ATOM 1 N PRO A 1 3.465 -15.936 8.807 1.00 29.86 N ANISOU 1 N PRO A 1 3768 18 14 3846 3731 -224 N ATOM 2 CA PRO A 1 2.192 -15.707 8.090 1.00 27.73 C ANISOU 2 CA PRO A 1 3531 -43 115 3513 3489 -202 C ATOM 3 C PRO A 1 2.461 -15.862 6.583 1.00 25.69 C ANISOU 3 C PRO A 1 3143 -65 -32 3280 3336 -82 C ATOM 4 O PRO A 1 3.571 -15.579 6.145 1.00 27.52 O ANISOU 4 O PRO A 1 3312 -111 35 3668 3474 32 O ATOM 5 CB PRO A 1 1.914 -14.234 8.417 1.00 28.25 C ANISOU 5 CB PRO A 1 3572 14 -53 3727 3435 -40 C ATOM 6 CG PRO A 1 3.245 -13.668 8.575 1.00 29.56 C ANISOU 6 CG PRO A 1 3888 79 -26 3914 3429 -149 C ATOM 7 CD PRO A 1 3.960 -14.683 9.374 1.00 31.50 C ANISOU 7 CD PRO A 1 4042 37 74 4003 3922 -88 C ATOM 8 N ASN A 2 1.456 -16.221 5.791 1.00 23.43 N ANISOU 8 N ASN A 2 2865 -67 222 2704 3334 -163 N ATOM 9 CA ASN A 2 1.603 -16.249 4.306 1.00 20.43 C ANISOU 9 CA ASN A 2 2382 -26 86 2357 3024 -170 C ATOM 10 C ASN A 2 0.624 -15.239 3.735 1.00 17.75 C ANISOU 10 C ASN A 2 1965 -15 222 1998 2779 -213 C ATOM 11 O ASN A 2 -0.580 -15.429 3.800 1.00 18.07 O ANISOU 11 O ASN A 2 2173 -193 217 2098 2595 -55 O ATOM 12 CB ASN A 2 1.285 -17.630 3.722 1.00 22.89 C ANISOU 12 CB ASN A 2 2684 155 145 2446 3565 -77 C ATOM 13 CG ASN A 2 1.673 -17.779 2.348 1.00 21.56 C ANISOU 13 CG ASN A 2 2387 -198 -147 2223 3581 -252 C ATOM 14 OD1 ASN A 2 2.100 -16.829 1.637 1.00 22.63 O ANISOU 14 OD1 ASN A 2 3283 286 114 2152 3163 -718 O ATOM 15 ND2 ASN A 2 1.745 -19.041 1.955 1.00 28.14 N ANISOU 15 ND2 ASN A 2 3755 -123 -691 2273 4663 70 N ATOM 16 N PHE A 3 1.170 -14.154 3.172 1.00 16.51 N ANISOU 16 N PHE A 3 1815 -148 309 1887 2568 -62 N ATOM 17 CA PHE A 3 0.401 -13.065 2.567 1.00 16.15 C ANISOU 17 CA PHE A 3 1815 -7 141 1864 2458 -47 C ATOM 18 C PHE A 3 0.051 -13.359 1.104 1.00 16.37 C ANISOU 18 C PHE A 3 1858 -111 177 1855 2503 -34 C ATOM 19 O PHE A 3 -0.626 -12.569 0.466 1.00 16.62 O ANISOU 19 O PHE A 3 1893 81 217 1917 2504 -73 O ATOM 20 CB PHE A 3 1.236 -11.774 2.614 1.00 16.05 C ANISOU 20 CB PHE A 3 1888 -97 166 1837 2373 -28 C ATOM 21 CG PHE A 3 1.374 -11.131 3.967 1.00 16.10 C ANISOU 21 CG PHE A 3 1970 -31 131 1864 2283 -23 C ATOM 22 CD1 PHE A 3 2.208 -11.642 4.952 1.00 18.21 C ANISOU 22 CD1 PHE A 3 2078 -14 134 2320 2521 -53 C ATOM 23 CD2 PHE A 3 0.687 -9.977 4.270 1.00 16.16 C ANISOU 23 CD2 PHE A 3 2027 -43 103 1903 2210 -14 C ATOM 24 CE1 PHE A 3 2.289 -11.017 6.182 1.00 18.38 C ANISOU 24 CE1 PHE A 3 2062 17 324 2541 2378 -59 C ATOM 25 CE2 PHE A 3 0.806 -9.356 5.479 1.00 17.19 C ANISOU 25 CE2 PHE A 3 2128 -99 51 1954 2450 -8 C ATOM 26 CZ PHE A 3 1.611 -9.872 6.430 1.00 17.91 C ANISOU 26 CZ PHE A 3 2122 -191 -66 2536 2145 35 C ATOM 27 N SER A 4 0.508 -14.470 0.543 1.00 16.35 N ANISOU 27 N SER A 4 1870 -31 178 1712 2630 -262 N ATOM 28 CA SER A 4 0.304 -14.746 -0.861 1.00 16.85 C ANISOU 28 CA SER A 4 1891 -93 10 1805 2705 -207 C ATOM 29 C SER A 4 -1.144 -14.824 -1.236 1.00 17.64 C ANISOU 29 C SER A 4 2016 -94 262 1830 2853 -309 C ATOM 30 O SER A 4 -1.945 -15.429 -0.552 1.00 19.35 O ANISOU 30 O SER A 4 2081 -171 417 2017 3253 -426 O ATOM 31 CB SER A 4 0.963 -16.059 -1.247 1.00 17.80 C ANISOU 31 CB SER A 4 2139 29 -57 1798 2825 -327 C ATOM 32 OG SER A 4 2.360 -16.055 -1.004 1.00 18.45 O ANISOU 32 OG SER A 4 2002 136 -413 1950 3059 -382 O ATOM 33 N GLY A 5 -1.472 -14.275 -2.401 1.00 17.78 N ANISOU 33 N GLY A 5 2012 -203 210 1974 2770 -484 N ATOM 34 CA GLY A 5 -2.829 -14.382 -2.939 1.00 18.88 C ANISOU 34 CA GLY A 5 2059 -208 194 2102 3009 -335 C ATOM 35 C GLY A 5 -3.175 -13.235 -3.831 1.00 17.59 C ANISOU 35 C GLY A 5 1939 -113 143 2012 2731 -364 C ATOM 36 O GLY A 5 -2.384 -12.338 -4.070 1.00 17.45 O ANISOU 36 O GLY A 5 1923 -155 214 1904 2803 -285 O ATOM 37 N ASN A 6 -4.411 -13.270 -4.301 1.00 16.69 N ANISOU 37 N ASN A 6 1963 -157 137 1817 2560 -393 N ATOM 38 CA ASN A 6 -5.022 -12.194 -5.042 1.00 16.37 C ANISOU 38 CA ASN A 6 2047 5 95 1853 2318 -82 C ATOM 39 C ASN A 6 -6.033 -11.574 -4.122 1.00 15.92 C ANISOU 39 C ASN A 6 1876 -31 117 2006 2167 -86 C ATOM 40 O ASN A 6 -6.952 -12.250 -3.659 1.00 19.00 O ANISOU 40 O ASN A 6 2317 -409 -61 2303 2599 198 O ATOM 41 CB ASN A 6 -5.718 -12.721 -6.291 1.00 18.29 C ANISOU 41 CB ASN A 6 2248 85 22 2243 2458 -214 C ATOM 42 CG ASN A 6 -4.760 -13.180 -7.333 1.00 23.16 C ANISOU 42 CG ASN A 6 3043 49 -185 2892 2864 -128 C ATOM 43 OD1 ASN A 6 -3.897 -12.437 -7.805 1.00 25.54 O ANISOU 43 OD1 ASN A 6 3102 41 -441 3634 2968 302 O ATOM 44 ND2 ASN A 6 -4.920 -14.415 -7.723 1.00 29.03 N ANISOU 44 ND2 ASN A 6 3901 -41 -350 3241 3889 78 N ATOM 45 N TRP A 7 -5.892 -10.293 -3.856 1.00 15.34 N ANISOU 45 N TRP A 7 1783 -7 235 1820 2224 195 N ATOM 46 CA TRP A 7 -6.585 -9.585 -2.804 1.00 15.33 C ANISOU 46 CA TRP A 7 1826 25 250 1904 2093 121 C ATOM 47 C TRP A 7 -7.506 -8.535 -3.418 1.00 16.02 C ANISOU 47 C TRP A 7 1940 75 270 2022 2125 145 C ATOM 48 O TRP A 7 -7.145 -7.847 -4.383 1.00 18.02 O ANISOU 48 O TRP A 7 2080 290 364 2294 2470 114 O ATOM 49 CB TRP A 7 -5.563 -8.914 -1.880 1.00 14.92 C ANISOU 49 CB TRP A 7 1805 53 200 1841 2020 208 C ATOM 50 CG TRP A 7 -4.726 -9.892 -1.128 1.00 14.60 C ANISOU 50 CG TRP A 7 1705 9 229 1760 2082 23 C ATOM 51 CD1 TRP A 7 -3.505 -10.387 -1.516 1.00 15.24 C ANISOU 51 CD1 TRP A 7 1752 2 357 1823 2216 312 C ATOM 52 CD2 TRP A 7 -5.008 -10.463 0.145 1.00 14.24 C ANISOU 52 CD2 TRP A 7 1690 -114 129 1658 2063 1 C ATOM 53 NE1 TRP A 7 -3.040 -11.243 -0.563 1.00 15.96 N ANISOU 53 NE1 TRP A 7 1800 160 368 1973 2289 258 N ATOM 54 CE2 TRP A 7 -3.937 -11.317 0.469 1.00 15.36 C ANISOU 54 CE2 TRP A 7 1733 19 184 1895 2208 -46 C ATOM 55 CE3 TRP A 7 -6.059 -10.369 1.029 1.00 13.36 C ANISOU 55 CE3 TRP A 7 1728 -95 54 1643 1706 -25 C ATOM 56 CZ2 TRP A 7 -3.888 -12.017 1.658 1.00 15.13 C ANISOU 56 CZ2 TRP A 7 1713 -39 51 1775 2260 -160 C ATOM 57 CZ3 TRP A 7 -6.022 -11.084 2.195 1.00 14.18 C ANISOU 57 CZ3 TRP A 7 1842 -105 8 1689 1856 -35 C ATOM 58 CH2 TRP A 7 -4.954 -11.907 2.494 1.00 15.10 C ANISOU 58 CH2 TRP A 7 2100 -169 136 1729 1908 -84 C ATOM 59 N LYS A 8 -8.690 -8.429 -2.833 1.00 15.14 N ANISOU 59 N LYS A 8 1790 152 -27 1936 2026 -8 N ATOM 60 CA LYS A 8 -9.691 -7.461 -3.299 1.00 16.24 C ANISOU 60 CA LYS A 8 1954 130 -20 2193 2023 -88 C ATOM 61 C LYS A 8 -10.080 -6.562 -2.154 1.00 14.37 C ANISOU 61 C LYS A 8 1687 71 -6 2051 1719 -151 C ATOM 62 O LYS A 8 -10.191 -6.993 -1.017 1.00 14.88 O ANISOU 62 O LYS A 8 1967 143 11 1917 1769 -183 O ATOM 63 CB LYS A 8 -10.904 -8.099 -3.890 1.00 18.43 C ANISOU 63 CB LYS A 8 2174 245 -436 2527 2302 -152 C ATOM 64 CG LYS A 8 -11.677 -8.842 -3.022 0.70 18.73 C ANISOU 64 CG LYS A 8 2706 -82 -119 2322 2087 -260 C ATOM 65 CD LYS A 8 -12.986 -9.304 -3.759 0.70 21.26 C ANISOU 65 CD LYS A 8 2658 -223 -177 2978 2439 -88 C ATOM 66 CE LYS A 8 -13.887 -10.049 -2.843 0.70 25.80 C ANISOU 66 CE LYS A 8 3076 -406 -79 3379 3348 -90 C ATOM 67 NZ LYS A 8 -15.044 -10.669 -3.579 0.70 28.54 N ANISOU 67 NZ LYS A 8 3138 -494 -159 3969 3737 -169 N ATOM 68 N ILE A 9 -10.285 -5.291 -2.450 1.00 13.92 N ANISOU 68 N ILE A 9 1818 123 15 1914 1556 -26 N ATOM 69 CA ILE A 9 -10.526 -4.311 -1.396 1.00 14.13 C ANISOU 69 CA ILE A 9 1654 93 50 2003 1713 -65 C ATOM 70 C ILE A 9 -11.936 -4.410 -0.860 1.00 14.15 C ANISOU 70 C ILE A 9 1522 -20 133 2048 1805 -123 C ATOM 71 O ILE A 9 -12.910 -4.571 -1.622 1.00 15.96 O ANISOU 71 O ILE A 9 1719 189 62 2569 1775 -232 O ATOM 72 CB ILE A 9 -10.203 -2.892 -1.871 1.00 14.61 C ANISOU 72 CB ILE A 9 1897 226 57 2027 1625 98 C ATOM 73 CG1 ILE A 9 -9.970 -1.972 -0.688 1.00 14.31 C ANISOU 73 CG1 ILE A 9 1794 0 -8 1832 1809 172 C ATOM 74 CG2 ILE A 9 -11.295 -2.348 -2.824 1.00 16.53 C ANISOU 74 CG2 ILE A 9 2282 330 96 2232 1766 -85 C ATOM 75 CD1 ILE A 9 -9.358 -0.659 -1.063 1.00 16.00 C ANISOU 75 CD1 ILE A 9 1840 56 84 2095 2142 71 C ATOM 76 N ILE A 10 -12.076 -4.324 0.465 1.00 13.24 N ANISOU 76 N ILE A 10 1431 15 7 2018 1581 -68 N ATOM 77 CA ILE A 10 -13.383 -4.309 1.124 1.00 13.66 C ANISOU 77 CA ILE A 10 1346 42 -48 1980 1863 -74 C ATOM 78 C ILE A 10 -13.633 -3.064 1.959 1.00 13.37 C ANISOU 78 C ILE A 10 1452 37 161 1800 1825 -97 C ATOM 79 O ILE A 10 -14.780 -2.769 2.224 1.00 13.94 O ANISOU 79 O ILE A 10 1395 51 -33 1904 1995 -42 O ATOM 80 CB ILE A 10 -13.625 -5.590 1.937 1.00 14.18 C ANISOU 80 CB ILE A 10 1409 -3 -59 1950 2025 40 C ATOM 81 CG1 ILE A 10 -12.662 -5.744 3.102 1.00 14.38 C ANISOU 81 CG1 ILE A 10 1536 5 33 1918 2008 115 C ATOM 82 CG2 ILE A 10 -13.607 -6.786 1.028 1.00 15.18 C ANISOU 82 CG2 ILE A 10 1412 -9 -144 2209 2144 21 C ATOM 83 CD1 ILE A 10 -13.216 -6.653 4.219 1.00 16.17 C ANISOU 83 CD1 ILE A 10 1794 -53 134 2093 2255 158 C ATOM 84 N ARG A 11 -12.587 -2.352 2.369 1.00 13.16 N ANISOU 84 N ARG A 11 1346 117 24 1856 1799 -45 N ATOM 85 CA ARG A 11 -12.747 -1.120 3.081 1.00 13.31 C ANISOU 85 CA ARG A 11 1335 132 24 1895 1825 -7 C ATOM 86 C ARG A 11 -11.655 -0.163 2.686 1.00 13.20 C ANISOU 86 C ARG A 11 1553 72 33 1746 1717 -37 C ATOM 87 O ARG A 11 -10.506 -0.565 2.472 1.00 13.53 O ANISOU 87 O ARG A 11 1405 104 30 1776 1960 37 O ATOM 88 CB ARG A 11 -12.656 -1.318 4.636 1.00 14.21 C ANISOU 88 CB ARG A 11 1615 52 63 1891 1890 41 C ATOM 89 CG ARG A 11 -13.679 -2.238 5.291 1.00 15.05 C ANISOU 89 CG ARG A 11 1820 -6 7 2045 1852 87 C ATOM 90 CD ARG A 11 -15.101 -1.757 5.202 1.00 16.56 C ANISOU 90 CD ARG A 11 1878 8 41 2379 2034 99 C ATOM 91 NE ARG A 11 -15.269 -0.454 5.787 1.00 17.56 N ANISOU 91 NE ARG A 11 1714 60 83 2351 2606 309 N ATOM 92 CZ ARG A 11 -15.532 -0.223 7.066 1.00 17.84 C ANISOU 92 CZ ARG A 11 1784 242 -130 2443 2549 -36 C ATOM 93 NH1 ARG A 11 -15.691 -1.195 7.951 1.00 18.19 N ANISOU 93 NH1 ARG A 11 2168 248 -102 2747 1997 77 N ATOM 94 NH2 ARG A 11 -15.597 1.017 7.470 1.00 20.46 N ANISOU 94 NH2 ARG A 11 2174 258 -431 2588 3010 -31 N ATOM 95 N SER A 12 -11.970 1.127 2.656 1.00 13.45 N ANISOU 95 N SER A 12 1391 181 53 1799 1918 0 N ATOM 96 CA SER A 12 -11.020 2.185 2.420 1.00 14.16 C ANISOU 96 CA SER A 12 1588 109 74 1824 1966 42 C ATOM 97 C SER A 12 -11.415 3.405 3.231 1.00 14.26 C ANISOU 97 C SER A 12 1619 167 67 1891 1907 123 C ATOM 98 O SER A 12 -12.563 3.850 3.140 1.00 16.14 O ANISOU 98 O SER A 12 1728 319 -76 2077 2325 -3 O ATOM 99 CB SER A 12 -10.991 2.512 0.929 1.00 15.00 C ANISOU 99 CB SER A 12 1774 168 200 1993 1931 128 C ATOM 100 OG SER A 12 -10.060 3.528 0.663 1.00 17.19 O ANISOU 100 OG SER A 12 2027 60 204 2106 2395 301 O ATOM 101 N GLU A 13 -10.481 3.958 3.994 1.00 14.49 N ANISOU 101 N GLU A 13 1693 109 -4 1819 1994 173 N ATOM 102 CA GLU A 13 -10.753 5.064 4.880 1.00 15.44 C ANISOU 102 CA GLU A 13 1753 172 -19 1889 2224 108 C ATOM 103 C GLU A 13 -9.636 6.081 4.756 1.00 15.71 C ANISOU 103 C GLU A 13 1831 102 -80 1752 2384 140 C ATOM 104 O GLU A 13 -8.455 5.770 4.947 1.00 15.58 O ANISOU 104 O GLU A 13 1690 138 -14 1635 2594 50 O ATOM 105 CB GLU A 13 -10.870 4.584 6.336 1.00 16.48 C ANISOU 105 CB GLU A 13 2040 69 -147 1974 2247 174 C ATOM 106 CG GLU A 13 -11.367 5.622 7.284 1.00 18.19 C ANISOU 106 CG GLU A 13 2313 112 -140 2204 2392 125 C ATOM 107 CD GLU A 13 -12.790 5.948 7.096 1.00 21.94 C ANISOU 107 CD GLU A 13 2521 119 -326 2648 3166 273 C ATOM 108 OE1 GLU A 13 -13.554 5.051 6.818 1.00 26.55 O ANISOU 108 OE1 GLU A 13 2410 147 -318 3493 4183 371 O ATOM 109 OE2 GLU A 13 -13.156 7.129 7.273 1.00 26.52 O ANISOU 109 OE2 GLU A 13 3096 353 -468 2793 4185 81 O ATOM 110 N ASN A 14 -9.996 7.317 4.429 1.00 16.37 N ANISOU 110 N ASN A 14 1846 230 0 1768 2604 -25 N ATOM 111 CA ASN A 14 -9.117 8.469 4.450 1.00 17.20 C ANISOU 111 CA ASN A 14 2079 213 27 1763 2692 20 C ATOM 112 C ASN A 14 -8.133 8.563 3.304 1.00 16.76 C ANISOU 112 C ASN A 14 2066 177 -36 1646 2654 -60 C ATOM 113 O ASN A 14 -7.137 9.285 3.407 1.00 17.84 O ANISOU 113 O ASN A 14 2111 -37 -42 1866 2800 35 O ATOM 114 CB ASN A 14 -8.404 8.591 5.819 1.00 16.71 C ANISOU 114 CB ASN A 14 2161 201 -24 1670 2516 46 C ATOM 115 CG ASN A 14 -8.150 10.025 6.257 1.00 16.28 C ANISOU 115 CG ASN A 14 2121 274 -4 1885 2179 359 C ATOM 116 OD1 ASN A 14 -8.914 10.941 5.934 1.00 18.92 O ANISOU 116 OD1 ASN A 14 2613 287 -31 1814 2761 356 O ATOM 117 ND2 ASN A 14 -7.092 10.204 7.014 1.00 18.17 N ANISOU 117 ND2 ASN A 14 2617 -21 -175 1976 2308 220 N ATOM 118 N PHE A 15 -8.360 7.841 2.210 1.00 16.39 N ANISOU 118 N PHE A 15 2065 86 -46 1548 2611 137 N ATOM 119 CA PHE A 15 -7.404 7.857 1.082 1.00 16.87 C ANISOU 119 CA PHE A 15 2101 121 -53 1722 2585 110 C ATOM 120 C PHE A 15 -7.324 9.206 0.370 1.00 16.56 C ANISOU 120 C PHE A 15 1872 56 -40 1803 2615 -62 C ATOM 121 O PHE A 15 -6.250 9.740 0.137 1.00 17.53 O ANISOU 121 O PHE A 15 1913 -124 1 1833 2914 -170 O ATOM 122 CB PHE A 15 -7.741 6.728 0.085 1.00 16.97 C ANISOU 122 CB PHE A 15 2051 121 -49 1691 2704 144 C ATOM 123 CG PHE A 15 -6.774 6.596 -1.086 1.00 17.77 C ANISOU 123 CG PHE A 15 2239 -25 85 1739 2773 166 C ATOM 124 CD1 PHE A 15 -5.419 6.550 -0.873 1.00 19.31 C ANISOU 124 CD1 PHE A 15 2244 51 104 2186 2906 -13 C ATOM 125 CD2 PHE A 15 -7.243 6.444 -2.367 1.00 20.82 C ANISOU 125 CD2 PHE A 15 2488 148 -165 2483 2938 398 C ATOM 126 CE1 PHE A 15 -4.527 6.384 -1.985 1.00 19.80 C ANISOU 126 CE1 PHE A 15 2346 -25 111 2206 2969 280 C ATOM 127 CE2 PHE A 15 -6.377 6.307 -3.451 1.00 22.46 C ANISOU 127 CE2 PHE A 15 2955 -66 -152 2940 2639 73 C ATOM 128 CZ PHE A 15 -5.035 6.287 -3.235 1.00 20.93 C ANISOU 128 CZ PHE A 15 2659 -11 -12 2352 2940 501 C ATOM 129 N GLU A 16 -8.457 9.783 0.016 1.00 17.41 N ANISOU 129 N GLU A 16 2043 -32 6 1850 2720 -151 N ATOM 130 CA GLU A 16 -8.423 11.062 -0.671 1.00 18.85 C ANISOU 130 CA GLU A 16 2360 41 128 1980 2821 -143 C ATOM 131 C GLU A 16 -7.757 12.147 0.157 1.00 18.82 C ANISOU 131 C GLU A 16 2515 72 105 1927 2705 -105 C ATOM 132 O GLU A 16 -6.998 12.971 -0.367 1.00 19.35 O ANISOU 132 O GLU A 16 2931 -44 113 1830 2589 -110 O ATOM 133 CB GLU A 16 -9.810 11.545 -1.100 1.00 20.60 C ANISOU 133 CB GLU A 16 2423 246 90 2334 3068 -164 C ATOM 134 CG GLU A 16 -9.621 12.851 -1.911 1.00 23.43 C ANISOU 134 CG GLU A 16 2921 310 237 2600 3382 -97 C ATOM 135 CD GLU A 16 -10.781 13.510 -2.526 1.00 26.46 C ANISOU 135 CD GLU A 16 3106 91 262 3213 3735 -146 C ATOM 136 OE1 GLU A 16 -11.845 12.919 -2.576 1.00 31.10 O ANISOU 136 OE1 GLU A 16 2705 11 95 4411 4700 -561 O ATOM 137 OE2 GLU A 16 -10.554 14.647 -3.040 1.00 28.96 O ANISOU 137 OE2 GLU A 16 3106 4 707 3321 4574 -266 O ATOM 138 N GLU A 17 -8.003 12.123 1.454 1.00 18.99 N ANISOU 138 N GLU A 17 2922 33 79 1585 2707 -57 N ATOM 139 CA GLU A 17 -7.421 13.112 2.361 1.00 20.67 C ANISOU 139 CA GLU A 17 3286 38 83 1780 2784 -46 C ATOM 140 C GLU A 17 -5.916 12.978 2.487 1.00 21.08 C ANISOU 140 C GLU A 17 3440 -271 147 1863 2706 -291 C ATOM 141 O GLU A 17 -5.163 13.962 2.546 1.00 23.61 O ANISOU 141 O GLU A 17 4015 -605 78 2046 2907 -576 O ATOM 142 CB GLU A 17 -8.154 12.976 3.700 1.00 24.09 C ANISOU 142 CB GLU A 17 3830 92 97 2370 2954 11 C ATOM 143 CG GLU A 17 -9.715 13.239 3.704 1.00 27.59 C ANISOU 143 CG GLU A 17 3895 51 49 3296 3292 265 C ATOM 144 CD GLU A 17 -10.691 12.104 3.210 1.00 29.62 C ANISOU 144 CD GLU A 17 3482 151 -12 3814 3958 226 C ATOM 145 OE1 GLU A 17 -10.307 10.990 2.739 1.00 25.92 O ANISOU 145 OE1 GLU A 17 2686 463 610 3158 4005 290 O ATOM 146 OE2 GLU A 17 -11.940 12.346 3.309 1.00 34.95 O ANISOU 146 OE2 GLU A 17 3974 126 122 4302 5000 322 O ATOM 147 N LEU A 18 -5.428 11.756 2.501 1.00 20.07 N ANISOU 147 N LEU A 18 2947 -187 190 1904 2774 -258 N ATOM 148 CA LEU A 18 -4.007 11.507 2.451 1.00 20.67 C ANISOU 148 CA LEU A 18 2763 -318 240 2264 2824 -406 C ATOM 149 C LEU A 18 -3.394 12.119 1.195 1.00 19.77 C ANISOU 149 C LEU A 18 2574 -484 269 2273 2665 -500 C ATOM 150 O LEU A 18 -2.360 12.818 1.265 1.00 22.95 O ANISOU 150 O LEU A 18 3057 -973 507 2908 2754 -659 O ATOM 151 CB LEU A 18 -3.778 10.015 2.447 1.00 20.23 C ANISOU 151 CB LEU A 18 2371 -98 400 2370 2945 -463 C ATOM 152 CG LEU A 18 -2.298 9.668 2.340 1.00 22.73 C ANISOU 152 CG LEU A 18 2489 -231 436 2959 3187 -286 C ATOM 153 CD1 LEU A 18 -1.501 10.253 3.526 1.00 28.51 C ANISOU 153 CD1 LEU A 18 3480 -229 116 3749 3602 -169 C ATOM 154 CD2 LEU A 18 -2.158 8.200 2.217 1.00 25.84 C ANISOU 154 CD2 LEU A 18 2777 30 471 3190 3849 -65 C ATOM 155 N LEU A 19 -3.998 11.905 0.049 1.00 19.13 N ANISOU 155 N LEU A 19 2607 -416 137 2017 2643 -530 N ATOM 156 CA LEU A 19 -3.514 12.548 -1.169 1.00 18.96 C ANISOU 156 CA LEU A 19 2531 -278 68 2026 2644 -406 C ATOM 157 C LEU A 19 -3.571 14.088 -1.125 1.00 19.61 C ANISOU 157 C LEU A 19 2775 -493 90 2059 2614 -602 C ATOM 158 O LEU A 19 -2.636 14.779 -1.583 1.00 20.93 O ANISOU 158 O LEU A 19 2732 -611 301 2202 3018 -661 O ATOM 159 CB LEU A 19 -4.298 12.050 -2.398 1.00 19.39 C ANISOU 159 CB LEU A 19 2476 -326 -21 2097 2794 -396 C ATOM 160 CG LEU A 19 -4.190 10.537 -2.696 1.00 19.15 C ANISOU 160 CG LEU A 19 2305 -96 92 1941 3029 -358 C ATOM 161 CD1 LEU A 19 -4.995 10.256 -3.913 1.00 20.67 C ANISOU 161 CD1 LEU A 19 2668 -83 -178 1997 3187 -293 C ATOM 162 CD2 LEU A 19 -2.740 10.065 -2.926 1.00 21.41 C ANISOU 162 CD2 LEU A 19 2661 -40 0 2449 3022 -240 C ATOM 163 N LYS A 20 -4.645 14.597 -0.533 1.00 19.46 N ANISOU 163 N LYS A 20 3099 -438 120 1740 2553 -461 N ATOM 164 CA LYS A 20 -4.866 16.045 -0.415 1.00 20.86 C ANISOU 164 CA LYS A 20 3471 -418 109 1877 2578 -471 C ATOM 165 C LYS A 20 -3.818 16.720 0.431 1.00 21.55 C ANISOU 165 C LYS A 20 3725 -610 219 1833 2629 -556 C ATOM 166 O LYS A 20 -3.259 17.737 0.030 1.00 22.92 O ANISOU 166 O LYS A 20 4118 -914 292 1990 2601 -834 O ATOM 167 CB LYS A 20 -6.262 16.346 0.095 1.00 20.80 C ANISOU 167 CB LYS A 20 3670 -339 200 1709 2523 -359 C ATOM 168 CG LYS A 20 -6.660 17.824 0.073 1.00 21.14 C ANISOU 168 CG LYS A 20 3597 -335 15 1746 2686 -143 C ATOM 169 CD LYS A 20 -8.114 18.019 0.447 1.00 23.06 C ANISOU 169 CD LYS A 20 3780 -259 74 1994 2987 -90 C ATOM 170 CE LYS A 20 -8.570 19.451 0.422 1.00 24.12 C ANISOU 170 CE LYS A 20 3954 -85 -88 2217 2993 -7 C ATOM 171 NZ LYS A 20 -9.948 19.557 0.928 1.00 28.45 N ANISOU 171 NZ LYS A 20 4206 -39 -98 2737 3866 205 N ATOM 172 N VAL A 21 -3.551 16.174 1.606 1.00 23.04 N ANISOU 172 N VAL A 21 3892 -760 151 2222 2640 -738 N ATOM 173 CA VAL A 21 -2.582 16.841 2.469 1.00 23.90 C ANISOU 173 CA VAL A 21 3751 -597 174 2503 2827 -642 C ATOM 174 C VAL A 21 -1.189 16.698 1.927 1.00 24.35 C ANISOU 174 C VAL A 21 3560 -621 348 2805 2886 -775 C ATOM 175 O VAL A 21 -0.312 17.463 2.379 1.00 27.58 O ANISOU 175 O VAL A 21 4000 -1221 178 2983 3493 -827 O ATOM 176 CB VAL A 21 -2.566 16.338 3.917 1.00 24.37 C ANISOU 176 CB VAL A 21 3823 -625 136 2647 2790 -644 C ATOM 177 CG1 VAL A 21 -3.867 16.496 4.531 1.00 27.19 C ANISOU 177 CG1 VAL A 21 4064 -57 55 2881 3384 -512 C ATOM 178 CG2 VAL A 21 -2.020 14.888 3.973 1.00 24.58 C ANISOU 178 CG2 VAL A 21 3727 -574 89 2711 2901 -483 C ATOM 179 N LEU A 22 -0.932 15.807 0.982 1.00 24.82 N ANISOU 179 N LEU A 22 3457 -638 503 2812 3159 -711 N ATOM 180 CA LEU A 22 0.264 15.712 0.187 1.00 25.17 C ANISOU 180 CA LEU A 22 3332 -339 377 3164 3067 -750 C ATOM 181 C LEU A 22 0.373 16.736 -0.951 1.00 25.79 C ANISOU 181 C LEU A 22 3170 -376 449 3162 3465 -586 C ATOM 182 O LEU A 22 1.449 16.909 -1.531 1.00 28.50 O ANISOU 182 O LEU A 22 3147 -164 798 3815 3864 -604 O ATOM 183 CB LEU A 22 0.518 14.302 -0.340 1.00 25.44 C ANISOU 183 CB LEU A 22 3191 -327 455 3349 3123 -770 C ATOM 184 CG LEU A 22 0.883 13.225 0.708 1.00 26.35 C ANISOU 184 CG LEU A 22 3131 -158 410 3563 3318 -697 C ATOM 185 CD1 LEU A 22 0.834 11.857 0.149 1.00 27.83 C ANISOU 185 CD1 LEU A 22 3245 39 325 3754 3572 -490 C ATOM 186 CD2 LEU A 22 2.285 13.502 1.271 1.00 27.25 C ANISOU 186 CD2 LEU A 22 3156 -138 396 3665 3533 -692 C ATOM 187 N GLY A 23 -0.693 17.437 -1.242 1.00 24.15 N ANISOU 187 N GLY A 23 3065 -540 471 2854 3255 -733 N ATOM 188 CA GLY A 23 -0.667 18.419 -2.307 1.00 23.31 C ANISOU 188 CA GLY A 23 3018 -416 374 2817 3021 -619 C ATOM 189 C GLY A 23 -1.096 17.887 -3.662 1.00 22.42 C ANISOU 189 C GLY A 23 2904 -366 307 2657 2955 -584 C ATOM 190 O GLY A 23 -0.936 18.590 -4.655 1.00 23.60 O ANISOU 190 O GLY A 23 3223 -598 398 2771 2971 -490 O ATOM 191 N VAL A 24 -1.688 16.691 -3.734 1.00 20.32 N ANISOU 191 N VAL A 24 2676 -281 311 2269 2773 -449 N ATOM 192 CA VAL A 24 -2.140 16.191 -5.015 1.00 21.24 C ANISOU 192 CA VAL A 24 2626 -133 140 2525 2919 -355 C ATOM 193 C VAL A 24 -3.345 17.009 -5.449 1.00 20.16 C ANISOU 193 C VAL A 24 2521 -137 -8 2411 2726 -315 C ATOM 194 O VAL A 24 -4.260 17.237 -4.679 1.00 19.05 O ANISOU 194 O VAL A 24 2464 -122 -134 2226 2547 -470 O ATOM 195 CB VAL A 24 -2.508 14.665 -4.939 1.00 20.81 C ANISOU 195 CB VAL A 24 2493 -48 226 2445 2967 -320 C ATOM 196 CG1 VAL A 24 -3.090 14.234 -6.276 1.00 22.08 C ANISOU 196 CG1 VAL A 24 2704 69 -75 2510 3175 -286 C ATOM 197 CG2 VAL A 24 -1.262 13.799 -4.547 1.00 22.64 C ANISOU 197 CG2 VAL A 24 2603 177 99 2836 3163 -78 C ATOM 198 N ASN A 25 -3.339 17.458 -6.695 1.00 20.95 N ANISOU 198 N ASN A 25 2718 45 -71 2551 2691 -322 N ATOM 199 CA ASN A 25 -4.386 18.334 -7.177 1.00 22.44 C ANISOU 199 CA ASN A 25 2892 36 -39 2779 2853 -307 C ATOM 200 C ASN A 25 -5.715 17.625 -7.285 1.00 22.35 C ANISOU 200 C ASN A 25 2979 65 -160 2792 2719 -396 C ATOM 201 O ASN A 25 -5.768 16.411 -7.365 1.00 22.60 O ANISOU 201 O ASN A 25 2846 -4 -236 2847 2891 -734 O ATOM 202 CB ASN A 25 -3.951 19.021 -8.483 1.00 23.89 C ANISOU 202 CB ASN A 25 3254 28 23 2857 2963 -273 C ATOM 203 CG ASN A 25 -4.014 18.108 -9.704 1.00 27.56 C ANISOU 203 CG ASN A 25 3493 105 -87 3620 3356 18 C ATOM 204 OD1 ASN A 25 -5.021 17.503 -9.975 1.00 31.71 O ANISOU 204 OD1 ASN A 25 4147 -93 -513 4537 3364 -38 O ATOM 205 ND2 ASN A 25 -2.939 18.070 -10.473 1.00 31.90 N ANISOU 205 ND2 ASN A 25 3915 71 -31 4563 3641 324 N ATOM 206 N VAL A 26 -6.802 18.386 -7.296 1.00 21.74 N ANISOU 206 N VAL A 26 2857 126 -189 2684 2719 -329 N ATOM 207 CA VAL A 26 -8.121 17.781 -7.191 1.00 23.44 C ANISOU 207 CA VAL A 26 3035 100 -179 2919 2948 -372 C ATOM 208 C VAL A 26 -8.463 16.893 -8.381 1.00 24.27 C ANISOU 208 C VAL A 26 3062 74 -156 3136 3024 -416 C ATOM 209 O VAL A 26 -9.088 15.881 -8.190 1.00 23.85 O ANISOU 209 O VAL A 26 2952 176 -457 3008 3101 -763 O ATOM 210 CB VAL A 26 -9.216 18.861 -6.938 1.00 24.16 C ANISOU 210 CB VAL A 26 2990 84 -176 3019 3168 -326 C ATOM 211 CG1 VAL A 26 -9.354 19.798 -8.154 1.00 25.47 C ANISOU 211 CG1 VAL A 26 3174 95 -66 3228 3273 -297 C ATOM 212 CG2 VAL A 26 -10.524 18.205 -6.503 1.00 25.17 C ANISOU 212 CG2 VAL A 26 3191 76 -144 3107 3262 -268 C ATOM 213 N MET A 27 -8.043 17.276 -9.582 1.00 25.51 N ANISOU 213 N MET A 27 3316 -54 -312 3321 3055 -378 N ATOM 214 CA MET A 27 -8.377 16.482 -10.780 1.00 27.05 C ANISOU 214 CA MET A 27 3478 -31 -304 3495 3304 -347 C ATOM 215 C MET A 27 -7.702 15.140 -10.666 1.00 27.85 C ANISOU 215 C MET A 27 3607 -50 -354 3582 3392 -299 C ATOM 216 O MET A 27 -8.294 14.068 -10.907 1.00 28.26 O ANISOU 216 O MET A 27 3626 -32 -529 3528 3583 -388 O ATOM 217 CB MET A 27 -7.923 17.225 -12.018 1.00 29.06 C ANISOU 217 CB MET A 27 3772 -94 -318 3763 3505 -246 C ATOM 218 N LEU A 28 -6.451 15.170 -10.245 1.00 27.32 N ANISOU 218 N LEU A 28 3529 21 -478 3476 3372 -198 N ATOM 219 CA LEU A 28 -5.702 13.959 -10.100 1.00 27.85 C ANISOU 219 CA LEU A 28 3615 -1 -405 3452 3515 -275 C ATOM 220 C LEU A 28 -6.190 13.151 -8.933 1.00 26.55 C ANISOU 220 C LEU A 28 3435 68 -504 3167 3483 -339 C ATOM 221 O LEU A 28 -6.222 11.944 -9.021 1.00 28.65 O ANISOU 221 O LEU A 28 3465 121 -715 3378 4041 -513 O ATOM 222 CB LEU A 28 -4.221 14.288 -10.002 1.00 29.29 C ANISOU 222 CB LEU A 28 3639 -11 -331 3720 3768 -215 C ATOM 223 CG LEU A 28 -3.228 13.162 -10.179 1.00 29.34 C ANISOU 223 CG LEU A 28 3736 -57 -210 3727 3684 -98 C ATOM 224 CD1 LEU A 28 -3.536 12.334 -11.400 1.00 29.87 C ANISOU 224 CD1 LEU A 28 3837 -24 -262 3697 3813 55 C ATOM 225 CD2 LEU A 28 -1.852 13.718 -10.219 1.00 30.57 C ANISOU 225 CD2 LEU A 28 3816 -99 -113 3954 3843 -146 C ATOM 226 N ARG A 29 -6.587 13.788 -7.814 1.00 24.58 N ANISOU 226 N ARG A 29 3295 222 -642 2893 3150 -361 N ATOM 227 CA ARG A 29 -7.207 13.057 -6.693 1.00 24.02 C ANISOU 227 CA ARG A 29 3278 124 -498 2593 3253 -426 C ATOM 228 C ARG A 29 -8.443 12.315 -7.082 1.00 25.08 C ANISOU 228 C ARG A 29 3463 168 -435 2691 3376 -436 C ATOM 229 O ARG A 29 -8.694 11.179 -6.631 1.00 25.88 O ANISOU 229 O ARG A 29 3909 110 -565 2272 3649 -751 O ATOM 230 CB ARG A 29 -7.608 13.972 -5.501 1.00 25.36 C ANISOU 230 CB ARG A 29 3368 160 -360 2939 3326 -347 C ATOM 231 CG ARG A 29 -6.473 14.536 -4.730 1.00 23.57 C ANISOU 231 CG ARG A 29 2937 108 -240 2825 3194 -198 C ATOM 232 CD ARG A 29 -6.833 15.106 -3.401 1.00 21.26 C ANISOU 232 CD ARG A 29 2821 -109 -296 2368 2885 -281 C ATOM 233 NE ARG A 29 -8.007 15.969 -3.291 1.00 20.03 N ANISOU 233 NE ARG A 29 2485 -253 -3 2193 2932 -144 N ATOM 234 CZ ARG A 29 -8.025 17.295 -3.418 1.00 18.48 C ANISOU 234 CZ ARG A 29 2290 -68 -42 2274 2457 -130 C ATOM 235 NH1 ARG A 29 -6.988 17.947 -3.863 1.00 18.59 N ANISOU 235 NH1 ARG A 29 2476 -174 -115 2117 2469 11 N ATOM 236 NH2 ARG A 29 -9.138 17.941 -3.198 1.00 21.46 N ANISOU 236 NH2 ARG A 29 2530 -164 -108 2516 3108 -8 N ATOM 237 N LYS A 30 -9.265 12.988 -7.868 1.00 24.06 N ANISOU 237 N LYS A 30 3330 234 -503 2616 3194 -570 N ATOM 238 CA LYS A 30 -10.502 12.391 -8.310 1.00 24.91 C ANISOU 238 CA LYS A 30 3327 116 -315 2861 3275 -341 C ATOM 239 C LYS A 30 -10.208 11.207 -9.200 1.00 23.20 C ANISOU 239 C LYS A 30 3182 25 -377 2792 2839 -463 C ATOM 240 O LYS A 30 -10.837 10.175 -8.996 1.00 25.92 O ANISOU 240 O LYS A 30 3555 193 -253 2906 3385 -597 O ATOM 241 CB LYS A 30 -11.423 13.388 -8.983 1.00 24.42 C ANISOU 241 CB LYS A 30 3270 204 -382 2748 3259 -297 C ATOM 242 N ILE A 31 -9.269 11.341 -10.139 1.00 24.46 N ANISOU 242 N ILE A 31 3428 -112 -409 2641 3224 -380 N ATOM 243 CA ILE A 31 -8.902 10.240 -11.058 1.00 25.39 C ANISOU 243 CA ILE A 31 3547 -125 -375 2908 3188 -152 C ATOM 244 C ILE A 31 -8.312 9.133 -10.249 1.00 24.41 C ANISOU 244 C ILE A 31 3552 -132 -496 2690 3030 -118 C ATOM 245 O ILE A 31 -8.638 7.954 -10.459 1.00 24.34 O ANISOU 245 O ILE A 31 3670 -81 -501 2405 3172 3 O ATOM 246 CB ILE A 31 -7.933 10.761 -12.197 1.00 26.86 C ANISOU 246 CB ILE A 31 3791 -111 -375 3033 3379 -66 C ATOM 247 CG1 ILE A 31 -8.696 11.713 -13.114 1.00 28.40 C ANISOU 247 CG1 ILE A 31 3981 -116 -257 3474 3335 -112 C ATOM 248 CG2 ILE A 31 -7.341 9.643 -12.966 1.00 27.98 C ANISOU 248 CG2 ILE A 31 3870 -55 -220 3248 3513 50 C ATOM 249 CD1 ILE A 31 -7.849 12.491 -14.060 1.00 29.25 C ANISOU 249 CD1 ILE A 31 4071 -94 -170 3423 3619 -14 C ATOM 250 N ALA A 32 -7.392 9.457 -9.350 1.00 23.29 N ANISOU 250 N ALA A 32 3240 -172 -299 2593 3013 -90 N ATOM 251 CA ALA A 32 -6.705 8.425 -8.574 1.00 23.29 C ANISOU 251 CA ALA A 32 3183 -142 -315 2731 2933 -97 C ATOM 252 C ALA A 32 -7.656 7.677 -7.657 1.00 21.96 C ANISOU 252 C ALA A 32 2952 -165 -363 2616 2773 -249 C ATOM 253 O ALA A 32 -7.587 6.455 -7.592 1.00 23.29 O ANISOU 253 O ALA A 32 3220 -190 -273 2666 2960 -83 O ATOM 254 CB ALA A 32 -5.575 9.041 -7.766 1.00 24.14 C ANISOU 254 CB ALA A 32 3235 -228 -170 2831 3106 -96 C ATOM 255 N VAL A 33 -8.582 8.365 -7.027 1.00 22.58 N ANISOU 255 N VAL A 33 3099 -232 -375 2628 2852 -243 N ATOM 256 CA VAL A 33 -9.563 7.727 -6.124 1.00 21.03 C ANISOU 256 CA VAL A 33 2997 -132 -251 2429 2563 -196 C ATOM 257 C VAL A 33 -10.432 6.766 -6.904 1.00 21.31 C ANISOU 257 C VAL A 33 2870 93 -174 2566 2661 -21 C ATOM 258 O VAL A 33 -10.616 5.626 -6.474 1.00 21.26 O ANISOU 258 O VAL A 33 3002 98 -221 2440 2634 293 O ATOM 259 CB VAL A 33 -10.312 8.804 -5.304 1.00 23.98 C ANISOU 259 CB VAL A 33 3303 39 -113 2812 2995 -111 C ATOM 260 CG1 VAL A 33 -11.415 8.186 -4.479 1.00 26.02 C ANISOU 260 CG1 VAL A 33 3486 -43 -97 3025 3374 -32 C ATOM 261 CG2 VAL A 33 -9.364 9.490 -4.306 1.00 25.37 C ANISOU 261 CG2 VAL A 33 3648 75 -168 3048 2943 -62 C ATOM 262 N ALA A 34 -10.989 7.242 -8.005 1.00 21.69 N ANISOU 262 N ALA A 34 3027 120 -100 2532 2680 -38 N ATOM 263 CA ALA A 34 -11.833 6.403 -8.806 1.00 21.93 C ANISOU 263 CA ALA A 34 2906 41 -20 2678 2747 -11 C ATOM 264 C ALA A 34 -11.089 5.235 -9.409 1.00 21.56 C ANISOU 264 C ALA A 34 2789 51 -29 2710 2692 29 C ATOM 265 O ALA A 34 -11.582 4.107 -9.358 1.00 21.89 O ANISOU 265 O ALA A 34 2780 21 78 2865 2670 55 O ATOM 266 CB ALA A 34 -12.579 7.177 -9.828 1.00 22.26 C ANISOU 266 CB ALA A 34 2988 123 -69 2609 2859 -223 C ATOM 267 N ALA A 35 -9.885 5.465 -9.938 1.00 20.99 N ANISOU 267 N ALA A 35 2787 17 79 2542 2645 35 N ATOM 268 CA ALA A 35 -9.081 4.418 -10.523 1.00 21.20 C ANISOU 268 CA ALA A 35 2918 -31 0 2595 2540 104 C ATOM 269 C ALA A 35 -8.763 3.312 -9.546 1.00 21.04 C ANISOU 269 C ALA A 35 2718 -22 -88 2617 2659 -39 C ATOM 270 O ALA A 35 -8.655 2.161 -9.944 1.00 21.45 O ANISOU 270 O ALA A 35 2727 -25 -158 2754 2666 148 O ATOM 271 CB ALA A 