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Copy path4wy4-original_and_AF_aligned.pdb
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4wy4-original_and_AF_aligned.pdb
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HELIX 1 1 ASP A 11 ASN A 73 1 63
HELIX 2 2 TRP B 172 SER B 195 1 24
HELIX 3 3 GLN B 196 TYR B 227 1 32
HELIX 4 4 ASP C 40 SER C 114 1 75
HELIX 5 5 LEU D 195 ARG D 256 1 62
MODEL 1
ATOM 1 N ASP A 11 -11.734 -13.315 59.860 1.00 71.70 N
ATOM 2 CA ASP A 11 -11.000 -12.111 59.474 1.00 59.00 C
ATOM 3 C ASP A 11 -11.881 -11.215 58.619 1.00 65.41 C
ATOM 4 O ASP A 11 -12.078 -11.484 57.433 1.00 77.78 O
ATOM 5 CB ASP A 11 -9.725 -12.475 58.710 1.00 43.89 C
ATOM 6 CG ASP A 11 -9.091 -13.751 59.216 1.00 46.02 C
ATOM 7 OD1 ASP A 11 -9.079 -13.964 60.450 1.00 69.71 O
ATOM 8 OD2 ASP A 11 -8.609 -14.548 58.375 1.00 70.88 O
ATOM 9 N ARG A 12 -12.405 -10.149 59.215 1.00 67.05 N
ANISOU 9 N ARG A 12 8482 9544 7451 150 473 2022 N
ATOM 10 CA ARG A 12 -13.429 -9.345 58.560 1.00 65.40 C
ANISOU 10 CA ARG A 12 8603 9443 6803 40 242 2083 C
ATOM 11 C ARG A 12 -12.839 -8.405 57.504 1.00 61.65 C
ANISOU 11 C ARG A 12 8915 9755 4754 -203 -176 2054 C
ATOM 12 O ARG A 12 -13.438 -8.194 56.444 1.00 60.14 O
ANISOU 12 O ARG A 12 8916 9883 4051 -335 -379 2454 O
ATOM 13 CB ARG A 12 -14.236 -8.561 59.608 1.00 65.42 C
ATOM 14 CG ARG A 12 -14.920 -9.460 60.636 1.00 63.70 C
ATOM 15 CD ARG A 12 -15.924 -10.431 60.011 0.19 34.74 C
ATOM 16 NE ARG A 12 -16.463 -9.999 58.725 0.46 48.17 N
ATOM 17 CZ ARG A 12 -16.401 -10.710 57.604 0.45 41.80 C
ATOM 18 NH1 ARG A 12 -16.936 -10.226 56.485 0.57 59.38 N
ATOM 19 NH2 ARG A 12 -15.789 -11.887 57.595 0.67 59.63 N
ATOM 20 N VAL A 13 -11.658 -7.862 57.781 1.00 58.51 N
ANISOU 20 N VAL A 13 9057 9526 3648 -106 -586 1903 N
ATOM 21 CA VAL A 13 -10.999 -6.993 56.806 1.00 56.40 C
ANISOU 21 CA VAL A 13 9143 9183 3105 165 -952 1499 C
ATOM 22 C VAL A 13 -10.670 -7.797 55.552 1.00 55.98 C
ANISOU 22 C VAL A 13 9160 9242 2866 244 -1228 1266 C
ATOM 23 O VAL A 13 -10.937 -7.348 54.440 1.00 54.44 O
ANISOU 23 O VAL A 13 8969 8968 2748 202 -1293 1085 O
ATOM 24 CB VAL A 13 -9.708 -6.356 57.372 1.00 55.56 C
ANISOU 24 CB VAL A 13 9138 9018 2956 404 -1125 1044 C
ATOM 25 CG1 VAL A 13 -9.124 -5.350 56.381 1.00 55.25 C
ANISOU 25 CG1 VAL A 13 9141 8814 3039 511 -1104 865 C
ATOM 26 CG2 VAL A 13 -9.992 -5.696 58.721 1.00 54.62 C
ANISOU 26 CG2 VAL A 13 9053 8865 2835 518 -1253 1095 C
ATOM 27 N ARG A 14 -10.127 -8.997 55.731 1.00 56.41 N
ANISOU 27 N ARG A 14 9212 9254 2968 350 -1285 1427 N
ATOM 28 CA ARG A 14 -9.754 -9.857 54.607 1.00 57.79 C
ANISOU 28 CA ARG A 14 9275 9562 3119 419 -1236 1603 C
ATOM 29 C ARG A 14 -10.977 -10.261 53.784 1.00 57.96 C
ANISOU 29 C ARG A 14 9274 9565 3182 195 -1044 1663 C
ATOM 30 O ARG A 14 -10.896 -10.370 52.562 1.00 56.87 O
ANISOU 30 O ARG A 14 9234 9216 3160 355 -1247 1786 O
ATOM 31 CB ARG A 14 -9.028 -11.108 55.105 1.00 58.97 C
ANISOU 31 CB ARG A 14 9306 9927 3174 591 -1312 1436 C
ATOM 32 N ASN A 15 -12.110 -10.461 54.455 1.00 55.56 N
ANISOU 32 N ASN A 15 9188 8638 3284 -198 -666 1710 N
ATOM 33 CA ASN A 15 -13.350 -10.844 53.791 1.00 54.79 C
ANISOU 33 CA ASN A 15 9073 8300 3444 -520 -408 1412 C
ATOM 34 C ASN A 15 -13.940 -9.716 52.921 1.00 50.36 C
ANISOU 34 C ASN A 15 8668 7331 3136 -563 -285 1373 C
ATOM 35 O ASN A 15 -14.315 -9.945 51.757 1.00 48.45 O
ANISOU 35 O ASN A 15 8690 6659 3060 -434 -428 1542 O
ATOM 36 CB ASN A 15 -14.391 -11.288 54.820 1.00 58.58 C
ANISOU 36 CB ASN A 15 9334 9048 3875 -829 -291 1134 C
ATOM 37 CG ASN A 15 -15.650 -11.828 54.173 0.76 62.38 C
ANISOU 37 CG ASN A 15 9571 9924 4208 -1168 -175 1154 C
ATOM 38 OD1 ASN A 15 -16.479 -11.064 53.675 0.68 63.46 O
ANISOU 38 OD1 ASN A 15 9654 10117 4342 -1338 -163 1207 O
ATOM 39 ND2 ASN A 15 -15.822 -13.149 54.212 0.79 63.48 N
ANISOU 39 ND2 ASN A 15 9649 10110 4360 -1284 -132 1267 N
ATOM 40 N LEU A 16 -14.041 -8.503 53.468 1.00 47.14 N
ANISOU 40 N LEU A 16 8219 6676 3017 -482 -131 890 N
ATOM 41 CA LEU A 16 -14.473 -7.364 52.656 1.00 45.15 C
ANISOU 41 CA LEU A 16 7809 6403 2942 -84 -156 382 C
ATOM 42 C LEU A 16 -13.475 -7.121 51.536 1.00 40.95 C
ANISOU 42 C LEU A 16 7390 5828 2343 145 -321 347 C
ATOM 43 O LEU A 16 -13.871 -6.755 50.421 1.00 37.16 O
ANISOU 43 O LEU A 16 7243 4951 1924 147 -299 488 O
ATOM 44 CB LEU A 16 -14.642 -6.090 53.491 1.00 46.92 C
ANISOU 44 CB LEU A 16 7795 6702 3331 112 -48 168 C
ATOM 45 CG LEU A 16 -16.061 -5.751 53.968 1.00 49.06 C
ANISOU 45 CG LEU A 16 7784 7110 3746 512 -61 118 C
ATOM 46 CD1 LEU A 16 -16.098 -4.456 54.778 1.00 49.18 C
ANISOU 46 CD1 LEU A 16 7743 7019 3925 755 -78 79 C
ATOM 47 CD2 LEU A 16 -17.024 -5.682 52.800 1.00 50.16 C
ANISOU 47 CD2 LEU A 16 7809 7335 3915 483 -52 240 C
ATOM 48 N GLN A 17 -12.188 -7.336 51.802 1.00 40.79 N
ANISOU 48 N GLN A 17 7130 6063 2304 346 -501 702 N
ATOM 49 CA GLN A 17 -11.180 -7.131 50.759 1.00 40.26 C
ANISOU 49 CA GLN A 17 6799 6012 2485 791 -979 1163 C
ATOM 50 C GLN A 17 -11.426 -8.117 49.633 1.00 39.54 C
ANISOU 50 C GLN A 17 6742 5664 2618 737 -1036 1159 C
ATOM 51 O GLN A 17 -11.250 -7.772 48.464 1.00 38.12 O
ANISOU 51 O GLN A 17 6511 5398 2573 694 -967 961 O
ATOM 52 CB GLN A 17 -9.751 -7.278 51.314 1.00 45.17 C
ANISOU 52 CB GLN A 17 6592 7635 2935 954 -1251 817 C
ATOM 53 CG GLN A 17 -9.231 -6.009 51.999 1.00 49.07 C
ANISOU 53 CG GLN A 17 6435 8922 3286 842 -1392 796 C
ATOM 54 CD GLN A 17 -7.750 -6.081 52.366 1.00 53.21 C
ANISOU 54 CD GLN A 17 6503 10098 3617 596 -1294 1006 C
ATOM 55 OE1 GLN A 17 -6.914 -5.372 51.793 1.00 55.03 O
ANISOU 55 OE1 GLN A 17 6498 10471 3941 685 -1153 992 O
ATOM 56 NE2 GLN A 17 -7.425 -6.929 53.326 1.00 52.74 N
ANISOU 56 NE2 GLN A 17 6419 10169 3450 409 -1523 1168 N
ATOM 57 N SER A 18 -11.880 -9.323 49.968 1.00 40.56 N
ANISOU 57 N SER A 18 7008 5699 2704 437 -912 1261 N
ATOM 58 CA SER A 18 -12.149 -10.327 48.940 1.00 40.96 C
ANISOU 58 CA SER A 18 7139 5413 3010 267 -763 1213 C
ATOM 59 C SER A 18 -13.350 -9.906 48.117 1.00 38.91 C
ANISOU 59 C SER A 18 6897 5092 2795 -118 -634 1176 C
ATOM 60 O SER A 18 -13.409 -10.163 46.904 1.00 37.65 O
ANISOU 60 O SER A 18 6969 4770 2568 62 -750 884 O
ATOM 61 CB SER A 18 -12.392 -11.708 49.553 1.00 42.70 C
ANISOU 61 CB SER A 18 7348 5499 3375 598 -898 1685 C
ATOM 62 OG SER A 18 -11.250 -12.163 50.261 1.00 47.21 O
ANISOU 62 OG SER A 18 7519 6676 3741 562 -814 1359 O
ATOM 63 N GLU A 19 -14.314 -9.246 48.747 1.00 38.46 N
ANISOU 63 N GLU A 19 6494 5363 2755 -613 -489 1124 N
ATOM 64 CA GLU A 19 -15.468 -8.767 47.988 1.00 39.34 C
ANISOU 64 CA GLU A 19 6126 5795 3026 -913 -485 1116 C
ATOM 65 C GLU A 19 -15.034 -7.656 47.029 1.00 34.75 C
ANISOU 65 C GLU A 19 5535 5106 2563 -749 -529 910 C
ATOM 66 O GLU A 19 -15.430 -7.642 45.855 1.00 35.13 O
ANISOU 66 O GLU A 19 5392 5588 2369 -408 -688 1152 O
ATOM 67 CB GLU A 19 -16.576 -8.265 48.909 1.00 45.14 C
