ATOM 1 N GLY A 1 27.186 -17.999 14.999 1.00 25.29 N ANISOU 1 N GLY A 1 2384 3402 3822 60 -115 386 N ATOM 2 CA GLY A 1 25.801 -18.501 14.772 1.00 20.77 C ANISOU 2 CA GLY A 1 1810 2918 3163 201 -162 226 C ATOM 3 C GLY A 1 24.758 -17.410 14.913 1.00 20.28 C ANISOU 3 C GLY A 1 2150 2630 2925 88 -50 240 C ATOM 4 O GLY A 1 25.068 -16.223 14.832 1.00 22.53 O ANISOU 4 O GLY A 1 2233 2880 3447 -86 156 374 O ATOM 5 N LEU A 2 23.513 -17.819 15.123 1.00 16.80 N ANISOU 5 N LEU A 2 1837 2420 2124 95 -208 214 N ATOM 6 CA LEU A 2 22.422 -16.872 15.325 1.00 13.86 C ANISOU 6 CA LEU A 2 1608 1925 1729 -109 -229 246 C ATOM 7 C LEU A 2 22.144 -16.719 16.807 1.00 14.32 C ANISOU 7 C LEU A 2 1718 1940 1780 -210 -184 193 C ATOM 8 O LEU A 2 22.281 -17.672 17.578 1.00 15.36 O ANISOU 8 O LEU A 2 2344 1916 1576 -17 -322 349 O ATOM 9 CB LEU A 2 21.154 -17.369 14.638 1.00 13.40 C ANISOU 9 CB LEU A 2 1628 2135 1329 -235 -253 151 C ATOM 10 CG LEU A 2 21.061 -17.164 13.128 1.00 12.48 C ANISOU 10 CG LEU A 2 1621 1874 1245 -107 -158 133 C ATOM 11 CD1 LEU A 2 22.030 -18.075 12.385 1.00 15.24 C ANISOU 11 CD1 LEU A 2 1988 1980 1821 -70 176 245 C ATOM 12 CD2 LEU A 2 19.634 -17.423 12.673 1.00 12.75 C ANISOU 12 CD2 LEU A 2 1654 1735 1453 -250 -264 132 C ATOM 13 N SER A 3 21.755 -15.515 17.205 1.00 14.49 N ANISOU 13 N SER A 3 1503 1944 2056 -154 -377 77 N ATOM 14 CA SER A 3 21.337 -15.274 18.575 1.00 15.01 C ANISOU 14 CA SER A 3 1828 1892 1982 -20 -308 92 C ATOM 15 C SER A 3 19.959 -15.891 18.791 1.00 14.55 C ANISOU 15 C SER A 3 1660 2126 1742 -74 -304 83 C ATOM 16 O SER A 3 19.257 -16.234 17.837 1.00 13.72 O ANISOU 16 O SER A 3 1570 1946 1695 -125 -288 -3 O ATOM 17 CB SER A 3 21.259 -13.772 18.833 1.00 14.89 C ANISOU 17 CB SER A 3 1859 1809 1986 -13 -401 50 C ATOM 18 OG SER A 3 20.203 -13.206 18.074 1.00 14.79 O ANISOU 18 OG SER A 3 1760 1974 1882 -143 -324 147 O ATOM 19 N ASP A 4 19.561 -16.022 20.050 1.00 16.10 N ANISOU 19 N ASP A 4 2038 2314 1764 -199 -93 364 N ATOM 20 CA ASP A 4 18.225 -16.508 20.347 1.00 15.74 C ANISOU 20 CA ASP A 4 2027 2220 1732 -14 -80 381 C ATOM 21 C ASP A 4 17.172 -15.596 19.708 1.00 15.42 C ANISOU 21 C ASP A 4 2032 2046 1779 -82 -104 161 C ATOM 22 O ASP A 4 16.182 -16.075 19.157 1.00 14.74 O ANISOU 22 O ASP A 4 1774 2207 1619 -68 -59 14 O ATOM 23 CB ASP A 4 18.021 -16.641 21.859 1.00 18.78 C ANISOU 23 CB ASP A 4 2406 2647 2082 198 165 448 C ATOM 24 CG ASP A 4 18.926 -17.703 22.482 1.00 20.75 C ANISOU 24 CG ASP A 4 2839 2762 2282 215 -121 74 C ATOM 25 OD1 ASP A 4 19.080 -18.789 21.881 1.00 24.27 O ANISOU 25 OD1 ASP A 4 3069 3041 3110 496 63 180 O ATOM 26 OD2 ASP A 4 19.477 -17.459 23.575 1.00 25.43 O ANISOU 26 OD2 ASP A 4 3327 3217 3117 161 -90 106 O ATOM 27 N GLY A 5 17.401 -14.286 19.751 1.00 15.01 N ANISOU 27 N GLY A 5 2045 2208 1448 46 -44 134 N ATOM 28 CA GLY A 5 16.477 -13.338 19.133 1.00 14.19 C ANISOU 28 CA GLY A 5 1933 1932 1527 74 -78 -42 C ATOM 29 C GLY A 5 16.359 -13.559 17.634 1.00 13.15 C ANISOU 29 C GLY A 5 1618 1888 1488 -162 66 -4 C ATOM 30 O GLY A 5 15.270 -13.509 17.061 1.00 13.19 O ANISOU 30 O GLY A 5 1438 1893 1677 -45 36 -67 O ATOM 31 N GLU A 6 17.491 -13.804 16.990 1.00 12.74 N ANISOU 31 N GLU A 6 1682 1788 1368 -64 47 -65 N ATOM 32 CA GLU A 6 17.489 -14.064 15.564 1.00 11.70 C ANISOU 32 CA GLU A 6 1273 1560 1611 -60 14 -110 C ATOM 33 C GLU A 6 16.745 -15.356 15.220 1.00 10.81 C ANISOU 33 C GLU A 6 1029 1567 1509 132 16 -34 C ATOM 34 O GLU A 6 15.949 -15.384 14.285 1.00 11.64 O ANISOU 34 O GLU A 6 1206 1710 1505 89 -154 -15 O ATOM 35 CB GLU A 6 18.915 -14.048 15.016 1.00 11.84 C ANISOU 35 CB GLU A 6 1113 1526 1859 -27 -50 -67 C ATOM 36 CG GLU A 6 19.489 -12.640 14.967 1.00 13.37 C ANISOU 36 CG GLU A 6 1500 1594 1985 -261 -4 -323 C ATOM 37 CD GLU A 6 20.981 -12.593 14.712 1.00 11.81 C ANISOU 37 CD GLU A 6 1265 1527 1696 21 -44 -128 C ATOM 38 OE1 GLU A 6 21.685 -13.585 15.008 1.00 14.10 O ANISOU 38 OE1 GLU A 6 1493 1671 2190 0 44 -45 O ATOM 39 OE2 GLU A 6 21.457 -11.545 14.229 1.00 13.37 O ANISOU 39 OE2 GLU A 6 1436 1520 2123 81 134 -112 O ATOM 40 N TRP A 7 16.982 -16.423 15.978 1.00 11.99 N ANISOU 40 N TRP A 7 1393 1436 1726 35 -63 4 N ATOM 41 CA TRP A 7 16.235 -17.654 15.745 1.00 11.78 C ANISOU 41 CA TRP A 7 1260 1450 1765 3 -60 -22 C ATOM 42 C TRP A 7 14.736 -17.430 15.896 1.00 11.85 C ANISOU 42 C TRP A 7 1344 1501 1656 244 9 -100 C ATOM 43 O TRP A 7 13.947 -17.970 15.132 1.00 11.77 O ANISOU 43 O TRP A 7 1289 1583 1598 -147 -153 -65 O ATOM 44 CB TRP A 7 16.694 -18.786 16.667 1.00 11.68 C ANISOU 44 CB TRP A 7 1375 1345 1716 109 88 65 C ATOM 45 CG TRP A 7 17.962 -19.450 16.205 1.00 12.11 C ANISOU 45 CG TRP A 7 1307 1675 1617 92 26 15 C ATOM 46 CD1 TRP A 7 19.137 -19.533 16.894 1.00 11.71 C ANISOU 46 CD1 TRP A 7 1236 1535 1675 26 -13 -42 C ATOM 47 CD2 TRP A 7 18.180 -20.122 14.954 1.00 11.64 C ANISOU 47 CD2 TRP A 7 1371 1579 1472 -57 29 75 C ATOM 48 NE1 TRP A 7 20.075 -20.212 16.152 1.00 11.70 N ANISOU 48 NE1 TRP A 7 1259 1603 1583 -49 152 13 N ATOM 49 CE2 TRP A 7 19.513 -20.586 14.958 1.00 11.56 C ANISOU 49 CE2 TRP A 7 1321 1566 1504 62 124 71 C ATOM 50 CE3 TRP A 7 17.377 -20.383 13.836 1.00 11.54 C ANISOU 50 CE3 TRP A 7 1429 1580 1375 23 215 110 C ATOM 51 CZ2 TRP A 7 20.066 -21.278 13.888 1.00 11.80 C ANISOU 51 CZ2 TRP A 7 1458 1362 1661 -66 362 269 C ATOM 52 CZ3 TRP A 7 17.932 -21.081 12.767 1.00 12.17 C ANISOU 52 CZ3 TRP A 7 1552 1501 1570 -115 206 234 C ATOM 53 CH2 TRP A 7 19.264 -21.520 12.805 1.00 11.71 C ANISOU 53 CH2 TRP A 7 1491 1363 1594 -157 234 162 C ATOM 54 N GLN A 8 14.338 -16.631 16.878 1.00 12.21 N ANISOU 54 N GLN A 8 1332 1585 1722 174 45 -40 N ATOM 55 CA GLN A 8 12.920 -16.360 17.063 1.00 12.71 C ANISOU 55 CA GLN A 8 1487 1672 1671 4 -160 -61 C ATOM 56 C GLN A 8 12.342 -15.669 15.831 1.00 11.42 C ANISOU 56 C GLN A 8 1259 1572 1509 68 -7 35 C ATOM 57 O GLN A 8 11.240 -15.995 15.385 1.00 11.28 O ANISOU 57 O GLN A 8 1189 1615 1479 -157 -62 139 O ATOM 58 CB GLN A 8 12.692 -15.519 18.317 1.00 12.42 C ANISOU 58 CB GLN A 8 1406 1556 1754 199 -22 -164 C ATOM 59 CG GLN A 8 11.233 -15.401 18.699 1.00 13.46 C ANISOU 59 CG GLN A 8 1519 1715 1880 -64 -2 -64 C ATOM 60 CD GLN A 8 11.034 -14.623 19.977 1.00 14.53 C ANISOU 60 CD GLN A 8 1964 1628 1929 -237 -137 -61 C ATOM 61 OE1 GLN A 8 11.721 -13.634 20.232 1.00 17.31 O ANISOU 61 OE1 GLN A 8 2305 1975 2295 -458 -8 77 O ATOM 62 NE2 GLN A 8 10.083 -15.061 20.790 1.00 15.59 N ANISOU 62 NE2 GLN A 8 2000 1761 2160 -151 86 280 N ATOM 63 N GLN A 9 13.095 -14.734 15.262 1.00 11.84 N ANISOU 63 N GLN A 9 1306 1683 1510 -8 -28 143 N ATOM 64 CA GLN A 9 12.659 -14.079 14.030 1.00 11.74 C ANISOU 64 CA GLN A 9 1413 1620 1427 -72 -6 10 C ATOM 65 C GLN A 9 12.544 -15.083 12.878 1.00 11.64 C ANISOU 65 C GLN A 9 1303 1619 1498 45 -1 101 C ATOM 66 O GLN A 9 11.573 -15.073 12.122 1.00 11.76 O ANISOU 66 O GLN A 9 1230 1715 1521 150 -38 73 O ATOM 67 CB GLN A 9 13.613 -12.942 13.652 1.00 14.09 C ANISOU 67 CB GLN A 9 1966 1775 1613 -262 369 -109 C ATOM 68 CG GLN A 9 13.518 -11.722 14.552 1.00 17.66 C ANISOU 68 CG GLN A 9 2503 2343 1862 -184 274 -238 C ATOM 69 CD GLN A 9 12.200 -10.989 14.392 1.00 22.95 C ANISOU 69 CD GLN A 9 3297 3091 2329 1 382 -130 C ATOM 70 OE1 GLN A 9 11.507 -10.715 15.373 1.00 26.63 O ANISOU 70 OE1 GLN A 9 3716 3615 2784 -33 496 -33 O ATOM 71 NE2 GLN A 9 11.840 -10.677 13.150 1.00 22.24 N ANISOU 71 NE2 GLN A 9 3163 3242 2043 -59 382 -133 N ATOM 72 N VAL A 10 13.543 -15.946 12.740 1.00 11.76 N ANISOU 72 N VAL A 10 1407 1403 1657 -22 -92 -189 N ATOM 73 CA VAL A 10 13.516 -16.953 11.684 1.00 11.42 C ANISOU 73 CA VAL A 10 1212 1489 1636 -62 -21 -120 C ATOM 74 C VAL A 10 12.251 -17.807 11.779 1.00 11.17 C ANISOU 74 C VAL A 10 1166 1541 1535 25 -138 9 C ATOM 75 O VAL A 10 11.565 -18.044 10.782 1.00 11.32 O ANISOU 75 O VAL A 10 1146 1686 1468 50 -44 13 O ATOM 76 CB VAL A 10 14.742 -17.880 11.767 1.00 11.16 C ANISOU 76 CB VAL A 10 1253 1314 1674 13 121 -7 C ATOM 77 CG1 VAL A 10 14.585 -19.066 10.817 1.00 12.20 C ANISOU 77 CG1 VAL A 10 1400 1418 1816 -83 34 65 C ATOM 78 CG2 VAL A 10 16.015 -17.106 11.458 1.00 12.34 C ANISOU 78 CG2 VAL A 10 1256 1508 1925 9 209 186 C ATOM 79 N LEU A 11 11.950 -18.287 12.980 1.00 11.61 N ANISOU 79 N LEU A 11 1178 1549 1684 -71 41 -128 N ATOM 80 CA LEU A 11 10.828 -19.199 13.136 1.00 11.67 C ANISOU 80 CA LEU A 11 1329 1378 1724 148 -139 125 C ATOM 81 C LEU A 11 9.484 -18.484 13.051 1.00 11.24 C ANISOU 81 C LEU A 11 1222 1327 1719 66 144 49 C ATOM 82 O LEU A 11 8.479 -19.088 12.677 1.00 12.73 O ANISOU 82 O LEU A 11 1192 1566 2076 -63 49 -31 O ATOM 83 CB LEU A 11 10.980 -20.040 14.405 1.00 12.14 C ANISOU 83 CB LEU A 11 1429 1558 1624 112 46 -4 C ATOM 84 CG LEU A 11 12.217 -20.950 14.353 1.00 13.06 C ANISOU 84 CG LEU A 11 1709 1688 1563 219 -18 29 C ATOM 85 CD1 LEU A 11 12.291 -21.834 15.590 1.00 14.16 C ANISOU 85 CD1 LEU A 11 2078 1716 1583 346 181 139 C ATOM 86 CD2 LEU A 11 12.203 -21.813 13.088 1.00 15.28 C ANISOU 86 CD2 LEU A 11 2237 1881 1688 355 14 36 C ATOM 87 N ASN A 12 9.474 -17.191 13.358 1.00 10.85 N ANISOU 87 N ASN A 12 1319 1298 1504 138 -62 68 N ATOM 88 CA ASN A 12 8.284 -16.384 13.144 1.00 11.79 C ANISOU 88 CA ASN A 12 1527 1437 1512 109 -46 -2 C ATOM 89 C ASN A 12 8.013 -16.217 11.650 1.00 11.93 C ANISOU 89 C ASN A 12 1270 1450 1813 75 -248 71 C ATOM 90 O ASN A 12 6.894 -16.421 11.184 1.00 13.27 O ANISOU 90 O ASN A 12 1304 1841 1897 153 -314 66 O ATOM 91 CB ASN A 12 8.436 -15.022 13.810 1.00 13.55 C ANISOU 91 CB ASN A 12 1694 1601 1851 307 -185 39 C ATOM 92 CG ASN A 12 7.139 -14.250 13.826 1.00 16.71 C ANISOU 92 CG ASN A 12 2037 2079 2234 291 119 92 C ATOM 93 OD1 ASN A 12 6.206 -14.601 14.548 1.00 21.35 O ANISOU 93 OD1 ASN A 12 2342 2809 2959 365 88 376 O ATOM 94 ND2 ASN A 12 7.067 -13.201 13.022 1.00 20.00 N ANISOU 94 ND2 ASN A 12 2792 2368 2436 371 2 299 N ATOM 95 N VAL A 13 9.046 -15.865 10.892 1.00 11.47 N ANISOU 95 N VAL A 13 1528 1507 1320 -13 -121 202 N ATOM 96 CA VAL A 13 8.915 -15.792 9.437 1.00 13.32 C ANISOU 96 CA VAL A 13 1628 1774 1658 -134 -292 167 C ATOM 97 C VAL A 13 8.443 -17.133 8.879 1.00 12.30 C ANISOU 97 C VAL A 13 1310 1938 1425 -93 -172 6 C ATOM 98 O VAL A 13 7.596 -17.192 7.985 1.00 13.55 O ANISOU 98 O VAL A 13 1498 2204 1444 -238 -182 59 O ATOM 99 CB VAL A 13 10.259 -15.417 8.779 1.00 14.39 C ANISOU 99 CB VAL A 13 1969 1999 1498 -343 -282 -25 C ATOM 100 CG1 VAL A 13 10.196 -15.596 7.267 1.00 15.78 C ANISOU 100 CG1 VAL A 13 2350 2235 1408 -197 -77 117 C ATOM 101 CG2 VAL A 13 10.652 -13.985 9.147 1.00 16.36 C ANISOU 101 CG2 VAL A 13 2347 2046 1822 -127 -251 -6 C ATOM 102 N TRP A 14 8.985 -18.219 9.414 1.00 12.65 N ANISOU 102 N TRP A 14 1489 1744 1574 -54 -67 117 N ATOM 103 CA TRP A 14 8.660 -19.535 8.887 1.00 12.62 C ANISOU 103 CA TRP A 14 1426 1912 1457 -135 -76 -54 C ATOM 104 C TRP A 14 7.176 -19.861 9.034 1.00 13.01 C ANISOU 104 C TRP A 14 1504 1811 1625 -56 16 -98 C ATOM 105 O TRP A 14 6.618 -20.632 8.249 1.00 12.13 O ANISOU 105 O TRP A 14 1436 1603 1567 -15 -322 -354 O ATOM 106 CB TRP A 14 9.524 -20.623 9.528 1.00 13.72 C ANISOU 106 CB TRP A 14 1655 1788 1768 66 -112 -74 C ATOM 107 CG TRP A 14 9.469 -21.896 8.757 1.00 13.45 C ANISOU 107 CG TRP A 14 1433 1880 1794 66 -244 -157 C ATOM 108 CD1 TRP A 14 8.837 -23.048 9.120 1.00 14.85 C ANISOU 108 CD1 TRP A 14 1765 1795 2081 245 -256 1 C ATOM 109 CD2 TRP A 14 10.038 -22.137 7.467 1.00 14.48 C ANISOU 109 CD2 TRP A 14 1696 1972 1833 315 -307 37 C ATOM 110 NE1 TRP A 14 8.985 -23.999 8.139 1.00 15.30 N ANISOU 110 NE1 TRP A 14 1679 2074 2061 225 -203 -62 N ATOM 111 CE2 TRP A 14 9.716 -23.465 7.110 1.00 13.14 C ANISOU 111 CE2 TRP A 14 1510 1814 1667 373 -144 31 C ATOM 112 CE3 TRP A 14 10.788 -21.362 6.577 1.00 14.20 C ANISOU 112 CE3 TRP A 14 1618 2127 1649 419 -262 -4 C ATOM 113 CZ2 TRP A 14 10.126 -24.035 5.904 1.00 14.55 C ANISOU 113 CZ2 TRP A 14 1724 2039 1764 310 -145 138 C ATOM 114 CZ3 TRP A 14 11.193 -21.929 5.376 1.00 15.22 C ANISOU 114 CZ3 TRP A 14 1790 1980 2010 452 -285 137 C ATOM 115 CH2 TRP A 14 10.856 -23.252 5.051 1.00 13.94 C ANISOU 115 CH2 TRP A 14 1643 1858 1794 362 -191 20 C ATOM 116 N GLY A 15 6.528 -19.273 10.036 1.00 12.45 N ANISOU 116 N GLY A 15 1528 1726 1474 -163 152 -248 N ATOM 117 CA GLY A 15 5.082 -19.432 10.187 1.00 13.88 C ANISOU 117 CA GLY A 15 1585 1731 1955 -143 67 -77 C ATOM 118 C GLY A 15 4.323 -19.009 8.940 1.00 12.98 C ANISOU 118 C GLY A 15 1657 1369 1903 -131 184 -24 C ATOM 119 O GLY A 15 3.270 -19.571 8.626 1.00 14.13 O ANISOU 119 O GLY A 15 1544 1680 2146 -229 110 -210 O ATOM 120 N LYS A 16 4.847 -18.015 8.225 1.00 13.15 N ANISOU 120 N LYS A 16 1576 1511 1907 38 208 -51 N ATOM 121 CA LYS A 16 4.223 -17.570 6.979 1.00 13.49 C ANISOU 121 CA LYS A 16 1707 1339 2076 -33 103 113 C ATOM 122 C LYS A 16 4.267 -18.691 5.954 1.00 12.84 C ANISOU 122 C LYS A 16 1431 1457 1988 58 -2 12 C ATOM 123 O LYS A 16 3.286 -18.968 5.257 1.00 13.00 O ANISOU 123 O LYS A 16 1459 1844 1636 242 126 61 O ATOM 124 CB LYS A 16 4.967 -16.358 6.414 1.00 14.30 C ANISOU 124 CB LYS A 16 1876 1236 2319 -376 234 82 C ATOM 125 CG LYS A 16 4.840 -15.095 7.234 1.00 18.26 C ANISOU 125 CG LYS A 16 2396 1661 2881 -293 334 16 C ATOM 126 CD LYS A 16 5.623 -13.958 6.584 1.00 18.53 C ANISOU 126 CD LYS A 16 2764 1308 2968 -484 14 119 C ATOM 127 CE LYS A 16 5.103 -12.590 7.008 1.00 21.85 C ANISOU 127 CE LYS A 16 3213 1894 3195 -530 78 70 C ATOM 128 NZ LYS A 16 5.066 -12.453 8.487 1.00 24.23 N ANISOU 128 NZ LYS A 16 3862 2165 3176 -570 -183 -417 N ATOM 129 N VAL A 17 5.427 -19.327 5.848 1.00 11.57 N ANISOU 129 N VAL A 17 1302 1283 1809 117 48 165 N ATOM 130 CA VAL A 17 5.594 -20.436 4.922 1.00 12.49 C ANISOU 130 CA VAL A 17 1451 1600 1692 149 -51 138 C ATOM 131 C VAL A 17 4.664 -21.598 5.283 1.00 11.79 C ANISOU 131 C VAL A 17 1297 1646 1534 -16 -104 -44 C ATOM 132 O VAL A 17 4.018 -22.184 4.411 1.00 12.12 O ANISOU 132 O VAL A 17 1292 1784 1526 66 -57 -19 O ATOM 133 CB VAL A 17 7.065 -20.910 4.888 1.00 11.67 C ANISOU 133 CB VAL A 17 1053 1569 1809 105 67 137 C ATOM 134 CG1 VAL A 17 7.214 -22.110 3.963 1.00 13.39 C ANISOU 134 CG1 VAL A 17 1447 1694 1947 236 64 -90 C ATOM 135 CG2 VAL A 17 7.970 -19.756 4.451 1.00 13.56 C ANISOU 135 CG2 VAL A 17 1405 1733 2011 149 239 378 C ATOM 136 N GLU A 18 4.579 -21.916 6.573 1.00 11.48 N ANISOU 136 N GLU A 18 1258 1497 1605 -60 -186 152 N ATOM 137 CA GLU A 18 3.778 -23.048 7.032 1.00 13.08 C ANISOU 137 CA GLU A 18 1488 1820 1661 -38 -201 223 C ATOM 138 C GLU A 18 2.281 -22.915 6.771 1.00 12.41 C ANISOU 138 C GLU A 18 1411 1720 1583 -131 -188 3 C ATOM 139 O GLU A 18 1.567 -23.917 6.725 1.00 13.53 O ANISOU 139 O GLU A 18 1553 1563 2022 -109 -51 49 O ATOM 140 CB GLU A 18 4.038 -23.330 8.506 1.00 14.36 C ANISOU 140 CB GLU A 18 1632 2113 1709 -207 -87 237 C ATOM 141 CG GLU A 18 5.450 -23.806 8.759 1.00 15.51 C ANISOU 141 CG GLU A 18 1701 2208 1981 173 -195 230 C ATOM 142 CD GLU A 18 5.688 -24.235 10.189 1.00 19.53 C ANISOU 142 CD GLU A 18 2336 2893 2189 225 -74 39 C ATOM 143 OE1 GLU A 18 4.924 -23.807 11.080 1.00 23.83 O ANISOU 143 OE1 GLU A 18 3184 3526 2342 295 23 -23 O ATOM 144 OE2 GLU A 18 6.640 -25.004 10.420 1.00 20.54 O ANISOU 144 OE2 GLU A 18 2601 2952 2248 471 -173 345 O ATOM 145 N ALA A 19 1.799 -21.688 6.605 1.00 11.79 N ANISOU 145 N ALA A 19 1313 1718 1448 -13 49 -26 N ATOM 146 CA ALA A 19 0.383 -21.473 6.299 1.00 12.70 C ANISOU 146 CA ALA A 19 1543 1725 1553 116 -60 -65 C ATOM 147 C ALA A 19 0.049 -21.920 4.877 1.00 11.16 C ANISOU 147 C ALA A 19 1289 1599 1350 5 -37 20 C ATOM 148 O ALA A 19 -1.098 -22.219 4.568 1.00 13.19 O ANISOU 148 O ALA A 19 1145 2218 1648 -154 60 -154 O ATOM 149 CB ALA A 19 -0.008 -20.015 6.517 1.00 12.76 C ANISOU 149 CB ALA A 19 1495 1545 1807 57 -4 -18 C ATOM 150 N ASP A 20 1.055 -21.958 4.008 1.00 11.50 N ANISOU 150 N ASP A 20 1258 1626 1485 134 -25 120 N ATOM 151 CA ASP A 20 0.850 -22.391 2.628 1.00 11.52 C ANISOU 151 CA ASP A 20 1238 1740 1397 302 51 232 C ATOM 152 C ASP A 20 2.157 -22.969 2.097 1.00 10.90 C ANISOU 152 C ASP A 20 1088 1692 1361 90 -144 34 C ATOM 153 O ASP A 20 2.823 -22.358 1.267 1.00 11.22 O ANISOU 153 O ASP A 20 1210 1640 1413 -129 80 73 O ATOM 154 CB ASP A 20 0.414 -21.208 1.761 1.00 12.71 C ANISOU 154 CB ASP A 20 1383 1840 1605 378 -99 -17 C ATOM 155 CG ASP A 20 0.173 -21.600 0.313 1.00 13.88 C ANISOU 155 CG ASP A 20 1310 2189 1772 243 -71 259 C ATOM 156 OD1 ASP A 20 0.047 -22.811 0.035 1.00 14.42 O ANISOU 156 OD1 ASP A 20 1141 2399 1936 -210 -48 76 O ATOM 157 OD2 ASP A 20 0.121 -20.697 -0.547 1.00 16.84 O ANISOU 157 OD2 ASP A 20 1698 2626 2072 65 -95 445 O ATOM 158 N ILE A 21 2.526 -24.148 2.586 1.00 12.13 N ANISOU 158 N ILE A 21 1342 1637 1629 -46 13 10 N ATOM 159 C ILE A 21 3.920 -25.052 0.756 1.00 13.63 C ANISOU 159 C ILE A 21 1878 1416 1883 -78 142 148 C ATOM 160 O ILE A 21 4.946 -24.782 0.129 1.00 13.61 O ANISOU 160 O ILE A 21 1819 1391 1960 91 324 34 O ATOM 161 CA AILE A 21 3.810 -24.757 2.242 0.50 13.55 C ANISOU 161 CA AILE A 21 1618 1711 1817 85 74 -29 C ATOM 162 CB AILE A 21 4.047 -26.066 3.020 0.50 15.01 C ANISOU 162 CB AILE A 21 1656 2144 1902 187 171 -126 C ATOM 163 CG1AILE A 21 4.397 -25.765 4.479 0.50 16.38 C ANISOU 163 CG1AILE A 21 1683 2431 2109 108 154 -243 C ATOM 164 CG2AILE A 21 5.151 -26.885 2.358 0.50 16.00 C ANISOU 164 CG2AILE A 21 1691 2328 2060 206 64 -79 C ATOM 165 CD1AILE A 21 5.769 -25.168 4.661 0.50 18.78 C ANISOU 165 CD1AILE A 21 1847 2818 2470 48 90 -231 C ATOM 166 CA BILE A 21 3.813 -24.731 2.243 0.50 13.10 C ANISOU 166 CA BILE A 21 1609 1587 1778 101 69 58 C ATOM 167 CB BILE A 21 4.111 -25.981 3.091 0.50 13.89 C ANISOU 167 CB BILE A 21 1621 1861 1792 203 172 48 