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*** 6y7f_apo ***elNémo ID: 2402150026362836896Job options:ID = 2402150026362836896 JOBID = 6y7f_apo USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 6y7f_apo CRYST1 63.229 72.459 112.043 90.00 100.03 90.00 P 1 21 1 4 ATOM 1 N ASN A 16 32.488 31.311 42.009 1.00 81.22 A N ANISOU 1 N ASN A 16 13518 9176 8165 -402 -4775 1022 A N ATOM 2 CA ASN A 16 31.321 31.403 42.888 1.00 81.25 A C ANISOU 2 CA ASN A 16 14012 8963 7894 -494 -4654 993 A C ATOM 3 C ASN A 16 30.054 31.660 42.069 1.00 80.20 A C ANISOU 3 C ASN A 16 13944 8727 7801 -510 -4248 880 A C ATOM 4 O ASN A 16 29.018 31.053 42.317 1.00 80.54 A O ANISOU 4 O ASN A 16 14253 8606 7743 -446 -4062 884 A O ATOM 5 CB ASN A 16 31.519 32.497 43.948 1.00 82.55 A C ANISOU 5 CB ASN A 16 14429 9125 7812 -751 -4854 974 A C ATOM 6 N TRP A 17 30.151 32.533 41.076 1.00 78.98 A N ANISOU 6 N TRP A 17 13535 8676 7798 -597 -4118 790 A N ATOM 7 CA TRP A 17 29.049 32.880 40.178 1.00 78.50 A C ANISOU 7 CA TRP A 17 13485 8544 7796 -611 -3759 686 A C ATOM 8 C TRP A 17 28.660 31.691 39.264 1.00 76.97 A C ANISOU 8 C TRP A 17 13145 8318 7784 -384 -3572 700 A C ATOM 9 O TRP A 17 27.480 31.506 38.957 1.00 77.04 A O ANISOU 9 O TRP A 17 13299 8206 7767 -366 -3306 652 A O ATOM 10 CB TRP A 17 29.469 34.100 39.351 1.00 78.73 A C ANISOU 10 CB TRP A 17 13269 8703 7943 -761 -3722 606 A C ATOM 11 CG TRP A 17 28.594 34.443 38.197 1.00 79.50 A C ANISOU 11 CG TRP A 17 13285 8770 8151 -750 -3393 512 A C ATOM 12 CD1 TRP A 17 27.467 35.209 38.216 1.00 80.61 A C ANISOU 12 CD1 TRP A 17 13662 8793 8173 -849 -3172 427 A C ATOM 13 CD2 TRP A 17 28.870 34.166 36.824 1.00 79.75 A C ANISOU 13 CD2 TRP A 17 12959 8911 8430 -640 -3266 493 A C ATOM 14 CE2 TRP A 17 27.844 34.758 36.060 1.00 80.55 A C ANISOU 14 CE2 TRP A 17 13111 8947 8546 -687 -2982 400 A C ATOM 15 CE3 TRP A 17 29.880 33.458 36.163 1.00 80.20 A C ANISOU 15 CE3 TRP A 17 12665 9117 8691 -490 -3359 546 A C ATOM 16 NE1 TRP A 17 26.997 35.389 36.934 1.00 80.95 A N ANISOU 16 NE1 TRP A 17 13515 8863 8381 -807 -2930 364 A N ATOM 17 CZ2 TRP A 17 27.802 34.660 34.678 1.00 81.04 A C ANISOU 17 CZ2 TRP A 17 12906 9082 8804 -608 -2805 360 A C ATOM 18 CZ3 TRP A 17 29.829 33.360 34.793 1.00 80.78 A C ANISOU 18 CZ3 TRP A 17 12478 9260 8955 -403 -3158 499 A C ATOM 19 CH2 TRP A 17 28.790 33.938 34.070 1.00 80.97 A C ANISOU 19 CH2 TRP A 17 12582 9208 8974 -469 -2890 408 A C ATOM 20 N ILE A 18 29.641 30.866 38.871 1.00 75.32 A N ANISOU 20 N ILE A 18 12658 8212 7747 -209 -3719 769 A N ATOM 21 CA ILE A 18 29.371 29.689 38.041 1.00 74.12 A C ANISOU 21 CA ILE A 18 12403 8008 7752 18 -3569 779 A C ATOM 22 C ILE A 18 28.767 28.518 38.863 1.00 72.27 A C ANISOU 22 C ILE A 18 12497 7579 7383 128 -3587 858 A C ATOM 23 O ILE A 18 28.386 27.512 38.274 1.00 73.11 A O ANISOU 23 O ILE A 18 12597 7595 7587 291 -3458 865 A O ATOM 24 CB ILE A 18 30.641 29.234 37.285 1.00 74.84 A C ANISOU 24 CB ILE A 18 12086 8275 8074 197 -3694 818 A C ATOM 25 N LYS A 19 28.663 28.638 40.201 1.00 69.60 A N ANISOU 25 N LYS A 19 12469 7165 6811 29 -3743 918 A N ATOM 26 CA LYS A 19 28.027 27.599 41.019 1.00 67.31 A C ANISOU 26 CA LYS A 19 12524 6684 6368 101 -3741 1001 A C ATOM 27 C LYS A 19 26.491 27.578 40.803 1.00 63.78 A C ANISOU 27 C LYS A 19 12291 6092 5851 22 -3404 940 A C ATOM 28 O LYS A 19 25.846 26.615 41.191 1.00 64.89 A O ANISOU 28 O LYS A 19 12670 6075 5911 79 -3341 1005 A O ATOM 29 CB LYS A 19 28.359 27.781 42.515 1.00 69.15 A C ANISOU 29 CB LYS A 19 13043 6885 6345 9 -4000 1085 A C ATOM 30 N ASP A 20 25.912 28.631 40.215 1.00 59.67 A N ANISOU 30 N ASP A 20 11688 5625 5359 -111 -3198 827 A N ATOM 31 CA ASP A 20 24.484 28.708 39.922 1.00 56.78 A C ANISOU 31 CA ASP A 20 11462 5160 4953 -177 -2883 769 A C ATOM 32 C ASP A 20 24.133 28.215 38.501 1.00 52.51 A C ANISOU 32 C ASP A 20 10682 4627 4644 -76 -2692 717 A C ATOM 33 O ASP A 20 22.980 28.317 38.095 1.00 51.60 A O ANISOU 33 O ASP A 20 10623 4456 4527 -135 -2443 667 A O ATOM 34 CB ASP A 20 23.997 30.160 40.066 1.00 59.32 A C ANISOU 34 CB ASP A 20 11844 5526 5169 -356 -2765 676 A C ATOM 35 CG ASP A 20 23.844 30.631 41.489 1.00 67.18 A C ANISOU 35 CG ASP A 20 13185 6461 5881 -475 -2854 705 A C ATOM 36 OD1 ASP A 20 23.752 29.777 42.386 1.00 68.40 A O ANISOU 36 OD1 ASP A 20 13577 6518 5893 -437 -2936 803 A O ATOM 37 OD2 ASP A 20 23.809 31.862 41.704 1.00 71.90 A O1- ANISOU 37 OD2 ASP A 20 13840 7095 6384 -606 -2839 630 A O1- ATOM 38 N ALA A 21 25.118 27.731 37.739 1.00 49.72 A N ANISOU 38 N ALA A 21 10058 4352 4481 75 -2807 725 A N ATOM 39 CA ALA A 21 24.893 27.276 36.388 1.00 48.22 A C ANISOU 39 CA ALA A 21 9664 4168 4489 177 -2642 668 A C ATOM 40 C ALA A 21 24.107 25.960 36.377 1.00 46.59 A C ANISOU 40 C ALA A 21 9652 3777 4272 260 -2548 714 A C ATOM 41 O ALA A 21 24.142 25.189 37.340 1.00 46.47 A O ANISOU 41 O ALA A 21 9874 3646 4139 298 -2669 813 A O ATOM 42 CB ALA A 21 26.220 27.115 35.666 1.00 48.39 A C ANISOU 42 CB ALA A 21 9359 4329 4696 330 -2783 667 A C ATOM 43 N ASP A 22 23.367 25.732 35.296 1.00 44.97 A N ANISOU 43 N ASP A 22 9368 3540 4180 269 -2339 646 A N ATOM 44 CA ASP A 22 22.575 24.527 35.105 1.00 44.20 A C ANISOU 44 CA ASP A 22 9439 3266 4089 314 -2242 677 A C ATOM 45 C ASP A 22 23.522 23.384 34.777 1.00 44.11 A C ANISOU 45 C ASP A 22 9375 3197 4187 544 -2391 718 A C ATOM 46 O ASP A 22 24.134 23.420 33.706 1.00 44.40 A O ANISOU 46 O ASP A 22 9156 3326 4386 664 -2375 651 A O ATOM 47 CB ASP A 22 21.575 24.783 33.962 1.00 43.85 A C ANISOU 47 CB ASP A 22 9293 3233 4136 239 -1999 582 A C ATOM 48 CG ASP A 22 20.622 23.659 33.596 1.00 44.25 A C ANISOU 48 CG ASP A 22 9495 3114 4205 235 -1883 599 A C ATOM 49 OD1 ASP A 22 20.743 22.562 34.179 1.00 45.12 A O ANISOU 49 OD1 ASP A 22 9810 3070 4264 302 -1982 686 A O ATOM 50 OD2 ASP A 22 19.756 23.879 32.725 1.00 42.86 A O1- ANISOU 50 OD2 ASP A 22 9240 2954 4092 156 -1706 529 A O1- ATOM 51 N PRO A 23 23.680 22.361 35.655 1.00 43.56 A N ANISOU 51 N PRO A 23 9548 2973 4028 623 -2530 829 A N ATOM 52 CA PRO A 23 24.624 21.274 35.327 1.00 43.20 A C ANISOU 52 CA PRO A 23 9458 2864 4093 882 -2676 868 A C ATOM 53 C PRO A 23 24.237 20.471 34.084 1.00 43.94 A C ANISOU 53 C PRO A 23 9522 2851 4321 979 -2528 798 A C ATOM 54 O PRO A 23 25.090 19.770 33.554 1.00 45.01 A O ANISOU 54 O PRO A 23 9563 2968 4573 1218 -2612 795 A O ATOM 55 CB PRO A 23 24.635 20.380 36.592 1.00 43.14 A C ANISOU 55 CB PRO A 23 9784 2676 3929 916 -2839 1010 A C ATOM 56 CG PRO A 23 23.411 20.700 37.325 1.00 43.62 A C ANISOU 56 CG PRO A 23 10094 2666 3814 668 -2704 1035 A C ATOM 57 CD PRO A 23 23.058 22.161 36.980 1.00 42.65 A C ANISOU 57 CD PRO A 23 9766 2738 3702 498 -2560 928 A C ATOM 58 N ARG A 24 22.991 20.556 33.608 1.00 43.42 A N ANISOU 58 N ARG A 24 9536 2722 4241 808 -2317 742 A N ATOM 59 CA ARG A 24 22.564 19.764 32.443 1.00 43.03 A C ANISOU 59 CA ARG A 24 9495 2556 4298 873 -2196 673 A C ATOM 60 C ARG A 24 23.304 20.138 31.175 1.00 42.85 A C ANISOU 60 C ARG A 24 9159 2686 4437 1015 -2154 564 A C ATOM 61 O ARG A 24 23.466 19.294 30.300 1.00 42.96 A O ANISOU 61 O ARG A 24 9185 2600 4537 1171 -2124 517 A O ATOM 62 CB ARG A 24 21.056 19.937 32.182 1.00 43.54 A C ANISOU 62 CB ARG A 24 9661 2565 4317 629 -1991 639 A C ATOM 63 CG ARG A 24 20.174 19.449 33.317 1.00 44.57 A C ANISOU 63 CG ARG A 24 10105 2540 4291 471 -1983 750 A C ATOM 64 CD ARG A 24 18.709 19.733 33.052 1.00 43.23 A C ANISOU 64 CD ARG A 24 9966 2367 4093 231 -1773 722 A C ATOM 65 NE ARG A 24 18.447 21.155 32.850 1.00 41.07 A N ANISOU 65 NE ARG A 24 9468 2309 3826 130 -1663 650 A N ATOM 66 CZ ARG A 24 17.267 21.661 32.498 1.00 40.19 A C ANISOU 66 CZ ARG A 24 9305 2251 3714 -46 -1479 612 A C ATOM 67 NH1 ARG A 24 16.218 20.864 32.338 1.00 38.43 A N1+ ANISOU 67 NH1 ARG A 24 9219 1899 3483 -167 -1385 645 A N1+ ATOM 68 NH2 ARG A 24 17.118 22.977 32.345 1.00 37.66 A N ANISOU 68 NH2 ARG A 24 8801 2111 3397 -105 -1394 549 A N ATOM 69 N VAL A 25 23.723 21.414 31.043 1.00 41.92 A N ANISOU 69 N VAL A 25 8779 2801 4348 953 -2141 519 A N ATOM 70 CA VAL A 25 24.362 21.873 29.806 1.00 41.37 A C ANISOU 70 CA VAL A 25 8407 2893 4419 1053 -2073 421 A C ATOM 71 C VAL A 25 25.906 21.891 29.888 1.00 43.14 A C ANISOU 71 C VAL A 25 8403 3260 4726 1266 -2236 453 A C ATOM 72 O VAL A 25 26.536 22.270 28.909 1.00 43.95 A O ANISOU 72 O VAL A 25 8238 3517 4944 1354 -2174 384 A O ATOM 73 CB VAL A 25 23.838 23.283 29.417 1.00 39.85 A C ANISOU 73 CB VAL A 25 8056 2864 4220 844 -1937 351 A C ATOM 74 CG1 VAL A 25 22.309 23.329 29.426 1.00 39.71 A C ANISOU 74 CG1 VAL A 25 8226 2737 4127 644 -1785 334 A C ATOM 75 CG2 VAL A 25 24.418 24.350 30.340 1.00 38.81 A C ANISOU 75 CG2 VAL A 25 7833 2884 4029 753 -2054 396 A C ATOM 76 N GLU A 26 26.501 21.503 31.021 1.00 44.09 A N ANISOU 76 N GLU A 26 8619 3343 4788 1345 -2440 562 A N ATOM 77 CA GLU A 26 27.949 21.523 31.248 1.00 46.04 A C ANISOU 77 CA GLU A 26 8636 3744 5112 1538 -2627 615 A C ATOM 78 C GLU A 26 28.806 21.034 30.063 1.00 48.04 A C ANISOU 78 C GLU A 26 8645 4072 5534 1807 -2574 558 A C ATOM 79 O GLU A 26 29.693 21.771 29.628 1.00 48.83 A O ANISOU 79 O GLU A 26 8408 4416 5731 1839 -2583 536 A O ATOM 80 CB GLU A 26 28.305 20.695 32.484 1.00 47.92 A C ANISOU 80 CB GLU A 26 9092 3852 5263 1647 -2853 747 A C ATOM 81 N ASP A 27 28.554 19.814 29.548 1.00 48.28 A N ANISOU 81 N ASP A 27 8856 3895 5591 1992 -2515 534 A N ATOM 82 CA ASP A 27 29.347 19.224 28.478 1.00 48.81 A C ANISOU 82 CA ASP A 27 8750 4002 5795 2284 -2455 476 A C ATOM 83 C ASP A 27 28.957 19.652 27.059 1.00 47.31 A C ANISOU 83 C ASP A 27 8429 3883 5663 2226 -2215 338 A C ATOM 84 O ASP A 27 29.546 19.152 26.091 1.00 48.15 A O ANISOU 84 O ASP A 27 8419 4013 5862 2468 -2133 276 A O ATOM 85 CB ASP A 27 29.234 17.707 28.568 1.00 52.79 A C ANISOU 85 CB ASP A 27 9562 4214 6281 2514 -2504 505 A C ATOM 86 CG ASP A 27 29.942 17.143 29.795 1.00 63.70 A C ANISOU 86 CG ASP A 27 11032 5542 7630 2672 -2760 650 A C ATOM 87 OD1 ASP A 27 30.900 17.801 30.293 1.00 66.49 A O ANISOU 87 OD1 ASP A 27 11105 6134 8025 2704 -2905 713 A O ATOM 88 OD2 ASP A 27 29.552 16.039 30.258 1.00 66.84 A O1- ANISOU 88 OD2 ASP A 27 11784 5655 7957 2756 -2827 706 A O1- ATOM 89 N TRP A 28 27.967 20.516 26.919 1.00 44.74 A N ANISOU 89 N TRP A 28 8142 3583 5276 1930 -2099 290 A N ATOM 90 CA TRP A 28 27.482 20.899 25.596 1.00 43.43 A C ANISOU 90 CA TRP A 28 7892 3463 5145 1863 -1887 168 A C ATOM 91 C TRP A 28 28.417 21.889 24.897 1.00 43.94 A C ANISOU 91 C TRP A 28 7572 3821 5304 1889 -1828 132 A C ATOM 92 O TRP A 28 29.115 22.660 25.555 1.00 44.00 A O ANISOU 92 O TRP A 28 7380 4009 5327 1829 -1942 198 A O ATOM 93 CB TRP A 28 26.045 21.447 25.706 1.00 41.54 A C ANISOU 93 CB TRP A 28 7827 3145 4810 1553 -1792 143 A C ATOM 94 CG TRP A 28 25.027 20.443 26.199 1.00 39.67 A C ANISOU 94 CG TRP A 28 7952 2632 4489 1498 -1810 175 A C ATOM 95 CD1 TRP A 28 25.239 19.140 26.590 1.00 39.49 A C ANISOU 95 CD1 TRP A 28 8153 2397 4453 1678 -1911 226 A C ATOM 96 CD2 TRP A 28 23.625 20.680 26.345 1.00 38.54 A C ANISOU 96 CD2 TRP A 28 7983 2397 4262 1236 -1721 167 A C ATOM 97 CE2 TRP A 28 23.042 19.478 26.806 1.00 39.22 A C ANISOU 97 CE2 TRP A 28 8387 2224 4291 1244 -1766 216 A C ATOM 98 CE3 TRP A 28 22.798 21.776 26.085 1.00 38.03 A C ANISOU 98 CE3 TRP A 28 7833 2444 4172 1004 -1602 125 A C ATOM 99 NE1 TRP A 28 24.059 18.573 26.996 1.00 39.04 A N ANISOU 99 NE1 TRP A 28 8408 2120 4305 1514 -1891 255 A N ATOM 100 CZ2 TRP A 28 21.673 19.362 27.035 1.00 39.42 A C ANISOU 100 CZ2 TRP A 28 8615 2126 4238 1007 -1692 231 A C ATOM 101 CZ3 TRP A 28 21.452 21.665 26.339 1.00 38.54 A C ANISOU 101 CZ3 TRP A 28 8091 2389 4162 802 -1532 139 A C ATOM 102 CH2 TRP A 28 20.899 20.469 26.802 1.00 38.68 A C ANISOU 102 CH2 TRP A 28 8393 2175 4129 795 -1573 193 A C ATOM 103 N LEU A 29 28.468 21.816 23.550 1.00 43.73 A N ANISOU 103 N LEU A 29 7451 3834 5329 1978 -1653 30 A N ATOM 104 CA LEU A 29 29.313 22.663 22.717 1.00 44.04 A C ANISOU 104 CA LEU A 29 7141 4142 5449 2004 -1558 -7 A C ATOM 105 C LEU A 29 29.214 24.149 23.093 1.00 43.33 A C ANISOU 105 C LEU A 29 6894 4233 5338 1715 -1576 23 A C ATOM 106 O LEU A 29 28.112 24.702 23.147 1.00 43.82 A O ANISOU 106 O LEU A 29 7112 4219 5320 1481 -1519 -4 A O ATOM 107 CB LEU A 29 28.941 22.493 21.238 1.00 44.65 A C ANISOU 107 CB LEU A 29 7243 4193 5529 2053 -1344 -129 A C ATOM 108 CG LEU A 29 30.087 22.713 20.265 1.00 46.20 A C ANISOU 108 CG LEU A 29 7121 4617 5815 2235 -1231 -164 A C ATOM 109 CD1 LEU A 29 31.112 21.608 20.416 1.00 46.26 A C ANISOU 109 CD1 LEU A 29 7075 4604 5896 2596 -1297 -134 A C ATOM 110 CD2 LEU A 29 29.585 22.771 18.830 1.00 46.84 A C ANISOU 110 CD2 LEU A 29 7257 4680 5859 2221 -1016 -285 A C ATOM 111 N LEU A 30 30.370 24.735 23.429 1.00 42.59 A N ANISOU 111 N LEU A 30 6503 4367 5312 1739 -1672 86 A N ATOM 112 CA LEU A 30 30.604 26.126 23.809 1.00 42.64 A C ANISOU 112 CA LEU A 30 6333 4558 5309 1488 -1720 123 A C ATOM 113 C LEU A 30 30.102 26.496 25.207 1.00 42.69 A C ANISOU 113 C LEU A 30 6531 4475 5214 1297 -1889 190 A C ATOM 114 O LEU A 30 30.207 27.666 25.572 1.00 42.74 A O ANISOU 114 O LEU A 30 6449 4599 5191 1077 -1934 210 A O ATOM 115 CB LEU A 30 29.987 27.083 22.796 1.00 43.15 A C ANISOU 115 CB LEU A 30 6366 4677 5351 1300 -1526 42 A C ATOM 116 CG LEU A 30 30.675 27.125 21.451 1.00 45.46 A C ANISOU 116 CG LEU A 30 6415 5130 5726 1426 -1359 -10 A C ATOM 117 CD1 LEU A 30 29.914 28.015 20.490 1.00 45.70 A C ANISOU 117 CD1 LEU A 30 6480 5176 5707 1234 -1181 -83 A C ATOM 118 CD2 LEU A 30 32.108 27.624 21.595 1.00 46.81 A C ANISOU 118 CD2 LEU A 30 6212 5575 5997 1460 -1434 62 A C ATOM 119 N MET A 31 29.629 25.528 26.011 1.00 42.54 A N ANISOU 119 N MET A 31 6783 4248 5132 1377 -1985 228 A N ATOM 120 CA MET A 31 29.050 25.874 27.299 1.00 43.21 A C ANISOU 120 CA MET A 31 7083 4241 5094 1191 -2112 287 A C ATOM 121 C MET A 31 30.015 25.790 28.490 1.00 45.08 A C ANISOU 121 C MET A 31 7260 4549 5319 1242 -2368 396 A C ATOM 122 O MET A 31 29.604 26.137 29.590 1.00 44.97 A O ANISOU 122 O MET A 31 7436 4468 5182 1082 -2478 444 A O ATOM 123 CB MET A 31 27.794 25.035 27.563 1.00 42.35 A C ANISOU 123 CB MET A 31 7331 3868 4893 1176 -2055 276 A C ATOM 124 CG MET A 31 26.699 25.213 26.501 1.00 41.68 A C ANISOU 124 CG MET A 31 7316 3719 4803 1079 -1831 176 A C ATOM 125 SD MET A 31 26.300 26.937 26.054 1.00 41.35 A S ANISOU 125 SD MET A 31 7131 3838 4741 817 -1712 121 A S ATOM 126 CE MET A 31 25.909 27.633 27.670 1.00 38.63 A C ANISOU 126 CE MET A 31 6964 3455 4257 616 -1844 194 A C ATOM 127 N SER A 32 31.293 25.445 28.274 1.00 46.83 A N ANISOU 127 N SER A 32 7206 4926 5662 1450 -2462 438 A N ATOM 128 CA SER A 32 32.267 25.330 29.376 1.00 48.85 A C ANISOU 128 CA SER A 32 7375 5268 5916 1513 -2735 553 A C ATOM 129 C SER A 32 32.529 26.684 30.038 1.00 48.99 A C ANISOU 129 C SER A 32 7296 5441 5876 1228 -2855 583 A C ATOM 130 O SER A 32 32.577 26.768 31.263 1.00 49.54 A O ANISOU 130 O SER A 32 7519 5467 5837 1143 -3063 657 A O ATOM 131 CB SER A 32 33.584 24.735 28.878 1.00 52.14 A C ANISOU 131 CB SER A 32 7461 5853 6497 1810 -2790 590 A C ATOM 132 OG SER A 32 34.033 25.499 27.765 1.00 57.61 A O ANISOU 132 OG SER A 32 7828 6765 7295 1760 -2627 529 A O ATOM 133 N SER A 33 32.666 27.739 29.242 1.00 48.35 A N ANISOU 133 N SER A 33 6998 5522 5850 1071 -2727 524 A N ATOM 134 CA SER A 33 32.908 29.094 29.746 1.00 48.71 A C ANISOU 134 CA SER A 33 6971 5696 5841 781 -2828 541 A C ATOM 135 C SER A 33 32.527 30.132 28.665 1.00 48.68 A C ANISOU 135 C SER A 33 6868 5762 5866 606 -2601 451 A C ATOM 136 O SER A 33 32.376 29.761 27.493 1.00 48.80 A O ANISOU 136 O SER A 33 6790 5785 5965 736 -2396 391 A O ATOM 137 CB SER A 33 34.371 29.250 30.178 1.00 50.51 A C ANISOU 137 CB SER A 33 6873 6161 6157 815 -3069 638 A C ATOM 138 OG SER A 33 35.225 29.773 29.173 1.00 53.16 A O ANISOU 138 OG SER A 33 6812 6744 6644 807 -2979 627 A O ATOM 139 N PRO A 34 32.348 31.426 29.017 1.00 48.31 A N ANISOU 139 N PRO A 34 6870 5749 5738 317 -2634 440 A N ATOM 140 CA PRO A 34 32.015 32.414 27.974 1.00 48.67 A C ANISOU 140 CA PRO A 34 6837 5848 5808 162 -2428 366 A C ATOM 141 C PRO A 34 33.216 32.814 27.103 1.00 49.81 A C ANISOU 141 C PRO A 34 6569 6254 6101 161 -2405 390 A C ATOM 142 O PRO A 34 33.029 33.557 26.145 1.00 50.06 A O ANISOU 142 O PRO A 34 6528 6338 6156 49 -2228 339 A O ATOM 143 CB PRO A 34 31.491 33.610 28.770 1.00 48.84 A C ANISOU 143 CB PRO A 34 7079 5794 5682 -124 -2495 355 A C ATOM 144 CG PRO A 34 32.111 33.483 30.111 1.00 48.88 A C ANISOU 144 CG PRO A 34 7133 5817 5621 -157 -2779 436 A C ATOM 145 CD PRO A 34 32.452 32.049 30.353 1.00 47.37 A C ANISOU 145 CD PRO A 34 6904 5607 5487 124 -2862 491 A C ATOM 146 N LEU A 35 34.438 32.319 27.421 1.00 50.35 A N ANISOU 146 N LEU A 35 6366 6496 6270 290 -2578 474 A N ATOM 147 CA LEU A 35 35.681 32.657 26.724 1.00 51.03 A C ANISOU 147 CA LEU A 35 6015 6869 6506 291 -2570 518 A C ATOM 148 C LEU A 35 35.734 32.165 25.260 1.00 50.08 A C ANISOU 148 C LEU A 35 5722 6815 6492 493 -2294 462 A C ATOM 149 O LEU A 35 35.971 33.016 24.402 1.00 50.28 A O ANISOU 149 O LEU A 35 5572 6977 6556 343 -2153 444 A O ATOM 150 CB LEU A 35 36.910 32.173 27.508 1.00 52.50 A C ANISOU 150 CB LEU A 35 5946 7228 6774 405 -2838 632 A C ATOM 151 CG LEU A 35 38.268 32.582 26.939 1.00 55.77 A C ANISOU 151 CG LEU A 35 5860 7978 7351 378 -2855 699 A C ATOM 152 CD1 LEU A 35 38.388 34.103 26.807 1.00 56.87 A C ANISOU 152 CD1 LEU A 35 5937 8215 7457 -18 -2856 699 A C ATOM 153 CD2 LEU A 35 39.397 32.062 27.804 1.00 56.66 A C ANISOU 153 CD2 LEU A 35 5725 8260 7544 503 -3148 820 A C ATOM 154 N PRO A 36 35.484 30.872 24.908 1.00 49.16 A N ANISOU 154 N PRO A 36 5682 6591 6407 811 -2202 429 A N ATOM 155 CA PRO A 36 35.528 30.482 23.477 1.00 48.63 A C ANISOU 155 CA PRO A 36 5483 6578 6414 988 -1934 362 A C ATOM 156 C PRO A 36 34.626 31.315 22.546 1.00 48.56 A C ANISOU 156 C PRO A 36 5613 6503 6336 791 -1710 274 A C ATOM 157 O PRO A 36 35.070 31.670 21.457 1.00 49.65 A O ANISOU 157 O PRO A 36 5529 6802 6532 789 -1535 256 A O ATOM 158 CB PRO A 36 35.064 29.028 23.492 1.00 49.31 A C ANISOU 158 CB PRO A 36 5786 6461 6490 1301 -1907 326 A C ATOM 159 CG PRO A 36 35.443 28.534 24.864 1.00 49.87 A C ANISOU 159 CG PRO A 36 5905 6492 6550 1368 -2190 420 A C ATOM 160 CD PRO A 36 35.215 29.704 25.771 1.00 48.34 A C ANISOU 160 CD PRO A 36 5797 6307 6264 1022 -2342 455 A C ATOM 161 N GLN A 37 33.383 31.641 22.953 1.00 46.98 A N ANISOU 161 N GLN A 37 5766 6078 6008 634 -1711 228 A N ATOM 162 CA GLN A 37 32.499 32.433 22.109 1.00 45.92 A C ANISOU 162 CA GLN A 37 5761 5878 5808 468 -1520 155 A C ATOM 163 C GLN A 37 32.958 33.897 22.036 1.00 46.27 A C ANISOU 163 C GLN A 37 5656 6074 5851 178 -1537 190 A C ATOM 164 O GLN A 37 32.716 34.544 21.027 1.00 46.31 A O ANISOU 164 O GLN A 37 5638 6113 5845 82 -1361 151 A O ATOM 165 CB GLN A 37 31.044 32.358 22.592 1.00 45.81 A C ANISOU 165 CB GLN A 37 6134 5600 5670 399 -1515 106 A C ATOM 166 CG GLN A 37 30.822 32.990 23.967 1.00 45.60 A C ANISOU 166 CG GLN A 37 6265 5505 5555 208 -1706 152 A C ATOM 167 CD GLN A 37 29.416 33.469 24.194 1.00 44.31 A C ANISOU 167 CD GLN A 37 6420 5146 5268 69 -1636 101 A C ATOM 168 NE2 GLN A 37 29.247 34.301 25.229 1.00 42.01 A N ANISOU 168 NE2 GLN A 37 6265 4811 4884 -122 -1762 127 A N ATOM 169 OE1 GLN A 37 28.483 33.117 23.450 1.00 43.42 A O ANISOU 169 OE1 GLN A 37 6432 4927 5140 133 -1474 39 A O ATOM 170 N THR A 38 33.610 34.425 23.090 1.00 46.29 A N ANISOU 170 N THR A 38 5579 6157 5854 27 -1758 266 A N ATOM 171 CA THR A 38 34.089 35.811 23.077 1.00 46.57 A C ANISOU 171 CA THR A 38 5494 6317 5882 -275 -1799 302 A C ATOM 172 C THR A 38 35.231 35.932 22.051 1.00 47.18 A C ANISOU 172 C THR A 38 5167 6669 6091 -249 -1688 343 A C ATOM 173 O THR A 38 35.279 36.911 21.314 1.00 47.18 A O ANISOU 173 O THR A 38 5108 6736 6081 -446 -1566 339 A O ATOM 174 CB THR A 38 34.488 36.278 24.500 1.00 46.54 A C ANISOU 174 CB THR A 38 5539 6316 5830 -452 -2085 368 A C ATOM 175 CG2 THR A 38 34.954 37.723 24.529 1.00 46.28 A C ANISOU 175 CG2 THR A 38 5428 6379 5777 -792 -2145 401 A C ATOM 176 OG1 THR A 38 33.365 36.134 25.374 1.00 46.82 A O ANISOU 176 OG1 THR A 38 5965 6097 5727 -458 -2141 326 A O ATOM 177 N ILE A 39 36.100 34.916 21.958 1.00 47.48 A N ANISOU 177 N ILE A 39 4938 6857 6245 11 -1709 381 A N ATOM 178 CA ILE A 39 37.173 34.888 20.971 1.00 48.11 A C ANISOU 178 CA ILE A 39 4616 7213 6451 87 -1571 419 A C ATOM 179 C ILE A 39 36.567 34.812 19.557 1.00 48.25 A C ANISOU 179 C ILE A 39 4718 7178 6435 170 -1262 331 A C ATOM 180 O ILE A 39 36.927 35.635 18.712 1.00 48.92 A O ANISOU 180 O ILE A 39 4642 7412 6534 8 -1119 348 A O ATOM 181 CB ILE A 39 38.120 33.700 21.259 1.00 49.09 A C ANISOU 181 CB ILE A 39 4474 7479 6699 408 -1661 473 A C ATOM 182 CG1 ILE A 39 38.867 33.899 22.586 1.00 50.05 A C ANISOU 182 CG1 ILE A 39 4461 7700 6854 297 -1987 579 A C ATOM 183 CG2 ILE A 39 39.090 33.477 20.113 1.00 49.81 A C ANISOU 183 CG2 ILE A 39 4169 7842 6913 565 -1455 494 A C ATOM 184 CD1 ILE A 39 39.614 32.665 23.062 1.00 51.31 A C ANISOU 184 CD1 ILE A 39 4434 7944 7117 639 -2120 637 A C ATOM 185 N LEU A 40 35.601 33.882 19.323 1.00 47.49 A N ANISOU 185 N LEU A 40 4903 6860 6280 389 -1173 242 A N ATOM 186 CA LEU A 40 34.909 33.736 18.029 1.00 47.48 A C ANISOU 186 CA LEU A 40 5033 6781 6225 466 -912 151 A C ATOM 187 C LEU A 40 34.223 35.045 17.584 1.00 46.04 A C ANISOU 187 C LEU A 40 5000 6543 5949 162 -829 132 A C ATOM 188 O LEU A 40 34.367 35.459 16.432 1.00 45.96 A O ANISOU 188 O LEU A 40 4901 6632 5930 121 -631 117 A O ATOM 189 CB LEU A 40 33.847 32.616 18.083 1.00 48.59 A C ANISOU 189 CB LEU A 40 5499 6659 6304 681 -891 66 A C ATOM 190 CG LEU A 40 34.348 31.186 18.111 1.00 51.78 A C ANISOU 190 CG LEU A 40 5831 7063 6779 1034 -900 57 A C ATOM 191 CD1 LEU A 40 33.204 30.213 18.397 1.00 52.76 A C ANISOU 191 CD1 LEU A 40 6330 6890 6828 1163 -927 -11 A C ATOM 192 CD2 LEU A 40 35.011 30.823 16.796 1.00 52.92 A C ANISOU 192 CD2 LEU A 40 5765 7370 6974 1229 -668 23 A C ATOM 193 N LEU A 41 33.466 35.678 18.488 1.00 44.69 A N ANISOU 193 N LEU A 41 5076 6206 5700 -36 -973 134 A N ATOM 194 CA LEU A 41 32.745 36.906 18.178 1.00 44.23 A C ANISOU 194 CA LEU A 41 5197 6061 5548 -295 -912 116 A C ATOM 195 C LEU A 41 33.697 38.110 18.033 1.00 44.50 A C ANISOU 195 C LEU A 41 5005 6287 5616 -559 -931 195 A C ATOM 196 O LEU A 41 33.424 39.011 17.239 1.00 44.21 A O ANISOU 196 O LEU A 41 5029 6244 5526 -722 -801 188 A O ATOM 197 CB LEU A 41 31.647 37.170 19.215 1.00 43.87 A C ANISOU 197 CB LEU A 41 5486 5778 5404 -390 -1043 90 A C ATOM 198 CG LEU A 41 30.502 36.138 19.189 1.00 44.38 A C ANISOU 198 CG LEU A 41 5797 5643 5423 -189 -990 16 A C ATOM 199 CD1 LEU A 41 29.630 36.255 20.406 1.00 44.77 A C ANISOU 199 CD1 LEU A 41 6117 5503 5390 -262 -1127 12 A C ATOM 200 CD2 LEU A 41 29.672 36.250 17.918 1.00 44.63 A C ANISOU 200 CD2 LEU A 41 5941 5610 5405 -166 -785 -50 A C ATOM 201 N GLY A 42 34.836 38.082 18.722 1.00 44.78 A N ANISOU 201 N GLY A 42 4772 6502 5742 -598 -1089 275 A N ATOM 202 CA GLY A 42 35.853 39.113 18.580 1.00 45.38 A C ANISOU 202 CA GLY A 42 4588 6788 5866 -860 -1117 362 A C ATOM 203 C GLY A 42 36.458 39.039 17.193 1.00 46.11 A C ANISOU 203 C GLY A 42 4417 7086 6017 -791 -868 376 A C ATOM 204 O GLY A 42 36.608 40.062 16.524 1.00 46.27 A O ANISOU 204 O GLY A 42 4405 7169 6007 -1027 -763 408 A O ATOM 205 N PHE A 43 36.735 37.810 16.722 1.00 46.51 A N ANISOU 205 N PHE A 43 4321 7217 6134 -457 -757 346 A N ATOM 206 CA PHE A 43 37.263 37.583 15.381 1.00 47.61 A C ANISOU 206 CA PHE A 43 4240 7542 6309 -336 -492 343 A C ATOM 207 C PHE A 43 36.204 37.949 14.321 1.00 47.18 A C ANISOU 207 C PHE A 43 4484 7321 6122 -378 -287 264 A C ATOM 208 O PHE A 43 36.556 38.554 13.316 1.00 47.92 A O ANISOU 208 O PHE A 43 4463 7549 6194 -491 -103 292 A O ATOM 209 CB PHE A 43 37.749 36.136 15.201 1.00 48.79 A C ANISOU 209 CB PHE A 43 4216 7779 6543 64 -430 317 A C ATOM 210 CG PHE A 43 39.154 35.884 15.713 1.00 51.01 A C ANISOU 210 CG PHE A 43 4054 8348 6980 128 -540 421 A C ATOM 211 CD1 PHE A 43 40.234 36.584 15.199 1.00 52.51 A C ANISOU 211 CD1 PHE A 43 3859 8846 7247 -36 -446 516 A C ATOM 212 CD2 PHE A 43 39.402 34.911 16.669 1.00 52.27 A C ANISOU 212 CD2 PHE A 43 4171 8480 7210 360 -732 434 A C ATOM 213 CE1 PHE A 43 41.528 36.355 15.674 1.00 53.56 A C ANISOU 213 CE1 PHE A 43 3544 9271 7536 20 -558 623 A C ATOM 214 CE2 PHE A 43 40.700 34.681 17.136 1.00 53.28 A C ANISOU 214 CE2 PHE A 43 3871 8887 7487 434 -852 541 A C ATOM 215 CZ PHE A 43 41.751 35.403 16.639 1.00 53.34 A C ANISOU 215 CZ PHE A 43 3470 9215 7580 264 -767 634 A C ATOM 216 N TYR A 44 34.918 37.632 14.560 1.00 45.71 A N ANISOU 216 N TYR A 44 4671 6854 5843 -306 -328 177 A N ATOM 217 CA TYR A 44 33.828 38.008 13.660 1.00 44.87 A C ANISOU 217 CA TYR A 44 4851 6584 5613 -354 -178 109 A C ATOM 218 C TYR A 44 33.743 39.546 13.518 1.00 45.79 A C ANISOU 218 C TYR A 44 5031 6698 5670 -700 -179 166 A C ATOM 219 O TYR A 44 33.701 40.045 12.394 1.00 45.63 A O ANISOU 219 O TYR A 44 5024 6725 5590 -771 3 169 A O ATOM 220 CB TYR A 44 32.488 37.440 14.166 1.00 43.68 A C ANISOU 220 CB TYR A 44 5049 6153 5394 -246 -262 26 A C ATOM 221 CG TYR A 44 31.251 38.151 13.639 1.00 42.89 A C ANISOU 221 CG TYR A 44 5252 5872 5172 -372 -194 -18 A C ATOM 222 CD1 TYR A 44 30.743 37.863 12.378 1.00 42.89 A C ANISOU 222 CD1 TYR A 44 5351 5842 5102 -268 -10 -78 A C ATOM 223 CD2 TYR A 44 30.580 39.094 14.411 1.00 42.44 A C ANISOU 223 CD2 TYR A 44 5392 5672 5063 -578 -321 0 A C ATOM 224 CE1 TYR A 44 29.607 38.501 11.897 1.00 42.81 A C ANISOU 224 CE1 TYR A 44 5604 5678 4985 -371 30 -108 A C ATOM 225 CE2 TYR A 44 29.452 39.750 13.932 1.00 42.47 A C ANISOU 225 CE2 TYR A 44 5655 5518 4965 -663 -261 -33 A C ATOM 226 CZ TYR A 44 28.967 39.447 12.674 1.00 42.90 A C ANISOU 226 CZ TYR A 44 5780 5558 4962 -560 -94 -82 A C ATOM 227 OH TYR A 44 27.827 40.048 12.202 1.00 43.15 A O ANISOU 227 OH TYR A 44 6056 5443 4896 -626 -56 -106 A O ATOM 228 N VAL A 45 33.711 40.294 14.647 1.00 46.43 A N ANISOU 228 N VAL A 45 5182 6707 5751 -914 -386 209 A N ATOM 229 CA VAL A 45 33.606 41.761 14.609 1.00 47.06 A C ANISOU 229 CA VAL A 45 5374 6742 5766 -1242 -408 257 A C ATOM 230 C VAL A 45 34.821 42.339 13.893 1.00 48.30 A C ANISOU 230 C VAL A 45 5217 7159 5977 -1409 -302 349 A C ATOM 231 O VAL A 45 34.671 43.204 13.031 1.00 48.68 A O ANISOU 231 O VAL A 45 5347 7195 5952 -1576 -170 373 A O ATOM 232 CB VAL A 45 33.424 42.379 16.024 1.00 47.16 A C ANISOU 232 CB VAL A 45 5537 6622 5758 -1426 -658 276 A C ATOM 233 CG1 VAL A 45 33.534 43.902 15.979 1.00 47.35 A C ANISOU 233 CG1 VAL A 45 5661 6607 5721 -1772 -687 332 A C ATOM 234 CG2 VAL A 45 32.090 41.961 16.631 1.00 47.44 A C ANISOU 234 CG2 VAL A 45 5909 6398 5719 -1286 -718 191 A C ATOM 235 N TYR A 46 36.017 41.812 14.200 1.00 48.75 A N ANISOU 235 N TYR A 46 4903 7459 6161 -1350 -350 407 A N ATOM 236 CA TYR A 46 37.253 42.254 13.572 1.00 49.74 A C ANISOU 236 CA TYR A 46 4664 7877 6358 -1497 -242 507 A C ATOM 237 C TYR A 46 37.200 42.008 12.057 1.00 49.71 A C ANISOU 237 C TYR A 46 4627 7956 6306 -1365 67 481 A C ATOM 238 O TYR A 46 37.551 42.893 11.275 1.00 50.11 A O ANISOU 238 O TYR A 46 4618 8106 6316 -1588 204 547 A O ATOM 239 CB TYR A 46 38.458 41.536 14.204 1.00 50.66 A C ANISOU 239 CB TYR A 46 4368 8249 6632 -1385 -353 569 A C ATOM 240 CG TYR A 46 39.755 41.822 13.485 1.00 52.76 A C ANISOU 240 CG TYR A 46 4195 8860 6990 -1491 -208 676 A C ATOM 241 CD1 TYR A 46 40.272 43.110 13.429 1.00 54.21 A C ANISOU 241 CD1 TYR A 46 4293 9137 7168 -1897 -238 778 A C ATOM 242 CD2 TYR A 46 40.433 40.818 12.807 1.00 54.06 A C ANISOU 242 CD2 TYR A 46 4048 9254 7239 -1185 -20 675 A C ATOM 243 CE1 TYR A 46 41.435 43.391 12.724 1.00 55.43 A C ANISOU 243 CE1 TYR A 46 4034 9623 7404 -2019 -84 887 A C ATOM 244 CE2 TYR A 46 41.603 41.083 12.108 1.00 55.28 A C ANISOU 244 CE2 TYR A 46 3782 9747 7475 -1272 147 777 A C ATOM 245 CZ TYR A 46 42.097 42.374 12.062 1.00 56.43 A C ANISOU 245 CZ TYR A 46 3824 10000 7619 -1700 118 888 A C ATOM 246 OH TYR A 46 43.251 42.650 11.369 1.00 58.01 A O ANISOU 246 OH TYR A 46 3591 10550 7900 -1812 295 1002 A O ATOM 247 N PHE A 47 36.742 40.823 11.650 1.00 48.96 A N ANISOU 247 N PHE A 47 4601 7804 6196 -1016 173 387 A N ATOM 248 CA PHE A 47 36.663 40.471 10.244 1.00 48.69 A C ANISOU 248 CA PHE A 47 4573 7833 6095 -862 455 346 A C ATOM 249 C PHE A 47 35.658 41.349 9.472 1.00 48.74 A C ANISOU 249 C PHE A 47 4926 7651 5942 -1030 546 321 A C ATOM 250 O PHE A 47 36.045 41.947 8.482 1.00 48.80 A O ANISOU 250 O PHE A 47 4864 7783 5895 -1158 733 374 A O ATOM 251 CB PHE A 47 36.323 38.968 10.052 1.00 48.10 A C ANISOU 251 CB PHE A 47 4554 7694 6027 -456 517 236 A C ATOM 252 CG PHE A 47 36.278 38.558 8.600 1.00 48.50 A C ANISOU 252 CG PHE A 47 4636 7804 5988 -289 805 182 A C ATOM 253 CD1 PHE A 47 37.445 38.378 7.877 1.00 49.22 A C ANISOU 253 CD1 PHE A 47 4382 8190 6129 -210 1012 233 A C ATOM 254 CD2 PHE A 47 35.066 38.402 7.943 1.00 49.30 A C ANISOU 254 CD2 PHE A 47 5110 7676 5945 -223 869 86 A C ATOM 255 CE1 PHE A 47 37.402 38.029 6.530 1.00 49.86 A C ANISOU 255 CE1 PHE A 47 4523 8322 6100 -57 1291 178 A C ATOM 256 CE2 PHE A 47 35.026 38.080 6.587 1.00 49.86 A C ANISOU 256 CE2 PHE A 47 5240 7796 5908 -91 1121 36 A C ATOM 257 CZ PHE A 47 36.192 37.896 5.890 1.00 49.62 A C ANISOU 257 CZ PHE A 47 4897 8045 5910 -6 1336 78 A C ATOM 258 N VAL A 48 34.387 41.426 9.898 1.00 48.60 A N ANISOU 258 N VAL A 48 5271 7347 5848 -1022 424 251 A N ATOM 259 CA VAL A 48 33.361 42.128 9.127 1.00 48.69 A C ANISOU 259 CA VAL A 48 5606 7181 5713 -1120 504 225 A C ATOM 260 C VAL A 48 33.501 43.657 9.119 1.00 49.78 A C ANISOU 260 C VAL A 48 5809 7299 5804 -1478 473 320 A C ATOM 261 O VAL A 48 32.973 44.292 8.205 1.00 50.42 A O ANISOU 261 O VAL A 48 6090 7301 5766 -1562 588 328 A O ATOM 262 CB VAL A 48 31.942 41.722 9.572 1.00 48.44 A C ANISOU 262 CB VAL A 48 5907 6871 5625 -990 389 129 A C ATOM 263 CG1 VAL A 48 31.775 40.206 9.514 1.00 48.52 A C ANISOU 263 CG1 VAL A 48 5892 6874 5669 -662 420 38 A C ATOM 264 CG2 VAL A 48 31.598 42.266 10.954 1.00 48.42 A C ANISOU 264 CG2 VAL A 48 6016 6726 5655 -1134 156 148 A C ATOM 265 N THR A 49 34.194 44.248 10.094 1.00 49.94 A N ANISOU 265 N THR A 49 5687 7380 5908 -1690 312 394 A N ATOM 266 CA THR A 49 34.322 45.701 10.150 1.00 50.92 A C ANISOU 266 CA THR A 49 5914 7452 5982 -2047 263 480 A C ATOM 267 C THR A 49 35.705 46.178 9.692 1.00 52.85 A C ANISOU 267 C THR A 49 5814 7980 6285 -2264 364 600 A C ATOM 268 O THR A 49 35.832 47.333 9.286 1.00 53.16 A O ANISOU 268 O THR A 49 5948 7993 6257 -2555 403 680 A O ATOM 269 CB THR A 49 34.027 46.227 11.578 1.00 51.29 A C ANISOU 269 CB THR A 49 6116 7326 6047 -2193 -5 477 A C ATOM 270 CG2 THR A 49 32.643 45.823 12.089 1.00 51.68 A C ANISOU 270 CG2 THR A 49 6492 7107 6036 -1996 -89 370 A C ATOM 271 OG1 THR A 49 35.031 