HEADER 1.10.8.60 1lv7A02 ATOM 1383 N PRO A 325 13.602 25.628 67.246 1.00 16.43 N ANISOU 1383 N PRO A 325 2117 2064 2060 -13 -2 2 N ATOM 1384 CA PRO A 325 13.846 25.222 68.631 1.00 15.93 C ANISOU 1384 CA PRO A 325 2109 1950 1994 92 -50 -2 C ATOM 1385 C PRO A 325 12.735 25.734 69.539 1.00 17.29 C ANISOU 1385 C PRO A 325 2274 2113 2181 63 35 31 C ATOM 1386 O PRO A 325 12.180 26.811 69.276 1.00 18.48 O ANISOU 1386 O PRO A 325 2689 2157 2176 256 -78 144 O ATOM 1387 CB PRO A 325 15.163 25.914 68.974 1.00 16.34 C ANISOU 1387 CB PRO A 325 2098 1994 2114 105 -2 0 C ATOM 1388 CG PRO A 325 15.208 27.091 68.090 1.00 17.29 C ANISOU 1388 CG PRO A 325 2244 2192 2131 -82 -44 -26 C ATOM 1389 CD PRO A 325 14.531 26.687 66.794 1.00 16.83 C ANISOU 1389 CD PRO A 325 2277 2056 2060 13 -69 30 C ATOM 1390 N ASP A 326 12.394 24.990 70.581 1.00 17.27 N ANISOU 1390 N ASP A 326 2438 1992 2133 67 -35 31 N ATOM 1391 CA ASP A 326 11.544 25.517 71.626 1.00 16.89 C ANISOU 1391 CA ASP A 326 2179 2047 2189 9 -5 68 C ATOM 1392 C ASP A 326 12.394 26.354 72.605 1.00 16.20 C ANISOU 1392 C ASP A 326 2123 2003 2030 0 21 34 C ATOM 1393 O ASP A 326 13.589 26.578 72.379 1.00 15.26 O ANISOU 1393 O ASP A 326 2100 1788 1909 101 -81 -8 O ATOM 1394 CB ASP A 326 10.751 24.433 72.360 1.00 17.24 C ANISOU 1394 CB ASP A 326 2168 2117 2264 -42 -19 78 C ATOM 1395 CG ASP A 326 11.615 23.402 73.006 1.00 19.29 C ANISOU 1395 CG ASP A 326 2452 2266 2611 -20 -106 95 C ATOM 1396 OD1 ASP A 326 12.762 23.703 73.420 1.00 17.23 O ANISOU 1396 OD1 ASP A 326 2303 1800 2442 -8 -133 179 O ATOM 1397 OD2 ASP A 326 11.184 22.233 73.151 1.00 23.33 O ANISOU 1397 OD2 ASP A 326 3166 2411 3286 -184 -137 199 O ATOM 1398 N VAL A 327 11.780 26.855 73.677 1.00 16.17 N ANISOU 1398 N VAL A 327 2153 1968 2023 25 18 94 N ATOM 1399 CA VAL A 327 12.487 27.757 74.579 1.00 16.32 C ANISOU 1399 CA VAL A 327 2176 1986 2037 68 33 87 C ATOM 1400 C VAL A 327 13.720 27.130 75.231 1.00 16.36 C ANISOU 1400 C VAL A 327 2114 1999 2100 42 36 78 C ATOM 1401 O VAL A 327 14.741 27.775 75.388 1.00 14.87 O ANISOU 1401 O VAL A 327 1820 1653 2175 336 -116 88 O ATOM 1402 CB VAL A 327 11.525 28.319 75.620 1.00 16.56 C ANISOU 1402 CB VAL A 327 2148 2037 2105 23 101 66 C ATOM 1403 CG1 VAL A 327 11.119 27.269 76.665 1.00 18.37 C ANISOU 1403 CG1 VAL A 327 2505 2177 2297 4 16 127 C ATOM 1404 CG2 VAL A 327 12.130 29.557 76.270 1.00 15.79 C ANISOU 1404 CG2 VAL A 327 2032 1985 1980 97 28 -9 C ATOM 1405 N ARG A 328 13.636 25.839 75.516 1.00 16.28 N ANISOU 1405 N ARG A 328 2212 1948 2025 112 -59 18 N ATOM 1406 CA ARG A 328 14.807 25.125 76.044 1.00 16.35 C ANISOU 1406 CA ARG A 328 2029 1997 2184 73 21 16 C ATOM 1407 C ARG A 328 15.905 25.004 74.986 1.00 15.50 C ANISOU 1407 C ARG A 328 2004 1808 2077 21 -44 -4 C ATOM 1408 O ARG A 328 17.063 25.216 75.284 1.00 16.67 O ANISOU 1408 O ARG A 328 2017 1911 2404 209 -182 0 O ATOM 1409 CB ARG A 328 14.385 23.719 76.475 1.00 17.52 C ANISOU 1409 CB ARG A 328 2270 2077 2307 43 55 49 C ATOM 1410 CG AARG A 328 15.211 23.168 77.647 0.25 18.58 C ANISOU 1410 CG AARG A 328 2276 2383 2400 25 -24 -2 C ATOM 1411 CG BARG A 328 14.221 23.395 77.966 0.25 18.98 C ANISOU 1411 CG BARG A 328 2445 2392 2372 24 2 -1 C ATOM 1412 CD AARG A 328 14.533 22.199 78.624 0.25 19.98 C ANISOU 1412 CD AARG A 328 2531 2515 2542 -17 -10 58 C ATOM 1413 CD BARG A 328 13.324 22.141 78.182 0.25 19.77 C ANISOU 1413 CD BARG A 328 2529 2454 2528 -7 -9 26 C ATOM 1414 NE AARG A 328 14.115 20.838 78.219 0.25 21.52 N ANISOU 1414 NE AARG A 328 2747 2652 2775 -12 4 -8 N ATOM 1415 NE BARG A 328 12.374 22.207 79.296 0.25 21.38 N ANISOU 1415 NE BARG A 328 2722 2696 2703 35 42 -13 N ATOM 1416 CZ AARG A 328 14.364 20.166 77.085 0.25 22.00 C ANISOU 1416 CZ AARG A 328 2818 2765 2776 35 7 0 C ATOM 1417 CZ BARG A 328 11.685 21.161 79.765 0.25 21.63 C ANISOU 1417 CZ BARG A 328 2722 2737 2759 2 8 -6 C ATOM 1418 NH1AARG A 328 15.084 20.645 76.087 0.25 22.62 N ANISOU 1418 NH1AARG A 328 2809 2858 2927 3 42 8 N ATOM 1419 NH1BARG A 328 10.845 21.318 80.785 0.25 21.39 N ANISOU 1419 NH1BARG A 328 2733 2688 2703 -26 28 17 N ATOM 1420 NH2AARG A 328 13.864 18.942 76.960 0.25 22.59 N ANISOU 1420 NH2AARG A 328 2843 2858 2882 -13 -22 -13 N ATOM 1421 NH2BARG A 328 11.828 19.949 79.228 0.25 22.35 N ANISOU 1421 NH2BARG A 328 2838 2817 2837 25 -15 -50 N ATOM 1422 N GLY A 329 15.512 24.704 73.741 1.00 15.60 N ANISOU 1422 N GLY A 329 2062 1794 2069 7 10 16 N ATOM 1423 CA GLY A 329 16.396 24.657 72.609 1.00 15.15 C ANISOU 1423 CA GLY A 329 1976 1762 2017 96 -24 -30 C ATOM 1424 C GLY A 329 17.053 25.985 72.330 1.00 14.95 C ANISOU 1424 C GLY A 329 1987 1799 1892 40 63 -60 C ATOM 1425 O GLY A 329 18.236 26.060 72.000 1.00 16.07 O ANISOU 1425 O GLY A 329 2129 1825 2149 225 65 49 O ATOM 1426 N ARG A 330 16.296 27.062 72.477 1.00 14.75 N ANISOU 1426 N ARG A 330 1992 1828 1784 95 -36 8 N ATOM 1427 CA ARG A 330 16.906 28.360 72.214 1.00 14.70 C ANISOU 1427 CA ARG A 330 1944 1776 1864 87 -42 -19 C ATOM 1428 C ARG A 330 17.995 28.692 73.234 1.00 14.75 C ANISOU 1428 C ARG A 330 1895 1804 1903 147 3 -92 C ATOM 1429 O ARG A 330 19.028 29.197 72.883 1.00 15.15 O ANISOU 1429 O ARG A 330 2086 1785 1882 41 -24 -107 O ATOM 1430 CB ARG A 330 15.865 29.485 72.263 1.00 14.18 C ANISOU 1430 CB ARG A 330 1769 1825 1792 211 32 -76 C ATOM 1431 CG ARG A 330 14.833 29.401 71.144 1.00 13.77 C ANISOU 1431 CG ARG A 330 1627 1677 1927 68 26 2 C ATOM 1432 CD ARG A 330 14.061 30.695 71.013 1.00 14.68 C ANISOU 1432 CD ARG A 330 2043 1636 1898 27 83 70 C ATOM 1433 NE ARG A 330 13.091 30.936 72.070 1.00 13.11 N ANISOU 1433 NE ARG A 330 2083 1248 1651 52 -68 -145 N ATOM 1434 CZ ARG A 330 11.874 30.430 72.108 1.00 14.37 C ANISOU 1434 CZ ARG A 330 2134 1694 1631 5 0 149 C ATOM 1435 NH1 ARG A 330 11.495 29.524 71.211 1.00 15.50 N ANISOU 1435 NH1 ARG A 330 2398 1684 1806 59 -54 128 N ATOM 1436 NH2 ARG A 330 11.031 30.792 73.053 1.00 13.83 N ANISOU 1436 NH2 ARG A 330 2052 1615 1585 -214 66 186 N ATOM 1437 N GLU A 331 17.735 28.400 74.500 1.00 15.61 N ANISOU 1437 N GLU A 331 2009 1901 2019 95 -25 5 N ATOM 1438 CA GLU A 331 18.725 28.639 75.538 1.00 15.08 C ANISOU 1438 CA GLU A 331 1972 1829 1926 67 -55 -37 C ATOM 1439 C GLU A 331 19.971 27.810 75.259 1.00 15.51 C ANISOU 1439 C GLU A 331 1936 1917 2039 5 -54 0 C ATOM 1440 O GLU A 331 21.083 28.318 75.358 1.00 16.11 O ANISOU 1440 O GLU A 331 1979 2067 2072 75 -169 -33 O ATOM 1441 CB GLU A 331 18.159 28.330 76.907 1.00 14.75 C ANISOU 1441 CB GLU A 331 1833 1732 2039 52 16 41 C ATOM 1442 CG GLU A 331 19.141 28.526 78.046 1.00 15.80 C ANISOU 1442 CG GLU A 331 2179 1826 1997 174 -92 -51 C ATOM 1443 CD GLU A 331 18.583 28.218 79.428 1.00 15.95 C ANISOU 1443 CD GLU A 331 2238 1653 2170 183 -3 6 C ATOM 1444 OE1 GLU A 331 19.379 28.355 80.413 1.00 19.22 O ANISOU 1444 OE1 GLU A 331 2545 2251 2505 395 -134 61 O ATOM 1445 OE2 GLU A 331 17.376 27.891 79.562 1.00 17.10 O ANISOU 1445 OE2 GLU A 331 2455 1875 2167 288 4 145 O ATOM 1446 N GLN A 332 19.770 26.532 74.890 1.00 15.61 N ANISOU 1446 N GLN A 332 2038 1879 2014 105 -99 -87 N ATOM 1447 CA GLN A 332 20.863 25.618 74.535 1.00 16.97 C ANISOU 1447 CA GLN A 332 2144 2021 2282 73 -38 21 C ATOM 1448 C GLN A 332 21.717 26.168 73.395 1.00 16.59 C ANISOU 1448 C GLN A 332 2192 1984 2125 138 4 -116 C ATOM 1449 O GLN A 332 22.959 26.214 73.467 1.00 17.44 O ANISOU 1449 O GLN A 332 2334 1778 2513 160 57 -33 O ATOM 1450 CB GLN A 332 20.246 24.254 74.194 1.00 16.69 C ANISOU 1450 CB GLN A 332 2086 2013 2242 124 -108 -7 C ATOM 1451 CG GLN A 332 21.209 23.155 73.701 1.00 18.64 C ANISOU 1451 CG GLN A 332 2364 2246 2471 122 -28 -61 C ATOM 1452 CD GLN A 332 20.459 21.901 73.315 1.00 19.64 C ANISOU 1452 CD GLN A 332 2511 2360 2590 41 -56 22 C ATOM 1453 OE1 GLN A 332 19.305 21.981 72.882 1.00 18.22 O ANISOU 1453 OE1 GLN A 332 2412 1961 2547 245 22 -334 O ATOM 1454 NE2 GLN A 332 21.097 20.744 73.477 1.00 21.23 N ANISOU 1454 NE2 GLN A 332 2904 2366 2794 188 87 -14 N ATOM 1455 N ILE A 333 21.059 26.590 72.329 1.00 16.95 N ANISOU 1455 N ILE A 333 2064 2061 2312 154 36 -95 N ATOM 1456 CA ILE A 333 21.732 27.117 71.152 1.00 