ANISOU 67 CB GLU A 19 6381 7081 3691 -1200 -379 1466 C
ATOM 68 CG GLU A 19 -17.205 -9.338 49.790 1.00 52.16 C
ANISOU 68 CG GLU A 19 6694 8859 4266 -1112 -340 1737 C
ATOM 69 CD GLU A 19 -17.817 -10.487 48.999 0.60 58.71 C
ANISOU 69 CD GLU A 19 6965 10588 4753 -943 -338 1725 C
ATOM 70 OE1 GLU A 19 -18.419 -10.230 47.936 0.66 61.08 O
ANISOU 70 OE1 GLU A 19 7032 11263 4911 -899 -321 1696 O
ATOM 71 OE2 GLU A 19 -17.712 -11.647 49.454 0.64 61.18 O
ANISOU 71 OE2 GLU A 19 7078 11205 4961 -878 -374 1638 O
ATOM 72 N VAL A 20 -14.203 -6.723 47.497 1.00 32.41 N
ANISOU 72 N VAL A 20 5117 4747 2452 -539 -480 708 N
ATOM 73 CA VAL A 20 -13.721 -5.659 46.618 1.00 29.31 C
ANISOU 73 CA VAL A 20 4680 4132 2325 -265 -548 424 C
ATOM 74 C VAL A 20 -12.956 -6.283 45.461 1.00 27.86 C
ANISOU 74 C VAL A 20 4382 4107 2098 56 -833 493 C
ATOM 75 O VAL A 20 -13.109 -5.860 44.313 1.00 27.09 O
ANISOU 75 O VAL A 20 4019 4312 1963 -78 -933 511 O
ATOM 76 CB VAL A 20 -12.798 -4.643 47.354 1.00 30.63 C
ANISOU 76 CB VAL A 20 4811 4390 2435 -197 -337 148 C
ATOM 77 CG1 VAL A 20 -12.210 -3.618 46.337 1.00 29.99 C
ANISOU 77 CG1 VAL A 20 4816 4250 2330 -296 -386 287 C
ATOM 78 CG2 VAL A 20 -13.546 -3.930 48.474 1.00 32.21 C
ANISOU 78 CG2 VAL A 20 4914 4676 2647 -6 -316 96 C
ATOM 79 N GLU A 21 -12.165 -7.314 45.740 1.00 28.42 N
ANISOU 79 N GLU A 21 4612 4064 2122 328 -818 421 N
ATOM 80 CA GLU A 21 -11.317 -7.904 44.710 1.00 30.17 C
ANISOU 80 CA GLU A 21 5006 4238 2221 728 -796 13 C
ATOM 81 C GLU A 21 -12.203 -8.568 43.624 1.00 29.60 C
ANISOU 81 C GLU A 21 5047 4136 2063 536 -821 250 C
ATOM 82 O GLU A 21 -11.906 -8.508 42.422 1.00 28.96 O
ANISOU 82 O GLU A 21 5167 3930 1907 640 -781 378 O
ATOM 83 CB GLU A 21 -10.321 -8.912 45.328 1.00 34.00 C
ANISOU 83 CB GLU A 21 5443 4786 2690 1481 -614 297 C
ATOM 84 CG GLU A 21 -9.650 -9.793 44.292 1.00 41.81 C
ANISOU 84 CG GLU A 21 5886 6633 3366 1950 -407 255 C
ATOM 85 CD GLU A 21 -9.363 -11.215 44.746 0.48 51.12 C
ANISOU 85 CD GLU A 21 6361 9082 3980 1831 -46 17 C
ATOM 86 OE1 GLU A 21 -9.662 -11.582 45.904 0.56 54.38 O
ANISOU 86 OE1 GLU A 21 6579 9842 4240 1558 111 -186 O
ATOM 87 OE2 GLU A 21 -8.856 -11.983 43.901 0.62 55.14 O
ANISOU 87 OE2 GLU A 21 6509 10129 4315 2034 118 147 O
ATOM 88 N GLY A 22 -13.328 -9.142 44.039 1.00 29.44 N
ANISOU 88 N GLY A 22 5109 3903 2175 377 -709 573 N
ATOM 89 CA GLY A 22 -14.248 -9.754 43.095 1.00 27.78 C
ANISOU 89 CA GLY A 22 4870 3393 2293 158 -791 538 C
ATOM 90 C GLY A 22 -14.873 -8.728 42.154 1.00 27.35 C
ANISOU 90 C GLY A 22 4634 3421 2337 -222 -654 572 C
ATOM 91 O GLY A 22 -15.017 -8.986 40.949 1.00 29.29 O
ANISOU 91 O GLY A 22 4671 4133 2325 -185 -796 690 O
ATOM 92 N VAL A 23 -15.269 -7.573 42.682 1.00 25.95 N
ANISOU 92 N VAL A 23 4192 3393 2276 -385 -531 496 N
ATOM 93 CA VAL A 23 -15.814 -6.508 41.832 1.00 24.00 C
ANISOU 93 CA VAL A 23 3668 3215 2234 -183 -483 524 C
ATOM 94 C VAL A 23 -14.716 -5.947 40.952 1.00 22.92 C
ANISOU 94 C VAL A 23 3320 3364 2024 32 -670 459 C
ATOM 95 O VAL A 23 -14.957 -5.689 39.772 1.00 24.66 O
ANISOU 95 O VAL A 23 3656 3886 1826 25 -744 481 O
ATOM 96 CB VAL A 23 -16.449 -5.360 42.643 1.00 24.92 C
ANISOU 96 CB VAL A 23 3317 3665 2486 -176 -413 389 C
ATOM 97 CG1 VAL A 23 -17.038 -4.293 41.718 1.00 24.77 C
ANISOU 97 CG1 VAL A 23 3145 3806 2461 39 -549 424 C
ATOM 98 CG2 VAL A 23 -17.509 -5.902 43.587 1.00 26.90 C
ANISOU 98 CG2 VAL A 23 3272 4211 2739 -331 -286 440 C
ATOM 99 N LYS A 24 -13.509 -5.777 41.486 1.00 24.28 N
ANISOU 99 N LYS A 24 3146 3829 2250 -131 -639 407 N
ATOM 100 CA LYS A 24 -12.388 -5.309 40.684 1.00 24.86 C
ANISOU 100 CA LYS A 24 3118 3777 2551 34 -925 300 C
ATOM 101 C LYS A 24 -12.107 -6.226 39.519 1.00 23.40 C
ANISOU 101 C LYS A 24 3340 3360 2189 430 -757 695 C
ATOM 102 O LYS A 24 -11.904 -5.750 38.392 1.00 23.34 O
ANISOU 102 O LYS A 24 3252 3935 1679 171 -723 740 O
ATOM 103 CB LYS A 24 -11.129 -5.201 41.558 1.00 27.38 C
ATOM 104 CG LYS A 24 -9.896 -4.736 40.820 1.00 32.90 C
ATOM 105 CD LYS A 24 -8.594 -5.082 41.549 0.37 24.77 C
ATOM 106 CE LYS A 24 -8.301 -6.557 41.460 0.33 22.85 C
ATOM 107 NZ LYS A 24 -6.832 -6.827 41.537 0.13 27.34 N
ATOM 108 N ASN A 25 -12.127 -7.536 39.756 1.00 25.06 N
ANISOU 108 N ASN A 25 3800 3440 2282 649 -703 548 N
ATOM 109 CA ASN A 25 -11.909 -8.491 38.662 1.00 26.42 C
ANISOU 109 CA ASN A 25 4054 3621 2366 528 -705 572 C
ATOM 110 C ASN A 25 -12.958 -8.383 37.551 1.00 25.56 C
ANISOU 110 C ASN A 25 3943 3665 2103 287 -623 699 C
ATOM 111 O ASN A 25 -12.609 -8.418 36.357 1.00 25.98 O
ANISOU 111 O ASN A 25 4094 3696 2082 130 -370 683 O
ATOM 112 CB ASN A 25 -11.862 -9.914 39.206 1.00 28.57 C
ANISOU 112 CB ASN A 25 4304 3829 2724 877 -828 842 C
ATOM 113 CG ASN A 25 -10.591 -10.189 39.987 1.00 32.86 C
ANISOU 113 CG ASN A 25 4581 4806 3098 732 -722 970 C
ATOM 114 OD1 ASN A 25 -9.605 -9.449 39.882 1.00 34.71 O
ANISOU 114 OD1 ASN A 25 4453 5426 3311 652 -843 860 O
ATOM 115 ND2 ASN A 25 -10.598 -11.263 40.749 1.00 35.38 N
ANISOU 115 ND2 ASN A 25 4929 5424 3088 745 -598 1379 N
ATOM 116 N ILE A 26 -14.235 -8.245 37.930 1.00 23.85 N
ANISOU 116 N ILE A 26 3757 3265 2041 -225 -644 496 N
ATOM 117 CA ILE A 26 -15.287 -8.079 36.919 1.00 22.66 C
ANISOU 117 CA ILE A 26 3619 2838 2151 -386 -611 386 C
ATOM 118 C ILE A 26 -15.075 -6.756 36.174 1.00 22.00 C
ANISOU 118 C ILE A 26 3274 3106 1978 -314 -566 336 C
ATOM 119 O ILE A 26 -15.201 -6.705 34.939 1.00 22.14 O
ANISOU 119 O ILE A 26 3266 3372 1775 -227 -372 357 O
ATOM 120 CB ILE A 26 -16.696 -8.106 37.545 1.00 24.02 C
ANISOU 120 CB ILE A 26 3683 3128 2317 -503 -520 578 C
ATOM 121 CG1 ILE A 26 -16.948 -9.428 38.289 1.00 25.99 C
ANISOU 121 CG1 ILE A 26 3768 3527 2580 -684 -267 533 C
ATOM 122 CG2 ILE A 26 -17.777 -7.915 36.448 1.00 24.84 C
ANISOU 122 CG2 ILE A 26 3779 3460 2200 -223 -480 538 C
ATOM 123 CD1 ILE A 26 -18.092 -9.374 39.315 1.00 27.53 C
ANISOU 123 CD1 ILE A 26 3840 3834 2787 -610 -198 389 C
ATOM 124 N MET A 27 -14.739 -5.685 36.886 1.00 21.57 N
ANISOU 124 N MET A 27 3056 3038 2100 -316 -673 601 N
ATOM 125 CA MET A 27 -14.541 -4.396 36.220 1.00 20.87 C
ANISOU 125 CA MET A 27 2927 2938 2064 -140 -598 315 C
ATOM 126 C MET A 27 -13.317 -4.373 35.317 1.00 21.21 C
ANISOU 126 C MET A 27 2934 3183 1943 -24 -631 313 C
ATOM 127 O MET A 27 -13.343 -3.729 34.268 1.00 21.38 O
ANISOU 127 O MET A 27 2904 3380 1841 77 -591 472 O
ATOM 128 CB MET A 27 -14.457 -3.252 37.243 1.00 20.96 C
ANISOU 128 CB MET A 27 2956 2918 2087 -38 -656 -20 C
ATOM 129 CG MET A 27 -15.785 -2.851 37.886 1.00 21.82 C
ANISOU 129 CG MET A 27 3024 3322 1946 188 -801 267 C
ATOM 130 SD MET A 27 -17.067 -2.412 36.667 1.00 21.95 S
ANISOU 130 SD MET A 27 3037 3327 1977 44 -691 176 S
ATOM 131 CE MET A 27 -16.247 -1.150 35.669 1.00 22.41 C
ANISOU 131 CE MET A 27 3310 3179 2028 -157 -574 571 C
ATOM 132 N THR A 28 -12.262 -5.086 35.677 1.00 21.78 N
ANISOU 132 N THR A 28 2940 3469 1866 -76 -611 405 N
