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*** TEST ***elNémo ID: 2502031627131711067Job options:ID = 2502031627131711067 JOBID = TEST 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 TEST CRYST1 53.430 53.700 81.800 90.00 90.00 90.00 P 21 21 21 8 ATOM 1 N ASP A 513 48.264 -24.342 19.914 1.00 23.96 A N ANISOU 1 N ASP A 513 2085 2970 4049 226 -319 188 A N ATOM 2 CA ASP A 513 48.245 -25.792 19.826 1.00 22.81 A C ANISOU 2 CA ASP A 513 1943 2793 3932 278 -303 206 A C ATOM 3 C ASP A 513 46.897 -26.289 20.311 1.00 25.07 A C ANISOU 3 C ASP A 513 2338 3081 4107 278 -320 216 A C ATOM 4 O ASP A 513 46.123 -25.481 20.816 1.00 22.27 A O ANISOU 4 O ASP A 513 2044 2756 3661 241 -351 210 A O ATOM 5 CB ASP A 513 49.418 -26.416 20.629 1.00 26.45 A C ANISOU 5 CB ASP A 513 2315 3238 4495 317 -385 243 A C ATOM 6 CG ASP A 513 49.324 -26.279 22.144 1.00 39.91 A C ANISOU 6 CG ASP A 513 4048 4967 6150 310 -517 277 A C ATOM 7 OD1 ASP A 513 48.640 -25.349 22.618 1.00 39.57 A O ANISOU 7 OD1 ASP A 513 4069 4957 6010 265 -548 262 A O ATOM 8 OD2 ASP A 513 49.942 -27.103 22.854 1.00 46.71 A O ANISOU 8 OD2 ASP A 513 4868 5812 7066 350 -589 319 A O ATOM 9 N ASN A 514 46.611 -27.595 20.121 1.00 22.55 A N ANISOU 9 N ASN A 514 2041 2725 3800 318 -292 229 A N ATOM 10 CA ASN A 514 45.363 -28.292 20.470 1.00 20.93 A C ANISOU 10 CA ASN A 514 1930 2511 3510 320 -295 242 A C ATOM 11 C ASN A 514 44.167 -27.708 19.738 1.00 21.34 A C ANISOU 11 C ASN A 514 2054 2583 3473 281 -231 205 A C ATOM 12 O ASN A 514 43.030 -27.795 20.188 1.00 23.82 A O ANISOU 12 O ASN A 514 2442 2905 3703 265 -245 213 A O ATOM 13 CB ASN A 514 45.126 -28.337 22.004 1.00 29.15 A C ANISOU 13 CB ASN A 514 3008 3571 4499 318 -400 288 A C ATOM 14 CG ASN A 514 43.997 -29.271 22.400 1.00 53.59 A C ANISOU 14 CG ASN A 514 6186 6646 7530 326 -397 314 A C ATOM 15 ND2 ASN A 514 43.149 -28.829 23.314 1.00 39.57 A N ANISOU 15 ND2 ASN A 514 4478 4904 5654 298 -438 329 A N ATOM 16 OD1 ASN A 514 43.821 -30.360 21.833 1.00 56.28 A O ANISOU 16 OD1 ASN A 514 6532 6941 7911 353 -347 315 A O ATOM 17 N LEU A 515 44.422 -27.172 18.576 1.00 15.29 A N ANISOU 17 N LEU A 515 1261 1820 2727 269 -158 168 A N ATOM 18 CA LEU A 515 43.379 -26.493 17.833 1.00 12.33 A C ANISOU 18 CA LEU A 515 948 1468 2271 233 -106 139 A C ATOM 19 C LEU A 515 42.508 -27.425 17.031 1.00 13.14 A C ANISOU 19 C LEU A 515 1103 1546 2343 243 -47 118 A C ATOM 20 O LEU A 515 42.953 -28.496 16.612 1.00 13.87 A O ANISOU 20 O LEU A 515 1175 1602 2495 277 -14 112 A O ATOM 21 CB LEU A 515 44.027 -25.440 16.936 1.00 12.13 A C ANISOU 21 CB LEU A 515 878 1459 2273 212 -56 116 A C ATOM 22 CG LEU A 515 44.932 -24.435 17.664 1.00 15.03 A C ANISOU 22 CG LEU A 515 1185 1844 2682 194 -114 129 A C ATOM 23 CD1 LEU A 515 45.595 -23.485 16.650 1.00 17.90 A C ANISOU 23 CD1 LEU A 515 1501 2216 3086 171 -49 111 A C ATOM 24 CD2 LEU A 515 44.160 -23.621 18.671 1.00 14.40 A C ANISOU 24 CD2 LEU A 515 1158 1790 2523 163 -182 136 A C ATOM 25 N VAL A 516 41.260 -27.020 16.840 1.00 11.18 A N ANISOU 25 N VAL A 516 923 1319 2008 213 -36 107 A N ATOM 26 CA VAL A 516 40.251 -27.798 16.148 1.00 10.91 A C ANISOU 26 CA VAL A 516 942 1266 1935 211 6 85 A C ATOM 27 C VAL A 516 39.722 -26.922 15.008 1.00 12.26 A C ANISOU 27 C VAL A 516 1140 1466 2052 182 57 54 A C ATOM 28 O VAL A 516 39.327 -25.762 15.232 1.00 11.18 A O ANISOU 28 O VAL A 516 1016 1362 1871 155 38 62 A O ATOM 29 CB VAL A 516 39.117 -28.178 17.148 1.00 14.78 A C ANISOU 29 CB VAL A 516 1487 1756 2375 202 -41 111 A C ATOM 30 CG1 VAL A 516 37.974 -28.919 16.450 1.00 15.91 A C ANISOU 30 CG1 VAL A 516 1680 1879 2484 192 -4 88 A C ATOM 31 CG2 VAL A 516 39.652 -29.007 18.306 1.00 15.96 A C ANISOU 31 CG2 VAL A 516 1617 1878 2567 230 -95 154 A C ATOM 32 N LEU A 517 39.683 -27.488 13.795 1.00 11.31 A N ANISOU 32 N LEU A 517 1033 1331 1933 189 121 19 A N ATOM 33 CA LEU A 517 39.178 -26.782 12.626 1.00 11.71 A C ANISOU 33 CA LEU A 517 1116 1410 1922 164 167 -7 A C ATOM 34 C LEU A 517 37.784 -27.249 12.317 1.00 15.39 A C ANISOU 34 C LEU A 517 1646 1876 2326 148 162 -24 A C ATOM 35 O LEU A 517 37.574 -28.435 12.024 1.00 17.22 A O ANISOU 35 O LEU A 517 1896 2074 2572 161 177 -48 A O ATOM 36 CB LEU A 517 40.089 -27.069 11.424 1.00 13.63 A C ANISOU 36 CB LEU A 517 1336 1644 2196 180 244 -39 A C ATOM 37 CG LEU A 517 39.808 -26.266 10.127 1.00 16.58 A C ANISOU 37 CG LEU A 517 1743 2052 2503 156 299 -58 A C ATOM 38 CD1 LEU A 517 40.085 -24.809 10.323 1.00 18.92 A C ANISOU 38 CD1 LEU A 517 2016 2379 2793 133 288 -26 A C ATOM 39 CD2 LEU A 517 40.730 -26.733 8.985 1.00 20.66 A C ANISOU 39 CD2 LEU A 517 2244 2559 3046 176 386 -93 A C ATOM 40 N ILE A 518 36.841 -26.321 12.378 1.00 12.93 A N ANISOU 40 N ILE A 518 1364 1597 1953 119 139 -12 A N ATOM 41 CA ILE A 518 35.445 -26.648 12.122 1.00 14.64 A C ANISOU 41 CA ILE A 518 1630 1816 2116 101 127 -25 A C ATOM 42 C ILE A 518 34.931 -25.910 10.913 1.00 15.08 A C ANISOU 42 C ILE A 518 1716 1905 2111 80 152 -42 A C ATOM 43 O ILE A 518 35.265 -24.747 10.715 1.00 13.88 A O ANISOU 43 O ILE A 518 1552 1778 1945 72 160 -25 A O ATOM 44 CB ILE A 518 34.629 -26.265 13.357 1.00 18.27 A C ANISOU 44 CB ILE A 518 2096 2286 2561 89 74 8 A C ATOM 45 CG1 ILE A 518 35.063 -27.127 14.578 1.00 21.07 A C ANISOU 45 CG1 ILE A 518 2433 2610 2963 109 45 32 A C ATOM 46 CG2 ILE A 518 33.085 -26.429 13.079 1.00 21.73 A C ANISOU 46 CG2 ILE A 518 2574 2732 2951 66 62 -1 A C ATOM 47 CD1 ILE A 518 34.514 -26.688 15.910 1.00 22.78 A C ANISOU 47 CD1 ILE A 518 2657 2840 3159 100 -1 66 A C ATOM 48 N ARG A 519 34.131 -26.595 10.103 1.00 15.67 A N ANISOU 48 N ARG A 519 1829 1975 2149 70 160 -73 A N ATOM 49 CA ARG A 519 33.458 -26.000 8.974 1.00 15.92 A C ANISOU 49 CA ARG A 519 1896 2040 2111 50 169 -86 A C ATOM 50 C ARG A 519 31.968 -26.209 9.202 1.00 17.94 A C ANISOU 50 C ARG A 519 2176 2299 2339 29 122 -86 A C ATOM 51 O ARG A 519 31.532 -27.237 9.735 1.00 17.79 A O ANISOU 51 O ARG A 519 2159 2251 2351 29 105 -96 A O ATOM 52 CB ARG A 519 33.894 -26.640 7.665 1.00 19.70 A C ANISOU 52 CB ARG A 519 2403 2516 2565 55 220 -133 A C ATOM 53 CG ARG A 519 35.333 -26.329 7.312 1.00 28.35 A C ANISOU 53 CG ARG A 519 3470 3613 3689 74 280 -132 A C ATOM 54 CD ARG A 519 35.762 -27.066 6.062 1.00 48.48 A C ANISOU 54 CD ARG A 519 6050 6158 6213 83 342 -185 A C ATOM 55 NE ARG A 519 37.206 -26.955 5.852 1.00 60.62 A N ANISOU 55 NE ARG A 519 7547 7689 7798 106 409 -186 A N ATOM 56 CZ ARG A 519 38.093 -27.834 6.303 1.00 77.61 A C ANISOU 56 CZ ARG A 519 9656 9798 10033 136 433 -201 A C ATOM 57 NH1 ARG A 519 37.695 -28.900 6.985 1.00 62.28 A N ANISOU 57 NH1 ARG A 519 7716 7815 8133 147 395 -214 A N ATOM 58 NH2 ARG A 519 39.385 -27.656 6.073 1.00 72.80 A N ANISOU 58 NH2 ARG A 519 9000 9185 9474 157 494 -199 A N ATOM 59 N MET A 520 31.177 -25.205 8.864 1.00 13.33 A N ANISOU 59 N MET A 520 1606 1751 1709 13 101 -68 A N ATOM 60 CA MET A 520 29.722 -25.312 8.997 1.00 11.83 A C ANISOU 60 CA MET A 520 1426 1567 1500 -7 56 -66 A C ATOM 61 C MET A 520 29.034 -24.399 8.018 1.00 12.06 A C ANISOU 61 C MET A 520 1477 1634 1469 -20 41 -58 A C ATOM 62 O MET A 520 29.479 -23.274 7.778 1.00 11.37 A O ANISOU 62 O MET A 520 1388 1567 1364 -15 54 -31 A O ATOM 63 CB MET A 520 29.228 -24.979 10.416 1.00 12.39 A C ANISOU 63 CB MET A 520 1470 1631 1605 -6 29 -31 A C ATOM 64 CG MET A 520 29.516 -23.575 10.878 1.00 13.09 A C ANISOU 64 CG MET A 520 1542 1739 1691 1 27 3 A C ATOM 65 SD MET A 520 28.933 -23.202 12.587 1.00 17.09 A S ANISOU 65 SD MET A 520 2028 2239 2226 3 1 33 A S ATOM 66 CE MET A 520 30.260 -23.840 13.506 1.00 15.32 A C ANISOU 66 CE MET A 520 1788 1990 2041 21 11 36 A C ATOM 67 N LYS A 521 27.986 -24.897 7.426 1.00 12.62 A N ANISOU 67 N LYS A 521 1569 1713 1513 -39 10 -80 A N ATOM 68 CA LYS A 521 27.149 -24.065 6.566 1.00 12.26 A C ANISOU 68 CA LYS A 521 1541 1706 1412 -51 -22 -66 A C ATOM 69 C LYS A 521 26.056 -23.456 7.452 1.00 12.86 A C ANISOU 69 C LYS A 521 1583 1784 1520 -54 -62 -30 A C ATOM 70 O LYS A 521 25.580 -24.104 8.382 1.00 11.60 A O ANISOU 70 O LYS A 521 1400 1602 1407 -58 -71 -34 A O ATOM 71 CB LYS A 521 26.514 -24.904 5.458 1.00 15.53 A C ANISOU 71 CB LYS A 521 1992 2130 1780 -71 -46 -111 A C ATOM 72 CG LYS A 521 27.555 -25.389 4.467 1.00 18.79 A C ANISOU 72 CG LYS A 521 2446 2544 2149 -66 3 -151 A C ATOM 73 CD LYS A 521 26.899 -25.956 3.225 1.00 24.84 A C ANISOU 73 CD LYS A 521 3261 3330 2846 -88 -27 -198 A C ATOM 74 CE LYS A 521 27.939 -26.230 2.163 1.00 34.10 A C ANISOU 74 CE LYS A 521 4484 4513 3960 -80 32 -237 A C ATOM 75 NZ LYS A 521 27.834 -27.621 1.657 1.00 38.19 A N ANISOU 75 NZ LYS A 521 5036 5005 4470 -93 35 -316 A N ATOM 76 N PRO A 522 25.573 -22.252 7.144 1.00 10.02 A N ANISOU 76 N PRO A 522 1220 1450 1137 -51 -83 5 A N ATOM 77 CA PRO A 522 24.458 -21.688 7.915 1.00 9.71 A C ANISOU 77 CA PRO A 522 1145 1411 1134 -50 -115 34 A C ATOM 78 C PRO A 522 23.148 -22.397 7.562 1.00 12.34 A C ANISOU 78 C PRO A 522 1469 1752 1469 -71 -163 16 A C ATOM 79 O PRO A 522 23.088 -23.152 6.559 1.00 12.55 A O ANISOU 79 O PRO A 522 1525 1787 1455 -88 -180 -19 A O ATOM 80 CB PRO A 522 24.396 -20.237 7.425 1.00 11.63 A C ANISOU 80 CB PRO A 522 1392 1673 1352 -38 -124 75 A C ATOM 81 CG PRO A 522 24.904 -20.307 5.991 1.00 14.26 A C ANISOU 81 CG PRO A 522 1772 2031 1615 -44 -120 66 A C ATOM 82 CD PRO A 522 25.997 -21.359 6.043 1.00 11.73 A C ANISOU 82 CD PRO A 522 1467 1694 1297 -46 -74 25 A C ATOM 83 N ASP A 523 22.102 -22.130 8.381 1.00 10.77 A N ANISOU 83 N ASP A 523 1228 1549 1317 -71 -183 36 A N ATOM 84 CA ASP A 523 20.791 -22.611 8.043 1.00 10.63 A C ANISOU 84 CA ASP A 523 1187 1540 1314 -92 -231 26 A C ATOM 85 C ASP A 523 20.269 -21.797 6.849 1.00 16.06 A C ANISOU 85 C ASP A 523 1885 2262 1956 -90 -281 45 A C ATOM 86 O ASP A 523 20.958 -20.897 6.352 1.00 15.17 A O ANISOU 86 O ASP A 523 1800 2162 1801 -73 -268 69 A O ATOM 87 CB ASP A 523 19.868 -22.599 9.272 1.00 12.06 A C ANISOU 87 CB ASP A 523 1314 1705 1564 -92 -226 44 A C ATOM 88 CG ASP A 523 19.498 -21.245 9.824 1.00 12.65 A C ANISOU 88 CG ASP A 523 1359 1787 1660 -65 -220 84 A C ATOM 89 OD1 ASP A 523 19.695 -20.247 9.122 1.00 13.05 A O ANISOU 89 OD1 ASP A 523 1424 1853 1679 -50 -236 106 A O ATOM 90 OD2 ASP A 523 18.979 -21.197 10.954 1.00 