.487 12.556 -2.850 1.00121.54 N
ANISOU 328 NH1 ARG A 41 14599 27221 4358 6954 115 -2005 N
ATOM 329 NH2 ARG A 41 -12.017 14.339 -1.466 1.00111.12 N
ANISOU 329 NH2 ARG A 41 12492 25412 4317 5238 698 -168 N
ATOM 330 N TRP A 42 -12.878 8.233 3.928 1.00 84.64 N
ANISOU 330 N TRP A 42 11123 15656 5380 5225 -1219 -4389 N
ATOM 331 CA TRP A 42 -12.167 8.609 5.148 1.00 77.46 C
ANISOU 331 CA TRP A 42 9851 14577 5003 4664 -744 -3752 C
ATOM 332 C TRP A 42 -10.676 8.330 5.031 1.00 82.06 C
ANISOU 332 C TRP A 42 10109 16057 5014 5327 -307 -3709 C
ATOM 333 O TRP A 42 -10.232 7.646 4.101 1.00 89.61 O
ANISOU 333 O TRP A 42 11171 17674 5202 6322 -410 -4312 O
ATOM 334 CB TRP A 42 -12.748 7.903 6.373 1.00 72.05 C
ANISOU 334 CB TRP A 42 9407 12592 5377 4162 -1129 -3957 C
ATOM 335 CG TRP A 42 -12.778 6.406 6.292 1.00 76.38 C
ANISOU 335 CG TRP A 42 10360 12542 6119 4766 -1760 -4844 C
ATOM 336 CD1 TRP A 42 -13.783 5.643 5.782 1.00 78.91 C
ANISOU 336 CD1 TRP A 42 11129 12192 6660 4948 -2546 -5508 C
ATOM 337 CD2 TRP A 42 -11.781 5.492 6.772 1.00 78.29 C
ANISOU 337 CD2 TRP A 42 10604 12683 6462 5237 -1778 -5145 C
ATOM 338 NE1 TRP A 42 -13.480 4.316 5.905 1.00 85.14 N
ANISOU 338 NE1 TRP A 42 12229 12404 7714 5495 -3114 -6214 N
ATOM 339 CE2 TRP A 42 -12.252 4.188 6.500 1.00 84.61 C
ANISOU 339 CE2 TRP A 42 11903 12688 7557 5717 -2637 -6026 C
ATOM 340 CE3 TRP A 42 -10.528 5.646 7.391 1.00 75.82 C
ANISOU 340 CE3 TRP A 42 9910 12841 6057 5307 -1222 -4750 C
ATOM 341 CZ2 TRP A 42 -11.515 3.036 6.822 1.00 88.60 C
ANISOU 341 CZ2 TRP A 42 12569 12829 8267 6303 -2964 -6548 C
ATOM 342 CZ3 TRP A 42 -9.796 4.500 7.715 1.00 80.59 C
ANISOU 342 CZ3 TRP A 42 10636 13161 6824 5891 -1476 -5255 C
ATOM 343 CH2 TRP A 42 -10.296 3.212 7.429 1.00 87.00 C
ANISOU 343 CH2 TRP A 42 11979 13149 7928 6399 -2342 -6156 C
ATOM 344 N LYS A 43 -9.903 8.886 5.962 1.00 77.18 N
ANISOU 344 N LYS A 43 9075 15510 4738 4827 154 -3002 N
ATOM 345 CA LYS A 43 -8.457 8.672 6.005 1.00 81.62 C
ANISOU 345 CA LYS A 43 9217 16896 4897 5345 580 -2822 C
ATOM 346 C LYS A 43 -8.019 8.279 7.416 1.00 76.47 C
ANISOU 346 C LYS A 43 8534 15452 5071 4944 569 -2729 C
ATOM 347 O LYS A 43 -8.540 8.822 8.388 1.00 69.14 O
ANISOU 347 O LYS A 43 7646 13770 4854 4075 531 -2326 O
ATOM 348 CB LYS A 43 -7.713 9.925 5.544 1.00 83.24 C
ANISOU 348 CB LYS A 43 8776 18293 4560 5151 1178 -1816 C
ATOM 349 CG LYS A 43 -7.933 10.255 4.061 1.00 90.80 C
ANISOU 349 CG LYS A 43 9672 20317 4509 5692 1263 -1809 C
ATOM 350 CD LYS A 43 -6.847 11.254 3.595 1.00 95.40 C
ANISOU 350 CD LYS A 43 9449 22312 4487 5663 1897 -697 C
ATOM 351 CE LYS A 43 -7.092 11.507 2.079 1.00104.66 C
ANISOU 351 CE LYS A 43 10560 24673 4533 6286 1990 -665 C
ATOM 352 NZ LYS A 43 -6.660 10.323 1.221 1.00113.27 N
ANISOU 352 NZ LYS A 43 11802 26599 4636 7692 1975 -1615 N
ATOM 353 N PRO A 44 -7.071 7.321 7.534 1.00 81.31 N
ANISOU 353 N PRO A 44 9082 16264 5549 5648 578 -3127 N
ATOM 354 CA PRO A 44 -6.547 6.936 8.848 1.00 77.18 C
ANISOU 354 CA PRO A 44 8495 15080 5750 5314 565 -2984 C
ATOM 355 C PRO A 44 -5.770 8.076 9.487 1.00 73.79 C
ANISOU 355 C PRO A 44 7496 15090 5451 4665 1071 -1977 C
ATOM 356 O PRO A 44 -5.092 8.836 8.798 1.00 77.21 O
ANISOU 356 O PRO A 44 7421 16620 5296 4800 1492 -1414 O
ATOM 357 CB PRO A 44 -5.597 5.765 8.533 1.00 84.95 C
ANISOU 357 CB PRO A 44 9463 16434 6380 6389 481 -3619 C
ATOM 358 CG PRO A 44 -5.948 5.321 7.168 1.00 92.33 C
ANISOU 358 CG PRO A 44 10668 17877 6535 7294 251 -4347 C
ATOM 359 CD PRO A 44 -6.436 6.541 6.454 1.00 91.01 C
ANISOU 359 CD PRO A 44 10300 18377 5901 6878 572 -3764 C
ATOM 360 N LYS A 45 -5.874 8.188 10.806 1.00 67.88 N
ANISOU 360 N LYS A 45 6822 13495 5475 3968 972 -1717 N
ATOM 361 CA LYS A 45 -5.256 9.285 11.537 1.00 65.09 C
ANISOU 361 CA LYS A 45 6041 13326 5364 3299 1262 -847 C
ATOM 362 C LYS A 45 -5.107 8.878 13.008 1.00 60.38 C
ANISOU 362 C LYS A 45 5592 11873 5475 2923 1084 -848 C
ATOM 363 O LYS A 45 -5.811 7.991 13.497 1.00 58.14 O
ANISOU 363 O LYS A 45 5751 10766 5574 2942 747 -1357 O
ATOM 364 CB LYS A 45 -6.125 10.548 11.401 1.00 61.97 C
ANISOU 364 CB LYS A 45 5687 12805 5054 2608 1259 -392 C
ATOM 365 CG LYS A 45 -5.404 11.873 11.625 1.00 63.55 C
ANISOU 365 CG LYS A 45 5383 13442 5321 2060 1474 552 C
ATOM 366 CD LYS A 45 -6.408 12.983 11.961 1.00 60.33 C
ANISOU 366 CD LYS A 45 5194 12443 5285 1331 1271 835 C
ATOM 367 CE LYS A 45 -5.823 14.042 12.907 1.00 59.55 C
ANISOU 367 CE LYS A 45 4846 12123 5655 684 1189 1531 C
ATOM 368 NZ LYS A 45 -4.580 14.718 12.396 1.00 66.01 N
ANISOU 368 NZ LYS A 45 4986 13833 6263 621 1378 2368 N
ATOM 369 N MET A 46 -4.177 9.525 13.699 1.00 59.51 N
ANISOU 369 N MET A 46 5082 11984 5544 2571 1263 -215 N
ATOM 370 CA MET A 46 -3.919 9.255 15.107 1.00 56.06 C
ANISOU 370 CA MET A 46 4751 10869 5681 2234 1099 -143 C
ATOM 371 C MET A 46 -3.977 10.555 15.895 1.00 51.66 C
ANISOU 371 C MET A 46 4100 10094 5434 1456 1069 478 C
ATOM 372 O MET A 46 -3.380 11.561 15.493 1.00 53.87 O
ANISOU 372 O MET A 46 3954 10944 5570 1242 1204 1079 O
ATOM 373 CB MET A 46 -2.548 8.617 15.274 1.00 61.12 C
ANISOU 373 CB MET A 46 5012 11951 6260 2703 1215 -82 C
ATOM 374 CG MET A 46 -2.487 7.660 16.428 1.00 61.61 C
ANISOU 374 CG MET A 46 5358 11235 6815 2704 941 -366 C
ATOM 375 SD MET A 46 -1.493 6.230 16.002 1.00 74.20 S
ANISOU 375 SD MET A 46 6808 13163 8223 3717 909 -874 S
ATOM 376 CE MET A 46 -2.213 5.770 14.415 1.00 78.17 C
ANISOU 376 CE MET A 46 7554 14010 8136 4437 877 -1570 C
ATOM 377 N ILE A 47 -4.711 10.541 17.002 1.00 45.71 N
ANISOU 377 N ILE A 47 3734 8534 5099 1063 844 356 N
ATOM 378 CA ILE A 47 -4.807 11.709 17.856 1.00 42.71 C
ANISOU 378 CA ILE A 47 3367 7876 4984 466 715 780 C
ATOM 379 C ILE A 47 -4.407 11.345 19.270 1.00 41.56 C
ANISOU 379 C ILE A 47 3337 7289 5166 334 551 796 C
ATOM 380 O ILE A 47 -4.658 10.230 19.731 1.00 40.29 O
ANISOU 380 O ILE A 47 3400 6788 5120 549 502 454 O
ATOM 381 CB ILE A 47 -6.226 12.372 17.842 1.00 39.09 C
ANISOU 381 CB ILE A 47 3259 7010 4585 161 604 656 C
ATOM 382 CG1 ILE A 47 -7.306 11.390 18.310 1.00 35.52 C
ANISOU 382 CG1 ILE A 47 3198 6013 4285 260 523 182 C
ATOM 383 CG2 ILE A 47 -6.545 12.933 16.447 1.00 41.51 C
ANISOU 383 CG2 ILE A 47 3424 7785 4562 228 717 755 C
ATOM 384 CD1 ILE A 47 -8.640 12.034 18.542 1.00 32.01 C
ANISOU 384 CD1 ILE A 47 3003 5223 3936 -24 433 134 C
ATOM 385 N GLY A 48 -3.776 12.288 19.957 1.00 41.99 N
ANISOU 385 N GLY A 48 3239 7321 5394 -28 391 1226 N
ATOM 386 CA GLY A 48 -3.287 12.017 21.294 1.00 42.35 C
ANISOU 386 CA GLY A 48 3384 7027 5679 -122 193 1263 C
ATOM 387 C GLY A 48 -3.968 12.821 22.372 1.00 40.63 C
ANISOU 387 C GLY A 48 3529 6318 5590 -458 -81 1252 C
ATOM 388 O GLY A 48 -4.295 14.001 22.190 1.00 40.89 O
ANISOU 388 O GLY A 48 3600 6286 5649 -721 -247 1402 O
ATOM 389 N GLY A 49 -4.158 12.189 23.520 1.00 39.23 N
ANISOU 389 N GLY A 49 3614 5820 5471 -399 -166 1086 N
ATOM 390 CA GLY A 49 -4.623 12.928 24.659 1.00 37.77 C
ANISOU 390 CA GLY A 49 3744 5320 5285 -576 -429 1061 C
ATOM 391 C GLY A 49 -3.918 12.531 25.907 1.00 38.16 C
ANISOU 391 C GLY A 49 3861 5254 5384 -542 -630 1137 C
ATOM 392 O GLY A 49 -2.763 12.092 25.881 1.00 39.68 O
ANISOU 392 O GLY A 49 3767 5597 5712 -499 -671 1331 O
ATOM 393 N ILE A 50 -4.625 12.695 27.014 1.00 36.77 N
ANISOU 393 N ILE A 50 4038 4882 5052 -512 -752 998 N
ATOM 394 CA ILE A 50 -4.126 12.310 28.302 1.00 38.04 C
ANISOU 394 CA ILE A 50 4326 4979 5149 -437 -951 1064 C
ATOM 395 C ILE A 50 -4.157 10.769 28.258 1.00 37.96 C
ANISOU 395 C ILE A 50 4217 4989 5217 -288 -682 1110 C
ATOM 396 O ILE A 50 -5.177 10.178 27.908 1.00 37.52 O
ANISOU 396 O ILE A 50 4223 4889 5142 -234 -439 1014 O
ATOM 397 CB ILE A 50 -5.053 12.912 29.397 1.00 38.27 C
ANISOU 397 CB ILE A 50 4753 4948 4841 -324 -1091 882 C
ATOM 398 CG1 ILE A 50 -4.281 13.852 30.319 1.00 39.63 C
ANISOU 398 CG1 ILE A 50 5107 4996 4956 -333 -1646 853 C
ATOM 399 CG2 ILE A 50 -5.800 11.845 30.152 1.00 39.48 C
ANISOU 399 CG2 ILE A 50 5005 5215 4781 -153 -828 936 C
ATOM 400 CD1 ILE A 50 -5.157 14.665 31.241 1.00 39.89 C
ANISOU 400 CD1 ILE A 50 5563 5014 4579 -75 -1860 542 C
ATOM 401 N GLY A 51 -3.059 10.115 28.564 1.00 39.69 N
ANISOU 401 N GLY A 51 4268 5222 5590 -226 -798 1269 N
ATOM 402 CA GLY A 51 -3.063 8.638 28.528 1.00 40.33 C
ANISOU 402 CA GLY A 51 4291 5205 5826 -49 -671 1292 C
ATOM 403 C GLY A 51 -2.517 8.020 27.246 1.00 40.31 C
ANISOU 403 C GLY A 51 3994 5293 6028 147 -531 1180 C
ATOM 404 O GLY A 51 -2.244 6.819 27.189 1.00 42.28 O
ANISOU 404 O GLY A 51 4194 5400 6470 377 -565 1139 O
ATOM 405 N GLY A 52 -2.354 8.846 26.223 1.00 38.79 N
ANISOU 405 N GLY A 52 3608 5361 5771 105 -414 1136 N
ATOM 406 CA GLY A 52 -1.758 8.400 24.992 1.00 40.31 C
ANISOU 406 CA GLY A 52 3475 5846 5997 392 -245 1047 C
ATOM 407 C GLY A 52 -2.633 8.670 23.797 1.00 38.34 C
ANISOU 407 C GLY A 52 3264 5716 5588 431 -34 828 C
ATOM 408 O GLY A 52 -3.435 9.603 23.795 1.00 36.47 O
ANISOU 408 O GLY A 52 3186 5416 5253 153 -23 851 O
ATOM 409 N PHE A 53 -2.523 7.787 22.816 1.00 40.09 N
ANISOU 409 N PHE A 53 3381 6076 5774 844 78 560 N
ATOM 410 CA APHE A 53 -3.102 8.026 21.509 0.50 39.82 C
ANISOU 410 CA APHE A 53 3324 6296 5509 981 254 347 C
ATOM 411 CA BPHE A 53 -3.092 8.009 21.496 0.50 39.86 C
ANISOU 411 CA BPHE A 53 3327 6306 5514 990 255 343 C
ATOM 412 C PHE A 53 -4.199 7.021 21.130 1.00 39.56 C
ANISOU 412 C PHE A 53 3627 5845 5558 1177 151 -95 C
ATOM 413 O PHE A 53 -4.223 5.889 21.625 1.00 41.42 O
ANISOU 413 O PHE A 53 4018 5656 6064 1340 -69 -243 O
ATOM 414 CB APHE A 53 -1.983 8.041 20.461 0.50 44.14 C
ANISOU 414 CB APHE A 53 3403 7554 5813 1389 449 413 C
ATOM 415 CB BPHE A 53 -1.980 7.914 20.450 0.50 44.31 C
ANISOU 415 CB BPHE A 53 3437 7558 5841 1435 442 373 C
ATOM 416 CG APHE A 53 -1.096 9.269 20.526 0.50 45.16 C
ANISOU 416 CG APHE A 53 3100 8153 5907 1063 517 1000 C
ATOM 417 CG BPHE A 53 -1.431 6.524 20.266 0.50 48.31 C
ANISOU 417 CG BPHE A 53 3919 8038 6399 2061 362 9 C
ATOM 418 CD1APHE A 53 -1.205 10.274 19.559 0.50 45.95 C
ANISOU 418 CD1APHE A 53 2961 8729 5769 916 676 1267 C
ATOM 419 CD1BPHE A 53 -0.360 6.078 21.029 0.50 50.48 C
ANISOU 419 CD1BPHE A 53 3984 8316 6880 2189 262 187 C
ATOM 420 CD2APHE A 53 -0.148 9.419 21.542 0.50 45.16 C
ANISOU 420 CD2APHE A 53 2914 8088 6157 873 340 1343 C
ATOM 421 CD2BPHE A 53 -1.983 5.662 19.324 0.50 51.22 C
ANISOU 421 CD2BPHE A 53 4498 8330 6634 2564 298 -551 C
ATOM 422 CE1APHE A 53 -0.391 11.413 19.607 0.50 47.85 C
ANISOU 422 CE1APHE A 53 2761 9321 6099 533 619 1927 C
ATOM 423 CE1BPHE A 53 0.153 4.796 20.856 0.50 55.60 C
ANISOU 423 CE1BPHE A 53 4622 8888 7614 2833 123 -182 C
ATOM 424 CE2APHE A 53 0.669 10.554 21.604 0.50 47.30 C
ANISOU 424 CE2APHE A 53 2767 8693 6511 510 258 1933 C
ATOM 425 CE2BPHE A 53 -1.478 4.377 19.146 0.50 56.84 C
ANISOU 425 CE2BPHE A 53 5245 8919 7432 3227 95 -976 C
ATOM 426 CZ APHE A 53 0.551 11.551 20.635 0.50 48.30 C
ANISOU 426 CZ APHE A 53 2632 9244 6477 316 379 2256 C
ATOM 427 CZ BPHE A 53 -0.406 3.944 19.912 0.50 58.53 C
ANISOU 427 CZ BPHE A 53 5238 9134 7866 3375 20 -789 C
ATOM 428 N ILE A 54 -5.109 7.449 20.252 1.00 37.34 N
ANISOU 428 N ILE A 54 3444 5641 5101 1128 232 -257 N
ATOM 429 CA ILE A 54 -6.039 6.515 19.592 1.00 36.94 C
ANISOU 429 CA ILE A 54 3652 5255 5130 1366 49 -702 C
ATOM 430 C ILE A 54 -5.997 6.672 18.080 1.00 38.42 C
ANISOU 430 C ILE A 54 3745 5943 4909 1766 163 -995 C
ATOM 431 O ILE A 54 -5.725 7.746 17.566 1.00 38.23 O
ANISOU 431 O ILE A 54 3485 6476 4566 1657 424 -731 O
ATOM 432 CB ILE A 54 -7.504 6.637 20.080 1.00 33.40 C
ANISOU 432 CB ILE A 54 3462 4322 4906 931 -65 -641 C
ATOM 433 CG1 ILE A 54 -8.066 8.055 19.829 1.00 29.71 C
ANISOU 433 CG1 ILE A 54 2951 4137 4200 613 148 -454 C
ATOM 434 CG2 ILE A 54 -7.615 6.150 21.537 1.00 32.48 C
ANISOU 434 CG2 ILE A 54 3431 3785 5124 672 -198 -357 C
ATOM 435 CD1 ILE A 54 -9.585 8.144 19.903 1.00 26.83 C
ANISOU 435 CD1 ILE A 54 2768 3446 3979 350 63 -486 C
ATOM 436 N LYS A 55 -6.285 5.576 17.381 1.00 37.23 N
ANISOU 436 N LYS A 55 3797 5570 4781 2245 -107 -1528 N
ATOM 437 CA LYS A 55 -6.428 5.553 15.933 1.00 40.15 C
ANISOU 437 CA LYS A 55 4179 6384 4691 2737 -90 -1933 C
ATOM 438 C LYS A 55 -7.882 5.963 15.621 1.00 37.64 C
ANISOU 438 C LYS A 55 4107 5741 4453 2342 -220 -1981 C
ATOM 439 O LYS A 55 -8.821 5.490 16.277 1.00 40.13 O
ANISOU 439 O LYS A 55 4655 5328 5263 1996 -522 -1989 O
ATOM 440 CB LYS A 55 -6.181 4.150 15.412 1.00 49.57 C
ANISOU 440 CB LYS A 55 5578 7340 5917 3487 -488 -2601 C
ATOM 441 CG LYS A 55 -4.697 3.647 15.483 1.00 56.03 C
ANISOU 441 CG LYS A 55 6113 8603 6571 4106 -369 -2669 C
ATOM 442 CD LYS A 55 -4.524 2.214 14.956 1.00 71.96 C
ANISOU 442 CD LYS A 55 8414 10282 8647 4975 -885 -3463 C
ATOM 443 CE LYS A 55 -4.958 1.187 16.030 1.00 71.48 C
ANISOU 443 CE LYS A 55 8686 9042 9431 4668 -1471 -3499 C
ATOM 444 NZ LYS A 55 -4.643 -0.147 15.578 1.00 79.49 N
ANISOU 444 NZ LYS A 55 9967 9647 10588 5522 -2073 -4240 N
ATOM 445 N VAL A 56 -8.053 6.834 14.624 1.00 42.55 N
ANISOU 445 N VAL A 56 4617 6952 4598 2392 2 -1934 N
ATOM 446 CA VAL A 56 -9.367 7.332 14.258 1.00 41.08 C
ANISOU 446 CA VAL A 56 4614 6539 4457 2050 -111 -1950 C
ATOM 447 C VAL A 56 -9.541 7.340 12.756 1.00 46.06 C
ANISOU 447 C VAL A 56 5296 7673 4532 2544 -158 -2321 C
ATOM 448 O VAL A 56 -8.571 7.229 12.007 1.00 50.89 O
ANISOU 448 O VAL A 56 5719 9013 4606 3132 28 -2442 O
ATOM 449 CB VAL A 56 -9.644 8.758 14.807 1.00 36.38 C
ANISOU 449 CB VAL A 56 3858 6059 3905 1420 169 -1360 C
ATOM 450 CG1 VAL A 56 -9.692 8.757 16.338 1.00 32.60 C
ANISOU 450 CG1 VAL A 56 3407 5086 3894 993 156 -1075 C
ATOM 451 CG2 VAL A 56 -8.633 9.783 14.277 1.00 37.37 C
ANISOU 451 CG2 VAL A 56 3620 6993 3587 1470 511 -955 C
ATOM 452 N ARG A 57 -10.790 7.449 12.320 1.00 45.15 N
ANISOU 452 N ARG A 57 5407 7237 4512 2350 -414 -2486 N
ATOM 453 CA ARG A 57 -11.090 7.632 10.908 1.00 49.13 C
ANISOU 453 CA ARG A 57 5982 8244 4440 2755 -482 -2785 C
ATOM 454 C ARG A 57 -11.452 9.100 10.718 1.00 45.12 C
ANISOU 454 C ARG A 57 5270 8124 3750 2269 -166 -2211 C
ATOM 455 O ARG A 57 -12.281 9.638 11.455 1.00 40.24 O
ANISOU 455 O ARG A 57 4687 7009 3593 1671 -202 -1929 O
ATOM 456 CB ARG A 57 -12.227 6.699 10.473 1.00 51.84 C
ANISOU 456 CB ARG A 57 6730 7904 5061 2895 -1125 -3387 C
ATOM 457 CG ARG A 57 -11.841 5.221 10.437 1.00 58.87 C
ANISOU 457 CG ARG A 57 7882 8353 6132 3487 -1620 -4037 C
ATOM 458 CD ARG A 57 -13.005 4.332 9.992 1.00 65.94 C
ANISOU 458 CD ARG A 57 9183 8444 7428 3548 -2432 -4587 C
ATOM 459 NE ARG A 57 -13.860 3.946 11.113 1.00 65.78 N
ANISOU 459 NE ARG A 57 9176 7467 8349 2822 -2739 -4247 N
ATOM 460 CZ ARG A 57 -15.145 4.268 11.249 1.00 64.81 C
ANISOU 460 CZ ARG A 57 9031 6958 8635 2227 -2924 -3971 C
ATOM 461 NH1 ARG A 57 -15.775 4.990 10.333 1.00 65.65 N
ANISOU 461 NH1 ARG A 57 9158 7436 8351 2237 -2894 -4042 N
ATOM 462 NH2 ARG A 57 -15.811 3.859 12.315 1.00 63.73 N
ANISOU 462 NH2 ARG A 57 8803 6121 9292 1633 -3137 -3560 N
ATOM 463 N GLN A 58 -10.797 9.759 9.772 1.00 48.08 N
ANISOU 463 N GLN A 58 5394 9419 3456 2552 133 -1987 N
ATOM 464 CA GLN A 58 -11.059 11.158 9.524 1.00 45.90 C
ANISOU 464 CA GLN A 58 4912 9475 3054 2091 339 -1374 C
ATOM 465 C GLN A 58 -11.997 11.317 8.334 1.00 48.99 C
ANISOU 465 C GLN A 58 5486 10062 3067 2269 128 -1608 C
ATOM 466 O GLN A 58 -11.671 10.903 7.219 1.00 54.30 O
ANISOU 466 O GLN A 58 6169 11407 3056 2924 123 -1917 O
ATOM 467 CB GLN A 58 -9.767 11.932 9.298 1.00 48.64 C
ANISOU 467 CB GLN A 58 4767 10711 3003 2125 757 -723 C
ATOM 468 CG GLN A 58 -9.986 13.421 9.030 1.00 48.37 C
ANISOU 468 CG GLN A 58 4509 10928 2942 1596 844 9 C
ATOM 469 CD GLN A 58 -8.705 14.166 8.689 1.00 55.04 C
ANISOU 469 CD GLN A 58 4777 12691 3446 1572 1173 806 C
ATOM 470 OE1 GLN A 58 -7.672 13.976 9.319 1.00 57.78 O
ANISOU 470 OE1 GLN A 58 4853 13164 3939 1580 1331 1019 O
ATOM 471 NE2 GLN A 58 -8.782 15.039 7.707 1.00 58.71 N
ANISOU 471 NE2 GLN A 58 5005 13803 3500 1498 1241 1341 N
ATOM 472 N TYR A 59 -13.160 11.907 8.610 1.00 44.81 N
ANISOU 472 N TYR A 59 5092 8979 2954 1745 -59 -1481 N
ATOM 473 CA TYR A 59 -14.181 12.242 7.628 1.00 47.17 C
ANISOU 473 CA TYR A 59 5538 9360 3023 1769 -301 -1596 C
ATOM 474 C TYR A 59 -14.257 13.760 7.438 1.00 46.13 C
ANISOU 474 C TYR A 59 5164 9552 2811 1335 -114 -872 C
ATOM 475 O TYR A 59 -14.448 14.513 8.403 1.00 42.06 O
ANISOU 475 O TYR A 59 4575 8584 2821 810 -71 -502 O
ATOM 476 CB TYR A 59 -15.543 11.728 8.102 1.00 44.35 C
ANISOU 476 CB TYR A 59 5460 8087 3302 1500 -726 -1956 C
ATOM 477 CG TYR A 59 -15.691 10.225 8.087 1.00 47.26 C
ANISOU 477 CG TYR A 59 6105 8001 3852 1875 -1135 -2639 C
ATOM 478 CD1 TYR A 59 -16.217 9.570 6.959 1.00 52.96 C
ANISOU 478 CD1 TYR A 59 7107 8750 4267 2335 -1615 -3224 C
ATOM 479 CD2 TYR A 59 -15.319 9.451 9.195 1.00 44.24 C
ANISOU 479 CD2 TYR A 59 5733 7105 3974 1778 -1144 -2701 C
ATOM 480 CE1 TYR A 59 -16.367 8.194 6.938 1.00 55.33 C
ANISOU 480 CE1 TYR A 59 7706 8483 4835 2681 -2166 -3883 C
ATOM 481 CE2 TYR A 59 -15.462 8.066 9.182 1.00 48.47 C
ANISOU 481 CE2 TYR A 59 6530 7104 4785 2088 -1644 -3275 C
ATOM 482 CZ TYR A 59 -15.990 7.446 8.039 1.00 54.66 C
ANISOU 482 CZ TYR A 59 7608 7832 5328 2540 -2194 -3883 C
ATOM 483 OH TYR A 59 -16.152 6.085 7.994 1.00 58.78 O
ANISOU 483 OH TYR A 59 8436 7689 6208 2856 -2861 -4488 O
ATOM 484 N ASP A 60 -14.124 14.206 6.196 1.00 50.88 N
ANISOU 484 N ASP A 60 5657 10930 2745 1595 -64 -676 N
ATOM 485 CA ASP A 60 -14.131 15.630 5.882 1.00 51.25 C
ANISOU 485 CA ASP A 60 5450 11299 2723 1187 28 106 C
ATOM 486 C ASP A 60 -15.496 16.105 5.413 1.00 50.56 C
