From b1ba556871db4e260f032d06273db77e23d14935 Mon Sep 17 00:00:00 2001 From: David Juergens Date: Fri, 20 Jun 2025 09:17:16 -0700 Subject: [PATCH] add .sh examples, gabarap pdb, import numpy --- examples/design_macrocyclic_binder.sh | 19 + examples/design_macrocyclic_monomer.sh | 17 + examples/input_pdbs/7zkr_GABARAP.pdb | 2628 ++++++++++++++++++++++++ rfdiffusion/Embeddings.py | 1 + rfdiffusion/util_module.py | 2 +- 5 files changed, 2666 insertions(+), 1 deletion(-) create mode 100755 examples/design_macrocyclic_binder.sh create mode 100755 examples/design_macrocyclic_monomer.sh create mode 100644 examples/input_pdbs/7zkr_GABARAP.pdb diff --git a/examples/design_macrocyclic_binder.sh b/examples/design_macrocyclic_binder.sh new file mode 100755 index 0000000..c0c69f0 --- /dev/null +++ b/examples/design_macrocyclic_binder.sh @@ -0,0 +1,19 @@ +#!/bin/bash + +prefix=./outputs/diffused_binder_cyclic2 + +# Note that the indices in this pdb file have been +# shifted by +2 in chain A relative to pdbID 7zkr. +pdb='./input_pdbs/7zkr_GABARAP.pdb' + +num_designs=10 +script="../scripts/run_inference.py" +$script --config-name base \ +inference.output_prefix=$prefix \ +inference.num_designs=$num_designs \ +'contigmap.contigs=[12-18 A3-117/0]' \ +inference.input_pdb=$pdb \ +inference.cyclic=True \ +diffuser.T=50 \ +inference.cyc_chains='a' \ +ppi.hotspot_res=[\'A51\',\'A52\',\'A50\',\'A48\',\'A62\',\'A65\'] \ diff --git a/examples/design_macrocyclic_monomer.sh b/examples/design_macrocyclic_monomer.sh new file mode 100755 index 0000000..96eda60 --- /dev/null +++ b/examples/design_macrocyclic_monomer.sh @@ -0,0 +1,17 @@ +#!/bin/bash + +prefix=./outputs/uncond_cycpep +# Note that the indices in this pdb file have been +# shifted by +2 in chain A relative to pdbID 7zkr. +pdb='./input_pdbs/7zkr_GABARAP.pdb' + +num_designs=10 +script="../scripts/run_inference.py" +$script --config-name base \ +inference.output_prefix=$prefix \ +inference.num_designs=$num_designs \ +'contigmap.contigs=[12-18]' \ +inference.input_pdb=$pdb \ +inference.cyclic=True \ +diffuser.T=50 \ +inference.cyc_chains='a' diff --git a/examples/input_pdbs/7zkr_GABARAP.pdb b/examples/input_pdbs/7zkr_GABARAP.pdb new file mode 100644 index 0000000..a53143a --- /dev/null +++ b/examples/input_pdbs/7zkr_GABARAP.pdb @@ -0,0 +1,2628 @@ +CRYST1 99.030 99.030 99.030 90.00 90.00 90.00 I 2 3 24 +ATOM 1 N AMET A 3 -31.883 -45.522 2.304 0.61 35.86 A N +ANISOU 1 N AMET A 3 5093 4593 3939 -144 285 397 A N +ATOM 2 N BMET A 3 -31.896 -45.710 2.124 0.39 35.31 A N +ANISOU 2 N BMET A 3 5004 4403 4008 -56 310 184 A N +ATOM 3 CA AMET A 3 -31.011 -45.197 3.427 0.61 34.83 A C +ANISOU 3 CA AMET A 3 4968 4470 3794 -103 376 344 A C +ATOM 4 CA BMET A 3 -31.088 -45.398 3.297 0.39 34.76 A C +ANISOU 4 CA BMET A 3 4941 4335 3932 -11 338 140 A C +ATOM 5 C AMET A 3 -31.542 -45.800 4.728 0.61 33.69 A C +ANISOU 5 C AMET A 3 4916 4248 3638 48 481 6 A C +ATOM 6 C BMET A 3 -31.655 -46.083 4.532 0.39 33.35 A C +ANISOU 6 C BMET A 3 4846 4112 3714 90 499 -95 A C +ATOM 7 O AMET A 3 -32.614 -45.424 5.205 0.61 35.36 A O +ANISOU 7 O AMET A 3 5152 4392 3893 103 441 65 A O +ATOM 8 O BMET A 3 -32.857 -46.019 4.790 0.39 34.52 A O +ANISOU 8 O BMET A 3 4946 4199 3972 62 490 79 A O +ATOM 9 CB AMET A 3 -30.855 -43.678 3.571 0.61 34.20 A C +ANISOU 9 CB AMET A 3 4738 4568 3691 -120 385 669 A C +ATOM 10 CB BMET A 3 -31.045 -43.890 3.533 0.39 35.17 A C +ANISOU 10 CB BMET A 3 4909 4470 3984 22 240 322 A C +ATOM 11 CG AMET A 3 -30.760 -42.927 2.247 0.61 33.33 A C +ANISOU 11 CG AMET A 3 4356 4807 3503 -30 435 852 A C +ATOM 12 CG BMET A 3 -31.205 -43.055 2.281 0.39 35.24 A C +ANISOU 12 CG BMET A 3 4822 4634 3936 115 156 403 A C +ATOM 13 SD AMET A 3 -29.715 -41.450 2.295 0.61 31.81 A S +ANISOU 13 SD AMET A 3 3824 5017 3244 58 627 1088 A S +ATOM 14 SD BMET A 3 -31.003 -41.303 2.640 0.39 34.59 A S +ANISOU 14 SD BMET A 3 4678 4701 3762 258 114 415 A S +ATOM 15 CE AMET A 3 -30.242 -40.673 3.816 0.61 31.50 A C +ANISOU 15 CE AMET A 3 3754 4986 3229 -114 628 1156 A C +ATOM 16 CE BMET A 3 -29.239 -41.220 2.909 0.39 34.83 A C +ANISOU 16 CE BMET A 3 4616 4767 3850 81 164 382 A C +ATOM 17 N LYS A 4 -30.786 -46.735 5.296 1.00 30.72 A N +ANISOU 17 N LYS A 4 4643 3812 3218 149 556 -513 A N +ATOM 18 CA LYS A 4 -31.172 -47.413 6.528 1.00 27.20 A C +ANISOU 18 CA LYS A 4 4245 3179 2911 221 449 -747 A C +ATOM 19 C LYS A 4 -30.637 -46.627 7.718 1.00 23.07 A C +ANISOU 19 C LYS A 4 3371 2901 2491 226 283 -711 A C +ATOM 20 O LYS A 4 -29.420 -46.468 7.869 1.00 26.59 A O +ANISOU 20 O LYS A 4 3417 3654 3033 325 389 -800 A O +ATOM 21 CB LYS A 4 -30.618 -48.837 6.549 1.00 29.66 A C +ANISOU 21 CB LYS A 4 4655 3191 3423 510 493 -643 A C +ATOM 22 CG LYS A 4 -30.939 -49.609 7.820 1.00 31.56 A C +ANISOU 22 CG LYS A 4 4935 3328 3727 534 421 -420 A C +ATOM 23 N PHE A 5 -31.540 -46.136 8.558 1.00 16.20 A N +ANISOU 23 N PHE A 5 2605 1645 1904 212 227 -232 A N +ATOM 24 CA PHE A 5 -31.152 -45.413 9.760 1.00 13.51 A C +ANISOU 24 CA PHE A 5 1964 1355 1815 226 174 -132 A C +ATOM 25 C PHE A 5 -31.314 -46.311 10.979 1.00 13.58 A C +ANISOU 25 C PHE A 5 1771 1389 1999 20 149 -33 A C +ATOM 26 O PHE A 5 -32.410 -46.820 11.250 1.00 14.37 A O +ANISOU 26 O PHE A 5 1718 1704 2038 -20 -44 -44 A O +ATOM 27 CB PHE A 5 -31.944 -44.118 9.905 1.00 13.90 A C +ANISOU 27 CB PHE A 5 1868 1484 1929 225 76 -38 A C +ATOM 28 CG PHE A 5 -31.464 -43.021 9.001 1.00 13.42 A C +ANISOU 28 CG PHE A 5 1748 1477 1874 317 63 -141 A C +ATOM 29 CD1 PHE A 5 -31.821 -42.996 7.661 1.00 14.97 A C +ANISOU 29 CD1 PHE A 5 2246 1611 1832 95 43 -118 A C +ATOM 30 CD2 PHE A 5 -30.630 -42.025 9.489 1.00 13.45 A C +ANISOU 30 CD2 PHE A 5 1662 1397 2050 349 -147 -136 A C +ATOM 31 CE1 PHE A 5 -31.367 -41.981 6.835 1.00 16.46 A C +ANISOU 31 CE1 PHE A 5 2482 1827 1945 212 25 -0 A C +ATOM 32 CE2 PHE A 5 -30.177 -41.004 8.668 1.00 13.92 A C +ANISOU 32 CE2 PHE A 5 1605 1468 2215 305 -74 130 A C +ATOM 33 CZ PHE A 5 -30.536 -40.988 7.340 1.00 15.06 A C +ANISOU 33 CZ PHE A 5 1988 1616 2120 312 88 174 A C +ATOM 34 N VAL A 6 -30.211 -46.508 11.703 1.00 13.38 A N +ANISOU 34 N VAL A 6 1774 1434 1875 245 24 65 A N +ATOM 35 CA VAL A 6 -30.229 -47.294 12.931 1.00 14.06 A C +ANISOU 35 CA VAL A 6 1746 1664 1933 256 -49 398 A C +ATOM 36 C VAL A 6 -31.199 -46.702 13.948 1.00 13.74 A C +ANISOU 36 C VAL A 6 1558 1606 2056 202 -24 449 A C +ATOM 37 O VAL A 6 -31.793 -47.434 14.751 1.00 15.03 A O +ANISOU 37 O VAL A 6 1568 1881 2261 -20 140 439 A O +ATOM 38 CB VAL A 6 -28.791 -47.395 13.477 1.00 15.31 A C +ANISOU 38 CB VAL A 6 1740 1855 2221 346 -32 298 A C +ATOM 39 CG1 VAL A 6 -28.772 -48.026 14.858 1.00 16.75 A C +ANISOU 39 CG1 VAL A 6 2016 2193 2155 283 -122 516 A C +ATOM 40 CG2 VAL A 6 -27.912 -48.177 12.507 1.00 16.59 A C +ANISOU 40 CG2 VAL A 6 1867 1843 2592 464 336 10 A C +ATOM 41 N TYR A 7 -31.387 -45.380 13.923 1.00 13.58 A N +ANISOU 41 N TYR A 7 1595 1652 1912 173 35 151 A N +ATOM 42 CA TYR A 7 -32.300 -44.729 14.859 1.00 13.92 A C +ANISOU 42 CA TYR A 7 1619 1698 1972 84 176 63 A C +ATOM 43 C TYR A 7 -33.685 -45.367 14.840 1.00 14.05 A C +ANISOU 43 C TYR A 7 1573 1725 2040 27 162 -32 A C +ATOM 44 O TYR A 7 -34.331 -45.497 15.885 1.00 15.56 A O +ANISOU 44 O TYR A 7 1878 1821 2214 -126 503 -196 A O +ATOM 45 CB TYR A 7 -32.404 -43.238 14.532 1.00 13.81 A C +ANISOU 45 CB TYR A 7 1701 1616 1929 56 70 139 A C +ATOM 46 CG TYR A 7 -33.169 -42.471 15.580 1.00 13.37 A C +ANISOU 46 CG TYR A 7 1675 1541 1863 66 28 127 A C +ATOM 47 CD1 TYR A 7 -32.554 -42.081 16.766 1.00 13.80 A C +ANISOU 47 CD1 TYR A 7 1775 1770 1697 65 -82 -57 A C +ATOM 48 CD2 TYR A 7 -34.513 -42.157 15.400 1.00 13.35 A C +ANISOU 48 CD2 TYR A 7 1500 1614 1957 14 93 109 A C +ATOM 49 CE1 TYR A 7 -33.247 -41.400 17.734 1.00 14.98 A C +ANISOU 49 CE1 TYR A 7 1892 1905 1895 163 -148 -117 A C +ATOM 50 CE2 TYR A 7 -35.219 -41.476 16.368 1.00 14.32 A C +ANISOU 50 CE2 TYR A 7 1566 1781 2094 37 -156 -78 A C +ATOM 51 CZ TYR A 7 -34.578 -41.099 17.534 1.00 14.74 A C +ANISOU 51 CZ TYR A 7 1721 1877 2002 119 62 -49 A C +ATOM 52 OH TYR A 7 -35.262 -40.422 18.518 1.00 16.24 A O +ANISOU 52 OH TYR A 7 1960 2087 2125 122 267 -319 A O +ATOM 53 N LYS A 8 -34.158 -45.780 13.663 1.00 15.42 A N +ANISOU 53 N LYS A 8 1474 1924 2462 -12 -81 -202 A N +ATOM 54 CA LYS A 8 -35.496 -46.359 13.584 1.00 17.79 A C +ANISOU 54 CA LYS A 8 1537 2233 2991 52 -217 -351 A C +ATOM 55 C LYS A 8 -35.571 -47.729 14.238 1.00 19.62 A C +ANISOU 55 C LYS A 8 1591 2273 3591 -155 45 -290 A C +ATOM 56 O LYS A 8 -36.645 -48.133 14.702 1.00 21.31 A O +ANISOU 56 O LYS A 8 1722 2469 3906 -31 81 -268 A O +ATOM 57 CB LYS A 8 -35.954 -46.454 12.138 1.00 19.18 A C +ANISOU 57 CB LYS A 8 1920 2570 2796 251 -564 -599 A C +ATOM 58 CG LYS A 8 -36.114 -45.125 11.474 1.00 19.26 A C +ANISOU 58 CG LYS A 8 2027 2705 2584 420 -470 -745 A C +ATOM 59 CD LYS A 8 -36.784 -45.337 10.148 1.00 20.85 A C +ANISOU 59 CD LYS A 8 2597 2494 2833 376 -453 -576 A C +ATOM 60 CE LYS A 8 -37.053 -44.030 9.447 1.00 21.50 A C +ANISOU 60 CE LYS A 8 2980 2233 2955 444 -553 -280 A C +ATOM 61 NZ LYS A 8 -37.777 -44.269 8.160 1.00 22.69 A N +ANISOU 61 NZ LYS A 8 3154 2523 2945 137 -692 -322 A N +ATOM 62 N GLU A 9 -34.461 -48.465 14.267 1.00 20.68 A N +ANISOU 62 N GLU A 9 1884 2203 3771 128 -200 -414 A N +ATOM 63 CA GLU A 9 -34.452 -49.715 15.015 1.00 23.09 A C +ANISOU 63 CA GLU A 9 2352 2477 3943 315 -242 -179 A C +ATOM 64 C GLU A 9 -34.603 -49.437 16.499 1.00 24.20 A C +ANISOU 64 C GLU A 9 2670 2614 3909 430 -253 259 A C +ATOM 65 O GLU A 9 -35.254 -50.199 17.220 1.00 26.54 A O +ANISOU 65 O GLU A 9 3153 2963 3969 173 148 581 A O +ATOM 66 CB GLU A 9 -33.142 -50.465 14.778 1.00 24.92 A C +ANISOU 66 CB GLU A 9 2620 2691 4159 457 -60 -556 A C +ATOM 67 CG GLU A 9 -32.817 -50.757 13.330 1.00 28.92 A C +ANISOU 67 CG GLU A 9 3184 3258 4546 628 243 -882 A C +ATOM 68 CD GLU A 9 -31.488 -51.476 13.173 1.00 33.47 A C +ANISOU 68 CD GLU A 9 3686 4003 5029 765 361 -1041 A C +ATOM 69 OE1 GLU A 9 -30.841 -51.772 14.204 1.00 33.70 A O +ANISOU 69 OE1 GLU A 9 3558 4100 5146 967 475 -1197 A O +ATOM 70 OE2 GLU A 9 -31.088 -51.741 12.021 1.00 35.33 A O +ANISOU 70 OE2 GLU A 9 3924 4328 5172 808 443 -1205 A O +ATOM 71 N GLU A 10 -34.012 -48.340 16.964 1.00 22.92 A N +ANISOU 71 N GLU A 10 2601 2467 3639 525 -325 58 A N +ATOM 72 CA GLU A 10 -33.950 -48.018 18.379 1.00 22.68 A C +ANISOU 72 CA GLU A 10 2673 2516 3429 532 -30 389 A C +ATOM 73 C GLU A 10 -35.225 -47.367 18.904 1.00 22.90 A C +ANISOU 73 C GLU A 10 2969 2437 3297 751 33 604 A C +ATOM 74 O GLU A 10 -35.416 -47.329 20.124 1.00 24.90 A O +ANISOU 74 O GLU A 10 3488 2834 3138 672 133 1216 A O +ATOM 75 CB GLU A 10 -32.718 -47.138 18.644 1.00 22.96 A C +ANISOU 75 CB GLU A 10 2410 2679 3633 421 272 498 A C +ATOM 76 CG GLU A 10 -31.413 -47.778 18.164 1.00 23.95 A C +ANISOU 76 CG GLU A 10 2399 2740 3959 512 654 589 A C +ATOM 77 CD GLU A 10 -30.186 -46.880 18.316 1.00 26.44 A C +ANISOU 77 CD GLU A 10 2747 2938 4362 584 271 339 A C +ATOM 78 OE1 GLU A 10 -30.339 -45.638 18.335 1.00 27.92 A O +ANISOU 78 OE1 GLU A 10 2989 2873 4747 377 315 68 A O +ATOM 79 OE2 GLU A 10 -29.060 -47.423 18.404 1.00 26.94 A O +ANISOU 79 OE2 GLU A 10 3038 3091 4105 466 53 376 A O +ATOM 80 N HIS A 11 -36.111 -46.882 18.023 1.00 20.36 A N +ANISOU 80 N HIS A 11 2470 2101 3167 875 63 709 A N +ATOM 81 CA HIS A 11 -37.269 -46.096 18.438 1.00 18.81 A C +ANISOU 81 CA HIS A 11 2189 1992 2965 310 160 670 A C +ATOM 82 C HIS A 11 -38.463 -46.350 17.527 1.00 18.32 A C +ANISOU 82 C HIS A 11 2207 1773 2981 275 108 610 A C +ATOM 83 O HIS A 11 -38.420 -45.998 16.340 1.00 19.00 A O +ANISOU 83 O HIS A 11 2337 2104 2778 203 -126 328 A O +ATOM 84 CB HIS A 11 -36.906 -44.612 18.422 1.00 18.82 A C +ANISOU 84 CB HIS A 11 2170 2077 2905 263 126 515 A C +ATOM 85 CG HIS A 11 -35.705 -44.289 19.250 1.00 20.12 A C +ANISOU 85 CG HIS A 11 2480 2388 2779 218 -135 531 A C +ATOM 86 CD2 HIS A 11 -34.400 -44.167 18.915 1.00 21.64 A C +ANISOU 86 CD2 HIS A 11 2582 2725 2915 -14 -347 610 A C +ATOM 87 ND1 HIS A 11 -35.771 -44.095 20.614 1.00 23.32 A N +ANISOU 87 ND1 HIS A 11 3049 2745 3067 -17 -136 203 A N +ATOM 88 CE1 HIS A 11 -34.559 -43.851 21.079 1.00 24.28 A C +ANISOU 88 CE1 HIS A 11 3112 2867 3246 -153 -412 322 A C +ATOM 89 NE2 HIS A 11 -33.709 -43.888 20.069 1.00 22.85 A N +ANISOU 89 NE2 HIS A 11 2839 2769 3075 -275 -456 401 A N +ATOM 90 N PRO A 12 -39.547 -46.932 18.042 1.00 20.11 A N +ANISOU 90 N PRO A 12 2270 1860 3511 -65 163 599 A N +ATOM 91 CA PRO A 12 -40.686 -47.259 17.179 1.00 20.86 A C +ANISOU 91 CA PRO A 12 2321 1831 3773 -124 48 413 A C +ATOM 92 C PRO A 12 -41.357 -46.013 16.630 1.00 18.50 A C +ANISOU 92 C PRO A 12 1987 1484 3556 26 426 162 A C +ATOM 93 O PRO A 12 -41.307 -44.934 17.229 1.00 17.99 A O +ANISOU 93 O PRO A 12 1925 1563 3348 52 334 291 A O +ATOM 94 CB PRO A 12 -41.631 -48.028 18.111 1.00 23.01 A C +ANISOU 94 CB PRO A 12 2507 2275 3961 -423 -110 503 A C +ATOM 95 CG PRO A 12 -41.262 -47.592 19.474 1.00 23.93 A C +ANISOU 95 CG PRO A 12 2617 2583 3893 -477 158 403 A C +ATOM 96 CD PRO A 12 -39.780 -47.337 19.439 1.00 21.88 A C +ANISOU 96 CD PRO A 12 2398 2247 3668 -373 430 694 A C +ATOM 97 N PHE A 13 -42.013 -46.197 15.480 1.00 18.71 A N +ANISOU 97 N PHE A 13 1977 1462 3670 -90 369 -6 A N +ATOM 98 CA PHE A 13 -42.589 -45.084 14.733 1.00 18.50 A C +ANISOU 98 CA PHE A 13 1976 1544 3510 -112 -26 -170 A C +ATOM 99 C PHE A 13 -43.473 -44.199 15.603 1.00 16.83 A C +ANISOU 99 C PHE A 13 1655 1400 3341 -211 17 -2 A C +ATOM 100 O PHE A 13 -43.370 -42.971 15.556 1.00 16.46 A O +ANISOU 100 O PHE A 13 1755 1416 3083 -262 135 33 A O +ATOM 101 CB PHE A 13 -43.388 -45.600 13.534 1.00 19.07 A C +ANISOU 101 CB PHE A 13 1967 1715 3564 -104 -139 -292 A C +ATOM 102 CG PHE A 13 -44.177 -44.526 12.841 1.00 18.88 A C +ANISOU 102 CG PHE A 13 1770 1770 3634 -275 -212 -291 A C +ATOM 103 CD1 PHE A 13 -43.560 -43.665 11.949 1.00 19.09 A C +ANISOU 103 CD1 PHE A 13 1850 1838 3566 -362 -95 -161 A C +ATOM 104 CD2 PHE A 13 -45.529 -44.359 13.101 1.00 20.08 A C +ANISOU 104 CD2 PHE A 13 1713 2038 3879 -214 -175 -27 A C +ATOM 105 CE1 PHE A 13 -44.277 -42.662 11.321 1.00 20.90 A C +ANISOU 105 CE1 PHE A 13 2020 2193 3728 -255 -94 -106 A C +ATOM 106 CE2 PHE A 13 -46.253 -43.357 12.476 1.00 21.12 A C +ANISOU 106 CE2 PHE A 13 1773 2311 3941 -214 -121 62 A C +ATOM 107 CZ PHE A 13 -45.626 -42.507 11.582 1.00 21.64 A C +ANISOU 107 CZ PHE A 13 2032 2282 3909 -256 -227 -62 A C +ATOM 108 N GLU A 14 -44.376 -44.799 16.379 1.00 17.84 A N +ANISOU 108 N GLU A 14 1820 1482 3478 -237 279 125 A N +ATOM 109 CA GLU A 14 -45.324 -43.975 17.125 1.00 19.32 A C +ANISOU 109 CA GLU A 14 1949 1840 3553 -246 586 305 A C +ATOM 110 C GLU A 14 -44.624 -43.114 18.168 1.00 18.88 A C +ANISOU 110 C GLU A 14 2125 1801 3248 -242 566 352 A C +ATOM 111 O GLU A 14 -45.042 -41.976 18.418 1.00 19.61 A O +ANISOU 111 O GLU A 14 2253 1785 3414 -42 725 334 A O +ATOM 112 CB GLU A 14 -46.435 -44.821 17.748 1.00 22.43 A C +ANISOU 112 CB GLU A 14 2178 2160 4183 -33 557 266 A C +ATOM 113 CG GLU A 14 -47.415 -44.016 18.610 1.00 24.62 A C +ANISOU 113 CG GLU A 14 2393 2308 4655 159 596 301 A C +ATOM 114 CD GLU A 14 -48.032 -42.817 17.887 1.00 26.64 A C +ANISOU 114 CD GLU A 14 2515 2535 5070 241 676 298 A C +ATOM 115 OE1 GLU A 14 -48.159 -42.853 16.642 1.00 27.65 A O +ANISOU 115 OE1 GLU A 14 2226 2903 5376 248 488 470 A O +ATOM 116 OE2 GLU A 14 -48.395 -41.831 18.570 1.00 27.99 A O +ANISOU 116 OE2 GLU A 14 2962 2454 5218 424 802 587 A O +ATOM 117 N ALYS A 15 -43.548 -43.622 18.773 0.52 19.15 A N +ANISOU 117 N ALYS A 15 2207 1967 3103 -366 425 338 A N +ATOM 118 N BLYS A 15 -43.562 -43.638 18.786 0.48 18.81 A N +ANISOU 118 N BLYS A 15 2242 1914 2991 -286 479 492 A N +ATOM 119 CA ALYS A 15 -42.804 -42.808 19.728 0.52 19.12 A C +ANISOU 119 CA ALYS A 15 2345 2015 2906 -287 243 286 A C +ATOM 120 CA BLYS A 15 -42.782 -42.833 19.720 0.48 18.28 A C +ANISOU 120 CA BLYS A 15 2379 1885 2681 -92 363 613 A C +ATOM 121 C ALYS A 15 -42.067 -41.672 19.028 0.52 17.12 A C +ANISOU 121 C ALYS A 15 2203 1770 2533 -133 364 249 A C +ATOM 122 C BLYS A 15 -42.116 -41.667 19.002 0.48 16.50 A C +ANISOU 122 C BLYS A 15 2237 1680 2354 49 459 465 A C +ATOM 123 O ALYS A 15 -42.009 -40.552 19.550 0.52 17.96 A O +ANISOU 123 O ALYS A 15 2353 1887 2582 -332 506 124 A O +ATOM 124 O BLYS A 15 -42.154 -40.527 19.479 0.48 17.01 A O +ANISOU 124 O BLYS A 15 2401 1778 2283 56 655 398 A O +ATOM 125 CB ALYS A 15 -41.847 -43.677 20.544 0.52 21.38 A C +ANISOU 125 CB ALYS A 15 2725 2264 3133 -319 69 391 A C +ATOM 126 CB BLYS A 15 -41.737 -43.703 20.420 0.48 19.43 A C +ANISOU 126 CB BLYS A 15 2744 1902 2737 -1 322 1026 A C +ATOM 127 CG ALYS A 15 -42.552 -44.656 21.473 0.52 24.30 A C +ANISOU 127 CG ALYS A 15 3118 2691 3422 -249 14 269 A C +ATOM 128 CG BLYS A 15 -42.317 -44.734 21.373 0.48 21.80 A C +ANISOU 128 CG BLYS A 15 3099 2277 2907 106 486 905 A C +ATOM 129 CD ALYS A 15 -41.566 -45.368 22.384 0.52 25.32 A C +ANISOU 129 CD ALYS A 15 3239 2912 3468 -304 -32 294 A C +ATOM 130 CD BLYS A 15 -43.025 -44.069 22.541 0.48 22.38 A C +ANISOU 130 CD BLYS A 15 3232 2489 2780 5 771 1002 A C +ATOM 131 N ARG A 16 -41.504 -41.938 17.846 1.00 15.23 A N +ANISOU 131 N ARG A 16 1946 1521 2320 83 191 335 A N +ATOM 132 CA ARG A 16 -40.866 -40.873 17.076 1.00 13.66 A C +ANISOU 132 CA ARG A 16 1669 1287 2235 52 256 209 A C +ATOM 133 C ARG A 16 -41.884 -39.821 16.666 1.00 13.36 A C +ANISOU 133 C ARG A 16 1475 1459 2142 -43 378 98 A C +ATOM 134 O ARG A 16 -41.649 -38.618 16.820 1.00 12.92 A O +ANISOU 134 O ARG A 16 1467 1446 1994 -28 195 19 A O +ATOM 135 CB ARG A 16 -40.189 -41.443 15.826 1.00 13.94 A C +ANISOU 135 CB ARG A 16 1552 1522 2222 192 182 -55 A C +ATOM 136 CG ARG A 16 -39.149 -42.522 16.097 1.00 14.86 A C +ANISOU 136 CG ARG A 16 1706 1499 2441 159 342 -119 A C +ATOM 137 CD ARG A 16 -38.321 -42.869 14.859 1.00 14.90 A C +ANISOU 137 CD ARG A 16 1664 1463 2535 18 11 -291 A C +ATOM 138 NE ARG A 16 -39.101 -43.072 13.639 1.00 16.16 A N +ANISOU 138 NE ARG A 16 1796 1669 2673 -131 80 -140 A N +ATOM 139 CZ ARG A 16 -39.382 -44.251 13.098 1.00 16.21 A C +ANISOU 139 CZ ARG A 16 1790 1678 2690 -96 50 -86 A C +ATOM 140 NH1 ARG A 16 -39.078 -45.390 13.707 1.00 17.93 A N +ANISOU 140 NH1 ARG A 16 2124 1793 2897 -34 345 -70 A N +ATOM 141 NH2 ARG A 16 -39.965 -44.291 11.903 1.00 18.54 A N +ANISOU 141 NH2 ARG A 16 1979 2243 2823 -159 82 -66 A N +ATOM 142 N ARG A 17 -43.023 -40.265 16.132 1.00 13.78 A N +ANISOU 142 N ARG A 17 1468 1408 2359 -85 303 33 A N +ATOM 143 CA ARG A 17 -44.028 -39.340 15.626 1.00 13.40 A C +ANISOU 143 CA ARG A 17 1365 1492 2235 -16 202 -182 A C +ATOM 144 C ARG A 17 -44.561 -38.448 16.736 1.00 13.56 A C +ANISOU 144 C ARG A 17 1357 1542 2254 -38 247 142 A C +ATOM 145 O ARG A 17 -44.716 -37.235 16.546 1.00 13.85 A O +ANISOU 145 O ARG A 17 1436 1592 2234 55 284 75 A O +ATOM 146 CB ARG A 17 -45.164 -40.127 14.976 1.00 14.86 A C +ANISOU 146 CB ARG A 17 1399 1694 2554 -126 75 -68 A C +ATOM 147 CG ARG A 17 -46.211 -39.269 14.290 1.00 15.94 A C +ANISOU 147 CG ARG A 17 1390 1863 2803 -47 247 -31 A C +ATOM 148 CD ARG A 17 -47.569 -39.960 14.323 1.00 19.05 A C +ANISOU 148 CD ARG A 17 1788 2095 3354 -51 204 -144 A C +ATOM 149 NE ARG A 17 -48.066 -40.056 15.691 1.00 19.69 A N +ANISOU 149 NE ARG A 17 1607 2163 3712 81 268 -24 A N +ATOM 150 CZ ARG A 17 -48.580 -39.038 16.368 1.00 20.41 A C +ANISOU 150 CZ ARG A 17 1865 2328 3564 479 388 280 A C +ATOM 151 NH1 ARG A 17 -48.750 -37.848 15.809 1.00 