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*** ***elNémo ID: 230516090313136077Job options:ID = 230516090313136077 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = on DORMSD = on NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:ATOM 1 N LYS A 2 -27.573 1.080 11.215 1.00 49.48 N ANISOU 1 N LYS A 2 6495 6262 6043 -203 -155 -109 N ATOM 2 CA LYS A 2 -27.424 -0.377 11.496 1.00 50.28 C ANISOU 2 CA LYS A 2 6691 6318 6093 -240 -170 -98 C ATOM 3 C LYS A 2 -27.281 -1.138 10.172 1.00 47.00 C ANISOU 3 C LYS A 2 6313 5875 5668 -224 -209 -91 C ATOM 4 O LYS A 2 -26.249 -1.815 9.985 1.00 43.48 O ANISOU 4 O LYS A 2 5937 5390 5194 -185 -236 -83 O ATOM 5 CB LYS A 2 -28.613 -0.891 12.319 1.00 55.27 C ANISOU 5 CB LYS A 2 7331 6961 6706 -332 -141 -106 C ATOM 6 CG LYS A 2 -28.632 -2.393 12.584 1.00 58.11 C ANISOU 6 CG LYS A 2 7804 7268 7004 -386 -157 -93 C ATOM 7 CD LYS A 2 -27.389 -2.924 13.287 1.00 59.97 C ANISOU 7 CD LYS A 2 8139 7449 7195 -347 -179 -80 C ATOM 8 CE LYS A 2 -27.640 -4.186 14.091 1.00 60.88 C ANISOU 8 CE LYS A 2 8375 7513 7241 -419 -185 -71 C ATOM 9 NZ LYS A 2 -28.082 -5.315 13.238 1.00 60.27 N1+ ANISOU 9 NZ LYS A 2 8359 7402 7135 -458 -214 -64 N1+ ATOM 10 N GLU A 3 -28.282 -1.071 9.291 1.00 42.08 N ANISOU 10 N GLU A 3 5647 5272 5069 -251 -215 -97 N ATOM 11 CA GLU A 3 -28.198 -1.768 7.983 1.00 40.65 C ANISOU 11 CA GLU A 3 5503 5062 4877 -238 -253 -90 C ATOM 12 C GLU A 3 -27.368 -0.912 7.015 1.00 33.43 C ANISOU 12 C GLU A 3 4560 4153 3987 -164 -266 -90 C ATOM 13 O GLU A 3 -26.473 -1.464 6.358 1.00 36.34 O ANISOU 13 O GLU A 3 4981 4490 4333 -127 -288 -85 O ATOM 14 CB GLU A 3 -29.585 -2.097 7.437 1.00 46.03 C ANISOU 14 CB GLU A 3 6156 5760 5571 -300 -260 -99 C ATOM 15 CG GLU A 3 -29.580 -3.362 6.605 1.00 52.08 C ANISOU 15 CG GLU A 3 7003 6482 6303 -318 -296 -88 C ATOM 16 CD GLU A 3 -30.870 -3.675 5.864 1.00 58.29 C ANISOU 16 CD GLU A 3 7760 7285 7103 -374 -310 -99 C ATOM 17 OE1 GLU A 3 -31.107 -4.872 5.577 1.00 59.79 O ANISOU 17 OE1 GLU A 3 8022 7438 7254 -419 -331 -91 O ATOM 18 OE2 GLU A 3 -31.615 -2.721 5.542 1.00 61.89 O1- ANISOU 18 OE2 GLU A 3 8123 7785 7605 -369 -308 -119 O1- ATOM 19 N CYS A 4 -27.584 0.399 7.001 1.00 28.55 N ANISOU 19 N CYS A 4 3867 3572 3408 -144 -251 -100 N ATOM 20 CA CYS A 4 -27.021 1.325 5.987 1.00 26.57 C ANISOU 20 CA CYS A 4 3594 3324 3174 -91 -262 -101 C ATOM 21 C CYS A 4 -26.168 2.386 6.678 1.00 26.79 C ANISOU 21 C CYS A 4 3594 3369 3212 -55 -236 -105 C ATOM 22 O CYS A 4 -26.530 2.826 7.779 1.00 26.98 O ANISOU 22 O CYS A 4 3585 3416 3249 -71 -213 -109 O ATOM 23 CB CYS A 4 -28.117 2.024 5.196 1.00 27.11 C ANISOU 23 CB CYS A 4 3613 3411 3275 -98 -279 -111 C ATOM 24 SG CYS A 4 -29.023 0.895 4.115 1.00 28.57 S ANISOU 24 SG CYS A 4 3828 3576 3450 -135 -317 -110 S ATOM 25 N ASP A 5 -25.119 2.838 6.002 1.00 23.47 N ANISOU 25 N ASP A 5 3186 2943 2787 -13 -239 -105 N ATOM 26 CA ASP A 5 -24.201 3.879 6.521 1.00 22.77 C ANISOU 26 CA ASP A 5 3073 2872 2705 15 -215 -111 C ATOM 27 C ASP A 5 -24.789 5.263 6.241 1.00 23.85 C ANISOU 27 C ASP A 5 3165 3026 2868 19 -213 -115 C ATOM 28 O ASP A 5 -24.269 6.248 6.794 1.00 23.55 O ANISOU 28 O ASP A 5 3106 3003 2837 35 -194 -119 O ATOM 29 CB ASP A 5 -22.805 3.696 5.925 1.00 21.27 C ANISOU 29 CB ASP A 5 2913 2674 2495 49 -214 -120 C ATOM 30 CG ASP A 5 -22.082 2.483 6.485 1.00 20.97 C ANISOU 30 CG ASP A 5 2915 2620 2431 62 -222 -125 C ATOM 31 OD1 ASP A 5 -22.364 2.102 7.646 1.00 22.52 O ANISOU 31 OD1 ASP A 5 3120 2812 2624 47 -219 -120 O ATOM 32 OD2 ASP A 5 -21.212 1.964 5.790 1.00 18.45 O1- ANISOU 32 OD2 ASP A 5 2623 2292 2093 89 -231 -138 O1- ATOM 33 N CYS A 6 -25.695 5.365 5.270 1.00 23.56 N ANISOU 33 N CYS A 6 3126 2983 2842 12 -240 -115 N ATOM 34 CA CYS A 6 -26.344 6.638 4.870 1.00 23.90 C ANISOU 34 CA CYS A 6 3140 3033 2906 24 -255 -123 C ATOM 35 C CYS A 6 -27.855 6.432 5.004 1.00 27.52 C ANISOU 35 C CYS A 6 3558 3507 3392 4 -275 -136 C ATOM 36 O CYS A 6 -28.339 5.360 4.571 1.00 28.13 O ANISOU 36 O CYS A 6 3650 3575 3462 -20 -291 -134 O ATOM 37 CB CYS A 6 -25.995 7.034 3.435 1.00 23.05 C ANISOU 37 CB CYS A 6 3075 2899 2782 39 -278 -121 C ATOM 38 SG CYS A 6 -24.231 7.250 3.049 1.00 22.98 S ANISOU 38 SG CYS A 6 3108 2882 2738 51 -248 -118 S ATOM 39 N SER A 7 -28.562 7.414 5.567 1.00 28.26 N ANISOU 39 N SER A 7 3599 3624 3512 14 -275 -153 N ATOM 40 CA SER A 7 -30.041 7.429 5.728 1.00 30.92 C ANISOU 40 CA SER A 7 3877 3989 3880 0 -293 -181 C ATOM 41 C SER A 7 -30.697 7.404 4.348 1.00 31.19 C ANISOU 41 C SER A 7 3923 4005 3921 12 -348 -189 C ATOM 42 O SER A 7 -31.779 6.795 4.191 1.00 31.68 O ANISOU 42 O SER A 7 3950 4086 4000 -12 -367 -209 O ATOM 43 CB SER A 7 -30.503 8.646 6.495 1.00 31.18 C ANISOU 43 CB SER A 7 3856 4051 3940 24 -288 -205 C ATOM 44 OG SER A 7 -29.952 8.683 7.796 1.00 37.44 O ANISOU 44 OG SER A 7 4640 4859 4725 12 -239 -198 O ATOM 45 N SER A 8 -30.138 8.176 3.424 1.00 28.08 N ANISOU 45 N SER A 8 3576 3578 3513 47 -374 -179 N ATOM 46 CA SER A 8 -30.780 8.502 2.131 1.00 28.65 C ANISOU 46 CA SER A 8 3670 3625 3588 69 -435 -190 C ATOM 47 C SER A 8 -30.068 7.770 0.999 1.00 26.77 C ANISOU 47 C SER A 8 3508 3347 3314 58 -443 -165 C ATOM 48 O SER A 8 -28.865 7.938 0.807 1.00 23.04 O ANISOU 48 O SER A 8 3086 2856 2811 61 -417 -145 O ATOM 49 CB SER A 8 -30.789 9.969 1.878 1.00 29.59 C ANISOU 49 CB SER A 8 3805 3727 3709 114 -465 -201 C ATOM 50 OG SER A 8 -31.108 10.202 0.519 1.00 29.30 O ANISOU 50 OG SER A 8 3822 3651 3660 134 -526 -203 O ATOM 51 N PRO A 9 -30.836 7.103 0.116 1.00 26.08 N ANISOU 51 N PRO A 9 3429 3247 3230 48 -486 -171 N ATOM 52 CA PRO A 9 -30.294 6.494 -1.099 1.00 26.08 C ANISOU 52 CA PRO A 9 3506 3206 3195 41 -501 -151 C ATOM 53 C PRO A 9 -29.653 7.513 -2.051 1.00 23.40 C ANISOU 53 C PRO A 9 3237 2826 2825 68 -520 -143 C ATOM 54 O PRO A 9 -28.817 7.119 -2.835 1.00 25.55 O ANISOU 54 O PRO A 9 3575 3071 3061 57 -508 -127 O ATOM 55 CB PRO A 9 -31.513 5.869 -1.796 1.00 27.04 C ANISOU 55 CB PRO A 9 3614 3324 3333 30 -555 -167 C ATOM 56 CG PRO A 9 -32.598 5.839 -0.739 1.00 29.50 C