*** ***
Job options:
ID = 23020803493855475
JOBID =
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
CRYST1 222.120 52.170 109.900 90.00 111.58 90.00 C 1 2 1 8
ATOM 1 N ALA A 2 -24.308 34.601 12.229 1.00 89.07 A N
ANISOU 1 N ALA A 2 10024 9120 14700 3618 6316 6527 A N
ATOM 2 CA ALA A 2 -23.197 34.350 11.317 1.00 87.80 A C
ANISOU 2 CA ALA A 2 9930 8928 14502 3483 6241 6448 A C
ATOM 3 C ALA A 2 -21.847 34.651 11.987 1.00 88.46 A C
ANISOU 3 C ALA A 2 10320 8308 14981 3225 6383 6040 A C
ATOM 4 O ALA A 2 -21.604 35.771 12.445 1.00 90.79 A O
ANISOU 4 O ALA A 2 10772 8079 15645 3369 6809 6097 A O
ATOM 5 CB ALA A 2 -23.357 35.185 10.051 1.00 92.53 A C
ANISOU 5 CB ALA A 2 10412 9719 15026 3909 6537 6999 A C
ATOM 6 N ASP A 3 -20.974 33.641 12.032 1.00 79.28 A N
ANISOU 6 N ASP A 3 9234 7158 13731 2844 6040 5621 A N
ATOM 7 CA ASP A 3 -19.634 33.716 12.616 1.00 75.69 A C
ANISOU 7 CA ASP A 3 9020 6164 13574 2568 6094 5187 A C
ATOM 8 C ASP A 3 -18.705 34.515 11.698 1.00 80.20 A C
ANISOU 8 C ASP A 3 9669 6478 14326 2687 6415 5350 A C
ATOM 9 O ASP A 3 -18.595 34.145 10.525 1.00 80.62 A O
ANISOU 9 O ASP A 3 9610 6887 14134 2752 6295 5554 A O
ATOM 10 CB ASP A 3 -19.095 32.285 12.821 1.00 72.81 A C
ANISOU 10 CB ASP A 3 8685 5988 12992 2185 5614 4751 A C
ATOM 11 CG ASP A 3 -17.914 32.139 13.757 1.00 69.96 A C
ANISOU 11 CG ASP A 3 8535 5175 12873 1890 5583 4244 A C
ATOM 12 OD1 ASP A 3 -17.049 33.039 13.765 1.00 67.63 A O
ANISOU 12 OD1 ASP A 3 8355 4458 12885 1909 5902 4188 A O
ATOM 13 OD2 ASP A 3 -17.823 31.088 14.437 1.00 71.17 A O1-
ANISOU 13 OD2 ASP A 3 8732 5421 12887 1638 5245 3898 A O1-
ATOM 14 N PRO A 4 -17.997 35.576 12.181 1.00 76.50 A N
ANISOU 14 N PRO A 4 9389 5404 14272 2689 6829 5240 A N
ATOM 15 CA PRO A 4 -17.109 36.323 11.267 1.00 77.43 A C
ANISOU 15 CA PRO A 4 9588 5269 14563 2784 7166 5394 A C
ATOM 16 C PRO A 4 -15.811 35.575 10.917 1.00 76.04 A C
ANISOU 16 C PRO A 4 9468 5083 14341 2456 6919 5021 A C
ATOM 17 O PRO A 4 -15.104 35.992 9.993 1.00 75.01 A O
ANISOU 17 O PRO A 4 9373 4847 14280 2516 7129 5156 A O
ATOM 18 CB PRO A 4 -16.806 37.606 12.040 1.00 81.50 A C
ANISOU 18 CB PRO A 4 10293 5136 15537 2831 7697 5327 A C
ATOM 19 CG PRO A 4 -16.918 37.226 13.469 1.00 83.55 A C
ANISOU 19 CG PRO A 4 10604 5263 15878 2579 7510 4887 A C
ATOM 20 CD PRO A 4 -18.017 36.190 13.531 1.00 77.81 A C
ANISOU 20 CD PRO A 4 9697 5106 14764 2609 7048 4982 A C
ATOM 21 N SER A 5 -15.508 34.466 11.650 1.00 67.34 A N
ANISOU 21 N SER A 5 8377 4095 13113 2131 6489 4566 A N
ATOM 22 CA SER A 5 -14.305 33.648 11.450 1.00 64.17 A C
ANISOU 22 CA SER A 5 8027 3711 12645 1835 6226 4189 A C
ATOM 23 C SER A 5 -14.525 32.538 10.421 1.00 65.43 A C
ANISOU 23 C SER A 5 8052 4415 12391 1825 5844 4320 A C
ATOM 24 O SER A 5 -13.563 31.921 9.986 1.00 62.85 A O
ANISOU 24 O SER A 5 7759 4135 11988 1641 5668 4099 A O
ATOM 25 CB SER A 5 -13.856 33.027 12.768 1.00 63.80 A C
ANISOU 25 CB SER A 5 8072 3511 12659 1534 5992 3656 A C
ATOM 26 OG SER A 5 -13.991 33.932 13.849 1.00 69.22 A O
ANISOU 26 OG SER A 5 8845 3799 13658 1545 6294 3540 A O
ATOM 27 N SER A 6 -15.784 32.305 10.027 1.00 62.17 A N
ANISOU 27 N SER A 6 7480 4432 11712 2019 5735 4668 A N
ATOM 28 CA SER A 6 -16.203 31.271 9.087 1.00 60.66 A C
ANISOU 28 CA SER A 6 7130 4818 11099 1999 5392 4791 A C
ATOM 29 C SER A 6 -16.814 31.897 7.816 1.00 69.67 A C
ANISOU 29 C SER A 6 8100 6284 12088 2349 5592 5346 A C
ATOM 30 O SER A 6 -17.228 33.056 7.834 1.00 72.54 A O
ANISOU 30 O SER A 6 8457 6464 12639 2650 5971 5681 A O
ATOM 31 CB SER A 6 -17.206 30.344 9.784 1.00 60.43 A C
ANISOU 31 CB SER A 6 7027 5099 10837 1881 5065 4665 A C
ATOM 32 OG SER A 6 -17.900 29.464 8.917 1.00 61.56 A O
ANISOU 32 OG SER A 6 6985 5841 10564 1870 4789 4810 A O
ATOM 33 N PHE A 7 -16.864 31.127 6.717 1.00 67.78 A N
ANISOU 33 N PHE A 7 7722 6536 11495 2322 5351 5444 A N
ATOM 34 CA PHE A 7 -17.484 31.508 5.434 1.00 71.34 A C
ANISOU 34 CA PHE A 7 7966 7442 11699 2645 5465 5955 A C
ATOM 35 C PHE A 7 -18.884 30.929 5.363 1.00 77.78 A C
ANISOU 35 C PHE A 7 8534 8875 12142 2715 5227 6119 A C
ATOM 36 O PHE A 7 -19.698 31.357 4.550 1.00 81.80 A O
ANISOU 36 O PHE A 7 8828 9811 12441 3044 5343 6576 A O
ATOM 37 CB PHE A 7 -16.673 30.976 4.239 1.00 72.97 A C
ANISOU 37 CB PHE A 7 8142 7878 11704 2550 5334 5934 A C
ATOM 38 CG PHE A 7 -15.408 31.710 3.879 1.00 75.56 A C
ANISOU 38 CG PHE A 7 8640 7740 12328 2573 5633 5925 A C
ATOM 39 CD1 PHE A 7 -15.456 32.897 3.158 1.00 83.02 A C
ANISOU 39 CD1 PHE A 7 9570 8581 13391 2936 6060 6389 A C
ATOM 40 CD2 PHE A 7 -14.165 31.171 4.180 1.00 75.30 A C
ANISOU 40 CD2 PHE A 7 8772 7413 12425 2243 5494 5465 A C
ATOM 41 CE1 PHE A 7 -14.279 33.558 2.785 1.00 84.84 A C
ANISOU 41 CE1 PHE A 7 9963 8378 13894 2929 6363 6369 A C
ATOM 42 CE2 PHE A 7 -12.991 31.827 3.805 1.00 78.93 A C
ANISOU 42 CE2 PHE A 7 9361 7488 13139 2240 5770 5437 A C
ATOM 43 CZ PHE A 7 -13.055 33.022 3.118 1.00 80.98 A C
ANISOU 43 CZ PHE A 7 9618 7614 13538 2564 6210 5878 A C
ATOM 44 N ALA A 8 -19.140 29.907 6.187 1.00 72.17 A N
ANISOU 44 N ALA A 8 7847 8245 11328 2400 4895 5736 A N
ATOM 45 CA ALA A 8 -20.398 29.181 6.239 1.00 72.83 A C
ANISOU 45 CA ALA A 8 7713 8899 11061 2360 4641 5776 A C
ATOM 46 C ALA A 8 -21.493 29.995 6.926 1.00 78.25 A C
ANISOU 46 C ALA A 8 8309 9572 11851 2628 4840 6035 A C
ATOM 47 O ALA A 8 -21.198 30.841 7.780 1.00 76.86 A O
ANISOU 47 O ALA A 8 8314 8828 12060 2713 5104 6006 A O
ATOM 48 CB ALA A 8 -20.194 27.865 6.963 1.00 70.19 A C
ANISOU 48 CB ALA A 8 7494 8538 10636 1928 4287 5266 A C
ATOM 49 N SER A 9 -22.751 29.758 6.527 1.00 77.47 A N
ANISOU 49 N SER A 9 7916 10122 11398 2758 4727 6279 A N
ATOM 50 CA SER A 9 -23.896 30.445 7.106 1.00 80.12 A C
ANISOU 50 CA SER A 9 8121 10550 11772 3032 4892 6545 A C
ATOM 51 C SER A 9 -24.717 29.450 7.949 1.00 82.32 A C
ANISOU 51 C SER A 9 8330 11075 11874 2735 4587 6236 A C
ATOM 52 O SER A 9 -25.414 28.596 7.385 1.00 82.64 A O
ANISOU 52 O SER A 9 8127 11771 11503 2609 4329 6221 A O
ATOM 53 CB SER A 9 -24.745 31.101 6.020 1.00 89.44 A C
ANISOU 53 CB SER A 9 8988 12315 12682 3480 5050 7116 A C
ATOM 54 OG SER A 9 -24.017 32.117 5.348 1.00103.62 A O
ANISOU 54 OG SER A 9 10885 13809 14678 3793 5399 7437 A O
ATOM 55 N PRO A 10 -24.623 29.517 9.300 1.00 76.72 A N
ANISOU 55 N PRO A 10 7831 9856 11462 2598 4623 5967 A N
ATOM 56 CA PRO A 10 -25.393 28.575 10.138 1.00 75.03 A C
ANISOU 56 CA PRO A 10 7573 9847 11088 2320 4361 5683 A C
ATOM 57 C PRO A 10 -26.899 28.854 10.123 1.00 83.31 A C
ANISOU 57 C PRO A 10 8304 11437 11912 2559 4400 6001 A C
ATOM 58 O PRO A 10 -27.674 27.984 10.509 1.00 82.14 A O
ANISOU 58 O PRO A 10 8036 11650 11524 2323 4167 5812 A O
ATOM 59 CB PRO A 10 -24.819 28.776 11.538 1.00 73.81 A C
ANISOU 59 CB PRO A 10 7726 8992 11328 2186 4444 5370 A C
ATOM 60 CG PRO A 10 -23.674 29.706 11.403 1.00 78.32 A C
ANISOU 60 CG PRO A 10 8495 9017 12247 2323 4717 5419 A C
ATOM 61 CD PRO A 10 -23.830 30.450 10.125 1.00 77.25 A C
ANISOU 61 CD PRO A 10 8178 9165 12009 2678 4918 5895 A C
ATOM 62 N GLU A 11 -27.305 30.060 9.674 1.00 84.59 A N
ANISOU 62 N GLU A 11 8332 11660 12148 3033 4714 6486 A N
ATOM 63 CA GLU A 11 -28.703 30.504 9.555 1.00 88.51 A C
ANISOU 63 CA GLU A 11 8498 12701 12429 3364 4801 6869 A C
ATOM 64 C GLU A 11 -29.360 29.939 8.279 1.00 93.67 A C
ANISOU 64 C GLU A 11 8771 14259 12559 3403 4598 7062 A C
ATOM 65 O GLU A 11 -30.589 29.914 8.183 1.00 95.79 A O
ANISOU 65 O GLU A 11 8706 15155 12534 3547 4549 7256 A O
ATOM 66 CB GLU A 11 -28.784 32.045 9.571 1.00 93.12 A C
ANISOU 66 CB GLU A 11 9121 12957 13304 3894 5261 7332 A C
ATOM 67 CG GLU A 11 -27.910 32.735 8.533 1.00109.60 A C
ANISOU 67 CG GLU A 11 11283 14880 15479 4146 5495 7617 A C
ATOM 68 CD GLU A 11 -27.446 34.142 8.865 1.00142.70 A C
ANISOU 68 CD GLU A 11 15711 18383 20125 4495 5994 7869 A C
ATOM 69 OE1 GLU A 11 -26.272 34.453 8.558 1.00139.14 A O
ANISOU 69 OE1 GLU A 11 15493 17466 19909 4449 6150 7810 A O
ATOM 70 OE2 GLU A 11 -28.251 34.942 9.398 1.00143.87 A O1-
ANISOU 70 OE2 GLU A 11 15812 18457 20395 4811 6252 8122 A O1-
ATOM 71 N LYS A 12 -28.539 29.498 7.306 1.00 88.17 A N
ANISOU 71 N LYS A 12 8108 13659 11735 3272 4487 6997 A N
ATOM 72 CA LYS A 12 -29.019 28.944 6.039 1.00 89.78 A C
ANISOU 72 CA LYS A 12 7962 14714 11435 3276 4298 7138 A C
ATOM 73 C LYS A 12 -29.141 27.427 6.137 1.00 89.41 A C
ANISOU 73 C LYS A 12 7880 14983 11111 2715 3913 6640 A C
ATOM 74 O LYS A 12 -30.143 26.874 5.697 1.00 90.62 A O
ANISOU 74 O LYS A 12 7680 15913 10839 2644 3745 6663 A O
ATOM 75 CB LYS A 12 -28.101 29.347 4.870 1.00 93.14 A C
ANISOU 75 CB LYS A 12 8435 15097 11857 3458 4415 7359 A C
ATOM 76 CG LYS A 12 -28.295 30.789 4.421 1.00114.88 A C
ANISOU 76 CG LYS A 12 11104 17830 14715 4079 4810 7966 A C
ATOM 77 CD LYS A 12 -27.390 31.160 3.250 1.00126.13 A C
ANISOU 77 CD LYS A 12 12574 19236 16112 4252 4937 8193 A C
ATOM 78 CE LYS A 12 -27.684 32.549 2.734 1.00141.43 A C
ANISOU 78 CE LYS A 12 14426 21198 18114 4899 5360 8836 A C
ATOM 79 NZ LYS A 12 -26.881 32.869 1.527 1.00153.15 A N1+
ANISOU 79 NZ LYS A 12 15938 22723 19530 5079 5492 9084 A N1+
ATOM 80 N PHE A 13 -28.125 26.764 6.736 1.00 81.54 A N
ANISOU 80 N PHE A 13 7248 13385 10349 2321 3797 6187 A N
ATOM 81 CA PHE A 13 -28.084 25.310 6.910 1.00 78.96 A C
ANISOU 81 CA PHE A 13 6978 13207 9815 1789 3486 5698 A C
ATOM 82 C PHE A 13 -27.182 24.892 8.080 1.00 74.76 A C
ANISOU 82 C PHE A 13 6879 11882 9644 1495 3446 5275 A C
ATOM 83 O PHE A 13 -26.459 25.719 8.643 1.00 70.85 A O
ANISOU 83 O PHE A 13 6623 10752 9546 1672 3640 5330 A O
ATOM 84 CB PHE A 13 -27.654 24.589 5.614 1.00 82.09 A C
ANISOU 84 CB PHE A 13 7265 14045 9880 1617 3324 5625 A C
ATOM 85 CG PHE A 13 -26.286 24.929 5.073 1.00 83.39 A C
ANISOU 85 CG PHE A 13 7665 13761 10260 1700 3416 5659 A C
ATOM 86 CD1 PHE A 13 -25.208 24.075 5.277 1.00 83.95 A C
ANISOU 86 CD1 PHE A 13 8052 13394 10453 1336 3282 5235 A C
ATOM 87 CD2 PHE A 13 -26.087 26.068 4.299 1.00 88.70 A C
ANISOU 87 CD2 PHE A 13 8233 14483 10988 2151 3652 6124 A C
ATOM 88 CE1 PHE A 13 -23.944 24.377 4.751 1.00 84.13 A C
ANISOU 88 CE1 PHE A 13 8264 13043 10658 1406 3366 5255 A C
ATOM 89 CE2 PHE A 13 -24.820 26.374 3.784 1.00 90.79 A C
ANISOU 89 CE2 PHE A 13 8711 14336 11450 2203 3755 6141 A C
ATOM 90 CZ PHE A 13 -23.760 25.525 4.014 1.00 85.17 A C
ANISOU 90 CZ PHE A 13 8290 13211 10859 1821 3602 5697 A C
ATOM 91 N ASN A 14 -27.261 23.597 8.444 1.00 69.31 A N
ANISOU 91 N ASN A 14 6279 11261 8796 1046 3212 4851 A N
ATOM 92 CA ASN A 14 -26.510 22.969 9.532 1.00 65.46 A C
ANISOU 92 CA ASN A 14 6178 10135 8560 754 3141 4437 A C
ATOM 93 C ASN A 14 -26.095 21.535 9.191 1.00 66.33 A C
ANISOU 93 C ASN A 14 6410 10351 8441 318 2918 4045 A C
ATOM 94 O ASN A 14 -26.875 20.778 8.606 1.00 66.28 A O
ANISOU 94 O ASN A 14 6181 10942 8062 112 2793 3978 A O
ATOM 95 CB ASN A 14 -27.342 22.941 10.836 1.00 68.15 A C
ANISOU 95 CB ASN A 14 6555 10334 9003 701 3159 4338 A C
ATOM 96 CG ASN A 14 -27.518 24.246 11.589 1.00 96.84 A C
ANISOU 96 CG ASN A 14 10199 13633 12962 1071 3401 4608 A C
ATOM 97 ND2 ASN A 14 -28.549 24.301 12.415 1.00 89.85 A N
ANISOU 97 ND2 ASN A 14 9202 12885 12051 1092 3425 4637 A N
ATOM 98 OD1 ASN A 14 -26.705 25.174 11.518 1.00 96.48 A O
ANISOU 98 OD1 ASN A 14 10285 13164 13209 1311 3585 4754 A O
ATOM 99 N ILE A 15 -24.860 21.166 9.580 1.00 60.34 A N
ANISOU 99 N ILE A 15 6006 9017 7905 179 2888 3773 A N
ATOM 100 CA ILE A 15 -24.341 19.796 9.472 1.00 57.28 A C
ANISOU 100 CA ILE A 15 5819 8583 7363 -210 2716 3383 A C
ATOM 101 C ILE A 15 -24.784 19.110 10.756 1.00 60.12 A C
ANISOU 101 C ILE A 15 6358 8720 7763 -439 2666 3107 A C
ATOM 102 O ILE A 15 -24.496 19.603 11.854 1.00 56.86 A O
ANISOU 102 O ILE A 15 6124 7828 7650 -319 2743 3084 A O
ATOM 103 CB ILE A 15 -22.804 19.673 9.207 1.00 56.45 A C
ANISOU 103 CB ILE A 15 5987 8023 7439 -219 2710 3239 A C
ATOM 104 CG1 ILE A 15 -22.389 20.379 7.893 1.00 57.38 A C
ANISOU 104 CG1 ILE A 15 5922 8374 7507 8 2780 3528 A C
ATOM 105 CG2 ILE A 15 -22.380 18.182 9.189 1.00 53.70 A C
ANISOU 105 CG2 ILE A 15 5867 7612 6924 -601 2556 2836 A C
ATOM 106 CD1 ILE A 15 -20.896 20.775 7.819 1.00 57.14 A C
ANISOU 106 CD1 ILE A 15 6123 7823 7766 115 2854 3483 A C
ATOM 107 N LYS A 16 -25.514 17.999 10.609 1.00 58.73 A N
ANISOU 107 N LYS A 16 6126 8912 7278 -775 2557 2896 A N
ATOM 108 CA LYS A 16 -26.074 17.265 11.726 1.00 58.05 A C
ANISOU 108 CA LYS A 16 6197 8675 7185 -1016 2533 2647 A C
ATOM 109 C LYS A 16 -25.284 15.983 12.047 1.00 59.84 A C
ANISOU 109 C LYS A 16 6804 8536 7397 -1329 2465 2258 A C
ATOM 110 O LYS A 16 -25.313 15.504 13.190 1.00 59.45 A O
ANISOU 110 O LYS A 16 7007 8130 7452 -1442 2477 2063 A O
ATOM 111 CB LYS A 16 -27.549 16.944 11.429 1.00 63.71 A C
ANISOU 111 CB LYS A 16 6581 10053 7572 -1183 2507 2678 A C
ATOM 112 CG LYS A 16 -28.453 18.190 11.387 1.00 78.18 A C
ANISOU 112 CG LYS A 16 8052 12229 9424 -830 2592 3073 A C
ATOM 113 CD LYS A 16 -28.781 18.717 12.792 1.00 85.70 A C
ANISOU 113 CD LYS A 16 9122 12786 10654 -688 2683 3111 A C
ATOM 114 CE LYS A 16 -29.129 20.182 12.777 1.00 95.97 A C
ANISOU 114 CE LYS A 16 10192 14159 12113 -234 2825 3529 A C
ATOM 115 NZ LYS A 16 -29.312 20.706 14.153 1.00101.75 A N1+
ANISOU 115 NZ LYS A 16 11065 14461 13132 -108 2929 3535 A N1+
ATOM 116 N HIS A 17 -24.592 15.428 11.053 1.00 53.92 A N
ANISOU 116 N HIS A 17 6100 7878 6509 -1449 2411 2158 A N
ATOM 117 CA HIS A 17 -23.806 14.204 11.205 1.00 51.01 A C
ANISOU 117 CA HIS A 17 6090 7184 6107 -1713 2373 1814 A C
ATOM 118 C HIS A 17 -22.729 14.132 10.140 1.00 56.56 A C
ANISOU 118 C HIS A 17 6835 7865 6791 -1665 2339 1812 A C
ATOM 119 O HIS A 17 -22.921 14.615 9.024 1.00 58.36 A O
ANISOU 119 O HIS A 17 6771 8518 6886 -1569 2328 2016 A O
ATOM 120 CB HIS A 17 -24.706 12.960 11.118 1.00 51.70 A C
ANISOU 120 CB HIS A 17 6183 7577 5885 -2133 2364 1555 A C
ATOM 121 CG HIS A 17 -24.018 11.654 11.410 1.00 53.03 A C
ANISOU 121 CG HIS A 17 6766 7354 6027 -2396 2381 1208 A C
ATOM 122 CD2 HIS A 17 -23.633 10.669 10.568 1.00 54.95 A C
ANISOU 122 CD2 HIS A 17 7125 7680 6075 -2652 2381 991 A C
ATOM 123 ND1 HIS A 17 -23.734 11.258 12.708 1.00 52.24 A N
ANISOU 123 ND1 HIS A 17 7013 6732 6103 -2393 2426 1067 A N
ATOM 124 CE1 HIS A 17 -23.157 10.071 12.613 1.00 50.77 A C
ANISOU 124 CE1 HIS A 17 7150 6310 5828 -2613 2460 797 A C
ATOM 125 NE2 HIS A 17 -23.098 9.661 11.353 1.00 53.11 A N
ANISOU 125 NE2 HIS A 17 7329 6941 5908 -2789 2442 729 A N
ATOM 126 N MET A 18 -21.614 13.487 10.487 1.00 51.62 A N
ANISOU 126 N MET A 18 6568 6767 6277 -1720 2329 1585 A N
ATOM 127 CA MET A 18 -20.497 13.241 9.609 1.00 50.57 A C
ANISOU 127 CA MET A 18 6530 6552 6132 -1701 2301 1528 A C
ATOM 128 C MET A 18 -20.054 11.800 9.689 1.00 51.56 A C
ANISOU 128 C MET A 18 6989 6471 6133 -1984 2297 1184 A C
ATOM 129 O MET A 18 -19.856 11.273 10.779 1.00 48.83 A O
ANISOU 129 O MET A 18 6940 5722 5890 -2018 2325 1019 A O
ATOM 130 CB MET A 18 -19.309 14.148 9.975 1.00 51.64 A C
ANISOU 130 CB MET A 18 6766 6256 6598 -1378 2323 1638 A C
ATOM 131 CG MET A 18 -19.427 15.573 9.499 1.00 56.68 A C
ANISOU 131 CG MET A 18 7107 7066 7362 -1087 2378 1986 A C
ATOM 132 SD MET A 18 -17.816 16.393 9.625 1.00 60.05 A S
ANISOU 132 SD MET A 18 7674 7012 8129 -815 2433 2025 A S
ATOM 133 CE MET A 18 -18.284 18.054 9.276 1.00 57.94 A C
ANISOU 133 CE MET A 18 7093 6901 8019 -498 2570 2441 A C
ATOM 134 N HIS A 19 -19.889 11.166 8.535 1.00 50.37 A N
ANISOU 134 N HIS A 19 6796 6590 5751 -2171 2281 1083 A N
ATOM 135 CA HIS A 19 -19.284 9.844 8.426 1.00 50.21 A C
ANISOU 135 CA HIS A 19 7111 6344 5625 -2408 2313 769 A C
ATOM 136 C HIS A 19 -17.907 10.107 7.791 1.00 51.84 A C
ANISOU 136 C HIS A 19 7387 6371 5938 -2211 2282 805 A C
ATOM 137 O HIS A 19 -17.855 10.638 6.686 1.00 51.85 A O
ANISOU 137 O HIS A 19 7128 6727 5847 -2160 2248 953 A O
ATOM 138 CB HIS A 19 -20.150 8.842 7.637 1.00 53.23 A C
ANISOU 138 CB HIS A 19 7413 7156 5658 -2819 2351 569 A C
ATOM 139 CG HIS A 19 -19.538 7.476 7.577 1.00 56.88 A C
ANISOU 139 CG HIS A 19 8261 7320 6030 -3061 2436 241 A C
ATOM 140 CD2 HIS A 19 -19.741 6.404 8.373 1.00 59.40 A C
ANISOU 140 CD2 HIS A 19 8926 7319 6325 -3277 2553 -6 A C
ATOM 141 ND1 HIS A 19 -18.566 7.159 6.647 1.00 59.00 A N
ANISOU 141 ND1 HIS A 19 8605 7571 6241 -3060 2429 166 A N
ATOM 142 CE1 HIS A 19 -18.223 5.906 6.892 1.00 58.89 A C
ANISOU 142 CE1 HIS A 19 8976 7231 6167 -3269 2546 -125 A C
ATOM 143 NE2 HIS A 19 -18.909 5.407 7.917 1.00 59.68 A N
ANISOU 143 NE2 HIS A 19 9259 7132 6285 -3402 2633 -231 A N
ATOM 144 N LEU A 20 -16.809 9.833 8.523 1.00 46.17 A N
ANISOU 144 N LEU A 20 6995 5135 5414 -2072 2294 693 A N
ATOM 145 CA LEU A 20 -15.455 10.137 8.061 1.00 43.88 A C
ANISOU 145 CA LEU A 20 6764 4660 5250 -1869 2269 716 A C
ATOM 146 C LEU A 20 -14.615 8.910 7.718 1.00 48.20 A C
ANISOU 146 C LEU A 20 7616 5017 5680 -2002 2303 455 A C
ATOM 147 O LEU A 20 -14.276 8.122 8.592 1.00 47.57 A O
ANISOU 147 O LEU A 20 7867 4575 5633 -2017 2352 278 A O
ATOM 148 CB LEU A 20 -14.695 10.968 9.109 1.00 41.57 A C
ANISOU 148 CB LEU A 20 6550 3972 5272 -1560 2258 794 A C
ATOM 149 CG LEU A 20 -15.245 12.342 9.494 1.00 46.54 A C
ANISOU 149 CG LEU A 20 6918 4678 6087 -1367 2261 1053 A C
ATOM 150 CD1 LEU A 20 -14.524 12.879 10.718 1.00 45.74 A C
ANISOU 150 CD1 LEU A 20 6958 4154 6266 -1144 2272 1024 A C
ATOM 151 CD2 LEU A 20 -15.084 13.341 8.385 1.00 48.57 A C
ANISOU 151 CD2 LEU A 20 6881 5202 6372 -1232 2270 1295 A C
ATOM 152 N LYS A 21 -14.226 8.791 6.444 1.00 45.55 A N
ANISOU 152 N LYS A 21 7175 4920 5211 -2064 2291 449 A N
ATOM 153 CA LYS A 21 -13.316 7.760 5.962 1.00 45.16 A C
ANISOU 153 CA LYS A 21 7390 4702 5065 -2152 2335 225 A C
ATOM 154 C LYS A 21 -11.961 8.451 5.749 1.00 47.62 A C
ANISOU 154 C LYS A 21 7686 4836 5572 -1851 2290 318 A C
ATOM 155 O LYS A 21 -11.770 9.122 4.736 1.00 48.20 A O
ANISOU 155 O LYS A 21 7511 5181 5620 -1797 2257 462 A O
ATOM 156 CB LYS A 21 -13.869 7.099 4.688 1.00 50.27 A C
ANISOU 156 CB LYS A 21 7925 5770 5403 -2471 2367 114 A C
ATOM 157 CG LYS A 21 -14.934 6.041 4.976 1.00 68.99 A C
ANISOU 157 CG LYS A 21 10440 8199 7574 -2834 2466 -111 A C
ATOM 158 CD LYS A 21 -15.993 5.887 3.881 1.00 83.40 A C
ANISOU 158 CD LYS A 21 11964 10632 9092 -3157 2469 -154 A C
ATOM 159 CE LYS A 21 -16.976 7.022 3.750 1.00 96.82 A C
ANISOU 159 CE LYS A 21 13226 12797 10765 -3076 2374 121 A C
ATOM 160 NZ LYS A 21 -18.020 6.719 2.741 1.00109.80 A N1+
ANISOU 160 NZ LYS A 21 14568 15090 12059 -3393 2377 47 A N1+
ATOM 161 N LEU A 22 -11.061 8.377 6.753 1.00 41.19 A N
ANISOU 161 N LEU A 22 7106 3595 4948 -1643 2293 249 A N
ATOM 162 CA LEU A 22 -9.768 9.052 6.696 1.00 38.66 A C
ANISOU 162 CA LEU A 22 6753 3115 4820 -1371 2257 302 A C
ATOM 163 C LEU A 22 -8.625 8.096 6.346 1.00 41.74 A C
ANISOU 163 C LEU A 22 7398 3324 5139 -1346 2289 104 A C
ATOM 164 O LEU A 22 -8.429 7.091 7.033 1.00 41.40 A O
ANISOU 164 O LEU A 22 7671 3018 5040 -1360 2343 -69 A O
ATOM 165 CB LEU A 22 -9.429 9.777 8.010 1.00 36.80 A C
ANISOU 165 CB LEU A 22 6540 2603 4839 -1133 2235 351 A C
ATOM 166 CG LEU A 22 -10.504 10.610 8.702 1.00 40.95 A C
ANISOU 166 CG LEU A 22 6889 3206 5464 -1126 2228 515 A C
ATOM 167 CD1 LEU A 22 -10.054 10.988 10.107 1.00 39.44 A C
ANISOU 167 CD1 LEU A 22 6812 2698 5475 -933 2221 470 A C
ATOM 168 CD2 LEU A 22 -10.833 11.864 7.918 1.00 40.94 A C
ANISOU 168 CD2 LEU A 22 6543 3464 5549 -1055 2230 768 A C
ATOM 169 N HIS A 23 -7.865 8.429 5.274 1.00 36.55 A N
ANISOU 169 N HIS A 23 6605 2804 4478 -1291 2273 146 A N
ATOM 170 CA HIS A 23 -6.699 7.675 4.838 1.00 35.95 A C
ANISOU 170 CA HIS A 23 6723 2589 4347 -1235 2302 -19 A C
ATOM 171 C HIS A 23 -5.464 8.460 5.265 1.00 36.36 A C
ANISOU 171 C HIS A 23 6714 2472 4631 -939 2263 18 A C
ATOM 172 O HIS A 23 -5.206 9.542 4.725 1.00 32.93 A O
ANISOU 172 O HIS A 23 6015 2185 4314 -865 2242 173 A O
ATOM 173 CB HIS A 23 -6.742 7.423 3.318 1.00 39.43 A C
ANISOU 173 CB HIS A 23 7051 3339 4591 -1415 2323 -29 A C
ATOM 174 CG HIS A 23 -5.559 6.659 2.799 1.00 44.36 A C
ANISOU 174 CG HIS A 23 7866 3832 5156 -1358 2366 -196 A C
ATOM 175 CD2 HIS A 23 -4.339 7.104 2.415 1.00 45.14 A C
ANISOU 175 CD2 HIS A 23 7888 3901 5360 -1163 2344 -172 A C
ATOM 176 ND1 HIS A 23 -5.582 5.265 2.687 1.00 48.07 A N
ANISOU 176 ND1 HIS A 23 8653 4167 5444 -1512 2467 -422 A N
ATOM 177 CE1 HIS A 23 -4.385 4.922 2.230 1.00 47.10 A C
ANISOU 177 CE1 HIS A 23 8631 3947 5318 -1381 2494 -512 A C
ATOM 178 NE2 HIS A 23 -3.603 5.990 2.054 1.00 45.99 A N
ANISOU 178 NE2 HIS A 23 8250 3881 5343 -1175 2412 -372 A N
ATOM 179 N VAL A 24 -4.742 7.951 6.280 1.00 33.46 A N
ANISOU 179 N VAL A 24 6583 1810 4322 -768 2268 -121 A N
ATOM 180 CA VAL A 24 -3.539 8.602 6.838 1.00 32.46 A C
ANISOU 180 CA VAL A 24 6393 1553 4388 -497 2231 -141 A C
ATOM 181 C VAL A 24 -2.301 8.060 6.132 1.00 37.39 A C
ANISOU 181 C VAL A 24 7102 2162 4943 -405 2250 -264 A C
ATOM 182 O VAL A 24 -2.019 6.870 6.250 1.00 36.58 A O
ANISOU 182 O VAL A 24 7285 1920 4692 -385 2300 -407 A O
ATOM 183 CB VAL A 24 -3.450 8.400 8.386 1.00 35.19 A C
ANISOU 183 CB VAL A 24 6904 1663 4804 -332 2215 -218 A C
ATOM 184 CG1 VAL A 24 -2.158 9.002 8.953 1.00 34.02 A C
ANISOU 184 CG1 VAL A 24 6666 1446 4813 -69 2176 -287 A C
ATOM 185 CG2 VAL A 24 -4.670 8.978 9.093 1.00 33.99 A C
ANISOU 185 CG2 VAL A 24 6658 1527 4729 -421 2202 -98 A C
ATOM 186 N ASP A 25 -1.562 8.924 5.400 1.00 34.98 A N
ANISOU 186 N ASP A 25 6561 1985 4747 -343 2236 -203 A N
ATOM 187 CA ASP A 25 -0.357 8.518 4.661 1.00 34.62 A C
ANISOU 187 CA ASP A 25 6553 1955 4644 -254 2256 -313 A C
ATOM 188 C ASP A 25 0.878 9.297 5.138 1.00 35.45 A C
ANISOU 188 C ASP A 25 6512 2014 4942 -27 2231 -363 A C
ATOM 189 O ASP A 25 1.027 10.469 4.808 1.00 32.66 A O
ANISOU 189 O ASP A 25 5899 1757 4755 -37 2243 -256 A O
ATOM 190 CB ASP A 25 -0.573 8.702 3.148 1.00 37.90 A C
ANISOU 190 CB ASP A 25 6821 2614 4965 -427 2284 -221 A C
ATOM 191 CG ASP A 25 0.427 7.951 2.290 1.00 56.69 A C
ANISOU 191 CG ASP A 25 9304 5009 7226 -386 2320 -357 A C
ATOM 192 OD1 ASP A 25 1.590 8.419 2.181 1.00 56.07 A O
ANISOU 192 OD1 ASP A 25 9111 4927 7265 -220 2315 -388 A O
ATOM 193 OD2 ASP A 25 0.047 6.890 1.720 1.00 68.27 A O1-
ANISOU 193 OD2 ASP A 25 10965 6493 8481 -533 2370 -449 A O1-
ATOM 194 N PHE A 26 1.772 8.635 5.899 1.00 33.74 A N
ANISOU 194 N PHE A 26 6461 1667 4690 181 2218 -530 A N
ATOM 195 CA PHE A 26 2.976 9.275 6.446 1.00 33.28 A C
ANISOU 195 CA PHE A 26 6249 1621 4775 393 2190 -627 A C
ATOM 196 C PHE A 26 4.018 9.613 5.386 1.00 37.40 A C
ANISOU 196 C PHE A 26 6606 2277 5326 410 2219 -662 A C
ATOM 197 O PHE A 26 4.752 10.576 5.583 1.00 39.66 A O
ANISOU 197 O PHE A 26 6665 2621 5784 480 2223 -705 A O
ATOM 198 CB PHE A 26 3.617 8.412 7.540 1.00 35.25 A C
ANISOU 198 CB PHE A 26 6704 1762 4927 644 2164 -781 A C
ATOM 199 CG PHE A 26 2.882 8.494 8.857 1.00 35.05 A C
ANISOU 199 CG PHE A 26 6752 1627 4937 682 2131 -761 A C
ATOM 200 CD1 PHE A 26 3.242 9.435 9.816 1.00 35.38 A C
ANISOU 200 CD1 PHE A 26 6594 1710 5139 787 2086 -812 A C
ATOM 201 CD2 PHE A 26 1.841 7.619 9.145 1.00 36.37 A C
ANISOU 201 CD2 PHE A 26 7188 1656 4973 595 2163 -709 A C
ATOM 202 CE1 PHE A 26 2.561 9.510 11.035 1.00 35.28 A C
ANISOU 202 CE1 PHE A 26 6648 1609 5148 823 2059 -799 A C
ATOM 203 CE2 PHE A 26 1.157 7.705 10.357 1.00 37.44 A C
ANISOU 203 CE2 PHE A 26 7391 1695 5139 629 2142 -685 A C
ATOM 204 CZ PHE A 26 1.516 8.657 11.289 1.00 34.17 A C
ANISOU 204 CZ PHE A 26 6762 1353 4869 742 2080 -711 A C
ATOM 205 N THR A 27 4.082 8.851 4.270 1.00 31.79 A N
ANISOU 205 N THR A 27 6005 1620 4453 327 2256 -659 A N
ATOM 206 CA THR A 27 5.015 9.113 3.183 1.00 31.35 A C
ANISOU 206 CA THR A 27 5804 1701 4408 332 2291 -683 A C
ATOM 207 C THR A 27 4.616 10.425 2.474 1.00 34.02 A C
ANISOU 207 C THR A 27 5861 2162 4903 177 2328 -502 A C
ATOM 208 O THR A 27 5.466 11.275 2.218 1.00 32.74 A O
ANISOU 208 O THR A 27 5491 2062 4887 224 2369 -517 A O
ATOM 209 CB THR A 27 5.093 7.905 2.232 1.00 42.72 A C
ANISOU 209 CB THR A 27 7457 3158 5618 279 2334 -739 A C
ATOM 210 CG2 THR A 27 6.072 8.119 1.084 1.00 40.90 A C
ANISOU 210 CG2 THR A 27 7085 3076 5381 293 2373 -771 A C
ATOM 211 OG1 THR A 27 5.508 6.761 2.980 1.00 44.60 A O
ANISOU 211 OG1 THR A 27 7977 3237 5731 464 2343 -883 A O
ATOM 212 N SER A 28 3.320 10.607 2.223 1.00 31.51 A N
ANISOU 212 N SER A 28 5537 1883 4552 5 2331 -329 A N
ATOM 213 CA SER A 28 2.779 11.800 1.585 1.00 31.24 A C
ANISOU 213 CA SER A 28 5261 1972 4636 -100 2385 -109 A C
ATOM 214 C SER A 28 2.510 12.952 2.568 1.00 31.91 A C
ANISOU 214 C SER A 28 5205 1951 4969 -52 2410 -36 A C
ATOM 215 O SER A 28 2.356 14.098 2.118 1.00 27.66 A O
ANISOU 215 O SER A 28 4465 1465 4581 -84 2503 139 A O
ATOM 216 CB SER A 28 1.474 11.448 0.891 1.00 35.92 A C
ANISOU 216 CB SER A 28 5885 2718 5047 -284 2378 43 A C
ATOM 217 OG SER A 28 1.713 10.718 -0.301 1.00 48.84 A O
ANISOU 217 OG SER A 28 7579 4506 6473 -370 2392 -3 A O
ATOM 218 N ARG A 29 2.445 12.648 3.910 1.00 29.56 A N
ANISOU 218 N ARG A 29 5026 1498 4708 33 2348 -163 A N
ATOM 219 CA ARG A 29 2.064 13.619 4.954 1.00 28.41 A C
ANISOU 219 CA ARG A 29 4776 1247 4772 62 2370 -124 A C
ATOM 220 C ARG A 29 0.689 14.138 4.551 1.00 34.62 A C
ANISOU 220 C ARG A 29 5489 2099 5567 -67 2409 136 A C
ATOM 221 O ARG A 29 0.494 15.342 4.331 1.00 34.32 A O
ANISOU 221 O ARG A 29 5261 2066 5712 -77 2514 296 A O
ATOM 222 CB ARG A 29 3.090 14.765 5.130 1.00 27.70 A C
ANISOU 222 CB ARG A 29 4475 1127 4924 127 2460 -199 A C
ATOM 223 CG ARG A 29 4.360 14.313 5.820 1.00 34.34 A C
ANISOU 223 CG ARG A 29 5346 1955 5748 274 2404 -479 A C
ATOM 224 CD ARG A 29 5.350 15.444 6.098 1.00 29.23 A C
ANISOU 224 CD ARG A 29 4464 1311 5331 292 2504 -605 A C
ATOM 225 NE ARG A 29 6.484 14.887 6.845 1.00 36.01 A N
ANISOU 225 NE ARG A 29 5329 2234 6118 451 2425 -885 A N
ATOM 226 CZ ARG A 29 7.276 15.556 7.675 1.00 45.74 A C
ANISOU 226 CZ ARG A 29 6387 3502 7490 492 2460 -1093 A C
ATOM 227 NH1 ARG A 29 7.096 16.854 7.874 1.00 35.24 A N1+
ANISOU 227 NH1 ARG A 29 4884 2095 6412 364 2601 -1070 A N1+
ATOM 228 NH2 ARG A 29 8.262 14.933 8.304 1.00 36.37 A N
ANISOU 228 NH2 ARG A 29 5193 2445 6180 666 2370 -1333 A N
ATOM 229 N ALA A 30 -0.246 13.199 4.346 1.00 30.48 A N
ANISOU 229 N ALA A 30 5112 1643 4827 -168 2346 178 A N
ATOM 230 CA ALA A 30 -1.562 13.588 3.883 1.00 30.31 A C
ANISOU 230 CA ALA A 30 4991 1767 4758 -289 2370 414 A C
ATOM 231 C ALA A 30 -2.675 12.868 4.579 1.00 34.59 A C
ANISOU 231 C ALA A 30 5683 2286 5174 -376 2306 396 A C
ATOM 232 O ALA A 30 -2.509 11.732 5.042 1.00 34.65 A O
ANISOU 232 O ALA A 30 5926 2189 5052 -385 2256 211 A O
ATOM 233 CB ALA A 30 -1.668 13.317 2.389 1.00 32.01 A C
ANISOU 233 CB ALA A 30 5142 2232 4787 -390 2388 514 A C
ATOM 234 N ILE A 31 -3.836 13.519 4.624 1.00 29.57 A N
ANISOU 234 N ILE A 31 4914 1751 4569 -434 2330 599 A N
ATOM 235 CA ILE A 31 -5.034 12.850 5.089 1.00 28.68 A C
ANISOU 235 CA ILE A 31 4906 1681 4312 -558 2283 598 A C
ATOM 236 C ILE A 31 -6.056 13.021 3.987 1.00 34.83 A C
ANISOU 236 C ILE A 31 5508 2801 4926 -693 2299 801 A C
ATOM 237 O ILE A 31 -6.529 14.134 3.737 1.00 35.40 A O
ANISOU 237 O ILE A 31 5355 2994 5101 -628 2356 1044 A O
ATOM 238 CB ILE A 31 -5.580 13.245 6.481 1.00 30.90 A C
ANISOU 238 CB ILE A 31 5214 1782 4745 -497 2278 604 A C
ATOM 239 CG1 ILE A 31 -4.481 13.155 7.572 1.00 30.65 A C
ANISOU 239 CG1 ILE A 31 5314 1478 4853 -340 2258 397 A C
ATOM 240 CG2 ILE A 31 -6.805 12.341 6.831 1.00 30.78 A C
ANISOU 240 CG2 ILE A 31 5329 1829 4539 -660 2239 579 A C
ATOM 241 CD1 ILE A 31 -4.960 13.549 9.034 1.00 34.27 A C
ANISOU 241 CD1 ILE A 31 5797 1769 5455 -273 2254 378 A C
ATOM 242 N ALA A 32 -6.338 11.925 3.281 1.00 32.55 A N
ANISOU 242 N ALA A 32 5316 2683 4369 -871 2268 699 A N
ATOM 243 CA ALA A 32 -7.318 11.911 2.209 1.00 34.26 A C
ANISOU 243 CA ALA A 32 5352 3303 4363 -1028 2270 841 A C
ATOM 244 C ALA A 32 -8.629 11.527 2.840 1.00 39.13 A C
ANISOU 244 C ALA A 32 5992 3999 4876 -1175 2246 833 A C
ATOM 245 O ALA A 32 -8.744 10.452 3.438 1.00 40.43 A O
ANISOU 245 O ALA A 32 6409 3999 4955 -1301 2236 611 A O
ATOM 246 CB ALA A 32 -6.899 10.944 1.108 1.00 36.20 A C
ANISOU 246 CB ALA A 32 5676 3710 4367 -1176 2266 691 A C
ATOM 247 N ALA A 33 -9.582 12.458 2.839 1.00 35.78 A N
ANISOU 247 N ALA A 33 5322 3788 4485 -1130 2258 1081 A N
ATOM 248 CA ALA A 33 -10.858 12.227 3.517 1.00 35.55 A C
ANISOU 248 CA ALA A 33 5279 3851 4376 -1253 2240 1087 A C
ATOM 249 C ALA A 33 -12.028 12.155 2.569 1.00 45.64 A C
ANISOU 249 C ALA A 33 6310 5659 5370 -1420 2228 1205 A C
ATOM 250 O ALA A 33 -12.179 12.988 1.670 1.00 45.99 A O
ANISOU 250 O ALA A 33 6085 6019 5370 -1310 2248 1454 A O
ATOM 251 CB ALA A 33 -11.114 13.308 4.552 1.00 34.06 A C
ANISOU 251 CB ALA A 33 5015 3470 4457 -1057 2269 1253 A C
ATOM 252 N SER A 34 -12.871 11.143 2.807 1.00 45.76 A N
ANISOU 252 N SER A 34 6418 5787 5181 -1686 2211 1019 A N
ATOM 253 CA SER A 34 -14.128 10.902 2.125 1.00 48.57 A C
ANISOU 253 CA SER A 34 6539 6681 5235 -1905 2198 1055 A C
ATOM 254 C SER A 34 -15.195 11.213 3.155 1.00 50.59 A C
ANISOU 254 C SER A 34 6733 6933 5555 -1905 2198 1131 A C
ATOM 255 O SER A 34 -15.513 10.357 3.983 1.00 51.43 A O
ANISOU 255 O SER A 34 7066 6835 5639 -2091 2215 907 A O
ATOM 256 CB SER A 34 -14.189 9.462 1.617 1.00 56.02 A C
ANISOU 256 CB SER A 34 7653 7728 5902 -2255 2216 726 A C
ATOM 257 OG SER A 34 -15.249 9.276 0.693 1.00 72.67 A O
ANISOU 257 OG SER A 34 9481 10450 7681 -2490 2203 731 A O
ATOM 258 N THR A 35 -15.646 12.481 3.205 1.00 45.32 A N
ANISOU 258 N THR A 35 5796 6421 5004 -1663 2205 1457 A N
ATOM 259 CA THR A 35 -16.611 12.922 4.211 1.00 45.17 A C
ANISOU 259 CA THR A 35 5704 6381 5078 -1613 2216 1561 A C
ATOM 260 C THR A 35 -18.053 12.901 3.673 1.00 53.33 A C
ANISOU 260 C THR A 35 6415 8042 5808 -1764 2197 1657 A C
ATOM 261 O THR A 35 -18.323 13.445 2.605 1.00 54.81 A O
ANISOU 261 O THR A 35 6297 8702 5828 -1675 2192 1876 A O
ATOM 262 CB THR A 35 -16.247 14.312 4.744 1.00 51.33 A C
ANISOU 262 CB THR A 35 6406 6913 6185 -1255 2272 1840 A C
ATOM 263 CG2 THR A 35 -14.793 14.442 5.086 1.00 42.98 A C
ANISOU 263 CG2 THR A 35 5590 5344 5396 -1114 2293 1741 A C
ATOM 264 OG1 THR A 35 -16.575 15.272 3.759 1.00 61.95 A O
ANISOU 264 OG1 THR A 35 7427 8661 7450 -1080 2310 2164 A O
ATOM 265 N SER A 36 -18.968 12.256 4.420 1.00 50.88 A N
ANISOU 265 N SER A 36 6164 7755 5411 -1988 2195 1491 A N
ATOM 266 CA SER A 36 -20.400 12.158 4.107 1.00 52.88 A C
ANISOU 266 CA SER A 36 6108 8607 5376 -2166 2181 1530 A C
ATOM 267 C SER A 36 -21.138 13.047 5.093 1.00 56.39 A C
ANISOU 267 C SER A 36 6438 8986 6001 -1957 2205 1751 A C
ATOM 268 O SER A 36 -21.237 12.697 6.276 1.00 53.88 A O
ANISOU 268 O SER A 36 6358 8280 5834 -2030 2227 1600 A O
ATOM 269 CB SER A 36 -20.875 10.708 4.179 1.00 56.66 A C
ANISOU 269 CB SER A 36 6751 9160 5617 -2621 2196 1139 A C
ATOM 270 OG SER A 36 -19.972 9.834 3.518 1.00 69.14 A O
ANISOU 270 OG SER A 36 8536 10633 7100 -2791 2207 905 A O
ATOM 271 N LEU A 37 -21.568 14.249 4.635 1.00 55.30 A N
ANISOU 271 N LEU A 37 5958 9185 5866 -1658 2221 2128 A N
ATOM 272 CA LEU A 37 -22.219 15.236 5.511 1.00 56.21 A C
ANISOU 272 CA LEU A 37 5956 9228 6175 -1403 2275 2380 A C
ATOM 273 C LEU A 37 -23.765 15.295 5.387 1.00 64.81 A C
ANISOU 273 C LEU A 37 6682 10958 6985 -1480 2261 2485 A C
ATOM 274 O LEU A 37 -24.298 15.615 4.319 1.00 67.61 A O
ANISOU 274 O LEU A 37 6679 11947 7061 -1419 2243 2675 A O
ATOM 275 CB LEU A 37 -21.668 16.659 5.285 1.00 55.98 A C
ANISOU 275 CB LEU A 37 5824 9058 6389 -967 2362 2757 A C
ATOM 276 CG LEU A 37 -20.226 16.855 4.840 1.00 59.91 A C
ANISOU 276 CG LEU A 37 6516 9177 7068 -856 2387 2738 A C
ATOM 277 CD1 LEU A 37 -20.005 18.283 4.443 1.00 60.91 A C
ANISOU 277 CD1 LEU A 37 6468 9318 7358 -463 2514 3139 A C
ATOM 278 CD2 LEU A 37 -19.233 16.463 5.925 1.00 60.39 A C
ANISOU 278 CD2 LEU A 37 6969 8547 7428 -906 2387 2475 A C
ATOM 279 N THR A 38 -24.469 15.071 6.509 1.00 61.43 A N
ANISOU 279 N THR A 38 6328 10383 6631 -1581 2276 2382 A N
ATOM 280 CA THR A 38 -25.931 15.172 6.575 1.00 63.78 A C
ANISOU 280 CA THR A 38 6287 11250 6698 -1644 2273 2471 A C
ATOM 281 C THR A 38 -26.243 16.653 6.760 1.00 68.88 A C
ANISOU 281 C THR A 38 6713 11932 7527 -1175 2353 2912 A C
ATOM 282 O THR A 38 -25.947 17.229 7.812 1.00 65.91 A O
ANISOU 282 O THR A 38 6535 11014 7492 -990 2423 2973 A O
ATOM 283 CB THR A 38 -26.493 14.266 7.673 1.00 72.84 A C
ANISOU 283 CB THR A 38 7633 12199 7843 -1975 2277 2152 A C
ATOM 284 CG2 THR A 38 -28.033 14.327 7.772 1.00 72.83 A C
ANISOU 284 CG2 THR A 38 7263 12825 7585 -2086 2277 2203 A C
ATOM 285 OG1 THR A 38 -26.056 12.929 7.416 1.00 75.76 A O
ANISOU 285 OG1 THR A 38 8267 12438 8080 -2369 2255 1765 A O
ATOM 286 N VAL A 39 -26.778 17.279 5.711 1.00 69.61 A N
ANISOU 286 N VAL A 39 6407 12653 7388 -966 2361 3224 A N
ATOM 287 CA VAL A 39 -27.054 18.716 5.694 1.00 70.31 A C
ANISOU 287 CA VAL A 39 6285 12805 7624 -474 2481 3692 A C
ATOM 288 C VAL A 39 -28.558 18.988 5.886 1.00 77.54 A C
ANISOU 288 C VAL A 39 6823 14320 8318 -408 2490 3858 A C
ATOM 289 O VAL A 39 -29.380 18.451 5.145 1.00 79.83 A O
ANISOU 289 O VAL A 39 6788 15353 8191 -599 2403 3798 A O
ATOM 290 CB VAL A 39 -26.507 19.360 4.388 1.00 74.22 A C
ANISOU 290 CB VAL A 39 6619 13546 8035 -191 2524 3997 A C
ATOM 291 CG1 VAL A 39 -26.807 20.854 4.334 1.00 75.29 A C
ANISOU 291 CG1 VAL A 39 6561 13728 8319 342 2701 4510 A C
ATOM 292 CG2 VAL A 39 -25.006 19.124 4.247 1.00 71.05 A C
ANISOU 292 CG2 VAL A 39 6583 12545 7869 -252 2524 3827 A C
ATOM 293 N ARG A 40 -28.897 19.843 6.865 1.00 73.96 A N
ANISOU 293 N ARG A 40 6400 13563 8138 -137 2606 4055 A N
ATOM 294 CA ARG A 40 -30.276 20.241 7.132 1.00 77.28 A C
ANISOU 294 CA ARG A 40 6472 14493 8396 -5 2641 4251 A C
ATOM 295 C ARG A 40 -30.477 21.696 6.710 1.00 84.72 A C
ANISOU 295 C ARG A 40 7181 15592 9418 574 2810 4798 A C
ATOM 296 O ARG A 40 -29.835 22.592 7.264 1.00 82.60 A O
ANISOU 296 O ARG A 40 7147 14685 9551 862 2971 4966 A O
ATOM 297 CB ARG A 40 -30.653 20.034 8.616 1.00 74.93 A C
ANISOU 297 CB ARG A 40 6386 13761 8324 -151 2663 4047 A C
ATOM 298 CG ARG A 40 -32.119 20.368 8.921 1.00 84.21 A C
ANISOU 298 CG ARG A 40 7194 15479 9323 -39 2698 4222 A C
ATOM 299 CD ARG A 40 -32.724 19.419 9.918 1.00 88.71 A C
ANISOU 299 CD ARG A 40 7870 15988 9847 -455 2633 3846 A C
ATOM 300 NE ARG A 40 -32.753 19.969 11.273 1.00 92.35 A N
ANISOU 300 NE ARG A 40 8549 15870 10668 -301 2740 3883 A N
ATOM 301 CZ ARG A 40 -32.554 19.256 12.378 1.00 98.21 A C
ANISOU 301 CZ ARG A 40 9632 16110 11572 -598 2717 3541 A C
ATOM 302 NH1 ARG A 40 -32.270 17.960 12.300 1.00 80.29 A N1+
ANISOU 302 NH1 ARG A 40 7561 13786 9159 -1054 2613 3148 A N1+
ATOM 303 NH2 ARG A 40 -32.613 19.839 13.570 1.00 78.75 A N
ANISOU 303 NH2 ARG A 40 7329 13182 9412 -429 2818 3596 A N
ATOM 304 N SER A 41 -31.377 21.922 5.738 1.00 86.35 A N
ANISOU 304 N SER A 41 6922 16658 9228 744 2792 5067 A N
ATOM 305 CA SER A 41 -31.720 23.254 5.229 1.00 89.46 A C
ANISOU 305 CA SER A 41 7054 17314 9621 1335 2974 5633 A C
ATOM 306 C SER A 41 -32.576 24.023 6.250 1.00 95.07 A C
ANISOU 306 C SER A 41 7690 17923 10508 1607 3118 5842 A C
ATOM 307 O SER A 41 -33.549 23.483 6.766 1.00 95.44 A O
ANISOU 307 O SER A 41 7562 18332 10371 1385 3022 5665 A O
ATOM 308 CB SER A 41 -32.456 23.140 3.896 1.00 97.60 A C
ANISOU 308 CB SER A 41 7586 19385 10113 1426 2891 5834 A C
ATOM 309 OG SER A 41 -32.966 24.386 3.447 1.00113.58 A O
ANISOU 309 OG SER A 41 9315 21765 12077 2035 3076 6414 A O
ATOM 310 N LEU A 42 -32.191 25.272 6.546 1.00 92.21 A N
ANISOU 310 N LEU A 42 7477 17046 10513 2069 3369 6198 A N
ATOM 311 CA LEU A 42 -32.879 26.162 7.484 1.00 93.37 A C
ANISOU 311 CA LEU A 42 7593 17005 10878 2388 3562 6434 A C
ATOM 312 C LEU A 42 -33.631 27.277 6.729 1.00104.90 A C
ANISOU 312 C LEU A 42 8674 19024 12159 2993 3760 7038 A C
ATOM 313 O LEU A 42 -34.494 27.940 7.308 1.00106.86 A O
ANISOU 313 O LEU A 42 8781 19358 12465 3291 3910 7279 A O
ATOM 314 CB LEU A 42 -31.866 26.768 8.476 1.00 89.87 A C
ANISOU 314 CB LEU A 42 7626 15518 11005 2454 3747 6360 A C
ATOM 315 CG LEU A 42 -31.688 26.070 9.837 1.00 90.93 A C
ANISOU 315 CG LEU A 42 8068 15116 11365 2047 3643 5891 A C
ATOM 316 CD1 LEU A 42 -31.071 24.690 9.695 1.00 88.55 A C
ANISOU 316 CD1 LEU A 42 7951 14752 10941 1515 3383 5412 A C
ATOM 317 CD2 LEU A 42 -30.813 26.898 10.752 1.00 90.54 A C
ANISOU 317 CD2 LEU A 42 8393 14170 11839 2209 3866 5895 A C
ATOM 318 N GLN A 43 -33.280 27.490 5.447 1.00105.53 A N
ANISOU 318 N GLN A 43 8603 19470 12023 3196 3778 7294 A N
ATOM 319 CA GLN A 43 -33.867 28.487 4.547 1.00110.53 A C
ANISOU 319 CA GLN A 43 8885 20675 12435 3802 3971 7900 A C
ATOM 320 C GLN A 43 -34.612 27.779 3.414 1.00118.50 A C
ANISOU 320 C GLN A 43 9394 22821 12809 3706 3735 7914 A C
ATOM 321 O GLN A 43 -34.133 26.766 2.898 1.00116.62 A O
ANISOU 321 O GLN A 43 9186 22746 12379 3249 3498 7541 A O
ATOM 322 CB GLN A 43 -32.764 29.407 3.980 1.00111.89 A C
ANISOU 322 CB GLN A 43 9313 20312 12888 4152 4230 8213 A C
ATOM 323 CG GLN A 43 -33.277 30.726 3.395 1.00134.94 A C
ANISOU 323 CG GLN A 43 12018 23493 15760 4886 4567 8904 A C
ATOM 324 CD GLN A 43 -32.304 31.380 2.436 1.00154.68 A C
ANISOU 324 CD GLN A 43 14657 25765 18347 5185 4776 9220 A C
ATOM 325 NE2 GLN A 43 -32.795 31.761 1.265 1.00152.20 A N
ANISOU 325 NE2 GLN A 43 13969 26241 17618 5611 4835 9689 A N
ATOM 326 OE1 GLN A 43 -31.125 31.595 2.743 1.00145.76 A O
ANISOU 326 OE1 GLN A 43 13958 23775 17648 5060 4906 9064 A O
ATOM 327 N ASP A 44 -35.771 28.317 3.021 1.00120.81 A N
ANISOU 327 N ASP A 44 9221 23915 12767 4143 3812 8340 A N
ATOM 328 CA ASP A 44 -36.585 27.747 1.949 1.00125.30 A C
ANISOU 328 CA ASP A 44 9240 25681 12686 4097 3603 8378 A C
ATOM 329 C ASP A 44 -35.927 27.960 0.576 1.00132.53 A C
ANISOU 329 C ASP A 44 10073 26898 13385 4327 3631 8647 A C
ATOM 330 O ASP A 44 -35.344 29.020 0.327 1.00133.13 A O
ANISOU 330 O ASP A 44 10319 26558 13706 4842 3917 9105 A O
ATOM 331 CB ASP A 44 -37.994 28.349 1.967 1.00132.17 A C
ANISOU 331 CB ASP A 44 9618 27341 13261 4550 3691 8777 A C
ATOM 332 CG ASP A 44 -38.722 28.185 3.289 1.00140.44 A C
ANISOU 332 CG ASP A 44 10710 28157 14493 4347 3675 8536 A C
ATOM 333 OD1 ASP A 44 -38.990 29.211 3.948 1.00141.37 A O
ANISOU 333 OD1 ASP A 44 10933 27860 14922 4799 3943 8877 A O
ATOM 334 OD2 ASP A 44 -39.024 27.029 3.663 1.00144.77 A O1-
ANISOU 334 OD2 ASP A 44 11202 28925 14878 3731 3415 8002 A O1-
ATOM 335 N SER A 45 -36.020 26.931 -0.300 1.00130.38 A N
ANISOU 335 N SER A 45 9549 27340 12651 3919 3351 8339 A N
ATOM 336 CA SER A 45 -35.503 26.857 -1.679 1.00132.10 A C
ANISOU 336 CA SER A 45 9623 28019 12551 4011 3304 8484 A C
ATOM 337 C SER A 45 -34.005 27.261 -1.795 1.00132.26 A C
ANISOU 337 C SER A 45 10167 27053 13032 4085 3467 8543 A C
ATOM 338 O SER A 45 -33.629 28.048 -2.670 1.00134.05 A O
ANISOU 338 O SER A 45 10351 27366 13214 4573 3657 9019 A O
ATOM 339 CB SER A 45 -36.372 27.673 -2.639 1.00141.89 A C
ANISOU 339 CB SER A 45 10320 30268 13323 4660 3413 9102 A C
ATOM 340 OG SER A 45 -36.365 29.060 -2.345 1.00149.38 A O
ANISOU 340 OG SER A 45 11699 30298 14762 5133 3664 9312 A O
ATOM 341 N LEU A 46 -33.155 26.678 -0.924 1.00123.50 A N
ANISOU 341 N LEU A 46 9538 25044 12342 3592 3394 8048 A N
ATOM 342 CA LEU A 46 -31.709 26.917 -0.916 1.00119.54 A C
ANISOU 342 CA LEU A 46 9527 23615 12278 3568 3516 7998 A C
ATOM 343 C LEU A 46 -31.058 26.233 -2.122 1.00122.85 A C
ANISOU 343 C LEU A 46 9883 24402 12391 3351 3360 7859 A C
ATOM 344 O LEU A 46 -31.238 25.031 -2.315 1.00121.87 A O
ANISOU 344 O LEU A 46 9648 24689 11968 2828 3086 7400 A O
ATOM 345 CB LEU A 46 -31.077 26.405 0.395 1.00114.26 A C
ANISOU 345 CB LEU A 46 9336 21997 12082 3107 3456 7491 A C
ATOM 346 CG LEU A 46 -30.262 27.400 1.239 1.00116.64 A C
ANISOU 346 CG LEU A 46 10077 21240 13001 3355 3742 7632 A C
ATOM 347 CD1 LEU A 46 -29.578 26.688 2.383 1.00111.83 A C
ANISOU 347 CD1 LEU A 46 9881 19859 12749 2856 3624 7080 A C
ATOM 348 CD2 LEU A 46 -29.188 28.109 0.418 1.00120.04 A C
ANISOU 348 CD2 LEU A 46 10691 21316 13603 3637 3946 7908 A C
ATOM 349 N ALA A 47 -30.299 26.994 -2.926 1.00119.57 A N
ANISOU 349 N ALA A 47 9552 23825 12054 3740 3557 8243 A N
ATOM 350 CA ALA A 47 -29.663 26.477 -4.135 1.00119.72 A C
ANISOU 350 CA ALA A 47 9510 24194 11785 3590 3438 8160 A C
ATOM 351 C ALA A 47 -28.179 26.138 -3.946 1.00117.24 A C
ANISOU 351 C ALA A 47 9705 22960 11881 3252 3432 7803 A C
ATOM 352 O ALA A 47 -27.688 25.210 -4.597 1.00115.16 A O
ANISOU 352 O ALA A 47 9447 22910 11399 2859 3228 7457 A O
ATOM 353 CB ALA A 47 -29.816 27.481 -5.265 1.00125.29 A C
ANISOU 353 CB ALA A 47 9962 25385 12259 4230 3655 8812 A C
ATOM 354 N SER A 48 -27.473 26.883 -3.070 1.00110.63 A N
ANISOU 354 N SER A 48 9276 21139 11619 3403 3664 7875 A N
ATOM 355 CA SER A 48 -26.039 26.710 -2.843 1.00106.30 A C
ANISOU 355 CA SER A 48 9188 19724 11478 3156 3696 7585 A C
ATOM 356 C SER A 48 -25.695 26.196 -1.434 1.00104.48 A C
ANISOU 356 C SER A 48 9307 18759 11631 2743 3601 7090 A C
ATOM 357 O SER A 48 -26.499 26.308 -0.513 1.00103.84 A O
ANISOU 357 O SER A 48 9167 18684 11603 2734 3587 7053 A O
ATOM 358 CB SER A 48 -25.309 28.027 -3.101 1.00111.04 A C
ANISOU 358 CB SER A 48 9980 19784 12425 3641 4071 8039 A C
ATOM 359 OG SER A 48 -25.832 29.071 -2.300 1.00121.95 A O
ANISOU 359 OG SER A 48 11415 20817 14104 3996 4334 8331 A O
ATOM 360 N LEU A 49 -24.471 25.650 -1.283 1.00 96.60 A N
ANISOU 360 N LEU A 49 8668 17150 10887 2425 3542 6723 A N
ATOM 361 CA LEU A 49 -23.929 25.116 -0.034 1.00 91.14 A C
ANISOU 361 CA LEU A 49 8336 15746 10549 2059 3458 6256 A C
ATOM 362 C LEU A 49 -22.485 25.618 0.166 1.00 89.89 A C
ANISOU 362 C LEU A 49 8556 14759 10840 2096 3626 6196 A C
ATOM 363 O LEU A 49 -21.582 25.187 -0.553 1.00 87.99 A O
ANISOU 363 O LEU A 49 8411 14482 10542 1940 3556 6047 A O
ATOM 364 CB LEU A 49 -23.982 23.579 -0.078 1.00 89.71 A C
ANISOU 364 CB LEU A 49 8154 15844 10086 1517 3139 5745 A C
ATOM 365 CG LEU A 49 -24.511 22.871 1.155 1.00 91.98 A C
ANISOU 365 CG LEU A 49 8570 15905 10472 1196 3014 5377 A C
ATOM 366 CD1 LEU A 49 -26.025 23.014 1.272 1.00 95.60 A C
ANISOU 366 CD1 LEU A 49 8670 16985 10667 1303 2993 5558 A C
ATOM 367 CD2 LEU A 49 -24.161 21.408 1.112 1.00 91.28 A C
ANISOU 367 CD2 LEU A 49 8631 15828 10225 669 2782 4855 A C
ATOM 368 N ILE A 50 -22.279 26.540 1.133 1.00 84.12 A N
ANISOU 368 N ILE A 50 8025 13389 10546 2295 3861 6301 A N
ATOM 369 CA ILE A 50 -20.978 27.151 1.448 1.00 81.35 A C
ANISOU 369 CA ILE A 50 8006 12256 10646 2335 4067 6238 A C
ATOM 370 C ILE A 50 -20.311 26.490 2.674 1.00 78.29 A C
ANISOU 370 C ILE A 50 7932 11276 10540 1958 3930 5716 A C
ATOM 371 O ILE A 50 -20.847 26.539 3.783 1.00 77.15 A O
ANISOU 371 O ILE A 50 7841 10930 10542 1921 3931 5614 A O
ATOM 372 CB ILE A 50 -21.072 28.692 1.635 1.00 87.36 A C
ANISOU 372 CB ILE A 50 8796 12678 11718 2801 4477 6686 A C
ATOM 373 CG1 ILE A 50 -22.349 29.111 2.445 1.00 90.36 A C
ANISOU 373 CG1 ILE A 50 9035 13198 12102 2990 4544 6866 A C
ATOM 374 CG2 ILE A 50 -21.001 29.390 0.288 1.00 91.37 A C
ANISOU 374 CG2 ILE A 50 9143 13515 12058 3169 4680 7163 A C
ATOM 375 CD1 ILE A 50 -22.440 30.572 2.909 1.00102.94 A C
ANISOU 375 CD1 ILE A 50 10729 14313 14070 3399 4972 7220 A C
ATOM 376 N LEU A 51 -19.124 25.895 2.465 1.00 69.29 A N
ANISOU 376 N LEU A 51 6992 9872 9464 1705 3826 5400 A N
ATOM 377 CA LEU A 51 -18.342 25.261 3.530 1.00 63.88 A C
ANISOU 377 CA LEU A 51 6602 8654 9017 1392 3705 4924 A C
ATOM 378 C LEU A 51 -16.948 25.874 3.625 1.00 64.84 A C
ANISOU 378 C LEU A 51 6952 8180 9502 1435 3892 4847 A C
ATOM 379 O LEU A 51 -16.437 26.401 2.633 1.00 64.95 A O
ANISOU 379 O LEU A 51 6917 8251 9510 1601 4042 5078 A O
ATOM 380 CB LEU A 51 -18.220 23.746 3.310 1.00 62.00 A C
ANISOU 380 CB LEU A 51 6398 8676 8483 1009 3385 4544 A C
ATOM 381 CG LEU A 51 -19.491 22.924 3.272 1.00 67.65 A C
ANISOU 381 CG LEU A 51 6913 9961 8830 852 3191 4499 A C
ATOM 382 CD1 LEU A 51 -19.196 21.532 2.807 1.00 66.69 A C
ANISOU 382 CD1 LEU A 51 6836 10082 8420 492 2956 4159 A C
ATOM 383 CD2 LEU A 51 -20.169 22.876 4.629 1.00 69.50 A C
ANISOU 383 CD2 LEU A 51 7230 9967 9209 775 3167 4355 A C
ATOM 384 N ASP A 52 -16.322 25.766 4.814 1.00 58.00 A N
ANISOU 384 N ASP A 52 6326 6778 8935 1276 3882 4508 A N
ATOM 385 CA ASP A 52 -14.972 26.271 5.078 1.00 55.75 A C
ANISOU 385 CA ASP A 52 6244 5945 8995 1263 4045 4350 A C
ATOM 386 C ASP A 52 -13.886 25.263 4.701 1.00 57.92 A C
ANISOU 386 C ASP A 52 6639 6195 9173 1010 3839 4011 A C
ATOM 387 O ASP A 52 -13.995 24.085 5.045 1.00 55.08 A O
ANISOU 387 O ASP A 52 6346 5945 8636 771 3572 3715 A O
ATOM 388 CB ASP A 52 -14.798 26.633 6.558 1.00 54.22 A C
ANISOU 388 CB ASP A 52 6217 5246 9137 1215 4131 4124 A C
ATOM 389 CG ASP A 52 -15.646 27.781 7.017 1.00 52.87 A C
ANISOU 389 CG ASP A 52 5976 4970 9144 1474 4399 4429 A C
ATOM 390 OD1 ASP A 52 -15.335 28.933 6.647 1.00 51.30 A O
ANISOU 390 OD1 ASP A 52 5787 4525 9179 1693 4738 4672 A O
ATOM 391 OD2 ASP A 52 -16.622 27.530 7.738 1.00 58.19 A O1-
ANISOU 391 OD2 ASP A 52 6591 5793 9725 1460 4296 4428 A O1-
ATOM 392 N THR A 53 -12.839 25.745 3.987 1.00 56.17 A N
ANISOU 392 N THR A 53 6456 5812 9076 1074 3994 4063 A N
ATOM 393 CA THR A 53 -11.641 24.987 3.584 1.00 54.22 A C
ANISOU 393 CA THR A 53 6322 5495 8786 880 3858 3767 A C
ATOM 394 C THR A 53 -10.415 25.877 3.735 1.00 56.55 A C
ANISOU 394 C THR A 53 6728 5318 9442 931 4112 3699 A C
ATOM 395 O THR A 53 -10.530 27.092 3.607 1.00 58.18 A O
ANISOU 395 O THR A 53 6893 5356 9856 1141 4428 3984 A O
ATOM 396 CB THR A 53 -11.713 24.421 2.143 1.00 64.12 A C
ANISOU 396 CB THR A 53 7443 7234 9688 869 3747 3909 A C
ATOM 397 CG2 THR A 53 -12.941 23.552 1.876 1.00 62.17 A C
ANISOU 397 CG2 THR A 53 7056 7511 9053 773 3511 3936 A C
ATOM 398 OG1 THR A 53 -11.599 25.473 1.192 1.00 71.78 A O
ANISOU 398 OG1 THR A 53 8294 8279 10700 1127 4012 4306 A O
ATOM 399 N LYS A 54 -9.250 25.281 4.011 1.00 51.12 A N
ANISOU 399 N LYS A 54 6177 4422 8823 741 3997 3318 A N
ATOM 400 CA LYS A 54 -7.976 26.001 4.129 1.00 51.12 A C
ANISOU 400 CA LYS A 54 6259 4031 9133 734 4214 3179 A C
ATOM 401 C LYS A 54 -6.864 25.054 3.698 1.00 52.50 A C
ANISOU 401 C LYS A 54 6498 4265 9183 566 4021 2883 A C
ATOM 402 O LYS A 54 -6.633 24.039 4.363 1.00 49.70 A O
ANISOU 402 O LYS A 54 6243 3900 8741 413 3775 2554 A O
ATOM 403 CB LYS A 54 -7.753 26.516 5.566 1.00 53.42 A C
ANISOU 403 CB LYS A 54 6649 3907 9741 689 4322 2942 A C
ATOM 404 CG LYS A 54 -6.689 27.599 5.671 1.00 63.95 A C
ANISOU 404 CG LYS A 54 8023 4853 11422 692 4643 2852 A C
ATOM 405 CD LYS A 54 -6.263 27.863 7.113 1.00 75.87 A C
ANISOU 405 CD LYS A 54 9620 6024 13184 571 4678 2482 A C
ATOM 406 CE LYS A 54 -5.129 28.872 7.151 1.00 84.81 A C
ANISOU 406 CE LYS A 54 10771 6812 14639 518 5003 2332 A C
ATOM 407 NZ LYS A 54 -4.565 29.053 8.522 1.00 88.88 A N1+
ANISOU 407 NZ LYS A 54 11340 7065 15366 372 5026 1916 A N1+
ATOM 408 N ASP A 55 -6.239 25.343 2.536 1.00 49.35 A N
ANISOU 408 N ASP A 55 6045 3953 8752 617 4141 3027 A N
ATOM 409 CA ASP A 55 -5.148 24.555 1.924 1.00 48.32 A C
ANISOU 409 CA ASP A 55 5957 3901 8500 490 4002 2797 A C
ATOM 410 C ASP A 55 -5.585 23.087 1.697 1.00 48.14 A C
ANISOU 410 C ASP A 55 5958 4222 8112 364 3658 2668 A C
ATOM 411 O ASP A 55 -4.807 22.157 1.894 1.00 43.93 A O
ANISOU 411 O ASP A 55 5532 3653 7509 228 3483 2344 A O
ATOM 412 CB ASP A 55 -3.859 24.628 2.780 1.00 49.82 A C
ANISOU 412 CB ASP A 55 6249 3732 8947 375 4037 2402 A C
ATOM 413 CG ASP A 55 -3.351 26.038 3.038 1.00 60.40 A C
ANISOU 413 CG ASP A 55 7574 4719 10656 435 4406 2456 A C
ATOM 414 OD1 ASP A 55 -3.171 26.792 2.059 1.00 64.87 A O
ANISOU 414 OD1 ASP A 55 8082 5286 11280 536 4655 2726 A O
ATOM 415 OD2 ASP A 55 -3.103 26.374 4.220 1.00 63.56 A O1-
ANISOU 415 OD2 ASP A 55 8025 4841 11284 374 4464 2215 A O1-
ATOM 416 N LEU A 56 -6.864 22.911 1.320 1.00 45.02 A N
ANISOU 416 N LEU A 56 5460 4162 7484 415 3589 2922 A N
ATOM 417 CA LEU A 56 -7.524 21.648 1.029 1.00 43.52 A C
ANISOU 417 CA LEU A 56 5267 4333 6937 275 3322 2833 A C
ATOM 418 C LEU A 56 -7.724 21.488 -0.462 1.00 52.03 A C
ANISOU 418 C LEU A 56 6199 5844 7726 304 3315 3054 A C
ATOM 419 O LEU A 56 -8.032 22.458 -1.157 1.00 54.42 A O
ANISOU 419 O LEU A 56 6353 6279 8046 499 3507 3418 A O
ATOM 420 CB LEU A 56 -8.907 21.590 1.713 1.00 43.06 A C
ANISOU 420 CB LEU A 56 5155 4407 6800 283 3256 2934 A C
ATOM 421 CG LEU A 56 -9.105 20.804 3.003 1.00 43.03 A C
ANISOU 421 CG LEU A 56 5311 4225 6816 132 3087 2621 A C
ATOM 422 CD1 LEU A 56 -10.575 20.700 3.302 1.00 42.98 A C
ANISOU 422 CD1 LEU A 56 5204 4464 6663 132 3034 2773 A C
ATOM 423 CD2 LEU A 56 -8.566 19.396 2.895 1.00 42.33 A C
ANISOU 423 CD2 LEU A 56 5368 4200 6515 -72 2878 2301 A C
ATOM 424 N THR A 57 -7.594 20.255 -0.950 1.00 49.11 A N
ANISOU 424 N THR A 57 5877 5707 7077 120 3110 2840 A N
ATOM 425 CA THR A 57 -7.828 19.942 -2.349 1.00 50.32 A C
ANISOU 425 CA THR A 57 5885 6327 6905 105 3075 2993 A C
ATOM 426 C THR A 57 -9.117 19.122 -2.406 1.00 54.35 A C
ANISOU 426 C THR A 57 6308 7257 7084 -33 2903 2978 A C
ATOM 427 O THR A 57 -9.189 18.051 -1.802 1.00 52.63 A O
ANISOU 427 O THR A 57 6244 6962 6791 -245 2745 2659 A O
ATOM 428 CB THR A 57 -6.603 19.249 -2.968 1.00 52.01 A C
ANISOU 428 CB THR A 57 6210 6488 7062 -10 3019 2748 A C
ATOM 429 CG2 THR A 57 -6.770 19.004 -4.459 1.00 49.80 A C
ANISOU 429 CG2 THR A 57 5776 6697 6449 -24 3002 2902 A C
ATOM 430 OG1 THR A 57 -5.442 20.059 -2.746 1.00 49.37 A O
ANISOU 430 OG1 THR A 57 5940 5761 7057 100 3189 2734 A O
ATOM 431 N ILE A 58 -10.140 19.646 -3.093 1.00 53.31 A N
ANISOU 431 N ILE A 58 5928 7574 6755 96 2955 3324 A N
ATOM 432 CA ILE A 58 -11.419 18.958 -3.238 1.00 55.10 A C
ANISOU 432 CA ILE A 58 6009 8288 6637 -42 2808 3317 A C
ATOM 433 C ILE A 58 -11.397 18.244 -4.593 1.00 59.52 A C
ANISOU 433 C ILE A 58 6447 9360 6807 -175 2721 3277 A C
ATOM 434 O ILE A 58 -11.257 18.889 -5.633 1.00 59.64 A O
ANISOU 434 O ILE A 58 6290 9651 6720 8 2823 3568 A O
ATOM 435 CB ILE A 58 -12.631 19.925 -3.047 1.00 60.75 A C
ANISOU 435 CB ILE A 58 6497 9240 7347 190 2908 3702 A C
ATOM 436 CG1 ILE A 58 -12.663 20.489 -1.611 1.00 59.85 A C
ANISOU 436 CG1 ILE A 58 6529 8599 7614 275 2989 3675 A C
ATOM 437 CG2 ILE A 58 -13.967 19.247 -3.363 1.00 62.81 A C
ANISOU 437 CG2 ILE A 58 6542 10122 7202 46 2759 3701 A C
ATOM 438 CD1 ILE A 58 -12.177 21.918 -1.518 1.00 68.66 A C
ANISOU 438 CD1 ILE A 58 7648 9372 9069 579 3257 3969 A C
ATOM 439 N LYS A 59 -11.478 16.902 -4.558 1.00 55.66 A N
ANISOU 439 N LYS A 59 6071 8967 6109 -497 2557 2904 A N
ATOM 440 CA LYS A 59 -11.444 16.053 -5.752 1.00 56.73 A C
ANISOU 440 CA LYS A 59 6124 9563 5869 -691 2477 2775 A C
ATOM 441 C LYS A 59 -12.826 16.005 -6.412 1.00 64.65 A C
ANISOU 441 C LYS A 59 6794 11296 6475 -734 2425 2943 A C
ATOM 442 O LYS A 59 -12.945 16.386 -7.575 1.00 65.89 A O
ANISOU 442 O LYS A 59 6709 11936 6391 -612 2460 3183 A O
ATOM 443 CB LYS A 59 -10.944 14.637 -5.418 1.00 55.79 A C
ANISOU 443 CB LYS A 59 6286 9210 5700 -1019 2373 2296 A C
ATOM 444 CG LYS A 59 -9.535 14.579 -4.843 1.00 46.54 A C
ANISOU 444 CG LYS A 59 5412 7414 4856 -962 2409 2116 A C
ATOM 445 CD LYS A 59 -9.229 13.162 -4.452 1.00 52.32 A C
ANISOU 445 CD LYS A 59 6425 7941 5514 -1241 2328 1686 A C
ATOM 446 CE LYS A 59 -8.143 13.010 -3.424 1.00 47.67 A C
ANISOU 446 CE LYS A 59 6131 6731 5249 -1164 2343 1497 A C
ATOM 447 NZ LYS A 59 -7.851 11.568 -3.194 1.00 43.20 A N1+
ANISOU 447 NZ LYS A 59 5849 5996 4569 -1396 2295 1116 A N1+
ATOM 448 N LYS A 60 -13.867 15.546 -5.674 1.00 62.85 A N
ANISOU 448 N LYS A 60 6538 11181 6162 -900 2348 2818 A N
ATOM 449 CA LYS A 60 -15.232 15.506 -6.188 1.00 66.61 A C
ANISOU 449 CA LYS A 60 6665 12388 6254 -954 2295 2949 A C
ATOM 450 C LYS A 60 -16.255 15.671 -5.066 1.00 72.99 A C
ANISOU 450 C LYS A 60 7440 13138 7156 -957 2278 2976 A C
ATOM 451 O LYS A 60 -15.970 15.372 -3.907 1.00 70.43 A O
ANISOU 451 O LYS A 60 7403 12248 7111 -1051 2271 2759 A O
ATOM 452 CB LYS A 60 -15.515 14.241 -7.024 1.00 71.19 A C
ANISOU 452 CB LYS A 60 7178 13467 6405 -1345 2191 2613 A C
ATOM 453 CG LYS A 60 -15.728 12.942 -6.261 1.00 87.19 A C
ANISOU 453 CG LYS A 60 9465 15244 8417 -1757 2128 2131 A C
ATOM 454 CD LYS A 60 -16.585 11.981 -7.089 1.00104.65 A C
ANISOU 454 CD LYS A 60 11471 18152 10141 -2134 2065 1880 A C
ATOM 455 CE LYS A 60 -16.810 10.639 -6.434 1.00119.58 A C
ANISOU 455 CE LYS A 60 13622 19817 11997 -2569 2055 1405 A C
ATOM 456 NZ LYS A 60 -15.619 9.758 -6.556 1.00129.12 A N1+
ANISOU 456 NZ LYS A 60 15212 20547 13301 -2743 2094 1072 A N1+
ATOM 457 N VAL A 61 -17.439 16.184 -5.430 1.00 74.08 A N
ANISOU 457 N VAL A 61 7209 13893 7044 -824 2279 3262 A N
ATOM 458 CA VAL A 61 -18.586 16.395 -4.552 1.00 74.74 A C
ANISOU 458 CA VAL A 61 7175 14079 7143 -805 2266 3333 A C
ATOM 459 C VAL A 61 -19.771 15.665 -5.177 1.00 85.68 A C
ANISOU 459 C VAL A 61 8233 16294 8025 -1072 2160 3208 A C
ATOM 460 O VAL A 61 -20.020 15.828 -6.370 1.00 88.58 A O
ANISOU 460 O VAL A 61 8284 17324 8046 -985 2147 3390 A O
ATOM 461 CB VAL A 61 -18.895 17.896 -4.290 1.00 78.60 A C
ANISOU 461 CB VAL A 61 7514 14503 7847 -323 2409 3840 A C
ATOM 462 CG1 VAL A 61 -20.065 18.054 -3.318 1.00 78.58 A C
ANISOU 462 CG1 VAL A 61 7403 14585 7867 -311 2397 3888 A C
ATOM 463 CG2 VAL A 61 -17.674 18.635 -3.757 1.00 75.44 A C
ANISOU 463 CG2 VAL A 61 7420 13313 7932 -104 2543 3922 A C
ATOM 464 N ALA A 62 -20.487 14.853 -4.377 1.00 84.76 A N
ANISOU 464 N ALA A 62 8187 16160 7856 -1406 2095 2886 A N
ATOM 465 CA ALA A 62 -21.657 14.089 -4.813 1.00 88.71 A C
ANISOU 465 CA ALA A 62 8388 17420 7897 -1735 2013 2690 A C
ATOM 466 C ALA A 62 -22.818 14.242 -3.830 1.00 94.24 A C
ANISOU 466 C ALA A 62 8972 18212 8625 -1754 2007 2720 A C
ATOM 467 O ALA A 62 -22.671 13.943 -2.645 1.00 91.65 A O
ANISOU 467 O ALA A 62 8963 17256 8604 -1857 2029 2539 A O
ATOM 468 CB ALA A 62 -21.293 12.620 -4.974 1.00 89.28 A C
ANISOU 468 CB ALA A 62 8701 17395 7828 -2250 1973 2150 A C
ATOM 469 N VAL A 63 -23.976 14.705 -4.332 1.00 95.34 A N
ANISOU 469 N VAL A 63 8636 19166 8422 -1638 1981 2957 A N
ATOM 470 CA VAL A 63 -25.197 14.891 -3.543 1.00 96.57 A C
ANISOU 470 CA VAL A 63 8600 19550 8540 -1640 1976 3011 A C
ATOM 471 C VAL A 63 -26.255 13.920 -4.094 1.00105.32 A C
ANISOU 471 C VAL A 63 9384 21498 9134 -2090 1891 2686 A C
ATOM 472 O VAL A 63 -26.736 14.099 -5.216 1.00108.67 A O
ANISOU 472 O VAL A 63 9384 22771 9135 -2029 1846 2824 A O
ATOM 473 CB VAL A 63 -25.686 16.371 -3.519 1.00101.79 A C
ANISOU 473 CB VAL A 63 8976 20424 9275 -1059 2050 3601 A C
ATOM 474 CG1 VAL A 63 -26.869 16.550 -2.573 1.00102.59 A C
ANISOU 474 CG1 VAL A 63 8888 20743 9349 -1056 2050 3645 A C
ATOM 475 CG2 VAL A 63 -24.559 17.325 -3.138 1.00 98.38 A C
ANISOU 475 CG2 VAL A 63 8873 19156 9350 -669 2174 3872 A C
ATOM 476 N ASN A 64 -26.572 12.871 -3.305 1.00101.91 A N
ANISOU 476 N ASN A 64 9165 20821 8734 -2555 1887 2237 A N
ATOM 477 CA ASN A 64 -27.522 11.785 -3.601 1.00105.29 A C
ANISOU 477 CA ASN A 64 9376 21891 8740 -3094 1852 1817 A C
ATOM 478 C ASN A 64 -27.104 10.952 -4.859 1.00110.67 A C
ANISOU 478 C ASN A 64 10002 22977 9070 -3430 1826 1513 A C
ATOM 479 O ASN A 64 -27.962 10.385 -5.544 1.00114.61 A O
ANISOU 479 O ASN A 64 10139 24305 9102 -3778 1793 1273 A O
ATOM 480 CB ASN A 64 -28.977 12.297 -3.716 1.00111.61 A C
ANISOU 480 CB ASN A 64 9608 23592 9205 -2983 1811 2030 A C
ATOM 481 CG ASN A 64 -29.680 12.582 -2.399 1.00141.96 A C
ANISOU 481 CG ASN A 64 13504 27140 13293 -2902 1848 2108 A C
ATOM 482 ND2 ASN A 64 -30.840 13.216 -2.482 1.00137.72 A N
ANISOU 482 ND2 ASN A 64 12476 27341 12509 -2693 1821 2377 A N
ATOM 483 OD1 ASN A 64 -29.225 12.221 -1.304 1.00137.37 A O
ANISOU 483 OD1 ASN A 64 13383 25712 13097 -3019 1904 1928 A O
ATOM 484 N GLY A 65 -25.791 10.860 -5.099 1.00103.59 A N
ANISOU 484 N GLY A 65 9466 21488 8404 -3347 1851 1494 A N
ATOM 485 CA GLY A 65 -25.183 10.060 -6.159 1.00104.27 A C
ANISOU 485 CA GLY A 65 9599 21776 8243 -3641 1848 1200 A C
ATOM 486 C GLY A 65 -25.359 10.498 -7.599 1.00111.08 A C
ANISOU 486 C GLY A 65 9991 23529 8684 -3472 1782 1427 A C
ATOM 487 O GLY A 65 -26.155 9.900 -8.325 1.00114.99 A O
ANISOU 487 O GLY A 65 10127 24868 8696 -3814 1746 1183 A O
ATOM 488 N LYS A 66 -24.569 11.493 -8.048 1.00105.83 A N
ANISOU 488 N LYS A 66 9332 22693 8184 -2965 1782 1871 A N
ATOM 489 CA LYS A 66 -24.577 11.984 -9.434 1.00108.70 A C
ANISOU 489 CA LYS A 66 9297 23833 8174 -2734 1741 2145 A C
ATOM 490 C LYS A 66 -23.266 12.709 -9.771 1.00110.51 A C
ANISOU 490 C LYS A 66 9773 23509 8707 -2332 1792 2454 A C
ATOM 491 O LYS A 66 -22.638 12.399 -10.788 1.00111.10 A O
ANISOU 491 O LYS A 66 9851 23768 8594 -2429 1784 2345 A O
ATOM 492 CB LYS A 66 -25.791 12.910 -9.709 1.00114.31 A C
ANISOU 492 CB LYS A 66 9444 25402 8588 -2380 1702 2579 A C
ATOM 493 CG LYS A 66 -25.839 13.541 -11.117 1.00121.31 A C
ANISOU 493 CG LYS A 66 9901 27123 9070 -2044 1675 2947 A C
ATOM 494 CD LYS A 66 -26.256 12.568 -12.229 1.00127.91 A C
ANISOU 494 CD LYS A 66 10413 28878 9310 -2500 1593 2554 A C
ATOM 495 CE LYS A 66 -25.797 13.021 -13.599 1.00132.74 A C
ANISOU 495 CE LYS A 66 10782 30033 9621 -2203 1582 2847 A C
ATOM 496 NZ LYS A 66 -26.602 14.158 -14.122 1.00142.00 A N1+
ANISOU 496 NZ LYS A 66 11420 32055 10480 -1659 1568 3428 A N1+
ATOM 497 N ASP A 67 -22.889 13.683 -8.910 1.00103.94 A N
ANISOU 497 N ASP A 67 9133 22025 8335 -1898 1860 2825 A N
ATOM 498 CA ASP A 67 -21.755 14.618 -8.935 1.00100.96 A C
ANISOU 498 CA ASP A 67 8986 21038 8334 -1467 1949 3171 A C
ATOM 499 C ASP A 67 -22.309 16.029 -9.029 1.00105.66 A C
ANISOU 499 C ASP A 67 9280 21922 8945 -898 2023 3784 A C
ATOM 500 O ASP A 67 -23.009 16.362 -9.987 1.00110.02 A O
ANISOU 500 O ASP A 67 9402 23322 9079 -712 2006 4051 A O
ATOM 501 CB ASP A 67 -20.713 14.340 -10.040 1.00103.27 A C
ANISOU 501 CB ASP A 67 9362 21368 8510 -1522 1953 3085 A C
ATOM 502 CG ASP A 67 -19.628 13.352 -9.646 1.00112.13 A C
ANISOU 502 CG ASP A 67 10958 21789 9859 -1890 1952 2604 A C
ATOM 503 OD1 ASP A 67 -19.888 12.498 -8.765 1.00110.79 A O
ANISOU 503 OD1 ASP A 67 11052 21158 9887 -2153 1945 2295 A O
ATOM 504 OD2 ASP A 67 -18.519 13.425 -10.227 1.00118.24 A O1-
ANISOU 504 OD2 ASP A 67 11842 22478 10607 -1895 1971 2551 A O1-
ATOM 505 N ALA A 68 -22.052 16.832 -7.992 1.00 98.30 A N
ANISOU 505 N ALA A 68 8568 20304 8478 -623 2119 3997 A N
ATOM 506 CA ALA A 68 -22.524 18.208 -7.872 1.00 98.92 A C
ANISOU 506 CA ALA A 68 8446 20475 8664 -73 2244 4568 A C
ATOM 507 C ALA A 68 -21.453 19.199 -8.308 1.00100.02 A C
ANISOU 507 C ALA A 68 8734 20203 9064 334 2407 4934 A C
ATOM 508 O ALA A 68 -20.258 18.943 -8.139 1.00 96.99 A O
ANISOU 508 O ALA A 68 8720 19151 8982 207 2431 4722 A O
ATOM 509 CB ALA A 68 -22.945 18.487 -6.439 1.00 97.46 A C
ANISOU 509 CB ALA A 68 8432 19753 8845 -31 2287 4562 A C
ATOM 510 N THR A 69 -21.886 20.331 -8.878 1.00 97.75 A N
ANISOU 510 N THR A 69 8157 20333 8651 834 2538 5490 A N
ATOM 511 CA THR A 69 -20.981 21.369 -9.365 1.00 96.62 A C
ANISOU 511 CA THR A 69 8129 19850 8730 1251 2746 5892 A C
ATOM 512 C THR A 69 -20.445 22.160 -8.164 1.00 94.85 A C
ANISOU 512 C THR A 69 8258 18666 9116 1443 2929 5997 A C
ATOM 513 O THR A 69 -21.224 22.791 -7.442 1.00 95.33 A O
ANISOU 513 O THR A 69 8236 18693 9295 1675 3017 6230 A O
ATOM 514 CB THR A 69 -21.689 22.252 -10.410 1.00107.72 A C
ANISOU 514 CB THR A 69 9107 22065 9754 1732 2851 6463 A C
ATOM 515 CG2 THR A 69 -20.725 23.105 -11.199 1.00107.02 A C
ANISOU 515 CG2 THR A 69 9126 21737 9799 2100 3069 6839 A C
ATOM 516 OG1 THR A 69 -22.422 21.419 -11.311 1.00110.21 A O
ANISOU 516 OG1 THR A 69 9041 23370 9464 1495 2648 6292 A O
ATOM 517 N PHE A 70 -19.123 22.073 -7.924 1.00 85.66 A N
ANISOU 517 N PHE A 70 7475 16747 8324 1322 2983 5789 A N
ATOM 518 CA PHE A 70 -18.482 22.788 -6.826 1.00 81.64 A C
ANISOU 518 CA PHE A 70 7296 15342 8381 1456 3159 5825 A C
ATOM 519 C PHE A 70 -17.552 23.886 -7.346 1.00 86.19 A C
ANISOU 519 C PHE A 70 7979 15567 9203 1817 3435 6186 A C
ATOM 520 O PHE A 70 -17.051 23.809 -8.481 1.00 85.83 A O
ANISOU 520 O PHE A 70 7856 15812 8942 1858 3447 6277 A O
ATOM 521 CB PHE A 70 -17.752 21.844 -5.858 1.00 78.71 A C
ANISOU 521 CB PHE A 70 7282 14342 8282 1030 3019 5269 A C
ATOM 522 CG PHE A 70 -16.646 21.001 -6.435 1.00 78.45 A C
ANISOU 522 CG PHE A 70 7429 14174 8206 753 2924 4937 A C
ATOM 523 CD1 PHE A 70 -15.325 21.430 -6.384 1.00 79.40 A C
ANISOU 523 CD1 PHE A 70 7815 13668 8685 833 3061 4921 A C
ATOM 524 CD2 PHE A 70 -16.916 19.755 -6.988 1.00 81.15 A C
ANISOU 524 CD2 PHE A 70 7677 15001 8153 391 2712 4609 A C
ATOM 525 CE1 PHE A 70 -14.298 20.644 -6.905 1.00 78.99 A C
ANISOU 525 CE1 PHE A 70 7919 13505 8588 595 2975 4617 A C
ATOM 526 CE2 PHE A 70 -15.886 18.959 -7.493 1.00 82.76 A C
ANISOU 526 CE2 PHE A 70 8066 15052 8327 146 2644 4297 A C
ATOM 527 CZ PHE A 70 -14.584 19.413 -7.456 1.00 78.99 A C
ANISOU 527 CZ PHE A 70 7839 13973 8199 267 2769 4317 A C
ATOM 528 N ALA A 71 -17.355 24.930 -6.513 1.00 83.05 A N
ANISOU 528 N ALA A 71 7757 14548 9251 2073 3681 6390 A N
ATOM 529 CA ALA A 71 -16.537 26.089 -6.857 1.00 84.38 A C
ANISOU 529 CA ALA A 71 8053 14298 9708 2408 4011 6731 A C
ATOM 530 C ALA A 71 -15.890 26.737 -5.630 1.00 86.81 A C
ANISOU 530 C ALA A 71 8685 13706 10593 2416 4208 6620 A C
ATOM 531 O ALA A 71 -16.582 27.144 -4.695 1.00 85.08 A O
ANISOU 531 O ALA A 71 8472 13316 10538 2505 4267 6678 A O
ATOM 532 CB ALA A 71 -17.379 27.120 -7.599 1.00 89.71 A C
ANISOU 532 CB ALA A 71 8450 15463 10174 2921 4238 7362 A C
ATOM 533 N LEU A 72 -14.550 26.859 -5.668 1.00 83.83 A N
ANISOU 533 N LEU A 72 8558 12785 10508 2322 4322 6457 A N
ATOM 534 CA LEU A 72 -13.743 27.510 -4.638 1.00 81.83 A C
ANISOU 534 CA LEU A 72 8595 11708 10788 2304 4533 6316 A C
ATOM 535 C LEU A 72 -13.642 29.011 -4.943 1.00 87.41 A C
ANISOU 535 C LEU A 72 9322 12158 11731 2728 4986 6811 A C
ATOM 536 O LEU A 72 -13.463 29.388 -6.098 1.00 89.31 A O
ANISOU 536 O LEU A 72 9470 12655 11808 2943 5136 7135 A O
ATOM 537 CB LEU A 72 -12.352 26.868 -4.558 1.00 79.34 A C
ANISOU 537 CB LEU A 72 8507 11004 10636 1979 4429 5867 A C
ATOM 538 CG LEU A 72 -12.198 25.629 -3.663 1.00 81.53 A C
ANISOU 538 CG LEU A 72 8909 11166 10902 1578 4094 5321 A C
ATOM 539 CD1 LEU A 72 -12.651 24.355 -4.373 1.00 82.32 A C
ANISOU 539 CD1 LEU A 72 8861 11887 10528 1361 3776 5163 A C
ATOM 540 CD2 LEU A 72 -10.748 25.445 -3.277 1.00 82.35 A C
ANISOU 540 CD2 LEU A 72 9266 10718 11306 1379 4110 4954 A C
ATOM 541 N GLY A 73 -13.784 29.838 -3.913 1.00 83.50 A N
ANISOU 541 N GLY A 73 8956 11163 11608 2846 5218 6868 A N
ATOM 542 CA GLY A 73 -13.753 31.290 -4.041 1.00 86.23 A C
ANISOU 542 CA GLY A 73 9363 11178 12223 3240 5704 7318 A C
ATOM 543 C GLY A 73 -12.369 31.879 -3.904 1.00 89.82 A C
ANISOU 543 C GLY A 73 10085 10939 13104 3148 5995 7162 A C
ATOM 544 O GLY A 73 -11.373 31.198 -4.168 1.00 87.54 A O
ANISOU 544 O GLY A 73 9874 10581 12806 2857 5824 6817 A O
ATOM 545 N THR A 74 -12.295 33.168 -3.519 1.00 88.48 A N
ANISOU 545 N THR A 74 10053 10257 13308 3395 6464 7415 A N
ATOM 546 CA THR A 74 -11.006 33.853 -3.356 1.00 87.63 A C
ANISOU 546 CA THR A 74 10193 9469 13632 3294 6811 7260 A C
ATOM 547 C THR A 74 -10.439 33.475 -1.986 1.00 86.19 A C
ANISOU 547 C THR A 74 10174 8817 13757 2902 6657 6666 A C
ATOM 548 O THR A 74 -11.159 33.485 -0.985 1.00 83.80 A O
ANISOU 548 O THR A 74 9874 8432 13535 2889 6587 6580 A O
ATOM 549 CB THR A 74 -11.112 35.381 -3.571 1.00 94.39 A C
ANISOU 549 CB THR A 74 11151 9948 14764 3693 7426 7751 A C
ATOM 550 CG2 THR A 74 -11.638 35.746 -4.934 1.00 94.90 A C
ANISOU 550 CG2 THR A 74 11061 10492 14506 4117 7594 8360 A C
ATOM 551 OG1 THR A 74 -11.959 35.950 -2.585 1.00100.39 A O
ANISOU 551 OG1 THR A 74 11929 10528 15686 3845 7557 7854 A O
ATOM 552 N THR A 75 -9.151 33.143 -1.954 1.00 80.89 A N
ANISOU 552 N THR A 75 9625 7875 13234 2600 6604 6266 A N
ATOM 553 CA THR A 75 -8.468 32.728 -0.740 1.00 77.73 A C
ANISOU 553 CA THR A 75 9357 7098 13079 2241 6443 5692 A C
ATOM 554 C THR A 75 -8.242 33.941 0.165 1.00 83.51 A C
ANISOU 554 C THR A 75 10251 7193 14284 2273 6888 5654 A C
ATOM 555 O THR A 75 -7.549 34.883 -0.209 1.00 85.47 A O
ANISOU 555 O THR A 75 10605 7077 14792 2330 7314 5755 A O
ATOM 556 CB THR A 75 -7.172 31.968 -1.098 1.00 81.07 A C
ANISOU 556 CB THR A 75 9824 7517 13464 1947 6244 5303 A C
ATOM 557 CG2 THR A 75 -6.404 31.486 0.133 1.00 74.23 A C
ANISOU 557 CG2 THR A 75 9063 6359 12780 1608 6034 4714 A C
ATOM 558 OG1 THR A 75 -7.517 30.844 -1.914 1.00 79.15 A O
ANISOU 558 OG1 THR A 75 9436 7864 12774 1934 5878 5368 A O
ATOM 559 N HIS A 76 -8.858 33.905 1.349 1.00 79.79 A N
ANISOU 559 N HIS A 76 9804 6595 13919 2224 6804 5497 A N
ATOM 560 CA HIS A 76 -8.742 34.928 2.381 1.00 81.75 A C
ANISOU 560 CA HIS A 76 10200 6266 14595 2213 7183 5390 A C
ATOM 561 C HIS A 76 -7.385 34.802 3.084 1.00 85.90 A C
ANISOU 561 C HIS A 76 10845 6405 15388 1841 7182 4815 A C
ATOM 562 O HIS A 76 -6.780 33.728 3.077 1.00 83.59 A O
ANISOU 562 O HIS A 76 10515 6326 14919 1602 6787 4470 A O
ATOM 563 CB HIS A 76 -9.897 34.795 3.385 1.00 82.11 A C
ANISOU 563 CB HIS A 76 10208 6378 14612 2268 7038 5388 A C
ATOM 564 CG HIS A 76 -10.061 35.983 4.274 1.00 87.82 A C
ANISOU 564 CG HIS A 76 11064 6570 15735 2360 7497 5426 A C
ATOM 565 CD2 HIS A 76 -10.865 37.062 4.134 1.00 93.25 A C
ANISOU 565 CD2 HIS A 76 11772 7125 16535 2720 7915 5900 A C
ATOM 566 ND1 HIS A 76 -9.321 36.122 5.432 1.00 88.38 A N
ANISOU 566 ND1 HIS A 76 11263 6192 16124 2064 7571 4927 A N
ATOM 567 CE1 HIS A 76 -9.696 37.276 5.958 1.00 90.50 A C
ANISOU 567 CE1 HIS A 76 11634 6053 16699 2220 8036 5088 A C
ATOM 568 NE2 HIS A 76 -10.628 37.874 5.217 1.00 93.80 A N
ANISOU 568 NE2 HIS A 76 12003 6621 17014 2627 8265 5681 A N
ATOM 569 N SER A 77 -6.928 35.900 3.703 1.00 85.54 A N
ANISOU 569 N SER A 77 10936 5807 15757 1796 7640 4706 A N
ATOM 570 CA SER A 77 -5.652 36.045 4.415 1.00 84.93 A C
ANISOU 570 CA SER A 77 10949 5352 15968 1450 7736 4162 A C
ATOM 571 C SER A 77 -5.471 35.019 5.561 1.00 85.10 A C
ANISOU 571 C SER A 77 10936 5501 15897 1174 7262 3640 A C
ATOM 572 O SER A 77 -4.338 34.591 5.806 1.00 84.30 A O
ANISOU 572 O SER A 77 10832 5377 15822 908 7116 3209 A O
ATOM 573 CB SER A 77 -5.526 37.469 4.961 1.00 91.61 A C
ANISOU 573 CB SER A 77 11939 5610 17258 1463 8340 4161 A C
ATOM 574 OG SER A 77 -4.198 37.776 5.350 1.00100.88 A O
ANISOU 574 OG SER A 77 13173 6452 18704 1121 8505 3650 A O
ATOM 575 N PHE A 78 -6.568 34.616 6.243 1.00 78.47 A N
ANISOU 575 N PHE A 78 10065 4811 14937 1253 7035 3692 A N
ATOM 576 CA PHE A 78 -6.492 33.647 7.352 1.00 74.95 A C
ANISOU 576 CA PHE A 78 9607 4476 14394 1029 6615 3246 A C
ATOM 577 C PHE A 78 -7.696 32.672 7.417 1.00 71.91 A C
ANISOU 577 C PHE A 78 9143 4520 13659 1135 6200 3416 A C
ATOM 578 O PHE A 78 -7.546 31.560 7.924 1.00 68.63 A O
ANISOU 578 O PHE A 78 8720 4296 13061 963 5795 3100 A O
ATOM 579 CB PHE A 78 -6.354 34.378 8.705 1.00 78.02 A C
ANISOU 579 CB PHE A 78 10077 4449 15117 905 6857 2941 A C
ATOM 580 CG PHE A 78 -7.386 35.458 8.961 1.00 82.31 A C
ANISOU 580 CG PHE A 78 10668 4764 15844 1139 7230 3292 A C
ATOM 581 CD1 PHE A 78 -8.608 35.150 9.551 1.00 84.08 A C
ANISOU 581 CD1 PHE A 78 10854 5166 15925 1261 7026 3423 A C
ATOM 582 CD2 PHE A 78 -7.129 36.781 8.622 1.00 88.17 A C
ANISOU 582 CD2 PHE A 78 11500 5097 16903 1241 7812 3489 A C
ATOM 583 CE1 PHE A 78 -9.562 36.141 9.777 1.00 87.61 A C
ANISOU 583 CE1 PHE A 78 11335 5418 16533 1503 7377 3756 A C
ATOM 584 CE2 PHE A 78 -8.081 37.772 8.854 1.00 93.58 A C
ANISOU 584 CE2 PHE A 78 12246 5552 17757 1492 8187 3831 A C
ATOM 585 CZ PHE A 78 -9.297 37.441 9.414 1.00 90.42 A C
ANISOU 585 CZ PHE A 78 11789 5368 17198 1634 7955 3971 A C
ATOM 586 N LYS A 79 -8.868 33.091 6.904 1.00 67.41 A N
ANISOU 586 N LYS A 79 8513 4109 12992 1420 6322 3909 A N
ATOM 587 CA LYS A 79 -10.121 32.331 6.920 1.00 64.85 A C
ANISOU 587 CA LYS A 79 8083 4212 12345 1524 5995 4095 A C
ATOM 588 C LYS A 79 -10.105 31.116 5.975 1.00 65.27 A C
ANISOU 588 C LYS A 79 8039 4763 11998 1466 5602 4119 A C
ATOM 589 O LYS A 79 -10.892 30.177 6.148 1.00 63.46 A O
ANISOU 589 O LYS A 79 7740 4884 11488 1425 5264 4099 A O
ATOM 590 CB LYS A 79 -11.313 33.243 6.572 1.00 69.69 A C
ANISOU 590 CB LYS A 79 8629 4882 12969 1874 6286 4627 A C
ATOM 591 CG LYS A 79 -11.682 34.252 7.651 1.00 76.96 A C
ANISOU 591 CG LYS A 79 9637 5397 14208 1937 6585 4600 A C
ATOM 592 CD LYS A 79 -13.135 34.673 7.543 1.00 87.55 A C
ANISOU 592 CD LYS A 79 10877 6939 15448 2283 6718 5091 A C
ATOM 593 CE LYS A 79 -13.304 36.112 7.145 1.00106.82 A C
ANISOU 593 CE LYS A 79 13392 9024 18171 2582 7306 5474 A C
ATOM 594 NZ LYS A 79 -14.727 36.538 7.226 1.00117.76 A N1+
ANISOU 594 NZ LYS A 79 14680 10594 19469 2947 7444 5934 A N1+
ATOM 595 N GLY A 80 -9.173 31.111 5.037 1.00 61.60 A N
ANISOU 595 N GLY A 80 7579 4308 11517 1432 5663 4122 A N
ATOM 596 CA GLY A 80 -9.033 30.049 4.053 1.00 59.71 A C
ANISOU 596 CA GLY A 80 7259 4507 10920 1372 5346 4134 A C
ATOM 597 C GLY A 80 -9.810 30.361 2.795 1.00 64.85 A C
ANISOU 597 C GLY A 80 7765 5533 11343 1647 5449 4657 A C
ATOM 598 O GLY A 80 -10.016 31.533 2.463 1.00 66.72 A O
ANISOU 598 O GLY A 80 7999 5599 11752 1899 5844 5016 A O
ATOM 599 N THR A 81 -10.281 29.322 2.110 1.00 60.13 A N
ANISOU 599 N THR A 81 7045 5459 10344 1611 5113 4705 A N
ATOM 600 CA THR A 81 -11.016 29.482 0.859 1.00 62.42 A C
ANISOU 600 CA THR A 81 7153 6226 10338 1857 5157 5170 A C
ATOM 601 C THR A 81 -12.441 28.987 0.997 1.00 66.58 A C
ANISOU 601 C THR A 81 7515 7220 10564 1922 4936 5316 A C
ATOM 602 O THR A 81 -12.645 27.887 1.496 1.00 64.66 A O
ANISOU 602 O THR A 81 7280 7131 10155 1672 4595 4993 A O
ATOM 603 CB THR A 81 -10.300 28.709 -0.252 1.00 63.57 A C
ANISOU 603 CB THR A 81 7261 6661 10232 1736 4978 5087 A C
ATOM 604 CG2 THR A 81 -10.788 29.077 -1.645 1.00 62.01 A C
ANISOU 604 CG2 THR A 81 6878 6926 9755 2010 5091 5574 A C
ATOM 605 OG1 THR A 81 -8.902 28.933 -0.128 1.00 61.84 A O
ANISOU 605 OG1 THR A 81 7199 6000 10297 1603 5120 4832 A O
ATOM 606 N PRO A 82 -13.447 29.720 0.500 1.00 66.20 A N
ANISOU 606 N PRO A 82 7303 7443 10406 2259 5126 5805 A N
ATOM 607 CA PRO A 82 -14.808 29.179 0.566 1.00 66.70 A C
ANISOU 607 CA PRO A 82 7162 8042 10138 2304 4898 5925 A C
ATOM 608 C PRO A 82 -15.066 28.162 -0.552 1.00 72.21 A C
ANISOU 608 C PRO A 82 7668 9412 10356 2206 4603 5936 A C
ATOM 609 O PRO A 82 -14.605 28.351 -1.674 1.00 73.31 A O
ANISOU 609 O PRO A 82 7749 9732 10374 2322 4695 6137 A O
ATOM 610 CB PRO A 82 -15.687 30.424 0.417 1.00 71.87 A C
ANISOU 610 CB PRO A 82 7706 8743 10859 2742 5248 6460 A C
ATOM 611 CG PRO A 82 -14.854 31.391 -0.399 1.00 77.98 A C
ANISOU 611 CG PRO A 82 8564 9249 11816 2960 5622 6732 A C
ATOM 612 CD PRO A 82 -13.406 31.051 -0.155 1.00 70.93 A C
ANISOU 612 CD PRO A 82 7892 7898 11161 2627 5574 6278 A C
ATOM 613 N LEU A 83 -15.806 27.090 -0.248 1.00 69.21 A N
ANISOU 613 N LEU A 83 7198 9396 9703 1975 4267 5702 A N
ATOM 614 CA LEU A 83 -16.215 26.085 -1.229 1.00 70.52 A C
ANISOU 614 CA LEU A 83 7166 10235 9393 1837 3997 5666 A C
ATOM 615 C LEU A 83 -17.756 26.114 -1.362 1.00 80.78 A C
ANISOU 615 C LEU A 83 8162 12161 10370 1996 3937 5942 A C
ATOM 616 O LEU A 83 -18.474 25.912 -0.376 1.00 79.07 A O
ANISOU 616 O LEU A 83 7946 11894 10202 1911 3856 5817 A O
ATOM 617 CB LEU A 83 -15.694 24.678 -0.869 1.00 66.89 A C
ANISOU 617 CB LEU A 83 6861 9699 8856 1391 3682 5119 A C
ATOM 618 CG LEU A 83 -16.376 23.485 -1.562 1.00 71.75 A C
ANISOU 618 CG LEU A 83 7291 10986 8987 1163 3398 4984 A C
ATOM 619 CD1 LEU A 83 -15.891 23.319 -2.995 1.00 73.73 A C
ANISOU 619 CD1 LEU A 83 7442 11591 8982 1172 3381 5070 A C
ATOM 620 CD2 LEU A 83 -16.177 22.208 -0.771 1.00 69.60 A C
ANISOU 620 CD2 LEU A 83 7210 10527 8708 762 3157 4474 A C
ATOM 621 N GLU A 84 -18.244 26.400 -2.586 1.00 83.54 A N
ANISOU 621 N GLU A 84 8238 13121 10382 2245 3990 6328 A N
ATOM 622 CA GLU A 84 -19.670 26.470 -2.923 1.00 87.24 A C
ANISOU 622 CA GLU A 84 8353 14314 10479 2439 3939 6627 A C
ATOM 623 C GLU A 84 -20.089 25.221 -3.688 1.00 94.50 A C
ANISOU 623 C GLU A 84 9051 15961 10894 2136 3616 6397 A C
ATOM 624 O GLU A 84 -19.437 24.861 -4.667 1.00 94.42 A O
ANISOU 624 O GLU A 84 9025 16148 10704 2055 3561 6352 A O
ATOM 625 CB GLU A 84 -19.996 27.726 -3.758 1.00 92.59 A C
ANISOU 625 CB GLU A 84 8846 15243 11090 2983 4250 7258 A C
ATOM 626 CG GLU A 84 -19.724 29.049 -3.068 1.00102.02 A C
ANISOU 626 CG GLU A 84 10243 15753 12765 3312 4639 7530 A C
ATOM 627 CD GLU A 84 -20.051 30.267 -3.906 1.00126.85 A C
ANISOU 627 CD GLU A 84 13235 19129 15834 3876 4988 8179 A C
ATOM 628 OE1 GLU A 84 -21.175 30.799 -3.759 1.00119.73 A O
ANISOU 628 OE1 GLU A 84 12118 18574 14800 4207 5086 8534 A O
ATOM 629 OE2 GLU A 84 -19.187 30.687 -4.710 1.00123.35 A O1-
ANISOU 629 OE2 GLU A 84 12882 18537 15446 4001 5173 8344 A O1-
ATOM 630 N ILE A 85 -21.170 24.563 -3.243 1.00 93.48 A N
ANISOU 630 N ILE A 85 8753 16228 10537 1951 3421 6234 A N
ATOM 631 CA ILE A 85 -21.722 23.373 -3.889 1.00 95.06 A C
ANISOU 631 CA ILE A 85 8725 17146 10248 1619 3143 5978 A C
ATOM 632 C ILE A 85 -23.136 23.671 -4.391 1.00104.63 A C
ANISOU 632 C ILE A 85 9476 19240 11038 1863 3132 6322 A C
ATOM 633 O ILE A 85 -23.998 24.075 -3.612 1.00104.83 A O
ANISOU 633 O ILE A 85 9410 19281 11138 2004 3184 6452 A O
ATOM 634 CB ILE A 85 -21.703 22.129 -2.961 1.00 94.98 A C
ANISOU 634 CB ILE A 85 8923 16866 10299 1105 2925 5402 A C
ATOM 635 CG1 ILE A 85 -20.267 21.769 -2.526 1.00 91.51 A C
ANISOU 635 CG1 ILE A 85 8909 15644 10215 893 2923 5066 A C
ATOM 636 CG2 ILE A 85 -22.399 20.921 -3.624 1.00 97.61 A C
ANISOU 636 CG2 ILE A 85 9008 17960 10118 737 2688 5126 A C
ATOM 637 CD1 ILE A 85 -20.169 21.173 -1.124 1.00 96.25 A C
ANISOU 637 CD1 ILE A 85 9803 15670 11097 621 2847 4679 A C
ATOM 638 N THR A 86 -23.356 23.409 -5.695 1.00105.53 A N
ANISOU 638 N THR A 86 9288 20124 10686 1894 3053 6440 A N
ATOM 639 CA THR A 86 -24.636 23.525 -6.382 1.00110.08 A C
ANISOU 639 CA THR A 86 9364 21709 10753 2091 3002 6723 A C
ATOM 640 C THR A 86 -25.383 22.215 -6.155 1.00115.04 A C
ANISOU 640 C THR A 86 9840 22807 11062 1560 2726 6226 A C
ATOM 641 O THR A 86 -24.902 21.151 -6.558 1.00113.48 A O
ANISOU 641 O THR A 86 9740 22655 10721 1114 2564 5793 A O
ATOM 642 CB THR A 86 -24.430 23.849 -7.872 1.00117.07 A C
ANISOU 642 CB THR A 86 10002 23201 11276 2360 3053 7056 A C
ATOM 643 CG2 THR A 86 -25.744 24.006 -8.627 1.00120.63 A C
ANISOU 643 CG2 THR A 86 9895 24778 11159 2623 3006 7384 A C
ATOM 644 OG1 THR A 86 -23.668 25.049 -7.987 1.00115.26 A O
ANISOU 644 OG1 THR A 86 9986 22403 11403 2809 3351 7479 A O
ATOM 645 N LEU A 87 -26.542 22.294 -5.490 1.00113.43 A N
ANISOU 645 N LEU A 87 9415 22920 10763 1602 2699 6280 A N
ATOM 646 CA LEU A 87 -27.379 21.134 -5.192 1.00113.57 A C
ANISOU 646 CA LEU A 87 9272 23391 10490 1104 2481 5826 A C
ATOM 647 C LEU A 87 -28.233 20.761 -6.412 1.00122.17 A C
ANISOU 647 C LEU A 87 9825 25679 10913 1054 2353 5866 A C
ATOM 648 O LEU A 87 -28.711 21.675 -7.090 1.00125.32 A O
ANISOU 648 O LEU A 87 9882 26655 11079 1559 2449 6383 A O
ATOM 649 CB LEU A 87 -28.276 21.430 -3.983 1.00113.25 A C
ANISOU 649 CB LEU A 87 9203 23201 10627 1177 2522 5872 A C
ATOM 650 CG LEU A 87 -27.576 21.488 -2.628 1.00113.18 A C
ANISOU 650 CG LEU A 87 9702 22101 11200 1051 2588 5655 A C
ATOM 651 CD1 LEU A 87 -27.310 22.925 -2.209 1.00112.94 A C
ANISOU 651 CD1 LEU A 87 9810 21517 11584 1601 2845 6130 A C
ATOM 652 CD2 LEU A 87 -28.395 20.779 -1.572 1.00114.39 A C
ANISOU 652 CD2 LEU A 87 9854 22269 11341 692 2480 5306 A C
ATOM 653 N PRO A 88 -28.455 19.447 -6.709 1.00119.04 A N
ANISOU 653 N PRO A 88 9343 25698 10189 465 2158 5330 A N
ATOM 654 CA PRO A 88 -29.303 19.082 -7.863 1.00123.82 A C
ANISOU 654 CA PRO A 88 9401 27515 10129 379 2038 5321 A C
ATOM 655 C PRO A 88 -30.742 19.588 -7.714 1.00132.02 A C
ANISOU 655 C PRO A 88 9941 29350 10869 644 2037 5606 A C
ATOM 656 O PRO A 88 -31.365 19.934 -8.719 1.00136.39 A O
ANISOU 656 O PRO A 88 9999 30889 10934 929 2016 5913 A O
ATOM 657 CB PRO A 88 -29.247 17.548 -7.881 1.00124.48 A C
ANISOU 657 CB PRO A 88 9590 27667 10038 -374 1881 4613 A C
ATOM 658 CG PRO A 88 -28.032 17.195 -7.099 1.00123.38 A C
ANISOU 658 CG PRO A 88 10085 26340 10456 -578 1928 4343 A C
ATOM 659 CD PRO A 88 -27.966 18.236 -6.021 1.00116.77 A C
ANISOU 659 CD PRO A 88 9445 24820 10102 -144 2064 4710 A C
ATOM 660 N PHE A 89 -31.249 19.666 -6.461 1.00127.44 A N
ANISOU 660 N PHE A 89 9488 28358 10577 586 2065 5526 A N
ATOM 661 CA PHE A 89 -32.581 20.182 -6.125 1.00130.78 A C
ANISOU 661 CA PHE A 89 9487 29410 10792 846 2082 5787 A C
ATOM 662 C PHE A 89 -32.485 21.164 -4.940 1.00132.47 A C
ANISOU 662 C PHE A 89 9999 28771 11564 1248 2264 6111 A C
ATOM 663 O PHE A 89 -31.626 21.010 -4.067 1.00126.83 A O
ANISOU 663 O PHE A 89 9809 27020 11360 1071 2311 5894 A O
ATOM 664 CB PHE A 89 -33.598 19.053 -5.870 1.00134.22 A C
ANISOU 664 CB PHE A 89 9664 30451 10884 248 1918 5260 A C
ATOM 665 CG PHE A 89 -33.295 18.061 -4.771 1.00131.54 A C
ANISOU 665 CG PHE A 89 9786 29306 10887 -348 1881 4682 A C
ATOM 666 CD1 PHE A 89 -34.017 18.074 -3.584 1.00133.64 A C
ANISOU 666 CD1 PHE A 89 10091 29347 11340 -432 1907 4594 A C
ATOM 667 CD2 PHE A 89 -32.348 17.058 -4.957 1.00131.08 A C
ANISOU 667 CD2 PHE A 89 10100 28786 10919 -831 1828 4218 A C
ATOM 668 CE1 PHE A 89 -33.763 17.132 -2.581 1.00130.98 A C
ANISOU 668 CE1 PHE A 89 10178 28302 11285 -967 1888 4077 A C
ATOM 669 CE2 PHE A 89 -32.089 16.123 -3.951 1.00130.38 A C
ANISOU 669 CE2 PHE A 89 10442 27978 11120 -1343 1819 3713 A C
ATOM 670 CZ PHE A 89 -32.799 16.165 -2.770 1.00127.56 A C
ANISOU 670 CZ PHE A 89 10130 27392 10946 -1405 1850 3651 A C
ATOM 671 N SER A 90 -33.358 22.191 -4.947 1.00133.60 A N
ANISOU 671 N SER A 90 9792 29385 11586 1812 2378 6639 A N
ATOM 672 CA SER A 90 -33.409 23.307 -3.992 1.00132.64 A C
ANISOU 672 CA SER A 90 9867 28606 11923 2297 2598 7040 A C
ATOM 673 C SER A 90 -33.909 22.957 -2.549 1.00134.79 A C
ANISOU 673 C SER A 90 10326 28397 12491 2000 2574 6724 A C
ATOM 674 O SER A 90 -33.868 23.837 -1.680 1.00132.80 A O
ANISOU 674 O SER A 90 10297 27495 12666 2347 2762 6993 A O
ATOM 675 CB SER A 90 -34.250 24.450 -4.560 1.00141.34 A C
ANISOU 675 CB SER A 90 10501 30469 12733 2998 2741 7703 A C
ATOM 676 OG SER A 90 -35.473 24.004 -5.126 1.00152.88 A O
ANISOU 676 OG SER A 90 11475 32945 13667 2842 2557 7520 A O
ATOM 677 N LEU A 91 -34.350 21.697 -2.292 1.00131.47 A N
ANISOU 677 N LEU A 91 9832 28267 11853 1363 2372 6157 A N
ATOM 678 CA LEU A 91 -34.831 21.186 -0.986 1.00129.23 A C
ANISOU 678 CA LEU A 91 9720 27590 11791 1010 2340 5805 A C
ATOM 679 C LEU A 91 -36.100 21.911 -0.465 1.00136.95 A C
ANISOU 679 C LEU A 91 10339 29013 12684 1381 2422 6138 A C
ATOM 680 O LEU A 91 -36.587 22.856 -1.090 1.00140.75 A O
ANISOU 680 O LEU A 91 10475 30028 12976 1967 2527 6681 A O
ATOM 681 CB LEU A 91 -33.734 21.258 0.111 1.00123.52 A C
ANISOU 681 CB LEU A 91 9652 25562 11716 924 2431 5649 A C
ATOM 682 CG LEU A 91 -32.413 20.527 -0.111 1.00124.58 A C
ANISOU 682 CG LEU A 91 10218 25087 12031 574 2370 5301 A C
ATOM 683 CD1 LEU A 91 -31.318 21.183 0.688 1.00120.39 A C
ANISOU 683 CD1 LEU A 91 10203 23432 12106 781 2517 5398 A C
ATOM 684 CD2 LEU A 91 -32.510 19.069 0.296 1.00125.75 A C
ANISOU 684 CD2 LEU A 91 10505 25212 12063 -132 2214 4661 A C
ATOM 685 N THR A 92 -36.632 21.448 0.686 1.00132.09 A N
ANISOU 685 N THR A 92 9813 28176 12199 1048 2387 5817 A N
ATOM 686 CA THR A 92 -37.793 22.037 1.365 1.00134.48 A C
ANISOU 686 CA THR A 92 9829 28796 12470 1334 2464 6062 A C
ATOM 687 C THR A 92 -37.511 22.047 2.883 1.00133.88 A C
ANISOU 687 C THR A 92 10242 27682 12945 1194 2547 5871 A C
ATOM 688 O THR A 92 -37.841 21.082 3.572 1.00132.48 A O
ANISOU 688 O THR A 92 10160 27422 12756 655 2447 5393 A O
ATOM 689 CB THR A 92 -39.124 21.317 0.996 1.00147.16 A C
ANISOU 689 CB THR A 92 10847 31587 13482 1029 2311 5841 A C
ATOM 690 CG2 THR A 92 -39.671 21.729 -0.368 1.00151.20 A C
ANISOU 690 CG2 THR A 92 10767 33260 13424 1369 2267 6184 A C
ATOM 691 OG1 THR A 92 -38.961 19.898 1.058 1.00145.13 A O
ANISOU 691 OG1 THR A 92 10745 31271 13127 251 2161 5172 A O
ATOM 692 N ARG A 93 -36.882 23.141 3.389 1.00127.64 A N
ANISOU 692 N ARG A 93 9767 26101 12629 1672 2749 6236 A N
ATOM 693 CA ARG A 93 -36.482 23.376 4.800 1.00122.64 A C
ANISOU 693 CA ARG A 93 9605 24447 12545 1634 2858 6117 A C
ATOM 694 C ARG A 93 -37.571 22.914 5.798 1.00124.12 A C
ANISOU 694 C ARG A 93 9663 24834 12665 1361 2804 5869 A C
ATOM 695 O ARG A 93 -38.735 23.240 5.573 1.00127.73 A O
ANISOU 695 O ARG A 93 9637 26096 12799 1583 2815 6100 A O
ATOM 696 CB ARG A 93 -36.177 24.878 5.020 1.00123.75 A C
ANISOU 696 CB ARG A 93 9869 24097 13054 2307 3134 6664 A C
ATOM 697 CG ARG A 93 -36.338 25.360 6.471 1.00131.50 A C
ANISOU 697 CG ARG A 93 11120 24370 14475 2390 3280 6648 A C
ATOM 698 CD ARG A 93 -37.447 26.374 6.666 1.00144.85 A C
ANISOU 698 CD ARG A 93 12469 26474 16094 2918 3458 7110 A C
ATOM 699 NE ARG A 93 -37.491 26.841 8.053 1.00152.12 A N
ANISOU 699 NE ARG A 93 13685 26654 17460 2985 3613 7074 A N
ATOM 700 CZ ARG A 93 -37.590 28.116 8.419 1.00169.14 A C
ANISOU 700 CZ ARG A 93 15900 28462 19904 3537 3909 7505 A C
ATOM 701 NH1 ARG A 93 -37.666 29.074 7.504 1.00162.58 A N1+
ANISOU 701 NH1 ARG A 93 14865 27938 18968 4105 4100 8043 A N1+
ATOM 702 NH2 ARG A 93 -37.616 28.442 9.705 1.00153.51 A N
ANISOU 702 NH2 ARG A 93 14193 25822 18314 3532 4037 7405 A N
ATOM 703 N GLY A 94 -37.244 22.191 6.880 1.00114.80 A N
ANISOU 703 N GLY A 94 8881 22978 11759 914 2757 5425 A N
ATOM 704 CA GLY A 94 -35.927 21.722 7.288 1.00108.63 A C
ANISOU 704 CA GLY A 94 8661 21273 11341 644 2737 5122 A C
ATOM 705 C GLY A 94 -35.661 20.307 6.833 1.00109.74 A C
ANISOU 705 C GLY A 94 8876 21589 11232 31 2554 4621 A C
ATOM 706 O GLY A 94 -35.661 19.377 7.646 1.00106.48 A O
ANISOU 706 O GLY A 94 8726 20822 10909 -421 2502 4196 A O
ATOM 707 N GLN A 95 -35.472 20.148 5.509 1.00107.90 A N
ANISOU 707 N GLN A 95 8406 21926 10665 29 2477 4681 A N
ATOM 708 CA GLN A 95 -35.183 18.893 4.817 1.00107.39 A C
ANISOU 708 CA GLN A 95 8371 22113 10321 -512 2330 4242 A C
ATOM 709 C GLN A 95 -33.702 18.547 4.945 1.00106.03 A C
ANISOU 709 C GLN A 95 8745 21049 10493 -646 2331 4045 A C
ATOM 710 O GLN A 95 -32.841 19.435 4.934 1.00103.29 A O
ANISOU 710 O GLN A 95 8589 20204 10453 -246 2425 4345 A O
ATOM 711 CB GLN A 95 -35.581 18.975 3.330 1.00113.09 A C
ANISOU 711 CB GLN A 95 8588 23846 10535 -405 2258 4421 A C
ATOM 712 CG GLN A 95 -35.914 17.621 2.704 1.00128.62 A C
ANISOU 712 CG GLN A 95 10412 26376 12080 -1034 2117 3919 A C
ATOM 713 CD GLN A 95 -36.429 17.727 1.291 1.00152.51 A C
ANISOU 713 CD GLN A 95 12880 30507 14561 -929 2042 4082 A C
ATOM 714 NE2 GLN A 95 -37.583 17.132 1.039 1.00149.43 A N
ANISOU 714 NE2 GLN A 95 12046 31020 13711 -1265 1964 3841 A N
ATOM 715 OE1 GLN A 95 -35.782 18.288 0.402 1.00147.83 A O
ANISOU 715 OE1 GLN A 95 12245 29988 13935 -577 2056 4395 A O
ATOM 716 N GLU A 96 -33.418 17.247 5.062 1.00100.70 A N
ANISOU 716 N GLU A 96 8316 20188 9756 -1212 2249 3534 A N
ATOM 717 CA GLU A 96 -32.066 16.727 5.196 1.00 96.05 A C
ANISOU 717 CA GLU A 96 8233 18818 9443 -1380 2241 3297 A C
ATOM 718 C GLU A 96 -31.646 15.987 3.928 1.00101.12 A C
ANISOU 718 C GLU A 96 8798 19858 9766 -1644 2156 3104 A C
ATOM 719 O GLU A 96 -32.470 15.323 3.293 1.00103.69 A O
ANISOU 719 O GLU A 96 8792 20946 9659 -1964 2091 2907 A O
ATOM 720 CB GLU A 96 -31.944 15.825 6.433 1.00 94.19 A C
ANISOU 720 CB GLU A 96 8418 17945 9427 -1765 2253 2887 A C
ATOM 721 CG GLU A 96 -31.867 16.607 7.736 1.00 95.20 A C
ANISOU 721 CG GLU A 96 8762 17437 9974 -1467 2345 3065 A C
ATOM 722 CD GLU A 96 -31.447 15.850 8.982 1.00 97.61 A C
ANISOU 722 CD GLU A 96 9543 17003 10543 -1750 2365 2716 A C
ATOM 723 OE1 GLU A 96 -31.268 14.614 8.903 1.00 60.70 A O
ANISOU 723 OE1 GLU A 96 5064 12267 5730 -2202 2328 2320 A O
ATOM 724 OE2 GLU A 96 -31.315 16.492 10.049 1.00 92.05 A O1-
ANISOU 724 OE2 GLU A 96 9016 15788 10172 -1512 2437 2841 A O1-
ATOM 725 N VAL A 97 -30.361 16.139 3.550 1.00 94.88 A N
ANISOU 725 N VAL A 97 8294 18572 9185 -1510 2166 3153 A N
ATOM 726 CA VAL A 97 -29.758 15.519 2.369 1.00 95.27 A C
ANISOU 726 CA VAL A 97 8328 18878 8990 -1714 2101 2990 A C
ATOM 727 C VAL A 97 -28.336 15.048 2.727 1.00 94.44 A C
ANISOU 727 C VAL A 97 8773 17881 9231 -1824 2117 2763 A C
ATOM 728 O VAL A 97 -27.760 15.545 3.698 1.00 91.28 A O
ANISOU 728 O VAL A 97 8679 16757 9246 -1610 2180 2855 A O
ATOM 729 CB VAL A 97 -29.794 16.486 1.147 1.00101.95 A C
ANISOU 729 CB VAL A 97 8781 20336 9621 -1290 2102 3436 A C
ATOM 730 CG1 VAL A 97 -28.738 17.594 1.241 1.00 99.32 A C
ANISOU 730 CG1 VAL A 97 8673 19373 9692 -794 2207 3813 A C
ATOM 731 CG2 VAL A 97 -29.689 15.724 -0.170 1.00104.22 A C
ANISOU 731 CG2 VAL A 97 8884 21232 9485 -1579 2013 3228 A C
ATOM 732 N ILE A 98 -27.784 14.085 1.966 1.00 90.13 A N
ANISOU 732 N ILE A 98 8340 17405 8499 -2161 2069 2452 A N
ATOM 733 CA ILE A 98 -26.423 13.591 2.210 1.00 86.06 A C
ANISOU 733 CA ILE A 98 8318 16116 8266 -2251 2086 2238 A C
ATOM 734 C ILE A 98 -25.483 14.108 1.112 1.00 86.84 A C
ANISOU 734 C ILE A 98 8371 16263 8362 -1989 2078 2457 A C
ATOM 735 O ILE A 98 -25.713 13.858 -0.073 1.00 88.44 A O
ANISOU 735 O ILE A 98 8287 17120 8196 -2086 2031 2454 A O
ATOM 736 CB ILE A 98 -26.342 12.043 2.345 1.00 89.36 A C
ANISOU 736 CB ILE A 98 9002 16406 8543 -2818 2084 1701 A C
ATOM 737 CG1 ILE A 98 -27.477 11.452 3.231 1.00 90.85 A C
ANISOU 737 CG1 ILE A 98 9173 16693 8651 -3132 2117 1473 A C
ATOM 738 CG2 ILE A 98 -24.928 11.575 2.777 1.00 86.22 A C
ANISOU 738 CG2 ILE A 98 9134 15168 8456 -2844 2116 1510 A C
ATOM 739 CD1 ILE A 98 -27.536 11.896 4.712 1.00 94.75 A C
ANISOU 739 CD1 ILE A 98 9908 16569 9525 -2939 2164 1572 A C
ATOM 740 N VAL A 99 -24.428 14.825 1.530 1.00 79.05 A N
ANISOU 740 N VAL A 99 7658 14599 7778 -1672 2133 2632 A N
ATOM 741 CA VAL A 99 -23.410 15.396 0.648 1.00 78.02 A C
ANISOU 741 CA VAL A 99 7541 14381 7721 -1408 2158 2843 A C
ATOM 742 C VAL A 99 -22.088 14.657 0.890 1.00 77.56 A C
ANISOU 742 C VAL A 99 7932 13665 7873 -1589 2151 2524 A C
ATOM 743 O VAL A 99 -21.506 14.755 1.972 1.00 73.03 A O
ANISOU 743 O VAL A 99 7680 12413 7654 -1526 2187 2447 A O
ATOM 744 CB VAL A 99 -23.266 16.935 0.830 1.00 81.23 A C
ANISOU 744 CB VAL A 99 7861 14589 8413 -878 2270 3325 A C
ATOM 745 CG1 VAL A 99 -22.255 17.518 -0.158 1.00 80.88 A C
ANISOU 745 CG1 VAL A 99 7826 14476 8430 -626 2328 3544 A C
ATOM 746 CG2 VAL A 99 -24.621 17.640 0.705 1.00 84.04 A C
ANISOU 746 CG2 VAL A 99 7790 15580 8563 -659 2298 3657 A C
ATOM 747 N GLU A 100 -21.648 13.893 -0.113 1.00 75.53 A N
ANISOU 747 N GLU A 100 7678 13647 7371 -1811 2107 2330 A N
ATOM 748 CA GLU A 100 -20.395 13.132 -0.082 1.00 73.28 A C
ANISOU 748 CA GLU A 100 7786 12831 7227 -1968 2108 2036 A C
ATOM 749 C GLU A 100 -19.275 13.979 -0.712 1.00 71.40 A C
ANISOU 749 C GLU A 100 7563 12406 7160 -1635 2145 2288 A C
ATOM 750 O GLU A 100 -19.453 14.467 -1.827 1.00 72.88 A O
ANISOU 750 O GLU A 100 7450 13118 7124 -1503 2144 2521 A O
ATOM 751 CB GLU A 100 -20.581 11.810 -0.834 1.00 77.31 A C
ANISOU 751 CB GLU A 100 8299 13704 7371 -2418 2071 1660 A C
ATOM 752 CG GLU A 100 -19.809 10.636 -0.259 1.00 92.50 A C
ANISOU 752 CG GLU A 100 10688 15040 9417 -2709 2104 1242 A C
ATOM 753 CD GLU A 100 -19.812 9.457 -1.212 1.00127.43 A C
ANISOU 753 CD GLU A 100 15135 19782 13500 -3123 2115 888 A C
ATOM 754 OE1 GLU A 100 -19.002 9.461 -2.168 1.00123.22 A O
ANISOU 754 OE1 GLU A 100 14626 19282 12910 -3078 2109 882 A O
ATOM 755 OE2 GLU A 100 -20.649 8.542 -1.026 1.00129.55 A O1-
ANISOU 755 OE2 GLU A 100 15397 20269 13556 -3509 2149 603 A O1-
ATOM 756 N ILE A 101 -18.156 14.204 0.008 1.00 61.97 A N
ANISOU 756 N ILE A 101 6694 10500 6350 -1488 2188 2254 A N
ATOM 757 CA ILE A 101 -17.043 15.005 -0.520 1.00 60.12 A C
ANISOU 757 CA ILE A 101 6488 10048 6305 -1203 2247 2459 A C
ATOM 758 C ILE A 101 -15.720 14.246 -0.379 1.00 61.03 A C
ANISOU 758 C ILE A 101 6965 9657 6565 -1328 2234 2148 A C
ATOM 759 O ILE A 101 -15.376 13.789 0.712 1.00 58.43 A O
ANISOU 759 O ILE A 101 6927 8832 6443 -1398 2228 1930 A O
ATOM 760 CB ILE A 101 -16.927 16.439 0.098 1.00 61.52 A C
ANISOU 760 CB ILE A 101 6624 9919 6832 -810 2361 2809 A C
ATOM 761 CG1 ILE A 101 -18.248 17.223 0.002 1.00 63.42 A C
ANISOU 761 CG1 ILE A 101 6515 10646 6936 -631 2399 3149 A C
ATOM 762 CG2 ILE A 101 -15.773 17.237 -0.572 1.00 60.44 A C
ANISOU 762 CG2 ILE A 101 6511 9581 6872 -558 2460 2999 A C
ATOM 763 CD1 ILE A 101 -18.316 18.432 0.888 1.00 66.96 A C
ANISOU 763 CD1 ILE A 101 6979 10726 7736 -309 2533 3417 A C
ATOM 764 N ASP A 102 -14.965 14.157 -1.486 1.00 56.71 A N
ANISOU 764 N ASP A 102 6388 9255 5902 -1322 2237 2150 A N
ATOM 765 CA ASP A 102 -13.646 13.535 -1.508 1.00 54.26 A C
ANISOU 765 CA ASP A 102 6380 8521 5713 -1391 2236 1896 A C
ATOM 766 C ASP A 102 -12.591 14.640 -1.545 1.00 52.37 A C
ANISOU 766 C ASP A 102 6156 7960 5783 -1067 2320 2120 A C
ATOM 767 O ASP A 102 -12.517 15.395 -2.516 1.00 52.47 A O
ANISOU 767 O ASP A 102 5948 8263 5727 -895 2377 2397 A O
ATOM 768 CB ASP A 102 -13.500 12.565 -2.696 1.00 58.74 A C
ANISOU 768 CB ASP A 102 6926 9454 5941 -1643 2198 1696 A C
ATOM 769 CG ASP A 102 -14.347 11.312 -2.588 1.00 81.37 A C
ANISOU 769 CG ASP A 102 9857 12526 8534 -2032 2157 1372 A C
ATOM 770 OD1 ASP A 102 -14.269 10.626 -1.540 1.00 82.58 A O
ANISOU 770 OD1 ASP A 102 10308 12243 8826 -2156 2167 1131 A O
ATOM 771 OD2 ASP A 102 -15.054 10.988 -3.567 1.00 93.82 A O1-
ANISOU 771 OD2 ASP A 102 11192 14705 9748 -2222 2133 1343 A O1-
ATOM 772 N SER A 103 -11.822 14.764 -0.457 1.00 43.42 A N
ANISOU 772 N SER A 103 5271 6247 4981 -983 2344 2002 A N
ATOM 773 CA SER A 103 -10.779 15.772 -0.304 1.00 40.08 A C
ANISOU 773 CA SER A 103 4879 5470 4878 -726 2444 2139 A C
ATOM 774 C SER A 103 -9.433 15.154 0.085 1.00 40.39 A C
ANISOU 774 C SER A 103 5203 5074 5070 -770 2421 1835 A C
ATOM 775 O SER A 103 -9.338 13.944 0.285 1.00 38.79 A O
ANISOU 775 O SER A 103 5198 4810 4731 -968 2339 1545 A O
ATOM 776 CB SER A 103 -11.200 16.807 0.735 1.00 41.08 A C
ANISOU 776 CB SER A 103 4961 5364 5282 -534 2526 2326 A C
ATOM 777 OG SER A 103 -11.142 16.315 2.065 1.00 45.18 A O
ANISOU 777 OG SER A 103 5705 5512 5951 -614 2473 2080 A O
ATOM 778 N VAL A 104 -8.385 15.994 0.141 1.00 36.51 A N
ANISOU 778 N VAL A 104 4725 4299 4848 -579 2515 1907 A N
ATOM 779 CA VAL A 104 -7.032 15.643 0.576 1.00 34.19 A C
ANISOU 779 CA VAL A 104 4644 3622 4723 -565 2506 1648 A C
ATOM 780 C VAL A 104 -6.394 16.918 1.152 1.00 37.77 A C
ANISOU 780 C VAL A 104 5054 3764 5535 -361 2639 1758 A C
ATOM 781 O VAL A 104 -6.553 18.007 0.589 1.00 38.38 A O
ANISOU 781 O VAL A 104 4948 3937 5696 -226 2777 2046 A O
ATOM 782 CB VAL A 104 -6.139 14.923 -0.496 1.00 38.33 A C
ANISOU 782 CB VAL A 104 5225 4261 5079 -644 2479 1510 A C
ATOM 783 CG1 VAL A 104 -5.822 15.801 -1.705 1.00 39.39 A C
ANISOU 783 CG1 VAL A 104 5150 4616 5202 -530 2584 1768 A C
ATOM 784 CG2 VAL A 104 -4.859 14.371 0.124 1.00 36.33 A C
ANISOU 784 CG2 VAL A 104 5200 3639 4965 -621 2454 1217 A C
ATOM 785 N THR A 105 -5.715 16.775 2.299 1.00 34.36 A N
ANISOU 785 N THR A 105 4787 2969 5298 -340 2617 1524 A N
ATOM 786 CA THR A 105 -5.015 17.858 2.999 1.00 34.43 A C
ANISOU 786 CA THR A 105 4769 2670 5641 -201 2744 1528 A C
ATOM 787 C THR A 105 -3.709 18.198 2.287 1.00 40.13 A C
ANISOU 787 C THR A 105 5460 3331 6457 -151 2830 1479 A C
ATOM 788 O THR A 105 -3.251 17.464 1.410 1.00 42.09 A O
ANISOU 788 O THR A 105 5743 3733 6515 -214 2764 1402 A O
ATOM 789 CB THR A 105 -4.723 17.472 4.484 1.00 41.08 A C
ANISOU 789 CB THR A 105 5780 3223 6604 -205 2669 1258 A C
ATOM 790 CG2 THR A 105 -5.957 17.108 5.262 1.00 35.12 A C
ANISOU 790 CG2 THR A 105 5075 2500 5770 -260 2596 1288 A C
ATOM 791 OG1 THR A 105 -3.773 16.402 4.549 1.00 40.34 A O
ANISOU 791 OG1 THR A 105 5856 3068 6403 -247 2560 978 A O
ATOM 792 N SER A 106 -3.110 19.315 2.679 1.00 35.42 A N
ANISOU 792 N SER A 106 4798 2503 6158 -55 2998 1505 A N
ATOM 793 CA SER A 106 -1.801 19.727 2.227 1.00 35.50 A C
ANISOU 793 CA SER A 106 4774 2411 6303 -27 3108 1414 A C
ATOM 794 C SER A 106 -0.809 19.295 3.310 1.00 39.15 A C
ANISOU 794 C SER A 106 5347 2657 6871 -43 3027 1046 A C
ATOM 795 O SER A 106 -1.216 19.273 4.474 1.00 37.64 A O
ANISOU 795 O SER A 106 5213 2332 6757 -36 2982 954 A O
ATOM 796 CB SER A 106 -1.770 21.237 1.984 1.00 40.58 A C
ANISOU 796 CB SER A 106 5280 2935 7205 66 3385 1654 A C
ATOM 797 OG SER A 106 -0.470 21.697 1.660 1.00 55.09 A O
ANISOU 797 OG SER A 106 7086 4643 9204 64 3524 1532 A O
ATOM 798 N PRO A 107 0.474 18.940 3.006 1.00 37.71 A N
ANISOU 798 N PRO A 107 5184 2463 6680 -47 3008 832 A N
ATOM 799 CA PRO A 107 1.403 18.566 4.097 1.00 37.53 A C
ANISOU 799 CA PRO A 107 5231 2296 6731 -24 2930 492 A C
ATOM 800 C PRO A 107 1.667 19.722 5.084 1.00 43.17 A C
ANISOU 800 C PRO A 107 5849 2803 7748 -9 3083 410 A C
ATOM 801 O PRO A 107 2.163 19.493 6.186 1.00 42.47 A O
ANISOU 801 O PRO A 107 5797 2637 7703 14 3010 145 A O
ATOM 802 CB PRO A 107 2.694 18.186 3.354 1.00 39.77 A C
ANISOU 802 CB PRO A 107 5499 2659 6953 -16 2924 334 A C
ATOM 803 CG PRO A 107 2.301 18.006 1.926 1.00 44.45 A C
ANISOU 803 CG PRO A 107 6070 3442 7378 -55 2944 566 A C
ATOM 804 CD PRO A 107 1.151 18.913 1.691 1.00 39.98 A C
ANISOU 804 CD PRO A 107 5412 2895 6883 -57 3062 890 A C
ATOM 805 N LYS A 108 1.322 20.954 4.678 1.00 42.05 A N
ANISOU 805 N LYS A 108 5591 2583 7802 -14 3313 640 A N
ATOM 806 CA LYS A 108 1.492 22.188 5.449 1.00 43.35 A C
ANISOU 806 CA LYS A 108 5673 2521 8278 -26 3531 587 A C
ATOM 807 C LYS A 108 0.259 22.497 6.325 1.00 47.80 A C
ANISOU 807 C LYS A 108 6272 2989 8901 0 3537 717 A C
ATOM 808 O LYS A 108 0.269 23.502 7.032 1.00 49.12 A O
ANISOU 808 O LYS A 108 6386 2952 9326 -11 3737 686 A O
ATOM 809 CB LYS A 108 1.776 23.371 4.503 1.00 46.63 A C
ANISOU 809 CB LYS A 108 5977 2855 8886 -31 3838 788 A C
ATOM 810 CG LYS A 108 3.011 23.195 3.618 1.00 62.94 A C
ANISOU 810 CG LYS A 108 7991 5004 10918 -68 3870 662 A C
ATOM 811 CD LYS A 108 4.273 23.818 4.178 1.00 68.06 A C
ANISOU 811 CD LYS A 108 8550 5507 11802 -151 4027 331 A C
ATOM 812 CE LYS A 108 5.435 23.452 3.294 1.00 65.85 A C
ANISOU 812 CE LYS A 108 8218 5365 11435 -179 4007 198 A C
ATOM 813 NZ LYS A 108 6.733 23.895 3.864 1.00 71.90 A N1+
ANISOU 813 NZ LYS A 108 8866 6064 12388 -277 4135 -171 A N1+
ATOM 814 N SER A 109 -0.808 21.654 6.255 1.00 43.34 A N
ANISOU 814 N SER A 109 5794 2571 8102 20 3341 850 A N
ATOM 815 CA SER A 109 -2.073 21.794 7.005 1.00 42.06 A C
ANISOU 815 CA SER A 109 5663 2368 7950 42 3320 981 A C
ATOM 816 C SER A 109 -1.833 22.403 8.411 1.00 46.64 A C
ANISOU 816 C SER A 109 6244 2718 8761 35 3396 759 A C
ATOM 817 O SER A 109 -1.096 21.825 9.216 1.00 45.56 A O
ANISOU 817 O SER A 109 6162 2565 8583 17 3261 446 A O
ATOM 818 CB SER A 109 -2.785 20.443 7.123 1.00 42.01 A C
ANISOU 818 CB SER A 109 5782 2536 7645 13 3060 962 A C
ATOM 819 OG SER A 109 -3.900 20.468 8.003 1.00 40.96 A O
ANISOU 819 OG SER A 109 5684 2365 7514 18 3024 1029 A O
ATOM 820 N SER A 110 -2.431 23.583 8.677 1.00 43.03 A N
ANISOU 820 N SER A 110 5719 2097 8533 63 3629 925 A N
ATOM 821 CA SER A 110 -2.304 24.289 9.948 1.00 43.06 A C
ANISOU 821 CA SER A 110 5712 1879 8769 37 3748 725 A C
ATOM 822 C SER A 110 -2.794 23.446 11.161 1.00 45.00 A C
ANISOU 822 C SER A 110 6056 2162 8880 37 3514 559 A C
ATOM 823 O SER A 110 -2.257 23.586 12.261 1.00 45.57 A O
ANISOU 823 O SER A 110 6127 2135 9054 6 3517 269 A O
ATOM 824 CB SER A 110 -3.043 25.623 9.896 1.00 47.55 A C
ANISOU 824 CB SER A 110 6221 2260 9584 86 4062 988 A C
ATOM 825 OG SER A 110 -4.415 25.490 9.550 1.00 49.80 A O
ANISOU 825 OG SER A 110 6514 2670 9737 181 4017 1340 A O
ATOM 826 N ALA A 111 -3.748 22.532 10.952 1.00 39.51 A N
ANISOU 826 N ALA A 111 5442 1631 7937 61 3319 721 A N
ATOM 827 CA ALA A 111 -4.272 21.677 12.019 1.00 36.41 A C
ANISOU 827 CA ALA A 111 5168 1265 7401 58 3122 594 A C
ATOM 828 C ALA A 111 -3.327 20.546 12.434 1.00 35.89 A C
ANISOU 828 C ALA A 111 5212 1262 7162 59 2918 295 A C
ATOM 829 O ALA A 111 -3.431 20.050 13.560 1.00 32.81 A O
ANISOU 829 O ALA A 111 4825 1019 6623 80 2809 121 A O
ATOM 830 CB ALA A 111 -5.587 21.062 11.574 1.00 36.57 A C
ANISOU 830 CB ALA A 111 5233 1447 7216 52 3020 854 A C
ATOM 831 N LEU A 112 -2.455 20.095 11.533 1.00 33.40 A N
ANISOU 831 N LEU A 112 4891 1050 6748 56 2873 246 A N
ATOM 832 CA LEU A 112 -1.655 18.907 11.835 1.00 33.36 A C
ANISOU 832 CA LEU A 112 5011 1114 6549 96 2689 8 A C
ATOM 833 C LEU A 112 -0.162 19.176 11.985 1.00 37.30 A C
ANISOU 833 C LEU A 112 5417 1619 7137 128 2724 -260 A C
ATOM 834 O LEU A 112 0.339 20.166 11.488 1.00 36.53 A O
ANISOU 834 O LEU A 112 5169 1475 7237 80 2899 -250 A O
ATOM 835 CB LEU A 112 -1.867 17.836 10.737 1.00 32.89 A C
ANISOU 835 CB LEU A 112 5058 1198 6242 71 2580 128 A C
ATOM 836 CG LEU A 112 -3.295 17.566 10.244 1.00 35.24 A C
ANISOU 836 CG LEU A 112 5395 1578 6416 -2 2559 391 A C
ATOM 837 CD1 LEU A 112 -3.281 16.879 8.891 1.00 34.98 A C
ANISOU 837 CD1 LEU A 112 5382 1722 6189 -60 2519 495 A C
ATOM 838 CD2 LEU A 112 -4.095 16.800 11.242 1.00 35.76 A C
ANISOU 838 CD2 LEU A 112 5623 1610 6355 -10 2449 336 A C
ATOM 839 N GLN A 113 0.538 18.260 12.671 1.00 34.79 A N