45.773 12.483 1.00 51.57 A O ANISOU 271 OG1 THR A 49 5843 7539 6213 -2203 -143 513 A O ATOM 272 N SER A 50 36.741 45.316 9.767 1.00 53.77 A N ANISOU 272 N SER A 50 5531 8369 6529 -2127 406 623 A N ATOM 273 CA SER A 50 38.089 45.742 9.439 1.00 54.72 A C ANISOU 273 CA SER A 50 5270 8795 6727 -2336 495 748 A C ATOM 274 C SER A 50 38.826 44.824 8.417 1.00 55.51 A C ANISOU 274 C SER A 50 5043 9181 6869 -2090 767 752 A C ATOM 275 O SER A 50 39.091 45.286 7.306 1.00 55.94 A O ANISOU 275 O SER A 50 5065 9342 6846 -2198 998 807 A O ATOM 276 CB SER A 50 38.901 45.877 10.724 1.00 56.46 A C ANISOU 276 CB SER A 50 5247 9122 7084 -2492 240 812 A C ATOM 277 OG SER A 50 40.248 46.227 10.454 1.00 59.87 A O ANISOU 277 OG SER A 50 5254 9883 7613 -2699 310 943 A O ATOM 278 N LEU A 51 39.179 43.566 8.779 1.00 55.53 A N ANISOU 278 N LEU A 51 4820 9300 6981 -1762 749 700 A N ATOM 279 CA LEU A 51 39.974 42.667 7.927 1.00 56.13 A C ANISOU 279 CA LEU A 51 4571 9651 7105 -1498 1002 700 A C ATOM 280 C LEU A 51 39.314 42.322 6.576 1.00 56.84 A C ANISOU 280 C LEU A 51 4901 9659 7035 -1310 1276 617 A C ATOM 281 O LEU A 51 39.945 42.514 5.540 1.00 57.26 A O ANISOU 281 O LEU A 51 4783 9925 7047 -1348 1537 673 A O ATOM 282 CB LEU A 51 40.340 41.373 8.676 1.00 56.15 A C ANISOU 282 CB LEU A 51 4360 9728 7245 -1154 895 651 A C ATOM 283 CG LEU A 51 41.232 40.389 7.924 1.00 57.33 A C ANISOU 283 CG LEU A 51 4161 10162 7461 -837 1143 649 A C ATOM 284 CD1 LEU A 51 42.563 41.019 7.559 1.00 57.83 A C ANISOU 284 CD1 LEU A 51 3759 10600 7612 -1053 1277 800 A C ATOM 285 CD2 LEU A 51 41.467 39.139 8.743 1.00 57.90 A C ANISOU 285 CD2 LEU A 51 4093 10246 7658 -486 1003 599 A C ATOM 286 N GLY A 52 38.093 41.802 6.601 1.00 56.77 A N ANISOU 286 N GLY A 52 5272 9362 6936 -1118 1216 490 A N ATOM 287 CA GLY A 52 37.331 41.430 5.413 1.00 57.06 A C ANISOU 287 CA GLY A 52 5582 9287 6810 -945 1420 399 A C ATOM 288 C GLY A 52 37.238 42.511 4.358 1.00 57.39 A C ANISOU 288 C GLY A 52 5756 9344 6706 -1199 1591 466 A C ATOM 289 O GLY A 52 37.715 42.317 3.237 1.00 57.52 A O ANISOU 289 O GLY A 52 5672 9534 6648 -1120 1863 477 A O ATOM 290 N PRO A 53 36.678 43.691 4.697 1.00 57.48 A N ANISOU 290 N PRO A 53 5996 9177 6666 -1507 1445 519 A N ATOM 291 CA PRO A 53 36.589 44.780 3.707 1.00 57.94 A C ANISOU 291 CA PRO A 53 6209 9228 6579 -1760 1594 598 A C ATOM 292 C PRO A 53 37.954 45.236 3.169 1.00 59.30 A C ANISOU 292 C PRO A 53 6015 9730 6789 -1952 1794 733 A C ATOM 293 O PRO A 53 38.035 45.714 2.033 1.00 59.74 A O ANISOU 293 O PRO A 53 6151 9844 6704 -2054 2016 785 A O ATOM 294 CB PRO A 53 35.918 45.911 4.489 1.00 58.19 A C ANISOU 294 CB PRO A 53 6504 9012 6594 -2040 1355 637 A C ATOM 295 CG PRO A 53 35.198 45.235 5.596 1.00 58.63 A C ANISOU 295 CG PRO A 53 6666 8885 6724 -1851 1126 533 A C ATOM 296 CD PRO A 53 36.054 44.076 5.976 1.00 56.93 A C ANISOU 296 CD PRO A 53 6092 8886 6651 -1620 1145 506 A C ATOM 297 N LYS A 54 39.023 45.095 3.970 1.00 59.58 A N ANISOU 297 N LYS A 54 5643 9989 7007 -2009 1716 799 A N ATOM 298 CA LYS A 54 40.365 45.466 3.531 1.00 60.13 A C ANISOU 298 CA LYS A 54 5298 10409 7138 -2191 1901 937 A C ATOM 299 C LYS A 54 40.848 44.473 2.480 1.00 60.73 A C ANISOU 299 C LYS A 54 5181 10716 7180 -1869 2222 895 A C ATOM 300 O LYS A 54 41.411 44.876 1.461 1.00 61.22 A O ANISOU 300 O LYS A 54 5131 10972 7158 -1987 2493 979 A O ATOM 301 CB LYS A 54 41.334 45.517 4.722 1.00 61.88 A C ANISOU 301 CB LYS A 54 5121 10816 7574 -2322 1697 1018 A C ATOM 302 N LEU A 55 40.602 43.173 2.708 1.00 60.65 A N ANISOU 302 N LEU A 55 5161 10667 7217 -1459 2201 763 A N ATOM 303 CA LEU A 55 40.979 42.119 1.768 1.00 61.04 A C ANISOU 303 CA LEU A 55 5084 10887 7221 -1101 2493 695 A C ATOM 304 C LEU A 55 40.137 42.176 0.484 1.00 61.72 A C ANISOU 304 C LEU A 55 5576 10815 7057 -1043 2695 624 A C ATOM 305 O LEU A 55 40.623 41.808 -0.584 1.00 61.82 A O ANISOU 305 O LEU A 55 5497 11016 6976 -897 3006 618 A O ATOM 306 CB LEU A 55 40.837 40.744 2.426 1.00 60.97 A C ANISOU 306 CB LEU A 55 5032 10815 7319 -691 2378 569 A C ATOM 307 CG LEU A 55 41.757 40.491 3.616 1.00 62.33 A C ANISOU 307 CG LEU A 55 4780 11172 7729 -676 2193 638 A C ATOM 308 CD1 LEU A 55 41.438 39.164 4.277 1.00 62.97 A C ANISOU 308 CD1 LEU A 55 4915 11124 7887 -277 2055 514 A C ATOM 309 CD2 LEU A 55 43.215 40.537 3.204 1.00 62.58 A C ANISOU 309 CD2 LEU A 55 4278 11634 7864 -691 2420 760 A C ATOM 310 N MET A 56 38.885 42.637 0.582 1.00 61.98 A N ANISOU 310 N MET A 56 6056 10515 6978 -1151 2520 573 A N ATOM 311 CA MET A 56 38.011 42.732 -0.580 1.00 62.78 A C ANISOU 311 CA MET A 56 6556 10455 6842 -1109 2662 513 A C ATOM 312 C MET A 56 38.202 44.037 -1.379 1.00 64.52 A C ANISOU 312 C MET A 56 6856 10733 6926 -1465 2802 651 A C ATOM 313 O MET A 56 37.737 44.110 -2.515 1.00 64.78 A O ANISOU 313 O MET A 56 7163 10705 6747 -1429 2974 626 A O ATOM 314 CB MET A 56 36.539 42.601 -0.157 1.00 62.24 A C ANISOU 314 CB MET A 56 6913 10018 6717 -1043 2410 404 A C ATOM 315 CG MET A 56 36.166 41.217 0.331 1.00 62.24 A C ANISOU 315 CG MET A 56 6936 9924 6790 -679 2316 257 A C ATOM 316 SD MET A 56 36.481 39.876 -0.850 1.00 60.75 A S ANISOU 316 SD MET A 56 6740 9855 6487 -281 2619 137 A S ATOM 317 CE MET A 56 35.571 40.466 -2.282 1.00 59.06 A C ANISOU 317 CE MET A 56 6965 9499 5975 -390 2757 120 A C ATOM 318 N GLU A 57 38.870 45.056 -0.797 1.00 65.34 A N ANISOU 318 N GLU A 57 6748 10941 7140 -1817 2720 799 A N ATOM 319 CA GLU A 57 39.080 46.365 -1.416 1.00 66.55 A C ANISOU 319 CA GLU A 57 6987 11121 7177 -2199 2821 947 A C ATOM 320 C GLU A 57 39.674 46.278 -2.826 1.00 67.94 A C ANISOU 320 C GLU A 57 7088 11531 7194 -2165 3204 994 A C ATOM 321 O GLU A 57 39.181 46.960 -3.724 1.00 68.43 A O ANISOU 321 O GLU A 57 7476 11477 7048 -2310 3303 1036 A O ATOM 322 CB GLU A 57 39.974 47.249 -0.533 1.00 68.45 A C ANISOU 322 CB GLU A 57 6922 11497 7588 -2563 2692 1096 A C ATOM 323 N ASN A 58 40.714 45.453 -3.035 1.00 68.35 A N ANISOU 323 N ASN A 58 6727 11908 7333 -1962 3425 991 A N ATOM 324 CA ASN A 58 41.321 45.329 -4.363 1.00 69.03 A C ANISOU 324 CA ASN A 58 6731 12237 7259 -1907 3822 1032 A C ATOM 325 C ASN A 58 40.948 43.994 -5.024 1.00 68.65 A C ANISOU 325 C ASN A 58 6826 12159 7099 -1434 3980 851 A C ATOM 326 O ASN A 58 41.763 43.405 -5.734 1.00 69.02 A O ANISOU 326 O ASN A 58 6635 12482 7108 -1241 4299 847 A O ATOM 327 CB ASN A 58 42.840 45.505 -4.301 1.00 71.16 A C ANISOU 327 CB ASN A 58 6425 12931 7681 -2048 4018 1181 A C ATOM 328 CG ASN A 58 43.266 46.943 -4.489 1.00 76.24 A C ANISOU 328 CG ASN A 58 7034 13646 8287 -2563 4053 1383 A C ATOM 329 ND2 ASN A 58 44.431 47.150 -5.102 1.00 76.93 A N ANISOU 329 ND2 ASN A 58 6740 14110 8380 -2693 4367 1520 A N ATOM 330 OD1 ASN A 58 42.559 47.884 -4.097 1.00 78.19 A O ANISOU 330 OD1 ASN A 58 7601 13610 8496 -2848 3807 1422 A O ATOM 331 N ARG A 59 39.706 43.538 -4.806 1.00 67.66 A N ANISOU 331 N ARG A 59 7099 11696 6911 -1255 3761 704 A N ATOM 332 CA ARG A 59 39.176 42.303 -5.379 1.00 67.10 A C ANISOU 332 CA ARG A 59 7245 11529 6721 -844 3852 523 A C ATOM 333 C ARG A 59 37.765 42.514 -5.945 1.00 65.78 A C ANISOU 333 C ARG A 59 7638 11025 6328 -863 3736 445 A C ATOM 334 O ARG A 59 37.040 43.407 -5.504 1.00 65.59 A O ANISOU 334 O ARG A 59 7819 10792 6309 -1114 3499 500 A O ATOM 335 CB ARG A 59 39.117 41.191 -4.311 1.00 69.11 A C ANISOU 335 CB ARG A 59 7354 11722 7182 -544 3653 404 A C ATOM 336 CG ARG A 59 40.450 40.622 -3.870 1.00 73.46 A C ANISOU 336 CG ARG A 59 7369 12603 7940 -391 3776 445 A C ATOM 337 CD ARG A 59 40.246 39.470 -2.906 1.00 78.10 A C ANISOU 337 CD ARG A 59 7906 13077 8692 -67 3569 320 A C ATOM 338 NE ARG A 59 41.405 39.284 -2.030 1.00 82.83 A N ANISOU 338 NE ARG A 59 7979 13947 9548 -33 3535 405 A N ATOM 339 CZ ARG A 59 42.335 38.350 -2.202 1.00 86.63 A C ANISOU 339 CZ ARG A 59 8131 14674 10109 296 3737 378 A C ATOM 340 NH1 ARG A 59 42.243 37.486 -3.207 1.00 86.91 A N1+ ANISOU 340 NH1 ARG A 59 8340 14703 9981 629 3999 255 A N1+ ATOM 341 NH2 ARG A 59 43.359 38.262 -1.361 1.00 86.96 A N ANISOU 341 NH2 ARG A 59 7678 14968 10393 307 3671 473 A N ATOM 342 N LYS A 60 37.355 41.661 -6.891 1.00 64.61 A N ANISOU 342 N LYS A 60 7744 10821 5985 -583 3888 312 A N ATOM 343 CA LYS A 60 35.991 41.700 -7.421 1.00 63.41 A C ANISOU 343 CA LYS A 60 8105 10362 5627 -569 3752 227 A C ATOM 344 C LYS A 60 35.061 40.944 -6.456 1.00 61.92 A C ANISOU 344 C LYS A 60 8039 9919 5570 -391 3435 94 A C ATOM 345 O LYS A 60 35.514 40.037 -5.756 1.00 61.79 A O ANISOU 345 O LYS A 60 7780 9968 5728 -171 3407 26 A O ATOM 346 CB LYS A 60 35.927 41.113 -8.845 1.00 64.69 A C ANISOU 346 CB LYS A 60 8514 10561 5503 -370 4029 140 A C ATOM 347 CG LYS A 60 36.605 39.768 -9.008 1.00 68.17 A C ANISOU 347 CG LYS A 60 8778 11151 5974 11 4231 11 A C ATOM 348 CD LYS A 60 36.228 39.134 -10.347 1.00 72.21 A C ANISOU 348 CD LYS A 60 9662 11604 6171 218 4435 -113 A C ATOM 349 CE LYS A 60 37.016 37.874 -10.617 1.00 76.08 A C ANISOU 349 CE LYS A 60 9991 12250 6664 605 4688 -236 A C ATOM 350 NZ LYS A 60 36.338 36.990 -11.597 1.00 78.41 A N1+ ANISOU 350 NZ LYS A 60 10738 12373 6683 853 4758 -415 A N1+ ATOM 351 N PRO A 61 33.766 41.313 -6.379 1.00 60.57 A N ANISOU 351 N PRO A 61 8231 9462 5321 -483 3191 67 A N ATOM 352 CA PRO A 61 32.865 40.611 -5.448 1.00 59.83 A C ANISOU 352 CA PRO A 61 8240 9141 5353 -335 2904 -47 A C ATOM 353 C PRO A 61 32.684 39.136 -5.787 1.00 59.51 A C ANISOU 353 C PRO A 61 8302 9053 5257 18 2963 -222 A C ATOM 354 O PRO A 61 32.733 38.750 -6.961 1.00 59.95 A O ANISOU 354 O PRO A 61 8535 9149 5096 139 3171 -282 A O ATOM 355 CB PRO A 61 31.531 41.348 -5.592 1.00 60.38 A C ANISOU 355 CB PRO A 61 8681 8953 5307 -497 2693 -31 A C ATOM 356 CG PRO A 61 31.811 42.565 -6.380 1.00 60.94 A C ANISOU 356 CG PRO A 61 8822 9102 5231 -755 2830 110 A C ATOM 357 CD PRO A 61 33.069 42.369 -7.136 1.00 59.52 A C ANISOU 357 CD PRO A 61 8423 9207 4985 -714 3170 146 A C ATOM 358 N PHE A 62 32.478 38.307 -4.758 1.00 58.47 A N ANISOU 358 N PHE A 62 8087 8823 5307 179 2779 -302 A N ATOM 359 CA PHE A 62 32.259 36.884 -4.959 1.00 58.13 A C ANISOU 359 CA PHE A 62 8172 8691 5224 504 2801 -467 A C ATOM 360 C PHE A 62 30.838 36.634 -5.439 1.00 57.92 A C ANISOU 360 C PHE A 62 8584 8396 5029 512 2642 -564 A C ATOM 361 O PHE A 62 29.907 37.335 -5.042 1.00 58.01 A O ANISOU 361 O PHE A 62 8726 8255 5059 319 2420 -515 A O ATOM 362 CB PHE A 62 32.520 36.093 -3.663 1.00 58.17 A C ANISOU 362 CB PHE A 62 7955 8670 5477 661 2647 -505 A C ATOM 363 CG PHE A 62 33.968 35.938 -3.267 1.00 59.11 A C ANISOU 363 CG PHE A 62 7634 9064 5759 754 2805 -442 A C ATOM 364 CD1 PHE A 62 34.632 36.950 -2.598 1.00 60.01 A C ANISOU 364 CD1 PHE A 62 7434 9343 6025 509 2767 -289 A C ATOM 365 CD2 PHE A 62 34.653 34.764 -3.522 1.00 60.13 A C ANISOU 365 CD2 PHE A 62 7665 9282 5898 1093 2976 -536 A C ATOM 366 CE1 PHE A 62 35.960 36.803 -2.224 1.00 60.67 A C ANISOU 366 CE1 PHE A 62 7082 9702 6269 582 2891 -221 A C ATOM 367 CE2 PHE A 62 35.982 34.621 -3.146 1.00 60.88 A C ANISOU 367 CE2 PHE A 62 7322 9653 6158 1198 3115 -468 A C ATOM 368 CZ PHE A 62 36.625 35.639 -2.496 1.00 60.57 A C ANISOU 368 CZ PHE A 62 6943 9798 6273 935 3065 -307 A C ATOM 369 N GLU A 63 30.671 35.654 -6.315 1.00 57.79 A N ANISOU 369 N GLU A 63 8795 8323 4839 734 2755 -700 A N ATOM 370 CA GLU A 63 29.357 35.263 -6.803 1.00 58.13 A C ANISOU 370 CA GLU A 63 9247 8120 4720 748 2591 -801 A C ATOM 371 C GLU A 63 28.894 34.142 -5.914 1.00 57.01 A C ANISOU 371 C GLU A 63 9135 7804 4724 917 2397 -910 A C ATOM 372 O GLU A 63 29.385 33.019 -6.035 1.00 57.96 A O ANISOU 372 O GLU A 63 9257 7926 4839 1178 2508 -1020 A O ATOM 373 CB GLU A 63 29.414 34.823 -8.273 1.00 62.04 A C ANISOU 373 CB GLU A 63 10020 8634 4920 872 2806 -893 A C ATOM 374 CG GLU A 63 28.056 34.418 -8.821 1.00 69.84 A C ANISOU 374 CG GLU A 63 11433 9374 5728 865 2611 -996 A C ATOM 375 CD GLU A 63 27.096 35.584 -8.946 1.00 80.38 A C ANISOU 375 CD GLU A 63 12903 10633 7004 591 2426 -887 A C ATOM 376 OE1 GLU A 63 27.385 36.505 -9.744 1.00 83.10 A O ANISOU 376 OE1 GLU A 63 13289 11092 7193 456 2572 -792 A O ATOM 377 OE2 GLU A 63 26.057 35.579 -8.246 1.00 83.38 A O1- ANISOU 377 OE2 GLU A 63 13349 10840 7491 517 2142 -891 A O1- ATOM 378 N LEU A 64 28.018 34.449 -4.969 1.00 55.00 A N ANISOU 378 N LEU A 64 8890 7402 4604 778 2121 -872 A N ATOM 379 CA LEU A 64 27.560 33.472 -3.997 1.00 53.69 A C ANISOU 379 CA LEU A 64 8739 7073 4588 899 1929 -950 A C ATOM 380 C LEU A 64 26.046 33.290 -4.035 1.00 52.43 A C ANISOU 380 C LEU A 64 8887 6677 4358 815 1687 -1002 A C ATOM 381 O LEU A 64 25.454 32.993 -3.003 1.00 52.49 A O ANISOU 381 O LEU A 64 8868 6557 4517 794 1482 -1005 A O ATOM 382 CB LEU A 64 27.992 33.956 -2.595 1.00 53.75 A C ANISOU 382 CB LEU A 64 8422 7148 4852 812 1822 -844 A C ATOM 383 CG LEU A 64 29.495 34.130 -2.407 1.00 54.91 A C ANISOU 383 CG LEU A 64 8211 7547 5104 875 2021 -777 A C ATOM 384 CD1 LEU A 64 29.807 34.778 -1.098 1.00 55.46 A C ANISOU 384 CD1 LEU A 64 8006 7674 5395 731 1879 -664 A C ATOM 385 CD2 LEU A 64 30.220 32.795 -2.546 1.00 55.43 A C ANISOU 385 CD2 LEU A 64 8230 7646 5185 1199 2157 -885 A C ATOM 386 N LYS A 65 25.420 33.470 -5.200 1.00 51.27 A N ANISOU 386 N LYS A 65 9019 6480 3981 759 1706 -1036 A N ATOM 387 CA LYS A 65 23.970 33.361 -5.347 1.00 51.06 A C ANISOU 387 CA LYS A 65 9262 6259 3881 664 1469 -1073 A C ATOM 388 C LYS A 65 23.440 31.998 -4.876 1.00 50.29 A C ANISOU 388 C LYS A 65 9291 5977 3842 797 1327 -1197 A C ATOM 389 O LYS A 65 22.527 31.964 -4.063 1.00 50.39 A O ANISOU 389 O LYS A 65 9305 5868 3974 704 1104 -1175 A O ATOM 390 CB LYS A 65 23.540 33.639 -6.802 1.00 53.73 A C ANISOU 390 CB LYS A 65 9892 6590 3935 613 1523 -1097 A C ATOM 391 CG LYS A 65 22.049 33.452 -7.049 1.00 58.79 A C ANISOU 391 CG LYS A 65 10801 7048 4490 520 1263 -1136 A C ATOM 392 CD LYS A 65 21.623 33.945 -8.413 1.00 64.13 A C ANISOU 392 CD LYS A 65 11744 7734 4889 441 1285 -1129 A C ATOM 393 CE LYS A 65 20.432 33.170 -8.910 1.00 69.44 A C ANISOU 393 CE LYS A 65 12723 8231 5430 432 1072 -1231 A C ATOM 394 NZ LYS A 65 19.891 33.717 -10.189 1.00 72.54 A N1+ ANISOU 394 NZ LYS A 65 13384 8629 5550 337 1040 -1209 A N1+ ATOM 395 N LYS A 66 24.005 30.892 -5.359 1.00 49.81 A N ANISOU 395 N LYS A 66 9341 5888 3695 1012 1462 -1322 A N ATOM 396 CA LYS A 66 23.555 29.553 -4.976 1.00 49.64 A C ANISOU 396 CA LYS A 66 9485 5666 3712 1138 1334 -1442 A C ATOM 397 C LYS A 66 23.825 29.271 -3.503 1.00 48.36 A C ANISOU 397 C LYS A 66 9075 5483 3816 1181 1244 -1396 A C ATOM 398 O LYS A 66 23.014 28.631 -2.844 1.00 48.72 A O ANISOU 398 O LYS A 66 9221 5351 3940 1152 1045 -1428 A O ATOM 399 CB LYS A 66 24.245 28.498 -5.852 1.00 52.59 A C ANISOU 399 CB LYS A 66 10048 6012 3922 1388 1529 -1587 A C ATOM 400 CG LYS A 66 23.738 27.082 -5.632 1.00 57.89 A C ANISOU 400 CG LYS A 66 10972 6434 4589 1510 1396 -1723 A C ATOM 401 N ALA A 67 24.950 29.768 -2.978 1.00 47.09 A N ANISOU 401 N ALA A 67 8592 5509 3790 1231 1382 -1313 A N ATOM 402 CA ALA A 67 25.322 29.587 -1.578 1.00 45.91 A C ANISOU 402 CA ALA A 67 8198 5364 3882 1269 1294 -1257 A C ATOM 403 C ALA A 67 24.336 30.323 -0.667 1.00 45.20 A C ANISOU 403 C ALA A 67 8062 5209 3904 1035 1068 -1164 A C ATOM 404 O ALA A 67 23.979 29.803 0.386 1.00 45.47 A O ANISOU 404 O ALA A 67 8075 5128 4075 1045 914 -1163 A O ATOM 405 CB ALA A 67 26.742 30.086 -1.348 1.00 45.69 A C ANISOU 405 CB ALA A 67 7827 5580 3954 1341 1483 -1178 A C ATOM 406 N MET A 68 23.889 31.526 -1.087 1.00 43.76 A N ANISOU 406 N MET A 68 7881 5093 3653 835 1055 -1085 A N ATOM 407 CA MET A 68 22.927 32.364 -0.367 1.00 42.19 A C ANISOU 407 CA MET A 68 7654 4840 3536 630 866 -997 A C ATOM 408 C MET A 68 21.553 31.721 -0.384 1.00 41.21 A C ANISOU 408 C MET A 68 7766 4521 3370 588 675 -1058 A C ATOM 409 O MET A 68 20.905 31.693 0.645 1.00 41.56 A O ANISOU 409 O MET A 68 7763 4484 3545 518 519 -1021 A O ATOM 410 CB MET A 68 22.836 33.769 -0.997 1.00 41.86 A C ANISOU 410 CB MET A 68 7597 4903 3404 460 916 -902 A C ATOM 411 CG MET A 68 23.952 34.704 -0.602 1.00 42.95 A C ANISOU 411 CG MET A 68 7468 5218 3633 401 1037 -799 A C ATOM 412 SD MET A 68 23.551 36.434 -0.984 1.00 44.78 A S ANISOU 412 SD MET A 68 7725 5497 3792 158 1021 -668 A S ATOM 413 CE MET A 68 23.472 36.400 -2.729 1.00 39.70 A C ANISOU 413 CE MET A 68 7317 4885 2882 184 1161 -713 A C ATOM 414 N ILE A 69 21.093 31.231 -1.546 1.00 40.00 A N ANISOU 414 N ILE A 69 7868 4300 3030 616 686 -1146 A N ATOM 415 CA ILE A 69 19.784 30.593 -1.681 1.00 39.97 A C ANISOU 415 CA ILE A 69 8090 4122 2975 550 492 -1204 A C ATOM 416 C ILE A 69 19.717 29.328 -0.808 1.00 40.26 A C ANISOU 416 C ILE A 69 8158 4012 3127 645 409 -1268 A C ATOM 417 O ILE A 69 18.742 29.153 -0.084 1.00 40.55 A O ANISOU 417 O ILE A 69 8208 3946 3253 538 230 -1241 A O ATOM 418 CB ILE A 69 19.493 30.268 -3.172 1.00 40.13 A C ANISOU 418 CB ILE A 69 8397 4104 2746 567 526 -1295 A C ATOM 419 CG1 ILE A 69 19.280 31.548 -3.998 1.00 41.04 A C ANISOU 419 CG1 ILE A 69 8522 4335 2735 440 556 -1212 A C ATOM 420 CG2 ILE A 69 18.326 29.286 -3.351 1.00 39.86 A C ANISOU 420 CG2 ILE A 69 8614 3877 2652 517 326 -1381 A C ATOM 421 CD1 ILE A 69 19.402 31.250 -5.553 1.00 42.41 A C ANISOU 421 CD1 ILE A 69 8976 4508 2629 493 656 -1303 A C ATOM 422 N THR A 70 20.752 28.468 -0.860 1.00 39.75 A N ANISOU 422 N THR A 70 8101 3940 3061 852 545 -1345 A N ATOM 423 CA THR A 70 20.807 27.250 -0.048 1.00 39.78 A C ANISOU 423 CA THR A 70 8157 3791 3168 968 475 -1400 A C ATOM 424 C THR A 70 20.812 27.611 1.438 1.00 39.18 A C ANISOU 424 C THR A 70 7840 3741 3307 904 383 -1292 A C ATOM 425 O THR A 70 20.048 27.049 2.214 1.00 40.04 A O ANISOU 425 O THR A 70 8016 3706 3492 843 226 -1287 A O ATOM 426 CB THR A 70 22.039 26.430 -0.421 1.00 41.49 A C ANISOU 426 CB THR A 70 8399 4020 3344 1237 660 -1489 A C ATOM 427 CG2 THR A 70 22.219 25.209 0.458 1.00 41.51 A C ANISOU 427 CG2 THR A 70 8455 3858 3457 1385 591 -1533 A C ATOM 428 OG1 THR A 70 21.937 26.049 -1.791 1.00 43.41 A O ANISOU 428 OG1 THR A 70 8916 4217 3363 1293 743 -1601 A O ATOM 429 N TYR A 71 21.637 28.585 1.815 1.00 37.73 A N ANISOU 429 N TYR A 71 7388 3741 3205 898 479 -1201 A N ATOM 430 CA TYR A 71 21.761 29.075 3.184 1.00 36.55 A C ANISOU 430 CA TYR A 71 7018 3635 3235 832 400 -1098 A C ATOM 431 C TYR A 71 20.433 29.618 3.706 1.00 35.69 A C ANISOU 431 C TYR A 71 6947 3455 3159 625 232 -1038 A C ATOM 432 O TYR A 71 20.065 29.299 4.826 1.00 35.72 A O ANISOU 432 O TYR A 71 6919 3377 3274 595 119 -1005 A O ATOM 433 CB TYR A 71 22.864 30.153 3.262 1.00 36.18 A C ANISOU 433 CB TYR A 71 6704 3805 3237 823 531 -1014 A C ATOM 434 CG TYR A 71 22.873 30.913 4.563 1.00 37.00 A C ANISOU 434 CG TYR A 71 6616 3952 3491 705 434 -906 A C ATOM 435 CD1 TYR A 71 23.407 30.352 5.716 1.00 38.09 A C ANISOU 435 CD1 TYR A 71 6639 4070 3763 795 377 -886 A C ATOM 436 CD2 TYR A 71 22.245 32.145 4.670 1.00 37.18 A C ANISOU 436 CD2 TYR A 71 6610 4010 3507 509 381 -828 A C ATOM 437 CE1 TYR A 71 23.371 31.034 6.928 1.00 38.89 A C ANISOU 437 CE1 TYR A 71 6602 4199 3977 679 276 -794 A C ATOM 438 CE2 TYR A 71 22.154 32.803 5.879 1.00 38.16 A C ANISOU 438 CE2 TYR A 71 6610 4143 3746 405 288 -744 A C ATOM 439 CZ TYR A 71 22.746 32.266 7.003 1.00 39.47 A C ANISOU 439 CZ TYR A 71 6663 4302 4033 483 238 -728 A C ATOM 440 OH TYR A 71 22.642 32.963 8.188 1.00 40.56 A O ANISOU 440 OH TYR A 71 6707 4444 4258 370 143 -649 A O ATOM 441 N ASN A 72 19.743 30.470 2.938 1.00 35.40 A N ANISOU 441 N ASN A 72 6967 3458 3025 492 220 -1014 A N ATOM 442 CA ASN A 72 18.478 31.069 3.367 1.00 35.52 A C ANISOU 442 CA ASN A 72 6994 3430 3073 321 73 -951 A C ATOM 443 C ASN A 72 17.391 30.002 3.519 1.00 36.89 A C ANISOU 443 C ASN A 72 7335 3437 3244 287 -71 -1003 A C ATOM 444 O ASN A 72 16.604 30.057 4.455 1.00 36.99 A O ANISOU 444 O ASN A 72 7301 3401 3353 195 -182 -949 A O ATOM 445 CB ASN A 72 18.031 32.151 2.391 1.00 34.57 A C ANISOU 445 CB ASN A 72 6912 3384 2838 219 89 -913 A C ATOM 446 CG ASN A 72 18.891 33.395 2.416 1.00 35.22 A C ANISOU 446 CG ASN A 72 6833 3613 2937 189 203 -832 A C ATOM 447 ND2 ASN A 72 19.204 33.940 1.257 1.00 35.59 A N ANISOU 447 ND2 ASN A 72 6938 3739 2845 178 305 -831 A N ATOM 448 OD1 ASN A 72 19.281 33.889 3.457 1.00 35.05 A O ANISOU 448 OD1 ASN A 72 6648 3629 3039 162 198 -767 A O ATOM 449 N PHE A 73 17.367 29.033 2.619 1.00 37.71 A N ANISOU 449 N PHE A 73 7641 3453 3233 355 -63 -1107 A N ATOM 450 CA PHE A 73 16.416 27.933 2.648 1.00 39.83 A C ANISOU 450 CA PHE A 73 8102 3550 3484 304 -204 -1165 A C ATOM 451 C PHE A 73 16.662 27.060 3.886 1.00 38.44 A C ANISOU 451 C PHE A 73 7897 3268 3442 365 -241 -1159 A C ATOM 452 O PHE A 73 15.715 26.696 4.577 1.00 38.62 A O ANISOU 452 O PHE A 73 7949 3197 3529 247 -371 -1126 A O ATOM 453 CB PHE A 73 16.553 27.117 1.355 1.00 42.19 A C ANISOU 453 CB PHE A 73 8657 3767 3605 380 -171 -1291 A C ATOM 454 CG PHE A 73 15.806 25.812 1.292 1.00 46.08 A C ANISOU 454 CG PHE A 73 9395 4052 4060 339 -307 -1372 A C ATOM 455 CD1 PHE A 73 14.487 25.770 0.861 1.00 48.45 A C ANISOU 455 CD1 PHE A 73 9811 4298 4299 147 -476 -1369 A C ATOM 456 CD2 PHE A 73 16.458 24.610 1.527 1.00 48.33 A C ANISOU 456 CD2 PHE A 73 9818 4193 4354 496 -267 -1455 A C ATOM 457 CE1 PHE A 73 13.823 24.554 0.711 1.00 49.96 A C ANISOU 457 CE1 PHE A 73 10246 4294 4441 79 -609 -1445 A C ATOM 458 CE2 PHE A 73 15.784 23.396 1.410 1.00 50.02 A C ANISOU 458 CE2 PHE A 73 10302 4187 4517 444 -397 -1533 A C ATOM 459 CZ PHE A 73 14.475 23.374 0.986 1.00 50.06 A C ANISOU 459 CZ PHE A 73 10421 4142 4460 220 -568 -1529 A C ATOM 460 N PHE A 74 17.930 26.782 4.199 1.00 36.96 A N ANISOU 460 N PHE A 74 7634 3110 3299 545 -125 -1177 A N ATOM 461 CA PHE A 74 18.284 26.025 5.384 1.00 36.46 A C ANISOU 461 CA PHE A 74 7540 2956 3357 624 -164 -1158 A C ATOM 462 C PHE A 74 17.858 26.788 6.647 1.00 34.47 A C ANISOU 462 C PHE A 74 7105 2761 3232 493 -237 -1039 A C ATOM 463 O PHE A 74 17.339 26.159 7.561 1.00 33.90 A O ANISOU 463 O PHE A 74 7085 2569 3225 446 -336 -1013 A O ATOM 464 CB PHE A 74 19.796 25.714 5.415 1.00 37.81 A C ANISOU 464 CB PHE A 74 7624 3187 3555 861 -28 -1187 A C ATOM 465 CG PHE A 74 20.295 25.184 6.745 1.00 39.99 A C ANISOU 465 CG PHE A 74 7818 3409 3967 950 -78 -1138 A C ATOM 466 CD1 PHE A 74 20.166 23.847 7.068 1.00 41.00 A C ANISOU 466 CD1 PHE A 74 8149 3329 4100 1041 -148 -1188 A C ATOM 467 CD2 PHE A 74 20.835 26.040 7.694 1.00 41.33 A C ANISOU 467 CD2 PHE A 74 7734 3722 4248 925 -73 -1037 A C ATOM 468 CE1 PHE A 74 20.578 23.376 8.306 1.00 41.88 A C ANISOU 468 CE1 PHE A 74 8205 3383 4324 1118 -208 -1130 A C ATOM 469 CE2 PHE A 74 21.229 25.562 8.939 1.00 41.89 A C ANISOU 469 CE2 PHE A 74 7749 3741 4426 994 -143 -985 A C ATOM 470 CZ PHE A 74 21.110 24.234 9.228 1.00 41.54 A C ANISOU 470 CZ PHE A 74 7903 3497 4384 1097 -208 -1029 A C ATOM 471 N ILE A 75 18.096 28.131 6.725 1.00 33.43 A N ANISOU 471 N ILE A 75 6779 2799 3125 434 -183 -967 A N ATOM 472 CA ILE A 75 17.725 28.875 7.919 1.00 32.83 A C ANISOU 472 CA ILE A 75 6563 2762 3149 327 -242 -866 A C ATOM 473 C ILE A 75 16.206 28.901 8.083 1.00 31.41 A C ANISOU 473 C ILE A 75 6459 2511 2966 164 -354 -838 A C ATOM 474 O ILE A 75 15.731 28.823 9.205 1.00 31.49 A O ANISOU 474 O ILE A 75 6434 2478 3053 103 -417 -781 A O ATOM 475 CB ILE A 75 18.317 30.306 7.982 1.00 34.80 A C ANISOU 475 CB ILE A 75 6625 3179 3417 292 -169 -799 A C ATOM 476 CG1 ILE A 75 19.859 30.280 7.928 1.00 36.01 A C ANISOU 476 CG1 ILE A 75 6654 3434 3596 432 -62 -809 A C ATOM 477 CG2 ILE A 75 17.856 30.987 9.275 1.00 35.71 A C ANISOU 477 CG2 ILE A 75 6650 3301 3619 188 -238 -711 A C ATOM 478 CD1 ILE A 75 20.535 29.571 9.158 1.00 37.07 A C ANISOU 478 CD1 ILE A 75 6722 3527 3837 531 -108 -787 A C ATOM 479 N VAL A 76 15.439 28.971 6.992 1.00 30.62 A N ANISOU 479 N VAL A 76 6457 2405 2773 95 -382 -874 A N ATOM 480 CA VAL A 76 13.970 28.976 7.072 1.00 30.88 A C ANISOU 480 CA VAL A 76 6527 2396 2810 -60 -498 -840 A C ATOM 481 C VAL A 76 13.478 27.661 7.684 1.00 31.25 A C ANISOU 481 C VAL A 76 6692 2286 2897 -97 -585 -860 A C ATOM 482 O VAL A 76 12.673 27.698 8.612 1.00 30.97 A O ANISOU 482 O VAL A 76 6598 2235 2935 -201 -643 -789 A O ATOM 483 CB VAL A 76 13.321 29.244 5.681 1.00 31.71 A C ANISOU 483 CB VAL A 76 6722 2530 2795 -121 -534 -875 A C ATOM 484 CG1 VAL A 76 11.849 28.830 5.635 1.00 32.13 A C ANISOU 484 CG1 VAL A 76 6829 2525 2851 -276 -680 -857 A C ATOM 485 CG2 VAL A 76 13.457 30.710 5.313 1.00 31.65 A C ANISOU 485 CG2 VAL A 76 6596 2667 2764 -129 -474 -817 A C ATOM 486 N LEU A 77 13.997 26.511 7.198 1.00 31.32 A N ANISOU 486 N LEU A 77 6878 2173 2851 -7 -582 -952 A N ATOM 487 CA LEU A 77 13.599 25.199 7.688 1.00 32.41 A C ANISOU 487 CA LEU A 77 7177 2127 3010 -43 -668 -974 A C ATOM 488 C LEU A 77 14.075 24.967 9.117 1.00 32.55 A C ANISOU 488 C LEU A 77 7123 2111 3136 11 -656 -910 A C ATOM 489 O LEU A 77 13.329 24.437 9.934 1.00 32.72 A O ANISOU 489 O LEU A 77 7189 2040 3205 -101 -732 -860 A O ATOM 490 CB LEU A 77 14.125 24.105 6.753 1.00 33.73 A C ANISOU 490 CB LEU A 77 7585 2155 3076 70 -658 -1098 A C ATOM 491 CG LEU A 77 13.431 24.033 5.381 1.00 37.07 A C ANISOU 491 CG LEU A 77 8160 2561 3364 -22 -714 -1170 A C ATOM 492 CD1 LEU A 77 13.943 22.850 4.575 1.00 37.98 A C ANISOU 492 CD1 LEU A 77 8563 2505 3365 97 -702 -1304 A C ATOM 493 CD2 LEU A 77 11.898 23.874 5.525 1.00 38.48 A C ANISOU 493 CD2 LEU A 77 8360 2699 3562 -271 -874 -1120 A C ATOM 494 N PHE A 78 15.286 25.417 9.434 1.00 32.50 A N ANISOU 494 N PHE A 78 6995 2191 3164 166 -564 -900 A N ATOM 495 CA PHE A 78 15.844 25.317 10.769 1.00 32.88 A C ANISOU 495 CA PHE A 78 6965 2228 3302 225 -566 -835 A C ATOM 496 C PHE A 78 15.011 26.174 11.758 1.00 31.23 A C ANISOU 496 C PHE A 78 6627 2090 3148 69 -598 -732 A C ATOM 497 O PHE A 78 14.774 25.736 12.887 1.00 31.09 A O ANISOU 497 O PHE A 78 6638 1997 3177 31 -644 -675 A O ATOM 498 CB PHE A 78 17.314 25.756 10.740 1.00 34.09 A C ANISOU 498 CB PHE A 78 6980 2496 3475 405 -472 -843 A C ATOM 499 CG PHE A 78 18.114 25.583 12.014 1.00 35.49 A C ANISOU 499 CG PHE A 78 7078 2670 3735 494 -493 -783 A C ATOM 500 CD1 PHE A 78 17.807 24.579 12.915 1.00 36.83 A C ANISOU 500 CD1 PHE A 78 7383 2677 3933 491 -579 -756 A C ATOM 501 CD2 PHE A 78 19.219 26.371 12.267 1.00 36.22 A C ANISOU 501 CD2 PHE A 78 6972 2920 3869 577 -436 -750 A C ATOM 502 CE1 PHE A 78 18.544 24.423 14.086 1.00 37.67 A C ANISOU 502 CE1 PHE A 78 7433 2780 4100 576 -614 -693 A C ATOM 503 CE2 PHE A 78 19.977 26.185 13.413 1.00 37.07 A C ANISOU 503 CE2 PHE A 78 7007 3031 4046 657 -481 -692 A C ATOM 504 CZ PHE A 78 19.613 25.246 14.337 1.00 37.11 A C ANISOU 504 CZ PHE A 78 7154 2876 4070 659 -574 -662 A C ATOM 505 N SER A 79 14.514 27.346 11.318 1.00 29.56 A N ANISOU 505 N SER A 79 6299 2011 2920 -15 -570 -707 A N ATOM 506 CA SER A 79 13.682 28.218 12.150 1.00 28.84 A C ANISOU 506 CA SER A 79 6098 1987 2872 -133 -582 -619 A C ATOM 507 C SER A 79 12.307 27.588 12.383 1.00 29.58 A C ANISOU 507 C SER A 79 6262 2002 2976 -280 -656 -590 A C ATOM 508 O SER A 79 11.785 27.686 13.482 1.00 30.91 A O ANISOU 508 O SER A 79 6388 2168 3189 -349 -661 -517 A O ATOM 509 CB SER A 79 13.524 29.607 11.517 1.00 27.88 A C ANISOU 509 CB SER A 79 5861 2007 2725 -159 -536 -603 A C ATOM 510 OG SER A 79 14.786 30.224 11.323 1.00 26.94 A O ANISOU 510 OG SER A 79 5669 1968 2599 -59 -464 -617 A O ATOM 511 N VAL A 80 11.719 26.959 11.366 1.00 29.24 A N ANISOU 511 N VAL A 80 6324 1902 2884 -340 -712 -644 A N ATOM 512 CA VAL A 80 10.444 26.236 11.491 1.00 30.58 A C ANISOU 512 CA VAL A 80 6558 1997 3066 -508 -799 -616 A C ATOM 513 C VAL A 80 10.619 25.093 12.521 1.00 32.34 A C ANISOU 513 C VAL A 80 6903 2064 3321 -518 -825 -594 A C ATOM 514 O VAL A 80 9.774 24.906 13.394 1.00 33.36 A O ANISOU 514 O VAL A 80 7006 2178 3492 -648 -845 -515 A O ATOM 515 CB VAL A 80 9.971 25.681 10.106 1.00 30.62 A C ANISOU 515 CB VAL A 80 6692 1950 2992 -573 -878 -693 A C ATOM 516 CG1 VAL A 80 8.886 24.626 10.253 1.00 31.00 A C ANISOU 516 CG1 VAL A 80 6846 1881 3050 -759 -988 -675 A C ATOM 517 CG2 VAL A 80 9.499 26.799 9.187 1.00 30.88 A C ANISOU 517 CG2 VAL A 80 6608 2135 2988 -598 -879 -686 A C ATOM 518 N TYR A 81 11.751 24.381 12.446 1.00 32.24 A N ANISOU 518 N TYR A 81 7019 1945 3288 -367 -813 -657 A N ATOM 519 CA TYR A 81 12.084 23.289 13.361 1.00 32.92 A C ANISOU 519 CA TYR A 81 7249 1865 3395 -337 -845 -636 A C ATOM 520 C TYR A 81 12.261 23.798 14.813 1.00 33.07 A C ANISOU 520 C TYR A 81 7153 1943 3468 -330 -811 -536 A C ATOM 521 O TYR A 81 11.729 23.185 15.743 1.00 33.67 A O ANISOU 521 O TYR A 81 7307 1925 3560 -429 -845 -468 A O ATOM 522 CB TYR A 81 13.356 22.570 12.883 1.00 33.00 A C ANISOU 522 CB TYR A 81 7393 1773 3373 -124 -831 -725 A C ATOM 523 CG TYR A 81 13.796 21.487 13.834 1.00 34.78 A C ANISOU 523 CG TYR A 81 7773 1820 3620 -55 -873 -697 A C ATOM 524 CD1 TYR A 81 13.204 20.231 13.806 1.00 35.32 A C ANISOU 524 CD1 TYR A 81 8090 1669 3660 -149 -955 -711 A C ATOM 525 CD2 TYR A 81 14.775 21.728 14.796 1.00 35.42 A C ANISOU 525 CD2 TYR A 81 7765 1946 3745 89 -846 -647 A C ATOM 526 CE1 TYR A 81 13.571 19.247 14.704 1.00 36.66 A C ANISOU 526 CE1 TYR A 81 8428 1657 3843 -88 -1000 -672 A C ATOM 527 CE2 TYR A 81 15.161 20.739 15.690 1.00 36.08 A C ANISOU 527 CE2 TYR A 81 8003 1864 3843 161 -901 -608 A C ATOM 528 CZ TYR A 81 14.538 19.511 15.656 1.00 37.35 A C ANISOU 528 CZ TYR A 81 8421 1797 3972 74 -973 -617 A C ATOM 529 OH TYR A 81 14.921 18.509 16.511 1.00 39.16 A O ANISOU 529 OH TYR A 81 8836 1839 4206 150 -1032 -573 A O ATOM 530 N MET A 82 13.013 24.891 15.014 1.00 32.30 A N ANISOU 530 N MET A 82 6892 1992 3387 -226 -746 -524 A N ATOM 531 CA MET A 82 13.216 25.439 16.353 1.00 31.25 A C ANISOU 531 CA MET A 82 6678 1913 3285 -224 -725 -440 A C ATOM 532 C MET A 82 11.928 25.981 16.918 1.00 31.46 A C ANISOU 532 C MET A 82 6634 1999 3320 -391 -705 -365 A C ATOM 533 O MET A 82 11.680 25.797 18.107 1.00 31.67 A O ANISOU 533 O MET A 82 6694 1990 3351 -441 -703 -292 A O ATOM 534 CB MET A 82 14.287 26.508 16.378 1.00 30.56 A C ANISOU 534 CB MET A 82 6444 1960 3206 -106 -676 -449 A C ATOM 535 CG MET A 82 15.660 25.951 16.266 1.00 32.48 A C ANISOU 535 CG MET A 82 6714 2167 3458 72 -688 -490 A C ATOM 536 SD MET A 82 16.924 27.223 16.454 1.00 36.84 A S ANISOU 536 SD MET A 82 7064 2900 4034 165 -643 -476 A S ATOM 537 CE MET A 82 16.522 28.300 15.043 1.00 28.13 A C ANISOU 537 CE MET A 82 5866 1923 2899 106 -565 -524 A C ATOM 538 N CYS A 83 11.065 26.589 16.077 1.00 31.14 A N ANISOU 538 N CYS A 83 6504 2050 3278 -473 -690 -378 A N ATOM 539 CA CYS A 83 9.762 27.087 16.528 1.00 31.10 A C ANISOU 539 CA CYS A 83 6404 2121 3292 -611 -664 -303 A C ATOM 540 C CYS A 83 8.913 25.911 17.035 1.00 29.92 A C ANISOU 540 C CYS A 83 6357 1859 3151 -758 -707 -254 A C ATOM 541 O CYS A 83 8.401 25.946 18.154 1.00 29.17 A O ANISOU 541 O CYS A 83 6242 1775 3065 -828 -664 -171 A O ATOM 542 CB CYS A 83 9.056 27.846 15.406 1.00 