ANISOU 486 C ASP A 60 5576 10869 2766 994 -318 28 C
ATOM 487 O ASP A 60 -16.293 15.323 4.888 1.00 51.52 O
ANISOU 487 O ASP A 60 5982 10834 2757 1301 -605 -587 O
ATOM 488 CB ASP A 60 -13.060 15.947 4.832 1.00 58.38 C
ANISOU 488 CB ASP A 60 5976 13407 2801 1529 334 620 C
ATOM 489 CG ASP A 60 -11.660 15.648 5.337 1.00 60.61 C
ANISOU 489 CG ASP A 60 5918 14094 3017 1666 694 856 C
ATOM 490 OD1 ASP A 60 -11.420 15.801 6.556 1.00 57.56 O
ANISOU 490 OD1 ASP A 60 5511 13048 3311 1234 693 974 O
ATOM 491 OD2 ASP A 60 -10.809 15.247 4.531 1.00 68.82 O
ANISOU 491 OD2 ASP A 60 6699 16154 3295 2258 966 908 O
ATOM 492 N GLN A 61 -15.770 17.387 5.643 1.00 48.80 N
ANISOU 492 N GLN A 61 5218 10454 2869 488 -373 640 N
ATOM 493 CA GLN A 61 -16.973 18.032 5.138 1.00 49.15 C
ANISOU 493 CA GLN A 61 5390 10260 3023 315 -696 694 C
ATOM 494 C GLN A 61 -18.222 17.223 5.525 1.00 45.94 C
ANISOU 494 C GLN A 61 5284 9132 3040 358 -978 -14 C
ATOM 495 O GLN A 61 -19.064 16.886 4.687 1.00 47.86 O
ANISOU 495 O GLN A 61 5691 9417 3076 557 -1272 -336 O
ATOM 496 CB GLN A 61 -16.860 18.277 3.620 1.00 56.43 C
ANISOU 496 CB GLN A 61 6223 12085 3132 614 -717 962 C
ATOM 497 CG GLN A 61 -15.554 18.986 3.241 1.00 62.82 C
ANISOU 497 CG GLN A 61 6597 13755 3516 555 -398 1831 C
ATOM 498 CD GLN A 61 -15.298 19.013 1.753 1.00 74.79 C
ANISOU 498 CD GLN A 61 7959 16419 4039 991 -308 2113 C
ATOM 499 OE1 GLN A 61 -15.268 17.967 1.080 1.00 80.03 O
ANISOU 499 OE1 GLN A 61 8797 17583 4028 1665 -264 1461 O
ATOM 500 NE2 GLN A 61 -15.101 20.218 1.220 1.00 80.09 N
ANISOU 500 NE2 GLN A 61 8306 17532 4593 644 -335 3104 N
ATOM 501 N ILE A 62 -18.312 16.902 6.812 1.00 40.71 N
ANISOU 501 N ILE A 62 4653 7847 2969 161 -915 -191 N
ATOM 502 CA ILE A 62 -19.480 16.250 7.376 1.00 39.16 C
ANISOU 502 CA ILE A 62 4598 6998 3281 90 -1148 -626 C
ATOM 503 C ILE A 62 -20.406 17.307 7.968 1.00 37.08 C
ANISOU 503 C ILE A 62 4259 6330 3499 -244 -1245 -352 C
ATOM 504 O ILE A 62 -19.963 18.180 8.696 1.00 34.83 O
ANISOU 504 O ILE A 62 3890 5946 3399 -436 -1107 -15 O
ATOM 505 CB ILE A 62 -19.084 15.208 8.470 1.00 36.37 C
ANISOU 505 CB ILE A 62 4277 6291 3252 110 -1018 -905 C
ATOM 506 CG1 ILE A 62 -18.388 13.988 7.845 1.00 40.01 C
ANISOU 506 CG1 ILE A 62 4868 7017 3317 553 -1066 -1339 C
ATOM 507 CG2 ILE A 62 -20.294 14.778 9.277 1.00 34.32 C
ANISOU 507 CG2 ILE A 62 4020 5413 3609 -94 -1208 -1068 C
ATOM 508 CD1 ILE A 62 -19.221 13.244 6.773 1.00 44.25 C
ANISOU 508 CD1 ILE A 62 5624 7508 3679 843 -1536 -1837 C
ATOM 509 N LEU A 63 -21.696 17.210 7.666 1.00 29.16 N
ANISOU 509 N LEU A 63 3595 5073 2413 -1145 -392 -69 N
ATOM 510 CA LEU A 63 -22.704 18.095 8.255 1.00 29.44 C
ANISOU 510 CA LEU A 63 3745 4766 2673 -1063 -543 140 C
ATOM 511 C LEU A 63 -23.070 17.648 9.663 1.00 28.65 C
ANISOU 511 C LEU A 63 3686 4365 2836 -810 -467 -8 C
ATOM 512 O LEU A 63 -23.451 16.476 9.867 1.00 28.01 O
ANISOU 512 O LEU A 63 3563 4280 2798 -700 -374 -203 O
ATOM 513 CB LEU A 63 -23.980 18.116 7.381 1.00 30.17 C
ANISOU 513 CB LEU A 63 3826 4908 2729 -1114 -669 240 C
ATOM 514 CG LEU A 63 -25.162 18.905 7.977 1.00 29.68 C
ANISOU 514 CG LEU A 63 3835 4506 2935 -975 -833 385 C
ATOM 515 CD1 LEU A 63 -24.877 20.432 8.033 1.00 30.98 C
ANISOU 515 CD1 LEU A 63 4075 4491 3204 -1065 -1045 669 C
ATOM 516 CD2 LEU A 63 -26.453 18.640 7.253 1.00 32.70 C
ANISOU 516 CD2 LEU A 63 4175 4954 3297 -979 -926 424 C
ATOM 517 N ILE A 64 -22.999 18.570 10.624 1.00 28.48 N
ANISOU 517 N ILE A 64 3731 4103 2985 -741 -527 85 N
ATOM 518 CA ILE A 64 -23.471 18.285 11.995 1.00 28.96 C
ANISOU 518 CA ILE A 64 3797 3956 3251 -538 -468 -42 C
ATOM 519 C ILE A 64 -24.364 19.418 12.473 1.00 29.38 C
ANISOU 519 C ILE A 64 3882 3787 3496 -453 -623 41 C
ATOM 520 O ILE A 64 -24.105 20.579 12.175 1.00 30.98 O
ANISOU 520 O ILE A 64 4139 3888 3745 -532 -776 200 O
ATOM 521 CB ILE A 64 -22.339 18.181 13.061 1.00 28.07 C
ANISOU 521 CB ILE A 64 3686 3810 3170 -498 -356 -123 C
ATOM 522 CG1 ILE A 64 -21.205 17.276 12.650 1.00 30.89 C
ANISOU 522 CG1 ILE A 64 3988 4368 3381 -557 -235 -223 C
ATOM 523 CG2 ILE A 64 -22.859 17.543 14.362 1.00 26.55 C
ANISOU 523 CG2 ILE A 64 3457 3517 3112 -346 -286 -247 C
ATOM 524 CD1 ILE A 64 -20.473 16.729 13.920 1.00 34.05 C
ANISOU 524 CD1 ILE A 64 4362 4701 3873 -456 -134 -326 C
ATOM 525 N GLU A 65 -25.418 19.080 13.201 1.00 29.11 N
ANISOU 525 N GLU A 65 3795 3684 3582 -300 -605 -75 N
ATOM 526 CA GLU A 65 -26.212 20.107 13.841 1.00 31.34 C
ANISOU 526 CA GLU A 65 4054 3787 4068 -170 -734 -98 C
ATOM 527 C GLU A 65 -25.915 20.047 15.327 1.00 30.54 C
ANISOU 527 C GLU A 65 3906 3667 4031 -72 -621 -268 C
ATOM 528 O GLU A 65 -26.089 19.007 15.951 1.00 28.91 O
ANISOU 528 O GLU A 65 3636 3590 3761 -51 -485 -362 O
ATOM 529 CB GLU A 65 -27.699 19.944 13.551 1.00 32.01 C
ANISOU 529 CB GLU A 65 4058 3891 4214 -80 -812 -123 C
ATOM 530 CG GLU A 65 -28.481 21.189 13.892 1.00 35.73 C
ANISOU 530 CG GLU A 65 4482 4168 4928 70 -1006 -157 C
ATOM 531 CD GLU A 65 -29.876 21.208 13.299 0.50 37.05 C
ANISOU 531 CD GLU A 65 4559 4359 5159 145 -1135 -135 C
ATOM 532 OE1 GLU A 65 -30.122 20.494 12.301 0.50 37.05 O
ANISOU 532 OE1 GLU A 65 4576 4506 4997 25 -1117 -16 O
ATOM 533 OE2 GLU A 65 -30.720 21.956 13.836 0.50 39.11 O
ANISOU 533 OE2 GLU A 65 4713 4507 5638 333 -1260 -266 O
ATOM 534 N ILE A 66 -25.422 21.151 15.868 1.00 31.89 N
ANISOU 534 N ILE A 66 4108 3685 4324 -43 -700 -290 N
ATOM 535 CA ILE A 66 -25.002 21.204 17.269 1.00 32.25 C
ANISOU 535 CA ILE A 66 4099 3758 4397 17 -596 -460 C
ATOM 536 C ILE A 66 -25.950 22.165 17.956 1.00 34.88 C
ANISOU 536 C ILE A 66 4335 3981 4938 187 -715 -650 C
ATOM 537 O ILE A 66 -25.958 23.376 17.670 1.00 35.80 O
ANISOU 537 O ILE A 66 4501 3848 5253 229 -917 -633 O
ATOM 538 CB ILE A 66 -23.515 21.676 17.416 1.00 32.35 C
ANISOU 538 CB ILE A 66 4203 3717 4372 -97 -579 -391 C
ATOM 539 CG1 ILE A 66 -22.566 20.727 16.667 1.00 30.80 C
ANISOU 539 CG1 ILE A 66 4053 3676 3975 -238 -466 -261 C
ATOM 540 CG2 ILE A 66 -23.100 21.799 18.885 1.00 31.57 C
ANISOU 540 CG2 ILE A 66 4036 3670 4290 -49 -485 -570 C
ATOM 541 CD1 ILE A 66 -21.240 21.369 16.314 1.00 33.93 C
ANISOU 541 CD1 ILE A 66 4525 4058 4308 -389 -498 -141 C
ATOM 542 N CYS A 67 -26.776 21.597 18.830 1.00 36.14 N
ANISOU 542 N CYS A 67 4336 4338 5056 274 -612 -832 N
ATOM 543 CA CYS A 67 -27.762 22.337 19.599 1.00 39.64 C
ANISOU 543 CA CYS A 67 4610 4796 5655 453 -687 -1103 C
ATOM 544 C CYS A 67 -28.506 23.325 18.673 1.00 41.11 C
ANISOU 544 C CYS A 67 4818 4711 6090 576 -940 -1074 C
ATOM 545 O CYS A 67 -28.735 24.494 19.022 1.00 43.46 O
ANISOU 545 O CYS A 67 5062 4803 6646 730 -1113 -1262 O
ATOM 546 CB CYS A 67 -27.079 23.005 20.808 1.00 40.48 C
ANISOU 546 CB CYS A 67 4666 4911 5803 482 -652 -1319 C
ATOM 547 SG CYS A 67 -28.204 23.697 22.020 1.00 52.32 S
ANISOU 547 SG CYS A 67 5874 6580 7425 697 -681 -1780 S
ATOM 548 N GLY A 68 -28.869 22.842 17.481 1.00 39.79 N
ANISOU 548 N GLY A 68 4722 4536 5860 504 -986 -840 N
ATOM 549 CA GLY A 68 -29.629 23.644 16.522 1.00 41.68 C
ANISOU 549 CA GLY A 68 4972 4558 6308 586 -1247 -743 C
ATOM 550 C GLY A 68 -28.821 24.569 15.622 1.00 42.55 C
ANISOU 550 C GLY A 68 5265 4365 6535 469 -1467 -477 C
ATOM 551 O GLY A 68 -29.398 25.366 14.869 1.00 45.78 O
ANISOU 551 O GLY A 68 5686 4552 7157 517 -1746 -349 O
ATOM 552 N HIS A 69 -27.495 24.482 15.701 1.00 39.76 N
ANISOU 552 N HIS A 69 5041 4021 6047 297 -1367 -371 N
ATOM 553 CA HIS A 69 -26.607 25.247 14.832 1.00 40.14 C
ANISOU 553 CA HIS A 69 5249 3876 6127 107 -1553 -78 C
ATOM 554 C HIS A 69 -25.921 24.288 13.889 1.00 37.63 C
ANISOU 554 C HIS A 69 5000 3826 5472 -129 -1399 145 C
ATOM 555 O HIS A 69 -25.232 23.387 14.336 1.00 35.44 O
ANISOU 555 O HIS A 69 4713 3756 4995 -173 -1148 53 O
ATOM 556 CB HIS A 69 -25.517 25.949 15.649 1.00 40.24 C
ANISOU 556 CB HIS A 69 5325 3741 6225 68 -1560 -156 C
ATOM 557 CG HIS A 69 -26.000 27.127 16.431 1.00 43.98 C
ANISOU 557 CG HIS A 69 5742 3895 7074 276 -1776 -394 C
ATOM 558 ND1 HIS A 69 -26.919 27.016 17.452 1.00 45.14 N
ANISOU 558 ND1 HIS A 69 5703 4125 7324 534 -1694 -780 N
ATOM 559 CD2 HIS A 69 -25.681 28.442 16.348 1.00 46.19 C
ANISOU 559 CD2 HIS A 69 6107 3779 7663 257 -2089 -327 C
ATOM 560 CE1 HIS A 69 -27.164 28.216 17.949 1.00 48.10 C
ANISOU 560 CE1 HIS A 69 6034 4179 8064 703 -1937 -998 C
ATOM 561 NE2 HIS A 69 -26.413 29.095 17.306 1.00 49.70 N
ANISOU 561 NE2 HIS A 69 6415 4044 8425 544 -2194 -723 N
ATOM 562 N LYS A 70 -26.069 24.511 12.590 1.00 38.01 N
ANISOU 562 N LYS A 70 5098 3881 5463 -287 -1569 429 N
ATOM 563 CA LYS A 70 -25.441 23.660 11.579 1.00 36.56 C
ANISOU 563 CA LYS A 70 4939 4015 4938 -521 -1435 589 C
ATOM 564 C LYS A 70 -23.986 24.052 11.325 1.00 36.41 C
ANISOU 564 C LYS A 70 4998 4060 4776 -763 -1435 753 C
ATOM 565 O LYS A 70 -23.664 25.228 11.242 1.00 38.44 O
ANISOU 565 O LYS A 70 5329 4088 5189 -864 -1676 941 O
ATOM 566 CB LYS A 70 -26.241 23.722 10.272 1.00 38.08 C
ANISOU 566 CB LYS A 70 5115 4286 5069 -629 -1614 818 C
ATOM 567 CG LYS A 70 -27.634 23.135 10.392 1.00 39.52 C
ANISOU 567 CG LYS A 70 5197 4494 5324 -426 -1581 658 C
ATOM 568 CD LYS A 70 -28.365 23.242 9.064 1.00 43.66 C
ANISOU 568 CD LYS A 70 5699 5117 5772 -557 -1774 907 C
ATOM 569 CE LYS A 70 -29.847 23.512 9.234 1.00 48.85 C
ANISOU 569 CE LYS A 70 6261 5623 6676 -329 -1932 839 C
ATOM 570 NZ LYS A 70 -30.528 22.368 9.874 1.00 47.56 N
ANISOU 570 NZ LYS A 70 5995 5633 6441 -170 -1679 543 N
ATOM 571 N ALA A 71 -23.124 23.051 11.194 1.00 34.05 N
ANISOU 571 N ALA A 71 4668 4071 4198 -858 -1185 674 N
ATOM 572 CA ALA A 71 -21.715 23.238 10.877 1.00 34.10 C
ANISOU 572 CA ALA A 71 4697 4256 4006 -1096 -1144 794 C
ATOM 573 C ALA A 71 -21.302 22.130 9.908 1.00 33.75 C
ANISOU 573 C ALA A 71 4561 4641 3621 -1231 -969 754 C
ATOM 574 O ALA A 71 -21.901 21.045 9.890 1.00 32.11 O
ANISOU 574 O ALA A 71 4295 4524 3381 -1089 -829 557 O
ATOM 575 CB ALA A 71 -20.864 23.217 12.170 1.00 32.83 C
ANISOU 575 CB ALA A 71 4546 4008 3920 -994 -999 609 C
ATOM 576 N ILE A 72 -20.336 22.421 9.048 1.00 34.90 N
ANISOU 576 N ILE A 72 4678 5072 3512 -1524 -1001 931 N
ATOM 577 CA ILE A 72 -19.791 21.407 8.159 1.00 35.64 C
ANISOU 577 CA ILE A 72 4637 5639 3265 -1648 -823 808 C
ATOM 578 C ILE A 72 -18.308 21.396 8.417 1.00 36.27 C
ANISOU 578 C ILE A 72 4657 5932 3190 -1759 -697 751 C
ATOM 579 O ILE A 72 -17.644 22.447 8.358 1.00 37.50 O
ANISOU 579 O ILE A 72 4856 6084 3307 -1986 -836 1004 O
ATOM 580 CB ILE A 72 -20.084 21.663 6.653 1.00 38.62 C
ANISOU 580 CB ILE A 72 4954 6347 3374 -1947 -966 1048 C
ATOM 581 CG1 ILE A 72 -21.539 21.332 6.315 1.00 38.35 C
ANISOU 581 CG1 ILE A 72 4933 6192 3446 -1815 -1041 1034 C
ATOM 582 CG2 ILE A 72 -19.217 20.761 5.774 1.00 40.50 C
ANISOU 582 CG2 ILE A 72 5005 7169 3213 -2113 -771 862 C
ATOM 583 CD1 ILE A 72 -21.934 21.684 4.894 1.00 40.11 C
ANISOU 583 CD1 ILE A 72 5098 6724 3420 -2120 -1221 1316 C
ATOM 584 N GLY A 73 -17.782 20.223 8.758 1.00 34.68 N
ANISOU 584 N GLY A 73 4355 5888 2935 -1599 -462 425 N
ATOM 585 CA GLY A 73 -16.356 20.154 9.052 1.00 34.72 C
ANISOU 585 CA GLY A 73 4272 6111 2811 -1670 -342 341 C
ATOM 586 C GLY A 73 -15.861 18.741 9.184 1.00 33.56 C
ANISOU 586 C GLY A 73 3977 6150 2624 -1480 -128 -35 C
ATOM 587 O GLY A 73 -16.587 17.774 8.933 1.00 32.62 O
ANISOU 587 O GLY A 73 3825 6009 2559 -1328 -79 -231 O
ATOM 588 N THR A 74 -14.608 18.637 9.585 1.00 34.01 N
ANISOU 588 N THR A 74 3939 6373 2613 -1492 -28 -134 N
ATOM 589 CA THR A 74 -13.987 17.349 9.809 1.00 33.68 C
ANISOU 589 CA THR A 74 3739 6460 2598 -1286 132 -494 C
ATOM 590 C THR A 74 -14.470 16.687 11.084 1.00 31.14 C
ANISOU 590 C THR A 74 3513 5699 2619 -986 150 -592 C
ATOM 591 O THR A 74 -14.458 17.277 12.205 1.00 29.66 O
ANISOU 591 O THR A 74 3443 5235 2591 -941 116 -447 O
ATOM 592 CB THR A 74 -12.437 17.453 9.769 1.00 35.75 C
ANISOU 592 CB THR A 74 3823 7098 2662 -1399 220 -574 C
ATOM 593 OG1 THR A 74 -12.048 17.733 8.432 1.00 38.36 O
ANISOU 593 OG1 THR A 74 3994 7967 2615 -1690 224 -553 O
ATOM 594 CG2 THR A 74 -11.774 16.139 10.209 1.00 34.92 C
ANISOU 594 CG2 THR A 74 3552 7028 2688 -1120 341 -954 C
ATOM 595 N VAL A 75 -14.901 15.447 10.919 1.00 30.70 N
ANISOU 595 N VAL A 75 3393 5600 2669 -804 189 -841 N
ATOM 596 CA VAL A 75 -15.246 14.641 12.071 1.00 29.15 C
ANISOU 596 CA VAL A 75 3252 5049 2775 -567 185 -915 C
ATOM 597 C VAL A 75 -14.331 13.429 12.104 1.00 30.24 C
ANISOU 597 C VAL A 75 3213 5280 2995 -408 237 -1219 C
ATOM 598 O VAL A 75 -14.143 12.763 11.089 1.00 31.86 O
ANISOU 598 O VAL A 75 3271 5726 3109 -394 266 -1483 O
ATOM 599 CB VAL A 75 -16.720 14.219 12.043 1.00 27.55 C
ANISOU 599 CB VAL A 75 3152 4606 2711 -494 121 -893 C
ATOM 600 CG1 VAL A 75 -17.040 13.303 13.216 1.00 26.76 C
ANISOU 600 CG1 VAL A 75 3080 4198 2887 -310 96 -935 C
ATOM 601 CG2 VAL A 75 -17.599 15.447 12.086 1.00 28.53 C
ANISOU 601 CG2 VAL A 75 3418 4618 2802 -606 45 -624 C
ATOM 602 N LEU A 76 -13.760 13.173 13.278 1.00 29.87 N
ANISOU 602 N LEU A 76 3164 5054 3129 -288 231 -1194 N
ATOM 603 CA LEU A 76 -12.971 11.970 13.530 1.00 31.27 C
ANISOU 603 CA LEU A 76 3183 5207 3490 -93 219 -1447 C
ATOM 604 C LEU A 76 -13.849 10.949 14.252 1.00 30.65 C
ANISOU 604 C LEU A 76 3188 4728 3730 57 106 -1430 C
ATOM 605 O LEU A 76 -14.640 11.299 15.133 1.00 28.67 O
ANISOU 605 O LEU A 76 3087 4261 3545 14 69 -1179 O
ATOM 606 CB LEU A 76 -11.718 12.292 14.345 1.00 31.38 C
ANISOU 606 CB LEU A 76 3118 5305 3500 -82 249 -1392 C
ATOM 607 CG LEU A 76 -10.906 13.530 13.942 1.00 31.78 C
ANISOU 607 CG LEU A 76 3129 5710 3235 -300 335 -1291 C
ATOM 608 CD1 LEU A 76 -9.734 13.744 14.898 1.00 34.07 C
ANISOU 608 CD1 LEU A 76 3343 6048 3552 -281 353 -1236 C
ATOM 609 CD2 LEU A 76 -10.411 13.431 12.526 1.00 34.78 C
ANISOU 609 CD2 LEU A 76 3316 6539 3360 -387 403 -1528 C
ATOM 610 N VAL A 77 -13.722 9.690 13.853 1.00 32.17 N
ANISOU 610 N VAL A 77 3262 4842 4118 218 36 -1713 N
ATOM 611 CA VAL A 77 -14.486 8.616 14.442 1.00 32.35 C
ANISOU 611 CA VAL A 77 3351 4474 4465 324 -118 -1684 C
ATOM 612 C VAL A 77 -13.520 7.568 14.992 1.00 34.59 C
ANISOU 612 C VAL A 77 3495 4588 5061 519 -246 -1829 C
ATOM 613 O VAL A 77 -12.616 7.111 14.281 1.00 36.74 O
ANISOU 613 O VAL A 77 3570 5024 5366 652 -237 -2184 O
ATOM 614 CB VAL A 77 -15.420 7.977 13.392 1.00 34.25 C
ANISOU 614 CB VAL A 77 3600 4680 4735 332 -158 -1889 C
ATOM 615 CG1 VAL A 77 -16.241 6.847 14.016 1.00 34.49 C
ANISOU 615 CG1 VAL A 77 3705 4286 5113 399 -349 -1824 C
ATOM 616 CG2 VAL A 77 -16.350 9.052 12.783 1.00 32.17 C
ANISOU 616 CG2 VAL A 77 3453 4604 4166 141 -57 -1725 C
ATOM 617 N GLY A 78 -13.700 7.193 16.254 1.00 33.13 N
ANISOU 617 N GLY A 78 3384 4105 5099 528 -381 -1562 N
ATOM 618 CA GLY A 78 -12.857 6.162 16.861 1.00 35.08 C
ANISOU 618 CA GLY A 78 3507 4128 5694 701 -568 -1626 C
ATOM 619 C GLY A 78 -13.184 5.970 18.329 1.00 33.93 C
ANISOU 619 C GLY A 78 3457 3737 5697 612 -714 -1214 C
ATOM 620 O GLY A 78 -14.143 6.577 18.831 1.00 31.85 O
ANISOU 620 O GLY A 78 3340 3502 5261 429 -652 -942 O
ATOM 621 N PRO A 79 -12.357 5.177 19.042 1.00 35.71 N
ANISOU 621 N PRO A 79 3573 3768 6226 731 -913 -1170 N
ATOM 622 CA PRO A 79 -12.653 4.748 20.410 1.00 35.30 C
ANISOU 622 CA PRO A 79 3579 3489 6343 617 -1116 -756 C
ATOM 623 C PRO A 79 -12.363 5.806 21.471 1.00 33.20 C
ANISOU 623 C PRO A 79 3339 3489 5785 449 -980 -458 C
ATOM 624 O PRO A 79 -11.637 5.539 22.431 1.00 33.92 O
ANISOU 624 O PRO A 79 3349 3543 5995 446 -1115 -263 O
ATOM 625 CB PRO A 79 -11.755 3.524 20.595 1.00 39.09 C
ANISOU 625 CB PRO A 79 3908 3662 7285 827 -1412 -851 C
ATOM 626 CG PRO A 79 -10.606 3.753 19.682 1.00 40.74 C
ANISOU 626 CG PRO A 79 3935 4102 7443 1049 -1272 -1292 C
ATOM 627 CD PRO A 79 -11.072 4.635 18.558 1.00 37.77 C
ANISOU 627 CD PRO A 79 3615 4053 6683 978 -974 -1520 C
ATOM 628 N THR A 80 -12.920 6.999 21.283 1.00 29.78 N
ANISOU 628 N THR A 80 3008 3313 4992 314 -737 -439 N
ATOM 629 CA THR A 80 -12.946 8.015 22.321 1.00 28.48 C
ANISOU 629 CA THR A 80 2886 3366 4571 138 -627 -192 C
ATOM 630 C THR A 80 -13.983 7.569 23.373 1.00 29.77 C
ANISOU 630 C THR A 80 3101 3432 4778 -38 -767 128 C
ATOM 631 O THR A 80 -15.003 6.966 23.015 1.00 29.45 O
ANISOU 631 O THR A 80 3123 3225 4842 -66 -853 140 O
ATOM 632 CB THR A 80 -13.303 9.422 21.757 1.00 26.63 C
ANISOU 632 CB THR A 80 2741 3370 4007 62 -379 -293 C
ATOM 633 OG1 THR A 80 -13.533 10.318 22.838 1.00 22.39 O
ANISOU 633 OG1 THR A 80 2241 2988 3278 -96 -311 -97 O
ATOM 634 CG2 THR A 80 -14.554 9.383 20.869 1.00 22.37 C
ANISOU 634 CG2 THR A 80 2302 2754 3442 50 -349 -381 C
ATOM 635 N PRO A 81 -13.723 7.847 24.662 1.00 30.00 N
ANISOU 635 N PRO A 81 3084 3613 4702 -185 -796 387 N
ATOM 636 CA PRO A 81 -14.734 7.420 25.636 1.00 31.11 C
ANISOU 636 CA PRO A 81 3233 3765 4822 -403 -925 693 C
ATOM 637 C PRO A 81 -16.001 8.271 25.634 1.00 29.15 C
ANISOU 637 C PRO A 81 3056 3717 4303 -528 -751 659 C
ATOM 638 O PRO A 81 -17.003 7.860 26.192 1.00 29.49 O
ANISOU 638 O PRO A 81 3087 3806 4313 -704 -842 854 O
ATOM 639 CB PRO A 81 -13.998 7.550 26.977 1.00 31.31 C
ANISOU 639 CB PRO A 81 3152 3987 4758 -541 -990 949 C
ATOM 640 CG PRO A 81 -12.968 8.522 26.747 1.00 30.92 C
ANISOU 640 CG PRO A 81 3081 4097 4568 -432 -801 746 C
ATOM 641 CD PRO A 81 -12.549 8.448 25.324 1.00 29.90 C
ANISOU 641 CD PRO A 81 2985 3802 4574 -195 -736 428 C
ATOM 642 N VAL A 82 -15.950 9.440 24.991 1.00 27.60 N
ANISOU 642 N VAL A 82 2916 3643 3928 -445 -527 419 N
ATOM 643 CA VAL A 82 -17.003 10.441 25.056 1.00 27.19 C
ANISOU 643 CA VAL A 82 2907 3773 3652 -524 -379 354 C
ATOM 644 C VAL A 82 -17.026 11.148 23.706 1.00 25.31 C