C ATOM 168 CG1BILE A 21 5.578 -26.383 2.957 0.50 15.79 C ANISOU 168 CG1BILE A 21 1781 2119 2099 271 147 73 C ATOM 169 CG2BILE A 21 3.165 -27.115 2.735 0.50 13.84 C ANISOU 169 CG2BILE A 21 1582 1759 1918 108 31 148 C ATOM 170 CD1BILE A 21 6.523 -25.432 3.636 0.50 18.06 C ANISOU 170 CD1BILE A 21 2303 2178 2377 458 292 -59 C ATOM 171 N ALA A 22 2.860 -25.622 0.191 1.00 14.63 N ANISOU 171 N ALA A 22 2101 1636 1822 -364 181 0 N ATOM 172 CA ALA A 22 2.857 -25.966 -1.226 1.00 15.05 C ANISOU 172 CA ALA A 22 2239 1650 1829 -478 116 0 C ATOM 173 C ALA A 22 2.982 -24.732 -2.124 1.00 13.92 C ANISOU 173 C ALA A 22 1986 1592 1710 -404 79 -23 C ATOM 174 O ALA A 22 3.703 -24.756 -3.117 1.00 14.41 O ANISOU 174 O ALA A 22 1950 1781 1742 -362 218 66 O ATOM 175 CB ALA A 22 1.620 -26.770 -1.575 1.00 17.22 C ANISOU 175 CB ALA A 22 2401 2038 2103 -704 -183 -224 C ATOM 176 N GLY A 23 2.281 -23.658 -1.775 1.00 13.76 N ANISOU 176 N GLY A 23 1776 1679 1773 -427 -115 -13 N ATOM 177 CA GLY A 23 2.321 -22.434 -2.568 1.00 13.35 C ANISOU 177 CA GLY A 23 1646 1612 1813 -254 -97 -141 C ATOM 178 C GLY A 23 3.680 -21.767 -2.495 1.00 11.76 C ANISOU 178 C GLY A 23 1331 1608 1530 -110 68 -133 C ATOM 179 O GLY A 23 4.245 -21.349 -3.512 1.00 12.37 O ANISOU 179 O GLY A 23 1463 1863 1371 31 -30 -77 O ATOM 180 N HIS A 24 4.226 -21.674 -1.289 1.00 11.09 N ANISOU 180 N HIS A 24 1413 1416 1383 -82 -234 10 N ATOM 181 CA HIS A 24 5.578 -21.158 -1.143 1.00 11.91 C ANISOU 181 CA HIS A 24 1166 1628 1731 -43 -126 -28 C ATOM 182 C HIS A 24 6.601 -22.036 -1.867 1.00 11.51 C ANISOU 182 C HIS A 24 1385 1543 1444 46 -139 185 C ATOM 183 O HIS A 24 7.496 -21.527 -2.541 1.00 11.93 O ANISOU 183 O HIS A 24 1276 1737 1518 -54 110 12 O ATOM 184 CB HIS A 24 5.954 -20.994 0.328 1.00 12.12 C ANISOU 184 CB HIS A 24 1472 1521 1611 46 -106 145 C ATOM 185 CG HIS A 24 5.315 -19.810 0.986 1.00 11.59 C ANISOU 185 CG HIS A 24 1387 1468 1545 -56 69 56 C ATOM 186 ND1 HIS A 24 4.021 -19.830 1.461 1.00 11.68 N ANISOU 186 ND1 HIS A 24 1321 1517 1598 -5 10 -31 N ATOM 187 CD2 HIS A 24 5.802 -18.580 1.276 1.00 11.54 C ANISOU 187 CD2 HIS A 24 1545 1589 1250 -44 -23 -27 C ATOM 188 CE1 HIS A 24 3.734 -18.659 1.999 1.00 12.55 C ANISOU 188 CE1 HIS A 24 1594 1491 1681 -78 43 11 C ATOM 189 NE2 HIS A 24 4.797 -17.882 1.902 1.00 12.92 N ANISOU 189 NE2 HIS A 24 1666 1482 1760 -251 5 68 N ATOM 190 N GLY A 25 6.463 -23.351 -1.739 1.00 11.46 N ANISOU 190 N GLY A 25 1347 1542 1465 130 -61 -13 N ATOM 191 CA GLY A 25 7.403 -24.276 -2.375 1.00 13.47 C ANISOU 191 CA GLY A 25 1761 1768 1586 295 -137 -12 C ATOM 192 C GLY A 25 7.375 -24.170 -3.884 1.00 12.28 C ANISOU 192 C GLY A 25 1492 1638 1533 42 -16 -61 C ATOM 193 O GLY A 25 8.415 -24.130 -4.543 1.00 13.16 O ANISOU 193 O GLY A 25 1588 1692 1718 167 89 4 O ATOM 194 N GLN A 26 6.170 -24.126 -4.436 1.00 13.60 N ANISOU 194 N GLN A 26 1540 1991 1637 -57 -37 -115 N ATOM 195 CA GLN A 26 6.002 -23.961 -5.868 1.00 14.31 C ANISOU 195 CA GLN A 26 1944 1738 1752 -163 -75 -147 C ATOM 196 C GLN A 26 6.678 -22.680 -6.346 1.00 12.49 C ANISOU 196 C GLN A 26 1579 1481 1684 -67 -63 -146 C ATOM 197 O GLN A 26 7.434 -22.693 -7.321 1.00 13.58 O ANISOU 197 O GLN A 26 1596 1868 1695 -96 209 -359 O ATOM 198 CB GLN A 26 4.513 -23.927 -6.215 1.00 16.39 C ANISOU 198 CB GLN A 26 2059 2070 2097 -70 -143 -117 C ATOM 199 CG GLN A 26 4.213 -23.711 -7.685 1.00 17.55 C ANISOU 199 CG GLN A 26 2246 2144 2276 95 -175 -256 C ATOM 200 CD GLN A 26 2.767 -23.322 -7.920 1.00 17.56 C ANISOU 200 CD GLN A 26 2248 1987 2435 652 -175 -519 C ATOM 201 OE1 GLN A 26 2.306 -22.285 -7.438 1.00 22.93 O ANISOU 201 OE1 GLN A 26 3073 2646 2990 741 -132 -426 O ATOM 202 NE2 GLN A 26 2.040 -24.153 -8.658 1.00 19.14 N ANISOU 202 NE2 GLN A 26 2271 2293 2708 981 -168 -567 N ATOM 203 N GLU A 27 6.414 -21.571 -5.661 1.00 12.60 N ANISOU 203 N GLU A 27 1341 1611 1833 -194 -18 -214 N ATOM 204 CA GLU A 27 6.956 -20.291 -6.107 1.00 14.09 C ANISOU 204 CA GLU A 27 1516 1827 2010 47 -50 -172 C ATOM 205 C GLU A 27 8.473 -20.254 -5.999 1.00 12.44 C ANISOU 205 C GLU A 27 1323 1730 1670 104 -104 -39 C ATOM 206 O GLU A 27 9.152 -19.675 -6.850 1.00 12.82 O ANISOU 206 O GLU A 27 1623 1632 1616 -25 -51 2 O ATOM 207 CB GLU A 27 6.316 -19.117 -5.362 1.00 14.32 C ANISOU 207 CB GLU A 27 1305 2054 2081 15 -55 -464 C ATOM 208 CG GLU A 27 4.864 -18.870 -5.751 1.00 16.22 C ANISOU 208 CG GLU A 27 1479 2279 2404 1 -6 -291 C ATOM 209 CD GLU A 27 4.347 -17.520 -5.281 1.00 16.73 C ANISOU 209 CD GLU A 27 1584 2332 2439 -76 -178 -343 C ATOM 210 OE1 GLU A 27 5.145 -16.558 -5.222 1.00 18.94 O ANISOU 210 OE1 GLU A 27 2484 2225 2486 151 -441 -209 O ATOM 211 OE2 GLU A 27 3.139 -17.423 -4.978 1.00 20.70 O ANISOU 211 OE2 GLU A 27 2029 2752 3085 -206 -123 -455 O ATOM 212 N VAL A 28 9.015 -20.892 -4.966 1.00 12.15 N ANISOU 212 N VAL A 28 1375 1591 1649 120 5 -39 N ATOM 213 CA VAL A 28 10.460 -20.941 -4.815 1.00 12.82 C ANISOU 213 CA VAL A 28 1292 1738 1841 60 0 -156 C ATOM 214 C VAL A 28 11.086 -21.698 -5.983 1.00 11.46 C ANISOU 214 C VAL A 28 1177 1713 1462 27 -76 -86 C ATOM 215 O VAL A 28 12.055 -21.236 -6.584 1.00 12.50 O ANISOU 215 O VAL A 28 1330 1743 1674 -76 61 108 O ATOM 216 CB VAL A 28 10.876 -21.571 -3.470 1.00 12.70 C ANISOU 216 CB VAL A 28 1470 1634 1722 53 -110 -16 C ATOM 217 CG1 VAL A 28 12.351 -21.956 -3.477 1.00 12.80 C ANISOU 217 CG1 VAL A 28 1236 1882 1745 213 -208 2 C ATOM 218 CG2 VAL A 28 10.585 -20.603 -2.321 1.00 13.55 C ANISOU 218 CG2 VAL A 28 1601 1991 1555 -49 27 68 C ATOM 219 N LEU A 29 10.531 -22.857 -6.322 1.00 11.88 N ANISOU 219 N LEU A 29 1276 1723 1513 6 -54 -201 N ATOM 220 CA LEU A 29 11.103 -23.642 -7.415 1.00 12.36 C ANISOU 220 CA LEU A 29 1482 1539 1675 51 -73 -58 C ATOM 221 C LEU A 29 10.927 -22.950 -8.766 1.00 11.72 C ANISOU 221 C LEU A 29 1293 1607 1550 92 -97 -1 C ATOM 222 O LEU A 29 11.816 -22.986 -9.609 1.00 13.30 O ANISOU 222 O LEU A 29 1401 2028 1623 0 211 29 O ATOM 223 CB LEU A 29 10.521 -25.050 -7.453 1.00 11.08 C ANISOU 223 CB LEU A 29 1267 1455 1488 189 -188 -143 C ATOM 224 CG LEU A 29 10.926 -25.938 -6.275 1.00 12.25 C ANISOU 224 CG LEU A 29 1177 1700 1777 74 -318 -24 C ATOM 225 CD1 LEU A 29 10.181 -27.259 -6.332 1.00 13.03 C ANISOU 225 CD1 LEU A 29 1441 1552 1955 -81 -570 155 C ATOM 226 CD2 LEU A 29 12.424 -26.183 -6.244 1.00 13.38 C ANISOU 226 CD2 LEU A 29 1260 1702 2119 30 -252 -233 C ATOM 227 N ILE A 30 9.787 -22.305 -8.981 1.00 12.62 N ANISOU 227 N ILE A 30 1387 1727 1679 47 -28 207 N ATOM 228 CA ILE A 30 9.576 -21.604 -10.240 1.00 12.96 C ANISOU 228 CA ILE A 30 1290 1802 1832 -5 -57 67 C ATOM 229 C ILE A 30 10.541 -20.430 -10.373 1.00 13.25 C ANISOU 229 C ILE A 30 1378 1803 1852 -15 -40 -117 C ATOM 230 O ILE A 30 11.099 -20.187 -11.449 1.00 13.21 O ANISOU 230 O ILE A 30 1482 1730 1806 -113 107 -26 O ATOM 231 CB ILE A 30 8.113 -21.158 -10.411 1.00 13.52 C ANISOU 231 CB ILE A 30 1441 1641 2052 134 -134 281 C ATOM 232 CG1 ILE A 30 7.236 -22.390 -10.633 1.00 14.27 C ANISOU 232 CG1 ILE A 30 1534 1744 2144 -173 -78 238 C ATOM 233 CG2 ILE A 30 7.987 -20.170 -11.572 1.00 14.29 C ANISOU 233 CG2 ILE A 30 1548 1762 2120 -190 -145 369 C ATOM 234 CD1 ILE A 30 5.748 -22.101 -10.705 1.00 15.50 C ANISOU 234 CD1 ILE A 30 1688 1969 2230 126 2 266 C ATOM 235 N ARG A 31 10.768 -19.720 -9.270 1.00 12.25 N ANISOU 235 N ARG A 31 1448 1548 1658 9 -27 -8 N ATOM 236 CA ARG A 31 11.742 -18.629 -9.267 1.00 12.97 C ANISOU 236 CA ARG A 31 1541 1785 1601 -69 -124 -30 C ATOM 237 C ARG A 31 13.125 -19.181 -9.626 1.00 13.02 C ANISOU 237 C ARG A 31 1549 1728 1670 64 -149 173 C ATOM 238 O ARG A 31 13.841 -18.625 -10.458 1.00 13.70 O ANISOU 238 O ARG A 31 1676 1717 1810 153 68 159 O ATOM 239 CB ARG A 31 11.751 -17.931 -7.903 1.00 14.57 C ANISOU 239 CB ARG A 31 1748 1856 1931 -116 -120 30 C ATOM 240 CG ARG A 31 12.796 -16.839 -7.733 1.00 14.92 C ANISOU 240 CG ARG A 31 1716 1754 2198 75 -193 -23 C ATOM 241 CD ARG A 31 12.502 -15.630 -8.599 1.00 15.48 C ANISOU 241 CD ARG A 31 1778 1828 2274 -91 -300 48 C ATOM 242 NE ARG A 31 13.481 -14.567 -8.383 1.00 16.64 N ANISOU 242 NE ARG A 31 1912 1928 2480 -33 30 -65 N ATOM 243 CZ ARG A 31 13.334 -13.319 -8.815 1.00 18.04 C ANISOU 243 CZ ARG A 31 2101 2034 2717 -52 -56 -127 C ATOM 244 NH1 ARG A 31 12.243 -12.972 -9.482 1.00 20.03 N ANISOU 244 NH1 ARG A 31 2464 2222 2923 181 10 -67 N ATOM 245 NH2 ARG A 31 14.278 -12.416 -8.581 1.00 19.34 N ANISOU 245 NH2 ARG A 31 2323 1923 3099 22 -135 -126 N ATOM 246 N LEU A 32 13.488 -20.298 -9.010 1.00 13.28 N ANISOU 246 N LEU A 32 1569 1703 1775 32 -175 28 N ATOM 247 CA LEU A 32 14.765 -20.948 -9.286 1.00 13.02 C ANISOU 247 CA LEU A 32 1512 1696 1737 97 -94 -17 C ATOM 248 C LEU A 32 14.908 -21.351 -10.762 1.00 12.32 C ANISOU 248 C LEU A 32 1404 1668 1606 -82 91 50 C ATOM 249 O LEU A 32 15.916 -21.046 -11.419 1.00 13.37 O ANISOU 249 O LEU A 32 1486 1933 1658 -18 97 -12 O ATOM 250 CB LEU A 32 14.879 -22.194 -8.410 1.00 13.24 C ANISOU 250 CB LEU A 32 1563 1579 1888 -21 -108 39 C ATOM 251 CG LEU A 32 16.146 -23.031 -8.540 1.00 12.84 C ANISOU 251 CG LEU A 32 1316 1571 1989 -122 20 -137 C ATOM 252 CD1 LEU A 32 17.352 -22.263 -7.997 1.00 13.32 C ANISOU 252 CD1 LEU A 32 1455 1512 2091 -358 -187 -123 C ATOM 253 CD2 LEU A 32 15.975 -24.354 -7.805 1.00 13.32 C ANISOU 253 CD2 LEU A 32 1552 1543 1966 -45 -181 0 C ATOM 254 N PHE A 33 13.903 -22.049 -11.281 1.00 12.72 N ANISOU 254 N PHE A 33 1531 1551 1750 184 -39 -203 N ATOM 255 CA PHE A 33 13.967 -22.602 -12.632 1.00 13.27 C ANISOU 255 CA PHE A 33 1644 1781 1616 45 -21 42 C ATOM 256 C PHE A 33 13.937 -21.520 -13.707 1.00 14.23 C ANISOU 256 C PHE A 33 1584 1982 1840 40 -2 74 C ATOM 257 O PHE A 33 14.613 -21.632 -14.725 1.00 15.75 O ANISOU 257 O PHE A 33 1949 2312 1720 32 88 118 O ATOM 258 CB PHE A 33 12.794 -23.553 -12.883 1.00 13.04 C ANISOU 258 CB PHE A 33 1390 1718 1846 -69 -126 -102 C ATOM 259 CG PHE A 33 12.823 -24.810 -12.059 1.00 12.56 C ANISOU 259 CG PHE A 33 1354 1761 1656 142 -122 35 C ATOM 260 CD1 PHE A 33 14.010 -25.319 -11.549 1.00 12.54 C ANISOU 260 CD1 PHE A 33 1361 1827 1577 117 -71 -2 C ATOM 261 CD2 PHE A 33 11.645 -25.510 -11.826 1.00 12.73 C ANISOU 261 CD2 PHE A 33 1195 1798 1841 115 -113 12 C ATOM 262 CE1 PHE A 33 14.012 -26.498 -10.809 1.00 13.00 C ANISOU 262 CE1 PHE A 33 1167 2072 1698 -62 -181 3 C ATOM 263 CE2 PHE A 33 11.644 -26.678 -11.087 1.00 13.30 C ANISOU 263 CE2 PHE A 33 1308 1902 1840 213 -169 78 C ATOM 264 CZ PHE A 33 12.828 -27.174 -10.576 1.00 13.13 C ANISOU 264 CZ PHE A 33 1197 2003 1789 219 -306 -60 C ATOM 265 N THR A 34 13.134 -20.485 -13.492 1.00 13.67 N ANISOU 265 N THR A 34 1762 1713 1717 112 -17 245 N ATOM 266 CA THR A 34 13.021 -19.415 -14.479 1.00 14.42 C ANISOU 266 CA THR A 34 1723 1898 1856 -98 -66 106 C ATOM 267 C THR A 34 14.232 -18.487 -14.458 1.00 13.10 C ANISOU 267 C THR A 34 1621 1724 1632 -201 -305 65 C ATOM 268 O THR A 34 14.694 -18.029 -15.501 1.00 13.93 O ANISOU 268 O THR A 34 1893 1995 1402 -292 -84 -103 O ATOM 269 CB THR A 34 11.705 -18.611 -14.323 1.00 14.15 C ANISOU 269 CB THR A 34 1626 1776 1973 -68 -66 5 C ATOM 270 OG1 THR A 34 11.655 -17.998 -13.029 1.00 15.54 O ANISOU 270 OG1 THR A 34 1802 2035 2066 -20 -34 64 O ATOM 271 CG2 THR A 34 10.500 -19.524 -14.493 1.00 15.19 C ANISOU 271 CG2 THR A 34 1759 1748 2265 -261 88 189 C ATOM 272 N GLY A 35 14.766 -18.232 -13.268 1.00 12.73 N ANISOU 272 N GLY A 35 1372 1811 1653 -186 -185 -5 N ATOM 273 CA GLY A 35 15.942 -17.386 -13.138 1.00 13.65 C ANISOU 273 CA GLY A 35 1537 1679 1970 24 -327 -197 C ATOM 274 C GLY A 35 17.215 -18.094 -13.560 1.00 13.70 C ANISOU 274 C GLY A 35 1553 1818 1831 24 -118 -84 C ATOM 275 O GLY A 35 18.159 -17.459 -14.026 1.00 12.12 O ANISOU 275 O GLY A 35 1582 1466 1557 128 -162 -105 O ATOM 276 N HIS A 36 17.227 -19.419 -13.414 1.00 12.82 N ANISOU 276 N HIS A 36 1547 1489 1834 9 -25 29 N ATOM 277 CA HIS A 36 18.430 -20.221 -13.649 1.00 12.12 C ANISOU 277 CA HIS A 36 1264 1587 1753 -57 -123 -13 C ATOM 278 C HIS A 36 18.065 -21.533 -14.345 1.00 12.99 C ANISOU 278 C HIS A 36 1458 1562 1913 -56 24 -55 C ATOM 279 O HIS A 36 18.028 -22.583 -13.709 1.00 13.73 O ANISOU 279 O HIS A 36 1689 1642 1884 83 67 179 O ATOM 280 CB HIS A 36 19.142 -20.498 -12.313 1.00 13.69 C ANISOU 280 CB HIS A 36 1657 1890 1653 -103 -89 -86 C ATOM 281 CG HIS A 36 19.328 -19.273 -11.475 1.00 13.76 C ANISOU 281 CG HIS A 36 1485 1922 1821 36 6 -50 C ATOM 282 ND1 HIS A 36 20.389 -18.410 -11.647 1.00 14.50 N ANISOU 282 ND1 HIS A 36 1577 2016 1917 -101 -125 -17 N ATOM 283 CD2 HIS A 36 18.565 -18.739 -10.490 1.00 14.79 C ANISOU 283 CD2 HIS A 36 1770 1922 1927 45 -1 -215 C ATOM 284 CE1 HIS A 36 20.286 -17.412 -10.787 1.00 15.49 C ANISOU 284 CE1 HIS A 36 1831 2174 1878 15 -62 -231 C ATOM 285 NE2 HIS A 36 19.188 -17.588 -10.073 1.00 15.52 N ANISOU 285 NE2 HIS A 36 1771 2171 1952 93 -110 -163 N ATOM 286 N PRO A 37 17.781 -21.475 -15.657 1.00 11.73 N ANISOU 286 N PRO A 37 1438 1386 1630 -264 -19 -63 N ATOM 287 CA PRO A 37 17.294 -22.657 -16.369 1.00 12.89 C ANISOU 287 CA PRO A 37 1606 1620 1671 -160 -8 -233 C ATOM 288 C PRO A 37 18.179 -23.883 -16.254 1.00 12.84 C ANISOU 288 C PRO A 37 1339 1749 1791 -101 -56 -58 C ATOM 289 O PRO A 37 17.680 -25.000 -16.397 1.00 13.90 O ANISOU 289 O PRO A 37 1565 1723 1992 -210 -97 -212 O ATOM 290 CB PRO A 37 17.197 -22.178 -17.819 1.00 13.29 C ANISOU 290 CB PRO A 37 1622 1710 1714 -97 -309 34 C ATOM 291 CG PRO A 37 16.972 -20.703 -17.692 1.00 12.62 C ANISOU 291 CG PRO A 37 1599 1453 1740 -416 12 -30 C ATOM 292 CD PRO A 37 17.845 -20.296 -16.540 1.00 12.70 C ANISOU 292 CD PRO A 37 1513 1646 1664 -23 55 -76 C ATOM 293 N GLU A 38 19.475 -23.695 -16.014 1.00 13.85 N ANISOU 293 N GLU A 38 1674 1646 1942 74 134 -74 N ATOM 294 CA GLU A 38 20.359 -24.845 -15.854 1.00 14.58 C ANISOU 294 CA GLU A 38 1619 1720 2198 112 130 133 C ATOM 295 C GLU A 38 19.925 -25.727 -14.684 1.00 14.67 C ANISOU 295 C GLU A 38 1744 1730 2098 242 180 100 C ATOM 296 O GLU A 38 20.173 -26.931 -14.682 1.00 15.00 O ANISOU 296 O GLU A 38 1787 1743 2169 82 231 41 O ATOM 297 CB GLU A 38 21.825 -24.419 -15.713 1.00 14.20 C ANISOU 297 CB GLU A 38 1582 1791 2023 304 -101 141 C ATOM 298 CG GLU A 38 22.178 -23.715 -14.416 1.00 13.95 C ANISOU 298 CG GLU A 38 1596 1665 2037 226 -137 24 C ATOM 299 CD GLU A 38 21.962 -22.219 -14.465 1.00 12.43 C ANISOU 299 CD GLU A 38 1408 1744 1571 64 -75 96 C ATOM 300 OE1 GLU A 38 21.047 -21.755 -15.183 1.00 13.72 O ANISOU 300 OE1 GLU A 38 1741 1731 1738 107 -111 -31 O ATOM 301 OE2 GLU A 38 22.704 -21.501 -13.767 1.00 12.62 O ANISOU 301 OE2 GLU A 38 1502 1835 1457 4 -38 -78 O ATOM 302 N THR A 39 19.248 -25.138 -13.702 1.00 14.33 N ANISOU 302 N THR A 39 1638 1919 1888 -107 104 135 N ATOM 303 CA THR A 39 18.839 -25.899 -12.530 1.00 15.14 C ANISOU 303 CA THR A 39 1641 2028 2082 20 116 101 C ATOM 304 C THR A 39 17.768 -26.926 -12.869 1.00 13.00 C ANISOU 304 C THR A 39 1359 1707 1871 193 60 201 C ATOM 305 O THR A 39 17.716 -27.997 -12.263 1.00 14.36 O ANISOU 305 O THR A 39 1761 1996 1697 13 -145 -145 O ATOM 306 CB THR A 39 18.361 -24.993 -11.373 1.00 13.22 C ANISOU 306 CB THR A 39 1461 1775 1787 79 -115 0 C ATOM 307 OG1 THR A 39 17.211 -24.236 -11.770 1.00 13.77 O ANISOU 307 OG1 THR A 39 1423 2073 1734 59 -67 207 O ATOM 308 CG2 THR A 39 19.469 -24.052 -10.938 1.00 14.89 C ANISOU 308 CG2 THR A 39 1818 1698 2138 -104 -28 122 C ATOM 309 N LEU A 40 16.909 -26.590 -13.832 1.00 14.78 N ANISOU 309 N LEU A 40 1523 1983 2108 -67 1 77 N ATOM 310 CA LEU A 40 15.858 -27.499 -14.264 1.00 15.47 C ANISOU 310 CA LEU A 40 1558 2246 2072 110 -179 126 C ATOM 311 C LEU A 40 16.461 -28.805 -14.772 1.00 12.39 C ANISOU 311 C LEU A 40 1173 1901 1633 -27 -89 3 C ATOM 312 O LEU A 40 15.871 -29.875 -14.624 1.00 15.15 O ANISOU 312 O LEU A 40 1569 2138 2049 -17 -74 -5 O ATOM 313 CB LEU A 40 15.020 -26.848 -15.363 1.00 16.40 C ANISOU 313 CB LEU A 40 1713 2505 2013 -270 -172 96 C ATOM 314 CG LEU A 40 13.727 -27.567 -15.740 1.00 16.13 C ANISOU 314 CG LEU A 40 1621 2502 2006 -271 32 33 C ATOM 315 CD1 LEU A 40 12.716 -27.441 -14.609 1.00 16.50 C ANISOU 315 CD1 LEU A 40 1954 2740 1574 -386 232 -287 C ATOM 316 CD2 LEU A 40 13.167 -26.985 -17.022 1.00 18.47 C ANISOU 316 CD2 LEU A 40 2041 2926 2052 14 -146 151 C ATOM 317 N GLU A 41 17.649 -28.717 -15.363 1.00 15.16 N ANISOU 317 N GLU A 41 1600 2281 1876 99 -138 -69 N ATOM 318 CA GLU A 41 18.277 -29.880 -15.984 1.00 15.73 C ANISOU 318 CA GLU A 41 1664 2414 1898 138 -68 -33 C ATOM 319 C GLU A 41 18.735 -30.920 -14.974 1.00 15.06 C ANISOU 319 C GLU A 41 1634 2203 1884 144 -22 -134 C ATOM 320 O GLU A 41 19.002 -32.067 -15.335 1.00 16.87 O ANISOU 320 O GLU A 41 1840 2774 1796 160 78 -384 O ATOM 321 CB GLU A 41 19.435 -29.459 -16.884 1.00 15.97 C ANISOU 321 CB GLU A 41 1744 2500 1824 63 -195 -43 C ATOM 322 CG GLU A 41 19.008 -28.557 -18.025 1.00 17.19 C ANISOU 322 CG GLU A 41 1962 2421 2147 -120 -443 113 C ATOM 323 CD GLU A 41 17.892 -29.159 -18.867 1.00 17.85 C ANISOU 323 CD GLU A 41 2064 2313 2405 59 -457 -45 C ATOM 324 OE1 GLU A 41 18.076 -30.277 -19.387 1.00 17.98 O ANISOU 324 OE1 GLU A 41 2092 2388 2348 -63 -145 -93 O ATOM 325 OE2 GLU A 41 16.830 -28.511 -19.009 1.00 20.61 O ANISOU 325 OE2 GLU A 41 2243 2761 2826 103 -295 -275 O ATOM 326 N LYS A 42 18.816 -30.521 -13.708 1.00 15.00 N ANISOU 326 N LYS A 42 1669 2343 1687 55 -181 82 N ATOM 327 CA LYS A 42 19.158 -31.461 -12.649 1.00 14.89 C ANISOU 327 CA LYS A 42 1741 2251 1665 -16 -201 84 C ATOM 328 C LYS A 42 17.970 -32.343 -12.295 1.00 14.40 C ANISOU 328 C LYS A 42 1604 2112 1752 188 27 208 C ATOM 329 O LYS A 42 18.121 -33.339 -11.590 1.00 14.83 O ANISOU 329 O LYS A 42 1707 2064 1861 61 -69 131 O ATOM 