ANISOU 839 N GLN A 113 5189 1371 6659 218 2572 -498 A N
ATOM 840 CA GLN A 113 1.982 18.297 12.862 1.00 36.13 A C
ANISOU 840 CA GLN A 113 5257 1628 6842 276 2566 -778 A C
ATOM 841 C GLN A 113 2.519 16.895 12.559 1.00 37.15 A C
ANISOU 841 C GLN A 113 5541 1878 6696 395 2400 -841 A C
ATOM 842 O GLN A 113 2.128 15.948 13.233 1.00 33.93 A O
ANISOU 842 O GLN A 113 5317 1468 6108 491 2279 -859 A O
ATOM 843 CB GLN A 113 2.352 18.795 14.287 1.00 39.30 A C
ANISOU 843 CB GLN A 113 5567 2030 7335 309 2578 -1036 A C
ATOM 844 CG GLN A 113 3.755 18.416 14.788 1.00 55.80 A C
ANISOU 844 CG GLN A 113 7568 4312 9323 419 2498 -1363 A C
ATOM 845 CD GLN A 113 4.819 19.413 14.477 1.00 74.14 A C
ANISOU 845 CD GLN A 113 9646 6689 11837 316 2655 -1550 A C
ATOM 846 NE2 GLN A 113 5.569 19.793 15.482 1.00 58.59 A N
ANISOU 846 NE2 GLN A 113 7510 4842 9909 318 2675 -1866 A N
ATOM 847 OE1 GLN A 113 5.049 19.778 13.328 1.00 81.18 A O
ANISOU 847 OE1 GLN A 113 10490 7542 12815 234 2760 -1434 A O
ATOM 848 N TRP A 114 3.369 16.764 11.494 1.00 33.86 A N
ANISOU 848 N TRP A 114 5068 1548 6250 390 2424 -857 A N
ATOM 849 CA TRP A 114 4.006 15.504 11.096 1.00 32.88 A C
ANISOU 849 CA TRP A 114 5084 1527 5882 511 2305 -925 A C
ATOM 850 C TRP A 114 5.426 15.443 11.663 1.00 40.99 A C
ANISOU 850 C TRP A 114 5991 2704 6880 652 2271 -1218 A C
ATOM 851 O TRP A 114 6.215 16.351 11.425 1.00 42.34 A O
ANISOU 851 O TRP A 114 5935 2938 7214 583 2373 -1339 A O
ATOM 852 CB TRP A 114 4.026 15.343 9.559 1.00 30.64 A C
ANISOU 852 CB TRP A 114 4765 1360 5516 383 2337 -722 A C
ATOM 853 CG TRP A 114 2.654 15.338 8.946 1.00 29.70 A C
ANISOU 853 CG TRP A 114 4728 1181 5375 268 2367 -459 A C
ATOM 854 CD1 TRP A 114 1.929 16.426 8.540 1.00 32.09 A C
ANISOU 854 CD1 TRP A 114 4938 1359 5897 182 2496 -286 A C
ATOM 855 CD2 TRP A 114 1.825 14.187 8.714 1.00 28.45 A C
ANISOU 855 CD2 TRP A 114 4754 1101 4953 229 2279 -344 A C
ATOM 856 CE2 TRP A 114 0.606 14.652 8.173 1.00 30.90 A C
ANISOU 856 CE2 TRP A 114 5100 1261 5381 132 2339 -146 A C
ATOM 857 CE3 TRP A 114 1.999 12.800 8.907 1.00 29.22 A C
ANISOU 857 CE3 TRP A 114 5101 1173 4827 315 2187 -440 A C
ATOM 858 NE1 TRP A 114 0.708 16.020 8.047 1.00 30.93 A N
ANISOU 858 NE1 TRP A 114 4886 1239 5626 105 2465 -65 A N
ATOM 859 CZ2 TRP A 114 -0.415 13.779 7.780 1.00 29.55 A C
ANISOU 859 CZ2 TRP A 114 5082 1135 5010 38 2288 -33 A C
ATOM 860 CZ3 TRP A 114 0.961 11.939 8.577 1.00 29.79 A C
ANISOU 860 CZ3 TRP A 114 5407 1145 4767 241 2173 -362 A C
ATOM 861 CH2 TRP A 114 -0.218 12.422 8.000 1.00 29.99 A C
ANISOU 861 CH2 TRP A 114 5383 1159 4855 78 2213 -170 A C
ATOM 862 N LEU A 115 5.729 14.402 12.455 1.00 39.32 A N
ANISOU 862 N LEU A 115 5924 2563 6454 856 2145 -1334 A N
ATOM 863 CA LEU A 115 7.050 14.216 13.057 1.00 40.40 A C
ANISOU 863 CA LEU A 115 5935 2914 6501 1043 2092 -1603 A C
ATOM 864 C LEU A 115 7.675 12.938 12.571 1.00 46.24 A C
ANISOU 864 C LEU A 115 6844 3734 6993 1243 2020 -1609 A C
ATOM 865 O LEU A 115 7.038 11.881 12.624 1.00 44.33 A O
ANISOU 865 O LEU A 115 6892 3372 6578 1329 1975 -1479 A O
ATOM 866 CB LEU A 115 7.001 14.181 14.599 1.00 40.87 A C
ANISOU 866 CB LEU A 115 5985 3045 6500 1179 2022 -1745 A C
ATOM 867 CG LEU A 115 6.328 15.325 15.321 1.00 46.05 A C
ANISOU 867 CG LEU A 115 6516 3603 7378 1005 2097 -1756 A C
ATOM 868 CD1 LEU A 115 4.948 14.918 15.806 1.00 44.71 A C
ANISOU 868 CD1 LEU A 115 6586 3248 7152 1005 2056 -1560 A C
ATOM 869 CD2 LEU A 115 7.151 15.743 16.505 1.00 53.35 A C
ANISOU 869 CD2 LEU A 115 7208 4750 8313 1073 2085 -2064 A C
ATOM 870 N ASN A 116 8.946 13.027 12.127 1.00 45.36 A N
ANISOU 870 N ASN A 116 6553 3820 6862 1315 2031 -1774 A N
ATOM 871 CA ASN A 116 9.729 11.867 11.723 1.00 46.41 A C
ANISOU 871 CA ASN A 116 6816 4057 6761 1545 1980 -1808 A C
ATOM 872 C ASN A 116 10.144 11.151 12.995 1.00 55.46 A C
ANISOU 872 C ASN A 116 8030 5349 7694 1865 1886 -1930 A C
ATOM 873 O ASN A 116 10.104 11.759 14.062 1.00 56.08 A O
ANISOU 873 O ASN A 116 7959 5523 7826 1874 1856 -2048 A O
ATOM 874 CB ASN A 116 10.957 12.293 10.895 1.00 43.90 A C
ANISOU 874 CB ASN A 116 6248 3934 6497 1521 2029 -1952 A C
ATOM 875 CG ASN A 116 10.635 13.132 9.685 1.00 64.21 A C
ANISOU 875 CG ASN A 116 8728 6388 9281 1228 2145 -1828 A C
ATOM 876 ND2 ASN A 116 11.224 14.312 9.606 1.00 50.19 A N
ANISOU 876 ND2 ASN A 116 6654 4708 7709 1082 2241 -1968 A N
ATOM 877 OD1 ASN A 116 9.865 12.736 8.805 1.00 67.22 A O
ANISOU 877 OD1 ASN A 116 9300 6606 9634 1129 2167 -1612 A O
ATOM 878 N LYS A 117 10.541 9.879 12.898 1.00 56.48 A N
ANISOU 878 N LYS A 117 8385 5499 7575 2138 1856 -1898 A N
ATOM 879 CA LYS A 117 10.994 9.077 14.035 1.00 58.87 A C
ANISOU 879 CA LYS A 117 8783 5952 7634 2514 1790 -1969 A C
ATOM 880 C LYS A 117 12.150 9.781 14.758 1.00 68.81 A C
ANISOU 880 C LYS A 117 9652 7614 8878 2643 1730 -2240 A C
ATOM 881 O LYS A 117 12.191 9.765 15.986 1.00 70.60 A O
ANISOU 881 O LYS A 117 9835 7997 8994 2825 1666 -2321 A O
ATOM 882 CB LYS A 117 11.383 7.667 13.587 1.00 61.78 A C
ANISOU 882 CB LYS A 117 9449 6266 7760 2794 1822 -1885 A C
ATOM 883 CG LYS A 117 12.410 7.602 12.454 1.00 68.11 A C
ANISOU 883 CG LYS A 117 10122 7198 8558 2800 1856 -1958 A C
ATOM 884 CD LYS A 117 12.401 6.267 11.748 1.00 66.12 A C
ANISOU 884 CD LYS A 117 10234 6767 8122 2968 1934 -1835 A C
ATOM 885 CE LYS A 117 13.164 6.341 10.450 1.00 66.61 A C
ANISOU 885 CE LYS A 117 10176 6918 8217 2896 1978 -1889 A C
ATOM 886 NZ LYS A 117 13.460 4.990 9.921 1.00 69.79 A N1+
ANISOU 886 NZ LYS A 117 10919 7182 8415 3112 2070 -1812 A N1+
ATOM 887 N GLU A 118 13.019 10.483 13.995 1.00 67.88 A N
ANISOU 887 N GLU A 118 9236 7676 8880 2509 1763 -2392 A N
ATOM 888 CA GLU A 118 14.156 11.267 14.494 1.00 70.37 A C
ANISOU 888 CA GLU A 118 9132 8399 9205 2545 1736 -2697 A C
ATOM 889 C GLU A 118 13.686 12.360 15.477 1.00 73.73 A C
ANISOU 889 C GLU A 118 9364 8854 9795 2344 1739 -2825 A C
ATOM 890 O GLU A 118 14.379 12.641 16.458 1.00 75.12 A O
ANISOU 890 O GLU A 118 9283 9391 9866 2475 1683 -3073 A O
ATOM 891 CB GLU A 118 14.943 11.904 13.329 1.00 72.38 A C
ANISOU 891 CB GLU A 118 9144 8744 9615 2340 1819 -2807 A C
ATOM 892 CG GLU A 118 15.564 10.910 12.359 1.00 86.32 A C
ANISOU 892 CG GLU A 118 11055 10522 11220 2530 1824 -2721 A C
ATOM 893 CD GLU A 118 14.719 10.538 11.153 1.00114.03 A C
ANISOU 893 CD GLU A 118 14855 13648 14824 2337 1897 -2458 A C
ATOM 894 OE1 GLU A 118 14.166 11.454 10.501 1.00110.86 A O
ANISOU 894 OE1 GLU A 118 14368 13081 14674 1990 1978 -2399 A O
ATOM 895 OE2 GLU A 118 14.673 9.333 10.814 1.00113.07 A O1-
ANISOU 895 OE2 GLU A 118 15036 13413 14514 2540 1892 -2321 A O1-
ATOM 896 N GLN A 119 12.502 12.948 15.216 1.00 67.95 A N
ANISOU 896 N GLN A 119 8750 7764 9302 2038 1812 -2659 A N
ATOM 897 CA GLN A 119 11.892 13.971 16.064 1.00 67.27 A C
ANISOU 897 CA GLN A 119 8535 7626 9397 1835 1848 -2740 A C
ATOM 898 C GLN A 119 11.286 13.354 17.339 1.00 71.70 A C
ANISOU 898 C GLN A 119 9277 8194 9773 2056 1747 -2688 A C
ATOM 899 O GLN A 119 11.431 13.941 18.407 1.00 72.96 A O
ANISOU 899 O GLN A 119 9238 8546 9937 2051 1727 -2888 A O
ATOM 900 CB GLN A 119 10.809 14.752 15.289 1.00 66.55 A C
ANISOU 900 CB GLN A 119 8528 7155 9602 1489 1973 -2534 A C
ATOM 901 CG GLN A 119 11.341 15.750 14.257 1.00 72.74 A C
ANISOU 901 CG GLN A 119 9092 7925 10621 1232 2121 -2597 A C
ATOM 902 CD GLN A 119 10.245 16.376 13.412 1.00 77.00 A C
ANISOU 902 CD GLN A 119 9746 8114 11397 969 2247 -2329 A C
ATOM 903 NE2 GLN A 119 9.540 17.362 13.979 1.00 66.91 A N
ANISOU 903 NE2 GLN A 119 8406 6691 10326 794 2342 -2328 A N
ATOM 904 OE1 GLN A 119 10.039 16.017 12.236 1.00 61.92 A O
ANISOU 904 OE1 GLN A 119 7963 6083 9480 928 2272 -2126 A O
ATOM 905 N THR A 120 10.626 12.169 17.231 1.00 67.34 A N
ANISOU 905 N THR A 120 9102 7434 9051 2239 1703 -2434 A N
ATOM 906 CA THR A 120 9.930 11.476 18.336 1.00 66.51 A C
ANISOU 906 CA THR A 120 9239 7264 8767 2447 1642 -2331 A C
ATOM 907 C THR A 120 10.893 10.893 19.401 1.00 73.88 A C
ANISOU 907 C THR A 120 10078 8594 9397 2854 1547 -2496 A C
ATOM 908 O THR A 120 12.111 10.896 19.212 1.00 75.34 A O
ANISOU 908 O THR A 120 10031 9115 9480 3002 1518 -2676 A O
ATOM 909 CB THR A 120 8.983 10.359 17.823 1.00 63.34 A C
ANISOU 909 CB THR A 120 9277 6514 8275 2494 1670 -2035 A C
ATOM 910 CG2 THR A 120 8.164 10.762 16.613 1.00 54.38 A C
ANISOU 910 CG2 THR A 120 8214 5075 7374 2132 1750 -1868 A C
ATOM 911 OG1 THR A 120 9.703 9.156 17.574 1.00 67.12 A O
ANISOU 911 OG1 THR A 120 9911 7076 8513 2804 1662 -2008 A O
ATOM 912 N ALA A 121 10.318 10.371 20.508 1.00 70.88 A N
ANISOU 912 N ALA A 121 9880 8195 8857 3049 1504 -2419 A N
ATOM 913 CA ALA A 121 11.047 9.784 21.632 1.00 73.29 A C
ANISOU 913 CA ALA A 121 10128 8881 8839 3477 1420 -2522 A C
ATOM 914 C ALA A 121 11.486 8.321 21.370 1.00 78.49 A C
ANISOU 914 C ALA A 121 11092 9525 9208 3898 1433 -2347 A C
ATOM 915 O ALA A 121 12.624 7.975 21.689 1.00 81.54 A O
ANISOU 915 O ALA A 121 11308 10320 9353 4250 1379 -2470 A O
ATOM 916 CB ALA A 121 10.205 9.868 22.899 1.00 73.91 A C
ANISOU 916 CB ALA A 121 10295 8924 8864 3514 1393 -2487 A C
ATOM 917 N GLY A 122 10.598 7.496 20.801 1.00 72.60 A N
ANISOU 917 N GLY A 122 10776 8325 8483 3855 1520 -2077 A N
ATOM 918 CA GLY A 122 10.856 6.086 20.491 1.00 72.78 A C
ANISOU 918 CA GLY A 122 11162 8223 8269 4204 1594 -1899 A C
ATOM 919 C GLY A 122 11.888 5.852 19.403 1.00 76.86 A C
ANISOU 919 C GLY A 122 11586 8857 8762 4278 1614 -1958 A C
ATOM 920 O GLY A 122 12.498 4.775 19.340 1.00 78.66 A O
ANISOU 920 O GLY A 122 12014 9130 8745 4674 1667 -1876 A O
ATOM 921 N LYS A 123 12.062 6.859 18.510 1.00 70.21 A N
ANISOU 921 N LYS A 123 10457 8041 8179 3899 1596 -2087 A N
ATOM 922 CA LYS A 123 13.030 6.934 17.404 1.00 69.15 A C
ANISOU 922 CA LYS A 123 10154 8040 8079 3875 1613 -2180 A C
ATOM 923 C LYS A 123 12.837 5.859 16.304 1.00 71.46 A C
ANISOU 923 C LYS A 123 10828 8005 8320 3914 1724 -1985 A C
ATOM 924 O LYS A 123 13.547 5.915 15.293 1.00 72.12 A O
ANISOU 924 O LYS A 123 10793 8164 8445 3862 1747 -2047 A O
ATOM 925 CB LYS A 123 14.493 6.895 17.926 1.00 73.65 A C
ANISOU 925 CB LYS A 123 10404 9157 8422 4252 1536 -2390 A C
ATOM 926 CG LYS A 123 14.826 7.867 19.069 1.00 74.91 A C
ANISOU 926 CG LYS A 123 10150 9730 8584 4223 1434 -2643 A C
ATOM 927 CD LYS A 123 14.984 9.317 18.613 1.00 79.57 A C
ANISOU 927 CD LYS A 123 10354 10394 9486 3756 1443 -2868 A C
ATOM 928 CE LYS A 123 15.276 10.247 19.765 1.00 86.93 A C
ANISOU 928 CE LYS A 123 10897 11711 10422 3692 1378 -3153 A C
ATOM 929 NZ LYS A 123 14.960 11.657 19.424 1.00 91.52 A N1+
ANISOU 929 NZ LYS A 123 11238 12168 11369 3175 1453 -3306 A N1+
ATOM 930 N ILE A 124 11.890 4.911 16.466 1.00 66.35 A N
ANISOU 930 N ILE A 124 10628 6995 7587 3978 1811 -1772 A N
ATOM 931 CA ILE A 124 11.628 3.856 15.466 1.00 65.62 A C
ANISOU 931 CA ILE A 124 10919 6573 7440 3977 1951 -1621 A C
ATOM 932 C ILE A 124 10.443 4.262 14.560 1.00 66.80 A C
ANISOU 932 C ILE A 124 11160 6392 7829 3464 1994 -1535 A C
ATOM 933 O ILE A 124 10.448 3.957 13.363 1.00 66.78 A O
ANISOU 933 O ILE A 124 11250 6259 7863 3312 2067 -1504 A O
ATOM 934 CB ILE A 124 11.372 2.465 16.134 1.00 70.62 A C
ANISOU 934 CB ILE A 124 12018 6999 7817 4358 2076 -1457 A C
ATOM 935 CG1 ILE A 124 12.529 2.061 17.089 1.00 74.45 A C
ANISOU 935 CG1 ILE A 124 12398 7865 8024 4932 2036 -1507 A C
ATOM 936 CG2 ILE A 124 11.130 1.356 15.082 1.00 71.43 A C
ANISOU 936 CG2 ILE A 124 12533 6738 7870 4326 2265 -1340 A C
ATOM 937 CD1 ILE A 124 12.207 0.914 18.121 1.00 81.60 A C
ANISOU 937 CD1 ILE A 124 13723 8610 8669 5360 2159 -1322 A C
ATOM 938 N HIS A 125 9.428 4.940 15.129 1.00 60.08 A N
ANISOU 938 N HIS A 125 10269 5436 7121 3214 1952 -1495 A N
ATOM 939 CA HIS A 125 8.228 5.275 14.377 1.00 56.70 A C
ANISOU 939 CA HIS A 125 9922 4742 6881 2777 1993 -1390 A C
ATOM 940 C HIS A 125 7.918 6.754 14.300 1.00 55.06 A C
ANISOU 940 C HIS A 125 9351 4636 6935 2457 1916 -1444 A C
ATOM 941 O HIS A 125 8.177 7.480 15.260 1.00 52.55 A O
ANISOU 941 O HIS A 125 8801 4503 6663 2528 1841 -1551 A O
ATOM 942 CB HIS A 125 7.019 4.568 14.999 1.00 57.27 A C
ANISOU 942 CB HIS A 125 10360 4519 6880 2744 2068 -1246 A C
ATOM 943 CG HIS A 125 7.066 3.082 14.825 1.00 62.24 A C
ANISOU 943 CG HIS A 125 11424 4932 7292 2961 2220 -1167 A C
ATOM 944 CD2 HIS A 125 6.820 2.335 13.727 1.00 64.14 A C
ANISOU 944 CD2 HIS A 125 11908 4963 7497 2820 2350 -1124 A C
ATOM 945 ND1 HIS A 125 7.418 2.246 15.866 1.00 65.75 A N
ANISOU 945 ND1 HIS A 125 12095 5363 7523 3374 2274 -1129 A N
ATOM 946 CE1 HIS A 125 7.352 1.023 15.378 1.00 66.80 A C
ANISOU 946 CE1 HIS A 125 12627 5237 7518 3471 2458 -1055 A C
ATOM 947 NE2 HIS A 125 7.010 1.028 14.090 1.00 66.23 A N
ANISOU 947 NE2 HIS A 125 12575 5044 7548 3131 2508 -1068 A N
ATOM 948 N PRO A 126 7.274 7.191 13.179 1.00 49.03 A N
ANISOU 948 N PRO A 126 8553 3743 6334 2103 1954 -1360 A N
ATOM 949 CA PRO A 126 6.811 8.594 13.090 1.00 46.08 A C
ANISOU 949 CA PRO A 126 7883 3410 6217 1815 1927 -1361 A C
ATOM 950 C PRO A 126 5.583 8.871 13.989 1.00 48.04 A C
ANISOU 950 C PRO A 126 8210 3515 6529 1701 1917 -1270 A C
ATOM 951 O PRO A 126 5.037 7.961 14.612 1.00 47.96 A O
ANISOU 951 O PRO A 126 8489 3366 6366 1814 1933 -1202 A O
ATOM 952 CB PRO A 126 6.456 8.745 11.609 1.00 46.74 A C
ANISOU 952 CB PRO A 126 7955 3417 6388 1545 1986 -1257 A C
ATOM 953 CG PRO A 126 6.022 7.390 11.191 1.00 52.03 A C
ANISOU 953 CG PRO A 126 8992 3916 6863 1577 2043 -1170 A C
ATOM 954 CD PRO A 126 6.876 6.417 11.977 1.00 49.18 A C
ANISOU 954 CD PRO A 126 8808 3584 6294 1958 2043 -1257 A C
ATOM 955 N TYR A 127 5.144 10.132 14.048 1.00 43.89 A N
ANISOU 955 N TYR A 127 7436 3008 6234 1481 1916 -1263 A N
ATOM 956 CA TYR A 127 4.010 10.555 14.873 1.00 41.94 A C
ANISOU 956 CA TYR A 127 7216 2645 6073 1367 1915 -1183 A C
ATOM 957 C TYR A 127 3.223 11.661 14.180 1.00 43.46 A C
ANISOU 957 C TYR A 127 7240 2772 6501 1065 1972 -1061 A C
ATOM 958 O TYR A 127 3.801 12.509 13.492 1.00 43.00 A O
ANISOU 958 O TYR A 127 6948 2796 6593 974 2014 -1101 A O
ATOM 959 CB TYR A 127 4.547 11.072 16.219 1.00 43.50 A C
ANISOU 959 CB TYR A 127 7244 2994 6290 1526 1863 -1358 A C
ATOM 960 CG TYR A 127 3.583 11.116 17.388 1.00 44.10 A C
ANISOU 960 CG TYR A 127 7420 2976 6360 1529 1849 -1311 A C
ATOM 961 CD1 TYR A 127 2.702 12.187 17.555 1.00 44.12 A C
ANISOU 961 CD1 TYR A 127 7294 2888 6583 1293 1890 -1248 A C
ATOM 962 CD2 TYR A 127 3.663 10.180 18.413 1.00 45.39 A C
ANISOU 962 CD2 TYR A 127 7784 3163 6298 1798 1807 -1337 A C
ATOM 963 CE1 TYR A 127 1.877 12.281 18.677 1.00 42.67 A C
ANISOU 963 CE1 TYR A 127 7180 2636 6396 1301 1879 -1222 A C
ATOM 964 CE2 TYR A 127 2.851 10.269 19.541 1.00 46.08 A C
ANISOU 964 CE2 TYR A 127 7946 3188 6376 1809 1797 -1306 A C
ATOM 965 CZ TYR A 127 1.973 11.332 19.677 1.00 51.61 A C
ANISOU 965 CZ TYR A 127 8503 3805 7302 1552 1826 -1265 A C
ATOM 966 OH TYR A 127 1.157 11.413 20.779 1.00 55.43 A O
ANISOU 966 OH TYR A 127 9060 4227 7772 1562 1822 -1237 A O
ATOM 967 N LEU A 128 1.901 11.667 14.405 1.00 39.34 A N
ANISOU 967 N LEU A 128 6831 2110 6005 927 1989 -909 A N
ATOM 968 CA LEU A 128 0.957 12.670 13.911 1.00 37.67 A C
ANISOU 968 CA LEU A 128 6476 1850 5989 690 2050 -754 A C
ATOM 969 C LEU A 128 -0.043 13.026 14.998 1.00 37.91 A C
ANISOU 969 C LEU A 128 6527 1794 6083 655 2051 -707 A C
ATOM 970 O LEU A 128 -0.551 12.137 15.683 1.00 36.65 A O
ANISOU 970 O LEU A 128 6596 1564 5766 721 2014 -694 A O
ATOM 971 CB LEU A 128 0.205 12.170 12.658 1.00 37.86 A C
ANISOU 971 CB LEU A 128 6609 1848 5928 525 2078 -574 A C
ATOM 972 CG LEU A 128 -1.092 12.929 12.275 1.00 41.22 A C
ANISOU 972 CG LEU A 128 6937 2257 6468 319 2131 -364 A C
ATOM 973 CD1 LEU A 128 -0.782 14.287 11.636 1.00 40.56 A C
ANISOU 973 CD1 LEU A 128 6572 2227 6611 255 2216 -295 A C
ATOM 974 CD2 LEU A 128 -1.993 12.077 11.400 1.00 43.46 A C
ANISOU 974 CD2 LEU A 128 7372 2567 6574 171 2132 -236 A C
ATOM 975 N PHE A 129 -0.335 14.332 15.139 1.00 32.56 A N
ANISOU 975 N PHE A 129 5538 1280 5555 491 2105 -612 A N
ATOM 976 CA PHE A 129 -1.339 14.821 16.055 1.00 31.56 A C
ANISOU 976 CA PHE A 129 5341 1198 5453 409 2123 -519 A C
ATOM 977 C PHE A 129 -1.964 16.082 15.483 1.00 33.02 A C
ANISOU 977 C PHE A 129 5422 1164 5961 316 2260 -428 A C
ATOM 978 O PHE A 129 -1.318 16.814 14.737 1.00 31.18 A O
ANISOU 978 O PHE A 129 4947 1106 5796 242 2339 -401 A O
ATOM 979 CB PHE A 129 -0.792 15.018 17.474 1.00 33.46 A C
ANISOU 979 CB PHE A 129 5597 1358 5759 569 2088 -755 A C
ATOM 980 CG PHE A 129 0.170 16.170 17.698 1.00 34.55 A C
ANISOU 980 CG PHE A 129 5515 1468 6143 596 2164 -987 A C
ATOM 981 CD1 PHE A 129 -0.295 17.417 18.105 1.00 35.69 A C
ANISOU 981 CD1 PHE A 129 5543 1446 6571 515 2298 -1028 A C
ATOM 982 CD2 PHE A 129 1.542 15.980 17.591 1.00 36.05 A C
ANISOU 982 CD2 PHE A 129 5657 1734 6308 747 2138 -1238 A C
ATOM 983 CE1 PHE A 129 0.591 18.486 18.314 1.00 38.77 A C
ANISOU 983 CE1 PHE A 129 5694 1883 7152 466 2406 -1242 A C
ATOM 984 CE2 PHE A 129 2.428 17.041 17.826 1.00 40.33 A C
ANISOU 984 CE2 PHE A 129 5931 2369 7023 699 2221 -1459 A C
ATOM 985 CZ PHE A 129 1.948 18.292 18.171 1.00 38.55 A C
ANISOU 985 CZ PHE A 129 5561 2033 7053 541 2365 -1468 A C
ATOM 986 N SER A 130 -3.237 16.295 15.806 1.00 32.08 A N
ANISOU 986 N SER A 130 5276 1103 5811 228 2287 -257 A N
ATOM 987 CA SER A 130 -4.028 17.427 15.352 1.00 32.52 A C
ANISOU 987 CA SER A 130 5192 1079 6087 148 2422 -84 A C
ATOM 988 C SER A 130 -4.303 18.437 16.466 1.00 37.86 A C
ANISOU 988 C SER A 130 5874 1443 7068 179 2515 -161 A C
ATOM 989 O SER A 130 -4.276 18.091 17.647 1.00 39.22 A O
ANISOU 989 O SER A 130 6129 1593 7178 241 2445 -316 A O
ATOM 990 CB SER A 130 -5.360 16.940 14.787 1.00 33.65 A C
ANISOU 990 CB SER A 130 5495 1106 6184 75 2399 141 A C
ATOM 991 OG SER A 130 -6.259 16.629 15.836 1.00 37.93 A O
ANISOU 991 OG SER A 130 6164 1558 6689 72 2359 141 A O
ATOM 992 N GLN A 131 -4.581 19.685 16.061 1.00 34.92 A N
ANISOU 992 N GLN A 131 5311 1054 6903 123 2692 -24 A N
ATOM 993 CA GLN A 131 -4.987 20.820 16.881 1.00 35.49 A C
ANISOU 993 CA GLN A 131 5267 1032 7187 109 2845 -38 A C
ATOM 994 C GLN A 131 -5.972 21.642 16.054 1.00 37.85 A C
ANISOU 994 C GLN A 131 5520 1200 7661 87 3010 286 A C
ATOM 995 O GLN A 131 -5.546 22.464 15.241 1.00 39.08 A O
ANISOU 995 O GLN A 131 5563 1309 7978 78 3179 366 A O
ATOM 996 CB GLN A 131 -3.786 21.649 17.361 1.00 37.32 A C
ANISOU 996 CB GLN A 131 5417 1109 7652 106 2960 -324 A C
ATOM 997 CG GLN A 131 -4.151 22.846 18.276 1.00 41.79 A C
ANISOU 997 CG GLN A 131 5894 1515 8470 67 3157 -389 A C
ATOM 998 CD GLN A 131 -5.171 22.533 19.359 1.00 51.29 A C
ANISOU 998 CD GLN A 131 7192 2701 9597 99 3078 -362 A C
ATOM 999 NE2 GLN A 131 -6.247 23.285 19.390 1.00 49.54 A N
ANISOU 999 NE2 GLN A 131 6943 2363 9518 85 3228 -140 A N
ATOM 1000 OE1 GLN A 131 -5.003 21.629 20.174 1.00 42.46 A O
ANISOU 1000 OE1 GLN A 131 6173 1676 8286 153 2896 -527 A O
ATOM 1001 N CYS A 132 -7.275 21.358 16.201 1.00 33.66 A N
ANISOU 1001 N CYS A 132 4887 1013 6889 107 2964 442 A N
ATOM 1002 CA CYS A 132 -8.269 22.034 15.381 1.00 35.13 A C
ANISOU 1002 CA CYS A 132 5032 1113 7204 126 3097 778 A C
ATOM 1003 C CYS A 132 -8.754 23.353 15.957 1.00 39.47 A C
ANISOU 1003 C CYS A 132 5578 1313 8106 145 3337 909 A C
ATOM 1004 O CYS A 132 -9.117 24.225 15.164 1.00 40.63 A O
ANISOU 1004 O CYS A 132 5620 1444 8375 202 3530 1175 A O
ATOM 1005 CB CYS A 132 -9.429 21.115 15.043 1.00 35.53 A C
ANISOU 1005 CB CYS A 132 5191 1257 7051 78 2952 979 A C
ATOM 1006 SG CYS A 132 -8.976 19.798 13.889 1.00 39.40 A S
ANISOU 1006 SG CYS A 132 5800 1891 7281 -10 2774 979 A S
ATOM 1007 N GLN A 133 -8.724 23.542 17.299 1.00 36.24 A N
ANISOU 1007 N GLN A 133 5083 1024 7663 161 3343 642 A N
ATOM 1008 CA GLN A 133 -9.163 24.817 17.910 1.00 36.07 A C
ANISOU 1008 CA GLN A 133 4929 922 7854 203 3595 666 A C
ATOM 1009 C GLN A 133 -8.155 25.941 17.548 1.00 39.73 A C
ANISOU 1009 C GLN A 133 5457 902 8735 157 3862 641 A C
ATOM 1010 O GLN A 133 -6.954 25.711 17.650 1.00 37.27 A O
ANISOU 1010 O GLN A 133 5042 805 8316 99 3805 343 A O
ATOM 1011 CB GLN A 133 -9.347 24.687 19.437 1.00 35.83 A C
ANISOU 1011 CB GLN A 133 4937 876 7801 164 3540 448 A C
ATOM 1012 CG GLN A 133 -10.265 25.774 20.039 1.00 37.10 A C
ANISOU 1012 CG GLN A 133 5072 822 8204 206 3773 567 A C
ATOM 1013 CD GLN A 133 -10.429 25.748 21.535 1.00 45.65 A C
ANISOU 1013 CD GLN A 133 6394 1462 9490 160 3744 373 A C
ATOM 1014 NE2 GLN A 133 -11.237 26.669 22.030 1.00 42.98 A N
ANISOU 1014 NE2 GLN A 133 6017 978 9334 197 3955 477 A N
ATOM 1015 OE1 GLN A 133 -9.918 24.870 22.255 1.00 41.81 A O
ANISOU 1015 OE1 GLN A 133 5985 1066 8836 129 3537 113 A O
ATOM 1016 N ALA A 134 -8.625 27.121 17.059 1.00 40.62 A N
ANISOU 1016 N ALA A 134 5473 912 9048 230 4165 882 A N
ATOM 1017 CA ALA A 134 -10.045 27.470 16.957 1.00 41.57 A C
ANISOU 1017 CA ALA A 134 5593 1009 9193 341 4252 1239 A C
ATOM 1018 C ALA A 134 -10.680 27.156 15.596 1.00 46.86 A C
ANISOU 1018 C ALA A 134 6240 1851 9714 422 4198 1645 A C
ATOM 1019 O ALA A 134 -11.778 26.590 15.558 1.00 46.23 A O
ANISOU 1019 O ALA A 134 6144 1988 9433 460 4049 1828 A O
ATOM 1020 CB ALA A 134 -10.240 28.947 17.274 1.00 44.09 A C
ANISOU 1020 CB ALA A 134 5912 959 9881 389 4651 1336 A C
ATOM 1021 N THR A 135 -10.029 27.573 14.500 1.00 45.17 A N
ANISOU 1021 N THR A 135 5978 1619 9567 453 4338 1763 A N
ATOM 1022 CA THR A 135 -10.542 27.440 13.132 1.00 46.55 A C
ANISOU 1022 CA THR A 135 6072 2043 9573 558 4325 2134 A C
ATOM 1023 C THR A 135 -9.606 26.613 12.222 1.00 49.70 A C
ANISOU 1023 C THR A 135 6483 2604 9795 471 4142 2028 A C
ATOM 1024 O THR A 135 -9.406 26.981 11.062 1.00 50.90 A O
ANISOU 1024 O THR A 135 6569 2828 9943 544 4266 2255 A O
ATOM 1025 CB THR A 135 -10.756 28.850 12.510 1.00 54.57 A C
ANISOU 1025 CB THR A 135 7016 2895 10823 733 4725 2470 A C
ATOM 1026 CG2 THR A 135 -11.887 29.613 13.147 1.00 55.31 A C
ANISOU 1026 CG2 THR A 135 7086 2885 11045 872 4918 2669 A C
ATOM 1027 OG1 THR A 135 -9.559 29.589 12.660 1.00 55.20 A O
ANISOU 1027 OG1 THR A 135 7140 2654 11179 659 4963 2251 A O
ATOM 1028 N HIS A 136 -9.057 25.495 12.712 1.00 45.36 A N
ANISOU 1028 N HIS A 136 6025 2125 9086 338 3862 1711 A N
ATOM 1029 CA HIS A 136 -8.161 24.693 11.866 1.00 44.77 A C
ANISOU 1029 CA HIS A 136 5973 2194 8845 272 3707 1610 A C
ATOM 1030 C HIS A 136 -8.787 23.391 11.369 1.00 46.71 A C
ANISOU 1030 C HIS A 136 6253 2752 8743 224 3431 1676 A C
ATOM 1031 O HIS A 136 -8.157 22.715 10.573 1.00 46.15 A O
ANISOU 1031 O HIS A 136 6205 2810 8520 174 3320 1618 A O
ATOM 1032 CB HIS A 136 -6.822 24.414 12.555 1.00 44.30 A C
ANISOU 1032 CB HIS A 136 5982 1989 8859 180 3642 1200 A C
ATOM 1033 CG HIS A 136 -6.114 25.664 12.969 1.00 48.63 A C
ANISOU 1033 CG HIS A 136 6478 2262 9736 172 3930 1077 A C
ATOM 1034 CD2 HIS A 136 -5.862 26.151 14.195 1.00 50.22 A C
ANISOU 1034 CD2 HIS A 136 6690 2269 10122 127 4024 828 A C
ATOM 1035 ND1 HIS A 136 -5.596 26.540 12.021 1.00 51.80 A N
ANISOU 1035 ND1 HIS A 136 6809 2576 10299 194 4180 1209 A N
ATOM 1036 CE1 HIS A 136 -5.021 27.507 12.706 1.00 52.65 A C
ANISOU 1036 CE1 HIS A 136 6895 2414 10695 143 4433 1020 A C
ATOM 1037 NE2 HIS A 136 -5.158 27.317 14.020 1.00 52.21 A N
ANISOU 1037 NE2 HIS A 136 6877 2301 10659 96 4344 778 A N
ATOM 1038 N CYS A 137 -10.035 23.074 11.745 1.00 43.70 A N
ANISOU 1038 N CYS A 137 5868 2502 8234 227 3350 1800 A N
ATOM 1039 CA CYS A 137 -10.686 21.847 11.263 1.00 42.02 A C
ANISOU 1039 CA CYS A 137 5684 2593 7690 137 3126 1835 A C
ATOM 1040 C CYS A 137 -10.863 21.891 9.735 1.00 45.69 A C
ANISOU 1040 C CYS A 137 6016 3342 8002 168 3152 2095 A C
ATOM 1041 O CYS A 137 -10.831 20.852 9.080 1.00 45.56 A O
ANISOU 1041 O CYS A 137 6036 3546 7728 58 2986 2032 A O
ATOM 1042 CB CYS A 137 -12.013 21.609 11.972 1.00 42.20 A C
ANISOU 1042 CB CYS A 137 5700 2715 7620 117 3068 1910 A C
ATOM 1043 SG CYS A 137 -12.685 19.945 11.736 1.00 44.92 A S
ANISOU 1043 SG CYS A 137 6135 3356 7578 -71 2815 1817 A S
ATOM 1044 N ARG A 138 -10.995 23.106 9.183 1.00 41.78 A N
ANISOU 1044 N ARG A 138 5381 2828 7667 324 3384 2380 A N
ATOM 1045 CA ARG A 138 -11.121 23.397 7.757 1.00 42.42 A C
ANISOU 1045 CA ARG A 138 5318 3171 7627 411 3461 2676 A C
ATOM 1046 C ARG A 138 -9.850 22.977 6.977 1.00 42.47 A C
ANISOU 1046 C ARG A 138 5381 3161 7595 338 3412 2520 A C
ATOM 1047 O ARG A 138 -9.950 22.749 5.774 1.00 41.50 A O
ANISOU 1047 O ARG A 138 5165 3333 7270 351 3385 2689 A O
ATOM 1048 CB ARG A 138 -11.444 24.896 7.519 1.00 43.06 A C
ANISOU 1048 CB ARG A 138 5280 3146 7935 638 3780 3020 A C
ATOM 1049 CG ARG A 138 -10.439 25.899 8.096 1.00 42.13 A C
ANISOU 1049 CG ARG A 138 5245 2565 8197 673 4030 2891 A C
ATOM 1050 CD ARG A 138 -10.970 27.331 8.045 1.00 48.39 A C
ANISOU 1050 CD ARG A 138 5962 3201 9222 894 4387 3228 A C
ATOM 1051 NE ARG A 138 -12.144 27.492 8.912 1.00 49.14 A N
ANISOU 1051 NE ARG A 138 6033 3308 9331 957 4387 3310 A N
ATOM 1052 CZ ARG A 138 -12.840 28.615 9.060 1.00 52.41 A C
ANISOU 1052 CZ ARG A 138 6392 3601 9921 1166 4679 3601 A C
ATOM 1053 NH1 ARG A 138 -12.493 29.716 8.397 1.00 45.72 A N1+
ANISOU 1053 NH1 ARG A 138 5525 2584 9262 1341 5025 3856 A N1+
ATOM 1054 NH2 ARG A 138 -13.888 28.647 9.866 1.00 39.33 A N
ANISOU 1054 NH2 ARG A 138 4544 2183 8215 1393 4529 3350 A N
ATOM 1055 N SER A 139 -8.681 22.855 7.671 1.00 37.72 A N
ANISOU 1055 N SER A 139 4912 2256 7162 265 3397 2191 A N
ATOM 1056 CA SER A 139 -7.398 22.365 7.140 1.00 36.93 A C
ANISOU 1056 CA SER A 139 4872 2129 7029 195 3336 1987 A C
ATOM 1057 C SER A 139 -7.360 20.819 7.066 1.00 39.20 A C
ANISOU 1057 C SER A 139 5276 2598 7019 57 3059 1781 A C
ATOM 1058 O SER A 139 -6.391 20.271 6.534 1.00 39.43 A O
ANISOU 1058 O SER A 139 5357 2651 6972 10 2996 1632 A O
ATOM 1059 CB SER A 139 -6.221 22.871 7.972 1.00 38.32 A C
ANISOU 1059 CB SER A 139 5110 1966 7484 182 3437 1709 A C
ATOM 1060 OG SER A 139 -6.138 24.281 7.917 1.00 51.34 A O
ANISOU 1060 OG SER A 139 6672 3419 9415 275 3744 1872 A O
ATOM 1061 N ILE A 140 -8.405 20.118 7.576 1.00 35.29 A N
ANISOU 1061 N ILE A 140 4830 2221 6357 -10 2923 1771 A N
ATOM 1062 CA ILE A 140 -8.472 18.656 7.500 1.00 33.97 A C
ANISOU 1062 CA ILE A 140 4802 2191 5914 -156 2716 1583 A C
ATOM 1063 C ILE A 140 -9.614 18.243 6.560 1.00 40.97 A C
ANISOU 1063 C ILE A 140 5577 3466 6521 -235 2664 1784 A C
ATOM 1064 O ILE A 140 -9.373 17.522 5.588 1.00 42.20 A O
ANISOU 1064 O ILE A 140 5743 3827 6463 -328 2593 1744 A O
ATOM 1065 CB ILE A 140 -8.598 17.957 8.885 1.00 35.35 A C
ANISOU 1065 CB ILE A 140 5161 2179 6091 -207 2611 1340 A C
ATOM 1066 CG1 ILE A 140 -7.557 18.503 9.894 1.00 34.57 A C
ANISOU 1066 CG1 ILE A 140 5120 1769 6247 -117 2665 1140 A C
ATOM 1067 CG2 ILE A 140 -8.525 16.409 8.748 1.00 32.24 A C
ANISOU 1067 CG2 ILE A 140 4956 1870 5422 -348 2454 1146 A C
ATOM 1068 CD1 ILE A 140 -7.699 17.976 11.327 1.00 34.65 A C
ANISOU 1068 CD1 ILE A 140 5285 1621 6261 -124 2581 937 A C
ATOM 1069 N ILE A 141 -10.853 18.670 6.867 1.00 37.61 A N
ANISOU 1069 N ILE A 141 5037 3169 6084 -206 2699 1977 A N
ATOM 1070 CA ILE A 141 -12.056 18.302 6.107 1.00 38.32 A C
ANISOU 1070 CA ILE A 141 4978 3695 5886 -287 2645 2148 A C
ATOM 1071 C ILE A 141 -12.909 19.544 5.748 1.00 45.23 A C
ANISOU 1071 C ILE A 141 5601 4765 6820 -95 2793 2534 A C
ATOM 1072 O ILE A 141 -12.877 20.526 6.494 1.00 43.49 A O
ANISOU 1072 O ILE A 141 5376 4272 6875 58 2931 2624 A O
ATOM 1073 CB ILE A 141 -12.907 17.264 6.912 1.00 40.67 A C
ANISOU 1073 CB ILE A 141 5394 4036 6025 -472 2520 1965 A C
ATOM 1074 CG1 ILE A 141 -13.319 17.800 8.319 1.00 39.51 A C
ANISOU 1074 CG1 ILE A 141 5296 3617 6099 -389 2568 1958 A C
ATOM 1075 CG2 ILE A 141 -12.204 15.880 6.993 1.00 38.94 A C
ANISOU 1075 CG2 ILE A 141 5430 3697 5668 -654 2404 1632 A C
ATOM 1076 CD1 ILE A 141 -14.428 17.122 8.933 1.00 45.94 A C
ANISOU 1076 CD1 ILE A 141 6152 4542 6760 -535 2493 1885 A C
ATOM 1077 N PRO A 142 -13.671 19.530 4.620 1.00 47.34 A N
ANISOU 1077 N PRO A 142 5652 5514 6820 -88 2782 2764 A N
ATOM 1078 CA PRO A 142 -14.579 20.659 4.340 1.00 50.42 A C
ANISOU 1078 CA PRO A 142 5799 6127 7233 142 2930 3160 A C
ATOM 1079 C PRO A 142 -15.767 20.597 5.308 1.00 53.56 A C
ANISOU 1079 C PRO A 142 6156 6583 7611 115 2896 3169 A C
ATOM 1080 O PRO A 142 -16.377 19.538 5.465 1.00 52.20 A O
ANISOU 1080 O PRO A 142 6002 6632 7200 -114 2736 2985 A O
ATOM 1081 CB PRO A 142 -14.995 20.443 2.881 1.00 55.04 A C
ANISOU 1081 CB PRO A 142 6161 7278 7473 142 2890 3352 A C
ATOM 1082 CG PRO A 142 -14.862 18.976 2.658 1.00 58.70 A C
ANISOU 1082 CG PRO A 142 6736 7889 7679 -176 2688 3010 A C
ATOM 1083 CD PRO A 142 -13.842 18.441 3.632 1.00 50.91 A C
ANISOU 1083 CD PRO A 142 6066 6363 6915 -289 2642 2661 A C
ATOM 1084 N CYS A 143 -16.044 21.703 6.012 1.00 51.21 A N
ANISOU 1084 N CYS A 143 5829 6047 7582 327 3066 3352 A N
ATOM 1085 CA CYS A 143 -17.089 21.738 7.041 1.00 51.58 A C
ANISOU 1085 CA CYS A 143 5853 6093 7653 319 3054 3353 A C
ATOM 1086 C CYS A 143 -17.594 23.150 7.297 1.00 54.92 A C
ANISOU 1086 C CYS A 143 6150 6421 8297 625 3294 3694 A C
ATOM 1087 O CYS A 143 -17.048 24.119 6.773 1.00 54.16 A O
ANISOU 1087 O CYS A 143 6025 6181 8374 837 3496 3908 A O
ATOM 1088 CB CYS A 143 -16.536 21.138 8.336 1.00 49.71 A C
ANISOU 1088 CB CYS A 143 5892 5418 7578 149 2966 2975 A C
ATOM 1089 SG CYS A 143 -14.996 21.911 8.909 1.00 52.42 A S
ANISOU 1089 SG CYS A 143 6427 5161 8329 256 3112 2836 A S
ATOM 1090 N GLN A 144 -18.615 23.257 8.171 1.00 50.88 A N
ANISOU 1090 N GLN A 144 5588 5946 7797 645 3298 3728 A N
ATOM 1091 CA GLN A 144 -19.103 24.519 8.694 1.00 51.02 A C
ANISOU 1091 CA GLN A 144 5538 5790 8057 919 3538 3993 A C
ATOM 1092 C GLN A 144 -18.243 24.740 9.928 1.00 49.97 A C
ANISOU 1092 C GLN A 144 5664 5049 8274 853 3600 3706 A C
ATOM 1093 O GLN A 144 -18.623 24.360 11.027 1.00 47.37 A O
ANISOU 1093 O GLN A 144 5425 4596 7979 739 3519 3509 A O
ATOM 1094 CB GLN A 144 -20.608 24.457 8.999 1.00 53.85 A C
ANISOU 1094 CB GLN A 144 5699 6530 8230 962 3499 4149 A C
ATOM 1095 CG GLN A 144 -21.525 24.531 7.778 1.00 65.35 A C
ANISOU 1095 CG GLN A 144 6831 8655 9342 1100 3486 4489 A C
ATOM 1096 CD GLN A 144 -22.972 24.569 8.200 1.00 69.75 A C
ANISOU 1096 CD GLN A 144 7177 9585 9739 1155 3466 4626 A C
ATOM 1097 NE2 GLN A 144 -23.681 25.614 7.804 1.00 54.74 A N
ANISOU 1097 NE2 GLN A 144 5047 7923 7828 1520 3664 5060 A N
ATOM 1098 OE1 GLN A 144 -23.463 23.675 8.899 1.00 62.34 A O
ANISOU 1098 OE1 GLN A 144 6281 8721 8682 883 3292 4351 A O
ATOM 1099 N ASP A 145 -17.020 25.235 9.729 1.00 46.79 A N
ANISOU 1099 N ASP A 145 5379 4300 8099 894 3727 3641 A N
ATOM 1100 CA ASP A 145 -16.052 25.375 10.811 1.00 45.15 A C
ANISOU 1100 CA ASP A 145 5387 3583 8183 803 3769 3317 A C
ATOM 1101 C ASP A 145 -16.375 26.570 11.716 1.00 53.09 A C
ANISOU 1101 C ASP A 145 6403 4269 9501 969 4037 3416 A C
ATOM 1102 O ASP A 145 -15.618 27.543 11.801 1.00 56.85 A O
ANISOU 1102 O ASP A 145 6941 4385 10273 1057 4289 3414 A O
ATOM 1103 CB ASP A 145 -14.626 25.440 10.251 1.00 45.74 A C
ANISOU 1103 CB ASP A 145 5555 3455 8368 759 3810 3179 A C
ATOM 1104 CG ASP A 145 -13.536 25.180 11.271 1.00 47.91 A C
ANISOU 1104 CG ASP A 145 6026 3350 8828 609 3757 2764 A C
ATOM 1105 OD1 ASP A 145 -13.806 24.468 12.270 1.00 47.67 A O
ANISOU 1105 OD1 ASP A 145 6091 3285 8736 489 3591 2536 A O
ATOM 1106 OD2 ASP A 145 -12.406 25.646 11.053 1.00 47.16 A O1-
ANISOU 1106 OD2 ASP A 145 5979 3025 8915 612 3881 2665 A O1-
ATOM 1107 N THR A 146 -17.518 26.470 12.393 1.00 49.29 A N
ANISOU 1107 N THR A 146 5861 3922 8945 992 3994 3481 A N
ATOM 1108 CA THR A 146 -18.054 27.437 13.351 1.00 49.42 A C
ANISOU 1108 CA THR A 146 5882 3689 9208 1137 4219 3564 A C
ATOM 1109 C THR A 146 -18.631 26.656 14.549 1.00 49.03 A C
ANISOU 1109 C THR A 146 5903 3654 9073 968 4020 3314 A C
ATOM 1110 O THR A 146 -19.397 25.717 14.343 1.00 48.84 A O
ANISOU 1110 O THR A 146 5806 4003 8749 861 3799 3323 A O
ATOM 1111 CB THR A 146 -19.065 28.416 12.705 1.00 56.52 A C
ANISOU 1111 CB THR A 146 6581 4797 10098 1449 4458 4050 A C
ATOM 1112 CG2 THR A 146 -20.179 27.723 11.924 1.00 52.36 A C
ANISOU 1112 CG2 THR A 146 5831 4891 9172 1470 4259 4272 A C
ATOM 1113 OG1 THR A 146 -19.645 29.196 13.735 1.00 60.94 A O
ANISOU 1113 OG1 THR A 146 7161 5117 10875 1568 4657 4094 A O
ATOM 1114 N PRO A 147 -18.276 27.029 15.800 1.00 43.93 A N
ANISOU 1114 N PRO A 147 5396 2616 8677 932 4111 3080 A N
ATOM 1115 CA PRO A 147 -18.794 26.294 16.980 1.00 42.59 A C
ANISOU 1115 CA PRO A 147 5309 2452 8421 786 3935 2848 A C
ATOM 1116 C PRO A 147 -20.330 26.333 17.145 1.00 51.47 A C
ANISOU 1116 C PRO A 147 6281 3866 9408 872 3940 3088 A C
ATOM 1117 O PRO A 147 -20.886 25.629 17.990 1.00 49.88 A O
ANISOU 1117 O PRO A 147 6134 3725 9094 738 3790 2925 A O
ATOM 1118 CB PRO A 147 -18.094 26.986 18.156 1.00 43.11 A C
ANISOU 1118 CB PRO A 147 5514 2067 8799 778 4092 2596 A C
ATOM 1119 CG PRO A 147 -17.730 28.335 17.642 1.00 49.07 A C
ANISOU 1119 CG PRO A 147 6217 2599 9830 960 4431 2792 A C
ATOM 1120 CD PRO A 147 -17.357 28.105 16.212 1.00 45.30 A C
ANISOU 1120 CD PRO A 147 5662 2339 9212 997 4388 2984 A C
ATOM 1121 N SER A 148 -21.005 27.103 16.292 1.00 53.98 A N
ANISOU 1121 N SER A 148 6404 4397 9711 1102 4110 3482 A N
ATOM 1122 CA SER A 148 -22.456 27.267 16.222 1.00 56.86 A C
ANISOU 1122 CA SER A 148 6562 5121 9921 1239 4139 3769 A C
ATOM 1123 C SER A 148 -23.133 26.008 15.686 1.00 58.84 A C
ANISOU 1123 C SER A 148 6694 5890 9770 1052 3846 3742 A C
ATOM 1124 O SER A 148 -24.325 25.812 15.922 1.00 57.01 A O
ANISOU 1124 O SER A 148 6314 5975 9372 1056 3800 3841 A O
ATOM 1125 CB SER A 148 -22.784 28.449 15.310 1.00 65.59 A C
ANISOU 1125 CB SER A 148 7493 6324 11105 1582 4421 4218 A C
ATOM 1126 OG SER A 148 -24.165 28.484 14.981 1.00 81.97 A O
ANISOU 1126 OG SER A 148 9316 8875 12954 1741 4417 4526 A O
ATOM 1127 N VAL A 149 -22.390 25.203 14.899 1.00 55.37 A N
ANISOU 1127 N VAL A 149 6308 5556 9174 887 3676 3611 A N
ATOM 1128 CA VAL A 149 -22.893 23.966 14.295 1.00 54.75 A C
ANISOU 1128 CA VAL A 149 6142 5941 8719 666 3429 3538 A C
ATOM 1129 C VAL A 149 -22.291 22.788 15.065 1.00 53.12 A C
ANISOU 1129 C VAL A 149 6203 5502 8479 363 3236 3114 A C
ATOM 1130 O VAL A 149 -21.073 22.620 15.112 1.00 52.02 A O
ANISOU 1130 O VAL A 149 6255 5049 8460 307 3209 2917 A O
ATOM 1131 CB VAL A 149 -22.614 23.905 12.759 1.00 60.66 A C
ANISOU 1131 CB VAL A 149 6743 7028 9277 714 3400 3720 A C
ATOM 1132 CG1 VAL A 149 -23.078 22.586 12.160 1.00 60.78 A C
ANISOU 1132 CG1 VAL A 149 6677 7515 8902 438 3161 3584 A C
ATOM 1133 CG2 VAL A 149 -23.267 25.087 12.023 1.00 63.49 A C
ANISOU 1133 CG2 VAL A 149 6840 7637 9648 1070 3615 4185 A C
ATOM 1134 N LYS A 150 -23.155 22.003 15.712 1.00 47.42 A N
ANISOU 1134 N LYS A 150 5493 4932 7593 187 3125 2985 A N
ATOM 1135 CA LYS A 150 -22.738 20.841 16.490 1.00 42.73 A C
ANISOU 1135 CA LYS A 150 5165 4129 6939 -73 2976 2621 A C
ATOM 1136 C LYS A 150 -23.286 19.612 15.846 1.00 44.19 A C
ANISOU 1136 C LYS A 150 5310 4705 6777 -336 2823 2529 A C
ATOM 1137 O LYS A 150 -24.471 19.544 15.539 1.00 44.87 A O
ANISOU 1137 O LYS A 150 5168 5216 6664 -380 2817 2663 A O
ATOM 1138 CB LYS A 150 -23.149 20.959 17.953 1.00 42.26 A C
ANISOU 1138 CB LYS A 150 5218 3825 7015 -74 3018 2508 A C
ATOM 1139 CG LYS A 150 -22.264 21.936 18.721 1.00 38.68 A C
ANISOU 1139 CG LYS A 150 4880 2909 6908 108 3157 2463 A C
ATOM 1140 CD LYS A 150 -22.049 21.523 20.168 1.00 52.03 A C
ANISOU 1140 CD LYS A 150 6803 4291 8674 15 3113 2177 A C
ATOM 1141 CE LYS A 150 -23.136 22.011 21.091 1.00 53.34 A C
ANISOU 1141 CE LYS A 150 6898 4465 8906 77 3208 2253 A C
ATOM 1142 NZ LYS A 150 -22.756 21.883 22.515 1.00 43.84 A N1+
ANISOU 1142 NZ LYS A 150 5912 2931 7816 38 3200 1991 A N1+
ATOM 1143 N PHE A 151 -22.403 18.659 15.597 1.00 39.11 A N
ANISOU 1143 N PHE A 151 4875 3935 6049 -510 2716 2293 A N
ATOM 1144 CA PHE A 151 -22.745 17.443 14.879 1.00 39.52 A C
ANISOU 1144 CA PHE A 151 4925 4311 5780 -789 2604 2165 A C
ATOM 1145 C PHE A 151 -22.175 16.197 15.543 1.00 43.33 A C
ANISOU 1145 C PHE A 151 5759 4493 6213 -1009 2533 1827 A C
ATOM 1146 O PHE A 151 -21.125 16.243 16.199 1.00 42.29 A O
ANISOU 1146 O PHE A 151 5859 3941 6270 -913 2533 1699 A O
ATOM 1147 CB PHE A 151 -22.184 17.564 13.424 1.00 41.01 A C
ANISOU 1147 CB PHE A 151 4981 4733 5869 -749 2581 2279 A C
ATOM 1148 CG PHE A 151 -20.692 17.791 13.348 1.00 39.36 A C
ANISOU 1148 CG PHE A 151 4963 4126 5865 -635 2591 2199 A C
ATOM 1149 CD1 PHE A 151 -20.163 19.074 13.417 1.00 41.35 A C
ANISOU 1149 CD1 PHE A 151 5152 4162 6398 -357 2713 2381 A C
ATOM 1150 CD2 PHE A 151 -19.813 16.719 13.202 1.00 39.67 A C
ANISOU 1150 CD2 PHE A 151 5246 4010 5816 -809 2501 1934 A C
ATOM 1151 CE1 PHE A 151 -18.783 19.281 13.389 1.00 40.48 A C
ANISOU 1151 CE1 PHE A 151 5199 3708 6473 -283 2732 2273 A C
ATOM 1152 CE2 PHE A 151 -18.430 16.927 13.180 1.00 41.08 A C
ANISOU 1152 CE2 PHE A 151 5578 3857 6174 -695 2507 1850 A C
ATOM 1153 CZ PHE A 151 -17.926 18.210 13.255 1.00 39.14 A C
ANISOU 1153 CZ PHE A 151 5242 3432 6200 -446 2616 2011 A C
ATOM 1154 N THR A 152 -22.850 15.079 15.322 1.00 40.96 A N
ANISOU 1154 N THR A 152 5489 4433 5641 -1301 2489 1682 A N
ATOM 1155 CA THR A 152 -22.433 13.754 15.746 1.00 39.26 A C
ANISOU 1155 CA THR A 152 5615 3977 5325 -1530 2463 1383 A C
ATOM 1156 C THR A 152 -21.514 13.209 14.653 1.00 41.91 A C
ANISOU 1156 C THR A 152 6028 4335 5560 -1599 2418 1295 A C
ATOM 1157 O THR A 152 -21.613 13.650 13.495 1.00 40.17 A O
ANISOU 1157 O THR A 152 5550 4457 5258 -1565 2397 1450 A O
ATOM 1158 CB THR A 152 -23.693 12.939 15.964 1.00 50.09 A C
ANISOU 1158 CB THR A 152 6959 5605 6468 -1826 2489 1280 A C
ATOM 1159 CG2 THR A 152 -23.502 11.481 15.865 1.00 49.37 A C
ANISOU 1159 CG2 THR A 152 7163 5404 6192 -2130 2508 996 A C
ATOM 1160 OG1 THR A 152 -24.214 13.279 17.243 1.00 54.00 A O
ANISOU 1160 OG1 THR A 152 7497 5925 7097 -1745 2535 1306 A O
ATOM 1161 N TYR A 153 -20.617 12.267 14.996 1.00 37.30 A N
ANISOU 1161 N TYR A 153 5795 3404 4973 -1670 2412 1062 A N
ATOM 1162 CA TYR A 153 -19.782 11.690 13.953 1.00 37.43 A C
ANISOU 1162 CA TYR A 153 5892 3444 4884 -1741 2382 968 A C
ATOM 1163 C TYR A 153 -19.394 10.242 14.215 1.00 40.96 A C
ANISOU 1163 C TYR A 153 6718 3643 5201 -1939 2421 690 A C
ATOM 1164 O TYR A 153 -19.427 9.749 15.339 1.00 38.90 A O
ANISOU 1164 O TYR A 153 6715 3083 4982 -1940 2467 579 A O
ATOM 1165 CB TYR A 153 -18.520 12.549 13.651 1.00 38.12 A C
ANISOU 1165 CB TYR A 153 5948 3352 5186 -1455 2350 1068 A C
ATOM 1166 CG TYR A 153 -17.321 12.395 14.571 1.00 37.92 A C
ANISOU 1166 CG TYR A 153 6212 2864 5333 -1293 2343 924 A C
ATOM 1167 CD1 TYR A 153 -16.383 11.383 14.365 1.00 40.05 A C
ANISOU 1167 CD1 TYR A 153 6750 2953 5514 -1345 2332 730 A C
ATOM 1168 CD2 TYR A 153 -17.031 13.357 15.531 1.00 36.66 A C
ANISOU 1168 CD2 TYR A 153 6024 2484 5421 -1064 2357 990 A C
ATOM 1169 CE1 TYR A 153 -15.238 11.280 15.159 1.00 39.07 A C
ANISOU 1169 CE1 TYR A 153 6850 2475 5519 -1156 2320 614 A C
ATOM 1170 CE2 TYR A 153 -15.884 13.270 16.325 1.00 36.22 A C
ANISOU 1170 CE2 TYR A 153 6181 2086 5494 -910 2342 844 A C
ATOM 1171 CZ TYR A 153 -14.985 12.238 16.130 1.00 40.87 A C
ANISOU 1171 CZ TYR A 153 7018 2541 5971 -942 2315 666 A C
ATOM 1172 OH TYR A 153 -13.843 12.198 16.897 1.00 40.01 A O
ANISOU 1172 OH TYR A 153 7078 2161 5963 -754 2295 537 A O
ATOM 1173 N TYR A 154 -19.034 9.572 13.123 1.00 39.50 A N
ANISOU 1173 N TYR A 154 6566 3593 4850 -2095 2421 590 A N
ATOM 1174 CA TYR A 154 -18.497 8.224 13.054 1.00 39.07 A C
ANISOU 1174 CA TYR A 154 6868 3309 4667 -2263 2489 340 A C
ATOM 1175 C TYR A 154 -17.317 8.269 12.116 1.00 42.05 A C
ANISOU 1175 C TYR A 154 7254 3660 5062 -2149 2443 335 A C
ATOM 1176 O TYR A 154 -17.436 8.833 11.028 1.00 42.78 A O
ANISOU 1176 O TYR A 154 7051 4104 5099 -2158 2390 459 A O
ATOM 1177 CB TYR A 154 -19.543 7.208 12.566 1.00 42.36 A C
ANISOU 1177 CB TYR A 154 7298 3986 4810 -2677 2583 172 A C
ATOM 1178 CG TYR A 154 -19.088 5.780 12.777 1.00 45.11 A C
ANISOU 1178 CG TYR A 154 8091 3990 5058 -2849 2721 -92 A C
ATOM 1179 CD1 TYR A 154 -19.464 5.069 13.914 1.00 47.35 A C
ANISOU 1179 CD1 TYR A 154 8680 3969 5342 -2929 2847 -204 A C
ATOM 1180 CD2 TYR A 154 -18.241 5.153 11.864 1.00 46.60 A C
ANISOU 1180 CD2 TYR A 154 8417 4132 5159 -2902 2750 -215 A C
ATOM 1181 CE1 TYR A 154 -19.017 3.771 14.134 1.00 48.46 A C
ANISOU 1181 CE1 TYR A 154 9264 3749 5398 -3043 3017 -416 A C
ATOM 1182 CE2 TYR A 154 -17.779 3.857 12.078 1.00 48.61 A C
ANISOU 1182 CE2 TYR A 154 9108 4027 5334 -3018 2912 -440 A C
ATOM 1183 CZ TYR A 154 -18.184 3.165 13.206 1.00 57.11 A C
ANISOU 1183 CZ TYR A 154 10495 4791 6412 -3085 3056 -533 A C
ATOM 1184 OH TYR A 154 -17.742 1.885 13.408 1.00 61.12 A O
ANISOU 1184 OH TYR A 154 11461 4923 6841 -3172 3259 -729 A O
ATOM 1185 N SER A 155 -16.186 7.684 12.508 1.00 37.55 A N
ANISOU 1185 N SER A 155 7009 2704 4553 -2022 2468 206 A N
ATOM 1186 CA SER A 155 -15.024 7.686 11.631 1.00 36.49 A C
ANISOU 1186 CA SER A 155 6887 2545 4433 -1911 2430 187 A C
ATOM 1187 C SER A 155 -14.347 6.331 11.538 1.00 41.47 A C
ANISOU 1187 C SER A 155 7898 2920 4940 -1996 2525 -39 A C
ATOM 1188 O SER A 155 -14.374 5.540 12.476 1.00 41.67 A O
ANISOU 1188 O SER A 155 8242 2643 4947 -1999 2618 -153 A O
ATOM 1189 CB SER A 155 -14.004 8.738 12.060 1.00 36.77 A C
ANISOU 1189 CB SER A 155 6845 2405 4723 -1559 2351 307 A C
ATOM 1190 OG SER A 155 -13.359 8.377 13.268 1.00 45.46 A O
ANISOU 1190 OG SER A 155 8228 3133 5913 -1388 2370 205 A O
ATOM 1191 N GLN A 156 -13.743 6.083 10.381 1.00 40.48 A N
ANISOU 1191 N GLN A 156 7739 2916 4724 -2049 2520 -89 A N
ATOM 1192 CA GLN A 156 -12.896 4.937 10.074 1.00 41.86 A C
ANISOU 1192 CA GLN A 156 8244 2863 4798 -2082 2616 -283 A C
ATOM 1193 C GLN A 156 -11.554 5.526 9.667 1.00 43.49 A C
ANISOU 1193 C GLN A 156 8373 3018 5132 -1795 2524 -216 A C
ATOM 1194 O GLN A 156 -11.527 6.381 8.779 1.00 43.45 A O
ANISOU 1194 O GLN A 156 8051 3305 5151 -1786 2439 -88 A O
ATOM 1195 CB GLN A 156 -13.509 4.042 8.981 1.00 45.62 A C
ANISOU 1195 CB GLN A 156 8736 3577 5021 -2469 2719 -443 A C
ATOM 1196 CG GLN A 156 -14.846 3.431 9.386 1.00 64.15 A C
ANISOU 1196 CG GLN A 156 11159 5983 7232 -2797 2839 -552 A C
ATOM 1197 CD GLN A 156 -15.423 2.535 8.329 1.00 84.18 A C
ANISOU 1197 CD GLN A 156 13698 8778 9509 -3218 2960 -761 A C
ATOM 1198 NE2 GLN A 156 -15.908 1.384 8.755 1.00 82.41 A N
ANISOU 1198 NE2 GLN A 156 13806 8333 9174 -3483 3172 -982 A N
ATOM 1199 OE1 GLN A 156 -15.486 2.877 7.139 1.00 76.83 A O
ANISOU 1199 OE1 GLN A 156 12465 8262 8463 -3324 2882 -732 A O
ATOM 1200 N VAL A 157 -10.456 5.154 10.368 1.00 37.92 A N
ANISOU 1200 N VAL A 157 7932 1965 4508 -1539 2544 -285 A N
ATOM 1201 CA VAL A 157 -9.117 5.706 10.094 1.00 34.70 A C
ANISOU 1201 CA VAL A 157 7443 1518 4225 -1263 2462 -249 A C
ATOM 1202 C VAL A 157 -8.141 4.630 9.667 1.00 37.12 A C
ANISOU 1202 C VAL A 157 8035 1650 4417 -1216 2548 -410 A C
ATOM 1203 O VAL A 157 -7.764 3.794 10.477 1.00 36.54 A O
ANISOU 1203 O VAL A 157 8293 1283 4308 -1090 2639 -504 A O
ATOM 1204 CB VAL A 157 -8.544 6.504 11.293 1.00 35.41 A C
ANISOU 1204 CB VAL A 157 7492 1441 4523 -950 2385 -183 A C
ATOM 1205 CG1 VAL A 157 -7.260 7.219 10.894 1.00 34.44 A C
ANISOU 1205 CG1 VAL A 157 7209 1347 4529 -724 2309 -161 A C
ATOM 1206 CG2 VAL A 157 -9.554 7.485 11.818 1.00 33.54 A C
ANISOU 1206 CG2 VAL A 157 7020 1322 4400 -993 2336 -38 A C
ATOM 1207 N SER A 158 -7.657 4.723 8.413 1.00 35.51 A N
ANISOU 1207 N SER A 158 7698 1634 4163 -1275 2528 -420 A N
ATOM 1208 CA SER A 158 -6.699 3.809 7.812 1.00 36.38 A C
ANISOU 1208 CA SER A 158 8034 1620 4167 -1232 2611 -564 A C
ATOM 1209 C SER A 158 -5.288 4.282 8.143 1.00 41.82 A C
ANISOU 1209 C SER A 158 8689 2197 5002 -864 2532 -539 A C
ATOM 1210 O SER A 158 -4.938 5.419 7.833 1.00 41.13 A O
ANISOU 1210 O SER A 158 8289 2284 5054 -776 2419 -427 A O
ATOM 1211 CB SER A 158 -6.921 3.749 6.299 1.00 41.04 A C
ANISOU 1211 CB SER A 158 8463 2509 4619 -1486 2623 -592 A C
ATOM 1212 OG SER A 158 -5.994 2.885 5.664 1.00 48.51 A O
ANISOU 1212 OG SER A 158 9624 3340 5469 -1450 2713 -738 A O
ATOM 1213 N VAL A 159 -4.486 3.427 8.800 1.00 39.06 A N
ANISOU 1213 N VAL A 159 8658 1569 4615 -643 2610 -643 A N
ATOM 1214 CA VAL A 159 -3.119 3.769 9.217 1.00 37.80 A C
ANISOU 1214 CA VAL A 159 8461 1345 4556 -280 2539 -648 A C
ATOM 1215 C VAL A 159 -2.147 2.580 8.997 1.00 44.98 A C
ANISOU 1215 C VAL A 159 9687 2074 5328 -117 2662 -776 A C
ATOM 1216 O VAL A 159 -2.614 1.435 8.887 1.00 45.93 A O
ANISOU 1216 O VAL A 159 10132 2021 5297 -259 2833 -859 A O
ATOM 1217 CB VAL A 159 -3.065 4.231 10.716 1.00 40.01 A C
ANISOU 1217 CB VAL A 159 8739 1517 4947 -45 2476 -603 A C
ATOM 1218 CG1 VAL A 159 -3.897 5.477 10.970 1.00 37.81 A C
ANISOU 1218 CG1 VAL A 159 8143 1395 4828 -162 2371 -479 A C
ATOM 1219 CG2 VAL A 159 -3.427 3.103 11.689 1.00 40.93 A C
ANISOU 1219 CG2 VAL A 159 9249 1365 4938 11 2610 -651 A C
ATOM 1220 N PRO A 160 -0.794 2.801 9.000 1.00 41.70 A N
ANISOU 1220 N PRO A 160 9200 1684 4960 189 2603 -804 A N
ATOM 1221 CA PRO A 160 0.118 1.645 8.937 1.00 42.88 A C
ANISOU 1221 CA PRO A 160 9667 1657 4970 405 2735 -905 A C
ATOM 1222 C PRO A 160 -0.165 0.757 10.146 1.00 49.08 A C
ANISOU 1222 C PRO A 160 10818 2163 5667 570 2861 -909 A C
ATOM 1223 O PRO A 160 -0.307 1.277 11.255 1.00 46.11 A O
ANISOU 1223 O PRO A 160 10363 1791 5365 719 2773 -846 A O
ATOM 1224 CB PRO A 160 1.514 2.275 8.977 1.00 44.03 A C
ANISOU 1224 CB PRO A 160 9585 1947 5196 719 2617 -919 A C
ATOM 1225 CG PRO A 160 1.309 3.725 8.613 1.00 46.94 A C
ANISOU 1225 CG PRO A 160 9525 2562 5749 566 2459 -844 A C
ATOM 1226 CD PRO A 160 -0.045 4.070 9.143 1.00 41.34 A C
ANISOU 1226 CD PRO A 160 8796 1822 5090 358 2443 -756 A C
ATOM 1227 N LYS A 161 -0.312 -0.564 9.912 1.00 49.40 A N
ANISOU 1227 N LYS A 161 11265 1956 5549 522 3091 -983 A N
ATOM 1228 CA LYS A 161 -0.679 -1.599 10.881 1.00 52.19 A C
ANISOU 1228 CA LYS A 161 12047 1987 5797 637 3292 -981 A C
ATOM 1229 C LYS A 161 0.111 -1.587 12.211 1.00 58.66 A C
ANISOU 1229 C LYS A 161 12936 2745 6607 1130 3250 -907 A C
ATOM 1230 O LYS A 161 -0.452 -1.987 13.227 1.00 60.93 A O
ANISOU 1230 O LYS A 161 13453 2846 6851 1198 3345 -855 A O
ATOM 1231 CB LYS A 161 -0.594 -3.008 10.246 1.00 57.80 A C
ANISOU 1231 CB LYS A 161 13189 2424 6350 568 3589 -1091 A C
ATOM 1232 CG LYS A 161 0.749 -3.391 9.607 1.00 64.11 A C
ANISOU 1232 CG LYS A 161 14042 3226 7090 857 3631 -1140 A C
ATOM 1233 CD LYS A 161 0.835 -4.889 9.340 1.00 74.31 A C
ANISOU 1233 CD LYS A 161 15857 4150 8226 880 3986 -1228 A C
ATOM 1234 CE LYS A 161 1.664 -5.261 8.128 1.00 93.12 A C
ANISOU 1234 CE LYS A 161 18261 6570 10551 876 4063 -1336 A C
ATOM 1235 NZ LYS A 161 3.044 -4.701 8.158 1.00105.62 A N1+
ANISOU 1235 NZ LYS A 161 19611 8355 12164 1313 3889 -1282 A N1+
ATOM 1236 N GLU A 162 1.374 -1.135 12.222 1.00 55.16 A N
ANISOU 1236 N GLU A 162 12285 2486 6188 1464 3115 -910 A N
ATOM 1237 CA GLU A 162 2.207 -1.116 13.437 1.00 55.81 A C
ANISOU 1237 CA GLU A 162 12382 2603 6222 1946 3063 -862 A C
ATOM 1238 C GLU A 162 1.911 0.085 14.334 1.00 58.99 A C
ANISOU 1238 C GLU A 162 12445 3212 6757 1945 2845 -820 A C
ATOM 1239 O GLU A 162 2.512 0.222 15.404 1.00 59.34 A O
ANISOU 1239 O GLU A 162 12450 3345 6752 2309 2781 -800 A O
ATOM 1240 CB GLU A 162 3.709 -1.144 13.070 1.00 58.18 A C
ANISOU 1240 CB GLU A 162 12566 3071 6470 2295 3015 -912 A C
ATOM 1241 CG GLU A 162 4.270 0.134 12.458 1.00 66.44 A C
ANISOU 1241 CG GLU A 162 13112 4459 7672 2191 2784 -968 A C
ATOM 1242 CD GLU A 162 4.003 0.441 10.993 1.00 82.58 A C
ANISOU 1242 CD GLU A 162 15016 6561 9799 1802 2776 -1009 A C
ATOM 1243 OE1 GLU A 162 3.403 -0.409 10.292 1.00 56.82 A O
ANISOU 1243 OE1 GLU A 162 12035 3098 6456 1576 2948 -1027 A O
ATOM 1244 OE2 GLU A 162 4.407 1.542 10.546 1.00 72.69 A O1-
ANISOU 1244 OE2 GLU A 162 13368 5566 8685 1722 2612 -1030 A O1-
ATOM 1245 N LEU A 163 1.025 0.974 13.887 1.00 54.20 A N
ANISOU 1245 N LEU A 163 11581 2706 6305 1555 2740 -810 A N
ATOM 1246 CA LEU A 163 0.728 2.176 14.641 1.00 51.94 A C
ANISOU 1246 CA LEU A 163 10972 2594 6168 1530 2562 -777 A C
ATOM 1247 C LEU A 163 -0.691 2.173 15.202 1.00 54.50 A C
ANISOU 1247 C LEU A 163 11404 2785 6519 1288 2607 -708 A C
ATOM 1248 O LEU A 163 -1.601 1.520 14.673 1.00 53.52 A O
ANISOU 1248 O LEU A 163 11489 2506 6341 1002 2742 -700 A O
ATOM 1249 CB LEU A 163 0.976 3.434 13.786 1.00 49.99 A C
ANISOU 1249 CB LEU A 163 10292 2599 6104 1343 2408 -798 A C
ATOM 1250 CG LEU A 163 2.420 3.664 13.288 1.00 55.02 A C
ANISOU 1250 CG LEU A 163 10744 3415 6744 1561 2346 -882 A C
ATOM 1251 CD1 LEU A 163 2.497 4.896 12.384 1.00 54.40 A C
ANISOU 1251 CD1 LEU A 163 10279 3535 6855 1326 2245 -883 A C
ATOM 1252 CD2 LEU A 163 3.411 3.828 14.445 1.00 56.54 A C
ANISOU 1252 CD2 LEU A 163 10846 3741 6895 1958 2270 -942 A C
ATOM 1253 N MET A 164 -0.835 2.878 16.328 1.00 51.05 A N
ANISOU 1253 N MET A 164 10816 2428 6153 1406 2502 -679 A N
ATOM 1254 CA MET A 164 -2.081 3.106 17.048 1.00 50.66 A C
ANISOU 1254 CA MET A 164 10802 2299 6149 1223 2515 -614 A C
ATOM 1255 C MET A 164 -2.669 4.439 16.557 1.00 50.08 A C
ANISOU 1255 C MET A 164 10334 2412 6283 937 2383 -584 A C
ATOM 1256 O MET A 164 -1.902 5.367 16.270 1.00 49.21 A O
ANISOU 1256 O MET A 164 9912 2490 6296 1006 2265 -619 A O
ATOM 1257 CB MET A 164 -1.782 3.130 18.572 1.00 54.73 A C
ANISOU 1257 CB MET A 164 11378 2813 6605 1557 2486 -603 A C
ATOM 1258 CG MET A 164 -3.000 3.412 19.490 1.00 59.31 A C
ANISOU 1258 CG MET A 164 11984 3319 7231 1407 2495 -538 A C
ATOM 1259 SD MET A 164 -4.162 2.036 19.446 1.00 66.60 A S
ANISOU 1259 SD MET A 164 13381 3912 8013 1189 2746 -484 A S
ATOM 1260 CE MET A 164 -5.364 2.610 20.475 1.00 62.14 A C
ANISOU 1260 CE MET A 164 12746 3344 7520 1056 2715 -422 A C
ATOM 1261 N ALA A 165 -4.011 4.518 16.427 1.00 44.09 A N
ANISOU 1261 N ALA A 165 9590 1606 5555 622 2425 -518 A N
ATOM 1262 CA ALA A 165 -4.765 5.728 16.070 1.00 41.59 A C
ANISOU 1262 CA ALA A 165 8930 1457 5415 383 2332 -448 A C
ATOM 1263 C ALA A 165 -5.834 6.019 17.130 1.00 42.44 A C
ANISOU 1263 C ALA A 165 9049 1513 5562 317 2337 -388 A C
ATOM 1264 O ALA A 165 -6.482 5.086 17.596 1.00 39.59 A O
ANISOU 1264 O ALA A 165 8985 986 5072 266 2451 -388 A O
ATOM 1265 CB ALA A 165 -5.410 5.580 14.708 1.00 42.26 A C
ANISOU 1265 CB ALA A 165 8962 1623 5472 62 2374 -414 A C
ATOM 1266 N LEU A 166 -6.006 7.306 17.525 1.00 37.94 A N
ANISOU 1266 N LEU A 166 8168 1074 5175 318 2240 -344 A N
ATOM 1267 CA LEU A 166 -7.030 7.691 18.511 1.00 37.29 A C
ANISOU 1267 CA LEU A 166 8013 1058 5097 246 2243 -271 A C
ATOM 1268 C LEU A 166 -7.767 8.930 18.062 1.00 38.54 A C
ANISOU 1268 C LEU A 166 7891 1262 5491 70 2202 -184 A C
ATOM 1269 O LEU A 166 -7.158 9.815 17.467 1.00 38.81 A O
ANISOU 1269 O LEU A 166 7677 1407 5662 100 2154 -175 A O
ATOM 1270 CB LEU A 166 -6.457 7.903 19.934 1.00 37.29 A C
ANISOU 1270 CB LEU A 166 7999 1099 5071 511 2198 -315 A C
ATOM 1271 CG LEU A 166 -5.858 6.681 20.660 1.00 42.67 A C
ANISOU 1271 CG LEU A 166 9116 1465 5631 803 2262 -412 A C
ATOM 1272 CD1 LEU A 166 -4.985 7.116 21.811 1.00 42.33 A C
ANISOU 1272 CD1 LEU A 166 8975 1518 5590 1119 2181 -495 A C
ATOM 1273 CD2 LEU A 166 -6.934 5.756 21.157 1.00 46.14 A C
ANISOU 1273 CD2 LEU A 166 9870 1719 5944 698 2391 -355 A C
ATOM 1274 N MET A 167 -9.081 9.010 18.371 1.00 34.43 A N
ANISOU 1274 N MET A 167 7226 1023 4832 -104 2240 -92 A N
ATOM 1275 CA MET A 167 -9.895 10.187 18.018 1.00 32.29 A C
ANISOU 1275 CA MET A 167 6585 1024 4660 -214 2220 11 A C
ATOM 1276 C MET A 167 -10.700 10.703 19.233 1.00 34.14 A C
ANISOU 1276 C MET A 167 6842 1091 5039 -204 2232 52 A C
ATOM 1277 O MET A 167 -10.789 10.031 20.265 1.00 33.25 A O
ANISOU 1277 O MET A 167 6849 1060 4723 -129 2256 -10 A O
ATOM 1278 CB MET A 167 -10.827 9.884 16.824 1.00 33.57 A C
ANISOU 1278 CB MET A 167 6816 1094 4847 -489 2254 101 A C
ATOM 1279 CG MET A 167 -10.086 9.815 15.503 1.00 35.92 A C
ANISOU 1279 CG MET A 167 7112 1347 5190 -542 2239 119 A C
ATOM 1280 SD MET A 167 -11.043 10.069 13.983 1.00 39.67 A S
ANISOU 1280 SD MET A 167 7349 2134 5589 -810 2252 263 A S
ATOM 1281 CE MET A 167 -11.421 11.816 14.116 1.00 34.41 A C
ANISOU 1281 CE MET A 167 6317 1586 5170 -710 2237 468 A C
ATOM 1282 N SER A 168 -11.277 11.912 19.118 1.00 32.08 A N
ANISOU 1282 N SER A 168 6216 1104 4869 -222 2230 134 A N
ATOM 1283 CA SER A 168 -12.083 12.515 20.188 1.00 31.16 A C
ANISOU 1283 CA SER A 168 5970 1084 4784 -191 2254 154 A C
ATOM 1284 C SER A 168 -13.486 11.854 20.216 1.00 34.96 A C
ANISOU 1284 C SER A 168 6738 1226 5319 -431 2300 269 A C
ATOM 1285 O SER A 168 -14.533 12.508 20.092 1.00 34.82 A O
ANISOU 1285 O SER A 168 6537 1314 5378 -523 2325 395 A O
ATOM 1286 CB SER A 168 -12.168 14.025 20.005 1.00 32.47 A C
ANISOU 1286 CB SER A 168 5916 1138 5283 -169 2281 269 A C
ATOM 1287 OG SER A 168 -12.537 14.378 18.683 1.00 38.15 A O
ANISOU 1287 OG SER A 168 6656 1631 6207 -331 2308 495 A O
ATOM 1288 N ALA A 169 -13.470 10.533 20.393 1.00 33.55 A N
ANISOU 1288 N ALA A 169 6755 1159 4833 -449 2325 141 A N
ATOM 1289 CA ALA A 169 -14.625 9.656 20.390 1.00 33.77 A C
ANISOU 1289 CA ALA A 169 6942 1178 4712 -661 2395 138 A C
ATOM 1290 C ALA A 169 -14.318 8.339 21.111 1.00 38.38 A C
ANISOU 1290 C ALA A 169 8104 1165 5313 -713 2484 97 A C
ATOM 1291 O ALA A 169 -13.161 8.054 21.453 1.00 38.46 A O
ANISOU 1291 O ALA A 169 8240 1091 5284 -473 2461 15 A O
ATOM 1292 CB ALA A 169 -15.018 9.374 18.945 1.00 34.29 A C
ANISOU 1292 CB ALA A 169 6980 1297 4752 -913 2405 192 A C
ATOM 1293 N LEU A 170 -15.355 7.514 21.305 1.00 36.31 A N
ANISOU 1293 N LEU A 170 7889 1126 4782 -866 2586 31 A N
ATOM 1294 CA LEU A 170 -15.188 6.210 21.909 1.00 37.12 A C
ANISOU 1294 CA LEU A 170 8380 1029 4694 -843 2718 -59 A C
ATOM 1295 C LEU A 170 -14.648 5.259 20.852 1.00 41.61 A C
ANISOU 1295 C LEU A 170 9284 1232 5293 -1004 2794 -101 A C
ATOM 1296 O LEU A 170 -15.064 5.345 19.698 1.00 40.72 A O
ANISOU 1296 O LEU A 170 8998 1320 5153 -1247 2783 -100 A O
ATOM 1297 CB LEU A 170 -16.516 5.670 22.495 1.00 37.46 A C
ANISOU 1297 CB LEU A 170 8554 1038 4639 -1059 2850 -77 A C
ATOM 1298 CG LEU A 170 -17.267 6.507 23.526 1.00 39.69 A C
ANISOU 1298 CG LEU A 170 8799 1121 5158 -1082 2819 45 A C
ATOM 1299 CD1 LEU A 170 -18.544 5.809 23.953 1.00 39.27 A C
ANISOU 1299 CD1 LEU A 170 8865 1106 4949 -1320 2970 0 A C
ATOM 1300 CD2 LEU A 170 -16.425 6.776 24.753 1.00 44.05 A C
ANISOU 1300 CD2 LEU A 170 9487 1450 5800 -745 2774 52 A C
ATOM 1301 N ARG A 171 -13.715 4.378 21.231 1.00 40.32 A N
ANISOU 1301 N ARG A 171 9405 932 4984 -777 2870 -172 A N
ATOM 1302 CA ARG A 171 -13.159 3.371 20.331 1.00 42.15 A C
ANISOU 1302 CA ARG A 171 9923 948 5144 -853 2976 -255 A C
ATOM 1303 C ARG A 171 -14.280 2.430 19.921 1.00 47.01 A C
ANISOU 1303 C ARG A 171 10722 1518 5620 -1249 3174 -332 A C
ATOM 1304 O ARG A 171 -15.075 2.064 20.787 1.00 47.61 A O
ANISOU 1304 O ARG A 171 10964 1473 5652 -1335 3295 -332 A O
ATOM 1305 CB ARG A 171 -12.021 2.587 21.025 1.00 47.25 A C
ANISOU 1305 CB ARG A 171 10918 1326 5708 -493 3052 -284 A C
ATOM 1306 CG ARG A 171 -10.813 3.466 21.392 1.00 61.35 A C
ANISOU 1306 CG ARG A 171 12493 3217 7602 -123 2858 -256 A C
ATOM 1307 CD ARG A 171 -9.922 2.732 22.380 1.00 72.35 A C
ANISOU 1307 CD ARG A 171 14196 4417 8878 265 2928 -264 A C
ATOM 1308 NE ARG A 171 -9.624 3.502 23.594 1.00 77.05 A N
ANISOU 1308 NE ARG A 171 14647 5097 9532 529 2806 -232 A N
ATOM 1309 CZ ARG A 171 -10.410 3.561 24.664 1.00 90.77 A C
ANISOU 1309 CZ ARG A 171 16467 6770 11250 519 2857 -189 A C
ATOM 1310 NH1 ARG A 171 -11.582 2.939 24.673 1.00 82.43 A N1+
ANISOU 1310 NH1 ARG A 171 15624 5566 10129 244 3029 -170 A N1+
ATOM 1311 NH2 ARG A 171 -10.036 4.251 25.727 1.00 79.61 A N
ANISOU 1311 NH2 ARG A 171 14912 5459 9876 766 2747 -184 A N
ATOM 1312 N ASP A 172 -14.397 2.085 18.616 1.00 43.73 A N
ANISOU 1312 N ASP A 172 10254 1229 5133 -1515 3214 -412 A N
ATOM 1313 CA ASP A 172 -15.476 1.210 18.153 1.00 46.26 A C
ANISOU 1313 CA ASP A 172 10709 1561 5307 -1947 3412 -534 A C
ATOM 1314 C ASP A 172 -14.932 0.012 17.366 1.00 53.25 A C
ANISOU 1314 C ASP A 172 11919 2258 6057 -2052 3605 -686 A C
ATOM 1315 O ASP A 172 -15.633 -0.550 16.518 1.00 54.43 A O
ANISOU 1315 O ASP A 172 12074 2522 6086 -2455 3735 -827 A O
ATOM 1316 CB ASP A 172 -16.542 1.994 17.339 1.00 47.93 A C
ANISOU 1316 CB ASP A 172 10473 2213 5523 -2263 3297 -508 A C
ATOM 1317 CG ASP A 172 -17.823 1.205 17.063 1.00 58.54 A C
ANISOU 1317 CG ASP A 172 11885 3652 6706 -2734 3489 -652 A C
ATOM 1318 OD1 ASP A 172 -18.329 0.544 17.989 1.00 58.48 A O
ANISOU 1318 OD1 ASP A 172 12151 3410 6660 -2808 3664 -698 A O
ATOM 1319 OD2 ASP A 172 -18.285 1.214 15.915 1.00 67.26 A O1-
ANISOU 1319 OD2 ASP A 172 12772 5074 7708 -3033 3479 -731 A O1-
ATOM 1320 N GLY A 173 -13.704 -0.396 17.683 1.00 50.95 A N
ANISOU 1320 N GLY A 173 11895 1692 5770 -1690 3639 -670 A N
ATOM 1321 CA GLY A 173 -13.079 -1.552 17.057 1.00 52.78 A C
ANISOU 1321 CA GLY A 173 12481 1691 5884 -1718 3850 -797 A C
ATOM 1322 C GLY A 173 -12.124 -1.296 15.910 1.00 57.23 A C
ANISOU 1322 C GLY A 173 12870 2411 6463 -1637 3722 -820 A C
ATOM 1323 O GLY A 173 -12.118 -0.225 15.293 1.00 56.11 A O
ANISOU 1323 O GLY A 173 12296 2614 6409 -1665 3483 -754 A O
ATOM 1324 N GLU A 174 -11.308 -2.312 15.639 1.00 55.11 A N
ANISOU 1324 N GLU A 174 12965 1869 6106 -1521 3911 -905 A N
ATOM 1325 CA GLU A 174 -10.306 -2.370 14.589 1.00 56.04 A C
ANISOU 1325 CA GLU A 174 13028 2056 6209 -1429 3859 -953 A C
ATOM 1326 C GLU A 174 -10.852 -3.207 13.442 1.00 64.96 A C
ANISOU 1326 C GLU A 174 14274 3205 7204 -1882 4065 -1152 A C
ATOM 1327 O GLU A 174 -11.606 -4.154 13.671 1.00 66.60 A O
ANISOU 1327 O GLU A 174 14806 3185 7313 -2148 4350 -1275 A O
ATOM 1328 CB GLU A 174 -8.976 -2.953 15.113 1.00 57.97 A C
ANISOU 1328 CB GLU A 174 13599 1995 6430 -949 3944 -912 A C
ATOM 1329 CG GLU A 174 -8.402 -2.212 16.317 1.00 67.22 A C
ANISOU 1329 CG GLU A 174 14661 3185 7696 -503 3758 -751 A C
ATOM 1330 CD GLU A 174 -7.146 -2.797 16.946 1.00 89.17 A C
ANISOU 1330 CD GLU A 174 17731 5737 10411 4 3837 -701 A C
ATOM 1331 OE1 GLU A 174 -6.485 -3.638 16.292 1.00 83.28 A O
ANISOU 1331 OE1 GLU A 174 17229 4835 9578 75 4000 -770 A O
ATOM 1332 OE2 GLU A 174 -6.810 -2.397 18.085 1.00 80.36 A O1-
ANISOU 1332 OE2 GLU A 174 16581 4631 9322 347 3736 -593 A O1-
ATOM 1333 N LEU A 175 -10.493 -2.827 12.211 1.00 62.88 A N
ANISOU 1333 N LEU A 175 13734 3226 6931 -1988 3933 -1195 A N
ATOM 1334 CA LEU A 175 -10.920 -3.473 10.967 1.00 65.30 A C
ANISOU 1334 CA LEU A 175 14066 3652 7094 -2422 4086 -1400 A C
ATOM 1335 C LEU A 175 -9.701 -3.758 10.077 1.00 67.75 A C
ANISOU 1335 C LEU A 175 14444 3922 7375 -2256 4096 -1453 A C
ATOM 1336 O LEU A 175 -8.684 -3.071 10.173 1.00 63.98 A O
ANISOU 1336 O LEU A 175 13801 3503 7004 -1873 3889 -1313 A O
ATOM 1337 CB LEU A 175 -11.925 -2.532 10.250 1.00 64.76 A C
ANISOU 1337 CB LEU A 175 13487 4108 7010 -2759 3884 -1382 A C
ATOM 1338 CG LEU A 175 -12.944 -3.137 9.272 1.00 71.96 A C
ANISOU 1338 CG LEU A 175 14358 5252 7731 -3321 4046 -1613 A C
ATOM 1339 CD1 LEU A 175 -13.873 -4.142 9.968 1.00 74.74 A C
ANISOU 1339 CD1 LEU A 175 15043 5351 8004 -3620 4341 -1767 A C
ATOM 1340 CD2 LEU A 175 -13.794 -2.042 8.646 1.00 72.26 A C
ANISOU 1340 CD2 LEU A 175 13832 5881 7742 -3517 3798 -1530 A C
ATOM 1341 N SER A 176 -9.795 -4.782 9.237 1.00 67.82 A N
ANISOU 1341 N SER A 176 14701 3826 7239 -2554 4355 -1675 A N
ATOM 1342 CA SER A 176 -8.717 -5.157 8.317 1.00 68.37 A C
ANISOU 1342 CA SER A 176 14861 3853 7265 -2439 4402 -1753 A C
ATOM 1343 C SER A 176 -8.903 -4.445 6.985 1.00 72.92 A C
ANISOU 1343 C SER A 176 14981 4934 7789 -2700 4202 -1793 A C
ATOM 1344 O SER A 176 -10.007 -4.470 6.428 1.00 73.93 A O
ANISOU 1344 O SER A 176 14939 5346 7804 -3157 4235 -1918 A O
ATOM 1345 CB SER A 176 -8.685 -6.670 8.106 1.00 74.46 A C
ANISOU 1345 CB SER A 176 16168 4218 7906 -2617 4826 -1981 A C
ATOM 1346 OG SER A 176 -9.906 -7.135 7.552 1.00 84.01 A O
ANISOU 1346 OG SER A 176 17372 5564 8984 -3210 5004 -2213 A O
ATOM 1347 N GLU A 177 -7.841 -3.774 6.494 1.00 67.95 A N
ANISOU 1347 N GLU A 177 14134 4453 7232 -2403 3997 -1683 A N
ATOM 1348 CA GLU A 177 -7.879 -3.123 5.197 1.00 66.53 A C
ANISOU 1348 CA GLU A 177 13551 4732 6996 -2595 3830 -1695 A C
ATOM 1349 C GLU A 177 -7.587 -4.221 4.201 1.00 73.24 A C
ANISOU 1349 C GLU A 177 14656 5494 7680 -2822 4074 -1945 A C
ATOM 1350 O GLU A 177 -6.463 -4.720 4.154 1.00 72.20 A O
ANISOU 1350 O GLU A 177 14777 5087 7569 -2542 4169 -1969 A O
ATOM 1351 CB GLU A 177 -6.887 -1.943 5.116 1.00 64.61 A C
ANISOU 1351 CB GLU A 177 12982 4659 6909 -2205 3545 -1479 A C
ATOM 1352 CG GLU A 177 -6.940 -1.214 3.785 1.00 71.92 A C
ANISOU 1352 CG GLU A 177 13493 6057 7775 -2376 3389 -1452 A C
ATOM 1353 CD GLU A 177 -6.938 0.300 3.861 1.00 86.02 A C
ANISOU 1353 CD GLU A 177 14831 8135 9717 -2190 3112 -1198 A C
ATOM 1354 OE1 GLU A 177 -5.898 0.914 3.528 1.00 80.45 A O
ANISOU 1354 OE1 GLU A 177 13987 7466 9114 -1917 2996 -1102 A O
ATOM 1355 OE2 GLU A 177 -8.000 0.875 4.183 1.00 72.73 A O1-
ANISOU 1355 OE2 GLU A 177 12929 6656 8047 -2334 3032 -1101 A O1-
ATOM 1356 N GLN A 178 -8.623 -4.662 3.478 1.00 74.20 A N
ANISOU 1356 N GLN A 178 14728 5841 7625 -3335 4202 -2152 A N
ATOM 1357 CA GLN A 178 -8.537 -5.756 2.507 1.00 78.05 A C
ANISOU 1357 CA GLN A 178 15452 6272 7932 -3652 4473 -2448 A C
ATOM 1358 C GLN A 178 -7.684 -5.376 1.289 1.00 82.58 A C
ANISOU 1358 C GLN A 178 15786 7131 8459 -3568 4333 -2439 A C
ATOM 1359 O GLN A 178 -7.113 -6.266 0.654 1.00 84.35 A O
ANISOU 1359 O GLN A 178 16282 7176 8591 -3636 4551 -2638 A O
ATOM 1360 CB GLN A 178 -9.940 -6.202 2.061 1.00 82.24 A C
ANISOU 1360 CB GLN A 178 15904 7075 8269 -4262 4619 -2692 A C
ATOM 1361 CG GLN A 178 -10.243 -7.672 2.356 1.00107.20 A C
ANISOU 1361 CG GLN A 178 19609 9783 11339 -4559 5069 -2998 A C
ATOM 1362 CD GLN A 178 -10.571 -7.927 3.811 1.00128.53 A C
ANISOU 1362 CD GLN A 178 22648 12027 14162 -4411 5215 -2911 A C
ATOM 1363 NE2 GLN A 178 -9.652 -8.560 4.528 1.00122.41 A N
ANISOU 1363 NE2 GLN A 178 22392 10659 13459 -4102 5469 -2904 A N
ATOM 1364 OE1 GLN A 178 -11.651 -7.583 4.302 1.00123.50 A O
ANISOU 1364 OE1 GLN A 178 21816 11569 13538 -4564 5119 -2847 A O
ATOM 1365 N SER A 179 -7.587 -4.064 0.982 1.00 77.01 A N
ANISOU 1365 N SER A 179 14592 6844 7823 -3413 3996 -2206 A N
ATOM 1366 CA SER A 179 -6.798 -3.524 -0.137 1.00 76.31 A C
ANISOU 1366 CA SER A 179 14229 7059 7705 -3308 3842 -2149 A C
ATOM 1367 C SER A 179 -5.299 -3.431 0.198 1.00 77.40 A C
ANISOU 1367 C SER A 179 14522 6878 8010 -2807 3801 -2031 A C
ATOM 1368 O SER A 179 -4.466 -3.679 -0.677 1.00 77.03 A O
ANISOU 1368 O SER A 179 14489 6876 7904 -2756 3834 -2106 A O
ATOM 1369 CB SER A 179 -7.316 -2.147 -0.541 1.00 79.32 A C
ANISOU 1369 CB SER A 179 14058 7977 8104 -3318 3545 -1922 A C
ATOM 1370 OG SER A 179 -8.666 -2.208 -0.971 1.00 93.88 A O
ANISOU 1370 OG SER A 179 15694 10232 9745 -3768 3568 -2035 A O
ATOM 1371 N ASP A 180 -4.955 -3.052 1.449 1.00 72.09 A N
ANISOU 1371 N ASP A 180 13937 5926 7527 -2441 3724 -1856 A N
ATOM 1372 CA ASP A 180 -3.559 -2.926 1.878 1.00 70.37 A C
ANISOU 1372 CA ASP A 180 13827 5465 7447 -1956 3675 -1755 A C
ATOM 1373 C ASP A 180 -3.314 -3.685 3.187 1.00 74.61 A C
ANISOU 1373 C ASP A 180 14793 5517 8040 -1699 3841 -1758 A C
ATOM 1374 O ASP A 180 -3.761 -3.263 4.256 1.00 74.43 A O
ANISOU 1374 O ASP A 180 14742 5427 8113 -1608 3764 -1636 A O
ATOM 1375 CB ASP A 180 -3.138 -1.450 2.004 1.00 68.89 A C
ANISOU 1375 CB ASP A 180 13205 5537 7432 -1695 3369 -1510 A C
ATOM 1376 CG ASP A 180 -1.644 -1.196 1.895 1.00 77.08 A C
ANISOU 1376 CG ASP A 180 14217 6505 8563 -1302 3301 -1459 A C
ATOM 1377 OD1 ASP A 180 -0.858 -2.085 2.279 1.00 77.14 A O
ANISOU 1377 OD1 ASP A 180 14576 6188 8546 -1076 3458 -1548 A O
ATOM 1378 OD2 ASP A 180 -1.261 -0.091 1.455 1.00 86.38 A O1-
ANISOU 1378 OD2 ASP A 180 15024 7956 9839 -1207 3106 -1323 A O1-
ATOM 1379 N SER A 181 -2.574 -4.802 3.081 1.00 71.80 A N
ANISOU 1379 N SER A 181 14836 4830 7614 -1561 4085 -1888 A N
ATOM 1380 CA SER A 181 -2.182 -5.718 4.163 1.00 71.27 A C
ANISOU 1380 CA SER A 181 15241 4281 7558 -1264 4309 -1886 A C
ATOM 1381 C SER A 181 -1.245 -5.036 5.161 1.00 70.02 A C
ANISOU 1381 C SER A 181 14976 4090 7540 -722 4110 -1676 A C
ATOM 1382 O SER A 181 -1.191 -5.443 6.325 1.00 69.85 A O
ANISOU 1382 O SER A 181 15233 3773 7534 -458 4215 -1609 A O
ATOM 1383 CB SER A 181 -1.509 -6.953 3.576 1.00 75.70 A C
ANISOU 1383 CB SER A 181 16216 4548 8000 -1236 4630 -2065 A C
ATOM 1384 OG SER A 181 -2.313 -7.462 2.527 1.00 85.64 A O
ANISOU 1384 OG SER A 181 17500 5916 9121 -1775 4791 -2296 A O
ATOM 1385 N ASN A 182 -0.516 -3.993 4.692 1.00 62.48 A N
ANISOU 1385 N ASN A 182 13610 3456 6674 -569 3839 -1584 A N
ATOM 1386 CA ASN A 182 0.370 -3.149 5.498 1.00 59.35 A C
ANISOU 1386 CA ASN A 182 13012 3126 6411 -125 3626 -1425 A C
ATOM 1387 C ASN A 182 -0.433 -2.160 6.336 1.00 56.41 A C
ANISOU 1387 C ASN A 182 12382 2887 6163 -177 3431 -1291 A C
ATOM 1388 O ASN A 182 0.177 -1.379 7.070 1.00 52.86 A O
ANISOU 1388 O ASN A 182 11739 2515 5831 137 3257 -1183 A O
ATOM 1389 CB ASN A 182 1.361 -2.358 4.609 1.00 58.80 A C
ANISOU 1389 CB ASN A 182 12595 3349 6399 -11 3448 -1406 A C
ATOM 1390 CG ASN A 182 2.468 -3.162 3.963 1.00 78.83 A C
ANISOU 1390 CG ASN A 182 15338 5775 8838 175 3600 -1511 A C
ATOM 1391 ND2 ASN A 182 2.964 -2.674 2.829 1.00 64.03 A N
ANISOU 1391 ND2 ASN A 182 13198 4162 6968 82 3507 -1542 A N
ATOM 1392 OD1 ASN A 182 2.945 -4.171 4.501 1.00 75.85 A O
ANISOU 1392 OD1 ASN A 182 15346 5088 8384 442 3802 -1546 A O
ATOM 1393 N ARG A 183 -1.790 -2.189 6.234 1.00 52.20 A N
ANISOU 1393 N ARG A 183 11833 2401 5598 -578 3468 -1313 A N
ATOM 1394 CA ARG A 183 -2.638 -1.233 6.929 1.00 50.59 A C
ANISOU 1394 CA ARG A 183 11371 2344 5508 -654 3297 -1184 A C
ATOM 1395 C ARG A 183 -3.758 -1.816 7.811 1.00 56.59 A C
ANISOU 1395 C ARG A 183 12387 2893 6221 -820 3441 -1203 A C
ATOM 1396 O ARG A 183 -4.322 -2.877 7.534 1.00 58.93 A O
ANISOU 1396 O ARG A 183 12995 3013 6383 -1078 3685 -1346 A O
ATOM 1397 CB ARG A 183 -3.259 -0.258 5.915 1.00 50.24 A C
ANISOU 1397 CB ARG A 183 10899 2699 5493 -958 3135 -1136 A C
ATOM 1398 CG ARG A 183 -2.285 0.856 5.528 1.00 50.32 A C
ANISOU 1398 CG ARG A 183 10560 2930 5630 -738 2939 -1036 A C
ATOM 1399 CD ARG A 183 -2.726 1.673 4.342 1.00 52.83 A C
ANISOU 1399 CD ARG A 183 10509 3621 5941 -998 2834 -974 A C
ATOM 1400 NE ARG A 183 -1.779 2.763 4.094 1.00 57.86 A N
ANISOU 1400 NE ARG A 183 10837 4419 6730 -776 2681 -863 A N
ATOM 1401 CZ ARG A 183 -1.855 3.969 4.648 1.00 62.28 A C
ANISOU 1401 CZ ARG A 183 11127 5064 7471 -661 2544 -714 A C
ATOM 1402 NH1 ARG A 183 -2.845 4.264 5.479 1.00 46.54 A N1+
ANISOU 1402 NH1 ARG A 183 9123 3032 5529 -727 2519 -644 A N1+
ATOM 1403 NH2 ARG A 183 -0.939 4.887 4.380 1.00 52.52 A N
ANISOU 1403 NH2 ARG A 183 9638 3944 6373 -490 2453 -646 A N
ATOM 1404 N LYS A 184 -4.117 -1.034 8.850 1.00 50.51 A N
ANISOU 1404 N LYS A 184 11460 2161 5570 -702 3296 -1070 A N
ATOM 1405 CA LYS A 184 -5.195 -1.315 9.803 1.00 49.95 A C
ANISOU 1405 CA LYS A 184 11554 1939 5484 -834 3388 -1054 A C
ATOM 1406 C LYS A 184 -6.217 -0.183 9.718 1.00 50.48 A C
ANISOU 1406 C LYS A 184 11216 2325 5640 -1070 3201 -959 A C
ATOM 1407 O LYS A 184 -5.858 0.909 9.277 1.00 47.83 A O
ANISOU 1407 O LYS A 184 10508 2250 5415 -989 2997 -862 A O
ATOM 1408 CB LYS A 184 -4.615 -1.421 11.229 1.00 51.73 A C
ANISOU 1408 CB LYS A 184 11977 1922 5755 -407 3395 -970 A C
ATOM 1409 CG LYS A 184 -5.408 -2.311 12.166 1.00 65.87 A C
ANISOU 1409 CG LYS A 184 14150 3408 7468 -473 3617 -989 A C
ATOM 1410 CD LYS A 184 -4.930 -2.216 13.614 1.00 75.73 A C
ANISOU 1410 CD LYS A 184 15517 4505 8752 -37 3583 -873 A C
ATOM 1411 CE LYS A 184 -3.646 -2.954 13.923 1.00 92.65 A C
ANISOU 1411 CE LYS A 184 17944 6447 10811 417 3693 -866 A C
ATOM 1412 NZ LYS A 184 -3.114 -2.605 15.267 1.00100.63 A N1+
ANISOU 1412 NZ LYS A 184 18939 7456 11839 858 3592 -749 A N1+
ATOM 1413 N ILE A 185 -7.474 -0.432 10.132 1.00 46.23 A N
ANISOU 1413 N ILE A 185 10749 1763 5052 -1352 3290 -981 A N
ATOM 1414 CA ILE A 185 -8.539 0.577 10.147 1.00 44.07 A C
ANISOU 1414 CA ILE A 185 10106 1793 4844 -1555 3137 -879 A C
ATOM 1415 C ILE A 185 -9.138 0.665 11.557 1.00 47.36 A C
ANISOU 1415 C ILE A 185 10629 2041 5326 -1466 3153 -809 A C
ATOM 1416 O ILE A 185 -9.806 -0.271 11.999 1.00 48.60 A O
ANISOU 1416 O ILE A 185 11092 1993 5382 -1641 3354 -901 A O
ATOM 1417 CB ILE A 185 -9.631 0.288 9.074 1.00 48.05 A C
ANISOU 1417 CB ILE A 185 10490 2571 5195 -2035 3208 -984 A C
ATOM 1418 CG1 ILE A 185 -9.074 0.492 7.659 1.00 47.95 A C
ANISOU 1418 CG1 ILE A 185 10278 2817 5123 -2101 3145 -1017 A C
ATOM 1419 CG2 ILE A 185 -10.915 1.138 9.318 1.00 47.77 A C
ANISOU 1419 CG2 ILE A 185 10122 2834 5194 -2223 3093 -872 A C
ATOM 1420 CD1 ILE A 185 -9.894 -0.169 6.579 1.00 59.72 A C
ANISOU 1420 CD1 ILE A 185 11756 4533 6401 -2559 3274 -1195 A C
ATOM 1421 N TYR A 186 -8.894 1.774 12.262 1.00 41.66 A N
ANISOU 1421 N TYR A 186 9664 1396 4770 -1211 2964 -660 A N
ATOM 1422 CA TYR A 186 -9.472 1.990 13.594 1.00 40.75 A C
ANISOU 1422 CA TYR A 186 9600 1164 4719 -1123 2958 -590 A C
ATOM 1423 C TYR A 186 -10.810 2.694 13.422 1.00 44.33 A C
ANISOU 1423 C TYR A 186 9755 1890 5200 -1418 2893 -521 A C
ATOM 1424 O TYR A 186 -10.966 3.482 12.494 1.00 44.95 A O
ANISOU 1424 O TYR A 186 9489 2277 5314 -1522 2775 -456 A O
ATOM 1425 CB TYR A 186 -8.519 2.787 14.506 1.00 40.16 A C
ANISOU 1425 CB TYR A 186 9419 1045 4794 -709 2808 -500 A C
ATOM 1426 CG TYR A 186 -7.272 2.029 14.913 1.00 42.08 A C
ANISOU 1426 CG TYR A 186 9961 1052 4975 -369 2880 -557 A C
ATOM 1427 CD1 TYR A 186 -7.223 1.321 16.112 1.00 45.26 A C
ANISOU 1427 CD1 TYR A 186 10693 1196 5309 -164 2996 -556 A C
ATOM 1428 CD2 TYR A 186 -6.152 1.982 14.078 1.00 41.25 A C
ANISOU 1428 CD2 TYR A 186 9813 999 4861 -234 2845 -602 A C
ATOM 1429 CE1 TYR A 186 -6.091 0.584 16.473 1.00 46.58 A C
ANISOU 1429 CE1 TYR A 186 11133 1177 5387 194 3078 -582 A C
ATOM 1430 CE2 TYR A 186 -4.997 1.297 14.456 1.00 42.17 A C
ANISOU 1430 CE2 TYR A 186 10182 937 4904 112 2912 -643 A C
ATOM 1431 CZ TYR A 186 -4.973 0.598 15.657 1.00 50.65 A C
ANISOU 1431 CZ TYR A 186 11576 1771 5897 340 3029 -626 A C
ATOM 1432 OH TYR A 186 -3.853 -0.107 16.034 1.00 50.75 A O
ANISOU 1432 OH TYR A 186 11836 1637 5808 726 3110 -641 A O
ATOM 1433 N ARG A 187 -11.795 2.363 14.245 1.00 41.92 A N
ANISOU 1433 N ARG A 187 9584 1489 4856 -1555 2989 -532 A N
ATOM 1434 CA ARG A 187 -13.125 2.964 14.134 1.00 41.13 A C
ANISOU 1434 CA ARG A 187 9201 1667 4758 -1829 2943 -472 A C
ATOM 1435 C ARG A 187 -13.510 3.602 15.432 1.00 42.95 A C
ANISOU 1435 C ARG A 187 9376 1826 5117 -1660 2881 -361 A C
ATOM 1436 O ARG A 187 -13.118 3.124 16.504 1.00 41.93 A O
ANISOU 1436 O ARG A 187 9540 1396 4995 -1455 2952 -382 A O
ATOM 1437 CB ARG A 187 -14.189 1.958 13.711 1.00 43.48 A C
ANISOU 1437 CB ARG A 187 9657 1998 4864 -2254 3137 -627 A C
ATOM 1438 CG ARG A 187 -13.873 1.206 12.432 1.00 48.98 A C
ANISOU 1438 CG ARG A 187 10443 2756 5410 -2469 3237 -785 A C
ATOM 1439 CD ARG A 187 -14.638 -0.093 12.417 1.00 61.01 A C
ANISOU 1439 CD ARG A 187 12282 4139 6758 -2844 3511 -995 A C
ATOM 1440 NE ARG A 187 -15.977 0.083 11.860 1.00 72.85 A N
ANISOU 1440 NE ARG A 187 13482 6057 8140 -3266 3505 -1054 A N
ATOM 1441 CZ ARG A 187 -16.831 -0.908 11.628 1.00 94.14 A C
ANISOU 1441 CZ ARG A 187 16340 8766 10661 -3699 3736 -1278 A C
ATOM 1442 NH1 ARG A 187 -16.503 -2.161 11.925 1.00 88.03 A N1+
ANISOU 1442 NH1 ARG A 187 16070 7546 9831 -3767 4022 -1450 A N1+
ATOM 1443 NH2 ARG A 187 -18.020 -0.656 11.105 1.00 81.08 A N
ANISOU 1443 NH2 ARG A 187 14346 7581 8880 -4066 3704 -1334 A N
ATOM 1444 N PHE A 188 -14.242 4.732 15.323 1.00 37.52 A N
ANISOU 1444 N PHE A 188 8304 1430 4525 -1716 2753 -229 A N
ATOM 1445 CA PHE A 188 -14.630 5.582 16.439 1.00 35.00 A C
ANISOU 1445 CA PHE A 188 7790 1238 4269 -1493 2671 -155 A C
ATOM 1446 C PHE A 188 -16.049 6.093 16.305 1.00 39.75 A C
ANISOU 1446 C PHE A 188 8191 1980 4934 -1803 2674 -32 A C
ATOM 1447 O PHE A 188 -16.500 6.408 15.200 1.00 39.33 A O
ANISOU 1447 O PHE A 188 7874 2255 4814 -1985 2638 8 A O
ATOM 1448 CB PHE A 188 -13.664 6.777 16.538 1.00 33.43 A C
ANISOU 1448 CB PHE A 188 7325 1144 4235 -1158 2517 -66 A C
ATOM 1449 CG PHE A 188 -12.211 6.379 16.590 1.00 33.18 A C
ANISOU 1449 CG PHE A 188 7451 984 4171 -914 2514 -133 A C
ATOM 1450 CD1 PHE A 188 -11.596 6.101 17.801 1.00 34.54 A C
ANISOU 1450 CD1 PHE A 188 7862 883 4377 -690 2537 -151 A C
ATOM 1451 CD2 PHE A 188 -11.464 6.259 15.423 1.00 34.80 A C
ANISOU 1451 CD2 PHE A 188 7716 1048 4458 -982 2496 -134 A C
ATOM 1452 CE1 PHE A 188 -10.268 5.679 17.843 1.00 35.46 A C
ANISOU 1452 CE1 PHE A 188 8153 845 4477 -460 2533 -204 A C
ATOM 1453 CE2 PHE A 188 -10.134 5.847 15.464 1.00 36.90 A C
ANISOU 1453 CE2 PHE A 188 8195 1068 4757 -764 2497 -205 A C
ATOM 1454 CZ PHE A 188 -9.547 5.547 16.673 1.00 35.02 A C
ANISOU 1454 CZ PHE A 188 8052 849 4403 -478 2514 -236 A C
ATOM 1455 N LYS A 189 -16.731 6.221 17.456 1.00 37.66 A N
ANISOU 1455 N LYS A 189 7972 1621 4715 -1780 2704 0 A N
ATOM 1456 CA LYS A 189 -18.101 6.718 17.529 1.00 38.41 A C
ANISOU 1456 CA LYS A 189 7815 1983 4795 -1974 2704 81 A C
ATOM 1457 C LYS A 189 -18.215 7.892 18.476 1.00 41.44 A C
ANISOU 1457 C LYS A 189 8020 2345 5378 -1733 2622 227 A C
ATOM 1458 O LYS A 189 -17.783 7.821 19.634 1.00 41.08 A O
ANISOU 1458 O LYS A 189 8178 2022 5407 -1540 2637 197 A O
ATOM 1459 CB LYS A 189 -19.092 5.612 17.927 1.00 43.02 A C
ANISOU 1459 CB LYS A 189 8634 2504 5207 -2279 2874 -56 A C
ATOM 1460 CG LYS A 189 -18.669 4.770 19.128 1.00 55.10 A C
ANISOU 1460 CG LYS A 189 10606 3598 6731 -2150 2996 -143 A C
ATOM 1461 CD LYS A 189 -19.632 3.648 19.408 1.00 59.38 A C
ANISOU 1461 CD LYS A 189 11400 4052 7108 -2479 3211 -280 A C
ATOM 1462 CE LYS A 189 -19.346 2.969 20.735 1.00 68.11 A C
ANISOU 1462 CE LYS A 189 12934 4734 8212 -2304 3350 -312 A C
ATOM 1463 NZ LYS A 189 -18.096 2.158 20.718 1.00 70.71 A N1+
ANISOU 1463 NZ LYS A 189 13629 4745 8493 -2116 3436 -381 A N1+
ATOM 1464 N GLN A 190 -18.785 8.987 17.968 1.00 37.60 A N
ANISOU 1464 N GLN A 190 7151 2166 4971 -1731 2549 388 A N
ATOM 1465 CA GLN A 190 -19.071 10.173 18.754 1.00 35.71 A C
ANISOU 1465 CA GLN A 190 6716 1929 4923 -1538 2509 532 A C
ATOM 1466 C GLN A 190 -20.558 10.504 18.556 1.00 42.07 A C
ANISOU 1466 C GLN A 190 7256 3074 5655 -1724 2537 640 A C
ATOM 1467 O GLN A 190 -20.936 11.150 17.569 1.00 41.06 A O
ANISOU 1467 O GLN A 190 6812 3282 5507 -1747 2500 782 A O
ATOM 1468 CB GLN A 190 -18.139 11.344 18.405 1.00 34.37 A C
ANISOU 1468 CB GLN A 190 6348 1753 4959 -1277 2434 648 A C
ATOM 1469 CG GLN A 190 -18.349 12.605 19.276 1.00 31.42 A C
ANISOU 1469 CG GLN A 190 5721 1483 4733 -969 2390 656 A C
ATOM 1470 CD GLN A 190 -18.351 12.325 20.771 1.00 43.31 A C
ANISOU 1470 CD GLN A 190 7527 2576 6352 -1005 2462 664 A C
ATOM 1471 NE2 GLN A 190 -17.213 12.515 21.433 1.00 29.30 A N
ANISOU 1471 NE2 GLN A 190 5582 1151 4401 -555 2369 321 A N
ATOM 1472 OE1 GLN A 190 -19.375 11.945 21.349 1.00 40.40 A O
ANISOU 1472 OE1 GLN A 190 7208 2245 5899 -1137 2511 659 A O
ATOM 1473 N ASN A 191 -21.391 10.024 19.497 1.00 39.40 A N
ANISOU 1473 N ASN A 191 7047 2667 5257 -1846 2610 575 A N
ATOM 1474 CA ASN A 191 -22.851 10.113 19.472 1.00 40.75 A C
ANISOU 1474 CA ASN A 191 7001 3158 5325 -2055 2653 632 A C
ATOM 1475 C ASN A 191 -23.376 11.343 20.199 1.00 45.62 A C
ANISOU 1475 C ASN A 191 7387 3826 6122 -1850 2634 812 A C
ATOM 1476 O ASN A 191 -24.597 11.565 20.256 1.00 47.03 A O
ANISOU 1476 O ASN A 191 7350 4288 6230 -1971 2668 886 A O
ATOM 1477 CB ASN A 191 -23.452 8.832 20.079 1.00 42.18 A C
ANISOU 1477 CB ASN A 191 7474 3214 5338 -2330 2778 441 A C
ATOM 1478 CG ASN A 191 -23.223 7.595 19.243 1.00 56.79 A C
ANISOU 1478 CG ASN A 191 9528 5063 6986 -2603 2853 252 A C
ATOM 1479 ND2 ASN A 191 -22.962 6.472 19.897 1.00 49.56 A N
ANISOU 1479 ND2 ASN A 191 9031 3794 6006 -2689 2986 85 A N
ATOM 1480 OD1 ASN A 191 -23.294 7.624 18.014 1.00 50.31 A O
ANISOU 1480 OD1 ASN A 191 8500 4559 6059 -2736 2813 256 A O
ATOM 1481 N VAL A 192 -22.463 12.140 20.765 1.00 40.53 A N
ANISOU 1481 N VAL A 192 6778 2918 5704 -1550 2596 867 A N
ATOM 1482 CA VAL A 192 -22.821 13.396 21.403 1.00 39.60 A C
ANISOU 1482 CA VAL A 192 6455 2806 5786 -1346 2609 1023 A C
ATOM 1483 C VAL A 192 -22.482 14.491 20.398 1.00 45.13 A C
ANISOU 1483 C VAL A 192 6869 3672 6607 -1181 2583 1213 A C
ATOM 1484 O VAL A 192 -21.346 14.505 19.913 1.00 45.53 A O
ANISOU 1484 O VAL A 192 6996 3587 6718 -1090 2543 1171 A O
ATOM 1485 CB VAL A 192 -22.131 13.610 22.778 1.00 41.31 A C
ANISOU 1485 CB VAL A 192 6886 2643 6167 -1151 2619 931 A C
ATOM 1486 CG1 VAL A 192 -22.520 14.957 23.384 1.00 40.77 A C
ANISOU 1486 CG1 VAL A 192 6600 2576 6312 -964 2661 1072 A C
ATOM 1487 CG2 VAL A 192 -22.444 12.465 23.742 1.00 41.13 A C
ANISOU 1487 CG2 VAL A 192 7172 2456 6000 -1287 2665 771 A C
ATOM 1488 N PRO A 193 -23.422 15.395 20.026 1.00 42.57 A N
ANISOU 1488 N PRO A 193 6219 3649 6309 -1126 2621 1434 A N
ATOM 1489 CA PRO A 193 -23.075 16.445 19.054 1.00 41.63 A C
ANISOU 1489 CA PRO A 193 5854 3665 6299 -936 2634 1646 A C
ATOM 1490 C PRO A 193 -21.935 17.313 19.557 1.00 40.51 A C
ANISOU 1490 C PRO A 193 5800 3147 6446 -694 2671 1636 A C
ATOM 1491 O PRO A 193 -21.942 17.744 20.702 1.00 38.36 A O
ANISOU 1491 O PRO A 193 5603 2639 6334 -596 2722 1588 A O
ATOM 1492 CB PRO A 193 -24.382 17.239 18.902 1.00 45.18 A C
ANISOU 1492 CB PRO A 193 5977 4460 6728 -870 2700 1892 A C
ATOM 1493 CG PRO A 193 -25.446 16.318 19.339 1.00 50.45 A C
ANISOU 1493 CG PRO A 193 6672 5315 7179 -1128 2683 1775 A C
ATOM 1494 CD PRO A 193 -24.829 15.521 20.452 1.00 44.75 A C
ANISOU 1494 CD PRO A 193 6330 4168 6506 -1209 2670 1516 A C
ATOM 1495 N ILE A 194 -20.927 17.505 18.709 1.00 35.73 A N
ANISOU 1495 N ILE A 194 5190 2496 5889 -624 2651 1648 A N
ATOM 1496 CA ILE A 194 -19.757 18.319 19.007 1.00 33.82 A C
ANISOU 1496 CA ILE A 194 4963 2006 5878 -366 2662 1531 A C
ATOM 1497 C ILE A 194 -19.558 19.394 17.930 1.00 38.43 A C
ANISOU 1497 C ILE A 194 5358 2636 6607 -277 2790 1850 A C
ATOM 1498 O ILE A 194 -19.908 19.164 16.766 1.00 39.14 A O
ANISOU 1498 O ILE A 194 5306 3044 6521 -332 2757 1988 A O
ATOM 1499 CB ILE A 194 -18.448 17.452 19.105 1.00 34.40 A C
ANISOU 1499 CB ILE A 194 5315 1834 5922 -448 2591 1315 A C
ATOM 1500 CG1 ILE A 194 -18.058 16.779 17.760 1.00 34.56 A C
ANISOU 1500 CG1 ILE A 194 5349 1998 5783 -576 2535 1350 A C
ATOM 1501 CG2 ILE A 194 -18.431 16.499 20.270 1.00 33.41 A C
ANISOU 1501 CG2 ILE A 194 5412 1613 5670 -486 2523 1048 A C
ATOM 1502 CD1 ILE A 194 -16.570 16.614 17.571 1.00 38.83 A C
ANISOU 1502 CD1 ILE A 194 6030 2321 6400 -509 2502 1206 A C
ATOM 1503 N PRO A 195 -18.844 20.490 18.260 1.00 34.30 A N
ANISOU 1503 N PRO A 195 4762 1937 6334 -20 2872 1774 A N
ATOM 1504 CA PRO A 195 -18.468 21.449 17.216 1.00 35.12 A C
ANISOU 1504 CA PRO A 195 4714 2061 6571 109 3000 2008 A C
ATOM 1505 C PRO A 195 -17.190 20.948 16.513 1.00 39.36 A C
ANISOU 1505 C PRO A 195 5397 2468 7092 -6 2952 1941 A C
ATOM 1506 O PRO A 195 -16.489 20.098 17.067 1.00 38.06 A O
ANISOU 1506 O PRO A 195 5435 2152 6873 -104 2835 1669 A O
ATOM 1507 CB PRO A 195 -18.245 22.734 17.996 1.00 36.49 A C
ANISOU 1507 CB PRO A 195 4877 1916 7072 256 3218 2063 A C
ATOM 1508 CG PRO A 195 -17.863 22.280 19.364 1.00 38.84 A C
ANISOU 1508 CG PRO A 195 5403 1919 7434 141 3166 1808 A C
ATOM 1509 CD PRO A 195 -18.358 20.912 19.591 1.00 34.73 A C
ANISOU 1509 CD PRO A 195 4930 1681 6585 39 2940 1594 A C
ATOM 1510 N SER A 196 -16.878 21.467 15.325 1.00 35.86 A N
ANISOU 1510 N SER A 196 4805 2161 6660 95 3014 2107 A N
ATOM 1511 CA SER A 196 -15.728 21.046 14.508 1.00 35.41 A C
ANISOU 1511 CA SER A 196 4812 2089 6554 51 2947 1996 A C
ATOM 1512 C SER A 196 -14.407 21.255 15.205 1.00 38.54 A C
ANISOU 1512 C SER A 196 5371 2105 7168 56 2986 1767 A C
ATOM 1513 O SER A 196 -13.488 20.524 14.934 1.00 37.03 A O
ANISOU 1513 O SER A 196 5293 1887 6888 -15 2876 1583 A O
ATOM 1514 CB SER A 196 -15.702 21.813 13.189 1.00 41.34 A C
ANISOU 1514 CB SER A 196 5386 2995 7327 153 3078 2314 A C
ATOM 1515 OG SER A 196 -15.645 23.212 13.430 1.00 50.94 A O
ANISOU 1515 OG SER A 196 6519 4004 8832 347 3319 2483 A O
ATOM 1516 N TYR A 197 -14.281 22.259 16.077 1.00 36.61 A N
ANISOU 1516 N TYR A 197 5097 1637 7177 168 3136 1718 A N
ATOM 1517 CA TYR A 197 -12.993 22.499 16.723 1.00 36.03 A C
ANISOU 1517 CA TYR A 197 5070 1379 7240 198 3161 1395 A C
ATOM 1518 C TYR A 197 -12.619 21.380 17.696 1.00 37.18 A C
ANISOU 1518 C TYR A 197 5472 1353 7300 71 2981 1157 A C
ATOM 1519 O TYR A 197 -11.454 21.273 18.084 1.00 35.59 A O
ANISOU 1519 O TYR A 197 5262 1179 7081 102 2946 860 A O
ATOM 1520 CB TYR A 197 -12.952 23.882 17.411 1.00 37.57 A C
ANISOU 1520 CB TYR A 197 5212 1301 7763 281 3415 1424 A C
ATOM 1521 CG TYR A 197 -13.705 23.999 18.724 1.00 38.48 A C
ANISOU 1521 CG TYR A 197 5399 1270 7953 268 3435 1379 A C
ATOM 1522 CD1 TYR A 197 -13.074 23.743 19.939 1.00 38.68 A C
ANISOU 1522 CD1 TYR A 197 5536 1152 8011 216 3371 1053 A C
ATOM 1523 CD2 TYR A 197 -15.012 24.488 18.760 1.00 39.41 A C
ANISOU 1523 CD2 TYR A 197 5444 1420 8109 333 3541 1666 A C
ATOM 1524 CE1 TYR A 197 -13.731 23.945 21.153 1.00 38.68 A C
ANISOU 1524 CE1 TYR A 197 5542 1116 8040 229 3404 973 A C
ATOM 1525 CE2 TYR A 197 -15.677 24.689 19.968 1.00 39.42 A C
ANISOU 1525 CE2 TYR A 197 5476 1328 8175 342 3579 1597 A C
ATOM 1526 CZ TYR A 197 -15.047 24.382 21.161 1.00 45.56 A C
ANISOU 1526 CZ TYR A 197 6384 1943 8985 274 3506 1262 A C
ATOM 1527 OH TYR A 197 -15.726 24.523 22.351 1.00 44.65 A O
ANISOU 1527 OH TYR A 197 6301 1756 8909 280 3537 1193 A O
ATOM 1528 N LEU A 198 -13.590 20.519 18.049 1.00 35.92 A N
ANISOU 1528 N LEU A 198 5360 1372 6915 15 2857 1161 A N
ATOM 1529 CA LEU A 198 -13.378 19.437 19.003 1.00 35.00 A C
ANISOU 1529 CA LEU A 198 5413 1268 6618 -29 2709 899 A C
ATOM 1530 C LEU A 198 -13.064 18.094 18.324 1.00 39.77 A C
ANISOU 1530 C LEU A 198 6222 1868 7022 -152 2568 874 A C
ATOM 1531 O LEU A 198 -12.916 17.067 19.002 1.00 37.73 A O
ANISOU 1531 O LEU A 198 6168 1554 6615 -184 2473 704 A O
ATOM 1532 CB LEU A 198 -14.584 19.328 19.945 1.00 35.34 A C
ANISOU 1532 CB LEU A 198 5492 1312 6624 -59 2712 943 A C
ATOM 1533 CG LEU A 198 -14.681 20.408 21.042 1.00 38.82 A C
ANISOU 1533 CG LEU A 198 5932 1466 7352 4 2849 940 A C
ATOM 1534 CD1 LEU A 198 -15.847 20.111 21.994 1.00 39.43 A C
ANISOU 1534 CD1 LEU A 198 6062 1571 7348 -33 2832 963 A C
ATOM 1535 CD2 LEU A 198 -13.405 20.484 21.858 1.00 36.83 A C
ANISOU 1535 CD2 LEU A 198 5751 1066 7176 57 2832 642 A C
ATOM 1536 N ILE A 199 -12.918 18.114 16.996 1.00 38.49 A N
ANISOU 1536 N ILE A 199 5962 1855 6807 -182 2573 1004 A N
ATOM 1537 CA ILE A 199 -12.501 16.952 16.238 1.00 38.51 A C
ANISOU 1537 CA ILE A 199 6088 1955 6588 -274 2464 924 A C
ATOM 1538 C ILE A 199 -10.967 16.838 16.447 1.00 38.95 A C
ANISOU 1538 C ILE A 199 6241 1845 6712 -182 2433 706 A C
ATOM 1539 O ILE A 199 -10.250 17.849 16.324 1.00 38.37 A O
ANISOU 1539 O ILE A 199 6036 1696 6845 -95 2517 705 A O
ATOM 1540 CB ILE A 199 -12.939 17.106 14.756 1.00 43.80 A C
ANISOU 1540 CB ILE A 199 6588 2889 7165 -336 2485 1141 A C
ATOM 1541 CG1 ILE A 199 -14.297 16.418 14.548 1.00 45.72 A C
ANISOU 1541 CG1 ILE A 199 6808 3376 7187 -490 2447 1237 A C
ATOM 1542 CG2 ILE A 199 -11.881 16.547 13.775 1.00 45.90 A C
ANISOU 1542 CG2 ILE A 199 6918 3192 7329 -365 2429 1049 A C
ATOM 1543 CD1 ILE A 199 -14.850 16.449 13.100 1.00 56.47 A C
ANISOU 1543 CD1 ILE A 199 7974 5095 8387 -564 2450 1432 A C
ATOM 1544 N ALA A 200 -10.486 15.635 16.807 1.00 32.41 A N
ANISOU 1544 N ALA A 200 5540 1161 5612 -158 2329 471 A N
ATOM 1545 CA ALA A 200 -9.065 15.380 17.045 1.00 31.65 A C
ANISOU 1545 CA ALA A 200 5469 1089 5466 -51 2290 270 A C
ATOM 1546 C ALA A 200 -8.643 14.001 16.576 1.00 35.40 A C
ANISOU 1546 C ALA A 200 6323 1262 5866 -109 2219 224 A C
ATOM 1547 O ALA A 200 -9.425 13.050 16.621 1.00 33.38 A O
ANISOU 1547 O ALA A 200 6159 1167 5356 -197 2204 221 A O
ATOM 1548 CB ALA A 200 -8.741 15.522 18.515 1.00 32.10 A C
ANISOU 1548 CB ALA A 200 5567 1066 5564 41 2282 131 A C
ATOM 1549 N LEU A 201 -7.368 13.897 16.193 1.00 33.56 A N
ANISOU 1549 N LEU A 201 6038 1126 5586 -12 2195 104 A N
ATOM 1550 CA LEU A 201 -6.735 12.681 15.713 1.00 33.41 A C
ANISOU 1550 CA LEU A 201 6214 1120 5362 1 2150 11 A C
ATOM 1551 C LEU A 201 -5.252 12.626 16.116 1.00 37.30 A C
ANISOU 1551 C LEU A 201 6786 1454 5934 201 2114 -176 A C
ATOM 1552 O LEU A 201 -4.530 13.597 15.928 1.00 36.03 A O
ANISOU 1552 O LEU A 201 6414 1334 5943 247 2134 -212 A O
ATOM 1553 CB LEU A 201 -6.858 12.619 14.164 1.00 33.15 A C
ANISOU 1553 CB LEU A 201 6136 1145 5315 -134 2168 122 A C
ATOM 1554 CG LEU A 201 -6.116 11.471 13.435 1.00 36.93 A C
ANISOU 1554 CG LEU A 201 6813 1595 5622 -136 2147 21 A C
ATOM 1555 CD1 LEU A 201 -6.611 10.076 13.891 1.00 35.92 A C
ANISOU 1555 CD1 LEU A 201 7004 1365 5279 -193 2161 -52 A C
ATOM 1556 CD2 LEU A 201 -6.215 11.625 11.937 1.00 37.33 A C
ANISOU 1556 CD2 LEU A 201 6727 1821 5636 -268 2166 127 A C
ATOM 1557 N VAL A 202 -4.818 11.467 16.644 1.00 36.38 A N
ANISOU 1557 N VAL A 202 6923 1269 5630 322 2080 -291 A N
ATOM 1558 CA VAL A 202 -3.426 11.138 16.981 1.00 37.09 A C
ANISOU 1558 CA VAL A 202 7053 1375 5663 549 2040 -461 A C
ATOM 1559 C VAL A 202 -3.115 9.766 16.372 1.00 40.06 A C
ANISOU 1559 C VAL A 202 7697 1704 5819 587 2055 -481 A C
ATOM 1560 O VAL A 202 -3.920 8.848 16.521 1.00 40.56 A O
ANISOU 1560 O VAL A 202 8012 1659 5741 514 2102 -433 A O
ATOM 1561 CB VAL A 202 -3.048 11.210 18.494 1.00 41.12 A C
ANISOU 1561 CB VAL A 202 7588 1875 6159 755 2004 -588 A C
ATOM 1562 CG1 VAL A 202 -3.863 10.245 19.339 1.00 41.49 A C
ANISOU 1562 CG1 VAL A 202 7922 1799 6042 787 2023 -543 A C
ATOM 1563 CG2 VAL A 202 -1.552 10.970 18.715 1.00 41.35 A C
ANISOU 1563 CG2 VAL A 202 7592 2012 6109 1002 1955 -764 A C
ATOM 1564 N VAL A 203 -1.975 9.658 15.649 1.00 35.13 A N
ANISOU 1564 N VAL A 203 6987 1215 5146 664 2036 -539 A N
ATOM 1565 CA VAL A 203 -1.472 8.421 15.044 1.00 35.22 A C
ANISOU 1565 CA VAL A 203 7227 1205 4949 725 2067 -565 A C
ATOM 1566 C VAL A 203 0.035 8.312 15.365 1.00 42.98 A C
ANISOU 1566 C VAL A 203 8212 2191 5928 1049 2031 -744 A C
ATOM 1567 O VAL A 203 0.831 9.137 14.918 1.00 45.12 A O
ANISOU 1567 O VAL A 203 8216 2604 6325 1057 1995 -806 A O
ATOM 1568 CB VAL A 203 -1.752 8.288 13.520 1.00 37.32 A C
ANISOU 1568 CB VAL A 203 7508 1432 5240 523 2112 -525 A C
ATOM 1569 CG1 VAL A 203 -1.224 6.944 12.980 1.00 38.52 A C
ANISOU 1569 CG1 VAL A 203 7946 1504 5186 593 2176 -592 A C
ATOM 1570 CG2 VAL A 203 -3.235 8.442 13.199 1.00 35.86 A C
ANISOU 1570 CG2 VAL A 203 7305 1249 5071 240 2143 -388 A C
ATOM 1571 N GLY A 204 0.404 7.290 16.128 1.00 40.22 A N
ANISOU 1571 N GLY A 204 8122 1770 5391 1296 2052 -793 A N
ATOM 1572 CA GLY A 204 1.790 7.059 16.513 1.00 41.81 A C
ANISOU 1572 CA GLY A 204 8287 2102 5496 1626 2013 -920 A C
ATOM 1573 C GLY A 204 1.992 5.779 17.291 1.00 49.79 A C
ANISOU 1573 C GLY A 204 9646 3007 6266 1924 2075 -912 A C
ATOM 1574 O GLY A 204 1.049 5.005 17.474 1.00 49.37 A O
ANISOU 1574 O GLY A 204 9895 2732 6130 1841 2172 -817 A O
ATOM 1575 N ALA A 205 3.240 5.532 17.733 1.00 49.68 A N
ANISOU 1575 N ALA A 205 9590 3161 6126 2281 2039 -1009 A N
ATOM 1576 CA ALA A 205 3.561 4.354 18.547 1.00 51.97 A C
ANISOU 1576 CA ALA A 205 10202 3380 6165 2651 2114 -975 A C
ATOM 1577 C ALA A 205 3.147 4.659 19.988 1.00 56.44 A C
ANISOU 1577 C ALA A 205 10739 4003 6702 2769 2065 -970 A C
ATOM 1578 O ALA A 205 3.935 5.207 20.769 1.00 58.05 A O
ANISOU 1578 O ALA A 205 10689 4496 6873 2989 1958 -1085 A O
ATOM 1579 CB ALA A 205 5.046 4.016 18.445 1.00 54.67 A C
ANISOU 1579 CB ALA A 205 10474 3939 6361 3019 2091 -1064 A C
ATOM 1580 N LEU A 206 1.870 4.381 20.306 1.00 51.09 A N
ANISOU 1580 N LEU A 206 10291 3078 6043 2582 2143 -856 A N
ATOM 1581 CA LEU A 206 1.298 4.715 21.604 1.00 50.97 A C
ANISOU 1581 CA LEU A 206 10256 3091 6018 2638 2107 -840 A C
ATOM 1582 C LEU A 206 1.065 3.506 22.490 1.00 56.11 A C
ANISOU 1582 C LEU A 206 11321 3569 6430 2919 2240 -733 A C
ATOM 1583 O LEU A 206 0.744 2.426 22.014 1.00 54.83 A O
ANISOU 1583 O LEU A 206 11527 3132 6173 2900 2410 -641 A O
ATOM 1584 CB LEU A 206 -0.037 5.488 21.436 1.00 48.68 A C
ANISOU 1584 CB LEU A 206 9867 2685 5946 2216 2097 -790 A C
ATOM 1585 CG LEU A 206 -0.009 6.784 20.608 1.00 50.79 A C
ANISOU 1585 CG LEU A 206 9746 3084 6467 1934 2006 -850 A C
ATOM 1586 CD1 LEU A 206 -1.411 7.298 20.361 1.00 48.99 A C
ANISOU 1586 CD1 LEU A 206 9492 2723 6401 1570 2035 -747 A C
ATOM 1587 CD2 LEU A 206 0.821 7.857 21.277 1.00 52.60 A C
ANISOU 1587 CD2 LEU A 206 9617 3586 6781 2057 1893 -1005 A C
ATOM 1588 N GLU A 207 1.194 3.730 23.806 1.00 56.05 A N
ANISOU 1588 N GLU A 207 11249 3723 6326 3167 2182 -751 A N
ATOM 1589 CA GLU A 207 0.952 2.753 24.868 1.00 58.54 A C
ANISOU 1589 CA GLU A 207 11922 3913 6407 3472 2306 -632 A C
ATOM 1590 C GLU A 207 0.042 3.411 25.908 1.00 62.53 A C
ANISOU 1590 C GLU A 207 12341 4438 6982 3340 2256 -625 A C
ATOM 1591 O GLU A 207 0.189 4.606 26.190 1.00 61.62 A O
ANISOU 1591 O GLU A 207 11833 4571 7009 3230 2097 -755 A O
ATOM 1592 CB GLU A 207 2.271 2.261 25.489 1.00 62.65 A C
ANISOU 1592 CB GLU A 207 12439 4702 6663 4026 2284 -651 A C
ATOM 1593 CG GLU A 207 3.130 1.421 24.557 1.00 77.21 A C
ANISOU 1593 CG GLU A 207 14454 6482 8400 4222 2382 -622 A C
ATOM 1594 CD GLU A 207 2.986 -0.085 24.676 1.00105.30 A C
ANISOU 1594 CD GLU A 207 18568 9692 11748 4476 2649 -438 A C
ATOM 1595 OE1 GLU A 207 3.232 -0.627 25.779 1.00106.33 A O
ANISOU 1595 OE1 GLU A 207 18880 9875 11645 4896 2721 -335 A O
ATOM 1596 OE2 GLU A 207 2.698 -0.731 23.642 1.00 94.93 A O1-
ANISOU 1596 OE2 GLU A 207 17508 8067 10493 4271 2805 -403 A O1-
ATOM 1597 N GLY A 208 -0.960 2.660 26.356 1.00 59.64 A N
ANISOU 1597 N GLY A 208 12343 3776 6540 3297 2418 -485 A N
ATOM 1598 CA GLY A 208 -1.949 3.118 27.317 1.00 58.92 A C
ANISOU 1598 CA GLY A 208 12231 3658 6500 3164 2405 -458 A C
ATOM 1599 C GLY A 208 -2.245 2.138 28.427 1.00 67.17 A C
ANISOU 1599 C GLY A 208 13656 4566 7301 3467 2561 -322 A C
ATOM 1600 O GLY A 208 -2.357 0.929 28.187 1.00 67.14 A O
ANISOU 1600 O GLY A 208 14077 4275 7159 3576 2777 -201 A O
ATOM 1601 N ARG A 209 -2.393 2.668 29.655 1.00 66.46 A N
ANISOU 1601 N ARG A 209 13425 4669 7157 3598 2477 -345 A N
ATOM 1602 CA ARG A 209 -2.729 1.878 30.839 1.00 69.40 A C
ANISOU 1602 CA ARG A 209 14126 4950 7293 3893 2618 -207 A C
ATOM 1603 C ARG A 209 -3.805 2.578 31.657 1.00 71.11 A C
ANISOU 1603 C ARG A 209 14241 5163 7615 3656 2580 -218 A C
ATOM 1604 O ARG A 209 -3.782 3.804 31.787 1.00 68.45 A O
ANISOU 1604 O ARG A 209 13492 5065 7450 3479 2394 -367 A O
ATOM 1605 CB ARG A 209 -1.488 1.597 31.705 1.00 75.70 A C
ANISOU 1605 CB ARG A 209 14868 6097 7799 4476 2560 -209 A C
ATOM 1606 CG ARG A 209 -1.602 0.303 32.513 1.00 91.37 A C
ANISOU 1606 CG ARG A 209 17337 7898 9482 4887 2795 10 A C
ATOM 1607 CD ARG A 209 -0.681 0.291 33.721 1.00109.09 A C
ANISOU 1607 CD ARG A 209 19446 10586 11419 5446 2703 15 A C
ATOM 1608 NE ARG A 209 -1.215 -0.538 34.808 1.00121.28 A N
ANISOU 1608 NE ARG A 209 21386 11974 12722 5741 2907 227 A N
ATOM 1609 CZ ARG A 209 -0.570 -1.554 35.378 1.00133.78 A C
ANISOU 1609 CZ ARG A 209 23271 13591 13969 6320 3069 416 A C
ATOM 1610 NH1 ARG A 209 0.653 -1.884 34.978 1.00123.89 A N1+
ANISOU 1610 NH1 ARG A 209 21952 12547 12572 6682 3040 413 A N1+
ATOM 1611 NH2 ARG A 209 -1.140 -2.242 36.357 1.00117.63 A N
ANISOU 1611 NH2 ARG A 209 21593 11379 11721 6562 3276 622 A N
ATOM 1612 N LYS A 210 -4.764 1.780 32.178 1.00 69.18 A N
ANISOU 1612 N LYS A 210 14389 4621 7274 3641 2786 -65 A N
ATOM 1613 CA LYS A 210 -5.899 2.186 33.015 1.00 68.41 A C
ANISOU 1613 CA LYS A 210 14285 4468 7239 3442 2803 -42 A C
ATOM 1614 C LYS A 210 -5.402 2.876 34.301 1.00 73.47 A C
ANISOU 1614 C LYS A 210 14662 5495 7759 3739 2645 -119 A C
ATOM 1615 O LYS A 210 -4.491 2.372 34.950 1.00 76.22 A O
ANISOU 1615 O LYS A 210 15085 6039 7835 4214 2649 -80 A O
ATOM 1616 CB LYS A 210 -6.769 0.946 33.347 1.00 72.45 A C
ANISOU 1616 CB LYS A 210 15330 4585 7613 3447 3102 142 A C
ATOM 1617 CG LYS A 210 -7.977 1.241 34.236 1.00 86.28 A C
ANISOU 1617 CG LYS A 210 17108 6260 9414 3236 3149 176 A C
ATOM 1618 CD LYS A 210 -8.950 0.066 34.373 1.00 96.88 A C
ANISOU 1618 CD LYS A 210 18968 7181 10662 3137 3474 330 A C
ATOM 1619 CE LYS A 210 -9.960 0.300 35.479 1.00102.57 A C
ANISOU 1619 CE LYS A 210 19717 7879 11374 3032 3522 373 A C
ATOM 1620 NZ LYS A 210 -11.217 -0.472 35.281 1.00106.18 A N1+
ANISOU 1620 NZ LYS A 210 20539 7940 11863 2685 3806 448 A N1+
ATOM 1621 N VAL A 211 -5.974 4.044 34.634 1.00 68.49 A N
ANISOU 1621 N VAL A 211 13705 4997 7322 3464 2512 -236 A N
ATOM 1622 CA VAL A 211 -5.638 4.847 35.826 1.00 68.79 A C
ANISOU 1622 CA VAL A 211 13454 5403 7281 3649 2371 -359 A C
ATOM 1623 C VAL A 211 -6.978 5.216 36.547 1.00 70.89 A C
ANISOU 1623 C VAL A 211 13763 5530 7641 3401 2431 -320 A C
ATOM 1624 O VAL A 211 -7.002 6.000 37.507 1.00 70.64 A O
ANISOU 1624 O VAL A 211 13504 5751 7583 3462 2338 -429 A O
ATOM 1625 CB VAL A 211 -4.754 6.096 35.462 1.00 71.87 A C
ANISOU 1625 CB VAL A 211 13332 6139 7836 3564 2154 -607 A C
ATOM 1626 CG1 VAL A 211 -4.299 6.862 36.706 1.00 72.95 A C
ANISOU 1626 CG1 VAL A 211 13170 6695 7855 3760 2029 -782 A C
ATOM 1627 CG2 VAL A 211 -3.530 5.693 34.636 1.00 72.49 A C
ANISOU 1627 CG2 VAL A 211 13376 6323 7842 3759 2111 -639 A C
ATOM 1628 N GLY A 212 -8.065 4.590 36.096 1.00 65.06 A N
ANISOU 1628 N GLY A 212 13322 4410 6989 3127 2600 -176 A N
ATOM 1629 CA GLY A 212 -9.407 4.800 36.627 1.00 63.45 A C
ANISOU 1629 CA GLY A 212 13186 4049 6873 2865 2683 -122 A C
ATOM 1630 C GLY A 212 -10.453 4.018 35.856 1.00 64.38 A C
ANISOU 1630 C GLY A 212 13620 3779 7063 2547 2881 7 A C
ATOM 1631 O GLY A 212 -10.185 3.597 34.732 1.00 61.97 A O
ANISOU 1631 O GLY A 212 13396 3344 6807 2446 2918 19 A O
ATOM 1632 N PRO A 213 -11.687 3.861 36.402 1.00 61.54 A N
ANISOU 1632 N PRO A 213 13415 3251 6716 2350 3014 83 A N
ATOM 1633 CA PRO A 213 -12.727 3.075 35.697 1.00 60.79 A C
ANISOU 1633 CA PRO A 213 13607 2820 6668 2008 3224 171 A C
ATOM 1634 C PRO A 213 -13.119 3.610 34.306 1.00 60.59 A C
ANISOU 1634 C PRO A 213 13339 2791 6892 1592 3145 103 A C
ATOM 1635 O PRO A 213 -13.758 2.905 33.537 1.00 59.15 A O
ANISOU 1635 O PRO A 213 13361 2390 6721 1316 3305 139 A O
ATOM 1636 CB PRO A 213 -13.922 3.128 36.661 1.00 62.89 A C
ANISOU 1636 CB PRO A 213 13963 3011 6920 1873 3332 224 A C
ATOM 1637 CG PRO A 213 -13.657 4.300 37.550 1.00 66.95 A C
ANISOU 1637 CG PRO A 213 14121 3836 7481 2020 3129 135 A C
ATOM 1638 CD PRO A 213 -12.172 4.321 37.717 1.00 63.37 A C
ANISOU 1638 CD PRO A 213 13579 3606 6894 2430 2996 78 A C
ATOM 1639 N ARG A 214 -12.707 4.830 33.965 1.00 56.54 A N
ANISOU 1639 N ARG A 214 12395 2526 6562 1554 2921 0 A N
ATOM 1640 CA ARG A 214 -13.027 5.435 32.664 1.00 54.18 A C
ANISOU 1640 CA ARG A 214 11837 2261 6488 1214 2843 -39 A C
ATOM 1641 C ARG A 214 -11.858 6.308 32.161 1.00 56.26 A C
ANISOU 1641 C ARG A 214 11768 2746 6863 1347 2647 -144 A C
ATOM 1642 O ARG A 214 -12.067 7.203 31.342 1.00 56.54 A O
ANISOU 1642 O ARG A 214 11502 2867 7112 1118 2559 -177 A O
ATOM 1643 CB ARG A 214 -14.345 6.235 32.766 1.00 51.58 A C
ANISOU 1643 CB ARG A 214 11299 1969 6331 892 2838 -23 A C
ATOM 1644 CG ARG A 214 -14.518 6.969 34.091 1.00 58.58 A C
ANISOU 1644 CG ARG A 214 12047 2979 7232 1038 2781 -55 A C
ATOM 1645 CD ARG A 214 -15.874 7.621 34.198 1.00 62.35 A C
ANISOU 1645 CD ARG A 214 12385 3455 7849 742 2821 -16 A C
ATOM 1646 NE ARG A 214 -15.963 8.469 35.383 1.00 62.42 A N
ANISOU 1646 NE ARG A 214 12224 3593 7901 872 2762 -70 A N
ATOM 1647 CZ ARG A 214 -17.085 9.026 35.824 1.00 73.02 A C
ANISOU 1647 CZ ARG A 214 13447 4951 9347 694 2800 -43 A C
ATOM 1648 NH1 ARG A 214 -18.236 8.806 35.199 1.00 57.14 A N1+
ANISOU 1648 NH1 ARG A 214 11452 2867 7391 384 2891 43 A N1+
ATOM 1649 NH2 ARG A 214 -17.069 9.794 36.903 1.00 63.14 A N
ANISOU 1649 NH2 ARG A 214 12048 3813 8129 822 2756 -114 A N
ATOM 1650 N THR A 215 -10.627 6.025 32.640 1.00 50.72 A N
ANISOU 1650 N THR A 215 11121 2147 6002 1725 2597 -192 A N
ATOM 1651 CA THR A 215 -9.428 6.769 32.286 1.00 48.44 A C
ANISOU 1651 CA THR A 215 10525 2093 5787 1865 2430 -319 A C
ATOM 1652 C THR A 215 -8.238 5.870 32.000 1.00 52.75 A C
ANISOU 1652 C THR A 215 11249 2654 6138 2173 2443 -318 A C
ATOM 1653 O THR A 215 -7.750 5.155 32.878 1.00 54.15 A O
ANISOU 1653 O THR A 215 11640 2864 6071 2528 2494 -280 A O
ATOM 1654 CB THR A 215 -9.056 7.776 33.389 1.00 52.60 A C
ANISOU 1654 CB THR A 215 10771 2879 6334 2021 2312 -449 A C
ATOM 1655 CG2 THR A 215 -7.827 8.640 33.015 1.00 46.50 A C
ANISOU 1655 CG2 THR A 215 9650 2367 5652 2113 2162 -624 A C
ATOM 1656 OG1 THR A 215 -10.180 8.616 33.675 1.00 49.13 A O
ANISOU 1656 OG1 THR A 215 10178 2406 6084 1751 2322 -444 A O
ATOM 1657 N THR A 216 -7.749 5.965 30.768 1.00 47.81 A N
ANISOU 1657 N THR A 216 10517 2030 5619 2059 2399 -352 A N
ATOM 1658 CA THR A 216 -6.539 5.325 30.279 1.00 48.05 A C