ANISOU 644 C VAL A 82 2764 3463 3391 -383 -250 104 C
ATOM 645 O VAL A 82 -15.950 11.398 23.151 1.00 25.40 O
ANISOU 645 O VAL A 82 2775 3457 3417 -288 -203 -8 O
ATOM 646 CB VAL A 82 -16.647 11.438 26.213 1.00 28.21 C
ANISOU 646 CB VAL A 82 2967 4193 3559 -638 -285 392 C
ATOM 647 CG1 VAL A 82 -17.324 12.766 26.064 1.00 29.97 C
ANISOU 647 CG1 VAL A 82 3230 4547 3612 -630 -129 202 C
ATOM 648 CG2 VAL A 82 -17.016 10.822 27.585 1.00 32.59 C
ANISOU 648 CG2 VAL A 82 3400 4940 4041 -856 -404 661 C
ATOM 649 N ASN A 83 -18.215 11.422 23.159 1.00 22.94 N
ANISOU 649 N ASN A 83 2521 3153 3043 -388 -211 37 N
ATOM 650 CA ASN A 83 -18.361 12.266 21.981 1.00 22.05 C
ANISOU 650 CA ASN A 83 2489 3019 2871 -304 -113 -140 C
ATOM 651 C ASN A 83 -17.922 13.694 22.323 1.00 21.10 C
ANISOU 651 C ASN A 83 2383 3026 2608 -326 -13 -190 C
ATOM 652 O ASN A 83 -18.451 14.312 23.259 1.00 21.31 O
ANISOU 652 O ASN A 83 2373 3173 2552 -389 10 -177 O
ATOM 653 CB ASN A 83 -19.806 12.343 21.487 1.00 21.80 C
ANISOU 653 CB ASN A 83 2496 2968 2819 -316 -116 -171 C
ATOM 654 CG ASN A 83 -20.378 11.001 20.985 1.00 25.31 C
ANISOU 654 CG ASN A 83 2943 3266 3408 -315 -227 -144 C
ATOM 655 OD1 ASN A 83 -19.697 10.221 20.300 1.00 24.78 O
ANISOU 655 OD1 ASN A 83 2882 3061 3475 -239 -281 -220 O
ATOM 656 ND2 ASN A 83 -21.676 10.757 21.299 1.00 22.71 N
ANISOU 656 ND2 ASN A 83 2592 2982 3053 -402 -268 -67 N
ATOM 657 N AILE A 84 -16.944 14.220 21.596 0.50 20.58 N
ANISOU 657 N AILE A 84 2350 2958 2512 -291 33 -264 N
ATOM 658 N BILE A 84 -16.997 14.207 21.517 0.50 20.82 N
ANISOU 658 N BILE A 84 2385 2982 2545 -288 32 -269 N
ATOM 659 CA AILE A 84 -16.451 15.561 21.892 0.50 20.21 C
ANISOU 659 CA AILE A 84 2329 2988 2362 -341 88 -290 C
ATOM 660 CA BILE A 84 -16.358 15.491 21.730 0.50 20.70 C
ANISOU 660 CA BILE A 84 2393 3044 2428 -335 88 -294 C
ATOM 661 C AILE A 84 -16.486 16.479 20.664 0.50 20.18 C
ANISOU 661 C AILE A 84 2412 2942 2313 -349 96 -342 C
ATOM 662 C BILE A 84 -16.618 16.436 20.551 0.50 20.42 C
ANISOU 662 C BILE A 84 2448 2963 2349 -344 93 -345 C
ATOM 663 O AILE A 84 -15.979 16.134 19.599 0.50 21.09 O
ANISOU 663 O AILE A 84 2525 3085 2402 -342 106 -370 O
ATOM 664 O BILE A 84 -16.365 16.077 19.407 0.50 21.31 O
ANISOU 664 O BILE A 84 2568 3087 2442 -332 95 -375 O
ATOM 665 CB AILE A 84 -15.035 15.535 22.562 0.50 20.59 C
ANISOU 665 CB AILE A 84 2310 3137 2377 -376 107 -253 C
ATOM 666 CB BILE A 84 -14.826 15.279 21.874 0.50 21.35 C
ANISOU 666 CB BILE A 84 2413 3206 2492 -342 107 -282 C
ATOM 667 CG1AILE A 84 -13.988 14.868 21.656 0.50 20.42 C
ANISOU 667 CG1AILE A 84 2244 3124 2389 -316 108 -297 C
ATOM 668 CG1BILE A 84 -14.497 14.546 23.183 0.50 20.78 C
ANISOU 668 CG1BILE A 84 2247 3186 2464 -362 64 -177 C
ATOM 669 CG2AILE A 84 -15.080 14.832 23.925 0.50 19.96 C
ANISOU 669 CG2AILE A 84 2137 3130 2318 -418 65 -143 C
ATOM 670 CG2BILE A 84 -14.069 16.610 21.775 0.50 21.72 C
ANISOU 670 CG2BILE A 84 2497 3330 2427 -425 151 -302 C
ATOM 671 CD1AILE A 84 -12.555 14.954 22.201 0.50 18.86 C
ANISOU 671 CD1AILE A 84 1957 3056 2152 -341 126 -275 C
ATOM 672 CD1BILE A 84 -13.134 13.886 23.191 0.50 20.07 C
ANISOU 672 CD1BILE A 84 2064 3131 2431 -316 36 -163 C
ATOM 673 N ILE A 85 -17.124 17.634 20.830 1.00 20.31 N
ANISOU 673 N ILE A 85 2483 2908 2325 -373 72 -362 N
ATOM 674 CA ILE A 85 -17.148 18.702 19.837 1.00 20.77 C
ANISOU 674 CA ILE A 85 2629 2893 2369 -420 18 -345 C
ATOM 675 C ILE A 85 -15.942 19.621 20.071 1.00 20.56 C
ANISOU 675 C ILE A 85 2622 2902 2289 -527 14 -315 C
ATOM 676 O ILE A 85 -15.868 20.321 21.075 1.00 20.38 O
ANISOU 676 O ILE A 85 2595 2848 2302 -540 -1 -364 O
ATOM 677 CB ILE A 85 -18.474 19.525 19.895 1.00 21.65 C
ANISOU 677 CB ILE A 85 2781 2869 2577 -369 -66 -388 C
ATOM 678 CG1 ILE A 85 -19.693 18.593 19.811 1.00 20.98 C
ANISOU 678 CG1 ILE A 85 2651 2798 2521 -286 -55 -416 C
ATOM 679 CG2 ILE A 85 -18.533 20.629 18.771 1.00 22.29 C
ANISOU 679 CG2 ILE A 85 2961 2823 2686 -438 -191 -303 C
ATOM 680 CD1 ILE A 85 -19.704 17.682 18.585 1.00 18.38 C
ANISOU 680 CD1 ILE A 85 2342 2491 2151 -296 -47 -367 C
ATOM 681 N GLY A 86 -15.024 19.635 19.109 1.00 21.42 N
ANISOU 681 N GLY A 86 2991 2806 2340 -736 -32 -403 N
ATOM 682 CA GLY A 86 -13.788 20.366 19.260 1.00 21.09 C
ANISOU 682 CA GLY A 86 2911 2897 2206 -742 30 -450 C
ATOM 683 C GLY A 86 -13.811 21.713 18.600 1.00 21.39 C
ANISOU 683 C GLY A 86 3033 3017 2076 -939 -27 -349 C
ATOM 684 O GLY A 86 -14.784 22.062 17.952 1.00 22.39 O
ANISOU 684 O GLY A 86 3248 3085 2176 -1013 -130 -261 O
ATOM 685 N ARG A 87 -12.723 22.473 18.746 1.00 21.78 N
ANISOU 685 N ARG A 87 3080 3204 1993 -1053 0 -348 N
ATOM 686 CA ARG A 87 -12.696 23.862 18.251 1.00 23.10 C
ANISOU 686 CA ARG A 87 3431 3363 1983 -1315 -142 -190 C
ATOM 687 C ARG A 87 -12.984 23.977 16.736 1.00 24.95 C
ANISOU 687 C ARG A 87 3745 3721 2016 -1589 -213 -156 C
ATOM 688 O ARG A 87 -13.548 24.976 16.289 1.00 26.69 O
ANISOU 688 O ARG A 87 4198 3784 2158 -1743 -433 31 O
ATOM 689 CB ARG A 87 -11.379 24.539 18.596 1.00 23.03 C
ANISOU 689 CB ARG A 87 3409 3537 1805 -1510 -110 -184 C
ATOM 690 CG ARG A 87 -11.066 24.590 20.130 1.00 20.66 C
ANISOU 690 CG ARG A 87 3051 3126 1672 -1271 -65 -198 C
ATOM 691 CD ARG A 87 -9.807 25.426 20.383 1.00 22.80 C
ANISOU 691 CD ARG A 87 3334 3595 1734 -1540 -69 -170 C
ATOM 692 NE ARG A 87 -8.616 24.768 19.824 1.00 26.38 N
ANISOU 692 NE ARG A 87 3505 4534 1983 -1676 103 -352 N
ATOM 693 CZ ARG A 87 -7.997 25.098 18.690 1.00 29.50 C
ANISOU 693 CZ ARG A 87 3856 5312 2039 -2086 111 -365 C
ATOM 694 NH1 ARG A 87 -8.421 26.103 17.924 1.00 28.52 N
ANISOU 694 NH1 ARG A 87 4029 5069 1739 -2471 -80 -136 N
ATOM 695 NH2 ARG A 87 -6.934 24.405 18.314 1.00 31.19 N
ANISOU 695 NH2 ARG A 87 3715 6076 2060 -2112 284 -627 N
ATOM 696 N ASN A 88 -12.609 22.972 15.945 1.00 26.03 N
ANISOU 696 N ASN A 88 3705 4126 2058 -1634 -70 -353 N
ATOM 697 CA ASN A 88 -12.874 23.038 14.510 1.00 27.96 C
ANISOU 697 CA ASN A 88 3995 4557 2069 -1920 -123 -342 C
ATOM 698 C ASN A 88 -14.360 23.261 14.212 1.00 27.95 C
ANISOU 698 C ASN A 88 4170 4259 2190 -1856 -307 -172 C
ATOM 699 O ASN A 88 -14.717 23.885 13.194 1.00 29.77 O
ANISOU 699 O ASN A 88 4552 4536 2222 -2130 -469 -28 O
ATOM 700 CB ASN A 88 -12.345 21.809 13.772 1.00 29.45 C
ANISOU 700 CB ASN A 88 3946 5087 2157 -1888 49 -672 C
ATOM 701 CG ASN A 88 -13.246 20.590 13.927 1.00 29.51 C
ANISOU 701 CG ASN A 88 3947 4829 2439 -1575 53 -796 C
ATOM 702 OD1 ASN A 88 -13.506 20.159 15.038 1.00 27.54 O
ANISOU 702 OD1 ASN A 88 3709 4298 2457 -1302 51 -772 O
ATOM 703 ND2 ASN A 88 -13.723 20.034 12.803 1.00 27.63 N
ANISOU 703 ND2 ASN A 88 3703 4700 2093 -1678 39 -913 N
ATOM 704 N LEU A 89 -15.232 22.752 15.081 1.00 25.14 N
ANISOU 704 N LEU A 89 3775 3658 2120 -1527 -303 -185 N
ATOM 705 CA LEU A 89 -16.677 22.982 14.895 1.00 25.42 C
ANISOU 705 CA LEU A 89 3888 3527 2243 -1438 -476 -65 C
ATOM 706 C LEU A 89 -17.223 24.085 15.807 1.00 25.02 C
ANISOU 706 C LEU A 89 3947 3253 2307 -1240 -662 64 C
ATOM 707 O LEU A 89 -18.197 24.759 15.449 1.00 26.29 O
ANISOU 707 O LEU A 89 4216 3310 2464 -1175 -903 158 O
ATOM 708 CB LEU A 89 -17.481 21.686 15.047 1.00 23.95 C
ANISOU 708 CB LEU A 89 3557 3335 2206 -1296 -386 -175 C
ATOM 709 CG LEU A 89 -17.194 20.606 13.985 1.00 26.57 C
ANISOU 709 CG LEU A 89 3842 3818 2434 -1445 -291 -354 C
ATOM 710 CD1 LEU A 89 -18.068 19.355 14.191 1.00 28.68 C
ANISOU 710 CD1 LEU A 89 4062 3985 2851 -1362 -283 -426 C
ATOM 711 CD2 LEU A 89 -17.388 21.143 12.577 1.00 26.36 C
ANISOU 711 CD2 LEU A 89 3895 3958 2161 -1717 -393 -295 C
ATOM 712 N LEU A 90 -16.604 24.255 16.975 1.00 23.62 N
ANISOU 712 N LEU A 90 3732 3018 2224 -1106 -580 31 N
ATOM 713 CA LEU A 90 -17.035 25.287 17.922 1.00 23.98 C
ANISOU 713 CA LEU A 90 3870 2875 2366 -880 -757 75 C
ATOM 714 C LEU A 90 -16.954 26.655 17.247 1.00 25.93 C
ANISOU 714 C LEU A 90 4451 2921 2481 -1031 -1079 220 C
ATOM 715 O LEU A 90 -17.855 27.488 17.408 1.00 27.77 O
ANISOU 715 O LEU A 90 4819 2948 2785 -792 -1373 234 O
ATOM 716 CB LEU A 90 -16.216 25.244 19.227 1.00 22.64 C
ANISOU 716 CB LEU A 90 3619 2710 2274 -776 -610 13 C
ATOM 717 CG LEU A 90 -16.415 23.996 20.123 1.00 21.96 C
ANISOU 717 CG LEU A 90 3275 2749 2319 -622 -392 -75 C
ATOM 718 CD1 LEU A 90 -15.472 24.091 21.328 1.00 19.88 C
ANISOU 718 CD1 LEU A 90 2966 2494 2092 -557 -292 -104 C
ATOM 719 CD2 LEU A 90 -17.872 23.786 20.567 1.00 20.36 C
ANISOU 719 CD2 LEU A 90 2926 2617 2193 -429 -449 -98 C
ATOM 720 N THR A 91 -15.886 26.894 16.488 1.00 27.00 N
ANISOU 720 N THR A 91 4723 3140 2398 -1435 -1066 317 N
ATOM 721 CA THR A 91 -15.726 28.183 15.818 1.00 30.90 C
ANISOU 721 CA THR A 91 5609 3424 2707 -1720 -1428 528 C
ATOM 722 C THR A 91 -16.880 28.429 14.837 1.00 33.75 C
ANISOU 722 C THR A 91 6116 3664 3046 -1683 -1712 629 C
ATOM 723 O THR A 91 -17.388 29.556 14.721 1.00 35.73 O
ANISOU 723 O THR A 91 6719 3556 3303 -1609 -2152 760 O
ATOM 724 CB THR A 91 -14.377 28.305 15.069 1.00 32.42 C
ANISOU 724 CB THR A 91 5859 3896 2561 -2298 -1342 631 C
ATOM 725 OG1 THR A 91 -14.211 27.200 14.175 1.00 32.32 O
ANISOU 725 OG1 THR A 91 5567 4294 2420 -2444 -1071 515 O
ATOM 726 CG2 THR A 91 -13.234 28.325 16.033 1.00 31.81 C
ANISOU 726 CG2 THR A 91 5671 3939 2477 -2340 -1152 550 C
ATOM 727 N GLN A 92 -17.336 27.359 14.176 1.00 33.37 N
ANISOU 727 N GLN A 92 5812 3884 2985 -1693 -1504 548 N
ATOM 728 CA GLN A 92 -18.379 27.503 13.162 1.00 36.70 C
ANISOU 728 CA GLN A 92 6329 4267 3347 -1705 -1753 644 C
ATOM 729 C GLN A 92 -19.738 27.838 13.748 1.00 37.04 C
ANISOU 729 C GLN A 92 6334 4120 3621 -1192 -1986 569 C
ATOM 730 O GLN A 92 -20.588 28.385 13.064 1.00 41.31 O
ANISOU 730 O GLN A 92 7034 4538 4124 -1119 -2338 664 O
ATOM 731 CB GLN A 92 -18.478 26.247 12.292 1.00 35.75 C
ANISOU 731 CB GLN A 92 5950 4504 3129 -1879 -1474 545 C
ATOM 732 CG GLN A 92 -17.117 25.697 11.981 1.00 40.12 C
ANISOU 732 CG GLN A 92 6395 5363 3485 -2223 -1179 462 C
ATOM 733 CD GLN A 92 -17.062 24.854 10.754 1.00 47.37 C
ANISOU 733 CD GLN A 92 7178 6629 4189 -2488 -1039 368 C
ATOM 734 OE1 GLN A 92 -16.015 24.776 10.107 1.00 54.36 O
ANISOU 734 OE1 GLN A 92 8015 7859 4781 -2855 -915 319 O
ATOM 735 NE2 GLN A 92 -18.178 24.229 10.396 1.00 48.67 N
ANISOU 735 NE2 GLN A 92 7254 6780 4456 -2331 -1063 314 N
ATOM 736 N ILE A 93 -19.971 27.479 14.996 1.00 34.92 N
ANISOU 736 N ILE A 93 5815 3896 3557 -835 -1802 381 N
ATOM 737 CA ILE A 93 -21.233 27.834 15.611 1.00 36.03 C
ANISOU 737 CA ILE A 93 5830 4009 3852 -347 -2007 245 C
ATOM 738 C ILE A 93 -21.064 29.103 16.457 1.00 37.91 C
ANISOU 738 C ILE A 93 6320 3910 4175 -59 -2314 193 C
ATOM 739 O ILE A 93 -21.987 29.499 17.166 1.00 39.99 O
ANISOU 739 O ILE A 93 6445 4192 4557 430 -2489 -14 O
ATOM 740 CB ILE A 93 -21.861 26.643 16.413 1.00 33.86 C
ANISOU 740 CB ILE A 93 5086 4102 3677 -176 -1663 61 C
ATOM 741 CG1 ILE A 93 -21.053 26.341 17.685 1.00 32.60 C
ANISOU 741 CG1 ILE A 93 4820 3967 3599 -142 -1392 -19 C
ATOM 742 CG2 ILE A 93 -22.016 25.393 15.506 1.00 33.61 C
ANISOU 742 CG2 ILE A 93 4904 4303 3562 -486 -1438 105 C
ATOM 743 CD1 ILE A 93 -21.638 25.261 18.559 1.00 30.85 C
ANISOU 743 CD1 ILE A 93 4213 4077 3432 -56 -1130 -136 C
ATOM 744 N GLY A 94 -19.879 29.720 16.392 1.00 38.60 N
ANISOU 744 N GLY A 94 6753 3741 4172 -374 -2384 346 N
ATOM 745 CA GLY A 94 -19.634 31.025 17.035 1.00 41.43 C
ANISOU 745 CA GLY A 94 7480 3676 4584 -191 -2766 329 C
ATOM 746 C GLY A 94 -19.523 30.929 18.550 1.00 41.25 C
ANISOU 746 C GLY A 94 7213 3748 4711 150 -2557 76 C
ATOM 747 O GLY A 94 -19.890 31.853 19.299 1.00 43.18 O
ANISOU 747 O GLY A 94 7606 3743 5059 560 -2874 -104 O
ATOM 748 N CYS A 95 -19.000 29.803 19.002 1.00 37.81 N
ANISOU 748 N CYS A 95 6422 3669 4275 -11 -2056 44 N
ATOM 749 CA CYS A 95 -18.888 29.529 20.405 1.00 37.41 C
ANISOU 749 CA CYS A 95 6107 3784 4324 231 -1826 -150 C
ATOM 750 C CYS A 95 -17.685 30.250 20.994 1.00 37.57 C
ANISOU 750 C CYS A 95 6395 3572 4308 66 -1875 -107 C
ATOM 751 O CYS A 95 -16.570 30.151 20.452 1.00 36.29 O
ANISOU 751 O CYS A 95 6375 3401 4011 -393 -1771 82 O
ATOM 752 CB CYS A 95 -18.741 28.027 20.620 1.00 34.59 C
ANISOU 752 CB CYS A 95 5354 3817 3971 84 -1360 -152 C
ATOM 753 SG CYS A 95 -18.950 27.612 22.292 1.00 37.46 S
ANISOU 753 SG CYS A 95 5373 4449 4410 354 -1140 -346 S
ATOM 754 N THR A 96 -17.925 30.960 22.106 1.00 38.86 N
ANISOU 754 N THR A 96 6586 3622 4557 433 -2031 -317 N
ATOM 755 CA THR A 96 -16.891 31.702 22.820 1.00 39.20 C
ANISOU 755 CA THR A 96 6886 3442 4569 307 -2110 -315 C
ATOM 756 C THR A 96 -16.811 31.319 24.304 1.00 38.11 C
ANISOU 756 C THR A 96 6403 3591 4487 549 -1834 -537 C
ATOM 757 O THR A 96 -17.809 30.897 24.903 1.00 38.31 O
ANISOU 757 O THR A 96 6067 3922 4569 915 -1733 -751 O
ATOM 758 CB THR A 96 -17.109 33.248 22.700 1.00 43.84 C
ANISOU 758 CB THR A 96 8023 3460 5174 476 -2723 -359 C
ATOM 759 OG1 THR A 96 -18.326 33.629 23.358 1.00 45.40 O
ANISOU 759 OG1 THR A 96 8077 3664 5507 1146 -2942 -719 O
ATOM 760 CG2 THR A 96 -17.170 33.683 21.241 1.00 46.05 C
ANISOU 760 CG2 THR A 96 8708 3432 5356 164 -3067 -76 C
ATOM 761 N LEU A 97 -15.617 31.440 24.879 1.00 36.74 N
ANISOU 761 N LEU A 97 6313 3395 4252 290 -1712 -474 N
ATOM 762 CA LEU A 97 -15.436 31.359 26.315 1.00 36.73 C
ANISOU 762 CA LEU A 97 6089 3595 4271 487 -1547 -669 C
ATOM 763 C LEU A 97 -15.445 32.778 26.883 1.00 40.14 C
ANISOU 763 C LEU A 97 6890 3646 4717 709 -1960 -863 C
ATOM 764 O LEU A 97 -14.847 33.691 26.300 1.00 42.36 O
ANISOU 764 O LEU A 97 7666 3485 4944 443 -2289 -716 O
ATOM 765 CB LEU A 97 -14.092 30.713 26.632 1.00 34.62 C
ANISOU 765 CB LEU A 97 5708 3522 3924 106 -1226 -510 C
ATOM 766 CG LEU A 97 -13.953 29.208 26.713 1.00 33.38 C
ANISOU 766 CG LEU A 97 5150 3751 3781 25 -828 -432 C
ATOM 767 CD1 LEU A 97 -12.463 28.910 26.883 1.00 33.30 C
ANISOU 767 CD1 LEU A 97 5119 3851 3680 -295 -652 -319 C
ATOM 768 CD2 LEU A 97 -14.737 28.668 27.912 1.00 33.05 C
ANISOU 768 CD2 LEU A 97 4768 4010 3779 321 -682 -592 C
ATOM 769 N ASN A 98 -16.103 32.954 28.026 1.00 42.09 N
ANISOU 769 N ASN A 98 6908 4083 5000 1157 -1966 -1200 N
ATOM 770 CA ASN A 98 -16.269 34.273 28.651 1.00 46.86 C
ANISOU 770 CA ASN A 98 7837 4336 5631 1502 -2397 -1505 C
ATOM 771 C ASN A 98 -16.056 34.212 30.174 1.00 46.65 C
ANISOU 771 C ASN A 98 7523 4658 5544 1668 -2191 -1775 C
ATOM 772 O ASN A 98 -16.650 33.378 30.836 1.00 45.02 O
ANISOU 772 O ASN A 98 6787 5028 5291 1836 -1867 -1907 O
ATOM 773 CB ASN A 98 -17.704 34.809 28.403 1.00 50.91 C
ANISOU 773 CB ASN A 98 8339 4771 6233 2111 -2766 -1829 C
ATOM 774 CG ASN A 98 -18.233 34.558 26.974 1.00 52.99 C
ANISOU 774 CG ASN A 98 8701 4893 6539 2012 -2886 -1585 C
ATOM 775 OD1 ASN A 98 -18.895 33.538 26.677 1.00 50.77 O
ANISOU 775 OD1 ASN A 98 7969 5074 6246 2024 -2575 -1539 O
ATOM 776 ND2 ASN A 98 -17.990 35.526 26.101 1.00 57.77 N
ANISOU 776 ND2 ASN A 98 9930 4852 7170 1891 -3387 -1427 N
ATOM 777 N PHE A 99 -15.257 35.122 30.733 1.00 48.78 N
ANISOU 777 N PHE A 99 8157 4599 5780 1584 -2413 -1853 N
ATOM 778 CA PHE A 99 -15.120 35.247 32.192 1.00 50.02 C
ANISOU 778 CA PHE A 99 8085 5063 5859 1782 -2291 -2166 C
ATOM 779 C PHE A 99 -14.577 36.633 32.572 1.00 54.34 C
ANISOU 779 C PHE A 99 9201 5043 6401 1825 -2761 -2357 C
ATOM 780 O PHE A 99 -14.479 37.015 33.760 1.00 55.98 O
ANISOU 780 O PHE A 99 9327 5404 6540 2037 -2774 -2694 O
ATOM 781 CB PHE A 99 -14.229 34.129 32.767 1.00 45.99 C
ANISOU 781 CB PHE A 99 7201 5031 5244 1364 -1767 -1907 C
ATOM 782 CG PHE A 99 -12.782 34.248 32.379 1.00 45.95 C
ANISOU 782 CG PHE A 99 7506 4765 5188 802 -1749 -1564 C
ATOM 783 CD1 PHE A 99 -12.338 33.763 31.152 1.00 44.14 C
ANISOU 783 CD1 PHE A 99 7360 4442 4967 420 -1664 -1202 C
ATOM 784 CD2 PHE A 99 -11.862 34.862 33.241 1.00 48.01 C
ANISOU 784 CD2 PHE A 99 7938 4953 5349 636 -1820 -1637 C
ATOM 785 CE1 PHE A 99 -11.016 33.889 30.785 1.00 44.22 C
ANISOU 785 CE1 PHE A 99 7570 4370 4864 -111 -1640 -938 C
ATOM 786 CE2 PHE A 99 -10.527 34.993 32.878 1.00 47.76 C
ANISOU 786 CE2 PHE A 99 8133 4795 5217 75 -1807 -1337 C
ATOM 787 CZ PHE A 99 -10.098 34.501 31.651 1.00 44.11 C
ANISOU 787 CZ PHE A 99 7699 4323 4737 -300 -1708 -996 C
ATOM 788 OXT PHE A 99 -14.215 37.407 31.676 1.00 56.36 O
ANISOU 788 OXT PHE A 99 10051 4665 6699 1598 -3169 -2162 O
TER 789 PHE A 99
ATOM 790 N PRO B 1 -12.096 38.200 30.141 1.00 64.30 N
ANISOU 790 N PRO B 1 11963 4795 7672 168 -3220 -1103 N
ATOM 791 CA PRO B 1 -12.521 38.703 28.836 1.00 67.01 C
ANISOU 791 CA PRO B 1 12850 4630 7980 126 -3615 -925 C
ATOM 792 C PRO B 1 -13.306 37.649 28.037 1.00 63.40 C
ANISOU 792 C PRO B 1 11931 4558 7601 310 -3346 -829 C
ATOM 793 O PRO B 1 -13.541 36.551 28.530 1.00 58.81 O
ANISOU 793 O PRO B 1 10658 4595 7091 462 -2884 -906 O
ATOM 794 CB PRO B 1 -11.188 38.996 28.147 1.00 68.28 C
ANISOU 794 CB PRO B 1 13431 4587 7925 -774 -3612 -513 C
ATOM 795 CG PRO B 1 -10.267 37.915 28.684 1.00 63.56 C
ANISOU 795 CG PRO B 1 12131 4705 7314 -1100 -2976 -428 C
ATOM 796 CD PRO B 1 -10.719 37.661 30.112 1.00 61.82 C
ANISOU 796 CD PRO B 1 11461 4785 7244 -543 -2827 -793 C
ATOM 797 N GLN B 2 -13.728 37.995 26.825 1.00 65.47 N
ANISOU 797 N GLN B 2 12626 4430 7821 266 -3675 -653 N
ATOM 798 CA GLN B 2 -14.343 37.017 25.930 1.00 62.83 C
ANISOU 798 CA GLN B 2 11916 4438 7518 313 -3425 -513 C
ATOM 799 C GLN B 2 -13.271 36.463 24.997 1.00 60.24 C
ANISOU 799 C GLN B 2 11604 4243 7040 -472 -3111 -96 C
ATOM 800 O GLN B 2 -12.448 37.205 24.475 1.00 63.22 O
ANISOU 800 O GLN B 2 12535 4251 7234 -1034 -3341 135 O
ATOM 801 CB GLN B 2 -15.487 37.639 25.110 1.00 66.99 C
ANISOU 801 CB GLN B 2 12838 4546 8067 754 -3965 -584 C