35 -7.817 4.968 -11.042 1.00 21.55 C ANISOU 271 CB ALA A 35 2826 77 -73 2586 2774 4 C ATOM 272 N ALA A 36 -8.579 3.670 -8.278 1.00 21.39 N ANISOU 272 N ALA A 36 2799 -1 -58 2631 2697 15 N ATOM 273 CA ALA A 36 -8.168 2.715 -7.232 1.00 22.26 C ANISOU 273 CA ALA A 36 2791 39 133 2920 2745 20 C ATOM 274 C ALA A 36 -9.350 2.198 -6.431 1.00 20.69 C ANISOU 274 C ALA A 36 2837 69 -201 2489 2533 79 C ATOM 275 O ALA A 36 -9.157 1.563 -5.411 1.00 22.97 O ANISOU 275 O ALA A 36 3347 -192 -3 2721 2659 18 O ATOM 276 CB ALA A 36 -7.163 3.427 -6.274 1.00 22.67 C ANISOU 276 CB ALA A 36 2679 -12 88 3000 2935 -82 C ATOM 277 N SER A 37 -10.570 2.413 -6.875 1.00 21.34 N ANISOU 277 N SER A 37 2912 136 -192 2575 2617 236 N ATOM 278 CA SER A 37 -11.704 1.966 -6.045 1.00 22.09 C ANISOU 278 CA SER A 37 2839 179 28 2763 2790 240 C ATOM 279 C SER A 37 -11.880 0.434 -5.961 1.00 20.81 C ANISOU 279 C SER A 37 2594 219 85 2721 2589 194 C ATOM 280 O SER A 37 -12.389 -0.044 -4.979 1.00 21.53 O ANISOU 280 O SER A 37 2589 210 235 2759 2831 311 O ATOM 281 CB SER A 37 -12.986 2.644 -6.479 1.00 24.29 C ANISOU 281 CB SER A 37 3067 152 157 3006 3156 179 C ATOM 282 OG SER A 37 -13.264 2.226 -7.758 1.00 27.23 O ANISOU 282 OG SER A 37 3402 224 180 3490 3453 244 O ATOM 283 N LYS A 38 -11.370 -0.311 -6.918 1.00 20.83 N ANISOU 283 N LYS A 38 2680 52 -21 2638 2594 270 N ATOM 284 CA LYS A 38 -11.450 -1.769 -6.975 1.00 22.62 C ANISOU 284 CA LYS A 38 2815 129 14 2820 2959 199 C ATOM 285 C LYS A 38 -10.158 -2.275 -7.592 1.00 22.39 C ANISOU 285 C LYS A 38 2874 119 -25 2815 2819 275 C ATOM 286 O LYS A 38 -10.118 -2.797 -8.734 1.00 24.42 O ANISOU 286 O LYS A 38 3223 161 -198 3025 3028 190 O ATOM 287 CB LYS A 38 -12.602 -2.202 -7.810 1.00 24.34 C ANISOU 287 CB LYS A 38 3073 45 -59 2937 3236 90 C ATOM 288 N PRO A 39 -9.072 -2.145 -6.858 1.00 20.85 N ANISOU 288 N PRO A 39 2769 158 139 2542 2608 337 N ATOM 289 CA PRO A 39 -7.789 -2.488 -7.417 1.00 21.00 C ANISOU 289 CA PRO A 39 2551 309 289 2506 2922 275 C ATOM 290 C PRO A 39 -7.587 -3.995 -7.483 1.00 22.18 C ANISOU 290 C PRO A 39 2743 234 330 2586 3099 448 C ATOM 291 O PRO A 39 -8.213 -4.770 -6.751 1.00 25.11 O ANISOU 291 O PRO A 39 3098 240 413 2849 3593 638 O ATOM 292 CB PRO A 39 -6.812 -1.833 -6.431 1.00 20.11 C ANISOU 292 CB PRO A 39 2241 287 190 2719 2678 403 C ATOM 293 CG PRO A 39 -7.539 -1.834 -5.119 1.00 23.02 C ANISOU 293 CG PRO A 39 2956 242 45 2836 2955 207 C ATOM 294 CD PRO A 39 -9.002 -1.679 -5.469 1.00 21.70 C ANISOU 294 CD PRO A 39 2999 121 307 2645 2598 272 C ATOM 295 N ALA A 40 -6.679 -4.411 -8.337 1.00 22.90 N ANISOU 295 N ALA A 40 2345 186 438 2822 3532 448 N ATOM 296 CA ALA A 40 -6.238 -5.778 -8.333 1.00 21.29 C ANISOU 296 CA ALA A 40 2246 42 405 2603 3240 315 C ATOM 297 C ALA A 40 -4.897 -5.761 -7.464 1.00 20.90 C ANISOU 297 C ALA A 40 1880 50 520 2579 3479 355 C ATOM 298 O ALA A 40 -3.978 -5.030 -7.732 1.00 21.62 O ANISOU 298 O ALA A 40 2074 -167 719 2683 3456 402 O ATOM 299 CB ALA A 40 -6.036 -6.286 -9.760 1.00 23.78 C ANISOU 299 CB ALA A 40 2592 -106 173 2996 3447 69 C ATOM 300 N VAL A 41 -4.784 -6.565 -6.398 1.00 21.94 N ANISOU 300 N VAL A 41 1990 101 753 2718 3626 458 N ATOM 301 CA VAL A 41 -3.533 -6.673 -5.625 1.00 20.42 C ANISOU 301 CA VAL A 41 2382 135 582 2282 3093 410 C ATOM 302 C VAL A 41 -3.112 -8.125 -5.654 1.00 19.07 C ANISOU 302 C VAL A 41 2256 78 632 1997 2992 404 C ATOM 303 O VAL A 41 -3.875 -9.015 -5.286 1.00 22.63 O ANISOU 303 O VAL A 41 2313 180 755 2416 3866 739 O ATOM 304 CB VAL A 41 -3.712 -6.221 -4.175 1.00 23.08 C ANISOU 304 CB VAL A 41 2981 234 487 2453 3333 612 C ATOM 305 CG1 VAL A 41 -2.501 -6.458 -3.316 1.00 24.40 C ANISOU 305 CG1 VAL A 41 3680 143 228 3028 2561 527 C ATOM 306 CG2 VAL A 41 -4.110 -4.746 -4.169 1.00 23.49 C ANISOU 306 CG2 VAL A 41 3239 504 407 2508 3175 828 C ATOM 307 N GLU A 42 -1.916 -8.364 -6.120 1.00 16.82 N ANISOU 307 N GLU A 42 1908 80 385 1955 2527 105 N ATOM 308 CA GLU A 42 -1.350 -9.710 -6.150 1.00 17.11 C ANISOU 308 CA GLU A 42 2101 -50 223 2005 2392 1 C ATOM 309 C GLU A 42 -0.112 -9.705 -5.290 1.00 15.37 C ANISOU 309 C GLU A 42 1684 20 158 1901 2255 27 C ATOM 310 O GLU A 42 0.768 -8.864 -5.461 1.00 16.34 O ANISOU 310 O GLU A 42 1826 -103 287 2046 2335 -6 O ATOM 311 CB GLU A 42 -0.961 -10.078 -7.568 1.00 18.24 C ANISOU 311 CB GLU A 42 2281 -13 194 2329 2317 -102 C ATOM 312 CG GLU A 42 -0.365 -11.472 -7.685 1.00 21.43 C ANISOU 312 CG GLU A 42 2906 11 -31 2540 2697 -63 C ATOM 313 CD GLU A 42 0.147 -11.801 -9.108 1.00 25.27 C ANISOU 313 CD GLU A 42 3536 149 -131 2930 3134 74 C ATOM 314 OE1 GLU A 42 0.156 -10.906 -9.964 1.00 32.27 O ANISOU 314 OE1 GLU A 42 4795 -149 -90 4003 3461 245 O ATOM 315 OE2 GLU A 42 0.564 -12.951 -9.321 1.00 33.66 O ANISOU 315 OE2 GLU A 42 4548 279 -440 3747 4492 177 O ATOM 316 N ILE A 43 -0.025 -10.665 -4.377 1.00 15.81 N ANISOU 316 N ILE A 43 1800 -94 188 1762 2441 -49 N ATOM 317 CA ILE A 43 1.162 -10.834 -3.522 1.00 14.93 C ANISOU 317 CA ILE A 43 1683 -50 -44 1712 2275 -66 C ATOM 318 C ILE A 43 1.671 -12.253 -3.733 1.00 15.77 C ANISOU 318 C ILE A 43 1734 -96 -128 1745 2511 -140 C ATOM 319 O ILE A 43 0.914 -13.210 -3.641 1.00 17.17 O ANISOU 319 O ILE A 43 1795 -67 2 1895 2832 -243 O ATOM 320 CB ILE A 43 0.839 -10.605 -2.025 1.00 15.46 C ANISOU 320 CB ILE A 43 1714 -45 71 1802 2355 5 C ATOM 321 CG1 ILE A 43 0.331 -9.186 -1.804 1.00 15.58 C ANISOU 321 CG1 ILE A 43 1939 31 8 1745 2235 203 C ATOM 322 CG2 ILE A 43 2.071 -10.878 -1.142 1.00 15.82 C ANISOU 322 CG2 ILE A 43 1902 -46 113 1701 2406 31 C ATOM 323 CD1 ILE A 43 -0.054 -8.855 -0.346 1.00 16.98 C ANISOU 323 CD1 ILE A 43 2146 -77 81 1999 2306 288 C ATOM 324 N LYS A 44 2.969 -12.355 -3.943 1.00 16.36 N ANISOU 324 N LYS A 44 1769 9 -189 1688 2757 -97 N ATOM 325 CA LYS A 44 3.655 -13.630 -3.879 1.00 17.64 C ANISOU 325 CA LYS A 44 2122 -12 -114 1886 2692 -234 C ATOM 326 C LYS A 44 4.737 -13.514 -2.808 1.00 17.54 C ANISOU 326 C LYS A 44 1904 108 -114 1902 2859 -276 C ATOM 327 O LYS A 44 5.595 -12.651 -2.895 1.00 19.02 O ANISOU 327 O LYS A 44 2027 -67 -36 2188 3009 -415 O ATOM 328 CB LYS A 44 4.293 -13.949 -5.242 0.50 16.36 C ANISOU 328 CB LYS A 44 1821 227 -301 1659 2733 -64 C ATOM 329 CG LYS A 44 3.351 -14.104 -6.430 0.50 20.35 C ANISOU 329 CG LYS A 44 2495 69 31 2317 2918 -118 C ATOM 330 CD LYS A 44 4.174 -14.265 -7.749 0.50 21.37 C ANISOU 330 CD LYS A 44 2840 63 -223 2379 2899 -87 C ATOM 331 CE LYS A 44 3.345 -14.656 -8.977 0.50 25.12 C ANISOU 331 CE LYS A 44 3225 21 -111 3186 3133 -66 C ATOM 332 NZ LYS A 44 4.180 -14.914 -10.201 0.50 27.26 N ANISOU 332 NZ LYS A 44 3614 57 -274 3358 3382 9 N ATOM 333 N GLN A 45 4.598 -14.292 -1.754 1.00 18.74 N ANISOU 333 N GLN A 45 2159 -68 -90 1968 2993 -458 N ATOM 334 CA GLN A 45 5.531 -14.311 -0.631 1.00 18.32 C ANISOU 334 CA GLN A 45 2213 -18 -22 1824 2922 -416 C ATOM 335 C GLN A 45 6.268 -15.628 -0.580 1.00 18.85 C ANISOU 335 C GLN A 45 2261 -16 -93 1809 3092 -369 C ATOM 336 O GLN A 45 5.629 -16.695 -0.521 1.00 20.54 O ANISOU 336 O GLN A 45 2318 -88 10 1867 3615 -434 O ATOM 337 CB GLN A 45 4.830 -14.111 0.698 1.00 18.98 C ANISOU 337 CB GLN A 45 2303 51 -101 1934 2972 -425 C ATOM 338 CG GLN A 45 5.789 -14.088 1.881 1.00 18.96 C ANISOU 338 CG GLN A 45 2225 126 6 2050 2928 -384 C ATOM 339 CD GLN A 45 5.091 -14.021 3.209 1.00 18.82 C ANISOU 339 CD GLN A 45 2034 -26 -101 1994 3120 -220 C ATOM 340 OE1 GLN A 45 3.856 -13.867 3.277 1.00 23.85 O ANISOU 340 OE1 GLN A 45 1892 75 -53 2624 4545 34 O ATOM 341 NE2 GLN A 45 5.843 -14.196 4.268 1.00 20.18 N ANISOU 341 NE2 GLN A 45 2261 92 76 2220 3185 -48 N ATOM 342 N GLU A 46 7.596 -15.574 -0.515 1.00 18.26 N ANISOU 342 N GLU A 46 2182 43 -16 1744 3010 -247 N ATOM 343 CA GLU A 46 8.428 -16.750 -0.266 1.00 19.07 C ANISOU 343 CA GLU A 46 2461 151 44 1897 2886 -164 C ATOM 344 C GLU A 46 9.347 -16.431 0.893 1.00 18.37 C ANISOU 344 C GLU A 46 2195 134 103 1901 2881 -146 C ATOM 345 O GLU A 46 10.403 -15.765 0.731 1.00 18.89 O ANISOU 345 O GLU A 46 2202 200 56 2001 2974 -134 O ATOM 346 CB GLU A 46 9.235 -17.063 -1.518 1.00 19.87 C ANISOU 346 CB GLU A 46 2523 225 30 2034 2993 -183 C ATOM 347 CG GLU A 46 8.392 -17.492 -2.675 1.00 22.79 C ANISOU 347 CG GLU A 46 3202 63 -100 2337 3120 -103 C ATOM 348 CD GLU A 46 9.212 -18.059 -3.851 1.00 25.98 C ANISOU 348 CD GLU A 46 3525 147 -262 2934 3410 -92 C ATOM 349 OE1 GLU A 46 10.398 -18.429 -3.679 1.00 31.96 O ANISOU 349 OE1 GLU A 46 4096 235 -367 4087 3960 345 O ATOM 350 OE2 GLU A 46 8.617 -18.189 -4.938 1.00 34.29 O ANISOU 350 OE2 GLU A 46 4844 320 -161 4198 3984 -128 O ATOM 351 N GLY A 47 8.926 -16.805 2.096 1.00 19.29 N ANISOU 351 N GLY A 47 2354 -134 34 1963 3013 -191 N ATOM 352 CA GLY A 47 9.639 -16.389 3.295 1.00 18.91 C ANISOU 352 CA GLY A 47 2360 -41 231 2049 2775 -161 C ATOM 353 C GLY A 47 9.627 -14.887 3.469 1.00 18.11 C ANISOU 353 C GLY A 47 2168 4 165 2052 2661 -128 C ATOM 354 O GLY A 47 8.569 -14.249 3.512 1.00 18.93 O ANISOU 354 O GLY A 47 1987 3 66 2305 2897 -13 O ATOM 355 N ASP A 48 10.810 -14.285 3.542 1.00 17.38 N ANISOU 355 N ASP A 48 1940 53 135 1989 2672 -104 N ATOM 356 CA ASP A 48 10.938 -12.839 3.652 1.00 16.34 C ANISOU 356 CA ASP A 48 1883 84 105 1912 2412 -70 C ATOM 357 C ASP A 48 10.977 -12.119 2.311 1.00 15.90 C ANISOU 357 C ASP A 48 1683 18 85 2004 2354 -119 C ATOM 358 O ASP A 48 11.114 -10.893 2.321 1.00 16.26 O ANISOU 358 O ASP A 48 1765 -171 145 2011 2401 -91 O ATOM 359 CB ASP A 48 12.204 -12.494 4.453 1.00 17.19 C ANISOU 359 CB ASP A 48 2018 -7 30 2018 2495 -91 C ATOM 360 CG ASP A 48 12.013 -12.553 5.961 1.00 19.98 C ANISOU 360 CG ASP A 48 2446 27 211 2417 2725 -223 C ATOM 361 OD1 ASP A 48 10.919 -12.764 6.477 1.00 21.83 O ANISOU 361 OD1 ASP A 48 2806 162 323 2681 2808 66 O ATOM 362 OD2 ASP A 48 13.037 -12.371 6.646 1.00 25.45 O ANISOU 362 OD2 ASP A 48 3100 -242 393 3637 2933 -593 O ATOM 363 N THR A 49 10.886 -12.836 1.206 1.00 16.51 N ANISOU 363 N THR A 49 1811 87 67 1979 2481 -123 N ATOM 364 CA THR A 49 10.910 -12.217 -0.111 1.00 16.35 C ANISOU 364 CA THR A 49 1748 4 -31 2010 2452 -19 C ATOM 365 C THR A 49 9.492 -12.049 -0.638 1.00 16.46 C ANISOU 365 C THR A 49 1817 -15 -43 1983 2451 -108 C ATOM 366 O THR A 49 8.688 -12.992 -0.591 1.00 17.41 O ANISOU 366 O THR A 49 1825 -6 26 1951 2839 -84 O ATOM 367 CB THR A 49 11.761 -13.041 -1.077 1.00 17.98 C ANISOU 367 CB THR A 49 1963 154 -60 2249 2617 18 C ATOM 368 OG1 THR A 49 13.086 -13.118 -0.523 1.00 20.48 O ANISOU 368 OG1 THR A 49 1823 257 -137 2769 3188 -55 O ATOM 369 CG2 THR A 49 11.836 -12.396 -2.440 1.00 18.95 C ANISOU 369 CG2 THR A 49 2109 177 -197 2566 2525 70 C ATOM 370 N PHE A 50 9.201 -10.844 -1.150 1.00 15.29 N ANISOU 370 N PHE A 50 1699 -75 53 1852 2258 -5 N ATOM 371 CA PHE A 50 7.889 -10.490 -1.617 1.00 15.35 C ANISOU 371 CA PHE A 50 1767 8 -47 1934 2130 -81 C ATOM 372 C PHE A 50 7.930 -9.909 -3.038 1.00 15.79 C ANISOU 372 C PHE A 50 1866 65 -49 1994 2137 19 C ATOM 373 O PHE A 50 8.828 -9.143 -3.386 1.00 17.09 O ANISOU 373 O PHE A 50 1880 -39 -99 2317 2295 -74 O ATOM 374 CB PHE A 50 7.288 -9.395 -0.687 1.00 15.11 C ANISOU 374 CB PHE A 50 1799 45 -43 1760 2180 -95 C ATOM 375 CG PHE A 50 6.873 -9.903 0.660 1.00 15.09 C ANISOU 375 CG PHE A 50 1810 -69 -109 1690 2230 -112 C ATOM 376 CD1 PHE A 50 7.797 -10.081 1.660 1.00 15.31 C ANISOU 376 CD1 PHE A 50 1859 -122 -56 1836 2120 6 C ATOM 377 CD2 PHE A 50 5.527 -10.219 0.924 1.00 15.77 C ANISOU 377 CD2 PHE A 50 1851 -80 -176 2147 1993 20 C ATOM 378 CE1 PHE A 50 7.414 -10.549 2.884 1.00 15.79 C ANISOU 378 CE1 PHE A 50 1882 -63 0 1833 2282 -9 C ATOM 379 CE2 PHE A 50 5.176 -10.643 2.190 1.00 17.15 C ANISOU 379 CE2 PHE A 50 2019 -224 -136 2027 2468 135 C ATOM 380 CZ PHE A 50 6.115 -10.805 3.142 1.00 17.24 C ANISOU 380 CZ PHE A 50 2139 -76 -74 2160 2249 165 C ATOM 381 N TYR A 51 6.884 -10.240 -3.788 1.00 15.58 N ANISOU 381 N TYR A 51 1850 39 -212 1957 2113 -33 N ATOM 382 CA TYR A 51 6.503 -9.544 -5.027 1.00 15.55 C ANISOU 382 CA TYR A 51 1840 93 -217 2090 1977 -46 C ATOM 383 C TYR A 51 5.080 -9.042 -4.790 1.00 15.38 C ANISOU 383 C TYR A 51 1795 6 -50 2115 1932 -22 C ATOM 384 O TYR A 51 4.217 -9.820 -4.350 1.00 15.81 O ANISOU 384 O TYR A 51 1763 43 -58 2121 2122 17 O ATOM 385 CB TYR A 51 6.533 -10.503 -6.222 1.00 17.63 C ANISOU 385 CB TYR A 51 2161 169 -459 2359 2177 19 C ATOM 386 CG TYR A 51 5.850 -9.961 -7.467 1.00 18.43 C ANISOU 386 CG TYR A 51 2217 245 -439 2568 2218 -26 C ATOM 387 CD1 TYR A 51 6.450 -9.013 -8.262 1.00 20.90 C ANISOU 387 CD1 TYR A 51 2516 146 -438 3080 2345 -18 C ATOM 388 CD2 TYR A 51 4.563 -10.338 -7.794 1.00 19.67 C ANISOU 388 CD2 TYR A 51 2406 139 -437 2642 2427 -172 C ATOM 389 CE1 TYR A 51 5.837 -8.535 -9.439 1.00 21.67 C ANISOU 389 CE1 TYR A 51 2679 191 -259 3169 2383 150 C ATOM 390 CE2 TYR A 51 3.939 -9.870 -8.955 1.00 21.31 C ANISOU 390 CE2 TYR A 51 2642 41 -466 2966 2488 -334 C ATOM 391 CZ TYR A 51 4.584 -8.963 -9.774 1.00 20.88 C ANISOU 391 CZ TYR A 51 2646 412 -399 3164 2121 79 C ATOM 392 OH TYR A 51 3.956 -8.517 -10.912 1.00 23.05 O ANISOU 392 OH TYR A 51 3146 444 -361 3425 2184 73 O ATOM 393 N ILE A 52 4.852 -7.749 -5.016 1.00 14.66 N ANISOU 393 N ILE A 52 1651 -69 27 2071 1846 98 N ATOM 394 CA ILE A 52 3.523 -7.197 -4.862 1.00 14.35 C ANISOU 394 CA ILE A 52 1674 37 63 1930 1847 68 C ATOM 395 C ILE A 52 3.226 -6.398 -6.113 1.00 14.92 C ANISOU 395 C ILE A 52 1712 -41 95 2110 1844 111 C ATOM 396 O ILE A 52 3.988 -5.500 -6.494 1.00 16.48 O ANISOU 396 O ILE A 52 1923 -146 377 2317 2021 111 O ATOM 397 CB ILE A 52 3.387 -6.295 -3.621 1.00 15.22 C ANISOU 397 CB ILE A 52 1751 -70 34 1981 2049 119 C ATOM 398 CG1 ILE A 52 3.821 -7.052 -2.365 1.00 15.09 C ANISOU 398 CG1 ILE A 52 1835 -14 -106 1974 1921 176 C ATOM 399 CG2 ILE A 52 1.974 -5.735 -3.554 1.00 15.55 C ANISOU 399 CG2 ILE A 52 2019 -8 24 1842 2045 169 C ATOM 400 CD1 ILE A 52 3.620 -6.336 -1.047 1.00 16.88 C ANISOU 400 CD1 ILE A 52 1939 63 -37 2369 2103 118 C ATOM 401 N LYS A 53 2.110 -6.725 -6.741 1.00 15.10 N ANISOU 401 N LYS A 53 1740 -35 156 2127 1868 43 N ATOM 402 CA LYS A 53 1.603 -5.989 -7.900 1.00 15.63 C ANISOU 402 CA LYS A 53 1911 26 172 2152 1872 88 C ATOM 403 C LYS A 53 0.268 -5.363 -7.537 1.00 15.61 C ANISOU 403 C LYS A 53 1789 23 257 2251 1889 148 C ATOM 404 O LYS A 53 -0.628 -6.041 -7.089 1.00 18.02 O ANISOU 404 O LYS A 53 1863 59 527 2319 2664 224 O ATOM 405 CB LYS A 53 1.449 -6.884 -9.102 1.00 17.63 C ANISOU 405 CB LYS A 53 2152 0 163 2383 2163 113 C ATOM 406 CG LYS A 53 0.906 -6.205 -10.356 1.00 19.03 C ANISOU 406 CG LYS A 53 2433 -42 291 2495 2301 -52 C ATOM 407 CD LYS A 53 0.933 -7.178 -11.594 1.00 23.21 C ANISOU 407 CD LYS A 53 3096 29 24 3278 2443 -33 C ATOM 408 CE LYS A 53 0.159 -6.808 -12.797 1.00 28.68 C ANISOU 408 CE LYS A 53 3890 65 18 3713 3293 -209 C ATOM 409 NZ LYS A 53 0.094 -8.019 -13.668 1.00 31.52 N ANISOU 409 NZ LYS A 53 4420 -40 -263 3954 3603 -228 N ATOM 410 N VAL A 54 0.135 -4.085 -7.792 1.00 15.49 N ANISOU 410 N VAL A 54 1792 43 387 2220 1870 205 N ATOM 411 CA VAL A 54 -1.095 -3.357 -7.567 1.00 15.44 C ANISOU 411 CA VAL A 54 1903 48 248 2166 1795 161 C ATOM 412 C VAL A 54 -1.512 -2.750 -8.888 1.00 15.87 C ANISOU 412 C VAL A 54 1905 84 254 2283 1841 190 C ATOM 413 O VAL A 54 -0.729 -2.022 -9.501 1.00 16.98 O ANISOU 413 O VAL A 54 1999 -104 411 2572 1878 219 O ATOM 414 CB VAL A 54 -0.933 -2.248 -6.520 1.00 17.64 C ANISOU 414 CB VAL A 54 2378 140 237 2316 2009 215 C ATOM 415 CG1 VAL A 54 -2.248 -1.503 -6.327 1.00 19.50 C ANISOU 415 CG1 VAL A 54 2659 269 -7 2453 2297 210 C ATOM 416 CG2 VAL A 54 -0.429 -2.818 -5.179 1.00 19.74 C ANISOU 416 CG2 VAL A 54 2853 388 153 2756 1892 144 C ATOM 417 N SER A 55 -2.730 -3.036 -9.311 1.00 16.20 N ANISOU 417 N SER A 55 1904 84 221 2280 1969 204 N ATOM 418 CA SER A 55 -3.226 -2.444 -10.563 1.00 17.21 C ANISOU 418 CA SER A 55 2044 75 90 2460 2034 176 C ATOM 419 C SER A 55 -4.554 -1.774 -10.386 1.00 16.84 C ANISOU 419 C SER A 55 1900 -28 147 2475 2021 240 C ATOM 420 O SER A 55 -5.457 -2.302 -9.749 1.00 19.62 O ANISOU 420 O SER A 55 2121 -30 477 2650 2682 372 O ATOM 421 CB SER A 55 -3.319 -3.463 -11.665 1.00 20.89 C ANISOU 421 CB SER A 55 2643 274 -51 2786 2506 128 C ATOM 422 OG SER A 55 -2.082 -4.053 -11.973 1.00 27.08 O ANISOU 422 OG SER A 55 3167 353 -322 3534 3586 151 O ATOM 423 N THR A 56 -4.632 -0.565 -10.905 1.00 16.57 N ANISOU 423 N THR A 56 1984 29 253 2577 1733 302 N ATOM 424 CA THR A 56 -5.849 0.221 -10.953 1.00 16.92 C ANISOU 424 CA THR A 56 2009 9 265 2637 1782 240 C ATOM 425 C THR A 56 -6.315 0.237 -12.385 1.00 17.59 C ANISOU 425 C THR A 56 2018 -43 194 2634 2032 155 C ATOM 426 O THR A 56 -5.772 -0.484 -13.235 1.00 18.81 O ANISOU 426 O THR A 56 2359 68 31 2909 1876 23 O ATOM 427 CB THR A 56 -5.595 1.658 -10.450 1.00 19.17 C ANISOU 427 CB THR A 56 2405 180 241 2831 2045 227 C ATOM 428 OG1 THR A 56 -4.821 2.308 -11.458 1.00 18.72 O ANISOU 428 OG1 THR A 56 2338 100 75 2610 2161 456 O ATOM 429 CG2 THR A 56 -4.924 1.681 -9.075 1.00 21.70 C ANISOU 429 CG2 THR A 56 3027 248 20 3061 2156 302 C ATOM 430 N THR A 57 -7.335 1.025 -12.688 1.00 17.83 N ANISOU 430 N THR A 57 2049 -19 265 2673 2051 26 N ATOM 431 CA THR A 57 -7.816 1.118 -14.045 1.00 18.61 C ANISOU 431 CA THR A 57 2198 -76 117 2734 2137 44 C ATOM 432 C THR A 57 -6.742 1.619 -15.018 1.00 17.94 C ANISOU 432 C THR A 57 2327 -161 223 2608 1880 -2 C ATOM 433 O THR A 57 -6.786 1.264 -16.203 1.00 21.04 O ANISOU 433 O THR A 57 2731 -502 291 3187 2076 -83 O ATOM 434 CB THR A 57 -9.078 1.994 -14.141 1.00 18.52 C ANISOU 434 CB THR A 57 2154 1 152 2615 2265 -21 C ATOM 435 OG1 THR A 57 -8.764 3.265 -13.583 1.00 22.61 O ANISOU 435 OG1 THR A 57 2738 72 -286 2991 2862 175 O ATOM 436 CG2 THR A 57 -10.209 1.425 -13.396 1.00 20.76 C ANISOU 436 CG2 THR A 57 2426 57 214 3161 2302 -14 C ATOM 437 N VAL A 58 -5.827 2.449 -14.553 1.00 17.35 N ANISOU 437 N VAL A 58 2166 36 244 2551 1874 188 N ATOM 438 CA VAL A 58 -4.904 3.115 -15.445 1.00 16.87 C ANISOU 438 CA VAL A 58 2202 31 161 2476 1730 217 C ATOM 439 C VAL A 58 -3.439 2.896 -15.113 1.00 16.16 C ANISOU 439 C VAL A 58 2057 40 199 2320 1761 212 C ATOM 440 O VAL A 58 -2.596 3.343 -15.854 1.00 16.65 O ANISOU 440 O VAL A 58 2241 46 257 2314 1770 336 O ATOM 441 CB VAL A 58 -5.161 4.627 -15.496 1.00 17.68 C ANISOU 441 CB VAL A 58 2278 143 184 2343 2095 60 C ATOM 442 CG1 VAL A 58 -6.545 4.950 -16.124 1.00 20.29 C ANISOU 442 CG1 VAL A 58 2448 39 272 2793 2467 149 C ATOM 443 CG2 VAL A 58 -4.989 5.314 -14.123 1.00 19.65 C ANISOU 443 CG2 VAL A 58 2754 134 133 2280 2432 258 C ATOM 444 N ARG A 59 -3.134 2.210 -14.004 1.00 15.85 N ANISOU 444 N ARG A 59 2022 14 190 2438 1562 279 N ATOM 445 CA ARG A 59 -1.762 2.110 -13.546 1.00 16.26 C ANISOU 445 CA ARG A 59 2073 74 166 2466 1638 242 C ATOM 446 C ARG A 59 -1.486 0.729 -12.982 1.00 16.28 C ANISOU 446 C ARG A 59 2054 47 295 2530 1601 295 C ATOM 447 O ARG A 59 -2.302 0.155 -12.330 1.00 18.70 O ANISOU 447 O ARG A 59 2145 88 588 2754 2206 380 O ATOM 448 CB ARG A 59 -1.474 3.213 -12.523 1.00 17.94 C ANISOU 448 CB ARG A 59 2391 47 0 2657 1766 390 C ATOM 449 CG ARG A 59 -0.040 3.238 -11.963 1.00 19.06 C ANISOU 449 CG ARG A 59 2575 -135 81 2694 1970 138 C ATOM 450 CD ARG A 59 0.252 4.464 -11.122 1.00 20.21 C ANISOU 450 CD ARG A 59 2584 33 -169 2986 2110 146 C ATOM 451 NE ARG A 59 0.248 5.670 -11.940 0.50 16.29 N ANISOU 451 NE ARG A 59 2364 -188 -517 2299 1524 211 N ATOM 452 CZ ARG A 59 1.262 6.041 -12.700 1.00 20.79 C ANISOU 452 CZ ARG A 59 2990 -66 -216 2635 2275 150 C ATOM 453 NH1 ARG A 59 2.367 5.319 -12.710 1.00 21.68 N ANISOU 453 NH1 ARG A 59 2726 -267 -62 3256 2255 357 N ATOM 454 NH2 ARG A 59 1.175 7.128 -13.444 1.00 22.59 N ANISOU 454 NH2 ARG A 59 3216 49 -180 2992 2375 384 N ATOM 455 N THR A 60 -0.268 0.271 -13.181 1.00 16.23 N ANISOU 455 N THR A 60 1980 17 341 2496 1689 136 N ATOM 456 CA THR A 60 0.247 -0.906 -12.528 1.00 16.93 C ANISOU 456 CA THR A 60 1956 -10 335 2592 1882 78 C ATOM 457 C THR A 60 1.528 -0.518 -11.808 1.00 17.58 C ANISOU 457 C THR A 60 1915 -190 431 2782 1981 157 C ATOM 458 O THR A 60 2.339 0.272 -12.343 1.00 19.99 O ANISOU 458 O THR A 60 2073 -310 828 3242 2280 1 O ATOM 459 CB THR A 60 0.473 -1.984 -13.538 1.00 20.58 C ANISOU 459 CB THR A 60 2678 64 294 2764 2376 -36 C ATOM 460 OG1 THR A 60 -0.790 -2.386 -14.048 1.00 24.66 O ANISOU 460 OG1 THR A 60 3079 194 -117 3288 3000 -8 O ATOM 461 CG2 THR A 60 1.080 -3.194 -12.948 1.00 24.01 C ANISOU 461 CG2 THR A 60 3489 299 189 2933 2698 -129 C ATOM 462 N THR A 61 1.692 -1.040 -10.604 1.00 17.90 N ANISOU 462 N THR A 61 1967 -266 435 2801 2031 -85 N ATOM 463 CA THR A 61 2.902 -0.816 -9.806 1.00 18.22 C ANISOU 463 CA THR A 61 2129 -131 372 2820 1970 102 C ATOM 464 C THR A 61 3.358 -2.195 -9.391 1.00 17.68 C ANISOU 464 C THR A 61 1937 -171 393 2769 2012 9 C ATOM 465 O THR A 61 2.578 -3.036 -8.955 1.00 19.04 O ANISOU 465 O THR A 61 1916 -137 700 2863 2455 10 O ATOM 466 CB THR A 61 2.573 0.077 -8.633 1.00 20.58 C ANISOU 466 CB THR A 61 2373 -283 77 2911 2533 -60 C ATOM 467 OG1 THR A 61 1.843 -0.610 -7.625 1.00 30.21 O ANISOU 467 OG1 THR A 61 3643 -339 82 4002 3830 122 O ATOM 468 CG2 THR A 61 1.939 1.341 -9.141 1.00 19.48 C ANISOU 468 CG2 THR A 61 2535 -148 99 2575 2290 -33 C ATOM 469 N GLU A 62 4.641 -2.442 -9.521 1.00 17.95 N ANISOU 469 N GLU A 62 1957 -224 502 2868 1995 49 N ATOM 470 CA GLU A 62 5.231 -3.676 -9.097 1.00 18.90 C ANISOU 470 CA GLU A 62 2114 -147 260 2849 2216 192 C ATOM 471 C GLU A 62 6.387 -3.384 -8.174 1.00 18.44 C ANISOU 471 C GLU A 62 1970 -174 359 2833 2200 61 C ATOM 472 O GLU A 62 7.281 -2.603 -8.526 1.00 20.99 O ANISOU 472 O GLU A 62 2036 -400 640 3342 2595 -106 O ATOM 473 CB GLU A 62 5.732 -4.472 -10.282 1.00 21.17 C ANISOU 473 CB GLU A 62 2565 -89 110 3030 2448 41 C ATOM 474 CG GLU A 62 4.619 -4.896 -11.173 1.00 21.60 C ANISOU 474 CG GLU A 62 2652 -42 -97 3163 2391 161 C ATOM 475 CD GLU A 62 5.178 -5.503 -12.446 1.00 25.40 C ANISOU 475 CD GLU A 62 3440 -3 -31 3484 2725 203 C ATOM 476 OE1 GLU A 62 5.488 -4.743 -13.391 1.00 30.48 O ANISOU 476 OE1 GLU A 62 4577 19 163 4120 2885 486 O ATOM 477 OE2 GLU A 62 5.306 -6.743 -12.494 1.00 27.86 O ANISOU 477 OE2 GLU A 62 4449 422 -269 3258 2879 251 O ATOM 478 N ILE A 63 6.450 -4.078 -7.051 1.00 17.21 N ANISOU 478 N ILE A 63 1933 -61 247 2617 1989 11 N ATOM 479 CA ILE A 63 7.605 -3.989 -6.175 1.00 18.00 C ANISOU 479 CA ILE A 63 2097 -137 175 2564 2179 89 C ATOM 480 C ILE A 63 8.111 -5.385 -5.833 1.00 17.34 C ANISOU 480 C ILE A 63 1999 -75 147 2634 1955 82 C ATOM 481 O ILE A 63 7.358 -6.359 -5.720 1.00 17.07 O ANISOU 481 O ILE A 63 1947 -103 198 2517 2022 -2 O ATOM 482 CB ILE A 63 7.368 -3.164 -4.890 1.00 19.18 C ANISOU 482 CB ILE A 63 2306 -29 103 2645 2337 104 C ATOM 483 CG1 ILE A 63 6.321 -3.782 -4.006 1.00 18.17 C ANISOU 483 CG1 ILE A 63 2070 -16 -27 2442 2390 220 C ATOM 484 CG2 ILE A 63 7.021 -1.757 -5.220 1.00 20.63 C ANISOU 484 CG2 ILE A 63 2575 -120 242 2628 2636 -27 C ATOM 485 CD1 ILE A 63 6.156 -3.121 -2.653 1.00 18.30 C ANISOU 485 CD1 ILE A 63 2269 15 134 2433 2248 35 C ATOM 486 N ASN A 64 9.424 -5.459 -5.649 1.00 18.14 N ANISOU 486 N ASN A 64 1887 -154 256 2780 2224 19 N ATOM 487 CA ASN A 64 10.128 -6.664 -5.261 1.00 18.06 C ANISOU 487 CA ASN A 64 1984 -115 163 2700 2175 137 C ATOM 488 C ASN A 64 11.018 -6.316 -4.113 1.00 17.73 C ANISOU 488 C ASN A 64 1889 -114 192 2665 2182 5 C ATOM 489 O ASN A 64 11.826 -5.384 -4.235 1.00 19.35 O ANISOU 489 O ASN A 64 2025 -435 468 2938 2388 -89 O ATOM 490 CB ASN A 64 11.006 -7.201 -6.388 1.00 19.57 C ANISOU 490 CB ASN A 64 2156 48 36 2996 2283 -14 C ATOM 491 CG ASN A 64 10.201 -7.765 -7.522 1.00 21.86 C ANISOU 491 CG ASN A 64 2502 60 -29 3346 2455 160 C ATOM 492 OD1 ASN A 64 9.785 -8.920 -7.468 1.00 24.03 O ANISOU 492 OD1 ASN A 64 2649 23 -351 3805 2673 66 O ATOM 493 ND2 ASN A 64 9.933 -6.940 -8.528 1.00 24.65 N ANISOU 493 ND2 ASN A 64 3061 -113 62 3767 2538 59 N ATOM 494 N PHE A 65 10.875 -7.001 -2.998 1.00 16.26 N ANISOU 494 N PHE A 65 1802 -116 116 2383 1991 -2 N ATOM 495 CA PHE A 65 11.701 -6.699 -1.850 1.00 15.82 C ANISOU 495 CA PHE A 65 1669 -146 87 2241 2097 1 C ATOM 496 C PHE A 65 11.922 -7.933 -0.994 1.00 15.53 C ANISOU 496 C PHE A 65 1658 -108 12 2042 2200 104 C ATOM 497 O PHE A 65 11.162 -8.895 -1.068 1.00 16.47 O ANISOU 497 O PHE A 65 1789 -102 -3 2186 2281 -49 O ATOM 498 CB PHE A 65 11.119 -5.552 -1.018 1.00 16.19 C ANISOU 498 CB PHE A 65 1809 -130 -14 2248 2095 -36 C ATOM 499 CG PHE A 65 9.813 -5.839 -0.326 1.00 15.47 C ANISOU 499 CG PHE A 65 1753 25 -51 1996 2126 36 C ATOM 500 CD1 PHE A 65 9.780 -6.429 0.920 1.00 15.63 C ANISOU 500 CD1 PHE A 65 1915 -28 -36 1992 2030 66 C ATOM 501 CD2 PHE A 65 8.614 -5.503 -0.926 1.00 16.28 C ANISOU 501 CD2 PHE A 65 1809 8 180 2175 2202 -62 C ATOM 502 CE1 PHE A 65 8.596 -6.672 1.558 1.00 15.89 C ANISOU 502 CE1 PHE A 65 2215 -10 -78 1849 1973 115 C ATOM 503 CE2 PHE A 65 7.413 -5.756 -0.285 1.00 16.92 C ANISOU 503 CE2 PHE A 65 1886 54 184 1993 2546 167 C ATOM 504 CZ PHE A 65 7.408 -6.327 0.947 1.00 15.88 C ANISOU 504 CZ PHE A 65 1923 -137 -58 1768 2340 169 C ATOM 505 N LYS A 66 12.981 -7.887 -0.212 1.00 14.88 N ANISOU 505 N LYS A 66 1577 -175 125 2058 2019 97 N ATOM 506 CA LYS A 66 13.178 -8.798 0.881 1.00 15.27 C ANISOU 506 CA LYS A 66 1634 -128 90 2012 2154 40 C ATOM 507 C LYS A 66 13.210 -8.005 2.157 1.00 14.35 C ANISOU 507 C LYS A 66 1493 -64 152 1997 1962 -10 C ATOM 508 O LYS A 66 13.818 -6.917 2.235 1.00 15.12 O ANISOU 508 O LYS A 66 1575 -201 191 2016 2152 20 O ATOM 509 CB ALYS A 66 14.459 -9.577 0.641 0.50 16.50 C ANISOU 509 CB ALYS A 66 1790 -119 66 2128 2351 52 C ATOM 510 CG ALYS A 66 14.685 -10.713 1.604 0.50 16.84 C ANISOU 510 CG ALYS A 66 1921 5 84 2108 2367 59 C ATOM 511 CD ALYS A 66 15.789 -11.667 1.136 0.50 18.40 C ANISOU 511 CD ALYS A 66 2198 18 -20 2262 2532 39 C ATOM 512 CE ALYS A 66 16.497 -12.328 2.309 0.50 20.91 C ANISOU 512 CE ALYS A 66 2693 283 9 2495 2755 145 C ATOM 513 NZ ALYS A 66 15.623 -13.210 3.149 0.50 24.05 N ANISOU 513 NZ ALYS A 66 2808 107 64 2837 3491 119 N ATOM 514 N VAL A 67 12.550 -8.495 3.190 1.00 15.05 N ANISOU 514 N VAL A 67 1646 -121 74 1939 2130 37 N ATOM 515 CA VAL A 67 12.556 -7.835 4.474 1.00 14.74 C ANISOU 515 CA VAL A 67 1633 -12 203 1876 2090 12 C ATOM 516 C VAL A 67 14.002 -7.579 4.892 1.00 15.32 C ANISOU 516 C VAL A 67 1787 70 40 2053 1980 20 C ATOM 517 O VAL A 67 14.852 -8.473 4.819 1.00 16.42 O ANISOU 517 O VAL A 67 1890 79 153 1870 2478 6 O ATOM 518 CB VAL A 67 11.786 -8.650 5.528 1.00 16.84 C ANISOU 518 CB VAL A 67 1969 -91 213 2181 2245 99 C ATOM 519 CG1 VAL A 67 11.849 -7.975 6.896 1.00 18.80 C ANISOU 519 CG1 VAL A 67 2486 -351 331 2565 2091 156 C ATOM 520 CG2 VAL A 67 10.313 -8.867 5.090 1.00 17.79 C ANISOU 520 CG2 VAL A 67 1982 -113 92 2280 2495 153 C ATOM 521 N GLY A 68 14.289 -6.368 5.321 1.00 13.95 N ANISOU 521 N GLY A 68 1627 25 89 1885 1787 -54 N ATOM 522 CA GLY A 68 15.631 -6.001 5.781 1.00 14.25 C ANISOU 522 CA GLY A 68 1584 62 81 1901 1930 -50 C ATOM 523 C GLY A 68 16.583 -5.511 4.706 1.00 14.71 C ANISOU 523 C GLY A 68 1627 87 42 2013 1947 -44 C ATOM 524 O GLY A 68 17.716 -5.150 5.023 1.00 15.88 O ANISOU 524 O GLY A 68 1597 -123 189 2310 2127 -149 O ATOM 525 N GLU A 69 16.142 -5.467 3.462 1.00 13.93 N ANISOU 525 N GLU A 69 1502 -42 156 1818 1972 -55 N ATOM 526 CA GLU A 69 16.987 -5.049 2.346 1.00 14.13 C ANISOU 526 CA GLU A 69 1525 -11 135 1881 1961 -34 C ATOM 527 C GLU A 69 16.351 -3.854 1.644 1.00 13.89 C ANISOU 527 C GLU A 69 1572 -20 227 1884 1822 72 C ATOM 528 O GLU A 69 15.184 -3.883 1.272 1.00 14.56 O ANISOU 528 O GLU A 69 1397 -44 219 2141 1993 -109 O ATOM 529 CB GLU A 69 17.205 -6.199 1.350 1.00 14.82 C ANISOU 529 CB GLU A 69 1497 23 17 2064 2069 98 C ATOM 530 CG GLU A 69 17.701 -7.470 2.024 1.00 15.83 C ANISOU 530 CG GLU A 69 1631 -39 212 1899 2484 91 C ATOM 531 CD GLU A 69 18.137 -8.583 1.072 1.00 17.44 C ANISOU 531 CD GLU A 69 1664 -131 88 2282 2677 65 C ATOM 532 OE1 GLU A 69 17.889 -8.465 -0.130 1.00 18.87 O ANISOU 532 OE1 GLU A 69 1975 -16 -340 2348 2844 16 O ATOM 533 OE2 GLU A 69 18.708 -9.580 1.583 1.00 20.86 O ANISOU 533 OE2 GLU A 69 1799 130 193 2182 3942 161 O ATOM 534 N GLU A 70 17.121 -2.806 1.426 1.00 13.42 N ANISOU 534 N GLU A 70 1445 2 155 1762 1891 96 N ATOM 535 CA GLU A 70 16.587 -1.625 0.749 1.00 14.05 C ANISOU 535 CA GLU A 70 1487 56 187 1936 1912 106 C ATOM 536 C GLU A 70 16.245 -1.882 -0.705 1.00 14.64 C ANISOU 536 C GLU A 70 1490 70 165 2064 2007 137 C ATOM 537 O GLU A 70 16.931 -2.630 -1.400 1.00 15.97 O ANISOU 537 O GLU A 70 1739 177 138 2328 2000 155 O ATOM 538 CB GLU A 70 17.618 -0.479 0.818 1.00 14.15 C ANISOU 538 CB GLU A 70 1503 175 168 1754 2118 -7 C ATOM 539 CG GLU A 70 17.710 0.113 2.184 1.00 16.04 C ANISOU 539 CG GLU A 70 1907 6 169 1770 2417 65 C ATOM 540 CD