ANISOU 1658 CA THR A 216 10638 2107 5514 2320 2392 -372 A C
ATOM 1659 C THR A 216 -5.570 6.455 30.000 1.00 50.71 A C
ANISOU 1659 C THR A 216 10544 2738 5984 2352 2208 -536 A C
ATOM 1660 O THR A 216 -6.003 7.462 29.447 1.00 46.16 A O
ANISOU 1660 O THR A 216 9698 2184 5657 2049 2150 -582 A O
ATOM 1661 CB THR A 216 -6.859 4.505 29.026 1.00 53.56 A C
ANISOU 1661 CB THR A 216 11572 2550 6227 2110 2518 -295 A C
ATOM 1662 CG2 THR A 216 -5.635 3.824 28.437 1.00 48.87 A C
ANISOU 1662 CG2 THR A 216 11088 1979 5500 2376 2532 -312 A C
ATOM 1663 OG1 THR A 216 -7.904 3.575 29.305 1.00 57.75 A O
ANISOU 1663 OG1 THR A 216 12477 2802 6664 1996 2718 -179 A O
ATOM 1664 N ILE A 217 -4.280 6.318 30.360 1.00 51.70 A N
ANISOU 1664 N ILE A 217 10597 3101 5945 2715 2136 -624 A N
ATOM 1665 CA ILE A 217 -3.328 7.380 30.028 1.00 52.34 A C
ANISOU 1665 CA ILE A 217 10261 3469 6156 2704 1986 -813 A C
ATOM 1666 C ILE A 217 -2.495 6.883 28.826 1.00 55.95 A C
ANISOU 1666 C ILE A 217 10758 3904 6595 2752 1991 -808 A C
ATOM 1667 O ILE A 217 -1.926 5.789 28.867 1.00 55.82 A O
ANISOU 1667 O ILE A 217 11000 3864 6346 3058 2053 -739 A O
ATOM 1668 CB ILE A 217 -2.498 7.912 31.240 1.00 57.73 A C
ANISOU 1668 CB ILE A 217 10700 4529 6704 2990 1878 -985 A C
ATOM 1669 CG1 ILE A 217 -3.460 8.618 32.247 1.00 58.23 A C
ANISOU 1669 CG1 ILE A 217 10680 4592 6853 2844 1880 -1013 A C
ATOM 1670 CG2 ILE A 217 -1.399 8.887 30.772 1.00 57.93 A C
ANISOU 1670 CG2 ILE A 217 10310 4848 6851 2956 1760 -1212 A C
ATOM 1671 CD1 ILE A 217 -2.850 9.281 33.559 1.00 71.81 A C
ANISOU 1671 CD1 ILE A 217 12140 6705 8441 3064 1786 -1216 A C
ATOM 1672 N TRP A 218 -2.504 7.673 27.730 1.00 50.88 A N
ANISOU 1672 N TRP A 218 9884 3245 6202 2448 1949 -859 A N
ATOM 1673 CA TRP A 218 -1.828 7.318 26.480 1.00 50.61 A C
ANISOU 1673 CA TRP A 218 9861 3185 6183 2431 1955 -857 A C
ATOM 1674 C TRP A 218 -0.620 8.203 26.192 1.00 57.42 A C
ANISOU 1674 C TRP A 218 10342 4347 7130 2490 1840 -1048 A C
ATOM 1675 O TRP A 218 -0.729 9.418 26.277 1.00 56.27 A O
ANISOU 1675 O TRP A 218 9885 4306 7189 2301 1789 -1160 A O
ATOM 1676 CB TRP A 218 -2.796 7.434 25.296 1.00 46.80 A C
ANISOU 1676 CB TRP A 218 9418 2473 5891 2036 2015 -753 A C
ATOM 1677 CG TRP A 218 -4.026 6.584 25.374 1.00 47.10 A C
ANISOU 1677 CG TRP A 218 9798 2236 5861 1896 2144 -600 A C
ATOM 1678 CD1 TRP A 218 -5.242 6.951 25.872 1.00 49.25 A C
ANISOU 1678 CD1 TRP A 218 10072 2421 6218 1694 2174 -539 A C
ATOM 1679 CD2 TRP A 218 -4.185 5.258 24.861 1.00 47.37 A C
ANISOU 1679 CD2 TRP A 218 10214 2047 5739 1913 2286 -508 A C
ATOM 1680 CE2 TRP A 218 -5.532 4.886 25.069 1.00 50.77 A C
ANISOU 1680 CE2 TRP A 218 10854 2269 6169 1683 2401 -410 A C
ATOM 1681 CE3 TRP A 218 -3.328 4.357 24.204 1.00 49.65 A C
ANISOU 1681 CE3 TRP A 218 10688 2284 5894 2082 2348 -510 A C
ATOM 1682 NE1 TRP A 218 -6.147 5.931 25.708 1.00 48.93 A N
ANISOU 1682 NE1 TRP A 218 10375 2139 6077 1571 2318 -423 A N
ATOM 1683 CZ2 TRP A 218 -6.024 3.625 24.717 1.00 51.07 A C
ANISOU 1683 CZ2 TRP A 218 11289 2043 6072 1606 2591 -336 A C
ATOM 1684 CZ3 TRP A 218 -3.817 3.107 23.854 1.00 52.25 A C
ANISOU 1684 CZ3 TRP A 218 11427 2329 6095 2024 2542 -424 A C
ATOM 1685 CH2 TRP A 218 -5.150 2.755 24.106 1.00 52.74 A C
ANISOU 1685 CH2 TRP A 218 11698 2181 6160 1774 2668 -349 A C
ATOM 1686 N THR A 219 0.500 7.600 25.748 1.00 58.24 A N
ANISOU 1686 N THR A 219 10475 4564 7090 2724 1826 -1087 A N
ATOM 1687 CA THR A 219 1.731 8.304 25.323 1.00 59.24 A C
ANISOU 1687 CA THR A 219 10249 4983 7277 2772 1734 -1277 A C
ATOM 1688 C THR A 219 2.798 7.266 24.869 1.00 65.68 A C
ANISOU 1688 C THR A 219 11208 5877 7869 3092 1749 -1261 A C
ATOM 1689 O THR A 219 2.485 6.074 24.764 1.00 66.64 A O
ANISOU 1689 O THR A 219 11717 5767 7834 3225 1854 -1094 A O
ATOM 1690 CB THR A 219 2.253 9.301 26.407 1.00 62.49 A C
ANISOU 1690 CB THR A 219 10310 5737 7696 2851 1641 -1499 A C
ATOM 1691 CG2 THR A 219 2.783 8.619 27.648 1.00 63.12 A C
ANISOU 1691 CG2 THR A 219 10477 6055 7450 3277 1605 -1525 A C
ATOM 1692 OG1 THR A 219 3.255 10.144 25.841 1.00 63.56 A O
ANISOU 1692 OG1 THR A 219 10086 6112 7952 2776 1588 -1704 A O
ATOM 1693 N GLU A 220 4.029 7.730 24.552 1.00 63.77 A N
ANISOU 1693 N GLU A 220 10658 5945 7625 3195 1669 -1440 A N
ATOM 1694 CA GLU A 220 5.157 6.855 24.174 1.00 66.16 A C
ANISOU 1694 CA GLU A 220 11036 6389 7711 3533 1675 -1446 A C
ATOM 1695 C GLU A 220 5.801 6.310 25.458 1.00 75.78 A C
ANISOU 1695 C GLU A 220 12277 7908 8609 4013 1638 -1477 A C
ATOM 1696 O GLU A 220 6.058 7.096 26.369 1.00 76.63 A O
ANISOU 1696 O GLU A 220 12084 8330 8702 4043 1542 -1648 A O
ATOM 1697 CB GLU A 220 6.200 7.614 23.325 1.00 67.03 A C
ANISOU 1697 CB GLU A 220 10778 6740 7950 3428 1611 -1634 A C
ATOM 1698 CG GLU A 220 5.830 7.796 21.865 1.00 72.75 A C
ANISOU 1698 CG GLU A 220 11543 7198 8902 3080 1669 -1557 A C
ATOM 1699 CD GLU A 220 6.973 8.317 21.017 1.00 87.84 A C
ANISOU 1699 CD GLU A 220 13149 9336 10891 3044 1633 -1717 A C
ATOM 1700 OE1 GLU A 220 7.797 7.494 20.555 1.00 75.89 A O
ANISOU 1700 OE1 GLU A 220 11734 7889 9210 3284 1650 -1702 A O
ATOM 1701 OE2 GLU A 220 7.062 9.553 20.837 1.00 78.48 A O1-
ANISOU 1701 OE2 GLU A 220 11630 8255 9934 2780 1609 -1862 A O1-
ATOM 1702 N LYS A 221 6.054 4.983 25.533 1.00 75.90 A N
ANISOU 1702 N LYS A 221 12645 7833 8360 4392 1732 -1313 A N
ATOM 1703 CA LYS A 221 6.643 4.241 26.670 1.00 79.03 A C
ANISOU 1703 CA LYS A 221 13138 8490 8400 4936 1736 -1266 A C
ATOM 1704 C LYS A 221 7.554 5.080 27.605 1.00 85.07 A C
ANISOU 1704 C LYS A 221 13426 9851 9047 5116 1565 -1512 A C
ATOM 1705 O LYS A 221 7.404 5.010 28.829 1.00 86.12 A O
ANISOU 1705 O LYS A 221 13561 10173 8989 5346 1538 -1502 A O
ATOM 1706 CB LYS A 221 7.451 3.043 26.153 1.00 83.54 A C
ANISOU 1706 CB LYS A 221 13964 9028 8749 5331 1843 -1143 A C
ATOM 1707 CG LYS A 221 6.596 1.879 25.688 1.00100.19 A C
ANISOU 1707 CG LYS A 221 16644 10585 10838 5315 2069 -889 A C
ATOM 1708 CD LYS A 221 7.447 0.778 25.082 1.00114.78 A C
ANISOU 1708 CD LYS A 221 18738 12366 12507 5665 2205 -792 A C
ATOM 1709 CE LYS A 221 6.619 -0.395 24.614 1.00128.36 A C
ANISOU 1709 CE LYS A 221 21043 13517 14210 5619 2475 -575 A C
ATOM 1710 NZ LYS A 221 7.441 -1.401 23.884 1.00139.20 A N1+
ANISOU 1710 NZ LYS A 221 22663 14780 15448 5908 2636 -502 A N1+
ATOM 1711 N GLU A 222 8.480 5.869 27.017 1.00 81.86 A N
ANISOU 1711 N GLU A 222 12607 9748 8748 4991 1465 -1747 A N
ATOM 1712 CA GLU A 222 9.462 6.726 27.696 1.00 83.59 A C
ANISOU 1712 CA GLU A 222 12319 10565 8877 5082 1321 -2049 A C
ATOM 1713 C GLU A 222 8.802 7.788 28.607 1.00 86.61 A C
ANISOU 1713 C GLU A 222 12487 11027 9394 4805 1265 -2204 A C
ATOM 1714 O GLU A 222 9.367 8.136 29.643 1.00 88.22 A O
ANISOU 1714 O GLU A 222 12399 11723 9398 5000 1173 -2401 A O
ATOM 1715 CB GLU A 222 10.388 7.419 26.677 1.00 84.71 A C
ANISOU 1715 CB GLU A 222 12105 10891 9190 4869 1276 -2269 A C
ATOM 1716 CG GLU A 222 11.128 6.467 25.744 1.00 97.95 A C
ANISOU 1716 CG GLU A 222 13944 12534 10740 5133 1327 -2152 A C
ATOM 1717 CD GLU A 222 10.385 5.944 24.525 1.00115.18 A C
ANISOU 1717 CD GLU A 222 16511 14134 13117 4899 1454 -1926 A C
ATOM 1718 OE1 GLU A 222 9.594 6.712 23.929 1.00105.46 A O
ANISOU 1718 OE1 GLU A 222 15238 12621 12211 4413 1471 -1944 A O
ATOM 1719 OE2 GLU A 222 10.622 4.774 24.143 1.00106.45 A O1-
ANISOU 1719 OE2 GLU A 222 15744 12873 11830 5210 1552 -1737 A O1-
ATOM 1720 N LEU A 223 7.621 8.296 28.214 1.00 80.43 A N
ANISOU 1720 N LEU A 223 11839 9789 8931 4363 1328 -2121 A N
ATOM 1721 CA LEU A 223 6.875 9.312 28.954 1.00 79.45 A C
ANISOU 1721 CA LEU A 223 11555 9656 8977 4074 1309 -2240 A C
ATOM 1722 C LEU A 223 5.739 8.723 29.800 1.00 81.95 A C
ANISOU 1722 C LEU A 223 12230 9710 9196 4165 1363 -2014 A C
ATOM 1723 O LEU A 223 5.134 9.470 30.576 1.00 81.57 A O
ANISOU 1723 O LEU A 223 12063 9685 9244 3984 1349 -2106 A O
ATOM 1724 CB LEU A 223 6.282 10.358 27.982 1.00 76.97 A C
ANISOU 1724 CB LEU A 223 11124 9033 9088 3538 1361 -2287 A C
ATOM 1725 CG LEU A 223 7.218 11.424 27.393 1.00 82.10 A C
ANISOU 1725 CG LEU A 223 11340 9939 9916 3322 1338 -2579 A C
ATOM 1726 CD1 LEU A 223 6.618 12.028 26.130 1.00 79.70 A C
ANISOU 1726 CD1 LEU A 223 11067 9242 9974 2910 1428 -2489 A C
ATOM 1727 CD2 LEU A 223 7.537 12.524 28.407 1.00 85.09 A C
ANISOU 1727 CD2 LEU A 223 11336 10661 10332 3202 1307 -2903 A C
ATOM 1728 N LEU A 224 5.448 7.409 29.660 1.00 77.44 A N
ANISOU 1728 N LEU A 224 12101 8879 8444 4429 1450 -1732 A N
ATOM 1729 CA LEU A 224 4.343 6.727 30.348 1.00 76.89 A C
ANISOU 1729 CA LEU A 224 12423 8505 8286 4499 1545 -1500 A C
ATOM 1730 C LEU A 224 4.485 6.708 31.880 1.00 86.02 A C
ANISOU 1730 C LEU A 224 13507 10015 9160 4829 1493 -1550 A C
ATOM 1731 O LEU A 224 3.575 7.178 32.569 1.00 84.68 A O
ANISOU 1731 O LEU A 224 13368 9735 9072 4653 1506 -1541 A O
ATOM 1732 CB LEU A 224 4.148 5.300 29.809 1.00 76.72 A C
ANISOU 1732 CB LEU A 224 12894 8126 8129 4704 1696 -1221 A C
ATOM 1733 CG LEU A 224 2.756 4.681 29.999 1.00 79.47 A C
ANISOU 1733 CG LEU A 224 13684 8000 8511 4571 1850 -987 A C
ATOM 1734 CD1 LEU A 224 1.703 5.402 29.185 1.00 76.04 A C
ANISOU 1734 CD1 LEU A 224 13209 7246 8437 4007 1864 -992 A C
ATOM 1735 CD2 LEU A 224 2.752 3.232 29.600 1.00 82.81 A C
ANISOU 1735 CD2 LEU A 224 14588 8118 8757 4822 2037 -758 A C
ATOM 1736 N GLU A 225 5.602 6.162 32.401 1.00 87.92 A N
ANISOU 1736 N GLU A 225 13645 10704 9057 5318 1438 -1597 A N
ATOM 1737 CA GLU A 225 5.892 6.064 33.836 1.00 91.31 A C
ANISOU 1737 CA GLU A 225 13975 11569 9149 5703 1380 -1641 A C
ATOM 1738 C GLU A 225 5.722 7.447 34.538 1.00 96.18 A C
ANISOU 1738 C GLU A 225 14162 12476 9906 5389 1265 -1951 A C
ATOM 1739 O GLU A 225 4.923 7.506 35.476 1.00 96.21 A O
ANISOU 1739 O GLU A 225 14277 12426 9853 5391 1289 -1892 A O
ATOM 1740 CB GLU A 225 7.295 5.474 34.065 1.00 96.47 A C
ANISOU 1740 CB GLU A 225 14483 12751 9420 6261 1320 -1677 A C
ATOM 1741 CG GLU A 225 7.555 4.940 35.464 1.00114.24 A C
ANISOU 1741 CG GLU A 225 16776 15402 11230 6803 1308 -1591 A C
ATOM 1742 CD GLU A 225 8.978 4.467 35.689 1.00148.36 A C
ANISOU 1742 CD GLU A 225 20879 20339 15151 7374 1236 -1639 A C
ATOM 1743 OE1 GLU A 225 9.207 3.235 35.673 1.00144.84 A O
ANISOU 1743 OE1 GLU A 225 20803 19784 14443 7869 1366 -1337 A O
ATOM 1744 OE2 GLU A 225 9.868 5.328 35.877 1.00149.40 A O1-
ANISOU 1744 OE2 GLU A 225 20467 21071 15229 7324 1069 -1986 A O1-
ATOM 1745 N PRO A 226 6.336 8.577 34.082 1.00 92.83 A N
ANISOU 1745 N PRO A 226 13284 12296 9691 5080 1175 -2275 A N
ATOM 1746 CA PRO A 226 6.109 9.857 34.790 1.00 92.93 A C
ANISOU 1746 CA PRO A 226 12940 12526 9845 4771 1121 -2573 A C
ATOM 1747 C PRO A 226 4.722 10.493 34.572 1.00 94.38 A C
ANISOU 1747 C PRO A 226 13277 12177 10405 4299 1211 -2491 A C
ATOM 1748 O PRO A 226 4.336 11.371 35.356 1.00 94.40 A O
ANISOU 1748 O PRO A 226 13091 12295 10481 4115 1202 -2671 A O
ATOM 1749 CB PRO A 226 7.205 10.768 34.233 1.00 95.23 A C
ANISOU 1749 CB PRO A 226 12757 13163 10264 4571 1057 -2926 A C
ATOM 1750 CG PRO A 226 7.510 10.220 32.895 1.00 97.81 A C
ANISOU 1750 CG PRO A 226 13254 13202 10707 4559 1099 -2759 A C
ATOM 1751 CD PRO A 226 7.331 8.742 32.999 1.00 94.09 A C
ANISOU 1751 CD PRO A 226 13229 12574 9947 5015 1142 -2405 A C
ATOM 1752 N SER A 227 3.983 10.084 33.522 1.00 88.61 A N
ANISOU 1752 N SER A 227 12864 10902 9902 4103 1303 -2238 A N
ATOM 1753 CA SER A 227 2.657 10.648 33.255 1.00 85.75 A C
ANISOU 1753 CA SER A 227 12630 10079 9873 3683 1387 -2138 A C
ATOM 1754 C SER A 227 1.601 10.090 34.203 1.00 90.92 A C
ANISOU 1754 C SER A 227 13596 10555 10394 3795 1441 -1939 A C
ATOM 1755 O SER A 227 0.705 10.834 34.606 1.00 89.05 A O
ANISOU 1755 O SER A 227 13307 10182 10347 3521 1473 -1979 A O
ATOM 1756 CB SER A 227 2.240 10.407 31.812 1.00 86.47 A C
ANISOU 1756 CB SER A 227 12923 9732 10200 3450 1460 -1947 A C
ATOM 1757 OG SER A 227 2.807 11.395 30.968 1.00 92.46 A O
ANISOU 1757 OG SER A 227 13361 10575 11195 3202 1440 -2141 A O
ATOM 1758 N VAL A 228 1.717 8.791 34.578 1.00 90.19 A N
ANISOU 1758 N VAL A 228 13835 10456 9976 4208 1474 -1721 A N
ATOM 1759 CA VAL A 228 0.768 8.136 35.485 1.00 90.60 A C
ANISOU 1759 CA VAL A 228 14225 10325 9875 4346 1558 -1511 A C
ATOM 1760 C VAL A 228 0.905 8.712 36.917 1.00 96.29 A C
ANISOU 1760 C VAL A 228 14701 11465 10420 4482 1481 -1696 A C
ATOM 1761 O VAL A 228 -0.115 8.843 37.586 1.00 94.87 A O
ANISOU 1761 O VAL A 228 14654 11109 10282 4365 1537 -1621 A O
ATOM 1762 CB VAL A 228 0.803 6.578 35.460 1.00 95.75 A C
ANISOU 1762 CB VAL A 228 15346 10793 10243 4743 1674 -1211 A C
ATOM 1763 CG1 VAL A 228 0.668 6.046 34.033 1.00 93.65 A C
ANISOU 1763 CG1 VAL A 228 15320 10105 10159 4552 1769 -1064 A C
ATOM 1764 CG2 VAL A 228 2.040 6.007 36.147 1.00 99.01 A C
ANISOU 1764 CG2 VAL A 228 15673 11693 10255 5306 1613 -1244 A C
ATOM 1765 N TYR A 229 2.133 9.095 37.362 1.00 96.09 A N
ANISOU 1765 N TYR A 229 14295 12013 10201 4697 1356 -1960 A N
ATOM 1766 CA TYR A 229 2.332 9.706 38.684 1.00 98.28 A C
ANISOU 1766 CA TYR A 229 14285 12761 10295 4796 1278 -2192 A C
ATOM 1767 C TYR A 229 1.735 11.120 38.705 1.00 99.89 A C
ANISOU 1767 C TYR A 229 14214 12868 10869 4275 1285 -2442 A C
ATOM 1768 O TYR A 229 1.029 11.471 39.654 1.00100.25 A O
ANISOU 1768 O TYR A 229 14257 12934 10898 4209 1306 -2483 A O
ATOM 1769 CB TYR A 229 3.826 9.748 39.113 1.00103.38 A C
ANISOU 1769 CB TYR A 229 14559 14113 10606 5151 1147 -2438 A C
ATOM 1770 CG TYR A 229 4.070 10.730 40.250 1.00107.80 A C
ANISOU 1770 CG TYR A 229 14699 15198 11061 5085 1062 -2798 A C
ATOM 1771 CD1 TYR A 229 3.788 10.384 41.570 1.00112.17 A C
ANISOU 1771 CD1 TYR A 229 15326 16012 11283 5388 1050 -2740 A C
ATOM 1772 CD2 TYR A 229 4.463 12.044 39.992 1.00108.51 A C
ANISOU 1772 CD2 TYR A 229 14344 15474 11410 4677 1027 -3199 A C
ATOM 1773 CE1 TYR A 229 3.918 11.311 42.607 1.00115.12 A C
ANISOU 1773 CE1 TYR A 229 15316 16858 11566 5286 984 -3092 A C
ATOM 1774 CE2 TYR A 229 4.570 12.985 41.018 1.00111.42 A C
ANISOU 1774 CE2 TYR A 229 14348 16271 11714 4549 989 -3561 A C
ATOM 1775 CZ TYR A 229 4.316 12.610 42.327 1.00121.12 A C
ANISOU 1775 CZ TYR A 229 15633 17796 12592 4855 956 -3517 A C
ATOM 1776 OH TYR A 229 4.464 13.526 43.344 1.00123.68 A O
ANISOU 1776 OH TYR A 229 15580 18584 12828 4723 919 -3903 A O
ATOM 1777 N GLU A 230 2.063 11.935 37.679 1.00 94.07 A N
ANISOU 1777 N GLU A 230 13249 12037 10456 3931 1285 -2607 A N
ATOM 1778 CA GLU A 230 1.629 13.328 37.538 1.00 92.22 A C
ANISOU 1778 CA GLU A 230 12757 11681 10601 3450 1335 -2838 A C
ATOM 1779 C GLU A 230 0.103 13.465 37.423 1.00 91.63 A C
ANISOU 1779 C GLU A 230 12959 11067 10789 3179 1445 -2605 A C
ATOM 1780 O GLU A 230 -0.453 14.454 37.906 1.00 90.23 A O
ANISOU 1780 O GLU A 230 12626 10850 10806 2913 1499 -2760 A O
ATOM 1781 CB GLU A 230 2.300 13.961 36.307 1.00 92.84 A C
ANISOU 1781 CB GLU A 230 12612 11712 10950 3195 1348 -2983 A C
ATOM 1782 CG GLU A 230 2.241 15.485 36.265 1.00104.34 A C
ANISOU 1782 CG GLU A 230 13728 13173 12745 2764 1425 -3301 A C
ATOM 1783 CD GLU A 230 3.184 16.252 37.177 1.00130.27 A C
ANISOU 1783 CD GLU A 230 16582 17029 15884 2768 1383 -3751 A C
ATOM 1784 OE1 GLU A 230 2.966 17.473 37.360 1.00129.11 A O
ANISOU 1784 OE1 GLU A 230 16210 16841 16005 2410 1491 -4014 A O
ATOM 1785 OE2 GLU A 230 4.154 15.646 37.688 1.00126.57 A O1-
ANISOU 1785 OE2 GLU A 230 15993 17067 15032 3126 1259 -3850 A O1-
ATOM 1786 N PHE A 231 -0.566 12.493 36.778 1.00 85.99 A N
ANISOU 1786 N PHE A 231 12641 9955 10078 3237 1495 -2252 A N
ATOM 1787 CA PHE A 231 -2.013 12.555 36.568 1.00 83.05 A C
ANISOU 1787 CA PHE A 231 12512 9112 9933 2973 1599 -2031 A C
ATOM 1788 C PHE A 231 -2.734 11.350 37.204 1.00 85.81 A C
ANISOU 1788 C PHE A 231 13271 9308 10023 3224 1645 -1752 A C
ATOM 1789 O PHE A 231 -3.716 10.850 36.654 1.00 84.11 A O
ANISOU 1789 O PHE A 231 13360 8688 9912 3089 1735 -1502 A O
ATOM 1790 CB PHE A 231 -2.320 12.677 35.059 1.00 82.54 A C
ANISOU 1790 CB PHE A 231 12506 8685 10170 2688 1652 -1899 A C
ATOM 1791 CG PHE A 231 -1.500 13.721 34.330 1.00 83.81 A C
ANISOU 1791 CG PHE A 231 12309 8976 10559 2488 1635 -2137 A C
ATOM 1792 CD1 PHE A 231 -1.516 15.054 34.735 1.00 87.16 A C
ANISOU 1792 CD1 PHE A 231 12420 9501 11196 2251 1675 -2395 A C
ATOM 1793 CD2 PHE A 231 -0.710 13.371 33.244 1.00 85.57 A C
ANISOU 1793 CD2 PHE A 231 12520 9205 10788 2529 1606 -2113 A C
ATOM 1794 CE1 PHE A 231 -0.753 16.018 34.067 1.00 88.01 A C
ANISOU 1794 CE1 PHE A 231 12220 9697 11522 2050 1705 -2621 A C
ATOM 1795 CE2 PHE A 231 0.062 14.333 32.582 1.00 88.56 A C
ANISOU 1795 CE2 PHE A 231 12574 9702 11374 2339 1611 -2335 A C
ATOM 1796 CZ PHE A 231 0.032 15.651 32.994 1.00 86.94 A C
ANISOU 1796 CZ PHE A 231 12071 9576 11384 2095 1670 -2586 A C
ATOM 1797 N ALA A 232 -2.271 10.928 38.397 1.00 83.17 A N
ANISOU 1797 N ALA A 232 12935 9318 9347 3576 1599 -1808 A N
ATOM 1798 CA ALA A 232 -2.845 9.814 39.159 1.00 83.02 A C
ANISOU 1798 CA ALA A 232 13302 9192 9050 3862 1670 -1553 A C
ATOM 1799 C ALA A 232 -4.243 10.137 39.714 1.00 81.86 A C
ANISOU 1799 C ALA A 232 13279 8776 9047 3615 1758 -1469 A C
ATOM 1800 O ALA A 232 -5.069 9.234 39.847 1.00 80.21 A O
ANISOU 1800 O ALA A 232 13455 8263 8759 3668 1872 -1206 A O
ATOM 1801 CB ALA A 232 -1.915 9.444 40.304 1.00 87.13 A C
ANISOU 1801 CB ALA A 232 13728 10228 9149 4331 1593 -1644 A C
ATOM 1802 N GLU A 233 -4.485 11.416 40.046 1.00 76.90 A N
ANISOU 1802 N GLU A 233 12328 8260 8630 3345 1728 -1705 A N
ATOM 1803 CA GLU A 233 -5.712 11.931 40.668 1.00 75.18 A C
ANISOU 1803 CA GLU A 233 12146 7860 8558 3117 1805 -1680 A C
ATOM 1804 C GLU A 233 -6.791 12.420 39.644 1.00 73.99 A C
ANISOU 1804 C GLU A 233 12037 7269 8806 2693 1891 -1562 A C
ATOM 1805 O GLU A 233 -7.678 13.201 40.027 1.00 72.24 A O
ANISOU 1805 O GLU A 233 11728 6946 8776 2461 1949 -1604 A O
ATOM 1806 CB GLU A 233 -5.338 13.079 41.630 1.00 77.94 A C
ANISOU 1806 CB GLU A 233 12114 8586 8913 3067 1751 -2021 A C
ATOM 1807 CG GLU A 233 -4.677 12.609 42.924 1.00 96.17 A C
ANISOU 1807 CG GLU A 233 14390 11362 10788 3472 1681 -2112 A C
ATOM 1808 CD GLU A 233 -3.977 13.656 43.776 1.00125.48 A C
ANISOU 1808 CD GLU A 233 17667 15567 14443 3442 1609 -2520 A C
ATOM 1809 OE1 GLU A 233 -4.547 14.754 43.977 1.00122.63 A O
ANISOU 1809 OE1 GLU A 233 17132 15113 14348 3111 1672 -2698 A O
ATOM 1810 OE2 GLU A 233 -2.876 13.351 44.291 1.00121.83 A O1-
ANISOU 1810 OE2 GLU A 233 17040 15604 13647 3763 1504 -2667 A O1-
ATOM 1811 N THR A 234 -6.750 11.918 38.377 1.00 66.69 A N
ANISOU 1811 N THR A 234 11251 6108 7982 2613 1908 -1405 A N
ATOM 1812 CA THR A 234 -7.698 12.293 37.312 1.00 62.93 A C
ANISOU 1812 CA THR A 234 10795 5285 7830 2250 1980 -1279 A C
ATOM 1813 C THR A 234 -9.160 11.948 37.673 1.00 66.20 A C
ANISOU 1813 C THR A 234 11451 5437 8266 2117 2087 -1079 A C
ATOM 1814 O THR A 234 -10.037 12.798 37.491 1.00 64.46 A O
ANISOU 1814 O THR A 234 11099 5088 8303 1839 2137 -1074 A O
ATOM 1815 CB THR A 234 -7.328 11.644 35.971 1.00 62.88 A C
ANISOU 1815 CB THR A 234 10911 5129 7851 2228 1976 -1155 A C
ATOM 1816 CG2 THR A 234 -8.082 12.251 34.819 1.00 57.76 A C
ANISOU 1816 CG2 THR A 234 10178 4242 7526 1868 2024 -1073 A C
ATOM 1817 OG1 THR A 234 -5.940 11.812 35.705 1.00 59.93 A O
ANISOU 1817 OG1 THR A 234 10339 5021 7411 2393 1881 -1330 A O
ATOM 1818 N GLU A 235 -9.411 10.713 38.175 1.00 63.68 A N
ANISOU 1818 N GLU A 235 11483 5039 7674 2324 2143 -912 A N
ATOM 1819 CA GLU A 235 -10.749 10.247 38.568 1.00 63.08 A C
ANISOU 1819 CA GLU A 235 11661 4724 7581 2204 2267 -733 A C
ATOM 1820 C GLU A 235 -11.329 11.121 39.683 1.00 66.80 A C
ANISOU 1820 C GLU A 235 11965 5311 8104 2151 2271 -839 A C
ATOM 1821 O GLU A 235 -12.484 11.544 39.586 1.00 65.83 A O
ANISOU 1821 O GLU A 235 11829 5018 8168 1888 2344 -769 A O
ATOM 1822 CB GLU A 235 -10.724 8.773 39.013 1.00 66.00 A C
ANISOU 1822 CB GLU A 235 12453 4994 7630 2475 2363 -557 A C
ATOM 1823 CG GLU A 235 -11.751 7.897 38.309 1.00 74.26 A C
ANISOU 1823 CG GLU A 235 13823 5675 8716 2253 2520 -351 A C
ATOM 1824 CD GLU A 235 -13.220 8.282 38.389 1.00 85.02 A C
ANISOU 1824 CD GLU A 235 15173 6881 10250 1918 2602 -291 A C
ATOM 1825 OE1 GLU A 235 -13.942 8.011 37.403 1.00 77.53 A O
ANISOU 1825 OE1 GLU A 235 14303 5728 9428 1631 2676 -197 A O
ATOM 1826 OE2 GLU A 235 -13.661 8.822 39.431 1.00 74.69 A O1-
ANISOU 1826 OE2 GLU A 235 13770 5676 8931 1946 2599 -341 A O1-
ATOM 1827 N LYS A 236 -10.506 11.417 40.717 1.00 64.74 A N
ANISOU 1827 N LYS A 236 11555 5376 7669 2403 2193 -1022 A N
ATOM 1828 CA LYS A 236 -10.840 12.285 41.847 1.00 65.21 A C
ANISOU 1828 CA LYS A 236 11424 5609 7744 2379 2191 -1183 A C
ATOM 1829 C LYS A 236 -11.305 13.645 41.315 1.00 67.21 A C
ANISOU 1829 C LYS A 236 11382 5769 8385 2028 2213 -1301 A C
ATOM 1830 O LYS A 236 -12.332 14.153 41.761 1.00 66.53 A O
ANISOU 1830 O LYS A 236 11273 5585 8422 1868 2291 -1282 A O
ATOM 1831 CB LYS A 236 -9.612 12.430 42.779 1.00 69.63 A C
ANISOU 1831 CB LYS A 236 11799 6611 8044 2690 2084 -1413 A C
ATOM 1832 CG LYS A 236 -9.822 13.308 44.028 1.00 70.83 A C
ANISOU 1832 CG LYS A 236 11745 7006 8162 2681 2083 -1625 A C
ATOM 1833 CD LYS A 236 -8.546 13.392 44.859 1.00 76.03 A C
ANISOU 1833 CD LYS A 236 12132 8169 8586 2925 1965 -1913 A C
ATOM 1834 CE LYS A 236 -8.503 14.600 45.759 1.00 88.09 A C
ANISOU 1834 CE LYS A 236 13431 9966 10073 2884 1971 -2169 A C
ATOM 1835 NZ LYS A 236 -7.216 14.679 46.496 1.00 99.71 A N1+
ANISOU 1835 NZ LYS A 236 14581 11986 11317 3070 1857 -2500 A N1+
ATOM 1836 N MET A 237 -10.575 14.193 40.321 1.00 62.80 A N
ANISOU 1836 N MET A 237 10618 5227 8017 1922 2165 -1400 A N
ATOM 1837 CA MET A 237 -10.896 15.479 39.703 1.00 61.47 A C
ANISOU 1837 CA MET A 237 10188 4950 8219 1624 2219 -1487 A C
ATOM 1838 C MET A 237 -12.208 15.391 38.912 1.00 61.18 A C
ANISOU 1838 C MET A 237 10281 4592 8373 1393 2309 -1224 A C
ATOM 1839 O MET A 237 -13.023 16.315 39.002 1.00 59.27 A O
ANISOU 1839 O MET A 237 9905 4254 8359 1206 2398 -1227 A O
ATOM 1840 CB MET A 237 -9.738 15.963 38.817 1.00 64.12 A C
ANISOU 1840 CB MET A 237 10304 5382 8677 1593 2165 -1639 A C
ATOM 1841 CG MET A 237 -8.652 16.676 39.598 1.00 70.35 A C
ANISOU 1841 CG MET A 237 10814 6513 9404 1681 2120 -1988 A C
ATOM 1842 SD MET A 237 -7.314 17.320 38.553 1.00 75.24 A S
ANISOU 1842 SD MET A 237 11160 7244 10183 1602 2087 -2190 A S
ATOM 1843 CE MET A 237 -6.256 15.883 38.497 1.00 72.98 A C
ANISOU 1843 CE MET A 237 11042 7186 9501 1965 1934 -2122 A C
ATOM 1844 N LEU A 238 -12.438 14.270 38.198 1.00 56.09 A N
ANISOU 1844 N LEU A 238 9892 3803 7616 1411 2302 -1008 A N
ATOM 1845 CA LEU A 238 -13.642 14.012 37.393 1.00 54.76 A C
ANISOU 1845 CA LEU A 238 9842 3395 7569 1185 2380 -777 A C
ATOM 1846 C LEU A 238 -14.866 13.858 38.282 1.00 57.47 A C
ANISOU 1846 C LEU A 238 10310 3663 7862 1127 2468 -685 A C
ATOM 1847 O LEU A 238 -15.932 14.379 37.945 1.00 55.68 A O
ANISOU 1847 O LEU A 238 9997 3333 7825 910 2540 -587 A O
ATOM 1848 CB LEU A 238 -13.446 12.745 36.526 1.00 55.13 A C
ANISOU 1848 CB LEU A 238 10149 3337 7463 1219 2369 -629 A C
ATOM 1849 CG LEU A 238 -14.474 12.442 35.421 1.00 59.55 A C
ANISOU 1849 CG LEU A 238 10788 3712 8125 956 2437 -436 A C
ATOM 1850 CD1 LEU A 238 -14.609 13.588 34.429 1.00 59.17 A C
ANISOU 1850 CD1 LEU A 238 10440 3675 8368 764 2427 -431 A C
ATOM 1851 CD2 LEU A 238 -14.073 11.218 34.661 1.00 63.00 A C
ANISOU 1851 CD2 LEU A 238 11486 4060 8393 999 2443 -352 A C
ATOM 1852 N LYS A 239 -14.705 13.165 39.421 1.00 55.12 A N
ANISOU 1852 N LYS A 239 10204 3441 7299 1339 2469 -710 A N
ATOM 1853 CA LYS A 239 -15.766 12.973 40.414 1.00 56.36 A C
ANISOU 1853 CA LYS A 239 10494 3544 7375 1314 2560 -638 A C
ATOM 1854 C LYS A 239 -16.145 14.326 41.070 1.00 58.99 A C
ANISOU 1854 C LYS A 239 10544 3964 7904 1223 2582 -781 A C
ATOM 1855 O LYS A 239 -17.332 14.668 41.140 1.00 57.59 A O
ANISOU 1855 O LYS A 239 10345 3679 7859 1043 2672 -687 A O
ATOM 1856 CB LYS A 239 -15.315 11.947 41.473 1.00 61.54 A C
ANISOU 1856 CB LYS A 239 11419 4285 7680 1615 2565 -627 A C
ATOM 1857 CG LYS A 239 -16.449 11.294 42.284 1.00 83.94 A C
ANISOU 1857 CG LYS A 239 14519 6993 10380 1589 2697 -480 A C
ATOM 1858 CD LYS A 239 -16.796 9.816 41.950 1.00 98.80 A C
ANISOU 1858 CD LYS A 239 16807 8649 12083 1598 2815 -275 A C
ATOM 1859 CE LYS A 239 -15.683 8.806 42.169 1.00116.09 A C
ANISOU 1859 CE LYS A 239 19245 10888 13977 1955 2810 -245 A C
ATOM 1860 NZ LYS A 239 -16.165 7.410 42.028 1.00125.67 A N1+
ANISOU 1860 NZ LYS A 239 20890 11825 15035 1945 2991 -50 A N1+
ATOM 1861 N TYR A 240 -15.125 15.107 41.488 1.00 56.13 A N
ANISOU 1861 N TYR A 240 9956 3803 7567 1334 2515 -1022 A N
ATOM 1862 CA TYR A 240 -15.280 16.436 42.118 1.00 56.67 A C
ANISOU 1862 CA TYR A 240 9755 3952 7825 1245 2564 -1217 A C
ATOM 1863 C TYR A 240 -16.018 17.410 41.185 1.00 56.69 A C
ANISOU 1863 C TYR A 240 9583 3767 8190 988 2657 -1140 A C
ATOM 1864 O TYR A 240 -16.859 18.184 41.635 1.00 56.38 A O
ANISOU 1864 O TYR A 240 9440 3674 8308 882 2762 -1156 A O
ATOM 1865 CB TYR A 240 -13.902 17.002 42.508 1.00 60.05 A C
ANISOU 1865 CB TYR A 240 9966 4644 8206 1371 2488 -1521 A C
ATOM 1866 CG TYR A 240 -13.399 16.629 43.892 1.00 65.62 A C
ANISOU 1866 CG TYR A 240 10708 5638 8587 1617 2433 -1676 A C
ATOM 1867 CD1 TYR A 240 -13.602 15.347 44.417 1.00 68.12 A C
ANISOU 1867 CD1 TYR A 240 11331 5962 8591 1820 2420 -1492 A C
ATOM 1868 CD2 TYR A 240 -12.706 17.545 44.667 1.00 69.20 A C
ANISOU 1868 CD2 TYR A 240 10890 6376 9027 1650 2410 -2013 A C
ATOM 1869 CE1 TYR A 240 -13.114 14.993 45.673 1.00 71.72 A C
ANISOU 1869 CE1 TYR A 240 11818 6713 8719 2087 2376 -1605 A C
ATOM 1870 CE2 TYR A 240 -12.220 17.204 45.931 1.00 73.07 A C
ANISOU 1870 CE2 TYR A 240 11380 7203 9179 1890 2349 -2163 A C
ATOM 1871 CZ TYR A 240 -12.423 15.925 46.429 1.00 82.43 A C
ANISOU 1871 CZ TYR A 240 12871 8404 10044 2129 2327 -1939 A C
ATOM 1872 OH TYR A 240 -11.949 15.580 47.673 1.00 86.57 A O
ANISOU 1872 OH TYR A 240 13397 9287 10208 2406 2274 -2055 A O
ATOM 1873 N ALA A 241 -15.730 17.319 39.879 1.00 50.95 A N
ANISOU 1873 N ALA A 241 8831 2951 7578 910 2627 -1038 A N
ATOM 1874 CA ALA A 241 -16.375 18.098 38.834 1.00 48.77 A C
ANISOU 1874 CA ALA A 241 8405 2525 7600 712 2712 -913 A C
ATOM 1875 C ALA A 241 -17.841 17.690 38.672 1.00 52.71 A C
ANISOU 1875 C ALA A 241 9019 2909 8097 591 2777 -663 A C
ATOM 1876 O ALA A 241 -18.685 18.567 38.513 1.00 52.60 A O
ANISOU 1876 O ALA A 241 8855 2832 8300 476 2885 -590 A O
ATOM 1877 CB ALA A 241 -15.639 17.906 37.524 1.00 48.31 A C
ANISOU 1877 CB ALA A 241 8314 2445 7598 689 2649 -864 A C
ATOM 1878 N GLU A 242 -18.143 16.368 38.709 1.00 49.80 A N
ANISOU 1878 N GLU A 242 8919 2521 7483 618 2736 -538 A N
ATOM 1879 CA GLU A 242 -19.501 15.821 38.572 1.00 50.07 A C
ANISOU 1879 CA GLU A 242 9075 2475 7474 472 2808 -336 A C
ATOM 1880 C GLU A 242 -20.398 16.263 39.707 1.00 57.83 A C
ANISOU 1880 C GLU A 242 10029 3469 8476 460 2897 -355 A C
ATOM 1881 O GLU A 242 -21.585 16.501 39.484 1.00 58.53 A O
ANISOU 1881 O GLU A 242 10051 3526 8663 309 2980 -217 A O
ATOM 1882 CB GLU A 242 -19.482 14.292 38.521 1.00 51.53 A C
ANISOU 1882 CB GLU A 242 9587 2609 7384 502 2790 -250 A C
ATOM 1883 CG GLU A 242 -19.217 13.695 37.159 1.00 54.97 A C
ANISOU 1883 CG GLU A 242 10076 2996 7812 410 2753 -158 A C
ATOM 1884 CD GLU A 242 -19.332 12.179 37.141 1.00 71.48 A C
ANISOU 1884 CD GLU A 242 12521 4990 9648 408 2795 -80 A C
ATOM 1885 OE1 GLU A 242 -18.759 11.523 38.044 1.00 57.94 A O
ANISOU 1885 OE1 GLU A 242 11024 3261 7728 621 2797 -133 A O
ATOM 1886 OE2 GLU A 242 -20.007 11.645 36.228 1.00 51.23 A O1-
ANISOU 1886 OE2 GLU A 242 10016 2372 7078 195 2847 31 A O1-
ATOM 1887 N ASP A 243 -19.830 16.379 40.926 1.00 56.24 A N
ANISOU 1887 N ASP A 243 9857 3347 8166 625 2879 -532 A N
ATOM 1888 CA ASP A 243 -20.522 16.849 42.130 1.00 56.66 A C
ANISOU 1888 CA ASP A 243 9877 3432 8221 635 2962 -592 A C
ATOM 1889 C ASP A 243 -20.993 18.297 41.944 1.00 61.08 A C
ANISOU 1889 C ASP A 243 10149 3958 9100 526 3059 -628 A C
ATOM 1890 O ASP A 243 -22.068 18.675 42.410 1.00 61.50 A O
ANISOU 1890 O ASP A 243 10159 3983 9225 456 3164 -567 A O
ATOM 1891 CB ASP A 243 -19.579 16.755 43.353 1.00 59.61 A C
ANISOU 1891 CB ASP A 243 10300 3959 8392 851 2908 -807 A C
ATOM 1892 CG ASP A 243 -19.166 15.359 43.793 1.00 70.41 A C
ANISOU 1892 CG ASP A 243 11972 5367 9414 1033 2852 -748 A C
ATOM 1893 OD1 ASP A 243 -18.444 15.248 44.810 1.00 72.65 A O
ANISOU 1893 OD1 ASP A 243 12282 5827 9493 1247 2805 -898 A O
ATOM 1894 OD2 ASP A 243 -19.580 14.377 43.136 1.00 76.79 A O1-
ANISOU 1894 OD2 ASP A 243 12992 6040 10145 965 2874 -555 A O1-
ATOM 1895 N LEU A 244 -20.184 19.087 41.226 1.00 57.27 A N
ANISOU 1895 N LEU A 244 9483 3467 8812 518 3046 -717 A N
ATOM 1896 CA LEU A 244 -20.396 20.502 40.946 1.00 57.16 A C
ANISOU 1896 CA LEU A 244 9218 3381 9118 443 3177 -756 A C
ATOM 1897 C LEU A 244 -21.265 20.761 39.715 1.00 57.72 A C
ANISOU 1897 C LEU A 244 9200 3363 9368 328 3242 -489 A C
ATOM 1898 O LEU A 244 -22.175 21.585 39.788 1.00 57.73 A O
ANISOU 1898 O LEU A 244 9074 3312 9549 284 3385 -403 A O
ATOM 1899 CB LEU A 244 -19.027 21.170 40.729 1.00 58.27 A C
ANISOU 1899 CB LEU A 244 9219 3553 9369 483 3160 -991 A C
ATOM 1900 CG LEU A 244 -18.261 21.761 41.930 1.00 66.86 A C
ANISOU 1900 CG LEU A 244 10219 4755 10429 546 3188 -1331 A C
ATOM 1901 CD1 LEU A 244 -18.229 20.823 43.141 1.00 68.62 A C
ANISOU 1901 CD1 LEU A 244 10615 5145 10314 678 3086 -1402 A C
ATOM 1902 CD2 LEU A 244 -16.838 22.047 41.538 1.00 71.13 A C
ANISOU 1902 CD2 LEU A 244 10645 5380 11002 569 3134 -1552 A C
ATOM 1903 N ALA A 245 -20.971 20.102 38.577 1.00 51.78 A N
ANISOU 1903 N ALA A 245 8498 2617 8558 294 3147 -360 A N
ATOM 1904 CA ALA A 245 -21.644 20.386 37.308 1.00 49.65 A C
ANISOU 1904 CA ALA A 245 8107 2327 8430 199 3196 -122 A C
ATOM 1905 C ALA A 245 -22.798 19.461 36.939 1.00 51.59 A C
ANISOU 1905 C ALA A 245 8445 2640 8516 89 3172 93 A C
ATOM 1906 O ALA A 245 -23.675 19.872 36.182 1.00 50.26 A O
ANISOU 1906 O ALA A 245 8124 2521 8451 19 3239 288 A O
ATOM 1907 CB ALA A 245 -20.631 20.371 36.195 1.00 49.30 A C
ANISOU 1907 CB ALA A 245 8020 2274 8437 206 3128 -127 A C
ATOM 1908 N GLY A 246 -22.779 18.235 37.433 1.00 48.68 A N
ANISOU 1908 N GLY A 246 8318 2288 7890 77 3095 55 A N
ATOM 1909 CA GLY A 246 -23.782 17.231 37.099 1.00 48.24 A C
ANISOU 1909 CA GLY A 246 8381 2282 7667 -69 3098 209 A C
ATOM 1910 C GLY A 246 -23.152 16.038 36.412 1.00 50.63 A C
ANISOU 1910 C GLY A 246 8886 2566 7783 -105 3006 209 A C
ATOM 1911 O GLY A 246 -21.923 15.962 36.355 1.00 50.06 A O
ANISOU 1911 O GLY A 246 8872 2453 7694 21 2928 93 A O
ATOM 1912 N PRO A 247 -23.951 15.100 35.849 1.00 47.12 A N
ANISOU 1912 N PRO A 247 8544 2163 7195 -286 3028 322 A N
ATOM 1913 CA PRO A 247 -23.358 13.886 35.251 1.00 46.44 A C
ANISOU 1913 CA PRO A 247 8694 2023 6927 -330 2980 302 A C
ATOM 1914 C PRO A 247 -22.459 14.101 34.039 1.00 47.24 A C
ANISOU 1914 C PRO A 247 8690 2150 7111 -307 2894 309 A C
ATOM 1915 O PRO A 247 -22.676 15.019 33.243 1.00 46.44 A O
ANISOU 1915 O PRO A 247 8317 2143 7185 -342 2890 394 A O
ATOM 1916 CB PRO A 247 -24.581 13.062 34.843 1.00 49.29 A C
ANISOU 1916 CB PRO A 247 9126 2445 7155 -588 3062 397 A C
ATOM 1917 CG PRO A 247 -25.690 13.566 35.702 1.00 54.13 A C
ANISOU 1917 CG PRO A 247 9627 3121 7817 -629 3145 438 A C
ATOM 1918 CD PRO A 247 -25.429 15.024 35.839 1.00 49.07 A C
ANISOU 1918 CD PRO A 247 8712 2515 7418 -468 3118 442 A C
ATOM 1919 N TYR A 248 -21.435 13.221 33.918 1.00 42.33 A N
ANISOU 1919 N TYR A 248 8295 1439 6347 -227 2840 230 A N
ATOM 1920 CA TYR A 248 -20.485 13.178 32.804 1.00 40.26 A C
ANISOU 1920 CA TYR A 248 7988 1190 6120 -203 2761 219 A C
ATOM 1921 C TYR A 248 -21.157 12.363 31.711 1.00 43.07 A C
ANISOU 1921 C TYR A 248 8403 1593 6367 -441 2795 311 A C
ATOM 1922 O TYR A 248 -21.466 11.198 31.934 1.00 44.36 A O
ANISOU 1922 O TYR A 248 8844 1672 6338 -530 2864 292 A O
ATOM 1923 CB TYR A 248 -19.137 12.573 33.261 1.00 40.32 A C
ANISOU 1923 CB TYR A 248 8206 1108 6004 16 2701 89 A C
ATOM 1924 CG TYR A 248 -18.050 12.573 32.205 1.00 38.47 A C
ANISOU 1924 CG TYR A 248 7885 962 5769 65 2620 56 A C
ATOM 1925 CD1 TYR A 248 -17.423 13.755 31.822 1.00 38.63 A C
ANISOU 1925 CD1 TYR A 248 7660 990 6029 128 2568 15 A C
ATOM 1926 CD2 TYR A 248 -17.606 11.383 31.632 1.00 38.87 A C
ANISOU 1926 CD2 TYR A 248 8184 939 5646 55 2621 57 A C
ATOM 1927 CE1 TYR A 248 -16.407 13.760 30.867 1.00 38.09 A C
ANISOU 1927 CE1 TYR A 248 7517 990 5965 167 2503 -17 A C
ATOM 1928 CE2 TYR A 248 -16.586 11.376 30.679 1.00 39.00 A C
ANISOU 1928 CE2 TYR A 248 8163 957 5699 110 2549 25 A C
ATOM 1929 CZ TYR A 248 -15.987 12.567 30.304 1.00 42.07 A C
ANISOU 1929 CZ TYR A 248 8281 1390 6314 168 2481 -13 A C
ATOM 1930 OH TYR A 248 -14.996 12.580 29.362 1.00 41.23 A O
ANISOU 1930 OH TYR A 248 8121 1312 6234 212 2421 -48 A O
ATOM 1931 N VAL A 249 -21.444 12.985 30.560 1.00 38.53 A N
ANISOU 1931 N VAL A 249 7566 1166 5908 -551 2772 408 A N
ATOM 1932 CA VAL A 249 -22.203 12.352 29.472 1.00 39.39 A C
ANISOU 1932 CA VAL A 249 7650 1409 5906 -803 2801 483 A C
ATOM 1933 C VAL A 249 -21.337 11.747 28.357 1.00 43.06 A C
ANISOU 1933 C VAL A 249 8201 1862 6299 -832 2749 447 A C
ATOM 1934 O VAL A 249 -21.865 11.062 27.485 1.00 46.77 A O
ANISOU 1934 O VAL A 249 8692 2437 6640 -1058 2783 464 A O
ATOM 1935 CB VAL A 249 -23.220 13.356 28.855 1.00 43.33 A C
ANISOU 1935 CB VAL A 249 7786 2152 6527 -891 2815 638 A C
ATOM 1936 CG1 VAL A 249 -24.246 13.829 29.882 1.00 43.19 A C
ANISOU 1936 CG1 VAL A 249 7689 2165 6555 -893 2889 679 A C
ATOM 1937 CG2 VAL A 249 -22.522 14.538 28.199 1.00 42.01 A C
ANISOU 1937 CG2 VAL A 249 7375 2020 6568 -726 2764 706 A C
ATOM 1938 N TRP A 250 -20.035 11.960 28.404 1.00 38.03 A N
ANISOU 1938 N TRP A 250 7568 1196 5687 -600 2674 357 A N
ATOM 1939 CA TRP A 250 -19.095 11.572 27.361 1.00 37.94 A C
ANISOU 1939 CA TRP A 250 7591 1196 5627 -584 2619 321 A C
ATOM 1940 C TRP A 250 -18.600 10.108 27.436 1.00 43.88 A C
ANISOU 1940 C TRP A 250 8770 1689 6214 -614 2666 249 A C
ATOM 1941 O TRP A 250 -17.856 9.674 26.549 1.00 41.58 A O
ANISOU 1941 O TRP A 250 8540 1383 5874 -608 2636 215 A O
ATOM 1942 CB TRP A 250 -17.917 12.530 27.394 1.00 36.29 A C
ANISOU 1942 CB TRP A 250 7158 1117 5515 -340 2539 257 A C
ATOM 1943 CG TRP A 250 -18.361 13.946 27.174 1.00 36.89 A C
ANISOU 1943 CG TRP A 250 6954 1192 5870 -347 2552 374 A C
ATOM 1944 CD1 TRP A 250 -18.672 14.872 28.129 1.00 39.20 A C
ANISOU 1944 CD1 TRP A 250 7203 1313 6377 -283 2596 401 A C
ATOM 1945 CD2 TRP A 250 -18.666 14.551 25.909 1.00 36.35 A C
ANISOU 1945 CD2 TRP A 250 6650 1259 5901 -428 2553 511 A C
ATOM 1946 CE2 TRP A 250 -19.079 15.878 26.169 1.00 40.59 A C
ANISOU 1946 CE2 TRP A 250 7003 1710 6709 -381 2617 640 A C
ATOM 1947 CE3 TRP A 250 -18.635 14.095 24.577 1.00 36.68 A C
ANISOU 1947 CE3 TRP A 250 6706 1333 5898 -576 2529 601 A C
ATOM 1948 NE1 TRP A 250 -19.056 16.054 27.532 1.00 39.14 A N
ANISOU 1948 NE1 TRP A 250 6909 1398 6566 -287 2642 532 A N
ATOM 1949 CZ2 TRP A 250 -19.438 16.762 25.142 1.00 39.84 A C
ANISOU 1949 CZ2 TRP A 250 6642 1760 6735 -390 2659 820 A C
ATOM 1950 CZ3 TRP A 250 -18.948 14.989 23.561 1.00 38.22 A C
ANISOU 1950 CZ3 TRP A 250 6624 1687 6210 -597 2546 773 A C
ATOM 1951 CH2 TRP A 250 -19.326 16.307 23.846 1.00 39.04 A C
ANISOU 1951 CH2 TRP A 250 6501 1807 6525 -485 2615 890 A C
ATOM 1952 N GLY A 251 -19.012 9.389 28.476 1.00 42.71 A N
ANISOU 1952 N GLY A 251 8876 1410 5942 -615 2756 216 A N
ATOM 1953 CA GLY A 251 -18.652 7.997 28.687 1.00 44.86 A C
ANISOU 1953 CA GLY A 251 9548 1485 6011 -597 2856 152 A C
ATOM 1954 C GLY A 251 -17.246 7.729 29.185 1.00 49.36 A C
ANISOU 1954 C GLY A 251 10294 1932 6531 -265 2808 88 A C
ATOM 1955 O GLY A 251 -17.078 7.020 30.175 1.00 53.31 A O
ANISOU 1955 O GLY A 251 11081 2282 6892 -106 2889 70 A O
ATOM 1956 N GLN A 252 -16.232 8.272 28.518 1.00 42.16 A N
ANISOU 1956 N GLN A 252 9207 1101 5712 -145 2688 59 A N
ATOM 1957 CA GLN A 252 -14.824 7.970 28.793 1.00 40.66 A C
ANISOU 1957 CA GLN A 252 9077 987 5386 155 2636 -11 A C
ATOM 1958 C GLN A 252 -14.009 9.249 28.937 1.00 41.54 A C
ANISOU 1958 C GLN A 252 8929 1113 5739 327 2493 -72 A C
ATOM 1959 O GLN A 252 -14.266 10.220 28.217 1.00 41.76 A O
ANISOU 1959 O GLN A 252 8665 1249 5952 187 2446 -38 A O
ATOM 1960 CB GLN A 252 -14.317 7.071 27.626 1.00 41.13 A C
ANISOU 1960 CB GLN A 252 9304 962 5360 92 2674 -25 A C
ATOM 1961 CG GLN A 252 -12.816 6.965 27.309 1.00 42.29 A C
ANISOU 1961 CG GLN A 252 9525 1009 5535 362 2595 -94 A C
ATOM 1962 CD GLN A 252 -12.619 6.656 25.829 1.00 53.68 A C
ANISOU 1962 CD GLN A 252 10939 2471 6986 194 2597 -95 A C
ATOM 1963 NE2 GLN A 252 -11.836 7.467 25.096 1.00 37.80 A N
ANISOU 1963 NE2 GLN A 252 8634 653 5075 254 2473 -120 A N
ATOM 1964 OE1 GLN A 252 -13.221 5.727 25.293 1.00 55.76 A O
ANISOU 1964 OE1 GLN A 252 11406 2636 7145 -24 2723 -82 A O
ATOM 1965 N TYR A 253 -13.044 9.266 29.872 1.00 37.89 A N
ANISOU 1965 N TYR A 253 8338 1025 5032 566 2438 -115 A N
ATOM 1966 CA TYR A 253 -12.161 10.427 30.019 1.00 37.72 A C
ANISOU 1966 CA TYR A 253 8040 1105 5188 691 2323 -214 A C
ATOM 1967 C TYR A 253 -10.715 9.950 29.930 1.00 41.19 A C
ANISOU 1967 C TYR A 253 8701 1299 5651 1015 2270 -370 A C
ATOM 1968 O TYR A 253 -10.148 9.544 30.934 1.00 42.37 A O
ANISOU 1968 O TYR A 253 8971 1495 5631 1277 2259 -431 A O
ATOM 1969 CB TYR A 253 -12.423 11.252 31.315 1.00 38.09 A C
ANISOU 1969 CB TYR A 253 7995 1135 5343 781 2313 -291 A C
ATOM 1970 CG TYR A 253 -11.628 12.540 31.323 1.00 39.22 A C
ANISOU 1970 CG TYR A 253 7890 1247 5763 872 2248 -470 A C
ATOM 1971 CD1 TYR A 253 -12.072 13.658 30.628 1.00 40.03 A C
ANISOU 1971 CD1 TYR A 253 7753 1309 6149 692 2275 -442 A C
ATOM 1972 CD2 TYR A 253 -10.388 12.616 31.952 1.00 40.95 A C
ANISOU 1972 CD2 TYR A 253 8077 1569 5912 1128 2179 -658 A C
ATOM 1973 CE1 TYR A 253 -11.306 14.821 30.560 1.00 42.86 A C
ANISOU 1973 CE1 TYR A 253 7837 1751 6698 717 2261 -579 A C
ATOM 1974 CE2 TYR A 253 -9.606 13.771 31.878 1.00 41.78 A C
ANISOU 1974 CE2 TYR A 253 7873 1808 6195 1128 2142 -827 A C
ATOM 1975 CZ TYR A 253 -10.072 14.875 31.186 1.00 49.38 A C
ANISOU 1975 CZ TYR A 253 8612 2710 7442 911 2198 -790 A C
ATOM 1976 OH TYR A 253 -9.336 16.041 31.151 1.00 50.31 A O
ANISOU 1976 OH TYR A 253 8451 2915 7752 890 2213 -966 A O
ATOM 1977 N ASP A 254 -10.131 9.970 28.729 1.00 37.29 A N
ANISOU 1977 N ASP A 254 7968 1142 5058 872 2221 -293 A N
ATOM 1978 CA ASP A 254 -8.751 9.523 28.549 1.00 37.29 A C
ANISOU 1978 CA ASP A 254 8016 1209 4943 1097 2159 -365 A C
ATOM 1979 C ASP A 254 -7.819 10.719 28.455 1.00 42.73 A C
ANISOU 1979 C ASP A 254 8502 1779 5956 1250 2085 -612 A C
ATOM 1980 O ASP A 254 -8.274 11.828 28.178 1.00 38.60 A O
ANISOU 1980 O ASP A 254 7700 1334 5632 1035 2084 -587 A O
ATOM 1981 CB ASP A 254 -8.633 8.668 27.282 1.00 37.75 A C
ANISOU 1981 CB ASP A 254 8248 1150 4944 1020 2210 -310 A C
ATOM 1982 CG ASP A 254 -9.064 7.214 27.396 1.00 48.41 A C
ANISOU 1982 CG ASP A 254 10165 2002 6227 1133 2359 -310 A C
ATOM 1983 OD1 ASP A 254 -9.632 6.834 28.451 1.00 49.32 A O
ANISOU 1983 OD1 ASP A 254 10460 2039 6240 1198 2429 -272 A O
ATOM 1984 OD2 ASP A 254 -8.828 6.454 26.431 1.00 49.71 A O1-
ANISOU 1984 OD2 ASP A 254 10488 2076 6324 1077 2417 -287 A O1-
ATOM 1985 N LEU A 255 -6.507 10.491 28.665 1.00 44.49 A N
ANISOU 1985 N LEU A 255 8698 2151 6056 1511 2020 -740 A N
ATOM 1986 CA LEU A 255 -5.494 11.548 28.532 1.00 44.84 A C
ANISOU 1986 CA LEU A 255 8404 2398 6237 1541 1947 -922 A C
ATOM 1987 C LEU A 255 -4.432 11.116 27.550 1.00 48.03 A C
ANISOU 1987 C LEU A 255 8806 2858 6584 1628 1912 -952 A C
ATOM 1988 O LEU A 255 -4.086 9.946 27.505 1.00 45.87 A O
ANISOU 1988 O LEU A 255 8794 2544 6089 1816 1924 -893 A O
ATOM 1989 CB LEU A 255 -4.827 11.919 29.871 1.00 46.48 A C
ANISOU 1989 CB LEU A 255 8481 2839 6342 1765 1891 -1115 A C
ATOM 1990 CG LEU A 255 -5.677 12.477 31.003 1.00 51.84 A C
ANISOU 1990 CG LEU A 255 9118 3512 7067 1708 1921 -1138 A C
ATOM 1991 CD1 LEU A 255 -4.868 12.550 32.263 1.00 54.88 A C
ANISOU 1991 CD1 LEU A 255 9413 4180 7260 1975 1858 -1332 A C
ATOM 1992 CD2 LEU A 255 -6.119 13.874 30.718 1.00 53.18 A C
ANISOU 1992 CD2 LEU A 255 9007 3644 7556 1440 1967 -1199 A C
ATOM 1993 N LEU A 256 -3.889 12.066 26.792 1.00 46.82 A N
ANISOU 1993 N LEU A 256 8368 2789 6631 1505 1892 -1045 A N
ATOM 1994 CA LEU A 256 -2.815 11.799 25.847 1.00 47.69 A C
ANISOU 1994 CA LEU A 256 8431 2980 6709 1574 1860 -1095 A C
ATOM 1995 C LEU A 256 -1.718 12.851 26.019 1.00 54.14 A C
ANISOU 1995 C LEU A 256 8898 4035 7639 1603 1821 -1335 A C
ATOM 1996 O LEU A 256 -1.994 14.044 25.891 1.00 53.71 A O
ANISOU 1996 O LEU A 256 8615 3954 7837 1391 1874 -1387 A O
ATOM 1997 CB LEU A 256 -3.356 11.776 24.408 1.00 46.57 A C
ANISOU 1997 CB LEU A 256 8324 2673 6697 1329 1910 -935 A C
ATOM 1998 CG LEU A 256 -2.335 11.507 23.312 1.00 51.46 A C
ANISOU 1998 CG LEU A 256 8903 3358 7293 1370 1889 -971 A C
ATOM 1999 CD1 LEU A 256 -2.369 10.078 22.879 1.00 52.03 A C
ANISOU 1999 CD1 LEU A 256 9308 3315 7144 1463 1914 -865 A C
ATOM 2000 CD2 LEU A 256 -2.608 12.363 22.129 1.00 52.59 A C
ANISOU 2000 CD2 LEU A 256 8857 3458 7668 1112 1931 -901 A C
ATOM 2001 N ILE A 257 -0.485 12.409 26.324 1.00 53.12 A N
ANISOU 2001 N ILE A 257 8724 4143 7315 1868 1751 -1486 A N
ATOM 2002 CA ILE A 257 0.636 13.336 26.488 1.00 54.33 A C
ANISOU 2002 CA ILE A 257 8525 4575 7542 1881 1720 -1758 A C
ATOM 2003 C ILE A 257 1.418 13.344 25.166 1.00 55.29 A C
ANISOU 2003 C ILE A 257 8560 4708 7738 1823 1727 -1766 A C
ATOM 2004 O ILE A 257 1.971 12.335 24.732 1.00 53.73 A O
ANISOU 2004 O ILE A 257 8515 4552 7347 2020 1688 -1710 A O
ATOM 2005 CB ILE A 257 1.496 13.073 27.761 1.00 60.56 A C
ANISOU 2005 CB ILE A 257 9227 5718 8066 2194 1635 -1960 A C
ATOM 2006 CG1 ILE A 257 0.674 13.398 29.050 1.00 61.66 A C
ANISOU 2006 CG1 ILE A 257 9382 5858 8186 2185 1645 -1986 A C
ATOM 2007 CG2 ILE A 257 2.792 13.915 27.762 1.00 63.06 A C
ANISOU 2007 CG2 ILE A 257 9154 6381 8427 2187 1606 -2279 A C
ATOM 2008 CD1 ILE A 257 -0.242 12.268 29.571 1.00 70.38 A C
ANISOU 2008 CD1 ILE A 257 10873 6776 9093 2343 1654 -1740 A C
ATOM 2009 N LEU A 258 1.387 14.510 24.510 1.00 50.18 A N
ANISOU 2009 N LEU A 258 7688 3996 7383 1548 1805 -1816 A N
ATOM 2010 CA LEU A 258 1.956 14.756 23.192 1.00 48.74 A C
ANISOU 2010 CA LEU A 258 7399 3791 7327 1431 1844 -1805 A C
ATOM 2011 C LEU A 258 3.454 15.075 23.207 1.00 54.01 A C
ANISOU 2011 C LEU A 258 7797 4770 7954 1526 1815 -2088 A C
ATOM 2012 O LEU A 258 4.004 15.313 24.279 1.00 55.52 A O
ANISOU 2012 O LEU A 258 7829 5217 8050 1639 1773 -2320 A O
ATOM 2013 CB LEU A 258 1.208 15.950 22.572 1.00 46.75 A C
ANISOU 2013 CB LEU A 258 7021 3336 7404 1120 1976 -1720 A C
ATOM 2014 CG LEU A 258 -0.152 15.724 21.931 1.00 47.23 A C
ANISOU 2014 CG LEU A 258 7281 3134 7531 982 2018 -1411 A C
ATOM 2015 CD1 LEU A 258 -0.134 14.612 20.920 1.00 44.35 A C
ANISOU 2015 CD1 LEU A 258 7124 2721 7004 1033 1969 -1251 A C
ATOM 2016 CD2 LEU A 258 -1.233 15.615 22.960 1.00 47.29 A C
ANISOU 2016 CD2 LEU A 258 7417 3049 7502 987 2012 -1336 A C
ATOM 2017 N PRO A 259 4.115 15.171 22.027 1.00 50.43 A N
ANISOU 2017 N PRO A 259 7257 4331 7572 1461 1845 -2093 A N
ATOM 2018 CA PRO A 259 5.528 15.587 22.008 1.00 52.40 A C
ANISOU 2018 CA PRO A 259 7211 4897 7803 1512 1836 -2387 A C
ATOM 2019 C PRO A 259 5.662 17.043 22.491 1.00 57.19 A C
ANISOU 2019 C PRO A 259 7511 5557 8661 1268 1955 -2631 A C
ATOM 2020 O PRO A 259 4.631 17.727 22.576 1.00 55.67 A O
ANISOU 2020 O PRO A 259 7365 5105 8681 1073 2057 -2515 A O
ATOM 2021 CB PRO A 259 5.916 15.422 20.523 1.00 53.71 A C
ANISOU 2021 CB PRO A 259 7395 4987 8026 1449 1870 -2284 A C
ATOM 2022 CG PRO A 259 4.849 14.521 19.917 1.00 56.01 A C
ANISOU 2022 CG PRO A 259 8034 4985 8263 1448 1857 -1949 A C
ATOM 2023 CD PRO A 259 3.622 14.931 20.652 1.00 50.79 A C
ANISOU 2023 CD PRO A 259 7445 4143 7709 1327 1893 -1849 A C
ATOM 2024 N PRO A 260 6.874 17.563 22.830 1.00 55.84 A N
ANISOU 2024 N PRO A 260 7024 5717 8475 1263 1968 -2978 A N
ATOM 2025 CA PRO A 260 6.959 18.955 23.343 1.00 56.28 A C
ANISOU 2025 CA PRO A 260 6809 5795 8778 992 2126 -3246 A C
ATOM 2026 C PRO A 260 6.475 20.041 22.373 1.00 57.81 A C
ANISOU 2026 C PRO A 260 6982 5633 9350 671 2351 -3130 A C
ATOM 2027 O PRO A 260 6.249 21.171 22.804 1.00 58.43 A O
ANISOU 2027 O PRO A 260 6921 5617 9663 448 2528 -3283 A O
ATOM 2028 CB PRO A 260 8.449 19.141 23.652 1.00 60.77 A C
ANISOU 2028 CB PRO A 260 7041 6825 9224 1037 2100 -3646 A C
ATOM 2029 CG PRO A 260 9.002 17.766 23.768 1.00 66.08 A C
ANISOU 2029 CG PRO A 260 7819 7770 9520 1424 1888 -3579 A C
ATOM 2030 CD PRO A 260 8.203 16.914 22.824 1.00 59.15 A C
ANISOU 2030 CD PRO A 260 7307 6528 8638 1501 1856 -3164 A C
ATOM 2031 N SER A 261 6.268 19.692 21.095 1.00 51.94 A N
ANISOU 2031 N SER A 261 6389 4691 8655 661 2362 -2850 A N
ATOM 2032 CA SER A 261 5.823 20.607 20.044 1.00 50.67 A C
ANISOU 2032 CA SER A 261 6222 4225 8807 417 2571 -2680 A C
ATOM 2033 C SER A 261 4.311 20.951 20.123 1.00 54.77 A C
ANISOU 2033 C SER A 261 6918 4414 9479 331 2651 -2390 A C
ATOM 2034 O SER A 261 3.874 21.840 19.387 1.00 56.15 A O
ANISOU 2034 O SER A 261 7076 4349 9911 159 2849 -2232 A O
ATOM 2035 CB SER A 261 6.172 20.040 18.669 1.00 51.36 A C
ANISOU 2035 CB SER A 261 6391 4284 8841 460 2537 -2489 A C
ATOM 2036 OG SER A 261 5.575 18.780 18.408 1.00 52.60 A O
ANISOU 2036 OG SER A 261 6824 4390 8774 643 2364 -2225 A O
ATOM 2037 N PHE A 262 3.521 20.300 21.021 1.00 48.88 A N
ANISOU 2037 N PHE A 262 6332 3666 8574 461 2517 -2313 A N
ATOM 2038 CA PHE A 262 2.088 20.616 21.176 1.00 46.66 A C
ANISOU 2038 CA PHE A 262 6195 3116 8419 387 2586 -2060 A C
ATOM 2039 C PHE A 262 1.943 22.123 21.528 1.00 50.87 A C
ANISOU 2039 C PHE A 262 6551 3505 9271 175 2841 -2194 A C
ATOM 2040 O PHE A 262 2.623 22.596 22.445 1.00 51.26 A O
ANISOU 2040 O PHE A 262 6425 3712 9337 131 2882 -2541 A O
ATOM 2041 CB PHE A 262 1.414 19.697 22.221 1.00 47.50 A C
ANISOU 2041 CB PHE A 262 6483 3274 8289 555 2414 -2012 A C
ATOM 2042 CG PHE A 262 -0.054 19.943 22.519 1.00 47.36 A C
ANISOU 2042 CG PHE A 262 6601 3026 8368 488 2469 -1778 A C
ATOM 2043 CD1 PHE A 262 -0.976 20.088 21.492 1.00 48.75 A C
ANISOU 2043 CD1 PHE A 262 6868 2997 8656 396 2542 -1456 A C
ATOM 2044 CD2 PHE A 262 -0.522 19.945 23.826 1.00 48.72 A C
ANISOU 2044 CD2 PHE A 262 6803 3228 8479 537 2437 -1873 A C
ATOM 2045 CE1 PHE A 262 -2.323 20.338 21.768 1.00 48.24 A C
ANISOU 2045 CE1 PHE A 262 6893 2768 8666 345 2595 -1245 A C
ATOM 2046 CE2 PHE A 262 -1.873 20.164 24.099 1.00 50.54 A C
ANISOU 2046 CE2 PHE A 262 7147 3261 8795 478 2492 -1660 A C
ATOM 2047 CZ PHE A 262 -2.763 20.362 23.066 1.00 47.27 A C
ANISOU 2047 CZ PHE A 262 6801 2654 8504 383 2570 -1349 A C
ATOM 2048 N PRO A 263 1.149 22.894 20.733 1.00 46.86 A N
ANISOU 2048 N PRO A 263 6077 2719 9011 46 3037 -1933 A N
ATOM 2049 CA PRO A 263 1.107 24.361 20.916 1.00 47.97 A C
ANISOU 2049 CA PRO A 263 6074 2674 9478 -144 3343 -2046 A C
ATOM 2050 C PRO A 263 0.403 24.873 22.167 1.00 50.86 A C
ANISOU 2050 C PRO A 263 6443 2959 9923 -180 3413 -2145 A C
ATOM 2051 O PRO A 263 0.442 26.076 22.399 1.00 49.45 A O
ANISOU 2051 O PRO A 263 6156 2618 10015 -343 3693 -2283 A O
ATOM 2052 CB PRO A 263 0.352 24.850 19.675 1.00 49.61 A C
ANISOU 2052 CB PRO A 263 6352 2628 9871 -192 3517 -1663 A C
ATOM 2053 CG PRO A 263 -0.480 23.691 19.273 1.00 52.54 A C
ANISOU 2053 CG PRO A 263 6909 3049 10005 -49 3281 -1350 A C
ATOM 2054 CD PRO A 263 0.372 22.491 19.542 1.00 47.24 A C
ANISOU 2054 CD PRO A 263 6274 2636 9038 74 3013 -1538 A C
ATOM 2055 N TYR A 264 -0.259 23.999 22.937 1.00 48.24 A N
ANISOU 2055 N TYR A 264 6247 2715 9367 -37 3195 -2073 A N
ATOM 2056 CA TYR A 264 -0.982 24.413 24.142 1.00 47.86 A C
ANISOU 2056 CA TYR A 264 6211 2604 9370 -59 3248 -2153 A C
ATOM 2057 C TYR A 264 -0.594 23.531 25.322 1.00 50.06 A C
ANISOU 2057 C TYR A 264 6498 3173 9348 83 3010 -2386 A C
ATOM 2058 O TYR A 264 0.252 22.654 25.181 1.00 46.69 A O
ANISOU 2058 O TYR A 264 6065 2986 8689 210 2825 -2478 A O
ATOM 2059 CB TYR A 264 -2.513 24.419 23.905 1.00 47.17 A C
ANISOU 2059 CB TYR A 264 6293 2285 9344 -30 3282 -1755 A C
ATOM 2060 CG TYR A 264 -2.923 25.365 22.799 1.00 48.77 A C
ANISOU 2060 CG TYR A 264 6467 2236 9825 -125 3541 -1506 A C
ATOM 2061 CD1 TYR A 264 -3.044 24.919 21.488 1.00 49.61 A C
ANISOU 2061 CD1 TYR A 264 6632 2337 9880 -82 3490 -1216 A C
ATOM 2062 CD2 TYR A 264 -3.113 26.725 23.048 1.00 50.21 A C
ANISOU 2062 CD2 TYR A 264 6565 2195 10318 -249 3863 -1572 A C
ATOM 2063 CE1 TYR A 264 -3.344 25.797 20.451 1.00 49.92 A C
ANISOU 2063 CE1 TYR A 264 6635 2184 10148 -135 3737 -974 A C
ATOM 2064 CE2 TYR A 264 -3.432 27.609 22.020 1.00 50.77 A C
ANISOU 2064 CE2 TYR A 264 6625 2027 10639 -295 4138 -1319 A C
ATOM 2065 CZ TYR A 264 -3.540 27.138 20.721 1.00 53.62 A C
ANISOU 2065 CZ TYR A 264 7032 2418 10922 -225 4066 -1010 A C
ATOM 2066 OH TYR A 264 -3.892 27.974 19.699 1.00 52.30 A O
ANISOU 2066 OH TYR A 264 6855 2051 10967 -231 4334 -724 A O
ATOM 2067 N GLY A 265 -1.138 23.847 26.491 1.00 48.63 A N
ANISOU 2067 N GLY A 265 6316 2982 9178 69 3043 -2495 A N
ATOM 2068 CA GLY A 265 -0.887 23.089 27.709 1.00 48.72 A C
ANISOU 2068 CA GLY A 265 6339 3275 8898 223 2841 -2691 A C
ATOM 2069 C GLY A 265 -1.872 21.951 27.864 1.00 48.69 A C
ANISOU 2069 C GLY A 265 6598 3224 8676 400 2657 -2381 A C
ATOM 2070 O GLY A 265 -1.517 20.872 28.344 1.00 46.20 A O
ANISOU 2070 O GLY A 265 6372 3128 8054 602 2454 -2417 A O
ATOM 2071 N GLY A 266 -3.120 22.230 27.472 1.00 44.90 A N
ANISOU 2071 N GLY A 266 6240 2464 8357 326 2754 -2078 A N
ATOM 2072 CA GLY A 266 -4.235 21.292 27.507 1.00 42.85 A C
ANISOU 2072 CA GLY A 266 6217 2127 7937 426 2631 -1778 A C
ATOM 2073 C GLY A 266 -5.257 21.573 26.421 1.00 44.53 A C
ANISOU 2073 C GLY A 266 6494 2104 8320 330 2733 -1429 A C
ATOM 2074 O GLY A 266 -5.426 22.721 26.001 1.00 39.97 A O
ANISOU 2074 O GLY A 266 5786 1385 8016 201 2943 -1388 A O
ATOM 2075 N MET A 267 -5.892 20.496 25.909 1.00 41.86 A N
ANISOU 2075 N MET A 267 6348 1758 7799 394 2600 -1173 A N
ATOM 2076 CA MET A 267 -6.933 20.560 24.883 1.00 40.77 A C
ANISOU 2076 CA MET A 267 6260 1488 7743 316 2660 -841 A C
ATOM 2077 C MET A 267 -8.011 19.523 25.234 1.00 42.84 A C
ANISOU 2077 C MET A 267 6728 1754 7795 353 2545 -670 A C
ATOM 2078 O MET A 267 -7.740 18.328 25.257 1.00 42.81 A O
ANISOU 2078 O MET A 267 6893 1827 7547 433 2402 -680 A O
ATOM 2079 CB MET A 267 -6.353 20.368 23.459 1.00 42.21 A C
ANISOU 2079 CB MET A 267 6415 1695 7929 291 2648 -740 A C
ATOM 2080 CG MET A 267 -7.382 20.511 22.349 1.00 44.26 A C
ANISOU 2080 CG MET A 267 6682 1886 8249 219 2713 -404 A C
ATOM 2081 SD MET A 267 -8.264 22.080 22.337 1.00 48.16 A S
ANISOU 2081 SD MET A 267 7017 2216 9065 154 2976 -243 A S
ATOM 2082 CE MET A 267 -9.893 21.490 21.968 1.00 43.76 A C
ANISOU 2082 CE MET A 267 6548 1709 8368 142 2916 97 A C
ATOM 2083 N GLU A 268 -9.227 20.025 25.524 1.00 38.65 A N
ANISOU 2083 N GLU A 268 6141 1219 7327 276 2636 -501 A N
ATOM 2084 CA GLU A 268 -10.426 19.324 25.987 1.00 36.83 A C
ANISOU 2084 CA GLU A 268 5976 1157 6861 245 2579 -329 A C
ATOM 2085 C GLU A 268 -11.102 18.444 24.917 1.00 39.44 A C
ANISOU 2085 C GLU A 268 6541 1267 7178 220 2521 -131 A C
ATOM 2086 O GLU A 268 -12.328 18.303 24.946 1.00 40.03 A O
ANISOU 2086 O GLU A 268 6649 1344 7217 153 2544 39 A O
ATOM 2087 CB GLU A 268 -11.445 20.375 26.517 1.00 37.57 A C
ANISOU 2087 CB GLU A 268 5979 1132 7164 208 2732 -260 A C
ATOM 2088 CG GLU A 268 -12.052 21.292 25.458 1.00 42.68 A C
ANISOU 2088 CG GLU A 268 6594 1486 8136 179 2889 -46 A C
ATOM 2089 CD GLU A 268 -11.435 22.669 25.291 1.00 58.15 A C
ANISOU 2089 CD GLU A 268 8380 3328 10384 172 3088 -128 A C
ATOM 2090 OE1 GLU A 268 -10.205 22.801 25.476 1.00 49.85 A O
ANISOU 2090 OE1 GLU A 268 7295 2288 9360 177 3074 -382 A O
ATOM 2091 OE2 GLU A 268 -12.190 23.623 24.996 1.00 45.75 A O1-
ANISOU 2091 OE2 GLU A 268 6710 1661 9013 166 3278 61 A O1-
ATOM 2092 N ASN A 269 -10.347 17.824 24.005 1.00 36.06 A N
ANISOU 2092 N ASN A 269 6029 1154 6519 200 2447 -117 A N
ATOM 2093 CA ASN A 269 -10.986 16.979 23.001 1.00 36.04 A C
ANISOU 2093 CA ASN A 269 6147 1153 6392 126 2403 50 A C
ATOM 2094 C ASN A 269 -11.880 15.936 23.703 1.00 39.60 A C
ANISOU 2094 C ASN A 269 6916 1388 6742 102 2356 73 A C
ATOM 2095 O ASN A 269 -11.416 15.293 24.648 1.00 39.80 A O
ANISOU 2095 O ASN A 269 7108 1372 6641 208 2303 -77 A O
ATOM 2096 CB ASN A 269 -9.969 16.319 22.049 1.00 37.91 A C
ANISOU 2096 CB ASN A 269 6534 1250 6619 153 2334 0 A C
ATOM 2097 CG ASN A 269 -8.972 17.292 21.475 1.00 45.77 A C
ANISOU 2097 CG ASN A 269 7345 2233 7813 190 2388 -66 A C
ATOM 2098 ND2 ASN A 269 -9.414 18.170 20.590 1.00 29.72 A N
ANISOU 2098 ND2 ASN A 269 4757 977 5559 99 2493 99 A N
ATOM 2099 OD1 ASN A 269 -7.796 17.262 21.829 1.00 40.78 A O
ANISOU 2099 OD1 ASN A 269 6712 1613 7169 287 2348 -273 A O
ATOM 2100 N PRO A 270 -13.188 15.845 23.338 1.00 35.53 A N
ANISOU 2100 N PRO A 270 6285 1117 6097 -25 2392 240 A N
ATOM 2101 CA PRO A 270 -14.101 14.909 24.041 1.00 34.72 A C
ANISOU 2101 CA PRO A 270 6342 1072 5777 -82 2380 236 A C
ATOM 2102 C PRO A 270 -13.575 13.486 24.059 1.00 37.54 A C
ANISOU 2102 C PRO A 270 7109 1134 6022 -82 2328 161 A C
ATOM 2103 O PRO A 270 -13.046 13.055 23.048 1.00 37.96 A O
ANISOU 2103 O PRO A 270 7200 1198 6026 -115 2301 164 A O
ATOM 2104 CB PRO A 270 -15.397 15.001 23.234 1.00 35.69 A C
ANISOU 2104 CB PRO A 270 6436 1158 5966 -263 2422 446 A C
ATOM 2105 CG PRO A 270 -15.343 16.309 22.564 1.00 40.57 A C
ANISOU 2105 CG PRO A 270 6821 1749 6843 -237 2481 593 A C
ATOM 2106 CD PRO A 270 -13.892 16.578 22.268 1.00 35.91 A C
ANISOU 2106 CD PRO A 270 6183 1150 6312 -117 2456 458 A C
ATOM 2107 N CYS A 271 -13.651 12.782 25.202 1.00 35.53 A N
ANISOU 2107 N CYS A 271 6926 1089 5486 -5 2332 69 A N
ATOM 2108 CA CYS A 271 -13.156 11.388 25.380 1.00 37.67 A C
ANISOU 2108 CA CYS A 271 7592 1120 5599 54 2328 3 A C
ATOM 2109 C CYS A 271 -11.608 11.266 25.368 1.00 42.31 A C
ANISOU 2109 C CYS A 271 8304 1520 6253 283 2262 -127 A C
ATOM 2110 O CYS A 271 -11.116 10.203 25.717 1.00 44.20 A O
ANISOU 2110 O CYS A 271 8810 1680 6303 415 2273 -183 A O
ATOM 2111 CB CYS A 271 -13.767 10.407 24.375 1.00 38.46 A C
ANISOU 2111 CB CYS A 271 7871 1145 5596 -155 2378 64 A C
ATOM 2112 SG CYS A 271 -15.552 10.577 24.146 1.00 42.50 A S
ANISOU 2112 SG CYS A 271 8324 1659 6166 -455 2448 203 A S
ATOM 2113 N LEU A 272 -10.851 12.308 24.973 1.00 38.46 A N
ANISOU 2113 N LEU A 272 7545 1133 5934 332 2216 -171 A N
ATOM 2114 CA LEU A 272 -9.391 12.232 24.935 1.00 37.62 A C
ANISOU 2114 CA LEU A 272 7386 1149 5759 510 2153 -298 A C
ATOM 2115 C LEU A 272 -8.756 13.634 25.102 1.00 38.61 A C
ANISOU 2115 C LEU A 272 7249 1263 6159 569 2144 -416 A C
ATOM 2116 O LEU A 272 -8.553 14.354 24.124 1.00 37.84 A O
ANISOU 2116 O LEU A 272 6960 1196 6221 475 2166 -375 A O
ATOM 2117 CB LEU A 272 -8.964 11.562 23.620 1.00 37.52 A C
ANISOU 2117 CB LEU A 272 7456 1120 5678 459 2146 -265 A C
ATOM 2118 CG LEU A 272 -7.491 11.227 23.370 1.00 40.38 A C
ANISOU 2118 CG LEU A 272 7878 1458 6008 668 2094 -405 A C
ATOM 2119 CD1 LEU A 272 -7.000 10.110 24.256 1.00 39.27 A C
ANISOU 2119 CD1 LEU A 272 8016 1272 5634 907 2090 -475 A C
ATOM 2120 CD2 LEU A 272 -7.315 10.815 21.945 1.00 40.69 A C
ANISOU 2120 CD2 LEU A 272 7942 1502 6016 555 2104 -347 A C
ATOM 2121 N THR A 273 -8.454 14.014 26.348 1.00 35.64 A N
ANISOU 2121 N THR A 273 6698 1185 5658 629 2118 -483 A N
ATOM 2122 CA THR A 273 -7.799 15.281 26.625 1.00 36.04 A C
ANISOU 2122 CA THR A 273 6488 1280 5925 643 2136 -633 A C
ATOM 2123 C THR A 273 -6.315 15.200 26.152 1.00 38.93 A C
ANISOU 2123 C THR A 273 6887 1537 6369 830 2095 -870 A C
ATOM 2124 O THR A 273 -5.626 14.241 26.470 1.00 37.63 A O
ANISOU 2124 O THR A 273 6847 1496 5955 997 2013 -919 A O
ATOM 2125 CB THR A 273 -7.964 15.677 28.111 1.00 38.13 A C
ANISOU 2125 CB THR A 273 6806 1414 6266 773 2156 -819 A C
ATOM 2126 CG2 THR A 273 -6.924 16.717 28.563 1.00 34.82 A C
ANISOU 2126 CG2 THR A 273 6000 1379 5853 701 2136 -946 A C
ATOM 2127 OG1 THR A 273 -9.281 16.233 28.309 1.00 37.24 A O
ANISOU 2127 OG1 THR A 273 6590 1341 6220 586 2235 -638 A O
ATOM 2128 N PHE A 274 -5.846 16.200 25.383 1.00 37.55 A N
ANISOU 2128 N PHE A 274 6435 1459 6371 696 2144 -875 A N
ATOM 2129 CA PHE A 274 -4.451 16.270 24.930 1.00 38.06 A C
ANISOU 2129 CA PHE A 274 6403 1604 6452 786 2113 -1059 A C
ATOM 2130 C PHE A 274 -3.680 17.150 25.938 1.00 46.46 A C
ANISOU 2130 C PHE A 274 7270 2770 7613 848 2142 -1364 A C
ATOM 2131 O PHE A 274 -4.157 18.240 26.254 1.00 45.52 A O
ANISOU 2131 O PHE A 274 7009 2572 7714 715 2258 -1397 A O
ATOM 2132 CB PHE A 274 -4.397 16.847 23.500 1.00 38.55 A C
ANISOU 2132 CB PHE A 274 6362 1565 6719 648 2194 -959 A C
ATOM 2133 CG PHE A 274 -4.809 15.951 22.353 1.00 38.79 A C
ANISOU 2133 CG PHE A 274 6557 1548 6635 603 2158 -746 A C
ATOM 2134 CD1 PHE A 274 -5.435 14.731 22.584 1.00 42.04 A C
ANISOU 2134 CD1 PHE A 274 7233 1916 6824 645 2098 -648 A C
ATOM 2135 CD2 PHE A 274 -4.584 16.333 21.038 1.00 40.77 A C
ANISOU 2135 CD2 PHE A 274 6699 1798 6996 504 2206 -655 A C
ATOM 2136 CE1 PHE A 274 -5.810 13.906 21.522 1.00 42.40 A C
ANISOU 2136 CE1 PHE A 274 7423 1926 6760 563 2090 -496 A C
ATOM 2137 CE2 PHE A 274 -4.978 15.516 19.974 1.00 43.01 A C
ANISOU 2137 CE2 PHE A 274 7115 2073 7155 444 2176 -484 A C
ATOM 2138 CZ PHE A 274 -5.575 14.300 20.224 1.00 41.31 A C
ANISOU 2138 CZ PHE A 274 7154 1823 6719 462 2118 -423 A C
ATOM 2139 N VAL A 275 -2.560 16.654 26.513 1.00 46.39 A N
ANISOU 2139 N VAL A 275 7239 2983 7405 1042 2044 -1574 A N
ATOM 2140 CA VAL A 275 -1.774 17.390 27.530 1.00 48.67 A C
ANISOU 2140 CA VAL A 275 7296 3489 7708 1082 2052 -1892 A C
ATOM 2141 C VAL A 275 -0.300 17.542 27.093 1.00 53.09 A C
ANISOU 2141 C VAL A 275 7651 4276 8244 1129 2025 -2118 A C
ATOM 2142 O VAL A 275 0.262 16.631 26.496 1.00 50.14 A O
ANISOU 2142 O VAL A 275 7380 3970 7701 1275 1937 -2051 A O
ATOM 2143 CB VAL A 275 -1.852 16.744 28.939 1.00 54.45 A C
ANISOU 2143 CB VAL A 275 8132 4384 8172 1298 1957 -1972 A C
ATOM 2144 CG1 VAL A 275 -1.414 17.730 30.020 1.00 55.93 A C
ANISOU 2144 CG1 VAL A 275 8059 4772 8420 1256 2000 -2289 A C
ATOM 2145 CG2 VAL A 275 -3.254 16.223 29.243 1.00 53.72 A C
ANISOU 2145 CG2 VAL A 275 8310 4069 8031 1289 1967 -1710 A C
ATOM 2146 N THR A 276 0.310 18.701 27.411 1.00 52.58 A N
ANISOU 2146 N THR A 276 7298 4329 8353 993 2123 -2403 A N
ATOM 2147 CA THR A 276 1.715 19.035 27.112 1.00 54.07 A C
ANISOU 2147 CA THR A 276 7235 4768 8540 988 2127 -2680 A C
ATOM 2148 C THR A 276 2.673 18.272 28.050 1.00 60.48 A C
ANISOU 2148 C THR A 276 7981 5996 9001 1269 1962 -2899 A C
ATOM 2149 O THR A 276 2.326 18.079 29.215 1.00 61.15 A O
ANISOU 2149 O THR A 276 8107 6194 8935 1383 1909 -2954 A O
ATOM 2150 CB THR A 276 1.946 20.580 27.228 1.00 59.00 A C
ANISOU 2150 CB THR A 276 7583 5355 9481 705 2337 -2936 A C
ATOM 2151 CG2 THR A 276 1.765 21.117 28.644 1.00 53.26 A C
ANISOU 2151 CG2 THR A 276 6736 4766 8735 672 2372 -3195 A C
ATOM 2152 OG1 THR A 276 3.252 20.928 26.761 1.00 64.05 A O
ANISOU 2152 OG1 THR A 276 7985 6202 10150 646 2373 -3190 A O
ATOM 2153 N PRO A 277 3.902 17.895 27.628 1.00 58.79 A N
ANISOU 2153 N PRO A 277 7643 6053 8643 1398 1888 -3036 A N
ATOM 2154 CA PRO A 277 4.819 17.277 28.595 1.00 60.86 A C
ANISOU 2154 CA PRO A 277 7798 6773 8552 1698 1743 -3247 A C
ATOM 2155 C PRO A 277 5.492 18.340 29.495 1.00 67.57 A C
ANISOU 2155 C PRO A 277 8266 7971 9437 1563 1796 -3687 A C
ATOM 2156 O PRO A 277 6.187 17.978 30.445 1.00 68.48 A O
ANISOU 2156 O PRO A 277 8237 8538 9245 1799 1678 -3895 A O
ATOM 2157 CB PRO A 277 5.824 16.533 27.708 1.00 62.73 A C
ANISOU 2157 CB PRO A 277 8036 7159 8641 1878 1666 -3213 A C
ATOM 2158 CG PRO A 277 5.829 17.273 26.430 1.00 65.63 A C
ANISOU 2158 CG PRO A 277 8329 7272 9335 1574 1799 -3179 A C
ATOM 2159 CD PRO A 277 4.529 18.012 26.290 1.00 59.86 A C
ANISOU 2159 CD PRO A 277 7713 6127 8905 1302 1935 -3005 A C
ATOM 2160 N THR A 278 5.256 19.654 29.215 1.00 65.70 A N
ANISOU 2160 N THR A 278 7868 7530 9565 1188 1994 -3831 A N
ATOM 2161 CA THR A 278 5.826 20.780 29.975 1.00 69.37 A C
ANISOU 2161 CA THR A 278 7981 8260 10116 977 2108 -4284 A C
ATOM 2162 C THR A 278 5.183 20.920 31.381 1.00 76.60 A C
ANISOU 2162 C THR A 278 8905 9278 10923 1018 2086 -4385 A C
ATOM 2163 O THR A 278 5.730 21.639 32.225 1.00 79.28 A O
ANISOU 2163 O THR A 278 8945 9942 11234 895 2144 -4800 A O
ATOM 2164 CB THR A 278 5.753 22.118 29.193 1.00 81.13 A C
ANISOU 2164 CB THR A 278 9347 9432 12046 570 2385 -4383 A C
ATOM 2165 CG2 THR A 278 6.319 22.018 27.784 1.00 79.90 A C
ANISOU 2165 CG2 THR A 278 9200 9155 12005 524 2422 -4253 A C
ATOM 2166 OG1 THR A 278 4.425 22.644 29.172 1.00 79.98 A O
ANISOU 2166 OG1 THR A 278 9395 8829 12164 415 2531 -4152 A O
ATOM 2167 N VAL A 279 4.042 20.245 31.638 1.00 72.17 A N
ANISOU 2167 N VAL A 279 8669 8458 10292 1170 2016 -4033 A N
ATOM 2168 CA VAL A 279 3.394 20.289 32.958 1.00 73.00 A C
ANISOU 2168 CA VAL A 279 8810 8651 10277 1232 1992 -4094 A C
ATOM 2169 C VAL A 279 3.971 19.187 33.874 1.00 80.43 A C
ANISOU 2169 C VAL A 279 9754 10066 10740 1639 1773 -4137 A C
ATOM 2170 O VAL A 279 3.690 19.206 35.076 1.00 81.91 A O
ANISOU 2170 O VAL A 279 9906 10458 10757 1726 1738 -4253 A O
ATOM 2171 CB VAL A 279 1.840 20.234 32.923 1.00 73.93 A C
ANISOU 2171 CB VAL A 279 9245 8283 10562 1169 2055 -3730 A C
ATOM 2172 CG1 VAL A 279 1.253 21.522 32.367 1.00 72.73 A C
ANISOU 2172 CG1 VAL A 279 9033 7748 10853 802 2301 -3737 A C
ATOM 2173 CG2 VAL A 279 1.318 19.010 32.168 1.00 71.54 A C
ANISOU 2173 CG2 VAL A 279 9286 7750 10145 1369 1945 -3298 A C
ATOM 2174 N LEU A 280 4.786 18.248 33.315 1.00 77.82 A N
ANISOU 2174 N LEU A 280 9464 9919 10185 1906 1642 -4037 A N
ATOM 2175 CA LEU A 280 5.405 17.155 34.071 1.00 79.97 A C
ANISOU 2175 CA LEU A 280 9755 10639 9992 2354 1461 -4032 A C
ATOM 2176 C LEU A 280 6.582 17.712 34.900 1.00 90.04 A C
ANISOU 2176 C LEU A 280 10574 12571 11068 2377 1416 -4517 A C
ATOM 2177 O LEU A 280 7.751 17.609 34.507 1.00 91.91 A O
ANISOU 2177 O LEU A 280 10574 13167 11181 2466 1360 -4698 A O
ATOM 2178 CB LEU A 280 5.846 15.988 33.149 1.00 79.07 A C
ANISOU 2178 CB LEU A 280 9850 10469 9724 2634 1375 -3758 A C
ATOM 2179 CG LEU A 280 4.793 15.380 32.189 1.00 80.11 A C
ANISOU 2179 CG LEU A 280 10406 10005 10028 2583 1426 -3321 A C
ATOM 2180 CD1 LEU A 280 5.450 14.523 31.128 1.00 79.66 A C
ANISOU 2180 CD1 LEU A 280 10460 9923 9883 2756 1382 -3168 A C
ATOM 2181 CD2 LEU A 280 3.763 14.553 32.928 1.00 81.91 A C
ANISOU 2181 CD2 LEU A 280 10988 10053 10083 2786 1402 -3041 A C
ATOM 2182 N ALA A 281 6.238 18.337 36.045 1.00 89.38 A N
ANISOU 2182 N ALA A 281 10350 12656 10955 2273 1450 -4746 A N
ATOM 2183 CA ALA A 281 7.163 18.975 36.990 1.00 92.92 A C
ANISOU 2183 CA ALA A 281 10350 13743 11212 2232 1428 -5252 A C
ATOM 2184 C ALA A 281 7.513 18.038 38.168 1.00 99.02 A C
ANISOU 2184 C ALA A 281 11095 15086 11444 2724 1235 -5244 A C
ATOM 2185 O ALA A 281 8.312 18.410 39.032 1.00102.11 A O
ANISOU 2185 O ALA A 281 11091 16128 11578 2765 1180 -5654 A O
ATOM 2186 CB ALA A 281 6.554 20.278 37.505 1.00 93.81 A C
ANISOU 2186 CB ALA A 281 10332 13689 11624 1805 1613 -5524 A C
ATOM 2187 N GLY A 282 6.919 16.839 38.172 1.00 93.72 A N
ANISOU 2187 N GLY A 282 10838 14176 10595 3087 1155 -4784 A N
ATOM 2188 CA GLY A 282 7.138 15.800 39.174 1.00 95.64 A C
ANISOU 2188 CA GLY A 282 11157 14853 10330 3614 1009 -4662 A C
ATOM 2189 C GLY A 282 6.556 16.041 40.555 1.00100.70 A C
ANISOU 2189 C GLY A 282 11763 15696 10802 3651 1003 -4767 A C
ATOM 2190 O GLY A 282 6.883 15.301 41.486 1.00103.34 A O
ANISOU 2190 O GLY A 282 12086 16503 10675 4099 888 -4722 A O
ATOM 2191 N ASP A 283 5.677 17.049 40.703 1.00 95.04 A N
ANISOU 2191 N ASP A 283 11042 14627 10443 3211 1138 -4888 A N
ATOM 2192 CA ASP A 283 5.073 17.404 41.989 1.00 95.55 A C
ANISOU 2192 CA ASP A 283 11063 14853 10388 3191 1155 -5020 A C
ATOM 2193 C ASP A 283 3.563 17.701 41.877 1.00 95.09 A C
ANISOU 2193 C ASP A 283 11341 14092 10695 2919 1295 -4766 A C
ATOM 2194 O ASP A 283 2.932 18.022 42.890 1.00 95.21 A O
ANISOU 2194 O ASP A 283 11352 14164 10660 2869 1331 -4854 A O
ATOM 2195 CB ASP A 283 5.813 18.617 42.596 1.00100.48 A C
ANISOU 2195 CB ASP A 283 11160 16006 11011 2898 1195 -5630 A C
ATOM 2196 CG ASP A 283 5.871 19.885 41.743 1.00109.25 A C
ANISOU 2196 CG ASP A 283 12093 16785 12633 2331 1389 -5905 A C
ATOM 2197 OD1 ASP A 283 5.359 19.865 40.600 1.00105.58 A O
ANISOU 2197 OD1 ASP A 283 11887 15706 12523 2180 1475 -5608 A O
ATOM 2198 OD2 ASP A 283 6.427 20.900 42.224 1.00119.67 A O1-
ANISOU 2198 OD2 ASP A 283 13014 18467 13987 2038 1475 -6422 A O1-
ATOM 2199 N ARG A 284 2.997 17.602 40.651 1.00 87.41 A N
ANISOU 2199 N ARG A 284 10639 12501 10072 2749 1374 -4462 A N
ATOM 2200 CA ARG A 284 1.584 17.834 40.320 1.00 83.54 A C
ANISOU 2200 CA ARG A 284 10454 11358 9931 2502 1505 -4185 A C
ATOM 2201 C ARG A 284 1.158 19.311 40.641 1.00 86.72 A C
ANISOU 2201 C ARG A 284 10631 11645 10674 2059 1677 -4504 A C
ATOM 2202 O ARG A 284 -0.033 19.592 40.824 1.00 84.50 A O
ANISOU 2202 O ARG A 284 10541 10971 10594 1909 1780 -4341 A O
ATOM 2203 CB ARG A 284 0.656 16.790 41.009 1.00 82.70 A C
ANISOU 2203 CB ARG A 284 10725 11111 9585 2800 1457 -3823 A C
ATOM 2204 CG ARG A 284 1.083 15.327 40.793 1.00 91.32 A C
ANISOU 2204 CG ARG A 284 12081 12274 10345 3247 1346 -3510 A C
ATOM 2205 CD ARG A 284 0.019 14.321 41.206 1.00 96.39 A C
ANISOU 2205 CD ARG A 284 13163 12618 10842 3460 1370 -3116 A C
ATOM 2206 NE ARG A 284 0.100 13.952 42.622 1.00105.34 A N
ANISOU 2206 NE ARG A 284 14278 14178 11570 3794 1311 -3168 A N
ATOM 2207 CZ ARG A 284 0.071 12.701 43.079 1.00120.28 A C
ANISOU 2207 CZ ARG A 284 16468 16140 13095 4243 1283 -2881 A C
ATOM 2208 NH1 ARG A 284 -0.020 11.679 42.235 1.00104.44 A N1+
ANISOU 2208 NH1 ARG A 284 14811 13786 11086 4393 1319 -2543 A N1+
ATOM 2209 NH2 ARG A 284 0.136 12.464 44.383 1.00109.66 A N
ANISOU 2209 NH2 ARG A 284 15082 15210 11376 4549 1240 -2929 A N
ATOM 2210 N SER A 285 2.135 20.255 40.656 1.00 84.69 A N
ANISOU 2210 N SER A 285 9973 11715 10492 1840 1732 -4962 A N
ATOM 2211 CA SER A 285 1.903 21.694 40.924 1.00 84.81 A C
ANISOU 2211 CA SER A 285 9766 11622 10837 1404 1947 -5316 A C
ATOM 2212 C SER A 285 1.251 22.396 39.719 1.00 85.40 A C
ANISOU 2212 C SER A 285 9982 11042 11425 1074 2150 -5129 A C
ATOM 2213 O SER A 285 0.630 23.451 39.877 1.00 84.61 A O
ANISOU 2213 O SER A 285 9845 10659 11642 764 2366 -5251 A O
ATOM 2214 CB SER A 285 3.209 22.399 41.292 1.00 91.43 A C
ANISOU 2214 CB SER A 285 10136 13033 11570 1262 1968 -5887 A C
ATOM 2215 OG SER A 285 4.151 22.391 40.230 1.00 97.30 A O
ANISOU 2215 OG SER A 285 10751 13823 12396 1213 1961 -5940 A O
ATOM 2216 N LEU A 286 1.397 21.794 38.517 1.00 80.02 A N
ANISOU 2216 N LEU A 286 9463 10136 10807 1164 2090 -4823 A N
ATOM 2217 CA LEU A 286 0.863 22.285 37.244 1.00 76.74 A C
ANISOU 2217 CA LEU A 286 9181 9164 10812 920 2252 -4592 A C
ATOM 2218 C LEU A 286 -0.230 21.336 36.702 1.00 76.95 A C
ANISOU 2218 C LEU A 286 9610 8797 10833 1089 2174 -4055 A C
ATOM 2219 O LEU A 286 -0.606 21.436 35.536 1.00 74.64 A O
ANISOU 2219 O LEU A 286 9442 8124 10793 968 2250 -3805 A O
ATOM 2220 CB LEU A 286 2.015 22.458 36.221 1.00 77.11 A C
ANISOU 2220 CB LEU A 286 9041 9317 10942 835 2269 -4733 A C
ATOM 2221 CG LEU A 286 3.220 23.342 36.647 1.00 84.61 A C
ANISOU 2221 CG LEU A 286 9565 10699 11883 637 2356 -5302 A C
ATOM 2222 CD1 LEU A 286 4.297 23.365 35.570 1.00 84.81 A C
ANISOU 2222 CD1 LEU A 286 9439 10818 11968 581 2362 -5388 A C
ATOM 2223 CD2 LEU A 286 2.789 24.781 37.008 1.00 86.93 A C
ANISOU 2223 CD2 LEU A 286 9734 10762 12535 237 2655 -5579 A C
ATOM 2224 N ALA A 287 -0.768 20.454 37.573 1.00 73.76 A N
ANISOU 2224 N ALA A 287 9398 8493 10136 1350 2044 -3893 A N
ATOM 2225 CA ALA A 287 -1.803 19.456 37.262 1.00 71.75 A C
ANISOU 2225 CA ALA A 287 9525 7915 9822 1503 1984 -3434 A C
ATOM 2226 C ALA A 287 -3.257 20.013 37.309 1.00 73.25 A C
ANISOU 2226 C ALA A 287 9859 7678 10293 1289 2133 -3246 A C
ATOM 2227 O ALA A 287 -4.198 19.253 37.051 1.00 72.79 A O
ANISOU 2227 O ALA A 287 10092 7361 10201 1365 2104 -2891 A O
ATOM 2228 CB ALA A 287 -1.683 18.272 38.207 1.00 73.87 A C
ANISOU 2228 CB ALA A 287 9943 8475 9649 1880 1822 -3354 A C
ATOM 2229 N SER A 288 -3.440 21.330 37.572 1.00 67.85 A N
ANISOU 2229 N SER A 288 8972 6914 9892 1014 2314 -3483 A N
ATOM 2230 CA SER A 288 -4.767 21.966 37.561 1.00 65.37 A C
ANISOU 2230 CA SER A 288 8763 6209 9866 826 2483 -3311 A C
ATOM 2231 C SER A 288 -5.301 22.029 36.117 1.00 62.89 A C
ANISOU 2231 C SER A 288 8574 5505 9816 713 2558 -2977 A C
ATOM 2232 O SER A 288 -6.502 22.227 35.897 1.00 61.16 A O
ANISOU 2232 O SER A 288 8489 4981 9769 631 2653 -2719 A O
ATOM 2233 CB SER A 288 -4.720 23.353 38.201 1.00 70.97 A C
ANISOU 2233 CB SER A 288 9230 6928 10805 582 2694 -3668 A C
ATOM 2234 OG SER A 288 -3.817 24.217 37.531 1.00 82.89 A O
ANISOU 2234 OG SER A 288 10520 8441 12534 386 2826 -3907 A O
ATOM 2235 N VAL A 289 -4.391 21.807 35.145 1.00 56.66 A N
ANISOU 2235 N VAL A 289 7727 4773 9028 727 2505 -2983 A N
ATOM 2236 CA VAL A 289 -4.628 21.722 33.701 1.00 53.70 A C
ANISOU 2236 CA VAL A 289 7445 4122 8835 653 2544 -2695 A C
ATOM 2237 C VAL A 289 -5.638 20.589 33.435 1.00 53.02 A C
ANISOU 2237 C VAL A 289 7661 3884 8601 781 2432 -2304 A C
ATOM 2238 O VAL A 289 -6.471 20.732 32.551 1.00 50.64 A O
ANISOU 2238 O VAL A 289 7444 3315 8481 671 2510 -2033 A O
ATOM 2239 CB VAL A 289 -3.284 21.547 32.915 1.00 57.59 A C
ANISOU 2239 CB VAL A 289 7809 4790 9284 680 2483 -2830 A C
ATOM 2240 CG1 VAL A 289 -2.604 20.200 33.174 1.00 57.57 A C
ANISOU 2240 CG1 VAL A 289 7904 5082 8889 969 2250 -2824 A C
ATOM 2241 CG2 VAL A 289 -3.440 21.802 31.416 1.00 55.70 A C
ANISOU 2241 CG2 VAL A 289 7607 4274 9283 554 2574 -2590 A C
ATOM 2242 N ILE A 290 -5.607 19.508 34.246 1.00 49.43 A N
ANISOU 2242 N ILE A 290 7361 3608 7810 1006 2275 -2284 A N
ATOM 2243 CA ILE A 290 -6.536 18.383 34.134 1.00 48.17 A C
ANISOU 2243 CA ILE A 290 7508 3301 7493 1107 2205 -1959 A C
ATOM 2244 C ILE A 290 -7.922 18.816 34.609 1.00 52.10 A C
ANISOU 2244 C ILE A 290 8070 3600 8125 984 2311 -1826 A C
ATOM 2245 O ILE A 290 -8.878 18.638 33.855 1.00 51.37 A O
ANISOU 2245 O ILE A 290 8100 3283 8134 885 2353 -1552 A O
ATOM 2246 CB ILE A 290 -6.018 17.120 34.877 1.00 52.79 A C
ANISOU 2246 CB ILE A 290 8262 4113 7683 1408 2057 -1971 A C
ATOM 2247 CG1 ILE A 290 -4.580 16.730 34.413 1.00 54.06 A C
ANISOU 2247 CG1 ILE A 290 8330 4513 7699 1565 1957 -2108 A C
ATOM 2248 CG2 ILE A 290 -6.992 15.924 34.750 1.00 53.05 A C
ANISOU 2248 CG2 ILE A 290 8646 3945 7567 1481 2038 -1649 A C
ATOM 2249 CD1 ILE A 290 -4.339 16.562 32.845 1.00 52.58 A C
ANISOU 2249 CD1 ILE A 290 8173 4155 7650 1467 1965 -1959 A C
ATOM 2250 N ALA A 291 -8.027 19.400 35.830 1.00 48.76 A N
ANISOU 2250 N ALA A 291 7545 3288 7695 986 2357 -2032 A N
ATOM 2251 CA ALA A 291 -9.289 19.892 36.388 1.00 48.58 A C
ANISOU 2251 CA ALA A 291 7562 3098 7800 881 2470 -1938 A C
ATOM 2252 C ALA A 291 -9.926 20.913 35.461 1.00 49.89 A C
ANISOU 2252 C ALA A 291 7628 2999 8330 665 2640 -1811 A C
ATOM 2253 O ALA A 291 -11.151 21.014 35.420 1.00 50.37 A O
ANISOU 2253 O ALA A 291 7771 2885 8483 598 2714 -1592 A O
ATOM 2254 CB ALA A 291 -9.058 20.517 37.759 1.00 51.34 A C
ANISOU 2254 CB ALA A 291 7769 3638 8100 900 2509 -2245 A C
ATOM 2255 N HIS A 292 -9.094 21.671 34.728 1.00 43.03 A N
ANISOU 2255 N HIS A 292 6576 2117 7655 570 2716 -1942 A N
ATOM 2256 CA HIS A 292 -9.555 22.686 33.783 1.00 41.09 A C
ANISOU 2256 CA HIS A 292 6216 1664 7732 385 2901 -1782 A C
ATOM 2257 C HIS A 292 -10.170 21.980 32.564 1.00 43.48 A C
ANISOU 2257 C HIS A 292 6681 1812 8027 411 2843 -1439 A C
ATOM 2258 O HIS A 292 -11.319 22.257 32.211 1.00 40.70 A O
ANISOU 2258 O HIS A 292 6346 1329 7790 340 2935 -1178 A O
ATOM 2259 CB HIS A 292 -8.405 23.649 33.394 1.00 40.73 A C
ANISOU 2259 CB HIS A 292 5926 1686 7863 255 3015 -2011 A C
ATOM 2260 CG HIS A 292 -8.760 24.587 32.282 1.00 41.58 A C
ANISOU 2260 CG HIS A 292 5993 1489 8316 148 3240 -1865 A C
ATOM 2261 CD2 HIS A 292 -8.602 24.436 30.945 1.00 40.31 A C
ANISOU 2261 CD2 HIS A 292 5813 1312 8191 116 3230 -1624 A C
ATOM 2262 ND1 HIS A 292 -9.347 25.808 32.530 1.00 43.78 A N
ANISOU 2262 ND1 HIS A 292 6220 1514 8902 57 3514 -1913 A N
ATOM 2263 CE1 HIS A 292 -9.536 26.353 31.342 1.00 42.34 A C
ANISOU 2263 CE1 HIS A 292 5968 1215 8905 -20 3661 -1651 A C
ATOM 2264 NE2 HIS A 292 -9.110 25.547 30.354 1.00 40.37 A N
ANISOU 2264 NE2 HIS A 292 5725 1129 8487 10 3487 -1473 A N
ATOM 2265 N GLU A 293 -9.414 21.057 31.942 1.00 41.12 A N
ANISOU 2265 N GLU A 293 6457 1621 7548 491 2688 -1416 A N
ATOM 2266 CA GLU A 293 -9.902 20.307 30.776 1.00 40.03 A C
ANISOU 2266 CA GLU A 293 6447 1409 7352 477 2626 -1112 A C
ATOM 2267 C GLU A 293 -11.149 19.468 31.141 1.00 42.60 A C
ANISOU 2267 C GLU A 293 6977 1687 7520 496 2575 -903 A C
ATOM 2268 O GLU A 293 -12.112 19.482 30.376 1.00 42.89 A O
ANISOU 2268 O GLU A 293 7036 1633 7627 403 2621 -652 A O
ATOM 2269 CB GLU A 293 -8.799 19.442 30.128 1.00 40.60 A C
ANISOU 2269 CB GLU A 293 6577 1594 7255 567 2488 -1162 A C
ATOM 2270 CG GLU A 293 -7.591 20.210 29.587 1.00 44.98 A C
ANISOU 2270 CG GLU A 293 6925 2204 7961 528 2543 -1357 A C
ATOM 2271 CD GLU A 293 -7.785 21.593 28.981 1.00 69.59 A C
ANISOU 2271 CD GLU A 293 9863 5157 11421 368 2755 -1320 A C
ATOM 2272 OE1 GLU A 293 -8.812 21.823 28.300 1.00 68.83 A O
ANISOU 2272 OE1 GLU A 293 9801 4913 11437 305 2832 -1033 A O
ATOM 2273 OE2 GLU A 293 -6.876 22.440 29.153 1.00 61.58 A O1-
ANISOU 2273 OE2 GLU A 293 8670 4176 10552 310 2860 -1580 A O1-
ATOM 2274 N ILE A 294 -11.165 18.831 32.334 1.00 38.62 A N
ANISOU 2274 N ILE A 294 6553 1358 6762 577 2492 -973 A N
ATOM 2275 CA ILE A 294 -12.304 18.048 32.841 1.00 38.04 A C
ANISOU 2275 CA ILE A 294 6663 1274 6515 575 2472 -797 A C
ATOM 2276 C ILE A 294 -13.583 18.913 32.851 1.00 42.26 A C
ANISOU 2276 C ILE A 294 7164 1569 7325 478 2619 -703 A C
ATOM 2277 O ILE A 294 -14.616 18.474 32.349 1.00 43.20 A O
ANISOU 2277 O ILE A 294 7366 1635 7414 395 2631 -473 A O
ATOM 2278 CB ILE A 294 -12.005 17.452 34.252 1.00 41.07 A C
ANISOU 2278 CB ILE A 294 7237 1654 6715 785 2414 -999 A C
ATOM 2279 CG1 ILE A 294 -11.129 16.222 34.132 1.00 41.27 A C
ANISOU 2279 CG1 ILE A 294 7445 1771 6466 959 2293 -1012 A C
ATOM 2280 CG2 ILE A 294 -13.290 17.136 35.028 1.00 41.60 A C
ANISOU 2280 CG2 ILE A 294 7446 1651 6710 756 2461 -873 A C
ATOM 2281 CD1 ILE A 294 -10.760 15.535 35.376 1.00 55.27 A C
ANISOU 2281 CD1 ILE A 294 9350 3690 7960 1185 2233 -1121 A C
ATOM 2282 N SER A 295 -13.488 20.143 33.391 1.00 39.12 A N
ANISOU 2282 N SER A 295 6531 1244 7090 423 2732 -819 A N
ATOM 2283 CA SER A 295 -14.569 21.114 33.525 1.00 39.03 A C
ANISOU 2283 CA SER A 295 6393 1160 7277 328 2898 -703 A C
ATOM 2284 C SER A 295 -15.160 21.531 32.154 1.00 41.50 A C
ANISOU 2284 C SER A 295 6694 1244 7832 281 2987 -471 A C
ATOM 2285 O SER A 295 -16.377 21.731 32.067 1.00 41.82 A O
ANISOU 2285 O SER A 295 6717 1248 7926 240 3064 -263 A O
ATOM 2286 CB SER A 295 -14.077 22.324 34.307 1.00 42.24 A C
ANISOU 2286 CB SER A 295 6706 1395 7948 350 3045 -1007 A C
ATOM 2287 OG SER A 295 -13.620 21.901 35.584 1.00 45.89 A O
ANISOU 2287 OG SER A 295 7225 2001 8208 435 2957 -1247 A O
ATOM 2288 N HIS A 296 -14.328 21.556 31.079 1.00 37.35 A N
ANISOU 2288 N HIS A 296 5936 1079 7176 210 2955 -396 A N
ATOM 2289 CA HIS A 296 -14.785 21.802 29.712 1.00 36.57 A C
ANISOU 2289 CA HIS A 296 5725 1025 7143 169 3016 -153 A C
ATOM 2290 C HIS A 296 -15.817 20.770 29.255 1.00 38.24 A C
ANISOU 2290 C HIS A 296 6194 1040 7297 165 2918 44 A C
ATOM 2291 O HIS A 296 -16.639 21.087 28.406 1.00 38.39 A O
ANISOU 2291 O HIS A 296 6137 1045 7407 130 2987 277 A O
ATOM 2292 CB HIS A 296 -13.624 21.804 28.719 1.00 37.08 A C
ANISOU 2292 CB HIS A 296 5766 1060 7264 172 2981 -205 A C
ATOM 2293 CG HIS A 296 -13.006 23.152 28.515 1.00 40.24 A C
ANISOU 2293 CG HIS A 296 6118 1092 8080 184 3178 -328 A C
ATOM 2294 CD2 HIS A 296 -11.722 23.544 28.675 1.00 41.27 A C
ANISOU 2294 CD2 HIS A 296 6231 1115 8337 191 3207 -617 A C
ATOM 2295 ND1 HIS A 296 -13.771 24.247 28.142 1.00 42.85 A N
ANISOU 2295 ND1 HIS A 296 6399 1166 8717 188 3400 -151 A N
ATOM 2296 CE1 HIS A 296 -12.935 25.272 28.103 1.00 43.09 A C
ANISOU 2296 CE1 HIS A 296 6323 1073 8977 162 3580 -318 A C
ATOM 2297 NE2 HIS A 296 -11.687 24.896 28.417 1.00 42.93 A N
ANISOU 2297 NE2 HIS A 296 6311 1135 8864 145 3467 -621 A N
ATOM 2298 N SER A 297 -15.809 19.554 29.826 1.00 34.85 A N
ANISOU 2298 N SER A 297 5799 999 6443 151 2779 -11 A N
ATOM 2299 CA SER A 297 -16.816 18.535 29.509 1.00 34.55 A C
ANISOU 2299 CA SER A 297 5904 994 6230 93 2724 131 A C
ATOM 2300 C SER A 297 -18.244 19.081 29.644 1.00 39.76 A C
ANISOU 2300 C SER A 297 6677 1233 7197 34 2830 326 A C
ATOM 2301 O SER A 297 -19.136 18.584 28.968 1.00 39.12 A O
ANISOU 2301 O SER A 297 6591 1260 7012 -70 2816 502 A O
ATOM 2302 CB SER A 297 -16.643 17.319 30.399 1.00 34.43 A C
ANISOU 2302 CB SER A 297 6163 940 5978 121 2630 32 A C
ATOM 2303 OG SER A 297 -15.360 16.779 30.148 1.00 35.04 A O
ANISOU 2303 OG SER A 297 6377 937 6000 198 2537 -80 A O
ATOM 2304 N TRP A 298 -18.424 20.169 30.447 1.00 38.62 A N
ANISOU 2304 N TRP A 298 6396 1056 7221 94 2950 268 A N
ATOM 2305 CA TRP A 298 -19.694 20.860 30.668 1.00 37.60 A C
ANISOU 2305 CA TRP A 298 6114 998 7173 82 3079 421 A C
ATOM 2306 C TRP A 298 -19.678 22.194 29.954 1.00 40.41 A C
ANISOU 2306 C TRP A 298 6308 1192 7853 132 3245 558 A C
ATOM 2307 O TRP A 298 -20.374 22.365 28.955 1.00 39.06 A O
ANISOU 2307 O TRP A 298 6017 1128 7695 121 3285 810 A O
ATOM 2308 CB TRP A 298 -19.978 21.028 32.169 1.00 36.17 A C
ANISOU 2308 CB TRP A 298 5925 901 6918 116 3122 264 A C
ATOM 2309 CG TRP A 298 -20.331 19.731 32.825 1.00 36.06 A C
ANISOU 2309 CG TRP A 298 6153 897 6653 73 3006 225 A C
ATOM 2310 CD1 TRP A 298 -21.569 19.163 32.906 1.00 38.05 A C
ANISOU 2310 CD1 TRP A 298 6555 1024 6880 -25 3015 382 A C
ATOM 2311 CD2 TRP A 298 -19.419 18.789 33.402 1.00 35.69 A C
ANISOU 2311 CD2 TRP A 298 6291 882 6389 116 2889 54 A C
ATOM 2312 CE2 TRP A 298 -20.176 17.673 33.819 1.00 38.38 A C
ANISOU 2312 CE2 TRP A 298 6956 999 6629 65 2855 109 A C
ATOM 2313 CE3 TRP A 298 -18.030 18.774 33.604 1.00 36.45 A C
ANISOU 2313 CE3 TRP A 298 6446 902 6499 211 2821 -137 A C
ATOM 2314 NE1 TRP A 298 -21.486 17.932 33.510 1.00 37.44 A N
ANISOU 2314 NE1 TRP A 298 6727 940 6560 -50 2933 293 A N
ATOM 2315 CZ2 TRP A 298 -19.600 16.583 34.462 1.00 37.52 A C
ANISOU 2315 CZ2 TRP A 298 7085 899 6274 136 2779 -6 A C
ATOM 2316 CZ3 TRP A 298 -17.462 17.689 34.244 1.00 36.93 A C
ANISOU 2316 CZ3 TRP A 298 6763 921 6349 300 2718 -252 A C
ATOM 2317 CH2 TRP A 298 -18.245 16.614 34.668 1.00 37.53 A C
ANISOU 2317 CH2 TRP A 298 7098 915 6248 280 2707 -177 A C
ATOM 2318 N THR A 299 -18.852 23.126 30.439 1.00 39.24 A N
ANISOU 2318 N THR A 299 6076 958 7874 190 3358 370 A N
ATOM 2319 CA THR A 299 -18.731 24.501 29.922 1.00 39.76 A C
ANISOU 2319 CA THR A 299 5968 913 8227 244 3584 451 A C
ATOM 2320 C THR A 299 -17.731 24.553 28.757 1.00 44.86 A C
ANISOU 2320 C THR A 299 6619 1465 8959 242 3563 476 A C
ATOM 2321 O THR A 299 -16.520 24.680 28.945 1.00 45.67 A O
ANISOU 2321 O THR A 299 6743 1494 9115 227 3553 227 A O
ATOM 2322 CB THR A 299 -18.380 25.412 31.075 1.00 42.55 A C
ANISOU 2322 CB THR A 299 6348 1007 8813 264 3746 212 A C
ATOM 2323 CG2 THR A 299 -19.533 25.552 32.041 1.00 39.38 A C
ANISOU 2323 CG2 THR A 299 5854 810 8298 268 3810 251 A C
ATOM 2324 OG1 THR A 299 -17.270 24.842 31.770 1.00 41.47 A O
ANISOU 2324 OG1 THR A 299 6298 912 8548 231 3602 -112 A O
ATOM 2325 N GLY A 300 -18.271 24.406 27.556 1.00 41.67 A N
ANISOU 2325 N GLY A 300 6147 1183 8503 250 3548 763 A N
ATOM 2326 CA GLY A 300 -17.507 24.367 26.324 1.00 40.82 A C
ANISOU 2326 CA GLY A 300 6000 1108 8402 248 3521 828 A C
ATOM 2327 C GLY A 300 -17.928 23.243 25.404 1.00 43.10 A C
ANISOU 2327 C GLY A 300 6318 1631 8428 188 3334 991 A C
ATOM 2328 O GLY A 300 -18.372 23.502 24.285 1.00 44.04 A O
ANISOU 2328 O GLY A 300 6312 1873 8548 218 3384 1249 A O
ATOM 2329 N ASN A 301 -17.786 21.983 25.864 1.00 37.87 A N
ANISOU 2329 N ASN A 301 5793 1099 7496 113 3134 820 A N
ATOM 2330 CA ASN A 301 -18.085 20.771 25.088 1.00 36.24 A C
ANISOU 2330 CA ASN A 301 5628 1140 7002 30 2972 882 A C
ATOM 2331 C ASN A 301 -19.582 20.416 25.103 1.00 42.31 A C
ANISOU 2331 C ASN A 301 6412 1971 7692 -67 2975 1102 A C
ATOM 2332 O ASN A 301 -20.125 20.010 24.074 1.00 44.17 A O
ANISOU 2332 O ASN A 301 6567 2425 7789 -141 2934 1267 A O
ATOM 2333 CB ASN A 301 -17.244 19.588 25.581 1.00 32.51 A C
ANISOU 2333 CB ASN A 301 5173 1040 6141 45 2807 553 A C
ATOM 2334 CG ASN A 301 -15.738 19.797 25.616 1.00 45.76 A C
ANISOU 2334 CG ASN A 301 7151 2070 8164 42 2798 479 A C
ATOM 2335 ND2 ASN A 301 -15.005 18.740 26.002 1.00 31.14 A N
ANISOU 2335 ND2 ASN A 301 5110 969 5752 77 2665 233 A N
ATOM 2336 OD1 ASN A 301 -15.206 20.881 25.294 1.00 36.06 A O
ANISOU 2336 OD1 ASN A 301 5639 1036 7026 106 2914 443 A O
ATOM 2337 N LEU A 302 -20.239 20.540 26.255 1.00 38.60 A N
ANISOU 2337 N LEU A 302 5978 1444 7244 -58 3018 1054 A N
ATOM 2338 CA LEU A 302 -21.681 20.286 26.381 1.00 38.58 A C
ANISOU 2338 CA LEU A 302 5911 1623 7126 -130 3035 1206 A C
ATOM 2339 C LEU A 302 -22.453 21.583 26.033 1.00 42.16 A C
ANISOU 2339 C LEU A 302 6110 2145 7764 -5 3206 1455 A C
ATOM 2340 O LEU A 302 -23.402 21.544 25.246 1.00 41.27 A O
ANISOU 2340 O LEU A 302 5832 2303 7545 -28 3215 1677 A O
ATOM 2341 CB LEU A 302 -22.008 19.780 27.804 1.00 37.04 A C
ANISOU 2341 CB LEU A 302 5887 1331 6857 -169 3013 1041 A C
ATOM 2342 CG LEU A 302 -23.382 19.191 28.058 1.00 41.49 A C
ANISOU 2342 CG LEU A 302 6438 2071 7254 -292 3014 1132 A C
ATOM 2343 CD1 LEU A 302 -23.682 18.022 27.128 1.00 41.66 A C
ANISOU 2343 CD1 LEU A 302 6510 2296 7025 -481 2918 1164 A C
ATOM 2344 CD2 LEU A 302 -23.491 18.750 29.506 1.00 40.89 A C
ANISOU 2344 CD2 LEU A 302 6556 1854 7127 -303 3012 961 A C
ATOM 2345 N VAL A 303 -22.034 22.712 26.614 1.00 41.21 A N
ANISOU 2345 N VAL A 303 5957 1795 7908 131 3359 1409 A N
ATOM 2346 CA VAL A 303 -22.602 24.028 26.311 1.00 44.66 A C
ANISOU 2346 CA VAL A 303 6195 2217 8556 289 3579 1643 A C
ATOM 2347 C VAL A 303 -21.488 24.826 25.611 1.00 48.22 A C
ANISOU 2347 C VAL A 303 6613 2499 9210 377 3690 1649 A C
ATOM 2348 O VAL A 303 -20.486 25.157 26.228 1.00 47.94 A O
ANISOU 2348 O VAL A 303 6672 2215 9329 374 3739 1407 A O
ATOM 2349 CB VAL A 303 -23.283 24.760 27.502 1.00 51.59 A C
ANISOU 2349 CB VAL A 303 7064 2954 9585 360 3732 1605 A C
ATOM 2350 CG1 VAL A 303 -22.357 25.068 28.667 1.00 52.29 A C
ANISOU 2350 CG1 VAL A 303 7285 2739 9846 362 3791 1297 A C
ATOM 2351 CG2 VAL A 303 -24.004 26.010 27.020 1.00 52.89 A C
ANISOU 2351 CG2 VAL A 303 7024 3151 9920 545 3972 1913 A C
ATOM 2352 N THR A 304 -21.625 25.024 24.290 1.00 44.72 A N
ANISOU 2352 N THR A 304 6033 2227 8733 437 3718 1906 A N
ATOM 2353 CA THR A 304 -20.603 25.627 23.427 1.00 45.03 A C
ANISOU 2353 CA THR A 304 6045 2143 8923 505 3816 1941 A C
ATOM 2354 C THR A 304 -20.865 27.114 23.138 1.00 50.60 A C
ANISOU 2354 C THR A 304 6620 2709 9898 712 4138 2186 A C
ATOM 2355 O THR A 304 -22.016 27.542 23.066 1.00 50.39 A O
ANISOU 2355 O THR A 304 6461 2825 9860 840 4246 2453 A O
ATOM 2356 CB THR A 304 -20.548 24.811 22.108 1.00 50.88 A C
ANISOU 2356 CB THR A 304 6734 3175 9425 443 3647 2071 A C
ATOM 2357 CG2 THR A 304 -19.350 25.160 21.211 1.00 43.87 A C
ANISOU 2357 CG2 THR A 304 5848 2177 8644 479 3701 2065 A C
ATOM 2358 OG1 THR A 304 -20.510 23.421 22.437 1.00 44.47 A O
ANISOU 2358 OG1 THR A 304 6064 2470 8362 256 3399 1865 A O
ATOM 2359 N ASN A 305 -19.780 27.898 22.967 1.00 47.89 A N
ANISOU 2359 N ASN A 305 6316 2085 9794 748 4313 2093 A N
ATOM 2360 CA ASN A 305 -19.866 29.313 22.580 1.00 50.02 A C
ANISOU 2360 CA ASN A 305 6505 2159 10342 941 4675 2323 A C
ATOM 2361 C ASN A 305 -20.358 29.375 21.132 1.00 55.01 A C
ANISOU 2361 C ASN A 305 6986 3069 10847 1090 4696 2729 A C
ATOM 2362 O ASN A 305 -19.899 28.581 20.318 1.00 53.91 A O
ANISOU 2362 O ASN A 305 6842 3123 10517 999 4489 2712 A O
ATOM 2363 CB ASN A 305 -18.511 30.019 22.751 1.00 53.64 A C
ANISOU 2363 CB ASN A 305 7055 2255 11070 884 4861 2067 A C
ATOM 2364 CG ASN A 305 -17.286 29.388 22.101 1.00 70.13 A C
ANISOU 2364 CG ASN A 305 9191 4386 13070 756 4685 1894 A C
ATOM 2365 ND2 ASN A 305 -17.430 28.404 21.235 1.00 65.95 A N
ANISOU 2365 ND2 ASN A 305 8627 4165 12265 727 4430 2020 A N
ATOM 2366 OD1 ASN A 305 -16.163 29.773 22.389 1.00 62.36 A O
ANISOU 2366 OD1 ASN A 305 8267 3167 12259 669 4784 1617 A O
ATOM 2367 N GLU A 306 -21.331 30.235 20.828 1.00 54.47 A N
ANISOU 2367 N GLU A 306 6787 3060 10849 1329 4934 3093 A N
ATOM 2368 CA GLU A 306 -21.914 30.360 19.490 1.00 56.34 A C
ANISOU 2368 CA GLU A 306 6844 3629 10932 1521 4969 3516 A C
ATOM 2369 C GLU A 306 -20.843 30.709 18.430 1.00 60.07 A C
ANISOU 2369 C GLU A 306 7344 3986 11495 1556 5077 3578 A C
ATOM 2370 O GLU A 306 -20.834 30.137 17.338 1.00 59.71 A O
ANISOU 2370 O GLU A 306 7202 4273 11211 1555 4912 3727 A O
ATOM 2371 CB GLU A 306 -23.014 31.425 19.511 1.00 60.87 A C
ANISOU 2371 CB GLU A 306 7292 4218 11618 1829 5278 3890 A C
ATOM 2372 CG GLU A 306 -23.833 31.544 18.235 1.00 75.96 A C
ANISOU 2372 CG GLU A 306 8973 6576 13311 2078 5305 4362 A C
ATOM 2373 CD GLU A 306 -24.843 30.440 17.988 1.00 96.73 A C
ANISOU 2373 CD GLU A 306 11419 9790 15544 1991 4975 4424 A C
ATOM 2374 OE1 GLU A 306 -25.286 29.787 18.960 1.00 90.35 A O
ANISOU 2374 OE1 GLU A 306 10654 9016 14661 1804 4799 4184 A O
ATOM 2375 OE2 GLU A 306 -25.218 30.252 16.811 1.00 92.28 A O1-
ANISOU 2375 OE2 GLU A 306 10660 9667 14734 2106 4910 4710 A O1-
ATOM 2376 N THR A 307 -19.961 31.654 18.761 1.00 55.47 A N
ANISOU 2376 N THR A 307 6886 2941 11250 1573 5371 3449 A N
ATOM 2377 CA THR A 307 -18.853 32.126 17.931 1.00 54.47 A C
ANISOU 2377 CA THR A 307 6808 2620 11268 1583 5536 3459 A C
ATOM 2378 C THR A 307 -17.630 32.336 18.852 1.00 55.46 A C
ANISOU 2378 C THR A 307 7099 2331 11642 1360 5604 2986 A C
ATOM 2379 O THR A 307 -17.755 32.201 20.069 1.00 52.77 A O
ANISOU 2379 O THR A 307 6824 1877 11350 1244 5543 2709 A O
ATOM 2380 CB THR A 307 -19.240 33.436 17.163 1.00 61.60 A C
ANISOU 2380 CB THR A 307 7652 3399 12356 1911 5976 3908 A C
ATOM 2381 CG2 THR A 307 -20.532 33.332 16.347 1.00 60.04 A C
ANISOU 2381 CG2 THR A 307 7247 3679 11887 2177 5924 4392 A C
ATOM 2382 OG1 THR A 307 -19.355 34.500 18.091 1.00 60.97 A O
ANISOU 2382 OG1 THR A 307 7664 2900 12602 1984 6337 3851 A O
ATOM 2383 N TRP A 308 -16.469 32.713 18.285 1.00 52.75 A N
ANISOU 2383 N TRP A 308 6809 1785 11448 1305 5749 2894 A N
ATOM 2384 CA TRP A 308 -15.260 33.011 19.058 1.00 52.14 A C
ANISOU 2384 CA TRP A 308 6847 1364 11600 1092 5848 2439 A C
ATOM 2385 C TRP A 308 -15.337 34.413 19.704 1.00 60.49 A C
ANISOU 2385 C TRP A 308 7967 1984 13033 1158 6330 2416 A C
ATOM 2386 O TRP A 308 -14.504 34.762 20.545 1.00 60.40 A O
ANISOU 2386 O TRP A 308 8030 1699 13219 964 6449 2003 A O
ATOM 2387 CB TRP A 308 -14.019 32.840 18.186 1.00 50.31 A C
ANISOU 2387 CB TRP A 308 6628 1121 11368 988 5817 2331 A C
ATOM 2388 CG TRP A 308 -13.946 31.448 17.657 1.00 49.01 A C
ANISOU 2388 CG TRP A 308 6425 1352 10845 910 5365 2311 A C
ATOM 2389 CD1 TRP A 308 -14.122 31.051 16.363 1.00 52.15 A C
ANISOU 2389 CD1 TRP A 308 6746 2029 11040 1003 5259 2612 A C
ATOM 2390 CD2 TRP A 308 -13.880 30.252 18.441 1.00 46.38 A C
ANISOU 2390 CD2 TRP A 308 6135 1194 10294 746 4982 2010 A C
ATOM 2391 CE2 TRP A 308 -13.968 29.162 17.550 1.00 49.43 A C
ANISOU 2391 CE2 TRP A 308 6488 1925 10371 726 4678 2124 A C
ATOM 2392 CE3 TRP A 308 -13.738 29.995 19.818 1.00 46.50 A C
ANISOU 2392 CE3 TRP A 308 6222 1110 10336 619 4884 1653 A C
ATOM 2393 NE1 TRP A 308 -14.086 29.680 16.284 1.00 49.82 A N
ANISOU 2393 NE1 TRP A 308 6452 2044 10432 872 4844 2473 A N
ATOM 2394 CZ2 TRP A 308 -13.899 27.834 17.985 1.00 46.36 A C
ANISOU 2394 CZ2 TRP A 308 6160 1732 9723 585 4314 1896 A C
ATOM 2395 CZ3 TRP A 308 -13.698 28.676 20.250 1.00 45.69 A C
ANISOU 2395 CZ3 TRP A 308 6171 1232 9958 508 4506 1458 A C
ATOM 2396 CH2 TRP A 308 -13.753 27.617 19.338 1.00 44.96 A C
ANISOU 2396 CH2 TRP A 308 6069 1428 9584 491 4240 1578 A C
ATOM 2397 N GLU A 309 -16.366 35.191 19.346 1.00 59.93 A N
ANISOU 2397 N GLU A 309 7858 1870 13042 1434 6614 2848 A N
ATOM 2398 CA GLU A 309 -16.639 36.479 19.970 1.00 63.56 A C
ANISOU 2398 CA GLU A 309 8395 1911 13844 1533 7097 2872 A C
ATOM 2399 C GLU A 309 -17.183 36.201 21.396 1.00 65.70 A C
ANISOU 2399 C GLU A 309 8683 2182 14096 1428 6958 2601 A C
ATOM 2400 O GLU A 309 -16.885 36.940 22.325 1.00 66.42 A O
ANISOU 2400 O GLU A 309 8864 1918 14455 1329 7240 2324 A O
ATOM 2401 CB GLU A 309 -17.632 37.289 19.118 1.00 68.05 A C
ANISOU 2401 CB GLU A 309 8913 2486 14456 1916 7424 3463 A C
ATOM 2402 CG GLU A 309 -17.116 37.555 17.711 1.00 80.28 A C
ANISOU 2402 CG GLU A 309 10444 4066 15994 2046 7564 3761 A C
ATOM 2403 CD GLU A 309 -18.039 38.329 16.789 1.00109.04 A C
ANISOU 2403 CD GLU A 309 14026 7767 19637 2473 7888 4382 A C
ATOM 2404 OE1 GLU A 309 -17.550 39.266 16.118 1.00104.59 A O
ANISOU 2404 OE1 GLU A 309 13551 6890 19300 2608 8328 4574 A O
ATOM 2405 OE2 GLU A 309 -19.239 37.979 16.704 1.00106.93 A O1-
ANISOU 2405 OE2 GLU A 309 13616 7883 19128 2680 7709 4683 A O1-
ATOM 2406 N ASN A 310 -17.904 35.076 21.552 1.00 59.41 A N
ANISOU 2406 N ASN A 310 7806 1797 12971 1422 6523 2651 A N
ATOM 2407 CA ASN A 310 -18.531 34.581 22.784 1.00 58.58 A C
ANISOU 2407 CA ASN A 310 7708 1780 12770 1336 6325 2447 A C
ATOM 2408 C ASN A 310 -17.658 33.533 23.520 1.00 56.94 A C
ANISOU 2408 C ASN A 310 7558 1665 12414 1042 5954 1963 A C
ATOM 2409 O ASN A 310 -18.168 32.847 24.401 1.00 53.58 A O
ANISOU 2409 O ASN A 310 7140 1393 11825 973 5712 1824 A O
ATOM 2410 CB ASN A 310 -19.898 33.955 22.455 1.00 58.61 A C
ANISOU 2410 CB ASN A 310 7585 2197 12486 1505 6102 2811 A C
ATOM 2411 CG ASN A 310 -20.909 34.941 21.930 1.00 75.89 A C
ANISOU 2411 CG ASN A 310 9689 4373 14774 1842 6445 3299 A C
ATOM 2412 ND2 ASN A 310 -21.147 34.913 20.631 1.00 67.68 A N
ANISOU 2412 ND2 ASN A 310 8540 3584 13593 2023 6438 3683 A N
ATOM 2413 OD1 ASN A 310 -21.510 35.707 22.678 1.00 65.39 A O
ANISOU 2413 OD1 ASN A 310 8382 2839 13624 1961 6716 3347 A O
ATOM 2414 N PHE A 311 -16.341 33.478 23.201 1.00 52.37 A N
ANISOU 2414 N PHE A 311 7019 983 11898 888 5943 1711 A N
ATOM 2415 CA PHE A 311 -15.340 32.558 23.754 1.00 50.08 A C
ANISOU 2415 CA PHE A 311 6758 819 11452 655 5624 1270 A C
ATOM 2416 C PHE A 311 -15.241 32.601 25.289 1.00 53.63 A C
ANISOU 2416 C PHE A 311 7269 1142 11966 523 5612 878 A C
ATOM 2417 O PHE A 311 -14.884 31.579 25.886 1.00 52.64 A O
ANISOU 2417 O PHE A 311 7171 1212 11616 407 5274 618 A O
ATOM 2418 CB PHE A 311 -13.947 32.804 23.124 1.00 52.16 A C
ANISOU 2418 CB PHE A 311 7040 937 11840 541 5715 1090 A C
ATOM 2419 CG PHE A 311 -12.864 31.797 23.470 1.00 52.12 A C
ANISOU 2419 CG PHE A 311 7051 1102 11649 353 5377 696 A C
ATOM 2420 CD1 PHE A 311 -13.114 30.418 23.410 1.00 52.25 A C
ANISOU 2420 CD1 PHE A 311 7083 1445 11325 351 4953 729 A C
ATOM 2421 CD2 PHE A 311 -11.591 32.219 23.833 1.00 54.22 A C
ANISOU 2421 CD2 PHE A 311 7313 1215 12071 184 5504 296 A C
ATOM 2422 CE1 PHE A 311 -12.115 29.488 23.742 1.00 51.00 A C
ANISOU 2422 CE1 PHE A 311 6957 1431 10989 225 4671 395 A C
ATOM 2423 CE2 PHE A 311 -10.590 31.287 24.154 1.00 55.37 A C
ANISOU 2423 CE2 PHE A 311 7452 1567 12021 54 5193 -47 A C
ATOM 2424 CZ PHE A 311 -10.854 29.928 24.096 1.00 51.20 A C
ANISOU 2424 CZ PHE A 311 6959 1338 11157 97 4782 24 A C
ATOM 2425 N TRP A 312 -15.598 33.726 25.932 1.00 50.40 A N
ANISOU 2425 N TRP A 312 6804 591 11756 549 5983 830 A N
ATOM 2426 CA TRP A 312 -15.550 33.854 27.395 1.00 50.42 A C
ANISOU 2426 CA TRP A 312 6824 544 11789 414 6001 457 A C
ATOM 2427 C TRP A 312 -16.561 32.908 28.086 1.00 53.02 A C
ANISOU 2427 C TRP A 312 7253 951 11943 478 5681 530 A C
ATOM 2428 O TRP A 312 -16.321 32.502 29.219 1.00 50.82 A O
ANISOU 2428 O TRP A 312 7006 730 11574 359 5535 189 A O
ATOM 2429 CB TRP A 312 -15.769 35.312 27.841 1.00 52.78 A C
ANISOU 2429 CB TRP A 312 7142 469 12441 433 6514 421 A C
ATOM 2430 CG TRP A 312 -17.210 35.728 27.928 1.00 54.22 A C
ANISOU 2430 CG TRP A 312 7372 511 12718 666 6674 795 A C
ATOM 2431 CD1 TRP A 312 -17.979 36.241 26.925 1.00 57.99 A C
ANISOU 2431 CD1 TRP A 312 7878 830 13326 931 6888 1299 A C
ATOM 2432 CD2 TRP A 312 -18.064 35.620 29.077 1.00 53.74 A C
ANISOU 2432 CD2 TRP A 312 7315 509 12596 675 6623 718 A C
ATOM 2433 CE2 TRP A 312 -19.345 36.069 28.691 1.00 58.17 A C
ANISOU 2433 CE2 TRP A 312 7907 928 13268 953 6805 1181 A C
ATOM 2434 CE3 TRP A 312 -17.869 35.194 30.402 1.00 53.15 A C
ANISOU 2434 CE3 TRP A 312 7274 486 12432 507 6446 314 A C
ATOM 2435 NE1 TRP A 312 -19.259 36.463 27.377 1.00 57.96 A N
ANISOU 2435 NE1 TRP A 312 7854 852 13316 1107 6971 1532 A N
ATOM 2436 CZ2 TRP A 312 -20.424 36.124 29.594 1.00 56.91 A C
ANISOU 2436 CZ2 TRP A 312 7741 800 13081 1032 6825 1227 A C
ATOM 2437 CZ3 TRP A 312 -18.934 35.249 31.291 1.00 53.71 A C
ANISOU 2437 CZ3 TRP A 312 7389 504 12513 592 6468 361 A C
ATOM 2438 CH2 TRP A 312 -20.197 35.690 30.881 1.00 55.27 A C
ANISOU 2438 CH2 TRP A 312 7572 639 12790 841 6651 810 A C
ATOM 2439 N LEU A 313 -17.689 32.581 27.426 1.00 50.98 A N
ANISOU 2439 N LEU A 313 6953 869 11547 649 5591 961 A N
ATOM 2440 CA LEU A 313 -18.690 31.665 27.986 1.00 51.09 A C
ANISOU 2440 CA LEU A 313 6967 1142 11302 671 5311 1037 A C
ATOM 2441 C LEU A 313 -18.071 30.285 28.196 1.00 54.49 A C
ANISOU 2441 C LEU A 313 7456 1811 11438 525 4900 803 A C
ATOM 2442 O LEU A 313 -18.356 29.607 29.180 1.00 55.27 A O
ANISOU 2442 O LEU A 313 7610 2016 11373 466 4712 637 A O
ATOM 2443 CB LEU A 313 -19.908 31.556 27.063 1.00 51.64 A C
ANISOU 2443 CB LEU A 313 6943 1417 11259 857 5298 1524 A C
ATOM 2444 CG LEU A 313 -20.755 32.807 26.915 1.00 57.00 A C
ANISOU 2444 CG LEU A 313 7561 1921 12175 1073 5694 1830 A C
ATOM 2445 CD1 LEU A 313 -21.707 32.663 25.763 1.00 57.67 A C
ANISOU 2445 CD1 LEU A 313 7513 2290 12107 1275 5659 2313 A C
ATOM 2446 CD2 LEU A 313 -21.534 33.076 28.177 1.00 57.62 A C
ANISOU 2446 CD2 LEU A 313 7661 1921 12310 1085 5783 1727 A C
ATOM 2447 N ASN A 314 -17.196 29.903 27.264 1.00 48.53 A N
ANISOU 2447 N ASN A 314 6698 1120 10622 484 4789 797 A N
ATOM 2448 CA ASN A 314 -16.412 28.686 27.264 1.00 45.90 A C
ANISOU 2448 CA ASN A 314 6429 975 10038 376 4451 592 A C
ATOM 2449 C ASN A 314 -15.355 28.744 28.373 1.00 48.31 A C
ANISOU 2449 C ASN A 314 6778 1193 10384 261 4436 133 A C
ATOM 2450 O ASN A 314 -15.413 27.975 29.335 1.00 47.51 A O
ANISOU 2450 O ASN A 314 6745 1214 10091 226 4234 -50 A O
ATOM 2451 CB ASN A 314 -15.709 28.558 25.888 1.00 46.45 A C
ANISOU 2451 CB ASN A 314 6463 1095 10092 380 4420 718 A C
ATOM 2452 CG ASN A 314 -16.026 27.360 25.057 1.00 62.44 A C
ANISOU 2452 CG ASN A 314 8504 3398 11821 381 4133 906 A C
ATOM 2453 ND2 ASN A 314 -17.237 27.303 24.536 1.00 56.74 A N
ANISOU 2453 ND2 ASN A 314 7718 2826 11016 464 4137 1244 A N
ATOM 2454 OD1 ASN A 314 -15.143 26.559 24.744 1.00 49.73 A O
ANISOU 2454 OD1 ASN A 314 6949 1881 10067 311 3937 756 A O
ATOM 2455 N GLU A 315 -14.389 29.671 28.232 1.00 44.91 A N
ANISOU 2455 N GLU A 315 6213 745 10107 186 4670 -45 A N
ATOM 2456 CA GLU A 315 -13.243 29.721 29.118 1.00 44.50 A C
ANISOU 2456 CA GLU A 315 6124 748 10037 42 4648 -485 A C
ATOM 2457 C GLU A 315 -13.497 30.354 30.485 1.00 48.40 A C
ANISOU 2457 C GLU A 315 6731 900 10758 23 4810 -776 A C
ATOM 2458 O GLU A 315 -12.943 29.841 31.447 1.00 47.57 A O
ANISOU 2458 O GLU A 315 6634 952 10489 -39 4634 -1106 A O
ATOM 2459 CB GLU A 315 -11.994 30.314 28.437 1.00 46.09 A C
ANISOU 2459 CB GLU A 315 6301 753 10456 -35 4812 -659 A C
ATOM 2460 CG GLU A 315 -11.358 29.334 27.431 1.00 48.15 A C
ANISOU 2460 CG GLU A 315 6645 1062 10586 3 4549 -598 A C
ATOM 2461 CD GLU A 315 -10.833 28.016 27.975 1.00 63.64 A C
ANISOU 2461 CD GLU A 315 8659 3300 12221 -2 4176 -804 A C
ATOM 2462 OE1 GLU A 315 -10.796 27.924 29.228 1.00 41.67 A O
ANISOU 2462 OE1 GLU A 315 5679 983 9171 -109 4109 -960 A O
ATOM 2463 OE2 GLU A 315 -10.549 27.065 27.188 1.00 44.05 A O1-
ANISOU 2463 OE2 GLU A 315 6220 974 9543 37 3951 -683 A O1-
ATOM 2464 N GLY A 316 -14.334 31.386 30.585 1.00 47.28 A N
ANISOU 2464 N GLY A 316 6496 685 10782 42 5129 -595 A N
ATOM 2465 CA GLY A 316 -14.653 32.025 31.860 1.00 48.24 A C
ANISOU 2465 CA GLY A 316 6628 675 11028 -11 5310 -830 A C
ATOM 2466 C GLY A 316 -15.372 31.117 32.843 1.00 50.06 A C
ANISOU 2466 C GLY A 316 6986 968 11067 58 5042 -882 A C
ATOM 2467 O GLY A 316 -15.017 31.089 34.023 1.00 49.21 A O
ANISOU 2467 O GLY A 316 6876 923 10899 -26 5010 -1240 A O
ATOM 2468 N HIS A 317 -16.385 30.362 32.368 1.00 46.44 A N
ANISOU 2468 N HIS A 317 6514 753 10380 157 4853 -490 A N
ATOM 2469 CA HIS A 317 -17.140 29.413 33.191 1.00 46.00 A C
ANISOU 2469 CA HIS A 317 6565 811 10101 201 4611 -482 A C
ATOM 2470 C HIS A 317 -16.266 28.202 33.580 1.00 50.66 A C
ANISOU 2470 C HIS A 317 7240 1601 10409 161 4276 -725 A C