17.61 C ANISOU 1456 CA ILE A 333 2279 2241 2171 104 42 -78 C ATOM 1457 C ILE A 333 22.447 28.408 71.446 1.00 17.68 C ANISOU 1457 C ILE A 333 2244 2254 2217 59 98 -66 C ATOM 1458 O ILE A 333 23.591 28.626 71.047 1.00 17.59 O ANISOU 1458 O ILE A 333 2300 2239 2142 73 185 -52 O ATOM 1459 CB ILE A 333 20.707 27.278 69.977 1.00 17.80 C ANISOU 1459 CB ILE A 333 2246 2259 2256 118 30 -83 C ATOM 1460 CG1 ILE A 333 20.244 25.891 69.518 1.00 17.11 C ANISOU 1460 CG1 ILE A 333 2143 2185 2171 84 39 -32 C ATOM 1461 CG2 ILE A 333 21.327 28.072 68.856 1.00 16.54 C ANISOU 1461 CG2 ILE A 333 1953 2107 2225 84 -4 -82 C ATOM 1462 CD1 ILE A 333 19.040 25.888 68.600 1.00 19.07 C ANISOU 1462 CD1 ILE A 333 2293 2528 2424 73 6 -150 C ATOM 1463 N LEU A 334 21.786 29.304 72.181 1.00 17.60 N ANISOU 1463 N LEU A 334 2201 2253 2232 114 45 -59 N ATOM 1464 CA LEU A 334 22.445 30.553 72.565 1.00 16.92 C ANISOU 1464 CA LEU A 334 2153 2156 2119 53 42 -46 C ATOM 1465 C LEU A 334 23.704 30.332 73.350 1.00 16.70 C ANISOU 1465 C LEU A 334 2099 2102 2142 68 123 -59 C ATOM 1466 O LEU A 334 24.715 30.997 73.123 1.00 17.51 O ANISOU 1466 O LEU A 334 2042 2277 2331 3 68 97 O ATOM 1467 CB LEU A 334 21.473 31.447 73.368 1.00 15.54 C ANISOU 1467 CB LEU A 334 1959 1879 2065 38 -74 -119 C ATOM 1468 CG LEU A 334 20.337 32.090 72.570 1.00 16.25 C ANISOU 1468 CG LEU A 334 2026 1969 2176 -1 -54 23 C ATOM 1469 CD1 LEU A 334 19.230 32.571 73.504 1.00 16.38 C ANISOU 1469 CD1 LEU A 334 2283 1788 2150 108 11 -20 C ATOM 1470 CD2 LEU A 334 20.900 33.316 71.815 1.00 16.48 C ANISOU 1470 CD2 LEU A 334 2216 1816 2228 59 7 110 C ATOM 1471 N LYS A 335 23.668 29.413 74.310 1.00 16.66 N ANISOU 1471 N LYS A 335 2054 2142 2133 -2 120 48 N ATOM 1472 CA LYS A 335 24.851 29.070 75.059 1.00 17.34 C ANISOU 1472 CA LYS A 335 2135 2218 2233 -35 4 22 C ATOM 1473 C LYS A 335 25.988 28.604 74.157 1.00 17.76 C ANISOU 1473 C LYS A 335 2258 2139 2349 114 -9 -19 C ATOM 1474 O LYS A 335 27.125 29.014 74.380 1.00 18.24 O ANISOU 1474 O LYS A 335 2289 2104 2537 147 20 -82 O ATOM 1475 CB LYS A 335 24.568 28.053 76.175 1.00 17.87 C ANISOU 1475 CB LYS A 335 2189 2326 2272 91 -70 97 C ATOM 1476 CG LYS A 335 23.769 28.635 77.342 1.00 19.69 C ANISOU 1476 CG LYS A 335 2499 2535 2445 45 -23 11 C ATOM 1477 CD LYS A 335 23.556 27.546 78.406 1.00 23.50 C ANISOU 1477 CD LYS A 335 3190 2876 2862 -36 -31 55 C ATOM 1478 CE LYS A 335 22.604 27.964 79.496 1.00 26.87 C ANISOU 1478 CE LYS A 335 3342 3502 3364 41 79 22 C ATOM 1479 NZ LYS A 335 22.243 26.802 80.373 1.00 30.24 N ANISOU 1479 NZ LYS A 335 4145 3665 3680 95 -61 136 N ATOM 1480 N VAL A 336 25.702 27.807 73.133 1.00 18.21 N ANISOU 1480 N VAL A 336 2239 2342 2338 66 31 27 N ATOM 1481 CA VAL A 336 26.746 27.397 72.183 1.00 18.44 C ANISOU 1481 CA VAL A 336 2266 2291 2446 139 47 -26 C ATOM 1482 C VAL A 336 27.395 28.617 71.504 1.00 18.90 C ANISOU 1482 C VAL A 336 2401 2428 2351 75 42 -13 C ATOM 1483 O VAL A 336 28.614 28.757 71.509 1.00 19.85 O ANISOU 1483 O VAL A 336 2479 2370 2690 217 75 67 O ATOM 1484 CB VAL A 336 26.198 26.396 71.149 1.00 19.21 C ANISOU 1484 CB VAL A 336 2425 2436 2435 150 80 -17 C ATOM 1485 CG1 VAL A 336 27.252 26.089 70.115 1.00 20.44 C ANISOU 1485 CG1 VAL A 336 2466 2644 2654 127 34 -91 C ATOM 1486 CG2 VAL A 336 25.775 25.116 71.858 1.00 19.41 C ANISOU 1486 CG2 VAL A 336 2341 2416 2618 165 0 -61 C ATOM 1487 N HIS A 337 26.564 29.512 70.950 1.00 19.13 N ANISOU 1487 N HIS A 337 2396 2321 2551 123 175 48 N ATOM 1488 CA HIS A 337 27.054 30.671 70.193 1.00 19.67 C ANISOU 1488 CA HIS A 337 2504 2445 2521 64 116 36 C ATOM 1489 C HIS A 337 27.649 31.740 71.084 1.00 19.05 C ANISOU 1489 C HIS A 337 2440 2338 2460 43 137 53 C ATOM 1490 O HIS A 337 28.463 32.541 70.618 1.00 20.21 O ANISOU 1490 O HIS A 337 2519 2596 2562 -120 254 122 O ATOM 1491 CB HIS A 337 25.961 31.243 69.276 1.00 19.61 C ANISOU 1491 CB HIS A 337 2458 2489 2504 -48 33 80 C ATOM 1492 CG HIS A 337 25.498 30.281 68.225 1.00 20.91 C ANISOU 1492 CG HIS A 337 2763 2669 2510 218 -36 48 C ATOM 1493 ND1 HIS A 337 26.367 29.722 67.315 1.00 25.32 N ANISOU 1493 ND1 HIS A 337 3063 3730 2825 -73 190 -140 N ATOM 1494 CD2 HIS A 337 24.278 29.754 67.960 1.00 22.98 C ANISOU 1494 CD2 HIS A 337 3231 2965 2535 -178 187 71 C ATOM 1495 CE1 HIS A 337 25.705 28.869 66.554 1.00 25.06 C ANISOU 1495 CE1 HIS A 337 3415 3324 2782 -9 35 -231 C ATOM 1496 NE2 HIS A 337 24.433 28.864 66.922 1.00 22.82 N ANISOU 1496 NE2 HIS A 337 3325 2765 2580 32 -31 124 N ATOM 1497 N MET A 338 27.347 31.732 72.387 1.00 18.04 N ANISOU 1497 N MET A 338 2401 2189 2263 75 92 75 N ATOM 1498 CA MET A 338 27.950 32.690 73.302 1.00 19.49 C ANISOU 1498 CA MET A 338 2503 2420 2481 11 54 4 C ATOM 1499 C MET A 338 29.242 32.241 73.946 1.00 21.15 C ANISOU 1499 C MET A 338 2705 2619 2711 18 13 -31 C ATOM 1500 O MET A 338 29.899 33.044 74.586 1.00 20.85 O ANISOU 1500 O MET A 338 2734 2459 2726 65 -37 -54 O ATOM 1501 CB MET A 338 26.929 33.042 74.409 1.00 19.31 C ANISOU 1501 CB MET A 338 2526 2457 2354 28 38 -84 C ATOM 1502 CG AMET A 338 25.734 33.850 73.849 0.50 21.24 C ANISOU 1502 CG AMET A 338 2794 2589 2685 119 33 20 C ATOM 1503 CG BMET A 338 25.867 34.004 73.925 0.50 20.94 C ANISOU 1503 CG BMET A 338 2707 2570 2677 101 27 39 C ATOM 1504 SD AMET A 338 24.148 33.801 74.788 0.50 23.54 S ANISOU 1504 SD AMET A 338 3026 2986 2933 -132 111 -203 S ATOM 1505 SD BMET A 338 25.033 34.954 75.248 0.50 21.54 S ANISOU 1505 SD BMET A 338 2826 2429 2927 60 -35 -85 S ATOM 1506 CE AMET A 338 24.781 33.457 76.364 0.50 23.17 C ANISOU 1506 CE AMET A 338 2883 2834 3083 4 9 19 C ATOM 1507 CE BMET A 338 23.889 33.663 75.747 0.50 23.12 C ANISOU 1507 CE BMET A 338 2961 2974 2850 -117 37 7 C ATOM 1508 N ARG A 339 29.620 30.966 73.781 1.00 22.07 N ANISOU 1508 N ARG A 339 2821 2655 2909 39 -50 -24 N ATOM 1509 CA ARG A 339 30.762 30.432 74.508 1.00 24.65 C ANISOU 1509 CA ARG A 339 3127 3057 3179 43 -44 -9 C ATOM 1510 C ARG A 339 32.035 31.240 74.343 1.00 24.53 C ANISOU 1510 C ARG A 339 3078 3029 3211 95 12 -37 C ATOM 1511 O ARG A 339 32.777 31.454 75.325 1.00 27.56 O ANISOU 1511 O ARG A 339 3360 3448 3660 50 -92 -96 O ATOM 1512 CB ARG A 339 31.004 28.970 74.158 1.00 24.59 C ANISOU 1512 CB ARG A 339 3081 3007 3254 153 15 -55 C ATOM 1513 CG ARG A 339 31.848 28.514 75.461 0.00 20.00 C ANISOU 1513 CG ARG A 339 2533 2533 2533 0 0 0 C ATOM 1514 CD ARG A 339 31.119 27.798 76.582 0.00 20.00 C ANISOU 1514 CD ARG A 339 2533 2533 2533 0 0 0 C ATOM 1515 NE ARG A 339 31.947 26.673 76.984 0.00 20.00 N ANISOU 1515 NE ARG A 339 2533 2533 2533 0 0 0 N ATOM 1516 CZ ARG A 339 31.437 25.789 77.837 0.00 20.00 C ANISOU 1516 CZ ARG A 339 2533 2533 2533 0 0 0 C ATOM 1517 NH1 ARG A 339 30.289 26.036 78.438 0.00 20.00 N ANISOU 1517 NH1 ARG A 339 2533 2533 2533 0 0 0 N ATOM 1518 NH2 ARG A 339 31.913 24.546 77.802 0.00 20.00 N ANISOU 1518 NH2 ARG A 339 2533 2533 2533 0 0 0 N ATOM 1519 N ARG A 340 32.298 31.719 73.149 1.00 24.46 N ANISOU 1519 N ARG A 340 3024 2944 3325 75 126 -88 N ATOM 1520 CA ARG A 340 33.558 32.441 72.916 1.00 24.59 C ANISOU 1520 CA ARG A 340 3008 3054 3279 20 53 -15 C ATOM 1521 C ARG A 340 33.370 33.963 72.889 1.00 24.84 C ANISOU 1521 C ARG A 340 3018 3077 3340 0 116 -12 C ATOM 1522 O ARG A 340 34.262 34.701 72.496 1.00 26.60 O ANISOU 1522 O ARG A 340 3149 3316 3640 -42 195 31 O ATOM 1523 CB ARG A 340 34.182 31.958 71.594 0.50 24.01 C ANISOU 1523 CB ARG A 340 2908 3019 3196 -4 91 -18 C ATOM 1524 CG ARG A 340 34.842 30.569 71.691 0.50 25.09 C ANISOU 1524 CG ARG A 340 3130 3109 3293 -7 -5 35 C ATOM 1525 CD ARG A 340 35.536 30.101 70.408 0.50 25.48 C ANISOU 1525 CD ARG A 340 3212 3163 3304 22 -11 47 C ATOM 1526 NE ARG A 340 36.935 29.743 70.642 0.25 26.76 N ANISOU 1526 NE ARG A 340 3315 3370 3482 21 -4 11 N ATOM 1527 CZ ARG A 340 37.904 30.591 70.978 0.25 27.06 C ANISOU 1527 CZ ARG A 340 3428 3386 3466 1 8 8 C ATOM 1528 NH1 ARG A 340 37.662 31.891 71.135 0.25 27.34 N ANISOU 1528 NH1 ARG A 340 3477 3376 3535 39 19 28 N ATOM 1529 NH2 ARG A 340 39.132 30.130 71.174 0.25 26.83 N ANISOU 1529 NH2 ARG A 340 3355 3389 3446 -9 25 21 N ATOM 1530 N VAL A 341 32.203 