33.04 A C ANISOU 542 CB CYS A 83 6538 2480 3536 -649 -666 -325 A C ATOM 543 SG CYS A 83 7.590 28.764 15.938 1.00 39.23 A S ANISOU 543 SG CYS A 83 7148 3402 4356 -752 -614 -229 A S ATOM 544 N TYR A 84 8.853 24.837 16.245 1.00 29.09 A N ANISOU 544 N TYR A 84 6389 1631 3032 -803 -786 -308 A N ATOM 545 CA TYR A 84 8.107 23.628 16.598 1.00 29.40 A C ANISOU 545 CA TYR A 84 6563 1534 3075 -967 -844 -266 A C ATOM 546 C TYR A 84 8.649 23.039 17.912 1.00 30.35 A C ANISOU 546 C TYR A 84 6806 1539 3188 -929 -828 -208 A C ATOM 547 O TYR A 84 7.869 22.639 18.779 1.00 31.22 A O ANISOU 547 O TYR A 84 6942 1618 3303 -1078 -814 -116 A O ATOM 548 CB TYR A 84 8.202 22.601 15.441 1.00 29.60 A C ANISOU 548 CB TYR A 84 6769 1412 3065 -992 -943 -357 A C ATOM 549 CG TYR A 84 7.618 21.244 15.767 1.00 31.54 A C ANISOU 549 CG TYR A 84 7211 1467 3303 -1163 -1019 -323 A C ATOM 550 CD1 TYR A 84 6.260 20.994 15.616 1.00 32.70 A C ANISOU 550 CD1 TYR A 84 7309 1645 3472 -1414 -1068 -267 A C ATOM 551 CD2 TYR A 84 8.422 20.211 16.230 1.00 33.47 A C ANISOU 551 CD2 TYR A 84 7691 1502 3523 -1077 -1049 -339 A C ATOM 552 CE1 TYR A 84 5.718 19.746 15.908 1.00 34.56 A C ANISOU 552 CE1 TYR A 84 7735 1698 3699 -1607 -1142 -228 A C ATOM 553 CE2 TYR A 84 7.886 18.968 16.556 1.00 34.63 A C ANISOU 553 CE2 TYR A 84 8053 1449 3657 -1245 -1122 -299 A C ATOM 554 CZ TYR A 84 6.531 18.743 16.400 1.00 36.09 A C ANISOU 554 CZ TYR A 84 8193 1660 3858 -1525 -1166 -243 A C ATOM 555 OH TYR A 84 6.006 17.502 16.694 1.00 39.82 A O ANISOU 555 OH TYR A 84 8890 1926 4315 -1724 -1243 -199 A O ATOM 556 N GLU A 85 9.979 23.019 18.078 1.00 29.65 A N ANISOU 556 N GLU A 85 6781 1402 3084 -732 -829 -251 A N ATOM 557 CA GLU A 85 10.579 22.450 19.280 1.00 29.45 A C ANISOU 557 CA GLU A 85 6880 1266 3044 -676 -840 -194 A C ATOM 558 C GLU A 85 10.282 23.326 20.497 1.00 29.68 A C ANISOU 558 C GLU A 85 6796 1415 3067 -715 -766 -102 A C ATOM 559 O GLU A 85 10.022 22.774 21.563 1.00 30.04 A O ANISOU 559 O GLU A 85 6951 1378 3086 -788 -766 -18 A O ATOM 560 CB GLU A 85 12.078 22.226 19.085 1.00 30.19 A C ANISOU 560 CB GLU A 85 7035 1303 3133 -443 -872 -259 A C ATOM 561 CG GLU A 85 12.357 21.082 18.141 1.00 31.88 A C ANISOU 561 CG GLU A 85 7435 1344 3333 -388 -935 -342 A C ATOM 562 CD GLU A 85 11.978 19.738 18.735 1.00 37.06 A C ANISOU 562 CD GLU A 85 8342 1770 3968 -478 -1005 -291 A C ATOM 563 OE1 GLU A 85 12.465 19.442 19.851 1.00 36.97 A O ANISOU 563 OE1 GLU A 85 8406 1692 3949 -415 -1022 -219 A O ATOM 564 OE2 GLU A 85 11.183 18.994 18.111 1.00 37.64 A O1- ANISOU 564 OE2 GLU A 85 8549 1726 4026 -627 -1051 -317 A O1- ATOM 565 N PHE A 86 10.246 24.671 20.342 1.00 28.32 A N ANISOU 565 N PHE A 86 6430 1424 2905 -677 -699 -115 A N ATOM 566 CA PHE A 86 9.875 25.538 21.450 1.00 28.33 A C ANISOU 566 CA PHE A 86 6353 1525 2885 -710 -620 -40 A C ATOM 567 C PHE A 86 8.413 25.333 21.816 1.00 29.78 A C ANISOU 567 C PHE A 86 6506 1736 3074 -896 -564 39 A C ATOM 568 O PHE A 86 8.077 25.389 22.987 1.00 30.89 A O ANISOU 568 O PHE A 86 6679 1883 3175 -947 -503 120 A O ATOM 569 CB PHE A 86 10.123 27.017 21.116 1.00 27.77 A C ANISOU 569 CB PHE A 86 6116 1615 2822 -628 -565 -76 A C ATOM 570 CG PHE A 86 11.541 27.476 21.316 1.00 27.46 A C ANISOU 570 CG PHE A 86 6079 1586 2767 -479 -594 -112 A C ATOM 571 CD1 PHE A 86 12.145 27.391 22.563 1.00 28.08 A C ANISOU 571 CD1 PHE A 86 6242 1623 2803 -443 -614 -64 A C ATOM 572 CD2 PHE A 86 12.247 28.073 20.279 1.00 27.45 A C ANISOU 572 CD2 PHE A 86 5987 1653 2789 -388 -601 -185 A C ATOM 573 CE1 PHE A 86 13.419 27.930 22.773 1.00 28.94 A C ANISOU 573 CE1 PHE A 86 6320 1770 2904 -326 -656 -88 A C ATOM 574 CE2 PHE A 86 13.541 28.559 20.476 1.00 27.82 A C ANISOU 574 CE2 PHE A 86 6002 1737 2831 -276 -624 -206 A C ATOM 575 CZ PHE A 86 14.112 28.503 21.721 1.00 28.01 A C ANISOU 575 CZ PHE A 86 6086 1730 2825 -249 -659 -157 A C ATOM 576 N VAL A 87 7.537 25.106 20.833 1.00 30.03 A N ANISOU 576 N VAL A 87 6469 1795 3146 -1004 -585 21 A N ATOM 577 CA VAL A 87 6.122 24.842 21.080 1.00 30.86 A C ANISOU 577 CA VAL A 87 6506 1947 3272 -1199 -543 104 A C ATOM 578 C VAL A 87 5.954 23.464 21.830 1.00 32.93 A C ANISOU 578 C VAL A 87 6969 2036 3508 -1334 -577 172 A C ATOM 579 O VAL A 87 5.205 23.356 22.806 1.00 32.94 A O ANISOU 579 O VAL A 87 6957 2067 3491 -1456 -496 275 A O ATOM 580 CB VAL A 87 5.342 24.864 19.732 1.00 30.75 A C ANISOU 580 CB VAL A 87 6376 1999 3307 -1287 -600 64 A C ATOM 581 CG1 VAL A 87 3.962 24.214 19.855 1.00 31.47 A C ANISOU 581 CG1 VAL A 87 6413 2113 3433 -1527 -602 151 A C ATOM 582 CG2 VAL A 87 5.220 26.265 19.167 1.00 30.10 A C ANISOU 582 CG2 VAL A 87 6096 2095 3244 -1182 -552 33 A C ATOM 583 N MET A 88 6.672 22.442 21.391 1.00 34.04 A N ANISOU 583 N MET A 88 7306 1990 3637 -1301 -686 118 A N ATOM 584 CA MET A 88 6.558 21.105 21.977 1.00 36.03 A C ANISOU 584 CA MET A 88 7788 2043 3860 -1421 -736 179 A C ATOM 585 C MET A 88 7.347 20.917 23.286 1.00 37.73 A C ANISOU 585 C MET A 88 8150 2171 4013 -1322 -716 239 A C ATOM 586 O MET A 88 7.138 19.908 23.970 1.00 37.67 A O ANISOU 586 O MET A 88 8337 2006 3968 -1434 -741 318 A O ATOM 587 CB MET A 88 6.978 20.069 20.938 1.00 36.60 A C ANISOU 587 CB MET A 88 8045 1926 3935 -1408 -863 91 A C ATOM 588 CG MET A 88 6.093 20.115 19.728 1.00 41.20 A C ANISOU 588 CG MET A 88 8524 2575 4555 -1547 -905 45 A C ATOM 589 SD MET A 88 4.384 19.615 20.098 1.00 57.38 A S ANISOU 589 SD MET A 88 10509 4660 6632 -1902 -893 173 A S ATOM 590 CE MET A 88 3.517 20.742 19.113 1.00 52.42 A C ANISOU 590 CE MET A 88 9560 4296 6064 -1939 -876 146 A C ATOM 591 N SER A 89 8.233 21.860 23.626 1.00 39.07 A N ANISOU 591 N SER A 89 8242 2436 4166 -1131 -686 208 A N ATOM 592 CA SER A 89 9.027 21.833 24.852 1.00 40.84 A C ANISOU 592 CA SER A 89 8588 2605 4324 -1032 -689 261 A C ATOM 593 C SER A 89 8.342 22.581 26.025 1.00 41.61 A C ANISOU 593 C SER A 89 8618 2828 4364 -1114 -563 354 A C ATOM 594 O SER A 89 8.853 22.543 27.161 1.00 42.96 A O ANISOU 594 O SER A 89 8917 2952 4455 -1065 -565 411 A O ATOM 595 CB SER A 89 10.385 22.476 24.601 1.00 43.25 A C ANISOU 595 CB SER A 89 8838 2957 4639 -801 -738 180 A C ATOM 596 OG SER A 89 11.083 21.795 23.574 1.00 46.55 A O ANISOU 596 OG SER A 89 9319 3270 5098 -695 -828 94 A O ATOM 597 N GLY A 90 7.265 23.333 25.739 1.00 40.10 A N ANISOU 597 N GLY A 90 8227 2801 4206 -1211 -456 363 A N ATOM 598 CA GLY A 90 6.549 24.069 26.768 1.00 38.55 A C ANISOU 598 CA GLY A 90 7961 2731 3954 -1265 -310 442 A C ATOM 599 C GLY A 90 5.445 25.004 26.315 1.00 37.39 A C ANISOU 599 C GLY A 90 7564 2781 3861 -1314 -194 441 A C ATOM 600 O GLY A 90 4.353 24.978 26.879 1.00 37.77 A O ANISOU 600 O GLY A 90 7547 2907 3895 -1447 -73 531 A O ATOM 601 N TRP A 91 5.707 25.846 25.305 1.00 36.01 A N ANISOU 601 N TRP A 91 7242 2695 3746 -1204 -224 349 A N ATOM 602 CA TRP A 91 4.792 26.914 24.861 1.00 34.68 A C ANISOU 602 CA TRP A 91 6841 2712 3624 -1199 -128 345 A C ATOM 603 C TRP A 91 3.406 26.443 24.361 1.00 35.75 A C ANISOU 603 C TRP A 91 6827 2925 3831 -1381 -102 405 A C ATOM 604 O TRP A 91 2.427 27.168 24.545 1.00 35.82 A O ANISOU 604 O TRP A 91 6651 3098 3861 -1396 20 454 A O ATOM 605 CB TRP A 91 5.463 27.798 23.803 1.00 32.67 A C ANISOU 605 CB TRP A 91 6500 2505 3407 -1051 -189 241 A C ATOM 606 CG TRP A 91 6.582 28.598 24.406 1.00 30.83 A C ANISOU 606 CG TRP A 91 6347 2256 3109 -898 -183 202 A C ATOM 607 CD1 TRP A 91 7.917 28.327 24.327 1.00 31.06 A C ANISOU 607 CD1 TRP A 91 6493 2188 3122 -808 -288 148 A C ATOM 608 CD2 TRP A 91 6.445 29.675 25.349 1.00 29.66 A C ANISOU 608 CD2 TRP A 91 6191 2183 2895 -835 -68 225 A C ATOM 609 CE2 TRP A 91 7.740 30.002 25.802 1.00 30.15 A C ANISOU 609 CE2 TRP A 91 6376 2181 2897 -734 -132 183 A C ATOM 610 CE3 TRP A 91 5.346 30.315 25.939 1.00 29.33 A C ANISOU 610 CE3 TRP A 91 6064 2251 2830 -854 86 281 A C ATOM 611 NE1 TRP A 91 8.624 29.203 25.121 1.00 31.05 A N ANISOU 611 NE1 TRP A 91 6535 2207 3054 -714 -265 140 A N ATOM 612 CZ2 TRP A 91 7.965 30.983 26.762 1.00 29.81 A C ANISOU 612 CZ2 TRP A 91 6395 2167 2764 -670 -65 187 A C ATOM 613 CZ3 TRP A 91 5.577 31.311 26.865 1.00 29.91 A C ANISOU 613 CZ3 TRP A 91 6206 2347 2810 -760 173 277 A C ATOM 614 CH2 TRP A 91 6.875 31.653 27.246 1.00 29.89 A C ANISOU 614 CH2 TRP A 91 6351 2266 2742 -679 90 226 A C ATOM 615 N GLY A 92 3.327 25.265 23.756 1.00 35.95 A N ANISOU 615 N GLY A 92 6933 2836 3892 -1514 -217 402 A N ATOM 616 CA GLY A 92 2.062 24.724 23.280 1.00 36.53 A C ANISOU 616 CA GLY A 92 6877 2972 4031 -1726 -224 463 A C ATOM 617 C GLY A 92 1.564 23.546 24.100 1.00 38.08 A C ANISOU 617 C GLY A 92 7202 3067 4199 -1939 -203 570 A C ATOM 618 O GLY A 92 0.569 22.914 23.730 1.00 38.92 A O ANISOU 618 O GLY A 92 7226 3203 4360 -2159 -230 628 A O ATOM 619 N ILE A 93 2.230 23.223 25.233 1.00 38.13 A N ANISOU 619 N ILE A 93 7419 2954 4115 -1894 -163 606 A N ATOM 620 CA ILE A 93 1.857 22.052 26.018 1.00 38.41 A C ANISOU 620 CA ILE A 93 7625 2862 4105 -2096 -150 715 A C ATOM 621 C ILE A 93 1.695 22.343 27.517 1.00 38.77 A C ANISOU 621 C ILE A 93 7721 2957 4051 -2091 19 817 A C ATOM 622 O ILE A 93 1.749 21.402 28.299 1.00 38.94 A O ANISOU 622 O ILE A 93 7959 2834 4002 -2210 17 902 A O ATOM 623 CB ILE A 93 2.876 20.901 25.811 1.00 38.71 A C ANISOU 623 CB ILE A 93 7971 2625 4113 -2077 -318 670 A C ATOM 624 CG1 ILE A 93 4.261 21.287 26.361 1.00 39.62 A C ANISOU 624 CG1 ILE A 93 8231 2666 4157 -1823 -343 615 A C ATOM 625 CG2 ILE A 93 2.961 20.453 24.335 1.00 38.77 A C ANISOU 625 CG2 ILE A 93 7976 2560 4196 -2101 -473 568 A C ATOM 626 CD1 ILE A 93 5.099 20.111 26.741 1.00 40.77 A C ANISOU 626 CD1 ILE A 93 8689 2555 4246 -1806 -458 630 A C ATOM 627 N GLY A 94 1.469 23.597 27.913 1.00 38.63 A N ANISOU 627 N GLY A 94 7535 3128 4014 -1960 163 811 A N ATOM 628 CA GLY A 94 1.244 23.883 29.332 1.00 38.58 A C ANISOU 628 CA GLY A 94 7598 3170 3890 -1958 338 901 A C ATOM 629 C GLY A 94 1.687 25.220 29.866 1.00 38.58 A C ANISOU 629 C GLY A 94 7573 3267 3819 -1732 434 847 A C ATOM 630 O GLY A 94 1.244 25.625 30.943 1.00 39.39 A O ANISOU 630 O GLY A 94 7694 3450 3823 -1729 612 915 A O ATOM 631 N TYR A 95 2.586 25.913 29.154 1.00 37.41 A N ANISOU 631 N TYR A 95 7406 3103 3706 -1548 323 724 A N ATOM 632 CA TYR A 95 3.035 27.247 29.563 1.00 36.57 A C ANISOU 632 CA TYR A 95 7287 3072 3535 -1351 394 665 A C ATOM 633 C TYR A 95 1.846 28.204 29.562 1.00 37.15 A C ANISOU 633 C TYR A 95 7124 3353 3640 -1328 582 692 A C ATOM 634 O TYR A 95 1.008 28.154 28.666 1.00 37.49 A O ANISOU 634 O TYR A 95 6942 3501 3803 -1396 582 704 A O ATOM 635 CB TYR A 95 4.137 27.789 28.638 1.00 35.12 A C ANISOU 635 CB TYR A 95 7096 2847 3403 -1195 241 539 A C ATOM 636 CG TYR A 95 5.555 27.371 28.976 1.00 33.80 A C ANISOU 636 CG TYR A 95 7151 2518 3173 -1122 96 502 A C ATOM 637 CD1 TYR A 95 5.819 26.162 29.626 1.00 34.07 A C ANISOU 637 CD1 TYR A 95 7389 2406 3151 -1210 37 570 A C ATOM 638 CD2 TYR A 95 6.633 28.124 28.552 1.00 33.53 A C ANISOU 638 CD2 TYR A 95 7113 2478 3148 -968 4 406 A C ATOM 639 CE1 TYR A 95 7.124 25.758 29.891 1.00 33.80 A C ANISOU 639 CE1 TYR A 95 7537 2233 3072 -1118 -112 543 A C ATOM 640 CE2 TYR A 95 7.934 27.731 28.804 1.00 33.62 A C ANISOU 640 CE2 TYR A 95 7281 2371 3121 -896 -137 379 A C ATOM 641 CZ TYR A 95 8.178 26.557 29.482 1.00 34.08 A C ANISOU 641 CZ TYR A 95 7528 2293 3126 -957 -197 447 A C ATOM 642 OH TYR A 95 9.485 26.247 29.725 1.00 34.90 A O ANISOU 642 OH TYR A 95 7764 2297 3200 -856 -344 425 A O ATOM 643 N SER A 96 1.740 29.011 30.597 1.00 37.27 A N ANISOU 643 N SER A 96 7199 3423 3538 -1234 739 708 A N ATOM 644 CA SER A 96 0.636 29.945 30.796 1.00 37.71 A C ANISOU 644 CA SER A 96 7061 3668 3600 -1171 949 738 A C ATOM 645 C SER A 96 0.786 31.264 30.033 1.00 37.98 A C ANISOU 645 C SER A 96 6970 3770 3689 -977 933 639 A C ATOM 646 O SER A 96 -0.189 32.011 29.943 1.00 38.57 A O ANISOU 646 O SER A 96 6850 4003 3802 -903 1083 661 A O ATOM 647 CB SER A 96 0.524 30.270 32.284 1.00 39.11 A C ANISOU 647 CB SER A 96 7411 3852 3598 -1130 1137 785 A C ATOM 648 OG SER A 96 1.636 31.047 32.702 1.00 40.48 A O ANISOU 648 OG SER A 96 7798 3924 3659 -975 1072 693 A O ATOM 649 N PHE A 97 2.002 31.582 29.542 1.00 37.41 A N ANISOU 649 N PHE A 97 7014 3584 3616 -887 762 538 A N ATOM 650 CA PHE A 97 2.339 32.865 28.893 1.00 37.07 A C ANISOU 650 CA PHE A 97 6913 3572 3601 -715 735 446 A C ATOM 651 C PHE A 97 2.423 34.025 29.940 1.00 37.98 A C ANISOU 651 C PHE A 97 7167 3689 3573 -570 879 421 A C ATOM 652 O PHE A 97 2.410 35.190 29.569 1.00 37.78 A O ANISOU 652 O PHE A 97 7100 3695 3557 -428 906 363 A O ATOM 653 CB PHE A 97 1.387 33.229 27.738 1.00 35.92 A C ANISOU 653 CB PHE A 97 6487 3566 3597 -694 749 452 A C ATOM 654 CG PHE A 97 1.556 32.337 26.529 1.00 35.66 A C ANISOU 654 CG PHE A 97 6369 3502 3680 -809 567 438 A C ATOM 655 CD1 PHE A 97 1.049 31.044 26.520 1.00 35.51 A C ANISOU 655 CD1 PHE A 97 6315 3475 3703 -1002 539 509 A C ATOM 656 CD2 PHE A 97 2.234 32.783 25.409 1.00 35.69 A C ANISOU 656 CD2 PHE A 97 6353 3472 3735 -734 429 353 A C ATOM 657 CE1 PHE A 97 1.221 30.218 25.418 1.00 35.78 A C ANISOU 657 CE1 PHE A 97 6315 3456 3824 -1106 369 484 A C ATOM 658 CE2 PHE A 97 2.368 31.963 24.289 1.00 36.08 A C ANISOU 658 CE2 PHE A 97 6349 3490 3869 -830 275 332 A C ATOM 659 CZ PHE A 97 1.863 30.685 24.302 1.00 35.47 A C ANISOU 659 CZ PHE A 97 6258 3393 3828 -1011 242 391 A C ATOM 660 N ARG A 98 2.549 33.682 31.237 1.00 38.91 A N ANISOU 660 N ARG A 98 7483 3756 3547 -611 959 464 A N ATOM 661 CA ARG A 98 2.682 34.604 32.363 1.00 40.40 A C ANISOU 661 CA ARG A 98 7867 3921 3563 -498 1087 439 A C ATOM 662 C ARG A 98 3.951 34.189 33.155 1.00 41.01 A C ANISOU 662 C ARG A 98 8233 3842 3508 -546 944 419 A C ATOM 663 O ARG A 98 5.044 34.344 32.606 1.00 41.24 A O ANISOU 663 O ARG A 98 8302 3791 3576 -524 752 350 A O ATOM 664 CB ARG A 98 1.392 34.623 33.201 1.00 42.29 A C ANISOU 664 CB ARG A 98 8050 4282 3736 -495 1355 523 A C ATOM 665 CG ARG A 98 0.267 35.294 32.456 1.00 47.43 A C ANISOU 665 CG ARG A 98 8410 5096 4513 -396 1481 533 A C ATOM 666 CD ARG A 98 -1.073 34.831 32.951 1.00 52.82 A C ANISOU 666 CD ARG A 98 8923 5941 5206 -459 1708 649 A C ATOM 667 NE ARG A 98 -2.154 35.427 32.170 1.00 57.14 A N ANISOU 667 NE ARG A 98 9149 6666 5896 -357 1804 670 A N ATOM 668 N CYS A 99 3.842 33.636 34.381 1.00 41.54 A N ANISOU 668 N CYS A 99 8486 3874 3423 -613 1027 487 A N ATOM 669 CA CYS A 99 5.029 33.183 35.106 1.00 42.78 A C ANISOU 669 CA CYS A 99 8908 3889 3457 -655 865 482 A C ATOM 670 C CYS A 99 5.358 31.745 34.721 1.00 41.40 A C ANISOU 670 C CYS A 99 8708 3649 3374 -786 714 541 A C ATOM 671 O CYS A 99 4.911 30.829 35.404 1.00 42.34 A O ANISOU 671 O CYS A 99 8913 3747 3427 -896 782 640 A O ATOM 672 CB CYS A 99 4.851 33.310 36.619 1.00 45.81 A C ANISOU 672 CB CYS A 99 9553 4246 3605 -656 1004 525 A C ATOM 673 SG CYS A 99 6.355 32.965 37.582 1.00 53.88 A S ANISOU 673 SG CYS A 99 10919 5103 4452 -687 775 517 A S ATOM 674 N ASP A 100 6.112 31.536 33.645 1.00 39.11 A N ANISOU 674 N ASP A 100 8317 3319 3226 -772 523 485 A N ATOM 675 CA ASP A 100 6.609 30.206 33.329 1.00 38.44 A C ANISOU 675 CA ASP A 100 8262 3138 3206 -861 365 524 A C ATOM 676 C ASP A 100 8.020 30.159 33.859 1.00 39.52 A C ANISOU 676 C ASP A 100 8598 3164 3255 -807 181 496 A C ATOM 677 O ASP A 100 8.836 31.011 33.494 1.00 40.27 A O ANISOU 677 O ASP A 100 8662 3268 3369 -715 88 411 A O ATOM 678 CB ASP A 100 6.547 29.914 31.838 1.00 37.36 A C ANISOU 678 CB ASP A 100 7907 3026 3263 -870 280 481 A C ATOM 679 CG ASP A 100 5.138 30.009 31.342 1.00 36.19 A C ANISOU 679 CG ASP A 100 7547 3004 3199 -929 437 516 A C ATOM 680 OD1 ASP A 100 4.279 29.280 31.870 1.00 36.03 A O ANISOU 680 OD1 ASP A 100 7538 3001 3151 -1054 544 614 A O ATOM 681 OD2 ASP A 100 4.883 30.827 30.448 1.00 34.92 A O1- ANISOU 681 OD2 ASP A 100 7207 2933 3129 -856 453 457 A O1- ATOM 682 N ILE A 101 8.281 29.270 34.806 1.00 39.31 A N ANISOU 682 N ILE A 101 8780 3039 3116 -867 135 576 A N ATOM 683 CA ILE A 101 9.603 29.153 35.399 1.00 39.68 A C ANISOU 683 CA ILE A 101 9013 2990 3074 -813 -59 567 A C ATOM 684 C ILE A 101 10.413 28.109 34.638 1.00 38.75 A C ANISOU 684 C ILE A 101 8853 2784 3085 -796 -254 566 A C ATOM 685 O ILE A 101 9.855 27.352 33.823 1.00 38.68 A O ANISOU 685 O ILE A 101 8736 2761 3200 -852 -228 582 A O ATOM 686 CB ILE A 101 9.486 28.807 36.919 1.00 41.17 A C ANISOU 686 CB ILE A 101 9485 3116 3043 -868 -15 660 A C ATOM 687 CG1 ILE A 101 9.012 27.363 37.145 1.00 42.07 A C ANISOU 687 CG1 ILE A 101 9687 3141 3155 -982 -1 777 A C ATOM 688 CG2 ILE A 101 8.571 29.816 37.622 1.00 42.21 A C ANISOU 688 CG2 ILE A 101 9659 3339 3039 -867 219 654 A C ATOM 689 CD1 ILE A 101 9.130 26.825 38.617 1.00 42.42 A C ANISOU 689 CD1 ILE A 101 10053 3092 2972 -1037 -6 885 A C ATOM 690 N VAL A 102 11.735 28.077 34.868 1.00 37.84 A N ANISOU 690 N VAL A 102 8821 2613 2943 -715 -453 546 A N ATOM 691 CA VAL A 102 12.562 27.045 34.244 1.00 37.45 A C ANISOU 691 CA VAL A 102 8748 2476 3004 -662 -629 550 A C ATOM 692 C VAL A 102 12.328 25.714 34.944 1.00 38.24 A C ANISOU 692 C VAL A 102 9061 2436 3031 -726 -656 663 A C ATOM 693 O VAL A 102 12.200 25.675 36.166 1.00 39.33 A O ANISOU 693 O VAL A 102 9406 2538 2998 -771 -634 739 A O ATOM 694 CB VAL A 102 14.065 27.389 34.282 1.00 36.46 A C ANISOU 694 CB VAL A 102 8610 2356 2885 -545 -834 507 A C ATOM 695 CG1 VAL A 102 14.877 26.360 33.470 1.00 35.90 A C ANISOU 695 CG1 VAL A 102 8476 2216 2950 -452 -983 500 A C ATOM 696 CG2 VAL A 102 14.321 28.819 33.821 1.00 35.70 A C ANISOU 696 CG2 VAL A 102 8356 2385 2821 -516 -806 411 A C ATOM 697 N ASP A 103 12.286 24.632 34.189 1.00 38.01 A N ANISOU 697 N ASP A 103 9009 2315 3117 -731 -707 675 A N ATOM 698 CA ASP A 103 12.239 23.273 34.716 1.00 37.69 A C ANISOU 698 CA ASP A 103 9194 2103 3023 -779 -770 780 A C ATOM 699 C ASP A 103 13.662 22.754 34.611 1.00 38.91 A C ANISOU 699 C ASP A 103 9403 2167 3214 -610 -1000 767 A C ATOM 700 O ASP A 103 14.131 22.528 33.503 1.00 39.61 A O ANISOU 700 O ASP A 103 9351 2250 3449 -516 -1064 692 A O ATOM 701 CB ASP A 103 11.250 22.412 33.910 1.00 37.96 A C ANISOU 701 CB ASP A 103 9187 2076 3159 -902 -685 797 A C ATOM 702 CG ASP A 103 11.005 20.998 34.432 1.00 43.28 A C ANISOU 702 CG ASP A 103 10120 2550 3773 -996 -728 915 A C ATOM 703 OD1 ASP A 103 11.816 20.510 35.277 1.00 42.22 A O ANISOU 703 OD1 ASP A 103 10206 2300 3538 -917 -863 980 A O ATOM 704 OD2 ASP A 103 10.018 20.368 33.987 1.00 46.01 A O1- ANISOU 704 OD2 ASP A 103 10456 2853 4172 -1154 -641 947 A O1- ATOM 705 N TYR A 104 14.366 22.607 35.742 1.00 39.40 A N ANISOU 705 N TYR A 104 9659 2171 3139 -560 -1124 840 A N ATOM 706 CA TYR A 104 15.760 22.152 35.789 1.00 39.19 A C ANISOU 706 CA TYR A 104 9668 2080 3141 -382 -1358 846 A C ATOM 707 C TYR A 104 15.931 20.645 35.948 1.00 40.82 A C ANISOU 707 C TYR A 104 10096 2072 3343 -339 -1465 936 A C ATOM 708 O TYR A 104 17.070 20.175 36.071 1.00 40.60 A O ANISOU 708 O TYR A 104 10113 1981 3334 -165 -1663 957 A O ATOM 709 CB TYR A 104 16.505 22.847 36.927 1.00 37.92 A C ANISOU 709 CB TYR A 104 9595 1980 2831 -345 -1474 879 A C ATOM 710 CG TYR A 104 16.734 24.328 36.677 1.00 37.30 A C ANISOU 710 CG TYR A 104 9309 2088 2774 -346 -1434 777 A C ATOM 711 CD1 TYR A 104 17.700 24.760 35.783 1.00 37.50 A C ANISOU 711 CD1 TYR A 104 9093 2208 2947 -228 -1534 691 A C ATOM 712 CD2 TYR A 104 16.015 25.291 37.373 1.00 37.46 A C ANISOU 712 CD2 TYR A 104 9396 2182 2654 -463 -1294 771 A C ATOM 713 CE1 TYR A 104 17.918 26.113 35.555 1.00 38.39 A C ANISOU 713 CE1 TYR A 104 9041 2473 3074 -251 -1504 607 A C ATOM 714 CE2 TYR A 104 16.224 26.645 37.156 1.00 38.37 A C ANISOU 714 CE2 TYR A 104 9363 2435 2779 -463 -1264 678 A C ATOM 715 CZ TYR A 104 17.182 27.057 36.248 1.00 39.07 A C ANISOU 715 CZ TYR A 104 9221 2604 3019 -369 -1377 599 A C ATOM 716 OH TYR A 104 17.406 28.402 36.035 1.00 39.08 A O ANISOU 716 OH TYR A 104 9098 2725 3025 -390 -1355 515 A O ATOM 717 N SER A 105 14.839 19.873 35.919 1.00 41.90 A N ANISOU 717 N SER A 105 10366 2091 3461 -491 -1343 994 A N ATOM 718 CA SER A 105 14.929 18.428 36.061 1.00 43.03 A C ANISOU 718 CA SER A 105 10762 1998 3591 -473 -1441 1083 A C ATOM 719 C SER A 105 15.477 17.770 34.771 1.00 44.38 A C ANISOU 719 C SER A 105 10838 2083 3940 -321 -1526 996 A C ATOM 720 O SER A 105 15.589 18.393 33.703 1.00 44.57 A O ANISOU 720 O SER A 105 10599 2241 4096 -270 -1478 872 A O ATOM 721 CB SER A 105 13.565 17.850 36.418 1.00 45.28 A C ANISOU 721 CB SER A 105 11215 2189 3799 -720 -1280 1176 A C ATOM 722 OG SER A 105 12.701 17.925 35.296 1.00 49.88 A O ANISOU 722 OG SER A 105 11609 2827 4518 -830 -1144 1098 A O ATOM 723 N ARG A 106 15.840 16.519 34.890 1.00 45.07 A N ANISOU 723 N ARG A 106 11166 1941 4018 -239 -1650 1063 A N ATOM 724 CA ARG A 106 16.357 15.732 33.788 1.00 46.79 A C ANISOU 724 CA ARG A 106 11370 2033 4374 -76 -1728 989 A C ATOM 725 C ARG A 106 15.250 14.892 33.166 1.00 46.71 A C ANISOU 725 C ARG A 106 11493 1861 4396 -264 -1629 989 A C ATOM 726 O ARG A 106 15.504 13.762 32.766 1.00 48.50 A O ANISOU 726 O ARG A 106 11917 1854 4655 -176 -1718 993 A O ATOM 727 CB ARG A 106 17.506 14.860 34.291 1.00 49.95 A C ANISOU 727 CB ARG A 106 11969 2265 4746 165 -1941 1060 A C ATOM 728 CG ARG A 106 18.608 15.730 34.859 1.00 55.47 A C ANISOU 728 CG ARG A 106 12500 3152 5425 329 -2060 1061 A C ATOM 729 CD ARG A 106 19.727 14.904 35.468 1.00 62.05 A C ANISOU 729 CD ARG A 106 13510 3842 6224 572 -2290 1152 A C ATOM 730 NE ARG A 106 20.864 15.746 35.871 1.00 66.10 A N ANISOU 730 NE ARG A 106 13810 4561 6742 727 -2428 1146 A N ATOM 731 CZ ARG A 106 21.779 16.219 35.029 1.00 66.51 A C ANISOU 731 CZ ARG A 106 13551 4776 6945 913 -2467 1043 A C ATOM 732 NH1 ARG A 106 21.681 15.975 33.723 1.00 64.83 A N1+ ANISOU 732 NH1 ARG A 106 13211 4547 6876 981 -2364 929 A N1+ ATOM 733 NH2 ARG A 106 22.791 16.949 35.482 1.00 65.57 A N ANISOU 733 NH2 ARG A 106 13245 4842 6824 1018 -2608 1057 A N ATOM 734 N SER A 107 14.024 15.419 33.122 1.00 45.34 A N ANISOU 734 N SER A 107 11221 1800 4205 -522 -1453 990 A N ATOM 735 CA SER A 107 12.888 14.773 32.485 1.00 44.82 A C ANISOU 735 CA SER A 107 11220 1629 4180 -741 -1360 990 A C ATOM 736 C SER A 107 13.022 14.971 30.979 1.00 44.60 A C ANISOU 736 C SER A 107 10982 1662 4302 -658 -1353 832 A C ATOM 737 O SER A 107 13.553 16.014 30.569 1.00 44.72 A O ANISOU 737 O SER A 107 10729 1887 4377 -526 -1335 738 A O ATOM 738 CB SER A 107 11.591 15.401 32.990 1.00 45.58 A C ANISOU 738 CB SER A 107 11224 1880 4216 -1019 -1171 1052 A C ATOM 739 OG SER A 107 11.387 16.706 32.445 1.00 45.18 A O ANISOU 739 OG SER A 107 10834 2098 4235 -1007 -1065 949 A O ATOM 740 N PRO A 108 12.494 14.068 30.129 1.00 43.35 A N ANISOU 740 N PRO A 108 10942 1333 4197 -756 -1360 799 A N ATOM 741 CA PRO A 108 12.633 14.282 28.671 1.00 42.38 A C ANISOU 741 CA PRO A 108 10640 1269 4192 -673 -1354 643 A C ATOM 742 C PRO A 108 12.149 15.644 28.163 1.00 40.50 A C ANISOU 742 C PRO A 108 10046 1333 4009 -744 -1228 569 A C ATOM 743 O PRO A 108 12.843 16.239 27.348 1.00 40.18 A O ANISOU 743 O PRO A 108 9817 1410 4039 -565 -1239 454 A O ATOM 744 CB PRO A 108 11.831 13.140 28.056 1.00 43.64 A C ANISOU 744 CB PRO A 108 11022 1198 4363 -858 -1373 643 A C ATOM 745 CG PRO A 108 11.964 12.005 29.103 1.00 44.36 A C ANISOU 745 CG PRO A 108 11486 1012 4355 -882 -1459 783 A C ATOM 746 CD PRO A 108 11.882 12.768 30.433 1.00 43.02 A C ANISOU 746 CD PRO A 108 11237 1012 4098 -932 -1395 899 A C ATOM 747 N THR A 109 11.002 16.154 28.634 1.00 39.62 A N ANISOU 747 N THR A 109 9841 1349 3865 -986 -1102 638 A N ATOM 748 CA THR A 109 10.486 17.446 28.165 1.00 39.53 A C ANISOU 748 CA THR A 109 9507 1609 3905 -1034 -983 575 A C ATOM 749 C THR A 109 11.356 18.615 28.635 1.00 38.48 A C ANISOU 749 C THR A 109 9216 1653 3751 -850 -975 548 A C ATOM 750 O THR A 109 11.561 19.557 27.861 1.00 38.90 A O ANISOU 750 O THR A 109 9035 1873 3871 -771 -942 449 A O ATOM 751 CB THR A 109 9.024 17.655 28.583 1.00 42.29 A C ANISOU 751 CB THR A 109 9787 2053 4227 -1316 -843 664 A C ATOM 752 CG2 THR A 109 8.378 18.862 27.910 1.00 41.69 A C ANISOU 752 CG2 THR A 109 9388 2232 4219 -1354 -732 597 A C ATOM 753 OG1 THR A 109 8.292 16.464 28.272 1.00 46.37 A O ANISOU 753 OG1 THR A 109 10479 2386 4755 -1517 -875 709 A O ATOM 754 N ALA A 110 11.881 18.568 29.883 1.00 37.15 A N ANISOU 754 N ALA A 110 9189 1445 3484 -792 -1016 636 A N ATOM 755 CA ALA A 110 12.714 19.688 30.384 1.00 36.89 A C ANISOU 755 CA ALA A 110 9024 1574 3420 -646 -1031 611 A C ATOM 756 C ALA A 110 14.066 19.749 29.657 1.00 35.73 A C ANISOU 756 C ALA A 110 8786 1436 3355 -400 -1154 516 A C ATOM 757 O ALA A 110 14.550 20.845 29.394 1.00 36.20 A O ANISOU 757 O ALA A 110 8635 1673 3447 -320 -1138 450 A O ATOM 758 CB ALA A 110 12.935 19.572 31.885 1.00 36.69 A C ANISOU 758 CB ALA A 110 9194 1497 3250 -656 -1065 729 A C ATOM 759 N LEU A 111 14.663 18.592 29.340 1.00 34.32 A N ANISOU 759 N LEU A 111 8769 1066 3207 -280 -1269 514 A N ATOM 760 CA LEU A 111 15.918 18.534 28.586 1.00 34.80 A C ANISOU 760 CA LEU A 111 8733 1139 3351 -28 -1363 427 A C ATOM 761 C LEU A 111 15.707 18.979 27.128 1.00 35.87 A C ANISOU 761 C LEU A 111 8667 1378 3586 -26 -1282 297 A C ATOM 762 O LEU A 111 16.591 19.608 26.548 1.00 36.71 A O ANISOU 762 O LEU A 111 8580 1617 3752 131 -1295 221 A O ATOM 763 CB LEU A 111 16.513 17.118 28.603 1.00 34.79 A C ANISOU 763 CB LEU A 111 8982 886 3350 122 -1490 456 A C ATOM 764 CG LEU A 111 17.241 16.746 29.894 1.00 35.77 A C ANISOU 764 CG LEU A 111 9271 929 3391 228 -1621 573 A C ATOM 765 CD1 LEU A 111 17.515 15.280 29.948 1.00 36.60 A C ANISOU 765 CD1 LEU A 111 9676 746 3483 338 -1730 619 A C ATOM 766 CD2 LEU A 111 18.520 17.519 30.042 1.00 36.49 A C ANISOU 766 CD2 LEU A 111 9149 1199 3518 435 -1706 547 A C ATOM 767 N ARG A 112 14.537 18.670 26.545 1.00 34.96 A N ANISOU 767 N ARG A 112 8593 1209 3481 -213 -1204 280 A N ATOM 768 CA ARG A 112 14.186 19.088 25.202 1.00 34.77 A C ANISOU 768 CA ARG A 112 8403 1279 3529 -240 -1139 169 A C ATOM 769 C ARG A 112 14.119 20.611 25.133 1.00 34.72 A C ANISOU 769 C ARG A 112 8125 1530 3539 -261 -1053 140 A C ATOM 770 O ARG A 112 14.596 21.189 24.159 1.00 36.09 A O ANISOU 770 O ARG A 112 8132 1813 3768 -162 -1035 47 A O ATOM 771 CB ARG A 112 12.849 18.476 24.811 1.00 36.18 A C ANISOU 771 CB ARG A 112 8682 1360 3704 -474 -1097 184 A C ATOM 772 CG ARG A 112 12.466 18.713 23.376 1.00 38.28 A C ANISOU 772 CG ARG A 112 8825 1691 4029 -506 -1063 73 A C ATOM 773 CD ARG A 112 11.112 18.117 23.123 1.00 39.73 A C ANISOU 773 CD ARG A 112 9096 1792 4207 -768 -1046 105 A C ATOM 774 NE ARG A 112 10.737 18.203 21.713 1.00 41.72 A N ANISOU 774 NE ARG A 112 9270 2081 4499 -807 -1047 -1 A N ATOM 775 CZ ARG A 112 9.647 17.648 21.200 1.00 43.31 A C ANISOU 775 CZ ARG A 112 9538 2214 4704 -1031 -1066 4 A C ATOM 776 NH1 ARG A 112 8.813 16.966 21.977 1.00 43.89 A N1+ ANISOU 776 NH1 ARG A 112 9740 2183 4752 -1247 -1070 114 A N1+ ATOM 777 NH2 ARG A 112 9.387 17.759 19.904 1.00 42.05 A N ANISOU 777 NH2 ARG A 112 9320 2090 4565 -1054 -1087 -96 A N ATOM 778 N MET A 113 13.572 21.272 26.168 1.00 32.94 A N ANISOU 778 N MET A 113 7871 1390 3254 -379 -995 219 A N ATOM 779 CA MET A 113 13.522 22.732 26.188 1.00 31.80 A C ANISOU 779 CA MET A 113 7513 1459 3112 -387 -917 191 A C ATOM 780 C MET A 113 14.946 23.288 26.328 1.00 32.68 A C ANISOU 780 C MET A 113 7540 1645 3233 -202 -995 159 A C ATOM 781 O MET A 113 15.301 24.258 25.655 1.00 33.31 A O ANISOU 781 O MET A 113 7431 1868 3356 -154 -963 90 A O ATOM 782 CB MET A 113 12.606 23.216 27.321 1.00 31.44 A C ANISOU 782 CB MET A 113 7497 1465 2982 -538 -827 280 A C ATOM 783 CG MET A 113 12.681 24.731 27.600 1.00 32.79 A C ANISOU 783 CG MET A 113 7510 1818 3128 -519 -758 256 A C ATOM 784 SD MET A 113 12.243 25.739 26.130 1.00 32.51 A S ANISOU 784 SD MET A 113 7227 1937 3189 -522 -678 155 A S ATOM 785 CE MET A 113 10.439 25.732 26.256 1.00 24.52 A C ANISOU 785 CE MET A 113 6184 964 2168 -718 -539 214 A C ATOM 786 N ALA A 114 15.781 22.664 27.178 1.00 33.38 A N ANISOU 786 N ALA A 114 7763 1638 3281 -101 -1108 217 A N ATOM 787 CA ALA A 114 17.155 23.155 27.366 1.00 33.42 A C ANISOU 787 CA ALA A 114 7662 1733 3303 64 -1202 201 A C ATOM 788 C ALA A 114 17.972 23.038 26.057 1.00 32.09 A C ANISOU 788 C ALA A 114 7347 1605 3240 222 -1216 105 A C ATOM 789 O ALA A 114 18.634 24.000 25.667 1.00 31.57 A O ANISOU 789 O ALA A 114 7080 1702 3212 272 -1205 59 A O ATOM 790 CB ALA A 114 17.836 22.413 28.497 1.00 33.31 A C ANISOU 790 CB ALA A 114 7822 1607 3226 149 -1339 291 A C ATOM 791 N ARG A 115 17.839 21.902 25.349 1.00 30.66 A N ANISOU 791 N ARG A 115 7282 1275 3094 281 -1223 74 A N ATOM 792 CA ARG A 115 18.542 21.632 24.101 1.00 29.97 A C ANISOU 792 CA ARG A 115 7103 1200 3082 444 -1217 -21 A C ATOM 793 C ARG A 115 18.039 22.528 22.963 1.00 29.42 A C ANISOU 793 C ARG A 115 6864 1270 3044 358 -1101 -107 A C ATOM 794 O ARG A 115 18.837 22.942 22.122 1.00 29.69 A O ANISOU 794 O ARG A 115 6738 1416 3127 477 -1076 -174 A O ATOM 795 CB ARG A 115 18.429 20.138 23.728 1.00 31.30 A C ANISOU 795 CB ARG A 115 7505 1133 3253 521 -1257 -36 A C ATOM 796 CG ARG A 115 19.132 19.766 22.424 1.00 34.14 A C ANISOU 796 CG ARG A 115 7814 1486 3670 712 -1234 -145 A C ATOM 797 CD ARG A 115 20.616 20.088 22.441 1.00 36.16 A C ANISOU 797 CD ARG A 115 7880 1877 3980 950 -1273 -152 A C ATOM 798 NE ARG A 115 21.391 19.010 23.056 1.00 39.10 A N ANISOU 798 NE ARG A 115 8401 2098 4356 1155 -1390 -100 A N ATOM 799 CZ ARG A 115 22.709 19.032 23.205 1.00 42.37 A C ANISOU 799 CZ ARG A 115 8665 2609 4824 1390 -1452 -85 A C ATOM 800 NH1 ARG A 115 23.411 20.099 22.825 1.00 42.88 A N1+ ANISOU 800 NH1 ARG A 115 8424 2926 4941 1419 -1406 -114 A N1+ ATOM 801 NH2 ARG A 115 23.338 17.998 23.752 1.00 42.94 A N ANISOU 801 NH2 ARG A 115 8887 2529 4900 1593 -1567 -31 A N ATOM 802 N THR A 116 16.744 22.888 22.967 1.00 28.39 A N ANISOU 802 N THR A 116 6754 1148 2884 154 -1029 -94 A N ATOM 803 CA THR A 116 16.207 23.811 21.980 1.00 27.97 A C ANISOU 803 CA THR A 116 6545 1230 2854 74 -936 -158 A C ATOM 804 C THR A 116 16.780 25.218 22.189 1.00 28.69 A C ANISOU 804 C THR A 116 6442 1510 2950 92 -909 -157 A C ATOM 805 O THR A 116 17.039 25.918 21.204 1.00 28.47 A O ANISOU 805 O THR A 116 6272 1595 2952 120 -858 -221 A O ATOM 806 CB THR A 116 14.692 23.835 22.025 1.00 27.09 A C ANISOU 806 CB THR A 116 6480 1095 2718 -131 -878 -128 A C ATOM 807 CG2 THR A 116 14.111 24.745 20.931 1.00 26.00 A C ANISOU 807 CG2 THR A 116 6185 1090 2603 -194 -802 -189 A C ATOM 808 OG1 THR A 116 14.209 22.488 21.911 1.00 25.65 A O ANISOU 808 OG1 THR A 116 6497 723 2528 -179 -921 -119 A O ATOM 809 N CYS A 117 16.999 25.628 23.470 1.00 28.88 A N ANISOU 809 N CYS A 117 6485 1558 2931 66 -948 -85 A N ATOM 810 CA CYS A 117 17.635 26.912 23.781 1.00 29.69 A C ANISOU 810 CA CYS A 117 6443 1812 3026 69 -949 -83 A C ATOM 811 C CYS A 117 19.067 26.889 23.239 1.00 30.77 A C ANISOU 