ATOM 2471 O HIS A 317 -16.365 27.724 34.714 1.00 51.18 A O
ANISOU 2471 O HIS A 317 7363 1779 10305 156 4156 -905 A O
ATOM 2472 CB HIS A 317 -18.435 28.944 32.487 1.00 45.29 A C
ANISOU 2472 CB HIS A 317 6498 786 9926 313 4534 -46 A C
ATOM 2473 CG HIS A 317 -19.442 30.027 32.264 1.00 49.69 A C
ANISOU 2473 CG HIS A 317 6981 1178 10719 418 4844 219 A C
ATOM 2474 CD2 HIS A 317 -20.628 30.284 32.844 1.00 51.31 A C
ANISOU 2474 CD2 HIS A 317 7171 1385 10939 493 4936 369 A C
ATOM 2475 ND1 HIS A 317 -19.208 30.996 31.311 1.00 53.25 A N
ANISOU 2475 ND1 HIS A 317 7369 1437 11425 477 5119 369 A N
ATOM 2476 CE1 HIS A 317 -20.247 31.814 31.341 1.00 53.95 A C
ANISOU 2476 CE1 HIS A 317 7414 1412 11673 610 5378 617 A C
ATOM 2477 NE2 HIS A 317 -21.124 31.436 32.236 1.00 53.08 A N
ANISOU 2477 NE2 HIS A 317 7318 1423 11427 624 5273 625 A N
ATOM 2478 N THR A 318 -15.412 27.728 32.657 1.00 46.33 A N
ANISOU 2478 N THR A 318 6689 1126 9788 148 4145 -713 A N
ATOM 2479 CA THR A 318 -14.498 26.595 32.878 1.00 45.07 A C
ANISOU 2479 CA THR A 318 6596 1179 9349 143 3854 -908 A C
ATOM 2480 C THR A 318 -13.470 26.985 33.950 1.00 50.97 A C
ANISOU 2480 C THR A 318 7282 1977 10108 84 3892 -1355 A C
ATOM 2481 O THR A 318 -13.239 26.196 34.866 1.00 50.53 A O
ANISOU 2481 O THR A 318 7288 2115 9798 126 3698 -1527 A O
ATOM 2482 CB THR A 318 -13.835 26.169 31.557 1.00 46.01 A C
ANISOU 2482 CB THR A 318 6709 1343 9428 146 3754 -783 A C
ATOM 2483 CG2 THR A 318 -12.826 25.065 31.736 1.00 39.28 A C
ANISOU 2483 CG2 THR A 318 5792 957 8175 106 3477 -897 A C
ATOM 2484 OG1 THR A 318 -14.843 25.753 30.642 1.00 43.31 A O
ANISOU 2484 OG1 THR A 318 6380 1071 9007 181 3706 -389 A O
ATOM 2485 N VAL A 319 -12.889 28.214 33.851 1.00 48.55 A N
ANISOU 2485 N VAL A 319 6853 1508 10087 -15 4166 -1545 A N
ATOM 2486 CA VAL A 319 -11.928 28.732 34.835 1.00 50.44 A C
ANISOU 2486 CA VAL A 319 6991 1817 10357 -120 4248 -2016 A C
ATOM 2487 C VAL A 319 -12.646 28.845 36.207 1.00 55.76 A C
ANISOU 2487 C VAL A 319 7693 2524 10971 -111 4277 -2142 A C
ATOM 2488 O VAL A 319 -12.049 28.505 37.227 1.00 57.01 A O
ANISOU 2488 O VAL A 319 7817 2917 10926 -119 4148 -2467 A O
ATOM 2489 CB VAL A 319 -11.267 30.074 34.391 1.00 55.79 A C
ANISOU 2489 CB VAL A 319 7548 2268 11383 -270 4599 -2194 A C
ATOM 2490 CG1 VAL A 319 -10.580 30.782 35.551 1.00 57.92 A C
ANISOU 2490 CG1 VAL A 319 7701 2590 11716 -424 4758 -2702 A C
ATOM 2491 CG2 VAL A 319 -10.271 29.838 33.261 1.00 53.99 A C
ANISOU 2491 CG2 VAL A 319 7274 2088 11150 -291 4529 -2176 A C
ATOM 2492 N TYR A 320 -13.934 29.239 36.220 1.00 51.01 A N
ANISOU 2492 N TYR A 320 7146 1728 10506 -70 4428 -1868 A N
ATOM 2493 CA TYR A 320 -14.711 29.318 37.455 1.00 50.73 A C
ANISOU 2493 CA TYR A 320 7144 1717 10414 -54 4459 -1952 A C
ATOM 2494 C TYR A 320 -14.870 27.925 38.082 1.00 52.27 A C
ANISOU 2494 C TYR A 320 7449 2191 10222 48 4115 -1922 A C
ATOM 2495 O TYR A 320 -14.568 27.761 39.260 1.00 52.09 A O
ANISOU 2495 O TYR A 320 7417 2338 10038 46 4052 -2208 A O
ATOM 2496 CB TYR A 320 -16.079 29.988 37.218 1.00 52.27 A C
ANISOU 2496 CB TYR A 320 7366 1667 10827 -6 4691 -1626 A C
ATOM 2497 CG TYR A 320 -16.865 30.194 38.492 1.00 54.19 A C
ANISOU 2497 CG TYR A 320 7633 1914 11043 0 4764 -1734 A C
ATOM 2498 CD1 TYR A 320 -16.758 31.379 39.220 1.00 59.21 A C
ANISOU 2498 CD1 TYR A 320 8201 2379 11916 -99 5082 -2018 A C
ATOM 2499 CD2 TYR A 320 -17.685 29.191 38.995 1.00 52.88 A C
ANISOU 2499 CD2 TYR A 320 7564 1917 10612 88 4535 -1572 A C
ATOM 2500 CE1 TYR A 320 -17.466 31.563 40.409 1.00 61.61 A C
ANISOU 2500 CE1 TYR A 320 8525 2697 12186 -96 5152 -2131 A C
ATOM 2501 CE2 TYR A 320 -18.373 29.351 40.192 1.00 54.77 A C
ANISOU 2501 CE2 TYR A 320 7824 2174 10811 93 4599 -1677 A C
ATOM 2502 CZ TYR A 320 -18.267 30.540 40.892 1.00 65.73 A C
ANISOU 2502 CZ TYR A 320 9136 3408 12431 8 4898 -1952 A C
ATOM 2503 OH TYR A 320 -18.977 30.682 42.052 1.00 66.41 A O
ANISOU 2503 OH TYR A 320 9243 3519 12469 15 4963 -2051 A O
ATOM 2504 N LEU A 321 -15.326 26.932 37.297 1.00 48.83 A N
ANISOU 2504 N LEU A 321 7120 1803 9629 134 3916 -1586 A N
ATOM 2505 CA LEU A 321 -15.491 25.532 37.720 1.00 47.86 A C
ANISOU 2505 CA LEU A 321 7145 1888 9151 228 3633 -1519 A C
ATOM 2506 C LEU A 321 -14.180 24.915 38.220 1.00 49.89 A C
ANISOU 2506 C LEU A 321 7401 2386 9169 275 3449 -1821 A C
ATOM 2507 O LEU A 321 -14.187 24.252 39.259 1.00 48.01 A O
ANISOU 2507 O LEU A 321 7242 2325 8673 360 3321 -1928 A O
ATOM 2508 CB LEU A 321 -16.042 24.676 36.573 1.00 47.07 A C
ANISOU 2508 CB LEU A 321 7148 1775 8963 263 3505 -1146 A C
ATOM 2509 CG LEU A 321 -17.518 24.850 36.193 1.00 53.27 A C
ANISOU 2509 CG LEU A 321 7943 2452 9845 255 3606 -810 A C
ATOM 2510 CD1 LEU A 321 -17.927 23.771 35.184 1.00 52.69 A C
ANISOU 2510 CD1 LEU A 321 7960 2452 9610 261 3445 -518 A C
ATOM 2511 CD2 LEU A 321 -18.446 24.789 37.431 1.00 55.39 A C
ANISOU 2511 CD2 LEU A 321 8271 2748 10027 273 3630 -838 A C
ATOM 2512 N GLU A 322 -13.067 25.145 37.482 1.00 46.84 A N
ANISOU 2512 N GLU A 322 6915 2024 8857 237 3447 -1947 A N
ATOM 2513 CA GLU A 322 -11.710 24.687 37.809 1.00 47.95 A C
ANISOU 2513 CA GLU A 322 7002 2429 8787 289 3291 -2243 A C
ATOM 2514 C GLU A 322 -11.310 25.186 39.201 1.00 55.45 A C
ANISOU 2514 C GLU A 322 7836 3560 9673 265 3346 -2636 A C
ATOM 2515 O GLU A 322 -10.874 24.394 40.037 1.00 56.20 A O
ANISOU 2515 O GLU A 322 7966 3942 9446 399 3161 -2772 A O
ATOM 2516 CB GLU A 322 -10.704 25.187 36.742 1.00 49.77 A C
ANISOU 2516 CB GLU A 322 7102 2618 9189 206 3355 -2328 A C
ATOM 2517 CG GLU A 322 -9.232 24.842 36.972 1.00 59.78 A C
ANISOU 2517 CG GLU A 322 8262 4190 10263 248 3217 -2657 A C
ATOM 2518 CD GLU A 322 -8.199 25.705 36.261 1.00 81.24 A C
ANISOU 2518 CD GLU A 322 10789 6879 13201 101 3362 -2874 A C
ATOM 2519 OE1 GLU A 322 -8.594 26.628 35.511 1.00 71.72 A O
ANISOU 2519 OE1 GLU A 322 9549 5374 12328 -34 3605 -2764 A O
ATOM 2520 OE2 GLU A 322 -6.987 25.439 36.432 1.00 77.75 A O1-
ANISOU 2520 OE2 GLU A 322 10231 6724 12589 134 3245 -3145 A O1-
ATOM 2521 N ARG A 323 -11.517 26.491 39.457 1.00 54.18 A N
ANISOU 2521 N ARG A 323 7547 3232 9808 104 3619 -2807 A N
ATOM 2522 CA ARG A 323 -11.165 27.117 40.726 1.00 55.74 A C
ANISOU 2522 CA ARG A 323 7612 3589 9977 30 3717 -3222 A C
ATOM 2523 C ARG A 323 -12.103 26.664 41.869 1.00 57.75 A C
ANISOU 2523 C ARG A 323 7982 3923 10037 131 3647 -3156 A C
ATOM 2524 O ARG A 323 -11.686 26.695 43.028 1.00 58.66 A O
ANISOU 2524 O ARG A 323 8014 4309 9966 144 3612 -3482 A O
ATOM 2525 CB ARG A 323 -11.083 28.638 40.590 1.00 56.92 A C
ANISOU 2525 CB ARG A 323 7618 3489 10519 -193 4077 -3433 A C
ATOM 2526 CG ARG A 323 -9.735 29.076 39.999 1.00 64.73 A C
ANISOU 2526 CG ARG A 323 8439 4549 11604 -321 4141 -3712 A C
ATOM 2527 CD ARG A 323 -9.731 30.525 39.552 1.00 70.22 A C
ANISOU 2527 CD ARG A 323 9052 4896 12733 -540 4548 -3825 A C
ATOM 2528 NE ARG A 323 -8.534 30.837 38.774 1.00 68.91 A N
ANISOU 2528 NE ARG A 323 8756 4762 12665 -661 4610 -4015 A N
ATOM 2529 CZ ARG A 323 -8.367 31.944 38.055 1.00 79.76 A C
ANISOU 2529 CZ ARG A 323 10086 5810 14410 -834 4962 -4051 A C
ATOM 2530 NH1 ARG A 323 -9.319 32.863 38.009 1.00 67.04 A N1+
ANISOU 2530 NH1 ARG A 323 8554 3808 13109 -882 5293 -3899 A N1+
ATOM 2531 NH2 ARG A 323 -7.247 32.135 37.367 1.00 66.12 A N
ANISOU 2531 NH2 ARG A 323 8242 4139 12742 -946 5004 -4230 A N
ATOM 2532 N ARG A 324 -13.309 26.166 41.552 1.00 51.91 A N
ANISOU 2532 N ARG A 324 7421 3000 9302 207 3613 -2750 A N
ATOM 2533 CA ARG A 324 -14.191 25.601 42.569 1.00 51.99 A C
ANISOU 2533 CA ARG A 324 7558 3089 9106 304 3539 -2665 A C
ATOM 2534 C ARG A 324 -13.686 24.200 42.968 1.00 59.25 A C
ANISOU 2534 C ARG A 324 8604 4304 9606 497 3253 -2643 A C
ATOM 2535 O ARG A 324 -13.770 23.843 44.141 1.00 61.54 A O
ANISOU 2535 O ARG A 324 8934 4795 9653 593 3189 -2761 A O
ATOM 2536 CB ARG A 324 -15.646 25.554 42.089 1.00 50.65 A C
ANISOU 2536 CB ARG A 324 7513 2656 9077 300 3618 -2262 A C
ATOM 2537 CG ARG A 324 -16.329 26.913 42.049 1.00 57.07 A C
ANISOU 2537 CG ARG A 324 8223 3204 10255 178 3927 -2267 A C
ATOM 2538 CD ARG A 324 -16.622 27.464 43.425 1.00 66.14 A C
ANISOU 2538 CD ARG A 324 9327 4405 11397 143 4055 -2532 A C
ATOM 2539 NE ARG A 324 -18.011 27.233 43.816 1.00 70.75 A N
ANISOU 2539 NE ARG A 324 10020 4908 11955 197 4083 -2271 A N
ATOM 2540 CZ ARG A 324 -18.409 26.252 44.612 1.00 74.39 A C
ANISOU 2540 CZ ARG A 324 10610 5548 12108 294 3905 -2212 A C
ATOM 2541 NH1 ARG A 324 -17.526 25.395 45.112 1.00 51.56 A N1+
ANISOU 2541 NH1 ARG A 324 7765 2927 8898 385 3689 -2371 A N1+
ATOM 2542 NH2 ARG A 324 -19.692 26.119 44.919 1.00 63.61 A N
ANISOU 2542 NH2 ARG A 324 9327 4100 10744 316 3959 -1985 A N
ATOM 2543 N ILE A 325 -13.100 23.436 42.001 1.00 55.12 A N
ANISOU 2543 N ILE A 325 8142 3809 8992 569 3102 -2500 A N
ATOM 2544 CA ILE A 325 -12.501 22.107 42.228 1.00 55.14 A C
ANISOU 2544 CA ILE A 325 8281 4057 8613 780 2867 -2461 A C
ATOM 2545 C ILE A 325 -11.251 22.310 43.099 1.00 63.71 A C
ANISOU 2545 C ILE A 325 9184 5517 9506 853 2805 -2871 A C
ATOM 2546 O ILE A 325 -11.030 21.534 44.022 1.00 65.21 A O
ANISOU 2546 O ILE A 325 9451 5975 9351 1053 2675 -2917 A O
ATOM 2547 CB ILE A 325 -12.217 21.334 40.889 1.00 55.97 A C
ANISOU 2547 CB ILE A 325 8495 4065 8705 819 2760 -2212 A C
ATOM 2548 CG1 ILE A 325 -13.540 20.983 40.160 1.00 53.62 A C
ANISOU 2548 CG1 ILE A 325 8371 3487 8514 751 2802 -1823 A C
ATOM 2549 CG2 ILE A 325 -11.343 20.056 41.096 1.00 56.53 A C
ANISOU 2549 CG2 ILE A 325 8691 4391 8397 1059 2555 -2220 A C
ATOM 2550 CD1 ILE A 325 -13.396 20.677 38.680 1.00 56.40 A C
ANISOU 2550 CD1 ILE A 325 8756 3709 8966 701 2768 -1612 A C
ATOM 2551 N ASP A 326 -10.512 23.411 42.871 1.00 63.63 A N
ANISOU 2551 N ASP A 326 8925 5534 9719 683 2928 -3176 A N
ATOM 2552 CA ASP A 326 -9.348 23.813 43.669 1.00 67.58 A C
ANISOU 2552 CA ASP A 326 9184 6420 10073 680 2908 -3635 A C
ATOM 2553 C ASP A 326 -9.762 24.154 45.102 1.00 78.25 A C
ANISOU 2553 C ASP A 326 10484 7938 11308 676 2969 -3852 A C
ATOM 2554 O ASP A 326 -8.967 23.972 46.025 1.00 81.04 A O
ANISOU 2554 O ASP A 326 10697 8729 11367 777 2872 -4159 A O
ATOM 2555 CB ASP A 326 -8.632 25.023 43.036 1.00 69.93 A C
ANISOU 2555 CB ASP A 326 9241 6630 10697 427 3095 -3913 A C
ATOM 2556 CG ASP A 326 -7.447 24.695 42.141 1.00 77.80 A C
ANISOU 2556 CG ASP A 326 10152 7765 11645 463 2984 -3959 A C
ATOM 2557 OD1 ASP A 326 -7.062 23.501 42.066 1.00 78.83 A O
ANISOU 2557 OD1 ASP A 326 10392 8103 11456 710 2748 -3809 A O
ATOM 2558 OD2 ASP A 326 -6.904 25.627 41.513 1.00 80.83 A O1-
ANISOU 2558 OD2 ASP A 326 10369 8035 12308 250 3155 -4145 A O1-
ATOM 2559 N GLY A 327 -10.996 24.651 45.256 1.00 76.24 A N
ANISOU 2559 N GLY A 327 10330 7365 11275 569 3132 -3691 A N
ATOM 2560 CA GLY A 327 -11.595 25.017 46.533 1.00 78.04 A C
ANISOU 2560 CA GLY A 327 10537 7680 11434 550 3219 -3851 A C
ATOM 2561 C GLY A 327 -11.822 23.810 47.415 1.00 84.78 A C
ANISOU 2561 C GLY A 327 11561 8791 11862 818 3017 -3712 A C
ATOM 2562 O GLY A 327 -11.312 23.762 48.537 1.00 86.40 A O
ANISOU 2562 O GLY A 327 11656 9379 11792 904 2964 -3997 A O
ATOM 2563 N ARG A 328 -12.542 22.795 46.891 1.00 81.98 A N
ANISOU 2563 N ARG A 328 11474 8245 11430 952 2916 -3279 A N
ATOM 2564 CA ARG A 328 -12.811 21.541 47.606 1.00 82.95 A C
ANISOU 2564 CA ARG A 328 11819 8536 11162 1212 2766 -3091 A C
ATOM 2565 C ARG A 328 -11.489 20.756 47.819 1.00 89.43 A C
ANISOU 2565 C ARG A 328 12600 9769 11610 1464 2571 -3216 A C
ATOM 2566 O ARG A 328 -11.410 19.915 48.719 1.00 90.13 A O
ANISOU 2566 O ARG A 328 12812 10113 11321 1723 2470 -3164 A O
ATOM 2567 CB ARG A 328 -13.876 20.699 46.857 1.00 81.66 A C
ANISOU 2567 CB ARG A 328 11949 8027 11052 1230 2758 -2628 A C
ATOM 2568 CG ARG A 328 -14.493 19.487 47.608 1.00 93.29 A C
ANISOU 2568 CG ARG A 328 13706 9556 12184 1444 2686 -2395 A C
ATOM 2569 CD ARG A 328 -14.701 19.634 49.119 1.00105.05 A C
ANISOU 2569 CD ARG A 328 15172 11285 13456 1537 2714 -2564 A C
ATOM 2570 NE ARG A 328 -15.658 20.680 49.483 1.00113.62 A N
ANISOU 2570 NE ARG A 328 16158 12198 14813 1319 2888 -2639 A N
ATOM 2571 CZ ARG A 328 -15.689 21.290 50.666 1.00129.45 A C
ANISOU 2571 CZ ARG A 328 18029 14410 16746 1308 2953 -2914 A C
ATOM 2572 NH1 ARG A 328 -14.800 20.981 51.604 1.00117.21 A N1+
ANISOU 2572 NH1 ARG A 328 16399 13292 14844 1499 2844 -3151 A N1+
ATOM 2573 NH2 ARG A 328 -16.599 22.221 50.916 1.00116.58 A N
ANISOU 2573 NH2 ARG A 328 16332 12582 15384 1116 3134 -2958 A N
ATOM 2574 N LEU A 329 -10.441 21.094 47.044 1.00 87.07 A N
ANISOU 2574 N LEU A 329 12115 9557 11412 1401 2537 -3389 A N
ATOM 2575 CA LEU A 329 -9.131 20.468 47.168 1.00 89.19 A C
ANISOU 2575 CA LEU A 329 12296 10244 11348 1636 2363 -3526 A C
ATOM 2576 C LEU A 329 -8.280 21.163 48.260 1.00 97.26 A C
ANISOU 2576 C LEU A 329 12991 11772 12190 1632 2355 -4015 A C
ATOM 2577 O LEU A 329 -8.405 20.827 49.442 1.00 98.51 A O
ANISOU 2577 O LEU A 329 13166 12246 12016 1826 2297 -4077 A O
ATOM 2578 CB LEU A 329 -8.404 20.467 45.814 1.00 88.10 A C
ANISOU 2578 CB LEU A 329 12108 9982 11386 1568 2330 -3478 A C
ATOM 2579 CG LEU A 329 -8.178 19.099 45.202 1.00 92.06 A C
ANISOU 2579 CG LEU A 329 12865 10451 11665 1831 2185 -3146 A C
ATOM 2580 CD1 LEU A 329 -8.774 19.017 43.816 1.00 89.41 A C
ANISOU 2580 CD1 LEU A 329 12696 9641 11634 1666 2244 -2833 A C
ATOM 2581 CD2 LEU A 329 -6.703 18.761 45.166 1.00 97.04 A C
ANISOU 2581 CD2 LEU A 329 13322 11494 12052 2022 2046 -3343 A C
ATOM 2582 N TYR A 330 -7.461 22.154 47.857 1.00 95.14 A N
ANISOU 2582 N TYR A 330 12425 11581 12142 1394 2435 -4368 A N
ATOM 2583 CA TYR A 330 -6.486 22.895 48.664 1.00 98.36 A C
ANISOU 2583 CA TYR A 330 12470 12489 12413 1315 2449 -4901 A C
ATOM 2584 C TYR A 330 -7.074 23.901 49.681 1.00102.25 A C
ANISOU 2584 C TYR A 330 12842 12996 13012 1099 2629 -5194 A C
ATOM 2585 O TYR A 330 -6.333 24.353 50.559 1.00105.21 A O
ANISOU 2585 O TYR A 330 12933 13868 13176 1066 2622 -5643 A O
ATOM 2586 CB TYR A 330 -5.508 23.636 47.734 1.00100.76 A C
ANISOU 2586 CB TYR A 330 12526 12791 12968 1080 2520 -5166 A C
ATOM 2587 CG TYR A 330 -4.979 22.779 46.602 1.00101.81 A C
ANISOU 2587 CG TYR A 330 12773 12853 13058 1249 2374 -4886 A C
ATOM 2588 CD1 TYR A 330 -3.892 21.929 46.792 1.00105.67 A C
ANISOU 2588 CD1 TYR A 330 13161 13849 13140 1545 2164 -4960 A C
ATOM 2589 CD2 TYR A 330 -5.573 22.808 45.343 1.00 99.88 A C
ANISOU 2589 CD2 TYR A 330 12728 12059 13162 1129 2452 -4543 A C
ATOM 2590 CE1 TYR A 330 -3.410 21.128 45.756 1.00105.37 A C
ANISOU 2590 CE1 TYR A 330 13239 13731 13066 1707 2049 -4706 A C
ATOM 2591 CE2 TYR A 330 -5.098 22.013 44.300 1.00 99.52 A C
ANISOU 2591 CE2 TYR A 330 12788 11953 13071 1270 2328 -4302 A C
ATOM 2592 CZ TYR A 330 -4.014 21.177 44.509 1.00109.52 A C
ANISOU 2592 CZ TYR A 330 13972 13689 13953 1553 2132 -4388 A C
ATOM 2593 OH TYR A 330 -3.539 20.403 43.474 1.00110.45 A O
ANISOU 2593 OH TYR A 330 14202 13733 14033 1694 2029 -4159 A O
ATOM 2594 N GLY A 331 -8.360 24.240 49.565 1.00 95.32 A N
ANISOU 2594 N GLY A 331 12161 11619 12439 956 2790 -4960 A N
ATOM 2595 CA GLY A 331 -9.010 25.183 50.475 1.00 95.47 A C
ANISOU 2595 CA GLY A 331 12098 11588 12588 759 2988 -5201 A C
ATOM 2596 C GLY A 331 -9.424 26.506 49.859 1.00 96.42 A C
ANISOU 2596 C GLY A 331 12151 11248 13238 396 3291 -5314 A C
ATOM 2597 O GLY A 331 -8.841 26.947 48.865 1.00 95.37 A O
ANISOU 2597 O GLY A 331 11925 10961 13351 246 3365 -5373 A O
ATOM 2598 N GLU A 332 -10.419 27.162 50.486 1.00 92.44 A N
ANISOU 2598 N GLU A 332 11693 10527 12903 267 3489 -5347 A N
ATOM 2599 CA GLU A 332 -11.005 28.444 50.080 1.00 91.22 A C
ANISOU 2599 CA GLU A 332 11512 9906 13243 -33 3828 -5421 A C
ATOM 2600 C GLU A 332 -9.954 29.563 49.988 1.00 96.16 A C
ANISOU 2600 C GLU A 332 11850 10633 14055 -324 4033 -5950 A C
ATOM 2601 O GLU A 332 -10.094 30.429 49.127 1.00 94.99 A O
ANISOU 2601 O GLU A 332 11705 10054 14332 -531 4292 -5924 A O
ATOM 2602 CB GLU A 332 -12.145 28.825 51.036 1.00 92.98 A C
ANISOU 2602 CB GLU A 332 11815 10002 13511 -66 3981 -5416 A C
ATOM 2603 CG GLU A 332 -13.004 30.020 50.626 1.00103.35 A C
ANISOU 2603 CG GLU A 332 13164 10781 15325 -297 4346 -5376 A C
ATOM 2604 CD GLU A 332 -13.673 30.045 49.260 1.00112.10 A C
ANISOU 2604 CD GLU A 332 14440 11390 16762 -281 4420 -4894 A C
ATOM 2605 OE1 GLU A 332 -13.842 28.968 48.643 1.00 96.68 A O
ANISOU 2605 OE1 GLU A 332 12643 9440 14650 -84 4172 -4494 A O
ATOM 2606 OE2 GLU A 332 -14.066 31.152 48.824 1.00 98.88 A O1-
ANISOU 2606 OE2 GLU A 332 12746 9323 15499 -461 4748 -4915 A O1-
ATOM 2607 N GLU A 333 -8.894 29.525 50.829 1.00 94.80 A N
ANISOU 2607 N GLU A 333 11426 11041 13553 -333 3927 -6419 A N
ATOM 2608 CA GLU A 333 -7.811 30.521 50.797 1.00 97.15 A C
ANISOU 2608 CA GLU A 333 11418 11516 13979 -640 4116 -6984 A C
ATOM 2609 C GLU A 333 -7.000 30.435 49.500 1.00 98.16 A C
ANISOU 2609 C GLU A 333 11506 11533 14257 -676 4080 -6893 A C
ATOM 2610 O GLU A 333 -6.591 31.474 48.980 1.00 98.34 A O
ANISOU 2610 O GLU A 333 11406 11330 14628 -985 4369 -7161 A O
ATOM 2611 CB GLU A 333 -6.871 30.380 52.001 1.00102.09 A C
ANISOU 2611 CB GLU A 333 11751 12892 14145 -614 3970 -7495 A C
ATOM 2612 CG GLU A 333 -7.455 30.912 53.298 1.00113.31 A C
ANISOU 2612 CG GLU A 333 13116 14439 15498 -722 4121 -7790 A C
ATOM 2613 CD GLU A 333 -8.276 29.934 54.117 1.00131.96 A C
ANISOU 2613 CD GLU A 333 15687 16910 17543 -394 3913 -7440 A C
ATOM 2614 OE1 GLU A 333 -8.505 30.232 55.312 1.00130.78 A O
ANISOU 2614 OE1 GLU A 333 15453 16992 17246 -453 3994 -7724 A O
ATOM 2615 OE2 GLU A 333 -8.689 28.878 53.581 1.00120.93 A O1-
ANISOU 2615 OE2 GLU A 333 14540 15367 16040 -93 3690 -6900 A O1-
ATOM 2616 N PHE A 334 -6.785 29.204 48.976 1.00 92.28 A N
ANISOU 2616 N PHE A 334 10883 10923 13257 -364 3753 -6515 A N
ATOM 2617 CA PHE A 334 -6.068 28.937 47.722 1.00 90.56 A C
ANISOU 2617 CA PHE A 334 10656 10615 13137 -348 3679 -6369 A C
ATOM 2618 C PHE A 334 -6.926 29.366 46.526 1.00 88.97 A C
ANISOU 2618 C PHE A 334 10673 9725 13407 -454 3883 -5969 A C
ATOM 2619 O PHE A 334 -6.399 29.909 45.547 1.00 88.60 A O
ANISOU 2619 O PHE A 334 10556 9477 13633 -624 4029 -6023 A O
ATOM 2620 CB PHE A 334 -5.689 27.445 47.618 1.00 91.30 A C
ANISOU 2620 CB PHE A 334 10848 11038 12802 40 3294 -6069 A C
ATOM 2621 CG PHE A 334 -4.952 27.062 46.355 1.00 92.02 A C
ANISOU 2621 CG PHE A 334 10940 11064 12959 83 3200 -5912 A C
ATOM 2622 CD1 PHE A 334 -3.586 27.314 46.217 1.00 98.15 A C
ANISOU 2622 CD1 PHE A 334 11413 12233 13645 -14 3180 -6320 A C
ATOM 2623 CD2 PHE A 334 -5.616 26.440 45.308 1.00 91.05 A C
ANISOU 2623 CD2 PHE A 334 11103 10521 12972 210 3136 -5376 A C
ATOM 2624 CE1 PHE A 334 -2.901 26.960 45.042 1.00 97.86 A C
ANISOU 2624 CE1 PHE A 334 11376 12136 13669 26 3100 -6174 A C
ATOM 2625 CE2 PHE A 334 -4.930 26.085 44.139 1.00 92.96 A C
ANISOU 2625 CE2 PHE A 334 11344 10712 13266 245 3055 -5242 A C
ATOM 2626 CZ PHE A 334 -3.579 26.346 44.015 1.00 93.40 A C
ANISOU 2626 CZ PHE A 334 11113 11133 13243 161 3037 -5633 A C
ATOM 2627 N ARG A 335 -8.252 29.123 46.619 1.00 81.13 A N
ANISOU 2627 N ARG A 335 9933 8403 12491 -343 3898 -5568 A N
ATOM 2628 CA ARG A 335 -9.234 29.497 45.603 1.00 77.57 A C
ANISOU 2628 CA ARG A 335 9675 7364 12436 -399 4082 -5159 A C
ATOM 2629 C ARG A 335 -9.207 31.017 45.400 1.00 82.86 A C
ANISOU 2629 C ARG A 335 10231 7705 13546 -718 4504 -5433 A C
ATOM 2630 O ARG A 335 -9.123 31.485 44.262 1.00 82.42 A O
ANISOU 2630 O ARG A 335 10204 7311 13802 -812 4669 -5279 A O
ATOM 2631 CB ARG A 335 -10.633 29.013 46.009 1.00 72.69 A C
ANISOU 2631 CB ARG A 335 9287 6570 11762 -240 4030 -4777 A C
ATOM 2632 CG ARG A 335 -11.692 29.328 44.973 1.00 73.48 A C
ANISOU 2632 CG ARG A 335 9555 6148 12216 -264 4195 -4337 A C
ATOM 2633 CD ARG A 335 -13.059 28.784 45.328 1.00 76.45 A C
ANISOU 2633 CD ARG A 335 10132 6405 12512 -117 4129 -3971 A C
ATOM 2634 NE ARG A 335 -14.079 29.438 44.507 1.00 85.78 A N
ANISOU 2634 NE ARG A 335 11399 7136 14057 -171 4357 -3640 A N
ATOM 2635 CZ ARG A 335 -14.854 30.446 44.909 1.00 97.02 A C
ANISOU 2635 CZ ARG A 335 12810 8309 15744 -271 4658 -3684 A C
ATOM 2636 NH1 ARG A 335 -14.771 30.906 46.151 1.00 91.67 A N1+
ANISOU 2636 NH1 ARG A 335 12047 7770 15012 -357 4768 -4065 A N1+
ATOM 2637 NH2 ARG A 335 -15.724 30.994 44.072 1.00 73.44 A N
ANISOU 2637 NH2 ARG A 335 9890 4951 13062 -269 4859 -3344 A N
ATOM 2638 N GLN A 336 -9.220 31.771 46.518 1.00 80.75 A N
ANISOU 2638 N GLN A 336 9840 7552 13290 -883 4693 -5854 A N
ATOM 2639 CA GLN A 336 -9.170 33.234 46.571 1.00 82.31 A C
ANISOU 2639 CA GLN A 336 9940 7453 13882 -1205 5145 -6197 A C
ATOM 2640 C GLN A 336 -7.865 33.757 45.975 1.00 87.39 A C
ANISOU 2640 C GLN A 336 10380 8180 14643 -1433 5270 -6560 A C
ATOM 2641 O GLN A 336 -7.884 34.794 45.315 1.00 86.45 A O
ANISOU 2641 O GLN A 336 10277 7628 14942 -1648 5651 -6605 A O
ATOM 2642 CB GLN A 336 -9.307 33.718 48.023 1.00 86.13 A C
ANISOU 2642 CB GLN A 336 10312 8162 14253 -1329 5266 -6637 A C
ATOM 2643 CG GLN A 336 -10.698 33.536 48.646 1.00 84.29 A C
ANISOU 2643 CG GLN A 336 10274 7747 14005 -1173 5268 -6330 A C
ATOM 2644 CD GLN A 336 -11.738 34.511 48.152 1.00 94.28 A C
ANISOU 2644 CD GLN A 336 11692 8386 15744 -1263 5662 -6093 A C
ATOM 2645 NE2 GLN A 336 -12.972 34.048 48.032 1.00 77.63 A N
ANISOU 2645 NE2 GLN A 336 9786 6070 13639 -1048 5579 -5598 A N
ATOM 2646 OE1 GLN A 336 -11.462 35.691 47.912 1.00 91.32 A O
ANISOU 2646 OE1 GLN A 336 11254 7717 15726 -1519 6064 -6357 A O
ATOM 2647 N PHE A 337 -6.740 33.024 46.191 1.00 85.96 A N
ANISOU 2647 N PHE A 337 10013 8560 14087 -1367 4963 -6801 A N
ATOM 2648 CA PHE A 337 -5.415 33.380 45.688 1.00 88.32 A C
ANISOU 2648 CA PHE A 337 10082 9044 14430 -1570 5032 -7171 A C
ATOM 2649 C PHE A 337 -5.340 33.186 44.182 1.00 90.53 A C
ANISOU 2649 C PHE A 337 10495 8974 14930 -1503 5024 -6753 A C
ATOM 2650 O PHE A 337 -4.774 34.048 43.505 1.00 91.90 A O
ANISOU 2650 O PHE A 337 10583 8923 15411 -1758 5319 -6946 A O
ATOM 2651 CB PHE A 337 -4.303 32.584 46.397 1.00 92.26 A C
ANISOU 2651 CB PHE A 337 10330 10303 14421 -1462 4685 -7511 A C
ATOM 2652 CG PHE A 337 -2.890 32.863 45.885 1.00 96.73 A C
ANISOU 2652 CG PHE A 337 10625 11141 14989 -1658 4724 -7901 A C
ATOM 2653 CD1 PHE A 337 -2.316 34.127 46.018 1.00104.12 A C
ANISOU 2653 CD1 PHE A 337 11346 12028 16185 -2087 5118 -8465 A C
ATOM 2654 CD2 PHE A 337 -2.140 31.864 45.260 1.00 98.19 A C
ANISOU 2654 CD2 PHE A 337 10772 11618 14918 -1425 4393 -7714 A C
ATOM 2655 CE1 PHE A 337 -1.019 34.386 45.530 1.00107.35 A C
ANISOU 2655 CE1 PHE A 337 11493 12698 16595 -2293 5170 -8842 A C
ATOM 2656 CE2 PHE A 337 -0.844 32.126 44.776 1.00103.41 A C
ANISOU 2656 CE2 PHE A 337 11167 12547 15577 -1605 4433 -8076 A C
ATOM 2657 CZ PHE A 337 -0.293 33.385 44.915 1.00105.13 A C
ANISOU 2657 CZ PHE A 337 11159 12734 16051 -2045 4817 -8641 A C
ATOM 2658 N LYS A 338 -5.918 32.079 43.649 1.00 83.25 A N
ANISOU 2658 N LYS A 338 9783 7996 13851 -1179 4712 -6194 A N
ATOM 2659 CA LYS A 338 -5.930 31.829 42.209 1.00 80.27 A C
ANISOU 2659 CA LYS A 338 9538 7313 13650 -1101 4685 -5775 A C
ATOM 2660 C LYS A 338 -6.820 32.878 41.518 1.00 83.86 A C
ANISOU 2660 C LYS A 338 10134 7138 14589 -1237 5085 -5541 A C
ATOM 2661 O LYS A 338 -6.501 33.307 40.408 1.00 82.72 A O
ANISOU 2661 O LYS A 338 9999 6727 14704 -1326 5255 -5432 A O
ATOM 2662 CB LYS A 338 -6.372 30.394 41.887 1.00 79.11 A C
ANISOU 2662 CB LYS A 338 9584 7268 13208 -753 4289 -5279 A C
ATOM 2663 CG LYS A 338 -5.245 29.366 41.994 1.00 86.59 A C
ANISOU 2663 CG LYS A 338 10417 8738 13747 -585 3941 -5406 A C
ATOM 2664 CD LYS A 338 -4.514 29.130 40.663 1.00 91.25 A C
ANISOU 2664 CD LYS A 338 10998 9251 14423 -579 3891 -5256 A C
ATOM 2665 CE LYS A 338 -3.877 27.745 40.604 1.00104.47 A C
ANISOU 2665 CE LYS A 338 12682 11337 15676 -292 3506 -5152 A C
ATOM 2666 NZ LYS A 338 -3.461 27.347 39.230 1.00114.05 A N1+
ANISOU 2666 NZ LYS A 338 13948 12416 16969 -249 3441 -4908 A N1+
ATOM 2667 N ALA A 339 -7.887 33.340 42.219 1.00 81.18 A N
ANISOU 2667 N ALA A 339 9895 6582 14368 -1245 5259 -5485 A N
ATOM 2668 CA ALA A 339 -8.800 34.406 41.779 1.00 81.67 A C
ANISOU 2668 CA ALA A 339 10086 6076 14868 -1336 5675 -5281 A C
ATOM 2669 C ALA A 339 -8.070 35.745 41.645 1.00 87.84 A C
ANISOU 2669 C ALA A 339 10742 6638 15995 -1669 6138 -5713 A C
ATOM 2670 O ALA A 339 -8.305 36.473 40.677 1.00 87.11 A O
ANISOU 2670 O ALA A 339 10745 6085 16265 -1719 6459 -5487 A O
ATOM 2671 CB ALA A 339 -9.950 34.555 42.768 1.00 82.69 A C
ANISOU 2671 CB ALA A 339 10312 6124 14984 -1270 5738 -5216 A C
ATOM 2672 N LEU A 340 -7.192 36.063 42.623 1.00 87.08 A N
ANISOU 2672 N LEU A 340 10428 6887 15770 -1898 6188 -6338 A N
ATOM 2673 CA LEU A 340 -6.399 37.292 42.666 1.00 90.54 A C
ANISOU 2673 CA LEU A 340 10719 7188 16495 -2276 6637 -6864 A C
ATOM 2674 C LEU A 340 -5.262 37.245 41.641 1.00 93.44 A C
ANISOU 2674 C LEU A 340 10975 7623 16904 -2374 6618 -6938 A C
ATOM 2675 O LEU A 340 -4.962 38.277 41.038 1.00 94.75 A O
ANISOU 2675 O LEU A 340 11148 7408 17446 -2616 7060 -7068 A O
ATOM 2676 CB LEU A 340 -5.856 37.549 44.080 1.00 94.09 A C
ANISOU 2676 CB LEU A 340 10940 8073 16737 -2498 6662 -7533 A C
ATOM 2677 CG LEU A 340 -4.991 38.814 44.327 1.00103.96 A C
ANISOU 2677 CG LEU A 340 12005 9248 18247 -2959 7149 -8198 A C
ATOM 2678 CD1 LEU A 340 -5.652 40.083 43.832 1.00105.60 A C
ANISOU 2678 CD1 LEU A 340 12418 8701 19003 -3117 7749 -8072 A C
ATOM 2679 CD2 LEU A 340 -4.762 39.000 45.771 1.00109.19 A C
ANISOU 2679 CD2 LEU A 340 12467 10339 18681 -3141 7158 -8787 A C
ATOM 2680 N GLY A 341 -4.672 36.062 41.442 1.00 87.24 A N
ANISOU 2680 N GLY A 341 10107 7297 15741 -2176 6138 -6840 A N
ATOM 2681 CA GLY A 341 -3.632 35.822 40.449 1.00 86.71 A C
ANISOU 2681 CA GLY A 341 9940 7344 15661 -2212 6052 -6855 A C
ATOM 2682 C GLY A 341 -4.184 35.965 39.045 1.00 89.11 A C
ANISOU 2682 C GLY A 341 10467 7119 16272 -2103 6191 -6294 A C
ATOM 2683 O GLY A 341 -3.452 36.336 38.123 1.00 89.31 A O
ANISOU 2683 O GLY A 341 10438 7023 16473 -2238 6353 -6344 A O
ATOM 2684 N GLY A 342 -5.482 35.684 38.898 1.00 84.22 A N
ANISOU 2684 N GLY A 342 10082 6217 15702 -1861 6134 -5768 A N
ATOM 2685 CA GLY A 342 -6.203 35.820 37.640 1.00 82.53 A C
ANISOU 2685 CA GLY A 342 10068 5546 15742 -1721 6259 -5198 A C
ATOM 2686 C GLY A 342 -6.303 37.271 37.217 1.00 89.85 A C
ANISOU 2686 C GLY A 342 11046 5947 17147 -1937 6852 -5266 A C
ATOM 2687 O GLY A 342 -6.018 37.614 36.063 1.00 89.52 A O
ANISOU 2687 O GLY A 342 11050 5647 17318 -1957 7034 -5065 A O
ATOM 2688 N TRP A 343 -6.641 38.149 38.187 1.00 89.35 A N
ANISOU 2688 N TRP A 343 10977 5724 17249 -2109 7185 -5579 A N
ATOM 2689 CA TRP A 343 -6.724 39.593 37.995 1.00 92.45 A C
ANISOU 2689 CA TRP A 343 11436 5590 18102 -2337 7821 -5718 A C
ATOM 2690 C TRP A 343 -5.385 40.130 37.473 1.00 98.43 A C
ANISOU 2690 C TRP A 343 12052 6344 19004 -2642 8061 -6116 A C
ATOM 2691 O TRP A 343 -5.372 40.938 36.546 1.00100.12 A O
ANISOU 2691 O TRP A 343 12379 6088 19574 -2705 8482 -5942 A O
ATOM 2692 CB TRP A 343 -7.117 40.280 39.312 1.00 94.34 A C
ANISOU 2692 CB TRP A 343 11655 5777 18412 -2506 8080 -6114 A C
ATOM 2693 CG TRP A 343 -7.318 41.762 39.190 1.00 99.47 A C
ANISOU 2693 CG TRP A 343 12417 5831 19546 -2721 8780 -6241 A C
ATOM 2694 CD1 TRP A 343 -6.388 42.739 39.382 1.00106.59 A C
ANISOU 2694 CD1 TRP A 343 13217 6609 20674 -3126 9231 -6825 A C
ATOM 2695 CD2 TRP A 343 -8.536 42.427 38.861 1.00 99.91 A C
ANISOU 2695 CD2 TRP A 343 12714 5336 19913 -2534 9137 -5776 A C
ATOM 2696 CE2 TRP A 343 -8.275 43.814 38.879 1.00108.47 A C
ANISOU 2696 CE2 TRP A 343 13860 5936 21417 -2822 9824 -6090 A C
ATOM 2697 CE3 TRP A 343 -9.833 41.985 38.555 1.00 98.47 A C
ANISOU 2697 CE3 TRP A 343 12692 5038 19684 -2150 8957 -5128 A C
ATOM 2698 NE1 TRP A 343 -6.949 43.973 39.178 1.00109.33 A N
ANISOU 2698 NE1 TRP A 343 13760 6307 21472 -3204 9874 -6742 A N
ATOM 2699 CZ2 TRP A 343 -9.250 44.760 38.562 1.00109.51 A C
ANISOU 2699 CZ2 TRP A 343 14229 5453 21926 -2691 10341 -5734 A C
ATOM 2700 CZ3 TRP A 343 -10.807 42.926 38.273 1.00101.51 A C
ANISOU 2700 CZ3 TRP A 343 13272 4875 20422 -2027 9439 -4796 A C
ATOM 2701 CH2 TRP A 343 -10.514 44.294 38.281 1.00106.59 A C
ANISOU 2701 CH2 TRP A 343 13992 5025 21481 -2274 10125 -5081 A C
ATOM 2702 N LYS A 344 -4.263 39.646 38.040 1.00 94.76 A N
ANISOU 2702 N LYS A 344 11334 6427 18244 -2810 7792 -6627 A N
ATOM 2703 CA LYS A 344 -2.921 40.062 37.641 1.00 96.73 A C
ANISOU 2703 CA LYS A 344 11397 6780 18575 -3120 7976 -7069 A C
ATOM 2704 C LYS A 344 -2.565 39.571 36.230 1.00 97.01 A C
ANISOU 2704 C LYS A 344 11484 6757 18618 -2960 7819 -6654 A C
ATOM 2705 O LYS A 344 -1.877 40.299 35.506 1.00 98.68 A O
ANISOU 2705 O LYS A 344 11667 6733 19093 -3188 8180 -6804 A O
ATOM 2706 CB LYS A 344 -1.873 39.600 38.661 1.00100.92 A C
ANISOU 2706 CB LYS A 344 11608 8008 18730 -3295 7688 -7706 A C
ATOM 2707 CG LYS A 344 -1.792 40.481 39.914 1.00119.74 A C
ANISOU 2707 CG LYS A 344 13870 10439 21188 -3629 8021 -8331 A C
ATOM 2708 CD LYS A 344 -0.966 41.758 39.715 1.00132.96 A C
ANISOU 2708 CD LYS A 344 15451 11840 23228 -4108 8629 -8857 A C
ATOM 2709 CE LYS A 344 -1.144 42.720 40.868 1.00146.27 A C
ANISOU 2709 CE LYS A 344 17075 13457 25043 -4442 9032 -9424 A C
ATOM 2710 NZ LYS A 344 -0.513 44.038 40.597 1.00152.43 A N1+
ANISOU 2710 NZ LYS A 344 18021 14126 25770 -4552 9043 -9299 A N1+
ATOM 2711 N GLU A 345 -3.047 38.367 35.833 1.00 86.88 A N
ANISOU 2711 N GLU A 345 10285 5672 17053 -2587 7313 -6147 A N
ATOM 2712 CA GLU A 345 -2.809 37.828 34.500 1.00 83.27 A C
ANISOU 2712 CA GLU A 345 9888 5175 16575 -2415 7140 -5728 A C
ATOM 2713 C GLU A 345 -3.627 38.622 33.472 1.00 86.17 A C
ANISOU 2713 C GLU A 345 10490 4915 17337 -2337 7547 -5238 A C
ATOM 2714 O GLU A 345 -3.158 38.864 32.362 1.00 85.40 A O
ANISOU 2714 O GLU A 345 10416 4637 17397 -2368 7704 -5086 A O
ATOM 2715 CB GLU A 345 -3.131 36.323 34.448 1.00 80.45 A C
ANISOU 2715 CB GLU A 345 9567 5198 15803 -2066 6525 -5369 A C
ATOM 2716 CG GLU A 345 -2.590 35.590 33.228 1.00 87.39 A C
ANISOU 2716 CG GLU A 345 10451 6180 16573 -1928 6283 -5080 A C
ATOM 2717 CD GLU A 345 -1.262 36.022 32.632 1.00113.96 A C
ANISOU 2717 CD GLU A 345 13647 9611 20042 -2170 6457 -5416 A C
ATOM 2718 OE1 GLU A 345 -1.289 36.709 31.586 1.00112.11 A O
ANISOU 2718 OE1 GLU A 345 13508 8966 20124 -2236 6799 -5204 A O
ATOM 2719 OE2 GLU A 345 -0.199 35.670 33.194 1.00112.36 A O1-
ANISOU 2719 OE2 GLU A 345 13212 9891 19589 -2275 6253 -5869 A O1-
ATOM 2720 N LEU A 346 -4.839 39.047 33.863 1.00 84.20 A N
ANISOU 2720 N LEU A 346 10405 4354 17235 -2221 7731 -4991 A N
ATOM 2721 CA LEU A 346 -5.720 39.896 33.059 1.00 85.18 A C
ANISOU 2721 CA LEU A 346 10743 3901 17722 -2108 8161 -4529 A C
ATOM 2722 C LEU A 346 -5.048 41.256 32.878 1.00 94.39 A C
ANISOU 2722 C LEU A 346 11909 4666 19289 -2435 8804 -4879 A C
ATOM 2723 O LEU A 346 -5.017 41.779 31.763 1.00 95.47 A O
ANISOU 2723 O LEU A 346 12159 4441 19675 -2392 9114 -4574 A O
ATOM 2724 CB LEU A 346 -7.101 40.035 33.733 1.00 84.54 A C
ANISOU 2724 CB LEU A 346 10798 3650 17674 -1921 8208 -4274 A C
ATOM 2725 CG LEU A 346 -8.109 40.989 33.089 1.00 90.25 A C
ANISOU 2725 CG LEU A 346 11728 3801 18761 -1768 8692 -3812 A C
ATOM 2726 CD1 LEU A 346 -8.490 40.538 31.686 1.00 88.35 A C
ANISOU 2726 CD1 LEU A 346 11574 3504 18492 -1477 8553 -3175 A C
ATOM 2727 CD2 LEU A 346 -9.333 41.114 33.943 1.00 91.58 A C
ANISOU 2727 CD2 LEU A 346 11984 3883 18928 -1618 8719 -3669 A C
ATOM 2728 N GLN A 347 -4.456 41.787 33.969 1.00 94.37 A N
ANISOU 2728 N GLN A 347 11771 4762 19325 -2776 9002 -5543 A N
ATOM 2729 CA GLN A 347 -3.681 43.036 33.989 1.00 99.01 A C
ANISOU 2729 CA GLN A 347 12328 5025 20265 -3176 9623 -6023 A C
ATOM 2730 C GLN A 347 -2.447 42.863 33.092 1.00103.60 A C
ANISOU 2730 C GLN A 347 12778 5763 20824 -3331 9582 -6168 A C
ATOM 2731 O GLN A 347 -2.107 43.775 32.340 1.00106.85 A O
ANISOU 2731 O GLN A 347 13276 5738 21584 -3503 10108 -6182 A O
ATOM 2732 CB GLN A 347 -3.287 43.385 35.436 1.00103.31 A C
ANISOU 2732 CB GLN A 347 12704 5800 20751 -3512 9725 -6747 A C
ATOM 2733 CG GLN A 347 -2.816 44.813 35.659 1.00129.89 A C
ANISOU 2733 CG GLN A 347 16092 8730 24529 -3944 10470 -7247 A C
ATOM 2734 CD GLN A 347 -2.596 45.082 37.129 1.00151.46 A C
ANISOU 2734 CD GLN A 347 18691 11867 26989 -4150 10290 -7782 A C
ATOM 2735 NE2 GLN A 347 -3.628 45.561 37.809 1.00143.25 A N
ANISOU 2735 NE2 GLN A 347 17778 10373 26277 -4190 10791 -7861 A N
ATOM 2736 OE1 GLN A 347 -1.512 44.852 37.675 1.00150.04 A O
ANISOU 2736 OE1 GLN A 347 18218 12195 26596 -4440 10137 -8396 A O
ATOM 2737 N ASN A 348 -1.829 41.660 33.124 1.00 96.75 A N
ANISOU 2737 N ASN A 348 11720 5497 19544 -3238 8971 -6230 A N
ATOM 2738 CA ASN A 348 -0.671 41.293 32.307 1.00 96.24 A C
ANISOU 2738 CA ASN A 348 11508 5667 19390 -3333 8839 -6342 A C
ATOM 2739 C ASN A 348 -1.047 41.189 30.820 1.00 97.16 A C
ANISOU 2739 C ASN A 348 11822 5452 19643 -3070 8879 -5672 A C
ATOM 2740 O ASN A 348 -0.208 41.470 29.965 1.00 98.83 A O
ANISOU 2740 O ASN A 348 11992 5572 19985 -3216 9077 -5736 A O
ATOM 2741 CB ASN A 348 -0.058 39.965 32.795 1.00 93.67 A C
ANISOU 2741 CB ASN A 348 10950 6075 18564 -3231 8169 -6531 A C
ATOM 2742 CG ASN A 348 1.170 39.506 32.037 1.00112.74 A C
ANISOU 2742 CG ASN A 348 13187 8799 20850 -3313 8002 -6680 A C
ATOM 2743 ND2 ASN A 348 1.062 38.345 31.391 1.00 97.64 A N
ANISOU 2743 ND2 ASN A 348 11314 7114 18670 -2983 7519 -6243 A N
ATOM 2744 OD1 ASN A 348 2.222 40.169 32.033 1.00108.27 A O
ANISOU 2744 OD1 ASN A 348 12442 8284 20414 -3682 8309 -7204 A O
ATOM 2745 N SER A 349 -2.289 40.778 30.513 1.00 89.02 A N
ANISOU 2745 N SER A 349 10985 4278 18562 -2692 8692 -5047 A N
ATOM 2746 CA SER A 349 -2.740 40.633 29.129 1.00 86.12 A C
ANISOU 2746 CA SER A 349 10780 3670 18272 -2417 8697 -4398 A C
ATOM 2747 C SER A 349 -3.223 41.952 28.552 1.00 93.24 A C
ANISOU 2747 C SER A 349 11884 3919 19623 -2436 9374 -4158 A C
ATOM 2748 O SER A 349 -2.957 42.223 27.378 1.00 92.45 A O
ANISOU 2748 O SER A 349 11856 3604 19667 -2385 9575 -3874 A O
ATOM 2749 CB SER A 349 -3.833 39.579 29.014 1.00 82.82 A C
ANISOU 2749 CB SER A 349 10452 3439 17578 -2023 8208 -3859 A C
ATOM 2750 OG SER A 349 -3.302 38.325 29.394 1.00 85.42 A O
ANISOU 2750 OG SER A 349 10628 4331 17498 -1985 7623 -4046 A O
ATOM 2751 N VAL A 350 -3.922 42.781 29.365 1.00 93.51 A N
ANISOU 2751 N VAL A 350 12020 3631 19877 -2494 9750 -4261 A N
ATOM 2752 CA VAL A 350 -4.425 44.068 28.879 1.00 96.81 A C
ANISOU 2752 CA VAL A 350 12660 3390 20733 -2476 10450 -4019 A C
ATOM 2753 C VAL A 350 -3.258 44.977 28.498 1.00105.31 A C
ANISOU 2753 C VAL A 350 13713 4198 22100 -2856 10980 -4431 A C
ATOM 2754 O VAL A 350 -3.401 45.692 27.522 1.00107.24 A O
ANISOU 2754 O VAL A 350 14139 3976 22633 -2768 11446 -4077 A O
ATOM 2755 CB VAL A 350 -5.454 44.798 29.786 1.00102.52 A C
ANISOU 2755 CB VAL A 350 13521 3786 21647 -2431 10784 -4013 A C
ATOM 2756 CG1 VAL A 350 -6.723 43.969 29.974 1.00 98.21 A C
ANISOU 2756 CG1 VAL A 350 13018 3453 20844 -2028 10322 -3515 A C
ATOM 2757 CG2 VAL A 350 -4.858 45.221 31.124 1.00105.06 A C
ANISOU 2757 CG2 VAL A 350 13713 4199 22007 -2847 10942 -4790 A C
ATOM 2758 N ASN A 351 -2.104 44.921 29.206 1.00104.06 A N
ANISOU 2758 N ASN A 351 13325 4360 21852 -3264 10912 -5155 A N
ATOM 2759 CA ASN A 351 -0.940 45.759 28.864 1.00108.18 A C
ANISOU 2759 CA ASN A 351 13798 4666 22640 -3673 11422 -5600 A C
ATOM 2760 C ASN A 351 -0.249 45.277 27.582 1.00110.49 A C
ANISOU 2760 C ASN A 351 14041 5095 22843 -3592 11238 -5347 A C
ATOM 2761 O ASN A 351 0.254 46.104 26.813 1.00113.70 A O
ANISOU 2761 O ASN A 351 14535 5113 23552 -3767 11767 -5370 A O
ATOM 2762 CB ASN A 351 0.081 45.849 30.014 1.00112.95 A C
ANISOU 2762 CB ASN A 351 14131 5627 23156 -4152 11425 -6485 A C
ATOM 2763 CG ASN A 351 0.759 44.563 30.449 1.00139.06 A C
ANISOU 2763 CG ASN A 351 17131 9732 25972 -4139 10679 -6758 A C
ATOM 2764 ND2 ASN A 351 0.829 44.356 31.753 1.00134.73 A N
ANISOU 2764 ND2 ASN A 351 16420 9542 25229 -4274 10485 -7222 A N
ATOM 2765 OD1 ASN A 351 1.337 43.815 29.652 1.00131.21 A O
ANISOU 2765 OD1 ASN A 351 16032 9045 24776 -4037 10320 -6613 A O
ATOM 2766 N THR A 352 -0.210 43.944 27.368 1.00101.43 A N
ANISOU 2766 N THR A 352 12767 4486 21285 -3335 10515 -5118 A N
ATOM 2767 CA THR A 352 0.423 43.335 26.198 1.00 99.39 A C
ANISOU 2767 CA THR A 352 12454 4419 20891 -3231 10267 -4874 A C
ATOM 2768 C THR A 352 -0.339 43.750 24.930 1.00102.73 A C
ANISOU 2768 C THR A 352 13141 4362 21531 -2924 10566 -4149 A C
ATOM 2769 O THR A 352 0.291 44.164 23.950 1.00103.40 A O
ANISOU 2769 O THR A 352 13261 4243 21784 -3012 10870 -4080 A O
ATOM 2770 CB THR A 352 0.508 41.799 26.357 1.00100.69 A C
ANISOU 2770 CB THR A 352 12457 5234 20566 -3007 9455 -4791 A C
ATOM 2771 CG2 THR A 352 1.363 41.139 25.272 1.00 95.88 A C
ANISOU 2771 CG2 THR A 352 11755 4877 19797 -2957 9196 -4666 A C
ATOM 2772 OG1 THR A 352 1.055 41.489 27.640 1.00101.45 A O
ANISOU 2772 OG1 THR A 352 12326 5767 20453 -3230 9217 -5412 A O
ATOM 2773 N PHE A 353 -1.688 43.667 24.971 1.00 96.97 A N
ANISOU 2773 N PHE A 353 12581 3476 20788 -2563 10496 -3621 A N
ATOM 2774 CA PHE A 353 -2.560 44.014 23.851 1.00 96.73 A C
ANISOU 2774 CA PHE A 353 12773 3076 20905 -2208 10738 -2894 A C
ATOM 2775 C PHE A 353 -2.848 45.519 23.776 1.00104.55 A C
ANISOU 2775 C PHE A 353 13984 3375 22364 -2281 11575 -2841 A C
ATOM 2776 O PHE A 353 -3.018 46.060 22.681 1.00105.02 A O
ANISOU 2776 O PHE A 353 14207 3086 22612 -2104 11949 -2386 A O
ATOM 2777 CB PHE A 353 -3.878 43.233 23.949 1.00 95.43 A C
ANISOU 2777 CB PHE A 353 12658 3113 20490 -1793 10290 -2377 A C
ATOM 2778 CG PHE A 353 -3.827 41.827 23.396 1.00 93.11 A C
ANISOU 2778 CG PHE A 353 12248 3345 19783 -1597 9593 -2138 A C
ATOM 2779 CD1 PHE A 353 -4.403 41.524 22.167 1.00 95.00 A C
ANISOU 2779 CD1 PHE A 353 12570 3587 19938 -1262 9493 -1497 A C
ATOM 2780 CD2 PHE A 353 -3.216 40.800 24.107 1.00 93.24 A C
ANISOU 2780 CD2 PHE A 353 12076 3867 19485 -1735 9056 -2554 A C
ATOM 2781 CE1 PHE A 353 -4.360 40.221 21.654 1.00 91.73 A C
ANISOU 2781 CE1 PHE A 353 12060 3646 19148 -1110 8880 -1309 A C
ATOM 2782 CE2 PHE A 353 -3.156 39.501 23.585 1.00 91.73 A C
ANISOU 2782 CE2 PHE A 353 11809 4116 18926 -1551 8462 -2336 A C
ATOM 2783 CZ PHE A 353 -3.734 39.219 22.364 1.00 88.19 A C
ANISOU 2783 CZ PHE A 353 11454 3637 18417 -1259 8384 -1730 A C
ATOM 2784 N GLY A 354 -2.888 46.175 24.933 1.00103.65 A N
ANISOU 2784 N GLY A 354 13881 3075 22426 -2532 11877 -3302 A N
ATOM 2785 CA GLY A 354 -3.207 47.590 25.063 1.00107.58 A C
ANISOU 2785 CA GLY A 354 14608 2895 23373 -2622 12697 -3315 A C
ATOM 2786 C GLY A 354 -4.514 47.774 25.809 1.00109.39 A C
ANISOU 2786 C GLY A 354 14958 2973 23633 -2372 12737 -3079 A C
ATOM 2787 O GLY A 354 -5.511 47.121 25.483 1.00106.30 A O
ANISOU 2787 O GLY A 354 14592 2773 23025 -1944 12343 -2505 A O
ATOM 2788 N ALA A 355 -4.510 48.657 26.836 1.00107.68 A N
ANISOU 2788 N ALA A 355 14803 2433 23677 -2659 13218 -3551 A N
ATOM 2789 CA ALA A 355 -5.652 48.988 27.700 1.00106.77 A C
ANISOU 2789 CA ALA A 355 14804 2131 23634 -2486 13345 -3435 A C
ATOM 2790 C ALA A 355 -6.845 49.533 26.899 1.00108.22 A C
ANISOU 2790 C ALA A 355 15250 1872 23997 -1987 13696 -2628 A C
ATOM 2791 O ALA A 355 -7.979 49.518 27.391 1.00105.61 A O
ANISOU 2791 O ALA A 355 14982 1525 23620 -1702 13619 -2342 A O
ATOM 2792 CB ALA A 355 -5.226 50.008 28.741 1.00111.90 A C
ANISOU 2792 CB ALA A 355 15493 2438 24586 -2938 13930 -4123 A C
ATOM 2793 N THR A 356 -6.579 49.964 25.656 1.00104.53 A N
ANISOU 2793 N THR A 356 14915 1103 23700 -1862 14053 -2251 A N
ATOM 2794 CA THR A 356 -7.546 50.529 24.726 1.00105.63 A C
ANISOU 2794 CA THR A 356 15288 853 23993 -1367 14431 -1463 A C
ATOM 2795 C THR A 356 -7.899 49.589 23.552 1.00105.70 A C
ANISOU 2795 C THR A 356 15212 1277 23671 -953 13885 -811 A C
ATOM 2796 O THR A 356 -8.814 49.914 22.791 1.00107.45 A O
ANISOU 2796 O THR A 356 15578 1310 23937 -488 14099 -116 A O
ATOM 2797 CB THR A 356 -7.019 51.859 24.185 1.00115.61 A C
ANISOU 2797 CB THR A 356 16764 1893 25269 -1451 14647 -1414 A C
ATOM 2798 CG2 THR A 356 -5.752 51.694 23.278 1.00114.26 A C
ANISOU 2798 CG2 THR A 356 16537 1732 25144 -1644 14737 -1489 A C
ATOM 2799 OG1 THR A 356 -8.092 52.468 23.482 1.00116.27 A O
ANISOU 2799 OG1 THR A 356 17055 1863 25261 -931 14662 -672 A O
ATOM 2800 N ASN A 357 -7.174 48.467 23.386 1.00 97.99 A N
ANISOU 2800 N ASN A 357 14004 863 22366 -1112 13224 -1032 A N
ATOM 2801 CA ASN A 357 -7.387 47.507 22.291 1.00 94.44 A C
ANISOU 2801 CA ASN A 357 13462 829 21591 -788 12701 -503 A C
ATOM 2802 C ASN A 357 -8.789 46.893 22.337 1.00 97.07 A C
ANISOU 2802 C ASN A 357 13771 1444 21666 -342 12295 35 A C
ATOM 2803 O ASN A 357 -9.125 46.270 23.343 1.00 92.16 A O
ANISOU 2803 O ASN A 357 13040 1117 20859 -415 11882 -220 A O
ATOM 2804 CB ASN A 357 -6.334 46.396 22.317 1.00 87.51 A C
ANISOU 2804 CB ASN A 357 12323 540 20387 -1064 12078 -928 A C
ATOM 2805 CG ASN A 357 -6.073 45.719 20.984 1.00103.04 A C
ANISOU 2805 CG ASN A 357 14253 2741 22156 -875 11757 -518 A C
ATOM 2806 ND2 ASN A 357 -4.819 45.393 20.723 1.00 94.27 A N
ANISOU 2806 ND2 ASN A 357 13020 1807 20990 -1180 11622 -907 A N
ATOM 2807 OD1 ASN A 357 -6.974 45.463 20.179 1.00 94.72 A O
ANISOU 2807 OD1 ASN A 357 13243 1789 20959 -456 11616 128 A O
ATOM 2808 N PRO A 358 -9.607 47.027 21.251 1.00 97.68 A N
ANISOU 2808 N PRO A 358 13933 1477 21705 121 12398 772 A N
ATOM 2809 CA PRO A 358 -10.959 46.424 21.257 1.00 94.97 A C
ANISOU 2809 CA PRO A 358 13529 1466 21091 531 12008 1269 A C
ATOM 2810 C PRO A 358 -10.934 44.905 21.398 1.00 89.31 A C
ANISOU 2810 C PRO A 358 12589 1416 19928 471 11153 1150 A C
ATOM 2811 O PRO A 358 -11.959 44.313 21.741 1.00 83.78 A O
ANISOU 2811 O PRO A 358 11821 1008 19002 686 10797 1376 A O
ATOM 2812 CB PRO A 358 -11.553 46.844 19.906 1.00 99.74 A C
ANISOU 2812 CB PRO A 358 14221 1971 21704 991 12280 2024 A C
ATOM 2813 CG PRO A 358 -10.366 47.184 19.047 1.00106.62 A C
ANISOU 2813 CG PRO A 358 15148 2640 22721 802 12556 1916 A C
ATOM 2814 CD PRO A 358 -9.364 47.770 19.993 1.00103.82 A C
ANISOU 2814 CD PRO A 358 14854 1923 22671 298 12898 1187 A C
ATOM 2815 N LEU A 359 -9.754 44.286 21.182 1.00 83.28 A N
ANISOU 2815 N LEU A 359 11719 879 19044 170 10852 773 A N
ATOM 2816 CA LEU A 359 -9.541 42.857 21.366 1.00 78.20 A C
ANISOU 2816 CA LEU A 359 10892 819 17999 83 10095 596 A C
ATOM 2817 C LEU A 359 -9.638 42.477 22.850 1.00 80.26 A C
ANISOU 2817 C LEU A 359 11090 1218 18185 -125 9844 114 A C
ATOM 2818 O LEU A 359 -9.892 41.306 23.156 1.00 74.16 A O
ANISOU 2818 O LEU A 359 10204 900 17071 -95 9247 85 A O
ATOM 2819 CB LEU A 359 -8.179 42.424 20.814 1.00 77.28 A C
ANISOU 2819 CB LEU A 359 10690 866 17808 -175 9921 294 A C
ATOM 2820 CG LEU A 359 -8.046 42.144 19.317 1.00 80.97 A C
ANISOU 2820 CG LEU A 359 11151 1450 18163 23 9862 746 A C
ATOM 2821 CD1 LEU A 359 -6.640 41.773 18.998 1.00 80.32 A C
ANISOU 2821 CD1 LEU A 359 10982 1496 18041 -281 9730 344 A C
ATOM 2822 CD2 LEU A 359 -9.032 41.099 18.831 1.00 80.08 A C
ANISOU 2822 CD2 LEU A 359 10960 1796 17673 344 9335 1226 A C
ATOM 2823 N THR A 360 -9.480 43.480 23.770 1.00 80.87 A N
ANISOU 2823 N THR A 360 11251 896 18579 -331 10328 -260 A N
ATOM 2824 CA THR A 360 -9.563 43.276 25.227 1.00 79.83 A C
ANISOU 2824 CA THR A 360 11061 875 18395 -536 10160 -741 A C
ATOM 2825 C THR A 360 -11.010 43.392 25.770 1.00 81.99 A C
ANISOU 2825 C THR A 360 11398 1103 18651 -250 10174 -407 A C
ATOM 2826 O THR A 360 -11.211 43.261 26.983 1.00 79.91 A O
ANISOU 2826 O THR A 360 11100 917 18345 -384 10061 -756 A O
ATOM 2827 CB THR A 360 -8.591 44.173 26.003 1.00 91.28 A C
ANISOU 2827 CB THR A 360 12529 2011 20142 -951 10618 -1389 A C
ATOM 2828 CG2 THR A 360 -7.130 43.891 25.649 1.00 89.61 A C
ANISOU 2828 CG2 THR A 360 12195 1974 19880 -1267 10503 -1805 A C
ATOM 2829 OG1 THR A 360 -8.922 45.548 25.809 1.00 94.53 A O
ANISOU 2829 OG1 THR A 360 13140 1814 20964 -892 11369 -1221 A O
ATOM 2830 N ASN A 361 -12.010 43.600 24.884 1.00 79.03 A N
ANISOU 2830 N ASN A 361 11095 654 18280 151 10293 260 A N
ATOM 2831 CA ASN A 361 -13.423 43.577 25.286 1.00 78.17 A C
ANISOU 2831 CA ASN A 361 11006 597 18099 454 10243 619 A C
ATOM 2832 C ASN A 361 -13.774 42.149 25.607 1.00 78.51 A C
ANISOU 2832 C ASN A 361 10898 1214 17719 471 9510 605 A C
ATOM 2833 O ASN A 361 -13.257 41.259 24.926 1.00 76.40 A O
ANISOU 2833 O ASN A 361 10543 1274 17211 439 9108 644 A O
ATOM 2834 CB ASN A 361 -14.336 44.061 24.161 1.00 78.29 A C
ANISOU 2834 CB ASN A 361 11060 547 18140 896 10519 1338 A C
ATOM 2835 CG ASN A 361 -14.244 45.507 23.792 1.00 94.00 A C
ANISOU 2835 CG ASN A 361 13271 1871 20575 991 11307 1499 A C
ATOM 2836 ND2 ASN A 361 -15.248 45.959 23.062 1.00 83.84 A N
ANISOU 2836 ND2 ASN A 361 11948 685 19221 1434 11557 2123 A N
ATOM 2837 OD1 ASN A 361 -13.282 46.213 24.110 1.00 91.40 A O
ANISOU 2837 OD1 ASN A 361 13035 1163 20531 671 11707 1055 A O
ATOM 2838 N LEU A 362 -14.656 41.916 26.601 1.00 73.64 A N
ANISOU 2838 N LEU A 362 10263 710 17009 524 9356 560 A N
ATOM 2839 CA LEU A 362 -15.074 40.568 26.967 1.00 69.20 A C
ANISOU 2839 CA LEU A 362 9584 656 16051 541 8707 557 A C
ATOM 2840 C LEU A 362 -15.713 39.887 25.770 1.00 71.57 A C
ANISOU 2840 C LEU A 362 9821 1267 16104 825 8423 1119 A C
ATOM 2841 O LEU A 362 -15.438 38.723 25.532 1.00 66.89 A O
ANISOU 2841 O LEU A 362 9147 1064 15205 757 7919 1071 A O
ATOM 2842 CB LEU A 362 -16.037 40.577 28.163 1.00 68.74 A C
ANISOU 2842 CB LEU A 362 9535 618 15967 585 8679 484 A C
ATOM 2843 CG LEU A 362 -16.291 39.234 28.838 1.00 68.80 A C
ANISOU 2843 CG LEU A 362 9452 1090 15598 521 8067 341 A C
ATOM 2844 CD1 LEU A 362 -15.022 38.667 29.444 1.00 67.09 A C
ANISOU 2844 CD1 LEU A 362 9193 1029 15269 195 7802 -230 A C
ATOM 2845 CD2 LEU A 362 -17.348 39.361 29.893 1.00 71.98 A C
ANISOU 2845 CD2 LEU A 362 9871 1479 16000 598 8107 338 A C
ATOM 2846 N VAL A 363 -16.539 40.625 25.007 1.00 71.98 A N
ANISOU 2846 N VAL A 363 9910 1156 16283 1148 8770 1644 A N
ATOM 2847 CA VAL A 363 -17.172 40.131 23.788 1.00 70.78 A C
ANISOU 2847 CA VAL A 363 9673 1321 15900 1439 8570 2199 A C
ATOM 2848 C VAL A 363 -16.538 40.979 22.655 1.00 76.01 A C
ANISOU 2848 C VAL A 363 10407 1693 16782 1533 8998 2420 A C
ATOM 2849 O VAL A 363 -17.041 42.053 22.337 1.00 78.28 A O
ANISOU 2849 O VAL A 363 10777 1666 17301 1792 9507 2762 A O
ATOM 2850 CB VAL A 363 -18.734 40.159 23.831 1.00 74.89 A C
ANISOU 2850 CB VAL A 363 10130 2019 16305 1777 8564 2657 A C
ATOM 2851 CG1 VAL A 363 -19.333 39.402 22.653 1.00 73.76 A C
ANISOU 2851 CG1 VAL A 363 9843 2354 15829 2003 8232 3126 A C
ATOM 2852 CG2 VAL A 363 -19.272 39.597 25.148 1.00 72.06 A C
ANISOU 2852 CG2 VAL A 363 9745 1801 15832 1649 8297 2370 A C
ATOM 2853 N PRO A 364 -15.370 40.560 22.104 1.00 71.61 A N
ANISOU 2853 N PRO A 364 9834 1202 16174 1321 8838 2205 A N
ATOM 2854 CA PRO A 364 -14.714 41.396 21.090 1.00 74.16 A C
ANISOU 2854 CA PRO A 364 10237 1221 16719 1382 9275 2382 A C
ATOM 2855 C PRO A 364 -15.283 41.250 19.685 1.00 80.69 A C
ANISOU 2855 C PRO A 364 10999 2298 17360 1733 9225 3007 A C
ATOM 2856 O PRO A 364 -15.935 40.256 19.367 1.00 78.32 A O
ANISOU 2856 O PRO A 364 10562 2488 16708 1847 8748 3218 A O
ATOM 2857 CB PRO A 364 -13.269 40.907 21.126 1.00 73.65 A C
ANISOU 2857 CB PRO A 364 10152 1194 16638 1004 9078 1872 A C
ATOM 2858 CG PRO A 364 -13.365 39.470 21.510 1.00 74.49 A C
ANISOU 2858 CG PRO A 364 10133 1805 16364 900 8398 1699 A C
ATOM 2859 CD PRO A 364 -14.586 39.331 22.377 1.00 68.93 A C
ANISOU 2859 CD PRO A 364 9413 1203 15575 1035 8286 1802 A C
ATOM 2860 N ASN A 365 -15.022 42.258 18.844 1.00 82.52 A N
ANISOU 2860 N ASN A 365 11333 2195 17826 1897 9744 3291 A N
ATOM 2861 CA ASN A 365 -15.393 42.247 17.442 1.00 84.14 A C
ANISOU 2861 CA ASN A 365 11480 2623 17866 2236 9761 3876 A C
ATOM 2862 C ASN A 365 -14.257 41.541 16.697 1.00 87.91 A C
ANISOU 2862 C ASN A 365 11907 3290 18203 2005 9471 3683 A C
ATOM 2863 O ASN A 365 -13.106 41.997 16.722 1.00 89.63 A O
ANISOU 2863 O ASN A 365 12225 3163 18666 1754 9741 3356 A O
ATOM 2864 CB ASN A 365 -15.636 43.667 16.927 1.00 91.32 A C
ANISOU 2864 CB ASN A 365 12544 3067 19086 2553 10489 4295 A C
ATOM 2865 CG ASN A 365 -16.412 43.724 15.633 1.00117.24 A C
ANISOU 2865 CG ASN A 365 15740 6653 22152 3025 10523 5004 A C
ATOM 2866 ND2 ASN A 365 -17.297 44.704 15.527 1.00110.81 A N
ANISOU 2866 ND2 ASN A 365 14997 5628 21477 3438 11003 5472 A N
ATOM 2867 OD1 ASN A 365 -16.230 42.908 14.716 1.00111.40 A O
ANISOU 2867 OD1 ASN A 365 14867 6348 21111 3038 10141 5143 A O
ATOM 2868 N LEU A 366 -14.562 40.391 16.096 1.00 80.75 A N
ANISOU 2868 N LEU A 366 10841 2940 16900 2059 8922 3838 A N
ATOM 2869 CA LEU A 366 -13.532 39.632 15.410 1.00 77.90 A C
ANISOU 2869 CA LEU A 366 10431 2788 16380 1852 8619 3653 A C
ATOM 2870 C LEU A 366 -13.693 39.687 13.886 1.00 84.79 A C
ANISOU 2870 C LEU A 366 11245 3876 17093 2138 8681 4184 A C
ATOM 2871 O LEU A 366 -13.114 38.849 13.188 1.00 83.33 A O
ANISOU 2871 O LEU A 366 10984 3996 16682 2022 8338 4118 A O
ATOM 2872 CB LEU A 366 -13.485 38.181 15.928 1.00 72.63 A C
ANISOU 2872 CB LEU A 366 9654 2554 15388 1625 7956 3323 A C
ATOM 2873 CG LEU A 366 -13.084 38.009 17.402 1.00 74.37 A C
ANISOU 2873 CG LEU A 366 9923 2613 15722 1323 7852 2753 A C
ATOM 2874 CD1 LEU A 366 -13.380 36.618 17.880 1.00 70.56 A C
ANISOU 2874 CD1 LEU A 366 9351 2567 14891 1214 7250 2578 A C
ATOM 2875 CD2 LEU A 366 -11.611 38.341 17.640 1.00 75.79 A C
ANISOU 2875 CD2 LEU A 366 10168 2503 16126 1007 8022 2267 A C
ATOM 2876 N HIS A 367 -14.417 40.707 13.364 1.00 85.39 A N
ANISOU 2876 N HIS A 367 11366 3785 17293 2520 9149 4705 A N
ATOM 2877 CA HIS A 367 -14.548 40.909 11.918 1.00 87.71 A C
ANISOU 2877 CA HIS A 367 11611 4273 17444 2834 9279 5241 A C
ATOM 2878 C HIS A 367 -13.164 41.244 11.366 1.00 91.72 A C
ANISOU 2878 C HIS A 367 12230 4472 18146 2631 9521 5048 A C
ATOM 2879 O HIS A 367 -12.517 42.167 11.859 1.00 91.43 A O
ANISOU 2879 O HIS A 367 12369 3872 18499 2487 10000 4813 A O
ATOM 2880 CB HIS A 367 -15.592 41.988 11.552 1.00 92.93 A C
ANISOU 2880 CB HIS A 367 12305 4807 18197 3331 9772 5852 A C
ATOM 2881 CG HIS A 367 -15.589 42.357 10.091 1.00100.04 A C
ANISOU 2881 CG HIS A 367 13177 5855 18979 3678 9995 6407 A C
ATOM 2882 CD2 HIS A 367 -15.633 41.562 8.992 1.00101.04 A C
ANISOU 2882 CD2 HIS A 367 13125 6547 18719 3768 9622 6640 A C
ATOM 2883 ND1 HIS A 367 -15.521 43.681 9.672 1.00106.98 A N
ANISOU 2883 ND1 HIS A 367 14233 6263 20152 3976 10696 6775 A N
ATOM 2884 CE1 HIS A 367 -15.520 43.643 8.346 1.00107.89 A C
ANISOU 2884 CE1 HIS A 367 14267 6686 20040 4254 10713 7234 A C
ATOM 2885 NE2 HIS A 367 -15.579 42.393 7.892 1.00104.77 A N
ANISOU 2885 NE2 HIS A 367 13650 6928 19231 4130 10070 7157 A N
ATOM 2886 N GLU A 368 -12.689 40.421 10.414 1.00 88.36 A N
ANISOU 2886 N GLU A 368 11698 4432 17443 2573 9170 5084 A N
ATOM 2887 CA GLU A 368 -11.379 40.488 9.750 1.00 88.25 A C
ANISOU 2887 CA GLU A 368 11745 4260 17526 2372 9284 4904 A C
ATOM 2888 C GLU A 368 -10.235 40.365 10.793 1.00 89.75 A C
ANISOU 2888 C GLU A 368 12009 4147 17946 1897 9240 4193 A C
ATOM 2889 O GLU A 368 -9.231 41.068 10.696 1.00 91.86 A O
ANISOU 2889 O GLU A 368 12390 4012 18501 1725 9633 3990 A O
ATOM 2890 CB GLU A 368 -11.240 41.765 8.879 1.00 94.81 A C
ANISOU 2890 CB GLU A 368 12714 4714 18598 2648 9956 5338 A C
ATOM 2891 CG GLU A 368 -12.081 41.768 7.607 1.00108.52 A C
ANISOU 2891 CG GLU A 368 14343 6853 20037 3115 9958 6031 A C
ATOM 2892 CD GLU A 368 -11.652 40.818 6.500 1.00130.83 A C
ANISOU 2892 CD GLU A 368 17024 10175 22509 3071 9549 6095 A C
ATOM 2893 OE1 GLU A 368 -10.429 40.659 6.279 1.00128.68 A O
ANISOU 2893 OE1 GLU A 368 16810 9742 22339 2774 9552 5762 A O
ATOM 2894 OE2 GLU A 368 -12.551 40.248 5.840 1.00125.19 A O1-
ANISOU 2894 OE2 GLU A 368 16128 10029 21409 3334 9243 6475 A O1-
ATOM 2895 N VAL A 369 -10.386 39.441 11.778 1.00 82.57 A N
ANISOU 2895 N VAL A 369 11022 3466 16886 1687 8760 3812 A N
ATOM 2896 CA VAL A 369 -9.386 39.214 12.834 1.00 80.63 A C
ANISOU 2896 CA VAL A 369 10805 3045 16784 1275 8653 3147 A C
ATOM 2897 C VAL A 369 -8.978 37.721 12.889 1.00 81.08 A C
ANISOU 2897 C VAL A 369 10740 3573 16494 1081 7992 2856 A C
ATOM 2898 O VAL A 369 -9.840 36.845 13.021 1.00 79.11 A O
ANISOU 2898 O VAL A 369 10409 3701 15949 1184 7580 2993 A O
ATOM 2899 CB VAL A 369 -9.882 39.715 14.226 1.00 85.10 A C
ANISOU 2899 CB VAL A 369 11435 3343 17557 1210 8813 2915 A C
ATOM 2900 CG1 VAL A 369 -8.881 39.378 15.330 1.00 83.10 A C
ANISOU 2900 CG1 VAL A 369 11172 3019 17383 799 8647 2221 A C
ATOM 2901 CG2 VAL A 369 -10.179 41.225 14.215 1.00 89.25 A C
ANISOU 2901 CG2 VAL A 369 12115 3335 18461 1381 9529 3157 A C
ATOM 2902 N ASP A 370 -7.657 37.455 12.815 1.00 76.47 A N
ANISOU 2902 N ASP A 370 10149 2952 15953 798 7923 2445 A N
ATOM 2903 CA ASP A 370 -7.041 36.131 12.919 1.00 72.93 A C
ANISOU 2903 CA ASP A 370 9612 2876 15220 608 7373 2117 A C
ATOM 2904 C ASP A 370 -7.152 35.688 14.387 1.00 74.13 A C
ANISOU 2904 C ASP A 370 9757 3059 15350 443 7130 1702 A C
ATOM 2905 O ASP A 370 -6.500 36.266 15.253 1.00 73.51 A O
ANISOU 2905 O ASP A 370 9707 2710 15514 234 7352 1297 A O
ATOM 2906 CB ASP A 370 -5.563 36.194 12.428 1.00 75.72 A C
ANISOU 2906 CB ASP A 370 9953 3149 15666 387 7467 1819 A C
ATOM 2907 CG ASP A 370 -4.913 34.863 12.032 1.00 86.74 A C
ANISOU 2907 CG ASP A 370 11264 4953 16741 291 6960 1652 A C
ATOM 2908 OD1 ASP A 370 -5.300 33.813 12.601 1.00 83.45 A O
ANISOU 2908 OD1 ASP A 370 10814 4823 16072 275 6512 1528 A O
ATOM 2909 OD2 ASP A 370 -3.981 34.882 11.190 1.00 94.91 A O1-
ANISOU 2909 OD2 ASP A 370 12278 5994 17790 221 7040 1617 A O1-
ATOM 2910 N VAL A 371 -8.012 34.694 14.664 1.00 70.67 A N
ANISOU 2910 N VAL A 371 9278 2957 14616 532 6699 1803 A N
ATOM 2911 CA VAL A 371 -8.318 34.203 16.022 1.00 69.05 A C
ANISOU 2911 CA VAL A 371 9077 2815 14345 427 6453 1492 A C
ATOM 2912 C VAL A 371 -7.076 33.679 16.781 1.00 69.10 A C
ANISOU 2912 C VAL A 371 9060 2865 14328 152 6255 915 A C
ATOM 2913 O VAL A 371 -6.988 33.881 17.996 1.00 67.74 A O
ANISOU 2913 O VAL A 371 8898 2588 14253 30 6283 579 A O
ATOM 2914 CB VAL A 371 -9.469 33.167 16.075 1.00 71.71 A C
ANISOU 2914 CB VAL A 371 9383 3515 14350 561 6043 1722 A C
ATOM 2915 CG1 VAL A 371 -10.797 33.810 15.703 1.00 73.43 A C
ANISOU 2915 CG1 VAL A 371 9589 3705 14605 827 6260 2212 A C
ATOM 2916 CG2 VAL A 371 -9.194 31.954 15.191 1.00 70.35 A C
ANISOU 2916 CG2 VAL A 371 9166 3709 13855 555 5664 1795 A C
ATOM 2917 N ASP A 372 -6.133 33.026 16.083 1.00 65.12 A N
ANISOU 2917 N ASP A 372 8515 2542 13685 72 6063 803 A N
ATOM 2918 CA ASP A 372 -4.913 32.491 16.707 1.00 65.44 A C
ANISOU 2918 CA ASP A 372 8508 2688 13669 -144 5868 286 A C
ATOM 2919 C ASP A 372 -4.008 33.627 17.200 1.00 74.84 A C
ANISOU 2919 C ASP A 372 9671 3575 15189 -348 6275 -79 A C
ATOM 2920 O ASP A 372 -3.383 33.501 18.260 1.00 74.89 A O
ANISOU 2920 O ASP A 372 9622 3640 15192 -522 6185 -546 A O
ATOM 2921 CB ASP A 372 -4.155 31.582 15.724 1.00 66.53 A C
ANISOU 2921 CB ASP A 372 8609 3088 13583 -151 5602 297 A C
ATOM 2922 CG ASP A 372 -5.029 30.538 15.053 1.00 79.05 A C
ANISOU 2922 CG ASP A 372 10223 4961 14851 14 5257 643 A C
ATOM 2923 OD1 ASP A 372 -5.820 29.870 15.770 1.00 76.02 A O
ANISOU 2923 OD1 ASP A 372 9874 4710 14299 54 5004 636 A O
ATOM 2924 OD2 ASP A 372 -4.951 30.411 13.809 1.00 90.33 A O1-
ANISOU 2924 OD2 ASP A 372 11637 6487 16197 90 5261 914 A O1-
ATOM 2925 N ALA A 373 -3.989 34.747 16.447 1.00 74.75 A N
ANISOU 2925 N ALA A 373 9699 3250 15452 -323 6743 138 A N
ATOM 2926 CA ALA A 373 -3.229 35.950 16.750 1.00 78.26 A C
ANISOU 2926 CA ALA A 373 10147 3341 16249 -531 7233 -163 A C
ATOM 2927 C ALA A 373 -3.973 36.850 17.745 1.00 86.69 A C
ANISOU 2927 C ALA A 373 11286 4098 17556 -536 7556 -202 A C
ATOM 2928 O ALA A 373 -3.386 37.813 18.253 1.00 90.21 A O
ANISOU 2928 O ALA A 373 11739 4242 18294 -752 7969 -536 A O
ATOM 2929 CB ALA A 373 -2.941 36.715 15.467 1.00 81.21 A C
ANISOU 2929 CB ALA A 373 10565 3488 16803 -483 7624 124 A C
ATOM 2930 N ALA A 374 -5.258 36.533 18.021 1.00 81.47 A N
ANISOU 2930 N ALA A 374 10672 3517 16766 -313 7381 119 A N
ATOM 2931 CA ALA A 374 -6.135 37.280 18.923 1.00 82.44 A C
ANISOU 2931 CA ALA A 374 10864 3382 17076 -267 7644 145 A C
ATOM 2932 C ALA A 374 -6.281 36.610 20.310 1.00 83.35 A C
ANISOU 2932 C ALA A 374 10932 3707 17032 -373 7299 -226 A C
ATOM 2933 O ALA A 374 -6.958 37.165 21.178 1.00 84.24 A O
ANISOU 2933 O ALA A 374 11091 3629 17285 -366 7493 -276 A O
ATOM 2934 CB ALA A 374 -7.506 37.437 18.283 1.00 83.48 A C
ANISOU 2934 CB ALA A 374 11061 3492 17166 74 7708 771 A C
ATOM 2935 N PHE A 375 -5.641 35.436 20.521 1.00 76.37 A N
ANISOU 2935 N PHE A 375 9963 3205 15851 -454 6814 -475 A N
ATOM 2936 CA PHE A 375 -5.699 34.667 21.774 1.00 73.37 A C
ANISOU 2936 CA PHE A 375 9541 3069 15266 -521 6459 -801 A C
ATOM 2937 C PHE A 375 -5.053 35.439 22.946 1.00 75.92 A C
ANISOU 2937 C PHE A 375 9812 3244 15791 -773 6714 -1341 A C
ATOM 2938 O PHE A 375 -3.963 36.002 22.794 1.00 77.91 A O
ANISOU 2938 O PHE A 375 9996 3402 16204 -984 6953 -1658 A O
ATOM 2939 CB PHE A 375 -5.039 33.287 21.587 1.00 72.61 A C
ANISOU 2939 CB PHE A 375 9385 3381 14821 -523 5956 -922 A C
ATOM 2940 CG PHE A 375 -5.051 32.390 22.808 1.00 72.71 A C
ANISOU 2940 CG PHE A 375 9374 3666 14587 -546 5589 -1215 A C
ATOM 2941 CD1 PHE A 375 -6.212 31.725 23.193 1.00 74.30 A C
ANISOU 2941 CD1 PHE A 375 9653 3974 14604 -388 5348 -973 A C
ATOM 2942 CD2 PHE A 375 -3.901 32.207 23.569 1.00 75.29 A C
ANISOU 2942 CD2 PHE A 375 9590 4168 14849 -718 5497 -1731 A C
ATOM 2943 CE1 PHE A 375 -6.224 30.908 24.332 1.00 74.05 A C
ANISOU 2943 CE1 PHE A 375 9621 4172 14344 -396 5043 -1225 A C
ATOM 2944 CE2 PHE A 375 -3.910 31.380 24.700 1.00 76.92 A C
ANISOU 2944 CE2 PHE A 375 9776 4646 14802 -697 5172 -1971 A C
ATOM 2945 CZ PHE A 375 -5.068 30.727 25.066 1.00 73.47 A C
ANISOU 2945 CZ PHE A 375 9449 4268 14196 -533 4954 -1706 A C
ATOM 2946 N SER A 376 -5.754 35.470 24.106 1.00 68.35 A N
ANISOU 2946 N SER A 376 8875 2282 14814 -765 6674 -1455 A N
ATOM 2947 CA SER A 376 -5.345 36.174 25.328 1.00 69.08 A C
ANISOU 2947 CA SER A 376 8914 2267 15065 -996 6904 -1963 A C
ATOM 2948 C SER A 376 -6.003 35.588 26.582 1.00 71.94 A C
ANISOU 2948 C SER A 376 9276 2833 15226 -944 6617 -2084 A C
ATOM 2949 O SER A 376 -6.869 34.718 26.472 1.00 68.70 A O
ANISOU 2949 O SER A 376 8926 2590 14587 -731 6289 -1744 A O
ATOM 2950 CB SER A 376 -5.704 37.654 25.223 1.00 72.95 A C
ANISOU 2950 CB SER A 376 9495 2255 15969 -1050 7526 -1888 A C
ATOM 2951 OG SER A 376 -7.099 37.823 25.032 1.00 75.11 A O
ANISOU 2951 OG SER A 376 9890 2364 16285 -782 7604 -1382 A O
ATOM 2952 N SER A 377 -5.613 36.102 27.772 1.00 71.10 A N
ANISOU 2952 N SER A 377 9099 2712 15204 -1155 6771 -2579 A N
ATOM 2953 CA SER A 377 -6.161 35.699 29.071 1.00 70.01 A C
ANISOU 2953 CA SER A 377 8953 2752 14894 -1129 6560 -2749 A C
ATOM 2954 C SER A 377 -7.439 36.472 29.411 1.00 73.93 A C
ANISOU 2954 C SER A 377 9573 2908 15608 -1036 6866 -2502 A C
ATOM 2955 O SER A 377 -8.033 36.232 30.463 1.00 73.10 A O
ANISOU 2955 O SER A 377 9477 2909 15389 -1006 6737 -2602 A O
ATOM 2956 CB SER A 377 -5.133 35.908 30.177 1.00 75.85 A C
ANISOU 2956 CB SER A 377 9533 3693 15594 -1396 6583 -3409 A C
ATOM 2957 OG SER A 377 -3.912 35.246 29.896 1.00 86.60 A O
ANISOU 2957 OG SER A 377 10756 5402 16747 -1464 6318 -3649 A O
ATOM 2958 N VAL A 378 -7.847 37.422 28.533 1.00 72.09 A N
ANISOU 2958 N VAL A 378 9435 2271 15683 -972 7291 -2175 A N
ATOM 2959 CA VAL A 378 -9.052 38.242 28.705 1.00 72.41 A C
ANISOU 2959 CA VAL A 378 9597 1966 15950 -835 7638 -1883 A C
ATOM 2960 C VAL A 378 -10.318 37.332 28.809 1.00 72.33 A C
ANISOU 2960 C VAL A 378 9629 2175 15679 -559 7259 -1467 A C
ATOM 2961 O VAL A 378 -10.996 37.448 29.824 1.00 71.69 A O
ANISOU 2961 O VAL A 378 9570 2076 15594 -547 7279 -1558 A O
ATOM 2962 CB VAL A 378 -9.214 39.327 27.612 1.00 78.50 A C
ANISOU 2962 CB VAL A 378 10469 2299 17060 -754 8157 -1543 A C
ATOM 2963 CG1 VAL A 378 -10.535 40.082 27.777 1.00 79.83 A C
ANISOU 2963 CG1 VAL A 378 10760 2153 17420 -538 8491 -1180 A C
ATOM 2964 CG2 VAL A 378 -8.031 40.295 27.619 1.00 81.62 A C
ANISOU 2964 CG2 VAL A 378 10843 2427 17742 -1066 8604 -1990 A C
ATOM 2965 N PRO A 379 -10.651 36.412 27.849 1.00 65.44 A N
ANISOU 2965 N PRO A 379 8760 1528 14577 -364 6920 -1055 A N
ATOM 2966 CA PRO A 379 -11.872 35.607 28.020 1.00 63.73 A C
ANISOU 2966 CA PRO A 379 8573 1518 14122 -156 6607 -719 A C
ATOM 2967 C PRO A 379 -11.851 34.730 29.281 1.00 64.87 A C
ANISOU 2967 C PRO A 379 8693 1946 14007 -236 6245 -1045 A C
ATOM 2968 O PRO A 379 -12.896 34.492 29.892 1.00 64.02 A O
ANISOU 2968 O PRO A 379 8622 1891 13811 -131 6156 -906 A O
ATOM 2969 CB PRO A 379 -11.925 34.756 26.751 1.00 64.08 A C
ANISOU 2969 CB PRO A 379 8606 1782 13958 -17 6322 -347 A C
ATOM 2970 CG PRO A 379 -10.561 34.831 26.152 1.00 68.20 A C
ANISOU 2970 CG PRO A 379 9083 2299 14528 -172 6353 -585 A C
ATOM 2971 CD PRO A 379 -9.986 36.114 26.560 1.00 66.01 A C
ANISOU 2971 CD PRO A 379 8809 1671 14600 -340 6838 -882 A C
ATOM 2972 N TYR A 380 -10.649 34.296 29.676 1.00 60.07 A N
ANISOU 2972 N TYR A 380 8018 1530 13277 -411 6064 -1477 A N
ATOM 2973 CA TYR A 380 -10.351 33.488 30.851 1.00 58.19 A C
ANISOU 2973 CA TYR A 380 7743 1594 12771 -476 5739 -1826 A C
ATOM 2974 C TYR A 380 -10.613 34.265 32.151 1.00 62.64 A C
ANISOU 2974 C TYR A 380 8293 2035 13471 -584 5976 -2143 A C
ATOM 2975 O TYR A 380 -11.505 33.907 32.911 1.00 61.36 A O
ANISOU 2975 O TYR A 380 8179 1951 13182 -491 5845 -2058 A O
ATOM 2976 CB TYR A 380 -8.862 33.064 30.800 1.00 59.06 A C
ANISOU 2976 CB TYR A 380 7750 1937 12752 -617 5571 -2207 A C
ATOM 2977 CG TYR A 380 -8.522 32.039 29.741 1.00 59.50 A C
ANISOU 2977 CG TYR A 380 7823 2191 12594 -510 5256 -1968 A C
ATOM 2978 CD1 TYR A 380 -8.600 32.350 28.384 1.00 61.44 A C
ANISOU 2978 CD1 TYR A 380 8095 2266 12985 -455 5400 -1628 A C
ATOM 2979 CD2 TYR A 380 -8.073 30.768 30.094 1.00 58.50 A C
ANISOU 2979 CD2 TYR A 380 7689 2423 12114 -457 4838 -2093 A C
ATOM 2980 CE1 TYR A 380 -8.282 31.406 27.405 1.00 60.28 A C
ANISOU 2980 CE1 TYR A 380 7959 2310 12633 -372 5120 -1433 A C
ATOM 2981 CE2 TYR A 380 -7.779 29.812 29.127 1.00 57.28 A C
ANISOU 2981 CE2 TYR A 380 7570 2426 11769 -363 4577 -1885 A C
ATOM 2982 CZ TYR A 380 -7.867 30.140 27.782 1.00 65.25 A C
ANISOU 2982 CZ TYR A 380 8593 3270 12927 -336 4714 -1572 A C
ATOM 2983 OH TYR A 380 -7.564 29.212 26.816 1.00 66.63 A O
ANISOU 2983 OH TYR A 380 8799 3609 12910 -259 4468 -1391 A O
ATOM 2984 N GLU A 381 -9.815 35.315 32.410 1.00 60.88 A N
ANISOU 2984 N GLU A 381 8004 1625 13503 -801 6339 -2528 A N
ATOM 2985 CA GLU A 381 -9.791 36.063 33.662 1.00 62.27 A C
ANISOU 2985 CA GLU A 381 8142 1720 13799 -969 6580 -2949 A C
ATOM 2986 C GLU A 381 -10.805 37.201 33.777 1.00 65.18 A C
ANISOU 2986 C GLU A 381 8614 1654 14499 -929 7043 -2763 A C
ATOM 2987 O GLU A 381 -11.252 37.464 34.901 1.00 65.34 A O
ANISOU 2987 O GLU A 381 8637 1666 14522 -976 7119 -2971 A O
ATOM 2988 CB GLU A 381 -8.376 36.589 33.924 1.00 66.40 A C
ANISOU 2988 CB GLU A 381 8522 2300 14406 -1265 6751 -3522 A C
ATOM 2989 CG GLU A 381 -7.303 35.500 33.934 1.00 72.54 A C
ANISOU 2989 CG GLU A 381 9170 3552 14838 -1286 6308 -3750 A C
ATOM 2990 CD GLU A 381 -7.534 34.290 34.822 1.00 85.34 A C
ANISOU 2990 CD GLU A 381 10781 5594 16052 -1140 5831 -3779 A C
ATOM 2991 OE1 GLU A 381 -8.228 34.418 35.858 1.00 93.25 A O
ANISOU 2991 OE1 GLU A 381 11811 6602 17017 -1126 5854 -3862 A O
ATOM 2992 OE2 GLU A 381 -7.014 33.204 34.477 1.00 71.28 A O1-
ANISOU 2992 OE2 GLU A 381 8973 4126 13984 -1033 5453 -3716 A O1-
ATOM 2993 N LYS A 382 -11.180 37.869 32.662 1.00 61.48 A N
ANISOU 2993 N LYS A 382 8204 889 14268 -828 7357 -2350 A N
ATOM 2994 CA LYS A 382 -12.221 38.906 32.727 1.00 63.72 A C
ANISOU 2994 CA LYS A 382 8584 794 14832 -721 7803 -2095 A C
ATOM 2995 C LYS A 382 -13.579 38.200 32.820 1.00 64.94 A C
ANISOU 2995 C LYS A 382 8820 1036 14817 -433 7518 -1677 A C
ATOM 2996 O LYS A 382 -14.482 38.673 33.495 1.00 64.74 A O
ANISOU 2996 O LYS A 382 8845 863 14892 -362 7709 -1624 A O
ATOM 2997 CB LYS A 382 -12.163 39.887 31.539 1.00 66.82 A C
ANISOU 2997 CB LYS A 382 9089 718 15583 -645 8268 -1817 A C
ATOM 2998 CG LYS A 382 -13.141 41.059 31.686 1.00 69.41 A C
ANISOU 2998 CG LYS A 382 9523 634 16217 -520 8805 -1582 A C
ATOM 2999 CD LYS A 382 -13.273 41.911 30.420 1.00 76.98 A C
ANISOU 2999 CD LYS A 382 10608 1167 17476 -348 9246 -1165 A C
ATOM 3000 CE LYS A 382 -12.197 42.963 30.310 1.00 79.40 A C
ANISOU 3000 CE LYS A 382 10960 1092 18116 -625 9770 -1537 A C
ATOM 3001 NZ LYS A 382 -12.489 43.965 29.249 1.00 88.07 A N1+
ANISOU 3001 NZ LYS A 382 12207 1726 19531 -426 10326 -1096 A N1+
ATOM 3002 N GLY A 383 -13.674 37.053 32.159 1.00 61.06 A N
ANISOU 3002 N GLY A 383 8305 860 14035 -301 7070 -1400 A N
ATOM 3003 CA GLY A 383 -14.838 36.174 32.177 1.00 58.23 A C
ANISOU 3003 CA GLY A 383 7968 728 13428 -88 6743 -1029 A C
ATOM 3004 C GLY A 383 -15.037 35.596 33.557 1.00 59.80 A C
ANISOU 3004 C GLY A 383 8158 1144 13420 -160 6503 -1330 A C
ATOM 3005 O GLY A 383 -16.154 35.595 34.061 1.00 57.77 A O
ANISOU 3005 O GLY A 383 7935 875 13139 -42 6518 -1152 A O
ATOM 3006 N PHE A 384 -13.942 35.119 34.183 1.00 57.18 A N
ANISOU 3006 N PHE A 384 7768 1029 12928 -342 6293 -1787 A N
ATOM 3007 CA PHE A 384 -13.977 34.581 35.540 1.00 56.15 A C
ANISOU 3007 CA PHE A 384 7621 1141 12573 -400 6072 -2103 A C
ATOM 3008 C PHE A 384 -14.351 35.672 36.551 1.00 62.39 A C
ANISOU 3008 C PHE A 384 8414 1697 13593 -494 6449 -2349 A C
ATOM 3009 O PHE A 384 -15.183 35.423 37.430 1.00 62.24 A O
ANISOU 3009 O PHE A 384 8427 1763 13457 -427 6360 -2326 A O
ATOM 3010 CB PHE A 384 -12.639 33.928 35.935 1.00 57.05 A C
ANISOU 3010 CB PHE A 384 7647 1571 12459 -541 5803 -2534 A C
ATOM 3011 CG PHE A 384 -12.542 33.685 37.427 1.00 58.88 A C
ANISOU 3011 CG PHE A 384 7838 2034 12501 -612 5684 -2925 A C
ATOM 3012 CD1 PHE A 384 -13.181 32.598 38.015 1.00 58.66 A C
ANISOU 3012 CD1 PHE A 384 7875 2261 12153 -467 5336 -2786 A C
ATOM 3013 CD2 PHE A 384 -11.912 34.606 38.259 1.00 63.32 A C
ANISOU 3013 CD2 PHE A 384 8303 2544 13213 -829 5963 -3425 A C
ATOM 3014 CE1 PHE A 384 -13.135 32.402 39.400 1.00 60.10 A C
ANISOU 3014 CE1 PHE A 384 8025 2663 12148 -507 5245 -3119 A C
ATOM 3015 CE2 PHE A 384 -11.869 34.410 39.638 1.00 66.58 A C
ANISOU 3015 CE2 PHE A 384 8661 3207 13428 -885 5858 -3782 A C
ATOM 3016 CZ PHE A 384 -12.474 33.311 40.201 1.00 62.37 A C
ANISOU 3016 CZ PHE A 384 8195 2941 12563 -708 5494 -3613 A C
ATOM 3017 N ALA A 385 -13.694 36.855 36.458 1.00 61.35 A N
ANISOU 3017 N ALA A 385 8255 1274 13782 -669 6883 -2617 A N
ATOM 3018 CA ALA A 385 -13.895 38.007 37.353 1.00 63.25 A C
ANISOU 3018 CA ALA A 385 8508 1241 14284 -805 7322 -2915 A C
ATOM 3019 C ALA A 385 -15.361 38.425 37.415 1.00 67.44 A C
ANISOU 3019 C ALA A 385 9143 1529 14952 -593 7525 -2510 A C
ATOM 3020 O ALA A 385 -15.860 38.739 38.496 1.00 66.79 A O
ANISOU 3020 O ALA A 385 9073 1416 14889 -633 7640 -2705 A O
ATOM 3021 CB ALA A 385 -13.039 39.193 36.906 1.00 67.02 A C
ANISOU 3021 CB ALA A 385 8974 1375 15115 -1014 7809 -3167 A C
ATOM 3022 N LEU A 386 -16.054 38.395 36.267 1.00 63.63 A N
ANISOU 3022 N LEU A 386 8717 923 14536 -357 7553 -1949 A N
ATOM 3023 CA LEU A 386 -17.463 38.736 36.181 1.00 64.09 A C
ANISOU 3023 CA LEU A 386 8842 820 14690 -111 7721 -1508 A C
ATOM 3024 C LEU A 386 -18.292 37.726 36.961 1.00 67.71 A C
ANISOU 3024 C LEU A 386 9284 1614 14828 -24 7318 -1438 A C
ATOM 3025 O LEU A 386 -19.171 38.124 37.714 1.00 68.95 A O
ANISOU 3025 O LEU A 386 9470 1674 15053 39 7485 -1418 A O
ATOM 3026 CB LEU A 386 -17.888 38.792 34.704 1.00 63.86 A C
ANISOU 3026 CB LEU A 386 8833 706 14727 126 7776 -938 A C
ATOM 3027 CG LEU A 386 -19.378 38.921 34.367 1.00 69.07 A C
ANISOU 3027 CG LEU A 386 9512 1329 15404 437 7866 -394 A C
ATOM 3028 CD1 LEU A 386 -19.997 40.209 34.929 1.00 73.19 A C
ANISOU 3028 CD1 LEU A 386 10108 1440 16259 503 8423 -404 A C
ATOM 3029 CD2 LEU A 386 -19.581 38.828 32.875 1.00 70.89 A C
ANISOU 3029 CD2 LEU A 386 9720 1595 15619 650 7845 114 A C
ATOM 3030 N LEU A 387 -17.986 36.425 36.807 1.00 61.67 A N
ANISOU 3030 N LEU A 387 8484 1228 13718 -26 6815 -1415 A N
ATOM 3031 CA LEU A 387 -18.707 35.349 37.481 1.00 59.04 A C
ANISOU 3031 CA LEU A 387 8161 1210 13062 46 6434 -1340 A C
ATOM 3032 C LEU A 387 -18.409 35.329 38.981 1.00 62.99 A C
ANISOU 3032 C LEU A 387 8652 1816 13466 -105 6400 -1821 A C
ATOM 3033 O LEU A 387 -19.301 35.046 39.777 1.00 61.50 A O
ANISOU 3033 O LEU A 387 8491 1720 13158 -37 6323 -1764 A O
ATOM 3034 CB LEU A 387 -18.376 34.004 36.835 1.00 56.33 A C
ANISOU 3034 CB LEU A 387 7814 1188 12400 79 5972 -1196 A C
ATOM 3035 CG LEU A 387 -18.740 33.860 35.344 1.00 59.99 A C
ANISOU 3035 CG LEU A 387 8270 1632 12890 224 5947 -721 A C
ATOM 3036 CD1 LEU A 387 -18.109 32.627 34.753 1.00 55.85 A C
ANISOU 3036 CD1 LEU A 387 7751 1390 12080 197 5539 -701 A C
ATOM 3037 CD2 LEU A 387 -20.256 33.829 35.139 1.00 63.23 A C
ANISOU 3037 CD2 LEU A 387 8677 2067 13279 420 5979 -275 A C
ATOM 3038 N PHE A 388 -17.186 35.686 39.367 1.00 61.45 A N
ANISOU 3038 N PHE A 388 8403 1624 13322 -313 6482 -2298 A N
ATOM 3039 CA PHE A 388 -16.791 35.741 40.766 1.00 62.48 A C
ANISOU 3039 CA PHE A 388 8489 1907 13342 -468 6465 -2796 A C
ATOM 3040 C PHE A 388 -17.366 37.006 41.431 1.00 70.37 A C
ANISOU 3040 C PHE A 388 9511 2581 14644 -528 6937 -2937 A C
ATOM 3041 O PHE A 388 -17.757 36.950 42.597 1.00 71.17 A O
ANISOU 3041 O PHE A 388 9609 2800 14632 -557 6909 -3144 A O
ATOM 3042 CB PHE A 388 -15.272 35.670 40.873 1.00 64.82 A C
ANISOU 3042 CB PHE A 388 8681 2385 13563 -671 6388 -3265 A C
ATOM 3043 CG PHE A 388 -14.715 35.590 42.270 1.00 67.71 A C
ANISOU 3043 CG PHE A 388 8957 3034 13734 -821 6308 -3800 A C
ATOM 3044 CD1 PHE A 388 -15.033 34.522 43.104 1.00 69.51 A C
ANISOU 3044 CD1 PHE A 388 9204 3619 13588 -706 5931 -3785 A C
ATOM 3045 CD2 PHE A 388 -13.810 36.541 42.728 1.00 73.32 A C
ANISOU 3045 CD2 PHE A 388 9555 3691 14610 -1084 6607 -4333 A C
ATOM 3046 CE1 PHE A 388 -14.492 34.430 44.389 1.00 71.80 A C
ANISOU 3046 CE1 PHE A 388 9397 4224 13660 -814 5850 -4265 A C
ATOM 3047 CE2 PHE A 388 -13.258 36.444 44.005 1.00 77.84 A C
ANISOU 3047 CE2 PHE A 388 10008 4606 14960 -1225 6515 -4849 A C
ATOM 3048 CZ PHE A 388 -13.605 35.389 44.830 1.00 74.31 A C
ANISOU 3048 CZ PHE A 388 9575 4533 14127 -1070 6129 -4798 A C
ATOM 3049 N TYR A 389 -17.479 38.118 40.679 1.00 67.93 A N
ANISOU 3049 N TYR A 389 9242 1856 14714 -524 7386 -2797 A N
ATOM 3050 CA TYR A 389 -18.100 39.340 41.178 1.00 70.31 A C
ANISOU 3050 CA TYR A 389 9599 1785 15332 -544 7890 -2869 A C
ATOM 3051 C TYR A 389 -19.630 39.108 41.348 1.00 73.30 A C
ANISOU 3051 C TYR A 389 10035 2158 15656 -279 7842 -2418 A C
ATOM 3052 O TYR A 389 -20.191 39.519 42.367 1.00 72.54 A O
ANISOU 3052 O TYR A 389 9961 1988 15614 -300 8023 -2579 A O
ATOM 3053 CB TYR A 389 -17.771 40.542 40.265 1.00 73.85 A C
ANISOU 3053 CB TYR A 389 10099 1767 16193 -587 8416 -2815 A C
ATOM 3054 CG TYR A 389 -18.715 41.725 40.340 1.00 77.80 A C
ANISOU 3054 CG TYR A 389 10709 1812 17041 -463 8961 -2618 A C
ATOM 3055 CD1 TYR A 389 -18.757 42.541 41.468 1.00 82.68 A C
ANISOU 3055 CD1 TYR A 389 11353 2248 17812 -626 9306 -3028 A C
ATOM 3056 CD2 TYR A 389 -19.485 42.087 39.247 1.00 78.72 A C
ANISOU 3056 CD2 TYR A 389 10897 1682 17330 -177 9164 -2034 A C
ATOM 3057 CE1 TYR A 389 -19.608 43.649 41.526 1.00 87.26 A C
ANISOU 3057 CE1 TYR A 389 12052 2374 18728 -498 9853 -2848 A C
ATOM 3058 CE2 TYR A 389 -20.321 43.190 39.285 1.00 83.02 A C
ANISOU 3058 CE2 TYR A 389 11547 1809 18189 -18 9694 -1826 A C
ATOM 3059 CZ TYR A 389 -20.405 43.952 40.436 1.00 94.12 A C
ANISOU 3059 CZ TYR A 389 12999 3005 19757 -172 10039 -2226 A C
ATOM 3060 OH TYR A 389 -21.244 45.030 40.450 1.00100.62 A O
ANISOU 3060 OH TYR A 389 13943 3393 20896 10 10588 -2003 A O
ATOM 3061 N LEU A 390 -20.274 38.385 40.399 1.00 69.02 A N
ANISOU 3061 N LEU A 390 9501 1744 14979 -52 7580 -1891 A N
ATOM 3062 CA LEU A 390 -21.705 38.045 40.474 1.00 68.24 A C
ANISOU 3062 CA LEU A 390 9420 1725 14784 183 7490 -1468 A C
ATOM 3063 C LEU A 390 -21.988 37.157 41.687 1.00 69.78 A C
ANISOU 3063 C LEU A 390 9605 2246 14662 127 7153 -1674 A C
ATOM 3064 O LEU A 390 -22.955 37.402 42.401 1.00 70.43 A O
ANISOU 3064 O LEU A 390 9705 2290 14766 206 7273 -1611 A O
ATOM 3065 CB LEU A 390 -22.194 37.342 39.188 1.00 65.83 A C
ANISOU 3065 CB LEU A 390 9092 1571 14351 386 7248 -931 A C
ATOM 3066 CG LEU A 390 -22.407 38.233 37.954 1.00 71.36 A C
ANISOU 3066 CG LEU A 390 9799 1978 15336 561 7607 -546 A C
ATOM 3067 CD1 LEU A 390 -22.727 37.408 36.727 1.00 67.72 A C
ANISOU 3067 CD1 LEU A 390 9286 1765 14680 718 7302 -95 A C
ATOM 3068 CD2 LEU A 390 -23.500 39.278 38.189 1.00 74.49 A C
ANISOU 3068 CD2 LEU A 390 10224 2106 15974 757 8039 -316 A C
ATOM 3069 N GLU A 391 -21.101 36.171 41.943 1.00 63.68 A N
ANISOU 3069 N GLU A 391 8809 1787 13600 1 6762 -1928 A N
ATOM 3070 CA GLU A 391 -21.155 35.242 43.077 1.00 62.43 A C
ANISOU 3070 CA GLU A 391 8656 1960 13104 -42 6433 -2138 A C
ATOM 3071 C GLU A 391 -21.248 36.002 44.422 1.00 68.99 A C
ANISOU 3071 C GLU A 391 9478 2712 14023 -153 6690 -2534 A C
ATOM 3072 O GLU A 391 -22.098 35.676 45.246 1.00 66.97 A O
ANISOU 3072 O GLU A 391 9250 2572 13625 -86 6612 -2482 A O
ATOM 3073 CB GLU A 391 -19.916 34.325 43.055 1.00 62.05 A C
ANISOU 3073 CB GLU A 391 8581 2208 12787 -143 6077 -2387 A C
ATOM 3074 CG GLU A 391 -19.736 33.455 44.288 1.00 72.71 A C
ANISOU 3074 CG GLU A 391 9938 3904 13783 -174 5785 -2659 A C
ATOM 3075 CD GLU A 391 -18.304 33.058 44.584 1.00 92.69 A C
ANISOU 3075 CD GLU A 391 12401 6699 16118 -290 5587 -3060 A C
ATOM 3076 OE1 GLU A 391 -17.733 32.288 43.783 1.00 82.34 A O
ANISOU 3076 OE1 GLU A 391 11099 5507 14678 -245 5343 -2921 A O
ATOM 3077 OE2 GLU A 391 -17.752 33.507 45.615 1.00100.47 A O1-
ANISOU 3077 OE2 GLU A 391 13310 7802 17062 -421 5676 -3520 A O1-
ATOM 3078 N GLN A 392 -20.375 37.006 44.623 1.00 69.59 A N
ANISOU 3078 N GLN A 392 9514 2596 14333 -341 7011 -2941 A N
ATOM 3079 CA GLN A 392 -20.302 37.823 45.837 1.00 72.60 A C
ANISOU 3079 CA GLN A 392 9874 2895 14817 -500 7302 -3396 A C
ATOM 3080 C GLN A 392 -21.557 38.694 45.988 1.00 80.17 A C
ANISOU 3080 C GLN A 392 10903 3515 16045 -375 7690 -3158 A C
ATOM 3081 O GLN A 392 -22.070 38.876 47.102 1.00 81.44 A O
ANISOU 3081 O GLN A 392 11070 3717 16156 -402 7772 -3348 A O
ATOM 3082 CB GLN A 392 -19.037 38.702 45.805 1.00 76.13 A C
ANISOU 3082 CB GLN A 392 10255 3200 15472 -763 7591 -3882 A C
ATOM 3083 CG GLN A 392 -17.738 37.897 45.806 1.00 77.20 A C
ANISOU 3083 CG GLN A 392 10284 3727 15321 -890 7225 -4184 A C
ATOM 3084 CD GLN A 392 -16.494 38.727 45.571 1.00102.85 A C
ANISOU 3084 CD GLN A 392 13445 6854 18780 -1156 7507 -4623 A C
ATOM 3085 NE2 GLN A 392 -15.345 38.122 45.814 1.00 94.15 A N
ANISOU 3085 NE2 GLN A 392 12212 6150 17410 -1279 7213 -4968 A N
ATOM 3086 OE1 GLN A 392 -16.536 39.901 45.172 1.00102.81 A O
ANISOU 3086 OE1 GLN A 392 13487 6406 19170 -1250 8003 -4657 A O
ATOM 3087 N LEU A 393 -22.067 39.194 44.851 1.00 76.35 A N
ANISOU 3087 N LEU A 393 10466 2724 15821 -211 7921 -2722 A N
ATOM 3088 CA LEU A 393 -23.257 40.038 44.758 1.00 77.04 A C
ANISOU 3088 CA LEU A 393 10614 2486 16173 -24 8313 -2405 A C
ATOM 3089 C LEU A 393 -24.556 39.279 44.987 1.00 75.81 A C
ANISOU 3089 C LEU A 393 10451 2558 15794 195 8053 -2017 A C
ATOM 3090 O LEU A 393 -25.505 39.878 45.481 1.00 74.62 A O
ANISOU 3090 O LEU A 393 10327 2247 15779 305 8329 -1921 A O
ATOM 3091 CB LEU A 393 -23.300 40.644 43.346 1.00 78.43 A C
ANISOU 3091 CB LEU A 393 10823 2346 16629 125 8588 -2014 A C
ATOM 3092 CG LEU A 393 -23.434 42.152 43.214 1.00 88.81 A C
ANISOU 3092 CG LEU A 393 12225 3135 18385 158 9254 -2024 A C
ATOM 3093 CD1 LEU A 393 -22.293 42.895 43.908 1.00 91.99 A C
ANISOU 3093 CD1 LEU A 393 12647 3335 18969 -187 9566 -2670 A C
ATOM 3094 CD2 LEU A 393 -23.467 42.538 41.763 1.00 92.58 A C
ANISOU 3094 CD2 LEU A 393 12737 3375 19063 373 9460 -1540 A C
ATOM 3095 N LEU A 394 -24.627 37.979 44.600 1.00 69.02 A N
ANISOU 3095 N LEU A 394 9560 2060 14603 255 7554 -1794 A N
ATOM 3096 CA LEU A 394 -25.887 37.233 44.641 1.00 67.52 A C
ANISOU 3096 CA LEU A 394 9359 2088 14207 438 7326 -1405 A C
ATOM 3097 C LEU A 394 -26.073 36.270 45.836 1.00 75.17 A C
ANISOU 3097 C LEU A 394 10341 3384 14835 358 7001 -1620 A C
ATOM 3098 O LEU A 394 -27.111 35.598 45.909 1.00 74.41 A O
ANISOU 3098 O LEU A 394 10242 3469 14562 478 6827 -1327 A O
ATOM 3099 CB LEU A 394 -26.099 36.476 43.323 1.00 64.53 A C
ANISOU 3099 CB LEU A 394 8947 1868 13702 568 7056 -958 A C
ATOM 3100 CG LEU A 394 -26.229 37.349 42.066 1.00 69.26 A C
ANISOU 3100 CG LEU A 394 9524 2201 14593 732 7368 -605 A C
ATOM 3101 CD1 LEU A 394 -25.818 36.589 40.832 1.00 66.38 A C
ANISOU 3101 CD1 LEU A 394 9124 2012 14085 763 7076 -352 A C
ATOM 3102 CD2 LEU A 394 -27.631 37.940 41.912 1.00 70.57 A C
ANISOU 3102 CD2 LEU A 394 9651 2282 14880 987 7624 -206 A C
ATOM 3103 N GLY A 395 -25.128 36.237 46.775 1.00 74.02 A N
ANISOU 3103 N GLY A 395 10203 3328 14594 165 6947 -2120 A N
ATOM 3104 CA GLY A 395 -25.291 35.393 47.959 1.00 72.86 A C
ANISOU 3104 CA GLY A 395 10076 3492 14116 121 6678 -2316 A C
ATOM 3105 C GLY A 395 -24.282 34.302 48.260 1.00 72.88 A C
ANISOU 3105 C GLY A 395 10087 3837 13768 34 6273 -2541 A C
ATOM 3106 O GLY A 395 -24.512 33.518 49.179 1.00 72.57 A O
ANISOU 3106 O GLY A 395 10084 4059 13428 48 6049 -2616 A O
ATOM 3107 N GLY A 396 -23.177 34.247 47.525 1.00 67.35 A N
ANISOU 3107 N GLY A 396 9355 3140 13095 -37 6195 -2642 A N
ATOM 3108 CA GLY A 396 -22.134 33.255 47.770 1.00 65.58 A C
ANISOU 3108 CA GLY A 396 9127 3248 12540 -90 5833 -2858 A C
ATOM 3109 C GLY A 396 -21.960 32.165 46.724 1.00 67.18 A C
ANISOU 3109 C GLY A 396 9378 3574 12572 1 5508 -2530 A C
ATOM 3110 O GLY A 396 -22.697 32.126 45.731 1.00 64.93 A O
ANISOU 3110 O GLY A 396 9117 3148 12407 95 5537 -2115 A O
ATOM 3111 N PRO A 397 -20.974 31.247 46.943 1.00 63.27 A N
ANISOU 3111 N PRO A 397 8893 3373 11774 -15 5200 -2715 A N
ATOM 3112 CA PRO A 397 -20.699 30.191 45.950 1.00 60.23 A C
ANISOU 3112 CA PRO A 397 8570 3090 11226 63 4912 -2438 A C
ATOM 3113 C PRO A 397 -21.811 29.156 45.806 1.00 62.61 A C
ANISOU 3113 C PRO A 397 8994 3464 11330 179 4723 -2042 A C
ATOM 3114 O PRO A 397 -22.085 28.726 44.690 1.00 60.06 A O
ANISOU 3114 O PRO A 397 8702 3094 11024 221 4632 -1716 A O
ATOM 3115 CB PRO A 397 -19.419 29.529 46.477 1.00 62.15 A C
ANISOU 3115 CB PRO A 397 8793 3642 11178 45 4674 -2770 A C
ATOM 3116 CG PRO A 397 -18.841 30.470 47.461 1.00 69.54 A C
ANISOU 3116 CG PRO A 397 9606 4628 12190 -82 4871 -3251 A C
ATOM 3117 CD PRO A 397 -20.014 31.181 48.064 1.00 66.28 A C
ANISOU 3117 CD PRO A 397 9214 4024 11945 -93 5122 -3194 A C
ATOM 3118 N GLU A 398 -22.431 28.751 46.928 1.00 60.72 A N
ANISOU 3118 N GLU A 398 8819 3355 10898 214 4677 -2088 A N
ATOM 3119 CA GLU A 398 -23.515 27.773 46.985 1.00 59.07 A C
ANISOU 3119 CA GLU A 398 8731 3223 10490 289 4534 -1766 A C
ATOM 3120 C GLU A 398 -24.717 28.238 46.154 1.00 62.64 A C
ANISOU 3120 C GLU A 398 9137 3488 11177 307 4697 -1403 A C
ATOM 3121 O GLU A 398 -25.246 27.450 45.363 1.00 61.02 A O
ANISOU 3121 O GLU A 398 8983 3334 10870 334 4557 -1089 A O
ATOM 3122 CB GLU A 398 -23.931 27.515 48.442 1.00 61.84 A C
ANISOU 3122 CB GLU A 398 9143 3724 10627 313 4520 -1925 A C
ATOM 3123 CG GLU A 398 -22.999 26.576 49.195 1.00 79.18 A C
ANISOU 3123 CG GLU A 398 11427 6199 12460 368 4281 -2135 A C
ATOM 3124 CD GLU A 398 -23.680 25.594 50.136 1.00103.76 A C
ANISOU 3124 CD GLU A 398 14696 9470 15260 447 4173 -2044 A C
ATOM 3125 OE1 GLU A 398 -23.389 25.640 51.354 1.00 93.19 A O
ANISOU 3125 OE1 GLU A 398 13349 8309 13748 480 4178 -2313 A O
ATOM 3126 OE2 GLU A 398 -24.469 24.749 49.654 1.00 97.81 A O1-
ANISOU 3126 OE2 GLU A 398 14070 8678 14416 469 4091 -1716 A O1-
ATOM 3127 N ILE A 399 -25.113 29.528 46.296 1.00 59.74 A N
ANISOU 3127 N ILE A 399 8667 2917 11114 299 5008 -1452 A N
ATOM 3128 CA ILE A 399 -26.220 30.132 45.550 1.00 59.10 A C
ANISOU 3128 CA ILE A 399 8517 2678 11262 367 5205 -1104 A C
ATOM 3129 C ILE A 399 -25.847 30.257 44.056 1.00 61.73 A C
ANISOU 3129 C ILE A 399 8797 2924 11732 392 5197 -879 A C
ATOM 3130 O ILE A 399 -26.671 29.891 43.207 1.00 61.59 A O
ANISOU 3130 O ILE A 399 8751 2967 11682 457 5139 -513 A O
ATOM 3131 CB ILE A 399 -26.664 31.491 46.166 1.00 64.76 A C
ANISOU 3131 CB ILE A 399 9164 3176 12267 383 5580 -1226 A C
ATOM 3132 CG1 ILE A 399 -27.209 31.281 47.604 1.00 65.70 A C
ANISOU 3132 CG1 ILE A 399 9330 3413 12222 367 5576 -1401 A C
ATOM 3133 CG2 ILE A 399 -27.712 32.205 45.273 1.00 66.87 A C
ANISOU 3133 CG2 ILE A 399 9346 3280 12781 511 5815 -833 A C
ATOM 3134 CD1 ILE A 399 -27.807 32.497 48.325 1.00 73.78 A C
ANISOU 3134 CD1 ILE A 399 10301 4236 13498 377 5946 -1539 A C
ATOM 3135 N PHE A 400 -24.609 30.733 43.735 1.00 56.87 A N
ANISOU 3135 N PHE A 400 8157 2204 11248 332 5252 -1107 A N
ATOM 3136 CA PHE A 400 -24.159 30.883 42.343 1.00 54.67 A C
ANISOU 3136 CA PHE A 400 7834 1838 11099 353 5259 -916 A C
ATOM 3137 C PHE A 400 -24.001 29.534 41.623 1.00 54.35 A C
ANISOU 3137 C PHE A 400 7853 2017 10780 355 4907 -734 A C
ATOM 3138 O PHE A 400 -24.202 29.488 40.411 1.00 52.15 A O
ANISOU 3138 O PHE A 400 7531 1723 10561 400 4895 -445 A O
ATOM 3139 CB PHE A 400 -22.850 31.679 42.229 1.00 57.42 A C
ANISOU 3139 CB PHE A 400 8144 2030 11644 260 5414 -1236 A C
ATOM 3140 CG PHE A 400 -22.665 32.280 40.850 1.00 59.33 A C
ANISOU 3140 CG PHE A 400 8332 2087 12124 305 5572 -1002 A C
ATOM 3141 CD1 PHE A 400 -23.499 33.308 40.400 1.00 63.22 A C
ANISOU 3141 CD1 PHE A 400 8778 2343 12898 417 5910 -739 A C
ATOM 3142 CD2 PHE A 400 -21.666 31.814 39.997 1.00 60.48 A C
ANISOU 3142 CD2 PHE A 400 8477 2302 12202 259 5396 -1026 A C
ATOM 3143 CE1 PHE A 400 -23.343 33.849 39.118 1.00 64.76 A C
ANISOU 3143 CE1 PHE A 400 8933 2384 13291 492 6070 -489 A C
ATOM 3144 CE2 PHE A 400 -21.490 32.375 38.722 1.00 63.36 A C
ANISOU 3144 CE2 PHE A 400 8795 2503 12775 306 5552 -802 A C
ATOM 3145 CZ PHE A 400 -22.329 33.392 38.292 1.00 62.81 A C
ANISOU 3145 CZ PHE A 400 8685 2205 12973 426 5890 -529 A C
ATOM 3146 N LEU A 401 -23.642 28.455 42.352 1.00 50.22 A N
ANISOU 3146 N LEU A 401 7436 1694 9950 317 4646 -898 A N
ATOM 3147 CA LEU A 401 -23.501 27.104 41.782 1.00 48.17 A C
ANISOU 3147 CA LEU A 401 7273 1610 9418 316 4349 -746 A C
ATOM 3148 C LEU A 401 -24.855 26.590 41.252 1.00 50.77 A C
ANISOU 3148 C LEU A 401 7606 2011 9674 338 4314 -374 A C
ATOM 3149 O LEU A 401 -24.889 25.981 40.186 1.00 49.93 A O
ANISOU 3149 O LEU A 401 7505 1975 9491 326 4188 -165 A O
ATOM 3150 CB LEU A 401 -22.903 26.120 42.801 1.00 47.89 A C
ANISOU 3150 CB LEU A 401 7373 1752 9072 312 4136 -984 A C
ATOM 3151 CG LEU A 401 -22.447 24.752 42.241 1.00 51.87 A C
ANISOU 3151 CG LEU A 401 8009 2391 9307 324 3867 -889 A C
ATOM 3152 CD1 LEU A 401 -21.237 24.892 41.318 1.00 52.62 A C
ANISOU 3152 CD1 LEU A 401 8050 2465 9480 316 3815 -985 A C
ATOM 3153 CD2 LEU A 401 -22.131 23.800 43.351 1.00 53.18 A C
ANISOU 3153 CD2 LEU A 401 8333 2719 9155 373 3712 -1041 A C
ATOM 3154 N GLY A 402 -25.946 26.898 41.968 1.00 48.38 A N
ANISOU 3154 N GLY A 402 7278 1707 9399 361 4441 -311 A N
ATOM 3155 CA GLY A 402 -27.312 26.558 41.575 1.00 47.21 A C
ANISOU 3155 CA GLY A 402 7085 1665 9189 374 4443 12 A C
ATOM 3156 C GLY A 402 -27.631 27.100 40.196 1.00 48.84 A C
ANISOU 3156 C GLY A 402 7141 1853 9564 431 4534 304 A C
ATOM 3157 O GLY A 402 -28.178 26.391 39.351 1.00 47.66 A O
ANISOU 3157 O GLY A 402 6963 1875 9271 402 4408 540 A O
ATOM 3158 N PHE A 403 -27.239 28.356 39.954 1.00 45.97 A N
ANISOU 3158 N PHE A 403 6685 1284 9497 508 4769 275 A N
ATOM 3159 CA PHE A 403 -27.375 29.006 38.649 1.00 45.53 A C
ANISOU 3159 CA PHE A 403 6499 1182 9620 604 4898 554 A C
ATOM 3160 C PHE A 403 -26.562 28.255 37.564 1.00 48.92 A C
ANISOU 3160 C PHE A 403 6958 1702 9926 544 4679 599 A C
ATOM 3161 O PHE A 403 -27.088 27.994 36.485 1.00 48.85 A O
ANISOU 3161 O PHE A 403 6859 1848 9854 580 4625 893 A O
ATOM 3162 CB PHE A 403 -26.930 30.471 38.717 1.00 47.28 A C
ANISOU 3162 CB PHE A 403 6672 1103 10189 684 5234 462 A C
ATOM 3163 CG PHE A 403 -26.525 31.045 37.377 1.00 48.13 A C
ANISOU 3163 CG PHE A 403 6704 1114 10468 765 5351 665 A C
ATOM 3164 CD1 PHE A 403 -27.479 31.308 36.395 1.00 50.78 A C
ANISOU 3164 CD1 PHE A 403 6906 1554 10832 924 5439 1083 A C
ATOM 3165 CD2 PHE A 403 -25.188 31.299 37.086 1.00 48.37 A C
ANISOU 3165 CD2 PHE A 403 6783 987 10608 690 5370 441 A C
ATOM 3166 CE1 PHE A 403 -27.097 31.798 35.142 1.00 51.69 A C
ANISOU 3166 CE1 PHE A 403 6957 1606 11076 1020 5546 1292 A C
ATOM 3167 CE2 PHE A 403 -24.814 31.812 35.841 1.00 51.69 A C
ANISOU 3167 CE2 PHE A 403 7145 1314 11182 763 5491 637 A C
ATOM 3168 CZ PHE A 403 -25.768 32.046 34.874 1.00 50.41 A C
ANISOU 3168 CZ PHE A 403 6868 1246 11038 935 5577 1071 A C
ATOM 3169 N LEU A 404 -25.285 27.965 37.842 1.00 44.57 A N
ANISOU 3169 N LEU A 404 6514 1081 9339 463 4567 304 A N
ATOM 3170 CA LEU A 404 -24.401 27.309 36.888 1.00 45.41 A C
ANISOU 3170 CA LEU A 404 6656 1253 9344 416 4379 313 A C
ATOM 3171 C LEU A 404 -24.917 25.934 36.501 1.00 43.85 A C
ANISOU 3171 C LEU A 404 6526 1292 8844 353 4126 466 A C
ATOM 3172 O LEU A 404 -24.849 25.593 35.318 1.00 40.76 A O
ANISOU 3172 O LEU A 404 6090 993 8403 343 4044 650 A O
ATOM 3173 CB LEU A 404 -22.970 27.203 37.414 1.00 46.59 A C
ANISOU 3173 CB LEU A 404 6893 1332 9476 355 4303 -54 A C
ATOM 3174 CG LEU A 404 -22.237 28.515 37.563 1.00 54.24 A C
ANISOU 3174 CG LEU A 404 7788 2076 10745 359 4564 -255 A C
ATOM 3175 CD1 LEU A 404 -21.026 28.326 38.403 1.00 54.86 A C
ANISOU 3175 CD1 LEU A 404 7921 2181 10741 283 4477 -669 A C
ATOM 3176 CD2 LEU A 404 -21.841 29.087 36.213 1.00 59.02 A C
ANISOU 3176 CD2 LEU A 404 8314 2574 11536 389 4674 -94 A C
ATOM 3177 N LYS A 405 -25.466 25.177 37.489 1.00 38.84 A N
ANISOU 3177 N LYS A 405 5961 825 7972 298 4031 383 A N
ATOM 3178 CA ALYS A 405 -26.061 23.855 37.282 0.50 37.24 A C
ANISOU 3178 CA ALYS A 405 5831 853 7466 214 3846 487 A C
ATOM 3179 CA BLYS A 405 -26.053 23.854 37.271 0.50 37.46 A C
ANISOU 3179 CA BLYS A 405 5868 861 7503 213 3845 489 A C
ATOM 3180 C LYS A 405 -27.265 23.956 36.335 1.00 40.90 A C
ANISOU 3180 C LYS A 405 6186 1366 7989 204 3897 824 A C
ATOM 3181 O LYS A 405 -27.377 23.174 35.402 1.00 39.83 A O
ANISOU 3181 O LYS A 405 6050 1386 7698 122 3770 947 A O
ATOM 3182 CB ALYS A 405 -26.504 23.238 38.630 0.50 38.53 A C
ANISOU 3182 CB ALYS A 405 6198 929 7514 171 3810 367 A C
ATOM 3183 CB BLYS A 405 -26.473 23.213 38.612 0.50 39.48 A C
ANISOU 3183 CB BLYS A 405 6322 1049 7631 170 3805 364 A C
ATOM 3184 CG ALYS A 405 -25.366 22.779 39.531 0.50 36.64 A C
ANISOU 3184 CG ALYS A 405 6023 859 7039 173 3705 81 A C
ATOM 3185 CG BLYS A 405 -25.425 22.304 39.237 0.50 45.59 A C
ANISOU 3185 CG BLYS A 405 7313 1807 8201 156 3642 135 A C
ATOM 3186 CD ALYS A 405 -25.857 22.419 40.933 0.50 34.09 A C
ANISOU 3186 CD ALYS A 405 5731 735 6487 154 3718 -15 A C
ATOM 3187 CD BLYS A 405 -25.961 21.630 40.512 0.50 47.58 A C
ANISOU 3187 CD BLYS A 405 7720 2102 8256 139 3626 52 A C
ATOM 3188 CE ALYS A 405 -24.944 21.393 41.555 0.50 40.74 A C
ANISOU 3188 CE ALYS A 405 6989 1210 7279 220 3565 -226 A C
ATOM 3189 CE BLYS A 405 -25.363 20.258 40.771 0.50 40.32 A C
ANISOU 3189 CE BLYS A 405 7053 1220 7047 126 3466 -27 A C
ATOM 3190 NZ ALYS A 405 -24.773 21.604 43.011 0.50 50.46 A N1+
ANISOU 3190 NZ ALYS A 405 8279 2458 8437 284 3606 -435 A N1+
ATOM 3191 NZ BLYS A 405 -25.864 19.229 39.817 0.50 35.17 A N1+
ANISOU 3191 NZ BLYS A 405 6467 657 6238 4 3398 158 A N1+
ATOM 3192 N SER A 406 -28.176 24.920 36.584 1.00 39.62 A N
ANISOU 3192 N SER A 406 5868 1196 7989 298 4094 955 A N
ATOM 3193 CA SER A 406 -29.378 25.105 35.753 1.00 40.87 A C
ANISOU 3193 CA SER A 406 5821 1575 8132 338 4158 1273 A C
ATOM 3194 C SER A 406 -29.013 25.600 34.359 1.00 44.68 A C
ANISOU 3194 C SER A 406 6167 2092 8717 424 4191 1470 A C
ATOM 3195 O SER A 406 -29.694 25.238 33.402 1.00 44.63 A O
ANISOU 3195 O SER A 406 6022 2362 8575 405 4131 1698 A O
ATOM 3196 CB SER A 406 -30.363 26.077 36.391 1.00 44.35 A C
ANISOU 3196 CB SER A 406 6134 1988 8729 467 4384 1369 A C
ATOM 3197 OG SER A 406 -30.538 25.778 37.762 1.00 60.62 A O
ANISOU 3197 OG SER A 406 8328 3984 10719 400 4374 1161 A O
ATOM 3198 N TYR A 407 -27.933 26.408 34.254 1.00 40.55 A N
ANISOU 3198 N TYR A 407 5677 1311 8418 507 4294 1366 A N
ATOM 3199 CA TYR A 407 -27.420 26.964 32.997 1.00 40.26 A C
ANISOU 3199 CA TYR A 407 5541 1249 8506 598 4360 1532 A C
ATOM 3200 C TYR A 407 -26.908 25.821 32.100 1.00 43.64 A C
ANISOU 3200 C TYR A 407 6025 1848 8708 465 4106 1527 A C
ATOM 3201 O TYR A 407 -27.284 25.763 30.929 1.00 46.05 A O
ANISOU 3201 O TYR A 407 6188 2363 8945 499 4085 1776 A O
ATOM 3202 CB TYR A 407 -26.342 28.035 33.283 1.00 41.85 A C
ANISOU 3202 CB TYR A 407 5794 1106 9001 667 4556 1353 A C
ATOM 3203 CG TYR A 407 -25.449 28.343 32.110 1.00 43.48 A C
ANISOU 3203 CG TYR A 407 5966 1247 9306 704 4584 1430 A C
ATOM 3204 CD1 TYR A 407 -25.926 29.056 31.012 1.00 47.76 A C
ANISOU 3204 CD1 TYR A 407 6349 1846 9952 871 4754 1777 A C
ATOM 3205 CD2 TYR A 407 -24.125 27.916 32.088 1.00 41.80 A C
ANISOU 3205 CD2 TYR A 407 5874 941 9066 593 4447 1170 A C
ATOM 3206 CE1 TYR A 407 -25.115 29.308 29.906 1.00 48.85 A C
ANISOU 3206 CE1 TYR A 407 6463 1933 10166 909 4786 1863 A C
ATOM 3207 CE2 TYR A 407 -23.298 28.182 30.999 1.00 42.15 A C
ANISOU 3207 CE2 TYR A 407 5885 934 9196 618 4476 1237 A C
ATOM 3208 CZ TYR A 407 -23.795 28.886 29.912 1.00 52.84 A C
ANISOU 3208 CZ TYR A 407 7094 2325 10659 769 4651 1582 A C
ATOM 3209 OH TYR A 407 -22.998 29.161 28.821 1.00 56.41 A O
ANISOU 3209 OH TYR A 407 7518 2727 11189 800 4695 1663 A O
ATOM 3210 N ILE A 408 -26.098 24.903 32.665 1.00 37.30 A N
ANISOU 3210 N ILE A 408 5374 1071 7727 350 3920 1214 A N
ATOM 3211 CA ILE A 408 -25.566 23.708 31.990 1.00 36.33 A C
ANISOU 3211 CA ILE A 408 5324 1126 7353 242 3690 1141 A C
ATOM 3212 C ILE A 408 -26.732 22.818 31.482 1.00 39.50 A C
ANISOU 3212 C ILE A 408 5745 1683 7581 86 3607 1386 A C
ATOM 3213 O ILE A 408 -26.697 22.383 30.328 1.00 39.00 A O
ANISOU 3213 O ILE A 408 5618 1794 7405 30 3522 1505 A O
ATOM 3214 CB ILE A 408 -24.601 22.918 32.934 1.00 36.91 A C
ANISOU 3214 CB ILE A 408 5658 1036 7330 150 3562 856 A C
ATOM 3215 CG1 ILE A 408 -23.248 23.658 33.067 1.00 36.02 A C
ANISOU 3215 CG1 ILE A 408 5469 899 7320 226 3619 637 A C
ATOM 3216 CG2 ILE A 408 -24.377 21.481 32.447 1.00 36.52 A C
ANISOU 3216 CG2 ILE A 408 5771 1085 7019 19 3360 835 A C
ATOM 3217 CD1 ILE A 408 -22.506 23.418 34.395 1.00 37.75 A C
ANISOU 3217 CD1 ILE A 408 5929 839 7575 201 3574 367 A C
ATOM 3218 N GLN A 409 -27.753 22.589 32.331 1.00 36.52 A N
ANISOU 3218 N GLN A 409 5358 1410 7110 52 3631 1372 A N
ATOM 3219 CA AGLN A 409 -28.939 21.782 32.004 0.50 36.55 A C
ANISOU 3219 CA AGLN A 409 5297 1698 6891 -104 3577 1514 A C
ATOM 3220 CA BGLN A 409 -28.930 21.780 31.990 0.50 36.41 A C
ANISOU 3220 CA BGLN A 409 5280 1682 6873 -105 3575 1515 A C
ATOM 3221 C GLN A 409 -29.789 22.461 30.929 1.00 42.20 A C
ANISOU 3221 C GLN A 409 5704 2697 7634 -11 3658 1816 A C
ATOM 3222 O GLN A 409 -30.250 21.793 29.998 1.00 42.70 A O
ANISOU 3222 O GLN A 409 5666 3067 7493 -137 3566 1914 A O
ATOM 3223 CB AGLN A 409 -29.790 21.516 33.256 0.50 37.63 A C
ANISOU 3223 CB AGLN A 409 5503 1835 6960 -163 3621 1435 A C
ATOM 3224 CB BGLN A 409 -29.778 21.465 33.233 0.50 37.33 A C
ANISOU 3224 CB BGLN A 409 5469 1803 6910 -172 3613 1432 A C
ATOM 3225 CG AGLN A 409 -29.177 20.506 34.220 0.50 45.40 A C
ANISOU 3225 CG AGLN A 409 6798 2645 7807 -275 3523 1180 A C
ATOM 3226 CG BGLN A 409 -29.207 20.347 34.102 0.50 41.72 A C
ANISOU 3226 CG BGLN A 409 6339 2204 7310 -300 3508 1185 A C
ATOM 3227 CD AGLN A 409 -29.660 20.666 35.643 0.50 61.53 A C
ANISOU 3227 CD AGLN A 409 8920 4593 9864 -250 3604 1079 A C
ATOM 3228 CD BGLN A 409 -29.073 19.037 33.356 0.50 51.50 A C
ANISOU 3228 CD BGLN A 409 7702 3556 8309 -497 3378 1157 A C
ATOM 3229 NE2AGLN A 409 -30.969 20.716 35.854 0.50 60.28 A N
ANISOU 3229 NE2AGLN A 409 8638 4626 9642 -312 3676 1193 A N
ATOM 3230 NE2BGLN A 409 -27.864 18.503 33.330 0.50 46.41 A N
ANISOU 3230 NE2BGLN A 409 7275 2731 7628 -490 3285 1006 A N
ATOM 3231 OE1AGLN A 409 -28.868 20.683 36.587 0.50 53.60 A O
ANISOU 3231 OE1AGLN A 409 8085 3377 8904 -182 3597 885 A O
ATOM 3232 OE1BGLN A 409 -30.048 18.474 32.840 0.50 42.63 A O
ANISOU 3232 OE1BGLN A 409 6483 2692 7023 -664 3374 1251 A O
ATOM 3233 N MET A 410 -29.992 23.783 31.058 1.00 39.60 A N
ANISOU 3233 N MET A 410 5225 2277 7544 216 3848 1960 A N
ATOM 3234 CA MET A 410 -30.778 24.566 30.110 1.00 41.84 A C
ANISOU 3234 CA MET A 410 5215 2819 7863 385 3966 2289 A C
ATOM 3235 C MET A 410 -30.214 24.474 28.690 1.00 44.61 A C
ANISOU 3235 C MET A 410 5485 3304 8160 401 3894 2417 A C
ATOM 3236 O MET A 410 -30.976 24.206 27.763 1.00 45.17 A O
ANISOU 3236 O MET A 410 5342 3782 8041 385 3846 2617 A O
ATOM 3237 CB MET A 410 -30.857 26.054 30.549 1.00 45.76 A C
ANISOU 3237 CB MET A 410 5637 3080 8668 656 4234 2403 A C
ATOM 3238 CG MET A 410 -31.674 26.943 29.617 1.00 52.67 A C
ANISOU 3238 CG MET A 410 6223 4204 9585 904 4400 2786 A C
ATOM 3239 SD MET A 410 -33.449 26.574 29.590 1.00 60.95 A S
ANISOU 3239 SD MET A 410 6996 5790 10373 894 4372 2991 A S
ATOM 3240 CE MET A 410 -33.805 26.958 27.875 1.00 60.32 A C
ANISOU 3240 CE MET A 410 6595 6139 10183 1105 4406 3393 A C
ATOM 3241 N PHE A 411 -28.896 24.673 28.523 1.00 40.20 A N
ANISOU 3241 N PHE A 411 5081 2444 7748 425 3886 2289 A N
ATOM 3242 CA PHE A 411 -28.302 24.747 27.198 1.00 40.51 A C
ANISOU 3242 CA PHE A 411 5046 2575 7770 467 3851 2419 A C
ATOM 3243 C PHE A 411 -27.448 23.545 26.775 1.00 42.70 A C
ANISOU 3243 C PHE A 411 5493 2863 7867 249 3626 2217 A C
ATOM 3244 O PHE A 411 -26.720 23.654 25.785 1.00 42.19 A O
ANISOU 3244 O PHE A 411 5405 2802 7821 284 3603 2276 A O
ATOM 3245 CB PHE A 411 -27.467 26.035 27.100 1.00 43.25 A C
ANISOU 3245 CB PHE A 411 5405 2589 8440 680 4063 2470 A C
ATOM 3246 CG PHE A 411 -28.239 27.315 27.308 1.00 47.70 A C
ANISOU 3246 CG PHE A 411 5814 3107 9204 934 4342 2710 A C
ATOM 3247 CD1 PHE A 411 -28.976 27.879 26.271 1.00 52.90 A C
ANISOU 3247 CD1 PHE A 411 6227 4049 9825 1143 4456 3090 A C
ATOM 3248 CD2 PHE A 411 -28.204 27.973 28.529 1.00 50.51 A C
ANISOU 3248 CD2 PHE A 411 6270 3147 9776 984 4508 2561 A C
ATOM 3249 CE1 PHE A 411 -29.676 29.071 26.452 1.00 56.75 A C
ANISOU 3249 CE1 PHE A 411 6587 4480 10495 1423 4746 3340 A C
ATOM 3250 CE2 PHE A 411 -28.897 29.170 28.710 1.00 56.55 A C
ANISOU 3250 CE2 PHE A 411 6914 3833 10738 1229 4802 2781 A C
ATOM 3251 CZ PHE A 411 -29.633 29.713 27.669 1.00 56.72 A C
ANISOU 3251 CZ PHE A 411 6707 4117 10728 1461 4927 3182 A C
ATOM 3252 N ALA A 412 -27.562 22.400 27.476 1.00 39.51 A N
ANISOU 3252 N ALA A 412 5263 2466 7281 36 3484 2000 A N
ATOM 3253 CA ALA A 412 -26.819 21.176 27.159 1.00 38.10 A C
ANISOU 3253 CA ALA A 412 5280 2275 6921 -158 3305 1812 A C
ATOM 3254 C ALA A 412 -27.060 20.742 25.721 1.00 43.00 A C
ANISOU 3254 C ALA A 412 5748 3235 7356 -242 3228 1960 A C
ATOM 3255 O ALA A 412 -28.211 20.747 25.264 1.00 43.03 A O
ANISOU 3255 O ALA A 412 5525 3603 7223 -272 3247 2137 A O
ATOM 3256 CB ALA A 412 -27.220 20.061 28.108 1.00 38.67 A C
ANISOU 3256 CB ALA A 412 5549 2331 6812 -350 3228 1622 A C
ATOM 3257 N PHE A 413 -25.961 20.391 25.005 1.00 39.88 A N
ANISOU 3257 N PHE A 413 5457 2751 6946 -273 3143 1881 A N
ATOM 3258 CA PHE A 413 -25.910 19.929 23.611 1.00 40.30 A C
ANISOU 3258 CA PHE A 413 5402 3086 6823 -361 3062 1973 A C
ATOM 3259 C PHE A 413 -26.194 21.082 22.607 1.00 45.12 A C
ANISOU 3259 C PHE A 413 5713 3905 7524 -147 3168 2289 A C
ATOM 3260 O PHE A 413 -26.274 20.852 21.397 1.00 44.73 A O
ANISOU 3260 O PHE A 413 5520 4162 7314 -186 3114 2408 A O
ATOM 3261 CB PHE A 413 -26.865 18.724 23.374 1.00 42.76 A C
ANISOU 3261 CB PHE A 413 5698 3726 6823 -635 2975 1916 A C
ATOM 3262 CG PHE A 413 -26.732 17.598 24.375 1.00 43.02 A C
ANISOU 3262 CG PHE A 413 6044 3542 6760 -828 2924 1648 A C
ATOM 3263 CD1 PHE A 413 -27.663 17.436 25.393 1.00 46.33 A C
ANISOU 3263 CD1 PHE A 413 6487 3973 7144 -895 2976 1610 A C
ATOM 3264 CD2 PHE A 413 -25.674 16.703 24.303 1.00 44.35 A C
ANISOU 3264 CD2 PHE A 413 6487 3498 6866 -919 2844 1451 A C
ATOM 3265 CE1 PHE A 413 -27.525 16.411 26.335 1.00 46.86 A C
ANISOU 3265 CE1 PHE A 413 6863 3825 7117 -1047 2957 1387 A C
ATOM 3266 CE2 PHE A 413 -25.555 15.657 25.226 1.00 46.87 A C
ANISOU 3266 CE2 PHE A 413 7114 3611 7084 -1052 2829 1239 A C
ATOM 3267 CZ PHE A 413 -26.474 15.525 26.245 1.00 45.38 A C
ANISOU 3267 CZ PHE A 413 6959 3421 6864 -1113 2891 1214 A C
ATOM 3268 N LYS A 414 -26.275 22.321 23.101 1.00 43.17 A N
ANISOU 3268 N LYS A 414 5392 3477 7535 90 3340 2419 A N
ATOM 3269 CA LYS A 414 -26.537 23.503 22.267 1.00 45.34 A C
ANISOU 3269 CA LYS A 414 5422 3883 7922 346 3501 2747 A C
ATOM 3270 C LYS A 414 -25.377 24.515 22.334 1.00 50.28 A C
ANISOU 3270 C LYS A 414 6146 4090 8867 522 3657 2734 A C