ATOM 802 CG GLN B 2 -16.305 36.619 24.302 1.00 65.07 C
ANISOU 802 CG GLN B 2 12145 4727 7853 874 -3716 -501 C
ATOM 803 CD GLN B 2 -16.999 37.219 23.083 1.00 70.84 C
ANISOU 803 CD GLN B 2 13399 4987 8531 992 -4243 -379 C
ATOM 804 OE1 GLN B 2 -16.353 37.554 22.086 1.00 73.28 O
ANISOU 804 OE1 GLN B 2 14245 4912 8684 397 -4405 -7 O
ATOM 805 NE2 GLN B 2 -18.322 37.342 23.153 1.00 73.45 N
ANISOU 805 NE2 GLN B 2 13546 5412 8949 1736 -4521 -702 N
ATOM 806 N ILE B 3 -13.310 35.154 24.781 1.00 55.41 N
ANISOU 806 N ILE B 3 10395 4191 6469 -522 -2611 -26 N
ATOM 807 CA ILE B 3 -12.296 34.432 24.016 1.00 52.85 C
ANISOU 807 CA ILE B 3 9928 4145 6006 -1143 -2249 254 C
ATOM 808 C ILE B 3 -12.953 33.601 22.881 1.00 50.08 C
ANISOU 808 C ILE B 3 9415 3965 5648 -1126 -2116 378 C
ATOM 809 O ILE B 3 -13.756 32.712 23.165 1.00 47.43 O
ANISOU 809 O ILE B 3 8639 3942 5439 -734 -1907 246 O
ATOM 810 CB ILE B 3 -11.524 33.475 24.985 1.00 49.18 C
ANISOU 810 CB ILE B 3 8882 4210 5596 -1184 -1762 171 C
ATOM 811 CG1 ILE B 3 -10.848 34.282 26.106 1.00 52.49 C
ANISOU 811 CG1 ILE B 3 9441 4505 5999 -1242 -1882 54 C
ATOM 812 CG2 ILE B 3 -10.487 32.656 24.262 1.00 47.96 C
ANISOU 812 CG2 ILE B 3 8498 4420 5305 -1679 -1405 352 C
ATOM 813 CD1 ILE B 3 -10.465 33.486 27.335 1.00 50.42 C
ANISOU 813 CD1 ILE B 3 8638 4695 5825 -1083 -1528 -91 C
ATOM 814 N THR B 4 -12.621 33.904 21.622 1.00 50.42 N
ANISOU 814 N THR B 4 9832 3827 5498 -1609 -2250 632 N
ATOM 815 CA THR B 4 -12.951 33.026 20.486 1.00 46.96 C
ANISOU 815 CA THR B 4 9216 3627 5000 -1736 -2050 765 C
ATOM 816 C THR B 4 -12.044 31.781 20.459 1.00 41.77 C
ANISOU 816 C THR B 4 8037 3532 4300 -1994 -1496 765 C
ATOM 817 O THR B 4 -11.074 31.688 21.200 1.00 40.74 O
ANISOU 817 O THR B 4 7711 3610 4159 -2131 -1300 699 O
ATOM 818 CB THR B 4 -12.741 33.733 19.162 1.00 51.13 C
ANISOU 818 CB THR B 4 10304 3852 5271 -2267 -2352 1038 C
ATOM 819 OG1 THR B 4 -11.484 34.414 19.206 1.00 54.31 O
ANISOU 819 OG1 THR B 4 10988 4202 5444 -2894 -2396 1163 O
ATOM 820 CG2 THR B 4 -13.880 34.715 18.860 1.00 56.09 C
ANISOU 820 CG2 THR B 4 11472 3895 5946 -1908 -2967 1050 C
ATOM 821 N LEU B 5 -12.334 30.845 19.563 1.00 37.73 N
ANISOU 821 N LEU B 5 7329 3259 3749 -2047 -1284 820 N
ATOM 822 CA LEU B 5 -11.713 29.524 19.638 1.00 33.19 C
ANISOU 822 CA LEU B 5 6269 3159 3183 -2080 -827 736 C
ATOM 823 C LEU B 5 -10.982 29.117 18.347 1.00 34.01 C
ANISOU 823 C LEU B 5 6353 3533 3036 -2572 -643 824 C
ATOM 824 O LEU B 5 -10.719 27.943 18.112 1.00 31.73 O
ANISOU 824 O LEU B 5 5723 3585 2749 -2509 -332 718 O
ATOM 825 CB LEU B 5 -12.767 28.493 20.063 1.00 30.15 C
ANISOU 825 CB LEU B 5 5585 2884 2987 -1600 -702 625 C
ATOM 826 CG LEU B 5 -13.259 28.613 21.526 1.00 28.23 C
ANISOU 826 CG LEU B 5 5182 2619 2925 -1174 -758 470 C
ATOM 827 CD1 LEU B 5 -14.583 27.855 21.720 1.00 24.55 C
ANISOU 827 CD1 LEU B 5 4503 2291 2536 -832 -732 394 C
ATOM 828 CD2 LEU B 5 -12.195 28.108 22.507 1.00 24.01 C
ANISOU 828 CD2 LEU B 5 4377 2317 2430 -1200 -513 385 C
ATOM 829 N TRP B 6 -10.632 30.116 17.533 1.00 37.25 N
ANISOU 829 N TRP B 6 7166 3793 3196 -3084 -870 1002 N
ATOM 830 CA TRP B 6 -9.811 29.915 16.335 1.00 39.57 C
ANISOU 830 CA TRP B 6 7432 4452 3151 -3685 -701 1071 C
ATOM 831 C TRP B 6 -8.421 29.398 16.693 1.00 39.68 C
ANISOU 831 C TRP B 6 6991 5041 3045 -3876 -343 883 C
ATOM 832 O TRP B 6 -7.804 28.658 15.929 1.00 40.97 O
ANISOU 832 O TRP B 6 6852 5707 3008 -4092 -63 765 O
ATOM 833 CB TRP B 6 -9.712 31.219 15.535 1.00 44.27 C
ANISOU 833 CB TRP B 6 8632 4750 3439 -4300 -1087 1342 C
ATOM 834 CG TRP B 6 -11.062 31.686 15.166 1.00 45.06 C
ANISOU 834 CG TRP B 6 9163 4297 3662 -4012 -1494 1487 C
ATOM 835 CD1 TRP B 6 -11.795 32.638 15.799 1.00 47.31 C
ANISOU 835 CD1 TRP B 6 9851 4002 4121 -3659 -1945 1520 C
ATOM 836 CD2 TRP B 6 -11.880 31.171 14.120 1.00 44.76 C
ANISOU 836 CD2 TRP B 6 9145 4278 3583 -3969 -1500 1561 C
ATOM 837 NE1 TRP B 6 -13.020 32.766 15.197 1.00 49.16 N
ANISOU 837 NE1 TRP B 6 10329 3924 4425 -3366 -2253 1597 N
ATOM 838 CE2 TRP B 6 -13.096 31.877 14.159 1.00 47.12 C
ANISOU 838 CE2 TRP B 6 9846 4025 4032 -3585 -1980 1651 C
ATOM 839 CE3 TRP B 6 -11.697 30.189 13.138 1.00 45.36 C
ANISOU 839 CE3 TRP B 6 8936 4805 3493 -4202 -1165 1529 C
ATOM 840 CZ2 TRP B 6 -14.129 31.640 13.248 1.00 49.02 C
ANISOU 840 CZ2 TRP B 6 10192 4177 4255 -3461 -2134 1742 C
ATOM 841 CZ3 TRP B 6 -12.727 29.946 12.235 1.00 46.08 C
ANISOU 841 CZ3 TRP B 6 9173 4768 3567 -4116 -1302 1633 C
ATOM 842 CH2 TRP B 6 -13.930 30.665 12.301 1.00 47.44 C
ANISOU 842 CH2 TRP B 6 9724 4413 3887 -3762 -1778 1753 C
ATOM 843 N GLN B 7 -7.953 29.783 17.873 0.50 38.63 N
ANISOU 843 N GLN B 7 6786 4863 3027 -3748 -372 814 N
ATOM 844 CA AGLN B 7 -6.705 29.272 18.407 0.50 38.80 C
ANISOU 844 CA AGLN B 7 6328 5436 2976 -3803 -74 607 C
ATOM 845 CA BGLN B 7 -6.709 29.265 18.412 0.50 38.74 C
ANISOU 845 CA BGLN B 7 6319 5428 2971 -3799 -73 606 C
ATOM 846 C GLN B 7 -6.991 28.579 19.750 1.00 35.07 C
ANISOU 846 C GLN B 7 5582 4872 2872 -3129 10 450 C
ATOM 847 O GLN B 7 -8.069 28.769 20.341 1.00 33.38 O
ANISOU 847 O GLN B 7 5568 4209 2904 -2747 -173 510 O
ATOM 848 CB AGLN B 7 -5.672 30.408 18.539 0.50 42.91 C
ANISOU 848 CB AGLN B 7 7013 6102 3188 -4451 -191 691 C
ATOM 849 CB BGLN B 7 -5.690 30.393 18.591 0.50 42.78 C
ANISOU 849 CB BGLN B 7 6991 6075 3188 -4423 -191 687 C
ATOM 850 CG AGLN B 7 -6.175 31.653 19.291 0.50 44.38 C
ANISOU 850 CG AGLN B 7 7744 5631 3486 -4443 -597 861 C
ATOM 851 CG BGLN B 7 -5.224 31.019 17.293 0.50 47.69 C
ANISOU 851 CG BGLN B 7 7866 6916 3337 -5254 -262 852 C
ATOM 852 CD AGLN B 7 -5.284 32.893 19.128 0.50 50.47 C
ANISOU 852 CD AGLN B 7 8894 6419 3864 -5259 -815 1022 C
ATOM 853 CD BGLN B 7 -4.026 31.969 17.484 0.50 55.20 C
ANISOU 853 CD BGLN B 7 8895 8181 3897 -6010 -328 910 C
ATOM 854 OE1AGLN B 7 -4.547 33.035 18.144 0.50 56.30 O
ANISOU 854 OE1AGLN B 7 9626 7593 4173 -5980 -736 1101 O
ATOM 855 OE1BGLN B 7 -4.089 32.790 18.501 0.50 57.68 O
ANISOU 855 OE1BGLN B 7 9521 8044 4349 -5939 -585 988 O
ATOM 856 NE2AGLN B 7 -5.368 33.803 20.089 0.50 50.73 N
ANISOU 856 NE2AGLN B 7 9280 5995 3998 -5195 -1107 1063 N
ATOM 857 NE2BGLN B 7 -3.016 31.860 16.502 0.50 60.10 N
ANISOU 857 NE2BGLN B 7 9237 9593 4004 -6739 -109 851 N
ATOM 858 N ARG B 8 -6.061 27.754 20.221 1.00 34.19 N
ANISOU 858 N ARG B 8 5005 5221 2764 -2975 261 233 N
ATOM 859 CA ARG B 8 -6.202 27.142 21.576 1.00 31.56 C
ANISOU 859 CA ARG B 8 4465 4802 2723 -2426 292 122 C
ATOM 860 C ARG B 8 -6.367 28.268 22.615 1.00 30.64 C
ANISOU 860 C ARG B 8 4586 4370 2686 -2462 76 218 C
ATOM 861 O ARG B 8 -5.654 29.267 22.539 1.00 32.68 O
ANISOU 861 O ARG B 8 4986 4696 2735 -2928 -15 277 O
ATOM 862 CB ARG B 8 -4.954 26.337 21.902 1.00 33.24 C
ANISOU 862 CB ARG B 8 4199 5561 2869 -2317 501 -123 C
ATOM 863 CG ARG B 8 -4.943 24.927 21.290 1.00 36.75 C
ANISOU 863 CG ARG B 8 4414 6206 3342 -1989 657 -312 C
ATOM 864 CD ARG B 8 -3.602 24.276 21.574 1.00 44.56 C
ANISOU 864 CD ARG B 8 4927 7769 4234 -1825 790 -619 C
ATOM 865 NE ARG B 8 -3.673 22.814 21.641 1.00 49.42 N
ANISOU 865 NE ARG B 8 5415 8362 5001 -1256 808 -825 N
ATOM 866 CZ ARG B 8 -3.083 21.987 20.775 1.00 53.02 C
ANISOU 866 CZ ARG B 8 5618 9215 5312 -1114 920 -1127 C
ATOM 867 NH1 ARG B 8 -2.372 22.469 19.758 1.00 57.76 N
ANISOU 867 NH1 ARG B 8 5985 10385 5578 -1553 1077 -1265 N
ATOM 868 NH2 ARG B 8 -3.193 20.670 20.927 1.00 52.71 N
ANISOU 868 NH2 ARG B 8 5583 9019 5424 -553 848 -1313 N
ATOM 869 N PRO B 9 -7.345 28.131 23.528 1.00 28.14 N
ANISOU 869 N PRO B 9 4336 3731 2625 -2019 -23 220 N
ATOM 870 CA PRO B 9 -7.612 29.111 24.574 1.00 28.20 C
ANISOU 870 CA PRO B 9 4537 3460 2716 -1948 -229 231 C
ATOM 871 C PRO B 9 -6.588 28.971 25.720 1.00 29.08 C
ANISOU 871 C PRO B 9 4360 3859 2832 -1924 -124 118 C
ATOM 872 O PRO B 9 -6.893 28.462 26.803 1.00 26.38 O
ANISOU 872 O PRO B 9 3851 3523 2650 -1563 -96 44 O
ATOM 873 CB PRO B 9 -9.044 28.785 24.988 1.00 25.24 C
ANISOU 873 CB PRO B 9 4206 2841 2545 -1489 -313 210 C
ATOM 874 CG PRO B 9 -9.153 27.308 24.807 1.00 24.55 C
ANISOU 874 CG PRO B 9 3831 2986 2513 -1295 -89 175 C
ATOM 875 CD PRO B 9 -8.307 27.006 23.572 1.00 25.55 C
ANISOU 875 CD PRO B 9 3904 3333 2471 -1604 49 191 C
ATOM 876 N LEU B 10 -5.368 29.427 25.433 1.00 28.35 N
ANISOU 876 N LEU B 10 4386 3474 2913 -1373 -1053 768 N
ATOM 877 CA LEU B 10 -4.244 29.352 26.375 1.00 28.56 C
ANISOU 877 CA LEU B 10 4308 3560 2983 -1281 -842 626 C
ATOM 878 C LEU B 10 -4.195 30.601 27.224 1.00 28.58 C
ANISOU 878 C LEU B 10 4373 3363 3125 -1131 -1029 670 C
ATOM 879 O LEU B 10 -4.374 31.710 26.706 1.00 31.79 O
ANISOU 879 O LEU B 10 4983 3588 3509 -1269 -1315 824 O
ATOM 880 CB LEU B 10 -2.916 29.230 25.634 1.00 30.07 C
ANISOU 880 CB LEU B 10 4542 3929 2953 -1635 -670 558 C
ATOM 881 CG LEU B 10 -2.676 27.883 24.965 1.00 32.35 C
ANISOU 881 CG LEU B 10 4699 4439 3152 -1755 -416 391 C
ATOM 882 CD1 LEU B 10 -1.495 28.010 23.982 1.00 38.14 C
ANISOU 882 CD1 LEU B 10 5472 5389 3631 -2200 -269 278 C
ATOM 883 CD2 LEU B 10 -2.428 26.808 26.014 1.00 34.79 C
ANISOU 883 CD2 LEU B 10 4775 4771 3674 -1431 -231 212 C
ATOM 884 N VAL B 11 -3.972 30.429 28.523 1.00 25.65 N
ANISOU 884 N VAL B 11 3846 3005 2896 -874 -902 540 N
ATOM 885 CA VAL B 11 -3.892 31.569 29.428 1.00 26.06 C
ANISOU 885 CA VAL B 11 3932 2890 3080 -734 -1041 525 C
ATOM 886 C VAL B 11 -2.658 31.433 30.331 1.00 24.65 C
ANISOU 886 C VAL B 11 3674 2816 2876 -724 -844 420 C
ATOM 887 O VAL B 11 -2.140 30.337 30.548 1.00 23.06 O
ANISOU 887 O VAL B 11 3339 2783 2641 -711 -632 337 O
ATOM 888 CB VAL B 11 -5.185 31.749 30.298 1.00 25.65 C
ANISOU 888 CB VAL B 11 3747 2745 3255 -415 -1141 430 C
ATOM 889 CG1 VAL B 11 -6.401 32.070 29.433 1.00 30.78 C
ANISOU 889 CG1 VAL B 11 4445 3256 3993 -392 -1410 514 C
ATOM 890 CG2 VAL B 11 -5.445 30.499 31.145 1.00 25.63 C
ANISOU 890 CG2 VAL B 11 3540 2945 3253 -279 -889 304 C
ATOM 891 N THR B 12 -2.216 32.555 30.871 1.00 24.77 N
ANISOU 891 N THR B 12 3772 2703 2936 -720 -953 419 N
ATOM 892 CA THR B 12 -1.168 32.561 31.857 1.00 25.05 C
ANISOU 892 CA THR B 12 3727 2825 2965 -693 -811 322 C
ATOM 893 C THR B 12 -1.757 32.234 33.240 1.00 24.73 C
ANISOU 893 C THR B 12 3532 2810 3053 -423 -749 203 C
ATOM 894 O THR B 12 -2.815 32.778 33.625 1.00 25.37 O
ANISOU 894 O THR B 12 3597 2778 3264 -265 -868 148 O
ATOM 895 CB THR B 12 -0.525 33.923 31.888 1.00 27.01 C
ANISOU 895 CB THR B 12 4143 2928 3190 -833 -959 365 C
ATOM 896 OG1 THR B 12 0.004 34.182 30.589 1.00 28.79 O
ANISOU 896 OG1 THR B 12 4537 3175 3229 -1180 -1013 484 O
ATOM 897 CG2 THR B 12 0.619 33.956 32.879 1.00 28.37 C
ANISOU 897 CG2 THR B 12 4225 3212 3342 -832 -819 262 C
ATOM 898 N ILE B 13 -1.090 31.321 33.955 1.00 22.98 N
ANISOU 898 N ILE B 13 3188 2746 2799 -395 -584 146 N
ATOM 899 CA ILE B 13 -1.462 30.989 35.325 1.00 22.55 C
ANISOU 899 CA ILE B 13 3032 2754 2784 -252 -533 63 C
ATOM 900 C ILE B 13 -0.252 31.198 36.232 1.00 23.44 C
ANISOU 900 C ILE B 13 3127 2918 2863 -297 -500 30 C
ATOM 901 O ILE B 13 0.912 31.152 35.780 1.00 23.49 O
ANISOU 901 O ILE B 13 3132 2957 2835 -408 -476 49 O
ATOM 902 CB ILE B 13 -1.995 29.549 35.470 1.00 21.92 C
ANISOU 902 CB ILE B 13 2861 2785 2684 -208 -444 74 C
ATOM 903 CG1 ILE B 13 -0.860 28.522 35.243 1.00 20.72 C
ANISOU 903 CG1 ILE B 13 2665 2690 2518 -268 -384 102 C
ATOM 904 CG2 ILE B 13 -3.171 29.331 34.511 1.00 23.25 C
ANISOU 904 CG2 ILE B 13 3035 2924 2875 -185 -474 102 C
ATOM 905 CD1 ILE B 13 -1.218 27.059 35.557 1.00 21.06 C
ANISOU 905 CD1 ILE B 13 2654 2775 2573 -230 -359 125 C
ATOM 906 N LYS B 14 -0.539 31.471 37.492 1.00 23.08 N
ANISOU 906 N LYS B 14 3049 2906 2815 -238 -496 -50 N
ATOM 907 CA LYS B 14 0.491 31.576 38.490 1.00 24.01 C
ANISOU 907 CA LYS B 14 3152 3092 2881 -295 -486 -71 C
ATOM 908 C LYS B 14 0.077 30.627 39.608 1.00 24.09 C
ANISOU 908 C LYS B 14 3105 3231 2818 -296 -452 -75 C
ATOM 909 O LYS B 14 -1.042 30.700 40.118 1.00 24.49 O
ANISOU 909 O LYS B 14 3130 3338 2836 -278 -413 -165 O
ATOM 910 CB LYS B 14 0.652 33.024 38.967 1.00 25.00 C
ANISOU 910 CB LYS B 14 3344 3134 3023 -314 -538 -165 C
ATOM 911 CG LYS B 14 1.829 33.186 39.943 1.00 26.06 C
ANISOU 911 CG LYS B 14 3466 3354 3083 -406 -533 -179 C
ATOM 912 CD LYS B 14 1.916 34.594 40.501 1.00 29.56 C
ANISOU 912 CD LYS B 14 3982 3710 3539 -436 -576 -299 C
ATOM 913 CE LYS B 14 3.082 34.683 41.465 1.00 32.94 C
ANISOU 913 CE LYS B 14 4394 4252 3871 -552 -573 -305 C
ATOM 914 NZ LYS B 14 3.189 36.065 41.987 1.00 35.82 N
ANISOU 914 NZ LYS B 14 4842 4524 4246 -599 -610 -440 N
ATOM 915 N ILE B 15 0.978 29.706 39.933 1.00 25.30 N
ANISOU 915 N ILE B 15 3232 3429 2951 -339 -491 12 N
ATOM 916 CA ILE B 15 0.736 28.635 40.894 1.00 26.61 C
ANISOU 916 CA ILE B 15 3404 3675 3032 -401 -538 82 C
ATOM 917 C ILE B 15 2.053 28.240 41.563 1.00 28.31 C
ANISOU 917 C ILE B 15 3607 3888 3259 -451 -675 157 C
ATOM 918 O ILE B 15 3.099 28.110 40.904 1.00 28.41 O
ANISOU 918 O ILE B 15 3542 3842 3411 -388 -717 150 O
ATOM 919 CB ILE B 15 0.034 27.400 40.241 1.00 26.78 C
ANISOU 919 CB ILE B 15 3422 3666 3088 -368 -535 156 C
ATOM 920 CG1 ILE B 15 -0.355 26.385 41.335 1.00 29.27 C
ANISOU 920 CG1 ILE B 15 3803 4051 3269 -506 -618 254 C
ATOM 921 CG2 ILE B 15 0.908 26.766 39.146 1.00 26.59 C
ANISOU 921 CG2 ILE B 15 3338 3540 3224 -287 -571 181 C
ATOM 922 CD1 ILE B 15 -1.084 25.146 40.818 1.00 29.58 C
ANISOU 922 CD1 ILE B 15 3870 4046 3324 -514 -636 334 C
ATOM 923 N GLY B 16 2.011 28.123 42.885 1.00 29.65 N
ANISOU 923 N GLY B 16 3840 4148 3276 -592 -749 202 N
ATOM 924 CA GLY B 16 3.205 27.823 43.682 1.00 30.76 C
ANISOU 924 CA GLY B 16 3985 4284 3420 -661 -942 295 C
ATOM 925 C GLY B 16 4.365 28.753 43.405 1.00 30.54 C
ANISOU 925 C GLY B 16 3871 4245 3489 -607 -931 207 C
ATOM 926 O GLY B 16 5.508 28.302 43.390 1.00 31.74 O
ANISOU 926 O GLY B 16 3932 4353 3775 -567 -1087 240 O
ATOM 927 N GLY B 17 4.067 30.039 43.182 1.00 28.87 N
ANISOU 927 N GLY B 17 3678 4061 3231 -611 -774 78 N
ATOM 928 CA GLY B 17 5.080 31.054 42.870 1.00 27.98 C
ANISOU 928 CA GLY B 17 3526 3936 3169 -621 -757 0 C
ATOM 929 C GLY B 17 5.608 31.048 41.433 1.00 26.19 C
ANISOU 929 C GLY B 17 3216 3651 3083 -555 -704 -36 C
ATOM 930 O GLY B 17 6.494 31.833 41.096 1.00 26.92 O
ANISOU 930 O GLY B 17 3278 3765 3185 -628 -684 -102 O
ATOM 931 N GLN B 18 5.078 30.150 40.607 1.00 24.08 N
ANISOU 931 N GLN B 18 2916 3339 2894 -468 -676 -7 N
ATOM 932 CA GLN B 18 5.596 29.905 39.247 1.00 23.27 C
ANISOU 932 CA GLN B 18 2713 3231 2896 -456 -612 -73 C
ATOM 933 C GLN B 18 4.599 30.349 38.209 1.00 21.54 C
ANISOU 933 C GLN B 18 2598 2958 2630 -470 -509 -64 C
ATOM 934 O GLN B 18 3.381 30.228 38.419 1.00 21.63 O
ANISOU 934 O GLN B 18 2689 2920 2608 -406 -503 -13 O
ATOM 935 CB GLN B 18 5.867 28.418 39.058 1.00 23.85 C
ANISOU 935 CB GLN B 18 2654 3281 3126 -352 -689 -77 C
ATOM 936 CG GLN B 18 6.881 27.870 40.036 1.00 26.88 C
ANISOU 936 CG GLN B 18 2931 3666 3618 -317 -887 -69 C
ATOM 937 CD GLN B 18 7.019 26.388 39.896 1.00 30.60 C
ANISOU 937 CD GLN B 18 3299 4027 4300 -186 -1040 -69 C
ATOM 938 OE1 GLN B 18 7.408 25.894 38.835 1.00 31.72 O
ANISOU 938 OE1 GLN B 18 3275 4168 4611 -119 -974 -236 O
ATOM 939 NE2 GLN B 18 6.691 25.651 40.965 1.00 32.74 N
ANISOU 939 NE2 GLN B 18 3682 4203 4556 -181 -1261 107 N
ATOM 940 N LEU B 19 5.112 30.779 37.061 1.00 20.25 N
ANISOU 940 N LEU B 19 2420 2821 2453 -586 -442 -122 N
ATOM 941 CA LEU B 19 4.265 31.228 35.959 1.00 19.76 C
ANISOU 941 CA LEU B 19 2486 2691 2329 -652 -405 -78 C
ATOM 942 C LEU B 19 4.254 30.171 34.884 1.00 19.75 C
ANISOU 942 C LEU B 19 2388 2754 2363 -669 -326 -124 C
ATOM 943 O LEU B 19 5.318 29.747 34.438 1.00 19.93 O
ANISOU 943 O LEU B 19 2252 2899 2423 -751 -259 -261 O
ATOM 944 CB LEU B 19 4.803 32.522 35.327 1.00 19.80 C
ANISOU 944 CB LEU B 19 2612 2682 2229 -878 -417 -78 C
ATOM 945 CG LEU B 19 5.072 33.646 36.314 1.00 24.13 C
ANISOU 945 CG LEU B 19 3251 3160 2757 -894 -495 -74 C
ATOM 946 CD1 LEU B 19 5.670 34.873 35.562 1.00 25.36 C
ANISOU 946 CD1 LEU B 19 3566 3274 2795 -1177 -538 -52 C
ATOM 947 CD2 LEU B 19 3.819 33.983 37.124 1.00 24.34 C
ANISOU 947 CD2 LEU B 19 3363 3045 2841 -711 -567 -51 C
ATOM 948 N LYS B 20 3.059 29.787 34.457 1.00 19.32 N
ANISOU 948 N LYS B 20 2405 2631 2304 -601 -328 -51 N
ATOM 949 CA LYS B 20 2.898 28.757 33.445 1.00 20.86 C
ANISOU 949 CA LYS B 20 2527 2878 2522 -625 -251 -101 C
ATOM 950 C LYS B 20 1.818 29.157 32.452 1.00 20.93 C
ANISOU 950 C LYS B 20 2688 2834 2432 -713 -268 -4 C
ATOM 951 O LYS B 20 1.070 30.108 32.673 1.00 21.67 O
ANISOU 951 O LYS B 20 2920 2812 2502 -688 -376 96 O
ATOM 952 CB LYS B 20 2.510 27.418 34.110 1.00 20.56 C
ANISOU 952 CB LYS B 20 2401 2802 2609 -433 -279 -97 C
ATOM 953 CG LYS B 20 3.591 26.865 35.044 1.00 23.90 C
ANISOU 953 CG LYS B 20 2684 3233 3163 -347 -350 -165 C
ATOM 954 CD LYS B 20 3.057 25.621 35.754 1.00 29.11 C
ANISOU 954 CD LYS B 20 3347 3798 3916 -212 -458 -90 C
ATOM 955 CE LYS B 20 4.132 24.988 36.632 1.00 34.40 C
ANISOU 955 CE LYS B 20 3901 4419 4749 -131 -623 -124 C
ATOM 956 NZ LYS B 20 5.205 24.454 35.767 1.00 39.40 N
ANISOU 956 NZ LYS B 20 4307 5079 5584 -98 -594 -359 N
ATOM 957 N GLU B 21 1.751 28.420 31.354 1.00 21.40 N
ANISOU 957 N GLU B 21 2705 2968 2456 -815 -184 -59 N
ATOM 958 CA GLU B 21 0.692 28.555 30.366 1.00 23.34 C
ANISOU 958 CA GLU B 21 3085 3176 2606 -911 -225 45 C
ATOM 959 C GLU B 21 -0.195 27.334 30.511 1.00 21.27 C
ANISOU 959 C GLU B 21 2750 2896 2433 -737 -196 41 C
ATOM 960 O GLU B 21 0.323 26.231 30.683 1.00 21.42 O
ANISOU 960 O GLU B 21 2628 2961 2550 -667 -115 -80 O
ATOM 961 CB GLU B 21 1.284 28.528 28.966 1.00 24.85 C