330 CB LYS A 42 19.667 -30.737 -11.401 1.00 14.95 C ANISOU 330 CB LYS A 42 1648 2258 1772 152 -167 -154 C ATOM 331 CG LYS A 42 21.019 -30.075 -11.581 1.00 15.97 C ANISOU 331 CG LYS A 42 1672 2413 1983 143 -165 41 C ATOM 332 CD LYS A 42 22.122 -31.105 -11.789 1.00 16.09 C ANISOU 332 CD LYS A 42 1608 2258 2247 174 -239 71 C ATOM 333 CE LYS A 42 23.456 -30.411 -11.998 1.00 16.70 C ANISOU 333 CE LYS A 42 1657 2260 2428 77 -162 403 C ATOM 334 NZ LYS A 42 24.592 -31.374 -12.031 1.00 16.93 N ANISOU 334 NZ LYS A 42 1682 2681 2067 116 34 144 N ATOM 335 N PHE A 43 16.795 -31.970 -12.802 1.00 14.54 N ANISOU 335 N PHE A 43 1433 2297 1793 130 -69 47 N ATOM 336 CA PHE A 43 15.556 -32.688 -12.517 1.00 15.95 C ANISOU 336 CA PHE A 43 1670 2335 2054 152 -51 58 C ATOM 337 C PHE A 43 15.066 -33.370 -13.784 1.00 16.67 C ANISOU 337 C PHE A 43 1946 2539 1845 64 -106 140 C ATOM 338 O PHE A 43 14.355 -32.766 -14.592 1.00 17.10 O ANISOU 338 O PHE A 43 1762 2957 1777 52 -51 54 O ATOM 339 CB PHE A 43 14.451 -31.723 -12.083 1.00 14.60 C ANISOU 339 CB PHE A 43 1484 2364 1698 178 -63 -2 C ATOM 340 CG PHE A 43 14.619 -31.160 -10.704 1.00 13.22 C ANISOU 340 CG PHE A 43 1470 1915 1636 37 -93 120 C ATOM 341 CD1 PHE A 43 15.283 -29.963 -10.507 1.00 14.11 C ANISOU 341 CD1 PHE A 43 1752 1852 1755 120 -299 323 C ATOM 342 CD2 PHE A 43 14.050 -31.792 -9.609 1.00 14.51 C ANISOU 342 CD2 PHE A 43 1700 2386 1428 140 119 47 C ATOM 343 CE1 PHE A 43 15.416 -29.429 -9.236 1.00 16.16 C ANISOU 343 CE1 PHE A 43 1855 2031 2254 337 -487 64 C ATOM 344 CE2 PHE A 43 14.177 -31.260 -8.336 1.00 15.18 C ANISOU 344 CE2 PHE A 43 1759 2158 1850 303 -134 20 C ATOM 345 CZ PHE A 43 14.852 -30.074 -8.155 1.00 14.62 C ANISOU 345 CZ PHE A 43 1712 2021 1819 371 -370 -66 C ATOM 346 N ASP A 44 15.422 -34.632 -13.959 1.00 19.35 N ANISOU 346 N ASP A 44 2093 2790 2468 210 -20 -137 N ATOM 347 CA ASP A 44 14.919 -35.376 -15.101 1.00 21.92 C ANISOU 347 CA ASP A 44 2486 3050 2791 15 -55 -84 C ATOM 348 C ASP A 44 13.394 -35.296 -15.151 1.00 20.98 C ANISOU 348 C ASP A 44 2234 3061 2675 -39 125 -157 C ATOM 349 O ASP A 44 12.801 -35.291 -16.229 1.00 21.97 O ANISOU 349 O ASP A 44 2335 3261 2752 -329 -105 -490 O ATOM 350 CB ASP A 44 15.384 -36.831 -15.043 1.00 25.36 C ANISOU 350 CB ASP A 44 2796 3371 3469 207 203 -50 C ATOM 351 CG ASP A 44 16.866 -36.975 -15.314 1.00 28.90 C ANISOU 351 CG ASP A 44 3313 3631 4035 345 278 146 C ATOM 352 OD1 ASP A 44 17.435 -36.083 -15.979 1.00 29.57 O ANISOU 352 OD1 ASP A 44 3446 3866 3922 501 616 187 O ATOM 353 OD2 ASP A 44 17.461 -37.977 -14.865 1.00 32.57 O ANISOU 353 OD2 ASP A 44 3739 3988 4647 345 276 226 O ATOM 354 N LYS A 45 12.760 -35.210 -13.985 1.00 19.35 N ANISOU 354 N LYS A 45 1854 2758 2738 -74 0 -20 N ATOM 355 CA LYS A 45 11.304 -35.206 -13.928 1.00 19.91 C ANISOU 355 CA LYS A 45 1947 2760 2858 17 -19 19 C ATOM 356 C LYS A 45 10.649 -33.836 -14.113 1.00 18.70 C ANISOU 356 C LYS A 45 1883 2611 2610 -81 -345 187 C ATOM 357 O LYS A 45 9.421 -33.723 -14.085 1.00 17.99 O ANISOU 357 O LYS A 45 1682 2793 2359 -225 -190 15 O ATOM 358 CB LYS A 45 10.807 -35.887 -12.655 1.00 19.09 C ANISOU 358 CB LYS A 45 2067 2749 2434 -71 47 -3 C ATOM 359 CG LYS A 45 10.909 -35.050 -11.393 1.00 18.71 C ANISOU 359 CG LYS A 45 1893 2873 2341 -139 -96 34 C ATOM 360 CD LYS A 45 10.300 -35.827 -10.243 1.00 20.67 C ANISOU 360 CD LYS A 45 2415 2977 2459 -94 159 78 C ATOM 361 CE LYS A 45 10.168 -34.997 -8.985 1.00 20.67 C ANISOU 361 CE LYS A 45 2537 2800 2516 61 93 89 C ATOM 362 NZ LYS A 45 9.297 -35.703 -8.004 1.00 22.34 N ANISOU 362 NZ LYS A 45 3114 2876 2495 35 290 181 N ATOM 363 N PHE A 46 11.460 -32.800 -14.302 1.00 16.15 N ANISOU 363 N PHE A 46 1696 2369 2071 -129 -199 103 N ATOM 364 CA PHE A 46 10.928 -31.475 -14.613 1.00 16.12 C ANISOU 364 CA PHE A 46 1772 2186 2165 -68 -96 122 C ATOM 365 C PHE A 46 11.427 -30.904 -15.936 1.00 16.08 C ANISOU 365 C PHE A 46 1850 2234 2023 -204 40 120 C ATOM 366 O PHE A 46 11.032 -29.806 -16.326 1.00 16.60 O ANISOU 366 O PHE A 46 2075 2085 2143 -4 -135 272 O ATOM 367 CB PHE A 46 11.171 -30.482 -13.472 1.00 16.79 C ANISOU 367 CB PHE A 46 1868 2232 2279 -44 -72 98 C ATOM 368 CG PHE A 46 10.456 -30.836 -12.202 1.00 16.28 C ANISOU 368 CG PHE A 46 1801 2237 2146 119 -68 -1 C ATOM 369 CD1 PHE A 46 9.121 -31.203 -12.219 1.00 16.06 C ANISOU 369 CD1 PHE A 46 1804 2260 2039 129 -60 -30 C ATOM 370 CD2 PHE A 46 11.118 -30.798 -10.988 1.00 15.59 C ANISOU 370 CD2 PHE A 46 1711 2197 2015 462 -163 28 C ATOM 371 CE1 PHE A 46 8.464 -31.532 -11.044 1.00 17.22 C ANISOU 371 CE1 PHE A 46 1984 2319 2240 285 -32 -10 C ATOM 372 CE2 PHE A 46 10.466 -31.124 -9.815 1.00 15.71 C ANISOU 372 CE2 PHE A 46 1891 2049 2029 448 95 -86 C ATOM 373 CZ PHE A 46 9.140 -31.494 -9.841 1.00 16.68 C ANISOU 373 CZ PHE A 46 1875 2276 2186 433 -10 -23 C ATOM 374 N LYS A 47 12.275 -31.654 -16.632 1.00 17.91 N ANISOU 374 N LYS A 47 2189 2368 2245 -245 449 125 N ATOM 375 CA LYS A 47 12.837 -31.204 -17.910 1.00 20.08 C ANISOU 375 CA LYS A 47 2495 2606 2526 -279 552 366 C ATOM 376 C LYS A 47 11.789 -30.919 -18.977 1.00 20.52 C ANISOU 376 C LYS A 47 2626 2811 2359 -425 503 283 C ATOM 377 O LYS A 47 12.030 -30.134 -19.898 1.00 22.94 O ANISOU 377 O LYS A 47 3075 2961 2680 -483 435 521 O ATOM 378 CB LYS A 47 13.830 -32.231 -18.458 1.00 22.23 C ANISOU 378 CB LYS A 47 2787 2848 2808 -152 467 353 C ATOM 379 CG LYS A 47 15.208 -32.152 -17.851 1.00 23.25 C ANISOU 379 CG LYS A 47 3036 2967 2829 -44 78 385 C ATOM 380 CD LYS A 47 16.132 -33.169 -18.499 1.00 22.44 C ANISOU 380 CD LYS A 47 2628 2903 2993 161 295 299 C ATOM 381 CE LYS A 47 17.502 -33.171 -17.849 1.00 24.34 C ANISOU 381 CE LYS A 47 3043 2987 3215 387 93 408 C ATOM 382 NZ LYS A 47 18.360 -34.271 -18.376 1.00 25.85 N ANISOU 382 NZ LYS A 47 3423 3116 3281 438 341 445 N ATOM 383 N HIS A 48 10.640 -31.575 -18.866 1.00 20.27 N ANISOU 383 N HIS A 48 2424 2950 2327 -488 465 167 N ATOM 384 CA HIS A 48 9.572 -31.436 -19.851 1.00 21.37 C ANISOU 384 CA HIS A 48 2725 3132 2260 -330 90 166 C ATOM 385 C HIS A 48 8.846 -30.109 -19.687 1.00 21.80 C ANISOU 385 C HIS A 48 2744 3281 2256 -349 -243 302 C ATOM 386 O HIS A 48 8.070 -29.707 -20.556 1.00 25.17 O ANISOU 386 O HIS A 48 3128 3903 2530 -386 -624 510 O ATOM 387 CB HIS A 48 8.562 -32.568 -19.690 1.00 21.25 C ANISOU 387 CB HIS A 48 2526 3086 2462 -229 -55 -58 C ATOM 388 CG HIS A 48 7.795 -32.499 -18.408 1.00 20.06 C ANISOU 388 CG HIS A 48 2187 3072 2362 -225 -185 -149 C ATOM 389 ND1 HIS A 48 8.304 -32.960 -17.212 1.00 20.55 N ANISOU 389 ND1 HIS A 48 2368 2995 2443 -161 -325 -44 N ATOM 390 CD2 HIS A 48 6.566 -32.003 -18.128 1.00 20.44 C ANISOU 390 CD2 HIS A 48 2107 2995 2662 -224 -333 -127 C ATOM 391 CE1 HIS A 48 7.417 -32.762 -16.254 1.00 19.42 C ANISOU 391 CE1 HIS A 48 2172 2885 2320 -326 -412 -141 C ATOM 392 NE2 HIS A 48 6.354 -32.182 -16.783 1.00 20.81 N ANISOU 392 NE2 HIS A 48 2325 2957 2623 -287 -490 -185 N ATOM 393 N LEU A 49 9.075 -29.441 -18.562 1.00 20.34 N ANISOU 393 N LEU A 49 2452 3053 2224 -562 26 311 N ATOM 394 CA LEU A 49 8.437 -28.160 -18.311 1.00 21.09 C ANISOU 394 CA LEU A 49 2543 2998 2470 -393 -98 569 C ATOM 395 C LEU A 49 9.103 -27.097 -19.165 1.00 22.74 C ANISOU 395 C LEU A 49 2639 3088 2914 -398 -17 538 C ATOM 396 O LEU A 49 10.180 -26.601 -18.841 1.00 23.90 O ANISOU 396 O LEU A 49 2476 3423 3181 -510 -325 1069 O ATOM 397 CB LEU A 49 8.501 -27.794 -16.829 1.00 19.28 C ANISOU 397 CB LEU A 49 2173 2829 2324 -482 0 525 C ATOM 398 CG LEU A 49 7.702 -28.723 -15.913 1.00 18.70 C ANISOU 398 CG LEU A 49 2012 2673 2420 -518 68 462 C ATOM 399 CD1 LEU A 49 7.914 -28.345 -14.463 1.00 18.52 C ANISOU 399 CD1 LEU A 49 2146 2797 2090 -342 279 316 C ATOM 400 CD2 LEU A 49 6.219 -28.695 -16.255 1.00 19.18 C ANISOU 400 CD2 LEU A 49 1908 2876 2502 -353 93 347 C ATOM 401 N LYS A 50 8.450 -26.757 -20.268 1.00 22.76 N ANISOU 401 N LYS A 50 2948 2960 2737 -27 106 546 N ATOM 402 CA LYS A 50 9.036 -25.861 -21.253 1.00 24.10 C ANISOU 402 CA LYS A 50 3348 2792 3015 -103 393 388 C ATOM 403 C LYS A 50 8.609 -24.409 -21.088 1.00 22.69 C ANISOU 403 C LYS A 50 3101 2640 2877 35 423 195 C ATOM 404 O LYS A 50 9.185 -23.519 -21.709 1.00 23.70 O ANISOU 404 O LYS A 50 3646 2372 2983 -42 520 295 O ATOM 405 CB LYS A 50 8.723 -26.344 -22.668 1.00 27.12 C ANISOU 405 CB LYS A 50 3692 3208 3401 -48 436 84 C ATOM 406 CG LYS A 50 9.623 -27.473 -23.148 1.00 29.50 C ANISOU 406 CG LYS A 50 3724 3423 4062 -12 512 -3 C ATOM 407 CD LYS A 50 11.064 -26.995 -23.290 1.00 31.43 C ANISOU 407 CD LYS A 50 3885 3634 4423 -111 515 -94 C ATOM 408 CE LYS A 50 11.933 -28.031 -23.986 1.00 32.72 C ANISOU 408 CE LYS A 50 3986 3757 4686 -93 429 -43 C ATOM 409 NZ LYS A 50 13.283 -27.489 -24.301 1.00 33.63 N ANISOU 409 NZ LYS A 50 4002 3920 4855 -107 305 -58 N ATOM 410 N THR A 51 7.600 -24.171 -20.258 1.00 19.11 N ANISOU 410 N THR A 51 2407 2340 2511 82 97 236 N ATOM 411 CA THR A 51 7.115 -22.817 -20.021 1.00 18.82 C ANISOU 411 CA THR A 51 2263 2440 2447 -121 -132 18 C ATOM 412 C THR A 51 6.775 -22.639 -18.553 1.00 19.48 C ANISOU 412 C THR A 51 2333 2418 2649 23 -56 133 C ATOM 413 O THR A 51 6.565 -23.618 -17.833 1.00 18.73 O ANISOU 413 O THR A 51 2234 2270 2609 -26 -162 210 O ATOM 414 CB THR A 51 5.838 -22.531 -20.830 1.00 17.67 C ANISOU 414 CB THR A 51 1717 2576 2418 -149 -132 83 C ATOM 415 OG1 THR A 51 4.776 -23.355 -20.332 1.00 18.38 O ANISOU 415 OG1 THR A 51 1944 2557 2480 -222 -213 87 O ATOM 416 CG2 THR A 51 6.057 -22.808 -22.319 1.00 18.51 C ANISOU 416 CG2 THR A 51 1920 2395 2716 -190 -219 94 C ATOM 417 N GLU A 52 6.706 -21.389 -18.108 1.00 17.97 N ANISOU 417 N GLU A 52 2198 2298 2330 -30 -102 42 N ATOM 418 CA GLU A 52 6.289 -21.123 -16.741 1.00 18.07 C ANISOU 418 CA GLU A 52 2333 2344 2187 -16 -163 4 C ATOM 419 C GLU A 52 4.848 -21.562 -16.487 1.00 18.27 C ANISOU 419 C GLU A 52 2230 2405 2305 46 -358 48 C ATOM 420 O GLU A 52 4.518 -22.011 -15.391 1.00 19.31 O ANISOU 420 O GLU A 52 2367 2610 2357 114 -185 117 O ATOM 421 CB GLU A 52 6.481 -19.655 -16.366 1.00 17.96 C ANISOU 421 CB GLU A 52 2390 2249 2184 18 -281 11 C ATOM 422 CG GLU A 52 6.108 -19.363 -14.922 1.00 18.38 C ANISOU 422 CG GLU A 52 2510 2212 2262 -20 -103 145 C ATOM 423 CD GLU A 52 6.472 -17.961 -14.494 1.00 18.13 C ANISOU 423 CD GLU A 52 2508 2229 2149 15 -234 33 C ATOM 424 OE1 GLU A 52 7.360 -17.356 -15.131 1.00 18.76 O ANISOU 424 OE1 GLU A 52 2431 2145 2551 -135 -286 167 O ATOM 425 OE2 GLU A 52 5.872 -17.470 -13.515 1.00 20.53 O ANISOU 425 OE2 GLU A 52 2773 2496 2531 -22 -235 -122 O ATOM 426 N ALA A 53 3.990 -21.442 -17.497 1.00 18.78 N ANISOU 426 N ALA A 53 2218 2666 2250 -124 -211 102 N ATOM 427 CA ALA A 53 2.618 -21.905 -17.353 1.00 18.13 C ANISOU 427 CA ALA A 53 2181 2366 2340 -137 -172 83 C ATOM 428 C ALA A 53 2.616 -23.395 -17.046 1.00 17.87 C ANISOU 428 C ALA A 53 2112 2478 2200 -67 -186 168 C ATOM 429 O ALA A 53 1.859 -23.865 -16.195 1.00 18.83 O ANISOU 429 O ALA A 53 2174 2466 2514 -338 -55 214 O ATOM 430 CB ALA A 53 1.818 -21.619 -18.617 1.00 17.68 C ANISOU 430 CB ALA A 53 2039 2333 2346 -200 -61 232 C ATOM 431 N GLU A 54 3.469 -24.140 -17.740 1.00 18.13 N ANISOU 431 N GLU A 54 2501 2397 1989 -33 -349 79 N ATOM 432 CA GLU A 54 3.558 -25.572 -17.511 1.00 18.32 C ANISOU 432 CA GLU A 54 2173 2495 2291 -107 -157 -56 C ATOM 433 C GLU A 54 4.065 -25.835 -16.098 1.00 17.66 C ANISOU 433 C GLU A 54 1875 2473 2360 -210 -309 -4 C ATOM 434 O GLU A 54 3.575 -26.730 -15.414 1.00 18.40 O ANISOU 434 O GLU A 54 2142 2509 2337 -376 -28 28 O ATOM 435 CB GLU A 54 4.438 -26.243 -18.570 1.00 18.87 C ANISOU 435 CB GLU A 54 2299 2620 2251 -88 -236 -266 C ATOM 436 CG GLU A 54 3.749 -26.360 -19.924 1.00 21.64 C ANISOU 436 CG GLU A 54 2744 3048 2430 45 -246 -390 C ATOM 437 CD GLU A 54 4.686 -26.771 -21.041 1.00 23.38 C ANISOU 437 CD GLU A 54 2819 3345 2716 252 -381 -290 C ATOM 438 OE1 GLU A 54 5.912 -26.815 -20.820 1.00 25.93 O ANISOU 438 OE1 GLU A 54 2949 3940 2961 462 -301 -241 O ATOM 439 OE2 GLU A 54 4.188 -27.043 -22.153 1.00 24.02 O ANISOU 439 OE2 GLU A 54 2931 3488 2707 360 -392 -592 O ATOM 440 N MET A 55 5.035 -25.041 -15.658 1.00 18.02 N ANISOU 440 N MET A 55 2083 2450 2312 -116 -80 68 N ATOM 441 CA MET A 55 5.530 -25.151 -14.289 1.00 17.77 C ANISOU 441 CA MET A 55 1921 2555 2274 -14 -107 135 C ATOM 442 C MET A 55 4.419 -24.901 -13.275 1.00 18.09 C ANISOU 442 C MET A 55 1984 2537 2350 -49 -30 102 C ATOM 443 O MET A 55 4.265 -25.656 -12.320 1.00 17.34 O ANISOU 443 O MET A 55 1923 2438 2225 120 -48 197 O ATOM 444 CB MET A 55 6.670 -24.166 -14.046 1.00 17.75 C ANISOU 444 CB MET A 55 1997 2391 2356 122 -36 43 C ATOM 445 CG MET A 55 7.905 -24.414 -14.880 1.00 17.70 C ANISOU 445 CG MET A 55 2138 2263 2324 -127 98 99 C ATOM 446 SD MET A 55 9.132 -23.143 -14.538 1.00 17.92 S ANISOU 446 SD MET A 55 2079 2292 2434 74 74 146 S ATOM 447 CE MET A 55 10.322 -23.473 -15.839 1.00 18.48 C ANISOU 447 CE MET A 55 2152 2629 2238 59 57 -28 C ATOM 448 N LYS A 56 3.650 -23.836 -13.487 1.00 17.36 N ANISOU 448 N LYS A 56 1949 2452 2193 47 -23 201 N ATOM 449 CA LYS A 56 2.561 -23.475 -12.577 1.00 18.19 C ANISOU 449 CA LYS A 56 2108 2468 2332 11 167 54 C ATOM 450 C LYS A 56 1.487 -24.557 -12.513 1.00 17.03 C ANISOU 450 C LYS A 56 1762 2356 2350 114 -14 6 C ATOM 451 O LYS A 56 0.875 -24.780 -11.462 1.00 17.72 O ANISOU 451 O LYS A 56 2030 2346 2353 -134 125 -87 O ATOM 452 CB LYS A 56 1.926 -22.151 -13.007 1.00 20.05 C ANISOU 452 CB LYS A 56 2282 2632 2702 -77 203 101 C ATOM 453 CG LYS A 56 2.845 -20.946 -12.916 1.00 22.65 C ANISOU 453 CG LYS A 56 2540 2831 3234 -148 -181 -39 C ATOM 454 CD LYS A 56 2.933 -20.402 -11.503 1.00 24.92 C ANISOU 454 CD LYS A 56 2940 2921 3604 -199 -232 -106 C ATOM 455 CE LYS A 56 3.836 -19.175 -11.453 1.00 26.19 C ANISOU 455 CE LYS A 56 3124 3040 3785 -235 -209 -32 C ATOM 456 NZ LYS A 56 3.993 -18.648 -10.067 1.00 29.29 N ANISOU 456 NZ LYS A 56 3678 3347 4104 -347 -5 -182 N ATOM 457 N ALA A 57 1.269 -25.228 -13.639 1.00 16.64 N ANISOU 457 N ALA A 57 1797 2415 2109 17 -37 14 N ATOM 458 CA ALA A 57 0.236 -26.253 -13.753 1.00 16.91 C ANISOU 458 CA ALA A 57 1983 2419 2020 92 20 12 C ATOM 459 C ALA A 57 0.702 -27.617 -13.257 1.00 15.76 C ANISOU 459 C ALA A 57 1601 2306 2080 96 48 -26 C ATOM 460 O ALA A 57 -0.092 -28.548 -13.150 1.00 15.97 O ANISOU 460 O ALA A 57 1734 2265 2067 277 186 -187 O ATOM 461 CB ALA A 57 -0.241 -26.353 -15.195 1.00 18.70 C ANISOU 461 CB ALA A 57 2352 2470 2280 58 -267 12 C ATOM 462 N SER A 58 1.989 -27.738 -12.949 1.00 14.76 N ANISOU 462 N SER A 58 1254 2561 1793 115 107 316 N ATOM 463 CA SER A 58 2.539 -29.023 -12.537 1.00 13.93 C ANISOU 463 CA SER A 58 1413 2319 1559 -66 124 111 C ATOM 464 C SER A 58 2.255 -29.344 -11.073 1.00 12.92 C ANISOU 464 C SER A 58 1282 2085 1541 -307 87 222 C ATOM 465 O SER A 58 2.806 -28.718 -10.162 1.00 14.64 O ANISOU 465 O SER A 58 1712 2427 1421 -461 -69 -65 O ATOM 466 CB SER A 58 4.046 -29.071 -12.788 1.00 13.77 C ANISOU 466 CB SER A 58 1463 2271 1498 82 119 -9 C ATOM 467 OG SER A 58 4.589 -30.276 -12.289 1.00 13.82 O ANISOU 467 OG SER A 58 1649 2046 1552 -49 -142 -159 O ATOM 468 N GLU A 59 1.419 -30.345 -10.841 1.00 15.20 N ANISOU 468 N GLU A 59 1476 2409 1890 -144 -259 348 N ATOM 469 CA GLU A 59 1.132 -30.745 -9.479 1.00 13.65 C ANISOU 469 CA GLU A 59 1447 2024 1714 49 -65 335 C ATOM 470 C GLU A 59 2.343 -31.422 -8.845 1.00 11.84 C ANISOU 470 C GLU A 59 1295 1830 1371 -92 -15 107 C ATOM 471 O GLU A 59 2.558 -31.327 -7.635 1.00 12.91 O ANISOU 471 O GLU A 59 1363 1989 1553 60 -168 -49 O ATOM 472 CB GLU A 59 -0.113 -31.630 -9.423 1.00 15.45 C ANISOU 472 CB GLU A 59 1480 2150 2237 -99 -210 565 C ATOM 473 CG GLU A 59 -1.378 -30.922 -9.907 1.00 18.38 C ANISOU 473 CG GLU A 59 1799 2322 2860 148 -271 777 C ATOM 474 CD GLU A 59 -1.707 -29.681 -9.088 1.00 17.66 C ANISOU 474 CD GLU A 59 1379 2376 2954 409 -200 769 C ATOM 475 OE1 GLU A 59 -1.391 -29.652 -7.885 1.00 20.05 O ANISOU 475 OE1 GLU A 59 2053 2194 3369 203 -91 944 O ATOM 476 OE2 GLU A 59 -2.300 -28.731 -9.645 1.00 22.54 O ANISOU 476 OE2 GLU A 59 2584 2344 3634 634 246 1010 O ATOM 477 N ASP A 60 3.163 -32.074 -9.662 1.00 12.60 N ANISOU 477 N ASP A 60 1223 1971 1592 70 -107 -16 N ATOM 478 CA ASP A 60 4.344 -32.728 -9.128 1.00 12.88 C ANISOU 478 CA ASP A 60 1522 1727 1644 78 108 -101 C ATOM 479 C ASP A 60 5.394 -31.720 -8.692 1.00 12.62 C ANISOU 479 C ASP A 60 1551 1740 1504 47 -95 -67 C ATOM 480 O ASP A 60 6.138 -31.965 -7.743 1.00 11.97 O ANISOU 480 O ASP A 60 1411 1836 1301 52 -264 -91 O ATOM 481 CB ASP A 60 4.957 -33.712 -10.116 1.00 13.32 C ANISOU 481 CB ASP A 60 1393 1898 1770 65 -52 -45 C ATOM 482 CG ASP A 60 5.888 -34.679 -9.431 1.00 14.11 C ANISOU 482 CG ASP A 60 1494 1999 1869 71 32 -39 C ATOM 483 OD1 ASP A 60 5.427 -35.340 -8.479 1.00 15.57 O ANISOU 483 OD1 ASP A 60 1538 2353 2025 169 238 64 O ATOM 484 OD2 ASP A 60 7.075 -34.759 -9.811 1.00 16.53 O ANISOU 484 OD2 ASP A 60 1446 2641 2191 183 243 22 O ATOM 485 N LEU A 61 5.463 -30.586 -9.380 1.00 12.25 N ANISOU 485 N LEU A 61 1427 1636 1591 -135 4 -44 N ATOM 486 C LEU A 61 5.968 -28.986 -7.602 1.00 11.29 C ANISOU 486 C LEU A 61 1298 1616 1372 49 -5 107 C ATOM 487 O LEU A 61 6.809 -28.754 -6.737 1.00 11.88 O ANISOU 487 O LEU A 61 1363 1895 1254 -231 -169 159 O ATOM 488 CA ALEU A 61 6.373 -29.527 -8.975 0.50 11.98 C ANISOU 488 CA ALEU A 61 1536 1589 1425 -140 -15 160 C ATOM 489 CB ALEU A 61 6.418 -28.418 -10.030 0.50 11.90 C ANISOU 489 CB ALEU A 61 1394 1502 1623 -134 8 128 C ATOM 490 CG ALEU A 61 7.431 -27.293 -9.812 0.50 12.23 C ANISOU 490 CG ALEU A 61 1373 1560 1711 -58 49 148 C ATOM 491 CD1ALEU A 61 7.864 -26.710 -11.148 0.50 12.68 C ANISOU 491 CD1ALEU