34.436 73.295 1.00 23.80 N ANISOU 1530 N VAL A 341 2928 2857 3257 93 125 -38 N ATOM 1531 CA VAL A 341 31.921 35.872 73.314 1.00 22.75 C ANISOU 1531 CA VAL A 341 2875 2757 3011 56 26 51 C ATOM 1532 C VAL A 341 32.016 36.348 74.765 1.00 21.63 C ANISOU 1532 C VAL A 341 2672 2630 2916 92 74 24 C ATOM 1533 O VAL A 341 31.461 35.707 75.651 1.00 22.35 O ANISOU 1533 O VAL A 341 3037 2630 2823 74 97 49 O ATOM 1534 CB VAL A 341 30.512 36.141 72.777 1.00 22.46 C ANISOU 1534 CB VAL A 341 2842 2793 2895 15 41 -32 C ATOM 1535 CG1 VAL A 341 30.171 37.600 72.898 1.00 23.01 C ANISOU 1535 CG1 VAL A 341 3103 2746 2894 89 -73 144 C ATOM 1536 CG2 VAL A 341 30.353 35.690 71.321 1.00 22.82 C ANISOU 1536 CG2 VAL A 341 2772 2923 2973 -6 61 -69 C ATOM 1537 N PRO A 342 32.718 37.431 75.049 1.00 20.37 N ANISOU 1537 N PRO A 342 2560 2494 2686 112 81 22 N ATOM 1538 CA PRO A 342 32.788 37.960 76.412 1.00 20.78 C ANISOU 1538 CA PRO A 342 2618 2612 2663 65 53 67 C ATOM 1539 C PRO A 342 31.437 38.491 76.876 1.00 20.05 C ANISOU 1539 C PRO A 342 2498 2619 2498 93 21 65 C ATOM 1540 O PRO A 342 30.873 39.348 76.195 1.00 21.07 O ANISOU 1540 O PRO A 342 2686 2850 2467 39 57 185 O ATOM 1541 CB PRO A 342 33.791 39.096 76.297 1.00 21.23 C ANISOU 1541 CB PRO A 342 2615 2747 2703 37 -41 5 C ATOM 1542 CG PRO A 342 33.724 39.503 74.863 1.00 22.73 C ANISOU 1542 CG PRO A 342 2955 2770 2911 -116 105 28 C ATOM 1543 CD PRO A 342 33.518 38.227 74.098 1.00 21.61 C ANISOU 1543 CD PRO A 342 2708 2635 2868 -37 57 -10 C ATOM 1544 N LEU A 343 30.940 38.010 78.015 1.00 19.47 N ANISOU 1544 N LEU A 343 2349 2558 2487 89 -98 121 N ATOM 1545 CA LEU A 343 29.615 38.341 78.521 1.00 18.66 C ANISOU 1545 CA LEU A 343 2297 2404 2387 19 -85 76 C ATOM 1546 C LEU A 343 29.651 39.145 79.830 1.00 17.98 C ANISOU 1546 C LEU A 343 2126 2388 2314 82 -77 42 C ATOM 1547 O LEU A 343 30.511 38.923 80.706 1.00 20.69 O ANISOU 1547 O LEU A 343 2687 2597 2575 68 -240 124 O ATOM 1548 CB LEU A 343 28.871 37.035 78.772 1.00 18.65 C ANISOU 1548 CB LEU A 343 2179 2503 2404 -22 -140 100 C ATOM 1549 CG LEU A 343 28.753 36.079 77.611 1.00 19.06 C ANISOU 1549 CG LEU A 343 2285 2432 2522 96 38 4 C ATOM 1550 CD1 LEU A 343 28.097 34.812 78.063 1.00 20.81 C ANISOU 1550 CD1 LEU A 343 2646 2637 2622 6 48 32 C ATOM 1551 CD2 LEU A 343 27.976 36.703 76.434 1.00 20.00 C ANISOU 1551 CD2 LEU A 343 2528 2460 2609 33 -87 26 C ATOM 1552 N ALA A 344 28.717 40.078 79.978 1.00 17.25 N ANISOU 1552 N ALA A 344 2170 2144 2236 5 -66 76 N ATOM 1553 CA ALA A 344 28.548 40.853 81.196 1.00 17.60 C ANISOU 1553 CA ALA A 344 2168 2268 2251 -9 -103 21 C ATOM 1554 C ALA A 344 27.909 39.952 82.241 1.00 17.82 C ANISOU 1554 C ALA A 344 2285 2206 2279 -24 -103 68 C ATOM 1555 O ALA A 344 27.251 38.977 81.888 1.00 17.77 O ANISOU 1555 O ALA A 344 2335 2109 2304 -28 -194 112 O ATOM 1556 CB ALA A 344 27.641 42.052 80.940 1.00 16.98 C ANISOU 1556 CB ALA A 344 2086 2275 2091 -17 -194 -17 C ATOM 1557 N PRO A 345 28.054 40.281 83.522 1.00 19.10 N ANISOU 1557 N PRO A 345 2484 2425 2349 -93 -123 98 N ATOM 1558 CA PRO A 345 27.300 39.594 84.587 1.00 19.45 C ANISOU 1558 CA PRO A 345 2418 2544 2427 -50 -66 88 C ATOM 1559 C PRO A 345 25.795 39.532 84.375 1.00 19.01 C ANISOU 1559 C PRO A 345 2388 2451 2385 -61 -56 92 C ATOM 1560 O PRO A 345 25.159 38.504 84.704 1.00 19.87 O ANISOU 1560 O PRO A 345 2568 2566 2413 -115 -134 295 O ATOM 1561 CB PRO A 345 27.630 40.409 85.848 1.00 19.66 C ANISOU 1561 CB PRO A 345 2406 2596 2467 -23 -48 12 C ATOM 1562 CG PRO A 345 28.947 41.024 85.556 1.00 20.58 C ANISOU 1562 CG PRO A 345 2574 2780 2463 -117 -16 61 C ATOM 1563 CD PRO A 345 28.973 41.295 84.067 1.00 19.65 C ANISOU 1563 CD PRO A 345 2468 2557 2442 -68 -106 74 C ATOM 1564 N ASP A 346 25.228 40.563 83.759 1.00 18.17 N ANISOU 1564 N ASP A 346 2265 2388 2250 -41 -70 128 N ATOM 1565 CA ASP A 346 23.778 40.584 83.571 1.00 17.28 C ANISOU 1565 CA ASP A 346 2176 2245 2143 -41 12 37 C ATOM 1566 C ASP A 346 23.234 39.614 82.492 1.00 17.52 C ANISOU 1566 C ASP A 346 2239 2253 2165 1 -13 33 C ATOM 1567 O ASP A 346 22.022 39.407 82.428 1.00 18.04 O ANISOU 1567 O ASP A 346 2334 2329 2190 -184 -110 89 O ATOM 1568 CB ASP A 346 23.228 42.026 83.440 1.00 16.99 C ANISOU 1568 CB ASP A 346 2176 2208 2070 -85 -18 147 C ATOM 1569 CG ASP A 346 23.442 42.663 82.091 1.00 16.42 C ANISOU 1569 CG ASP A 346 1946 2190 2102 3 -41 53 C ATOM 1570 OD1 ASP A 346 23.884 41.999 81.131 1.00 16.77 O ANISOU 1570 OD1 ASP A 346 2035 2407 1929 -103 35 287 O ATOM 1571 OD2 ASP A 346 23.125 43.889 81.974 1.00 17.66 O ANISOU 1571 OD2 ASP A 346 2177 2235 2297 -96 -68 309 O ATOM 1572 N ILE A 347 24.110 38.978 81.716 1.00 17.06 N ANISOU 1572 N ILE A 347 2213 2194 2073 23 -39 87 N ATOM 1573 CA ILE A 347 23.651 38.070 80.673 1.00 17.10 C ANISOU 1573 CA ILE A 347 2207 2102 2186 2 -93 39 C ATOM 1574 C ILE A 347 22.953 36.844 81.270 1.00 16.79 C ANISOU 1574 C ILE A 347 2115 2122 2139 -12 -114 49 C ATOM 1575 O ILE A 347 23.479 36.155 82.151 1.00 18.31 O ANISOU 1575 O ILE A 347 2257 2318 2380 -62 -269 227 O ATOM 1576 CB ILE A 347 24.825 37.650 79.707 1.00 17.72 C ANISOU 1576 CB ILE A 347 2252 2241 2238 -55 -18 60 C ATOM 1577 CG1 ILE A 347 25.314 38.851 78.864 1.00 17.55 C ANISOU 1577 CG1 ILE A 347 2187 2160 2319 18 -96 26 C ATOM 1578 CG2 ILE A 347 24.440 36.462 78.834 1.00 19.58 C ANISOU 1578 CG2 ILE A 347 2370 2417 2650 37 -91 51 C ATOM 1579 CD1 ILE A 347 24.359 39.335 77.786 1.00 18.34 C ANISOU 1579 CD1 ILE A 347 2604 2112 2249 -206 -108 95 C ATOM 1580 N ASP A 348 21.745 36.579 80.783 1.00 15.67 N ANISOU 1580 N ASP A 348 2063 1861 2028 -3 -110 -20 N ATOM 1581 CA ASP A 348 20.986 35.401 81.144 1.00 15.52 C ANISOU 1581 CA ASP A 348 2036 1924 1933 33 -92 37 C ATOM 1582 C ASP A 348 20.405 34.803 79.869 1.00 15.11 C ANISOU 1582 C ASP A 348 2047 1754 1936 63 -31 -19 C ATOM 1583 O ASP A 348 19.483 35.357 79.268 1.00 14.25 O ANISOU 1583 O ASP A 348 1968 1525 1920 68 -145 -108 O ATOM 1584 CB ASP A 348 19.904 35.817 82.114 1.00 15.16 C ANISOU 1584 CB ASP A 348 2000 1769 1989 -55 -64 -6 C ATOM 1585 CG ASP A 348 19.175 34.650 82.706 1.00 16.33 C ANISOU 1585 CG ASP A 348 2343 1870 1992 -78 -80 56 C ATOM 1586 OD1 ASP A 348 18.958 33.638 81.965 1.00 18.06 O ANISOU 1586 OD1 ASP A 348 2865 1831 2166 -153 -18 -111 O ATOM 1587 OD2 ASP A 348 18.808 34.644 83.896 1.00 17.55 O ANISOU 1587 OD2 ASP A 348 2736 1663 2269 -109 98 -26 O ATOM 1588 N ALA A 349 20.960 33.684 79.426 1.00 15.28 N ANISOU 1588 N ALA A 349 2123 1677 2005 100 -88 -12 N ATOM 1589 CA ALA A 349 20.491 33.051 78.196 1.00 15.74 C ANISOU 1589 CA ALA A 349 2102 1814 2063 108 -1 -24 C ATOM 1590 C ALA A 349 19.069 32.561 78.266 1.00 15.18 C ANISOU 1590 C ALA A 349 2080 1679 2008 121 21 -26 C ATOM 1591 O ALA A 349 18.408 32.528 77.240 1.00 15.46 O ANISOU 1591 O ALA A 349 2124 1651 2100 162 21 55 O ATOM 1592 CB ALA A 349 21.418 31.894 77.829 1.00 16.24 C ANISOU 1592 CB ALA A 349 1977 1971 2219 201 82 -43 C ATOM 1593 N ALA A 350 18.585 32.180 79.451 1.00 14.64 N ANISOU 1593 N ALA A 350 1992 1627 1943 137 -106 6 N ATOM 1594 CA ALA A 350 17.209 31.786 79.622 1.00 14.64 C ANISOU 1594 CA ALA A 350 2003 1671 1887 127 -12 -18 C ATOM 1595 C ALA A 350 16.289 32.968 79.397 1.00 14.03 C ANISOU 1595 C ALA A 350 1916 1534 1878 60 -89 -13 C ATOM 1596 O ALA A 350 15.236 32.801 78.766 1.00 14.09 O ANISOU 1596 O ALA A 350 2019 1293 2042 189 -66 6 O ATOM 1597 CB ALA A 350 16.973 31.153 80.996 1.00 14.99 C ANISOU 1597 CB ALA A 350 2028 1710 1957 205 32 -54 C ATOM 1598 N ILE A 351 16.705 34.158 79.855 1.00 13.26 N ANISOU 1598 N ILE A 351 1827 1491 1719 76 -73 13 N ATOM 1599 CA ILE A 351 15.862 35.319 79.632 1.00 12.25 C ANISOU 1599 CA ILE A 351 1724 1376 1554 83 -24 -10 C ATOM 1600 C ILE A 351 15.865 35.701 78.139 1.00 12.62 C ANISOU 1600 C ILE A 351 1746 1398 1648 25 -66 46 C ATOM 1601 O ILE A 351 14.811 36.017 77.580 1.00 12.65 O ANISOU 1601 O ILE A 351 1776 1288 1740 13 -78 213 O ATOM 1602 CB ILE A 351 16.312 36.490 80.508 1.00 12.83 C ANISOU 1602 CB ILE A 351 1756 1416 1701 68 -85 7 C ATOM 1603 CG1 ILE A 351 15.975 36.165 81.962 1.00 14.36 C ANISOU 1603 CG1 ILE A 351 