811 C CYS A 117 6448 2021 3224 228 -1005 -119 A C ATOM 812 O CYS A 117 19.494 27.837 22.574 1.00 29.88 A O ANISOU 812 O CYS A 117 6171 2043 3139 226 -962 -160 A O ATOM 813 CB CYS A 117 17.622 27.197 25.282 1.00 30.25 A C ANISOU 813 CB CYS A 117 6608 1870 3018 12 -999 -4 A C ATOM 814 SG CYS A 117 15.983 27.537 25.956 1.00 32.49 A S ANISOU 814 SG CYS A 117 6997 2125 3222 -166 -888 40 A S ATOM 815 N TRP A 118 19.791 25.771 23.480 1.00 32.09 A N ANISOU 815 N TRP A 118 6685 2096 3410 370 -1094 -100 A N ATOM 816 CA TRP A 118 21.148 25.583 22.984 1.00 33.87 A C ANISOU 816 CA TRP A 118 6771 2396 3703 554 -1138 -126 A C ATOM 817 C TRP A 118 21.189 25.678 21.453 1.00 33.64 A C ANISOU 817 C TRP A 118 6639 2424 3719 603 -1028 -219 A C ATOM 818 O TRP A 118 22.138 26.227 20.896 1.00 33.85 A O ANISOU 818 O TRP A 118 6472 2599 3791 679 -1004 -245 A O ATOM 819 CB TRP A 118 21.729 24.238 23.447 1.00 35.21 A C ANISOU 819 CB TRP A 118 7067 2427 3884 726 -1243 -89 A C ATOM 820 CG TRP A 118 23.099 23.991 22.898 1.00 37.91 A C ANISOU 820 CG TRP A 118 7242 2857 4304 949 -1272 -115 A C ATOM 821 CD1 TRP A 118 24.275 24.481 23.388 1.00 39.76 A C ANISOU 821 CD1 TRP A 118 7285 3244 4577 1025 -1360 -69 A C ATOM 822 CD2 TRP A 118 23.412 23.379 21.642 1.00 39.17 A C ANISOU 822 CD2 TRP A 118 7375 2996 4511 1107 -1191 -199 A C ATOM 823 CE2 TRP A 118 24.810 23.446 21.479 1.00 40.82 A C ANISOU 823 CE2 TRP A 118 7367 3350 4792 1302 -1221 -193 A C ATOM 824 CE3 TRP A 118 22.649 22.754 20.647 1.00 40.27 A C ANISOU 824 CE3 TRP A 118 7661 3007 4631 1103 -1101 -278 A C ATOM 825 NE1 TRP A 118 25.315 24.116 22.564 1.00 40.71 A N ANISOU 825 NE1 TRP A 118 7243 3445 4778 1238 -1335 -108 A N ATOM 826 CZ2 TRP A 118 25.455 22.919 20.357 1.00 42.54 A C ANISOU 826 CZ2 TRP A 118 7513 3592 5059 1510 -1136 -266 A C ATOM 827 CZ3 TRP A 118 23.295 22.192 19.563 1.00 41.94 A C ANISOU 827 CZ3 TRP A 118 7842 3217 4877 1304 -1038 -358 A C ATOM 828 CH2 TRP A 118 24.678 22.288 19.417 1.00 42.54 A C ANISOU 828 CH2 TRP A 118 7700 3442 5020 1514 -1041 -353 A C ATOM 829 N LEU A 119 20.182 25.113 20.788 1.00 33.28 A N ANISOU 829 N LEU A 119 6729 2264 3654 551 -968 -264 A N ATOM 830 CA LEU A 119 20.058 25.104 19.327 1.00 33.75 A C ANISOU 830 CA LEU A 119 6747 2350 3726 582 -875 -355 A C ATOM 831 C LEU A 119 19.844 26.524 18.812 1.00 32.29 A C ANISOU 831 C LEU A 119 6400 2334 3536 466 -796 -372 A C ATOM 832 O LEU A 119 20.462 26.900 17.829 1.00 32.42 A O ANISOU 832 O LEU A 119 6293 2456 3570 533 -732 -423 A O ATOM 833 CB LEU A 119 18.867 24.223 18.939 1.00 35.15 A C ANISOU 833 CB LEU A 119 7131 2356 3869 500 -864 -384 A C ATOM 834 CG LEU A 119 18.975 23.260 17.780 1.00 38.72 A C ANISOU 834 CG LEU A 119 7694 2704 4316 612 -839 -473 A C ATOM 835 CD1 LEU A 119 20.275 22.487 17.813 1.00 40.56 A C ANISOU 835 CD1 LEU A 119 7933 2897 4581 866 -870 -489 A C ATOM 836 CD2 LEU A 119 17.809 22.257 17.839 1.00 39.30 A C ANISOU 836 CD2 LEU A 119 8009 2571 4352 491 -879 -471 A C ATOM 837 N TYR A 120 18.979 27.300 19.493 1.00 30.65 A N ANISOU 837 N TYR A 120 6204 2144 3296 300 -793 -325 A N ATOM 838 CA TYR A 120 18.701 28.693 19.175 1.00 30.20 A C ANISOU 838 CA TYR A 120 6030 2217 3227 195 -730 -329 A C ATOM 839 C TYR A 120 19.975 29.520 19.302 1.00 30.00 A C ANISOU 839 C TYR A 120 5841 2331 3228 240 -745 -316 A C ATOM 840 O TYR A 120 20.298 30.312 18.411 1.00 30.74 A O ANISOU 840 O TYR A 120 5817 2534 3329 226 -680 -347 A O ATOM 841 CB TYR A 120 17.588 29.241 20.075 1.00 29.80 A C ANISOU 841 CB TYR A 120 6046 2141 3134 50 -723 -278 A C ATOM 842 CG TYR A 120 17.208 30.676 19.761 1.00 31.01 A C ANISOU 842 CG TYR A 120 6112 2400 3271 -38 -658 -282 A C ATOM 843 CD1 TYR A 120 16.466 30.991 18.630 1.00 32.32 A C ANISOU 843 CD1 TYR A 120 6250 2593 3436 -76 -592 -321 A C ATOM 844 CD2 TYR A 120 17.576 31.710 20.604 1.00 32.41 A C ANISOU 844 CD2 TYR A 120 6258 2634 3422 -84 -675 -247 A C ATOM 845 CE1 TYR A 120 16.103 32.299 18.349 1.00 34.10 A C ANISOU 845 CE1 TYR A 120 6417 2898 3643 -138 -541 -316 A C ATOM 846 CE2 TYR A 120 17.229 33.026 20.328 1.00 34.04 A C ANISOU 846 CE2 TYR A 120 6421 2907 3606 -155 -618 -251 A C ATOM 847 CZ TYR A 120 16.482 33.314 19.203 1.00 35.53 A C ANISOU 847 CZ TYR A 120 6581 3118 3801 -174 -548 -283 A C ATOM 848 OH TYR A 120 16.140 34.614 18.925 1.00 38.46 A O ANISOU 848 OH TYR A 120 6927 3540 4148 -226 -499 -279 A O ATOM 849 N TYR A 121 20.711 29.309 20.377 1.00 29.33 A N ANISOU 849 N TYR A 121 5751 2244 3152 283 -840 -265 A N ATOM 850 CA TYR A 121 21.992 29.955 20.648 1.00 29.75 A C ANISOU 850 CA TYR A 121 5636 2432 3236 313 -890 -239 A C ATOM 851 C TYR A 121 23.004 29.633 19.513 1.00 30.99 A C ANISOU 851 C TYR A 121 5636 2684 3455 456 -838 -282 A C ATOM 852 O TYR A 121 23.660 30.535 18.985 1.00 30.73 A O ANISOU 852 O TYR A 121 5435 2799 3443 420 -793 -286 A O ATOM 853 CB TYR A 121 22.512 29.479 22.021 1.00 28.73 A C ANISOU 853 CB TYR A 121 5558 2259 3097 353 -1030 -171 A C ATOM 854 CG TYR A 121 23.984 29.723 22.268 1.00 28.62 A C ANISOU 854 CG TYR A 121 5354 2384 3136 424 -1119 -137 A C ATOM 855 CD1 TYR A 121 24.480 31.011 22.414 1.00 29.17 A C ANISOU 855 CD1 TYR A 121 5293 2589 3202 297 -1137 -119 A C ATOM 856 CD2 TYR A 121 24.877 28.663 22.386 1.00 29.30 A C ANISOU 856 CD2 TYR A 121 5391 2463 3277 616 -1195 -117 A C ATOM 857 CE1 TYR A 121 25.824 31.241 22.655 1.00 29.62 A C ANISOU 857 CE1 TYR A 121 5151 2790 3313 333 -1233 -78 A C ATOM 858 CE2 TYR A 121 26.221 28.882 22.658 1.00 30.04 A C ANISOU 858 CE2 TYR A 121 5273 2710 3430 684 -1289 -73 A C ATOM 859 CZ TYR A 121 26.689 30.178 22.791 1.00 30.81 A C ANISOU 859 CZ TYR A 121 5219 2960 3529 528 -1310 -51 A C ATOM 860 OH TYR A 121 28.014 30.435 23.042 1.00 33.19 A O ANISOU 860 OH TYR A 121 5284 3431 3894 562 -1413 0 A O ATOM 861 N PHE A 122 23.120 28.351 19.155 1.00 31.76 A N ANISOU 861 N PHE A 122 5804 2689 3573 617 -837 -313 A N ATOM 862 CA PHE A 122 24.025 27.903 18.107 1.00 33.73 A C ANISOU 862 CA PHE A 122 5937 3012 3868 790 -767 -363 A C ATOM 863 C PHE A 122 23.627 28.492 16.743 1.00 32.14 A C ANISOU 863 C PHE A 122 5705 2871 3634 728 -627 -429 A C ATOM 864 O PHE A 122 24.501 28.843 15.960 1.00 31.87 A O ANISOU 864 O PHE A 122 5503 2982 3624 791 -546 -448 A O ATOM 865 CB PHE A 122 24.036 26.371 18.027 1.00 36.02 A C ANISOU 865 CB PHE A 122 6381 3140 4165 978 -793 -393 A C ATOM 866 CG PHE A 122 25.223 25.843 17.274 1.00 40.01 A C ANISOU 866 CG PHE A 122 6753 3726 4721 1213 -736 -431 A C ATOM 867 CD1 PHE A 122 26.471 25.765 17.880 1.00 42.48 A C ANISOU 867 CD1 PHE A 122 6880 4154 5107 1351 -810 -371 A C ATOM 868 CD2 PHE A 122 25.092 25.401 15.964 1.00 42.51 A C ANISOU 868 CD2 PHE A 122 7132 4011 5008 1305 -610 -525 A C ATOM 869 CE1 PHE A 122 27.569 25.274 17.177 1.00 44.65 A C ANISOU 869 CE1 PHE A 122 7002 4526 5437 1591 -739 -401 A C ATOM 870 CE2 PHE A 122 26.186 24.884 15.269 1.00 44.37 A C ANISOU 870 CE2 PHE A 122 7256 4324 5280 1548 -531 -565 A C ATOM 871 CZ PHE A 122 27.416 24.817 15.880 1.00 44.79 A C ANISOU 871 CZ PHE A 122 7096 4503 5418 1699 -588 -501 A C ATOM 872 N SER A 123 22.321 28.613 16.472 1.00 30.69 A N ANISOU 872 N SER A 123 5677 2590 3395 602 -600 -455 A N ATOM 873 CA SER A 123 21.837 29.180 15.226 1.00 31.08 A C ANISOU 873 CA SER A 123 5722 2687 3401 537 -494 -507 A C ATOM 874 C SER A 123 22.315 30.643 15.062 1.00 31.51 A C ANISOU 874 C SER A 123 5605 2909 3456 431 -449 -473 A C ATOM 875 O SER A 123 22.439 31.113 13.930 1.00 32.03 A O ANISOU 875 O SER A 123 5622 3055 3492 421 -350 -506 A O ATOM 876 CB SER A 123 20.312 29.101 15.140 1.00 31.81 A C ANISOU 876 CB SER A 123 5983 2659 3444 410 -505 -520 A C ATOM 877 OG SER A 123 19.662 30.108 15.899 1.00 33.07 A O ANISOU 877 OG SER A 123 6127 2843 3594 258 -530 -463 A O ATOM 878 N LYS A 124 22.593 31.355 16.179 1.00 30.61 A N ANISOU 878 N LYS A 124 5427 2838 3366 344 -525 -405 A N ATOM 879 CA LYS A 124 23.090 32.734 16.128 1.00 30.44 A C ANISOU 879 CA LYS A 124 5273 2950 3343 223 -503 -369 A C ATOM 880 C LYS A 124 24.498 32.778 15.523 1.00 30.91 A C ANISOU 880 C LYS A 124 5122 3173 3450 304 -450 -366 A C ATOM 881 O LYS A 124 24.834 33.759 14.881 1.00 30.84 A O ANISOU 881 O LYS A 124 5017 3275 3427 211 -378 -354 A O ATOM 882 CB LYS A 124 23.103 33.363 17.533 1.00 30.32 A C ANISOU 882 CB LYS A 124 5274 2921 3327 114 -613 -307 A C ATOM 883 CG LYS A 124 21.757 33.372 18.248 1.00 31.03 A C ANISOU 883 CG LYS A 124 5553 2871 3365 42 -642 -301 A C ATOM 884 CD LYS A 124 20.774 34.270 17.562 1.00 32.44 A C ANISOU 884 CD LYS A 124 5789 3039 3498 -56 -561 -319 A C ATOM 885 CE LYS A 124 19.508 33.558 17.235 1.00 33.99 A C ANISOU 885 CE LYS A 124 6108 3132 3674 -35 -531 -348 A C ATOM 886 NZ LYS A 124 18.586 34.396 16.422 1.00 34.84 A N1+ ANISOU 886 NZ LYS A 124 6244 3249 3744 -107 -464 -360 A N1+ ATOM 887 N PHE A 125 25.317 31.722 15.735 1.00 31.11 A N ANISOU 887 N PHE A 125 5074 3214 3531 481 -482 -369 A N ATOM 888 CA PHE A 125 26.662 31.618 15.167 1.00 32.36 A C ANISOU 888 CA PHE A 125 5004 3546 3747 598 -417 -363 A C ATOM 889 C PHE A 125 26.575 31.282 13.675 1.00 33.26 A C ANISOU 889 C PHE A 125 5145 3677 3816 694 -250 -438 A C ATOM 890 O PHE A 125 27.359 31.802 12.887 1.00 33.42 A O ANISOU 890 O PHE A 125 4994 3864 3841 691 -137 -431 A O ATOM 891 CB PHE A 125 27.509 30.570 15.905 1.00 32.35 A C ANISOU 891 CB PHE A 125 4922 3549 3820 791 -511 -338 A C ATOM 892 CG PHE A 125 27.950 31.057 17.259 1.00 33.62 A C ANISOU 892 CG PHE A 125 5001 3755 4018 692 -677 -252 A C ATOM 893 CD1 PHE A 125 29.059 31.875 17.392 1.00 34.68 A C ANISOU 893 CD1 PHE A 125 4876 4094 4208 615 -702 -191 A C ATOM 894 CD2 PHE A 125 27.209 30.769 18.392 1.00 34.44 A C ANISOU 894 CD2 PHE A 125 5299 3698 4087 646 -807 -230 A C ATOM 895 CE1 PHE A 125 29.442 32.356 18.641 1.00 35.34 A C ANISOU 895 CE1 PHE A 125 4908 4210 4308 500 -878 -117 A C ATOM 896 CE2 PHE A 125 27.591 31.256 19.627 1.00 35.02 A C ANISOU 896 CE2 PHE A 125 5332 3807 4168 546 -961 -157 A C ATOM 897 CZ PHE A 125 28.712 32.031 19.750 1.00 34.97 A C ANISOU 897 CZ PHE A 125 5081 3994 4213 475 -1008 -104 A C ATOM 898 N ILE A 126 25.614 30.431 13.276 1.00 33.35 A N ANISOU 898 N ILE A 126 5381 3518 3773 761 -235 -508 A N ATOM 899 CA ILE A 126 25.401 30.130 11.861 1.00 33.89 A C ANISOU 899 CA ILE A 126 5528 3579 3770 831 -96 -588 A C ATOM 900 C ILE A 126 24.963 31.410 11.126 1.00 34.53 A C ANISOU 900 C ILE A 126 5600 3735 3784 642 -22 -575 A C ATOM 901 O ILE A 126 25.412 31.647 10.010 1.00 35.13 A O ANISOU 901 O ILE A 126 5620 3915 3811 674 114 -602 A O ATOM 902 CB ILE A 126 24.361 29.011 11.695 1.00 34.58 A C ANISOU 902 CB ILE A 126 5882 3451 3807 893 -133 -659 A C ATOM 903 CG1 ILE A 126 24.892 27.695 12.290 1.00 36.11 A C ANISOU 903 CG1 ILE A 126 6114 3550 4055 1102 -194 -671 A C ATOM 904 CG2 ILE A 126 23.984 28.833 10.233 1.00 35.03 A C ANISOU 904 CG2 ILE A 126 6058 3488 3762 922 -15 -745 A C ATOM 905 CD1 ILE A 126 23.900 26.602 12.379 1.00 37.77 A C ANISOU 905 CD1 ILE A 126 6599 3526 4225 1126 -260 -721 A C ATOM 906 N GLU A 127 24.127 32.250 11.772 1.00 33.83 A N ANISOU 906 N GLU A 127 5573 3594 3687 458 -106 -530 A N ATOM 907 CA GLU A 127 23.620 33.481 11.171 1.00 33.70 A C ANISOU 907 CA GLU A 127 5579 3617 3607 293 -57 -510 A C ATOM 908 C GLU A 127 24.699 34.572 11.015 1.00 33.92 A C ANISOU 908 C GLU A 127 5411 3822 3654 204 4 -449 A C ATOM 909 O GLU A 127 24.473 35.568 10.315 1.00 33.33 A O ANISOU 909 O GLU A 127 5360 3786 3518 82 68 -430 A O ATOM 910 CB GLU A 127 22.408 33.989 11.937 1.00 35.55 A C ANISOU 910 CB GLU A 127 5942 3737 3830 160 -155 -482 A C ATOM 911 CG GLU A 127 21.208 33.087 11.698 1.00 39.17 A C ANISOU 911 CG GLU A 127 6580 4050 4251 200 -185 -535 A C ATOM 912 CD GLU A 127 20.055 33.242 12.670 1.00 44.47 A C ANISOU 912 CD GLU A 127 7349 4616 4932 108 -276 -503 A C ATOM 913 OE1 GLU A 127 20.008 34.265 13.393 1.00 44.21 A O ANISOU 913 OE1 GLU A 127 7280 4610 4910 8 -303 -448 A O ATOM 914 OE2 GLU A 127 19.201 32.325 12.713 1.00 46.90 A O1- ANISOU 914 OE2 GLU A 127 7777 4812 5232 132 -316 -533 A O1- ATOM 915 N LEU A 128 25.908 34.348 11.579 1.00 34.01 A N ANISOU 915 N LEU A 128 5226 3947 3750 267 -15 -414 A N ATOM 916 CA LEU A 128 27.045 35.229 11.332 1.00 33.51 A C ANISOU 916 CA LEU A 128 4942 4076 3715 179 50 -354 A C ATOM 917 C LEU A 128 27.411 35.187 9.825 1.00 33.51 A C ANISOU 917 C LEU A 128 4904 4180 3650 242 242 -388 A C ATOM 918 O LEU A 128 27.971 36.150 9.314 1.00 33.20 A O ANISOU 918 O LEU A 128 4751 4274 3590 112 328 -336 A O ATOM 919 CB LEU A 128 28.254 34.842 12.202 1.00 32.65 A C ANISOU 919 CB LEU A 128 4602 4085 3717 254 -22 -307 A C ATOM 920 CG LEU A 128 28.076 34.984 13.714 1.00 33.18 A C ANISOU 920 CG LEU A 128 4704 4073 3829 175 -217 -262 A C ATOM 921 CD1 LEU A 128 29.354 34.620 14.456 1.00 33.20 A C ANISOU 921 CD1 LEU A 128 4462 4216 3935 250 -302 -207 A C ATOM 922 CD2 LEU A 128 27.639 36.395 14.098 1.00 33.32 A C ANISOU 922 CD2 LEU A 128 4798 4060 3804 -80 -269 -217 A C ATOM 923 N LEU A 129 27.078 34.077 9.122 1.00 33.66 A N ANISOU 923 N LEU A 129 5043 4126 3622 429 309 -475 A N ATOM 924 CA LEU A 129 27.288 33.925 7.689 1.00 34.40 A C ANISOU 924 CA LEU A 129 5162 4288 3620 506 490 -524 A C ATOM 925 C LEU A 129 26.604 35.049 6.910 1.00 34.30 A C ANISOU 925 C LEU A 129 5270 4265 3498 316 536 -502 A C ATOM 926 O LEU A 129 27.129 35.409 5.870 1.00 34.24 A O ANISOU 926 O LEU A 129 5213 4380 3417 305 694 -495 A O ATOM 927 CB LEU A 129 26.803 32.575 7.190 1.00 35.14 A C ANISOU 927 CB LEU A 129 5444 4246 3660 710 513 -633 A C ATOM 928 CG LEU A 129 27.801 31.437 7.372 1.00 38.00 A C ANISOU 928 CG LEU A 129 5686 4658 4094 964 557 -666 A C ATOM 929 CD1 LEU A 129 27.159 30.100 7.030 1.00 38.59 A C ANISOU 929 CD1 LEU A 129 6017 4536 4109 1143 544 -776 A C ATOM 930 CD2 LEU A 129 29.027 31.654 6.503 1.00 39.15 A C ANISOU 930 CD2 LEU A 129 5616 5031 4227 1049 762 -653 A C ATOM 931 N ASP A 130 25.494 35.647 7.428 1.00 34.18 A N ANISOU 931 N ASP A 130 5404 4114 3469 172 407 -480 A N ATOM 932 CA ASP A 130 24.827 36.806 6.793 1.00 35.56 A C ANISOU 932 CA ASP A 130 5695 4268 3549 5 429 -444 A C ATOM 933 C ASP A 130 25.822 37.931 6.508 1.00 35.62 A C ANISOU 933 C ASP A 130 5546 4435 3553 -136 522 -360 A C ATOM 934 O ASP A 130 25.846 38.494 5.408 1.00 36.23 A O ANISOU 934 O ASP A 130 5679 4563 3523 -197 638 -344 A O ATOM 935 CB ASP A 130 23.719 37.427 7.699 1.00 38.04 A C ANISOU 935 CB ASP A 130 6129 4441 3884 -115 276 -412 A C ATOM 936 CG ASP A 130 22.488 36.605 8.005 1.00 44.59 A C ANISOU 936 CG ASP A 130 7118 5113 4710 -44 177 -469 A C ATOM 937 OD1 ASP A 130 22.271 35.577 7.317 1.00 44.92 A O ANISOU 937 OD1 ASP A 130 7239 5119 4707 78 211 -542 A O ATOM 938 OD2 ASP A 130 21.731 36.995 8.933 1.00 47.53 A O1- ANISOU 938 OD2 ASP A 130 7545 5397 5119 -116 70 -439 A O1- ATOM 939 N THR A 131 26.632 38.262 7.527 1.00 34.62 A N ANISOU 939 N THR A 131 5233 4383 3536 -205 460 -300 A N ATOM 940 CA THR A 131 27.602 39.346 7.454 1.00 34.82 A C ANISOU 940 CA THR A 131 5096 4557 3578 -381 517 -209 A C ATOM 941 C THR A 131 28.795 38.942 6.610 1.00 35.09 A C ANISOU 941 C THR A 131 4919 4799 3614 -295 698 -204 A C ATOM 942 O THR A 131 29.328 39.788 5.902 1.00 35.09 A O ANISOU 942 O THR A 131 4854 4918 3562 -435 818 -140 A O ATOM 943 CB THR A 131 28.036 39.841 8.841 1.00 35.73 A C ANISOU 943 CB THR A 131 5097 4679 3801 -505 365 -148 A C ATOM 944 CG2 THR A 131 28.299 41.325 8.853 1.00 35.57 A C ANISOU 944 CG2 THR A 131 5081 4683 3752 -768 358 -59 A C ATOM 945 OG1 THR A 131 27.059 39.529 9.841 1.00 36.91 A O ANISOU 945 OG1 THR A 131 5404 4649 3971 -465 209 -185 A O ATOM 946 N ILE A 132 29.185 37.654 6.622 1.00 35.28 A N ANISOU 946 N ILE A 132 4853 4864 3686 -57 735 -269 A N ATOM 947 CA ILE A 132 30.262 37.146 5.769 1.00 36.08 A C ANISOU 947 CA ILE A 132 4765 5162 3782 82 934 -278 A C ATOM 948 C ILE A 132 29.841 37.299 4.302 1.00 37.23 A C ANISOU 948 C ILE A 132 5094 5297 3754 87 1106 -317 A C ATOM 949 O ILE A 132 30.643 37.752 3.484 1.00 37.87 A O ANISOU 949 O ILE A 132 5045 5557 3785 35 1289 -269 A O ATOM 950 CB ILE A 132 30.624 35.682 6.114 1.00 36.42 A C ANISOU 950 CB ILE A 132 4733 5203 3902 374 924 -351 A C ATOM 951 CG1 ILE A 132 30.916 35.506 7.626 1.00 37.69 A C ANISOU 951 CG1 ILE A 132 4757 5349 4215 369 722 -308 A C ATOM 952 CG2 ILE A 132 31.774 35.173 5.261 1.00 36.67 A C ANISOU 952 CG2 ILE A 132 4556 5448 3931 551 1148 -362 A C ATOM 953 CD1 ILE A 132 32.005 36.340 8.140 1.00 39.12 A C ANISOU 953 CD1 ILE A 132 4638 5732 4493 208 699 -196 A C ATOM 954 N PHE A 133 28.557 37.004 3.977 1.00 37.13 A N ANISOU 954 N PHE A 133 5384 5081 3643 123 1039 -391 A N ATOM 955 CA PHE A 133 28.048 37.184 2.613 1.00 37.03 A C ANISOU 955 CA PHE A 133 5578 5042 3448 113 1162 -425 A C ATOM 956 C PHE A 133 28.124 38.667 2.233 1.00 37.50 A C ANISOU 956 C PHE A 133 5640 5162 3445 -139 1204 -316 A C ATOM 957 O PHE A 133 28.582 38.962 1.141 1.00 37.87 A O ANISOU 957 O PHE A 133 5690 5324 3376 -164 1387 -295 A O ATOM 958 CB PHE A 133 26.611 36.657 2.457 1.00 36.43 A C ANISOU 958 CB PHE A 133 5802 4744 3295 167 1037 -510 A C ATOM 959 CG PHE A 133 26.482 35.153 2.333 1.00 36.74 A C ANISOU 959 CG PHE A 133 5928 4705 3328 406 1041 -629 A C ATOM 960 CD1 PHE A 133 27.087 34.473 1.291 1.00 37.39 A C ANISOU 960 CD1 PHE A 133 6032 4867 3309 573 1229 -698 A C ATOM 961 CD2 PHE A 133 25.698 34.431 3.219 1.00 36.98 A C ANISOU 961 CD2 PHE A 133 6050 4566 3435 459 863 -674 A C ATOM 962 CE1 PHE A 133 26.951 33.093 1.169 1.00 38.22 A C ANISOU 962 CE1 PHE A 133 6261 4867 3396 798 1228 -816 A C ATOM 963 CE2 PHE A 133 25.579 33.054 3.104 1.00 37.52 A C ANISOU 963 CE2 PHE A 133 6230 4537 3491 662 859 -779 A C ATOM 964 CZ PHE A 133 26.197 32.395 2.076 1.00 37.63 A C ANISOU 964 CZ PHE A 133 6281 4611 3406 832 1035 -853 A C ATOM 965 N PHE A 134 27.752 39.596 3.148 1.00 37.16 A N ANISOU 965 N PHE A 134 5605 5041 3474 -324 1045 -245 A N ATOM 966 CA PHE A 134 27.832 41.038 2.876 1.00 37.57 A C ANISOU 966 CA PHE A 134 5691 5114 3469 -569 1068 -139 A C ATOM 967 C PHE A 134 29.247 41.453 2.520 1.00 38.62 A C ANISOU 967 C PHE A 134 5571 5481 3621 -665 1239 -58 A C ATOM 968 O PHE A 134 29.435 42.238 1.607 1.00 38.78 A O ANISOU 968 O PHE A 134 5651 5559 3525 -800 1366 7 A O ATOM 969 CB PHE A 134 27.405 41.908 4.080 1.00 37.41 A C ANISOU 969 CB PHE A 134 5705 4974 3536 -733 876 -83 A C ATOM 970 CG PHE A 134 26.029 41.797 4.690 1.00 37.51 A C ANISOU 970 CG PHE A 134 5927 4772 3553 -686 702 -131 A C ATOM 971 CD1 PHE A 134 24.962 41.322 3.954 1.00 37.87 A C ANISOU 971 CD1 PHE A 134 6176 4714 3498 -576 697 -195 A C ATOM 972 CD2 PHE A 134 25.791 42.235 5.983 1.00 37.50 A C ANISOU 972 CD2 PHE A 134 5923 4681 3646 -768 544 -105 A C ATOM 973 CE1 PHE A 134 23.701 41.223 4.523 1.00 38.28 A C ANISOU 973 CE1 PHE A 134 6381 4597 3567 -542 544 -227 A C ATOM 974 CE2 PHE A 134 24.532 42.139 6.544 1.00 37.69 A C ANISOU 974 CE2 PHE A 134 6120 4528 3671 -719 412 -143 A C ATOM 975 CZ PHE A 134 23.493 41.643 5.811 1.00 37.81 A C ANISOU 975 CZ PHE A 134 6296 4462 3606 -608 416 -198 A C ATOM 976 N VAL A 135 30.241 40.965 3.276 1.00 39.20 A N ANISOU 976 N VAL A 135 5356 5695 3844 -608 1235 -48 A N ATOM 977 CA VAL A 135 31.642 41.321 3.065 1.00 39.85 A C ANISOU 977 CA VAL A 135 5132 6034 3976 -704 1384 40 A C ATOM 978 C VAL A 135 32.153 40.752 1.730 1.00 40.47 A C ANISOU 978 C VAL A 135 5166 6267 3943 -552 1652 7 A C ATOM 979 O VAL A 135 32.680 41.513 0.916 1.00 41.18 A O ANISOU 979 O VAL A 135 5211 6490 3947 -709 1821 90 A O ATOM 980 CB VAL A 135 32.522 40.866 4.259 1.00 40.24 A C ANISOU 980 CB VAL A 135 4869 6198 4220 -656 1281 60 A C ATOM 981 CG1 VAL A 135 34.010 40.965 3.923 1.00 40.72 A C ANISOU 981 CG1 VAL A 135 4559 6569 4345 -696 1457 144 A C ATOM 982 CG2 VAL A 135 32.190 41.672 5.515 1.00 39.90 A C ANISOU 982 CG2 VAL A 135 4876 6028 4256 -864 1039 111 A C ATOM 983 N LEU A 136 31.962 39.448 1.485 1.00 40.02 A N ANISOU 983 N LEU A 136 5157 6177 3870 -256 1697 -113 A N ATOM 984 CA LEU A 136 32.425 38.813 0.256 1.00 40.23 A C ANISOU 984 CA LEU A 136 5179 6333 3776 -76 1955 -165 A C ATOM 985 C LEU A 136 31.738 39.368 -0.980 1.00 40.28 A C ANISOU 985 C LEU A 136 5486 6262 3555 -171 2056 -167 A C ATOM 986 O LEU A 136 32.355 39.401 -2.049 1.00 40.88 A O ANISOU 986 O LEU A 136 5526 6498 3508 -145 2304 -151 A O ATOM 987 CB LEU A 136 32.224 37.294 0.307 1.00 40.38 A C ANISOU 987 CB LEU A 136 5261 6271 3810 260 1949 -306 A C ATOM 988 CG LEU A 136 32.894 36.537 1.452 1.00 41.25 A C ANISOU 988 CG LEU A 136 5105 6442 4127 416 1852 -312 A C ATOM 989 CD1 LEU A 136 32.676 35.049 1.284 1.00 41.31 A C ANISOU 989 CD1 LEU A 136 5239 6344 4112 754 1875 -452 A C ATOM 990 CD2 LEU A 136 34.394 36.857 1.553 1.00 41.45 A C ANISOU 990 CD2 LEU A 136 4704 6780 4267 384 1996 -207 A C ATOM 991 N ARG A 137 30.467 39.780 -0.862 1.00 39.45 A N ANISOU 991 N ARG A 137 5676 5924 3388 -268 1870 -182 A N ATOM 992 CA ARG A 137 29.761 40.364 -2.011 1.00 39.31 A C ANISOU 992 CA ARG A 137 5954 5829 3154 -359 1931 -171 A C ATOM 993 C ARG A 137 30.027 41.871 -2.164 1.00 41.25 A C ANISOU 993 C ARG A 137 6186 6125 3364 -661 1959 -20 A C ATOM 994 O ARG A 137 29.554 42.476 -3.131 1.00 42.60 A O ANISOU 994 O ARG A 137 6595 6243 3350 -753 2016 15 A O ATOM 995 CB ARG A 137 28.261 40.122 -1.921 1.00 38.34 A C ANISOU 995 CB ARG A 137 6141 5451 2976 -314 1722 -246 A C ATOM 996 CG ARG A 137 27.885 38.663 -1.973 1.00 37.64 A C ANISOU 996 CG ARG A 137 6138 5284 2882 -52 1696 -393 A C ATOM 997 CD ARG A 137 26.398 38.519 -1.801 1.00 38.53 A C ANISOU 997 CD ARG A 137 6515 5164 2960 -56 1475 -446 A C ATOM 998 NE ARG A 137 25.686 38.765 -3.051 1.00 39.88 A N ANISOU 998 NE ARG A 137 6967 5277 2909 -86 1507 -460 A N ATOM 999 CZ ARG A 137 24.819 39.755 -3.245 1.00 41.36 A C ANISOU 999 CZ ARG A 137 7319 5369 3026 -244 1393 -388 A C ATOM 1000 NH1 ARG A 137 24.521 40.587 -2.261 1.00 39.42 A N1+ ANISOU 1000 NH1 ARG A 137 7001 5063 2914 -377 1250 -308 A N1+ ATOM 1001 NH2 ARG A 137 24.231 39.909 -4.426 1.00 41.97 A N ANISOU 1001 NH2 ARG A 137 7651 5405 2891 -256 1415 -398 A N ATOM 1002 N LYS A 138 30.806 42.466 -1.240 1.00 41.38 A N ANISOU 1002 N LYS A 138 5939 6238 3545 -821 1915 73 A N ATOM 1003 CA LYS A 138 31.184 43.873 -1.186 1.00 41.79 A C ANISOU 1003 CA LYS A 138 5960 6327 3592 -1133 1920 220 A C ATOM 1004 C LYS A 138 29.962 44.767 -0.979 1.00 41.91 A C ANISOU 1004 C LYS A 138 6294 6083 3546 -1265 1722 246 A C ATOM 1005 O LYS A 138 29.927 45.887 -1.471 1.00 42.34 A O ANISOU 1005 O LYS A 138 6485 6105 3499 -1479 1757 349 A O ATOM 1006 CB LYS A 138 31.995 44.294 -2.418 1.00 43.56 A C ANISOU 1006 CB LYS A 138 6136 6744 3670 -1233 2198 301 A C ATOM 1007 CG LYS A 138 33.271 43.474 -2.576 1.00 47.54 A C ANISOU 1007 CG LYS A 138 6282 7532 4248 -1090 2414 287 A C ATOM 1008 CD LYS A 138 34.168 44.002 -3.682 1.00 52.62 A C ANISOU 1008 CD LYS A 138 6833 8400 4761 -1224 2710 390 A C ATOM 1009 CE LYS A 138 34.714 45.361 -3.342 1.00 56.73 A C ANISOU 1009 CE LYS A 138 7239 8979 5336 -1599 2681 560 A C ATOM 1010 NZ LYS A 138 35.896 45.699 -4.177 1.00 59.68 A N1+ ANISOU 1010 NZ LYS A 138 7384 9644 5647 -1730 2987 674 A N1+ ATOM 1011 N LYS A 139 28.993 44.287 -0.205 1.00 41.34 A N ANISOU 1011 N LYS A 139 6331 5831 3545 -1138 1518 159 A N ATOM 1012 CA LYS A 139 27.795 45.013 0.160 1.00 41.63 A C ANISOU 1012 CA LYS A 139 6629 5633 3555 -1215 1325 174 A C ATOM 1013 C LYS A 139 28.052 45.672 1.498 1.00 42.67 A C ANISOU 1013 C LYS A 139 6651 5719 3841 -1368 1175 227 A C ATOM 1014 O LYS A 139 27.411 45.359 2.503 1.00 43.17 A O ANISOU 1014 O LYS A 139 6744 5658 4001 -1289 1003 171 A O ATOM 1015 CB LYS A 139 26.585 44.063 0.222 1.00 42.60 A C ANISOU 1015 CB LYS A 139 6914 5609 3663 -993 1205 53 A C ATOM 1016 CG LYS A 139 26.324 43.278 -1.079 1.00 44.01 A C ANISOU 1016 CG LYS A 139 7224 5821 3678 -837 1330 -19 A C ATOM 1017 CD LYS A 139 25.935 44.154 -2.263 1.00 46.38 A C ANISOU 1017 CD LYS A 139 7764 6083 3774 -946 1393 50 A C ATOM 1018 CE LYS A 139 24.865 45.197 -1.980 1.00 49.16 A C ANISOU 1018 CE LYS A 139 8329 6242 4108 -1056 1210 114 A C ATOM 1019 NZ LYS A 139 23.584 44.605 -1.507 1.00 51.05 A N1+ ANISOU 1019 NZ LYS A 139 8675 6327 4393 -911 1018 29 A N1+ ATOM 1020 N ASN A 140 29.020 46.578 1.518 1.00 42.81 A N ANISOU 1020 N ASN A 140 6548 5842 3875 -1603 1243 339 A N ATOM 1021 CA ASN A 140 29.402 47.276 2.734 1.00 43.36 A C ANISOU 1021 CA ASN A 140 6526 5876 4073 -1787 1099 395 A C ATOM 1022 C ASN A 140 28.262 48.130 3.311 1.00 42.35 A C ANISOU 1022 C ASN A 140 6697 5477 3917 -1852 912 400 A C ATOM 1023 O ASN A 140 28.255 48.364 4.517 1.00 43.11 A O ANISOU 1023 O ASN A 140 6766 5496 4118 -1912 757 395 A O ATOM 1024 CB ASN A 140 30.652 48.117 2.489 1.00 45.58 A C ANISOU 1024 CB ASN A 140 6632 6325 4359 -2061 1212 523 A C ATOM 1025 CG ASN A 140 31.883 47.245 2.274 1.00 51.03 A C ANISOU 1025 CG ASN A 140 6946 7313 5131 -1981 1374 520 A C ATOM 1026 ND2 ASN A 140 32.863 47.778 1.554 1.00 52.12 A N ANISOU 1026 ND2 ASN A 140 6937 7641 5225 -2169 1557 628 A N ATOM 1027 OD1 ASN A 140 31.967 46.082 2.743 1.00 52.67 A O ANISOU 1027 OD1 ASN A 140 6992 7583 5439 -1744 1344 427 A O ATOM 1028 N SER A 141 27.262 48.514 2.493 1.00 40.53 A N ANISOU 1028 N SER A 141 6751 5102 3545 -1810 920 404 A N ATOM 1029 CA SER A 141 26.115 49.283 2.993 1.00 39.06 A C ANISOU 1029 CA SER A 141 6840 4667 3336 -1823 756 408 A C ATOM 1030 C SER A 141 25.194 48.434 3.871 1.00 36.86 A C ANISOU 1030 C SER A 141 6565 4296 3144 -1609 618 299 A C ATOM 1031 O SER A 141 24.382 49.008 4.591 1.00 36.50 A O ANISOU 1031 O SER A 141 6684 4069 3113 -1613 485 298 A O ATOM 1032 CB SER A 141 25.309 49.895 1.851 1.00 40.65 A C ANISOU 1032 CB SER A 141 7323 4756 3365 -1816 791 453 A C ATOM 1033 OG SER A 141 24.515 48.925 1.185 1.00 44.01 A O ANISOU 1033 OG SER A 141 7798 5193 3733 -1587 806 370 A O ATOM 1034 N GLN A 142 25.287 47.086 3.803 1.00 35.24 A N ANISOU 1034 N GLN A 142 6197 4204 2988 -1421 659 210 A N ATOM 1035 CA GLN A 142 24.495 46.196 4.643 1.00 33.98 A C ANISOU 1035 CA GLN A 142 6033 3966 2912 -1241 538 116 A C ATOM 1036 C GLN A 142 25.212 45.877 5.995 1.00 33.58 A C ANISOU 1036 C GLN A 142 5784 3964 3011 -1269 459 102 A C ATOM 1037 O GLN A 142 24.585 45.336 6.916 1.00 32.40 A O ANISOU 1037 O GLN A 142 5652 3728 2928 -1160 345 43 A O ATOM 1038 CB GLN A 142 24.172 44.900 3.882 1.00 34.57 A C ANISOU 1038 CB GLN A 142 6085 4101 2950 -1035 602 29 A C ATOM 1039 CG GLN A 142 23.049 45.075 2.874 1.00 35.31 A C ANISOU 1039 CG GLN A 142 6413 4097 2906 -978 595 23 A C ATOM 1040 CD GLN A 142 22.711 43.806 2.141 1.00 36.16 A C ANISOU 1040 CD GLN A 142 6532 4246 2963 -799 636 -71 A C ATOM 1041 NE2 GLN A 142 21.651 43.155 2.557 1.00 35.63 A N ANISOU 1041 NE2 GLN A 142 6529 4075 2934 -683 513 -136 A N ATOM 1042 OE1 GLN A 142 23.385 43.404 1.192 1.00 36.72 A O ANISOU 1042 OE1 GLN A 142 6565 4436 2952 -770 782 -85 A O ATOM 1043 N VAL A 143 26.528 46.199 6.115 1.00 34.00 A N ANISOU 1043 N VAL A 143 5641 4166 3111 -1421 516 163 A N ATOM 1044 CA VAL A 143 27.264 45.997 7.365 1.00 34.34 A C ANISOU 1044 CA VAL A 143 5496 4266 3285 -1469 417 165 A C ATOM 1045 C VAL A 143 27.076 47.257 8.211 1.00 34.20 A C ANISOU 1045 C VAL A 143 5634 4099 3263 -1673 287 218 A C ATOM 1046 O VAL A 143 27.938 48.126 8.257 1.00 35.24 A O ANISOU 1046 O VAL A 143 5709 4285 3397 -1904 293 300 A O ATOM 1047 CB VAL A 143 28.757 45.667 7.128 1.00 35.25 A C ANISOU 1047 CB VAL A 143 5291 4634 3467 -1523 523 207 A C ATOM 1048 CG1 VAL A 143 29.442 45.280 8.430 1.00 35.78 A C ANISOU 1048 CG1 VAL A 143 5154 4767 3672 -1532 390 205 A C ATOM 1049 CG2 VAL A 143 28.923 44.559 6.092 1.00 35.49 A C ANISOU 1049 CG2 VAL A 143 5222 4794 3467 -1310 688 152 A C ATOM 1050 N THR A 144 25.903 47.401 8.797 1.00 33.11 A N ANISOU 1050 N THR A 144 5713 3764 3104 -1593 181 174 A N ATOM 1051 CA THR A 144 25.550 48.562 9.601 1.00 32.64 A C ANISOU 1051 CA THR A 144 5858 3526 3019 -1738 67 206 A C ATOM 1052 C THR A 144 25.751 48.266 11.082 1.00 33.35 A C ANISOU 1052 C THR A 144 5886 3592 3192 -1740 -73 171 A C ATOM 1053 O THR A 144 25.943 47.106 11.466 1.00 34.05 A O ANISOU 1053 O THR A 144 5801 3779 3358 -1598 -89 122 A O ATOM 1054 CB THR A 144 24.070 48.914 9.315 1.00 32.69 A C ANISOU 1054 CB THR A 144 6138 3339 2944 -1615 53 181 A C ATOM 1055 CG2 THR A 144 23.840 49.347 7.883 1.00 32.27 A C ANISOU 1055 CG2 THR A 144 6186 3288 2786 -1628 162 229 A C ATOM 1056 OG1 THR A 144 23.265 47.765 9.635 1.00 32.92 A O ANISOU 1056 OG1 THR A 144 6127 3364 3017 -1390 25 98 A O ATOM 1057 N PHE A 145 25.640 49.300 11.945 1.00 32.93 A N ANISOU 1057 N PHE A 145 6015 3385 3110 -1890 -182 192 A N ATOM 1058 CA PHE A 145 25.730 49.152 13.395 1.00 32.94 A C ANISOU 1058 CA PHE A 145 6025 3335 3155 -1904 -326 158 A C ATOM 1059 C PHE A 145 24.625 48.221 13.854 1.00 32.22 A C ANISOU 1059 C PHE A 145 5987 3177 3078 -1652 -341 79 A C ATOM 1060 O PHE A 145 24.902 47.268 14.574 1.00 33.26 A O ANISOU 1060 O PHE A 145 5978 3384 3276 -1570 -397 45 A O ATOM 1061 CB PHE A 145 25.640 50.527 14.119 1.00 33.30 A C ANISOU 1061 CB PHE A 145 6334 3187 3130 -2099 -426 183 A C ATOM 1062 CG PHE A 145 25.661 50.348 15.619 1.00 35.72 A C ANISOU 1062 CG PHE A 145 6687 3431 3453 -2101 -573 139 A C ATOM 1063 CD1 PHE A 145 26.858 50.177 16.296 1.00 37.48 A C ANISOU 1063 CD1 PHE A 145 6723 3784 3735 -2257 -681 166 A C ATOM 1064 CD2 PHE A 145 24.481 50.241 16.339 1.00 37.17 A C ANISOU 1064 CD2 PHE A 145 7077 3452 3593 -1933 -600 74 A C ATOM 1065 CE1 PHE A 145 26.873 49.938 17.671 1.00 38.53 A C ANISOU 1065 CE1 PHE A 145 6911 3865 3866 -2251 -829 127 A C ATOM 1066 CE2 PHE A 145 24.503 49.988 17.712 1.00 38.24 A C ANISOU 1066 CE2 PHE A 145 7263 3541 3726 -1926 -721 35 A C ATOM 1067 CZ PHE A 145 25.696 49.839 18.367 1.00 38.03 A C ANISOU 1067 CZ PHE A 145 7082 3627 3742 -2086 -841 60 A C ATOM 1068 N LEU A 146 23.382 48.441 13.366 1.00 30.61 A N ANISOU 1068 N LEU A 146 5972 2846 2813 -1529 -288 58 A N ATOM 1069 CA LEU A 146 22.211 47.617 13.693 1.00 30.44 A C ANISOU 1069 CA LEU A 146 5995 2767 2804 -1310 -292 -5 A C ATOM 1070 C LEU A 146 22.518 46.121 13.446 1.00 30.91 A C ANISOU 1070 C LEU A 146 5826 2981 2938 -1179 -261 -42 A C ATOM 1071 O LEU A 146 22.322 45.291 14.344 1.00 31.40 A O ANISOU 1071 O LEU A 146 5849 3037 3044 -1086 -319 -81 A O ATOM 1072 CB LEU A 146 20.993 48.088 12.861 1.00 29.79 A C ANISOU 1072 CB LEU A 146 6085 2580 2655 -1214 -232 -1 A C ATOM 1073 CG LEU A 146 19.625 47.375 13.011 1.00 30.68 A C ANISOU 1073 CG LEU A 146 6236 2643 2778 -1007 -230 -49 A C ATOM 1074 CD1 LEU A 146 18.550 48.153 12.303 1.00 30.62 A C ANISOU 1074 CD1 LEU A 146 6398 2532 2705 -943 -200 -24 A C ATOM 1075 CD2 LEU A 146 19.614 45.975 12.406 1.00 31.08 A C ANISOU 1075 CD2 LEU A 146 6109 2822 2877 -894 -191 -86 A C ATOM 1076 N HIS A 147 23.048 45.787 12.247 1.00 30.19 A N ANISOU 1076 N HIS A 147 5603 3018 2849 -1172 -164 -27 A N ATOM 1077 CA HIS A 147 23.311 44.386 11.915 1.00 29.70 A C ANISOU 