15.47 A O ANISOU 90 OD2 ASP A 523 1681 2131 2066 -60 -197 95 A O ATOM 91 N GLU A 524 19.064 -22.126 6.374 1.00 15.71 A N ANISOU 91 N GLU A 524 1815 2231 1921 -110 -340 38 A N ATOM 92 CA GLU A 524 18.481 -21.458 5.211 1.00 16.97 A C ANISOU 92 CA GLU A 524 1985 2428 2035 -109 -403 59 A C ATOM 93 C GLU A 524 18.291 -19.971 5.396 1.00 21.92 A C ANISOU 93 C GLU A 524 2590 3061 2677 -76 -405 119 A C ATOM 94 O GLU A 524 18.268 -19.222 4.401 1.00 23.33 A O ANISOU 94 O GLU A 524 2796 3266 2803 -66 -440 149 A O ATOM 95 CB GLU A 524 17.188 -22.157 4.819 1.00 18.63 A C ANISOU 95 CB GLU A 524 2161 2649 2269 -139 -474 38 A C ATOM 96 CG GLU A 524 17.430 -23.546 4.240 1.00 22.01 A C ANISOU 96 CG GLU A 524 2627 3070 2664 -175 -484 -28 A C ATOM 97 CD GLU A 524 16.182 -24.304 3.812 1.00 30.00 A C ANISOU 97 CD GLU A 524 3606 4090 3704 -213 -561 -57 A C ATOM 98 OE1 GLU A 524 15.079 -23.718 3.862 1.00 27.47 A O ANISOU 98 OE1 GLU A 524 3226 3785 3426 -211 -613 -22 A O ATOM 99 OE2 GLU A 524 16.298 -25.515 3.526 1.00 33.79 A O ANISOU 99 OE2 GLU A 524 4111 4550 4176 -246 -565 -117 A O ATOM 100 N ASN A 525 18.250 -19.520 6.656 1.00 15.92 A N ANISOU 100 N ASN A 525 1791 2275 1984 -57 -362 136 A N ATOM 101 CA ASN A 525 18.149 -18.119 7.004 1.00 15.67 A C ANISOU 101 CA ASN A 525 1739 2236 1978 -23 -352 183 A C ATOM 102 C ASN A 525 19.440 -17.435 7.432 1.00 16.78 A C ANISOU 102 C ASN A 525 1913 2358 2105 -6 -292 193 A C ATOM 103 O ASN A 525 19.401 -16.346 8.003 1.00 17.49 A O ANISOU 103 O ASN A 525 1985 2430 2232 19 -274 222 A O ATOM 104 CB ASN A 525 16.989 -17.844 7.932 1.00 16.65 A C ANISOU 104 CB ASN A 525 1792 2347 2186 -12 -356 196 A C ATOM 105 CG ASN A 525 15.683 -17.969 7.186 1.00 25.18 A C ANISOU 105 CG ASN A 525 2832 3451 3286 -21 -431 208 A C ATOM 106 ND2 ASN A 525 15.136 -19.168 7.160 1.00 16.16 A N ANISOU 106 ND2 ASN A 525 1668 2313 2158 -55 -453 172 A N ATOM 107 OD1 ASN A 525 15.242 -17.040 6.491 1.00 23.32 A O ANISOU 107 OD1 ASN A 525 2587 3228 3045 0 -478 249 A O ATOM 108 N GLY A 526 20.584 -18.079 7.162 1.00 13.18 A N ANISOU 108 N GLY A 526 1503 1903 1603 -19 -261 166 A N ATOM 109 CA GLY A 526 21.895 -17.473 7.343 1.00 12.98 A C ANISOU 109 CA GLY A 526 1505 1863 1563 -8 -211 176 A C ATOM 110 C GLY A 526 22.465 -17.531 8.749 1.00 13.62 A C ANISOU 110 C GLY A 526 1568 1915 1691 -1 -165 161 A C ATOM 111 O GLY A 526 23.474 -16.874 9.046 1.00 15.53 A O ANISOU 111 O GLY A 526 1822 2143 1936 7 -132 170 A O ATOM 112 N ARG A 527 21.817 -18.287 9.638 1.00 11.67 A N ANISOU 112 N ARG A 527 1293 1661 1481 -8 -166 141 A N ATOM 113 CA ARG A 527 22.214 -18.348 11.043 1.00 10.88 A C ANISOU 113 CA ARG A 527 1180 1538 1415 -1 -128 132 A C ATOM 114 C ARG A 527 22.953 -19.624 11.377 1.00 10.60 A C ANISOU 114 C ARG A 527 1159 1494 1372 -15 -108 103 A C ATOM 115 O ARG A 527 22.660 -20.696 10.828 1.00 10.51 A O ANISOU 115 O ARG A 527 1154 1488 1351 -33 -123 83 A O ATOM 116 CB ARG A 527 21.016 -18.197 11.956 1.00 13.01 A C ANISOU 116 CB ARG A 527 1409 1803 1731 5 -129 138 A C ATOM 117 CG ARG A 527 20.313 -16.852 11.684 1.00 15.73 A C ANISOU 117 CG ARG A 527 1732 2147 2097 27 -146 168 A C ATOM 118 CD ARG A 527 19.251 -16.528 12.727 1.00 25.28 A C ANISOU 118 CD ARG A 527 2898 3347 3360 41 -130 171 A C ATOM 119 NE ARG A 527 18.508 -15.311 12.381 1.00 34.04 A N ANISOU 119 NE ARG A 527 3981 4451 4502 67 -148 200 A N ATOM 120 CZ ARG A 527 17.343 -15.290 11.734 1.00 47.67 A C ANISOU 120 CZ ARG A 527 5668 6190 6255 70 -190 218 A C ATOM 121 NH1 ARG A 527 16.752 -16.425 11.373 1.00 26.81 A N ANISOU 121 NH1 ARG A 527 3007 3568 3611 44 -218 206 A N ATOM 122 NH2 ARG A 527 16.750 -14.135 11.462 1.00 41.28 A N ANISOU 122 NH2 ARG A 527 4834 5371 5482 99 -207 249 A N ATOM 123 N PHE A 528 23.904 -19.503 12.281 1.00 8.72 A N ANISOU 123 N PHE A 528 929 1242 1144 -6 -79 101 A N ATOM 124 CA PHE A 528 24.753 -20.634 12.676 1.00 8.16 A C ANISOU 124 CA PHE A 528 869 1158 1073 -13 -62 82 A C ATOM 125 C PHE A 528 24.363 -21.220 14.031 1.00 8.88 A C ANISOU 125 C PHE A 528 948 1237 1190 -14 -52 83 A C ATOM 126 O PHE A 528 24.656 -22.395 14.247 1.00 9.87 A O ANISOU 126 O PHE A 528 1080 1348 1323 -21 -46 73 A O ATOM 127 CB PHE A 528 26.200 -20.189 12.727 1.00 8.83 A C ANISOU 127 CB PHE A 528 965 1236 1152 -3 -42 82 A C ATOM 128 CG PHE A 528 26.744 -19.815 11.375 1.00 8.31 A C ANISOU 128 CG PHE A 528 917 1183 1058 -5 -37 83 A C ATOM 129 CD1 PHE A 528 27.113 -20.796 10.455 1.00 9.52 A C ANISOU 129 CD1 PHE A 528 1089 1340 1190 -12 -30 60 A C ATOM 130 CD2 PHE A 528 26.878 -18.487 11.015 1.00 9.42 A C ANISOU 130 CD2 PHE A 528 1058 1327 1193 1 -36 107 A C ATOM 131 CE1 PHE A 528 27.642 -20.455 9.217 1.00 11.27 A C ANISOU 131 CE1 PHE A 528 1333 1576 1373 -14 -16 61 A C ATOM 132 CE2 PHE A 528 27.373 -18.138 9.752 1.00 10.39 A C ANISOU 132 CE2 PHE A 528 1202 1463 1283 -2 -25 116 A C ATOM 133 CZ PHE A 528 27.749 -19.123 8.859 1.00 10.12 A C ANISOU 133 CZ PHE A 528 1189 1439 1216 -10 -14 93 A C ATOM 134 N GLY A 529 23.777 -20.435 14.933 1.00 7.35 A N ANISOU 134 N GLY A 529 739 1044 1008 -5 -45 96 A N ATOM 135 CA GLY A 529 23.320 -20.988 16.206 1.00 8.47 A C ANISOU 135 CA GLY A 529 876 1180 1164 -7 -28 100 A C ATOM 136 C GLY A 529 24.267 -20.849 17.366 1.00 10.52 A C ANISOU 136 C GLY A 529 1153 1432 1410 3 -15 102 A C ATOM 137 O GLY A 529 24.019 -21.453 18.410 1.00 11.88 A O ANISOU 137 O GLY A 529 1330 1601 1581 1 -1 110 A O ATOM 138 N PHE A 530 25.345 -20.082 17.223 1.00 7.72 A N ANISOU 138 N PHE A 530 808 1077 1047 12 -21 97 A N ATOM 139 CA PHE A 530 26.260 -19.845 18.314 1.00 7.61 A C ANISOU 139 CA PHE A 530 809 1060 1024 20 -21 95 A C ATOM 140 C PHE A 530 26.316 -18.374 18.627 1.00 9.47 A C ANISOU 140 C PHE A 530 1045 1295 1258 28 -20 87 A C ATOM 141 O PHE A 530 26.033 -17.519 17.778 1.00 9.03 A O ANISOU 141 O PHE A 530 979 1236 1214 30 -20 88 A O ATOM 142 CB PHE A 530 27.647 -20.444 18.053 1.00 8.58 A C ANISOU 142 CB PHE A 530 935 1174 1151 20 -32 93 A C ATOM 143 CG PHE A 530 28.458 -19.756 16.986 1.00 7.63 A C ANISOU 143 CG PHE A 530 806 1053 1040 20 -33 86 A C ATOM 144 CD1 PHE A 530 29.424 -18.808 17.326 1.00 9.83 A C ANISOU 144 CD1 PHE A 530 1081 1328 1327 23 -40 83 A C ATOM 145 CD2 PHE A 530 28.276 -20.071 15.642 1.00 9.11 A C ANISOU 145 CD2 PHE A 530 992 1243 1225 15 -27 84 A C ATOM 146 CE1 PHE A 530 30.181 -18.183 16.343 1.00 10.84 A C ANISOU 146 CE1 PHE A 530 1198 1452 1468 19 -32 83 A C ATOM 147 CE2 PHE A 530 29.050 -19.455 14.658 1.00 9.42 A C ANISOU 147 CE2 PHE A 530 1029 1285 1265 15 -18 84 A C ATOM 148 CZ PHE A 530 29.988 -18.497 15.015 1.00 10.18 A C ANISOU 148 CZ PHE A 530 1117 1374 1377 16 -17 87 A C ATOM 149 N ASN A 531 26.674 -18.108 19.885 1.00 8.65 A N ANISOU 149 N ASN A 531 957 1191 1138 31 -20 79 A N ATOM 150 CA ASN A 531 26.886 -16.730 20.323 1.00 8.62 A C ANISOU 150 CA ASN A 531 960 1179 1135 37 -21 61 A C ATOM 151 C ASN A 531 28.337 -16.580 20.663 1.00 9.33 A C ANISOU 151 C ASN A 531 1056 1265 1225 31 -47 52 A C ATOM 152 O ASN A 531 29.015 -17.537 21.022 1.00 9.67 A O ANISOU 152 O ASN A 531 1102 1314 1258 29 -63 60 A O ATOM 153 CB ASN A 531 26.102 -16.440 21.619 1.00 9.80 A C ANISOU 153 CB ASN A 531 1129 1335 1261 44 -1 49 A C ATOM 154 CG ASN A 531 24.624 -16.522 21.504 1.00 10.53 A C ANISOU 154 CG ASN A 531 1206 1432 1364 50 30 57 A C ATOM 155 ND2 ASN A 531 23.949 -16.264 22.620 1.00 14.23 A N ANISOU 155 ND2 ASN A 531 1689 1906 1812 58 60 44 A N ATOM 156 OD1 ASN A 531 24.058 -16.913 20.491 1.00 10.98 A O ANISOU 156 OD1 ASN A 531 1237 1490 1445 47 29 73 A O ATOM 157 N VAL A 532 28.822 -15.331 20.572 1.00 9.18 A N ANISOU 157 N VAL A 532 1034 1230 1223 29 -54 36 A N ATOM 158 CA VAL A 532 30.190 -15.037 20.996 1.00 9.64 A C ANISOU 158 CA VAL A 532 1091 1281 1291 19 -83 23 A C ATOM 159 C VAL A 532 30.219 -13.855 21.962 1.00 10.12 A C ANISOU 159 C VAL A 532 1171 1330 1346 15 -92 -10 A C ATOM 160 O VAL A 532 29.350 -12.983 21.894 1.00 9.25 A O ANISOU 160 O VAL A 532 1068 1204 1243 22 -69 -22 A O ATOM 161 CB VAL A 532 31.145 -14.716 19.822 1.00 12.93 A C ANISOU 161 CB VAL A 532 1478 1684 1749 9 -84 33 A C ATOM 162 CG1 VAL A 532 31.375 -15.949 18.941 1.00 13.58 A C ANISOU 162 CG1 VAL A 532 1547 1779 1834 13 -75 55 A C ATOM 163 CG2 VAL A 532 30.661 -13.521 18.985 1.00 14.07 A C ANISOU 163 CG2 VAL A 532 1619 1808 1918 8 -64 37 A C ATOM 164 N LYS A 533 31.215 -13.855 22.865 1.00 9.68 A N ANISOU 164 N LYS A 533 1124 1278 1278 6 -130 -28 A N ATOM 165 CA LYS A 533 31.566 -12.727 23.719 1.00 10.03 A C ANISOU 165 CA LYS A 533 1186 1305 1319 -5 -151 -70 A C ATOM 166 C LYS A 533 33.040 -12.429 23.409 1.00 11.09 A C ANISOU 166 C LYS A 533 1287 1426 1501 -25 -189 -73 A C ATOM 167 O LYS A 533 33.724 -13.262 22.775 1.00 10.57 A O ANISOU 167 O LYS A 533 1189 1370 1458 -25 -196 -43 A O ATOM 168 CB LYS A 533 31.433 -13.055 25.225 1.00 12.09 A C ANISOU 168 CB LYS A 533 1491 1591 1511 -2 -172 -92 A C ATOM 169 CG LYS A 533 29.992 -13.208 25.701 1.00 15.65 A C ANISOU 169 CG LYS A 533 1974 2055 1918 15 -124 -94 A C ATOM 170 CD LYS A 533 29.907 -13.623 27.149 1.00 17.24 A C ANISOU 170 CD LYS A 533 2225 2285 2041 17 -136 -108 A C ATOM 171 CE LYS A 533 28.485 -13.814 27.592 1.00 20.69 A C ANISOU 171 CE LYS A 533 2687 2735 2440 33 -76 -106 A C ATOM 172 NZ LYS A 533 28.428 -14.060 29.078 1.00 26.22 A N ANISOU 172 NZ LYS A 533 3447 3465 3051 33 -80 -122 A N ATOM 173 N GLY A 534 33.529 -11.276 23.861 1.00 9.59 A N ANISOU 173 N GLY A 534 1102 1211 1333 -43 -212 -111 A N ATOM 174 CA GLY A 534 34.942 -10.966 23.689 1.00 10.22 A C ANISOU 174 CA GLY A 534 1142 1275 1466 -68 -251 -116 A C ATOM 175 C GLY A 534 35.289 -10.148 22.456 1.00 12.26 A C ANISOU 175 C GLY A 534 1363 1497 1798 -82 -222 -100 A C ATOM 176 O GLY A 534 34.419 -9.726 21.689 1.00 10.37 A O ANISOU 176 O GLY A 534 1133 1242 1567 -71 -177 -84 A O ATOM 177 N GLY A 535 36.578 -9.941 22.271 1.00 11.19 A N ANISOU 177 N GLY A 535 1184 1349 1719 -107 -249 -100 A N ATOM 178 CA GLY A 535 37.094 -9.099 21.203 1.00 11.25 A C ANISOU 178 CA GLY A 535 1155 1319 1801 -127 -220 -83 A C ATOM 179 C GLY A 535 38.021 -8.055 21.803 1.00 11.10 A C ANISOU 179 C GLY A 535 1116 1263 1837 -164 -262 -122 A C ATOM 180 O GLY A 535 38.057 -7.826 23.022 1.00 11.72 A O ANISOU 180 O GLY A 535 1222 1344 1886 -172 -313 -170 A O ATOM 