ANISOU 56 CG PRO A 9 3830 3689 3688 17 -550 -196 C ATOM 57 CD PRO A 9 -32.302 7.000 0.185 1.00 29.07 C ANISOU 57 CD PRO A 9 3743 3655 3647 45 -524 -204 C ATOM 58 N GLU A 10 -29.991 8.796 -1.914 1.00 23.99 N ANISOU 58 N GLU A 10 3303 2898 2912 98 -545 -158 N ATOM 59 CA GLU A 10 -29.422 9.886 -2.758 1.00 24.90 C ANISOU 59 CA GLU A 10 3502 2966 2989 115 -565 -151 C ATOM 60 C GLU A 10 -27.983 10.184 -2.316 1.00 22.80 C ANISOU 60 C GLU A 10 3260 2707 2695 98 -498 -134 C ATOM 61 O GLU A 10 -27.270 10.886 -3.043 1.00 24.61 O ANISOU 61 O GLU A 10 3567 2901 2881 92 -496 -127 O ATOM 62 CB GLU A 10 -30.302 11.140 -2.708 1.00 27.28 C ANISOU 62 CB GLU A 10 3795 3257 3310 158 -623 -175 C ATOM 63 CG GLU A 10 -31.746 10.861 -3.104 1.00 30.00 C ANISOU 63 CG GLU A 10 4100 3606 3690 181 -694 -204 C ATOM 64 CD GLU A 10 -32.610 12.076 -3.395 1.00 33.71 C ANISOU 64 CD GLU A 10 4583 4053 4172 237 -774 -236 C ATOM 65 OE1 GLU A 10 -32.091 13.201 -3.318 1.00 38.27 O ANISOU 65 OE1 GLU A 10 5214 4601 4724 257 -776 -231 O ATOM 66 OE2 GLU A 10 -33.810 11.883 -3.707 1.00 40.66 O1- ANISOU 66 OE2 GLU A 10 5418 4943 5085 262 -839 -270 O1- ATOM 67 N ASN A 11 -27.589 9.762 -1.117 1.00 21.20 N ANISOU 67 N ASN A 11 2995 2546 2511 88 -445 -132 N ATOM 68 CA ASN A 11 -26.314 10.229 -0.522 1.00 19.18 C ANISOU 68 CA ASN A 11 2747 2303 2236 79 -389 -125 C ATOM 69 C ASN A 11 -25.152 9.613 -1.292 1.00 18.20 C ANISOU 69 C ASN A 11 2675 2166 2071 56 -358 -117 C ATOM 70 O ASN A 11 -24.959 8.392 -1.280 1.00 18.67 O ANISOU 70 O ASN A 11 2723 2238 2133 47 -344 -114 O ATOM 71 CB ASN A 11 -26.254 9.890 0.967 1.00 18.52 C ANISOU 71 CB ASN A 11 2589 2262 2182 77 -351 -127 C ATOM 72 CG ASN A 11 -25.053 10.471 1.679 1.00 18.42 C ANISOU 72 CG ASN A 11 2576 2264 2155 73 -302 -125 C ATOM 73 ND2 ASN A 11 -25.237 10.746 2.956 1.00 18.58 N ANISOU 73 ND2 ASN A 11 2543 2313 2202 81 -284 -129 N ATOM 74 OD1 ASN A 11 -23.969 10.612 1.100 1.00 17.48 O ANISOU 74 OD1 ASN A 11 2502 2136 2003 60 -279 -123 O ATOM 75 N PRO A 12 -24.300 10.432 -1.928 1.00 18.38 N ANISOU 75 N PRO A 12 2759 2169 2054 42 -342 -117 N ATOM 76 CA PRO A 12 -23.212 9.923 -2.754 1.00 19.37 C ANISOU 76 CA PRO A 12 2931 2290 2138 17 -308 -120 C ATOM 77 C PRO A 12 -22.054 9.347 -1.934 1.00 17.98 C ANISOU 77 C PRO A 12 2707 2158 1965 12 -250 -130 C ATOM 78 O PRO A 12 -21.167 8.778 -2.509 1.00 17.69 O ANISOU 78 O PRO A 12 2690 2127 1900 0 -221 -142 O ATOM 79 CB PRO A 12 -22.774 11.165 -3.535 1.00 20.44 C ANISOU 79 CB PRO A 12 3145 2393 2227 -5 -307 -122 C ATOM 80 CG PRO A 12 -23.009 12.277 -2.550 1.00 20.46 C ANISOU 80 CG PRO A 12 3120 2404 2250 8 -311 -121 C ATOM 81 CD PRO A 12 -24.327 11.903 -1.907 1.00 18.87 C ANISOU 81 CD PRO A 12 2855 2211 2102 45 -355 -119 C ATOM 82 N CYS A 13 -22.069 9.529 -0.611 1.00 16.64 N ANISOU 82 N CYS A 13 2475 2018 1827 26 -235 -131 N ATOM 83 CA CYS A 13 -20.997 8.997 0.272 1.00 16.13 C ANISOU 83 CA CYS A 13 2368 1993 1768 29 -191 -144 C ATOM 84 C CYS A 13 -21.115 7.477 0.387 1.00 16.15 C ANISOU 84 C CYS A 13 2357 1999 1780 43 -200 -144 C ATOM 85 O CYS A 13 -20.116 6.831 0.750 1.00 15.46 O ANISOU 85 O CYS A 13 2254 1934 1685 53 -174 -161 O ATOM 86 CB CYS A 13 -21.045 9.639 1.650 1.00 15.96 C ANISOU 86 CB CYS A 13 2297 1994 1773 39 -179 -142 C ATOM 87 SG CYS A 13 -20.629 11.401 1.628 1.00 15.43 S ANISOU 87 SG CYS A 13 2255 1920 1686 21 -164 -145 S ATOM 88 N CYS A 14 -22.279 6.918 0.043 1.00 16.83 N ANISOU 88 N CYS A 14 2453 2063 1878 44 -239 -129 N ATOM 89 CA CYS A 14 -22.506 5.455 0.081 1.00 17.07 C ANISOU 89 CA CYS A 14 2485 2088 1910 49 -253 -127 C ATOM 90 C CYS A 14 -22.597 4.896 -1.332 1.00 17.76 C ANISOU 90 C CYS A 14 2628 2147 1973 42 -274 -127 C ATOM 91 O CYS A 14 -23.153 5.587 -2.214 1.00 18.49 O ANISOU 91 O CYS A 14 2751 2216 2057 33 -297 -120 O ATOM 92 CB CYS A 14 -23.774 5.121 0.839 1.00 18.05 C ANISOU 92 CB CYS A 14 2577 2213 2065 43 -277 -115 C ATOM 93 SG CYS A 14 -23.544 5.334 2.619 1.00 20.30 S ANISOU 93 SG CYS A 14 2810 2530 2373 47 -248 -117 S ATOM 94 N ASP A 15 -22.122 3.667 -1.499 1.00 17.27 N ANISOU 94 N ASP A 15 2584 2081 1894 51 -272 -134 N ATOM 95 CA AASP A 15 -22.373 2.878 -2.733 0.50 17.95 C ANISOU 95 CA AASP A 15 2724 2137 1957 46 -297 -132 C ATOM 96 CA BASP A 15 -22.370 2.867 -2.728 0.50 18.37 C ANISOU 96 CA BASP A 15 2777 2190 2010 46 -297 -132 C ATOM 97 C ASP A 15 -23.879 2.610 -2.820 1.00 17.44 C ANISOU 97 C ASP A 15 2659 2051 1914 31 -343 -112 C ATOM 98 O ASP A 15 -24.441 2.048 -1.879 1.00 15.47 O ANISOU 98 O ASP A 15 2379 1811 1685 25 -351 -106 O ATOM 99 CB AASP A 15 -21.572 1.578 -2.737 0.50 19.29 C ANISOU 99 CB AASP A 15 2914 2307 2107 65 -291 -148 C ATOM 100 CB BASP A 15 -21.564 1.565 -2.709 0.50 20.32 C ANISOU 100 CB BASP A 15 3043 2437 2238 65 -291 -148 C ATOM 101 CG AASP A 15 -20.093 1.767 -3.024 0.50 21.12 C ANISOU 101 CG AASP A 15 3144 2563 2315 81 -250 -181 C ATOM 102 CG BASP A 15 -21.909 0.600 -3.833 0.50 22.91 C ANISOU 102 CG BASP A 15 3430 2732 2542 62 -320 -144 C ATOM 103 OD1AASP A 15 -19.745 2.737 -3.731 0.50 22.00 O ANISOU 103 OD1AASP A 15 3266 2680 2410 62 -226 -189 O ATOM 104 OD2AASP A 15 -19.307 0.945 -2.536 0.50 24.34 O1- ANISOU 104 OD2AASP A 15 3544 2985 2718 111 -243 -204 O1- ATOM 105 OD1BASP A 15 -22.665 0.997 -4.733 0.50 27.36 O ANISOU 105 OD1BASP A 15 4020 3272 3102 43 -344 -131 O ATOM 106 OD2BASP A 15 -21.458 -0.545 -3.772 0.50 25.98 O1- ANISOU 106 OD2BASP A 15 3842 3114 2916 81 -327 -156 O1- ATOM 107 N ALA A 16 -24.488 2.909 -3.963 1.00 16.11 N ANISOU 107 N ALA A 16 2528 1856 1736 22 -375 -106 N ATOM 108 CA ALA A 16 -25.936 2.699 -4.137 1.00 16.41 C ANISOU 108 CA ALA A 16 2558 1880 1797 10 -425 -97 C ATOM 109 C ALA A 16 -26.279 1.217 -3.915 1.00 15.86 C ANISOU 109 C ALA A 16 2495 1804 1726 -3 -437 -92 C ATOM 110 O ALA A 16 -27.366 0.930 -3.390 1.00 16.56 O ANISOU 110 O ALA A 16 2548 1901 1841 -23 -459 -90 O ATOM 111 CB ALA A 16 -26.341 3.172 -5.500 1.00 16.54 C ANISOU 111 CB ALA A 16 2627 1860 1795 8 -463 -95 C ATOM 112 N ALA A 17 -25.468 0.310 -4.449 1.00 16.57 N ANISOU 112 N ALA A 17 