1077 CA HIS A 147 5364 3078 2842 -1025 -122 -71 A C ATOM 1078 C HIS A 147 24.404 43.746 12.793 1.00 30.82 A C ANISOU 1078 C HIS A 147 5310 3326 3073 -1034 -185 -70 A C ATOM 1079 O HIS A 147 24.187 42.653 13.338 1.00 31.20 A O ANISOU 1079 O HIS A 147 5316 3371 3169 -893 -227 -115 A O ATOM 1080 CB HIS A 147 23.679 44.248 10.417 1.00 28.10 A C ANISOU 1080 CB HIS A 147 5092 2986 2599 -1009 11 -60 A C ATOM 1081 CG HIS A 147 23.983 42.837 10.004 1.00 25.76 A C ANISOU 1081 CG HIS A 147 4648 2797 2344 -844 67 -115 A C ATOM 1082 CD2 HIS A 147 25.164 42.177 9.993 1.00 26.21 A C ANISOU 1082 CD2 HIS A 147 4486 3010 2465 -811 109 -114 A C ATOM 1083 ND1 HIS A 147 22.972 41.954 9.621 1.00 27.52 A N ANISOU 1083 ND1 HIS A 147 4961 2954 2542 -686 73 -178 A N ATOM 1084 CE1 HIS A 147 23.565 40.785 9.395 1.00 27.47 A C ANISOU 1084 CE1 HIS A 147 4823 3040 2576 -562 118 -222 A C ATOM 1085 NE2 HIS A 147 24.885 40.866 9.585 1.00 27.63 A N ANISOU 1085 NE2 HIS A 147 4648 3199 2651 -612 149 -186 A N ATOM 1086 N VAL A 148 25.594 44.374 12.868 1.00 31.39 A N ANISOU 1086 N VAL A 148 5256 3504 3169 -1202 -195 -12 A N ATOM 1087 CA VAL A 148 26.742 43.815 13.583 1.00 32.58 A C ANISOU 1087 CA VAL A 148 5179 3791 3410 -1214 -265 5 A C ATOM 1088 C VAL A 148 26.482 43.766 15.092 1.00 33.04 A C ANISOU 1088 C VAL A 148 5328 3744 3482 -1225 -428 -10 A C ATOM 1089 O VAL A 148 26.798 42.763 15.724 1.00 33.26 A O ANISOU 1089 O VAL A 148 5242 3823 3572 -1109 -493 -28 A O ATOM 1090 CB VAL A 148 28.052 44.566 13.254 1.00 33.53 A C ANISOU 1090 CB VAL A 148 5117 4069 3555 -1419 -239 84 A C ATOM 1091 CG1 VAL A 148 29.234 43.960 14.010 1.00 34.07 A C ANISOU 1091 CG1 VAL A 148 4913 4303 3730 -1418 -330 110 A C ATOM 1092 CG2 VAL A 148 28.308 44.542 11.752 1.00 33.63 A C ANISOU 1092 CG2 VAL A 148 5047 4195 3536 -1397 -52 100 A C ATOM 1093 N PHE A 149 25.868 44.816 15.651 1.00 32.30 A N ANISOU 1093 N PHE A 149 5463 3491 3318 -1344 -489 -4 A N ATOM 1094 CA PHE A 149 25.503 44.838 17.055 1.00 32.21 A C ANISOU 1094 CA PHE A 149 5587 3363 3287 -1349 -623 -25 A C ATOM 1095 C PHE A 149 24.515 43.694 17.401 1.00 31.19 A C ANISOU 1095 C PHE A 149 5514 3170 3166 -1129 -613 -82 A C ATOM 1096 O PHE A 149 24.730 42.959 18.366 1.00 30.78 A O ANISOU 1096 O PHE A 149 5424 3128 3143 -1072 -707 -90 A O ATOM 1097 CB PHE A 149 24.887 46.187 17.393 1.00 33.09 A C ANISOU 1097 CB PHE A 149 5971 3297 3303 -1480 -650 -20 A C ATOM 1098 CG PHE A 149 24.400 46.328 18.809 1.00 35.39 A C ANISOU 1098 CG PHE A 149 6453 3452 3543 -1478 -762 -50 A C ATOM 1099 CD1 PHE A 149 25.297 46.437 19.859 1.00 37.27 A C ANISOU 1099 CD1 PHE A 149 6658 3720 3782 -1608 -913 -32 A C ATOM 1100 CD2 PHE A 149 23.047 46.384 19.090 1.00 36.90 A C ANISOU 1100 CD2 PHE A 149 6855 3491 3674 -1350 -717 -93 A C ATOM 1101 CE1 PHE A 149 24.848 46.589 21.168 1.00 38.63 A C ANISOU 1101 CE1 PHE A 149 7040 3759 3878 -1608 -1012 -62 A C ATOM 1102 CE2 PHE A 149 22.599 46.520 20.398 1.00 38.59 A C ANISOU 1102 CE2 PHE A 149 7253 3585 3823 -1340 -794 -120 A C ATOM 1103 CZ PHE A 149 23.502 46.630 21.428 1.00 38.84 A C ANISOU 1103 CZ PHE A 149 7286 3634 3838 -1470 -939 -109 A C ATOM 1104 N HIS A 150 23.453 43.537 16.610 1.00 30.12 A N ANISOU 1104 N HIS A 150 5469 2972 3002 -1019 -509 -112 A N ATOM 1105 CA HIS A 150 22.458 42.503 16.840 1.00 30.52 A C ANISOU 1105 CA HIS A 150 5570 2964 3062 -846 -496 -157 A C ATOM 1106 C HIS A 150 23.101 41.110 16.742 1.00 29.61 A C ANISOU 1106 C HIS A 150 5273 2956 3022 -727 -503 -172 A C ATOM 1107 O HIS A 150 22.950 40.303 17.653 1.00 27.49 A O ANISOU 1107 O HIS A 150 5023 2651 2773 -652 -573 -184 A O ATOM 1108 CB HIS A 150 21.292 42.642 15.819 1.00 32.23 A C ANISOU 1108 CB HIS A 150 5883 3122 3240 -775 -397 -176 A C ATOM 1109 CG HIS A 150 20.263 41.555 15.889 1.00 35.77 A C ANISOU 1109 CG HIS A 150 6360 3528 3703 -627 -383 -215 A C ATOM 1110 CD2 HIS A 150 18.973 41.615 16.296 1.00 37.56 A C ANISOU 1110 CD2 HIS A 150 6716 3654 3902 -577 -379 -226 A C ATOM 1111 ND1 HIS A 150 20.537 40.257 15.453 1.00 37.61 A N ANISOU 1111 ND1 HIS A 150 6479 3826 3985 -523 -366 -244 A N ATOM 1112 CE1 HIS A 150 19.419 39.570 15.639 1.00 38.33 A C ANISOU 1112 CE1 HIS A 150 6646 3843 4073 -441 -367 -268 A C ATOM 1113 NE2 HIS A 150 18.442 40.341 16.129 1.00 38.94 A N ANISOU 1113 NE2 HIS A 150 6849 3835 4110 -471 -370 -254 A N ATOM 1114 N HIS A 151 23.853 40.858 15.644 1.00 30.49 A N ANISOU 1114 N HIS A 151 5224 3195 3167 -704 -424 -167 A N ATOM 1115 CA HIS A 151 24.489 39.562 15.397 1.00 30.77 A C ANISOU 1115 CA HIS A 151 5098 3326 3268 -558 -407 -188 A C ATOM 1116 C HIS A 151 25.632 39.265 16.380 1.00 31.61 A C ANISOU 1116 C HIS A 151 5051 3519 3441 -570 -520 -152 A C ATOM 1117 O HIS A 151 26.046 38.124 16.451 1.00 31.34 A O ANISOU 1117 O HIS A 151 4915 3531 3463 -417 -533 -167 A O ATOM 1118 CB HIS A 151 24.987 39.446 13.947 1.00 30.46 A C ANISOU 1118 CB HIS A 151 4942 3404 3229 -519 -270 -197 A C ATOM 1119 CG HIS A 151 23.941 38.966 12.985 1.00 30.75 A C ANISOU 1119 CG HIS A 151 5106 3366 3212 -417 -185 -251 A C ATOM 1120 CD2 HIS A 151 24.068 38.195 11.883 1.00 30.87 A C ANISOU 1120 CD2 HIS A 151 5082 3433 3212 -297 -84 -294 A C ATOM 1121 ND1 HIS A 151 22.600 39.274 13.159 1.00 32.29 A N ANISOU 1121 ND1 HIS A 151 5490 3421 3357 -436 -213 -265 A N ATOM 1122 CE1 HIS A 151 21.963 38.712 12.142 1.00 31.86 A C ANISOU 1122 CE1 HIS A 151 5494 3347 3266 -349 -146 -308 A C ATOM 1123 NE2 HIS A 151 22.801 38.045 11.353 1.00 31.45 A N ANISOU 1123 NE2 HIS A 151 5330 3396 3223 -266 -69 -333 A N ATOM 1124 N THR A 152 26.138 40.263 17.130 1.00 32.24 A N ANISOU 1124 N THR A 152 5126 3613 3510 -746 -614 -104 A N ATOM 1125 CA THR A 152 27.186 40.023 18.116 1.00 33.80 A C ANISOU 1125 CA THR A 152 5182 3898 3764 -774 -754 -63 A C ATOM 1126 C THR A 152 26.567 39.780 19.499 1.00 35.04 A C ANISOU 1126 C THR A 152 5524 3915 3877 -758 -886 -73 A C ATOM 1127 O THR A 152 26.853 38.765 20.123 1.00 35.60 A O ANISOU 1127 O THR A 152 5541 4000 3986 -636 -967 -68 A O ATOM 1128 CB THR A 152 28.195 41.190 18.176 1.00 35.32 A C ANISOU 1128 CB THR A 152 5258 4197 3964 -1002 -806 -1 A C ATOM 1129 CG2 THR A 152 29.312 40.944 19.186 1.00 35.59 A C ANISOU 1129 CG2 THR A 152 5120 4343 4059 -1044 -979 50 A C ATOM 1130 OG1 THR A 152 28.748 41.404 16.881 1.00 36.57 A O ANISOU 1130 OG1 THR A 152 5248 4493 4152 -1024 -661 17 A O ATOM 1131 N ILE A 153 25.681 40.671 19.945 1.00 35.18 A N ANISOU 1131 N ILE A 153 5772 3789 3805 -863 -895 -86 A N ATOM 1132 CA ILE A 153 25.088 40.641 21.278 1.00 35.29 A C ANISOU 1132 CA ILE A 153 5984 3674 3752 -870 -997 -93 A C ATOM 1133 C ILE A 153 24.017 39.541 21.442 1.00 33.88 A C ANISOU 1133 C ILE A 153 5908 3400 3564 -696 -947 -128 A C ATOM 1134 O ILE A 153 23.790 39.124 22.581 1.00 34.30 A O ANISOU 1134 O ILE A 153 6072 3385 3577 -672 -1035 -120 A O ATOM 1135 CB ILE A 153 24.536 42.057 21.641 1.00 36.30 A C ANISOU 1135 CB ILE A 153 6332 3680 3779 -1028 -1001 -100 A C ATOM 1136 CG1 ILE A 153 24.719 42.348 23.115 1.00 39.65 A C ANISOU 1136 CG1 ILE A 153 6902 4036 4128 -1115 -1154 -90 A C ATOM 1137 CG2 ILE A 153 23.091 42.270 21.211 1.00 35.87 A C ANISOU 1137 CG2 ILE A 153 6453 3502 3675 -952 -869 -139 A C ATOM 1138 CD1 ILE A 153 26.203 42.433 23.594 1.00 42.61 A C ANISOU 1138 CD1 ILE A 153 7107 4541 4543 -1241 -1324 -39 A C ATOM 1139 N MET A 154 23.360 39.089 20.360 1.00 32.24 A N ANISOU 1139 N MET A 154 5681 3186 3382 -596 -817 -160 A N ATOM 1140 CA MET A 154 22.359 38.030 20.501 1.00 32.41 A C ANISOU 1140 CA MET A 154 5796 3119 3400 -465 -783 -186 A C ATOM 1141 C MET A 154 23.036 36.701 20.913 1.00 31.86 A C ANISOU 1141 C MET A 154 5639 3081 3386 -345 -860 -174 A C ATOM 1142 O MET A 154 22.723 36.220 22.003 1.00 30.82 A O ANISOU 1142 O MET A 154 5623 2870 3219 -324 -935 -157 A O ATOM 1143 CB MET A 154 21.461 37.871 19.267 1.00 33.05 A C ANISOU 1143 CB MET A 154 5892 3180 3486 -408 -653 -223 A C ATOM 1144 CG MET A 154 20.418 38.977 19.165 1.00 36.20 A C ANISOU 1144 CG MET A 154 6428 3506 3821 -482 -596 -227 A C ATOM 1145 SD MET A 154 19.138 38.907 20.446 1.00 38.94 A S ANISOU 1145 SD MET A 154 6965 3724 4105 -470 -608 -223 A S ATOM 1146 CE MET A 154 18.500 37.194 20.151 1.00 29.14 A C ANISOU 1146 CE MET A 154 5696 2462 2913 -347 -585 -239 A C ATOM 1147 N PRO A 155 24.017 36.142 20.153 1.00 32.45 A N ANISOU 1147 N PRO A 155 5523 3269 3537 -259 -845 -175 A N ATOM 1148 CA PRO A 155 24.676 34.907 20.630 1.00 32.56 A C ANISOU 1148 CA PRO A 155 5470 3298 3604 -116 -928 -159 A C ATOM 1149 C PRO A 155 25.447 35.147 21.919 1.00 32.78 A C ANISOU 1149 C PRO A 155 5474 3358 3623 -177 -1096 -101 A C ATOM 1150 O PRO A 155 25.339 34.330 22.825 1.00 32.42 A O ANISOU 1150 O PRO A 155 5521 3236 3560 -103 -1189 -79 A O ATOM 1151 CB PRO A 155 25.633 34.522 19.489 1.00 33.10 A C ANISOU 1151 CB PRO A 155 5323 3503 3751 -9 -855 -173 A C ATOM 1152 CG PRO A 155 25.827 35.797 18.701 1.00 33.47 A C ANISOU 1152 CG PRO A 155 5290 3643 3783 -156 -771 -171 A C ATOM 1153 CD PRO A 155 24.527 36.548 18.823 1.00 31.88 A C ANISOU 1153 CD PRO A 155 5303 3312 3500 -268 -738 -190 A C ATOM 1154 N TRP A 156 26.162 36.295 22.055 1.00 32.99 A N ANISOU 1154 N TRP A 156 5407 3483 3646 -334 -1146 -72 A N ATOM 1155 CA TRP A 156 26.973 36.527 23.256 1.00 33.83 A C ANISOU 1155 CA TRP A 156 5486 3630 3737 -411 -1334 -16 A C ATOM 1156 C TRP A 156 26.148 36.441 24.550 1.00 33.45 A C ANISOU 1156 C TRP A 156 5706 3423 3580 -441 -1417 -12 A C ATOM 1157 O TRP A 156 26.549 35.763 25.513 1.00 33.67 A O ANISOU 1157 O TRP A 156 5757 3439 3595 -382 -1560 29 A O ATOM 1158 CB TRP A 156 27.742 37.864 23.211 1.00 34.34 A C ANISOU 1158 CB TRP A 156 5448 3800 3799 -622 -1383 12 A C ATOM 1159 CG TRP A 156 28.838 37.903 24.244 1.00 35.53 A C ANISOU 1159 CG TRP A 156 5496 4041 3962 -689 -1598 75 A C ATOM 1160 CD1 TRP A 156 30.060 37.301 24.159 1.00 36.52 A C ANISOU 1160 CD1 TRP A 156 5337 4342 4196 -603 -1683 127 A C ATOM 1161 CD2 TRP A 156 28.739 38.421 25.579 1.00 36.01 A C ANISOU 1161 CD2 TRP A 156 5752 4015 3914 -824 -1765 94 A C ATOM 1162 CE2 TRP A 156 29.960 38.143 26.231 1.00 36.95 A C ANISOU 1162 CE2 TRP A 156 5689 4269 4081 -837 -1969 162 A C ATOM 1163 CE3 TRP A 156 27.743 39.105 26.285 1.00 36.74 A C ANISOU 1163 CE3 TRP A 156 6160 3933 3866 -926 -1759 59 A C ATOM 1164 NE1 TRP A 156 30.747 37.454 25.344 1.00 36.94 A N ANISOU 1164 NE1 TRP A 156 5379 4434 4223 -692 -1912 185 A N ATOM 1165 CZ2 TRP A 156 30.213 38.539 27.550 1.00 38.13 A C ANISOU 1165 CZ2 TRP A 156 5981 4377 4131 -971 -2184 194 A C ATOM 1166 CZ3 TRP A 156 28.011 39.527 27.576 1.00 37.87 A C ANISOU 1166 CZ3 TRP A 156 6454 4030 3904 -1051 -1947 83 A C ATOM 1167 CH2 TRP A 156 29.220 39.216 28.206 1.00 38.27 A C ANISOU 1167 CH2 TRP A 156 6341 4209 3994 -1078 -2165 149 A C ATOM 1168 N THR A 157 24.972 37.069 24.535 1.00 32.53 A N ANISOU 1168 N THR A 157 5790 3189 3382 -511 -1316 -50 A N ATOM 1169 CA THR A 157 24.114 37.105 25.713 1.00 32.27 A C ANISOU 1169 CA THR A 157 6012 3017 3233 -542 -1353 -48 A C ATOM 1170 C THR A 157 23.346 35.801 25.900 1.00 31.37 A C ANISOU 1170 C THR A 157 5986 2813 3118 -397 -1310 -48 A C ATOM 1171 O THR A 157 23.103 35.397 27.032 1.00 30.95 A O ANISOU 1171 O THR A 157 6092 2682 2986 -391 -1387 -18 A O ATOM 1172 CB THR A 157 23.152 38.296 25.664 1.00 32.70 A C ANISOU 1172 CB THR A 157 6236 2987 3202 -650 -1251 -85 A C ATOM 1173 CG2 THR A 157 22.450 38.510 27.004 1.00 32.52 A C ANISOU 1173 CG2 THR A 157 6475 2841 3040 -689 -1287 -82 A C ATOM 1174 OG1 THR A 157 23.878 39.484 25.302 1.00 33.47 A O ANISOU 1174 OG1 THR A 157 6263 3150 3306 -793 -1282 -84 A O ATOM 1175 N TRP A 158 22.949 35.153 24.798 1.00 31.52 A N ANISOU 1175 N TRP A 158 5928 2836 3213 -296 -1191 -78 A N ATOM 1176 CA TRP A 158 22.227 33.880 24.876 1.00 31.87 A C ANISOU 1176 CA TRP A 158 6065 2783 3261 -182 -1156 -78 A C ATOM 1177 C TRP A 158 23.065 32.759 25.479 1.00 31.85 A C ANISOU 1177 C TRP A 158 6037 2776 3287 -68 -1290 -32 A C ATOM 1178 O TRP A 158 22.490 31.785 25.957 1.00 32.68 A O ANISOU 1178 O TRP A 158 6286 2768 3363 -8 -1298 -13 A O ATOM 1179 CB TRP A 158 21.664 33.462 23.528 1.00 32.08 A C ANISOU 1179 CB TRP A 158 6033 2806 3351 -117 -1021 -126 A C ATOM 1180 CG TRP A 158 20.187 33.654 23.490 1.00 32.71 A C ANISOU 1180 CG TRP A 158 6252 2798 3378 -171 -915 -144 A C ATOM 1181 CD1 TRP A 158 19.506 34.771 23.093 1.00 33.43 A C ANISOU 1181 CD1 TRP A 158 6359 2903 3439 -254 -826 -166 A C ATOM 1182 CD2 TRP A 158 19.222 32.776 24.063 1.00 33.56 A C ANISOU 1182 CD2 TRP A 158 6506 2795 3449 -155 -898 -124 A C ATOM 1183 CE2 TRP A 158 17.961 33.379 23.908 1.00 34.09 A C ANISOU 1183 CE2 TRP A 158 6635 2838 3480 -225 -788 -137 A C ATOM 1184 CE3 TRP A 158 19.294 31.487 24.621 1.00 35.40 A C ANISOU 1184 CE3 TRP A 158 6822 2945 3683 -85 -963 -91 A C ATOM 1185 NE1 TRP A 158 18.160 34.598 23.305 1.00 33.83 A N ANISOU 1185 NE1 TRP A 158 6526 2877 3452 -269 -749 -165 A N ATOM 1186 CZ2 TRP A 158 16.788 32.756 24.326 1.00 35.66 A C ANISOU 1186 CZ2 TRP A 158 6946 2957 3648 -244 -734 -114 A C ATOM 1187 CZ3 TRP A 158 18.134 30.875 25.035 1.00 36.87 A C ANISOU 1187 CZ3 TRP A 158 7152 3029 3827 -120 -912 -68 A C ATOM 1188 CH2 TRP A 158 16.897 31.491 24.858 1.00 36.95 A C ANISOU 1188 CH2 TRP A 158 7190 3041 3809 -204 -794 -79 A C ATOM 1189 N TRP A 159 24.402 32.915 25.574 1.00 31.49 A N ANISOU 1189 N TRP A 159 5820 2851 3293 -47 -1408 -4 A N ATOM 1190 CA TRP A 159 25.241 31.924 26.262 1.00 31.74 A C ANISOU 1190 CA TRP A 159 5823 2886 3350 78 -1562 52 A C ATOM 1191 C TRP A 159 24.812 31.838 27.736 1.00 31.85 A C ANISOU 1191 C TRP A 159 6074 2789 3237 14 -1671 102 A C ATOM 1192 O TRP A 159 24.678 30.743 28.277 1.00 32.17 A O ANISOU 1192 O TRP A 159 6234 2732 3257 118 -1729 141 A O ATOM 1193 CB TRP A 159 26.738 32.304 26.181 1.00 31.64 A C ANISOU 1193 CB TRP A 159 5549 3057 3416 86 -1680 87 A C ATOM 1194 CG TRP A 159 27.649 31.315 26.854 1.00 31.83 A C ANISOU 1194 CG TRP A 159 5514 3103 3477 240 -1852 153 A C ATOM 1195 CD1 TRP A 159 28.214 30.206 26.289 1.00 32.52 A C ANISOU 1195 CD1 TRP A 159 5477 3215 3666 467 -1844 158 A C ATOM 1196 CD2 TRP A 159 28.016 31.289 28.249 1.00 31.92 A C ANISOU 1196 CD2 TRP A 159 5626 3092 3408 199 -2062 226 A C ATOM 1197 CE2 TRP A 159 28.818 30.147 28.449 1.00 32.81 A C ANISOU 1197 CE2 TRP A 159 5651 3225 3590 410 -2183 282 A C ATOM 1198 CE3 TRP A 159 27.748 32.124 29.346 1.00 32.20 A C ANISOU 1198 CE3 TRP A 159 5839 3087 3309 11 -2161 246 A C ATOM 1199 NE1 TRP A 159 28.959 29.526 27.232 1.00 33.06 A N ANISOU 1199 NE1 TRP A 159 5537 3287 3737 579 -2041 237 A N ATOM 1200 CZ2 TRP A 159 29.310 29.798 29.706 1.00 33.25 A C ANISOU 1200 CZ2 TRP A 159 5789 3261 3585 434 -2410 366 A C ATOM 1201 CZ3 TRP A 159 28.256 31.786 30.582 1.00 33.20 A C ANISOU 1201 CZ3 TRP A 159 6053 3197 3363 23 -2381 322 A C ATOM 1202 CH2 TRP A 159 29.051 30.656 30.749 1.00 33.58 A C ANISOU 1202 CH2 TRP A 159 6000 3275 3486 227 -2512 386 A C ATOM 1203 N PHE A 160 24.550 33.007 28.364 1.00 30.65 A N ANISOU 1203 N PHE A 160 6020 2639 2987 -157 -1689 98 A N ATOM 1204 CA PHE A 160 24.136 33.088 29.767 1.00 30.03 A C ANISOU 1204 CA PHE A 160 6190 2462 2758 -229 -1774 136 A C ATOM 1205 C PHE A 160 22.727 32.511 29.955 1.00 29.85 A C ANISOU 1205 C PHE A 160 6378 2294 2669 -210 -1631 129 A C ATOM 1206 O PHE A 160 22.492 31.869 30.967 1.00 30.91 A O ANISOU 1206 O PHE A 160 6696 2338 2710 -193 -1696 182 A O ATOM 1207 CB PHE A 160 24.211 34.530 30.285 1.00 29.82 A C ANISOU 1207 CB PHE A 160 6236 2461 2634 -408 -1811 118 A C ATOM 1208 CG PHE A 160 25.605 35.106 30.213 1.00 30.48 A C ANISOU 1208 CG PHE A 160 6115 2690 2776 -472 -1974 139 A C ATOM 1209 CD1 PHE A 160 26.496 34.947 31.268 1.00 31.24 A C ANISOU 1209 CD1 PHE A 160 6231 2821 2819 -495 -2206 202 A C ATOM 1210 CD2 PHE A 160 26.057 35.730 29.057 1.00 31.01 A C ANISOU 1210 CD2 PHE A 160 5955 2872 2956 -510 -1901 107 A C ATOM 1211 CE1 PHE A 160 27.795 35.447 31.187 1.00 32.17 A C ANISOU 1211 CE1 PHE A 160 6121 3096 3004 -569 -2369 232 A C ATOM 1212 CE2 PHE A 160 27.362 36.201 28.966 1.00 32.29 A C ANISOU 1212 CE2 PHE A 160 5896 3188 3183 -584 -2042 140 A C ATOM 1213 CZ PHE A 160 28.214 36.091 30.045 1.00 32.27 A C ANISOU 1213 CZ PHE A 160 5896 3230 3136 -622 -2279 202 A C ATOM 1214 N GLY A 161 21.836 32.676 28.972 1.00 28.77 A N ANISOU 1214 N GLY A 161 6205 2144 2582 -214 -1449 75 A N ATOM 1215 CA GLY A 161 20.504 32.089 29.033 1.00 29.02 A C ANISOU 1215 CA GLY A 161 6385 2065 2574 -209 -1317 76 A C ATOM 1216 C GLY A 161 20.540 30.564 28.973 1.00 29.59 A C ANISOU 1216 C GLY A 161 6490 2059 2693 -94 -1353 112 A C ATOM 1217 O GLY A 161 19.854 29.901 29.754 1.00 29.83 A O ANISOU 1217 O GLY A 161 6708 1981 2643 -110 -1342 159 A O ATOM 1218 N VAL A 162 21.362 29.984 28.076 1.00 29.57 A N ANISOU 1218 N VAL A 162 6322 2102 2812 26 -1393 93 A N ATOM 1219 CA VAL A 162 21.479 28.516 28.020 1.00 30.32 A C ANISOU 1219 CA VAL A 162 6479 2095 2945 158 -1437 122 A C ATOM 1220 C VAL A 162 22.196 28.007 29.291 1.00 32.20 A C ANISOU 1220 C VAL A 162 6826 2291 3118 209 -1620 207 A C ATOM 1221 O VAL A 162 21.823 26.971 29.848 1.00 33.25 A O ANISOU 1221 O VAL A 162 7146 2284 3204 249 -1651 261 A O ATOM 1222 CB VAL A 162 22.202 28.012 26.747 1.00 30.26 A C ANISOU 1222 CB VAL A 162 6288 2140 3069 305 -1420 73 A C ATOM 1223 CG1 VAL A 162 22.277 26.466 26.734 1.00 30.95 A C ANISOU 1223 CG1 VAL A 162 6493 2084 3183 457 -1467 97 A C ATOM 1224 CG2 VAL A 162 21.539 28.553 25.482 1.00 29.81 A C ANISOU 1224 CG2 VAL A 162 6143 2129 3056 249 -1257 -6 A C ATOM 1225 N LYS A 163 23.217 28.753 29.763 1.00 32.38 A N ANISOU 1225 N LYS A 163 6740 2432 3130 193 -1751 227 A N ATOM 1226 CA LYS A 163 24.033 28.360 30.906 1.00 32.51 A C ANISOU 1226 CA LYS A 163 6830 2437 3087 244 -1958 311 A C ATOM 1227 C LYS A 163 23.268 28.392 32.232 1.00 32.95 A C ANISOU 1227 C LYS A 163 7177 2378 2963 132 -1981 365 A C ATOM 1228 O LYS A 163 23.491 27.531 33.082 1.00 33.15 A O ANISOU 1228 O LYS A 163 7358 2313 2924 198 -2108 445 A O ATOM 1229 CB LYS A 163 25.270 29.270 31.011 1.00 33.14 A C ANISOU 1229 CB LYS A 163 6698 2691 3201 214 -2100 317 A C ATOM 1230 CG LYS A 163 26.316 28.823 32.051 1.00 35.30 A C ANISOU 1230 CG LYS A 163 6984 2988 3439 288 -2354 410 A C ATOM 1231 CD LYS A 163 26.917 27.460 31.708 1.00 36.09 A C ANISOU 1231 CD LYS A 163 7013 3055 3647 534 -2418 449 A C ATOM 1232 CE LYS A 163 28.189 27.198 32.435 1.00 36.19 A C ANISOU 1232 CE LYS A 163 6923 3154 3674 636 -2676 538 A C ATOM 1233 NZ LYS A 163 28.643 25.824 32.165 1.00 37.92 A N1+ ANISOU 1233 NZ LYS A 163 7120 3305 3983 904 -2726 579 A N1+ ATOM 1234 N PHE A 164 22.346 29.341 32.397 1.00 32.76 A N ANISOU 1234 N PHE A 164 7242 2352 2853 -23 -1848 325 A N ATOM 1235 CA PHE A 164 21.644 29.519 33.667 1.00 33.47 A C ANISOU 1235 CA PHE A 164 7604 2356 2755 -126 -1842 370 A C ATOM 1236 C PHE A 164 20.132 29.292 33.644 1.00 33.28 A C ANISOU 1236 C PHE A 164 7727 2237 2679 -191 -1627 363 A C ATOM 1237 O PHE A 164 19.607 28.827 34.651 1.00 34.16 A O ANISOU 1237 O PHE A 164 8072 2253 2654 -229 -1623 429 A O ATOM 1238 CB PHE A 164 21.880 30.959 34.183 1.00 33.95 A C ANISOU 1238 CB PHE A 164 7687 2495 2719 -255 -1880 336 A C ATOM 1239 CG PHE A 164 23.317 31.219 34.567 1.00 35.69 A C ANISOU 1239 CG PHE A 164 7805 2807 2947 -244 -2126 366 A C ATOM 1240 CD1 PHE A 164 23.807 30.812 35.798 1.00 37.12 A C ANISOU 1240 CD1 PHE A 164 8159 2946 2999 -238 -2323 446 A C ATOM 1241 CD2 PHE A 164 24.193 31.824 33.677 1.00 36.71 A C ANISOU 1241 CD2 PHE A 164 7656 3076 3216 -243 -2168 324 A C ATOM 1242 CE1 PHE A 164 25.140 31.017 36.136 1.00 38.30 A C ANISOU 1242 CE1 PHE A 164 8186 3198 3166 -231 -2575 484 A C ATOM 1243 CE2 PHE A 164 25.525 32.020 34.014 1.00 37.78 A C ANISOU 1243 CE2 PHE A 164 7658 3322 3376 -245 -2400 364 A C ATOM 1244 CZ PHE A 164 25.984 31.635 35.246 1.00 38.10 A C ANISOU 1244 CZ PHE A 164 7855 3326 3294 -240 -2610 443 A C ATOM 1245 N ALA A 165 19.426 29.644 32.566 1.00 32.28 A N ANISOU 1245 N ALA A 165 7469 2147 2648 -213 -1455 294 A N ATOM 1246 CA ALA A 165 17.964 29.587 32.558 1.00 32.43 A C ANISOU 1246 CA ALA A 165 7587 2112 2625 -288 -1257 293 A C ATOM 1247 C ALA A 165 17.417 29.150 31.189 1.00 33.27 A C ANISOU 1247 C ALA A 165 7538 2223 2879 -259 -1145 247 A C ATOM 1248 O ALA A 165 16.702 29.895 30.523 1.00 33.50 A O ANISOU 1248 O ALA A 165 7473 2310 2944 -306 -1009 194 A O ATOM 1249 CB ALA A 165 17.410 30.971 32.935 1.00 32.78 A C ANISOU 1249 CB ALA A 165 7674 2210 2571 -380 -1151 253 A C ATOM 1250 N ALA A 166 17.749 27.918 30.764 1.00 33.09 A N ANISOU 1250 N ALA A 166 7511 2128 2935 -174 -1211 268 A N ATOM 1251 CA ALA A 166 17.324 27.408 29.464 1.00 32.38 A C ANISOU 1251 CA ALA A 166 7311 2024 2967 -147 -1129 218 A C ATOM 1252 C ALA A 166 15.869 26.908 29.503 1.00 31.79 A C ANISOU 1252 C ALA A 166 7340 1873 2864 -257 -995 247 A C ATOM 1253 O ALA A 166 15.610 25.724 29.398 1.00 32.15 A O ANISOU 1253 O ALA A 166 7487 1800 2930 -254 -1013 280 A O ATOM 1254 CB ALA A 166 18.263 26.307 29.013 1.00 31.95 A C ANISOU 1254 CB ALA A 166 7240 1905 2994 -1 -1248 219 A C ATOM 1255 N GLY A 167 14.929 27.836 29.632 1.00 31.08 A N ANISOU 1255 N GLY A 167 7222 1856 2733 -355 -860 236 A N ATOM 1256 CA GLY A 167 13.509 27.502 29.701 1.00 30.44 A C ANISOU 1256 CA GLY A 167 7188 1746 2631 -469 -719 273 A C ATOM 1257 C GLY A 167 12.681 28.609 30.321 1.00 29.85 A C ANISOU 1257 C GLY A 167 7115 1756 2471 -536 -581 282 A C ATOM 1258 O GLY A 167 13.213 29.657 30.702 1.00 29.28 A O ANISOU 1258 O GLY A 167 7042 1741 2343 -501 -601 250 A O ATOM 1259 N GLY A 168 11.379 28.383 30.429 1.00 29.15 A N ANISOU 1259 N GLY A 168 7031 1675 2370 -634 -438 325 A N ATOM 1260 CA GLY A 168 10.493 29.368 31.043 1.00 29.24 A C ANISOU 1260 CA GLY A 168 7041 1770 2298 -672 -278 338 A C ATOM 1261 C GLY A 168 10.205 30.613 30.224 1.00 29.29 A C ANISOU 1261 C GLY A 168 6872 1889 2367 -626 -205 262 A C ATOM 1262 O GLY A 168 10.407 30.636 29.006 1.00 29.74 A O ANISOU 1262 O GLY A 168 6782 1975 2545 -596 -253 207 A O ATOM 1263 N LEU A 169 9.788 31.678 30.907 1.00 28.62 A N ANISOU 1263 N LEU A 169 6832 1857 2186 -608 -91 257 A N ATOM 1264 CA LEU A 169 9.365 32.933 30.295 1.00 28.37 A C ANISOU 1264 CA LEU A 169 6675 1913 2192 -554 -3 198 A C ATOM 1265 C LEU A 169 10.482 33.648 29.505 1.00 28.69 A C ANISOU 1265 C LEU A 169 6655 1958 2290 -492 -130 119 A C ATOM 1266 O LEU A 169 10.192 34.454 28.628 1.00 29.70 A O ANISOU 1266 O LEU A 169 6659 2144 2483 -455 -87 74 A O ATOM 1267 CB LEU A 169 8.753 33.845 31.361 1.00 28.41 A C ANISOU 1267 CB LEU A 169 6797 1942 2057 -529 148 210 A C ATOM 1268 CG LEU A 169 9.620 34.317 32.521 1.00 29.13 A C ANISOU 1268 CG LEU A 169 7121 1964 1982 -513 84 195 A C ATOM 1269 CD1 LEU A 169 10.313 35.615 32.175 1.00 29.54 A C ANISOU 1269 CD1 LEU A 169 7176 2018 2030 -454 23 111 A C ATOM 1270 CD2 LEU A 169 8.768 34.572 33.744 1.00 29.08 A C ANISOU 1270 CD2 LEU A 169 7274 1962 1812 -516 261 237 A C ATOM 1271 N GLY A 170 11.738 33.331 29.789 1.00 28.19 A N ANISOU 1271 N GLY A 170 6668 1840 2203 -485 -287 110 A N ATOM 1272 CA GLY A 170 12.860 33.934 29.078 1.00 27.82 A C ANISOU 1272 CA GLY A 170 6541 1815 2213 -445 -402 49 A C ATOM 1273 C GLY A 170 12.986 33.479 27.637 1.00 27.33 A C ANISOU 1273 C GLY A 170 6302 1786 2297 -423 -432 18 A C ATOM 1274 O GLY A 170 13.691 34.112 26.852 1.00 28.63 A O ANISOU 1274 O GLY A 170 6372 1992 2512 -395 -480 -31 A O ATOM 1275 N THR A 171 12.325 32.375 27.272 1.00 25.97 A N ANISOU 1275 N THR A 171 6098 1590 2181 -446 -405 47 A N ATOM 1276 CA THR A 171 12.411 31.843 25.923 1.00 25.42 A C ANISOU 1276 CA THR A 171 5899 1533 2225 -428 -439 11 A C ATOM 1277 C THR A 171 11.262 32.298 25.020 1.00 25.72 A C ANISOU 1277 C THR A 171 5817 1638 2316 -452 -337 -5 A C ATOM 1278 O THR A 171 11.245 31.899 23.865 1.00 25.30 A O ANISOU 1278 O THR A 171 5677 1597 2340 -447 -367 -38 A O ATOM 1279 CB THR A 171 12.466 30.299 25.977 1.00 25.53 A C ANISOU 1279 CB THR A 171 5982 1455 2265 -444 -501 44 A C ATOM 1280 CG2 THR A 171 13.564 29.807 26.864 1.00 24.98 A C ANISOU 1280 CG2 THR A 171 6029 1317 2145 -398 -615 71 A C ATOM 1281 OG1 THR A 171 11.204 29.762 26.399 1.00 26.84 A O ANISOU 1281 OG1 THR A 171 6194 1596 2409 -537 -413 104 A O ATOM 1282 N PHE A 172 10.325 33.146 25.501 1.00 26.71 A N ANISOU 1282 N PHE A 172 5940 1813 2397 -464 -221 18 A N ATOM 1283 CA PHE A 172 9.197 33.579 24.666 1.00 27.33 A C ANISOU 1283 CA PHE A 172 5883 1968 2532 -468 -136 16 A C ATOM 1284 C PHE A 172 9.671 34.334 23.440 1.00 26.89 A C ANISOU 1284 C PHE A 172 5736 1952 2527 -416 -180 -44 A C ATOM 1285 O PHE A 172 9.154 34.108 22.344 1.00 26.63 A O ANISOU 1285 O PHE A 172 5598 1959 2562 -429 -188 -55 A O ATOM 1286 CB PHE A 172 8.193 34.419 25.451 1.00 27.18 A C ANISOU 1286 CB PHE A 172 5874 2000 2455 -450 7 51 A C ATOM 1287 CG PHE A 172 7.100 35.054 24.614 1.00 28.69 A C ANISOU 1287 CG PHE A 172 5907 2286 2710 -419 84 55 A C ATOM 1288 CD1 PHE A 172 5.972 34.340 24.261 1.00 30.04 A C ANISOU 1288 CD1 PHE A 172 5949 2518 2946 -486 122 105 A C ATOM 1289 CD2 PHE A 172 7.201 36.375 24.187 1.00 29.10 A C ANISOU 1289 CD2 PHE A 172 5941 2363 2753 -329 105 17 A C ATOM 1290 CE1 PHE A 172 4.972 34.928 23.484 1.00 30.05 A C ANISOU 1290 CE1 PHE A 172 5785 2623 3011 -450 171 118 A C ATOM 1291 CE2 PHE A 172 6.197 36.954 23.429 1.00 29.62 A C ANISOU 1291 CE2 PHE A 172 5868 2512 2874 -279 162 30 A C ATOM 1292 CZ PHE A 172 5.091 36.228 23.086 1.00 29.67 A C ANISOU 1292 CZ PHE A 172 5726 2598 2952 -334 190 82 A C ATOM 1293 N HIS A 173 10.649 35.216 23.613 1.00 27.08 A N ANISOU 1293 N HIS A 173 5812 1966 2512 -374 -213 -78 A N ATOM 1294 CA HIS A 173 11.167 36.003 22.493 1.00 26.81 A C ANISOU 1294 CA HIS A 173 5706 1967 2512 -341 -244 -124 A C ATOM 1295 C HIS A 173 11.821 35.088 21.457 1.00 27.67 A C ANISOU 1295 C HIS A 173 5750 2076 2685 -344 -324 -154 A C ATOM 1296 O HIS A 173 11.801 35.440 20.292 1.00 28.69 A O ANISOU 1296 O HIS A 173 5806 2248 2848 -329 -325 -182 A O ATOM 1297 CB HIS A 173 12.150 37.093 22.963 1.00 26.03 A C ANISOU 1297 CB HIS A 173 5686 1850 2355 -331 -272 -145 A C ATOM 1298 CG HIS A 173 13.483 36.562 23.398 1.00 26.10 A C ANISOU 1298 CG HIS A 173 5727 1834 2355 -349 -379 -152 A C ATOM 1299 CD2 HIS A 173 14.608 36.372 22.674 1.00 26.84 A C ANISOU 1299 CD2 HIS A 173 5744 1957 2498 -342 -456 -178 A C ATOM 1300 ND1 HIS A 173 13.717 36.163 24.714 1.00 26.88 A N ANISOU 1300 ND1 HIS A 173 5941 1884 2387 -366 -413 -124 A N ATOM 1301 CE1 HIS A 173 14.971 35.754 24.738 1.00 27.75 A C ANISOU 1301 CE1 HIS A 173 6030 1997 2518 -364 -526 -130 A C ATOM 1302 NE2 HIS A 173 15.537 35.829 23.531 1.00 28.23 A N ANISOU 1302 NE2 HIS A 173 5963 2109 2653 -344 -546 -162 A N ATOM 1303 N ALA A 174 12.371 33.912 21.859 1.00 27.17 A N ANISOU 1303 N ALA A 174 5733 1961 2631 -351 -387 -148 A N ATOM 1304 CA ALA A 174 13.000 32.990 20.916 1.00 27.21 A C ANISOU 1304 CA ALA A 174 5702 1950 2687 -324 -450 -184 A C ATOM 1305 C ALA A 174 11.947 32.264 20.101 1.00 27.63 A C ANISOU 1305 C ALA A 174 5728 1993 2776 -363 -434 -188 A C ATOM 1306 O ALA A 174 12.116 32.094 18.897 1.00 28.14 A O ANISOU 1306 O ALA A 174 5750 2076 2867 -343 -455 -234 A O ATOM 1307 CB ALA A 174 13.883 32.001 21.647 1.00 27.26 A C ANISOU 1307 CB ALA A 174 5781 1888 2688 -294 -526 -171 A C ATOM 1308 N LEU A 175 10.833 31.872 20.735 1.00 27.27 A N ANISOU 1308 N LEU A 175 5708 1929 2725 -431 -396 -137 A N ATOM 1309 CA LEU A 175 9.682 31.270 20.063 1.00 27.09 A C ANISOU 1309 CA LEU A 175 5640 1914 2739 -505 -391 -126 A C ATOM 1310 C LEU A 175 9.149 32.234 18.974 1.00 28.23 A C ANISOU 1310 C LEU A 175 5669 2154 2902 -489 -368 -147 A C ATOM 1311 O LEU A 175 8.924 31.838 17.833 1.00 29.39 A O ANISOU 1311 O LEU A 175 5787 2307 3071 -511 -416 -180 A O ATOM 1312 CB LEU A 175 8.579 30.979 21.106 1.00 26.47 A C ANISOU 1312 CB LEU A 175 5572 1835 2648 -590 -327 -48 A C ATOM 1313 CG LEU A 175 7.195 30.644 20.547 1.00 27.19 A C ANISOU 1313 CG LEU A 175 5564 1980 2787 -690 -309 -14 A C ATOM 1314 CD1 LEU A 175 7.165 29.219 20.054 1.00 26.97 A C ANISOU 1314 CD1 LEU A 175 5610 1855 2783 -781 -398 -26 A C ATOM 1315 CD2 LEU A 175 6.098 30.915 21.562 1.00 27.57 A C ANISOU 1315 CD2 LEU A 175 5559 2093 2824 -742 -197 69 A C ATOM 1316 N LEU A 176 8.997 33.505 19.330 1.00 28.17 A N ANISOU 1316 N LEU A 176 5624 2207 2873 -443 -303 -131 A N ATOM 1317 CA LEU A 176 8.487 34.507 18.413 1.00 28.77 A C ANISOU 1317 CA LEU A 176 5614 2360 2960 -410 -284 -137 A C ATOM 1318 C LEU A 176 9.512 34.809 17.310 1.00 29.22 A C ANISOU 1318 C LEU A 176 5680 2416 3006 -368 -334 -196 A C ATOM 1319 O LEU A 176 9.146 34.814 16.133 1.00 31.08 A O ANISOU 1319 O LEU A 176 5870 2687 3250 -375 -366 -213 A O ATOM 1320 CB LEU A 176 8.110 35.766 19.206 1.00 29.05 A C ANISOU 1320 CB LEU A 176 5648 2426 2963 -354 -196 -105 A C ATOM 1321 CG LEU A 176 7.274 36.838 18.523 1.00 32.26 A C ANISOU 1321 CG LEU A 176 5973 2904 3382 -298 -162 -88 A C ATOM 1322 CD1 LEU A 176 6.060 36.240 17.752 1.00 34.24 A C ANISOU 1322 CD1 LEU A 176 6092 3228 3691 -345 -191 -55 A C ATOM 1323 CD2 LEU A 176 6.813 37.884 19.523 1.00 31.97 A C ANISOU 1323 CD2 LEU A 176 5968 2873 3307 -226 -58 -57 A C ATOM 1324 N ASN A 177 10.791 34.939 17.670 1.00 27.35 A N ANISOU 1324 N ASN A 177 5498 2145 2747 -337 -346 -222 A N ATOM 1325 CA ASN A 177 11.863 35.241 16.733 1.00 26.68 A C ANISOU 1325 CA ASN A 177 5404 2080 2653 -303 -370 -267 A C ATOM 1326 C ASN A 177 12.078 34.158 15.692 1.00 25.87 A C ANISOU 1326 C ASN A 177 5304 1963 2563 -299 -413 -313 A C ATOM 1327 O ASN A 177 12.311 34.491 14.529 1.00 25.23 A O ANISOU 1327 O ASN A 177 5203 1921 2461 -282 -411 -344 A O ATOM 1328 CB ASN A 177 13.162 35.514 17.468 1.00 27.99 A C ANISOU 1328 CB ASN A 177 5596 2233 2805 -284 -381 -273 A C ATOM 1329 CG ASN A 177 14.268 35.949 16.542 1.00 30.24 A C ANISOU 1329 CG ASN A 177 5841 2565 3085 -263 -385 -305 A C ATOM 1330 ND2 ASN A 177 13.966 36.922 15.670 1.00 29.29 A N ANISOU 1330 ND2 ASN A 177 5704 2483 2941 -272 -352 -303 A N ATOM 1331 OD1 ASN A 177 15.382 35.397 16.583 1.00 30.54 A O ANISOU 1331 OD1 ASN A 177 5855 2609 3139 -234 -412 -325 A O ATOM 1332 N THR A 178 12.002 32.861 16.079 1.00 25.48 A N ANISOU 1332 N THR A 178 5304 1844 2533 -315 -449 -319 A N ATOM 1333 CA THR A 178 12.150 31.800 15.095 1.00 26.42 A C ANISOU 1333 CA THR A 178 5468 1921 2651 -306 -491 -373 A C ATOM 1334 C THR A 178 10.964 31.855 14.107 1.00 27.00 A C ANISOU 1334 C THR A 178 5520 2026 2714 -370 -513 -375 A C ATOM 1335 O THR A 178 11.186 31.645 12.932 1.00 28.24 A O ANISOU 1335 O THR A 178 5706 2186 2837 -352 -534 -429 A O ATOM 1336 CB THR A 178 12.291 30.390 15.762 1.00 27.01 A C ANISOU 1336 CB THR A 178 5637 1883 2743 -310 -535 -374 A C ATOM 1337 CG2 THR A 178 13.567 30.254 16.579 1.00 27.02 A C ANISOU 1337 CG2 THR A 178 5655 1860 2751 -224 -541 -371 A C ATOM 1338 OG1 THR A 178 11.164 30.155 16.597 1.00 27.77 A O ANISOU 1338 OG1 THR A 178 5742 1954 2853 -406 -535 -312 A O