20.20 A N +ANISOU 151 NH1 ARG A 17 1775 2463 3435 447 344 351 A N +ATOM 152 NH2 ARG A 17 -48.921 -39.213 17.641 1.00 22.79 A N +ANISOU 152 NH2 ARG A 17 2192 2747 3719 517 609 478 A N +ATOM 153 N ASER A 18 -44.861 -39.034 17.898 0.52 14.56 A N +ANISOU 153 N ASER A 18 1631 1602 2297 22 445 248 A N +ATOM 154 N BSER A 18 -44.855 -39.034 17.902 0.37 14.02 A N +ANISOU 154 N BSER A 18 1476 1551 2302 4 340 184 A N +ATOM 155 N CSER A 18 -44.840 -39.025 17.908 0.11 13.76 A N +ANISOU 155 N CSER A 18 1404 1607 2216 4 162 134 A N +ATOM 156 CA ASER A 18 -45.352 -38.238 19.017 0.52 16.00 A C +ANISOU 156 CA ASER A 18 1870 1829 2380 -171 602 161 A C +ATOM 157 CA BSER A 18 -45.353 -38.244 19.024 0.37 14.86 A C +ANISOU 157 CA BSER A 18 1621 1667 2358 -174 445 101 A C +ATOM 158 CA CSER A 18 -45.363 -38.226 19.012 0.11 14.20 A C +ANISOU 158 CA CSER A 18 1507 1710 2178 -5 91 82 A C +ATOM 159 C ASER A 18 -44.330 -37.189 19.427 0.52 14.52 A C +ANISOU 159 C ASER A 18 1697 1674 2146 90 410 33 A C +ATOM 160 C BSER A 18 -44.334 -37.198 19.448 0.37 14.34 A C +ANISOU 160 C BSER A 18 1581 1628 2238 75 328 7 A C +ATOM 161 C CSER A 18 -44.338 -37.205 19.491 0.11 14.19 A C +ANISOU 161 C CSER A 18 1524 1696 2170 97 181 86 A C +ATOM 162 O ASER A 18 -44.678 -36.025 19.654 0.52 14.61 A O +ANISOU 162 O ASER A 18 1712 1747 2092 194 401 105 A O +ATOM 163 O BSER A 18 -44.688 -36.044 19.715 0.37 14.94 A O +ANISOU 163 O BSER A 18 1603 1714 2359 176 302 -1 A O +ATOM 164 O CSER A 18 -44.695 -36.076 19.846 0.11 14.67 A O +ANISOU 164 O CSER A 18 1547 1747 2279 157 152 70 A O +ATOM 165 CB ASER A 18 -45.688 -39.149 20.199 0.52 18.61 A C +ANISOU 165 CB ASER A 18 2264 2122 2684 -179 677 257 A C +ATOM 166 CB BSER A 18 -45.696 -39.162 20.199 0.37 15.88 A C +ANISOU 166 CB BSER A 18 1762 1761 2509 -262 495 171 A C +ATOM 167 CB CSER A 18 -45.804 -39.134 20.159 0.11 14.40 A C +ANISOU 167 CB CSER A 18 1552 1785 2134 37 -161 71 A C +ATOM 168 OG ASER A 18 -46.084 -38.388 21.326 0.52 20.92 A O +ANISOU 168 OG ASER A 18 2539 2503 2905 34 661 329 A O +ATOM 169 OG BSER A 18 -46.765 -40.034 19.877 0.37 16.65 A O +ANISOU 169 OG BSER A 18 1770 1964 2592 -190 475 195 A O +ATOM 170 OG CSER A 18 -44.707 -39.856 20.689 0.11 14.37 A O +ANISOU 170 OG CSER A 18 1515 1865 2078 122 -370 39 A O +ATOM 171 N GLU A 19 -43.058 -37.583 19.504 1.00 13.80 A N +ANISOU 171 N GLU A 19 1518 1651 2076 91 304 176 A N +ATOM 172 CA GLU A 19 -42.012 -36.642 19.880 1.00 13.53 A C +ANISOU 172 CA GLU A 19 1496 1594 2051 10 97 256 A C +ATOM 173 C GLU A 19 -41.848 -35.548 18.832 1.00 12.00 A C +ANISOU 173 C GLU A 19 1258 1509 1794 114 138 -39 A C +ATOM 174 O GLU A 19 -41.645 -34.380 19.180 1.00 12.28 A O +ANISOU 174 O GLU A 19 1414 1534 1718 92 8 11 A O +ATOM 175 CB GLU A 19 -40.690 -37.384 20.074 1.00 13.61 A C +ANISOU 175 CB GLU A 19 1592 1551 2028 129 -63 193 A C +ATOM 176 CG GLU A 19 -39.543 -36.452 20.447 1.00 15.92 A C +ANISOU 176 CG GLU A 19 1762 2000 2285 284 -143 -48 A C +ATOM 177 CD GLU A 19 -38.256 -37.175 20.798 1.00 17.58 A C +ANISOU 177 CD GLU A 19 2174 2299 2208 294 -180 40 A C +ATOM 178 OE1 GLU A 19 -37.866 -38.112 20.075 1.00 21.73 A O +ANISOU 178 OE1 GLU A 19 2436 2977 2845 816 51 -150 A O +ATOM 179 OE2 GLU A 19 -37.612 -36.789 21.793 1.00 20.41 A O +ANISOU 179 OE2 GLU A 19 2508 2622 2625 445 -424 -118 A O +ATOM 180 N GLY A 20 -41.913 -35.915 17.548 1.00 11.83 A N +ANISOU 180 N GLY A 20 1186 1541 1769 107 127 60 A N +ATOM 181 CA GLY A 20 -41.746 -34.932 16.492 1.00 11.91 A C +ANISOU 181 CA GLY A 20 1326 1428 1771 44 102 117 A C +ATOM 182 C GLY A 20 -42.861 -33.907 16.469 1.00 11.60 A C +ANISOU 182 C GLY A 20 1340 1374 1693 -85 -33 136 A C +ATOM 183 O GLY A 20 -42.614 -32.716 16.265 1.00 11.61 A O +ANISOU 183 O GLY A 20 1242 1412 1758 34 4 -74 A O +ATOM 184 N GLU A 21 -44.107 -34.352 16.663 1.00 12.01 A N +ANISOU 184 N GLU A 21 1269 1479 1815 54 -70 56 A N +ATOM 185 CA GLU A 21 -45.222 -33.408 16.739 1.00 12.57 A C +ANISOU 185 CA GLU A 21 1283 1472 2022 6 -71 43 A C +ATOM 186 C GLU A 21 -45.007 -32.405 17.868 1.00 11.97 A C +ANISOU 186 C GLU A 21 1159 1396 1992 84 119 111 A C +ATOM 187 O GLU A 21 -45.156 -31.189 17.685 1.00 12.58 A O +ANISOU 187 O GLU A 21 1236 1555 1988 99 66 3 A O +ATOM 188 CB GLU A 21 -46.538 -34.161 16.950 1.00 13.63 A C +ANISOU 188 CB GLU A 21 1210 1760 2209 -141 -29 158 A C +ATOM 189 CG GLU A 21 -47.721 -33.233 17.217 1.00 14.49 A C +ANISOU 189 CG GLU A 21 1247 1812 2445 -63 151 170 A C +ATOM 190 CD GLU A 21 -49.037 -33.963 17.471 1.00 15.76 A C +ANISOU 190 CD GLU A 21 1339 1842 2808 40 202 139 A C +ATOM 191 OE1 GLU A 21 -49.027 -35.204 17.644 1.00 16.56 A O +ANISOU 191 OE1 GLU A 21 1414 1738 3141 -27 244 271 A O +ATOM 192 OE2 GLU A 21 -50.090 -33.287 17.494 1.00 16.07 A O +ANISOU 192 OE2 GLU A 21 1439 1974 2693 72 287 71 A O +ATOM 193 N LYS A 22 -44.643 -32.903 19.050 1.00 12.00 A N +ANISOU 193 N LYS A 22 1113 1619 1828 -6 52 114 A N +ATOM 194 CA LYS A 22 -44.461 -32.023 20.198 1.00 12.16 A C +ANISOU 194 CA LYS A 22 1300 1768 1552 -65 144 105 A C +ATOM 195 C LYS A 22 -43.312 -31.041 19.993 1.00 11.25 A C +ANISOU 195 C LYS A 22 1308 1444 1524 139 89 157 A C +ATOM 196 O LYS A 22 -43.413 -29.874 20.393 1.00 11.86 A O +ANISOU 196 O LYS A 22 1212 1521 1775 280 246 143 A O +ATOM 197 CB LYS A 22 -44.231 -32.854 21.457 1.00 13.76 A C +ANISOU 197 CB LYS A 22 1656 1915 1659 -94 363 285 A C +ATOM 198 CG LYS A 22 -45.439 -33.664 21.897 1.00 16.57 A C +ANISOU 198 CG LYS A 22 2384 2066 1845 -65 478 233 A C +ATOM 199 CD LYS A 22 -45.093 -34.577 23.064 1.00 22.56 A C +ANISOU 199 CD LYS A 22 3341 2794 2437 -307 644 525 A C +ATOM 200 CE LYS A 22 -46.238 -35.524 23.390 1.00 27.51 A C +ANISOU 200 CE LYS A 22 4106 3382 2965 -248 630 675 A C +ATOM 201 NZ LYS A 22 -45.828 -36.565 24.373 1.00 31.03 A N +ANISOU 201 NZ LYS A 22 4648 3795 3348 -71 586 568 A N +ATOM 202 N ILE A 23 -42.196 -31.498 19.415 1.00 10.52 A N +ANISOU 202 N ILE A 23 1253 1359 1385 187 104 49 A N +ATOM 203 CA ILE A 23 -41.028 -30.627 19.307 1.00 10.17 A C +ANISOU 203 CA ILE A 23 1190 1319 1357 141 28 144 A C +ATOM 204 C ILE A 23 -41.271 -29.520 18.289 1.00 10.02 A C +ANISOU 204 C ILE A 23 1081 1379 1347 82 28 -62 A C +ATOM 205 O ILE A 23 -40.750 -28.409 18.439 1.00 10.04 A O +ANISOU 205 O ILE A 23 1179 1373 1264 66 -35 -14 A O +ATOM 206 CB ILE A 23 -39.745 -31.440 19.020 1.00 10.56 A C +ANISOU 206 CB ILE A 23 1188 1407 1418 149 -61 -6 A C +ATOM 207 CG1 ILE A 23 -38.494 -30.698 19.520 1.00 11.14 A C +ANISOU 207 CG1 ILE A 23 1253 1517 1461 -73 -144 7 A C +ATOM 208 CG2 ILE A 23 -39.612 -31.774 17.534 1.00 11.43 A C +ANISOU 208 CG2 ILE A 23 1326 1519 1498 239 -21 -176 A C +ATOM 209 CD1 ILE A 23 -38.357 -30.664 21.029 1.00 11.67 A C +ANISOU 209 CD1 ILE A 23 1547 1518 1368 85 -152 63 A C +ATOM 210 N ARG A 24 -42.070 -29.792 17.248 1.00 10.13 A N +ANISOU 210 N ARG A 24 1067 1417 1363 193 50 -15 A N +ATOM 211 CA ARG A 24 -42.405 -28.756 16.276 1.00 10.91 A C +ANISOU 211 CA ARG A 24 1113 1546 1486 260 -19 7 A C +ATOM 212 C ARG A 24 -43.279 -27.680 16.906 1.00 10.23 A C +ANISOU 212 C ARG A 24 939 1499 1450 58 -12 1 A C +ATOM 213 O ARG A 24 -43.120 -26.493 16.608 1.00 11.27 A O +ANISOU 213 O ARG A 24 1174 1544 1565 80 103 65 A O +ATOM 214 CB ARG A 24 -43.091 -29.385 15.062 1.00 11.39 A C +ANISOU 214 CB ARG A 24 1161 1618 1547 33 34 -60 A C +ATOM 215 CG ARG A 24 -42.137 -30.159 14.123 1.00 12.46 A C +ANISOU 215 CG ARG A 24 1245 1910 1578 173 46 -47 A C +ATOM 216 CD ARG A 24 -41.237 -29.203 13.333 1.00 13.61 A C +ANISOU 216 CD ARG A 24 1191 2530 1452 -16 29 68 A C +ATOM 217 NE ARG A 24 -42.038 -28.375 12.445 1.00 15.27 A N +ANISOU 217 NE ARG A 24 1314 2925 1562 -408 -321 450 A N +ATOM 218 CZ ARG A 24 -41.785 -27.108 12.146 1.00 16.10 A C +ANISOU 218 CZ ARG A 24 1299 3002 1817 -385 -329 408 A C +ATOM 219 NH1 ARG A 24 -40.699 -26.491 12.587 1.00 15.84 A N +ANISOU 219 NH1 ARG A 24 1407 2633 1979 -241 -367 -14 A N +ATOM 220 NH2 ARG A 24 -42.663 -26.432 11.410 1.00 19.26 A N +ANISOU 220 NH2 ARG A 24 1777 3160 2381 -579 -731 912 A N +ATOM 221 N LYS A 25 -44.201 -28.072 17.791 1.00 10.56 A N +ANISOU 221 N LYS A 25 974 1485 1551 144 31 -41 A N +ATOM 222 CA LYS A 25 -45.023 -27.079 18.477 1.00 10.85 A C +ANISOU 222 CA LYS A 25 1049 1436 1638 135 76 -104 A C +ATOM 223 C LYS A 25 -44.210 -26.244 19.455 1.00 10.66 A C +ANISOU 223 C LYS A 25 1099 1475 1477 99 38 -35 A C +ATOM 224 O LYS A 25 -44.476 -25.048 19.629 1.00 11.54 A O +ANISOU 224 O LYS A 25 1279 1305 1801 81 -99 -126 A O +ATOM 225 CB LYS A 25 -46.153 -27.769 19.229 1.00 11.95 A C +ANISOU 225 CB LYS A 25 1162 1563 1814 -89 212 -133 A C +ATOM 226 CG LYS A 25 -47.211 -28.354 18.335 1.00 12.32 A C +ANISOU 226 CG LYS A 25 1126 1609 1946 -124 139 -158 A C +ATOM 227 CD LYS A 25 -48.185 -29.192 19.135 1.00 13.36 A C +ANISOU 227 CD LYS A 25 1257 1970 1849 -112 -37 -180 A C +ATOM 228 CE LYS A 25 -49.298 -29.678 18.254 1.00 13.94 A C +ANISOU 228 CE LYS A 25 1408 1929 1960 -365 -108 275 A C +ATOM 229 NZ LYS A 25 -50.233 -30.582 18.980 1.00 14.81 A N +ANISOU 229 NZ LYS A 25 1505 2119 2004 -263 -99 201 A N +ATOM 230 N ALYS A 26 -43.240 -26.859 20.130 0.51 10.23 A N +ANISOU 230 N ALYS A 26 1071 1434 1383 64 104 -40 A N +ATOM 231 N BLYS A 26 -43.238 -26.859 20.128 0.49 10.64 A N +ANISOU 231 N BLYS A 26 1121 1482 1438 60 110 -47 A N +ATOM 232 CA ALYS A 26 -42.468 -26.129 21.126 0.51 11.21 A C +ANISOU 232 CA ALYS A 26 1269 1694 1295 193 -102 -133 A C +ATOM 233 CA BLYS A 26 -42.464 -26.137 21.128 0.49 12.05 A C +ANISOU 233 CA BLYS A 26 1386 1759 1432 149 -39 -183 A C +ATOM 234 C ALYS A 26 -41.455 -25.201 20.470 0.51 10.58 A C +ANISOU 234 C ALYS A 26 1071 1577 1373 132 -71 -313 A C +ATOM 235 C BLYS A 26 -41.428 -25.224 20.491 0.49 11.18 A C +ANISOU 235 C BLYS A 26 1213 1609 1425 58 -63 -399 A C +ATOM 236 O ALYS A 26 -41.221 -24.089 20.957 0.51 11.70 A O +ANISOU 236 O ALYS A 26 1193 1704 1548 258 29 -312 A O +ATOM 237 O BLYS A 26 -41.150 -24.142 21.023 0.49 12.09 A O +ANISOU 237 O BLYS A 26 1383 1684 1525 88 -7 -553 A O +ATOM 238 CB ALYS A 26 -41.775 -27.113 22.071 0.51 16.79 A C +ANISOU 238 CB ALYS A 26 2025 2377 1978 299 -279 -27 A C +ATOM 239 CB BLYS A 26 -41.789 -27.127 22.080 0.49 17.15 A C +ANISOU 239 CB BLYS A 26 2064 2430 2023 272 -235 -57 A C +ATOM 240 CG ALYS A 26 -41.222 -26.480 23.341 0.51 23.29 A C +ANISOU 240 CG ALYS A 26 2927 3148 2772 209 -254 84 A C +ATOM 241 CG BLYS A 26 -41.218 -26.490 23.338 0.49 23.48 A C +ANISOU 241 CG BLYS A 26 2958 3166 2797 190 -243 76 A C +ATOM 242 CD ALYS A 26 -40.661 -27.532 24.294 0.51 27.50 A C +ANISOU 242 CD ALYS A 26 3476 3587 3385 124 -64 108 A C +ATOM 243 CD BLYS A 26 -40.831 -27.538 24.376 0.49 27.32 A C +ANISOU 243 CD BLYS A 26 3467 3584 3329 100 -122 144 A C +ATOM 244 CE ALYS A 26 -41.756 -28.329 24.979 0.51 29.50 A C +ANISOU 244 CE ALYS A 26 3715 3773 3722 74 42 -96 A C +ATOM 245 CE BLYS A 26 -40.323 -26.882 25.653 0.49 29.00 A C +ANISOU 245 CE BLYS A 26 3694 3745 3581 20 -140 8 A C +ATOM 246 NZ ALYS A 26 -42.194 -27.702 26.257 0.51 30.90 A N +ANISOU 246 NZ ALYS A 26 3937 3922 3883 15 50 -202 A N +ATOM 247 NZ BLYS A 26 -39.971 -27.881 26.703 0.49 29.41 A N +ANISOU 247 NZ BLYS A 26 3746 3775 3655 -18 -130 30 A N +ATOM 248 N TYR A 27 -40.857 -25.634 19.362 1.00 10.01 A N +ANISOU 248 N TYR A 27 1132 1356 1316 129 -45 -207 A N +ATOM 249 CA TYR A 27 -39.777 -24.902 18.706 1.00 9.64 A C +ANISOU 249 CA TYR A 27 996 1318 1348 50 12 -50 A C +ATOM 250 C TYR A 27 -40.076 -24.802 17.216 1.00 9.92 A C +ANISOU 250 C TYR A 27 1136 1303 1330 -47 -89 -180 A C +ATOM 251 O TYR A 27 -39.412 -25.452 16.394 1.00 10.26 A O +ANISOU 251 O TYR A 27 1185 1384 1330 26 -10 -209 A O +ATOM 252 CB TYR A 27 -38.438 -25.599 18.944 1.00 10.24 A C +ANISOU 252 CB TYR A 27 1052 1431 1409 193 -125 -34 A C +ATOM 253 CG TYR A 27 -38.076 -25.792 20.399 1.00 10.47 A C +ANISOU 253 CG TYR A 27 1041 1426 1512 111 -102 -131 A C +ATOM 254 CD1 TYR A 27 -37.576 -24.739 21.155 1.00 11.25 A C +ANISOU 254 CD1 TYR A 27 1330 1473 1471 7 -66 -154 A C +ATOM 255 CD2 TYR A 27 -38.236 -27.020 21.017 1.00 10.98 A C +ANISOU 255 CD2 TYR A 27 1309 1431 1432 244 73 -144 A C +ATOM 256 CE1 TYR A 27 -37.231 -24.917 22.490 1.00 12.71 A C +ANISOU 256 CE1 TYR A 27 1718 1684 1429 206 -254 -130 A C +ATOM 257 CE2 TYR A 27 -37.892 -27.206 22.343 1.00 12.26 A C +ANISOU 257 CE2 TYR A 27 1528 1729 1402 282 -40 -145 A C +ATOM 258 CZ TYR A 27 -37.386 -26.155 23.074 1.00 12.86 A C +ANISOU 258 CZ TYR A 27 1765 1863 1258 351 -264 -164 A C +ATOM 259 OH TYR A 27 -37.043 -26.326 24.398 1.00 15.11 A O +ANISOU 259 OH TYR A 27 2144 2037 1560 169 -319 -68 A O +ATOM 260 N PRO A 28 -41.056 -23.975 16.822 1.00 10.55 A N +ANISOU 260 N PRO A 28 1047 1496 1466 104 -86 -17 A N +ATOM 261 CA PRO A 28 -41.476 -23.971 15.404 1.00 11.73 A C +ANISOU 261 CA PRO A 28 1124 1718 1615 32 -276 -22 A C +ATOM 262 C PRO A 28 -40.450 -23.377 14.453 1.00 10.96 A C +ANISOU 262 C PRO A 28 1232 1561 1373 204 -253 -35 A C +ATOM 263 O PRO A 28 -40.552 -23.573 13.230 1.00 12.35 A O +ANISOU 263 O PRO A 28 1446 1684 1562 -19 -246 -7 A O +ATOM 264 CB PRO A 28 -42.777 -23.157 15.422 1.00 13.33 A C +ANISOU 264 CB PRO A 28 1214 1819 2032 147 -245 -10 A C +ATOM 265 CG PRO A 28 -42.626 -22.279 16.619 1.00 13.18 A C +ANISOU 265 CG PRO A 28 1296 1756 1955 314 44 251 A C +ATOM 266 CD PRO A 28 -41.932 -23.123 17.648 1.00 11.57 A C +ANISOU 266 CD PRO A 28 1108 1593 1696 268 161 48 A C +ATOM 267 N ASP A 29 -39.477 -22.645 14.978 1.00 10.28 A N +ANISOU 267 N ASP A 29 1116 1294 1494 220 -143 -50 A N +ATOM 268 CA ASP A 29 -38.382 -22.075 14.213 1.00 9.99 A C +ANISOU 268 CA ASP A 29 1131 1276 1390 142 -23 -34 A C +ATOM 269 C ASP A 29 -37.166 -22.991 14.181 1.00 9.44 A C +ANISOU 269 C ASP A 29 1116 1291 1178 103 -60 -62 A C +ATOM 270 O ASP A 29 -36.085 -22.560 13.769 1.00 10.14 A O +ANISOU 270 O ASP A 29 1240 1247 1365 72 17 -128 A O +ATOM 271 CB ASP A 29 -38.022 -20.687 14.762 1.00 10.76 A C +ANISOU 271 CB ASP A 29 1245 1382 1462 156 13 -119 A C +ATOM 272 CG ASP A 29 -37.747 -20.683 16.261 1.00 11.02 A C +ANISOU 272 CG ASP A 29 1245 1182 1762 172 -202 -223 A C +ATOM 273 OD1 ASP A 29 -37.843 -21.747 16.902 1.00 11.22 A O +ANISOU 273 OD1 ASP A 29 1499 1256 1509 137 -109 -231 A O +ATOM 274 OD2 ASP A 29 -37.434 -19.601 16.799 1.00 13.53 A O +ANISOU 274 OD2 ASP A 29 1719 1347 2075 146 -540 -216 A O +ATOM 275 N ARG A 30 -37.328 -24.241 14.604 1.00 9.07 A N +ANISOU 275 N ARG A 30 1064 1208 1174 90 -99 -143 A N +ATOM 276 CA ARG A 30 -36.303 -25.264 14.516 1.00 9.15 A C +ANISOU 276 CA ARG A 30 1064 1212 1199 129 -97 -194 A C +ATOM 277 C ARG A 30 -36.899 -26.494 13.853 1.00 9.06 A C +ANISOU 277 C ARG A 30 1045 1220 1177 9 -140 -100 A C +ATOM 278 O ARG A 30 -38.122 -26.661 13.797 1.00 9.88 A O +ANISOU 278 O ARG A 30 1084 1354 1315 9 -205 -150 A O +ATOM 279 CB ARG A 30 -35.768 -25.637 15.904 1.00 9.52 A C +ANISOU 279 CB ARG A 30 1187 1357 1071 38 -262 -181 A C +ATOM 280 CG ARG A 30 -35.041 -24.496 16.616 1.00 10.00 A C +ANISOU 280 CG ARG A 30 1261 1405 1134 73 -216 -229 A C +ATOM 281 CD ARG A 30 -34.587 -24.943 17.992 1.00 9.84 A C +ANISOU 281 CD ARG A 30 1180 1256 1302 95 -208 -248 A C +ATOM 282 NE ARG A 30 -33.599 -24.083 18.632 1.00 10.06 A N +ANISOU 282 NE ARG A 30 1247 1335 1239 132 -179 -341 A N +ATOM 283 CZ ARG A 30 -33.879 -23.177 19.561 1.00 10.16 A C +ANISOU 283 CZ ARG A 30 1291 1281 1287 105 -80 -290 A C +ATOM 284 NH1 ARG A 30 -35.118 -22.764 19.770 1.00 10.80 A N +ANISOU 284 NH1 ARG A 30 1121 1435 1549 147 56 -377 A N +ATOM 285 NH2 ARG A 30 -32.899 -22.710 20.331 1.00 10.69 A N +ANISOU 285 NH2 ARG A 30 1363 1332 1365 47 -248 -379 A N +ATOM 286 N VAL A 31 -36.031 -27.356 13.338 1.00 9.17 A N +ANISOU 286 N VAL A 31 1231 1119 1133 109 -174 -152 A N +ATOM 287 CA VAL A 31 -36.500 -28.626 12.792 1.00 10.80 A C +ANISOU 287 CA VAL A 31 1642 1290 1171 180 -355 -184 A C +ATOM 288 C VAL A 31 -35.731 -29.790 13.396 1.00 9.55 A C +ANISOU 288 C VAL A 31 1175 1364 1088 215 -205 -129 A C +ATOM 289 O VAL A 31 -34.501 -29.728 13.585 1.00 9.69 A O +ANISOU 289 O VAL A 31 1286 1315 1080 102 -97 -130 A O +ATOM 290 CB VAL A 31 -36.511 -28.662 11.259 1.00 12.78 A C +ANISOU 290 CB VAL A 31 1935 1495 1428 183 -380 -126 A C +ATOM 291 CG1 VAL A 31 -37.530 -27.671 10.704 1.00 13.81 A C +ANISOU 291 CG1 VAL A 31 2160 1559 1528 173 -419 -101 A C +ATOM 292 CG2 VAL A 31 -35.143 -28.400 10.743 1.00 12.23 A C +ANISOU 292 CG2 VAL A 31 1532 1528 1589 99 -341 -150 A C +ATOM 293 N PRO A 32 -36.434 -30.873 13.706 1.00 9.26 A N +ANISOU 293 N PRO A 32 1120 1193 1205 102 -120 -89 A N +ATOM 294 CA PRO A 32 -35.793 -32.032 14.320 1.00 9.42 A C +ANISOU 294 CA PRO A 32 1195 1202 1181 120 -84 -67 A C +ATOM 295 C PRO A 32 -35.192 -32.911 13.234 1.00 9.41 A C +ANISOU 295 C PRO A 32 1117 1224 1234 2 -239 37 A C +ATOM 296 O PRO A 32 -35.834 -33.194 12.219 1.00 9.79 A O +ANISOU 296 O PRO A 32 1188 1266 1267 134 -197 -174 A O +ATOM 297 CB PRO A 32 -36.958 -32.725 15.031 1.00 10.35 A C +ANISOU 297 CB PRO A 32 1256 1354 1322 88 -89 -62 A C +ATOM 298 CG PRO A 32 -38.156 -32.396 14.179 1.00 10.83 A C +ANISOU 298 CG PRO A 32 1185 1412 1519 19 -132 -199 A C +ATOM 299 CD PRO A 32 -37.907 -30.995 13.675 1.00 10.58 A C +ANISOU 299 CD PRO A 32 1098 1534 1386 73 -124 -181 A C +ATOM 300 N AVAL A 33 -33.958 -33.357 13.467 0.62 9.86 A N +ANISOU 300 N AVAL A 33 1206 1246 1293 338 -288 -251 A N +ATOM 301 N BVAL A 33 -33.940 -33.307 13.433 0.38 9.49 A N +ANISOU 301 N BVAL A 33 1152 1158 1294 -166 -57 354 A N +ATOM 302 CA AVAL A 33 -33.167 -34.060 12.464 0.62 9.95 A C +ANISOU 302 CA AVAL A 33 1244 1289 1248 419 -174 -387 A C +ATOM 303 CA BVAL A 33 -33.214 -34.087 12.444 0.38 9.98 A C +ANISOU 303 CA BVAL A 33 1407 1257 1129 -169 -11 313 A C +ATOM 304 C AVAL A 33 -32.506 -35.272 13.103 0.62 10.18 A C +ANISOU 304 C AVAL A 33 1157 1462 1250 398 -385 -374 A C +ATOM 305 C BVAL A 33 -32.560 -35.283 13.114 0.38 10.38 A C +ANISOU 305 C BVAL A 33 1462 1384 1098 -6 -113 214 A C +ATOM 306 O AVAL A 33 -31.964 -35.184 14.209 0.62 12.16 A O +ANISOU 306 O AVAL A 33 1696 1419 1506 678 -535 -579 A O +ATOM 307 O BVAL A 33 -32.110 -35.203 14.262 0.38 12.92 A O +ANISOU 307 O BVAL A 33 2010 1483 1417 171 -512 236 A O +ATOM 308 CB AVAL A 33 -32.080 -33.143 11.865 0.62 10.80 A C +ANISOU 308 CB AVAL A 33 1513 1199 1393 259 -14 -54 A C +ATOM 309 CB BVAL A 33 -32.170 -33.246 11.674 0.38 11.02 A C +ANISOU 309 CB BVAL A 33 1566 1470 1150 -276 -15 120 A C +ATOM 310 CG1AVAL A 33 -31.406 -33.821 10.686 0.62 11.91 A C +ANISOU 310 CG1AVAL A 33 1676 1285 1562 177 432 -208 A C +ATOM 311 CG1BVAL A 33 -32.841 -32.086 10.953 0.38 11.68 A C +ANISOU 311 CG1BVAL A 33 1596 1841 999 -154 -5 -55 A C +ATOM 312 CG2AVAL A 33 -32.659 -31.797 11.453 0.62 11.35 A C +ANISOU 312 CG2AVAL A 33 1667 1331 1315 101 -353 -79 A C +ATOM 313 CG2BVAL A 33 -31.081 -32.743 12.604 0.38 11.21 A C +ANISOU 313 CG2BVAL A 33 1515 1655 1089 -333 -191 2 A C +ATOM 314 N ILE A 34 -32.515 -36.392 12.386 1.00 9.70 A N +ANISOU 314 N ILE A 34 1231 1298 1157 226 -164 -122 A N +ATOM 315 CA ILE A 34 -31.722 -37.560 12.740 1.00 9.97 A C +ANISOU 315 CA ILE A 34 1300 1251 1236 273 -154 -22 A C +ATOM 316 C ILE A 34 -30.529 -37.554 11.799 1.00 10.27 A C +ANISOU 316 C ILE A 34 1440 1361 1100 310 -120 -63 A C +ATOM 317 O ILE A 34 -30.711 -37.520 10.575 1.00 10.64 A O +ANISOU 317 O ILE A 34 1345 1535 1162 208 -166 4 A O +ATOM 318 CB ILE A 34 -32.532 -38.856 12.572 1.00 10.97 A C +ANISOU 318 CB ILE A 34 1507 1351 1312 140 -155 30 A C +ATOM 319 CG1 ILE A 34 -33.804 -38.839 13.424 1.00 11.00 A C +ANISOU 319 CG1 ILE A 34 1446 1296 1436 79 -201 -14 A C +ATOM 320 CG2 ILE A 34 -31.659 -40.083 12.851 1.00 11.58 A C +ANISOU 320 CG2 ILE A 34 1622 1250 1527 167 -213 45 A C +ATOM 321 CD1 ILE A 34 -33.571 -38.568 14.897 1.00 11.46 A C +ANISOU 321 CD1 ILE A 34 1498 1461 1394 91 -41 -40 A C +ATOM 322 N VAL A 35 -29.319 -37.577 12.357 1.00 10.01 A N +ANISOU 322 N VAL A 35 1297 1356 1151 203 -159 -12 A N +ATOM 323 CA VAL A 35 -28.073 -37.503 11.601 1.00 9.97 A C +ANISOU 323 CA VAL A 35 1238 1279 1270 200 -95 -8 A C +ATOM 324 C VAL A 35 -27.299 -38.785 11.864 1.00 10.63 A C +ANISOU 324 C VAL A 35 1364 1448 1228 217 -138 -37 A C +ATOM 325 O VAL A 35 -26.993 -39.100 13.023 1.00 11.45 A O +ANISOU 325 O VAL A 35 1499 1664 1188 349 -211 133 A O +ATOM 326 CB VAL A 35 -27.227 -36.287 12.019 1.00 11.11 A C +ANISOU 326 CB VAL A 35 1393 1374 1453 69 -106 -49 A C +ATOM 327 CG1 VAL A 35 -25.902 -36.257 11.248 1.00 12.59 A C +ANISOU 327 CG1 VAL A 35 1297 1796 1691 65 22 -119 A C +ATOM 328 CG2 VAL A 35 -28.005 -34.987 11.836 1.00 11.98 A C +ANISOU 328 CG2 VAL A 35 1557 1415 1581 22 -115 16 A C +ATOM 329 N GLU A 36 -26.971 -39.521 10.802 1.00 10.35 A N +ANISOU 329 N GLU A 36 1241 1382 1309 282 -112 -22 A N +ATOM 330 CA GLU A 36 -26.175 -40.734 10.921 1.00 11.00 A C +ANISOU 330 CA GLU A 36 1321 1462 1395 241 4 93 A C +ATOM 331 C GLU A 36 -25.076 -40.748 9.872 1.00 11.01 A C +ANISOU 331 C GLU A 36 1311 1479 1392 316 27 247 A C +ATOM 332 O GLU A 36 -25.209 -40.158 8.798 1.00 11.67 A O +ANISOU 332 O GLU A 36 1356 1831 1248 319 77 287 A O +ATOM 333 CB GLU A 36 -27.038 -41.989 10.782 1.00 11.57 A C +ANISOU 333 CB GLU A 36 1535 1294 1568 161 126 115 A C +ATOM 334 CG GLU A 36 -27.944 -42.190 11.979 1.00 12.17 A C +ANISOU 334 CG GLU A 36 1606 1519 1498 106 259 64 A C +ATOM 335 CD GLU A 36 -28.703 -43.505 11.984 1.00 13.26 A C +ANISOU 335 CD GLU A 36 1763 1642 1631 229 164 43 A C +ATOM 336 OE1 GLU A 36 -28.222 -44.501 11.394 1.00 14.22 A O +ANISOU 336 OE1 GLU A 36 1826 1557 2019 194 53 -2 A O +ATOM 337 OE2 GLU A 36 -29.791 -43.536 12.599 1.00 13.84 A O +ANISOU 337 OE2 GLU A 36 1848 1677 1733 2 171 116 A O +ATOM 338 N ALYS A 37 -23.977 -41.413 10.208 0.52 11.87 A N +ANISOU 338 N ALYS A 37 1602 1531 1378 394 138 317 A N +ATOM 339 N BLYS A 37 -23.988 -41.440 10.194 0.48 11.94 A N +ANISOU 339 N BLYS A 37 1478 1583 1474 281 140 249 A N +ATOM 340 CA ALYS A 37 -22.899 -41.620 9.257 0.52 12.10 A C +ANISOU 340 CA ALYS A 37 1694 1560 1345 414 128 333 A C +ATOM 341 CA BLYS A 37 -22.883 -41.611 9.264 0.48 11.86 A C +ANISOU 341 CA BLYS A 37 1377 1594 1536 206 194 277 A C +ATOM 342 C ALYS A 37 -23.315 -42.690 8.254 0.52 13.61 A C +ANISOU 342 C ALYS A 37 2202 1634 1335 162 91 325 A C +ATOM 343 C BLYS A 37 -23.062 -42.893 8.462 0.48 13.08 A C +ANISOU 343 C BLYS A 37 1606 1865 1498 -167 354 267 A C +ATOM 344 O ALYS A 37 -23.807 -43.755 8.641 0.52 15.63 A O +ANISOU 344 O ALYS A 37 2714 1719 1505 -277 278 145 A O +ATOM 345 O BLYS A 37 -23.488 -43.922 8.995 0.48 15.18 A O +ANISOU 345 O BLYS A 37 2175 2060 1531 -338 75 109 A O +ATOM 346 CB ALYS A 37 -21.632 -42.050 9.996 0.52 12.25 A C +ANISOU 346 CB ALYS A 37 1681 1503 1469 639 248 202 A C +ATOM 347 CB BLYS A 37 -21.553 -41.673 10.017 0.48 12.04 A C +ANISOU 347 CB BLYS A 37 1399 1356 1818 429 164 229 A C +ATOM 348 CG ALYS A 37 -20.381 -42.019 9.127 0.52 14.20 A C +ANISOU 348 CG ALYS A 37 1988 1745 1662 811 296 299 A C +ATOM 349 CG BLYS A 37 -20.340 -41.581 9.095 0.48 12.91 A C +ANISOU 349 CG BLYS A 37 1469 1444 1994 237 285 140 A C +ATOM 350 CD ALYS A 37 -19.140 -42.371 9.920 0.52 17.76 A C +ANISOU 350 CD ALYS A 37 2302 2222 2222 828 224 612 A C +ATOM 351 CD BLYS A 37 -19.043 -41.829 9.836 0.48 12.65 A C +ANISOU 351 CD BLYS A 37 1439 1331 2035 154 171 346 A C +ATOM 352 CE ALYS A 37 -19.130 -43.841 10.292 0.52 20.77 A C +ANISOU 352 CE ALYS A 37 2902 2322 2666 832 213 945 A C +ATOM 353 CE BLYS A 37 -18.866 -43.307 10.139 0.48 13.86 A C +ANISOU 353 CE BLYS A 37 1489 1718 2060 -94 173 407 A C +ATOM 354 NZ ALYS A 37 -19.160 -44.706 9.087 0.52 23.05 A N +ANISOU 354 NZ ALYS A 37 3219 2163 3376 1059 501 803 A N +ATOM 355 NZ BLYS A 37 -17.583 -43.597 10.837 0.48 15.06 A N +ANISOU 355 NZ BLYS A 37 1620 2043 2057 96 -219 119 A N +ATOM 356 N AALA A 38 -23.137 -42.400 6.966 0.52 14.66 A N +ANISOU 356 N AALA A 38 2672 1561 1337 285 55 258 A N +ATOM 357 N BALA A 38 -22.734 -42.824 7.177 0.48 13.41 A N +ANISOU 357 N BALA A 38 1725 1879 1492 -169 253 82 A N +ATOM 358 CA AALA A 38 -23.469 -43.377 5.943 0.52 17.78 A C +ANISOU 358 CA AALA A 38 3505 1714 1534 108 -108 154 A C +ATOM 359 CA BALA A 38 -22.666 -44.029 6.366 0.48 13.74 A C +ANISOU 359 CA BALA A 38 2007 1843 1370 332 82 289 A C +ATOM 360 C AALA A 38 -22.643 -44.645 6.153 0.52 19.67 A C +ANISOU 360 C AALA A 38 4290 1635 1548 61 88 -59 A C +ATOM 361 C BALA A 38 -21.645 -44.981 6.987 0.48 13.44 A C +ANISOU 361 C BALA A 38 2137 1581 1389 107 77 134 A C +ATOM 362 O AALA A 38 -21.505 -44.584 6.628 0.52 18.39 A O +ANISOU 362 O AALA A 38 4279 1293 1417 303 137 -62 A O +ATOM 363 O BALA A 38 -20.543 -44.545 7.354 0.48 13.63 A O +ANISOU 363 O BALA A 38 2021 1585 1573 57 -47 58 A O +ATOM 364 CB AALA A 38 -23.184 -42.807 4.556 0.52 17.45 A C +ANISOU 364 CB AALA A 38 3580 1749 1301 184 -354 319 A C +ATOM 365 CB BALA A 38 -22.253 -43.669 4.941 0.48 14.87 A C +ANISOU 365 CB BALA A 38 1988 2130 1531 608 98 298 A C +ATOM 366 N APRO A 39 -23.195 -45.811 5.824 0.52 24.65 A N +ANISOU 366 N APRO A 39 5012 1988 2366 -105 95 112 A N +ATOM 367 N BPRO A 39 -21.966 -46.271 7.130 0.48 15.99 A N +ANISOU 367 N BPRO A 39 2672 1639 1767 3 -31 227 A N +ATOM 368 CA APRO A 39 -22.454 -47.059 6.045 0.52 26.76 A C +ANISOU 368 CA APRO A 39 5351 2061 2755 -86 315 144 A C +ATOM 369 CA BPRO A 39 -21.100 -47.152 7.936 0.48 17.37 A C +ANISOU 369 CA BPRO A 39 3094 1665 1843 159 22 370 A C +ATOM 370 C APRO A 39 -21.146 -47.080 5.266 0.52 27.00 A C +ANISOU 370 C APRO A 39 5441 2072 2745 152 554 -115 A C +ATOM 371 C BPRO A 39 -19.681 -47.268 7.410 0.48 18.32 A C +ANISOU 371 C BPRO A 39 3346 1570 2045 403 64 541 A C +ATOM 372 O APRO A 39 -21.112 -46.795 4.067 0.52 23.87 A O +ANISOU 372 O APRO A 39 5286 1744 2039 -97 486 -200 A O +ATOM 373 O BPRO A 39 -18.731 -47.336 8.200 0.48 18.09 A O +ANISOU 373 O BPRO A 39 3085 1753 2035 332 -225 829 A O +ATOM 374 CB APRO A 39 -23.426 -48.141 5.557 0.52 27.77 A C +ANISOU 374 CB APRO A 39 5442 2185 2923 -347 294 296 A C +ATOM 375 CB BPRO A 39 -21.844 -48.495 7.898 0.48 18.26 A C +ANISOU 375 CB BPRO A 39 3145 1909 1885 -79 -59 138 A C +ATOM 376 CG APRO A 39 -24.394 -47.427 4.672 0.52 28.72 A C +ANISOU 376 CG APRO A 39 5434 2401 3077 -298 245 149 A C +ATOM 377 CG BPRO A 39 -22.637 -48.440 6.634 0.48 18.44 A C +ANISOU 377 CG BPRO A 39 3038 1859 2109 -60 -196 129 A C +ATOM 378 CD APRO A 39 -24.530 -46.055 5.255 0.52 27.29 A C +ANISOU 378 CD APRO A 39 5281 2243 2844 -256 175 159 A C +ATOM 379 CD BPRO A 39 -23.079 -47.009 6.511 0.48 17.08 A C +ANISOU 379 CD BPRO A 39 2735 1660 2095 -29 -204 248 A C +ATOM 380 N ALYS A 40 -20.064 -47.397 5.978 0.52 29.00 A N +ANISOU 380 N ALYS A 40 5515 2330 3175 717 799 -88 A N +ATOM 381 N BLYS A 40 -19.509 -47.285 6.091 0.48 21.48 A N +ANISOU 381 N BLYS A 40 3958 1787 2414 597 616 483 A N +ATOM 382 CA ALYS A 40 -18.685 -47.561 5.503 0.52 30.90 A C +ANISOU 382 CA ALYS A 40 5485 2730 3525 1073 1208 -182 A C +ATOM 383 CA BLYS A 40 -18.188 -47.437 5.497 0.48 26.07 A C +ANISOU 383 CA BLYS A 40 4487 2347 3070 808 1069 204 A C +ATOM 384 C ALYS A 40 -17.898 -46.260 5.346 0.52 30.02 A C +ANISOU 384 C ALYS A 40 5312 2760 3334 1349 1534 33 A C +ATOM 385 C BLYS A 40 -17.389 -46.141 5.471 0.48 25.91 A C +ANISOU 385 C BLYS A 40 4525 2417 2901 1167 1440 179 A C +ATOM 386 O ALYS A 40 -16.748 -46.317 4.897 0.52 31.72 A O +ANISOU 386 O ALYS A 40 5374 3027 3652 1607 1595 -169 A O +ATOM 387 O BLYS A 40 -16.190 -46.180 5.176 0.48 27.36 A O +ANISOU 387 O BLYS A 40 4646 2543 3209 1230 1431 -262 A O +ATOM 388 CB ALYS A 40 -18.536 -48.420 4.233 0.52 32.56 A C +ANISOU 388 CB ALYS A 40 5482 2954 3934 1113 1203 -245 A C +ATOM 389 CB BLYS A 40 -18.302 -48.004 4.077 0.48 29.90 A C +ANISOU 389 CB BLYS A 40 4846 2775 3739 563 1124 120 A C +ATOM 390 CG ALYS A 40 -18.575 -49.927 4.469 0.52 34.42 A C +ANISOU 390 CG ALYS A 40 5519 3279 4280 881 1063 16 A C +ATOM 391 CG BLYS A 40 -18.492 -49.517 4.004 0.48 32.76 A C +ANISOU 391 CG BLYS A 40 5094 3147 4205 335 1083 291 A C +ATOM 392 CD ALYS A 40 -19.975 -50.420 4.802 0.52 34.75 A C +ANISOU 392 CD ALYS A 40 5498 3314 4393 797 1041 209 A C +ATOM 393 CD BLYS A 40 -19.877 -49.956 4.466 0.48 33.98 A C +ANISOU 393 CD BLYS A 40 5178 3388 4345 295 1140 342 A C +ATOM 394 N AALA A 41 -18.456 -45.103 5.696 0.52 26.75 A N +ANISOU 394 N AALA A 41 4895 2418 2853 1354 1680 361 A N +ATOM 395 N BALA A 41 -18.012 -45.003 5.770 0.48 23.57 A N +ANISOU 395 N BALA A 41 4311 2159 2486 1332 1548 605 A N +ATOM 396 CA AALA A 41 -17.705 -43.861 5.568 0.52 26.30 A C +ANISOU 396 CA AALA A 41 4678 2400 2916 1224 1757 522 A C +ATOM 397 CA BALA A 41 -17.295 -43.737 5.734 0.48 24.45 A C +ANISOU 397 CA BALA A 41 4306 2256 2727 1261 1601 613 A C +ATOM 398 C AALA A 41 -16.547 -43.844 6.559 0.52 25.63 A C +ANISOU 398 C AALA A 41 4064 2472 3203 1234 1921 698 A C +ATOM 399 C BALA A 41 -16.242 -43.706 6.833 0.48 25.32 A C +ANISOU 399 C BALA A 41 3954 2509 3157 1267 1833 671 A C +ATOM 400 O AALA A 41 -16.683 -44.294 7.700 0.52 26.42 A O +ANISOU 400 O AALA A 41 3883 2980 3174 1521 1847 1073 A O +ATOM 401 O BALA A 41 -16.556 -43.868 8.016 0.48 26.61 A O +ANISOU 401 O BALA A 41 3906 2995 3210 1422 1836 947 A O +ATOM 402 CB AALA A 41 -18.622 -42.663 5.811 0.52 25.46 A C +ANISOU 402 CB AALA A 41 4795 2133 2747 1255 1603 695 A C +ATOM 403 CB BALA A 41 -18.274 -42.577 5.909 0.48 24.42 A C +ANISOU 403 CB BALA A 41 4460 2142 2674 1244 1531 592 A C +ATOM 404 N AARG A 42 -15.399 -43.328 6.116 0.52 25.14 A N +ANISOU 404 N AARG A 42 3994 2132 3428 894 2091 583 A N +ATOM 405 N BARG A 42 -14.988 -43.496 6.440 0.48 25.84 A N +ANISOU 405 N BARG A 42 3969 2318 3531 1155 1775 441 A N +ATOM 406 CA AARG A 42 -14.182 -43.394 6.918 0.52 25.36 A C +ANISOU 406 CA AARG A 42 3821 2021 3796 589 1981 99 A C +ATOM 407 CA BARG A 42 -13.876 -43.528 7.381 0.48 27.90 A C +ANISOU 407 CA BARG A 42 4203 2433 3966 923 1632 14 A C +ATOM 408 C AARG A 42 -13.820 -42.054 7.551 0.52 24.51 A C +ANISOU 408 C AARG A 42 3266 2354 3691 643 1732 -125 A C +ATOM 409 C BARG A 42 -13.722 -42.235 8.168 0.48 28.48 A C +ANISOU 409 C BARG A 42 4212 2740 3869 721 1410 -100 A C +ATOM 410 O AARG A 42 -12.681 -41.589 7.435 0.52 26.19 A O +ANISOU 410 O AARG A 42 3260 2833 3860 712 1752 -181 A O +ATOM 411 O BARG A 42 -12.664 -42.015 8.766 0.48 30.83 A O +ANISOU 411 O BARG A 42 4564 3049 4100 603 1112 -255 A O +ATOM 412 CB AARG A 42 -13.023 -43.952 6.092 0.52 26.05 A C +ANISOU 412 CB AARG A 42 3933 1913 4052 361 2102 127 A C +ATOM 413 CB BARG A 42 -12.572 -43.879 6.657 0.48 29.21 A C +ANISOU 413 CB BARG A 42 4357 2370 4371 814 1795 -123 A C +ATOM 414 CG AARG A 42 -13.267 -45.356 5.564 0.52 25.58 A C +ANISOU 414 CG AARG A 42 3926 1725 4069 133 2069 443 A C +ATOM 415 CG BARG A 42 -12.635 -45.197 5.904 0.48 30.08 A C +ANISOU 415 CG BARG A 42 4546 2270 4615 617 1836 -53 A C +ATOM 416 CD AARG A 42 -13.471 -46.353 6.699 0.52 27.20 A C +ANISOU 416 CD AARG A 42 4163 1821 4350 16 1661 753 A C +ATOM 417 CD BARG A 42 -13.285 -46.273 6.759 0.48 31.56 A C +ANISOU 417 CD BARG A 42 4809 2262 4919 450 1711 159 A C +ATOM 418 NE AARG A 42 -13.771 -47.690 6.198 0.52 29.69 A N +ANISOU 418 NE AARG A 42 4553 2091 4638 15 1362 941 A N +ATOM 419 NE BARG A 42 -13.538 -47.497 6.010 0.48 33.01 A N +ANISOU 419 NE BARG A 42 5023 2395 5124 256 1640 367 A N +ATOM 420 CZ AARG A 42 -14.767 -48.453 6.631 0.52 31.18 A C +ANISOU 420 CZ AARG A 42 4774 2469 4604 23 1246 1106 A C +ATOM 421 CZ BARG A 42 -14.257 -48.515 6.465 0.48 34.24 A C +ANISOU 421 CZ BARG A 42 5171 2596 5243 131 1548 470 A C +ATOM 422 NH1AARG A 42 -15.569 -48.057 7.607 0.52 31.66 A N +ANISOU 422 NH1AARG A 42 4863 2652 4513 -61 1274 1315 A N +ATOM 423 NH1BARG A 42 -14.821 -48.482 7.662 0.48 34.14 A N +ANISOU 423 NH1BARG A 42 5196 2560 5214 97 1550 661 A N +ATOM 424 NH2AARG A 42 -14.956 -49.648 6.080 0.52 32.15 A N +ANISOU 424 NH2AARG A 42 4881 2742 4592 -32 1180 1034 A N +ATOM 425 NH2BARG A 42 -14.415 -49.591 5.700 0.48 35.10 A N +ANISOU 425 NH2BARG A 42 5233 2794 5309 24 1475 407 A N +ATOM 426 N AILE A 43 -14.782 -41.435 8.232 0.52 20.46 A N +ANISOU 426 N AILE A 43 2556 2064 3153 840 1270 90 A N +ATOM 427 N BILE A 43 -14.745 -41.383 8.181 0.48 26.44 A N +ANISOU 427 N BILE A 43 3845 2591 3612 889 1455 121 A N +ATOM 428 CA AILE A 43 -14.577 -40.198 8.974 0.52 17.86 A C +ANISOU 428 CA AILE A 43 1936 1938 2912 443 999 154 A C +ATOM 429 CA BILE A 43 -14.701 -40.126 8.920 0.48 24.37 A C +ANISOU 429 CA BILE A 43 3429 2444 3386 902 1296 350 A C +ATOM 430 C AILE A 43 -15.258 -40.333 10.331 0.52 18.10 A C +ANISOU 430 C AILE A 43 1760 1914 3203 477 984 371 A C +ATOM 431 C BILE A 43 -15.232 -40.335 10.331 0.48 21.59 A C +ANISOU 431 C BILE A 43 2681 2195 3329 829 1082 535 A C +ATOM 432 O AILE A 43 -15.902 -41.342 10.627 0.52 18.46 A O +ANISOU 432 O AILE A 43 1840 1789 3386 344 860 155 A O +ATOM 433 O BILE A 43 -15.745 -41.410 10.666 0.48 21.40 A O +ANISOU 433 O BILE A 43 2768 2039 3323 869 1012 600 A O +ATOM 434 CB AILE A 43 -15.077 -38.956 8.208 0.52 14.93 A C +ANISOU 434 CB AILE A 43 1346 2067 2260 51 482 -113 A C +ATOM 435 CB BILE A 43 -15.463 -39.004 8.191 0.48 25.85 A C +ANISOU 435 CB BILE A 43 3663 2900 3258 720 1146 292 A C +ATOM 436 CG1AILE A 43 -16.488 -39.198 7.674 0.52 14.39 A C +ANISOU 436 CG1AILE A 43 924 2598 1944 90 165 -158 A C +ATOM 437 CG1BILE A 43 -16.891 -39.446 7.870 0.48 26.14 A C +ANISOU 437 CG1BILE A 43 3762 3056 3113 709 821 186 A C +ATOM 438 CG2AILE A 43 -14.134 -38.605 7.071 0.52 14.66 A C +ANISOU 438 CG2AILE A 43 1342 2217 2009 151 215 -384 A C +ATOM 439 CG2BILE A 43 -14.721 -38.587 6.930 0.48 26.21 A C +ANISOU 439 CG2BILE A 43 3641 3068 3252 648 1222 306 A C +ATOM 440 CD1AILE A 43 -17.156 -37.967 7.058 0.52 14.67 A C +ANISOU 440 CD1AILE A 43 914 2761 1899 428 -143 -646 A C +ATOM 441 CD1BILE A 43 -17.685 -38.412 7.105 0.48 25.73 A C +ANISOU 441 CD1BILE A 43 3715 3017 3043 781 768 23 A C +ATOM 442 N GLY A 44 -15.115 -39.302 11.160 1.00 19.84 A N +ANISOU 442 N GLY A 44 2005 2259 3273 749 979 384 A N +ATOM 443 CA GLY A 44 -15.472 -39.424 12.558 1.00 18.59 A C +ANISOU 443 CA GLY A 44 1797 2328 2936 665 324 512 A C +ATOM 444 C GLY A 44 -16.956 -39.602 12.815 1.00 14.75 A C +ANISOU 444 C GLY A 44 1586 1784 2236 664 118 236 A C +ATOM 445 O GLY A 44 -17.826 -39.268 12.004 1.00 15.65 A O +ANISOU 445 O GLY A 44 1823 2008 2116 625 251 462 A O +ATOM 446 N ASP A 45 -17.227 -40.108 14.014 1.00 13.96 A N +ANISOU 446 N ASP A 45 1646 1762 1895 465 -17 100 A N +ATOM 447 CA ASP A 45 -18.568 -40.368 14.511 1.00 13.10 A C +ANISOU 447 CA ASP A 45 1667 1601 1708 369 -26 0 A C +ATOM 448 C ASP A 45 -18.997 -39.308 15.514 1.00 12.46 A C +ANISOU 448 C ASP A 45 1501 1577 1657 270 -91 -218 A C +ATOM 449 O ASP A 45 -18.200 -38.845 16.332 1.00 13.91 A O +ANISOU 449 O ASP A 45 1507 1909 1868 363 -112 -453 A O +ATOM 450 CB ASP A 45 -18.585 -41.700 15.256 1.00 15.07 A C +ANISOU 450 CB ASP A 45 2081 1692 1951 585 44 29 A C +ATOM 451 CG ASP A 45 -18.160 -42.851 14.389 1.00 18.69 A C +ANISOU 451 CG ASP A 45 2443 2264 2392 835 -301 -265 A C +ATOM 452 OD1 ASP A 45 -18.758 -43.020 13.315 1.00 19.30 A O +ANISOU 452 OD1 ASP A 45 2527 2340 2465 529 -306 -632 A O +ATOM 453 OD2 ASP A 45 -17.227 -43.588 14.772 1.00 23.18 A O +ANISOU 453 OD2 ASP A 45 3233 2652 2921 1192 -660 -567 A O +ATOM 454 N LEU A 46 -20.280 -38.971 15.477 1.00 11.64 A N +ANISOU 454 N LEU A 46 1449 1493 1481 318 -59 -104 A N +ATOM 455 CA LEU A 46 -20.911 -38.192 16.529 1.00 10.74 A C +ANISOU 455 CA LEU A 46 1421 1320 1338 317 -73 -87 A C +ATOM 456 C LEU A 46 -21.343 -39.128 17.660 1.00 11.07 A C +ANISOU 456 C LEU A 46 1511 1303 1392 185 -217 -208 A C +ATOM 457 O LEU A 46 -21.413 -40.348 17.494 1.00 13.15 A O +ANISOU 457 O LEU A 46 2255 1220 1521 215 -90 -166 A O +ATOM 458 CB LEU A 46 -22.129 -37.460 15.966 1.00 10.87 A C +ANISOU 458 CB LEU A 46 1479 1271 1382 202 -184 -79 A C +ATOM 459 CG LEU A 46 -21.838 -36.530 14.789 1.00 10.99 A C +ANISOU 459 CG LEU A 46 1539 1276 1361 182 -167 -167 A C +ATOM 460 CD1 LEU A 46 -23.123 -35.978 14.200 1.00 12.41 A C +ANISOU 460 CD1 LEU A 46 1701 1505 1509 261 -263 -76 A C +ATOM 461 CD2 LEU A 46 -20.884 -35.415 15.196 1.00 12.46 A C +ANISOU 461 CD2 LEU A 46 1584 1398 1752 -34 -233 -16 A C +ATOM 462 N ASP A 47 -21.643 -38.548 18.824 1.00 10.57 A N +ANISOU 462 N ASP A 47 1419 1263 1335 153 -218 -138 A N +ATOM 463 CA ASP A 47 -22.099 -39.332 19.967 1.00 10.89 A C +ANISOU 463 CA ASP A 47 1416 1311 1409 139 -196 -55 A C +ATOM 464 C ASP A 47 -23.610 -39.381 20.089 1.00 11.90 A C +ANISOU 464 C ASP A 47 1388 1680 1454 -4 -386 112 A C +ATOM 465 O ASP A 47 -24.123 -40.116 20.940 1.00 14.47 A O +ANISOU 465 O ASP A 47 1488 2181 1829 -64 -519 519 A O +ATOM 466 CB ASP A 47 -21.512 -38.775 21.266 1.00 10.81 A C +ANISOU 466 CB ASP A 47 1430 1344 1332 154 -311 -190 A C +ATOM 467 CG ASP A 47 -20.007 -38.821 21.276 1.00 10.71 A C +ANISOU 467 CG ASP A 47 1437 1264 1369 242 -360 -88 A C +ATOM 468 OD1 ASP A 47 -19.425 -39.855 20.878 1.00 12.68 A O +ANISOU 468 OD1 ASP A 47 1494 1551 1773 277 -384 -321 A O +ATOM 469 OD2 ASP A 47 -19.406 -37.806 21.689 1.00 10.71 A O +ANISOU 469 OD2 ASP A 47 1316 1279 1473 130 -210 -132 A O +ATOM 470 N LYS A 48 -24.322 -38.612 19.273 1.00 10.99 A N +ANISOU 470 N LYS A 48 1293 1540 1344 123 -365 -20 A N +ATOM 471 CA LYS A 48 -25.772 -38.568 19.262 1.00 11.48 A C +ANISOU 471 CA LYS A 48 1411 1634 1315 130 -381 -139 A C +ATOM 472 C LYS A 48 -26.233 -38.709 17.820 1.00 11.03 A C +ANISOU 472 C LYS A 48 1387 1390 1413 110 -304 -59 A C +ATOM 473 O LYS A 48 -25.451 -38.535 16.882 1.00 11.41 A O +ANISOU 473 O LYS A 48 1455 1516 1365 145 -341 -250 A O +ATOM 474 CB LYS A 48 -26.276 -37.233 19.829 1.00 12.83 A C +ANISOU 474 CB LYS A 48 1519 2057 1298 302 -367 -459 A C +ATOM 475 CG LYS A 48 -25.876 -36.990 21.266 1.00 16.28 A C +ANISOU 475 CG LYS A 48 1861 2746 1577 63 -189 -461 A C +ATOM 476 CD LYS A 48 -26.577 -37.953 22.199 1.00 19.27 A C +ANISOU 476 CD LYS A 48 2342 3171 1809 26 -363 -204 A C +ATOM 477 CE LYS A 48 -26.151 -37.733 23.632 1.00 23.85 A C +ANISOU 477 CE LYS A 48 2995 3518 2549 221 -138 -190 A C +ATOM 478 NZ LYS A 48 -26.319 -36.307 23.985 1.00 25.12 A N +ANISOU 478 NZ LYS A 48 3110 3602 2831 637 163 -370 A N +ATOM 479 N LYS A 49 -27.524 -39.005 17.662 1.00 10.81 A N +ANISOU 479 N LYS A 49 1409 1341 1357 163 -340 -42 A N +ATOM 480 CA LYS A 49 -28.191 -39.020 16.368 1.00 11.14 A C +ANISOU 480 CA LYS A 49 1559 1359 1313 171 -445 -106 A C +ATOM 481 C LYS A 49 -29.242 -37.931 16.237 1.00 11.00 A C +ANISOU 481 C LYS A 49 1366 1508 1307 112 -258 -77 A C +ATOM 482 O LYS A 49 -29.469 -37.427 15.138 1.00 11.56 A O +ANISOU 482 O LYS A 49 1499 1662 1232 283 -275 -47 A O +ATOM 483 CB LYS A 49 -28.869 -40.377 16.130 1.00 12.79 A C +ANISOU 483 CB LYS A 49 1670 1427 1762 138 -332 -188 A C +ATOM 484 CG LYS A 49 -27.892 -41.526 15.953 1.00 13.46 A C +ANISOU 484 CG LYS A 49 1658 1240 2217 142 -296 -212 A C +ATOM 485 CD LYS A 49 -28.626 -42.856 15.841 1.00 15.47 A C +ANISOU 485 CD LYS A 49 1800 1492 2587 131 -355 -429 A C +ATOM 486 CE LYS A 49 -27.693 -43.994 15.458 1.00 16.66 A C +ANISOU 486 