2635 1876 1782 4 -429 -95 N ATOM 113 CA ALA A 17 -25.767 -1.140 -4.469 1.00 16.72 C ANISOU 113 CA ALA A 17 2687 1875 1788 -7 -451 -90 C ATOM 114 C ALA A 17 -25.890 -1.672 -3.024 1.00 16.50 C ANISOU 114 C ALA A 17 2627 1865 1774 -18 -437 -88 C ATOM 115 O ALA A 17 -26.769 -2.502 -2.755 1.00 16.07 O ANISOU 115 O ALA A 17 2581 1800 1722 -50 -460 -80 O ATOM 116 CB ALA A 17 -24.674 -1.868 -5.218 1.00 17.23 C ANISOU 116 CB ALA A 17 2811 1921 1812 15 -441 -101 C ATOM 117 N THR A 18 -25.023 -1.223 -2.117 1.00 16.79 N ANISOU 117 N THR A 18 2634 1926 1816 3 -401 -95 N ATOM 118 CA THR A 18 -24.862 -1.842 -0.770 1.00 17.09 C ANISOU 118 CA THR A 18 2664 1972 1855 0 -390 -95 C ATOM 119 C THR A 18 -25.478 -0.983 0.343 1.00 17.96 C ANISOU 119 C THR A 18 2709 2113 1998 -20 -371 -91 C ATOM 120 O THR A 18 -25.730 -1.550 1.416 1.00 16.96 O ANISOU 120 O THR A 18 2584 1989 1870 -41 -366 -88 O ATOM 121 CB THR A 18 -23.387 -2.095 -0.459 1.00 17.02 C ANISOU 121 CB THR A 18 2673 1967 1826 43 -370 -113 C ATOM 122 CG2 THR A 18 -22.740 -2.999 -1.486 1.00 16.57 C ANISOU 122 CG2 THR A 18 2676 1884 1734 68 -386 -126 C ATOM 123 OG1 THR A 18 -22.755 -0.818 -0.408 1.00 16.11 O ANISOU 123 OG1 THR A 18 2510 1884 1725 60 -337 -123 O ATOM 124 N CYS A 19 -25.609 0.332 0.133 1.00 19.17 N ANISOU 124 N CYS A 19 2819 2288 2176 -11 -361 -94 N ATOM 125 CA CYS A 19 -25.929 1.385 1.142 1.00 19.61 C ANISOU 125 CA CYS A 19 2811 2375 2261 -14 -340 -97 C ATOM 126 C CYS A 19 -24.871 1.443 2.251 1.00 19.32 C ANISOU 126 C CYS A 19 2767 2353 2219 4 -307 -101 C ATOM 127 O CYS A 19 -25.140 2.088 3.297 1.00 20.09 O ANISOU 127 O CYS A 19 2821 2474 2337 -2 -288 -102 O ATOM 128 CB CYS A 19 -27.348 1.224 1.677 1.00 22.61 C ANISOU 128 CB CYS A 19 3154 2769 2666 -53 -353 -97 C ATOM 129 SG CYS A 19 -27.585 -0.028 2.966 1.00 26.13 S ANISOU 129 SG CYS A 19 3616 3214 3096 -95 -338 -93 S ATOM 130 N LYS A 20 -23.677 0.923 1.968 1.00 18.79 N ANISOU 130 N LYS A 20 2736 2275 2125 32 -301 -110 N ATOM 131 CA LYS A 20 -22.469 1.083 2.820 1.00 19.71 C ANISOU 131 CA LYS A 20 2843 2409 2237 61 -276 -124 C ATOM 132 C LYS A 20 -21.604 2.210 2.260 1.00 18.23 C ANISOU 132 C LYS A 20 2632 2242 2050 79 -251 -138 C ATOM 133 O LYS A 20 -21.684 2.500 1.060 1.00 17.38 O ANISOU 133 O LYS A 20 2543 2126 1933 74 -256 -138 O ATOM 134 CB LYS A 20 -21.656 -0.211 2.877 1.00 20.95 C ANISOU 134 CB LYS A 20 3049 2545 2363 87 -291 -136 C ATOM 135 CG LYS A 20 -22.355 -1.396 3.537 1.00 23.52 C ANISOU 135 CG LYS A 20 3419 2841 2675 63 -316 -122 C ATOM 136 CD LYS A 20 -22.812 -1.146 4.962 1.00 25.81 C ANISOU 136 CD LYS A 20 3688 3142 2976 38 -302 -113 C ATOM 137 CE LYS A 20 -23.631 -2.295 5.510 1.00 28.69 C ANISOU 137 CE LYS A 20 4107 3475 3318 -4 -321 -99 C ATOM 138 NZ LYS A 20 -23.998 -2.096 6.928 1.00 30.83 N1+ ANISOU 138 NZ LYS A 20 4366 3755 3592 -34 -302 -94 N1+ ATOM 139 N LEU A 21 -20.750 2.792 3.095 1.00 17.52 N ANISOU 139 N LEU A 21 2512 2178 1966 96 -226 -151 N ATOM 140 CA LEU A 21 -19.780 3.826 2.666 1.00 17.10 C ANISOU 140 CA LEU A 21 2439 2148 1908 103 -196 -170 C ATOM 141 C LEU A 21 -19.022 3.352 1.427 1.00 17.89 C ANISOU 141 C LEU A 21 2571 2246 1980 112 -193 -192 C ATOM 142 O LEU A 21 -18.530 2.205 1.388 1.00 17.83 O ANISOU 142 O LEU A 21 2583 2232 1958 138 -206 -209 O ATOM 143 CB LEU A 21 -18.797 4.110 3.798 1.00 16.59 C ANISOU 143 CB LEU A 21 2341 2112 1849 123 -175 -189 C ATOM 144 CG LEU A 21 -19.399 4.812 5.004 1.00 16.63 C ANISOU 144 CG LEU A 21 2316 2124 1878 112 -170 -172 C ATOM 145 CD1 LEU A 21 -18.338 4.975 6.079 1.00 16.08 C ANISOU 145 CD1 LEU A 21 2220 2077 1809 134 -154 -192 C ATOM 146 CD2 LEU A 21 -19.986 6.156 4.605 1.00 16.80 C ANISOU 146 CD2 LEU A 21 2324 2149 1911 90 -160 -159 C ATOM 147 N ARG A 22 -18.817 4.272 0.497 1.00 18.42 N ANISOU 147 N ARG A 22 2646 2318 2036 93 -174 -197 N ATOM 148 CA ARG A 22 -18.004 4.019 -0.710 1.00 20.22 C ANISOU 148 CA ARG A 22 2901 2548 2230 91 -157 -224 C ATOM 149 C ARG A 22 -16.552 3.865 -0.275 1.00 20.84 C ANISOU 149 C ARG A 22 2943 2670 2303 115 -126 -270 C ATOM 150 O ARG A 22 -16.155 4.276 0.811 1.00 19.45 O ANISOU 150 O ARG A 22 2725 2519 2146 125 -115 -278 O ATOM 151 CB ARG A 22 -18.220 5.156 -1.712 1.00 20.58 C ANISOU 151 CB ARG A 22 2977 2583 2258 53 -144 -216 C ATOM 152 CG ARG A 22 -17.530 6.450 -1.318 1.00 21.64 C ANISOU 152 CG ARG A 22 3086 2746 2390 33 -106 -229 C ATOM 153 CD ARG A 22 -17.909 7.622 -2.191 1.00 22.92 C ANISOU 153 CD ARG A 22 3298 2882 2528 -6 -105 -214 C ATOM 154 NE ARG A 22 -17.103 8.787 -1.862 1.00 23.82 N ANISOU 154 NE ARG A 22 3399 3021 2629 -33 -65 -231 N ATOM 155 CZ ARG A 22 -17.445 10.035 -2.143 1.00 23.84 C ANISOU 155 CZ ARG A 22 3444 2999 2614 -64 -68 -215 C ATOM 156 NH1 ARG A 22 -16.631 11.022 -1.821 1.00 25.27 N1+ ANISOU 156 NH1 ARG A 22 3618 3203 2779 -96 -30 -232 N1+ ATOM 157 NH2 ARG A 22 -18.621 10.301 -2.686 1.00 26.16 N ANISOU 157 NH2 ARG A 22 3788 3244 2907 -62 -116 -186 N ATOM 158 N PRO A 23 -15.695 3.250 -1.111 1.00 22.37 N ANISOU 158 N PRO A 23 3149 2878 2472 128 -112 -309 N ATOM 159 CA PRO A 23 -14.295 3.068 -0.744 1.00 23.43 C ANISOU 159 CA PRO A 23 3237 3061 2603 157 -86 -367 C ATOM 160 C PRO A 23 -13.652 4.421 -0.405 1.00 23.68 C ANISOU 160 C PRO A 23 3225 3134 2637 124 -41 -383 C ATOM 161 O PRO A 23 -13.886 5.397 -1.076 1.00 23.45 O ANISOU 161 O PRO A 23 3219 3098 2591 73 -16 -368 O ATOM 162 CB PRO A 23 -13.702 2.371 -1.982 1.00 25.22 C ANISOU 162 CB PRO A 23 3488 3295 2797 165 -73 -406 C ATOM 163 CG PRO A 23 -14.894 1.675 -2.620 1.00 24.10 C ANISOU 163 CG PRO A 23 3413 3095 2649 161 -115 -361 C ATOM 164 CD PRO A 23 -16.039 2.639 -2.406 1.00 23.90 C ANISOU 164 CD PRO A 23 3398 3042 2639 120 -124 -305 C ATOM 165 N GLY A 24 -12.876 4.465 0.673 1.00 24.49 N ANISOU 165 N GLY A 24 3272 3273 2758 152 -36 -412 N ATOM 166 CA GLY A 24 -12.174 5.686 1.108 1.00 24.28 C ANISOU 166 CA GLY A 24 3201 3288 2735 120 5 -432 C ATOM 167 C GLY A 24 -13.053 6.610 1.930 1.00 23.16 C ANISOU 167 C GLY A 24 3065 3121 2613 98 -5 -379 C ATOM 168 O GLY A 24 -12.508 7.541 2.531 1.00 26.79 