GLU A 70 18.927 0.979 2.443 1.00 17.80 C ANISOU 540 CD GLU A 70 2368 43 120 1973 2422 66 C ATOM 541 OE1 GLU A 70 19.066 1.459 3.564 1.00 24.73 O ANISOU 541 OE1 GLU A 70 4110 -719 179 2502 2784 -254 O ATOM 542 OE2 GLU A 70 19.740 1.230 1.590 1.00 18.41 O ANISOU 542 OE2 GLU A 70 2063 -24 -94 2193 2736 155 O ATOM 543 N PHE A 71 15.173 -1.259 -1.147 1.00 14.84 N ANISOU 543 N PHE A 71 1564 59 228 2220 1852 11 N ATOM 544 CA PHE A 71 14.691 -1.362 -2.491 1.00 16.37 C ANISOU 544 CA PHE A 71 1997 130 125 2268 1954 65 C ATOM 545 C PHE A 71 14.124 -0.044 -2.914 1.00 16.38 C ANISOU 545 C PHE A 71 1854 4 240 2320 2047 15 C ATOM 546 O PHE A 71 13.947 0.836 -2.110 1.00 17.41 O ANISOU 546 O PHE A 71 2376 249 358 2153 2084 -7 O ATOM 547 CB PHE A 71 13.624 -2.465 -2.637 1.00 16.20 C ANISOU 547 CB PHE A 71 1980 34 104 2279 1895 -17 C ATOM 548 CG PHE A 71 12.352 -2.244 -1.878 1.00 15.59 C ANISOU 548 CG PHE A 71 1759 35 90 2059 2103 -134 C ATOM 549 CD1 PHE A 71 12.297 -2.445 -0.518 1.00 14.65 C ANISOU 549 CD1 PHE A 71 1765 32 253 1940 1859 -81 C ATOM 550 CD2 PHE A 71 11.190 -1.854 -2.541 1.00 16.84 C ANISOU 550 CD2 PHE A 71 1892 -53 263 2475 2030 -242 C ATOM 551 CE1 PHE A 71 11.121 -2.264 0.177 1.00 16.50 C ANISOU 551 CE1 PHE A 71 1842 -89 141 2080 2345 4 C ATOM 552 CE2 PHE A 71 10.002 -1.664 -1.822 1.00 17.36 C ANISOU 552 CE2 PHE A 71 1896 -13 267 2240 2457 -220 C ATOM 553 CZ PHE A 71 9.958 -1.863 -0.489 1.00 16.41 C ANISOU 553 CZ PHE A 71 1682 -91 -11 2078 2473 11 C ATOM 554 N GLU A 72 13.831 0.097 -4.202 1.00 18.79 N ANISOU 554 N GLU A 72 2362 280 175 2675 2100 -71 N ATOM 555 CA GLU A 72 13.245 1.319 -4.726 1.00 21.03 C ANISOU 555 CA GLU A 72 2553 167 282 2927 2511 -72 C ATOM 556 C GLU A 72 11.791 1.116 -5.095 1.00 19.52 C ANISOU 556 C GLU A 72 2434 233 291 2711 2270 -211 C ATOM 557 O GLU A 72 11.417 0.097 -5.673 1.00 21.81 O ANISOU 557 O GLU A 72 2778 417 283 3204 2303 -390 O ATOM 558 CB GLU A 72 14.015 1.744 -5.965 1.00 21.92 C ANISOU 558 CB GLU A 72 2726 342 380 3056 2544 -134 C ATOM 559 CG GLU A 72 15.398 2.178 -5.574 1.00 27.38 C ANISOU 559 CG GLU A 72 3251 56 288 3612 3540 -24 C ATOM 560 CD GLU A 72 16.193 2.876 -6.653 1.00 29.60 C ANISOU 560 CD GLU A 72 3471 -69 301 4052 3723 120 C ATOM 561 OE1 GLU A 72 15.673 3.101 -7.772 1.00 35.06 O ANISOU 561 OE1 GLU A 72 4496 55 537 4828 3995 336 O ATOM 562 OE2 GLU A 72 17.385 3.155 -6.364 1.00 36.92 O ANISOU 562 OE2 GLU A 72 3894 -26 282 5124 5009 6 O ATOM 563 N GLU A 73 10.994 2.133 -4.762 1.00 20.25 N ANISOU 563 N GLU A 73 2449 198 354 3052 2191 -119 N ATOM 564 CA GLU A 73 9.597 2.164 -5.179 1.00 20.33 C ANISOU 564 CA GLU A 73 2354 107 273 2960 2409 -150 C ATOM 565 C GLU A 73 9.197 3.624 -5.326 1.00 21.58 C ANISOU 565 C GLU A 73 2423 148 380 3108 2667 -251 C ATOM 566 O GLU A 73 10.063 4.500 -5.568 1.00 22.51 O ANISOU 566 O GLU A 73 2411 311 769 3150 2989 -308 O ATOM 567 CB GLU A 73 8.693 1.384 -4.212 1.00 20.01 C ANISOU 567 CB GLU A 73 2404 60 318 2776 2422 -201 C ATOM 568 CG GLU A 73 8.710 1.851 -2.790 1.00 20.14 C ANISOU 568 CG GLU A 73 2382 -7 128 2906 2363 47 C ATOM 569 CD GLU A 73 7.652 1.236 -1.886 1.00 19.30 C ANISOU 569 CD GLU A 73 2108 100 95 2743 2481 1 C ATOM 570 OE1 GLU A 73 6.722 0.567 -2.372 1.00 24.44 O ANISOU 570 OE1 GLU A 73 2586 -428 -379 3458 3242 94 O ATOM 571 OE2 GLU A 73 7.719 1.505 -0.673 1.00 18.41 O ANISOU 571 OE2 GLU A 73 1962 215 335 2590 2441 154 O ATOM 572 N GLN A 74 7.908 3.900 -5.263 1.00 22.04 N ANISOU 572 N GLN A 74 2440 188 244 3055 2878 -206 N ATOM 573 CA GLN A 74 7.419 5.271 -5.242 1.00 21.97 C ANISOU 573 CA GLN A 74 2574 212 395 3013 2758 -180 C ATOM 574 C GLN A 74 6.519 5.438 -4.048 1.00 21.19 C ANISOU 574 C GLN A 74 2335 250 386 2825 2891 -118 C ATOM 575 O GLN A 74 5.901 4.486 -3.593 1.00 21.52 O ANISOU 575 O GLN A 74 2385 141 374 2634 3158 -28 O ATOM 576 CB GLN A 74 6.593 5.599 -6.495 1.00 23.23 C ANISOU 576 CB GLN A 74 2858 243 448 3290 2677 -227 C ATOM 577 CG GLN A 74 7.353 5.418 -7.789 1.00 25.93 C ANISOU 577 CG GLN A 74 3137 162 490 3765 2948 -172 C ATOM 578 CD GLN A 74 6.433 5.539 -8.991 1.00 29.22 C ANISOU 578 CD GLN A 74 3668 122 266 4006 3426 -314 C ATOM 579 OE1 GLN A 74 5.864 4.548 -9.441 1.00 34.28 O ANISOU 579 OE1 GLN A 74 4593 -63 78 4483 3945 -454 O ATOM 580 NE2 GLN A 74 6.239 6.766 -9.472 1.00 33.98 N ANISOU 580 NE2 GLN A 74 4619 157 267 4257 4035 -14 N ATOM 581 N THR A 75 6.421 6.668 -3.590 1.00 20.30 N ANISOU 581 N THR A 75 2325 251 542 2524 2863 -187 N ATOM 582 CA THR A 75 5.465 7.005 -2.586 1.00 20.52 C ANISOU 582 CA THR A 75 2197 213 478 2561 3037 -180 C ATOM 583 C THR A 75 4.069 6.958 -3.205 1.00 21.52 C ANISOU 583 C THR A 75 2369 225 380 2619 3188 -125 C ATOM 584 O THR A 75 3.902 6.835 -4.436 1.00 23.26 O ANISOU 584 O THR A 75 2360 267 467 3006 3471 -330 O ATOM 585 CB THR A 75 5.707 8.422 -2.105 1.00 21.25 C ANISOU 585 CB THR A 75 2339 191 490 2604 3132 -9 C ATOM 586 OG1 THR A 75 5.499 9.338 -3.206 1.00 23.73 O ANISOU 586 OG1 THR A 75 2655 145 1003 2650 3711 -280 O ATOM 587 CG2 THR A 75 7.141 8.602 -1.584 1.00 20.66 C ANISOU 587 CG2 THR A 75 2463 45 508 2314 3071 -118 C ATOM 588 N VAL A 76 3.084 7.070 -2.341 1.00 23.31 N ANISOU 588 N VAL A 76 2278 82 400 2950 3628 -172 N ATOM 589 CA VAL A 76 1.689 7.020 -2.758 1.00 24.83 C ANISOU 589 CA VAL A 76 2532 198 397 3150 3752 -263 C ATOM 590 C VAL A 76 1.372 8.084 -3.803 1.00 26.55 C ANISOU 590 C VAL A 76 2755 163 380 3392 3939 -326 C ATOM 591 O VAL A 76 0.514 7.851 -4.668 1.00 29.37 O ANISOU 591 O VAL A 76 3024 163 473 3809 4324 -604 O ATOM 592 CB VAL A 76 0.762 7.055 -1.509 1.00 26.32 C ANISOU 592 CB VAL A 76 2657 22 322 3374 3968 -187 C ATOM 593 CG1 VAL A 76 0.804 8.383 -0.812 1.00 27.47 C ANISOU 593 CG1 VAL A 76 2946 99 193 3466 4025 52 C ATOM 594 CG2 VAL A 76 -0.684 6.657 -1.854 1.00 27.06 C ANISOU 594 CG2 VAL A 76 2672 1 408 3497 4110 -162 C ATOM 595 N ASP A 77 2.035 9.233 -3.715 1.00 26.11 N ANISOU 595 N ASP A 77 2864 328 596 3188 3868 -317 N ATOM 596 CA ASP A 77 1.825 10.339 -4.666 1.00 26.57 C ANISOU 596 CA ASP A 77 3009 307 536 3335 3749 -317 C ATOM 597 C ASP A 77 2.817 10.304 -5.813 1.00 27.40 C ANISOU 597 C ASP A 77 3246 398 609 3393 3772 -310 C ATOM 598 O ASP A 77 2.914 11.260 -6.593 1.00 29.39 O ANISOU 598 O ASP A 77 3560 470 965 3673 3931 -324 O ATOM 599 CB ASP A 77 1.834 11.680 -3.932 1.00 26.97 C ANISOU 599 CB ASP A 77 3123 374 587 3267 3856 -249 C ATOM 600 CG ASP A 77 3.141 11.993 -3.254 1.00 29.24 C ANISOU 600 CG ASP A 77 3468 69 536 3324 4316 -226 C ATOM 601 OD1 ASP A 77 3.671 11.095 -2.571 1.00 28.55 O ANISOU 601 OD1 ASP A 77 3257 414 827 2891 4699 -152 O ATOM 602 OD2 ASP A 77 3.594 13.158 -3.324 1.00 32.48 O ANISOU 602 OD2 ASP A 77 4247 26 483 3400 4690 -67 O ATOM 603 N GLY A 78 3.571 9.211 -5.935 1.00 26.62 N ANISOU 603 N GLY A 78 2916 503 584 3494 3704 -397 N ATOM 604 CA GLY A 78 4.377 8.965 -7.104 1.00 26.37 C ANISOU 604 CA GLY A 78 3031 333 608 3503 3484 -353 C ATOM 605 C GLY A 78 5.836 9.387 -7.090 1.00 27.24 C ANISOU 605 C GLY A 78 3149 326 598 3690 3508 -215 C ATOM 606 O GLY A 78 6.506 9.261 -8.125 1.00 30.10 O ANISOU 606 O GLY A 78 3320 303 752 4282 3834 -123 O ATOM 607 N ARG A 79 6.346 9.842 -5.945 1.00 25.41 N ANISOU 607 N ARG A 79 2881 373 785 3346 3427 -248 N ATOM 608 CA ARG A 79 7.740 10.264 -5.872 1.00 24.79 C ANISOU 608 CA ARG A 79 2896 321 825 3186 3334 -153 C ATOM 609 C ARG A 79 8.673 9.062 -5.614 1.00 24.06 C ANISOU 609 C ARG A 79 2902 341 941 3036 3202 -141 C ATOM 610 O ARG A 79 8.453 8.274 -4.708 1.00 23.12 O ANISOU 610 O ARG A 79 2525 147 1101 2787 3470 -37 O ATOM 611 CB ARG A 79 7.907 11.258 -4.787 1.00 24.50 C ANISOU 611 CB ARG A 79 2921 416 866 2897 3487 -152 C ATOM 612 CG ARG A 79 7.054 12.544 -5.011 1.00 27.18 C ANISOU 612 CG ARG A 79 3403 289 732 3205 3719 -148 C ATOM 613 CD ARG A 79 7.109 13.453 -3.839 1.00 28.94 C ANISOU 613 CD ARG A 79 3646 276 518 3466 3882 -67 C ATOM 614 NE ARG A 79 8.407 14.110 -3.764 1.00 33.01 N ANISOU 614 NE ARG A 79 4294 4 263 3713 4532 -136 N ATOM 615 CZ ARG A 79 8.751 15.048 -2.884 1.00 33.64 C ANISOU 615 CZ ARG A 79 4511 91 152 3919 4352 -26 C ATOM 616 NH1 ARG A 79 7.941 15.422 -1.907 1.00 34.40 N ANISOU 616 NH1 ARG A 79 4719 219 278 3502 4849 177 N ATOM 617 NH2 ARG A 79 9.952 15.566 -2.954 1.00 34.98 N ANISOU 617 NH2 ARG A 79 4716 -92 68 3693 4879 126 N ATOM 618 N PRO A 80 9.736 8.908 -6.412 1.00 24.16 N ANISOU 618 N PRO A 80 2809 306 919 3131 3237 16 N ATOM 619 CA PRO A 80 10.640 7.772 -6.186 1.00 23.18 C ANISOU 619 CA PRO A 80 2650 181 693 3013 3142 28 C ATOM 620 C PRO A 80 11.282 7.812 -4.807 1.00 22.50 C ANISOU 620 C PRO A 80 2464 87 661 2941 3144 45 C ATOM 621 O PRO A 80 11.645 8.859 -4.291 1.00 22.75 O ANISOU 621 O PRO A 80 2587 246 850 2796 3261 -71 O ATOM 622 CB PRO A 80 11.686 7.972 -7.275 1.00 24.38 C ANISOU 622 CB PRO A 80 2826 253 634 3228 3206 69 C ATOM 623 CG PRO A 80 10.971 8.698 -8.342 1.00 25.44 C ANISOU 623 CG PRO A 80 3145 140 653 3290 3231 29 C ATOM 624 CD PRO A 80 10.135 9.668 -7.611 1.00 26.16 C ANISOU 624 CD PRO A 80 3182 205 736 3485 3271 73 C ATOM 625 N CYS A 81 11.391 6.642 -4.190 1.00 20.59 N ANISOU 625 N CYS A 81 2339 -15 679 2515 2967 4 N ATOM 626 CA CYS A 81 11.924 6.542 -2.848 1.00 20.32 C ANISOU 626 CA CYS A 81 2297 14 621 2503 2921 38 C ATOM 627 C CYS A 81 12.682 5.243 -2.673 1.00 18.45 C ANISOU 627 C CYS A 81 2029 88 497 2350 2631 88 C ATOM 628 O CYS A 81 12.523 4.292 -3.437 1.00 20.87 O ANISOU 628 O CYS A 81 2340 110 618 2812 2778 -165 O ATOM 629 CB CYS A 81 10.821 6.636 -1.797 1.00 19.76 C ANISOU 629 CB CYS A 81 2262 123 614 2374 2869 10 C ATOM 630 SG CYS A 81 9.544 5.375 -1.818 1.00 20.32 S ANISOU 630 SG CYS A 81 2058 6 757 2569 3093 10 S ATOM 631 N LYS A 82 13.579 5.285 -1.697 1.00 19.05 N ANISOU 631 N LYS A 82 2172 -66 466 2286 2777 -10 N ATOM 632 CA LYS A 82 14.238 4.077 -1.196 1.00 18.00 C ANISOU 632 CA LYS A 82 2075 20 432 2214 2550 80 C ATOM 633 C LYS A 82 13.488 3.602 0.038 1.00 18.02 C ANISOU 633 C LYS A 82 2058 75 287 2267 2522 28 C ATOM 634 O LYS A 82 13.255 4.369 0.964 1.00 20.50 O ANISOU 634 O LYS A 82 2903 -160 156 2005 2881 262 O ATOM 635 CB LYS A 82 15.721 4.397 -0.864 1.00 19.33 C ANISOU 635 CB LYS A 82 2003 89 451 2572 2770 60 C ATOM 636 CG LYS A 82 16.526 3.189 -0.394 1.00 20.47 C ANISOU 636 CG LYS A 82 2228 -21 388 2581 2968 -58 C ATOM 637 CD LYS A 82 18.013 3.472 -0.120 1.00 21.38 C ANISOU 637 CD LYS A 82 2397 53 368 2736 2989 -114 C ATOM 638 CE LYS A 82 18.206 4.169 1.167 1.00 21.98 C ANISOU 638 CE LYS A 82 2345 157 326 2769 3236 -306 C ATOM 639 NZ LYS A 82 19.681 4.208 1.485 1.00 22.63 N ANISOU 639 NZ LYS A 82 2387 102 446 2437 3773 -411 N ATOM 640 N SER A 83 13.119 2.341 0.039 1.00 15.84 N ANISOU 640 N SER A 83 1819 -32 133 2086 2111 41 N ATOM 641 CA SER A 83 12.251 1.786 1.090 1.00 15.41 C ANISOU 641 CA SER A 83 1714 80 147 1952 2186 97 C ATOM 642 C SER A 83 12.972 0.667 1.807 1.00 14.42 C ANISOU 642 C SER A 83 1604 33 125 1900 1974 39 C ATOM 643 O SER A 83 13.862 0.012 1.242 1.00 14.99 O ANISOU 643 O SER A 83 1584 117 129 2057 2051 54 O ATOM 644 CB SER A 83 10.979 1.299 0.446 1.00 15.99 C ANISOU 644 CB SER A 83 1649 108 228 2154 2270 44 C ATOM 645 OG SER A 83 10.177 2.431 0.068 1.00 17.64 O ANISOU 645 OG SER A 83 1888 305 389 2324 2488 28 O ATOM 646 N LEU A 84 12.494 0.392 3.005 1.00 14.41 N ANISOU 646 N LEU A 84 1526 130 51 1867 2079 19 N ATOM 647 CA LEU A 84 13.023 -0.695 3.840 1.00 14.77 C ANISOU 647 CA LEU A 84 1559 35 98 1924 2126 35 C ATOM 648 C LEU A 84 11.887 -1.234 4.684 1.00 14.62 C ANISOU 648 C LEU A 84 1521 81 101 1946 2088 1 C ATOM 649 O LEU A 84 11.283 -0.479 5.447 1.00 15.19 O ANISOU 649 O LEU A 84 1584 -9 -106 1881 2303 165 O ATOM 650 CB LEU A 84 14.139 -0.157 4.742 1.00 15.04 C ANISOU 650 CB LEU A 84 1620 22 -41 1935 2160 17 C ATOM 651 CG LEU A 84 14.758 -1.157 5.690 1.00 15.33 C ANISOU 651 CG LEU A 84 1631 -10 85 2156 2036 -13 C ATOM 652 CD1 LEU A 84 15.439 -2.260 4.962 1.00 16.23 C ANISOU 652 CD1 LEU A 84 1728 22 63 2258 2177 -168 C ATOM 653 CD2 LEU A 84 15.728 -0.453 6.618 1.00 18.71 C ANISOU 653 CD2 LEU A 84 2042 130 -30 2638 2427 -16 C ATOM 654 N VAL A 85 11.656 -2.522 4.556 1.00 14.35 N ANISOU 654 N VAL A 85 1511 110 20 1846 2093 137 N ATOM 655 CA VAL A 85 10.616 -3.190 5.340 1.00 15.11 C ANISOU 655 CA VAL A 85 1580 79 105 2066 2094 140 C ATOM 656 C VAL A 85 11.229 -3.982 6.487 1.00 15.38 C ANISOU 656 C VAL A 85 1697 39 94 2037 2109 75 C ATOM 657 O VAL A 85 12.291 -4.591 6.348 1.00 16.57 O ANISOU 657 O VAL A 85 1576 232 269 2408 2310 190 O ATOM 658 CB VAL A 85 9.841 -4.152 4.415 1.00 15.01 C ANISOU 658 CB VAL A 85 1668 45 14 1958 2074 176 C ATOM 659 CG1 VAL A 85 8.801 -4.959 5.196 1.00 15.88 C ANISOU 659 CG1 VAL A 85 1774 -99 51 2309 1951 253 C ATOM 660 CG2 VAL A 85 9.124 -3.374 3.300 1.00 15.90 C ANISOU 660 CG2 VAL A 85 1924 -73 144 1985 2129 155 C ATOM 661 N LYS A 86 10.564 -3.943 7.637 1.00 15.12 N ANISOU 661 N LYS A 86 1619 92 125 2118 2006 148 N ATOM 662 CA LYS A 86 10.900 -4.748 8.801 1.00 15.94 C ANISOU 662 CA LYS A 86 1725 49 151 2230 2099 -47 C ATOM 663 C LYS A 86 9.651 -5.437 9.302 1.00 15.27 C ANISOU 663 C LYS A 86 1697 39 215 2223 1878 -73 C ATOM 664 O LYS A 86 8.545 -4.944 9.122 1.00 16.33 O ANISOU 664 O LYS A 86 1742 123 257 2410 2053 -45 O ATOM 665 CB LYS A 86 11.451 -3.870 9.905 1.00 18.62 C ANISOU 665 CB LYS A 86 2032 -277 330 2614 2428 -141 C ATOM 666 N TRP A 87 9.812 -6.559 10.002 1.00 15.64 N ANISOU 666 N TRP A 87 1592 37 220 2320 2029 -162 N ATOM 667 CA TRP A 87 8.729 -7.154 10.712 1.00 15.83 C ANISOU 667 CA TRP A 87 1715 1 172 2374 1926 -99 C ATOM 668 C TRP A 87 8.565 -6.440 12.049 1.00 17.50 C ANISOU 668 C TRP A 87 1989 64 97 2593 2065 -105 C ATOM 669 O TRP A 87 9.494 -6.410 12.864 1.00 19.85 O ANISOU 669 O TRP A 87 2125 97 30 3295 2120 -401 O ATOM 670 CB TRP A 87 8.975 -8.657 10.963 1.00 17.00 C ANISOU 670 CB TRP A 87 1920 65 254 2487 2051 -126 C ATOM 671 CG TRP A 87 8.968 -9.526 9.776 1.00 17.50 C ANISOU 671 CG TRP A 87 2046 137 275 2299 2303 0 C ATOM 672 CD1 TRP A 87 10.005 -10.181 9.260 1.00 18.42 C ANISOU 672 CD1 TRP A 87 2184 125 297 2408 2407 -118 C ATOM 673 CD2 TRP A 87 7.831 -9.854 8.981 1.00 16.44 C ANISOU 673 CD2 TRP A 87 2003 -25 317 2298 1945 -96 C ATOM 674 NE1 TRP A 87 9.624 -10.868 8.160 1.00 18.80 N ANISOU 674 NE1 TRP A 87 2278 158 126 2387 2478 122 N ATOM 675 CE2 TRP A 87 8.272 -10.705 7.978 1.00 17.34 C ANISOU 675 CE2 TRP A 87 2112 -30 342 2289 2186 23 C ATOM 676 CE3 TRP A 87 6.469 -9.547 9.048 1.00 17.67 C ANISOU 676 CE3 TRP A 87 2076 56 43 2457 2177 -64 C ATOM 677 CZ2 TRP A 87 7.408 -11.244 7.022 1.00 18.85 C ANISOU 677 CZ2 TRP A 87 2508 120 69 2455 2199 59 C ATOM 678 CZ3 TRP A 87 5.616 -10.066 8.111 1.00 18.17 C ANISOU 678 CZ3 TRP A 87 2221 -63 112 2473 2209 13 C ATOM 679 CH2 TRP A 87 6.090 -10.902 7.112 1.00 18.81 C ANISOU 679 CH2 TRP A 87 2386 -25 105 2528 2232 -125 C ATOM 680 N GLU A 88 7.419 -5.841 12.289 1.00 18.23 N ANISOU 680 N GLU A 88 2063 180 47 3008 1855 -163 N ATOM 681 CA GLU A 88 7.101 -5.284 13.596 1.00 19.89 C ANISOU 681 CA GLU A 88 2241 108 82 3219 2097 -110 C ATOM 682 C GLU A 88 6.696 -6.400 14.536 1.00 20.86 C ANISOU 682 C GLU A 88 2446 101 135 3418 2061 -44 C ATOM 683 O GLU A 88 6.970 -6.339 15.748 1.00 24.67 O ANISOU 683 O GLU A 88 3047 219 241 4291 2034 -154 O ATOM 684 CB GLU A 88 5.966 -4.279 13.480 1.00 20.76 C ANISOU 684 CB GLU A 88 2496 185 -146 3246 2146 2 C ATOM 685 CG GLU A 88 5.553 -3.684 14.826 1.00 23.14 C ANISOU 685 CG GLU A 88 2879 248 -299 3455 2457 21 C ATOM 686 CD GLU A 88 4.511 -2.639 14.686 1.00 23.91 C ANISOU 686 CD GLU A 88 2989 160 -154 3440 2653 -54 C ATOM 687 OE1 GLU A 88 4.849 -1.554 14.170 1.00 27.46 O ANISOU 687 OE1 GLU A 88 3723 462 -12 3660 3048 322 O ATOM 688 OE2 GLU A 88 3.373 -2.910 15.125 1.00 27.41 O ANISOU 688 OE2 GLU A 88 3146 217 -535 4099 3169 -223 O ATOM 689 N SER A 89 5.989 -7.378 13.999 1.00 20.75 N ANISOU 689 N SER A 89 2332 -6 362 3426 2124 -67 N ATOM 690 CA SER A 89 5.527 -8.566 14.697 1.00 21.68 C ANISOU 690 CA SER A 89 2391 47 396 3325 2520 -145 C ATOM 691 C SER A 89 5.445 -9.720 13.735 1.00 22.31 C ANISOU 691 C SER A 89 2266 -29 482 3360 2847 -268 C ATOM 692 O SER A 89 5.679 -9.560 12.546 1.00 23.23 O ANISOU 692 O SER A 89 2484 -167 527 3539 2801 -261 O ATOM 693 CB ASER A 89 4.290 -8.293 15.545 0.50 23.21 C ANISOU 693 CB ASER A 89 2726 45 366 3407 2685 3 C ATOM 694 OG ASER A 89 3.353 -7.496 14.860 0.50 22.48 O ANISOU 694 OG ASER A 89 2790 124 218 3317 2434 1 O ATOM 695 N GLU A 90 5.034 -10.880 14.211 1.00 23.95 N ANISOU 695 N GLU A 90 2685 68 679 3429 2984 -458 N ATOM 696 CA GLU A 90 4.921 -12.041 13.398 1.00 24.08 C ANISOU 696 CA GLU A 90 2882 218 572 3154 3111 -339 C ATOM 697 C GLU A 90 4.035 -11.796 12.163 1.00 23.38 C ANISOU 697 C GLU A 90 2599 59 402 3127 3157 -293 C ATOM 698 O GLU A 90 4.287 -12.322 11.082 1.00 24.14 O ANISOU 698 O GLU A 90 2773 410 549 2977 3420 66 O ATOM 699 CB GLU A 90 4.335 -13.212 14.264 1.00 26.05 C ANISOU 699 CB GLU A 90 3247 162 601 3451 3197 -376 C ATOM 700 CG GLU A 90 4.025 -14.430 13.431 1.00 28.56 C ANISOU 700 CG GLU A 90 3618 113 451 3637 3595 -280 C ATOM 701 CD GLU A 90 3.680 -15.687 14.212 1.00 31.53 C ANISOU 701 CD GLU A 90 4154 77 390 3712 4114 -202 C ATOM 702 OE1 GLU A 90 3.241 -15.580 15.376 1.00 39.51 O ANISOU 702 OE1 GLU A 90 5298 226 249 4932 4781 160 O ATOM 703 OE2 GLU A 90 3.850 -16.775 13.628 1.00 40.59 O ANISOU 703 OE2 GLU A 90 5553 185 -118 4875 4992 -84 O ATOM 704 N ASN A 91 3.002 -10.994 12.320 1.00 19.92 N ANISOU 704 N ASN A 91 2173 52 576 2683 2710 -150 N ATOM 705 CA ASN A 91 1.952 -10.849 11.302 1.00 18.11 C ANISOU 705 CA ASN A 91 2149 4 356 2484 2247 -155 C ATOM 706 C ASN A 91 1.918 -9.506 10.640 1.00 16.30 C ANISOU 706 C ASN A 91 1878 69 297 2191 2123 -68 C ATOM 707 O ASN A 91 0.992 -9.235 9.885 1.00 15.93 O ANISOU 707 O ASN A 91 1985 26 110 2056 2010 -200 O ATOM 708 CB ASN A 91 0.627 -11.152 11.956 1.00 19.62 C ANISOU 708 CB ASN A 91 2225 -102 345 2750 2478 -105 C ATOM 709 CG ASN A 91 0.583 -12.535 12.491 1.00 22.27 C ANISOU 709 CG ASN A 91 2566 -124 250 3034 2860 -110 C ATOM 710 OD1 ASN A 91 0.907 -13.473 11.793 1.00 25.04 O ANISOU 710 OD1 ASN A 91 3592 -348 611 2648 3272 -107 O ATOM 711 ND2 ASN A 91 0.283 -12.664 13.753 1.00 25.56 N ANISOU 711 ND2 ASN A 91 3083 -80 587 3455 3172 265 N ATOM 712 N LYS A 92 2.892 -8.656 10.907 1.00 15.69 N ANISOU 712 N LYS A 92 1791 91 271 2217 1951 -193 N ATOM 713 CA LYS A 92 2.834 -7.262 10.490 1.00 14.97 C ANISOU 713 CA LYS A 92 1659 79 120 2188 1841 10 C ATOM 714 C LYS A 92 4.190 -6.743 10.041 1.00 14.88 C ANISOU 714 C LYS A 92 1629 0 42 2275 1747 -31 C ATOM 715 O LYS A 92 5.153 -6.790 10.810 1.00 16.37 O ANISOU 715 O LYS A 92 1751 -31 175 2615 1851 -189 O ATOM 716 CB LYS A 92 2.327 -6.379 11.612 1.00 16.22 C ANISOU 716 CB LYS A 92 1931 -80 68 2369 1863 3 C ATOM 717 CG LYS A 92 2.254 -4.892 11.238 1.00 16.57 C ANISOU 717 CG LYS A 92 1940 -9 -220 2380 1974 136 C ATOM 718 CD LYS A 92 1.697 -4.097 12.393 1.00 18.81 C ANISOU 718 CD LYS A 92 2129 -12 -131 2567 2451 319 C ATOM 719 CE LYS A 92 1.695 -2.621 12.135 1.00 19.76 C ANISOU 719 CE LYS A 92 2258 81 -287 2639 2608 508 C ATOM 720 NZ LYS A 92 1.339 -1.856 13.353 1.00 21.22 N ANISOU 720 NZ LYS A 92 2743 -31 -370 3076 2244 253 N ATOM 721 N MET A 93 4.233 -6.184 8.841 1.00 13.91 N ANISOU 721 N MET A 93 1528 -48 107 2042 1714 0 N ATOM 722 CA MET A 93 5.432 -5.528 8.323 1.00 14.70 C ANISOU 722 CA MET A 93 1602 12 16 2049 1934 -2 C ATOM 723 C MET A 93 5.221 -4.040 8.213 1.00 14.32 C ANISOU 723 C MET A 93 1579 1 29 1999 1861 29 C ATOM 724 O MET A 93 4.092 -3.569 8.020 1.00 14.54 O ANISOU 724 O MET A 93 1551 19 40 1916 2057 16 O ATOM 725 CB MET A 93 5.824 -6.105 6.968 1.00 15.68 C ANISOU 725 CB MET A 93 1684 -115 123 2089 2182 207 C ATOM 726 CG MET A 93 4.939 -5.718 5.856 1.00 17.13 C ANISOU 726 CG MET A 93 2033 34 -99 2290 2182 71 C ATOM 727 SD MET A 93 5.214 -6.540 4.284 1.00 18.22 S ANISOU 727 SD MET A 93 2172 66 -6 2494 2253 121 S ATOM 728 CE MET A 93 4.354 -8.077 4.592 1.00 17.80 C ANISOU 728 CE MET A 93 1916 -177 -28 2094 2751 37 C ATOM 729 N VAL A 94 6.303 -3.299 8.351 1.00 14.39 N ANISOU 729 N VAL A 94 1574 -19 -36 1989 1902 45 N ATOM 730 CA VAL A 94 6.288 -1.864 8.323 1.00 14.71 C ANISOU 730 CA VAL A 94 1647 -6 -13 1984 1957 65 C ATOM 731 C VAL A 94 7.384 -1.382 7.367 1.00 14.64 C ANISOU 731 C VAL A 94 1726 -54 -52 1874 1962 41 C ATOM 732 O VAL A 94 8.512 -1.863 7.432 1.00 15.94 O ANISOU 732 O VAL A 94 1664 30 133 2249 2141 7 O ATOM 733 CB AVAL A 94 6.400 -1.264 9.730 0.50 16.71 C ANISOU 733 CB AVAL A 94 2035 -69 -115 2187 2125 75 C ATOM 734 CG1AVAL A 94 5.244 -1.765 10.615 0.50 17.04 C ANISOU 734 CG1AVAL A 94 1969 145 54 2564 1939 -98 C ATOM 735 CG2AVAL A 94 7.712 -1.618 10.355 0.50 17.24 C ANISOU 735 CG2AVAL A 94 2266 34 -42 2352 1931 25 C ATOM 736 N CYS A 95 7.070 -0.412 6.529 1.00 15.53 N ANISOU 736 N CYS A 95 1571 96 89 2006 2322 207 N ATOM 737 CA CYS A 95 7.980 0.101 5.515 1.00 15.74 C ANISOU 737 CA CYS A 95 1737 220 67 1912 2331 237 C ATOM 738 C CYS A 95 8.253 1.559 5.761 1.00 15.99 C ANISOU 738 C CYS A 95 1628 135 39 1929 2517 226 C ATOM 739 O CYS A 95 7.328 2.360 5.833 1.00 18.50 O ANISOU 739 O CYS A 95 1839 144 20 1964 3225 231 O ATOM 740 CB CYS A 95 7.389 -0.076 4.143 1.00 15.76 C ANISOU 740 CB CYS A 95 1752 148 35 1858 2375 325 C ATOM 741 SG CYS A 95 8.544 0.405 2.849 1.00 18.26 S ANISOU 741 SG CYS A 95 1794 -60 287 2765 2377 198 S ATOM 742 N GLU A 96 9.534 1.899 5.919 1.00 16.64 N ANISOU 742 N GLU A 96 1797 -2 -107 1994 2529 103 N ATOM 743 CA GLU A 96 9.955 3.264 5.994 1.00 17.86 C ANISOU 743 CA GLU A 96 2007 -86 -76 2166 2611 121 C ATOM 744 C GLU A 96 10.477 3.686 4.605 1.00 17.11 C ANISOU 744 C GLU A 96 2111 -200 -118 1856 2532 222 C ATOM 745 O GLU A 96 11.194 2.964 3.967 1.00 18.44 O ANISOU 745 O GLU A 96 2259 76 133 2103 2641 321 O ATOM 746 CB GLU A 96 11.042 3.384 7.018 1.00 19.85 C ANISOU 746 CB GLU A 96 2491 -370 33 2384 2665 64 C ATOM 747 N GLN A 97 10.129 4.895 4.177 1.00 18.82 N ANISOU 747 N GLN A 97 2334 16 -159 1991 2826 307 N ATOM 748 CA GLN A 97 10.468 5.430 2.854 1.00 18.40 C ANISOU 748 CA GLN A 97 2209 -2 -14 1883 2898 253 C ATOM 749 C GLN A 97 11.358 6.657 2.998 1.00 19.31 C ANISOU 749 C GLN A 97 2254 34 -64 2026 3058 178 C ATOM 750 O GLN A 97 11.118 7.479 3.866 1.00 21.96 O ANISOU 750 O GLN A 97 2614 -61 -210 2276 3452 315 O ATOM 751 CB GLN A 97 9.211 5.829 2.072 1.00 18.60 C ANISOU 751 CB GLN A 97 2187 -35 -12 1982 2895 255 C ATOM 752 CG GLN A 97 8.279 4.651 1.866 1.00 18.01 C ANISOU 752 CG GLN A 97 2097 -98 -10 1994 2751 350 C ATOM 753 CD GLN A 97 7.041 4.967 1.056 1.00 18.73 C ANISOU 753 CD GLN A 97 2228 -76 277 1980 2907 383 C ATOM 754 OE1 GLN A 97 6.462 6.038 1.199 1.00 20.80 O ANISOU 754 OE1 GLN A 97 2254 53 40 2153 3494 201 O ATOM 755 NE2 GLN A 97 6.608 4.028 0.246 1.00 19.18 N ANISOU 755 NE2 GLN A 97 2203 -220 191 2349 2735 272 N ATOM 756 N LYS A 98 12.333 6.788 2.106 1.00 19.21 N ANISOU 756 N LYS A 98 2139 -95 -13 1916 3243 266 N ATOM 757 CA LYS A 98 13.251 7.940 2.026 1.00 20.31 C ANISOU 757 CA LYS A 98 2285 -83 38 2206 3223 163 C ATOM 758 C LYS A 98 13.284 8.400 0.589 1.00 19.43 C ANISOU 758 C LYS A 98 2059 -175 172 2060 3262 197 C ATOM 759 O LYS A 98 13.606 7.643 -0.298 1.00 21.14 O ANISOU 759 O LYS A 98 2545 -47 337 2207 3279 22 O ATOM 760 CB LYS A 98 14.637 7.529 2.478 1.00 21.27 C ANISOU 760 CB LYS A 98 2410 -291 66 2408 3261 53 C ATOM 761 N LEU A 99 12.927 9.648 0.309 1.00 21.59 N ANISOU 761 N LEU A 99 2378 -52 153 2363 3460 228 N ATOM 762 CA LEU A 99 12.913 10.113 -1.095 1.00 22.47 C ANISOU 762 CA LEU A 99 2536 -10 225 2472 3526 93 C ATOM 763 C LEU A 99 14.282 9.989 -1.790 1.00 23.78 C ANISOU 763 C LEU A 99 2535 -134 176 2825 3673 126 C ATOM 764 O LEU A 99 15.327 10.229 -1.148 1.00 25.57 O ANISOU 764 O LEU A 99 2538 -90 309 3129 4046 153 O ATOM 765 CB LEU A 99 12.480 11.560 -1.171 1.00 23.28 C ANISOU 765 CB LEU A 99 2753 42 343 2353 3737 46 C ATOM 766 CG LEU A 99 11.000 11.805 -0.865 1.00 25.06 C ANISOU 766 CG LEU A 99 3122 56 162 2502 3897 171 C ATOM 767 CD1 LEU A 99 10.833 13.289 -0.760 1.00 28.47 C ANISOU 767 CD1 LEU A 99 3791 289 222 2799 4227 38 C ATOM 768 CD2 LEU A 99 10.071 11.292 -1.920 1.00 25.62 C ANISOU 768 CD2 LEU A 99 3118 219 181 2858 3756 188 C ATOM 769 N LEU A 100 14.295 9.605 -3.073 1.00 25.10 N ANISOU 769 N LEU A 100 2560 -35 266 3182 3794 232 N ATOM 770 CA LEU A 100 15.564 9.559 -3.832 1.00 26.38 C ANISOU 770 CA LEU A 100 2909 -5 172 3240 3874 262 C ATOM 771 C LEU A 100 16.106 10.954 -4.057 1.00 28.93 C ANISOU 771 C LEU A 100 3175 -106 137 3577 4239 258 C ATOM 772 O LEU A 100 17.330 11.137 -4.095 1.00 30.92 O ANISOU 772 O LEU A 100 3179 -232 50 4033 4534 599 O ATOM 773 CB LEU A 100 15.432 8.802 -5.160 1.00 27.23 C ANISOU 773 CB LEU A 100 3018 26 256 3440 3886 149 C ATOM 774 CG LEU A 100 15.164 7.301 -5.024 1.00 27.09 C ANISOU 774 CG LEU A 100 3121 113 196 3364 3808 102 C ATOM 775 CD1 LEU A 100 15.217 6.633 -6.378 1.00 29.79 C ANISOU 775 CD1 LEU A 100 3678 114 91 3726 3914 37 C ATOM 776 CD2 LEU A 100 16.103 6.584 -4.070 1.00 27.74 C ANISOU 776 CD2 LEU A 100 3452 115 161 3329 3759 185 C ATOM 777 N LYS A 101 15.219 11.923 -4.249 1.00 30.08 N ANISOU 777 N LYS A 101 3502 -165 228 3511 4414 378 N ATOM 778 CA LYS A 101 15.615 13.307 -4.548 1.00 31.19 C ANISOU 778 CA LYS A 101 3784 -99 122 3611 4456 242 C ATOM 779 C LYS A 101 14.746 14.223 -3.714 1.00 32.44 C ANISOU 779 C LYS A 101 3933 -81 92 3798 4593 266 C ATOM 780 O LYS A 101 13.544 14.010 -3.588 1.00 33.78 O ANISOU 780 O LYS A 101 3978 -135 128 4002 4854 461 O ATOM 781 CB LYS A 101 15.400 13.587 -6.014 1.00 32.59 C ANISOU 781 CB LYS A 101 4071 -147 95 3762 4547 211 C ATOM 782 N GLY A 102 15.353 15.216 -3.092 1.00 32.21 N ANISOU 782 N GLY A 102 3894 -22 73 3687 4654 278 N ATOM 783 CA GLY A 102 14.577 16.258 -2.474 1.00 31.93 C ANISOU 783 CA GLY A 102 3923 14 71 3599 4608 276 C ATOM 784 C GLY A 102 14.056 15.860 -1.113 1.00 31.24 C ANISOU 784 C GLY A 102 3797 89 117 3463 4609 264 C ATOM 785 O GLY A 102 14.516 14.891 -0.471 1.00 30.77 O ANISOU 785 O GLY A 102 3612 29 246 3230 4847 352 O ATOM 786 N GLU A 103 13.073 16.617 -0.660 1.00 30.35 N ANISOU 786 N GLU A 103 3686 193 183 3196 4646 287 N ATOM 787 CA GLU A 103 12.552 16.459 0.683 1.00 29.02 C ANISOU 787 CA GLU A 103 3508 213 108 3092 4427 249 C ATOM 788 C GLU A 103 11.042 16.473 0.667 1.00 27.83 C ANISOU 788 C GLU A 103 3374 130 144 2857 4341 299 C ATOM 789 O GLU A 103 10.435 16.856 -0.318 1.00 26.80 O ANISOU 789 O GLU A 103 3274 63 186 2409 4500 482 O ATOM 790 CB GLU A 103 13.047 17.552 1.579 1.00 29.90 C ANISOU 790 CB GLU A 103 3333 194 98 3466 4562 144 C ATOM 791 CG GLU A 103 14.551 17.653 1.639 1.00 29.97 C ANISOU 791 CG GLU A 103 3223 155 91 3563 4600 253 C ATOM 792 CD GLU A 103 14.950 18.879 2.395 0.50 30.57 C ANISOU 792 CD GLU A 103 3614 156 29 3583 4415 116 C ATOM 793 OE1 GLU A 103 15.617 19.752 1.807 0.50 32.62 O ANISOU 793 OE1 GLU A 103 3857 239 208 3965 4569 182 O ATOM 794 OE2 GLU A 103 14.549 18.984 3.567 0.50 31.23 O ANISOU 794 OE2 GLU A 103 3589 12 184 3961 4317 -20 O ATOM 795 N GLY A 104 10.433 16.004 1.750 1.00 26.71 N ANISOU 795 N GLY A 104 3224 285 171 2584 4339 354 N ATOM 796 CA GLY A 104 8.983 15.881 1.761 1.00 26.87 C ANISOU 796 CA GLY A 104 3301 84 97 2688 4217 262 C ATOM 797 C GLY A 104 8.489 15.345 3.077 1.00 25.71 C ANISOU 797 C GLY A 104 3164 98 22 2555 4046 279 C ATOM 798 O GLY A 104 9.243 15.180 4.010 1.00 26.44 O ANISOU 798 O GLY A 104 2852 28 57 2782 4410 343 O ATOM 799 N PRO A 105 7.166 15.147 3.191 1.00 24.86 N ANISOU 799 N PRO A 105 3091 -90 -35 2305 4048 201 N ATOM 800 CA PRO A 105 6.579 14.555 4.390 1.00 24.93 C ANISOU 800 CA PRO A 105 3112 -28 -82 2410 3950 187 C ATOM 801 C PRO A 105 7.128 13.154 4.724 1.00 22.74 C ANISOU 801 C PRO A 105 2923 -137 -194 1997 3717 226 C ATOM 802 O PRO A 105 7.633 12.464 3.843 1.00 25.89 O ANISOU 802 O PRO A 105 3476 -181 -32 2177 4184 554 O ATOM 803 CB PRO A 105 5.083 14.431 4.016 1.00 25.27 C ANISOU 803 CB PRO A 105 3140 -32 -45 2453 4007 154 C ATOM 804 CG PRO A 105 4.862 15.285 2.850 1.00 27.39 C ANISOU 804 CG PRO A 105 3262 -279 -23 3181 3961 92 C ATOM 805 CD PRO A 105 6.187 15.453 2.155 1.00 26.15 C ANISOU 805 CD PRO A 105 3236 -228 -127 2751 3949 235 C ATOM 806 N LYS A 106 7.078 12.772 5.987 1.00 23.74 N ANISOU 806 N LYS A 106 2967 -205 -218 2139 3911 136 N ATOM 807 CA LYS A 106 7.497 11.427 6.357 1.00 22.52 C ANISOU 807 CA LYS A 106 2787 -227 -227 2108 3659 197 C ATOM 808 C LYS A 106 6.434 10.431 5.949 1.00 22.53 C ANISOU 808 C LYS A 106 2639 -299 -328 2241 3678 266 C ATOM 809 O LYS A 106 5.370 10.440 6.560 1.00 24.12 O ANISOU 809 O LYS A 106 2787 -339 -581 2368 4009 481 O ATOM 810 CB LYS A 106 7.726 11.330 7.822 1.00 24.14 C ANISOU 810 CB