2016 1590 1850 30 -43 -43 C ATOM 1604 CG2 ILE A 351 15.633 37.821 80.019 1.00 12.60 C ANISOU 1604 CG2 ILE A 351 1629 1490 1665 281 -89 -238 C ATOM 1605 CD1 ILE A 351 16.325 37.281 82.925 1.00 17.16 C ANISOU 1605 CD1 ILE A 351 2421 2153 1946 -103 -81 -113 C ATOM 1606 N ILE A 352 17.021 35.635 77.501 1.00 12.38 N ANISOU 1606 N ILE A 352 1857 1225 1622 -53 -36 131 N ATOM 1607 CA ILE A 352 17.067 35.885 76.056 1.00 13.12 C ANISOU 1607 CA ILE A 352 1831 1495 1657 19 -92 38 C ATOM 1608 C ILE A 352 16.124 34.916 75.313 1.00 13.05 C ANISOU 1608 C ILE A 352 1795 1397 1765 61 -89 60 C ATOM 1609 O ILE A 352 15.319 35.328 74.457 1.00 13.00 O ANISOU 1609 O ILE A 352 1697 1371 1870 14 -249 103 O ATOM 1610 CB ILE A 352 18.503 35.847 75.514 1.00 13.31 C ANISOU 1610 CB ILE A 352 1907 1430 1720 -49 -63 109 C ATOM 1611 CG1 ILE A 352 19.392 36.905 76.175 1.00 14.60 C ANISOU 1611 CG1 ILE A 352 2099 1601 1845 -154 -75 88 C ATOM 1612 CG2 ILE A 352 18.502 36.084 74.026 1.00 14.23 C ANISOU 1612 CG2 ILE A 352 2023 1748 1636 -48 -15 -2 C ATOM 1613 CD1 ILE A 352 20.863 36.717 75.965 1.00 15.73 C ANISOU 1613 CD1 ILE A 352 2200 1710 2065 -180 -99 155 C ATOM 1614 N ALA A 353 16.165 33.645 75.680 1.00 12.41 N ANISOU 1614 N ALA A 353 1684 1338 1691 0 -24 72 N ATOM 1615 CA ALA A 353 15.317 32.644 75.075 1.00 13.87 C ANISOU 1615 CA ALA A 353 1967 1591 1712 35 -30 57 C ATOM 1616 C ALA A 353 13.841 32.927 75.271 1.00 13.15 C ANISOU 1616 C ALA A 353 1917 1405 1673 74 -28 7 C ATOM 1617 O ALA A 353 13.039 32.755 74.341 1.00 13.40 O ANISOU 1617 O ALA A 353 2004 1442 1645 -3 -91 -13 O ATOM 1618 CB ALA A 353 15.690 31.281 75.644 1.00 12.45 C ANISOU 1618 CB ALA A 353 1770 1374 1583 241 61 -34 C ATOM 1619 N ARG A 354 13.445 33.438 76.452 1.00 12.52 N ANISOU 1619 N ARG A 354 1813 1410 1532 153 -5 9 N ATOM 1620 CA ARG A 354 12.045 33.765 76.704 1.00 12.98 C ANISOU 1620 CA ARG A 354 1701 1555 1676 22 -126 28 C ATOM 1621 C ARG A 354 11.537 34.820 75.734 1.00 12.15 C ANISOU 1621 C ARG A 354 1668 1320 1627 -4 -28 -68 C ATOM 1622 O ARG A 354 10.371 34.852 75.407 1.00 12.49 O ANISOU 1622 O ARG A 354 1739 1236 1770 -35 -226 61 O ATOM 1623 CB ARG A 354 11.846 34.333 78.105 1.00 14.82 C ANISOU 1623 CB ARG A 354 1922 1922 1787 57 -88 44 C ATOM 1624 CG ARG A 354 12.042 33.439 79.306 1.00 18.12 C ANISOU 1624 CG ARG A 354 2403 2077 2405 141 -6 98 C ATOM 1625 CD ARG A 354 11.978 34.301 80.621 1.00 20.94 C ANISOU 1625 CD ARG A 354 2740 2813 2400 121 -19 97 C ATOM 1626 NE ARG A 354 11.860 33.408 81.761 1.00 23.62 N ANISOU 1626 NE ARG A 354 3318 2803 2851 -38 163 177 N ATOM 1627 CZ ARG A 354 11.430 33.755 82.962 1.00 22.93 C ANISOU 1627 CZ ARG A 354 3204 2671 2837 154 85 -2 C ATOM 1628 NH1 ARG A 354 11.122 35.031 83.245 1.00 19.81 N ANISOU 1628 NH1 ARG A 354 3027 2137 2361 -70 -67 -83 N ATOM 1629 NH2 ARG A 354 11.323 32.817 83.906 1.00 24.35 N ANISOU 1629 NH2 ARG A 354 3430 2594 3226 115 30 67 N ATOM 1630 N GLY A 355 12.411 35.711 75.340 1.00 12.35 N ANISOU 1630 N GLY A 355 1741 1292 1656 -29 -105 -1 N ATOM 1631 CA GLY A 355 12.009 36.827 74.507 1.00 12.40 C ANISOU 1631 CA GLY A 355 1671 1429 1611 -79 -171 62 C ATOM 1632 C GLY A 355 12.128 36.601 73.017 1.00 12.88 C ANISOU 1632 C GLY A 355 1770 1485 1637 -77 -124 9 C ATOM 1633 O GLY A 355 11.853 37.532 72.258 1.00 13.86 O ANISOU 1633 O GLY A 355 2075 1538 1651 -71 -302 63 O ATOM 1634 N THR A 356 12.496 35.391 72.596 1.00 12.42 N ANISOU 1634 N THR A 356 1780 1458 1480 -113 -121 -28 N ATOM 1635 CA THR A 356 12.779 35.104 71.181 1.00 13.20 C ANISOU 1635 CA THR A 356 1882 1514 1616 -53 -107 25 C ATOM 1636 C THR A 356 11.953 33.931 70.619 1.00 12.61 C ANISOU 1636 C THR A 356 1854 1438 1497 16 -91 22 C ATOM 1637 O THR A 356 12.504 33.117 69.862 1.00 13.77 O ANISOU 1637 O THR A 356 1990 1439 1802 156 -233 -35 O ATOM 1638 CB THR A 356 14.283 34.862 70.959 1.00 13.81 C ANISOU 1638 CB THR A 356 1980 1689 1577 -156 -103 -11 C ATOM 1639 OG1 THR A 356 14.796 33.915 71.923 1.00 14.18 O ANISOU 1639 OG1 THR A 356 1743 1865 1776 -53 -79 120 O ATOM 1640 CG2 THR A 356 15.112 36.139 71.135 1.00 15.23 C ANISOU 1640 CG2 THR A 356 2222 1808 1754 -200 -49 97 C ATOM 1641 N PRO A 357 10.646 33.870 70.856 1.00 12.51 N ANISOU 1641 N PRO A 357 1830 1328 1593 -61 -120 -40 N ATOM 1642 CA PRO A 357 9.868 32.755 70.272 1.00 12.53 C ANISOU 1642 CA PRO A 357 1807 1354 1598 -88 -87 4 C ATOM 1643 C PRO A 357 9.976 32.764 68.751 1.00 14.26 C ANISOU 1643 C PRO A 357 2013 1598 1807 -46 0 -29 C ATOM 1644 O PRO A 357 10.024 33.813 68.124 1.00 13.12 O ANISOU 1644 O PRO A 357 1918 1461 1603 -314 -184 12 O ATOM 1645 CB PRO A 357 8.439 33.073 70.701 1.00 12.46 C ANISOU 1645 CB PRO A 357 1807 1295 1631 -107 -68 -68 C ATOM 1646 CG PRO A 357 8.451 34.598 70.942 1.00 12.02 C ANISOU 1646 CG PRO A 357 1794 1269 1503 -22 -53 -4 C ATOM 1647 CD PRO A 357 9.767 34.842 71.518 1.00 12.52 C ANISOU 1647 CD PRO A 357 1694 1426 1636 33 -112 3 C ATOM 1648 N GLY A 358 10.019 31.567 68.164 1.00 14.36 N ANISOU 1648 N GLY A 358 2063 1637 1754 -37 -16 -90 N ATOM 1649 CA GLY A 358 10.085 31.431 66.731 1.00 14.94 C ANISOU 1649 CA GLY A 358 2051 1849 1775 10 -23 -93 C ATOM 1650 C GLY A 358 11.413 31.722 66.074 1.00 14.27 C ANISOU 1650 C GLY A 358 1897 1746 1778 70 -38 -58 C ATOM 1651 O GLY A 358 11.539 31.604 64.829 1.00 16.37 O ANISOU 1651 O GLY A 358 2113 2191 1915 31 70 -221 O ATOM 1652 N PHE A 359 12.433 32.082 66.852 1.00 14.03 N ANISOU 1652 N PHE A 359 1823 1798 1710 47 -16 -156 N ATOM 1653 CA PHE A 359 13.768 32.280 66.264 1.00 15.02 C ANISOU 1653 CA PHE A 359 1978 1976 1751 53 54 -67 C ATOM 1654 C PHE A 359 14.345 30.958 65.870 1.00 15.61 C ANISOU 1654 C PHE A 359 1999 2002 1930 57 85 0 C ATOM 1655 O PHE A 359 14.337 30.005 66.645 1.00 16.27 O ANISOU 1655 O PHE A 359 2184 1936 2062 149 165 -53 O ATOM 1656 CB PHE A 359 14.753 32.980 67.223 1.00 14.52 C ANISOU 1656 CB PHE A 359 1821 1810 1885 2 -1 40 C ATOM 1657 CG PHE A 359 14.668 34.478 67.236 1.00 14.90 C ANISOU 1657 CG PHE A 359 2168 2012 1479 -34 6 -3 C ATOM 1658 CD1 PHE A 359 13.457 35.122 67.325 1.00 15.87 C ANISOU 1658 CD1 PHE A 359 2294 1790 1943 -152 -168 126 C ATOM 1659 CD2 PHE A 359 15.834 35.240 67.237 1.00 16.85 C ANISOU 1659 CD2 PHE A 359 2420 2114 1868 -53 -190 88 C ATOM 1660 CE1 PHE A 359 13.409 36.498 67.360 1.00 17.25 C ANISOU 1660 CE1 PHE A 359 2251 2031 2273 -81 -55 -64 C ATOM 1661 CE2 PHE A 359 15.762 36.635 67.302 1.00 16.67 C ANISOU 1661 CE2 PHE A 359 2209 2169 1956 -146 -114 95 C ATOM 1662 CZ PHE A 359 14.601 37.233 67.352 1.00 16.47 C ANISOU 1662 CZ PHE A 359 2208 1874 2175 -166 -24 38 C ATOM 1663 N SER A 360 14.896 30.920 64.650 1.00 16.36 N ANISOU 1663 N SER A 360 2181 2114 1919 78 53 -12 N ATOM 1664 CA SER A 360 15.608 29.721 64.215 1.00 15.00 C ANISOU 1664 CA SER A 360 1935 1886 1879 -11 52 -59 C ATOM 1665 C SER A 360 17.041 29.666 64.758 1.00 15.32 C ANISOU 1665 C SER A 360 2046 1871 1903 0 20 -4 C ATOM 1666 O SER A 360 17.529 30.634 65.340 1.00 15.22 O ANISOU 1666 O SER A 360 1989 1846 1947 -193 87 64 O ATOM 1667 CB SER A 360 15.699 29.722 62.691 1.00 15.70 C ANISOU 1667 CB SER A 360 2022 2058 1883 -70 27 -84 C ATOM 1668 OG SER A 360 16.603 30.749 62.252 1.00 15.96 O ANISOU 1668 OG SER A 360 2276 2002 1784 -66 57 56 O ATOM 1669 N GLY A 361 17.752 28.553 64.541 1.00 16.63 N ANISOU 1669 N GLY A 361 2184 2053 2082 -45 30 -77 N ATOM 1670 CA GLY A 361 19.141 28.514 64.890 1.00 17.00 C ANISOU 1670 CA GLY A 361 2238 2070 2149 -12 -24 -23 C ATOM 1671 C GLY A 361 19.979 29.606 64.265 1.00 17.00 C ANISOU 1671 C GLY A 361 2227 2107 2125 -4 -33 -10 C ATOM 1672 O GLY A 361 20.829 30.159 64.935 1.00 16.76 O ANISOU 1672 O GLY A 361 2078 2208 2082 -37 -64 -77 O ATOM 1673 N ALA A 362 19.753 29.899 62.987 1.00 16.50 N ANISOU 1673 N ALA A 362 2189 2081 1996 -4 -50 -119 N ATOM 1674 CA ALA A 362 20.483 30.948 62.312 1.00 16.34 C ANISOU 1674 CA ALA A 362 2111 2116 1982 24 16 -62 C ATOM 1675 C ALA A 362 20.144 32.271 62.940 1.00 15.53 C ANISOU 1675 C ALA A 362 2018 2038 1842 8 -65 -76 C ATOM 1676 O ALA A 362 21.021 33.088 63.147 1.00 16.27 O ANISOU 1676 O ALA A 362 2151 2267 1763 -170 146 -133 O ATOM 