O ANISOU 168 O GLY A 24 3489 3610 3077 80 19 -393 O ATOM 169 N ALA A 25 -14.371 6.435 1.936 1.00 20.05 N ANISOU 169 N ALA A 25 2710 2677 2228 98 -39 -326 N ATOM 170 CA ALA A 25 -15.260 7.312 2.735 1.00 18.51 C ANISOU 170 CA ALA A 25 2514 2463 2053 83 -50 -284 C ATOM 171 C ALA A 25 -15.188 6.916 4.217 1.00 17.43 C ANISOU 171 C ALA A 25 2344 2335 1944 118 -67 -283 C ATOM 172 O ALA A 25 -15.091 5.722 4.523 1.00 17.24 O ANISOU 172 O ALA A 25 2324 2303 1921 154 -92 -292 O ATOM 173 CB ALA A 25 -16.678 7.269 2.236 1.00 18.29 C ANISOU 173 CB ALA A 25 2528 2389 2029 71 -81 -240 C ATOM 174 N GLN A 26 -15.272 7.907 5.113 1.00 16.79 N ANISOU 174 N GLN A 26 2240 2262 1876 106 -56 -271 N ATOM 175 CA GLN A 26 -15.269 7.693 6.581 1.00 16.33 C ANISOU 175 CA GLN A 26 2158 2207 1838 132 -70 -267 C ATOM 176 C GLN A 26 -16.671 7.889 7.143 1.00 15.38 C ANISOU 176 C GLN A 26 2051 2057 1734 122 -88 -223 C ATOM 177 O GLN A 26 -16.944 7.424 8.275 1.00 15.95 O ANISOU 177 O GLN A 26 2120 2122 1818 137 -102 -214 O ATOM 178 CB GLN A 26 -14.295 8.661 7.231 1.00 17.00 C ANISOU 178 CB GLN A 26 2204 2328 1926 125 -44 -292 C ATOM 179 CG GLN A 26 -12.869 8.409 6.783 1.00 18.19 C ANISOU 179 CG GLN A 26 2324 2522 2063 135 -24 -349 C ATOM 180 CD GLN A 26 -11.910 9.363 7.438 1.00 19.13 C ANISOU 180 CD GLN A 26 2400 2681 2186 121 1 -379 C ATOM 181 NE2 GLN A 26 -10.860 8.815 8.038 1.00 23.44 N ANISOU 181 NE2 GLN A 26 2904 3261 2738 160 -7 -427 N ATOM 182 OE1 GLN A 26 -12.126 10.571 7.458 1.00 19.21 O ANISOU 182 OE1 GLN A 26 2417 2689 2191 79 23 -360 O ATOM 183 N CYS A 27 -17.530 8.590 6.412 1.00 15.14 N ANISOU 183 N CYS A 27 2038 2010 1704 96 -88 -201 N ATOM 184 CA CYS A 27 -18.863 8.983 6.918 1.00 14.69 C ANISOU 184 CA CYS A 27 1979 1935 1667 89 -103 -172 C ATOM 185 C CYS A 27 -19.744 9.479 5.777 1.00 14.47 C ANISOU 185 C CYS A 27 1977 1885 1636 73 -119 -158 C ATOM 186 O CYS A 27 -19.210 9.793 4.705 1.00 14.01 O ANISOU 186 O CYS A 27 1945 1822 1553 60 -111 -167 O ATOM 187 CB CYS A 27 -18.742 10.052 7.996 1.00 14.74 C ANISOU 187 CB CYS A 27 1960 1955 1684 87 -88 -170 C ATOM 188 SG CYS A 27 -17.841 11.537 7.470 1.00 16.86 S ANISOU 188 SG CYS A 27 2236 2236 1934 65 -62 -184 S ATOM 189 N GLY A 28 -21.050 9.528 6.004 1.00 14.96 N ANISOU 189 N GLY A 28 2031 1934 1717 72 -141 -141 N ATOM 190 CA GLY A 28 -21.988 10.135 5.042 1.00 15.64 C ANISOU 190 CA GLY A 28 2139 1998 1804 67 -168 -134 C ATOM 191 C GLY A 28 -22.816 11.264 5.623 1.00 17.17 C ANISOU 191 C GLY A 28 2313 2193 2018 75 -179 -132 C ATOM 192 O GLY A 28 -23.533 11.919 4.868 1.00 18.71 O ANISOU 192 O GLY A 28 2529 2366 2213 80 -210 -132 O ATOM 193 N GLU A 29 -22.858 11.396 6.943 1.00 17.91 N ANISOU 193 N GLU A 29 2368 2307 2129 80 -161 -134 N ATOM 194 CA GLU A 29 -23.752 12.374 7.588 1.00 19.09 C ANISOU 194 CA GLU A 29 2491 2461 2299 92 -171 -138 C ATOM 195 C GLU A 29 -23.221 12.651 8.989 1.00 17.81 C ANISOU 195 C GLU A 29 2303 2319 2142 93 -139 -140 C ATOM 196 O GLU A 29 -22.431 11.845 9.521 1.00 17.38 O ANISOU 196 O GLU A 29 2248 2276 2080 86 -118 -138 O ATOM 197 CB GLU A 29 -25.197 11.876 7.635 1.00 22.88 C ANISOU 197 CB GLU A 29 2939 2947 2806 94 -195 -145 C ATOM 198 CG GLU A 29 -25.314 10.493 8.236 1.00 27.30 C ANISOU 198 CG GLU A 29 3481 3521 3369 72 -177 -141 C ATOM 199 CD GLU A 29 -26.584 9.738 7.874 1.00 31.09 C ANISOU 199 CD GLU A 29 3940 4005 3865 57 -200 -149 C ATOM 200 OE1 GLU A 29 -26.894 9.638 6.678 1.00 32.66 O ANISOU 200 OE1 GLU A 29 4160 4186 4062 62 -232 -148 O ATOM 201 OE2 GLU A 29 -27.250 9.242 8.807 1.00 35.58 O1- ANISOU 201 OE2 GLU A 29 4475 4596 4445 36 -184 -157 O1- ATOM 202 N GLY A 30 -23.709 13.743 9.554 1.00 17.99 N ANISOU 202 N GLY A 30 2312 2345 2176 106 -143 -147 N ATOM 203 CA GLY A 30 -23.319 14.225 10.884 1.00 16.93 C ANISOU 203 CA GLY A 30 2158 2228 2046 108 -116 -149 C ATOM 204 C GLY A 30 -22.680 15.599 10.810 1.00 15.92 C ANISOU 204 C GLY A 30 2057 2087 1902 114 -116 -150 C ATOM 205 O GLY A 30 -22.141 15.969 9.756 1.00 15.23 O ANISOU 205 O GLY A 30 2012 1981 1792 105 -125 -147 O ATOM 206 N LEU A 31 -22.647 16.302 11.937 1.00 15.30 N ANISOU 206 N LEU A 31 1963 2018 1829 122 -102 -154 N ATOM 207 CA LEU A 31 -22.086 17.668 12.004 1.00 15.44 C ANISOU 207 CA LEU A 31 2013 2022 1829 124 -103 -156 C ATOM 208 C LEU A 31 -20.575 17.620 11.757 1.00 14.42 C ANISOU 208 C LEU A 31 1907 1896 1673 96 -78 -153 C ATOM 209 O LEU A 31 -20.009 18.670 11.400 1.00 16.36 O ANISOU 209 O LEU A 31 2194 2127 1894 82 -78 -154 O ATOM 210 CB LEU A 31 -22.416 18.246 13.381 1.00 16.58 C ANISOU 210 CB LEU A 31 2133 2180 1987 140 -91 -162 C ATOM 211 CG LEU A 31 -23.879 18.645 13.581 1.00 18.53 C ANISOU 211 CG LEU A 31 2353 2428 2258 170 -114 -179 C ATOM 212 CD1 LEU A 31 -24.159 18.952 15.033 1.00 18.11 C ANISOU 212 CD1 LEU A 31 2267 2395 2216 179 -91 -190 C ATOM 213 CD2 LEU A 31 -24.241 19.824 12.700 1.00 20.94 C ANISOU 213 CD2 LEU A 31 2703 2699 2551 194 -157 -186 C ATOM 214 N CYS A 32 -19.929 16.458 11.942 1.00 12.98 N ANISOU 214 N CYS A 32 1703 1735 1494 88 -60 -154 N ATOM 215 CA CYS A 32 -18.454 16.320 11.821 1.00 12.74 C ANISOU 215 CA CYS A 32 1675 1720 1444 69 -38 -165 C ATOM 216 C CYS A 32 -18.108 15.435 10.624 1.00 12.75 C ANISOU 216 C CYS A 32 1687 1722 1434 59 -39 -170 C ATOM 217 O CYS A 32 -17.042 14.759 10.629 1.00 11.35 O ANISOU 217 O CYS A 32 1494 1567 1250 55 -23 -187 O ATOM 218 CB CYS A 32 -17.842 15.801 13.116 1.00 12.66 C ANISOU 218 CB CYS A 32 1634 1731 1443 79 -24 -172 C ATOM 219 SG CYS A 32 -18.050 16.997 14.466 1.00 13.73 S ANISOU 219 SG CYS A 32 1767 1866 1584 84 -18 -168 S ATOM 220 N CYS A 33 -18.946 15.505 9.591 1.00 13.62 N ANISOU 220 N CYS A 33 1825 1809 1541 58 -60 -160 N ATOM 221 CA CYS A 33 -18.684 14.881 8.281 1.00 14.97 C ANISOU 221 CA CYS A 33 2020 1973 1695 44 -62 -164 C ATOM 222 C CYS A 33 -18.546 15.991 7.238 1.00 16.28 C ANISOU 222 C CYS A 33 2243 2113 1827 17 -66 -164 C ATOM 223 O CYS A 33 -19.424 16.883 7.194 1.00 15.15 O ANISOU 223 O CYS A 33 2129 1942 1685 27 -94 -153 O ATOM 224 CB CYS A 33 -19.762 13.872 7.920 1.00 