LYS A 106 2965 -243 -173 2326 3879 30 C ATOM 811 N THR A 107 6.747 9.548 4.995 1.00 20.91 N ANISOU 811 N THR A 107 2408 -293 -246 2014 3521 360 N ATOM 812 CA THR A 107 5.765 8.548 4.522 1.00 20.00 C ANISOU 812 CA THR A 107 2251 -222 -169 1952 3395 328 C ATOM 813 C THR A 107 6.174 7.135 4.864 1.00 18.67 C ANISOU 813 C THR A 107 2024 -233 -138 1947 3119 366 C ATOM 814 O THR A 107 7.353 6.798 4.941 1.00 19.56 O ANISOU 814 O THR A 107 2065 -260 -278 1968 3397 395 O ATOM 815 CB THR A 107 5.516 8.686 2.997 1.00 20.43 C ANISOU 815 CB THR A 107 2329 -153 -155 1934 3498 329 C ATOM 816 OG1 THR A 107 6.739 8.487 2.289 1.00 22.57 O ANISOU 816 OG1 THR A 107 2374 -234 167 2384 3816 445 O ATOM 817 CG2 THR A 107 4.980 10.056 2.673 1.00 23.33 C ANISOU 817 CG2 THR A 107 2836 37 80 2267 3760 221 C ATOM 818 N SER A 108 5.171 6.304 5.044 1.00 17.93 N ANISOU 818 N SER A 108 1922 -260 -117 1897 2991 329 N ATOM 819 CA SER A 108 5.383 4.937 5.431 1.00 17.78 C ANISOU 819 CA SER A 108 1892 -96 -60 1936 2925 246 C ATOM 820 C SER A 108 4.144 4.132 5.053 1.00 16.36 C ANISOU 820 C SER A 108 1649 -105 -233 1800 2765 340 C ATOM 821 O SER A 108 3.090 4.704 4.744 1.00 17.28 O ANISOU 821 O SER A 108 1835 15 -128 1713 3016 285 O ATOM 822 CB SER A 108 5.665 4.832 6.909 1.00 19.51 C ANISOU 822 CB SER A 108 2161 -121 -110 2185 3065 280 C ATOM 823 OG SER A 108 4.667 5.440 7.695 1.00 21.28 O ANISOU 823 OG SER A 108 2477 -44 -54 2658 2948 337 O ATOM 824 N TRP A 109 4.269 2.814 5.099 1.00 16.43 N ANISOU 824 N TRP A 109 1631 6 -50 1701 2908 180 N ATOM 825 CA TRP A 109 3.116 1.931 4.967 1.00 15.37 C ANISOU 825 CA TRP A 109 1512 -6 21 1732 2596 187 C ATOM 826 C TRP A 109 3.304 0.706 5.816 1.00 15.17 C ANISOU 826 C TRP A 109 1522 22 1 1647 2594 107 C ATOM 827 O TRP A 109 4.422 0.390 6.224 1.00 16.01 O ANISOU 827 O TRP A 109 1470 -13 -67 1730 2882 65 O ATOM 828 CB TRP A 109 2.849 1.580 3.496 1.00 15.74 C ANISOU 828 CB TRP A 109 1679 -47 173 1613 2689 179 C ATOM 829 CG TRP A 109 3.926 0.894 2.702 1.00 15.77 C ANISOU 829 CG TRP A 109 1721 79 47 1799 2468 136 C ATOM 830 CD1 TRP A 109 4.746 1.501 1.797 1.00 17.76 C ANISOU 830 CD1 TRP A 109 2032 105 207 1964 2749 272 C ATOM 831 CD2 TRP A 109 4.254 -0.501 2.652 1.00 15.55 C ANISOU 831 CD2 TRP A 109 1589 -55 115 1845 2475 159 C ATOM 832 NE1 TRP A 109 5.569 0.583 1.219 1.00 17.50 N ANISOU 832 NE1 TRP A 109 1816 0 120 2217 2613 313 N ATOM 833 CE2 TRP A 109 5.300 -0.643 1.729 1.00 16.88 C ANISOU 833 CE2 TRP A 109 1832 41 1 1943 2636 144 C ATOM 834 CE3 TRP A 109 3.805 -1.629 3.329 1.00 16.14 C ANISOU 834 CE3 TRP A 109 1674 60 1 1936 2522 251 C ATOM 835 CZ2 TRP A 109 5.884 -1.881 1.444 1.00 17.31 C ANISOU 835 CZ2 TRP A 109 1799 22 -57 2035 2742 136 C ATOM 836 CZ3 TRP A 109 4.401 -2.849 3.063 1.00 16.39 C ANISOU 836 CZ3 TRP A 109 1782 80 -99 1843 2602 253 C ATOM 837 CH2 TRP A 109 5.422 -2.972 2.125 1.00 17.14 C ANISOU 837 CH2 TRP A 109 1945 160 -66 1949 2618 249 C ATOM 838 N THR A 110 2.193 0.027 6.068 1.00 14.64 N ANISOU 838 N THR A 110 1443 24 -43 1702 2418 46 N ATOM 839 CA THR A 110 2.206 -1.213 6.813 1.00 14.02 C ANISOU 839 CA THR A 110 1573 -6 14 1686 2068 -6 C ATOM 840 C THR A 110 1.265 -2.203 6.172 1.00 13.27 C ANISOU 840 C THR A 110 1505 1 29 1688 1848 123 C ATOM 841 O THR A 110 0.293 -1.816 5.535 1.00 13.67 O ANISOU 841 O THR A 110 1514 97 66 1746 1933 51 O ATOM 842 CB THR A 110 1.841 -1.057 8.313 1.00 15.04 C ANISOU 842 CB THR A 110 1642 54 -229 1824 2245 -116 C ATOM 843 OG1 THR A 110 0.431 -0.867 8.479 1.00 16.05 O ANISOU 843 OG1 THR A 110 1745 -58 -220 2060 2293 124 O ATOM 844 CG2 THR A 110 2.596 0.094 8.941 1.00 16.96 C ANISOU 844 CG2 THR A 110 1847 80 -283 2191 2406 -143 C ATOM 845 N LEU A 111 1.558 -3.482 6.363 1.00 12.91 N ANISOU 845 N LEU A 111 1425 37 37 1715 1766 94 N ATOM 846 CA LEU A 111 0.669 -4.583 6.005 1.00 12.49 C ANISOU 846 CA LEU A 111 1465 42 50 1679 1599 2 C ATOM 847 C LEU A 111 0.598 -5.568 7.133 1.00 12.64 C ANISOU 847 C LEU A 111 1603 49 -51 1550 1647 -12 C ATOM 848 O LEU A 111 1.623 -5.977 7.651 1.00 13.68 O ANISOU 848 O LEU A 111 1633 66 142 1793 1769 -80 O ATOM 849 CB LEU A 111 1.144 -5.324 4.730 1.00 13.60 C ANISOU 849 CB LEU A 111 1643 145 4 1856 1667 86 C ATOM 850 CG LEU A 111 1.074 -4.575 3.397 1.00 14.74 C ANISOU 850 CG LEU A 111 1842 99 -62 1866 1890 116 C ATOM 851 CD1 LEU A 111 1.724 -5.378 2.304 1.00 16.22 C ANISOU 851 CD1 LEU A 111 1959 235 -115 2314 1887 231 C ATOM 852 CD2 LEU A 111 -0.370 -4.264 2.996 1.00 15.69 C ANISOU 852 CD2 LEU A 111 2069 320 -36 2095 1795 4 C ATOM 853 N GLU A 112 -0.619 -5.973 7.465 1.00 12.76 N ANISOU 853 N GLU A 112 1602 54 27 1678 1568 48 N ATOM 854 CA GLU A 112 -0.870 -6.898 8.576 1.00 13.78 C ANISOU 854 CA GLU A 112 1745 35 98 1808 1682 -5 C ATOM 855 C GLU A 112 -1.906 -7.914 8.183 1.00 12.85 C ANISOU 855 C GLU A 112 1701 -21 151 1659 1522 -81 C ATOM 856 O GLU A 112 -2.934 -7.562 7.653 1.00 14.78 O ANISOU 856 O GLU A 112 1779 67 150 1740 2094 -382 O ATOM 857 CB GLU A 112 -1.341 -6.146 9.831 1.00 15.39 C ANISOU 857 CB GLU A 112 2213 -84 78 2058 1575 -47 C ATOM 858 CG GLU A 112 -1.671 -7.043 11.033 1.00 16.46 C ANISOU 858 CG GLU A 112 2301 85 15 2072 1879 -63 C ATOM 859 CD GLU A 112 -1.847 -6.331 12.383 1.00 19.62 C ANISOU 859 CD GLU A 112 2834 60 183 2525 2095 279 C ATOM 860 OE1 GLU A 112 -1.870 -5.109 12.450 1.00 17.99 O ANISOU 860 OE1 GLU A 112 2512 214 -3 2390 1931 181 O ATOM 861 OE2 GLU A 112 -1.850 -7.080 13.408 1.00 25.42 O ANISOU 861 OE2 GLU A 112 4930 186 283 2597 2130 414 O ATOM 862 N LEU A 113 -1.632 -9.186 8.456 1.00 13.87 N ANISOU 862 N LEU A 113 1707 39 120 1746 1815 -169 N ATOM 863 CA LEU A 113 -2.553 -10.290 8.159 1.00 14.71 C ANISOU 863 CA LEU A 113 1992 -28 57 1873 1723 -5 C ATOM 864 C LEU A 113 -3.246 -10.693 9.434 1.00 15.08 C ANISOU 864 C LEU A 113 2048 6 115 1889 1793 -117 C ATOM 865 O LEU A 113 -2.588 -10.978 10.424 1.00 17.63 O ANISOU 865 O LEU A 113 2261 -136 394 2491 1945 -232 O ATOM 866 CB LEU A 113 -1.729 -11.453 7.565 1.00 16.26 C ANISOU 866 CB LEU A 113 2310 10 169 1709 2157 -111 C ATOM 867 CG LEU A 113 -2.510 -12.662 7.083 1.00 17.07 C ANISOU 867 CG LEU A 113 2229 -13 -102 2104 2152 149 C ATOM 868 CD1 LEU A 113 -3.336 -12.244 5.883 1.00 20.89 C ANISOU 868 CD1 LEU A 113 2759 45 -205 2629 2547 -145 C ATOM 869 CD2 LEU A 113 -1.583 -13.779 6.748 1.00 19.28 C ANISOU 869 CD2 LEU A 113 2521 10 -101 2262 2540 247 C ATOM 870 N THR A 114 -4.559 -10.747 9.389 1.00 15.56 N ANISOU 870 N THR A 114 2060 -103 289 2112 1740 -18 N ATOM 871 CA THR A 114 -5.352 -11.091 10.572 1.00 16.52 C ANISOU 871 CA THR A 114 2241 46 132 2202 1834 156 C ATOM 872 C THR A 114 -5.661 -12.576 10.602 1.00 16.57 C ANISOU 872 C THR A 114 2278 83 194 2278 1739 220 C ATOM 873 O THR A 114 -5.478 -13.303 9.645 1.00 17.72 O ANISOU 873 O THR A 114 2539 70 202 2101 2093 366 O ATOM 874 CB THR A 114 -6.688 -10.323 10.587 1.00 17.66 C ANISOU 874 CB THR A 114 2391 -20 150 2429 1887 223 C ATOM 875 OG1 THR A 114 -7.548 -10.863 9.605 1.00 17.63 O ANISOU 875 OG1 THR A 114 2205 -25 285 2531 1962 122 O ATOM 876 CG2 THR A 114 -6.494 -8.851 10.358 1.00 19.64 C ANISOU 876 CG2 THR A 114 2814 134 -15 2411 2237 157 C ATOM 877 N ASN A 115 -6.134 -13.020 11.759 1.00 18.60 N ANISOU 877 N ASN A 115 2546 81 314 2479 2039 386 N ATOM 878 CA ASN A 115 -6.376 -14.446 11.944 1.00 19.85 C ANISOU 878 CA ASN A 115 2645 36 444 2496 2401 373 C ATOM 879 C ASN A 115 -7.416 -15.009 10.972 1.00 21.43 C ANISOU 879 C ASN A 115 3115 -22 352 2531 2493 413 C ATOM 880 O ASN A 115 -7.305 -16.157 10.513 1.00 25.06 O ANISOU 880 O ASN A 115 3704 -90 315 2468 3347 271 O ATOM 881 CB ASN A 115 -6.848 -14.593 13.409 1.00 21.31 C ANISOU 881 CB ASN A 115 2852 72 516 2827 2415 300 C ATOM 882 CG ASN A 115 -7.037 -16.033 13.892 1.00 23.62 C ANISOU 882 CG ASN A 115 3095 212 568 2983 2896 443 C ATOM 883 OD1 ASN A 115 -6.241 -16.952 13.665 1.00 28.28 O ANISOU 883 OD1 ASN A 115 3850 426 671 3585 3310 362 O ATOM 884 ND2 ASN A 115 -8.087 -16.195 14.663 1.00 27.34 N ANISOU 884 ND2 ASN A 115 3696 160 311 3586 3106 442 N ATOM 885 N ASP A 116 -8.419 -14.222 10.589 1.00 21.44 N ANISOU 885 N ASP A 116 2989 -211 462 2664 2491 260 N ATOM 886 CA ASP A 116 -9.410 -14.686 9.632 1.00 22.55 C ANISOU 886 CA ASP A 116 3050 -225 232 2785 2731 183 C ATOM 887 C ASP A 116 -9.005 -14.444 8.171 1.00 22.60 C ANISOU 887 C ASP A 116 3149 -367 242 2737 2697 120 C ATOM 888 O ASP A 116 -9.806 -14.627 7.273 1.00 24.93 O ANISOU 888 O ASP A 116 3479 -550 139 2897 3096 30 O ATOM 889 CB ASP A 116 -10.791 -14.094 9.901 1.00 24.09 C ANISOU 889 CB ASP A 116 3115 -259 218 3187 2852 217 C ATOM 890 CG ASP A 116 -10.951 -12.672 9.390 1.00 26.30 C ANISOU 890 CG ASP A 116 3221 -192 -101 3142 3630 95 C ATOM 891 OD1 ASP A 116 -9.972 -11.908 9.340 1.00 30.95 O ANISOU 891 OD1 ASP A 116 3273 -519 -302 4012 4473 215 O ATOM 892 OD2 ASP A 116 -12.079 -12.300 9.015 1.00 31.58 O ANISOU 892 OD2 ASP A 116 3486 -171 55 4325 4187 5 O ATOM 893 N GLY A 117 -7.770 -14.023 7.939 1.00 20.25 N ANISOU 893 N GLY A 117 2991 -392 32 2202 2499 76 N ATOM 894 CA GLY A 117 -7.235 -13.856 6.606 1.00 20.45 C ANISOU 894 CA GLY A 117 2974 -267 -16 2406 2387 110 C ATOM 895 C GLY A 117 -7.502 -12.526 5.946 1.00 19.42 C ANISOU 895 C GLY A 117 2837 -347 35 2406 2134 119 C ATOM 896 O GLY A 117 -7.410 -12.452 4.735 1.00 22.32 O ANISOU 896 O GLY A 117 3530 -346 82 2874 2074 187 O ATOM 897 N GLU A 118 -7.883 -11.489 6.698 1.00 16.61 N ANISOU 897 N GLU A 118 2321 -380 232 2157 1830 183 N ATOM 898 CA GLU A 118 -7.982 -10.159 6.133 1.00 16.27 C ANISOU 898 CA GLU A 118 2150 -282 124 2150 1880 -88 C ATOM 899 C GLU A 118 -6.610 -9.526 6.125 1.00 14.44 C ANISOU 899 C GLU A 118 1886 -133 57 1949 1650 -192 C ATOM 900 O GLU A 118 -5.754 -9.775 6.957 1.00 16.87 O ANISOU 900 O GLU A 118 2110 -286 400 2349 1948 -192 O ATOM 901 CB GLU A 118 -9.012 -9.318 6.868 1.00 17.54 C ANISOU 901 CB GLU A 118 2198 -189 269 2386 2080 -101 C ATOM 902 CG GLU A 118 -10.368 -10.014 6.778 1.00 21.59 C ANISOU 902 CG GLU A 118 2374 -309 169 3236 2592 57 C ATOM 903 CD GLU A 118 -11.558 -9.290 7.372 0.50 19.82 C ANISOU 903 CD GLU A 118 2476 -196 185 2554 2497 60 C ATOM 904 OE1 GLU A 118 -12.391 -9.986 8.034 0.50 21.61 O ANISOU 904 OE1 GLU A 118 2061 -527 25 3127 3020 340 O ATOM 905 OE2 GLU A 118 -11.680 -8.074 7.191 0.50 20.16 O ANISOU 905 OE2 GLU A 118 2578 -165 131 2687 2393 -251 O ATOM 906 N LEU A 119 -6.397 -8.671 5.145 1.00 13.24 N ANISOU 906 N LEU A 119 1754 -63 9 1639 1635 -133 N ATOM 907 CA LEU A 119 -5.160 -7.912 4.995 1.00 12.83 C ANISOU 907 CA LEU A 119 1610 -22 -116 1680 1582 -71 C ATOM 908 C LEU A 119 -5.448 -6.464 5.269 1.00 12.36 C ANISOU 908 C LEU A 119 1626 -6 20 1578 1489 -45 C ATOM 909 O LEU A 119 -6.271 -5.851 4.583 1.00 13.74 O ANISOU 909 O LEU A 119 1729 89 3 1707 1783 -240 O ATOM 910 CB LEU A 119 -4.635 -8.114 3.592 1.00 13.85 C ANISOU 910 CB LEU A 119 1672 -65 -119 1837 1751 -35 C ATOM 911 CG LEU A 119 -3.386 -7.354 3.219 1.00 14.54 C ANISOU 911 CG LEU A 119 1730 -60 -267 1947 1848 82 C ATOM 912 CD1 LEU A 119 -2.235 -7.878 4.042 1.00 15.99 C ANISOU 912 CD1 LEU A 119 1855 -177 -146 2039 2180 74 C ATOM 913 CD2 LEU A 119 -3.091 -7.472 1.705 1.00 16.65 C ANISOU 913 CD2 LEU A 119 1993 -259 -170 2407 1925 123 C ATOM 914 N ILE A 120 -4.771 -5.906 6.255 1.00 12.48 N ANISOU 914 N ILE A 120 1602 33 -70 1620 1520 15 N ATOM 915 CA ILE A 120 -4.913 -4.500 6.587 1.00 12.05 C ANISOU 915 CA ILE A 120 1493 36 87 1572 1513 34 C ATOM 916 C ILE A 120 -3.691 -3.771 6.060 1.00 12.14 C ANISOU 916 C ILE A 120 1507 35 -16 1559 1543 59 C ATOM 917 O ILE A 120 -2.557 -4.130 6.409 1.00 13.05 O ANISOU 917 O ILE A 120 1431 34 26 1750 1774 13 O ATOM 918 CB ILE A 120 -5.033 -4.262 8.103 1.00 13.38 C ANISOU 918 CB ILE A 120 1663 88 -26 1776 1642 80 C ATOM 919 CG1 ILE A 120 -6.160 -5.083 8.727 1.00 14.02 C ANISOU 919 CG1 ILE A 120 1807 73 98 1752 1765 261 C ATOM 920 CG2 ILE A 120 -5.179 -2.790 8.403 1.00 14.42 C ANISOU 920 CG2 ILE A 120 1922 -1 -125 1866 1689 62 C ATOM 921 CD1 ILE A 120 -6.158 -5.091 10.230 1.00 15.80 C ANISOU 921 CD1 ILE A 120 2130 116 310 1972 1899 205 C ATOM 922 N GLU A 121 -3.912 -2.722 5.282 1.00 12.77 N ANISOU 922 N GLU A 121 1426 -42 64 1636 1789 52 N ATOM 923 CA GLU A 121 -2.879 -1.812 4.852 1.00 12.91 C ANISOU 923 CA GLU A 121 1448 -10 8 1645 1809 45 C ATOM 924 C GLU A 121 -3.077 -0.487 5.543 1.00 12.82 C ANISOU 924 C GLU A 121 1423 21 89 1672 1773 -6 C ATOM 925 O GLU A 121 -4.173 0.022 5.557 1.00 14.09 O ANISOU 925 O GLU A 121 1480 99 -48 1770 2102 -30 O ATOM 926 CB AGLU A 121 -2.952 -1.618 3.320 0.50 13.79 C ANISOU 926 CB AGLU A 121 1643 72 -51 1729 1868 24 C ATOM 927 CG AGLU A 121 -1.806 -0.879 2.711 0.50 14.54 C ANISOU 927 CG AGLU A 121 1919 151 -39 1672 1932 103 C ATOM 928 CD AGLU A 121 -2.033 -0.656 1.229 0.50 17.78 C ANISOU 928 CD AGLU A 121 2204 25 197 2370 2180 110 C ATOM 929 OE1AGLU A 121 -3.043 -0.071 0.841 0.50 20.11 O ANISOU 929 OE1AGLU A 121 2846 667 138 2611 2183 245 O ATOM 930 OE2AGLU A 121 -1.203 -1.092 0.429 0.50 25.10 O ANISOU 930 OE2AGLU A 121 3243 625 -175 3054 3238 268 O ATOM 931 N THR A 122 -2.002 0.102 6.044 1.00 13.09 N ANISOU 931 N THR A 122 1516 4 -47 1533 1924 -71 N ATOM 932 CA THR A 122 -2.050 1.503 6.378 1.00 13.94 C ANISOU 932 CA THR A 122 1625 -9 -29 1617 2052 13 C ATOM 933 C THR A 122 -0.996 2.249 5.553 1.00 14.10 C ANISOU 933 C THR A 122 1625 -54 -9 1577 2155 1 C ATOM 934 O THR A 122 0.024 1.686 5.157 1.00 14.76 O ANISOU 934 O THR A 122 1614 77 19 1638 2354 57 O ATOM 935 CB THR A 122 -1.904 1.793 7.871 1.00 15.51 C ANISOU 935 CB THR A 122 1830 50 -28 1774 2289 31 C ATOM 936 OG1 THR A 122 -0.554 1.586 8.296 1.00 16.44 O ANISOU 936 OG1 THR A 122 1897 84 -105 2069 2277 -66 O ATOM 937 CG2 THR A 122 -2.844 0.959 8.696 1.00 16.01 C ANISOU 937 CG2 THR A 122 2088 87 -43 2094 1901 123 C ATOM 938 N MET A 123 -1.291 3.506 5.295 1.00 14.66 N ANISOU 938 N MET A 123 1605 18 -38 1616 2348 127 N ATOM 939 CA MET A 123 -0.367 4.432 4.642 1.00 15.33 C ANISOU 939 CA MET A 123 1845 -33 -50 1621 2358 142 C ATOM 940 C MET A 123 -0.420 5.728 5.413 1.00 15.70 C ANISOU 940 C MET A 123 1753 9 -65 1679 2530 200 C ATOM 941 O MET A 123 -1.495 6.217 5.696 1.00 16.85 O ANISOU 941 O MET A 123 1854 4 -144 1610 2936 187 O ATOM 942 CB MET A 123 -0.748 4.710 3.177 1.00 16.75 C ANISOU 942 CB MET A 123 2109 -108 2 1836 2418 203 C ATOM 943 CG MET A 123 -0.645 3.524 2.269 1.00 18.05 C ANISOU 943 CG MET A 123 2280 28 -56 2395 2182 -108 C ATOM 944 SD MET A 123 -0.979 3.798 0.522 1.00 23.95 S ANISOU 944 SD MET A 123 3077 190 19 3121 2901 -37 S ATOM 945 CE MET A 123 -2.650 4.005 0.755 1.00 24.44 C ANISOU 945 CE MET A 123 3067 112 120 3538 2679 228 C ATOM 946 N THR A 124 0.754 6.268 5.720 1.00 16.14 N ANISOU 946 N THR A 124 1860 -29 -285 1720 2552 237 N ATOM 947 CA THR A 124 0.831 7.457 6.547 1.00 16.66 C ANISOU 947 CA THR A 124 1982 -77 -258 1706 2641 195 C ATOM 948 C THR A 124 1.656 8.508 5.875 1.00 18.04 C ANISOU 948 C THR A 124 2168 -114 -324 1825 2862 313 C ATOM 949 O THR A 124 2.725 8.210 5.308 1.00 20.36 O ANISOU 949 O THR A 124 2298 -174 -395 1893 3542 479 O ATOM 950 CB ATHR A 124 1.578 7.206 7.800 0.50 18.16 C ANISOU 950 CB ATHR A 124 2270 -106 -250 1993 2633 189 C ATOM 951 OG1ATHR A 124 2.924 6.872 7.465 0.50 25.94 O ANISOU 951 OG1ATHR A 124 2964 189 -65 3260 3632 86 O ATOM 952 CG2ATHR A 124 0.925 6.120 8.608 0.50 18.26 C ANISOU 952 CG2ATHR A 124 2253 7 -68 2144 2539 84 C ATOM 953 N ALA A 125 1.244 9.752 6.065 1.00 18.26 N ANISOU 953 N ALA A 125 2247 -230 -320 1748 2943 330 N ATOM 954 CA ALA A 125 2.089 10.914 5.781 1.00 20.69 C ANISOU 954 CA ALA A 125 2699 -181 -303 2031 3129 249 C ATOM 955 C ALA A 125 2.026 11.809 6.977 1.00 21.73 C ANISOU 955 C ALA A 125 2877 -103 -334 2047 3331 159 C ATOM 956 O ALA A 125 0.974 12.316 7.296 1.00 21.23 O ANISOU 956 O ALA A 125 2791 -179 -397 1940 3336 299 O ATOM 957 CB ALA A 125 1.634 11.600 4.575 1.00 22.06 C ANISOU 957 CB ALA A 125 2892 -111 -277 2285 3202 287 C ATOM 958 N ASP A 126 3.151 11.939 7.661 1.00 22.17 N ANISOU 958 N ASP A 126 2916 -255 -468 2022 3482 138 N ATOM 959 CA ASP A 126 3.200 12.713 8.903 1.00 22.84 C ANISOU 959 CA ASP A 126 3023 -141 -370 2283 3370 38 C ATOM 960 C ASP A 126 2.082 12.204 9.849 1.00 23.28 C ANISOU 960 C ASP A 126 3083 -131 -386 2395 3367 92 C ATOM 961 O ASP A 126 2.144 11.056 10.290 1.00 25.21 O ANISOU 961 O ASP A 126 3401 -152 -354 2603 3572 80 O ATOM 962 CB ASP A 126 3.145 14.235 8.637 1.00 23.66 C ANISOU 962 CB ASP A 126 3118 -254 -502 2288 3581 34 C ATOM 963 CG ASP A 126 4.370 14.745 7.902 1.00 25.51 C ANISOU 963 CG ASP A 126 3293 -251 -383 2464 3933 24 C ATOM 964 OD1 ASP A 126 5.448 14.130 8.001 1.00 28.08 O ANISOU 964 OD1 ASP A 126 3477 -488 -594 2649 4542 82 O ATOM 965 OD2 ASP A 126 4.249 15.800 7.238 1.00 29.67 O ANISOU 965 OD2 ASP A 126 3925 -105 62 3092 4256 404 O ATOM 966 N ASP A 127 1.100 13.034 10.208 1.00 23.11 N ANISOU 966 N ASP A 127 3079 -104 -381 2445 3253 158 N ATOM 967 CA ASP A 127 0.050 12.658 11.153 1.00 22.61 C ANISOU 967 CA ASP A 127 3011 -85 -319 2423 3154 94 C ATOM 968 C ASP A 127 -1.285 12.244 10.506 1.00 22.16 C ANISOU 968 C ASP A 127 2878 -112 -324 2504 3038 215 C ATOM 969 O ASP A 127 -2.303 12.230 11.162 1.00 24.51 O ANISOU 969 O ASP A 127 2947 -122 -266 3114 3251 321 O ATOM 970 CB ASP A 127 -0.144 13.809 12.149 1.00 23.98 C ANISOU 970 CB ASP A 127 3146 -10 -357 2795 3167 55 C ATOM 971 CG ASP A 127 -0.538 15.123 11.491 1.00 25.53 C ANISOU 971 CG ASP A 127 3616 -19 -362 2856 3229 124 C ATOM 972 OD1 ASP A 127 -0.433 15.291 10.272 1.00 25.35 O ANISOU 972 OD1 ASP A 127 3884 -10 -661 2353 3393 158 O ATOM 973 OD2 ASP A 127 -0.911 16.067 12.237 1.00 28.38 O ANISOU 973 OD2 ASP A 127 4324 127 -530 2963 3494 526 O ATOM 974 N VAL A 128 -1.294 11.974 9.203 1.00 20.22 N ANISOU 974 N VAL A 128 2785 -94 -348 2083 2812 328 N ATOM 975 CA VAL A 128 -2.509 11.548 8.501 1.00 19.31 C ANISOU 975 CA VAL A 128 2601 35 -320 1956 2777 353 C ATOM 976 C VAL A 128 -2.362 10.083 8.070 1.00 17.91 C ANISOU 976 C VAL A 128 2357 60 -284 1740 2708 326 C ATOM 977 O VAL A 128 -1.366 9.704 7.437 1.00 18.49 O ANISOU 977 O VAL A 128 2386 -27 -275 1921 2716 395 O ATOM 978 CB VAL A 128 -2.750 12.433 7.289 1.00 19.56 C ANISOU 978 CB VAL A 128 2653 70 -258 1902 2877 355 C ATOM 979 CG1 VAL A 128 -3.971 11.989 6.522 1.00 21.58 C ANISOU 979 CG1 VAL A 128 2859 61 38 2051 3288 162 C ATOM 980 CG2 VAL A 128 -2.955 13.882 7.771 1.00 22.80 C ANISOU 980 CG2 VAL A 128 3166 122 -175 2171 3323 325 C ATOM 981 N VAL A 129 -3.344 9.273 8.458 1.00 16.87 N ANISOU 981 N VAL A 129 2309 -33 -277 1792 2307 333 N ATOM 982 CA VAL A 129 -3.311 7.831 8.241 1.00 16.37 C ANISOU 982 CA VAL A 129 2197 63 -180 1844 2177 182 C ATOM 983 C VAL A 129 -4.488 7.431 7.361 1.00 15.14 C ANISOU 983 C VAL A 129 1891 77 -123 1721 2137 202 C ATOM 984 O VAL A 129 -5.613 7.814 7.631 1.00 16.15 O ANISOU 984 O VAL A 129 2085 143 -177 1819 2233 321 O ATOM 985 CB VAL A 129 -3.361 7.079 9.577 1.00 17.77 C ANISOU 985 CB VAL A 129 2343 17 -58 1972 2435 93 C ATOM 986 CG1 VAL A 129 -3.348 5.562 9.322 1.00 18.82 C ANISOU 986 CG1 VAL A 129 2731 63 -76 2045 2374 5 C ATOM 987 CG2 VAL A 129 -2.199 7.457 10.480 1.00 18.74 C ANISOU 987 CG2 VAL A 129 2444 9 -24 2245 2428 10 C ATOM 988 N CYS A 130 -4.219 6.610 6.339 1.00 14.68 N ANISOU 988 N CYS A 130 1793 58 -130 1685 2099 200 N ATOM 989 CA CYS A 130 -5.226 5.943 5.521 1.00 14.45 C ANISOU 989 CA CYS A 130 1709 11 -97 1678 2103 160 C ATOM 990 C CYS A 130 -5.160 4.442 5.819 1.00 13.85 C ANISOU 990 C CYS A 130 1637 10 -7 1698 1927 125 C ATOM 991 O CYS A 130 -4.075 3.888 5.946 1.00 14.61 O ANISOU 991 O CYS A 130 1593 -32 59 1630 2328 139 O ATOM 992 CB CYS A 130 -4.952 6.229 4.027 1.00 15.70 C ANISOU 992 CB CYS A 130 1888 20 45 1790 2288 57 C ATOM 993 SG CYS A 130 -5.771 5.135 2.874 1.00 16.52 S ANISOU 993 SG CYS A 130 2141 95 -55 1784 2351 127 S ATOM 994 N THR A 131 -6.319 3.811 5.980 1.00 13.35 N ANISOU 994 N THR A 131 1544 56 5 1594 1933 255 N ATOM 995 CA THR A 131 -6.420 2.381 6.164 1.00 13.45 C ANISOU 995 CA THR A 131 1649 92 -123 1592 1868 110 C ATOM 996 C THR A 131 -7.252 1.774 5.052 1.00 13.27 C ANISOU 996 C THR A 131 1529 18 12 1643 1867 86 C ATOM 997 O THR A 131 -8.322 2.288 4.716 1.00 14.40 O ANISOU 997 O THR A 131 1616 188 -20 1788 2066 -27 O ATOM 998 CB THR A 131 -7.042 2.051 7.538 1.00 13.74 C ANISOU 998 CB THR A 131 1542 26 43 1732 1947 160 C ATOM 999 OG1 THR A 131 -6.140 2.557 8.528 1.00 14.94 O ANISOU 999 OG1 THR A 131 1974 -50 -99 1778 1924 46 O ATOM 1000 CG2 THR A 131 -7.249 0.574 7.727 1.00 14.31 C ANISOU 1000 CG2 THR A 131 1816 56 64 1791 1829 213 C ATOM 1001 N LYS A 132 -6.772 0.657 4.519 1.00 13.16 N ANISOU 1001 N LYS A 132 1533 57 -95 1588 1878 82 N ATOM 1002 CA LYS A 132 -7.522 -0.169 3.568 1.00 13.37 C ANISOU 1002 CA LYS A 132 1523 62 22 1643 1912 11 C ATOM 1003 C LYS A 132 -7.527 -1.602 4.059 1.00 13.69 C ANISOU 1003 C LYS A 132 1525 118 -51 1771 1902 -39 C ATOM 1004 O LYS A 132 -6.583 -2.043 4.707 1.00 14.88 O ANISOU 1004 O LYS A 132 1708 67 59 1763 2181 -411 O ATOM 1005 CB LYS A 132 -6.914 -0.046 2.165 1.00 14.09 C ANISOU 1005 CB LYS A 132 1666 4 -26 1735 1952 -108 C ATOM 1006 CG LYS A 132 -6.942 1.364 1.621 1.00 14.45 C ANISOU 1006 CG LYS A 132 1877 140 73 1685 1926 223 C ATOM 1007 CD LYS A 132 -6.317 1.469 0.234 1.00 15.59 C ANISOU 1007 CD LYS A 132 1942 70 19 1823 2158 227 C ATOM 1008 CE LYS A 132 -6.264 2.915 -0.268 1.00 17.16 C ANISOU 1008 CE LYS A 132 2272 -79 117 1978 2267 343 C ATOM 1009 NZ LYS A 132 -5.721 2.979 -1.630 1.00 20.60 N ANISOU 1009 NZ LYS A 132 3090 -225 128 2535 2201 476 N ATOM 1010 N VAL A 133 -8.600 -2.316 3.766 1.00 12.33 N ANISOU 1010 N VAL A 133 1338 -67 62 1558 1788 -46 N ATOM 1011 CA VAL A 133 -8.704 -3.713 4.173 1.00 12.85 C ANISOU 1011 CA VAL A 133 1469 60 65 1628 1783 20 C ATOM 1012 C VAL A 133 -9.068 -4.509 2.934 1.00 12.40 C ANISOU 1012 C VAL A 133 1477 -90 8 1499 1734 24 C ATOM 1013 O VAL A 133 -9.905 -4.071 2.143 1.00 12.91 O ANISOU 1013 O VAL A 133 1464 38 -7 1763 1676 -24 O ATOM 1014 CB VAL A 133 -9.741 -3.904 5.287 1.00 13.43 C ANISOU 1014 CB VAL A 133 1664 -13 25 1643 1794 46 C ATOM 1015 CG1 VAL A 133 -9.753 -5.363 5.727 1.00 14.05 C ANISOU 1015 CG1 VAL A 133 1721 -39 114 1870 1746 232 C ATOM 1016 CG2 VAL A 133 -9.493 -3.008 6.457 1.00 14.62 C ANISOU 1016 CG2 VAL A 133 1735 104 -40 1952 1867 146 C ATOM 1017 N PHE A 134 -8.445 -5.670 2.786 1.00 12.70 N ANISOU 1017 N PHE A 134 1664 44 37 1657 1503 3 N ATOM 1018 CA PHE A 134 -8.634 -6.572 1.673 1.00 12.95 C ANISOU 1018 CA PHE A 134 1645 46 -3 1623 1649 -84 C ATOM 1019 C PHE A 134 -8.931 -7.971 2.143 1.00 12.95 C ANISOU 1019 C PHE A 134 1495 -14 -26 1717 1708 -40 C ATOM 1020 O PHE A 134 -8.567 -8.372 3.242 1.00 13.91 O ANISOU 1020 O PHE A 134 1797 -57 58 1859 1626 -110 O ATOM 1021 CB PHE A 134 -7.370 -6.626 0.787 1.00 13.35 C ANISOU 1021 CB PHE A 134 1832 44 -22 1604 1637 -18 C ATOM 1022 CG PHE A 134 -6.837 -5.281 0.296 1.00 13.72 C ANISOU 1022 CG PHE A 134 1665 48 -81 1757 1789 12 C ATOM 1023 CD1 PHE A 134 -6.083 -4.469 1.115 1.00 13.87 C ANISOU 1023 CD1 PHE A 134 1819 -81 17 1749 1702 142 C ATOM 1024 CD2 PHE A 134 -7.044 -4.884 -1.012 1.00 13.63 C ANISOU 1024 CD2 PHE A 134 1691 -51 86 1807 1678 31 C ATOM 1025 CE1 PHE A 134 -5.610 -3.284 0.683 1.00 15.20 C ANISOU 1025 CE1 PHE A 134 1755 -65 -235 1904 2115 157 C ATOM 1026 CE2 PHE A 134 -6.560 -3.678 -1.461 1.00 14.56 C ANISOU 1026 CE2 PHE A 134 1766 -31 236 1928 1837 128 C ATOM 1027 CZ PHE A 134 -5.831 -2.880 -0.597 1.00 15.07 C ANISOU 1027 CZ PHE A 134 1857 -87 53 1749 2118 324 C ATOM 1028 N VAL A 135 -9.566 -8.739 1.262 1.00 14.19 N ANISOU 1028 N VAL A 135 1752 -29 -87 1848 1789 -178 N ATOM 1029 CA VAL A 135 -9.761 -10.192 1.442 1.00 14.44 C ANISOU 1029 CA VAL A 135 1736 -87 -10 1816 1933 -94 C ATOM 1030 C VAL A 135 -9.260 -10.934 0.228 1.00 14.29 C ANISOU 1030 C VAL A 135 1661 -119 34 1751 2016 2 C ATOM 1031 O VAL A 135 -9.149 -10.381 -0.872 1.00 14.74 O ANISOU 1031 O VAL A 135 1912 -106 -7 1758 1929 -60 O ATOM 1032 CB VAL A 135 -11.238 -10.551 1.718 1.00 16.66 C ANISOU 1032 CB VAL A 135 2113 -196 -70 1942 2272 60 C ATOM 1033 CG1 VAL A 135 -11.710 -9.843 2.945 1.00 18.79 C ANISOU 1033 CG1 VAL A 135 2257 -183 -110 2347 2533 373 C ATOM 1034 CG2 VAL A 135 -12.114 -10.291 0.528 1.00 18.00 C ANISOU 1034 CG2 VAL A 135 1971 -3 -224 2194 2672 26 C ATOM 1035 N ARG A 136 -8.955 -12.214 0.410 1.00 15.82 N ANISOU 1035 N ARG A 136 1960 -172 -56 1847 2203 32 N ATOM 1036 CA ARG A 136 -8.523 -13.028 -0.727 1.00 17.62 C ANISOU 1036 CA ARG A 136 2274 -24 -44 2089 2331 155 C ATOM 1037 C ARG A 136 -9.689 -13.320 -1.648 1.00 19.70 C ANISOU 1037 C ARG A 136 2507 -462 -221 2287 2688 166 C ATOM 1038 O ARG A 136 -10.842 -13.589 -1.222 1.00 21.72 O ANISOU 1038 O ARG A 136 2624 -647 -317 2902 2726 171 O ATOM 1039 CB ARG A 136 -7.987 -14.356 -0.341 1.00 18.33 C ANISOU 1039 CB ARG A 136 2231 25 35 2202 2531 36 C ATOM 1040 CG ARG A 136 -6.630 -14.258 0.183 1.00 19.54 C ANISOU 1040 CG ARG A 136 2461 -356 226 2234 2728 -367 C ATOM 1041 CD ARG A 136 -6.040 -15.631 0.338 1.00 21.14 C ANISOU 1041 CD ARG A 136 2738 -155 -95 2285 3006 -135 C ATOM 1042 NE ARG A 136 -4.686 -15.615 0.791 1.00 21.62 N ANISOU 1042 NE ARG A 136 3016 -192 -111 2074 3121 -382 N ATOM 1043 CZ ARG A 136 -4.248 -15.761 2.030 1.00 20.97 C ANISOU 1043 CZ ARG A 136 2726 -119 216 2170 3071 -156 C ATOM 1044 NH1 ARG A 136 -5.037 -15.863 3.079 1.00 24.69 N ANISOU 1044 NH1 ARG A 136 3392 -537 -14 2796 3192 -118 N ATOM 1045 NH2 ARG A 136 -2.948 -15.680 2.175 1.00 23.08 N ANISOU 1045 NH2 ARG A 136 2613 -130 783 2650 3506 -304 N ATOM 1046 N GLU A 137 -9.384 -13.310 -2.920 1.00 19.67 N ANISOU 1046 N GLU A 137 2429 -357 -237 2422 2620 131 N ATOM 1047 CA GLU A 137 -10.245 -13.938 -3.920 1.00 22.65 C ANISOU 1047 CA GLU A 137 2720 -211 -286 2779 3105 56 C ATOM 1048 C GLU A 137 -10.010 -15.472 -3.924 1.00 23.06 C ANISOU 1048 C GLU A 137 2716 -284 -328 2697 3348 -43 C ATOM 1049 O GLU A 137 -8.840 -15.960 -3.984 1.00 23.68 O ANISOU 1049 O GLU A 137 2920 -233 -583 2412 3664 -176 O ATOM 1050 CB AGLU A 137 -9.925 -13.324 -5.286 0.50 22.70 C ANISOU 1050 CB AGLU A 137 2743 -121 -201 2802 3079 -46 C ATOM 1051 CG AGLU A 137 -10.656 -13.901 -6.456 0.50 23.72 C ANISOU 1051 CG AGLU A 137 2910 -134 -178 2952 3150 -37 C ATOM 1052 CD AGLU A 137 -10.055 -13.479 -7.785 0.50 24.95 C ANISOU 1052 CD AGLU A 137 3067 -84 -56 3201 3210 -25 C ATOM 1053 OE1AGLU A 137 -8.827 -13.666 -8.044 0.50 25.44 O ANISOU 1053 OE1AGLU A 137 3153 15 131 3262 3249 -313 O ATOM 1054 OE2AGLU A 137 -10.844 -12.958 -8.603 0.50 30.12 O ANISOU 1054 OE2AGLU A 137 3579 295 320 3838 4025 -93 O ATOM 1055 OXT GLU A 137 -10.975 -16.242 -3.933 1.00 25.27 O ANISOU 1055 OXT GLU A 137 2982 -237 -361 2773 3847 69 O TER 1056 GLU A 137 ATOM 1268 N PRO A 1 -15.721 27.462 34.955 1.00 27.08 N ANISOU 1268 N PRO B 1 3774 32 16 3446 3066 375 N ATOM 1269 CA PRO A 1 -14.604 27.207 34.038 1.00 24.49 C ANISOU 1269 CA PRO B 1 3408 -44 35 3102 2794 315 C ATOM 1270 C PRO A 1 -14.935 27.671 32.642 1.00 23.69 C ANISOU 1270 C PRO B 1 3186 -80 77 3017 2798 291 C ATOM 1271 O PRO A 1 -16.103 27.759 32.288 1.00 25.39 O ANISOU 1271 O PRO B 1 3274 -112 211 3587 2783 368 O ATOM 1272 CB PRO A 1 -14.436 25.686 34.091 1.00 25.19 C ANISOU 1272 CB PRO B 1 3502 -73 16 3160 2906 239 C ATOM 1273 CG PRO A 1 -15.683 25.173 34.776 1.00 25.46 C ANISOU 1273 CG PRO B 1 3627 -121 100 3176 2869 362 C ATOM 1274 CD PRO A 1 -16.184 26.243 35.617 1.00 27.97 C ANISOU 1274 CD PRO B 1 3789 55 43 3517 3318 341 C ATOM 1275 N ASN A 2 -13.895 27.933 31.849 1.00 21.61 N ANISOU 1275 N ASN B 2 3118 -5 -137 2683 2407 476 N ATOM 1276 CA ASN A 2 -14.037 28.373 30.472 1.00 21.29 C ANISOU 1276 CA ASN B 2 3088 -86 -214 2458 2539 339 C ATOM 1277 C ASN A 2 -13.424 27.347 29.485 1.00 19.21 C ANISOU 1277 C ASN B 2 2701 -107 -242 2216 2379 420 C ATOM 1278 O ASN A 2 -12.192 27.300 29.320 1.00 20.58 O ANISOU 1278 O ASN B 2 2872 -334 -333 2329 2616 316 O ATOM 1279 CB ASN A 2 -13.345 29.693 30.292 1.00 21.66 C ANISOU 1279 CB ASN B 2 3396 -188 -253 2446 2385 369 C ATOM 1280 CG ASN A 2 -13.260 30.069 28.872 1.00 23.19 C ANISOU 1280 CG ASN B 2 3708 -386 -233 2794 2306 338 C ATOM 1281 OD1 ASN A 2 -14.193 29.781 28.135 1.00 24.05 O ANISOU 1281 OD1 ASN B 2 3638 -206 128 2746 2752 345 O ATOM 1282 ND2 ASN A 2 -12.153 30.725 28.455 1.00 26.80 N ANISOU 1282 ND2 ASN B 2 4524 -725 -271 2748 2909 293 N ATOM 1283 N PHE A 3 -14.272 26.520 28.876 1.00 17.87 N ANISOU 1283 N PHE B 3 2335 -95 -232 2075 2376 407 N ATOM 1284 CA PHE A 3 -13.803 25.489 27.941 1.00 17.26 C ANISOU 1284 CA PHE B 3 2276 66 -162 1960 2322 266 C ATOM 1285 C PHE A 3 -13.790 25.965 26.505 1.00 16.88 C ANISOU 1285 C PHE B 3 2187 27 -145 1846 2377 327 C ATOM 1286 O PHE A 3 -13.349 25.232 