181 N TYR A 536 38.793 -7.409 20.950 1.00 10.66 A N ANISOU 181 N TYR A 536 1016 1174 1861 -190 -241 -102 A N ATOM 182 CA TYR A 536 39.812 -6.460 21.394 1.00 10.53 A C ANISOU 182 CA TYR A 536 966 1117 1916 -234 -282 -136 A C ATOM 183 C TYR A 536 39.233 -5.346 22.261 1.00 12.79 A C ANISOU 183 C TYR A 536 1302 1364 2194 -245 -304 -192 A C ATOM 184 O TYR A 536 39.847 -4.932 23.237 1.00 14.22 A O ANISOU 184 O TYR A 536 1481 1533 2390 -273 -366 -245 A O ATOM 185 CB TYR A 536 40.515 -5.862 20.181 1.00 13.69 A C ANISOU 185 CB TYR A 536 1315 1481 2406 -260 -234 -95 A C ATOM 186 CG TYR A 536 41.569 -4.851 20.536 1.00 17.24 A C ANISOU 186 CG TYR A 536 1722 1882 2948 -311 -270 -125 A C ATOM 187 CD1 TYR A 536 42.850 -5.251 20.903 1.00 19.19 A C ANISOU 187 CD1 TYR A 536 1902 2143 3245 -335 -319 -135 A C ATOM 188 CD2 TYR A 536 41.298 -3.485 20.488 1.00 19.41 A C ANISOU 188 CD2 TYR A 536 2017 2089 3270 -336 -256 -143 A C ATOM 189 CE1 TYR A 536 43.826 -4.316 21.236 1.00 20.52 A C ANISOU 189 CE1 TYR A 536 2023 2265 3508 -388 -358 -166 A C ATOM 190 CE2 TYR A 536 42.248 -2.548 20.866 1.00 22.15 A C ANISOU 190 CE2 TYR A 536 2326 2384 3708 -389 -293 -177 A C ATOM 191 CZ TYR A 536 43.514 -2.966 21.214 1.00 23.49 A C ANISOU 191 CZ TYR A 536 2427 2574 3927 -417 -345 -188 A C ATOM 192 OH TYR A 536 44.442 -2.006 21.511 1.00 24.55 A O ANISOU 192 OH TYR A 536 2515 2652 4161 -475 -382 -221 A O ATOM 193 N ASP A 537 38.036 -4.854 21.891 1.00 12.05 A N ANISOU 193 N ASP A 537 1252 1248 2077 -222 -254 -184 A N ATOM 194 CA ASP A 537 37.372 -3.792 22.648 1.00 11.15 A C ANISOU 194 CA ASP A 537 1188 1090 1960 -224 -262 -240 A C ATOM 195 C ASP A 537 36.865 -4.255 24.006 1.00 13.62 A C ANISOU 195 C ASP A 537 1551 1441 2182 -206 -299 -294 A C ATOM 196 O ASP A 537 36.618 -3.407 24.872 1.00 13.94 A O ANISOU 196 O ASP A 537 1632 1448 2217 -216 -317 -358 A O ATOM 197 CB ASP A 537 36.209 -3.260 21.818 1.00 10.82 A C ANISOU 197 CB ASP A 537 1170 1018 1925 -196 -197 -206 A C ATOM 198 CG ASP A 537 35.219 -4.293 21.353 1.00 10.31 A C ANISOU 198 CG ASP A 537 1119 1007 1792 -152 -164 -163 A C ATOM 199 OD1 ASP A 537 35.641 -5.429 21.030 1.00 10.25 A O ANISOU 199 OD1 ASP A 537 1088 1050 1757 -148 -169 -131 A O ATOM 200 OD2 ASP A 537 34.017 -3.952 21.236 1.00 11.35 A O ANISOU 200 OD2 ASP A 537 1281 1124 1907 -122 -131 -159 A O ATOM 201 N GLN A 538 36.718 -5.556 24.207 1.00 12.36 A N ANISOU 201 N GLN A 538 1395 1347 1954 -182 -307 -270 A N ATOM 202 CA GLN A 538 36.286 -6.123 25.479 1.00 12.35 A C ANISOU 202 CA GLN A 538 1444 1388 1860 -167 -339 -307 A C ATOM 203 C GLN A 538 37.501 -6.588 26.307 1.00 16.63 A C ANISOU 203 C GLN A 538 1969 1960 2391 -191 -421 -328 A C ATOM 204 O GLN A 538 37.314 -7.059 27.428 1.00 18.67 A O ANISOU 204 O GLN A 538 2272 2256 2565 -183 -458 -356 A O ATOM 205 CB GLN A 538 35.304 -7.265 25.264 1.00 11.20 A C ANISOU 205 CB GLN A 538 1316 1290 1648 -126 -299 -264 A C ATOM 206 CG GLN A 538 33.992 -6.768 24.645 1.00 11.32 A C ANISOU 206 CG GLN A 538 1351 1281 1671 -100 -230 -251 A C ATOM 207 CD GLN A 538 32.953 -7.853 24.611 1.00 11.22 A C ANISOU 207 CD GLN A 538 1354 1314 1594 -66 -197 -219 A C ATOM 208 NE2 GLN A 538 31.937 -7.637 23.806 1.00 10.79 A N ANISOU 208 NE2 GLN A 538 1297 1246 1558 -44 -146 -192 A N ATOM 209 OE1 GLN A 538 33.069 -8.905 25.285 1.00 12.51 A O ANISOU 209 OE1 GLN A 538 1531 1524 1697 -60 -221 -214 A O ATOM 210 N LYS A 539 38.717 -6.503 25.728 1.00 14.79 A N ANISOU 210 N LYS A 539 1668 1710 2241 -220 -447 -308 A N ATOM 211 CA LYS A 539 39.969 -6.899 26.396 1.00 15.08 A C ANISOU 211 CA LYS A 539 1669 1771 2291 -245 -531 -322 A C ATOM 212 C LYS A 539 39.939 -8.347 26.807 1.00 19.18 A C ANISOU 212 C LYS A 539 2196 2353 2738 -213 -555 -287 A C ATOM 213 O LYS A 539 40.492 -8.741 27.845 1.00 19.51 A O ANISOU 213 O LYS A 539 2247 2427 2740 -219 -633 -307 A O ATOM 214 CB LYS A 539 40.301 -6.001 27.612 1.00 18.14 A C ANISOU 214 CB LYS A 539 2091 2140 2664 -278 -603 -402 A C ATOM 215 CG LYS A 539 40.329 -4.517 27.322 1.00 23.58 A C ANISOU 215 CG LYS A 539 2776 2752 3429 -312 -583 -444 A C ATOM 216 CD LYS A 539 40.585 -3.776 28.637 1.00 35.83 A C ANISOU 216 CD LYS A 539 4374 4290 4950 -343 -659 -535 A C ATOM 217 CE LYS A 539 39.664 -2.603 28.878 1.00 46.60 A C ANISOU 217 CE LYS A 539 5801 5597 6307 -343 -616 -596 A C ATOM 218 NZ LYS A 539 39.858 -1.528 27.868 1.00 45.37 A N ANISOU 218 NZ LYS A 539 5602 5359 6276 -368 -571 -584 A N ATOM 219 N MET A 540 39.247 -9.157 25.995 1.00 16.74 A N ANISOU 219 N MET A 540 1887 2062 2412 -179 -489 -234 A N ATOM 220 CA AMET A 540 39.241 -10.578 26.254 0.50 17.09 A C ANISOU 220 CA AMET A 540 1933 2155 2404 -150 -504 -196 A C ATOM 221 CA BMET A 540 39.046 -10.579 26.253 0.50 16.03 A C ANISOU 221 CA BMET A 540 1808 2022 2261 -147 -496 -196 A C ATOM 222 C MET A 540 39.165 -11.350 24.965 1.00 17.92 A C ANISOU 222 C MET A 540 1998 2262 2547 -129 -443 -139 A C ATOM 223 O MET A 540 38.767 -10.804 23.923 1.00 15.46 A O ANISOU 223 O MET A 540 1677 1924 2273 -131 -381 -127 A O ATOM 224 CB AMET A 540 38.204 -10.996 27.303 0.50 20.22 A C ANISOU 224 CB AMET A 540 2409 2584 2689 -127 -507 -210 A C ATOM 225 CB BMET A 540 37.617 -10.803 26.806 0.50 18.00 A C ANISOU 225 CB BMET A 540 2135 2291 2415 -120 -460 -204 A C ATOM 226 CG AMET A 540 36.804 -10.729 26.908 0.50 24.00 A C ANISOU 226 CG AMET A 540 2929 3052 3138 -108 -428 -209 A C ATOM 227 CG BMET A 540 37.418 -10.331 28.252 0.50 22.77 A C ANISOU 227 CG BMET A 540 2802 2907 2941 -129 -506 -260 A C ATOM 228 SD AMET A 540 35.733 -11.350 28.207 0.50 29.80 A S ANISOU 228 SD AMET A 540 3746 3830 3748 -84 -425 -220 A S ATOM 229 SD BMET A 540 38.580 -11.021 29.467 0.50 29.11 A S ANISOU 229 SD BMET A 540 3606 3753 3703 -140 -619 -264 A S ATOM 230 CE AMET A 540 34.171 -10.875 27.534 0.50 24.78 A C ANISOU 230 CE AMET A 540 3130 3172 3114 -64 -329 -219 A C ATOM 231 CE BMET A 540 38.097 -12.739 29.476 0.50 25.43 A C ANISOU 231 CE BMET A 540 3153 3331 3179 -98 -597 -191 A C ATOM 232 N PRO A 541 39.603 -12.629 24.967 1.00 16.60 A N ANISOU 232 N PRO A 541 1807 2125 2376 -108 -461 -102 A N ATOM 233 CA PRO A 541 39.577 -13.369 23.705 1.00 14.45 A C ANISOU 233 CA PRO A 541 1499 1852 2140 -90 -400 -58 A C ATOM 234 C PRO A 541 38.122 -13.608 23.254 1.00 14.26 A C ANISOU 234 C PRO A 541 1527 1833 2060 -69 -337 -46 A C ATOM 235 O PRO A 541 37.166 -13.543 24.067 1.00 13.48 A O ANISOU 235 O PRO A 541 1484 1745 1891 -61 -340 -62 A O ATOM 236 CB PRO A 541 40.227 -14.712 24.055 1.00 17.90 A C ANISOU 236 CB PRO A 541 1911 2314 2578 -68 -439 -29 A C ATOM 237 CG PRO A 541 40.040 -14.849 25.540 1.00 24.64 A C ANISOU 237 CG PRO A 541 2814 3191 3356 -66 -507 -45 A C ATOM 238 CD PRO A 541 40.148 -13.462 26.073 1.00 19.04 A C ANISOU 238 CD PRO A 541 2120 2466 2647 -99 -537 -97 A C ATOM 239 N VAL A 542 37.949 -13.834 21.944 1.00 11.88 A N ANISOU 239 N VAL A 542 1203 1522 1788 -61 -277 -19 A N ATOM 240 CA VAL A 542 36.635 -14.170 21.410 1.00 11.44 A C ANISOU 240 CA VAL A 542 1185 1473 1687 -43 -226 -4 A C ATOM 241 C VAL A 542 36.307 -15.595 21.841 1.00 12.52 A C ANISOU 241 C VAL A 542 1339 1635 1782 -19 -235 15 A C ATOM 242 O VAL A 542 37.087 -16.514 21.577 1.00 12.08 A O ANISOU 242 O VAL A 542 1250 1584 1756 -10 -243 34 A O ATOM 243 CB VAL A 542 36.559 -13.993 19.885 1.00 13.91 A C ANISOU 243 CB VAL A 542 1478 1775 2034 -44 -169 18 A C ATOM 244 CG1 VAL A 542 35.222 -14.479 19.357 1.00 12.81 A C ANISOU 244 CG1 VAL A 542 1372 1646 1848 -26 -132 32 A C ATOM 245 CG2 VAL A 542 36.765 -12.524 19.521 1.00 15.09 A C ANISOU 245 CG2 VAL A 542 1618 1893 2224 -67 -158 8 A C ATOM 246 N ILE A 543 35.234 -15.768 22.588 1.00 11.78 A N ANISOU 246 N ILE A 543 1294 1555 1628 -10 -234 10 A N ATOM 247 CA ILE A 543 34.833 -17.081 23.152 1.00 10.92 A C ANISOU 247 CA ILE A 543 1207 1466 1477 8 -240 33 A C ATOM 248 C ILE A 543 33.403 -17.378 22.731 1.00 12.74 A C ANISOU 248 C ILE A 543 1464 1699 1678 17 -190 42 A C ATOM 249 O ILE A 543 32.535 -16.481 22.745 1.00 13.31 A O ANISOU 249 O ILE A 543 1555 1768 1735 13 -167 24 A O ATOM 250 CB ILE A 543 34.933 -17.071 24.722 1.00 16.14 A C ANISOU 250 CB ILE A 543 1905 2145 2083 7 -291 22 A C ATOM 251 CG1 ILE A 543 36.326 -16.620 25.234 1.00 18.89 A C ANISOU 251 CG1 ILE A 543 2225 2491 2460 -6 -356 6 A C ATOM 252 CG2 ILE A 543 34.524 -18.427 25.385 1.00 20.22 A C ANISOU 252 CG2 ILE A 543 2450 2678 2553 25 -296 57 A C ATOM 253 CD1 ILE A 543 37.442 -17.621 25.120 1.00 28.20 A C ANISOU 253 CD1 ILE A 543 3359 3672 3683 5 -392 37 A C ATOM 254 N VAL A 544 33.136 -18.663 22.438 1.00 10.46 A N ANISOU 254 N VAL A 544 1174 1413 1387 29 -176 68 A N ATOM 255 CA VAL A 544 31.772 -19.105 22.151 1.00 10.13 A C ANISOU 255 CA VAL A 544 1152 1375 1322 32 -137 78 A C ATOM 256 C VAL A 544 31.061 -19.153 23.485 1.00 12.45 A C ANISOU 256 C VAL A 544 1485 1683 1562 34 -140 79 A C ATOM 257 O VAL A 544 31.490 -19.862 24.414 1.00 12.11 A O ANISOU 257 O VAL A 544 1459 1649 1493 39 -168 96 A O ATOM 258 CB VAL A 544 31.793 -20.487 21.481 1.00 11.57 A C ANISOU 258 CB VAL A 544 1323 1549 1525 40 -125 100 A C ATOM 259 CG1 VAL A 544 30.364 -20.991 21.259 1.00 11.18 A C ANISOU 259 CG1 VAL A 544 1289 1501 1458 38 -92 108 A C ATOM 260 CG2 VAL A 544 32.539 -20.393 20.153 1.00 11.73 A C ANISOU 260 CG2 VAL A 544 1310 1558 1590 39 -112 93 A C ATOM 261 N SER A 545 29.965 -18.398 23.612 1.00 10.11 A N ANISOU 261 N SER A 545 1205 1391 1247 32 -110 63 A N ATOM 262 CA SER A 545 29.248 -18.311 24.864 1.00 9.54 A C ANISOU 262 CA SER A 545 1172 1334 1120 35 -98 59 A C ATOM 263 C SER A 545 27.966 -19.130 24.925 1.00 12.03 A C ANISOU 263 C SER A 545 1494 1655 1423 37 -55 82 A C ATOM 264 O SER A 545 27.409 -19.327 26.017 1.00 13.28 A O ANISOU 264 O SER A 545 1686 1829 1532 39 -37 89 A O ATOM 265 CB SER A 545 28.959 -16.846 25.166 1.00 11.99 A C ANISOU 265 CB SER A 545 1494 1640 1422 33 -89 18 A C ATOM 266 OG SER A 545 28.298 -16.254 24.057 1.00 11.80 A O ANISOU 266 OG SER A 545 1442 1599 1442 35 -59 15 A O ATOM 267 N ARG A 546 27.452 -19.581 23.762 1.00 8.37 A N ANISOU 267 N ARG A 546 999 1180 1001 35 -36 94 A N ATOM 268 CA ARG A 546 26.242 -20.386 23.716 1.00 8.80 A C ANISOU 268 CA ARG A 546 1050 1236 1059 31 -1 115 A C ATOM 269 C ARG A 546 26.237 -21.112 22.388 1.00 9.81 A C ANISOU 269 