A 61 1321 1532 1965 -92 117 308 C ATOM 492 CD2ALEU A 61 6.845 -26.224 -8.908 0.50 13.98 C ANISOU 492 CD2ALEU A 61 1740 1651 1921 -256 68 -51 C ATOM 493 CA BLEU A 61 6.377 -29.528 -8.969 0.50 12.20 C ANISOU 493 CA BLEU A 61 1550 1589 1496 -92 39 133 C ATOM 494 CB BLEU A 61 6.448 -28.407 -10.010 0.50 11.74 C ANISOU 494 CB BLEU A 61 1356 1485 1618 -50 77 69 C ATOM 495 CG BLEU A 61 7.469 -27.304 -9.709 0.50 11.62 C ANISOU 495 CG BLEU A 61 1278 1512 1625 57 141 27 C ATOM 496 CD1BLEU A 61 8.846 -27.897 -9.438 0.50 12.37 C ANISOU 496 CD1BLEU A 61 1356 1519 1825 36 166 -197 C ATOM 497 CD2BLEU A 61 7.528 -26.305 -10.851 0.50 13.40 C ANISOU 497 CD2BLEU A 61 1641 1581 1869 32 246 115 C ATOM 498 N LYS A 62 4.669 -28.804 -7.397 1.00 11.45 N ANISOU 498 N LYS A 62 1206 1664 1478 17 -83 63 N ATOM 499 C LYS A 62 4.518 -29.395 -5.027 1.00 11.01 C ANISOU 499 C LYS A 62 1247 1323 1610 -12 -130 85 C ATOM 500 O LYS A 62 4.939 -29.039 -3.930 1.00 11.33 O ANISOU 500 O LYS A 62 1340 1498 1467 16 -143 -62 O ATOM 501 CA ALYS A 62 4.162 -28.367 -6.096 0.50 11.90 C ANISOU 501 CA ALYS A 62 1311 1569 1640 107 -144 115 C ATOM 502 CB ALYS A 62 2.642 -28.157 -6.125 0.50 11.94 C ANISOU 502 CB ALYS A 62 1043 1580 1911 97 -248 51 C ATOM 503 CG ALYS A 62 2.155 -26.947 -6.912 0.50 12.63 C ANISOU 503 CG ALYS A 62 1271 1615 1910 61 -95 -3 C ATOM 504 CD ALYS A 62 0.631 -26.866 -6.838 0.50 14.04 C ANISOU 504 CD ALYS A 62 1515 1845 1974 159 -116 100 C ATOM 505 CE ALYS A 62 0.027 -26.199 -8.058 0.50 16.66 C ANISOU 505 CE ALYS A 62 1806 2279 2245 165 2 -74 C ATOM 506 NZ ALYS A 62 -1.419 -26.531 -8.179 0.50 17.34 N ANISOU 506 NZ ALYS A 62 1867 2662 2058 435 48 -217 N ATOM 507 CA BLYS A 62 4.150 -28.379 -6.103 0.50 11.52 C ANISOU 507 CA BLYS A 62 1310 1510 1557 118 -115 137 C ATOM 508 CB BLYS A 62 2.633 -28.240 -6.182 0.50 12.19 C ANISOU 508 CB BLYS A 62 1196 1597 1835 110 -99 106 C ATOM 509 CG BLYS A 62 1.987 -27.742 -4.917 0.50 12.58 C ANISOU 509 CG BLYS A 62 1460 1590 1730 160 99 121 C ATOM 510 CD BLYS A 62 0.478 -27.720 -5.092 0.50 12.25 C ANISOU 510 CD BLYS A 62 1319 1498 1837 -8 117 115 C ATOM 511 CE BLYS A 62 -0.087 -26.339 -4.817 0.50 15.78 C ANISOU 511 CE BLYS A 62 1866 1715 2413 96 125 327 C ATOM 512 NZ BLYS A 62 -1.463 -26.173 -5.366 0.50 13.84 N ANISOU 512 NZ BLYS A 62 1642 1409 2207 116 354 357 N ATOM 513 N LYS A 63 4.342 -30.669 -5.353 1.00 9.88 N ANISOU 513 N LYS A 63 1237 1114 1403 -93 119 21 N ATOM 514 CA LYS A 63 4.698 -31.748 -4.452 1.00 10.89 C ANISOU 514 CA LYS A 63 1222 1368 1547 -28 -189 -68 C ATOM 515 C LYS A 63 6.177 -31.680 -4.065 1.00 9.70 C ANISOU 515 C LYS A 63 1403 1071 1211 7 -70 59 C ATOM 516 O LYS A 63 6.532 -31.777 -2.884 1.00 10.06 O ANISOU 516 O LYS A 63 1391 1164 1266 -25 -71 -16 O ATOM 517 CB LYS A 63 4.364 -33.083 -5.111 1.00 10.63 C ANISOU 517 CB LYS A 63 1371 1114 1552 23 40 -33 C ATOM 518 CG LYS A 63 4.631 -34.305 -4.263 1.00 10.65 C ANISOU 518 CG LYS A 63 1404 1024 1617 78 58 -22 C ATOM 519 CD LYS A 63 4.291 -35.555 -5.073 1.00 11.78 C ANISOU 519 CD LYS A 63 1572 1104 1799 58 -98 -53 C ATOM 520 CE LYS A 63 4.541 -36.831 -4.307 1.00 12.37 C ANISOU 520 CE LYS A 63 1987 1023 1689 267 -2 -30 C ATOM 521 NZ LYS A 63 4.275 -38.023 -5.168 1.00 15.26 N ANISOU 521 NZ LYS A 63 2896 1077 1822 -71 -339 265 N ATOM 522 N HIS A 64 7.049 -31.513 -5.053 1.00 9.83 N ANISOU 522 N HIS A 64 1112 1242 1378 5 -112 -84 N ATOM 523 CA HIS A 64 8.454 -31.399 -4.727 1.00 9.79 C ANISOU 523 CA HIS A 64 1175 1287 1256 -21 98 -101 C ATOM 524 C HIS A 64 8.755 -30.161 -3.881 1.00 9.89 C ANISOU 524 C HIS A 64 1233 1399 1123 13 2 -57 C ATOM 525 O HIS A 64 9.583 -30.199 -2.977 1.00 10.02 O ANISOU 525 O HIS A 64 1275 1443 1087 -36 -12 145 O ATOM 526 CB HIS A 64 9.356 -31.446 -5.952 1.00 10.72 C ANISOU 526 CB HIS A 64 1210 1471 1391 45 10 -103 C ATOM 527 CG HIS A 64 10.781 -31.693 -5.590 1.00 12.02 C ANISOU 527 CG HIS A 64 1485 1681 1398 18 -65 -242 C ATOM 528 ND1 HIS A 64 11.198 -32.889 -5.050 1.00 13.99 N ANISOU 528 ND1 HIS A 64 1764 1519 2030 300 46 31 N ATOM 529 CD2 HIS A 64 11.866 -30.885 -5.604 1.00 13.17 C ANISOU 529 CD2 HIS A 64 1680 2020 1301 11 307 -13 C ATOM 530 CE1 HIS A 64 12.488 -32.818 -4.777 1.00 13.99 C ANISOU 530 CE1 HIS A 64 1460 2322 1530 309 46 172 C ATOM 531 NE2 HIS A 64 12.918 -31.612 -5.102 1.00 13.17 N ANISOU 531 NE2 HIS A 64 1561 1991 1451 26 185 -162 N ATOM 532 N GLY A 65 8.062 -29.065 -4.156 1.00 10.06 N ANISOU 532 N GLY A 65 1230 1147 1442 -24 -65 0 N ATOM 533 CA GLY A 65 8.225 -27.865 -3.343 1.00 10.77 C ANISOU 533 CA GLY A 65 1321 1334 1435 27 -111 -168 C ATOM 534 C GLY A 65 7.881 -28.123 -1.886 1.00 9.46 C ANISOU 534 C GLY A 65 1041 1217 1334 103 -2 -5 C ATOM 535 O GLY A 65 8.546 -27.624 -0.978 1.00 10.82 O ANISOU 535 O GLY A 65 1172 1481 1457 153 -151 -289 O ATOM 536 N THR A 66 6.835 -28.909 -1.660 1.00 10.74 N ANISOU 536 N THR A 66 1357 1226 1496 50 -96 -4 N ATOM 537 CA THR A 66 6.452 -29.296 -0.308 1.00 10.56 C ANISOU 537 CA THR A 66 1168 1339 1502 -10 9 -171 C ATOM 538 C THR A 66 7.538 -30.144 0.364 1.00 9.88 C ANISOU 538 C THR A 66 1013 1402 1337 148 48 -117 C ATOM 539 O THR A 66 7.857 -29.941 1.533 1.00 9.33 O ANISOU 539 O THR A 66 1006 1307 1230 14 -39 -206 O ATOM 540 CB THR A 66 5.121 -30.058 -0.319 1.00 11.46 C ANISOU 540 CB THR A 66 1121 1616 1613 13 60 -252 C ATOM 541 OG1 THR A 66 4.086 -29.167 -0.749 1.00 13.80 O ANISOU 541 OG1 THR A 66 1230 1962 2049 181 -83 -73 O ATOM 542 CG2 THR A 66 4.800 -30.581 1.073 1.00 12.89 C ANISOU 542 CG2 THR A 66 1395 1884 1618 -142 96 -11 C ATOM 543 N VAL A 67 8.098 -31.093 -0.375 1.00 9.71 N ANISOU 543 N VAL A 67 958 1385 1343 85 38 33 N ATOM 544 CA VAL A 67 9.153 -31.942 0.161 1.00 9.43 C ANISOU 544 CA VAL A 67 1020 1206 1355 49 138 -24 C ATOM 545 C VAL A 67 10.372 -31.089 0.540 1.00 9.31 C ANISOU 545 C VAL A 67 987 1552 997 27 91 -39 C ATOM 546 O VAL A 67 10.939 -31.225 1.633 1.00 9.25 O ANISOU 546 O VAL A 67 875 1330 1308 -23 22 4 O ATOM 547 CB VAL A 67 9.525 -33.051 -0.845 1.00 9.51 C ANISOU 547 CB VAL A 67 1047 1109 1455 -79 135 -91 C ATOM 548 CG1 VAL A 67 10.827 -33.740 -0.447 1.00 10.36 C ANISOU 548 CG1 VAL A 67 893 1376 1666 85 217 126 C ATOM 549 CG2 VAL A 67 8.392 -34.080 -0.943 1.00 9.83 C ANISOU 549 CG2 VAL A 67 1094 1092 1549 -200 167 -143 C ATOM 550 N VAL A 68 10.756 -30.186 -0.355 1.00 9.30 N ANISOU 550 N VAL A 68 995 1255 1282 -5 104 -2 N ATOM 551 CA VAL A 68 11.906 -29.325 -0.116 1.00 9.81 C ANISOU 551 CA VAL A 68 1288 1310 1127 56 -92 39 C ATOM 552 C VAL A 68 11.713 -28.424 1.109 1.00 8.74 C ANISOU 552 C VAL A 68 1034 1186 1098 6 19 64 C ATOM 553 O VAL A 68 12.548 -28.387 2.017 1.00 9.53 O ANISOU 553 O VAL A 68 1090 1212 1318 -30 -44 -60 O ATOM 554 CB VAL A 68 12.212 -28.480 -1.372 1.00 10.08 C ANISOU 554 CB VAL A 68 1306 1140 1381 122 -70 -58 C ATOM 555 CG1 VAL A 68 13.215 -27.373 -1.060 1.00 9.72 C ANISOU 555 CG1 VAL A 68 1202 1002 1489 29 -78 -14 C ATOM 556 CG2 VAL A 68 12.699 -29.379 -2.502 1.00 10.50 C ANISOU 556 CG2 VAL A 68 1279 1321 1388 264 -49 64 C ATOM 557 N LEU A 69 10.600 -27.696 1.155 1.00 10.25 N ANISOU 557 N LEU A 69 1045 1404 1443 -22 0 -42 N ATOM 558 CA LEU A 69 10.412 -26.764 2.260 1.00 9.92 C ANISOU 558 CA LEU A 69 1187 1328 1254 94 58 -15 C ATOM 559 C LEU A 69 10.138 -27.464 3.587 1.00 9.78 C ANISOU 559 C LEU A 69 974 1367 1373 120 -65 15 C ATOM 560 O LEU A 69 10.487 -26.946 4.644 1.00 10.27 O ANISOU 560 O LEU A 69 1182 1422 1298 -158 -125 -21 O ATOM 561 CB LEU A 69 9.351 -25.715 1.940 1.00 10.13 C ANISOU 561 CB LEU A 69 1196 1337 1314 70 68 16 C ATOM 562 CG LEU A 69 9.703 -24.706 0.833 1.00 9.66 C ANISOU 562 CG LEU A 69 1107 1197 1366 52 178 98 C ATOM 563 CD1 LEU A 69 8.688 -23.569 0.835 1.00 10.79 C ANISOU 563 CD1 LEU A 69 1355 1232 1509 561 310 208 C ATOM 564 CD2 LEU A 69 11.113 -24.150 1.001 1.00 12.03 C ANISOU 564 CD2 LEU A 69 1278 1640 1651 26 129 -70 C ATOM 565 N THR A 70 9.550 -28.657 3.537 1.00 10.19 N ANISOU 565 N THR A 70 1307 1265 1297 41 -84 -84 N ATOM 566 CA THR A 70 9.346 -29.423 4.767 1.00 10.02 C ANISOU 566 CA THR A 70 1085 1336 1386 9 -25 -94 C ATOM 567 C THR A 70 10.697 -29.833 5.355 1.00 9.59 C ANISOU 567 C THR A 70 906 1332 1405 -81 80 -95 C ATOM 568 O THR A 70 10.915 -29.741 6.563 1.00 9.88 O ANISOU 568 O THR A 70 1154 1390 1209 45 77 -118 O ATOM 569 CB THR A 70 8.487 -30.667 4.529 1.00 10.85 C ANISOU 569 CB THR A 70 1174 1429 1518 -41 -7 -9 C ATOM 570 OG1 THR A 70 7.173 -30.256 4.125 1.00 11.06 O ANISOU 570 OG1 THR A 70 941 1652 1608 -7 228 -252 O ATOM 571 CG2 THR A 70 8.381 -31.496 5.806 1.00 12.22 C ANISOU 571 CG2 THR A 70 1406 1768 1468 -281 134 -140 C ATOM 572 N ALA A 71 11.625 -30.239 4.496 1.00 9.95 N ANISOU 572 N ALA A 71 1054 1317 1408 -54 221 13 N ATOM 573 CA ALA A 71 12.959 -30.615 4.965 1.00 9.25 C ANISOU 573 CA ALA A 71 749 1449 1316 6 120 -16 C ATOM 574 C ALA A 71 13.664 -29.386 5.550 1.00 9.54 C ANISOU 574 C ALA A 71 1007 1302 1315 -100 106 50 C ATOM 575 O ALA A 71 14.267 -29.451 6.628 1.00 9.93 O ANISOU 575 O ALA A 71 1060 1464 1248 -23 43 98 O ATOM 576 CB ALA A 71 13.775 -31.194 3.820 1.00 10.03 C ANISOU 576 CB ALA A 71 903 1684 1221 -122 224 -1 C ATOM 577 N LEU A 72 13.584 -28.259 4.847 1.00 9.89 N ANISOU 577 N LEU A 72 1094 1311 1353 -58 72 -10 N ATOM 578 CA LEU A 72 14.223 -27.045 5.320 1.00 9.47 C ANISOU 578 CA LEU A 72 957 1332 1309 -83 -43 68 C ATOM 579 C LEU A 72 13.631 -26.594 6.652 1.00 9.92 C ANISOU 579 C LEU A 72 1014 1482 1269 -5 -8 -30 C ATOM 580 O LEU A 72 14.360 -26.192 7.564 1.00 10.03 O ANISOU 580 O LEU A 72 1135 1431 1242 -286 -147 6 O ATOM 581 CB LEU A 72 14.122 -25.930 4.277 1.00 9.15 C ANISOU 581 CB LEU A 72 841 1337 1298 67 19 90 C ATOM 582 CG LEU A 72 14.765 -24.601 4.682 1.00 9.40 C ANISOU 582 CG LEU A 72 855 1291 1424 61 13 -113 C ATOM 583 CD1 LEU A 72 16.254 -24.760 4.996 1.00 11.60 C ANISOU 583 CD1 LEU A 72 965 1467 1972 79 -74 0 C ATOM 584 CD2 LEU A 72 14.572 -23.577 3.571 1.00 10.13 C ANISOU 584 CD2 LEU A 72 1173 1335 1341 158 -111 153 C ATOM 585 N GLY A 73 12.310 -26.660 6.775 1.00 10.52 N ANISOU 585 N GLY A 73 1136 1442 1416 -202 -10 -51 N ATOM 586 CA GLY A 73 11.649 -26.277 8.019 1.00 10.51 C ANISOU 586 CA GLY A 73 1218 1436 1337 -228 -6 52 C ATOM 587 C GLY A 73 12.099 -27.114 9.201 1.00 10.81 C ANISOU 587 C GLY A 73 1164 1405 1537 -221 -112 118 C ATOM 588 O GLY A 73 12.318 -26.591 10.292 1.00 10.65 O ANISOU 588 O GLY A 73 1095 1588 1363 -377 -94 71 O ATOM 589 N GLY A 74 12.242 -28.418 8.986 1.00 11.32 N ANISOU 589 N GLY A 74 1328 1371 1601 -211 -63 138 N ATOM 590 CA GLY A 74 12.737 -29.309 10.035 1.00 12.14 C ANISOU 590 CA GLY A 74 1362 1455 1796 -242 -162 216 C ATOM 591 C GLY A 74 14.123 -28.899 10.479 1.00 11.22 C ANISOU 591 C GLY A 74 1365 1465 1433 -114 -111 253 C ATOM 592 O GLY A 74 14.436 -28.891 11.671 1.00 12.41 O ANISOU 592 O GLY A 74 1424 1858 1433 -105 -61 214 O ATOM 593 N ILE A 75 14.963 -28.562 9.507 1.00 11.30 N ANISOU 593 N ILE A 75 1146 1626 1519 -107 -9 225 N ATOM 594 CA ILE A 75 16.316 -28.107 9.798 1.00 10.83 C ANISOU 594 CA ILE A 75 1191 1323 1599 -91 53 82 C ATOM 595 C ILE A 75 16.313 -26.789 10.574 1.00 9.76 C ANISOU 595 C ILE A 75 1039 1355 1314 69 -30 42 C ATOM 596 O ILE A 75 16.994 -26.655 11.594 1.00 9.79 O ANISOU 596 O ILE A 75 900 1570 1246 69 -20 -1 O ATOM 597 CB ILE A 75 17.148 -28.014 8.504 1.00 10.99 C ANISOU 597 CB ILE A 75 1304 1284 1586 125 9 2 C ATOM 598 CG1 ILE A 75 17.463 -29.425 7.999 1.00 12.95 C ANISOU 598 CG1 ILE A 75 1636 1598 1682 81 38 -213 C ATOM 599 CG2 ILE A 75 18.419 -27.195 8.717 1.00 12.44 C ANISOU 599 CG2 ILE A 75 1313 1664 1749 -213 -83 32 C ATOM 600 CD1 ILE A 75 17.915 -29.481 6.555 1.00 15.87 C ANISOU 600 CD1 ILE A 75 2287 1686 2057 93 441 -272 C ATOM 601 N LEU A 76 15.525 -25.821 10.117 1.00 9.28 N ANISOU 601 N LEU A 76 997 1319 1208 -75 144 49 N ATOM 602 CA LEU A 76 15.485 -24.523 10.788 1.00 9.23 C ANISOU 602 CA LEU A 76 1024 1201 1280 -46 172 -52 C ATOM 603 C LEU A 76 15.026 -24.644 12.239 1.00 8.91 C ANISOU 603 C LEU A 76 778 1101 1507 -32 58 -15 C ATOM 604 O LEU A 76 15.526 -23.937 13.121 1.00 9.65 O ANISOU 604 O LEU A 76 939 1411 1315 242 -57 -11 O ATOM 605 CB LEU A 76 14.588 -23.541 10.033 1.00 9.61 C ANISOU 605 CB LEU A 76 815 1322 1515 -107 72 64 C ATOM 606 CG LEU A 76 15.053 -23.145 8.630 1.00 10.38 C ANISOU 606 CG LEU A 76 972 1688 1281 -205 156 6 C ATOM 607 CD1 LEU A 76 13.997 -22.278 7.962 1.00 11.96 C ANISOU 607 CD1 LEU A 76 1299 1771 1474 101 179 244 C ATOM 608 CD2 LEU A 76 16.389 -22.414 8.717 1.00 12.22 C ANISOU 608 CD2 LEU A 76 1138 1758 1747 -360 417 9 C ATOM 609 N LYS A 77 14.074 -25.538 12.494 1.00 9.61 N ANISOU 609 N LYS A 77 974 1413 1264 170 218 275 N ATOM 610 CA LYS A 77 13.569 -25.691 13.850 1.00 9.90 C ANISOU 610 CA LYS A 77 922 1371 1466 129 75 284 C ATOM 611 C LYS A 77 14.584 -26.287 14.821 1.00 9.73 C ANISOU 611 C LYS A 77 917 1413 1365 240 -162 -163 C ATOM 612 O LYS A 77 14.383 -26.231 16.028 1.00 10.16 O ANISOU 612 O LYS A 77 1081 1371 1407 577 31 161 O ATOM 613 CB LYS A 77 12.243 -26.439 13.856 1.00 11.23 C ANISOU 613 CB LYS A 77 876 1674 1717 13 89 504 C ATOM 614 CG LYS A 77 11.151 -25.633 13.174 1.00 13.61 C ANISOU 614 CG LYS A 77 1202 2177 1790 163 -244 683 C ATOM 615 CD LYS A 77 9.824 -26.334 13.172 1.00 14.61 C ANISOU 615 CD LYS A 77 1475 1871 2204 163 -150 877 C ATOM 616 CE LYS A 77 8.803 -25.507 12.424 1.00 13.86 C ANISOU 616 CE LYS A 77 1511 1768 1987 177 -192 1087 C ATOM 617 NZ LYS A 77 7.451 -26.085 12.562 1.00 14.55 N ANISOU 617 NZ LYS A 77 1749 1533 2244 -104 45 781 N ATOM 618 N LYS A 78 15.684 -26.825 14.297 1.00 11.12 N ANISOU 618 N LYS A 78 971 1634 1620 -107 -82 85 N ATOM 619 CA LYS A 78 16.784 -27.295 15.144 1.00 11.42 C ANISOU 619 CA LYS A 78 1183 1611 1544 36 -7 66 C ATOM 620 C LYS A 78 17.695 -26.150 15.592 1.00 11.85 C ANISOU 620 C LYS A 78 1320 1564 1616 56 -27 23 C ATOM 621 O LYS A 78 18.591 -26.353 16.408 1.00 12.49 O ANISOU 621 O LYS A 78 1177 1798 1768 -17 -203 86 O ATOM 622 CB LYS A 78 17.607 -28.365 14.425 1.00 13.05 C ANISOU 622 CB LYS A 78 1493 1493 1973 119 197 -133 C ATOM 623 CG LYS A 78 16.856 -29.664 14.156 1.00 16.49 C ANISOU 623 CG LYS A 78 1816 1780 2669 2 -55 -177 C ATOM 624 CD LYS A 78 16.365 -30.301 15.445 1.00 21.00 C ANISOU 624 CD LYS A 78 2364 2003 3609 -95 398 -126 C ATOM 625 CE LYS A 78 15.746 -31.663 15.179 1.00 27.47 C ANISOU 625 CE LYS A 78 3042 3146 4246 -261 221 -70 C ATOM 626 NZ LYS A 78 15.039 -32.192 16.376 1.00 32.10 N ANISOU 626 NZ LYS A 78 3922 3533 4740 -370 253 40 N ATOM 627 N LYS A 79 17.476 -24.954 15.049 1.00 11.12 N ANISOU 627 N LYS A 79 1291 1389 1545 -86 0 -177 N ATOM 628 C LYS A 79 19.744 -24.030 15.429 1.00 12.72 C ANISOU 628 C LYS A 79 1334 1832 1666 53 -43 14 C ATOM 629 O LYS A 79 20.463 -23.695 16.382 1.00 12.19 O ANISOU 629 O LYS A 79 1347 1609 1675 18 -19 -117 O ATOM 630 CA ALYS A 79 18.238 -23.777 15.453 0.50 11.79 C ANISOU 630 CA ALYS A 79 1153 1651 1673 9 91 -79 C ATOM 631 CB ALYS A 79 17.787 -23.293 16.835 0.50 12.11 C ANISOU 631 CB ALYS A 79 1050 1866 1683 -85 54 -18 C ATOM 632 CG ALYS A 79 16.329 -22.842 16.877 0.50 12.43 C ANISOU 632 CG ALYS A 79 1150 1719 1852 -30 339 -118 C ATOM 633 CD ALYS A 79 15.816 -22.703 18.307 0.50 12.55 C ANISOU 633 CD ALYS A 79 1219 1782 1765 -107 336 84 C ATOM 634 CE ALYS A 79 16.516 -21.573 19.049 0.50 13.14 C ANISOU 634 CE ALYS A 79 1468 1748 1777 14 362 45 C ATOM 635 NZ ALYS A 79 16.043 -21.456 20.464 0.50 12.25 N ANISOU 635 NZ ALYS A 79 1204 1581 1868 131 515 409 N ATOM 636 CA BLYS A 79 18.241 -23.773 15.439 0.50 11.58 C ANISOU 636 CA BLYS A 79 1147 1609 1643 45 74 -44 C ATOM 637 CB BLYS A 79 17.776 -23.240 16.797 0.50 11.50 C ANISOU 637 CB BLYS A 79 1055 1731 1584 12 3 111 C ATOM 638 CG BLYS A 79 16.313 -22.805 16.809 0.50 11.09 C ANISOU 638 CG BLYS A 79 1116 1463 1634 113 239 71 C ATOM 639 CD BLYS A 79 15.948 -22.067 18.090 0.50 11.08 C ANISOU 639 CD BLYS A 79 1348 1447 1413 152 207 357 C ATOM 640 CE BLYS A 79 16.236 -22.904 19.326 0.50 9.71 C ANISOU 640 CE BLYS A 79 1308 1147 1234 38 322 517 C ATOM 641 NZ BLYS A 79 15.793 -22.200 20.564 0.50 9.72 N ANISOU 641 NZ BLYS A 79 1127 1194 1370 42 379 536 N ATOM 642 N GLY A 80 20.220 -24.613 14.334 1.00 11.75 N ANISOU 642 N GLY A 80 1187 1482 1794 -55 95 -108 N ATOM 643 CA GLY A 80 21.651 -24.826 14.154 1.00 12.76 C ANISOU 643 CA GLY A 80 1213 1795 1839 157 113 -168 C ATOM 644 C GLY A 80 22.148 -26.195 14.577 1.00 13.52 C ANISOU 644 C GLY A 80 1430 1880 1826 232 89 -71 C ATOM 645 O GLY A 80 23.223 -26.623 14.153 1.00 14.55 O ANISOU 645 O GLY A 80 1211 2054 2261 175 228 -313 O ATOM 646 N HIS A 81 21.373 -26.885 15.410 1.00 12.97 N ANISOU 646 N HIS A 81 1542 1682 1704 248 117 0 N ATOM 647 CA HIS A 81 21.761 -28.209 15.895 1.00 13.56 C ANISOU 647 CA HIS A 81 1703 1811 1638 214 83 -119 C ATOM 648 C HIS A 81 21.210 -29.265 14.961 1.00 12.54 C ANISOU 648 C HIS A 81 1428 1407 1928 147 -33 51 C ATOM 649 O HIS A 81 20.386 -30.094 15.353 1.00 14.55 O ANISOU 649 O HIS A 81 1678 1852 1996 177 195 124 O ATOM 650 CB HIS A 81 21.225 -28.433 17.304 1.00 16.42 C ANISOU 650 CB HIS A 81 2277 1971 1991 263 -126 36 C ATOM 651 CG HIS A 81 21.741 -27.445 18.298 1.00 20.76 C ANISOU 651 CG HIS A 81 2703 2797 2386 162 -242 -241 C ATOM 652 ND1 HIS A 81 22.971 -27.577 18.904 1.00 24.49 N ANISOU 652 ND1 HIS A 81 2994 3354 2956 114 -364 -327 N ATOM 653 CD2 HIS A 81 21.203 -26.300 18.779 1.00 21.91 C ANISOU 653 CD2 HIS A 81 2778 2945 2598 84 -139 -502 C ATOM 654 CE1 HIS A 81 23.165 -26.561 19.726 1.00 24.11 C ANISOU 654 CE1 HIS A 81 3046 3176 2938 74 -338 -626 C ATOM 655 NE2 HIS A 81 22.107 -25.772 19.669 1.00 24.04 N ANISOU 655 NE2 HIS A 81 2806 3433 2892 37 -406 -568 N ATOM 656 N