25.600 1.00 17.38 O ANISOU 1286 O PHE B 3 2235 156 -174 1939 2426 289 O ATOM 1287 CB PHE A 3 -14.703 24.245 28.036 1.00 17.02 C ANISOU 1287 CB PHE B 3 2099 -21 -122 2077 2290 93 C ATOM 1288 CG PHE A 3 -14.551 23.478 29.312 1.00 17.24 C ANISOU 1288 CG PHE B 3 2180 54 -26 2008 2362 38 C ATOM 1289 CD1 PHE A 3 -15.307 23.764 30.437 1.00 19.14 C ANISOU 1289 CD1 PHE B 3 2828 141 98 2205 2237 -39 C ATOM 1290 CD2 PHE A 3 -13.685 22.404 29.381 1.00 18.04 C ANISOU 1290 CD2 PHE B 3 2294 -158 3 1820 2741 10 C ATOM 1291 CE1 PHE A 3 -15.158 23.031 31.589 1.00 21.48 C ANISOU 1291 CE1 PHE B 3 3077 271 103 2561 2521 172 C ATOM 1292 CE2 PHE A 3 -13.553 21.691 30.514 1.00 18.25 C ANISOU 1292 CE2 PHE B 3 2270 9 58 1881 2783 -122 C ATOM 1293 CZ PHE A 3 -14.273 21.982 31.597 1.00 19.85 C ANISOU 1293 CZ PHE B 3 2920 97 147 2068 2554 -180 C ATOM 1294 N SER A 4 -14.253 27.183 26.235 1.00 18.24 N ANISOU 1294 N SER B 4 2495 184 32 2015 2420 435 N ATOM 1295 CA SER A 4 -14.352 27.619 24.855 1.00 18.88 C ANISOU 1295 CA SER B 4 2572 208 47 2067 2534 543 C ATOM 1296 C SER A 4 -12.995 27.654 24.166 1.00 18.70 C ANISOU 1296 C SER B 4 2468 134 -124 1983 2652 495 C ATOM 1297 O SER A 4 -11.977 28.050 24.757 1.00 20.40 O ANISOU 1297 O SER B 4 2652 -42 -300 2334 2762 720 O ATOM 1298 CB SER A 4 -14.948 29.015 24.749 1.00 20.69 C ANISOU 1298 CB SER B 4 2925 431 152 2099 2835 646 C ATOM 1299 OG SER A 4 -16.289 29.030 25.239 1.00 23.85 O ANISOU 1299 OG SER B 4 3037 778 666 2866 3157 1158 O ATOM 1300 N GLY A 5 -12.949 27.203 22.917 1.00 18.37 N ANISOU 1300 N GLY B 5 2488 -46 -1 1945 2544 514 N ATOM 1301 CA GLY A 5 -11.672 27.087 22.210 1.00 18.84 C ANISOU 1301 CA GLY B 5 2438 31 -56 1955 2763 433 C ATOM 1302 C GLY A 5 -11.788 26.234 20.977 1.00 17.58 C ANISOU 1302 C GLY B 5 2360 95 4 1829 2489 423 C ATOM 1303 O GLY A 5 -12.747 25.502 20.791 1.00 18.34 O ANISOU 1303 O GLY B 5 2235 133 -95 2141 2591 372 O ATOM 1304 N ASN A 6 -10.774 26.344 20.130 1.00 18.12 N ANISOU 1304 N ASN B 6 2482 93 87 1796 2606 491 N ATOM 1305 CA ASN A 6 -10.596 25.460 18.980 1.00 18.39 C ANISOU 1305 CA ASN B 6 2384 51 197 2239 2364 325 C ATOM 1306 C ASN A 6 -9.370 24.634 19.297 1.00 17.25 C ANISOU 1306 C ASN B 6 2187 107 -61 2011 2354 394 C ATOM 1307 O ASN A 6 -8.264 25.088 19.143 1.00 18.43 O ANISOU 1307 O ASN B 6 2333 47 141 2016 2651 423 O ATOM 1308 CB ASN A 6 -10.412 26.281 17.711 1.00 19.50 C ANISOU 1308 CB ASN B 6 2529 182 310 2372 2505 479 C ATOM 1309 CG ASN A 6 -11.600 27.143 17.451 1.00 23.34 C ANISOU 1309 CG ASN B 6 3252 100 268 2943 2670 210 C ATOM 1310 OD1 ASN A 6 -12.452 26.739 16.690 1.00 29.43 O ANISOU 1310 OD1 ASN B 6 3511 115 539 3746 3925 -401 O ATOM 1311 ND2 ASN A 6 -11.680 28.305 18.094 1.00 28.36 N ANISOU 1311 ND2 ASN B 6 4190 214 329 3497 3089 660 N ATOM 1312 N TRP A 7 -9.596 23.456 19.860 1.00 16.72 N ANISOU 1312 N TRP B 7 2067 63 75 1916 2368 140 N ATOM 1313 CA TRP A 7 -8.567 22.696 20.523 1.00 16.45 C ANISOU 1313 CA TRP B 7 1992 81 -94 2006 2250 125 C ATOM 1314 C TRP A 7 -7.936 21.697 19.568 1.00 16.30 C ANISOU 1314 C TRP B 7 2089 -56 36 1890 2215 124 C ATOM 1315 O TRP A 7 -8.640 20.952 18.913 1.00 18.93 O ANISOU 1315 O TRP B 7 2290 113 -490 2225 2674 41 O ATOM 1316 CB TRP A 7 -9.201 21.977 21.691 1.00 16.28 C ANISOU 1316 CB TRP B 7 2007 48 -17 1878 2301 9 C ATOM 1317 CG TRP A 7 -9.749 22.863 22.783 1.00 15.57 C ANISOU 1317 CG TRP B 7 1958 158 79 1694 2261 137 C ATOM 1318 CD1 TRP A 7 -11.052 23.300 22.927 1.00 16.55 C ANISOU 1318 CD1 TRP B 7 1959 -10 44 1934 2394 176 C ATOM 1319 CD2 TRP A 7 -9.038 23.414 23.877 1.00 14.85 C ANISOU 1319 CD2 TRP B 7 2101 44 65 1557 1982 241 C ATOM 1320 NE1 TRP A 7 -11.175 24.094 24.055 1.00 17.02 N ANISOU 1320 NE1 TRP B 7 2268 84 -147 1829 2367 252 N ATOM 1321 CE2 TRP A 7 -9.960 24.166 24.665 1.00 15.71 C ANISOU 1321 CE2 TRP B 7 2062 -89 92 1763 2144 246 C ATOM 1322 CE3 TRP A 7 -7.727 23.340 24.302 1.00 15.23 C ANISOU 1322 CE3 TRP B 7 2180 114 258 1760 1845 269 C ATOM 1323 CZ2 TRP A 7 -9.585 24.812 25.802 1.00 16.77 C ANISOU 1323 CZ2 TRP B 7 2466 121 44 1650 2254 252 C ATOM 1324 CZ3 TRP A 7 -7.371 23.988 25.465 1.00 17.07 C ANISOU 1324 CZ3 TRP B 7 2185 -23 57 2062 2238 243 C ATOM 1325 CH2 TRP A 7 -8.297 24.717 26.195 1.00 16.98 C ANISOU 1325 CH2 TRP B 7 2528 -69 78 1837 2088 293 C ATOM 1326 N LYS A 8 -6.607 21.701 19.506 1.00 15.13 N ANISOU 1326 N LYS B 8 1965 132 -3 1803 1980 134 N ATOM 1327 CA LYS A 8 -5.872 20.785 18.622 1.00 16.75 C ANISOU 1327 CA LYS B 8 2329 169 109 2122 1912 196 C ATOM 1328 C LYS A 8 -5.059 19.826 19.463 1.00 15.73 C ANISOU 1328 C LYS B 8 2284 228 74 2030 1663 126 C ATOM 1329 O LYS A 8 -4.551 20.169 20.513 1.00 16.31 O ANISOU 1329 O LYS B 8 2451 161 184 1970 1774 174 O ATOM 1330 CB LYS A 8 -5.002 21.483 17.613 1.00 18.86 C ANISOU 1330 CB LYS B 8 2616 273 225 2586 1961 352 C ATOM 1331 CG LYS A 8 -4.022 22.373 18.163 1.00 20.93 C ANISOU 1331 CG LYS B 8 2767 123 327 2746 2438 196 C ATOM 1332 CD LYS A 8 -3.019 22.909 17.069 1.00 22.31 C ANISOU 1332 CD LYS B 8 3112 -21 323 2913 2449 259 C ATOM 1333 CE LYS A 8 -2.011 23.793 17.735 1.00 24.50 C ANISOU 1333 CE LYS B 8 2943 -221 519 3525 2840 387 C ATOM 1334 NZ LYS A 8 -0.941 24.328 16.805 1.00 27.79 N ANISOU 1334 NZ LYS B 8 3204 -412 626 4081 3274 462 N ATOM 1335 N ILE A 9 -4.952 18.596 18.994 1.00 15.98 N ANISOU 1335 N ILE B 9 2385 149 119 2001 1685 8 N ATOM 1336 CA ILE A 9 -4.347 17.545 19.800 1.00 15.92 C ANISOU 1336 CA ILE B 9 2273 188 108 2047 1728 142 C ATOM 1337 C ILE A 9 -2.843 17.669 19.828 1.00 16.69 C ANISOU 1337 C ILE B 9 2238 224 210 2237 1865 252 C ATOM 1338 O ILE A 9 -2.206 17.940 18.813 1.00 18.76 O ANISOU 1338 O ILE B 9 2559 391 366 2637 1932 434 O ATOM 1339 CB ILE A 9 -4.835 16.142 19.347 1.00 16.96 C ANISOU 1339 CB ILE B 9 2462 259 60 2088 1892 102 C ATOM 1340 CG1 ILE A 9 -4.682 15.118 20.473 1.00 17.61 C ANISOU 1340 CG1 ILE B 9 2662 149 101 1924 2105 -153 C ATOM 1341 CG2 ILE A 9 -4.126 15.695 18.093 1.00 19.62 C ANISOU 1341 CG2 ILE B 9 2857 250 -21 2417 2181 107 C ATOM 1342 CD1 ILE A 9 -5.483 13.832 20.270 1.00 18.28 C ANISOU 1342 CD1 ILE B 9 2679 227 120 2143 2120 145 C ATOM 1343 N ILE A 10 -2.263 17.392 20.983 1.00 15.82 N ANISOU 1343 N ILE B 10 1997 223 228 2089 1922 174 N ATOM 1344 CA ILE A 10 -0.828 17.283 21.133 1.00 17.15 C ANISOU 1344 CA ILE B 10 2081 150 211 2194 2241 216 C ATOM 1345 C ILE A 10 -0.346 15.915 21.589 1.00 17.12 C ANISOU 1345 C ILE B 10 2109 180 185 2072 2324 246 C ATOM 1346 O ILE A 10 0.770 15.565 21.286 1.00 20.01 O ANISOU 1346 O ILE B 10 2088 317 299 2492 3022 326 O ATOM 1347 CB ILE A 10 -0.254 18.402 21.965 1.00 18.85 C ANISOU 1347 CB ILE B 10 2094 194 99 2516 2551 153 C ATOM 1348 CG1 ILE A 10 -0.686 18.342 23.418 1.00 19.67 C ANISOU 1348 CG1 ILE B 10 2285 -54 -124 2677 2511 -67 C ATOM 1349 CG2 ILE A 10 -0.538 19.756 21.338 1.00 21.38 C ANISOU 1349 CG2 ILE B 10 2751 167 19 2499 2873 -5 C ATOM 1350 CD1 ILE A 10 0.094 19.274 24.342 1.00 21.39 C ANISOU 1350 CD1 ILE B 10 2577 -53 -31 2747 2803 -91 C ATOM 1351 N ARG A 11 -1.155 15.124 22.263 1.00 16.42 N ANISOU 1351 N ARG B 11 2093 207 211 1981 2163 170 N ATOM 1352 CA ARG A 11 -0.778 13.781 22.711 1.00 18.13 C ANISOU 1352 CA ARG B 11 2176 230 201 2185 2528 35 C ATOM 1353 C ARG A 11 -2.004 12.926 22.849 1.00 16.38 C ANISOU 1353 C ARG B 11 2221 236 255 1967 2032 220 C ATOM 1354 O ARG A 11 -3.053 13.438 23.197 1.00 16.78 O ANISOU 1354 O ARG B 11 2157 366 179 2164 2056 361 O ATOM 1355 CB ARG A 11 -0.145 13.857 24.121 1.00 21.65 C ANISOU 1355 CB ARG B 11 2769 234 390 2300 3154 -198 C ATOM 1356 CG ARG A 11 1.121 14.470 24.227 1.00 27.17 C ANISOU 1356 CG ARG B 11 3580 52 134 3250 3491 -112 C ATOM 1357 CD ARG A 11 1.785 13.907 25.479 1.00 26.52 C ANISOU 1357 CD ARG B 11 3059 164 68 3593 3424 -358 C ATOM 1358 NE ARG A 11 1.162 14.131 26.791 1.00 28.35 N ANISOU 1358 NE ARG B 11 2896 208 -18 3953 3920 -375 N ATOM 1359 CZ ARG A 11 1.034 15.318 27.400 1.00 26.06 C ANISOU 1359 CZ ARG B 11 2423 132 -56 3886 3591 -227 C ATOM 1360 NH1 ARG A 11 1.321 16.432 26.772 1.00 25.78 N ANISOU 1360 NH1 ARG B 11 2832 342 47 3553 3407 -349 N ATOM 1361 NH2 ARG A 11 0.571 15.403 28.625 1.00 28.31 N ANISOU 1361 NH2 ARG B 11 3097 -143 157 4049 3609 -217 N ATOM 1362 N SER A 12 -1.857 11.631 22.634 1.00 17.42 N ANISOU 1362 N SER B 12 2207 311 154 2040 2369 341 N ATOM 1363 CA SER A 12 -2.958 10.664 22.772 1.00 18.66 C ANISOU 1363 CA SER B 12 2425 282 4 2067 2595 344 C ATOM 1364 C SER A 12 -2.359 9.361 23.276 1.00 17.85 C ANISOU 1364 C SER B 12 2287 277 47 1953 2539 405 C ATOM 1365 O SER A 12 -1.290 8.977 22.820 1.00 20.74 O ANISOU 1365 O SER B 12 2431 434 251 2262 3187 675 O ATOM 1366 CB SER A 12 -3.586 10.405 21.374 1.00 21.43 C ANISOU 1366 CB SER B 12 2526 51 126 2690 2926 78 C ATOM 1367 OG SER A 12 -4.640 9.470 21.392 1.00 25.12 O ANISOU 1367 OG SER B 12 3302 57 9 2998 3245 -14 O ATOM 1368 N GLU A 13 -3.054 8.683 24.163 1.00 16.65 N ANISOU 1368 N GLU B 13 2266 308 -6 1805 2252 301 N ATOM 1369 CA GLU A 13 -2.654 7.341 24.574 1.00 18.36 C ANISOU 1369 CA GLU B 13 2349 183 11 2090 2533 139 C ATOM 1370 C GLU A 13 -3.855 6.458 24.768 1.00 17.06 C ANISOU 1370 C GLU B 13 2231 233 33 1871 2378 124 C ATOM 1371 O GLU A 13 -4.903 6.897 25.241 1.00 16.61 O ANISOU 1371 O GLU B 13 2156 216 -60 1929 2224 136 O ATOM 1372 CB GLU A 13 -1.782 7.383 25.784 1.00 22.26 C ANISOU 1372 CB GLU B 13 2822 -40 229 2642 2993 -32 C ATOM 1373 CG GLU A 13 -2.387 7.630 27.055 1.00 23.58 C ANISOU 1373 CG GLU B 13 2813 140 -154 2900 3244 -94 C ATOM 1374 CD GLU A 13 -1.426 7.423 28.275 1.00 24.98 C ANISOU 1374 CD GLU B 13 3010 14 -34 3358 3121 -57 C ATOM 1375 OE1 GLU A 13 -0.181 7.405 28.153 1.00 29.01 O ANISOU 1375 OE1 GLU B 13 3144 -308 -349 4339 3538 15 O ATOM 1376 OE2 GLU A 13 -1.959 7.299 29.386 1.00 27.21 O ANISOU 1376 OE2 GLU B 13 3220 -274 146 4107 3012 -75 O ATOM 1377 N ASN A 14 -3.689 5.181 24.423 1.00 16.88 N ANISOU 1377 N ASN B 14 2240 341 -54 1837 2333 239 N ATOM 1378 CA ASN A 14 -4.644 4.117 24.678 1.00 16.96 C ANISOU 1378 CA ASN B 14 2445 278 -106 1776 2220 191 C ATOM 1379 C ASN A 14 -5.934 4.163 23.898 1.00 16.64 C ANISOU 1379 C ASN B 14 2445 161 -73 1796 2081 131 C ATOM 1380 O ASN A 14 -6.890 3.486 24.259 1.00 17.58 O ANISOU 1380 O ASN B 14 2510 68 -20 2058 2112 221 O ATOM 1381 CB ASN A 14 -4.973 3.951 26.166 1.00 17.60 C ANISOU 1381 CB ASN B 14 2625 269 73 1868 2191 95 C ATOM 1382 CG ASN A 14 -3.852 3.372 26.961 1.00 21.52 C ANISOU 1382 CG ASN B 14 3100 486 66 2594 2482 273 C ATOM 1383 OD1 ASN A 14 -2.934 2.743 26.417 1.00 24.55 O ANISOU 1383 OD1 ASN B 14 3486 1086 135 3064 2776 6 O ATOM 1384 ND2 ASN A 14 -3.946 3.512 28.264 1.00 23.58 N ANISOU 1384 ND2 ASN B 14 3308 655 -27 3182 2467 -347 N ATOM 1385 N PHE A 15 -5.993 4.910 22.799 1.00 16.68 N ANISOU 1385 N PHE B 15 2523 112 -64 1759 2054 155 N ATOM 1386 CA PHE A 15 -7.203 4.888 22.010 1.00 17.20 C ANISOU 1386 CA PHE B 15 2536 197 -80 1928 2071 114 C ATOM 1387 C PHE A 15 -7.489 3.481 21.458 1.00 16.86 C ANISOU 1387 C PHE B 15 2529 61 -61 1912 1962 193 C ATOM 1388 O PHE A 15 -8.596 2.957 21.616 1.00 16.81 O ANISOU 1388 O PHE B 15 2425 146 -129 2003 1957 183 O ATOM 1389 CB PHE A 15 -7.133 5.909 20.913 1.00 19.01 C ANISOU 1389 CB PHE B 15 2849 161 -21 1991 2381 103 C ATOM 1390 CG PHE A 15 -8.296 5.890 19.982 1.00 19.59 C ANISOU 1390 CG PHE B 15 2859 219 22 2253 2329 87 C ATOM 1391 CD1 PHE A 15 -9.547 6.248 20.431 1.00 22.78 C ANISOU 1391 CD1 PHE B 15 3149 202 270 2798 2705 -118 C ATOM 1392 CD2 PHE A 15 -8.133 5.516 18.634 1.00 21.90 C ANISOU 1392 CD2 PHE B 15 2965 23 345 2750 2606 32 C ATOM 1393 CE1 PHE A 15 -10.650 6.229 19.581 1.00 24.26 C ANISOU 1393 CE1 PHE B 15 2989 207 97 3168 3059 3 C ATOM 1394 CE2 PHE A 15 -9.246 5.521 17.766 1.00 23.09 C ANISOU 1394 CE2 PHE B 15 3260 -4 136 3098 2413 -21 C ATOM 1395 CZ PHE A 15 -10.492 5.885 18.256 1.00 22.90 C ANISOU 1395 CZ PHE B 15 3190 225 168 2711 2798 -149 C ATOM 1396 N GLU A 16 -6.520 2.873 20.770 1.00 16.80 N ANISOU 1396 N GLU B 16 2470 108 4 1919 1992 292 N ATOM 1397 CA GLU A 16 -6.760 1.555 20.238 1.00 16.71 C ANISOU 1397 CA GLU B 16 2399 74 -3 1947 2001 188 C ATOM 1398 C GLU A 16 -6.994 0.532 21.350 1.00 17.03 C ANISOU 1398 C GLU B 16 2407 1 -38 2128 1935 313 C ATOM 1399 O GLU A 16 -7.811 -0.381 21.187 1.00 17.21 O ANISOU 1399 O GLU B 16 2685 -78 -52 2026 1825 329 O ATOM 1400 CB BGLU A 16 -5.626 1.075 19.308 0.70 17.00 C ANISOU 1400 CB BGLU B 16 2443 72 51 2125 1890 345 C ATOM 1401 CG BGLU A 16 -5.542 1.856 18.018 0.70 17.81 C ANISOU 1401 CG BGLU B 16 2642 153 111 2164 1960 207 C ATOM 1402 CD BGLU A 16 -4.330 1.547 17.200 0.70 17.53 C ANISOU 1402 CD BGLU B 16 2520 -34 -93 2205 1934 101 C ATOM 1403 OE1BGLU A 16 -3.323 2.297 17.304 0.70 21.97 O ANISOU 1403 OE1BGLU B 16 2857 -262 -359 2610 2878 293 O ATOM 1404 OE2BGLU A 16 -4.386 0.525 16.494 0.70 17.72 O ANISOU 1404 OE2BGLU B 16 2649 22 -74 2111 1972 149 O ATOM 1405 N GLU A 17 -6.264 0.666 22.456 1.00 17.38 N ANISOU 1405 N GLU B 17 2587 165 -17 1906 2109 234 N ATOM 1406 CA GLU A 17 -6.458 -0.249 23.588 1.00 17.58 C ANISOU 1406 CA GLU B 17 2607 96 75 1986 2084 184 C ATOM 1407 C GLU A 17 -7.860 -0.219 24.117 1.00 18.15 C ANISOU 1407 C GLU B 17 2833 121 -56 2007 2054 167 C ATOM 1408 O GLU A 17 -8.421 -1.254 24.501 1.00 18.82 O ANISOU 1408 O GLU B 17 2871 30 72 2066 2212 318 O ATOM 1409 CB GLU A 17 -5.454 0.041 24.703 1.00 19.71 C ANISOU 1409 CB GLU B 17 2713 180 -17 2341 2435 177 C ATOM 1410 CG GLU A 17 -5.382 -1.051 25.757 1.00 23.10 C ANISOU 1410 CG GLU B 17 3335 91 124 2615 2827 85 C ATOM 1411 CD GLU A 17 -4.909 -2.398 25.253 1.00 27.45 C ANISOU 1411 CD GLU B 17 3845 215 151 3040 3542 64 C ATOM 1412 OE1 GLU A 17 -4.184 -2.461 24.244 1.00 30.61 O ANISOU 1412 OE1 GLU B 17 3992 520 76 3503 4135 230 O ATOM 1413 OE2 GLU A 17 -5.254 -3.385 25.916 1.00 34.84 O ANISOU 1413 OE2 GLU B 17 4826 -144 142 3623 4787 171 O ATOM 1414 N LEU A 18 -8.427 0.985 24.211 1.00 16.89 N ANISOU 1414 N LEU B 18 2610 80 111 1940 1868 302 N ATOM 1415 CA LEU A 18 -9.784 1.136 24.691 1.00 17.40 C ANISOU 1415 CA LEU B 18 2528 42 -2 2148 1933 263 C ATOM 1416 C LEU A 18 -10.751 0.422 23.749 1.00 16.64 C ANISOU 1416 C LEU B 18 2433 48 68 2080 1806 316 C ATOM 1417 O LEU A 18 -11.625 -0.329 24.178 1.00 17.83 O ANISOU 1417 O LEU B 18 2819 -74 49 2169 1786 385 O ATOM 1418 CB LEU A 18 -10.078 2.607 24.843 1.00 17.38 C ANISOU 1418 CB LEU B 18 2317 134 -26 2207 2080 253 C ATOM 1419 CG LEU A 18 -11.516 2.898 25.270 1.00 19.22 C ANISOU 1419 CG LEU B 18 2543 52 -109 2491 2266 261 C ATOM 1420 CD1 LEU A 18 -11.867 2.270 26.627 1.00 21.78 C ANISOU 1420 CD1 LEU B 18 2808 -75 -286 2914 2553 544 C ATOM 1421 CD2 LEU A 18 -11.662 4.411 25.351 1.00 20.51 C ANISOU 1421 CD2 LEU B 18 2411 167 -229 2598 2781 252 C ATOM 1422 N LEU A 19 -10.604 0.634 22.446 1.00 16.22 N ANISOU 1422 N LEU B 19 2554 84 80 1847 1761 406 N ATOM 1423 CA LEU A 19 -11.439 -0.072 21.493 1.00 16.03 C ANISOU 1423 CA LEU B 19 2469 65 62 1804 1816 333 C ATOM 1424 C LEU A 19 -11.272 -1.592 21.607 1.00 15.92 C ANISOU 1424 C LEU B 19 2399 59 143 1975 1674 357 C ATOM 1425 O LEU A 19 -12.230 -2.340 21.490 1.00 16.94 O ANISOU 1425 O LEU B 19 2523 -12 113 1946 1965 355 O ATOM 1426 CB LEU A 19 -11.125 0.379 20.055 1.00 15.67 C ANISOU 1426 CB LEU B 19 2503 96 21 1742 1709 287 C ATOM 1427 CG LEU A 19 -11.443 1.827 19.731 1.00 16.55 C ANISOU 1427 CG LEU B 19 2587 201 22 1783 1917 232 C ATOM 1428 CD1 LEU A 19 -11.142 2.075 18.265 1.00 19.41 C ANISOU 1428 CD1 LEU B 19 3151 169 271 2131 2090 103 C ATOM 1429 CD2 LEU A 19 -12.885 2.143 20.027 1.00 19.86 C ANISOU 1429 CD2 LEU B 19 2948 88 142 2121 2474 211 C ATOM 1430 N LYS A 20 -10.056 -2.038 21.816 1.00 16.22 N ANISOU 1430 N LYS B 20 2621 67 107 1701 1839 280 N ATOM 1431 CA LYS A 20 -9.768 -3.466 21.910 1.00 16.98 C ANISOU 1431 CA LYS B 20 2805 53 83 1751 1894 326 C ATOM 1432 C LYS A 20 -10.476 -4.097 23.097 1.00 18.03 C ANISOU 1432 C LYS B 20 2864 37 133 1857 2128 356 C ATOM 1433 O LYS A 20 -11.049 -5.156 22.986 1.00 18.75 O ANISOU 1433 O LYS B 20 3117 46 88 1776 2230 398 O ATOM 1434 CB LYS A 20 -8.271 -3.648 22.014 1.00 16.92 C ANISOU 1434 CB LYS B 20 2800 -22 103 1701 1926 264 C ATOM 1435 CG LYS A 20 -7.788 -5.096 22.057 1.00 17.84 C ANISOU 1435 CG LYS B 20 2843 -23 28 1809 2122 210 C ATOM 1436 CD LYS A 20 -6.256 -5.187 22.032 1.00 20.20 C ANISOU 1436 CD LYS B 20 2960 89 -6 2081 2631 231 C ATOM 1437 CE LYS A 20 -5.735 -6.608 22.128 1.00 23.05 C ANISOU 1437 CE LYS B 20 3306 104 -88 2305 3143 163 C ATOM 1438 NZ LYS A 20 -4.240 -6.545 22.199 1.00 24.51 N ANISOU 1438 NZ LYS B 20 3135 243 89 2634 3544 15 N ATOM 1439 N VAL A 21 -10.439 -3.471 24.259 1.00 19.13 N ANISOU 1439 N VAL B 21 3115 -74 236 2105 2048 430 N ATOM 1440 CA VAL A 21 -11.079 -4.082 25.443 1.00 19.88 C ANISOU 1440 CA VAL B 21 3237 17 312 2311 2004 369 C ATOM 1441 C VAL A 21 -12.589 -4.053 25.293 1.00 19.22 C ANISOU 1441 C VAL B 21 3148 -108 178 2209 1944 369 C ATOM 1442 O VAL A 21 -13.317 -4.852 25.921 1.00 22.12 O ANISOU 1442 O VAL B 21 3620 -130 451 2514 2269 531 O ATOM 1443 CB VAL A 21 -10.593 -3.436 26.754 1.00 22.74 C ANISOU 1443 CB VAL B 21 3288 -90 246 3062 2289 261 C ATOM 1444 CG1 VAL A 21 -11.182 -2.110 26.972 1.00 22.11 C ANISOU 1444 CG1 VAL B 21 3675 -294 354 2711 2013 248 C ATOM 1445 CG2 VAL A 21 -10.852 -4.252 27.968 0.50 21.32 C ANISOU 1445 CG2 VAL B 21 3261 -45 247 2543 2295 196 C ATOM 1446 N LEU A 22 -13.121 -3.125 24.496 1.00 18.60 N ANISOU 1446 N LEU B 22 2911 -31 189 2027 2127 545 N ATOM 1447 CA LEU A 22 -14.535 -3.098 24.186 1.00 19.19 C ANISOU 1447 CA LEU B 22 2890 -14 61 2285 2117 509 C ATOM 1448 C LEU A 22 -14.975 -4.147 23.197 1.00 19.90 C ANISOU 1448 C LEU B 22 2694 -95 -85 2319 2546 549 C ATOM 1449 O LEU A 22 -16.151 -4.325 22.963 1.00 21.94 O ANISOU 1449 O LEU B 22 2750 -60 -472 2551 3034 686 O ATOM 1450 CB LEU A 22 -14.964 -1.704 23.732 1.00 19.60 C ANISOU 1450 CB LEU B 22 2810 -23 -117 2279 2355 568 C ATOM 1451 CG LEU A 22 -14.969 -0.619 24.805 1.00 19.83 C ANISOU 1451 CG LEU B 22 2826 -27 -104 2336 2372 322 C ATOM 1452 CD1 LEU A 22 -14.981 0.755 24.218 1.00 20.91 C ANISOU 1452 CD1 LEU B 22 2882 152 -74 2493 2568 389 C ATOM 1453 CD2 LEU A 22 -16.108 -0.778 25.759 1.00 20.80 C ANISOU 1453 CD2 LEU B 22 2955 120 -148 2403 2544 580 C ATOM 1454 N GLY A 23 -14.036 -4.845 22.593 1.00 18.86 N ANISOU 1454 N GLY B 23 2699 -32 -69 2177 2289 598 N ATOM 1455 CA GLY A 23 -14.369 -5.915 21.683 1.00 19.24 C ANISOU 1455 CA GLY B 23 2846 -86 -36 2143 2318 526 C ATOM 1456 C GLY A 23 -14.329 -5.550 20.195 1.00 18.63 C ANISOU 1456 C GLY B 23 2759 -79 -175 2072 2247 662 C ATOM 1457 O GLY A 23 -14.741 -6.369 19.363 1.00 19.96 O ANISOU 1457 O GLY B 23 2972 -262 -226 2199 2411 785 O ATOM 1458 N VAL A 24 -13.846 -4.356 19.840 1.00 17.60 N ANISOU 1458 N VAL B 24 2611 -9 -92 1984 2091 541 N ATOM 1459 CA VAL A 24 -13.751 -3.962 18.439 1.00 16.60 C ANISOU 1459 CA VAL B 24 2237 96 -108 2037 2032 476 C ATOM 1460 C VAL A 24 -12.611 -4.739 17.772 1.00 15.99 C ANISOU 1460 C VAL B 24 2115 72 -126 2058 1900 446 C ATOM 1461 O VAL A 24 -11.484 -4.767 18.278 1.00 16.54 O ANISOU 1461 O VAL B 24 2122 164 -143 2086 2073 373 O ATOM 1462 CB VAL A 24 -13.506 -2.454 18.353 1.00 16.53 C ANISOU 1462 CB VAL B 24 2268 106 -166 2018 1993 496 C ATOM 1463 CG1 VAL A 24 -13.439 -2.003 16.887 1.00 17.58 C ANISOU 1463 CG1 VAL B 24 2266 107 -47 2240 2172 399 C ATOM 1464 CG2 VAL A 24 -14.600 -1.686 19.097 1.00 18.21 C ANISOU 1464 CG2 VAL B 24 2579 222 -94 2100 2238 359 C ATOM 1465 N ASN A 25 -12.888 -5.353 16.629 1.00 16.15 N ANISOU 1465 N ASN B 25 2153 -18 -40 2039 1944 359 N ATOM 1466 CA ASN A 25 -11.885 -6.191 15.967 1.00 15.67 C ANISOU 1466 CA ASN B 25 2234 -21 -122 1929 1790 360 C ATOM 1467 C ASN A 25 -10.796 -5.331 15.357 1.00 15.24 C ANISOU 1467 C ASN B 25 2174 38 0 1908 1708 307 C ATOM 1468 O ASN A 25 -10.939 -4.111 15.178 1.00 15.68 O ANISOU 1468 O ASN B 25 2271 77 0 1789 1895 402 O ATOM 1469 CB ASN A 25 -12.526 -7.184 14.981 1.00 16.93 C ANISOU 1469 CB ASN B 25 2187 -48 -93 2115 2128 418 C ATOM 1470 CG ASN A 25 -13.031 -6.539 13.746 1.00 17.41 C ANISOU 1470 CG ASN B 25 2151 -88 -114 2235 2227 265 C ATOM 1471 OD1 ASN A 25 -12.375 -5.706 13.111 1.00 18.03 O ANISOU 1471 OD1 ASN B 25 2235 -106 -57 2178 2435 280 O ATOM 1472 ND2 ASN A 25 -14.206 -6.986 13.317 1.00 20.85 N ANISOU 1472 ND2 ASN B 25 2521 -387 153 2962 2436 125 N ATOM 1473 N VAL A 26 -9.667 -5.972 15.045 1.00 14.88 N ANISOU 1473 N VAL B 26 2081 83 8 1797 1773 242 N ATOM 1474 CA VAL A 26 -8.509 -5.192 14.636 1.00 14.92 C ANISOU 1474 CA VAL B 26 2070 44 -64 1850 1747 218 C ATOM 1475 C VAL A 26 -8.716 -4.413 13.350 1.00 14.83 C ANISOU 1475 C VAL B 26 2002 -18 -28 1817 1816 282 C ATOM 1476 O VAL A 26 -8.230 -3.287 13.233 1.00 14.74 O ANISOU 1476 O VAL B 26 1980 8 48 1748 1869 156 O ATOM 1477 CB VAL A 26 -7.245 -6.059 14.638 1.00 15.96 C ANISOU 1477 CB VAL B 26 2162 109 172 1988 1914 213 C ATOM 1478 CG1 VAL A 26 -7.329 -7.175 13.579 1.00 15.76 C ANISOU 1478 CG1 VAL B 26 2163 332 137 1946 1876 284 C ATOM 1479 CG2 VAL A 26 -6.012 -5.239 14.438 1.00 17.11 C ANISOU 1479 CG2 VAL B 26 2161 205 90 2256 2085 93 C ATOM 1480 N MET A 27 -9.448 -4.971 12.396 1.00 14.60 N ANISOU 1480 N MET B 27 2122 -68 25 1720 1702 208 N ATOM 1481 CA MET A 27 -9.738 -4.230 11.174 1.00 15.31 C ANISOU 1481 CA MET B 27 2184 -71 5 1888 1742 210 C ATOM 1482 C MET A 27 -10.450 -2.945 11.471 1.00 15.02 C ANISOU 1482 C MET B 27 2077 26 60 1869 1759 210 C ATOM 1483 O MET A 27 -10.104 -1.871 10.985 1.00 15.98 O ANISOU 1483 O MET B 27 2171 11 5 1937 1961 278 O ATOM 1484 CB MET A 27 -10.588 -5.083 10.222 1.00 17.25 C ANISOU 1484 CB MET B 27 2502 -56 45 2183 1870 81 C ATOM 1485 CG MET A 27 -9.893 -6.335 9.714 1.00 18.48 C ANISOU 1485 CG MET B 27 2558 -317 -140 2424 2038 249 C ATOM 1486 SD MET A 27 -9.996 -7.772 10.850 0.50 18.16 S ANISOU 1486 SD MET B 27 2562 -195 -189 1995 2341 239 S ATOM 1487 CE MET A 27 -11.743 -8.078 10.661 0.50 19.40 C ANISOU 1487 CE MET B 27 2521 -192 -259 2392 2457 474 C ATOM 1488 N LEU A 28 -11.481 -3.029 12.300 1.00 15.54 N ANISOU 1488 N LEU B 28 2044 -20 133 2015 1845 231 N ATOM 1489 CA LEU A 28 -12.238 -1.850 12.653 1.00 16.00 C ANISOU 1489 CA LEU B 28 2014 64 208 2118 1944 198 C ATOM 1490 C LEU A 28 -11.445 -0.874 13.487 1.00 15.35 C ANISOU 1490 C LEU B 28 2045 86 186 1897 1890 311 C ATOM 1491 O LEU A 28 -11.654 0.331 13.354 1.00 15.86 O ANISOU 1491 O LEU B 28 2238 219 218 1853 1933 255 O ATOM 1492 CB LEU A 28 -13.537 -2.263 13.358 1.00 17.14 C ANISOU 1492 CB LEU B 28 2139 80 287 2236 2135 278 C ATOM 1493 CG LEU A 28 -14.543 -3.042 12.520 1.00 19.79 C ANISOU 1493 CG LEU B 28 2347 -147 403 2822 2349 248 C ATOM 1494 CD1 LEU A 28 -15.741 -3.412 13.380 1.00 22.91 C ANISOU 1494 CD1 LEU B 28 2766 -246 203 3215 2722 378 C ATOM 1495 CD2 LEU A 28 -15.002 -2.222 11.318 1.00 23.41 C ANISOU 1495 CD2 LEU B 28 2728 -155 574 3380 2784 -18 C ATOM 1496 N ARG A 29 -10.542 -1.341 14.345 1.00 15.28 N ANISOU 1496 N ARG B 29 2135 209 128 1800 1869 319 N ATOM 1497 CA ARG A 29 -9.708 -0.437 15.098 1.00 15.38 C ANISOU 1497 CA ARG B 29 2089 182 28 1894 1858 325 C ATOM 1498 C ARG A 29 -8.779 0.338 14.165 1.00 15.40 C ANISOU 1498 C ARG B 29 2225 97 -26 1883 1743 219 C ATOM 1499 O ARG A 29 -8.582 1.538 14.360 1.00 15.96 O ANISOU 1499 O ARG B 29 2363 121 -16 1749 1949 266 O ATOM 1500 CB ARG A 29 -8.871 -1.181 16.146 1.00 15.49 C ANISOU 1500 CB ARG B 29 2222 69 -4 1857 1805 239 C ATOM 1501 CG ARG A 29 -9.714 -1.875 17.212 1.00 15.86 C ANISOU 1501 CG ARG B 29 2328 205 47 1675 2019 321 C ATOM 1502 CD ARG A 29 -8.905 -2.288 18.429 1.00 16.07 C ANISOU 1502 CD ARG B 29 2334 125 -74 1879 1893 263 C ATOM 1503 NE ARG A 29 -7.701 -3.052 18.131 1.00 15.30 N ANISOU 1503 NE ARG B 29 2259 83 -147 1745 1808 139 N ATOM 1504 CZ ARG A 29 -7.577 -4.376 18.167 1.00 14.88 C ANISOU 1504 CZ ARG B 29 2129 56 0 1922 1602 157 C ATOM 1505 NH1 ARG A 29 -8.619 -5.177 18.307 1.00 15.35 N ANISOU 1505 NH1 ARG B 29 2273 193 76 1645 1914 381 N ATOM 1506 NH2 ARG A 29 -6.376 -4.882 18.044 1.00 16.57 N ANISOU 1506 NH2 ARG B 29 2180 66 94 1973 2141 324 N ATOM 1507 N LYS A 30 -8.207 -0.311 13.161 1.00 14.83 N ANISOU 1507 N LYS B 30 2115 142 33 1728 1791 235 N ATOM 1508 CA LYS A 30 -7.342 0.406 12.260 1.00 15.30 C ANISOU 1508 CA LYS B 30 2128 28 28 1775 1908 289 C ATOM 1509 C LYS A 30 -8.094 1.369 11.346 1.00 15.24 C ANISOU 1509 C LYS B 30 2025 59 87 1831 1933 267 C ATOM 1510 O LYS A 30 -7.578 2.457 11.028 1.00 15.38 O ANISOU 1510 O LYS B 30 2252 -57 152 1722 1869 250 O ATOM 1511 CB LYS A 30 -6.485 -0.548 11.433 1.00 15.15 C ANISOU 1511 CB LYS B 30 2068 24 -18 1894 1793 247 C ATOM 1512 CG LYS A 30 -5.600 -1.472 12.294 1.00 15.26 C ANISOU 1512 CG LYS B 30 2119 68 -94 1857 1820 286 C ATOM 1513 CD LYS A 30 -4.632 -0.737 13.183 1.00 16.32 C ANISOU 1513 CD LYS B 30 2112 158 -231 2190 1896 225 C ATOM 1514 CE LYS A 30 -3.827 -1.699 14.051 1.00 17.13 C ANISOU 1514 CE LYS B 30 2146 312 -270 2278 2083 95 C ATOM 1515 NZ LYS A 30 -2.780 -1.037 14.845 1.00 19.33 N ANISOU 1515 NZ LYS B 30 2426 162 -296 2622 2295 19 N ATOM 1516 N ILE A 31 -9.325 1.028 10.977 1.00 14.76 N ANISOU 1516 N ILE B 31 2001 55 119 1750 1855 224 N ATOM 1517 CA ILE A 31 -10.158 1.998 10.273 1.00 15.98 C ANISOU 1517 CA ILE B 31 2233 79 124 1859 1979 212 C ATOM 1518 C ILE A 31 -10.443 3.185 11.193 1.00 15.78 C ANISOU 1518 C ILE B 31 2224 122 182 1763 2007 137 C ATOM 1519 O ILE A 31 -10.409 4.324 10.737 1.00 16.57 O ANISOU 1519 O ILE B 31 2493 176 177 1739 2062 317 O ATOM 1520 CB ILE A 31 -11.453 1.304 9.797 1.00 15.95 C ANISOU 1520 CB ILE B 31 2160 72 196 1809 2091 105 C ATOM 1521 CG1 ILE A 31 -11.116 0.338 8.682 1.00 16.34 C ANISOU 1521 CG1 ILE B 31 2239 78 264 1946 2022 161 C ATOM 1522 CG2 ILE A 31 -12.524 2.284 9.368 1.00 16.74 C ANISOU 1522 CG2 ILE B 31 2142 8 207 2126 2091 134 C ATOM 1523 CD1 ILE A 31 -12.165 -0.609 8.333 1.00 20.10 C ANISOU 1523 CD1 ILE B 31 2509 49 32 2442 2685 156 C ATOM 1524 N ALA A 32 -10.732 2.939 12.482 1.00 15.82 N ANISOU 1524 N ALA B 32 2496 129 120 1679 1836 296 N ATOM 1525 CA ALA A 32 -10.963 4.029 13.412 1.00 17.30 C ANISOU 1525 CA ALA B 32 2527 134 70 2058 1987 283 C ATOM 1526 C ALA A 32 -9.761 4.939 13.543 1.00 17.40 C ANISOU 1526 C ALA B 32 2699 85 17 2012 1897 244 C ATOM 1527 O ALA A 32 -9.911 6.154 13.684 1.00 19.19 O ANISOU 1527 O ALA B 32 3079 242 -181 1787 2424 264 O ATOM 1528 CB ALA A 32 -11.413 3.503 14.791 1.00 17.69 C ANISOU 1528 CB ALA B 32 2665 115 5 1983 2074 408 C ATOM 1529 N VAL A 33 -8.548 4.396 13.548 1.00 18.08 N ANISOU 1529 N VAL B 33 2715 94 -48 2028 2124 76 N ATOM 1530 CA VAL A 33 -7.342 5.210 13.608 1.00 18.09 C ANISOU 1530 CA VAL B 33 2598 58 20 2130 2144 103 C ATOM 1531 C VAL A 33 -7.284 6.139 12.386 1.00 18.05 C ANISOU 1531 C VAL B 33 2564 42 -37 2011 2280 149 C ATOM 1532 O VAL A 33 -7.047 7.340 12.525 1.00 19.47 O ANISOU 1532 O VAL B 33 3119 -33 -110 1870 2408 112 O ATOM 1533 CB VAL A 33 -6.110 4.321 13.707 1.00 19.42 C ANISOU 1533 CB VAL B 33 2690 9 53 2237 2449 -46 C ATOM 1534 CG1 VAL A 33 -4.816 5.142 13.475 1.00 21.72 C ANISOU 1534 CG1 VAL B 33 2780 -91 219 2636 2834 -220 C ATOM 1535 CG2 VAL A 33 -6.042 3.626 15.070 1.00 21.18 C ANISOU 1535 CG2 VAL B 33 3053 -56 131 2390 2604 -377 C ATOM 1536 N ALA A 34 -7.535 5.601 11.207 1.00 16.33 N ANISOU 1536 N ALA B 34 2386 -34 -60 1822 1995 227 N ATOM 1537 CA ALA A 34 -7.534 6.428 9.995 1.00 16.61 C ANISOU 1537 CA ALA B 34 2389 90 -49 1845 2076 321 C ATOM 1538 C ALA A 34 -8.563 7.530 10.097 1.00 17.18 C ANISOU 1538 C ALA B 34 2498 142 -29 1834 2195 347 C ATOM 1539 O ALA A 34 -8.294 8.696 9.745 1.00 18.87 O ANISOU 1539 O ALA B 34 2752 163 167 1857 2561 493 O ATOM 1540 CB ALA A 34 -7.782 5.582 8.771 1.00 16.42 C ANISOU 1540 CB ALA B 34 2417 115 -4 1711 2108 348 C ATOM 1541 N ALA A 35 -9.739 7.185 10.608 1.00 17.24 N ANISOU 1541 N ALA B 35 2353 153 49 1870 2325 262 N ATOM 1542 CA ALA A 35 -10.881 8.152 10.720 1.00 18.54 C ANISOU 1542 CA ALA B 35 2492 218 -154 2047 2503 262 C ATOM 1543 C ALA A 35 -10.684 9.160 11.841 1.00 19.68 C ANISOU 1543 C ALA B 35 2744 158 -175 2064 2669 275 C ATOM 1544 O ALA A 35 -11.446 10.122 11.959 1.00 21.82 O ANISOU 1544 O ALA B 35 2944 404 -412 2169 3175 223 O ATOM 1545 CB ALA A 35 -12.192 7.377 10.945 1.00 19.12 C ANISOU 1545 CB ALA B 35 2489 214 -189 2144 2629 253 C ATOM 1546 N ALA A 36 -9.665 8.982 12.652 1.00 20.48 N ANISOU 1546 N ALA B 36 2954 278 -462 2156 2668 236 N ATOM 1547 CA ALA A 36 -9.337 9.874 13.768 1.00 21.69 C ANISOU 1547 CA ALA B 36 3122 88 -352 2527 2591 197 C ATOM 1548 C ALA A 36 -8.170 10.756 13.443 1.00 23.01 C ANISOU 1548 C ALA B 36 3190 -47 -382 2861 2693 134 C ATOM 1549 O ALA A 36 -7.707 11.459 14.300 1.00 26.90 O ANISOU 1549 O ALA B 36 3981 -401 -388 3352 2885 227 O ATOM 1550 CB ALA A 36 -9.029 9.076 15.022 1.00 