C ARG A 546 1148 1349 1231 25 -6 123 A C ATOM 270 O ARG A 546 26.712 -20.577 21.370 1.00 9.44 A O ANISOU 270 O ARG A 546 1083 1297 1208 26 -19 109 A O ATOM 271 CB ARG A 546 24.979 -19.487 23.785 1.00 11.29 A C ANISOU 271 CB ARG A 546 1357 1557 1377 34 38 99 A C ATOM 272 CG ARG A 546 23.713 -20.313 24.012 1.00 18.08 A C ANISOU 272 CG ARG A 546 2208 2421 2243 28 78 122 A C ATOM 273 CD ARG A 546 22.458 -19.497 24.259 1.00 30.78 A C ANISOU 273 CD ARG A 546 3800 4035 3860 35 123 108 A C ATOM 274 NE ARG A 546 21.305 -20.401 24.271 1.00 43.48 A N ANISOU 274 NE ARG A 546 5384 5643 5491 23 158 134 A N ATOM 275 CZ ARG A 546 20.528 -20.641 23.219 1.00 57.42 A C ANISOU 275 CZ ARG A 546 7103 7401 7312 14 155 139 A C ATOM 276 NH1 ARG A 546 20.717 -19.983 22.080 1.00 34.55 A N ANISOU 276 NH1 ARG A 546 4186 4500 4442 21 122 124 A N ATOM 277 NH2 ARG A 546 19.532 -21.514 23.309 1.00 46.25 A N ANISOU 277 NH2 ARG A 546 5663 5984 5924 -2 184 161 A N ATOM 278 N VAL A 547 25.707 -22.334 22.391 1.00 9.25 A N ANISOU 278 N VAL A 547 1075 1270 1170 17 7 146 A N ATOM 279 CA VAL A 547 25.478 -23.114 21.185 1.00 9.01 A C ANISOU 279 CA VAL A 547 1023 1224 1178 8 6 146 A C ATOM 280 C VAL A 547 24.053 -23.628 21.328 1.00 11.60 A C ANISOU 280 C VAL A 547 1338 1549 1519 -7 35 159 A C ATOM 281 O VAL A 547 23.748 -24.339 22.307 1.00 12.19 A O ANISOU 281 O VAL A 547 1428 1620 1583 -12 54 185 A O ATOM 282 CB VAL A 547 26.474 -24.254 21.009 1.00 10.80 A C ANISOU 282 CB VAL A 547 1255 1429 1421 10 -13 157 A C ATOM 283 CG1 VAL A 547 26.087 -25.117 19.798 1.00 12.28 A C ANISOU 283 CG1 VAL A 547 1427 1596 1644 -2 -9 147 A C ATOM 284 CG2 VAL A 547 27.908 -23.712 20.867 1.00 10.78 A C ANISOU 284 CG2 VAL A 547 1251 1428 1416 24 -39 145 A C ATOM 285 N ALA A 548 23.180 -23.273 20.380 1.00 9.53 A N ANISOU 285 N ALA A 548 1047 1291 1283 -14 37 145 A N ATOM 286 CA ALA A 548 21.772 -23.639 20.449 1.00 10.08 A C ANISOU 286 CA ALA A 548 1091 1361 1379 -30 61 155 A C ATOM 287 C ALA A 548 21.487 -25.049 19.883 1.00 10.15 A C ANISOU 287 C ALA A 548 1090 1345 1423 -54 55 161 A C ATOM 288 O ALA A 548 22.062 -25.456 18.861 1.00 10.00 A O ANISOU 288 O ALA A 548 1074 1314 1412 -57 27 143 A O ATOM 289 CB ALA A 548 20.929 -22.607 19.724 1.00 11.43 A C ANISOU 289 CB ALA A 548 1229 1546 1569 -26 57 141 A C ATOM 290 N PRO A 549 20.572 -25.783 20.512 1.00 9.56 A N ANISOU 290 N PRO A 549 1003 1260 1370 -73 84 184 A N ATOM 291 CA PRO A 549 20.291 -27.144 20.040 1.00 9.27 A C ANISOU 291 CA PRO A 549 958 1190 1376 -100 77 187 A C ATOM 292 C PRO A 549 19.773 -27.213 18.601 1.00 9.85 A C ANISOU 292 C PRO A 549 1001 1260 1480 -117 44 155 A C ATOM 293 O PRO A 549 18.931 -26.413 18.217 1.00 10.63 A O ANISOU 293 O PRO A 549 1066 1383 1589 -118 38 147 A O ATOM 294 CB PRO A 549 19.182 -27.642 20.992 1.00 11.87 A C ANISOU 294 CB PRO A 549 1269 1512 1730 -120 123 221 A C ATOM 295 CG PRO A 549 19.321 -26.791 22.243 1.00 15.73 A C ANISOU 295 CG PRO A 549 1780 2029 2167 -97 157 239 A C ATOM 296 CD PRO A 549 19.795 -25.441 21.725 1.00 10.33 A C ANISOU 296 CD PRO A 549 1097 1371 1456 -71 130 206 A C ATOM 297 N GLY A 550 20.328 -28.138 17.815 1.00 9.60 A N ANISOU 297 N GLY A 550 985 1201 1462 -128 21 135 A N ATOM 298 CA GLY A 550 19.834 -28.422 16.469 1.00 9.98 A C ANISOU 298 CA GLY A 550 1016 1246 1532 -150 -14 99 A C ATOM 299 C GLY A 550 20.229 -27.424 15.416 1.00 11.17 A C ANISOU 299 C GLY A 550 1172 1428 1643 -132 -44 73 A C ATOM 300 O GLY A 550 19.704 -27.485 14.301 1.00 12.22 A O ANISOU 300 O GLY A 550 1294 1568 1780 -150 -78 47 A O ATOM 301 N THR A 551 21.132 -26.529 15.741 1.00 8.90 A N ANISOU 301 N THR A 551 904 1158 1318 -102 -35 82 A N ATOM 302 CA THR A 551 21.626 -25.541 14.809 1.00 9.16 A C ANISOU 302 CA THR A 551 946 1217 1316 -86 -55 67 A C ATOM 303 C THR A 551 22.926 -26.015 14.180 1.00 8.33 A C ANISOU 303 C THR A 551 874 1099 1192 -78 -56 45 A C ATOM 304 O THR A 551 23.522 -27.003 14.644 1.00 9.58 A O ANISOU 304 O THR A 551 1045 1226 1367 -77 -42 45 A O ATOM 305 CB THR A 551 21.859 -24.226 15.526 1.00 8.42 A C ANISOU 305 CB THR A 551 851 1145 1205 -61 -41 87 A C ATOM 306 CG2 THR A 551 20.551 -23.656 16.124 1.00 10.23 A C ANISOU 306 CG2 THR A 551 1045 1386 1456 -62 -30 103 A C ATOM 307 OG1 THR A 551 22.892 -24.371 16.506 1.00 8.05 A O ANISOU 307 OG1 THR A 551 827 1087 1146 -46 -21 97 A O ATOM 308 N PRO A 552 23.433 -25.362 13.125 1.00 8.43 A N ANISOU 308 N PRO A 552 900 1131 1171 -69 -68 29 A N ATOM 309 CA PRO A 552 24.678 -25.835 12.502 1.00 9.11 A C ANISOU 309 CA PRO A 552 1013 1205 1243 -61 -56 6 A C ATOM 310 C PRO A 552 25.833 -25.976 13.484 1.00 9.03 A C ANISOU 310 C PRO A 552 1005 1177 1248 -40 -33 22 A C ATOM 311 O PRO A 552 26.625 -26.936 13.388 1.00 9.57 A O ANISOU 311 O PRO A 552 1084 1217 1333 -34 -21 7 A O ATOM 312 CB PRO A 552 24.964 -24.771 11.425 1.00 9.92 A C ANISOU 312 CB PRO A 552 1128 1340 1303 -54 -63 2 A C ATOM 313 CG PRO A 552 23.542 -24.360 11.012 1.00 10.78 A C ANISOU 313 CG PRO A 552 1220 1470 1407 -69 -98 8 A C ATOM 314 CD PRO A 552 22.796 -24.288 12.324 1.00 9.51 A C ANISOU 314 CD PRO A 552 1028 1300 1285 -69 -91 33 A C ATOM 315 N ALA A 553 25.932 -25.049 14.440 1.00 7.79 A N ANISOU 315 N ALA A 553 838 1034 1087 -27 -30 49 A N ATOM 316 CA ALA A 553 27.017 -25.090 15.416 1.00 7.40 A C ANISOU 316 CA ALA A 553 791 974 1046 -10 -22 64 A C ATOM 317 C ALA A 553 26.913 -26.300 16.357 1.00 8.50 A C ANISOU 317 C ALA A 553 934 1084 1210 -12 -19 80 A C ATOM 318 O ALA A 553 27.915 -26.729 16.947 1.00 8.14 A O ANISOU 318 O ALA A 553 894 1022 1179 5 -19 92 A O ATOM 319 CB ALA A 553 27.069 -23.786 16.206 1.00 8.76 A C ANISOU 319 CB ALA A 553 959 1168 1203 0 -25 81 A C ATOM 320 N ASP A 554 25.670 -26.795 16.553 1.00 7.97 A N ANISOU 320 N ASP A 554 863 1010 1154 -32 -17 86 A N ATOM 321 CA ASP A 554 25.456 -27.954 17.404 1.00 7.52 A C ANISOU 321 CA ASP A 554 812 921 1124 -38 -8 108 A C ATOM 322 C ASP A 554 25.674 -29.251 16.630 1.00 8.86 A C ANISOU 322 C ASP A 554 989 1049 1330 -47 -8 86 A C ATOM 323 O ASP A 554 25.886 -30.290 17.245 1.00 8.88 A O ANISOU 323 O ASP A 554 999 1012 1363 -45 -1 106 A O ATOM 324 CB ASP A 554 24.009 -27.903 17.907 1.00 7.51 A C ANISOU 324 CB ASP A 554 797 929 1129 -60 3 125 A C ATOM 325 CG ASP A 554 23.619 -29.033 18.804 1.00 9.10 A C ANISOU 325 CG ASP A 554 1003 1096 1357 -73 20 157 A C ATOM 326 OD1 ASP A 554 24.342 -29.278 19.806 1.00 9.63 A O ANISOU 326 OD1 ASP A 554 1091 1155 1412 -56 25 189 A O ATOM 327 OD2 ASP A 554 22.614 -29.702 18.504 1.00 10.29 A O ANISOU 327 OD2 ASP A 554 1138 1227 1543 -102 26 153 A O ATOM 328 N LEU A 555 25.501 -29.198 15.290 1.00 8.28 A N ANISOU 328 N LEU A 555 915 982 1250 -57 -16 44 A N ATOM 329 CA LEU A 555 25.509 -30.427 14.472 1.00 9.16 A C ANISOU 329 CA LEU A 555 1038 1051 1391 -71 -15 8 A C ATOM 330 C LEU A 555 26.750 -30.625 13.632 1.00 10.34 A C ANISOU 330 C LEU A 555 1202 1190 1536 -49 -4 -26 A C ATOM 331 O LEU A 555 26.846 -31.622 12.910 1.00 10.41 A O ANISOU 331 O LEU A 555 1225 1162 1567 -56 2 -64 A O ATOM 332 CB LEU A 555 24.267 -30.421 13.554 1.00 9.14 A C ANISOU 332 CB LEU A 555 1029 1062 1383 -104 -36 -22 A C ATOM 333 CG LEU A 555 22.926 -30.280 14.247 1.00 9.94 A C ANISOU 333 CG LEU A 555 1102 1171 1503 -128 -42 7 A C ATOM 334 CD1 LEU A 555 21.815 -30.202 13.220 1.00 10.40 A C ANISOU 334 CD1 LEU A 555 1146 1246 1561 -159 -73 -24 A C ATOM 335 CD2 LEU A 555 22.681 -31.488 15.169 1.00 11.73 A C ANISOU 335 CD2 LEU A 555 1328 1347 1783 -143 -24 32 A C ATOM 336 N CYS A 556 27.725 -29.723 13.777 1.00 9.26 A N ANISOU 336 N CYS A 556 1060 1080 1377 -23 2 -13 A N ATOM 337 CA CYS A 556 28.920 -29.789 12.967 1.00 8.71 A C ANISOU 337 CA CYS A 556 997 1006 1307 -2 22 -41 A C ATOM 338 C CYS A 556 29.900 -30.843 13.417 1.00 10.74 A C ANISOU 338 C CYS A 556 1250 1214 1619 23 37 -38 A C ATOM 339 O CYS A 556 29.700 -31.496 14.450 1.00 9.99 A O ANISOU 339 O CYS A 556 1151 1087 1556 24 27 -4 A O ATOM 340 CB CYS A 556 29.543 -28.406 12.828 1.00 9.43 A C ANISOU 340 CB CYS A 556 1078 1142 1364 11 26 -29 A C ATOM 341 SG CYS A 556 29.826 -27.559 14.380 1.00 10.71 A S ANISOU 341 SG CYS A 556 1219 1320 1531 23 9 22 A S ATOM 342 N VAL A 557 30.972 -31.016 12.631 1.00 11.46 A N ANISOU 342 N VAL A 557 1340 1295 1721 44 64 -69 A N ATOM 343 CA VAL A 557 31.971 -32.057 12.850 1.00 13.26 A C ANISOU 343 CA VAL A 557 1557 1469 2012 74 82 -73 A C ATOM 344 C VAL A 557 33.318 -31.461 13.251 1.00 15.42 A C ANISOU 344 C VAL A 557 1796 1757 2305 106 89 -48 A C ATOM 345 O VAL A 557 34.032 -30.983 12.349 1.00 17.68 A O ANISOU 345 O VAL A 557 2074 2063 2580 115 121 -77 A O ATOM 346 CB VAL A 557 32.120 -32.930 11.583 1.00 17.10 A C ANISOU 346 CB VAL A 557 2065 1922 2509 75 117 -139 A C ATOM 347 CG1 VAL A 557 33.241 -33.967 11.754 1.00 17.95 A C ANISOU 347 CG1 VAL A 557 2157 1969 2695 114 143 -145 A C ATOM 348 CG2 VAL A 557 30.796 -33.573 11.189 1.00 16.64 A C ANISOU 348 CG2 VAL A 557 2039 1846 2439 37 100 -168 A C ATOM 349 N PRO A 558 33.744 -31.530 14.531 1.00 12.45 A N ANISOU 349 N PRO A 558 1400 1371 1961 124 61 3 A N ATOM 350 CA PRO A 558 32.955 -31.917 15.708 1.00 11.67 A C ANISOU 350 CA PRO A 558 1314 1259 1863 113 28 47 A C ATOM 351 C PRO A 558 32.106 -30.717 16.121 1.00 11.51 A C ANISOU 351 C PRO A 558 1301 1294 1778 87 9 65 A C ATOM 352 O PRO A 558 32.172 -29.659 15.472 1.00 11.61 A O ANISOU 352 O PRO A 558 1309 1347 1755 80 17 44 A O ATOM 353 CB PRO A 558 34.039 -32.267 16.730 1.00 12.83 A C ANISOU 353 CB PRO A 558 1436 1384 2056 148 6 92 A C ATOM 354 CG PRO A 558 35.091 -31.196 16.446 1.00 16.38 A C ANISOU 354 CG PRO A 558 1851 1872 2500 161 8 82 A C ATOM 355 CD PRO A 558 35.075 -31.025 14.947 1.00 14.28 A C ANISOU 355 CD PRO A 558 1591 1614 2222 153 55 24 A C ATOM 356 N ARG A 559 31.359 -30.859 17.197 1.00 10.43 A N ANISOU 356 N ARG A 559 1177 1157 1630 76 -10 104 A N ATOM 357 CA ARG A 559 30.495 -29.784 17.665 1.00 8.26 A C ANISOU 357 CA ARG A 559 909 929 1302 55 -21 117 A C ATOM 358 C ARG A 559 31.305 -28.569 18.073 1.00 8.68 A C ANISOU 358 C ARG A 559 947 1020 1331 68 -37 126 A C ATOM 359 O ARG A 559 32.385 -28.729 18.626 1.00 10.77 A O ANISOU 359 O ARG A 559 1197 1275 1619 91 -54 144 A O ATOM 360 CB ARG A 559 29.719 -30.290 18.884 1.00 9.26 A C ANISOU 360 CB ARG A 559 1052 1044 1423 