1677 CB ALA A 362 20.168 30.994 60.836 1.00 17.24 C ANISOU 1677 CB ALA A 362 2362 2114 2075 -31 72 -131 C ATOM 1678 N ASP A 363 18.854 32.498 63.228 1.00 15.19 N ANISOU 1678 N ASP A 363 1960 2094 1718 -45 30 -171 N ATOM 1679 CA ASP A 363 18.433 33.737 63.883 1.00 15.17 C ANISOU 1679 CA ASP A 363 2027 1924 1811 -52 -6 -49 C ATOM 1680 C ASP A 363 19.157 33.917 65.216 1.00 15.11 C ANISOU 1680 C ASP A 363 2022 1905 1810 -66 16 -60 C ATOM 1681 O ASP A 363 19.519 35.045 65.546 1.00 16.04 O ANISOU 1681 O ASP A 363 2174 1951 1967 -112 101 -191 O ATOM 1682 CB ASP A 363 16.954 33.749 64.182 1.00 16.06 C ANISOU 1682 CB ASP A 363 2157 2059 1885 48 73 -160 C ATOM 1683 CG ASP A 363 16.055 33.814 62.975 1.00 17.63 C ANISOU 1683 CG ASP A 363 2242 2336 2119 -35 -23 -72 C ATOM 1684 OD1 ASP A 363 16.425 34.381 61.907 1.00 20.33 O ANISOU 1684 OD1 ASP A 363 2642 2785 2294 -221 -109 168 O ATOM 1685 OD2 ASP A 363 14.878 33.379 63.043 1.00 19.26 O ANISOU 1685 OD2 ASP A 363 2447 2353 2515 -57 119 -45 O ATOM 1686 N LEU A 364 19.308 32.851 65.987 1.00 14.14 N ANISOU 1686 N LEU A 364 1879 1748 1746 -141 -60 -114 N ATOM 1687 CA LEU A 364 19.998 32.919 67.283 1.00 15.25 C ANISOU 1687 CA LEU A 364 2044 1926 1822 -4 -26 -26 C ATOM 1688 C LEU A 364 21.494 33.187 67.100 1.00 15.90 C ANISOU 1688 C LEU A 364 2060 2023 1958 -15 25 -72 C ATOM 1689 O LEU A 364 22.090 33.995 67.814 1.00 16.10 O ANISOU 1689 O LEU A 364 2038 2156 1922 -104 -6 -23 O ATOM 1690 CB LEU A 364 19.764 31.663 68.105 1.00 15.48 C ANISOU 1690 CB LEU A 364 2095 1945 1839 -6 -41 -33 C ATOM 1691 CG LEU A 364 18.329 31.445 68.509 1.00 15.55 C ANISOU 1691 CG LEU A 364 2006 1997 1903 52 -134 19 C ATOM 1692 CD1 LEU A 364 18.120 30.045 68.989 1.00 19.36 C ANISOU 1692 CD1 LEU A 364 2564 2479 2312 -181 -30 147 C ATOM 1693 CD2 LEU A 364 17.822 32.469 69.533 1.00 16.58 C ANISOU 1693 CD2 LEU A 364 1943 2265 2090 -1 11 -37 C ATOM 1694 N ALA A 365 22.131 32.545 66.119 1.00 16.17 N ANISOU 1694 N ALA A 365 2052 2208 1883 -104 67 -196 N ATOM 1695 CA ALA A 365 23.534 32.857 65.841 1.00 15.70 C ANISOU 1695 CA ALA A 365 1992 2015 1958 -12 -12 -107 C ATOM 1696 C ALA A 365 23.699 34.329 65.450 1.00 16.23 C ANISOU 1696 C ALA A 365 2018 2175 1971 -97 71 -45 C ATOM 1697 O ALA A 365 24.638 34.993 65.876 1.00 16.89 O ANISOU 1697 O ALA A 365 2230 2214 1971 -219 77 -156 O ATOM 1698 CB ALA A 365 24.053 31.946 64.748 1.00 16.66 C ANISOU 1698 CB ALA A 365 2219 2082 2027 -79 12 -151 C ATOM 1699 N ASN A 366 22.782 34.819 64.640 1.00 15.54 N ANISOU 1699 N ASN A 366 2101 1916 1888 -38 58 -45 N ATOM 1700 CA ASN A 366 22.810 36.212 64.209 1.00 16.39 C ANISOU 1700 CA ASN A 366 2137 2031 2059 -80 12 -89 C ATOM 1701 C ASN A 366 22.475 37.193 65.315 1.00 15.81 C ANISOU 1701 C ASN A 366 1995 2013 1998 -112 95 -118 C ATOM 1702 O ASN A 366 23.013 38.284 65.354 1.00 14.93 O ANISOU 1702 O ASN A 366 1910 1919 1842 -185 61 18 O ATOM 1703 CB ASN A 366 22.032 36.389 62.906 1.00 18.20 C ANISOU 1703 CB ASN A 366 2638 2205 2069 -34 61 83 C ATOM 1704 CG AASN A 366 22.993 37.016 61.795 0.50 14.35 C ANISOU 1704 CG AASN A 366 1655 1626 2170 15 32 -125 C ATOM 1705 CG BASN A 366 21.859 37.850 62.403 0.25 16.26 C ANISOU 1705 CG BASN A 366 2224 1998 1955 80 0 -107 C ATOM 1706 OD1AASN A 366 24.214 36.914 61.916 0.50 16.09 O ANISOU 1706 OD1AASN A 366 2104 1926 2082 -33 -46 127 O ATOM 1707 OD1BASN A 366 22.637 38.368 61.648 0.25 17.34 O ANISOU 1707 OD1BASN A 366 2283 2122 2183 -27 -65 39 O ATOM 1708 ND2AASN A 366 22.453 37.592 60.771 0.50 18.70 N ANISOU 1708 ND2AASN A 366 2703 2208 2194 -204 -173 153 N ATOM 1709 ND2BASN A 366 20.749 38.469 62.802 0.25 19.15 N ANISOU 1709 ND2BASN A 366 2371 2645 2259 -14 -58 0 N ATOM 1710 N LEU A 367 21.612 36.788 66.239 1.00 15.61 N ANISOU 1710 N LEU A 367 2074 1949 1906 -248 49 -38 N ATOM 1711 CA LEU A 367 21.289 37.593 67.403 1.00 14.59 C ANISOU 1711 CA LEU A 367 1831 1907 1803 -154 33 -22 C ATOM 1712 C LEU A 367 22.556 37.832 68.224 1.00 14.04 C ANISOU 1712 C LEU A 367 1795 1822 1716 -86 74 -45 C ATOM 1713 O LEU A 367 22.848 38.978 68.610 1.00 14.30 O ANISOU 1713 O LEU A 367 1907 1749 1777 -328 138 -1 O ATOM 1714 CB LEU A 367 20.197 36.931 68.233 1.00 15.87 C ANISOU 1714 CB LEU A 367 2060 2006 1961 -185 16 -12 C ATOM 1715 CG LEU A 367 19.812 37.647 69.516 1.00 16.39 C ANISOU 1715 CG LEU A 367 2080 2195 1952 -104 99 34 C ATOM 1716 CD1 LEU A 367 19.153 38.954 69.218 1.00 18.81 C ANISOU 1716 CD1 LEU A 367 2520 2398 2228 68 143 -153 C ATOM 1717 CD2 LEU A 367 18.891 36.764 70.326 1.00 17.58 C ANISOU 1717 CD2 LEU A 367 2338 2224 2116 -260 315 -84 C ATOM 1718 N VAL A 368 23.332 36.789 68.462 1.00 14.91 N ANISOU 1718 N VAL A 368 1880 1920 1864 -110 121 -35 N ATOM 1719 CA VAL A 368 24.588 36.915 69.209 1.00 15.33 C ANISOU 1719 CA VAL A 368 2007 2004 1813 -59 1 -25 C ATOM 1720 C VAL A 368 25.548 37.824 68.412 1.00 14.79 C ANISOU 1720 C VAL A 368 1930 1900 1791 -54 -10 -30 C ATOM 1721 O VAL A 368 26.192 38.683 68.960 1.00 14.87 O ANISOU 1721 O VAL A 368 1907 1953 1787 -78 -125 -3 O ATOM 1722 CB VAL A 368 25.241 35.548 69.504 1.00 16.19 C ANISOU 1722 CB VAL A 368 2141 2060 1948 -123 -15 -60 C ATOM 1723 CG1 VAL A 368 26.625 35.703 70.131 1.00 16.89 C ANISOU 1723 CG1 VAL A 368 2325 2131 1960 55 107 40 C ATOM 1724 CG2 VAL A 368 24.276 34.709 70.365 1.00 17.45 C ANISOU 1724 CG2 VAL A 368 2325 2260 2045 -51 86 -131 C ATOM 1725 N ASN A 369 25.655 37.608 67.108 1.00 14.72 N ANISOU 1725 N ASN A 369 1863 2023 1707 21 -58 46 N ATOM 1726 CA ASN A 369 26.499 38.465 66.288 1.00 14.43 C ANISOU 1726 CA ASN A 369 1777 1920 1784 -25 -32 -38 C ATOM 1727 C ASN A 369 26.089 39.922 66.355 1.00 13.99 C ANISOU 1727 C ASN A 369 1661 1929 1725 -56 -67 -33 C ATOM 1728 O ASN A 369 26.926 40.796 66.492 1.00 14.39 O ANISOU 1728 O ASN A 369 1751 1891 1823 -70 41 -19 O ATOM 1729 CB ASN A 369 26.428 38.045 64.804 1.00 14.86 C ANISOU 1729 CB ASN A 369 2010 1920 1713 -31 27 17 C ATOM 1730 CG ASN A 369 27.167 36.763 64.500 1.00 15.80 C ANISOU 1730 CG ASN A 369 1999 2164 1838 105 -62 -27 C ATOM 1731 OD1 ASN A 369 28.077 36.360 65.212 1.00 15.63 O ANISOU 1731 OD1 ASN A 369 2203 1994 1741 153 -2 -61 O ATOM 1732 ND2 ASN A 369 26.792 36.143 63.379 1.00 14.29 N ANISOU 1732 ND2 ASN A 369 1763 1805 1861 -61 -26 -145 N ATOM 1733 N GLU A 370 24.784 40.194 66.238 1.00 14.45 N ANISOU 1733 N GLU A 370 1667 1870 1952 93 45 -23 N ATOM 1734 CA GLU A 370 24.317 41.576 66.228 1.00 14.98 C ANISOU 1734 CA GLU A 370 1876 1832 1984 -62 76 19 C ATOM 1735 C GLU A 370 24.489 42.215 67.599 1.00 14.09 C ANISOU 1735 C GLU A 370 1661 1800 1889 -43 -8 34 C ATOM 1736 O GLU A 370 24.816 43.405 67.689 1.00 14.53 O ANISOU 1736 O GLU A 370 1781 1883 1856 -105 -45 -28 O ATOM 1737 CB GLU A 370 22.889 41.662 65.768 1.00 16.73 C ANISOU 1737 CB GLU A 370 2144 1995 2215 -50 30 40 C ATOM 1738 CG GLU A 370 22.608 41.276 64.323 1.00 19.32 C ANISOU 1738 CG GLU A 370 2521 2478 2340 -153 -87 114 C ATOM 1739 CD GLU A 370 23.080 42.250 63.220 1.00 23.07 C ANISOU 1739 CD GLU A 370 3124 2693 2945 -26 -41 240 C ATOM 1740 OE1 GLU A 370 23.748 43.193 63.494 1.00 23.35 O ANISOU 1740 OE1 GLU A 370 2777 2939 3156 -3 -285 382 O ATOM 1741 OE2 GLU A 370 22.777 41.995 62.033 1.00 28.80 O ANISOU 1741 OE2 GLU A 370 3918 3745 3280 37 21 229 O ATOM 1742 N ALA A 371 24.337 41.440 68.661 1.00 14.38 N ANISOU 1742 N ALA A 371 1816 1825 1824 -129 -34 14 N ATOM 1743 CA ALA A 371 24.613 41.952 70.019 1.00 13.77 C ANISOU 1743 CA ALA A 371 1692 1756 1782 4 18 61 C ATOM 1744 C ALA A 371 26.122 42.321 70.175 1.00 13.79 C ANISOU 1744 C ALA A 371 1713 1784 1742 -66 -22 -22 C ATOM 1745 O ALA A 371 26.485 43.357 70.706 1.00 13.75 O ANISOU 1745 O ALA A 371 1457 1651 2115 -107 30 61 O ATOM 1746 CB ALA A 371 24.181 40.957 71.059 1.00 14.28 C ANISOU 1746 CB ALA A 371 1827 1768 1830 -57 22 43 C ATOM 1747 N ALA A 372 26.980 41.434 69.675 1.00 13.68 N ANISOU 1747 N ALA A 372 1634 1732 1831 -46 -41 -62 N ATOM 1748 CA ALA A 372 28.415 41.694 69.672 1.00 13.47 C ANISOU 1748 CA ALA A 372 1618 1743 1757 57 -111 -13 C ATOM 1749 C ALA A 372 28.761 42.912 68.834 1.00 13.79 C ANISOU 1749 C ALA A 372 1614 1798 1825 24 -101 -15 C ATOM 1750 O ALA A 372 29.600 43.733 69.238 1.00 12.91 O ANISOU 1750 O ALA A 372 1431 1588 1886 18 -56 77 O ATOM 1751 CB ALA A 372 29.185 40.454 69.218 1.00 13.86 C ANISOU 1751 CB ALA A 372 1613 1722 1931 -78 -181 -102 C ATOM 1752 N LEU A 373 28.088 43.067 67.683 1.00 12.97 N ANISOU 1752 N LEU A 373 1562 1583 1783 107 -83 0 N ATOM 1753 CA LEU A 373 28.291 44.257 66.857 1.00 13.47 C ANISOU 1753 CA LEU A 373 1508 1792 1818 -44 -71 94 C ATOM 1754 C LEU A 373 27.863 45.530 67.572 1.00 13.05 C ANISOU 1754 C LEU A 373 1436 1799 1722 45 -132 106 C ATOM 1755 O LEU A 373 28.578 46.537 67.540 1.00 12.42 O ANISOU 1755 O LEU A 373 1228 1504 1984 211 -230 96 O ATOM 1756 CB LEU A 373 27.592 44.123 65.514 1.00 14.08 C ANISOU 1756 CB LEU A 373 1612 1824 1913 47 -103 73 C ATOM 1757 CG LEU A 373 27.820 45.207 64.477 1.00 15.12 C ANISOU 1757 CG LEU A 373 1717 1946 2080 91 -150 163 C ATOM 1758 CD1 LEU A 373 29.266 45.380 64.166 1.00 15.25 C ANISOU 1758 CD1 LEU A 373 1885 1807 2099 -80 27 214 C ATOM 1759 CD2 LEU A 373 27.083 44.829 63.218 1.00 16.31 C ANISOU 1759 CD2 LEU A 373 2123 2043 2030 57 -23 79 C ATOM 1760 N PHE A 374 26.708 45.510 68.249 1.00 12.38 N ANISOU 1760 N PHE A 374 1320 1671 1710 124 -140 112 N ATOM 1761 CA PHE A 374 26.295 46.664 69.036 1.00 13.50 C ANISOU 1761 CA PHE A 374 1564 1761 1801 29 -13 14 C ATOM 1762 C PHE A 374 27.307 46.967 70.165 1.00 12.90 C ANISOU 1762 C PHE A 374 1524 1638 1736 167 -24 -53 C ATOM 1763 O PHE A 374 27.561 48.120 70.500 1.00 13.88 O ANISOU 1763 O PHE A 374 1399 1722 2153 39 -78 -25 O ATOM 1764 CB PHE A 374 24.887 46.449 69.623 1.00 14.28 C ANISOU 1764 CB PHE A 374 1573 1966 1884 129 -19 42 C ATOM 1765 CG PHE A 374 23.768 46.886 68.714 1.00 14.89 C ANISOU 1765 CG PHE A 374 1732 1953 1973 107 -90 20 C ATOM 1766 CD1 PHE A 374 23.625 48.211 68.352 1.00 18.91 C ANISOU 1766 CD1 PHE A 374 2345 2340 2497 -109 -129 203 C ATOM 1767 CD2 PHE A 374 22.878 45.958 68.226 1.00 17.42 C ANISOU 1767 CD2 PHE A 374 1965 2424 2227 -9 -111 31 C ATOM 1768 CE1 PHE A 374 22.581 48.602 67.508 1.00 19.91 C ANISOU 1768 CE1 PHE A 374 2347 2516 2702 22 -67 246 C ATOM 1769 CE2 PHE A 374 21.828 46.356 67.376 1.00 18.98 C ANISOU 1769 CE2 PHE A 374 1945 2679 2584 131 -58 105 C ATOM 1770 CZ PHE A 374 21.714 47.660 67.013 1.00 20.25 C ANISOU 1770 CZ PHE A 374 2448 2650 2595 74 -116 115 C ATOM 1771 N ALA A 375 27.859 45.930 70.779 1.00 13.72 N ANISOU 1771 N ALA A 375 1634 1775 1801 130 -80 32 N ATOM 1772 CA ALA A 375 28.876 46.154 71.803 1.00 13.36 C ANISOU 1772 CA ALA A 375 1595 1650 1828 90 -44 7 C ATOM 1773 C ALA A 375 30.092 46.826 71.190 1.00 13.55 C ANISOU 1773 C ALA A 375 1620 1647 1880 116 -85 83 C ATOM 1774 O ALA A 375 30.613 47.744 71.762 1.00 13.22 O ANISOU 1774 O ALA A 375 1502 1555 1964 66 -186 31 O ATOM 1775 CB ALA A 375 29.247 44.838 72.506 1.00 13.95 C ANISOU 1775 CB ALA A 375 1792 1728 1780 20 -110 101 C ATOM 1776 N ALA A 376 30.515 46.396 70.020 1.00 12.63 N ANISOU 1776 N ALA A 376 1449 1556 1792 -21 -153 0 N ATOM 1777 CA ALA A 376 31.650 46.994 69.344 1.00 13.33 C ANISOU 1777 CA ALA A 376 1470 1688 1906 57 26 55 C ATOM 1778 C ALA A 376 31.364 48.449 68.993 1.00 13.76 C ANISOU 1778 C ALA A 376 1580 1628 2018 -5 3 60 C ATOM 1779 O ALA A 376 32.203 49.316 69.160 1.00 14.24 O ANISOU 1779 O ALA A 376 1534 1713 2160 134 -125 -15 O ATOM 1780 CB ALA A 376 32.002 46.208 68.099 1.00 12.98 C ANISOU 1780 CB ALA A 376 1309 1606 2015 75 9 148 C ATOM 1781 N ARG A 377 30.140 48.704 68.512 1.00 14.39 N ANISOU 1781 N ARG A 377 1715 1580 2169 38 -110 25 N ATOM 1782 CA ARG A 377 29.676 50.040 68.090 1.00 15.86 C ANISOU 1782 CA ARG A 377 1907 1914 2204 30 -26 131 C ATOM 1783 C ARG A 377 29.673 51.000 69.259 1.00 15.71 C ANISOU 1783 C ARG A 377 1867 1964 2137 12 -74 118 C ATOM 1784 O ARG A 377 29.868 52.220 69.103 1.00 17.15 O ANISOU 1784 O ARG A 377 1899 2148 2469 36 -72 200 O ATOM 1785 CB ARG A 377 28.275 49.919 67.498 1.00 17.21 C ANISOU 1785 CB ARG A 377 2078 2088 2371 69 -48 134 C ATOM 1786 CG ARG A 377 28.202 49.878 66.000 0.50 20.18 C ANISOU 1786 CG ARG A 377 2505 2642 2519 22 5 53 C ATOM 1787 CD ARG A 377 26.807 49.557 65.438 0.50 22.45 C ANISOU 1787 CD ARG A 377 2762 2954 2812 -113 -59 41 C ATOM 1788 NE ARG A 377 26.391 50.546 64.444 0.50 23.71 N ANISOU 1788 NE ARG A 377 3076 2879 3050 44 -50 -1 N ATOM 1789 CZ ARG A 377 25.639 51.804 64.625 0.00 20.00 C ANISOU 1789 CZ ARG A 377 2533 2533 2533 0 0 0 C ATOM 1790 NH1 ARG A 377 25.438 52.673 63.642 0.00 20.00 N ANISOU 1790 NH1 ARG A 377 2533 2533 2533 0 0 0 N ATOM 1791 NH2 ARG A 377 24.997 51.978 65.773 0.00 20.00 N ANISOU 1791 NH2 ARG A 377 2533 2533 2533 0 0 0 N ATOM 1792 N GLY A 378 29.428 50.471 70.459 1.00 14.18 N ANISOU 1792 N GLY A 378 1644 1715 2025 33 3 124 N ATOM 1793 CA GLY A 378 29.403 51.239 71.670 1.00 13.72 C ANISOU 1793 CA GLY A 378 1571 1716 1925 3 -105 42 C ATOM 1794 C GLY A 378 30.716 51.253 72.436 1.00 13.76 C ANISOU 1794 C GLY A 378 1616 1767 1842 113 -106 -18 C ATOM 1795 O GLY A 378 30.773 51.795 73.540 1.00 14.93 O ANISOU 1795 O GLY A 378 1719 1752 2200 116 -96 92 O ATOM 1796 N ASN A 379 31.720 50.602 71.842 1.00 14.60 N ANISOU 1796 N ASN A 379 1719 1826 2000 31 -45 73 N ATOM 1797 CA ASN A 379 33.073 50.462 72.389 1.00 13.22 C ANISOU 1797 CA ASN A 379 1529 1642 1852 66 -56 35 C ATOM 1798 C ASN A 379 33.129 49.763 73.753 1.00 13.11 C ANISOU 1798 C ASN A 379 1560 1608 1813 10 21 31 C ATOM 1799 O ASN A 379 33.823 50.193 74.717 1.00 13.49 O ANISOU 1799 O ASN A 379 1380 1700 2043 -8 26 204 O ATOM 1800 CB ASN A 379 33.756 51.841 72.458 1.00 14.25 C ANISOU 1800 CB ASN A 379 1546 1841 2028 39 -31 116 C ATOM 1801 CG ASN A 379 35.247 51.722 72.470 1.00 13.52 C ANISOU 1801 CG ASN A 379 1576 1661 1897 185 -67 42 C ATOM 1802 OD1 ASN A 379 35.738 50.716 71.991 1.00 14.58 O ANISOU 1802 OD1 ASN A 379 1388 2060 2091 474 -161 258 O ATOM 1803 ND2 ASN A 379 35.954 52.702 73.050 1.00 13.90 N ANISOU 1803 ND2 ASN A 379 1455 1692 2132 361 -102 134 N ATOM 1804 N LYS A 380 32.357 48.694 73.848 1.00 12.94 N ANISOU 1804 N LYS A 380 1486 1585 1845 16 -90 -8 N ATOM 1805 CA LYS A 380 32.227 47.958 75.097 1.00 13.82 C ANISOU 1805 CA LYS A 380 1643 1726 1881 29 2 26 C ATOM 1806 C LYS A 380 33.076 46.684 75.030 1.00 14.36 C ANISOU 1806 C LYS A 380 1643 1827 1983 -8 23 53 C ATOM 1807 O LYS A 380 33.042 45.969 74.049 1.00 14.36 O ANISOU 1807 O LYS A 380 1516 1904 2033 108 3 128 O ATOM 1808 CB LYS A 380 30.777 47.547 75.367 1.00 14.49 C ANISOU 1808 CB LYS A 380 1806 1835 1863 -29 16 83 C ATOM 1809 CG LYS A 380 29.797 48.719 75.431 1.00 16.66 C ANISOU 1809 CG LYS A 380 1852 2112 2363 97 134 192 C ATOM 1810 CD LYS A 380 30.170 49.714 76.501 1.00 19.70 C ANISOU 1810 CD LYS A 380 2264 2559 2662 61 121 21 C ATOM 1811 CE LYS A 380 29.076 50.792 76.828 1.00 24.17 C ANISOU 1811 CE LYS A 380 2866 3031 3286 200 120 82 C ATOM 1812 NZ LYS A 380 28.514 51.298 75.563 1.00 28.75 N ANISOU 1812 NZ LYS A 380 3436 3817 3668 166 -16 184 N ATOM 1813 N ARG A 381 33.751 46.403 76.131 1.00 16.24 N ANISOU 1813 N ARG A 381 1887 2065 2218 -33 -38 121 N ATOM 1814 CA ARG A 381 34.583 45.218 76.176 1.00 18.64 C ANISOU 1814 CA ARG A 381 2273 2338 2471 71 36 52 C ATOM 1815 C ARG A 381 33.774 43.940 76.222 1.00 17.97 C ANISOU 1815 C ARG A 381 2212 2296 2318 38 44 13 C ATOM 1816 O ARG A 381 34.189 42.958 75.623 1.00 21.02 O ANISOU 1816 O ARG A 381 2453 2612 2920 234 138 195 O ATOM 1817 CB ARG A 381 35.522 45.261 77.364 1.00 20.68 C ANISOU 1817 CB ARG A 381 2573 2626 2659 11 11 89 C ATOM 1818 CG AARG A 381 36.820 44.422 77.138 0.50 23.01 C ANISOU 1818 CG AARG A 381 2853 2890 2999 87 40 39 C ATOM 1819 CG BARG A 381 36.602 44.165 77.299 0.50 22.53 C ANISOU 1819 CG BARG A 381 2835 2792 2931 106 -34 47 C ATOM 1820 CD AARG A 381 37.742 44.563 78.309 0.50 26.06 C ANISOU 1820 CD AARG A 381 3252 3345 3303 -22 -99 71 C ATOM 1821 CD BARG A 381 37.897 44.473 78.009 0.50 23.17 C ANISOU 1821 CD BARG A 381 2882 2989 2930 -29 -10 56 C ATOM 1822 NE AARG A 381 38.591 43.472 78.804 0.25 27.10 N ANISOU 1822 NE AARG A 381 3419 3394 3482 73 44 41 N ATOM 1823 NE BARG A 381 37.855 44.236 79.470 0.25 23.83 