CE LYS A 49 1923 1678 2729 211 -510 -311 A C +ATOM 487 NZ LYS A 49 -26.604 -44.146 16.456 1.00 16.99 A N +ANISOU 487 NZ LYS A 49 2251 1573 2632 340 -229 -38 A N +ATOM 488 N LYS A 50 -29.874 -37.541 17.328 1.00 10.73 A N +ANISOU 488 N LYS A 50 1411 1288 1377 139 -175 6 A N +ATOM 489 CA LYS A 50 -31.003 -36.629 17.288 1.00 10.92 A C +ANISOU 489 CA LYS A 50 1286 1442 1422 113 11 42 A C +ATOM 490 C LYS A 50 -30.527 -35.214 17.608 1.00 10.35 A C +ANISOU 490 C LYS A 50 1367 1356 1211 337 -215 -110 A C +ATOM 491 O LYS A 50 -29.928 -34.979 18.665 1.00 11.90 A O +ANISOU 491 O LYS A 50 1715 1529 1276 408 -400 -122 A O +ATOM 492 CB LYS A 50 -32.036 -37.125 18.298 1.00 15.10 A C +ANISOU 492 CB LYS A 50 1645 2202 1889 407 45 237 A C +ATOM 493 CG LYS A 50 -33.342 -36.400 18.283 1.00 15.81 A C +ANISOU 493 CG LYS A 50 1957 2098 1953 244 283 153 A C +ATOM 494 CD LYS A 50 -34.394 -37.071 19.176 1.00 16.91 A C +ANISOU 494 CD LYS A 50 1953 2213 2258 250 513 242 A C +ATOM 495 CE LYS A 50 -33.989 -37.102 20.645 1.00 17.70 A C +ANISOU 495 CE LYS A 50 1862 2395 2470 403 721 879 A C +ATOM 496 NZ LYS A 50 -34.987 -37.796 21.518 1.00 18.69 A N +ANISOU 496 NZ LYS A 50 2015 2405 2682 339 547 776 A N +ATOM 497 N TYR A 51 -30.809 -34.280 16.696 1.00 9.98 A N +ANISOU 497 N TYR A 51 1309 1222 1261 314 -113 -187 A N +ATOM 498 CA TYR A 51 -30.438 -32.876 16.800 1.00 9.52 A C +ANISOU 498 CA TYR A 51 1238 1203 1176 332 -228 -232 A C +ATOM 499 C TYR A 51 -31.664 -32.019 16.520 1.00 10.04 A C +ANISOU 499 C TYR A 51 1230 1314 1270 170 -269 -263 A C +ATOM 500 O TYR A 51 -32.631 -32.465 15.898 1.00 10.60 A O +ANISOU 500 O TYR A 51 1203 1294 1530 206 -369 -378 A O +ATOM 501 CB TYR A 51 -29.299 -32.541 15.813 1.00 9.99 A C +ANISOU 501 CB TYR A 51 1303 1283 1211 307 -170 -211 A C +ATOM 502 CG TYR A 51 -28.031 -33.277 16.177 1.00 9.56 A C +ANISOU 502 CG TYR A 51 1065 1299 1268 233 -73 -212 A C +ATOM 503 CD1 TYR A 51 -27.119 -32.704 17.052 1.00 10.18 A C +ANISOU 503 CD1 TYR A 51 1100 1360 1409 75 -209 -183 A C +ATOM 504 CD2 TYR A 51 -27.773 -34.568 15.711 1.00 9.86 A C +ANISOU 504 CD2 TYR A 51 1149 1257 1340 208 -130 -168 A C +ATOM 505 CE1 TYR A 51 -25.965 -33.377 17.438 1.00 10.26 A C +ANISOU 505 CE1 TYR A 51 1161 1317 1421 128 -215 -256 A C +ATOM 506 CE2 TYR A 51 -26.625 -35.251 16.092 1.00 9.68 A C +ANISOU 506 CE2 TYR A 51 1276 1191 1213 132 -144 -109 A C +ATOM 507 CZ TYR A 51 -25.728 -34.657 16.962 1.00 10.31 A C +ANISOU 507 CZ TYR A 51 1252 1345 1319 274 -201 -216 A C +ATOM 508 OH TYR A 51 -24.599 -35.347 17.340 1.00 10.90 A O +ANISOU 508 OH TYR A 51 1214 1426 1500 366 -344 -222 A O +ATOM 509 N LEU A 52 -31.629 -30.779 16.996 1.00 9.22 A N +ANISOU 509 N LEU A 52 1149 1214 1139 189 -212 -134 A N +ATOM 510 CA LEU A 52 -32.728 -29.837 16.789 1.00 9.26 A C +ANISOU 510 CA LEU A 52 1018 1226 1275 240 -44 -79 A C +ATOM 511 C LEU A 52 -32.101 -28.543 16.283 1.00 9.00 A C +ANISOU 511 C LEU A 52 1054 1160 1204 61 -74 -40 A C +ATOM 512 O LEU A 52 -31.485 -27.802 17.058 1.00 10.03 A O +ANISOU 512 O LEU A 52 1321 1216 1273 -29 -187 -128 A O +ATOM 513 CB LEU A 52 -33.519 -29.635 18.074 1.00 9.47 A C +ANISOU 513 CB LEU A 52 1164 1262 1170 190 -12 -105 A C +ATOM 514 CG LEU A 52 -34.778 -28.777 17.896 1.00 10.01 A C +ANISOU 514 CG LEU A 52 1216 1405 1183 154 20 -162 A C +ATOM 515 CD1 LEU A 52 -35.805 -29.457 16.983 1.00 10.69 A C +ANISOU 515 CD1 LEU A 52 1107 1634 1319 74 -8 -259 A C +ATOM 516 CD2 LEU A 52 -35.396 -28.461 19.239 1.00 10.85 A C +ANISOU 516 CD2 LEU A 52 1253 1520 1348 129 63 -17 A C +ATOM 517 N VAL A 53 -32.238 -28.289 14.985 1.00 9.13 A N +ANISOU 517 N VAL A 53 1066 1268 1135 134 -94 -29 A N +ATOM 518 CA VAL A 53 -31.420 -27.279 14.318 1.00 9.45 A C +ANISOU 518 CA VAL A 53 1045 1329 1218 114 -117 -68 A C +ATOM 519 C VAL A 53 -32.273 -26.090 13.896 1.00 9.31 A C +ANISOU 519 C VAL A 53 1017 1400 1122 51 -73 -113 A C +ATOM 520 O VAL A 53 -33.482 -26.240 13.660 1.00 9.62 A O +ANISOU 520 O VAL A 53 1104 1338 1213 81 -65 -69 A O +ATOM 521 CB VAL A 53 -30.667 -27.880 13.120 1.00 10.43 A C +ANISOU 521 CB VAL A 53 1272 1306 1386 279 -31 -150 A C +ATOM 522 CG1 VAL A 53 -29.894 -29.119 13.555 1.00 11.23 A C +ANISOU 522 CG1 VAL A 53 1319 1463 1485 381 -126 -195 A C +ATOM 523 CG2 VAL A 53 -31.621 -28.214 11.977 1.00 11.15 A C +ANISOU 523 CG2 VAL A 53 1427 1489 1320 60 -146 -195 A C +ATOM 524 N PRO A 54 -31.693 -24.900 13.771 1.00 9.27 A N +ANISOU 524 N PRO A 54 1133 1230 1158 62 -111 -165 A N +ATOM 525 CA PRO A 54 -32.482 -23.756 13.302 1.00 9.61 A C +ANISOU 525 CA PRO A 54 1246 1231 1173 234 -218 -139 A C +ATOM 526 C PRO A 54 -33.005 -23.994 11.898 1.00 9.42 A C +ANISOU 526 C PRO A 54 1221 1166 1194 198 -113 -63 A C +ATOM 527 O PRO A 54 -32.293 -24.492 11.029 1.00 9.60 A O +ANISOU 527 O PRO A 54 1198 1247 1202 194 -10 -80 A O +ATOM 528 CB PRO A 54 -31.479 -22.596 13.330 1.00 10.12 A C +ANISOU 528 CB PRO A 54 1249 1243 1355 53 -191 -225 A C +ATOM 529 CG PRO A 54 -30.442 -23.027 14.326 1.00 10.34 A C +ANISOU 529 CG PRO A 54 1260 1215 1455 8 -234 -162 A C +ATOM 530 CD PRO A 54 -30.320 -24.507 14.138 1.00 10.05 A C +ANISOU 530 CD PRO A 54 1181 1230 1407 -51 -126 -167 A C +ATOM 531 N ASER A 55 -34.257 -23.602 11.665 0.56 9.25 A N +ANISOU 531 N ASER A 55 1160 1219 1136 219 -255 -110 A N +ATOM 532 N BSER A 55 -34.272 -23.632 11.690 0.44 10.37 A N +ANISOU 532 N BSER A 55 1346 1336 1258 180 -175 -75 A N +ATOM 533 CA ASER A 55 -34.806 -23.721 10.320 0.56 9.42 A C +ANISOU 533 CA ASER A 55 1152 1294 1133 302 -189 -86 A C +ATOM 534 CA BSER A 55 -34.854 -23.674 10.358 0.44 12.24 A C +ANISOU 534 CA BSER A 55 1607 1630 1414 375 -166 -144 A C +ATOM 535 C ASER A 55 -33.984 -22.945 9.299 0.56 9.47 A C +ANISOU 535 C ASER A 55 1309 1102 1186 298 -331 -47 A C +ATOM 536 C BSER A 55 -34.089 -22.807 9.369 0.44 11.58 A C +ANISOU 536 C BSER A 55 1658 1385 1356 266 -125 -3 A C +ATOM 537 O ASER A 55 -33.848 -23.385 8.152 0.56 9.11 A O +ANISOU 537 O ASER A 55 1260 1088 1112 211 -182 -85 A O +ATOM 538 O BSER A 55 -34.158 -23.054 8.160 0.44 12.09 A O +ANISOU 538 O BSER A 55 1931 1350 1311 498 -190 74 A O +ATOM 539 CB ASER A 55 -36.264 -23.276 10.314 0.56 9.56 A C +ANISOU 539 CB ASER A 55 929 1457 1245 110 -108 102 A C +ATOM 540 CB BSER A 55 -36.305 -23.208 10.434 0.44 15.17 A C +ANISOU 540 CB BSER A 55 1911 2125 1727 575 -344 -254 A C +ATOM 541 OG ASER A 55 -37.018 -24.137 11.146 0.56 10.23 A O +ANISOU 541 OG ASER A 55 972 1570 1344 -41 -161 -25 A O +ATOM 542 OG BSER A 55 -36.893 -23.174 9.152 0.44 18.15 A O +ANISOU 542 OG BSER A 55 2392 2433 2070 677 -340 -495 A O +ATOM 543 N AASP A 56 -33.414 -21.807 9.685 0.56 10.05 A N +ANISOU 543 N AASP A 56 1397 1187 1235 418 -419 -67 A N +ATOM 544 N BASP A 56 -33.364 -21.801 9.849 0.44 10.46 A N +ANISOU 544 N BASP A 56 1335 1361 1276 -120 101 -57 A N +ATOM 545 CA AASP A 56 -32.667 -21.010 8.722 0.56 12.21 A C +ANISOU 545 CA AASP A 56 1727 1196 1717 474 -325 -142 A C +ATOM 546 CA BASP A 56 -32.633 -20.889 8.979 0.44 10.66 A C +ANISOU 546 CA BASP A 56 1429 1431 1191 -124 21 -38 A C +ATOM 547 C AASP A 56 -31.194 -21.394 8.601 0.56 12.43 A C +ANISOU 547 C AASP A 56 1654 1266 1802 344 -243 -11 A C +ATOM 548 C BASP A 56 -31.186 -21.308 8.731 0.44 10.89 A C +ANISOU 548 C BASP A 56 1427 1460 1251 -18 -15 101 A C +ATOM 549 O AASP A 56 -30.481 -20.770 7.808 0.56 13.90 A O +ANISOU 549 O AASP A 56 1815 1446 2020 197 -269 70 A O +ATOM 550 O BASP A 56 -30.493 -20.636 7.961 0.44 11.45 A O +ANISOU 550 O BASP A 56 1444 1659 1249 -68 59 415 A O +ATOM 551 CB AASP A 56 -32.842 -19.505 8.970 0.56 14.18 A C +ANISOU 551 CB AASP A 56 2199 1281 1907 589 -531 -302 A C +ATOM 552 CB BASP A 56 -32.685 -19.461 9.535 0.44 12.65 A C +ANISOU 552 CB BASP A 56 1659 1536 1610 -16 111 120 A C +ATOM 553 CG AASP A 56 -32.283 -19.050 10.302 0.56 15.37 A C +ANISOU 553 CG AASP A 56 2373 1371 2094 212 -531 -226 A C +ATOM 554 CG BASP A 56 -34.075 -18.847 9.446 0.44 15.85 A C +ANISOU 554 CG BASP A 56 2169 1779 2073 221 -25 43 A C +ATOM 555 OD1AASP A 56 -31.598 -19.840 10.982 0.56 15.40 A O +ANISOU 555 OD1AASP A 56 2220 1531 2099 148 -557 -239 A O +ATOM 556 OD1BASP A 56 -34.908 -19.346 8.659 0.44 17.40 A O +ANISOU 556 OD1BASP A 56 2083 2176 2352 481 -24 46 A O +ATOM 557 OD2AASP A 56 -32.522 -17.877 10.661 0.56 17.18 A O +ANISOU 557 OD2AASP A 56 2892 1460 2175 243 -623 -377 A O +ATOM 558 OD2BASP A 56 -34.331 -17.856 10.160 0.44 18.04 A O +ANISOU 558 OD2BASP A 56 2515 1891 2450 228 -5 -86 A O +ATOM 559 N LEU A 57 -30.722 -22.391 9.351 1.00 10.99 A N +ANISOU 559 N LEU A 57 1328 1439 1409 207 -81 16 A N +ATOM 560 CA LEU A 57 -29.369 -22.891 9.134 1.00 10.82 A C +ANISOU 560 CA LEU A 57 1317 1514 1281 230 -19 123 A C +ATOM 561 C LEU A 57 -29.260 -23.475 7.726 1.00 10.55 A C +ANISOU 561 C LEU A 57 1300 1583 1124 238 -53 134 A C +ATOM 562 O LEU A 57 -30.132 -24.230 7.291 1.00 11.92 A O +ANISOU 562 O LEU A 57 1314 1928 1285 -0 -141 -78 A O +ATOM 563 CB LEU A 57 -29.095 -24.005 10.148 1.00 11.04 A C +ANISOU 563 CB LEU A 57 1362 1583 1248 317 51 101 A C +ATOM 564 CG LEU A 57 -27.669 -24.571 10.186 1.00 10.74 A C +ANISOU 564 CG LEU A 57 1274 1587 1221 236 -26 -10 A C +ATOM 565 CD1 LEU A 57 -26.741 -23.656 10.977 1.00 11.87 A C +ANISOU 565 CD1 LEU A 57 1393 1849 1266 132 -135 -211 A C +ATOM 566 CD2 LEU A 57 -27.670 -25.980 10.759 1.00 11.85 A C +ANISOU 566 CD2 LEU A 57 1385 1622 1495 371 -102 58 A C +ATOM 567 N THR A 58 -28.173 -23.168 7.021 1.00 10.97 A N +ANISOU 567 N THR A 58 1329 1649 1190 153 -30 129 A N +ATOM 568 CA THR A 58 -27.991 -23.763 5.702 1.00 11.11 A C +ANISOU 568 CA THR A 58 1447 1570 1204 129 11 98 A C +ATOM 569 C THR A 58 -27.213 -25.070 5.791 1.00 10.42 A C +ANISOU 569 C THR A 58 1310 1516 1134 121 -69 5 A C +ATOM 570 O THR A 58 -26.504 -25.337 6.766 1.00 10.73 A O +ANISOU 570 O THR A 58 1405 1600 1072 177 11 13 A O +ATOM 571 CB THR A 58 -27.246 -22.827 4.754 1.00 11.76 A C +ANISOU 571 CB THR A 58 1608 1571 1290 100 -58 134 A C +ATOM 572 CG2 THR A 58 -27.973 -21.494 4.593 1.00 14.30 A C +ANISOU 572 CG2 THR A 58 1801 1860 1772 197 50 324 A C +ATOM 573 OG1 THR A 58 -25.920 -22.623 5.254 1.00 12.28 A O +ANISOU 573 OG1 THR A 58 1540 1691 1436 -4 50 152 A O +ATOM 574 N VAL A 59 -27.336 -25.877 4.732 1.00 11.05 A N +ANISOU 574 N VAL A 59 1473 1593 1134 36 -117 81 A N +ATOM 575 CA VAL A 59 -26.496 -27.064 4.591 1.00 11.26 A C +ANISOU 575 CA VAL A 59 1428 1666 1183 21 -134 -65 A C +ATOM 576 C VAL A 59 -25.029 -26.682 4.735 1.00 10.30 A C +ANISOU 576 C VAL A 59 1449 1442 1023 -22 -3 -118 A C +ATOM 577 O VAL A 59 -24.266 -27.344 5.441 1.00 10.99 A O +ANISOU 577 O VAL A 59 1534 1410 1231 112 -23 -123 A O +ATOM 578 CB VAL A 59 -26.794 -27.782 3.260 1.00 11.43 A C +ANISOU 578 CB VAL A 59 1557 1590 1197 -87 -143 -25 A C +ATOM 579 CG1 VAL A 59 -25.733 -28.851 2.965 1.00 12.39 A C +ANISOU 579 CG1 VAL A 59 1751 1703 1253 41 27 -110 A C +ATOM 580 CG2 VAL A 59 -28.192 -28.383 3.280 1.00 12.15 A C +ANISOU 580 CG2 VAL A 59 1759 1498 1359 -320 -332 98 A C +ATOM 581 N GLY A 60 -24.617 -25.595 4.072 1.00 10.85 A N +ANISOU 581 N GLY A 60 1458 1611 1054 -129 -2 -20 A N +ATOM 582 CA GLY A 60 -23.227 -25.167 4.164 1.00 11.70 A C +ANISOU 582 CA GLY A 60 1612 1637 1195 -31 1 13 A C +ATOM 583 C GLY A 60 -22.789 -24.855 5.585 1.00 10.78 A C +ANISOU 583 C GLY A 60 1414 1422 1261 -73 84 8 A C +ATOM 584 O GLY A 60 -21.679 -25.209 5.996 1.00 10.97 A O +ANISOU 584 O GLY A 60 1393 1537 1238 -35 34 -85 A O +ATOM 585 N GLN A 61 -23.653 -24.191 6.359 1.00 10.33 A N +ANISOU 585 N GLN A 61 1435 1314 1177 -12 20 -8 A N +ATOM 586 CA GLN A 61 -23.302 -23.934 7.754 1.00 10.39 A C +ANISOU 586 CA GLN A 61 1521 1249 1177 48 -29 -57 A C +ATOM 587 C GLN A 61 -23.220 -25.230 8.547 1.00 9.72 A C +ANISOU 587 C GLN A 61 1270 1306 1115 41 -22 -145 A C +ATOM 588 O GLN A 61 -22.364 -25.367 9.430 1.00 10.22 A O +ANISOU 588 O GLN A 61 1344 1440 1101 -22 -131 -83 A O +ATOM 589 CB GLN A 61 -24.333 -23.021 8.399 1.00 10.88 A C +ANISOU 589 CB GLN A 61 1655 1236 1241 94 71 -179 A C +ATOM 590 CG GLN A 61 -24.275 -21.590 7.951 1.00 12.32 A C +ANISOU 590 CG GLN A 61 1716 1205 1760 34 75 -77 A C +ATOM 591 CD GLN A 61 -25.411 -20.792 8.546 1.00 13.91 A C +ANISOU 591 CD GLN A 61 1946 1523 1817 160 -117 -261 A C +ATOM 592 NE2 GLN A 61 -25.073 -19.814 9.371 1.00 18.67 A N +ANISOU 592 NE2 GLN A 61 2449 2114 2530 358 -286 -831 A N +ATOM 593 OE1 GLN A 61 -26.583 -21.069 8.294 1.00 13.31 A O +ANISOU 593 OE1 GLN A 61 1712 1495 1850 220 55 -245 A O +ATOM 594 N PHE A 62 -24.112 -26.184 8.258 1.00 9.38 A N +ANISOU 594 N PHE A 62 1330 1174 1059 31 62 -37 A N +ATOM 595 CA PHE A 62 -24.063 -27.480 8.930 1.00 9.86 A C +ANISOU 595 CA PHE A 62 1294 1292 1160 45 37 -92 A C +ATOM 596 C PHE A 62 -22.782 -28.231 8.573 1.00 10.36 A C +ANISOU 596 C PHE A 62 1430 1271 1237 95 -166 -120 A C +ATOM 597 O PHE A 62 -22.144 -28.834 9.445 1.00 10.63 A O +ANISOU 597 O PHE A 62 1374 1378 1287 34 -6 -90 A O +ATOM 598 CB PHE A 62 -25.319 -28.282 8.569 1.00 10.47 A C +ANISOU 598 CB PHE A 62 1301 1442 1233 -53 15 9 A C +ATOM 599 CG PHE A 62 -25.805 -29.260 9.631 1.00 10.87 A C +ANISOU 599 CG PHE A 62 1478 1287 1366 -64 -33 -63 A C +ATOM 600 CD1 PHE A 62 -24.991 -29.733 10.654 1.00 11.51 A C +ANISOU 600 CD1 PHE A 62 1899 1274 1200 -2 125 -4 A C +ATOM 601 CD2 PHE A 62 -27.126 -29.693 9.592 1.00 12.06 A C +ANISOU 601 CD2 PHE A 62 1620 1580 1382 77 187 -20 A C +ATOM 602 CE1 PHE A 62 -25.489 -30.633 11.597 1.00 11.74 A C +ANISOU 602 CE1 PHE A 62 1661 1434 1366 70 63 -202 A C +ATOM 603 CE2 PHE A 62 -27.617 -30.587 10.534 1.00 13.59 A C +ANISOU 603 CE2 PHE A 62 1890 1656 1619 138 113 -124 A C +ATOM 604 CZ PHE A 62 -26.792 -31.055 11.532 1.00 13.39 A C +ANISOU 604 CZ PHE A 62 1962 1553 1572 18 123 -67 A C +ATOM 605 N TYR A 63 -22.370 -28.185 7.299 1.00 10.03 A N +ANISOU 605 N TYR A 63 1303 1359 1150 77 62 -133 A N +ATOM 606 CA TYR A 63 -21.090 -28.776 6.910 1.00 10.64 A C +ANISOU 606 CA TYR A 63 1336 1537 1170 99 3 -37 A C +ATOM 607 C TYR A 63 -19.945 -28.181 7.718 1.00 10.85 A C +ANISOU 607 C TYR A 63 1443 1503 1177 97 12 -70 A C +ATOM 608 O TYR A 63 -19.061 -28.906 8.190 1.00 11.43 A O +ANISOU 608 O TYR A 63 1487 1581 1276 256 -18 -94 A O +ATOM 609 CB TYR A 63 -20.818 -28.502 5.431 1.00 11.59 A C +ANISOU 609 CB TYR A 63 1591 1615 1200 6 39 -68 A C +ATOM 610 CG TYR A 63 -21.528 -29.346 4.386 1.00 11.57 A C +ANISOU 610 CG TYR A 63 1609 1362 1426 154 -1 -158 A C +ATOM 611 CD1 TYR A 63 -22.027 -30.611 4.673 1.00 12.54 A C +ANISOU 611 CD1 TYR A 63 1771 1592 1403 91 -218 -41 A C +ATOM 612 CD2 TYR A 63 -21.663 -28.868 3.092 1.00 12.30 A C +ANISOU 612 CD2 TYR A 63 1892 1600 1183 194 -37 -25 A C +ATOM 613 CE1 TYR A 63 -22.658 -31.371 3.681 1.00 12.95 A C +ANISOU 613 CE1 TYR A 63 1907 1583 1431 76 -199 -13 A C +ATOM 614 CE2 TYR A 63 -22.282 -29.613 2.105 1.00 11.62 A C +ANISOU 614 CE2 TYR A 63 1836 1525 1055 134 -70 -177 A C +ATOM 615 CZ TYR A 63 -22.766 -30.872 2.390 1.00 11.49 A C +ANISOU 615 CZ TYR A 63 1732 1386 1247 107 -50 -38 A C +ATOM 616 OH TYR A 63 -23.378 -31.632 1.411 1.00 11.69 A O +ANISOU 616 OH TYR A 63 1807 1353 1283 74 -269 -59 A O +ATOM 617 N PHE A 64 -19.912 -26.849 7.830 1.00 10.68 A N +ANISOU 617 N PHE A 64 1386 1547 1123 76 -11 -98 A N +ATOM 618 CA PHE A 64 -18.824 -26.190 8.549 1.00 12.62 A C +ANISOU 618 CA PHE A 64 1599 1790 1406 -187 -38 -29 A C +ATOM 619 C PHE A 64 -18.763 -26.674 9.990 1.00 11.37 A C +ANISOU 619 C PHE A 64 1413 1583 1326 207 -44 -159 A C +ATOM 620 O PHE A 64 -17.688 -26.994 10.512 1.00 12.87 A O +ANISOU 620 O PHE A 64 1464 2025 1400 244 -127 -227 A O +ATOM 621 CB PHE A 64 -19.030 -24.671 8.485 1.00 14.82 A C +ANISOU 621 CB PHE A 64 1967 1920 1745 -567 -130 47 A C +ATOM 622 CG PHE A 64 -18.006 -23.882 9.240 1.00 18.97 A C +ANISOU 622 CG PHE A 64 2432 2418 2357 -741 -47 -147 A C +ATOM 623 CD1 PHE A 64 -16.826 -23.495 8.629 1.00 23.51 A C +ANISOU 623 CD1 PHE A 64 2784 3056 3092 -1126 161 -40 A C +ATOM 624 CD2 PHE A 64 -18.221 -23.521 10.559 1.00 19.92 A C +ANISOU 624 CD2 PHE A 64 2788 2391 2389 -686 -296 -477 A C +ATOM 625 CE1 PHE A 64 -15.876 -22.768 9.321 1.00 25.46 A C +ANISOU 625 CE1 PHE A 64 3125 3269 3278 -1345 5 -212 A C +ATOM 626 CE2 PHE A 64 -17.276 -22.789 11.254 1.00 22.65 A C +ANISOU 626 CE2 PHE A 64 3270 2612 2722 -957 -371 -365 A C +ATOM 627 CZ PHE A 64 -16.105 -22.416 10.632 1.00 25.13 A C +ANISOU 627 CZ PHE A 64 3336 3174 3036 -1065 -271 -264 A C +ATOM 628 N LEU A 65 -19.922 -26.747 10.645 1.00 10.27 A N +ANISOU 628 N LEU A 65 1395 1306 1201 158 -4 -153 A N +ATOM 629 CA LEU A 65 -19.971 -27.178 12.039 1.00 10.41 A C +ANISOU 629 CA LEU A 65 1469 1397 1088 341 5 -104 A C +ATOM 630 C LEU A 65 -19.543 -28.637 12.197 1.00 10.76 A C +ANISOU 630 C LEU A 65 1490 1478 1122 381 -8 -109 A C +ATOM 631 O LEU A 65 -18.754 -28.962 13.088 1.00 11.69 A O +ANISOU 631 O LEU A 65 1664 1560 1216 407 -160 -114 A O +ATOM 632 CB LEU A 65 -21.370 -26.934 12.599 1.00 10.96 A C +ANISOU 632 CB LEU A 65 1548 1335 1281 271 54 -118 A C +ATOM 633 CG LEU A 65 -21.691 -25.461 12.846 1.00 10.99 A C +ANISOU 633 CG LEU A 65 1498 1408 1269 201 20 -247 A C +ATOM 634 CD1 LEU A 65 -23.171 -25.290 13.155 1.00 13.24 A C +ANISOU 634 CD1 LEU A 65 1569 1733 1730 184 27 -198 A C +ATOM 635 CD2 LEU A 65 -20.843 -24.888 13.976 1.00 13.01 A C +ANISOU 635 CD2 LEU A 65 1793 1695 1455 310 -299 -427 A C +ATOM 636 N AILE A 66 -19.999 -29.531 11.315 0.56 10.25 A N +ANISOU 636 N AILE A 66 1496 1396 1001 166 -204 -85 A N +ATOM 637 N BILE A 66 -20.095 -29.530 11.367 0.44 10.63 A N +ANISOU 637 N BILE A 66 1424 1448 1167 470 123 -79 A N +ATOM 638 CA AILE A 66 -19.574 -30.927 11.423 0.56 10.92 A C +ANISOU 638 CA AILE A 66 1537 1356 1257 162 -169 -253 A C +ATOM 639 CA BILE A 66 -19.750 -30.949 11.441 0.44 11.85 A C +ANISOU 639 CA BILE A 66 1608 1490 1405 578 84 -3 A C +ATOM 640 C AILE A 66 -18.075 -31.067 11.173 0.56 11.21 A C +ANISOU 640 C AILE A 66 1667 1450 1144 145 -129 -99 A C +ATOM 641 C BILE A 66 -18.262 -31.145 11.189 0.44 10.95 A C +ANISOU 641 C BILE A 66 1433 1561 1167 523 7 -251 A C +ATOM 642 O AILE A 66 -17.380 -31.779 11.908 0.56 12.14 A O +ANISOU 642 O AILE A 66 1790 1453 1370 257 -329 -1 A O +ATOM 643 O BILE A 66 -17.582 -31.880 11.915 0.44 11.03 A O +ANISOU 643 O BILE A 66 1384 1611 1196 516 198 -332 A O +ATOM 644 CB AILE A 66 -20.412 -31.848 10.514 0.56 11.04 A C +ANISOU 644 CB AILE A 66 1465 1399 1331 280 -150 -424 A C +ATOM 645 CB BILE A 66 -20.600 -31.765 10.448 0.44 13.83 A C +ANISOU 645 CB BILE A 66 1902 1679 1675 466 131 258 A C +ATOM 646 CG1AILE A 66 -21.823 -32.001 11.084 0.56 11.57 A C +ANISOU 646 CG1AILE A 66 1412 1448 1537 303 -234 -493 A C +ATOM 647 CG1BILE A 66 -22.066 -31.808 10.883 0.44 14.80 A C +ANISOU 647 CG1BILE A 66 2183 1793 1649 470 339 310 A C +ATOM 648 CG2AILE A 66 -19.740 -33.231 10.336 0.56 11.39 A C +ANISOU 648 CG2AILE A 66 1357 1555 1417 577 -110 -515 A C +ATOM 649 CG2BILE A 66 -20.038 -33.181 10.283 0.44 14.92 A C +ANISOU 649 CG2BILE A 66 1886 1936 1847 320 95 389 A C +ATOM 650 CD1AILE A 66 -22.787 -32.670 10.148 0.56 11.39 A C +ANISOU 650 CD1AILE A 66 1391 1503 1434 342 -439 -400 A C +ATOM 651 CD1BILE A 66 -22.369 -32.880 11.906 0.44 14.96 A C +ANISOU 651 CD1BILE A 66 2362 1722 1598 670 538 176 A C +ATOM 652 N AARG A 67 -17.551 -30.398 10.139 0.56 11.97 A N +ANISOU 652 N AARG A 67 1558 1655 1333 207 -56 -194 A N +ATOM 653 N BARG A 67 -17.738 -30.492 10.148 0.44 11.03 A N +ANISOU 653 N BARG A 67 1311 1623 1257 404 -62 -323 A N +ATOM 654 CA AARG A 67 -16.121 -30.494 9.849 0.56 12.65 A C +ANISOU 654 CA AARG A 67 1445 1935 1426 