HIS A 82 21.687 -29.232 13.722 1.00 12.01 N ANISOU 656 N HIS A 82 1271 1682 1609 110 -45 -30 N ATOM 657 CA HIS A 82 21.026 -29.929 12.626 1.00 11.03 C ANISOU 657 CA HIS A 82 1274 1445 1470 81 -171 -103 C ATOM 658 C HIS A 82 21.936 -30.916 11.906 1.00 11.88 C ANISOU 658 C HIS A 82 1284 1437 1791 -2 -34 -77 C ATOM 659 O HIS A 82 21.661 -31.292 10.770 1.00 12.69 O ANISOU 659 O HIS A 82 1719 1369 1732 67 -69 -265 O ATOM 660 CB HIS A 82 20.469 -28.916 11.623 1.00 11.90 C ANISOU 660 CB HIS A 82 1348 1557 1616 6 10 25 C ATOM 661 CG HIS A 82 21.489 -27.940 11.124 1.00 10.53 C ANISOU 661 CG HIS A 82 1142 1483 1373 52 70 77 C ATOM 662 ND1 HIS A 82 21.201 -26.611 10.901 1.00 11.67 N ANISOU 662 ND1 HIS A 82 1171 1608 1654 21 153 -85 N ATOM 663 CD2 HIS A 82 22.798 -28.100 10.808 1.00 12.09 C ANISOU 663 CD2 HIS A 82 1377 1738 1476 13 85 -26 C ATOM 664 CE1 HIS A 82 22.286 -25.995 10.463 1.00 10.24 C ANISOU 664 CE1 HIS A 82 1020 1362 1509 -16 113 69 C ATOM 665 NE2 HIS A 82 23.270 -26.875 10.401 1.00 11.60 N ANISOU 665 NE2 HIS A 82 1296 1545 1565 179 47 -94 N ATOM 666 N GLU A 83 23.010 -31.346 12.560 1.00 11.73 N ANISOU 666 N GLU A 83 1292 1550 1615 54 10 -96 N ATOM 667 CA GLU A 83 23.935 -32.277 11.919 1.00 12.11 C ANISOU 667 CA GLU A 83 1326 1555 1717 -35 -30 -169 C ATOM 668 C GLU A 83 23.231 -33.518 11.360 1.00 11.57 C ANISOU 668 C GLU A 83 1390 1546 1461 71 100 -94 C ATOM 669 O GLU A 83 23.459 -33.902 10.218 1.00 12.68 O ANISOU 669 O GLU A 83 1706 1515 1596 -6 48 -239 O ATOM 670 CB GLU A 83 25.057 -32.680 12.883 1.00 13.74 C ANISOU 670 CB GLU A 83 1354 1857 2008 114 -222 -136 C ATOM 671 CG GLU A 83 25.905 -33.863 12.412 1.00 15.69 C ANISOU 671 CG GLU A 83 1593 2092 2274 -100 -55 -34 C ATOM 672 CD GLU A 83 26.834 -33.531 11.254 1.00 16.15 C ANISOU 672 CD GLU A 83 1882 2027 2226 -35 -101 65 C ATOM 673 OE1 GLU A 83 27.042 -32.335 10.960 1.00 18.28 O ANISOU 673 OE1 GLU A 83 2102 2196 2647 -76 138 110 O ATOM 674 OE2 GLU A 83 27.371 -34.478 10.641 1.00 16.74 O ANISOU 674 OE2 GLU A 83 1991 2093 2275 62 342 100 O ATOM 675 N ALA A 84 22.377 -34.143 12.166 1.00 11.57 N ANISOU 675 N ALA A 84 1341 1549 1504 -93 25 -146 N ATOM 676 CA ALA A 84 21.726 -35.390 11.762 1.00 11.82 C ANISOU 676 CA ALA A 84 1493 1419 1578 -169 -68 -135 C ATOM 677 C ALA A 84 20.804 -35.194 10.555 1.00 12.24 C ANISOU 677 C ALA A 84 1488 1435 1726 -140 -126 -154 C ATOM 678 O ALA A 84 20.668 -36.079 9.700 1.00 12.84 O ANISOU 678 O ALA A 84 1690 1517 1672 127 -196 -298 O ATOM 679 CB ALA A 84 20.947 -35.981 12.930 1.00 15.68 C ANISOU 679 CB ALA A 84 1930 1988 2040 -446 -197 -145 C ATOM 680 N GLU A 85 20.166 -34.032 10.501 1.00 12.29 N ANISOU 680 N GLU A 85 1375 1584 1709 -102 -125 -78 N ATOM 681 CA GLU A 85 19.215 -33.714 9.446 1.00 13.05 C ANISOU 681 CA GLU A 85 1560 1830 1565 75 -294 -108 C ATOM 682 C GLU A 85 19.946 -33.266 8.191 1.00 14.16 C ANISOU 682 C GLU A 85 1758 1930 1690 -108 -426 -73 C ATOM 683 O GLU A 85 19.562 -33.593 7.068 1.00 15.26 O ANISOU 683 O GLU A 85 2243 1977 1578 -373 -572 85 O ATOM 684 CB GLU A 85 18.300 -32.570 9.901 1.00 14.29 C ANISOU 684 CB GLU A 85 1679 2069 1682 70 -366 -267 C ATOM 685 CG GLU A 85 17.287 -32.932 10.976 1.00 15.63 C ANISOU 685 CG GLU A 85 1676 2168 2095 3 -21 -143 C ATOM 686 CD GLU A 85 17.845 -32.909 12.395 1.00 17.50 C ANISOU 686 CD GLU A 85 1951 2346 2350 -39 151 -277 C ATOM 687 OE1 GLU A 85 19.011 -32.512 12.609 1.00 15.32 O ANISOU 687 OE1 GLU A 85 1817 2112 1891 243 60 -391 O ATOM 688 OE2 GLU A 85 17.086 -33.280 13.315 1.00 20.24 O ANISOU 688 OE2 GLU A 85 2409 2794 2486 -80 232 2 O ATOM 689 N LEU A 86 21.012 -32.509 8.398 1.00 13.85 N ANISOU 689 N LEU A 86 1897 1796 1569 -144 -311 110 N ATOM 690 C LEU A 86 22.692 -32.788 6.580 1.00 14.10 C ANISOU 690 C LEU A 86 1815 1919 1622 -70 -27 237 C ATOM 691 O LEU A 86 22.778 -32.775 5.353 1.00 15.72 O ANISOU 691 O LEU A 86 2397 2170 1405 -14 187 -22 O ATOM 692 CA ALEU A 86 21.692 -31.874 7.288 0.50 13.86 C ANISOU 692 CA ALEU A 86 1781 1906 1577 -208 -5 38 C ATOM 693 CB ALEU A 86 22.329 -30.553 7.727 0.50 13.99 C ANISOU 693 CB ALEU A 86 1894 1891 1528 -150 -119 -51 C ATOM 694 CG ALEU A 86 22.992 -29.713 6.642 0.50 13.53 C ANISOU 694 CG ALEU A 86 1688 1674 1778 -41 46 -41 C ATOM 695 CD1ALEU A 86 22.807 -28.233 6.929 0.50 11.17 C ANISOU 695 CD1ALEU A 86 1544 1204 1494 -204 -169 -201 C ATOM 696 CD2ALEU A 86 24.464 -30.080 6.527 0.50 10.01 C ANISOU 696 CD2ALEU A 86 1255 1364 1183 125 122 46 C ATOM 697 CA BLEU A 86 21.717 -31.859 7.304 0.50 15.47 C ANISOU 697 CA BLEU A 86 1978 2164 1734 -222 58 94 C ATOM 698 CB BLEU A 86 22.448 -30.615 7.818 0.50 17.60 C ANISOU 698 CB BLEU A 86 2269 2462 1955 -281 57 -10 C ATOM 699 CG BLEU A 86 22.929 -29.606 6.779 0.50 18.43 C ANISOU 699 CG BLEU A 86 2291 2600 2109 -161 214 44 C ATOM 700 CD1BLEU A 86 21.810 -29.267 5.813 0.50 19.64 C ANISOU 700 CD1BLEU A 86 2484 2894 2083 -99 144 49 C ATOM 701 CD2BLEU A 86 23.442 -28.356 7.469 0.50 17.35 C ANISOU 701 CD2BLEU A 86 2156 2477 1956 -318 190 237 C ATOM 702 N LYS A 87 23.434 -33.594 7.338 1.00 14.96 N ANISOU 702 N LYS A 87 1828 2162 1693 358 141 260 N ATOM 703 CA LYS A 87 24.432 -34.470 6.724 1.00 16.17 C ANISOU 703 CA LYS A 87 2024 2389 1728 371 -91 20 C ATOM 704 C LYS A 87 23.900 -35.319 5.556 1.00 14.81 C ANISOU 704 C LYS A 87 1753 1949 1926 478 215 6 C ATOM 705 O LYS A 87 24.470 -35.302 4.465 1.00 15.62 O ANISOU 705 O LYS A 87 1716 2717 1501 327 198 121 O ATOM 706 CB LYS A 87 25.143 -35.340 7.764 1.00 16.79 C ANISOU 706 CB LYS A 87 2028 2308 2040 270 -111 -72 C ATOM 707 CG LYS A 87 26.282 -36.161 7.169 1.00 16.53 C ANISOU 707 CG LYS A 87 1789 2166 2325 187 -407 1 C ATOM 708 CD LYS A 87 26.834 -37.166 8.157 1.00 17.33 C ANISOU 708 CD LYS A 87 1865 2244 2474 52 -399 -224 C ATOM 709 CE LYS A 87 27.862 -38.068 7.483 1.00 18.19 C ANISOU 709 CE LYS A 87 2045 2134 2732 103 -374 -123 C ATOM 710 NZ LYS A 87 28.380 -39.108 8.411 1.00 18.35 N ANISOU 710 NZ LYS A 87 2234 2263 2474 -167 -488 20 N ATOM 711 N PRO A 88 22.817 -36.076 5.780 1.00 14.29 N ANISOU 711 N PRO A 88 1653 2068 1707 90 277 138 N ATOM 712 CA PRO A 88 22.229 -36.908 4.719 1.00 13.81 C ANISOU 712 CA PRO A 88 1439 1913 1894 171 199 257 C ATOM 713 C PRO A 88 21.753 -36.121 3.489 1.00 14.17 C ANISOU 713 C PRO A 88 1331 1806 2248 175 206 178 C ATOM 714 O PRO A 88 21.861 -36.603 2.358 1.00 13.35 O ANISOU 714 O PRO A 88 1292 1714 2066 237 165 216 O ATOM 715 CB PRO A 88 21.061 -37.612 5.418 1.00 17.85 C ANISOU 715 CB PRO A 88 2025 2415 2341 -25 411 17 C ATOM 716 CG PRO A 88 20.792 -36.801 6.633 1.00 15.14 C ANISOU 716 CG PRO A 88 1720 2257 1776 -180 375 -309 C ATOM 717 CD PRO A 88 22.103 -36.225 7.058 1.00 15.23 C ANISOU 717 CD PRO A 88 1953 2033 1798 -159 480 -102 C ATOM 718 N LEU A 89 21.236 -34.919 3.700 1.00 12.87 N ANISOU 718 N LEU A 89 1132 1720 2038 77 -13 187 N ATOM 719 C LEU A 89 22.033 -33.589 1.800 1.00 12.76 C ANISOU 719 C LEU A 89 1535 1582 1728 -11 -208 98 C ATOM 720 O LEU A 89 22.040 -33.610 0.568 1.00 13.05 O ANISOU 720 O LEU A 89 1702 1501 1756 -59 -432 -26 O ATOM 721 CA ALEU A 89 20.813 -34.054 2.605 0.50 13.92 C ANISOU 721 CA ALEU A 89 1359 1831 2098 126 -128 27 C ATOM 722 CB ALEU A 89 20.084 -32.842 3.186 0.50 14.69 C ANISOU 722 CB ALEU A 89 1682 1752 2147 128 -45 -65 C ATOM 723 CG ALEU A 89 19.242 -31.979 2.249 0.50 13.81 C ANISOU 723 CG ALEU A 89 1515 1872 1857 153 109 -34 C ATOM 724 CD1ALEU A 89 18.095 -32.790 1.664 0.50 15.70 C ANISOU 724 CD1ALEU A 89 1945 1876 2142 69 -7 -205 C ATOM 725 CD2ALEU A 89 18.710 -30.780 3.009 0.50 15.53 C ANISOU 725 CD2ALEU A 89 1752 1971 2177 194 43 -147 C ATOM 726 CA BLEU A 89 20.825 -34.085 2.579 0.50 13.50 C ANISOU 726 CA BLEU A 89 1280 1776 2072 101 -231 32 C ATOM 727 CB BLEU A 89 19.989 -32.908 3.058 0.50 14.63 C ANISOU 727 CB BLEU A 89 1698 1726 2134 120 -231 -97 C ATOM 728 CG BLEU A 89 18.529 -33.265 3.303 0.50 13.83 C ANISOU 728 CG BLEU A 89 1501 1869 1885 133 -310 78 C ATOM 729 CD1BLEU A 89 17.807 -32.056 3.857 0.50 15.48 C ANISOU 729 CD1BLEU A 89 1928 1831 2123 356 -183 -138 C ATOM 730 CD2BLEU A 89 17.862 -33.761 2.019 0.50 14.13 C ANISOU 730 CD2BLEU A 89 1511 2028 1829 43 -304 318 C ATOM 731 N ALA A 90 23.062 -33.148 2.508 1.00 11.75 N ANISOU 731 N ALA A 90 1349 1600 1516 -302 -314 50 N ATOM 732 CA ALA A 90 24.274 -32.722 1.835 1.00 13.85 C ANISOU 732 CA ALA A 90 1489 2157 1617 -288 -93 97 C ATOM 733 C ALA A 90 24.802 -33.880 1.002 1.00 12.68 C ANISOU 733 C ALA A 90 1271 1933 1614 -342 -225 257 C ATOM 734 O ALA A 90 25.202 -33.713 -0.148 1.00 14.58 O ANISOU 734 O ALA A 90 1777 2290 1472 -450 -196 127 O ATOM 735 CB ALA A 90 25.310 -32.289 2.853 1.00 14.87 C ANISOU 735 CB ALA A 90 1755 2128 1767 -613 -155 -57 C ATOM 736 N GLN A 91 24.802 -35.072 1.582 1.00 12.95 N ANISOU 736 N GLN A 91 1221 1823 1876 -98 -275 -21 N ATOM 737 CA GLN A 91 25.396 -36.202 0.888 1.00 13.04 C ANISOU 737 CA GLN A 91 1218 1985 1752 -120 -188 206 C ATOM 738 C GLN A 91 24.567 -36.671 -0.318 1.00 12.34 C ANISOU 738 C GLN A 91 931 1857 1901 -70 29 114 C ATOM 739 O GLN A 91 25.116 -37.002 -1.367 1.00 12.88 O ANISOU 739 O GLN A 91 1202 1680 2009 -4 194 72 O ATOM 740 CB GLN A 91 25.782 -37.305 1.868 1.00 14.86 C ANISOU 740 CB GLN A 91 1572 2143 1931 -167 -152 208 C ATOM 741 CG GLN A 91 26.821 -36.807 2.895 1.00 15.92 C ANISOU 741 CG GLN A 91 1603 2363 2082 -207 -89 197 C ATOM 742 CD GLN A 91 27.541 -37.915 3.631 1.00 17.24 C ANISOU 742 CD GLN A 91 1712 2363 2475 -470 -190 203 C ATOM 743 OE1 GLN A 91 26.953 -38.943 3.964 1.00 18.98 O ANISOU 743 OE1 GLN A 91 2067 2388 2753 -721 -7 499 O ATOM 744 NE2 GLN A 91 28.824 -37.702 3.905 1.00 16.24 N ANISOU 744 NE2 GLN A 91 1329 2335 2505 -296 -200 214 N ATOM 745 N SER A 92 23.244 -36.659 -0.196 1.00 11.84 N ANISOU 745 N SER A 92 917 1636 1946 -156 -62 98 N ATOM 746 C SER A 92 22.544 -35.975 -2.446 1.00 12.80 C ANISOU 746 C SER A 92 1210 1759 1892 20 -211 51 C ATOM 747 O SER A 92 22.555 -36.316 -3.628 1.00 12.04 O ANISOU 747 O SER A 92 1272 1524 1778 72 -73 -77 O ATOM 748 CA ASER A 92 22.422 -37.022 -1.340 0.50 11.14 C ANISOU 748 CA ASER A 92 870 1381 1982 7 86 113 C ATOM 749 CB ASER A 92 20.959 -37.219 -0.943 0.50 11.80 C ANISOU 749 CB ASER A 92 677 1697 2107 -48 258 216 C ATOM 750 OG ASER A 92 20.297 -35.975 -0.817 0.50 8.53 O ANISOU 750 OG ASER A 92 692 932 1614 191 170 -226 O ATOM 751 CA BSER A 92 22.376 -36.993 -1.314 0.50 13.49 C ANISOU 751 CA BSER A 92 1245 1764 2116 -115 -15 164 C ATOM 752 CB BSER A 92 20.925 -37.018 -0.831 0.50 16.61 C ANISOU 752 CB BSER A 92 1490 2386 2433 -224 29 317 C ATOM 753 OG BSER A 92 20.018 -36.893 -1.904 0.50 20.08 O ANISOU 753 OG BSER A 92 2263 2697 2666 -372 -166 245 O ATOM 754 N HIS A 93 22.673 -34.709 -2.071 1.00 11.52 N ANISOU 754 N HIS A 93 1236 1435 1703 4 -218 121 N ATOM 755 CA HIS A 93 22.786 -33.657 -3.067 1.00 11.42 C ANISOU 755 CA HIS A 93 1191 1527 1621 3 -15 -80 C ATOM 756 C HIS A 93 24.124 -33.617 -3.790 1.00 11.23 C ANISOU 756 C HIS A 93 1159 1513 1594 82 42 26 C ATOM 757 O HIS A 93 24.185 -33.280 -4.969 1.00 12.16 O ANISOU 757 O HIS A 93 1269 1660 1688 136 -98 -89 O ATOM 758 CB HIS A 93 22.332 -32.317 -2.504 1.00 10.99 C ANISOU 758 CB HIS A 93 998 1568 1610 89 103 -12 C ATOM 759 CG HIS A 93 20.843 -32.228 -2.382 1.00 10.84 C ANISOU 759 CG HIS A 93 920 1586 1611 -301 81 -23 C ATOM 760 ND1 HIS A 93 20.111 -33.051 -1.549 1.00 11.33 N ANISOU 760 ND1 HIS A 93 1133 1664 1507 -90 -33 200 N ATOM 761 CD2 HIS A 93 19.941 -31.470 -3.045 1.00 8.78 C ANISOU 761 CD2 HIS A 93 735 1228 1372 -115 14 84 C ATOM 762 CE1 HIS A 93 18.824 -32.784 -1.693 1.00 10.62 C ANISOU 762 CE1 HIS A 93 1164 1480 1390 -86 -100 96 C ATOM 763 NE2 HIS A 93 18.693 -31.826 -2.593 1.00 8.85 N ANISOU 763 NE2 HIS A 93 1025 1048 1291 -158 -38 18 N ATOM 764 N ALA A 94 25.191 -34.007 -3.096 1.00 10.85 N ANISOU 764 N ALA A 94 986 1486 1649 29 57 -70 N ATOM 765 CA ALA A 94 26.497 -34.113 -3.735 1.00 12.00 C ANISOU 765 CA ALA A 94 1445 1370 1743 87 80 -167 C ATOM 766 C ALA A 94 26.625 -35.385 -4.570 1.00 12.18 C ANISOU 766 C ALA A 94 1559 1390 1678 55 -2 -14 C ATOM 767 O ALA A 94 27.038 -35.340 -5.726 1.00 15.66 O ANISOU 767 O ALA A 94 2465 1629 1854 4 455 -76 O ATOM 768 CB ALA A 94 27.599 -34.082 -2.683 1.00 11.58 C ANISOU 768 CB ALA A 94 1019 1839 1540 168 -159 -215 C ATOM 769 N THR A 95 26.257 -36.523 -3.994 1.00 12.72 N ANISOU 769 N THR A 95 1552 1361 1917 47 -105 -104 N ATOM 770 C THR A 95 25.542 -38.290 -5.606 1.00 15.80 C ANISOU 770 C THR A 95 1891 1856 2253 125 38 -230 C ATOM 771 O THR A 95 25.888 -38.854 -6.647 1.00 18.32 O ANISOU 771 O THR A 95 2267 2447 2246 52 -30 -561 O ATOM 772 CA ATHR A 95 26.586 -37.797 -4.617 0.50 15.30 C ANISOU 772 CA ATHR A 95 1912 1794 2104 150 27 -206 C ATOM 773 CB ATHR A 95 26.902 -38.885 -3.574 0.50 15.74 C ANISOU 773 CB ATHR A 95 1948 1826 2203 221 24 -77 C ATOM 774 OG1ATHR A 95 27.879 -38.391 -2.647 0.50 18.49 O ANISOU 774 OG1ATHR A 95 2135 2476 2412 182 -7 -98 O ATOM 775 CG2ATHR A 95 27.445 -40.129 -4.256 0.50 18.01 C ANISOU 775 CG2ATHR A 95 2258 2089 2494 210 133 -174 C ATOM 776 CA BTHR A 95 26.573 -37.818 -4.596 0.50 14.11 C ANISOU 776 CA BTHR A 95 1778 1619 1961 137 -12 -202 C ATOM 777 CB BTHR A 95 26.769 -38.918 -3.525 0.50 12.88 C ANISOU 777 CB BTHR A 95 1572 1417 1904 205 -84 -30 C ATOM 778 OG1BTHR A 95 25.517 -39.208 -2.886 0.50 12.37 O ANISOU 778 OG1BTHR A 95 1646 1197 1856 -32 -36 -240 O ATOM 779 CG2BTHR A 95 27.789 -38.473 -2.477 0.50 15.47 C ANISOU 779 CG2BTHR A 95 1841 2051 1984 161 -147 -95 C ATOM 780 N LYS A 96 24.271 -38.078 -5.294 1.00 14.89 N ANISOU 780 N LYS A 96 1670 1713 2271 99 -220 -241 N ATOM 781 CA LYS A 96 23.219 -38.556 -6.178 1.00 15.83 C ANISOU 781 CA LYS A 96 1842 1856 2316 94 -198 -220 C ATOM 782 C LYS A 96 22.734 -37.477 -7.142 1.00 14.36 C ANISOU 782 C LYS A 96 1847 1672 1935 109 -110 -259 C ATOM 783 O LYS A 96 22.711 -37.685 -8.358 1.00 17.33 O ANISOU 783 O LYS A 96 2403 2018 2161 209 -283 -608 O ATOM 784 CB LYS A 96 22.050 -39.131 -5.377 1.00 17.68 C ANISOU 784 CB LYS A 96 1953 1984 2779 -209 -343 7 C ATOM 785 CG LYS A 96 20.991 -39.769 -6.260 1.00 21.32 C ANISOU 785 CG LYS A 96 2391 2575 3133 -158 -390 144 C ATOM 786 CD LYS A 96 20.013 -40.615 -5.474 1.00 23.96 C ANISOU 786 CD LYS A 96 2875 3099 3131 -111 -511 250 C ATOM 787 CE LYS A 96 19.300 -41.570 -6.409 1.00 25.22 C ANISOU 787 CE LYS A 96 3221 3300 3061 -229 -594 352 C ATOM 788 NZ LYS A 96 18.913 -40.879 -7.674 1.00 27.83 N ANISOU 788 NZ LYS A 96 3502 3636 3433 -148 -617 536 N ATOM 789 N HIS A 97 22.360 -36.317 -6.608 1.00 13.11 N ANISOU 789 N HIS A 97 1576 1593 1811 -78 -40 -180 N ATOM 790 CA HIS A 97 21.728 -35.295 -7.430 1.00 12.71 C ANISOU 790 CA HIS A 97 1541 1572 1714 -66 -41 -49 C ATOM 791 C HIS A 97 22.721 -34.393 -8.145 1.00 14.13 C ANISOU 791 C HIS A 97 1713 1879 1774 -112 38 -9 C ATOM 792 O HIS A 97 22.375 -33.751 -9.134 1.00 14.78 O ANISOU 792 O HIS A 97 1759 2033 1821 -158 -37 115 O ATOM 793 CB HIS A 97 20.729 -34.464 -6.622 1.00 13.19 C ANISOU 793 CB HIS A 97 1490 1893 1626 -177 154 -127 C ATOM 794 CG HIS A 97 19.740 -35.288 -5.857 1.00 12.50 C ANISOU 794 CG HIS A 97 1434 1597 1717 -224 -49 -97 C ATOM 795 ND1 HIS A 97 19.045 -36.336 -6.422 1.00 14.96 N ANISOU 795 ND1 HIS A 97 1778 1838 2066 -277 -125 -114 N ATOM 796 CD2 HIS A 97 19.325 -35.211 -4.570 1.00 13.68 C ANISOU 796 CD2 HIS A 97 1674 1641 1881 123 -34 -60 C ATOM 797 CE1 HIS A 97 18.251 -36.873 -5.514 1.00 14.95 C ANISOU 797 CE1 HIS A 97 1745 2065 1869 -66 -57 -47 C ATOM 798 NE2 HIS A 97 18.404 -36.211 -4.381 1.00 14.09 N ANISOU 798 NE2 HIS A 97 1481 1916 1955 -187 -330 0 N ATOM 799 N LYS A 98 23.944 -34.330 -7.623 1.00 13.06 N ANISOU 799 N LYS A 98 1457 1760 1743 83 164 -189 N ATOM 800 CA LYS A 98 25.017 -33.523 -8.221 1.00 13.18 C ANISOU 800 CA LYS A 98 1606 1798 1601 -68 286 133 C ATOM 801 C LYS A 98 24.656 -32.040 -8.268 1.00 12.91 C ANISOU 801 C LYS A 98 1511 1774 1618 137 12 43 C ATOM 802 O LYS A 98 24.769 -31.401 -9.310 1.00 13.87 O ANISOU 802 O LYS A 98 1686 1912 1671 133 -75 84 O ATOM 803 CB LYS A 98 25.358 -34.003 -9.636 1.00 17.15 C ANISOU 803 CB LYS A 98 2245 2176 2096 204 384 72 C ATOM 804 CG LYS A 98 25.493 -35.502 -9.790 1.00 22.93 C ANISOU 804 CG LYS A 98 2998 2810 2904 43 676 16 C ATOM 805 CD LYS A 98 26.601 -36.058 -8.926 1.00 26.31 C ANISOU 805 CD LYS A 98 3428 3295 3270 16 373 48 C ATOM 806 CE LYS A 98 26.970 -37.469 -9.370 1.00 29.27 C ANISOU 806 CE LYS A 98 3803 3622 3696 73 368 104 C ATOM 807 NZ LYS A 98 27.894 -38.132 -8.411 1.00 31.55 N ANISOU 807 NZ LYS A 98 3860 3953 4172 129 319 371 N ATOM 808 N ILE A 99 24.233 -31.494 -7.133 1.00 12.55 N ANISOU 808 N ILE A 99 1513 1708 1548 321 -30 46 N ATOM 809 CA ILE A 99 23.799 -30.102 -7.072 1.00 12.12 C ANISOU 809 CA ILE A 99 1551 1539 1515 137 57 35 C ATOM 810 C ILE A 99 24.936 -29.209 -6.578 1.00 12.32 C ANISOU 810 C ILE A 99 1386 1782 1513 91 56 9 C ATOM 811 O ILE A 99 25.292 -29.240 -5.403 1.00 12.86 O ANISOU 811 O ILE A 99 1526 1770 1587 19 -193 155 O ATOM 812 CB ILE A 99 22.596 -29.944 -6.122 1.00 11.93 C ANISOU 812 CB ILE A 99 1524 1531 1476 152 -39 145 C ATOM 813 CG1 ILE A 99 21.471 -30.911 -6.507 1.00 12.51 C ANISOU 813 CG1 ILE A 99 1592 1584 1576 83 -173 41 C ATOM 814 CG2 ILE A 99 22.103 -28.497 -6.110 1.00 12.47 C ANISOU 814 CG2 ILE A 99 1337 1438 1963 97 -12 155 C ATOM 815 CD1 ILE A 99 21.039 -30.821 -7.959 1.00 13.16 C ANISOU 815 CD1 ILE A 99 1512 1794 1693 6 -113 62 C ATOM 816 N PRO A 100 25.535 -28.420 -7.479 1.00 12.32 N ANISOU 816 N PRO A 100 1362 2040 1278 24 -125 -101 N ATOM 817 CA PRO A 100 26.603 -27.544 -7.010 1.00 12.64 C ANISOU 817 CA PRO A 100 1415 1912 1476 63 88 -124 C ATOM 818 C PRO A 100 26.102 -26.559 -5.960 1.00 12.18 C ANISOU 818 C PRO A 100 1442 1700 1485 232 76 130 C ATOM 819 O PRO A 100 24.931 -26.161 -5.975 1.00 12.36 O ANISOU 819 O PRO A 100 1299 1608 1787 232 0 -83 O ATOM 820 CB PRO A 100 27.059 -26.810 -8.279 1.00 13.45 C ANISOU 820 CB PRO A 100 1520 2058 1531 -300 154 -137 C ATOM 821 CG PRO A 100 26.009 -27.038 -9.284 1.00 17.15 C ANISOU 821 CG PRO A 100 2082 2432 2002 -299 -359 70 C ATOM 822 CD PRO A 100 25.277 -28.287 -8.922 1.00 13.05 C ANISOU 822 CD PRO A 100 1501 1907 1550 -139 -118 157 C ATOM 823 N ILE A 101 26.993 -26.156 -5.063 1.00 12.24 N ANISOU 823 N ILE A 101 1500 1688 1461 203 24 -44 N ATOM 824 CA ILE A 101 26.619 -25.248 -3.990 1.00 12.26 C ANISOU 824 CA ILE A 101 1384 1792 1482 55 -46 -46 C ATOM 825 C ILE A 101 26.047 -23.937 -4.530 1.00 11.66 C ANISOU 825 C ILE A 101 1286 1687 1456 21 -36 -15 C ATOM 826 O ILE A 101 25.194 -23.320 -3.902 1.00 12.11 O ANISOU 826 O ILE A 101 1096 1825 1679 -43 -2 -106 O ATOM 827 CB ILE A 101 27.785 -25.015 -3.001 1.00 14.36 C ANISOU 827 CB ILE A 101 1692 2176 1589 31 -14 3 C ATOM 828 CG1 ILE A 101 27.296 -24.360 -1.712 1.00 17.17 C ANISOU 828 CG1 ILE A 101 2248 2536 1737 -115 74 -132 C ATOM 829 CG2 ILE A 101 28.939 -24.283 -3.653 1.00 16.07 C ANISOU 829 CG2 ILE A 101 1802 2405 1898 -57 -254 276 C ATOM 830 CD1 ILE A 101 26.726 -25.357 -0.726 1.00 19.92 C ANISOU 830 CD1 ILE A 101 2505 2659 2402 0 273 -130 C ATOM 831 N LYS A 102 26.498 -23.535 -5.715 1.00 12.20 N ANISOU 831 N LYS A 102 1397 1689 1551 99 -62 142 N ATOM 832 CA LYS A 102 25.945 -22.361 -6.382 1.00 12.02 C ANISOU 832 CA LYS A 102 1279 1582 1704 -19 30 5 C ATOM 833 C LYS A 102 24.427 -22.437 -6.481 1.00 11.13 C ANISOU 833 C LYS A 102 1227 1562 1436 4 -93 -210 C ATOM 834 O LYS A 102 23.739 -21.427 -6.335 1.00 11.45 O ANISOU 834 O LYS A 102 1179 1569 1600 30 29 -43 O ATOM 835 CB LYS A 102 26.542 -22.214 -7.790 1.00 12.14 C ANISOU 835 CB LYS A 102 1346 1722 1542 -83 115 42 C ATOM 836 CG LYS A 102 26.212 -20.888 -8.453 1.00 16.96 C ANISOU 836 CG LYS A 102 2058 2634 1749 -322 -15 -300 C ATOM 837 CD LYS A 102 27.020 -19.784 -7.804 1.00 20.74 C ANISOU 837 CD LYS A 102 3444 2650 1785 -342 -314 -703 C ATOM 838 CE LYS A 102 26.724 -18.424 -8.395 1.00 21.26 C ANISOU 838 CE LYS A 102 3494 2708 1875 -644 -410 -845 C ATOM 839 NZ LYS A 102 27.408 -17.384 -7.586 1.00 20.35 N ANISOU 839 NZ LYS A 102 3248 3083 1400 -1029 -530 -1032 N ATOM 840 N TYR A 103 23.906 -23.624 -6.770 1.00 11.29 N ANISOU 840 N TYR A 103 1161 1614 1514 40 -66 -109 N ATOM 841 CA TYR A 103 22.455 -23.760 -6.909 1.00 11.34 C ANISOU 841 CA TYR A 103 1027 1662 1616 -89 22 -84 C ATOM 842 C TYR A 103 21.743 -23.597 -5.560 1.00 10.52 C ANISOU 842 C TYR A 103 1141 1292 1564 96 21 54 C ATOM 843 O TYR A 103 20.588 -23.164 -5.514 1.00 11.39 O ANISOU 843 O TYR A 103 1200 1499 1625 -48 -68 -35 O ATOM 844 CB TYR A 103 22.056 -25.085 -7.575 1.00 12.66 C ANISOU 844 CB TYR A 103 1499 1795 1516 -20 161 44 C ATOM 845 CG TYR A 103 22.513 -25.262 -9.016 1.00 11.50 C ANISOU 845 CG TYR A 103 1195 1737 1438 85 146 143 C ATOM 846 CD1 TYR A 103 23.314 -24.315 -9.648 1.00 14.01 C ANISOU 846 CD1 TYR A 103 1492 2350 1478 -19 -73 136 C ATOM 847 CD2 TYR A 103 22.174 -26.407 -9.724 1.00 12.72 C ANISOU 847 CD2 TYR A 103 1450 2028 1353 158 42 44 C ATOM 848 CE1 TYR A 103 23.744 -24.504 -10.962 1.00 14.57 C ANISOU 848 CE1 TYR A 103 1637 2220 1679 2 140 -113 C ATOM 849 CE2 TYR A 103 22.599 -26.607 -11.024 1.00 13.80 C ANISOU 849 CE2 TYR A 103 1553 2096 1593 395 93 119 C ATOM 850 CZ TYR A 103 23.382 -25.656 -11.644 1.00 13.33 C ANISOU 850 CZ TYR A 103 1504 2073 1485 142 224 88 C ATOM 851 OH TYR A 103 23.815 -25.862 -12.944 1.00 15.40 O ANISOU 851 OH TYR A 103 1872 2307 1672 28 314 132 O ATOM 852 N LEU A 104 22.426 -23.950 -4.469 1.00 10.24 N ANISOU 852 N LEU A 104 1169 1351 1370 -38 23 -68 N ATOM 853 C LEU A 104 21.885 -22.252 -2.781 1.00 9.87 C ANISOU 853 C LEU A 104 1084 1332 1331 -112 41 112 C ATOM 854 O LEU A 104 20.998 -21.765 -2.077 1.00 11.10 O ANISOU 854 O LEU A 104 1256 1378 1583 2 19 -219 O ATOM 855 CA ALEU A 104 21.878 -23.736 -3.133 0.50 10.30 C ANISOU 855 CA ALEU A 104 1134 1321 1459 69 -38 66 C ATOM 856 CB ALEU A 104 22.635 -24.557 -2.087 0.50 12.37 C ANISOU 856 CB ALEU A 104 1356 1570 1773 -27 -63 91 C ATOM 857 CG ALEU A 104 22.626 -26.069 -2.325 0.50 13.53 C ANISOU 857 CG ALEU A 104 1193 1853 2093 20 -50 63 C ATOM 858 CD1ALEU A 104 21.205 -26.612 -2.391 0.50 10.79 C ANISOU 858 CD1ALEU A 104 974 1459 1665 55 10 47 C ATOM 859 CD2ALEU A 104 23.385 -26.390 -3.597 0.50 17.06 C ANISOU 859 CD2ALEU A 104 2123 2015 2340 112 -232 -33 C ATOM 860 CA BLEU A 104 21.885 -23.739 -3.130 0.50 9.82 C ANISOU 860 CA BLEU A 104 1058 1236 1435 59 -50 122 C ATOM 861 CB BLEU A 104 22.657 -24.565 -2.094 0.50 11.14 C ANISOU 861 CB BLEU A 104 1175 1340 1715 -81 -87 234 C ATOM 862 CG BLEU A 104 22.336 -26.065 -2.098 0.50 11.06 C ANISOU 862 CG BLEU A 104 841 1383 1978 -56 -80 344 C ATOM 863 CD1BLEU A 104 23.367 -26.865 -1.321 0.50 9.79 C ANISOU 863 CD1BLEU A 104 945 1174 1598 -137 -215 483 C ATOM 864 CD2BLEU A 104 20.946 -26.317 -1.546 0.50 12.42 C ANISOU 864 CD2BLEU A 104 1113 1512 2095 -122 -11 390 C ATOM 865 N GLU A 105 22.877 -21.528 -3.289 1.00 10.75 N ANISOU 865 N GLU A 105 1410 1209 1463 -72 -107 73 N ATOM 866 CA GLU A 105 22.863 -20.078 -3.191 1.00 10.42 C ANISOU 866 CA GLU A 105 1147 1379 1431 -50 -227 137 C ATOM 867 C GLU A 105 21.640 -19.534 -3.955 1.00 10.87 C ANISOU 867 C GLU A 105 1257 1329 1542 -43 -186 -105 C ATOM 868 O GLU A 105 20.886 -18.698 -3.440 1.00 11.18 O ANISOU 868 O GLU A 105 1290 1282 1675 -55 -7 -40 O ATOM 869 CB GLU A 105 24.146 -19.502 -3.785 1.00 11.55 C ANISOU 869 CB GLU A 105 1210 1494 1682 -79 -163 149 C ATOM 870 CG GLU A 105 24.221 -18.000 -3.703 1.00 13.22 C ANISOU 870 CG GLU A 105 1557 1528 1939 -174 -357 187 C ATOM 871 CD GLU A 105 25.351 -17.432 -4.543 1.00 13.70 C ANISOU 871 CD GLU A 105 1816 1795 1594 55 -179 97 C ATOM 872 OE1 GLU A 105 26.137 -18.223 -5.114 1.00 14.87 O ANISOU 872 OE1 GLU A 105 1845 2174 1630 -153 -177 42 O ATOM 873 OE2 GLU A 105 25.449 -16.193 -4.638 1.00 16.20 O ANISOU 873 OE2 GLU A 105 2372 1826 1955 -205 -146 -393 O ATOM 874 N PHE A 106 21.437 -20.009 -5.184 1.00 10.39 N ANISOU 874 N PHE A 106 1312 1354 1281 -61 -103 29 N ATOM 875 CA PHE A 106 20.295 -19.560 -5.992 1.00 10.33 C ANISOU 875 CA PHE A 106 1154 1522 1247 -13 -74 31 C ATOM 876 C PHE A 106 18.973 -19.788 -5.241 1.00 9.94 C ANISOU 876 C PHE A 106 1233 1140 1402 -70 -29 -61 C ATOM 877 O PHE A 106 18.113 -18.910 -5.203 1.00 10.44 O ANISOU 877 O PHE A 106 1197 1265 1501 109 -63 -155 O ATOM 878 CB PHE A 106 20.207 -20.306 -7.333 1.00 10.48 C ANISOU 878 CB PHE A 106 1305 1553 1121 -125 200 -39 C ATOM 879 CG PHE A 106 21.332 -20.018 -8.301 1.00 11.54 C ANISOU 879 CG PHE A 106 1347 1486 1553 14 -34 -8 C ATOM 880 CD1 PHE A 106 22.071 -18.850 -8.231 1.00 12.23 C ANISOU 880 CD1 PHE A 106 1327 1761 1559 24 106 -20 C ATOM 881 CD2 PHE A 106 21.607 -20.918 -9.321 1.00 12.39 C ANISOU 881 CD2 PHE A 106 1360 1803 1542 172 84 113 C ATOM 882 CE1 PHE A 106 23.083 -18.600 -9.151 1.00 13.75 C ANISOU 882 CE1 PHE A 106 1663 1960 1601 -104 -24 -87 C ATOM 883 CE2 PHE A 106 22.617 -20.675 -10.241 1.00 12.93 C ANISOU 883 CE2 PHE A 106 1588 1916 1410 -83 -69 -75 C ATOM 884 CZ PHE A 106 23.350 -19.515 -10.155 1.00 14.12 C ANISOU 884 CZ PHE A 106 1602 2067 1695 -137 33 43 C ATOM 885 N ILE A 107 18.791 -20.971 -4.662 1.00 10.10 N ANISOU 885 N ILE A 107 1240 1278 1316 -77 60 -5 N ATOM 886 CA ILE A 107 17.506 -21.262 -4.028 1.00 11.00 C ANISOU 886 CA ILE A 107 1264 1507 1407 88 86 80 C ATOM 887 C ILE A 107 17.325 -20.467 -2.734 1.00 10.84 C ANISOU 887 C ILE A 107 1309 1300 1508 100 127 -53 C ATOM 888 O ILE A 107 16.207 -20.098 -2.368 1.00 11.48 O ANISOU 888 O ILE A 107 1143 1551 1667 192 115 14 O ATOM 889 CB ILE A 107 17.262 -22.778 -3.828 1.00 10.24 C ANISOU 889 CB ILE A 107 1065 1348 1478 71 69 56 C ATOM 890 CG1 ILE A 107 15.762 -23.072 -3.717 1.00 10.78 C ANISOU 890 CG1 ILE A 107 1139 1339 1617 -18 -70 71 C ATOM 891 CG2 ILE A 107 17.993 -23.311 -2.582 1.00 11.15 C ANISOU 891 CG2 ILE A 107 1179 1456 1600 -8 -144 -16 C ATOM 892 CD1 ILE A 107 15.429 -24.552 -3.615 1.00 11.44 C ANISOU 892 CD1 ILE A 107 1416 1277 1651 -19 -202 106 C ATOM 893 N SER A 108 18.431 -20.178 -2.055 1.00 11.29 N ANISOU 893 N SER A 108 1281 1587 1419 32 8 -91 N ATOM 894 CA SER A 108 18.388 -19.346 -0.851 1.00 11.89 C ANISOU 894 CA SER A 108 1393 1630 1492 107 -61 -85 C ATOM 895 C SER A 108 17.887 -17.951 -1.214 1.00 11.83 C ANISOU 895 C SER A 108 1241 1692 1560 103 -34 -122 C ATOM 896 O SER A 108 17.010 -17.389 -0.551 1.00 12.35 O ANISOU 896 O SER A 108 1399 1519 1773 -21 16 -317 O ATOM 897 CB SER A 108 19.773 -19.255 -0.200 1.00 13.29 C ANISOU 897 CB SER A 108 1515 1802 1732 169 -288 34 C ATOM 898 OG SER A 108 20.204 -20.509 0.310 1.00 13.17 O ANISOU 898 OG SER A 108 1529 1916 1558 47 71 113 O ATOM 899 N ASP A 109 18.457 -17.398 -2.279 1.00 11.83 N ANISOU 899 N ASP A 109 1379 1389 1724 70 -8 -78 N ATOM 900 CA ASP A 109 18.027 -16.106 -2.791 1.00 11.99 C ANISOU 900 CA ASP A 109 1280 1487 1788 2 -44 -69 C ATOM 901 C ASP A 109 16.562 -16.133 -3.218 1.00 10.69 C ANISOU 901 C ASP A 109 1166 1427 1467 53 -122 -200 C ATOM 902 O ASP A 109 15.821 -15.177 -2.978 1.00 11.25 O ANISOU 902 O ASP A 109 1289 1316 1667 105 -34 -111 O ATOM 903 CB ASP A 109 18.916 -15.682 -3.960 1.00 12.53 C ANISOU 903 CB ASP A 109 1252 1617 1890 -80 83 148 C ATOM 904 CG ASP A 109 20.284 -15.200 -3.510 1.00 15.55 C ANISOU 904 CG ASP A 109 1865 1907 2136 -129 -155 243 C ATOM 905 OD1 ASP A 109 20.475 -14.983 -2.298 1.00 18.94 O ANISOU 905 OD1 ASP A 109 2075 2702 2419 -472 -345 325 O ATOM 906 OD2 ASP A 109 21.166 -15.029 -4.376 1.00 17.41 O ANISOU 906 OD2 ASP A 109 1821 2182 2609 -306 -72 231 O ATOM 907 N ALA A 110 16.150 -17.224 -3.855 1.00 11.26 N ANISOU 907 N ALA A 110 1239 1436 1603 45 55 -37 N ATOM 908 CA ALA A 110 14.757 -17.385 -4.256 1.00 10.32 C ANISOU 908 CA ALA A 110 1331 1288 1300 -78 -72 -178 C ATOM 909 C ALA A 110 13.796 -17.351 -3.067 1.00 10.44 C ANISOU 909 C ALA A 110 1390 1210 1365 42 -34 -97 C ATOM 910 O ALA A 110 12.719 -16.769 -3.150 1.00 11.67 O ANISOU 910 O ALA A 110 1346 1412 1673 124 39 -4 O ATOM 911 CB ALA A 110 14.573 -18.665 -5.047 1.00 11.58 C ANISOU 911 CB ALA A 110 1403 1371 1622 -135 148 -198 C ATOM 912 N ILE A 111 14.190 -17.967 -1.959 1.00 10.26 N ANISOU 912 N ILE A 111 1265 1351 1281 -111 -34 -114 N ATOM 913 CA ILE A 111 13.358 -17.960 -0.763 1.00 10.20 C ANISOU 913 CA ILE A 111 1295 1240 1339 31 -157 -145 C ATOM 914 C ILE A 111 13.147 -16.540 -0.254 1.00 10.05 C ANISOU 914 C ILE A 111 1172 1246 1399 28 -86 10 C ATOM 915 O ILE A 111 12.026 -16.152 0.073 1.00 11.11 O ANISOU 915 O ILE A 111 1131 1516 1572 96 89 -140 O ATOM 916 CB ILE A 111 13.953 -18.863 0.330 1.00 10.18 C ANISOU 916 CB ILE A 111 1325 1330 1211 17 -251 151 C ATOM 917 CG1 ILE A 111 13.805 -20.328 -0.091 1.00 10.52 C ANISOU 917 CG1 ILE A 111 1128 1328 1539 53 -258 28 C ATOM 918 CG2 ILE A 111 13.287 -18.613 1.674 1.00 11.49 C ANISOU 918 CG2 ILE A 111 1356 1570 1440 -167 -55 -17 C ATOM 919 CD1 ILE A 111 14.673 -21.303 0.682 1.00 11.23 C ANISOU 919 CD1 ILE A 111 1333 1179 1754 -8 -516 70 C ATOM 920 N ILE A 112 14.221 -15.755 -0.193 1.00 10.93 N ANISOU 920 N ILE A 112 1182 1470 1500 -111 -38 83 N ATOM 921 CA ILE A 112 14.101 -14.364 0.236 1.00 10.75 C ANISOU 921 CA ILE A 112 1177 1458 1449 48 -204 87 C ATOM 922 C ILE A 112 13.201 -13.582 -0.717 1.00 10.48 C ANISOU 922 C ILE A 112 1230 1475 1275 10 59 -42 C ATOM 923 O ILE A 112 12.335 -12.810 -0.286 1.00 11.28 O ANISOU 923 O ILE A 112 1237 1650 1396 119 -8 -71 O ATOM 924 CB ILE A 112 15.492 -13.696 0.366 1.00 10.59 C ANISOU 924 CB ILE A 112 1240 1428 1355 162 -60 213 C ATOM 925 CG1 ILE A 112 16.314 -14.376 1.471 1.00 10.82 C ANISOU 925 CG1 ILE A 112 1320 1596 1194 266 31 21 C ATOM 926 CG2 ILE A 112 15.366 -12.198 0.596 1.00 11.01 C ANISOU 926 CG2 ILE A 112 1443 1392 1346 228 -55 -16 C ATOM 927 CD1 ILE A 112 15.704 -14.273 2.862 1.00 11.56 C ANISOU 927 CD1 ILE A 112 1433 1884 1073 154 285 3 C ATOM 928 N HIS A 113 13.375 -13.804 -2.016 1.00 10.90 N ANISOU 928 N HIS A 113 1256 1565 1318 85 -111 110 N ATOM 929 CA HIS A 113 12.537 -13.124 -2.987 1.00 11.24 C ANISOU 929 CA HIS A 113 1080 1726 1464 6 70 -6 C ATOM 930 C HIS A 113 11.059 -13.472 -2.819 1.00 10.77 C ANISOU 930 C HIS A 113 1268 1468 1356 69 -91 23 C ATOM 931 O HIS A 113 10.196 -12.589 -2.832 1.00 11.26 O ANISOU 931 O HIS A 113 1184 1432 1661 4 -22 105 O ATOM 932 CB HIS A 113 12.973 -13.437 -4.414 1.00 11.36 C ANISOU 932 CB HIS A 113 1453 1682 1182 11 -136 -48 C ATOM 933 CG HIS A 113 12.089 -12.808 -5.440 1.00 14.16 C ANISOU 933 CG HIS A 113 2233 1879 1268 41 55 -275 C ATOM 934 ND1 HIS A 113 12.272 -11.519 -5.889 1.00 18.35 N ANISOU 934 ND1 HIS A 113 3198 2066 1706 239 -339 -323 N ATOM 935 CD2 HIS A 113 10.988 -13.276 -6.073 1.00 16.40 C ANISOU 935 CD2 HIS A 113 2282 2328 1621 245 -137 -298 C ATOM 936 CE1 HIS A 113 11.332 -11.225 -6.770 1.00 19.39 C ANISOU 936 CE1 HIS A 113 3015 2385 1965 353 -379 -428 C ATOM 937 NE2 HIS A 113 10.541 -12.275 -6.900 1.00 19.42 N ANISOU 937 NE2 HIS A 113 2797 2472 2107 406 -210 -102 N ATOM 938 N VAL A 114 10.772 -14.762 -2.683 1.00 11.03 N ANISOU 938 N VAL A 114 1078 1493 1621 52 12 -76 N ATOM 939 CA VAL A 114 9.396 -15.221 -2.559 1.00 11.20 C ANISOU 939 CA VAL A 114 1344 1442 1468 75 2 149 C ATOM 940 C VAL A 114 8.738 -14.683 -1.287 1.00 11.01 C ANISOU 940 C VAL A 114 1242 1547 1393 116 15 0 C ATOM 941 O VAL A 114 7.562 -14.307 -1.293 1.00 11.43 O ANISOU 941 O VAL A 114 1111 1604 1627 116 54 -46 O ATOM 942 CB VAL A 114 9.309 -16.756 -2.640 1.00 10.94 C ANISOU 942 CB VAL A 114 1273 1309 1574 26 14 -23 C ATOM 943 CG1 VAL A 114 7.904 -17.238 -2.259 1.00 12.02 C ANISOU 943 CG1 VAL A 114 1413 1385 1769 -42 59 135 C ATOM 944 CG2 VAL A 114 9.662 -17.209 -4.052 1.00 12.52 C ANISOU 944 CG2 VAL A 114 1409 1686 1660 64 55 61 C ATOM 945 N LEU A 115 9.499 -14.607 -0.200 1.00 10.92 N ANISOU 945 N LEU A 115 1189 1632 1327 -43 35 81 N ATOM 946 CA LEU A 115 8.938 -14.067 1.031 1.00 10.67 C ANISOU 946 CA LEU A 115 1134 1586 1333 120 118 64 C ATOM 947 C LEU A 115 8.496 -12.614 0.829 1.00 10.68 C ANISOU 947 C LEU A 115 907 1616 1534 -97 -126 -6 C ATOM 948 O LEU A 115 7.402 -12.221 1.230 1.00 11.38 O ANISOU 948 O LEU A 115 1039 1491 1794 35 -92 -86 O ATOM 949 CB LEU A 115 9.915 -14.214 2.199 1.00 12.13 C ANISOU 949 CB LEU A 115 1360 1656 1592 -143 -48 98 C ATOM 950 CG LEU A 115 10.075 -15.648 2.709 1.00 11.45 C ANISOU 950 CG LEU A 115 1390 1536 1422 -141 -23 324 C ATOM 951 CD1 LEU A 115 11.311 -15.774 3.586 1.00 12.69 C ANISOU 951 CD1 LEU A 115 1443 1910 1469 -163 -65 187 C ATOM 952 CD2 LEU A 115 8.832 -16.077 3.467 1.00 13.57 C ANISOU 952 CD2 LEU A 115 1536 2039 1580 -109 -143 280 C ATOM 953 N HIS A 116 9.339 -11.810 0.192 1.00 10.44 N ANISOU 953 N HIS A 116 1134 1596 1236 -56 -227 120 N ATOM 954 CA HIS A 116 8.934 -10.439 -0.114 1.00 10.75 C ANISOU 954 CA HIS A 116 1266 1522 1295 35 -131 236 C ATOM 955 C HIS A 116 7.775 -10.362 -1.105 1.00 10.53 C ANISOU 955 C HIS A 116 1348 1277 1373 35 -62 13 C ATOM 956 O HIS A 116 6.884 -9.512 -0.978 1.00 11.74 O ANISOU 956 O HIS A 116 1253 1429 1779 161 -20 -154 O ATOM 957 CB HIS A 116 10.119 -9.653 -0.669 1.00 11.01 C ANISOU 957 CB HIS A 116 1347 1511 1324 -79 -94 106 C ATOM 958 CG HIS A 116 11.048 -9.140 0.382 1.00 10.35 C ANISOU 958 CG HIS A 116 1308 1277 1346 -50 50 45 C ATOM 959 ND1 HIS A 116 10.656 -8.240 1.348 1.00 10.17 N ANISOU 959 ND1 HIS A 116 1284 1243 1336 34 -78 130 N ATOM 960 CD2 HIS A 116 12.362 -9.379 0.598 1.00 10.40 C ANISOU 960 CD2 HIS A 116 1297 1324 1328 12 95 3 C ATOM 961 CE1 HIS A 116 11.687 -7.960 2.127 1.00 10.18 C ANISOU 961 CE1 HIS A 116 1223 1200 1443 61 -29 -171 C ATOM 962 NE2 HIS A 116 12.734 -8.642 1.695 1.00 9.35 N ANISOU 962 NE2 HIS A 116 1367 952 1233 59 78 3 N ATOM 963 N SER A 117 7.786 -11.234 -2.106 1.00 10.78 N ANISOU 963 N SER A 117 1155 1594 1344 -108 -85 127 N ATOM 964 CA SER A 117 6.762 -11.185 -3.140 1.00 11.55 C ANISOU 964 CA SER A 117 1184 1815 1388 136 -63 169 C ATOM 965 C SER A 117 5.388 -11.570 -2.601 1.00 11.06 C ANISOU 965 C SER A 117 1171 1407 1621 -58 7 -5 C ATOM 966 O SER A 117 4.372 -10.987 -2.986 1.00 12.29 O ANISOU 966 O SER A 117 1204 1659 1806 -33 -97 108 O ATOM 967 CB SER A 117 7.140 -12.097 -4.302 1.00 11.98 C ANISOU 967 CB SER A 117 1188 1828 1533 -22 -178 -137 C ATOM 968 OG SER A 117 6.156 -12.024 -5.315 1.00 15.51 O ANISOU 968 OG SER A 117 1757 2319 1814 -177 -245 153 O ATOM 969 N LYS A 118 5.359 -12.554 -1.710 1.00 10.76 N ANISOU 969 N LYS A 118 1083 1766 1238 -1 7 -3 N ATOM 970 CA LYS A 118 4.101 -13.027 -1.145 1.00 10.90 C ANISOU 970 CA LYS A 118 1320 1559 1261 -90 120 109 C ATOM 971 C LYS A 118 3.654 -12.216 0.070 1.00 11.15 C ANISOU 971 C LYS A 118 1191 1631 1414 -173 53 -48 C ATOM 972 O LYS A 118 2.473 -12.231 0.434 1.00 12.25 O ANISOU 972 O LYS A 118 1163 1693 1799 -151 125 -169 O ATOM 973 CB LYS A 118 4.207 -14.513 -0.801 1.00 11.25 C ANISOU 973 CB LYS A 118 1491 1653 1126 -101 -14 101 C ATOM 974 CG LYS A 118 4.275 -15.412 -2.033 1.00 11.17 C ANISOU 974 CG LYS A 118 2025 1286 932 -207 -139 119 C ATOM 975 CD LYS A 118 4.311 -16.887 -1.668 1.00 12.73 C ANISOU 975 CD LYS A 118 1901 1584 1350 -205 -146 298 C ATOM 976 CE LYS A 118 2.929 -17.420 -1.315 1.00 14.61 C ANISOU 976 CE LYS A 118 1921 2139 1489 -177 -185 694 C ATOM 977 NZ LYS A 118 1.974 -17.279 -2.458 1.00 15.14 N ANISOU 977 NZ LYS A 118 1830 2336 1585 -510 -367 651 N ATOM 978 N HIS A 119 4.591 -11.498 0.687 1.00 