15.97 C ANISOU 224 CB CYS A 33 2141 2087 1839 62 -89 -153 C ATOM 225 SG CYS A 33 -19.260 12.825 6.529 1.00 17.26 S ANISOU 225 SG CYS A 33 2329 2246 1981 50 -88 -160 S ATOM 226 N GLU A 34 -17.450 15.949 6.488 1.00 17.08 N ANISOU 226 N GLU A 34 2364 2227 1898 -16 -39 -180 N ATOM 227 CA GLU A 34 -17.167 16.898 5.380 1.00 20.88 C ANISOU 227 CA GLU A 34 2916 2681 2333 -59 -34 -182 C ATOM 228 C GLU A 34 -16.740 16.106 4.152 1.00 18.73 C ANISOU 228 C GLU A 34 2664 2413 2039 -80 -21 -194 C ATOM 229 O GLU A 34 -15.676 15.503 4.195 1.00 18.22 O ANISOU 229 O GLU A 34 2561 2389 1970 -92 14 -222 O ATOM 230 CB GLU A 34 -16.077 17.897 5.767 1.00 24.65 C ANISOU 230 CB GLU A 34 3403 3177 2786 -100 1 -199 C ATOM 231 CG GLU A 34 -16.619 19.017 6.632 1.00 31.52 C ANISOU 231 CG GLU A 34 4288 4024 3662 -87 -19 -184 C ATOM 232 CD GLU A 34 -15.570 19.991 7.136 1.00 37.27 C ANISOU 232 CD GLU A 34 5025 4768 4364 -130 13 -199 C ATOM 233 OE1 GLU A 34 -14.995 20.728 6.299 1.00 42.10 O ANISOU 233 OE1 GLU A 34 5703 5366 4927 -189 31 -207 O ATOM 234 OE2 GLU A 34 -15.340 20.011 8.360 1.00 37.75 O1- ANISOU 234 OE2 GLU A 34 5034 4855 4452 -110 20 -202 O1- ATOM 235 N GLN A 35 -17.499 16.216 3.062 1.00 19.14 N ANISOU 235 N GLN A 35 2778 2421 2070 -84 -51 -180 N ATOM 236 CA GLN A 35 -17.311 15.442 1.811 1.00 19.60 C ANISOU 236 CA GLN A 35 2867 2473 2105 -101 -46 -187 C ATOM 237 C GLN A 35 -16.925 13.996 2.147 1.00 17.21 C ANISOU 237 C GLN A 35 2494 2211 1832 -73 -31 -202 C ATOM 238 O GLN A 35 -15.892 13.508 1.657 1.00 17.06 O ANISOU 238 O GLN A 35 2466 2221 1792 -95 4 -231 O ATOM 239 CB GLN A 35 -16.315 16.145 0.883 1.00 22.38 C ANISOU 239 CB GLN A 35 3283 2823 2398 -169 -7 -207 C ATOM 240 CG GLN A 35 -16.550 15.779 -0.577 1.00 26.12 C ANISOU 240 CG GLN A 35 3825 3263 2833 -189 -17 -205 C ATOM 241 CD GLN A 35 -15.718 16.585 -1.547 1.00 28.40 C ANISOU 241 CD GLN A 35 4197 3540 3052 -268 21 -222 C ATOM 242 NE2 GLN A 35 -15.462 16.000 -2.709 1.00 28.51 N ANISOU 242 NE2 GLN A 35 4250 3549 3033 -295 37 -235 N ATOM 243 OE1 GLN A 35 -15.326 17.718 -1.261 1.00 30.84 O ANISOU 243 OE1 GLN A 35 4541 3842 3333 -309 37 -225 O ATOM 244 N CYS A 36 -17.723 13.336 2.974 1.00 16.05 N ANISOU 244 N CYS A 36 2302 2065 1728 -29 -59 -187 N ATOM 245 CA CYS A 36 -17.614 11.882 3.271 1.00 16.65 C ANISOU 245 CA CYS A 36 2336 2162 1826 0 -61 -194 C ATOM 246 C CYS A 36 -16.348 11.570 4.091 1.00 16.41 C ANISOU 246 C CYS A 36 2255 2178 1801 6 -27 -224 C ATOM 247 O CYS A 36 -16.003 10.379 4.194 1.00 17.10 O ANISOU 247 O CYS A 36 2319 2279 1896 32 -31 -239 O ATOM 248 CB CYS A 36 -17.580 11.056 1.995 1.00 17.21 C ANISOU 248 CB CYS A 36 2441 2221 1876 -6 -66 -200 C ATOM 249 SG CYS A 36 -18.818 11.510 0.749 1.00 18.01 S ANISOU 249 SG CYS A 36 2615 2265 1960 -18 -108 -173 S ATOM 250 N LYS A 37 -15.695 12.574 4.681 1.00 16.63 N ANISOU 250 N LYS A 37 2269 2226 1824 -12 -3 -235 N ATOM 251 CA LYS A 37 -14.510 12.370 5.565 1.00 17.51 C ANISOU 251 CA LYS A 37 2325 2382 1943 -2 21 -269 C ATOM 252 C LYS A 37 -14.798 12.948 6.948 1.00 15.93 C ANISOU 252 C LYS A 37 2101 2182 1766 12 12 -253 C ATOM 253 O LYS A 37 -15.548 13.930 7.026 1.00 14.76 O ANISOU 253 O LYS A 37 1981 2008 1618 -1 3 -228 O ATOM 254 CB LYS A 37 -13.277 13.091 5.022 1.00 20.86 C ANISOU 254 CB LYS A 37 2747 2840 2335 -50 65 -307 C ATOM 255 CG LYS A 37 -12.956 12.774 3.577 1.00 24.54 C ANISOU 255 CG LYS A 37 3246 3308 2768 -79 85 -327 C ATOM 256 CD LYS A 37 -12.349 11.423 3.447 1.00 27.93 C ANISOU 256 CD LYS A 37 3635 3768 3207 -42 85 -362 C ATOM 257 CE LYS A 37 -11.867 11.113 2.048 1.00 32.58 C ANISOU 257 CE LYS A 37 4249 4368 3761 -72 113 -392 C ATOM 258 NZ LYS A 37 -11.276 9.758 2.016 1.00 36.01 N1+ ANISOU 258 NZ LYS A 37 4641 4832 4207 -23 106 -432 N1+ ATOM 259 N PHE A 38 -14.126 12.463 7.984 1.00 15.14 N ANISOU 259 N PHE A 38 1958 2111 1684 38 14 -273 N ATOM 260 CA PHE A 38 -14.246 13.097 9.320 1.00 15.05 C ANISOU 260 CA PHE A 38 1928 2099 1688 47 10 -262 C ATOM 261 C PHE A 38 -13.720 14.530 9.241 1.00 15.73 C ANISOU 261 C PHE A 38 2023 2196 1756 4 37 -270 C ATOM 262 O PHE A 38 -12.631 14.775 8.689 1.00 15.87 O ANISOU 262 O PHE A 38 2031 2245 1753 -27 66 -305 O ATOM 263 CB PHE A 38 -13.515 12.292 10.395 1.00 15.29 C ANISOU 263 CB PHE A 38 1921 2153 1733 83 1 -286 C ATOM 264 CG PHE A 38 -14.025 10.885 10.557 1.00 14.07 C ANISOU 264 CG PHE A 38 1777 1979 1588 120 -28 -277 C ATOM 265 CD1 PHE A 38 -15.380 10.621 10.670 1.00 13.78 C ANISOU 265 CD1 PHE A 38 1766 1908 1560 120 -45 -237 C ATOM 266 CD2 PHE A 38 -13.140 9.834 10.680 1.00 14.48 C ANISOU 266 CD2 PHE A 38 1814 2048 1638 155 -43 -312 C ATOM 267 CE1 PHE A 38 -15.841 9.328 10.867 1.00 14.07 C ANISOU 267 CE1 PHE A 38 1821 1925 1599 142 -71 -229 C ATOM 268 CE2 PHE A 38 -13.601 8.545 10.875 1.00 14.50 C ANISOU 268 CE2 PHE A 38 1844 2024 1642 187 -76 -302 C ATOM 269 CZ PHE A 38 -14.943 8.292 10.995 1.00 13.95 C ANISOU 269 CZ PHE A 38 1806 1917 1575 175 -87 -259 C ATOM 270 N SER A 39 -14.452 15.452 9.861 1.00 14.88 N ANISOU 270 N SER A 39 1934 2065 1655 2 27 -243 N ATOM 271 CA SER A 39 -14.032 16.863 10.063 1.00 15.80 C ANISOU 271 CA SER A 39 2069 2182 1752 -34 45 -246 C ATOM 272 C SER A 39 -12.736 16.888 10.876 1.00 15.93 C ANISOU 272 C SER A 39 2038 2243 1771 -39 66 -281 C ATOM 273 O SER A 39 -12.491 15.948 11.628 1.00 15.99 O ANISOU 273 O SER A 39 2005 2268 1801 0 53 -293 O ATOM 274 CB SER A 39 -15.109 17.691 10.717 1.00 16.06 C ANISOU 274 CB SER A 39 2126 2181 1795 -19 23 -215 C ATOM 275 OG SER A 39 -16.234 17.847 9.857 1.00 16.89 O ANISOU 275 OG SER A 39 2273 2248 1895 -14 0 -193 O ATOM 276 N ARG A 40 -11.920 17.914 10.673 1.00 19.20 N ANISOU 276 N ARG A 40 2462 2673 2158 -90 93 -301 N ATOM 277 CA ARG A 40 -10.707 18.208 11.486 1.00 20.58 C ANISOU 277 CA ARG A 40 2590 2892 2334 -105 112 -339 C ATOM 278 C ARG A 40 -11.028 18.107 12.991 1.00 17.87 C ANISOU 278 C ARG A 40 2226 2541 2021 -57 86 -323 C ATOM 279 O ARG A 40 -11.970 18.784 13.483 1.00 16.87 O ANISOU 279 O ARG A 40 2136 2377 1897 -50 72 -285 O ATOM 280 CB ARG A 40 -10.195 