ATOM 133 CA THR A 28 -11.093 -5.188 34.822 1.00 22.97 C
ANISOU 133 CA THR A 28 2959 3803 1964 322 -757 536 C
ATOM 134 C THR A 28 -11.489 -5.860 33.494 1.00 22.45 C
ANISOU 134 C THR A 28 3090 3478 1964 52 -662 478 C
ATOM 135 O THR A 28 -11.092 -5.399 32.418 1.00 22.37 O
ANISOU 135 O THR A 28 3164 3355 1979 212 -641 501 O
ATOM 136 CB THR A 28 -9.961 -5.961 35.513 1.00 24.57 C
ANISOU 136 CB THR A 28 3169 4105 2062 453 -723 505 C
ATOM 137 OG1 THR A 28 -9.568 -5.244 36.694 1.00 25.64 O
ANISOU 137 OG1 THR A 28 3392 4238 2111 213 -695 252 O
ATOM 138 CG2 THR A 28 -8.772 -6.083 34.601 1.00 27.83 C
ANISOU 138 CG2 THR A 28 3194 4997 2380 741 -526 171 C
ATOM 139 N GLN A 29 -12.285 -6.931 33.578 1.00 22.09 N
ANISOU 139 N GLN A 29 3249 3091 2054 -2 -745 157 N
ATOM 140 CA GLN A 29 -12.752 -7.598 32.372 1.00 23.42 C
ANISOU 140 CA GLN A 29 3389 3172 2336 -23 -860 240 C
ATOM 141 C GLN A 29 -13.655 -6.650 31.582 1.00 21.79 C
ANISOU 141 C GLN A 29 3028 3232 2021 -45 -781 161 C
ATOM 142 O GLN A 29 -13.576 -6.605 30.336 1.00 21.73 O
ANISOU 142 O GLN A 29 3194 3188 1875 -33 -475 342 O
ATOM 143 CB GLN A 29 -13.502 -8.888 32.684 1.00 26.17 C
ANISOU 143 CB GLN A 29 3841 3034 3070 -306 -900 206 C
ATOM 144 CG GLN A 29 -13.869 -9.644 31.387 1.00 31.87 C
ANISOU 144 CG GLN A 29 4228 3896 3986 -501 -763 405 C
ATOM 145 CD GLN A 29 -14.871 -10.761 31.593 0.59 36.75 C
ANISOU 145 CD GLN A 29 4518 4661 4784 -576 -703 458 C
ATOM 146 OE1 GLN A 29 -16.074 -10.552 31.467 0.75 39.33 O
ANISOU 146 OE1 GLN A 29 4724 5108 5110 -691 -633 255 O
ATOM 147 NE2 GLN A 29 -14.378 -11.963 31.877 0.63 38.34 N
ANISOU 147 NE2 GLN A 29 4598 4882 5087 -405 -701 706 N
ATOM 148 N ASN A 30 -14.505 -5.899 32.281 1.00 19.95 N
ANISOU 148 N ASN A 30 2886 2825 1868 -34 -650 325 N
ATOM 149 CA ASN A 30 -15.403 -4.952 31.608 1.00 20.30 C
ANISOU 149 CA ASN A 30 2767 3067 1880 -188 -483 245 C
ATOM 150 C ASN A 30 -14.606 -3.900 30.847 1.00 19.53 C
ANISOU 150 C ASN A 30 2593 3029 1797 -403 -471 355 C
ATOM 151 O ASN A 30 -14.973 -3.536 29.735 1.00 19.56 O
ANISOU 151 O ASN A 30 2655 3076 1700 -55 -573 384 O
ATOM 152 CB ASN A 30 -16.341 -4.263 32.604 1.00 20.50 C
ANISOU 152 CB ASN A 30 2698 3237 1854 -360 -335 278 C
ATOM 153 CG ASN A 30 -17.469 -5.167 33.098 1.00 20.55 C
ANISOU 153 CG ASN A 30 2930 3148 1728 -427 -455 68 C
ATOM 154 OD1 ASN A 30 -17.822 -6.163 32.470 1.00 21.76 O
ANISOU 154 OD1 ASN A 30 3189 3319 1760 -538 -437 260 O
ATOM 155 ND2 ASN A 30 -18.032 -4.812 34.244 1.00 20.39 N
ANISOU 155 ND2 ASN A 30 2882 3173 1692 -207 -365 111 N
ATOM 156 N VAL A 31 -13.510 -3.398 31.399 1.00 19.62 N
ANISOU 156 N VAL A 31 2614 2966 1873 -243 -381 270 N
ATOM 157 CA VAL A 31 -12.676 -2.439 30.681 1.00 18.80 C
ANISOU 157 CA VAL A 31 2543 2591 2010 -49 -602 124 C
ATOM 158 C VAL A 31 -12.027 -3.100 29.451 1.00 19.40 C
ANISOU 158 C VAL A 31 2568 2762 2043 -4 -706 473 C
ATOM 159 O VAL A 31 -12.029 -2.522 28.361 1.00 19.86 O
ANISOU 159 O VAL A 31 2513 3053 1981 65 -712 768 O
ATOM 160 CB VAL A 31 -11.588 -1.826 31.617 1.00 21.00 C
ANISOU 160 CB VAL A 31 2628 3228 2123 -11 -593 198 C
ATOM 161 CG1 VAL A 31 -10.561 -1.034 30.790 1.00 22.15 C
ANISOU 161 CG1 VAL A 31 2649 3650 2117 -456 -642 309 C
ATOM 162 CG2 VAL A 31 -12.274 -0.926 32.631 1.00 21.81 C
ANISOU 162 CG2 VAL A 31 2898 3264 2126 -59 -545 286 C
ATOM 163 N GLU A 32 -11.488 -4.313 29.604 1.00 20.02 N
ANISOU 163 N GLU A 32 2663 2898 2046 230 -686 299 N
ATOM 164 CA GLU A 32 -10.921 -5.029 28.473 1.00 20.99 C
ANISOU 164 CA GLU A 32 2838 2905 2234 213 -492 -236 C
ATOM 165 C GLU A 32 -11.958 -5.178 27.365 1.00 21.47 C
ANISOU 165 C GLU A 32 2925 3245 1986 -151 -479 195 C
ATOM 166 O GLU A 32 -11.682 -4.912 26.176 1.00 22.14 O
ANISOU 166 O GLU A 32 3088 3486 1837 35 -438 517 O
ATOM 167 CB GLU A 32 -10.436 -6.409 28.892 1.00 22.27 C
ATOM 168 CG GLU A 32 -9.152 -6.408 29.740 0.57 39.03 C
ATOM 169 CD GLU A 32 -8.979 -7.676 30.572 0.56 69.72 C
ATOM 170 OE1 GLU A 32 -9.789 -8.615 30.423 0.63 40.64 O
ATOM 171 OE2 GLU A 32 -8.016 -7.743 31.365 0.81 68.98 O
ATOM 172 N ARG A 33 -13.160 -5.601 27.741 1.00 21.91 N
ANISOU 172 N ARG A 33 3041 3386 1899 132 -620 258 N
ATOM 173 CA ARG A 33 -14.198 -5.830 26.732 1.00 22.06 C
ANISOU 173 CA ARG A 33 3226 3118 2037 -102 -817 528 C
ATOM 174 C ARG A 33 -14.734 -4.535 26.121 1.00 20.06 C
ANISOU 174 C ARG A 33 2991 2758 1872 -180 -613 395 C
ATOM 175 O ARG A 33 -15.047 -4.501 24.910 1.00 20.17 O
ANISOU 175 O ARG A 33 3164 2706 1795 -265 -824 488 O
ATOM 176 CB ARG A 33 -15.326 -6.629 27.351 1.00 24.61 C
ANISOU 176 CB ARG A 33 3696 3124 2531 -251 -926 622 C
ATOM 177 CG ARG A 33 -14.877 -8.015 27.760 1.00 28.31 C
ANISOU 177 CG ARG A 33 4284 3446 3025 87 -847 877 C
ATOM 178 CD ARG A 33 -14.853 -8.998 26.632 1.00 34.74 C
ANISOU 178 CD ARG A 33 4741 4822 3638 154 -472 608 C
ATOM 179 NE ARG A 33 -16.121 -9.720 26.630 0.18 38.29 N
ANISOU 179 NE ARG A 33 4913 5824 3812 310 -381 382 N
ATOM 180 CZ ARG A 33 -17.215 -9.322 25.992 0.69 40.23 C
ANISOU 180 CZ ARG A 33 5069 6375 3843 505 -331 381 C
ATOM 181 NH1 ARG A 33 -17.203 -8.221 25.252 0.19 41.36 N
ANISOU 181 NH1 ARG A 33 5168 6581 3968 658 -256 440 N
ATOM 182 NH2 ARG A 33 -18.325 -10.040 26.079 0.73 40.63 N
ANISOU 182 NH2 ARG A 33 4890 6758 3789 643 -350 344 N
ATOM 183 N ILE A 34 -14.781 -3.438 26.871 1.00 17.87 N
ANISOU 183 N ILE A 34 2563 2424 1804 -106 -645 279 N
ATOM 184 CA ILE A 34 -15.234 -2.167 26.285 1.00 18.49 C
ANISOU 184 CA ILE A 34 2563 2539 1925 -35 -558 141 C
ATOM 185 C ILE A 34 -14.159 -1.590 25.371 1.00 18.47 C
ANISOU 185 C ILE A 34 2399 2798 1823 -153 -819 83 C
ATOM 186 O ILE A 34 -14.484 -0.938 24.358 1.00 17.87 O
ANISOU 186 O ILE A 34 2584 2560 1645 -167 -764 119 O
ATOM 187 CB ILE A 34 -15.687 -1.114 27.380 1.00 19.24 C
ANISOU 187 CB ILE A 34 2466 2854 1991 -172 -560 155 C
ATOM 188 CG1 ILE A 34 -16.846 -0.250 26.842 1.00 19.84 C
ANISOU 188 CG1 ILE A 34 2247 3157 2136 -66 -526 460 C
ATOM 189 CG2 ILE A 34 -14.510 -0.256 27.901 1.00 20.12 C
ANISOU 189 CG2 ILE A 34 2641 2943 2059 -325 -668 0 C
ATOM 190 CD1 ILE A 34 -18.153 -1.024 26.687 1.00 21.76 C
ANISOU 190 CD1 ILE A 34 2198 3935 2132 -391 -574 168 C
ATOM 191 N LEU A 35 -12.883 -1.872 25.623 1.00 19.16 N
ANISOU 191 N LEU A 35 2433 2976 1873 -222 -828 293 N
ATOM 192 CA LEU A 35 -11.817 -1.451 24.704 1.00 19.65 C
ANISOU 192 CA LEU A 35 2399 3093 1973 -228 -834 169 C
ATOM 193 C LEU A 35 -11.967 -2.172 23.361 1.00 18.49 C
ANISOU 193 C LEU A 35 2547 2606 1874 -142 -886 104 C
ATOM 194 O LEU A 35 -11.870 -1.561 22.288 1.00 18.98 O
ANISOU 194 O LEU A 35 2556 2836 1820 -169 -724 454 O
ATOM 195 CB LEU A 35 -10.428 -1.737 25.300 1.00 21.22 C
ANISOU 195 CB LEU A 35 2473 3566 2023 -200 -949 53 C
ATOM 196 CG LEU A 35 -10.043 -0.817 26.466 1.00 21.52 C
ANISOU 196 CG LEU A 35 2754 3480 1942 -265 -941 341 C
ATOM 197 CD1 LEU A 35 -8.814 -1.333 27.205 1.00 23.19 C