10.69 N ANISOU 978 N HIS A 119 1288 1422 1351 -59 28 -238 N ATOM 979 CA HIS A 119 4.304 -10.767 1.921 1.00 11.62 C ANISOU 979 CA HIS A 119 1373 1675 1364 -136 -6 -116 C ATOM 980 C HIS A 119 4.898 -9.366 1.890 1.00 10.59 C ANISOU 980 C HIS A 119 1111 1484 1428 -168 57 -166 C ATOM 981 O HIS A 119 5.627 -8.972 2.803 1.00 12.06 O ANISOU 981 O HIS A 119 1342 1524 1716 -97 86 -153 O ATOM 982 CB HIS A 119 4.827 -11.544 3.135 1.00 12.28 C ANISOU 982 CB HIS A 119 1710 1518 1436 -176 42 -114 C ATOM 983 CG HIS A 119 4.439 -12.989 3.126 1.00 12.23 C ANISOU 983 CG HIS A 119 1595 1649 1401 -284 217 -55 C ATOM 984 ND1 HIS A 119 3.242 -13.444 3.637 1.00 13.30 N ANISOU 984 ND1 HIS A 119 1802 1822 1429 -247 206 189 N ATOM 985 CD2 HIS A 119 5.091 -14.081 2.661 1.00 13.28 C ANISOU 985 CD2 HIS A 119 1882 1608 1553 -120 -4 -118 C ATOM 986 CE1 HIS A 119 3.172 -14.754 3.476 1.00 12.26 C ANISOU 986 CE1 HIS A 119 1593 1702 1360 -320 26 -162 C ATOM 987 NE2 HIS A 119 4.280 -15.164 2.887 1.00 13.23 N ANISOU 987 NE2 HIS A 119 1873 1810 1344 -467 50 -125 N ATOM 988 N PRO A 120 4.570 -8.598 0.842 1.00 11.26 N ANISOU 988 N PRO A 120 1204 1610 1463 -146 -30 -208 N ATOM 989 CA PRO A 120 5.245 -7.320 0.670 1.00 11.98 C ANISOU 989 CA PRO A 120 1391 1600 1558 -136 -118 -287 C ATOM 990 C PRO A 120 4.902 -6.370 1.806 1.00 11.32 C ANISOU 990 C PRO A 120 1340 1494 1465 -162 -43 -271 C ATOM 991 O PRO A 120 3.729 -6.208 2.146 1.00 12.70 O ANISOU 991 O PRO A 120 1403 1835 1586 -54 29 -336 O ATOM 992 CB PRO A 120 4.673 -6.797 -0.650 1.00 12.29 C ANISOU 992 CB PRO A 120 1443 1566 1659 -121 -313 -234 C ATOM 993 CG PRO A 120 3.324 -7.484 -0.769 1.00 12.30 C ANISOU 993 CG PRO A 120 1289 1442 1942 -240 -162 -204 C ATOM 994 CD PRO A 120 3.583 -8.855 -0.220 1.00 12.02 C ANISOU 994 CD PRO A 120 1268 1653 1642 -69 -16 -205 C ATOM 995 N GLY A 121 5.919 -5.751 2.389 1.00 10.47 N ANISOU 995 N GLY A 121 1369 1366 1243 -112 -125 -359 N ATOM 996 CA GLY A 121 5.711 -4.855 3.516 1.00 11.20 C ANISOU 996 CA GLY A 121 1600 1599 1055 43 -2 -153 C ATOM 997 C GLY A 121 5.568 -5.585 4.838 1.00 12.49 C ANISOU 997 C GLY A 121 1671 1626 1447 -182 26 -233 C ATOM 998 O GLY A 121 5.464 -4.944 5.890 1.00 13.95 O ANISOU 998 O GLY A 121 2075 1729 1495 39 234 -222 O ATOM 999 N ASP A 122 5.583 -6.918 4.795 1.00 11.29 N ANISOU 999 N ASP A 122 1256 1593 1441 92 80 -1 N ATOM 1000 CA ASP A 122 5.441 -7.719 6.007 1.00 12.54 C ANISOU 1000 CA ASP A 122 1278 1624 1861 -54 102 -202 C ATOM 1001 C ASP A 122 6.639 -8.639 6.264 1.00 12.84 C ANISOU 1001 C ASP A 122 1388 1591 1899 12 71 7 C ATOM 1002 O ASP A 122 6.535 -9.608 7.007 1.00 16.34 O ANISOU 1002 O ASP A 122 1630 2355 2223 53 402 561 O ATOM 1003 CB ASP A 122 4.160 -8.548 5.939 1.00 15.40 C ANISOU 1003 CB ASP A 122 1668 2050 2130 -85 386 -46 C ATOM 1004 CG ASP A 122 3.791 -9.158 7.272 1.00 19.01 C ANISOU 1004 CG ASP A 122 2032 2732 2459 -108 544 -157 C ATOM 1005 OD1 ASP A 122 3.961 -8.475 8.305 1.00 21.45 O ANISOU 1005 OD1 ASP A 122 2523 3391 2234 -128 702 -160 O ATOM 1006 OD2 ASP A 122 3.332 -10.318 7.282 1.00 22.60 O ANISOU 1006 OD2 ASP A 122 2724 3092 2771 -226 595 19 O ATOM 1007 N PHE A 123 7.770 -8.335 5.641 1.00 11.26 N ANISOU 1007 N PHE A 123 1248 1417 1611 23 108 -40 N ATOM 1008 CA PHE A 123 8.996 -9.108 5.839 1.00 11.55 C ANISOU 1008 CA PHE A 123 1400 1392 1595 125 44 -144 C ATOM 1009 C PHE A 123 10.054 -8.052 6.141 1.00 12.06 C ANISOU 1009 C PHE A 123 1336 1621 1624 261 67 -17 C ATOM 1010 O PHE A 123 10.763 -7.580 5.252 1.00 11.99 O ANISOU 1010 O PHE A 123 1515 1508 1533 64 -125 99 O ATOM 1011 CB PHE A 123 9.304 -9.918 4.568 1.00 11.89 C ANISOU 1011 CB PHE A 123 1580 1421 1514 257 53 -154 C ATOM 1012 CG PHE A 123 10.518 -10.817 4.664 1.00 10.74 C ANISOU 1012 CG PHE A 123 1490 1281 1309 22 52 38 C ATOM 1013 CD1 PHE A 123 10.879 -11.432 5.855 1.00 11.79 C ANISOU 1013 CD1 PHE A 123 1435 1605 1439 245 241 172 C ATOM 1014 CD2 PHE A 123 11.282 -11.070 3.535 1.00 10.77 C ANISOU 1014 CD2 PHE A 123 1440 1068 1585 -224 73 -219 C ATOM 1015 CE1 PHE A 123 11.996 -12.268 5.918 1.00 12.56 C ANISOU 1015 CE1 PHE A 123 1739 1627 1405 95 182 49 C ATOM 1016 CE2 PHE A 123 12.384 -11.901 3.587 1.00 11.74 C ANISOU 1016 CE2 PHE A 123 1523 1478 1459 -145 164 -176 C ATOM 1017 CZ PHE A 123 12.748 -12.497 4.782 1.00 11.43 C ANISOU 1017 CZ PHE A 123 1584 1497 1261 -66 102 -15 C ATOM 1018 N GLY A 124 10.132 -7.676 7.414 1.00 12.70 N ANISOU 1018 N GLY A 124 1359 1533 1932 280 -186 -275 N ATOM 1019 CA GLY A 124 10.906 -6.518 7.836 1.00 13.90 C ANISOU 1019 CA GLY A 124 1310 1832 2139 222 -151 -282 C ATOM 1020 C GLY A 124 12.402 -6.708 7.729 1.00 12.17 C ANISOU 1020 C GLY A 124 1363 1343 1917 200 -394 -156 C ATOM 1021 O GLY A 124 12.895 -7.824 7.523 1.00 11.81 O ANISOU 1021 O GLY A 124 1285 1482 1718 115 -305 -203 O ATOM 1022 N ALA A 125 13.130 -5.613 7.904 1.00 12.34 N ANISOU 1022 N ALA A 125 1424 1465 1798 79 -336 -60 N ATOM 1023 CA ALA A 125 14.570 -5.645 7.741 1.00 11.41 C ANISOU 1023 CA ALA A 125 1229 1573 1531 73 -404 146 C ATOM 1024 C ALA A 125 15.224 -6.602 8.737 1.00 10.92 C ANISOU 1024 C ALA A 125 1419 1231 1500 -80 -245 3 C ATOM 1025 O ALA A 125 16.150 -7.328 8.386 1.00 11.35 O ANISOU 1025 O ALA A 125 1331 1675 1304 190 -286 -45 O ATOM 1026 CB ALA A 125 15.146 -4.249 7.885 1.00 12.31 C ANISOU 1026 CB ALA A 125 1565 1398 1711 -198 -231 231 C ATOM 1027 N ASP A 126 14.741 -6.609 9.975 1.00 11.06 N ANISOU 1027 N ASP A 126 1256 1425 1521 48 -80 109 N ATOM 1028 CA ASP A 126 15.277 -7.526 10.979 1.00 12.38 C ANISOU 1028 CA ASP A 126 1548 1685 1470 -18 144 40 C ATOM 1029 C ASP A 126 15.017 -8.983 10.588 1.00 11.31 C ANISOU 1029 C ASP A 126 1324 1577 1395 186 22 15 C ATOM 1030 O ASP A 126 15.902 -9.837 10.684 1.00 12.04 O ANISOU 1030 O ASP A 126 1479 1675 1418 161 82 -1 O ATOM 1031 CB ASP A 126 14.758 -7.192 12.392 1.00 15.91 C ANISOU 1031 CB ASP A 126 2186 2116 1741 126 410 -124 C ATOM 1032 CG ASP A 126 13.236 -7.123 12.478 1.00 19.15 C ANISOU 1032 CG ASP A 126 2883 2422 1968 139 617 -151 C ATOM 1033 OD1 ASP A 126 12.549 -7.291 11.452 1.00 19.48 O ANISOU 1033 OD1 ASP A 126 2683 2433 2283 381 595 -189 O ATOM 1034 OD2 ASP A 126 12.725 -6.895 13.597 1.00 24.33 O ANISOU 1034 OD2 ASP A 126 3344 3240 2659 159 751 -203 O ATOM 1035 N ALA A 127 13.813 -9.250 10.099 1.00 11.24 N ANISOU 1035 N ALA A 127 1363 1454 1454 4 101 -150 N ATOM 1036 CA ALA A 127 13.416 -10.591 9.694 1.00 12.22 C ANISOU 1036 CA ALA A 127 1282 1736 1625 4 293 -28 C ATOM 1037 C ALA A 127 14.247 -11.077 8.502 1.00 11.07 C ANISOU 1037 C ALA A 127 1297 1447 1460 66 200 38 C ATOM 1038 O ALA A 127 14.704 -12.221 8.477 1.00 10.88 O ANISOU 1038 O ALA A 127 1210 1340 1583 48 86 23 O ATOM 1039 CB ALA A 127 11.917 -10.621 9.373 1.00 12.68 C ANISOU 1039 CB ALA A 127 1286 1881 1650 0 223 -134 C ATOM 1040 N GLN A 128 14.456 -10.208 7.517 1.00 11.15 N ANISOU 1040 N GLN A 128 1247 1526 1461 71 215 74 N ATOM 1041 CA GLN A 128 15.318 -10.576 6.404 1.00 11.00 C ANISOU 1041 CA GLN A 128 1203 1502 1471 61 104 87 C ATOM 1042 C GLN A 128 16.735 -10.895 6.878 1.00 10.94 C ANISOU 1042 C GLN A 128 1200 1495 1461 -55 160 79 C ATOM 1043 O GLN A 128 17.337 -11.875 6.443 1.00 10.51 O ANISOU 1043 O GLN A 128 1480 1338 1172 172 125 67 O ATOM 1044 CB GLN A 128 15.348 -9.505 5.316 1.00 11.43 C ANISOU 1044 CB GLN A 128 1232 1731 1379 91 68 190 C ATOM 1045 CG GLN A 128 16.235 -9.904 4.152 1.00 11.34 C ANISOU 1045 CG GLN A 128 1198 1895 1214 -12 14 64 C ATOM 1046 CD GLN A 128 16.244 -8.892 3.032 1.00 9.43 C ANISOU 1046 CD GLN A 128 1011 1307 1263 -44 -141 -39 C ATOM 1047 OE1 GLN A 128 15.294 -8.130 2.852 1.00 10.41 O ANISOU 1047 OE1 GLN A 128 1089 1533 1333 47 -42 -40 O ATOM 1048 NE2 GLN A 128 17.318 -8.891 2.251 1.00 11.01 N ANISOU 1048 NE2 GLN A 128 1044 1591 1547 -77 121 97 N ATOM 1049 N GLY A 129 17.268 -10.072 7.775 1.00 10.53 N ANISOU 1049 N GLY A 129 1158 1381 1461 85 25 -14 N ATOM 1050 CA GLY A 129 18.594 -10.335 8.327 1.00 10.98 C ANISOU 1050 CA GLY A 129 1286 1424 1459 128 68 130 C ATOM 1051 C GLY A 129 18.672 -11.712 8.959 1.00 9.52 C ANISOU 1051 C GLY A 129 1082 1266 1266 102 35 -86 C ATOM 1052 O GLY A 129 19.601 -12.483 8.695 1.00 10.71 O ANISOU 1052 O GLY A 129 1206 1461 1403 -33 -16 -100 O ATOM 1053 N ALA A 130 17.700 -12.027 9.807 1.00 9.54 N ANISOU 1053 N ALA A 130 1095 1339 1189 -101 -23 31 N ATOM 1054 CA ALA A 130 17.736 -13.294 10.529 1.00 9.90 C ANISOU 1054 CA ALA A 130 1127 1285 1347 12 34 -22 C ATOM 1055 C ALA A 130 17.584 -14.479 9.578 1.00 9.69 C ANISOU 1055 C ALA A 130 1126 1305 1249 -159 12 55 C ATOM 1056 O ALA A 130 18.342 -15.450 9.666 1.00 10.14 O ANISOU 1056 O ALA A 130 1231 1272 1349 -38 -27 45 O ATOM 1057 CB ALA A 130 16.668 -13.327 11.616 1.00 10.90 C ANISOU 1057 CB ALA A 130 1431 1540 1167 -184 78 80 C ATOM 1058 N MET A 131 16.610 -14.410 8.672 1.00 10.09 N ANISOU 1058 N MET A 131 1125 1471 1234 -222 -1 -13 N ATOM 1059 CA MET A 131 16.402 -15.499 7.719 1.00 9.64 C ANISOU 1059 CA MET A 131 965 1412 1286 -223 -85 132 C ATOM 1060 C MET A 131 17.628 -15.698 6.836 1.00 9.50 C ANISOU 1060 C MET A 131 1097 1202 1310 -180 -173 34 C ATOM 1061 O MET A 131 18.005 -16.834 6.531 1.00 10.57 O ANISOU 1061 O MET A 131 1182 1145 1688 147 -40 -35 O ATOM 1062 CB MET A 131 15.162 -15.253 6.865 1.00 10.93 C ANISOU 1062 CB MET A 131 1194 1585 1372 -110 -84 165 C ATOM 1063 CG MET A 131 14.819 -16.404 5.923 1.00 12.35 C ANISOU 1063 CG MET A 131 1680 1623 1389 -403 -141 167 C ATOM 1064 SD MET A 131 14.582 -18.029 6.718 1.00 16.33 S ANISOU 1064 SD MET A 131 2284 2319 1601 -779 -566 244 S ATOM 1065 CE MET A 131 13.012 -17.793 7.508 1.00 18.98 C ANISOU 1065 CE MET A 131 2683 2742 1784 205 -621 -47 C ATOM 1066 N THR A 132 18.266 -14.599 6.448 1.00 9.82 N ANISOU 1066 N THR A 132 998 1441 1290 -163 -30 -21 N ATOM 1067 CA THR A 132 19.471 -14.680 5.635 1.00 10.44 C ANISOU 1067 CA THR A 132 1261 1207 1497 -9 -3 -91 C ATOM 1068 C THR A 132 20.574 -15.419 6.388 1.00 10.30 C ANISOU 1068 C THR A 132 1182 1388 1342 -66 -64 -92 C ATOM 1069 O THR A 132 21.231 -16.296 5.825 1.00 11.10 O ANISOU 1069 O THR A 132 1174 1358 1685 6 131 -147 O ATOM 1070 CB THR A 132 19.934 -13.284 5.208 1.00 10.39 C ANISOU 1070 CB THR A 132 1261 1236 1449 -2 88 13 C ATOM 1071 OG1 THR A 132 18.938 -12.718 4.348 1.00 11.70 O ANISOU 1071 OG1 THR A 132 1380 1629 1437 -10 7 300 O ATOM 1072 CG2 THR A 132 21.243 -13.351 4.449 1.00 12.72 C ANISOU 1072 CG2 THR A 132 1459 1494 1879 38 213 -89 C ATOM 1073 N LYS A 133 20.767 -15.085 7.663 1.00 10.33 N ANISOU 1073 N LYS A 133 1234 1330 1359 -43 -201 -41 N ATOM 1074 CA LYS A 133 21.755 -15.796 8.474 1.00 10.82 C ANISOU 1074 CA LYS A 133 1052 1515 1543 95 -132 -61 C ATOM 1075 C LYS A 133 21.450 -17.291 8.546 1.00 10.88 C ANISOU 1075 C LYS A 133 1242 1357 1533 -30 68 -25 C ATOM 1076 O LYS A 133 22.353 -18.131 8.486 1.00 10.79 O ANISOU 1076 O LYS A 133 1061 1435 1601 -9 -192 -139 O ATOM 1077 CB LYS A 133 21.848 -15.209 9.888 1.00 12.64 C ANISOU 1077 CB LYS A 133 1474 1620 1706 -216 -211 -223 C ATOM 1078 CG LYS A 133 22.635 -13.900 9.970 1.00 13.72 C ANISOU 1078 CG LYS A 133 1666 1818 1726 -384 -339 -68 C ATOM 1079 CD LYS A 133 22.835 -13.430 11.416 1.00 14.27 C ANISOU 1079 CD LYS A 133 1795 1981 1645 -220 -100 58 C ATOM 1080 CE LYS A 133 23.802 -14.326 12.176 1.00 16.52 C ANISOU 1080 CE LYS A 133 2224 2337 1716 -369 14 40 C ATOM 1081 NZ LYS A 133 24.138 -13.753 13.516 1.00 20.12 N ANISOU 1081 NZ LYS A 133 2406 3175 2064 -478 9 80 N ATOM 1082 N ALA A 134 20.179 -17.638 8.717 1.00 10.16 N ANISOU 1082 N ALA A 134 1209 1348 1303 -91 -79 -60 N ATOM 1083 CA ALA A 134 19.819 -19.044 8.830 1.00 10.27 C ANISOU 1083 CA ALA A 134 1244 1399 1258 43 -134 -208 C ATOM 1084 C ALA A 134 20.098 -19.800 7.539 1.00 9.20 C ANISOU 1084 C ALA A 134 896 1378 1221 49 -102 92 C ATOM 1085 O ALA A 134 20.581 -20.932 7.569 1.00 9.75 O ANISOU 1085 O ALA A 134 1075 1333 1296 76 -112 -38 O ATOM 1086 CB ALA A 134 18.361 -19.200 9.253 1.00 11.23 C ANISOU 1086 CB ALA A 134 1057 1684 1524 -206 39 -47 C ATOM 1087 N LEU A 135 19.792 -19.174 6.408 1.00 9.59 N ANISOU 1087 N LEU A 135 1061 1358 1224 -104 -182 32 N ATOM 1088 CA LEU A 135 20.039 -19.804 5.114 1.00 10.03 C ANISOU 1088 CA LEU A 135 1214 1278 1315 82 -265 -3 C ATOM 1089 C LEU A 135 21.532 -19.901 4.804 1.00 10.29 C ANISOU 1089 C LEU A 135 1114 1252 1544 9 -195 -21 C ATOM 1090 O LEU A 135 21.992 -20.880 4.198 1.00 10.37 O ANISOU 1090 O LEU A 135 1306 1262 1371 117 -212 -67 O ATOM 1091 CB LEU A 135 19.305 -19.068 4.002 1.00 10.08 C ANISOU 1091 CB LEU A 135 1189 1408 1232 39 -177 20 C ATOM 1092 CG LEU A 135 17.783 -19.122 4.092 1.00 11.03 C ANISOU 1092 CG LEU A 135 992 1547 1652 -197 -209 -55 C ATOM 1093 CD1 LEU A 135 17.163 -18.132 3.103 1.00 12.07 C ANISOU 1093 CD1 LEU A 135 1175 2020 1389 191 -134 53 C ATOM 1094 CD2 LEU A 135 17.276 -20.537 3.831 1.00 14.40 C ANISOU 1094 CD2 LEU A 135 1317 1895 2260 -276 -284 -36 C ATOM 1095 N GLU A 136 22.306 -18.904 5.236 1.00 9.90 N ANISOU 1095 N GLU A 136 1094 1268 1399 -28 -122 86 N ATOM 1096 CA GLU A 136 23.760 -18.962 5.075 1.00 10.02 C ANISOU 1096 CA GLU A 136 929 1373 1505 -151 -21 -135 C ATOM 1097 C GLU A 136 24.356 -20.088 5.921 1.00 10.21 C ANISOU 1097 C GLU A 136 1120 1368 1389 -229 -146 -133 C ATOM 1098 O GLU A 136 25.249 -20.797 5.469 1.00 10.68 O ANISOU 1098 O GLU A 136 1059 1375 1624 58 -23 -179 O ATOM 1099 CB GLU A 136 24.400 -17.628 5.446 1.00 11.21 C ANISOU 1099 CB GLU A 136 1136 1426 1695 -85 -15 -187 C ATOM 1100 CG GLU A 136 24.186 -16.556 4.401 1.00 13.24 C ANISOU 1100 CG GLU A 136 1506 1490 2034 -36 158 -92 C ATOM 1101 CD GLU A 136 24.646 -15.188 4.856 1.00 16.83 C ANISOU 1101 CD GLU A 136 2290 1929 2173 -174 213 -82 C ATOM 1102 OE1 GLU A 136 24.648 -14.918 6.077 1.00 15.90 O ANISOU 1102 OE1 GLU A 136 1607 1818 2613 7 159 -41 O ATOM 1103 OE2 GLU A 136 24.993 -14.376 3.977 1.00 22.43 O ANISOU 1103 OE2 GLU A 136 3318 2413 2788 -627 801 -82 O ATOM 1104 N LEU A 137 23.863 -20.254 7.146 1.00 9.55 N ANISOU 1104 N LEU A 137 1104 1256 1268 0 -215 -31 N ATOM 1105 CA LEU A 137 24.349 -21.325 8.013 1.00 10.81 C ANISOU 1105 CA LEU A 137 1279 1452 1375 10 -14 -55 C ATOM 1106 C LEU A 137 24.069 -22.689 7.382 1.00 10.41 C ANISOU 1106 C LEU A 137 1165 1326 1462 69 -106 72 C ATOM 1107 O LEU A 137 24.929 -23.572 7.352 1.00 10.42 O ANISOU 1107 O LEU A 137 1211 1274 1473 118 -43 -58 O ATOM 1108 CB LEU A 137 23.679 -21.224 9.384 1.00 11.24 C ANISOU 1108 CB LEU A 137 1233 1538 1497 159 61 189 C ATOM 1109 CG LEU A 137 24.064 -22.305 10.394 1.00 13.31 C ANISOU 1109 CG LEU A 137 1346 2146 1564 87 -38 327 C ATOM 1110 CD1 LEU A 137 25.548 -22.236 10.773 1.00 15.17 C ANISOU 1110 CD1 LEU A 137 1391 2561 1811 54 61 182 C ATOM 1111 CD2 LEU A 137 23.199 -22.166 11.637 1.00 13.94 C ANISOU 1111 CD2 LEU A 137 1671 2284 1337 57 362 199 C ATOM 1112 N PHE A 138 22.848 -22.860 6.884 1.00 10.14 N ANISOU 1112 N PHE A 138 1075 1360 1415 -163 -172 -63 N ATOM 1113 CA PHE A 138 22.442 -24.068 6.170 1.00 10.69 C ANISOU 1113 CA PHE A 138 1171 1386 1502 -122 61 -37 C ATOM 1114 C PHE A 138 23.399 -24.347 4.998 1.00 11.11 C ANISOU 1114 C PHE A 138 1257 1405 1559 -52 -174 -80 C ATOM 1115 O PHE A 138 23.972 -25.431 4.893 1.00 11.57 O ANISOU 1115 O PHE A 138 1289 1410 1693 150 49 97 O ATOM 1116 CB PHE A 138 20.994 -23.863 5.706 1.00 11.55 C ANISOU 1116 CB PHE A 138 1166 1541 1679 -52 -216 -147 C ATOM 1117 CG PHE A 138 20.498 -24.856 4.688 1.00 12.90 C ANISOU 1117 CG PHE A 138 1468 1530 1904 -178 -140 -102 C ATOM 1118 CD1 PHE A 138 20.116 -26.133 5.058 1.00 13.15 C ANISOU 1118 CD1 PHE A 138 1430 1548 2018 -107 -241 -275 C ATOM 1119 CD2 PHE A 138 20.341 -24.472 3.364 1.00 14.38 C ANISOU 1119 CD2 PHE A 138 1815 1911 1738 -119 -283 -109 C ATOM 1120 CE1 PHE A 138 19.626 -27.029 4.112 1.00 15.62 C ANISOU 1120 CE1 PHE A 138 2004 1972 1958 -290 -144 -72 C ATOM 1121 CE2 PHE A 138 19.855 -25.353 2.415 1.00 15.32 C ANISOU 1121 CE2 PHE A 138 1914 1874 2033 -284 -277 -67 C ATOM 1122 CZ PHE A 138 19.494 -26.634 2.788 1.00 14.51 C ANISOU 1122 CZ PHE A 138 1857 1837 1818 -162 -481 -191 C ATOM 1123 N ARG A 139 23.585 -23.350 4.139 1.00 11.34 N ANISOU 1123 N ARG A 139 1388 1441 1479 57 98 5 N ATOM 1124 CA ARG A 139 24.448 -23.474 2.964 1.00 12.82 C ANISOU 1124 CA ARG A 139 1649 1656 1563 232 68 151 C ATOM 1125 C ARG A 139 25.891 -23.759 3.355 1.00 12.44 C ANISOU 1125 C ARG A 139 1616 1545 1565 327 338 -83 C ATOM 1126 O ARG A 139 26.585 -24.577 2.730 1.00 12.33 O ANISOU 1126 O ARG A 139 1655 1374 1655 199 378 -25 O ATOM 1127 CB ARG A 139 24.367 -22.173 2.152 1.00 16.60 C ANISOU 1127 CB ARG A 139 2097 2400 1809 376 219 309 C ATOM 1128 CG ARG A 139 25.009 -22.222 0.797 1.00 18.42 C ANISOU 1128 CG ARG A 139 2106 2482 2408 48 -121 287 C ATOM 1129 CD ARG A 139 24.357 -21.196 -0.122 1.00 14.40 C ANISOU 1129 CD ARG A 139 1695 1784 1991 -170 -457 388 C ATOM 1130 NE ARG A 139 24.814 -19.818 0.084 1.00 13.50 N ANISOU 1130 NE ARG A 139 1574 1883 1670 -339 -531 214 N ATOM 1131 CZ ARG A 139 24.073 -18.834 0.592 1.00 13.28 C ANISOU 1131 CZ ARG A 139 1182 2024 1840 -438 -285 451 C ATOM 1132 NH1 ARG A 139 22.823 -19.065 0.990 1.00 14.68 N ANISOU 1132 NH1 ARG A 139 1391 2130 2057 -391 -86 530 N ATOM 1133 NH2 ARG A 139 24.589 -17.612 0.711 1.00 14.29 N ANISOU 1133 NH2 ARG A 139 1331 2084 2014 -408 -214 300 N ATOM 1134 N ASN A 140 26.351 -23.074 4.392 1.00 11.59 N ANISOU 1134 N ASN A 140 1284 1589 1529 179 104 110 N ATOM 1135 CA ASN A 140 27.731 -23.214 4.812 1.00 11.42 C ANISOU 1135 CA ASN A 140 1431 1481 1427 -14 121 163 C ATOM 1136 C ASN A 140 28.032 -24.588 5.407 1.00 10.80 C ANISOU 1136 C ASN A 140 1102 1544 1457 164 22 154 C ATOM 1137 O ASN A 140 29.108 -25.157 