ATOM 1339 N ALA A 179 9.739 32.186 14.564 1.00 26.30 A N ANISOU 1339 N ALA A 179 5373 1971 2648 -437 -505 -316 A N ATOM 1340 CA ALA A 179 8.597 32.288 13.659 1.00 26.39 A C ANISOU 1340 CA ALA A 179 5331 2035 2660 -497 -545 -304 A C ATOM 1341 C ALA A 179 8.757 33.493 12.683 1.00 27.04 A C ANISOU 1341 C ALA A 179 5375 2195 2705 -438 -533 -314 A C ATOM 1342 O ALA A 179 8.436 33.360 11.505 1.00 27.70 A O ANISOU 1342 O ALA A 179 5472 2299 2754 -459 -590 -340 A O ATOM 1343 CB ALA A 179 7.313 32.420 14.452 1.00 26.03 A C ANISOU 1343 CB ALA A 179 5195 2036 2660 -563 -524 -226 A C ATOM 1344 N VAL A 180 9.304 34.634 13.150 1.00 26.71 A N ANISOU 1344 N VAL A 180 5313 2181 2654 -373 -467 -294 A N ATOM 1345 CA VAL A 180 9.503 35.787 12.267 1.00 26.96 A C ANISOU 1345 CA VAL A 180 5337 2263 2642 -330 -454 -294 A C ATOM 1346 C VAL A 180 10.678 35.530 11.295 1.00 28.89 A C ANISOU 1346 C VAL A 180 5644 2499 2836 -307 -455 -356 A C ATOM 1347 O VAL A 180 10.604 35.937 10.131 1.00 29.12 A O ANISOU 1347 O VAL A 180 5693 2564 2809 -301 -470 -366 A O ATOM 1348 CB VAL A 180 9.715 37.094 13.077 1.00 25.52 A C ANISOU 1348 CB VAL A 180 5148 2088 2459 -285 -388 -253 A C ATOM 1349 CG1 VAL A 180 9.989 38.290 12.152 1.00 25.59 A C ANISOU 1349 CG1 VAL A 180 5182 2125 2417 -253 -378 -245 A C ATOM 1350 CG2 VAL A 180 8.524 37.365 13.978 1.00 24.67 A C ANISOU 1350 CG2 VAL A 180 4987 1998 2390 -279 -361 -197 A C ATOM 1351 N HIS A 181 11.757 34.864 11.765 1.00 29.99 A N ANISOU 1351 N HIS A 181 5809 2598 2987 -284 -434 -393 A N ATOM 1352 CA HIS A 181 12.928 34.568 10.924 1.00 31.83 A C ANISOU 1352 CA HIS A 181 6075 2840 3178 -239 -409 -450 A C ATOM 1353 C HIS A 181 12.509 33.603 9.740 1.00 31.69 A C ANISOU 1353 C HIS A 181 6135 2795 3111 -247 -456 -508 A C ATOM 1354 O HIS A 181 13.149 33.616 8.681 1.00 31.03 A O ANISOU 1354 O HIS A 181 6093 2737 2958 -209 -424 -553 A O ATOM 1355 CB HIS A 181 14.125 34.028 11.770 1.00 33.77 A C ANISOU 1355 CB HIS A 181 6308 3061 3463 -190 -387 -467 A C ATOM 1356 CG HIS A 181 15.245 35.015 12.163 1.00 37.54 A C ANISOU 1356 CG HIS A 181 6721 3598 3946 -177 -339 -441 A C ATOM 1357 CD2 HIS A 181 15.399 36.373 11.992 1.00 38.99 A C ANISOU 1357 CD2 HIS A 181 6879 3832 4104 -214 -305 -405 A C ATOM 1358 ND1 HIS A 181 16.382 34.531 12.804 1.00 39.71 A N ANISOU 1358 ND1 HIS A 181 6956 3874 4257 -129 -339 -450 A N ATOM 1359 CE1 HIS A 181 17.202 35.560 12.973 1.00 41.37 A C ANISOU 1359 CE1 HIS A 181 7101 4152 4466 -155 -309 -421 A C ATOM 1360 NE2 HIS A 181 16.700 36.696 12.494 1.00 41.42 A N ANISOU 1360 NE2 HIS A 181 7126 4180 4432 -213 -283 -395 A N ATOM 1361 N VAL A 182 11.362 32.881 9.864 1.00 31.58 A N ANISOU 1361 N VAL A 182 6144 2737 3118 -312 -531 -501 A N ATOM 1362 CA VAL A 182 10.835 32.088 8.750 1.00 31.71 A C ANISOU 1362 CA VAL A 182 6251 2722 3076 -352 -602 -552 A C ATOM 1363 C VAL A 182 10.408 33.039 7.587 1.00 31.55 A C ANISOU 1363 C VAL A 182 6224 2782 2981 -363 -621 -538 A C ATOM 1364 O VAL A 182 10.629 32.746 6.410 1.00 32.04 A O ANISOU 1364 O VAL A 182 6387 2839 2948 -353 -639 -595 A O ATOM 1365 CB VAL A 182 9.665 31.149 9.175 1.00 31.76 A C ANISOU 1365 CB VAL A 182 6270 2669 3128 -458 -692 -534 A C ATOM 1366 CG1 VAL A 182 9.009 30.485 7.958 1.00 31.46 A C ANISOU 1366 CG1 VAL A 182 6331 2603 3018 -532 -795 -582 A C ATOM 1367 CG2 VAL A 182 10.138 30.097 10.176 1.00 31.29 A C ANISOU 1367 CG2 VAL A 182 6267 2505 3117 -448 -682 -548 A C ATOM 1368 N VAL A 183 9.816 34.172 7.929 1.00 30.93 A N ANISOU 1368 N VAL A 183 6049 2769 2935 -370 -615 -461 A N ATOM 1369 CA VAL A 183 9.382 35.172 6.954 1.00 30.58 A C ANISOU 1369 CA VAL A 183 6003 2790 2825 -365 -640 -428 A C ATOM 1370 C VAL A 183 10.594 35.981 6.466 1.00 29.98 A C ANISOU 1370 C VAL A 183 5972 2738 2682 -307 -546 -439 A C ATOM 1371 O VAL A 183 10.749 36.225 5.266 1.00 30.58 A O ANISOU 1371 O VAL A 183 6126 2840 2654 -302 -553 -456 A O ATOM 1372 CB VAL A 183 8.299 36.123 7.554 1.00 30.40 A C ANISOU 1372 CB VAL A 183 5868 2817 2865 -364 -660 -336 A C ATOM 1373 CG1 VAL A 183 7.822 37.135 6.502 1.00 30.65 A C ANISOU 1373 CG1 VAL A 183 5915 2905 2827 -339 -706 -293 A C ATOM 1374 CG2 VAL A 183 7.119 35.333 8.102 1.00 30.73 A C ANISOU 1374 CG2 VAL A 183 5830 2864 2983 -434 -732 -310 A C ATOM 1375 N MET A 184 11.460 36.374 7.395 1.00 28.67 A N ANISOU 1375 N MET A 184 5760 2566 2569 -277 -462 -426 A N ATOM 1376 CA MET A 184 12.626 37.185 7.071 1.00 28.30 A C ANISOU 1376 CA MET A 184 5724 2553 2475 -253 -374 -422 A C ATOM 1377 C MET A 184 13.584 36.484 6.120 1.00 27.76 A C ANISOU 1377 C MET A 184 5715 2500 2332 -224 -323 -493 A C ATOM 1378 O MET A 184 13.924 37.073 5.099 1.00 28.25 A O ANISOU 1378 O MET A 184 5829 2607 2299 -226 -281 -486 A O ATOM 1379 CB MET A 184 13.359 37.621 8.334 1.00 28.35 A C ANISOU 1379 CB MET A 184 5664 2551 2557 -249 -321 -396 A C ATOM 1380 CG MET A 184 14.174 38.866 8.139 1.00 30.55 A C ANISOU 1380 CG MET A 184 5945 2865 2799 -269 -256 -357 A C ATOM 1381 SD MET A 184 15.531 39.025 9.339 1.00 32.16 A S ANISOU 1381 SD MET A 184 6072 3078 3069 -285 -206 -352 A S ATOM 1382 CE MET A 184 16.474 37.659 8.824 1.00 34.63 A C ANISOU 1382 CE MET A 184 6349 3429 3381 -225 -171 -424 A C ATOM 1383 N TYR A 185 13.990 35.240 6.402 1.00 26.98 A N ANISOU 1383 N TYR A 185 5627 2361 2265 -187 -321 -557 A N ATOM 1384 CA TYR A 185 14.898 34.522 5.505 1.00 26.81 A C ANISOU 1384 CA TYR A 185 5672 2348 2167 -125 -256 -633 A C ATOM 1385 C TYR A 185 14.209 34.010 4.255 1.00 26.43 A C ANISOU 1385 C TYR A 185 5766 2273 2002 -140 -312 -684 A C ATOM 1386 O TYR A 185 14.913 33.717 3.295 1.00 27.17 A O ANISOU 1386 O TYR A 185 5942 2387 1994 -86 -238 -743 A O ATOM 1387 CB TYR A 185 15.651 33.409 6.208 1.00 27.17 A C ANISOU 1387 CB TYR A 185 5697 2346 2279 -49 -234 -682 A C ATOM 1388 CG TYR A 185 16.691 33.970 7.150 1.00 28.15 A C ANISOU 1388 CG TYR A 185 5683 2528 2484 -26 -171 -637 A C ATOM 1389 CD1 TYR A 185 17.890 34.474 6.671 1.00 29.09 A C ANISOU 1389 CD1 TYR A 185 5734 2746 2572 9 -61 -633 A C ATOM 1390 CD2 TYR A 185 16.464 34.018 8.515 1.00 29.45 A C ANISOU 1390 CD2 TYR A 185 5787 2656 2747 -54 -225 -592 A C ATOM 1391 CE1 TYR A 185 18.829 35.037 7.527 1.00 30.43 A C ANISOU 1391 CE1 TYR A 185 5764 2980 2819 0 -27 -584 A C ATOM 1392 CE2 TYR A 185 17.429 34.501 9.388 1.00 30.65 A C ANISOU 1392 CE2 TYR A 185 5829 2857 2960 -45 -193 -553 A C ATOM 1393 CZ TYR A 185 18.599 35.039 8.886 1.00 31.74 A C ANISOU 1393 CZ TYR A 185 5886 3096 3076 -27 -104 -547 A C ATOM 1394 OH TYR A 185 19.546 35.553 9.731 1.00 34.29 A O ANISOU 1394 OH TYR A 185 6088 3479 3462 -46 -94 -502 A O ATOM 1395 N SER A 186 12.862 33.939 4.214 1.00 25.98 A N ANISOU 1395 N SER A 186 5737 2183 1951 -214 -438 -661 A N ATOM 1396 CA SER A 186 12.178 33.648 2.949 1.00 26.72 A C ANISOU 1396 CA SER A 186 5966 2267 1919 -251 -519 -698 A C ATOM 1397 C SER A 186 12.297 34.915 2.065 1.00 26.85 A C ANISOU 1397 C SER A 186 6000 2366 1834 -253 -480 -645 A C ATOM 1398 O SER A 186 12.581 34.791 0.885 1.00 27.51 A O ANISOU 1398 O SER A 186 6218 2463 1772 -239 -457 -690 A O ATOM 1399 CB SER A 186 10.728 33.247 3.164 1.00 28.86 A C ANISOU 1399 CB SER A 186 6227 2504 2234 -344 -677 -673 A C ATOM 1400 OG SER A 186 10.622 32.018 3.869 1.00 31.89 A O ANISOU 1400 OG SER A 186 6632 2796 2690 -365 -713 -718 A O ATOM 1401 N TYR A 187 12.203 36.129 2.659 1.00 27.09 A N ANISOU 1401 N TYR A 187 5921 2439 1931 -263 -458 -553 A N ATOM 1402 CA TYR A 187 12.421 37.384 1.923 1.00 27.92 A C ANISOU 1402 CA TYR A 187 6064 2599 1945 -268 -415 -491 A C ATOM 1403 C TYR A 187 13.852 37.416 1.378 1.00 29.09 A C ANISOU 1403 C TYR A 187 6252 2789 2014 -236 -259 -527 A C ATOM 1404 O TYR A 187 14.038 37.708 0.202 1.00 28.99 A O ANISOU 1404 O TYR A 187 6355 2810 1852 -241 -225 -529 A O ATOM 1405 CB TYR A 187 12.173 38.618 2.820 1.00 27.97 A C ANISOU 1405 CB TYR A 187 5972 2611 2043 -276 -410 -395 A C ATOM 1406 CG TYR A 187 12.657 39.913 2.201 1.00 28.01 A C ANISOU 1406 CG TYR A 187 6037 2644 1960 -288 -346 -330 A C ATOM 1407 CD1 TYR A 187 11.869 40.611 1.297 1.00 28.82 A C ANISOU 1407 CD1 TYR A 187 6233 2752 1966 -293 -424 -272 A C ATOM 1408 CD2 TYR A 187 13.928 40.407 2.475 1.00 28.50 A C ANISOU 1408 CD2 TYR A 187 6068 2731 2031 -306 -215 -318 A C ATOM 1409 CE1 TYR A 187 12.325 41.781 0.692 1.00 29.19 A C ANISOU 1409 CE1 TYR A 187 6368 2806 1917 -312 -366 -204 A C ATOM 1410 CE2 TYR A 187 14.400 41.565 1.867 1.00 29.26 A C ANISOU 1410 CE2 TYR A 187 6234 2846 2039 -347 -152 -251 A C ATOM 1411 CZ TYR A 187 13.600 42.243 0.966 1.00 30.22 A C ANISOU 1411 CZ TYR A 187 6477 2952 2054 -349 -223 -194 A C ATOM 1412 OH TYR A 187 14.063 43.393 0.375 1.00 32.56 A O ANISOU 1412 OH TYR A 187 6870 3247 2254 -397 -163 -118 A O ATOM 1413 N TYR A 188 14.862 37.134 2.251 1.00 30.18 A N ANISOU 1413 N TYR A 188 6283 2936 2248 -203 -164 -548 A N ATOM 1414 CA TYR A 188 16.277 37.103 1.876 1.00 31.25 A C ANISOU 1414 CA TYR A 188 6395 3138 2338 -164 -7 -574 A C ATOM 1415 C TYR A 188 16.533 36.053 0.775 1.00 33.36 A C ANISOU 1415 C TYR A 188 6795 3403 2477 -97 37 -673 A C ATOM 1416 O TYR A 188 17.280 36.336 -0.167 1.00 34.52 A O ANISOU 1416 O TYR A 188 6993 3620 2502 -81 162 -679 A O ATOM 1417 CB TYR A 188 17.164 36.821 3.096 1.00 30.56 A C ANISOU 1417 CB TYR A 188 6153 3064 2394 -131 43 -577 A C ATOM 1418 CG TYR A 188 17.600 38.049 3.881 1.00 30.79 A C ANISOU 1418 CG TYR A 188 6072 3132 2496 -201 70 -487 A C ATOM 1419 CD1 TYR A 188 17.976 39.220 3.234 1.00 31.39 A C ANISOU 1419 CD1 TYR A 188 6172 3262 2493 -271 139 -422 A C ATOM 1420 CD2 TYR A 188 17.768 37.991 5.255 1.00 31.52 A C ANISOU 1420 CD2 TYR A 188 6057 3199 2722 -205 32 -470 A C ATOM 1421 CE1 TYR A 188 18.436 40.324 3.945 1.00 32.31 A C ANISOU 1421 CE1 TYR A 188 6217 3393 2668 -354 156 -345 A C ATOM 1422 CE2 TYR A 188 18.240 39.077 5.973 1.00 32.61 A C ANISOU 1422 CE2 TYR A 188 6121 3359 2909 -279 47 -400 A C ATOM 1423 CZ TYR A 188 18.542 40.258 5.323 1.00 33.73 A C ANISOU 1423 CZ TYR A 188 6298 3541 2977 -360 104 -339 A C ATOM 1424 OH TYR A 188 19.029 41.319 6.064 1.00 34.77 A O ANISOU 1424 OH TYR A 188 6384 3673 3155 -453 107 -272 A O ATOM 1425 N GLY A 189 15.869 34.899 0.864 1.00 33.11 A N ANISOU 1425 N GLY A 189 6840 3283 2458 -70 -62 -746 A N ATOM 1426 CA GLY A 189 16.002 33.821 -0.116 1.00 33.87 A C ANISOU 1426 CA GLY A 189 7108 3338 2423 -7 -41 -855 A C ATOM 1427 C GLY A 189 15.458 34.214 -1.471 1.00 34.20 A C ANISOU 1427 C GLY A 189 7322 3397 2275 -55 -76 -856 A C ATOM 1428 O GLY A 189 16.092 33.966 -2.500 1.00 33.12 A O ANISOU 1428 O GLY A 189 7315 3288 1981 1 34 -915 A O ATOM 1429 N LEU A 190 14.296 34.891 -1.465 1.00 35.11 A N ANISOU 1429 N LEU A 190 7436 3504 2399 -150 -226 -781 A N ATOM 1430 CA LEU A 190 13.666 35.350 -2.701 1.00 36.54 A C ANISOU 1430 CA LEU A 190 7777 3704 2404 -200 -298 -762 A C ATOM 1431 C LEU A 190 14.484 36.465 -3.342 1.00 36.73 A C ANISOU 1431 C LEU A 190 7818 3816 2323 -196 -151 -698 A C ATOM 1432 O LEU A 190 14.593 36.505 -4.560 1.00 36.82 A O ANISOU 1432 O LEU A 190 8007 3848 2134 -197 -119 -721 A O ATOM 1433 CB LEU A 190 12.225 35.817 -2.450 1.00 37.31 A C ANISOU 1433 CB LEU A 190 7831 3786 2561 -280 -501 -683 A C ATOM 1434 CG LEU A 190 11.205 34.728 -2.085 1.00 39.19 A C ANISOU 1434 CG LEU A 190 8073 3952 2867 -327 -669 -732 A C ATOM 1435 CD1 LEU A 190 9.850 35.353 -1.775 1.00 40.17 A C ANISOU 1435 CD1 LEU A 190 8091 4103 3070 -394 -840 -632 A C ATOM 1436 CD2 LEU A 190 11.109 33.633 -3.186 1.00 39.13 A C ANISOU 1436 CD2 LEU A 190 8301 3883 2684 -342 -729 -847 A C ATOM 1437 N SER A 191 15.086 37.347 -2.516 1.00 36.69 A N ANISOU 1437 N SER A 191 7643 3857 2441 -206 -61 -618 A N ATOM 1438 CA ASER A 191 15.909 38.450 -3.011 0.50 37.09 A C ANISOU 1438 CA ASER A 191 7699 3985 2408 -236 81 -544 A C ATOM 1439 CA BSER A 191 15.926 38.449 -2.972 0.50 37.05 A C ANISOU 1439 CA BSER A 191 7688 3980 2409 -235 82 -543 A C ATOM 1440 C SER A 191 17.238 37.960 -3.583 1.00 37.74 A C ANISOU 1440 C SER A 191 7795 4142 2401 -177 290 -607 A C ATOM 1441 O SER A 191 17.774 38.604 -4.473 1.00 37.52 A O ANISOU 1441 O SER A 191 7846 4183 2227 -207 409 -565 A O ATOM 1442 CB ASER A 191 16.168 39.474 -1.908 0.50 37.56 A C ANISOU 1442 CB ASER A 191 7590 4055 2625 -283 100 -448 A C ATOM 1443 CB BSER A 191 16.232 39.386 -1.808 0.50 37.39 A C ANISOU 1443 CB BSER A 191 7553 4034 2618 -278 106 -455 A C ATOM 1444 OG ASER A 191 17.039 38.956 -0.919 0.50 38.93 A O ANISOU 1444 OG ASER A 191 7598 4252 2943 -246 182 -486 A O ATOM 1445 OG BSER A 191 16.935 40.521 -2.276 0.50 38.61 A O ANISOU 1445 OG BSER A 191 7729 4246 2694 -341 221 -370 A O ATOM 1446 N ALA A 192 17.771 36.835 -3.085 1.00 38.83 A N ANISOU 1446 N ALA A 192 7862 4270 2623 -84 342 -701 A N ATOM 1447 CA ALA A 192 19.025 36.262 -3.575 1.00 40.68 A C ANISOU 1447 CA ALA A 192 8088 4582 2788 14 549 -768 A C ATOM 1448 C ALA A 192 18.891 35.709 -5.002 1.00 43.52 A C ANISOU 1448 C ALA A 192 8704 4927 2903 61 592 -852 A C ATOM 1449 O ALA A 192 19.910 35.527 -5.672 1.00 44.17 A O ANISOU 1449 O ALA A 192 8810 5098 2877 137 800 -888 A O ATOM 1450 CB ALA A 192 19.500 35.159 -2.643 1.00 40.31 A C ANISOU 1450 CB ALA A 192 7920 4502 2894 127 563 -844 A C ATOM 1451 N LEU A 193 17.648 35.451 -5.481 1.00 44.99 A N ANISOU 1451 N LEU A 193 9083 5014 2997 14 400 -880 A N ATOM 1452 CA LEU A 193 17.395 34.944 -6.834 1.00 46.55 A C ANISOU 1452 CA LEU A 193 9563 5182 2942 37 399 -962 A C ATOM 1453 C LEU A 193 17.844 35.940 -7.921 1.00 49.11 A C ANISOU 1453 C LEU A 193 9988 5607 3063 -6 535 -891 A C ATOM 1454 O LEU A 193 18.124 35.518 -9.040 1.00 49.73 A O ANISOU 1454 O LEU A 193 10284 5697 2914 44 632 -965 A O ATOM 1455 CB LEU A 193 15.912 34.590 -7.019 1.00 46.51 A C ANISOU 1455 CB LEU A 193 9707 5064 2899 -40 126 -983 A C ATOM 1456 CG LEU A 193 15.382 33.455 -6.129 1.00 48.03 A C ANISOU 1456 CG LEU A 193 9857 5143 3250 -22 -9 -1060 A C ATOM 1457 CD1 LEU A 193 13.874 33.347 -6.212 1.00 48.22 A C ANISOU 1457 CD1 LEU A 193 9958 5095 3269 -139 -283 -1041 A C ATOM 1458 CD2 LEU A 193 16.011 32.130 -6.495 1.00 48.91 A C ANISOU 1458 CD2 LEU A 193 10127 5184 3272 101 89 -1212 A C ATOM 1459 N GLY A 194 17.928 37.234 -7.601 1.00 50.64 A N ANISOU 1459 N GLY A 194 10052 5864 3327 -100 549 -750 A N ATOM 1460 CA GLY A 194 18.394 38.226 -8.564 1.00 52.99 A C ANISOU 1460 CA GLY A 194 10448 6246 3438 -161 683 -664 A C ATOM 1461 C GLY A 194 17.574 39.490 -8.633 1.00 55.37 A C ANISOU 1461 C GLY A 194 10795 6519 3726 -280 533 -524 A C ATOM 1462 O GLY A 194 16.494 39.552 -8.054 1.00 55.43 A O ANISOU 1462 O GLY A 194 10767 6444 3849 -302 312 -503 A O ATOM 1463 N PRO A 195 18.057 40.505 -9.382 1.00 57.63 A N ANISOU 1463 N PRO A 195 11170 6868 3859 -353 657 -423 A N ATOM 1464 CA PRO A 195 17.289 41.768 -9.515 1.00 58.88 A C ANISOU 1464 CA PRO A 195 11409 6977 3986 -450 513 -280 A C ATOM 1465 C PRO A 195 15.922 41.588 -10.192 1.00 59.94 A C ANISOU 1465 C PRO A 195 11753 7030 3989 -440 261 -290 A C ATOM 1466 O PRO A 195 15.000 42.358 -9.915 1.00 60.85 A O ANISOU 1466 O PRO A 195 11864 7087 4168 -472 75 -194 A O ATOM 1467 CB PRO A 195 18.193 42.665 -10.380 1.00 59.67 A C ANISOU 1467 CB PRO A 195 11614 7156 3900 -531 721 -184 A C ATOM 1468 CG PRO A 195 19.511 41.979 -10.456 1.00 59.94 A C ANISOU 1468 CG PRO A 195 11536 7310 3926 -482 992 -263 A C ATOM 1469 CD PRO A 195 19.307 40.528 -10.166 1.00 57.79 A C ANISOU 1469 CD PRO A 195 11230 7008 3721 -345 941 -428 A C ATOM 1470 N ALA A 196 15.798 40.584 -11.072 1.00 59.48 A N ANISOU 1470 N ALA A 196 11880 6972 3749 -392 252 -406 A N ATOM 1471 CA ALA A 196 14.565 40.241 -11.772 1.00 59.73 A C ANISOU 1471 CA ALA A 196 12115 6939 3641 -399 -1 -431 A C ATOM 1472 C ALA A 196 13.474 39.771 -10.808 1.00 60.05 A C ANISOU 1472 C ALA A 196 11996 6913 3908 -390 -243 -456 A C ATOM 1473 O ALA A 196 12.299 40.047 -11.028 1.00 61.27 A O ANISOU 1473 O ALA A 196 12206 7033 4039 -421 -486 -400 A O ATOM 1474 CB ALA A 196 14.841 39.142 -12.780 1.00 59.41 A C ANISOU 1474 CB ALA A 196 12310 6900 3365 -353 64 -574 A C ATOM 1475 N TYR A 197 13.849 39.035 -9.761 1.00 58.44 A N ANISOU 1475 N TYR A 197 11592 6698 3915 -346 -177 -535 A N ATOM 1476 CA TYR A 197 12.886 38.517 -8.791 1.00 57.18 A C ANISOU 1476 CA TYR A 197 11279 6481 3967 -349 -374 -558 A C ATOM 1477 C TYR A 197 12.603 39.517 -7.661 1.00 54.83 A C ANISOU 1477 C TYR A 197 10753 6185 3894 -363 -410 -438 A C ATOM 1478 O TYR A 197 11.547 39.443 -7.035 1.00 54.53 A O ANISOU 1478 O TYR A 197 10608 6115 3995 -373 -595 -413 A O ATOM 1479 CB TYR A 197 13.378 37.183 -8.203 1.00 57.79 A C ANISOU 1479 CB TYR A 197 11289 6523 4145 -292 -298 -698 A C ATOM 1480 CG TYR A 197 13.483 36.104 -9.256 1.00 59.20 A C ANISOU 1480 CG TYR A 197 11726 6665 4102 -265 -291 -833 A C ATOM 1481 CD1 TYR A 197 14.571 36.049 -10.116 1.00 60.52 A C ANISOU 1481 CD1 TYR A 197 12040 6881 4074 -206 -62 -881 A C ATOM 1482 CD2 TYR A 197 12.462 35.186 -9.443 1.00 60.49 A C ANISOU 1482 CD2 TYR A 197 12004 6744 4234 -307 -516 -908 A C ATOM 1483 CE1 TYR A 197 14.644 35.106 -11.127 1.00 61.80 A C ANISOU 1483 CE1 TYR A 197 12479 6997 4004 -168 -47 -1012 A C ATOM 1484 CE2 TYR A 197 12.533 34.222 -10.441 1.00 61.84 A C ANISOU 1484 CE2 TYR A 197 12460 6857 4179 -292 -525 -1039 A C ATOM 1485 CZ TYR A 197 13.627 34.187 -11.284 1.00 63.23 A C ANISOU 1485 CZ TYR A 197 12803 7071 4150 -211 -286 -1096 A C ATOM 1486 OH TYR A 197 13.720 33.237 -12.275 1.00 65.87 A O ANISOU 1486 OH TYR A 197 13451 7338 4240 -178 -278 -1237 A O ATOM 1487 N GLN A 198 13.531 40.450 -7.406 1.00 53.14 A N ANISOU 1487 N GLN A 198 10471 6010 3710 -372 -232 -363 A N ATOM 1488 CA GLN A 198 13.391 41.455 -6.356 1.00 52.14 A C ANISOU 1488 CA GLN A 198 10175 5866 3771 -388 -249 -259 A C ATOM 1489 C GLN A 198 12.222 42.416 -6.620 1.00 50.72 A C ANISOU 1489 C GLN A 198 10063 5648 3559 -397 -439 -143 A C ATOM 1490 O GLN A 198 11.676 42.957 -5.670 1.00 50.39 A O ANISOU 1490 O GLN A 198 9885 5572 3688 -378 -513 -83 A O ATOM 1491 CB GLN A 198 14.700 42.239 -6.177 1.00 53.34 A C ANISOU 1491 CB GLN A 198 10276 6062 3930 -426 -26 -205 A C ATOM 1492 CG GLN A 198 15.816 41.417 -5.517 1.00 55.83 A C ANISOU 1492 CG GLN A 198 10430 6427 4356 -396 142 -295 A C ATOM 1493 CD GLN A 198 17.190 42.027 -5.665 1.00 59.20 A C ANISOU 1493 CD GLN A 198 10810 6936 4746 -448 370 -248 A C ATOM 1494 NE2 GLN A 198 18.206 41.327 -5.216 1.00 57.16 A N ANISOU 1494 NE2 GLN A 198 10401 6745 4573 -407 516 -317 A N ATOM 1495 OE1 GLN A 198 17.364 43.124 -6.193 1.00 62.98 A O ANISOU 1495 OE1 GLN A 198 11385 7423 5120 -527 415 -141 A O ATOM 1496 N LYS A 199 11.804 42.589 -7.883 1.00 50.03 A N ANISOU 1496 N LYS A 199 10191 5567 3251 -410 -525 -114 A N ATOM 1497 CA LYS A 199 10.685 43.483 -8.241 1.00 49.56 A C ANISOU 1497 CA LYS A 199 10205 5477 3148 -397 -725 6 A C ATOM 1498 C LYS A 199 9.322 42.975 -7.701 1.00 48.56 A C ANISOU 1498 C LYS A 199 9937 5345 3168 -361 -958 -7 A C ATOM 1499 O LYS A 199 8.377 43.761 -7.583 1.00 48.06 A O ANISOU 1499 O LYS A 199 9839 5268 3154 -317 -1110 99 A O ATOM 1500 CB LYS A 199 10.614 43.677 -9.763 1.00 50.39 A C ANISOU 1500 CB LYS A 199 10590 5597 2961 -424 -771 38 A C ATOM 1501 N TYR A 200 9.223 41.676 -7.382 1.00 47.30 A N ANISOU 1501 N TYR A 200 9698 5197 3078 -376 -983 -130 A N ATOM 1502 CA TYR A 200 7.988 41.101 -6.849 1.00 46.88 A C ANISOU 1502 CA TYR A 200 9497 5149 3166 -375 -1187 -139 A C ATOM 1503 C TYR A 200 7.937 41.139 -5.302 1.00 46.80 A C ANISOU 1503 C TYR A 200 9234 5127 3423 -343 -1126 -132 A C ATOM 1504 O TYR A 200 6.931 40.732 -4.717 1.00 47.89 A O ANISOU 1504 O TYR A 200 9220 5280 3697 -345 -1264 -126 A O ATOM 1505 CB TYR A 200 7.814 39.662 -7.360 1.00 46.60 A C ANISOU 1505 CB TYR A 200 9549 5109 3046 -433 -1269 -269 A C ATOM 1506 CG TYR A 200 7.800 39.596 -8.873 1.00 47.55 A C ANISOU 1506 CG TYR A 200 9948 5237 2881 -466 -1342 -285 A C ATOM 1507 CD1 TYR A 200 6.649 39.887 -9.589 1.00 48.42 A C ANISOU 1507 CD1 TYR A 200 10124 5375 2899 -490 -1596 -211 A C ATOM 1508 CD2 TYR A 200 8.952 39.312 -9.590 1.00 48.72 A C ANISOU 1508 CD2 TYR A 200 10292 5375 2843 -464 -1151 -364 A C ATOM 1509 CE1 TYR A 200 6.646 39.894 -10.972 1.00 49.64 A C ANISOU 1509 CE1 TYR A 200 10558 5533 2770 -522 -1674 -217 A C ATOM 1510 CE2 TYR A 200 8.955 39.303 -10.978 1.00 49.95 A C ANISOU 1510 CE2 TYR A 200 10730 5537 2711 -490 -1200 -376 A C ATOM 1511 CZ TYR A 200 7.795 39.581 -11.667 1.00 51.44 A C ANISOU 1511 CZ TYR A 200 11007 5739 2798 -525 -1470 -305 A C ATOM 1512 OH TYR A 200 7.778 39.551 -13.047 1.00 54.63 A O ANISOU 1512 OH TYR A 200 11717 6146 2895 -558 -1538 -317 A O ATOM 1513 N LEU A 201 9.007 41.637 -4.639 1.00 45.32 A N ANISOU 1513 N LEU A 201 9000 4917 3302 -325 -922 -127 A N ATOM 1514 CA LEU A 201 9.087 41.724 -3.191 1.00 43.54 A C ANISOU 1514 CA LEU A 201 8574 4672 3296 -300 -857 -123 A C ATOM 1515 C LEU A 201 8.606 43.095 -2.740 1.00 43.13 A C ANISOU 1515 C LEU A 201 8482 4596 3310 -246 -885 1 A C ATOM 1516 O LEU A 201 9.303 43.799 -1.998 1.00 43.59 A O ANISOU 1516 O LEU A 201 8506 4616 3439 -239 -756 29 A O ATOM 1517 CB LEU A 201 10.529 41.463 -2.732 1.00 42.88 A C ANISOU 1517 CB LEU A 201 8468 4583 3240 -317 -646 -187 A C ATOM 1518 CG LEU A 201 11.163 40.138 -3.166 1.00 43.85 A C ANISOU 1518 CG LEU A 201 8649 4719 3295 -332 -585 -313 A C ATOM 1519 CD1 LEU A 201 12.520 39.984 -2.561 1.00 43.78 A C ANISOU 1519 CD1 LEU A 201 8563 4722 3350 -322 -388 -355 A C ATOM 1520 CD2 LEU A 201 10.335 38.961 -2.730 1.00 44.40 A C ANISOU 1520 CD2 LEU A 201 8650 4765 3455 -340 -715 -382 A C ATOM 1521 N TRP A 202 7.407 43.485 -3.194 1.00 42.14 A N ANISOU 1521 N TRP A 202 8366 4487 3159 -202 -1064 76 A N ATOM 1522 CA TRP A 202 6.810 44.781 -2.847 1.00 42.15 A C ANISOU 1522 CA TRP A 202 8346 4454 3215 -112 -1106 197 A C ATOM 1523 C TRP A 202 6.471 44.883 -1.348 1.00 40.94 A C ANISOU 1523 C TRP A 202 7996 4285 3276 -56 -1062 199 A C ATOM 1524 O TRP A 202 6.283 45.975 -0.855 1.00 42.03 A O ANISOU 1524 O TRP A 202 8140 4367 3462 25 -1038 276 A O ATOM 1525 CB TRP A 202 5.527 45.029 -3.672 1.00 42.68 A C ANISOU 1525 CB TRP A 202 8436 4564 3218 -56 -1328 278 A C ATOM 1526 CG TRP A 202 4.498 43.959 -3.455 1.00 44.17 A C ANISOU 1526 CG TRP A 202 8446 4833 3503 -76 -1476 237 A C ATOM 1527 CD1 TRP A 202 4.399 42.773 -4.120 1.00 45.28 A C ANISOU 1527 CD1 TRP A 202 8626 5015 3562 -177 -1565 154 A C ATOM 1528 CD2 TRP A 202 3.479 43.939 -2.443 1.00 44.99 A C ANISOU 1528 CD2 TRP A 202 8310 4980 3803 -11 -1535 275 A C ATOM 1529 CE2 TRP A 202 2.819 42.696 -2.540 1.00 46.04 A C ANISOU 1529 CE2 TRP A 202 8331 5189 3974 -101 -1661 219 A C ATOM 1530 CE3 TRP A 202 3.080 44.842 -1.444 1.00 45.87 A C ANISOU 1530 CE3 TRP A 202 8303 5070 4055 114 -1480 347 A C ATOM 1531 NE1 TRP A 202 3.393 42.010 -3.578 1.00 46.16 A N ANISOU 1531 NE1 TRP A 202 8536 5189 3815 -202 -1688 142 A N ATOM 1532 CZ2 TRP A 202 1.780 42.334 -1.684 1.00 46.80 A C ANISOU 1532 CZ2 TRP A 202 8176 5358 4250 -86 -1728 246 A C ATOM 1533 CZ3 TRP A 202 2.069 44.471 -0.581 1.00 47.10 A C ANISOU 1533 CZ3 TRP A 202 8215 5301 4382 154 -1530 364 A C ATOM 1534 CH2 TRP A 202 1.413 43.243 -0.722 1.00 47.16 A C ANISOU 1534 CH2 TRP A 202 8089 5401 4429 49 -1653 322 A C ATOM 1535 N TRP A 203 6.343 43.754 -0.643 1.00 38.59 A N ANISOU 1535 N TRP A 203 7548 4024 3091 -96 -1056 117 A N ATOM 1536 CA TRP A 203 5.949 43.696 0.759 1.00 36.45 A C ANISOU 1536 CA TRP A 203 7098 3748 3004 -53 -1015 116 A C ATOM 1537 C TRP A 203 7.109 43.826 1.743 1.00 34.13 A C ANISOU 1537 C TRP A 203 6807 3394 2768 -79 -839 72 A C ATOM 1538 O TRP A 203 6.943 43.474 2.909 1.00 34.02 A O ANISOU 1538 O TRP A 203 6664 3377 2884 -68 -799 47 A O ATOM 1539 CB TRP A 203 5.236 42.356 1.042 1.00 35.98 A C ANISOU 1539 CB TRP A 203 6890 3753 3028 -108 -1100 60 A C ATOM 1540 CG TRP A 203 5.937 41.147 0.496 1.00 36.04 A C ANISOU 1540 CG TRP A 203 6979 3756 2957 -212 -1088 -46 A C ATOM 1541 CD1 TRP A 203 5.791 40.612 -0.751 1.00 36.51 A C ANISOU 1541 CD1 TRP A 203 7158 3838 2875 -267 -1196 -77 A C ATOM 1542 CD2 TRP A 203 6.859 40.287 1.199 1.00 36.30 A C ANISOU 1542 CD2 TRP A 203 6996 3753 3044 -258 -967 -137 A C ATOM 1543 CE2 TRP A 203 7.234 39.258 0.308 1.00 36.92 A C ANISOU 1543 CE2 TRP A 203 7189 3826 3012 -322 -997 -224 A C ATOM 1544 CE3 TRP A 203 7.380 40.270 2.506 1.00 37.02 A C ANISOU 1544 CE3 TRP A 203 6997 3810 3258 -243 -847 -153 A C ATOM 1545 NE1 TRP A 203 6.561 39.474 -0.870 1.00 36.78 A N ANISOU 1545 NE1 TRP A 203 7262 3843 2870 -335 -1135 -190 A N ATOM 1546 CZ2 TRP A 203 8.124 38.233 0.679 1.00 37.89 A C ANISOU 1546 CZ2 TRP A 203 7332 3910 3156 -350 -902 -323 A C ATOM 1547 CZ3 TRP A 203 8.248 39.249 2.876 1.00 37.87 A C ANISOU 1547 CZ3 TRP A 203 7113 3889 3386 -284 -772 -243 A C ATOM 1548 CH2 TRP A 203 8.610 38.246 1.973 1.00 38.04 A C ANISOU 1548 CH2 TRP A 203 7240 3903 3309 -327 -796 -325 A C ATOM 1549 N LYS A 204 8.272 44.308 1.303 1.00 32.33 A N ANISOU 1549 N LYS A 204 6716 3127 2442 -122 -739 66 A N ATOM 1550 CA LYS A 204 9.459 44.478 2.156 1.00 31.53 A C ANISOU 1550 CA LYS A 204 6606 2984 2390 -166 -590 33 A C ATOM 1551 C LYS A 204 9.133 45.220 3.470 1.00 31.56 A C ANISOU 1551 C LYS A 204 6550 2928 2512 -108 -563 71 A C ATOM 1552 O LYS A 204 9.514 44.750 4.525 1.00 32.14 A O ANISOU 1552 O LYS A 204 6536 2996 2679 -129 -504 22 A O ATOM 1553 CB LYS A 204 10.536 45.265 1.381 1.00 32.09 A C ANISOU 1553 CB LYS A 204 6829 3032 2333 -225 -502 65 A C ATOM 1554 CG LYS A 204 11.841 45.370 2.118 1.00 32.52 A C ANISOU 1554 CG LYS A 204 6852 3072 2433 -296 -365 36 A C ATOM 1555 CD LYS A 204 12.805 46.327 1.469 1.00 32.09 A C ANISOU 1555 CD LYS A 204 6927 2996 2267 -376 -277 92 A C ATOM 1556 CE LYS A 204 14.086 46.289 2.247 1.00 33.32 A C ANISOU 1556 CE LYS A 204 7003 3167 2488 -462 -160 62 A C ATOM 1557 NZ LYS A 204 15.140 47.130 1.657 1.00 34.46 A N1+ ANISOU 1557 NZ LYS A 204 7241 3315 2537 -575 -60 120 A N1+ ATOM 1558 N LYS A 205 8.367 46.322 3.397 1.00 31.50 A N ANISOU 1558 N LYS A 205 6603 2873 2493 -19 -613 156 A N ATOM 1559 CA LYS A 205 7.971 47.154 4.542 1.00 32.17 A C ANISOU 1559 CA LYS A 205 6675 2883 2663 66 -581 191 A C ATOM 1560 C LYS A 205 7.075 46.412 5.511 1.00 33.00 A C ANISOU 1560 C LYS A 205 6599 3044 2897 124 -600 163 A C ATOM 1561 O LYS A 205 7.110 46.724 6.696 1.00 32.73 A O ANISOU 1561 O LYS A 205 6546 2958 2931 158 -529 155 A O ATOM 1562 CB LYS A 205 7.267 48.421 4.078 1.00 32.89 A C ANISOU 1562 CB LYS A 205 6887 2908 2702 180 -638 289 A C ATOM 1563 CG LYS A 205 8.217 49.384 3.409 1.00 38.13 A C ANISOU 1563 CG LYS A 205 7765 3480 3242 110 -595 332 A C ATOM 1564 CD LYS A 205 7.523 50.612 2.839 1.00 44.07 A C ANISOU 1564 CD LYS A 205 8674 4144 3926 229 -666 439 A C ATOM 1565 CE LYS A 205 6.709 51.368 3.841 1.00 50.29 A C ANISOU 1565 CE LYS A 205 9458 4849 4802 393 -664 470 A C ATOM 1566 NZ LYS A 205 6.032 52.525 3.190 1.00 55.71 A N1+ ANISOU 1566 NZ LYS A 205 10307 5443 5417 536 -743 579 A N1+ ATOM 1567 N TYR A 206 6.264 45.453 5.020 1.00 33.43 A N ANISOU 1567 N TYR A 206 6532 3197 2972 121 -694 153 A N ATOM 1568 CA TYR A 206 5.411 44.617 5.873 1.00 34.97 A C ANISOU 1568 CA TYR A 206 6542 3457 3287 139 -710 135 A C ATOM 1569 C TYR A 206 6.249 43.652 6.708 1.00 33.60 A C ANISOU 1569 C TYR A 206 6334 3273 3161 41 -629 52 A C ATOM 1570 O TYR A 206 5.831 43.286 7.807 1.00 34.10 A O ANISOU 1570 O TYR A 206 6293 3347 3316 57 -590 45 A O ATOM 1571 CB TYR A 206 4.376 43.831 5.052 1.00 37.09 A C ANISOU 1571 CB TYR A 206 6701 3832 3560 121 -853 152 A C ATOM 1572 CG TYR A 206 3.264 44.717 4.541 1.00 41.07 A C ANISOU 1572 CG TYR A 206 7172 4374 4058 249 -951 251 A C ATOM 1573 CD1 TYR A 206 2.286 45.204 5.399 1.00 43.32 A C ANISOU 1573 CD1 TYR A 206 7321 4690 4450 381 -929 310 A C ATOM 1574 CD2 TYR A 206 3.226 45.123 3.212 1.00 43.12 A C ANISOU 1574 CD2 TYR A 206 7549 4637 4199 256 -1058 292 A C ATOM 1575 CE1 TYR A 206 1.282 46.050 4.941 1.00 45.26 A C ANISOU 1575 CE1 TYR A 206 7525 4973 4698 533 -1017 407 A C ATOM 1576 CE2 TYR A 206 2.223 45.959 2.742 1.00 44.82 A C ANISOU 1576 CE2 TYR A 206 7739 4882 4406 392 -1165 394 A C ATOM 1577 CZ TYR A 206 1.242 46.405 3.606 1.00 46.91 A C ANISOU 1577 CZ TYR A 206 7844 5183 4794 538 -1148 452 A C ATOM 1578 OH TYR A 206 0.243 47.225 3.141 1.00 50.66 A O ANISOU 1578 OH TYR A 206 8279 5696 5272 702 -1256 558 A O ATOM 1579 N LEU A 207 7.424 43.234 6.198 1.00 31.56 A N ANISOU 1579 N LEU A 207 6161 2996 2835 -49 -597 -5 A N ATOM 1580 CA LEU A 207 8.340 42.390 6.945 1.00 29.67 A C ANISOU 1580 CA LEU A 207 5894 2741 2636 -117 -526 -76 A C ATOM 1581 C LEU A 207 8.992 43.238 8.044 1.00 27.86 A C ANISOU 1581 C LEU A 207 5704 2445 2436 -102 -435 -65 A C ATOM 1582 O LEU A 207 9.025 42.811 9.191 1.00 27.46 A O ANISOU 1582 O LEU A 207 5596 2382 2456 -107 -399 -88 A O ATOM 1583 CB LEU A 207 9.383 41.763 6.014 1.00 29.32 A C ANISOU 1583 CB LEU A 207 5916 2711 2511 -185 -511 -134 A C ATOM 1584 CG LEU A 207 10.582 41.097 6.690 1.00 30.07 A C ANISOU 1584 CG LEU A 207 5991 2792 2642 -228 -429 -197 A C ATOM 1585 CD1 LEU A 207 10.164 39.989 7.680 1.00 29.89 A C ANISOU 1585 CD1 LEU A 207 5878 2763 2715 -233 -450 -231 A C ATOM 1586 CD2 LEU A 207 11.526 40.584 5.666 1.00 30.74 A C ANISOU 1586 CD2 LEU A 207 6133 2904 2641 -259 -396 -247 A C ATOM 1587 N THR A 208 9.428 44.477 7.730 1.00 26.96 A N ANISOU 1587 N THR A 208 5707 2277 2259 -92 -406 -23 A N ATOM 1588 CA THR A 208 10.020 45.343 8.744 1.00 26.06 A C ANISOU 1588 CA THR A 208 5662 2081 2159 -100 -339 -15 A C ATOM 1589 C THR A 208 8.965 45.644 9.841 1.00 26.53 A C ANISOU 1589 C THR A 208 5688 2110 2284 3 -331 6 A C ATOM 1590 O THR A 208 9.302 45.597 11.023 1.00 27.26 A O ANISOU 1590 O THR A 208 5783 2163 2410 -13 -282 -21 A O ATOM 1591 CB THR A 208 10.611 46.608 8.119 1.00 27.06 A C ANISOU 1591 CB THR A 208 5945 2139 2198 -129 -321 33 A C ATOM 1592 CG2 THR A 208 11.474 47.396 9.114 1.00 25.51 A C ANISOU 1592 CG2 THR A 208 5836 1851 2004 -189 -265 31 A C ATOM 1593 OG1 THR A 208 11.378 46.251 6.956 1.00 28.24 A O ANISOU 1593 OG1 THR A 208 6109 2346 2277 -210 -315 23 A O ATOM 1594 N SER A 209 7.675 45.838 9.459 1.00 26.18 A N ANISOU 1594 N SER A 209 5593 2098 2254 110 -379 55 A N ATOM 1595 CA SER A 209 6.592 46.068 10.427 1.00 26.40 A C ANISOU 1595 CA SER A 209 5556 2128 2349 228 -350 80 A C ATOM 1596 C SER A 209 6.435 44.881 11.348 1.00 25.71 A C ANISOU 1596 C SER A 209 5336 2098 2333 179 -322 39 A C ATOM 1597 O SER A 209 6.168 45.066 12.535 1.00 26.01 A O ANISOU 1597 O SER A 209 5373 2107 2401 229 -249 37 A O ATOM 1598 CB SER A 209 5.261 46.301 9.726 1.00 28.72 A C ANISOU 1598 CB SER A 209 5763 2489 2661 346 -421 147 A C ATOM 1599 OG SER A 209 5.394 47.261 8.707 1.00 34.88 A O ANISOU 1599 OG SER A 209 6676 3215 3360 386 -469 194 A O ATOM 1600 N LEU A 210 6.552 43.655 10.790 1.00 24.77 A N ANISOU 1600 N LEU A 210 5129 2052 2232 86 -378 7 A N ATOM 1601 CA LEU A 210 6.426 42.427 11.544 1.00 24.19 A C ANISOU 1601 CA LEU A 210 4956 2015 2220 25 -365 -26 A C ATOM 1602 C LEU A 210 7.551 42.355 12.593 