ANISOU 961 CB GLU B 21 3291 3516 2635 -1237 -128 -33 C
ATOM 962 CG GLU B 21 2.099 29.762 28.640 1.00 32.69 C
ANISOU 962 CG GLU B 21 4403 4548 3468 -1523 -166 -5 C
ATOM 963 CD GLU B 21 1.293 30.746 27.849 1.00 40.86 C
ANISOU 963 CD GLU B 21 5718 5456 4349 -1728 -364 217 C
ATOM 964 OE1 GLU B 21 0.034 30.702 27.946 1.00 43.68 O
ANISOU 964 OE1 GLU B 21 6144 5654 4800 -1532 -507 345 O
ATOM 965 OE2 GLU B 21 1.919 31.538 27.110 1.00 44.59 O
ANISOU 965 OE2 GLU B 21 6341 5995 4607 -2111 -397 257 O
ATOM 966 N ALA B 22 -1.508 27.536 30.415 1.00 20.14 N
ANISOU 966 N ALA B 22 2698 2676 2277 -675 -288 158 N
ATOM 967 CA ALA B 22 -2.485 26.453 30.572 1.00 19.29 C
ANISOU 967 CA ALA B 22 2536 2572 2222 -554 -264 163 C
ATOM 968 C ALA B 22 -3.700 26.648 29.683 1.00 19.72 C
ANISOU 968 C ALA B 22 2668 2606 2217 -612 -344 249 C
ATOM 969 O ALA B 22 -4.081 27.783 29.365 1.00 20.64 O
ANISOU 969 O ALA B 22 2889 2640 2313 -654 -495 335 O
ATOM 970 CB ALA B 22 -2.930 26.326 32.043 1.00 18.57 C
ANISOU 970 CB ALA B 22 2400 2451 2206 -370 -295 172 C
ATOM 971 N LEU B 23 -4.335 25.542 29.329 1.00 19.62 N
ANISOU 971 N LEU B 23 2612 2642 2200 -608 -283 232 N
ATOM 972 CA LEU B 23 -5.415 25.537 28.373 1.00 21.73 C
ANISOU 972 CA LEU B 23 2934 2919 2404 -690 -356 303 C
ATOM 973 C LEU B 23 -6.733 25.594 29.139 1.00 21.24 C
ANISOU 973 C LEU B 23 2808 2835 2426 -512 -437 322 C
ATOM 974 O LEU B 23 -6.968 24.777 30.039 1.00 22.41 O
ANISOU 974 O LEU B 23 2877 3031 2608 -423 -350 270 O
ATOM 975 CB LEU B 23 -5.283 24.238 27.545 1.00 21.98 C
ANISOU 975 CB LEU B 23 2933 3040 2378 -813 -218 225 C
ATOM 976 CG LEU B 23 -6.181 23.866 26.380 1.00 25.65 C
ANISOU 976 CG LEU B 23 3449 3561 2736 -967 -244 269 C
ATOM 977 CD1 LEU B 23 -5.928 24.798 25.193 1.00 28.42 C
ANISOU 977 CD1 LEU B 23 3940 3940 2917 -1240 -338 351 C
ATOM 978 CD2 LEU B 23 -5.917 22.393 26.002 1.00 25.42 C
ANISOU 978 CD2 LEU B 23 3351 3594 2713 -1023 -74 122 C
ATOM 979 N LEU B 24 -7.593 26.561 28.810 1.00 22.31 N
ANISOU 979 N LEU B 24 2973 2900 2602 -482 -625 378 N
ATOM 980 CA LEU B 24 -8.962 26.546 29.347 1.00 22.15 C
ANISOU 980 CA LEU B 24 2822 2909 2685 -328 -689 316 C
ATOM 981 C LEU B 24 -9.773 25.437 28.671 1.00 23.12 C
ANISOU 981 C LEU B 24 2908 3140 2735 -415 -635 332 C
ATOM 982 O LEU B 24 -10.098 25.514 27.475 1.00 24.42 O
ANISOU 982 O LEU B 24 3149 3286 2842 -540 -749 423 O
ATOM 983 CB LEU B 24 -9.644 27.893 29.207 1.00 23.27 C
ANISOU 983 CB LEU B 24 2957 2906 2976 -221 -957 318 C
ATOM 984 CG LEU B 24 -8.929 29.142 29.749 1.00 23.83 C
ANISOU 984 CG LEU B 24 3095 2820 3139 -150 -1062 301 C
ATOM 985 CD1 LEU B 24 -9.752 30.348 29.370 1.00 25.93 C
ANISOU 985 CD1 LEU B 24 3373 2874 3606 -41 -1409 308 C
ATOM 986 CD2 LEU B 24 -8.743 29.081 31.233 1.00 25.70 C
ANISOU 986 CD2 LEU B 24 3199 3143 3422 -17 -896 133 C
ATOM 987 N ASP B 25 -10.132 24.426 29.451 1.00 21.74 N
ANISOU 987 N ASP B 25 2641 3080 2540 -389 -485 257 N
ATOM 988 CA ASP B 25 -10.586 23.166 28.895 1.00 20.99 C
ANISOU 988 CA ASP B 25 2550 3068 2357 -508 -400 272 C
ATOM 989 C ASP B 25 -11.953 22.729 29.447 1.00 21.56 C
ANISOU 989 C ASP B 25 2479 3281 2432 -489 -383 194 C
ATOM 990 O ASP B 25 -12.039 22.027 30.455 1.00 20.64 O
ANISOU 990 O ASP B 25 2331 3246 2264 -522 -271 146 O
ATOM 991 CB ASP B 25 -9.516 22.082 29.122 1.00 21.36 C
ANISOU 991 CB ASP B 25 2666 3086 2364 -571 -255 266 C
ATOM 992 CG ASP B 25 -9.839 20.774 28.419 1.00 21.27 C
ANISOU 992 CG ASP B 25 2685 3105 2293 -698 -185 259 C
ATOM 993 OD1 ASP B 25 -10.961 20.643 27.874 1.00 23.24 O
ANISOU 993 OD1 ASP B 25 2901 3437 2492 -760 -223 274 O
ATOM 994 OD2 ASP B 25 -8.952 19.885 28.389 1.00 22.46 O
ANISOU 994 OD2 ASP B 25 2880 3182 2473 -729 -113 215 O
ATOM 995 N THR B 26 -13.013 23.141 28.757 1.00 21.52 N
ANISOU 995 N THR B 26 2390 3313 2473 -473 -518 182 N
ATOM 996 CA THR B 26 -14.369 22.814 29.165 1.00 22.41 C
ANISOU 996 CA THR B 26 2310 3604 2602 -467 -504 56 C
ATOM 997 C THR B 26 -14.683 21.308 29.132 1.00 22.07 C
ANISOU 997 C THR B 26 2307 3682 2398 -659 -348 78 C
ATOM 998 O THR B 26 -15.640 20.865 29.789 1.00 22.60 O
ANISOU 998 O THR B 26 2231 3940 2417 -727 -276 -37 O
ATOM 999 CB THR B 26 -15.407 23.584 28.332 1.00 24.09 C
ANISOU 999 CB THR B 26 2399 3804 2949 -387 -744 30 C
ATOM 1000 OG1 THR B 26 -15.335 23.164 26.956 1.00 22.17 O
ANISOU 1000 OG1 THR B 26 2311 3512 2601 -544 -820 200 O
ATOM 1001 CG2 THR B 26 -15.154 25.089 28.422 1.00 23.92 C
ANISOU 1001 CG2 THR B 26 2362 3597 3129 -194 -966 7 C
ATOM 1002 N GLY B 27 -13.865 20.538 28.405 1.00 20.04 N
ANISOU 1002 N GLY B 27 2233 3319 2062 -768 -296 192 N
ATOM 1003 CA GLY B 27 -13.981 19.070 28.366 1.00 21.21 C
ANISOU 1003 CA GLY B 27 2460 3498 2101 -937 -183 208 C
ATOM 1004 C GLY B 27 -13.302 18.320 29.514 1.00 21.61 C
ANISOU 1004 C GLY B 27 2600 3486 2125 -972 -105 221 C
ATOM 1005 O GLY B 27 -13.394 17.104 29.598 1.00 22.05 O
ANISOU 1005 O GLY B 27 2751 3510 2117 -1116 -71 250 O
ATOM 1006 N ALA B 28 -12.614 19.050 30.386 1.00 20.93 N
ANISOU 1006 N ALA B 28 2502 3356 2092 -857 -115 213 N
ATOM 1007 CA ALA B 28 -11.930 18.459 31.523 1.00 21.02 C
ANISOU 1007 CA ALA B 28 2613 3300 2074 -905 -102 255 C
ATOM 1008 C ALA B 28 -12.728 18.734 32.820 1.00 22.72 C
ANISOU 1008 C ALA B 28 2736 3723 2174 -997 -63 190 C
ATOM 1009 O ALA B 28 -12.964 19.898 33.177 1.00 22.55 O
ANISOU 1009 O ALA B 28 2566 3801 2199 -881 -53 78 O
ATOM 1010 CB ALA B 28 -10.531 19.065 31.629 1.00 20.44 C
ANISOU 1010 CB ALA B 28 2583 3070 2113 -757 -135 274 C
ATOM 1011 N ASP B 29 -13.131 17.675 33.517 1.00 24.59 N
ANISOU 1011 N ASP B 29 3064 4025 2255 -1236 -48 239 N
ATOM 1012 CA ASP B 29 -13.776 17.802 34.839 1.00 26.74 C
ANISOU 1012 CA ASP B 29 3273 4546 2340 -1436 15 162 C
ATOM 1013 C ASP B 29 -12.828 18.466 35.846 1.00 27.70 C
ANISOU 1013 C ASP B 29 3435 4619 2469 -1375 -13 175 C
ATOM 1014 O ASP B 29 -13.251 19.325 36.648 1.00 28.58 O
ANISOU 1014 O ASP B 29 3389 4955 2516 -1401 72 4 O
ATOM 1015 CB ASP B 29 -14.157 16.417 35.379 1.00 28.08 C
ANISOU 1015 CB ASP B 29 3629 4748 2293 -1793 -11 281 C
ATOM 1016 CG ASP B 29 -15.239 15.737 34.564 1.00 32.03 C
ANISOU 1016 CG ASP B 29 4081 5354 2737 -1922 37 245 C
ATOM 1017 OD1 ASP B 29 -15.896 16.389 33.699 1.00 31.86 O
ANISOU 1017 OD1 ASP B 29 3838 5446 2820 -1756 95 105 O
ATOM 1018 OD2 ASP B 29 -15.439 14.526 34.795 1.00 32.79 O
ANISOU 1018 OD2 ASP B 29 4377 5400 2681 -2211 -19 373 O
ATOM 1019 N AASP B 30 -11.552 18.069 35.757 0.50 26.40 N
ANISOU 1019 N AASP B 30 3454 4169 2407 -1287 -135 338 N
ATOM 1020 N BASP B 30 -11.561 18.061 35.849 0.50 26.54 N
ANISOU 1020 N BASP B 30 3476 4196 2413 -1302 -136 340 N
ATOM 1021 CA AASP B 30 -10.502 18.436 36.710 0.50 27.30 C
ANISOU 1021 CA AASP B 30 3647 4201 2526 -1261 -210 398 C
ATOM 1022 CA BASP B 30 -10.627 18.580 36.849 0.50 27.58 C
ANISOU 1022 CA BASP B 30 3659 4284 2537 -1277 -191 374 C
ATOM 1023 C AASP B 30 -9.386 19.277 36.080 0.50 24.85 C
ANISOU 1023 C AASP B 30 3286 3713 2441 -960 -237 376 C
ATOM 1024 C BASP B 30 -9.318 19.078 36.237 0.50 25.21 C
ANISOU 1024 C BASP B 30 3365 3744 2470 -995 -258 402 C
ATOM 1025 O AASP B 30 -9.152 19.266 34.852 0.50 23.77 O
ANISOU 1025 O AASP B 30 3122 3460 2450 -814 -229 361 O
ATOM 1026 O BASP B 30 -8.903 18.647 35.164 0.50 25.26 O
ANISOU 1026 O BASP B 30 3394 3580 2623 -881 -287 426 O
ATOM 1027 CB AASP B 30 -9.863 17.180 37.337 0.50 28.41 C
ANISOU 1027 CB AASP B 30 4042 4143 2611 -1449 -401 608 C
ATOM 1028 CB BASP B 30 -10.362 17.551 37.960 0.50 28.92 C
ANISOU 1028 CB BASP B 30 4056 4406 2524 -1577 -328 550 C
ATOM 1029 CG AASP B 30 -10.872 16.109 37.687 0.50 29.85 C
ANISOU 1029 CG AASP B 30 4348 4430 2563 -1803 -420 684 C
ATOM 1030 CG BASP B 30 -11.621 17.169 38.735 0.50 32.22 C
ANISOU 1030 CG BASP B 30 4478 5141 2625 -1966 -235 504 C
ATOM 1031 OD1AASP B 30 -12.013 16.454 38.062 0.50 31.51 O
ANISOU 1031 OD1AASP B 30 4430 4981 2562 -1996 -253 549 O
ATOM 1032 OD1BASP B 30 -12.334 18.062 39.260 0.50 32.12 O
ANISOU 1032 OD1BASP B 30 4259 5452 2491 -2031 -58 282 O
ATOM 1033 OD2AASP B 30 -10.520 14.909 37.589 0.50 31.31 O
ANISOU 1033 OD2AASP B 30 4751 4353 2793 -1899 -615 855 O
ATOM 1034 OD2BASP B 30 -11.880 15.953 38.847 0.50 36.31 O
ANISOU 1034 OD2BASP B 30 5199 5582 3015 -2234 -348 666 O
ATOM 1035 N THR B 31 -8.697 20.019 36.933 1.00 25.11 N
ANISOU 1035 N THR B 31 3315 3757 2468 -921 -259 364 N
ATOM 1036 CA THR B 31 -7.468 20.662 36.516 1.00 23.21 C
ANISOU 1036 CA THR B 31 3060 3352 2407 -707 -303 364 C
ATOM 1037 C THR B 31 -6.281 19.718 36.640 1.00 24.32 C
ANISOU 1037 C THR B 31 3322 3265 2654 -696 -463 484 C
ATOM 1038 O THR B 31 -6.109 19.047 37.666 1.00 25.44 O
ANISOU 1038 O THR B 31 3593 3366 2709 -853 -601 604 O
ATOM 1039 CB THR B 31 -7.296 21.895 37.352 1.00 24.30 C
ANISOU 1039 CB THR B 31 3128 3599 2505 -673 -265 276 C
ATOM 1040 OG1 THR B 31 -8.361 22.793 37.005 1.00 22.55 O
ANISOU 1040 OG1 THR B 31 2755 3520 2294 -609 -165 113 O
ATOM 1041 CG2 THR B 31 -5.872 22.554 37.170 1.00 19.59 C
ANISOU 1041 CG2 THR B 31 2540 2849 2054 -514 -324 293 C
ATOM 1042 N VAL B 32 -5.484 19.628 35.583 1.00 22.94 N
ANISOU 1042 N VAL B 32 3101 2944 2671 -538 -468 434 N
ATOM 1043 CA VAL B 32 -4.316 18.729 35.593 1.00 24.30 C
ANISOU 1043 CA VAL B 32 3312 2887 3033 -474 -632 457 C
ATOM 1044 C VAL B 32 -3.130 19.484 35.054 1.00 23.09 C
ANISOU 1044 C VAL B 32 3030 2712 3033 -318 -588 331 C
ATOM 1045 O VAL B 32 -3.157 19.937 33.915 1.00 21.99 O
ANISOU 1045 O VAL B 32 2810 2637 2910 -284 -446 220 O
ATOM 1046 CB VAL B 32 -4.469 17.483 34.645 1.00 25.22 C
ANISOU 1046 CB VAL B 32 3453 2852 3279 -470 -664 415 C
ATOM 1047 CG1 VAL B 32 -3.521 16.371 35.082 1.00 25.23 C
ANISOU 1047 CG1 VAL B 32 3516 2565 3505 -418 -929 445 C
ATOM 1048 CG2 VAL B 32 -5.876 17.000 34.609 1.00 26.53 C
ANISOU 1048 CG2 VAL B 32 3705 3115 3261 -642 -610 488 C
ATOM 1049 N LEU B 33 -2.077 19.564 35.862 1.00 25.92 N
ANISOU 1049 N LEU B 33 2841 3148 3861 -375 -604 398 N
ATOM 1050 CA LEU B 33 -0.852 20.213 35.460 1.00 26.36 C
ANISOU 1050 CA LEU B 33 2505 3156 4356 -261 -644 258 C
ATOM 1051 C LEU B 33 0.287 19.232 35.252 1.00 29.17 C
ANISOU 1051 C LEU B 33 2734 3345 5003 -79 -872 140 C
ATOM 1052 O LEU B 33 0.356 18.199 35.921 1.00 29.11 O
ANISOU 1052 O LEU B 33 3030 3203 4825 27 -1209 173 O
ATOM 1053 CB LEU B 33 -0.433 21.247 36.528 1.00 27.50 C
ANISOU 1053 CB LEU B 33 2577 3276 4596 -257 -858 122 C
ATOM 1054 CG LEU B 33 -1.441 22.360 36.860 1.00 26.84 C
ANISOU 1054 CG LEU B 33 2562 3319 4316 -419 -646 169 C
ATOM 1055 CD1 LEU B 33 -0.828 23.407 37.771 1.00 27.78 C
ANISOU 1055 CD1 LEU B 33 2551 3392 4612 -409 -841 -22 C
ATOM 1056 CD2 LEU B 33 -1.972 23.045 35.586 1.00 25.53 C
ANISOU 1056 CD2 LEU B 33 2214 3235 4250 -478 -242 253 C
ATOM 1057 N GLU B 34 1.211 19.582 34.358 1.00 30.40 N
ANISOU 1057 N GLU B 34 2469 3457 5624 -44 -665 -28 N
ATOM 1058 CA GLU B 34 2.413 18.788 34.187 1.00 35.51 C
ANISOU 1058 CA GLU B 34 2849 3923 6718 137 -863 -266 C
ATOM 1059 C GLU B 34 3.244 18.819 35.460 1.00 39.53 C
ANISOU 1059 C GLU B 34 3280 4284 7456 336 -1479 -489 C
ATOM 1060 O GLU B 34 2.985 19.616 36.382 1.00 39.60 O
ANISOU 1060 O GLU B 34 3420 4347 7281 293 -1665 -474 O
ATOM 1061 CB GLU B 34 3.237 19.282 33.004 1.00 36.98 C
ANISOU 1061 CB GLU B 34 2584 4062 7405 63 -377 -480 C
ATOM 1062 CG GLU B 34 2.460 19.334 31.694 1.00 37.75 C
ANISOU 1062 CG GLU B 34 2894 4269 7179 -94 174 -264 C
ATOM 1063 CD GLU B 34 3.317 19.819 30.523 1.00 44.82 C
ANISOU 1063 CD GLU B 34 3517 5045 8467 -206 754 -465 C
ATOM 1064 OE1 GLU B 34 4.407 19.247 30.292 1.00 49.96 O
ANISOU 1064 OE1 GLU B 34 3803 5536 9644 -139 803 -792 O
ATOM 1065 OE2 GLU B 34 2.890 20.772 29.834 1.00 47.28 O
ANISOU 1065 OE2 GLU B 34 4019 5382 8565 -360 1181 -315 O
ATOM 1066 N GLU B 35 4.241 17.945 35.514 1.00 44.14 N
ANISOU 1066 N GLU B 35 3663 4662 8446 585 -1845 -736 N
ATOM 1067 CA GLU B 35 5.083 17.815 36.693 1.00 49.50 C
ANISOU 1067 CA GLU B 35 4310 5147 9350 877 -2607 -997 C
ATOM 1068 C GLU B 35 5.565 19.159 37.234 1.00 50.78 C
ANISOU 1068 C GLU B 35 4114 5356 9824 824 -2696 -1268 C
ATOM 1069 O GLU B 35 6.097 20.001 36.510 1.00 50.65 O
ANISOU 1069 O GLU B 35 3517 5369 10360 665 -2233 -1516 O
ATOM 1070 CB GLU B 35 6.266 16.875 36.431 1.00 54.25 C
ANISOU 1070 CB GLU B 35 4521 5492 10600 1190 -2966 -1366 C
ATOM 1071 CG GLU B 35 6.889 16.294 37.716 1.00 62.26 C
ANISOU 1071 CG GLU B 35 5786 6232 11638 1617 -3984 -1542 C
ATOM 1072 CD GLU B 35 5.856 15.580 38.596 1.00 63.85 C
ANISOU 1072 CD GLU B 35 7018 6363 10880 1648 -4278 -1051 C
ATOM 1073 OE1 GLU B 35 5.087 14.734 38.070 1.00 63.06 O
ANISOU 1073 OE1 GLU B 35 7287 6265 10409 1519 -3915 -723 O
ATOM 1074 OE2 GLU B 35 5.805 15.874 39.811 1.00 66.96 O
ANISOU 1074 OE2 GLU B 35 7879 6675 10887 1772 -4826 -1024 O
ATOM 1075 N MET B 36 5.333 19.335 38.523 1.00 52.55 N
ANISOU 1075 N MET B 36 4773 5552 9642 933 -3248 -1216 N
ATOM 1076 CA MET B 36 5.809 20.490 39.264 1.00 55.69 C
ANISOU 1076 CA MET B 36 4906 5961 10291 936 -3500 -1521 C
ATOM 1077 C MET B 36 5.790 20.142 40.744 1.00 59.74 C
ANISOU 1077 C MET B 36 6059 6338 10300 1200 -4346 -1514 C
ATOM 1078 O MET B 36 5.102 19.202 41.159 1.00 60.07 O
ANISOU 1078 O MET B 36 6870 6302 9652 1258 -4506 -1155 O
ATOM 1079 CB MET B 36 4.931 21.721 38.981 1.00 50.70 C
ANISOU 1079 CB MET B 36 4279 5559 9426 564 -2831 -1317 C
ATOM 1080 CG MET B 36 3.476 21.601 39.410 1.00 47.01 C
ANISOU 1080 CG MET B 36 4541 5236 8085 401 -2660 -860 C
ATOM 1081 SD MET B 36 2.600 23.171 39.271 1.00 44.00 S
ANISOU 1081 SD MET B 36 4068 5057 7594 73 -2074 -766 S
ATOM 1082 CE MET B 36 3.607 24.206 40.353 1.00 47.97 C
ANISOU 1082 CE MET B 36 4274 5461 8493 173 -2572 -1233 C
ATOM 1083 N ASN B 37 6.556 20.888 41.529 1.00 64.66 N
ANISOU 1083 N ASN B 37 6419 6894 11255 1350 -4872 -1934 N
ATOM 1084 CA ASN B 37 6.490 20.794 42.975 1.00 69.26 C
ANISOU 1084 CA ASN B 37 7720 7352 11243 1581 -5665 -1943 C
ATOM 1085 C ASN B 37 5.344 21.635 43.493 1.00 65.78 C
ANISOU 1085 C ASN B 37 7780 7114 10100 1237 -5226 -1651 C
ATOM 1086 O ASN B 37 5.394 22.869 43.439 1.00 64.91 O
ANISOU 1086 O ASN B 37 7206 7147 10311 1037 -4934 -1860 O
ATOM 1087 CB ASN B 37 7.788 21.302 43.616 1.00 76.08 C
ANISOU 1087 CB ASN B 37 8059 8061 12786 1907 -6489 -2608 C
ATOM 1088 CG ASN B 37 8.852 20.225 43.751 1.00 83.86 C
ANISOU 1088 CG ASN B 37 8910 8732 14220 2432 -7381 -2941 C
ATOM 1089 OD1 ASN B 37 8.729 19.127 43.191 1.00 84.22 O
ANISOU 1089 OD1 ASN B 37 9132 8673 14195 2525 -7275 -2689 O
ATOM 1090 ND2 ASN B 37 9.921 20.539 44.504 1.00 91.77 N
ANISOU 1090 ND2 ASN B 37 9566 9557 15746 2809 -8326 -3570 N
ATOM 1091 N LEU B 38 4.302 20.971 43.975 1.00 64.84 N
ANISOU 1091 N LEU B 38 8588 6971 9078 1146 -5118 -1206 N
ATOM 1092 CA LEU B 38 3.322 21.644 44.798 1.00 64.21 C
ANISOU 1092 CA LEU B 38 9087 7001 8308 884 -4863 -1048 C
ATOM 1093 C LEU B 38 3.627 21.276 46.238 1.00 71.50 C
ANISOU 1093 C LEU B 38 10901 7665 8601 1168 -5709 -1130 C
ATOM 1094 O LEU B 38 3.844 20.098 46.556 1.00 75.20 O
ANISOU 1094 O LEU B 38 12001 7852 8720 1442 -6202 -981 O
ATOM 1095 CB LEU B 38 1.893 21.280 44.406 1.00 59.32 C
ANISOU 1095 CB LEU B 38 8876 6505 7158 524 -4063 -600 C
ATOM 1096 CG LEU B 38 1.362 22.051 43.200 1.00 53.15 C
ANISOU 1096 CG LEU B 38 7366 5998 6829 234 -3276 -548 C
ATOM 1097 CD1 LEU B 38 -0.091 21.690 42.957 1.00 49.86 C
ANISOU 1097 CD1 LEU B 38 7337 5683 5923 -72 -2632 -216 C
ATOM 1098 CD2 LEU B 38 1.516 23.561 43.393 1.00 51.58 C
ANISOU 1098 CD2 LEU B 38 6721 5929 6947 122 -3164 -814 C
ATOM 1099 N PRO B 39 3.692 22.288 47.113 1.00 74.29 N
ANISOU 1099 N PRO B 39 11363 8070 8794 1134 -5927 -1385 N
ATOM 1100 CA PRO B 39 4.023 21.939 48.484 1.00 81.86 C
ANISOU 1100 CA PRO B 39 13288 8753 9062 1442 -6806 -1482 C
ATOM 1101 C PRO B 39 2.799 21.333 49.170 1.00 82.36 C
ANISOU 1101 C PRO B 39 14618 8698 7976 1188 -6389 -1017 C
ATOM 1102 O PRO B 39 1.662 21.646 48.783 1.00 77.13 O
ANISOU 1102 O PRO B 39 13889 8249 7165 726 -5419 -787 O
ATOM 1103 CB PRO B 39 4.432 23.282 49.110 1.00 83.98 C
ANISOU 1103 CB PRO B 39 13212 9136 9559 1435 -7078 -1950 C
ATOM 1104 CG PRO B 39 3.842 24.350 48.251 1.00 76.69 C
ANISOU 1104 CG PRO B 39 11462 8537 9140 992 -6093 -1932 C
ATOM 1105 CD PRO B 39 3.464 23.737 46.920 1.00 71.55 C
ANISOU 1105 CD PRO B 39 10379 7982 8826 840 -5425 -1592 C
ATOM 1106 N GLY B 40 3.038 20.444 50.135 1.00 89.14 N
ANISOU 1106 N GLY B 40 16622 9173 8073 1495 -7105 -909 N
ATOM 1107 CA GLY B 40 1.966 19.898 50.970 1.00 91.35 C
ANISOU 1107 CA GLY B 40 18293 9239 7179 1224 -6689 -520 C
ATOM 1108 C GLY B 40 1.550 18.460 50.716 1.00 91.45 C
ANISOU 1108 C GLY B 40 19013 8945 6790 1209 -6477 -73 C
ATOM 1109 O GLY B 40 2.263 17.701 50.042 1.00 91.49 O
ANISOU 1109 O GLY B 40 18599 8830 7332 1549 -6919 -60 O
ATOM 1110 N ARG B 41 0.383 18.103 51.273 1.00 91.96 N
ANISOU 1110 N ARG B 41 20140 8853 5948 783 -5736 243 N
ATOM 1111 CA ARG B 41 -0.161 16.747 51.213 1.00 92.96 C
ANISOU 1111 CA ARG B 41 21148 8605 5567 669 -5402 663 C
ATOM 1112 C ARG B 41 -0.847 16.481 49.877 1.00 84.02 C
ANISOU 1112 C ARG B 41 19045 7754 5126 327 -4509 786 C
ATOM 1113 O ARG B 41 -1.584 17.347 49.345 1.00 77.80 O
ANISOU 1113 O ARG B 41 17438 7386 4735 -68 -3733 664 O
ATOM 1114 CB ARG B 41 -1.189 16.525 52.334 1.00 98.48 C
ANISOU 1114 CB ARG B 41 23357 8990 5071 249 -4786 879 C
ATOM 1115 CG ARG B 41 -0.634 16.555 53.750 1.00108.48 C
ANISOU 1115 CG ARG B 41 26015 9853 5349 578 -5646 839 C
ATOM 1116 CD ARG B 41 -0.090 15.188 54.161 1.00116.61 C
ANISOU 1116 CD ARG B 41 28311 10229 5765 1018 -6418 1157 C
ATOM 1117 NE ARG B 41 0.731 15.253 55.374 1.00127.62 N