292 -3 -269 A C +ATOM 655 CA BARG A 67 -16.326 -30.624 9.805 0.44 11.88 A C +ANISOU 655 CA BARG A 67 1410 1847 1258 205 -43 -297 A C +ATOM 656 C AARG A 67 -15.277 -30.145 11.068 0.56 13.72 A C +ANISOU 656 C AARG A 67 1682 1930 1600 418 -40 -422 A C +ATOM 657 C BARG A 67 -15.433 -30.333 11.004 0.44 11.12 A C +ANISOU 657 C BARG A 67 1289 1697 1238 132 -38 -184 A C +ATOM 658 O AARG A 67 -14.268 -30.806 11.345 0.56 14.35 A O +ANISOU 658 O AARG A 67 1737 1983 1732 424 -204 -584 A O +ATOM 659 O BARG A 67 -14.499 -31.089 11.296 0.44 12.25 A O +ANISOU 659 O BARG A 67 1333 1953 1370 216 -56 -83 A O +ATOM 660 CB AARG A 67 -15.748 -29.588 8.673 0.56 13.76 A C +ANISOU 660 CB AARG A 67 1792 2159 1278 -55 93 -151 A C +ATOM 661 CB BARG A 67 -15.995 -29.685 8.643 0.44 13.25 A C +ANISOU 661 CB BARG A 67 1693 2039 1303 89 44 -267 A C +ATOM 662 CG AARG A 67 -16.251 -30.073 7.320 0.56 15.76 A C +ANISOU 662 CG AARG A 67 2024 2419 1546 -292 234 -174 A C +ATOM 663 CG BARG A 67 -14.513 -29.474 8.401 0.44 14.44 A C +ANISOU 663 CG BARG A 67 1735 2214 1539 -71 1 -193 A C +ATOM 664 CD AARG A 67 -15.691 -29.241 6.172 0.56 19.42 A C +ANISOU 664 CD AARG A 67 2287 2877 2214 -115 280 -16 A C +ATOM 665 CD BARG A 67 -14.267 -28.743 7.087 0.44 15.33 A C +ANISOU 665 CD BARG A 67 1947 2434 1443 -287 308 -289 A C +ATOM 666 NE AARG A 67 -14.253 -29.430 6.030 0.56 21.25 A N +ANISOU 666 NE AARG A 67 2449 3108 2517 42 247 -119 A N +ATOM 667 NE BARG A 67 -14.750 -29.508 5.943 0.44 16.02 A N +ANISOU 667 NE BARG A 67 2027 2459 1601 -361 467 -160 A N +ATOM 668 CZ AARG A 67 -13.693 -30.426 5.357 0.56 22.54 A C +ANISOU 668 CZ AARG A 67 2543 3313 2709 202 334 -100 A C +ATOM 669 CZ BARG A 67 -14.059 -30.464 5.337 0.44 16.88 A C +ANISOU 669 CZ BARG A 67 2314 2419 1682 -399 650 -79 A C +ATOM 670 NH1AARG A 67 -14.424 -31.329 4.723 0.56 22.78 A N +ANISOU 670 NH1AARG A 67 2560 3381 2713 339 178 -57 A N +ATOM 671 NH1BARG A 67 -12.836 -30.786 5.726 0.44 17.88 A N +ANISOU 671 NH1BARG A 67 2554 2414 1826 -347 802 -26 A N +ATOM 672 NH2AARG A 67 -12.367 -30.521 5.324 0.56 23.66 A N +ANISOU 672 NH2AARG A 67 2645 3474 2872 240 571 26 A N +ATOM 673 NH2BARG A 67 -14.611 -31.117 4.318 0.44 17.53 A N +ANISOU 673 NH2BARG A 67 2324 2513 1822 -190 302 -113 A N +ATOM 674 N ALYS A 68 -15.672 -29.108 11.808 0.56 12.99 A N +ANISOU 674 N ALYS A 68 1587 1744 1604 116 90 -287 A N +ATOM 675 N BLYS A 68 -15.708 -29.238 11.713 0.44 10.66 A N +ANISOU 675 N BLYS A 68 1303 1666 1082 -31 -15 -185 A N +ATOM 676 CA ALYS A 68 -14.927 -28.711 12.998 0.56 12.68 A C +ANISOU 676 CA ALYS A 68 1585 1807 1426 -47 154 -222 A C +ATOM 677 CA BLYS A 68 -14.891 -28.886 12.870 0.44 11.10 A C +ANISOU 677 CA BLYS A 68 1536 1637 1045 -115 -19 -334 A C +ATOM 678 C ALYS A 68 -15.218 -29.619 14.188 0.56 12.08 A C +ANISOU 678 C ALYS A 68 1511 1795 1285 73 38 -178 A C +ATOM 679 C BLYS A 68 -15.174 -29.803 14.055 0.44 10.77 A C +ANISOU 679 C BLYS A 68 1359 1671 1063 -90 62 -314 A C +ATOM 680 O ALYS A 68 -14.325 -29.871 15.005 0.56 13.21 A O +ANISOU 680 O ALYS A 68 1487 2121 1411 104 -85 94 A O +ATOM 681 O BLYS A 68 -14.245 -30.226 14.754 0.44 10.52 A O +ANISOU 681 O BLYS A 68 1165 1725 1104 65 0 -387 A O +ATOM 682 CB ALYS A 68 -15.236 -27.252 13.344 0.56 13.55 A C +ANISOU 682 CB ALYS A 68 1795 1917 1438 -194 215 12 A C +ATOM 683 CB BLYS A 68 -15.110 -27.420 13.244 0.44 12.62 A C +ANISOU 683 CB BLYS A 68 1820 1730 1247 -145 177 -99 A C +ATOM 684 CG ALYS A 68 -14.880 -26.261 12.242 0.56 16.72 A C +ANISOU 684 CG ALYS A 68 1945 2490 1917 -382 120 227 A C +ATOM 685 CG BLYS A 68 -14.528 -26.441 12.238 0.44 14.87 A C +ANISOU 685 CG BLYS A 68 2041 1899 1711 56 345 -204 A C +ATOM 686 CD ALYS A 68 -13.414 -26.364 11.851 0.56 18.46 A C +ANISOU 686 CD ALYS A 68 2170 2715 2130 -270 33 402 A C +ATOM 687 CD BLYS A 68 -14.695 -25.008 12.707 0.44 16.82 A C +ANISOU 687 CD BLYS A 68 2441 1970 1981 125 482 -112 A C +ATOM 688 N ARG A 69 -16.450 -30.117 14.298 1.00 10.61 A N +ANISOU 688 N ARG A 69 1435 1517 1078 92 129 -189 A N +ATOM 689 CA ARG A 69 -16.813 -31.013 15.396 1.00 10.67 A C +ANISOU 689 CA ARG A 69 1272 1595 1188 233 -190 -160 A C +ATOM 690 C ARG A 69 -16.076 -32.350 15.332 1.00 10.94 A C +ANISOU 690 C ARG A 69 1317 1619 1219 293 -94 -173 A C +ATOM 691 O ARG A 69 -15.643 -32.872 16.368 1.00 11.27 A O +ANISOU 691 O ARG A 69 1302 1681 1300 288 -123 -30 A O +ATOM 692 CB ARG A 69 -18.330 -31.230 15.387 1.00 10.44 A C +ANISOU 692 CB ARG A 69 1423 1402 1141 251 -111 -37 A C +ATOM 693 CG ARG A 69 -18.861 -32.411 16.209 1.00 10.50 A C +ANISOU 693 CG ARG A 69 1476 1348 1163 107 -55 -6 A C +ATOM 694 CD ARG A 69 -18.686 -32.246 17.715 1.00 10.07 A C +ANISOU 694 CD ARG A 69 1538 1220 1069 63 -93 -33 A C +ATOM 695 NE ARG A 69 -19.140 -33.434 18.430 1.00 10.14 A N +ANISOU 695 NE ARG A 69 1415 1252 1185 235 -179 -200 A N +ATOM 696 CZ ARG A 69 -18.437 -34.559 18.521 1.00 10.42 A C +ANISOU 696 CZ ARG A 69 1510 1242 1207 218 -145 -78 A C +ATOM 697 NH1 ARG A 69 -17.213 -34.651 18.019 1.00 11.13 A N +ANISOU 697 NH1 ARG A 69 1486 1358 1383 331 -134 -159 A N +ATOM 698 NH2 ARG A 69 -18.983 -35.624 19.103 1.00 11.11 A N +ANISOU 698 NH2 ARG A 69 1636 1283 1303 176 -98 -30 A N +ATOM 699 N ILE A 70 -15.934 -32.927 14.134 1.00 11.97 A N +ANISOU 699 N ILE A 70 1588 1655 1307 340 -57 -224 A N +ATOM 700 CA ILE A 70 -15.261 -34.214 13.976 1.00 13.44 A C +ANISOU 700 CA ILE A 70 1818 1907 1380 592 -43 -220 A C +ATOM 701 C ILE A 70 -13.824 -34.060 13.488 1.00 14.91 A C +ANISOU 701 C ILE A 70 1830 2292 1542 782 -131 -302 A C +ATOM 702 O ILE A 70 -13.194 -35.049 13.100 1.00 16.56 A O +ANISOU 702 O ILE A 70 1896 2189 2209 828 -216 -528 A O +ATOM 703 CB ILE A 70 -16.073 -35.241 13.165 1.00 12.96 A C +ANISOU 703 CB ILE A 70 1868 1707 1348 438 9 -147 A C +ATOM 704 CG1 ILE A 70 -16.217 -34.823 11.699 1.00 12.73 A C +ANISOU 704 CG1 ILE A 70 1724 1655 1459 353 -166 -182 A C +ATOM 705 CG2 ILE A 70 -17.422 -35.488 13.837 1.00 14.98 A C +ANISOU 705 CG2 ILE A 70 2160 1715 1817 122 420 -276 A C +ATOM 706 CD1 ILE A 70 -16.936 -35.848 10.833 1.00 13.70 A C +ANISOU 706 CD1 ILE A 70 1800 1708 1699 413 -91 -316 A C +ATOM 707 N AHIS A 71 -13.291 -32.839 13.501 0.80 14.18 A N +ANISOU 707 N AHIS A 71 1573 2294 1520 531 -215 -355 A N +ATOM 708 N BHIS A 71 -13.295 -32.835 13.495 0.20 16.65 A N +ANISOU 708 N BHIS A 71 1910 2757 1659 657 -113 -320 A N +ATOM 709 CA AHIS A 71 -11.871 -32.592 13.257 0.80 16.56 A C +ANISOU 709 CA AHIS A 71 1265 3320 1706 454 -389 -511 A C +ATOM 710 CA BHIS A 71 -11.878 -32.575 13.245 0.20 19.06 A C +ANISOU 710 CA BHIS A 71 1936 3421 1887 554 -113 -404 A C +ATOM 711 C AHIS A 71 -11.432 -33.108 11.887 0.80 17.16 A C +ANISOU 711 C AHIS A 71 1416 3463 1642 681 -311 -620 A C +ATOM 712 C BHIS A 71 -11.434 -33.115 11.885 0.20 18.54 A C +ANISOU 712 C BHIS A 71 1804 3496 1744 660 -47 -582 A C +ATOM 713 O AHIS A 71 -10.384 -33.742 11.755 0.80 19.10 A O +ANISOU 713 O AHIS A 71 1628 3794 1835 1069 -449 -646 A O +ATOM 714 O BHIS A 71 -10.396 -33.770 11.760 0.20 19.59 A O +ANISOU 714 O BHIS A 71 1961 3627 1855 732 -5 -720 A O +ATOM 715 CB AHIS A 71 -11.004 -33.182 14.375 0.80 20.37 A C +ANISOU 715 CB AHIS A 71 1553 4303 1886 247 -469 -709 A C +ATOM 716 CB BHIS A 71 -11.005 -33.117 14.382 0.20 22.25 A C +ANISOU 716 CB BHIS A 71 2180 4013 2260 367 -180 -344 A C +ATOM 717 CG AHIS A 71 -9.705 -32.467 14.580 0.80 25.66 A C +ANISOU 717 CG AHIS A 71 2164 5081 2506 -159 -75 -680 A C +ATOM 718 CG BHIS A 71 -9.625 -32.536 14.421 0.20 25.41 A C +ANISOU 718 CG BHIS A 71 2467 4514 2675 174 -179 -217 A C +ATOM 719 CD2AHIS A 71 -8.888 -31.825 13.711 0.80 28.80 A C +ANISOU 719 CD2AHIS A 71 2538 5430 2976 -357 50 -666 A C +ATOM 720 CD2BHIS A 71 -8.495 -32.966 15.029 0.20 26.67 A C +ANISOU 720 CD2BHIS A 71 2554 4717 2864 155 -153 -161 A C +ATOM 721 ND1AHIS A 71 -9.104 -32.365 15.815 0.80 27.16 A N +ANISOU 721 ND1AHIS A 71 2347 5296 2676 -403 94 -944 A N +ATOM 722 ND1BHIS A 71 -9.291 -31.364 13.777 0.20 26.80 A N +ANISOU 722 ND1BHIS A 71 2606 4707 2870 93 -213 -191 A N +ATOM 723 CE1AHIS A 71 -7.975 -31.689 15.701 0.80 28.72 A C +ANISOU 723 CE1AHIS A 71 2432 5479 3002 -527 77 -842 A C +ATOM 724 CE1BHIS A 71 -8.014 -31.097 13.987 0.20 27.38 A C +ANISOU 724 CE1BHIS A 71 2649 4817 2937 60 -246 -155 A C +ATOM 725 NE2AHIS A 71 -7.821 -31.348 14.434 0.80 30.32 A N +ANISOU 725 NE2AHIS A 71 2737 5564 3220 -456 74 -683 A N +ATOM 726 NE2BHIS A 71 -7.508 -32.054 14.744 0.20 27.30 A N +ANISOU 726 NE2BHIS A 71 2616 4830 2928 66 -238 -166 A N +ATOM 727 N LEU A 72 -12.235 -32.845 10.857 1.00 17.33 A N +ANISOU 727 N LEU A 72 1550 3484 1552 708 -88 -598 A N +ATOM 728 CA LEU A 72 -11.855 -33.267 9.516 1.00 19.56 A C +ANISOU 728 CA LEU A 72 1670 3963 1799 461 -68 -628 A C +ATOM 729 C LEU A 72 -10.604 -32.529 9.065 1.00 23.98 A C +ANISOU 729 C LEU A 72 1974 4985 2154 105 161 -877 A C +ATOM 730 O LEU A 72 -10.373 -31.371 9.423 1.00 25.94 A O +ANISOU 730 O LEU A 72 2254 5096 2507 -384 239 -682 A O +ATOM 731 CB LEU A 72 -12.968 -32.992 8.513 1.00 17.24 A C +ANISOU 731 CB LEU A 72 1614 3236 1699 247 -10 -352 A C +ATOM 732 CG LEU A 72 -14.201 -33.876 8.650 1.00 18.41 A C +ANISOU 732 CG LEU A 72 2010 2877 2108 306 80 -228 A C +ATOM 733 CD1 LEU A 72 -15.136 -33.617 7.492 1.00 18.65 A C +ANISOU 733 CD1 LEU A 72 1932 3092 2062 48 -303 -252 A C +ATOM 734 CD2 LEU A 72 -13.823 -35.342 8.733 1.00 20.76 A C +ANISOU 734 CD2 LEU A 72 2399 2894 2594 616 -43 -24 A C +ATOM 735 N ARG A 73 -9.786 -33.225 8.285 1.00 25.90 A N +ANISOU 735 N ARG A 73 1880 5657 2305 288 383 -894 A N +ATOM 736 CA ARG A 73 -8.648 -32.605 7.635 1.00 28.50 A C +ANISOU 736 CA ARG A 73 1979 6265 2586 167 227 -672 A C +ATOM 737 C ARG A 73 -9.116 -31.891 6.372 1.00 29.75 A C +ANISOU 737 C ARG A 73 2141 6471 2691 -311 -66 -533 A C +ATOM 738 O ARG A 73 -10.189 -32.172 5.835 1.00 27.83 A O +ANISOU 738 O ARG A 73 1705 6230 2638 -494 -97 -516 A O +ATOM 739 CB ARG A 73 -7.610 -33.663 7.266 1.00 30.51 A C +ANISOU 739 CB ARG A 73 2141 6515 2936 595 575 -417 A C +ATOM 740 CG ARG A 73 -7.218 -34.576 8.417 1.00 35.25 A C +ANISOU 740 CG ARG A 73 3007 6836 3551 728 586 -403 A C +ATOM 741 CD ARG A 73 -6.118 -35.540 8.002 1.00 39.88 A C +ANISOU 741 CD ARG A 73 3859 7077 4215 606 357 -367 A C +ATOM 742 NE ARG A 73 -6.534 -36.418 6.914 1.00 43.95 A N +ANISOU 742 NE ARG A 73 4616 7298 4785 347 80 -249 A N +ATOM 743 CZ ARG A 73 -7.008 -37.645 7.081 1.00 46.85 A C +ANISOU 743 CZ ARG A 73 5144 7495 5163 156 -29 -198 A C +ATOM 744 NH1 ARG A 73 -7.147 -38.175 8.286 1.00 48.08 A N +ANISOU 744 NH1 ARG A 73 5327 7577 5364 52 35 -110 A N +ATOM 745 NH2 ARG A 73 -7.347 -38.361 6.013 1.00 47.68 A N +ANISOU 745 NH2 ARG A 73 5312 7531 5274 150 -68 -281 A N +ATOM 746 N ALA A 74 -8.293 -30.952 5.897 1.00 32.02 A N +ANISOU 746 N ALA A 74 2377 6738 3052 -606 -226 -415 A N +ATOM 747 CA ALA A 74 -8.647 -30.207 4.691 1.00 33.50 A C +ANISOU 747 CA ALA A 74 2584 6914 3230 -610 -417 -324 A C +ATOM 748 C ALA A 74 -8.872 -31.143 3.509 1.00 32.55 A C +ANISOU 748 C ALA A 74 2342 7068 2958 -557 -414 -203 A C +ATOM 749 O ALA A 74 -9.761 -30.908 2.678 1.00 34.50 A O +ANISOU 749 O ALA A 74 2560 7223 3325 -566 -649 -77 A O +ATOM 750 CB ALA A 74 -7.560 -29.181 4.370 1.00 35.23 A C +ANISOU 750 CB ALA A 74 2956 6924 3506 -728 -384 -493 A C +ATOM 751 N GLU A 75 -8.090 -32.217 3.426 1.00 30.97 A N +ANISOU 751 N GLU A 75 2187 7046 2534 -341 65 -236 A N +ATOM 752 CA GLU A 75 -8.205 -33.159 2.321 1.00 30.59 A C +ANISOU 752 CA GLU A 75 2184 7029 2410 -80 232 -448 A C +ATOM 753 C GLU A 75 -9.363 -34.134 2.483 1.00 28.15 A C +ANISOU 753 C GLU A 75 2029 6592 2075 154 100 -683 A C +ATOM 754 O GLU A 75 -9.576 -34.967 1.594 1.00 29.55 A O +ANISOU 754 O GLU A 75 2318 6831 2078 211 270 -850 A O +ATOM 755 CB GLU A 75 -6.896 -33.932 2.134 1.00 33.17 A C +ANISOU 755 CB GLU A 75 2259 7364 2982 319 162 -374 A C +ATOM 756 CG GLU A 75 -6.580 -34.905 3.258 1.00 35.46 A C +ANISOU 756 CG GLU A 75 2490 7692 3292 656 -320 -359 A C +ATOM 757 CD GLU A 75 -5.672 -34.312 4.322 1.00 39.40 A C +ANISOU 757 CD GLU A 75 3085 8050 3835 812 -544 -288 A C +ATOM 758 OE1 GLU A 75 -5.699 -33.078 4.525 1.00 40.32 A O +ANISOU 758 OE1 GLU A 75 3211 8216 3892 875 -517 -273 A O +ATOM 759 OE2 GLU A 75 -4.922 -35.086 4.953 1.00 41.33 A O +ANISOU 759 OE2 GLU A 75 3340 8180 4185 859 -656 -309 A O +ATOM 760 N ASP A 76 -10.104 -34.060 3.584 1.00 24.52 A N +ANISOU 760 N ASP A 76 1735 5655 1927 525 220 -504 A N +ATOM 761 CA ASP A 76 -11.262 -34.913 3.796 1.00 22.86 A C +ANISOU 761 CA ASP A 76 1982 5052 1653 753 104 -603 A C +ATOM 762 C ASP A 76 -12.491 -34.245 3.199 1.00 19.56 A C +ANISOU 762 C ASP A 76 1881 4025 1525 434 105 -499 A C +ATOM 763 O ASP A 76 -12.711 -33.048 3.400 1.00 19.53 A O +ANISOU 763 O ASP A 76 1963 3627 1829 18 -56 -604 A O +ATOM 764 CB ASP A 76 -11.496 -35.120 5.291 1.00 25.42 A C +ANISOU 764 CB ASP A 76 2427 5484 1748 1428 -118 -682 A C +ATOM 765 CG ASP A 76 -10.418 -35.958 5.945 1.00 29.87 A C +ANISOU 765 CG ASP A 76 3262 5885 2203 2000 -300 -650 A C +ATOM 766 OD1 ASP A 76 -9.759 -36.746 5.236 1.00 33.04 A O +ANISOU 766 OD1 ASP A 76 3880 5866 2809 2392 -393 -764 A O +ATOM 767 OD2 ASP A 76 -10.233 -35.830 7.175 1.00 31.20 A O +ANISOU 767 OD2 ASP A 76 3453 6228 2173 1978 -467 -475 A O +ATOM 768 N ALA A 77 -13.285 -35.019 2.472 1.00 17.87 A N +ANISOU 768 N ALA A 77 1892 3448 1449 326 -70 -357 A N +ATOM 769 CA ALA A 77 -14.546 -34.535 1.941 1.00 15.99 A C +ANISOU 769 CA ALA A 77 1817 2873 1386 121 -9 -410 A C +ATOM 770 C ALA A 77 -15.658 -34.764 2.958 1.00 14.66 A C +ANISOU 770 C ALA A 77 1747 2576 1246 313 -0 -201 A C +ATOM 771 O ALA A 77 -15.543 -35.596 3.860 1.00 16.28 A O +ANISOU 771 O ALA A 77 1878 2829 1478 721 -26 -61 A O +ATOM 772 CB ALA A 77 -14.885 -35.266 0.644 1.00 16.60 A C +ANISOU 772 CB ALA A 77 2066 2821 1420 1 110 -473 A C +ATOM 773 N LEU A 78 -16.753 -34.028 2.784 1.00 13.09 A N +ANISOU 773 N LEU A 78 1531 2175 1267 110 -28 -150 A N +ATOM 774 CA LEU A 78 -17.942 -34.211 3.610 1.00 12.25 A C +ANISOU 774 CA LEU A 78 1597 1864 1194 73 31 17 A C +ATOM 775 C LEU A 78 -19.158 -33.954 2.740 1.00 11.84 A C +ANISOU 775 C LEU A 78 1704 1687 1109 94 -152 31 A C +ATOM 776 O LEU A 78 -19.281 -32.870 2.165 1.00 13.12 A O +ANISOU 776 O LEU A 78 1691 1762 1533 -89 -220 101 A O +ATOM 777 CB LEU A 78 -17.936 -33.239 4.789 1.00 13.00 A C +ANISOU 777 CB LEU A 78 1781 1815 1342 -27 -59 -200 A C +ATOM 778 CG LEU A 78 -19.176 -33.313 5.687 1.00 12.52 A C +ANISOU 778 CG LEU A 78 1751 1744 1262 7 49 -199 A C +ATOM 779 CD1 LEU A 78 -19.306 -34.676 6.361 1.00 13.34 A C +ANISOU 779 CD1 LEU A 78 1978 1788 1302 -200 138 90 A C +ATOM 780 CD2 LEU A 78 -19.137 -32.203 6.712 1.00 13.18 A C +ANISOU 780 CD2 LEU A 78 1752 1767 1490 10 84 -286 A C +ATOM 781 N PHE A 79 -20.053 -34.937 2.656 1.00 11.12 A N +ANISOU 781 N PHE A 79 1571 1586 1068 -37 -55 -112 A N +ATOM 782 CA PHE A 79 -21.285 -34.844 1.887 1.00 11.03 A C +ANISOU 782 CA PHE A 79 1574 1483 1133 -127 -43 -9 A C +ATOM 783 C PHE A 79 -22.458 -35.199 2.788 1.00 10.74 A C +ANISOU 783 C PHE A 79 1573 1394 1115 38 -145 93 A C +ATOM 784 O PHE A 79 -22.344 -36.060 3.671 1.00 11.44 A O +ANISOU 784 O PHE A 79 1647 1515 1184 219 -40 281 A O +ATOM 785 CB PHE A 79 -21.303 -35.856 0.727 1.00 11.61 A C +ANISOU 785 CB PHE A 79 1782 1532 1098 -141 26 -197 A C +ATOM 786 CG PHE A 79 -20.171 -35.699 -0.251 1.00 12.72 A C +ANISOU 786 CG PHE A 79 2083 1699 1052 -182 -12 -22 A C +ATOM 787 CD1 PHE A 79 -18.965 -36.356 -0.051 1.00 12.67 A C +ANISOU 787 CD1 PHE A 79 1854 1923 1038 -172 133 -191 A C +ATOM 788 CD2 PHE A 79 -20.307 -34.903 -1.380 1.00 14.10 A C +ANISOU 788 CD2 PHE A 79 2609 1712 1036 -262 3 55 A C +ATOM 789 CE1 PHE A 79 -17.923 -36.229 -0.961 1.00 14.63 A C +ANISOU 789 CE1 PHE A 79 2230 2140 1186 -264 157 -167 A C +ATOM 790 CE2 PHE A 79 -19.260 -34.772 -2.288 1.00 14.66 A C +ANISOU 790 CE2 PHE A 79 2568 1779 1224 -350 -116 54 A C +ATOM 791 CZ PHE A 79 -18.077 -35.441 -2.078 1.00 15.30 A C +ANISOU 791 CZ PHE A 79 2515 1939 1358 -366 84 -166 A C +ATOM 792 N PHE A 80 -23.591 -34.542 2.546 1.00 10.60 A N +ANISOU 792 N PHE A 80 1617 1364 1044 116 -178 8 A N +ATOM 793 CA PHE A 80 -24.875 -34.953 3.096 1.00 10.48 A C +ANISOU 793 CA PHE A 80 1627 1297 1056 159 -25 -111 A C +ATOM 794 C PHE A 80 -25.686 -35.665 2.020 1.00 10.18 A C +ANISOU 794 C PHE A 80 1574 1257 1036 347 -10 24 A C +ATOM 795 O PHE A 80 -25.564 -35.370 0.828 1.00 10.94 A O +ANISOU 795 O PHE A 80 1709 1365 1085 171 -129 21 A O +ATOM 796 CB PHE A 80 -25.720 -33.746 3.522 1.00 11.47 A C +ANISOU 796 CB PHE A 80 1980 1305 1073 300 -61 -208 A C +ATOM 797 CG PHE A 80 -25.437 -33.188 4.892 1.00 12.58 A C +ANISOU 797 CG PHE A 80 2162 1385 1233 251 -172 -114 A C +ATOM 798 CD1 PHE A 80 -24.486 -33.728 5.746 1.00 12.61 A C +ANISOU 798 CD1 PHE A 80 2264 1318 1211 142 -191 -204 A C +ATOM 799 CD2 PHE A 80 -26.190 -32.104 5.332 1.00 13.11 A C +ANISOU 799 CD2 PHE A 80 2086 1525 1369 25 94 -126 A C +ATOM 800 CE1 PHE A 80 -24.288 -33.167 7.011 1.00 14.36 A C +ANISOU 800 CE1 PHE A 80 2636 1308 1512 334 -284 -74 A C +ATOM 801 CE2 PHE A 80 -25.997 -31.548 6.576 1.00 14.66 A C +ANISOU 801 CE2 PHE A 80 2311 1556 1703 237 5 -26 A C +ATOM 802 CZ PHE A 80 -25.052 -32.079 7.420 1.00 14.71 A C +ANISOU 802 CZ PHE A 80 2460 1655 1475 178 -167 -78 A C +ATOM 803 N PHE A 81 -26.567 -36.559 2.467 1.00 10.41 A N +ANISOU 803 N PHE A 81 1547 1318 1092 192 -66 59 A N +ATOM 804 CA PHE A 81 -27.571 -37.189 1.620 1.00 11.20 A C +ANISOU 804 CA PHE A 81 1758 1314 1184 51 -200 -30 A C +ATOM 805 C PHE A 81 -28.907 -37.146 2.338 1.00 12.02 A C +ANISOU 805 C PHE A 81 1765 1519 1283 1 -333 121 A C +ATOM 806 O PHE A 81 -28.992 -37.473 3.527 1.00 12.65 A O +ANISOU 806 O PHE A 81 1774 1784 1248 -61 -352 163 A O +ATOM 807 CB PHE A 81 -27.209 -38.646 1.308 1.00 12.73 A C +ANISOU 807 CB PHE A 81 2078 1167 1593 26 -405 -70 A C +ATOM 808 CG PHE A 81 -25.907 -38.792 0.592 1.00 13.51 A C +ANISOU 808 CG PHE A 81 1938 1426 1769 365 -465 -197 A C +ATOM 809 CD1 PHE A 81 -24.728 -38.916 1.303 1.00 15.91 A C +ANISOU 809 CD1 PHE A 81 2260 1567 2217 725 -609 -490 A C +ATOM 810 CD2 PHE A 81 -25.851 -38.768 -0.789 1.00 13.22 A C +ANISOU 810 CD2 PHE A 81 1881 1463 1678 369 -230 -147 A C +ATOM 811 CE1 PHE A 81 -23.516 -39.034 0.652 1.00 17.90 A C +ANISOU 811 CE1 PHE A 81 2346 1931 2523 776 -528 -602 A C +ATOM 812 CE2 PHE A 81 -24.646 -38.878 -1.444 1.00 15.40 A C +ANISOU 812 CE2 PHE A 81 2072 1585 2194 559 -171 -338 A C +ATOM 813 CZ PHE A 81 -23.477 -39.016 -0.722 1.00 16.59 A C +ANISOU 813 CZ PHE A 81 2072 1791 2441 664 -391 -497 A C +ATOM 814 N VAL A 82 -29.947 -36.749 1.615 1.00 11.98 A N +ANISOU 814 N VAL A 82 1687 1530 1333 -58 -219 27 A N +ATOM 815 CA VAL A 82 -31.327 -36.919 2.044 1.00 13.03 A C +ANISOU 815 CA VAL A 82 1762 1787 1402 22 -255 -64 A C +ATOM 816 C VAL A 82 -31.987 -37.758 0.964 1.00 14.54 A C +ANISOU 816 C VAL A 82 1774 2137 1613 -19 -361 22 A C +ATOM 817 O VAL A 82 -31.951 -37.392 -0.217 1.00 14.71 A O +ANISOU 817 O VAL A 82 2011 2154 1425 -5 -407 17 A O +ATOM 818 CB VAL A 82 -32.041 -35.569 2.215 1.00 14.41 A C +ANISOU 818 CB VAL A 82 1815 2057 1605 245 -199 -194 A C +ATOM 819 CG1 VAL A 82 -33.495 -35.779 2.626 1.00 15.84 A C +ANISOU 819 CG1 VAL A 82 1789 2391 1839 442 -90 -149 A C +ATOM 820 CG2 VAL A 82 -31.314 -34.696 3.232 1.00 15.31 A C +ANISOU 820 CG2 VAL A 82 2028 1842 1948 301 -122 -309 A C +ATOM 821 N ASN A 83 -32.539 -38.904 1.351 1.00 16.01 A N +ANISOU 821 N ASN A 83 2095 2508 1479 -273 -240 -246 A N +ATOM 822 CA ASN A 83 -33.107 -39.842 0.381 