ANISOU 197 CD1 LEU A 35 2765 3801 2246 -79 -1133 493 C
ATOM 198 CD2 LEU A 35 -9.809 0.607 25.991 1.00 20.88 C
ANISOU 198 CD2 LEU A 35 2930 2878 2123 -460 -648 180 C
ATOM 199 N ALA A 36 -12.234 -3.464 23.418 1.00 18.91 N
ANISOU 199 N ALA A 36 2659 2615 1909 88 -944 -19 N
ATOM 200 CA ALA A 36 -12.498 -4.235 22.205 1.00 18.75 C
ANISOU 200 CA ALA A 36 2728 2395 2000 264 -941 119 C
ATOM 201 C ALA A 36 -13.738 -3.691 21.492 1.00 18.67 C
ANISOU 201 C ALA A 36 2570 2698 1824 112 -754 389 C
ATOM 202 O ALA A 36 -13.736 -3.546 20.251 1.00 18.74 O
ANISOU 202 O ALA A 36 2624 2755 1739 145 -781 258 O
ATOM 203 CB ALA A 36 -12.674 -5.708 22.548 1.00 20.77 C
ANISOU 203 CB ALA A 36 2978 2556 2359 246 -971 157 C
ATOM 204 N ARG A 37 -14.790 -3.374 22.244 1.00 18.74 N
ANISOU 204 N ARG A 37 2627 2782 1712 20 -657 259 N
ATOM 205 CA AARG A 37 -15.991 -2.809 21.639 0.47 18.16 C
ANISOU 205 CA AARG A 37 2493 2556 1852 -70 -552 198 C
ATOM 206 CA BARG A 37 -16.005 -2.811 21.630 0.53 18.36 C
ANISOU 206 CA BARG A 37 2576 2516 1885 -71 -508 255 C
ATOM 207 C ARG A 37 -15.667 -1.537 20.877 1.00 17.71 C
ANISOU 207 C ARG A 37 2427 2600 1703 -246 -629 320 C
ATOM 208 O ARG A 37 -16.159 -1.318 19.768 1.00 17.28 O
ANISOU 208 O ARG A 37 2539 2723 1302 -82 -686 295 O
ATOM 209 CB AARG A 37 -17.028 -2.522 22.709 0.47 18.35 C
ANISOU 209 CB AARG A 37 2436 2713 1825 -90 -556 -91 C
ATOM 210 CB BARG A 37 -17.110 -2.508 22.659 0.53 19.14 C
ANISOU 210 CB BARG A 37 2682 2694 1895 -184 -446 33 C
ATOM 211 CG AARG A 37 -18.314 -1.895 22.184 0.47 17.70 C
ANISOU 211 CG AARG A 37 2353 2555 1816 150 -593 -244 C
ATOM 212 CG BARG A 37 -18.429 -2.043 21.950 0.53 18.89 C
ANISOU 212 CG BARG A 37 2702 2629 1848 92 -471 223 C
ATOM 213 CD AARG A 37 -19.187 -1.681 23.384 0.47 20.20 C
ANISOU 213 CD AARG A 37 2391 3392 1892 86 -478 -57 C
ATOM 214 CD BARG A 37 -19.560 -1.507 22.864 0.53 20.74 C
ANISOU 214 CD BARG A 37 2782 3126 1971 -70 -322 88 C
ATOM 215 NE AARG A 37 -20.507 -1.153 23.083 0.47 19.05 N
ANISOU 215 NE AARG A 37 2147 3241 1850 -158 -514 114 N
ATOM 216 NE BARG A 37 -19.264 -0.164 23.370 0.53 20.81 N
ANISOU 216 NE BARG A 37 2716 3187 2006 159 -226 56 N
ATOM 217 CZ AARG A 37 -20.875 0.107 23.289 0.47 20.82 C
ANISOU 217 CZ AARG A 37 2076 4031 1802 -79 -539 497 C
ATOM 218 CZ BARG A 37 -20.170 0.717 23.803 0.53 19.87 C
ANISOU 218 CZ BARG A 37 2477 2909 2166 -17 -268 -106 C
ATOM 219 NH1AARG A 37 -22.122 0.481 23.047 0.47 21.17 N
ANISOU 219 NH1AARG A 37 1996 4261 1784 -17 -616 716 N
ATOM 220 NH1BARG A 37 -19.764 1.910 24.215 0.53 18.73 N
ANISOU 220 NH1BARG A 37 2513 2285 2321 -215 -296 -96 N
ATOM 221 NH2AARG A 37 -20.002 0.997 23.740 0.47 20.36 N
ANISOU 221 NH2AARG A 37 1884 4021 1831 -134 -389 95 N
ATOM 222 NH2BARG A 37 -21.472 0.422 23.833 0.53 19.80 N
ANISOU 222 NH2BARG A 37 2298 3105 2122 247 -261 310 N
ATOM 223 N GLY A 38 -14.838 -0.666 21.443 1.00 17.06 N
ANISOU 223 N GLY A 38 2214 2490 1779 -193 -629 322 N
ATOM 224 CA GLY A 38 -14.481 0.564 20.773 1.00 17.30 C
ANISOU 224 CA GLY A 38 2259 2540 1773 -30 -601 173 C
ATOM 225 C GLY A 38 -13.806 0.284 19.447 1.00 16.50 C
ANISOU 225 C GLY A 38 2189 2338 1741 43 -655 259 C
ATOM 226 O GLY A 38 -14.054 0.985 18.459 1.00 17.67 O
ANISOU 226 O GLY A 38 2140 2538 2037 34 -603 455 O
ATOM 227 N GLU A 39 -12.923 -0.708 19.392 1.00 18.03 N
ANISOU 227 N GLU A 39 2275 2837 1737 160 -705 275 N
ATOM 228 CA GLU A 39 -12.268 -1.090 18.134 1.00 20.20 C
ANISOU 228 CA GLU A 39 2343 3284 2048 593 -858 123 C
ATOM 229 C GLU A 39 -13.282 -1.640 17.129 1.00 17.88 C
ANISOU 229 C GLU A 39 2208 2697 1888 663 -804 525 C
ATOM 230 O GLU A 39 -13.238 -1.350 15.926 1.00 18.89 O
ANISOU 230 O GLU A 39 2300 2982 1897 539 -537 616 O
ATOM 231 CB GLU A 39 -11.216 -2.167 18.387 1.00 25.31 C
ANISOU 231 CB GLU A 39 2732 4474 2410 874 -1120 -105 C
ATOM 232 CG GLU A 39 -10.020 -1.734 19.136 1.00 27.76 C
ANISOU 232 CG GLU A 39 3049 4633 2864 490 -916 -895 C
ATOM 233 CD GLU A 39 -8.982 -2.807 19.022 0.57 28.82 C
ANISOU 233 CD GLU A 39 2940 4536 3473 808 -1133 -794 C
ATOM 234 OE1 GLU A 39 -9.316 -3.943 19.411 0.64 27.84 O
ANISOU 234 OE1 GLU A 39 2644 4381 3554 840 -1550 -1034 O
ATOM 235 OE2 GLU A 39 -7.886 -2.550 18.471 0.69 31.91 O
ANISOU 235 OE2 GLU A 39 3291 4845 3987 855 -683 -909 O
ATOM 236 N ASN A 40 -14.182 -2.493 17.603 1.00 17.79 N
ANISOU 236 N ASN A 40 2430 2573 1757 295 -599 153 N
ATOM 237 CA ASN A 40 -15.217 -3.036 16.715 1.00 18.10 C
ANISOU 237 CA ASN A 40 2638 2427 1814 343 -801 122 C
ATOM 238 C ASN A 40 -16.139 -1.941 16.196 1.00 16.16 C
ANISOU 238 C ASN A 40 2409 2122 1608 520 -646 -7 C
ATOM 239 O ASN A 40 -16.564 -1.968 15.027 1.00 18.15 O
ANISOU 239 O ASN A 40 2759 2610 1526 268 -770 0 O
ATOM 240 CB ASN A 40 -16.001 -4.086 17.466 1.00 19.36 C
ANISOU 240 CB ASN A 40 3120 2154 2080 57 -808 159 C
ATOM 241 CG ASN A 40 -15.131 -5.244 17.895 1.00 23.44 C
ANISOU 241 CG ASN A 40 3855 2558 2493 -76 -660 73 C
ATOM 242 OD1 ASN A 40 -14.084 -5.498 17.305 1.00 27.15 O
ANISOU 242 OD1 ASN A 40 4411 2939 2964 608 -437 123 O
ATOM 243 ND2 ASN A 40 -15.559 -5.955 18.927 1.00 24.08 N
ANISOU 243 ND2 ASN A 40 3917 2697 2537 -157 -987 502 N
ATOM 244 N LEU A 41 -16.393 -0.929 17.000 1.00 15.88 N
ANISOU 244 N LEU A 41 2194 2164 1674 362 -428 72 N
ATOM 245 CA LEU A 41 -17.182 0.221 16.571 1.00 16.11 C
ANISOU 245 CA LEU A 41 1922 2474 1724 195 -364 -233 C
ATOM 246 C LEU A 41 -16.426 1.037 15.541 1.00 15.93 C
ANISOU 246 C LEU A 41 1820 2567 1666 112 -526 -61 C
ATOM 247 O LEU A 41 -17.036 1.542 14.577 1.00 16.35 O
ANISOU 247 O LEU A 41 2039 2598 1577 262 -666 87 O
ATOM 248 CB LEU A 41 -17.558 1.099 17.777 1.00 15.49 C
ANISOU 248 CB LEU A 41 1827 2368 1690 35 -316 -239 C
ATOM 249 CG LEU A 41 -18.634 0.538 18.694 1.00 16.16 C
ANISOU 249 CG LEU A 41 1848 2634 1658 -107 -450 24 C
ATOM 250 CD1 LEU A 41 -18.698 1.373 19.972 1.00 16.28 C
ANISOU 250 CD1 LEU A 41 1844 2854 1486 160 -389 -227 C
ATOM 251 CD2 LEU A 41 -20.038 0.530 18.022 1.00 18.30 C
ANISOU 251 CD2 LEU A 41 2106 3160 1685 -88 -563 166 C
ATOM 252 N GLU A 42 -15.121 1.210 15.689 1.00 16.42 N
ANISOU 252 N GLU A 42 1960 2530 1750 -147 -475 22 N
ATOM 253 CA GLU A 42 -14.376 1.984 14.711 1.00 17.85 C
ANISOU 253 CA GLU A 42 2121 2632 2028 -259 -411 80 C
ATOM 254 C GLU A 42 -14.419 1.291 13.364 1.00 15.69 C
ANISOU 254 C GLU A 42 1957 2248 1755 45 -423 293 C
ATOM 255 O GLU A 42 -14.595 1.936 12.306 1.00 17.46 O
ANISOU 255 O GLU A 42 1836 3012 1787 106 -456 393 O
ATOM 256 CB GLU A 42 -12.913 2.160 15.157 1.00 23.23 C
ANISOU 256 CB GLU A 42 2478 3745 2605 -687 -385 3 C
ATOM 257 CG GLU A 42 -12.077 3.025 14.241 1.00 29.53 C
ANISOU 257 CG GLU A 42 3100 4849 3273 -431 -271 108 C
ATOM 258 CD GLU A 42 -12.580 4.477 14.159 1.00 35.25 C
ANISOU 258 CD GLU A 42 3691 5867 3836 -732 -212 -30 C
ATOM 259 OE1 GLU A 42 -13.355 4.922 15.043 1.00 38.55 O
ANISOU 259 OE1 GLU A 42 4086 6261 4298 -785 -221 -321 O