ANISOU 1117 NE ARG B 41 30891 11240 6360 1545 -7617 1051 N
ATOM 1118 CZ ARG B 41 1.970 15.751 55.422 1.00129.22 C
ANISOU 1118 CZ ARG B 41 30413 11562 7125 2179 -8889 646 C
ATOM 1119 NH1 ARG B 41 2.551 16.256 54.322 1.00121.20 N
ANISOU 1119 NH1 ARG B 41 27549 11025 7475 2310 -9009 323 N
ATOM 1120 NH2 ARG B 41 2.630 15.751 56.578 1.00138.71 N
ANISOU 1120 NH2 ARG B 41 32817 12371 7517 2674 -10034 524 N
ATOM 1121 N TRP B 42 -0.614 15.270 49.357 1.00 83.37 N
ANISOU 1121 N TRP B 42 19113 7402 5163 510 -4675 1009 N
ATOM 1122 CA TRP B 42 -1.295 14.812 48.155 1.00 75.93 C
ANISOU 1122 CA TRP B 42 17465 6646 4739 203 -3887 1130 C
ATOM 1123 C TRP B 42 -1.806 13.389 48.313 1.00 79.54 C
ANISOU 1123 C TRP B 42 18952 6612 4656 75 -3608 1474 C
ATOM 1124 O TRP B 42 -1.443 12.692 49.262 1.00 86.37 O
ANISOU 1124 O TRP B 42 21079 6947 4792 318 -4147 1656 O
ATOM 1125 CB TRP B 42 -0.383 14.929 46.931 1.00 70.96 C
ANISOU 1125 CB TRP B 42 15522 6289 5149 531 -4264 943 C
ATOM 1126 CG TRP B 42 0.927 14.252 47.105 1.00 75.18 C
ANISOU 1126 CG TRP B 42 16224 6486 5856 1147 -5338 872 C
ATOM 1127 CD1 TRP B 42 2.044 14.779 47.680 1.00 78.66 C
ANISOU 1127 CD1 TRP B 42 16546 6876 6466 1607 -6301 567 C
ATOM 1128 CD2 TRP B 42 1.272 12.926 46.692 1.00 76.83 C
ANISOU 1128 CD2 TRP B 42 16679 6336 6177 1404 -5612 1036 C
ATOM 1129 NE1 TRP B 42 3.067 13.865 47.658 1.00 84.48 N
ANISOU 1129 NE1 TRP B 42 17408 7240 7450 2164 -7203 501 N
ATOM 1130 CE2 TRP B 42 2.622 12.713 47.060 1.00 83.45 C
ANISOU 1130 CE2 TRP B 42 17529 6905 7273 2056 -6792 807 C
ATOM 1131 CE3 TRP B 42 0.571 11.890 46.058 1.00 74.95 C
ANISOU 1131 CE3 TRP B 42 16633 5953 5891 1156 -5001 1304 C
ATOM 1132 CZ2 TRP B 42 3.293 11.503 46.811 1.00 86.65 C
ANISOU 1132 CZ2 TRP B 42 18137 6888 7899 2494 -7384 853 C
ATOM 1133 CZ3 TRP B 42 1.240 10.684 45.806 1.00 78.94 C
ANISOU 1133 CZ3 TRP B 42 17376 6044 6574 1557 -5543 1379 C
ATOM 1134 CH2 TRP B 42 2.589 10.506 46.183 1.00 84.27 C
ANISOU 1134 CH2 TRP B 42 18064 6444 7512 2231 -6726 1161 C
ATOM 1135 N LYS B 43 -2.669 12.972 47.390 1.00 74.38 N
ANISOU 1135 N LYS B 43 17814 6099 4346 -306 -2777 1545 N
ATOM 1136 CA LYS B 43 -3.207 11.609 47.370 1.00 77.67 C
ANISOU 1136 CA LYS B 43 19040 6056 4415 -492 -2391 1819 C
ATOM 1137 C LYS B 43 -3.071 11.030 45.960 1.00 72.35 C
ANISOU 1137 C LYS B 43 17376 5556 4558 -407 -2309 1789 C
ATOM 1138 O LYS B 43 -3.267 11.757 44.978 1.00 65.52 O
ANISOU 1138 O LYS B 43 15314 5215 4364 -515 -2011 1582 O
ATOM 1139 CB LYS B 43 -4.689 11.603 47.775 1.00 78.73 C
ANISOU 1139 CB LYS B 43 19699 6124 4090 -1197 -1235 1846 C
ATOM 1140 CG LYS B 43 -4.995 12.092 49.195 1.00 85.65 C
ANISOU 1140 CG LYS B 43 21714 6775 4055 -1399 -1084 1861 C
ATOM 1141 CD LYS B 43 -4.760 10.983 50.241 1.00 95.45 C
ANISOU 1141 CD LYS B 43 24738 7235 4292 -1290 -1357 2205 C
ATOM 1142 CE LYS B 43 -5.021 11.496 51.657 1.00104.19 C
ANISOU 1142 CE LYS B 43 27113 8097 4377 -1482 -1212 2211 C
ATOM 1143 NZ LYS B 43 -4.150 12.739 52.022 1.00102.82 N
ANISOU 1143 NZ LYS B 43 26459 8307 4299 -1050 -2100 1964 N
ATOM 1144 N PRO B 44 -2.743 9.725 45.850 1.00 76.21 N
ANISOU 1144 N PRO B 44 18430 5569 4956 -203 -2574 1990 N
ATOM 1145 CA PRO B 44 -2.658 9.086 44.535 1.00 71.99 C
ANISOU 1145 CA PRO B 44 17049 5160 5143 -150 -2443 1936 C
ATOM 1146 C PRO B 44 -4.039 8.998 43.912 1.00 68.69 C
ANISOU 1146 C PRO B 44 16292 4951 4857 -764 -1369 1884 C
ATOM 1147 O PRO B 44 -5.026 8.769 44.619 1.00 71.64 O
ANISOU 1147 O PRO B 44 17460 5072 4689 -1225 -711 1969 O
ATOM 1148 CB PRO B 44 -2.139 7.668 44.853 1.00 78.67 C
ANISOU 1148 CB PRO B 44 18866 5321 5705 164 -2924 2176 C
ATOM 1149 CG PRO B 44 -1.652 7.720 46.254 1.00 85.93 C
ANISOU 1149 CG PRO B 44 21012 5802 5834 443 -3582 2332 C
ATOM 1150 CD PRO B 44 -2.453 8.771 46.937 1.00 85.02 C
ANISOU 1150 CD PRO B 44 21087 5961 5258 -3 -3009 2278 C
ATOM 1151 N LYS B 45 -4.101 9.191 42.596 1.00 63.27 N
ANISOU 1151 N LYS B 45 14445 4697 4899 -771 -1192 1696 N
ATOM 1152 CA LYS B 45 -5.358 9.196 41.870 1.00 60.80 C
ANISOU 1152 CA LYS B 45 13641 4630 4828 -1261 -342 1550 C
ATOM 1153 C LYS B 45 -5.077 8.830 40.417 1.00 56.50 C
ANISOU 1153 C LYS B 45 12205 4318 4944 -1092 -420 1426 C
ATOM 1154 O LYS B 45 -3.960 9.016 39.924 1.00 54.49 O
ANISOU 1154 O LYS B 45 11476 4188 5039 -662 -997 1391 O
ATOM 1155 CB LYS B 45 -5.979 10.595 41.933 1.00 58.01 C
ANISOU 1155 CB LYS B 45 12723 4756 4564 -1492 -8 1349 C
ATOM 1156 CG LYS B 45 -7.490 10.606 41.970 1.00 60.76 C
ANISOU 1156 CG LYS B 45 13057 5145 4883 -2069 890 1173 C
ATOM 1157 CD LYS B 45 -8.017 11.885 41.353 1.00 59.44 C
ANISOU 1157 CD LYS B 45 11893 5533 5160 -2147 1080 895 C
ATOM 1158 CE LYS B 45 -9.511 11.784 41.065 1.00 62.79 C
ANISOU 1158 CE LYS B 45 12017 6022 5816 -2638 1868 589 C
ATOM 1159 NZ LYS B 45 -9.962 12.937 40.218 1.00 59.46 N
ANISOU 1159 NZ LYS B 45 10572 6109 5910 -2583 1876 312 N
ATOM 1160 N MET B 46 -6.084 8.299 39.736 1.00 55.76 N
ANISOU 1160 N MET B 46 11887 4259 5041 -1445 182 1305 N
ATOM 1161 CA MET B 46 -5.970 8.016 38.309 1.00 52.23 C
ANISOU 1161 CA MET B 46 10637 4062 5147 -1328 163 1144 C
ATOM 1162 C MET B 46 -7.092 8.686 37.530 1.00 48.56 C
ANISOU 1162 C MET B 46 9448 4036 4965 -1632 656 867 C
ATOM 1163 O MET B 46 -8.246 8.689 37.974 1.00 50.46 O
ANISOU 1163 O MET B 46 9866 4218 5090 -2054 1203 739 O
ATOM 1164 CB MET B 46 -5.904 6.514 38.050 1.00 56.02 C
ANISOU 1164 CB MET B 46 11531 4095 5661 -1324 200 1211 C
ATOM 1165 CG MET B 46 -4.570 5.910 38.465 1.00 60.44 C
ANISOU 1165 CG MET B 46 12567 4263 6136 -842 -501 1416 C
ATOM 1166 SD MET B 46 -4.263 4.297 37.764 1.00 69.14 S
ANISOU 1166 SD MET B 46 13838 4926 7506 -704 -570 1417 S
ATOM 1167 CE MET B 46 -4.452 3.260 39.222 1.00 74.85 C
ANISOU 1167 CE MET B 46 16079 4814 7545 -806 -560 1761 C
ATOM 1168 N ILE B 47 -6.739 9.293 36.395 1.00 43.43 N
ANISOU 1168 N ILE B 47 8017 3792 4694 -1408 459 743 N
ATOM 1169 CA ILE B 47 -7.713 9.960 35.552 1.00 40.84 C
ANISOU 1169 CA ILE B 47 7051 3849 4616 -1577 751 481 C
ATOM 1170 C ILE B 47 -7.594 9.458 34.123 1.00 39.48 C
ANISOU 1170 C ILE B 47 6440 3809 4750 -1436 679 343 C
ATOM 1171 O ILE B 47 -6.503 9.143 33.648 1.00 38.46 O
ANISOU 1171 O ILE B 47 6264 3631 4716 -1141 377 439 O
ATOM 1172 CB ILE B 47 -7.582 11.510 35.572 1.00 38.31 C
ANISOU 1172 CB ILE B 47 6325 3893 4340 -1460 619 460 C
ATOM 1173 CG1 ILE B 47 -6.165 11.944 35.168 1.00 36.26 C
ANISOU 1173 CG1 ILE B 47 5853 3724 4201 -1070 174 590 C
ATOM 1174 CG2 ILE B 47 -7.993 12.063 36.951 1.00 41.00 C
ANISOU 1174 CG2 ILE B 47 7063 4137 4378 -1675 795 499 C
ATOM 1175 CD1 ILE B 47 -6.075 13.350 34.726 1.00 33.72 C
ANISOU 1175 CD1 ILE B 47 5054 3735 4023 -973 129 530 C
ATOM 1176 N GLY B 48 -8.724 9.391 33.437 1.00 39.72 N
ANISOU 1176 N GLY B 48 6136 3995 4961 -1642 949 57 N
ATOM 1177 CA GLY B 48 -8.735 8.836 32.101 1.00 39.90 C
ANISOU 1177 CA GLY B 48 5845 4118 5197 -1529 876 -117 C
ATOM 1178 C GLY B 48 -9.072 9.849 31.037 1.00 38.45 C
ANISOU 1178 C GLY B 48 5148 4336 5124 -1381 746 -292 C
ATOM 1179 O GLY B 48 -9.907 10.747 31.231 1.00 38.76 O
ANISOU 1179 O GLY B 48 4962 4557 5209 -1474 811 -434 O
ATOM 1180 N GLY B 49 -8.444 9.691 29.885 1.00 37.33 N
ANISOU 1180 N GLY B 49 4874 4294 5016 -1142 570 -304 N
ATOM 1181 CA GLY B 49 -8.841 10.482 28.750 1.00 35.99 C
ANISOU 1181 CA GLY B 49 4404 4421 4847 -995 441 -469 C
ATOM 1182 C GLY B 49 -8.908 9.658 27.508 1.00 36.59 C
ANISOU 1182 C GLY B 49 4445 4508 4949 -917 388 -680 C
ATOM 1183 O GLY B 49 -9.142 8.454 27.558 1.00 38.03 O
ANISOU 1183 O GLY B 49 4710 4492 5248 -1067 503 -818 O
ATOM 1184 N ILE B 50 -8.683 10.325 26.381 1.00 35.58 N
ANISOU 1184 N ILE B 50 4270 4576 4674 -688 234 -705 N
ATOM 1185 CA ILE B 50 -8.599 9.662 25.106 1.00 36.94 C
ANISOU 1185 CA ILE B 50 4509 4766 4761 -579 178 -899 C
ATOM 1186 C ILE B 50 -7.258 8.904 25.143 1.00 36.91 C
ANISOU 1186 C ILE B 50 4649 4563 4813 -536 339 -738 C
ATOM 1187 O ILE B 50 -6.233 9.456 25.509 1.00 36.62 O
ANISOU 1187 O ILE B 50 4631 4492 4790 -446 393 -502 O
ATOM 1188 CB ILE B 50 -8.644 10.735 23.986 1.00 37.54 C
ANISOU 1188 CB ILE B 50 4679 5042 4542 -337 -3 -910 C
ATOM 1189 CG1 ILE B 50 -9.795 10.500 23.024 1.00 38.79 C
ANISOU 1189 CG1 ILE B 50 4806 5308 4624 -259 -293 -1300 C
ATOM 1190 CG2 ILE B 50 -7.319 10.870 23.273 1.00 38.35 C
ANISOU 1190 CG2 ILE B 50 5019 5095 4457 -202 177 -732 C
ATOM 1191 CD1 ILE B 50 -10.076 11.691 22.144 1.00 39.15 C
ANISOU 1191 CD1 ILE B 50 5054 5491 4330 20 -590 -1289 C
ATOM 1192 N GLY B 51 -7.243 7.636 24.795 1.00 38.89 N
ANISOU 1192 N GLY B 51 4954 4652 5172 -590 399 -917 N
ATOM 1193 CA GLY B 51 -5.960 6.904 24.851 1.00 39.32 C
ANISOU 1193 CA GLY B 51 5096 4476 5369 -503 507 -819 C
ATOM 1194 C GLY B 51 -5.688 6.160 26.158 1.00 38.97 C
ANISOU 1194 C GLY B 51 5166 4111 5530 -590 501 -659 C
ATOM 1195 O GLY B 51 -4.787 5.335 26.231 1.00 40.60 O
ANISOU 1195 O GLY B 51 5452 4054 5920 -483 494 -645 O
ATOM 1196 N GLY B 52 -6.469 6.452 27.189 1.00 37.67 N
ANISOU 1196 N GLY B 52 5064 3928 5320 -770 501 -558 N
ATOM 1197 CA GLY B 52 -6.383 5.711 28.431 1.00 38.56 C
ANISOU 1197 CA GLY B 52 5487 3677 5489 -886 527 -397 C
ATOM 1198 C GLY B 52 -6.192 6.576 29.647 1.00 36.80 C
ANISOU 1198 C GLY B 52 5396 3454 5134 -891 449 -132 C
ATOM 1199 O GLY B 52 -6.640 7.710 29.686 1.00 35.55 O
ANISOU 1199 O GLY B 52 5041 3583 4884 -930 462 -130 O
ATOM 1200 N PHE B 53 -5.454 6.050 30.612 1.00 38.00 N
ANISOU 1200 N PHE B 53 5912 3255 5271 -806 308 75 N
ATOM 1201 CA APHE B 53 -5.358 6.643 31.938 0.50 37.75 C
ANISOU 1201 CA APHE B 53 6175 3135 5035 -833 207 306 C
ATOM 1202 CA BPHE B 53 -5.371 6.667 31.922 0.50 37.65 C
ANISOU 1202 CA BPHE B 53 6151 3132 5023 -835 210 303 C
ATOM 1203 C PHE B 53 -3.955 7.123 32.298 1.00 37.31 C
ANISOU 1203 C PHE B 53 6074 3042 5063 -486 -186 440 C
ATOM 1204 O PHE B 53 -2.955 6.565 31.832 1.00 38.95 O
ANISOU 1204 O PHE B 53 6165 3102 5532 -227 -384 373 O
ATOM 1205 CB APHE B 53 -5.793 5.615 32.986 0.50 41.38 C
ANISOU 1205 CB APHE B 53 7297 3119 5307 -1036 328 429 C
ATOM 1206 CB BPHE B 53 -5.933 5.703 32.982 0.50 41.13 C
ANISOU 1206 CB BPHE B 53 7239 3123 5265 -1073 368 414 C
ATOM 1207 CG APHE B 53 -4.744 4.579 33.293 0.50 44.51 C
ANISOU 1207 CG APHE B 53 8102 3054 5756 -760 2 568 C
ATOM 1208 CG BPHE B 53 -7.450 5.579 32.967 0.50 41.84 C
ANISOU 1208 CG BPHE B 53 7302 3262 5335 -1514 852 210 C
ATOM 1209 CD1APHE B 53 -4.695 3.387 32.579 0.50 46.49 C
ANISOU 1209 CD1APHE B 53 8371 3067 6226 -739 72 438 C
ATOM 1210 CD1BPHE B 53 -8.223 6.190 33.962 0.50 42.42 C
ANISOU 1210 CD1BPHE B 53 7579 3339 5198 -1796 1114 238 C
ATOM 1211 CD2APHE B 53 -3.801 4.800 34.296 0.50 46.69 C
ANISOU 1211 CD2APHE B 53 8739 3111 5891 -482 -440 785 C
ATOM 1212 CD2BPHE B 53 -8.100 4.845 31.974 0.50 41.42 C
ANISOU 1212 CD2BPHE B 53 6983 3229 5523 -1653 1054 -85 C
ATOM 1213 CE1APHE B 53 -3.729 2.422 32.859 0.50 50.71 C
ANISOU 1213 CE1APHE B 53 9272 3126 6869 -438 -274 536 C
ATOM 1214 CE1BPHE B 53 -9.621 6.085 33.959 0.50 43.78 C
ANISOU 1214 CE1BPHE B 53 7613 3531 5490 -2221 1607 -63 C
ATOM 1215 CE2APHE B 53 -2.822 3.851 34.577 0.50 51.32 C
ANISOU 1215 CE2APHE B 53 9687 3230 6582 -145 -866 864 C
ATOM 1216 CE2BPHE B 53 -9.496 4.731 31.959 0.50 43.56 C
ANISOU 1216 CE2BPHE B 53 7112 3528 5909 -2053 1467 -391 C
ATOM 1217 CZ APHE B 53 -2.791 2.654 33.862 0.50 53.23 C
ANISOU 1217 CZ APHE B 53 9943 3211 7071 -118 -774 749 C
ATOM 1218 CZ BPHE B 53 -10.258 5.347 32.950 0.50 44.41 C
ANISOU 1218 CZ BPHE B 53 7349 3630 5894 -2344 1764 -399 C
ATOM 1219 N ILE B 54 -3.880 8.147 33.146 1.00 35.24 N
ANISOU 1219 N ILE B 54 5859 2890 4640 -486 -296 561 N
ATOM 1220 CA ILE B 54 -2.605 8.488 33.801 1.00 34.78 C
ANISOU 1220 CA ILE B 54 5834 2706 4675 -172 -742 638 C
ATOM 1221 C ILE B 54 -2.782 8.530 35.308 1.00 35.91 C
ANISOU 1221 C ILE B 54 6615 2599 4431 -222 -924 836 C
ATOM 1222 O ILE B 54 -3.852 8.811 35.812 1.00 35.94 O
ANISOU 1222 O ILE B 54 6870 2660 4124 -540 -598 894 O
ATOM 1223 CB ILE B 54 -1.978 9.798 33.299 1.00 31.74 C
ANISOU 1223 CB ILE B 54 4868 2667 4525 -53 -774 533 C
ATOM 1224 CG1 ILE B 54 -2.920 10.992 33.554 1.00 29.84 C
ANISOU 1224 CG1 ILE B 54 4559 2728 4049 -289 -542 582 C
ATOM 1225 CG2 ILE B 54 -1.558 9.653 31.822 1.00 31.17 C
ANISOU 1225 CG2 ILE B 54 4332 2736 4774 24 -580 340 C
ATOM 1226 CD1 ILE B 54 -2.236 12.359 33.499 1.00 27.65 C
ANISOU 1226 CD1 ILE B 54 3891 2667 3947 -177 -626 535 C
ATOM 1227 N LYS B 55 -1.712 8.229 36.031 1.00 35.30 N
ANISOU 1227 N LYS B 55 6823 2210 4379 111 -1464 896 N
ATOM 1228 CA LYS B 55 -1.621 8.348 37.495 1.00 38.02 C
ANISOU 1228 CA LYS B 55 7881 2281 4283 167 -1794 1076 C
ATOM 1229 C LYS B 55 -1.182 9.806 37.799 1.00 36.05 C
ANISOU 1229 C LYS B 55 7212 2365 4119 248 -1978 979 C
ATOM 1230 O LYS B 55 -0.273 10.361 37.153 1.00 38.17 O
ANISOU 1230 O LYS B 55 6784 2831 4889 468 -2162 775 O
ATOM 1231 CB LYS B 55 -0.598 7.388 38.037 1.00 46.75 C
ANISOU 1231 CB LYS B 55 9466 2878 5420 587 -2449 1128 C
ATOM 1232 CG LYS B 55 -1.030 5.872 38.070 1.00 54.06 C
ANISOU 1232 CG LYS B 55 11088 3304 6147 516 -2317 1287 C
ATOM 1233 CD LYS B 55 0.037 5.014 38.682 1.00 66.68 C
ANISOU 1233 CD LYS B 55 13229 4337 7768 1021 -3095 1345 C
ATOM 1234 CE LYS B 55 1.171 4.856 37.655 1.00 66.02 C
ANISOU 1234 CE LYS B 55 12237 4356 8492 1408 -3421 1014 C
ATOM 1235 NZ LYS B 55 2.068 3.839 38.073 1.00 72.53 N
ANISOU 1235 NZ LYS B 55 13505 4590 9462 1903 -4140 1003 N
ATOM 1236 N VAL B 56 -1.849 10.417 38.775 1.00 40.73 N
ANISOU 1236 N VAL B 56 8241 2989 4246 29 -1849 1089 N
ATOM 1237 CA VAL B 56 -1.642 11.812 39.113 1.00 39.55 C
ANISOU 1237 CA VAL B 56 7748 3140 4140 38 -1937 989 C
ATOM 1238 C VAL B 56 -1.541 11.941 40.624 1.00 44.69 C
ANISOU 1238 C VAL B 56 9210 3525 4244 94 -2292 1098 C
ATOM 1239 O VAL B 56 -1.900 11.017 41.362 1.00 48.99 O
ANISOU 1239 O VAL B 56 10663 3668 4282 29 -2298 1293 O
ATOM 1240 CB VAL B 56 -2.781 12.730 38.586 1.00 35.42 C
ANISOU 1240 CB VAL B 56 6804 3025 3631 -335 -1303 934 C
ATOM 1241 CG1 VAL B 56 -2.795 12.789 37.036 1.00 31.57 C
ANISOU 1241 CG1 VAL B 56 5582 2805 3608 -329 -1050 815 C
ATOM 1242 CG2 VAL B 56 -4.139 12.313 39.131 1.00 36.22 C
ANISOU 1242 CG2 VAL B 56 7461 3010 3290 -734 -803 1021 C
ATOM 1243 N ARG B 57 -1.008 13.064 41.078 1.00 44.33 N
ANISOU 1243 N ARG B 57 8907 3656 4279 218 -2591 961 N
ATOM 1244 CA ARG B 57 -1.036 13.390 42.502 1.00 48.58 C
ANISOU 1244 CA ARG B 57 10225 4006 4228 232 -2882 1021 C
ATOM 1245 C ARG B 57 -2.109 14.460 42.697 1.00 45.08 C
ANISOU 1245 C ARG B 57 9654 3880 3592 -189 -2253 983 C
ATOM 1246 O ARG B 57 -2.166 15.436 41.954 1.00 40.52 O
ANISOU 1246 O ARG B 57 8241 3681 3474 -256 -2026 829 O
ATOM 1247 CB ARG B 57 0.339 13.841 42.993 1.00 51.80 C
ANISOU 1247 CB ARG B 57 10463 4336 4881 698 -3754 810 C
ATOM 1248 CG ARG B 57 1.407 12.732 42.931 1.00 57.81 C
ANISOU 1248 CG ARG B 57 11374 4709 5882 1180 -4482 773 C
ATOM 1249 CD ARG B 57 2.804 13.268 43.231 1.00 63.60 C
ANISOU 1249 CD ARG B 57 11637 5409 7118 1656 -5353 404 C
ATOM 1250 NE ARG B 57 3.099 14.475 42.452 1.00 61.52 N
ANISOU 1250 NE ARG B 57 10243 5588 7543 1523 -5027 110 N
ATOM 1251 CZ ARG B 57 4.119 15.293 42.688 1.00 64.71 C
ANISOU 1251 CZ ARG B 57 10082 6049 8457 1771 -5539 -285 C
ATOM 1252 NH1 ARG B 57 4.961 15.045 43.688 1.00 74.98 N
ANISOU 1252 NH1 ARG B 57 11784 7026 9680 2222 -6522 -478 N
ATOM 1253 NH2 ARG B 57 4.297 16.362 41.926 1.00 60.23 N
ANISOU 1253 NH2 ARG B 57 8583 5819 8483 1576 -5088 -513 N
ATOM 1254 N GLN B 58 -3.005 14.227 43.645 1.00 48.05 N
ANISOU 1254 N GLN B 58 10895 4057 3306 -489 -1911 1110 N
ATOM 1255 CA GLN B 58 -4.096 15.140 43.889 1.00 46.30 C
ANISOU 1255 CA GLN B 58 10558 4083 2951 -900 -1267 1006 C
ATOM 1256 C GLN B 58 -3.759 16.042 45.072 1.00 49.80 C
ANISOU 1256 C GLN B 58 11409 4505 3007 -834 -1579 917 C
ATOM 1257 O GLN B 58 -3.554 15.561 46.195 1.00 55.00 O
ANISOU 1257 O GLN B 58 13119 4786 2991 -768 -1867 1036 O
ATOM 1258 CB GLN B 58 -5.402 14.386 44.131 1.00 48.42 C
ANISOU 1258 CB GLN B 58 11403 4151 2844 -1367 -507 1083 C
ATOM 1259 CG GLN B 58 -6.611 15.307 44.312 1.00 48.18 C
ANISOU 1259 CG GLN B 58 11106 4370 2831 -1801 210 863 C
ATOM 1260 CD GLN B 58 -7.886 14.581 44.707 1.00 54.43 C
ANISOU 1260 CD GLN B 58 12462 4903 3314 -2318 1037 824 C
ATOM 1261 OE1 GLN B 58 -8.287 13.601 44.082 1.00 56.65 O
ANISOU 1261 OE1 GLN B 58 12696 5054 3774 -2445 1307 859 O
ATOM 1262 NE2 GLN B 58 -8.544 15.085 45.723 1.00 58.01 N
ANISOU 1262 NE2 GLN B 58 13410 5273 3356 -2651 1503 693 N
ATOM 1263 N TYR B 59 -3.679 17.340 44.780 1.00 46.03 N
ANISOU 1263 N TYR B 59 10150 4398 2942 -833 -1546 707 N
ATOM 1264 CA TYR B 59 -3.466 18.392 45.758 1.00 48.98 C
ANISOU 1264 CA TYR B 59 10715 4821 3072 -818 -1753 543 C
ATOM 1265 C TYR B 59 -4.746 19.208 45.935 1.00 47.91 C
ANISOU 1265 C TYR B 59 10456 4885 2862 -1259 -973 407 C
ATOM 1266 O TYR B 59 -5.288 19.751 44.955 1.00 43.47 O
ANISOU 1266 O TYR B 59 9053 4614 2848 -1376 -583 312 O
ATOM 1267 CB TYR B 59 -2.345 19.329 45.293 1.00 46.42 C
ANISOU 1267 CB TYR B 59 9531 4717 3389 -491 -2281 337 C
ATOM 1268 CG TYR B 59 -0.966 18.715 45.258 1.00 48.86 C
ANISOU 1268 CG TYR B 59 9828 4823 3913 -25 -3116 309 C
ATOM 1269 CD1 TYR B 59 -0.096 18.825 46.360 1.00 54.32 C
ANISOU 1269 CD1 TYR B 59 11032 5296 4313 285 -3908 167 C
ATOM 1270 CD2 TYR B 59 -0.513 18.050 44.124 1.00 45.09 C
ANISOU 1270 CD2 TYR B 59 8802 4358 3971 132 -3156 355 C
ATOM 1271 CE1 TYR B 59 1.176 18.268 46.321 1.00 57.26 C
ANISOU 1271 CE1 TYR B 59 11293 5457 5008 769 -4762 43 C
ATOM 1272 CE2 TYR B 59 0.750 17.491 44.075 1.00 48.76 C
ANISOU 1272 CE2 TYR B 59 9154 4617 4755 567 -3897 241 C