1.00 18.72 A C +ANISOU 822 CA ASN A 83 2495 2901 1717 -683 -150 -404 A C +ATOM 823 C ASN A 83 -32.130 -40.128 -0.759 1.00 18.63 A C +ANISOU 823 C ASN A 83 2878 2536 1664 -887 -80 -490 A C +ATOM 824 O ASN A 83 -32.491 -40.114 -1.938 1.00 21.19 A O +ANISOU 824 O ASN A 83 3167 3162 1724 -1238 -104 -574 A O +ATOM 825 CB ASN A 83 -34.458 -39.363 -0.148 1.00 20.86 A C +ANISOU 825 CB ASN A 83 2595 3454 1875 -668 -161 -364 A C +ATOM 826 CG ASN A 83 -35.495 -39.254 0.941 1.00 20.99 A C +ANISOU 826 CG ASN A 83 2759 3406 1811 -758 -262 -356 A C +ATOM 827 ND2 ASN A 83 -36.399 -38.292 0.805 1.00 21.90 A N +ANISOU 827 ND2 ASN A 83 2814 3336 2172 -505 -459 -259 A N +ATOM 828 OD1 ASN A 83 -35.476 -40.018 1.907 1.00 21.81 A O +ANISOU 828 OD1 ASN A 83 2990 3461 1836 -1070 -43 -296 A O +ATOM 829 N AASN A 84 -30.870 -40.364 -0.394 0.43 17.90 A N +ANISOU 829 N AASN A 84 3023 2011 1768 -612 54 -406 A N +ATOM 830 N BASN A 84 -30.868 -40.363 -0.394 0.57 17.43 A N +ANISOU 830 N BASN A 84 3052 1840 1731 -546 71 -474 A N +ATOM 831 CA AASN A 84 -29.812 -40.777 -1.314 0.43 18.51 A C +ANISOU 831 CA AASN A 84 3159 1892 1981 -323 270 -416 A C +ATOM 832 CA BASN A 84 -29.795 -40.768 -1.300 0.57 18.26 A C +ANISOU 832 CA BASN A 84 3206 1747 1984 -218 333 -461 A C +ATOM 833 C AASN A 84 -29.379 -39.686 -2.288 0.43 16.01 A C +ANISOU 833 C AASN A 84 2674 1672 1736 -201 106 -307 A C +ATOM 834 C BASN A 84 -29.348 -39.677 -2.267 0.57 15.71 A C +ANISOU 834 C BASN A 84 2674 1605 1690 -37 152 -315 A C +ATOM 835 O AASN A 84 -28.688 -39.990 -3.267 0.43 16.95 A O +ANISOU 835 O AASN A 84 2650 1777 2016 -246 150 -400 A O +ATOM 836 O BASN A 84 -28.603 -39.972 -3.209 0.57 16.42 A O +ANISOU 836 O BASN A 84 2602 1807 1830 77 105 -358 A O +ATOM 837 CB AASN A 84 -30.171 -42.059 -2.081 0.43 22.56 A C +ANISOU 837 CB AASN A 84 3639 2303 2629 -415 437 -382 A C +ATOM 838 CB BASN A 84 -30.106 -42.075 -2.043 0.57 22.57 A C +ANISOU 838 CB BASN A 84 3727 2151 2698 -394 461 -462 A C +ATOM 839 CG AASN A 84 -29.013 -43.027 -2.177 0.43 26.42 A C +ANISOU 839 CG AASN A 84 3981 2930 3127 -303 394 -246 A C +ATOM 840 CG BASN A 84 -29.941 -43.297 -1.164 0.57 26.24 A C +ANISOU 840 CG BASN A 84 4116 2653 3202 -416 254 -427 A C +ATOM 841 ND2AASN A 84 -29.056 -44.078 -1.368 0.43 27.95 A N +ANISOU 841 ND2AASN A 84 4030 3304 3286 -20 463 -173 A N +ATOM 842 ND2BASN A 84 -30.754 -44.319 -1.408 0.57 28.23 A N +ANISOU 842 ND2BASN A 84 4224 3078 3426 -700 157 -240 A N +ATOM 843 OD1AASN A 84 -28.097 -42.841 -2.976 0.43 28.85 A O +ANISOU 843 OD1AASN A 84 4275 3269 3418 -336 212 -173 A O +ATOM 844 OD1BASN A 84 -29.089 -43.325 -0.276 0.57 27.61 A O +ANISOU 844 OD1BASN A 84 4391 2712 3387 -255 261 -477 A O +ATOM 845 N VAL A 85 -29.753 -38.428 -2.052 1.00 14.05 A N +ANISOU 845 N VAL A 85 2367 1548 1424 -213 -57 -180 A N +ATOM 846 CA VAL A 85 -29.413 -37.325 -2.942 1.00 14.42 A C +ANISOU 846 CA VAL A 85 2487 1620 1370 -88 -350 -184 A C +ATOM 847 C VAL A 85 -28.754 -36.217 -2.133 1.00 12.48 A C +ANISOU 847 C VAL A 85 2157 1466 1119 53 -261 1 A C +ATOM 848 O VAL A 85 -29.218 -35.872 -1.039 1.00 12.09 A O +ANISOU 848 O VAL A 85 1916 1525 1152 -26 -256 -101 A O +ATOM 849 CB VAL A 85 -30.663 -36.790 -3.667 1.00 18.50 A C +ANISOU 849 CB VAL A 85 2866 2242 1922 -235 -998 -84 A C +ATOM 850 CG1 VAL A 85 -30.302 -35.620 -4.567 1.00 20.99 A C +ANISOU 850 CG1 VAL A 85 3384 2295 2296 -57 -1345 191 A C +ATOM 851 CG2 VAL A 85 -31.326 -37.901 -4.480 1.00 20.89 A C +ANISOU 851 CG2 VAL A 85 2992 2637 2308 -397 -982 -309 A C +ATOM 852 N ILE A 86 -27.683 -35.646 -2.675 1.00 12.71 A N +ANISOU 852 N ILE A 86 2162 1505 1163 218 -170 -64 A N +ATOM 853 CA ILE A 86 -26.992 -34.545 -2.004 1.00 11.46 A C +ANISOU 853 CA ILE A 86 1840 1384 1130 115 -33 -98 A C +ATOM 854 C ILE A 86 -27.857 -33.289 -2.052 1.00 10.72 A C +ANISOU 854 C ILE A 86 1679 1267 1125 75 -186 15 A C +ATOM 855 O ILE A 86 -28.173 -32.802 -3.147 1.00 11.17 A O +ANISOU 855 O ILE A 86 1551 1513 1182 218 -108 40 A O +ATOM 856 CB ILE A 86 -25.627 -34.263 -2.652 1.00 11.74 A C +ANISOU 856 CB ILE A 86 1815 1463 1184 378 35 -44 A C +ATOM 857 CG1 ILE A 86 -24.739 -35.509 -2.635 1.00 13.04 A C +ANISOU 857 CG1 ILE A 86 2057 1674 1225 458 128 -128 A C +ATOM 858 CG2 ILE A 86 -24.950 -33.093 -1.955 1.00 11.61 A C +ANISOU 858 CG2 ILE A 86 1468 1654 1289 228 44 63 A C +ATOM 859 CD1 ILE A 86 -23.506 -35.398 -3.515 1.00 14.63 A C +ANISOU 859 CD1 ILE A 86 2260 1812 1485 687 177 103 A C +ATOM 860 N PRO A 87 -28.242 -32.718 -0.915 1.00 10.97 A N +ANISOU 860 N PRO A 87 1735 1299 1132 57 -55 -75 A N +ATOM 861 CA PRO A 87 -29.041 -31.487 -0.933 1.00 11.32 A C +ANISOU 861 CA PRO A 87 1676 1384 1242 226 147 -96 A C +ATOM 862 C PRO A 87 -28.170 -30.300 -1.292 1.00 11.08 A C +ANISOU 862 C PRO A 87 1626 1414 1169 297 -62 1 A C +ATOM 863 O PRO A 87 -26.963 -30.303 -1.014 1.00 11.37 A O +ANISOU 863 O PRO A 87 1572 1381 1366 241 18 -36 A O +ATOM 864 CB PRO A 87 -29.530 -31.373 0.518 1.00 11.97 A C +ANISOU 864 CB PRO A 87 1839 1480 1230 245 196 -100 A C +ATOM 865 CG PRO A 87 -28.417 -32.002 1.316 1.00 11.91 A C +ANISOU 865 CG PRO A 87 1893 1510 1124 321 115 -77 A C +ATOM 866 CD PRO A 87 -27.937 -33.161 0.461 1.00 11.44 A C +ANISOU 866 CD PRO A 87 1971 1367 1009 112 -18 -121 A C +ATOM 867 N PRO A 88 -28.752 -29.244 -1.860 1.00 11.30 A N +ANISOU 867 N PRO A 88 1620 1454 1218 105 -56 28 A N +ATOM 868 CA PRO A 88 -27.950 -28.063 -2.197 1.00 11.62 A C +ANISOU 868 CA PRO A 88 1808 1504 1102 107 -87 73 A C +ATOM 869 C PRO A 88 -27.317 -27.432 -0.968 1.00 10.95 A C +ANISOU 869 C PRO A 88 1689 1355 1117 163 -49 -12 A C +ATOM 870 O PRO A 88 -27.949 -27.289 0.080 1.00 11.19 A O +ANISOU 870 O PRO A 88 1718 1457 1076 214 75 -1 A O +ATOM 871 CB PRO A 88 -28.969 -27.116 -2.840 1.00 12.98 A C +ANISOU 871 CB PRO A 88 1966 1690 1277 136 -157 62 A C +ATOM 872 CG PRO A 88 -30.088 -28.004 -3.297 1.00 14.17 A C +ANISOU 872 CG PRO A 88 1965 1808 1610 49 -291 331 A C +ATOM 873 CD PRO A 88 -30.160 -29.096 -2.272 1.00 13.20 A C +ANISOU 873 CD PRO A 88 1861 1662 1494 261 -237 178 A C +ATOM 874 N THR A 89 -26.063 -27.013 -1.121 1.00 11.31 A N +ANISOU 874 N THR A 89 1823 1382 1094 203 8 40 A N +ATOM 875 CA THR A 89 -25.343 -26.375 -0.025 1.00 11.74 A C +ANISOU 875 CA THR A 89 1734 1554 1174 117 46 -38 A C +ATOM 876 C THR A 89 -26.052 -25.112 0.448 1.00 11.18 A C +ANISOU 876 C THR A 89 1647 1401 1201 47 28 22 A C +ATOM 877 O THR A 89 -26.017 -24.789 1.642 1.00 11.49 A O +ANISOU 877 O THR A 89 1608 1569 1188 105 20 10 A O +ATOM 878 CB THR A 89 -23.906 -26.101 -0.473 1.00 12.81 A C +ANISOU 878 CB THR A 89 1704 1718 1446 67 192 -31 A C +ATOM 879 CG2 THR A 89 -23.060 -25.527 0.657 1.00 14.52 A C +ANISOU 879 CG2 THR A 89 1628 2290 1598 24 -13 -263 A C +ATOM 880 OG1 THR A 89 -23.323 -27.333 -0.900 1.00 13.16 A O +ANISOU 880 OG1 THR A 89 1748 1729 1524 165 254 11 A O +ATOM 881 N SER A 90 -26.732 -24.412 -0.462 1.00 11.38 A N +ANISOU 881 N SER A 90 1732 1423 1170 112 10 159 A N +ATOM 882 CA SER A 90 -27.444 -23.190 -0.119 1.00 12.60 A C +ANISOU 882 CA SER A 90 1946 1386 1457 180 153 185 A C +ATOM 883 C SER A 90 -28.792 -23.432 0.548 1.00 12.36 A C +ANISOU 883 C SER A 90 1771 1619 1304 216 -31 115 A C +ATOM 884 O SER A 90 -29.386 -22.470 1.047 1.00 12.74 A O +ANISOU 884 O SER A 90 1648 1637 1555 352 -15 -19 A O +ATOM 885 CB SER A 90 -27.691 -22.379 -1.390 1.00 16.08 A C +ANISOU 885 CB SER A 90 2509 1844 1758 158 174 377 A C +ATOM 886 OG SER A 90 -28.476 -23.133 -2.301 1.00 18.47 A O +ANISOU 886 OG SER A 90 2897 2506 1617 238 37 683 A O +ATOM 887 N ALA A 91 -29.306 -24.662 0.548 1.00 11.62 A N +ANISOU 887 N ALA A 91 1724 1606 1083 54 -27 126 A N +ATOM 888 CA ALA A 91 -30.636 -24.904 1.098 1.00 11.56 A C +ANISOU 888 CA ALA A 91 1575 1626 1193 62 -29 36 A C +ATOM 889 C ALA A 91 -30.653 -24.721 2.610 1.00 10.98 A C +ANISOU 889 C ALA A 91 1503 1676 992 119 -106 18 A C +ATOM 890 O ALA A 91 -29.691 -25.065 3.302 1.00 11.86 A O +ANISOU 890 O ALA A 91 1504 1879 1121 228 -106 -5 A O +ATOM 891 CB ALA A 91 -31.087 -26.328 0.789 1.00 12.27 A C +ANISOU 891 CB ALA A 91 1669 1813 1182 -51 -63 -73 A C +ATOM 892 N THR A 92 -31.764 -24.188 3.126 1.00 11.15 A N +ANISOU 892 N THR A 92 1465 1688 1085 170 -35 1 A N +ATOM 893 CA THR A 92 -31.939 -24.162 4.570 1.00 10.95 A C +ANISOU 893 CA THR A 92 1373 1620 1167 166 -95 22 A C +ATOM 894 C THR A 92 -32.525 -25.477 5.073 1.00 10.47 A C +ANISOU 894 C THR A 92 1245 1686 1048 153 -83 -98 A C +ATOM 895 O THR A 92 -33.189 -26.222 4.345 1.00 10.95 A O +ANISOU 895 O THR A 92 1400 1645 1114 171 -93 -82 A O +ATOM 896 CB THR A 92 -32.853 -23.025 5.037 1.00 11.78 A C +ANISOU 896 CB THR A 92 1496 1563 1419 134 -41 25 A C +ATOM 897 CG2 THR A 92 -32.375 -21.681 4.518 1.00 13.24 A C +ANISOU 897 CG2 THR A 92 1861 1614 1557 69 -111 18 A C +ATOM 898 OG1 THR A 92 -34.201 -23.283 4.614 1.00 11.72 A O +ANISOU 898 OG1 THR A 92 1323 1725 1404 215 -124 -51 A O +ATOM 899 N AMET A 93 -32.266 -25.752 6.354 0.58 10.44 A N +ANISOU 899 N AMET A 93 1345 1548 1073 380 -93 -34 A N +ATOM 900 N BMET A 93 -32.309 -25.735 6.361 0.41 10.95 A N +ANISOU 900 N BMET A 93 1410 1733 1019 -53 25 37 A N +ATOM 901 CA AMET A 93 -32.851 -26.920 7.002 0.58 10.42 A C +ANISOU 901 CA AMET A 93 1471 1474 1014 295 -260 -88 A C +ATOM 902 CA BMET A 93 -32.848 -26.947 6.961 0.41 11.67 A C +ANISOU 902 CA BMET A 93 1532 1826 1076 -157 -120 -23 A C +ATOM 903 C AMET A 93 -34.370 -26.884 6.934 0.58 10.43 A C +ANISOU 903 C AMET A 93 1438 1489 1035 220 -213 -85 A C +ATOM 904 C BMET A 93 -34.372 -26.902 7.060 0.41 11.51 A C +ANISOU 904 C BMET A 93 1443 1774 1157 -39 -57 -178 A C +ATOM 905 O AMET A 93 -35.013 -27.914 6.698 0.58 9.68 A O +ANISOU 905 O AMET A 93 1451 1411 816 134 -88 -146 A O +ATOM 906 O BMET A 93 -35.020 -27.955 7.053 0.41 12.02 A O +ANISOU 906 O BMET A 93 1437 1937 1193 -26 -1 -159 A O +ATOM 907 CB AMET A 93 -32.389 -26.992 8.456 0.58 11.23 A C +ANISOU 907 CB AMET A 93 1664 1503 1101 375 -166 -45 A C +ATOM 908 CB BMET A 93 -32.177 -27.204 8.311 0.41 12.98 A C +ANISOU 908 CB BMET A 93 1836 1930 1167 -83 -304 -195 A C +ATOM 909 CG AMET A 93 -30.920 -27.326 8.614 0.58 11.80 A C +ANISOU 909 CG AMET A 93 1712 1397 1375 103 -180 24 A C +ATOM 910 CG BMET A 93 -30.638 -27.186 8.252 0.41 12.88 A C +ANISOU 910 CG BMET A 93 1751 2132 1011 26 -371 -173 A C +ATOM 911 SD AMET A 93 -30.537 -28.978 8.019 0.58 11.42 A S +ANISOU 911 SD AMET A 93 1367 1582 1388 164 -60 -34 A S +ATOM 912 SD BMET A 93 -29.909 -28.401 7.129 0.41 14.41 A S +ANISOU 912 SD BMET A 93 1792 2268 1415 182 -40 -341 A S +ATOM 913 CE AMET A 93 -29.528 -28.579 6.602 0.58 11.95 A C +ANISOU 913 CE AMET A 93 1435 1758 1346 224 -52 -211 A C +ATOM 914 CE BMET A 93 -30.814 -29.836 7.666 0.41 17.56 A C +ANISOU 914 CE BMET A 93 2359 2478 1834 60 23 -338 A C +ATOM 915 N GLY A 94 -34.962 -25.703 7.133 1.00 11.25 A N +ANISOU 915 N GLY A 94 1413 1630 1232 116 41 -167 A N +ATOM 916 CA GLY A 94 -36.409 -25.593 7.060 1.00 11.85 A C +ANISOU 916 CA GLY A 94 1268 1686 1549 114 -32 -295 A C +ATOM 917 C GLY A 94 -36.946 -25.960 5.689 1.00 11.76 A C +ANISOU 917 C GLY A 94 1277 1545 1647 89 -12 -142 A C +ATOM 918 O GLY A 94 -37.992 -26.614 5.578 1.00 12.40 A O +ANISOU 918 O GLY A 94 1341 1665 1706 -14 -16 -266 A O +ATOM 919 N AGLN A 95 -36.242 -25.551 4.632 0.52 11.89 A N +ANISOU 919 N AGLN A 95 1383 1579 1556 76 -268 -184 A N +ATOM 920 N BGLN A 95 -36.253 -25.538 4.625 0.48 11.24 A N +ANISOU 920 N BGLN A 95 1401 1274 1597 54 -98 -75 A N +ATOM 921 CA AGLN A 95 -36.666 -25.917 3.286 0.52 12.55 A C +ANISOU 921 CA AGLN A 95 1525 1763 1480 199 -314 -97 A C +ATOM 922 CA BGLN A 95 -36.668 -25.923 3.278 0.48 11.48 A C +ANISOU 922 CA BGLN A 95 1494 1327 1540 -6 22 -32 A C +ATOM 923 C AGLN A 95 -36.534 -27.419 3.055 0.52 11.76 A C +ANISOU 923 C AGLN A 95 1413 1627 1426 186 -324 51 A C +ATOM 924 C BGLN A 95 -36.551 -27.430 3.079 0.48 10.96 A C +ANISOU 924 C BGLN A 95 1423 1328 1416 -47 3 -122 A C +ATOM 925 O AGLN A 95 -37.431 -28.046 2.480 0.52 12.99 A O +ANISOU 925 O AGLN A 95 1464 1937 1536 253 -575 159 A O +ATOM 926 O BGLN A 95 -37.463 -28.069 2.542 0.48 12.10 A O +ANISOU 926 O BGLN A 95 1558 1508 1533 -168 -10 -405 A O +ATOM 927 CB AGLN A 95 -35.875 -25.111 2.255 0.52 14.48 A C +ANISOU 927 CB AGLN A 95 1832 2105 1564 248 -489 16 A C +ATOM 928 CB BGLN A 95 -35.856 -25.164 2.223 0.48 12.78 A C +ANISOU 928 CB BGLN A 95 1719 1444 1692 -85 -26 160 A C +ATOM 929 CG AGLN A 95 -36.497 -25.080 0.874 0.52 16.16 A C +ANISOU 929 CG AGLN A 95 2238 2258 1646 473 -731 178 A C +ATOM 930 CG BGLN A 95 -36.114 -25.590 0.767 0.48 14.71 A C +ANISOU 930 CG BGLN A 95 2048 1713 1829 -57 -173 375 A C +ATOM 931 CD AGLN A 95 -36.070 -26.254 0.034 0.52 17.27 A C +ANISOU 931 CD AGLN A 95 2427 2461 1674 391 -377 -82 A C +ATOM 932 CD BGLN A 95 -37.463 -25.132 0.220 0.48 15.48 A C +ANISOU 932 CD BGLN A 95 2054 2087 1742 -208 -245 300 A C +ATOM 933 NE2AGLN A 95 -36.872 -26.587 -0.970 0.52 18.37 A N +ANISOU 933 NE2AGLN A 95 2667 2624 1691 212 -307 -383 A N +ATOM 934 NE2BGLN A 95 -37.911 -25.775 -0.854 0.48 16.07 A N +ANISOU 934 NE2BGLN A 95 2106 2374 1625 -220 -505 494 A N +ATOM 935 OE1AGLN A 95 -35.026 -26.859 0.282 0.52 17.81 A O +ANISOU 935 OE1AGLN A 95 2569 2441 1757 338 -288 -39 A O +ATOM 936 OE1BGLN A 95 -38.087 -24.210 0.746 0.48 16.71 A O +ANISOU 936 OE1BGLN A 95 2171 2220 1958 -45 -234 343 A O +ATOM 937 N LEU A 96 -35.429 -28.018 3.508 1.00 11.36 A N +ANISOU 937 N LEU A 96 1489 1430 1399 146 -114 -76 A N +ATOM 938 CA LEU A 96 -35.273 -29.467 3.385 1.00 11.48 A C +ANISOU 938 CA LEU A 96 1481 1543 1338 154 -158 -189 A C +ATOM 939 C LEU A 96 -36.326 -30.204 4.195 1.00 11.14 A C +ANISOU 939 C LEU A 96 1330 1543 1358 30 -232 -203 A C +ATOM 940 O LEU A 96 -36.844 -31.238 3.756 1.00 12.27 A O +ANISOU 940 O LEU A 96 1581 1593 1486 56 -272 -251 A O +ATOM 941 CB LEU A 96 -33.880 -29.903 3.827 1.00 12.11 A C +ANISOU 941 CB LEU A 96 1428 1720 1452 113 -154 -183 A C +ATOM 942 CG LEU A 96 -32.706 -29.424 2.983 1.00 13.09 A C +ANISOU 942 CG LEU A 96 1514 1881 1578 54 -82 -168 A C +ATOM 943 CD1 LEU A 96 -31.426 -29.995 3.564 1.00 15.08 A C +ANISOU 943 CD1 LEU A 96 1586 2305 1840 -52 -320 -407 A C +ATOM 944 CD2 LEU A 96 -32.870 -29.821 1.524 1.00 13.67 A C +ANISOU 944 CD2 LEU A 96 1699 1954 1540 208 15 77 A C +ATOM 945 N TYR A 97 -36.649 -29.686 5.382 1.00 11.73 A N +ANISOU 945 N TYR A 97 1498 1662 1297 -3 -108 -159 A N +ATOM 946 CA TYR A 97 -37.666 -30.303 6.218 1.00 12.57 A C +ANISOU 946 CA TYR A 97 1511 1672 1594 -69 -21 -159 A C +ATOM 947 C TYR A 97 -39.015 -30.286 5.517 1.00 13.53 A C +ANISOU 947 C TYR A 97 1648 1608 1883 6 -26 -203 A C +ATOM 948 O TYR A 97 -39.718 -31.302 5.474 1.00 14.47 A O +ANISOU 948 O TYR A 97 1696 1716 2088 -281 -121 -229 A O +ATOM 949 CB TYR A 97 -37.748 -29.550 7.547 1.00 13.04 A C +ANISOU 949 CB TYR A 97 1660 1721 1572 -210 274 -360 A C +ATOM 950 CG TYR A 97 -38.742 -30.155 8.499 1.00 12.77 A C +ANISOU 950 CG TYR A 97 1560 1680 1613 -228 182 -349 A C +ATOM 951 CD1 TYR A 97 -38.381 -31.210 9.324 1.00 12.42 A C +ANISOU 951 CD1 TYR A 97 1644 1625 1450 -248 99 -351 A C +ATOM 952 CD2 TYR A 97 -40.047 -29.687 8.564 1.00 13.52 A C +ANISOU 952 CD2 TYR A 97 1620 1733 1783 -63 43 -154 A C +ATOM 953 CE1 TYR A 97 -39.284 -31.781 10.183 1.00 11.89 A C +ANISOU 953 CE1 TYR A 97 1546 1375 1595 -124 87 -319 A C +ATOM 954 CE2 TYR A 97 -40.954 -30.257 9.428 1.00 13.08 A C +ANISOU 954 CE2 TYR A 97 1442 1626 1901 41 -47 -23 A C +ATOM 955 CZ TYR A 97 -40.571 -31.300 10.231 1.00 12.18 A C +ANISOU 955 CZ TYR A 97 1366 1521 1743 -9 1 -205 A C +ATOM 956 OH TYR A 97 -41.488 -31.858 11.088 1.00 12.40 A O +ANISOU 956 OH TYR A 97 1230 1667 1814 0 -55 19 A O +ATOM 957 N AGLN A 98 -39.421 -29.125 5.002 0.55 13.81 A N +ANISOU 957 N AGLN A 98 1546 1567 2135 77 -58 -202 A N +ATOM 958 N BGLN A 98 -39.361 -29.143 4.919 0.45 15.12 A N +ANISOU 958 N BGLN A 98 1638 1734 2375 24 -91 -157 A N +ATOM 959 CA AGLN A 98 -40.715 -29.029 4.336 0.55 14.07 A C +ANISOU 959 CA AGLN A 98 1530 1607 2210 171 -216 -49 A C +ATOM 960 CA BGLN A 98 -40.601 -28.987 4.167 0.45 17.48 A C +ANISOU 960 CA BGLN A 98 1749 2037 2856 60 -303 -12 A C +ATOM 961 C AGLN A 98 -40.853 -30.085 3.250 0.55 12.68 A C +ANISOU 961 C AGLN A 98 1482 1634 1704 -80 -172 -93 A C +ATOM 962 C BGLN A 98 -40.631 -29.870 2.924 0.45 18.36 A C +ANISOU 962 C BGLN A 98 1679 2232 3065 -174 -663 17 A C +ATOM 963 O AGLN A 98 -41.886 -30.754 3.147 0.55 13.77 A O +ANISOU 963 O AGLN A 98 1609 1831 1791 -253 -183 -31 A O +ATOM 964 O BGLN A 98 -41.710 -30.277 2.478 0.45 20.66 A O +ANISOU 964 O BGLN A 98 1845 2475 3531 -479 -771 186 A O +ATOM 965 CB AGLN A 98 -40.864 -27.635 3.733 0.55 16.96 A C +ANISOU 965 CB AGLN A 98 1760 1937 2746 407 -585 -64 A C +ATOM 966 CB BGLN A 98 -40.729 -27.509 3.794 0.45 19.70 A C +ANISOU 966 CB BGLN A 98 2038 2406 3041 144 -427 47 A C +ATOM 967 CG AGLN A 98 -42.165 -27.385 3.012 0.55 20.36 A C +ANISOU 967 CG AGLN A 98 2263 2462 3011 32 -675 30 A C +ATOM 968 CG BGLN A 98 -41.816 -27.126 2.819 0.45 22.48 A C +ANISOU 968 CG BGLN A 98 2521 2839 3183 128 -515 55 A C +ATOM 969 CD AGLN A 98 -42.139 -26.073 2.256 0.55 23.34 A C +ANISOU 969 CD AGLN A 98 2860 2712 3294 -145 -507 119 A C +ATOM 970 CD BGLN A 98 -41.814 -25.630 2.560 0.45 24.80 A C +ANISOU 970 CD BGLN A 98 2912 3045 3464 -52 -436 246 A C +ATOM 971 NE2AGLN A 98 -41.555 -26.090 1.062 0.55 24.15 A N +ANISOU 971 NE2AGLN A 98 3076 2630 3469 -114 -470 417 A N +ATOM 972 NE2BGLN A 98 -41.548 -25.239 1.321 0.45 26.52 A N +ANISOU 972 NE2BGLN A 98 3198 3124 3755 -290 -355 326 A N +ATOM 973 OE1AGLN A 98 -42.618 -25.052 2.745 0.55 25.26 A O +ANISOU 973 OE1AGLN A 98 3201 2919 3478 -184 -516 -195 A O +ATOM 974 OE1BGLN A 98 -42.021 -24.835 3.474 0.45 26.41 A O +ANISOU 974 OE1BGLN A 98 3153 3220 3663 -100 -449 339 A O +ATOM 975 N AGLU A 99 -39.804 -30.260 2.444 0.52 12.67 A N +ANISOU 975 N AGLU A 99 1689 1494 1632 2 -486 -147 A N +ATOM 976 N BGLU A 99 -39.466 -30.177 2.352 0.48 16.65 A N +ANISOU 976 N BGLU A 99 1713 1973 2641 -74 -793 96 A N +ATOM 977 CA AGLU A 99 -39.854 -31.147 1.289 0.52 13.81 A C +ANISOU 977 CA AGLU A 99 1955 1696 1594 -18 -491 -127 A C +ATOM 978 CA BGLU A 99 -39.401 -31.009 1.156 0.48 16.47 A C +ANISOU 978 CA BGLU A 99 1916 1920 2421 -196 -1003 250 A C +ATOM 979 C AGLU A 99 -39.709 -32.614 1.676 0.52 13.49 A C +ANISOU 979 C AGLU A 99 1819 1700 1606 -120 -529 -168 A C +ATOM 980 C BGLU A 99 -39.308 -32.500 1.460 0.48 15.29 A C +ANISOU 980 C BGLU A 99 1933 1742 2136 -314 -953 -3 A C +ATOM 981 O AGLU A 99 -40.372 -33.479 1.090 0.52 14.58 A O +ANISOU 981 O AGLU A 99 1926 1783 1831 -347 -628 -53 A O +ATOM 982 O BGLU A 99 -39.742 -33.314 0.633 0.48 15.41 A O +ANISOU 982 O BGLU A 99 1975 1786 2095 -275 -999 255 A O +ATOM 983 CB AGLU A 99 -38.737 -30.768 0.317 0.52 15.39 A C +ANISOU 983 CB AGLU A 99 2508 1983 1356 -123 -644 -217 A C +ATOM 984 CB BGLU A 99 -38.191 -30.620 0.297 0.48 17.31 A C +ANISOU 984 CB BGLU A 99 2255 1935 2387 -344 -1159 448 A C +ATOM 985 CG AGLU A 99 -38.862 -29.377 -0.260 0.52 19.24 A C +ANISOU 985 CG AGLU A 99 2926 2429 1956 -296 -657 -50 A C +ATOM 986 CG BGLU A 99 -38.262 -29.253 -0.372 0.48 19.43 A C +ANISOU 986 CG BGLU A 99 2640 2291 2450 -195 -1303 554 A C +ATOM 987 CD AGLU A 99 -40.149 -29.202 -1.023 0.52 21.15 A C +ANISOU 987 CD AGLU A 99 3088 2725 2224 -36 -680 95 A C +ATOM 988 CD BGLU A 99 -36.967 -28.894 -1.089 0.48 23.00 A C +ANISOU 988 CD BGLU A 99 3273 2710 2757 -38 -1112 523 A C +ATOM 989 OE1AGLU A 99 -40.482 -30.099 -1.826 0.52 21.35 A O +ANISOU 989 OE1AGLU A 99 3079 3033 2002 