5.198 1.00 11.88 O ANISOU 1137 O ASN A 140 1211 1613 1689 202 234 238 O ATOM 1138 CB ASN A 140 28.099 -22.110 5.788 1.00 13.06 C ANISOU 1138 CB ASN A 140 1340 1908 1711 -54 134 -23 C ATOM 1139 CG ASN A 140 29.574 -21.995 5.968 1.00 14.11 C ANISOU 1139 CG ASN A 140 1526 1933 1900 25 39 -108 C ATOM 1140 OD1 ASN A 140 30.091 -22.255 7.043 1.00 15.49 O ANISOU 1140 OD1 ASN A 140 1698 2358 1827 338 -422 -88 O ATOM 1141 ND2 ASN A 140 30.276 -21.639 4.896 1.00 14.24 N ANISOU 1141 ND2 ASN A 140 1558 1952 1899 95 121 -44 N ATOM 1142 N ASP A 141 27.083 -25.122 6.161 1.00 10.85 N ANISOU 1142 N ASP A 141 1160 1587 1374 19 143 261 N ATOM 1143 CA ASP A 141 27.253 -26.455 6.718 1.00 10.37 C ANISOU 1143 CA ASP A 141 1173 1405 1361 -25 -81 155 C ATOM 1144 C ASP A 141 27.188 -27.518 5.620 1.00 10.64 C ANISOU 1144 C ASP A 141 1170 1408 1462 37 40 318 C ATOM 1145 O ASP A 141 27.916 -28.507 5.661 1.00 11.89 O ANISOU 1145 O ASP A 141 1329 1351 1838 225 19 94 O ATOM 1146 CB ASP A 141 26.248 -26.708 7.844 1.00 11.43 C ANISOU 1146 CB ASP A 141 1211 1708 1420 -128 21 193 C ATOM 1147 CG ASP A 141 26.622 -25.985 9.131 1.00 12.51 C ANISOU 1147 CG ASP A 141 1062 1855 1833 -125 -86 372 C ATOM 1148 OD1 ASP A 141 27.723 -25.396 9.204 1.00 13.01 O ANISOU 1148 OD1 ASP A 141 1319 1893 1730 -273 26 215 O ATOM 1149 OD2 ASP A 141 25.813 -26.006 10.077 1.00 13.07 O ANISOU 1149 OD2 ASP A 141 1220 2044 1700 -376 175 -3 O ATOM 1150 N ILE A 142 26.344 -27.305 4.616 1.00 11.05 N ANISOU 1150 N ILE A 142 1353 1398 1446 71 -8 -77 N ATOM 1151 CA ILE A 142 26.353 -28.183 3.450 1.00 12.03 C ANISOU 1151 CA ILE A 142 1239 1948 1381 231 9 172 C ATOM 1152 C ILE A 142 27.702 -28.092 2.735 1.00 12.86 C ANISOU 1152 C ILE A 142 1405 1780 1701 268 111 199 C ATOM 1153 O ILE A 142 28.271 -29.108 2.342 1.00 11.71 O ANISOU 1153 O ILE A 142 1285 1640 1521 279 16 -54 O ATOM 1154 CB ILE A 142 25.211 -27.848 2.468 1.00 12.51 C ANISOU 1154 CB ILE A 142 1279 2040 1434 193 101 -165 C ATOM 1155 CG1 ILE A 142 23.869 -28.239 3.092 1.00 14.80 C ANISOU 1155 CG1 ILE A 142 1460 2152 2010 134 -20 -180 C ATOM 1156 CG2 ILE A 142 25.405 -28.600 1.149 1.00 13.02 C ANISOU 1156 CG2 ILE A 142 1453 1837 1656 314 49 -9 C ATOM 1157 CD1 ILE A 142 22.664 -27.824 2.273 1.00 17.74 C ANISOU 1157 CD1 ILE A 142 1765 2596 2379 77 -223 -68 C ATOM 1158 N ALA A 143 28.215 -26.874 2.584 1.00 11.87 N ANISOU 1158 N ALA A 143 1372 1626 1511 322 236 32 N ATOM 1159 CA ALA A 143 29.492 -26.669 1.909 1.00 12.31 C ANISOU 1159 CA ALA A 143 1454 1485 1738 288 346 123 C ATOM 1160 C ALA A 143 30.622 -27.442 2.580 1.00 11.36 C ANISOU 1160 C ALA A 143 1407 1388 1519 120 149 49 C ATOM 1161 O ALA A 143 31.515 -27.953 1.905 1.00 11.03 O ANISOU 1161 O ALA A 143 1303 1375 1511 154 262 -87 O ATOM 1162 CB ALA A 143 29.827 -25.189 1.851 1.00 14.32 C ANISOU 1162 CB ALA A 143 1672 1752 2015 301 620 233 C ATOM 1163 N ALA A 144 30.602 -27.513 3.907 1.00 10.72 N ANISOU 1163 N ALA A 144 1319 1316 1437 187 186 28 N ATOM 1164 CA ALA A 144 31.633 -28.272 4.622 1.00 10.61 C ANISOU 1164 CA ALA A 144 1247 1406 1374 19 71 90 C ATOM 1165 C ALA A 144 31.554 -29.753 4.254 1.00 10.26 C ANISOU 1165 C ALA A 144 1068 1286 1541 -20 -73 -92 C ATOM 1166 O ALA A 144 32.574 -30.424 4.069 1.00 10.51 O ANISOU 1166 O ALA A 144 1095 1339 1559 93 -194 -202 O ATOM 1167 CB ALA A 144 31.486 -28.084 6.123 1.00 12.25 C ANISOU 1167 CB ALA A 144 1778 1673 1202 -185 -13 50 C ATOM 1168 N LYS A 145 30.334 -30.268 4.143 1.00 10.25 N ANISOU 1168 N LYS A 145 1106 1372 1414 -148 -18 -175 N ATOM 1169 CA LYS A 145 30.124 -31.659 3.754 1.00 10.60 C ANISOU 1169 CA LYS A 145 1241 1386 1398 -135 30 60 C ATOM 1170 C LYS A 145 30.555 -31.886 2.303 1.00 9.48 C ANISOU 1170 C LYS A 145 1056 1249 1297 -14 -59 46 C ATOM 1171 O LYS A 145 31.147 -32.919 1.974 1.00 10.75 O ANISOU 1171 O LYS A 145 1241 1297 1544 70 -114 -108 O ATOM 1172 CB LYS A 145 28.655 -32.067 3.937 1.00 11.44 C ANISOU 1172 CB LYS A 145 1171 1600 1576 -226 47 -89 C ATOM 1173 CG LYS A 145 28.110 -31.915 5.347 1.00 15.27 C ANISOU 1173 CG LYS A 145 1822 2150 1829 -228 74 31 C ATOM 1174 CD LYS A 145 28.891 -32.744 6.350 1.00 16.60 C ANISOU 1174 CD LYS A 145 1691 2776 1837 -217 170 -32 C ATOM 1175 CE LYS A 145 28.253 -32.651 7.729 1.00 18.44 C ANISOU 1175 CE LYS A 145 2329 3093 1583 -185 191 52 C ATOM 1176 NZ LYS A 145 29.121 -33.235 8.784 1.00 20.64 N ANISOU 1176 NZ LYS A 145 2620 3439 1781 -209 298 72 N ATOM 1177 N TYR A 146 30.254 -30.925 1.435 1.00 10.05 N ANISOU 1177 N TYR A 146 1248 1424 1144 134 -48 40 N ATOM 1178 CA TYR A 146 30.702 -31.010 0.047 1.00 10.33 C ANISOU 1178 CA TYR A 146 1093 1645 1185 198 28 -78 C ATOM 1179 C TYR A 146 32.231 -31.066 -0.021 1.00 11.26 C ANISOU 1179 C TYR A 146 1235 1583 1461 161 -50 -105 C ATOM 1180 O TYR A 146 32.799 -31.855 -0.782 1.00 11.35 O ANISOU 1180 O TYR A 146 1240 1799 1270 280 -126 -203 O ATOM 1181 CB TYR A 146 30.201 -29.803 -0.744 1.00 10.58 C ANISOU 1181 CB TYR A 146 1011 1610 1399 86 -20 64 C ATOM 1182 CG TYR A 146 28.795 -29.923 -1.311 1.00 10.31 C ANISOU 1182 CG TYR A 146 1057 1591 1268 48 -14 22 C ATOM 1183 CD1 TYR A 146 27.877 -30.837 -0.807 1.00 10.59 C ANISOU 1183 CD1 TYR A 146 1222 1729 1069 84 -155 56 C ATOM 1184 CD2 TYR A 146 28.385 -29.093 -2.343 1.00 11.69 C ANISOU 1184 CD2 TYR A 146 1342 1706 1391 115 -228 168 C ATOM 1185 CE1 TYR A 146 26.593 -30.931 -1.340 1.00 10.84 C ANISOU 1185 CE1 TYR A 146 1284 1524 1310 68 -108 83 C ATOM 1186 CE2 TYR A 146 27.115 -29.181 -2.876 1.00 12.20 C ANISOU 1186 CE2 TYR A 146 1128 1869 1638 -94 -96 262 C ATOM 1187 CZ TYR A 146 26.222 -30.099 -2.372 1.00 10.55 C ANISOU 1187 CZ TYR A 146 865 1736 1407 -159 -132 210 C ATOM 1188 OH TYR A 146 24.964 -30.192 -2.920 1.00 11.12 O ANISOU 1188 OH TYR A 146 1058 1766 1399 -210 9 200 O ATOM 1189 N LYS A 147 32.906 -30.230 0.766 1.00 10.88 N ANISOU 1189 N LYS A 147 1135 1499 1498 54 -29 13 N ATOM 1190 CA LYS A 147 34.366 -30.257 0.767 1.00 10.40 C ANISOU 1190 CA LYS A 147 1158 1340 1451 181 -44 83 C ATOM 1191 C LYS A 147 34.904 -31.611 1.227 1.00 10.01 C ANISOU 1191 C LYS A 147 1041 1379 1384 -11 19 -87 C ATOM 1192 O LYS A 147 35.853 -32.142 0.648 1.00 11.97 O ANISOU 1192 O LYS A 147 1065 1595 1888 93 181 -258 O ATOM 1193 CB LYS A 147 34.946 -29.138 1.627 1.00 11.75 C ANISOU 1193 CB LYS A 147 1080 1626 1756 74 84 -147 C ATOM 1194 CG LYS A 147 36.470 -29.167 1.677 1.00 14.81 C ANISOU 1194 CG LYS A 147 1729 1590 2307 -83 -90 24 C ATOM 1195 CD LYS A 147 37.022 -27.994 2.469 1.00 17.06 C ANISOU 1195 CD LYS A 147 1861 2064 2557 -57 -33 -43 C ATOM 1196 CE LYS A 147 38.541 -28.040 2.566 1.00 19.47 C ANISOU 1196 CE LYS A 147 1972 2470 2955 432 121 394 C ATOM 1197 NZ LYS A 147 38.999 -28.926 3.673 1.00 21.93 N ANISOU 1197 NZ LYS A 147 2413 2472 3445 442 216 474 N ATOM 1198 N GLU A 148 34.297 -32.164 2.270 1.00 10.43 N ANISOU 1198 N GLU A 148 1229 1312 1422 16 -144 35 N ATOM 1199 C GLU A 148 34.662 -34.495 1.598 1.00 12.37 C ANISOU 1199 C GLU A 148 1446 1556 1697 159 -117 34 C ATOM 1200 O GLU A 148 35.598 -35.290 1.437 1.00 12.49 O ANISOU 1200 O GLU A 148 1454 1503 1787 146 -247 32 O ATOM 1201 CA AGLU A 148 34.688 -33.485 2.744 0.50 11.95 C ANISOU 1201 CA AGLU A 148 1455 1465 1620 -11 -126 12 C ATOM 1202 CB AGLU A 148 33.786 -33.934 3.894 0.50 14.28 C ANISOU 1202 CB AGLU A 148 1705 1917 1802 -171 -11 128 C ATOM 1203 CG AGLU A 148 33.906 -33.061 5.130 0.50 15.65 C ANISOU 1203 CG AGLU A 148 1991 2099 1857 -258 224 84 C ATOM 1204 CD AGLU A 148 32.833 -33.342 6.161 0.50 18.00 C ANISOU 1204 CD AGLU A 148 2381 2477 1979 -371 286 -94 C ATOM 1205 OE1AGLU A 148 32.291 -34.468 6.162 0.50 17.41 O ANISOU 1205 OE1AGLU A 148 2613 2496 1505 -332 185 151 O ATOM 1206 OE2AGLU A 148 32.537 -32.433 6.970 0.50 15.81 O ANISOU 1206 OE2AGLU A 148 1997 2521 1488 -570 391 -363 O ATOM 1207 CA BGLU A 148 34.647 -33.494 2.760 0.50 11.55 C ANISOU 1207 CA BGLU A 148 1411 1462 1514 51 -181 37 C ATOM 1208 CB BGLU A 148 33.623 -33.917 3.820 0.50 13.00 C ANISOU 1208 CB BGLU A 148 1693 1691 1555 44 -112 221 C ATOM 1209 CG BGLU A 148 33.908 -35.238 4.505 0.50 11.74 C ANISOU 1209 CG BGLU A 148 1536 1615 1310 16 -211 112 C ATOM 1210 CD BGLU A 148 32.886 -35.578 5.580 0.50 12.84 C ANISOU 1210 CD BGLU A 148 1561 1862 1455 74 -139 75 C ATOM 1211 OE1BGLU A 148 31.876 -34.858 5.708 0.50 12.11 O ANISOU 1211 OE1BGLU A 148 1430 1808 1361 -491 -389 -410 O ATOM 1212 OE2BGLU A 148 33.102 -36.569 6.309 0.50 16.14 O ANISOU 1212 OE2BGLU A 148 2056 2329 1746 -60 262 169 O ATOM 1213 N LEU A 149 33.612 -34.438 0.783 1.00 10.99 N ANISOU 1213 N LEU A 149 1259 1487 1427 -5 -223 51 N ATOM 1214 CA LEU A 149 33.441 -35.340 -0.359 1.00 11.78 C ANISOU 1214 CA LEU A 149 1448 1485 1541 -46 -208 60 C ATOM 1215 C LEU A 149 34.232 -34.953 -1.605 1.00 11.49 C ANISOU 1215 C LEU A 149 1543 1365 1457 41 -108 -93 C ATOM 1216 O LEU A 149 34.260 -35.700 -2.581 1.00 12.94 O ANISOU 1216 O LEU A 149 1761 1656 1499 -164 156 -67 O ATOM 1217 CB LEU A 149 31.965 -35.445 -0.731 1.00 12.91 C ANISOU 1217 CB LEU A 149 1562 1626 1715 -20 -154 48 C ATOM 1218 CG LEU A 149 31.025 -35.890 0.382 1.00 12.25 C ANISOU 1218 CG LEU A 149 1152 1685 1817 -93 -61 -92 C ATOM 1219 CD1 LEU A 149 29.579 -35.592 0.010 1.00 16.19 C ANISOU 1219 CD1 LEU A 149 1481 2407 2264 -58 -210 48 C ATOM 1220 CD2 LEU A 149 31.221 -37.362 0.692 1.00 14.50 C ANISOU 1220 CD2 LEU A 149 1651 1885 1973 84 319 164 C ATOM 1221 N GLY A 150 34.858 -33.783 -1.576 1.00 11.13 N ANISOU 1221 N GLY A 150 1220 1417 1592 -32 37 5 N ATOM 1222 CA GLY A 150 35.558 -33.274 -2.745 1.00 10.97 C ANISOU 1222 CA GLY A 150 1143 1552 1472 7 -97 137 C ATOM 1223 C GLY A 150 34.616 -32.928 -3.881 1.00 10.12 C ANISOU 1223 C GLY A 150 1099 1272 1475 -215 14 -52 C ATOM 1224 O GLY A 150 35.012 -32.923 -5.046 1.00 11.41 O ANISOU 1224 O GLY A 150 1250 1573 1513 -353 150 -77 O ATOM 1225 N PHE A 151 33.366 -32.627 -3.548 1.00 11.49 N ANISOU 1225 N PHE A 151 1266 1548 1551 -80 -99 -100 N ATOM 1226 CA PHE A 151 32.380 -32.354 -4.575 1.00 12.72 C ANISOU 1226 CA PHE A 151 1654 1564 1613 -163 -69 196 C ATOM 1227 C PHE A 151 32.372 -30.900 -4.995 1.00 15.05 C ANISOU 1227 C PHE A 151 1861 1870 1985 -181 3 79 C ATOM 1228 O PHE A 151 32.369 -30.003 -4.153 1.00 16.48 O ANISOU 1228 O PHE A 151 2531 1714 2016 -349 -71 -34 O ATOM 1229 CB PHE A 151 30.981 -32.742 -4.098 1.00 13.01 C ANISOU 1229 CB PHE A 151 1497 1801 1645 -126 -1 73 C ATOM 1230 CG PHE A 151 29.913 -32.416 -5.091 1.00 14.33 C ANISOU 1230 CG PHE A 151 1766 1668 2010 -8 -99 18 C ATOM 1231 CD1 PHE A 151 29.821 -33.129 -6.274 1.00 14.71 C ANISOU 1231 CD1 PHE A 151 1762 2030 1796 -335 -235 17 C ATOM 1232 CD2 PHE A 151 29.007 -31.397 -4.854 1.00 14.78 C ANISOU 1232 CD2 PHE A 151 1455 1838 2320 -9 -135 188 C ATOM 1233 CE1 PHE A 151 28.852 -32.830 -7.203 1.00 16.37 C ANISOU 1233 CE1 PHE A 151 1882 1924 2411 -316 -338 259 C ATOM 1234 CE2 PHE A 151 28.032 -31.096 -5.780 1.00 16.24 C ANISOU 1234 CE2 PHE A 151 1910 1865 2395 -74 -256 212 C ATOM 1235 CZ PHE A 151 27.956 -31.810 -6.958 1.00 15.63 C ANISOU 1235 CZ PHE A 151 1711 2094 2133 -170 -175 120 C ATOM 1236 N GLN A 152 32.358 -30.673 -6.306 1.00 14.97 N ANISOU 1236 N GLN A 152 1969 1782 1935 -203 -150 171 N ATOM 1237 CA GLN A 152 32.253 -29.323 -6.844 1.00 16.30 C ANISOU 1237 CA GLN A 152 1963 1947 2281 -211 -121 24 C ATOM 1238 C GLN A 152 31.010 -29.185 -7.717 1.00 18.83 C ANISOU 1238 C GLN A 152 2247 2280 2626 49 -362 -107 C ATOM 1239 O GLN A 152 30.276 -28.200 -7.620 1.00 23.21 O ANISOU 1239 O GLN A 152 2672 2773 3371 251 -376 -275 O ATOM 1240 CB GLN A 152 33.519 -28.953 -7.628 1.00 16.37 C ANISOU 1240 CB GLN A 152 2001 2029 2188 -300 23 150 C ATOM 1241 CG GLN A 152 34.735 -28.720 -6.740 1.00 16.58 C ANISOU 1241 CG GLN A 152 2240 1766 2291 -196 -28 -266 C ATOM 1242 CD GLN A 152 34.691 -27.383 -6.033 1.00 15.83 C ANISOU 1242 CD GLN A 152 1844 1782 2386 63 -76 -301 C ATOM 1243 OE1 GLN A 152 33.818 -26.554 -6.303 1.00 18.85 O ANISOU 1243 OE1 GLN A 152 2287 1911 2964 40 -196 -300 O ATOM 1244 NE2 GLN A 152 35.640 -27.159 -5.128 1.00 17.15 N ANISOU 1244 NE2 GLN A 152 2129 1971 2414 -91 -10 -233 N ATOM 1245 N GLY A 153 30.758 -30.187 -8.553 1.00 20.74 N ANISOU 1245 N GLY A 153 2614 2570 2695 99 -597 -176 N ATOM 1246 CA GLY A 153 29.606 -30.156 -9.449 1.00 21.84 C ANISOU 1246 CA GLY A 153 2552 2890 2853 275 -748 -160 C ATOM 1247 C GLY A 153 29.465 -31.452 -10.220 1.00 25.07 C ANISOU 1247 C GLY A 153 2891 3283 3349 235 -674 -189 C ATOM 1248 O GLY A 153 30.338 -32.319 -10.155 1.00 26.59 O ANISOU 1248 O GLY A 153 3201 3198 3703 417 -585 -312 O ATOM 1249 OXT GLY A 153 28.483 -31.672 -10.926 1.00 27.56 O ANISOU 1249 OXT GLY A 153 3121 3668 3682 -16 -755 -295 O TER 1250 GLY A 153 HETATM 1251 FE HEM A1154 16.805 -31.093 -3.299 1.00 9.44 FE ANISOU 1251 FE HEM A1154 1004 1320 1263 -1 -15 14 FE HETATM 1252 CHA HEM A1154 15.415 -34.229 -3.771 1.00 9.40 C ANISOU 1252 CHA HEM A1154 1032 1599 938 52 101 46 C HETATM 1253 CHB HEM A1154 15.514 -31.056 -0.106 1.00 9.41 C ANISOU 1253 CHB HEM A1154 1000 1113 1460 -4 -62 -13 C HETATM 1254 CHC HEM A1154 17.674 -27.768 -2.953 1.00 9.50 C ANISOU 1254 CHC HEM A1154 997 1525 1087 73 151 96 C HETATM 1255 CHD HEM A1154 17.605 -30.925 -6.641 1.00 9.34 C ANISOU 1255 CHD HEM A1154 902 1307 1339 46 -71 82 C HETATM 1256 NA HEM A1154 15.641 -32.386 -2.178 1.00 8.75 N ANISOU 1256 NA HEM A1154 954 1087 1284 -91 114 -44 N HETATM 1257 C1A HEM A1154 15.283 -33.670 -2.522 1.00 9.43 C ANISOU 1257 C1A HEM A1154 1017 1240 1324 61 -154 -1 C HETATM 1258 C2A HEM A1154 14.715 -34.322 -1.363 1.00 9.49 C ANISOU 1258 C2A HEM A1154 979 1339 1286 -37 -116 32 C HETATM 1259 C3A HEM A1154 14.737 -33.448 -0.354 1.00 9.81 C ANISOU 1259 C3A HEM A1154 1070 1243 1414 -71 -95 -7 C HETATM 1260 C4A HEM A1154 15.302 -32.207 -0.846 1.00 8.57 C ANISOU 1260 C4A HEM A1154 966 1041 1247 27 18 33 C HETATM 1261 CMA HEM A1154 14.234 -33.682 1.079 1.00 10.62 C ANISOU 1261 CMA HEM A1154 1307 1417 1309 -3 110 17 C HETATM 1262 CAA HEM A1154 14.231 -35.784 -1.333 1.00 10.38 C ANISOU 1262 CAA HEM A1154 1241 1286 1416 10 -220 64 C HETATM 1263 CBA HEM A1154 15.257 -36.640 -0.564 1.00 10.12 C ANISOU 1263 CBA HEM A1154 1075 1295 1474 -127 145 -15 C HETATM 1264 CGA HEM A1154 16.660 -36.643 -1.141 1.00 11.89 C ANISOU 1264 CGA HEM A1154 1413 1569 1533 -13 -69 50 C HETATM 1265 O1A HEM A1154 16.833 -37.024 -2.328 1.00 13.90 O ANISOU 1265 O1A HEM A1154 1462 1934 1885 11 34 -185 O HETATM 1266 O2A HEM A1154 17.630 -36.301 -0.400 1.00 11.83 O ANISOU 1266 O2A HEM A1154 1346 1632 1514 -28 -23 -59 O HETATM 1267 NB HEM A1154 16.588 -29.649 -1.809 1.00 8.62 N ANISOU 1267 NB HEM A1154 1115 1032 1127 27 -2 -280 N HETATM 1268 C1B HEM A1154 16.112 -29.884 -0.531 1.00 8.73 C ANISOU 1268 C1B HEM A1154 897 1075 1345 71 -46 -14 C HETATM 1269 C2B HEM A1154 16.331 -28.693 0.260 1.00 9.77 C ANISOU 1269 C2B HEM A1154 894 1486 1332 -86 80 38 C HETATM 1270 C3B HEM A1154 16.918 -27.787 -0.537 1.00 10.14 C ANISOU 1270 C3B HEM A1154 1064 1520 1266 30 9 16 C HETATM 1271 C4B HEM A1154 17.087 -28.371 -1.853 1.00 9.73 C ANISOU 1271 C4B HEM A1154 964 1433 1299 110 31 -87 C HETATM 1272 CMB HEM A1154 15.937 -28.558 1.748 1.00 10.40 C ANISOU 1272 CMB HEM A1154 1129 1395 1427 4 101 91 C HETATM 1273 CAB HEM A1154 17.345 -26.358 -0.177 1.00 10.57 C ANISOU 1273 CAB HEM A1154 1179 1469 1365 13 -31 95 C HETATM 1274 CBB HEM A1154 16.541 -25.566 0.544 1.00 11.51 C ANISOU 1274 CBB HEM A1154 1326 1730 1314 202 -97 42 C HETATM 1275 NC HEM A1154 17.517 -29.599 -4.578 1.00 9.04 N ANISOU 1275 NC HEM A1154 1165 1038 1230 119 145 236 N HETATM 1276 C1C HEM A1154 17.819 -28.305 -4.222 1.00 9.00 C ANISOU 1276 C1C HEM A1154 925 1335 1160 103 -35 65 C HETATM 1277 C2C HEM A1154 18.292 -27.624 -5.412 1.00 9.63 C ANISOU 1277 C2C HEM A1154 984 1262 1411 85 3 5 C HETATM 1278 C3C HEM A1154 18.253 -28.507 -6.431 1.00 10.24 C ANISOU 1278 C3C HEM A1154 1133 1385 1371 32 -40 -49 C HETATM 1279 C4C HEM A1154 17.772 -29.767 -5.918 1.00 10.15 C ANISOU 1279 C4C HEM A1154 1188 1130 1538 108 -157 -142 C HETATM 1280 CMC HEM A1154 18.736 -26.150 -5.433 1.00 10.88 C ANISOU 1280 CMC HEM A1154 1260 1454 1418 -133 178 53 C HETATM 1281 CAC HEM A1154 18.633 -28.327 -7.916 1.00 11.26 C ANISOU 1281 CAC HEM A1154 1142 1532 1603 163 -19 6 C HETATM 1282 CBC HEM A1154 18.968 -27.145 -8.430 1.00 13.05 C ANISOU 1282 CBC HEM A1154 1424 1740 1792 -82 -195 221 C HETATM 1283 ND HEM A1154 16.528 -32.360 -4.935 1.00 9.22 N ANISOU 1283 ND HEM A1154 1126 1033 1344 -131 -139 -41 N HETATM 1284 C1D HEM A1154 16.999 -32.081 -6.217 1.00 9.77 C ANISOU 1284 C1D HEM A1154 1074 1324 1311 -75 -101 -2 C HETATM 1285 C2D HEM A1154 16.724 -33.209 -7.068 1.00 10.01 C ANISOU 1285 C2D HEM A1154 978 1521 1305 -69 -204 -64 C HETATM 1286 C3D HEM A1154 16.043 -34.234 -6.187 1.00 10.45 C ANISOU 1286 C3D HEM A1154 1288 1501 1182 -77 -98 -6 C HETATM 1287 C4D HEM A1154 15.961 -33.627 -4.881 1.00 9.17 C ANISOU 1287 C4D HEM A1154 897 1287 1301 -89 -143 -32 C HETATM 1288 CMD HEM A1154 17.054 -33.365 -8.561 1.00 11.47 C ANISOU 1288 CMD HEM A1154 1261 2059 1035 -75 139 -119 C HETATM 1289 CAD HEM A1154 15.510 -35.601 -6.638 1.00 11.31 C ANISOU 1289 CAD HEM A1154 1244 1355 1696 -235 -142 -205 C HETATM 1290 CBD HEM A1154 14.136 -35.279 -7.244 1.00 13.88 C ANISOU 1290 CBD HEM A1154 1823 1774 1677 -377 -67 -235 C HETATM 1291 CGD HEM A1154 13.442 -36.460 -7.866 1.00 14.61 C ANISOU 1291 CGD HEM A1154 2032 1675 1842 -55 179 -60 C HETATM 1292 O1D HEM A1154 13.728 -36.790 -9.047 1.00 17.20 O ANISOU 1292 O1D HEM A1154 2707 1757 2071 -83 117 -183 O HETATM 1293 O2D HEM A1154 12.580 -37.058 -7.181 1.00 16.80 O ANISOU 1293 O2D HEM A1154 2237 1733 2414 -158 121 0 O