45 -28 162 A C ATOM 361 CG ARG A 559 28.550 -29.372 19.185 1.00 11.18 A C ANISOU 361 CG ARG A 559 1300 1328 1622 22 -24 165 A C ATOM 362 CD ARG A 559 28.183 -29.507 20.631 1.00 14.23 A C ANISOU 362 CD ARG A 559 1703 1718 1986 21 -27 214 A C ATOM 363 NE ARG A 559 26.902 -28.881 20.942 1.00 9.81 A N ANISOU 363 NE ARG A 559 1145 1186 1396 -1 -9 216 A N ATOM 364 CZ ARG A 559 26.742 -28.046 21.948 1.00 10.48 A C ANISOU 364 CZ ARG A 559 1242 1305 1435 3 -8 233 A C ATOM 365 NH1 ARG A 559 27.796 -27.663 22.688 1.00 12.30 A N ANISOU 365 NH1 ARG A 559 1486 1549 1639 24 -34 246 A N ATOM 366 NH2 ARG A 559 25.539 -27.574 22.232 1.00 12.19 A N ANISOU 366 NH2 ARG A 559 1456 1541 1634 -13 18 235 A N ATOM 367 N LEU A 560 30.748 -27.369 17.858 1.00 9.03 A N ANISOU 367 N LEU A 560 993 1103 1335 53 -35 114 A N ATOM 368 CA LEU A 560 31.339 -26.155 18.420 1.00 8.49 A C ANISOU 368 CA LEU A 560 915 1065 1246 59 -52 122 A C ATOM 369 C LEU A 560 30.850 -26.133 19.874 1.00 12.37 A C ANISOU 369 C LEU A 560 1426 1565 1710 57 -70 154 A C ATOM 370 O LEU A 560 29.684 -26.464 20.144 1.00 14.91 A O ANISOU 370 O LEU A 560 1764 1886 2017 43 -57 164 A O ATOM 371 CB LEU A 560 30.834 -24.928 17.661 1.00 9.02 A C ANISOU 371 CB LEU A 560 980 1160 1287 45 -41 101 A C ATOM 372 CG LEU A 560 31.487 -23.618 18.062 1.00 10.22 A C ANISOU 372 CG LEU A 560 1122 1332 1429 48 -55 101 A C ATOM 373 CD1 LEU A 560 32.969 -23.582 17.694 1.00 11.75 A C ANISOU 373 CD1 LEU A 560 1287 1518 1658 60 -57 96 A C ATOM 374 CD2 LEU A 560 30.752 -22.472 17.391 1.00 11.49 A C ANISOU 374 CD2 LEU A 560 1286 1511 1568 35 -43 89 A C ATOM 375 N ASN A 561 31.720 -25.804 20.821 1.00 10.20 A N ANISOU 375 N ASN A 561 1149 1299 1428 70 -101 170 A N ATOM 376 CA ASN A 561 31.330 -25.847 22.228 1.00 9.80 A C ANISOU 376 CA ASN A 561 1127 1260 1336 69 -117 201 A C ATOM 377 C ASN A 561 31.477 -24.526 22.934 1.00 10.40 A C ANISOU 377 C ASN A 561 1212 1369 1370 65 -137 189 A C ATOM 378 O ASN A 561 32.393 -23.742 22.658 1.00 10.33 A O ANISOU 378 O ASN A 561 1180 1367 1377 67 -156 169 A O ATOM 379 CB ASN A 561 32.146 -26.909 22.982 1.00 10.07 A C ANISOU 379 CB ASN A 561 1165 1273 1389 88 -148 240 A C ATOM 380 CG ASN A 561 31.820 -28.293 22.570 1.00 12.82 A C ANISOU 380 CG ASN A 561 1514 1578 1777 91 -127 256 A C ATOM 381 ND2 ASN A 561 32.814 -29.016 22.073 1.00 13.13 A N ANISOU 381 ND2 ASN A 561 1529 1585 1874 112 -135 256 A N ATOM 382 OD1 ASN A 561 30.660 -28.707 22.697 1.00 15.38 A O ANISOU 382 OD1 ASN A 561 1859 1896 2088 74 -99 267 A O ATOM 383 N GLU A 562 30.630 -24.319 23.922 1.00 9.69 A N ANISOU 383 N GLU A 562 1155 1297 1230 57 -129 201 A N ATOM 384 CA GLU A 562 30.791 -23.171 24.812 1.00 9.42 A C ANISOU 384 CA GLU A 562 1140 1290 1148 55 -149 185 A C ATOM 385 C GLU A 562 32.166 -23.214 25.447 1.00 12.74 A C ANISOU 385 C GLU A 562 1557 1714 1569 66 -207 195 A C ATOM 386 O GLU A 562 32.654 -24.305 25.810 1.00 13.03 A O ANISOU 386 O GLU A 562 1595 1738 1616 79 -231 232 A O ATOM 387 CB GLU A 562 29.716 -23.201 25.902 1.00 10.83 A C ANISOU 387 CB GLU A 562 1361 1486 1266 49 -124 200 A C ATOM 388 CG GLU A 562 28.350 -22.970 25.340 1.00 13.15 A C ANISOU 388 CG GLU A 562 1648 1780 1570 39 -70 187 A C ATOM 389 CD GLU A 562 27.574 -24.207 24.951 1.00 25.28 A C ANISOU 389 CD GLU A 562 3176 3295 3135 32 -40 216 A C ATOM 390 OE1 GLU A 562 28.179 -25.298 24.756 1.00 19.52 A O ANISOU 390 OE1 GLU A 562 2441 2541 2433 37 -58 241 A O ATOM 391 OE2 GLU A 562 26.329 -24.066 24.861 1.00 24.90 A O ANISOU 391 OE2 GLU A 562 3123 3252 3088 21 1 213 A O ATOM 392 N GLY A 563 32.818 -22.062 25.479 1.00 10.84 A N ANISOU 392 N GLY A 563 1304 1485 1329 60 -233 162 A N ATOM 393 CA GLY A 563 34.160 -21.971 26.039 1.00 11.14 A C ANISOU 393 CA GLY A 563 1328 1529 1377 66 -297 165 A C ATOM 394 C GLY A 563 35.256 -22.083 24.999 1.00 11.83 A C ANISOU 394 C GLY A 563 1354 1595 1545 72 -306 160 A C ATOM 395 O GLY A 563 36.416 -21.731 25.281 1.00 13.63 A O ANISOU 395 O GLY A 563 1552 1826 1800 72 -357 155 A O ATOM 396 N ASP A 564 34.888 -22.498 23.761 1.00 9.69 A N ANISOU 396 N ASP A 564 1062 1304 1314 74 -255 158 A N ATOM 397 CA ASP A 564 35.895 -22.573 22.721 1.00 9.25 A C ANISOU 397 CA ASP A 564 954 1233 1329 81 -249 149 A C ATOM 398 C ASP A 564 36.351 -21.170 22.383 1.00 10.69 A C ANISOU 398 C ASP A 564 1114 1423 1526 62 -251 119 A C ATOM 399 O ASP A 564 35.521 -20.260 22.236 1.00 10.66 A O ANISOU 399 O ASP A 564 1133 1425 1491 47 -228 99 A O ATOM 400 CB ASP A 564 35.318 -23.202 21.454 1.00 10.11 A C ANISOU 400 CB ASP A 564 1059 1324 1459 83 -192 145 A C ATOM 401 CG ASP A 564 35.141 -24.724 21.454 1.00 13.08 A C ANISOU 401 CG ASP A 564 1442 1675 1851 101 -184 170 A C ATOM 402 OD1 ASP A 564 35.553 -25.377 22.442 1.00 12.21 A O ANISOU 402 OD1 ASP A 564 1338 1560 1742 115 -222 201 A O ATOM 403 OD2 ASP A 564 34.556 -25.236 20.470 1.00 12.25 A O ANISOU 403 OD2 ASP A 564 1341 1555 1757 98 -141 158 A O ATOM 404 N GLN A 565 37.671 -20.971 22.262 1.00 10.10 A N ANISOU 404 N GLN A 565 988 1341 1507 64 -279 116 A N ATOM 405 CA GLN A 565 38.221 -19.659 21.936 1.00 10.98 A C ANISOU 405 CA GLN A 565 1072 1453 1647 42 -280 91 A C ATOM 406 C GLN A 565 38.441 -19.601 20.430 1.00 12.04 A C ANISOU 406 C GLN A 565 1174 1574 1828 41 -219 87 A C ATOM 407 O GLN A 565 39.087 -20.503 19.869 1.00 12.71 A O ANISOU 407 O GLN A 565 1224 1648 1957 59 -201 98 A O ATOM 408 CB GLN A 565 39.560 -19.457 22.653 1.00 12.32 A C ANISOU 408 CB GLN A 565 1197 1624 1860 39 -346 90 A C ATOM 409 CG GLN A 565 40.182 -18.111 22.299 1.00 21.20 A C ANISOU 409 CG GLN A 565 2286 2741 3028 10 -346 64 A C ATOM 410 CD GLN A 565 41.544 -17.877 22.912 1.00 41.34 A C ANISOU 410 CD GLN A 565 4779 5291 5636 1 -414 61 A C ATOM 411 NE2 GLN A 565 42.328 -16.996 22.293 1.00 25.13 A N ANISOU 411 NE2 GLN A 565 2672 3223 3654 -23 -400 47 A N ATOM 412 OE1 GLN A 565 41.890 -18.432 23.962 1.00 40.28 A O ANISOU 412 OE1 GLN A 565 4650 5171 5485 12 -483 73 A O ATOM 413 N VAL A 566 37.906 -18.557 19.773 1.00 10.52 A N ANISOU 413 N VAL A 566 994 1380 1623 22 -184 73 A N ATOM 414 CA VAL A 566 38.039 -18.459 18.317 1.00 10.38 A C ANISOU 414 CA VAL A 566 957 1354 1631 20 -124 74 A C ATOM 415 C VAL A 566 39.392 -17.856 17.958 1.00 12.17 A C ANISOU 415 C VAL A 566 1125 1571 1929 7 -120 73 A C ATOM 416 O VAL A 566 39.698 -16.741 18.386 1.00 14.16 A O ANISOU 416 O VAL A 566 1366 1817 2198 -16 -145 63 A O ATOM 417 CB VAL A 566 36.862 -17.667 17.719 1.00 13.34 A C ANISOU 417 CB VAL A 566 1372 1731 1964 8 -92 71 A C ATOM 418 CG1 VAL A 566 36.953 -17.614 16.191 1.00 13.09 A C ANISOU 418 CG1 VAL A 566 1332 1697 1942 6 -34 77 A C ATOM 419 CG2 VAL A 566 35.534 -18.317 18.125 1.00 13.08 A C ANISOU 419 CG2 VAL A 566 1385 1709 1875 19 -96 72 A C ATOM 420 N VAL A 567 40.217 -18.591 17.195 1.00 10.70 A N ANISOU 420 N VAL A 567 897 1378 1789 21 -86 80 A N ATOM 421 CA VAL A 567 41.555 -18.142 16.791 1.00 11.41 A C ANISOU 421 CA VAL A 567 918 1459 1958 10 -70 81 A C ATOM 422 C VAL A 567 41.511 -17.569 15.378 1.00 13.88 A C ANISOU 422 C VAL A 567 1233 1769 2271 -3 8 86 A C ATOM 423 O VAL A 567 42.017 -16.467 15.153 1.00 13.86 A O ANISOU 423 O VAL A 567 1204 1758 2306 -30 20 90 A O ATOM 424 CB VAL A 567 42.565 -19.327 16.883 1.00 15.75 A C ANISOU 424 CB VAL A 567 1413 2002 2569 39 -75 88 A C ATOM 425 CG1 VAL A 567 43.955 -18.919 16.370 1.00 18.11 A C ANISOU 425 CG1 VAL A 567 1628 2291 2961 30 -47 90 A C ATOM 426 CG2 VAL A 567 42.642 -19.844 18.324 1.00 15.48 A C ANISOU 426 CG2 VAL A 567 1380 1971 2529 53 -161 94 A C ATOM 427 N LEU A 568 40.886 -18.308 14.435 1.00 11.05 A N ANISOU 427 N LEU A 568 911 1418 1868 13 59 85 A N ATOM 428 CA LEU A 568 40.759 -17.852 13.037 1.00 11.50 A C ANISOU 428 CA LEU A 568 984 1480 1904 2 131 92 A C ATOM 429 C LEU A 568 39.331 -17.951 12.596 1.00 11.43 A C ANISOU 429 C LEU A 568 1047 1484 1812 5 135 91 A C ATOM 430 O LEU A 568 38.597 -18.847 13.023 1.00 10.71 A O ANISOU 430 O LEU A 568 983 1396 1688 21 108 80 A O ATOM 431 CB LEU A 568 41.530 -18.734 12.063 1.00 12.84 A C ANISOU 431 CB LEU A 568 1127 1650 2101 21 197 86 A C ATOM 432 CG LEU A 568 43.038 -18.952 12.246 1.00 16.98 A C ANISOU 432 CG LEU A 568 1567 2162 2724 28 211 86 A C ATOM 433 CD1 LEU A 568 43.592 -19.832 11.104 1.00 16.63 A C ANISOU 433 CD1 LEU A 568 1508 2118 2695 51 296 74 A C ATOM 434 CD2 LEU A 568 43.813 -17.634 12.274 1.00 15.17 A C ANISOU 434 CD2 LEU A 568 1288 1925 2551 -6 216 103 A C ATOM 435 N ILE A 569 38.924 -17.008 11.713 1.00 10.23 A N ANISOU 435 N ILE A 569 921 1337 1628 -13 169 107 A N ATOM 436 CA ILE A 569 37.632 -17.033 11.074 1.00 9.02 A C ANISOU 436 CA ILE A 569 828 1199 1400 -11 173 110 A C ATOM 437 C ILE A 569 37.913 -16.979 9.595 1.00 11.76 A C ANISOU 437 C ILE A 569 1190 1559 1720 -15 240 121 A C ATOM 438 O ILE A 569 38.464 -15.974 9.120 1.00 12.40 A O ANISOU 438 O ILE A 569 1257 1634 1821 -33 273 146 A O ATOM 439 CB ILE A 569 36.714 -15.875 11.509 1.00 10.47 A C ANISOU 439 CB ILE A 569 1036 1377 1565 -24 137 125 A C ATOM 440 CG1 ILE A 569 36.476 -15.976 13.022 1.00 12.10 A C ANISOU 440 CG1 ILE A 569 1235 1575 1789 -19 79 109 A C ATOM 441 CG2 ILE A 569 35.385 -15.904 10.697 1.00 11.21 A C ANISOU 441 CG2 ILE A 569 1182 1488 1588 -20 140 134 A C ATOM 442 CD1 ILE A 569 35.697 -14.851 13.611 1.00 15.69 A C ANISOU 442 CD1 ILE A 569 1708 2018 2235 -28 50 113 A C ATOM 443 N ASN A 570 37.523 -18.020 8.856 1.00 11.01 A N ANISOU 443 N ASN A 570 1127 1479 1576 -1 262 101 A N ATOM 444 CA ASN A 570 37.829 -18.088 7.422 1.00 11.42 A C ANISOU 444 CA ASN A 570 1203 1549 1588 -4 331 104 A C ATOM 445 C ASN A 570 39.304 -17.765 7.161 1.00 14.84 A C ANISOU 445 C ASN A 570 1583 1973 2084 -9 392 114 A C ATOM 446 O ASN A 570 39.636 -17.018 6.239 1.00 16.10 A O ANISOU 446 O ASN A 570 1753 2141 2225 -24 446 141 A O ATOM 447 CB ASN A 570 36.904 -17.183 6.616 1.00 12.46 A C ANISOU 447 CB ASN A 570 1386 1697 1649 -18 328 135 A C ATOM 448 CG ASN A 570 35.480 -17.645 6.725 1.00 12.74 A C ANISOU 448 CG ASN A 570 1464 1745 1630 -12 273 121 A C ATOM 449 ND2 ASN A 570 34.574 -16.696 6.788 1.00 11.82 A N ANISOU 449 ND2 ASN A 570 1368 1631 1493 -20 236 151 A N ATOM 450 OD1 ASN A 570 35.201 -18.854 6.707 1.00 13.87 A O ANISOU 450 OD1 ASN A 570 1620 1892 1758 -1 265 84 A O ATOM 451 N GLY A 571 40.163 -18.320 8.002 1.00 13.92 A N ANISOU 451 N GLY A 571 1407 1837 2044 4 381 97 A N ATOM 452 CA GLY A 571 41.617 -18.165 7.856 1.00 15.02 A C ANISOU 452 CA GLY A 571 1478 1965 2263 2 435 103 A C ATOM 453 C GLY A 571 42.251 -16.907 8.396 1.00 19.08 A C ANISOU 453 C GLY A 571 1943 2464 2844 -26 420 133 A C ATOM 454 O GLY A 571 43.491 -16.795 8.422 1.00 22.03 A O ANISOU 454 O GLY A 571 2244 2825 3300 -30 455 137 A O ATOM 455 N ARG A 572 41.417 -15.959 8.849 1.00 15.19 A N ANISOU 455 N ARG A 572 1482 1966 2324 -44 367 150 A N ATOM 456 CA ARG A 572 41.880 -14.665 9.315 1.00 15.56 A C ANISOU 456 CA ARG A 572 1493 1990 2430 -74 351 174 A C ATOM 457 C ARG A 572 42.108 -14.644 10.792 1.00 16.13 A C ANISOU 457 C ARG A 572 1525 2045 2557 -75 271 154 A C ATOM 458 O ARG A 572 41.236 -15.057 11.545 1.00 13.72 A O ANISOU 458 O ARG A 572 1256 1747 2212 -60 213 137 A O ATOM 459 CB ARG A 572 40.844 -13.626 8.954 1.00 16.61 A C ANISOU 459 CB ARG A 572 1685 2120 2507 -89 342 201 A C ATOM 460 CG ARG A 572 41.272 -12.200 9.236 1.00 21.71 A C ANISOU 460 CG ARG A 572 2302 2732 3214 -123 337 227 A C ATOM 461 CD ARG A 572 40.077 -11.289 9.287 1.00 20.67 A C ANISOU 461 CD ARG A 572 2228 2589 3038 -127 304 246 A C ATOM 462 NE ARG A 572 39.256 -11.369 8.077 1.00 25.01 A N ANISOU 462 NE ARG A 572 2839 3162 3502 -117 339 274 A N ATOM 463 CZ ARG A 572 39.364 -10.557 7.031 1.00 40.51 A C ANISOU 463 CZ ARG A 572 4823 5119 5450 -133 392 323 A C ATOM 464 NH1 ARG A 572 40.262 -9.576 7.030 1.00 30.90 A N ANISOU 464 NH1 ARG A 572 3566 3868 4309 -164 422 351 A N ATOM 465 NH2 ARG A 572 38.549 -10.691 5.997 1.00 28.17 A N ANISOU 465 NH2 ARG A 572 3322 3585 3797 -122 409 348 A N ATOM 466 N ASP A 573 43.276 -14.147 11.215 1.00 16.65 A N ANISOU 466 N ASP A 573 1520 2092 2716 -95 267 157 A N ATOM 467 CA ASP A 573 43.627 -13.973 12.601 1.00 15.93 A C ANISOU 467 CA ASP A 573 1389 1986 2676 -102 185 139 A C ATOM 468 C ASP A 573 42.825 -12.781 13.130 1.00 18.63 A C ANISOU 468 C ASP A 573 1774 2310 2993 -125 141 139 A C ATOM 469 O ASP A 573 42.991 -11.650 12.653 1.00 20.86 A O ANISOU 469 O ASP A 573 2052 2569 3304 -155 171 160 A O ATOM 470 CB ASP A 573 45.147 -13.701 12.680 1.00 18.31 A C ANISOU 470 CB ASP A 573 1595 2271 3091 -122 198 143 A C ATOM 471 CG ASP A 573 45.695 -13.441 14.060 1.00 25.64 A C ANISOU 471 CG ASP A 573 2475 3187 4080 -135 105 123 A C ATOM 472 OD1 ASP A 573 44.899 -13.402 15.022 1.00 22.14 A O ANISOU 472 OD1 ASP A 573 2082 2747 3585 -130 33 105 A O ATOM 473 OD2 ASP A 573 46.917 -13.214 14.174 1.00 33.63 A O ANISOU 473 OD2 ASP A 573 3400 4185 5192 -154 104 126 A O ATOM 474 N ILE A 574 41.992 -13.018 14.128 1.00 14.44 A N ANISOU 474 N ILE A 574 1283 1786 2416 -112 75 118 A N ATOM 475 CA ILE A 574 41.126 -11.958 14.668 1.00 14.49 A C ANISOU 475 CA ILE A 574 1334 1775 2397 -127 40 111 A C ATOM 476 C ILE A 574 41.587 -11.303 15.973 1.00 18.07 A C ANISOU 476 C ILE A 574 1763 2208 2896 -149 -30 82 A C ATOM 477 O ILE A 574 40.819 -10.560 16.581 1.00 17.45 A O ANISOU 477 O ILE A 574 1726 2114 2789 -155 -61 65 A O ATOM 478 CB ILE A 574 39.675 -12.497 14.786 1.00 16.17 A C ANISOU 478 CB ILE A 574 1615 2008 2520 -99 28 106 A C ATOM 479 CG1 ILE A 574 39.618 -13.739 15.727 1.00 17.06 A C ANISOU 479 CG1 ILE A 574 1728 2143 2610 -74 -17 85 A C ATOM 480 CG2 ILE A 574 39.093 -12.768 13.389 1.00 19.78 A C ANISOU 480 CG2 ILE A 574 2105 2481 2931 -88 90 133 A C ATOM 481 CD1 ILE A 574 38.226 -14.068 16.244 1.00 20.69 A C ANISOU 481 CD1 ILE A 574 2247 2616 2997 -56 -40 76 A C ATOM 482 N ALA A 575 42.821 -11.567 16.419 1.00 17.99 A N ANISOU 482 N ALA A 575 1685 2196 2953 -159 -59 73 A N ATOM 483 CA ALA A 575 43.298 -11.049 17.711 1.00 19.03 A C ANISOU 483 CA ALA A 575 1795 2314 3120 -181 -140 40 A C ATOM 484 C ALA A 575 43.153 -9.561 17.970 1.00 23.11 A C ANISOU 484 C ALA A 575 2327 2791 3664 -219 -154 23 A C ATOM 485 O ALA A 575 42.893 -9.161 19.105 1.00 26.10 A O ANISOU 485 O ALA A 575 2732 3162 4022 -228 -220 -15 A O ATOM 486 CB ALA A 575 44.744 -11.485 17.942 1.00 20.98 A C ANISOU 486 CB ALA A 575 1954 2565 3454 -189 -167 40 A C ATOM 487 N GLU A 576 43.355 -8.739 16.962 1.00 18.70 A N ANISOU 487 N GLU A 576 1753 2202 3152 -242 -92 50 A N ATOM 488 CA GLU A 576 43.323 -7.294 17.219 1.00 18.74 A C ANISOU 488 CA GLU A 576 1766 2155 3201 -281 -106 35 A C ATOM 489 C GLU A 576 42.003 -6.654 16.828 1.00 16.75 A C ANISOU 489 C GLU A 576 1588 1884 2892 -267 -73 47 A C ATOM 490 O GLU A 576 41.875 -5.430 16.878 1.00 18.33 A O ANISOU 490 O GLU A 576 1800 2032 3132 -294 -72 42 A O ATOM 491 CB GLU A 576 44.491 -6.599 16.492 1.00 22.32 A C ANISOU 491 CB GLU A 576 2147 2573 3763 -324 -64 62 A C ATOM 492 CG GLU A 576 45.876 -7.189 16.771 1.00 36.39 A C ANISOU 492 CG GLU A 576 3835 4369 5622 -337 -90 54 A C ATOM 493 CD GLU A 576 46.355 -7.260 18.213 1.00 69.33 A C ANISOU 493 CD GLU A 576 7982 8545 9814 -349 -199 2 A C ATOM 494 OE1 GLU A 576 46.005 -6.363 19.015 1.00 68.29 A O ANISOU 494 OE1 GLU A 576 7887 8383 9676 -373 -252 -38 A O ATOM 495 OE2 GLU A 576 47.123 -8.198 18.529 1.00 70.46 A O ANISOU 495 OE2 GLU A 576 8070 8721 9983 -335 -233 1 A O ATOM 496 N HIS A 577 41.007 -7.495 16.476 1.00 13.65 A N ANISOU 496 N HIS A 577 1243 1531 2413 -226 -51 63 A N ATOM 497 CA HIS A 577 39.733 -7.025 15.992 1.00 12.91 A C ANISOU 497 CA HIS A 577 1210 1426 2269 -208 -22 81 A C ATOM 498 C HIS A 577 38.696 -6.880 17.078 1.00 13.23 A C ANISOU 498 C HIS A 577 1301 1466 2261 -190 -68 40 A C ATOM 499 O HIS A 577 38.682 -7.635 18.057 1.00 13.34 A O ANISOU 499 O HIS A 577 1321 1511 2239 -178 -113 7 A O ATOM 500 CB HIS A 577 39.204 -7.953 14.878 1.00 13.20 A C ANISOU 500 CB HIS A 577 1266 1503 2245 -178 28 121 A C ATOM 501 CG HIS A 577 39.982 -7.854 13.602 1.00 16.41 A C ANISOU 501 CG HIS A 577 1643 1908 2685 -194 92 166 A C ATOM 502 CD2 HIS A 577 39.949 -6.901 12.645 1.00 19.13 A C ANISOU 502 CD2 HIS A 577 1997 2221 3050 -211 141 211 A C ATOM 503 ND1 HIS A 577 40.869 -8.847 13.219 1.00 20.54 A N ANISOU 503 ND1 HIS A 577 2124 2461 3219 -189 118 171 A N ATOM 504 CE1 HIS A 577 41.396 -8.434 12.071 1.00 20.30 A C ANISOU 504 CE1 HIS A 577 2077 2420 3214 -206 186 213 A C ATOM 505 NE2 HIS A 577 40.850 -7.294 11.667 1.00 20.23 A N ANISOU 505 NE2 HIS A 577 2102 2377 3207 -220 201 242 A N ATOM 506 N THR A 578 37.833 -5.874 16.902 1.00 11.17 A N ANISOU 506 N THR A 578 1075 1166 2001 -187 -52 46 A N ATOM 507 CA THR A 578 36.792 -5.683 17.893 1.00 10.94 A C ANISOU 507 CA THR A 578 1093 1134 1930 -167 -81 5 A C ATOM 508 C THR A 578 35.752 -6.791 17.748 1.00 11.55 A C ANISOU 508 C THR A 578 1198 1264 1927 -128 -71 19 A C ATOM 509 O THR A 578 35.656 -7.484 16.715 1.00 10.99 A O ANISOU 509 O THR A 578 1120 1221 1834 -116 -39 61 A O ATOM 510 CB THR A 578 36.081 -4.349 17.678 1.00 11.54 A C ANISOU 510 CB THR A 578 1195 1150 2039 -167 -62 10 A C ATOM 511 CG2 THR A 578 37.011 -3.155 17.723 1.00 11.62 A C ANISOU 511 CG2 THR A 578 1181 1096 2141 -210 -66 -1 A C ATOM 512 OG1 THR A 578 35.315 -4.402 16.462 1.00 12.62 A O ANISOU 512 OG1 THR A 578 1346 1295 2155 -144 -18 70 A O ATOM 513 N HIS A 579 34.879 -6.877 18.760 1.00 9.91 A N ANISOU 513 N HIS A 579 1025 1065 1676 -108 -93 -18 A N ATOM 514 CA HIS A 579 33.764 -7.798 18.734 1.00 9.13 A C ANISOU 514 CA HIS A 579 950 1007 1512 -75 -81 -8 A C ATOM 515 C HIS A 579 32.940 -7.633 17.451 1.00 10.33 A C ANISOU 515 C HIS A 579 1108 1156 1662 -59 -43 41 A C ATOM 516 O HIS A 579 32.620 -8.638 16.803 1.00 9.53 A O ANISOU 516 O HIS A 579 1005 1093 1523 -45 -31 67 A O ATOM 517 CB HIS A 579 32.856 -7.502 19.951 1.00 9.33 A C ANISOU 517 CB HIS A 579 1012 1028 1506 -60 -95 -53 A C ATOM 518 CG HIS A 579 31.687 -8.424 20.119 1.00 9.54 A C ANISOU 518 CG HIS A 579 1058 1093 1473 -30 -81 -45 A C ATOM 519 CD2 HIS A 579 30.452 -8.364 19.566 1.00 10.44 A C ANISOU 519 CD2 HIS A 579 1179 1208 1580 -6 -52 -22 A C ATOM 520 ND1 HIS A 579 31.751 -9.541 20.934 1.00 9.89 A N ANISOU 520 ND1 HIS A 579 1113 1180 1466 -25 -100 -57 A N ATOM 521 CE1 HIS A 579 30.547 -10.114 20.865 1.00 8.86 A C ANISOU 521 CE1 HIS A 579 995 1071 1302 -2 -76 -43 A C ATOM 522 NE2 HIS A 579 29.730 -9.432 20.069 1.00 9.08 A N ANISOU 522 NE2 HIS A 579 1018 1076 1355 10 -50 -25 A N ATOM 523 N ASP A 580 32.498 -6.397 17.140 1.00 10.04 A N ANISOU 523 N ASP A 580 1080 1071 1664 -58 -29 52 A N ATOM 524 CA ASP A 580 31.639 -6.218 15.976 1.00 8.97 A C ANISOU 524 CA ASP A 580 952 935 1522 -38 -4 103 A C ATOM 525 C ASP A 580 32.392 -6.467 14.668 1.00 11.39 A C ANISOU 525 C ASP A 580 1245 1255 1830 -54 19 153 A C ATOM 526 O ASP A 580 31.754 -6.886 13.693 1.00 10.25 A O ANISOU 526 O ASP A 580 1111 1137 1648 -38 31 192 A O ATOM 527 CB ASP A 580 30.960 -4.859 16.015 1.00 10.04 A C ANISOU 527 CB ASP A 580 1100 1011 1704 -27 4 107 A C ATOM 528 CG ASP A 580 29.845 -4.731 17.049 1.00 9.76 A C ANISOU 528 CG ASP A 580 1081 971 1656 1 -2 64 A C ATOM 529 OD1 ASP A 580 29.471 -5.771 17.684 1.00 9.56 A O ANISOU 529 OD1 ASP A 580 1060 994 1578 11 -10 40 A O ATOM 530 OD2 ASP A 580 29.344 -3.601 17.227 1.00 12.52 A O ANISOU 530 OD2 ASP A 580 1440 1265 2053 13 6 57 A O ATOM 531 N GLN A 581 33.705 -6.248 14.634 1.00 10.25 A N ANISOU 531 N GLN A 581 1076 1094 1726 -85 25 151 A N ATOM 532 CA GLN A 581 34.468 -6.595 13.429 1.00 10.53 A C ANISOU 532 CA GLN A 581 1096 1148 1758 -98 59 195 A C ATOM 533 C GLN A 581 34.443 -8.099 13.220 1.00 12.97 A C ANISOU 533 C GLN A 581 1403 1516 2008 -84 59 188 A C ATOM 534 O GLN A 581 34.241 -8.562 12.081 1.00 12.63 A O ANISOU 534 O GLN A 581 1373 1501 1926 -76 87 223 A O ATOM 535 CB GLN A 581 35.891 -6.100 13.545 1.00 12.17 A C ANISOU 535 CB GLN A 581 1266 1326 2034 -135 68 191 A C ATOM 536 CG GLN A 581 35.994 -4.611 13.224 1.00 12.27 A C ANISOU 536 CG GLN A 581 1281 1273 2110 -155 85 218 A C ATOM 537 CD GLN A 581 37.303 -4.003 13.636 1.00 16.95 A C ANISOU 537 CD GLN A 581 1830 1825 2785 -198 83 200 A C ATOM 538 NE2 GLN A 581 37.426 -2.701 13.406 1.00 24.40 A N ANISOU 538 NE2 GLN A 581 2774 2701 3795 -221 98 223 A N ATOM 539 OE1 GLN A 581 38.142 -4.607 14.290 1.00 14.66 A O ANISOU 539 OE1 GLN A 581 1505 1555 2509 -212 59 163 A O ATOM 540 N VAL A 582 34.533 -8.861 14.328 1.00 9.71 A N ANISOU 540 N VAL A 582 983 1123 1584 -78 28 144 A N ATOM 541 CA VAL A 582 34.458 -10.334 14.303 1.00 