188 -884 31 A O +ATOM 990 OE1BGLU A 99 -35.987 -29.659 -0.964 0.48 25.52 A O +ANISOU 990 OE1BGLU A 99 3469 2906 3321 9 -859 559 A O +ATOM 991 OE2AGLU A 99 -40.834 -28.182 -0.805 0.52 22.42 A O +ANISOU 991 OE2AGLU A 99 3081 2833 2604 235 -927 -5 A O +ATOM 992 OE2BGLU A 99 -36.924 -27.851 -1.776 0.48 23.46 A O +ANISOU 992 OE2BGLU A 99 3575 2837 2501 -284 -838 239 A O +ATOM 993 N AHIS A 100 -38.842 -32.917 2.647 0.55 12.63 A N +ANISOU 993 N AHIS A 100 1756 1615 1429 46 -519 -215 A N +ATOM 994 N BHIS A 100 -38.753 -32.886 2.622 0.45 13.72 A N +ANISOU 994 N BHIS A 100 1837 1582 1794 -86 -726 -107 A N +ATOM 995 CA AHIS A 100 -38.364 -34.279 2.841 0.55 12.38 A C +ANISOU 995 CA AHIS A 100 1649 1618 1436 -11 -189 -121 A C +ATOM 996 CA BHIS A 100 -38.361 -34.276 2.827 0.45 12.81 A C +ANISOU 996 CA BHIS A 100 1703 1604 1561 -105 -332 -91 A C +ATOM 997 C AHIS A 100 -38.678 -34.891 4.196 0.55 12.67 A C +ANISOU 997 C AHIS A 100 1604 1676 1534 -57 -314 -145 A C +ATOM 998 C BHIS A 100 -38.677 -34.883 4.189 0.45 12.79 A C +ANISOU 998 C BHIS A 100 1645 1652 1564 -68 -333 -131 A C +ATOM 999 O AHIS A 100 -38.311 -36.050 4.418 0.55 12.79 A O +ANISOU 999 O AHIS A 100 1757 1554 1547 -121 -379 -96 A O +ATOM 1000 O BHIS A 100 -38.305 -36.040 4.407 0.45 13.03 A O +ANISOU 1000 O BHIS A 100 1816 1535 1598 -68 -352 -126 A O +ATOM 1001 CB AHIS A 100 -36.848 -34.363 2.629 0.55 13.11 A C +ANISOU 1001 CB AHIS A 100 1734 1751 1497 -15 -39 -74 A C +ATOM 1002 CB BHIS A 100 -36.856 -34.468 2.573 0.45 13.14 A C +ANISOU 1002 CB BHIS A 100 1728 1725 1541 -250 -256 -99 A C +ATOM 1003 CG AHIS A 100 -36.384 -33.830 1.312 0.55 15.39 A C +ANISOU 1003 CG AHIS A 100 2113 2175 1561 95 -139 30 A C +ATOM 1004 CG BHIS A 100 -36.370 -33.883 1.286 0.45 15.30 A C +ANISOU 1004 CG BHIS A 100 2098 2134 1583 14 -176 27 A C +ATOM 1005 CD2AHIS A 100 -35.580 -32.783 1.015 0.55 16.93 A C +ANISOU 1005 CD2AHIS A 100 2237 2346 1848 69 152 137 A C +ATOM 1006 CD2BHIS A 100 -35.553 -32.831 1.044 0.45 16.55 A C +ANISOU 1006 CD2BHIS A 100 2214 2297 1776 3 131 165 A C +ATOM 1007 ND1AHIS A 100 -36.731 -34.403 0.107 0.55 18.16 A N +ANISOU 1007 ND1AHIS A 100 2601 2513 1788 -26 71 -56 A N +ATOM 1008 ND1BHIS A 100 -36.700 -34.404 0.054 0.45 18.02 A N +ANISOU 1008 ND1BHIS A 100 2577 2483 1787 -32 26 -68 A N +ATOM 1009 CE1AHIS A 100 -36.168 -33.723 -0.877 0.55 19.11 A C +ANISOU 1009 CE1AHIS A 100 2600 2559 2103 -126 117 67 A C +ATOM 1010 CE1BHIS A 100 -36.119 -33.689 -0.893 0.45 18.79 A C +ANISOU 1010 CE1BHIS A 100 2573 2534 2034 -111 85 52 A C +ATOM 1011 NE2AHIS A 100 -35.463 -32.736 -0.353 0.55 18.66 A N +ANISOU 1011 NE2AHIS A 100 2500 2542 2047 -41 198 131 A N +ATOM 1012 NE2BHIS A 100 -35.415 -32.729 -0.318 0.45 18.10 A N +ANISOU 1012 NE2BHIS A 100 2444 2503 1930 -63 147 142 A N +ATOM 1013 N HIS A 101 -39.315 -34.168 5.116 1.00 12.46 A N +ANISOU 1013 N HIS A 101 1554 1646 1534 -137 -275 -139 A N +ATOM 1014 CA HIS A 101 -39.597 -34.774 6.416 1.00 12.74 A C +ANISOU 1014 CA HIS A 101 1709 1649 1482 -142 -273 -214 A C +ATOM 1015 C HIS A 101 -40.438 -36.037 6.257 1.00 12.59 A C +ANISOU 1015 C HIS A 101 1567 1698 1520 -12 -383 -190 A C +ATOM 1016 O HIS A 101 -41.279 -36.147 5.362 1.00 13.84 A O +ANISOU 1016 O HIS A 101 1563 1897 1798 15 -509 -306 A O +ATOM 1017 CB HIS A 101 -40.285 -33.802 7.377 1.00 13.87 A C +ANISOU 1017 CB HIS A 101 1787 1667 1816 -229 -132 -391 A C +ATOM 1018 CG HIS A 101 -41.729 -33.559 7.071 1.00 16.49 A C +ANISOU 1018 CG HIS A 101 1747 1974 2543 -54 12 -203 A C +ATOM 1019 CD2 HIS A 101 -42.335 -32.553 6.400 1.00 21.33 A C +ANISOU 1019 CD2 HIS A 101 2088 2398 3616 377 -414 279 A C +ATOM 1020 ND1 HIS A 101 -42.735 -34.413 7.473 1.00 19.09 A N +ANISOU 1020 ND1 HIS A 101 1744 2394 3117 17 -47 -261 A N +ATOM 1021 CE1 HIS A 101 -43.898 -33.945 7.059 1.00 23.77 A C +ANISOU 1021 CE1 HIS A 101 2154 2913 3965 222 -202 -64 A C +ATOM 1022 NE2 HIS A 101 -43.684 -32.816 6.408 1.00 23.99 A N +ANISOU 1022 NE2 HIS A 101 2006 2906 4201 457 -509 203 A N +ATOM 1023 N GLU A 102 -40.183 -37.006 7.125 1.00 12.64 A N +ANISOU 1023 N GLU A 102 1517 1568 1719 -166 -282 -178 A N +ATOM 1024 CA GLU A 102 -40.936 -38.245 7.129 1.00 12.79 A C +ANISOU 1024 CA GLU A 102 1518 1628 1714 -132 -90 -227 A C +ATOM 1025 C GLU A 102 -42.215 -38.081 7.950 1.00 13.36 A C +ANISOU 1025 C GLU A 102 1528 1744 1803 -9 -166 -171 A C +ATOM 1026 O GLU A 102 -42.471 -37.041 8.568 1.00 13.67 A O +ANISOU 1026 O GLU A 102 1650 1715 1831 61 -74 -147 A O +ATOM 1027 CB GLU A 102 -40.060 -39.399 7.613 1.00 13.67 A C +ANISOU 1027 CB GLU A 102 1548 1661 1987 127 -41 -243 A C +ATOM 1028 CG GLU A 102 -38.898 -39.673 6.671 1.00 14.53 A C +ANISOU 1028 CG GLU A 102 1748 1750 2021 98 -240 -176 A C +ATOM 1029 CD GLU A 102 -38.233 -41.015 6.887 1.00 16.01 A C +ANISOU 1029 CD GLU A 102 1849 1971 2263 28 -35 -168 A C +ATOM 1030 OE1 GLU A 102 -38.689 -41.780 7.762 1.00 16.61 A O +ANISOU 1030 OE1 GLU A 102 2038 1963 2312 -19 -112 -139 A O +ATOM 1031 OE2 GLU A 102 -37.252 -41.302 6.169 1.00 17.04 A O +ANISOU 1031 OE2 GLU A 102 2070 2159 2244 45 -27 -362 A O +ATOM 1032 N GLU A 103 -43.029 -39.135 7.960 1.00 14.34 A N +ANISOU 1032 N GLU A 103 1444 1943 2060 -251 -105 -156 A N +ATOM 1033 CA GLU A 103 -44.309 -39.081 8.651 1.00 16.60 A C +ANISOU 1033 CA GLU A 103 1655 2343 2309 -374 -52 -234 A C +ATOM 1034 C GLU A 103 -44.167 -39.029 10.166 1.00 14.76 A C +ANISOU 1034 C GLU A 103 1451 1963 2192 -265 -6 -77 A C +ATOM 1035 O GLU A 103 -45.156 -38.745 10.853 1.00 16.57 A O +ANISOU 1035 O GLU A 103 1492 2380 2422 -147 -55 -138 A O +ATOM 1036 CB GLU A 103 -45.195 -40.242 8.201 1.00 20.67 A C +ANISOU 1036 CB GLU A 103 2113 2977 2764 -843 -243 -414 A C +ATOM 1037 CG GLU A 103 -45.610 -40.121 6.735 1.00 25.29 A C +ANISOU 1037 CG GLU A 103 2871 3568 3169 -920 -672 -424 A C +ATOM 1038 CD GLU A 103 -46.587 -41.193 6.288 1.00 32.41 A C +ANISOU 1038 CD GLU A 103 4043 4214 4057 -581 -637 -54 A C +ATOM 1039 OE1 GLU A 103 -46.850 -42.133 7.067 1.00 34.88 A O +ANISOU 1039 OE1 GLU A 103 4401 4282 4572 -738 -307 165 A O +ATOM 1040 OE2 GLU A 103 -47.097 -41.090 5.150 1.00 36.37 A O +ANISOU 1040 OE2 GLU A 103 4533 4684 4603 -348 -686 -88 A O +ATOM 1041 N ASP A 104 -42.973 -39.273 10.701 1.00 13.47 A N +ANISOU 1041 N ASP A 104 1435 1713 1972 -170 -65 -51 A N +ATOM 1042 CA ASP A 104 -42.720 -39.075 12.121 1.00 13.31 A C +ANISOU 1042 CA ASP A 104 1409 1627 2022 -210 84 12 A C +ATOM 1043 C ASP A 104 -42.331 -37.643 12.459 1.00 12.37 A C +ANISOU 1043 C ASP A 104 1192 1651 1858 -71 3 -1 A C +ATOM 1044 O ASP A 104 -41.978 -37.366 13.609 1.00 13.40 A O +ANISOU 1044 O ASP A 104 1259 1919 1914 -29 15 146 A O +ATOM 1045 CB ASP A 104 -41.665 -40.059 12.643 1.00 14.75 A C +ANISOU 1045 CB ASP A 104 1482 1748 2373 42 119 261 A C +ATOM 1046 CG ASP A 104 -40.315 -39.902 11.966 1.00 14.28 A C +ANISOU 1046 CG ASP A 104 1556 1622 2246 138 -12 233 A C +ATOM 1047 OD1 ASP A 104 -40.150 -38.985 11.131 1.00 13.29 A O +ANISOU 1047 OD1 ASP A 104 1397 1612 2041 83 -25 47 A O +ATOM 1048 OD2 ASP A 104 -39.418 -40.713 12.275 1.00 15.17 A O +ANISOU 1048 OD2 ASP A 104 1624 1800 2339 229 188 420 A O +ATOM 1049 N PHE A 105 -42.383 -36.735 11.485 1.00 11.76 A N +ANISOU 1049 N PHE A 105 1124 1576 1769 -22 8 -55 A N +ATOM 1050 CA PHE A 105 -42.046 -35.325 11.648 1.00 12.34 A C +ANISOU 1050 CA PHE A 105 1362 1609 1718 -66 87 -158 A C +ATOM 1051 C PHE A 105 -40.552 -35.055 11.801 1.00 11.23 A C +ANISOU 1051 C PHE A 105 1276 1494 1495 68 -42 -72 A C +ATOM 1052 O PHE A 105 -40.178 -33.928 12.151 1.00 12.02 A O +ANISOU 1052 O PHE A 105 1330 1540 1698 81 -180 -163 A O +ATOM 1053 CB PHE A 105 -42.862 -34.637 12.750 1.00 14.21 A C +ANISOU 1053 CB PHE A 105 1444 1839 2117 60 342 -14 A C +ATOM 1054 CG PHE A 105 -44.340 -34.734 12.543 1.00 15.60 A C +ANISOU 1054 CG PHE A 105 1556 1906 2465 284 506 337 A C +ATOM 1055 CD1 PHE A 105 -44.953 -34.042 11.515 1.00 19.41 A C +ANISOU 1055 CD1 PHE A 105 1556 2816 3004 662 560 899 A C +ATOM 1056 CD2 PHE A 105 -45.115 -35.526 13.363 1.00 16.26 A C +ANISOU 1056 CD2 PHE A 105 1702 1948 2528 -195 546 80 A C +ATOM 1057 CE1 PHE A 105 -46.314 -34.124 11.315 1.00 21.60 A C +ANISOU 1057 CE1 PHE A 105 1751 3123 3332 652 411 920 A C +ATOM 1058 CE2 PHE A 105 -46.481 -35.616 13.169 1.00 16.59 A C +ANISOU 1058 CE2 PHE A 105 1584 2001 2717 8 521 38 A C +ATOM 1059 CZ PHE A 105 -47.081 -34.911 12.142 1.00 19.45 A C +ANISOU 1059 CZ PHE A 105 1661 2659 3069 437 612 571 A C +ATOM 1060 N PHE A 106 -39.690 -36.036 11.524 1.00 11.29 A N +ANISOU 1060 N PHE A 106 1247 1586 1457 -8 -8 50 A N +ATOM 1061 CA PHE A 106 -38.248 -35.827 11.512 1.00 11.29 A C +ANISOU 1061 CA PHE A 106 1143 1666 1480 10 -193 -39 A C +ATOM 1062 C PHE A 106 -37.718 -35.760 10.083 1.00 10.76 A C +ANISOU 1062 C PHE A 106 1150 1533 1404 35 -291 -50 A C +ATOM 1063 O PHE A 106 -38.268 -36.379 9.166 1.00 11.99 A O +ANISOU 1063 O PHE A 106 1298 1684 1574 -104 -272 -111 A O +ATOM 1064 CB PHE A 106 -37.518 -36.962 12.238 1.00 12.04 A C +ANISOU 1064 CB PHE A 106 1418 1788 1368 121 -91 116 A C +ATOM 1065 CG PHE A 106 -37.547 -36.852 13.740 1.00 11.59 A C +ANISOU 1065 CG PHE A 106 1299 1601 1502 128 -131 228 A C +ATOM 1066 CD1 PHE A 106 -38.660 -37.256 14.462 1.00 13.29 A C +ANISOU 1066 CD1 PHE A 106 1467 2053 1529 -113 -28 49 A C +ATOM 1067 CD2 PHE A 106 -36.448 -36.364 14.438 1.00 11.23 A C +ANISOU 1067 CD2 PHE A 106 1263 1512 1493 145 -107 53 A C +ATOM 1068 CE1 PHE A 106 -38.679 -37.167 15.844 1.00 14.02 A C +ANISOU 1068 CE1 PHE A 106 1425 2323 1580 13 81 58 A C +ATOM 1069 CE2 PHE A 106 -36.468 -36.275 15.833 1.00 11.81 A C +ANISOU 1069 CE2 PHE A 106 1440 1468 1578 250 -188 74 A C +ATOM 1070 CZ PHE A 106 -37.587 -36.674 16.532 1.00 12.79 A C +ANISOU 1070 CZ PHE A 106 1459 1848 1551 123 10 110 A C +ATOM 1071 N LEU A 107 -36.641 -34.991 9.908 1.00 10.65 A N +ANISOU 1071 N LEU A 107 1282 1423 1341 -74 -69 -59 A N +ATOM 1072 CA LEU A 107 -35.815 -35.015 8.707 1.00 10.38 A C +ANISOU 1072 CA LEU A 107 1260 1312 1373 124 -142 -43 A C +ATOM 1073 C LEU A 107 -34.621 -35.925 8.965 1.00 10.46 A C +ANISOU 1073 C LEU A 107 1406 1274 1296 49 -199 -134 A C +ATOM 1074 O LEU A 107 -34.026 -35.875 10.041 1.00 12.06 A O +ANISOU 1074 O LEU A 107 1718 1562 1300 341 -447 -239 A O +ATOM 1075 CB LEU A 107 -35.305 -33.602 8.420 1.00 10.77 A C +ANISOU 1075 CB LEU A 107 1297 1408 1385 153 -114 -73 A C +ATOM 1076 CG LEU A 107 -34.315 -33.414 7.265 1.00 10.95 A C +ANISOU 1076 CG LEU A 107 1361 1564 1236 -18 -82 -12 A C +ATOM 1077 CD1 LEU A 107 -34.925 -33.805 5.918 1.00 12.04 A C +ANISOU 1077 CD1 LEU A 107 1648 1748 1177 19 -121 -11 A C +ATOM 1078 CD2 LEU A 107 -33.778 -31.983 7.242 1.00 12.54 A C +ANISOU 1078 CD2 LEU A 107 1597 1726 1442 -25 -178 89 A C +ATOM 1079 N TYR A 108 -34.271 -36.751 7.978 1.00 10.37 A N +ANISOU 1079 N TYR A 108 1290 1305 1345 88 -169 -138 A N +ATOM 1080 CA TYR A 108 -33.201 -37.740 8.103 1.00 10.61 A C +ANISOU 1080 CA TYR A 108 1477 1344 1212 104 -151 -88 A C +ATOM 1081 C TYR A 108 -32.057 -37.364 7.168 1.00 10.57 A C +ANISOU 1081 C TYR A 108 1539 1315 1163 160 -228 -48 A C +ATOM 1082 O TYR A 108 -32.260 -37.237 5.957 1.00 12.03 A O +ANISOU 1082 O TYR A 108 1554 1756 1262 66 -268 -61 A O +ATOM 1083 CB TYR A 108 -33.733 -39.144 7.781 1.00 11.05 A C +ANISOU 1083 CB TYR A 108 1570 1311 1319 -31 -145 -79 A C +ATOM 1084 CG TYR A 108 -34.597 -39.721 8.882 1.00 11.27 A C +ANISOU 1084 CG TYR A 108 1444 1384 1454 126 -93 -173 A C +ATOM 1085 CD1 TYR A 108 -35.923 -39.336 9.034 1.00 11.58 A C +ANISOU 1085 CD1 TYR A 108 1312 1377 1712 31 -28 -186 A C +ATOM 1086 CD2 TYR A 108 -34.074 -40.629 9.789 1.00 11.54 A C +ANISOU 1086 CD2 TYR A 108 1565 1372 1448 103 -161 -191 A C +ATOM 1087 CE1 TYR A 108 -36.699 -39.842 10.063 1.00 12.39 A C +ANISOU 1087 CE1 TYR A 108 1428 1432 1849 -68 21 -111 A C +ATOM 1088 CE2 TYR A 108 -34.836 -41.143 10.809 1.00 11.90 A C +ANISOU 1088 CE2 TYR A 108 1567 1422 1532 75 -3 -192 A C +ATOM 1089 CZ TYR A 108 -36.149 -40.744 10.948 1.00 12.42 A C +ANISOU 1089 CZ TYR A 108 1572 1406 1743 86 -71 -113 A C +ATOM 1090 OH TYR A 108 -36.910 -41.259 11.975 1.00 13.21 A O +ANISOU 1090 OH TYR A 108 1633 1586 1800 55 94 46 A O +ATOM 1091 N ILE A 109 -30.858 -37.207 7.728 1.00 10.47 A N +ANISOU 1091 N ILE A 109 1460 1351 1166 178 -150 25 A N +ATOM 1092 CA ILE A 109 -29.668 -36.823 6.976 1.00 10.62 A C +ANISOU 1092 CA ILE A 109 1353 1403 1281 148 -115 17 A C +ATOM 1093 C ILE A 109 -28.574 -37.848 7.237 1.00 10.10 A C +ANISOU 1093 C ILE A 109 1307 1398 1134 210 -164 -44 A C +ATOM 1094 O ILE A 109 -28.267 -38.151 8.397 1.00 11.03 A O +ANISOU 1094 O ILE A 109 1498 1514 1178 322 -103 -20 A O +ATOM 1095 CB ILE A 109 -29.159 -35.432 7.408 1.00 11.84 A C +ANISOU 1095 CB ILE A 109 1470 1396 1634 226 -26 -48 A C +ATOM 1096 CG1 ILE A 109 -30.200 -34.356 7.148 1.00 14.48 A C +ANISOU 1096 CG1 ILE A 109 1740 1663 2098 426 -382 -236 A C +ATOM 1097 CG2 ILE A 109 -27.850 -35.094 6.712 1.00 14.16 A C +ANISOU 1097 CG2 ILE A 109 1646 1552 2181 -50 179 -143 A C +ATOM 1098 CD1 ILE A 109 -29.742 -33.016 7.625 1.00 18.08 A C +ANISOU 1098 CD1 ILE A 109 2035 2037 2797 381 -421 -419 A C +ATOM 1099 N ALA A 110 -27.959 -38.347 6.170 1.00 10.47 A N +ANISOU 1099 N ALA A 110 1431 1375 1171 229 -60 11 A N +ATOM 1100 CA ALA A 110 -26.750 -39.147 6.286 1.00 11.06 A C +ANISOU 1100 CA ALA A 110 1481 1502 1217 343 5 9 A C +ATOM 1101 C ALA A 110 -25.554 -38.304 5.870 1.00 10.62 A C +ANISOU 1101 C ALA A 110 1396 1666 972 259 31 60 A C +ATOM 1102 O ALA A 110 -25.652 -37.465 4.973 1.00 11.79 A O +ANISOU 1102 O ALA A 110 1541 1805 1135 129 -74 340 A O +ATOM 1103 CB ALA A 110 -26.837 -40.397 5.408 1.00 13.15 A C +ANISOU 1103 CB ALA A 110 1751 1487 1757 399 80 -37 A C +ATOM 1104 N TYR A 111 -24.411 -38.533 6.511 1.00 11.04 A N +ANISOU 1104 N TYR A 111 1484 1593 1117 372 -2 151 A N +ATOM 1105 CA TYR A 111 -23.183 -37.874 6.089 1.00 10.90 A C +ANISOU 1105 CA TYR A 111 1366 1550 1226 200 112 204 A C +ATOM 1106 C TYR A 111 -22.108 -38.898 5.746 1.00 10.64 A C +ANISOU 1106 C TYR A 111 1349 1566 1128 361 63 153 A C +ATOM 1107 O TYR A 111 -22.089 -40.011 6.282 1.00 11.67 A O +ANISOU 1107 O TYR A 111 1553 1562 1319 477 103 168 A O +ATOM 1108 CB TYR A 111 -22.684 -36.817 7.103 1.00 11.42 A C +ANISOU 1108 CB TYR A 111 1461 1590 1287 200 -76 143 A C +ATOM 1109 CG TYR A 111 -22.096 -37.358 8.378 1.00 11.21 A C +ANISOU 1109 CG TYR A 111 1465 1510 1284 279 91 121 A C +ATOM 1110 CD1 TYR A 111 -22.905 -37.646 9.467 1.00 11.53 A C +ANISOU 1110 CD1 TYR A 111 1463 1642 1277 144 82 138 A C +ATOM 1111 CD2 TYR A 111 -20.724 -37.547 8.510 1.00 11.35 A C +ANISOU 1111 CD2 TYR A 111 1477 1465 1370 258 -43 131 A C +ATOM 1112 CE1 TYR A 111 -22.369 -38.132 10.651 1.00 11.84 A C +ANISOU 1112 CE1 TYR A 111 1402 1808 1287 226 -23 -23 A C +ATOM 1113 CE2 TYR A 111 -20.175 -38.039 9.686 1.00 11.25 A C +ANISOU 1113 CE2 TYR A 111 1433 1481 1362 214 -46 -10 A C +ATOM 1114 CZ TYR A 111 -21.005 -38.331 10.759 1.00 11.12 A C +ANISOU 1114 CZ TYR A 111 1465 1476 1285 211 -14 111 A C +ATOM 1115 OH TYR A 111 -20.497 -38.815 11.945 1.00 12.00 A O +ANISOU 1115 OH TYR A 111 1510 1726 1324 267 48 177 A O +ATOM 1116 N SER A 112 -21.199 -38.500 4.862 1.00 11.49 A N +ANISOU 1116 N SER A 112 1480 1718 1167 305 165 155 A N +ATOM 1117 CA SER A 112 -20.225 -39.436 4.331 1.00 11.97 A C +ANISOU 1117 CA SER A 112 1619 1661 1267 263 126 21 A C +ATOM 1118 C SER A 112 -19.015 -38.688 3.789 1.00 12.03 A C +ANISOU 1118 C SER A 112 1568 1842 1161 379 7 30 A C +ATOM 1119 O SER A 112 -19.060 -37.475 3.554 1.00 13.10 A O +ANISOU 1119 O SER A 112 1670 1847 1460 360 84 166 A O +ATOM 1120 CB SER A 112 -20.847 -40.272 3.208 1.00 13.62 A C +ANISOU 1120 CB SER A 112 1705 1987 1484 197 143 -51 A C +ATOM 1121 OG SER A 112 -19.937 -41.253 2.756 1.00 14.56 A O +ANISOU 1121 OG SER A 112 1863 2183 1485 150 253 -214 A O +ATOM 1122 N ASP A 113 -17.933 -39.443 3.582 1.00 11.90 A N +ANISOU 1122 N ASP A 113 1538 1852 1132 381 26 -32 A N +ATOM 1123 CA ASP A 113 -16.775 -38.969 2.842 1.00 13.92 A C +ANISOU 1123 CA ASP A 113 1671 2357 1261 318 131 149 A C +ATOM 1124 C ASP A 113 -16.845 -39.320 1.360 1.00 14.81 A C +ANISOU 1124 C ASP A 113 1816 2508 1305 602 304 222 A C +ATOM 1125 O ASP A 113 -15.921 -38.980 0.613 1.00 18.00 A O +ANISOU 1125 O ASP A 113 1952 3105 1780 356 625 293 A O +ATOM 1126 CB ASP A 113 -15.471 -39.503 3.454 1.00 16.99 A C +ANISOU 1126 CB ASP A 113 1693 2919 1842 480 -152 -6 A C +ATOM 1127 CG ASP A 113 -15.433 -41.020 3.564 1.00 20.33 A C +ANISOU 1127 CG ASP A 113 1953 3526 2245 1204 30 198 A C +ATOM 1128 OD1 ASP A 113 -16.429 -41.704 3.261 1.00 19.10 A O +ANISOU 1128 OD1 ASP A 113 2404 2976 1876 1223 140 539 A O +ATOM 1129 OD2 ASP A 113 -14.376 -41.540 3.974 1.00 26.79 A O +ANISOU 1129 OD2 ASP A 113 2451 4270 3458 1247 -264 84 A O +ATOM 1130 N AGLU A 114 -17.931 -39.943 0.904 0.54 14.36 A N +ANISOU 1130 N AGLU A 114 1802 2470 1182 712 -27 153 A N +ATOM 1131 N BGLU A 114 -17.893 -40.023 0.939 0.46 15.05 A N +ANISOU 1131 N BGLU A 114 1911 2578 1231 617 251 -11 A N +ATOM 1132 CA AGLU A 114 -18.125 -40.274 -0.501 0.54 15.12 A C +ANISOU 1132 CA AGLU A 114 2158 2456 1132 850 -140 122 A C +ATOM 1133 CA BGLU A 114 -18.051 -40.498 -0.426 0.46 16.33 A C +ANISOU 1133 CA BGLU A 114 2367 2603 1236 674 89 -257 A C +ATOM 1134 C AGLU A 114 -19.384 -39.589 -1.024 0.54 12.40 A C +ANISOU 1134 C AGLU A 114 1786 1849 1078 382 -78 84 A C +ATOM 1135 C BGLU A 114 -19.087 -39.650 -1.152 0.46 14.84 A C +ANISOU 1135 C BGLU A 114 1943 2408 1288 589 -55 -187 A C +ATOM 1136 O AGLU A 114 -20.292 -39.251 -0.262 0.54 12.25 A O +ANISOU 1136 O AGLU A 114 1755 1697 1201 13 -3 190 A O +ATOM 1137 O BGLU A 114 -20.056 -39.174 -0.554 0.46 13.93 A O +ANISOU 1137 O BGLU A 114 1824 2231 1239 629 -18 -253 A O +ATOM 1138 CB AGLU A 114 -18.225 -41.795 -0.697 0.54 20.03 A C +ANISOU 1138 CB AGLU A 114 2841 2967 1802 1200 -275 25 A C +ATOM 1139 CB BGLU A 114 -18.494 -41.966 -0.447 0.46 18.33 A C +ANISOU 1139 CB BGLU A 114 3026 2594 1344 814 63 -633 A C +ATOM 1140 CG AGLU A 114 -17.827 -42.284 -2.082 0.54 26.19 A C +ANISOU 1140 CG AGLU A 114 3590 3743 2617 948 -234 170 A C +ATOM 1141 CG BGLU A 114 -17.630 -42.882 -1.307 0.46 21.30 A C +ANISOU 1141 CG BGLU A 114 3585 2816 1692 758 212 -656 A C +ATOM 1142 CD AGLU A 114 -17.715 -43.797 -2.161 0.54 30.59 A C +ANISOU 1142 CD AGLU A 114 4052 4351 3221 732 53 7 A C +ATOM 1143 CD BGLU A 114 -17.574 -42.453 -2.765 0.46 22.99 A C +ANISOU 1143 CD BGLU A 114 3692 3093 1952 583 599 -732 A C +ATOM 1144 OE1AGLU A 114 -18.151 -44.479 -1.210 0.54 32.19 A O +ANISOU 1144 OE1AGLU A 114 4195 4526 3508 551 -10 65 A O +ATOM 1145 OE1BGLU A 114 -16.808 -41.520 -3.082 0.46 23.83 A O +ANISOU 1145 OE1BGLU A 114 3733 3015 2306 476 450 -938 A O +ATOM 1146 OE2AGLU A 114 -17.189 -44.304 -3.174 0.54 32.73 A O +ANISOU 1146 OE2AGLU A 114 4288 4626 3523 696 259 -19 A O +ATOM 1147 OE2BGLU A 114 -18.301 -43.043 -3.592 0.46 24.73 A O +ANISOU 1147 OE2BGLU A 114 3633 3410 2354 318 798 -269 A O +ATOM 1148 N ASER A 115 -19.432 -39.386 -2.344 0.54 11.90 A N +ANISOU 1148 N ASER A 115 1884 1565 1073 299 -74 95 A N +ATOM 1149 N BSER A 115 -18.882 -39.485 -2.455 0.46 14.11 A N +ANISOU 1149 N BSER A 115 1898 2229 1232 540 -188 80 A N +ATOM 1150 CA ASER A 115 -20.519 -38.645 -2.981 0.54 11.36 A C +ANISOU 1150 CA ASER A 115 1770 1336 1209 181 -75 -19 A C +ATOM 1151 CA BSER A 115 -19.682 -38.574 -3.262 0.46 14.16 A C +ANISOU 1151 CA BSER A 115 1992 2045 1341 421 -200 32 A C +ATOM 1152 C ASER A 115 -21.673 -39.536 -3.416 0.54 11.17 A C +ANISOU 