N ANISOU 1823 NE BARG A 381 3073 3025 2954 -22 31 45 N ATOM 1824 CZ AARG A 381 38.301 42.180 78.959 0.25 27.74 C ANISOU 1824 CZ AARG A 381 3548 3453 3536 2 12 -7 C ATOM 1825 CZ BARG A 381 37.564 45.137 80.410 0.25 23.27 C ANISOU 1825 CZ BARG A 381 2885 2958 2996 -21 41 50 C ATOM 1826 NH1AARG A 381 39.223 41.436 79.561 0.25 28.67 N ANISOU 1826 NH1AARG A 381 3628 3587 3677 20 -1 8 N ATOM 1827 NH1BARG A 381 37.239 46.372 80.094 0.25 23.51 N ANISOU 1827 NH1BARG A 381 2894 2963 3073 -9 14 32 N ATOM 1828 NH2AARG A 381 37.224 41.592 78.452 0.25 27.99 N ANISOU 1828 NH2AARG A 381 3597 3473 3564 57 20 -6 N ATOM 1829 NH2BARG A 381 37.591 44.798 81.696 0.25 23.57 N ANISOU 1829 NH2BARG A 381 3017 2999 2939 -19 0 -13 N ATOM 1830 N VAL A 382 32.608 43.935 76.898 1.00 16.98 N ANISOU 1830 N VAL A 382 1918 2228 2304 52 -2 162 N ATOM 1831 CA VAL A 382 31.781 42.715 76.964 1.00 17.59 C ANISOU 1831 CA VAL A 382 2099 2295 2289 70 -79 85 C ATOM 1832 C VAL A 382 30.429 42.989 76.363 1.00 16.74 C ANISOU 1832 C VAL A 382 1905 2193 2263 -32 -47 111 C ATOM 1833 O VAL A 382 30.109 44.134 76.189 1.00 16.92 O ANISOU 1833 O VAL A 382 1709 2326 2392 -113 24 320 O ATOM 1834 CB VAL A 382 31.565 42.214 78.416 1.00 18.76 C ANISOU 1834 CB VAL A 382 2315 2349 2463 -74 -85 157 C ATOM 1835 CG1 VAL A 382 32.906 41.994 79.076 1.00 20.64 C ANISOU 1835 CG1 VAL A 382 2579 2619 2645 19 -151 114 C ATOM 1836 CG2 VAL A 382 30.755 43.133 79.222 1.00 19.49 C ANISOU 1836 CG2 VAL A 382 2369 2650 2385 -138 -179 158 C ATOM 1837 N VAL A 383 29.671 41.935 76.093 1.00 16.12 N ANISOU 1837 N VAL A 383 1800 2143 2182 41 -108 167 N ATOM 1838 CA VAL A 383 28.321 42.033 75.558 1.00 15.97 C ANISOU 1838 CA VAL A 383 1879 2061 2126 43 -62 62 C ATOM 1839 C VAL A 383 27.352 41.895 76.750 1.00 16.27 C ANISOU 1839 C VAL A 383 1928 2125 2127 30 -14 89 C ATOM 1840 O VAL A 383 27.418 40.938 77.500 1.00 16.89 O ANISOU 1840 O VAL A 383 2008 2118 2289 154 81 110 O ATOM 1841 CB VAL A 383 28.052 40.951 74.521 1.00 16.73 C ANISOU 1841 CB VAL A 383 1929 2193 2233 47 -62 97 C ATOM 1842 CG1 VAL A 383 26.705 41.211 73.934 1.00 17.41 C ANISOU 1842 CG1 VAL A 383 2077 2285 2251 19 -216 -63 C ATOM 1843 CG2 VAL A 383 29.161 41.001 73.449 1.00 17.13 C ANISOU 1843 CG2 VAL A 383 2093 2203 2210 68 -73 15 C ATOM 1844 N SER A 384 26.444 42.848 76.889 1.00 14.86 N ANISOU 1844 N SER A 384 1824 1846 1974 43 -59 12 N ATOM 1845 CA SER A 384 25.418 42.859 77.963 1.00 15.42 C ANISOU 1845 CA SER A 384 1903 1987 1967 -43 -72 33 C ATOM 1846 C SER A 384 24.025 42.701 77.433 1.00 15.24 C ANISOU 1846 C SER A 384 1852 1952 1986 17 30 36 C ATOM 1847 O SER A 384 23.796 42.704 76.238 1.00 15.33 O ANISOU 1847 O SER A 384 1846 2199 1777 -72 118 29 O ATOM 1848 CB SER A 384 25.416 44.112 78.775 1.00 16.13 C ANISOU 1848 CB SER A 384 1920 2100 2106 -120 61 82 C ATOM 1849 OG ASER A 384 26.695 44.668 78.901 0.50 15.38 O ANISOU 1849 OG ASER A 384 1806 2071 1966 75 -154 76 O ATOM 1850 OG BSER A 384 25.504 45.298 78.027 0.50 17.94 O ANISOU 1850 OG BSER A 384 2264 2264 2289 -148 -118 130 O ATOM 1851 N MET A 385 23.079 42.575 78.345 1.00 14.99 N ANISOU 1851 N MET A 385 1936 2031 1725 -1 -2 -5 N ATOM 1852 CA MET A 385 21.721 42.371 77.945 1.00 14.77 C ANISOU 1852 CA MET A 385 1807 1965 1840 25 56 45 C ATOM 1853 C MET A 385 21.178 43.497 77.094 1.00 14.58 C ANISOU 1853 C MET A 385 1788 1909 1843 -38 80 85 C ATOM 1854 O MET A 385 20.388 43.229 76.204 1.00 14.98 O ANISOU 1854 O MET A 385 1699 2120 1873 -180 115 258 O ATOM 1855 CB MET A 385 20.814 42.113 79.133 1.00 14.18 C ANISOU 1855 CB MET A 385 1686 1926 1775 -27 54 69 C ATOM 1856 CG MET A 385 21.027 40.794 79.782 1.00 14.62 C ANISOU 1856 CG MET A 385 1716 1762 2074 15 130 -41 C ATOM 1857 SD MET A 385 20.568 39.388 78.779 1.00 16.28 S ANISOU 1857 SD MET A 385 2148 1809 2227 -77 49 -114 S ATOM 1858 CE MET A 385 18.861 39.220 79.218 1.00 17.08 C ANISOU 1858 CE MET A 385 2334 1929 2225 -68 47 -107 C ATOM 1859 N VAL A 386 21.587 44.738 77.343 1.00 15.18 N ANISOU 1859 N VAL A 386 1925 1994 1848 59 60 78 N ATOM 1860 CA VAL A 386 21.073 45.813 76.507 1.00 15.18 C ANISOU 1860 CA VAL A 386 1844 2014 1908 52 81 86 C ATOM 1861 C VAL A 386 21.497 45.684 75.045 1.00 14.89 C ANISOU 1861 C VAL A 386 1848 2009 1800 69 62 91 C ATOM 1862 O VAL A 386 20.717 46.013 74.151 1.00 15.31 O ANISOU 1862 O VAL A 386 1777 2076 1962 18 148 267 O ATOM 1863 CB VAL A 386 21.388 47.178 77.045 1.00 14.92 C ANISOU 1863 CB VAL A 386 1822 1950 1896 34 34 73 C ATOM 1864 CG1 VAL A 386 22.861 47.543 76.928 1.00 15.81 C ANISOU 1864 CG1 VAL A 386 1786 2180 2039 -78 138 -108 C ATOM 1865 CG2 VAL A 386 20.544 48.204 76.336 1.00 15.72 C ANISOU 1865 CG2 VAL A 386 1802 2054 2116 59 24 171 C ATOM 1866 N GLU A 387 22.680 45.139 74.778 1.00 14.73 N ANISOU 1866 N GLU A 387 1771 2016 1806 74 8 133 N ATOM 1867 CA GLU A 387 23.061 44.882 73.385 1.00 14.47 C ANISOU 1867 CA GLU A 387 1749 1924 1824 29 29 -7 C ATOM 1868 C GLU A 387 22.196 43.777 72.766 1.00 14.98 C ANISOU 1868 C GLU A 387 1833 1992 1864 19 113 -32 C ATOM 1869 O GLU A 387 21.859 43.838 71.600 1.00 15.79 O ANISOU 1869 O GLU A 387 2029 1936 2034 -69 106 -29 O ATOM 1870 CB GLU A 387 24.566 44.569 73.270 1.00 14.79 C ANISOU 1870 CB GLU A 387 1796 1959 1863 91 119 29 C ATOM 1871 CG GLU A 387 25.413 45.852 73.378 1.00 19.22 C ANISOU 1871 CG GLU A 387 2264 2537 2501 -154 4 3 C ATOM 1872 CD GLU A 387 25.837 46.232 74.776 1.00 20.56 C ANISOU 1872 CD GLU A 387 2417 2597 2797 131 -53 -26 C ATOM 1873 OE1 GLU A 387 25.907 45.377 75.677 1.00 25.30 O ANISOU 1873 OE1 GLU A 387 3282 3322 3007 136 57 175 O ATOM 1874 OE2 GLU A 387 26.075 47.421 74.990 1.00 23.58 O ANISOU 1874 OE2 GLU A 387 3051 2805 3103 -256 -276 -29 O ATOM 1875 N PHE A 388 21.835 42.779 73.557 1.00 15.94 N ANISOU 1875 N PHE A 388 2037 1982 2038 -42 -24 38 N ATOM 1876 CA PHE A 388 20.842 41.801 73.117 1.00 16.65 C ANISOU 1876 CA PHE A 388 2176 2068 2081 -64 -27 -2 C ATOM 1877 C PHE A 388 19.484 42.410 72.829 1.00 17.34 C ANISOU 1877 C PHE A 388 2192 2227 2166 -76 6 -41 C ATOM 1878 O PHE A 388 18.836 42.027 71.852 1.00 17.59 O ANISOU 1878 O PHE A 388 2083 2417 2183 -232 -58 33 O ATOM 1879 CB PHE A 388 20.757 40.584 74.054 1.00 16.66 C ANISOU 1879 CB PHE A 388 2128 2099 2101 -126 -25 53 C ATOM 1880 CG PHE A 388 21.789 39.552 73.779 1.00 17.07 C ANISOU 1880 CG PHE A 388 2222 2088 2176 -137 4 27 C ATOM 1881 CD1 PHE A 388 21.546 38.559 72.821 1.00 19.15 C ANISOU 1881 CD1 PHE A 388 2518 2433 2323 -76 121 -77 C ATOM 1882 CD2 PHE A 388 23.015 39.569 74.412 1.00 16.92 C ANISOU 1882 CD2 PHE A 388 2262 2096 2068 -288 20 32 C ATOM 1883 CE1 PHE A 388 22.470 37.607 72.535 1.00 17.17 C ANISOU 1883 CE1 PHE A 388 2214 2290 2017 -1 -74 -28 C ATOM 1884 CE2 PHE A 388 23.949 38.617 74.156 1.00 18.13 C ANISOU 1884 CE2 PHE A 388 2405 2313 2167 -164 -61 22 C ATOM 1885 CZ PHE A 388 23.722 37.629 73.183 1.00 17.36 C ANISOU 1885 CZ PHE A 388 2063 2352 2178 -39 126 -76 C ATOM 1886 N GLU A 389 19.039 43.370 73.645 1.00 16.94 N ANISOU 1886 N GLU A 389 2057 2250 2127 -10 9 21 N ATOM 1887 CA GLU A 389 17.759 44.022 73.416 1.00 18.00 C ANISOU 1887 CA GLU A 389 2174 2329 2337 -48 -19 32 C ATOM 1888 C GLU A 389 17.806 44.786 72.109 1.00 17.97 C ANISOU 1888 C GLU A 389 2145 2424 2257 -23 -41 49 C ATOM 1889 O GLU A 389 16.891 44.689 71.301 1.00 18.99 O ANISOU 1889 O GLU A 389 2162 2729 2324 -153 -52 260 O ATOM 1890 CB GLU A 389 17.447 44.931 74.586 1.00 19.50 C ANISOU 1890 CB GLU A 389 2374 2580 2454 -26 -17 36 C ATOM 1891 CG GLU A 389 16.097 45.573 74.502 1.00 21.16 C ANISOU 1891 CG GLU A 389 2518 2785 2737 29 -7 40 C ATOM 1892 CD GLU A 389 15.932 46.596 75.597 1.00 24.69 C ANISOU 1892 CD GLU A 389 3034 3291 3057 80 100 -62 C ATOM 1893 OE1 GLU A 389 16.335 46.291 76.743 1.00 26.47 O ANISOU 1893 OE1 GLU A 389 3561 3387 3110 346 51 -143 O ATOM 1894 OE2 GLU A 389 15.453 47.702 75.322 1.00 25.87 O ANISOU 1894 OE2 GLU A 389 3423 3286 3120 -113 -55 124 O ATOM 1895 N LYS A 390 18.882 45.517 71.870 1.00 17.78 N ANISOU 1895 N LYS A 390 2169 2354 2229 -23 -36 80 N ATOM 1896 CA LYS A 390 19.022 46.269 70.637 1.00 18.91 C ANISOU 1896 CA LYS A 390 