ATOM 3271 O LYS A 414 -24.449 24.351 23.131 1.00 48.31 A O
ANISOU 3271 O LYS A 414 6119 3493 8745 445 3629 2455 A O
ATOM 3272 CB LYS A 414 -27.862 24.172 22.678 1.00 48.95 A C
ANISOU 3272 CB LYS A 414 5674 4530 8396 495 3637 2964 A C
ATOM 3273 CG LYS A 414 -29.101 23.323 22.361 1.00 61.46 A C
ANISOU 3273 CG LYS A 414 7075 6632 9646 330 3512 3016 A C
ATOM 3274 CD LYS A 414 -30.356 23.702 23.166 1.00 73.89 A C
ANISOU 3274 CD LYS A 414 8506 8344 11226 412 3615 3120 A C
ATOM 3275 CE LYS A 414 -31.194 24.816 22.594 1.00 91.75 A C
ANISOU 3275 CE LYS A 414 10453 10884 13523 740 3794 3513 A C
ATOM 3276 NZ LYS A 414 -32.404 25.063 23.436 1.00104.01 A N1+
ANISOU 3276 NZ LYS A 414 11872 12587 15060 804 3881 3586 A N1+
ATOM 3277 N SER A 415 -25.429 25.536 21.452 1.00 47.89 A N
ANISOU 3277 N SER A 415 5670 3853 8674 758 3833 3037 A N
ATOM 3278 CA SER A 415 -24.489 26.650 21.380 1.00 48.04 A C
ANISOU 3278 CA SER A 415 5754 3492 9008 932 4054 3071 A C
ATOM 3279 C SER A 415 -25.159 27.882 21.974 1.00 55.71 A C
ANISOU 3279 C SER A 415 6652 4304 10213 1168 4343 3253 A C
ATOM 3280 O SER A 415 -26.390 27.973 21.916 1.00 58.26 A O
ANISOU 3280 O SER A 415 6792 4935 10411 1274 4371 3484 A O
ATOM 3281 CB SER A 415 -24.030 26.886 19.951 1.00 49.85 A C
ANISOU 3281 CB SER A 415 5879 3863 9197 1033 4089 3288 A C
ATOM 3282 OG SER A 415 -22.978 25.985 19.657 1.00 47.28 A O
ANISOU 3282 OG SER A 415 5697 3499 8770 822 3883 3037 A O
ATOM 3283 N VAL A 416 -24.375 28.785 22.612 1.00 51.78 A N
ANISOU 3283 N VAL A 416 6293 3338 10043 1231 4564 3119 A N
ATOM 3284 CA VAL A 416 -24.929 29.918 23.352 1.00 54.20 A C
ANISOU 3284 CA VAL A 416 6580 3415 10597 1421 4868 3221 A C
ATOM 3285 C VAL A 416 -24.197 31.246 23.068 1.00 58.33 A C
ANISOU 3285 C VAL A 416 7152 3549 11461 1600 5234 3313 A C
ATOM 3286 O VAL A 416 -22.979 31.265 22.872 1.00 55.42 A O
ANISOU 3286 O VAL A 416 6901 2951 11204 1487 5236 3109 A O
ATOM 3287 CB VAL A 416 -24.978 29.587 24.896 1.00 58.11 A C
ANISOU 3287 CB VAL A 416 7223 3716 11141 1253 4797 2868 A C
ATOM 3288 CG1 VAL A 416 -23.610 29.287 25.513 1.00 56.66 A C
ANISOU 3288 CG1 VAL A 416 7245 3235 11047 1051 4702 2451 A C
ATOM 3289 CG2 VAL A 416 -25.748 30.629 25.688 1.00 59.58 A C
ANISOU 3289 CG2 VAL A 416 7379 3712 11547 1432 5096 2965 A C
ATOM 3290 N THR A 417 -24.989 32.356 23.023 1.00 57.51 A N
ANISOU 3290 N THR A 417 6954 3381 11515 1887 5566 3633 A N
ATOM 3291 CA THR A 417 -24.535 33.746 22.889 1.00 59.13 A C
ANISOU 3291 CA THR A 417 7229 3166 12074 2087 6012 3755 A C
ATOM 3292 C THR A 417 -24.521 34.379 24.277 1.00 63.19 A C
ANISOU 3292 C THR A 417 7876 3277 12858 2038 6232 3491 A C
ATOM 3293 O THR A 417 -25.167 33.867 25.201 1.00 62.38 A O
ANISOU 3293 O THR A 417 7763 3295 12643 1944 6065 3347 A O
ATOM 3294 CB THR A 417 -25.410 34.577 21.917 1.00 64.70 A C
ANISOU 3294 CB THR A 417 7764 4047 12773 2480 6284 4308 A C
ATOM 3295 CG2 THR A 417 -25.286 34.148 20.476 1.00 59.95 A C
ANISOU 3295 CG2 THR A 417 7030 3813 11934 2550 6133 4569 A C
ATOM 3296 OG1 THR A 417 -26.778 34.561 22.327 1.00 63.57 A O
ANISOU 3296 OG1 THR A 417 7468 4192 12495 2633 6267 4508 A O
ATOM 3297 N THR A 418 -23.768 35.474 24.425 1.00 60.43 A N
ANISOU 3297 N THR A 418 7652 2450 12857 2081 6621 3408 A N
ATOM 3298 CA THR A 418 -23.666 36.242 25.660 1.00 61.16 A C
ANISOU 3298 CA THR A 418 7871 2129 13236 2028 6904 3140 A C
ATOM 3299 C THR A 418 -25.070 36.778 26.052 1.00 67.09 A C
ANISOU 3299 C THR A 418 8536 2947 14007 2295 7100 3441 A C
ATOM 3300 O THR A 418 -25.353 36.895 27.235 1.00 66.34 A O
ANISOU 3300 O THR A 418 8499 2714 13991 2209 7141 3202 A O
ATOM 3301 CB THR A 418 -22.630 37.359 25.455 1.00 67.69 A C
ANISOU 3301 CB THR A 418 8833 2461 14424 2024 7336 3041 A C
ATOM 3302 CG2 THR A 418 -22.674 38.420 26.545 1.00 66.38 A C
ANISOU 3302 CG2 THR A 418 8787 1843 14589 2014 7752 2830 A C
ATOM 3303 OG1 THR A 418 -21.338 36.755 25.421 1.00 64.69 A O
ANISOU 3303 OG1 THR A 418 8518 2058 14004 1729 7106 2662 A O
ATOM 3304 N GLU A 419 -25.927 37.080 25.050 1.00 66.53 A N
ANISOU 3304 N GLU A 419 8312 3128 13839 2628 7210 3962 A N
ATOM 3305 CA GLU A 419 -27.290 37.554 25.240 1.00 69.31 A C
ANISOU 3305 CA GLU A 419 8537 3636 14163 2934 7383 4310 A C
ATOM 3306 C GLU A 419 -28.162 36.460 25.856 1.00 70.06 A C
ANISOU 3306 C GLU A 419 8508 4163 13947 2791 6970 4202 A C
ATOM 3307 O GLU A 419 -28.906 36.774 26.787 1.00 71.24 A O
ANISOU 3307 O GLU A 419 8655 4243 14168 2855 7095 4172 A O
ATOM 3308 CB GLU A 419 -27.904 38.066 23.926 1.00 74.00 A C
ANISOU 3308 CB GLU A 419 8963 4486 14666 3340 7562 4898 A C
ATOM 3309 CG GLU A 419 -28.443 39.495 24.010 1.00 93.88 A C
ANISOU 3309 CG GLU A 419 11520 6681 17468 3742 8139 5238 A C
ATOM 3310 CD GLU A 419 -29.604 39.779 24.956 1.00129.09 A C
ANISOU 3310 CD GLU A 419 15915 11186 21947 3897 8255 5307 A C
ATOM 3311 OE1 GLU A 419 -29.710 40.937 25.423 1.00128.93 A O
ANISOU 3311 OE1 GLU A 419 16022 10715 22249 4114 8761 5399 A O
ATOM 3312 OE2 GLU A 419 -30.406 38.856 25.230 1.00125.72 A O1-
ANISOU 3312 OE2 GLU A 419 15318 11232 21219 3799 7868 5267 A O1-
ATOM 3313 N GLU A 420 -28.062 35.183 25.366 1.00 61.84 A N
ANISOU 3313 N GLU A 420 7381 3545 12571 2587 6510 4130 A N
ATOM 3314 CA GLU A 420 -28.819 34.030 25.916 1.00 59.25 A C
ANISOU 3314 CA GLU A 420 6963 3610 11940 2402 6131 3998 A C
ATOM 3315 C GLU A 420 -28.416 33.769 27.365 1.00 59.04 A C
ANISOU 3315 C GLU A 420 7125 3286 12020 2138 6063 3530 A C
ATOM 3316 O GLU A 420 -29.282 33.547 28.206 1.00 58.78 A O
ANISOU 3316 O GLU A 420 7052 3373 11910 2120 6012 3487 A O
ATOM 3317 CB GLU A 420 -28.627 32.753 25.086 1.00 58.68 A C
ANISOU 3317 CB GLU A 420 6810 3960 11524 2205 5716 3969 A C
ATOM 3318 CG GLU A 420 -29.285 32.791 23.722 1.00 74.06 A C
ANISOU 3318 CG GLU A 420 8510 6372 13258 2441 5707 4418 A C
ATOM 3319 CD GLU A 420 -28.874 31.645 22.827 1.00 93.19 A C
ANISOU 3319 CD GLU A 420 10886 9135 15387 2222 5350 4343 A C
ATOM 3320 OE1 GLU A 420 -29.713 30.745 22.592 1.00 98.50 A O
ANISOU 3320 OE1 GLU A 420 11389 10307 15730 2120 5092 4385 A O
ATOM 3321 OE2 GLU A 420 -27.702 31.630 22.388 1.00 82.44 A O1-
ANISOU 3321 OE2 GLU A 420 9662 7535 14125 2129 5340 4213 A O1-
ATOM 3322 N TRP A 421 -27.106 33.844 27.654 1.00 54.57 A N
ANISOU 3322 N TRP A 421 6750 2356 11628 1947 6082 3186 A N
ATOM 3323 CA TRP A 421 -26.555 33.683 28.996 1.00 52.57 A C
ANISOU 3323 CA TRP A 421 6665 1836 11472 1714 6038 2725 A C
ATOM 3324 C TRP A 421 -27.129 34.742 29.954 1.00 56.89 A C
ANISOU 3324 C TRP A 421 7242 2101 12270 1849 6399 2715 A C
ATOM 3325 O TRP A 421 -27.476 34.391 31.078 1.00 57.32 A O
ANISOU 3325 O TRP A 421 7337 2175 12265 1730 6297 2488 A O
ATOM 3326 CB TRP A 421 -25.005 33.747 28.967 1.00 50.08 A C
ANISOU 3326 CB TRP A 421 6499 1229 11302 1528 6044 2392 A C
ATOM 3327 CG TRP A 421 -24.369 33.766 30.336 1.00 50.74 A C
ANISOU 3327 CG TRP A 421 6723 1066 11489 1319 6046 1914 A C
ATOM 3328 CD1 TRP A 421 -24.028 32.686 31.097 1.00 51.11 A C
ANISOU 3328 CD1 TRP A 421 6839 1258 11321 1100 5702 1592 A C
ATOM 3329 CD2 TRP A 421 -24.047 34.930 31.121 1.00 52.76 A C
ANISOU 3329 CD2 TRP A 421 7061 913 12071 1322 6430 1707 A C
ATOM 3330 CE2 TRP A 421 -23.520 34.473 32.351 1.00 54.92 A C
ANISOU 3330 CE2 TRP A 421 7424 1158 12286 1091 6266 1247 A C
ATOM 3331 CE3 TRP A 421 -24.158 36.317 30.902 1.00 57.40 A C
ANISOU 3331 CE3 TRP A 421 7665 1153 12990 1500 6924 1865 A C
ATOM 3332 NE1 TRP A 421 -23.487 33.101 32.295 1.00 50.85 A N
ANISOU 3332 NE1 TRP A 421 6905 980 11437 980 5822 1205 A N
ATOM 3333 CZ2 TRP A 421 -23.087 35.349 33.351 1.00 55.76 A C
ANISOU 3333 CZ2 TRP A 421 7607 940 12640 1004 6556 909 A C
ATOM 3334 CZ3 TRP A 421 -23.765 37.185 31.911 1.00 60.80 A C
ANISOU 3334 CZ3 TRP A 421 8199 1209 13691 1403 7240 1529 A C
ATOM 3335 CH2 TRP A 421 -23.215 36.702 33.108 1.00 59.87 A C
ANISOU 3335 CH2 TRP A 421 8143 1108 13497 1142 7046 1039 A C
ATOM 3336 N LYS A 422 -27.201 36.028 29.518 1.00 55.41 A N
ANISOU 3336 N LYS A 422 7053 1636 12366 2100 6844 2959 A N
ATOM 3337 CA LYS A 422 -27.694 37.133 30.341 1.00 58.02 A C
ANISOU 3337 CA LYS A 422 7434 1640 12969 2249 7260 2963 A C
ATOM 3338 C LYS A 422 -29.192 37.002 30.561 1.00 62.17 A C
ANISOU 3338 C LYS A 422 7803 2486 13333 2451 7224 3256 A C
ATOM 3339 O LYS A 422 -29.642 37.238 31.679 1.00 61.80 A O
ANISOU 3339 O LYS A 422 7800 2313 13367 2423 7329 3087 A O
ATOM 3340 CB LYS A 422 -27.335 38.493 29.726 1.00 64.10 A C
ANISOU 3340 CB LYS A 422 8271 2007 14077 2474 7779 3171 A C
ATOM 3341 CG LYS A 422 -27.370 39.629 30.747 1.00 75.30 A C
ANISOU 3341 CG LYS A 422 9828 2939 15842 2501 8245 2981 A C
ATOM 3342 CD LYS A 422 -26.758 40.920 30.200 1.00 82.80 A C
ANISOU 3342 CD LYS A 422 10903 3402 17155 2645 8795 3093 A C
ATOM 3343 CE LYS A 422 -27.768 42.043 30.135 1.00101.42 A C
ANISOU 3343 CE LYS A 422 13259 5566 19708 3048 9295 3500 A C
ATOM 3344 NZ LYS A 422 -28.732 41.868 29.016 1.00116.67 A N1+
ANISOU 3344 NZ LYS A 422 14993 7926 21410 3431 9207 4109 A N1+
ATOM 3345 N LYS A 423 -29.953 36.582 29.526 1.00 60.51 A N
ANISOU 3345 N LYS A 423 7392 2727 12874 2634 7065 3666 A N
ATOM 3346 CA LYS A 423 -31.394 36.326 29.637 1.00 62.68 A C
ANISOU 3346 CA LYS A 423 7464 3416 12936 2803 6985 3938 A C
ATOM 3347 C LYS A 423 -31.651 35.182 30.626 1.00 65.63 A C
ANISOU 3347 C LYS A 423 7856 3994 13087 2492 6612 3602 A C
ATOM 3348 O LYS A 423 -32.612 35.259 31.396 1.00 67.46 A O
ANISOU 3348 O LYS A 423 8024 4317 13290 2556 6667 3628 A O
ATOM 3349 CB LYS A 423 -31.993 35.974 28.266 1.00 66.73 A C
ANISOU 3349 CB LYS A 423 7734 4446 13175 2998 6839 4374 A C
ATOM 3350 CG LYS A 423 -32.410 37.162 27.418 1.00 90.23 A C
ANISOU 3350 CG LYS A 423 10609 7383 16292 3456 7251 4868 A C
ATOM 3351 CD LYS A 423 -32.953 36.706 26.062 1.00106.66 A C
ANISOU 3351 CD LYS A 423 12418 10069 18040 3630 7056 5269 A C
ATOM 3352 CE LYS A 423 -33.877 37.722 25.415 1.00127.05 A C
ANISOU 3352 CE LYS A 423 14813 12818 20642 4158 7416 5830 A C
ATOM 3353 NZ LYS A 423 -33.144 38.868 24.812 1.00139.18 A N1+
ANISOU 3353 NZ LYS A 423 16503 13903 22476 4417 7845 6044 A N1+
ATOM 3354 N PHE A 424 -30.782 34.127 30.621 1.00 58.12 A N
ANISOU 3354 N PHE A 424 7003 3100 11979 2169 6255 3294 A N
ATOM 3355 CA PHE A 424 -30.945 33.001 31.542 1.00 54.90 A C
ANISOU 3355 CA PHE A 424 6652 2853 11355 1888 5930 2989 A C
ATOM 3356 C PHE A 424 -30.579 33.412 32.962 1.00 57.45 A C
ANISOU 3356 C PHE A 424 7153 2794 11881 1784 6074 2626 A C
ATOM 3357 O PHE A 424 -31.263 33.009 33.907 1.00 55.55 A O
ANISOU 3357 O PHE A 424 6914 2662 11531 1706 5985 2512 A O
ATOM 3358 CB PHE A 424 -30.133 31.769 31.118 1.00 53.97 A C
ANISOU 3358 CB PHE A 424 6607 2890 11010 1618 5550 2793 A C
ATOM 3359 CG PHE A 424 -30.465 30.573 31.982 1.00 52.84 A C
ANISOU 3359 CG PHE A 424 6527 2931 10619 1372 5254 2551 A C
ATOM 3360 CD1 PHE A 424 -31.672 29.895 31.825 1.00 56.07 A C
ANISOU 3360 CD1 PHE A 424 6777 3764 10765 1354 5108 2727 A C
ATOM 3361 CD2 PHE A 424 -29.615 30.177 33.010 1.00 53.40 A C
ANISOU 3361 CD2 PHE A 424 6811 2762 10718 1169 5154 2147 A C
ATOM 3362 CE1 PHE A 424 -32.026 28.854 32.692 1.00 55.80 A C
ANISOU 3362 CE1 PHE A 424 6825 3853 10522 1126 4895 2507 A C
ATOM 3363 CE2 PHE A 424 -29.965 29.123 33.864 1.00 55.02 A C
ANISOU 3363 CE2 PHE A 424 7097 3114 10696 981 4927 1956 A C
ATOM 3364 CZ PHE A 424 -31.166 28.473 33.698 1.00 53.67 A C
ANISOU 3364 CZ PHE A 424 6796 3307 10289 954 4812 2139 A C
ATOM 3365 N LEU A 425 -29.498 34.226 33.104 1.00 55.21 A N
ANISOU 3365 N LEU A 425 7011 2082 11884 1768 6308 2432 A N
ATOM 3366 CA LEU A 425 -29.056 34.745 34.406 1.00 55.08 A C
ANISOU 3366 CA LEU A 425 7144 1714 12070 1657 6485 2052 A C
ATOM 3367 C LEU A 425 -30.200 35.538 35.106 1.00 60.01 A C
ANISOU 3367 C LEU A 425 7715 2262 12824 1851 6784 2192 A C
ATOM 3368 O LEU A 425 -30.412 35.368 36.306 1.00 58.40 A O
ANISOU 3368 O LEU A 425 7574 2018 12596 1733 6753 1927 A O
ATOM 3369 CB LEU A 425 -27.796 35.619 34.227 1.00 55.41 A C
ANISOU 3369 CB LEU A 425 7303 1342 12407 1613 6748 1856 A C
ATOM 3370 CG LEU A 425 -27.232 36.317 35.468 1.00 58.67 A C
ANISOU 3370 CG LEU A 425 7849 1391 13052 1478 6990 1428 A C
ATOM 3371 CD1 LEU A 425 -26.449 35.345 36.364 1.00 55.86 A C
ANISOU 3371 CD1 LEU A 425 7577 1149 12500 1185 6641 971 A C
ATOM 3372 CD2 LEU A 425 -26.372 37.485 35.073 1.00 56.96 A C
ANISOU 3372 CD2 LEU A 425 7707 755 13179 1504 7400 1360 A C
ATOM 3373 N TYR A 426 -30.940 36.357 34.343 1.00 59.93 A N
ANISOU 3373 N TYR A 426 7585 2262 12925 2168 7067 2621 A N
ATOM 3374 CA TYR A 426 -32.060 37.164 34.830 1.00 63.33 A C
ANISOU 3374 CA TYR A 426 7947 2640 13476 2417 7382 2823 A C
ATOM 3375 C TYR A 426 -33.282 36.301 35.077 1.00 68.17 A C
ANISOU 3375 C TYR A 426 8394 3730 13779 2426 7106 2965 A C
ATOM 3376 O TYR A 426 -34.062 36.600 35.979 1.00 68.47 A O
ANISOU 3376 O TYR A 426 8418 3738 13859 2485 7243 2928 A O
ATOM 3377 CB TYR A 426 -32.389 38.270 33.831 1.00 67.35 A C
ANISOU 3377 CB TYR A 426 8382 3029 14179 2796 7781 3274 A C
ATOM 3378 CG TYR A 426 -31.599 39.536 34.041 1.00 70.50 A C
ANISOU 3378 CG TYR A 426 8973 2827 14986 2842 8269 3131 A C
ATOM 3379 CD1 TYR A 426 -30.287 39.649 33.581 1.00 71.48 A C
ANISOU 3379 CD1 TYR A 426 9226 2695 15240 2670 8294 2928 A C
ATOM 3380 CD2 TYR A 426 -32.178 40.645 34.647 1.00 73.80 A C
ANISOU 3380 CD2 TYR A 426 9443 2933 15666 3057 8740 3203 A C
ATOM 3381 CE1 TYR A 426 -29.564 40.828 33.748 1.00 75.09 A C
ANISOU 3381 CE1 TYR A 426 9855 2598 16077 2677 8780 2773 A C
ATOM 3382 CE2 TYR A 426 -31.464 41.823 34.825 1.00 76.84 A C
ANISOU 3382 CE2 TYR A 426 10022 2737 16438 3072 9240 3051 A C
ATOM 3383 CZ TYR A 426 -30.166 41.920 34.355 1.00 82.96 A C
ANISOU 3383 CZ TYR A 426 10918 3267 17337 2874 9266 2836 A C
ATOM 3384 OH TYR A 426 -29.473 43.090 34.540 1.00 86.04 A O
ANISOU 3384 OH TYR A 426 11496 3081 18113 2850 9793 2655 A O
ATOM 3385 N SER A 427 -33.462 35.237 34.266 1.00 63.89 A N
ANISOU 3385 N SER A 427 7723 3630 12923 2348 6736 3108 A N
ATOM 3386 CA SER A 427 -34.590 34.316 34.433 1.00 62.94 A C
ANISOU 3386 CA SER A 427 7437 3993 12485 2297 6471 3207 A C
ATOM 3387 C SER A 427 -34.443 33.544 35.741 1.00 63.94 A C
ANISOU 3387 C SER A 427 7715 4065 12515 1993 6267 2793 A C
ATOM 3388 O SER A 427 -35.407 33.457 36.502 1.00 63.73 A O
ANISOU 3388 O SER A 427 7622 4177 12414 2013 6289 2801 A O
ATOM 3389 CB SER A 427 -34.698 33.362 33.247 1.00 64.58 A C
ANISOU 3389 CB SER A 427 7493 4655 12390 2233 6154 3394 A C
ATOM 3390 OG SER A 427 -36.066 33.131 32.950 1.00 72.51 A O
ANISOU 3390 OG SER A 427 8235 6154 13163 2354 6095 3677 A O
ATOM 3391 N TYR A 428 -33.216 33.036 36.020 1.00 57.66 A N
ANISOU 3391 N TYR A 428 7119 3067 11720 1739 6091 2439 A N
ATOM 3392 CA TYR A 428 -32.871 32.282 37.231 1.00 54.25 A C
ANISOU 3392 CA TYR A 428 6853 2578 11181 1478 5899 2043 A C
ATOM 3393 C TYR A 428 -32.950 33.202 38.470 1.00 58.60 A C
ANISOU 3393 C TYR A 428 7487 2814 11964 1529 6191 1842 A C
ATOM 3394 O TYR A 428 -33.642 32.860 39.417 1.00 56.61 A O
ANISOU 3394 O TYR A 428 7244 2667 11599 1467 6139 1743 A O
ATOM 3395 CB TYR A 428 -31.464 31.647 37.090 1.00 51.76 A C
ANISOU 3395 CB TYR A 428 6705 2144 10818 1264 5679 1753 A C
ATOM 3396 CG TYR A 428 -31.123 30.706 38.227 1.00 50.67 A C
ANISOU 3396 CG TYR A 428 6727 2025 10498 1034 5448 1398 A C
ATOM 3397 CD1 TYR A 428 -31.474 29.360 38.176 1.00 50.89 A C
ANISOU 3397 CD1 TYR A 428 6776 2353 10205 884 5138 1411 A C
ATOM 3398 CD2 TYR A 428 -30.477 31.170 39.370 1.00 51.22 A C
ANISOU 3398 CD2 TYR A 428 6928 1829 10705 974 5567 1051 A C
ATOM 3399 CE1 TYR A 428 -31.228 28.504 39.256 1.00 48.78 A C
ANISOU 3399 CE1 TYR A 428 6677 2094 9763 714 4967 1126 A C
ATOM 3400 CE2 TYR A 428 -30.227 30.327 40.454 1.00 50.82 A C
ANISOU 3400 CE2 TYR A 428 7012 1840 10457 809 5367 757 A C
ATOM 3401 CZ TYR A 428 -30.590 28.991 40.387 1.00 54.49 A C
ANISOU 3401 CZ TYR A 428 7518 2579 10608 696 5071 814 A C
ATOM 3402 OH TYR A 428 -30.316 28.174 41.455 1.00 51.87 A O
ANISOU 3402 OH TYR A 428 7343 2287 10079 568 4908 554 A O
ATOM 3403 N PHE A 429 -32.251 34.362 38.462 1.00 58.29 A N
ANISOU 3403 N PHE A 429 7516 2386 12246 1624 6517 1768 A N
ATOM 3404 CA PHE A 429 -32.275 35.289 39.594 1.00 61.40 A C
ANISOU 3404 CA PHE A 429 7998 2456 12876 1645 6834 1536 A C
ATOM 3405 C PHE A 429 -33.384 36.356 39.424 1.00 71.90 A C
ANISOU 3405 C PHE A 429 9213 3717 14390 1957 7217 1872 A C
ATOM 3406 O PHE A 429 -33.123 37.546 39.549 1.00 74.11 A O
ANISOU 3406 O PHE A 429 9567 3609 14984 2063 7627 1809 A O
ATOM 3407 CB PHE A 429 -30.902 35.944 39.833 1.00 62.97 A C
ANISOU 3407 CB PHE A 429 8342 2262 13323 1532 7018 1205 A C
ATOM 3408 CG PHE A 429 -29.786 34.984 40.169 1.00 61.10 A C
ANISOU 3408 CG PHE A 429 8209 2106 12899 1251 6671 826 A C
ATOM 3409 CD1 PHE A 429 -29.686 34.414 41.438 1.00 62.30 A C
ANISOU 3409 CD1 PHE A 429 8442 2315 12915 1086 6536 477 A C
ATOM 3410 CD2 PHE A 429 -28.807 34.682 39.234 1.00 60.55 A C
ANISOU 3410 CD2 PHE A 429 8155 2072 12778 1176 6492 827 A C
ATOM 3411 CE1 PHE A 429 -28.638 33.530 41.742 1.00 61.22 A C
ANISOU 3411 CE1 PHE A 429 8398 2282 12581 878 6228 156 A C
ATOM 3412 CE2 PHE A 429 -27.759 33.804 39.546 1.00 60.28 A C
ANISOU 3412 CE2 PHE A 429 8214 2127 12563 955 6186 491 A C
ATOM 3413 CZ PHE A 429 -27.669 33.248 40.799 1.00 57.62 A C
ANISOU 3413 CZ PHE A 429 7953 1858 12081 821 6059 167 A C
ATOM 3414 N LYS A 430 -34.632 35.902 39.208 1.00 71.47 A N
ANISOU 3414 N LYS A 430 8978 4049 14127 2091 7096 2201 A N
ATOM 3415 CA LYS A 430 -35.818 36.745 39.022 1.00 75.19 A C
ANISOU 3415 CA LYS A 430 9292 4578 14697 2426 7406 2573 A C
ATOM 3416 C LYS A 430 -36.166 37.555 40.271 1.00 81.00 A C
ANISOU 3416 C LYS A 430 10113 5021 15641 2478 7733 2390 A C
ATOM 3417 O LYS A 430 -36.667 38.674 40.139 1.00 84.51 A O
ANISOU 3417 O LYS A 430 10520 5271 16318 2779 8149 2626 A O
ATOM 3418 CB LYS A 430 -37.023 35.892 38.613 1.00 78.58 A C
ANISOU 3418 CB LYS A 430 9489 5571 14798 2479 7142 2866 A C
ATOM 3419 CG LYS A 430 -37.777 36.482 37.436 1.00104.22 A C
ANISOU 3419 CG LYS A 430 12508 9042 18050 2845 7315 3379 A C
ATOM 3420 CD LYS A 430 -38.893 35.562 36.966 1.00120.03 A C
ANISOU 3420 CD LYS A 430 14241 11678 19688 2849 7029 3617 A C
ATOM 3421 CE LYS A 430 -39.394 35.945 35.592 1.00137.96 A C
ANISOU 3421 CE LYS A 430 16249 14271 21899 3209 7149 4120 A C
ATOM 3422 NZ LYS A 430 -38.388 35.668 34.525 1.00147.40 A N1+
ANISOU 3422 NZ LYS A 430 17471 15465 23069 3176 7027 4198 A N1+
ATOM 3423 N ASP A 431 -35.944 36.991 41.474 1.00 74.90 A N
ANISOU 3423 N ASP A 431 9459 4221 14777 2208 7568 1983 A N
ATOM 3424 CA ASP A 431 -36.216 37.680 42.741 1.00 76.01 A C
ANISOU 3424 CA ASP A 431 9685 4107 15087 2215 7854 1750 A C
ATOM 3425 C ASP A 431 -35.073 38.637 43.114 1.00 80.49 A C
ANISOU 3425 C ASP A 431 10440 4167 15977 2132 8171 1414 A C
ATOM 3426 O ASP A 431 -35.295 39.592 43.868 1.00 83.57 A O
ANISOU 3426 O ASP A 431 10891 4253 16606 2219 8567 1305 A O
ATOM 3427 CB ASP A 431 -36.446 36.667 43.877 1.00 76.06 A C
ANISOU 3427 CB ASP A 431 9733 4334 14831 1968 7549 1461 A C
ATOM 3428 CG ASP A 431 -37.637 35.758 43.661 1.00 89.08 A C
ANISOU 3428 CG ASP A 431 11207 6458 16180 2006 7298 1737 A C
ATOM 3429 OD1 ASP A 431 -37.425 34.539 43.451 1.00 88.68 A O
ANISOU 3429 OD1 ASP A 431 11165 6681 15850 1801 6908 1687 A O
ATOM 3430 OD2 ASP A 431 -38.783 36.257 43.720 1.00 98.20 A O1-
ANISOU 3430 OD2 ASP A 431 12218 7718 17377 2234 7508 1993 A O1-
ATOM 3431 N LYS A 432 -33.859 38.370 42.576 1.00 74.22 A N
ANISOU 3431 N LYS A 432 9728 3291 15180 1951 8009 1234 A N
ATOM 3432 CA LYS A 432 -32.611 39.111 42.793 1.00 74.12 A C
ANISOU 3432 CA LYS A 432 9869 2865 15428 1804 8249 869 A C
ATOM 3433 C LYS A 432 -32.256 40.001 41.571 1.00 78.58 A C
ANISOU 3433 C LYS A 432 10439 3157 16259 1994 8571 1140 A C
ATOM 3434 O LYS A 432 -31.135 40.501 41.480 1.00 77.78 A O
ANISOU 3434 O LYS A 432 10453 2741 16360 1851 8751 868 A O
ATOM 3435 CB LYS A 432 -31.457 38.117 43.083 1.00 72.95 A C
ANISOU 3435 CB LYS A 432 9791 2856 15069 1482 7842 482 A C
ATOM 3436 CG LYS A 432 -31.539 37.418 44.440 1.00 77.43 A C
ANISOU 3436 CG LYS A 432 10402 3611 15408 1290 7604 141 A C
ATOM 3437 CD LYS A 432 -30.393 36.428 44.639 1.00 75.37 A C
ANISOU 3437 CD LYS A 432 10207 3514 14918 1039 7216 -178 A C
ATOM 3438 CE LYS A 432 -30.457 35.696 45.959 1.00 82.83 A C
ANISOU 3438 CE LYS A 432 11204 4659 15608 888 6990 -483 A C
ATOM 3439 NZ LYS A 432 -30.043 36.560 47.101 1.00 94.30 A N1+
ANISOU 3439 NZ LYS A 432 12714 5894 17221 779 7267 -922 A N1+
ATOM 3440 N VAL A 433 -33.222 40.191 40.646 1.00 76.07 A N
ANISOU 3440 N VAL A 433 9988 2991 15924 2320 8654 1675 A N
ATOM 3441 CA VAL A 433 -33.136 40.989 39.416 1.00 77.70 A C
ANISOU 3441 CA VAL A 433 10177 3014 16331 2587 8959 2052 A C
ATOM 3442 C VAL A 433 -32.698 42.458 39.729 1.00 83.45 A C
ANISOU 3442 C VAL A 433 11078 3136 17493 2656 9586 1908 A C
ATOM 3443 O VAL A 433 -32.039 43.084 38.894 1.00 82.62 A O
ANISOU 3443 O VAL A 433 11044 2753 17595 2735 9850 2022 A O
ATOM 3444 CB VAL A 433 -34.492 40.885 38.647 1.00 82.81 A C
ANISOU 3444 CB VAL A 433 10608 4038 16817 2955 8927 2638 A C
ATOM 3445 CG1 VAL A 433 -35.014 42.224 38.136 1.00 86.51 A C
ANISOU 3445 CG1 VAL A 433 11075 4223 17571 3378 9495 3035 A C
ATOM 3446 CG2 VAL A 433 -34.403 39.858 37.522 1.00 80.13 A C
ANISOU 3446 CG2 VAL A 433 10129 4139 16178 2923 8486 2863 A C
ATOM 3447 N ASP A 434 -33.009 42.967 40.947 1.00 82.18 A N
ANISOU 3447 N ASP A 434 10998 2763 17465 2596 9831 1625 A N
ATOM 3448 CA ASP A 434 -32.607 44.309 41.385 1.00 85.68 A C
ANISOU 3448 CA ASP A 434 11620 2619 18314 2603 10447 1411 A C
ATOM 3449 C ASP A 434 -31.080 44.388 41.600 1.00 88.13 A C
ANISOU 3449 C ASP A 434 12068 2672 18746 2211 10458 872 A C
ATOM 3450 O ASP A 434 -30.487 45.433 41.357 1.00 90.60 A O
ANISOU 3450 O ASP A 434 12521 2504 19398 2206 10957 775 A O
ATOM 3451 CB ASP A 434 -33.359 44.720 42.662 1.00 89.40 A C
ANISOU 3451 CB ASP A 434 12124 2984 18859 2621 10676 1228 A C
ATOM 3452 CG ASP A 434 -32.998 43.933 43.900 1.00 97.61 A C
ANISOU 3452 CG ASP A 434 13175 4221 19693 2244 10317 695 A C
ATOM 3453 OD1 ASP A 434 -33.519 42.800 44.058 1.00 98.69 A O
ANISOU 3453 OD1 ASP A 434 13184 4833 19482 2213 9824 785 A O
ATOM 3454 OD2 ASP A 434 -32.204 44.448 44.718 1.00 99.01 A O1-
ANISOU 3454 OD2 ASP A 434 13485 4090 20046 1979 10545 183 A O1-
ATOM 3455 N ILE A 435 -30.456 43.284 42.037 1.00 81.08 A N
ANISOU 3455 N ILE A 435 11133 2106 17570 1893 9931 530 A N
ATOM 3456 CA ILE A 435 -29.016 43.201 42.274 1.00 80.71 A C
ANISOU 3456 CA ILE A 435 11166 1935 17565 1528 9866 12 A C
ATOM 3457 C ILE A 435 -28.287 43.100 40.898 1.00 84.49 A C
ANISOU 3457 C ILE A 435 11637 2390 18075 1562 9803 232 A C
ATOM 3458 O ILE A 435 -27.176 43.623 40.752 1.00 85.21 A O
ANISOU 3458 O ILE A 435 11817 2191 18367 1363 10024 -73 A O
ATOM 3459 CB ILE A 435 -28.667 42.015 43.235 1.00 80.85 A C
ANISOU 3459 CB ILE A 435 11135 2349 17233 1239 9329 -387 A C
ATOM 3460 CG1 ILE A 435 -29.497 42.057 44.529 1.00 81.80 A C
ANISOU 3460 CG1 ILE A 435 11252 2547 17283 1244 9363 -528 A C
ATOM 3461 CG2 ILE A 435 -27.177 41.986 43.570 1.00 82.44 A C
ANISOU 3461 CG2 ILE A 435 11391 2465 17467 883 9295 -956 A C
ATOM 3462 CD1 ILE A 435 -29.664 40.667 45.259 1.00 89.32 A C
ANISOU 3462 CD1 ILE A 435 12141 3984 17812 1098 8784 -676 A C
ATOM 3463 N LEU A 436 -28.925 42.442 39.902 1.00 78.90 A N
ANISOU 3463 N LEU A 436 10812 2005 17163 1802 9515 745 A N
ATOM 3464 CA LEU A 436 -28.386 42.289 38.554 1.00 78.00 A C
ANISOU 3464 CA LEU A 436 10671 1927 17038 1872 9432 1011 A C
ATOM 3465 C LEU A 436 -28.324 43.659 37.827 1.00 89.23 A C
ANISOU 3465 C LEU A 436 12191 2870 18842 2103 10058 1264 A C
ATOM 3466 O LEU A 436 -27.315 43.963 37.182 1.00 90.22 A O
ANISOU 3466 O LEU A 436 12385 2787 19107 2000 10185 1183 A O
ATOM 3467 CB LEU A 436 -29.207 41.267 37.743 1.00 75.14 A C
ANISOU 3467 CB LEU A 436 10141 2070 16339 2063 8990 1476 A C
ATOM 3468 CG LEU A 436 -29.179 39.775 38.218 1.00 74.61 A C
ANISOU 3468 CG LEU A 436 10004 2468 15877 1832 8369 1276 A C
ATOM 3469 CD1 LEU A 436 -30.097 38.918 37.385 1.00 72.50 A C
ANISOU 3469 CD1 LEU A 436 9574 2658 15316 2012 8039 1732 A C
ATOM 3470 CD2 LEU A 436 -27.776 39.174 38.172 1.00 71.62 A C
ANISOU 3470 CD2 LEU A 436 9686 2108 15417 1526 8098 897 A C
ATOM 3471 N ASP A 437 -29.367 44.499 37.991 1.00 88.31 A N
ANISOU 3471 N ASP A 437 12094 2562 18897 2414 10475 1557 A N
ATOM 3472 CA ASP A 437 -29.469 45.821 37.373 1.00 92.37 A C
ANISOU 3472 CA ASP A 437 12727 2598 19771 2701 11130 1854 A C
ATOM 3473 C ASP A 437 -28.450 46.829 37.957 1.00 99.25 A C
ANISOU 3473 C ASP A 437 13815 2874 21021 2424 11644 1346 A C
ATOM 3474 O ASP A 437 -28.329 47.952 37.449 1.00100.29 A O
ANISOU 3474 O ASP A 437 14094 2526 21487 2600 12243 1524 A O
ATOM 3475 CB ASP A 437 -30.909 46.358 37.514 1.00 96.47 A C
ANISOU 3475 CB ASP A 437 13198 3121 20334 3129 11416 2293 A C
ATOM 3476 CG ASP A 437 -31.924 45.616 36.656 1.00105.68 A C
ANISOU 3476 CG ASP A 437 14131 4854 21170 3460 11043 2869 A C
ATOM 3477 OD1 ASP A 437 -31.520 45.025 35.623 1.00103.50 A O
ANISOU 3477 OD1 ASP A 437 13769 4834 20721 3462 10745 3063 A O
ATOM 3478 OD2 ASP A 437 -33.121 45.651 36.995 1.00115.09 A O1-
ANISOU 3478 OD2 ASP A 437 15214 6243 22271 3715 11071 3121 A O1-
ATOM 3479 N LYS A 438 -27.691 46.410 38.988 1.00 95.39 A N
ANISOU 3479 N LYS A 438 13341 2438 20465 1988 11419 713 A N
ATOM 3480 CA LYS A 438 -26.656 47.234 39.621 1.00 97.52 A C
ANISOU 3480 CA LYS A 438 13769 2252 21034 1644 11837 131 A C
ATOM 3481 C LYS A 438 -25.313 47.108 38.884 1.00 98.75 A C
ANISOU 3481 C LYS A 438 13943 2355 21224 1392 11758 -77 A C
ATOM 3482 O LYS A 438 -24.483 48.016 38.972 1.00102.20 A O
ANISOU 3482 O LYS A 438 14518 2341 21974 1178 12243 -419 A O
ATOM 3483 CB LYS A 438 -26.460 46.827 41.091 1.00 98.71 A C
ANISOU 3483 CB LYS A 438 13887 2568 21049 1305 11616 -465 A C
ATOM 3484 CG LYS A 438 -27.623 47.111 42.021 1.00109.31 A C
ANISOU 3484 CG LYS A 438 15239 3881 22411 1474 11785 -399 A C
ATOM 3485 CD LYS A 438 -27.344 46.476 43.376 1.00113.33 A C
ANISOU 3485 CD LYS A 438 15688 4684 22690 1141 11429 -952 A C
ATOM 3486 CE LYS A 438 -28.204 47.045 44.466 1.00120.41 A C
ANISOU 3486 CE LYS A 438 16634 5422 23693 1201 11742 -1072 A C
ATOM 3487 NZ LYS A 438 -27.392 47.358 45.667 1.00125.21 A N1+
ANISOU 3487 NZ LYS A 438 17291 5928 24357 780 11868 -1809 A N1+
ATOM 3488 N VAL A 439 -25.098 45.985 38.181 1.00 89.07 A N
ANISOU 3488 N VAL A 439 12579 1587 19677 1399 11170 107 A N
ATOM 3489 CA VAL A 439 -23.836 45.694 37.489 1.00 86.61 A C
ANISOU 3489 CA VAL A 439 12260 1300 19347 1168 11019 -81 A C
ATOM 3490 C VAL A 439 -23.754 46.563 36.218 1.00 90.63 A C
ANISOU 3490 C VAL A 439 12870 1439 20128 1414 11490 346 A C
ATOM 3491 O VAL A 439 -24.765 46.809 35.550 1.00 90.46 A O
ANISOU 3491 O VAL A 439 12838 1414 20116 1835 11629 944 A O
ATOM 3492 CB VAL A 439 -23.667 44.167 37.197 1.00 85.61 A C
ANISOU 3492 CB VAL A 439 11972 1775 18781 1103 10251 -31 A C
ATOM 3493 CG1 VAL A 439 -22.386 43.808 36.433 1.00 83.52 A C
ANISOU 3493 CG1 VAL A 439 11691 1560 18484 913 10088 -166 A C
ATOM 3494 CG2 VAL A 439 -23.852 43.286 38.428 1.00 83.31 A C
ANISOU 3494 CG2 VAL A 439 11609 1831 18214 894 9823 -417 A C
ATOM 3495 N ASP A 440 -22.538 47.037 35.919 1.00 88.03 A N
ANISOU 3495 N ASP A 440 12626 816 20005 1149 11747 25 A N
ATOM 3496 CA ASP A 440 -22.227 47.857 34.749 1.00 90.80 A C
ANISOU 3496 CA ASP A 440 13095 784 20622 1316 12216 351 A C
ATOM 3497 C ASP A 440 -21.903 46.888 33.589 1.00 89.33 A C
ANISOU 3497 C ASP A 440 12777 1014 20151 1402 11703 666 A C
ATOM 3498 O ASP A 440 -20.742 46.590 33.306 1.00 86.98 A O
ANISOU 3498 O ASP A 440 12458 764 19826 1113 11550 359 A O
ATOM 3499 CB ASP A 440 -21.070 48.833 35.085 1.00 96.00 A C
ANISOU 3499 CB ASP A 440 13907 930 21640 935 12761 -208 A C
ATOM 3500 CG ASP A 440 -20.568 49.760 33.988 1.00110.29 A C
ANISOU 3500 CG ASP A 440 15877 2261 23766 1034 13332 33 A C
ATOM 3501 OD1 ASP A 440 -20.985 49.590 32.820 1.00108.86 A O
ANISOU 3501 OD1 ASP A 440 15675 2188 23499 1413 13260 660 A O
ATOM 3502 OD2 ASP A 440 -19.751 50.655 34.298 1.00122.38 A O1-
ANISOU 3502 OD2 ASP A 440 17552 3325 25622 722 13865 -418 A O1-
ATOM 3503 N TRP A 441 -22.959 46.410 32.923 1.00 84.39 A N
ANISOU 3503 N TRP A 441 12032 749 19286 1784 11453 1273 A N
ATOM 3504 CA TRP A 441 -22.905 45.455 31.826 1.00 81.83 A C
ANISOU 3504 CA TRP A 441 11587 827 18679 1917 10965 1617 A C
ATOM 3505 C TRP A 441 -22.094 45.936 30.627 1.00 88.30 A C
ANISOU 3505 C TRP A 441 12480 1407 19662 1957 11241 1792 A C
ATOM 3506 O TRP A 441 -21.332 45.142 30.093 1.00 86.38 A O
ANISOU 3506 O TRP A 441 12156 1441 19226 1790 10839 1698 A O
ATOM 3507 CB TRP A 441 -24.313 45.068 31.385 1.00 80.01 A C
ANISOU 3507 CB TRP A 441 11224 960 18215 2343 10765 2223 A C
ATOM 3508 CG TRP A 441 -25.051 44.279 32.428 1.00 78.36 A C
ANISOU 3508 CG TRP A 441 10909 1105 17761 2268 10356 2060 A C
ATOM 3509 CD1 TRP A 441 -26.091 44.709 33.209 1.00 82.69 A C
ANISOU 3509 CD1 TRP A 441 11465 1580 18374 2442 10563 2148 A C
ATOM 3510 CD2 TRP A 441 -24.752 42.943 32.854 1.00 73.65 A C
ANISOU 3510 CD2 TRP A 441 10201 961 16821 1994 9704 1766 A C
ATOM 3511 CE2 TRP A 441 -25.673 42.612 33.869 1.00 76.75 A C
ANISOU 3511 CE2 TRP A 441 10541 1539 17081 2016 9546 1705 A C
ATOM 3512 CE3 TRP A 441 -23.796 41.984 32.469 1.00 71.59 A C
ANISOU 3512 CE3 TRP A 441 9892 960 16351 1748 9257 1558 A C
ATOM 3513 NE1 TRP A 441 -26.468 43.714 34.076 1.00 78.65 A N
ANISOU 3513 NE1 TRP A 441 10848 1459 17578 2281 10071 1927 A N
ATOM 3514 CZ2 TRP A 441 -25.660 41.367 34.512 1.00 72.59 A C
ANISOU 3514 CZ2 TRP A 441 9932 1426 16224 1798 8978 1450 A C
ATOM 3515 CZ3 TRP A 441 -23.777 40.762 33.118 1.00 69.29 A C
ANISOU 3515 CZ3 TRP A 441 9521 1068 15736 1549 8702 1308 A C
ATOM 3516 CH2 TRP A 441 -24.714 40.457 34.113 1.00 69.16 A C
ANISOU 3516 CH2 TRP A 441 9469 1214 15595 1578 8573 1266 A C
ATOM 3517 N LYS A 442 -22.238 47.201 30.222 1.00 89.60 A N
ANISOU 3517 N LYS A 442 12811 1056 20177 2177 11935 2041 A N
ATOM 3518 CA LYS A 442 -21.506 47.825 29.114 1.00 91.32 A C
ANISOU 3518 CA LYS A 442 13138 966 20594 2235 12311 2228 A C
ATOM 3519 C LYS A 442 -19.991 47.865 29.427 1.00 93.61 A C
ANISOU 3519 C LYS A 442 13489 1053 21026 1711 12350 1564 A C
ATOM 3520 O LYS A 442 -19.181 47.476 28.582 1.00 90.54 A O
ANISOU 3520 O LYS A 442 13058 793 20552 1614 12165 1579 A O
ATOM 3521 CB LYS A 442 -22.069 49.223 28.825 1.00 99.15 A C
ANISOU 3521 CB LYS A 442 14331 1396 21947 2599 13117 2620 A C
ATOM 3522 CG LYS A 442 -21.471 49.948 27.611 1.00128.58 A C
ANISOU 3522 CG LYS A 442 18193 4838 25823 2724 13485 2897 A C
ATOM 3523 CD LYS A 442 -22.171 49.595 26.291 1.00139.74 A C
ANISOU 3523 CD LYS A 442 19445 7108 26541 3080 12571 3465 A C
ATOM 3524 CE LYS A 442 -21.325 49.939 25.093 1.00149.42 A C
ANISOU 3524 CE LYS A 442 20706 8824 27245 2905 11780 3382 A C
ATOM 3525 NZ LYS A 442 -21.454 48.916 24.017 1.00152.45 A N1+
ANISOU 3525 NZ LYS A 442 20899 9631 27393 3102 11486 3792 A N1+
ATOM 3526 N GLY A 443 -19.653 48.276 30.653 1.00 91.89 A N
ANISOU 3526 N GLY A 443 13329 611 20975 1372 12559 982 A N
ATOM 3527 CA GLY A 443 -18.285 48.314 31.157 1.00 91.89 A C
ANISOU 3527 CA GLY A 443 13321 534 21057 842 12583 281 A C
ATOM 3528 C GLY A 443 -17.655 46.936 31.226 1.00 89.86 A C
ANISOU 3528 C GLY A 443 12892 807 20444 622 11808 11 A C
ATOM 3529 O GLY A 443 -16.469 46.772 30.931 1.00 88.11 A O
ANISOU 3529 O GLY A 443 12639 610 20229 330 11739 -317 A O
ATOM 3530 N TRP A 444 -18.457 45.924 31.577 1.00 84.26 A N
ANISOU 3530 N TRP A 444 12046 579 19389 765 11238 173 A N
ATOM 3531 CA TRP A 444 -17.997 44.529 31.651 1.00 79.63 A C
ANISOU 3531 CA TRP A 444 11291 555 18408 599 10504 -13 A C
ATOM 3532 C TRP A 444 -17.909 43.839 30.289 1.00 82.43 A C
ANISOU 3532 C TRP A 444 11574 1187 18559 788 10186 432 A C
ATOM 3533 O TRP A 444 -16.964 43.085 30.074 1.00 78.37 A O
ANISOU 3533 O TRP A 444 10981 924 17871 570 9822 183 A O
ATOM 3534 CB TRP A 444 -18.915 43.697 32.561 1.00 75.86 A C
ANISOU 3534 CB TRP A 444 10681 540 17602 648 10063 -1 A C
ATOM 3535 CG TRP A 444 -18.581 43.786 34.018 1.00 76.61 A C
ANISOU 3535 CG TRP A 444 10789 583 17737 342 10076 -616 A C
ATOM 3536 CD1 TRP A 444 -19.225 44.525 34.960 1.00 81.07 A C
ANISOU 3536 CD1 TRP A 444 11459 830 18515 372 10434 -750 A C
ATOM 3537 CD2 TRP A 444 -17.525 43.103 34.698 1.00 74.90 A C
ANISOU 3537 CD2 TRP A 444 10483 643 17335 -11 9716 -1188 A C
ATOM 3538 CE2 TRP A 444 -17.591 43.479 36.060 1.00 80.05 A C
ANISOU 3538 CE2 TRP A 444 11177 1158 18082 -189 9873 -1659 A C
ATOM 3539 CE3 TRP A 444 -16.526 42.209 34.292 1.00 73.72 A C
ANISOU 3539 CE3 TRP A 444 10264 767 16981 -154 9285 -1368 A C
ATOM 3540 NE1 TRP A 444 -18.627 44.362 36.186 1.00 79.98 A N
ANISOU 3540 NE1 TRP A 444 11278 799 18313 28 10320 -1383 A N
ATOM 3541 CZ2 TRP A 444 -16.699 42.982 37.018 1.00 79.10 A C
ANISOU 3541 CZ2 TRP A 444 10957 1319 17779 -517 9595 -2265 A C
ATOM 3542 CZ3 TRP A 444 -15.646 41.715 35.241 1.00 74.64 A C
ANISOU 3542 CZ3 TRP A 444 10290 1142 16928 -460 9021 -1955 A C
ATOM 3543 CH2 TRP A 444 -15.742 42.095 36.588 1.00 76.94 A C
ANISOU 3543 CH2 TRP A 444 10580 1389 17266 -632 9167 -2390 A C
ATOM 3544 N MET A 445 -18.889 44.053 29.390 1.00 83.94 A N
ANISOU 3544 N MET A 445 11774 1378 18742 1198 10306 1079 A N
ATOM 3545 CA MET A 445 -18.970 43.334 28.113 1.00 85.02 A C
ANISOU 3545 CA MET A 445 11816 1855 18634 1395 9973 1522 A C
ATOM 3546 C MET A 445 -18.292 43.996 26.923 1.00 93.59 A C
ANISOU 3546 C MET A 445 12978 2664 19915 1465 10342 1732 A C
ATOM 3547 O MET A 445 -17.712 43.282 26.100 1.00 90.91 A O
ANISOU 3547 O MET A 445 12562 2595 19384 1411 10010 1787 A O
ATOM 3548 CB MET A 445 -20.438 43.099 27.711 1.00 88.62 A C
ANISOU 3548 CB MET A 445 12187 2584 18902 1813 9850 2124 A C
ATOM 3549 CG MET A 445 -21.251 42.310 28.715 1.00 91.94 A C
ANISOU 3549 CG MET A 445 12513 3339 19079 1780 9446 2008 A C
ATOM 3550 SD MET A 445 -20.754 40.603 28.787 1.00 93.33 A S
ANISOU 3550 SD MET A 445 12562 4075 18826 1518 8660 1747 A S
ATOM 3551 CE MET A 445 -21.900 39.997 30.013 1.00 88.62 A C
ANISOU 3551 CE MET A 445 11905 3739 18028 1535 8383 1678 A C
ATOM 3552 N HIS A 446 -18.439 45.330 26.766 1.00 95.18 A N
ANISOU 3552 N HIS A 446 13342 2335 20486 1618 11039 1899 A N
ATOM 3553 CA HIS A 446 -17.944 46.007 25.572 1.00 97.52 A C
ANISOU 3553 CA HIS A 446 13734 2352 20966 1752 11445 2195 A C
ATOM 3554 C HIS A 446 -17.042 47.205 25.851 1.00102.00 A C
ANISOU 3554 C HIS A 446 14503 2279 21975 1501 12124 1824 A C
ATOM 3555 O HIS A 446 -17.084 48.192 25.111 1.00104.83 A O
ANISOU 3555 O HIS A 446 15018 2222 22592 1723 12712 2168 A O
ATOM 3556 CB HIS A 446 -19.132 46.450 24.707 1.00101.10 A C
ANISOU 3556 CB HIS A 446 14198 2817 21398 2307 11685 2957 A C
ATOM 3557 CG HIS A 446 -20.053 45.335 24.344 1.00101.44 A C
ANISOU 3557 CG HIS A 446 14023 3514 21006 2537 11065 3321 A C
ATOM 3558 CD2 HIS A 446 -19.937 44.400 23.374 1.00101.30 A C
ANISOU 3558 CD2 HIS A 446 13857 3968 20667 2587 10598 3540 A C
ATOM 3559 ND1 HIS A 446 -21.214 45.105 25.050 1.00102.77 A N
ANISOU 3559 ND1 HIS A 446 14108 3898 21041 2705 10905 3445 A N
ATOM 3560 CE1 HIS A 446 -21.774 44.046 24.491 1.00 99.76 A C
ANISOU 3560 CE1 HIS A 446 13528 4112 20264 2837 10357 3726 A C
ATOM 3561 NE2 HIS A 446 -21.045 43.589 23.473 1.00 99.11 A N
ANISOU 3561 NE2 HIS A 446 13403 4200 20055 2772 10158 3791 A N
ATOM 3562 N THR A 447 -16.195 47.105 26.873 1.00 96.33 A N
ANISOU 3562 N THR A 447 13776 1502 21324 1036 12054 1121 A N
ATOM 3563 CA THR A 447 -15.253 48.169 27.177 1.00 99.46 A C
ANISOU 3563 CA THR A 447 14329 1347 22113 714 12673 671 A C
ATOM 3564 C THR A 447 -13.840 47.543 27.253 1.00 99.41 A C
ANISOU 3564 C THR A 447 14202 1576 21995 253 12333 95 A C
ATOM 3565 O THR A 447 -13.662 46.556 27.960 1.00 93.35 A O
ANISOU 3565 O THR A 447 13269 1261 20939 67 11747 -241 A O
ATOM 3566 CB THR A 447 -15.682 48.938 28.429 1.00109.25 A C
ANISOU 3566 CB THR A 447 15677 2238 23593 606 13077 351 A C
ATOM 3567 CG2 THR A 447 -14.759 50.111 28.745 1.00111.25 A C
ANISOU 3567 CG2 THR A 447 16106 1892 24272 245 13792 -140 A C
ATOM 3568 OG1 THR A 447 -17.012 49.432 28.225 1.00114.39 A O
ANISOU 3568 OG1 THR A 447 16422 2727 24313 1092 13355 953 A O
ATOM 3569 N PRO A 448 -12.823 48.114 26.544 1.00 98.49 A N
ANISOU 3569 N PRO A 448 14165 1158 22097 77 12717 -20 A N
ATOM 3570 CA PRO A 448 -11.454 47.554 26.634 1.00 96.71 A C
ANISOU 3570 CA PRO A 448 13800 1181 21763 -358 12415 -586 A C
ATOM 3571 C PRO A 448 -10.814 47.754 28.014 1.00100.96 A C
ANISOU 3571 C PRO A 448 14286 1684 22391 -825 12489 -1379 A C
ATOM 3572 O PRO A 448 -11.294 48.566 28.804 1.00103.41 A O
ANISOU 3572 O PRO A 448 14714 1640 22936 -862 12926 -1526 A O
ATOM 3573 CB PRO A 448 -10.667 48.345 25.570 1.00101.42 A C
ANISOU 3573 CB PRO A 448 14523 1380 22631 -410 12943 -480 A C
ATOM 3574 CG PRO A 448 -11.421 49.580 25.367 1.00109.95 A C
ANISOU 3574 CG PRO A 448 15852 1858 24066 -146 13689 -105 A C
ATOM 3575 CD PRO A 448 -12.869 49.284 25.639 1.00103.92 A C
ANISOU 3575 CD PRO A 448 15073 1277 23133 279 13458 364 A C
ATOM 3576 N GLY A 449 -9.735 47.017 28.277 1.00 94.61 A N
ANISOU 3576 N GLY A 449 13295 1272 21381 -1164 12067 -1882 A N
ATOM 3577 CA GLY A 449 -8.952 47.153 29.496 1.00 95.44 A C
ANISOU 3577 CA GLY A 449 13296 1454 21514 -1625 12097 -2672 A C
ATOM 3578 C GLY A 449 -9.464 46.436 30.715 1.00 97.27 A C
ANISOU 3578 C GLY A 449 13407 2082 21470 -1629 11622 -2890 A C
ATOM 3579 O GLY A 449 -10.084 45.370 30.612 1.00 93.48 A O
ANISOU 3579 O GLY A 449 12853 2009 20656 -1354 11035 -2540 A O
ATOM 3580 N MET A 450 -9.184 47.020 31.887 1.00 96.31 A N
ANISOU 3580 N MET A 450 13266 1847 21482 -1962 11895 -3497 A N
ATOM 3581 CA MET A 450 -9.546 46.425 33.170 1.00 94.38 A C
ANISOU 3581 CA MET A 450 12900 1977 20982 -2016 11499 -3797 A C
ATOM 3582 C MET A 450 -11.047 46.557 33.475 1.00 98.46 A C
ANISOU 3582 C MET A 450 13552 2331 21526 -1656 11553 -3333 A C
ATOM 3583 O MET A 450 -11.680 47.521 33.036 1.00100.46 A O
ANISOU 3583 O MET A 450 14006 2060 22106 -1475 12116 -2987 A O
ATOM 3584 CB MET A 450 -8.683 46.980 34.311 1.00 99.86 A C
ANISOU 3584 CB MET A 450 13497 2668 21777 -2509 11767 -4633 A C
ATOM 3585 CG MET A 450 -7.216 46.521 34.229 1.00103.44 A C
ANISOU 3585 CG MET A 450 13724 3522 22057 -2854 11511 -5152 A C
ATOM 3586 SD MET A 450 -6.987 44.737 33.994 1.00101.94 A S
ANISOU 3586 SD MET A 450 13327 4096 21307 -2632 10542 -4946 A S
ATOM 3587 CE MET A 450 -7.202 44.188 35.613 1.00 97.51 A C
ANISOU 3587 CE MET A 450 12618 3993 20436 -2717 10164 -5378 A C
ATOM 3588 N PRO A 451 -11.625 45.544 34.185 1.00 93.00 A N
ANISOU 3588 N PRO A 451 12752 2106 20480 -1529 10967 -3297 A N
ATOM 3589 CA PRO A 451 -13.063 45.564 34.494 1.00 92.81 A C
ANISOU 3589 CA PRO A 451 12823 1997 20444 -1196 10967 -2871 A C
ATOM 3590 C PRO A 451 -13.498 46.782 35.311 1.00103.61 A C
ANISOU 3590 C PRO A 451 14327 2887 22151 -1294 11603 -3099 A C
ATOM 3591 O PRO A 451 -12.671 47.370 36.018 1.00106.22 A O
ANISOU 3591 O PRO A 451 14630 3101 22628 -1695 11901 -3742 A O
ATOM 3592 CB PRO A 451 -13.259 44.282 35.305 1.00 90.43 A C
ANISOU 3592 CB PRO A 451 12365 2291 19704 -1183 10265 -3002 A C
ATOM 3593 CG PRO A 451 -12.153 43.401 34.925 1.00 91.86 A C
ANISOU 3593 CG PRO A 451 12399 2870 19633 -1326 9823 -3192 A C
ATOM 3594 CD PRO A 451 -11.001 44.318 34.723 1.00 91.18 A C
ANISOU 3594 CD PRO A 451 12310 2502 19831 -1662 10293 -3624 A C
ATOM 3595 N PRO A 452 -14.793 47.175 35.228 1.00101.97 A N
ANISOU 3595 N PRO A 452 14257 2422 22064 -936 11831 -2594 A N
ATOM 3596 CA PRO A 452 -15.247 48.387 35.947 1.00106.62 A C
ANISOU 3596 CA PRO A 452 15005 2505 23002 -996 12494 -2776 A C
ATOM 3597 C PRO A 452 -15.124 48.309 37.473 1.00112.23 A C
ANISOU 3597 C PRO A 452 15624 3413 23607 -1302 12387 -3412 A C
ATOM 3598 O PRO A 452 -14.774 49.310 38.095 1.00116.28 A O
ANISOU 3598 O PRO A 452 16217 3559 24406 -1595 12943 -3890 A O
ATOM 3599 CB PRO A 452 -16.716 48.532 35.528 1.00108.12 A C
ANISOU 3599 CB PRO A 452 15307 2544 23231 -481 12594 -2043 A C
ATOM 3600 CG PRO A 452 -17.095 47.211 34.972 1.00107.51 A C
ANISOU 3600 CG PRO A 452 15078 3027 22744 -232 11859 -1624 A C
ATOM 3601 CD PRO A 452 -15.870 46.613 34.389 1.00100.81 A C
ANISOU 3601 CD PRO A 452 14124 2423 21756 -460 11550 -1835 A C
ATOM 3602 N VAL A 453 -15.390 47.132 38.063 1.00104.86 A N
ANISOU 3602 N VAL A 453 14529 3053 22261 -1243 11701 -3429 A N
ATOM 3603 CA VAL A 453 -15.334 46.887 39.508 1.00104.84 A C
ANISOU 3603 CA VAL A 453 14422 3334 22080 -1477 11512 -3973 A C
ATOM 3604 C VAL A 453 -14.419 45.670 39.789 1.00106.01 A C
ANISOU 3604 C VAL A 453 14348 4122 21807 -1657 10835 -4298 A C
ATOM 3605 O VAL A 453 -14.366 44.746 38.976 1.00102.58 A O
ANISOU 3605 O VAL A 453 13863 3963 21149 -1466 10382 -3923 A O
ATOM 3606 CB VAL A 453 -16.776 46.696 40.073 1.00107.76 A C
ANISOU 3606 CB VAL A 453 14843 3740 22360 -1162 11409 -3617 A C
ATOM 3607 CG1 VAL A 453 -17.600 45.726 39.221 1.00103.18 A C
ANISOU 3607 CG1 VAL A 453 14235 3443 21524 -754 10914 -2921 A C
ATOM 3608 CG2 VAL A 453 -16.783 46.288 41.552 1.00107.27 A C
ANISOU 3608 CG2 VAL A 453 14670 4021 22065 -1369 11161 -4131 A C
ATOM 3609 N GLN A 454 -13.687 45.695 40.921 1.00103.61 A N
ANISOU 3609 N GLN A 454 13914 4060 21394 -2017 10797 -4998 A N
ATOM 3610 CA GLN A 454 -12.810 44.605 41.342 1.00100.77 A C
ANISOU 3610 CA GLN A 454 13335 4335 20619 -2165 10200 -5347 A C
ATOM 3611 C GLN A 454 -13.490 43.775 42.441 1.00102.24 A C
ANISOU 3611 C GLN A 454 13458 4937 20453 -2043 9759 -5372 A C
ATOM 3612 O GLN A 454 -13.938 44.355 43.438 1.00103.92 A O
ANISOU 3612 O GLN A 454 13699 5028 20757 -2143 10030 -5642 A O
ATOM 3613 CB GLN A 454 -11.440 45.126 41.827 1.00105.22 A C
ANISOU 3613 CB GLN A 454 13749 4987 21242 -2640 10431 -6122 A C
ATOM 3614 CG GLN A 454 -10.424 44.007 42.089 1.00117.45 A C
ANISOU 3614 CG GLN A 454 15052 7219 22354 -2747 9828 -6436 A C
ATOM 3615 CD GLN A 454 -9.146 44.486 42.732 1.00137.48 A C
ANISOU 3615 CD GLN A 454 17386 9964 24886 -3213 10020 -7250 A C
ATOM 3616 NE2 GLN A 454 -8.287 45.133 41.955 1.00134.07 A N
ANISOU 3616 NE2 GLN A 454 16945 9275 24720 -3453 10389 -7434 A N
ATOM 3617 OE1 GLN A 454 -8.895 44.250 43.914 1.00131.09 A O
ANISOU 3617 OE1 GLN A 454 16409 9589 23810 -3364 9829 -7726 A O
ATOM 3618 N PRO A 455 -13.553 42.423 42.296 1.00 94.08 A N
ANISOU 3618 N PRO A 455 12348 4380 19016 -1840 9108 -5112 A N
ATOM 3619 CA PRO A 455 -14.153 41.596 43.361 1.00 91.88 A C
ANISOU 3619 CA PRO A 455 12027 4491 18393 -1728 8711 -5138 A C
ATOM 3620 C PRO A 455 -13.327 41.614 44.652 1.00 97.71 A C
ANISOU 3620 C PRO A 455 12593 5598 18932 -2028 8652 -5858 A C
ATOM 3621 O PRO A 455 -12.115 41.826 44.595 1.00100.47 A O
ANISOU 3621 O PRO A 455 12803 6086 19284 -2301 8718 -6315 A O
ATOM 3622 CB PRO A 455 -14.165 40.180 42.754 1.00 88.80 A C
ANISOU 3622 CB PRO A 455 11612 4483 17646 -1484 8095 -4735 A C
ATOM 3623 CG PRO A 455 -13.942 40.365 41.305 1.00 92.82 A C
ANISOU 3623 CG PRO A 455 12177 4734 18355 -1405 8207 -4376 A C
ATOM 3624 CD PRO A 455 -13.089 41.583 41.177 1.00 92.24 A C
ANISOU 3624 CD PRO A 455 12084 4338 18627 -1705 8735 -4788 A C
ATOM 3625 N LYS A 456 -13.977 41.371 45.809 1.00 92.46 A N
ANISOU 3625 N LYS A 456 11922 5137 18074 -1976 8521 -5961 A N
ATOM 3626 CA LYS A 456 -13.304 41.311 47.113 1.00 93.66 A C
ANISOU 3626 CA LYS A 456 11897 5719 17973 -2216 8426 -6612 A C
ATOM 3627 C LYS A 456 -12.516 39.991 47.241 1.00 94.01 A C
ANISOU 3627 C LYS A 456 11784 6400 17535 -2141 7815 -6682 A C
ATOM 3628 O LYS A 456 -13.113 38.917 47.136 1.00 89.23 A O
ANISOU 3628 O LYS A 456 11250 5988 16665 -1844 7391 -6242 A O
ATOM 3629 CB LYS A 456 -14.309 41.456 48.278 1.00 96.44 A C
ANISOU 3629 CB LYS A 456 12305 6079 18261 -2151 8488 -6651 A C
ATOM 3630 CG LYS A 456 -15.099 42.764 48.265 1.00116.75 A C
ANISOU 3630 CG LYS A 456 15035 8033 21294 -2200 9114 -6600 A C
ATOM 3631 CD LYS A 456 -15.676 43.140 49.637 1.00129.66 A C
ANISOU 3631 CD LYS A 456 16657 9730 22880 -2303 9284 -6957 A C
ATOM 3632 CE LYS A 456 -14.883 44.208 50.366 1.00138.68 A C
ANISOU 3632 CE LYS A 456 17701 10784 24207 -2736 9761 -7705 A C
ATOM 3633 NZ LYS A 456 -14.880 45.510 49.646 1.00148.58 A N1+
ANISOU 3633 NZ LYS A 456 19110 11342 26000 -2859 10431 -7673 A N1+
ATOM 3634 N TYR A 457 -11.178 40.079 47.430 1.00 92.11 A N
ANISOU 3634 N TYR A 457 11333 6481 17185 -2407 7796 -7229 A N
ATOM 3635 CA TYR A 457 -10.311 38.907 47.561 1.00 90.26 A C
ANISOU 3635 CA TYR A 457 10931 6871 16492 -2323 7260 -7329 A C
ATOM 3636 C TYR A 457 -9.669 38.776 48.930 1.00 98.18 A C
ANISOU 3636 C TYR A 457 11701 8460 17144 -2483 7127 -7949 A C
ATOM 3637 O TYR A 457 -9.372 39.784 49.572 1.00102.00 A O
ANISOU 3637 O TYR A 457 12076 8895 17786 -2810 7513 -8496 A O
ATOM 3638 CB TYR A 457 -9.155 38.937 46.540 1.00 91.54 A C
ANISOU 3638 CB TYR A 457 10990 7057 16735 -2448 7264 -7422 A C
ATOM 3639 CG TYR A 457 -9.519 39.162 45.098 1.00 91.41 A C
ANISOU 3639 CG TYR A 457 11159 6515 17055 -2331 7424 -6889 A C
ATOM 3640 CD1 TYR A 457 -10.030 38.129 44.319 1.00 88.51 A C
ANISOU 3640 CD1 TYR A 457 10919 6174 16536 -1993 7039 -6276 A C
ATOM 3641 CD2 TYR A 457 -9.222 40.364 44.472 1.00 95.50 A C
ANISOU 3641 CD2 TYR A 457 11711 6558 18016 -2573 7958 -7027 A C
ATOM 3642 CE1 TYR A 457 -10.309 38.315 42.969 1.00 86.45 A C
ANISOU 3642 CE1 TYR A 457 10798 5505 16545 -1886 7169 -5803 A C
ATOM 3643 CE2 TYR A 457 -9.486 40.559 43.123 1.00 95.24 A C
ANISOU 3643 CE2 TYR A 457 11837 6090 18261 -2441 8103 -6528 A C
ATOM 3644 CZ TYR A 457 -10.027 39.530 42.373 1.00 95.96 A C
ANISOU 3644 CZ TYR A 457 12029 6255 18175 -2094 7692 -5919 A C
ATOM 3645 OH TYR A 457 -10.282 39.731 41.044 1.00 94.09 A O
ANISOU 3645 OH TYR A 457 11925 5643 18183 -1964 7831 -5440 A O
ATOM 3646 N ASP A 458 -9.375 37.524 49.335 1.00 95.09 A N
ANISOU 3646 N ASP A 458 11225 8644 16261 -2255 6595 -7877 A N
ATOM 3647 CA ASP A 458 -8.591 37.229 50.532 1.00 98.72 A C
ANISOU 3647 CA ASP A 458 11426 9785 16299 -2342 6396 -8428 A C
ATOM 3648 C ASP A 458 -7.126 37.436 50.121 1.00108.07 A C
ANISOU 3648 C ASP A 458 12350 11263 17448 -2579 6416 -8873 A C
ATOM 3649 O ASP A 458 -6.727 36.953 49.063 1.00105.68 A O
ANISOU 3649 O ASP A 458 12083 10907 17164 -2458 6246 -8577 A O
ATOM 3650 CB ASP A 458 -8.871 35.812 51.063 1.00 98.18 A C
ANISOU 3650 CB ASP A 458 11399 10178 15725 -1959 5863 -8117 A C
ATOM 3651 CG ASP A 458 -7.892 35.353 52.133 1.00114.86 A C
ANISOU 3651 CG ASP A 458 13226 13084 17334 -1966 5598 -8614 A C
ATOM 3652 OD1 ASP A 458 -8.019 35.811 53.291 1.00118.10 A O
ANISOU 3652 OD1 ASP A 458 13513 13722 17639 -2119 5736 -9043 A O
ATOM 3653 OD2 ASP A 458 -6.995 34.544 51.809 1.00124.34 A O1-
ANISOU 3653 OD2 ASP A 458 14318 14696 18229 -1802 5258 -8568 A O1-
ATOM 3654 N MET A 459 -6.353 38.202 50.905 1.00111.94 A N
ANISOU 3654 N MET A 459 12578 12046 17909 -2939 6654 -9595 A N
ATOM 3655 CA MET A 459 -4.967 38.585 50.575 1.00115.97 A C
ANISOU 3655 CA MET A 459 12807 12835 18423 -3245 6756 -10113 A C
ATOM 3656 C MET A 459 -3.902 37.801 51.352 1.00120.89 A C
ANISOU 3656 C MET A 459 13086 14387 18459 -3180 6336 -10507 A C
ATOM 3657 O MET A 459 -2.715 38.126 51.233 1.00121.76 A O
ANISOU 3657 O MET A 459 12906 14842 18518 -3449 6408 -11010 A O
ATOM 3658 CB MET A 459 -4.771 40.094 50.861 1.00123.98 A C
ANISOU 3658 CB MET A 459 13736 13551 19819 -3753 7375 -10723 A C
ATOM 3659 CG MET A 459 -5.813 41.000 50.223 1.00127.96 A C
ANISOU 3659 CG MET A 459 14573 13144 20901 -3805 7866 -10375 A C
ATOM 3660 SD MET A 459 -5.511 41.259 48.462 1.00131.30 A S
ANISOU 3660 SD MET A 459 15149 12997 21740 -3809 8056 -9973 A S
ATOM 3661 CE MET A 459 -6.926 42.278 48.063 1.00128.08 A C
ANISOU 3661 CE MET A 459 15118 11636 21910 -3784 8620 -9561 A C
ATOM 3662 N THR A 460 -4.318 36.786 52.143 1.00117.56 A N
ANISOU 3662 N THR A 460 12692 14383 17592 -2818 5921 -10279 A N
ATOM 3663 CA THR A 460 -3.442 35.972 52.999 1.00119.61 A C
ANISOU 3663 CA THR A 460 12650 15555 17241 -2664 5517 -10580 A C
ATOM 3664 C THR A 460 -2.200 35.447 52.239 1.00121.97 A C
ANISOU 3664 C THR A 460 12749 16233 17363 -2604 5280 -10628 A C
ATOM 3665 O THR A 460 -1.078 35.690 52.688 1.00125.90 A O
ANISOU 3665 O THR A 460 12862 17359 17614 -2811 5270 -11236 A O
ATOM 3666 CB THR A 460 -4.230 34.806 53.649 1.00130.24 A C
ANISOU 3666 CB THR A 460 14175 17116 18195 -2191 5119 -10109 A C
ATOM 3667 CG2 THR A 460 -3.404 34.032 54.672 1.00133.29 A C
ANISOU 3667 CG2 THR A 460 14261 18456 17928 -1994 4749 -10412 A C
ATOM 3668 OG1 THR A 460 -5.407 35.311 54.282 1.00130.62 A O
ANISOU 3668 OG1 THR A 460 14409 16789 18430 -2252 5351 -10049 A O
ATOM 3669 N LEU A 461 -2.397 34.763 51.100 1.00112.84 A N
ANISOU 3669 N LEU A 461 11831 14720 16324 -2338 5104 -10016 A N
ATOM 3670 CA LEU A 461 -1.294 34.172 50.337 1.00111.26 A C
ANISOU 3670 CA LEU A 461 11475 14848 15952 -2236 4866 -9998 A C
ATOM 3671 C LEU A 461 -0.588 35.167 49.405 1.00114.95 A C
ANISOU 3671 C LEU A 461 11828 15008 16839 -2645 5228 -10295 A C
ATOM 3672 O LEU A 461 0.583 34.957 49.072 1.00116.74 A O
ANISOU 3672 O LEU A 461 11796 15668 16891 -2687 5099 -10538 A O
ATOM 3673 CB LEU A 461 -1.797 32.970 49.522 1.00106.30 A C
ANISOU 3673 CB LEU A 461 11156 13992 15242 -1779 4525 -9235 A C
ATOM 3674 CG LEU A 461 -2.234 31.740 50.332 1.00109.58 A C
ANISOU 3674 CG LEU A 461 11669 14803 15161 -1327 4123 -8929 A C
ATOM 3675 CD1 LEU A 461 -3.172 30.852 49.531 1.00104.84 A C
ANISOU 3675 CD1 LEU A 461 11472 13711 14650 -995 3954 -8168 A C
ATOM 3676 CD2 LEU A 461 -1.027 30.943 50.817 1.00114.39 A C
ANISOU 3676 CD2 LEU A 461 11974 16275 15214 -1112 3782 -9181 A C
ATOM 3677 N ALA A 462 -1.286 36.238 48.992 1.00108.78 A N
ANISOU 3677 N ALA A 462 11241 13493 16599 -2931 5695 -10268 A N
ATOM 3678 CA ALA A 462 -0.760 37.229 48.055 1.00109.14 A C
ANISOU 3678 CA ALA A 462 11249 13127 17094 -3307 6109 -10481 A C
ATOM 3679 C ALA A 462 0.150 38.275 48.687 1.00117.60 A C
ANISOU 3679 C ALA A 462 11974 14500 18210 -3823 6465 -11342 A C
ATOM 3680 O ALA A 462 1.065 38.751 48.007 1.00119.15 A O
ANISOU 3680 O ALA A 462 12016 14668 18587 -4109 6675 -11629 A O
ATOM 3681 CB ALA A 462 -1.907 37.931 47.367 1.00107.77 A C
ANISOU 3681 CB ALA A 462 11448 12037 17463 -3343 6485 -10044 A C
ATOM 3682 N ASN A 463 -0.119 38.671 49.953 1.00115.91 A N
ANISOU 3682 N ASN A 463 11640 14554 17846 -3968 6564 -11766 A N
ATOM 3683 CA ASN A 463 0.615 39.717 50.676 1.00120.82 A C
ANISOU 3683 CA ASN A 463 11937 15465 18504 -4499 6939 -12634 A C
ATOM 3684 C ASN A 463 2.148 39.573 50.569 1.00127.16 A C
ANISOU 3684 C ASN A 463 12300 16992 19023 -4689 6805 -13166 A C
ATOM 3685 O ASN A 463 2.822 40.559 50.274 1.00129.67 A O
ANISOU 3685 O ASN A 463 12460 17180 19628 -5182 7240 -13690 A O
ATOM 3686 CB ASN A 463 0.180 39.779 52.145 1.00123.36 A C
ANISOU 3686 CB ASN A 463 12151 16188 18533 -4514 6897 -12966 A C
ATOM 3687 CG ASN A 463 -1.108 40.542 52.391 1.00144.73 A C
ANISOU 3687 CG ASN A 463 15189 18154 21647 -4602 7294 -12799 A C
ATOM 3688 ND2 ASN A 463 -1.764 40.241 53.503 1.00137.08 A N
ANISOU 3688 ND2 ASN A 463 14238 17450 20396 -4425 7124 -12790 A N
ATOM 3689 OD1 ASN A 463 -1.519 41.417 51.614 1.00136.11 A O
ANISOU 3689 OD1 ASN A 463 14336 16266 21114 -4813 7771 -12679 A O
ATOM 3690 N ALA A 464 2.683 38.350 50.737 1.00122.88 A N
ANISOU 3690 N ALA A 464 11579 17173 17938 -4290 6234 -13002 A N
ATOM 3691 CA ALA A 464 4.120 38.071 50.647 1.00125.12 A C
ANISOU 3691 CA ALA A 464 11428 18223 17890 -4383 6048 -13444 A C
ATOM 3692 C ALA A 464 4.672 38.318 49.232 1.00127.62 A C
ANISOU 3692 C ALA A 464 11808 18108 18573 -4525 6220 -13296 A C
ATOM 3693 O ALA A 464 5.817 38.771 49.109 1.00131.30 A O
ANISOU 3693 O ALA A 464 11915 18966 19007 -4881 6366 -13878 A O
ATOM 3694 CB ALA A 464 4.405 36.640 51.076 1.00124.19 A C
ANISOU 3694 CB ALA A 464 11181 18878 17127 -3826 5415 -13168 A C
ATOM 3695 N CYS A 465 3.854 38.053 48.181 1.00118.21 A N
ANISOU 3695 N CYS A 465 11056 16133 17724 -4268 6222 -12545 A N
ATOM 3696 CA CYS A 465 4.221 38.217 46.767 1.00115.75 A C
ANISOU 3696 CA CYS A 465 10861 15355 17762 -4341 6372 -12293 A C
ATOM 3697 C CYS A 465 4.332 39.696 46.383 1.00121.64 A C
ANISOU 3697 C CYS A 465 11633 15516 19069 -4916 7050 -12700 A C
ATOM 3698 O CYS A 465 5.291 40.076 45.703 1.00123.96 A O
ANISOU 3698 O CYS A 465 11746 15861 19495 -5200 7236 -12997 A O
ATOM 3699 CB CYS A 465 3.229 37.497 45.857 1.00110.26 A C
ANISOU 3699 CB CYS A 465 10611 14061 17221 -3890 6170 -11387 A C
ATOM 3700 SG CYS A 465 2.910 35.770 46.298 1.00110.33 A S
ANISOU 3700 SG CYS A 465 10688 14602 16631 -3223 5459 -10857 A S
ATOM 3701 N ILE A 466 3.328 40.511 46.785 1.00116.83 A N
ANISOU 3701 N ILE A 466 11270 14323 18799 -5072 7441 -12687 A N
ATOM 3702 CA ILE A 466 3.239 41.954 46.505 1.00118.99 A C
ANISOU 3702 CA ILE A 466 11646 13928 19637 -5580 8157 -13017 A C
ATOM 3703 C ILE A 466 4.425 42.690 47.162 1.00125.73 A C
ANISOU 3703 C ILE A 466 12175 15326 20270 -5995 8243 -13723 A C
ATOM 3704 O ILE A 466 5.023 43.573 46.536 1.00125.00 A O
ANISOU 3704 O ILE A 466 12230 14916 20348 -6174 8410 -13608 A O
ATOM 3705 CB ILE A 466 1.862 42.526 46.967 1.00121.20 A C
ANISOU 3705 CB ILE A 466 12280 13546 20227 -5543 8467 -12766 A C
ATOM 3706 CG1 ILE A 466 0.685 41.693 46.410 1.00115.38 A C
ANISOU 3706 CG1 ILE A 466 11924 12411 19504 -4971 8132 -11824 A C
ATOM 3707 CG2 ILE A 466 1.701 44.011 46.591 1.00124.72 A C
ANISOU 3707 CG2 ILE A 466 12925 13201 21263 -5969 9208 -12947 A C
ATOM 3708 CD1 ILE A 466 -0.562 41.652 47.307 1.00122.83 A C
ANISOU 3708 CD1 ILE A 466 13072 13174 20423 -4778 8112 -11604 A C
ATOM 3709 N THR A 467 4.773 42.291 48.405 1.00123.52 A N
ANISOU 3709 N THR A 467 11560 15890 19482 -5983 7937 -14169 A N
ATOM 3710 CA THR A 467 5.863 42.864 49.212 1.00123.58 A C
ANISOU 3710 CA THR A 467 11455 16489 19012 -6057 7639 -14322 A C
ATOM 3711 C THR A 467 7.235 42.634 48.538 1.00123.18 A C
ANISOU 3711 C THR A 467 11161 16871 18770 -6101 7433 -14403 A C
ATOM 3712 O THR A 467 7.931 43.604 48.242 1.00121.64 A O
ANISOU 3712 O THR A 467 11067 16478 18672 -6332 7565 -14391 A O
ATOM 3713 CB THR A 467 5.829 42.305 50.650 1.00133.60 A C
ANISOU 3713 CB THR A 467 12829 18431 19502 -5510 6870 -13852 A C
ATOM 3714 CG2 THR A 467 4.738 42.909 51.461 1.00132.09 A C
ANISOU 3714 CG2 THR A 467 12828 17884 19477 -5600 7133 -13932 A C
ATOM 3715 OG1 THR A 467 5.601 40.898 50.634 1.00140.04 A O
ANISOU 3715 OG1 THR A 467 13564 19647 19999 -5057 6433 -13559 A O
ATOM 3716 N LEU A 468 7.586 41.366 48.251 1.00120.60 A N
ANISOU 3716 N LEU A 468 10387 17160 18275 -6012 7274 -14757 A N
ATOM 3717 CA LEU A 468 8.853 40.983 47.611 1.00120.29 A C
ANISOU 3717 CA LEU A 468 10080 17606 18019 -5999 7046 -14834 A C
ATOM 3718 C LEU A 468 9.077 41.703 46.263 1.00121.18 A C
ANISOU 3718 C LEU A 468 10463 16947 18632 -6194 7381 -14547 A C
ATOM 3719 O LEU A 468 10.159 42.265 46.054 1.00120.91 A O
ANISOU 3719 O LEU A 468 10390 17079 18472 -6326 7303 -14544 A O
ATOM 3720 CB LEU A 468 8.930 39.458 47.440 1.00119.72 A C
ANISOU 3720 CB LEU A 468 9678 18176 17636 -5639 6667 -14890 A C
ATOM 3721 CG LEU A 468 10.262 38.857 46.946 1.00124.03 A C
ANISOU 3721 CG LEU A 468 10011 19319 17797 -5431 6250 -14753 A C
ATOM 3722 CD1 LEU A 468 11.466 39.385 47.727 1.00125.05 A C
ANISOU 3722 CD1 LEU A 468 10079 19996 17440 -5438 5947 -14720 A C
ATOM 3723 CD2 LEU A 468 10.216 37.350 47.007 1.00125.15 A C
ANISOU 3723 CD2 LEU A 468 10024 20025 17501 -4861 5718 -14473 A C
ATOM 3724 N GLY A 469 8.051 41.725 45.410 1.00117.66 A N
ANISOU 3724 N GLY A 469 10174 15693 18837 -6344 7919 -14559 A N
ATOM 3725 CA GLY A 469 8.095 42.397 44.113 1.00117.23 A C
ANISOU 3725 CA GLY A 469 10384 14840 19316 -6529 8338 -14305 A C
ATOM 3726 C GLY A 469 8.403 43.876 44.224 1.00121.40 A C
ANISOU 3726 C GLY A 469 11316 14965 19848 -6615 8363 -13904 A C
ATOM 3727 O GLY A 469 9.269 44.389 43.505 1.00121.55 A O
ANISOU 3727 O GLY A 469 11365 14906 19915 -6742 8395 -13812 A O
ATOM 3728 N GLN A 470 7.720 44.563 45.159 1.00119.14 A N
ANISOU 3728 N GLN A 470 11175 14465 19626 -6727 8558 -14027 A N
ATOM 3729 CA GLN A 470 7.922 45.977 45.437 1.00119.42 A C
ANISOU 3729 CA GLN A 470 11507 14157 19709 -6881 8674 -13864 A C
ATOM 3730 C GLN A 470 9.363 46.203 45.886 1.00123.80 A C
ANISOU 3730 C GLN A 470 11954 15395 19690 -6797 8105 -13757 A C
ATOM 3731 O GLN A 470 10.031 47.095 45.358 1.00123.60 A O
ANISOU 3731 O GLN A 470 12064 15110 19787 -6961 8212 -13633 A O
ATOM 3732 CB GLN A 470 6.922 46.460 46.512 1.00120.61 A C
ANISOU 3732 CB GLN A 470 11886 14113 19828 -6799 8699 -13780 A C
ATOM 3733 CG GLN A 470 6.366 47.854 46.254 1.00125.07 A C
ANISOU 3733 CG GLN A 470 13062 13873 20586 -6636 8736 -13034 A C
ATOM 3734 CD GLN A 470 7.110 48.963 46.957 1.00138.76 A C
ANISOU 3734 CD GLN A 470 15190 15820 21714 -6238 7911 -12214 A C
ATOM 3735 NE2 GLN A 470 6.585 50.175 46.846 1.00132.58 A N
ANISOU 3735 NE2 GLN A 470 14607 14380 21386 -6544 8490 -12386 A N
ATOM 3736 OE1 GLN A 470 8.142 48.759 47.610 1.00137.11 A O
ANISOU 3736 OE1 GLN A 470 14679 16265 21151 -6363 7691 -12590 A O
ATOM 3737 N LYS A 471 9.863 45.352 46.816 1.00123.02 A N
ANISOU 3737 N LYS A 471 11473 16183 19085 -6703 7721 -14097 A N
ATOM 3738 CA LYS A 471 11.229 45.445 47.343 1.00124.11 A C
ANISOU 3738 CA LYS A 471 11414 17019 18725 -6683 7301 -14158 A C
ATOM 3739 C LYS A 471 12.245 45.384 46.211 1.00127.52 A C
ANISOU 3739 C LYS A 471 11845 17450 19159 -6632 7152 -13860 A C
ATOM 3740 O LYS A 471 13.179 46.180 46.211 1.00127.74 A O
ANISOU 3740 O LYS A 471 11907 17533 19095 -6768 7082 -13813 A O
ATOM 3741 CB LYS A 471 11.506 44.345 48.386 1.00126.85 A C
ANISOU 3741 CB LYS A 471 11499 18247 18449 -6337 6749 -14186 A C
ATOM 3742 CG LYS A 471 10.939 44.667 49.771 1.00141.92 A C
ANISOU 3742 CG LYS A 471 14121 19974 19827 -5599 5977 -12956 A C
ATOM 3743 CD LYS A 471 11.165 43.542 50.782 1.00150.16 A C
ANISOU 3743 CD LYS A 471 15293 21593 20167 -4922 5196 -12282 A C
ATOM 3744 CE LYS A 471 10.737 43.946 52.178 1.00155.68 A C
ANISOU 3744 CE LYS A 471 16510 22144 20498 -4466 4733 -11519 A C
ATOM 3745 NZ LYS A 471 10.935 42.849 53.163 1.00160.61 A N1+
ANISOU 3745 NZ LYS A 471 17270 23216 20538 -3898 4144 -10949 A N1+
ATOM 3746 N TRP A 472 12.018 44.498 45.212 1.00125.01 A N
ANISOU 3746 N TRP A 472 11334 17080 19084 -6647 7343 -14021 A N
ATOM 3747 CA TRP A 472 12.917 44.336 44.073 1.00125.01 A C
ANISOU 3747 CA TRP A 472 11223 17116 19159 -6703 7341 -13961 A C
ATOM 3748 C TRP A 472 12.899 45.528 43.094 1.00127.01 A C
ANISOU 3748 C TRP A 472 11925 16525 19809 -6801 7590 -13464 A C
ATOM 3749 O TRP A 472 13.966 45.893 42.598 1.00126.53 A O
ANISOU 3749 O TRP A 472 11791 16586 19698 -6924 7543 -13453 A O
ATOM 3750 CB TRP A 472 12.628 43.030 43.319 1.00124.01 A C
ANISOU 3750 CB TRP A 472 10843 17144 19132 -6575 7366 -14111 A C
ATOM 3751 CG TRP A 472 13.408 41.856 43.840 1.00125.34 A C
ANISOU 3751 CG TRP A 472 10603 18315 18704 -6292 6829 -14268 A C
ATOM 3752 CD1 TRP A 472 12.916 40.783 44.527 1.00127.46 A C
ANISOU 3752 CD1 TRP A 472 10734 19049 18647 -5950 6506 -14273 A C
ATOM 3753 CD2 TRP A 472 14.832 41.670 43.767 1.00125.70 A C
ANISOU 3753 CD2 TRP A 472 10396 19003 18362 -6241 6498 -14298 A C
ATOM 3754 CE2 TRP A 472 15.126 40.443 44.401 1.00128.75 A C
ANISOU 3754 CE2 TRP A 472 10539 20195 18184 -5808 5965 -14236 A C
ATOM 3755 CE3 TRP A 472 15.888 42.409 43.196 1.00126.77 A C
ANISOU 3755 CE3 TRP A 472 10608 19033 18526 -6388 6497 -14120 A C
ATOM 3756 NE1 TRP A 472 13.942 39.935 44.877 1.00127.60 A N
ANISOU 3756 NE1 TRP A 472 10382 19990 18108 -5715 6047 -14393 A N
ATOM 3757 CZ2 TRP A 472 16.434 39.958 44.521 1.00128.89 A C
ANISOU 3757 CZ2 TRP A 472 10263 20973 17737 -5648 5584 -14259 A C
ATOM 3758 CZ3 TRP A 472 17.182 41.920 43.302 1.00128.38 A C
ANISOU 3758 CZ3 TRP A 472 10557 19954 18268 -6210 6074 -14071 A C
ATOM 3759 CH2 TRP A 472 17.446 40.713 43.964 1.00129.27 A C
ANISOU 3759 CH2 TRP A 472 10370 20880 17866 -5845 5637 -14138 A C
ATOM 3760 N VAL A 473 11.717 46.119 42.805 1.00124.46 A N
ANISOU 3760 N VAL A 473 11914 15402 19974 -6908 8055 -13364 A N
ATOM 3761 CA VAL A 473 11.617 47.256 41.871 1.00124.16 A C
ANISOU 3761 CA VAL A 473 12238 14582 20354 -7047 8408 -13030 A C
ATOM 3762 C VAL A 473 12.118 48.571 42.513 1.00126.01 A C
ANISOU 3762 C VAL A 473 12730 14766 20382 -7055 8190 -12758 A C
ATOM 3763 O VAL A 473 12.539 49.476 41.786 1.00125.25 A O
ANISOU 3763 O VAL A 473 12804 14281 20505 -7211 8386 -12600 A O
ATOM 3764 CB VAL A 473 10.207 47.459 41.239 1.00126.48 A C
ANISOU 3764 CB VAL A 473 12938 14019 21100 -6889 8726 -12573 A C
ATOM 3765 CG1 VAL A 473 9.870 46.351 40.268 1.00125.88 A C
ANISOU 3765 CG1 VAL A 473 12736 13842 21252 -6795 8860 -12564 A C
ATOM 3766 CG2 VAL A 473 9.111 47.621 42.284 1.00126.50 A C
ANISOU 3766 CG2 VAL A 473 13080 13876 21110 -6811 8781 -12601 A C
ATOM 3767 N LYS A 474 12.065 48.681 43.853 1.00123.71 A N
ANISOU 3767 N LYS A 474 12345 14855 19806 -7074 8026 -13022 A N
ATOM 3768 CA LYS A 474 12.495 49.900 44.543 1.00123.97 A C
ANISOU 3768 CA LYS A 474 12556 14835 19713 -7166 7929 -12942 A C
ATOM 3769 C LYS A 474 13.906 49.762 45.150 1.00127.35 A C
ANISOU 3769 C LYS A 474 12813 15997 19578 -7020 7320 -12832 A C
ATOM 3770 O LYS A 474 14.409 50.719 45.751 1.00127.52 A O
ANISOU 3770 O LYS A 474 12937 16026 19487 -7113 7225 -12808 A O
ATOM 3771 CB LYS A 474 11.468 50.324 45.610 1.00125.70 A C
ANISOU 3771 CB LYS A 474 13013 14861 19886 -7033 7897 -12832 A C
ATOM 3772 CG LYS A 474 10.155 50.835 45.014 1.00133.45 A C
ANISOU 3772 CG LYS A 474 14596 15040 21066 -6574 7774 -11875 A C
ATOM 3773 CD LYS A 474 9.462 51.859 45.898 1.00140.61 A C
ANISOU 3773 CD LYS A 474 15969 15681 21774 -6217 7386 -11239 A C
ATOM 3774 CE LYS A 474 9.473 53.246 45.304 1.00144.17 A C
ANISOU 3774 CE LYS A 474 16857 15644 22279 -6019 7171 -10529 A C
ATOM 3775 NZ LYS A 474 9.021 54.268 46.285 1.00147.23 A N1+
ANISOU 3775 NZ LYS A 474 17559 15878 22502 -5805 6892 -10189 A N1+
ATOM 3776 N ALA A 475 14.567 48.608 44.938 1.00124.97 A N
ANISOU 3776 N ALA A 475 12121 16301 19060 -6990 7161 -13090 A N
ATOM 3777 CA ALA A 475 15.919 48.380 45.448 1.00125.50 A C
ANISOU 3777 CA ALA A 475 11931 17077 18678 -6948 6752 -13169 A C
ATOM 3778 C ALA A 475 16.967 49.084 44.601 1.00127.79 A C
ANISOU 3778 C ALA A 475 12345 17185 19025 -6987 6660 -12821 A C
ATOM 3779 O ALA A 475 16.860 49.111 43.373 1.00126.86 A O
ANISOU 3779 O ALA A 475 12285 16672 19244 -7082 6935 -12741 A O
ATOM 3780 CB ALA A 475 16.224 46.892 45.496 1.00126.18 A C
ANISOU 3780 CB ALA A 475 11668 17842 18432 -6714 6454 -13286 A C
ATOM 3781 N THR A 476 17.992 49.638 45.256 1.00125.96 A N
ANISOU 3781 N THR A 476 11999 17302 18557 -7113 6491 -12961 A N
ATOM 3782 CA THR A 476 19.129 50.260 44.578 1.00125.89 A C
ANISOU 3782 CA THR A 476 11984 17251 18600 -7255 6468 -12844 A C
ATOM 3783 C THR A 476 20.259 49.213 44.572 1.00128.45 A C
ANISOU 3783 C THR A 476 12018 18275 18512 -7018 6021 -12745 A C
ATOM 3784 O THR A 476 19.996 48.049 44.893 1.00128.07 A O
ANISOU 3784 O THR A 476 11748 18679 18235 -6832 5874 -12897 A O
ATOM 3785 CB THR A 476 19.508 51.600 45.248 1.00132.10 A C
ANISOU 3785 CB THR A 476 13163 17762 19267 -7122 6152 -12318 A C
ATOM 3786 CG2 THR A 476 18.478 52.698 44.999 1.00129.65 A C
ANISOU 3786 CG2 THR A 476 13188 16709 19366 -7285 6545 -12269 A C
ATOM 3787 OG1 THR A 476 19.691 51.398 46.650 1.00133.29 A O
ANISOU 3787 OG1 THR A 476 13231 18374 19041 -6999 5848 -12416 A O
ATOM 3788 N GLU A 477 21.499 49.599 44.202 1.00126.08 A N
ANISOU 3788 N GLU A 477 11560 18154 18193 -7213 6012 -12842 A N
ATOM 3789 CA GLU A 477 22.634 48.672 44.230 1.00126.08 A C
ANISOU 3789 CA GLU A 477 11212 18851 17841 -7081 5694 -12904 A C
ATOM 3790 C GLU A 477 23.038 48.384 45.690 1.00128.60 A C
ANISOU 3790 C GLU A 477 11484 19688 17688 -6832 5249 -12810 A C
ATOM 3791 O GLU A 477 23.479 47.272 45.989 1.00128.58 A O
ANISOU 3791 O GLU A 477 11195 20309 17349 -6628 4990 -12890 A O
ATOM 3792 CB GLU A 477 23.824 49.211 43.417 1.00127.36 A C
ANISOU 3792 CB GLU A 477 11381 18933 18078 -7179 5651 -12693 A C
ATOM 3793 CG GLU A 477 23.712 48.918 41.929 1.00133.23 A C
ANISOU 3793 CG GLU A 477 12376 19221 19023 -6927 5604 -12079 A C
ATOM 3794 CD GLU A 477 24.934 49.280 41.107 1.00143.78 A C
ANISOU 3794 CD GLU A 477 14077 20336 20216 -6470 5031 -10979 A C
ATOM 3795 OE1 GLU A 477 25.180 50.490 40.900 1.00139.54 A O
ANISOU 3795 OE1 GLU A 477 13574 19514 19931 -6848 5323 -11193 A O
ATOM 3796 OE2 GLU A 477 25.632 48.349 40.646 1.00137.13 A O1-
ANISOU 3796 OE2 GLU A 477 12832 19984 19286 -6548 5085 -11334 A O1-
ATOM 3797 N SER A 478 22.833 49.374 46.595 1.00125.69 A N
ANISOU 3797 N SER A 478 11235 19164 17356 -7035 5357 -12993 A N
ATOM 3798 CA SER A 478 23.117 49.297 48.029 1.00125.91 A C
ANISOU 3798 CA SER A 478 11199 19636 17007 -6918 5063 -13057 A C
ATOM 3799 C SER A 478 22.160 48.342 48.788 1.00128.07 A C
ANISOU 3799 C SER A 478 11473 20136 17053 -6611 4910 -13025 A C
ATOM 3800 O SER A 478 22.547 47.817 49.835 1.00129.11 A O
ANISOU 3800 O SER A 478 11461 20809 16785 -6417 4602 -13044 A O
ATOM 3801 CB SER A 478 23.057 50.694 48.646 1.00128.24 A C
ANISOU 3801 CB SER A 478 11862 19464 17399 -6989 5042 -12820 A C
ATOM 3802 OG SER A 478 22.764 50.677 50.033 1.00134.98 A O
ANISOU 3802 OG SER A 478 12995 20360 17931 -6600 4625 -12395 A O
ATOM 3803 N ASP A 479 20.923 48.146 48.292 1.00123.52 A N
ANISOU 3803 N ASP A 479 10889 19261 16783 -6762 5306 -13324 A N
ATOM 3804 CA ASP A 479 19.906 47.293 48.927 1.00122.78 A C
ANISOU 3804 CA ASP A 479 10725 19379 16547 -6580 5279 -13467 A C
ATOM 3805 C ASP A 479 20.023 45.809 48.530 1.00124.12 A C
ANISOU 3805 C ASP A 479 10647 20024 16488 -6273 5054 -13403 A C
ATOM 3806 O ASP A 479 19.472 44.945 49.216 1.00122.92 A O
ANISOU 3806 O ASP A 479 10350 20257 16096 -6084 4939 -13554 A O
ATOM 3807 CB ASP A 479 18.502 47.797 48.563 1.00123.40 A C
ANISOU 3807 CB ASP A 479 11122 18728 17039 -6650 5621 -13382 A C
ATOM 3808 CG ASP A 479 18.145 49.158 49.123 1.00131.17 A C
ANISOU 3808 CG ASP A 479 12685 19060 18094 -6505 5474 -12764 A C
ATOM 3809 OD1 ASP A 479 17.919 49.252 50.348 1.00132.33 A O
ANISOU 3809 OD1 ASP A 479 12898 19390 17992 -6391 5291 -12760 A O
ATOM 3810 OD2 ASP A 479 17.993 50.107 48.322 1.00134.53 A O1-
ANISOU 3810 OD2 ASP A 479 13444 18829 18841 -6543 5598 -12392 A O1-
ATOM 3811 N LEU A 480 20.743 45.518 47.430 1.00121.77 A N
ANISOU 3811 N LEU A 480 10115 19851 16302 -6397 5151 -13540 A N
ATOM 3812 CA LEU A 480 20.927 44.169 46.883 1.00121.50 A C
ANISOU 3812 CA LEU A 480 9780 20285 16098 -6173 5008 -13602 A C
ATOM 3813 C LEU A 480 21.415 43.164 47.931 1.00125.09 A C
ANISOU 3813 C LEU A 480 10093 21455 15982 -5748 4510 -13422 A C
ATOM 3814 O LEU A 480 20.986 42.013 47.895 1.00124.64 A O
ANISOU 3814 O LEU A 480 9842 21755 15760 -5507 4412 -13516 A O
ATOM 3815 CB LEU A 480 21.882 44.178 45.680 1.00121.33 A C
ANISOU 3815 CB LEU A 480 9657 20237 16208 -6261 5045 -13522 A C
ATOM 3816 CG LEU A 480 21.393 44.887 44.416 1.00123.89 A C
ANISOU 3816 CG LEU A 480 10321 19715 17038 -6403 5354 -13231 A C
ATOM 3817 CD1 LEU A 480 22.492 44.954 43.377 1.00124.04 A C
ANISOU 3817 CD1 LEU A 480 10239 19771 17121 -6481 5344 -13129 A C
ATOM 3818 CD2 LEU A 480 20.169 44.200 43.825 1.00125.55 A C
ANISOU 3818 CD2 LEU A 480 10631 19611 17462 -6250 5493 -13144 A C
ATOM 3819 N GLY A 481 22.255 43.621 48.863 1.00123.49 A N
ANISOU 3819 N GLY A 481 9793 21602 15523 -5828 4358 -13529 A N
ATOM 3820 CA GLY A 481 22.800 42.811 49.948 1.00124.13 A C
ANISOU 3820 CA GLY A 481 9692 22387 15085 -5515 3969 -13478 A C
ATOM 3821 C GLY A 481 21.786 42.343 50.976 1.00126.72 A C
ANISOU 3821 C GLY A 481 10168 22771 15208 -5240 3833 -13357 A C
ATOM 3822 O GLY A 481 22.035 41.361 51.683 1.00126.67 A O
ANISOU 3822 O GLY A 481 9973 23378 14779 -4925 3544 -13332 A O
ATOM 3823 N SER A 482 20.638 43.040 51.071 1.00124.17 A N
ANISOU 3823 N SER A 482 9981 22004 15192 -5506 4172 -13621 A N
ATOM 3824 CA SER A 482 19.559 42.721 52.009 1.00124.01 A C
ANISOU 3824 CA SER A 482 10025 22055 15038 -5363 4153 -13694 A C
ATOM 3825 C SER A 482 18.796 41.454 51.593 1.00126.09 A C
ANISOU 3825 C SER A 482 10223 22440 15247 -5039 4077 -13591 A C
ATOM 3826 O SER A 482 18.278 40.753 52.464 1.00126.28 A O
ANISOU 3826 O SER A 482 10184 22821 14976 -4792 3918 -13621 A O
ATOM 3827 CB SER A 482 18.590 43.895 52.135 1.00126.02 A C
ANISOU 3827 CB SER A 482 10708 21513 15661 -5550 4408 -13553 A C
ATOM 3828 OG SER A 482 19.240 45.072 52.587 1.00133.44 A O
ANISOU 3828 OG SER A 482 12110 22004 16586 -5477 4182 -12946 A O
ATOM 3829 N PHE A 483 18.720 41.169 50.275 1.00122.73 A N
ANISOU 3829 N PHE A 483 9599 21913 15119 -5197 4318 -13837 A N
ATOM 3830 CA PHE A 483 18.011 40.007 49.728 1.00122.19 A C
ANISOU 3830 CA PHE A 483 9357 22011 15060 -4983 4321 -13937 A C
ATOM 3831 C PHE A 483 18.764 38.707 50.005 1.00126.34 A C
ANISOU 3831 C PHE A 483 9742 23211 15050 -4453 3823 -13592 A C
ATOM 3832 O PHE A 483 19.987 38.659 49.870 1.00126.46 A O
ANISOU 3832 O PHE A 483 9633 23537 14877 -4414 3646 -13493 A O
ATOM 3833 CB PHE A 483 17.768 40.166 48.220 1.00122.37 A C
ANISOU 3833 CB PHE A 483 9454 21467 15575 -5168 4620 -13918 A C
ATOM 3834 CG PHE A 483 16.857 41.313 47.840 1.00122.58 A C
ANISOU 3834 CG PHE A 483 9836 20592 16147 -5496 5047 -13887 A C
ATOM 3835 CD1 PHE A 483 15.475 41.150 47.818 1.00123.92 A C
ANISOU 3835 CD1 PHE A 483 10197 20327 16562 -5430 5218 -13828 A C
ATOM 3836 CD2 PHE A 483 17.380 42.548 47.480 1.00123.60 A C
ANISOU 3836 CD2 PHE A 483 10217 20222 16523 -5758 5201 -13706 A C
ATOM 3837 CE1 PHE A 483 14.634 42.208 47.455 1.00123.70 A C
ANISOU 3837 CE1 PHE A 483 10505 19451 17043 -5706 5631 -13768 A C
ATOM 3838 CE2 PHE A 483 16.537 43.605 47.119 1.00124.86 A C
ANISOU 3838 CE2 PHE A 483 10767 19526 17148 -5960 5543 -13539 A C
ATOM 3839 CZ PHE A 483 15.171 43.428 47.105 1.00122.83 A C
ANISOU 3839 CZ PHE A 483 10575 18926 17170 -6003 5832 -13709 A C
ATOM 3840 N SER A 484 18.025 37.656 50.398 1.00124.98 A N
ANISOU 3840 N SER A 484 9383 23457 14648 -4172 3713 -13749 A N
ATOM 3841 CA SER A 484 18.576 36.339 50.723 1.00125.88 A C
ANISOU 3841 CA SER A 484 9272 24318 14239 -3677 3307 -13585 A C
ATOM 3842 C SER A 484 17.621 35.224 50.276 1.00129.45 A C
ANISOU 3842 C SER A 484 9779 24712 14693 -3299 3218 -13389 A C
ATOM 3843 O SER A 484 16.548 35.522 49.744 1.00128.85 A O
ANISOU 3843 O SER A 484 9790 24123 15045 -3517 3524 -13579 A O
ATOM 3844 CB SER A 484 18.850 36.242 52.224 1.00129.45 A C
ANISOU 3844 CB SER A 484 9906 25037 14242 -3395 2992 -13229 A C
ATOM 3845 OG SER A 484 17.659 36.358 52.987 1.00136.28 A O
ANISOU 3845 OG SER A 484 11240 25386 15154 -3227 2970 -12816 A O
ATOM 3846 N ALA A 485 18.002 33.942 50.498 1.00128.13 A N
ANISOU 3846 N ALA A 485 9321 25321 14043 -2837 2890 -13374 A N
ATOM 3847 CA ALA A 485 17.178 32.774 50.144 1.00128.03 A C
ANISOU 3847 CA ALA A 485 9185 25527 13934 -2456 2785 -13398 A C
ATOM 3848 C ALA A 485 15.852 32.766 50.917 1.00131.18 A C
ANISOU 3848 C ALA A 485 9850 25621 14370 -2364 2824 -13278 A C
ATOM 3849 O ALA A 485 14.854 32.243 50.417 1.00130.54 A O
ANISOU 3849 O ALA A 485 9711 25426 14464 -2263 2905 -13428 A O
ATOM 3850 CB ALA A 485 17.945 31.489 50.414 1.00129.09 A C
ANISOU 3850 CB ALA A 485 9181 26373 13496 -1858 2360 -13074 A C
ATOM 3851 N ASP A 486 15.849 33.397 52.112 1.00129.62 A N
ANISOU 3851 N ASP A 486 9687 25550 14011 -2514 2842 -13395 A N
ATOM 3852 CA ASP A 486 14.721 33.538 53.036 1.00129.92 A C
ANISOU 3852 CA ASP A 486 9861 25469 14034 -2506 2910 -13462 A C
ATOM 3853 C ASP A 486 13.479 34.167 52.383 1.00133.19 A C
ANISOU 3853 C ASP A 486 10542 25003 15062 -2815 3277 -13506 A C
ATOM 3854 O ASP A 486 12.361 33.886 52.813 1.00133.34 A O
ANISOU 3854 O ASP A 486 10609 24953 15101 -2710 3323 -13575 A O
ATOM 3855 CB ASP A 486 15.140 34.402 54.244 1.00131.54 A C
ANISOU 3855 CB ASP A 486 10304 25591 14083 -2644 2867 -13278 A C
ATOM 3856 CG ASP A 486 16.376 33.934 55.002 1.00135.77 A C
ANISOU 3856 CG ASP A 486 11085 26353 14149 -2234 2444 -12564 A C
ATOM 3857 OD1 ASP A 486 16.671 32.716 54.973 1.00135.29 A O
ANISOU 3857 OD1 ASP A 486 10873 26803 13727 -1787 2184 -12393 A O
ATOM 3858 OD2 ASP A 486 17.027 34.781 55.651 1.00138.98 A O1-
ANISOU 3858 OD2 ASP A 486 11812 26429 14564 -2366 2394 -12225 A O1-
ATOM 3859 N ASP A 487 13.683 35.019 51.365 1.00130.81 A N
ANISOU 3859 N ASP A 487 10183 24260 15258 -3297 3630 -13809 A N
ATOM 3860 CA ASP A 487 12.637 35.737 50.630 1.00130.12 A C
ANISOU 3860 CA ASP A 487 10261 23351 15827 -3691 4091 -13998 A C
ATOM 3861 C ASP A 487 11.684 34.815 49.850 1.00132.94 A C
ANISOU 3861 C ASP A 487 10640 23478 16393 -3454 4103 -13899 A C
ATOM 3862 O ASP A 487 10.496 35.134 49.727 1.00131.73 A O
ANISOU 3862 O ASP A 487 10629 22743 16680 -3656 4430 -14028 A O
ATOM 3863 CB ASP A 487 13.279 36.722 49.638 1.00130.96 A C
ANISOU 3863 CB ASP A 487 10536 22877 16347 -4061 4339 -13899 A C
ATOM 3864 CG ASP A 487 14.270 37.724 50.210 1.00138.19 A C
ANISOU 3864 CG ASP A 487 11900 23526 17078 -4028 4113 -13236 A C
ATOM 3865 OD1 ASP A 487 14.336 37.860 51.455 1.00139.81 A O
ANISOU 3865 OD1 ASP A 487 12216 23953 16953 -3891 3916 -13093 A O
ATOM 3866 OD2 ASP A 487 14.979 38.372 49.414 1.00140.17 A O1-
ANISOU 3866 OD2 ASP A 487 12317 23403 17540 -4178 4169 -12987 A O1-
ATOM 3867 N VAL A 488 12.209 33.705 49.290 1.00131.44 A N
ANISOU 3867 N VAL A 488 10107 23895 15939 -3141 3852 -14003 A N
ATOM 3868 CA VAL A 488 11.425 32.785 48.452 1.00128.20 A C
ANISOU 3868 CA VAL A 488 9909 23098 15704 -2793 3754 -13592 A C
ATOM 3869 C VAL A 488 11.248 31.394 49.112 1.00131.44 A C
ANISOU 3869 C VAL A 488 10380 24049 15512 -2069 3242 -13135 A C
ATOM 3870 O VAL A 488 10.336 30.660 48.720 1.00126.44 A O
ANISOU 3870 O VAL A 488 10236 22823 14984 -1677 3096 -12408 A O
ATOM 3871 CB VAL A 488 12.014 32.668 47.010 1.00130.13 A C
ANISOU 3871 CB VAL A 488 10215 23010 16218 -2822 3792 -13369 A C
ATOM 3872 CG1 VAL A 488 12.031 34.022 46.304 1.00130.96 A C
ANISOU 3872 CG1 VAL A 488 10360 22439 16961 -3494 4341 -13707 A C
ATOM 3873 CG2 VAL A 488 13.407 32.032 46.999 1.00132.98 A C
ANISOU 3873 CG2 VAL A 488 10091 24366 16068 -2616 3495 -13639 A C
ATOM 3874 N LYS A 489 12.065 31.098 50.160 1.00132.59 A N
ANISOU 3874 N LYS A 489 10032 25313 15033 -1916 3011 -13585 A N
ATOM 3875 CA LYS A 489 12.120 29.861 50.959 1.00132.35 A C
ANISOU 3875 CA LYS A 489 9959 25986 14342 -1232 2560 -13271 A C
ATOM 3876 C LYS A 489 10.746 29.426 51.504 1.00132.03 A C
ANISOU 3876 C LYS A 489 10403 25437 14326 -930 2490 -12734 A C
ATOM 3877 O LYS A 489 10.424 28.236 51.447 1.00128.85 A O
ANISOU 3877 O LYS A 489 10288 25003 13664 -323 2186 -12098 A O
ATOM 3878 CB LYS A 489 13.098 30.044 52.137 1.00136.35 A C
ANISOU 3878 CB LYS A 489 10416 27050 14340 -1149 2363 -13161 A C
ATOM 3879 CG LYS A 489 13.641 28.737 52.716 1.00143.74 A C
ANISOU 3879 CG LYS A 489 11796 28116 14703 -367 1881 -12110 A C
ATOM 3880 CD LYS A 489 13.409 28.637 54.224 1.00147.53 A C
ANISOU 3880 CD LYS A 489 12748 28414 14894 -159 1739 -11501 A C
ATOM 3881 CE LYS A 489 14.516 29.248 55.050 1.00150.92 A C
ANISOU 3881 CE LYS A 489 13602 28481 15260 -294 1663 -10912 A C
ATOM 3882 NZ LYS A 489 14.217 29.169 56.504 1.00156.24 A N1+
ANISOU 3882 NZ LYS A 489 14725 28926 15715 -124 1554 -10384 A N1+
ATOM 3883 N ASP A 490 9.956 30.381 52.037 1.00128.01 A N
ANISOU 3883 N ASP A 490 9981 24533 14123 -1356 2792 -13001 A N
ATOM 3884 CA ASP A 490 8.631 30.126 52.612 1.00124.63 A C
ANISOU 3884 CA ASP A 490 9975 23633 13747 -1147 2773 -12572 A C
ATOM 3885 C ASP A 490 7.500 30.276 51.573 1.00122.27 A C
ANISOU 3885 C ASP A 490 10257 22106 14094 -1231 2970 -11983 A C
ATOM 3886 O ASP A 490 6.327 30.268 51.959 1.00119.39 A O
ANISOU 3886 O ASP A 490 10236 21246 13882 -1177 3037 -11687 A O
ATOM 3887 CB ASP A 490 8.382 31.081 53.799 1.00130.43 A C
ANISOU 3887 CB ASP A 490 10472 24648 14439 -1547 2999 -13195 A C
ATOM 3888 CG ASP A 490 9.321 30.919 54.982 1.00144.42 A C
ANISOU 3888 CG ASP A 490 12244 27050 15578 -1282 2688 -12954 A C
ATOM 3889 OD1 ASP A 490 8.945 31.339 56.101 1.00145.52 A O
ANISOU 3889 OD1 ASP A 490 12563 27147 15582 -1322 2704 -12870 A O
ATOM 3890 OD2 ASP A 490 10.444 30.399 54.787 1.00150.26 A O1-
ANISOU 3890 OD2 ASP A 490 13155 27897 16040 -973 2401 -12377 A O1-
ATOM 3891 N LEU A 491 7.834 30.370 50.264 1.00116.56 A N
ANISOU 3891 N LEU A 491 9638 20930 13721 -1336 3051 -11796 A N
ATOM 3892 CA LEU A 491 6.810 30.564 49.235 1.00111.21 A C
ANISOU 3892 CA LEU A 491 9467 19158 13629 -1418 3245 -11259 A C
ATOM 3893 C LEU A 491 6.541 29.301 48.431 1.00111.62 A C
ANISOU 3893 C LEU A 491 9871 18945 13596 -893 2942 -10505 A C
ATOM 3894 O LEU A 491 7.469 28.557 48.120 1.00112.70 A O
ANISOU 3894 O LEU A 491 9833 19581 13408 -612 2693 -10465 A O
ATOM 3895 CB LEU A 491 7.183 31.707 48.265 1.00111.59 A C
ANISOU 3895 CB LEU A 491 9447 18723 14229 -1978 3648 -11564 A C
ATOM 3896 CG LEU A 491 7.397 33.127 48.817 1.00120.34 A C
ANISOU 3896 CG LEU A 491 10275 19882 15567 -2606 4074 -12321 A C
ATOM 3897 CD1 LEU A 491 7.808 34.068 47.712 1.00120.75 A C
ANISOU 3897 CD1 LEU A 491 10310 19429 16142 -3079 4466 -12523 A C
ATOM 3898 CD2 LEU A 491 6.137 33.677 49.474 1.00122.71 A C
ANISOU 3898 CD2 LEU A 491 10852 19664 16108 -2728 4298 -12243 A C
ATOM 3899 N SER A 492 5.272 29.080 48.067 1.00103.71 A N
ANISOU 3899 N SER A 492 9357 17159 12890 -774 2985 -9923 A N
ATOM 3900 CA SER A 492 4.866 27.961 47.218 1.00 99.32 A C
ANISOU 3900 CA SER A 492 9179 16237 12321 -350 2758 -9212 A C
ATOM 3901 C SER A 492 5.201 28.296 45.762 1.00101.90 A C
ANISOU 3901 C SER A 492 9573 16075 13068 -564 2911 -9096 A C
ATOM 3902 O SER A 492 5.540 29.446 45.475 1.00103.02 A O
ANISOU 3902 O SER A 492 9530 16062 13552 -1040 3228 -9516 A O
ATOM 3903 CB SER A 492 3.373 27.685 47.380 1.00 99.31 A C
ANISOU 3903 CB SER A 492 9632 15630 12472 -197 2770 -8695 A C
ATOM 3904 OG SER A 492 2.602 28.818 47.017 1.00107.13 A O
ANISOU 3904 OG SER A 492 10764 15924 14015 -617 3133 -8734 A O
ATOM 3905 N SER A 493 5.109 27.309 44.847 1.00 95.97 A N
ANISOU 3905 N SER A 493 9094 15079 12291 -224 2711 -8539 A N
ATOM 3906 CA SER A 493 5.373 27.504 43.418 1.00 94.18 A C
ANISOU 3906 CA SER A 493 8962 14397 12426 -371 2825 -8358 A C
ATOM 3907 C SER A 493 4.452 28.592 42.820 1.00 96.17 A C
ANISOU 3907 C SER A 493 9428 13833 13279 -770 3201 -8273 A C
ATOM 3908 O SER A 493 4.934 29.448 42.077 1.00 96.49 A O
ANISOU 3908 O SER A 493 9344 13664 13652 -1121 3461 -8504 A O
ATOM 3909 CB SER A 493 5.210 26.186 42.659 1.00 95.37 A C
ANISOU 3909 CB SER A 493 9423 14389 12426 80 2552 -7741 A C
ATOM 3910 OG SER A 493 3.878 25.708 42.756 1.00104.92 A O
ANISOU 3910 OG SER A 493 11046 15108 13710 258 2516 -7238 A O
ATOM 3911 N HIS A 494 3.151 28.594 43.201 1.00 91.03 A N
ANISOU 3911 N HIS A 494 9080 12756 12752 -709 3251 -7962 A N
ATOM 3912 CA HIS A 494 2.145 29.575 42.750 1.00 89.00 A C
ANISOU 3912 CA HIS A 494 9040 11750 13024 -1009 3603 -7826 A C
ATOM 3913 C HIS A 494 2.454 30.968 43.288 1.00 92.56 A C
ANISOU 3913 C HIS A 494 9230 12230 13707 -1482 3976 -8445 A C
ATOM 3914 O HIS A 494 2.202 31.961 42.605 1.00 91.25 A O
ANISOU 3914 O HIS A 494 9141 11515 14014 -1799 4343 -8466 A O
ATOM 3915 CB HIS A 494 0.728 29.129 43.143 1.00 87.67 A C
ANISOU 3915 CB HIS A 494 9217 11241 12854 -791 3531 -7369 A C
ATOM 3916 CG HIS A 494 0.295 27.889 42.416 1.00 88.26 A C
ANISOU 3916 CG HIS A 494 9594 11141 12797 -411 3255 -6752 A C
ATOM 3917 CD2 HIS A 494 -0.256 27.757 41.187 1.00 87.56 A C
ANISOU 3917 CD2 HIS A 494 9770 10507 12993 -390 3303 -6285 A C
ATOM 3918 ND1 HIS A 494 0.518 26.618 42.938 1.00 90.33 A N
ANISOU 3918 ND1 HIS A 494 9893 11854 12575 -8 2907 -6602 A N
ATOM 3919 CE1 HIS A 494 0.059 25.764 42.032 1.00 86.66 A C
ANISOU 3919 CE1 HIS A 494 9731 11061 12137 215 2776 -6069 A C
ATOM 3920 NE2 HIS A 494 -0.411 26.398 40.958 1.00 85.18 A N
ANISOU 3920 NE2 HIS A 494 9672 10300 12392 -9 2990 -5872 A N
ATOM 3921 N GLN A 495 3.040 31.036 44.490 1.00 91.50 A N
ANISOU 3921 N GLN A 495 8783 12754 13228 -1526 3901 -8957 A N
ATOM 3922 CA GLN A 495 3.473 32.292 45.095 1.00 95.36 A C
ANISOU 3922 CA GLN A 495 8977 13384 13871 -2002 4249 -9640 A C
ATOM 3923 C GLN A 495 4.696 32.843 44.341 1.00 99.53 A C
ANISOU 3923 C GLN A 495 9226 14049 14543 -2315 4421 -10033 A C
ATOM 3924 O GLN A 495 4.771 34.050 44.111 1.00 99.97 A O
ANISOU 3924 O GLN A 495 9223 13757 15003 -2774 4861 -10376 A O
ATOM 3925 CB GLN A 495 3.773 32.116 46.590 1.00100.29 A C
ANISOU 3925 CB GLN A 495 9318 14766 14023 -1940 4084 -10079 A C
ATOM 3926 CG GLN A 495 2.522 32.198 47.462 1.00117.38 A C
ANISOU 3926 CG GLN A 495 11715 16676 16209 -1864 4130 -9906 A C
ATOM 3927 CD GLN A 495 2.820 31.990 48.923 1.00143.10 A C
ANISOU 3927 CD GLN A 495 14696 20707 18967 -1775 3956 -10311 A C
ATOM 3928 NE2 GLN A 495 2.382 32.917 49.753 1.00139.30 A N
ANISOU 3928 NE2 GLN A 495 14163 20147 18619 -2076 4232 -10679 A N
ATOM 3929 OE1 GLN A 495 3.418 30.990 49.329 1.00141.10 A O
ANISOU 3929 OE1 GLN A 495 14288 21127 18196 -1411 3584 -10277 A O
ATOM 3930 N LEU A 496 5.619 31.956 43.912 1.00 96.18 A N
ANISOU 3930 N LEU A 496 8653 14088 13802 -2060 4103 -9957 A N
ATOM 3931 CA LEU A 496 6.794 32.348 43.131 1.00 97.79 A C
ANISOU 3931 CA LEU A 496 8592 14454 14111 -2315 4229 -10284 A C
ATOM 3932 C LEU A 496 6.379 32.811 41.722 1.00 97.21 A C
ANISOU 3932 C LEU A 496 8820 13537 14577 -2464 4502 -9902 A C
ATOM 3933 O LEU A 496 6.991 33.746 41.200 1.00 98.86 A O
ANISOU 3933 O LEU A 496 8878 13594 15091 -2876 4850 -10258 A O
ATOM 3934 CB LEU A 496 7.846 31.222 43.061 1.00 98.43 A C
ANISOU 3934 CB LEU A 496 8443 15269 13689 -1949 3806 -10264 A C
ATOM 3935 CG LEU A 496 9.248 31.575 42.474 1.00106.40 A C
ANISOU 3935 CG LEU A 496 9072 16659 14696 -2206 3895 -10713 A C
ATOM 3936 CD1 LEU A 496 9.804 32.899 43.012 1.00111.83 A C
ANISOU 3936 CD1 LEU A 496 9391 17566 15533 -2796 4280 -11510 A C
ATOM 3937 CD2 LEU A 496 10.247 30.470 42.736 1.00109.83 A C
ANISOU 3937 CD2 LEU A 496 9232 17949 14550 -1795 3466 -10745 A C
ATOM 3938 N ILE A 497 5.324 32.195 41.131 1.00 88.34 A N
ANISOU 3938 N ILE A 497 8116 11880 13568 -2147 4372 -9196 A N
ATOM 3939 CA ILE A 497 4.805 32.586 39.811 1.00 86.26 A C
ANISOU 3939 CA ILE A 497 8147 10851 13778 -2235 4611 -8776 A C
ATOM 3940 C ILE A 497 4.270 34.041 39.883 1.00 93.97 A C
ANISOU 3940 C ILE A 497 9189 11272 15245 -2666 5146 -9001 A C
ATOM 3941 O ILE A 497 4.625 34.868 39.035 1.00 95.11 A O
ANISOU 3941 O ILE A 497 9324 11056 15758 -2963 5501 -9105 A O
ATOM 3942 CB ILE A 497 3.731 31.583 39.284 1.00 84.67 A C
ANISOU 3942 CB ILE A 497 8345 10285 13539 -1810 4346 -8014 A C
ATOM 3943 CG1 ILE A 497 4.376 30.245 38.880 1.00 83.37 A C
ANISOU 3943 CG1 ILE A 497 8158 10531 12987 -1430 3918 -7776 A C
ATOM 3944 CG2 ILE A 497 2.934 32.166 38.103 1.00 83.80 A C
ANISOU 3944 CG2 ILE A 497 8535 9380 13925 -1916 4639 -7589 A C
ATOM 3945 CD1 ILE A 497 3.458 29.020 39.007 1.00 89.17 A C
ANISOU 3945 CD1 ILE A 497 9207 11193 13479 -984 3586 -7208 A C
ATOM 3946 N GLU A 498 3.475 34.343 40.936 1.00 91.74 A N
ANISOU 3946 N GLU A 498 8967 10943 14946 -2692 5220 -9095 A N
ATOM 3947 CA GLU A 498 2.832 35.626 41.190 1.00 93.36 A C
ANISOU 3947 CA GLU A 498 9267 10630 15574 -3039 5717 -9284 A C
ATOM 3948 C GLU A 498 3.853 36.767 41.362 1.00 99.33 A C
ANISOU 3948 C GLU A 498 9713 11518 16509 -3563 6131 -10021 A C
ATOM 3949 O GLU A 498 3.685 37.806 40.724 1.00 99.78 A O
ANISOU 3949 O GLU A 498 9899 10969 17044 -3858 6616 -10041 A O
ATOM 3950 CB GLU A 498 1.900 35.507 42.416 1.00 95.36 A C
ANISOU 3950 CB GLU A 498 9601 10967 15664 -2915 5629 -9278 A C
ATOM 3951 CG GLU A 498 1.160 36.778 42.805 1.00114.65 A C
ANISOU 3951 CG GLU A 498 12160 12885 18517 -3231 6135 -9459 A C
ATOM 3952 CD GLU A 498 0.097 37.307 41.866 1.00147.13 A C
ANISOU 3952 CD GLU A 498 16643 16147 23112 -3197 6443 -8918 A C
ATOM 3953 OE1 GLU A 498 -0.384 36.549 40.992 1.00138.39 A O
ANISOU 3953 OE1 GLU A 498 15754 14840 21988 -2866 6196 -8295 A O
ATOM 3954 OE2 GLU A 498 -0.304 38.476 42.064 1.00153.75 A O1-
ANISOU 3954 OE2 GLU A 498 17554 16535 24327 -3488 6942 -9119 A O1-
ATOM 3955 N VAL A 499 4.900 36.584 42.191 1.00 97.43 A N
ANISOU 3955 N VAL A 499 9067 12068 15883 -3676 5963 -10617 A N
ATOM 3956 CA VAL A 499 5.925 37.621 42.403 1.00102.08 A C
ANISOU 3956 CA VAL A 499 9314 12876 16596 -4213 6347 -11388 A C
ATOM 3957 C VAL A 499 6.679 37.914 41.066 1.00107.50 A C
ANISOU 3957 C VAL A 499 9983 13301 17559 -4389 6547 -11350 A C
ATOM 3958 O VAL A 499 6.974 39.080 40.792 1.00111.28 A O
ANISOU 3958 O VAL A 499 10424 13427 18429 -4860 7081 -11727 A O
ATOM 3959 CB VAL A 499 6.883 37.322 43.602 1.00109.37 A C
ANISOU 3959 CB VAL A 499 9759 14810 16988 -4278 6093 -12044 A C
ATOM 3960 CG1 VAL A 499 7.524 35.949 43.510 1.00107.67 A C
ANISOU 3960 CG1 VAL A 499 9377 15275 16258 -3832 5518 -11834 A C
ATOM 3961 CG2 VAL A 499 7.948 38.402 43.777 1.00114.78 A C
ANISOU 3961 CG2 VAL A 499 10070 15735 17805 -4890 6521 -12890 A C
ATOM 3962 N LEU A 500 6.927 36.881 40.220 1.00100.05 A N
ANISOU 3962 N LEU A 500 9104 12475 16434 -4013 6158 -10877 A N
ATOM 3963 CA LEU A 500 7.600 37.058 38.928 1.00 99.56 A C
ANISOU 3963 CA LEU A 500 9042 12183 16604 -4131 6308 -10785 A C
ATOM 3964 C LEU A 500 6.702 37.815 37.942 1.00102.12 A C
ANISOU 3964 C LEU A 500 9771 11540 17490 -4212 6730 -10329 A C
ATOM 3965 O LEU A 500 7.182 38.720 37.254 1.00102.81 A O
ANISOU 3965 O LEU A 500 9838 11290 17934 -4566 7173 -10531 A O
ATOM 3966 CB LEU A 500 8.045 35.707 38.334 1.00 96.54 A C
ANISOU 3966 CB LEU A 500 8634 12190 15858 -3683 5776 -10392 A C
ATOM 3967 CG LEU A 500 9.270 35.042 38.978 1.00103.24 A C
ANISOU 3967 CG LEU A 500 9030 14021 16176 -3611 5425 -10856 A C
ATOM 3968 CD1 LEU A 500 9.436 33.629 38.485 1.00 99.96 A C
ANISOU 3968 CD1 LEU A 500 8692 13888 15402 -3073 4905 -10353 A C
ATOM 3969 CD2 LEU A 500 10.558 35.844 38.723 1.00108.51 A C
ANISOU 3969 CD2 LEU A 500 9319 14965 16947 -4085 5726 -11506 A C
ATOM 3970 N ALA A 501 5.399 37.449 37.902 1.00 97.34 A N
ANISOU 3970 N ALA A 501 9523 10514 16947 -3879 6608 -9722 A N
ATOM 3971 CA ALA A 501 4.356 38.072 37.082 1.00 96.22 A C
ANISOU 3971 CA ALA A 501 9767 9518 17276 -3863 6960 -9217 A C
ATOM 3972 C ALA A 501 4.216 39.568 37.415 1.00106.86 A C
ANISOU 3972 C ALA A 501 11136 10410 19055 -4323 7620 -9630 A C
ATOM 3973 O ALA A 501 4.072 40.374 36.493 1.00107.49 A O
ANISOU 3973 O ALA A 501 11403 9875 19565 -4471 8065 -9452 A O
ATOM 3974 CB ALA A 501 3.024 37.362 37.303 1.00 92.68 A C
ANISOU 3974 CB ALA A 501 9610 8883 16720 -3443 6669 -8615 A C
ATOM 3975 N ILE A 502 4.302 39.949 38.717 1.00107.96 A N
ANISOU 3975 N ILE A 502 11086 10857 19077 -4552 7711 -10193 A N
ATOM 3976 CA ILE A 502 4.187 41.355 39.121 1.00112.64 A C
ANISOU 3976 CA ILE A 502 11704 11025 20069 -5012 8364 -10642 A C
ATOM 3977 C ILE A 502 5.482 42.114 38.763 1.00121.22 A C
ANISOU 3977 C ILE A 502 12532 12209 21316 -5506 8747 -11251 A C
ATOM 3978 O ILE A 502 5.417 43.316 38.490 1.00123.55 A O
ANISOU 3978 O ILE A 502 12962 11906 22077 -5864 9391 -11428 A O
ATOM 3979 CB ILE A 502 3.745 41.577 40.600 1.00118.70 A C
ANISOU 3979 CB ILE A 502 12381 12032 20686 -5115 8383 -11037 A C
ATOM 3980 CG1 ILE A 502 4.822 41.195 41.630 1.00122.33 A C
ANISOU 3980 CG1 ILE A 502 12375 13439 20667 -5278 8090 -11736 A C
ATOM 3981 CG2 ILE A 502 2.387 40.915 40.906 1.00115.85 A C
ANISOU 3981 CG2 ILE A 502 12307 11490 20220 -4652 8075 -10412 A C
ATOM 3982 CD1 ILE A 502 4.747 41.992 42.895 1.00132.02 A C
ANISOU 3982 CD1 ILE A 502 13453 14821 21887 -5625 8375 -12372 A C
ATOM 3983 N LEU A 503 6.643 41.412 38.735 1.00119.14 A N
ANISOU 3983 N LEU A 503 11913 12678 20675 -5512 8375 -11549 A N
ATOM 3984 CA LEU A 503 7.925 42.001 38.326 1.00122.87 A C
ANISOU 3984 CA LEU A 503 12106 13325 21255 -5962 8682 -12112 A C
ATOM 3985 C LEU A 503 7.949 42.247 36.823 1.00127.16 A C
ANISOU 3985 C LEU A 503 12900 13247 22169 -5929 8930 -11648 A C
ATOM 3986 O LEU A 503 8.545 43.223 36.373 1.00129.31 A O
ANISOU 3986 O LEU A 503 13189 13252 22693 -6282 9346 -11855 A O
ATOM 3987 CB LEU A 503 9.115 41.116 38.726 1.00123.44 A C
ANISOU 3987 CB LEU A 503 11712 14406 20782 -5912 8180 -12510 A C
ATOM 3988 CG LEU A 503 9.606 41.266 40.144 1.00130.35 A C
ANISOU 3988 CG LEU A 503 12279 16013 21234 -6052 7984 -13064 A C
ATOM 3989 CD1 LEU A 503 10.517 40.138 40.521 1.00130.89 A C
ANISOU 3989 CD1 LEU A 503 11890 17085 20759 -5866 7474 -13370 A C
ATOM 3990 CD2 LEU A 503 10.319 42.576 40.331 1.00132.33 A C
ANISOU 3990 CD2 LEU A 503 12735 16202 21340 -6189 7926 -12864 A C
ATOM 3991 N LEU A 504 7.293 41.361 36.049 1.00120.58 A N
ANISOU 3991 N LEU A 504 12325 12229 21262 -5416 8546 -10861 A N
ATOM 3992 CA LEU A 504 7.199 41.468 34.593 1.00119.22 A C
ANISOU 3992 CA LEU A 504 12402 11509 21388 -5309 8716 -10335 A C
ATOM 3993 C LEU A 504 6.236 42.590 34.175 1.00126.98 A C
ANISOU 3993 C LEU A 504 13764 11571 22911 -5411 9336 -10043 A C
ATOM 3994 O LEU A 504 6.436 43.202 33.124 1.00128.66 A O
ANISOU 3994 O LEU A 504 14118 11300 23466 -5539 9742 -9885 A O
ATOM 3995 CB LEU A 504 6.759 40.132 33.981 1.00113.10 A C
ANISOU 3995 CB LEU A 504 11771 10871 20329 -4740 8107 -9621 A C
ATOM 3996 CG LEU A 504 7.848 39.064 33.875 1.00116.20 A C
ANISOU 3996 CG LEU A 504 11858 12020 20271 -4593 7584 -9763 A C
ATOM 3997 CD1 LEU A 504 7.242 37.703 33.759 1.00110.87 A C
ANISOU 3997 CD1 LEU A 504 11338 11527 19261 -4038 6984 -9160 A C
ATOM 3998 CD2 LEU A 504 8.777 39.327 32.695 1.00119.32 A C
ANISOU 3998 CD2 LEU A 504 12182 12323 20832 -4762 7775 -9794 A C
ATOM 3999 N LEU A 505 5.196 42.850 35.008 1.00124.14 A N
ANISOU 3999 N LEU A 505 13571 10986 22611 -5326 9412 -9955 A N
ATOM 4000 CA LEU A 505 4.161 43.879 34.817 1.00125.46 A C
ANISOU 4000 CA LEU A 505 14096 10325 23248 -5360 9981 -9670 A C
ATOM 4001 C LEU A 505 4.695 45.312 35.068 1.00132.20 A C
ANISOU 4001 C LEU A 505 15004 10969 24256 -5746 10396 -9996 A C
ATOM 4002 O LEU A 505 4.065 46.277 34.628 1.00131.85 A O
ANISOU 4002 O LEU A 505 15320 10297 24480 -5666 10707 -9547 A O
ATOM 4003 CB LEU A 505 2.965 43.603 35.750 1.00123.94 A C
ANISOU 4003 CB LEU A 505 14034 10121 22936 -5106 9781 -9468 A C
ATOM 4004 CG LEU A 505 1.569 43.948 35.208 1.00127.42 A C
ANISOU 4004 CG LEU A 505 14886 9834 23694 -4807 10025 -8766 A C
ATOM 4005 CD1 LEU A 505 0.544 42.931 35.666 1.00123.28 A C
ANISOU 4005 CD1 LEU A 505 14449 9535 22857 -4350 9464 -8300 A C
ATOM 4006 CD2 LEU A 505 1.124 45.339 35.632 1.00135.01 A C
ANISOU 4006 CD2 LEU A 505 16004 10209 25084 -5113 10754 -9039 A C
ATOM 4007 N GLU A 506 5.834 45.450 35.776 1.00129.53 A N
ANISOU 4007 N GLU A 506 14362 11260 23594 -6033 10193 -10584 A N
ATOM 4008 CA GLU A 506 6.444 46.752 36.051 1.00129.16 A C
ANISOU 4008 CA GLU A 506 14446 11226 23404 -6199 10162 -10580 A C
ATOM 4009 C GLU A 506 7.534 47.077 35.022 1.00130.52 A C
ANISOU 4009 C GLU A 506 14605 11499 23486 -6252 10037 -10414 A C
ATOM 4010 O GLU A 506 7.620 46.396 33.999 1.00129.40 A O
ANISOU 4010 O GLU A 506 14377 11243 23547 -6225 10188 -10364 A O
ATOM 4011 CB GLU A 506 6.987 46.814 37.487 1.00130.85 A C
ANISOU 4011 CB GLU A 506 14463 12140 23115 -6267 9714 -10947 A C
ATOM 4012 CG GLU A 506 5.931 47.217 38.505 1.00140.16 A C
ANISOU 4012 CG GLU A 506 15984 13281 23989 -5857 9258 -10386 A C
ATOM 4013 CD GLU A 506 5.313 48.589 38.303 1.00159.54 A C
ANISOU 4013 CD GLU A 506 19128 15524 25966 -5170 8389 -8984 A C
ATOM 4014 OE1 GLU A 506 4.282 48.681 37.598 1.00161.02 A O
ANISOU 4014 OE1 GLU A 506 19539 15140 26502 -5039 8695 -8635 A O
ATOM 4015 OE2 GLU A 506 5.857 49.571 38.856 1.00158.20 A O1-
ANISOU 4015 OE2 GLU A 506 18963 15400 25746 -5393 8463 -9243 A O1-
ATOM 4016 N LYS A 507 8.326 48.146 35.262 1.00128.27 A N
ANISOU 4016 N LYS A 507 14345 11281 23109 -6492 10070 -10569 A N
ATOM 4017 CA LYS A 507 9.399 48.579 34.357 1.00128.13 A C
ANISOU 4017 CA LYS A 507 14302 11316 23065 -6621 10057 -10500 A C
ATOM 4018 C LYS A 507 10.596 47.587 34.369 1.00130.21 A C
ANISOU 4018 C LYS A 507 14165 12385 22924 -6626 9588 -10771 A C
ATOM 4019 O LYS A 507 10.801 46.913 35.378 1.00130.13 A O
ANISOU 4019 O LYS A 507 13867 12971 22604 -6630 9300 -11159 A O
ATOM 4020 CB LYS A 507 9.867 50.015 34.695 1.00130.25 A C
ANISOU 4020 CB LYS A 507 14783 11555 23151 -6683 9892 -10313 A C
ATOM 4021 CG LYS A 507 10.563 50.191 36.050 1.00140.56 A C
ANISOU 4021 CG LYS A 507 16057 13694 23657 -6394 8880 -10077 A C
ATOM 4022 CD LYS A 507 11.480 51.418 36.083 1.00146.10 A C
ANISOU 4022 CD LYS A 507 16952 14541 24020 -6293 8390 -9636 A C
ATOM 4023 CE LYS A 507 12.916 51.097 35.727 1.00150.45 A C
ANISOU 4023 CE LYS A 507 17360 15692 24113 -6124 7749 -9360 A C
ATOM 4024 NZ LYS A 507 13.815 52.262 35.942 1.00154.27 A N1+
ANISOU 4024 NZ LYS A 507 18022 16308 24286 -6005 7256 -8923 A N1+
ATOM 4025 N PRO A 508 11.407 47.509 33.281 1.00127.62 A N
ANISOU 4025 N PRO A 508 13730 12021 22740 -6776 9769 -10827 A N
ATOM 4026 CA PRO A 508 12.545 46.567 33.257 1.00127.65 A C
ANISOU 4026 CA PRO A 508 13307 12761 22432 -6834 9449 -11194 A C
ATOM 4027 C PRO A 508 13.597 46.835 34.343 1.00129.76 A C
ANISOU 4027 C PRO A 508 13372 13775 22156 -6874 8936 -11401 A C
ATOM 4028 O PRO A 508 14.017 47.973 34.570 1.00129.86 A O
ANISOU 4028 O PRO A 508 13532 13688 22120 -7004 8936 -11313 A O
ATOM 4029 CB PRO A 508 13.129 46.774 31.858 1.00128.90 A C
ANISOU 4029 CB PRO A 508 13569 12675 22732 -6832 9547 -10864 A C
ATOM 4030 CG PRO A 508 11.985 47.267 31.046 1.00131.46 A C
ANISOU 4030 CG PRO A 508 14356 12191 23401 -6609 9806 -10212 A C
ATOM 4031 CD PRO A 508 11.274 48.194 31.979 1.00128.50 A C
ANISOU 4031 CD PRO A 508 14168 11507 23150 -6718 10039 -10308 A C
ATOM 4032 N LEU A 509 13.995 45.756 35.024 1.00126.24 A N
ANISOU 4032 N LEU A 509 12470 14029 21467 -6932 8771 -11983 A N
ATOM 4033 CA LEU A 509 14.959 45.769 36.120 1.00125.82 A C
ANISOU 4033 CA LEU A 509 12133 14748 20927 -6990 8375 -12310 A C
ATOM 4034 C LEU A 509 16.398 45.917 35.635 1.00126.73 A C
ANISOU 4034 C LEU A 509 12096 15250 20807 -7041 8136 -12260 A C
ATOM 4035 O LEU A 509 16.726 45.385 34.578 1.00126.71 A O
ANISOU 4035 O LEU A 509 12006 15211 20928 -7023 8213 -12207 A O
ATOM 4036 CB LEU A 509 14.850 44.454 36.917 1.00125.80 A C
ANISOU 4036 CB LEU A 509 11779 15430 20589 -6807 8049 -12635 A C
ATOM 4037 CG LEU A 509 13.632 44.257 37.802 1.00128.11 A C
ANISOU 4037 CG LEU A 509 12251 15576 20850 -6595 7964 -12494 A C
ATOM 4038 CD1 LEU A 509 13.394 42.795 38.042 1.00127.82 A C
ANISOU 4038 CD1 LEU A 509 11898 16037 20631 -6388 7748 -12738 A C
ATOM 4039 CD2 LEU A 509 13.795 44.960 39.136 1.00130.64 A C
ANISOU 4039 CD2 LEU A 509 12664 16172 20803 -6549 7656 -12435 A C
ATOM 4040 N PRO A 510 17.299 46.538 36.432 1.00122.93 A N
ANISOU 4040 N PRO A 510 11426 15181 20102 -7283 8065 -12615 A N
ATOM 4041 CA PRO A 510 18.725 46.594 36.039 1.00122.48 A C
ANISOU 4041 CA PRO A 510 11146 15543 19849 -7384 7898 -12688 A C
ATOM 4042 C PRO A 510 19.382 45.205 35.949 1.00122.68 A C
ANISOU 4042 C PRO A 510 10737 16323 19551 -7222 7586 -12931 A C
ATOM 4043 O PRO A 510 18.909 44.260 36.592 1.00121.39 A O
ANISOU 4043 O PRO A 510 10360 16552 19212 -7076 7442 -13189 A O
ATOM 4044 CB PRO A 510 19.378 47.402 37.171 1.00124.45 A C
ANISOU 4044 CB PRO A 510 11438 16084 19764 -7400 7584 -12630 A C
ATOM 4045 CG PRO A 510 18.260 48.105 37.851 1.00127.66 A C
ANISOU 4045 CG PRO A 510 12230 16022 20251 -7281 7597 -12336 A C
ATOM 4046 CD PRO A 510 17.073 47.211 37.725 1.00124.19 A C
ANISOU 4046 CD PRO A 510 11705 15434 20047 -7265 7887 -12608 A C
ATOM 4047 N VAL A 511 20.498 45.095 35.169 1.00119.71 A N
ANISOU 4047 N VAL A 511 10081 16217 19186 -7419 7674 -13175 A N
ATOM 4048 CA VAL A 511 21.276 43.851 34.947 1.00119.32 A C
ANISOU 4048 CA VAL A 511 9592 16911 18831 -7272 7391 -13416 A C
ATOM 4049 C VAL A 511 21.825 43.336 36.304 1.00121.29 A C
ANISOU 4049 C VAL A 511 9564 18015 18506 -7066 6886 -13573 A C
ATOM 4050 O VAL A 511 21.885 42.127 36.513 1.00121.13 A O
ANISOU 4050 O VAL A 511 9230 18589 18206 -6825 6629 -13764 A O
ATOM 4051 CB VAL A 511 22.409 44.018 33.873 1.00122.40 A C
ANISOU 4051 CB VAL A 511 10005 17310 19190 -7248 7282 -13086 A C
ATOM 4052 CG1 VAL A 511 23.184 42.715 33.641 1.00122.21 A C
ANISOU 4052 CG1 VAL A 511 9566 18025 18844 -7033 6970 -13259 A C
ATOM 4053 CG2 VAL A 511 21.851 44.524 32.545 1.00121.82 A C
ANISOU 4053 CG2 VAL A 511 10244 16392 19652 -7410 7762 -12855 A C
ATOM 4054 N SER A 512 22.161 44.253 37.228 1.00118.38 A N
ANISOU 4054 N SER A 512 9166 17761 18053 -7322 6939 -13814 A N
ATOM 4055 CA SER A 512 22.667 43.959 38.572 1.00118.37 A C
ANISOU 4055 CA SER A 512 8920 18506 17549 -7187 6541 -13992 A C
ATOM 4056 C SER A 512 21.631 43.240 39.462 1.00120.05 A C
ANISOU 4056 C SER A 512 9123 18887 17603 -6946 6399 -14061 A C
ATOM 4057 O SER A 512 22.007 42.411 40.292 1.00119.80 A O
ANISOU 4057 O SER A 512 8797 19614 17108 -6703 6023 -14204 A O
ATOM 4058 CB SER A 512 23.093 45.255 39.253 1.00120.69 A C
ANISOU 4058 CB SER A 512 9486 18584 17787 -7295 6457 -13731 A C
ATOM 4059 OG SER A 512 21.971 46.100 39.463 1.00125.46 A O
ANISOU 4059 OG SER A 512 10625 18409 18636 -7231 6558 -13280 A O