ATOM 1273 CZ TYR B 59 1.593 17.609 45.177 1.00 55.22 C
ANISOU 1273 CZ TYR B 59 10405 5210 5365 900 -4725 67 C
ATOM 1274 OH TYR B 59 2.841 17.056 45.115 1.00 59.37 O
ANISOU 1274 OH TYR B 59 10723 5509 6324 1380 -5533 -136 O
ATOM 1275 N ASP B 60 -5.200 19.321 47.180 1.00 52.62 N
ANISOU 1275 N ASP B 60 11914 5295 2784 -1476 -777 365 N
ATOM 1276 CA ASP B 60 -6.428 20.038 47.499 1.00 52.86 C
ANISOU 1276 CA ASP B 60 11877 5455 2751 -1915 11 155 C
ATOM 1277 C ASP B 60 -6.164 21.455 47.991 1.00 52.62 C
ANISOU 1277 C ASP B 60 11556 5620 2817 -1855 -165 -102 C
ATOM 1278 O ASP B 60 -5.094 21.755 48.528 1.00 54.19 O
ANISOU 1278 O ASP B 60 11975 5757 2856 -1541 -877 -127 O
ATOM 1279 CB ASP B 60 -7.256 19.233 48.514 1.00 59.56 C
ANISOU 1279 CB ASP B 60 13885 5933 2812 -2310 587 213 C
ATOM 1280 CG ASP B 60 -7.641 17.846 47.978 1.00 61.22 C
ANISOU 1280 CG ASP B 60 14335 5912 3012 -2438 882 428 C
ATOM 1281 OD1 ASP B 60 -7.971 17.727 46.775 1.00 57.81 O
ANISOU 1281 OD1 ASP B 60 12991 5716 3260 -2442 1055 386 O
ATOM 1282 OD2 ASP B 60 -7.595 16.872 48.749 1.00 70.05 O
ANISOU 1282 OD2 ASP B 60 16614 6581 3420 -2521 917 636 O
ATOM 1283 N GLN B 61 -7.137 22.335 47.770 1.00 50.50 N
ANISOU 1283 N GLN B 61 10728 5570 2889 -2132 446 -344 N
ATOM 1284 CA GLN B 61 -7.080 23.696 48.280 1.00 51.05 C
ANISOU 1284 CA GLN B 61 10555 5784 3057 -2137 413 -623 C
ATOM 1285 C GLN B 61 -5.755 24.383 47.890 1.00 48.37 C
ANISOU 1285 C GLN B 61 9659 5572 3148 -1716 -360 -629 C
ATOM 1286 O GLN B 61 -5.055 24.963 48.722 1.00 50.81 O
ANISOU 1286 O GLN B 61 10239 5829 3236 -1582 -801 -781 O
ATOM 1287 CB GLN B 61 -7.349 23.707 49.793 1.00 58.07 C
ANISOU 1287 CB GLN B 61 12521 6439 3104 -2373 615 -748 C
ATOM 1288 CG GLN B 61 -8.564 22.858 50.171 1.00 62.83 C
ANISOU 1288 CG GLN B 61 13763 6824 3285 -2848 1488 -752 C
ATOM 1289 CD GLN B 61 -8.489 22.323 51.588 1.00 74.14 C
ANISOU 1289 CD GLN B 61 16663 7867 3640 -3012 1558 -688 C
ATOM 1290 OE1 GLN B 61 -8.244 21.119 51.807 1.00 79.04 O
ANISOU 1290 OE1 GLN B 61 18154 8155 3721 -2981 1423 -379 O
ATOM 1291 NE2 GLN B 61 -8.700 23.216 52.565 1.00 77.45 N
ANISOU 1291 NE2 GLN B 61 17449 8281 3698 -3181 1768 -982 N
ATOM 1292 N ILE B 62 -5.422 24.282 46.605 1.00 42.94 N
ANISOU 1292 N ILE B 62 8208 5025 3084 -1533 -486 -504 N
ATOM 1293 CA ILE B 62 -4.274 24.969 46.022 1.00 41.35 C
ANISOU 1293 CA ILE B 62 7349 4922 3442 -1225 -993 -561 C
ATOM 1294 C ILE B 62 -4.738 26.300 45.427 1.00 38.50 C
ANISOU 1294 C ILE B 62 6254 4748 3627 -1312 -644 -728 C
ATOM 1295 O ILE B 62 -5.734 26.343 44.723 1.00 35.78 O
ANISOU 1295 O ILE B 62 5613 4499 3482 -1453 -172 -692 O
ATOM 1296 CB ILE B 62 -3.607 24.102 44.904 1.00 38.81 C
ANISOU 1296 CB ILE B 62 6684 4591 3469 -1001 -1234 -349 C
ATOM 1297 CG1 ILE B 62 -2.953 22.838 45.485 1.00 43.37 C
ANISOU 1297 CG1 ILE B 62 7956 4922 3601 -819 -1727 -209 C
ATOM 1298 CG2 ILE B 62 -2.598 24.911 44.092 1.00 37.23 C
ANISOU 1298 CG2 ILE B 62 5700 4481 3964 -792 -1486 -461 C
ATOM 1299 CD1 ILE B 62 -1.772 23.100 46.434 1.00 47.79 C
ANISOU 1299 CD1 ILE B 62 8788 5337 4032 -532 -2498 -397 C
ATOM 1300 N LEU B 63 -4.007 27.377 45.697 1.00 29.24 N
ANISOU 1300 N LEU B 63 3791 5000 2320 -1398 -207 -275 N
ATOM 1301 CA LEU B 63 -4.301 28.687 45.109 1.00 29.51 C
ANISOU 1301 CA LEU B 63 3657 4968 2586 -1123 -90 -545 C
ATOM 1302 C LEU B 63 -3.714 28.791 43.715 1.00 28.41 C
ANISOU 1302 C LEU B 63 3534 4528 2732 -812 -189 -395 C
ATOM 1303 O LEU B 63 -2.510 28.522 43.523 1.00 27.83 O
ANISOU 1303 O LEU B 63 3557 4309 2709 -774 -319 -190 O
ATOM 1304 CB LEU B 63 -3.741 29.828 45.992 1.00 31.26 C
ANISOU 1304 CB LEU B 63 3863 5253 2763 -1177 -57 -726 C
ATOM 1305 CG LEU B 63 -3.832 31.256 45.408 1.00 30.85 C
ANISOU 1305 CG LEU B 63 3694 5037 2993 -890 -22 -971 C
ATOM 1306 CD1 LEU B 63 -5.286 31.713 45.227 1.00 32.84 C
ANISOU 1306 CD1 LEU B 63 3731 5382 3364 -792 105 -1325 C
ATOM 1307 CD2 LEU B 63 -3.056 32.259 46.232 1.00 33.79 C
ANISOU 1307 CD2 LEU B 63 4095 5419 3323 -957 -24 -1097 C
ATOM 1308 N ILE B 64 -4.533 29.210 42.748 1.00 28.44 N
ANISOU 1308 N ILE B 64 3431 4456 2918 -615 -140 -518 N
ATOM 1309 CA ILE B 64 -4.047 29.455 41.367 1.00 28.62 C
ANISOU 1309 CA ILE B 64 3488 4226 3160 -396 -229 -393 C
ATOM 1310 C ILE B 64 -4.593 30.780 40.895 1.00 28.98 C
ANISOU 1310 C ILE B 64 3454 4160 3398 -223 -246 -595 C
ATOM 1311 O ILE B 64 -5.725 31.139 41.214 1.00 30.79 O
ANISOU 1311 O ILE B 64 3537 4490 3670 -190 -186 -844 O
ATOM 1312 CB ILE B 64 -4.550 28.428 40.304 1.00 28.57 C
ANISOU 1312 CB ILE B 64 3487 4172 3197 -352 -241 -257 C
ATOM 1313 CG1 ILE B 64 -4.342 26.990 40.691 1.00 31.34 C
ANISOU 1313 CG1 ILE B 64 3917 4584 3406 -509 -267 -82 C
ATOM 1314 CG2 ILE B 64 -3.801 28.585 38.948 1.00 27.04 C
ANISOU 1314 CG2 ILE B 64 3350 3772 3152 -226 -317 -127 C
ATOM 1315 CD1 ILE B 64 -4.298 26.114 39.367 1.00 33.20 C
ANISOU 1315 CD1 ILE B 64 4180 4680 3755 -418 -307 56 C
ATOM 1316 N GLU B 65 -3.787 31.516 40.154 1.00 28.75 N
ANISOU 1316 N GLU B 65 3513 3920 3492 -131 -349 -507 N
ATOM 1317 CA GLU B 65 -4.278 32.739 39.563 1.00 31.26 C
ANISOU 1317 CA GLU B 65 3815 4047 4015 17 -458 -635 C
ATOM 1318 C GLU B 65 -4.381 32.467 38.077 1.00 30.47 C
ANISOU 1318 C GLU B 65 3788 3802 3986 62 -558 -445 C
ATOM 1319 O GLU B 65 -3.412 32.041 37.464 1.00 28.59 O
ANISOU 1319 O GLU B 65 3653 3538 3672 -25 -558 -252 O
ATOM 1320 CB GLU B 65 -3.355 33.910 39.867 1.00 33.09 C
ANISOU 1320 CB GLU B 65 4142 4139 4294 8 -535 -673 C
ATOM 1321 CG GLU B 65 -4.041 35.238 39.752 1.00 39.06 C
ANISOU 1321 CG GLU B 65 4868 4685 5289 158 -679 -889 C
ATOM 1322 CD GLU B 65 -3.157 36.360 40.233 1.00 45.84 C
ANISOU 1322 CD GLU B 65 5832 5407 6177 117 -747 -950 C
ATOM 1323 OE1 GLU B 65 -1.920 36.162 40.229 1.00 48.88 O
ANISOU 1323 OE1 GLU B 65 6337 5831 6405 -30 -714 -757 O
ATOM 1324 OE2 GLU B 65 -3.688 37.430 40.609 1.00 50.48 O
ANISOU 1324 OE2 GLU B 65 6367 5846 6968 236 -844 -1219 O
ATOM 1325 N ILE B 66 -5.575 32.648 37.524 1.00 31.89 N
ANISOU 1325 N ILE B 66 3887 3923 4307 178 -638 -533 N
ATOM 1326 CA ILE B 66 -5.838 32.281 36.130 1.00 32.30 C
ANISOU 1326 CA ILE B 66 4009 3877 4385 177 -737 -350 C
ATOM 1327 C ILE B 66 -6.233 33.556 35.439 1.00 35.07 C
ANISOU 1327 C ILE B 66 4426 3951 4949 278 -1006 -373 C
ATOM 1328 O ILE B 66 -7.277 34.137 35.734 1.00 36.15 O
ANISOU 1328 O ILE B 66 4417 4021 5296 449 -1113 -596 O
ATOM 1329 CB ILE B 66 -6.963 31.214 36.009 1.00 32.23 C
ANISOU 1329 CB ILE B 66 3862 4039 4347 194 -649 -389 C
ATOM 1330 CG1 ILE B 66 -6.552 29.918 36.699 1.00 31.14 C
ANISOU 1330 CG1 ILE B 66 3716 4114 4003 59 -452 -326 C
ATOM 1331 CG2 ILE B 66 -7.366 30.960 34.534 1.00 31.95 C
ANISOU 1331 CG2 ILE B 66 3894 3899 4345 185 -775 -225 C
ATOM 1332 CD1 ILE B 66 -7.746 29.107 37.176 1.00 34.89 C
ANISOU 1332 CD1 ILE B 66 4043 4800 4414 22 -345 -447 C
ATOM 1333 N CYS B 67 -5.349 34.009 34.556 1.00 36.58 N
ANISOU 1333 N CYS B 67 4833 3977 5088 148 -1133 -162 N
ATOM 1334 CA CYS B 67 -5.526 35.240 33.806 1.00 40.26 C
ANISOU 1334 CA CYS B 67 5459 4124 5713 160 -1462 -96 C
ATOM 1335 C CYS B 67 -5.966 36.373 34.748 1.00 41.96 C
ANISOU 1335 C CYS B 67 5589 4166 6189 363 -1597 -361 C
ATOM 1336 O CYS B 67 -6.817 37.199 34.403 1.00 44.66 O
ANISOU 1336 O CYS B 67 5923 4237 6810 521 -1907 -443 O
ATOM 1337 CB CYS B 67 -6.518 35.014 32.649 1.00 41.21 C
ANISOU 1337 CB CYS B 67 5597 4159 5904 177 -1658 15 C
ATOM 1338 SG CYS B 67 -6.467 36.289 31.380 1.00 52.19 S
ANISOU 1338 SG CYS B 67 7305 5141 7384 42 -2140 254 S
ATOM 1339 N GLY B 68 -5.379 36.403 35.949 1.00 40.61 N
ANISOU 1339 N GLY B 68 5343 4143 5946 358 -1386 -518 N
ATOM 1340 CA GLY B 68 -5.648 37.468 36.915 1.00 42.46 C
ANISOU 1340 CA GLY B 68 5490 4248 6396 509 -1464 -820 C
ATOM 1341 C GLY B 68 -6.852 37.237 37.818 1.00 43.41 C
ANISOU 1341 C GLY B 68 5285 4554 6655 691 -1334 -1203 C
ATOM 1342 O GLY B 68 -7.239 38.134 38.581 1.00 46.87 O
ANISOU 1342 O GLY B 68 5591 4902 7317 833 -1392 -1550 O
ATOM 1343 N HIS B 69 -7.454 36.054 37.725 1.00 40.48 N
ANISOU 1343 N HIS B 69 4774 4454 6153 662 -1156 -1177 N
ATOM 1344 CA HIS B 69 -8.560 35.658 38.590 1.00 40.99 C
ANISOU 1344 CA HIS B 69 4523 4793 6258 733 -976 -1537 C
ATOM 1345 C HIS B 69 -8.049 34.585 39.529 1.00 38.30 C
ANISOU 1345 C HIS B 69 4177 4819 5556 499 -649 -1485 C
ATOM 1346 O HIS B 69 -7.590 33.542 39.079 1.00 35.74 O
ANISOU 1346 O HIS B 69 3978 4579 5022 367 -577 -1178 O
ATOM 1347 CB HIS B 69 -9.709 35.053 37.771 1.00 41.26 C
ANISOU 1347 CB HIS B 69 4418 4870 6387 821 -1046 -1527 C
ATOM 1348 CG HIS B 69 -10.485 36.053 36.975 1.00 45.32 C
ANISOU 1348 CG HIS B 69 4880 5036 7303 1069 -1425 -1630 C
ATOM 1349 ND1 HIS B 69 -9.957 36.704 35.881 1.00 46.21 N
ANISOU 1349 ND1 HIS B 69 5286 4766 7505 1069 -1761 -1311 N
ATOM 1350 CD2 HIS B 69 -11.757 36.506 37.111 1.00 47.91 C
ANISOU 1350 CD2 HIS B 69 4891 5335 7978 1306 -1559 -2023 C
ATOM 1351 CE1 HIS B 69 -10.864 37.533 35.391 1.00 50.49 C
ANISOU 1351 CE1 HIS B 69 5736 5008 8441 1302 -2137 -1458 C
ATOM 1352 NE2 HIS B 69 -11.967 37.424 36.113 1.00 51.24 N
ANISOU 1352 NE2 HIS B 69 5434 5304 8732 1484 -2024 -1910 N
ATOM 1353 N LYS B 70 -8.158 34.827 40.827 1.00 38.81 N
ANISOU 1353 N LYS B 70 4097 5092 5555 431 -479 -1800 N
ATOM 1354 CA LYS B 70 -7.756 33.849 41.839 1.00 37.28 C
ANISOU 1354 CA LYS B 70 3924 5244 4998 154 -227 -1744 C
ATOM 1355 C LYS B 70 -8.827 32.769 42.072 1.00 37.35 C
ANISOU 1355 C LYS B 70 3760 5575 4856 26 -59 -1844 C
ATOM 1356 O LYS B 70 -10.013 33.072 42.118 1.00 39.57 O
ANISOU 1356 O LYS B 70 3774 5955 5305 127 -31 -2200 O
ATOM 1357 CB LYS B 70 -7.443 34.580 43.151 1.00 39.19 C
ANISOU 1357 CB LYS B 70 4107 5612 5171 51 -117 -2041 C
ATOM 1358 CG LYS B 70 -6.253 35.508 43.048 1.00 39.98 C
ANISOU 1358 CG LYS B 70 4407 5432 5350 104 -261 -1908 C
ATOM 1359 CD LYS B 70 -5.978 36.191 44.374 1.00 44.19 C
ANISOU 1359 CD LYS B 70 4880 6111 5798 -22 -141 -2220 C
ATOM 1360 CE LYS B 70 -5.256 37.507 44.189 1.00 49.10 C
ANISOU 1360 CE LYS B 70 5629 6392 6636 108 -324 -2252 C
ATOM 1361 NZ LYS B 70 -3.970 37.284 43.493 1.00 48.05 N
ANISOU 1361 NZ LYS B 70 5768 6095 6396 43 -436 -1786 N
ATOM 1362 N ALA B 71 -8.392 31.521 42.221 1.00 34.83 N
ANISOU 1362 N ALA B 71 3587 5407 4240 -202 27 -1547 N
ATOM 1363 CA ALA B 71 -9.259 30.404 42.570 1.00 35.10 C
ANISOU 1363 CA ALA B 71 3530 5750 4057 -420 176 -1588 C
ATOM 1364 C ALA B 71 -8.498 29.514 43.531 1.00 34.87 C
ANISOU 1364 C ALA B 71 3689 5892 3668 -756 243 -1373 C
ATOM 1365 O ALA B 71 -7.268 29.486 43.522 1.00 32.89 O
ANISOU 1365 O ALA B 71 3639 5466 3393 -746 137 -1108 O
ATOM 1366 CB ALA B 71 -9.661 29.618 41.311 1.00 33.45 C
ANISOU 1366 CB ALA B 71 3359 5423 3928 -320 91 -1354 C
ATOM 1367 N ILE B 72 -9.221 28.825 44.400 1.00 36.24 N
ANISOU 1367 N ILE B 72 3795 6416 3557 -1083 397 -1502 N
ATOM 1368 CA ILE B 72 -8.631 27.819 45.267 1.00 36.93 C
ANISOU 1368 CA ILE B 72 4111 6640 3280 -1462 384 -1237 C
ATOM 1369 C ILE B 72 -9.368 26.532 44.979 1.00 37.73 C
ANISOU 1369 C ILE B 72 4257 6852 3224 -1655 397 -1087 C
ATOM 1370 O ILE B 72 -10.610 26.492 44.976 1.00 38.87 O
ANISOU 1370 O ILE B 72 4183 7252 3334 -1740 554 -1373 O
ATOM 1371 CB ILE B 72 -8.698 28.190 46.777 1.00 40.55 C
ANISOU 1371 CB ILE B 72 4529 7447 3431 -1830 531 -1496 C
ATOM 1372 CG1 ILE B 72 -7.671 29.280 47.103 1.00 39.58 C
ANISOU 1372 CG1 ILE B 72 4446 7164 3428 -1678 471 -1543 C
ATOM 1373 CG2 ILE B 72 -8.389 26.982 47.658 1.00 42.42 C
ANISOU 1373 CG2 ILE B 72 5027 7857 3235 -2321 469 -1194 C
ATOM 1374 CD1 ILE B 72 -7.704 29.752 48.541 1.00 42.02 C
ANISOU 1374 CD1 ILE B 72 4708 7817 3442 -2039 624 -1836 C
ATOM 1375 N GLY B 73 -8.619 25.485 44.663 1.00 35.93 N
ANISOU 1375 N GLY B 73 4290 6416 2946 -1703 218 -668 N
ATOM 1376 CA GLY B 73 -9.278 24.222 44.385 1.00 35.86 C
ANISOU 1376 CA GLY B 73 4362 6465 2797 -1901 199 -511 C
ATOM 1377 C GLY B 73 -8.279 23.121 44.229 1.00 34.61 C
ANISOU 1377 C GLY B 73 4500 6026 2624 -1947 -51 -83 C
ATOM 1378 O GLY B 73 -7.083 23.299 44.475 1.00 33.50 O
ANISOU 1378 O GLY B 73 4478 5698 2552 -1863 -205 75 O
ATOM 1379 N THR B 74 -8.794 21.980 43.814 1.00 34.98 N
ANISOU 1379 N THR B 74 4643 6039 2609 -2076 -105 72 N
ATOM 1380 CA THR B 74 -7.986 20.803 43.587 1.00 34.59 C
ANISOU 1380 CA THR B 74 4857 5679 2608 -2100 -377 432 C
ATOM 1381 C THR B 74 -7.170 20.904 42.318 1.00 31.62 C
ANISOU 1381 C THR B 74 4434 4963 2618 -1652 -458 494 C
ATOM 1382 O THR B 74 -7.678 21.210 41.205 1.00 30.23 O
ANISOU 1382 O THR B 74 4103 4764 2618 -1415 -333 367 O
ATOM 1383 CB THR B 74 -8.872 19.544 43.549 1.00 36.55 C
ANISOU 1383 CB THR B 74 5238 5987 2664 -2414 -415 554 C
ATOM 1384 OG1 THR B 74 -9.399 19.331 44.850 1.00 39.63 O
ANISOU 1384 OG1 THR B 74 5733 6700 2625 -2944 -381 545 O
ATOM 1385 CG2 THR B 74 -8.079 18.300 43.117 1.00 36.11 C
ANISOU 1385 CG2 THR B 74 5435 5521 2765 -2361 -736 886 C
ATOM 1386 N VAL B 75 -5.893 20.620 42.479 1.00 31.28 N
ANISOU 1386 N VAL B 75 4519 4670 2697 -1569 -684 679 N
ATOM 1387 CA VAL B 75 -5.010 20.511 41.337 1.00 29.52 C
ANISOU 1387 CA VAL B 75 4246 4159 2812 -1221 -762 708 C
ATOM 1388 C VAL B 75 -4.405 19.115 41.286 1.00 30.82 C
ANISOU 1388 C VAL B 75 4585 4035 3090 -1258 -1054 924 C
ATOM 1389 O VAL B 75 -3.864 18.612 42.283 1.00 32.63 O
ANISOU 1389 O VAL B 75 4987 4174 3237 -1442 -1313 1107 O
ATOM 1390 CB VAL B 75 -3.916 21.585 41.389 1.00 27.91 C
ANISOU 1390 CB VAL B 75 3947 3910 2746 -1018 -759 634 C
ATOM 1391 CG1 VAL B 75 -2.940 21.429 40.239 1.00 26.57 C
ANISOU 1391 CG1 VAL B 75 3704 3506 2885 -736 -818 623 C
ATOM 1392 CG2 VAL B 75 -4.549 22.958 41.395 1.00 28.08 C
ANISOU 1392 CG2 VAL B 75 3818 4144 2709 -964 -524 412 C
ATOM 1393 N LEU B 76 -4.529 18.493 40.118 1.00 30.40 N
ANISOU 1393 N LEU B 76 4491 3824 3235 -1094 -1039 893 N
ATOM 1394 CA LEU B 76 -3.882 17.228 39.814 1.00 31.90 C
ANISOU 1394 CA LEU B 76 4790 3682 3649 -1035 -1314 1007 C
ATOM 1395 C LEU B 76 -2.540 17.483 39.126 1.00 31.12 C
ANISOU 1395 C LEU B 76 4524 3404 3896 -708 -1364 879 C
ATOM 1396 O LEU B 76 -2.442 18.323 38.236 1.00 28.88 O
ANISOU 1396 O LEU B 76 4062 3233 3679 -540 -1126 699 O
ATOM 1397 CB LEU B 76 -4.788 16.414 38.887 1.00 31.93 C
ANISOU 1397 CB LEU B 76 4816 3646 3672 -1063 -1235 979 C
ATOM 1398 CG LEU B 76 -5.895 15.516 39.447 1.00 35.54 C
ANISOU 1398 CG LEU B 76 5483 4158 3863 -1423 -1306 1136 C
ATOM 1399 CD1 LEU B 76 -6.490 15.907 40.826 1.00 37.54 C
ANISOU 1399 CD1 LEU B 76 5841 4701 3722 -1795 -1279 1226 C
ATOM 1400 CD2 LEU B 76 -6.994 15.298 38.405 1.00 34.83 C
ANISOU 1400 CD2 LEU B 76 5313 4182 3739 -1424 -1084 1022 C
ATOM 1401 N VAL B 77 -1.513 16.746 39.528 1.00 32.90 N
ANISOU 1401 N VAL B 77 4806 3351 4343 -644 -1698 960 N
ATOM 1402 CA VAL B 77 -0.189 16.869 38.924 1.00 33.19 C
ANISOU 1402 CA VAL B 77 4630 3242 4737 -350 -1757 775 C
ATOM 1403 C VAL B 77 0.257 15.515 38.376 1.00 35.50 C
ANISOU 1403 C VAL B 77 4913 3184 5391 -209 -2015 711 C
ATOM 1404 O VAL B 77 0.236 14.513 39.090 1.00 38.05 O
ANISOU 1404 O VAL B 77 5444 3241 5772 -312 -2388 913 O
ATOM 1405 CB VAL B 77 0.855 17.349 39.949 1.00 35.31 C
ANISOU 1405 CB VAL B 77 4884 3491 5040 -337 -1965 846 C
ATOM 1406 CG1 VAL B 77 2.234 17.551 39.267 1.00 36.23 C
ANISOU 1406 CG1 VAL B 77 4716 3521 5527 -46 -1984 590 C
ATOM 1407 CG2 VAL B 77 0.394 18.662 40.599 1.00 33.83 C
ANISOU 1407 CG2 VAL B 77 4721 3630 4502 -495 -1726 882 C
ATOM 1408 N GLY B 78 0.670 15.485 37.118 1.00 33.98 N
ANISOU 1408 N GLY B 78 4487 2982 5440 -1 -1838 417 N
ATOM 1409 CA GLY B 78 1.131 14.242 36.505 1.00 36.31 C
ANISOU 1409 CA GLY B 78 4712 2954 6130 161 -2047 249 C
ATOM 1410 C GLY B 78 1.440 14.411 35.032 1.00 34.99 C
ANISOU 1410 C GLY B 78 4265 2911 6118 302 -1732 -134 C
ATOM 1411 O GLY B 78 1.392 15.530 34.519 1.00 32.84 O
ANISOU 1411 O GLY B 78 3883 2955 5641 257 -1397 -221 O
ATOM 1412 N PRO B 79 1.724 13.291 34.335 1.00 37.24 N
ANISOU 1412 N PRO B 79 4454 2942 6753 435 -1851 -370 N
ATOM 1413 CA PRO B 79 2.213 13.325 32.957 1.00 36.78 C
ANISOU 1413 CA PRO B 79 4092 3013 6868 534 -1568 -813 C
ATOM 1414 C PRO B 79 1.130 13.612 31.926 1.00 34.32 C
ANISOU 1414 C PRO B 79 3848 2961 6231 344 -1194 -824 C
ATOM 1415 O PRO B 79 0.954 12.832 30.991 1.00 35.19 O
ANISOU 1415 O PRO B 79 3892 3000 6476 349 -1119 -1060 O
ATOM 1416 CB PRO B 79 2.810 11.924 32.757 1.00 41.31 C
ANISOU 1416 CB PRO B 79 4554 3180 7964 743 -1885 -1076 C
ATOM 1417 CG PRO B 79 2.080 11.057 33.695 1.00 42.74 C
ANISOU 1417 CG PRO B 79 5098 3022 8118 662 -2270 -683 C
ATOM 1418 CD PRO B 79 1.653 11.912 34.862 1.00 39.81 C
ANISOU 1418 CD PRO B 79 4961 2823 7342 474 -2299 -249 C
ATOM 1419 N THR B 80 0.406 14.712 32.110 1.00 30.54 N
ANISOU 1419 N THR B 80 3493 2761 5350 182 -993 -585 N
ATOM 1420 CA THR B 80 -0.472 15.226 31.072 1.00 29.31 C
ANISOU 1420 CA THR B 80 3359 2867 4911 19 -674 -608 C
ATOM 1421 C THR B 80 0.432 15.914 30.024 1.00 30.41 C
ANISOU 1421 C THR B 80 3249 3229 5076 1 -430 -934 C
ATOM 1422 O THR B 80 1.459 16.511 30.390 1.00 30.38 O
ANISOU 1422 O THR B 80 3102 3276 5163 74 -452 -1023 O
ATOM 1423 CB THR B 80 -1.504 16.230 31.648 1.00 26.88 C
ANISOU 1423 CB THR B 80 3228 2749 4238 -114 -597 -291 C
ATOM 1424 OG1 THR B 80 -2.196 16.864 30.577 1.00 24.23 O
ANISOU 1424 OG1 THR B 80 2882 2640 3685 -243 -351 -329 O
ATOM 1425 CG2 THR B 80 -0.834 17.303 32.532 1.00 23.83 C
ANISOU 1425 CG2 THR B 80 2808 2441 3804 -67 -635 -207 C
ATOM 1426 N PRO B 81 0.085 15.806 28.729 1.00 30.78 N
ANISOU 1426 N PRO B 81 3247 3430 5020 -143 -201 -1120 N
ATOM 1427 CA PRO B 81 0.958 16.480 27.759 1.00 31.98 C
ANISOU 1427 CA PRO B 81 3188 3841 5122 -263 35 -1425 C
ATOM 1428 C PRO B 81 0.833 18.010 27.761 1.00 30.01 C