ATOM 260 OE2 GLU A 42 -12.205 5.180 13.197 0.14 36.43 O
ANISOU 260 OE2 GLU A 42 3764 6123 3955 -737 -216 137 O
ATOM 261 N HIS A 43 -14.275 -0.027 13.372 1.00 15.90 N
ANISOU 261 N HIS A 43 2004 2416 1619 217 -659 -66 N
ATOM 262 CA AHIS A 43 -14.261 -0.699 12.099 0.46 17.17 C
ANISOU 262 CA AHIS A 43 2121 2487 1918 613 -645 -16 C
ATOM 263 CA BHIS A 43 -14.344 -0.849 12.163 0.54 16.84 C
ANISOU 263 CA BHIS A 43 2051 2577 1771 431 -764 -259 C
ATOM 264 C HIS A 43 -15.690 -0.677 11.488 1.00 16.41 C
ANISOU 264 C HIS A 43 1896 2544 1794 355 -536 -12 C
ATOM 265 O HIS A 43 -15.806 -0.495 10.259 1.00 16.56 O
ANISOU 265 O HIS A 43 1835 2897 1562 116 -573 1 O
ATOM 266 CB AHIS A 43 -13.648 -2.098 12.261 0.46 20.06 C
ANISOU 266 CB AHIS A 43 2400 2848 2376 935 -409 241 C
ATOM 267 CB BHIS A 43 -14.129 -2.333 12.493 0.54 17.51 C
ANISOU 267 CB BHIS A 43 2175 2469 2009 466 -761 -336 C
ATOM 268 CG AHIS A 43 -12.143 -2.080 12.352 0.46 22.71 C
ANISOU 268 CG AHIS A 43 2569 3324 2736 968 -167 514 C
ATOM 269 CG BHIS A 43 -13.579 -3.119 11.344 0.54 19.84 C
ANISOU 269 CG BHIS A 43 2409 2827 2305 456 -668 -430 C
ATOM 270 ND1AHIS A 43 -11.458 -1.852 13.529 0.46 26.01 N
ANISOU 270 ND1AHIS A 43 2623 4208 3053 1072 -85 500 N
ATOM 271 ND1BHIS A 43 -13.427 -4.488 11.365 0.54 21.08 N
ANISOU 271 ND1BHIS A 43 2370 3278 2360 203 -830 -855 N
ATOM 272 CD2AHIS A 43 -11.196 -2.253 11.398 0.46 24.53 C
ANISOU 272 CD2AHIS A 43 2576 3820 2923 1035 -112 641 C
ATOM 273 CD2BHIS A 43 -13.127 -2.711 10.137 0.54 21.49 C
ANISOU 273 CD2BHIS A 43 2794 2782 2588 337 -304 -604 C
ATOM 274 CE1AHIS A 43 -10.156 -1.885 13.294 0.46 26.09 C
ANISOU 274 CE1AHIS A 43 2649 4196 3069 1103 -179 588 C
ATOM 275 CE1BHIS A 43 -12.901 -4.887 10.216 0.54 21.51 C
ANISOU 275 CE1BHIS A 43 2385 3321 2468 318 -793 -792 C
ATOM 276 NE2AHIS A 43 -9.971 -2.131 12.010 0.46 26.00 N
ANISOU 276 NE2AHIS A 43 2619 4167 3093 952 -133 505 N
ATOM 277 NE2BHIS A 43 -12.710 -3.828 9.456 0.54 23.48 N
ANISOU 277 NE2BHIS A 43 2737 3564 2620 56 -424 -867 N
ATOM 278 N LEU A 44 -16.741 -0.800 12.276 1.00 16.02 N
ANISOU 278 N LEU A 44 1897 2377 1812 260 -327 -24 N
ATOM 279 CA LEU A 44 -18.100 -0.666 11.748 1.00 15.48 C
ANISOU 279 CA LEU A 44 1983 2098 1802 46 -338 13 C
ATOM 280 C LEU A 44 -18.361 0.733 11.230 1.00 14.25 C
ANISOU 280 C LEU A 44 1923 1854 1636 -2 -414 64 C
ATOM 281 O LEU A 44 -19.015 0.902 10.190 1.00 15.94 O
ANISOU 281 O LEU A 44 1939 2656 1459 -168 -557 348 O
ATOM 282 CB LEU A 44 -19.117 -1.066 12.800 1.00 15.24 C
ANISOU 282 CB LEU A 44 1707 2174 1909 -98 -441 78 C
ATOM 283 CG LEU A 44 -20.592 -0.977 12.336 1.00 16.03 C
ANISOU 283 CG LEU A 44 2034 2099 1958 -98 -380 -49 C
ATOM 284 CD1 LEU A 44 -20.801 -1.851 11.068 1.00 17.34 C
ANISOU 284 CD1 LEU A 44 2257 2281 2050 83 -570 -194 C
ATOM 285 CD2 LEU A 44 -21.521 -1.385 13.451 1.00 18.85 C
ANISOU 285 CD2 LEU A 44 2359 2736 2067 -213 -151 233 C
ATOM 286 N ARG A 45 -17.852 1.756 11.884 1.00 14.33 N
ANISOU 286 N ARG A 45 1848 1925 1671 -20 -470 -104 N
ATOM 287 CA AARG A 45 -17.995 3.130 11.431 0.36 15.53 C
ANISOU 287 CA AARG A 45 2082 2166 1651 146 -404 -258 C
ATOM 288 CA BARG A 45 -18.026 3.129 11.420 0.64 15.30 C
ANISOU 288 CA BARG A 45 1969 2209 1636 117 -459 -430 C
ATOM 289 C ARG A 45 -17.426 3.276 10.031 1.00 15.48 C
ANISOU 289 C ARG A 45 1869 2362 1653 170 -459 -121 C
ATOM 290 O ARG A 45 -18.060 3.852 9.142 1.00 15.72 O
ANISOU 290 O ARG A 45 1997 2332 1644 149 -753 119 O
ATOM 291 CB AARG A 45 -17.286 4.097 12.395 0.36 16.51 C
ANISOU 291 CB AARG A 45 2453 2110 1710 211 -449 -157 C
ATOM 292 CB BARG A 45 -17.391 4.159 12.393 0.64 15.54 C
ANISOU 292 CB BARG A 45 1995 2167 1741 187 -784 -254 C
ATOM 293 CG AARG A 45 -17.602 5.570 12.134 0.36 18.59 C
ANISOU 293 CG AARG A 45 2731 2490 1842 57 -435 -332 C
ATOM 294 CG BARG A 45 -17.470 5.623 11.845 0.64 17.09 C
ANISOU 294 CG BARG A 45 2026 2521 1947 17 -919 -540 C
ATOM 295 CD AARG A 45 -16.355 6.455 12.271 0.36 21.52 C
ANISOU 295 CD AARG A 45 2956 3133 2088 2 -418 -46 C
ATOM 296 CD BARG A 45 -16.979 6.700 12.840 0.64 22.73 C
ANISOU 296 CD BARG A 45 2262 4048 2326 3 -829 -525 C
ATOM 297 NE AARG A 45 -15.823 6.504 13.629 0.36 23.92 N
ANISOU 297 NE AARG A 45 3168 3533 2390 188 -312 21 N
ATOM 298 NE BARG A 45 -15.564 6.577 13.129 0.64 24.52 N
ANISOU 298 NE BARG A 45 2814 3663 2840 -289 -657 -278 N
ATOM 299 CZ AARG A 45 -16.175 7.402 14.544 0.36 25.35 C
ANISOU 299 CZ AARG A 45 3159 3964 2506 576 -429 109 C
ATOM 300 CZ BARG A 45 -14.933 7.362 14.002 0.64 25.37 C
ANISOU 300 CZ BARG A 45 3005 3546 3089 -102 -976 -514 C
ATOM 301 NH1AARG A 45 -15.630 7.372 15.750 0.36 25.70 N
ANISOU 301 NH1AARG A 45 3165 4156 2444 472 -455 332 N
ATOM 302 NH1BARG A 45 -15.613 8.308 14.645 0.64 24.01 N
ANISOU 302 NH1BARG A 45 3095 2896 3133 135 -1197 -112 N
ATOM 303 NH2AARG A 45 -17.075 8.328 14.258 0.36 24.96 N
ANISOU 303 NH2AARG A 45 3133 3722 2629 1139 -559 24 N
ATOM 304 NH2BARG A 45 -13.645 7.183 14.262 0.64 29.79 N
ANISOU 304 NH2BARG A 45 3347 4537 3434 60 -685 -716 N
ATOM 305 N ASN A 46 -16.221 2.759 9.814 1.00 14.87 N
ANISOU 305 N ASN A 46 1652 2199 1800 -135 -398 76 N
ATOM 306 CA ASN A 46 -15.625 2.853 8.495 1.00 16.25 C
ANISOU 306 CA ASN A 46 1697 2544 1934 -126 -486 233 C
ATOM 307 C ASN A 46 -16.458 2.101 7.468 1.00 14.35 C
ANISOU 307 C ASN A 46 1620 2131 1701 27 -472 250 C
ATOM 308 O ASN A 46 -16.654 2.583 6.331 1.00 14.95 O
ANISOU 308 O ASN A 46 1729 2363 1589 141 -457 253 O
ATOM 309 CB ASN A 46 -14.192 2.303 8.538 1.00 20.79 C
ANISOU 309 CB ASN A 46 1671 3836 2394 -223 -680 310 C
ATOM 310 CG ASN A 46 -13.266 3.175 9.343 1.00 28.27 C
ANISOU 310 CG ASN A 46 2394 5207 3141 -519 -851 756 C
ATOM 311 OD1 ASN A 46 -13.506 4.366 9.511 1.00 29.99 O
ANISOU 311 OD1 ASN A 46 2645 5318 3431 -855 -998 563 O
ATOM 312 ND2 ASN A 46 -12.201 2.575 9.863 1.00 32.22 N
ANISOU 312 ND2 ASN A 46 2584 6244 3415 -977 -875 1335 N
ATOM 313 N LYS A 47 -16.949 0.923 7.821 1.00 14.09 N
ANISOU 313 N LYS A 47 1631 2039 1684 116 -543 -33 N
ATOM 314 CA LYS A 47 -17.802 0.166 6.894 1.00 13.75 C
ANISOU 314 CA LYS A 47 1625 1879 1720 192 -544 -59 C
ATOM 315 C LYS A 47 -19.093 0.913 6.560 1.00 12.72 C
ANISOU 315 C LYS A 47 1456 1887 1489 158 -399 143 C
ATOM 316 O LYS A 47 -19.546 0.865 5.384 1.00 13.97 O
ANISOU 316 O LYS A 47 1682 2234 1391 195 -555 40 O
ATOM 317 CB LYS A 47 -18.159 -1.193 7.494 1.00 14.17 C
ANISOU 317 CB LYS A 47 1841 1765 1777 245 -400 169 C
ATOM 318 CG LYS A 47 -16.990 -2.156 7.553 1.00 16.24 C
ANISOU 318 CG LYS A 47 2041 2080 2050 329 -470 154 C
ATOM 319 CD LYS A 47 -17.326 -3.377 8.353 1.00 17.97 C
ANISOU 319 CD LYS A 47 2268 2317 2245 543 -366 488 C
ATOM 320 CE LYS A 47 -16.132 -4.344 8.469 1.00 20.02 C
ANISOU 320 CE LYS A 47 2319 2861 2427 382 -504 110 C
ATOM 321 NZ LYS A 47 -15.820 -4.859 7.107 1.00 19.91 N
ANISOU 321 NZ LYS A 47 2149 2986 2430 207 -496 -252 N
ATOM 322 N THR A 48 -19.685 1.612 7.512 1.00 13.32 N