ATOM 4060 N HIS A 513 20.344 43.584 39.308 1.00117.40 A N
ANISOU 4060 N HIS A 513 8960 17926 17721 -7170 6872 -14263 A N
ATOM 4061 CA HIS A 513 19.253 43.032 40.114 1.00117.30 A C
ANISOU 4061 CA HIS A 513 8930 17986 17654 -7028 6848 -14417 A C
ATOM 4062 C HIS A 513 18.920 41.600 39.732 1.00119.15 A C
ANISOU 4062 C HIS A 513 8946 18551 17775 -6709 6660 -14446 A C
ATOM 4063 O HIS A 513 18.716 40.779 40.628 1.00119.45 A O
ANISOU 4063 O HIS A 513 8774 19180 17432 -6446 6341 -14581 A O
ATOM 4064 CB HIS A 513 18.008 43.922 40.007 1.00117.52 A C
ANISOU 4064 CB HIS A 513 9395 17081 18176 -7197 7285 -14255 A C
ATOM 4065 CG HIS A 513 18.109 45.180 40.807 1.00120.35 A C
ANISOU 4065 CG HIS A 513 10077 17190 18460 -7260 7214 -13985 A C
ATOM 4066 CD2 HIS A 513 17.178 45.788 41.576 1.00121.74 A C
ANISOU 4066 CD2 HIS A 513 10549 16981 18724 -7247 7299 -13858 A C
ATOM 4067 ND1 HIS A 513 19.278 45.926 40.841 1.00122.20 A N
ANISOU 4067 ND1 HIS A 513 10347 17566 18517 -7325 7024 -13804 A N
ATOM 4068 CE1 HIS A 513 19.021 46.954 41.631 1.00122.18 A C
ANISOU 4068 CE1 HIS A 513 10574 17303 18546 -7447 7091 -13766 A C
ATOM 4069 NE2 HIS A 513 17.769 46.913 42.098 1.00122.10 A N
ANISOU 4069 NE2 HIS A 513 10733 16976 18682 -7393 7246 -13782 A N
ATOM 4070 N VAL A 514 18.859 41.294 38.417 1.00115.64 A N
ANISOU 4070 N VAL A 514 8377 17826 17734 -6888 7023 -14661 A N
ATOM 4071 CA VAL A 514 18.567 39.941 37.930 1.00115.11 A C
ANISOU 4071 CA VAL A 514 8030 18079 17627 -6646 6911 -14830 A C
ATOM 4072 C VAL A 514 19.779 39.018 38.201 1.00118.63 A C
ANISOU 4072 C VAL A 514 8167 19500 17409 -6245 6274 -14706 A C
ATOM 4073 O VAL A 514 19.602 37.807 38.345 1.00118.74 A O
ANISOU 4073 O VAL A 514 7909 20062 17143 -5906 5985 -14832 A O
ATOM 4074 CB VAL A 514 18.091 39.877 36.454 1.00116.89 A C
ANISOU 4074 CB VAL A 514 8506 17533 18376 -6674 7238 -14539 A C
ATOM 4075 CG1 VAL A 514 16.687 40.466 36.307 1.00115.97 A C
ANISOU 4075 CG1 VAL A 514 8781 16451 18831 -6832 7736 -14413 A C
ATOM 4076 CG2 VAL A 514 19.076 40.548 35.494 1.00116.89 A C
ANISOU 4076 CG2 VAL A 514 8578 17323 18512 -6884 7387 -14387 A C
ATOM 4077 N LYS A 515 20.993 39.605 38.302 1.00116.45 A N
ANISOU 4077 N LYS A 515 7749 19540 16957 -6435 6224 -14804 A N
ATOM 4078 CA LYS A 515 22.228 38.902 38.653 1.00116.90 A C
ANISOU 4078 CA LYS A 515 7456 20520 16440 -6159 5743 -14814 A C
ATOM 4079 C LYS A 515 22.180 38.523 40.129 1.00119.82 A C
ANISOU 4079 C LYS A 515 7806 21438 16284 -5812 5300 -14674 A C
ATOM 4080 O LYS A 515 22.623 37.436 40.505 1.00119.22 A O
ANISOU 4080 O LYS A 515 7404 22159 15735 -5436 4914 -14740 A O
ATOM 4081 CB LYS A 515 23.463 39.776 38.361 1.00118.79 A C
ANISOU 4081 CB LYS A 515 7820 20660 16655 -6316 5708 -14531 A C
ATOM 4082 CG LYS A 515 23.991 39.661 36.942 1.00122.85 A C
ANISOU 4082 CG LYS A 515 8684 20705 17287 -6053 5554 -13733 A C
ATOM 4083 CD LYS A 515 25.163 40.596 36.689 1.00128.00 A C
ANISOU 4083 CD LYS A 515 9760 21001 17874 -5964 5310 -12919 A C
ATOM 4084 CE LYS A 515 25.838 40.307 35.370 1.00133.66 A C
ANISOU 4084 CE LYS A 515 10847 21392 18545 -5528 4967 -11937 A C
ATOM 4085 NZ LYS A 515 27.054 41.143 35.170 1.00141.04 A N1+
ANISOU 4085 NZ LYS A 515 12231 21956 19403 -5351 4648 -11025 A N1+
ATOM 4086 N ARG A 516 21.622 39.433 40.961 1.00118.68 A N
ANISOU 4086 N ARG A 516 7838 20993 16261 -6065 5493 -14793 A N
ATOM 4087 CA ARG A 516 21.457 39.253 42.400 1.00119.26 A C
ANISOU 4087 CA ARG A 516 7859 21539 15914 -5862 5200 -14818 A C
ATOM 4088 C ARG A 516 20.378 38.194 42.672 1.00123.56 A C
ANISOU 4088 C ARG A 516 8474 22142 16333 -5437 4998 -14635 A C
ATOM 4089 O ARG A 516 20.532 37.417 43.615 1.00124.24 A O
ANISOU 4089 O ARG A 516 8387 22909 15911 -5070 4608 -14605 A O
ATOM 4090 CB ARG A 516 21.123 40.592 43.072 1.00119.54 A C
ANISOU 4090 CB ARG A 516 8226 21045 16147 -6167 5415 -14759 A C
ATOM 4091 CG ARG A 516 21.137 40.572 44.605 1.00128.07 A C
ANISOU 4091 CG ARG A 516 9684 22256 16722 -5674 4850 -14044 A C
ATOM 4092 CD ARG A 516 22.534 40.466 45.196 1.00136.15 A C
ANISOU 4092 CD ARG A 516 11005 23460 17265 -5197 4219 -13134 A C
ATOM 4093 NE ARG A 516 22.493 40.449 46.657 1.00141.67 A N
ANISOU 4093 NE ARG A 516 12165 24079 17586 -4737 3746 -12375 A N
ATOM 4094 CZ ARG A 516 22.880 39.430 47.415 1.00151.59 A C
ANISOU 4094 CZ ARG A 516 13856 25352 18389 -3989 3123 -11323 A C
ATOM 4095 NH1 ARG A 516 23.379 38.332 46.861 1.00143.67 A N1+
ANISOU 4095 NH1 ARG A 516 12320 25056 17210 -3938 3118 -11779 A N1+
ATOM 4096 NH2 ARG A 516 22.798 39.511 48.737 1.00140.91 A N
ANISOU 4096 NH2 ARG A 516 12146 24620 16774 -4170 3169 -11976 A N
ATOM 4097 N MET A 517 19.309 38.147 41.833 1.00121.13 A N
ANISOU 4097 N MET A 517 8197 21288 16539 -5643 5414 -14892 A N
ATOM 4098 CA MET A 517 18.230 37.154 41.936 1.00121.16 A C
ANISOU 4098 CA MET A 517 8108 21388 16539 -5382 5360 -15014 A C
ATOM 4099 C MET A 517 18.774 35.745 41.751 1.00122.61 A C
ANISOU 4099 C MET A 517 7970 22361 16255 -4877 4897 -14953 A C
ATOM 4100 O MET A 517 18.436 34.852 42.523 1.00121.97 A O
ANISOU 4100 O MET A 517 7708 22863 15773 -4495 4582 -15018 A O
ATOM 4101 CB MET A 517 17.128 37.407 40.898 1.00122.25 A C
ANISOU 4101 CB MET A 517 8564 20537 17349 -5568 5804 -14892 A C
ATOM 4102 CG MET A 517 16.237 38.541 41.249 1.00125.05 A C
ANISOU 4102 CG MET A 517 9407 20044 18063 -5786 6110 -14625 A C
ATOM 4103 SD MET A 517 14.923 38.761 40.043 1.00127.51 A S
ANISOU 4103 SD MET A 517 10160 19167 19120 -5879 6587 -14288 A S
ATOM 4104 CE MET A 517 14.221 40.217 40.665 1.00125.23 A C
ANISOU 4104 CE MET A 517 10204 18201 19177 -6253 7032 -14336 A C
ATOM 4105 N GLN A 518 19.627 35.557 40.729 1.00119.84 A N
ANISOU 4105 N GLN A 518 7369 22195 15970 -4968 4951 -15125 A N
ATOM 4106 CA GLN A 518 20.259 34.281 40.420 1.00119.30 A C
ANISOU 4106 CA GLN A 518 6947 22907 15473 -4507 4552 -15134 A C
ATOM 4107 C GLN A 518 21.166 33.848 41.567 1.00122.71 A C
ANISOU 4107 C GLN A 518 7333 24099 15192 -4065 4016 -14777 A C
ATOM 4108 O GLN A 518 21.170 32.674 41.929 1.00123.07 A O
ANISOU 4108 O GLN A 518 7177 24810 14774 -3530 3631 -14708 A O
ATOM 4109 CB GLN A 518 21.046 34.377 39.101 1.00119.90 A C
ANISOU 4109 CB GLN A 518 7008 22767 15782 -4642 4679 -15046 A C
ATOM 4110 CG GLN A 518 21.643 33.047 38.598 1.00123.56 A C
ANISOU 4110 CG GLN A 518 7368 23742 15837 -4027 4204 -14665 A C
ATOM 4111 CD GLN A 518 20.746 31.839 38.798 1.00135.33 A C
ANISOU 4111 CD GLN A 518 9386 24947 17086 -3251 3734 -13718 A C
ATOM 4112 NE2 GLN A 518 21.313 30.760 39.310 1.00130.00 A N
ANISOU 4112 NE2 GLN A 518 8289 25292 15812 -2780 3340 -13902 A N
ATOM 4113 OE1 GLN A 518 19.549 31.850 38.490 1.00127.64 A O
ANISOU 4113 OE1 GLN A 518 8709 23296 16491 -3285 3908 -13568 A O
ATOM 4114 N GLU A 519 21.888 34.807 42.156 1.00120.07 A N
ANISOU 4114 N GLU A 519 6994 23823 14804 -4387 4098 -14874 A N
ATOM 4115 CA GLU A 519 22.813 34.605 43.264 1.00120.94 A C
ANISOU 4115 CA GLU A 519 7022 24587 14344 -4106 3704 -14659 A C
ATOM 4116 C GLU A 519 22.107 34.041 44.520 1.00124.46 A C
ANISOU 4116 C GLU A 519 7630 25238 14423 -3685 3407 -14377 A C
ATOM 4117 O GLU A 519 22.593 33.055 45.071 1.00124.94 A O
ANISOU 4117 O GLU A 519 7527 25989 13955 -3190 3015 -14192 A O
ATOM 4118 CB GLU A 519 23.533 35.939 43.579 1.00122.17 A C
ANISOU 4118 CB GLU A 519 7410 24365 14646 -4502 3840 -14515 A C
ATOM 4119 CG GLU A 519 24.518 35.932 44.740 1.00128.11 A C
ANISOU 4119 CG GLU A 519 8460 25286 14931 -4122 3367 -13774 A C
ATOM 4120 CD GLU A 519 25.838 35.208 44.558 1.00135.94 A C
ANISOU 4120 CD GLU A 519 10041 25950 15661 -3437 2808 -12377 A C
ATOM 4121 OE1 GLU A 519 26.150 34.766 43.427 1.00136.39 A O
ANISOU 4121 OE1 GLU A 519 10131 25847 15843 -3320 2801 -12152 A O
ATOM 4122 OE2 GLU A 519 26.571 35.093 45.566 1.00123.19 A O1-
ANISOU 4122 OE2 GLU A 519 8061 25090 13654 -3417 2657 -12702 A O1-
ATOM 4123 N VAL A 520 20.977 34.629 44.957 1.00121.87 A N
ANISOU 4123 N VAL A 520 7386 24555 14364 -3978 3689 -14692 A N
ATOM 4124 CA VAL A 520 20.320 34.171 46.188 1.00121.85 A C
ANISOU 4124 CA VAL A 520 7383 24906 14009 -3684 3479 -14676 A C
ATOM 4125 C VAL A 520 19.145 33.198 45.955 1.00125.18 A C
ANISOU 4125 C VAL A 520 7919 25198 14446 -3281 3371 -14484 A C
ATOM 4126 O VAL A 520 18.873 32.393 46.848 1.00125.76 A O
ANISOU 4126 O VAL A 520 7916 25818 14049 -2818 3050 -14364 A O
ATOM 4127 CB VAL A 520 19.879 35.331 47.121 1.00123.92 A C
ANISOU 4127 CB VAL A 520 8012 24625 14446 -3995 3655 -14569 A C
ATOM 4128 CG1 VAL A 520 21.077 35.963 47.815 1.00124.33 A C
ANISOU 4128 CG1 VAL A 520 8096 24886 14257 -4093 3516 -14423 A C
ATOM 4129 CG2 VAL A 520 19.047 36.381 46.386 1.00122.85 A C
ANISOU 4129 CG2 VAL A 520 8099 23583 14995 -4518 4174 -14769 A C
ATOM 4130 N TYR A 521 18.443 33.268 44.810 1.00122.36 A N
ANISOU 4130 N TYR A 521 7502 24368 14623 -3558 3726 -14826 A N
ATOM 4131 CA TYR A 521 17.280 32.395 44.600 1.00120.04 A C
ANISOU 4131 CA TYR A 521 7359 23851 14399 -3193 3631 -14616 A C
ATOM 4132 C TYR A 521 17.575 31.180 43.717 1.00121.67 A C
ANISOU 4132 C TYR A 521 7724 24086 14420 -2600 3267 -13986 A C
ATOM 4133 O TYR A 521 16.779 30.237 43.725 1.00118.07 A O
ANISOU 4133 O TYR A 521 7674 23340 13846 -2050 2988 -13304 A O
ATOM 4134 CB TYR A 521 16.080 33.173 44.011 1.00117.32 A C
ANISOU 4134 CB TYR A 521 7575 22240 14762 -3511 4027 -14293 A C
ATOM 4135 CG TYR A 521 15.686 34.453 44.728 1.00121.76 A C
ANISOU 4135 CG TYR A 521 8071 22581 15611 -4117 4470 -14862 A C
ATOM 4136 CD1 TYR A 521 15.798 34.565 46.110 1.00124.67 A C
ANISOU 4136 CD1 TYR A 521 8413 23417 15538 -3996 4254 -14864 A C
ATOM 4137 CD2 TYR A 521 15.114 35.514 44.035 1.00121.33 A C
ANISOU 4137 CD2 TYR A 521 8328 21537 16234 -4605 4987 -14859 A C
ATOM 4138 CE1 TYR A 521 15.418 35.730 46.775 1.00125.05 A C
ANISOU 4138 CE1 TYR A 521 8734 22978 15803 -4356 4513 -14870 A C
ATOM 4139 CE2 TYR A 521 14.713 36.677 44.692 1.00122.90 A C
ANISOU 4139 CE2 TYR A 521 8720 21317 16660 -4993 5305 -14994 A C
ATOM 4140 CZ TYR A 521 14.870 36.783 46.064 1.00128.02 A C
ANISOU 4140 CZ TYR A 521 9550 22288 16803 -4719 4926 -14634 A C
ATOM 4141 OH TYR A 521 14.487 37.927 46.725 1.00126.72 A O
ANISOU 4141 OH TYR A 521 9617 21704 16828 -5041 5183 -14692 A O
ATOM 4142 N ASN A 522 18.703 31.197 42.957 1.00120.15 A N
ANISOU 4142 N ASN A 522 7222 24222 14208 -2724 3290 -14221 A N
ATOM 4143 CA ASN A 522 19.136 30.132 42.036 1.00117.04 A C
ANISOU 4143 CA ASN A 522 6936 23875 13660 -2221 2994 -13702 A C
ATOM 4144 C ASN A 522 17.972 29.662 41.124 1.00114.16 A C
ANISOU 4144 C ASN A 522 7281 22408 13686 -1945 2975 -12839 A C
ATOM 4145 O ASN A 522 17.668 28.464 41.027 1.00109.89 A O
ANISOU 4145 O ASN A 522 7006 21873 12875 -1321 2625 -12240 A O
ATOM 4146 CB ASN A 522 19.762 28.959 42.791 1.00118.36 A C
ANISOU 4146 CB ASN A 522 6792 25102 13077 -1577 2519 -13651 A C
ATOM 4147 CG ASN A 522 20.832 28.280 41.985 1.00138.92 A C
ANISOU 4147 CG ASN A 522 9684 27565 15534 -1184 2261 -12865 A C
ATOM 4148 ND2 ASN A 522 22.073 28.434 42.426 1.00136.90 A N
ANISOU 4148 ND2 ASN A 522 9247 27798 14973 -1191 2144 -12855 A N
ATOM 4149 OD1 ASN A 522 20.573 27.682 40.935 1.00125.08 A O
ANISOU 4149 OD1 ASN A 522 7845 25758 13922 -1018 2260 -12943 A O
ATOM 4150 N LEU A 523 17.332 30.629 40.454 1.00108.79 A N
ANISOU 4150 N LEU A 523 6899 20799 13638 -2422 3380 -12796 A N
ATOM 4151 CA LEU A 523 16.186 30.379 39.584 1.00102.50 A C
ANISOU 4151 CA LEU A 523 6731 18970 13244 -2251 3419 -12050 A C
ATOM 4152 C LEU A 523 16.573 29.724 38.254 1.00103.56 A C
ANISOU 4152 C LEU A 523 7024 18868 13457 -2012 3303 -11610 A C
ATOM 4153 O LEU A 523 15.685 29.248 37.547 1.00 98.80 A O
ANISOU 4153 O LEU A 523 6916 17553 13072 -1768 3248 -10950 A O
ATOM 4154 CB LEU A 523 15.410 31.684 39.340 1.00102.10 A C
ANISOU 4154 CB LEU A 523 6914 18067 13814 -2817 3917 -12165 A C
ATOM 4155 CG LEU A 523 14.810 32.359 40.581 1.00107.45 A C
ANISOU 4155 CG LEU A 523 7552 18786 14487 -3036 4064 -12495 A C
ATOM 4156 CD1 LEU A 523 14.586 33.824 40.343 1.00109.14 A C
ANISOU 4156 CD1 LEU A 523 7784 18433 15250 -3712 4638 -12902 A C
ATOM 4157 CD2 LEU A 523 13.526 31.675 41.034 1.00105.04 A C
ANISOU 4157 CD2 LEU A 523 7706 18066 14138 -2606 3851 -11865 A C
ATOM 4158 N ASN A 524 17.883 29.652 37.932 1.00103.08 A N
ANISOU 4158 N ASN A 524 6536 19440 13191 -2066 3254 -11973 A N
ATOM 4159 CA ASN A 524 18.383 29.019 36.711 1.00100.55 A C
ANISOU 4159 CA ASN A 524 6313 18987 12902 -1839 3141 -11614 A C
ATOM 4160 C ASN A 524 18.211 27.500 36.736 1.00103.19 A C
ANISOU 4160 C ASN A 524 6866 19522 12819 -1098 2685 -11020 A C
ATOM 4161 O ASN A 524 18.132 26.908 35.656 1.00 99.88 A O
ANISOU 4161 O ASN A 524 6742 18681 12528 -875 2613 -10529 A O
ATOM 4162 CB ASN A 524 19.862 29.344 36.469 1.00104.09 A C
ANISOU 4162 CB ASN A 524 6206 20133 13210 -2095 3213 -12205 A C
ATOM 4163 CG ASN A 524 20.146 30.597 35.669 1.00121.21 A C
ANISOU 4163 CG ASN A 524 8311 21829 15912 -2773 3703 -12562 A C
ATOM 4164 ND2 ASN A 524 21.426 30.898 35.494 1.00119.27 A N
ANISOU 4164 ND2 ASN A 524 7565 22209 15544 -3040 3789 -13120 A N
ATOM 4165 OD1 ASN A 524 19.248 31.317 35.217 1.00108.67 A O
ANISOU 4165 OD1 ASN A 524 7112 19337 14839 -3059 4024 -12348 A O
ATOM 4166 N ASP A 525 18.154 26.860 37.934 1.00102.44 A N
ANISOU 4166 N ASP A 525 6643 20053 12225 -713 2401 -11055 A N
ATOM 4167 CA ASP A 525 18.008 25.398 38.012 1.00101.49 A C
ANISOU 4167 CA ASP A 525 6752 20114 11694 11 2012 -10492 A C
ATOM 4168 C ASP A 525 16.567 24.934 38.381 1.00104.28 A C
ANISOU 4168 C ASP A 525 7644 19852 12124 264 1939 -9940 A C
ATOM 4169 O ASP A 525 16.365 23.741 38.629 1.00102.88 A O
ANISOU 4169 O ASP A 525 7676 19823 11592 847 1654 -9504 A O
ATOM 4170 CB ASP A 525 19.040 24.771 38.968 1.00108.05 A C
ANISOU 4170 CB ASP A 525 7096 22107 11850 400 1725 -10802 A C
ATOM 4171 CG ASP A 525 20.451 24.646 38.414 1.00122.25 A C
ANISOU 4171 CG ASP A 525 8444 24556 13448 417 1673 -11111 A C
ATOM 4172 OD1 ASP A 525 20.616 24.024 37.336 1.00119.29 A O
ANISOU 4172 OD1 ASP A 525 8292 23872 13162 649 1607 -10707 A O
ATOM 4173 OD2 ASP A 525 21.400 25.094 39.100 1.00135.11 A O1-
ANISOU 4173 OD2 ASP A 525 9481 27069 14787 231 1680 -11760 A O1-
ATOM 4174 N VAL A 526 15.573 25.846 38.354 1.00100.64 A N
ANISOU 4174 N VAL A 526 7424 18682 12132 -161 2217 -9938 A N
ATOM 4175 CA VAL A 526 14.168 25.503 38.615 1.00 97.66 A C
ANISOU 4175 CA VAL A 526 7544 17691 11873 22 2180 -9432 A C
ATOM 4176 C VAL A 526 13.596 24.862 37.343 1.00 99.48 A C
ANISOU 4176 C VAL A 526 8256 17186 12358 214 2148 -8773 A C
ATOM 4177 O VAL A 526 13.625 25.484 36.274 1.00 98.36 A O
ANISOU 4177 O VAL A 526 8186 16546 12641 -123 2378 -8753 A O
ATOM 4178 CB VAL A 526 13.327 26.714 39.094 1.00101.93 A C
ANISOU 4178 CB VAL A 526 8139 17796 12795 -474 2497 -9681 A C
ATOM 4179 CG1 VAL A 526 11.835 26.384 39.113 1.00 97.48 A C
ANISOU 4179 CG1 VAL A 526 8106 16522 12409 -300 2478 -9106 A C
ATOM 4180 CG2 VAL A 526 13.786 27.190 40.472 1.00106.69 A C
ANISOU 4180 CG2 VAL A 526 8289 19162 13085 -625 2502 -10317 A C
ATOM 4181 N LYS A 527 13.111 23.612 37.455 1.00 94.75 A N
ANISOU 4181 N LYS A 527 7978 16539 11483 750 1880 -8251 A N
ATOM 4182 CA LYS A 527 12.554 22.879 36.316 1.00 90.73 A C
ANISOU 4182 CA LYS A 527 7920 15397 11154 951 1833 -7644 A C
ATOM 4183 C LYS A 527 11.108 23.305 36.001 1.00 92.07 A C
ANISOU 4183 C LYS A 527 8512 14706 11764 727 2013 -7301 A C
ATOM 4184 O LYS A 527 10.702 23.179 34.841 1.00 90.04 A O
ANISOU 4184 O LYS A 527 8539 13882 11790 685 2078 -6932 A O
ATOM 4185 CB LYS A 527 12.626 21.356 36.534 1.00 92.39 A C
ANISOU 4185 CB LYS A 527 8330 15869 10906 1592 1526 -7239 A C
ATOM 4186 CG LYS A 527 14.022 20.774 36.341 1.00104.98 A C
ANISOU 4186 CG LYS A 527 9609 18142 12135 1884 1363 -7397 A C
ATOM 4187 CD LYS A 527 14.008 19.256 36.400 1.00112.74 A C
ANISOU 4187 CD LYS A 527 10880 19227 12728 2530 1122 -6916 A C
ATOM 4188 CE LYS A 527 15.368 18.642 36.158 1.00122.38 A C
ANISOU 4188 CE LYS A 527 11806 21116 13578 2874 973 -7034 A C
ATOM 4189 NZ LYS A 527 15.751 18.682 34.721 1.00126.43 A N1+
ANISOU 4189 NZ LYS A 527 12375 21290 14374 2715 1055 -6935 A N1+
ATOM 4190 N ASN A 528 10.345 23.810 37.012 1.00 87.98 A N
ANISOU 4190 N ASN A 528 8016 14125 11287 592 2093 -7426 A N
ATOM 4191 CA ASN A 528 8.943 24.262 36.908 1.00 84.41 A C
ANISOU 4191 CA ASN A 528 7923 12937 11214 402 2266 -7134 A C
ATOM 4192 C ASN A 528 8.779 25.320 35.794 1.00 86.27 A C
ANISOU 4192 C ASN A 528 8203 12588 11988 -41 2582 -7148 A C
ATOM 4193 O ASN A 528 9.154 26.481 35.969 1.00 88.60 A O
ANISOU 4193 O ASN A 528 8236 12924 12504 -454 2845 -7606 A O
ATOM 4194 CB ASN A 528 8.452 24.797 38.262 1.00 85.13 A C
ANISOU 4194 CB ASN A 528 7914 13197 11234 287 2329 -7413 A C
ATOM 4195 CG ASN A 528 6.957 25.005 38.367 1.00100.85 A C
ANISOU 4195 CG ASN A 528 10284 14533 13500 219 2443 -7062 A C
ATOM 4196 ND2 ASN A 528 6.283 24.119 39.087 1.00 91.12 A N
ANISOU 4196 ND2 ASN A 528 9271 13364 11987 571 2244 -6772 A N
ATOM 4197 OD1 ASN A 528 6.397 25.989 37.867 1.00 90.43 A O
ANISOU 4197 OD1 ASN A 528 9052 12671 12636 -143 2729 -7060 A O
ATOM 4198 N SER A 529 8.218 24.877 34.648 1.00 78.19 A N
ANISOU 4198 N SER A 529 7520 11031 11157 58 2570 -6638 A N
ATOM 4199 CA SER A 529 7.989 25.589 33.385 1.00 76.01 A C
ANISOU 4199 CA SER A 529 7356 10186 11336 -237 2826 -6492 A C
ATOM 4200 C SER A 529 7.416 26.998 33.533 1.00 79.31 A C
ANISOU 4200 C SER A 529 7754 10203 12177 -668 3196 -6688 A C
ATOM 4201 O SER A 529 7.863 27.900 32.821 1.00 80.91 A O
ANISOU 4201 O SER A 529 7828 10229 12686 -998 3475 -6890 A O
ATOM 4202 CB SER A 529 7.053 24.774 32.490 1.00 76.50 A C
ANISOU 4202 CB SER A 529 7839 9759 11469 -11 2721 -5861 A C
ATOM 4203 OG SER A 529 7.565 23.472 32.252 1.00 86.51 A O
ANISOU 4203 OG SER A 529 9168 11316 12385 371 2433 -5666 A O
ATOM 4204 N GLU A 530 6.409 27.177 34.410 1.00 72.56 A N
ANISOU 4204 N GLU A 530 7047 9176 11348 -658 3225 -6610 A N
ATOM 4205 CA GLU A 530 5.741 28.463 34.610 1.00 71.67 A C
ANISOU 4205 CA GLU A 530 6958 8642 11629 -1019 3590 -6752 A C
ATOM 4206 C GLU A 530 6.677 29.466 35.280 1.00 76.44 A C
ANISOU 4206 C GLU A 530 7172 9604 12266 -1375 3812 -7440 A C
ATOM 4207 O GLU A 530 6.643 30.654 34.948 1.00 76.31 A O
ANISOU 4207 O GLU A 530 7120 9226 12648 -1758 4207 -7637 A O
ATOM 4208 CB GLU A 530 4.439 28.298 35.422 1.00 71.30 A C
ANISOU 4208 CB GLU A 530 7153 8382 11555 -884 3539 -6503 A C
ATOM 4209 CG GLU A 530 3.306 27.641 34.648 1.00 75.58 A C
ANISOU 4209 CG GLU A 530 8085 8455 12178 -656 3435 -5853 A C
ATOM 4210 CD GLU A 530 2.690 28.419 33.499 1.00 89.44 A C
ANISOU 4210 CD GLU A 530 10011 9587 14384 -848 3726 -5565 A C
ATOM 4211 OE1 GLU A 530 2.666 29.668 33.557 1.00 86.67 A O
ANISOU 4211 OE1 GLU A 530 9566 8999 14365 -1171 4088 -5813 A O
ATOM 4212 OE2 GLU A 530 2.169 27.774 32.563 1.00 81.96 A O1-
ANISOU 4212 OE2 GLU A 530 9303 8388 13448 -667 3608 -5082 A O1-
ATOM 4213 N ILE A 531 7.521 28.975 36.207 1.00 73.29 A N
ANISOU 4213 N ILE A 531 6480 9930 11437 -1243 3574 -7804 A N
ATOM 4214 CA ILE A 531 8.507 29.777 36.935 1.00 75.97 A C
ANISOU 4214 CA ILE A 531 6388 10767 11710 -1567 3733 -8512 A C
ATOM 4215 C ILE A 531 9.668 30.129 35.984 1.00 77.41 A C
ANISOU 4215 C ILE A 531 6337 11062 12012 -1789 3866 -8758 A C
ATOM 4216 O ILE A 531 10.035 31.298 35.880 1.00 77.41 A O
ANISOU 4216 O ILE A 531 6165 10929 12317 -2250 4247 -9179 A O
ATOM 4217 CB ILE A 531 9.002 29.058 38.232 1.00 81.10 A C
ANISOU 4217 CB ILE A 531 6778 12235 11800 -1300 3408 -8787 A C
ATOM 4218 CG1 ILE A 531 7.817 28.785 39.202 1.00 80.40 A C
ANISOU 4218 CG1 ILE A 531 6927 12006 11615 -1116 3319 -8561 A C
ATOM 4219 CG2 ILE A 531 10.123 29.861 38.930 1.00 86.33 A C
ANISOU 4219 CG2 ILE A 531 6929 13525 12348 -1653 3556 -9568 A C
ATOM 4220 CD1 ILE A 531 8.096 27.889 40.408 1.00 91.93 A C
ANISOU 4220 CD1 ILE A 531 8232 14196 12501 -746 2977 -8666 A C
ATOM 4221 N ARG A 532 10.217 29.120 35.284 1.00 73.15 A N
ANISOU 4221 N ARG A 532 5814 10735 11246 -1467 3581 -8489 A N
ATOM 4222 CA ARG A 532 11.349 29.259 34.364 1.00 74.36 A C
ANISOU 4222 CA ARG A 532 5749 11053 11453 -1607 3651 -8676 A C
ATOM 4223 C ARG A 532 11.055 30.254 33.230 1.00 77.79 A C
ANISOU 4223 C ARG A 532 6351 10768 12438 -1972 4061 -8565 A C
ATOM 4224 O ARG A 532 11.894 31.125 32.983 1.00 79.95 A O
ANISOU 4224 O ARG A 532 6357 11130 12888 -2361 4348 -9019 A O
ATOM 4225 CB ARG A 532 11.770 27.896 33.796 1.00 71.88 A C
ANISOU 4225 CB ARG A 532 5509 10997 10807 -1134 3271 -8304 A C
ATOM 4226 CG ARG A 532 13.124 27.920 33.085 1.00 77.10 A C
ANISOU 4226 CG ARG A 532 5853 12035 11404 -1228 3284 -8585 A C
ATOM 4227 CD ARG A 532 13.738 26.546 33.016 1.00 73.38 A C
ANISOU 4227 CD ARG A 532 5337 12080 10463 -719 2881 -8387 A C
ATOM 4228 NE ARG A 532 14.682 26.424 31.915 1.00 88.90 A N
ANISOU 4228 NE ARG A 532 7180 14127 12471 -747 2899 -8403 A N
ATOM 4229 CZ ARG A 532 16.004 26.619 31.969 1.00106.39 A C
ANISOU 4229 CZ ARG A 532 8941 16976 14506 -859 2902 -8891 A C
ATOM 4230 NH1 ARG A 532 16.743 26.472 30.876 1.00 89.84 A N1+
ANISOU 4230 NH1 ARG A 532 6783 14876 12475 -872 2926 -8841 A N1+
ATOM 4231 NH2 ARG A 532 16.596 26.920 33.120 1.00 93.21 A N
ANISOU 4231 NH2 ARG A 532 6863 15991 12561 -945 2869 -9434 A N
ATOM 4232 N PHE A 533 9.877 30.147 32.574 1.00 71.05 A N
ANISOU 4232 N PHE A 533 5922 9233 11841 -1853 4107 -7980 A N
ATOM 4233 CA PHE A 533 9.483 31.036 31.472 1.00 71.06 A C
ANISOU 4233 CA PHE A 533 6116 8548 12338 -2121 4491 -7781 A C
ATOM 4234 C PHE A 533 9.480 32.517 31.911 1.00 78.51 A C
ANISOU 4234 C PHE A 533 6937 9258 13635 -2611 4980 -8242 A C
ATOM 4235 O PHE A 533 10.021 33.376 31.201 1.00 79.30 A O
ANISOU 4235 O PHE A 533 6956 9134 14040 -2943 5342 -8437 A O
ATOM 4236 CB PHE A 533 8.107 30.628 30.909 1.00 69.28 A C
ANISOU 4236 CB PHE A 533 6332 7739 12253 -1869 4424 -7088 A C
ATOM 4237 CG PHE A 533 7.340 31.703 30.169 1.00 70.84 A C
ANISOU 4237 CG PHE A 533 6747 7220 12948 -2109 4854 -6867 A C
ATOM 4238 CD1 PHE A 533 7.784 32.178 28.937 1.00 74.76 A C
ANISOU 4238 CD1 PHE A 533 7256 7440 13710 -2270 5098 -6785 A C
ATOM 4239 CD2 PHE A 533 6.150 32.209 30.684 1.00 72.58 A C
ANISOU 4239 CD2 PHE A 533 7170 7047 13359 -2138 5019 -6706 A C
ATOM 4240 CE1 PHE A 533 7.076 33.174 28.258 1.00 75.71 A C
ANISOU 4240 CE1 PHE A 533 7587 6909 14269 -2443 5518 -6544 A C
ATOM 4241 CE2 PHE A 533 5.435 33.196 29.998 1.00 75.21 A C
ANISOU 4241 CE2 PHE A 533 7707 6735 14135 -2305 5432 -6467 A C
ATOM 4242 CZ PHE A 533 5.908 33.678 28.795 1.00 74.08 A C
ANISOU 4242 CZ PHE A 533 7575 6330 14242 -2448 5685 -6381 A C
ATOM 4243 N ARG A 534 8.902 32.796 33.087 1.00 76.26 A N
ANISOU 4243 N ARG A 534 6645 9027 13301 -2657 5010 -8426 A N
ATOM 4244 CA ARG A 534 8.808 34.141 33.651 1.00 79.40 A C
ANISOU 4244 CA ARG A 534 6952 9205 14010 -3108 5479 -8878 A C
ATOM 4245 C ARG A 534 10.187 34.670 34.045 1.00 88.72 A C
ANISOU 4245 C ARG A 534 7677 10936 15096 -3478 5627 -9636 A C
ATOM 4246 O ARG A 534 10.492 35.837 33.785 1.00 91.30 A O
ANISOU 4246 O ARG A 534 7934 10968 15786 -3933 6120 -9985 A O
ATOM 4247 CB ARG A 534 7.850 34.142 34.844 1.00 80.22 A C
ANISOU 4247 CB ARG A 534 7157 9298 14024 -3018 5416 -8872 A C
ATOM 4248 CG ARG A 534 6.398 34.138 34.392 1.00 84.41 A C
ANISOU 4248 CG ARG A 534 8126 9136 14809 -2823 5477 -8222 A C
ATOM 4249 CD ARG A 534 5.396 33.985 35.517 1.00 86.60 A C
ANISOU 4249 CD ARG A 534 8519 9425 14959 -2678 5361 -8149 A C
ATOM 4250 NE ARG A 534 4.034 34.031 34.991 1.00 83.29 A N
ANISOU 4250 NE ARG A 534 8489 8360 14798 -2514 5446 -7539 A N
ATOM 4251 CZ ARG A 534 3.397 32.996 34.455 1.00 85.43 A C
ANISOU 4251 CZ ARG A 534 8994 8542 14922 -2135 5116 -6954 A C
ATOM 4252 NH1 ARG A 534 3.985 31.807 34.391 1.00 68.22 A N1+
ANISOU 4252 NH1 ARG A 534 6738 6830 12351 -1863 4691 -6880 A N1+
ATOM 4253 NH2 ARG A 534 2.164 33.138 33.987 1.00 70.53 A N
ANISOU 4253 NH2 ARG A 534 7416 6114 13269 -2025 5224 -6448 A N
ATOM 4254 N TRP A 535 11.030 33.796 34.625 1.00 85.42 A N
ANISOU 4254 N TRP A 535 6949 11322 14183 -3274 5219 -9877 A N
ATOM 4255 CA TRP A 535 12.389 34.112 35.048 1.00 89.07 A C
ANISOU 4255 CA TRP A 535 6918 12474 14452 -3565 5274 -10596 A C
ATOM 4256 C TRP A 535 13.254 34.480 33.838 1.00 94.05 A C
ANISOU 4256 C TRP A 535 7454 12967 15312 -3801 5502 -10681 A C
ATOM 4257 O TRP A 535 13.981 35.476 33.897 1.00 99.13 A O
ANISOU 4257 O TRP A 535 7831 13697 16138 -4297 5887 -11272 A O
ATOM 4258 CB TRP A 535 12.995 32.930 35.832 1.00 87.84 A C
ANISOU 4258 CB TRP A 535 6488 13216 13671 -3166 4741 -10696 A C
ATOM 4259 CG TRP A 535 14.488 32.960 36.030 1.00 92.99 A C
ANISOU 4259 CG TRP A 535 6609 14686 14039 -3337 4694 -11319 A C
ATOM 4260 CD1 TRP A 535 15.376 31.978 35.701 1.00 95.79 A C
ANISOU 4260 CD1 TRP A 535 6767 15607 14022 -3009 4340 -11246 A C
ATOM 4261 CD2 TRP A 535 15.260 34.020 36.610 1.00 98.10 A C
ANISOU 4261 CD2 TRP A 535 6839 15693 14742 -3885 5029 -12124 A C
ATOM 4262 CE2 TRP A 535 16.611 33.605 36.605 1.00104.85 A C
ANISOU 4262 CE2 TRP A 535 7227 17384 15229 -3858 4832 -12510 A C
ATOM 4263 CE3 TRP A 535 14.941 35.286 37.140 1.00102.27 A C
ANISOU 4263 CE3 TRP A 535 7341 15924 15594 -4405 5496 -12574 A C
ATOM 4264 NE1 TRP A 535 16.649 32.350 36.058 1.00100.17 A N
ANISOU 4264 NE1 TRP A 535 6785 16897 14378 -3295 4408 -11946 A N
ATOM 4265 CZ2 TRP A 535 17.639 34.402 37.116 1.00109.94 A C
ANISOU 4265 CZ2 TRP A 535 7357 18613 15802 -4351 5071 -13344 A C
ATOM 4266 CZ3 TRP A 535 15.959 36.074 37.641 1.00109.56 A C
ANISOU 4266 CZ3 TRP A 535 7783 17381 16464 -4909 5755 -13406 A C
ATOM 4267 CH2 TRP A 535 17.291 35.631 37.632 1.00113.06 A C
ANISOU 4267 CH2 TRP A 535 7742 18694 16522 -4891 5536 -13795 A C
ATOM 4268 N LEU A 536 13.161 33.702 32.743 1.00 85.27 A N
ANISOU 4268 N LEU A 536 6568 11632 14198 -3471 5290 -10109 A N
ATOM 4269 CA LEU A 536 13.929 33.960 31.524 1.00 84.74 A C
ANISOU 4269 CA LEU A 536 6442 11421 14333 -3646 5481 -10118 A C
ATOM 4270 C LEU A 536 13.474 35.266 30.858 1.00 89.85 A C
ANISOU 4270 C LEU A 536 7311 11260 15567 -4060 6077 -10090 A C
ATOM 4271 O LEU A 536 14.331 36.068 30.488 1.00 92.55 A O
ANISOU 4271 O LEU A 536 7445 11610 16110 -4476 6440 -10517 A O
ATOM 4272 CB LEU A 536 13.860 32.787 30.530 1.00 79.89 A C
ANISOU 4272 CB LEU A 536 6037 10759 13561 -3179 5111 -9500 A C
ATOM 4273 CG LEU A 536 14.402 31.415 30.979 1.00 82.90 A C
ANISOU 4273 CG LEU A 536 6243 11880 13373 -2716 4559 -9456 A C
ATOM 4274 CD1 LEU A 536 14.259 30.390 29.875 1.00 78.31 A C
ANISOU 4274 CD1 LEU A 536 5929 11105 12721 -2317 4294 -8842 A C
ATOM 4275 CD2 LEU A 536 15.856 31.479 31.429 1.00 89.67 A C
ANISOU 4275 CD2 LEU A 536 6563 13570 13939 -2876 4511 -10117 A C
ATOM 4276 N ARG A 537 12.137 35.497 30.752 1.00 84.78 A N
ANISOU 4276 N ARG A 537 7081 9943 15189 -3946 6199 -9604 A N
ATOM 4277 CA ARG A 537 11.538 36.710 30.171 1.00 85.84 A C
ANISOU 4277 CA ARG A 537 7476 9273 15867 -4248 6775 -9485 A C
ATOM 4278 C ARG A 537 11.978 37.980 30.918 1.00 95.64 A C
ANISOU 4278 C ARG A 537 8498 10513 17329 -4804 7279 -10204 A C
ATOM 4279 O ARG A 537 12.246 39.003 30.280 1.00 97.58 A O
ANISOU 4279 O ARG A 537 8792 10309 17975 -5175 7814 -10352 A O
ATOM 4280 CB ARG A 537 10.007 36.625 30.169 1.00 83.44 A C
ANISOU 4280 CB ARG A 537 7593 8401 15711 -3968 6749 -8872 A C
ATOM 4281 CG ARG A 537 9.425 36.332 28.803 1.00 91.47 A C
ANISOU 4281 CG ARG A 537 8940 8921 16894 -3703 6724 -8160 A C
ATOM 4282 CD ARG A 537 7.955 36.691 28.742 1.00 94.05 A C
ANISOU 4282 CD ARG A 537 9642 8613 17479 -3565 6894 -7660 A C
ATOM 4283 NE ARG A 537 7.738 38.064 28.280 1.00106.56 A N
ANISOU 4283 NE ARG A 537 11365 9564 19560 -3884 7542 -7695 A N
ATOM 4284 CZ ARG A 537 6.552 38.569 27.953 1.00124.58 A C
ANISOU 4284 CZ ARG A 537 13975 11226 22133 -3773 7802 -7224 A C
ATOM 4285 NH1 ARG A 537 5.456 37.821 28.033 1.00111.76 A N1+
ANISOU 4285 NH1 ARG A 537 12556 9554 20356 -3384 7456 -6705 A N1+
ATOM 4286 NH2 ARG A 537 6.451 39.824 27.536 1.00115.67 A N
ANISOU 4286 NH2 ARG A 537 12974 9529 21446 -4042 8429 -7264 A N
ATOM 4287 N LEU A 538 12.063 37.901 32.262 1.00 94.12 A N
ANISOU 4287 N LEU A 538 8068 10828 16864 -4865 7127 -10657 A N
ATOM 4288 CA LEU A 538 12.495 38.998 33.123 1.00 99.83 A C
ANISOU 4288 CA LEU A 538 8543 11664 17724 -5400 7560 -11411 A C
ATOM 4289 C LEU A 538 13.954 39.368 32.836 1.00106.91 A C
ANISOU 4289 C LEU A 538 9034 12995 18594 -5806 7750 -12034 A C
ATOM 4290 O LEU A 538 14.288 40.559 32.788 1.00109.90 A O
ANISOU 4290 O LEU A 538 9350 13083 19324 -6343 8340 -12505 A O
ATOM 4291 CB LEU A 538 12.309 38.604 34.606 1.00101.37 A C
ANISOU 4291 CB LEU A 538 8541 12447 17528 -5295 7244 -11717 A C
ATOM 4292 CG LEU A 538 12.421 39.703 35.658 1.00112.77 A C
ANISOU 4292 CG LEU A 538 9788 13961 19098 -5807 7670 -12441 A C
ATOM 4293 CD1 LEU A 538 11.185 40.632 35.652 1.00112.93 A C
ANISOU 4293 CD1 LEU A 538 10231 13073 19605 -5929 8147 -12187 A C
ATOM 4294 CD2 LEU A 538 12.599 39.102 37.044 1.00117.80 A C
ANISOU 4294 CD2 LEU A 538 10110 15436 19213 -5669 7253 -12801 A C
ATOM 4295 N CYS A 539 14.811 38.347 32.631 1.00102.15 A N
ANISOU 4295 N CYS A 539 8167 13066 17580 -5547 7275 -12030 A N
ATOM 4296 CA CYS A 539 16.238 38.511 32.351 1.00105.80 A C
ANISOU 4296 CA CYS A 539 8202 14058 17939 -5861 7366 -12588 A C
ATOM 4297 C CYS A 539 16.484 39.124 30.969 1.00111.51 A C
ANISOU 4297 C CYS A 539 9108 14156 19103 -6088 7795 -12403 A C
ATOM 4298 O CYS A 539 17.418 39.914 30.828 1.00114.92 A O
ANISOU 4298 O CYS A 539 9276 14696 19693 -6596 8202 -12987 A O
ATOM 4299 CB CYS A 539 16.971 37.183 32.492 1.00104.23 A C
ANISOU 4299 CB CYS A 539 7706 14731 17165 -5433 6726 -12548 A C
ATOM 4300 SG CYS A 539 17.198 36.621 34.196 1.00109.91 A S
ANISOU 4300 SG CYS A 539 8030 16436 17294 -5276 6305 -13011 A S
ATOM 4301 N ILE A 540 15.662 38.777 29.963 1.00105.77 A N
ANISOU 4301 N ILE A 540 8821 12807 18561 -5726 7720 -11611 A N
ATOM 4302 CA ILE A 540 15.828 39.283 28.595 1.00107.08 A C
ANISOU 4302 CA ILE A 540 9189 12385 19112 -5865 8096 -11343 A C
ATOM 4303 C ILE A 540 15.542 40.783 28.549 1.00115.52 A C
ANISOU 4303 C ILE A 540 10427 12750 20717 -6370 8856 -11584 A C
ATOM 4304 O ILE A 540 16.360 41.535 28.008 1.00119.64 A O
ANISOU 4304 O ILE A 540 10831 13145 21483 -6793 9310 -11934 A O
ATOM 4305 CB ILE A 540 14.976 38.482 27.573 1.00105.43 A C
ANISOU 4305 CB ILE A 540 9388 11753 18916 -5329 7799 -10438 A C
ATOM 4306 CG1 ILE A 540 15.558 37.060 27.347 1.00103.57 A C
ANISOU 4306 CG1 ILE A 540 8976 12177 18198 -4905 7157 -10259 A C
ATOM 4307 CG2 ILE A 540 14.813 39.241 26.247 1.00107.18 A C
ANISOU 4307 CG2 ILE A 540 9906 11212 19605 -5470 8289 -10087 A C
ATOM 4308 CD1 ILE A 540 16.998 36.977 26.577 1.00114.96 A C
ANISOU 4308 CD1 ILE A 540 10096 14014 19567 -5089 7199 -10574 A C
ATOM 4309 N ARG A 541 14.405 41.210 29.140 1.00111.31 A N
ANISOU 4309 N ARG A 541 10167 11767 20360 -6328 9013 -11413 A N
ATOM 4310 CA ARG A 541 14.010 42.615 29.232 1.00114.69 A C
ANISOU 4310 CA ARG A 541 10790 11498 21287 -6760 9751 -11623 A C
ATOM 4311 C ARG A 541 15.080 43.408 29.977 1.00120.63 A C
ANISOU 4311 C ARG A 541 11273 12711 21850 -7171 9804 -12218 A C
ATOM 4312 O ARG A 541 15.429 44.507 29.538 1.00119.93 A O
ANISOU 4312 O ARG A 541 11408 12259 21900 -7343 10040 -12021 A O
ATOM 4313 CB ARG A 541 12.644 42.771 29.915 1.00114.45 A C
ANISOU 4313 CB ARG A 541 11068 11065 21354 -6554 9764 -11309 A C
ATOM 4314 CG ARG A 541 11.468 42.449 28.993 1.00126.67 A C
ANISOU 4314 CG ARG A 541 13084 11976 23070 -6075 9681 -10376 A C
ATOM 4315 CD ARG A 541 10.125 42.752 29.636 1.00139.06 A C
ANISOU 4315 CD ARG A 541 14955 13116 24766 -5905 9762 -10075 A C
ATOM 4316 NE ARG A 541 9.938 44.184 29.891 1.00144.77 A N
ANISOU 4316 NE ARG A 541 16121 13671 25216 -5733 9456 -9425 A N
ATOM 4317 CZ ARG A 541 9.193 44.992 29.142 1.00151.23 A C
ANISOU 4317 CZ ARG A 541 17470 14057 25932 -5315 9176 -8398 A C
ATOM 4318 NH1 ARG A 541 8.544 44.518 28.084 1.00140.83 A N1+
ANISOU 4318 NH1 ARG A 541 16172 12054 25281 -5405 9942 -8448 A N1+
ATOM 4319 NH2 ARG A 541 9.081 46.276 29.451 1.00139.42 A N
ANISOU 4319 NH2 ARG A 541 16057 12057 24859 -5718 9880 -8768 A N
ATOM 4320 N ALA A 542 15.667 42.804 31.047 1.00118.19 A N
ANISOU 4320 N ALA A 542 10503 13277 21128 -7235 9457 -12815 A N
ATOM 4321 CA ALA A 542 16.744 43.416 31.835 1.00118.33 A C
ANISOU 4321 CA ALA A 542 10351 13884 20723 -7383 9165 -13029 A C
ATOM 4322 C ALA A 542 17.981 43.696 30.985 1.00121.05 A C
ANISOU 4322 C ALA A 542 10674 14404 20915 -7400 9001 -12802 A C
ATOM 4323 O ALA A 542 18.748 44.603 31.310 1.00121.78 A O
ANISOU 4323 O ALA A 542 10812 14641 20817 -7526 8879 -12743 A O
ATOM 4324 CB ALA A 542 17.118 42.522 33.005 1.00119.25 A C
ANISOU 4324 CB ALA A 542 10065 14954 20291 -7219 8627 -13391 A C
ATOM 4325 N GLY A 543 18.150 42.933 29.906 1.00117.81 A N
ANISOU 4325 N GLY A 543 10072 13940 20751 -7456 9243 -12987 A N
ATOM 4326 CA GLY A 543 19.269 43.078 28.984 1.00117.80 A C
ANISOU 4326 CA GLY A 543 9973 14080 20704 -7553 9235 -12934 A C
ATOM 4327 C GLY A 543 20.476 42.258 29.381 1.00120.69 A C
ANISOU 4327 C GLY A 543 9914 15471 20470 -7378 8618 -13118 A C
ATOM 4328 O GLY A 543 21.613 42.622 29.058 1.00120.90 A O
ANISOU 4328 O GLY A 543 9847 15766 20324 -7474 8502 -13084 A O
ATOM 4329 N TRP A 544 20.229 41.136 30.073 1.00118.08 A N
ANISOU 4329 N TRP A 544 9183 15738 19946 -7274 8436 -13618 A N
ATOM 4330 CA TRP A 544 21.273 40.210 30.498 1.00118.39 A C
ANISOU 4330 CA TRP A 544 8738 16820 19424 -7091 7915 -13911 A C
ATOM 4331 C TRP A 544 21.650 39.312 29.312 1.00121.27 A C
ANISOU 4331 C TRP A 544 9013 17289 19773 -6853 7771 -13714 A C
ATOM 4332 O TRP A 544 20.797 38.608 28.767 1.00117.60 A O
ANISOU 4332 O TRP A 544 8732 16499 19450 -6557 7713 -13388 A O
ATOM 4333 CB TRP A 544 20.812 39.383 31.723 1.00117.15 A C
ANISOU 4333 CB TRP A 544 8307 17275 18929 -6888 7598 -14249 A C
ATOM 4334 CG TRP A 544 21.923 38.782 32.544 1.00118.17 A C
ANISOU 4334 CG TRP A 544 8028 18491 18381 -6647 7017 -14416 A C
ATOM 4335 CD1 TRP A 544 23.264 38.946 32.361 1.00120.54 A C
ANISOU 4335 CD1 TRP A 544 8239 19203 18359 -6586 6736 -14217 A C
ATOM 4336 CD2 TRP A 544 21.777 37.927 33.688 1.00118.07 A C
ANISOU 4336 CD2 TRP A 544 7738 19223 17900 -6337 6595 -14622 A C
ATOM 4337 CE2 TRP A 544 23.076 37.606 34.139 1.00121.47 A C
ANISOU 4337 CE2 TRP A 544 7976 20449 17729 -6053 6063 -14436 A C
ATOM 4338 CE3 TRP A 544 20.675 37.399 34.378 1.00118.14 A C
ANISOU 4338 CE3 TRP A 544 7771 19222 17894 -6151 6527 -14698 A C
ATOM 4339 NE1 TRP A 544 23.961 38.273 33.334 1.00120.61 A N
ANISOU 4339 NE1 TRP A 544 7900 20150 17775 -6306 6241 -14362 A N
ATOM 4340 CZ2 TRP A 544 23.303 36.768 35.237 1.00121.38 A C
ANISOU 4340 CZ2 TRP A 544 7667 21300 17151 -5692 5597 -14565 A C
ATOM 4341 CZ3 TRP A 544 20.899 36.575 35.470 1.00119.43 A C
ANISOU 4341 CZ3 TRP A 544 7674 20249 17455 -5758 5999 -14760 A C
ATOM 4342 CH2 TRP A 544 22.198 36.276 35.897 1.00120.80 A C
ANISOU 4342 CH2 TRP A 544 7594 21246 17059 -5533 5557 -14700 A C
ATOM 4343 N GLU A 545 22.912 39.397 28.878 1.00119.86 A N
ANISOU 4343 N GLU A 545 8602 17511 19427 -6964 7702 -13834 A N
ATOM 4344 CA GLU A 545 23.446 38.611 27.769 1.00120.14 A C
ANISOU 4344 CA GLU A 545 8462 17730 19454 -6830 7635 -13809 A C
ATOM 4345 C GLU A 545 23.593 37.133 28.130 1.00123.32 A C
ANISOU 4345 C GLU A 545 8573 18917 19365 -6319 7043 -13816 A C
ATOM 4346 O GLU A 545 23.483 36.280 27.251 1.00119.20 A O
ANISOU 4346 O GLU A 545 8221 18267 18802 -5918 6798 -13313 A O
ATOM 4347 CB GLU A 545 24.808 39.166 27.333 1.00121.94 A C
ANISOU 4347 CB GLU A 545 8659 18192 19480 -6906 7504 -13612 A C
ATOM 4348 CG GLU A 545 24.711 40.385 26.434 1.00129.72 A C
ANISOU 4348 CG GLU A 545 10342 18233 20712 -6859 7592 -12642 A C
ATOM 4349 CD GLU A 545 25.955 41.250 26.371 1.00145.12 A C
ANISOU 4349 CD GLU A 545 12918 20160 22061 -6240 6673 -11099 A C
ATOM 4350 OE1 GLU A 545 27.013 40.753 25.917 1.00138.34 A O
ANISOU 4350 OE1 GLU A 545 11757 19776 21031 -6213 6557 -11250 A O
ATOM 4351 OE2 GLU A 545 25.863 42.439 26.753 1.00141.89 A O1-
ANISOU 4351 OE2 GLU A 545 12624 19438 21849 -6575 6955 -11220 A O1-
ATOM 4352 N ASP A 546 23.846 36.841 29.420 1.00121.75 A N
ANISOU 4352 N ASP A 546 8080 19473 18707 -6191 6694 -14109 A N
ATOM 4353 CA ASP A 546 24.078 35.498 29.964 1.00121.51 A C
ANISOU 4353 CA ASP A 546 7720 20314 18134 -5689 6135 -14179 A C
ATOM 4354 C ASP A 546 22.870 34.561 29.827 1.00118.97 A C
ANISOU 4354 C ASP A 546 7926 19513 17764 -5057 5758 -13318 A C
ATOM 4355 O ASP A 546 23.059 33.342 29.799 1.00116.21 A O
ANISOU 4355 O ASP A 546 7545 19612 16999 -4491 5250 -12986 A O
ATOM 4356 CB ASP A 546 24.483 35.589 31.448 1.00123.97 A C
ANISOU 4356 CB ASP A 546 7898 21280 17924 -5545 5759 -14220 A C
ATOM 4357 CG ASP A 546 25.725 36.422 31.751 1.00131.92 A C
ANISOU 4357 CG ASP A 546 9218 22267 18639 -5467 5464 -13527 A C
ATOM 4358 OD1 ASP A 546 26.092 37.278 30.915 1.00131.71 A O
ANISOU 4358 OD1 ASP A 546 9371 21740 18933 -5768 5754 -13388 A O
ATOM 4359 OD2 ASP A 546 26.258 36.304 32.876 1.00137.60 A O1-
ANISOU 4359 OD2 ASP A 546 10012 23403 18865 -5135 4991 -13147 A O1-
ATOM 4360 N VAL A 547 21.648 35.121 29.741 1.00112.75 A N
ANISOU 4360 N VAL A 547 7617 17831 17393 -5151 6024 -12967 A N
ATOM 4361 CA VAL A 547 20.404 34.357 29.644 1.00106.83 A C
ANISOU 4361 CA VAL A 547 7363 16596 16630 -4626 5722 -12193 A C
ATOM 4362 C VAL A 547 20.027 33.990 28.174 1.00106.03 A C
ANISOU 4362 C VAL A 547 7679 15832 16776 -4388 5719 -11487 A C
ATOM 4363 O VAL A 547 19.141 33.150 27.987 1.00102.34 A O
ANISOU 4363 O VAL A 547 7576 15084 16225 -3915 5406 -10846 A O
ATOM 4364 CB VAL A 547 19.260 35.124 30.357 1.00110.90 A C
ANISOU 4364 CB VAL A 547 8144 16569 17425 -4822 5989 -12187 A C
ATOM 4365 CG1 VAL A 547 18.668 36.217 29.475 1.00110.28 A C
ANISOU 4365 CG1 VAL A 547 8437 15500 17966 -5172 6554 -11978 A C
ATOM 4366 CG2 VAL A 547 18.177 34.175 30.861 1.00106.29 A C
ANISOU 4366 CG2 VAL A 547 7861 15920 16606 -4271 5555 -11635 A C
ATOM 4367 N ILE A 548 20.683 34.601 27.149 1.00102.21 A N
ANISOU 4367 N ILE A 548 7137 15118 16580 -4721 6070 -11611 A N
ATOM 4368 CA ILE A 548 20.386 34.349 25.726 1.00 97.83 A C
ANISOU 4368 CA ILE A 548 6943 13972 16255 -4537 6106 -10989 A C
ATOM 4369 C ILE A 548 20.442 32.821 25.407 1.00 98.92 A C
ANISOU 4369 C ILE A 548 7145 14467 15973 -3905 5511 -10512 A C
ATOM 4370 O ILE A 548 19.444 32.328 24.868 1.00 94.34 A O
ANISOU 4370 O ILE A 548 7002 13365 15478 -3575 5371 -9850 A O
ATOM 4371 CB ILE A 548 21.266 35.197 24.752 1.00103.75 A C
ANISOU 4371 CB ILE A 548 7556 14547 17318 -4995 6570 -11270 A C
ATOM 4372 CG1 ILE A 548 21.026 36.708 24.965 1.00107.69 A C
ANISOU 4372 CG1 ILE A 548 8107 14521 18289 -5597 7230 -11646 A C
ATOM 4373 CG2 ILE A 548 21.037 34.810 23.269 1.00100.23 A C
ANISOU 4373 CG2 ILE A 548 7452 13592 17038 -4751 6554 -10615 A C
ATOM 4374 CD1 ILE A 548 22.132 37.636 24.379 1.00120.94 A C
ANISOU 4374 CD1 ILE A 548 9518 16224 20210 -6161 7735 -12176 A C
ATOM 4375 N PRO A 549 21.508 32.038 25.762 1.00 97.48 A N
ANISOU 4375 N PRO A 549 6552 15156 15328 -3707 5165 -10815 A N
ATOM 4376 CA PRO A 549 21.489 30.598 25.425 1.00 93.83 A C
ANISOU 4376 CA PRO A 549 6216 14937 14499 -3087 4658 -10322 A C
ATOM 4377 C PRO A 549 20.460 29.770 26.217 1.00 94.59 A C
ANISOU 4377 C PRO A 549 6588 14984 14368 -2637 4304 -9925 A C
ATOM 4378 O PRO A 549 20.139 28.671 25.772 1.00 91.67 A O
ANISOU 4378 O PRO A 549 6485 14523 13824 -2165 3986 -9391 A O
ATOM 4379 CB PRO A 549 22.921 30.141 25.725 1.00 99.12 A C
ANISOU 4379 CB PRO A 549 6341 16578 14741 -3016 4447 -10812 A C
ATOM 4380 CG PRO A 549 23.412 31.105 26.760 1.00108.40 A C
ANISOU 4380 CG PRO A 549 7098 18171 15919 -3493 4694 -11562 A C
ATOM 4381 CD PRO A 549 22.795 32.417 26.396 1.00104.04 A C
ANISOU 4381 CD PRO A 549 6789 16792 15948 -4027 5242 -11605 A C
ATOM 4382 N LEU A 550 19.946 30.283 27.366 1.00 91.63 A N
ANISOU 4382 N LEU A 550 6161 14657 13997 -2795 4380 -10190 A N
ATOM 4383 CA LEU A 550 18.934 29.604 28.188 1.00 88.25 A C
ANISOU 4383 CA LEU A 550 5988 14171 13373 -2416 4090 -9851 A C
ATOM 4384 C LEU A 550 17.528 29.828 27.629 1.00 83.82 A C
ANISOU 4384 C LEU A 550 5967 12682 13200 -2404 4240 -9271 A C
ATOM 4385 O LEU A 550 16.721 28.898 27.605 1.00 77.84 A O
ANISOU 4385 O LEU A 550 5531 11747 12297 -1980 3948 -8747 A O
ATOM 4386 CB LEU A 550 18.979 30.071 29.658 1.00 92.31 A C
ANISOU 4386 CB LEU A 550 6209 15143 13721 -2595 4118 -10386 A C
ATOM 4387 CG LEU A 550 20.165 29.610 30.519 1.00101.97 A C
ANISOU 4387 CG LEU A 550 6898 17432 14415 -2454 3849 -10890 A C
ATOM 4388 CD1 LEU A 550 20.259 30.444 31.799 1.00106.22 A C
ANISOU 4388 CD1 LEU A 550 7104 18359 14896 -2821 4017 -11535 A C
ATOM 4389 CD2 LEU A 550 20.056 28.119 30.874 1.00103.81 A C
ANISOU 4389 CD2 LEU A 550 7242 18045 14157 -1759 3337 -10467 A C
ATOM 4390 N ALA A 551 17.239 31.077 27.205 1.00 80.26 A N
ANISOU 4390 N ALA A 551 5607 11657 13232 -2870 4719 -9376 A N
ATOM 4391 CA ALA A 551 15.965 31.474 26.614 1.00 76.33 A C
ANISOU 4391 CA ALA A 551 5577 10300 13125 -2888 4928 -8856 A C
ATOM 4392 C ALA A 551 15.773 30.773 25.263 1.00 77.57 A C
ANISOU 4392 C ALA A 551 6018 10133 13323 -2607 4794 -8259 A C
ATOM 4393 O ALA A 551 14.677 30.286 24.986 1.00 73.38 A O
ANISOU 4393 O ALA A 551 5864 9183 12836 -2340 4665 -7701 A O
ATOM 4394 CB ALA A 551 15.903 32.987 26.456 1.00 79.35 A C
ANISOU 4394 CB ALA A 551 5952 10209 13987 -3434 5515 -9151 A C
ATOM 4395 N LEU A 552 16.848 30.686 24.452 1.00 76.75 A N
ANISOU 4395 N LEU A 552 5715 10265 13182 -2672 4818 -8398 A N
ATOM 4396 CA LEU A 552 16.852 29.998 23.156 1.00 74.82 A C
ANISOU 4396 CA LEU A 552 5686 9805 12938 -2424 4689 -7905 A C
ATOM 4397 C LEU A 552 16.602 28.497 23.335 1.00 77.61 A C
ANISOU 4397 C LEU A 552 6173 10442 12875 -1878 4175 -7545 A C
ATOM 4398 O LEU A 552 15.896 27.889 22.525 1.00 73.12 A O
ANISOU 4398 O LEU A 552 5948 9498 12338 -1632 4056 -6992 A O
ATOM 4399 CB LEU A 552 18.186 30.207 22.416 1.00 77.57 A C
ANISOU 4399 CB LEU A 552 5736 10441 13298 -2623 4824 -8218 A C
ATOM 4400 CG LEU A 552 18.424 31.553 21.733 1.00 85.18 A C
ANISOU 4400 CG LEU A 552 6675 10971 14719 -3127 5378 -8413 A C
ATOM 4401 CD1 LEU A 552 19.890 31.713 21.374 1.00 88.65 A C
ANISOU 4401 CD1 LEU A 552 6716 11882 15084 -3349 5475 -8880 A C
ATOM 4402 CD2 LEU A 552 17.568 31.706 20.481 1.00 84.22 A C
ANISOU 4402 CD2 LEU A 552 6977 10117 14907 -3059 5549 -7791 A C
ATOM 4403 N ALA A 553 17.185 27.913 24.403 1.00 77.41 A N
ANISOU 4403 N ALA A 553 5872 11090 12449 -1693 3895 -7866 A N
ATOM 4404 CA ALA A 553 17.047 26.505 24.756 1.00 75.54 A C
ANISOU 4404 CA ALA A 553 5742 11171 11786 -1162 3446 -7581 A C
ATOM 4405 C ALA A 553 15.581 26.154 25.057 1.00 75.59 A C
ANISOU 4405 C ALA A 553 6173 10706 11842 -960 3345 -7103 A C
ATOM 4406 O ALA A 553 15.010 25.303 24.373 1.00 72.22 A O
ANISOU 4406 O ALA A 553 6070 10005 11365 -671 3176 -6598 A O
ATOM 4407 CB ALA A 553 17.929 26.176 25.953 1.00 79.76 A C
ANISOU 4407 CB ALA A 553 5873 12526 11907 -1036 3241 -8055 A C
ATOM 4408 N MET A 554 14.947 26.881 26.009 1.00 72.38 A N
ANISOU 4408 N MET A 554 5763 10182 11557 -1153 3482 -7278 A N
ATOM 4409 CA MET A 554 13.551 26.661 26.401 1.00 68.66 A C
ANISOU 4409 CA MET A 554 5652 9297 11140 -1002 3414 -6883 A C
ATOM 4410 C MET A 554 12.573 26.939 25.236 1.00 68.74 A C
ANISOU 4410 C MET A 554 6033 8571 11514 -1076 3595 -6379 A C
ATOM 4411 O MET A 554 11.551 26.258 25.124 1.00 63.77 A O
ANISOU 4411 O MET A 554 5731 7669 10828 -820 3427 -5914 A O
ATOM 4412 CB MET A 554 13.174 27.491 27.633 1.00 72.72 A C
ANISOU 4412 CB MET A 554 6046 9855 11730 -1235 3569 -7231 A C
ATOM 4413 CG MET A 554 11.938 26.954 28.355 1.00 73.74 A C
ANISOU 4413 CG MET A 554 6469 9798 11750 -976 3388 -6892 A C
ATOM 4414 SD MET A 554 11.412 27.926 29.780 1.00 79.67 A S
ANISOU 4414 SD MET A 554 7115 10546 12609 -1246 3586 -7265 A S
ATOM 4415 CE MET A 554 10.023 26.958 30.319 1.00 72.83 A C
ANISOU 4415 CE MET A 554 6634 9479 11560 -844 3305 -6744 A C
ATOM 4416 N ALA A 555 12.900 27.907 24.365 1.00 67.57 A N
ANISOU 4416 N ALA A 555 5826 8133 11714 -1414 3942 -6470 A N
ATOM 4417 CA ALA A 555 12.068 28.255 23.213 1.00 65.95 A C
ANISOU 4417 CA ALA A 555 5933 7289 11835 -1471 4141 -6000 A C
ATOM 4418 C ALA A 555 12.128 27.188 22.110 1.00 69.01 A C
ANISOU 4418 C ALA A 555 6492 7662 12065 -1179 3901 -5582 A C
ATOM 4419 O ALA A 555 11.189 27.099 21.312 1.00 67.00 A O
ANISOU 4419 O ALA A 555 6537 6967 11952 -1103 3934 -5105 A O
ATOM 4420 CB ALA A 555 12.494 29.602 22.650 1.00 69.35 A C
ANISOU 4420 CB ALA A 555 6249 7441 12660 -1895 4613 -6231 A C
ATOM 4421 N THR A 556 13.215 26.383 22.059 1.00 66.49 A N
ANISOU 4421 N THR A 556 5975 7846 11441 -1011 3670 -5766 A N
ATOM 4422 CA THR A 556 13.367 25.360 21.019 1.00 64.73 A C
ANISOU 4422 CA THR A 556 5905 7629 11059 -742 3464 -5418 A C
ATOM 4423 C THR A 556 13.162 23.922 21.541 1.00 66.05 A C
ANISOU 4423 C THR A 556 6213 8059 10823 -304 3067 -5223 A C
ATOM 4424 O THR A 556 12.870 23.039 20.730 1.00 62.21 A O
ANISOU 4424 O THR A 556 5973 7423 10243 -82 2921 -4838 A O
ATOM 4425 CB THR A 556 14.724 25.467 20.303 1.00 73.85 A C
ANISOU 4425 CB THR A 556 6784 9086 12188 -843 3531 -5690 A C
ATOM 4426 CG2 THR A 556 14.831 26.708 19.443 1.00 71.82 A C
ANISOU 4426 CG2 THR A 556 6492 8459 12339 -1230 3943 -5739 A C
ATOM 4427 OG1 THR A 556 15.785 25.407 21.253 1.00 77.81 A O
ANISOU 4427 OG1 THR A 556 6914 10200 12451 -845 3438 -6203 A O
ATOM 4428 N GLU A 557 13.323 23.672 22.864 1.00 64.20 A N
ANISOU 4428 N GLU A 557 5833 8219 10340 -177 2911 -5487 A N
ATOM 4429 CA GLU A 557 13.134 22.313 23.402 1.00 62.63 A C
ANISOU 4429 CA GLU A 557 5792 8252 9753 263 2575 -5287 A C
ATOM 4430 C GLU A 557 11.654 21.998 23.593 1.00 61.67 A C
ANISOU 4430 C GLU A 557 6050 7691 9689 357 2528 -4875 A C
ATOM 4431 O GLU A 557 11.278 20.833 23.715 1.00 60.37 A O
ANISOU 4431 O GLU A 557 6120 7548 9269 693 2304 -4598 A O
ATOM 4432 CB GLU A 557 13.898 22.078 24.715 1.00 67.14 A C
ANISOU 4432 CB GLU A 557 6066 9456 9988 421 2420 -5683 A C
ATOM 4433 CG GLU A 557 15.403 22.037 24.556 1.00 83.80 A C
ANISOU 4433 CG GLU A 557 7800 12131 11910 456 2379 -6042 A C
ATOM 4434 CD GLU A 557 16.162 21.760 25.836 1.00111.08 A C
ANISOU 4434 CD GLU A 557 10928 16293 14983 648 2212 -6422 A C
ATOM 4435 OE1 GLU A 557 16.091 22.580 26.783 1.00117.40 A O
ANISOU 4435 OE1 GLU A 557 11496 17259 15852 386 2331 -6797 A O
ATOM 4436 OE2 GLU A 557 16.921 20.768 25.843 1.00101.39 A O1-
ANISOU 4436 OE2 GLU A 557 9666 15480 13378 1068 1976 -6354 A O1-
ATOM 4437 N GLN A 558 10.818 23.025 23.593 1.00 56.14 A N
ANISOU 4437 N GLN A 558 5417 6589 9327 65 2760 -4832 A N
ATOM 4438 CA GLN A 558 9.373 22.867 23.691 1.00 52.87 A C
ANISOU 4438 CA GLN A 558 5332 5755 9002 115 2748 -4446 A C
ATOM 4439 C GLN A 558 8.734 23.849 22.709 1.00 58.23 A C
ANISOU 4439 C GLN A 558 6108 5932 10085 -166 3035 -4244 A C
ATOM 4440 O GLN A 558 9.412 24.754 22.222 1.00 61.08 A O
ANISOU 4440 O GLN A 558 6276 6268 10664 -419 3271 -4460 A O
ATOM 4441 CB GLN A 558 8.871 23.022 25.142 1.00 53.70 A C
ANISOU 4441 CB GLN A 558 5411 5977 9015 144 2703 -4605 A C
ATOM 4442 CG GLN A 558 9.214 24.338 25.829 1.00 61.55 A C
ANISOU 4442 CG GLN A 558 6122 7052 10213 -186 2948 -5050 A C
ATOM 4443 CD GLN A 558 8.269 25.455 25.461 1.00 67.13 A C
ANISOU 4443 CD GLN A 558 6952 7211 11342 -478 3263 -4907 A C
ATOM 4444 NE2 GLN A 558 8.808 26.584 25.023 1.00 54.60 A N
ANISOU 4444 NE2 GLN A 558 5184 5516 10044 -803 3574 -5154 A N
ATOM 4445 OE1 GLN A 558 7.052 25.310 25.531 1.00 58.88 A O
ANISOU 4445 OE1 GLN A 558 6169 5836 10367 -408 3251 -4565 A O
ATOM 4446 N GLY A 559 7.461 23.646 22.408 1.00 52.60 A N
ANISOU 4446 N GLY A 559 5687 4845 9452 -109 3026 -3828 A N
ATOM 4447 CA GLY A 559 6.732 24.460 21.444 1.00 50.93 A C
ANISOU 4447 CA GLY A 559 5589 4187 9574 -297 3278 -3554 A C
ATOM 4448 C GLY A 559 5.391 24.967 21.898 1.00 55.28 A C
ANISOU 4448 C GLY A 559 6296 4413 10293 -353 3390 -3352 A C
ATOM 4449 O GLY A 559 4.549 25.312 21.065 1.00 54.67 A O
ANISOU 4449 O GLY A 559 6370 3999 10405 -398 3526 -3002 A O
ATOM 4450 N ARG A 560 5.181 25.040 23.225 1.00 52.65 A N
ANISOU 4450 N ARG A 560 5915 4207 9881 -338 3340 -3567 A N
ATOM 4451 CA ARG A 560 3.957 25.567 23.814 1.00 51.08 A C
ANISOU 4451 CA ARG A 560 5841 3729 9837 -393 3456 -3424 A C
ATOM 4452 C ARG A 560 3.987 27.088 23.600 1.00 56.46 A C
ANISOU 4452 C ARG A 560 6410 4129 10911 -688 3863 -3557 A C
ATOM 4453 O ARG A 560 4.907 27.760 24.071 1.00 57.60 A O
ANISOU 4453 O ARG A 560 6325 4430 11132 -876 4015 -3995 A O
ATOM 4454 CB ARG A 560 3.851 25.160 25.291 1.00 50.67 A C
ANISOU 4454 CB ARG A 560 5758 3933 9561 -285 3285 -3643 A C
ATOM 4455 CG ARG A 560 2.545 25.552 25.960 1.00 62.83 A C
ANISOU 4455 CG ARG A 560 7446 5210 11215 -306 3365 -3474 A C
ATOM 4456 CD ARG A 560 2.516 25.077 27.395 1.00 64.24 A C
ANISOU 4456 CD ARG A 560 7590 5676 11143 -187 3190 -3695 A C
ATOM 4457 NE ARG A 560 1.399 25.661 28.129 1.00 59.75 A N
ANISOU 4457 NE ARG A 560 7109 4872 10723 -260 3321 -3628 A N
ATOM 4458 CZ ARG A 560 1.203 25.503 29.431 1.00 68.94 A C
ANISOU 4458 CZ ARG A 560 8246 6226 11722 -198 3231 -3813 A C
ATOM 4459 NH1 ARG A 560 2.041 24.770 30.152 1.00 52.03 A N1+
ANISOU 4459 NH1 ARG A 560 5990 4531 9246 -40 3008 -4062 A N1+
ATOM 4460 NH2 ARG A 560 0.163 26.075 30.024 1.00 60.10 A N
ANISOU 4460 NH2 ARG A 560 7209 4870 10756 -271 3370 -3740 A N
ATOM 4461 N MET A 561 3.038 27.593 22.788 1.00 52.94 A N
ANISOU 4461 N MET A 561 6127 3286 10703 -720 4054 -3172 A N
ATOM 4462 CA MET A 561 2.921 28.988 22.365 1.00 56.08 A C
ANISOU 4462 CA MET A 561 6487 3333 11485 -943 4486 -3176 A C
ATOM 4463 C MET A 561 2.974 29.974 23.511 1.00 58.90 A C
ANISOU 4463 C MET A 561 6730 3633 12017 -1145 4731 -3557 A C
ATOM 4464 O MET A 561 3.605 31.014 23.348 1.00 61.89 A O
ANISOU 4464 O MET A 561 6986 3877 12653 -1391 5081 -3813 A O
ATOM 4465 CB MET A 561 1.642 29.221 21.572 1.00 58.58 A C
ANISOU 4465 CB MET A 561 7011 3294 11953 -854 4605 -2648 A C
ATOM 4466 CG MET A 561 1.753 28.774 20.154 1.00 62.67 A C
ANISOU 4466 CG MET A 561 7595 3804 12413 -760 4532 -2321 A C
ATOM 4467 SD MET A 561 0.599 29.667 19.108 1.00 69.32 A S
ANISOU 4467 SD MET A 561 8575 4233 13529 -733 4857 -1804 A S
ATOM 4468 CE MET A 561 -0.729 28.575 19.137 1.00 63.45 A C
ANISOU 4468 CE MET A 561 8001 3565 12541 -509 4537 -1419 A C
ATOM 4469 N LYS A 562 2.356 29.644 24.668 1.00 51.61 A N
ANISOU 4469 N LYS A 562 5845 2815 10948 -1058 4567 -3621 A N
ATOM 4470 CA LYS A 562 2.383 30.481 25.872 1.00 54.14 A C
ANISOU 4470 CA LYS A 562 6052 3134 11386 -1242 4766 -4014 A C
ATOM 4471 C LYS A 562 3.823 30.816 26.277 1.00 60.73 A C
ANISOU 4471 C LYS A 562 6597 4291 12186 -1457 4838 -4595 A C
ATOM 4472 O LYS A 562 4.087 31.923 26.750 1.00 62.25 A O
ANISOU 4472 O LYS A 562 6669 4371 12614 -1735 5184 -4952 A O
ATOM 4473 CB LYS A 562 1.668 29.757 27.027 1.00 55.62 A C
ANISOU 4473 CB LYS A 562 6312 3501 11319 -1064 4483 -3992 A C
ATOM 4474 CG LYS A 562 1.465 30.589 28.282 1.00 60.85 A C
ANISOU 4474 CG LYS A 562 6888 4136 12095 -1232 4684 -4337 A C
ATOM 4475 CD LYS A 562 0.904 29.722 29.393 1.00 66.04 A C
ANISOU 4475 CD LYS A 562 7605 5044 12444 -1032 4366 -4325 A C
ATOM 4476 CE LYS A 562 0.645 30.505 30.647 1.00 67.09 A C
ANISOU 4476 CE LYS A 562 7656 5166 12669 -1191 4554 -4659 A C
ATOM 4477 NZ LYS A 562 0.217 29.622 31.757 1.00 69.39 A N1+
ANISOU 4477 NZ LYS A 562 7989 5748 12628 -987 4240 -4667 A N1+
ATOM 4478 N PHE A 563 4.750 29.859 26.076 1.00 56.70 A N
ANISOU 4478 N PHE A 563 5973 4193 11378 -1330 4530 -4696 A N
ATOM 4479 CA PHE A 563 6.141 30.036 26.445 1.00 59.79 A C
ANISOU 4479 CA PHE A 563 6053 4990 11674 -1497 4548 -5240 A C
ATOM 4480 C PHE A 563 7.036 30.421 25.244 1.00 65.49 A C
ANISOU 4480 C PHE A 563 6683 5638 12564 -1654 4742 -5280 A C
ATOM 4481 O PHE A 563 7.770 31.400 25.340 1.00 69.10 A O
ANISOU 4481 O PHE A 563 6940 6096 13220 -1973 5063 -5694 A O
ATOM 4482 CB PHE A 563 6.680 28.764 27.123 1.00 61.46 A C
ANISOU 4482 CB PHE A 563 6162 5770 11420 -1229 4102 -5364 A C
ATOM 4483 CG PHE A 563 5.931 28.180 28.307 1.00 62.44 A C
ANISOU 4483 CG PHE A 563 6381 6034 11309 -1025 3870 -5310 A C
ATOM 4484 CD1 PHE A 563 5.321 29.004 29.245 1.00 67.12 A C
ANISOU 4484 CD1 PHE A 563 6962 6486 12055 -1193 4070 -5489 A C
ATOM 4485 CD2 PHE A 563 5.917 26.802 28.530 1.00 63.60 A C
ANISOU 4485 CD2 PHE A 563 6626 6469 11072 -668 3476 -5110 A C
ATOM 4486 CE1 PHE A 563 4.661 28.464 30.354 1.00 67.76 A C
ANISOU 4486 CE1 PHE A 563 7123 6716 11907 -1006 3861 -5448 A C
ATOM 4487 CE2 PHE A 563 5.272 26.263 29.645 1.00 65.89 A C
ANISOU 4487 CE2 PHE A 563 7009 6888 11137 -480 3289 -5064 A C
ATOM 4488 CZ PHE A 563 4.647 27.098 30.548 1.00 65.16 A C
ANISOU 4488 CZ PHE A 563 6894 6667 11196 -651 3472 -5232 A C
ATOM 4489 N THR A 564 6.984 29.651 24.136 1.00 59.57 A N
ANISOU 4489 N THR A 564 6076 4828 11729 -1449 4565 -4872 A N
ATOM 4490 CA THR A 564 7.811 29.824 22.927 1.00 59.49 A C
ANISOU 4490 CA THR A 564 5996 4780 11825 -1545 4696 -4856 A C
ATOM 4491 C THR A 564 7.616 31.210 22.254 1.00 65.16 A C
ANISOU 4491 C THR A 564 6763 5004 12991 -1828 5211 -4810 A C
ATOM 4492 O THR A 564 8.610 31.898 22.018 1.00 66.90 A O
ANISOU 4492 O THR A 564 6792 5272 13357 -2091 5472 -5158 A O
ATOM 4493 CB THR A 564 7.548 28.663 21.949 1.00 62.77 A C
ANISOU 4493 CB THR A 564 6598 5208 12042 -1245 4394 -4387 A C
ATOM 4494 CG2 THR A 564 8.305 28.803 20.636 1.00 63.56 A C
ANISOU 4494 CG2 THR A 564 6648 5258 12243 -1323 4522 -4324 A C
ATOM 4495 OG1 THR A 564 7.966 27.454 22.575 1.00 60.85 A O
ANISOU 4495 OG1 THR A 564 6299 5420 11401 -1000 3990 -4492 A O
ATOM 4496 N ARG A 565 6.358 31.607 21.956 1.00 60.97 A N
ANISOU 4496 N ARG A 565 6484 4017 12665 -1764 5372 -4384 A N
ATOM 4497 CA ARG A 565 6.037 32.868 21.285 1.00 62.72 A C
ANISOU 4497 CA ARG A 565 6799 3737 13296 -1952 5878 -4243 A C
ATOM 4498 C ARG A 565 6.606 34.110 22.058 1.00 71.35 A C
ANISOU 4498 C ARG A 565 7726 4733 14650 -2327 6309 -4789 A C
ATOM 4499 O ARG A 565 7.377 34.839 21.434 1.00 75.13 A O
ANISOU 4499 O ARG A 565 8122 5079 15344 -2563 6654 -4962 A O
ATOM 4500 CB ARG A 565 4.521 32.976 21.044 1.00 62.11 A C
ANISOU 4500 CB ARG A 565 6993 3279 13327 -1758 5929 -3696 A C
ATOM 4501 CG ARG A 565 4.076 34.245 20.344 1.00 76.75 A C
ANISOU 4501 CG ARG A 565 8970 4611 15579 -1870 6460 -3467 A C
ATOM 4502 CD ARG A 565 3.057 33.921 19.284 1.00 79.21 A C
ANISOU 4502 CD ARG A 565 9492 4733 15870 -1593 6390 -2811 A C
ATOM 4503 NE ARG A 565 2.845 35.045 18.381 1.00 86.15 A N
ANISOU 4503 NE ARG A 565 10476 5168 17088 -1648 6896 -2552 A N
ATOM 4504 CZ ARG A 565 1.912 35.966 18.550 1.00 93.20 A C
ANISOU 4504 CZ ARG A 565 11506 5670 18237 -1624 7254 -2347 A C
ATOM 4505 NH1 ARG A 565 1.799 36.965 17.686 1.00 76.70 A N1+
ANISOU 4505 NH1 ARG A 565 9522 3179 16441 -1638 7739 -2090 A N1+
ATOM 4506 NH2 ARG A 565 1.098 35.909 19.597 1.00 81.32 A N
ANISOU 4506 NH2 ARG A 565 10038 4167 16694 -1571 7151 -2394 A N
ATOM 4507 N PRO A 566 6.315 34.363 23.374 1.00 66.69 A N
ANISOU 4507 N PRO A 566 7075 4222 14041 -2414 6319 -5098 A N
ATOM 4508 CA PRO A 566 6.914 35.529 24.044 1.00 70.11 A C
ANISOU 4508 CA PRO A 566 7341 4583 14716 -2810 6752 -5661 A C
ATOM 4509 C PRO A 566 8.444 35.474 24.146 1.00 76.64 A C
ANISOU 4509 C PRO A 566 7835 5869 15415 -3048 6725 -6231 A C
ATOM 4510 O PRO A 566 9.074 36.523 24.022 1.00 80.50 A O
ANISOU 4510 O PRO A 566 8217 6189 16180 -3415 7187 -6593 A O
ATOM 4511 CB PRO A 566 6.292 35.485 25.441 1.00 71.40 A C
ANISOU 4511 CB PRO A 566 7492 4861 14774 -2788 6637 -5848 A C
ATOM 4512 CG PRO A 566 5.055 34.708 25.278 1.00 71.92 A C
ANISOU 4512 CG PRO A 566 7809 4809 14707 -2411 6328 -5257 A C
ATOM 4513 CD PRO A 566 5.433 33.643 24.308 1.00 65.09 A C
ANISOU 4513 CD PRO A 566 6957 4169 13605 -2182 5973 -4970 A C
ATOM 4514 N LEU A 567 9.042 34.276 24.372 1.00 69.97 A N
ANISOU 4514 N LEU A 567 6829 5601 14156 -2841 6215 -6316 A N
ATOM 4515 CA LEU A 567 10.501 34.141 24.488 1.00 72.21 A C
ANISOU 4515 CA LEU A 567 6763 6406 14269 -3017 6150 -6843 A C
ATOM 4516 C LEU A 567 11.193 34.579 23.189 1.00 77.70 A C
ANISOU 4516 C LEU A 567 7444 6900 15179 -3179 6429 -6788 A C
ATOM 4517 O LEU A 567 12.163 35.320 23.260 1.00 81.54 A O
ANISOU 4517 O LEU A 567 7688 7503 15791 -3542 6733 -7295 A O
ATOM 4518 CB LEU A 567 10.931 32.711 24.875 1.00 70.08 A C
ANISOU 4518 CB LEU A 567 6363 6763 13502 -2678 5560 -6846 A C
ATOM 4519 CG LEU A 567 10.742 32.284 26.332 1.00 74.64 A C
ANISOU 4519 CG LEU A 567 6817 7756 13788 -2578 5296 -7117 A C
ATOM 4520 CD1 LEU A 567 10.894 30.792 26.470 1.00 72.41 A C
ANISOU 4520 CD1 LEU A 567 6535 7930 13048 -2145 4750 -6912 A C
ATOM 4521 CD2 LEU A 567 11.710 32.984 27.265 1.00 80.97 A C
ANISOU 4521 CD2 LEU A 567 7230 8976 14559 -2935 5478 -7859 A C
ATOM 4522 N TYR A 568 10.645 34.182 22.018 1.00 71.15 A N
ANISOU 4522 N TYR A 568 6873 5761 14400 -2932 6359 -6185 A N
ATOM 4523 CA TYR A 568 11.128 34.562 20.698 1.00 72.43 A C
ANISOU 4523 CA TYR A 568 7069 5689 14760 -3035 6621 -6033 A C
ATOM 4524 C TYR A 568 10.967 36.071 20.433 1.00 81.85 A C
ANISOU 4524 C TYR A 568 8357 6315 16427 -3376 7286 -6107 A C
ATOM 4525 O TYR A 568 11.902 36.686 19.911 1.00 86.18 A O
ANISOU 4525 O TYR A 568 8774 6825 17145 -3663 7617 -6379 A O
ATOM 4526 CB TYR A 568 10.402 33.758 19.608 1.00 70.24 A C
ANISOU 4526 CB TYR A 568 7055 5245 14388 -2667 6369 -5353 A C
ATOM 4527 CG TYR A 568 11.187 32.557 19.124 1.00 69.64 A C
ANISOU 4527 CG TYR A 568 6860 5638 13963 -2462 5938 -5337 A C
ATOM 4528 CD1 TYR A 568 12.351 32.715 18.374 1.00 73.09 A C
ANISOU 4528 CD1 TYR A 568 7118 6225 14428 -2621 6065 -5548 A C
ATOM 4529 CD2 TYR A 568 10.765 31.263 19.408 1.00 66.86 A C
ANISOU 4529 CD2 TYR A 568 6588 5558 13256 -2105 5433 -5106 A C
ATOM 4530 CE1 TYR A 568 13.084 31.615 17.937 1.00 72.00 A C
ANISOU 4530 CE1 TYR A 568 6871 6516 13969 -2415 5685 -5532 A C
ATOM 4531 CE2 TYR A 568 11.488 30.153 18.972 1.00 66.67 A C
ANISOU 4531 CE2 TYR A 568 6481 5932 12917 -1898 5074 -5085 A C
ATOM 4532 CZ TYR A 568 12.648 30.335 18.237 1.00 74.52 A C
ANISOU 4532 CZ TYR A 568 7287 7085 13943 -2045 5197 -5297 A C
ATOM 4533 OH TYR A 568 13.361 29.252 17.791 1.00 71.30 A O
ANISOU 4533 OH TYR A 568 6801 7061 13229 -1826 4863 -5271 A O
ATOM 4534 N ARG A 569 9.800 36.660 20.794 1.00 77.69 A N
ANISOU 4534 N ARG A 569 8062 5343 16111 -3340 7502 -5867 A N
ATOM 4535 CA ARG A 569 9.490 38.085 20.623 1.00 80.80 A C
ANISOU 4535 CA ARG A 569 8600 5138 16960 -3606 8164 -5881 A C
ATOM 4536 C ARG A 569 10.473 38.946 21.400 1.00 90.13 A C
ANISOU 4536 C ARG A 569 9526 6431 18289 -4090 8533 -6637 A C
ATOM 4537 O ARG A 569 11.103 39.836 20.820 1.00 93.74 A O
ANISOU 4537 O ARG A 569 9965 6619 19032 -4396 9032 -6816 A O
ATOM 4538 CB ARG A 569 8.060 38.392 21.089 1.00 79.41 A C
ANISOU 4538 CB ARG A 569 8681 4581 16909 -3432 8247 -5532 A C
ATOM 4539 CG ARG A 569 7.161 38.985 20.006 1.00 84.75 A C
ANISOU 4539 CG ARG A 569 9674 4667 17862 -3256 8582 -4892 A C
ATOM 4540 CD ARG A 569 5.904 39.637 20.569 1.00 87.15 A C
ANISOU 4540 CD ARG A 569 10192 4553 18368 -3173 8831 -4670 A C
ATOM 4541 NE ARG A 569 5.034 38.707 21.300 1.00 92.15 A N
ANISOU 4541 NE ARG A 569 10849 5455 18707 -2893 8315 -4498 A N
ATOM 4542 CZ ARG A 569 4.873 38.701 22.620 1.00107.02 A C
ANISOU 4542 CZ ARG A 569 12641 7508 20515 -2992 8217 -4873 A C
ATOM 4543 NH1 ARG A 569 4.057 37.824 23.191 1.00 88.09 A N1+
ANISOU 4543 NH1 ARG A 569 10289 5333 17848 -2718 7762 -4667 A N1+
ATOM 4544 NH2 ARG A 569 5.524 39.572 23.380 1.00104.18 A N
ANISOU 4544 NH2 ARG A 569 12141 7103 20339 -3380 8589 -5470 A N
ATOM 4545 N ASP A 570 10.615 38.660 22.711 1.00 86.51 A N
ANISOU 4545 N ASP A 570 8860 6393 17614 -4165 8292 -7090 A N
ATOM 4546 CA ASP A 570 11.524 39.345 23.622 1.00 90.53 A C
ANISOU 4546 CA ASP A 570 9072 7146 18179 -4624 8563 -7873 A C
ATOM 4547 C ASP A 570 12.987 39.209 23.149 1.00 97.78 A C
ANISOU 4547 C ASP A 570 9674 8488 18990 -4849 8553 -8282 A C
ATOM 4548 O ASP A 570 13.729 40.193 23.176 1.00102.13 A O
ANISOU 4548 O ASP A 570 10082 8936 19788 -5312 9055 -8780 A O
ATOM 4549 CB ASP A 570 11.348 38.796 25.047 1.00 91.50 A C
ANISOU 4549 CB ASP A 570 9022 7758 17985 -4550 8177 -8185 A C
ATOM 4550 CG ASP A 570 10.102 39.288 25.765 1.00104.54 A C
ANISOU 4550 CG ASP A 570 10919 8997 19805 -4489 8336 -8001 A C
ATOM 4551 OD1 ASP A 570 9.028 39.346 25.127 1.00103.80 A O
ANISOU 4551 OD1 ASP A 570 11165 8384 19888 -4233 8417 -7368 A O
ATOM 4552 OD2 ASP A 570 10.196 39.598 26.969 1.00114.41 A O1-
ANISOU 4552 OD2 ASP A 570 12004 10479 20987 -4685 8370 -8491 A O1-
ATOM 4553 N LEU A 571 13.379 38.010 22.677 1.00 91.33 A N
ANISOU 4553 N LEU A 571 8763 8120 17819 -4528 8018 -8067 A N
ATOM 4554 CA LEU A 571 14.728 37.743 22.180 1.00 93.08 A C
ANISOU 4554 CA LEU A 571 8683 8785 17897 -4669 7950 -8394 A C
ATOM 4555 C LEU A 571 15.036 38.563 20.909 1.00102.07 A C
ANISOU 4555 C LEU A 571 9953 9422 19405 -4887 8462 -8245 A C
ATOM 4556 O LEU A 571 16.175 39.014 20.738 1.00104.84 A O
ANISOU 4556 O LEU A 571 10042 9970 19823 -5253 8723 -8739 A O
ATOM 4557 CB LEU A 571 14.930 36.240 21.909 1.00 88.63 A C
ANISOU 4557 CB LEU A 571 8059 8730 16887 -4214 7283 -8104 A C
ATOM 4558 CG LEU A 571 15.480 35.382 23.060 1.00 92.67 A C
ANISOU 4558 CG LEU A 571 8244 10025 16942 -4091 6805 -8508 A C
ATOM 4559 CD1 LEU A 571 15.298 33.925 22.774 1.00 88.24 A C
ANISOU 4559 CD1 LEU A 571 7773 9754 16000 -3568 6213 -8057 A C
ATOM 4560 CD2 LEU A 571 16.949 35.632 23.300 1.00 99.26 A C
ANISOU 4560 CD2 LEU A 571 8619 11430 17664 -4427 6900 -9207 A C
ATOM 4561 N TYR A 572 14.014 38.780 20.045 1.00 98.84 A N
ANISOU 4561 N TYR A 572 9940 8389 19227 -4663 8624 -7574 A N
ATOM 4562 CA TYR A 572 14.135 39.559 18.807 1.00100.91 A C
ANISOU 4562 CA TYR A 572 10383 8125 19834 -4794 9127 -7321 A C
ATOM 4563 C TYR A 572 14.310 41.052 19.125 1.00109.28 A C
ANISOU 4563 C TYR A 572 11468 8727 21328 -5286 9877 -7729 A C
ATOM 4564 O TYR A 572 15.135 41.716 18.499 1.00111.37 A O
ANISOU 4564 O TYR A 572 11671 8836 21810 -5607 10320 -7952 A O
ATOM 4565 CB TYR A 572 12.914 39.337 17.885 1.00 99.31 A C
ANISOU 4565 CB TYR A 572 10573 7458 19702 -4372 9063 -6477 A C
ATOM 4566 CG TYR A 572 13.032 40.023 16.541 1.00103.51 A C
ANISOU 4566 CG TYR A 572 11292 7504 20533 -4432 9540 -6147 A C
ATOM 4567 CD1 TYR A 572 13.720 39.427 15.491 1.00104.45 A C
ANISOU 4567 CD1 TYR A 572 11336 7843 20506 -4337 9360 -5996 A C
ATOM 4568 CD2 TYR A 572 12.449 41.268 16.318 1.00107.71 A C
ANISOU 4568 CD2 TYR A 572 12087 7351 21487 -4563 10190 -5968 A C
ATOM 4569 CE1 TYR A 572 13.850 40.063 14.258 1.00108.51 A C
ANISOU 4569 CE1 TYR A 572 12020 7930 21279 -4386 9808 -5690 A C
ATOM 4570 CE2 TYR A 572 12.574 41.916 15.090 1.00111.11 A C
ANISOU 4570 CE2 TYR A 572 12700 7337 22181 -4592 10660 -5645 A C
ATOM 4571 CZ TYR A 572 13.273 41.307 14.060 1.00120.70 A C
ANISOU 4571 CZ TYR A 572 13825 8800 23233 -4506 10459 -5504 A C
ATOM 4572 OH TYR A 572 13.404 41.939 12.845 1.00127.13 A O
ANISOU 4572 OH TYR A 572 14820 9194 24289 -4524 10925 -5175 A O
ATOM 4573 N ASN A 573 13.536 41.571 20.097 1.00106.66 A N
ANISOU 4573 N ASN A 573 11238 8168 21123 -5353 10040 -7837 A N
ATOM 4574 CA ASN A 573 13.599 42.974 20.515 1.00111.54 A C
ANISOU 4574 CA ASN A 573 11910 8318 22153 -5815 10772 -8240 A C
ATOM 4575 C ASN A 573 14.897 43.265 21.297 1.00118.46 A C
ANISOU 4575 C ASN A 573 12359 9690 22961 -6340 10899 -9160 A C
ATOM 4576 O ASN A 573 15.192 44.427 21.573 1.00122.40 A O
ANISOU 4576 O ASN A 573 12856 9850 23799 -6817 11554 -9608 A O
ATOM 4577 CB ASN A 573 12.358 43.347 21.343 1.00112.39 A C
ANISOU 4577 CB ASN A 573 12245 8076 22381 -5698 10867 -8075 A C
ATOM 4578 CG ASN A 573 11.038 43.095 20.639 1.00143.67 A C
ANISOU 4578 CG ASN A 573 16593 11593 26401 -5198 10766 -7203 A C
ATOM 4579 ND2 ASN A 573 9.960 43.046 21.410 1.00137.65 A N
ANISOU 4579 ND2 ASN A 573 15969 10718 25614 -5003 10640 -7028 A N
ATOM 4580 OD1 ASN A 573 10.961 42.937 19.409 1.00137.70 A O
ANISOU 4580 OD1 ASN A 573 16000 10623 25696 -4983 10799 -6687 A O
ATOM 4581 N PHE A 574 15.672 42.209 21.624 1.00113.44 A N
ANISOU 4581 N PHE A 574 11361 9863 21879 -6244 10294 -9436 A N
ATOM 4582 CA PHE A 574 16.954 42.278 22.322 1.00117.29 A C
ANISOU 4582 CA PHE A 574 11371 10997 22195 -6664 10293 -10281 A C
ATOM 4583 C PHE A 574 18.077 42.289 21.259 1.00122.75 A C
ANISOU 4583 C PHE A 574 11902 11822 22915 -6837 10431 -10393 A C
ATOM 4584 O PHE A 574 18.464 41.241 20.725 1.00119.50 A O
ANISOU 4584 O PHE A 574 11378 11841 22187 -6511 9920 -10152 A O
ATOM 4585 CB PHE A 574 17.078 41.107 23.324 1.00116.85 A C
ANISOU 4585 CB PHE A 574 11023 11763 21611 -6387 9561 -10458 A C
ATOM 4586 CG PHE A 574 18.251 41.090 24.282 1.00122.51 A C
ANISOU 4586 CG PHE A 574 11209 13277 22061 -6742 9474 -11323 A C
ATOM 4587 CD1 PHE A 574 19.019 42.229 24.496 1.00128.08 A C
ANISOU 4587 CD1 PHE A 574 11902 14014 22749 -7080 9653 -11515 A C
ATOM 4588 CD2 PHE A 574 18.557 39.946 25.008 1.00123.15 A C
ANISOU 4588 CD2 PHE A 574 10993 14181 21616 -6433 8802 -11441 A C
ATOM 4589 CE1 PHE A 574 20.095 42.209 25.387 1.00129.62 A C
ANISOU 4589 CE1 PHE A 574 11784 15043 22423 -7109 9170 -11801 A C
ATOM 4590 CE2 PHE A 574 19.625 39.930 25.907 1.00130.02 A C
ANISOU 4590 CE2 PHE A 574 11342 15860 22199 -6724 8712 -12226 A C
ATOM 4591 CZ PHE A 574 20.396 41.057 26.080 1.00129.46 A C
ANISOU 4591 CZ PHE A 574 11325 15809 22055 -6982 8790 -12241 A C
ATOM 4592 N GLU A 575 18.550 43.509 20.934 1.00122.19 A N
ANISOU 4592 N GLU A 575 11912 11397 23116 -7235 10970 -10552 A N
ATOM 4593 CA GLU A 575 19.555 43.865 19.925 1.00122.25 A C
ANISOU 4593 CA GLU A 575 11904 11457 23089 -7345 11029 -10433 A C
ATOM 4594 C GLU A 575 20.738 42.880 19.839 1.00124.44 A C
ANISOU 4594 C GLU A 575 11746 12596 22938 -7283 10513 -10712 A C
ATOM 4595 O GLU A 575 21.061 42.419 18.742 1.00123.97 A O
ANISOU 4595 O GLU A 575 11655 12466 22983 -7240 10627 -10595 A O
ATOM 4596 CB GLU A 575 20.103 45.284 20.179 1.00123.86 A C
ANISOU 4596 CB GLU A 575 12294 11642 23127 -7486 10946 -10235 A C
ATOM 4597 CG GLU A 575 19.047 46.369 20.338 1.00131.31 A C
ANISOU 4597 CG GLU A 575 13819 12064 24009 -7147 10740 -9376 A C
ATOM 4598 CD GLU A 575 18.595 46.627 21.764 1.00138.24 A C
ANISOU 4598 CD GLU A 575 14843 13315 24367 -6804 9947 -9031 A C
ATOM 4599 OE1 GLU A 575 19.415 47.119 22.573 1.00136.61 A O
ANISOU 4599 OE1 GLU A 575 14471 13531 23905 -6978 9719 -9310 A O
ATOM 4600 OE2 GLU A 575 17.410 46.365 22.064 1.00128.64 A O1-
ANISOU 4600 OE2 GLU A 575 13644 11504 23729 -7011 10709 -9458 A O1-
ATOM 4601 N LYS A 576 21.373 42.569 20.987 1.00121.48 A N
ANISOU 4601 N LYS A 576 10942 12962 22255 -7436 10236 -11353 A N
ATOM 4602 CA LYS A 576 22.533 41.674 21.084 1.00121.34 A C
ANISOU 4602 CA LYS A 576 10434 13829 21841 -7417 9828 -11760 A C
ATOM 4603 C LYS A 576 22.194 40.234 20.666 1.00121.20 A C
ANISOU 4603 C LYS A 576 10335 14035 21681 -6995 9460 -11567 A C
ATOM 4604 O LYS A 576 23.044 39.546 20.094 1.00118.88 A O
ANISOU 4604 O LYS A 576 9806 14227 21136 -6867 9174 -11594 A O
ATOM 4605 CB LYS A 576 23.097 41.681 22.516 1.00123.53 A C
ANISOU 4605 CB LYS A 576 10458 14888 21592 -7372 9285 -12009 A C
ATOM 4606 CG LYS A 576 23.646 43.035 22.971 1.00134.96 A C
ANISOU 4606 CG LYS A 576 12399 16330 22548 -7061 8620 -11012 A C
ATOM 4607 CD LYS A 576 23.440 43.226 24.467 1.00141.00 A C
ANISOU 4607 CD LYS A 576 13311 17439 22824 -6728 7958 -10664 A C
ATOM 4608 CE LYS A 576 23.599 44.648 24.935 1.00143.22 A C
ANISOU 4608 CE LYS A 576 14011 17505 22901 -6597 7618 -9990 A C
ATOM 4609 NZ LYS A 576 23.119 44.811 26.335 1.00145.80 A N1+
ANISOU 4609 NZ LYS A 576 14496 18014 22886 -6324 7136 -9732 A N1+
ATOM 4610 N ALA A 577 20.949 39.793 20.935 1.00113.88 A N
ANISOU 4610 N ALA A 577 9755 12798 20716 -6563 9177 -10996 A N
ATOM 4611 CA ALA A 577 20.482 38.441 20.635 1.00108.59 A C
ANISOU 4611 CA ALA A 577 9218 12340 19700 -5928 8511 -10387 A C
ATOM 4612 C ALA A 577 19.857 38.290 19.235 1.00109.01 A C
ANISOU 4612 C ALA A 577 9694 11772 19952 -5643 8571 -9611 A C
ATOM 4613 O ALA A 577 19.926 37.199 18.683 1.00105.15 A O
ANISOU 4613 O ALA A 577 9225 11545 19183 -5236 8102 -9239 A O
ATOM 4614 CB ALA A 577 19.469 38.013 21.684 1.00106.85 A C
ANISOU 4614 CB ALA A 577 9120 12174 19304 -5636 8169 -10222 A C
ATOM 4615 N ARG A 578 19.238 39.362 18.683 1.00107.61 A N
ANISOU 4615 N ARG A 578 9850 10797 20238 -5839 9152 -9369 A N
ATOM 4616 CA ARG A 578 18.492 39.427 17.411 1.00105.21 A C
ANISOU 4616 CA ARG A 578 9965 9852 20156 -5586 9302 -8622 A C
ATOM 4617 C ARG A 578 19.026 38.529 16.289 1.00107.54 A C
ANISOU 4617 C ARG A 578 10223 10397 20238 -5319 8980 -8307 A C
ATOM 4618 O ARG A 578 18.230 37.819 15.677 1.00102.29 A O
ANISOU 4618 O ARG A 578 9828 9568 19469 -4880 8671 -7657 A O
ATOM 4619 CB ARG A 578 18.403 40.871 16.890 1.00110.13 A C
ANISOU 4619 CB ARG A 578 10796 9752 21298 -5979 10114 -8653 A C
ATOM 4620 CG ARG A 578 17.331 41.069 15.807 1.00120.13 A C
ANISOU 4620 CG ARG A 578 12529 10319 22797 -5669 10307 -7833 A C
ATOM 4621 CD ARG A 578 17.105 42.530 15.451 1.00136.79 A C
ANISOU 4621 CD ARG A 578 14883 11678 25412 -6000 11140 -7825 A C
ATOM 4622 NE ARG A 578 16.339 43.229 16.484 1.00140.90 A N
ANISOU 4622 NE ARG A 578 15641 12183 25712 -5843 10802 -7542 A N
ATOM 4623 CZ ARG A 578 15.341 44.077 16.250 1.00151.69 A C
ANISOU 4623 CZ ARG A 578 17516 13345 26776 -5376 10326 -6537 A C
ATOM 4624 NH1 ARG A 578 14.712 44.661 17.257 1.00146.50 A N1+
ANISOU 4624 NH1 ARG A 578 16909 12340 26415 -5585 10748 -6860 A N1+
ATOM 4625 NH2 ARG A 578 14.971 44.352 15.004 1.00141.99 A N
ANISOU 4625 NH2 ARG A 578 16459 11318 26174 -5483 11249 -6404 A N
ATOM 4626 N GLU A 579 20.343 38.575 16.000 1.00108.57 A N
ANISOU 4626 N GLU A 579 10021 10925 20306 -5593 9070 -8772 A N
ATOM 4627 CA GLU A 579 20.955 37.793 14.926 1.00107.00 A C
ANISOU 4627 CA GLU A 579 9762 10975 19918 -5378 8813 -8534 A C
ATOM 4628 C GLU A 579 20.834 36.281 15.159 1.00106.32 A C
ANISOU 4628 C GLU A 579 9608 11436 19352 -4869 8057 -8304 A C
ATOM 4629 O GLU A 579 20.308 35.579 14.294 1.00102.38 A O
ANISOU 4629 O GLU A 579 9358 10782 18762 -4489 7805 -7708 A O
ATOM 4630 CB GLU A 579 22.426 38.177 14.733 1.00113.04 A C
ANISOU 4630 CB GLU A 579 10137 12112 20702 -5807 9074 -9160 A C
ATOM 4631 CG GLU A 579 22.628 39.246 13.676 1.00126.85 A C
ANISOU 4631 CG GLU A 579 12061 13267 22869 -6124 9737 -9062 A C
ATOM 4632 CD GLU A 579 24.035 39.332 13.120 1.00139.81 A C
ANISOU 4632 CD GLU A 579 13379 15308 24433 -6399 9839 -9451 A C
ATOM 4633 OE1 GLU A 579 24.738 40.320 13.434 1.00139.66 A O
ANISOU 4633 OE1 GLU A 579 13371 15410 24283 -6593 9812 -9459 A O
ATOM 4634 OE2 GLU A 579 24.429 38.420 12.359 1.00118.34 A O1-
ANISOU 4634 OE2 GLU A 579 10562 12906 21498 -6146 9522 -9286 A O1-
ATOM 4635 N GLN A 580 21.293 35.797 16.330 1.00102.97 A N
ANISOU 4635 N GLN A 580 8860 11644 18619 -4860 7723 -8773 A N
ATOM 4636 CA GLN A 580 21.290 34.387 16.730 1.00 99.07 A C
ANISOU 4636 CA GLN A 580 8278 11709 17653 -4386 7050 -8630 A C
ATOM 4637 C GLN A 580 19.871 33.803 16.823 1.00 96.33 A C
ANISOU 4637 C GLN A 580 8336 11008 17258 -3965 6764 -7996 A C
ATOM 4638 O GLN A 580 19.681 32.645 16.468 1.00 91.71 A O
ANISOU 4638 O GLN A 580 7860 10589 16396 -3541 6324 -7607 A O
ATOM 4639 CB GLN A 580 22.005 34.225 18.081 1.00103.03 A C
ANISOU 4639 CB GLN A 580 8349 12933 17864 -4495 6851 -9286 A C
ATOM 4640 CG GLN A 580 22.545 32.817 18.346 1.00108.88 A C
ANISOU 4640 CG GLN A 580 8875 14407 18087 -4055 6240 -9278 A C
ATOM 4641 CD GLN A 580 23.046 32.616 19.766 1.00121.66 A C
ANISOU 4641 CD GLN A 580 10098 16751 19377 -4074 6013 -9838 A C
ATOM 4642 NE2 GLN A 580 23.179 31.353 20.157 1.00111.79 A N
ANISOU 4642 NE2 GLN A 580 8770 16032 17674 -3587 5474 -9699 A N
ATOM 4643 OE1 GLN A 580 23.332 33.568 20.518 1.00112.35 A O
ANISOU 4643 OE1 GLN A 580 8678 15681 18329 -4515 6327 -10402 A O
ATOM 4644 N THR A 581 18.892 34.596 17.283 1.00 92.44 A N
ANISOU 4644 N THR A 581 8061 10028 17033 -4091 7034 -7906 A N
ATOM 4645 CA THR A 581 17.504 34.150 17.461 1.00 87.95 A C
ANISOU 4645 CA THR A 581 7848 9133 16436 -3738 6805 -7354 A C
ATOM 4646 C THR A 581 16.812 33.900 16.122 1.00 88.55 A C
ANISOU 4646 C THR A 581 8274 8755 16616 -3488 6809 -6660 A C
ATOM 4647 O THR A 581 16.084 32.917 16.002 1.00 84.11 A O
ANISOU 4647 O THR A 581 7900 8229 15829 -3092 6399 -6220 A O
ATOM 4648 CB THR A 581 16.715 35.144 18.318 1.00 96.76 A C
ANISOU 4648 CB THR A 581 9077 9862 17827 -3964 7145 -7478 A C
ATOM 4649 CG2 THR A 581 17.370 35.397 19.658 1.00 95.45 A C
ANISOU 4649 CG2 THR A 581 8552 10177 17539 -4233 7148 -8190 A C
ATOM 4650 OG1 THR A 581 16.559 36.372 17.609 1.00101.66 A O
ANISOU 4650 OG1 THR A 581 9867 9862 18895 -4262 7757 -7391 A O
ATOM 4651 N VAL A 582 17.035 34.781 15.128 1.00 88.32 A N
ANISOU 4651 N VAL A 582 8327 8319 16913 -3723 7285 -6573 A N
ATOM 4652 CA VAL A 582 16.491 34.667 13.766 1.00 86.35 A C
ANISOU 4652 CA VAL A 582 8372 7676 16762 -3516 7348 -5944 A C
ATOM 4653 C VAL A 582 17.058 33.400 13.135 1.00 86.84 A C
ANISOU 4653 C VAL A 582 8349 8179 16469 -3230 6879 -5807 A C
ATOM 4654 O VAL A 582 16.303 32.598 12.595 1.00 83.15 A O
ANISOU 4654 O VAL A 582 8112 7632 15850 -2879 6581 -5288 A O
ATOM 4655 CB VAL A 582 16.790 35.943 12.920 1.00 94.51 A C
ANISOU 4655 CB VAL A 582 9473 8231 18204 -3850 8005 -5953 A C
ATOM 4656 CG1 VAL A 582 16.574 35.703 11.428 1.00 92.83 A C
ANISOU 4656 CG1 VAL A 582 9471 7789 18010 -3637 8029 -5383 A C
ATOM 4657 CG2 VAL A 582 15.948 37.124 13.391 1.00 96.30 A C
ANISOU 4657 CG2 VAL A 582 9901 7894 18795 -4028 8484 -5909 A C
ATOM 4658 N ASN A 583 18.381 33.200 13.269 1.00 85.23 A N
ANISOU 4658 N ASN A 583 7800 8468 16116 -3383 6816 -6300 A N
ATOM 4659 CA ASN A 583 19.104 32.043 12.751 1.00 83.70 A C
ANISOU 4659 CA ASN A 583 7483 8736 15583 -3129 6412 -6254 A C
ATOM 4660 C ASN A 583 18.729 30.761 13.503 1.00 83.69 A C
ANISOU 4660 C ASN A 583 7503 9103 15190 -2729 5837 -6146 A C
ATOM 4661 O ASN A 583 18.753 29.695 12.896 1.00 80.95 A O
ANISOU 4661 O ASN A 583 7250 8908 14600 -2407 5505 -5843 A O
ATOM 4662 CB ASN A 583 20.626 32.271 12.787 1.00 89.89 A C
ANISOU 4662 CB ASN A 583 7858 9980 16317 -3410 6532 -6848 A C
ATOM 4663 CG ASN A 583 21.140 33.317 11.816 1.00109.29 A C
ANISOU 4663 CG ASN A 583 10307 12105 19112 -3765 7071 -6908 A C
ATOM 4664 ND2 ASN A 583 20.845 33.177 10.531 1.00100.64 A N
ANISOU 4664 ND2 ASN A 583 9452 10707 18081 -3608 7121 -6404 A N
ATOM 4665 OD1 ASN A 583 21.818 34.264 12.209 1.00101.62 A O
ANISOU 4665 OD1 ASN A 583 9114 11157 18341 -4194 7465 -7418 A O
ATOM 4666 N THR A 584 18.366 30.855 14.794 1.00 80.71 A N
ANISOU 4666 N THR A 584 7062 8849 14755 -2747 5746 -6382 A N
ATOM 4667 CA THR A 584 17.933 29.690 15.583 1.00 77.95 A C
ANISOU 4667 CA THR A 584 6762 8808 14048 -2367 5247 -6266 A C
ATOM 4668 C THR A 584 16.544 29.242 15.101 1.00 76.75 A C
ANISOU 4668 C THR A 584 7028 8209 13923 -2090 5115 -5618 A C
ATOM 4669 O THR A 584 16.303 28.046 14.972 1.00 73.27 A O
ANISOU 4669 O THR A 584 6710 7939 13191 -1735 4724 -5348 A O
ATOM 4670 CB THR A 584 17.955 30.001 17.098 1.00 86.22 A C
ANISOU 4670 CB THR A 584 7610 10117 15031 -2489 5227 -6714 A C
ATOM 4671 CG2 THR A 584 17.517 28.816 17.957 1.00 77.77 A C
ANISOU 4671 CG2 THR A 584 6599 9368 13583 -2084 4740 -6589 A C
ATOM 4672 OG1 THR A 584 19.286 30.371 17.468 1.00 92.37 A O
ANISOU 4672 OG1 THR A 584 7963 11381 15753 -2760 5345 -7338 A O
ATOM 4673 N PHE A 585 15.652 30.215 14.817 1.00 73.46 A N
ANISOU 4673 N PHE A 585 6824 7234 13854 -2256 5469 -5379 A N
ATOM 4674 CA PHE A 585 14.290 29.967 14.338 1.00 69.74 A C
ANISOU 4674 CA PHE A 585 6712 6353 13432 -2032 5401 -4780 A C
ATOM 4675 C PHE A 585 14.276 29.336 12.952 1.00 71.98 A C
ANISOU 4675 C PHE A 585 7142 6579 13628 -1844 5291 -4363 A C
ATOM 4676 O PHE A 585 13.457 28.449 12.719 1.00 68.55 A O
ANISOU 4676 O PHE A 585 6919 6122 13006 -1555 4991 -3973 A O
ATOM 4677 CB PHE A 585 13.458 31.258 14.310 1.00 72.18 A C
ANISOU 4677 CB PHE A 585 7177 6113 14134 -2243 5857 -4639 A C
ATOM 4678 CG PHE A 585 12.128 31.137 13.593 1.00 70.74 A C
ANISOU 4678 CG PHE A 585 7326 5535 14015 -2022 5847 -4000 A C
ATOM 4679 CD1 PHE A 585 11.108 30.345 14.109 1.00 70.28 A C
ANISOU 4679 CD1 PHE A 585 7431 5511 13763 -1757 5505 -3737 A C
ATOM 4680 CD2 PHE A 585 11.899 31.814 12.400 1.00 73.57 A C
ANISOU 4680 CD2 PHE A 585 7822 5520 14612 -2076 6191 -3664 A C
ATOM 4681 CE1 PHE A 585 9.878 30.241 13.450 1.00 68.85 A C
ANISOU 4681 CE1 PHE A 585 7516 5026 13619 -1572 5497 -3178 A C
ATOM 4682 CE2 PHE A 585 10.667 31.707 11.742 1.00 74.10 A C
ANISOU 4682 CE2 PHE A 585 8154 5300 14699 -1856 6175 -3079 A C
ATOM 4683 CZ PHE A 585 9.667 30.918 12.272 1.00 69.03 A C
ANISOU 4683 CZ PHE A 585 7642 4729 13857 -1616 5822 -2854 A C
ATOM 4684 N LEU A 586 15.131 29.823 12.020 1.00 70.87 A N
ANISOU 4684 N LEU A 586 6895 6404 13627 -2024 5555 -4446 A N
ATOM 4685 CA LEU A 586 15.164 29.298 10.654 1.00 69.21 A C
ANISOU 4685 CA LEU A 586 6809 6151 13338 -1867 5483 -4070 A C
ATOM 4686 C LEU A 586 15.619 27.841 10.668 1.00 72.06 A C
ANISOU 4686 C LEU A 586 7122 6958 13299 -1579 5001 -4089 A C
ATOM 4687 O LEU A 586 14.973 27.018 10.020 1.00 70.17 A O
ANISOU 4687 O LEU A 586 7102 6654 12905 -1332 4779 -3675 A O
ATOM 4688 CB LEU A 586 16.025 30.162 9.718 1.00 72.18 A C
ANISOU 4688 CB LEU A 586 7068 6417 13940 -2131 5885 -4192 A C
ATOM 4689 CG LEU A 586 15.586 31.639 9.553 1.00 79.28 A C
ANISOU 4689 CG LEU A 586 8064 6802 15258 -2400 6445 -4121 A C
ATOM 4690 CD1 LEU A 586 16.659 32.457 8.882 1.00 82.97 A C
ANISOU 4690 CD1 LEU A 586 8376 7221 15927 -2698 6854 -4364 A C
ATOM 4691 CD2 LEU A 586 14.269 31.774 8.798 1.00 79.84 A C
ANISOU 4691 CD2 LEU A 586 8459 6455 15420 -2204 6521 -3483 A C
ATOM 4692 N LYS A 587 16.618 27.496 11.516 1.00 70.67 A N
ANISOU 4692 N LYS A 587 6671 7241 12941 -1593 4841 -4564 A N
ATOM 4693 CA LYS A 587 17.149 26.136 11.663 1.00 69.78 A C
ANISOU 4693 CA LYS A 587 6499 7575 12439 -1287 4419 -4614 A C
ATOM 4694 C LYS A 587 16.140 25.186 12.316 1.00 71.83 A C
ANISOU 4694 C LYS A 587 6990 7819 12482 -981 4081 -4353 A C
ATOM 4695 O LYS A 587 16.345 23.982 12.246 1.00 70.77 A O
ANISOU 4695 O LYS A 587 6916 7928 12043 -688 3766 -4259 A O
ATOM 4696 CB LYS A 587 18.461 26.137 12.478 1.00 75.24 A C
ANISOU 4696 CB LYS A 587 6801 8800 12985 -1367 4368 -5194 A C
ATOM 4697 CG LYS A 587 19.681 26.637 11.721 1.00 94.79 A C
ANISOU 4697 CG LYS A 587 9023 11438 15556 -1595 4600 -5465 A C
ATOM 4698 CD LYS A 587 20.900 26.718 12.642 1.00111.36 A C
ANISOU 4698 CD LYS A 587 10694 14117 17500 -1702 4561 -6076 A C
ATOM 4699 CE LYS A 587 22.122 27.313 11.979 1.00123.16 A C
ANISOU 4699 CE LYS A 587 11899 15798 19100 -1979 4822 -6404 A C
ATOM 4700 NZ LYS A 587 22.879 26.304 11.192 1.00131.56 A N1+
ANISOU 4700 NZ LYS A 587 12917 17170 19900 -1706 4585 -6296 A N1+
ATOM 4701 N ASN A 588 15.063 25.708 12.954 1.00 68.46 A N
ANISOU 4701 N ASN A 588 6703 7099 12211 -1048 4168 -4238 A N
ATOM 4702 CA ASN A 588 14.044 24.895 13.636 1.00 65.37 A C
ANISOU 4702 CA ASN A 588 6530 6671 11637 -795 3884 -4005 A C
ATOM 4703 C ASN A 588 12.621 25.059 13.039 1.00 66.37 A C
ANISOU 4703 C ASN A 588 6967 6334 11915 -772 3963 -3501 A C
ATOM 4704 O ASN A 588 11.702 24.360 13.469 1.00 62.64 A O
ANISOU 4704 O ASN A 588 6691 5812 11298 -583 3745 -3280 A O
ATOM 4705 CB ASN A 588 14.021 25.237 15.126 1.00 66.20 A C
ANISOU 4705 CB ASN A 588 6492 6936 11725 -856 3865 -4347 A C
ATOM 4706 CG ASN A 588 15.202 24.701 15.888 1.00 94.76 A C
ANISOU 4706 CG ASN A 588 9823 11120 15063 -756 3669 -4777 A C
ATOM 4707 ND2 ASN A 588 16.260 25.488 15.985 1.00 90.28 A N
ANISOU 4707 ND2 ASN A 588 8932 10770 14600 -1017 3878 -5213 A N
ATOM 4708 OD1 ASN A 588 15.186 23.572 16.382 1.00 92.39 A O
ANISOU 4708 OD1 ASN A 588 9585 11081 14440 -437 3345 -4722 A O
ATOM 4709 N ARG A 589 12.460 25.952 12.042 1.00 65.02 A N
ANISOU 4709 N ARG A 589 6835 5856 12014 -950 4278 -3316 A N
ATOM 4710 CA ARG A 589 11.223 26.321 11.332 1.00 64.11 A C
ANISOU 4710 CA ARG A 589 6960 5345 12055 -935 4415 -2840 A C
ATOM 4711 C ARG A 589 10.433 25.118 10.773 1.00 67.02 A C
ANISOU 4711 C ARG A 589 7556 5742 12166 -674 4104 -2447 A C
ATOM 4712 O ARG A 589 9.192 25.115 10.840 1.00 65.59 A O
ANISOU 4712 O ARG A 589 7555 5361 12003 -605 4075 -2140 A O
ATOM 4713 CB ARG A 589 11.578 27.265 10.171 1.00 65.28 A C
ANISOU 4713 CB ARG A 589 7075 5275 12452 -1110 4783 -2729 A C
ATOM 4714 CG ARG A 589 10.466 28.210 9.780 1.00 69.13 A C
ANISOU 4714 CG ARG A 589 7729 5339 13197 -1157 5082 -2355 A C
ATOM 4715 CD ARG A 589 10.797 28.919 8.491 1.00 74.15 A C
ANISOU 4715 CD ARG A 589 8362 5785 14024 -1265 5428 -2183 A C
ATOM 4716 NE ARG A 589 9.744 29.858 8.116 1.00 85.27 A N
ANISOU 4716 NE ARG A 589 9932 6802 15664 -1259 5741 -1789 A N
ATOM 4717 CZ ARG A 589 9.956 31.000 7.473 1.00112.94 A C
ANISOU 4717 CZ ARG A 589 13445 10022 19443 -1392 6196 -1682 A C
ATOM 4718 NH1 ARG A 589 11.187 31.353 7.119 1.00102.16 A N1+
ANISOU 4718 NH1 ARG A 589 11934 8715 18168 -1581 6394 -1962 A N1+
ATOM 4719 NH2 ARG A 589 8.941 31.802 7.179 1.00108.24 A N
ANISOU 4719 NH2 ARG A 589 13008 9089 19031 -1326 6477 -1288 A N
ATOM 4720 N SER A 590 11.144 24.114 10.218 1.00 62.78 A N
ANISOU 4720 N SER A 590 7007 5458 11389 -541 3891 -2472 A N
ATOM 4721 CA SER A 590 10.552 22.914 9.616 1.00 60.26 A C
ANISOU 4721 CA SER A 590 6901 5177 10817 -329 3630 -2158 A C
ATOM 4722 C SER A 590 10.122 21.873 10.649 1.00 64.59 A C
ANISOU 4722 C SER A 590 7565 5854 11122 -135 3328 -2203 A C
ATOM 4723 O SER A 590 9.264 21.039 10.349 1.00 63.92 A O
ANISOU 4723 O SER A 590 7697 5712 10876 -6 3165 -1924 A O
ATOM 4724 CB SER A 590 11.546 22.266 8.649 1.00 63.04 A C
ANISOU 4724 CB SER A 590 7204 5730 11016 -266 3558 -2197 A C
ATOM 4725 OG SER A 590 11.974 23.172 7.648 1.00 67.80 A O
ANISOU 4725 OG SER A 590 7717 6217 11827 -435 3842 -2133 A O
ATOM 4726 N PHE A 591 10.726 21.901 11.849 1.00 63.06 A N
ANISOU 4726 N PHE A 591 7222 5852 10885 -120 3267 -2558 A N
ATOM 4727 CA PHE A 591 10.478 20.928 12.923 1.00 62.83 A C
ANISOU 4727 CA PHE A 591 7287 5978 10606 92 3001 -2623 A C
ATOM 4728 C PHE A 591 9.423 21.399 13.956 1.00 66.67 A C
ANISOU 4728 C PHE A 591 7843 6292 11199 43 3032 -2583 A C
ATOM 4729 O PHE A 591 9.159 20.683 14.929 1.00 66.34 A O
ANISOU 4729 O PHE A 591 7878 6370 10961 209 2837 -2640 A O
ATOM 4730 CB PHE A 591 11.804 20.597 13.635 1.00 66.94 A C
ANISOU 4730 CB PHE A 591 7583 6898 10952 195 2892 -3027 A C
ATOM 4731 CG PHE A 591 12.960 20.319 12.694 1.00 70.17 A C
ANISOU 4731 CG PHE A 591 7871 7507 11283 226 2895 -3121 A C
ATOM 4732 CD1 PHE A 591 13.882 21.313 12.390 1.00 75.79 A C
ANISOU 4732 CD1 PHE A 591 8309 8305 12182 2 3114 -3381 A C
ATOM 4733 CD2 PHE A 591 13.113 19.070 12.102 1.00 72.20 A C
ANISOU 4733 CD2 PHE A 591 8296 7852 11285 466 2706 -2959 A C
ATOM 4734 CE1 PHE A 591 14.935 21.066 11.507 1.00 78.03 A C
ANISOU 4734 CE1 PHE A 591 8474 8781 12394 26 3123 -3467 A C
ATOM 4735 CE2 PHE A 591 14.174 18.818 11.224 1.00 76.47 A C
ANISOU 4735 CE2 PHE A 591 8725 8578 11754 502 2718 -3045 A C
ATOM 4736 CZ PHE A 591 15.082 19.817 10.937 1.00 76.71 A C
ANISOU 4736 CZ PHE A 591 8467 8715 11965 287 2916 -3296 A C
ATOM 4737 N MET A 592 8.799 22.572 13.730 1.00 62.61 A N
ANISOU 4737 N MET A 592 7324 5486 10979 -158 3285 -2455 A N
ATOM 4738 CA MET A 592 7.783 23.085 14.646 1.00 62.08 A C
ANISOU 4738 CA MET A 592 7322 5243 11025 -202 3338 -2409 A C
ATOM 4739 C MET A 592 6.366 23.043 14.037 1.00 62.98 A C
ANISOU 4739 C MET A 592 7661 5082 11186 -174 3356 -1957 A C
ATOM 4740 O MET A 592 6.191 22.915 12.825 1.00 62.36 A O
ANISOU 4740 O MET A 592 7657 4938 11101 -165 3384 -1691 A O
ATOM 4741 CB MET A 592 8.125 24.503 15.145 1.00 66.89 A C
ANISOU 4741 CB MET A 592 7733 5748 11934 -446 3647 -2676 A C
ATOM 4742 CG MET A 592 8.520 25.475 14.052 1.00 72.61 A C
ANISOU 4742 CG MET A 592 8379 6295 12915 -631 3961 -2621 A C
ATOM 4743 SD MET A 592 9.055 27.096 14.647 1.00 80.66 A S
ANISOU 4743 SD MET A 592 9182 7174 14291 -953 4385 -3000 A S
ATOM 4744 CE MET A 592 10.473 26.652 15.648 1.00 79.36 A C
ANISOU 4744 CE MET A 592 8732 7511 13910 -972 4202 -3586 A C
ATOM 4745 N HIS A 593 5.363 23.167 14.908 1.00 58.26 A N
ANISOU 4745 N HIS A 593 7151 4364 10621 -159 3339 -1884 A N
ATOM 4746 CA HIS A 593 3.939 23.164 14.589 1.00 55.32 A C
ANISOU 4746 CA HIS A 593 6953 3781 10286 -134 3358 -1491 A C
ATOM 4747 C HIS A 593 3.593 24.332 13.641 1.00 61.29 A C
ANISOU 4747 C HIS A 593 7667 4305 11314 -254 3668 -1261 A C
ATOM 4748 O HIS A 593 4.149 25.414 13.829 1.00 64.42 A O
ANISOU 4748 O HIS A 593 7927 4595 11956 -397 3933 -1451 A O
ATOM 4749 CB HIS A 593 3.140 23.260 15.885 1.00 54.24 A C
ANISOU 4749 CB HIS A 593 6871 3571 10165 -116 3326 -1523 A C
ATOM 4750 CG HIS A 593 1.669 23.045 15.698 1.00 54.78 A C
ANISOU 4750 CG HIS A 593 7118 3518 10178 -54 3265 -1149 A C
ATOM 4751 CD2 HIS A 593 0.968 21.895 15.768 1.00 52.82 A C
ANISOU 4751 CD2 HIS A 593 7041 3355 9671 62 3026 -1003 A C
ATOM 4752 ND1 HIS A 593 0.833 24.041 15.275 1.00 56.18 A N
ANISOU 4752 ND1 HIS A 593 7295 3480 10571 -117 3490 -882 A N
ATOM 4753 CE1 HIS A 593 -0.357 23.465 15.137 1.00 53.05 A C
ANISOU 4753 CE1 HIS A 593 7037 3094 10025 -40 3354 -598 A C
ATOM 4754 NE2 HIS A 593 -0.311 22.189 15.417 1.00 51.76 A N
ANISOU 4754 NE2 HIS A 593 6986 3095 9586 45 3085 -673 A N
ATOM 4755 N PRO A 594 2.711 24.151 12.618 1.00 56.00 A N
ANISOU 4755 N PRO A 594 7109 3571 10597 -198 3664 -862 A N
ATOM 4756 CA PRO A 594 2.431 25.258 11.675 1.00 57.06 A C
ANISOU 4756 CA PRO A 594 7204 3515 10961 -260 3972 -605 A C
ATOM 4757 C PRO A 594 1.854 26.541 12.299 1.00 63.37 A C
ANISOU 4757 C PRO A 594 7978 4047 12054 -326 4274 -562 A C
ATOM 4758 O PRO A 594 2.117 27.623 11.762 1.00 65.37 A O
ANISOU 4758 O PRO A 594 8176 4109 12552 -400 4611 -487 A O
ATOM 4759 CB PRO A 594 1.408 24.656 10.701 1.00 57.19 A C
ANISOU 4759 CB PRO A 594 7333 3603 10793 -155 3847 -197 A C
ATOM 4760 CG PRO A 594 1.530 23.226 10.833 1.00 59.14 A C
ANISOU 4760 CG PRO A 594 7673 4061 10735 -85 3510 -297 A C
ATOM 4761 CD PRO A 594 1.990 22.923 12.224 1.00 54.44 A C
ANISOU 4761 CD PRO A 594 7070 3498 10116 -80 3396 -644 A C
ATOM 4762 N VAL A 595 1.056 26.432 13.384 1.00 59.85 A N
ANISOU 4762 N VAL A 595 7588 3567 11586 -294 4183 -598 A N
ATOM 4763 CA VAL A 595 0.451 27.605 14.037 1.00 61.23 A C
ANISOU 4763 CA VAL A 595 7752 3482 12029 -345 4468 -568 A C
ATOM 4764 C VAL A 595 1.537 28.385 14.791 1.00 65.64 A C
ANISOU 4764 C VAL A 595 8183 3961 12798 -523 4680 -1013 A C
ATOM 4765 O VAL A 595 1.611 29.619 14.667 1.00 67.31 A O
ANISOU 4765 O VAL A 595 8357 3909 13308 -629 5071 -1008 A O
ATOM 4766 CB VAL A 595 -0.747 27.280 14.965 1.00 63.90 A C
ANISOU 4766 CB VAL A 595 8183 3820 12275 -262 4314 -469 A C
ATOM 4767 CG1 VAL A 595 -1.446 28.568 15.409 1.00 65.43 A C
ANISOU 4767 CG1 VAL A 595 8371 3728 12762 -298 4650 -402 A C
ATOM 4768 CG2 VAL A 595 -1.744 26.369 14.271 1.00 62.05 A C
ANISOU 4768 CG2 VAL A 595 8050 3716 11809 -128 4105 -87 A C
ATOM 4769 N THR A 596 2.349 27.662 15.595 1.00 58.87 A N
ANISOU 4769 N THR A 596 7252 3347 11769 -550 4439 -1398 A N
ATOM 4770 CA THR A 596 3.454 28.226 16.358 1.00 59.18 A C
ANISOU 4770 CA THR A 596 7122 3435 11929 -725 4578 -1880 A C
ATOM 4771 C THR A 596 4.416 28.910 15.375 1.00 64.18 A C
ANISOU 4771 C THR A 596 7652 3993 12739 -865 4851 -1948 A C
ATOM 4772 O THR A 596 4.731 30.078 15.584 1.00 65.46 A O
ANISOU 4772 O THR A 596 7734 3951 13186 -1059 5220 -2142 A O
ATOM 4773 CB THR A 596 4.105 27.139 17.214 1.00 58.25 A C
ANISOU 4773 CB THR A 596 6940 3679 11515 -653 4221 -2201 A C
ATOM 4774 CG2 THR A 596 5.140 27.685 18.175 1.00 54.61 A C
ANISOU 4774 CG2 THR A 596 6264 3357 11127 -826 4334 -2727 A C
ATOM 4775 OG1 THR A 596 3.078 26.468 17.941 1.00 55.46 A O
ANISOU 4775 OG1 THR A 596 6724 3354 10993 -506 3993 -2059 A O
ATOM 4776 N GLU A 597 4.773 28.225 14.260 1.00 60.87 A N
ANISOU 4776 N GLU A 597 7254 3710 12163 -776 4704 -1771 A N
ATOM 4777 CA GLU A 597 5.669 28.717 13.209 1.00 63.03 A C
ANISOU 4777 CA GLU A 597 7442 3946 12560 -884 4926 -1798 A C
ATOM 4778 C GLU A 597 5.158 30.025 12.581 1.00 71.48 A C
ANISOU 4778 C GLU A 597 8568 4631 13960 -964 5385 -1539 A C
ATOM 4779 O GLU A 597 5.917 31.000 12.535 1.00 72.69 A O
ANISOU 4779 O GLU A 597 8623 4637 14360 -1169 5738 -1777 A O
ATOM 4780 CB GLU A 597 5.872 27.634 12.109 1.00 62.71 A C
ANISOU 4780 CB GLU A 597 7454 4114 12260 -734 4661 -1577 A C
ATOM 4781 CG GLU A 597 6.973 27.927 11.089 1.00 68.15 A C
ANISOU 4781 CG GLU A 597 8037 4837 13019 -834 4830 -1654 A C
ATOM 4782 CD GLU A 597 6.682 28.998 10.049 1.00 86.72 A C
ANISOU 4782 CD GLU A 597 10434 6887 15628 -894 5230 -1348 A C
ATOM 4783 OE1 GLU A 597 5.576 28.984 9.461 1.00 67.47 A O
ANISOU 4783 OE1 GLU A 597 8136 4330 13170 -752 5241 -900 A O
ATOM 4784 OE2 GLU A 597 7.545 29.884 9.858 1.00 92.53 A O1-
ANISOU 4784 OE2 GLU A 597 11060 7514 16582 -1082 5554 -1559 A O1-
ATOM 4785 N MET A 598 3.899 30.039 12.071 1.00 70.32 A N
ANISOU 4785 N MET A 598 8575 4338 13808 -799 5401 -1053 A N
ATOM 4786 CA MET A 598 3.340 31.228 11.415 1.00 73.79 A C
ANISOU 4786 CA MET A 598 9082 4430 14524 -798 5839 -730 A C
ATOM 4787 C MET A 598 3.355 32.434 12.357 1.00 76.17 A C
ANISOU 4787 C MET A 598 9365 4427 15151 -969 6226 -976 A C
ATOM 4788 O MET A 598 3.726 33.530 11.934 1.00 79.29 A O
ANISOU 4788 O MET A 598 9758 4539 15829 -1095 6681 -987 A O
ATOM 4789 CB MET A 598 1.908 30.982 10.892 1.00 76.54 A C
ANISOU 4789 CB MET A 598 9561 4761 14760 -561 5747 -190 A C
ATOM 4790 CG MET A 598 1.417 32.115 9.962 1.00 85.15 A C
ANISOU 4790 CG MET A 598 10715 5560 16079 -485 6192 221 A C
ATOM 4791 SD MET A 598 -0.368 32.499 9.961 1.00 91.95 A S
ANISOU 4791 SD MET A 598 11686 6308 16943 -234 6267 754 A S
ATOM 4792 CE MET A 598 -0.575 33.260 11.594 1.00 89.85 A C
ANISOU 4792 CE MET A 598 11438 5765 16935 -364 6460 420 A C
ATOM 4793 N LEU A 599 2.964 32.219 13.628 1.00 67.89 A N
ANISOU 4793 N LEU A 599 8310 3430 14055 -982 6063 -1187 A N
ATOM 4794 CA LEU A 599 2.911 33.256 14.643 1.00 68.18 A C
ANISOU 4794 CA LEU A 599 8329 3211 14364 -1150 6392 -1457 A C
ATOM 4795 C LEU A 599 4.334 33.721 15.057 1.00 73.48 A C
ANISOU 4795 C LEU A 599 8826 3929 15164 -1450 6576 -2033 A C
ATOM 4796 O LEU A 599 4.543 34.925 15.179 1.00 75.28 A O
ANISOU 4796 O LEU A 599 9053 3835 15715 -1647 7058 -2187 A O
ATOM 4797 CB LEU A 599 2.081 32.789 15.852 1.00 66.09 A C
ANISOU 4797 CB LEU A 599 8100 3042 13969 -1066 6129 -1512 A C
ATOM 4798 CG LEU A 599 0.553 32.645 15.635 1.00 67.85 A C
ANISOU 4798 CG LEU A 599 8478 3156 14146 -824 6072 -989 A C
ATOM 4799 CD1 LEU A 599 -0.107 32.155 16.864 1.00 65.79 A C
ANISOU 4799 CD1 LEU A 599 8239 3011 13746 -773 5811 -1099 A C
ATOM 4800 CD2 LEU A 599 -0.105 33.971 15.277 1.00 73.44 A C
ANISOU 4800 CD2 LEU A 599 9276 3439 15188 -805 6591 -713 A C
ATOM 4801 N VAL A 600 5.322 32.796 15.179 1.00 68.10 A N
ANISOU 4801 N VAL A 600 7997 3646 14233 -1484 6233 -2339 A N
ATOM 4802 CA VAL A 600 6.696 33.169 15.541 1.00 69.24 A C
ANISOU 4802 CA VAL A 600 7928 3927 14452 -1762 6377 -2899 A C
ATOM 4803 C VAL A 600 7.393 33.884 14.335 1.00 77.55 A C
ANISOU 4803 C VAL A 600 8967 4781 15716 -1898 6758 -2830 A C
ATOM 4804 O VAL A 600 8.182 34.796 14.563 1.00 79.08 A O
ANISOU 4804 O VAL A 600 9046 4857 16145 -2193 7137 -3215 A O
ATOM 4805 CB VAL A 600 7.512 31.966 16.107 1.00 69.39 A C
ANISOU 4805 CB VAL A 600 7779 4475 14113 -1709 5894 -3236 A C
ATOM 4806 CG1 VAL A 600 8.989 32.305 16.274 1.00 71.46 A C
ANISOU 4806 CG1 VAL A 600 7778 4959 14413 -1975 6030 -3785 A C
ATOM 4807 CG2 VAL A 600 6.943 31.521 17.448 1.00 67.37 A C
ANISOU 4807 CG2 VAL A 600 7527 4371 13698 -1623 5633 -3373 A C
ATOM 4808 N ALA A 601 7.053 33.524 13.078 1.00 76.60 A N
ANISOU 4808 N ALA A 601 8968 4613 15521 -1697 6695 -2344 A N
ATOM 4809 CA ALA A 601 7.649 34.135 11.878 1.00 80.42 A C
ANISOU 4809 CA ALA A 601 9458 4922 16175 -1785 7041 -2218 A C
ATOM 4810 C ALA A 601 7.140 35.540 11.632 1.00 91.03 A C
ANISOU 4810 C ALA A 601 10939 5745 17904 -1868 7643 -2022 A C
ATOM 4811 O ALA A 601 7.882 36.360 11.096 1.00 94.52 A O
ANISOU 4811 O ALA A 601 11355 5985 18574 -2066 8067 -2138 A O
ATOM 4812 CB ALA A 601 7.381 33.282 10.651 1.00 79.26 A C
ANISOU 4812 CB ALA A 601 9395 4923 15796 -1528 6773 -1756 A C
ATOM 4813 N LYS A 602 5.878 35.820 11.993 1.00 89.21 A N
ANISOU 4813 N LYS A 602 10865 5288 17745 -1707 7705 -1713 A N
ATOM 4814 CA LYS A 602 5.284 37.148 11.829 1.00 92.67 A C
ANISOU 4814 CA LYS A 602 11459 5210 18541 -1728 8295 -1483 A C
ATOM 4815 C LYS A 602 5.912 38.117 12.835 1.00100.65 A C
ANISOU 4815 C LYS A 602 12397 6001 19845 -2089 8699 -2047 A C
ATOM 4816 O LYS A 602 6.273 39.228 12.452 1.00104.88 A O
ANISOU 4816 O LYS A 602 12996 6151 20702 -2266 9279 -2086 A O
ATOM 4817 CB LYS A 602 3.754 37.093 11.968 1.00 94.09 A C
ANISOU 4817 CB LYS A 602 11800 5275 18677 -1427 8211 -999 A C
ATOM 4818 CG LYS A 602 3.047 36.616 10.696 1.00106.97 A C
ANISOU 4818 CG LYS A 602 13518 7021 20105 -1100 8028 -380 A C
ATOM 4819 CD LYS A 602 1.520 36.538 10.851 1.00115.93 A C
ANISOU 4819 CD LYS A 602 14768 8116 21163 -810 7927 75 A C
ATOM 4820 CE LYS A 602 0.798 37.856 10.637 1.00132.56 A C
ANISOU 4820 CE LYS A 602 17027 9764 23574 -687 8504 446 A C
ATOM 4821 NZ LYS A 602 0.804 38.285 9.211 1.00144.40 A N1+
ANISOU 4821 NZ LYS A 602 18592 11183 25091 -514 8757 912 A N1+
ATOM 4822 N ASP A 603 6.072 37.678 14.104 1.00 95.93 A N
ANISOU 4822 N ASP A 603 11664 5664 19120 -2206 8405 -2495 A N
ATOM 4823 CA ASP A 603 6.717 38.399 15.211 1.00 98.39 A C
ANISOU 4823 CA ASP A 603 11846 5915 19622 -2570 8680 -3126 A C
ATOM 4824 C ASP A 603 8.160 38.845 14.872 1.00107.16 A C
ANISOU 4824 C ASP A 603 12783 7082 20852 -2917 8955 -3581 A C
ATOM 4825 O ASP A 603 8.559 39.968 15.197 1.00110.95 A O
ANISOU 4825 O ASP A 603 13249 7258 21649 -3246 9495 -3931 A O
ATOM 4826 CB ASP A 603 6.760 37.493 16.450 1.00 96.88 A C
ANISOU 4826 CB ASP A 603 11499 6174 19139 -2559 8164 -3477 A C
ATOM 4827 CG ASP A 603 5.436 37.273 17.131 1.00100.30 A C
ANISOU 4827 CG ASP A 603 12077 6529 19504 -2321 7979 -3188 A C
ATOM 4828 OD1 ASP A 603 4.520 38.097 16.927 1.00102.23 A O
ANISOU 4828 OD1 ASP A 603 12517 6331 19995 -2234 8348 -2835 A O
ATOM 4829 OD2 ASP A 603 5.323 36.294 17.897 1.00103.28 A O1-
ANISOU 4829 OD2 ASP A 603 12373 7290 19581 -2214 7487 -3314 A O1-
ATOM 4830 N LEU A 604 8.927 37.951 14.221 1.00103.05 A N
ANISOU 4830 N LEU A 604 12131 6949 20076 -2851 8598 -3586 A N
ATOM 4831 CA LEU A 604 10.324 38.157 13.833 1.00105.77 A C
ANISOU 4831 CA LEU A 604 12277 7446 20464 -3141 8765 -3996 A C
ATOM 4832 C LEU A 604 10.465 38.953 12.507 1.00114.91 A C
ANISOU 4832 C LEU A 604 13587 8195 21880 -3171 9262 -3662 A C
ATOM 4833 O LEU A 604 11.591 39.172 12.050 1.00116.96 A O
ANISOU 4833 O LEU A 604 13703 8548 22189 -3404 9434 -3945 A O
ATOM 4834 CB LEU A 604 11.010 36.774 13.703 1.00102.63 A C
ANISOU 4834 CB LEU A 604 11684 7657 19652 -3000 8143 -4109 A C
ATOM 4835 CG LEU A 604 11.779 36.216 14.917 1.00106.88 A C
ANISOU 4835 CG LEU A 604 11932 8711 19966 -3145 7822 -4730 A C
ATOM 4836 CD1 LEU A 604 10.884 35.952 16.116 1.00105.00 A C
ANISOU 4836 CD1 LEU A 604 11744 8538 19611 -3009 7564 -4737 A C
ATOM 4837 CD2 LEU A 604 12.457 34.926 14.561 1.00106.46 A C
ANISOU 4837 CD2 LEU A 604 11721 9189 19541 -2972 7315 -4768 A C
ATOM 4838 N HIS A 605 9.331 39.361 11.880 1.00112.50 A N
ANISOU 4838 N HIS A 605 13561 7469 21716 -2914 9487 -3047 A N
ATOM 4839 CA HIS A 605 9.260 40.099 10.599 1.00115.13 A C
ANISOU 4839 CA HIS A 605 14079 7401 22264 -2845 9960 -2604 A C
ATOM 4840 C HIS A 605 9.855 39.260 9.423 1.00118.63 A C
ANISOU 4840 C HIS A 605 14447 8168 22460 -2716 9660 -2408 A C
ATOM 4841 O HIS A 605 10.347 39.823 8.438 1.00120.67 A O
ANISOU 4841 O HIS A 605 14746 8223 22879 -2811 10054 -2314 A O
ATOM 4842 CB HIS A 605 9.932 41.499 10.682 1.00121.10 A C
ANISOU 4842 CB HIS A 605 14872 7694 23448 -3235 10728 -2939 A C
ATOM 4843 CG HIS A 605 9.462 42.357 11.822 1.00126.71 A C
ANISOU 4843 CG HIS A 605 15649 8083 24411 -3411 11066 -3205 A C
ATOM 4844 CD2 HIS A 605 8.205 42.708 12.187 1.00128.17 A C
ANISOU 4844 CD2 HIS A 605 16043 7961 24694 -3179 11174 -2844 A C
ATOM 4845 ND1 HIS A 605 10.359 42.934 12.704 1.00131.58 A N
ANISOU 4845 ND1 HIS A 605 16092 8712 25192 -3881 11335 -3934 A N
ATOM 4846 CE1 HIS A 605 9.625 43.613 13.572 1.00132.36 A C
ANISOU 4846 CE1 HIS A 605 16313 8489 25488 -3927 11603 -4000 A C
ATOM 4847 NE2 HIS A 605 8.323 43.506 13.302 1.00130.63 A N
ANISOU 4847 NE2 HIS A 605 16330 8059 25243 -3504 11519 -3348 A N
ATOM 4848 N ILE A 606 9.771 37.917 9.529 1.00111.67 A N
ANISOU 4848 N ILE A 606 13473 7767 21191 -2493 8987 -2336 A N
ATOM 4849 CA ILE A 606 10.262 36.972 8.527 1.00110.01 A C
ANISOU 4849 CA ILE A 606 13194 7899 20705 -2350 8639 -2171 A C
ATOM 4850 C ILE A 606 9.117 36.685 7.519 1.00113.37 A C
ANISOU 4850 C ILE A 606 13827 8237 21013 -1966 8539 -1442 A C
ATOM 4851 O ILE A 606 9.129 37.280 6.439 1.00115.76 A O
ANISOU 4851 O ILE A 606 14230 8314 21440 -1917 8892 -1113 A O
ATOM 4852 CB ILE A 606 10.870 35.702 9.214 1.00110.35 A C
ANISOU 4852 CB ILE A 606 13021 8507 20399 -2346 8022 -2561 A C