23.51 C ANISOU 1550 CB ALA B 36 3529 -44 -337 2797 2604 101 C ATOM 1551 N SER A 37 -7.735 10.821 12.199 1.00 21.90 N ANISOU 1551 N SER B 37 2856 168 -517 2736 2725 327 N ATOM 1552 CA SER A 37 -6.593 11.673 11.873 1.00 21.88 C ANISOU 1552 CA SER B 37 2723 222 -472 2728 2860 212 C ATOM 1553 C SER A 37 -6.853 13.165 12.092 1.00 23.39 C ANISOU 1553 C SER B 37 2794 164 -539 2885 3207 125 C ATOM 1554 O SER A 37 -7.887 13.713 11.687 1.00 24.12 O ANISOU 1554 O SER B 37 2964 221 -749 2986 3213 65 O ATOM 1555 CB SER A 37 -6.187 11.516 10.405 1.00 22.00 C ANISOU 1555 CB SER B 37 2869 248 -467 2635 2853 302 C ATOM 1556 OG SER A 37 -5.787 10.174 10.085 1.00 20.52 O ANISOU 1556 OG SER B 37 2796 408 -277 2171 2828 463 O ATOM 1557 N LYS A 38 -5.895 13.834 12.725 1.00 24.43 N ANISOU 1557 N LYS B 38 2801 114 -730 3012 3469 65 N ATOM 1558 CA LYS A 38 -5.929 15.300 12.961 1.00 25.29 C ANISOU 1558 CA LYS B 38 3021 138 -617 3094 3493 86 C ATOM 1559 C LYS A 38 -7.207 15.737 13.698 1.00 26.27 C ANISOU 1559 C LYS B 38 3203 97 -649 3116 3662 48 C ATOM 1560 O LYS A 38 -7.882 16.668 13.231 1.00 28.30 O ANISOU 1560 O LYS B 38 3204 160 -770 3685 3861 168 O ATOM 1561 CB LYS A 38 -5.795 16.111 11.689 1.00 27.45 C ANISOU 1561 CB LYS B 38 3315 92 -552 3306 3807 114 C ATOM 1562 CG LYS A 38 -4.584 15.751 10.838 1.00 30.91 C ANISOU 1562 CG LYS B 38 3826 321 -550 3759 4159 174 C ATOM 1563 CD LYS A 38 -3.503 16.702 10.924 1.00 35.52 C ANISOU 1563 CD LYS B 38 4337 89 -81 4456 4703 126 C ATOM 1564 CE LYS A 38 -3.893 18.074 10.454 1.00 34.99 C ANISOU 1564 CE LYS B 38 4523 184 -298 4031 4739 43 C ATOM 1565 NZ LYS A 38 -2.829 18.738 9.703 1.00 38.46 N ANISOU 1565 NZ LYS B 38 5055 39 -89 4638 4919 90 N ATOM 1566 N PRO A 39 -7.445 15.125 14.863 1.00 25.80 N ANISOU 1566 N PRO B 39 3015 -76 -820 3297 3488 199 N ATOM 1567 CA PRO A 39 -8.655 15.383 15.686 1.00 26.88 C ANISOU 1567 CA PRO B 39 3276 -12 -737 3396 3539 116 C ATOM 1568 C PRO A 39 -8.588 16.660 16.442 1.00 26.36 C ANISOU 1568 C PRO B 39 3209 -21 -671 3366 3437 31 C ATOM 1569 O PRO A 39 -7.553 17.000 17.027 1.00 27.64 O ANISOU 1569 O PRO B 39 3365 134 -964 3652 3482 10 O ATOM 1570 CB PRO A 39 -8.642 14.254 16.684 1.00 28.11 C ANISOU 1570 CB PRO B 39 3394 -34 -612 3678 3605 123 C ATOM 1571 CG PRO A 39 -7.209 13.911 16.838 1.00 29.65 C ANISOU 1571 CG PRO B 39 3472 -201 -461 3868 3922 1 C ATOM 1572 CD PRO A 39 -6.513 14.242 15.565 1.00 28.02 C ANISOU 1572 CD PRO B 39 3506 -136 -658 3552 3587 75 C ATOM 1573 N ALA A 40 -9.699 17.356 16.388 1.00 25.23 N ANISOU 1573 N ALA B 40 3005 -46 -752 3130 3451 116 N ATOM 1574 CA ALA A 40 -9.814 18.657 16.983 1.00 24.04 C ANISOU 1574 CA ALA B 40 2933 -48 -551 2948 3251 160 C ATOM 1575 C ALA A 40 -11.163 18.739 17.635 1.00 23.02 C ANISOU 1575 C ALA B 40 2596 -140 -611 2876 3272 57 C ATOM 1576 O ALA A 40 -12.133 18.125 17.220 1.00 25.34 O ANISOU 1576 O ALA B 40 2965 -101 -923 3159 3502 303 O ATOM 1577 CB ALA A 40 -9.695 19.703 15.921 1.00 24.25 C ANISOU 1577 CB ALA B 40 3040 36 -478 2928 3244 311 C ATOM 1578 N VAL A 41 -11.235 19.577 18.642 1.00 21.14 N ANISOU 1578 N VAL B 41 2497 -23 -550 2340 3194 51 N ATOM 1579 CA VAL A 41 -12.435 19.744 19.350 1.00 20.46 C ANISOU 1579 CA VAL B 41 2537 -104 -443 2266 2968 172 C ATOM 1580 C VAL A 41 -12.757 21.246 19.440 1.00 19.97 C ANISOU 1580 C VAL B 41 2451 56 -379 2305 2831 124 C ATOM 1581 O VAL A 41 -12.020 21.974 20.076 1.00 19.79 O ANISOU 1581 O VAL B 41 2493 32 -389 2273 2751 163 O ATOM 1582 CB VAL A 41 -12.365 19.093 20.744 1.00 21.84 C ANISOU 1582 CB VAL B 41 2820 99 -374 2353 3125 18 C ATOM 1583 CG1 VAL A 41 -13.633 19.177 21.430 1.00 24.34 C ANISOU 1583 CG1 VAL B 41 3237 33 -53 2631 3380 115 C ATOM 1584 CG2 VAL A 41 -11.919 17.632 20.664 1.00 25.17 C ANISOU 1584 CG2 VAL B 41 3196 31 -135 2677 3690 -56 C ATOM 1585 N GLU A 42 -13.847 21.692 18.780 1.00 19.83 N ANISOU 1585 N GLU B 42 2435 104 -224 2295 2801 94 N ATOM 1586 CA GLU A 42 -14.276 23.099 18.867 1.00 20.01 C ANISOU 1586 CA GLU B 42 2524 89 -113 2444 2634 289 C ATOM 1587 C GLU A 42 -15.369 23.110 19.939 1.00 17.92 C ANISOU 1587 C GLU B 42 2231 34 13 2139 2439 303 C ATOM 1588 O GLU A 42 -16.339 22.396 19.824 1.00 19.60 O ANISOU 1588 O GLU B 42 2353 -98 -55 2549 2544 208 O ATOM 1589 CB GLU A 42 -14.866 23.608 17.545 1.00 21.05 C ANISOU 1589 CB GLU B 42 2660 48 -163 2653 2682 329 C ATOM 1590 CG GLU A 42 -15.350 25.050 17.637 1.00 24.02 C ANISOU 1590 CG GLU B 42 3265 160 61 2837 3023 73 C ATOM 1591 CD GLU A 42 -16.034 25.616 16.387 1.00 27.88 C ANISOU 1591 CD GLU B 42 3827 163 80 3271 3494 -48 C ATOM 1592 OE1 GLU A 42 -16.333 24.864 15.457 1.00 35.59 O ANISOU 1592 OE1 GLU B 42 5547 59 -23 4211 3763 -285 O ATOM 1593 OE2 GLU A 42 -16.293 26.844 16.367 1.00 36.73 O ANISOU 1593 OE2 GLU B 42 5280 74 257 3810 4865 -145 O ATOM 1594 N ILE A 43 -15.168 23.889 20.963 1.00 18.28 N ANISOU 1594 N ILE B 43 2211 153 45 2424 2312 278 N ATOM 1595 CA ILE A 43 -16.131 23.996 22.052 1.00 18.10 C ANISOU 1595 CA ILE B 43 2286 58 137 2361 2228 286 C ATOM 1596 C ILE A 43 -16.601 25.443 22.082 1.00 18.96 C ANISOU 1596 C ILE B 43 2317 124 163 2542 2343 281 C ATOM 1597 O ILE A 43 -15.795 26.392 22.192 1.00 18.96 O ANISOU 1597 O ILE B 43 2384 358 147 2323 2494 329 O ATOM 1598 CB ILE A 43 -15.491 23.640 23.403 1.00 17.14 C ANISOU 1598 CB ILE B 43 2084 96 146 2111 2314 103 C ATOM 1599 CG1 ILE A 43 -14.968 22.211 23.358 1.00 17.54 C ANISOU 1599 CG1 ILE B 43 2184 39 116 2111 2368 108 C ATOM 1600 CG2 ILE A 43 -16.514 23.859 24.513 1.00 18.01 C ANISOU 1600 CG2 ILE B 43 2281 86 158 2360 2201 98 C ATOM 1601 CD1 ILE A 43 -14.282 21.756 24.602 1.00 18.71 C ANISOU 1601 CD1 ILE B 43 2279 -37 182 2254 2574 57 C ATOM 1602 N LYS A 44 -17.929 25.591 22.090 1.00 19.14 N ANISOU 1602 N LYS B 44 2346 226 302 2669 2255 242 N ATOM 1603 CA LYS A 44 -18.600 26.851 22.370 1.00 19.66 C ANISOU 1603 CA LYS B 44 2570 211 309 2616 2282 319 C ATOM 1604 C LYS A 44 -19.372 26.636 23.659 1.00 19.57 C ANISOU 1604 C LYS B 44 2551 202 338 2480 2404 371 C ATOM 1605 O LYS A 44 -20.265 25.818 23.692 1.00 22.03 O ANISOU 1605 O LYS B 44 2747 21 286 3181 2441 573 O ATOM 1606 CB LYS A 44 -19.565 27.197 21.244 1.00 21.31 C ANISOU 1606 CB LYS B 44 2630 259 374 2867 2598 312 C ATOM 1607 N GLN A 45 -18.951 27.292 24.702 1.00 20.83 N ANISOU 1607 N GLN B 45 2765 65 288 2599 2548 543 N ATOM 1608 CA GLN A 45 -19.595 27.184 26.008 1.00 20.16 C ANISOU 1608 CA GLN B 45 2731 108 178 2494 2434 430 C ATOM 1609 C GLN A 45 -20.347 28.430 26.307 1.00 20.79 C ANISOU 1609 C GLN B 45 2751 40 223 2501 2644 405 C ATOM 1610 O GLN A 45 -19.752 29.517 26.331 1.00 22.58 O ANISOU 1610 O GLN B 45 2943 29 54 2449 3185 628 O ATOM 1611 CB GLN A 45 -18.571 26.944 27.087 1.00 20.01 C ANISOU 1611 CB GLN B 45 2589 114 185 2467 2545 502 C ATOM 1612 CG GLN A 45 -19.186 26.883 28.487 1.00 19.71 C ANISOU 1612 CG GLN B 45 2574 236 186 2411 2504 450 C ATOM 1613 CD GLN A 45 -18.167 26.735 29.582 1.00 19.82 C ANISOU 1613 CD GLN B 45 2593 125 88 2313 2623 206 C ATOM 1614 OE1 GLN A 45 -16.966 26.536 29.341 1.00 22.79 O ANISOU 1614 OE1 GLN B 45 2563 235 -99 2685 3409 360 O ATOM 1615 NE2 GLN A 45 -18.626 26.855 30.816 1.00 20.13 N ANISOU 1615 NE2 GLN B 45 2827 123 343 2457 2363 228 N ATOM 1616 N GLU A 46 -21.635 28.277 26.620 1.00 19.81 N ANISOU 1616 N GLU B 46 2665 175 128 2232 2626 321 N ATOM 1617 CA GLU A 46 -22.489 29.356 27.048 1.00 20.53 C ANISOU 1617 CA GLU B 46 2871 166 86 2323 2603 252 C ATOM 1618 C GLU A 46 -23.032 29.039 28.436 1.00 19.99 C ANISOU 1618 C GLU B 46 2660 283 166 2267 2665 268 C ATOM 1619 O GLU A 46 -24.073 28.435 28.571 1.00 20.56 O ANISOU 1619 O GLU B 46 2719 286 103 2599 2490 316 O ATOM 1620 CB GLU A 46 -23.613 29.542 26.028 1.00 21.37 C ANISOU 1620 CB GLU B 46 3033 193 45 2308 2777 227 C ATOM 1621 CG GLU A 46 -23.107 29.993 24.651 1.00 23.80 C ANISOU 1621 CG GLU B 46 3523 146 50 2647 2873 85 C ATOM 1622 CD GLU A 46 -24.208 30.582 23.783 1.00 27.09 C ANISOU 1622 CD GLU B 46 3914 263 229 3248 3130 117 C ATOM 1623 OE1 GLU A 46 -25.155 31.204 24.328 1.00 31.39 O ANISOU 1623 OE1 GLU B 46 4032 393 348 3860 4032 123 O ATOM 1624 OE2 GLU A 46 -24.096 30.464 22.547 1.00 34.87 O ANISOU 1624 OE2 GLU B 46 5137 278 12 4549 3561 -140 O ATOM 1625 N GLY A 47 -22.254 29.372 29.457 1.00 20.61 N ANISOU 1625 N GLY B 47 2705 121 128 2474 2650 381 N ATOM 1626 CA GLY A 47 -22.606 29.016 30.838 1.00 20.65 C ANISOU 1626 CA GLY B 47 2748 148 116 2401 2697 274 C ATOM 1627 C GLY A 47 -22.568 27.522 30.995 1.00 20.58 C ANISOU 1627 C GLY B 47 2639 180 264 2610 2569 184 C ATOM 1628 O GLY A 47 -21.512 26.895 30.886 1.00 21.49 O ANISOU 1628 O GLY B 47 2514 185 336 2787 2862 294 O ATOM 1629 N ASP A 48 -23.727 26.963 31.255 1.00 19.56 N ANISOU 1629 N ASP B 48 2571 121 157 2559 2302 237 N ATOM 1630 CA ASP A 48 -23.868 25.538 31.435 1.00 18.94 C ANISOU 1630 CA ASP B 48 2416 167 175 2555 2224 226 C ATOM 1631 C ASP A 48 -24.226 24.761 30.156 1.00 18.76 C ANISOU 1631 C ASP B 48 2414 163 205 2491 2222 176 C ATOM 1632 O ASP A 48 -24.419 23.559 30.194 1.00 18.99 O ANISOU 1632 O ASP B 48 2446 116 381 2562 2207 190 O ATOM 1633 CB ASP A 48 -24.895 25.266 32.548 1.00 19.15 C ANISOU 1633 CB ASP B 48 2518 139 225 2791 1967 257 C ATOM 1634 CG ASP A 48 -26.305 25.700 32.202 0.50 16.96 C ANISOU 1634 CG ASP B 48 2341 178 -23 2240 1862 319 C ATOM 1635 OD1 ASP A 48 -26.500 26.349 31.162 0.50 20.68 O ANISOU 1635 OD1 ASP B 48 2393 134 361 2865 2599 399 O ATOM 1636 OD2 ASP A 48 -27.231 25.352 32.979 0.50 17.38 O ANISOU 1636 OD2 ASP B 48 2076 246 178 2422 2103 434 O ATOM 1637 N THR A 49 -24.299 25.479 29.016 1.00 19.02 N ANISOU 1637 N THR B 49 2490 151 228 2501 2234 182 N ATOM 1638 CA THR A 49 -24.696 24.865 27.748 1.00 19.08 C ANISOU 1638 CA THR B 49 2391 190 174 2681 2177 180 C ATOM 1639 C THR A 49 -23.508 24.810 26.819 1.00 18.22 C ANISOU 1639 C THR B 49 2414 146 252 2464 2042 149 C ATOM 1640 O THR A 49 -22.788 25.778 26.683 1.00 20.88 O ANISOU 1640 O THR B 49 2728 210 101 2676 2530 328 O ATOM 1641 CB THR A 49 -25.876 25.639 27.117 1.00 20.87 C ANISOU 1641 CB THR B 49 2596 206 184 2887 2445 150 C ATOM 1642 OG1 THR A 49 -26.994 25.602 28.031 1.00 23.87 O ANISOU 1642 OG1 THR B 49 2709 400 257 3290 3069 576 O ATOM 1643 CG2 THR A 49 -26.269 25.048 25.795 1.00 22.21 C ANISOU 1643 CG2 THR B 49 2774 173 103 3015 2650 40 C ATOM 1644 N PHE A 50 -23.323 23.654 26.198 1.00 18.00 N ANISOU 1644 N PHE B 50 2279 135 258 2624 1936 246 N ATOM 1645 CA PHE A 50 -22.159 23.389 25.391 1.00 18.18 C ANISOU 1645 CA PHE B 50 2253 192 259 2706 1946 182 C ATOM 1646 C PHE A 50 -22.574 22.941 24.002 1.00 19.33 C ANISOU 1646 C PHE B 50 2347 85 323 3038 1958 171 C ATOM 1647 O PHE A 50 -23.493 22.139 23.825 1.00 20.58 O ANISOU 1647 O PHE B 50 2506 40 281 3315 1997 182 O ATOM 1648 CB PHE A 50 -21.331 22.270 26.028 1.00 18.09 C ANISOU 1648 CB PHE B 50 2339 156 350 2664 1868 162 C ATOM 1649 CG PHE A 50 -20.625 22.702 27.284 1.00 16.94 C ANISOU 1649 CG PHE B 50 2271 66 177 2219 1945 122 C ATOM 1650 CD1 PHE A 50 -21.297 22.765 28.485 1.00 17.09 C ANISOU 1650 CD1 PHE B 50 2364 129 344 2263 1864 21 C ATOM 1651 CD2 PHE A 50 -19.296 23.038 27.254 1.00 18.88 C ANISOU 1651 CD2 PHE B 50 2513 -13 414 2693 1964 161 C ATOM 1652 CE1 PHE A 50 -20.635 23.189 29.624 1.00 17.88 C ANISOU 1652 CE1 PHE B 50 2280 17 286 2458 2052 67 C ATOM 1653 CE2 PHE A 50 -18.650 23.428 28.392 1.00 19.33 C ANISOU 1653 CE2 PHE B 50 2431 -262 325 2694 2219 142 C ATOM 1654 CZ PHE A 50 -19.318 23.520 29.571 1.00 18.32 C ANISOU 1654 CZ PHE B 50 2581 -97 378 2467 1912 -57 C ATOM 1655 N TYR A 51 -21.817 23.423 23.026 1.00 20.23 N ANISOU 1655 N TYR B 51 2371 143 268 3304 2010 237 N ATOM 1656 CA TYR A 51 -21.830 22.898 21.688 1.00 21.73 C ANISOU 1656 CA TYR B 51 2459 1 130 3518 2276 208 C ATOM 1657 C TYR A 51 -20.415 22.423 21.407 1.00 21.51 C ANISOU 1657 C TYR B 51 2415 -76 2 3441 2317 285 C ATOM 1658 O TYR A 51 -19.454 23.187 21.533 1.00 23.73 O ANISOU 1658 O TYR B 51 2545 -79 -290 3734 2735 325 O ATOM 1659 CB TYR A 51 -22.231 23.964 20.682 1.00 24.12 C ANISOU 1659 CB TYR B 51 2708 54 299 3787 2669 175 C ATOM 1660 CG TYR A 51 -21.809 23.629 19.262 1.00 25.77 C ANISOU 1660 CG TYR B 51 3052 94 154 3947 2793 162 C ATOM 1661 CD1 TYR A 51 -22.598 22.808 18.458 1.00 30.96 C ANISOU 1661 CD1 TYR B 51 3852 66 159 4647 3264 -144 C ATOM 1662 CD2 TYR A 51 -20.603 24.104 18.730 1.00 27.34 C ANISOU 1662 CD2 TYR B 51 3309 -133 35 4055 3023 -22 C ATOM 1663 CE1 TYR A 51 -22.258 22.520 17.156 1.00 32.02 C ANISOU 1663 CE1 TYR B 51 3820 256 87 4750 3594 120 C ATOM 1664 CE2 TYR A 51 -20.247 23.813 17.380 1.00 28.10 C ANISOU 1664 CE2 TYR B 51 3526 -53 113 4126 3024 449 C ATOM 1665 CZ TYR A 51 -21.079 23.012 16.624 1.00 29.04 C ANISOU 1665 CZ TYR B 51 3498 67 195 4571 2964 267 C ATOM 1666 OH TYR A 51 -20.738 22.725 15.294 1.00 30.32 O ANISOU 1666 OH TYR B 51 3767 202 147 4723 3027 23 O ATOM 1667 N ILE A 52 -20.285 21.161 21.101 1.00 20.44 N ANISOU 1667 N ILE B 52 2113 -223 -66 3354 2299 56 N ATOM 1668 CA ILE A 52 -18.978 20.602 20.840 1.00 20.81 C ANISOU 1668 CA ILE B 52 2260 -175 -210 3224 2421 179 C ATOM 1669 C ILE A 52 -18.978 19.999 19.449 1.00 21.95 C ANISOU 1669 C ILE B 52 2375 -326 -240 3574 2389 205 C ATOM 1670 O ILE A 52 -19.847 19.180 19.129 1.00 24.45 O ANISOU 1670 O ILE B 52 2573 -610 -521 4224 2491 379 O ATOM 1671 CB ILE A 52 -18.567 19.595 21.908 1.00 21.18 C ANISOU 1671 CB ILE B 52 2228 -356 -162 3158 2660 58 C ATOM 1672 CG1 ILE A 52 -18.591 20.244 23.318 1.00 20.68 C ANISOU 1672 CG1 ILE B 52 2191 -157 2 3110 2553 55 C ATOM 1673 CG2 ILE A 52 -17.199 19.026 21.536 1.00 21.26 C ANISOU 1673 CG2 ILE B 52 2510 -217 -200 2804 2765 25 C ATOM 1674 CD1 ILE A 52 -18.080 19.383 24.435 1.00 21.54 C ANISOU 1674 CD1 ILE B 52 2503 -192 -67 2995 2685 1 C ATOM 1675 N LYS A 53 -18.047 20.433 18.596 1.00 20.80 N ANISOU 1675 N LYS B 53 2337 -179 -159 3368 2195 151 N ATOM 1676 CA LYS A 53 -17.851 19.833 17.280 1.00 21.53 C ANISOU 1676 CA LYS B 53 2425 -34 -65 3283 2470 118 C ATOM 1677 C LYS A 53 -16.508 19.152 17.248 1.00 20.87 C ANISOU 1677 C LYS B 53 2286 -18 -168 3050 2593 116 C ATOM 1678 O LYS A 53 -15.478 19.770 17.482 1.00 20.14 O ANISOU 1678 O LYS B 53 2147 32 -384 2866 2638 154 O ATOM 1679 CB LYS A 53 -17.923 20.897 16.200 1.00 22.09 C ANISOU 1679 CB LYS B 53 2686 112 14 3323 2384 154 C ATOM 1680 CG LYS A 53 -17.736 20.304 14.835 1.00 25.17 C ANISOU 1680 CG LYS B 53 3135 0 -135 3691 2736 124 C ATOM 1681 CD LYS A 53 -18.113 21.271 13.706 1.00 28.73 C ANISOU 1681 CD LYS B 53 3654 50 118 4114 3145 71 C ATOM 1682 CE LYS A 53 -17.547 22.603 13.864 1.00 34.01 C ANISOU 1682 CE LYS B 53 4401 36 54 4437 4083 25 C ATOM 1683 NZ LYS A 53 -18.357 23.399 14.820 1.00 38.31 N ANISOU 1683 NZ LYS B 53 4840 199 -132 5064 4650 30 N ATOM 1684 N VAL A 54 -16.547 17.849 17.026 1.00 21.61 N ANISOU 1684 N VAL B 54 2246 -208 -84 2935 3029 16 N ATOM 1685 CA VAL A 54 -15.351 17.064 16.853 1.00 23.08 C ANISOU 1685 CA VAL B 54 2766 -136 -205 2827 3175 -82 C ATOM 1686 C VAL A 54 -15.126 16.820 15.399 1.00 23.40 C ANISOU 1686 C VAL B 54 2720 -109 -228 2838 3331 11 C ATOM 1687 O VAL A 54 -15.967 16.235 14.728 1.00 24.13 O ANISOU 1687 O VAL B 54 2915 -213 -288 3100 3152 -222 O ATOM 1688 CB VAL A 54 -15.437 15.748 17.594 1.00 24.51 C ANISOU 1688 CB VAL B 54 3097 -103 -66 2954 3259 -197 C ATOM 1689 CG1 VAL A 54 -14.187 14.904 17.341 1.00 25.88 C ANISOU 1689 CG1 VAL B 54 3532 -5 -259 2873 3426 -334 C ATOM 1690 CG2 VAL A 54 -15.691 15.977 19.074 1.00 26.66 C ANISOU 1690 CG2 VAL B 54 3523 -170 -64 3194 3411 -262 C ATOM 1691 N SER A 55 -13.975 17.253 14.906 1.00 23.55 N ANISOU 1691 N SER B 55 2853 -20 -457 2732 3363 225 N ATOM 1692 CA SER A 55 -13.633 17.146 13.504 1.00 24.48 C ANISOU 1692 CA SER B 55 2979 149 -398 2958 3364 237 C ATOM 1693 C SER A 55 -12.352 16.314 13.337 1.00 24.38 C ANISOU 1693 C SER B 55 2924 251 -629 2893 3447 151 C ATOM 1694 O SER A 55 -11.423 16.383 14.148 1.00 26.73 O ANISOU 1694 O SER B 55 3232 286 -1074 3154 3769 169 O ATOM 1695 CB ASER A 55 -13.340 18.515 12.936 0.50 25.02 C ANISOU 1695 CB ASER B 55 3062 139 -309 3117 3326 313 C ATOM 1696 OG ASER A 55 -12.273 19.063 13.661 0.50 25.70 O ANISOU 1696 OG ASER B 55 3274 187 -414 3270 3218 347 O ATOM 1697 N THR A 56 -12.355 15.458 12.327 1.00 23.84 N ANISOU 1697 N THR B 56 3063 174 -629 2670 3323 320 N ATOM 1698 CA THR A 56 -11.129 14.799 11.852 1.00 22.38 C ANISOU 1698 CA THR B 56 2896 240 -480 2423 3182 246 C ATOM 1699 C THR A 56 -11.060 15.041 10.380 1.00 23.38 C ANISOU 1699 C THR B 56 3177 293 -410 2366 3340 218 C ATOM 1700 O THR A 56 -11.933 15.660 9.787 1.00 24.10 O ANISOU 1700 O THR B 56 3157 443 -525 2673 3326 260 O ATOM 1701 CB THR A 56 -11.203 13.306 12.125 1.00 22.48 C ANISOU 1701 CB THR B 56 2918 59 -374 2391 3229 143 C ATOM 1702 OG1 THR A 56 -12.183 12.693 11.268 1.00 22.66 O ANISOU 1702 OG1 THR B 56 3002 204 -407 2497 3110 -33 O ATOM 1703 CG2 THR A 56 -11.543 13.056 13.567 1.00 22.96 C ANISOU 1703 CG2 THR B 56 2872 245 -446 2595 3254 116 C ATOM 1704 N THR A 57 -10.076 14.440 9.721 1.00 22.30 N ANISOU 1704 N THR B 57 3033 373 -334 2246 3190 304 N ATOM 1705 CA THR A 57 -9.978 14.638 8.305 1.00 23.74 C ANISOU 1705 CA THR B 57 3282 287 -238 2495 3241 200 C ATOM 1706 C THR A 57 -11.160 14.006 7.581 1.00 22.67 C ANISOU 1706 C THR B 57 2956 383 -230 2644 3012 230 C ATOM 1707 O THR A 57 -11.403 14.361 6.438 1.00 27.10 O ANISOU 1707 O THR B 57 3485 421 -50 3239 3570 -124 O ATOM 1708 CB THR A 57 -8.662 14.117 7.711 1.00 22.73 C ANISOU 1708 CB THR B 57 3064 321 -115 2455 3115 291 C ATOM 1709 OG1 THR A 57 -8.498 12.714 7.955 1.00 22.63 O ANISOU 1709 OG1 THR B 57 3288 120 -441 2098 3213 593 O ATOM 1710 CG2 THR A 57 -7.456 14.843 8.252 1.00 23.76 C ANISOU 1710 CG2 THR B 57 3120 106 -267 2683 3223 242 C ATOM 1711 N VAL A 58 -11.857 13.034 8.206 1.00 24.62 N ANISOU 1711 N VAL B 58 3317 183 -244 2738 3297 44 N ATOM 1712 CA VAL A 58 -12.975 12.324 7.570 1.00 25.07 C ANISOU 1712 CA VAL B 58 3236 143 -278 3042 3246 12 C ATOM 1713 C VAL A 58 -14.370 12.745 7.970 1.00 26.95 C ANISOU 1713 C VAL B 58 3427 131 -241 3455 3357 -15 C ATOM 1714 O VAL A 58 -15.308 12.558 7.203 1.00 28.18 O ANISOU 1714 O VAL B 58 3425 211 -330 3776 3503 -179 O ATOM 1715 CB VAL A 58 -12.919 10.775 7.781 1.00 24.99 C ANISOU 1715 CB VAL B 58 3132 -2 -351 2996 3367 111 C ATOM 1716 CG1 VAL A 58 -11.642 10.231 7.355 1.00 25.42 C ANISOU 1716 CG1 VAL B 58 2933 53 -372 3209 3516 18 C ATOM 1717 CG2 VAL A 58 -13.135 10.374 9.172 1.00 27.98 C ANISOU 1717 CG2 VAL B 58 3312 154 15 3479 3838 -185 C ATOM 1718 N ARG A 59 -14.565 13.265 9.171 1.00 26.95 N ANISOU 1718 N ARG B 59 3319 34 -363 3536 3382 -6 N ATOM 1719 CA ARG A 59 -15.912 13.596 9.583 1.00 28.39 C ANISOU 1719 CA ARG B 59 3456 52 -190 3740 3589 81 C ATOM 1720 C ARG A 59 -15.942 14.653 10.619 1.00 27.97 C ANISOU 1720 C ARG B 59 3249 23 -203 3904 3472 120 C ATOM 1721 O ARG A 59 -14.938 14.977 11.246 1.00 27.47 O ANISOU 1721 O ARG B 59 3109 20 -390 3886 3439 193 O ATOM 1722 CB ARG A 59 -16.601 12.375 10.086 1.00 29.65 C ANISOU 1722 CB ARG B 59 3568 3 -173 3916 3780 167 C ATOM 1723 N THR A 60 -17.145 15.174 10.810 1.00 29.63 N ANISOU 1723 N THR B 60 3437 108 -197 4232 3586 43 N ATOM 1724 CA THR A 60 -17.422 16.133 11.837 1.00 30.15 C ANISOU 1724 CA THR B 60 3551 18 -150 4207 3695 95 C ATOM 1725 C THR A 60 -18.680 15.651 12.564 1.00 29.91 C ANISOU 1725 C THR B 60 3437 -64 -221 4382 3544 80 C ATOM 1726 O THR A 60 -19.666 15.236 11.928 1.00 30.19 O ANISOU 1726 O THR B 60 3393 61 -454 4634 3442 0 O ATOM 1727 CB THR A 60 -17.644 17.512 11.221 1.00 32.00 C ANISOU 1727 CB THR B 60 3920 20 -39 4309 3927 76 C ATOM 1728 OG1 THR A 60 -16.395 18.024 10.739 1.00 35.09 O ANISOU 1728 OG1 THR B 60 4333 114 278 4405 4594 210 O ATOM 1729 CG2 THR A 60 -18.202 18.440 12.208 1.00 34.30 C ANISOU 1729 CG2 THR B 60 4269 130 -40 4526 4236 43 C ATOM 1730 N THR A 61 -18.629 15.675 13.890 1.00 28.13 N ANISOU 1730 N THR B 61 3248 -139 -336 4133 3306 -10 N ATOM 1731 CA THR A 61 -19.766 15.277 14.712 1.00 28.74 C ANISOU 1731 CA THR B 61 3267 -200 -375 4096 3556 24 C ATOM 1732 C THR A 61 -20.027 16.396 15.654 1.00 27.18 C ANISOU 1732 C THR B 61 3051 -242 -480 4066 3209 -1 C ATOM 1733 O THR A 61 -19.104 17.015 16.141 1.00 27.00 O ANISOU 1733 O THR B 61 2848 -478 -469 3867 3543 -153 O ATOM 1734 CB THR A 61 -19.455 14.037 15.563 1.00 28.78 C ANISOU 1734 CB THR B 61 3296 -303 -321 3983 3653 56 C ATOM 1735 OG1 THR A 61 -18.371 14.277 16.483 1.00 35.63 O ANISOU 1735 OG1 THR B 61 4222 -42 -171 4995 4318 49 O ATOM 1736 CG2 THR A 61 -19.068 12.943 14.676 1.00 30.65 C ANISOU 1736 CG2 THR B 61 3778 -47 -159 4234 3631 120 C ATOM 1737 N GLU A 62 -21.291 16.625 15.942 1.00 27.34 N ANISOU 1737 N GLU B 62 2982 -336 -493 4197 3209 12 N ATOM 1738 CA GLU A 62 -21.688 17.677 16.854 1.00 26.77 C ANISOU 1738 CA GLU B 62 3046 -299 -398 4066 3059 180 C ATOM 1739 C GLU A 62 -22.472 17.069 18.019 1.00 26.74 C ANISOU 1739 C GLU B 62 2928 -467 -445 4178 3053 148 C ATOM 1740 O GLU A 62 -23.356 16.234 17.809 1.00 27.49 O ANISOU 1740 O GLU B 62 3004 -750 -673 4377 3063 216 O ATOM 1741 CB GLU A 62 -22.522 18.696 16.128 1.00 28.08 C ANISOU 1741 CB GLU B 62 3470 -285 -429 4073 3126 260 C ATOM 1742 N ILE A 63 -22.170 17.491 19.244 1.00 25.53 N ANISOU 1742 N ILE B 63 2871 -370 -395 3979 2849 156 N ATOM 1743 CA ILE A 63 -23.074 17.227 20.361 1.00 26.48 C ANISOU 1743 CA ILE B 63 3231 -291 -253 3815 3015 125 C ATOM 1744 C ILE A 63 -23.408 18.553 20.985 1.00 24.70 C ANISOU 1744 C ILE B 63 3100 -337 -284 3682 2600 87 C ATOM 1745 O ILE A 63 -22.630 19.494 20.957 1.00 26.06 O ANISOU 1745 O ILE B 63 3350 -381 -273 3845 2706 447 O ATOM 1746 CB ILE A 63 -22.578 16.192 21.448 1.00 27.39 C ANISOU 1746 CB ILE B 63 3355 -258 -243 3754 3296 24 C ATOM 1747 CG1 ILE A 63 -21.270 16.628 22.076 1.00 27.78 C ANISOU 1747 CG1 ILE B 63 3197 -37 -146 3840 3515 64 C ATOM 1748 CG2 ILE A 63 -22.381 14.786 20.864 1.00 28.99 C ANISOU 1748 CG2 ILE B 63 3644 -212 -172 3869 3500 166 C ATOM 1749 CD1 ILE A 63 -20.952 15.878 23.347 1.00 27.42 C ANISOU 1749 CD1 ILE B 63 3317 23 -173 3856 3246 80 C ATOM 1750 N ASN A 64 -24.611 18.629 21.495 1.00 24.54 N ANISOU 1750 N ASN B 64 3162 -335 -232 3656 2505 51 N ATOM 1751 CA ASN A 64 -25.076 19.791 22.191 1.00 24.04 C ANISOU 1751 CA ASN B 64 3059 -233 -53 3533 2539 239 C ATOM 1752 C ASN A 64 -25.636 19.279 23.525 1.00 22.30 C ANISOU 1752 C ASN B 64 2947 -263 -64 3341 2183 125 C ATOM 1753 O ASN A 64 -26.434 18.324 23.541 1.00 24.30 O ANISOU 1753 O ASN B 64 3294 -536 -256 3713 2225 118 O ATOM 1754 CB ASN A 64 -26.248 20.430 21.431 1.00 25.68 C ANISOU 1754 CB ASN B 64 3410 -156 15 3743 2601 151 C ATOM 1755 CG ASN A 64 -25.852 21.144 20.146 1.00 30.00 C ANISOU 1755 CG ASN B 64 3713 -155 160 4271 3415 221 C ATOM 1756 OD1 ASN A 64 -25.883 20.556 19.080 1.00 34.80 O ANISOU 1756 OD1 ASN B 64 4066 -276 -58 5122 4034 -17 O ATOM 1757 ND2 ASN A 64 -25.601 22.432 20.246 1.00 31.96 N ANISOU 1757 ND2 ASN B 64 3954 216 259 4412 3777 163 N ATOM 1758 N PHE A 65 -25.243 19.882 24.629 1.00 20.10 N ANISOU 1758 N PHE B 65 2580 -62 -33 3005 2051 151 N ATOM 1759 CA PHE A 65 -25.788 19.452 25.930 1.00 19.49 C ANISOU 1759 CA PHE B 65 2492 -22 91 2807 2106 68 C ATOM 1760 C PHE A 65 -25.823 20.613 26.890 1.00 18.50 C ANISOU 1760 C PHE B 65 2266 25 126 2709 2053 25 C ATOM 1761 O PHE A 65 -25.090 21.605 26.760 1.00 19.23 O ANISOU 1761 O PHE B 65 2460 25 128 2852 1994 145 O ATOM 1762 CB PHE A 65 -25.016 18.256 26.532 1.00 19.94 C ANISOU 1762 CB PHE B 65 2562 -45 30 2820 2191 121 C ATOM 1763 CG PHE A 65 -23.572 18.552 26.861 1.00 19.38 C ANISOU 1763 CG PHE B 65 2582 113 90 2658 2122 103 C ATOM 1764 CD1 PHE A 65 -23.204 19.097 28.067 1.00 18.33 C ANISOU 1764 CD1 PHE B 65 2460 -5 206 2519 1986 13 C ATOM 1765 CD2 PHE A 65 -22.592 18.231 25.956 1.00 20.35 C ANISOU 1765 CD2 PHE B 65 2671 -64 -161 2935 2124 43 C ATOM 1766 CE1 PHE A 65 -21.892 19.352 28.356 1.00 19.22 C ANISOU 1766 CE1 PHE B 65 2655 104 259 2384 2260 -49 C ATOM 1767 CE2 PHE A 65 -21.263 18.437 26.253 1.00 20.33 C ANISOU 1767 CE2 PHE B 65 2537 -56 145 2721 2465 194 C ATOM 1768 CZ PHE A 65 -20.927 19.032 27.439 1.00 19.03 C ANISOU 1768 CZ PHE B 65 2497 55 220 2259 2473 44 C ATOM 1769 N LYS A 66 -26.648 20.453 27.924 1.00 17.59 N ANISOU 1769 N LYS B 66 2114 53 231 2645 1924 3 N ATOM 1770 CA LYS A 66 -26.660 21.328 29.087 1.00 17.37 C ANISOU 1770 CA LYS B 66 2193 94 167 2418 1985 12 C ATOM 1771 C LYS A 66 -26.235 20.466 30.273 1.00 16.22 C ANISOU 1771 C LYS B 66 2054 72 172 2253 1853 77 C ATOM 1772 O LYS A 66 -26.702 19.318 30.441 1.00 16.68 O ANISOU 1772 O LYS B 66 2149 134 172 2401 1787 5 O ATOM 1773 CB LYS A 66 -28.069 21.859 29.310 1.00 18.67 C ANISOU 1773 CB LYS B 66 2346 148 265 2609 2136 -93 C ATOM 1774 CG LYS A 66 -28.242 22.768 30.511 1.00 20.73 C ANISOU 1774 CG LYS B 66 2623 160 234 2852 2401 16 C ATOM 1775 CD LYS A 66 -29.689 23.247 30.689 1.00 22.23 C ANISOU 1775 CD LYS B 66 2777 363 89 2948 2720 42 C ATOM 1776 CE LYS A 66 -29.871 24.237 31.814 0.50 23.67 C ANISOU 1776 CE LYS B 66 3099 204 56 3228 2664 7 C ATOM 1777 NZ LYS A 66 -31.264 24.734 31.797 0.50 27.05 N ANISOU 1777 NZ LYS B 66 3441 321 -67 3505 3332 116 N ATOM 1778 N VAL A 67 -25.347 20.991 31.097 1.00 16.15 N ANISOU 1778 N VAL B 67 2118 -1 139 2196 1820 104 N ATOM 1779 CA VAL A 67 -24.965 20.263 32.318 1.00 16.18 C ANISOU 1779 CA VAL B 67 2151 82 115 2228 1768 120 C ATOM 1780 C VAL A 67 -26.197 19.899 33.126 1.00 16.45 C ANISOU 1780 C VAL B 67 2184 155 88 2232 1831 86 C ATOM 1781 O VAL A 67 -27.049 20.752 33.363 1.00 18.10 O ANISOU 1781 O VAL B 67 2430 281 170 2454 1993 83 O ATOM 1782 CB VAL A 67 -23.952 21.096 33.139 1.00 17.06 C ANISOU 1782 CB VAL B 67 2216 -23 183 2259 2006 43 C ATOM 1783 CG1 VAL A 67 -23.697 20.417 34.464 1.00 18.41 C ANISOU 1783 CG1 VAL B 67 2554 -70 144 2454 1987 -43 C ATOM 1784 CG2 VAL A 67 -22.656 21.213 32.345 1.00 17.92 C ANISOU 1784 CG2 VAL B 67 2424 -67 190 2292 2094 -161 C ATOM 1785 N GLY A 68 -26.293 18.619 33.493 1.00 15.96 N ANISOU 1785 N GLY B 68 2052 141 101 2263 1749 162 N ATOM 1786 CA GLY A 68 -27.419 18.157 34.285 1.00 16.69 C ANISOU 1786 CA GLY B 68 2112 44 96 2368 1860 117 C ATOM 1787 C GLY A 68 -28.626 17.683 33.512 1.00 17.17 C ANISOU 1787 C GLY B 68 2072 81 94 2558 1892 176 C ATOM 1788 O GLY A 68 -29.580 17.225 34.129 1.00 19.10 O ANISOU 1788 O GLY B 68 2227 -174 166 3021 2007 177 O ATOM 1789 N GLU A 69 -28.602 17.769 32.186 1.00 16.77 N ANISOU 1789 N GLU B 69 1887 129 -21 2625 1859 125 N ATOM 1790 CA GLU A 69 -29.731 17.334 31.362 1.00 17.10 C ANISOU 1790 CA GLU B 69 2051 76 -2 2544 1901 55 C ATOM 1791 C GLU A 69 -29.290 16.210 30.422 1.00 16.65 C ANISOU 1791 C GLU B 69 2009 55 11 2403 1915 -198 C ATOM 1792 O GLU A 69 -28.284 16.341 29.713 1.00 17.00 O ANISOU 1792 O GLU B 69 1876 44 62 2648 1933 -6 O ATOM 1793 CB GLU A 69 -30.269 18.512 30.531 1.00 17.36 C ANISOU 1793 CB GLU B 69 2005 195 -131 2491 2100 76 C ATOM 1794 CG GLU A 69 -31.486 18.144 29.752 1.00 19.86 C ANISOU 1794 CG GLU B 69 2311 186 -92 2767 2466 -28 C ATOM 1795 CD GLU A 69 -32.200 19.285 29.085 1.00 21.84 C ANISOU 1795 CD GLU B 69 2543 153 -89 3056 2695 -257 C ATOM 1796 OE1 GLU A 69 -32.008 20.434 29.475 1.00 26.40 O ANISOU 1796 OE1 GLU B 69 3128 339 -112 3022 3880 -650 O ATOM 1797 OE2 GLU A 69 -32.987 18.986 28.158 1.00 25.55 O ANISOU 1797 OE2 GLU B 69 2832 492 -145 3672 3202 -375 O ATOM 1798 N GLU A 70 -30.029 15.104 30.384 1.00 17.31 N ANISOU 1798 N GLU B 70 1931 2 -11 2562 2083 -36 N ATOM 1799 CA GLU A 70 -29.671 13.997 29.519 1.00 18.31 C ANISOU 1799 CA GLU B 70 2114 -14 -25 2625 2217 -143 C ATOM 1800 C GLU A 70 -29.679 14.406 28.075 1.00 17.98 C ANISOU 1800 C GLU B 70 2034 114 -142 2649 2148 -238 C ATOM 1801 O GLU A 70 -30.488 15.212 27.658 1.00 19.34 O ANISOU 1801 O GLU B 70 1991 312 -146 3029 2325 -222 O ATOM 1802 CB GLU A 70 -30.606 12.833 29.776 1.00 20.85 C ANISOU 1802 CB GLU B 70 2492 -128 -53 2779 2650 -62 C ATOM 1803 CG GLU A 70 -30.370 12.226 31.143 1.00 22.21 C ANISOU 1803 CG GLU B 70 2698 -211 -28 2899 2840 -46 C ATOM 1804 CD GLU A 70 -31.311 11.094 31.485 0.50 22.42 C ANISOU 1804 CD GLU B 70 2665 -192 158 2964 2889 -102 C ATOM 1805 OE1 GLU A 70 -30.952 10.274 32.351 0.50 25.18 O ANISOU 1805 OE1 GLU B 70 3292 -292 364 2934 3340 -139 O ATOM 1806 OE2 GLU A 70 -32.404 11.020 30.882 0.50 25.69 O ANISOU 1806 OE2 GLU B 70 2758 -308 213 3294 3708 -153 O ATOM 1807 N PHE A 71 -28.797 13.787 27.291 1.00 18.48 N ANISOU 1807 N PHE B 71 2065 220 -146 2705 2249 -181 N ATOM 1808 CA PHE A 71 -28.740 13.975 25.845 1.00 18.98 C ANISOU 1808 CA PHE B 71 2357 170 -123 2714 2142 -283 C ATOM 1809 C PHE A 71 -28.321 12.658 25.198 1.00 20.13 C ANISOU 1809 C PHE B 71 2507 202 -122 2794 2347 -348 C ATOM 1810 O PHE A 71 -27.900 11.735 25.875 1.00 