ANISOU 1428 C PRO B 81 3032 3826 4546 -423 145 -1217 C
ATOM 1429 O PRO B 81 1.639 18.677 27.144 1.00 30.51 O
ANISOU 1429 O PRO B 81 2959 4100 4532 -570 301 -1417 O
ATOM 1430 CB PRO B 81 0.485 15.905 26.413 1.00 32.60 C
ANISOU 1430 CB PRO B 81 3241 4028 5116 -446 228 -1643 C
ATOM 1431 CG PRO B 81 -0.862 15.495 26.630 1.00 31.01 C
ANISOU 1431 CG PRO B 81 3284 3711 4789 -462 137 -1339 C
ATOM 1432 CD PRO B 81 -0.989 15.049 28.055 1.00 30.87 C
ANISOU 1432 CD PRO B 81 3377 3410 4940 -251 -147 -1096 C
ATOM 1433 N VAL B 82 -0.167 18.548 28.462 1.00 28.25 N
ANISOU 1433 N VAL B 82 3029 3564 4142 -412 52 -848 N
ATOM 1434 CA VAL B 82 -0.550 19.955 28.363 1.00 27.46 C
ANISOU 1434 CA VAL B 82 3043 3623 3769 -547 111 -656 C
ATOM 1435 C VAL B 82 -1.156 20.321 29.708 1.00 25.35 C
ANISOU 1435 C VAL B 82 2903 3249 3480 -412 -45 -378 C
ATOM 1436 O VAL B 82 -1.920 19.521 30.247 1.00 25.45 O
ANISOU 1436 O VAL B 82 2993 3149 3529 -347 -137 -268 O
ATOM 1437 CB VAL B 82 -1.623 20.104 27.217 1.00 28.84 C
ANISOU 1437 CB VAL B 82 3334 3915 3711 -755 204 -587 C
ATOM 1438 CG1 VAL B 82 -2.354 21.421 27.274 1.00 29.21 C
ANISOU 1438 CG1 VAL B 82 3533 4017 3549 -831 146 -335 C
ATOM 1439 CG2 VAL B 82 -0.954 19.920 25.836 1.00 33.06 C
ANISOU 1439 CG2 VAL B 82 3755 4628 4178 -994 390 -881 C
ATOM 1440 N ASN B 83 -0.777 21.469 30.273 1.00 22.97 N
ANISOU 1440 N ASN B 83 2620 2997 3111 -406 -68 -295 N
ATOM 1441 CA ASN B 83 -1.452 22.031 31.432 1.00 22.08 C
ANISOU 1441 CA ASN B 83 2614 2845 2929 -332 -168 -88 C
ATOM 1442 C ASN B 83 -2.899 22.357 31.084 1.00 20.96 C
ANISOU 1442 C ASN B 83 2574 2751 2640 -389 -152 34 C
ATOM 1443 O ASN B 83 -3.164 23.136 30.148 1.00 20.97 O
ANISOU 1443 O ASN B 83 2612 2818 2539 -495 -117 45 O
ATOM 1444 CB ASN B 83 -0.801 23.326 31.900 1.00 21.97 C
ANISOU 1444 CB ASN B 83 2601 2877 2868 -339 -180 -65 C
ATOM 1445 CG ASN B 83 0.641 23.149 32.393 1.00 25.41 C
ANISOU 1445 CG ASN B 83 2909 3293 3453 -280 -217 -187 C
ATOM 1446 OD1 ASN B 83 0.974 22.176 33.079 1.00 24.09 O
ANISOU 1446 OD1 ASN B 83 2692 3014 3446 -167 -334 -201 O
ATOM 1447 ND2 ASN B 83 1.491 24.141 32.075 1.00 23.23 N
ANISOU 1447 ND2 ASN B 83 2588 3113 3125 -375 -156 -264 N
ATOM 1448 N AILE B 84 -3.845 21.754 31.795 0.50 20.28 N
ANISOU 1448 N AILE B 84 2531 2638 2536 -352 -202 123 N
ATOM 1449 N BILE B 84 -3.807 21.794 31.877 0.50 20.52 N
ANISOU 1449 N BILE B 84 2561 2667 2568 -347 -207 125 N
ATOM 1450 CA AILE B 84 -5.253 22.005 31.501 0.50 19.80 C
ANISOU 1450 CA AILE B 84 2504 2651 2369 -394 -190 186 C
ATOM 1451 CA BILE B 84 -5.241 21.889 31.664 0.50 20.27 C
ANISOU 1451 CA BILE B 84 2564 2704 2433 -388 -196 190 C
ATOM 1452 C AILE B 84 -6.042 22.486 32.731 0.50 19.65 C
ANISOU 1452 C AILE B 84 2481 2690 2295 -357 -227 231 C
ATOM 1453 C BILE B 84 -5.934 22.578 32.849 0.50 19.95 C
ANISOU 1453 C BILE B 84 2518 2725 2336 -350 -231 231 C
ATOM 1454 O AILE B 84 -5.987 21.875 33.800 0.50 20.68 O
ANISOU 1454 O AILE B 84 2636 2818 2404 -380 -257 264 O
ATOM 1455 O BILE B 84 -5.731 22.182 34.004 0.50 20.89 O
ANISOU 1455 O BILE B 84 2658 2842 2438 -360 -264 259 O
ATOM 1456 CB AILE B 84 -5.953 20.782 30.803 0.50 20.13 C
ANISOU 1456 CB AILE B 84 2563 2690 2396 -468 -159 177 C
ATOM 1457 CB BILE B 84 -5.839 20.462 31.490 0.50 20.68 C
ANISOU 1457 CB BILE B 84 2644 2726 2489 -443 -192 198 C
ATOM 1458 CG1AILE B 84 -5.938 19.533 31.691 0.50 20.52 C
ANISOU 1458 CG1AILE B 84 2654 2647 2495 -467 -220 209 C
ATOM 1459 CG1BILE B 84 -5.372 19.827 30.171 0.50 20.06 C
ANISOU 1459 CG1BILE B 84 2542 2613 2465 -497 -128 88 C
ATOM 1460 CG2AILE B 84 -5.322 20.472 29.439 0.50 19.67 C
ANISOU 1460 CG2AILE B 84 2483 2629 2361 -548 -85 65 C
ATOM 1461 CG2BILE B 84 -7.378 20.485 31.595 0.50 21.24 C
ANISOU 1461 CG2BILE B 84 2717 2910 2445 -501 -182 249 C
ATOM 1462 CD1AILE B 84 -6.747 18.360 31.111 0.50 18.97 C
ANISOU 1462 CD1AILE B 84 2501 2430 2276 -562 -207 209 C
ATOM 1463 CD1BILE B 84 -5.500 18.306 30.139 0.50 17.17 C
ANISOU 1463 CD1BILE B 84 2205 2134 2184 -517 -159 51 C
ATOM 1464 N ILE B 85 -6.724 23.616 32.571 1.00 19.72 N
ANISOU 1464 N ILE B 85 2458 2748 2288 -322 -247 212 N
ATOM 1465 CA ILE B 85 -7.642 24.164 33.582 1.00 20.37 C
ANISOU 1465 CA ILE B 85 2468 2925 2346 -285 -255 151 C
ATOM 1466 C ILE B 85 -9.025 23.593 33.328 1.00 19.96 C
ANISOU 1466 C ILE B 85 2349 2986 2251 -336 -231 119 C
ATOM 1467 O ILE B 85 -9.669 23.903 32.325 1.00 20.42 O
ANISOU 1467 O ILE B 85 2375 3033 2352 -310 -286 116 O
ATOM 1468 CB ILE B 85 -7.707 25.724 33.549 1.00 21.24 C
ANISOU 1468 CB ILE B 85 2544 2985 2542 -180 -334 86 C
ATOM 1469 CG1 ILE B 85 -6.286 26.335 33.631 1.00 21.20 C
ANISOU 1469 CG1 ILE B 85 2620 2878 2557 -174 -355 125 C
ATOM 1470 CG2 ILE B 85 -8.700 26.291 34.658 1.00 22.47 C
ANISOU 1470 CG2 ILE B 85 2556 3261 2718 -125 -320 -89 C
ATOM 1471 CD1 ILE B 85 -5.489 25.913 34.831 1.00 21.64 C
ANISOU 1471 CD1 ILE B 85 2680 2972 2570 -196 -306 122 C
ATOM 1472 N GLY B 86 -9.510 22.807 34.273 1.00 21.08 N
ANISOU 1472 N GLY B 86 2510 3416 2084 -408 -192 84 N
ATOM 1473 CA GLY B 86 -10.773 22.130 34.095 1.00 20.56 C
ANISOU 1473 CA GLY B 86 2538 3370 1906 -510 -205 162 C
ATOM 1474 C GLY B 86 -11.907 22.811 34.821 1.00 21.09 C
ANISOU 1474 C GLY B 86 2458 3720 1834 -598 -180 51 C
ATOM 1475 O GLY B 86 -11.705 23.812 35.515 1.00 22.12 O
ANISOU 1475 O GLY B 86 2459 3969 1976 -538 -172 -101 O
ATOM 1476 N ARG B 87 -13.101 22.231 34.707 1.00 21.66 N
ANISOU 1476 N ARG B 87 2536 3956 1738 -750 -180 95 N
ATOM 1477 CA ARG B 87 -14.322 22.885 35.195 1.00 23.04 C
ANISOU 1477 CA ARG B 87 2473 4536 1745 -784 -145 -97 C
ATOM 1478 C ARG B 87 -14.275 23.211 36.690 1.00 24.87 C
ANISOU 1478 C ARG B 87 2526 5117 1804 -871 -158 -210 C
ATOM 1479 O ARG B 87 -14.837 24.222 37.109 1.00 26.72 O
ANISOU 1479 O ARG B 87 2534 5629 1990 -726 -137 -495 O
ATOM 1480 CB ARG B 87 -15.577 22.076 34.836 1.00 23.26 C
ANISOU 1480 CB ARG B 87 2479 4812 1546 -1017 -138 -29 C
ATOM 1481 CG ARG B 87 -15.860 21.979 33.292 1.00 21.16 C
ANISOU 1481 CG ARG B 87 2342 4270 1429 -911 -119 21 C
ATOM 1482 CD ARG B 87 -17.195 21.225 33.017 1.00 24.23 C
ANISOU 1482 CD ARG B 87 2670 4993 1541 -1196 -116 69 C
ATOM 1483 NE ARG B 87 -17.193 19.857 33.559 1.00 26.92 N
ANISOU 1483 NE ARG B 87 3233 5362 1634 -1620 -189 318 N
ATOM 1484 CZ ARG B 87 -17.742 19.463 34.715 1.00 30.67 C
ANISOU 1484 CZ ARG B 87 3601 6302 1750 -1997 -221 344 C
ATOM 1485 NH1 ARG B 87 -18.385 20.308 35.520 1.00 29.23 N
ANISOU 1485 NH1 ARG B 87 2997 6709 1402 -1970 -142 76 N
ATOM 1486 NH2 ARG B 87 -17.639 18.193 35.074 1.00 32.62 N
ANISOU 1486 NH2 ARG B 87 4198 6427 1770 -2421 -365 629 N
ATOM 1487 N ASN B 88 -13.599 22.385 37.489 1.00 25.65 N
ANISOU 1487 N ASN B 88 2745 5195 1804 -1074 -226 -16 N
ATOM 1488 CA ASN B 88 -13.480 22.649 38.911 1.00 27.64 C
ANISOU 1488 CA ASN B 88 2849 5788 1866 -1208 -246 -96 C
ATOM 1489 C ASN B 88 -12.947 24.054 39.220 1.00 27.44 C
ANISOU 1489 C ASN B 88 2678 5740 2009 -926 -206 -362 C
ATOM 1490 O ASN B 88 -13.337 24.674 40.229 1.00 29.44 O
ANISOU 1490 O ASN B 88 2717 6383 2087 -954 -186 -591 O
ATOM 1491 CB ASN B 88 -12.658 21.566 39.619 1.00 29.24 C
ANISOU 1491 CB ASN B 88 3283 5859 1967 -1429 -397 190 C
ATOM 1492 CG ASN B 88 -11.165 21.722 39.417 1.00 29.61 C
ANISOU 1492 CG ASN B 88 3433 5517 2302 -1155 -456 237 C
ATOM 1493 OD1 ASN B 88 -10.696 21.706 38.291 1.00 27.33 O
ANISOU 1493 OD1 ASN B 88 3231 4903 2252 -934 -431 248 O
ATOM 1494 ND2 ASN B 88 -10.403 21.858 40.532 1.00 29.72 N
ANISOU 1494 ND2 ASN B 88 3402 5643 2249 -1202 -535 249 N
ATOM 1495 N LEU B 89 -12.088 24.571 38.346 1.00 24.60 N
ANISOU 1495 N LEU B 89 2445 4957 1943 -698 -207 -353 N
ATOM 1496 CA LEU B 89 -11.568 25.926 38.516 1.00 25.21 C
ANISOU 1496 CA LEU B 89 2492 4937 2150 -516 -218 -570 C
ATOM 1497 C LEU B 89 -12.236 26.941 37.591 1.00 25.14 C
ANISOU 1497 C LEU B 89 2529 4761 2260 -284 -244 -769 C
ATOM 1498 O LEU B 89 -12.360 28.115 37.934 1.00 26.48 O
ANISOU 1498 O LEU B 89 2699 4915 2446 -118 -322 -1032 O
ATOM 1499 CB LEU B 89 -10.042 25.950 38.345 1.00 24.37 C
ANISOU 1499 CB LEU B 89 2495 4562 2201 -525 -240 -435 C
ATOM 1500 CG LEU B 89 -9.250 25.123 39.366 1.00 26.48 C
ANISOU 1500 CG LEU B 89 2724 4972 2363 -663 -294 -282 C
ATOM 1501 CD1 LEU B 89 -7.738 25.242 39.109 1.00 28.96 C
ANISOU 1501 CD1 LEU B 89 3051 5133 2818 -612 -321 -224 C
ATOM 1502 CD2 LEU B 89 -9.576 25.573 40.773 1.00 29.73 C
ANISOU 1502 CD2 LEU B 89 2996 5727 2573 -772 -308 -429 C
ATOM 1503 N LEU B 90 -12.665 26.490 36.416 1.00 23.65 N
ANISOU 1503 N LEU B 90 2426 4414 2145 -260 -223 -650 N
ATOM 1504 CA LEU B 90 -13.363 27.367 35.483 1.00 24.33 C
ANISOU 1504 CA LEU B 90 2589 4330 2324 -41 -300 -804 C
ATOM 1505 C LEU B 90 -14.603 27.977 36.140 1.00 26.60 C
ANISOU 1505 C LEU B 90 2654 4991 2462 168 -366 -1150 C
ATOM 1506 O LEU B 90 -14.878 29.168 35.944 1.00 28.24 O
ANISOU 1506 O LEU B 90 2959 5024 2749 464 -531 -1406 O
ATOM 1507 CB LEU B 90 -13.738 26.638 34.190 1.00 22.32 C
ANISOU 1507 CB LEU B 90 2424 3935 2122 -88 -260 -617 C
ATOM 1508 CG LEU B 90 -12.564 26.191 33.288 1.00 20.98 C
ANISOU 1508 CG LEU B 90 2448 3432 2092 -211 -209 -378 C
ATOM 1509 CD1 LEU B 90 -13.149 25.406 32.111 1.00 18.02 C
ANISOU 1509 CD1 LEU B 90 2141 2985 1720 -252 -169 -246 C
ATOM 1510 CD2 LEU B 90 -11.676 27.367 32.787 1.00 22.79 C
ANISOU 1510 CD2 LEU B 90 2863 3356 2442 -198 -285 -416 C
ATOM 1511 N THR B 91 -15.332 27.174 36.918 1.00 27.57 N
ANISOU 1511 N THR B 91 2498 5644 2333 6 -272 -1180 N
ATOM 1512 CA THR B 91 -16.532 27.665 37.600 1.00 31.74 C
ANISOU 1512 CA THR B 91 2691 6730 2638 180 -301 -1576 C
ATOM 1513 C THR B 91 -16.181 28.792 38.587 1.00 34.86 C
ANISOU 1513 C THR B 91 3056 7154 3035 401 -390 -1906 C
ATOM 1514 O THR B 91 -16.914 29.791 38.714 1.00 37.05 O
ANISOU 1514 O THR B 91 3217 7574 3285 802 -531 -2341 O
ATOM 1515 CB THR B 91 -17.310 26.544 38.350 1.00 33.43 C
ANISOU 1515 CB THR B 91 2593 7635 2473 -203 -169 -1526 C
ATOM 1516 OG1 THR B 91 -16.442 25.824 39.223 1.00 31.09 O
ANISOU 1516 OG1 THR B 91 2395 7332 2085 -566 -116 -1265 O
ATOM 1517 CG2 THR B 91 -17.909 25.572 37.405 1.00 31.45 C
ANISOU 1517 CG2 THR B 91 2379 7406 2165 -408 -127 -1286 C
ATOM 1518 N GLN B 92 -15.027 28.656 39.247 1.00 34.42 N
ANISOU 1518 N GLN B 92 3129 6933 3016 180 -346 -1725 N
ATOM 1519 CA GLN B 92 -14.628 29.617 40.269 1.00 37.96 C
ANISOU 1519 CA GLN B 92 3563 7430 3428 303 -419 -2011 C
ATOM 1520 C GLN B 92 -14.241 30.977 39.694 1.00 38.75 C
ANISOU 1520 C GLN B 92 4005 6949 3768 628 -636 -2185 C
ATOM 1521 O GLN B 92 -14.261 31.975 40.404 1.00 43.21 O
ANISOU 1521 O GLN B 92 4602 7524 4291 845 -772 -2541 O
ATOM 1522 CB GLN B 92 -13.457 29.085 41.113 1.00 36.78 C
ANISOU 1522 CB GLN B 92 3461 7280 3235 -47 -338 -1748 C
ATOM 1523 CG GLN B 92 -13.518 27.615 41.523 1.00 39.54 C
ANISOU 1523 CG GLN B 92 3684 7961 3378 -440 -221 -1432 C
ATOM 1524 CD GLN B 92 -14.623 27.291 42.502 1.00 46.43 C
ANISOU 1524 CD GLN B 92 4207 9580 3855 -613 -155 -1641 C
ATOM 1525 OE1 GLN B 92 -15.738 26.871 42.111 1.00 50.84 O
ANISOU 1525 OE1 GLN B 92 4585 10481 4252 -654 -109 -1701 O
ATOM 1526 NE2 GLN B 92 -14.335 27.480 43.784 1.00 49.50 N
ANISOU 1526 NE2 GLN B 92 4468 10306 4035 -766 -145 -1765 N
ATOM 1527 N ILE B 93 -13.812 31.015 38.445 1.00 36.51 N
ANISOU 1527 N ILE B 93 4026 6145 3700 607 -693 -1924 N
ATOM 1528 CA ILE B 93 -13.486 32.284 37.817 1.00 37.77 C
ANISOU 1528 CA ILE B 93 4601 5725 4025 802 -953 -2031 C
ATOM 1529 C ILE B 93 -14.665 32.791 36.975 1.00 40.02 C
ANISOU 1529 C ILE B 93 4956 5893 4356 1209 -1163 -2251 C
ATOM 1530 O ILE B 93 -14.535 33.789 36.271 1.00 42.19 O
ANISOU 1530 O ILE B 93 5668 5609 4754 1372 -1454 -2296 O
ATOM 1531 CB ILE B 93 -12.146 32.221 37.022 1.00 35.36 C
ANISOU 1531 CB ILE B 93 4612 4967 3857 452 -927 -1638 C
ATOM 1532 CG1 ILE B 93 -12.294 31.344 35.771 1.00 34.14 C
ANISOU 1532 CG1 ILE B 93 4452 4743 3778 345 -815 -1341 C
ATOM 1533 CG2 ILE B 93 -10.974 31.772 37.958 1.00 34.86 C
ANISOU 1533 CG2 ILE B 93 4418 5097 3730 132 -766 -1489 C
ATOM 1534 CD1 ILE B 93 -11.052 31.249 34.882 1.00 35.31 C
ANISOU 1534 CD1 ILE B 93 4824 4586 4005 17 -771 -1029 C
ATOM 1535 N GLY B 94 -15.809 32.103 37.054 1.00 40.80 N
ANISOU 1535 N GLY B 94 4645 6537 4319 1337 -1048 -2378 N
ATOM 1536 CA GLY B 94 -17.038 32.541 36.399 1.00 43.85 C
ANISOU 1536 CA GLY B 94 4974 6981 4705 1779 -1253 -2660 C
ATOM 1537 C GLY B 94 -17.013 32.368 34.889 1.00 43.34 C
ANISOU 1537 C GLY B 94 5203 6462 4802 1711 -1326 -2333 C
ATOM 1538 O GLY B 94 -17.604 33.163 34.130 1.00 45.33 O
ANISOU 1538 O GLY B 94 5682 6406 5133 2087 -1642 -2499 O
ATOM 1539 N CYS B 95 -16.340 31.315 34.447 1.00 39.64 N
ANISOU 1539 N CYS B 95 4742 5955 4364 1254 -1066 -1889 N
ATOM 1540 CA CYS B 95 -16.129 31.084 33.040 1.00 38.78 C
ANISOU 1540 CA CYS B 95 4904 5453 4380 1112 -1090 -1573 C
ATOM 1541 C CYS B 95 -17.348 30.393 32.438 1.00 38.85 C
ANISOU 1541 C CYS B 95 4647 5814 4301 1208 -1041 -1593 C
ATOM 1542 O CYS B 95 -17.838 29.396 32.990 1.00 37.53 O
ANISOU 1542 O CYS B 95 4102 6198 3960 1044 -821 -1587 O
ATOM 1543 CB CYS B 95 -14.856 30.254 32.828 1.00 35.32 C
ANISOU 1543 CB CYS B 95 4552 4877 3991 652 -851 -1179 C
ATOM 1544 SG CYS B 95 -14.473 30.119 31.107 1.00 37.51 S
ANISOU 1544 SG CYS B 95 5150 4731 4372 460 -878 -865 S
ATOM 1545 N THR B 96 -17.840 30.950 31.319 1.00 40.30 N
ANISOU 1545 N THR B 96 5062 5684 4566 1425 -1281 -1604 N
ATOM 1546 CA THR B 96 -19.014 30.430 30.601 1.00 40.56 C
ANISOU 1546 CA THR B 96 4865 6033 4513 1533 -1284 -1632 C
ATOM 1547 C THR B 96 -18.740 30.198 29.112 1.00 39.28 C
ANISOU 1547 C THR B 96 5034 5440 4451 1323 -1314 -1282 C
ATOM 1548 O THR B 96 -17.894 30.868 28.513 1.00 39.30 O
ANISOU 1548 O THR B 96 5487 4870 4575 1227 -1465 -1119 O
ATOM 1549 CB THR B 96 -20.246 31.379 30.727 1.00 45.40 C
ANISOU 1549 CB THR B 96 5324 6856 5071 2147 -1620 -2113 C
ATOM 1550 OG1 THR B 96 -20.004 32.587 29.995 1.00 46.93 O
ANISOU 1550 OG1 THR B 96 6067 6332 5434 2430 -2038 -2135 O
ATOM 1551 CG2 THR B 96 -20.539 31.711 32.174 1.00 47.11 C
ANISOU 1551 CG2 THR B 96 5184 7563 5151 2393 -1602 -2547 C
ATOM 1552 N LEU B 97 -19.433 29.221 28.530 1.00 38.08 N
ANISOU 1552 N LEU B 97 4662 5608 4201 1178 -1166 -1163 N
ATOM 1553 CA LEU B 97 -19.461 29.044 27.090 1.00 37.66 C
ANISOU 1553 CA LEU B 97 4863 5248 4197 1043 -1223 -911 C
ATOM 1554 C LEU B 97 -20.707 29.728 26.548 1.00 41.22 C
ANISOU 1554 C LEU B 97 5264 5787 4611 1473 -1552 -1146 C
ATOM 1555 O LEU B 97 -21.781 29.619 27.132 1.00 43.57 O
ANISOU 1555 O LEU B 97 5120 6672 4764 1735 -1568 -1454 O
ATOM 1556 CB LEU B 97 -19.551 27.571 26.730 1.00 35.20 C
ANISOU 1556 CB LEU B 97 4381 5211 3782 653 -917 -672 C
ATOM 1557 CG LEU B 97 -18.334 26.674 26.762 1.00 32.40 C
ANISOU 1557 CG LEU B 97 4156 4683 3473 263 -657 -399 C
ATOM 1558 CD1 LEU B 97 -18.830 25.225 26.635 1.00 30.10 C
ANISOU 1558 CD1 LEU B 97 3702 4709 3026 -15 -462 -267 C
ATOM 1559 CD2 LEU B 97 -17.390 27.041 25.615 1.00 30.82 C
ANISOU 1559 CD2 LEU B 97 4331 3990 3388 118 -702 -199 C
ATOM 1560 N ASN B 98 -20.569 30.424 25.431 1.00 43.09 N
ANISOU 1560 N ASN B 98 5938 5495 4939 1529 -1834 -1012 N
ATOM 1561 CA ASN B 98 -21.705 31.097 24.793 1.00 47.73 C
ANISOU 1561 CA ASN B 98 6554 6081 5500 1980 -2232 -1209 C
ATOM 1562 C ASN B 98 -21.663 30.961 23.273 1.00 47.19 C
ANISOU 1562 C ASN B 98 6826 5671 5434 1726 -2330 -874 C
ATOM 1563 O ASN B 98 -20.609 31.052 22.663 1.00 45.03 O
ANISOU 1563 O ASN B 98 6974 4924 5210 1327 -2287 -561 O
ATOM 1564 CB ASN B 98 -21.775 32.580 25.219 1.00 52.44 C
ANISOU 1564 CB ASN B 98 7459 6278 6186 2523 -2723 -1524 C
ATOM 1565 CG ASN B 98 -23.077 33.288 24.777 1.00 60.09 C
ANISOU 1565 CG ASN B 98 8387 7324 7122 3178 -3214 -1855 C
ATOM 1566 OD1 ASN B 98 -23.572 33.100 23.660 1.00 63.84 O
ANISOU 1566 OD1 ASN B 98 8948 7750 7560 3137 -3343 -1683 O
ATOM 1567 ND2 ASN B 98 -23.609 34.147 25.655 1.00 65.94 N
ANISOU 1567 ND2 ASN B 98 9006 8183 7866 3829 -3528 -2366 N
ATOM 1568 N PHE B 99 -22.833 30.742 22.679 1.00 49.21 N
ANISOU 1568 N PHE B 99 6851 6254 5591 1935 -2458 -968 N
ATOM 1569 CA PHE B 99 -22.993 30.689 21.231 1.00 50.03 C
ANISOU 1569 CA PHE B 99 7256 6087 5665 1751 -2609 -693 C
ATOM 1570 C PHE B 99 -24.469 30.932 20.865 1.00 54.35 C
ANISOU 1570 C PHE B 99 7533 7003 6116 2246 -2941 -956 C
ATOM 1571 O PHE B 99 -24.869 31.012 19.690 1.00 55.61 O
ANISOU 1571 O PHE B 99 7903 6999 6228 2212 -3166 -790 O
ATOM 1572 CB PHE B 99 -22.486 29.354 20.672 1.00 45.56 C
ANISOU 1572 CB PHE B 99 6610 5670 5030 1121 -2137 -357 C
ATOM 1573 CG PHE B 99 -23.331 28.174 21.063 1.00 45.74 C
ANISOU 1573 CG PHE B 99 6076 6403 4901 1033 -1837 -456 C
ATOM 1574 CD1 PHE B 99 -23.155 27.555 22.300 1.00 43.63 C
ANISOU 1574 CD1 PHE B 99 5477 6508 4592 937 -1538 -568 C
ATOM 1575 CD2 PHE B 99 -24.308 27.680 20.191 1.00 46.91 C
ANISOU 1575 CD2 PHE B 99 6064 6859 4900 977 -1880 -416 C
ATOM 1576 CE1 PHE B 99 -23.938 26.480 22.668 1.00 44.08 C
ANISOU 1576 CE1 PHE B 99 5099 7211 4436 737 -1308 -621 C
ATOM 1577 CE2 PHE B 99 -25.105 26.593 20.557 1.00 47.45 C
ANISOU 1577 CE2 PHE B 99 5656 7611 4762 786 -1627 -491 C
ATOM 1578 CZ PHE B 99 -24.922 25.991 21.788 1.00 44.04 C
ANISOU 1578 CZ PHE B 99 4945 7526 4263 636 -1350 -582 C
ATOM 1579 OXT PHE B 99 -25.314 31.070 21.761 1.00 56.77 O
ANISOU 1579 OXT PHE B 99 7358 7854 6358 2707 -3002 -1377 O
TER 1580 PHE B 99
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elNémo
is maintained by Yves-Henri Sanejouand.
It was developed
by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.
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