2292 2501 2391 22 -6 66 C ATOM 1897 C LYS A 390 19.068 45.335 69.439 1.00 19.47 C ANISOU 1897 C LYS A 390 2349 2668 2380 -87 -45 85 C ATOM 1898 O LYS A 390 18.500 45.628 68.377 1.00 20.30 O ANISOU 1898 O LYS A 390 2039 3129 2542 -39 -67 219 O ATOM 1899 CB LYS A 390 20.280 47.140 70.697 1.00 19.21 C ANISOU 1899 CB LYS A 390 2400 2495 2404 -40 -36 86 C ATOM 1900 CG LYS A 390 20.212 48.291 71.696 1.00 21.49 C ANISOU 1900 CG LYS A 390 2694 2802 2668 120 -68 24 C ATOM 1901 CD LYS A 390 21.564 49.057 71.818 1.00 24.13 C ANISOU 1901 CD LYS A 390 3079 2980 3108 -95 7 68 C ATOM 1902 CE LYS A 390 21.519 50.256 72.766 0.75 24.43 C ANISOU 1902 CE LYS A 390 3077 3106 3099 39 11 72 C ATOM 1903 NZ LYS A 390 20.390 50.688 72.953 0.00 20.00 N ANISOU 1903 NZ LYS A 390 2533 2533 2533 0 0 0 N ATOM 1904 N ALA A 391 19.750 44.218 69.596 1.00 18.60 N ANISOU 1904 N ALA A 391 2211 2582 2274 14 -45 9 N ATOM 1905 CA ALA A 391 19.911 43.237 68.523 1.00 20.33 C ANISOU 1905 CA ALA A 391 2491 2791 2442 -80 7 -20 C ATOM 1906 C ALA A 391 18.584 42.582 68.197 1.00 21.97 C ANISOU 1906 C ALA A 391 2533 3176 2637 -110 3 -36 C ATOM 1907 O ALA A 391 18.239 42.423 67.024 1.00 23.54 O ANISOU 1907 O ALA A 391 2534 3752 2655 -232 108 10 O ATOM 1908 CB ALA A 391 20.921 42.199 68.891 1.00 20.48 C ANISOU 1908 CB ALA A 391 2632 2714 2433 -74 20 -50 C ATOM 1909 N LYS A 392 17.832 42.227 69.232 1.00 22.13 N ANISOU 1909 N LYS A 392 2615 3144 2648 -173 26 -20 N ATOM 1910 CA LYS A 392 16.551 41.534 69.031 1.00 23.87 C ANISOU 1910 CA LYS A 392 2836 3265 2966 -154 32 -31 C ATOM 1911 C LYS A 392 15.613 42.455 68.266 1.00 25.64 C ANISOU 1911 C LYS A 392 3032 3551 3157 -122 77 -7 C ATOM 1912 O LYS A 392 14.897 42.017 67.344 1.00 25.38 O ANISOU 1912 O LYS A 392 2702 3822 3120 -231 34 -11 O ATOM 1913 CB LYS A 392 15.964 41.103 70.397 1.00 23.69 C ANISOU 1913 CB LYS A 392 2858 3250 2891 -168 108 -52 C ATOM 1914 CG LYS A 392 14.614 40.393 70.315 0.50 24.15 C ANISOU 1914 CG LYS A 392 3008 3120 3046 -105 -62 -19 C ATOM 1915 CD LYS A 392 14.620 39.821 72.020 0.00 20.00 C ANISOU 1915 CD LYS A 392 2533 2533 2533 0 0 0 C ATOM 1916 CE LYS A 392 15.760 38.955 72.570 0.00 20.00 C ANISOU 1916 CE LYS A 392 2533 2533 2533 0 0 0 C ATOM 1917 NZ LYS A 392 15.244 38.051 73.597 0.00 20.00 N ANISOU 1917 NZ LYS A 392 2533 2533 2533 0 0 0 N ATOM 1918 N ASP A 393 15.667 43.736 68.579 1.00 27.38 N ANISOU 1918 N ASP A 393 3327 3643 3432 -87 47 11 N ATOM 1919 CA ASP A 393 14.792 44.726 67.975 1.00 29.97 C ANISOU 1919 CA ASP A 393 3593 4007 3786 -36 -15 57 C ATOM 1920 C ASP A 393 15.178 44.981 66.529 1.00 31.38 C ANISOU 1920 C ASP A 393 3813 4235 3873 -21 -33 56 C ATOM 1921 O ASP A 393 14.312 45.211 65.673 1.00 33.05 O ANISOU 1921 O ASP A 393 3791 4672 4094 -177 -144 113 O ATOM 1922 CB ASP A 393 14.866 46.059 68.723 1.00 29.96 C ANISOU 1922 CB ASP A 393 3604 3943 3836 17 -23 39 C ATOM 1923 CG ASP A 393 14.123 46.042 70.086 1.00 32.28 C ANISOU 1923 CG ASP A 393 4124 4174 3965 -49 35 -48 C ATOM 1924 OD1 ASP A 393 14.228 47.044 70.807 1.00 33.63 O ANISOU 1924 OD1 ASP A 393 4247 4239 4291 124 110 -118 O ATOM 1925 OD2 ASP A 393 13.411 45.102 70.525 1.00 35.46 O ANISOU 1925 OD2 ASP A 393 4546 4528 4397 -153 264 -45 O ATOM 1926 N LYS A 394 16.476 45.022 66.258 1.00 31.77 N ANISOU 1926 N LYS A 394 3811 4300 3958 -16 -19 15 N ATOM 1927 CA LYS A 394 16.943 45.307 64.903 1.00 32.78 C ANISOU 1927 CA LYS A 394 4046 4318 4088 -14 -21 56 C ATOM 1928 C LYS A 394 16.452 44.197 64.013 1.00 33.57 C ANISOU 1928 C LYS A 394 4095 4472 4187 -30 0 23 C ATOM 1929 O LYS A 394 15.961 44.471 62.908 1.00 35.46 O ANISOU 1929 O LYS A 394 4379 4831 4260 -102 -75 104 O ATOM 1930 CB LYS A 394 18.467 45.392 64.835 0.75 32.23 C ANISOU 1930 CB LYS A 394 3992 4200 4051 -19 0 16 C ATOM 1931 CG LYS A 394 19.035 45.108 63.449 0.75 33.03 C ANISOU 1931 CG LYS A 394 4103 4321 4124 -20 -18 17 C ATOM 1932 CD LYS A 394 20.513 45.410 63.345 0.75 33.09 C ANISOU 1932 CD LYS A 394 4122 4290 4161 -17 11 44 C ATOM 1933 CE LYS A 394 20.972 45.245 61.904 0.50 32.91 C ANISOU 1933 CE LYS A 394 4169 4178 4155 33 10 41 C ATOM 1934 NZ LYS A 394 20.247 46.174 60.977 0.50 33.14 N ANISOU 1934 NZ LYS A 394 4110 4260 4221 -18 -60 48 N ATOM 1935 N ILE A 395 16.539 42.971 64.523 1.00 33.72 N ANISOU 1935 N ILE A 395 4064 4519 4229 1 -41 36 N ATOM 1936 CA ILE A 395 16.190 41.759 63.812 1.00 34.47 C ANISOU 1936 CA ILE A 395 4240 4539 4318 -18 15 4 C ATOM 1937 C ILE A 395 14.668 41.734 63.569 1.00 35.84 C ANISOU 1937 C ILE A 395 4383 4735 4500 -29 -31 -24 C ATOM 1938 O ILE A 395 14.209 41.343 62.496 1.00 37.26 O ANISOU 1938 O ILE A 395 4625 4961 4570 -150 -10 -68 O ATOM 1939 CB ILE A 395 16.641 40.520 64.588 1.00 33.80 C ANISOU 1939 CB ILE A 395 4119 4509 4213 -9 49 -23 C ATOM 1940 CG1 ILE A 395 18.180 40.376 64.524 1.00 32.53 C ANISOU 1940 CG1 ILE A 395 4032 4271 4055 5 -5 -65 C ATOM 1941 CG2 ILE A 395 15.988 39.286 64.043 1.00 35.22 C ANISOU 1941 CG2 ILE A 395 4460 4635 4287 -76 56 -20 C ATOM 1942 CD1 ILE A 395 18.733 39.103 65.154 1.00 33.23 C ANISOU 1942 CD1 ILE A 395 4244 4324 4057 -76 1 12 C ATOM 1943 N MET A 396 13.903 42.160 64.558 1.00 36.89 N ANISOU 1943 N MET A 396 4604 4802 4610 -24 -8 -26 N ATOM 1944 CA MET A 396 12.464 42.354 64.407 1.00 37.93 C ANISOU 1944 CA MET A 396 4729 4872 4809 15 -3 18 C ATOM 1945 C MET A 396 12.194 43.694 63.716 1.00 38.40 C ANISOU 1945 C MET A 396 4849 4898 4843 1 14 29 C ATOM 1946 O MET A 396 11.545 44.572 64.279 1.00 40.36 O ANISOU 1946 O MET A 396 5117 5093 5124 -17 13 62 O ATOM 1947 CB MET A 396 11.798 42.419 65.779 1.00 38.73 C ANISOU 1947 CB MET A 396 4799 5002 4913 3 13 34 C ATOM 1948 CG MET A 396 12.149 41.339 66.748 1.00 40.11 C ANISOU 1948 CG MET A 396 4963 5203 5073 45 1 103 C ATOM 1949 SD MET A 396 11.876 39.740 66.078 1.00 45.25 S ANISOU 1949 SD MET A 396 5726 5567 5898 -104 -101 198 S ATOM 1950 CE MET A 396 11.143 39.066 67.420 1.00 42.18 C ANISOU 1950 CE MET A 396 5266 5421 5338 43 -16 -43 C ATOM 1951 N MET A 397 12.702 43.883 62.513 0.50 38.21 N ANISOU 1951 N MET A 397 4841 4841 4835 6 8 37 N ATOM 1952 CA MET A 397 12.440 45.115 61.781 0.50 37.69 C ANISOU 1952 CA MET A 397 4772 4778 4769 0 3 12 C ATOM 1953 C MET A 397 12.790 44.750 60.366 0.50 37.62 C ANISOU 1953 C MET A 397 4759 4770 4764 -4 3 17 C ATOM 1954 O MET A 397 12.449 45.446 59.409 0.50 37.73 O ANISOU 1954 O MET A 397 4758 4786 4790 -30 10 33 O ATOM 1955 CB MET A 397 13.292 46.270 62.308 0.50 37.49 C ANISOU 1955 CB MET A 397 4747 4760 4735 1 2 24 C ATOM 1956 CG MET A 397 12.694 47.625 62.042 0.50 36.88 C ANISOU 1956 CG MET A 397 4671 4692 4649 -4 26 -16 C ATOM 1957 SD MET A 397 13.502 48.881 62.791 0.00 20.00 S ANISOU 1957 SD MET A 397 2533 2533 2533 0 0 0 S ATOM 1958 CE MET A 397 12.522 50.208 62.080 0.00 20.00 C ANISOU 1958 CE MET A 397 2533 2533 2533 0 0 0 C ATOM 1959 N GLY A 398 13.497 43.629 60.276 0.50 37.48 N ANISOU 1959 N GLY A 398 4743 4747 4748 4 11 9 N ATOM 1960 CA GLY A 398 13.547 42.833 59.073 0.50 37.33 C ANISOU 1960 CA GLY A 398 4730 4728 4726 -4 -1 0 C ATOM 1961 C GLY A 398 12.352 41.902 59.108 0.50 37.32 C ANISOU 1961 C GLY A 398 4744 4722 4711 -1 -7 13 C ATOM 1962 O GLY A 398 12.450 40.735 59.485 0.50 37.29 O ANISOU 1962 O GLY A 398 4767 4717 4681 -7 1 -9 O ATOM 1963 N LEU A 399 11.210 42.450 58.717 0.50 37.52 N ANISOU 1963 N LEU A 399 4734 4763 4756 -12 16 0 N ATOM 1964 CA LEU A 399 9.957 41.712 58.639 0.50 37.58 C ANISOU 1964 CA LEU A 399 4780 4752 4746 -29 9 3 C ATOM 1965 C LEU A 399 8.842 42.694 58.322 0.50 37.69 C ANISOU 1965 C LEU A 399 4784 4785 4751 -28 7 0 C ATOM 1966 O LEU A 399 8.845 43.837 58.797 0.50 37.86 O ANISOU 1966 O LEU A 399 4837 4793 4755 -72 5 -2 O ATOM 1967 CB LEU A 399 9.586 41.035 59.873 0.00 20.00 C ANISOU 1967 CB LEU A 399 2533 2533 2533 0 0 0 C ATOM 1968 CG LEU A 399 8.232 40.335 59.861 0.00 20.00 C ANISOU 1968 CG LEU A 399 2533 2533 2533 0 0 0 C ATOM 1969 CD1 LEU A 399 7.937 39.601 61.171 0.00 20.00 C ANISOU 1969 CD1 LEU A 399 2533 2533 2533 0 0 0 C ATOM 1970 CD2 LEU A 399 7.078 41.316 59.651 0.00 20.00 C ANISOU 1970 CD2 LEU A 399 2533 2533 2533 0 0 0 C TER 1971 LEU A 399 END