ANISOU 322 N THR A 48 1466 1964 1632 154 -367 -36 N
ATOM 323 CA THR A 48 -20.920 2.322 7.255 1.00 13.22 C
ANISOU 323 CA THR A 48 1581 1843 1598 126 -287 -5 C
ATOM 324 C THR A 48 -20.647 3.611 6.484 1.00 13.04 C
ANISOU 324 C THR A 48 1460 1877 1618 -303 -335 115 C
ATOM 325 O THR A 48 -21.551 4.077 5.749 1.00 13.54 O
ANISOU 325 O THR A 48 1547 2041 1556 47 -516 -36 O
ATOM 326 CB THR A 48 -21.750 2.584 8.533 1.00 14.11 C
ANISOU 326 CB THR A 48 1781 1915 1666 5 -442 -112 C
ATOM 327 OG1 THR A 48 -21.027 3.390 9.499 1.00 15.21 O
ANISOU 327 OG1 THR A 48 1803 2286 1691 -75 -606 -170 O
ATOM 328 CG2 THR A 48 -22.204 1.279 9.153 1.00 15.41 C
ANISOU 328 CG2 THR A 48 1972 2001 1881 120 -303 293 C
ATOM 329 N GLU A 49 -19.465 4.205 6.589 1.00 12.63 N
ANISOU 329 N GLU A 49 1328 1766 1705 -187 -260 237 N
ATOM 330 CA GLU A 49 -19.100 5.334 5.735 1.00 12.59 C
ANISOU 330 CA GLU A 49 1327 1739 1720 -295 -281 -49 C
ATOM 331 C GLU A 49 -19.084 4.849 4.285 1.00 12.94 C
ANISOU 331 C GLU A 49 1465 1879 1573 50 -459 -32 C
ATOM 332 O GLU A 49 -19.639 5.504 3.367 1.00 14.11 O
ANISOU 332 O GLU A 49 1566 2078 1717 -140 -554 172 O
ATOM 333 CB GLU A 49 -17.719 5.938 6.117 1.00 14.85 C
ANISOU 333 CB GLU A 49 1626 2105 1910 -732 -385 217 C
ATOM 334 CG GLU A 49 -17.330 7.107 5.220 1.00 15.23 C
ANISOU 334 CG GLU A 49 1640 2066 2081 -558 -403 160 C
ATOM 335 CD GLU A 49 -15.992 7.720 5.510 0.78 15.70 C
ANISOU 335 CD GLU A 49 1804 1967 2193 -643 -538 432 C
ATOM 336 OE1 GLU A 49 -15.528 8.519 4.696 0.83 17.87 O
ANISOU 336 OE1 GLU A 49 1902 2577 2312 -261 -280 224 O
ATOM 337 OE2 GLU A 49 -15.449 7.428 6.601 0.61 18.15 O
ANISOU 337 OE2 GLU A 49 1835 2628 2433 -968 -948 802 O
ATOM 338 N ASP A 50 -18.405 3.735 4.047 1.00 13.02 N
ANISOU 338 N ASP A 50 1469 1884 1595 118 -329 -286 N
ATOM 339 CA ASP A 50 -18.351 3.158 2.704 1.00 13.36 C
ANISOU 339 CA ASP A 50 1435 1948 1695 79 -379 -83 C
ATOM 340 C ASP A 50 -19.771 2.808 2.234 1.00 13.36 C
ANISOU 340 C ASP A 50 1513 1944 1621 38 -271 121 C
ATOM 341 O ASP A 50 -20.091 3.019 1.044 1.00 13.90 O
ANISOU 341 O ASP A 50 1519 2338 1422 48 -359 142 O
ATOM 342 CB ASP A 50 -17.425 1.927 2.688 1.00 15.05 C
ANISOU 342 CB ASP A 50 1351 2283 2084 323 -244 -104 C
ATOM 343 CG ASP A 50 -15.949 2.289 2.812 1.00 20.98 C
ANISOU 343 CG ASP A 50 2041 2889 3041 127 -144 248 C
ATOM 344 OD1 ASP A 50 -15.591 3.476 2.673 1.00 24.80 O
ANISOU 344 OD1 ASP A 50 2286 3730 3407 276 -131 533 O
ATOM 345 OD2 ASP A 50 -15.149 1.354 3.063 1.00 24.57 O
ANISOU 345 OD2 ASP A 50 2290 3585 3461 490 -194 -17 O
ATOM 346 N LEU A 51 -20.595 2.257 3.096 1.00 13.31 N
ANISOU 346 N LEU A 51 1423 1931 1701 -45 -476 61 N
ATOM 347 CA LEU A 51 -21.985 1.925 2.763 1.00 12.55 C
ANISOU 347 CA LEU A 51 1516 1680 1573 -146 -397 191 C
ATOM 348 C LEU A 51 -22.737 3.152 2.332 1.00 12.63 C
ANISOU 348 C LEU A 51 1604 1715 1481 71 -399 -7 C
ATOM 349 O LEU A 51 -23.482 3.129 1.327 1.00 13.37 O
ANISOU 349 O LEU A 51 1626 2174 1280 32 -508 132 O
ATOM 350 CB LEU A 51 -22.672 1.300 3.963 1.00 13.72 C
ANISOU 350 CB LEU A 51 1463 2070 1678 -329 -313 276 C
ATOM 351 CG LEU A 51 -24.105 0.844 3.765 1.00 15.06 C
ANISOU 351 CG LEU A 51 1635 2210 1877 -283 -278 35 C
ATOM 352 CD1 LEU A 51 -24.107 -0.464 2.934 1.00 17.92 C
ANISOU 352 CD1 LEU A 51 2190 2555 2063 -118 -272 20 C
ATOM 353 CD2 LEU A 51 -24.852 0.684 5.079 1.00 15.53 C
ANISOU 353 CD2 LEU A 51 1912 2135 1852 -173 -138 268 C
ATOM 354 N GLU A 52 -22.566 4.275 3.005 1.00 12.79 N
ANISOU 354 N GLU A 52 1614 1511 1737 101 -294 -153 N
ATOM 355 CA GLU A 52 -23.259 5.485 2.645 1.00 12.52 C
ANISOU 355 CA GLU A 52 1612 1391 1753 106 -237 -101 C
ATOM 356 C GLU A 52 -22.805 5.902 1.241 1.00 12.35 C
ANISOU 356 C GLU A 52 1251 1837 1603 75 -252 196 C
ATOM 357 O GLU A 52 -23.653 6.318 0.400 1.00 13.47 O
ANISOU 357 O GLU A 52 1422 2068 1628 37 -551 43 O
ATOM 358 CB GLU A 52 -23.014 6.620 3.685 1.00 13.48 C
ANISOU 358 CB GLU A 52 1631 1413 2079 214 -351 -137 C
ATOM 359 CG GLU A 52 -23.772 7.891 3.300 1.00 14.47 C
ANISOU 359 CG GLU A 52 1872 1500 2127 269 -409 -308 C
ATOM 360 CD GLU A 52 -23.602 9.075 4.214 1.00 16.84 C
ANISOU 360 CD GLU A 52 2369 1934 2094 363 -560 123 C
ATOM 361 OE1 GLU A 52 -23.982 10.195 3.847 1.00 19.03 O
ANISOU 361 OE1 GLU A 52 2816 2164 2252 260 -579 -81 O
ATOM 362 OE2 GLU A 52 -23.142 8.883 5.362 1.00 17.91 O
ANISOU 362 OE2 GLU A 52 2501 2220 2083 262 -551 112 O
ATOM 363 N ALA A 53 -21.514 5.875 0.938 1.00 12.28 N
ANISOU 363 N ALA A 53 1026 2007 1634 -63 -59 37 N
ATOM 364 CA ALA A 53 -21.076 6.238 -0.417 1.00 12.93 C
ANISOU 364 CA ALA A 53 1242 2145 1528 -345 -18 -190 C
ATOM 365 C ALA A 53 -21.720 5.300 -1.451 1.00 11.88 C
ANISOU 365 C ALA A 53 1444 1558 1511 75 -154 34 C
ATOM 366 O ALA A 53 -22.185 5.763 -2.518 1.00 13.96 O
ANISOU 366 O ALA A 53 1576 2256 1470 72 -424 344 O
ATOM 367 CB ALA A 53 -19.544 6.219 -0.507 1.00 13.97 C
ANISOU 367 CB ALA A 53 1098 2598 1611 -154 -67 212 C
ATOM 368 N THR A 54 -21.713 4.006 -1.194 1.00 12.28 N
ANISOU 368 N THR A 54 1551 1518 1595 53 -345 -83 N
ATOM 369 CA THR A 54 -22.317 3.037 -2.133 1.00 12.90 C
ANISOU 369 CA THR A 54 1526 1671 1707 288 -381 -44 C
ATOM 370 C THR A 54 -23.787 3.378 -2.369 1.00 13.87 C
ANISOU 370 C THR A 54 1469 2154 1646 154 -328 71 C
ATOM 371 O THR A 54 -24.296 3.306 -3.505 1.00 13.78 O
ANISOU 371 O THR A 54 1467 2247 1524 58 -512 112 O
ATOM 372 CB THR A 54 -22.185 1.624 -1.573 1.00 13.34 C
ANISOU 372 CB THR A 54 1481 1676 1911 88 -525 -227 C
ATOM 373 OG1 THR A 54 -20.803 1.320 -1.448 1.00 15.35 O
ANISOU 373 OG1 THR A 54 1635 2329 1866 202 -429 -83 O
ATOM 374 CG2 THR A 54 -22.769 0.587 -2.504 1.00 16.57 C
ANISOU 374 CG2 THR A 54 1979 2037 2280 -100 -677 -274 C
ATOM 375 N SER A 55 -24.503 3.776 -1.345 1.00 13.03 N
ANISOU 375 N SER A 55 1342 2070 1538 -88 -350 130 N
ATOM 376 CA SER A 55 -25.917 4.092 -1.456 1.00 12.83 C
ANISOU 376 CA SER A 55 1319 2102 1454 75 -335 161 C
ATOM 377 C SER A 55 -26.123 5.327 -2.297 1.00 13.13 C
ANISOU 377 C SER A 55 1417 1911 1659 -403 -375 -99 C
ATOM 378 O SER A 55 -27.167 5.416 -2.967 1.00 13.50 O
ANISOU 378 O SER A 55 1297 2196 1639 -86 -509 -70 O
ATOM 379 CB SER A 55 -26.523 4.270 -0.070 1.00 13.96 C
ANISOU 379 CB SER A 55 1419 2399 1487 167 -257 -305 C
ATOM 380 OG SER A 55 -26.207 5.522 0.516 1.00 14.37 O
ANISOU 380 OG SER A 55 1590 2436 1432 5 -335 -123 O
ATOM 381 N GLU A 56 -25.186 6.273 -2.282 1.00 12.94 N
ANISOU 381 N GLU A 56 1450 1764 1703 -6 -441 137 N
ATOM 382 CA GLU A 56 -25.258 7.450 -3.156 1.00 13.67 C
ANISOU 382 CA GLU A 56 1732 1764 1701 -102 -536 -42 C
ATOM 383 C GLU A 56 -25.133 7.009 -4.603 1.00 13.68 C
ANISOU 383 C GLU A 56 1459 2109 1632 67 -466 -189 C
ATOM 384 O GLU A 56 -25.876 7.519 -5.468 1.00 14.35 O
ANISOU 384 O GLU A 56 1534 2252 1665 58 -576 160 O
ATOM 385 CB GLU A 56 -24.163 8.473 -2.824 1.00 15.56 C
ANISOU 385 CB GLU A 56 2054 1814 2043 -269 -738 -294 C