1.00 24.92 A C ANISOU 1602 C LEU A 210 5127 2036 2304 -23 -297 -70 A C ATOM 1603 O LEU A 210 7.301 41.990 13.738 1.00 25.37 A O ANISOU 1603 O LEU A 210 5154 2088 2398 -20 -249 -72 A O ATOM 1604 CB LEU A 210 6.450 41.193 10.591 1.00 23.71 A C ANISOU 1604 CB LEU A 210 4843 2009 2158 -67 -451 -59 A C ATOM 1605 CG LEU A 210 6.326 39.850 11.295 1.00 24.79 A C ANISOU 1605 CG LEU A 210 4908 2158 2352 -142 -450 -89 A C ATOM 1606 CD1 LEU A 210 4.999 39.728 12.006 1.00 25.03 A C ANISOU 1606 CD1 LEU A 210 4806 2249 2455 -117 -436 -33 A C ATOM 1607 CD2 LEU A 210 6.597 38.643 10.325 1.00 25.26 A C ANISOU 1607 CD2 LEU A 210 4982 2227 2389 -232 -533 -141 A C ATOM 1608 N GLN A 211 8.781 42.728 12.206 1.00 25.00 A N ANISOU 1608 N GLN A 211 5234 2002 2261 -71 -294 -97 A N ATOM 1609 CA GLN A 211 9.927 42.764 13.111 1.00 25.08 A C ANISOU 1609 CA GLN A 211 5304 1961 2264 -126 -254 -129 A C ATOM 1610 C GLN A 211 9.705 43.790 14.222 1.00 25.87 A C ANISOU 1610 C GLN A 211 5494 1988 2349 -75 -203 -109 A C ATOM 1611 O GLN A 211 9.909 43.456 15.382 1.00 27.08 A O ANISOU 1611 O GLN A 211 5658 2117 2512 -93 -176 -128 A O ATOM 1612 CB GLN A 211 11.215 43.059 12.341 1.00 25.38 A C ANISOU 1612 CB GLN A 211 5394 1994 2254 -194 -260 -146 A C ATOM 1613 CG GLN A 211 11.572 41.890 11.408 1.00 26.73 A C ANISOU 1613 CG GLN A 211 5497 2230 2427 -228 -288 -184 A C ATOM 1614 CD GLN A 211 12.662 42.276 10.445 1.00 29.81 A C ANISOU 1614 CD GLN A 211 5926 2640 2758 -277 -268 -189 A C ATOM 1615 NE2 GLN A 211 13.862 41.759 10.655 1.00 28.23 A N ANISOU 1615 NE2 GLN A 211 5688 2467 2573 -322 -243 -223 A N ATOM 1616 OE1 GLN A 211 12.442 43.054 9.505 1.00 31.60 A O ANISOU 1616 OE1 GLN A 211 6216 2867 2925 -271 -271 -155 A O ATOM 1617 N LEU A 212 9.177 44.972 13.904 1.00 25.16 A N ANISOU 1617 N LEU A 212 5481 1854 2226 2 -190 -71 A N ATOM 1618 CA LEU A 212 8.879 45.982 14.924 1.00 25.42 A C ANISOU 1618 CA LEU A 212 5634 1795 2230 75 -132 -60 A C ATOM 1619 C LEU A 212 7.799 45.493 15.904 1.00 26.68 A C ANISOU 1619 C LEU A 212 5711 1995 2432 159 -75 -54 A C ATOM 1620 O LEU A 212 7.945 45.662 17.113 1.00 26.81 A O ANISOU 1620 O LEU A 212 5811 1954 2420 166 -20 -74 A O ATOM 1621 CB LEU A 212 8.419 47.266 14.251 1.00 24.75 A C ANISOU 1621 CB LEU A 212 5655 1645 2102 169 -134 -16 A C ATOM 1622 CG LEU A 212 9.502 48.058 13.561 1.00 25.19 A C ANISOU 1622 CG LEU A 212 5851 1627 2094 74 -164 -10 A C ATOM 1623 CD1 LEU A 212 8.899 49.114 12.643 1.00 24.97 A C ANISOU 1623 CD1 LEU A 212 5919 1545 2025 172 -183 49 A C ATOM 1624 CD2 LEU A 212 10.378 48.713 14.582 1.00 25.93 A C ANISOU 1624 CD2 LEU A 212 6103 1607 2142 1 -140 -38 A C ATOM 1625 N VAL A 213 6.709 44.898 15.380 1.00 27.19 A N ANISOU 1625 N VAL A 213 5613 2162 2556 211 -90 -21 A N ATOM 1626 CA VAL A 213 5.600 44.376 16.183 1.00 27.95 A C ANISOU 1626 CA VAL A 213 5590 2327 2702 272 -28 2 A C ATOM 1627 C VAL A 213 6.132 43.239 17.091 1.00 27.89 A C ANISOU 1627 C VAL A 213 5567 2325 2705 159 -14 -33 A C ATOM 1628 O VAL A 213 5.732 43.155 18.255 1.00 27.79 A O ANISOU 1628 O VAL A 213 5569 2307 2683 191 71 -26 A O ATOM 1629 CB VAL A 213 4.425 43.943 15.273 1.00 29.73 A C ANISOU 1629 CB VAL A 213 5624 2676 2995 310 -78 53 A C ATOM 1630 CG1 VAL A 213 3.485 42.975 15.965 1.00 30.64 A C ANISOU 1630 CG1 VAL A 213 5572 2891 3178 292 -33 80 A C ATOM 1631 CG2 VAL A 213 3.656 45.156 14.755 1.00 30.43 A C ANISOU 1631 CG2 VAL A 213 5724 2760 3076 474 -75 106 A C ATOM 1632 N GLN A 214 7.102 42.442 16.601 1.00 28.01 A N ANISOU 1632 N GLN A 214 5579 2339 2724 41 -89 -68 A N ATOM 1633 CA GLN A 214 7.758 41.382 17.384 1.00 28.13 A C ANISOU 1633 CA GLN A 214 5601 2341 2745 -50 -95 -98 A C ATOM 1634 C GLN A 214 8.426 41.986 18.651 1.00 28.60 A C ANISOU 1634 C GLN A 214 5808 2317 2742 -47 -48 -116 A C ATOM 1635 O GLN A 214 8.208 41.457 19.738 1.00 29.82 A O ANISOU 1635 O GLN A 214 5978 2467 2886 -58 -6 -110 A O ATOM 1636 CB GLN A 214 8.785 40.680 16.506 1.00 28.82 A C ANISOU 1636 CB GLN A 214 5675 2434 2840 -132 -176 -135 A C ATOM 1637 CG GLN A 214 9.862 39.899 17.236 1.00 31.70 A C ANISOU 1637 CG GLN A 214 6081 2764 3201 -196 -197 -167 A C ATOM 1638 CD GLN A 214 11.019 39.530 16.342 1.00 34.25 A C ANISOU 1638 CD GLN A 214 6393 3096 3524 -238 -252 -204 A C ATOM 1639 NE2 GLN A 214 11.540 40.450 15.533 1.00 36.20 A N ANISOU 1639 NE2 GLN A 214 6667 3347 3740 -238 -254 -207 A N ATOM 1640 OE1 GLN A 214 11.477 38.422 16.381 1.00 36.36 A O ANISOU 1640 OE1 GLN A 214 6636 3364 3815 -265 -285 -227 A O ATOM 1641 N PHE A 215 9.211 43.085 18.526 1.00 27.28 A N ANISOU 1641 N PHE A 215 5765 2079 2522 -47 -62 -133 A N ATOM 1642 CA PHE A 215 9.871 43.701 19.689 1.00 27.02 A C ANISOU 1642 CA PHE A 215 5894 1957 2416 -68 -44 -155 A C ATOM 1643 C PHE A 215 8.823 44.256 20.668 1.00 27.21 A C ANISOU 1643 C PHE A 215 5995 1946 2396 41 61 -141 A C ATOM 1644 O PHE A 215 8.966 44.085 21.886 1.00 27.59 A O ANISOU 1644 O PHE A 215 6138 1957 2389 25 94 -155 A O ATOM 1645 CB PHE A 215 10.845 44.818 19.270 1.00 27.07 A C ANISOU 1645 CB PHE A 215 6020 1889 2374 -116 -87 -169 A C ATOM 1646 CG PHE A 215 11.840 44.358 18.233 1.00 27.68 A C ANISOU 1646 CG PHE A 215 6005 2023 2490 -209 -159 -175 A C ATOM 1647 CD1 PHE A 215 12.509 43.153 18.377 1.00 27.88 A C ANISOU 1647 CD1 PHE A 215 5933 2105 2554 -268 -202 -193 A C ATOM 1648 CD2 PHE A 215 12.105 45.129 17.108 1.00 28.02 A C ANISOU 1648 CD2 PHE A 215 6069 2057 2520 -224 -173 -161 A C ATOM 1649 CE1 PHE A 215 13.396 42.702 17.394 1.00 28.01 A C ANISOU 1649 CE1 PHE A 215 5860 2181 2603 -322 -245 -203 A C ATOM 1650 CE2 PHE A 215 12.989 44.673 16.129 1.00 28.73 A C ANISOU 1650 CE2 PHE A 215 6070 2213 2633 -300 -212 -166 A C ATOM 1651 CZ PHE A 215 13.622 43.456 16.274 1.00 27.58 A C ANISOU 1651 CZ PHE A 215 5815 2134 2531 -340 -241 -191 A C ATOM 1652 N VAL A 216 7.736 44.842 20.148 1.00 26.29 A N ANISOU 1652 N VAL A 216 5833 1853 2302 163 117 -111 A N ATOM 1653 CA VAL A 216 6.657 45.333 21.007 1.00 26.65 A C ANISOU 1653 CA VAL A 216 5921 1890 2316 301 240 -94 A C ATOM 1654 C VAL A 216 6.028 44.175 21.810 1.00 25.76 A C ANISOU 1654 C VAL A 216 5691 1866 2231 279 305 -72 A C ATOM 1655 O VAL A 216 5.907 44.289 23.022 1.00 26.10 A O ANISOU 1655 O VAL A 216 5848 1869 2199 308 392 -83 A O ATOM 1656 CB VAL A 216 5.571 46.113 20.218 1.00 28.13 A C ANISOU 1656 CB VAL A 216 6039 2107 2540 460 279 -52 A C ATOM 1657 CG1 VAL A 216 4.391 46.460 21.127 1.00 28.69 A C ANISOU 1657 CG1 VAL A 216 6105 2202 2593 626 430 -30 A C ATOM 1658 CG2 VAL A 216 6.155 47.389 19.591 1.00 28.96 A C ANISOU 1658 CG2 VAL A 216 6321 2089 2593 487 230 -65 A C ATOM 1659 N ILE A 217 5.673 43.057 21.157 1.00 25.21 A N ANISOU 1659 N ILE A 217 5422 1904 2252 213 258 -43 A N ATOM 1660 CA ILE A 217 5.059 41.919 21.828 1.00 25.34 A C ANISOU 1660 CA ILE A 217 5334 1995 2297 163 310 -10 A C ATOM 1661 C ILE A 217 6.022 41.307 22.876 1.00 25.81 A C ANISOU 1661 C ILE A 217 5533 1984 2290 63 290 -39 A C ATOM 1662 O ILE A 217 5.576 40.944 23.961 1.00 26.69 A O ANISOU 1662 O ILE A 217 5679 2106 2358 63 383 -16 A O ATOM 1663 CB ILE A 217 4.585 40.856 20.795 1.00 25.64 A C ANISOU 1663 CB ILE A 217 5166 2135 2440 85 233 21 A C ATOM 1664 CG1 ILE A 217 3.499 41.422 19.877 1.00 25.99 A C ANISOU 1664 CG1 ILE A 217 5059 2270 2546 185 239 63 A C ATOM 1665 CG2 ILE A 217 4.086 39.593 21.497 1.00 25.61 A C ANISOU 1665 CG2 ILE A 217 5085 2184 2462 -9 271 58 A C ATOM 1666 CD1 ILE A 217 3.177 40.473 18.680 1.00 27.20 A C ANISOU 1666 CD1 ILE A 217 5046 2507 2782 86 121 82 A C ATOM 1667 N VAL A 218 7.336 41.241 22.569 1.00 25.10 A N ANISOU 1667 N VAL A 218 5521 1829 2185 -16 173 -82 A N ATOM 1668 CA VAL A 218 8.357 40.736 23.482 1.00 25.13 A C ANISOU 1668 CA VAL A 218 5645 1773 2131 -98 123 -103 A C ATOM 1669 C VAL A 218 8.428 41.622 24.733 1.00 26.41 A C ANISOU 1669 C VAL A 218 6008 1858 2171 -54 192 -119 A C ATOM 1670 O VAL A 218 8.503 41.097 25.853 1.00 26.53 A O ANISOU 1670 O VAL A 218 6112 1851 2117 -88 216 -108 A O ATOM 1671 CB VAL A 218 9.727 40.617 22.776 1.00 25.17 A C ANISOU 1671 CB VAL A 218 5650 1753 2160 -170 -11 -138 A C ATOM 1672 CG1 VAL A 218 10.866 40.426 23.784 1.00 24.96 A C ANISOU 1672 CG1 VAL A 218 5751 1668 2066 -234 -79 -155 A C ATOM 1673 CG2 VAL A 218 9.702 39.470 21.764 1.00 25.65 A C ANISOU 1673 CG2 VAL A 218 5557 1874 2314 -210 -69 -131 A C ATOM 1674 N ALA A 219 8.378 42.956 24.548 1.00 27.14 A N ANISOU 1674 N ALA A 219 6197 1893 2220 21 223 -143 A N ATOM 1675 CA ALA A 219 8.411 43.899 25.657 1.00 27.80 A C ANISOU 1675 CA ALA A 219 6512 1879 2171 71 288 -172 A C ATOM 1676 C ALA A 219 7.144 43.775 26.486 1.00 29.45 A C ANISOU 1676 C ALA A 219 6719 2129 2340 178 460 -143 A C ATOM 1677 O ALA A 219 7.229 43.848 27.697 1.00 30.69 A O ANISOU 1677 O ALA A 219 7054 2232 2375 178 515 -158 A O ATOM 1678 CB ALA A 219 8.560 45.339 25.141 1.00 26.87 A C ANISOU 1678 CB ALA A 219 6514 1671 2023 134 282 -202 A C ATOM 1679 N ILE A 220 5.959 43.654 25.853 1.00 29.39 A N ANISOU 1679 N ILE A 220 6514 2227 2426 270 548 -98 A N ATOM 1680 CA ILE A 220 4.700 43.550 26.598 1.00 29.30 A C ANISOU 1680 CA ILE A 220 6454 2289 2392 374 731 -57 A C ATOM 1681 C ILE A 220 4.691 42.241 27.411 1.00 29.28 A C ANISOU 1681 C ILE A 220 6421 2334 2370 253 750 -21 A C ATOM 1682 O ILE A 220 4.298 42.256 28.578 1.00 30.02 A O ANISOU 1682 O ILE A 220 6630 2420 2355 290 884 -11 A O ATOM 1683 CB ILE A 220 3.479 43.649 25.647 1.00 29.63 A C ANISOU 1683 CB ILE A 220 6242 2458 2558 481 791 -4 A C ATOM 1684 CG1 ILE A 220 3.372 45.066 25.037 1.00 31.36 A C ANISOU 1684 CG1 ILE A 220 6540 2608 2768 638 794 -30 A C ATOM 1685 CG2 ILE A 220 2.175 43.258 26.372 1.00 29.27 A C ANISOU 1685 CG2 ILE A 220 6065 2537 2518 554 980 58 A C ATOM 1686 CD1 ILE A 220 2.325 45.171 23.955 1.00 33.02 A C ANISOU 1686 CD1 ILE A 220 6500 2942 3104 741 802 28 A C ATOM 1687 N HIS A 221 5.163 41.130 26.816 1.00 27.61 A N ANISOU 1687 N HIS A 221 6087 2157 2248 115 618 -3 A N ATOM 1688 CA HIS A 221 5.213 39.849 27.525 1.00 27.42 A C ANISOU 1688 CA HIS A 221 6062 2151 2207 -2 617 37 A C ATOM 1689 C HIS A 221 6.172 39.920 28.723 1.00 28.11 A C ANISOU 1689 C HIS A 221 6410 2127 2145 -43 582 6 A C ATOM 1690 O HIS A 221 5.783 39.534 29.812 1.00 29.06 A O ANISOU 1690 O HIS A 221 6621 2250 2170 -56 684 41 A O ATOM 1691 CB HIS A 221 5.631 38.701 26.580 1.00 26.58 A C ANISOU 1691 CB HIS A 221 5814 2068 2218 -122 468 50 A C ATOM 1692 CG HIS A 221 5.896 37.403 27.292 1.00 29.47 A C ANISOU 1692 CG HIS A 221 6233 2408 2557 -239 436 88 A C ATOM 1693 CD2 HIS A 221 5.030 36.464 27.733 1.00 29.60 A C ANISOU 1693 CD2 HIS A 221 6184 2477 2585 -308 519 159 A C ATOM 1694 ND1 HIS A 221 7.180 37.029 27.665 1.00 31.66 A N ANISOU 1694 ND1 HIS A 221 6656 2592 2783 -294 305 59 A N ATOM 1695 CE1 HIS A 221 7.055 35.879 28.305 1.00 31.28 A C ANISOU 1695 CE1 HIS A 221 6644 2527 2712 -377 307 113 A C ATOM 1696 NE2 HIS A 221 5.783 35.503 28.377 1.00 31.24 A N ANISOU 1696 NE2 HIS A 221 6528 2603 2740 -401 437 174 A N ATOM 1697 N ILE A 222 7.431 40.355 28.519 1.00 27.59 A N ANISOU 1697 N ILE A 222 6456 1974 2054 -77 432 -50 A N ATOM 1698 CA ILE A 222 8.409 40.387 29.598 1.00 27.87 A C ANISOU 1698 CA ILE A 222 6720 1917 1954 -133 358 -74 A C ATOM 1699 C ILE A 222 8.046 41.423 30.661 1.00 29.56 A C ANISOU 1699 C ILE A 222 7163 2067 2002 -51 483 -103 A C ATOM 1700 O ILE A 222 8.443 41.237 31.806 1.00 29.10 A O ANISOU 1700 O ILE A 222 7304 1951 1802 -96 469 -104 A O ATOM 1701 CB ILE A 222 9.838 40.616 29.065 1.00 27.65 A C ANISOU 1701 CB ILE A 222 6712 1837 1955 -202 163 -117 A C ATOM 1702 CG1 ILE A 222 10.876 40.011 30.007 1.00 28.12 A C ANISOU 1702 CG1 ILE A 222 6907 1847 1930 -291 35 -111 A C ATOM 1703 CG2 ILE A 222 10.122 42.100 28.783 1.00 27.69 A C ANISOU 1703 CG2 ILE A 222 6822 1778 1919 -159 157 -173 A C ATOM 1704 CD1 ILE A 222 10.856 38.448 30.011 1.00 27.82 A C ANISOU 1704 CD1 ILE A 222 6765 1848 1958 -340 -6 -53 A C ATOM 1705 N SER A 223 7.276 42.492 30.309 1.00 30.88 A N ANISOU 1705 N SER A 223 7323 2237 2175 80 606 -126 A N ATOM 1706 CA SER A 223 6.880 43.507 31.303 1.00 32.91 A C ANISOU 1706 CA SER A 223 7824 2415 2263 188 744 -164 A C ATOM 1707 C SER A 223 5.998 42.895 32.417 1.00 34.29 A C ANISOU 1707 C SER A 223 8040 2648 2342 220 927 -117 A C ATOM 1708 O SER A 223 5.985 43.433 33.518 1.00 35.18 A O ANISOU 1708 O SER A 223 8418 2681 2268 268 1014 -151 A O ATOM 1709 CB SER A 223 6.164 44.687 30.653 1.00 34.63 A C ANISOU 1709 CB SER A 223 8017 2622 2519 353 846 -189 A C ATOM 1710 OG SER A 223 4.830 44.363 30.298 1.00 37.81 A O ANISOU 1710 OG SER A 223 8179 3165 3021 461 1006 -128 A O ATOM 1711 N GLN A 224 5.305 41.762 32.153 1.00 34.31 A N ANISOU 1711 N GLN A 224 7801 2780 2455 175 982 -37 A N ATOM 1712 CA GLN A 224 4.483 41.091 33.162 1.00 34.72 A C ANISOU 1712 CA GLN A 224 7872 2897 2422 171 1159 26 A C ATOM 1713 C GLN A 224 5.292 40.709 34.383 1.00 36.57 A C ANISOU 1713 C GLN A 224 8388 3034 2472 75 1097 20 A C ATOM 1714 O GLN A 224 4.765 40.739 35.489 1.00 37.46 A O ANISOU 1714 O GLN A 224 8660 3149 2424 114 1267 38 A O ATOM 1715 CB GLN A 224 3.852 39.814 32.605 1.00 34.31 A C ANISOU 1715 CB GLN A 224 7535 2975 2526 74 1168 117 A C ATOM 1716 CG GLN A 224 2.871 40.027 31.485 1.00 35.48 A C ANISOU 1716 CG GLN A 224 7384 3249 2849 151 1231 144 A C ATOM 1717 CD GLN A 224 2.429 38.668 31.019 1.00 37.04 A C ANISOU 1717 CD GLN A 224 7351 3545 3176 6 1195 227 A C ATOM 1718 NE2 GLN A 224 3.267 37.982 30.262 1.00 32.45 A N ANISOU 1718 NE2 GLN A 224 6733 2914 2683 -109 986 212 A N ATOM 1719 OE1 GLN A 224 1.354 38.205 31.372 1.00 40.95 A O ANISOU 1719 OE1 GLN A 224 7713 4158 3687 -11 1358 306 A O ATOM 1720 N PHE A 225 6.566 40.332 34.187 1.00 37.32 A N ANISOU 1720 N PHE A 225 8539 3054 2586 -43 855 -1 A N ATOM 1721 CA PHE A 225 7.471 39.926 35.251 1.00 38.43 A C ANISOU 1721 CA PHE A 225 8927 3107 2567 -138 740 0 A C ATOM 1722 C PHE A 225 7.545 40.962 36.389 1.00 39.04 A C ANISOU 1722 C PHE A 225 9339 3087 2405 -75 816 -61 A C ATOM 1723 O PHE A 225 7.521 40.593 37.574 1.00 39.76 A O ANISOU 1723 O PHE A 225 9645 3148 2313 -109 865 -33 A O ATOM 1724 CB PHE A 225 8.884 39.659 34.699 1.00 38.93 A C ANISOU 1724 CB PHE A 225 8962 3119 2709 -237 461 -24 A C ATOM 1725 CG PHE A 225 9.823 39.258 35.810 1.00 40.57 A C ANISOU 1725 CG PHE A 225 9409 3249 2757 -323 319 -13 A C ATOM 1726 CD1 PHE A 225 9.802 37.969 36.323 1.00 41.62 A C ANISOU 1726 CD1 PHE A 225 9550 3395 2868 -391 295 70 A C ATOM 1727 CD2 PHE A 225 10.641 40.197 36.420 1.00 41.14 A C ANISOU 1727 CD2 PHE A 225 9726 3226 2678 -340 212 -79 A C ATOM 1728 CE1 PHE A 225 10.609 37.620 37.391 1.00 42.35 A C ANISOU 1728 CE1 PHE A 225 9880 3415 2798 -456 160 91 A C ATOM 1729 CE2 PHE A 225 11.449 39.841 37.483 1.00 42.29 A C ANISOU 1729 CE2 PHE A 225 10096 3309 2663 -421 67 -62 A C ATOM 1730 CZ PHE A 225 11.411 38.559 37.973 1.00 42.26 A C ANISOU 1730 CZ PHE A 225 10090 3326 2640 -468 44 25 A C ATOM 1731 N PHE A 226 7.631 42.246 36.044 1.00 38.38 A N ANISOU 1731 N PHE A 226 9331 2942 2309 13 824 -142 A N ATOM 1732 CA PHE A 226 7.737 43.316 37.037 1.00 38.69 A C ANISOU 1732 CA PHE A 226 9725 2859 2116 75 882 -217 A C ATOM 1733 C PHE A 226 6.489 43.434 37.916 1.00 39.04 A C ANISOU 1733 C PHE A 226 9873 2943 2018 209 1183 -199 A C ATOM 1734 O PHE A 226 6.587 43.973 39.017 1.00 39.37 A O ANISOU 1734 O PHE A 226 10256 2884 1818 241 1242 -249 A O ATOM 1735 CB PHE A 226 8.021 44.675 36.336 1.00 38.85 A C ANISOU 1735 CB PHE A 226 9803 2787 2170 142 830 -303 A C ATOM 1736 CG PHE A 226 9.262 44.596 35.472 1.00 39.42 A C ANISOU 1736 CG PHE A 226 9762 2839 2376 0 557 -312 A C ATOM 1737 CD1 PHE A 226 10.523 44.704 36.033 1.00 40.24 A C ANISOU 1737 CD1 PHE A 226 10066 2852 2370 -143 337 -344 A C ATOM 1738 CD2 PHE A 226 9.169 44.306 34.118 1.00 39.67 A C ANISOU 1738 CD2 PHE A 226 9471 2963 2640 2 520 -281 A C ATOM 1739 CE1 PHE A 226 11.660 44.560 35.249 1.00 40.78 A C ANISOU 1739 CE1 PHE A 226 9987 2935 2573 -271 105 -340 A C ATOM 1740 CE2 PHE A 226 10.310 44.145 33.346 1.00 40.11 A C ANISOU 1740 CE2 PHE A 226 9413 3017 2809 -122 296 -284 A C ATOM 1741 CZ PHE A 226 11.546 44.263 33.914 1.00 40.03 A C ANISOU 1741 CZ PHE A 226 9575 2932 2702 -254 99 -310 A C ATOM 1742 N PHE A 227 5.321 42.950 37.446 1.00 39.13 A N ANISOU 1742 N PHE A 227 9595 3104 2168 285 1375 -128 A N ATOM 1743 CA PHE A 227 4.059 43.083 38.193 1.00 39.92 A C ANISOU 1743 CA PHE A 227 9731 3279 2158 425 1692 -100 A C ATOM 1744 C PHE A 227 3.587 41.799 38.870 1.00 41.70 A C ANISOU 1744 C PHE A 227 9891 3609 2343 322 1796 9 A C ATOM 1745 O PHE A 227 2.691 41.863 39.714 1.00 42.24 A O ANISOU 1745 O PHE A 227 10041 3736 2274 410 2063 37 A O ATOM 1746 CB PHE A 227 2.936 43.544 37.251 1.00 39.04 A C ANISOU 1746 CB PHE A 227 9319 3288 2228 594 1859 -82 A C ATOM 1747 CG PHE A 227 3.192 44.852 36.551 1.00 38.51 A C ANISOU 1747 CG PHE A 227 9318 3115 2199 723 1794 -174 A C ATOM 1748 CD1 PHE A 227 2.963 46.056 37.190 1.00 38.83 A C ANISOU 1748 CD1 PHE A 227 9656 3039 2058 901 1935 -257 A C ATOM 1749 CD2 PHE A 227 3.612 44.880 35.237 1.00 38.82 A C ANISOU 1749 CD2 PHE A 227 9140 3165 2446 671 1604 -173 A C ATOM 1750 CE1 PHE A 227 3.175 47.262 36.529 1.00 38.74 A C ANISOU 1750 CE1 PHE A 227 9732 2908 2080 1015 1872 -333 A C ATOM 1751 CE2 PHE A 227 3.830 46.092 34.584 1.00 38.73 A C ANISOU 1751 CE2 PHE A 227 9207 3048 2460 779 1548 -244 A C ATOM 1752 CZ PHE A 227 3.613 47.269 35.237 1.00 38.15 A C ANISOU 1752 CZ PHE A 227 9436 2845 2212 945 1677 -321 A C ATOM 1753 N MET A 228 4.125 40.643 38.481 1.00 42.62 A N ANISOU 1753 N MET A 228 9862 3751 2581 145 1608 74 A N ATOM 1754 CA MET A 228 3.649 39.370 39.037 1.00 44.16 A C ANISOU 1754 CA MET A 228 10000 4028 2751 31 1697 189 A C ATOM 1755 C MET A 228 4.184 39.080 40.428 1.00 46.20 A C ANISOU 1755 C MET A 228 10625 4188 2739 -41 1679 200 A C ATOM 1756 O MET A 228 5.364 38.770 40.589 1.00 46.00 A O ANISOU 1756 O MET A 228 10752 4056 2671 -147 1419 183 A O ATOM 1757 CB MET A 228 3.965 38.197 38.105 1.00 43.96 A C ANISOU 1757 CB MET A 228 9716 4043 2946 -119 1509 254 A C ATOM 1758 CG MET A 228 3.234 38.293 36.797 1.00 45.68 A C ANISOU 1758 CG MET A 228 9569 4379 3408 -69 1549 265 A C ATOM 1759 SD MET A 228 3.469 36.845 35.736 1.00 49.91 A S ANISOU 1759 SD MET A 228 9839 4951 4173 -248 1353 336 A S ATOM 1760 CE MET A 228 5.147 37.047 35.189 1.00 40.57 A C ANISOU 1760 CE MET A 228 8766 3627 3023 -275 1030 247 A C ATOM 1761 N GLU A 229 3.296 39.141 41.433 1.00 48.19 A N ANISOU 1761 N GLU A 229 11010 4492 2809 18 1960 237 A N ATOM 1762 CA GLU A 229 3.646 38.765 42.799 1.00 50.69 A C ANISOU 1762 CA GLU A 229 11685 4730 2845 -57 1973 266 A C ATOM 1763 C GLU A 229 3.816 37.257 42.865 1.00 53.04 A C ANISOU 1763 C GLU A 229 11901 5051 3201 -248 1868 394 A C ATOM 1764 O GLU A 229 3.172 36.522 42.101 1.00 54.02 A O ANISOU 1764 O GLU A 229 11698 5288 3541 -305 1920 474 A O ATOM 1765 CB GLU A 229 2.570 39.219 43.796 1.00 54.14 A C ANISOU 1765 CB GLU A 229 12275 5231 3066 67 2339 276 A C ATOM 1766 CG GLU A 229 2.193 40.679 43.662 1.00 62.25 A C ANISOU 1766 CG GLU A 229 13363 6236 4052 294 2487 156 A C ATOM 1767 CD GLU A 229 1.103 41.119 44.617 1.00 73.30 A C ANISOU 1767 CD GLU A 229 14901 7708 5241 452 2876 162 A C ATOM 1768 OE1 GLU A 229 1.176 40.753 45.813 1.00 74.93 A O ANISOU 1768 OE1 GLU A 229 15415 7877 5179 390 2962 195 A O ATOM 1769 OE2 GLU A 229 0.182 41.843 44.174 1.00 78.54 A O1- ANISOU 1769 OE2 GLU A 229 15373 8467 6001 652 3099 136 A O1- ATOM 1770 N ASP A 230 4.726 36.793 43.726 1.00 53.71 A N ANISOU 1770 N ASP A 230 12290 5017 3099 -349 1692 413 A N ATOM 1771 CA ASP A 230 5.010 35.380 43.944 1.00 54.58 A C ANISOU 1771 CA ASP A 230 12407 5108 3223 -515 1571 536 A C ATOM 1772 C ASP A 230 5.415 34.623 42.656 1.00 53.00 A C ANISOU 1772 C ASP A 230 11890 4919 3329 -588 1354 560 A C ATOM 1773 O ASP A 230 5.258 33.400 42.585 1.00 53.34 A O ANISOU 1773 O ASP A 230 11858 4967 3441 -710 1324 670 A O ATOM 1774 CB ASP A 230 3.827 34.701 44.639 1.00 59.76 A C ANISOU 1774 CB ASP A 230 13066 5861 3779 -570 1876 661 A C ATOM 1775 CG ASP A 230 3.493 35.366 45.978 1.00 71.44 A C ANISOU 1775 CG ASP A 230 14898 7324 4922 -493 2100 639 A C ATOM 1776 OD1 ASP A 230 4.435 35.606 46.783 1.00 73.30 A O ANISOU 1776 OD1 ASP A 230 15498 7422 4930 -505 1927 594 A O ATOM 1777 OD2 ASP A 230 2.295 35.682 46.209 1.00 76.05 A O1- ANISOU 1777 OD2 ASP A 230 15391 8038 5466 -413 2448 664 A O1- ATOM 1778 N CYS A 231 5.958 35.338 41.655 1.00 51.14 A N ANISOU 1778 N CYS A 231 11497 4673 3260 -517 1203 457 A N ATOM 1779 CA CYS A 231 6.473 34.668 40.460 1.00 49.78 A C ANISOU 1779 CA CYS A 231 11068 4501 3346 -574 992 466 A C ATOM 1780 C CYS A 231 7.836 34.121 40.852 1.00 48.81 A C ANISOU 1780 C CYS A 231 11135 4256 3153 -640 696 476 A C ATOM 1781 O CYS A 231 8.669 34.863 41.386 1.00 49.07 A O ANISOU 1781 O CYS A 231 11382 4219 3044 -609 570 408 A O ATOM 1782 CB CYS A 231 6.541 35.604 39.258 1.00 48.77 A C ANISOU 1782 CB CYS A 231 10712 4415 3405 -479 954 366 A C ATOM 1783 SG CYS A 231 7.206 34.842 37.761 1.00 53.63 A S ANISOU 1783 SG CYS A 231 11038 5033 4308 -536 712 365 A S ATOM 1784 N LYS A 232 8.029 32.824 40.685 1.00 47.28 A N ANISOU 1784 N LYS A 232 10889 4033 3042 -732 589 566 A N ATOM 1785 CA LYS A 232 9.255 32.182 41.125 1.00 46.30 A C ANISOU 1785 CA LYS A 232 10942 3798 2851 -772 316 596 A C ATOM 1786 C LYS A 232 10.237 31.929 39.984 1.00 44.14 A C ANISOU 1786 C LYS A 232 10461 3507 2802 -749 70 552 A C ATOM 1787 O LYS A 232 11.096 31.054 40.102 1.00 44.12 A O ANISOU 1787 O LYS A 232 10522 3429 2811 -771 -141 601 A O ATOM 1788 CB LYS A 232 8.936 30.882 41.869 1.00 48.31 A C ANISOU 1788 CB LYS A 232 11349 3997 3008 -872 346 735 A C ATOM 1789 CG LYS A 232 8.207 31.137 43.184 1.00 52.33 A C ANISOU 1789 CG LYS A 232 12124 4517 3243 -897 569 784 A C ATOM 1790 CD LYS A 232 7.838 29.823 43.862 1.00 57.49 A C ANISOU 1790 CD LYS A 232 12927 5115 3802 -1018 614 938 A C ATOM 1791 N TYR A 233 10.185 32.747 38.917 1.00 41.82 A N ANISOU 1791 N TYR A 233 9938 3282 2671 -689 91 459 A N ATOM 1792 CA TYR A 233 11.161 32.693 37.821 1.00 40.10 A C ANISOU 1792 CA TYR A 233 9529 3062 2644 -660 -119 406 A C ATOM 1793 C TYR A 233 12.547 32.973 38.433 1.00 40.15 A C ANISOU 1793 C TYR A 233 9700 3009 2545 -652 -363 384 A C ATOM 1794 O TYR A 233 12.707 33.907 39.221 1.00 40.45 A O ANISOU 1794 O TYR A 233 9929 3031 2411 -652 -357 343 A O ATOM 1795 CB TYR A 233 10.792 33.700 36.733 1.00 38.55 A C ANISOU 1795 CB TYR A 233 9112 2946 2589 -604 -30 317 A C ATOM 1796 CG TYR A 233 11.803 33.710 35.615 1.00 37.32 A C ANISOU 1796 CG TYR A 233 8772 2798 2608 -579 -221 265 A C ATOM 1797 CD1 TYR A 233 12.022 32.577 34.839 1.00 37.20 A C ANISOU 1797 CD1 TYR A 233 8613 2774 2746 -589 -307 299 A C ATOM 1798 CD2 TYR A 233 12.562 34.839 35.351 1.00 37.15 A C ANISOU 1798 CD2 TYR A 233 8739 2787 2588 -550 -311 183 A C ATOM 1799 CE1 TYR A 233 12.975 32.572 33.831 1.00 37.59 A C ANISOU 1799 CE1 TYR A 233 8500 2840 2941 -550 -461 250 A C ATOM 1800 CE2 TYR A 233 13.498 34.855 34.333 1.00 37.28 A C ANISOU 1800 CE2 TYR A 233 8577 2830 2759 -535 -465 145 A C ATOM 1801 CZ TYR A 233 13.697 33.727 33.566 1.00 37.55 A C ANISOU 1801 CZ TYR A 233 8456 2870 2940 -525 -530 176 A C ATOM 1802 OH TYR A 233 14.623 33.763 32.548 1.00 37.01 A O ANISOU 1802 OH TYR A 233 8212 2838 3013 -495 -656 135 A O ATOM 1803 N GLN A 234 13.460 32.046 38.232 1.00 39.37 A N ANISOU 1803 N GLN A 234 9563 2870 2524 -651 -572 425 A N ATOM 1804 CA GLN A 234 14.690 31.938 38.998 1.00 38.60 A C ANISOU 1804 CA GLN A 234 9624 2723 2319 -651 -818 447 A C ATOM 1805 C GLN A 234 15.777 32.946 38.679 1.00 38.57 A C ANISOU 1805 C GLN A 234 9539 2762 2353 -636 -989 364 A C ATOM 1806 O GLN A 234 16.694 33.076 39.487 1.00 38.54 A O ANISOU 1806 O GLN A 234 9687 2732 2226 -658 -1187 381 A O ATOM 1807 CB GLN A 234 15.251 30.511 38.859 1.00 36.33 A C ANISOU 1807 CB GLN A 234 9310 2378 2117 -625 -977 530 A C ATOM 1808 CG GLN A 234 14.253 29.480 39.336 1.00 36.44 A C ANISOU 1808 CG GLN A 234 9460 2324 2063 -675 -833 629 A C ATOM 1809 CD GLN A 234 13.440 28.848 38.204 1.00 37.09 A C ANISOU 1809 CD GLN A 234 9330 2421 2342 -686 -698 629 A C ATOM 1810 NE2 GLN A 234 13.055 27.580 38.375 1.00 35.07 A N ANISOU 1810 NE2 GLN A 234 9163 2075 2086 -730 -685 725 A N ATOM 1811 OE1 GLN A 234 13.148 29.483 37.165 1.00 33.94 A O ANISOU 1811 OE1 GLN A 234 8702 2105 2088 -664 -615 546 A O ATOM 1812 N PHE A 235 15.704 33.652 37.550 1.00 38.38 A N ANISOU 1812 N PHE A 235 9290 2805 2490 -614 -926 285 A N ATOM 1813 CA PHE A 235 16.744 34.619 37.188 1.00 37.75 A C ANISOU 1813 CA PHE A 235 9126 2766 2452 -627 -1081 216 A C ATOM 1814 C PHE A 235 16.127 35.952 36.733 1.00 37.94 A C ANISOU 1814 C PHE A 235 9125 2812 2477 -635 -919 129 A C ATOM 1815 O PHE A 235 16.162 36.271 35.551 1.00 37.61 A O ANISOU 1815 O PHE A 235 8860 2825 2605 -612 -887 86 A O ATOM 1816 CB PHE A 235 17.667 34.036 36.089 1.00 37.79 A C ANISOU 1816 CB PHE A 235 8854 2828 2676 -581 -1223 219 A C ATOM 1817 CG PHE A 235 18.671 33.046 36.636 1.00 38.91 A C ANISOU 1817 CG PHE A 235 9033 2949 2803 -552 -1449 294 A C ATOM 1818 CD1 PHE A 235 18.366 31.693 36.722 1.00 39.43 A C ANISOU 1818 CD1 PHE A 235 9132 2954 2896 -499 -1437 369 A C ATOM 1819 CD2 PHE A 235 19.895 33.475 37.123 1.00 39.59 A C ANISOU 1819 CD2 PHE A 235 9137 3067 2839 -583 -1683 297 A C ATOM 1820 CE1 PHE A 235 19.272 30.797 37.287 1.00 40.50 A C ANISOU 1820 CE1 PHE A 235 9331 3051 3005 -450 -1652 446 A C ATOM 1821 CE2 PHE A 235 20.793 32.584 37.684 1.00 40.10 A C ANISOU 1821 CE2 PHE A 235 9232 3119 2884 -538 -1903 377 A C ATOM 1822 CZ PHE A 235 20.488 31.242 37.744 1.00 40.39 A C ANISOU 1822 CZ PHE A 235 9310 3087 2950 -457 -1885 451 A C ATOM 1823 N PRO A 236 15.623 36.764 37.692 1.00 38.02 A N ANISOU 1823 N PRO A 236 9392 2771 2283 -658 -825 102 A N ATOM 1824 CA PRO A 236 15.022 38.070 37.342 1.00 37.98 A C ANISOU 1824 CA PRO A 236 9405 2763 2262 -639 -671 18 A C ATOM 1825 C PRO A 236 15.853 38.968 36.436 1.00 37.98 A C ANISOU 1825 C PRO A 236 9264 2787 2380 -671 -789 -46 A C ATOM 1826 O PRO A 236 15.269 39.747 35.703 1.00 39.21 A O ANISOU 1826 O PRO A 236 9345 2950 2601 -632 -652 -96 A O ATOM 1827 CB PRO A 236 14.861 38.761 38.699 1.00 38.53 A C ANISOU 1827 CB PRO A 236 9831 2749 2059 -666 -642 -7 A C ATOM 1828 CG PRO A 236 14.674 37.604 39.663 1.00 39.34 A C ANISOU 1828 CG PRO A 236 10071 2834 2044 -676 -645 84 A C ATOM 1829 CD PRO A 236 15.513 36.480 39.139 1.00 37.56 A C ANISOU 1829 CD PRO A 236 9640 2646 1985 -688 -841 148 A C ATOM 1830 N VAL A 237 17.190 38.889 36.477 1.00 36.70 A N ANISOU 1830 N VAL A 237 9058 2642 2243 -742 -1040 -36 A N ATOM 1831 CA VAL A 237 18.063 39.741 35.664 1.00 35.70 A C ANISOU 1831 CA VAL A 237 8791 2553 2222 -802 -1155 -83 A C ATOM 1832 C VAL A 237 17.745 39.575 34.160 1.00 34.75 A C ANISOU 1832 C VAL A 237 8374 2505 2325 -739 -1044 -93 A C ATOM 1833 O VAL A 237 17.898 40.538 33.412 1.00 35.24 A O ANISOU 1833 O VAL A 237 8369 2575 2444 -769 -1025 -140 A O ATOM 1834 CB VAL A 237 19.562 39.461 35.964 1.00 35.96 A C ANISOU 1834 CB VAL A 237 8766 2630 2267 -886 -1444 -48 A C ATOM 1835 CG1 VAL A 237 19.965 38.049 35.541 1.00 35.87 A C ANISOU 1835 CG1 VAL A 237 8530 2693 2407 -810 -1514 22 A C ATOM 1836 CG2 VAL A 237 20.469 40.502 35.318 1.00 36.49 A C ANISOU 1836 CG2 VAL A 237 8723 2735 2407 -990 -1559 -91 A C ATOM 1837 N PHE A 238 17.260 38.377 33.721 1.00 33.07 A N ANISOU 1837 N PHE A 238 8012 2332 2220 -661 -970 -46 A N ATOM 1838 CA PHE A 238 16.943 38.163 32.311 1.00 31.62 A C ANISOU 1838 CA PHE A 238 7577 2212 2226 -608 -878 -59 A C ATOM 1839 C PHE A 238 15.700 38.943 31.891 1.00 32.25 A C ANISOU 1839 C PHE A 238 7678 2276 2301 -566 -668 -97 A C ATOM 1840 O PHE A 238 15.628 39.341 30.739 1.00 31.54 A O ANISOU 1840 O PHE A 238 7426 2227 2329 -549 -626 -124 A O ATOM 1841 CB PHE A 238 16.799 36.686 31.950 1.00 30.42 A C ANISOU 1841 CB PHE A 238 7293 2085 2179 -549 -877 -7 A C ATOM 1842 CG PHE A 238 18.127 35.963 31.964 1.00 30.31 A C ANISOU 1842 CG PHE A 238 7189 2104 2225 -546 -1084 25 A C ATOM 1843 CD1 PHE A 238 19.201 36.436 31.229 1.00 30.66 A C ANISOU 1843 CD1 PHE A 238 7061 2223 2365 -567 -1190 -1 A C ATOM 1844 CD2 PHE A 238 18.294 34.798 32.691 1.00 30.05 A C ANISOU 1844 CD2 PHE A 238 7235 2031 2152 -514 -1165 90 A C ATOM 1845 CE1 PHE A 238 20.425 35.777 31.253 1.00 30.12 A C ANISOU 1845 CE1 PHE A 238 6876 2208 2360 -543 -1371 36 A C ATOM 1846 CE2 PHE A 238 19.521 34.154 32.728 1.00 29.92 A C ANISOU 1846 CE2 PHE A 238 7130 2046 2192 -480 -1360 125 A C ATOM 1847 CZ PHE A 238 20.577 34.648 32.015 1.00 29.49 A C ANISOU 1847 CZ PHE A 238 6879 2085 2242 -488 -1460 97 A C ATOM 1848 N ALA A 239 14.761 39.238 32.811 1.00 33.46 A N ANISOU 1848 N ALA A 239 8031 2374 2310 -542 -535 -97 A N ATOM 1849 CA ALA A 239 13.611 40.093 32.475 1.00 34.60 A C ANISOU 1849 CA ALA A 239 8190 2510 2447 -475 -335 -131 A C ATOM 1850 C ALA A 239 14.102 41.498 32.075 1.00 36.11 A C ANISOU 1850 C ALA A 239 8438 2658 2622 -499 -380 -195 A C ATOM 1851 O ALA A 239 13.596 42.086 31.119 1.00 35.99 A O ANISOU 1851 O ALA A 239 8320 2661 2695 -447 -289 -217 A O ATOM 1852 CB ALA A 239 12.661 40.200 33.656 1.00 33.98 A C ANISOU 1852 CB ALA A 239 8327 2386 2196 -434 -180 -121 A C ATOM 1853 N CYS A 240 15.118 42.012 32.790 1.00 36.69 A N ANISOU 1853 N CYS A 240 8683 2673 2584 -592 -537 -218 A N ATOM 1854 CA CYS A 240 15.675 43.327 32.484 1.00 37.69 A C ANISOU 1854 CA CYS A 240 8892 2741 2686 -656 -602 -273 A C ATOM 1855 C CYS A 240 16.455 43.321 31.194 1.00 35.35 A C ANISOU 1855 C CYS A 240 8340 2523 2568 -707 -693 -264 A C ATOM 1856 O CYS A 240 16.415 44.315 30.464 1.00 35.25 A O ANISOU 1856 O CYS A 240 8328 2479 2587 -718 -658 -295 A O ATOM 1857 CB CYS A 240 16.536 43.829 33.633 1.00 41.23 A C ANISOU 1857 CB CYS A 240 9599 3108 2959 -771 -763 -296 A C ATOM 1858 SG CYS A 240 15.581 44.283 35.088 1.00 51.89 A S ANISOU 1858 SG CYS A 240 11334 4334 4047 -705 -621 -333 A S ATOM 1859 N ILE A 241 17.193 42.246 30.927 1.00 32.95 A N ANISOU 1859 N ILE A 241 7839 2312 2368 -731 -807 -221 A N ATOM 1860 CA ILE A 241 17.972 42.151 29.708 1.00 32.54 A C ANISOU 1860 CA ILE A 241 7537 2350 2477 -765 -873 -212 A C ATOM 1861 C ILE A 241 17.028 42.063 28.510 1.00 31.64 A C ANISOU 1861 C ILE A 241 7277 2270 2475 -669 -710 -217 A C ATOM 1862 O ILE A 241 17.154 42.845 27.580 1.00 31.78 A O ANISOU 1862 O ILE A 241 7234 2294 2545 -692 -688 -235 A O ATOM 1863 CB ILE A 241 18.957 40.951 29.794 1.00 33.28 A C ANISOU 1863 CB ILE A 241 7468 2531 2646 -776 -1021 -166 A C ATOM 1864 CG1 ILE A 241 20.105 41.290 30.794 1.00 34.20 A C ANISOU 1864 CG1 ILE A 241 7691 2636 2665 -897 -1228 -156 A C ATOM 1865 CG2 ILE A 241 19.500 40.545 28.415 1.00 33.36 A C ANISOU 1865 CG2 ILE A 241 7194 2648 2831 -754 -1026 -157 A C ATOM 1866 CD1 ILE A 241 20.784 40.024 31.317 1.00 36.12 A C ANISOU 1866 CD1 ILE A 241 7852 2937 2934 -864 -1368 -99 A C ATOM 1867 N ILE A 242 