ATOM 4853 CG1 ILE A 606 12.288 36.024 9.749 1.00113.77 A C
ANISOU 4853 CG1 ILE A 606 13192 9117 20917 -2725 8173 -3256 A C
ATOM 4854 CG2 ILE A 606 10.902 34.469 8.292 1.00107.58 A C
ANISOU 4854 CG2 ILE A 606 12669 8501 19706 -2087 7562 -2269 A C
ATOM 4855 CD1 ILE A 606 12.877 35.030 10.751 1.00121.38 A C
ANISOU 4855 CD1 ILE A 606 13922 10626 21572 -2729 7658 -3707 A C
ATOM 4856 N SER A 607 8.115 35.843 7.895 1.00106.30 A N
ANISOU 4856 N SER A 607 12989 7523 19879 -1706 8095 -1201 A N
ATOM 4857 CA SER A 607 6.953 35.429 7.090 1.00119.05 A C
ANISOU 4857 CA SER A 607 14752 9161 21320 -1356 7924 -569 A C
ATOM 4858 C SER A 607 7.387 34.815 5.741 1.00143.22 A C
ANISOU 4858 C SER A 607 17789 12459 24169 -1246 7763 -334 A C
ATOM 4859 O SER A 607 8.333 34.026 5.679 1.00 95.57 A O
ANISOU 4859 O SER A 607 11617 6746 17950 -1336 7460 -645 A O
ATOM 4860 CB SER A 607 5.994 36.599 6.866 1.00123.74 A C
ANISOU 4860 CB SER A 607 15528 9301 22186 -1238 8428 -148 A C
ATOM 4861 OG SER A 607 4.857 36.221 6.107 1.00127.87 A O
ANISOU 4861 OG SER A 607 16153 9923 22510 -890 8247 447 A O
ATOM 4862 N ALA A 2 -36.485 -4.645 20.166 1.00116.42 B N
ANISOU 4862 N ALA A 2 8971 19100 16164 -7475 6772 -10380 B N
ATOM 4863 CA ALA A 2 -36.469 -4.664 21.626 1.00109.81 B C
ANISOU 4863 CA ALA A 2 8774 16808 16140 -6827 6727 -9599 B C
ATOM 4864 C ALA A 2 -37.888 -4.668 22.163 1.00114.42 B C
ANISOU 4864 C ALA A 2 9315 17529 16630 -6731 6622 -9424 B C
ATOM 4865 O ALA A 2 -38.238 -5.533 22.969 1.00114.99 B O
ANISOU 4865 O ALA A 2 9468 16624 17600 -6674 7030 -9628 B O
ATOM 4866 CB ALA A 2 -35.700 -3.462 22.161 1.00103.24 B C
ANISOU 4866 CB ALA A 2 8564 15626 15036 -6152 6146 -8394 B C
ATOM 4867 N ASP A 3 -38.710 -3.710 21.697 1.00110.66 B N
ANISOU 4867 N ASP A 3 8670 18278 15097 -6703 6103 -8999 B N
ATOM 4868 CA ASP A 3 -40.106 -3.562 22.078 1.00109.95 B C
ANISOU 4868 CA ASP A 3 8493 18508 14776 -6619 5941 -8775 B C
ATOM 4869 C ASP A 3 -40.936 -4.666 21.428 1.00120.01 B C
ANISOU 4869 C ASP A 3 9065 20408 16125 -7356 6459 -10037 B C
ATOM 4870 O ASP A 3 -40.998 -4.742 20.200 1.00126.04 B O
ANISOU 4870 O ASP A 3 9194 22512 16182 -7948 6525 -10750 B O
ATOM 4871 CB ASP A 3 -40.627 -2.161 21.684 1.00110.81 B C
ANISOU 4871 CB ASP A 3 8556 19760 13787 -6352 5274 -7859 B C
ATOM 4872 CG ASP A 3 -42.069 -1.831 22.049 1.00126.65 B C
ANISOU 4872 CG ASP A 3 10457 22175 15489 -6216 5055 -7487 B C
ATOM 4873 OD1 ASP A 3 -42.561 -2.345 23.085 1.00126.40 B O
ANISOU 4873 OD1 ASP A 3 10730 21123 16172 -6010 5237 -7471 B O
ATOM 4874 OD2 ASP A 3 -42.686 -1.005 21.338 1.00135.42 B O1-
ANISOU 4874 OD2 ASP A 3 11176 24621 15657 -6269 4694 -7100 B O1-
ATOM 4875 N PRO A 4 -41.571 -5.540 22.239 1.00115.68 B N
ANISOU 4875 N PRO A 4 8573 18944 16435 -7352 6866 -10357 B N
ATOM 4876 CA PRO A 4 -42.434 -6.593 21.670 1.00122.97 B C
ANISOU 4876 CA PRO A 4 8797 20407 17520 -8074 7421 -11623 B C
ATOM 4877 C PRO A 4 -43.668 -6.021 20.952 1.00129.47 B C
ANISOU 4877 C PRO A 4 9119 22896 17178 -8337 7033 -11644 B C
ATOM 4878 O PRO A 4 -44.368 -6.766 20.263 1.00131.27 B O
ANISOU 4878 O PRO A 4 8985 23603 17289 -8575 7074 -12057 B O
ATOM 4879 CB PRO A 4 -42.836 -7.416 22.901 1.00122.78 B C
ANISOU 4879 CB PRO A 4 9062 18875 18714 -7816 7858 -11601 B C
ATOM 4880 CG PRO A 4 -42.746 -6.459 24.033 1.00118.65 B C
ANISOU 4880 CG PRO A 4 9302 17632 18148 -6963 7280 -10174 B C
ATOM 4881 CD PRO A 4 -41.593 -5.566 23.713 1.00110.79 B C
ANISOU 4881 CD PRO A 4 8604 16863 16629 -6700 6840 -9560 B C
ATOM 4882 N SER A 5 -43.915 -4.697 21.098 1.00121.49 B N
ANISOU 4882 N SER A 5 8409 22398 15355 -7798 6302 -10408 B N
ATOM 4883 CA SER A 5 -45.048 -3.986 20.498 1.00124.45 B C
ANISOU 4883 CA SER A 5 8323 24329 14635 -7906 5880 -10111 B C
ATOM 4884 C SER A 5 -44.720 -3.449 19.091 1.00133.12 B C
ANISOU 4884 C SER A 5 8814 27189 14575 -8293 5640 -10230 B C
ATOM 4885 O SER A 5 -45.636 -3.053 18.366 1.00135.98 B O
ANISOU 4885 O SER A 5 8718 28888 14061 -8351 5294 -9918 B O
ATOM 4886 CB SER A 5 -45.503 -2.840 21.402 1.00121.30 B C
ANISOU 4886 CB SER A 5 8493 23491 14104 -7113 5313 -8678 B C
ATOM 4887 OG SER A 5 -45.492 -3.204 22.774 1.00125.06 B O
ANISOU 4887 OG SER A 5 9617 22283 15616 -6672 5485 -8412 B O
ATOM 4888 N SER A 6 -43.431 -3.461 18.709 1.00128.21 B N
ANISOU 4888 N SER A 6 8322 26335 14059 -8348 5729 -10377 B N
ATOM 4889 CA SER A 6 -42.928 -2.984 17.414 1.00131.86 B C
ANISOU 4889 CA SER A 6 8320 28240 13542 -8606 5495 -10354 B C
ATOM 4890 C SER A 6 -42.301 -4.125 16.601 1.00133.71 B C
ANISOU 4890 C SER A 6 8757 27677 14370 -8529 5610 -10657 B C
ATOM 4891 O SER A 6 -41.917 -5.153 17.167 1.00131.95 B O
ANISOU 4891 O SER A 6 8751 26214 15172 -8659 6118 -11347 B O
ATOM 4892 CB SER A 6 -41.897 -1.874 17.632 1.00129.36 B C
ANISOU 4892 CB SER A 6 8525 27535 13090 -8024 5092 -9238 B C
ATOM 4893 OG SER A 6 -41.198 -1.476 16.459 1.00138.01 B O
ANISOU 4893 OG SER A 6 9222 29825 13389 -8254 4941 -9226 B O
ATOM 4894 N PHE A 7 -42.238 -3.950 15.271 1.00132.18 B N
ANISOU 4894 N PHE A 7 8313 28428 13481 -8498 5272 -10353 B N
ATOM 4895 CA PHE A 7 -41.607 -4.902 14.358 1.00131.69 B C
ANISOU 4895 CA PHE A 7 8333 27922 13782 -8534 5378 -10695 B C
ATOM 4896 C PHE A 7 -40.219 -4.384 13.968 1.00133.64 B C
ANISOU 4896 C PHE A 7 8748 28158 13871 -8441 5291 -10459 B C
ATOM 4897 O PHE A 7 -39.394 -5.166 13.501 1.00132.73 B O
ANISOU 4897 O PHE A 7 8755 27451 14226 -8521 5500 -10867 B O
ATOM 4898 CB PHE A 7 -42.477 -5.172 13.113 1.00133.81 B C
ANISOU 4898 CB PHE A 7 8467 28730 13642 -8329 5000 -10266 B C
ATOM 4899 CG PHE A 7 -43.563 -6.219 13.275 1.00134.79 B C
ANISOU 4899 CG PHE A 7 8633 28296 14287 -8307 5109 -10504 B C
ATOM 4900 CD1 PHE A 7 -43.240 -7.549 13.532 1.00136.01 B C
ANISOU 4900 CD1 PHE A 7 9043 27251 15385 -8329 5449 -10985 B C
ATOM 4901 CD2 PHE A 7 -44.901 -5.890 13.095 1.00136.86 B C
ANISOU 4901 CD2 PHE A 7 8758 29098 14146 -8126 4798 -10007 B C
ATOM 4902 CE1 PHE A 7 -44.242 -8.518 13.665 1.00136.38 B C
ANISOU 4902 CE1 PHE A 7 9098 26852 15869 -8307 5542 -11143 B C
ATOM 4903 CE2 PHE A 7 -45.897 -6.865 13.206 1.00138.66 B C
ANISOU 4903 CE2 PHE A 7 9058 28770 14854 -8068 4867 -10151 B C
ATOM 4904 CZ PHE A 7 -45.563 -8.168 13.498 1.00136.39 B C
ANISOU 4904 CZ PHE A 7 8890 27536 15396 -8253 5285 -10843 B C
ATOM 4905 N ALA A 8 -39.962 -3.071 14.190 1.00131.64 B N
ANISOU 4905 N ALA A 8 8308 28863 12847 -8484 5098 -10042 B N
ATOM 4906 CA ALA A 8 -38.693 -2.400 13.913 1.00131.44 B C
ANISOU 4906 CA ALA A 8 8321 29105 12517 -8505 5046 -9868 B C
ATOM 4907 C ALA A 8 -37.586 -2.847 14.877 1.00132.18 B C
ANISOU 4907 C ALA A 8 8808 27861 13555 -8631 5522 -10474 B C
ATOM 4908 O ALA A 8 -37.871 -3.228 16.014 1.00131.69 B O
ANISOU 4908 O ALA A 8 8917 26914 14206 -8726 5890 -10905 B O
ATOM 4909 CB ALA A 8 -38.874 -0.895 14.001 1.00133.01 B C
ANISOU 4909 CB ALA A 8 8341 30409 11787 -8292 4621 -8878 B C
ATOM 4910 N SER A 9 -36.325 -2.813 14.403 1.00128.18 B N
ANISOU 4910 N SER A 9 8275 27404 13021 -8837 5673 -10785 B N
ATOM 4911 CA SER A 9 -35.139 -3.191 15.176 1.00126.22 B C
ANISOU 4911 CA SER A 9 8332 25937 13690 -9021 6205 -11429 B C
ATOM 4912 C SER A 9 -34.292 -1.950 15.510 1.00121.24 B C
ANISOU 4912 C SER A 9 8314 24876 12876 -8283 5655 -10057 B C
ATOM 4913 O SER A 9 -33.610 -1.425 14.628 1.00121.86 B O
ANISOU 4913 O SER A 9 8170 25837 12295 -8392 5485 -9909 B O
ATOM 4914 CB SER A 9 -34.308 -4.234 14.434 1.00127.16 B C
ANISOU 4914 CB SER A 9 8604 25321 14391 -8954 6341 -11706 B C
ATOM 4915 OG SER A 9 -35.047 -5.435 14.267 1.00130.58 B O
ANISOU 4915 OG SER A 9 9197 24999 15420 -8684 6310 -11648 B O
ATOM 4916 N PRO A 10 -34.359 -1.449 16.776 1.00109.50 B N
ANISOU 4916 N PRO A 10 7564 22079 11961 -7541 5391 -9059 B N
ATOM 4917 CA PRO A 10 -33.575 -0.251 17.148 1.00102.46 B C
ANISOU 4917 CA PRO A 10 7228 20724 10976 -6866 4925 -7840 B C
ATOM 4918 C PRO A 10 -32.064 -0.509 17.194 1.00103.59 B C
ANISOU 4918 C PRO A 10 7701 19969 11689 -6825 5127 -8041 B C
ATOM 4919 O PRO A 10 -31.280 0.441 17.139 1.00 99.93 B O
ANISOU 4919 O PRO A 10 7510 19476 10983 -6453 4801 -7271 B O
ATOM 4920 CB PRO A 10 -34.119 0.130 18.545 1.00 97.57 B C
ANISOU 4920 CB PRO A 10 7220 18950 10902 -6225 4718 -7021 B C
ATOM 4921 CG PRO A 10 -35.322 -0.716 18.764 1.00104.74 B C
ANISOU 4921 CG PRO A 10 7836 19983 11977 -6538 4977 -7652 B C
ATOM 4922 CD PRO A 10 -35.143 -1.942 17.927 1.00107.40 B C
ANISOU 4922 CD PRO A 10 7614 20743 12449 -7312 5536 -9035 B C
ATOM 4923 N GLU A 11 -31.663 -1.789 17.277 1.00102.21 B N
ANISOU 4923 N GLU A 11 7459 19053 12325 -7210 5707 -9066 B N
ATOM 4924 CA GLU A 11 -30.264 -2.241 17.314 1.00100.80 B C
ANISOU 4924 CA GLU A 11 7508 17975 12819 -7232 6010 -9372 B C
ATOM 4925 C GLU A 11 -29.632 -2.263 15.909 1.00108.95 B C
ANISOU 4925 C GLU A 11 8007 20188 13200 -7791 6121 -10019 B C
ATOM 4926 O GLU A 11 -28.401 -2.309 15.787 1.00106.61 B O
ANISOU 4926 O GLU A 11 7909 19374 13223 -7741 6228 -10050 B O
ATOM 4927 CB GLU A 11 -30.168 -3.641 17.964 1.00103.85 B C
ANISOU 4927 CB GLU A 11 7920 17101 14438 -7424 6682 -10164 B C
ATOM 4928 CG GLU A 11 -31.064 -4.700 17.324 1.00126.07 B C
ANISOU 4928 CG GLU A 11 10028 20567 17307 -8182 7225 -11445 B C
ATOM 4929 CD GLU A 11 -31.517 -5.832 18.229 1.00147.61 B C
ANISOU 4929 CD GLU A 11 13009 21927 21148 -7873 7482 -11369 B C
ATOM 4930 OE1 GLU A 11 -31.285 -7.008 17.867 1.00145.90 B O
ANISOU 4930 OE1 GLU A 11 12734 21232 21467 -7880 7661 -11610 B O
ATOM 4931 OE2 GLU A 11 -32.118 -5.546 19.289 1.00139.15 B O1-
ANISOU 4931 OE2 GLU A 11 12141 20331 20399 -7678 7555 -11110 B O1-
ATOM 4932 N LYS A 12 -30.474 -2.258 14.856 1.00111.23 B N
ANISOU 4932 N LYS A 12 7579 22128 12556 -8341 6108 -10548 B N
ATOM 4933 CA LYS A 12 -30.004 -2.296 13.472 1.00116.83 B C
ANISOU 4933 CA LYS A 12 7657 24236 12497 -8946 6220 -11220 B C
ATOM 4934 C LYS A 12 -29.827 -0.888 12.897 1.00116.80 B C
ANISOU 4934 C LYS A 12 7620 25350 11411 -8605 5592 -10099 B C
ATOM 4935 O LYS A 12 -28.796 -0.619 12.288 1.00116.42 B O
ANISOU 4935 O LYS A 12 7549 25528 11158 -8663 5576 -10076 B O
ATOM 4936 CB LYS A 12 -30.956 -3.130 12.590 1.00123.56 B C
ANISOU 4936 CB LYS A 12 8048 25818 13081 -9216 6244 -11697 B C
ATOM 4937 CG LYS A 12 -30.780 -4.635 12.767 1.00134.89 B C
ANISOU 4937 CG LYS A 12 10107 25322 15823 -8624 6264 -11460 B C
ATOM 4938 CD LYS A 12 -31.718 -5.433 11.863 1.00143.68 B C
ANISOU 4938 CD LYS A 12 11369 26352 16869 -8112 5773 -10787 B C
ATOM 4939 CE LYS A 12 -31.451 -6.916 11.938 1.00148.26 B C
ANISOU 4939 CE LYS A 12 12324 25566 18441 -7812 5870 -10756 B C
ATOM 4940 NZ LYS A 12 -32.291 -7.676 10.978 1.00152.19 B N1+
ANISOU 4940 NZ LYS A 12 12848 26182 18797 -7552 5536 -10385 B N1+
ATOM 4941 N PHE A 13 -30.841 -0.016 13.021 1.00111.49 B N
ANISOU 4941 N PHE A 13 6866 25424 10071 -8280 5131 -9189 B N
ATOM 4942 CA PHE A 13 -30.779 1.351 12.497 1.00109.80 B C
ANISOU 4942 CA PHE A 13 6532 26244 8942 -7913 4607 -7999 B C
ATOM 4943 C PHE A 13 -31.620 2.294 13.346 1.00105.87 B C
ANISOU 4943 C PHE A 13 6386 25381 8459 -7225 4186 -6748 B C
ATOM 4944 O PHE A 13 -32.528 1.846 14.056 1.00104.24 B O
ANISOU 4944 O PHE A 13 6292 24695 8618 -7200 4264 -6945 B O
ATOM 4945 CB PHE A 13 -31.191 1.423 11.014 1.00121.09 B C
ANISOU 4945 CB PHE A 13 6961 29950 9097 -8540 4586 -8386 B C
ATOM 4946 CG PHE A 13 -32.561 0.895 10.665 1.00124.52 B C
ANISOU 4946 CG PHE A 13 7124 30809 9378 -8574 4517 -8517 B C
ATOM 4947 CD1 PHE A 13 -32.750 -0.447 10.358 1.00126.05 B C
ANISOU 4947 CD1 PHE A 13 7527 30042 10324 -8613 4740 -9231 B C
ATOM 4948 CD2 PHE A 13 -33.651 1.752 10.578 1.00127.17 B C
ANISOU 4948 CD2 PHE A 13 7288 31897 9132 -8179 4094 -7450 B C
ATOM 4949 CE1 PHE A 13 -34.014 -0.930 10.005 1.00127.06 B C
ANISOU 4949 CE1 PHE A 13 7574 30250 10454 -8469 4599 -9128 B C
ATOM 4950 CE2 PHE A 13 -34.916 1.268 10.230 1.00129.51 B C
ANISOU 4950 CE2 PHE A 13 7580 32080 9546 -7976 3964 -7345 B C
ATOM 4951 CZ PHE A 13 -35.090 -0.071 9.953 1.00127.56 B C
ANISOU 4951 CZ PHE A 13 7406 31199 9862 -8231 4242 -8303 B C
ATOM 4952 N ASN A 14 -31.320 3.599 13.269 1.00 97.39 B N
ANISOU 4952 N ASN A 14 5453 24505 7047 -6680 3790 -5483 B N
ATOM 4953 CA ASN A 14 -31.984 4.623 14.072 1.00 91.87 B C
ANISOU 4953 CA ASN A 14 5083 23344 6479 -6000 3452 -4255 B C
ATOM 4954 C ASN A 14 -32.468 5.809 13.242 1.00 98.72 B C
ANISOU 4954 C ASN A 14 5371 25719 6418 -5806 3134 -3151 B C
ATOM 4955 O ASN A 14 -31.683 6.386 12.483 1.00102.14 B O
ANISOU 4955 O ASN A 14 5587 26770 6450 -5773 3059 -2744 B O
ATOM 4956 CB ASN A 14 -30.995 5.122 15.118 1.00 85.07 B C
ANISOU 4956 CB ASN A 14 5082 20739 6502 -5392 3382 -3687 B C
ATOM 4957 CG ASN A 14 -31.453 5.054 16.540 1.00103.52 B C
ANISOU 4957 CG ASN A 14 8034 21670 9628 -4983 3363 -3474 B C
ATOM 4958 ND2 ASN A 14 -30.699 4.334 17.360 1.00 90.27 B N
ANISOU 4958 ND2 ASN A 14 6895 18626 8779 -4950 3578 -3996 B N
ATOM 4959 OD1 ASN A 14 -32.403 5.730 16.943 1.00102.52 B O
ANISOU 4959 OD1 ASN A 14 7900 21652 9399 -4649 3159 -2742 B O
ATOM 4960 N ILE A 15 -33.752 6.181 13.393 1.00 95.18 B N
ANISOU 4960 N ILE A 15 4645 25847 5673 -5650 2970 -2597 B N
ATOM 4961 CA ILE A 15 -34.341 7.355 12.739 1.00 98.88 B C
ANISOU 4961 CA ILE A 15 4527 27646 5395 -5364 2700 -1338 B C
ATOM 4962 C ILE A 15 -33.913 8.533 13.584 1.00 97.39 B C
ANISOU 4962 C ILE A 15 4961 26112 5929 -4568 2562 -138 B C
ATOM 4963 O ILE A 15 -34.215 8.576 14.781 1.00 92.58 B O
ANISOU 4963 O ILE A 15 4969 24118 6090 -4222 2563 -40 B O
ATOM 4964 CB ILE A 15 -35.889 7.272 12.545 1.00106.41 B C
ANISOU 4964 CB ILE A 15 4860 29811 5758 -5529 2611 -1211 B C
ATOM 4965 CG1 ILE A 15 -36.266 6.150 11.562 1.00113.44 B C
ANISOU 4965 CG1 ILE A 15 5011 32228 5862 -6410 2792 -2522 B C
ATOM 4966 CG2 ILE A 15 -36.478 8.629 12.088 1.00110.96 B C
ANISOU 4966 CG2 ILE A 15 4870 31521 5768 -5074 2357 375 B C
ATOM 4967 CD1 ILE A 15 -37.740 5.686 11.669 1.00112.40 B C
ANISOU 4967 CD1 ILE A 15 4457 32830 5419 -6662 2790 -2829 B C
ATOM 4968 N LYS A 16 -33.189 9.466 12.973 1.00 95.33 B N
ANISOU 4968 N LYS A 16 4510 26264 5445 -4309 2484 715 B N
ATOM 4969 CA LYS A 16 -32.619 10.619 13.657 1.00 89.85 B C
ANISOU 4969 CA LYS A 16 4335 24316 5486 -3613 2437 1757 B C
ATOM 4970 C LYS A 16 -33.411 11.907 13.417 1.00 98.42 B C
ANISOU 4970 C LYS A 16 4922 26095 6380 -3132 2332 3243 B C
ATOM 4971 O LYS A 16 -33.396 12.795 14.268 1.00 94.67 B O
ANISOU 4971 O LYS A 16 4866 24421 6684 -2562 2359 4014 B O
ATOM 4972 CB LYS A 16 -31.149 10.798 13.227 1.00 90.46 B C
ANISOU 4972 CB LYS A 16 4590 24120 5659 -3614 2501 1693 B C
ATOM 4973 CG LYS A 16 -30.219 9.678 13.710 1.00 88.50 B C
ANISOU 4973 CG LYS A 16 4947 22789 5888 -3945 2651 405 B C
ATOM 4974 CD LYS A 16 -29.887 9.802 15.206 1.00 81.42 B C
ANISOU 4974 CD LYS A 16 4954 19921 6062 -3513 2679 415 B C
ATOM 4975 CE LYS A 16 -29.500 8.490 15.824 1.00 80.03 B C
ANISOU 4975 CE LYS A 16 5228 18842 6339 -3848 2848 -800 B C
ATOM 4976 NZ LYS A 16 -29.289 8.632 17.285 1.00 86.45 B N1+
ANISOU 4976 NZ LYS A 16 6807 17978 8063 -3425 2852 -683 B N1+
ATOM 4977 N HIS A 17 -34.107 12.002 12.280 1.00104.11 B N
ANISOU 4977 N HIS A 17 4694 28766 6096 -3370 2252 3641 B N
ATOM 4978 CA HIS A 17 -34.877 13.185 11.908 1.00109.49 B C
ANISOU 4978 CA HIS A 17 4733 30321 6547 -2917 2189 5179 B C
ATOM 4979 C HIS A 17 -35.962 12.828 10.914 1.00122.72 B C
ANISOU 4979 C HIS A 17 5403 34166 7060 -3333 2077 5210 B C
ATOM 4980 O HIS A 17 -35.804 11.902 10.114 1.00125.42 B O
ANISOU 4980 O HIS A 17 5416 35593 6644 -3981 2070 4155 B O
ATOM 4981 CB HIS A 17 -33.944 14.260 11.303 1.00112.74 B C
ANISOU 4981 CB HIS A 17 4904 30926 7005 -2548 2251 6262 B C
ATOM 4982 CG HIS A 17 -34.598 15.577 11.014 1.00121.33 B C
ANISOU 4982 CG HIS A 17 5362 32588 8150 -1971 2291 8008 B C
ATOM 4983 CD2 HIS A 17 -34.972 16.114 9.828 1.00127.10 B C
ANISOU 4983 CD2 HIS A 17 5700 34055 8536 -1861 2278 8546 B C
ATOM 4984 ND1 HIS A 17 -34.862 16.486 12.020 1.00118.95 B N
ANISOU 4984 ND1 HIS A 17 5489 30771 8937 -1352 2432 8794 B N
ATOM 4985 CE1 HIS A 17 -35.406 17.533 11.421 1.00125.35 B C
ANISOU 4985 CE1 HIS A 17 5491 32514 9624 -943 2516 10346 B C
ATOM 4986 NE2 HIS A 17 -35.475 17.363 10.100 1.00126.65 B N
ANISOU 4986 NE2 HIS A 17 5669 33212 9241 -1216 2412 9772 B N
ATOM 4987 N MET A 18 -37.051 13.597 10.955 1.00124.00 B N
ANISOU 4987 N MET A 18 5089 34861 7166 -2946 2024 6397 B N
ATOM 4988 CA MET A 18 -38.183 13.469 10.058 1.00125.05 B C
ANISOU 4988 CA MET A 18 5213 35161 7140 -2983 1953 6108 B C
ATOM 4989 C MET A 18 -38.589 14.821 9.507 1.00129.45 B C
ANISOU 4989 C MET A 18 6044 34789 8354 -2302 1991 7172 B C
ATOM 4990 O MET A 18 -38.756 15.775 10.266 1.00129.06 B O
ANISOU 4990 O MET A 18 5960 34214 8864 -1801 2075 8271 B O
ATOM 4991 CB MET A 18 -39.389 12.848 10.784 1.00126.36 B C
ANISOU 4991 CB MET A 18 5381 35323 7305 -3157 1901 5633 B C
ATOM 4992 CG MET A 18 -39.319 11.357 10.965 1.00128.51 B C
ANISOU 4992 CG MET A 18 5812 35722 7295 -3864 1930 3968 B C
ATOM 4993 SD MET A 18 -40.946 10.731 11.490 1.00131.47 B S
ANISOU 4993 SD MET A 18 6287 35840 7825 -3975 1893 3412 B S
ATOM 4994 CE MET A 18 -40.528 9.047 11.852 1.00128.75 B C
ANISOU 4994 CE MET A 18 5921 35849 7148 -4889 2051 1542 B C
ATOM 4995 N HIS A 19 -38.752 14.902 8.187 1.00128.47 B N
ANISOU 4995 N HIS A 19 5930 34891 7992 -2354 1950 6972 B N
ATOM 4996 CA HIS A 19 -39.317 16.067 7.518 1.00129.20 B C
ANISOU 4996 CA HIS A 19 6131 34488 8472 -1884 1972 7799 B C
ATOM 4997 C HIS A 19 -40.703 15.601 7.049 1.00132.41 B C
ANISOU 4997 C HIS A 19 6714 34763 8831 -2006 1854 7183 B C
ATOM 4998 O HIS A 19 -40.789 14.642 6.282 1.00132.00 B O
ANISOU 4998 O HIS A 19 6664 35140 8349 -2397 1781 6270 B O
ATOM 4999 CB HIS A 19 -38.425 16.604 6.382 1.00130.40 B C
ANISOU 4999 CB HIS A 19 6459 34437 8650 -1789 2027 7908 B C
ATOM 5000 CG HIS A 19 -38.991 17.831 5.738 1.00133.31 B C
ANISOU 5000 CG HIS A 19 7083 34057 9513 -1360 2068 8547 B C
ATOM 5001 CD2 HIS A 19 -38.755 19.136 6.003 1.00134.51 B C
ANISOU 5001 CD2 HIS A 19 7371 33417 10319 -899 2217 9456 B C
ATOM 5002 ND1 HIS A 19 -39.954 17.746 4.743 1.00135.13 B N
ANISOU 5002 ND1 HIS A 19 7457 34280 9607 -1425 1962 8167 B N
ATOM 5003 CE1 HIS A 19 -40.253 18.994 4.424 1.00134.82 B C
ANISOU 5003 CE1 HIS A 19 7490 33769 9966 -1043 2027 8943 B C
ATOM 5004 NE2 HIS A 19 -39.555 19.866 5.152 1.00134.65 B N
ANISOU 5004 NE2 HIS A 19 7488 33216 10456 -728 2192 9686 B N
ATOM 5005 N LEU A 20 -41.780 16.199 7.584 1.00130.71 B N
ANISOU 5005 N LEU A 20 6379 34390 8896 -1714 1846 7846 B N
ATOM 5006 CA LEU A 20 -43.144 15.762 7.284 1.00131.41 B C
ANISOU 5006 CA LEU A 20 6472 34593 8864 -1832 1729 7416 B C
ATOM 5007 C LEU A 20 -43.949 16.747 6.438 1.00135.36 B C
ANISOU 5007 C LEU A 20 7315 34317 9800 -1485 1711 7754 B C
ATOM 5008 O LEU A 20 -44.254 17.851 6.884 1.00134.39 B O
ANISOU 5008 O LEU A 20 7178 33745 10139 -1083 1795 8644 B O
ATOM 5009 CB LEU A 20 -43.924 15.483 8.587 1.00131.19 B C
ANISOU 5009 CB LEU A 20 6312 34553 8982 -1815 1724 7524 B C
ATOM 5010 CG LEU A 20 -43.406 14.405 9.543 1.00134.33 B C
ANISOU 5010 CG LEU A 20 6790 34982 9267 -2169 1741 6747 B C
ATOM 5011 CD1 LEU A 20 -44.124 14.474 10.872 1.00134.17 B C
ANISOU 5011 CD1 LEU A 20 6663 34805 9512 -2017 1761 7154 B C
ATOM 5012 CD2 LEU A 20 -43.609 13.027 8.973 1.00136.72 B C
ANISOU 5012 CD2 LEU A 20 7208 35543 9196 -2707 1676 5371 B C
ATOM 5013 N LYS A 21 -44.345 16.312 5.234 1.00134.73 B N
ANISOU 5013 N LYS A 21 7266 34538 9388 -1686 1605 7212 B N
ATOM 5014 CA LYS A 21 -45.218 17.066 4.335 1.00135.40 B C
ANISOU 5014 CA LYS A 21 7475 34334 9637 -1462 1549 7509 B C
ATOM 5015 C LYS A 21 -46.599 16.396 4.421 1.00138.96 B C
ANISOU 5015 C LYS A 21 8066 34569 10162 -1580 1432 6922 B C
ATOM 5016 O LYS A 21 -46.826 15.365 3.783 1.00138.89 B O
ANISOU 5016 O LYS A 21 8039 34916 9817 -1899 1344 6154 B O
ATOM 5017 CB LYS A 21 -44.647 17.094 2.905 1.00137.58 B C
ANISOU 5017 CB LYS A 21 8002 34499 9772 -1535 1526 7166 B C
ATOM 5018 CG LYS A 21 -43.560 18.154 2.695 1.00147.96 B C
ANISOU 5018 CG LYS A 21 10119 34250 11849 -1223 1669 7241 B C
ATOM 5019 CD LYS A 21 -42.431 17.730 1.721 1.00155.62 B C
ANISOU 5019 CD LYS A 21 11673 34537 12916 -1361 1702 6463 B C
ATOM 5020 CE LYS A 21 -42.789 17.433 0.281 1.00163.39 B C
ANISOU 5020 CE LYS A 21 13266 34741 14073 -1407 1620 5714 B C
ATOM 5021 NZ LYS A 21 -41.575 17.077 -0.511 1.00167.37 B N1+
ANISOU 5021 NZ LYS A 21 14161 34814 14619 -1515 1681 5177 B N1+
ATOM 5022 N LEU A 22 -47.484 16.925 5.287 1.00137.08 B N
ANISOU 5022 N LEU A 22 7687 34208 10189 -1357 1444 7477 B N
ATOM 5023 CA LEU A 22 -48.808 16.331 5.513 1.00137.42 B C
ANISOU 5023 CA LEU A 22 7663 34356 10195 -1472 1341 7113 B C
ATOM 5024 C LEU A 22 -49.922 17.072 4.775 1.00141.36 B C
ANISOU 5024 C LEU A 22 8454 34215 11041 -1234 1268 7240 B C
ATOM 5025 O LEU A 22 -50.087 18.280 4.956 1.00140.71 B O
ANISOU 5025 O LEU A 22 8400 33752 11312 -893 1336 7996 B O
ATOM 5026 CB LEU A 22 -49.159 16.268 7.015 1.00136.84 B C
ANISOU 5026 CB LEU A 22 7448 34214 10331 -1401 1401 7379 B C
ATOM 5027 CG LEU A 22 -48.096 15.779 8.012 1.00139.34 B C
ANISOU 5027 CG LEU A 22 7868 34370 10707 -1526 1497 7128 B C
ATOM 5028 CD1 LEU A 22 -48.529 16.065 9.437 1.00138.79 B C
ANISOU 5028 CD1 LEU A 22 7699 34051 10984 -1315 1575 7681 B C
ATOM 5029 CD2 LEU A 22 -47.814 14.293 7.853 1.00141.10 B C
ANISOU 5029 CD2 LEU A 22 8136 34912 10562 -2014 1446 5982 B C
ATOM 5030 N HIS A 23 -50.690 16.335 3.950 1.00140.53 B N
ANISOU 5030 N HIS A 23 8294 34449 10652 -1451 1133 6685 B N
ATOM 5031 CA HIS A 23 -51.842 16.862 3.221 1.00141.68 B C
ANISOU 5031 CA HIS A 23 8538 34346 10949 -1294 1032 6817 B C
ATOM 5032 C HIS A 23 -53.113 16.367 3.928 1.00146.45 B C
ANISOU 5032 C HIS A 23 9257 34562 11825 -1329 975 6440 B C
ATOM 5033 O HIS A 23 -53.391 15.165 3.912 1.00146.25 B O
ANISOU 5033 O HIS A 23 9135 34876 11557 -1637 916 5765 B O
ATOM 5034 CB HIS A 23 -51.807 16.436 1.737 1.00142.84 B C
ANISOU 5034 CB HIS A 23 8841 34574 10859 -1449 928 6310 B C
ATOM 5035 CG HIS A 23 -52.979 16.926 0.937 1.00145.87 B C
ANISOU 5035 CG HIS A 23 9427 34545 11453 -1298 811 6333 B C
ATOM 5036 CD2 HIS A 23 -54.207 16.377 0.772 1.00147.59 B C
ANISOU 5036 CD2 HIS A 23 9658 34716 11704 -1389 688 5932 B C
ATOM 5037 ND1 HIS A 23 -52.924 18.114 0.232 1.00147.29 B N
ANISOU 5037 ND1 HIS A 23 9821 34299 11846 -1032 818 6794 B N
ATOM 5038 CE1 HIS A 23 -54.110 18.247 -0.342 1.00147.53 B C
ANISOU 5038 CE1 HIS A 23 9855 34296 11902 -988 688 6746 B C
ATOM 5039 NE2 HIS A 23 -54.917 17.228 -0.042 1.00147.94 B N
ANISOU 5039 NE2 HIS A 23 9797 34548 11864 -1189 605 6244 B N
ATOM 5040 N VAL A 24 -53.877 17.272 4.558 1.00145.42 B N
ANISOU 5040 N VAL A 24 9049 34205 11997 -1054 1001 7064 B N
ATOM 5041 CA VAL A 24 -55.085 16.821 5.248 1.00146.30 B C
ANISOU 5041 CA VAL A 24 9070 34302 12215 -1103 950 6870 B C
ATOM 5042 C VAL A 24 -56.328 17.250 4.447 1.00151.42 B C
ANISOU 5042 C VAL A 24 10014 34364 13153 -971 831 6718 B C
ATOM 5043 O VAL A 24 -56.491 18.427 4.110 1.00151.23 B O
ANISOU 5043 O VAL A 24 10077 34040 13344 -703 845 7252 B O
ATOM 5044 CB VAL A 24 -55.167 17.200 6.763 1.00148.42 B C
ANISOU 5044 CB VAL A 24 9393 34098 12902 -920 1075 7230 B C
ATOM 5045 CG1 VAL A 24 -53.909 16.773 7.514 1.00147.70 B C
ANISOU 5045 CG1 VAL A 24 9256 34157 12706 -1032 1186 7186 B C
ATOM 5046 CG2 VAL A 24 -55.443 18.681 6.987 1.00148.03 B C
ANISOU 5046 CG2 VAL A 24 9413 33535 13298 -520 1156 8052 B C
ATOM 5047 N ASP A 25 -57.158 16.264 4.086 1.00150.97 B N
ANISOU 5047 N ASP A 25 9835 34643 12886 -1204 710 6172 B N
ATOM 5048 CA ASP A 25 -58.407 16.494 3.372 1.00152.23 B C
ANISOU 5048 CA ASP A 25 10048 34644 13150 -1128 577 6123 B C
ATOM 5049 C ASP A 25 -59.543 15.932 4.199 1.00156.17 B C
ANISOU 5049 C ASP A 25 10602 34810 13925 -1174 553 5786 B C
ATOM 5050 O ASP A 25 -59.535 14.754 4.566 1.00155.76 B O
ANISOU 5050 O ASP A 25 10426 35047 13708 -1445 557 5268 B O
ATOM 5051 CB ASP A 25 -58.398 15.906 1.955 1.00154.35 B C
ANISOU 5051 CB ASP A 25 10496 34908 13242 -1296 455 5560 B C
ATOM 5052 CG ASP A 25 -59.655 16.254 1.178 1.00163.71 B C
ANISOU 5052 CG ASP A 25 12210 35058 14934 -1126 325 5272 B C
ATOM 5053 OD1 ASP A 25 -59.767 17.412 0.717 1.00164.82 B O
ANISOU 5053 OD1 ASP A 25 12513 34866 15245 -884 317 5694 B O
ATOM 5054 OD2 ASP A 25 -60.544 15.384 1.070 1.00167.91 B O1-
ANISOU 5054 OD2 ASP A 25 12894 35272 15634 -1247 233 4698 B O1-
ATOM 5055 N PHE A 26 -60.501 16.798 4.516 1.00154.93 B N
ANISOU 5055 N PHE A 26 10356 34525 13984 -940 534 6278 B N
ATOM 5056 CA PHE A 26 -61.662 16.481 5.334 1.00155.32 B C
ANISOU 5056 CA PHE A 26 10278 34539 14199 -948 515 6206 B C
ATOM 5057 C PHE A 26 -62.754 15.732 4.566 1.00159.06 B C
ANISOU 5057 C PHE A 26 10877 34842 14719 -1095 359 5573 B C
ATOM 5058 O PHE A 26 -63.505 14.983 5.193 1.00159.13 B O
ANISOU 5058 O PHE A 26 10739 34966 14758 -1227 347 5293 B O
ATOM 5059 CB PHE A 26 -62.229 17.768 5.941 1.00156.43 B C
ANISOU 5059 CB PHE A 26 10512 34155 14770 -604 581 6829 B C
ATOM 5060 CG PHE A 26 -61.457 18.247 7.148 1.00156.69 B C
ANISOU 5060 CG PHE A 26 10595 33899 15039 -460 763 7234 B C
ATOM 5061 CD1 PHE A 26 -61.814 17.840 8.426 1.00158.55 B C
ANISOU 5061 CD1 PHE A 26 10821 33943 15478 -483 839 7142 B C
ATOM 5062 CD2 PHE A 26 -60.374 19.110 7.007 1.00157.65 B C
ANISOU 5062 CD2 PHE A 26 10936 33655 15308 -297 863 7568 B C
ATOM 5063 CE1 PHE A 26 -61.104 18.286 9.544 1.00158.27 B C
ANISOU 5063 CE1 PHE A 26 10815 33650 15672 -337 1007 7566 B C
ATOM 5064 CE2 PHE A 26 -59.659 19.549 8.127 1.00158.72 B C
ANISOU 5064 CE2 PHE A 26 11172 33394 15741 -157 1035 7902 B C
ATOM 5065 CZ PHE A 26 -60.028 19.130 9.388 1.00157.10 B C
ANISOU 5065 CZ PHE A 26 10759 33317 15613 -170 1105 8017 B C
ATOM 5066 N THR A 27 -62.852 15.925 3.231 1.00157.00 B N
ANISOU 5066 N THR A 27 10603 34798 14253 -1098 236 5570 B N
ATOM 5067 CA THR A 27 -63.850 15.247 2.397 1.00157.52 B C
ANISOU 5067 CA THR A 27 10641 34954 14256 -1238 76 5123 B C
ATOM 5068 C THR A 27 -63.521 13.743 2.343 1.00159.21 B C
ANISOU 5068 C THR A 27 10909 35220 14363 -1569 79 4350 B C
ATOM 5069 O THR A 27 -64.420 12.915 2.508 1.00159.29 B O
ANISOU 5069 O THR A 27 10795 35322 14405 -1727 24 3972 B O
ATOM 5070 CB THR A 27 -63.923 15.898 1.002 1.00165.42 B C
ANISOU 5070 CB THR A 27 12190 35125 15539 -1069 -30 4985 B C
ATOM 5071 CG2 THR A 27 -64.984 15.264 0.110 1.00165.88 B C
ANISOU 5071 CG2 THR A 27 12204 35268 15554 -1180 -206 4613 B C
ATOM 5072 OG1 THR A 27 -64.199 17.291 1.148 1.00165.95 B O
ANISOU 5072 OG1 THR A 27 12339 34882 15833 -771 -4 5562 B O
ATOM 5073 N SER A 28 -62.231 13.405 2.165 1.00155.41 B N
ANISOU 5073 N SER A 28 10333 35180 13536 -1721 149 4283 B N
ATOM 5074 CA SER A 28 -61.746 12.028 2.099 1.00154.55 B C
ANISOU 5074 CA SER A 28 10163 35339 13219 -2064 175 3611 B C
ATOM 5075 C SER A 28 -61.453 11.425 3.481 1.00154.94 B C
ANISOU 5075 C SER A 28 10150 35371 13349 -2195 316 3405 B C
ATOM 5076 O SER A 28 -61.395 10.195 3.595 1.00154.47 B O
ANISOU 5076 O SER A 28 10018 35479 13195 -2500 344 2777 B O
ATOM 5077 CB SER A 28 -60.489 11.953 1.241 1.00156.56 B C
ANISOU 5077 CB SER A 28 10698 35393 13393 -2095 203 3435 B C
ATOM 5078 OG SER A 28 -60.798 12.094 -0.135 1.00162.49 B O
ANISOU 5078 OG SER A 28 11901 35432 14406 -1969 81 3248 B O
ATOM 5079 N ARG A 29 -61.247 12.282 4.515 1.00150.91 B N
ANISOU 5079 N ARG A 29 9413 35142 12785 -2028 402 4057 B N
ATOM 5080 CA ARG A 29 -60.919 11.926 5.910 1.00149.62 B C
ANISOU 5080 CA ARG A 29 9101 35136 12612 -2124 534 4041 B C
ATOM 5081 C ARG A 29 -59.572 11.161 5.985 1.00150.00 B C
ANISOU 5081 C ARG A 29 9245 35256 12493 -2364 630 3571 B C
ATOM 5082 O ARG A 29 -59.437 10.207 6.757 1.00149.89 B O
ANISOU 5082 O ARG A 29 9145 35379 12427 -2625 710 3079 B O
ATOM 5083 CB ARG A 29 -62.056 11.124 6.587 1.00150.62 B C
ANISOU 5083 CB ARG A 29 9120 35230 12878 -2272 526 3653 B C
ATOM 5084 CG ARG A 29 -63.310 11.939 6.894 1.00159.64 B C
ANISOU 5084 CG ARG A 29 10682 35263 14713 -1906 488 3894 B C
ATOM 5085 CD ARG A 29 -64.525 11.050 7.098 1.00168.14 B C
ANISOU 5085 CD ARG A 29 12067 35526 16291 -1976 459 3247 B C
ATOM 5086 NE ARG A 29 -65.065 10.558 5.828 1.00175.44 B N
ANISOU 5086 NE ARG A 29 13404 35712 17543 -1986 332 2720 B N
ATOM 5087 CZ ARG A 29 -66.052 9.675 5.719 1.00186.19 B C
ANISOU 5087 CZ ARG A 29 15241 35943 19561 -1983 296 2114 B C
ATOM 5088 NH1 ARG A 29 -66.622 9.167 6.806 1.00178.60 B N1+
ANISOU 5088 NH1 ARG A 29 13698 35876 18287 -2192 361 2152 B N1+
ATOM 5089 NH2 ARG A 29 -66.477 9.291 4.523 1.00176.74 B N
ANISOU 5089 NH2 ARG A 29 13579 35722 17852 -2189 146 2049 B N
ATOM 5090 N ALA A 30 -58.573 11.604 5.199 1.00145.45 B N
ANISOU 5090 N ALA A 30 8576 35104 11584 -2347 623 3838 B N
ATOM 5091 CA ALA A 30 -57.249 10.980 5.164 1.00144.00 B C
ANISOU 5091 CA ALA A 30 8393 35174 11148 -2587 708 3454 B C
ATOM 5092 C ALA A 30 -56.115 12.014 5.189 1.00143.45 B C
ANISOU 5092 C ALA A 30 8427 34991 11084 -2351 776 4058 B C
ATOM 5093 O ALA A 30 -56.326 13.185 4.871 1.00142.70 B O
ANISOU 5093 O ALA A 30 8362 34753 11102 -2039 743 4738 B O
ATOM 5094 CB ALA A 30 -57.120 10.101 3.929 1.00144.99 B C
ANISOU 5094 CB ALA A 30 8641 35289 11159 -2810 644 2797 B C
ATOM 5095 N ILE A 31 -54.910 11.562 5.580 1.00139.40 B N
ANISOU 5095 N ILE A 31 7721 35008 10238 -2578 874 3894 B N
ATOM 5096 CA ILE A 31 -53.690 12.358 5.647 1.00137.95 B C
ANISOU 5096 CA ILE A 31 7553 34869 9992 -2417 951 4425 B C
ATOM 5097 C ILE A 31 -52.678 11.694 4.734 1.00138.00 B C
ANISOU 5097 C ILE A 31 7654 35032 9749 -2665 965 3856 B C
ATOM 5098 O ILE A 31 -52.222 10.578 5.004 1.00137.68 B O
ANISOU 5098 O ILE A 31 7573 35180 9558 -3015 1025 3127 B O
ATOM 5099 CB ILE A 31 -53.124 12.597 7.088 1.00139.42 B C
ANISOU 5099 CB ILE A 31 7771 34816 10385 -2324 1076 4710 B C
ATOM 5100 CG1 ILE A 31 -54.196 13.179 8.036 1.00139.62 B C
ANISOU 5100 CG1 ILE A 31 7716 34626 10707 -2077 1077 5247 B C
ATOM 5101 CG2 ILE A 31 -51.869 13.513 7.030 1.00139.67 B C
ANISOU 5101 CG2 ILE A 31 7923 34646 10498 -2097 1159 5285 B C
ATOM 5102 CD1 ILE A 31 -53.720 13.481 9.496 1.00145.55 B C
ANISOU 5102 CD1 ILE A 31 8731 34663 11911 -1904 1210 5469 B C
ATOM 5103 N ALA A 32 -52.374 12.360 3.627 1.00133.98 B N
ANISOU 5103 N ALA A 32 7029 34897 8981 -2559 910 4265 B N
ATOM 5104 CA ALA A 32 -51.380 11.884 2.677 1.00132.73 B C
ANISOU 5104 CA ALA A 32 6914 34977 8542 -2765 925 3848 B C
ATOM 5105 C ALA A 32 -50.051 12.465 3.108 1.00132.99 B C
ANISOU 5105 C ALA A 32 6979 34980 8570 -2658 1039 4246 B C
ATOM 5106 O ALA A 32 -49.905 13.691 3.170 1.00131.82 B O
ANISOU 5106 O ALA A 32 6817 34717 8553 -2318 1059 5100 B O
ATOM 5107 CB ALA A 32 -51.753 12.299 1.264 1.00133.72 B C
ANISOU 5107 CB ALA A 32 7196 34939 8671 -2627 819 3963 B C
ATOM 5108 N ALA A 33 -49.126 11.593 3.534 1.00130.06 B N
ANISOU 5108 N ALA A 33 6404 35145 7870 -3012 1121 3736 B N
ATOM 5109 CA ALA A 33 -47.846 12.050 4.053 1.00129.38 B C
ANISOU 5109 CA ALA A 33 6296 35117 7746 -2946 1226 4092 B C
ATOM 5110 C ALA A 33 -46.672 11.672 3.173 1.00131.60 B C
ANISOU 5110 C ALA A 33 6772 35320 7909 -3104 1274 3631 B C
ATOM 5111 O ALA A 33 -46.546 10.531 2.721 1.00130.96 B O
ANISOU 5111 O ALA A 33 6690 35420 7650 -3465 1282 2759 B O
ATOM 5112 CB ALA A 33 -47.626 11.510 5.453 1.00129.30 B C
ANISOU 5112 CB ALA A 33 6187 35177 7762 -3124 1308 3837 B C
ATOM 5113 N SER A 34 -45.807 12.661 2.952 1.00129.38 B N
ANISOU 5113 N SER A 34 6401 35227 7532 -2890 1315 4357 B N
ATOM 5114 CA SER A 34 -44.550 12.548 2.240 1.00129.15 B C
ANISOU 5114 CA SER A 34 6452 35297 7323 -3003 1375 4145 B C
ATOM 5115 C SER A 34 -43.484 12.684 3.317 1.00131.84 B C
ANISOU 5115 C SER A 34 6844 35439 7809 -2982 1492 4286 B C
ATOM 5116 O SER A 34 -43.141 13.803 3.705 1.00131.55 B O
ANISOU 5116 O SER A 34 6787 35228 7967 -2638 1537 5184 B O
ATOM 5117 CB SER A 34 -44.456 13.623 1.161 1.00131.87 B C
ANISOU 5117 CB SER A 34 7063 35175 7866 -2653 1353 4712 B C
ATOM 5118 OG SER A 34 -43.405 13.350 0.251 1.00136.99 B O
ANISOU 5118 OG SER A 34 8147 35256 8648 -2699 1414 4252 B O
ATOM 5119 N THR A 35 -43.068 11.552 3.905 1.00129.50 B N
ANISOU 5119 N THR A 35 6356 35616 7231 -3424 1542 3504 B N
ATOM 5120 CA THR A 35 -42.110 11.557 5.016 1.00129.17 B C
ANISOU 5120 CA THR A 35 6244 35637 7197 -3498 1638 3570 B C
ATOM 5121 C THR A 35 -40.677 11.310 4.519 1.00131.99 B C
ANISOU 5121 C THR A 35 6820 35787 7545 -3625 1728 3181 B C
ATOM 5122 O THR A 35 -40.428 10.345 3.796 1.00131.98 B O
ANISOU 5122 O THR A 35 6889 35863 7393 -3957 1755 2296 B O
ATOM 5123 CB THR A 35 -42.503 10.526 6.094 1.00135.69 B C
ANISOU 5123 CB THR A 35 7350 35848 8360 -3727 1686 2702 B C
ATOM 5124 CG2 THR A 35 -41.669 10.657 7.354 1.00135.86 B C
ANISOU 5124 CG2 THR A 35 7318 35871 8433 -3751 1767 2893 B C
ATOM 5125 OG1 THR A 35 -43.903 10.593 6.416 1.00133.39 B O
ANISOU 5125 OG1 THR A 35 6897 35699 8087 -3653 1604 2894 B O
ATOM 5126 N SER A 36 -39.744 12.192 4.920 1.00129.13 B N
ANISOU 5126 N SER A 36 6284 35656 7124 -3429 1778 3981 B N
ATOM 5127 CA SER A 36 -38.316 12.104 4.603 1.00128.51 B C
ANISOU 5127 CA SER A 36 6236 35685 6906 -3567 1863 3791 B C
ATOM 5128 C SER A 36 -37.595 11.709 5.886 1.00130.07 B C
ANISOU 5128 C SER A 36 6458 35766 7196 -3754 1941 3492 B C
ATOM 5129 O SER A 36 -37.480 12.524 6.805 1.00129.42 B O
ANISOU 5129 O SER A 36 6276 35592 7304 -3449 1949 4383 B O
ATOM 5130 CB SER A 36 -37.800 13.429 4.045 1.00130.59 B C
ANISOU 5130 CB SER A 36 6662 35507 7450 -3079 1890 4795 B C
ATOM 5131 OG SER A 36 -38.677 13.962 3.067 1.00136.17 B O
ANISOU 5131 OG SER A 36 7733 35531 8475 -2790 1832 4948 B O
ATOM 5132 N LEU A 37 -37.190 10.442 5.985 1.00127.02 B N
ANISOU 5132 N LEU A 37 5945 35843 6474 -4361 2010 2292 B N
ATOM 5133 CA LEU A 37 -36.548 9.916 7.187 1.00125.98 B C
ANISOU 5133 CA LEU A 37 5741 35839 6288 -4723 2105 1752 B C
ATOM 5134 C LEU A 37 -35.020 9.836 7.023 1.00127.10 B C
ANISOU 5134 C LEU A 37 6015 35847 6428 -4880 2211 1448 B C
ATOM 5135 O LEU A 37 -34.527 9.310 6.023 1.00126.44 B O
ANISOU 5135 O LEU A 37 5991 35827 6223 -5108 2273 803 B O
ATOM 5136 CB LEU A 37 -37.122 8.524 7.553 1.00125.72 B C
ANISOU 5136 CB LEU A 37 5750 35753 6264 -5267 2198 385 B C
ATOM 5137 CG LEU A 37 -38.654 8.395 7.718 1.00129.31 B C
ANISOU 5137 CG LEU A 37 6313 35841 6976 -5073 2110 476 B C
ATOM 5138 CD1 LEU A 37 -39.326 7.975 6.414 1.00130.02 B C
ANISOU 5138 CD1 LEU A 37 6488 35832 7081 -5061 2060 152 B C
ATOM 5139 CD2 LEU A 37 -38.995 7.359 8.736 1.00130.18 B C
ANISOU 5139 CD2 LEU A 37 6506 35680 7276 -5479 2238 -517 B C
ATOM 5140 N THR A 38 -34.286 10.378 8.009 1.00123.98 B N
ANISOU 5140 N THR A 38 5399 35790 5917 -4865 2225 2003 B N
ATOM 5141 CA THR A 38 -32.831 10.308 8.087 1.00123.48 B C
ANISOU 5141 CA THR A 38 5373 35759 5783 -5090 2326 1712 B C
ATOM 5142 C THR A 38 -32.522 9.048 8.881 1.00125.42 B C
ANISOU 5142 C THR A 38 5892 35545 6215 -5715 2504 167 B C
ATOM 5143 O THR A 38 -32.808 8.980 10.083 1.00118.11 B O
ANISOU 5143 O THR A 38 5701 32973 6202 -5371 2512 147 B O
ATOM 5144 CB THR A 38 -32.254 11.585 8.691 1.00129.85 B C
ANISOU 5144 CB THR A 38 6335 35959 7042 -4436 2279 3130 B C
ATOM 5145 CG2 THR A 38 -30.724 11.556 8.787 1.00123.22 B C
ANISOU 5145 CG2 THR A 38 5947 34296 6576 -4449 2384 2807 B C
ATOM 5146 OG1 THR A 38 -32.664 12.698 7.899 1.00129.09 B O
ANISOU 5146 OG1 THR A 38 6178 35759 7112 -3825 2219 4351 B O
ATOM 5147 N VAL A 39 -31.986 8.035 8.193 1.00122.79 B N
ANISOU 5147 N VAL A 39 5606 35244 5806 -6238 2682 -1117 B N
ATOM 5148 CA VAL A 39 -31.710 6.729 8.782 1.00122.06 B C
ANISOU 5148 CA VAL A 39 5743 34590 6046 -6881 2974 -2739 B C
ATOM 5149 C VAL A 39 -30.209 6.565 9.064 1.00121.07 B C
ANISOU 5149 C VAL A 39 6296 33052 6653 -6792 3127 -3117 B C
ATOM 5150 O VAL A 39 -29.392 6.719 8.159 1.00124.92 B O
ANISOU 5150 O VAL A 39 6439 34386 6641 -7002 3158 -3144 B O
ATOM 5151 CB VAL A 39 -32.268 5.593 7.873 1.00125.24 B C
ANISOU 5151 CB VAL A 39 6344 34462 6781 -6991 3073 -3643 B C
ATOM 5152 CG1 VAL A 39 -31.943 4.209 8.429 1.00124.32 B C
ANISOU 5152 CG1 VAL A 39 6441 33582 7212 -7582 3457 -5227 B C
ATOM 5153 CG2 VAL A 39 -33.775 5.749 7.677 1.00125.58 B C
ANISOU 5153 CG2 VAL A 39 6254 34750 6712 -6709 2881 -3120 B C
ATOM 5154 N ARG A 40 -29.860 6.242 10.325 1.00109.29 B N
ANISOU 5154 N ARG A 40 5727 29480 6318 -6484 3224 -3385 B N
ATOM 5155 CA ARG A 40 -28.480 5.990 10.736 1.00103.44 B C
ANISOU 5155 CA ARG A 40 5649 27292 6359 -6385 3380 -3763 B C
ATOM 5156 C ARG A 40 -28.304 4.498 10.992 1.00108.40 B C
ANISOU 5156 C ARG A 40 6430 27235 7523 -6945 3778 -5296 B C
ATOM 5157 O ARG A 40 -28.958 3.949 11.886 1.00104.67 B O
ANISOU 5157 O ARG A 40 6275 25854 7641 -6886 3874 -5612 B O
ATOM 5158 CB ARG A 40 -28.086 6.818 11.975 1.00 93.05 B C
ANISOU 5158 CB ARG A 40 5191 24210 5954 -5585 3214 -2800 B C
ATOM 5159 CG ARG A 40 -26.617 6.631 12.376 1.00 93.59 B C
ANISOU 5159 CG ARG A 40 5890 22907 6764 -5466 3348 -3111 B C
ATOM 5160 CD ARG A 40 -25.972 7.923 12.835 1.00 88.07 B C
ANISOU 5160 CD ARG A 40 5615 21431 6415 -4781 3142 -1930 B C
ATOM 5161 NE ARG A 40 -25.907 8.033 14.290 1.00 87.53 B N
ANISOU 5161 NE ARG A 40 6318 19649 7289 -4316 3117 -1735 B N
ATOM 5162 CZ ARG A 40 -26.090 9.160 14.971 1.00 93.06 B C
ANISOU 5162 CZ ARG A 40 7297 19753 8309 -3725 2949 -717 B C
ATOM 5163 NH1 ARG A 40 -26.387 10.287 14.336 1.00 70.06 B N1+
ANISOU 5163 NH1 ARG A 40 3953 17713 4953 -3475 2821 292 B N1+
ATOM 5164 NH2 ARG A 40 -26.001 9.164 16.292 1.00 84.23 B N
ANISOU 5164 NH2 ARG A 40 6826 17198 7978 -3390 2950 -695 B N
ATOM 5165 N SER A 41 -27.426 3.847 10.202 1.00109.68 B N
ANISOU 5165 N SER A 41 6327 27812 7535 -7484 4055 -6225 B N
ATOM 5166 CA SER A 41 -27.125 2.422 10.317 1.00111.54 B C
ANISOU 5166 CA SER A 41 6603 27386 8392 -8055 4552 -7713 B C
ATOM 5167 C SER A 41 -26.276 2.150 11.564 1.00111.33 B C
ANISOU 5167 C SER A 41 7493 25160 9649 -7603 4675 -7653 B C
ATOM 5168 O SER A 41 -25.291 2.847 11.811 1.00105.43 B O
ANISOU 5168 O SER A 41 7197 23715 9148 -7152 4499 -6957 B O
ATOM 5169 CB SER A 41 -26.428 1.921 9.059 1.00120.92 B C
ANISOU 5169 CB SER A 41 7178 29732 9035 -8758 4836 -8666 B C
ATOM 5170 OG SER A 41 -25.962 0.587 9.185 1.00125.35 B O
ANISOU 5170 OG SER A 41 8035 28989 10605 -8960 5267 -9716 B O
ATOM 5171 N LEU A 42 -26.694 1.155 12.366 1.00110.56 B N
ANISOU 5171 N LEU A 42 7617 24033 10356 -7716 4987 -8333 B N
ATOM 5172 CA LEU A 42 -26.016 0.738 13.599 1.00104.97 B C
ANISOU 5172 CA LEU A 42 7658 21366 10859 -7326 5154 -8293 B C
ATOM 5173 C LEU A 42 -25.274 -0.591 13.371 1.00115.32 B C
ANISOU 5173 C LEU A 42 8823 22113 12881 -7873 5781 -9568 B C
ATOM 5174 O LEU A 42 -24.434 -0.981 14.185 1.00110.26 B O
ANISOU 5174 O LEU A 42 8690 19980 13224 -7597 5978 -9537 B O
ATOM 5175 CB LEU A 42 -27.042 0.622 14.749 1.00101.02 B C
ANISOU 5175 CB LEU A 42 7485 20068 10830 -6983 5081 -7966 B C
ATOM 5176 CG LEU A 42 -27.197 1.830 15.683 1.00 98.67 B C
ANISOU 5176 CG LEU A 42 7756 19161 10573 -6192 4587 -6625 B C
ATOM 5177 CD1 LEU A 42 -27.758 3.056 14.959 1.00101.07 B C
ANISOU 5177 CD1 LEU A 42 7707 20833 9861 -6047 4164 -5782 B C
ATOM 5178 CD2 LEU A 42 -28.111 1.493 16.845 1.00 97.80 B C
ANISOU 5178 CD2 LEU A 42 7967 18143 11049 -5935 4618 -6514 B C
ATOM 5179 N GLN A 43 -25.546 -1.237 12.221 1.00122.98 B N
ANISOU 5179 N GLN A 43 9035 24362 13331 -8658 6114 -10664 B N
ATOM 5180 CA GLN A 43 -24.954 -2.504 11.798 1.00127.79 B C
ANISOU 5180 CA GLN A 43 9397 24560 14597 -9202 6737 -11896 B C
ATOM 5181 C GLN A 43 -23.968 -2.271 10.659 1.00131.62 B C
ANISOU 5181 C GLN A 43 9918 25429 14662 -8999 6419 -11471 B C
ATOM 5182 O GLN A 43 -24.168 -1.382 9.826 1.00132.00 B O
ANISOU 5182 O GLN A 43 9714 26789 13649 -8924 5985 -10883 B O
ATOM 5183 CB GLN A 43 -26.052 -3.499 11.380 1.00129.01 B C
ANISOU 5183 CB GLN A 43 9451 24703 14864 -9058 6602 -11905 B C
ATOM 5184 CG GLN A 43 -25.691 -4.951 11.671 1.00142.29 B C
ANISOU 5184 CG GLN A 43 11772 24482 17809 -8367 6520 -11443 B C
ATOM 5185 CD GLN A 43 -26.896 -5.857 11.653 1.00159.63 B C
ANISOU 5185 CD GLN A 43 14412 25984 20257 -7541 5911 -10373 B C
ATOM 5186 NE2 GLN A 43 -27.543 -6.010 12.802 1.00154.66 B N
ANISOU 5186 NE2 GLN A 43 13733 24908 20124 -7749 6297 -10805 B N
ATOM 5187 OE1 GLN A 43 -27.248 -6.446 10.624 1.00158.16 B O
ANISOU 5187 OE1 GLN A 43 14042 26245 19805 -7583 5783 -10437 B O
ATOM 5188 N ASP A 44 -22.906 -3.087 10.636 1.00129.32 B N
ANISOU 5188 N ASP A 44 9778 24148 15209 -9103 6810 -12010 B N
ATOM 5189 CA ASP A 44 -21.815 -3.034 9.676 1.00130.12 B C
ANISOU 5189 CA ASP A 44 9882 24461 15097 -9061 6695 -11905 B C
ATOM 5190 C ASP A 44 -22.252 -3.160 8.206 1.00134.87 B C
ANISOU 5190 C ASP A 44 10369 25922 14955 -8726 6133 -11270 B C
ATOM 5191 O ASP A 44 -21.671 -2.477 7.358 1.00136.01 B O
ANISOU 5191 O ASP A 44 10427 26789 14460 -8648 5884 -10878 B O
ATOM 5192 CB ASP A 44 -20.776 -4.115 9.995 1.00130.21 B C
ANISOU 5192 CB ASP A 44 10175 22986 16312 -9017 7113 -12326 B C
ATOM 5193 CG ASP A 44 -19.405 -3.550 10.296 1.00136.28 B C
ANISOU 5193 CG ASP A 44 11320 23089 17372 -8772 7088 -11954 B C
ATOM 5194 OD1 ASP A 44 -18.961 -2.650 9.555 1.00137.51 B O
ANISOU 5194 OD1 ASP A 44 11376 24159 16711 -8767 6787 -11621 B O
ATOM 5195 OD2 ASP A 44 -18.776 -4.008 11.272 1.00139.63 B O1-
ANISOU 5195 OD2 ASP A 44 12123 22071 18860 -8554 7372 -11932 B O1-
ATOM 5196 N SER A 45 -23.235 -4.028 7.900 1.00132.31 B N
ANISOU 5196 N SER A 45 9893 25659 14718 -8767 6138 -11493 B N
ATOM 5197 CA SER A 45 -23.699 -4.226 6.524 1.00133.08 B C
ANISOU 5197 CA SER A 45 9816 26537 14211 -8620 5792 -11165 B C
ATOM 5198 C SER A 45 -25.223 -4.419 6.472 1.00136.12 B C
ANISOU 5198 C SER A 45 10172 27135 14411 -8396 5528 -10803 B C
ATOM 5199 O SER A 45 -25.720 -5.552 6.488 1.00135.27 B O
ANISOU 5199 O SER A 45 10105 26413 14878 -8444 5700 -11179 B O
ATOM 5200 CB SER A 45 -22.974 -5.404 5.876 1.00135.02 B C
ANISOU 5200 CB SER A 45 10245 26008 15048 -8514 5877 -11355 B C
ATOM 5201 OG SER A 45 -23.224 -6.610 6.579 1.00140.29 B O
ANISOU 5201 OG SER A 45 11262 25343 16699 -8258 5975 -11350 B O
ATOM 5202 N LEU A 46 -25.959 -3.296 6.404 1.00134.61 B N
ANISOU 5202 N LEU A 46 9725 28086 13334 -8369 5247 -10324 B N
ATOM 5203 CA LEU A 46 -27.416 -3.287 6.352 1.00134.98 B C
ANISOU 5203 CA LEU A 46 9637 28556 13094 -8260 5046 -10061 B C
ATOM 5204 C LEU A 46 -27.937 -3.357 4.925 1.00138.52 B C
ANISOU 5204 C LEU A 46 10070 29448 13114 -7925 4675 -9476 B C
ATOM 5205 O LEU A 46 -27.567 -2.535 4.085 1.00138.91 B O
ANISOU 5205 O LEU A 46 10030 30178 12570 -7776 4457 -8957 B O
ATOM 5206 CB LEU A 46 -27.977 -2.038 7.039 1.00135.67 B C
ANISOU 5206 CB LEU A 46 9619 29275 12655 -8185 4864 -9539 B C
ATOM 5207 CG LEU A 46 -28.542 -2.221 8.437 1.00138.44 B C
ANISOU 5207 CG LEU A 46 10183 28819 13598 -8181 5032 -9729 B C
ATOM 5208 CD1 LEU A 46 -28.959 -0.897 9.000 1.00139.46 B C
ANISOU 5208 CD1 LEU A 46 10217 29625 13148 -8094 4828 -9129 B C
ATOM 5209 CD2 LEU A 46 -29.755 -3.154 8.439 1.00140.06 B C
ANISOU 5209 CD2 LEU A 46 10415 28665 14135 -8086 5013 -9841 B C
ATOM 5210 N ALA A 47 -28.819 -4.331 4.664 1.00135.99 B N
ANISOU 5210 N ALA A 47 9655 29015 13001 -8035 4743 -9844 B N
ATOM 5211 CA ALA A 47 -29.434 -4.516 3.356 1.00136.47 B C
ANISOU 5211 CA ALA A 47 9630 29524 12697 -7875 4502 -9547 B C
ATOM 5212 C ALA A 47 -30.922 -4.161 3.381 1.00139.96 B C
ANISOU 5212 C ALA A 47 10070 30194 12914 -7605 4226 -9002 B C
ATOM 5213 O ALA A 47 -31.435 -3.674 2.377 1.00140.93 B O
ANISOU 5213 O ALA A 47 10116 30858 12573 -7404 3968 -8517 B O
ATOM 5214 CB ALA A 47 -29.249 -5.951 2.890 1.00136.20 B C
ANISOU 5214 CB ALA A 47 9712 28783 13255 -7966 4679 -10064 B C
ATOM 5215 N SER A 48 -31.615 -4.411 4.513 1.00136.79 B N
ANISOU 5215 N SER A 48 9565 29676 12734 -7824 4404 -9375 B N
ATOM 5216 CA SER A 48 -33.057 -4.169 4.651 1.00136.94 B C
ANISOU 5216 CA SER A 48 9454 30071 12506 -7730 4232 -9086 B C
ATOM 5217 C SER A 48 -33.389 -3.087 5.688 1.00139.04 B C
ANISOU 5217 C SER A 48 9723 30568 12537 -7589 4116 -8598 B C
ATOM 5218 O SER A 48 -32.582 -2.805 6.571 1.00138.20 B O
ANISOU 5218 O SER A 48 9666 30282 12563 -7730 4290 -8791 B O
ATOM 5219 CB SER A 48 -33.777 -5.459 5.029 1.00139.15 B C
ANISOU 5219 CB SER A 48 9899 29470 13500 -7746 4380 -9486 B C
ATOM 5220 OG SER A 48 -33.341 -6.578 4.272 1.00145.13 B O
ANISOU 5220 OG SER A 48 10987 29416 14740 -7493 4310 -9401 B O
ATOM 5221 N LEU A 49 -34.598 -2.504 5.581 1.00137.19 B N
ANISOU 5221 N LEU A 49 9250 31055 11820 -7517 3913 -8202 B N
ATOM 5222 CA LEU A 49 -35.118 -1.462 6.470 1.00137.29 B C
ANISOU 5222 CA LEU A 49 9149 31528 11488 -7427 3792 -7713 B C
ATOM 5223 C LEU A 49 -36.565 -1.788 6.870 1.00140.32 B C
ANISOU 5223 C LEU A 49 9579 31663 12074 -7278 3698 -7577 B C
ATOM 5224 O LEU A 49 -37.464 -1.695 6.030 1.00140.66 B O
ANISOU 5224 O LEU A 49 9519 32090 11834 -7104 3480 -7195 B O
ATOM 5225 CB LEU A 49 -35.032 -0.099 5.757 1.00138.19 B C
ANISOU 5225 CB LEU A 49 9143 32459 10905 -7106 3471 -6729 B C
ATOM 5226 CG LEU A 49 -34.450 1.068 6.549 1.00141.46 B C
ANISOU 5226 CG LEU A 49 9639 32950 11159 -6900 3381 -6087 B C
ATOM 5227 CD1 LEU A 49 -32.937 0.941 6.705 1.00140.71 B C
ANISOU 5227 CD1 LEU A 49 9660 32565 11238 -7099 3583 -6494 B C
ATOM 5228 CD2 LEU A 49 -34.782 2.381 5.883 1.00144.44 B C
ANISOU 5228 CD2 LEU A 49 9967 33853 11059 -6419 3049 -4897 B C
ATOM 5229 N ILE A 50 -36.779 -2.196 8.144 1.00137.61 B N
ANISOU 5229 N ILE A 50 9203 30996 12087 -7568 3971 -8169 B N
ATOM 5230 CA ILE A 50 -38.096 -2.585 8.694 1.00137.65 B C
ANISOU 5230 CA ILE A 50 9152 30882 12268 -7581 3983 -8271 B C
ATOM 5231 C ILE A 50 -38.738 -1.459 9.523 1.00140.51 B C
ANISOU 5231 C ILE A 50 9489 31592 12307 -7343 3776 -7554 B C
ATOM 5232 O ILE A 50 -38.196 -1.043 10.550 1.00139.80 B O
ANISOU 5232 O ILE A 50 9432 31410 12275 -7475 3923 -7678 B O
ATOM 5233 CB ILE A 50 -38.041 -3.907 9.517 1.00138.88 B C
ANISOU 5233 CB ILE A 50 9557 29851 13358 -7748 4349 -9047 B C
ATOM 5234 CG1 ILE A 50 -36.778 -3.974 10.427 1.00138.53 B C
ANISOU 5234 CG1 ILE A 50 9706 29137 13790 -7922 4676 -9496 B C
ATOM 5235 CG2 ILE A 50 -38.144 -5.115 8.578 1.00139.07 B C
ANISOU 5235 CG2 ILE A 50 9647 29455 13738 -7759 4397 -9360 B C
ATOM 5236 CD1 ILE A 50 -36.727 -5.097 11.475 1.00142.77 B C
ANISOU 5236 CD1 ILE A 50 10616 28228 15404 -7878 5001 -9918 B C
ATOM 5237 N LEU A 51 -39.911 -0.990 9.075 1.00139.07 B N
ANISOU 5237 N LEU A 51 9060 32132 11648 -7193 3519 -7027 B N
ATOM 5238 CA LEU A 51 -40.677 0.059 9.753 1.00139.73 B C
ANISOU 5238 CA LEU A 51 9004 32729 11359 -6996 3324 -6316 B C
ATOM 5239 C LEU A 51 -42.089 -0.415 10.087 1.00143.04 B C
ANISOU 5239 C LEU A 51 9506 32741 12099 -6859 3274 -6295 B C
ATOM 5240 O LEU A 51 -42.621 -1.293 9.403 1.00142.71 B O
ANISOU 5240 O LEU A 51 9474 32480 12269 -6915 3297 -6636 B O
ATOM 5241 CB LEU A 51 -40.760 1.336 8.896 1.00140.62 B C
ANISOU 5241 CB LEU A 51 8985 33574 10869 -6602 2976 -5217 B C
ATOM 5242 CG LEU A 51 -39.460 2.035 8.519 1.00143.62 B C
ANISOU 5242 CG LEU A 51 9540 33873 11157 -6399 2914 -4773 B C
ATOM 5243 CD1 LEU A 51 -39.722 3.100 7.493 1.00144.42 B C
ANISOU 5243 CD1 LEU A 51 9561 34457 10857 -5993 2635 -3787 B C
ATOM 5244 CD2 LEU A 51 -38.771 2.640 9.736 1.00145.14 B C
ANISOU 5244 CD2 LEU A 51 9803 33978 11364 -6392 2970 -4558 B C
ATOM 5245 N ASP A 52 -42.710 0.203 11.107 1.00141.47 B N
ANISOU 5245 N ASP A 52 9145 32905 11703 -6868 3248 -6037 B N
ATOM 5246 CA ASP A 52 -44.070 -0.109 11.550 1.00141.71 B C
ANISOU 5246 CA ASP A 52 9107 32858 11878 -6852 3234 -6082 B C
ATOM 5247 C ASP A 52 -45.131 0.692 10.786 1.00146.09 B C
ANISOU 5247 C ASP A 52 9653 33683 12173 -6351 2851 -5039 B C
ATOM 5248 O ASP A 52 -44.979 1.901 10.607 1.00145.81 B O
ANISOU 5248 O ASP A 52 9496 34205 11699 -6083 2643 -4175 B O
ATOM 5249 CB ASP A 52 -44.220 0.165 13.057 1.00142.55 B C
ANISOU 5249 CB ASP A 52 9270 32738 12153 -6920 3366 -6149 B C
ATOM 5250 CG ASP A 52 -43.405 -0.710 13.987 1.00146.82 B C
ANISOU 5250 CG ASP A 52 10289 31934 13562 -7026 3707 -6868 B C
ATOM 5251 OD1 ASP A 52 -43.099 -0.257 15.094 1.00146.94 B O
ANISOU 5251 OD1 ASP A 52 10369 31819 13643 -7109 3832 -6910 B O
ATOM 5252 OD2 ASP A 52 -43.159 -1.889 13.644 1.00149.46 B O1-
ANISOU 5252 OD2 ASP A 52 10913 31340 14537 -7023 3862 -7358 B O1-
ATOM 5253 N THR A 53 -46.206 0.001 10.341 1.00145.08 B N
ANISOU 5253 N THR A 53 9441 33518 12163 -6410 2836 -5297 B N
ATOM 5254 CA THR A 53 -47.381 0.565 9.650 1.00146.22 B C
ANISOU 5254 CA THR A 53 9479 34000 12078 -6102 2560 -4596 B C
ATOM 5255 C THR A 53 -48.644 -0.123 10.160 1.00149.73 B C
ANISOU 5255 C THR A 53 10045 33872 12974 -6066 2591 -4805 B C
ATOM 5256 O THR A 53 -48.582 -1.292 10.540 1.00149.05 B O
ANISOU 5256 O THR A 53 10039 33288 13304 -6355 2835 -5617 B O
ATOM 5257 CB THR A 53 -47.306 0.446 8.102 1.00153.44 B C
ANISOU 5257 CB THR A 53 10740 34351 13207 -5749 2371 -4261 B C
ATOM 5258 CG2 THR A 53 -46.053 1.070 7.493 1.00153.19 B C
ANISOU 5258 CG2 THR A 53 10749 34548 12907 -5652 2324 -3949 B C
ATOM 5259 OG1 THR A 53 -47.461 -0.916 7.694 1.00153.42 B O
ANISOU 5259 OG1 THR A 53 10823 33914 13558 -5986 2510 -5014 B O
ATOM 5260 N LYS A 54 -49.785 0.582 10.147 1.00148.49 B N
ANISOU 5260 N LYS A 54 9674 34198 12546 -5883 2402 -4221 B N
ATOM 5261 CA LYS A 54 -51.083 0.038 10.557 1.00148.75 B C
ANISOU 5261 CA LYS A 54 9652 34056 12812 -5933 2425 -4425 B C
ATOM 5262 C LYS A 54 -52.170 0.727 9.741 1.00152.25 B C
ANISOU 5262 C LYS A 54 10140 34504 13205 -5514 2131 -3621 B C
ATOM 5263 O LYS A 54 -52.372 1.932 9.897 1.00152.12 B O
ANISOU 5263 O LYS A 54 10018 34862 12919 -5244 1980 -2840 B O
ATOM 5264 CB LYS A 54 -51.312 0.206 12.076 1.00150.46 B C
ANISOU 5264 CB LYS A 54 9912 34040 13216 -5948 2544 -4445 B C
ATOM 5265 CG LYS A 54 -52.416 -0.691 12.633 1.00160.56 B C
ANISOU 5265 CG LYS A 54 11612 34098 15297 -5735 2577 -4567 B C
ATOM 5266 CD LYS A 54 -52.859 -0.288 14.035 1.00166.35 B C
ANISOU 5266 CD LYS A 54 12549 34336 16322 -5508 2593 -4227 B C
ATOM 5267 CE LYS A 54 -54.036 -1.116 14.493 1.00172.71 B C
ANISOU 5267 CE LYS A 54 13624 34247 17752 -5360 2621 -4329 B C
ATOM 5268 NZ LYS A 54 -54.598 -0.637 15.780 1.00177.67 B N1+
ANISOU 5268 NZ LYS A 54 14433 34440 18633 -5124 2623 -3958 B N1+
ATOM 5269 N ASP A 55 -52.823 -0.022 8.825 1.00150.44 B N
ANISOU 5269 N ASP A 55 9845 34292 13025 -5626 2095 -3939 B N
ATOM 5270 CA ASP A 55 -53.885 0.459 7.926 1.00151.38 B C
ANISOU 5270 CA ASP A 55 9911 34570 13037 -5374 1859 -3410 B C
ATOM 5271 C ASP A 55 -53.395 1.663 7.091 1.00155.36 B C
ANISOU 5271 C ASP A 55 10614 35001 13415 -4961 1663 -2603 B C
ATOM 5272 O ASP A 55 -54.142 2.613 6.846 1.00155.47 B O
ANISOU 5272 O ASP A 55 10548 35229 13296 -4694 1495 -1950 B O
ATOM 5273 CB ASP A 55 -55.177 0.798 8.707 1.00152.97 B C
ANISOU 5273 CB ASP A 55 10040 34719 13362 -5225 1796 -3084 B C
ATOM 5274 CG ASP A 55 -55.722 -0.337 9.554 1.00157.66 B C
ANISOU 5274 CG ASP A 55 10905 34408 14591 -5296 1949 -3600 B C
ATOM 5275 OD1 ASP A 55 -55.923 -1.444 9.007 1.00157.62 B O
ANISOU 5275 OD1 ASP A 55 10963 34103 14823 -5465 2008 -4115 B O
ATOM 5276 OD2 ASP A 55 -55.976 -0.110 10.755 1.00160.80 B O1-
ANISOU 5276 OD2 ASP A 55 11422 34450 15226 -5185 2012 -3453 B O1-
ATOM 5277 N LEU A 56 -52.119 1.599 6.672 1.00153.76 B N
ANISOU 5277 N LEU A 56 10440 34941 13040 -5076 1732 -2789 B N
ATOM 5278 CA LEU A 56 -51.424 2.592 5.858 1.00154.32 B C
ANISOU 5278 CA LEU A 56 10575 35190 12868 -4831 1613 -2210 B C
ATOM 5279 C LEU A 56 -51.241 2.085 4.445 1.00158.42 B C
ANISOU 5279 C LEU A 56 11390 35215 13586 -4748 1543 -2373 B C
ATOM 5280 O LEU A 56 -50.967 0.898 4.245 1.00157.71 B O
ANISOU 5280 O LEU A 56 11341 34928 13655 -5014 1657 -3056 B O
ATOM 5281 CB LEU A 56 -50.034 2.887 6.451 1.00153.77 B C
ANISOU 5281 CB LEU A 56 10542 35190 12692 -4890 1734 -2216 B C
ATOM 5282 CG LEU A 56 -49.798 4.160 7.267 1.00157.05 B C
ANISOU 5282 CG LEU A 56 11050 35502 13118 -4546 1682 -1412 B C
ATOM 5283 CD1 LEU A 56 -48.319 4.333 7.515 1.00156.38 B C
ANISOU 5283 CD1 LEU A 56 11020 35470 12927 -4627 1788 -1481 B C
ATOM 5284 CD2 LEU A 56 -50.301 5.405 6.552 1.00159.62 B C
ANISOU 5284 CD2 LEU A 56 11466 35760 13422 -4111 1497 -534 B C
ATOM 5285 N THR A 57 -51.340 2.987 3.469 1.00157.63 B N
ANISOU 5285 N THR A 57 11259 35400 13234 -4530 1387 -1828 B N
ATOM 5286 CA THR A 57 -51.113 2.651 2.071 1.00158.34 B C
ANISOU 5286 CA THR A 57 11485 35374 13303 -4523 1320 -1968 B C
ATOM 5287 C THR A 57 -49.806 3.328 1.661 1.00161.93 B C
ANISOU 5287 C THR A 57 12212 35553 13760 -4317 1335 -1650 B C
ATOM 5288 O THR A 57 -49.703 4.553 1.735 1.00161.77 B O
ANISOU 5288 O THR A 57 12165 35718 13582 -4076 1273 -999 B O
ATOM 5289 CB THR A 57 -52.321 3.043 1.209 1.00165.89 B C
ANISOU 5289 CB THR A 57 12778 35635 14616 -4139 1116 -1533 B C
ATOM 5290 CG2 THR A 57 -52.168 2.610 -0.247 1.00165.78 B C
ANISOU 5290 CG2 THR A 57 12867 35584 14536 -4170 1043 -1714 B C
ATOM 5291 OG1 THR A 57 -53.507 2.473 1.766 1.00165.95 B O
ANISOU 5291 OG1 THR A 57 12680 35564 14810 -4229 1104 -1745 B O
ATOM 5292 N ILE A 58 -48.799 2.530 1.284 1.00160.10 B N
ANISOU 5292 N ILE A 58 11986 35379 13464 -4562 1446 -2178 B N
ATOM 5293 CA ILE A 58 -47.502 3.052 0.863 1.00160.32 B C
ANISOU 5293 CA ILE A 58 12115 35461 13336 -4490 1483 -1994 B C
ATOM 5294 C ILE A 58 -47.516 3.108 -0.668 1.00165.26 B C
ANISOU 5294 C ILE A 58 13073 35622 14098 -4260 1363 -1830 B C
ATOM 5295 O ILE A 58 -47.677 2.077 -1.326 1.00164.94 B O
ANISOU 5295 O ILE A 58 13069 35454 14147 -4423 1368 -2309 B O
ATOM 5296 CB ILE A 58 -46.319 2.227 1.458 1.00161.56 B C
ANISOU 5296 CB ILE A 58 12398 35286 13702 -4699 1672 -2557 B C
ATOM 5297 CG1 ILE A 58 -46.293 2.327 2.997 1.00161.33 B C
ANISOU 5297 CG1 ILE A 58 12275 35262 13759 -4782 1777 -2610 B C
ATOM 5298 CG2 ILE A 58 -44.964 2.662 0.882 1.00161.84 B C
ANISOU 5298 CG2 ILE A 58 12549 35347 13597 -4634 1708 -2413 B C
ATOM 5299 CD1 ILE A 58 -46.808 1.106 3.702 1.00166.07 B C
ANISOU 5299 CD1 ILE A 58 13069 35133 14896 -4889 1870 -3165 B C
ATOM 5300 N LYS A 59 -47.402 4.330 -1.221 1.00164.78 B N
ANISOU 5300 N LYS A 59 13002 35810 13795 -4027 1274 -1208 B N
ATOM 5301 CA LYS A 59 -47.417 4.578 -2.664 1.00165.93 B C
ANISOU 5301 CA LYS A 59 13307 35872 13866 -3890 1173 -1045 B C
ATOM 5302 C LYS A 59 -46.039 4.289 -3.268 1.00169.69 B C
ANISOU 5302 C LYS A 59 14083 35930 14462 -3874 1261 -1242 B C
ATOM 5303 O LYS A 59 -45.940 3.431 -4.148 1.00169.67 B O
ANISOU 5303 O LYS A 59 14155 35826 14486 -3994 1254 -1638 B O
ATOM 5304 CB LYS A 59 -47.865 6.015 -2.981 1.00168.35 B C
ANISOU 5304 CB LYS A 59 13742 36044 14178 -3524 1061 -286 B C
ATOM 5305 CG LYS A 59 -49.262 6.371 -2.497 1.00179.29 B C
ANISOU 5305 CG LYS A 59 15590 36268 16263 -3151 955 -13 B C
ATOM 5306 CD LYS A 59 -49.514 7.839 -2.764 1.00186.86 B C
ANISOU 5306 CD LYS A 59 16981 36451 17566 -2706 893 628 B C
ATOM 5307 CE LYS A 59 -50.604 8.432 -1.916 1.00194.34 B C
ANISOU 5307 CE LYS A 59 18210 36586 19042 -2435 850 880 B C
ATOM 5308 NZ LYS A 59 -50.879 9.833 -2.326 1.00200.49 B N1+
ANISOU 5308 NZ LYS A 59 19395 36646 20135 -2075 807 1358 B N1+
ATOM 5309 N LYS A 60 -44.980 4.989 -2.797 1.00167.69 B N
ANISOU 5309 N LYS A 60 13733 35976 14004 -3866 1354 -1001 B N
ATOM 5310 CA LYS A 60 -43.616 4.763 -3.271 1.00167.64 B C
ANISOU 5310 CA LYS A 60 13824 35942 13928 -3945 1454 -1206 B C
ATOM 5311 C LYS A 60 -42.586 5.082 -2.186 1.00170.43 B C
ANISOU 5311 C LYS A 60 14269 36057 14431 -3904 1578 -1116 B C
ATOM 5312 O LYS A 60 -42.852 5.868 -1.273 1.00170.00 B O
ANISOU 5312 O LYS A 60 14107 36141 14343 -3793 1570 -698 B O
ATOM 5313 CB LYS A 60 -43.308 5.543 -4.574 1.00170.14 B C
ANISOU 5313 CB LYS A 60 14391 36058 14197 -3690 1385 -801 B C
ATOM 5314 CG LYS A 60 -43.058 7.044 -4.444 1.00180.84 B C
ANISOU 5314 CG LYS A 60 16328 36329 16054 -3145 1363 -42 B C
ATOM 5315 CD LYS A 60 -42.197 7.534 -5.609 1.00187.76 B C
ANISOU 5315 CD LYS A 60 17735 36417 17188 -2870 1382 144 B C
ATOM 5316 CE LYS A 60 -41.951 9.025 -5.607 1.00194.89 B C
ANISOU 5316 CE LYS A 60 19090 36502 18456 -2477 1411 727 B C
ATOM 5317 NZ LYS A 60 -40.936 9.433 -4.600 1.00200.32 B N1+
ANISOU 5317 NZ LYS A 60 20033 36575 19505 -2355 1544 808 B N1+
ATOM 5318 N VAL A 61 -41.420 4.432 -2.289 1.00168.39 B N
ANISOU 5318 N VAL A 61 13959 35939 14082 -4141 1704 -1574 B N
ATOM 5319 CA VAL A 61 -40.270 4.603 -1.401 1.00168.10 B C
ANISOU 5319 CA VAL A 61 13887 35943 14039 -4221 1835 -1620 B C
ATOM 5320 C VAL A 61 -39.070 4.974 -2.279 1.00171.43 B C
ANISOU 5320 C VAL A 61 14568 36077 14491 -4069 1873 -1457 B C
ATOM 5321 O VAL A 61 -38.822 4.305 -3.285 1.00171.34 B O
ANISOU 5321 O VAL A 61 14640 35982 14481 -4159 1882 -1806 B O
ATOM 5322 CB VAL A 61 -39.987 3.355 -0.512 1.00170.08 B C
ANISOU 5322 CB VAL A 61 14223 35749 14651 -4455 1961 -2322 B C
ATOM 5323 CG1 VAL A 61 -38.809 3.602 0.428 1.00169.33 B C
ANISOU 5323 CG1 VAL A 61 14089 35711 14540 -4551 2093 -2378 B C
ATOM 5324 CG2 VAL A 61 -41.221 2.942 0.285 1.00169.85 B C
ANISOU 5324 CG2 VAL A 61 14087 35688 14758 -4524 1929 -2464 B C
ATOM 5325 N ALA A 62 -38.349 6.049 -1.912 1.00169.34 B N
ANISOU 5325 N ALA A 62 14177 36177 13988 -3979 1907 -959 B N
ATOM 5326 CA ALA A 62 -37.176 6.539 -2.637 1.00169.45 B C
ANISOU 5326 CA ALA A 62 14284 36220 13880 -3903 1962 -769 B C
ATOM 5327 C ALA A 62 -36.015 6.790 -1.681 1.00171.80 B C
ANISOU 5327 C ALA A 62 14664 36280 14330 -3892 2078 -721 B C
ATOM 5328 O ALA A 62 -36.144 7.582 -0.746 1.00171.37 B O
ANISOU 5328 O ALA A 62 14501 36359 14251 -3791 2071 -282 B O
ATOM 5329 CB ALA A 62 -37.518 7.812 -3.402 1.00170.70 B C
ANISOU 5329 CB ALA A 62 14548 36352 13957 -3573 1874 -30 B C
ATOM 5330 N VAL A 63 -34.899 6.082 -1.891 1.00169.28 B N
ANISOU 5330 N VAL A 63 14291 36106 13922 -4141 2192 -1223 B N
ATOM 5331 CA VAL A 63 -33.699 6.221 -1.070 1.00168.85 B C
ANISOU 5331 CA VAL A 63 14199 36072 13882 -4240 2311 -1289 B C
ATOM 5332 C VAL A 63 -32.647 6.960 -1.922 1.00172.40 B C
ANISOU 5332 C VAL A 63 14909 36204 14390 -3984 2340 -879 B C
ATOM 5333 O VAL A 63 -32.159 6.426 -2.921 1.00172.25 B O
ANISOU 5333 O VAL A 63 14977 36123 14345 -4055 2373 -1193 B O
ATOM 5334 CB VAL A 63 -33.210 4.875 -0.443 1.00170.69 B C
ANISOU 5334 CB VAL A 63 14549 35846 14460 -4514 2429 -2136 B C
ATOM 5335 CG1 VAL A 63 -33.301 3.701 -1.418 1.00170.46 B C
ANISOU 5335 CG1 VAL A 63 14602 35625 14541 -4661 2449 -2722 B C
ATOM 5336 CG2 VAL A 63 -31.817 4.991 0.175 1.00170.08 B C
ANISOU 5336 CG2 VAL A 63 14457 35772 14395 -4641 2560 -2270 B C
ATOM 5337 N ASN A 64 -32.376 8.232 -1.539 1.00170.63 B N
ANISOU 5337 N ASN A 64 14555 36286 13989 -3816 2339 -174 B N
ATOM 5338 CA ASN A 64 -31.472 9.219 -2.153 1.00171.16 B C
ANISOU 5338 CA ASN A 64 14704 36348 13981 -3616 2383 353 B C
ATOM 5339 C ASN A 64 -31.695 9.343 -3.694 1.00174.88 B C
ANISOU 5339 C ASN A 64 15487 36411 14546 -3413 2343 434 B C
ATOM 5340 O ASN A 64 -30.741 9.449 -4.472 1.00174.99 B O
ANISOU 5340 O ASN A 64 15584 36414 14491 -3408 2414 419 B O
ATOM 5341 CB ASN A 64 -29.990 8.970 -1.786 1.00171.59 B C
ANISOU 5341 CB ASN A 64 14781 36329 14086 -3760 2513 78 B C
ATOM 5342 CG ASN A 64 -29.366 7.704 -2.315 1.00187.57 B C
ANISOU 5342 CG ASN A 64 17693 36510 17066 -3536 2559 -604 B C
ATOM 5343 ND2 ASN A 64 -28.732 7.796 -3.472 1.00182.37 B N
ANISOU 5343 ND2 ASN A 64 16862 36407 16022 -3649 2603 -628 B N
ATOM 5344 OD1 ASN A 64 -29.412 6.647 -1.681 1.00183.60 B O
ANISOU 5344 OD1 ASN A 64 16963 36298 16497 -3881 2592 -1234 B O
ATOM 5345 N GLY A 65 -32.969 9.380 -4.091 1.00172.85 B N
ANISOU 5345 N GLY A 65 15139 36369 14166 -3378 2227 542 B N
ATOM 5346 CA GLY A 65 -33.392 9.510 -5.480 1.00173.44 B C
ANISOU 5346 CA GLY A 65 15363 36366 14171 -3267 2167 622 B C
ATOM 5347 C GLY A 65 -33.177 8.259 -6.304 1.00176.12 B C
ANISOU 5347 C GLY A 65 15921 36335 14662 -3392 2177 -51 B C
ATOM 5348 O GLY A 65 -32.340 8.241 -7.212 1.00176.06 B O
ANISOU 5348 O GLY A 65 16010 36311 14573 -3394 2237 -115 B O
ATOM 5349 N LYS A 66 -33.946 7.204 -5.980 1.00173.49 B N
ANISOU 5349 N LYS A 66 15404 36220 14295 -3627 2128 -555 B N
ATOM 5350 CA LYS A 66 -33.941 5.894 -6.641 1.00173.25 B C
ANISOU 5350 CA LYS A 66 15420 36080 14325 -3825 2134 -1212 B C
ATOM 5351 C LYS A 66 -35.282 5.201 -6.397 1.00175.89 B C
ANISOU 5351 C LYS A 66 15836 36070 14922 -3816 2029 -1428 B C
ATOM 5352 O LYS A 66 -35.771 5.214 -5.268 1.00175.24 B O
ANISOU 5352 O LYS A 66 15614 36065 14904 -3878 2026 -1441 B O
ATOM 5353 CB LYS A 66 -32.771 5.022 -6.129 1.00174.20 B C
ANISOU 5353 CB LYS A 66 15585 35957 14645 -4016 2270 -1742 B C
ATOM 5354 CG LYS A 66 -32.521 3.742 -6.936 1.00184.38 B C
ANISOU 5354 CG LYS A 66 17444 36034 16577 -3853 2260 -2151 B C
ATOM 5355 CD LYS A 66 -33.195 2.508 -6.317 1.00190.79 B C
ANISOU 5355 CD LYS A 66 18506 36017 17968 -3822 2215 -2521 B C
ATOM 5356 CE LYS A 66 -33.125 1.284 -7.201 1.00198.43 B C
ANISOU 5356 CE LYS A 66 19915 36028 19450 -3661 2167 -2762 B C
ATOM 5357 NZ LYS A 66 -34.064 1.366 -8.353 1.00205.28 B N1+
ANISOU 5357 NZ LYS A 66 21194 36238 20566 -3314 2003 -2433 B N1+
ATOM 5358 N ASP A 67 -35.858 4.567 -7.438 1.00173.98 B N
ANISOU 5358 N ASP A 67 15571 35967 14567 -3897 1959 -1668 B N
ATOM 5359 CA ASP A 67 -37.124 3.840 -7.320 1.00173.83 B C
ANISOU 5359 CA ASP A 67 15496 35891 14659 -3976 1866 -1922 B C
ATOM 5360 C ASP A 67 -36.872 2.508 -6.590 1.00175.80 B C
ANISOU 5360 C ASP A 67 15801 35722 15274 -4170 1952 -2549 B C
ATOM 5361 O ASP A 67 -36.638 1.472 -7.222 1.00175.39 B O
ANISOU 5361 O ASP A 67 15801 35525 15316 -4308 1982 -2998 B O
ATOM 5362 CB ASP A 67 -37.779 3.632 -8.700 1.00175.72 B C
ANISOU 5362 CB ASP A 67 15930 35920 14914 -3855 1750 -1886 B C
ATOM 5363 CG ASP A 67 -39.254 3.981 -8.734 1.00181.67 B C
ANISOU 5363 CG ASP A 67 16969 36047 16009 -3557 1584 -1544 B C
ATOM 5364 OD1 ASP A 67 -40.056 3.235 -8.129 1.00181.47 B O
ANISOU 5364 OD1 ASP A 67 16850 35956 16146 -3670 1553 -1814 B O
ATOM 5365 OD2 ASP A 67 -39.609 4.988 -9.380 1.00185.83 B O1-
ANISOU 5365 OD2 ASP A 67 17783 36206 16619 -3251 1497 -1059 B O1-
ATOM 5366 N ALA A 68 -36.873 2.567 -5.243 1.00172.85 B N
ANISOU 5366 N ALA A 68 15172 35652 14850 -4345 2023 -2666 B N
ATOM 5367 CA ALA A 68 -36.621 1.432 -4.355 1.00171.73 B C
ANISOU 5367 CA ALA A 68 14949 35360 14942 -4630 2145 -3311 B C
ATOM 5368 C ALA A 68 -37.787 0.448 -4.341 1.00174.21 B C
ANISOU 5368 C ALA A 68 15346 35276 15569 -4652 2079 -3586 B C
ATOM 5369 O ALA A 68 -38.946 0.850 -4.470 1.00174.41 B O
ANISOU 5369 O ALA A 68 15325 35430 15513 -4535 1952 -3287 B O
ATOM 5370 CB ALA A 68 -36.345 1.927 -2.944 1.00171.74 B C
ANISOU 5370 CB ALA A 68 14866 35402 14987 -4658 2216 -3210 B C
ATOM 5371 N THR A 69 -37.465 -0.845 -4.179 1.00171.16 B N
ANISOU 5371 N THR A 69 14850 34860 15324 -4981 2210 -4298 B N
ATOM 5372 CA THR A 69 -38.436 -1.939 -4.125 1.00170.94 B C
ANISOU 5372 CA THR A 69 14790 34625 15533 -5115 2200 -4683 B C
ATOM 5373 C THR A 69 -38.787 -2.227 -2.651 1.00172.94 B C
ANISOU 5373 C THR A 69 15052 34536 16119 -5166 2271 -4830 B C
ATOM 5374 O THR A 69 -37.889 -2.305 -1.807 1.00171.99 B O
ANISOU 5374 O THR A 69 14901 34355 16091 -5304 2421 -5066 B O
ATOM 5375 CB THR A 69 -37.928 -3.177 -4.906 1.00176.86 B C
ANISOU 5375 CB THR A 69 15904 34530 16765 -5028 2212 -4938 B C
ATOM 5376 CG2 THR A 69 -36.492 -3.577 -4.559 1.00174.99 B C
ANISOU 5376 CG2 THR A 69 15649 34217 16622 -5217 2402 -5328 B C
ATOM 5377 OG1 THR A 69 -38.814 -4.279 -4.710 1.00177.10 B O
ANISOU 5377 OG1 THR A 69 15911 34298 17081 -5152 2219 -5282 B O
ATOM 5378 N PHE A 70 -40.099 -2.348 -2.349 1.00170.55 B N
ANISOU 5378 N PHE A 70 14563 34477 15760 -5249 2215 -4877 B N
ATOM 5379 CA PHE A 70 -40.606 -2.592 -0.996 1.00169.81 B C
ANISOU 5379 CA PHE A 70 14361 34305 15855 -5383 2303 -5090 B C
ATOM 5380 C PHE A 70 -41.658 -3.714 -0.961 1.00172.23 B C
ANISOU 5380 C PHE A 70 14762 34115 16564 -5406 2285 -5350 B C
ATOM 5381 O PHE A 70 -42.497 -3.807 -1.862 1.00172.67 B O
ANISOU 5381 O PHE A 70 14826 34237 16542 -5319 2144 -5204 B O
ATOM 5382 CB PHE A 70 -41.178 -1.299 -0.380 1.00171.52 B C
ANISOU 5382 CB PHE A 70 14543 34740 15884 -5152 2183 -4470 B C
ATOM 5383 CG PHE A 70 -42.320 -0.646 -1.128 1.00173.50 B C
ANISOU 5383 CG PHE A 70 14833 35095 15994 -4887 1970 -3934 B C
ATOM 5384 CD1 PHE A 70 -43.641 -0.921 -0.791 1.00175.83 B C
ANISOU 5384 CD1 PHE A 70 15156 35143 16507 -4817 1887 -3885 B C
ATOM 5385 CD2 PHE A 70 -42.074 0.283 -2.132 1.00175.58 B C
ANISOU 5385 CD2 PHE A 70 15234 35416 16062 -4617 1850 -3401 B C
ATOM 5386 CE1 PHE A 70 -44.695 -0.309 -1.474 1.00177.33 B C
ANISOU 5386 CE1 PHE A 70 15375 35411 16590 -4593 1701 -3431 B C
ATOM 5387 CE2 PHE A 70 -43.128 0.898 -2.811 1.00178.39 B C
ANISOU 5387 CE2 PHE A 70 15699 35684 16398 -4348 1668 -2920 B C
ATOM 5388 CZ PHE A 70 -44.432 0.598 -2.477 1.00177.29 B C
ANISOU 5388 CZ PHE A 70 15422 35629 16311 -4406 1602 -2994 B C
ATOM 5389 N ALA A 71 -41.615 -4.548 0.101 1.00168.62 B N
ANISOU 5389 N ALA A 71 14149 33587 16332 -5729 2499 -5950 B N
ATOM 5390 CA ALA A 71 -42.525 -5.680 0.301 1.00167.91 B C
ANISOU 5390 CA ALA A 71 14022 33211 16565 -5878 2561 -6340 B C
ATOM 5391 C ALA A 71 -43.043 -5.766 1.744 1.00169.13 B C
ANISOU 5391 C ALA A 71 14172 33099 16992 -5908 2650 -6412 B C
ATOM 5392 O ALA A 71 -42.335 -5.397 2.685 1.00168.25 B O
ANISOU 5392 O ALA A 71 14036 33004 16887 -5980 2775 -6490 B O
ATOM 5393 CB ALA A 71 -41.824 -6.978 -0.072 1.00167.74 B C
ANISOU 5393 CB ALA A 71 14113 32708 16912 -6033 2715 -6841 B C
ATOM 5394 N LEU A 72 -44.281 -6.273 1.905 1.00166.31 B N
ANISOU 5394 N LEU A 72 13629 32881 16681 -6057 2663 -6634 B N
ATOM 5395 CA LEU A 72 -44.948 -6.452 3.200 1.00165.52 B C
ANISOU 5395 CA LEU A 72 13439 32663 16788 -6164 2780 -6813 B C
ATOM 5396 C LEU A 72 -44.996 -7.940 3.557 1.00167.13 B C
ANISOU 5396 C LEU A 72 13795 32097 17608 -6272 2960 -7270 B C
ATOM 5397 O LEU A 72 -45.258 -8.776 2.689 1.00166.92 B O
ANISOU 5397 O LEU A 72 13790 31937 17697 -6310 2932 -7416 B O
ATOM 5398 CB LEU A 72 -46.365 -5.839 3.199 1.00166.26 B C
ANISOU 5398 CB LEU A 72 13421 33086 16665 -6014 2582 -6391 B C
ATOM 5399 CG LEU A 72 -46.440 -4.308 3.310 1.00169.95 B C
ANISOU 5399 CG LEU A 72 13960 33786 16827 -5674 2374 -5628 B C
ATOM 5400 CD1 LEU A 72 -46.484 -3.655 1.941 1.00170.81 B C
ANISOU 5400 CD1 LEU A 72 14106 34173 16621 -5469 2161 -5186 B C
ATOM 5401 CD2 LEU A 72 -47.646 -3.863 4.123 1.00172.10 B C
ANISOU 5401 CD2 LEU A 72 14193 34052 17147 -5539 2291 -5311 B C
ATOM 5402 N GLY A 73 -44.706 -8.249 4.820 1.00163.74 B N
ANISOU 5402 N GLY A 73 13274 31511 17428 -6520 3239 -7743 B N
ATOM 5403 CA GLY A 73 -44.674 -9.615 5.336 1.00162.63 B C
ANISOU 5403 CA GLY A 73 13191 30730 17873 -6706 3502 -8280 B C
ATOM 5404 C GLY A 73 -46.017 -10.142 5.801 1.00165.20 B C
ANISOU 5404 C GLY A 73 13554 30747 18468 -6618 3461 -8176 B C
ATOM 5405 O GLY A 73 -47.062 -9.749 5.271 1.00165.97 B O
ANISOU 5405 O GLY A 73 13561 31227 18273 -6507 3239 -7852 B O
ATOM 5406 N THR A 74 -45.997 -11.050 6.794 1.00161.36 B N
ANISOU 5406 N THR A 74 13000 29853 18455 -6881 3805 -8762 B N
ATOM 5407 CA THR A 74 -47.218 -11.643 7.345 1.00160.93 B C
ANISOU 5407 CA THR A 74 12881 29609 18656 -6926 3871 -8868 B C
ATOM 5408 C THR A 74 -47.866 -10.640 8.303 1.00162.96 B C
ANISOU 5408 C THR A 74 13117 30070 18732 -6794 3775 -8532 B C
ATOM 5409 O THR A 74 -47.191 -10.079 9.173 1.00162.16 B O
ANISOU 5409 O THR A 74 13029 29951 18632 -6839 3903 -8611 B O
ATOM 5410 CB THR A 74 -46.950 -13.013 7.990 1.00165.57 B C
ANISOU 5410 CB THR A 74 13811 29061 20036 -6791 4041 -8914 B C
ATOM 5411 CG2 THR A 74 -46.443 -14.040 6.988 1.00164.03 B C
ANISOU 5411 CG2 THR A 74 13640 28665 20018 -6880 4096 -9145 B C
ATOM 5412 OG1 THR A 74 -46.032 -12.877 9.078 1.00164.95 B O
ANISOU 5412 OG1 THR A 74 13828 28603 20243 -6841 4278 -9109 B O
ATOM 5413 N THR A 75 -49.166 -10.379 8.090 1.00160.58 B N
ANISOU 5413 N THR A 75 12577 30288 18150 -6843 3656 -8455 B N
ATOM 5414 CA THR A 75 -49.962 -9.420 8.858 1.00160.55 B C
ANISOU 5414 CA THR A 75 12444 30668 17890 -6782 3570 -8192 B C
ATOM 5415 C THR A 75 -50.167 -9.886 10.318 1.00160.92 B C
ANISOU 5415 C THR A 75 12577 30124 18443 -6845 3837 -8464 B C
ATOM 5416 O THR A 75 -50.221 -11.089 10.593 1.00159.74 B O
ANISOU 5416 O THR A 75 12490 29383 18820 -6973 4082 -8881 B O
ATOM 5417 CB THR A 75 -51.297 -9.128 8.136 1.00167.91 B C
ANISOU 5417 CB THR A 75 13526 31554 18717 -6374 3164 -7421 B C
ATOM 5418 CG2 THR A 75 -52.197 -10.367 7.977 1.00167.13 B C
ANISOU 5418 CG2 THR A 75 13404 31128 18969 -6481 3245 -7704 B C
ATOM 5419 OG1 THR A 75 -51.990 -8.080 8.817 1.00168.52 B O
ANISOU 5419 OG1 THR A 75 13501 31977 18553 -6263 3059 -7069 B O
ATOM 5420 N HIS A 76 -50.257 -8.910 11.243 1.00157.63 B N
ANISOU 5420 N HIS A 76 11969 30169 17755 -6951 3903 -8495 B N
ATOM 5421 CA HIS A 76 -50.464 -9.137 12.676 1.00156.44 B C
ANISOU 5421 CA HIS A 76 11841 29581 18016 -7063 4192 -8820 B C
ATOM 5422 C HIS A 76 -51.860 -8.651 13.107 1.00158.19 B C
ANISOU 5422 C HIS A 76 11968 30069 18069 -6928 4024 -8456 B C
ATOM 5423 O HIS A 76 -52.440 -7.780 12.453 1.00159.00 B O
ANISOU 5423 O HIS A 76 11924 30854 17637 -6788 3708 -7963 B O
ATOM 5424 CB HIS A 76 -49.368 -8.443 13.500 1.00156.53 B C
ANISOU 5424 CB HIS A 76 11959 29478 18039 -7079 4323 -8863 B C
ATOM 5425 CG HIS A 76 -49.228 -8.983 14.889 1.00157.95 B C
ANISOU 5425 CG HIS A 76 12371 28706 18936 -7087 4657 -9158 B C
ATOM 5426 CD2 HIS A 76 -48.441 -9.982 15.352 1.00158.05 B C
ANISOU 5426 CD2 HIS A 76 12608 27797 19647 -7128 4970 -9523 B C
ATOM 5427 ND1 HIS A 76 -49.969 -8.474 15.940 1.00159.28 B N
ANISOU 5427 ND1 HIS A 76 12556 28795 19168 -7019 4693 -9028 B N
ATOM 5428 CE1 HIS A 76 -49.608 -9.171 17.004 1.00157.84 B C
ANISOU 5428 CE1 HIS A 76 12535 27724 19714 -7121 5104 -9489 B C
ATOM 5429 NE2 HIS A 76 -48.694 -10.092 16.700 1.00157.30 B N
ANISOU 5429 NE2 HIS A 76 12602 27098 20067 -7163 5275 -9751 B N
ATOM 5430 N SER A 77 -52.390 -9.227 14.207 1.00153.65 B N
ANISOU 5430 N SER A 77 11286 29198 17896 -7170 4374 -9000 B N
ATOM 5431 CA SER A 77 -53.712 -8.942 14.774 1.00153.20 B C
ANISOU 5431 CA SER A 77 11078 29382 17749 -7148 4322 -8863 B C
ATOM 5432 C SER A 77 -53.886 -7.478 15.219 1.00154.34 B C
ANISOU 5432 C SER A 77 11140 30117 17383 -7005 4116 -8362 B C
ATOM 5433 O SER A 77 -54.975 -6.928 15.050 1.00154.86 B O
ANISOU 5433 O SER A 77 11040 30666 17135 -6896 3903 -7976 B O
ATOM 5434 CB SER A 77 -53.982 -9.864 15.959 1.00154.70 B C
ANISOU 5434 CB SER A 77 11486 28583 18710 -7140 4640 -9158 B C
ATOM 5435 OG SER A 77 -55.355 -9.867 16.315 1.00161.90 B O
ANISOU 5435 OG SER A 77 12560 29233 19720 -6791 4395 -8550 B O
ATOM 5436 N PHE A 78 -52.831 -6.858 15.784 1.00149.98 B N
ANISOU 5436 N PHE A 78 10512 29829 16647 -7200 4284 -8625 B N
ATOM 5437 CA PHE A 78 -52.884 -5.481 16.291 1.00149.63 B C
ANISOU 5437 CA PHE A 78 10328 30465 16058 -7126 4121 -8183 B C
ATOM 5438 C PHE A 78 -51.602 -4.666 15.995 1.00149.99 B C
ANISOU 5438 C PHE A 78 10441 30795 15753 -7059 4009 -7913 B C
ATOM 5439 O PHE A 78 -51.699 -3.447 15.827 1.00150.30 B O
ANISOU 5439 O PHE A 78 10324 31618 15165 -6888 3717 -7241 B O
ATOM 5440 CB PHE A 78 -53.169 -5.470 17.808 1.00150.47 B C
ANISOU 5440 CB PHE A 78 10560 30030 16581 -7162 4383 -8398 B C
ATOM 5441 CG PHE A 78 -52.304 -6.394 18.638 1.00150.30 B C
ANISOU 5441 CG PHE A 78 10843 28858 17406 -7299 4843 -9060 B C
ATOM 5442 CD1 PHE A 78 -51.091 -5.957 19.158 1.00151.99 B C
ANISOU 5442 CD1 PHE A 78 11287 28705 17759 -7274 4961 -9080 B C
ATOM 5443 CD2 PHE A 78 -52.712 -7.693 18.915 1.00151.27 B C
ANISOU 5443 CD2 PHE A 78 11136 28056 18285 -7294 5094 -9404 B C
ATOM 5444 CE1 PHE A 78 -50.288 -6.814 19.916 1.00151.46 B C
ANISOU 5444 CE1 PHE A 78 11509 27456 18583 -7357 5418 -9628 B C
ATOM 5445 CE2 PHE A 78 -51.909 -8.548 19.673 1.00152.01 B C
ANISOU 5445 CE2 PHE A 78 11551 26961 19247 -7293 5491 -9785 B C
ATOM 5446 CZ PHE A 78 -50.706 -8.102 20.172 1.00150.13 B C
ANISOU 5446 CZ PHE A 78 11418 26466 19159 -7399 5719 -10023 B C
ATOM 5447 N LYS A 79 -50.419 -5.323 15.948 1.00144.92 B N
ANISOU 5447 N LYS A 79 9822 29840 15403 -7385 4347 -8663 B N
ATOM 5448 CA LYS A 79 -49.131 -4.654 15.693 1.00143.86 B C
ANISOU 5448 CA LYS A 79 9703 30007 14951 -7420 4310 -8576 B C
ATOM 5449 C LYS A 79 -49.069 -4.002 14.301 1.00147.45 B C
ANISOU 5449 C LYS A 79 10124 31069 14831 -7115 3862 -7806 B C
ATOM 5450 O LYS A 79 -48.345 -3.019 14.131 1.00147.64 B O
ANISOU 5450 O LYS A 79 10110 31577 14408 -7027 3713 -7399 B O
ATOM 5451 CB LYS A 79 -47.954 -5.635 15.834 1.00143.23 B C
ANISOU 5451 CB LYS A 79 9892 28948 15582 -7573 4678 -9229 B C
ATOM 5452 CG LYS A 79 -47.629 -6.056 17.254 1.00140.17 B C
ANISOU 5452 CG LYS A 79 9746 27589 15925 -7668 5100 -9683 B C
ATOM 5453 CD LYS A 79 -46.188 -6.549 17.364 1.00139.47 B C
ANISOU 5453 CD LYS A 79 9937 26617 16440 -7713 5389 -10050 B C
ATOM 5454 CE LYS A 79 -46.102 -8.027 17.662 1.00138.16 B C
ANISOU 5454 CE LYS A 79 9989 25240 17265 -7699 5746 -10465 B C
ATOM 5455 NZ LYS A 79 -44.710 -8.438 17.982 1.00140.72 B N1+
ANISOU 5455 NZ LYS A 79 10685 24518 18266 -7567 5958 -10517 B N1+
ATOM 5456 N GLY A 80 -49.751 -4.614 13.326 1.00145.31 B N
ANISOU 5456 N GLY A 80 9689 31025 14496 -7173 3785 -7922 B N
ATOM 5457 CA GLY A 80 -49.797 -4.178 11.932 1.00145.71 B C
ANISOU 5457 CA GLY A 80 9641 31653 14071 -7003 3468 -7431 B C
ATOM 5458 C GLY A 80 -48.981 -5.046 10.989 1.00147.38 B C
ANISOU 5458 C GLY A 80 10056 31371 14572 -7025 3529 -7722 B C
ATOM 5459 O GLY A 80 -48.364 -6.025 11.418 1.00146.28 B O
ANISOU 5459 O GLY A 80 10047 30569 14962 -7239 3849 -8374 B O
ATOM 5460 N THR A 81 -48.976 -4.700 9.691 1.00144.99 B N
ANISOU 5460 N THR A 81 9578 31724 13789 -6994 3314 -7471 B N
ATOM 5461 CA THR A 81 -48.202 -5.439 8.691 1.00144.37 B C
ANISOU 5461 CA THR A 81 9592 31420 13840 -7083 3373 -7788 B C
ATOM 5462 C THR A 81 -46.847 -4.713 8.520 1.00146.57 B C
ANISOU 5462 C THR A 81 10016 31748 13925 -6956 3318 -7503 B C
ATOM 5463 O THR A 81 -46.851 -3.492 8.337 1.00147.20 B O
ANISOU 5463 O THR A 81 10002 32431 13497 -6753 3086 -6853 B O
ATOM 5464 CB THR A 81 -48.992 -5.601 7.375 1.00150.91 B C
ANISOU 5464 CB THR A 81 10613 32037 14689 -6723 3047 -7233 B C
ATOM 5465 CG2 THR A 81 -48.454 -6.733 6.508 1.00149.76 B C
ANISOU 5465 CG2 THR A 81 10544 31559 14800 -6883 3167 -7715 B C
ATOM 5466 OG1 THR A 81 -50.373 -5.844 7.659 1.00150.55 B O
ANISOU 5466 OG1 THR A 81 10450 32031 14721 -6724 3003 -7209 B O
ATOM 5467 N PRO A 82 -45.684 -5.415 8.623 1.00142.56 B N
ANISOU 5467 N PRO A 82 9521 30976 13669 -7269 3622 -8204 B N
ATOM 5468 CA PRO A 82 -44.388 -4.715 8.504 1.00141.98 B C
ANISOU 5468 CA PRO A 82 9477 31139 13329 -7262 3616 -8070 B C
ATOM 5469 C PRO A 82 -44.093 -4.221 7.088 1.00144.46 B C
ANISOU 5469 C PRO A 82 9852 31763 13273 -6999 3327 -7513 B C
ATOM 5470 O PRO A 82 -44.704 -4.703 6.133 1.00144.80 B O
ANISOU 5470 O PRO A 82 9892 31790 13337 -6956 3229 -7517 B O
ATOM 5471 CB PRO A 82 -43.361 -5.779 8.927 1.00142.08 B C
ANISOU 5471 CB PRO A 82 9715 30254 14016 -7455 3965 -8758 B C
ATOM 5472 CG PRO A 82 -44.152 -6.897 9.532 1.00144.71 B C
ANISOU 5472 CG PRO A 82 10212 29741 15030 -7444 4125 -9047 B C
ATOM 5473 CD PRO A 82 -45.484 -6.856 8.866 1.00142.60 B C
ANISOU 5473 CD PRO A 82 9694 30087 14399 -7442 3927 -8876 B C
ATOM 5474 N LEU A 83 -43.156 -3.258 6.960 1.00140.87 B N
ANISOU 5474 N LEU A 83 9237 31985 12302 -7039 3283 -7284 B N
ATOM 5475 CA LEU A 83 -42.736 -2.687 5.678 1.00140.67 B C
ANISOU 5475 CA LEU A 83 9178 32421 11849 -6876 3079 -6841 B C
ATOM 5476 C LEU A 83 -41.217 -2.844 5.521 1.00141.34 B C
ANISOU 5476 C LEU A 83 9429 32195 12078 -6951 3221 -7098 B C
ATOM 5477 O LEU A 83 -40.445 -2.198 6.239 1.00140.89 B O
ANISOU 5477 O LEU A 83 9363 32268 11901 -6982 3282 -7001 B O
ATOM 5478 CB LEU A 83 -43.180 -1.204 5.557 1.00141.51 B C
ANISOU 5478 CB LEU A 83 9163 33195 11410 -6553 2792 -5886 B C
ATOM 5479 CG LEU A 83 -42.589 -0.342 4.413 1.00145.03 B C
ANISOU 5479 CG LEU A 83 9771 33717 11617 -6189 2574 -5172 B C
ATOM 5480 CD1 LEU A 83 -43.056 -0.816 3.038 1.00145.66 B C
ANISOU 5480 CD1 LEU A 83 9903 33739 11701 -6106 2455 -5167 B C
ATOM 5481 CD2 LEU A 83 -42.941 1.119 4.600 1.00146.89 B C
ANISOU 5481 CD2 LEU A 83 9974 34295 11541 -5820 2366 -4198 B C
ATOM 5482 N GLU A 84 -40.795 -3.728 4.602 1.00137.32 B N
ANISOU 5482 N GLU A 84 8851 31681 11643 -7195 3349 -7663 B N
ATOM 5483 CA GLU A 84 -39.376 -3.973 4.354 1.00136.02 B C
ANISOU 5483 CA GLU A 84 8767 31327 11588 -7342 3516 -8018 B C
ATOM 5484 C GLU A 84 -38.912 -3.178 3.132 1.00137.08 B C
ANISOU 5484 C GLU A 84 8923 31902 11259 -7090 3275 -7414 B C
ATOM 5485 O GLU A 84 -39.482 -3.333 2.052 1.00136.95 B O
ANISOU 5485 O GLU A 84 8877 32073 11084 -6991 3125 -7245 B O
ATOM 5486 CB GLU A 84 -39.086 -5.481 4.182 1.00136.27 B C
ANISOU 5486 CB GLU A 84 8959 30543 12276 -7520 3758 -8724 B C
ATOM 5487 CG GLU A 84 -37.600 -5.816 4.087 1.00142.75 B C
ANISOU 5487 CG GLU A 84 10176 30506 13556 -7358 3834 -8724 B C
ATOM 5488 CD GLU A 84 -37.234 -7.289 4.075 1.00152.56 B C
ANISOU 5488 CD GLU A 84 11940 30295 15733 -7093 3881 -8771 B C
ATOM 5489 OE1 GLU A 84 -37.855 -8.058 3.305 1.00144.23 B O
ANISOU 5489 OE1 GLU A 84 10528 29776 14499 -7454 3994 -9331 B O
ATOM 5490 OE2 GLU A 84 -36.290 -7.665 4.808 1.00145.52 B O1-
ANISOU 5490 OE2 GLU A 84 10894 29276 15122 -7522 4286 -9561 B O1-
ATOM 5491 N ILE A 85 -37.891 -2.314 3.315 1.00133.18 B N
ANISOU 5491 N ILE A 85 8277 31959 10368 -7188 3316 -7303 B N
ATOM 5492 CA ILE A 85 -37.311 -1.531 2.221 1.00132.84 B C
ANISOU 5492 CA ILE A 85 8204 32404 9866 -7000 3143 -6775 B C
ATOM 5493 C ILE A 85 -35.940 -2.145 1.955 1.00134.13 B C
ANISOU 5493 C ILE A 85 8580 32017 10367 -7099 3320 -7213 B C
ATOM 5494 O ILE A 85 -35.053 -2.051 2.807 1.00132.73 B O
ANISOU 5494 O ILE A 85 8412 31699 10323 -7277 3504 -7504 B O
ATOM 5495 CB ILE A 85 -37.273 0.004 2.512 1.00135.23 B C
ANISOU 5495 CB ILE A 85 8493 33111 9775 -6660 2935 -5819 B C
ATOM 5496 CG1 ILE A 85 -38.692 0.569 2.748 1.00135.77 B C
ANISOU 5496 CG1 ILE A 85 8445 33482 9659 -6449 2739 -5262 B C
ATOM 5497 CG2 ILE A 85 -36.567 0.763 1.380 1.00135.76 B C
ANISOU 5497 CG2 ILE A 85 8598 33478 9507 -6432 2807 -5268 B C
ATOM 5498 CD1 ILE A 85 -38.765 1.715 3.759 1.00139.61 B C
ANISOU 5498 CD1 ILE A 85 9025 33887 10135 -6142 2633 -4518 B C
ATOM 5499 N THR A 86 -35.795 -2.884 0.847 1.00132.20 B N
ANISOU 5499 N THR A 86 8314 31783 10133 -7201 3348 -7531 B N
ATOM 5500 CA THR A 86 -34.524 -3.549 0.544 1.00131.57 B C
ANISOU 5500 CA THR A 86 8348 31310 10331 -7365 3544 -8029 B C
ATOM 5501 C THR A 86 -33.624 -2.554 -0.223 1.00135.49 B C
ANISOU 5501 C THR A 86 8988 31987 10506 -7053 3373 -7358 B C
ATOM 5502 O THR A 86 -33.882 -2.229 -1.388 1.00136.11 B O
ANISOU 5502 O THR A 86 9060 32397 10260 -6855 3189 -6930 B O
ATOM 5503 CB THR A 86 -34.720 -4.935 -0.124 1.00134.96 B C
ANISOU 5503 CB THR A 86 9047 30898 11333 -7297 3575 -8336 B C
ATOM 5504 CG2 THR A 86 -35.786 -4.947 -1.220 1.00133.70 B C
ANISOU 5504 CG2 THR A 86 8795 31152 10855 -7182 3364 -8061 B C
ATOM 5505 OG1 THR A 86 -33.467 -5.411 -0.627 1.00135.01 B O
ANISOU 5505 OG1 THR A 86 9145 30637 11516 -7400 3719 -8664 B O
ATOM 5506 N LEU A 87 -32.587 -2.046 0.490 1.00132.94 B N
ANISOU 5506 N LEU A 87 8579 31834 10098 -7229 3523 -7508 B N
ATOM 5507 CA LEU A 87 -31.604 -1.050 0.042 1.00133.34 B C
ANISOU 5507 CA LEU A 87 8628 32259 9775 -7084 3445 -7024 B C
ATOM 5508 C LEU A 87 -30.800 -1.518 -1.174 1.00136.83 B C
ANISOU 5508 C LEU A 87 9293 32325 10370 -6960 3440 -7068 B C
ATOM 5509 O LEU A 87 -30.411 -2.688 -1.228 1.00135.86 B O
ANISOU 5509 O LEU A 87 9241 31700 10680 -7188 3631 -7765 B O
ATOM 5510 CB LEU A 87 -30.626 -0.680 1.179 1.00132.72 B C
ANISOU 5510 CB LEU A 87 8565 32038 9824 -7241 3613 -7208 B C
ATOM 5511 CG LEU A 87 -31.221 -0.076 2.456 1.00136.06 B C
ANISOU 5511 CG LEU A 87 9044 32364 10288 -7082 3532 -6789 B C
ATOM 5512 CD1 LEU A 87 -30.264 -0.233 3.623 1.00135.23 B C
ANISOU 5512 CD1 LEU A 87 9019 31812 10551 -7354 3792 -7335 B C
ATOM 5513 CD2 LEU A 87 -31.594 1.392 2.266 1.00138.76 B C
ANISOU 5513 CD2 LEU A 87 9358 33220 10144 -6658 3250 -5665 B C
ATOM 5514 N PRO A 88 -30.513 -0.607 -2.137 1.00135.97 B N
ANISOU 5514 N PRO A 88 9089 32836 9736 -6793 3300 -6510 B N
ATOM 5515 CA PRO A 88 -29.732 -1.003 -3.333 1.00136.06 B C
ANISOU 5515 CA PRO A 88 9194 32757 9746 -6789 3334 -6658 B C
ATOM 5516 C PRO A 88 -28.258 -1.303 -3.032 1.00137.58 B C
ANISOU 5516 C PRO A 88 9531 32488 10258 -6907 3523 -7023 B C
ATOM 5517 O PRO A 88 -27.666 -2.182 -3.659 1.00136.65 B O
ANISOU 5517 O PRO A 88 9479 32073 10368 -7043 3643 -7500 B O
ATOM 5518 CB PRO A 88 -29.854 0.215 -4.260 1.00138.51 B C
ANISOU 5518 CB PRO A 88 9555 33451 9621 -6394 3110 -5737 B C
ATOM 5519 CG PRO A 88 -30.956 1.062 -3.675 1.00142.10 B C
ANISOU 5519 CG PRO A 88 10052 33917 10022 -6094 2928 -5056 B C
ATOM 5520 CD PRO A 88 -30.914 0.812 -2.211 1.00138.12 B C
ANISOU 5520 CD PRO A 88 9334 33546 9597 -6436 3081 -5543 B C
ATOM 5521 N PHE A 89 -27.674 -0.559 -2.083 1.00135.14 B N
ANISOU 5521 N PHE A 89 9056 32527 9762 -7055 3609 -6988 B N
ATOM 5522 CA PHE A 89 -26.288 -0.706 -1.648 1.00134.38 B C
ANISOU 5522 CA PHE A 89 9010 32158 9891 -7261 3820 -7401 B C
ATOM 5523 C PHE A 89 -26.254 -0.909 -0.132 1.00135.36 B C
ANISOU 5523 C PHE A 89 9190 31818 10421 -7439 3979 -7777 B C
ATOM 5524 O PHE A 89 -27.011 -0.257 0.594 1.00135.37 B O
ANISOU 5524 O PHE A 89 9089 32137 10207 -7373 3876 -7422 B O
ATOM 5525 CB PHE A 89 -25.442 0.510 -2.080 1.00136.60 B C
ANISOU 5525 CB PHE A 89 9331 32770 9800 -6989 3700 -6660 B C
ATOM 5526 CG PHE A 89 -25.951 1.857 -1.611 1.00138.78 B C
ANISOU 5526 CG PHE A 89 9556 33452 9723 -6683 3501 -5746 B C
ATOM 5527 CD1 PHE A 89 -26.879 2.570 -2.363 1.00142.22 B C
ANISOU 5527 CD1 PHE A 89 10059 34050 9928 -6262 3261 -4922 B C
ATOM 5528 CD2 PHE A 89 -25.479 2.427 -0.433 1.00140.19 B C
ANISOU 5528 CD2 PHE A 89 9764 33520 9984 -6693 3542 -5591 B C
ATOM 5529 CE1 PHE A 89 -27.350 3.811 -1.927 1.00143.56 B C
ANISOU 5529 CE1 PHE A 89 10166 34536 9843 -5974 3110 -4056 B C
ATOM 5530 CE2 PHE A 89 -25.944 3.673 -0.005 1.00142.89 B C
ANISOU 5530 CE2 PHE A 89 10086 34133 10075 -6349 3354 -4644 B C
ATOM 5531 CZ PHE A 89 -26.880 4.355 -0.751 1.00142.55 B C
ANISOU 5531 CZ PHE A 89 9938 34550 9676 -6056 3160 -3924 B C
ATOM 5532 N SER A 90 -25.399 -1.832 0.336 1.00131.21 B N
ANISOU 5532 N SER A 90 8642 30859 10352 -7870 4324 -8726 B N
ATOM 5533 CA SER A 90 -25.255 -2.160 1.755 1.00129.80 B C
ANISOU 5533 CA SER A 90 8504 30149 10663 -8145 4589 -9297 B C
ATOM 5534 C SER A 90 -24.611 -1.009 2.532 1.00131.41 B C
ANISOU 5534 C SER A 90 8739 30546 10644 -8082 4548 -8882 B C
ATOM 5535 O SER A 90 -23.435 -0.687 2.327 1.00131.56 B O
ANISOU 5535 O SER A 90 8809 30543 10634 -8114 4613 -8872 B O
ATOM 5536 CB SER A 90 -24.450 -3.445 1.934 1.00131.84 B C
ANISOU 5536 CB SER A 90 9044 29231 11816 -8249 4872 -9971 B C
ATOM 5537 OG SER A 90 -23.205 -3.382 1.254 1.00140.28 B O
ANISOU 5537 OG SER A 90 10468 29751 13082 -7892 4749 -9543 B O
ATOM 5538 N LEU A 91 -25.409 -0.375 3.402 1.00127.97 B N
ANISOU 5538 N LEU A 91 8072 30688 9863 -8208 4515 -8747 B N
ATOM 5539 CA LEU A 91 -25.004 0.739 4.261 1.00127.44 B C
ANISOU 5539 CA LEU A 91 7937 31004 9480 -8232 4483 -8362 B C
ATOM 5540 C LEU A 91 -23.995 0.281 5.309 1.00126.80 B C
ANISOU 5540 C LEU A 91 8099 29964 10114 -8533 4861 -9131 B C
ATOM 5541 O LEU A 91 -24.030 -0.874 5.741 1.00125.10 B O
ANISOU 5541 O LEU A 91 8006 28878 10647 -8781 5198 -10000 B O
ATOM 5542 CB LEU A 91 -26.239 1.345 4.953 1.00128.14 B C
ANISOU 5542 CB LEU A 91 7893 31553 9241 -8090 4284 -7819 B C
ATOM 5543 CG LEU A 91 -26.475 2.846 4.756 1.00132.73 B C
ANISOU 5543 CG LEU A 91 8431 32778 9224 -7555 3881 -6423 B C
ATOM 5544 CD1 LEU A 91 -27.024 3.145 3.369 1.00133.74 B C
ANISOU 5544 CD1 LEU A 91 8479 33322 9015 -7200 3628 -5794 B C
ATOM 5545 CD2 LEU A 91 -27.458 3.373 5.777 1.00134.56 B C
ANISOU 5545 CD2 LEU A 91 8635 33124 9366 -7423 3760 -5929 B C
ATOM 5546 N THR A 92 -23.094 1.187 5.711 1.00123.86 B N
ANISOU 5546 N THR A 92 7617 30034 9411 -8724 4927 -9020 B N
ATOM 5547 CA THR A 92 -22.066 0.881 6.703 1.00122.25 B C
ANISOU 5547 CA THR A 92 7640 28906 9902 -9083 5365 -9821 B C
ATOM 5548 C THR A 92 -22.475 1.417 8.088 1.00123.78 B C
ANISOU 5548 C THR A 92 7991 28799 10243 -9084 5401 -9657 B C
ATOM 5549 O THR A 92 -23.374 2.262 8.192 1.00122.44 B O
ANISOU 5549 O THR A 92 7733 29302 9486 -8719 4981 -8668 B O
ATOM 5550 CB THR A 92 -20.694 1.390 6.242 1.00126.26 B C
ANISOU 5550 CB THR A 92 8385 29146 10441 -8841 5273 -9401 B C
ATOM 5551 CG2 THR A 92 -20.587 2.910 6.235 1.00125.87 B C
ANISOU 5551 CG2 THR A 92 8108 30220 9499 -8709 4966 -8424 B C
ATOM 5552 OG1 THR A 92 -19.692 0.827 7.085 1.00125.90 B O
ANISOU 5552 OG1 THR A 92 8653 27854 11330 -9118 5745 -10243 B O
ATOM 5553 N ARG A 93 -21.796 0.897 9.139 1.00113.04 B N
ANISOU 5553 N ARG A 93 7344 25467 10141 -8801 5623 -9836 B N
ATOM 5554 CA AARG A 93 -22.005 1.251 10.545 0.50103.99 B C
ANISOU 5554 CA AARG A 93 6962 22786 9765 -8062 5385 -8961 B C
ATOM 5555 CA BARG A 93 -22.010 1.252 10.540 0.50104.04 B C
ANISOU 5555 CA BARG A 93 6964 22803 9765 -8064 5384 -8961 B C
ATOM 5556 C ARG A 93 -21.634 2.718 10.771 1.00101.58 B C
ANISOU 5556 C ARG A 93 7046 22374 9175 -7342 4852 -7513 B C
ATOM 5557 O ARG A 93 -20.502 3.117 10.518 1.00 99.38 B O
ANISOU 5557 O ARG A 93 6958 21816 8984 -7201 4820 -7276 B O
ATOM 5558 CB AARG A 93 -21.170 0.325 11.450 0.50 99.94 B C
ANISOU 5558 CB AARG A 93 6969 20439 10566 -7990 5792 -9493 B C
ATOM 5559 CB BARG A 93 -21.184 0.318 11.436 0.50100.13 B C
ANISOU 5559 CB BARG A 93 6982 20483 10579 -7998 5794 -9503 B C
ATOM 5560 CG AARG A 93 -21.614 0.274 12.907 0.50100.07 B C
ANISOU 5560 CG AARG A 93 7598 19040 11385 -7421 5686 -8928 B C
ATOM 5561 CG BARG A 93 -21.747 0.105 12.828 0.50101.44 B C
ANISOU 5561 CG BARG A 93 7675 19329 11538 -7528 5749 -9102 B C
ATOM 5562 CD AARG A 93 -20.502 -0.208 13.824 0.50 99.84 B C
ANISOU 5562 CD AARG A 93 8120 17313 12502 -7132 5927 -8938 B C
ATOM 5563 CD BARG A 93 -20.915 0.829 13.855 0.50 98.39 B C
ANISOU 5563 CD BARG A 93 8039 17625 11720 -6795 5469 -8120 B C
ATOM 5564 NE AARG A 93 -20.299 -1.658 13.772 0.50107.94 B N
ANISOU 5564 NE AARG A 93 8882 17784 14345 -7651 6617 -10119 B N
ATOM 5565 NE BARG A 93 -21.134 0.347 15.219 0.50 94.47 B N
ANISOU 5565 NE BARG A 93 8002 15758 12135 -6439 5565 -7951 B N
ATOM 5566 CZ AARG A 93 -19.177 -2.274 14.135 0.50118.28 B C
ANISOU 5566 CZ AARG A 93 10418 17917 16605 -7596 6983 -10353 B C
ATOM 5567 CZ BARG A 93 -21.842 0.990 16.141 0.50 92.54 B C
ANISOU 5567 CZ BARG A 93 8096 15207 11859 -5937 5206 -7129 B C
ATOM 5568 NH1AARG A 93 -18.136 -1.573 14.571 0.50 91.16 B N1+
ANISOU 5568 NH1AARG A 93 7490 13813 13333 -7069 6680 -9536 B N1+
ATOM 5569 NH1BARG A 93 -22.427 2.147 15.853 0.50 73.57 B N1+
ANISOU 5569 NH1BARG A 93 5624 13678 8650 -5713 4759 -6382 B N1+
ATOM 5570 NH2AARG A 93 -19.082 -3.594 14.057 0.50113.52 B N
ANISOU 5570 NH2AARG A 93 9488 16798 16845 -8076 7696 -11409 B N
ATOM 5571 NH2BARG A 93 -21.966 0.486 17.360 0.50 71.84 B N
ANISOU 5571 NH2BARG A 93 5840 11416 10040 -5650 5324 -7014 B N
ATOM 5572 N GLY A 94 -22.621 3.502 11.198 1.00 95.19 B N
ANISOU 5572 N GLY A 94 6294 21818 8057 -6927 4489 -6599 B N
ATOM 5573 CA GLY A 94 -22.468 4.927 11.463 1.00 90.54 B C
ANISOU 5573 CA GLY A 94 5992 21105 7304 -6247 4064 -5220 B C
ATOM 5574 C GLY A 94 -22.705 5.826 10.266 1.00 98.57 B C
ANISOU 5574 C GLY A 94 6352 23870 7231 -6307 3844 -4566 B C
ATOM 5575 O GLY A 94 -22.342 7.006 10.301 1.00 95.21 B O
ANISOU 5575 O GLY A 94 6078 23349 6747 -5774 3590 -3433 B O
ATOM 5576 N GLN A 95 -23.323 5.289 9.199 1.00102.71 B N
ANISOU 5576 N GLN A 95 6077 26053 6893 -6961 3972 -5254 B N
ATOM 5577 CA GLN A 95 -23.618 6.090 8.010 1.00108.45 B C
ANISOU 5577 CA GLN A 95 6040 28702 6464 -7048 3768 -4577 B C
ATOM 5578 C GLN A 95 -25.080 6.503 8.000 1.00112.48 B C
ANISOU 5578 C GLN A 95 6112 30226 6400 -6945 3553 -3969 B C
ATOM 5579 O GLN A 95 -25.939 5.729 8.412 1.00113.03 B O
ANISOU 5579 O GLN A 95 6139 30201 6605 -7230 3675 -4695 B O
ATOM 5580 CB GLN A 95 -23.263 5.340 6.718 1.00117.94 B C
ANISOU 5580 CB GLN A 95 6512 31393 6908 -7865 4031 -5660 B C
ATOM 5581 CG GLN A 95 -22.914 6.261 5.549 1.00123.83 B C
ANISOU 5581 CG GLN A 95 6890 33229 6932 -7571 3782 -4632 B C
ATOM 5582 CD GLN A 95 -22.451 5.506 4.328 1.00129.81 B C
ANISOU 5582 CD GLN A 95 8082 33016 8224 -7286 3815 -4932 B C
ATOM 5583 NE2 GLN A 95 -21.255 5.841 3.853 1.00118.45 B N
ANISOU 5583 NE2 GLN A 95 6220 32578 6207 -7704 3949 -5100 B N
ATOM 5584 OE1 GLN A 95 -23.162 4.650 3.780 1.00127.30 B O
ANISOU 5584 OE1 GLN A 95 7674 32763 7931 -7452 3874 -5514 B O
ATOM 5585 N GLU A 96 -25.351 7.728 7.535 1.00108.78 B N
ANISOU 5585 N GLU A 96 5287 30694 5352 -6522 3269 -2593 B N
ATOM 5586 CA GLU A 96 -26.694 8.279 7.441 1.00111.23 B C
ANISOU 5586 CA GLU A 96 5094 32070 5098 -6351 3061 -1774 B C
ATOM 5587 C GLU A 96 -27.124 8.392 5.983 1.00121.21 B C
ANISOU 5587 C GLU A 96 5670 34888 5496 -6485 2988 -1533 B C
ATOM 5588 O GLU A 96 -26.304 8.701 5.114 1.00120.51 B O
ANISOU 5588 O GLU A 96 5557 34949 5283 -6377 2994 -1274 B O
ATOM 5589 CB GLU A 96 -26.790 9.636 8.152 1.00107.39 B C
ANISOU 5589 CB GLU A 96 5000 30658 5146 -5465 2844 -189 B C
ATOM 5590 CG GLU A 96 -26.875 9.507 9.664 1.00105.70 B C
ANISOU 5590 CG GLU A 96 5727 28347 6086 -5072 2858 -324 B C
ATOM 5591 CD GLU A 96 -27.298 10.733 10.458 1.00110.85 B C
ANISOU 5591 CD GLU A 96 6681 28163 7275 -4303 2705 1028 B C
ATOM 5592 OE1 GLU A 96 -27.513 11.801 9.841 1.00109.33 B O
ANISOU 5592 OE1 GLU A 96 5964 28900 6677 -3987 2613 2249 B O
ATOM 5593 OE2 GLU A 96 -27.393 10.634 11.704 1.00 81.47 B O1-
ANISOU 5593 OE2 GLU A 96 3679 22853 4422 -4018 2718 882 B O1-
ATOM 5594 N VAL A 97 -28.410 8.111 5.723 1.00119.24 B N
ANISOU 5594 N VAL A 97 5279 34904 5123 -6451 2909 -1572 B N
ATOM 5595 CA VAL A 97 -29.028 8.165 4.391 1.00119.85 B C
ANISOU 5595 CA VAL A 97 5363 35056 5119 -6160 2806 -1261 B C
ATOM 5596 C VAL A 97 -30.443 8.761 4.530 1.00124.38 B C
ANISOU 5596 C VAL A 97 6006 35405 5850 -5653 2613 -376 B C
ATOM 5597 O VAL A 97 -31.007 8.735 5.625 1.00123.78 B O
ANISOU 5597 O VAL A 97 5832 35402 5796 -5731 2593 -359 B O
ATOM 5598 CB VAL A 97 -29.018 6.768 3.697 1.00121.56 B C
ANISOU 5598 CB VAL A 97 5850 34688 5649 -6495 2968 -2573 B C
ATOM 5599 CG1 VAL A 97 -30.085 5.825 4.265 1.00120.61 B C
ANISOU 5599 CG1 VAL A 97 5736 34359 5731 -6778 3039 -3372 B C
ATOM 5600 CG2 VAL A 97 -29.147 6.895 2.184 1.00121.98 B C
ANISOU 5600 CG2 VAL A 97 5937 34839 5573 -6240 2879 -2248 B C
ATOM 5601 N ILE A 98 -30.997 9.317 3.443 1.00124.32 B N
ANISOU 5601 N ILE A 98 5952 35564 5720 -5298 2497 304 B N
ATOM 5602 CA ILE A 98 -32.346 9.891 3.466 1.00125.43 B C
ANISOU 5602 CA ILE A 98 6051 35686 5921 -4923 2349 1055 B C
ATOM 5603 C ILE A 98 -33.303 8.972 2.705 1.00129.95 B C
ANISOU 5603 C ILE A 98 6929 35703 6745 -4986 2329 302 B C
ATOM 5604 O ILE A 98 -33.080 8.683 1.524 1.00130.29 B O
ANISOU 5604 O ILE A 98 7076 35688 6742 -5025 2347 4 B O
ATOM 5605 CB ILE A 98 -32.405 11.352 2.931 1.00128.35 B C
ANISOU 5605 CB ILE A 98 6523 35771 6472 -4281 2269 2402 B C
ATOM 5606 CG1 ILE A 98 -31.248 12.242 3.472 1.00128.69 B C
ANISOU 5606 CG1 ILE A 98 6534 35727 6638 -4051 2326 3174 B C
ATOM 5607 CG2 ILE A 98 -33.800 11.985 3.142 1.00128.84 B C
ANISOU 5607 CG2 ILE A 98 6540 35742 6672 -3925 2154 3136 B C
ATOM 5608 CD1 ILE A 98 -31.178 12.469 5.008 1.00134.00 B C
ANISOU 5608 CD1 ILE A 98 7345 35852 7718 -3903 2333 3473 B C
ATOM 5609 N VAL A 99 -34.365 8.520 3.396 1.00128.14 B N
ANISOU 5609 N VAL A 99 6578 35590 6520 -5119 2294 45 B N
ATOM 5610 CA VAL A 99 -35.394 7.639 2.851 1.00128.55 B C
ANISOU 5610 CA VAL A 99 6702 35482 6661 -5259 2271 -591 B C
ATOM 5611 C VAL A 99 -36.705 8.434 2.763 1.00132.88 B C
ANISOU 5611 C VAL A 99 7422 35609 7458 -4746 2101 273 B C
ATOM 5612 O VAL A 99 -37.280 8.815 3.786 1.00131.95 B O
ANISOU 5612 O VAL A 99 7158 35625 7351 -4651 2058 684 B O
ATOM 5613 CB VAL A 99 -35.553 6.321 3.670 1.00130.62 B C
ANISOU 5613 CB VAL A 99 7109 35267 7255 -5654 2411 -1714 B C
ATOM 5614 CG1 VAL A 99 -36.575 5.385 3.025 1.00130.47 B C
ANISOU 5614 CG1 VAL A 99 7121 35101 7351 -5786 2399 -2302 B C
ATOM 5615 CG2 VAL A 99 -34.215 5.607 3.850 1.00129.92 B C
ANISOU 5615 CG2 VAL A 99 7110 34972 7283 -6038 2621 -2575 B C
ATOM 5616 N GLU A 100 -37.146 8.709 1.530 1.00132.32 B N
ANISOU 5616 N GLU A 100 7405 35557 7316 -4565 2018 526 B N
ATOM 5617 CA GLU A 100 -38.382 9.428 1.239 1.00133.08 B C
ANISOU 5617 CA GLU A 100 7517 35565 7483 -4218 1878 1209 B C
ATOM 5618 C GLU A 100 -39.509 8.416 1.034 1.00136.29 B C
ANISOU 5618 C GLU A 100 8133 35490 8161 -4325 1833 527 B C
ATOM 5619 O GLU A 100 -39.344 7.491 0.237 1.00135.75 B O
ANISOU 5619 O GLU A 100 8129 35390 8059 -4558 1867 -160 B O
ATOM 5620 CB GLU A 100 -38.199 10.310 -0.019 1.00134.73 B C
ANISOU 5620 CB GLU A 100 7901 35582 7707 -3892 1833 1803 B C
ATOM 5621 CG GLU A 100 -38.918 11.648 0.025 1.00142.25 B C
ANISOU 5621 CG GLU A 100 9284 35533 9234 -3292 1771 2738 B C
ATOM 5622 CD GLU A 100 -39.978 11.913 -1.031 1.00154.80 B C
ANISOU 5622 CD GLU A 100 11791 35353 11674 -2855 1687 2648 B C
ATOM 5623 OE1 GLU A 100 -39.655 11.888 -2.240 1.00157.52 B O
ANISOU 5623 OE1 GLU A 100 12387 35413 12051 -2784 1684 2581 B O
ATOM 5624 OE2 GLU A 100 -41.139 12.159 -0.638 1.00143.50 B O1-
ANISOU 5624 OE2 GLU A 100 9878 34726 9921 -2918 1591 2923 B O1-
ATOM 5625 N ILE A 101 -40.625 8.543 1.781 1.00134.88 B N
ANISOU 5625 N ILE A 101 7800 35441 8008 -4277 1766 733 B N
ATOM 5626 CA ILE A 101 -41.759 7.617 1.645 1.00135.36 B C
ANISOU 5626 CA ILE A 101 7875 35380 8176 -4444 1723 148 B C
ATOM 5627 C ILE A 101 -43.060 8.400 1.443 1.00139.32 B C
ANISOU 5627 C ILE A 101 8533 35480 8923 -4038 1575 817 B C
ATOM 5628 O ILE A 101 -43.380 9.295 2.230 1.00138.65 B O
ANISOU 5628 O ILE A 101 8333 35484 8864 -3814 1545 1501 B O
ATOM 5629 CB ILE A 101 -41.902 6.594 2.816 1.00137.01 B C
ANISOU 5629 CB ILE A 101 8125 35296 8635 -4729 1829 -595 B C
ATOM 5630 CG1 ILE A 101 -40.592 5.813 3.068 1.00136.94 B C
ANISOU 5630 CG1 ILE A 101 8201 35139 8690 -5050 2005 -1335 B C
ATOM 5631 CG2 ILE A 101 -43.075 5.617 2.553 1.00137.86 B C
ANISOU 5631 CG2 ILE A 101 8267 35198 8918 -4874 1798 -1163 B C
ATOM 5632 CD1 ILE A 101 -40.529 5.100 4.401 1.00142.98 B C
ANISOU 5632 CD1 ILE A 101 9246 35104 9977 -5152 2129 -1868 B C
ATOM 5633 N ASP A 102 -43.813 8.031 0.393 1.00138.22 B N
ANISOU 5633 N ASP A 102 8388 35424 8704 -4077 1488 612 B N
ATOM 5634 CA ASP A 102 -45.111 8.619 0.090 1.00138.97 B C
ANISOU 5634 CA ASP A 102 8481 35447 8873 -3827 1348 1092 B C
ATOM 5635 C ASP A 102 -46.197 7.640 0.526 1.00142.06 B C
ANISOU 5635 C ASP A 102 8964 35454 9557 -3959 1325 523 B C
ATOM 5636 O ASP A 102 -46.300 6.538 -0.017 1.00141.71 B O
ANISOU 5636 O ASP A 102 8950 35369 9526 -4217 1344 -184 B O
ATOM 5637 CB ASP A 102 -45.227 8.981 -1.402 1.00140.95 B C
ANISOU 5637 CB ASP A 102 8951 35471 9133 -3646 1262 1273 B C
ATOM 5638 CG ASP A 102 -44.346 10.136 -1.833 1.00147.05 B C
ANISOU 5638 CG ASP A 102 10154 35517 10200 -3255 1295 1872 B C
ATOM 5639 OD1 ASP A 102 -44.407 11.208 -1.182 1.00147.26 B O
ANISOU 5639 OD1 ASP A 102 10147 35477 10328 -3002 1302 2560 B O
ATOM 5640 OD2 ASP A 102 -43.636 9.989 -2.849 1.00150.03 B O1-
ANISOU 5640 OD2 ASP A 102 10842 35499 10663 -3224 1321 1673 B O1-
ATOM 5641 N SER A 103 -46.964 8.027 1.553 1.00140.00 B N
ANISOU 5641 N SER A 103 8480 35434 9280 -3900 1298 863 B N
ATOM 5642 CA SER A 103 -48.027 7.209 2.121 1.00140.07 B C
ANISOU 5642 CA SER A 103 8404 35400 9418 -4076 1287 404 B C
ATOM 5643 C SER A 103 -49.353 7.978 2.195 1.00143.86 B C
ANISOU 5643 C SER A 103 9001 35482 10176 -3720 1157 993 B C
ATOM 5644 O SER A 103 -49.409 9.163 1.865 1.00143.84 B O
ANISOU 5644 O SER A 103 9020 35479 10153 -3404 1092 1745 B O
ATOM 5645 CB SER A 103 -47.625 6.707 3.511 1.00141.67 B C
ANISOU 5645 CB SER A 103 8633 35395 9800 -4244 1423 37 B C
ATOM 5646 OG SER A 103 -47.646 7.729 4.496 1.00147.38 B O
ANISOU 5646 OG SER A 103 9572 35575 10852 -3868 1418 741 B O
ATOM 5647 N VAL A 104 -50.423 7.277 2.597 1.00142.20 B N
ANISOU 5647 N VAL A 104 8620 35420 9991 -3897 1133 630 B N
ATOM 5648 CA VAL A 104 -51.760 7.820 2.827 1.00142.66 B C
ANISOU 5648 CA VAL A 104 8603 35432 10167 -3686 1024 1074 B C
ATOM 5649 C VAL A 104 -52.433 6.941 3.894 1.00145.07 B C
ANISOU 5649 C VAL A 104 8940 35422 10759 -3848 1087 575 B C
ATOM 5650 O VAL A 104 -52.311 5.711 3.861 1.00144.22 B O
ANISOU 5650 O VAL A 104 8820 35304 10671 -4184 1165 -219 B O
ATOM 5651 CB VAL A 104 -52.629 8.031 1.545 1.00146.29 B C
ANISOU 5651 CB VAL A 104 9293 35486 10805 -3487 874 1188 B C
ATOM 5652 CG1 VAL A 104 -52.970 6.722 0.837 1.00146.47 B C
ANISOU 5652 CG1 VAL A 104 9352 35450 10852 -3769 857 412 B C
ATOM 5653 CG2 VAL A 104 -53.892 8.835 1.849 1.00146.59 B C
ANISOU 5653 CG2 VAL A 104 9251 35473 10973 -3236 772 1738 B C
ATOM 5654 N THR A 105 -53.092 7.591 4.865 1.00143.33 B N
ANISOU 5654 N THR A 105 8511 35427 10520 -3711 1068 1080 B N
ATOM 5655 CA THR A 105 -53.812 6.939 5.959 1.00143.27 B C
ANISOU 5655 CA THR A 105 8385 35415 10635 -3882 1127 734 B C
ATOM 5656 C THR A 105 -55.139 6.365 5.457 1.00146.96 B C
ANISOU 5656 C THR A 105 8981 35459 11398 -3870 1037 437 B C
ATOM 5657 O THR A 105 -55.586 6.675 4.347 1.00147.22 B O