9.93 A C ANISOU 541 CA VAL A 582 1010 1197 1565 -63 24 135 A C ATOM 542 C VAL A 582 33.082 -10.774 13.852 1.00 10.72 A C ANISOU 542 C VAL A 582 1143 1321 1612 -39 26 148 A C ATOM 543 O VAL A 582 32.963 -11.725 13.057 1.00 10.82 A O ANISOU 543 O VAL A 582 1160 1363 1586 -32 41 159 A O ATOM 544 CB VAL A 582 34.846 -10.879 15.701 1.00 11.44 A C ANISOU 544 CB VAL A 582 1190 1397 1761 -62 -15 94 A C ATOM 545 CG1 VAL A 582 34.421 -12.340 15.884 1.00 12.12 A C ANISOU 545 CG1 VAL A 582 1286 1520 1799 -42 -23 88 A C ATOM 546 CG2 VAL A 582 36.354 -10.739 15.912 1.00 12.60 A C ANISOU 546 CG2 VAL A 582 1293 1530 1963 -86 -22 86 A C ATOM 547 N VAL A 583 31.999 -10.130 14.337 1.00 9.08 A N ANISOU 547 N VAL A 583 952 1097 1401 -27 11 143 A N ATOM 548 CA VAL A 583 30.662 -10.460 13.889 1.00 8.48 A C ANISOU 548 CA VAL A 583 894 1040 1287 -6 9 158 A C ATOM 549 C VAL A 583 30.542 -10.271 12.369 1.00 11.30 A C ANISOU 549 C VAL A 583 1261 1405 1627 -7 27 204 A C ATOM 550 O VAL A 583 30.017 -11.186 11.693 1.00 10.05 A O ANISOU 550 O VAL A 583 1114 1282 1423 1 25 211 A O ATOM 551 CB VAL A 583 29.608 -9.631 14.669 1.00 9.89 A C ANISOU 551 CB VAL A 583 1080 1194 1483 10 -3 145 A C ATOM 552 CG1 VAL A 583 28.208 -9.718 14.046 1.00 10.25 A C ANISOU 552 CG1 VAL A 583 1132 1254 1510 32 -7 170 A C ATOM 553 CG2 VAL A 583 29.589 -10.052 16.123 1.00 9.80 A C ANISOU 553 CG2 VAL A 583 1071 1189 1464 12 -16 100 A C ATOM 554 N LEU A 584 31.063 -9.154 11.834 1.00 10.75 A N ANISOU 554 N LEU A 584 1192 1304 1589 -18 44 234 A N ATOM 555 CA LEU A 584 30.946 -8.980 10.379 1.00 10.39 A C ANISOU 555 CA LEU A 584 1165 1270 1514 -19 63 285 A C ATOM 556 C LEU A 584 31.757 -10.059 9.649 1.00 12.32 A C ANISOU 556 C LEU A 584 1411 1553 1718 -29 89 282 A C ATOM 557 O LEU A 584 31.275 -10.575 8.631 1.00 12.28 A O ANISOU 557 O LEU A 584 1431 1581 1655 -23 92 301 A O ATOM 558 CB LEU A 584 31.406 -7.581 9.964 1.00 11.32 A C ANISOU 558 CB LEU A 584 1284 1341 1676 -31 83 327 A C ATOM 559 CG LEU A 584 31.162 -7.242 8.450 1.00 14.96 A C ANISOU 559 CG LEU A 584 1775 1814 2097 -29 101 393 A C ATOM 560 CD1 LEU A 584 29.714 -7.476 8.057 1.00 16.09 A C ANISOU 560 CD1 LEU A 584 1938 1982 2195 -2 63 409 A C ATOM 561 CD2 LEU A 584 31.579 -5.823 8.140 1.00 17.78 A C ANISOU 561 CD2 LEU A 584 2134 2114 2508 -42 122 441 A C ATOM 562 N PHE A 585 32.958 -10.431 10.143 1.00 10.28 A N ANISOU 562 N PHE A 585 1125 1291 1490 -44 106 255 A N ATOM 563 CA PHE A 585 33.700 -11.504 9.460 1.00 10.04 A C ANISOU 563 CA PHE A 585 1092 1292 1431 -48 138 248 A C ATOM 564 C PHE A 585 32.866 -12.793 9.444 1.00 11.16 A C ANISOU 564 C PHE A 585 1252 1469 1521 -31 116 222 A C ATOM 565 O PHE A 585 32.843 -13.504 8.419 1.00 10.97 A O ANISOU 565 O PHE A 585 1249 1472 1446 -29 137 225 A O ATOM 566 CB PHE A 585 35.000 -11.812 10.189 1.00 11.22 A C ANISOU 566 CB PHE A 585 1198 1430 1634 -59 148 221 A C ATOM 567 CG PHE A 585 36.010 -10.702 10.089 1.00 12.78 A C ANISOU 567 CG PHE A 585 1368 1595 1893 -84 174 243 A C ATOM 568 CD1 PHE A 585 36.102 -9.916 8.935 1.00 16.72 A C ANISOU 568 CD1 PHE A 585 1885 2085 2382 -95 217 292 A C ATOM 569 CD2 PHE A 585 36.867 -10.433 11.141 1.00 16.38 A C ANISOU 569 CD2 PHE A 585 1781 2025 2415 -98 154 217 A C ATOM 570 CE1 PHE A 585 37.053 -8.889 8.834 1.00 19.79 A C ANISOU 570 CE1 PHE A 585 2245 2437 2837 -123 247 318 A C ATOM 571 CE2 PHE A 585 37.797 -9.395 11.050 1.00 19.54 A C ANISOU 571 CE2 PHE A 585 2151 2390 2884 -127 176 236 A C ATOM 572 CZ PHE A 585 37.870 -8.622 9.902 1.00 18.30 A C ANISOU 572 CZ PHE A 585 2009 2220 2725 -140 225 286 A C ATOM 573 N ILE A 586 32.152 -13.098 10.536 1.00 9.75 A N ANISOU 573 N ILE A 586 1067 1287 1351 -20 78 196 A N ATOM 574 CA ILE A 586 31.315 -14.299 10.503 1.00 8.98 A C ANISOU 574 CA ILE A 586 984 1216 1214 -9 60 176 A C ATOM 575 C ILE A 586 30.207 -14.184 9.457 1.00 11.02 A C ANISOU 575 C ILE A 586 1270 1493 1424 -5 48 199 A C ATOM 576 O ILE A 586 29.849 -15.179 8.831 1.00 12.39 A O ANISOU 576 O ILE A 586 1460 1692 1555 -4 45 186 A O ATOM 577 CB ILE A 586 30.749 -14.559 11.927 1.00 10.26 A C ANISOU 577 CB ILE A 586 1134 1370 1395 -1 28 151 A C ATOM 578 CG1 ILE A 586 31.929 -14.983 12.866 1.00 10.96 A C ANISOU 578 CG1 ILE A 586 1199 1449 1517 -5 30 129 A C ATOM 579 CG2 ILE A 586 29.659 -15.675 11.927 1.00 11.73 A C ANISOU 579 CG2 ILE A 586 1331 1577 1550 6 11 138 A C ATOM 580 CD1 ILE A 586 31.630 -14.901 14.382 1.00 10.35 A C ANISOU 580 CD1 ILE A 586 1117 1362 1452 0 0 110 A C ATOM 581 N LYS A 587 29.655 -12.990 9.303 1.00 9.45 A N ANISOU 581 N LYS A 587 1076 1280 1236 -1 37 232 A N ATOM 582 CA LYS A 587 28.556 -12.760 8.357 1.00 10.76 A C ANISOU 582 CA LYS A 587 1263 1462 1362 7 14 262 A C ATOM 583 C LYS A 587 29.060 -12.501 6.938 1.00 13.70 A C ANISOU 583 C LYS A 587 1668 1851 1687 -2 38 298 A C ATOM 584 O LYS A 587 28.231 -12.358 6.023 1.00 14.15 A O ANISOU 584 O LYS A 587 1749 1928 1697 3 13 327 A O ATOM 585 CB LYS A 587 27.669 -11.621 8.880 1.00 13.99 A C ANISOU 585 CB LYS A 587 1661 1844 1812 22 -11 284 A C ATOM 586 CG LYS A 587 27.058 -12.015 10.225 1.00 15.81 A C ANISOU 586 CG LYS A 587 1867 2067 2073 31 -26 246 A C ATOM 587 CD LYS A 587 25.979 -11.056 10.725 1.00 20.59 A C ANISOU 587 CD LYS A 587 2458 2648 2718 51 -44 259 A C ATOM 588 CE LYS A 587 24.658 -11.241 9.993 1.00 20.24 A C ANISOU 588 CE LYS A 587 2409 2626 2654 64 -79 283 A C ATOM 589 NZ LYS A 587 23.549 -10.566 10.742 1.00 25.16 A N ANISOU 589 NZ LYS A 587 3004 3227 3330 88 -90 284 A N ATOM 590 N ALA A 588 30.385 -12.442 6.720 1.00 12.54 A N ANISOU 590 N ALA A 588 1519 1698 1549 -15 87 298 A N ATOM 591 CA ALA A 588 30.931 -12.159 5.378 1.00 12.81 A C ANISOU 591 CA ALA A 588 1585 1748 1534 -25 125 336 A C ATOM 592 C ALA A 588 30.868 -13.441 4.550 1.00 12.90 A C ANISOU 592 C ALA A 588 1626 1802 1471 -26 133 305 A C ATOM 593 O ALA A 588 31.809 -14.229 4.494 1.00 13.85 A O ANISOU 593 O ALA A 588 1740 1929 1593 -31 176 272 A O ATOM 594 CB ALA A 588 32.368 -11.660 5.491 1.00 14.38 A C ANISOU 594 CB ALA A 588 1761 1922 1780 -41 182 345 A C ATOM 595 N SER A 589 29.702 -13.663 3.932 1.00 12.10 A N ANISOU 595 N SER A 589 1556 1729 1313 -20 87 313 A N ATOM 596 CA SER A 589 29.457 -14.897 3.188 1.00 10.34 A C ANISOU 596 CA SER A 589 1366 1543 1020 -24 81 274 A C ATOM 597 C SER A 589 30.433 -15.215 2.050 1.00 14.76 A C ANISOU 597 C SER A 589 1966 2128 1516 -34 144 271 A C ATOM 598 O SER A 589 30.655 -16.383 1.736 1.00 14.66 A O ANISOU 598 O SER A 589 1969 2131 1469 -36 161 218 A O ATOM 599 CB SER A 589 28.022 -14.930 2.662 1.00 11.97 A C ANISOU 599 CB SER A 589 1595 1775 1179 -21 11 287 A C ATOM 600 OG SER A 589 27.885 -13.959 1.631 1.00 15.04 A O ANISOU 600 OG SER A 589 2021 2179 1514 -20 7 349 A O ATOM 601 N SER A 590 31.044 -14.195 1.424 1.00 0.00 A N ATOM 602 CA SER A 590 31.913 -14.462 0.281 1.00 0.00 A C ATOM 603 C SER A 590 33.303 -14.842 0.736 1.00 0.00 A C ATOM 604 O SER A 590 34.141 -15.203 -0.142 1.00 0.00 A O ATOM 605 CB SER A 590 31.940 -13.252 -0.685 1.00 0.00 A C ATOM 606 OG SER A 590 32.566 -12.098 -0.115 1.00 0.00 A O ATOM 607 N GLU A 591 33.628 -14.804 2.026 1.00 14.12 A N ANISOU 607 N GLU A 591 1839 2013 1513 -47 318 278 A N ATOM 608 CA GLU A 591 34.919 -15.232 2.569 1.00 13.81 A C ANISOU 608 CA GLU A 591 1750 1954 1544 -47 373 248 A C ATOM 609 C GLU A 591 34.868 -16.683 2.987 1.00 15.21 A C ANISOU 609 C GLU A 591 1917 2133 1728 -34 360 181 A C ATOM 610 O GLU A 591 35.865 -17.233 3.441 1.00 15.01 A O ANISOU 610 O GLU A 591 1849 2092 1762 -28 397 153 A O ATOM 611 CB GLU A 591 35.321 -14.339 3.734 1.00 15.28 A C ANISOU 611 CB GLU A 591 1878 2099 1830 -53 357 269 A C ATOM 612 CG GLU A 591 35.489 -12.909 3.276 1.00 17.17 A C ANISOU 612 CG GLU A 591 2125 2323 2074 -68 378 336 A C ATOM 613 CD GLU A 591 35.823 -11.878 4.334 1.00 21.32 A C ANISOU 613 CD GLU A 591 2602 2802 2698 -79 359 353 A C ATOM 614 OE1 GLU A 591 36.252 -12.266 5.447 1.00 21.61 A O ANISOU 614 OE1 GLU A 591 2589 2820 2800 -76 340 313 A O ATOM 615 OE2 GLU A 591 35.676 -10.676 4.030 1.00 19.93 A O ANISOU 615 OE2 GLU A 591 2438 2604 2530 -89 363 408 A O ATOM 616 N ARG A 592 33.703 -17.334 2.789 1.00 14.93 A N ANISOU 616 N ARG A 592 1919 2117 1637 -30 307 157 A N ATOM 617 CA ARG A 592 33.543 -18.734 3.094 1.00 14.99 A C ANISOU 617 CA ARG A 592 1924 2120 1651 -21 294 95 A C ATOM 618 C ARG A 592 34.063 -19.533 1.920 1.00 25.06 A C ANISOU 618 C ARG A 592 3241 3417 2863 -20 354 59 A C ATOM 619 O ARG A 592 34.051 -19.051 0.791 1.00 29.19 A O ANISOU 619 O ARG A 592 3813 3971 3307 -28 382 81 A O ATOM 620 CB ARG A 592 32.054 -19.036 3.333 1.00 13.06 A C ANISOU 620 CB ARG A 592 1698 1884 1381 -23 214 86 A C ATOM 621 CG ARG A 592 31.527 -18.293 4.554 1.00 13.20 A C ANISOU 621 CG ARG A 592 1674 1879 1462 -21 165 115 A C ATOM 622 CD ARG A 592 30.051 -18.492 4.792 1.00 12.87 A C ANISOU 622 CD ARG A 592 1640 1844 1405 -22 96 112 A C ATOM 623 NE ARG A 592 29.580 -17.549 5.801 1.00 11.22 A N ANISOU 623 NE ARG A 592 1397 1616 1248 -17 65 144 A N ATOM 624 CZ ARG A 592 28.311 -17.156 5.947 1.00 11.58 A C ANISOU 624 CZ ARG A 592 1441 1668 1292 -15 13 161 A C ATOM 625 NH1 ARG A 592 27.351 -17.654 5.157 1.00 11.91 A N ANISOU 625 NH1 ARG A 592 1507 1735 1283 -21 -24 153 A N ATOM 626 NH2 ARG A 592 28.003 -16.206 6.820 1.00 10.70 A N ANISOU 626 NH2 ARG A 592 1301 1534 1228 -7 -2 187 A N ATOM 627 N HIS A 593 34.538 -20.726 2.179 1.00 22.60 A N ANISOU 627 N HIS A 593 2914 3087 2586 -8 377 4 A N ATOM 628 CA HIS A 593 34.988 -21.595 1.100 1.00 23.03 A C ANISOU 628 CA HIS A 593 3010 3156 2584 -3 438 -45 A C ATOM 629 C HIS A 593 33.923 -22.658 0.913 1.00 25.40 A C ANISOU 629 C HIS A 593 3351 3458 2841 -7 384 -98 A C ATOM 630 O HIS A 593 33.550 -23.369 1.852 1.00 23.04 A O ANISOU 630 O HIS A 593 3022 3128 2605 -2 341 -120 A O ATOM 631 CB HIS A 593 36.374 -22.182 1.376 1.00 24.56 A C ANISOU 631 CB HIS A 593 3156 3322 2855 16 513 -72 A C ATOM 632 N SER A 594 33.378 -22.727 -0.310 1.00 24.19 A N ANISOU 632 N SER A 594 3270 3343 2579 -20 382 -114 A N ATOM 633 CA SER A 594 32.309 -23.665 -0.673 1.00 24.13 A C ANISOU 633 CA SER A 594 3307 3341 2521 -32 323 -168 A C ATOM 634 C SER A 594 31.074 -23.499 0.240 1.00 24.15 A C ANISOU 634 C SER A 594 3278 3334 2566 -41 226 -144 A C ATOM 635 O SER A 594 