19.600 11.084 1.00 24.91 C ANISOU 280 CB ARG A 40 3178 3442 2844 -179 142 -347 C ATOM 281 CG ARG A 40 -8.926 20.067 11.776 1.00 29.18 C ANISOU 281 CG ARG A 40 3673 4033 3381 -210 165 -391 C ATOM 282 CD ARG A 40 -8.624 21.513 11.393 1.00 32.10 C ANISOU 282 CD ARG A 40 4101 4390 3703 -293 193 -390 C ATOM 283 NE ARG A 40 -9.318 22.500 12.223 1.00 34.02 N ANISOU 283 NE ARG A 40 4393 4586 3945 -283 169 -351 N ATOM 284 CZ ARG A 40 -10.385 23.228 11.856 1.00 33.94 C ANISOU 284 CZ ARG A 40 4467 4512 3914 -284 147 -308 C ATOM 285 NH1 ARG A 40 -10.918 23.092 10.653 1.00 35.37 N1+ ANISOU 285 NH1 ARG A 40 4699 4664 4074 -296 144 -294 N1+ ATOM 286 NH2 ARG A 40 -10.896 24.120 12.687 1.00 31.80 N ANISOU 286 NH2 ARG A 40 4233 4206 3643 -270 125 -282 N ATOM 287 N ALA A 41 -10.176 17.395 13.734 1.00 17.55 N ANISOU 287 N ALA A 41 2132 2537 1999 -28 79 -357 N ATOM 288 CA ALA A 41 -10.160 17.392 15.210 1.00 16.49 C ANISOU 288 CA ALA A 41 1984 2399 1883 5 57 -351 C ATOM 289 C ALA A 41 -10.081 18.840 15.709 1.00 15.95 C ANISOU 289 C ALA A 41 1936 2322 1800 -32 71 -341 C ATOM 290 O ALA A 41 -9.201 19.561 15.264 1.00 17.51 O ANISOU 290 O ALA A 41 2126 2548 1976 -84 97 -370 O ATOM 291 CB ALA A 41 -8.994 16.579 15.714 1.00 17.42 C ANISOU 291 CB ALA A 41 2046 2558 2013 36 44 -402 C ATOM 292 N GLY A 42 -10.970 19.236 16.617 1.00 14.47 N ANISOU 292 N GLY A 42 1777 2099 1620 -12 55 -305 N ATOM 293 CA GLY A 42 -10.926 20.556 17.271 1.00 15.08 C ANISOU 293 CA GLY A 42 1880 2164 1685 -37 61 -295 C ATOM 294 C GLY A 42 -11.821 21.574 16.595 1.00 14.87 C ANISOU 294 C GLY A 42 1913 2097 1637 -62 65 -265 C ATOM 295 O GLY A 42 -12.021 22.647 17.174 1.00 16.03 O ANISOU 295 O GLY A 42 2094 2224 1773 -73 62 -252 O ATOM 296 N LYS A 43 -12.450 21.210 15.478 1.00 15.27 N ANISOU 296 N LYS A 43 1983 2132 1684 -62 63 -253 N ATOM 297 CA LYS A 43 -13.396 22.140 14.807 1.00 15.80 C ANISOU 297 CA LYS A 43 2116 2155 1732 -74 52 -227 C ATOM 298 C LYS A 43 -14.687 22.256 15.630 1.00 14.34 C ANISOU 298 C LYS A 43 1937 1941 1569 -24 27 -201 C ATOM 299 O LYS A 43 -15.311 21.230 15.931 1.00 13.50 O ANISOU 299 O LYS A 43 1796 1840 1491 12 19 -194 O ATOM 300 CB LYS A 43 -13.702 21.703 13.380 1.00 17.31 C ANISOU 300 CB LYS A 43 2329 2336 1911 -86 52 -224 C ATOM 301 CG LYS A 43 -14.502 22.723 12.576 1.00 19.08 C ANISOU 301 CG LYS A 43 2633 2509 2106 -101 32 -204 C ATOM 302 CD LYS A 43 -15.050 22.222 11.246 1.00 20.76 C ANISOU 302 CD LYS A 43 2873 2702 2310 -101 20 -197 C ATOM 303 CE LYS A 43 -16.412 21.546 11.316 1.00 22.26 C ANISOU 303 CE LYS A 43 3045 2876 2537 -41 -12 -178 C ATOM 304 NZ LYS A 43 -17.505 22.415 11.847 1.00 23.30 N1+ ANISOU 304 NZ LYS A 43 3202 2973 2676 -5 -45 -165 N1+ ATOM 305 N ILE A 44 -15.128 23.481 15.895 1.00 13.77 N ANISOU 305 N ILE A 44 1912 1837 1481 -26 15 -190 N ATOM 306 CA ILE A 44 -16.395 23.728 16.631 1.00 14.07 C ANISOU 306 CA ILE A 44 1952 1852 1539 22 -6 -176 C ATOM 307 C ILE A 44 -17.524 23.086 15.842 1.00 13.72 C ANISOU 307 C ILE A 44 1902 1797 1512 50 -25 -169 C ATOM 308 O ILE A 44 -17.606 23.308 14.594 1.00 14.32 O ANISOU 308 O ILE A 44 2020 1853 1568 34 -37 -166 O ATOM 309 CB ILE A 44 -16.617 25.237 16.839 1.00 15.30 C ANISOU 309 CB ILE A 44 2171 1973 1670 18 -22 -172 C ATOM 310 CG1 ILE A 44 -15.710 25.768 17.940 1.00 17.61 C ANISOU 310 CG1 ILE A 44 2460 2278 1952 0 -5 -179 C ATOM 311 CG2 ILE A 44 -18.082 25.549 17.090 1.00 15.66 C ANISOU 311 CG2 ILE A 44 2223 1993 1732 74 -52 -168 C ATOM 312 CD1 ILE A 44 -16.256 25.576 19.338 1.00 18.51 C ANISOU 312 CD1 ILE A 44 2540 2399 2093 42 -6 -177 C ATOM 313 N CYS A 45 -18.397 22.345 16.514 1.00 12.43 N ANISOU 313 N CYS A 45 1695 1645 1381 87 -27 -166 N ATOM 314 CA CYS A 45 -19.578 21.733 15.858 1.00 12.78 C ANISOU 314 CA CYS A 45 1726 1684 1445 111 -46 -164 C ATOM 315 C CYS A 45 -20.889 21.986 16.612 1.00 13.11 C ANISOU 315 C CYS A 45 1744 1725 1509 150 -58 -171 C ATOM 316 O CYS A 45 -21.971 21.737 16.023 1.00 14.39 O ANISOU 316 O CYS A 45 1895 1884 1688 172 -80 -178 O ATOM 317 CB CYS A 45 -19.348 20.250 15.605 1.00 12.17 C ANISOU 317 CB CYS A 45 1612 1630 1381 104 -34 -162 C ATOM 318 SG CYS A 45 -18.824 19.296 17.052 1.00 12.48 S ANISOU 318 SG CYS A 45 1612 1696 1433 106 -10 -165 S ATOM 319 N ARG A 46 -20.855 22.536 17.816 1.00 13.91 N ANISOU 319 N ARG A 46 1841 1831 1611 160 -47 -176 N ATOM 320 CA ARG A 46 -22.105 22.864 18.549 1.00 15.08 C ANISOU 320 CA ARG A 46 1964 1984 1779 196 -53 -192 C ATOM 321 C ARG A 46 -21.822 23.986 19.539 1.00 16.77 C ANISOU 321 C ARG A 46 2203 2187 1979 206 -49 -196 C ATOM 322 O ARG A 46 -20.813 23.929 20.263 1.00 16.45 O ANISOU 322 O ARG A 46 2170 2153 1927 181 -26 -187 O ATOM 323 CB ARG A 46 -22.680 21.639 19.256 1.00 15.39 C ANISOU 323 CB ARG A 46 1949 2056 1842 192 -27 -197 C ATOM 324 CG ARG A 46 -24.025 21.888 19.924 1.00 15.51 C ANISOU 324 CG ARG A 46 1926 2088 1877 220 -24 -224 C ATOM 325 CD ARG A 46 -24.535 20.659 20.648 1.00 15.63 C ANISOU 325 CD ARG A 46 1899 2135 1905 197 9 -229 C ATOM 326 NE ARG A 46 -24.742 19.484 19.813 1.00 16.02 N ANISOU 326 NE ARG A 46 1932 2190 1962 178 5 -222 N ATOM 327 CZ ARG A 46 -23.968 18.399 19.801 1.00 16.32 C ANISOU 327 CZ ARG A 46 1985 2226 1989 148 17 -201 C ATOM 328 NH1 ARG A 46 -22.874 18.344 20.537 1.00 16.42 N1+ ANISOU 328 NH1 ARG A 46 2024 2230 1983 137 30 -187 N1+ ATOM 329 NH2 ARG A 46 -24.268 17.390 19.009 1.00 17.87 N ANISOU 329 NH2 ARG A 46 2170 2425 2191 134 10 -197 N ATOM 330 N ILE A 47 -22.632 25.037 19.458 1.00 18.20 N ANISOU 330 N ILE A 47 2405 2349 2159 243 -78 -213 N ATOM 331 CA ILE A 47 -22.503 26.201 20.367 1.00 20.17 C ANISOU 331 CA ILE A 47 2687 2582 2393 259 -81 -220 C ATOM 332 C ILE A 47 -23.794 26.312 21.160 1.00 20.25 C ANISOU 332 C ILE A 47 2651 2613 2428 305 -79 -252 C ATOM 333 O ILE A 47 -24.887 26.426 20.605 1.00 21.51 O ANISOU 333 O ILE A 47 2790 2776 2606 344 -108 -277 O ATOM 334 CB ILE A 47 -22.143 27.462 19.575 1.00 22.39 C ANISOU 334 CB ILE A 47 3051 2815 2640 262 -120 -216 C ATOM 335 CG1 ILE A 47 -23.141 27.726 18.455 1.00 24.42 C ANISOU 335 CG1 