20.82 O ANISOU 1810 O PHE B 71 2852 160 -270 2750 2308 -401 O ATOM 1811 CB PHE A 71 -27.816 15.107 25.444 1.00 19.07 C ANISOU 1811 CB PHE B 71 2414 197 -130 2771 2061 -279 C ATOM 1812 CG PHE A 71 -26.383 14.868 25.756 1.00 18.70 C ANISOU 1812 CG PHE B 71 2507 149 -89 2522 2077 -105 C ATOM 1813 CD1 PHE A 71 -25.921 15.036 27.049 1.00 19.03 C ANISOU 1813 CD1 PHE B 71 2426 18 -1 2470 2333 -193 C ATOM 1814 CD2 PHE A 71 -25.484 14.526 24.761 1.00 20.50 C ANISOU 1814 CD2 PHE B 71 2682 215 -158 2879 2227 -207 C ATOM 1815 CE1 PHE A 71 -24.616 14.865 27.328 1.00 20.78 C ANISOU 1815 CE1 PHE B 71 2449 -42 31 2863 2583 -266 C ATOM 1816 CE2 PHE A 71 -24.122 14.335 25.089 1.00 21.44 C ANISOU 1816 CE2 PHE B 71 2712 130 -82 2688 2743 78 C ATOM 1817 CZ PHE A 71 -23.737 14.528 26.371 1.00 19.90 C ANISOU 1817 CZ PHE B 71 2261 46 209 2671 2627 -83 C ATOM 1818 N GLU A 72 -28.452 12.582 23.882 1.00 21.41 N ANISOU 1818 N GLU B 72 2790 222 -182 2979 2365 -355 N ATOM 1819 CA GLU A 72 -28.112 11.360 23.167 1.00 22.76 C ANISOU 1819 CA GLU B 72 2974 115 -153 3066 2606 -326 C ATOM 1820 C GLU A 72 -26.836 11.558 22.398 1.00 21.78 C ANISOU 1820 C GLU B 72 3007 187 -236 2829 2436 -284 C ATOM 1821 O GLU A 72 -26.637 12.583 21.760 1.00 24.31 O ANISOU 1821 O GLU B 72 3518 245 -167 3035 2683 -143 O ATOM 1822 CB AGLU A 72 -29.234 10.976 22.199 0.50 23.69 C ANISOU 1822 CB AGLU B 72 3074 48 -186 3241 2684 -333 C ATOM 1823 CG AGLU A 72 -30.550 10.693 22.886 0.50 25.30 C ANISOU 1823 CG AGLU B 72 3198 -90 -136 3433 2982 -207 C ATOM 1824 CD AGLU A 72 -31.426 9.653 22.155 0.50 26.07 C ANISOU 1824 CD AGLU B 72 3309 -56 -49 3336 3259 -191 C ATOM 1825 OE1AGLU A 72 -31.159 9.343 20.977 0.50 28.63 O ANISOU 1825 OE1AGLU B 72 3762 -136 -40 3667 3447 -216 O ATOM 1826 OE2AGLU A 72 -32.360 9.131 22.800 0.50 29.49 O ANISOU 1826 OE2AGLU B 72 3466 -7 32 3797 3939 -111 O ATOM 1827 N GLU A 73 -25.947 10.582 22.484 1.00 21.66 N ANISOU 1827 N GLU B 73 3009 173 -230 2904 2314 -313 N ATOM 1828 CA GLU A 73 -24.768 10.538 21.634 1.00 22.01 C ANISOU 1828 CA GLU B 73 2988 133 -240 2932 2440 -133 C ATOM 1829 C GLU A 73 -24.449 9.070 21.366 1.00 21.54 C ANISOU 1829 C GLU B 73 2950 133 -245 2864 2369 -152 C ATOM 1830 O GLU A 73 -25.363 8.221 21.377 1.00 22.27 O ANISOU 1830 O GLU B 73 2986 181 -440 2994 2481 -75 O ATOM 1831 CB GLU A 73 -23.610 11.306 22.249 1.00 21.91 C ANISOU 1831 CB GLU B 73 2921 145 -184 2874 2530 -20 C ATOM 1832 CG GLU A 73 -23.188 10.797 23.614 1.00 21.63 C ANISOU 1832 CG GLU B 73 2843 84 -140 2926 2447 -89 C ATOM 1833 CD GLU A 73 -21.903 11.410 24.154 1.00 21.79 C ANISOU 1833 CD GLU B 73 2788 93 -223 2992 2499 23 C ATOM 1834 OE1 GLU A 73 -21.185 12.128 23.396 1.00 26.27 O ANISOU 1834 OE1 GLU B 73 3167 -121 272 3753 3059 0 O ATOM 1835 OE2 GLU A 73 -21.628 11.223 25.363 1.00 20.64 O ANISOU 1835 OE2 GLU B 73 2604 192 -440 2856 2381 -30 O ATOM 1836 N GLN A 74 -23.187 8.771 21.065 1.00 22.94 N ANISOU 1836 N GLN B 74 2948 97 -339 3003 2764 -77 N ATOM 1837 CA GLN A 74 -22.738 7.395 20.928 1.00 23.25 C ANISOU 1837 CA GLN B 74 3087 109 -293 3013 2733 -25 C ATOM 1838 C GLN A 74 -21.524 7.162 21.799 1.00 22.24 C ANISOU 1838 C GLN B 74 2908 210 -413 2876 2665 84 C ATOM 1839 O GLN A 74 -20.765 8.067 22.083 1.00 22.92 O ANISOU 1839 O GLN B 74 2913 159 -424 2884 2910 124 O ATOM 1840 CB GLN A 74 -22.362 7.054 19.460 1.00 24.95 C ANISOU 1840 CB GLN B 74 3324 153 -299 3272 2883 -6 C ATOM 1841 CG GLN A 74 -23.548 7.017 18.537 1.00 27.85 C ANISOU 1841 CG GLN B 74 3606 90 -179 3767 3207 -80 C ATOM 1842 CD GLN A 74 -23.192 6.670 17.102 1.00 29.83 C ANISOU 1842 CD GLN B 74 3977 100 -189 4016 3339 -9 C ATOM 1843 OE1 GLN A 74 -22.024 6.540 16.747 1.00 35.77 O ANISOU 1843 OE1 GLN B 74 4640 292 -185 4880 4069 203 O ATOM 1844 NE2 GLN A 74 -24.204 6.543 16.275 1.00 36.63 N ANISOU 1844 NE2 GLN B 74 4693 90 -181 4905 4319 -212 N ATOM 1845 N THR A 75 -21.351 5.931 22.242 1.00 21.41 N ANISOU 1845 N THR B 75 2846 79 -388 2713 2573 25 N ATOM 1846 CA THR A 75 -20.116 5.540 22.905 1.00 21.66 C ANISOU 1846 CA THR B 75 2911 124 -405 2683 2636 24 C ATOM 1847 C THR A 75 -18.924 5.604 21.936 1.00 21.57 C ANISOU 1847 C THR B 75 3045 176 -355 2642 2506 8 C ATOM 1848 O THR A 75 -19.077 5.763 20.728 1.00 22.75 O ANISOU 1848 O THR B 75 3261 307 -364 2736 2646 120 O ATOM 1849 CB THR A 75 -20.227 4.129 23.429 1.00 20.87 C ANISOU 1849 CB THR B 75 2841 42 -433 2715 2372 48 C ATOM 1850 OG1 THR A 75 -20.366 3.218 22.332 1.00 22.61 O ANISOU 1850 OG1 THR B 75 3252 -109 -554 2642 2695 60 O ATOM 1851 CG2 THR A 75 -21.408 3.970 24.401 1.00 22.90 C ANISOU 1851 CG2 THR B 75 3021 -16 -412 2883 2796 95 C ATOM 1852 N VAL A 76 -17.717 5.433 22.476 1.00 21.35 N ANISOU 1852 N VAL B 76 2867 150 -264 2646 2596 101 N ATOM 1853 CA VAL A 76 -16.510 5.528 21.665 1.00 21.59 C ANISOU 1853 CA VAL B 76 3034 112 -252 2515 2653 224 C ATOM 1854 C VAL A 76 -16.480 4.452 20.575 1.00 23.15 C ANISOU 1854 C VAL B 76 3153 80 -250 2780 2861 214 C ATOM 1855 O VAL A 76 -15.907 4.671 19.503 1.00 24.84 O ANISOU 1855 O VAL B 76 3486 185 -182 3008 2943 436 O ATOM 1856 CB VAL A 76 -15.249 5.443 22.555 1.00 22.31 C ANISOU 1856 CB VAL B 76 2938 26 -184 2560 2979 220 C ATOM 1857 CG1 VAL A 76 -15.121 4.079 23.232 1.00 22.10 C ANISOU 1857 CG1 VAL B 76 2960 17 -244 2474 2960 188 C ATOM 1858 CG2 VAL A 76 -13.971 5.777 21.775 1.00 22.44 C ANISOU 1858 CG2 VAL B 76 2915 78 -211 2598 3011 240 C ATOM 1859 N ASP A 77 -17.086 3.298 20.830 1.00 23.18 N ANISOU 1859 N ASP B 77 3243 90 -373 2734 2830 212 N ATOM 1860 CA ASP A 77 -17.176 2.193 19.855 1.00 23.90 C ANISOU 1860 CA ASP B 77 3312 121 -422 2900 2868 188 C ATOM 1861 C ASP A 77 -18.470 2.251 19.050 1.00 24.22 C ANISOU 1861 C ASP B 77 3428 134 -453 2984 2789 73 C ATOM 1862 O ASP A 77 -18.768 1.304 18.306 1.00 27.09 O ANISOU 1862 O ASP B 77 3898 161 -769 3258 3136 -1 O ATOM 1863 CB ASP A 77 -17.020 0.811 20.534 1.00 24.38 C ANISOU 1863 CB ASP B 77 3448 62 -445 2780 3034 179 C ATOM 1864 CG ASP A 77 -18.043 0.513 21.601 1.00 25.52 C ANISOU 1864 CG ASP B 77 3484 0 -348 2660 3552 126 C ATOM 1865 OD1 ASP A 77 -18.379 1.402 22.402 1.00 24.90 O ANISOU 1865 OD1 ASP B 77 3658 208 -272 2792 3009 402 O ATOM 1866 OD2 ASP A 77 -18.431 -0.664 21.738 1.00 28.55 O ANISOU 1866 OD2 ASP B 77 3978 -238 -405 3048 3822 348 O ATOM 1867 N GLY A 78 -19.217 3.358 19.128 1.00 24.68 N ANISOU 1867 N GLY B 78 3416 216 -462 3194 2765 70 N ATOM 1868 CA GLY A 78 -20.349 3.643 18.220 1.00 25.53 C ANISOU 1868 CA GLY B 78 3449 123 -448 3292 2958 8 C ATOM 1869 C GLY A 78 -21.750 3.186 18.598 1.00 26.23 C ANISOU 1869 C GLY B 78 3458 29 -386 3414 3091 -165 C ATOM 1870 O GLY A 78 -22.674 3.196 17.753 1.00 28.66 O ANISOU 1870 O GLY B 78 3853 109 -382 3848 3187 -353 O ATOM 1871 N ARG A 79 -21.958 2.803 19.850 1.00 24.67 N ANISOU 1871 N ARG B 79 3222 16 -472 3229 2923 -78 N ATOM 1872 CA ARG A 79 -23.266 2.340 20.306 1.00 25.07 C ANISOU 1872 CA ARG B 79 3297 4 -404 3214 3011 -42 C ATOM 1873 C ARG A 79 -24.085 3.547 20.811 1.00 24.45 C ANISOU 1873 C ARG B 79 3251 22 -509 3082 2957 -171 C ATOM 1874 O ARG A 79 -23.574 4.376 21.579 1.00 24.17 O ANISOU 1874 O ARG B 79 3080 -15 -654 3195 2904 -387 O ATOM 1875 CB AARG A 79 -23.088 1.307 21.404 0.50 24.95 C ANISOU 1875 CB AARG B 79 3257 -13 -401 3155 3066 -31 C ATOM 1876 CG AARG A 79 -22.107 0.183 21.012 0.50 25.41 C ANISOU 1876 CG AARG B 79 3346 -23 -284 3064 3244 -25 C ATOM 1877 CD AARG A 79 -21.914 -0.794 22.149 0.50 25.62 C ANISOU 1877 CD AARG B 79 3400 -73 -224 3144 3189 -16 C ATOM 1878 NE AARG A 79 -23.158 -1.481 22.493 0.50 25.75 N ANISOU 1878 NE AARG B 79 3637 -184 -214 3032 3115 -54 N ATOM 1879 CZ AARG A 79 -23.280 -2.369 23.479 0.50 25.80 C ANISOU 1879 CZ AARG B 79 3466 -219 -56 3018 3315 -108 C ATOM 1880 NH1AARG A 79 -22.233 -2.703 24.236 0.50 25.60 N ANISOU 1880 NH1AARG B 79 3481 -122 -48 2734 3512 -43 N ATOM 1881 NH2AARG A 79 -24.462 -2.942 23.691 0.50 25.28 N ANISOU 1881 NH2AARG B 79 3444 -138 57 2913 3247 18 N ATOM 1882 N PRO A 80 -25.336 3.719 20.358 1.00 24.21 N ANISOU 1882 N PRO B 80 3240 -46 -624 3033 2926 -215 N ATOM 1883 CA PRO A 80 -26.146 4.806 20.876 1.00 23.68 C ANISOU 1883 CA PRO B 80 3117 -4 -400 3060 2817 -203 C ATOM 1884 C PRO A 80 -26.302 4.783 22.403 1.00 23.01 C ANISOU 1884 C PRO B 80 2949 -83 -362 2930 2862 -196 C ATOM 1885 O PRO A 80 -26.531 3.735 23.012 1.00 22.99 O ANISOU 1885 O PRO B 80 2984 -316 -642 2840 2909 -331 O ATOM 1886 CB PRO A 80 -27.494 4.639 20.152 1.00 24.38 C ANISOU 1886 CB PRO B 80 3162 -26 -319 3190 2910 -124 C ATOM 1887 CG PRO A 80 -27.224 3.776 19.004 1.00 25.97 C ANISOU 1887 CG PRO B 80 3429 -11 -456 3346 3089 -235 C ATOM 1888 CD PRO A 80 -26.018 2.975 19.277 1.00 24.73 C ANISOU 1888 CD PRO B 80 3402 -8 -524 3336 2656 -399 C ATOM 1889 N CYS A 81 -26.187 5.963 23.010 1.00 21.63 N ANISOU 1889 N CYS B 81 2792 -74 -347 2808 2619 -225 N ATOM 1890 CA CYS A 81 -26.334 6.064 24.457 1.00 21.54 C ANISOU 1890 CA CYS B 81 2769 -166 -323 2799 2614 -186 C ATOM 1891 C CYS A 81 -27.018 7.346 24.844 1.00 20.54 C ANISOU 1891 C CYS B 81 2559 -227 -240 2685 2558 -192 C ATOM 1892 O CYS A 81 -27.048 8.300 24.073 1.00 22.96 O ANISOU 1892 O CYS B 81 2928 -174 -296 2955 2840 -24 O ATOM 1893 CB CYS A 81 -24.961 5.930 25.154 1.00 21.24 C ANISOU 1893 CB CYS B 81 2733 -131 -350 2688 2647 -173 C ATOM 1894 SG CYS A 81 -23.736 7.217 24.783 1.00 21.04 S ANISOU 1894 SG CYS B 81 2677 -175 -542 2791 2525 -186 S ATOM 1895 N LYS A 82 -27.506 7.350 26.088 1.00 20.57 N ANISOU 1895 N LYS B 82 2591 -222 -318 2624 2600 -123 N ATOM 1896 CA LYS A 82 -27.977 8.526 26.787 1.00 21.00 C ANISOU 1896 CA LYS B 82 2637 -173 -320 2751 2589 -223 C ATOM 1897 C LYS A 82 -26.844 8.944 27.726 1.00 20.45 C ANISOU 1897 C LYS B 82 2615 -79 -236 2664 2489 -295 C ATOM 1898 O LYS A 82 -26.301 8.115 28.448 1.00 23.64 O ANISOU 1898 O LYS B 82 3114 -71 -189 2745 3121 -624 O ATOM 1899 CB LYS A 82 -29.272 8.204 27.552 1.00 23.38 C ANISOU 1899 CB LYS B 82 2874 65 -328 3131 2877 -54 C ATOM 1900 CG LYS A 82 -30.011 9.341 28.142 0.80 23.85 C ANISOU 1900 CG LYS B 82 2961 -137 -320 3018 3083 22 C ATOM 1901 CD LYS A 82 -31.428 8.980 28.509 0.80 25.63 C ANISOU 1901 CD LYS B 82 3074 -69 -105 3337 3326 36 C ATOM 1902 CE LYS A 82 -31.480 7.916 29.559 0.80 26.19 C ANISOU 1902 CE LYS B 82 3034 -217 27 3581 3336 133 C ATOM 1903 NZ LYS A 82 -32.786 8.005 30.281 0.80 26.65 N ANISOU 1903 NZ LYS B 82 2956 -44 -23 3983 3185 92 N ATOM 1904 N SER A 83 -26.518 10.218 27.707 1.00 18.57 N ANISOU 1904 N SER B 83 2444 -37 -206 2464 2146 -251 N ATOM 1905 CA SER A 83 -25.376 10.772 28.456 1.00 17.51 C ANISOU 1905 CA SER B 83 2226 17 -180 2413 2012 -168 C ATOM 1906 C SER A 83 -25.829 11.871 29.368 1.00 17.32 C ANISOU 1906 C SER B 83 2093 -9 -62 2389 2097 -121 C ATOM 1907 O SER A 83 -26.867 12.485 29.140 1.00 18.15 O ANISOU 1907 O SER B 83 2103 34 -97 2630 2160 -189 O ATOM 1908 CB SER A 83 -24.372 11.318 27.463 1.00 17.74 C ANISOU 1908 CB SER B 83 2290 97 -167 2343 2106 43 C ATOM 1909 OG SER A 83 -23.696 10.246 26.801 1.00 19.68 O ANISOU 1909 OG SER B 83 2518 135 -468 2787 2170 -96 O ATOM 1910 N LEU A 84 -25.067 12.078 30.449 1.00 16.40 N ANISOU 1910 N LEU B 84 1957 -3 -188 2311 1961 -129 N ATOM 1911 CA LEU A 84 -25.389 13.107 31.429 1.00 16.47 C ANISOU 1911 CA LEU B 84 1992 -9 -133 2346 1920 5 C ATOM 1912 C LEU A 84 -24.070 13.640 31.935 1.00 15.87 C ANISOU 1912 C LEU B 84 1829 39 -120 2346 1853 15 C ATOM 1913 O LEU A 84 -23.252 12.903 32.501 1.00 15.98 O ANISOU 1913 O LEU B 84 1851 -33 67 2208 2013 -3 O ATOM 1914 CB LEU A 84 -26.199 12.494 32.562 1.00 16.68 C ANISOU 1914 CB LEU B 84 1966 43 -116 2423 1946 33 C ATOM 1915 CG LEU A 84 -26.619 13.426 33.680 1.00 17.75 C ANISOU 1915 CG LEU B 84 2110 -145 5 2554 2079 109 C ATOM 1916 CD1 LEU A 84 -27.389 14.586 33.161 1.00 19.08 C ANISOU 1916 CD1 LEU B 84 2184 -13 166 3017 2049 184 C ATOM 1917 CD2 LEU A 84 -27.406 12.660 34.742 1.00 18.60 C ANISOU 1917 CD2 LEU B 84 2337 -14 41 2791 1939 214 C ATOM 1918 N VAL A 85 -23.865 14.948 31.754 1.00 15.04 N ANISOU 1918 N VAL B 85 1802 -19 -110 2148 1764 -4 N ATOM 1919 CA VAL A 85 -22.647 15.631 32.168 1.00 15.07 C ANISOU 1919 CA VAL B 85 1796 90 -44 2259 1670 -38 C ATOM 1920 C VAL A 85 -22.913 16.409 33.448 1.00 15.07 C ANISOU 1920 C VAL B 85 1825 61 -13 2250 1649 37 C ATOM 1921 O VAL A 85 -23.945 17.086 33.578 1.00 15.99 O ANISOU 1921 O VAL B 85 1939 127 -42 2376 1757 91 O ATOM 1922 CB VAL A 85 -22.183 16.598 31.063 1.00 14.61 C ANISOU 1922 CB VAL B 85 1791 37 -65 2232 1526 -38 C ATOM 1923 CG1 VAL A 85 -20.942 17.394 31.487 1.00 15.59 C ANISOU 1923 CG1 VAL B 85 1994 66 118 2350 1579 59 C ATOM 1924 CG2 VAL A 85 -21.867 15.877 29.759 1.00 16.49 C ANISOU 1924 CG2 VAL B 85 2058 34 31 2404 1803 50 C ATOM 1925 N LYS A 86 -21.953 16.335 34.366 1.00 14.77 N ANISOU 1925 N LYS B 86 1736 92 -123 2246 1628 30 N ATOM 1926 CA LYS A 86 -21.964 17.074 35.617 1.00 14.87 C ANISOU 1926 CA LYS B 86 1938 24 -51 2205 1505 64 C ATOM 1927 C LYS A 86 -20.622 17.745 35.823 1.00 14.94 C ANISOU 1927 C LYS B 86 1996 27 -6 2176 1504 139 C ATOM 1928 O LYS A 86 -19.587 17.256 35.360 1.00 15.19 O ANISOU 1928 O LYS B 86 1896 -10 -150 2247 1627 195 O ATOM 1929 CB LYS A 86 -22.318 16.142 36.819 1.00 15.07 C ANISOU 1929 CB LYS B 86 1990 -25 -36 2265 1469 168 C ATOM 1930 CG LYS A 86 -23.688 15.570 36.688 1.00 16.33 C ANISOU 1930 CG LYS B 86 2038 -141 -3 2428 1736 -44 C ATOM 1931 CD LYS A 86 -24.123 14.773 37.901 1.00 17.06 C ANISOU 1931 CD LYS B 86 2186 -198 110 2578 1715 -32 C ATOM 1932 CE LYS A 86 -25.531 14.250 37.651 1.00 19.37 C ANISOU 1932 CE LYS B 86 2421 -294 31 3084 1853 59 C ATOM 1933 NZ LYS A 86 -26.002 13.404 38.773 1.00 20.97 N ANISOU 1933 NZ LYS B 86 2996 -561 -88 3161 1809 234 N ATOM 1934 N TRP A 87 -20.629 18.870 36.506 1.00 14.88 N ANISOU 1934 N TRP B 87 1877 33 -157 2220 1556 215 N ATOM 1935 CA TRP A 87 -19.408 19.524 36.913 1.00 15.36 C ANISOU 1935 CA TRP B 87 2011 -6 -1 2251 1572 208 C ATOM 1936 C TRP A 87 -18.690 18.680 37.926 1.00 15.64 C ANISOU 1936 C TRP B 87 1971 -37 -87 2395 1574 186 C ATOM 1937 O TRP A 87 -19.327 18.050 38.745 1.00 16.69 O ANISOU 1937 O TRP B 87 2058 -79 237 2552 1729 196 O ATOM 1938 CB TRP A 87 -19.662 20.882 37.549 1.00 16.61 C ANISOU 1938 CB TRP B 87 2298 -140 -10 2265 1747 196 C ATOM 1939 CG TRP A 87 -20.529 21.883 36.801 1.00 17.79 C ANISOU 1939 CG TRP B 87 2605 -137 47 2216 1936 170 C ATOM 1940 CD1 TRP A 87 -21.768 22.327 37.175 1.00 19.88 C ANISOU 1940 CD1 TRP B 87 2830 42 104 2535 2189 194 C ATOM 1941 CD2 TRP A 87 -20.220 22.582 35.593 1.00 19.90 C ANISOU 1941 CD2 TRP B 87 2971 -250 -139 2369 2220 42 C ATOM 1942 NE1 TRP A 87 -22.236 23.262 36.292 1.00 19.81 N ANISOU 1942 NE1 TRP B 87 2798 212 167 2492 2237 236 N ATOM 1943 CE2 TRP A 87 -21.305 23.420 35.295 1.00 17.91 C ANISOU 1943 CE2 TRP B 87 2598 -8 41 2309 1898 129 C ATOM 1944 CE3 TRP A 87 -19.128 22.587 34.743 1.00 18.45 C ANISOU 1944 CE3 TRP B 87 2732 -146 -69 2502 1775 213 C ATOM 1945 CZ2 TRP A 87 -21.323 24.266 34.190 1.00 20.75 C ANISOU 1945 CZ2 TRP B 87 3023 87 75 2506 2352 160 C ATOM 1946 CZ3 TRP A 87 -19.168 23.438 33.598 1.00 19.13 C ANISOU 1946 CZ3 TRP B 87 2667 -139 66 2406 2193 74 C ATOM 1947 CH2 TRP A 87 -20.255 24.231 33.358 1.00 20.12 C ANISOU 1947 CH2 TRP B 87 2982 -124 213 2530 2129 57 C ATOM 1948 N GLU A 88 -17.374 18.752 37.935 1.00 16.38 N ANISOU 1948 N GLU B 88 2075 -75 37 2612 1535 120 N ATOM 1949 CA GLU A 88 -16.578 18.227 39.039 1.00 17.84 C ANISOU 1949 CA GLU B 88 2302 -56 -45 2685 1788 106 C ATOM 1950 C GLU A 88 -15.471 19.216 39.334 1.00 18.57 C ANISOU 1950 C GLU B 88 2383 -154 -143 3030 1642 50 C ATOM 1951 O GLU A 88 -14.786 19.698 38.396 1.00 19.31 O ANISOU 1951 O GLU B 88 2406 -197 -18 2978 1952 47 O ATOM 1952 CB GLU A 88 -16.049 16.837 38.729 1.00 18.55 C ANISOU 1952 CB GLU B 88 2495 107 98 2755 1796 46 C ATOM 1953 CG GLU A 88 -15.229 16.228 39.863 1.00 20.35 C ANISOU 1953 CG GLU B 88 2518 92 138 2926 2285 -18 C ATOM 1954 CD GLU A 88 -15.062 14.789 39.663 1.00 22.89 C ANISOU 1954 CD GLU B 88 3117 42 199 2961 2619 87 C ATOM 1955 OE1 GLU A 88 -14.348 14.432 38.743 1.00 30.15 O ANISOU 1955 OE1 GLU B 88 4207 260 210 3633 3615 589 O ATOM 1956 OE2 GLU A 88 -15.553 13.978 40.491 1.00 32.88 O ANISOU 1956 OE2 GLU B 88 4670 -149 436 3708 4115 742 O ATOM 1957 N SER A 89 -15.243 19.472 40.609 1.00 21.24 N ANISOU 1957 N SER B 89 2836 -282 -157 3123 2110 -47 N ATOM 1958 CA SER A 89 -14.196 20.426 41.004 1.00 22.34 C ANISOU 1958 CA SER B 89 2968 -314 -167 3209 2309 -71 C ATOM 1959 C SER A 89 -14.371 21.766 40.302 1.00 22.21 C ANISOU 1959 C SER B 89 2997 -328 -231 3180 2262 65 C ATOM 1960 O SER A 89 -15.462 22.112 39.910 1.00 22.52 O ANISOU 1960 O SER B 89 3412 -417 -123 3018 2126 238 O ATOM 1961 CB SER A 89 -12.821 19.792 40.806 1.00 23.72 C ANISOU 1961 CB SER B 89 3010 -365 -45 3324 2677 -188 C ATOM 1962 OG SER A 89 -11.767 20.569 41.338 1.00 29.80 O ANISOU 1962 OG SER B 89 3561 -541 -75 4423 3335 -414 O ATOM 1963 N GLU A 90 -13.291 22.546 40.162 1.00 22.38 N ANISOU 1963 N GLU B 90 3253 -384 -228 3057 2193 241 N ATOM 1964 CA GLU A 90 -13.404 23.865 39.573 1.00 22.97 C ANISOU 1964 CA GLU B 90 3284 -190 -224 3095 2348 282 C ATOM 1965 C GLU A 90 -13.143 23.884 38.078 0.50 18.68 C ANISOU 1965 C GLU B 90 2620 -236 -269 2572 1905 433 C ATOM 1966 O GLU A 90 -13.424 24.889 37.455 0.50 18.54 O ANISOU 1966 O GLU B 90 2714 22 -458 2399 1928 208 O ATOM 1967 CB GLU A 90 -12.431 24.881 40.174 1.00 24.24 C ANISOU 1967 CB GLU B 90 3527 -302 -174 3303 2379 346 C ATOM 1968 CG GLU A 90 -11.037 24.465 40.332 1.00 29.15 C ANISOU 1968 CG GLU B 90 3932 -129 -14 3774 3368 104 C ATOM 1969 CD GLU A 90 -10.221 25.394 41.281 0.50 27.78 C ANISOU 1969 CD GLU B 90 3645 -177 -134 3620 3288 154 C ATOM 1970 OE1 GLU A 90 -10.777 26.014 42.227 0.50 29.00 O ANISOU 1970 OE1 GLU B 90 4180 -361 -179 3694 3141 -76 O ATOM 1971 OE2 GLU A 90 -8.993 25.457 41.100 0.50 34.31 O ANISOU 1971 OE2 GLU B 90 4116 -85 132 4544 4374 3 O ATOM 1972 N ASN A 91 -12.635 22.809 37.487 1.00 19.55 N ANISOU 1972 N ASN B 91 2798 -436 -253 2470 2159 452 N ATOM 1973 CA ASN A 91 -12.115 22.853 36.094 1.00 19.39 C ANISOU 1973 CA ASN B 91 2666 -265 -179 2509 2190 342 C ATOM 1974 C ASN A 91 -12.458 21.646 35.256 1.00 17.13 C ANISOU 1974 C ASN B 91 2341 -241 -159 2226 1940 451 C ATOM 1975 O ASN A 91 -11.799 21.393 34.258 1.00 17.42 O ANISOU 1975 O ASN B 91 2421 -277 -210 2222 1975 620 O ATOM 1976 CB AASN A 91 -10.585 22.876 36.259 0.50 18.97 C ANISOU 1976 CB AASN B 91 2609 -320 -170 2417 2179 344 C ATOM 1977 CG AASN A 91 -10.018 21.615 36.967 0.50 19.89 C ANISOU 1977 CG AASN B 91 2505 -214 -31 2768 2284 242 C ATOM 1978 OD1AASN A 91 -10.696 20.941 37.774 0.50 19.15 O ANISOU 1978 OD1AASN B 91 2290 -356 47 2528 2457 63 O ATOM 1979 ND2AASN A 91 -8.754 21.306 36.669 0.50 20.96 N ANISOU 1979 ND2AASN B 91 2726 -147 -158 2895 2342 -91 N ATOM 1980 N LYS A 92 -13.470 20.872 35.645 1.00 16.25 N ANISOU 1980 N LYS B 92 2173 -187 -289 2276 1725 401 N ATOM 1981 CA LYS A 92 -13.697 19.572 35.032 1.00 15.53 C ANISOU 1981 CA LYS B 92 2179 -125 -119 2157 1564 195 C ATOM 1982 C LYS A 92 -15.178 19.334 34.830 1.00 15.72 C ANISOU 1982 C LYS B 92 2123 -129 -150 2160 1689 322 C ATOM 1983 O LYS A 92 -16.057 19.906 35.533 1.00 17.73 O ANISOU 1983 O LYS B 92 2222 -234 -431 2503 2011 364 O ATOM 1984 CB LYS A 92 -13.040 18.507 35.920 1.00 17.13 C ANISOU 1984 CB LYS B 92 2341 3 -125 2435 1729 123 C ATOM 1985 CG LYS A 92 -13.048 17.109 35.452 1.00 19.22 C ANISOU 1985 CG LYS B 92 2593 -74 97 2536 2173 38 C ATOM 1986 CD LYS A 92 -12.213 16.267 36.411 1.00 22.60 C ANISOU 1986 CD LYS B 92 3033 178 125 2862 2691 -28 C ATOM 1987 CE LYS A 92 -12.372 14.824 36.098 1.00 25.67 C ANISOU 1987 CE LYS B 92 3323 513 212 3141 3290 -380 C ATOM 1988 NZ LYS A 92 -11.712 14.042 37.211 1.00 27.90 N ANISOU 1988 NZ LYS B 92 3906 267 753 3467 3225 -110 N ATOM 1989 N MET A 93 -15.465 18.472 33.876 1.00 14.23 N ANISOU 1989 N MET B 93 1857 -103 -148 1922 1628 186 N ATOM 1990 CA MET A 93 -16.795 17.899 33.677 1.00 15.15 C ANISOU 1990 CA MET B 93 1937 -66 -109 2024 1795 195 C ATOM 1991 C MET A 93 -16.647 16.413 33.472 1.00 14.80 C ANISOU 1991 C MET B 93 1846 -16 -99 2017 1758 139 C ATOM 1992 O MET A 93 -15.668 15.956 32.926 1.00 15.26 O ANISOU 1992 O MET B 93 1939 -146 -132 1995 1863 252 O ATOM 1993 CB AMET A 93 -17.551 18.559 32.568 0.60 17.11 C ANISOU 1993 CB AMET B 93 2150 -31 -141 2145 2205 42 C ATOM 1994 CG AMET A 93 -17.099 18.110 31.255 0.60 18.94 C ANISOU 1994 CG AMET B 93 2353 -97 -36 2528 2313 85 C ATOM 1995 SD AMET A 93 -17.868 18.976 29.882 0.60 20.39 S ANISOU 1995 SD AMET B 93 2447 -1 210 2676 2622 55 S ATOM 1996 CE AMET A 93 -17.106 20.596 30.039 0.60 20.87 C ANISOU 1996 CE AMET B 93 2744 58 84 2440 2746 2 C ATOM 1997 N VAL A 94 -17.645 15.677 33.946 1.00 15.05 N ANISOU 1997 N VAL B 94 1901 -87 20 2029 1788 121 N ATOM 1998 CA VAL A 94 -17.670 14.212 33.858 1.00 15.03 C ANISOU 1998 CA VAL B 94 1857 70 -10 1998 1855 107 C ATOM 1999 C VAL A 94 -18.981 13.787 33.228 1.00 15.01 C ANISOU 1999 C VAL B 94 1959 -18 22 1850 1893 115 C ATOM 2000 O VAL A 94 -20.041 14.265 33.622 1.00 16.53 O ANISOU 2000 O VAL B 94 1898 107 -176 2274 2108 112 O ATOM 2001 CB AVAL A 94 -17.578 13.530 35.238 0.50 16.56 C ANISOU 2001 CB AVAL B 94 2066 -79 99 2158 2068 83 C ATOM 2002 CG1AVAL A 94 -17.552 12.006 35.042 0.50 17.51 C ANISOU 2002 CG1AVAL B 94 2196 -70 172 2227 2227 99 C ATOM 2003 CG2AVAL A 94 -16.359 13.992 36.001 0.50 18.19 C ANISOU 2003 CG2AVAL B 94 2273 18 24 2356 2280 117 C ATOM 2004 N CYS A 95 -18.917 12.878 32.284 1.00 15.98 N ANISOU 2004 N CYS B 95 1758 23 -220 2078 2233 55 N ATOM 2005 CA CYS A 95 -20.084 12.364 31.588 1.00 16.28 C ANISOU 2005 CA CYS B 95 1772 27 -140 2092 2321 43 C ATOM 2006 C CYS A 95 -20.220 10.882 31.814 1.00 16.97 C ANISOU 2006 C CYS B 95 1913 -47 -140 2164 2371 27 C ATOM 2007 O CYS A 95 -19.310 10.112 31.514 1.00 19.11 O ANISOU 2007 O CYS B 95 2173 -36 -214 2144 2944 214 O ATOM 2008 CB CYS A 95 -19.936 12.623 30.084 1.00 16.97 C ANISOU 2008 CB CYS B 95 1852 -57 -247 2160 2434 -63 C ATOM 2009 SG CYS A 95 -21.387 12.133 29.166 1.00 19.86 S ANISOU 2009 SG CYS B 95 2184 -200 -307 3080 2283 2 S ATOM 2010 N GLU A 96 -21.380 10.495 32.326 1.00 17.33 N ANISOU 2010 N GLU B 96 1953 -117 -128 2376 2255 77 N ATOM 2011 CA GLU A 96 -21.767 9.114 32.399 1.00 18.95 C ANISOU 2011 CA GLU B 96 2291 -125 -82 2475 2434 -114 C ATOM 2012 C GLU A 96 -22.694 8.767 31.249 1.00 18.62 C ANISOU 2012 C GLU B 96 2288 -154 -110 2356 2429 -186 C ATOM 2013 O GLU A 96 -23.517 9.557 30.866 1.00 19.41 O ANISOU 2013 O GLU B 96 2441 -40 -145 2352 2582 -409 O ATOM 2014 CB GLU A 96 -22.466 8.795 33.717 1.00 20.27 C ANISOU 2014 CB GLU B 96 2573 -318 -114 2593 2535 49 C ATOM 2015 CG GLU A 96 -21.528 9.025 34.910 1.00 24.89 C ANISOU 2015 CG GLU B 96 3184 -68 -14 3156 3116 -136 C ATOM 2016 CD GLU A 96 -22.165 8.750 36.263 0.50 24.64 C ANISOU 2016 CD GLU B 96 3172 -160 -46 3236 2951 -32 C ATOM 2017 OE1 GLU A 96 -23.220 8.061 36.361 0.50 29.45 O ANISOU 2017 OE1 GLU B 96 3846 -164 143 3692 3648 -36 O ATOM 2018 OE2 GLU A 96 -21.587 9.237 37.253 0.50 30.55 O ANISOU 2018 OE2 GLU B 96 4232 -313 -22 3852 3523 -86 O ATOM 2019 N GLN A 97 -22.525 7.564 30.747 1.00 19.85 N ANISOU 2019 N GLN B 97 2564 -52 -101 2397 2579 -361 N ATOM 2020 CA GLN A 97 -23.265 7.060 29.598 1.00 20.32 C ANISOU 2020 CA GLN B 97 2643 -167 -129 2376 2699 -259 C ATOM 2021 C GLN A 97 -24.080 5.832 29.969 1.00 21.05 C ANISOU 2021 C GLN B 97 2785 -98 -20 2375 2838 -122 C ATOM 2022 O GLN A 97 -23.664 5.018 30.792 1.00 23.83 O ANISOU 2022 O GLN B 97 3069 -243 191 2596 3387 -279 O ATOM 2023 CB GLN A 97 -22.285 6.737 28.476 1.00 19.41 C ANISOU 2023 CB GLN B 97 2639 -78 -162 2272 2462 -292 C ATOM 2024 CG GLN A 97 -21.448 7.937 28.025 1.00 19.89 C ANISOU 2024 CG GLN B 97 2549 -34 1 2213 2793 -269 C ATOM 2025 CD GLN A 97 -20.537 7.638 26.834 1.00 20.61 C ANISOU 2025 CD GLN B 97 2789 -182 -135 2308 2733 -225 C ATOM 2026 OE1 GLN A 97 -19.937 6.558 26.759 1.00 22.83 O ANISOU 2026 OE1 GLN B 97 2906 42 -53 2447 3321 -52 O ATOM 2027 NE2 GLN A 97 -20.378 8.596 25.932 1.00 20.98 N ANISOU 2027 NE2 GLN B 97 2799 -86 -103 2427 2744 -314 N ATOM 2028 N LYS A 98 -25.277 5.741 29.402 1.00 21.91 N ANISOU 2028 N LYS B 98 2837 -204 -39 2425 3062 -159 N ATOM 2029 CA LYS A 98 -26.139 4.563 29.546 1.00 23.62 C ANISOU 2029 CA LYS B 98 3018 -252 -71 2728 3225 -55 C ATOM 2030 C LYS A 98 -26.638 4.159 28.172 1.00 22.91 C ANISOU 2030 C LYS B 98 2871 -304 -141 2528 3304 -119 C ATOM 2031 O LYS A 98 -27.186 4.967 27.458 1.00 22.96 O ANISOU 2031 O LYS B 98 2964 -335 -420 2686 3072 -158 O ATOM 2032 CB LYS A 98 -27.311 4.889 30.471 1.00 25.18 C ANISOU 2032 CB LYS B 98 3226 -310 -59 3058 3283 -3 C ATOM 2033 CG LYS A 98 -28.216 3.674 30.764 1.00 28.15 C ANISOU 2033 CG LYS B 98 3526 -240 30 3380 3787 7 C ATOM 2034 CD LYS A 98 -29.209 4.018 31.807 1.00 30.01 C ANISOU 2034 CD LYS B 98 3646 -217 14 3806 3949 195 C ATOM 2035 CE LYS A 98 -30.094 2.825 32.192 1.00 33.37 C ANISOU 2035 CE LYS B 98 4124 -322 134 4193 4360 186 C ATOM 2036 NZ LYS A 98 -31.352 2.767 31.401 1.00 38.62 N ANISOU 2036 NZ LYS B 98 4764 -115 -3 5082 4826 -79 N ATOM 2037 N LEU A 99 -26.466 2.889 27.819 1.00 24.29 N ANISOU 2037 N LEU B 99 2961 -150 -260 2810 3456 -154 N ATOM 2038 CA LEU A 99 -26.886 2.462 26.474 1.00 24.43 C ANISOU 2038 CA LEU B 99 3010 -166 -268 2794 3475 -163 C ATOM 2039 C LEU A 99 -28.383 2.645 26.266 1.00 25.26 C ANISOU 2039 C LEU B 99 3042 -182 -308 2892 3663 -127 C ATOM 2040 O LEU A 99 -29.148 2.429 27.199 1.00 25.64 O ANISOU 2040 O LEU B 99 2993 -322 -336 2882 3867 -197 O ATOM 2041 CB LEU A 99 -26.546 1.021 26.205 1.00 24.87 C ANISOU 2041 CB LEU B 99 3028 -145 -203 2809 3612 -103 C ATOM 2042 CG LEU A 99 -25.047 0.732 26.190 1.00 24.84 C ANISOU 2042 CG LEU B 99 3057 -4 -276 2734 3645 -75 C ATOM 2043 CD1 LEU A 99 -24.838 -0.760 26.407 1.00 28.52 C ANISOU 2043 CD1 LEU B 99 3804 76 -83 3173 3857 -78 C ATOM 2044 CD2 LEU A 99 -24.400 1.219 24.932 1.00 25.52 C ANISOU 2044 CD2 LEU B 99 3163 -56 -374 2856 3675 -107 C ATOM 2045 N LEU A 100 -28.774 3.061 25.058 1.00 25.43 N ANISOU 2045 N LEU B 100 2907 -166 -352 3010 3743 -145 N ATOM 2046 CA LEU A 100 -30.218 3.143 24.729 1.00 26.56 C ANISOU 2046 CA LEU B 100 3045 -79 -293 3224 3819 -115 C ATOM 2047 C LEU A 100 -30.871 1.793 24.696 1.00 28.13 C ANISOU 2047 C LEU B 100 3156 -90 -327 3434 4098 -90 C ATOM 2048 O LEU A 100 -32.062 1.680 24.995 1.00 29.51 O ANISOU 2048 O LEU B 100 3176 -183 -300 3668 4365 -80 O ATOM 2049 CB LEU A 100 -30.439 3.850 23.390 1.00 26.78 C ANISOU 2049 CB LEU B 100 3037 8 -306 3337 3800 -183 C ATOM 2050 CG LEU A 100 -29.920 5.272 23.237 1.00 29.47 C ANISOU 2050 CG LEU B 100 3534 50 -145 3731 3929 -93 C ATOM 2051 CD1 LEU A 100 -30.298 5.914 21.885 1.00 29.94 C ANISOU 2051 CD1 LEU B 100 3642 152 78 3653 4080 -43 C ATOM 2052 CD2 LEU A 100 -30.454 6.061 24.374 1.00 29.31 C ANISOU 2052 CD2 LEU B 100 3635 26 -249 3457 4043 -132 C ATOM 2053 N LYS A 101 -30.104 0.788 24.283 1.00 28.50 N ANISOU 2053 N LYS B 101 3217 -141 -371 3409 4204 -238 N ATOM 2054 CA LYS A 101 -30.586 -0.552 24.099 1.00 29.39 C ANISOU 2054 CA LYS B 101 3549 -115 -267 3484 4131 -109 C ATOM 2055 C LYS A 101 -29.505 -1.470 24.575 1.00 30.36 C ANISOU 2055 C LYS B 101 3740 -102 -248 3486 4309 -64 C ATOM 2056 O LYS A 101 -28.331 -1.295 24.222 1.00 30.80 O ANISOU 2056 O LYS B 101 3682 -85 -297 3474 4547 -42 O ATOM 2057 CB LYS A 101 -30.891 -0.798 22.622 1.00 30.42 C ANISOU 2057 CB LYS B 101 3799 -128 -300 3565 4194 -105 C ATOM 2058 N GLY A 102 -29.870 -2.440 25.401 1.00 31.04 N ANISOU 2058 N GLY B 102 3823 43 -124 3636 4333 -52 N ATOM 2059 CA GLY A 102 -28.944 -3.503 25.716 1.00 30.89 C ANISOU 2059 CA GLY B 102 3928 59 -158 3466 4342 -53 C ATOM 2060 C GLY A 102 -28.049 -3.115 26.857 1.00 30.82 C ANISOU 2060 C GLY B 102 3908 56 -62 3530 4272 -69 C ATOM 2061 O GLY A 102 -28.322 -2.170 27.614 1.00 31.47 O ANISOU 2061 O GLY B 102 3870 94 -126 3556 4530 -47 O ATOM 2062 N GLU A 103 -26.953 -3.832 26.963 1.00 30.28 N ANISOU 2062 N GLU B 103 3951 48 -120 3323 4228 -93 N ATOM 2063 CA GLU A 103 -26.077 -3.721 28.103 1.00 30.50 C ANISOU 2063 CA GLU B 103 4009 67 -53 3432 4147 -101 C ATOM 2064 C GLU A 103 -24.643 -3.835 27.658 1.00 29.40 C ANISOU 2064 C GLU B 103 3961 -1 -65 3198 4012 -118 C ATOM 2065 O GLU A 103 -24.340 -4.216 26.522 1.00 28.68 O ANISOU 2065 O GLU B 103 3928 26 -87 2871 4095 -235 O ATOM 2066 CB GLU A 103 -26.404 -4.839 29.094 1.00 30.56 C ANISOU 2066 CB GLU B 103 3915 -28 -11 3510 4186 -46 C ATOM 2067 CG GLU A 103 -27.782 -4.769 29.679 1.00 32.63 C ANISOU 2067 CG GLU B 103 4118 46 -82 3948 4331 -42 C ATOM 2068 CD GLU A 103 -28.042 -5.908 30.613 0.50 32.85 C ANISOU 2068 CD GLU B 103 4211 50 21 3927 4342 -27 C ATOM 2069 OE1 