ATOM 386 CG GLU A 56 -24.360 9.189 -1.490 1.00 16.83 C
ANISOU 386 CG GLU A 56 2097 2119 2179 10 -798 -127 C
ATOM 387 CD GLU A 56 -25.433 10.290 -1.507 1.00 21.00 C
ANISOU 387 CD GLU A 56 2763 2744 2473 65 -701 -200 C
ATOM 388 OE1 GLU A 56 -25.727 10.885 -0.460 1.00 23.00 O
ANISOU 388 OE1 GLU A 56 3063 3125 2549 393 -632 -357 O
ATOM 389 OE2 GLU A 56 -26.024 10.618 -2.552 1.00 23.55 O
ANISOU 389 OE2 GLU A 56 3229 3171 2549 326 -753 -179 O
ATOM 390 N HIS A 57 -24.218 6.094 -4.904 1.00 13.23 N
ANISOU 390 N HIS A 57 1393 2059 1573 -98 -328 -274 N
ATOM 391 CA HIS A 57 -24.088 5.623 -6.299 1.00 13.16 C
ANISOU 391 CA HIS A 57 1183 2220 1596 -29 -321 -64 C
ATOM 392 C HIS A 57 -25.404 4.985 -6.745 1.00 12.86 C
ANISOU 392 C HIS A 57 1281 2087 1518 -144 -111 149 C
ATOM 393 O HIS A 57 -25.842 5.186 -7.892 1.00 14.49 O
ANISOU 393 O HIS A 57 1621 2465 1419 26 -407 211 O
ATOM 394 CB HIS A 57 -22.949 4.601 -6.463 1.00 14.36 C
ANISOU 394 CB HIS A 57 1134 2373 1951 126 -512 -88 C
ATOM 395 CG HIS A 57 -21.621 5.080 -5.984 1.00 15.61 C
ANISOU 395 CG HIS A 57 1573 2385 1972 -51 -493 -59 C
ATOM 396 ND1 HIS A 57 -21.174 6.363 -6.209 1.00 16.98 N
ANISOU 396 ND1 HIS A 57 1618 2636 2199 -388 -438 302 N
ATOM 397 CD2 HIS A 57 -20.658 4.449 -5.258 1.00 16.09 C
ANISOU 397 CD2 HIS A 57 1433 2624 2057 24 -563 130 C
ATOM 398 CE1 HIS A 57 -19.970 6.498 -5.662 1.00 18.13 C
ANISOU 398 CE1 HIS A 57 1751 2800 2340 -195 -522 701 C
ATOM 399 NE2 HIS A 57 -19.652 5.359 -5.058 1.00 18.07 N
ANISOU 399 NE2 HIS A 57 1785 2880 2199 -350 -529 467 N
ATOM 400 N PHE A 58 -25.969 4.137 -5.919 1.00 12.94 N
ANISOU 400 N PHE A 58 1078 2055 1785 -351 -360 84 N
ATOM 401 CA PHE A 58 -27.234 3.468 -6.238 1.00 12.63 C
ANISOU 401 CA PHE A 58 1264 1805 1729 -42 -292 201 C
ATOM 402 C PHE A 58 -28.351 4.483 -6.503 1.00 12.41 C
ANISOU 402 C PHE A 58 1558 1548 1607 289 -303 -136 C
ATOM 403 O PHE A 58 -29.066 4.381 -7.525 1.00 14.13 O
ANISOU 403 O PHE A 58 1631 2294 1443 104 -655 -10 O
ATOM 404 CB PHE A 58 -27.629 2.510 -5.104 1.00 13.43 C
ANISOU 404 CB PHE A 58 1422 2045 1635 -281 -394 159 C
ATOM 405 CG PHE A 58 -28.977 1.888 -5.263 1.00 13.24 C
ANISOU 405 CG PHE A 58 1337 2066 1628 -61 -567 115 C
ATOM 406 CD1 PHE A 58 -29.193 0.895 -6.217 1.00 15.76 C
ANISOU 406 CD1 PHE A 58 1539 2325 2124 -102 -308 -376 C
ATOM 407 CD2 PHE A 58 -30.030 2.297 -4.496 1.00 16.23 C
ANISOU 407 CD2 PHE A 58 1504 3019 1642 -160 -538 8 C
ATOM 408 CE1 PHE A 58 -30.461 0.328 -6.360 1.00 18.18 C
ANISOU 408 CE1 PHE A 58 1659 2942 2305 -348 -293 -507 C
ATOM 409 CE2 PHE A 58 -31.304 1.713 -4.611 1.00 15.70 C
ANISOU 409 CE2 PHE A 58 1662 2622 1680 -33 -715 -230 C
ATOM 410 CZ PHE A 58 -31.516 0.713 -5.553 1.00 16.11 C
ANISOU 410 CZ PHE A 58 1684 2484 1953 -83 -590 -113 C
ATOM 411 N LYS A 59 -28.480 5.496 -5.678 1.00 12.46 N
ANISOU 411 N LYS A 59 1316 1626 1791 252 -184 -194 N
ATOM 412 CA ALYS A 59 -29.495 6.530 -5.848 0.45 13.26 C
ANISOU 412 CA ALYS A 59 1418 1821 1798 307 -214 -242 C
ATOM 413 CA BLYS A 59 -29.504 6.515 -5.856 0.55 13.14 C
ANISOU 413 CA BLYS A 59 1346 1807 1840 294 -209 -237 C
ATOM 414 C LYS A 59 -29.250 7.268 -7.151 1.00 14.38 C
ANISOU 414 C LYS A 59 1400 2308 1756 83 -379 153 C
ATOM 415 O LYS A 59 -30.182 7.473 -7.952 1.00 15.13 O
ANISOU 415 O LYS A 59 1606 2225 1919 224 -637 122 O
ATOM 416 CB ALYS A 59 -29.477 7.514 -4.658 0.45 14.60 C
ANISOU 416 CB ALYS A 59 1768 1856 1925 560 -185 -438 C
ATOM 417 CB BLYS A 59 -29.524 7.488 -4.662 0.55 14.72 C
ANISOU 417 CB BLYS A 59 1573 1924 2096 501 -206 -322 C
ATOM 418 CG ALYS A 59 -30.409 8.717 -4.817 0.45 16.84 C
ANISOU 418 CG ALYS A 59 2278 2007 2114 512 -229 -691 C
ATOM 419 CG BLYS A 59 -30.539 8.604 -4.838 0.55 17.41 C
ANISOU 419 CG BLYS A 59 2027 2165 2423 584 -293 -412 C
ATOM 420 CD ALYS A 59 -30.335 9.635 -3.600 0.45 19.40 C
ANISOU 420 CD ALYS A 59 3045 2087 2240 557 -127 -696 C
ATOM 421 CD BLYS A 59 -30.722 9.423 -3.579 0.55 19.54 C
ANISOU 421 CD BLYS A 59 2777 1932 2714 329 -184 -484 C
ATOM 422 CE ALYS A 59 -31.263 10.828 -3.746 0.45 24.97 C
ANISOU 422 CE ALYS A 59 3765 3327 2395 645 -84 -744 C
ATOM 423 CE BLYS A 59 -29.601 10.397 -3.402 0.55 26.57 C
ANISOU 423 CE BLYS A 59 3688 3405 3002 270 13 -895 C
ATOM 424 NZ ALYS A 59 -31.195 11.755 -2.588 0.45 28.26 N
ANISOU 424 NZ ALYS A 59 4140 3998 2598 489 24 -852 N
ATOM 425 NZ BLYS A 59 -29.870 11.238 -2.197 0.55 29.86 N
ANISOU 425 NZ BLYS A 59 4169 3983 3193 716 41 -995 N
ATOM 426 N THR A 60 -28.018 7.705 -7.391 1.00 12.83 N
ANISOU 426 N THR A 60 1419 1868 1587 -164 -388 100 N
ATOM 427 CA THR A 60 -27.713 8.449 -8.624 1.00 13.51 C
ANISOU 427 CA THR A 60 1504 1993 1637 -183 -646 49 C
ATOM 428 C THR A 60 -28.032 7.644 -9.869 1.00 13.29 C
ANISOU 428 C THR A 60 1623 1772 1654 28 -560 102 C
ATOM 429 O THR A 60 -28.656 8.160 -10.826 1.00 15.11 O
ANISOU 429 O THR A 60 1892 2151 1699 -70 -629 311 O
ATOM 430 CB THR A 60 -26.220 8.852 -8.647 1.00 14.46 C
ANISOU 430 CB THR A 60 1478 2266 1750 -224 -535 65 C
ATOM 431 OG1 THR A 60 -26.038 9.786 -7.570 1.00 15.19 O
ANISOU 431 OG1 THR A 60 1751 2202 1819 -238 -601 -159 O
ATOM 432 CG2 THR A 60 -25.784 9.517 -9.970 1.00 16.89 C
ANISOU 432 CG2 THR A 60 1749 2746 1924 -289 -319 503 C
ATOM 433 N THR A 61 -27.635 6.381 -9.889 1.00 13.00 N
ANISOU 433 N THR A 61 1671 1718 1550 102 -378 -147 N
ATOM 434 CA THR A 61 -27.855 5.546 -11.071 1.00 13.54 C
ANISOU 434 CA THR A 61 1607 1891 1646 -87 -384 -272 C
ATOM 435 C THR A 61 -29.358 5.315 -11.269 1.00 14.62 C
ANISOU 435 C THR A 61 1617 2134 1804 -80 -428 33 C
ATOM 436 O THR A 61 -29.864 5.320 -12.415 1.00 15.89 O
ANISOU 436 O THR A 61 1902 2418 1719 -70 -698 26 O
ATOM 437 CB THR A 61 -27.085 4.231 -10.933 1.00 14.74 C
ANISOU 437 CB THR A 61 1684 2054 1864 113 -304 -253 C
ATOM 438 OG1 THR A 61 -25.703 4.559 -10.974 1.00 15.57 O
ANISOU 438 OG1 THR A 61 1815 2226 1876 7 -376 -1 O
ATOM 439 CG2 THR A 61 -27.401 3.215 -12.034 1.00 18.67 C
ANISOU 439 CG2 THR A 61 1993 2832 2269 266 -404 -722 C
ATOM 440 N SER A 62 -30.098 5.148 -10.200 1.00 14.23 N
ANISOU 440 N SER A 62 1380 2207 1820 54 -485 117 N
ATOM 441 CA ASER A 62 -31.532 4.910 -10.305 0.58 14.62 C
ANISOU 441 CA ASER A 62 1486 2250 1820 47 -570 233 C
ATOM 442 CA BSER A 62 -31.551 4.952 -10.235 0.42 15.21 C
ANISOU 442 CA BSER A 62 1540 2427 1810 -23 -516 74 C
ATOM 443 C SER A 62 -32.235 6.177 -10.811 1.00 15.27 C
ANISOU 443 C SER A 62 1593 2176 2033 -15 -668 -4 C
ATOM 444 O SER A 62 -33.202 6.066 -11.567 1.00 16.97 O
ANISOU 444 O SER A 62 1664 2745 2041 6 -891 103 O
ATOM 445 CB ASER A 62 -32.078 4.452 -8.952 0.58 14.37 C
ANISOU 445 CB ASER A 62 1639 2003 1819 -134 -540 448 C
ATOM 446 CB BSER A 62 -32.097 4.680 -8.822 0.42 15.44 C
ANISOU 446 CB BSER A 62 1715 2478 1675 -258 -415 -59 C
ATOM 447 OG ASER A 62 -31.498 3.206 -8.596 0.58 15.04 O
ANISOU 447 OG ASER A 62 1637 2243 1834 -55 -620 183 O
ATOM 448 OG BSER A 62 -32.279 5.880 -8.071 0.42 17.46 O