ILE A 47 3326 3048 2901 301 -170 -231 C ATOM 336 CG2 ILE A 47 -20.710 27.359 19.064 1.00 22.57 C ANISOU 336 CG2 ILE A 47 3110 2831 2634 200 -104 -192 C ATOM 337 CD1 ILE A 47 -23.670 29.143 18.466 1.00 27.33 C ANISOU 337 CD1 ILE A 47 3760 3373 3250 349 -220 -250 C ATOM 338 N PRO A 48 -23.687 26.164 22.491 1.00 20.55 N ANISOU 338 N PRO A 48 2666 2672 2467 297 -42 -255 N ATOM 339 CA PRO A 48 -24.806 26.398 23.392 1.00 22.27 C ANISOU 339 CA PRO A 48 2844 2913 2702 332 -31 -291 C ATOM 340 C PRO A 48 -25.053 27.905 23.541 1.00 22.60 C ANISOU 340 C PRO A 48 2931 2924 2729 380 -66 -311 C ATOM 341 O PRO A 48 -24.245 28.714 23.094 1.00 22.20 O ANISOU 341 O PRO A 48 2952 2831 2650 374 -94 -291 O ATOM 342 CB PRO A 48 -24.334 25.776 24.712 1.00 22.21 C ANISOU 342 CB PRO A 48 2823 2926 2688 296 19 -281 C ATOM 343 CG PRO A 48 -22.836 25.978 24.678 1.00 22.48 C ANISOU 343 CG PRO A 48 2911 2933 2696 265 14 -246 C ATOM 344 CD PRO A 48 -22.428 25.926 23.214 1.00 21.83 C ANISOU 344 CD PRO A 48 2848 2833 2611 256 -14 -230 C ATOM 345 N ARG A 49 -26.184 28.253 24.139 1.00 27.75 N ANISOU 345 N ARG A 49 3544 3600 3400 426 -65 -356 N ATOM 346 CA ARG A 49 -26.374 29.591 24.754 1.00 30.21 C ANISOU 346 CA ARG A 49 3895 3888 3695 474 -88 -379 C ATOM 347 C ARG A 49 -25.753 29.592 26.149 1.00 32.46 C ANISOU 347 C ARG A 49 4188 4180 3963 443 -39 -367 C ATOM 348 O ARG A 49 -25.597 28.497 26.738 1.00 36.64 O ANISOU 348 O ARG A 49 4677 4742 4500 398 10 -355 O ATOM 349 CB ARG A 49 -27.857 29.912 24.875 1.00 33.23 C ANISOU 349 CB ARG A 49 4218 4300 4105 541 -104 -444 C ATOM 350 CG ARG A 49 -28.661 29.505 23.658 1.00 32.10 C ANISOU 350 CG ARG A 49 4038 4168 3990 567 -143 -465 C ATOM 351 CD ARG A 49 -30.083 29.830 24.011 1.00 32.33 C ANISOU 351 CD ARG A 49 3994 4239 4049 634 -154 -541 C ATOM 352 NE ARG A 49 -30.828 29.926 22.799 1.00 31.89 N ANISOU 352 NE ARG A 49 3926 4176 4013 683 -219 -569 N ATOM 353 CZ ARG A 49 -32.087 30.285 22.742 1.00 27.75 C ANISOU 353 CZ ARG A 49 3340 3684 3519 756 -253 -644 C ATOM 354 NH1 ARG A 49 -32.711 30.687 23.835 1.00 27.56 N1+ ANISOU 354 NH1 ARG A 49 3265 3700 3505 789 -226 -699 N1+ ATOM 355 NH2 ARG A 49 -32.677 30.284 21.574 1.00 28.29 N ANISOU 355 NH2 ARG A 49 3402 3740 3604 798 -319 -666 N ATOM 356 N GLY A 50 -25.450 30.780 26.662 1.00 35.05 N ANISOU 356 N GLY A 50 4577 4474 4265 467 -59 -370 N ATOM 357 CA GLY A 50 -24.703 30.959 27.917 1.00 37.34 C ANISOU 357 CA GLY A 50 4894 4760 4533 439 -24 -354 C ATOM 358 C GLY A 50 -23.306 30.379 27.799 1.00 37.91 C ANISOU 358 C GLY A 50 4993 4820 4589 373 -10 -304 C ATOM 359 O GLY A 50 -22.848 30.162 26.660 1.00 40.13 O ANISOU 359 O GLY A 50 5288 5089 4870 353 -32 -283 O ATOM 360 N ASP A 51 -22.685 30.069 28.935 1.00 39.36 N ANISOU 360 N ASP A 51 5181 5012 4761 341 24 -291 N ATOM 361 CA ASP A 51 -21.216 29.870 29.044 1.00 40.34 C ANISOU 361 CA ASP A 51 5341 5121 4866 290 27 -255 C ATOM 362 C ASP A 51 -20.888 28.382 29.171 1.00 38.72 C ANISOU 362 C ASP A 51 5092 4944 4673 254 56 -240 C ATOM 363 O ASP A 51 -19.716 28.080 29.484 1.00 41.45 O ANISOU 363 O ASP A 51 5457 5285 5007 220 57 -220 O ATOM 364 CB ASP A 51 -20.650 30.658 30.224 1.00 42.19 C ANISOU 364 CB ASP A 51 5621 5335 5072 287 31 -253 C ATOM 365 CG ASP A 51 -20.843 32.158 30.086 1.00 43.00 C ANISOU 365 CG ASP A 51 5784 5400 5154 321 -3 -265 C ATOM 366 OD1 ASP A 51 -20.973 32.632 28.921 1.00 39.11 O ANISOU 366 OD1 ASP A 51 5314 4885 4658 332 -39 -264 O ATOM 367 OD2 ASP A 51 -20.868 32.838 31.143 1.00 46.19 O1- ANISOU 367 OD2 ASP A 51 6218 5791 5540 335 1 -275 O1- ATOM 368 N MET A 52 -21.866 27.498 28.930 1.00 37.54 N ANISOU 368 N MET A 52 4891 4824 4548 260 73 -254 N ATOM 369 CA MET A 52 -21.654 26.027 28.832 1.00 37.99 C ANISOU 369 CA MET A 52 4918 4901 4613 226 93 -240 C ATOM 370 C MET A 52 -20.604 25.764 27.759 1.00 30.42 C ANISOU 370 C MET A 52 3971 3932 3655 206 69 -217 C ATOM 371 O MET A 52 -20.457 26.549 26.833 1.00 30.56 O ANISOU 371 O MET A 52 4007 3934 3671 216 42 -215 O ATOM 372 CB MET A 52 -22.943 25.291 28.466 1.00 45.45 C ANISOU 372 CB MET A 52 5809 5876 5582 232 110 -261 C ATOM 373 CG MET A 52 -23.696 24.749 29.668 1.00 54.46 C ANISOU 373 CG MET A 52 6931 7041 6718 217 155 -281 C ATOM 374 SD MET A 52 -25.277 23.986 29.195 1.00 69.54 S ANISOU 374 SD MET A 52 8767 8997 8655 215 179 -317 S ATOM 375 CE MET A 52 -24.732 22.726 28.039 1.00 61.98 C ANISOU 375 CE MET A 52 7807 8033 7707 185 161 -284 C ATOM 376 N PRO A 53 -19.744 24.732 27.902 1.00 24.35 N ANISOU 376 N PRO A 53 3200 3169 2883 178 74 -201 N ATOM 377 CA PRO A 53 -18.677 24.544 26.928 1.00 22.12 C ANISOU 377 CA PRO A 53 2919 2883 2599 160 55 -189 C ATOM 378 C PRO A 53 -19.266 24.217 25.543 1.00 19.04 C ANISOU 378 C PRO A 53 2506 2499 2226 165 45 -189 C ATOM 379 O PRO A 53 -20.262 23.498 25.436 1.00 18.66 O ANISOU 379 O PRO A 53 2429 2466 2195 173 56 -195 O ATOM 380 CB PRO A 53 -17.812 23.404 27.503 1.00 22.97 C ANISOU 380 CB PRO A 53 3026 2999 2703 143 58 -184 C ATOM 381 CG PRO A 53 -18.660 22.762 28.597 1.00 25.78 C ANISOU 381 CG PRO A 53 3383 3356 3054 144 81 -187 C ATOM 382 CD PRO A 53 -19.691 23.784 29.024 1.00 25.81 C ANISOU 382 CD PRO A 53 3387 3359 3058 162 96 -200 C ATOM 383 N ASP A 54 -18.621 24.734 24.504 1.00 17.84 N ANISOU 383 N ASP A 54 2372 2338 2067 154 27 -184 N ATOM 384 CA ASP A 54 -18.868 24.318 23.103 1.00 17.88 C ANISOU 384 CA ASP A 54 2365 2345 2081 151 16 -181 C ATOM 385 C ASP A 54 -18.400 22.873 22.905 1.00 16.81 C ANISOU 385 C ASP A 54 2200 2230 1955 135 25 -177 C ATOM 386 O ASP A 54 -17.519 22.380 23.664 1.00 17.82 O ANISOU 386 O ASP A 54 2326 2366 2078 125 31 -177 O ATOM 387 CB ASP A 54 -18.118 25.190 22.110 1.00 20.08 C ANISOU 387 CB ASP A 54 2684 2607 2339 129 0 -178 C ATOM 388 CG ASP A 54 -18.379 26.653 22.382 1.00 23.94 C ANISOU 388 CG ASP A 54 3221 3065 2808 142 -16 -182 C ATOM 389 OD1 ASP A 54 -19.563 26.975 22.654 1.00 24.87 O ANISOU 389 OD1 ASP A 54 3335 3175 2937 183 -26 -192 O ATOM 390 OD2 ASP A 54 -17.393 27.421 22.442 1.00 25.74 O1- ANISOU 390 OD2 ASP A 54 3488 3281 3009 