30.391 -24.476 0.553 1.00 23.45 A O ANISOU 635 O SER A 594 3187 3224 2499 -48 183 -188 A O ATOM 636 CB SER A 594 32.825 -25.103 -0.692 1.00 30.35 A C ANISOU 636 CB SER A 594 4098 4095 3340 -20 365 -249 A C ATOM 637 OG SER A 594 34.010 -25.174 -1.468 1.00 42.72 A O ANISOU 637 OG SER A 594 5683 5669 4878 -7 467 -270 A O ATOM 638 N GLY A 595 30.832 -22.253 0.673 1.00 19.57 A N ANISOU 638 N GLY A 595 2670 2762 2004 -41 200 -74 A N ATOM 639 CA GLY A 595 29.688 -21.881 1.500 1.00 18.46 A C ANISOU 639 CA GLY A 595 2498 2615 1902 -47 120 -44 A C ATOM 640 C GLY A 595 29.865 -22.185 2.978 1.00 18.94 A C ANISOU 640 C GLY A 595 2496 2633 2066 -37 115 -46 A C ATOM 641 O GLY A 595 28.949 -21.933 3.755 1.00 17.18 A O ANISOU 641 O GLY A 595 2246 2403 1879 -40 61 -25 A O ATOM 642 N GLU A 596 31.026 -22.711 3.378 1.00 16.28 A N ANISOU 642 N GLU A 596 2137 2270 1780 -23 172 -67 A N ATOM 643 CA GLU A 596 31.238 -23.078 4.776 1.00 14.64 A C ANISOU 643 CA GLU A 596 1877 2024 1661 -12 161 -66 A C ATOM 644 C GLU A 596 32.015 -22.028 5.524 1.00 14.32 A C ANISOU 644 C GLU A 596 1795 1977 1669 -4 178 -21 A C ATOM 645 O GLU A 596 33.083 -21.563 5.065 1.00 14.77 A O ANISOU 645 O GLU A 596 1846 2038 1727 1 232 -10 A O ATOM 646 CB GLU A 596 32.042 -24.383 4.880 1.00 16.09 A C ANISOU 646 CB GLU A 596 2054 2176 1884 1 201 -115 A C ATOM 647 CG GLU A 596 31.267 -25.608 4.444 1.00 22.47 A C ANISOU 647 CG GLU A 596 2896 2972 2668 -10 178 -169 A C ATOM 648 CD GLU A 596 32.114 -26.850 4.291 1.00 32.90 A C ANISOU 648 CD GLU A 596 4220 4257 4023 6 227 -222 A C ATOM 649 OE1 GLU A 596 33.279 -26.729 3.850 1.00 31.21 A O ANISOU 649 OE1 GLU A 596 4002 4045 3813 23 293 -229 A O ATOM 650 OE2 GLU A 596 31.610 -27.945 4.622 1.00 40.64 A O ANISOU 650 OE2 GLU A 596 5204 5203 5036 2 203 -255 A O ATOM 651 N LEU A 597 31.455 -21.613 6.652 1.00 10.01 A N ANISOU 651 N LEU A 597 1221 1420 1164 -4 134 4 A N ATOM 652 CA LEU A 597 32.188 -20.811 7.607 1.00 9.67 A C ANISOU 652 CA LEU A 597 1136 1362 1175 3 141 33 A C ATOM 653 C LEU A 597 33.258 -21.738 8.237 1.00 11.76 A C ANISOU 653 C LEU A 597 1370 1600 1497 17 165 10 A C ATOM 654 O LEU A 597 32.940 -22.851 8.665 1.00 12.01 A O ANISOU 654 O LEU A 597 1402 1614 1545 23 148 -14 A O ATOM 655 CB LEU A 597 31.242 -20.341 8.716 1.00 9.45 A C ANISOU 655 CB LEU A 597 1093 1328 1170 1 90 52 A C ATOM 656 CG LEU A 597 31.895 -19.665 9.944 1.00 11.17 A C ANISOU 656 CG LEU A 597 1274 1527 1441 6 85 69 A C ATOM 657 CD1 LEU A 597 32.424 -18.288 9.575 1.00 11.13 A C ANISOU 657 CD1 LEU A 597 1264 1525 1440 0 104 99 A C ATOM 658 CD2 LEU A 597 30.905 -19.556 11.065 1.00 10.65 A C ANISOU 658 CD2 LEU A 597 1203 1457 1387 7 45 75 A C ATOM 659 N MET A 598 34.510 -21.287 8.245 1.00 11.12 A N ANISOU 659 N MET A 598 1259 1513 1452 23 202 21 A N ATOM 660 CA MET A 598 35.601 -22.035 8.848 1.00 11.88 A C ANISOU 660 CA MET A 598 1314 1585 1613 40 219 6 A C ATOM 661 C MET A 598 36.000 -21.335 10.145 1.00 14.51 A C ANISOU 661 C MET A 598 1606 1908 1999 40 183 32 A C ATOM 662 O MET A 598 36.263 -20.115 10.153 1.00 16.02 A O ANISOU 662 O MET A 598 1784 2105 2196 27 185 56 A O ATOM 663 CB MET A 598 36.809 -22.022 7.873 1.00 16.17 A C ANISOU 663 CB MET A 598 1844 2132 2168 46 291 -3 A C ATOM 664 CG MET A 598 38.033 -22.747 8.391 1.00 23.82 A C ANISOU 664 CG MET A 598 2759 3075 3218 69 312 -15 A C ATOM 665 SD MET A 598 39.633 -21.870 8.146 1.00 34.28 A S ANISOU 665 SD MET A 598 4019 4399 4606 67 370 6 A S ATOM 666 CE MET A 598 39.550 -20.786 9.669 1.00 28.10 A C ANISOU 666 CE MET A 598 3201 3610 3865 51 288 42 A C ATOM 667 N LEU A 599 35.993 -22.074 11.252 1.00 11.24 A N ANISOU 667 N LEU A 599 1176 1476 1619 52 147 29 A N ATOM 668 CA LEU A 599 36.487 -21.543 12.516 1.00 10.35 A C ANISOU 668 CA LEU A 599 1028 1356 1548 52 108 47 A C ATOM 669 C LEU A 599 37.627 -22.410 12.961 1.00 11.40 A C ANISOU 669 C LEU A 599 1119 1469 1744 74 110 43 A C ATOM 670 O LEU A 599 37.523 -23.656 12.927 1.00 13.66 A O ANISOU 670 O LEU A 599 1414 1738 2039 92 114 29 A O ATOM 671 CB LEU A 599 35.433 -21.584 13.642 1.00 10.55 A C ANISOU 671 CB LEU A 599 1076 1382 1551 49 56 56 A C ATOM 672 CG LEU A 599 34.139 -20.832 13.321 1.00 11.70 A C ANISOU 672 CG LEU A 599 1256 1544 1644 34 50 60 A C ATOM 673 CD1 LEU A 599 33.141 -20.971 14.481 1.00 12.81 A C ANISOU 673 CD1 LEU A 599 1411 1684 1770 33 12 66 A C ATOM 674 CD2 LEU A 599 34.417 -19.330 13.110 1.00 13.61 A C ANISOU 674 CD2 LEU A 599 1490 1792 1890 21 56 75 A C ATOM 675 N LEU A 600 38.727 -21.784 13.405 1.00 9.43 A N ANISOU 675 N LEU A 600 820 1216 1547 73 101 55 A N ATOM 676 CA LEU A 600 39.821 -22.525 14.039 1.00 9.72 A C ANISOU 676 CA LEU A 600 805 1234 1654 95 85 58 A C ATOM 677 C LEU A 600 39.680 -22.150 15.506 1.00 11.37 A C ANISOU 677 C LEU A 600 1011 1446 1861 89 10 75 A C ATOM 678 O LEU A 600 39.726 -20.962 15.811 1.00 10.61 A O ANISOU 678 O LEU A 600 911 1362 1760 67 -9 79 A O ATOM 679 CB LEU A 600 41.199 -22.149 13.472 1.00 10.77 A C ANISOU 679 CB LEU A 600 874 1364 1855 97 127 57 A C ATOM 680 CG LEU A 600 42.323 -22.945 14.109 1.00 12.18 A C ANISOU 680 CG LEU A 600 989 1522 2117 125 104 63 A C ATOM 681 CD1 LEU A 600 42.214 -24.429 13.795 1.00 12.42 A C ANISOU 681 CD1 LEU A 600 1033 1528 2158 159 130 48 A C ATOM 682 CD2 LEU A 600 43.665 -22.423 13.659 1.00 13.55 A C ANISOU 682 CD2 LEU A 600 1087 1693 2369 122 143 65 A C ATOM 683 N VAL A 601 39.410 -23.144 16.381 1.00 9.99 A N ANISOU 683 N VAL A 601 850 1261 1684 108 -29 84 A N ATOM 684 CA VAL A 601 39.162 -22.839 17.792 1.00 9.76 A C ANISOU 684 CA VAL A 601 834 1241 1632 102 -97 101 A C ATOM 685 C VAL A 601 40.062 -23.619 18.721 1.00 11.40 A C ANISOU 685 C VAL A 601 1007 1436 1888 127 -147 122 A C ATOM 686 O VAL A 601 40.628 -24.661 18.353 1.00 11.40 A O ANISOU 686 O VAL A 601 979 1412 1940 154 -128 126 A O ATOM 687 CB VAL A 601 37.665 -23.123 18.153 1.00 11.20 A C ANISOU 687 CB VAL A 601 1081 1430 1744 96 -102 104 A C ATOM 688 CG1 VAL A 601 36.713 -22.374 17.227 1.00 11.00 A C ANISOU 688 CG1 VAL A 601 1085 1417 1677 76 -63 88 A C ATOM 689 CG2 VAL A 601 37.356 -24.623 18.129 1.00 10.98 A C ANISOU 689 CG2 VAL A 601 1069 1379 1725 117 -94 113 A C ATOM 690 N ARG A 602 40.217 -23.095 19.959 1.00 10.84 A N ANISOU 690 N ARG A 602 938 1380 1800 118 -214 134 A N ATOM 691 CA ARG A 602 40.937 -23.789 21.000 1.00 11.15 A C ANISOU 691 CA ARG A 602 955 1413 1867 140 -278 161 A C ATOM 692 C ARG A 602 39.906 -24.210 22.049 1.00 14.34 A C ANISOU 692 C ARG A 602 1427 1826 2194 140 -311 183 A C ATOM 693 O ARG A 602 39.321 -23.333 22.728 1.00 13.35 A O ANISOU 693 O ARG A 602 1341 1726 2006 117 -333 173 A O ATOM 694 CB ARG A 602 42.008 -22.872 21.602 1.00 13.46 A C ANISOU 694 CB ARG A 602 1199 1720 2197 127 -337 158 A C ATOM 695 CG ARG A 602 42.900 -23.611 22.602 1.00 22.78 A C ANISOU 695 CG ARG A 602 2344 2896 3414 152 -415 191 A C ATOM 696 CD ARG A 602 43.952 -22.680 23.178 1.00 32.84 A C ANISOU 696 CD ARG A 602 3565 4186 4728 134 -482 182 A C ATOM 697 NE ARG A 602 45.042 -22.450 22.229 1.00 42.06 A N ANISOU 697 NE ARG A 602 4643 5337 5999 134 -446 171 A N ATOM 698 CZ ARG A 602 45.233 -21.326 21.545 1.00 49.96 A C ANISOU 698 CZ ARG A 602 5620 6340 7023 101 -407 142 A C ATOM 699 NH1 ARG A 602 44.410 -20.294 21.703 1.00 42.02 A N ANISOU 699 NH1 ARG A 602 4671 5348 5946 67 -404 120 A N ATOM 700 NH2 ARG A 602 46.249 -21.224 20.698 1.00 27.36 A N ANISOU 700 NH2 ARG A 602 2675 3464 4258 103 -365 139 A N ATOM 701 N PRO A 603 39.674 -25.522 22.230 1.00 13.78 A N ANISOU 701 N PRO A 603 1373 1733 2131 166 -309 211 A N ATOM 702 CA PRO A 603 38.748 -25.953 23.306 1.00 14.78 A C ANISOU 702 CA PRO A 603 1563 1868 2187 164 -335 241 A C ATOM 703 C PRO A 603 39.234 -25.464 24.687 1.00 18.70 A C ANISOU 703 C PRO A 603 2068 2392 2645 161 -417 260 A C ATOM 704 O PRO A 603 40.436 -25.290 24.894 1.00 19.79 A O ANISOU 704 O PRO A 603 2153 2532 2835 171 -467 264 A O ATOM 705 CB PRO A 603 38.839 -27.485 23.241 1.00 17.96 A C ANISOU 705 CB PRO A 603 1963 2230 2633 195 -328 275 A C ATOM 706 CG PRO A 603 39.217 -27.777 21.815 1.00 21.38 A C ANISOU 706 CG PRO A 603 2355 2636 3134 205 -268 242 A C ATOM 707 CD PRO A 603 40.228 -26.681 21.504 1.00 15.93 A C ANISOU 707 CD PRO A 603 1609 1967 2478 197 -278 218 A C ATOM 708 N ASN A 604 38.285 -25.228 25.634 1.00 20.16 A N ANISOU 708 N ASN A 604 2319 2601 2740 146 -429 269 A N ATOM 709 CA ASN A 604 38.602 -24.751 26.993 1.00 34.42 A C ANISOU 709 CA ASN A 604 4152 4440 4487 141 -503 280 A C ATOM 710 C ASN A 604 39.311 -25.807 27.824 1.00 58.61 A C ANISOU 710 C ASN A 604 7212 7495 7562 170 -569 338 A C ATOM 711 O ASN A 604 39.149 -26.989 27.546 1.00 37.43 A O ANISOU 711 O ASN A 604 4528 4779 4914 193 -544 375 A O ATOM 712 CB ASN A 604 37.347 -24.226 27.722 1.00 35.76 A C ANISOU 712 CB ASN A 604 4397 4637 4553 119 -482 270 A C ATOM 713 CG ASN A 604 36.227 -25.216 27.992 1.00 57.59 A C ANISOU 713 CG ASN A 604 7213 7392 7276 126 -439 309 A C ATOM 714 ND2 ASN A 604 35.181 -24.742 28.657 1.00 43.75 A N ANISOU 714 ND2 ASN A 604 5519 5666 5440 109 -414 301 A N ATOM 715 OD1 ASN A 604 36.245 -26.381 27.573 1.00 57.34 A O ANISOU 715 OD1 ASN A 604 7167 7327 7293 144 -421 343 A O TER HETATM 716 C1 GOL A 1 15.466 -25.894 15.333 1.00 37.25 E C HETATM 717 O1 GOL A 1 16.758 -25.259 15.128 1.00 38.59 E O HETATM 718 C2 GOL A 1 15.509 -26.958 16.437 1.00 36.37 E C HETATM 719 O2 GOL A 1 16.653 -26.735 17.210 1.00 37.74 E O HETATM 720 C3 GOL A 1 14.443 -26.614 17.426 1.00 35.33 E C HETATM 721 O3 GOL A 1 14.293 -27.667 18.332 1.00 30.41 E O HETATM 722 C1 GOL A 605 25.638 -26.999 25.963 1.00 27.91 F C HETATM 723 O1 GOL A 605 25.279 -26.222 24.826 1.00 22.00 F O HETATM 724 C2 GOL A 605 24.487 -27.773 26.552 1.00 28.81 F C HETATM 725 O2 GOL A 605 23.815 -28.524 25.560 1.00 29.42 F O HETATM 726 C3 GOL A 605 24.941 -28.817 27.551 1.00 28.51 F C HETATM 727 O3 GOL A 605 25.982 -28.304 28.344 1.00 28.03 F O CONECT 716 717 718 CONECT 717 716 CONECT 718 716 719 720 CONECT 719 718 CONECT 720 718 721 CONECT 721 720 CONECT 722 723 724 CONECT 723 722 CONECT 724 722 725 726 CONECT 725 724 CONECT 726 724 727 CONECT 727 726 END If you find results from this site helpful for your research, please cite one of our papers:
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