ANISOU 5657 O THR A 105 9059 35476 11403 -3733 908 643 B O
ATOM 5658 CB THR A 105 -54.075 7.934 7.127 1.00148.43 B C
ANISOU 5658 CB THR A 105 9224 35523 11650 -3504 1139 1433 B C
ATOM 5659 CG2 THR A 105 -52.810 8.575 7.667 1.00146.06 B C
ANISOU 5659 CG2 THR A 105 8864 35457 11176 -3443 1220 1833 B C
ATOM 5660 OG1 THR A 105 -55.003 8.945 6.724 1.00149.10 B O
ANISOU 5660 OG1 THR A 105 9309 35504 11838 -3161 1014 2127 B O
ATOM 5661 N SER A 106 -55.769 5.540 6.289 1.00144.64 B N
ANISOU 5661 N SER A 106 8483 35359 11115 -4138 1111 -36 B N
ATOM 5662 CA SER A 106 -57.097 5.006 6.038 1.00145.11 B C
ANISOU 5662 CA SER A 106 8485 35322 11329 -4192 1040 -272 B C
ATOM 5663 C SER A 106 -58.075 5.895 6.817 1.00147.74 B C
ANISOU 5663 C SER A 106 8831 35421 11884 -3873 980 367 B C
ATOM 5664 O SER A 106 -57.661 6.418 7.860 1.00146.57 B O
ANISOU 5664 O SER A 106 8599 35416 11675 -3809 1057 689 B O
ATOM 5665 CB SER A 106 -57.173 3.546 6.482 1.00147.71 B C
ANISOU 5665 CB SER A 106 8942 35213 11967 -4508 1185 -1164 B C
ATOM 5666 OG SER A 106 -58.483 3.014 6.370 1.00156.45 B O
ANISOU 5666 OG SER A 106 10372 35400 13674 -4347 1116 -1280 B O
ATOM 5667 N PRO A 107 -59.351 6.112 6.378 1.00146.05 B N
ANISOU 5667 N PRO A 107 8449 35389 11654 -3784 847 590 B N
ATOM 5668 CA PRO A 107 -60.269 6.946 7.186 1.00145.88 B C
ANISOU 5668 CA PRO A 107 8299 35398 11732 -3541 810 1194 B C
ATOM 5669 C PRO A 107 -60.550 6.351 8.573 1.00147.43 B C
ANISOU 5669 C PRO A 107 8482 35406 12127 -3681 943 875 B C
ATOM 5670 O PRO A 107 -61.003 7.064 9.469 1.00147.43 B O
ANISOU 5670 O PRO A 107 8386 35435 12195 -3482 950 1404 B O
ATOM 5671 CB PRO A 107 -61.552 6.990 6.345 1.00147.97 B C
ANISOU 5671 CB PRO A 107 8621 35410 12191 -3413 657 1250 B C
ATOM 5672 CG PRO A 107 -61.145 6.560 4.977 1.00151.40 B C
ANISOU 5672 CG PRO A 107 9355 35461 12709 -3441 589 909 B C
ATOM 5673 CD PRO A 107 -60.028 5.596 5.171 1.00147.73 B C
ANISOU 5673 CD PRO A 107 8774 35376 11982 -3812 730 304 B C
ATOM 5674 N LYS A 108 -60.250 5.048 8.746 1.00143.92 B N
ANISOU 5674 N LYS A 108 7897 35246 11540 -4131 1066 18 B N
ATOM 5675 CA LYS A 108 -60.445 4.276 9.972 1.00143.29 B C
ANISOU 5675 CA LYS A 108 7731 35151 11562 -4387 1228 -475 B C
ATOM 5676 C LYS A 108 -59.222 4.336 10.909 1.00144.17 B C
ANISOU 5676 C LYS A 108 7979 35122 11678 -4441 1380 -555 B C
ATOM 5677 O LYS A 108 -59.264 3.739 11.989 1.00143.01 B O
ANISOU 5677 O LYS A 108 7769 34973 11596 -4695 1543 -1044 B O
ATOM 5678 CB LYS A 108 -60.786 2.815 9.612 1.00145.41 B C
ANISOU 5678 CB LYS A 108 8136 34990 12122 -4686 1309 -1380 B C
ATOM 5679 CG LYS A 108 -62.088 2.665 8.803 1.00156.73 B C
ANISOU 5679 CG LYS A 108 10092 35162 14296 -4299 1140 -1197 B C
ATOM 5680 CD LYS A 108 -63.295 2.366 9.714 1.00163.95 B C
ANISOU 5680 CD LYS A 108 11263 35201 15830 -4135 1171 -1198 B C
ATOM 5681 CE LYS A 108 -64.640 2.674 9.104 1.00173.34 B C
ANISOU 5681 CE LYS A 108 12828 35435 17598 -3729 988 -808 B C
ATOM 5682 NZ LYS A 108 -65.743 2.434 10.067 1.00179.71 B N1+
ANISOU 5682 NZ LYS A 108 13829 35503 18951 -3606 1036 -823 B N1+
ATOM 5683 N SER A 109 -58.160 5.086 10.512 1.00141.61 B N
ANISOU 5683 N SER A 109 7598 35167 11039 -4322 1336 -89 B N
ATOM 5684 CA SER A 109 -56.901 5.292 11.248 1.00140.63 B C
ANISOU 5684 CA SER A 109 7493 35162 10777 -4389 1451 -60 B C
ATOM 5685 C SER A 109 -57.150 5.386 12.758 1.00143.42 B C
ANISOU 5685 C SER A 109 7898 35252 11344 -4347 1551 33 B C
ATOM 5686 O SER A 109 -57.906 6.253 13.204 1.00143.24 B O
ANISOU 5686 O SER A 109 7758 35317 11352 -4048 1469 789 B O
ATOM 5687 CB SER A 109 -56.196 6.552 10.747 1.00142.32 B C
ANISOU 5687 CB SER A 109 7857 35250 10968 -3978 1348 823 B C
ATOM 5688 OG SER A 109 -54.894 6.705 11.284 1.00145.06 B O
ANISOU 5688 OG SER A 109 8492 35171 11453 -3942 1450 797 B O
ATOM 5689 N SER A 110 -56.568 4.440 13.528 1.00140.98 B N
ANISOU 5689 N SER A 110 7521 35091 10955 -4790 1753 -807 B N
ATOM 5690 CA SER A 110 -56.717 4.351 14.988 1.00140.63 B C
ANISOU 5690 CA SER A 110 7419 35047 10968 -4902 1885 -916 B C
ATOM 5691 C SER A 110 -56.196 5.612 15.719 1.00143.36 B C
ANISOU 5691 C SER A 110 7857 35296 11318 -4483 1812 128 B C
ATOM 5692 O SER A 110 -56.741 5.979 16.766 1.00143.76 B O
ANISOU 5692 O SER A 110 7832 35360 11431 -4365 1832 515 B O
ATOM 5693 CB SER A 110 -56.031 3.094 15.524 1.00142.12 B C
ANISOU 5693 CB SER A 110 7842 34712 11445 -5340 2157 -2102 B C
ATOM 5694 OG SER A 110 -54.671 2.995 15.135 1.00146.62 B O
ANISOU 5694 OG SER A 110 8799 34695 12217 -5288 2200 -2261 B O
ATOM 5695 N ALA A 111 -55.187 6.295 15.144 1.00139.82 B N
ANISOU 5695 N ALA A 111 7299 35269 10556 -4360 1734 648 B N
ATOM 5696 CA ALA A 111 -54.604 7.506 15.723 1.00139.30 B C
ANISOU 5696 CA ALA A 111 7188 35297 10444 -3974 1680 1754 B C
ATOM 5697 C ALA A 111 -55.488 8.748 15.586 1.00142.26 B C
ANISOU 5697 C ALA A 111 7634 35261 11156 -3363 1553 2921 B C
ATOM 5698 O ALA A 111 -55.334 9.678 16.373 1.00141.25 B O
ANISOU 5698 O ALA A 111 7439 35066 11165 -3006 1561 3894 B O
ATOM 5699 CB ALA A 111 -53.265 7.793 15.072 1.00139.49 B C
ANISOU 5699 CB ALA A 111 7334 35311 10357 -3942 1676 1843 B C
ATOM 5700 N LEU A 112 -56.366 8.801 14.580 1.00141.38 B N
ANISOU 5700 N LEU A 112 7435 35273 11008 -3315 1449 2917 B N
ATOM 5701 CA LEU A 112 -57.131 10.024 14.329 1.00142.11 B C
ANISOU 5701 CA LEU A 112 7524 35117 11354 -2817 1355 3925 B C
ATOM 5702 C LEU A 112 -58.633 9.895 14.570 1.00147.03 B C
ANISOU 5702 C LEU A 112 8264 35261 12339 -2725 1325 3799 B C
ATOM 5703 O LEU A 112 -59.178 8.799 14.537 1.00146.74 B O
ANISOU 5703 O LEU A 112 8156 35403 12198 -3089 1341 2962 B O
ATOM 5704 CB LEU A 112 -56.898 10.494 12.876 1.00142.32 B C
ANISOU 5704 CB LEU A 112 7652 35086 11337 -2690 1260 4056 B C
ATOM 5705 CG LEU A 112 -55.459 10.450 12.327 1.00145.00 B C
ANISOU 5705 CG LEU A 112 8264 35181 11647 -2741 1298 3826 B C
ATOM 5706 CD1 LEU A 112 -55.456 10.445 10.823 1.00145.35 B C
ANISOU 5706 CD1 LEU A 112 8405 35224 11597 -2768 1205 3592 B C
ATOM 5707 CD2 LEU A 112 -54.611 11.576 12.885 1.00145.76 B C
ANISOU 5707 CD2 LEU A 112 8469 34946 11969 -2360 1358 4732 B C
ATOM 5708 N GLN A 113 -59.294 11.039 14.791 1.00146.49 B N
ANISOU 5708 N GLN A 113 8119 35034 12506 -2300 1292 4757 B N
ATOM 5709 CA GLN A 113 -60.740 11.142 14.956 1.00147.90 B C
ANISOU 5709 CA GLN A 113 8257 35021 12919 -2184 1251 4854 B C
ATOM 5710 C GLN A 113 -61.237 12.277 14.060 1.00152.38 B C
ANISOU 5710 C GLN A 113 9111 34905 13883 -1787 1173 5334 B C
ATOM 5711 O GLN A 113 -60.812 13.424 14.220 1.00151.59 B O
ANISOU 5711 O GLN A 113 9063 34535 14001 -1432 1223 6146 B O
ATOM 5712 CB GLN A 113 -61.134 11.336 16.439 1.00148.69 B C
ANISOU 5712 CB GLN A 113 8330 34874 13292 -2025 1354 5267 B C
ATOM 5713 CG GLN A 113 -62.523 11.949 16.687 1.00162.25 B C
ANISOU 5713 CG GLN A 113 10712 35001 15936 -1647 1359 5224 B C
ATOM 5714 CD GLN A 113 -63.655 10.958 16.806 1.00179.33 B C
ANISOU 5714 CD GLN A 113 13631 35704 18800 -1762 1362 4010 B C
ATOM 5715 NE2 GLN A 113 -64.424 11.085 17.872 1.00172.84 B N
ANISOU 5715 NE2 GLN A 113 12383 35416 17871 -1733 1412 4461 B N
ATOM 5716 OE1 GLN A 113 -63.909 10.135 15.917 1.00178.63 B O
ANISOU 5716 OE1 GLN A 113 13434 35941 18496 -2015 1283 3460 B O
ATOM 5717 N TRP A 114 -62.122 11.931 13.111 1.00151.88 B N
ANISOU 5717 N TRP A 114 8960 35050 13697 -1912 1053 4968 B N
ATOM 5718 CA TRP A 114 -62.740 12.851 12.160 1.00152.78 B C
ANISOU 5718 CA TRP A 114 9163 34902 13983 -1644 954 5356 B C
ATOM 5719 C TRP A 114 -64.205 13.066 12.554 1.00156.48 B C
ANISOU 5719 C TRP A 114 9735 34862 14859 -1492 930 5384 B C
ATOM 5720 O TRP A 114 -65.066 12.239 12.228 1.00156.85 B O
ANISOU 5720 O TRP A 114 9690 35080 14826 -1712 853 4840 B O
ATOM 5721 CB TRP A 114 -62.623 12.315 10.718 1.00152.66 B C
ANISOU 5721 CB TRP A 114 9180 35120 13705 -1855 834 4818 B C
ATOM 5722 CG TRP A 114 -61.239 11.899 10.319 1.00153.17 B C
ANISOU 5722 CG TRP A 114 9369 35276 13554 -2027 873 4489 B C
ATOM 5723 CD1 TRP A 114 -60.673 10.670 10.488 1.00155.08 B C
ANISOU 5723 CD1 TRP A 114 9698 35533 13694 -2372 931 3693 B C
ATOM 5724 CD2 TRP A 114 -60.257 12.707 9.660 1.00152.84 B C
ANISOU 5724 CD2 TRP A 114 9453 35153 13465 -1854 872 4883 B C
ATOM 5725 CE2 TRP A 114 -59.111 11.904 9.472 1.00155.33 B C
ANISOU 5725 CE2 TRP A 114 9957 35399 13661 -2097 924 4286 B C
ATOM 5726 CE3 TRP A 114 -60.232 14.038 9.210 1.00153.69 B C
ANISOU 5726 CE3 TRP A 114 9709 34890 13796 -1494 856 5553 B C
ATOM 5727 NE1 TRP A 114 -59.392 10.666 9.988 1.00154.45 B N
ANISOU 5727 NE1 TRP A 114 9700 35566 13418 -2440 957 3618 B N
ATOM 5728 CZ2 TRP A 114 -57.955 12.383 8.846 1.00154.56 B C
ANISOU 5728 CZ2 TRP A 114 9953 35336 13436 -2027 939 4500 B C
ATOM 5729 CZ3 TRP A 114 -59.085 14.513 8.595 1.00154.44 B C
ANISOU 5729 CZ3 TRP A 114 9987 34844 13849 -1418 882 5700 B C
ATOM 5730 CH2 TRP A 114 -57.965 13.690 8.415 1.00154.67 B C
ANISOU 5730 CH2 TRP A 114 10064 35080 13625 -1679 918 5203 B C
ATOM 5731 N LEU A 115 -64.475 14.153 13.302 1.00153.97 B N
ANISOU 5731 N LEU A 115 9323 34391 14786 -1154 1003 6222 B N
ATOM 5732 CA LEU A 115 -65.821 14.489 13.766 1.00154.21 B C
ANISOU 5732 CA LEU A 115 9286 34206 15100 -999 997 6443 B C
ATOM 5733 C LEU A 115 -66.455 15.554 12.858 1.00157.11 B C
ANISOU 5733 C LEU A 115 9908 34005 15781 -732 916 6656 B C
ATOM 5734 O LEU A 115 -65.817 16.560 12.533 1.00156.32 B O
ANISOU 5734 O LEU A 115 9921 33695 15778 -510 951 7133 B O
ATOM 5735 CB LEU A 115 -65.851 14.911 15.254 1.00153.64 B C
ANISOU 5735 CB LEU A 115 9178 33860 15336 -791 1158 6994 B C
ATOM 5736 CG LEU A 115 -64.958 16.062 15.727 1.00155.97 B C
ANISOU 5736 CG LEU A 115 9781 33418 16060 -447 1300 7607 B C
ATOM 5737 CD1 LEU A 115 -65.697 16.952 16.690 1.00155.61 B C
ANISOU 5737 CD1 LEU A 115 9749 32844 16530 -116 1427 8243 B C
ATOM 5738 CD2 LEU A 115 -63.705 15.541 16.399 1.00157.37 B C
ANISOU 5738 CD2 LEU A 115 10071 33563 16161 -568 1393 7447 B C
ATOM 5739 N ASN A 116 -67.715 15.302 12.443 1.00155.31 B N
ANISOU 5739 N ASN A 116 9483 34024 15505 -786 806 6512 B N
ATOM 5740 CA ASN A 116 -68.504 16.141 11.534 1.00155.54 B C
ANISOU 5740 CA ASN A 116 9573 33843 15681 -594 701 6723 B C
ATOM 5741 C ASN A 116 -68.799 17.544 12.105 1.00157.97 B C
ANISOU 5741 C ASN A 116 10115 33399 16509 -211 807 7316 B C
ATOM 5742 O ASN A 116 -68.532 17.811 13.279 1.00156.81 B O
ANISOU 5742 O ASN A 116 9926 33092 16562 -85 964 7713 B O
ATOM 5743 CB ASN A 116 -69.817 15.432 11.177 1.00155.54 B C
ANISOU 5743 CB ASN A 116 9444 34007 15646 -754 572 6262 B C
ATOM 5744 CG ASN A 116 -69.624 14.153 10.403 1.00163.80 B C
ANISOU 5744 CG ASN A 116 11141 34170 16927 -1040 491 4999 B C
ATOM 5745 ND2 ASN A 116 -69.883 14.202 9.107 1.00156.02 B N
ANISOU 5745 ND2 ASN A 116 9843 33874 15562 -1099 332 5102 B N
ATOM 5746 OD1 ASN A 116 -69.237 13.116 10.951 1.00159.17 B O
ANISOU 5746 OD1 ASN A 116 10243 34220 16014 -1312 550 4777 B O
ATOM 5747 N LYS A 117 -69.348 18.438 11.248 1.00156.21 B N
ANISOU 5747 N LYS A 117 9865 33146 16344 -32 726 7626 B N
ATOM 5748 CA LYS A 117 -69.735 19.820 11.564 1.00155.75 B C
ANISOU 5748 CA LYS A 117 9892 32589 16697 309 818 8242 B C
ATOM 5749 C LYS A 117 -70.899 19.857 12.584 1.00158.51 B C
ANISOU 5749 C LYS A 117 10288 32524 17414 383 872 8187 B C
ATOM 5750 O LYS A 117 -71.083 20.863 13.277 1.00157.38 B O
ANISOU 5750 O LYS A 117 10182 31962 17652 648 1017 8727 B O
ATOM 5751 CB LYS A 117 -70.124 20.544 10.269 1.00158.13 B C
ANISOU 5751 CB LYS A 117 10404 32633 17045 394 681 8139 B C
ATOM 5752 CG LYS A 117 -69.982 22.058 10.321 1.00167.64 B C
ANISOU 5752 CG LYS A 117 12303 32522 18869 655 765 8097 B C
ATOM 5753 CD LYS A 117 -69.871 22.675 8.921 1.00174.93 B C
ANISOU 5753 CD LYS A 117 13752 32844 19868 660 626 7635 B C
ATOM 5754 CE LYS A 117 -71.158 22.675 8.122 1.00184.56 B C
ANISOU 5754 CE LYS A 117 15410 33422 21293 599 423 6857 B C
ATOM 5755 NZ LYS A 117 -72.187 23.579 8.702 1.00191.96 B N1+
ANISOU 5755 NZ LYS A 117 16738 33477 22719 737 434 6629 B N1+
ATOM 5756 N GLU A 118 -71.667 18.749 12.667 1.00156.98 B N
ANISOU 5756 N GLU A 118 9815 32854 16977 159 777 7822 B N
ATOM 5757 CA GLU A 118 -72.783 18.530 13.589 1.00157.14 B C
ANISOU 5757 CA GLU A 118 9703 32803 17200 179 819 7824 B C
ATOM 5758 C GLU A 118 -72.250 18.066 14.960 1.00159.17 B C
ANISOU 5758 C GLU A 118 10049 32831 17597 133 985 7783 B C
ATOM 5759 O GLU A 118 -72.908 18.290 15.979 1.00158.56 B O
ANISOU 5759 O GLU A 118 9902 32544 17801 262 1094 8060 B O
ATOM 5760 CB GLU A 118 -73.747 17.484 12.995 1.00159.24 B C
ANISOU 5760 CB GLU A 118 9892 33319 17294 -80 645 7133 B C
ATOM 5761 CG GLU A 118 -75.191 17.623 13.448 1.00167.02 B C
ANISOU 5761 CG GLU A 118 11196 33475 18791 -8 631 6739 B C
ATOM 5762 CD GLU A 118 -76.188 16.742 12.716 1.00180.95 B C
ANISOU 5762 CD GLU A 118 13597 34216 20941 -213 464 5462 B C
ATOM 5763 OE1 GLU A 118 -76.363 16.928 11.489 1.00177.00 B O
ANISOU 5763 OE1 GLU A 118 12934 34096 20223 -209 310 5551 B O
ATOM 5764 OE2 GLU A 118 -76.828 15.893 13.378 1.00175.39 B O1-
ANISOU 5764 OE2 GLU A 118 12446 34121 20074 -366 495 5472 B O1-
ATOM 5765 N GLN A 119 -71.052 17.424 14.970 1.00156.44 B N
ANISOU 5765 N GLN A 119 9581 32960 16901 -37 1011 7736 B N
ATOM 5766 CA GLN A 119 -70.348 16.902 16.153 1.00155.63 B C
ANISOU 5766 CA GLN A 119 9419 32929 16783 -104 1155 7814 B C
ATOM 5767 C GLN A 119 -69.502 17.976 16.854 1.00157.81 B C
ANISOU 5767 C GLN A 119 9998 32457 17504 201 1339 8357 B C
ATOM 5768 O GLN A 119 -69.127 17.795 18.014 1.00156.38 B O
ANISOU 5768 O GLN A 119 9760 32199 17459 246 1489 8625 B O
ATOM 5769 CB GLN A 119 -69.441 15.728 15.762 1.00156.51 B C
ANISOU 5769 CB GLN A 119 9538 33464 16465 -456 1092 7170 B C
ATOM 5770 CG GLN A 119 -70.109 14.369 15.843 1.00162.24 B C
ANISOU 5770 CG GLN A 119 10533 33823 17286 -777 1060 6113 B C
ATOM 5771 CD GLN A 119 -69.130 13.266 15.537 1.00170.34 B C
ANISOU 5771 CD GLN A 119 12137 34181 18402 -1054 1061 5070 B C
ATOM 5772 NE2 GLN A 119 -68.398 12.823 16.550 1.00163.00 B N
ANISOU 5772 NE2 GLN A 119 10852 33927 17154 -1157 1178 5372 B N
ATOM 5773 OE1 GLN A 119 -69.010 12.807 14.397 1.00166.39 B O
ANISOU 5773 OE1 GLN A 119 11441 34236 17545 -1247 941 4802 B O
ATOM 5774 N THR A 120 -69.180 19.072 16.140 1.00156.45 B N
ANISOU 5774 N THR A 120 9885 32111 17449 422 1346 8805 B N
ATOM 5775 CA THR A 120 -68.395 20.202 16.659 1.00155.79 B C
ANISOU 5775 CA THR A 120 9964 31437 17792 723 1540 9447 B C
ATOM 5776 C THR A 120 -69.313 21.170 17.416 1.00158.54 B C
ANISOU 5776 C THR A 120 10522 30966 18750 981 1666 9689 B C
ATOM 5777 O THR A 120 -70.535 20.999 17.372 1.00159.14 B O
ANISOU 5777 O THR A 120 10503 31140 18824 943 1586 9501 B O
ATOM 5778 CB THR A 120 -67.649 20.924 15.516 1.00163.13 B C
ANISOU 5778 CB THR A 120 11424 31768 18790 735 1462 9063 B C
ATOM 5779 CG2 THR A 120 -66.564 20.070 14.890 1.00162.04 B C
ANISOU 5779 CG2 THR A 120 11216 32172 18179 506 1386 8783 B C
ATOM 5780 OG1 THR A 120 -68.585 21.354 14.523 1.00165.12 B O
ANISOU 5780 OG1 THR A 120 11735 31991 19013 749 1313 8861 B O
ATOM 5781 N ALA A 121 -68.732 22.187 18.098 1.00155.01 B N
ANISOU 5781 N ALA A 121 10084 30034 18778 1283 1903 10432 B N
ATOM 5782 CA ALA A 121 -69.493 23.194 18.841 1.00154.17 B C
ANISOU 5782 CA ALA A 121 10046 29255 19278 1557 2081 10852 B C
ATOM 5783 C ALA A 121 -70.403 23.981 17.885 1.00157.32 B C
ANISOU 5783 C ALA A 121 10625 29453 19696 1587 1938 10585 B C
ATOM 5784 O ALA A 121 -69.925 24.765 17.054 1.00156.51 B O
ANISOU 5784 O ALA A 121 10616 29240 19610 1674 1927 10735 B O
ATOM 5785 CB ALA A 121 -68.555 24.124 19.595 1.00153.34 B C
ANISOU 5785 CB ALA A 121 10141 28362 19759 1798 2356 11327 B C
ATOM 5786 N GLY A 122 -71.701 23.673 17.970 1.00155.87 B N
ANISOU 5786 N GLY A 122 10200 29586 19437 1561 1859 10545 B N
ATOM 5787 CA GLY A 122 -72.756 24.254 17.146 1.00156.29 B C
ANISOU 5787 CA GLY A 122 10246 29659 19477 1610 1729 10453 B C
ATOM 5788 C GLY A 122 -72.868 23.605 15.781 1.00159.60 B C
ANISOU 5788 C GLY A 122 10724 30536 19380 1365 1445 9812 B C
ATOM 5789 O GLY A 122 -73.198 22.419 15.677 1.00159.96 B O
ANISOU 5789 O GLY A 122 10601 31106 19070 1129 1316 9400 B O
ATOM 5790 N LYS A 123 -72.583 24.395 14.724 1.00156.89 B N
ANISOU 5790 N LYS A 123 10353 30288 18971 1472 1398 10082 B N
ATOM 5791 CA LYS A 123 -72.616 24.021 13.304 1.00157.30 B C
ANISOU 5791 CA LYS A 123 10372 30812 18584 1314 1165 9725 B C
ATOM 5792 C LYS A 123 -71.802 25.071 12.530 1.00158.50 B C
ANISOU 5792 C LYS A 123 10798 30589 18835 1435 1188 9868 B C
ATOM 5793 O LYS A 123 -72.379 25.942 11.872 1.00158.53 B O
ANISOU 5793 O LYS A 123 10874 30399 18961 1560 1135 9962 B O
ATOM 5794 CB LYS A 123 -74.082 23.942 12.807 1.00159.95 B C
ANISOU 5794 CB LYS A 123 10722 31142 18910 1265 988 9326 B C
ATOM 5795 CG LYS A 123 -74.280 23.217 11.480 1.00168.90 B C
ANISOU 5795 CG LYS A 123 12324 32025 19826 985 708 8212 B C
ATOM 5796 CD LYS A 123 -75.533 23.720 10.773 1.00174.75 B C
ANISOU 5796 CD LYS A 123 13396 32221 20780 1015 543 7722 B C
ATOM 5797 CE LYS A 123 -75.998 22.796 9.677 1.00181.63 B C
ANISOU 5797 CE LYS A 123 14555 32904 21554 775 308 6791 B C
ATOM 5798 NZ LYS A 123 -76.757 21.638 10.216 1.00187.31 B N1+
ANISOU 5798 NZ LYS A 123 15406 33321 22444 601 280 6133 B N1+
ATOM 5799 N ILE A 124 -70.461 25.033 12.665 1.00154.50 B N
ANISOU 5799 N ILE A 124 10174 30302 18226 1456 1307 10253 B N
ATOM 5800 CA ILE A 124 -69.605 26.035 12.021 1.00153.46 B C
ANISOU 5800 CA ILE A 124 10184 29934 18191 1591 1369 10558 B C
ATOM 5801 C ILE A 124 -68.611 25.376 11.036 1.00154.67 B C
ANISOU 5801 C ILE A 124 10406 30476 17884 1387 1236 10207 B C
ATOM 5802 O ILE A 124 -68.663 25.690 9.844 1.00154.97 B O
ANISOU 5802 O ILE A 124 10512 30635 17737 1369 1103 10094 B O
ATOM 5803 CB ILE A 124 -68.876 26.943 13.073 1.00154.49 B C
ANISOU 5803 CB ILE A 124 10548 29276 18877 1785 1639 10905 B C
ATOM 5804 CG1 ILE A 124 -69.831 27.483 14.189 1.00154.42 B C
ANISOU 5804 CG1 ILE A 124 10549 28752 19373 1958 1788 11121 B C
ATOM 5805 CG2 ILE A 124 -68.071 28.077 12.413 1.00154.54 B C
ANISOU 5805 CG2 ILE A 124 10764 28921 19034 1904 1707 11110 B C
ATOM 5806 CD1 ILE A 124 -70.985 28.490 13.754 1.00159.86 B C
ANISOU 5806 CD1 ILE A 124 11574 28882 20285 2021 1692 10780 B C
ATOM 5807 N HIS A 125 -67.705 24.498 11.530 1.00150.31 B N
ANISOU 5807 N HIS A 125 9575 30458 17079 1286 1307 10390 B N
ATOM 5808 CA HIS A 125 -66.665 23.835 10.725 1.00149.46 B C
ANISOU 5808 CA HIS A 125 9431 30848 16509 1095 1216 10169 B C
ATOM 5809 C HIS A 125 -66.306 22.422 11.265 1.00149.63 B C
ANISOU 5809 C HIS A 125 9330 31313 16209 833 1183 9767 B C
ATOM 5810 O HIS A 125 -66.553 22.167 12.446 1.00148.62 B O
ANISOU 5810 O HIS A 125 9089 31109 16271 871 1295 9929 B O
ATOM 5811 CB HIS A 125 -65.392 24.711 10.702 1.00149.20 B C
ANISOU 5811 CB HIS A 125 9581 30410 16698 1247 1376 10540 B C
ATOM 5812 CG HIS A 125 -65.481 25.913 9.814 1.00151.66 B C
ANISOU 5812 CG HIS A 125 10179 30241 17203 1381 1351 10570 B C
ATOM 5813 CD2 HIS A 125 -65.442 25.998 8.464 1.00153.56 B C
ANISOU 5813 CD2 HIS A 125 10563 30620 17163 1289 1182 10257 B C
ATOM 5814 ND1 HIS A 125 -65.604 27.187 10.338 1.00152.17 B N
ANISOU 5814 ND1 HIS A 125 10414 29589 17817 1627 1522 10940 B N
ATOM 5815 CE1 HIS A 125 -65.646 28.001 9.297 1.00152.11 B C
ANISOU 5815 CE1 HIS A 125 10509 29506 17780 1692 1458 10996 B C
ATOM 5816 NE2 HIS A 125 -65.551 27.332 8.148 1.00153.19 B N
ANISOU 5816 NE2 HIS A 125 10651 30127 17428 1500 1251 10595 B N
ATOM 5817 N PRO A 126 -65.675 21.512 10.457 1.00145.97 B N
ANISOU 5817 N PRO A 126 8623 31681 15157 594 1063 9556 B N
ATOM 5818 CA PRO A 126 -65.286 20.188 10.997 1.00144.95 B C
ANISOU 5818 CA PRO A 126 8307 32086 14683 322 1048 9197 B C
ATOM 5819 C PRO A 126 -64.057 20.260 11.922 1.00143.49 B C
ANISOU 5819 C PRO A 126 8119 31796 14606 388 1231 9552 B C
ATOM 5820 O PRO A 126 -63.477 21.332 12.102 1.00142.04 B O
ANISOU 5820 O PRO A 126 8026 31173 14770 655 1381 10142 B O
ATOM 5821 CB PRO A 126 -64.985 19.371 9.736 1.00147.04 B C
ANISOU 5821 CB PRO A 126 8661 32706 14504 32 867 8497 B C
ATOM 5822 CG PRO A 126 -64.517 20.379 8.752 1.00150.40 B C
ANISOU 5822 CG PRO A 126 9448 32598 15099 188 851 8573 B C
ATOM 5823 CD PRO A 126 -65.292 21.639 9.031 1.00147.30 B C
ANISOU 5823 CD PRO A 126 8952 31940 15077 515 930 9286 B C
ATOM 5824 N TYR A 127 -63.660 19.118 12.509 1.00139.40 B N
ANISOU 5824 N TYR A 127 7241 32047 13678 155 1235 9451 B N
ATOM 5825 CA TYR A 127 -62.532 19.053 13.439 1.00138.05 B C
ANISOU 5825 CA TYR A 127 7032 31838 13583 200 1396 9773 B C
ATOM 5826 C TYR A 127 -61.781 17.731 13.303 1.00139.61 B C
ANISOU 5826 C TYR A 127 7188 32615 13243 -198 1309 9057 B C
ATOM 5827 O TYR A 127 -62.394 16.689 13.053 1.00139.55 B O
ANISOU 5827 O TYR A 127 7035 33130 12857 -513 1179 8413 B O
ATOM 5828 CB TYR A 127 -63.063 19.194 14.871 1.00138.69 B C
ANISOU 5828 CB TYR A 127 7107 31475 14115 365 1546 10092 B C
ATOM 5829 CG TYR A 127 -62.081 19.639 15.935 1.00139.17 B C
ANISOU 5829 CG TYR A 127 7313 30929 14635 585 1772 10582 B C
ATOM 5830 CD1 TYR A 127 -62.089 20.947 16.410 1.00139.77 B C
ANISOU 5830 CD1 TYR A 127 7593 30061 15452 969 1978 11195 B C
ATOM 5831 CD2 TYR A 127 -61.281 18.714 16.605 1.00139.54 B C
ANISOU 5831 CD2 TYR A 127 7325 31239 14455 392 1796 10342 B C
ATOM 5832 CE1 TYR A 127 -61.254 21.346 17.452 1.00139.14 B C
ANISOU 5832 CE1 TYR A 127 7616 29347 15904 1190 2225 11677 B C
ATOM 5833 CE2 TYR A 127 -60.429 19.105 17.640 1.00139.19 B C
ANISOU 5833 CE2 TYR A 127 7379 30614 14894 624 2017 10870 B C
ATOM 5834 CZ TYR A 127 -60.415 20.425 18.057 1.00142.89 B C
ANISOU 5834 CZ TYR A 127 8262 29814 16216 993 2218 11240 B C
ATOM 5835 OH TYR A 127 -59.588 20.820 19.081 1.00141.33 B O
ANISOU 5835 OH TYR A 127 8162 28932 16606 1236 2476 11747 B O
ATOM 5836 N LEU A 128 -60.452 17.782 13.495 1.00136.06 B N
ANISOU 5836 N LEU A 128 6596 32456 12644 -180 1404 9428 B N
ATOM 5837 CA LEU A 128 -59.545 16.635 13.475 1.00135.65 B C
ANISOU 5837 CA LEU A 128 6450 33022 12070 -553 1355 8839 B C
ATOM 5838 C LEU A 128 -58.542 16.750 14.608 1.00136.50 B C
ANISOU 5838 C LEU A 128 6611 32830 12424 -430 1523 9226 B C
ATOM 5839 O LEU A 128 -58.000 17.830 14.847 1.00135.73 B O
ANISOU 5839 O LEU A 128 6608 32167 12796 -64 1674 9993 B O
ATOM 5840 CB LEU A 128 -58.799 16.509 12.125 1.00136.02 B C
ANISOU 5840 CB LEU A 128 6594 33322 11764 -717 1256 8451 B C
ATOM 5841 CG LEU A 128 -57.529 15.618 12.110 1.00139.26 B C
ANISOU 5841 CG LEU A 128 7194 33805 11914 -1022 1266 7771 B C
ATOM 5842 CD1 LEU A 128 -57.873 14.122 12.128 1.00139.66 B C
ANISOU 5842 CD1 LEU A 128 7140 34372 11551 -1498 1184 6768 B C
ATOM 5843 CD2 LEU A 128 -56.601 15.982 10.959 1.00141.48 B C
ANISOU 5843 CD2 LEU A 128 7724 33895 12136 -1004 1239 7660 B C
ATOM 5844 N PHE A 129 -58.282 15.627 15.288 1.00133.09 B N
ANISOU 5844 N PHE A 129 5853 33182 11534 -749 1510 8922 B N
ATOM 5845 CA PHE A 129 -57.279 15.546 16.337 1.00131.77 B C
ANISOU 5845 CA PHE A 129 5633 32957 11477 -683 1647 9294 B C
ATOM 5846 C PHE A 129 -56.697 14.138 16.376 1.00133.06 B C
ANISOU 5846 C PHE A 129 5778 33743 11036 -1235 1565 8226 B C
ATOM 5847 O PHE A 129 -57.377 13.170 16.027 1.00134.18 B O
ANISOU 5847 O PHE A 129 5867 34306 10809 -1634 1460 7311 B O
ATOM 5848 CB PHE A 129 -57.816 15.997 17.704 1.00132.58 B C
ANISOU 5848 CB PHE A 129 5776 32365 12234 -334 1815 9966 B C
ATOM 5849 CG PHE A 129 -58.822 15.101 18.381 1.00134.27 B C
ANISOU 5849 CG PHE A 129 5914 32804 12297 -573 1761 9445 B C
ATOM 5850 CD1 PHE A 129 -58.412 14.119 19.273 1.00136.37 B C
ANISOU 5850 CD1 PHE A 129 6212 33226 12375 -852 1781 8940 B C
ATOM 5851 CD2 PHE A 129 -60.185 15.286 18.183 1.00136.36 B C
ANISOU 5851 CD2 PHE A 129 6222 32848 12740 -507 1708 9345 B C
ATOM 5852 CE1 PHE A 129 -59.348 13.301 19.911 1.00137.65 B C
ANISOU 5852 CE1 PHE A 129 6298 33592 12413 -1088 1753 8440 B C
ATOM 5853 CE2 PHE A 129 -61.122 14.476 18.827 1.00138.94 B C
ANISOU 5853 CE2 PHE A 129 6536 33243 13010 -714 1678 8825 B C
ATOM 5854 CZ PHE A 129 -60.700 13.485 19.684 1.00137.55 B C
ANISOU 5854 CZ PHE A 129 6207 33536 12520 -1008 1706 8478 B C
ATOM 5855 N SER A 130 -55.425 14.045 16.774 1.00127.99 B N
ANISOU 5855 N SER A 130 4902 33579 10151 -1283 1631 8559 B N
ATOM 5856 CA SER A 130 -54.671 12.801 16.856 1.00127.28 B C
ANISOU 5856 CA SER A 130 4715 34219 9425 -1858 1584 7557 B C
ATOM 5857 C SER A 130 -54.419 12.366 18.300 1.00128.64 B C
ANISOU 5857 C SER A 130 4881 34288 9708 -1918 1675 7584 B C
ATOM 5858 O SER A 130 -54.433 13.190 19.216 1.00125.38 B O
ANISOU 5858 O SER A 130 4684 32888 10066 -1378 1809 8538 B O
ATOM 5859 CB SER A 130 -53.330 12.953 16.139 1.00129.06 B C
ANISOU 5859 CB SER A 130 5155 34314 9570 -1898 1590 7393 B C
ATOM 5860 OG SER A 130 -52.397 13.663 16.939 1.00132.20 B O
ANISOU 5860 OG SER A 130 5835 33832 10563 -1498 1728 8118 B O
ATOM 5861 N GLN A 131 -54.138 11.065 18.470 1.00123.80 B N
ANISOU 5861 N GLN A 131 4398 33959 8683 -2542 1658 6190 B N
ATOM 5862 CA GLN A 131 -53.797 10.383 19.718 1.00114.68 B C
ANISOU 5862 CA GLN A 131 4337 30819 8418 -2560 1789 5141 B C
ATOM 5863 C GLN A 131 -52.860 9.233 19.339 1.00118.93 B C
ANISOU 5863 C GLN A 131 5089 31458 8643 -3161 1831 3723 B C
ATOM 5864 O GLN A 131 -53.329 8.156 18.951 1.00121.91 B O
ANISOU 5864 O GLN A 131 5126 32707 8487 -3772 1858 2638 B O
ATOM 5865 CB GLN A 131 -55.073 9.902 20.490 1.00114.53 B C
ANISOU 5865 CB GLN A 131 4437 30426 8653 -2609 1818 4783 B C
ATOM 5866 CG GLN A 131 -54.800 9.209 21.839 1.00115.97 B C
ANISOU 5866 CG GLN A 131 5682 28636 9746 -2596 1969 3815 B C
ATOM 5867 CD GLN A 131 -53.758 9.902 22.703 1.00125.37 B C
ANISOU 5867 CD GLN A 131 7698 28110 11825 -2104 2059 4197 B C
ATOM 5868 NE2 GLN A 131 -52.717 9.174 23.079 1.00110.51 B N
ANISOU 5868 NE2 GLN A 131 6435 25336 10215 -2309 2137 3255 B N
ATOM 5869 OE1 GLN A 131 -53.868 11.085 23.045 1.00120.02 B O
ANISOU 5869 OE1 GLN A 131 7069 26903 11630 -1556 2096 5312 B O
ATOM 5870 N CYS A 132 -51.536 9.480 19.393 1.00112.93 B N
ANISOU 5870 N CYS A 132 4810 29874 8225 -3005 1877 3738 B N
ATOM 5871 CA CYS A 132 -50.524 8.507 18.981 1.00112.50 B C
ANISOU 5871 CA CYS A 132 4919 29887 7938 -3524 1950 2535 B C
ATOM 5872 C CYS A 132 -50.220 7.468 20.051 1.00108.45 B C
ANISOU 5872 C CYS A 132 5268 27751 8189 -3689 2136 1333 B C
ATOM 5873 O CYS A 132 -50.254 6.278 19.731 1.00109.83 B O
ANISOU 5873 O CYS A 132 5277 28353 8101 -4294 2270 102 B O
ATOM 5874 CB CYS A 132 -49.252 9.202 18.520 1.00112.61 B C
ANISOU 5874 CB CYS A 132 5011 29825 7951 -3301 1923 3091 B C
ATOM 5875 SG CYS A 132 -49.346 9.845 16.835 1.00127.63 B S
ANISOU 5875 SG CYS A 132 5670 34208 8617 -3452 1763 3971 B S
ATOM 5876 N GLN A 133 -49.882 7.894 21.290 1.00 96.67 B N
ANISOU 5876 N GLN A 133 4625 24457 7648 -3179 2187 1666 B N
ATOM 5877 CA GLN A 133 -49.571 6.975 22.392 1.00 89.70 B C
ANISOU 5877 CA GLN A 133 4525 22051 7505 -3257 2364 721 B C
ATOM 5878 C GLN A 133 -50.694 5.908 22.544 1.00 94.37 B C
ANISOU 5878 C GLN A 133 4893 22967 7995 -3669 2477 -125 B C
ATOM 5879 O GLN A 133 -51.870 6.265 22.508 1.00 95.02 B O
ANISOU 5879 O GLN A 133 4584 23689 7832 -3578 2380 365 B O
ATOM 5880 CB GLN A 133 -49.353 7.747 23.703 1.00 84.39 B C
ANISOU 5880 CB GLN A 133 4611 19742 7710 -2643 2374 1362 B C
ATOM 5881 CG GLN A 133 -48.718 6.909 24.821 1.00 92.40 B C
ANISOU 5881 CG GLN A 133 6419 19242 9446 -2661 2542 564 B C
ATOM 5882 CD GLN A 133 -48.544 7.660 26.111 1.00100.93 B C
ANISOU 5882 CD GLN A 133 8154 18927 11267 -2121 2551 1124 B C
ATOM 5883 NE2 GLN A 133 -47.759 7.096 27.012 1.00 86.53 B N
ANISOU 5883 NE2 GLN A 133 6955 15939 9984 -2092 2669 605 B N
ATOM 5884 OE1 GLN A 133 -49.112 8.735 26.324 1.00 96.27 B O
ANISOU 5884 OE1 GLN A 133 7467 18320 10792 -1743 2487 2012 B O
ATOM 5885 N ALA A 134 -50.345 4.604 22.607 1.00 91.20 B N
ANISOU 5885 N ALA A 134 4639 22230 7782 -4147 2718 -1381 B N
ATOM 5886 CA ALA A 134 -48.974 4.093 22.664 1.00 88.07 B C
ANISOU 5886 CA ALA A 134 4666 21051 7745 -4266 2878 -1976 B C
ATOM 5887 C ALA A 134 -48.395 3.742 21.293 1.00 98.69 B C
ANISOU 5887 C ALA A 134 5396 23733 8370 -4797 2919 -2527 B C
ATOM 5888 O ALA A 134 -47.318 4.233 20.945 1.00 96.98 B O
ANISOU 5888 O ALA A 134 5303 23469 8074 -4654 2837 -2187 B O
ATOM 5889 CB ALA A 134 -48.919 2.875 23.567 1.00 85.65 B C
ANISOU 5889 CB ALA A 134 4819 19522 8201 -4441 3201 -2932 B C
ATOM 5890 N THR A 135 -49.094 2.890 20.524 1.00102.73 B N
ANISOU 5890 N THR A 135 5223 25453 8359 -5437 3069 -3428 B N
ATOM 5891 CA THR A 135 -48.597 2.410 19.238 1.00109.77 B C
ANISOU 5891 CA THR A 135 5463 27692 8551 -6059 3175 -4182 B C
ATOM 5892 C THR A 135 -49.502 2.822 18.068 1.00124.40 B C
ANISOU 5892 C THR A 135 6290 31754 9223 -6354 2966 -3879 B C
ATOM 5893 O THR A 135 -49.708 2.012 17.163 1.00130.54 B O
ANISOU 5893 O THR A 135 6394 33758 9448 -7052 3147 -4913 B O
ATOM 5894 CB THR A 135 -48.427 0.877 19.293 1.00119.48 B C
ANISOU 5894 CB THR A 135 6680 28469 10247 -6690 3660 -5768 B C
ATOM 5895 CG2 THR A 135 -47.320 0.437 20.236 1.00110.40 B C
ANISOU 5895 CG2 THR A 135 6388 25388 10172 -6439 3896 -6012 B C
ATOM 5896 OG1 THR A 135 -49.668 0.304 19.709 1.00127.68 B O
ANISOU 5896 OG1 THR A 135 7537 29532 11444 -6874 3804 -6207 B O
ATOM 5897 N HIS A 136 -49.995 4.073 18.034 1.00123.56 B N
ANISOU 5897 N HIS A 136 6023 32151 8774 -5817 2619 -2446 B N
ATOM 5898 CA HIS A 136 -50.865 4.472 16.920 1.00132.20 B C
ANISOU 5898 CA HIS A 136 6171 35202 8858 -5984 2419 -1982 B C
ATOM 5899 C HIS A 136 -50.175 5.416 15.918 1.00135.03 B C
ANISOU 5899 C HIS A 136 6600 35606 9100 -5510 2190 -962 B C
ATOM 5900 O HIS A 136 -50.790 5.747 14.907 1.00135.51 B O
ANISOU 5900 O HIS A 136 6597 35762 9127 -5230 2026 -478 B O
ATOM 5901 CB HIS A 136 -52.199 5.092 17.375 1.00133.46 B C
ANISOU 5901 CB HIS A 136 6197 35467 9046 -5584 2244 -1059 B C
ATOM 5902 CG HIS A 136 -52.893 4.405 18.502 1.00134.11 B C
ANISOU 5902 CG HIS A 136 6652 34575 9728 -5676 2425 -1725 B C
ATOM 5903 CD2 HIS A 136 -53.598 3.247 18.563 1.00137.34 B C
ANISOU 5903 CD2 HIS A 136 7035 34804 10346 -6199 2695 -3055 B C
ATOM 5904 ND1 HIS A 136 -52.923 4.997 19.748 1.00128.94 B N
ANISOU 5904 ND1 HIS A 136 6723 32368 9902 -4990 2353 -870 B N
ATOM 5905 CE1 HIS A 136 -53.609 4.184 20.524 1.00126.22 B C
ANISOU 5905 CE1 HIS A 136 6669 31233 10056 -5153 2541 -1647 B C
ATOM 5906 NE2 HIS A 136 -54.022 3.113 19.864 1.00131.68 B N
ANISOU 5906 NE2 HIS A 136 6893 32739 10400 -5891 2771 -2972 B N
ATOM 5907 N CYS A 137 -48.899 5.791 16.132 1.00132.36 B N
ANISOU 5907 N CYS A 137 6206 35571 8514 -5591 2221 -790 B N
ATOM 5908 CA CYS A 137 -48.198 6.657 15.175 1.00132.61 B C
ANISOU 5908 CA CYS A 137 6201 35808 8375 -5220 2055 105 B C
ATOM 5909 C CYS A 137 -48.050 5.959 13.804 1.00134.27 B C
ANISOU 5909 C CYS A 137 6605 35711 8702 -5367 2084 -651 B C
ATOM 5910 O CYS A 137 -48.044 6.645 12.778 1.00133.54 B O
ANISOU 5910 O CYS A 137 6443 35826 8471 -5044 1925 68 B O
ATOM 5911 CB CYS A 137 -46.852 7.116 15.717 1.00129.45 B C
ANISOU 5911 CB CYS A 137 6209 34697 8280 -5014 2090 420 B C
ATOM 5912 SG CYS A 137 -46.121 8.486 14.788 1.00135.50 B S
ANISOU 5912 SG CYS A 137 6734 35972 8776 -4501 1910 1869 B S
ATOM 5913 N ARG A 138 -48.022 4.593 13.797 1.00131.53 B N
ANISOU 5913 N ARG A 138 6255 35294 8428 -5976 2323 -2101 B N
ATOM 5914 CA ARG A 138 -48.013 3.728 12.602 1.00131.23 B C
ANISOU 5914 CA ARG A 138 6299 35053 8511 -6169 2381 -2842 B C
ATOM 5915 C ARG A 138 -49.183 4.037 11.711 1.00133.70 B C
ANISOU 5915 C ARG A 138 6618 35307 8874 -5790 2156 -2232 B C
ATOM 5916 O ARG A 138 -49.081 3.918 10.497 1.00133.04 B O
ANISOU 5916 O ARG A 138 6550 35282 8717 -5753 2083 -2266 B O
ATOM 5917 CB ARG A 138 -48.156 2.240 12.976 1.00131.62 B C
ANISOU 5917 CB ARG A 138 6513 34451 9047 -6648 2697 -4231 B C
ATOM 5918 CG ARG A 138 -47.134 1.674 13.900 1.00137.78 B C
ANISOU 5918 CG ARG A 138 7763 34144 10444 -6794 2976 -4920 B C
ATOM 5919 CD ARG A 138 -47.751 0.606 14.779 1.00140.18 B C
ANISOU 5919 CD ARG A 138 8314 33507 11441 -6984 3253 -5758 B C
ATOM 5920 NE ARG A 138 -46.960 0.449 15.995 1.00143.98 B N
ANISOU 5920 NE ARG A 138 9180 33079 12445 -7059 3508 -6145 B N
ATOM 5921 CZ ARG A 138 -46.324 -0.662 16.343 1.00150.26 B C
ANISOU 5921 CZ ARG A 138 10572 32278 14244 -7029 3794 -6813 B C
ATOM 5922 NH1 ARG A 138 -45.597 -0.694 17.451 1.00142.55 B N1+
ANISOU 5922 NH1 ARG A 138 9472 31345 13347 -7582 4236 -7681 B N1+
ATOM 5923 NH2 ARG A 138 -46.420 -1.755 15.596 1.00135.54 B N
ANISOU 5923 NH2 ARG A 138 8227 30993 12279 -7681 4119 -7984 B N
ATOM 5924 N SER A 139 -50.332 4.361 12.337 1.00131.28 B N
ANISOU 5924 N SER A 139 6061 35367 8453 -5705 2082 -1838 B N
ATOM 5925 CA SER A 139 -51.585 4.641 11.644 1.00131.80 B C
ANISOU 5925 CA SER A 139 6037 35516 8524 -5439 1901 -1358 B C
ATOM 5926 C SER A 139 -51.547 5.991 10.917 1.00134.67 B C
ANISOU 5926 C SER A 139 6492 35811 8865 -4858 1679 -126 B C
ATOM 5927 O SER A 139 -52.490 6.291 10.189 1.00134.90 B O
ANISOU 5927 O SER A 139 6478 35859 8918 -4652 1542 223 B O
ATOM 5928 CB SER A 139 -52.767 4.584 12.609 1.00134.87 B C
ANISOU 5928 CB SER A 139 6460 35591 9194 -5337 1905 -1258 B C
ATOM 5929 OG SER A 139 -52.910 3.294 13.180 1.00141.21 B O
ANISOU 5929 OG SER A 139 7656 35383 10613 -5588 2119 -2326 B O
ATOM 5930 N ILE A 140 -50.464 6.788 11.080 1.00131.94 B N
ANISOU 5930 N ILE A 140 6037 35835 8258 -4735 1668 476 B N
ATOM 5931 CA ILE A 140 -50.327 8.070 10.384 1.00131.91 B C
ANISOU 5931 CA ILE A 140 6018 35897 8206 -4249 1522 1607 B C
ATOM 5932 C ILE A 140 -49.179 7.986 9.367 1.00134.88 B C
ANISOU 5932 C ILE A 140 6683 35941 8625 -4259 1544 1350 B C
ATOM 5933 O ILE A 140 -49.400 8.224 8.176 1.00134.94 B O
ANISOU 5933 O ILE A 140 6734 35942 8595 -4124 1452 1515 B O
ATOM 5934 CB ILE A 140 -50.157 9.298 11.334 1.00133.55 B C
ANISOU 5934 CB ILE A 140 6248 35877 8620 -3778 1502 2775 B C
ATOM 5935 CG1 ILE A 140 -51.200 9.293 12.471 1.00133.50 B C
ANISOU 5935 CG1 ILE A 140 6119 35846 8757 -3710 1504 2990 B C
ATOM 5936 CG2 ILE A 140 -50.198 10.625 10.533 1.00134.26 B C
ANISOU 5936 CG2 ILE A 140 6398 35749 8865 -3255 1411 3857 B C
ATOM 5937 CD1 ILE A 140 -51.016 10.370 13.548 1.00133.55 B C
ANISOU 5937 CD1 ILE A 140 6142 35545 9055 -3255 1524 4123 B C
ATOM 5938 N ILE A 141 -47.957 7.679 9.844 1.00132.24 B N
ANISOU 5938 N ILE A 141 6275 35885 8086 -4542 1664 985 B N
ATOM 5939 CA ILE A 141 -46.744 7.635 9.021 1.00132.02 B C
ANISOU 5939 CA ILE A 141 6350 35875 7937 -4622 1701 790 B C
ATOM 5940 C ILE A 141 -45.928 6.336 9.246 1.00133.29 B C
ANISOU 5940 C ILE A 141 6709 35702 8233 -5115 1896 -489 B C
ATOM 5941 O ILE A 141 -45.978 5.779 10.346 1.00131.57 B O
ANISOU 5941 O ILE A 141 6415 35528 8046 -5426 2029 -1041 B O
ATOM 5942 CB ILE A 141 -45.853 8.893 9.302 1.00134.27 B C
ANISOU 5942 CB ILE A 141 6735 35961 8319 -4189 1672 1851 B C
ATOM 5943 CG1 ILE A 141 -45.466 9.006 10.805 1.00134.35 B C
ANISOU 5943 CG1 ILE A 141 6686 35977 8383 -4224 1746 2026 B C
ATOM 5944 CG2 ILE A 141 -46.503 10.192 8.757 1.00135.29 B C
ANISOU 5944 CG2 ILE A 141 6883 35904 8617 -3627 1547 3016 B C
ATOM 5945 CD1 ILE A 141 -44.327 9.859 11.100 1.00140.63 B C
ANISOU 5945 CD1 ILE A 141 7751 36208 9473 -3857 1768 2755 B C
ATOM 5946 N PRO A 142 -45.156 5.852 8.231 1.00131.04 B N
ANISOU 5946 N PRO A 142 6432 35557 7800 -5338 1949 -1014 B N
ATOM 5947 CA PRO A 142 -44.288 4.681 8.475 1.00130.39 B C
ANISOU 5947 CA PRO A 142 6462 35218 7863 -5828 2182 -2199 B C
ATOM 5948 C PRO A 142 -43.097 5.112 9.341 1.00132.97 B C
ANISOU 5948 C PRO A 142 6945 35306 8273 -5799 2264 -2039 B C
ATOM 5949 O PRO A 142 -42.456 6.120 9.044 1.00132.57 B O
ANISOU 5949 O PRO A 142 6839 35533 7998 -5515 2156 -1199 B O
ATOM 5950 CB PRO A 142 -43.879 4.233 7.068 1.00131.74 B C
ANISOU 5950 CB PRO A 142 6800 35156 8097 -5834 2173 -2504 B C
ATOM 5951 CG PRO A 142 -43.981 5.459 6.225 1.00135.30 B C
ANISOU 5951 CG PRO A 142 7369 35556 8484 -5287 1953 -1381 B C
ATOM 5952 CD PRO A 142 -44.966 6.400 6.868 1.00132.55 B C
ANISOU 5952 CD PRO A 142 6734 35689 7939 -5043 1824 -517 B C
ATOM 5953 N CYS A 143 -42.846 4.398 10.449 1.00131.18 B N
ANISOU 5953 N CYS A 143 6683 35008 8151 -6239 2484 -2882 B N
ATOM 5954 CA CYS A 143 -41.804 4.771 11.417 1.00131.06 B C
ANISOU 5954 CA CYS A 143 6694 35016 8087 -6352 2581 -2842 B C
ATOM 5955 C CYS A 143 -41.340 3.590 12.261 1.00132.43 B C
ANISOU 5955 C CYS A 143 7123 34432 8762 -6864 2938 -4214 B C
ATOM 5956 O CYS A 143 -41.921 2.508 12.200 1.00132.13 B O
ANISOU 5956 O CYS A 143 7177 33911 9115 -7097 3115 -5083 B O
ATOM 5957 CB CYS A 143 -42.337 5.884 12.323 1.00131.83 B C
ANISOU 5957 CB CYS A 143 6649 35417 8024 -5965 2396 -1664 B C
ATOM 5958 SG CYS A 143 -43.895 5.479 13.161 1.00134.84 B S
ANISOU 5958 SG CYS A 143 7097 35418 8720 -5929 2403 -1835 B S
ATOM 5959 N GLN A 144 -40.316 3.831 13.101 1.00128.38 B N
ANISOU 5959 N GLN A 144 6544 34129 8106 -7182 3102 -4475 B N
ATOM 5960 CA GLN A 144 -39.863 2.897 14.124 1.00121.31 B C
ANISOU 5960 CA GLN A 144 6427 31311 8355 -7209 3422 -5379 B C
ATOM 5961 C GLN A 144 -40.723 3.244 15.336 1.00119.59 B C
ANISOU 5961 C GLN A 144 6731 29964 8742 -6645 3280 -4683 B C
ATOM 5962 O GLN A 144 -40.315 4.050 16.177 1.00112.39 B O
ANISOU 5962 O GLN A 144 6501 27796 8406 -5966 3102 -3730 B O
ATOM 5963 CB GLN A 144 -38.358 3.040 14.395 1.00116.57 B C
ANISOU 5963 CB GLN A 144 6477 29448 8368 -6942 3480 -5283 B C
ATOM 5964 CG GLN A 144 -37.451 2.448 13.321 1.00121.33 B C
ANISOU 5964 CG GLN A 144 6642 30890 8566 -7565 3720 -6227 B C
ATOM 5965 CD GLN A 144 -35.998 2.579 13.707 1.00119.17 B C
ANISOU 5965 CD GLN A 144 7058 29238 8984 -7252 3775 -6082 B C
ATOM 5966 NE2 GLN A 144 -35.301 1.454 13.762 1.00109.37 B N
ANISOU 5966 NE2 GLN A 144 5971 27233 8352 -7673 4207 -7281 B N
ATOM 5967 OE1 GLN A 144 -35.488 3.675 13.981 1.00104.29 B O
ANISOU 5967 OE1 GLN A 144 5544 26925 7158 -6637 3474 -4911 B O
ATOM 5968 N ASP A 145 -41.972 2.744 15.351 1.00119.35 B N
ANISOU 5968 N ASP A 145 6296 30565 8488 -6941 3347 -5112 B N
ATOM 5969 CA ASP A 145 -42.943 3.097 16.378 1.00114.92 B C
ANISOU 5969 CA ASP A 145 6104 29197 8364 -6456 3205 -4444 B C
ATOM 5970 C ASP A 145 -42.647 2.390 17.709 1.00110.68 B C
ANISOU 5970 C ASP A 145 6433 26583 9036 -6256 3455 -4923 B C
ATOM 5971 O ASP A 145 -43.441 1.581 18.197 1.00110.73 B O
ANISOU 5971 O ASP A 145 6447 26225 9401 -6456 3666 -5552 B O
ATOM 5972 CB ASP A 145 -44.382 2.837 15.890 1.00123.91 B C
ANISOU 5972 CB ASP A 145 6463 31821 8798 -6838 3178 -4687 B C
ATOM 5973 CG ASP A 145 -45.468 3.561 16.673 1.00131.02 B C
ANISOU 5973 CG ASP A 145 7551 32357 9874 -6279 2935 -3651 B C
ATOM 5974 OD1 ASP A 145 -45.173 4.616 17.266 1.00126.58 B O
ANISOU 5974 OD1 ASP A 145 7493 30914 9686 -5582 2716 -2467 B O
ATOM 5975 OD2 ASP A 145 -46.619 3.098 16.655 1.00139.57 B O1-
ANISOU 5975 OD2 ASP A 145 8226 34085 10720 -6565 2990 -4048 B O1-
ATOM 5976 N THR A 146 -41.494 2.742 18.296 1.00100.05 B N
ANISOU 5976 N THR A 146 5777 23938 8299 -5838 3429 -4541 B N
ATOM 5977 CA THR A 146 -40.989 2.265 19.582 1.00 92.64 B C
ANISOU 5977 CA THR A 146 5651 21099 8447 -5544 3615 -4728 B C
ATOM 5978 C THR A 146 -40.382 3.460 20.342 1.00 89.55 B C
ANISOU 5978 C THR A 146 5888 19762 8374 -4812 3322 -3552 B C
ATOM 5979 O THR A 146 -39.569 4.193 19.768 1.00 88.56 B O
ANISOU 5979 O THR A 146 5704 20018 7927 -4685 3167 -3068 B O
ATOM 5980 CB THR A 146 -40.001 1.073 19.442 1.00101.93 B C
ANISOU 5980 CB THR A 146 6903 21696 10131 -5984 4047 -5870 B C
ATOM 5981 CG2 THR A 146 -38.860 1.327 18.441 1.00103.96 B C
ANISOU 5981 CG2 THR A 146 6939 22618 9943 -6185 4020 -5964 B C
ATOM 5982 OG1 THR A 146 -39.450 0.778 20.732 1.00 94.44 B O
ANISOU 5982 OG1 THR A 146 6710 18975 10198 -5584 4179 -5755 B O
ATOM 5983 N PRO A 147 -40.760 3.672 21.629 1.00 80.74 B N
ANISOU 5983 N PRO A 147 5338 17443 7897 -4352 3276 -3120 B N
ATOM 5984 CA PRO A 147 -40.218 4.825 22.383 1.00 75.21 B C
ANISOU 5984 CA PRO A 147 5171 15890 7516 -3719 3053 -2125 B C
ATOM 5985 C PRO A 147 -38.686 4.800 22.584 1.00 76.08 B C
ANISOU 5985 C PRO A 147 5722 15160 8027 -3608 3120 -2227 B C
ATOM 5986 O PRO A 147 -38.104 5.782 23.051 1.00 71.47 B O
ANISOU 5986 O PRO A 147 5498 14006 7651 -3157 2964 -1500 B O
ATOM 5987 CB PRO A 147 -40.965 4.742 23.721 1.00 72.59 B C
ANISOU 5987 CB PRO A 147 5272 14550 7761 -3405 3071 -1947 B C
ATOM 5988 CG PRO A 147 -41.383 3.308 23.843 1.00 78.43 B C
ANISOU 5988 CG PRO A 147 5907 15138 8753 -3832 3375 -2946 B C
ATOM 5989 CD PRO A 147 -41.727 2.908 22.448 1.00 81.12 B C
ANISOU 5989 CD PRO A 147 5509 16927 8386 -4408 3447 -3530 B C
ATOM 5990 N SER A 148 -38.041 3.693 22.177 1.00 74.93 B N
ANISOU 5990 N SER A 148 5483 14985 8003 -4047 3389 -3153 B N
ATOM 5991 CA SER A 148 -36.600 3.460 22.222 1.00 72.78 B C
ANISOU 5991 CA SER A 148 5522 14037 8093 -4037 3506 -3383 B C
ATOM 5992 C SER A 148 -35.856 4.343 21.204 1.00 80.19 B C
ANISOU 5992 C SER A 148 6228 15781 8460 -4025 3318 -2967 B C
ATOM 5993 O SER A 148 -34.658 4.597 21.377 1.00 77.71 B O
ANISOU 5993 O SER A 148 6257 14843 8427 -3840 3309 -2817 B O
ATOM 5994 CB SER A 148 -36.325 1.990 21.929 1.00 79.16 B C
ANISOU 5994 CB SER A 148 6143 14713 9219 -4568 3929 -4523 B C
ATOM 5995 OG SER A 148 -34.954 1.738 21.685 1.00 85.19 B O
ANISOU 5995 OG SER A 148 7074 15038 10258 -4632 4071 -4785 B O
ATOM 5996 N VAL A 149 -36.555 4.763 20.119 1.00 81.37 B N
ANISOU 5996 N VAL A 149 5738 17386 7791 -4239 3185 -2776 B N
ATOM 5997 CA VAL A 149 -36.003 5.602 19.047 1.00 83.14 B C
ANISOU 5997 CA VAL A 149 5604 18596 7390 -4233 3022 -2277 B C
ATOM 5998 C VAL A 149 -36.549 7.022 19.218 1.00 84.47 B C
ANISOU 5998 C VAL A 149 5740 18945 7410 -3695 2751 -1011 B C
ATOM 5999 O VAL A 149 -37.763 7.231 19.158 1.00 86.54 B O
ANISOU 5999 O VAL A 149 5654 19862 7364 -3674 2664 -690 B O
ATOM 6000 CB VAL A 149 -36.290 5.025 17.624 1.00 94.64 B C
ANISOU 6000 CB VAL A 149 6239 21732 7988 -4888 3113 -2934 B C
ATOM 6001 CG1 VAL A 149 -35.766 5.952 16.525 1.00 98.10 B C
ANISOU 6001 CG1 VAL A 149 6249 23303 7721 -4843 2933 -2274 B C
ATOM 6002 CG2 VAL A 149 -35.694 3.636 17.457 1.00 95.55 B C
ANISOU 6002 CG2 VAL A 149 6352 21541 8412 -5448 3490 -4266 B C
ATOM 6003 N LYS A 150 -35.652 7.986 19.450 1.00 76.63 B N
ANISOU 6003 N LYS A 150 5082 17323 6711 -3266 2665 -314 B N
ATOM 6004 CA LYS A 150 -36.031 9.386 19.625 1.00 76.28 B C
ANISOU 6004 CA LYS A 150 4987 17272 6724 -2743 2520 880 B C
ATOM 6005 C LYS A 150 -35.439 10.222 18.492 1.00 84.38 B C
ANISOU 6005 C LYS A 150 5549 19247 7267 -2687 2458 1542 B C
ATOM 6006 O LYS A 150 -34.250 10.118 18.179 1.00 83.66 B O
ANISOU 6006 O LYS A 150 5617 18948 7223 -2772 2505 1283 B O
ATOM 6007 CB LYS A 150 -35.626 9.910 21.009 1.00 72.30 B C
ANISOU 6007 CB LYS A 150 5212 15169 7088 -2270 2546 1163 B C
ATOM 6008 CG LYS A 150 -36.526 9.373 22.125 1.00 66.61 B C
ANISOU 6008 CG LYS A 150 4815 13735 6759 -2229 2581 837 B C
ATOM 6009 CD LYS A 150 -36.740 10.385 23.236 1.00 69.34 B C
ANISOU 6009 CD LYS A 150 5524 13139 7684 -1718 2569 1525 B C
ATOM 6010 CE LYS A 150 -35.708 10.275 24.328 1.00 65.89 B C
ANISOU 6010 CE LYS A 150 5746 11409 7879 -1551 2635 1235 B C
ATOM 6011 NZ LYS A 150 -36.098 11.030 25.548 1.00 64.38 B N1+
ANISOU 6011 NZ LYS A 150 5873 10365 8223 -1165 2665 1656 B N1+
ATOM 6012 N PHE A 151 -36.300 10.990 17.819 1.00 85.50 B N
ANISOU 6012 N PHE A 151 5047 20528 6913 -2559 2369 2418 B N
ATOM 6013 CA PHE A 151 -35.923 11.797 16.660 1.00 89.57 B C
ANISOU 6013 CA PHE A 151 4955 22186 6889 -2490 2326 3216 B C
ATOM 6014 C PHE A 151 -36.489 13.205 16.740 1.00 92.85 B C
ANISOU 6014 C PHE A 151 5092 22639 7547 -1913 2330 4652 B C
ATOM 6015 O PHE A 151 -37.505 13.441 17.398 1.00 92.55 B O
ANISOU 6015 O PHE A 151 5092 22271 7801 -1692 2332 4985 B O
ATOM 6016 CB PHE A 151 -36.415 11.119 15.360 1.00 99.28 B C
ANISOU 6016 CB PHE A 151 5346 25356 7020 -3060 2264 2816 B C
ATOM 6017 CG PHE A 151 -37.916 10.923 15.280 1.00105.16 B C
ANISOU 6017 CG PHE A 151 5597 27017 7341 -3177 2192 2935 B C
ATOM 6018 CD1 PHE A 151 -38.510 9.761 15.761 1.00106.60 B C
ANISOU 6018 CD1 PHE A 151 5986 26921 7597 -3561 2246 1832 B C
ATOM 6019 CD2 PHE A 151 -38.734 11.902 14.726 1.00113.34 B C
ANISOU 6019 CD2 PHE A 151 5921 29190 7955 -2889 2102 4198 B C
ATOM 6020 CE1 PHE A 151 -39.899 9.588 15.702 1.00111.54 B C
ANISOU 6020 CE1 PHE A 151 6154 28382 7845 -3675 2185 1919 B C
ATOM 6021 CE2 PHE A 151 -40.125 11.743 14.700 1.00119.97 B C
ANISOU 6021 CE2 PHE A 151 6299 30862 8424 -2975 2031 4348 B C
ATOM 6022 CZ PHE A 151 -40.697 10.580 15.174 1.00115.91 B C
ANISOU 6022 CZ PHE A 151 6028 30075 7939 -3387 2058 3164 B C
ATOM 6023 N THR A 152 -35.837 14.119 16.035 1.00 90.33 B N
ANISOU 6023 N THR A 152 4441 22739 7141 -1679 2372 5507 B N
ATOM 6024 CA THR A 152 -36.205 15.523 15.852 1.00 93.15 B C
ANISOU 6024 CA THR A 152 4359 23262 7770 -1130 2474 7006 B C
ATOM 6025 C THR A 152 -37.099 15.621 14.612 1.00106.37 B C
ANISOU 6025 C THR A 152 4968 27015 8433 -1274 2371 7715 B C
ATOM 6026 O THR A 152 -37.017 14.741 13.750 1.00108.93 B O
ANISOU 6026 O THR A 152 4915 28650 7821 -1821 2239 7001 B O
ATOM 6027 CB THR A 152 -34.939 16.382 15.706 1.00 93.52 B C
ANISOU 6027 CB THR A 152 4568 22667 8298 -827 2626 7519 B C
ATOM 6028 CG2 THR A 152 -34.415 16.866 17.033 1.00 78.49 B C
ANISOU 6028 CG2 THR A 152 3455 18809 7560 -450 2804 7461 B C
ATOM 6029 OG1 THR A 152 -33.933 15.747 14.905 1.00 93.90 B O
ANISOU 6029 OG1 THR A 152 4644 23222 7812 -1233 2547 6782 B O
ATOM 6030 N TYR A 153 -37.965 16.652 14.514 1.00108.26 B N
ANISOU 6030 N TYR A 153 4661 27622 8851 -815 2461 9082 B N
ATOM 6031 CA TYR A 153 -38.795 16.758 13.317 1.00117.85 B C
ANISOU 6031 CA TYR A 153 4768 30971 9038 -935 2354 9870 B C
ATOM 6032 C TYR A 153 -39.138 18.195 12.928 1.00126.01 B C
ANISOU 6032 C TYR A 153 5486 31789 10605 -328 2543 11319 B C
ATOM 6033 O TYR A 153 -39.068 19.123 13.735 1.00124.20 B O
ANISOU 6033 O TYR A 153 5283 30557 11349 230 2813 12345 B O
ATOM 6034 CB TYR A 153 -40.080 15.895 13.410 1.00120.14 B C
ANISOU 6034 CB TYR A 153 4834 32060 8752 -1304 2183 9253 B C
ATOM 6035 CG TYR A 153 -41.262 16.470 14.161 1.00121.07 B C
ANISOU 6035 CG TYR A 153 4919 31627 9454 -883 2260 10018 B C
ATOM 6036 CD1 TYR A 153 -42.171 17.316 13.526 1.00125.55 B C
ANISOU 6036 CD1 TYR A 153 5224 32343 10137 -578 2292 10775 B C
ATOM 6037 CD2 TYR A 153 -41.577 16.029 15.441 1.00114.53 B C
ANISOU 6037 CD2 TYR A 153 4927 29246 9342 -875 2282 9193 B C
ATOM 6038 CE1 TYR A 153 -43.302 17.794 14.185 1.00125.84 B C
ANISOU 6038 CE1 TYR A 153 5281 31805 10728 -247 2372 11304 B C
ATOM 6039 CE2 TYR A 153 -42.714 16.487 16.107 1.00115.67 B C
ANISOU 6039 CE2 TYR A 153 5013 28971 9965 -543 2356 9805 B C
ATOM 6040 CZ TYR A 153 -43.573 17.370 15.473 1.00128.15 B C
ANISOU 6040 CZ TYR A 153 5683 31661 11345 -209 2418 11258 B C
ATOM 6041 OH TYR A 153 -44.688 17.832 16.117 1.00126.99 B O
ANISOU 6041 OH TYR A 153 5475 31042 11734 119 2522 11851 B O
ATOM 6042 N TYR A 154 -39.503 18.340 11.653 1.00126.12 B N
ANISOU 6042 N TYR A 154 5514 32196 10210 -474 2434 10989 B N
ATOM 6043 CA TYR A 154 -39.994 19.546 11.006 1.00127.18 B C
ANISOU 6043 CA TYR A 154 5822 31635 10864 -97 2537 11534 B C
ATOM 6044 C TYR A 154 -41.184 19.140 10.164 1.00133.02 B C
ANISOU 6044 C TYR A 154 6828 32488 11226 -375 2325 10625 B C
ATOM 6045 O TYR A 154 -41.097 18.157 9.428 1.00133.68 B O
ANISOU 6045 O TYR A 154 6884 33310 10597 -827 2157 9720 B O
ATOM 6046 CB TYR A 154 -38.915 20.233 10.142 1.00128.06 B C
ANISOU 6046 CB TYR A 154 6097 31438 11122 10 2636 11697 B C
ATOM 6047 CG TYR A 154 -39.328 21.629 9.716 1.00129.05 B C
ANISOU 6047 CG TYR A 154 6438 30666 11928 407 2788 12277 B C
ATOM 6048 CD1 TYR A 154 -38.942 22.747 10.451 1.00129.57 B C
ANISOU 6048 CD1 TYR A 154 6669 29550 13011 856 3085 13009 B C
ATOM 6049 CD2 TYR A 154 -40.152 21.829 8.609 1.00129.92 B C
ANISOU 6049 CD2 TYR A 154 6633 31007 11724 305 2649 11976 B C
ATOM 6050 CE1 TYR A 154 -39.345 24.030 10.083 1.00129.34 B C
ANISOU 6050 CE1 TYR A 154 6785 28794 13563 1149 3233 13448 B C
ATOM 6051 CE2 TYR A 154 -40.581 23.106 8.246 1.00130.07 B C
ANISOU 6051 CE2 TYR A 154 6804 30315 12301 624 2773 12480 B C
ATOM 6052 CZ TYR A 154 -40.166 24.205 8.981 1.00132.03 B C
ANISOU 6052 CZ TYR A 154 7298 29356 13510 991 3042 12999 B C
ATOM 6053 OH TYR A 154 -40.584 25.466 8.631 1.00128.90 B O
ANISOU 6053 OH TYR A 154 6906 28462 13606 1275 3186 13562 B O
ATOM 6054 N SER A 155 -42.289 19.877 10.250 1.00131.91 B N
ANISOU 6054 N SER A 155 6670 31976 11473 -90 2366 11132 B N
ATOM 6055 CA SER A 155 -43.448 19.530 9.442 1.00133.23 B C
ANISOU 6055 CA SER A 155 6876 32503 11242 -298 2179 10565 B C
ATOM 6056 C SER A 155 -44.091 20.731 8.770 1.00138.26 B C
ANISOU 6056 C SER A 155 7934 32173 12425 -14 2220 10725 B C
ATOM 6057 O SER A 155 -44.033 21.851 9.278 1.00138.32 B O
ANISOU 6057 O SER A 155 8040 31372 13143 363 2410 11427 B O
ATOM 6058 CB SER A 155 -44.497 18.804 10.278 1.00135.54 B C
ANISOU 6058 CB SER A 155 7162 32835 11501 -427 2094 10187 B C
ATOM 6059 OG SER A 155 -45.110 19.682 11.207 1.00140.18 B O
ANISOU 6059 OG SER A 155 8027 32285 12949 -29 2238 10692 B O
ATOM 6060 N GLN A 156 -44.710 20.469 7.617 1.00136.89 B N
ANISOU 6060 N GLN A 156 7711 32527 11772 -203 2060 10329 B N
ATOM 6061 CA GLN A 156 -45.515 21.398 6.835 1.00137.10 B C
ANISOU 6061 CA GLN A 156 7861 32218 12011 -11 2044 10577 B C
ATOM 6062 C GLN A 156 -46.876 20.737 6.684 1.00140.83 B C
ANISOU 6062 C GLN A 156 8470 32723 12318 -192 1865 9905 B C
ATOM 6063 O GLN A 156 -46.939 19.581 6.262 1.00141.09 B O
ANISOU 6063 O GLN A 156 8431 33369 11809 -541 1724 9182 B O
ATOM 6064 CB GLN A 156 -44.863 21.714 5.478 1.00138.35 B C
ANISOU 6064 CB GLN A 156 8209 32387 11971 -76 2018 10373 B C
ATOM 6065 CG GLN A 156 -43.514 22.417 5.599 1.00144.61 B C
ANISOU 6065 CG GLN A 156 9628 31952 13366 49 2180 10219 B C
ATOM 6066 CD GLN A 156 -42.905 22.755 4.267 1.00151.71 B C
ANISOU 6066 CD GLN A 156 11216 32085 14341 -57 2143 9483 B C
ATOM 6067 NE2 GLN A 156 -42.380 23.964 4.166 1.00143.12 B N
ANISOU 6067 NE2 GLN A 156 9859 31034 13485 226 2307 10440 B N
ATOM 6068 OE1 GLN A 156 -42.855 21.934 3.342 1.00148.78 B O
ANISOU 6068 OE1 GLN A 156 10664 32499 13368 -301 2026 9118 B O
ATOM 6069 N VAL A 157 -47.953 21.420 7.081 1.00138.69 B N
ANISOU 6069 N VAL A 157 8112 32185 12398 51 1894 10399 B N
ATOM 6070 CA VAL A 157 -49.280 20.820 6.985 1.00139.33 B C
ANISOU 6070 CA VAL A 157 8142 32525 12271 -91 1736 9978 B C
ATOM 6071 C VAL A 157 -50.221 21.765 6.219 1.00142.44 B C
ANISOU 6071 C VAL A 157 8845 32292 12985 87 1691 10004 B C
ATOM 6072 O VAL A 157 -50.330 22.949 6.542 1.00141.48 B O
ANISOU 6072 O VAL A 157 8771 31612 13374 399 1828 10646 B O
ATOM 6073 CB VAL A 157 -49.850 20.344 8.362 1.00141.85 B C
ANISOU 6073 CB VAL A 157 8476 32581 12840 -91 1763 9873 B C
ATOM 6074 CG1 VAL A 157 -49.944 21.472 9.392 1.00141.04 B C
ANISOU 6074 CG1 VAL A 157 8400 31725 13463 312 1964 10701 B C
ATOM 6075 CG2 VAL A 157 -51.183 19.610 8.209 1.00142.27 B C
ANISOU 6075 CG2 VAL A 157 8433 33008 12614 -287 1596 9370 B C
ATOM 6076 N SER A 158 -50.858 21.221 5.170 1.00141.28 B N
ANISOU 6076 N SER A 158 8641 32640 12398 -111 1513 9552 B N
ATOM 6077 CA SER A 158 -51.803 21.918 4.301 1.00141.94 B C
ANISOU 6077 CA SER A 158 8848 32494 12589 11 1431 9623 B C
ATOM 6078 C SER A 158 -53.216 21.792 4.886 1.00145.22 B C
ANISOU 6078 C SER A 158 9375 32540 13261 38 1358 9383 B C
ATOM 6079 O SER A 158 -53.737 20.677 4.971 1.00145.03 B O
ANISOU 6079 O SER A 158 9215 32971 12917 -202 1241 8877 B O
ATOM 6080 CB SER A 158 -51.725 21.341 2.891 1.00145.20 B C
ANISOU 6080 CB SER A 158 9487 33045 12637 -220 1281 8926 B C
ATOM 6081 OG SER A 158 -50.450 21.558 2.306 1.00151.73 B O
ANISOU 6081 OG SER A 158 10791 33265 13595 -251 1350 8599 B O
ATOM 6082 N VAL A 159 -53.809 22.926 5.348 1.00143.31 B N
ANISOU 6082 N VAL A 159 9098 31882 13471 341 1452 10022 B N
ATOM 6083 CA VAL A 159 -55.128 22.968 6.022 1.00143.54 B C
ANISOU 6083 CA VAL A 159 9055 31762 13721 422 1420 10078 B C
ATOM 6084 C VAL A 159 -56.031 24.140 5.518 1.00147.52 B C
ANISOU 6084 C VAL A 159 9882 31535 14635 623 1396 10139 B C
ATOM 6085 O VAL A 159 -55.475 25.160 5.120 1.00146.88 B O
ANISOU 6085 O VAL A 159 9918 31123 14765 787 1491 10501 B O
ATOM 6086 CB VAL A 159 -54.959 23.056 7.571 1.00145.24 B C
ANISOU 6086 CB VAL A 159 9330 31464 14392 544 1585 10289 B C
ATOM 6087 CG1 VAL A 159 -54.204 21.857 8.119 1.00144.95 B C
ANISOU 6087 CG1 VAL A 159 9171 31870 14032 308 1581 9957 B C
ATOM 6088 CG2 VAL A 159 -54.287 24.358 8.004 1.00144.34 B C
ANISOU 6088 CG2 VAL A 159 9325 30676 14842 851 1807 10952 B C
ATOM 6089 N PRO A 160 -57.399 24.082 5.624 1.00146.38 B N
ANISOU 6089 N PRO A 160 9589 31518 14510 653 1304 10143 B N
ATOM 6090 CA PRO A 160 -58.226 25.235 5.185 1.00146.64 B C
ANISOU 6090 CA PRO A 160 9729 31145 14844 864 1297 10424 B C
ATOM 6091 C PRO A 160 -57.948 26.522 5.985 1.00149.01 B C
ANISOU 6091 C PRO A 160 10270 30544 15804 1128 1510 10833 B C
ATOM 6092 O PRO A 160 -57.408 26.449 7.090 1.00148.14 B O
ANISOU 6092 O PRO A 160 10091 30261 15936 1191 1669 11074 B O
ATOM 6093 CB PRO A 160 -59.664 24.750 5.403 1.00148.25 B C
ANISOU 6093 CB PRO A 160 9883 31413 15033 802 1162 10106 B C
ATOM 6094 CG PRO A 160 -59.573 23.262 5.453 1.00151.51 B C
ANISOU 6094 CG PRO A 160 10332 32139 15097 492 1046 9373 B C
ATOM 6095 CD PRO A 160 -58.255 22.973 6.097 1.00147.75 B C
ANISOU 6095 CD PRO A 160 9661 31967 14509 466 1192 9672 B C
ATOM 6096 N LYS A 161 -58.305 27.695 5.414 1.00146.87 B N
ANISOU 6096 N LYS A 161 10004 30058 15741 1323 1544 11236 B N
ATOM 6097 CA LYS A 161 -58.051 29.029 5.979 1.00146.13 B C
ANISOU 6097 CA LYS A 161 10008 29272 16243 1583 1766 11753 B C
ATOM 6098 C LYS A 161 -58.522 29.203 7.438 1.00148.29 B C
ANISOU 6098 C LYS A 161 10347 28968 17027 1693 1907 11822 B C
ATOM 6099 O LYS A 161 -57.688 29.513 8.290 1.00147.12 B O
ANISOU 6099 O LYS A 161 10197 28468 17233 1798 2118 12134 B O
ATOM 6100 CB LYS A 161 -58.666 30.132 5.108 1.00148.38 B C
ANISOU 6100 CB LYS A 161 10532 29161 16686 1678 1707 11714 B C
ATOM 6101 CG LYS A 161 -57.947 31.466 5.264 1.00158.65 B C
ANISOU 6101 CG LYS A 161 12575 29151 18553 1714 1823 11290 B C
ATOM 6102 CD LYS A 161 -58.869 32.647 5.028 1.00166.29 B C
ANISOU 6102 CD LYS A 161 14058 29273 19853 1748 1748 10841 B C
ATOM 6103 CE LYS A 161 -58.226 33.963 5.398 1.00173.23 B C
ANISOU 6103 CE LYS A 161 15505 29094 21221 1769 1867 10532 B C
ATOM 6104 NZ LYS A 161 -58.114 34.137 6.873 1.00178.41 B N1+
ANISOU 6104 NZ LYS A 161 16460 29009 22320 1755 1983 10217 B N1+
ATOM 6105 N GLU A 162 -59.830 29.032 7.722 1.00146.51 B N
ANISOU 6105 N GLU A 162 9915 28933 16819 1741 1843 11907 B N
ATOM 6106 CA GLU A 162 -60.355 29.203 9.081 1.00145.85 B C
ANISOU 6106 CA GLU A 162 9757 28457 17203 1882 2002 12161 B C
ATOM 6107 C GLU A 162 -59.988 28.019 9.998 1.00148.68 B C
ANISOU 6107 C GLU A 162 10117 28928 17446 1729 2004 11857 B C
ATOM 6108 O GLU A 162 -59.903 28.197 11.217 1.00147.99 B O
ANISOU 6108 O GLU A 162 10007 28411 17812 1861 2198 12135 B O
ATOM 6109 CB GLU A 162 -61.875 29.419 9.074 1.00147.23 B C
ANISOU 6109 CB GLU A 162 9942 28548 17452 1915 1893 12009 B C
ATOM 6110 CG GLU A 162 -62.332 30.566 9.967 1.00153.44 B C
ANISOU 6110 CG GLU A 162 11194 28178 18927 2047 2029 11814 B C
ATOM 6111 CD GLU A 162 -61.984 30.465 11.443 1.00161.86 B C
ANISOU 6111 CD GLU A 162 12869 28192 20437 1946 2119 11108 B C
ATOM 6112 OE1 GLU A 162 -62.476 29.526 12.111 1.00154.16 B O
ANISOU 6112 OE1 GLU A 162 11503 27691 19380 1960 2139 11369 B O
ATOM 6113 OE2 GLU A 162 -61.193 31.308 11.925 1.00154.13 B O1-
ANISOU 6113 OE2 GLU A 162 11667 27000 19896 2175 2409 11874 B O1-
ATOM 6114 N LEU A 163 -59.764 26.825 9.419 1.00146.52 B N
ANISOU 6114 N LEU A 163 9593 29540 16538 1513 1842 11655 B N
ATOM 6115 CA LEU A 163 -59.381 25.640 10.187 1.00145.84 B C
ANISOU 6115 CA LEU A 163 9338 29844 16231 1363 1845 11515 B C
ATOM 6116 C LEU A 163 -57.875 25.691 10.494 1.00146.90 B C
ANISOU 6116 C LEU A 163 9614 29717 16485 1370 1988 11602 B C
ATOM 6117 O LEU A 163 -57.061 25.219 9.696 1.00147.15 B O
ANISOU 6117 O LEU A 163 9659 30160 16091 1201 1896 11347 B O
ATOM 6118 CB LEU A 163 -59.768 24.347 9.447 1.00146.78 B C
ANISOU 6118 CB LEU A 163 9349 30738 15683 1047 1590 10881 B C
ATOM 6119 CG LEU A 163 -61.232 23.943 9.536 1.00150.60 B C
ANISOU 6119 CG LEU A 163 9911 31146 16164 958 1443 10405 B C
ATOM 6120 CD1 LEU A 163 -61.999 24.356 8.290 1.00151.41 B C
ANISOU 6120 CD1 LEU A 163 10094 31281 16152 966 1286 10246 B C
ATOM 6121 CD2 LEU A 163 -61.358 22.462 9.737 1.00152.98 B C
ANISOU 6121 CD2 LEU A 163 10164 31892 16069 648 1313 9740 B C
ATOM 6122 N MET A 164 -57.509 26.301 11.644 1.00142.44 B N
ANISOU 6122 N MET A 164 8889 28740 16493 1637 2268 12326 B N
ATOM 6123 CA MET A 164 -56.115 26.457 12.091 1.00140.82 B C
ANISOU 6123 CA MET A 164 8692 28289 16524 1722 2463 12646 B C
ATOM 6124 C MET A 164 -55.539 25.105 12.513 1.00140.92 B C
ANISOU 6124 C MET A 164 8576 28852 16117 1505 2390 12366 B C
ATOM 6125 O MET A 164 -56.253 24.278 13.074 1.00140.43 B O
ANISOU 6125 O MET A 164 8359 29077 15923 1419 2332 12235 B O
ATOM 6126 CB MET A 164 -55.987 27.494 13.230 1.00141.55 B C
ANISOU 6126 CB MET A 164 8977 27294 17513 1999 2764 13021 B C
ATOM 6127 CG MET A 164 -56.801 28.789 13.019 1.00144.34 B C
ANISOU 6127 CG MET A 164 9592 26949 18303 2137 2805 12990 B C
ATOM 6128 SD MET A 164 -56.591 29.629 11.419 1.00148.23 B S
ANISOU 6128 SD MET A 164 10390 27371 18558 2066 2655 12670 B S
ATOM 6129 CE MET A 164 -57.787 30.937 11.585 1.00145.76 B C
ANISOU 6129 CE MET A 164 10037 26574 18773 2305 2771 13043 B C
ATOM 6130 N ALA A 165 -54.256 24.876 12.208 1.00137.28 B N
ANISOU 6130 N ALA A 165 7933 28849 15378 1456 2423 12574 B N
ATOM 6131 CA ALA A 165 -53.554 23.621 12.485 1.00136.49 B C
ANISOU 6131 CA ALA A 165 7665 29401 14795 1222 2348 12313 B C
ATOM 6132 C ALA A 165 -52.498 23.794 13.563 1.00135.95 B C
ANISOU 6132 C ALA A 165 7648 28765 15244 1395 2594 12704 B C
ATOM 6133 O ALA A 165 -51.827 24.825 13.579 1.00135.38 B O
ANISOU 6133 O ALA A 165 7710 28012 15716 1630 2800 13117 B O
ATOM 6134 CB ALA A 165 -52.900 23.114 11.210 1.00137.73 B C
ANISOU 6134 CB ALA A 165 7863 30180 14287 945 2159 11796 B C
ATOM 6135 N LEU A 166 -52.337 22.796 14.460 1.00131.63 B N
ANISOU 6135 N LEU A 166 6747 28765 14502 1329 2618 12886 B N
ATOM 6136 CA LEU A 166 -51.316 22.830 15.520 1.00129.99 B C
ANISOU 6136 CA LEU A 166 6518 28069 14802 1515 2869 13340 B C
ATOM 6137 C LEU A 166 -50.642 21.478 15.682 1.00131.47 B C
ANISOU 6137 C LEU A 166 6615 29010 14327 1178 2706 12827 B C
ATOM 6138 O LEU A 166 -51.303 20.451 15.534 1.00131.18 B O
ANISOU 6138 O LEU A 166 6391 29845 13607 858 2478 12316 B O
ATOM 6139 CB LEU A 166 -51.875 23.282 16.878 1.00129.24 B C
ANISOU 6139 CB LEU A 166 6470 27042 15595 1826 3141 13806 B C
ATOM 6140 CG LEU A 166 -52.361 24.725 17.013 1.00131.93 B C
ANISOU 6140 CG LEU A 166 7150 26188 16790 2103 3347 13969 B C
ATOM 6141 CD1 LEU A 166 -53.243 24.871 18.235 1.00131.60 B C
ANISOU 6141 CD1 LEU A 166 7128 25482 17391 2286 3534 14170 B C
ATOM 6142 CD2 LEU A 166 -51.188 25.717 17.090 1.00132.11 B C
ANISOU 6142 CD2 LEU A 166 7408 25286 17502 2311 3624 14220 B C
ATOM 6143 N MET A 167 -49.331 21.474 16.011 1.00127.52 B N
ANISOU 6143 N MET A 167 5956 28517 13981 1290 2873 13298 B N
ATOM 6144 CA MET A 167 -48.557 20.242 16.219 1.00126.70 B C
ANISOU 6144 CA MET A 167 5671 29244 13226 973 2739 12923 B C
ATOM 6145 C MET A 167 -47.754 20.279 17.535 1.00127.84 B C
ANISOU 6145 C MET A 167 5942 28509 14124 1231 3011 13328 B C
ATOM 6146 O MET A 167 -47.620 21.343 18.146 1.00126.61 B O
ANISOU 6146 O MET A 167 5911 27155 15042 1690 3368 14036 B O
ATOM 6147 CB MET A 167 -47.626 19.965 15.019 1.00128.38 B C
ANISOU 6147 CB MET A 167 5967 30032 12780 669 2568 12354 B C
ATOM 6148 CG MET A 167 -48.382 19.473 13.794 1.00131.08 B C
ANISOU 6148 CG MET A 167 6381 31037 12385 290 2282 11472 B C
ATOM 6149 SD MET A 167 -47.435 18.544 12.562 1.00133.50 B S
ANISOU 6149 SD MET A 167 6796 32077 11851 -208 2081 10445 B S
ATOM 6150 CE MET A 167 -47.137 17.023 13.424 1.00130.82 B C
ANISOU 6150 CE MET A 167 6157 32643 10907 -644 1995 9881 B C
ATOM 6151 N SER A 168 -47.228 19.112 17.975 1.00125.11 B N
ANISOU 6151 N SER A 168 5319 29017 13201 966 2903 13138 B N
ATOM 6152 CA SER A 168 -46.427 18.996 19.199 1.00116.28 B C
ANISOU 6152 CA SER A 168 5180 26043 12959 1017 3042 12332 B C
ATOM 6153 C SER A 168 -45.002 19.556 18.955 1.00120.21 B C
ANISOU 6153 C SER A 168 5875 25970 13828 1167 3202 12510 B C
ATOM 6154 O SER A 168 -43.984 18.881 19.150 1.00113.64 B O
ANISOU 6154 O SER A 168 5689 24625 12862 861 3072 11403 B O
ATOM 6155 CB SER A 168 -46.393 17.555 19.690 1.00111.91 B C
ANISOU 6155 CB SER A 168 5300 25299 11923 460 2751 10667 B C
ATOM 6156 OG SER A 168 -46.051 16.654 18.654 1.00121.07 B O
ANISOU 6156 OG SER A 168 6126 27911 11963 -45 2485 10071 B O
ATOM 6157 N ALA A 169 -44.966 20.826 18.539 1.00123.50 B N
ANISOU 6157 N ALA A 169 5684 26445 14793 1669 3532 13983 B N
ATOM 6158 CA ALA A 169 -43.778 21.576 18.170 1.00124.66 B C
ANISOU 6158 CA ALA A 169 5841 26150 15376 1888 3757 14427 B C
ATOM 6159 C ALA A 169 -44.030 23.080 18.250 1.00128.01 B C
ANISOU 6159 C ALA A 169 6688 25080 16868 2213 4051 14571 B C
ATOM 6160 O ALA A 169 -45.173 23.518 18.390 1.00128.59 B O
ANISOU 6160 O ALA A 169 6798 24886 17176 2295 4067 14621 B O
ATOM 6161 CB ALA A 169 -43.378 21.198 16.752 1.00126.11 B C
ANISOU 6161 CB ALA A 169 5948 27534 14433 1475 3397 13865 B C
ATOM 6162 N LEU A 170 -42.965 23.873 18.147 1.00125.75 B N
ANISOU 6162 N LEU A 170 6494 24081 17206 2427 4330 14890 B N
ATOM 6163 CA LEU A 170 -43.083 25.325 18.151 1.00125.22 B C
ANISOU 6163 CA LEU A 170 6653 22859 18065 2692 4633 15106 B C
ATOM 6164 C LEU A 170 -43.561 25.781 16.787 1.00129.90 B C
ANISOU 6164 C LEU A 170 7438 24002 17918 2440 4275 14611 B C
ATOM 6165 O LEU A 170 -43.151 25.202 15.778 1.00130.18 B O
ANISOU 6165 O LEU A 170 7358 25065 17040 2181 3987 14364 B O
ATOM 6166 CB LEU A 170 -41.738 26.001 18.504 1.00124.26 B C
ANISOU 6166 CB LEU A 170 6711 21659 18843 2906 5027 15275 B C
ATOM 6167 CG LEU A 170 -41.048 25.620 19.821 1.00126.43 B C
ANISOU 6167 CG LEU A 170 7251 20843 19944 3026 5347 15081 B C
ATOM 6168 CD1 LEU A 170 -39.694 26.290 19.928 1.00125.91 B C
ANISOU 6168 CD1 LEU A 170 7368 19829 20641 3169 5699 15099 B C
ATOM 6169 CD2 LEU A 170 -41.917 25.947 21.037 1.00127.61 B C
ANISOU 6169 CD2 LEU A 170 7648 19838 21001 3169 5627 14907 B C
ATOM 6170 N ARG A 171 -44.442 26.787 16.750 1.00128.88 B N
ANISOU 6170 N ARG A 171 7365 23349 18255 2596 4391 14789 B N
ATOM 6171 CA ARG A 171 -44.938 27.354 15.493 1.00130.17 B C
ANISOU 6171 CA ARG A 171 7572 23965 17922 2478 4167 14624 B C
ATOM 6172 C ARG A 171 -43.772 27.993 14.751 1.00134.22 B C
ANISOU 6172 C ARG A 171 8396 24145 18456 2411 4176 14346 B C
ATOM 6173 O ARG A 171 -42.944 28.643 15.391 1.00133.02 B O
ANISOU 6173 O ARG A 171 8339 23073 19131 2615 4511 14586 B O
ATOM 6174 CB ARG A 171 -46.044 28.387 15.754 1.00130.21 B C
ANISOU 6174 CB ARG A 171 7691 23274 18509 2642 4294 14726 B C
ATOM 6175 CG ARG A 171 -47.287 27.833 16.429 1.00137.68 B C
ANISOU 6175 CG ARG A 171 8904 24154 19256 2475 4077 14093 B C
ATOM 6176 CD ARG A 171 -48.135 28.972 16.949 1.00143.39 B C
ANISOU 6176 CD ARG A 171 10079 23786 20616 2534 4161 13705 B C
ATOM 6177 NE ARG A 171 -48.452 28.825 18.372 1.00149.13 B N
ANISOU 6177 NE ARG A 171 11183 23599 21883 2525 4266 13237 B N
ATOM 6178 CZ ARG A 171 -47.669 29.227 19.371 1.00158.83 B C
ANISOU 6178 CZ ARG A 171 13089 23599 23662 2431 4359 12433 B C
ATOM 6179 NH1 ARG A 171 -46.490 29.785 19.120 1.00154.07 B N1+
ANISOU 6179 NH1 ARG A 171 12303 22771 23465 2597 4626 12921 B N1+
ATOM 6180 NH2 ARG A 171 -48.054 29.061 20.631 1.00143.44 B N
ANISOU 6180 NH2 ARG A 171 10545 21279 22678 2833 4892 13478 B N
ATOM 6181 N ASP A 172 -43.672 27.776 13.429 1.00134.38 B N
ANISOU 6181 N ASP A 172 8343 25057 17660 2208 3908 14162 B N
ATOM 6182 CA ASP A 172 -42.570 28.331 12.638 1.00135.46 B C
ANISOU 6182 CA ASP A 172 8623 25070 17776 2182 3945 14111 B C
ATOM 6183 C ASP A 172 -43.083 29.192 11.444 1.00141.70 B C
ANISOU 6183 C ASP A 172 9792 25731 18317 2044 3750 13607 B C
ATOM 6184 O ASP A 172 -42.407 29.324 10.419 1.00141.51 B O
ANISOU 6184 O ASP A 172 9779 26060 17928 1950 3677 13546 B O
ATOM 6185 CB ASP A 172 -41.623 27.211 12.168 1.00136.99 B C
ANISOU 6185 CB ASP A 172 8773 26055 17222 1921 3749 13757 B C
ATOM 6186 CG ASP A 172 -40.317 27.705 11.563 1.00141.92 B C
ANISOU 6186 CG ASP A 172 9789 26221 17911 1830 3772 13369 B C
ATOM 6187 OD1 ASP A 172 -39.708 28.641 12.135 1.00141.43 B O
ANISOU 6187 OD1 ASP A 172 9864 25194 18679 2050 4063 13633 B O
ATOM 6188 OD2 ASP A 172 -39.922 27.181 10.505 1.00144.91 B O1-
ANISOU 6188 OD2 ASP A 172 10276 27224 17560 1556 3538 12870 B O1-
ATOM 6189 N GLY A 173 -44.252 29.807 11.635 1.00141.70 B N
ANISOU 6189 N GLY A 173 9828 25403 18607 2149 3770 13685 B N
ATOM 6190 CA GLY A 173 -44.869 30.698 10.661 1.00143.07 B C
ANISOU 6190 CA GLY A 173 10144 25532 18684 2136 3673 13581 B C
ATOM 6191 C GLY A 173 -45.956 30.102 9.795 1.00149.43 B C
ANISOU 6191 C GLY A 173 11172 26864 18741 1859 3293 12851 B C
ATOM 6192 O GLY A 173 -46.137 28.881 9.739 1.00149.24 B O
ANISOU 6192 O GLY A 173 10993 27555 18155 1687 3121 12623 B O
ATOM 6193 N GLU A 174 -46.691 30.996 9.118 1.00150.03 B N
ANISOU 6193 N GLU A 174 11345 26788 18870 1907 3247 12858 B N
ATOM 6194 CA GLU A 174 -47.778 30.685 8.187 1.00151.96 B C
ANISOU 6194 CA GLU A 174 11619 27550 18567 1763 2981 12516 B C
ATOM 6195 C GLU A 174 -47.284 30.871 6.754 1.00157.72 B C
ANISOU 6195 C GLU A 174 12718 28320 18890 1567 2810 11959 B C
ATOM 6196 O GLU A 174 -46.414 31.715 6.520 1.00157.07 B O
ANISOU 6196 O GLU A 174 12727 27869 19083 1650 2950 12166 B O
ATOM 6197 CB GLU A 174 -48.999 31.586 8.454 1.00152.84 B C
ANISOU 6197 CB GLU A 174 11828 27177 19069 1895 3004 12577 B C
ATOM 6198 CG GLU A 174 -49.525 31.519 9.880 1.00161.05 B C
ANISOU 6198 CG GLU A 174 13258 27393 20543 1858 3019 12040 B C
ATOM 6199 CD GLU A 174 -50.757 32.340 10.211 1.00180.32 B C
ANISOU 6199 CD GLU A 174 16700 28597 23219 1643 2782 10667 B C
ATOM 6200 OE1 GLU A 174 -51.226 33.124 9.352 1.00177.89 B O
ANISOU 6200 OE1 GLU A 174 16297 28411 22883 1727 2764 10923 B O
ATOM 6201 OE2 GLU A 174 -51.257 32.196 11.350 1.00178.24 B O1-
ANISOU 6201 OE2 GLU A 174 16260 28170 23293 1762 2909 10931 B O1-
ATOM 6202 N LEU A 175 -47.838 30.094 5.794 1.00158.22 B N
ANISOU 6202 N LEU A 175 12726 29064 18325 1389 2579 11629 B N
ATOM 6203 CA LEU A 175 -47.470 30.158 4.371 1.00159.77 B C
ANISOU 6203 CA LEU A 175 13071 29510 18124 1262 2461 11369 B C
ATOM 6204 C LEU A 175 -48.631 29.717 3.438 1.00165.09 B C
ANISOU 6204 C LEU A 175 13991 30314 18421 1092 2195 10710 B C
ATOM 6205 O LEU A 175 -49.691 29.308 3.918 1.00164.54 B O
ANISOU 6205 O LEU A 175 13797 30379 18340 1100 2121 10667 B O
ATOM 6206 CB LEU A 175 -46.201 29.324 4.090 1.00159.99 B C
ANISOU 6206 CB LEU A 175 13079 29911 17798 1099 2457 11169 B C
ATOM 6207 CG LEU A 175 -44.899 30.124 3.928 1.00163.08 B C
ANISOU 6207 CG LEU A 175 13761 29715 18486 1128 2600 11159 B C
ATOM 6208 CD1 LEU A 175 -43.693 29.289 4.296 1.00163.01 B C
ANISOU 6208 CD1 LEU A 175 13686 29939 18311 1018 2650 11055 B C
ATOM 6209 CD2 LEU A 175 -44.747 30.675 2.508 1.00165.67 B C
ANISOU 6209 CD2 LEU A 175 14349 29979 18619 1058 2519 10931 B C
ATOM 6210 N SER A 176 -48.416 29.830 2.102 1.00165.01 B N
ANISOU 6210 N SER A 176 14053 30561 18082 1016 2106 10595 B N
ATOM 6211 CA SER A 176 -49.378 29.512 1.036 1.00166.40 B C
ANISOU 6211 CA SER A 176 14297 31019 17909 919 1900 10254 B C
ATOM 6212 C SER A 176 -48.981 28.263 0.210 1.00171.06 B C
ANISOU 6212 C SER A 176 15088 31882 18023 646 1746 9519 B C
ATOM 6213 O SER A 176 -47.810 27.870 0.214 1.00170.70 B O
ANISOU 6213 O SER A 176 15024 31990 17845 560 1819 9469 B O
ATOM 6214 CB SER A 176 -49.518 30.709 0.097 1.00169.19 B C
ANISOU 6214 CB SER A 176 14966 30892 18425 989 1885 10231 B C
ATOM 6215 OG SER A 176 -48.273 31.044 -0.495 1.00174.83 B O
ANISOU 6215 OG SER A 176 16113 31138 19178 890 1931 9869 B O
ATOM 6216 N GLU A 177 -49.963 27.671 -0.521 1.00170.11 B N
ANISOU 6216 N GLU A 177 14877 32185 17573 566 1568 9301 B N
ATOM 6217 CA GLU A 177 -49.785 26.486 -1.379 1.00170.86 B C
ANISOU 6217 CA GLU A 177 14979 32745 17195 344 1437 8799 B C
ATOM 6218 C GLU A 177 -49.863 26.833 -2.892 1.00174.67 B C
ANISOU 6218 C GLU A 177 15821 32972 17574 304 1332 8476 B C
ATOM 6219 O GLU A 177 -50.199 27.965 -3.250 1.00174.55 B O
ANISOU 6219 O GLU A 177 15905 32660 17756 451 1340 8754 B O
ATOM 6220 CB GLU A 177 -50.825 25.403 -1.029 1.00171.99 B C
ANISOU 6220 CB GLU A 177 15025 33119 17203 224 1301 8396 B C
ATOM 6221 CG GLU A 177 -50.263 24.228 -0.240 1.00178.52 B C
ANISOU 6221 CG GLU A 177 16112 33624 18093 31 1322 7707 B C
ATOM 6222 CD GLU A 177 -49.293 23.292 -0.944 1.00192.14 B C
ANISOU 6222 CD GLU A 177 18685 34357 19962 -203 1291 6498 B C
ATOM 6223 OE1 GLU A 177 -49.325 23.211 -2.194 1.00186.94 B O
ANISOU 6223 OE1 GLU A 177 17875 34206 18948 -241 1210 6581 B O
ATOM 6224 OE2 GLU A 177 -48.537 22.592 -0.233 1.00187.77 B O1-
ANISOU 6224 OE2 GLU A 177 17829 34294 19219 -291 1370 6597 B O1-
ATOM 6225 N GLN A 178 -49.547 25.847 -3.768 1.00172.96 B N
ANISOU 6225 N GLN A 178 15520 33287 16911 130 1252 8185 B N
ATOM 6226 CA GLN A 178 -49.536 25.988 -5.233 1.00173.69 B C
ANISOU 6226 CA GLN A 178 15795 33409 16789 89 1161 8015 B C
ATOM 6227 C GLN A 178 -50.852 25.467 -5.852 1.00176.75 B C
ANISOU 6227 C GLN A 178 16324 33717 17115 25 960 7549 B C
ATOM 6228 O GLN A 178 -51.815 26.230 -5.945 1.00176.53 B O
ANISOU 6228 O GLN A 178 16309 33512 17252 154 896 7743 B O
ATOM 6229 CB GLN A 178 -48.317 25.260 -5.845 1.00174.90 B C
ANISOU 6229 CB GLN A 178 16061 33707 16685 -75 1204 7690 B C
ATOM 6230 CG GLN A 178 -46.961 25.680 -5.277 1.00187.42 B C
ANISOU 6230 CG GLN A 178 18352 34040 18818 -81 1375 7235 B C
ATOM 6231 CD GLN A 178 -46.378 26.874 -5.985 1.00203.73 B C
ANISOU 6231 CD GLN A 178 21482 34482 21444 -66 1410 6555 B C
ATOM 6232 NE2 GLN A 178 -45.261 26.662 -6.664 1.00200.10 B N
ANISOU 6232 NE2 GLN A 178 20900 34457 20672 -134 1472 6665 B N
ATOM 6233 OE1 GLN A 178 -46.893 27.996 -5.903 1.00200.66 B O
ANISOU 6233 OE1 GLN A 178 20974 34094 21173 79 1420 7028 B O
ATOM 6234 N SER A 179 -50.885 24.180 -6.277 1.00174.66 B N
ANISOU 6234 N SER A 179 15887 34011 16462 -163 871 7206 B N
ATOM 6235 CA SER A 179 -52.054 23.512 -6.862 1.00175.08 B C
ANISOU 6235 CA SER A 179 15918 34230 16373 -242 686 6859 B C
ATOM 6236 C SER A 179 -52.917 22.906 -5.748 1.00176.90 B C
ANISOU 6236 C SER A 179 16067 34350 16798 -270 649 6651 B C
ATOM 6237 O SER A 179 -52.407 22.692 -4.643 1.00175.96 B O
ANISOU 6237 O SER A 179 15801 34305 16752 -285 764 6761 B O
ATOM 6238 CB SER A 179 -51.617 22.439 -7.856 1.00178.14 B C
ANISOU 6238 CB SER A 179 16517 34621 16546 -433 627 6256 B C
ATOM 6239 OG SER A 179 -52.703 22.004 -8.658 1.00185.00 B O
ANISOU 6239 OG SER A 179 17774 34932 17585 -463 453 5682 B O
ATOM 6240 N ASP A 180 -54.221 22.635 -6.038 1.00174.57 B N
ANISOU 6240 N ASP A 180 15588 34342 16397 -278 490 6605 B N
ATOM 6241 CA ASP A 180 -55.237 22.122 -5.095 1.00173.91 B C
ANISOU 6241 CA ASP A 180 15293 34378 16409 -301 438 6527 B C
ATOM 6242 C ASP A 180 -55.319 23.110 -3.910 1.00175.20 B C
ANISOU 6242 C ASP A 180 15496 34103 16968 -113 560 6916 B C
ATOM 6243 O ASP A 180 -55.187 22.729 -2.746 1.00174.15 B O
ANISOU 6243 O ASP A 180 15181 34086 16904 -141 638 6968 B O
ATOM 6244 CB ASP A 180 -54.937 20.666 -4.655 1.00174.84 B C
ANISOU 6244 CB ASP A 180 15334 34705 16392 -528 443 6019 B C
ATOM 6245 CG ASP A 180 -56.112 19.947 -4.021 1.00180.51 B C
ANISOU 6245 CG ASP A 180 16239 34898 17451 -572 362 5507 B C
ATOM 6246 OD1 ASP A 180 -57.028 19.537 -4.766 1.00181.28 B O
ANISOU 6246 OD1 ASP A 180 16370 35003 17505 -623 210 5229 B O
ATOM 6247 OD2 ASP A 180 -56.098 19.762 -2.785 1.00183.31 B O1-
ANISOU 6247 OD2 ASP A 180 16652 34919 18079 -562 451 5427 B O1-
ATOM 6248 N SER A 181 -55.518 24.402 -4.256 1.00172.45 B N
ANISOU 6248 N SER A 181 15119 33695 16707 81 581 7447 B N
ATOM 6249 CA SER A 181 -55.547 25.597 -3.405 1.00171.37 B C
ANISOU 6249 CA SER A 181 14951 33249 16914 291 710 7978 B C
ATOM 6250 C SER A 181 -56.467 25.522 -2.166 1.00172.66 B C
ANISOU 6250 C SER A 181 15035 33203 17364 349 719 7983 B C
ATOM 6251 O SER A 181 -56.319 26.371 -1.284 1.00171.81 B O
ANISOU 6251 O SER A 181 14893 32825 17564 509 856 8404 B O
ATOM 6252 CB SER A 181 -55.939 26.814 -4.236 1.00174.20 B C
ANISOU 6252 CB SER A 181 15625 33086 17478 434 669 8068 B C
ATOM 6253 OG SER A 181 -55.663 28.034 -3.567 1.00179.39 B O
ANISOU 6253 OG SER A 181 16647 32866 18647 576 803 8147 B O
ATOM 6254 N ASN A 182 -57.373 24.519 -2.068 1.00169.65 B N
ANISOU 6254 N ASN A 182 14352 33358 16751 238 595 7811 B N
ATOM 6255 CA ASN A 182 -58.288 24.346 -0.926 1.00168.72 B C
ANISOU 6255 CA ASN A 182 14031 33261 16813 284 603 7908 B C
ATOM 6256 C ASN A 182 -57.519 23.847 0.332 1.00169.04 B C
ANISOU 6256 C ASN A 182 14006 33284 16940 229 748 7904 B C
ATOM 6257 O ASN A 182 -57.869 22.822 0.929 1.00168.59 B O
ANISOU 6257 O ASN A 182 13772 33512 16773 93 714 7646 B O
ATOM 6258 CB ASN A 182 -59.438 23.397 -1.301 1.00170.28 B C
ANISOU 6258 CB ASN A 182 14201 33614 16885 147 419 7413 B C
ATOM 6259 CG ASN A 182 -60.812 23.973 -1.052 1.00187.75 B C
ANISOU 6259 CG ASN A 182 17358 34049 19930 238 332 6554 B C
ATOM 6260 ND2 ASN A 182 -61.504 23.441 -0.054 1.00183.20 B N
ANISOU 6260 ND2 ASN A 182 16346 33963 19299 223 345 6753 B N
ATOM 6261 OD1 ASN A 182 -61.280 24.875 -1.758 1.00183.02 B O
ANISOU 6261 OD1 ASN A 182 16615 33674 19249 372 271 6969 B O
ATOM 6262 N ARG A 183 -56.477 24.614 0.726 1.00164.98 B N
ANISOU 6262 N ARG A 183 13363 32834 16488 358 921 8489 B N
ATOM 6263 CA ARG A 183 -55.555 24.386 1.847 1.00163.50 B C
ANISOU 6263 CA ARG A 183 13047 32701 16373 353 1080 8686 B C
ATOM 6264 C ARG A 183 -54.706 25.665 2.126 1.00163.83 B C
ANISOU 6264 C ARG A 183 13258 32204 16787 555 1260 9150 B C
ATOM 6265 O ARG A 183 -54.822 26.654 1.396 1.00163.73 B O
ANISOU 6265 O ARG A 183 13373 31954 16884 677 1258 9357 B O
ATOM 6266 CB ARG A 183 -54.647 23.156 1.577 1.00164.40 B C
ANISOU 6266 CB ARG A 183 13158 33190 16114 98 1049 8203 B C
ATOM 6267 CG ARG A 183 -53.858 23.190 0.256 1.00174.18 B C
ANISOU 6267 CG ARG A 183 15043 33739 17397 -1 1002 7541 B C
ATOM 6268 CD ARG A 183 -53.335 21.817 -0.146 1.00182.63 B C
ANISOU 6268 CD ARG A 183 16467 34559 18365 -261 945 6634 B C
ATOM 6269 NE ARG A 183 -52.605 21.836 -1.417 1.00188.65 B N
ANISOU 6269 NE ARG A 183 17656 34920 19102 -318 920 6250 B N
ATOM 6270 CZ ARG A 183 -51.621 20.997 -1.733 1.00197.91 B C
ANISOU 6270 CZ ARG A 183 19334 35468 20395 -471 951 5505 B C
ATOM 6271 NH1 ARG A 183 -51.205 20.089 -0.859 1.00188.59 B N1+
ANISOU 6271 NH1 ARG A 183 17505 35366 18786 -620 996 5734 B N1+
ATOM 6272 NH2 ARG A 183 -51.018 21.087 -2.911 1.00188.63 B N
ANISOU 6272 NH2 ARG A 183 17750 35264 18655 -517 930 5912 B N
ATOM 6273 N LYS A 184 -53.881 25.637 3.202 1.00159.24 B N
ANISOU 6273 N LYS A 184 12396 31815 16292 623 1433 9624 B N
ATOM 6274 CA LYS A 184 -52.980 26.710 3.666 1.00157.59 B C
ANISOU 6274 CA LYS A 184 12218 31196 16462 822 1641 10176 B C
ATOM 6275 C LYS A 184 -51.901 26.084 4.559 1.00157.47 B C
ANISOU 6275 C LYS A 184 12142 31241 16447 752 1753 10164 B C
ATOM 6276 O LYS A 184 -52.232 25.268 5.423 1.00157.10 B O
ANISOU 6276 O LYS A 184 11940 31417 16335 674 1733 10036 B O
ATOM 6277 CB LYS A 184 -53.763 27.813 4.418 1.00158.89 B C
ANISOU 6277 CB LYS A 184 12498 30672 17200 1049 1738 10473 B C
ATOM 6278 CG LYS A 184 -52.972 29.091 4.703 1.00168.03 B C
ANISOU 6278 CG LYS A 184 14323 30557 18962 1125 1873 10202 B C
ATOM 6279 CD LYS A 184 -53.127 30.134 3.601 1.00175.32 B C
ANISOU 6279 CD LYS A 184 15793 30810 20012 1108 1781 9760 B C
ATOM 6280 CE LYS A 184 -52.365 31.398 3.914 1.00182.90 B C
ANISOU 6280 CE LYS A 184 17299 30731 21462 1144 1898 9520 B C
ATOM 6281 NZ LYS A 184 -52.488 32.398 2.822 1.00190.27 B N1+
ANISOU 6281 NZ LYS A 184 18759 31077 22459 1097 1789 9053 B N1+
ATOM 6282 N ILE A 185 -50.620 26.459 4.345 1.00152.89 B N
ANISOU 6282 N ILE A 185 11410 30841 15842 821 1891 10625 B N
ATOM 6283 CA ILE A 185 -49.475 25.896 5.071 1.00151.22 B C
ANISOU 6283 CA ILE A 185 11061 30811 15584 768 2001 10720 B C
ATOM 6284 C ILE A 185 -49.220 26.599 6.423 1.00150.70 B C
ANISOU 6284 C ILE A 185 10989 30117 16153 1004 2222 11220 B C
ATOM 6285 O ILE A 185 -49.101 27.822 6.498 1.00149.73 B O
ANISOU 6285 O ILE A 185 10950 29423 16519 1228 2374 11655 B O
ATOM 6286 CB ILE A 185 -48.189 25.875 4.182 1.00153.44 B C
ANISOU 6286 CB ILE A 185 11556 31080 15666 652 2011 10467 B C
ATOM 6287 CG1 ILE A 185 -48.313 24.816 3.059 1.00154.50 B C
ANISOU 6287 CG1 ILE A 185 11700 31823 15181 371 1813 9837 B C
ATOM 6288 CG2 ILE A 185 -46.909 25.639 5.009 1.00153.22 B C
ANISOU 6288 CG2 ILE A 185 11502 30934 15782 655 2163 10598 B C
ATOM 6289 CD1 ILE A 185 -47.287 24.939 1.909 1.00159.72 B C
ANISOU 6289 CD1 ILE A 185 12784 32159 15744 257 1801 9382 B C
ATOM 6290 N TYR A 186 -49.133 25.773 7.478 1.00146.52 B N
ANISOU 6290 N TYR A 186 10097 30031 15545 991 2272 11457 B N
ATOM 6291 CA TYR A 186 -48.765 26.098 8.855 1.00144.84 B C
ANISOU 6291 CA TYR A 186 9802 29333 15899 1200 2496 11951 B C
ATOM 6292 C TYR A 186 -47.537 25.240 9.154 1.00145.58 B C
ANISOU 6292 C TYR A 186 9839 29718 15757 1057 2520 11800 B C
ATOM 6293 O TYR A 186 -47.660 24.013 9.177 1.00146.03 B O
ANISOU 6293 O TYR A 186 9767 30416 15301 809 2370 11366 B O
ATOM 6294 CB TYR A 186 -49.925 25.799 9.834 1.00145.69 B C
ANISOU 6294 CB TYR A 186 9866 29294 16197 1237 2476 11904 B C
ATOM 6295 CG TYR A 186 -50.956 26.899 9.988 1.00146.91 B C
ANISOU 6295 CG TYR A 186 10182 28776 16862 1440 2538 12082 B C
ATOM 6296 CD1 TYR A 186 -50.800 27.899 10.944 1.00147.40 B C
ANISOU 6296 CD1 TYR A 186 10394 27907 17706 1686 2786 12435 B C
ATOM 6297 CD2 TYR A 186 -52.131 26.890 9.241 1.00148.17 B C
ANISOU 6297 CD2 TYR A 186 10374 29177 16748 1363 2350 11803 B C
ATOM 6298 CE1 TYR A 186 -51.765 28.892 11.118 1.00147.64 B C
ANISOU 6298 CE1 TYR A 186 10522 27397 18180 1852 2852 12589 B C
ATOM 6299 CE2 TYR A 186 -53.105 27.875 9.408 1.00148.69 B C
ANISOU 6299 CE2 TYR A 186 10538 28712 17247 1544 2403 11992 B C
ATOM 6300 CZ TYR A 186 -52.915 28.878 10.345 1.00152.67 B C
ANISOU 6300 CZ TYR A 186 11385 28128 18494 1710 2604 12031 B C
ATOM 6301 OH TYR A 186 -53.861 29.861 10.506 1.00152.49 B O
ANISOU 6301 OH TYR A 186 11446 27620 18873 1864 2660 12175 B O
ATOM 6302 N ARG A 187 -46.347 25.845 9.293 1.00140.82 B N
ANISOU 6302 N ARG A 187 9065 29009 15430 1244 2734 12446 B N
ATOM 6303 CA ARG A 187 -45.131 25.050 9.520 1.00139.88 B C
ANISOU 6303 CA ARG A 187 8827 29264 15059 1122 2760 12390 B C
ATOM 6304 C ARG A 187 -44.707 25.029 11.005 1.00139.86 B C
ANISOU 6304 C ARG A 187 8791 28694 15654 1310 2975 12755 B C
ATOM 6305 O ARG A 187 -44.953 25.987 11.742 1.00138.56 B O
ANISOU 6305 O ARG A 187 8680 27681 16286 1616 3212 13256 B O
ATOM 6306 CB ARG A 187 -43.967 25.490 8.606 1.00139.78 B C
ANISOU 6306 CB ARG A 187 8914 29230 14968 1108 2810 12426 B C
ATOM 6307 CG ARG A 187 -43.684 26.987 8.585 1.00144.95 B C
ANISOU 6307 CG ARG A 187 10058 28610 16407 1321 2985 12475 B C
ATOM 6308 CD ARG A 187 -42.816 27.397 7.418 1.00149.94 B C
ANISOU 6308 CD ARG A 187 11060 29028 16881 1194 2936 12054 B C
ATOM 6309 NE ARG A 187 -42.161 28.682 7.663 1.00153.08 B N
ANISOU 6309 NE ARG A 187 11784 28389 17989 1373 3139 12197 B N
ATOM 6310 CZ ARG A 187 -41.055 29.092 7.050 1.00160.80 B C
ANISOU 6310 CZ ARG A 187 13271 28813 19015 1239 3130 11644 B C
ATOM 6311 NH1 ARG A 187 -40.462 28.319 6.147 1.00149.84 B N1+
ANISOU 6311 NH1 ARG A 187 11277 28709 16945 1192 3108 12151 B N1+
ATOM 6312 NH2 ARG A 187 -40.530 30.274 7.338 1.00151.64 B N
ANISOU 6312 NH2 ARG A 187 11729 27406 18481 1588 3454 12683 B N
ATOM 6313 N PHE A 188 -44.097 23.905 11.436 1.00136.23 B N
ANISOU 6313 N PHE A 188 7979 29015 14768 1172 2939 12810 B N
ATOM 6314 CA PHE A 188 -43.657 23.677 12.817 1.00134.50 B C
ANISOU 6314 CA PHE A 188 7651 28402 15050 1347 3140 13210 B C
ATOM 6315 C PHE A 188 -42.245 23.060 12.894 1.00134.85 B C
ANISOU 6315 C PHE A 188 7681 28686 14870 1216 3151 13059 B C
ATOM 6316 O PHE A 188 -41.832 22.341 11.981 1.00135.07 B O
ANISOU 6316 O PHE A 188 7628 29610 14081 883 2938 12559 B O
ATOM 6317 CB PHE A 188 -44.661 22.768 13.550 1.00135.84 B C
ANISOU 6317 CB PHE A 188 7740 28889 14984 1207 3005 12909 B C
ATOM 6318 CG PHE A 188 -46.072 23.305 13.601 1.00136.96 B C
ANISOU 6318 CG PHE A 188 7958 28693 15388 1323 2989 12960 B C
ATOM 6319 CD1 PHE A 188 -46.459 24.196 14.593 1.00138.29 B C
ANISOU 6319 CD1 PHE A 188 8323 27708 16513 1649 3247 13336 B C
ATOM 6320 CD2 PHE A 188 -47.013 22.925 12.650 1.00139.32 B C
ANISOU 6320 CD2 PHE A 188 8287 29599 15050 1065 2716 12386 B C
ATOM 6321 CE1 PHE A 188 -47.758 24.708 14.626 1.00139.18 B C
ANISOU 6321 CE1 PHE A 188 8497 27550 16835 1735 3227 13350 B C
ATOM 6322 CE2 PHE A 188 -48.310 23.442 12.680 1.00141.44 B C
ANISOU 6322 CE2 PHE A 188 8681 29478 15581 1166 2691 12363 B C
ATOM 6323 CZ PHE A 188 -48.672 24.332 13.666 1.00139.40 B C
ANISOU 6323 CZ PHE A 188 8421 28379 16166 1518 2950 12996 B C
ATOM 6324 N LYS A 189 -41.526 23.331 14.004 1.00130.03 B N
ANISOU 6324 N LYS A 189 6885 27509 15010 1551 3474 13834 B N
ATOM 6325 CA LYS A 189 -40.186 22.805 14.265 1.00128.93 B C
ANISOU 6325 CA LYS A 189 6658 27527 14803 1510 3541 13892 B C
ATOM 6326 C LYS A 189 -40.054 22.223 15.697 1.00128.55 B C
ANISOU 6326 C LYS A 189 6554 27066 15223 1647 3701 14105 B C
ATOM 6327 O LYS A 189 -40.337 22.902 16.687 1.00126.79 B O
ANISOU 6327 O LYS A 189 6409 25675 16089 2048 4058 14646 B O
ATOM 6328 CB LYS A 189 -39.090 23.861 13.999 1.00130.61 B C
ANISOU 6328 CB LYS A 189 7150 26776 15702 1733 3793 14107 B C
ATOM 6329 CG LYS A 189 -39.336 25.248 14.598 1.00139.93 B C
ANISOU 6329 CG LYS A 189 9100 26013 18053 1945 4017 13737 B C
ATOM 6330 CD LYS A 189 -38.122 26.149 14.413 1.00144.01 B C
ANISOU 6330 CD LYS A 189 10051 25557 19111 2002 4182 13511 B C
ATOM 6331 CE LYS A 189 -38.292 27.492 15.077 1.00148.60 B C
ANISOU 6331 CE LYS A 189 11136 24598 20726 2173 4420 13283 B C
ATOM 6332 NZ LYS A 189 -37.040 28.292 15.018 1.00155.38 B N1+
ANISOU 6332 NZ LYS A 189 12476 24558 22001 2132 4516 12828 B N1+
ATOM 6333 N GLN A 190 -39.635 20.946 15.775 1.00122.78 B N
ANISOU 6333 N GLN A 190 5691 27287 13675 1279 3456 13596 B N
ATOM 6334 CA GLN A 190 -39.372 20.208 17.006 1.00111.49 B C
ANISOU 6334 CA GLN A 190 5326 24369 12666 1044 3366 12134 B C
ATOM 6335 C GLN A 190 -37.906 19.763 16.990 1.00108.93 B C
ANISOU 6335 C GLN A 190 5593 23498 12297 799 3294 11209 B C
ATOM 6336 O GLN A 190 -37.560 18.748 16.376 1.00107.70 B O
ANISOU 6336 O GLN A 190 5432 24275 11215 317 3009 10389 B O
ATOM 6337 CB GLN A 190 -40.347 19.029 17.190 1.00110.65 B C
ANISOU 6337 CB GLN A 190 5311 24906 11824 611 3042 11218 B C
ATOM 6338 CG GLN A 190 -40.181 18.272 18.511 1.00 98.76 B C
ANISOU 6338 CG GLN A 190 4831 21904 10789 414 2981 9855 B C
ATOM 6339 CD GLN A 190 -40.154 19.170 19.735 1.00104.78 B C
ANISOU 6339 CD GLN A 190 6088 20915 12809 850 3299 10116 B C
ATOM 6340 NE2 GLN A 190 -41.304 19.328 20.390 1.00101.32 B N
ANISOU 6340 NE2 GLN A 190 5613 20176 12708 1004 3373 10341 B N
ATOM 6341 OE1 GLN A 190 -39.106 19.708 20.123 1.00 86.03 B O
ANISOU 6341 OE1 GLN A 190 4115 17465 11109 1018 3499 10046 B O
ATOM 6342 N ASN A 191 -37.051 20.571 17.642 1.00102.24 B N
ANISOU 6342 N ASN A 191 5188 21161 12497 1125 3599 11357 B N
ATOM 6343 CA ASN A 191 -35.597 20.436 17.686 1.00 97.95 B C
ANISOU 6343 CA ASN A 191 5156 19947 12112 1004 3607 10710 B C
ATOM 6344 C ASN A 191 -35.111 19.603 18.871 1.00 94.85 B C
ANISOU 6344 C ASN A 191 5750 18297 11993 742 3481 9276 B C
ATOM 6345 O ASN A 191 -33.905 19.369 19.004 1.00 91.67 B O
ANISOU 6345 O ASN A 191 5809 17317 11705 615 3464 8646 B O
ATOM 6346 CB ASN A 191 -34.941 21.821 17.701 1.00 98.84 B C
ANISOU 6346 CB ASN A 191 5109 19217 13228 1491 4052 11687 B C
ATOM 6347 CG ASN A 191 -35.164 22.625 16.436 1.00120.78 B C
ANISOU 6347 CG ASN A 191 6873 23258 15758 1773 4213 13197 B C
ATOM 6348 ND2 ASN A 191 -35.387 23.924 16.578 1.00118.42 B N
ANISOU 6348 ND2 ASN A 191 6187 22299 16509 2304 4706 14398 B N
ATOM 6349 OD1 ASN A 191 -35.140 22.101 15.318 1.00109.45 B O
ANISOU 6349 OD1 ASN A 191 4938 23427 13223 1516 3941 13321 B O
ATOM 6350 N VAL A 192 -36.041 19.142 19.716 1.00 88.82 B N
ANISOU 6350 N VAL A 192 5262 17170 11316 668 3399 8815 B N
ATOM 6351 CA VAL A 192 -35.721 18.260 20.834 1.00 80.63 B C
ANISOU 6351 CA VAL A 192 5058 15116 10460 427 3276 7560 B C
ATOM 6352 C VAL A 192 -36.108 16.847 20.382 1.00 83.05 B C
ANISOU 6352 C VAL A 192 5326 16414 9816 -65 2950 6738 B C
ATOM 6353 O VAL A 192 -37.247 16.674 19.936 1.00 86.69 B O
ANISOU 6353 O VAL A 192 5290 17853 9794 -135 2859 7053 B O
ATOM 6354 CB VAL A 192 -36.401 18.676 22.169 1.00 81.72 B C
ANISOU 6354 CB VAL A 192 5554 14085 11410 662 3456 7523 B C
ATOM 6355 CG1 VAL A 192 -36.035 17.715 23.295 1.00 74.70 B C
ANISOU 6355 CG1 VAL A 192 5449 12318 10614 415 3317 6309 B C
ATOM 6356 CG2 VAL A 192 -36.029 20.100 22.563 1.00 83.01 B C
ANISOU 6356 CG2 VAL A 192 5658 13285 12598 1091 3879 8246 B C
ATOM 6357 N PRO A 193 -35.191 15.838 20.444 1.00 75.49 B N
ANISOU 6357 N PRO A 193 4812 15258 8612 -419 2816 5700 B N
ATOM 6358 CA PRO A 193 -35.566 14.478 20.017 1.00 75.59 B C
ANISOU 6358 CA PRO A 193 4731 16118 7870 -920 2618 4839 B C
ATOM 6359 C PRO A 193 -36.721 13.935 20.840 1.00 78.04 B C
ANISOU 6359 C PRO A 193 5212 16156 8284 -975 2576 4486 B C
ATOM 6360 O PRO A 193 -36.729 14.028 22.077 1.00 72.60 B O
ANISOU 6360 O PRO A 193 5084 14238 8264 -783 2649 4278 B O
ATOM 6361 CB PRO A 193 -34.293 13.657 20.243 1.00 72.84 B C
ANISOU 6361 CB PRO A 193 4925 15133 7618 -1176 2601 3869 B C
ATOM 6362 CG PRO A 193 -33.197 14.653 20.269 1.00 76.20 B C
ANISOU 6362 CG PRO A 193 5493 14958 8501 -865 2720 4381 B C
ATOM 6363 CD PRO A 193 -33.788 15.869 20.913 1.00 72.67 B C
ANISOU 6363 CD PRO A 193 5014 13891 8706 -394 2885 5245 B C
ATOM 6364 N ILE A 194 -37.735 13.438 20.126 1.00 79.02 B N
ANISOU 6364 N ILE A 194 4782 17530 7714 -1238 2469 4466 B N
ATOM 6365 CA ILE A 194 -38.965 12.913 20.703 1.00 78.13 B C
ANISOU 6365 CA ILE A 194 4697 17393 7597 -1321 2429 4186 B C
ATOM 6366 C ILE A 194 -39.269 11.502 20.166 1.00 83.88 B C
ANISOU 6366 C ILE A 194 5212 19005 7653 -1912 2349 3168 B C
ATOM 6367 O ILE A 194 -38.952 11.197 19.016 1.00 88.46 B O
ANISOU 6367 O ILE A 194 5296 20775 7540 -2246 2305 2995 B O
ATOM 6368 CB ILE A 194 -40.184 13.875 20.465 1.00 86.07 B C
ANISOU 6368 CB ILE A 194 5127 19018 8556 -999 2447 5314 B C
ATOM 6369 CG1 ILE A 194 -40.518 14.082 18.974 1.00 94.70 B C
ANISOU 6369 CG1 ILE A 194 5278 21940 8762 -1132 2362 5962 B C
ATOM 6370 CG2 ILE A 194 -40.034 15.210 21.193 1.00 85.29 B C
ANISOU 6370 CG2 ILE A 194 5261 17782 9364 -435 2647 6174 B C
ATOM 6371 CD1 ILE A 194 -41.940 13.871 18.651 1.00104.26 B C
ANISOU 6371 CD1 ILE A 194 5903 24260 9451 -1254 2271 6188 B C
ATOM 6372 N PRO A 195 -39.909 10.629 20.974 1.00 77.75 B N
ANISOU 6372 N PRO A 195 4752 17695 7093 -2070 2371 2460 B N
ATOM 6373 CA PRO A 195 -40.321 9.324 20.442 1.00 79.99 B C
ANISOU 6373 CA PRO A 195 4741 18805 6846 -2651 2386 1477 B C
ATOM 6374 C PRO A 195 -41.558 9.521 19.559 1.00 90.77 B C
ANISOU 6374 C PRO A 195 5276 21755 7455 -2794 2286 1910 B C
ATOM 6375 O PRO A 195 -42.230 10.555 19.658 1.00 92.35 B O
ANISOU 6375 O PRO A 195 5258 22107 7725 -2382 2222 2967 B O
ATOM 6376 CB PRO A 195 -40.606 8.508 21.702 1.00 76.20 B C
ANISOU 6376 CB PRO A 195 4863 17096 6994 -2663 2488 793 B C
ATOM 6377 CG PRO A 195 -40.967 9.516 22.720 1.00 77.07 B C
ANISOU 6377 CG PRO A 195 5332 16276 7674 -2114 2455 1593 B C
ATOM 6378 CD PRO A 195 -40.397 10.828 22.354 1.00 73.90 B C
ANISOU 6378 CD PRO A 195 4805 15950 7324 -1746 2421 2552 B C
ATOM 6379 N SER A 196 -41.833 8.546 18.683 1.00 91.52 B N
ANISOU 6379 N SER A 196 4852 23071 6852 -3394 2309 1090 B N
ATOM 6380 CA SER A 196 -42.954 8.544 17.741 1.00 98.91 B C
ANISOU 6380 CA SER A 196 4888 25788 6904 -3667 2215 1296 B C
ATOM 6381 C SER A 196 -44.338 8.753 18.402 1.00102.21 B C
ANISOU 6381 C SER A 196 5262 26066 7506 -3435 2165 1723 B C
ATOM 6382 O SER A 196 -45.206 9.356 17.772 1.00107.23 B O
ANISOU 6382 O SER A 196 5187 27981 7573 -3349 2045 2547 B O
ATOM 6383 CB SER A 196 -42.971 7.236 16.960 1.00107.32 B C
ANISOU 6383 CB SER A 196 5531 27865 7380 -4446 2339 -43 B C
ATOM 6384 OG SER A 196 -43.011 6.130 17.847 1.00113.27 B O
ANISOU 6384 OG SER A 196 6843 27392 8801 -4649 2548 -1116 B O
ATOM 6385 N TYR A 197 -44.539 8.296 19.661 1.00 92.39 B N
ANISOU 6385 N TYR A 197 4730 23328 7045 -3313 2263 1249 B N
ATOM 6386 CA TYR A 197 -45.836 8.426 20.335 1.00 92.00 B C
ANISOU 6386 CA TYR A 197 4680 23072 7203 -3119 2236 1557 B C
ATOM 6387 C TYR A 197 -46.148 9.883 20.725 1.00 97.92 B C
ANISOU 6387 C TYR A 197 5464 23429 8311 -2455 2160 2956 B C
ATOM 6388 O TYR A 197 -47.304 10.199 21.017 1.00 99.44 B O
ANISOU 6388 O TYR A 197 5454 23777 8552 -2277 2131 3435 B O
ATOM 6389 CB TYR A 197 -45.940 7.483 21.559 1.00 85.81 B C
ANISOU 6389 CB TYR A 197 4600 20863 7139 -3187 2390 666 B C
ATOM 6390 CG TYR A 197 -45.196 7.904 22.806 1.00 77.93 B C
ANISOU 6390 CG TYR A 197 4461 18112 7037 -2716 2438 912 B C
ATOM 6391 CD1 TYR A 197 -45.810 8.699 23.771 1.00 77.06 B C
ANISOU 6391 CD1 TYR A 197 4642 17211 7426 -2238 2411 1620 B C
ATOM 6392 CD2 TYR A 197 -43.925 7.414 23.080 1.00 73.97 B C
ANISOU 6392 CD2 TYR A 197 4447 16764 6893 -2794 2542 338 B C
ATOM 6393 CE1 TYR A 197 -45.163 9.024 24.961 1.00 70.85 B C
ANISOU 6393 CE1 TYR A 197 4580 14941 7398 -1883 2478 1708 B C
ATOM 6394 CE2 TYR A 197 -43.270 7.729 24.269 1.00 67.75 B C
ANISOU 6394 CE2 TYR A 197 4382 14506 6852 -2407 2583 502 B C
ATOM 6395 CZ TYR A 197 -43.880 8.565 25.191 1.00 71.86 B C
ANISOU 6395 CZ TYR A 197 5148 14372 7782 -1967 2546 1173 B C
ATOM 6396 OH TYR A 197 -43.239 8.921 26.350 1.00 67.42 B O
ANISOU 6396 OH TYR A 197 5217 12522 7876 -1638 2599 1278 B O
ATOM 6397 N LEU A 198 -45.131 10.766 20.686 1.00 93.88 B N
ANISOU 6397 N LEU A 198 5153 22423 8093 -2111 2175 3590 B N
ATOM 6398 CA LEU A 198 -45.285 12.165 21.070 1.00 93.05 B C
ANISOU 6398 CA LEU A 198 5064 21779 8510 -1500 2219 4842 B C
ATOM 6399 C LEU A 198 -45.552 13.126 19.878 1.00103.85 B C
ANISOU 6399 C LEU A 198 5527 24602 9331 -1331 2174 6052 B C
ATOM 6400 O LEU A 198 -45.696 14.331 20.111 1.00104.00 B O
ANISOU 6400 O LEU A 198 5446 24187 9881 -808 2294 7185 B O
ATOM 6401 CB LEU A 198 -44.075 12.625 21.899 1.00 86.58 B C
ANISOU 6401 CB LEU A 198 4996 19401 8499 -1194 2336 4823 B C
ATOM 6402 CG LEU A 198 -44.030 12.126 23.351 1.00 83.62 B C
ANISOU 6402 CG LEU A 198 5446 17493 8834 -1136 2410 4126 B C
ATOM 6403 CD1 LEU A 198 -42.866 12.739 24.080 1.00 78.83 B C
ANISOU 6403 CD1 LEU A 198 5418 15616 8917 -837 2522 4229 B C
ATOM 6404 CD2 LEU A 198 -45.316 12.467 24.113 1.00 85.58 B C
ANISOU 6404 CD2 LEU A 198 5688 17413 9418 -898 2454 4512 B C
ATOM 6405 N ILE A 199 -45.688 12.614 18.624 1.00107.27 B N
ANISOU 6405 N ILE A 199 5224 26800 8736 -1771 2046 5853 B N
ATOM 6406 CA ILE A 199 -46.052 13.498 17.497 1.00116.15 B C
ANISOU 6406 CA ILE A 199 5371 29512 9251 -1599 1996 7124 B C
ATOM 6407 C ILE A 199 -47.574 13.762 17.603 1.00124.94 B C
ANISOU 6407 C ILE A 199 5969 31266 10238 -1454 1963 7777 B C
ATOM 6408 O ILE A 199 -48.328 12.828 17.887 1.00123.72 B O
ANISOU 6408 O ILE A 199 5880 31286 9841 -1822 1894 6882 B O
ATOM 6409 CB ILE A 199 -45.613 13.020 16.065 1.00126.02 B C
ANISOU 6409 CB ILE A 199 5896 32627 9359 -2102 1877 6825 B C
ATOM 6410 CG1 ILE A 199 -46.423 11.826 15.534 1.00130.67 B C
ANISOU 6410 CG1 ILE A 199 6018 34587 9043 -2794 1770 5741 B C
ATOM 6411 CG2 ILE A 199 -44.107 12.786 15.940 1.00122.36 B C
ANISOU 6411 CG2 ILE A 199 5924 31504 9062 -2225 1929 6232 B C
ATOM 6412 CD1 ILE A 199 -47.452 12.175 14.477 1.00137.30 B C
ANISOU 6412 CD1 ILE A 199 6893 35341 9935 -2640 1699 5789 B C
ATOM 6413 N ALA A 200 -48.018 15.020 17.430 1.00126.43 B N
ANISOU 6413 N ALA A 200 5653 31685 10699 -905 2059 9329 B N
ATOM 6414 CA ALA A 200 -49.445 15.353 17.548 1.00130.25 B C
ANISOU 6414 CA ALA A 200 5684 32616 11191 -713 2057 10009 B C
ATOM 6415 C ALA A 200 -49.923 16.289 16.450 1.00134.04 B C
ANISOU 6415 C ALA A 200 6454 32490 11987 -476 2050 10097 B C
ATOM 6416 O ALA A 200 -49.123 17.041 15.901 1.00133.08 B O
ANISOU 6416 O ALA A 200 6405 32068 12093 -253 2135 10545 B O
ATOM 6417 CB ALA A 200 -49.723 15.986 18.898 1.00125.41 B C
ANISOU 6417 CB ALA A 200 5699 30153 11796 -220 2276 10360 B C
ATOM 6418 N LEU A 201 -51.239 16.258 16.149 1.00133.02 B N
ANISOU 6418 N LEU A 201 6205 32614 11721 -523 1956 9960 B N
ATOM 6419 CA LEU A 201 -51.846 17.138 15.149 1.00133.36 B C
ANISOU 6419 CA LEU A 201 6345 32376 11948 -318 1933 10189 B C
ATOM 6420 C LEU A 201 -53.316 17.419 15.474 1.00136.45 B C
ANISOU 6420 C LEU A 201 6897 32213 12733 -168 1925 10177 B C
ATOM 6421 O LEU A 201 -54.078 16.486 15.724 1.00136.36 B O
ANISOU 6421 O LEU A 201 6745 32712 12355 -459 1812 9626 B O
ATOM 6422 CB LEU A 201 -51.719 16.538 13.726 1.00134.12 B C
ANISOU 6422 CB LEU A 201 6457 33136 11367 -714 1743 9327 B C
ATOM 6423 CG LEU A 201 -52.430 17.277 12.577 1.00138.01 B C
ANISOU 6423 CG LEU A 201 7227 33145 12065 -563 1679 9264 B C
ATOM 6424 CD1 LEU A 201 -51.877 18.697 12.386 1.00137.74 B C
ANISOU 6424 CD1 LEU A 201 7342 32420 12572 -139 1830 10092 B C
ATOM 6425 CD2 LEU A 201 -52.371 16.475 11.294 1.00140.69 B C
ANISOU 6425 CD2 LEU A 201 7698 33860 11899 -945 1514 8284 B C
ATOM 6426 N VAL A 202 -53.702 18.710 15.442 1.00134.11 B N
ANISOU 6426 N VAL A 202 6623 31287 13044 270 2065 11013 B N
ATOM 6427 CA VAL A 202 -55.076 19.197 15.599 1.00134.24 B C
ANISOU 6427 CA VAL A 202 6648 30966 13391 447 2073 11212 B C
ATOM 6428 C VAL A 202 -55.351 20.184 14.462 1.00137.30 B C
ANISOU 6428 C VAL A 202 7341 30858 13968 570 2031 11138 B C
ATOM 6429 O VAL A 202 -54.516 21.053 14.198 1.00136.36 B O
ANISOU 6429 O VAL A 202 7324 30329 14156 781 2160 11572 B O
ATOM 6430 CB VAL A 202 -55.429 19.794 16.998 1.00136.26 B C
ANISOU 6430 CB VAL A 202 7092 30159 14523 799 2311 11722 B C
ATOM 6431 CG1 VAL A 202 -54.561 21.001 17.347 1.00135.35 B C
ANISOU 6431 CG1 VAL A 202 7148 29069 15209 1199 2598 12444 B C
ATOM 6432 CG2 VAL A 202 -56.912 20.157 17.093 1.00136.26 B C
ANISOU 6432 CG2 VAL A 202 7064 29956 14754 914 2295 11814 B C
ATOM 6433 N VAL A 203 -56.498 20.008 13.764 1.00135.97 B N
ANISOU 6433 N VAL A 203 7036 31137 13490 455 1867 10882 B N
ATOM 6434 CA VAL A 203 -56.973 20.874 12.676 1.00136.13 B C
ANISOU 6434 CA VAL A 203 7162 30973 13587 576 1810 10973 B C
ATOM 6435 C VAL A 203 -58.475 21.156 12.912 1.00139.34 B C
ANISOU 6435 C VAL A 203 7703 30939 14302 663 1770 10843 B C
ATOM 6436 O VAL A 203 -59.300 20.244 12.855 1.00139.38 B O
ANISOU 6436 O VAL A 203 7557 31457 13945 432 1622 10379 B O
ATOM 6437 CB VAL A 203 -56.705 20.321 11.243 1.00139.29 B C
ANISOU 6437 CB VAL A 203 7727 31763 13434 267 1602 10189 B C
ATOM 6438 CG1 VAL A 203 -57.189 21.305 10.182 1.00139.38 B C
ANISOU 6438 CG1 VAL A 203 7853 31529 13577 431 1558 10379 B C
ATOM 6439 CG2 VAL A 203 -55.230 19.991 11.030 1.00138.97 B C
ANISOU 6439 CG2 VAL A 203 7716 31947 13141 136 1634 10064 B C
ATOM 6440 N GLY A 204 -58.803 22.418 13.170 1.00136.93 B N
ANISOU 6440 N GLY A 204 7399 30060 14566 1018 1932 11550 B N
ATOM 6441 CA GLY A 204 -60.176 22.852 13.405 1.00137.12 B C
ANISOU 6441 CA GLY A 204 7408 29814 14876 1150 1927 11661 B C
ATOM 6442 C GLY A 204 -60.313 24.347 13.575 1.00140.17 B C
ANISOU 6442 C GLY A 204 8144 29114 15999 1459 2101 11976 B C
ATOM 6443 O GLY A 204 -59.336 25.080 13.412 1.00139.22 B O
ANISOU 6443 O GLY A 204 8128 28643 16127 1596 2240 12294 B O
ATOM 6444 N ALA A 205 -61.536 24.813 13.882 1.00139.13 B N
ANISOU 6444 N ALA A 205 7926 28780 16157 1607 2132 12199 B N
ATOM 6445 CA ALA A 205 -61.817 26.233 14.116 1.00138.99 B C
ANISOU 6445 CA ALA A 205 8069 27927 16814 1903 2326 12630 B C
ATOM 6446 C ALA A 205 -61.348 26.588 15.528 1.00141.81 B C
ANISOU 6446 C ALA A 205 8661 27358 17862 2056 2597 12778 B C
ATOM 6447 O ALA A 205 -62.121 26.501 16.488 1.00141.66 B O
ANISOU 6447 O ALA A 205 8593 27076 18153 2132 2687 12870 B O
ATOM 6448 CB ALA A 205 -63.304 26.514 13.933 1.00139.97 B C
ANISOU 6448 CB ALA A 205 8189 28007 16987 1934 2224 12503 B C
ATOM 6449 N LEU A 206 -60.053 26.919 15.660 1.00139.16 B N
ANISOU 6449 N LEU A 206 8298 26813 17764 2170 2787 13178 B N
ATOM 6450 CA LEU A 206 -59.434 27.188 16.957 1.00138.27 B C
ANISOU 6450 CA LEU A 206 8251 25933 18351 2357 3101 13525 B C
ATOM 6451 C LEU A 206 -59.112 28.655 17.182 1.00140.34 B C
ANISOU 6451 C LEU A 206 8838 25112 19373 2561 3348 13650 B C
ATOM 6452 O LEU A 206 -58.750 29.373 16.247 1.00140.42 B O
ANISOU 6452 O LEU A 206 8925 25128 19300 2574 3311 13673 B O
ATOM 6453 CB LEU A 206 -58.134 26.366 17.124 1.00138.21 B C
ANISOU 6453 CB LEU A 206 8211 26197 18105 2248 3109 13476 B C
ATOM 6454 CG LE | 