16.060 41.147 28.545 1.00 30.60 A N ANISOU 1867 N ILE A 242 7102 2155 2369 -574 -604 -196 A N ATOM 1868 CA ILE A 242 15.083 40.992 27.467 1.00 29.36 A C ANISOU 1868 CA ILE A 242 6805 2037 2312 -494 -470 -195 A C ATOM 1869 C ILE A 242 14.330 42.329 27.180 1.00 30.34 A C ANISOU 1869 C ILE A 242 7024 2109 2394 -456 -360 -225 A C ATOM 1870 O ILE A 242 14.236 42.730 26.026 1.00 31.44 A O ANISOU 1870 O ILE A 242 7054 2279 2615 -439 -334 -232 A O ATOM 1871 CB ILE A 242 14.117 39.851 27.819 1.00 27.84 A C ANISOU 1871 CB ILE A 242 6587 1860 2129 -435 -385 -160 A C ATOM 1872 CG1 ILE A 242 14.872 38.493 27.866 1.00 26.91 A C ANISOU 1872 CG1 ILE A 242 6382 1773 2069 -454 -500 -129 A C ATOM 1873 CG2 ILE A 242 12.968 39.786 26.829 1.00 28.47 A C ANISOU 1873 CG2 ILE A 242 6535 1986 2298 -368 -257 -156 A C ATOM 1874 CD1 ILE A 242 14.096 37.391 28.503 1.00 26.20 A C ANISOU 1874 CD1 ILE A 242 6334 1664 1955 -433 -443 -84 A C ATOM 1875 N MET A 243 13.846 43.011 28.220 1.00 29.98 A N ANISOU 1875 N MET A 243 7199 1979 2212 -432 -298 -243 A N ATOM 1876 CA MET A 243 13.120 44.277 28.128 1.00 30.97 A C ANISOU 1876 CA MET A 243 7457 2030 2279 -363 -188 -274 A C ATOM 1877 C MET A 243 13.998 45.356 27.488 1.00 29.82 A C ANISOU 1877 C MET A 243 7358 1832 2141 -446 -282 -301 A C ATOM 1878 O MET A 243 13.557 45.993 26.536 1.00 30.85 A O ANISOU 1878 O MET A 243 7443 1954 2324 -392 -220 -302 A O ATOM 1879 CB MET A 243 12.653 44.700 29.530 1.00 33.56 A C ANISOU 1879 CB MET A 243 8051 2266 2432 -324 -114 -297 A C ATOM 1880 CG MET A 243 11.852 45.988 29.557 1.00 41.33 A C ANISOU 1880 CG MET A 243 9205 3155 3341 -214 16 -335 A C ATOM 1881 SD MET A 243 10.165 45.791 28.936 1.00 57.97 A S ANISOU 1881 SD MET A 243 11128 5353 5544 -21 232 -298 A S ATOM 1882 CE MET A 243 9.344 46.295 30.232 1.00 53.13 A C ANISOU 1882 CE MET A 243 10760 4667 4760 96 396 -324 A C ATOM 1883 N SER A 244 15.253 45.527 27.975 1.00 28.14 A N ANISOU 1883 N SER A 244 7224 1592 1878 -590 -440 -311 A N ATOM 1884 CA ASER A 244 16.167 46.525 27.440 0.50 28.36 A C ANISOU 1884 CA ASER A 244 7291 1576 1909 -711 -537 -325 A C ATOM 1885 CA BSER A 244 16.195 46.509 27.445 0.50 28.20 A C ANISOU 1885 CA BSER A 244 7268 1558 1890 -714 -540 -324 A C ATOM 1886 C SER A 244 16.589 46.214 26.007 1.00 28.61 A C ANISOU 1886 C SER A 244 7058 1718 2095 -735 -553 -295 A C ATOM 1887 O SER A 244 16.686 47.144 25.210 1.00 29.09 A O ANISOU 1887 O SER A 244 7146 1738 2169 -769 -539 -296 A O ATOM 1888 CB ASER A 244 17.401 46.659 28.321 0.50 29.02 A C ANISOU 1888 CB ASER A 244 7479 1634 1912 -877 -717 -332 A C ATOM 1889 CB BSER A 244 17.455 46.568 28.298 0.50 28.40 A C ANISOU 1889 CB BSER A 244 7380 1567 1843 -880 -724 -328 A C ATOM 1890 OG ASER A 244 18.137 45.449 28.323 0.50 30.79 A O ANISOU 1890 OG ASER A 244 7487 1988 2222 -909 -817 -293 A O ATOM 1891 OG BSER A 244 17.134 46.708 29.669 0.50 29.37 A O ANISOU 1891 OG BSER A 244 7764 1593 1802 -864 -723 -357 A O ATOM 1892 N TYR A 245 16.865 44.928 25.675 1.00 27.81 A N ANISOU 1892 N TYR A 245 6728 1743 2097 -716 -581 -267 A N ATOM 1893 CA TYR A 245 17.281 44.575 24.313 1.00 27.50 A C ANISOU 1893 CA TYR A 245 6457 1807 2184 -724 -584 -247 A C ATOM 1894 C TYR A 245 16.151 44.823 23.330 1.00 27.87 A C ANISOU 1894 C TYR A 245 6471 1848 2270 -616 -454 -247 A C ATOM 1895 O TYR A 245 16.400 45.364 22.260 1.00 28.09 A O ANISOU 1895 O TYR A 245 6443 1894 2336 -647 -445 -238 A O ATOM 1896 CB TYR A 245 17.750 43.123 24.196 1.00 27.80 A C ANISOU 1896 CB TYR A 245 6296 1956 2310 -698 -632 -228 A C ATOM 1897 CG TYR A 245 19.154 42.832 24.689 1.00 28.77 A C ANISOU 1897 CG TYR A 245 6357 2134 2442 -798 -784 -212 A C ATOM 1898 CD1 TYR A 245 19.778 43.658 25.627 1.00 29.62 A C ANISOU 1898 CD1 TYR A 245 6619 2183 2455 -919 -889 -216 A C ATOM 1899 CD2 TYR A 245 19.833 41.690 24.275 1.00 28.60 A C ANISOU 1899 CD2 TYR A 245 6129 2220 2518 -761 -831 -192 A C ATOM 1900 CE1 TYR A 245 21.042 43.350 26.139 1.00 29.73 A C ANISOU 1900 CE1 TYR A 245 6552 2264 2479 -1013 -1053 -191 A C ATOM 1901 CE2 TYR A 245 21.111 41.402 24.740 1.00 28.90 A C ANISOU 1901 CE2 TYR A 245 6079 2326 2575 -827 -976 -168 A C ATOM 1902 CZ TYR A 245 21.697 42.208 25.700 1.00 29.63 A C ANISOU 1902 CZ TYR A 245 6300 2378 2580 -957 -1094 -162 A C ATOM 1903 OH TYR A 245 22.962 41.888 26.132 1.00 29.93 A O ANISOU 1903 OH TYR A 245 6220 2506 2648 -1025 -1257 -128 A O ATOM 1904 N SER A 246 14.905 44.494 23.692 1.00 28.26 A N ANISOU 1904 N SER A 246 6556 1880 2304 -495 -354 -248 A N ATOM 1905 CA SER A 246 13.772 44.714 22.795 1.00 29.08 A C ANISOU 1905 CA SER A 246 6604 1996 2450 -387 -249 -238 A C ATOM 1906 C SER A 246 13.583 46.219 22.561 1.00 29.52 A C ANISOU 1906 C SER A 246 6825 1948 2445 -374 -218 -246 A C ATOM 1907 O SER A 246 13.330 46.603 21.430 1.00 30.39 A O ANISOU 1907 O SER A 246 6875 2074 2598 -344 -196 -229 A O ATOM 1908 CB SER A 246 12.506 44.029 23.308 1.00 31.20 A C ANISOU 1908 CB SER A 246 6844 2288 2722 -278 -152 -225 A C ATOM 1909 OG SER A 246 11.917 44.741 24.378 1.00 35.28 A O ANISOU 1909 OG SER A 246 7552 2719 3134 -220 -78 -238 A O ATOM 1910 N PHE A 247 13.852 47.078 23.571 1.00 29.13 A N ANISOU 1910 N PHE A 247 7005 1779 2283 -413 -236 -272 A N ATOM 1911 CA PHE A 247 13.818 48.538 23.407 1.00 28.25 A C ANISOU 1911 CA PHE A 247 7102 1531 2100 -416 -224 -285 A C ATOM 1912 C PHE A 247 14.967 48.995 22.512 1.00 28.19 A C ANISOU 1912 C PHE A 247 7054 1531 2125 -575 -319 -267 A C ATOM 1913 O PHE A 247 14.764 49.863 21.664 1.00 28.33 A O ANISOU 1913 O PHE A 247 7134 1490 2141 -559 -293 -250 A O ATOM 1914 CB PHE A 247 13.919 49.273 24.758 1.00 28.72 A C ANISOU 1914 CB PHE A 247 7454 1445 2015 -439 -234 -328 A C ATOM 1915 CG PHE A 247 12.699 49.289 25.650 1.00 30.43 A C ANISOU 1915 CG PHE A 247 7788 1616 2157 -263 -98 -349 A C ATOM 1916 CD1 PHE A 247 11.458 48.899 25.167 1.00 32.30 A C ANISOU 1916 CD1 PHE A 247 7869 1934 2469 -89 30 -320 A C ATOM 1917 CD2 PHE A 247 12.803 49.634 26.988 1.00 30.78 A C ANISOU 1917 CD2 PHE A 247 8089 1552 2053 -278 -99 -393 A C ATOM 1918 CE1 PHE A 247 10.332 48.938 25.989 1.00 33.06 A C ANISOU 1918 CE1 PHE A 247 8045 2013 2503 74 175 -330 A C ATOM 1919 CE2 PHE A 247 11.680 49.675 27.802 1.00 31.79 A C ANISOU 1919 CE2 PHE A 247 8330 1649 2102 -106 55 -411 A C ATOM 1920 CZ PHE A 247 10.450 49.342 27.299 1.00 32.18 A C ANISOU 1920 CZ PHE A 247 8200 1790 2237 72 200 -376 A C ATOM 1921 N MET A 248 16.186 48.451 22.706 1.00 28.58 A N ANISOU 1921 N MET A 248 7002 1656 2202 -728 -429 -263 A N ATOM 1922 CA MET A 248 17.337 48.811 21.860 1.00 30.40 A C ANISOU 1922 CA MET A 248 7149 1929 2471 -889 -503 -236 A C ATOM 1923 C MET A 248 17.080 48.474 20.390 1.00 30.48 A C ANISOU 1923 C MET A 248 6973 2038 2571 -830 -439 -205 A C ATOM 1924 O MET A 248 17.381 49.293 19.521 1.00 30.54 A O ANISOU 1924 O MET A 248 7019 2014 2569 -901 -434 -178 A O ATOM 1925 CB MET A 248 18.618 48.095 22.302 1.00 33.03 A C ANISOU 1925 CB MET A 248 7339 2370 2840 -1025 -622 -229 A C ATOM 1926 CG MET A 248 19.327 48.748 23.480 1.00 39.72 A C ANISOU 1926 CG MET A 248 8377 3124 3589 -1173 -740 -246 A C ATOM 1927 SD MET A 248 20.565 47.563 24.111 1.00 57.98 A S ANISOU 1927 SD MET A 248 10473 5597 5960 -1260 -886 -226 A S ATOM 1928 CE MET A 248 21.685 48.716 24.859 1.00 58.92 A C ANISOU 1928 CE MET A 248 10768 5635 5985 -1517 -1055 -225 A C ATOM 1929 N PHE A 249 16.521 47.277 20.112 1.00 29.21 A N ANISOU 1929 N PHE A 249 6633 1984 2482 -711 -394 -207 A N ATOM 1930 CA PHE A 249 16.253 46.882 18.741 1.00 29.76 A C ANISOU 1930 CA PHE A 249 6549 2141 2616 -659 -347 -187 A C ATOM 1931 C PHE A 249 15.076 47.641 18.165 1.00 30.37 A C ANISOU 1931 C PHE A 249 6728 2146 2667 -546 -277 -172 A C ATOM 1932 O PHE A 249 15.084 47.937 16.985 1.00 28.85 A O ANISOU 1932 O PHE A 249 6501 1978 2484 -552 -262 -145 A O ATOM 1933 CB PHE A 249 16.025 45.365 18.617 1.00 29.18 A C ANISOU 1933 CB PHE A 249 6287 2182 2618 -582 -338 -198 A C ATOM 1934 CG PHE A 249 17.292 44.620 18.932 1.00 30.59 A C ANISOU 1934 CG PHE A 249 6348 2440 2834 -667 -411 -203 A C ATOM 1935 CD1 PHE A 249 18.485 44.970 18.330 1.00 31.86 A C ANISOU 1935 CD1 PHE A 249 6434 2662 3011 -782 -443 -185 A C ATOM 1936 CD2 PHE A 249 17.295 43.564 19.835 1.00 31.60 A C ANISOU 1936 CD2 PHE A 249 6434 2590 2982 -628 -446 -216 A C ATOM 1937 CE1 PHE A 249 19.668 44.295 18.651 1.00 32.96 A C ANISOU 1937 CE1 PHE A 249 6434 2896 3196 -841 -512 -182 A C ATOM 1938 CE2 PHE A 249 18.480 42.899 20.153 1.00 32.23 A C ANISOU 1938 CE2 PHE A 249 6405 2742 3098 -682 -527 -212 A C ATOM 1939 CZ PHE A 249 19.658 43.271 19.561 1.00 32.12 A C ANISOU 1939 CZ PHE A 249 6292 2802 3110 -779 -560 -196 A C ATOM 1940 N LEU A 250 14.069 47.968 18.976 1.00 32.01 A N ANISOU 1940 N LEU A 250 7060 2270 2834 -434 -231 -185 A N ATOM 1941 CA LEU A 250 12.925 48.738 18.505 1.00 34.58 A C ANISOU 1941 CA LEU A 250 7469 2530 3139 -296 -167 -164 A C ATOM 1942 C LEU A 250 13.395 50.130 18.030 1.00 34.94 A C ANISOU 1942 C LEU A 250 7707 2449 3120 -365 -189 -144 A C ATOM 1943 O LEU A 250 13.011 50.557 16.954 1.00 35.48 A O ANISOU 1943 O LEU A 250 7775 2512 3194 -315 -175 -106 A O ATOM 1944 CB LEU A 250 11.911 48.838 19.643 1.00 36.89 A C ANISOU 1944 CB LEU A 250 7857 2765 3396 -161 -97 -184 A C ATOM 1945 CG LEU A 250 10.503 49.362 19.371 1.00 40.76 A C ANISOU 1945 CG LEU A 250 8371 3228 3887 36 -13 -160 A C ATOM 1946 CD1 LEU A 250 9.924 48.776 18.101 1.00 41.23 A C ANISOU 1946 CD1 LEU A 250 8221 3413 4033 87 -22 -119 A C ATOM 1947 CD2 LEU A 250 9.586 48.991 20.555 1.00 42.31 A C ANISOU 1947 CD2 LEU A 250 8571 3437 4068 156 79 -177 A C ATOM 1948 N LEU A 251 14.358 50.731 18.730 1.00 34.66 A N ANISOU 1948 N LEU A 251 7823 2322 3023 -511 -242 -163 A N ATOM 1949 CA LEU A 251 14.933 52.028 18.375 1.00 35.12 A C ANISOU 1949 CA LEU A 251 8085 2244 3014 -626 -276 -140 A C ATOM 1950 C LEU A 251 15.822 51.923 17.121 1.00 32.93 A C ANISOU 1950 C LEU A 251 7668 2066 2778 -768 -304 -93 A C ATOM 1951 O LEU A 251 15.743 52.774 16.229 1.00 31.91 A O ANISOU 1951 O LEU A 251 7647 1864 2614 -783 -291 -48 A O ATOM 1952 CB LEU A 251 15.731 52.539 19.563 1.00 37.23 A C ANISOU 1952 CB LEU A 251 8538 2403 3207 -772 -345 -176 A C ATOM 1953 CG LEU A 251 16.489 53.817 19.370 1.00 43.40 A C ANISOU 1953 CG LEU A 251 9544 3032 3914 -950 -403 -155 A C ATOM 1954 CD1 LEU A 251 15.560 55.065 19.471 1.00 44.83 A C ANISOU 1954 CD1 LEU A 251 10048 2983 4001 -812 -352 -162 A C ATOM 1955 CD2 LEU A 251 17.623 53.914 20.386 1.00 45.89 A C ANISOU 1955 CD2 LEU A 251 9928 3322 4185 -1167 -514 -182 A C ATOM 1956 N LEU A 252 16.654 50.877 17.052 1.00 31.65 A N ANISOU 1956 N LEU A 252 7276 2067 2683 -858 -334 -100 A N ATOM 1957 CA LEU A 252 17.502 50.641 15.889 1.00 31.19 A C ANISOU 1957 CA LEU A 252 7061 2129 2661 -969 -332 -60 A C ATOM 1958 C LEU A 252 16.651 50.355 14.648 1.00 30.12 A C ANISOU 1958 C LEU A 252 6856 2047 2542 -832 -270 -37 A C ATOM 1959 O LEU A 252 16.931 50.923 13.598 1.00 30.16 A O ANISOU 1959 O LEU A 252 6899 2047 2512 -897 -252 11 A O ATOM 1960 CB LEU A 252 18.477 49.484 16.130 1.00 31.27 A C ANISOU 1960 CB LEU A 252 6832 2305 2743 -1039 -365 -78 A C ATOM 1961 CG LEU A 252 19.609 49.797 17.114 1.00 32.58 A C ANISOU 1961 CG LEU A 252 7025 2457 2895 -1219 -455 -81 A C ATOM 1962 CD1 LEU A 252 20.292 48.515 17.581 1.00 33.48 A C ANISOU 1962 CD1 LEU A 252 6909 2726 3086 -1215 -498 -100 A C ATOM 1963 CD2 LEU A 252 20.590 50.787 16.523 1.00 32.88 A C ANISOU 1963 CD2 LEU A 252 7107 2481 2905 -1432 -474 -27 A C ATOM 1964 N PHE A 253 15.588 49.545 14.769 1.00 29.07 A N ANISOU 1964 N PHE A 253 6639 1957 2448 -658 -245 -64 A N ATOM 1965 CA PHE A 253 14.714 49.242 13.627 1.00 28.66 A C ANISOU 1965 CA PHE A 253 6520 1961 2409 -539 -215 -41 A C ATOM 1966 C PHE A 253 13.842 50.445 13.239 1.00 29.73 A C ANISOU 1966 C PHE A 253 6845 1966 2485 -449 -204 2 A C ATOM 1967 O PHE A 253 13.511 50.576 12.060 1.00 30.12 A O ANISOU 1967 O PHE A 253 6887 2043 2514 -412 -202 43 A O ATOM 1968 CB PHE A 253 13.844 48.013 13.863 1.00 27.38 A C ANISOU 1968 CB PHE A 253 6204 1888 2311 -412 -207 -74 A C ATOM 1969 CG PHE A 253 14.544 46.718 13.516 1.00 28.07 A C ANISOU 1969 CG PHE A 253 6105 2109 2449 -464 -216 -102 A C ATOM 1970 CD1 PHE A 253 15.543 46.206 14.331 1.00 28.33 A C ANISOU 1970 CD1 PHE A 253 6076 2176 2512 -546 -238 -130 A C ATOM 1971 CD2 PHE A 253 14.236 46.035 12.345 1.00 28.52 A C ANISOU 1971 CD2 PHE A 253 6066 2253 2516 -422 -210 -101 A C ATOM 1972 CE1 PHE A 253 16.175 45.002 14.011 1.00 29.20 A C ANISOU 1972 CE1 PHE A 253 6023 2400 2671 -558 -242 -155 A C ATOM 1973 CE2 PHE A 253 14.877 44.844 12.027 1.00 28.62 A C ANISOU 1973 CE2 PHE A 253 5942 2368 2565 -447 -209 -136 A C ATOM 1974 CZ PHE A 253 15.849 44.342 12.853 1.00 28.49 A C ANISOU 1974 CZ PHE A 253 5859 2379 2587 -504 -219 -162 A C ATOM 1975 N LEU A 254 13.482 51.318 14.190 1.00 30.08 A N ANISOU 1975 N LEU A 254 7076 1862 2490 -402 -200 -6 A N ATOM 1976 CA LEU A 254 12.748 52.545 13.839 1.00 31.18 A C ANISOU 1976 CA LEU A 254 7425 1852 2569 -298 -190 37 A C ATOM 1977 C LEU A 254 13.695 53.476 13.092 1.00 30.89 A C ANISOU 1977 C LEU A 254 7538 1733 2464 -468 -214 86 A C ATOM 1978 O LEU A 254 13.274 54.047 12.097 1.00 32.39 A O ANISOU 1978 O LEU A 254 7812 1879 2615 -410 -216 145 A O ATOM 1979 CB LEU A 254 12.104 53.240 15.045 1.00 32.57 A C ANISOU 1979 CB LEU A 254 7789 1878 2710 -179 -162 7 A C ATOM 1980 CG LEU A 254 10.866 52.509 15.605 1.00 34.79 A C ANISOU 1980 CG LEU A 254 7930 2240 3047 25 -110 -16 A C ATOM 1981 CD1 LEU A 254 10.567 52.970 17.001 1.00 34.43 A C ANISOU 1981 CD1 LEU A 254 8054 2075 2954 99 -62 -62 A C ATOM 1982 CD2 LEU A 254 9.649 52.693 14.703 1.00 35.31 A C ANISOU 1982 CD2 LEU A 254 7941 2338 3138 219 -99 39 A C ATOM 1983 N HIS A 255 14.988 53.558 13.484 1.00 29.96 A N ANISOU 1983 N HIS A 255 7432 1616 2336 -688 -239 73 A N ATOM 1984 CA HIS A 255 15.966 54.354 12.728 1.00 30.59 A C ANISOU 1984 CA HIS A 255 7615 1648 2359 -889 -252 132 A C ATOM 1985 C HIS A 255 16.132 53.744 11.318 1.00 30.24 A C ANISOU 1985 C HIS A 255 7396 1766 2329 -901 -219 174 A C ATOM 1986 O HIS A 255 16.199 54.472 10.338 1.00 30.56 A O ANISOU 1986 O HIS A 255 7561 1750 2301 -948 -209 243 A O ATOM 1987 CB HIS A 255 17.319 54.422 13.452 1.00 32.43 A C ANISOU 1987 CB HIS A 255 7831 1895 2597 -1133 -293 116 A C ATOM 1988 CG HIS A 255 18.404 55.032 12.622 1.00 35.93 A C ANISOU 1988 CG HIS A 255 8303 2347 3001 -1369 -293 186 A C ATOM 1989 CD2 HIS A 255 19.391 54.431 11.918 1.00 37.30 A C ANISOU 1989 CD2 HIS A 255 8250 2711 3212 -1507 -263 214 A C ATOM 1990 ND1 HIS A 255 18.482 56.407 12.429 1.00 38.97 A N ANISOU 1990 ND1 HIS A 255 8986 2525 3294 -1473 -312 241 A N ATOM 1991 CE1 HIS A 255 19.510 56.596 11.617 1.00 39.64 A C ANISOU 1991 CE1 HIS A 255 9006 2690 3364 -1695 -293 308 A C ATOM 1992 NE2 HIS A 255 20.080 55.429 11.271 1.00 39.82 A N ANISOU 1992 NE2 HIS A 255 8704 2963 3464 -1713 -254 294 A N ATOM 1993 N PHE A 256 16.147 52.402 11.210 1.00 29.27 A N ANISOU 1993 N PHE A 256 7014 1829 2278 -849 -203 132 A N ATOM 1994 CA PHE A 256 16.232 51.726 9.923 1.00 28.32 A C ANISOU 1994 CA PHE A 256 6752 1852 2155 -839 -170 152 A C ATOM 1995 C PHE A 256 15.026 52.090 9.073 1.00 28.93 A C ANISOU 1995 C PHE A 256 6932 1876 2185 -679 -180 194 A C ATOM 1996 O PHE A 256 15.215 52.493 7.930 1.00 29.59 A O ANISOU 1996 O PHE A 256 7086 1963 2194 -729 -165 253 A O ATOM 1997 CB PHE A 256 16.337 50.187 10.064 1.00 27.50 A C ANISOU 1997 CB PHE A 256 6395 1921 2133 -786 -159 88 A C ATOM 1998 CG PHE A 256 16.264 49.496 8.715 1.00 27.47 A C ANISOU 1998 CG PHE A 256 6294 2038 2104 -750 -127 96 A C ATOM 1999 CD1 PHE A 256 17.360 49.461 7.877 1.00 28.27 A C ANISOU 1999 CD1 PHE A 256 6344 2231 2166 -880 -69 121 A C ATOM 2000 CD2 PHE A 256 15.065 48.978 8.243 1.00 27.96 A C ANISOU 2000 CD2 PHE A 256 6335 2121 2168 -593 -153 84 A C ATOM 2001 CE1 PHE A 256 17.286 48.830 6.632 1.00 29.25 A C ANISOU 2001 CE1 PHE A 256 6415 2458 2241 -838 -29 119 A C ATOM 2002 CE2 PHE A 256 14.987 48.387 6.982 1.00 28.39 A C ANISOU 2002 CE2 PHE A 256 6341 2271 2176 -572 -140 87 A C ATOM 2003 CZ PHE A 256 16.100 48.297 6.194 1.00 28.23 A C ANISOU 2003 CZ PHE A 256 6293 2330 2102 -687 -73 98 A C ATOM 2004 N TRP A 257 13.785 51.975 9.617 1.00 28.61 A N ANISOU 2004 N TRP A 257 6897 1793 2181 -489 -206 171 A N ATOM 2005 CA TRP A 257 12.570 52.337 8.877 1.00 29.18 A C ANISOU 2005 CA TRP A 257 7036 1828 2222 -319 -234 219 A C ATOM 2006 C TRP A 257 12.658 53.775 8.354 1.00 30.30 A C ANISOU 2006 C TRP A 257 7445 1803 2265 -346 -245 299 A C ATOM 2007 O TRP A 257 12.342 54.033 7.197 1.00 30.58 A O ANISOU 2007 O TRP A 257 7538 1844 2237 -311 -268 362 A O ATOM 2008 CB TRP A 257 11.315 52.205 9.755 1.00 28.32 A C ANISOU 2008 CB TRP A 257 6890 1695 2175 -119 -244 194 A C ATOM 2009 CG TRP A 257 10.041 52.466 8.991 1.00 27.46 A C ANISOU 2009 CG TRP A 257 6791 1588 2055 67 -286 250 A C ATOM 2010 CD1 TRP A 257 9.622 53.644 8.420 1.00 27.47 A C ANISOU 2010 CD1 TRP A 257 6995 1459 1985 153 -315 326 A C ATOM 2011 CD2 TRP A 257 9.042 51.496 8.689 1.00 27.15 A C ANISOU 2011 CD2 TRP A 257 6545 1693 2077 181 -322 243 A C ATOM 2012 CE2 TRP A 257 8.057 52.134 7.904 1.00 27.87 A C ANISOU 2012 CE2 TRP A 257 6699 1756 2135 333 -380 319 A C ATOM 2013 CE3 TRP A 257 8.882 50.142 9.014 1.00 26.78 A C ANISOU 2013 CE3 TRP A 257 6275 1789 2109 160 -319 186 A C ATOM 2014 NE1 TRP A 257 8.445 53.444 7.740 1.00 27.40 A N ANISOU 2014 NE1 TRP A 257 6897 1523 1992 324 -373 370 A N ATOM 2015 CZ2 TRP A 257 6.922 51.463 7.453 1.00 28.20 A C ANISOU 2015 CZ2 TRP A 257 6559 1928 2226 452 -445 339 A C ATOM 2016 CZ3 TRP A 257 7.760 49.488 8.562 1.00 27.62 A C ANISOU 2016 CZ3 TRP A 257 6229 2006 2260 264 -375 202 A C ATOM 2017 CH2 TRP A 257 6.809 50.138 7.767 1.00 27.74 A C ANISOU 2017 CH2 TRP A 257 6283 2011 2245 399 -442 278 A C ATOM 2018 N TYR A 258 13.126 54.681 9.206 1.00 30.97 A N ANISOU 2018 N TYR A 258 7710 1729 2327 -422 -236 296 A N ATOM 2019 CA TYR A 258 13.268 56.083 8.870 1.00 31.87 A C ANISOU 2019 CA TYR A 258 8119 1643 2345 -468 -250 368 A C ATOM 2020 C TYR A 258 14.190 56.295 7.676 1.00 33.66 A C ANISOU 2020 C TYR A 258 8382 1912 2497 -663 -235 438 A C ATOM 2021 O TYR A 258 13.790 57.030 6.760 1.00 35.89 A O ANISOU 2021 O TYR A 258 8841 2103 2695 -614 -256 520 A O ATOM 2022 CB TYR A 258 13.772 56.879 10.088 1.00 31.66 A C ANISOU 2022 CB TYR A 258 8286 1441 2302 -562 -251 335 A C ATOM 2023 CG TYR A 258 13.980 58.361 9.819 1.00 32.72 A C ANISOU 2023 CG TYR A 258 8772 1331 2331 -635 -272 406 A C ATOM 2024 CD1 TYR A 258 12.911 59.190 9.516 1.00 34.10 A C ANISOU 2024 CD1 TYR A 258 9157 1342 2456 -414 -291 455 A C ATOM 2025 CD2 TYR A 258 15.240 58.932 9.896 1.00 33.81 A C ANISOU 2025 CD2 TYR A 258 9031 1397 2420 -926 -279 430 A C ATOM 2026 CE1 TYR A 258 13.094 60.549 9.280 1.00 36.07 A C ANISOU 2026 CE1 TYR A 258 9766 1337 2601 -472 -315 523 A C ATOM 2027 CE2 TYR A 258 15.436 60.291 9.666 1.00 35.94 A C ANISOU 2027 CE2 TYR A 258 9650 1419 2586 -1020 -304 500 A C ATOM 2028 CZ TYR A 258 14.360 61.097 9.362 1.00 37.68 A C ANISOU 2028 CZ TYR A 258 10113 1453 2749 -787 -322 544 A C ATOM 2029 OH TYR A 258 14.557 62.429 9.122 1.00 43.35 A O ANISOU 2029 OH TYR A 258 11209 1902 3359 -873 -351 616 A O ATOM 2030 N ARG A 259 15.409 55.703 7.657 1.00 33.37 A N ANISOU 2030 N ARG A 259 8186 2011 2483 -875 -195 414 A N ATOM 2031 CA ARG A 259 16.294 56.004 6.533 1.00 34.52 A C ANISOU 2031 CA ARG A 259 8371 2198 2545 -1063 -154 490 A C ATOM 2032 C ARG A 259 16.006 55.152 5.323 1.00 33.87 A C ANISOU 2032 C ARG A 259 8146 2286 2436 -984 -128 500 A C ATOM 2033 O ARG A 259 16.097 55.677 4.225 1.00 34.13 A O ANISOU 2033 O ARG A 259 8315 2293 2361 -1036 -112 583 A O ATOM 2034 CB ARG A 259 17.783 55.998 6.879 1.00 36.73 A C ANISOU 2034 CB ARG A 259 8566 2545 2844 -1337 -113 488 A C ATOM 2035 CG ARG A 259 18.287 54.804 7.533 1.00 39.56 A C ANISOU 2035 CG ARG A 259 8636 3085 3310 -1348 -97 403 A C ATOM 2036 CD ARG A 259 19.774 54.701 7.285 1.00 41.93 A C ANISOU 2036 CD ARG A 259 8798 3518 3614 -1599 -40 433 A C ATOM 2037 NE ARG A 259 20.172 53.296 7.412 1.00 42.46 A N ANISOU 2037 NE ARG A 259 8557 3805 3772 -1545 -5 363 A N ATOM 2038 CZ ARG A 259 20.507 52.520 6.390 1.00 41.39 A C ANISOU 2038 CZ ARG A 259 8263 3843 3619 -1527 78 365 A C ATOM 2039 NH1 ARG A 259 20.574 53.022 5.155 1.00 39.59 A N1+ ANISOU 2039 NH1 ARG A 259 8147 3615 3280 -1583 142 441 A N1+ ATOM 2040 NH2 ARG A 259 20.814 51.247 6.595 1.00 39.17 A N ANISOU 2040 NH2 ARG A 259 7735 3727 3420 -1451 102 294 A N ATOM 2041 N ALA A 260 15.568 53.905 5.496 1.00 32.80 A N ANISOU 2041 N ALA A 260 7781 2301 2382 -857 -134 421 A N ATOM 2042 CA ALA A 260 15.282 53.033 4.374 1.00 32.73 A C ANISOU 2042 CA ALA A 260 7661 2439 2336 -790 -123 417 A C ATOM 2043 C ALA A 260 13.962 53.366 3.650 1.00 33.14 A C ANISOU 2043 C ALA A 260 7835 2429 2328 -609 -202 467 A C ATOM 2044 O ALA A 260 13.894 53.191 2.427 1.00 33.03 A O ANISOU 2044 O ALA A 260 7853 2480 2215 -611 -204 506 A O ATOM 2045 CB ALA A 260 15.251 51.577 4.844 1.00 32.10 A C ANISOU 2045 CB ALA A 260 7322 2513 2360 -727 -117 316 A C ATOM 2046 N TYR A 261 12.913 53.803 4.381 1.00 32.95 A N ANISOU 2046 N TYR A 261 7869 2294 2357 -443 -268 468 A N ATOM 2047 CA TYR A 261 11.608 54.018 3.748 1.00 32.73 A C ANISOU 2047 CA TYR A 261 7900 2241 2296 -247 -355 519 A C ATOM 2048 C TYR A 261 11.176 55.471 3.783 1.00 34.85 A C ANISOU 2048 C TYR A 261 8439 2296 2505 -168 -391 606 A C ATOM 2049 O TYR A 261 10.865 56.024 2.723 1.00 35.99 A O ANISOU 2049 O TYR A 261 8737 2394 2542 -130 -441 696 A O ATOM 2050 CB TYR A 261 10.523 53.131 4.390 1.00 31.10 A C ANISOU 2050 CB TYR A 261 7485 2124 2209 -74 -401 457 A C ATOM 2051 CG TYR A 261 10.910 51.670 4.504 1.00 29.72 A C ANISOU 2051 CG TYR A 261 7073 2123 2098 -145 -373 367 A C ATOM 2052 CD1 TYR A 261 11.504 51.004 3.447 1.00 29.65 A C ANISOU 2052 CD1 TYR A 261 7024 2224 2016 -244 -355 356 A C ATOM 2053 CD2 TYR A 261 10.662 50.953 5.663 1.00 29.50 A C ANISOU 2053 CD2 TYR A 261 6883 2136 2189 -102 -358 293 A C ATOM 2054 CE1 TYR A 261 11.883 49.670 3.555 1.00 29.93 A C ANISOU 2054 CE1 TYR A 261 6873 2393 2105 -289 -326 269 A C ATOM 2055 CE2 TYR A 261 11.000 49.608 5.768 1.00 29.43 A C ANISOU 2055 CE2 TYR A 261 6686 2262 2236 -158 -340 217 A C ATOM 2056 CZ TYR A 261 11.615 48.968 4.712 1.00 29.73 A C ANISOU 2056 CZ TYR A 261 6695 2394 2207 -244 -326 202 A C ATOM 2057 OH TYR A 261 11.957 47.640 4.815 1.00 29.41 A O ANISOU 2057 OH TYR A 261 6498 2463 2216 -278 -307 123 A O ATOM 2058 N THR A 262 11.188 56.116 4.964 1.00 34.69 A N ANISOU 2058 N THR A 262 8511 2132 2536 -142 -370 582 A N ATOM 2059 CA THR A 262 10.765 57.512 5.071 1.00 35.55 A C ANISOU 2059 CA THR A 262 8916 2007 2585 -45 -401 655 A C ATOM 2060 C THR A 262 11.697 58.410 4.235 1.00 37.31 A C ANISOU 2060 C THR A 262 9390 2113 2675 -247 -386 743 A C ATOM 2061 O THR A 262 11.235 59.350 3.572 1.00 37.56 A O ANISOU 2061 O THR A 262 9662 1996 2613 -160 -438 841 A O ATOM 2062 CB THR A 262 10.695 57.905 6.555 1.00 35.42 A C ANISOU 2062 CB THR A 262 8962 1861 2634 6 -368 590 A C ATOM 2063 CG2 THR A 262 10.192 59.310 6.766 1.00 34.84 A C ANISOU 2063 CG2 THR A 262 9216 1523 2498 142 -393 648 A C ATOM 2064 OG1 THR A 262 9.881 56.947 7.253 1.00 35.59 A O ANISOU 2064 OG1 THR A 262 8729 2024 2771 167 -362 517 A O ATOM 2065 N LYS A 263 13.008 58.123 4.249 1.00 38.50 A N ANISOU 2065 N LYS A 263 9479 2336 2815 -515 -316 720 A N ATOM 2066 CA ALYS A 263 13.978 58.893 3.460 0.50 39.72 A C ANISOU 2066 CA ALYS A 263 9832 2412 2847 -746 -281 811 A C ATOM 2067 CA BLYS A 263 13.979 58.892 3.462 0.50 39.61 A C ANISOU 2067 CA BLYS A 263 9818 2399 2834 -746 -281 811 A C ATOM 2068 C LYS A 263 14.330 58.204 2.122 1.00 40.87 A C ANISOU 2068 C LYS A 263 9863 2751 2916 -825 -243 847 A C ATOM 2069 O LYS A 263 15.097 58.760 1.339 1.00 41.57 A O ANISOU 2069 O LYS A 263 10099 2805 2889 -1014 -195 933 A O ATOM 2070 CB ALYS A 263 15.255 59.157 4.266 0.50 41.49 A C ANISOU 2070 CB ALYS A 263 10066 2600 3098 -1014 -223 783 A C ATOM 2071 CB BLYS A 263 15.260 59.155 4.270 0.50 41.06 A C ANISOU 2071 CB BLYS A 263 10011 2546 3044 -1015 -223 782 A C ATOM 2072 CG ALYS A 263 15.109 60.304 5.261 0.50 45.01 A C ANISOU 2072 CG ALYS A 263 10789 2773 3538 -1007 -265 785 A C ATOM 2073 CG BLYS A 263 15.034 59.966 5.550 0.50 43.96 A C ANISOU 2073 CG BLYS A 263 10566 2689 3446 -974 -263 747 A C ATOM 2074 CD ALYS A 263 16.232 60.304 6.278 0.50 49.64 A C ANISOU 2074 CD ALYS A 263 11326 3360 4175 -1252 -241 728 A C ATOM 2075 CD BLYS A 263 14.441 61.338 5.280 0.50 47.65 A C ANISOU 2075 CD BLYS A 263 11420 2874 3813 -881 -314 836 A C ATOM 2076 CE ALYS A 263 17.571 60.713 5.720 0.50 54.01 A C ANISOU 2076 CE ALYS A 263 11923 3934 4663 -1594 -195 805 A C ATOM 2077 CE BLYS A 263 15.400 62.446 5.602 0.50 51.07 A C ANISOU 2077 CE BLYS A 263 12138 3092 4174 -1149 -311 881 A C ATOM 2078 NZ ALYS A 263 18.651 60.574 6.735 0.50 56.15 A N1+ ANISOU 2078 NZ ALYS A 263 12082 4251 5003 -1828 -194 750 A N1+ ATOM 2079 NZ BLYS A 263 14.750 63.771 5.447 0.50 55.00 A N1+ ANISOU 2079 NZ BLYS A 263 13050 3275 4574 -1027 -367 959 A N1+ ATOM 2080 N GLY A 264 13.764 57.019 1.875 1.00 41.23 A N ANISOU 2080 N GLY A 264 9666 2986 3015 -688 -262 783 A N ATOM 2081 CA GLY A 264 13.910 56.231 0.657 1.00 41.87 A C ANISOU 2081 CA GLY A 264 9650 3243 3015 -717 -239 792 A C ATOM 2082 C GLY A 264 15.281 55.713 0.289 1.00 41.67 A C ANISOU 2082 C GLY A 264 9510 3365 2958 -946 -111 773 A C ATOM 2083 O GLY A 264 15.562 55.572 -0.898 1.00 42.07 A O ANISOU 2083 O GLY A 264 9610 3496 2879 -1006 -66 820 A O ATOM 2084 N GLN A 265 16.125 55.370 1.276 1.00 40.67 A N ANISOU 2084 N GLN A 265 9219 3291 2944 -1061 -49 704 A N ATOM 2085 CA GLN A 265 17.463 54.872 0.971 1.00 39.94 A C ANISOU 2085 CA GLN A 265 8977 3360 2839 -1260 78 692 A C ATOM 2086 C GLN A 265 17.471 53.408 0.556 1.00 39.36 A C ANISOU 2086 C GLN A 265 8667 3497 2790 -1172 117 602 A C ATOM 2087 O GLN A 265 18.355 53.007 -0.200 1.00 39.79 A O ANISOU 2087 O GLN A 265 8649 3691 2777 -1279 233 609 A O ATOM 2088 CB GLN A 265 18.408 55.083 2.140 1.00 41.31 A C ANISOU 2088 CB GLN A 265 9059 3519 3119 -1421 107 664 A C ATOM 2089 CG GLN A 265 18.889 56.536 2.221 1.00 45.67 A C ANISOU 2089 CG GLN A 265 9865 3886 3602 -1615 106 768 A C ATOM 2090 CD GLN A 265 19.802 56.761 3.393 1.00 51.92 A C ANISOU 2090 CD GLN A 265 10578 4659 4489 -1796 107 740 A C ATOM 2091 NE2 GLN A 265 19.896 58.014 3.817 1.00 54.04 A N ANISOU 2091 NE2 GLN A 265 11107 4707 4719 -1921 58 801 A N ATOM 2092 OE1 GLN A 265 20.426 55.833 3.932 1.00 53.16 A O ANISOU 2092 OE1 GLN A 265 10460 4989 4750 -1824 139 665 A O ATOM 2093 N ARG A 266 16.517 52.600 1.049 1.00 37.93 A N ANISOU 2093 N ARG A 266 8373 3338 2701 -983 32 518 A N ATOM 2094 CA ARG A 266 16.476 51.181 0.717 1.00 37.75 A C ANISOU 2094 CA ARG A 266 8159 3482 2701 -905 54 427 A C ATOM 2095 C ARG A 266 15.028 50.713 0.470 1.00 38.51 A C ANISOU 2095 C ARG A 266 8270 3564 2800 -711 -73 402 A C ATOM 2096 O ARG A 266 14.564 49.764 1.089 1.00 38.04 A O ANISOU 2096 O ARG A 266 8050 3555 2847 -618 -116 318 A O ATOM 2097 CB ARG A 266 17.141 50.342 1.822 1.00 36.74 A C ANISOU 2097 CB ARG A 266 7799 3437 2722 -929 93 336 A C ATOM 2098 CG ARG A 266 18.523 50.824 2.226 1.00 36.40 A C ANISOU 2098 CG ARG A 266 7704 3422 2704 -1124 187 367 A C ATOM 2099 CD ARG A 266 19.163 49.867 3.238 1.00 37.90 A C ANISOU 2099 CD ARG A 266 7651 3714 3034 -1124 205 281 A C ATOM 2100 NE ARG A 266 19.412 48.551 2.657 1.00 36.41 A N ANISOU 2100 NE ARG A 266 7310 3682 2844 -1043 268 209 A N ATOM 2101 CZ ARG A 266 20.470 48.243 1.915 1.00 37.08 A C ANISOU 2101 CZ ARG A 266 7307 3906 2875 -1117 400 217 A C ATOM 2102 NH1 ARG A 266 21.412 49.151 1.675 1.00 35.41 A N1+ ANISOU 2102 NH1 ARG A 266 7117 3719 2619 -1301 484 303 A N1+ ATOM 2103 NH2 ARG A 266 20.592 47.027 1.397 1.00 36.93 A N ANISOU 2103 NH2 ARG A 266 7187 4003 2843 -1010 456 139 A N ATOM 2104 N LEU A 267 14.311 51.411 -0.409 1.00 39.52 A N ANISOU 2104 N LEU A 267 8587 3619 2808 -659 -142 484 A N ATOM 2105 CA LEU A 267 12.929 51.093 -0.772 1.00 41.33 A C ANISOU 2105 CA LEU A 267 8824 3849 3028 -487 -283 484 A C ATOM 2106 C LEU A 267 12.860 49.760 -1.490 1.00 44.22 A C ANISOU 2106 C LEU A 267 9087 4362 3354 -469 -289 404 A C ATOM 2107 O LEU A 267 13.829 49.379 -2.154 1.00 44.07 A O ANISOU 2107 O LEU A 267 9079 4424 3243 -570 -176 382 A O ATOM 2108 CB LEU A 267 12.376 52.193 -1.713 1.00 41.28 A C ANISOU 2108 CB LEU A 267 9066 3740 2877 -449 -357 607 A C ATOM 2109 CG LEU A 267 12.138 53.566 -1.114 1.00 42.77 A C ANISOU 2109 CG LEU A 267 9417 3743 3091 -418 -386 691 A C ATOM 2110 CD1 LEU A 267 11.774 54.576 -2.185 1.00 42.92 A C ANISOU 2110 CD1 LEU A 267 9705 3658 2944 -392 -450 821 A C ATOM 2111 CD2 LEU A 267 11.078 53.507 -0.020 1.00 43.19 A C ANISOU 2111 CD2 LEU A 267 9358 3754 3300 -240 -470 655 A C ATOM 2112 N PRO A 268 11.712 49.053 -1.444 1.00 46.61 A N ANISOU 2112 N PRO A 268 9301 4700 3708 -346 -418 365 A N ATOM 2113 CA PRO A 268 11.596 47.816 -2.238 1.00 48.20 A C ANISOU 2113 CA PRO A 268 9458 5013 3844 -345 -445 290 A C ATOM 2114 C PRO A 268 11.713 48.125 -3.734 1.00 51.16 A C ANISOU 2114 C PRO A 268 10038 5403 3997 -381 -454 346 A C ATOM 2115 O PRO A 268 11.375 49.221 -4.194 1.00 50.66 A O ANISOU 2115 O PRO A 268 10140 5262 3846 -364 -508 457 A O ATOM 2116 CB PRO A 268 10.218 47.276 -1.874 1.00 48.35 A C ANISOU 2116 CB PRO A 268 9362 5048 3961 -231 -607 269 A C ATOM 2117 CG PRO A 268 9.467 48.447 -1.379 1.00 48.80 A C ANISOU 2117 CG PRO A 268 9456 5012 4074 -139 -674 365 A C ATOM 2118 CD PRO A 268 10.456 49.375 -0.735 1.00 46.77 A C ANISOU 2118 CD PRO A 268 9268 4663 3839 -207 -542 394 A C ATOM 2119 N LYS A 269 12.244 47.174 -4.484 1.00 53.81 A N ANISOU 2119 N LYS A 269 10387 5829 4231 -426 -391 270 A N ATOM 2120 CA LYS A 269 12.475 47.348 -5.912 1.00 56.52 A C ANISOU 2120 CA LYS A 269 10940 6197 4337 -469 -371 310 A C ATOM 2121 C LYS A 269 11.218 46.971 -6.704 1.00 57.25 A C ANISOU 2121 C LYS A 269 11116 6300 4335 -394 -581 313 A C ATOM 2122 O LYS A 269 10.526 47.852 -7.216 1.00 57.77 A O ANISOU 2122 O LYS A 269 11321 6314 4316 -355 -703 424 A O ATOM 2123 CB LYS A 269 13.691 46.501 -6.344 1.00 60.33 A C ANISOU 2123 CB LYS A 269 11406 6776 4740 -537 -181 219 A C ATOM 2124 CG LYS A 269 14.890 46.711 -5.428 1.00 66.82 A C ANISOU 2124 CG LYS A 269 12078 7617 5693 -608 -1 210 A C ATOM 2125 CD LYS A 269 16.176 46.195 -6.023 1.00 73.81 A C ANISOU 2125 CD LYS A 269 12955 8612 6477 -668 210 162 A C ATOM 2126 CE LYS A 269 17.364 46.809 -5.318 1.00 79.61 A C ANISOU 2126 CE LYS A 269 13565 9374 7311 -774 370 207 A C ATOM 2127 NZ LYS A 269 18.620 46.068 -5.615 1.00 83.53 A N1+ ANISOU 2127 NZ LYS A 269 13954 10009 7774 -798 578 142 A N1+ TER END If you find results from this site helpful for your research, please cite one of our papers:
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