1152 C ASER A 115 1797 1482 966 66 12 -74 A C +ATOM 1153 C BSER A 115 -20.928 -39.224 -3.851 0.46 14.31 A C +ANISOU 1153 C BSER A 115 2112 1903 1423 650 -290 -161 A C +ATOM 1154 O ASER A 115 -22.657 -39.032 -3.966 0.54 11.50 A O +ANISOU 1154 O ASER A 115 1643 1566 1160 -51 292 216 A O +ATOM 1155 O BSER A 115 -21.726 -38.529 -4.491 0.46 15.52 A O +ANISOU 1155 O BSER A 115 2209 2053 1634 611 -498 -330 A O +ATOM 1156 CB ASER A 115 -20.003 -37.840 -4.182 0.54 10.71 A C +ANISOU 1156 CB ASER A 115 1479 1376 1215 239 -55 -155 A C +ATOM 1157 CB BSER A 115 -18.830 -38.005 -4.394 0.46 13.06 A C +ANISOU 1157 CB BSER A 115 1777 1932 1254 267 -125 -110 A C +ATOM 1158 OG ASER A 115 -19.837 -38.660 -5.323 0.54 11.07 A O +ANISOU 1158 OG ASER A 115 1626 1591 988 81 112 68 A O +ATOM 1159 OG BSER A 115 -18.468 -39.028 -5.307 0.46 13.52 A O +ANISOU 1159 OG BSER A 115 1890 1948 1299 302 121 30 A O +ATOM 1160 N AVAL A 116 -21.576 -40.839 -3.187 0.54 12.51 A N +ANISOU 1160 N AVAL A 116 2007 1459 1287 262 220 -136 A N +ATOM 1161 N BVAL A 116 -21.094 -40.535 -3.664 0.46 15.78 A N +ANISOU 1161 N BVAL A 116 2468 1824 1705 305 166 -326 A N +ATOM 1162 CA AVAL A 116 -22.656 -41.781 -3.446 0.54 13.91 A C +ANISOU 1162 CA AVAL A 116 2444 1644 1199 286 274 390 A C +ATOM 1163 CA BVAL A 116 -22.234 -41.295 -4.167 0.46 21.26 A C +ANISOU 1163 CA BVAL A 116 3068 2596 2415 208 749 -297 A C +ATOM 1164 C AVAL A 116 -22.952 -42.492 -2.136 0.54 15.58 A C +ANISOU 1164 C AVAL A 116 2716 1831 1374 253 249 177 A C +ATOM 1165 C BVAL A 116 -22.587 -42.385 -3.164 0.46 24.66 A C +ANISOU 1165 C BVAL A 116 3453 2869 3049 -145 776 -260 A C +ATOM 1166 O AVAL A 116 -22.034 -42.985 -1.471 0.54 15.83 A O +ANISOU 1166 O AVAL A 116 2732 1709 1573 299 290 26 A O +ATOM 1167 O BVAL A 116 -21.997 -43.470 -3.186 0.46 25.51 A O +ANISOU 1167 O BVAL A 116 3449 2935 3307 -303 626 -495 A O +ATOM 1168 CB AVAL A 116 -22.266 -42.791 -4.539 0.54 17.46 A C +ANISOU 1168 CB AVAL A 116 3076 2064 1496 -362 -66 -251 A C +ATOM 1169 CB BVAL A 116 -21.936 -41.924 -5.541 0.46 23.17 A C +ANISOU 1169 CB BVAL A 116 3284 2930 2591 540 1085 -478 A C +ATOM 1170 CG1AVAL A 116 -23.376 -43.810 -4.737 0.54 18.13 A C +ANISOU 1170 CG1AVAL A 116 3258 1977 1656 -706 108 -534 A C +ATOM 1171 CG1BVAL A 116 -22.595 -41.138 -6.622 0.46 23.43 A C +ANISOU 1171 CG1BVAL A 116 3337 3010 2553 777 1359 -468 A C +ATOM 1172 CG2AVAL A 116 -21.943 -42.070 -5.850 0.54 19.17 A C +ANISOU 1172 CG2AVAL A 116 3304 2624 1357 -399 -202 -352 A C +ATOM 1173 CG2BVAL A 116 -20.435 -42.023 -5.785 0.46 23.86 A C +ANISOU 1173 CG2BVAL A 116 3397 2988 2681 591 1169 -436 A C +ATOM 1174 N ATYR A 117 -24.225 -42.533 -1.760 0.54 16.55 A N +ANISOU 1174 N ATYR A 117 2783 1848 1660 67 402 414 A N +ATOM 1175 N BTYR A 117 -23.550 -42.115 -2.290 0.46 26.45 A N +ANISOU 1175 N BTYR A 117 3900 2917 3235 -88 759 -337 A N +ATOM 1176 CA ATYR A 117 -24.604 -43.079 -0.464 0.54 19.62 A C +ANISOU 1176 CA ATYR A 117 3202 2151 2102 414 623 430 A C +ATOM 1177 CA BTYR A 117 -23.934 -43.090 -1.272 0.46 27.09 A C +ANISOU 1177 CA BTYR A 117 4076 2777 3442 -115 720 -349 A C +ATOM 1178 C ATYR A 117 -24.225 -44.548 -0.322 0.54 21.54 A C +ANISOU 1178 C ATYR A 117 3665 2209 2310 701 416 807 A C +ATOM 1179 C BTYR A 117 -25.160 -43.898 -1.686 0.46 26.09 A C +ANISOU 1179 C BTYR A 117 4131 2310 3472 -193 1013 -403 A C +ATOM 1180 O ATYR A 117 -23.634 -44.942 0.683 0.54 23.35 A O +ANISOU 1180 O ATYR A 117 4057 2357 2457 1145 343 607 A O +ATOM 1181 O BTYR A 117 -25.172 -45.126 -1.566 0.46 24.58 A O +ANISOU 1181 O BTYR A 117 4139 1740 3459 -241 1294 -619 A O +ATOM 1182 CB ATYR A 117 -26.101 -42.880 -0.208 0.54 21.49 A C +ANISOU 1182 CB ATYR A 117 3375 2436 2353 217 1009 227 A C +ATOM 1183 CB BTYR A 117 -24.183 -42.400 0.070 0.46 27.85 A C +ANISOU 1183 CB BTYR A 117 4114 2907 3562 -117 519 -373 A C +ATOM 1184 CG ATYR A 117 -26.593 -43.486 1.088 0.54 22.84 A C +ANISOU 1184 CG ATYR A 117 3569 2645 2466 -30 1284 142 A C +ATOM 1185 CD1ATYR A 117 -26.494 -42.790 2.287 0.54 23.10 A C +ANISOU 1185 CD1ATYR A 117 3630 2673 2474 -289 1528 34 A C +ATOM 1186 CD2ATYR A 117 -27.166 -44.751 1.111 0.54 23.52 A C +ANISOU 1186 CD2ATYR A 117 3779 2754 2403 -179 1342 181 A C +ATOM 1187 CE1ATYR A 117 -26.948 -43.342 3.474 0.54 24.00 A C +ANISOU 1187 CE1ATYR A 117 3981 2602 2535 -385 1381 -105 A C +ATOM 1188 CE2ATYR A 117 -27.620 -45.309 2.289 0.54 24.12 A C +ANISOU 1188 CE2ATYR A 117 3998 2756 2410 -114 1391 -6 A C +ATOM 1189 CZ ATYR A 117 -27.510 -44.601 3.467 0.54 24.88 A C +ANISOU 1189 CZ ATYR A 117 4120 2806 2528 -275 1370 -57 A C +ATOM 1190 OH ATYR A 117 -27.964 -45.154 4.643 0.54 26.43 A O +ANISOU 1190 OH ATYR A 117 4322 2999 2723 -357 1317 174 A O +TER +ATOM 1191 N AASP B 1 -18.961 -17.548 14.614 0.48 23.48 B N +ANISOU 1191 N AASP B 1 2514 3589 2818 -75 904 -345 B N +ATOM 1192 N BASP B 1 -21.193 -19.145 14.261 0.52 24.03 B N +ANISOU 1192 N BASP B 1 3011 3406 2712 512 679 82 B N +ATOM 1193 CA AASP B 1 -20.346 -17.106 14.730 0.48 22.35 B C +ANISOU 1193 CA AASP B 1 2596 3324 2571 -167 635 -163 B C +ATOM 1194 CA BASP B 1 -20.746 -17.862 14.788 0.52 22.73 B C +ANISOU 1194 CA BASP B 1 3045 3257 2334 389 631 -95 B C +ATOM 1195 C AASP B 1 -20.863 -17.397 16.141 0.48 19.47 B C +ANISOU 1195 C AASP B 1 2239 2855 2302 -240 279 -255 B C +ATOM 1196 C BASP B 1 -21.118 -17.721 16.265 0.52 22.34 B C +ANISOU 1196 C BASP B 1 2999 3092 2396 471 626 138 B C +ATOM 1197 O AASP B 1 -20.628 -18.479 16.681 0.48 21.24 B O +ANISOU 1197 O AASP B 1 2378 2936 2757 -432 37 -337 B O +ATOM 1198 O BASP B 1 -20.956 -18.665 17.036 0.52 23.88 B O +ANISOU 1198 O BASP B 1 3316 3147 2611 585 785 231 B O +ATOM 1199 CB AASP B 1 -21.209 -17.790 13.664 0.48 23.01 B C +ANISOU 1199 CB AASP B 1 2944 3360 2440 -193 463 183 B C +ATOM 1200 CB BASP B 1 -21.318 -16.707 13.956 0.52 21.31 B C +ANISOU 1200 CB BASP B 1 2993 3111 1992 335 356 -272 B C +ATOM 1201 CG AASP B 1 -22.614 -17.228 13.596 0.48 21.40 B C +ANISOU 1201 CG AASP B 1 2930 3085 2114 -384 492 346 B C +ATOM 1202 CG BASP B 1 -22.825 -16.780 13.806 0.52 22.02 B C +ANISOU 1202 CG BASP B 1 3153 3030 2184 522 121 -509 B C +ATOM 1203 OD1AASP B 1 -23.393 -17.476 14.534 0.48 16.32 B O +ANISOU 1203 OD1AASP B 1 2347 2452 1401 -772 382 534 B O +ATOM 1204 OD1BASP B 1 -23.445 -17.665 14.426 0.52 19.62 B O +ANISOU 1204 OD1BASP B 1 2950 2625 1879 433 122 -806 B O +ATOM 1205 OD2AASP B 1 -22.940 -16.536 12.607 0.48 24.24 B O +ANISOU 1205 OD2AASP B 1 3294 3595 2322 -196 763 268 B O +ATOM 1206 OD2BASP B 1 -23.392 -15.946 13.065 0.52 25.24 B O +ANISOU 1206 OD2BASP B 1 3480 3474 2638 494 -3 -69 B O +ATOM 1207 N AALA B 2 -21.562 -16.432 16.737 0.48 15.15 B N +ANISOU 1207 N AALA B 2 1640 2440 1676 -307 -14 -103 B N +ATOM 1208 N BALA B 2 -21.614 -16.552 16.660 0.52 20.23 B N +ANISOU 1208 N BALA B 2 2544 2903 2238 235 366 130 B N +ATOM 1209 CA AALA B 2 -21.931 -16.536 18.146 0.48 11.53 B C +ANISOU 1209 CA AALA B 2 1435 1725 1221 -229 -51 22 B C +ATOM 1210 CA BALA B 2 -22.002 -16.340 18.050 0.52 17.03 B C +ANISOU 1210 CA BALA B 2 2189 2367 1914 35 275 -2 B C +ATOM 1211 C AALA B 2 -23.363 -17.006 18.384 0.48 10.31 B C +ANISOU 1211 C AALA B 2 1451 1253 1211 3 -133 115 B C +ATOM 1212 C BALA B 2 -23.309 -17.057 18.363 0.52 12.56 B C +ANISOU 1212 C BALA B 2 1631 1747 1394 89 6 101 B C +ATOM 1213 O AALA B 2 -23.825 -17.018 19.523 0.48 11.58 B O +ANISOU 1213 O AALA B 2 1618 1400 1382 156 -218 -27 B O +ATOM 1214 O BALA B 2 -23.618 -17.312 19.522 0.52 11.22 B O +ANISOU 1214 O BALA B 2 1320 1752 1193 211 -69 86 B O +ATOM 1215 CB AALA B 2 -21.671 -15.220 18.872 0.48 11.07 B C +ANISOU 1215 CB AALA B 2 1251 1521 1434 -388 -170 -412 B C +ATOM 1216 CB BALA B 2 -22.119 -14.854 18.360 0.52 18.91 B C +ANISOU 1216 CB BALA B 2 2524 2520 2140 -196 276 -317 B C +HETATM 1217 N LE1 B 3 -24.066 -17.396 17.323 1.00 10.69 B N +ANISOU 1217 N LE1 B 3 1442 1277 1344 35 -99 -18 B N +HETATM 1218 CA LE1 B 3 -25.382 -18.066 17.499 1.00 10.13 B C +ANISOU 1218 CA LE1 B 3 1528 1128 1193 193 -167 -45 B C +HETATM 1219 C LE1 B 3 -25.310 -19.487 16.925 1.00 9.37 B C +ANISOU 1219 C LE1 B 3 1295 1166 1100 188 -180 -2 B C +HETATM 1220 O LE1 B 3 -25.669 -20.431 17.657 1.00 9.69 B O +ANISOU 1220 O LE1 B 3 1311 1195 1176 172 -138 -100 B O +HETATM 1221 CB LE1 B 3 -26.584 -17.209 17.019 1.00 10.44 B C +ANISOU 1221 CB LE1 B 3 1614 1194 1161 142 -102 -150 B C +HETATM 1222 SG LE1 B 3 -28.164 -18.046 17.471 1.00 10.40 B S +ANISOU 1222 SG LE1 B 3 1476 1230 1244 182 -213 -155 B S +HETATM 1223 C8 LE1 B 3 -26.580 -15.903 17.804 1.00 11.19 B C +ANISOU 1223 C8 LE1 B 3 1671 1262 1318 73 -8 -102 B C +HETATM 1224 C9 LE1 B 3 -26.534 -16.916 15.524 1.00 11.81 B C +ANISOU 1224 C9 LE1 B 3 1808 1323 1355 325 -230 -77 B C +ATOM 1225 N TYR B 4 -24.856 -19.639 15.686 1.00 9.94 B N +ANISOU 1225 N TYR B 4 1432 1223 1122 226 -63 -79 B N +ATOM 1226 CA TYR B 4 -24.805 -20.950 15.053 1.00 10.28 B C +ANISOU 1226 CA TYR B 4 1443 1190 1271 254 -108 -149 B C +ATOM 1227 C TYR B 4 -23.556 -21.705 15.499 1.00 10.20 B C +ANISOU 1227 C TYR B 4 1377 1250 1250 160 -59 -170 B C +ATOM 1228 O TYR B 4 -22.549 -21.762 14.790 1.00 12.57 B O +ANISOU 1228 O TYR B 4 1687 1678 1410 386 44 77 B O +ATOM 1229 CB TYR B 4 -24.855 -20.814 13.530 1.00 11.18 B C +ANISOU 1229 CB TYR B 4 1636 1529 1082 272 -172 0 B C +ATOM 1230 CG TYR B 4 -26.122 -20.165 13.018 1.00 11.21 B C +ANISOU 1230 CG TYR B 4 1605 1457 1197 187 -173 -17 B C +ATOM 1231 CD1 TYR B 4 -27.348 -20.817 13.103 1.00 12.25 B C +ANISOU 1231 CD1 TYR B 4 1707 1618 1331 208 -236 29 B C +ATOM 1232 CD2 TYR B 4 -26.093 -18.903 12.440 1.00 13.39 B C +ANISOU 1232 CD2 TYR B 4 1735 1789 1564 203 -186 116 B C +ATOM 1233 CE1 TYR B 4 -28.512 -20.221 12.630 1.00 12.64 B C +ANISOU 1233 CE1 TYR B 4 1764 1590 1447 217 -349 -18 B C +ATOM 1234 CE2 TYR B 4 -27.247 -18.301 11.962 1.00 13.99 B C +ANISOU 1234 CE2 TYR B 4 1883 1913 1522 264 -184 232 B C +ATOM 1235 CZ TYR B 4 -28.452 -18.966 12.053 1.00 13.35 B C +ANISOU 1235 CZ TYR B 4 1781 1900 1391 409 -315 84 B C +ATOM 1236 OH TYR B 4 -29.602 -18.368 11.581 1.00 16.33 B O +ANISOU 1236 OH TYR B 4 2078 2233 1894 605 -329 307 B O +ATOM 1237 N THR B 5 -23.635 -22.298 16.680 1.00 10.31 B N +ANISOU 1237 N THR B 5 1311 1274 1334 238 -177 -74 B N +ATOM 1238 CA THR B 5 -22.556 -23.077 17.266 1.00 10.03 B C +ANISOU 1238 CA THR B 5 1181 1226 1403 292 -228 -117 B C +ATOM 1239 C THR B 5 -22.956 -24.546 17.308 1.00 9.65 B C +ANISOU 1239 C THR B 5 1254 1258 1153 310 -204 -107 B C +ATOM 1240 O THR B 5 -24.107 -24.913 17.073 1.00 9.98 B O +ANISOU 1240 O THR B 5 1242 1204 1349 125 -244 -80 B O +ATOM 1241 CB THR B 5 -22.257 -22.605 18.691 1.00 10.12 B C +ANISOU 1241 CB THR B 5 1301 1176 1367 214 -142 -169 B C +ATOM 1242 CG2 THR B 5 -21.944 -21.116 18.728 1.00 11.07 B C +ANISOU 1242 CG2 THR B 5 1387 1273 1546 227 -152 -53 B C +ATOM 1243 OG1 THR B 5 -23.391 -22.887 19.519 1.00 10.19 B O +ANISOU 1243 OG1 THR B 5 1272 1197 1403 265 -122 -65 B O +ATOM 1244 N TRP B 6 -21.999 -25.407 17.655 1.00 9.62 B N +ANISOU 1244 N TRP B 6 1324 1154 1175 161 -120 -103 B N +ATOM 1245 CA TRP B 6 -22.338 -26.816 17.809 1.00 9.43 B C +ANISOU 1245 CA TRP B 6 1201 1195 1186 138 -159 -130 B C +ATOM 1246 C TRP B 6 -23.430 -27.005 18.860 1.00 9.42 B C +ANISOU 1246 C TRP B 6 1295 1066 1219 134 -233 -280 B C +ATOM 1247 O TRP B 6 -24.406 -27.732 18.634 1.00 9.56 B O +ANISOU 1247 O TRP B 6 1218 1093 1321 147 -217 -246 B O +ATOM 1248 CB TRP B 6 -21.094 -27.651 18.129 1.00 9.90 B C +ANISOU 1248 CB TRP B 6 1261 1198 1303 260 -227 -194 B C +ATOM 1249 CG TRP B 6 -21.431 -29.111 18.178 1.00 9.54 B C +ANISOU 1249 CG TRP B 6 1214 1218 1191 257 -61 -149 B C +ATOM 1250 CD1 TRP B 6 -21.502 -29.911 19.286 1.00 10.07 B C +ANISOU 1250 CD1 TRP B 6 1230 1096 1501 380 23 -108 B C +ATOM 1251 CD2 TRP B 6 -21.813 -29.925 17.069 1.00 9.69 B C +ANISOU 1251 CD2 TRP B 6 1224 1133 1325 340 -142 -177 B C +ATOM 1252 CE2 TRP B 6 -22.095 -31.212 17.568 1.00 9.69 B C +ANISOU 1252 CE2 TRP B 6 1206 1178 1297 332 -12 -242 B C +ATOM 1253 CE3 TRP B 6 -21.930 -29.693 15.694 1.00 11.34 B C +ANISOU 1253 CE3 TRP B 6 1661 1398 1249 461 -266 -288 B C +ATOM 1254 NE1 TRP B 6 -21.911 -31.175 18.929 1.00 10.54 B N +ANISOU 1254 NE1 TRP B 6 1308 1317 1381 322 -47 -221 B N +ATOM 1255 CZ2 TRP B 6 -22.510 -32.257 16.738 1.00 11.22 B C +ANISOU 1255 CZ2 TRP B 6 1436 1345 1480 370 -134 -179 B C +ATOM 1256 CZ3 TRP B 6 -22.329 -30.730 14.877 1.00 12.55 B C +ANISOU 1256 CZ3 TRP B 6 1824 1481 1463 397 -346 -409 B C +ATOM 1257 CH2 TRP B 6 -22.613 -31.995 15.399 1.00 12.07 B C +ANISOU 1257 CH2 TRP B 6 1601 1258 1727 331 -377 -388 B C +ATOM 1258 N GLU B 7 -23.303 -26.328 20.008 1.00 9.32 B N +ANISOU 1258 N GLU B 7 1167 1233 1141 102 -174 -113 B N +ATOM 1259 CA GLU B 7 -24.291 -26.516 21.065 1.00 9.14 B C +ANISOU 1259 CA GLU B 7 1158 1272 1043 121 -214 -58 B C +ATOM 1260 C GLU B 7 -25.668 -25.992 20.668 1.00 9.66 B C +ANISOU 1260 C GLU B 7 1226 1294 1150 106 -90 -274 B C +ATOM 1261 O GLU B 7 -26.682 -26.477 21.187 1.00 9.83 B O +ANISOU 1261 O GLU B 7 1229 1356 1151 7 -116 -161 B O +ATOM 1262 CB GLU B 7 -23.814 -25.887 22.373 1.00 10.20 B C +ANISOU 1262 CB GLU B 7 1253 1376 1248 240 -325 -98 B C +ATOM 1263 CG GLU B 7 -22.567 -26.537 22.935 1.00 11.94 B C +ANISOU 1263 CG GLU B 7 1504 1487 1546 147 -264 3 B C +ATOM 1264 CD GLU B 7 -22.699 -28.030 23.086 1.00 15.30 B C +ANISOU 1264 CD GLU B 7 1927 1867 2021 231 -520 95 B C +ATOM 1265 OE1 GLU B 7 -23.733 -28.480 23.614 1.00 19.03 B O +ANISOU 1265 OE1 GLU B 7 2409 1897 2927 129 -265 782 B O +ATOM 1266 OE2 GLU B 7 -21.766 -28.751 22.666 1.00 17.15 B O +ANISOU 1266 OE2 GLU B 7 2331 2053 2134 723 -820 -367 B O +ATOM 1267 N CYS B 8 -25.732 -25.008 19.762 1.00 9.37 B N +ANISOU 1267 N CYS B 8 1113 1225 1223 186 -226 -266 B N +ATOM 1268 CA CYS B 8 -27.018 -24.545 19.242 1.00 10.07 B C +ANISOU 1268 CA CYS B 8 1168 1295 1364 175 -229 -216 B C +ATOM 1269 C CYS B 8 -27.834 -25.701 18.674 1.00 9.76 B C +ANISOU 1269 C CYS B 8 1099 1346 1264 212 -190 -191 B C +ATOM 1270 O CYS B 8 -29.067 -25.702 18.777 1.00 10.05 B O +ANISOU 1270 O CYS B 8 1109 1291 1418 168 -207 -263 B O +ATOM 1271 CB CYS B 8 -26.769 -23.464 18.177 1.00 10.64 B C +ANISOU 1271 CB CYS B 8 1403 1269 1371 272 -268 -33 B C +ATOM 1272 SG CYS B 8 -28.178 -22.909 17.188 1.00 11.14 B S +ANISOU 1272 SG CYS B 8 1464 1350 1417 210 -324 -180 B S +ATOM 1273 N LEU B 9 -27.167 -26.698 18.085 1.00 9.59 B N +ANISOU 1273 N LEU B 9 1144 1268 1231 194 -283 -279 B N +ATOM 1274 CA LEU B 9 -27.856 -27.789 17.407 1.00 10.25 B C +ANISOU 1274 CA LEU B 9 1195 1386 1312 248 -313 -425 B C +ATOM 1275 C LEU B 9 -28.321 -28.889 18.351 1.00 10.21 B C +ANISOU 1275 C LEU B 9 1161 1228 1491 225 -244 -286 B C +ATOM 1276 O LEU B 9 -29.015 -29.814 17.914 1.00 11.03 B O +ANISOU 1276 O LEU B 9 1243 1310 1640 120 -290 -294 B O +ATOM 1277 CB LEU B 9 -26.937 -28.405 16.354 1.00 11.70 B C +ANISOU 1277 CB LEU B 9 1358 1575 1512 68 -265 -504 B C +ATOM 1278 CG LEU B 9 -26.195 -27.468 15.402 1.00 13.04 B C +ANISOU 1278 CG LEU B 9 1538 1816 1602 15 49 -496 B C +ATOM 1279 CD1 LEU B 9 -25.454 -28.286 14.356 1.00 14.97 B C +ANISOU 1279 CD1 LEU B 9 1811 2071 1807 -178 332 -676 B C +ATOM 1280 CD2 LEU B 9 -27.119 -26.456 14.746 1.00 13.48 B C +ANISOU 1280 CD2 LEU B 9 1563 2067 1491 197 -190 -138 B C +ATOM 1281 N ALA B 10 -27.933 -28.842 19.619 1.00 10.51 B N +ANISOU 1281 N ALA B 10 1457 1255 1280 188 -227 -186 B N +ATOM 1282 CA ALA B 10 -28.180 -29.963 20.511 1.00 11.80 B C +ANISOU 1282 CA ALA B 10 1511 1437 1534 174 -330 -151 B C +ATOM 1283 C ALA B 10 -29.664 -30.105 20.813 1.00 11.31 B C +ANISOU 1283 C ALA B 10 1479 1326 1494 209 -139 -123 B C +ATOM 1284 O ALA B 10 -30.378 -29.113 20.995 1.00 12.52 B O +ANISOU 1284 O ALA B 10 1622 1461 1673 366 15 -91 B O +ATOM 1285 CB ALA B 10 -27.409 -29.765 21.817 1.00 12.95 B C +ANISOU 1285 CB ALA B 10 1772 1487 1662 12 -489 -32 B C +ATOM 1286 N TRP B 11 -30.120 -31.353 20.873 1.00 11.46 B N +ANISOU 1286 N TRP B 11 1496 1414 1444 129 -138 -75 B N +ATOM 1287 CA TRP B 11 -31.478 -31.620 21.303 1.00 11.77 B C +ANISOU 1287 CA TRP B 11 1647 1381 1445 122 -128 -18 B C +ATOM 1288 C TRP B 11 -31.668 -31.063 22.710 1.00 13.48 B C +ANISOU 1288 C TRP B 11 1837 1804 1480 401 -181 -68 B C +ATOM 1289 O TRP B 11 -30.787 -31.224 23.562 1.00 15.87 B O +ANISOU 1289 O TRP B 11 1998 2481 1551 516 -380 -33 B O +ATOM 1290 CB TRP B 11 -31.717 -33.127 21.338 1.00 13.70 B C +ANISOU 1290 CB TRP B 11 1700 1701 1805 -183 -77 227 B C +ATOM 1291 CG TRP B 11 -33.163 -33.471 21.440 1.00 14.07 B C +ANISOU 1291 CG TRP B 11 1880 1948 1519 -194 -127 58 B C +ATOM 1292 CD1 TRP B 11 -33.868 -33.794 22.564 1.00 17.07 B C +ANISOU 1292 CD1 TRP B 11 1992 2659 1836 -267 -103 84 B C +ATOM 1293 CD2 TRP B 11 -34.094 -33.504 20.359 1.00 13.90 B C +ANISOU 1293 CD2 TRP B 11 1820 1638 1825 -127 -320 -71 B C +ATOM 1294 CE2 TRP B 11 -35.346 -33.865 20.890 1.00 15.56 B C +ANISOU 1294 CE2 TRP B 11 1854 2015 2045 -273 -162 -97 B C +ATOM 1295 CE3 TRP B 11 -33.986 -33.268 18.987 1.00 14.13 B C +ANISOU 1295 CE3 TRP B 11 2254 1390 1725 7 -481 -49 B C +ATOM 1296 NE1 TRP B 11 -35.184 -34.033 22.241 1.00 17.31 B N +ANISOU 1296 NE1 TRP B 11 1915 2742 1922 -462 93 19 B N +ATOM 1297 CZ2 TRP B 11 -36.484 -33.997 20.092 1.00 16.23 B C +ANISOU 1297 CZ2 TRP B 11 2007 1671 2490 -99 -288 36 B C +ATOM 1298 CZ3 TRP B 11 -35.103 -33.408 18.202 1.00 16.04 B C +ANISOU 1298 CZ3 TRP B 11 2484 1380 2230 -30 -656 -4 B C +ATOM 1299 CH2 TRP B 11 -36.336 -33.767 18.755 1.00 16.02 B C +ANISOU 1299 CH2 TRP B 11 2112 1350 2625 238 -566 185 B C +ATOM 1300 N PRO B 12 -32.794 -30.402 22.995 1.00 15.14 B N +ANISOU 1300 N PRO B 12 2073 2340 1342 408 36 -166 B N +ATOM 1301 CA PRO B 12 -32.969 -29.803 24.324 1.00 18.51 B C +ANISOU 1301 CA PRO B 12 2522 2908 1602 542 -59 -304 B C +ATOM 1302 C PRO B 12 -33.070 -30.836 25.445 1.00 23.19 B C +ANISOU 1302 C PRO B 12 3623 3513 1674 188 139 -254 B C +ATOM 1303 O PRO B 12 -33.542 -31.950 25.220 1.00 26.39 B O +ANISOU 1303 O PRO B 12 4321 3901 1806 -91 514 10 B O +ATOM 1304 CB PRO B 12 -34.268 -28.993 24.191 1.00 19.70 B C +ANISOU 1304 CB PRO B 12 2497 3008 1981 700 66 -478 B C +ATOM 1305 CG PRO B 12 -34.929 -29.482 22.961 1.00 18.14 B C +ANISOU 1305 CG PRO B 12 2269 2735 1887 618 99 -307 B C +ATOM 1306 CD PRO B 12 -33.882 -30.060 22.066 1.00 14.89 B C +ANISOU 1306 CD PRO B 12 1889 2285 1484 506 -42 -183 B C +TER +CONECT 1211 1217 1217 +CONECT 1212 1217 1217 +CONECT 1217 1211 1212 1218 1211 +CONECT 1217 1212 +CONECT 1218 1217 1219 1221 +CONECT 1219 1218 1220 1225 1225 +CONECT 1220 1219 +CONECT 1221 1218 1222 1223 1224 +CONECT 1222 1221 +CONECT 1223 1221 +CONECT 1224 1221 +CONECT 1225 1219 1219 +END diff --git a/rfdiffusion/Embeddings.py b/rfdiffusion/Embeddings.py index eb93910..be35948 100644 --- a/rfdiffusion/Embeddings.py +++ b/rfdiffusion/Embeddings.py @@ -8,6 +8,7 @@ from rfdiffusion.util_module import Dropout, create_custom_forward, rbf, init_le from rfdiffusion.Attention_module import Attention, FeedForwardLayer, AttentionWithBias from rfdiffusion.Track_module import PairStr2Pair import math +import numpy as np # Module contains classes and functions to generate initial embeddings diff --git a/rfdiffusion/util_module.py b/rfdiffusion/util_module.py index 19f3101..839b761 100644 --- a/rfdiffusion/util_module.py +++ b/rfdiffusion/util_module.py @@ -98,7 +98,7 @@ def rbf(D): RBF = torch.exp(-((D_expand - D_mu) / D_sigma)**2) return RBF -def get_seqsep(idx): +def get_seqsep(idx, cyclic=None): ''' Input: - idx: residue indices of given sequence (B,L)