GLU A 103 -27.466 -5.894 31.713 0.50 37.72 O ANISOU 2069 OE1 GLU B 103 4780 40 29 4807 4745 -118 O ATOM 2070 OE2 GLU A 103 -28.811 -6.816 30.243 0.50 36.17 O ANISOU 2070 OE2 GLU B 103 4520 -48 37 4434 4788 -138 O ATOM 2071 N GLY A 104 -23.750 -3.411 28.532 1.00 29.30 N ANISOU 2071 N GLY B 104 3957 104 -20 3115 4059 -156 N ATOM 2072 CA GLY A 104 -22.363 -3.338 28.181 1.00 28.35 C ANISOU 2072 CA GLY B 104 3925 25 -27 2972 3872 -43 C ATOM 2073 C GLY A 104 -21.549 -2.799 29.339 1.00 27.60 C ANISOU 2073 C GLY B 104 3820 115 77 2891 3775 -79 C ATOM 2074 O GLY A 104 -22.062 -2.507 30.400 1.00 29.13 O ANISOU 2074 O GLY B 104 3979 200 -11 2979 4107 -17 O ATOM 2075 N PRO A 105 -20.263 -2.641 29.125 1.00 28.05 N ANISOU 2075 N PRO B 105 3882 -23 103 2932 3841 -67 N ATOM 2076 CA PRO A 105 -19.418 -2.127 30.173 1.00 27.63 C ANISOU 2076 CA PRO B 105 3813 -79 123 2931 3751 -35 C ATOM 2077 C PRO A 105 -19.792 -0.675 30.496 1.00 26.73 C ANISOU 2077 C PRO B 105 3697 -141 126 2762 3697 -120 C ATOM 2078 O PRO A 105 -20.408 0.027 29.694 1.00 27.51 O ANISOU 2078 O PRO B 105 3966 -313 109 2774 3709 -212 O ATOM 2079 CB PRO A 105 -18.052 -2.169 29.537 1.00 27.71 C ANISOU 2079 CB PRO B 105 3784 -11 87 2948 3795 -27 C ATOM 2080 CG PRO A 105 -18.343 -2.011 28.101 1.00 29.61 C ANISOU 2080 CG PRO B 105 3907 -72 114 3443 3899 105 C ATOM 2081 CD PRO A 105 -19.507 -2.875 27.888 1.00 29.28 C ANISOU 2081 CD PRO B 105 3936 -48 92 3297 3890 -62 C ATOM 2082 N LYS A 106 -19.479 -0.243 31.694 1.00 26.94 N ANISOU 2082 N LYS B 106 3747 -35 114 2829 3660 -86 N ATOM 2083 CA LYS A 106 -19.638 1.150 32.040 1.00 25.74 C ANISOU 2083 CA LYS B 106 3432 -150 179 2782 3565 -79 C ATOM 2084 C LYS A 106 -18.649 1.994 31.227 1.00 24.92 C ANISOU 2084 C LYS B 106 3102 -75 281 2842 3522 -90 C ATOM 2085 O LYS A 106 -17.446 1.735 31.177 1.00 27.25 O ANISOU 2085 O LYS B 106 3375 -21 683 3090 3889 -187 O ATOM 2086 CB LYS A 106 -19.435 1.338 33.508 1.00 26.55 C ANISOU 2086 CB LYS B 106 3459 -150 182 3067 3561 -13 C ATOM 2087 N THR A 107 -19.180 2.997 30.549 1.00 23.09 N ANISOU 2087 N THR B 107 2849 -104 201 2545 3378 -135 N ATOM 2088 CA THR A 107 -18.368 3.923 29.777 1.00 21.50 C ANISOU 2088 CA THR B 107 2717 -55 33 2380 3070 -64 C ATOM 2089 C THR A 107 -18.601 5.342 30.254 1.00 20.15 C ANISOU 2089 C THR B 107 2534 -90 -13 2303 2817 -34 C ATOM 2090 O THR A 107 -19.692 5.711 30.687 1.00 20.29 O ANISOU 2090 O THR B 107 2516 -181 32 2236 2958 20 O ATOM 2091 CB THR A 107 -18.614 3.816 28.264 1.00 21.87 C ANISOU 2091 CB THR B 107 2933 -46 -42 2315 3058 -42 C ATOM 2092 OG1 THR A 107 -19.976 4.114 27.989 1.00 22.41 O ANISOU 2092 OG1 THR B 107 2976 -57 87 2499 3038 -274 O ATOM 2093 CG2 THR A 107 -18.329 2.430 27.733 1.00 24.05 C ANISOU 2093 CG2 THR B 107 3425 -92 -200 2390 3323 -71 C ATOM 2094 N SER A 108 -17.558 6.147 30.164 1.00 18.98 N ANISOU 2094 N SER B 108 2346 -6 -115 2163 2703 142 N ATOM 2095 CA SER A 108 -17.644 7.522 30.599 1.00 18.39 C ANISOU 2095 CA SER B 108 2299 -2 -141 2128 2559 72 C ATOM 2096 C SER A 108 -16.583 8.335 29.887 1.00 17.50 C ANISOU 2096 C SER B 108 2136 27 -210 2064 2449 115 C ATOM 2097 O SER A 108 -15.653 7.798 29.293 1.00 18.34 O ANISOU 2097 O SER B 108 2253 -8 -196 2013 2702 210 O ATOM 2098 CB SER A 108 -17.465 7.600 32.111 1.00 20.37 C ANISOU 2098 CB SER B 108 2526 8 -110 2449 2763 71 C ATOM 2099 OG SER A 108 -16.269 7.012 32.517 1.00 23.98 O ANISOU 2099 OG SER B 108 3029 78 -235 3265 2815 -121 O ATOM 2100 N TRP A 109 -16.702 9.650 29.985 1.00 17.18 N ANISOU 2100 N TRP B 109 2065 -86 -200 1933 2527 184 N ATOM 2101 CA TRP A 109 -15.648 10.544 29.548 1.00 16.68 C ANISOU 2101 CA TRP B 109 2027 -1 -213 1956 2352 139 C ATOM 2102 C TRP A 109 -15.575 11.742 30.451 1.00 15.80 C ANISOU 2102 C TRP B 109 1990 0 -209 1830 2182 128 C ATOM 2103 O TRP A 109 -16.503 12.047 31.182 1.00 16.74 O ANISOU 2103 O TRP B 109 1904 -102 -267 1954 2500 312 O ATOM 2104 CB TRP A 109 -15.808 10.978 28.085 1.00 17.55 C ANISOU 2104 CB TRP B 109 2056 -157 -255 2114 2497 97 C ATOM 2105 CG TRP A 109 -17.083 11.661 27.642 1.00 17.07 C ANISOU 2105 CG TRP B 109 2021 -50 -187 2081 2384 135 C ATOM 2106 CD1 TRP A 109 -18.119 11.098 26.995 1.00 19.19 C ANISOU 2106 CD1 TRP B 109 2333 32 -263 2333 2624 108 C ATOM 2107 CD2 TRP A 109 -17.398 13.058 27.740 1.00 17.67 C ANISOU 2107 CD2 TRP B 109 2077 113 -163 2278 2359 187 C ATOM 2108 NE1 TRP A 109 -19.081 12.015 26.717 1.00 18.97 N ANISOU 2108 NE1 TRP B 109 2245 58 -202 2549 2412 -3 N ATOM 2109 CE2 TRP A 109 -18.664 13.232 27.166 1.00 18.19 C ANISOU 2109 CE2 TRP B 109 2147 -18 -74 2293 2470 156 C ATOM 2110 CE3 TRP A 109 -16.763 14.162 28.307 1.00 18.83 C ANISOU 2110 CE3 TRP B 109 2133 32 -44 2244 2778 119 C ATOM 2111 CZ2 TRP A 109 -19.296 14.492 27.119 1.00 18.79 C ANISOU 2111 CZ2 TRP B 109 2111 119 -75 2505 2524 65 C ATOM 2112 CZ3 TRP A 109 -17.398 15.389 28.275 1.00 18.60 C ANISOU 2112 CZ3 TRP B 109 2149 -51 46 2163 2752 197 C ATOM 2113 CH2 TRP A 109 -18.655 15.539 27.693 1.00 18.96 C ANISOU 2113 CH2 TRP B 109 2187 74 -25 2287 2729 324 C ATOM 2114 N THR A 110 -14.434 12.408 30.400 1.00 15.07 N ANISOU 2114 N THR B 110 1902 40 -246 1817 2004 214 N ATOM 2115 CA THR A 110 -14.220 13.630 31.163 1.00 15.51 C ANISOU 2115 CA THR B 110 2059 27 -160 1848 1984 183 C ATOM 2116 C THR A 110 -13.470 14.652 30.303 1.00 14.41 C ANISOU 2116 C THR B 110 1822 17 -235 1745 1908 258 C ATOM 2117 O THR A 110 -12.736 14.306 29.399 1.00 15.51 O ANISOU 2117 O THR B 110 2055 74 -235 1823 2016 365 O ATOM 2118 CB THR A 110 -13.386 13.389 32.429 1.00 16.35 C ANISOU 2118 CB THR B 110 2276 -36 -267 1904 2030 284 C ATOM 2119 OG1 THR A 110 -12.032 13.082 32.088 1.00 17.58 O ANISOU 2119 OG1 THR B 110 2178 181 8 2245 2255 89 O ATOM 2120 CG2 THR A 110 -13.964 12.285 33.308 1.00 17.21 C ANISOU 2120 CG2 THR B 110 2269 66 90 2130 2137 46 C ATOM 2121 N LEU A 111 -13.661 15.914 30.653 1.00 14.23 N ANISOU 2121 N LEU B 111 1805 62 -163 1702 1897 282 N ATOM 2122 CA LEU A 111 -12.874 17.036 30.108 1.00 15.00 C ANISOU 2122 CA LEU B 111 1972 8 -148 1834 1891 238 C ATOM 2123 C LEU A 111 -12.399 17.884 31.267 1.00 14.64 C ANISOU 2123 C LEU B 111 2033 -32 -108 1688 1838 312 C ATOM 2124 O LEU A 111 -13.172 18.209 32.170 1.00 16.00 O ANISOU 2124 O LEU B 111 2212 -122 -213 1933 1934 502 O ATOM 2125 CB LEU A 111 -13.711 17.924 29.195 1.00 15.85 C ANISOU 2125 CB LEU B 111 2115 158 94 1997 1908 245 C ATOM 2126 CG LEU A 111 -14.061 17.316 27.852 1.00 16.95 C ANISOU 2126 CG LEU B 111 2154 137 54 2136 2150 28 C ATOM 2127 CD1 LEU A 111 -14.987 18.248 27.066 1.00 18.50 C ANISOU 2127 CD1 LEU B 111 2399 192 46 2492 2138 -68 C ATOM 2128 CD2 LEU A 111 -12.839 17.057 26.975 1.00 16.63 C ANISOU 2128 CD2 LEU B 111 2531 158 -101 1985 1800 87 C ATOM 2129 N GLU A 112 -11.149 18.291 31.240 1.00 15.61 N ANISOU 2129 N GLU B 112 2159 -130 -280 1882 1888 344 N ATOM 2130 CA GLU A 112 -10.546 19.065 32.312 1.00 17.16 C ANISOU 2130 CA GLU B 112 2402 -266 -262 2146 1970 331 C ATOM 2131 C GLU A 112 -9.590 20.102 31.761 1.00 16.35 C ANISOU 2131 C GLU B 112 2306 -191 -312 2006 1898 392 C ATOM 2132 O GLU A 112 -8.772 19.815 30.896 1.00 17.67 O ANISOU 2132 O GLU B 112 2455 -192 -304 2082 2177 631 O ATOM 2133 CB GLU A 112 -9.753 18.160 33.267 1.00 18.78 C ANISOU 2133 CB GLU B 112 2609 -307 -253 2325 2201 179 C ATOM 2134 CG AGLU A 112 -9.241 18.878 34.508 0.50 20.32 C ANISOU 2134 CG AGLU B 112 2791 -171 -179 2551 2378 8 C ATOM 2135 CD AGLU A 112 -7.988 18.264 35.038 0.50 22.42 C ANISOU 2135 CD AGLU B 112 2843 -174 -182 2945 2731 67 C ATOM 2136 OE1AGLU A 112 -7.851 17.037 34.957 0.50 26.52 O ANISOU 2136 OE1AGLU B 112 3458 -40 -243 3204 3414 -23 O ATOM 2137 OE2AGLU A 112 -7.170 19.015 35.608 0.50 28.92 O ANISOU 2137 OE2AGLU B 112 3650 -490 -293 3824 3514 -404 O ATOM 2138 N LEU A 113 -9.676 21.315 32.291 1.00 16.95 N ANISOU 2138 N LEU B 113 2389 -291 -424 1972 2079 503 N ATOM 2139 CA LEU A 113 -8.768 22.403 31.954 1.00 17.19 C ANISOU 2139 CA LEU B 113 2377 -274 -227 2134 2021 315 C ATOM 2140 C LEU A 113 -7.619 22.458 32.960 1.00 17.95 C ANISOU 2140 C LEU B 113 2453 -305 -223 2286 2080 212 C ATOM 2141 O LEU A 113 -7.821 22.554 34.174 1.00 20.26 O ANISOU 2141 O LEU B 113 2726 -326 -217 2891 2079 326 O ATOM 2142 CB LEU A 113 -9.512 23.739 32.016 1.00 17.88 C ANISOU 2142 CB LEU B 113 2444 -246 -214 2068 2282 231 C ATOM 2143 CG LEU A 113 -10.627 23.817 31.017 1.00 17.55 C ANISOU 2143 CG LEU B 113 2221 -40 -73 2138 2309 159 C ATOM 2144 CD1 LEU A 113 -11.655 24.826 31.476 1.00 20.61 C ANISOU 2144 CD1 LEU B 113 2473 126 -312 2691 2665 -46 C ATOM 2145 CD2 LEU A 113 -10.104 24.117 29.622 1.00 19.13 C ANISOU 2145 CD2 LEU B 113 2492 55 49 2348 2426 73 C ATOM 2146 N THR A 114 -6.406 22.482 32.453 1.00 19.22 N ANISOU 2146 N THR B 114 2509 -345 -262 2706 2084 247 N ATOM 2147 CA THR A 114 -5.243 22.597 33.342 1.00 20.42 C ANISOU 2147 CA THR B 114 2739 -296 -183 2669 2349 0 C ATOM 2148 C THR A 114 -4.950 24.078 33.584 1.00 22.76 C ANISOU 2148 C THR B 114 3048 -271 -332 3029 2571 -3 C ATOM 2149 O THR A 114 -5.486 24.952 32.923 1.00 22.69 O ANISOU 2149 O THR B 114 3307 -249 -620 2686 2627 98 O ATOM 2150 CB THR A 114 -4.007 21.988 32.754 1.00 21.23 C ANISOU 2150 CB THR B 114 2862 -262 -122 2772 2430 -100 C ATOM 2151 OG1 THR A 114 -3.541 22.807 31.689 1.00 20.21 O ANISOU 2151 OG1 THR B 114 2580 -378 -185 2730 2367 55 O ATOM 2152 CG2 THR A 114 -4.258 20.579 32.271 1.00 21.73 C ANISOU 2152 CG2 THR B 114 2953 -249 -78 2760 2541 -40 C ATOM 2153 N ASN A 115 -4.036 24.347 34.515 1.00 25.00 N ANISOU 2153 N ASN B 115 3271 -309 -293 3315 2911 -157 N ATOM 2154 CA ASN A 115 -3.649 25.728 34.820 1.00 26.10 C ANISOU 2154 CA ASN B 115 3499 -342 -291 3332 3084 -118 C ATOM 2155 C ASN A 115 -2.713 26.344 33.788 1.00 27.47 C ANISOU 2155 C ASN B 115 3695 -390 -295 3405 3335 -81 C ATOM 2156 O ASN A 115 -2.344 27.531 33.916 1.00 30.71 O ANISOU 2156 O ASN B 115 4353 -507 -328 3483 3830 -6 O ATOM 2157 CB ASN A 115 -3.030 25.811 36.209 1.00 27.18 C ANISOU 2157 CB ASN B 115 3698 -356 -284 3542 3087 -95 C ATOM 2158 N ASP A 116 -2.304 25.575 32.791 1.00 25.70 N ANISOU 2158 N ASP B 116 3327 -396 -335 3372 3064 -45 N ATOM 2159 CA ASP A 116 -1.349 26.043 31.779 1.00 26.12 C ANISOU 2159 CA ASP B 116 3405 -277 -153 3289 3228 -62 C ATOM 2160 C ASP A 116 -1.909 25.954 30.358 1.00 25.42 C ANISOU 2160 C ASP B 116 3318 -211 -192 3162 3179 -12 C ATOM 2161 O ASP A 116 -1.169 25.763 29.386 1.00 27.95 O ANISOU 2161 O ASP B 116 3421 -231 -79 3742 3456 62 O ATOM 2162 CB ASP A 116 0.011 25.326 31.887 1.00 28.08 C ANISOU 2162 CB ASP B 116 3593 -213 -151 3668 3406 -64 C ATOM 2163 CG ASP A 116 -0.074 23.821 32.131 0.50 29.38 C ANISOU 2163 CG ASP B 116 3660 -135 -69 3768 3734 -57 C ATOM 2164 OD1 ASP A 116 -0.817 23.080 31.437 0.50 29.26 O ANISOU 2164 OD1 ASP B 116 3228 -69 -74 4149 3739 -112 O ATOM 2165 OD2 ASP A 116 0.686 23.355 33.010 0.50 34.66 O ANISOU 2165 OD2 ASP B 116 3933 -65 -39 4703 4532 -141 O ATOM 2166 N GLY A 117 -3.227 26.060 30.232 1.00 23.27 N ANISOU 2166 N GLY B 117 3172 -148 -287 2627 3043 0 N ATOM 2167 CA GLY A 117 -3.832 26.186 28.937 1.00 22.24 C ANISOU 2167 CA GLY B 117 3132 -157 -147 2307 3009 -34 C ATOM 2168 C GLY A 117 -4.122 24.903 28.187 1.00 20.87 C ANISOU 2168 C GLY B 117 2978 -142 -119 2190 2760 -120 C ATOM 2169 O GLY A 117 -4.293 24.958 26.979 1.00 23.46 O ANISOU 2169 O GLY B 117 3715 -315 199 2249 2947 -308 O ATOM 2170 N GLU A 118 -4.122 23.749 28.836 1.00 17.87 N ANISOU 2170 N GLU B 118 2448 -137 -127 2049 2292 6 N ATOM 2171 CA GLU A 118 -4.412 22.516 28.123 1.00 16.40 C ANISOU 2171 CA GLU B 118 2206 -61 -95 1945 2079 50 C ATOM 2172 C GLU A 118 -5.796 22.034 28.459 1.00 15.96 C ANISOU 2172 C GLU B 118 2112 -31 -101 1969 1983 194 C ATOM 2173 O GLU A 118 -6.370 22.388 29.528 1.00 16.83 O ANISOU 2173 O GLU B 118 2063 -170 -193 2363 1966 218 O ATOM 2174 CB GLU A 118 -3.408 21.442 28.498 1.00 16.50 C ANISOU 2174 CB GLU B 118 2036 -32 -17 2073 2157 64 C ATOM 2175 CG GLU A 118 -2.001 21.794 28.019 1.00 18.59 C ANISOU 2175 CG GLU B 118 2180 19 49 2511 2371 73 C ATOM 2176 CD GLU A 118 -0.999 20.746 28.311 1.00 19.78 C ANISOU 2176 CD GLU B 118 2353 39 293 2721 2437 92 C ATOM 2177 OE1 GLU A 118 -1.148 19.975 29.254 1.00 22.14 O ANISOU 2177 OE1 GLU B 118 2635 397 318 2954 2820 198 O ATOM 2178 OE2 GLU A 118 -0.014 20.687 27.524 1.00 24.44 O ANISOU 2178 OE2 GLU B 118 2565 342 294 3709 3010 331 O ATOM 2179 N LEU A 119 -6.325 21.210 27.591 1.00 15.43 N ANISOU 2179 N LEU B 119 1977 -81 -43 1914 1969 254 N ATOM 2180 CA LEU A 119 -7.571 20.508 27.776 1.00 14.65 C ANISOU 2180 CA LEU B 119 1941 -93 -5 1749 1873 284 C ATOM 2181 C LEU A 119 -7.241 19.014 27.765 1.00 14.69 C ANISOU 2181 C LEU B 119 1922 -23 -43 1907 1752 200 C ATOM 2182 O LEU A 119 -6.650 18.529 26.799 1.00 15.45 O ANISOU 2182 O LEU B 119 2222 62 -73 1887 1762 301 O ATOM 2183 CB LEU A 119 -8.543 20.811 26.671 1.00 15.49 C ANISOU 2183 CB LEU B 119 1951 -114 -91 1831 2104 242 C ATOM 2184 CG LEU A 119 -9.901 20.113 26.692 1.00 16.17 C ANISOU 2184 CG LEU B 119 2024 -148 153 1898 2222 98 C ATOM 2185 CD1 LEU A 119 -10.740 20.610 27.825 1.00 17.97 C ANISOU 2185 CD1 LEU B 119 2073 -12 175 2169 2585 262 C ATOM 2186 CD2 LEU A 119 -10.586 20.283 25.356 1.00 18.98 C ANISOU 2186 CD2 LEU B 119 2115 -56 198 2374 2723 19 C ATOM 2187 N ILE A 120 -7.598 18.321 28.834 1.00 14.79 N ANISOU 2187 N ILE B 120 2068 0 -12 1827 1721 247 N ATOM 2188 CA ILE A 120 -7.392 16.905 28.927 1.00 14.52 C ANISOU 2188 CA ILE B 120 1996 -5 -52 1762 1757 245 C ATOM 2189 C ILE A 120 -8.729 16.200 28.775 1.00 14.39 C ANISOU 2189 C ILE B 120 2062 21 -81 1572 1831 172 C ATOM 2190 O ILE A 120 -9.669 16.496 29.531 1.00 15.11 O ANISOU 2190 O ILE B 120 2054 -63 -93 1845 1842 355 O ATOM 2191 CB AILE A 120 -6.797 16.470 30.277 0.50 16.42 C ANISOU 2191 CB AILE B 120 2224 37 17 1990 2022 130 C ATOM 2192 CG1AILE A 120 -5.695 17.409 30.715 0.50 17.30 C ANISOU 2192 CG1AILE B 120 2396 211 -22 2016 2162 -84 C ATOM 2193 CG2AILE A 120 -6.301 15.034 30.191 0.50 16.36 C ANISOU 2193 CG2AILE B 120 2230 13 77 2040 1945 -11 C ATOM 2194 CD1AILE A 120 -4.643 17.488 29.706 0.50 19.47 C ANISOU 2194 CD1AILE B 120 2786 76 68 2215 2396 -12 C ATOM 2195 N GLU A 121 -8.815 15.280 27.836 1.00 14.46 N ANISOU 2195 N GLU B 121 1928 13 29 1757 1806 310 N ATOM 2196 CA GLU A 121 -9.974 14.417 27.680 1.00 14.85 C ANISOU 2196 CA GLU B 121 2001 38 55 1797 1843 230 C ATOM 2197 C GLU A 121 -9.589 13.017 28.136 1.00 15.32 C ANISOU 2197 C GLU B 121 2114 51 -136 1715 1991 336 C ATOM 2198 O GLU A 121 -8.540 12.519 27.762 1.00 15.68 O ANISOU 2198 O GLU B 121 2071 137 14 1756 2130 405 O ATOM 2199 CB GLU A 121 -10.392 14.342 26.229 1.00 16.42 C ANISOU 2199 CB GLU B 121 2192 78 -36 2065 1981 134 C ATOM 2200 CG GLU A 121 -11.620 13.478 26.003 1.00 18.16 C ANISOU 2200 CG GLU B 121 2427 -5 50 2179 2291 30 C ATOM 2201 CD GLU A 121 -12.010 13.356 24.574 1.00 23.01 C ANISOU 2201 CD GLU B 121 2811 -250 27 3176 2756 -190 C ATOM 2202 OE1 GLU A 121 -11.213 13.633 23.663 1.00 29.33 O ANISOU 2202 OE1 GLU B 121 3955 -501 -108 4369 2819 -364 O ATOM 2203 OE2 GLU A 121 -13.141 12.872 24.364 1.00 32.19 O ANISOU 2203 OE2 GLU B 121 3463 -460 -56 4669 4096 -666 O ATOM 2204 N THR A 122 -10.456 12.382 28.915 1.00 14.98 N ANISOU 2204 N THR B 122 2169 38 -48 1608 1915 288 N ATOM 2205 CA THR A 122 -10.340 10.980 29.128 1.00 15.98 C ANISOU 2205 CA THR B 122 2082 81 -91 1812 2175 225 C ATOM 2206 C THR A 122 -11.592 10.278 28.703 1.00 15.53 C ANISOU 2206 C THR B 122 1883 -28 -13 1817 2199 292 C ATOM 2207 O THR A 122 -12.690 10.829 28.716 1.00 16.38 O ANISOU 2207 O THR B 122 2064 35 -104 1840 2319 279 O ATOM 2208 CB THR A 122 -9.994 10.581 30.556 1.00 16.63 C ANISOU 2208 CB THR B 122 2225 205 -2 1921 2172 241 C ATOM 2209 OG1 THR A 122 -11.113 10.700 31.434 1.00 18.63 O ANISOU 2209 OG1 THR B 122 2518 130 15 2273 2284 153 O ATOM 2210 CG2 THR A 122 -8.838 11.383 31.093 1.00 18.38 C ANISOU 2210 CG2 THR B 122 2499 148 173 2336 2149 76 C ATOM 2211 N MET A 123 -11.402 9.025 28.315 1.00 15.87 N ANISOU 2211 N MET B 123 2019 13 -99 1726 2283 343 N ATOM 2212 CA MET A 123 -12.490 8.115 27.987 1.00 17.08 C ANISOU 2212 CA MET B 123 2187 97 -143 1909 2392 261 C ATOM 2213 C MET A 123 -12.159 6.788 28.639 1.00 17.43 C ANISOU 2213 C MET B 123 2268 -9 -154 1902 2451 214 C ATOM 2214 O MET A 123 -11.046 6.288 28.467 1.00 18.14 O ANISOU 2214 O MET B 123 2385 103 -62 1753 2751 352 O ATOM 2215 CB MET A 123 -12.638 7.890 26.489 1.00 18.19 C ANISOU 2215 CB MET B 123 2299 95 -104 1995 2614 244 C ATOM 2216 CG MET A 123 -13.009 9.138 25.709 1.00 20.58 C ANISOU 2216 CG MET B 123 2808 334 -144 2637 2373 167 C ATOM 2217 SD MET A 123 -13.279 8.815 23.980 1.00 25.87 S ANISOU 2217 SD MET B 123 3671 580 -126 3459 2698 -99 S ATOM 2218 CE MET A 123 -11.612 8.528 23.491 1.00 26.98 C ANISOU 2218 CE MET B 123 3475 129 -69 3573 3200 20 C ATOM 2219 N THR A 124 -13.111 6.215 29.343 1.00 17.91 N ANISOU 2219 N THR B 124 2388 -19 -102 1848 2565 186 N ATOM 2220 CA THR A 124 -12.860 5.008 30.143 1.00 19.69 C ANISOU 2220 CA THR B 124 2624 -60 -63 2079 2776 201 C ATOM 2221 C THR A 124 -13.854 3.924 29.902 1.00 20.27 C ANISOU 2221 C THR B 124 2613 -5 -136 1987 3098 323 C ATOM 2222 O THR A 124 -15.054 4.188 29.787 1.00 23.61 O ANISOU 2222 O THR B 124 2789 -214 -177 2120 4059 210 O ATOM 2223 CB THR A 124 -12.919 5.371 31.633 1.00 20.51 C ANISOU 2223 CB THR B 124 2684 -69 -45 2315 2792 285 C ATOM 2224 OG1 THR A 124 -11.982 6.415 31.920 1.00 20.91 O ANISOU 2224 OG1 THR B 124 3211 17 -128 2266 2465 243 O ATOM 2225 CG2 THR A 124 -12.643 4.183 32.561 1.00 22.98 C ANISOU 2225 CG2 THR B 124 3235 4 136 2603 2892 121 C ATOM 2226 N ALA A 125 -13.362 2.694 29.884 1.00 20.54 N ANISOU 2226 N ALA B 125 2838 -110 -8 2017 2947 345 N ATOM 2227 CA ALA A 125 -14.202 1.497 30.009 1.00 22.02 C ANISOU 2227 CA ALA B 125 3089 -168 -45 2238 3039 224 C ATOM 2228 C ALA A 125 -13.316 0.339 30.466 1.00 22.18 C ANISOU 2228 C ALA B 125 3140 -172 180 2109 3175 342 C ATOM 2229 O ALA A 125 -12.190 0.262 30.041 1.00 22.33 O ANISOU 2229 O ALA B 125 3373 -2 245 1934 3177 335 O ATOM 2230 CB ALA A 125 -14.781 1.147 28.714 1.00 23.09 C ANISOU 2230 CB ALA B 125 3249 -141 188 2388 3133 80 C ATOM 2231 N ASP A 126 -13.863 -0.670 31.164 1.00 24.31 N ANISOU 2231 N ASP B 126 3520 -95 182 2512 3203 392 N ATOM 2232 CA ASP A 126 -13.164 -1.968 31.350 1.00 26.17 C ANISOU 2232 CA ASP B 126 3655 -65 218 2923 3365 233 C ATOM 2233 C ASP A 126 -11.749 -1.776 31.933 1.00 27.72 C ANISOU 2233 C ASP B 126 3827 -25 278 3229 3475 160 C ATOM 2234 O ASP A 126 -10.797 -2.492 31.560 1.00 30.98 O ANISOU 2234 O ASP B 126 4044 17 232 3664 4062 146 O ATOM 2235 CB ASP A 126 -13.093 -2.749 30.014 1.00 26.10 C ANISOU 2235 CB ASP B 126 3671 -67 168 2760 3483 315 C ATOM 2236 CG ASP A 126 -14.464 -3.218 29.503 0.50 23.49 C ANISOU 2236 CG ASP B 126 3492 140 -25 2460 2974 103 C ATOM 2237 OD1 ASP A 126 -15.250 -3.708 30.321 0.50 23.59 O ANISOU 2237 OD1 ASP B 126 3371 149 -221 2386 3206 244 O ATOM 2238 OD2 ASP A 126 -14.730 -3.180 28.273 0.50 22.85 O ANISOU 2238 OD2 ASP B 126 3510 204 281 2104 3067 318 O ATOM 2239 N ASP A 127 -11.569 -0.783 32.791 1.00 27.92 N ANISOU 2239 N ASP B 127 3837 -47 419 3383 3388 32 N ATOM 2240 CA ASP A 127 -10.265 -0.517 33.398 1.00 27.80 C ANISOU 2240 CA ASP B 127 3805 -20 365 3370 3386 -12 C ATOM 2241 C ASP A 127 -9.186 0.038 32.483 1.00 27.30 C ANISOU 2241 C ASP B 127 3697 -34 381 3377 3297 -128 C ATOM 2242 O ASP A 127 -7.998 0.078 32.862 1.00 29.51 O ANISOU 2242 O ASP B 127 3949 -74 660 3756 3506 -216 O ATOM 2243 CB ASP A 127 -9.768 -1.765 34.084 1.00 29.30 C ANISOU 2243 CB ASP B 127 4025 -8 456 3610 3496 -71 C ATOM 2244 N VAL A 128 -9.597 0.520 31.309 1.00 23.17 N ANISOU 2244 N VAL B 128 3396 64 352 2613 2791 -124 N ATOM 2245 CA VAL A 128 -8.701 1.156 30.342 1.00 21.67 C ANISOU 2245 CA VAL B 128 3167 171 126 2376 2688 -59 C ATOM 2246 C VAL A 128 -9.140 2.599 30.252 1.00 18.98 C ANISOU 2246 C VAL B 128 2902 163 141 2080 2229 -15 C ATOM 2247 O VAL A 128 -10.324 2.884 30.049 1.00 19.38 O ANISOU 2247 O VAL B 128 2886 65 -30 2030 2446 55 O ATOM 2248 CB VAL A 128 -8.724 0.445 28.953 1.00 21.07 C ANISOU 2248 CB VAL B 128 3167 154 38 2206 2633 -91 C ATOM 2249 CG1 VAL A 128 -7.857 1.169 27.937 1.00 21.54 C ANISOU 2249 CG1 VAL B 128 3131 128 -223 2496 2557 11 C ATOM 2250 CG2 VAL A 128 -8.241 -0.990 29.095 1.00 24.92 C ANISOU 2250 CG2 VAL B 128 3425 254 -93 2616 3426 -147 C ATOM 2251 N VAL A 129 -8.147 3.454 30.304 1.00 18.74 N ANISOU 2251 N VAL B 129 2792 266 141 2083 2244 36 N ATOM 2252 CA VAL A 129 -8.335 4.894 30.165 1.00 18.16 C ANISOU 2252 CA VAL B 129 2753 167 44 1943 2202 212 C ATOM 2253 C VAL A 129 -7.565 5.395 28.955 1.00 17.83 C ANISOU 2253 C VAL B 129 2652 258 19 1979 2142 250 C ATOM 2254 O VAL A 129 -6.335 5.242 28.869 1.00 18.46 O ANISOU 2254 O VAL B 129 2583 269 115 2150 2279 247 O ATOM 2255 CB VAL A 129 -7.877 5.659 31.406 1.00 19.44 C ANISOU 2255 CB VAL B 129 2816 134 -15 2226 2345 131 C ATOM 2256 CG1 VAL A 129 -8.203 7.142 31.287 1.00 20.10 C ANISOU 2256 CG1 VAL B 129 3104 -25 -84 2129 2403 386 C ATOM 2257 CG2 VAL A 129 -8.541 5.114 32.663 1.00 20.23 C ANISOU 2257 CG2 VAL B 129 3191 108 -3 2427 2066 47 C ATOM 2258 N CYS A 130 -8.275 5.990 28.012 1.00 16.41 N ANISOU 2258 N CYS B 130 2204 188 -24 1869 2160 231 N ATOM 2259 CA CYS A 130 -7.676 6.714 26.916 1.00 15.85 C ANISOU 2259 CA CYS B 130 2081 225 15 1823 2118 204 C ATOM 2260 C CYS A 130 -7.590 8.184 27.331 1.00 15.80 C ANISOU 2260 C CYS B 130 2029 204 -14 1806 2165 92 C ATOM 2261 O CYS A 130 -8.551 8.715 27.849 1.00 16.35 O ANISOU 2261 O CYS B 130 2102 156 -53 1820 2287 257 O ATOM 2262 CB CYS A 130 -8.558 6.549 25.698 1.00 16.86 C ANISOU 2262 CB CYS B 130 2322 174 -79 1771 2311 175 C ATOM 2263 SG CYS A 130 -8.123 7.664 24.319 1.00 17.79 S ANISOU 2263 SG CYS B 130 2471 196 -2 2090 2197 142 S ATOM 2264 N THR A 131 -6.406 8.768 27.182 1.00 15.43 N ANISOU 2264 N THR B 131 1994 214 -78 1784 2085 233 N ATOM 2265 CA THR A 131 -6.186 10.167 27.492 1.00 14.93 C ANISOU 2265 CA THR B 131 1993 216 -76 1737 1943 149 C ATOM 2266 C THR A 131 -5.727 10.898 26.243 1.00 15.39 C ANISOU 2266 C THR B 131 2140 183 -34 1782 1922 259 C ATOM 2267 O THR A 131 -4.828 10.450 25.548 1.00 16.59 O ANISOU 2267 O THR B 131 2225 263 -57 1923 2153 368 O ATOM 2268 CB THR A 131 -5.135 10.326 28.611 1.00 17.22 C ANISOU 2268 CB THR B 131 2350 135 0 1981 2210 128 C ATOM 2269 OG1 THR A 131 -5.604 9.634 29.775 1.00 19.02 O ANISOU 2269 OG1 THR B 131 2667 89 73 2538 2020 -118 O ATOM 2270 CG2 THR A 131 -4.875 11.781 28.937 1.00 18.30 C ANISOU 2270 CG2 THR B 131 2505 111 -31 2153 2296 42 C ATOM 2271 N LYS A 132 -6.334 12.069 25.993 1.00 14.86 N ANISOU 2271 N LYS B 132 2043 145 -31 1727 1876 233 N ATOM 2272 CA LYS A 132 -5.946 12.966 24.894 1.00 15.56 C ANISOU 2272 CA LYS B 132 2005 147 0 1912 1996 213 C ATOM 2273 C LYS A 132 -5.721 14.343 25.488 1.00 14.82 C ANISOU 2273 C LYS B 132 1993 180 -30 1754 1881 246 C ATOM 2274 O LYS A 132 -6.483 14.783 26.329 1.00 16.51 O ANISOU 2274 O LYS B 132 2169 -4 -117 1847 2254 630 O ATOM 2275 CB LYS A 132 -7.030 12.994 23.832 1.00 16.54 C ANISOU 2275 CB LYS B 132 2190 92 70 2099 1993 234 C ATOM 2276 CG LYS A 132 -7.242 11.600 23.174 1.00 18.52 C ANISOU 2276 CG LYS B 132 2511 -158 141 2317 2207 58 C ATOM 2277 CD LYS A 132 -8.364 11.582 22.176 1.00 22.77 C ANISOU 2277 CD LYS B 132 2910 -189 118 2829 2911 -68 C ATOM 2278 CE LYS A 132 -8.615 10.227 21.562 1.00 26.19 C ANISOU 2278 CE LYS B 132 3543 -262 -102 3345 3061 -256 C ATOM 2279 NZ LYS A 132 -9.427 10.229 20.273 1.00 31.12 N ANISOU 2279 NZ LYS B 132 3852 -246 23 4261 3708 -501 N ATOM 2280 N VAL A 133 -4.659 15.004 25.050 1.00 14.21 N ANISOU 2280 N VAL B 133 1864 180 54 1733 1801 267 N ATOM 2281 CA VAL A 133 -4.303 16.326 25.529 1.00 14.27 C ANISOU 2281 CA VAL B 133 1863 177 45 1844 1714 162 C ATOM 2282 C VAL A 133 -4.339 17.273 24.343 1.00 13.88 C ANISOU 2282 C VAL B 133 1866 90 19 1729 1680 117 C ATOM 2283 O VAL A 133 -3.770 16.966 23.297 1.00 14.51 O ANISOU 2283 O VAL B 133 1944 214 86 1892 1676 254 O ATOM 2284 CB VAL A 133 -2.939 16.325 26.200 1.00 15.72 C ANISOU 2284 CB VAL B 133 2002 8 98 1897 2071 -28 C ATOM 2285 CG1 VAL A 133 -2.615 17.672 26.781 1.00 18.01 C ANISOU 2285 CG1 VAL B 133 2173 -117 224 2299 2368 -222 C ATOM 2286 CG2 VAL A 133 -2.932 15.272 27.307 1.00 17.74 C ANISOU 2286 CG2 VAL B 133 2401 22 324 2212 2126 -219 C ATOM 2287 N PHE A 134 -4.967 18.426 24.544 1.00 14.25 N ANISOU 2287 N PHE B 134 2032 81 91 1761 1621 247 N ATOM 2288 CA PHE A 134 -5.144 19.439 23.526 1.00 14.54 C ANISOU 2288 CA PHE B 134 1979 105 35 1869 1674 169 C ATOM 2289 C PHE A 134 -4.668 20.814 24.035 1.00 14.64 C ANISOU 2289 C PHE B 134 2019 149 82 1789 1754 175 C ATOM 2290 O PHE A 134 -4.643 21.083 25.242 1.00 15.09 O ANISOU 2290 O PHE B 134 2045 37 103 1919 1770 221 O ATOM 2291 CB PHE A 134 -6.618 19.594 23.127 1.00 14.57 C ANISOU 2291 CB PHE B 134 1949 93 159 1889 1697 157 C ATOM 2292 CG PHE A 134 -7.330 18.350 22.714 1.00 14.95 C ANISOU 2292 CG PHE B 134 1988 208 52 1951 1740 175 C ATOM 2293 CD1 PHE A 134 -7.819 17.445 23.654 1.00 15.49 C ANISOU 2293 CD1 PHE B 134 1998 84 203 1953 1932 217 C ATOM 2294 CD2 PHE A 134 -7.563 18.098 21.386 1.00 16.52 C ANISOU 2294 CD2 PHE B 134 1939 76 91 2286 2050 73 C ATOM 2295 CE1 PHE A 134 -8.500 16.320 23.231 1.00 17.28 C ANISOU 2295 CE1 PHE B 134 2190 -4 333 2208 2168 85 C ATOM 2296 CE2 PHE A 134 -8.197 16.956 20.976 1.00 17.36 C ANISOU 2296 CE2 PHE B 134 2163 91 -84 2537 1897 -19 C ATOM 2297 CZ PHE A 134 -8.668 16.073 21.905 1.00 17.87 C ANISOU 2297 CZ PHE B 134 2155 -76 11 2222 2411 85 C ATOM 2298 N VAL A 135 -4.363 21.701 23.080 1.00 15.55 N ANISOU 2298 N VAL B 135 2265 112 129 1921 1721 103 N ATOM 2299 CA VAL A 135 -4.102 23.106 23.340 1.00 15.73 C ANISOU 2299 CA VAL B 135 2156 -6 29 1953 1867 126 C ATOM 2300 C VAL A 135 -4.993 23.950 22.428 1.00 15.10 C ANISOU 2300 C VAL B 135 2070 9 33 1825 1843 161 C ATOM 2301 O VAL A 135 -5.434 23.474 21.386 1.00 15.29 O ANISOU 2301 O VAL B 135 2237 41 61 1678 1892 204 O ATOM 2302 CB VAL A 135 -2.632 23.498 23.133 1.00 17.52 C ANISOU 2302 CB VAL B 135 2314 -99 195 2166 2177 73 C ATOM 2303 CG1 VAL A 135 -1.761 22.735 24.100 1.00 19.05 C ANISOU 2303 CG1 VAL B 135 2361 74 340 2461 2415 118 C ATOM 2304 CG2 VAL A 135 -2.200 23.291 21.704 1.00 17.55 C ANISOU 2304 CG2 VAL B 135 2127 -9 336 2225 2314 113 C ATOM 2305 N ARG A 136 -5.240 25.190 22.826 1.00 15.74 N ANISOU 2305 N ARG B 136 2301 -6 75 1826 1853 128 N ATOM 2306 CA ARG A 136 -6.012 26.072 21.940 1.00 16.55 C ANISOU 2306 CA ARG B 136 2432 56 43 1801 2052 245 C ATOM 2307 C ARG A 136 -5.177 26.484 20.758 1.00 16.72 C ANISOU 2307 C ARG B 136 2388 30 11 1750 2211 273 C ATOM 2308 O ARG A 136 -4.032 26.941 20.912 1.00 18.96 O ANISOU 2308 O ARG B 136 2629 -266 313 2257 2317 154 O ATOM 2309 CB ARG A 136 -6.450 27.348 22.632 1.00 17.96 C ANISOU 2309 CB ARG B 136 2490 92 -30 1961 2372 166 C ATOM 2310 CG ARG A 136 -7.543 27.181 23.638 1.00 18.24 C ANISOU 2310 CG ARG B 136 2421 50 26 1982 2526 277 C ATOM 2311 CD ARG A 136 -8.108 28.581 24.056 1.00 17.81 C ANISOU 2311 CD ARG B 136 2568 98 -69 1726 2470 332 C ATOM 2312 NE ARG A 136 -9.181 28.446 25.031 1.00 18.78 N ANISOU 2312 NE ARG B 136 2722 -10 32 1834 2578 249 N ATOM 2313 CZ ARG A 136 -9.030 28.306 26.335 1.00 20.80 C ANISOU 2313 CZ ARG B 136 2851 -38 -280 2345 2706 405 C ATOM 2314 NH1 ARG A 136 -7.837 28.362 26.902 1.00 22.21 N ANISOU 2314 NH1 ARG B 136 3249 48 -347 2638 2551 297 N ATOM 2315 NH2 ARG A 136 -10.092 28.147 27.096 1.00 22.07 N ANISOU 2315 NH2 ARG B 136 3215 -75 -149 2640 2527 505 N ATOM 2316 N GLU A 137 -5.749 26.403 19.586 1.00 16.79 N ANISOU 2316 N GLU B 137 2272 8 273 1884 2220 234 N ATOM 2317 CA GLU A 137 -5.114 26.952 18.403 1.00 17.31 C ANISOU 2317 CA GLU B 137 2338 92 186 1977 2262 378 C ATOM 2318 C GLU A 137 -5.471 28.430 18.258 1.00 17.29 C ANISOU 2318 C GLU B 137 2280 35 226 1980 2309 382 C ATOM 2319 O GLU A 137 -6.671 28.788 18.344 1.00 18.01 O ANISOU 2319 O GLU B 137 2365 108 234 2041 2436 260 O ATOM 2320 CB GLU A 137 -5.563 26.193 17.180 1.00 17.95 C ANISOU 2320 CB GLU B 137 2430 112 242 2172 2216 223 C ATOM 2321 CG GLU A 137 -4.906 26.690 15.893 1.00 18.78 C ANISOU 2321 CG GLU B 137 2509 89 225 2248 2375 378 C ATOM 2322 CD GLU A 137 -5.474 26.059 14.702 1.00 21.13 C ANISOU 2322 CD GLU B 137 2873 74 115 2681 2473 253 C ATOM 2323 OE1 GLU A 137 -4.706 25.443 13.964 1.00 22.53 O ANISOU 2323 OE1 GLU B 137 2922 369 11 3459 2179 361 O ATOM 2324 OE2 GLU A 137 -6.713 26.139 14.471 1.00 23.89 O ANISOU 2324 OE2 GLU B 137 3117 177 -207 2932 3026 158 O ATOM 2325 OXT GLU A 137 -4.545 29.210 17.975 1.00 19.55 O ANISOU 2325 OXT GLU B 137 2404 135 222 2089 2934 343 O TER 2326 GLU B 137 END