ANISOU 448 OG BSER A 62 1782 3311 1541 -385 -572 -59 O
ATOM 449 N GLN A 63 -31.762 7.354 -10.413 1.00 15.30 N
ANISOU 449 N GLN A 63 1847 1962 2005 168 -603 9 N
ATOM 450 CA GLN A 63 -32.324 8.616 -10.913 1.00 16.05 C
ANISOU 450 CA GLN A 63 1977 2155 1966 208 -665 9 C
ATOM 451 C GLN A 63 -32.073 8.721 -12.415 1.00 16.97 C
ANISOU 451 C GLN A 63 2123 2346 1977 400 -839 42 C
ATOM 452 O GLN A 63 -32.950 9.173 -13.164 1.00 18.51 O
ANISOU 452 O GLN A 63 2274 2555 2204 369 -1109 15 O
ATOM 453 CB GLN A 63 -31.739 9.820 -10.186 1.00 16.56 C
ANISOU 453 CB GLN A 63 2123 1932 2236 297 -564 -245 C
ATOM 454 CG GLN A 63 -32.221 9.936 -8.746 1.00 19.12 C
ANISOU 454 CG GLN A 63 2410 2479 2376 154 -664 -139 C
ATOM 455 CD GLN A 63 -31.439 10.958 -7.953 1.00 21.71 C
ANISOU 455 CD GLN A 63 2706 2707 2835 218 -605 -40 C
ATOM 456 OE1 GLN A 63 -30.230 11.113 -8.144 1.00 22.05 O
ANISOU 456 OE1 GLN A 63 2709 2841 2828 60 -864 -328 O
ATOM 457 NE2 GLN A 63 -32.107 11.618 -7.031 1.00 26.36 N
ANISOU 457 NE2 GLN A 63 3075 3764 3178 447 -574 -527 N
ATOM 458 N LYS A 64 -30.883 8.360 -12.855 1.00 16.44 N
ANISOU 458 N LYS A 64 2305 2122 1821 48 -725 185 N
ATOM 459 CA LYS A 64 -30.553 8.440 -14.276 1.00 17.92 C
ANISOU 459 CA LYS A 64 2550 2308 1949 149 -635 252 C
ATOM 460 C LYS A 64 -31.441 7.487 -15.073 1.00 18.55 C
ANISOU 460 C LYS A 64 2833 2213 2002 174 -729 -1 C
ATOM 461 O LYS A 64 -31.926 7.848 -16.155 1.00 20.15 O
ANISOU 461 O LYS A 64 2944 2909 1802 197 -1033 240 O
ATOM 462 CB LYS A 64 -29.063 8.122 -14.489 1.00 20.71 C
ANISOU 462 CB LYS A 64 2649 3070 2149 440 -481 433 C
ATOM 463 CG LYS A 64 -28.549 8.316 -15.942 1.00 27.73 C
ANISOU 463 CG LYS A 64 3075 4834 2627 388 -351 385 C
ATOM 464 CD LYS A 64 -27.029 8.234 -15.959 1.00 34.34 C
ANISOU 464 CD LYS A 64 3311 6535 3203 354 -130 525 C
ATOM 465 CE LYS A 64 -26.521 8.037 -17.350 1.00 40.87 C
ANISOU 465 CE LYS A 64 3615 8109 3803 460 -69 943 C
ATOM 466 NZ LYS A 64 -25.078 7.694 -17.347 1.00 45.12 N
ANISOU 466 NZ LYS A 64 3862 9086 4196 374 50 1047 N
ATOM 467 N VAL A 65 -31.697 6.292 -14.569 1.00 18.77 N
ANISOU 467 N VAL A 65 2809 2142 2180 32 -1008 -143 N
ATOM 468 CA VAL A 65 -32.576 5.344 -15.263 1.00 19.69 C
ANISOU 468 CA VAL A 65 2965 2171 2346 112 -1222 -120 C
ATOM 469 C VAL A 65 -34.011 5.840 -15.284 1.00 20.26 C
ANISOU 469 C VAL A 65 2799 2625 2273 358 -1119 -91 C
ATOM 470 O VAL A 65 -34.686 5.706 -16.324 1.00 21.51 O
ANISOU 470 O VAL A 65 2760 3306 2106 158 -1274 -133 O
ATOM 471 CB VAL A 65 -32.502 3.940 -14.640 1.00 21.82 C
ANISOU 471 CB VAL A 65 3550 2024 2715 69 -1340 -186 C
ATOM 472 CG1 VAL A 65 -33.632 3.026 -15.172 1.00 24.74 C
ANISOU 472 CG1 VAL A 65 4104 2496 2800 -41 -1411 20 C
ATOM 473 CG2 VAL A 65 -31.194 3.350 -15.032 1.00 24.55 C
ANISOU 473 CG2 VAL A 65 3680 2772 2878 152 -1161 -28 C
ATOM 474 N ALA A 66 -34.478 6.475 -14.214 1.00 19.85 N
ANISOU 474 N ALA A 66 2521 2703 2320 379 -1005 40 N
ATOM 475 CA ALA A 66 -35.839 6.974 -14.181 1.00 21.46 C
ANISOU 475 CA ALA A 66 2586 3219 2350 276 -1155 89 C
ATOM 476 C ALA A 66 -35.963 8.081 -15.230 1.00 21.16 C
ANISOU 476 C ALA A 66 2731 2865 2444 -152 -1311 301 C
ATOM 477 O ALA A 66 -37.008 8.163 -15.902 1.00 22.97 O
ANISOU 477 O ALA A 66 2635 3592 2501 424 -1270 190 O
ATOM 478 CB ALA A 66 -36.214 7.486 -12.795 1.00 22.77 C
ANISOU 478 CB ALA A 66 2667 3704 2280 345 -986 -15 C
ATOM 479 N ARG A 67 -34.936 8.916 -15.416 1.00 20.95 N
ANISOU 479 N ARG A 67 3010 2451 2499 23 -1280 373 N
ATOM 480 CA ARG A 67 -34.965 9.977 -16.430 1.00 23.73 C
ANISOU 480 CA ARG A 67 3333 2866 2815 -154 -1251 415 C
ATOM 481 C ARG A 67 -35.066 9.360 -17.787 1.00 23.98 C
ANISOU 481 C ARG A 67 3212 3226 2674 -182 -1229 548 C
ATOM 482 O ARG A 67 -35.862 9.812 -18.627 1.00 25.88 O
ANISOU 482 O ARG A 67 3264 3968 2600 -336 -1370 946 O
ATOM 483 CB ARG A 67 -33.699 10.862 -16.372 1.00 25.13 C
ANISOU 483 CB ARG A 67 3775 2556 3216 -411 -1408 295 C
ATOM 484 CG ARG A 67 -33.550 11.693 -15.152 1.00 28.68 C
ANISOU 484 CG ARG A 67 4112 3122 3664 -256 -1597 233 C
ATOM 485 CD ARG A 67 -32.501 12.833 -15.328 1.00 29.00 C
ANISOU 485 CD ARG A 67 4205 3005 3810 -187 -1852 477 C
ATOM 486 NE ARG A 67 -31.102 12.406 -15.520 1.00 29.67 N
ANISOU 486 NE ARG A 67 4317 3349 3607 -229 -2213 456 N
ATOM 487 CZ ARG A 67 -30.229 12.201 -14.534 1.00 29.85 C
ANISOU 487 CZ ARG A 67 4382 3360 3601 24 -1993 180 C
ATOM 488 NH1 ARG A 67 -30.602 12.330 -13.269 1.00 29.57 N
ANISOU 488 NH1 ARG A 67 4481 3050 3706 -85 -1707 182 N
ATOM 489 NH2 ARG A 67 -28.982 11.860 -14.835 1.00 30.38 N
ANISOU 489 NH2 ARG A 67 4341 3699 3501 168 -1989 122 N
ATOM 490 N LYS A 68 -34.257 8.338 -18.014 1.00 22.35 N
ANISOU 490 N LYS A 68 3157 2859 2475 -491 -1016 79 N
ATOM 491 CA LYS A 68 -34.168 7.662 -19.311 1.00 23.74 C
ANISOU 491 CA LYS A 68 3307 3232 2482 -283 -946 -118 C
ATOM 492 C LYS A 68 -35.529 7.104 -19.706 1.00 25.39 C
ANISOU 492 C LYS A 68 3404 3837 2407 -605 -1128 -101 C
ATOM 493 O LYS A 68 -35.991 7.276 -20.866 1.00 26.72 O
ANISOU 493 O LYS A 68 3529 4263 2360 -677 -1373 172 O
ATOM 494 CB LYS A 68 -33.119 6.535 -19.252 1.00 25.96 C
ANISOU 494 CB LYS A 68 3556 3549 2760 -29 -750 -303 C
ATOM 495 CG LYS A 68 -33.073 5.656 -20.515 1.00 29.53 C
ANISOU 495 CG LYS A 68 4068 4155 2996 465 -470 -551 C
ATOM 496 CD LYS A 68 -32.023 4.539 -20.418 1.00 32.61 C
ANISOU 496 CD LYS A 68 4626 4608 3156 707 -267 -854 C
ATOM 497 CE LYS A 68 -32.115 3.588 -21.603 1.00 37.06 C
ANISOU 497 CE LYS A 68 5049 5645 3389 876 -227 -641 C
ATOM 498 NZ LYS A 68 -31.040 2.569 -21.554 1.00 40.80 N
ANISOU 498 NZ LYS A 68 5335 6607 3560 842 -202 -61 N
ATOM 499 N PHE A 69 -36.190 6.421 -18.776 1.00 24.89 N
ANISOU 499 N PHE A 69 3394 3588 2475 -284 -1309 -137 N
ATOM 500 CA PHE A 69 -37.482 5.803 -19.079 1.00 25.01 C
ANISOU 500 CA PHE A 69 3408 3298 2798 -491 -1342 260 C
ATOM 501 C PHE A 69 -38.592 6.811 -19.169 1.00 27.49 C
ANISOU 501 C PHE A 69 3453 3841 3152 -578 -1546 225 C
ATOM 502 O PHE A 69 -39.524 6.611 -19.952 1.00 31.23 O
ANISOU 502 O PHE A 69 3410 5281 3175 -898 -1720 17 O
ATOM 503 CB PHE A 69 -37.809 4.702 -18.067 1.00 25.74 C
ANISOU 503 CB PHE A 69 3678 3418 2686 -678 -1101 122 C
ATOM 504 CG PHE A 69 -37.170 3.419 -18.428 1.00 27.36 C
ANISOU 504 CG PHE A 69 3992 3684 2719 -645 -1022 -139 C
ATOM 505 CD1 PHE A 69 -37.880 2.461 -19.125 1.00 29.09 C
ANISOU 505 CD1 PHE A 69 4100 3874 3078 -812 -1103 -249 C
ATOM 506 CD2 PHE A 69 -35.820 3.229 -18.231 1.00 28.32 C
ANISOU 506 CD2 PHE A 69 4212 3802 2748 -556 -971 -79 C
ATOM 507 CE1 PHE A 69 -37.270 1.292 -19.541 1.00 30.24 C
ANISOU 507 CE1 PHE A 69 4217 4101 3172 -597 -1177 -333 C
ATOM 508 CE2 PHE A 69 -35.197 2.055 -18.634 1.00 28.52 C
ANISOU 508 CE2 PHE A 69 4292 3632 2912 -494 -1130 -272 C
ATOM 509 CZ PHE A 69 -35.916 1.090 -19.295 1.00 30.40 C
ANISOU 509 CZ PHE A 69 4247 4111 3194 -540 -1167 -241 C
ATOM 510 N TRP A 70 -38.475 7.920 -18.456 1.00 28.11 N