111 -17 -180 O1- ATOM 391 N ASP A 55 -18.888 22.256 21.846 1.00 14.67 N ANISOU 391 N ASP A 55 1914 1963 1696 137 18 -175 N ATOM 392 CA ASP A 55 -18.422 20.920 21.432 1.00 13.86 C ANISOU 392 CA ASP A 55 1791 1874 1598 125 21 -172 C ATOM 393 C ASP A 55 -17.617 21.058 20.133 1.00 13.87 C ANISOU 393 C ASP A 55 1802 1875 1591 106 13 -173 C ATOM 394 O ASP A 55 -17.970 21.900 19.279 1.00 14.55 O ANISOU 394 O ASP A 55 1912 1946 1669 104 2 -171 O ATOM 395 CB ASP A 55 -19.594 19.955 21.291 1.00 14.39 C ANISOU 395 CB ASP A 55 1836 1947 1683 133 25 -171 C ATOM 396 CG ASP A 55 -20.415 19.805 22.556 1.00 15.47 C ANISOU 396 CG ASP A 55 1964 2089 1822 137 43 -176 C ATOM 397 OD1 ASP A 55 -19.817 19.461 23.618 1.00 17.19 O ANISOU 397 OD1 ASP A 55 2196 2305 2027 129 52 -174 O ATOM 398 OD2 ASP A 55 -21.655 20.022 22.477 1.00 17.58 O1- ANISOU 398 OD2 ASP A 55 2210 2363 2103 148 47 -187 O1- ATOM 399 N ARG A 56 -16.618 20.201 19.997 1.00 13.28 N ANISOU 399 N ARG A 56 1713 1818 1514 96 15 -180 N ATOM 400 CA ARG A 56 -15.685 20.184 18.844 1.00 13.61 C ANISOU 400 CA ARG A 56 1755 1870 1545 72 16 -190 C ATOM 401 C ARG A 56 -15.573 18.770 18.294 1.00 12.62 C ANISOU 401 C ARG A 56 1608 1757 1429 80 13 -195 C ATOM 402 O ARG A 56 -15.679 17.809 19.072 1.00 11.11 O ANISOU 402 O ARG A 56 1406 1567 1246 99 7 -194 O ATOM 403 CB ARG A 56 -14.299 20.664 19.265 1.00 15.91 C ANISOU 403 CB ARG A 56 2040 2180 1823 51 24 -210 C ATOM 404 CG ARG A 56 -14.274 22.137 19.631 1.00 17.96 C ANISOU 404 CG ARG A 56 2333 2424 2066 34 27 -205 C ATOM 405 CD ARG A 56 -13.040 22.493 20.430 1.00 19.90 C ANISOU 405 CD ARG A 56 2568 2690 2303 16 32 -225 C ATOM 406 NE ARG A 56 -13.139 23.882 20.848 1.00 22.91 N ANISOU 406 NE ARG A 56 2989 3049 2665 0 32 -218 N ATOM 407 CZ ARG A 56 -12.751 24.926 20.123 1.00 25.30 C ANISOU 407 CZ ARG A 56 3330 3343 2939 -43 38 -222 C ATOM 408 NH1 ARG A 56 -12.177 24.772 18.935 1.00 26.31 N1+ ANISOU 408 NH1 ARG A 56 3455 3486 3052 -82 51 -235 N1+ ATOM 409 NH2 ARG A 56 -12.951 26.143 20.605 1.00 27.90 N ANISOU 409 NH2 ARG A 56 3707 3644 3249 -51 32 -213 N ATOM 410 N CYS A 57 -15.387 18.673 16.977 1.00 13.01 N ANISOU 410 N CYS A 57 1662 1810 1472 64 14 -199 N ATOM 411 CA CYS A 57 -15.168 17.388 16.275 1.00 12.79 C ANISOU 411 CA CYS A 57 1617 1792 1448 72 10 -207 C ATOM 412 C CYS A 57 -13.930 16.687 16.854 1.00 13.79 C ANISOU 412 C CYS A 57 1717 1945 1575 83 8 -235 C ATOM 413 O CYS A 57 -12.991 17.362 17.298 1.00 13.39 O ANISOU 413 O CYS A 57 1655 1913 1518 70 15 -254 O ATOM 414 CB CYS A 57 -15.053 17.636 14.778 1.00 13.49 C ANISOU 414 CB CYS A 57 1723 1880 1522 47 15 -211 C ATOM 415 SG CYS A 57 -16.546 18.402 14.089 1.00 14.45 S ANISOU 415 SG CYS A 57 1884 1964 1643 48 0 -184 S ATOM 416 N THR A 58 -13.901 15.363 16.781 1.00 14.57 N ANISOU 416 N THR A 58 1810 2046 1681 107 -6 -241 N ATOM 417 CA THR A 58 -12.794 14.553 17.336 1.00 15.27 C ANISOU 417 CA THR A 58 1878 2152 1769 132 -23 -273 C ATOM 418 C THR A 58 -11.768 14.206 16.261 1.00 16.73 C ANISOU 418 C THR A 58 2035 2371 1950 129 -17 -311 C ATOM 419 O THR A 58 -10.643 13.806 16.630 1.00 17.36 O ANISOU 419 O THR A 58 2085 2478 2031 152 -31 -353 O ATOM 420 CB THR A 58 -13.331 13.284 17.995 1.00 16.21 C ANISOU 420 CB THR A 58 2022 2246 1890 163 -49 -261 C ATOM 421 CG2 THR A 58 -14.442 13.534 18.987 1.00 17.14 C ANISOU 421 CG2 THR A 58 2166 2336 2008 156 -45 -228 C ATOM 422 OG1 THR A 58 -13.778 12.414 16.953 1.00 16.39 O ANISOU 422 OG1 THR A 58 2053 2261 1911 166 -54 -255 O ATOM 423 N GLY A 59 -12.142 14.216 14.988 1.00 15.98 N ANISOU 423 N GLY A 59 1948 2273 1848 108 -3 -303 N ATOM 424 CA GLY A 59 -11.267 13.717 13.919 1.00 16.77 C ANISOU 424 CA GLY A 59 2026 2405 1941 104 5 -342 C ATOM 425 C GLY A 59 -11.483 12.236 13.658 1.00 16.89 C ANISOU 425 C GLY A 59 2049 2407 1960 145 -21 -345 C ATOM 426 O GLY A 59 -10.939 11.732 12.660 1.00 17.05 O ANISOU 426 O GLY A 59 2055 2448 1973 146 -15 -375 O ATOM 427 N GLN A 60 -12.229 11.540 14.520 1.00 16.98 N ANISOU 427 N GLN A 60 2088 2384 1978 173 -49 -318 N ATOM 428 CA GLN A 60 -12.401 10.068 14.402 1.00 17.93 C ANISOU 428 CA GLN A 60 2231 2484 2094 209 -81 -321 C ATOM 429 C GLN A 60 -13.869 9.653 14.470 1.00 15.73 C ANISOU 429 C GLN A 60 1996 2164 1816 197 -87 -273 C ATOM 430 O GLN A 60 -14.116 8.437 14.474 1.00 15.96 O ANISOU 430 O GLN A 60 2057 2170 1837 218 -114 -270 O ATOM 431 CB GLN A 60 -11.632 9.350 15.497 1.00 22.74 C ANISOU 431 CB GLN A 60 2844 3092 2702 256 -118 -349 C ATOM 432 CG GLN A 60 -10.133 9.557 15.373 1.00 28.23 C ANISOU 432 CG GLN A 60 3485 3838 3402 276 -119 -412 C ATOM 433 CD GLN A 60 -9.644 10.593 16.346 1.00 33.53 C ANISOU 433 CD GLN A 60 4131 4527 4079 264 -111 -420 C ATOM 434 NE2 GLN A 60 -8.852 11.537 15.850 1.00 34.19 N ANISOU 434 NE2 GLN A 60 4164 4658 4165 232 -77 -452 N ATOM 435 OE1 GLN A 60 -9.928 10.511 17.543 1.00 41.45 O ANISOU 435 OE1 GLN A 60 5165 5502 5082 280 -134 -401 O ATOM 436 N SER A 61 -14.791 10.606 14.346 1.00 14.27 N ANISOU 436 N SER A 61 1810 1972 1637 164 -65 -242 N ATOM 437 CA SER A 61 -16.254 10.394 14.442 1.00 13.82 C ANISOU 437 CA SER A 61 1777 1887 1585 148 -67 -206 C ATOM 438 C SER A 61 -16.926 11.469 13.598 1.00 13.41 C ANISOU 438 C SER A 61 1717 1838 1540 123 -50 -192 C ATOM 439 O SER A 61 -16.417 12.597 13.592 1.00 11.96 O ANISOU 439 O SER A 61 1520 1667 1355 113 -35 -200 O ATOM 440 CB SER A 61 -16.747 10.445 15.863 1.00 14.58 C ANISOU 440 CB SER A 61 1885 1971 1682 147 -68 -193 C ATOM 441 OG SER A 61 -18.174 10.580 15.907 1.00 16.86 O ANISOU 441 OG SER A 61 2178 2248 1979 124 -59 -168 O ATOM 442 N ALA A 62 -18.080 11.161 13.015 1.00 14.27 N ANISOU 442 N ALA A 62 1836 1930 1655 113 -58 -173 N ATOM 443 CA ALA A 62 -18.832 12.108 12.167 1.00 14.11 C ANISOU 443 CA ALA A 62 1816 1904 1639 99 -56 -163 C ATOM 444 C ALA A 62 -19.875 12.844 13.000 1.00 13.57 C ANISOU 444 C ALA A 62 1736 1833 1586 97 -53 -152 C ATOM 445 O ALA A 62 -20.476 13.796 12.473 1.00 14.09 O ANISOU 445 O ALA A 62 1804 1891 1657 96 -60 -149 O ATOM 446 CB ALA A 62 -19.484 11.378 11.033 1.00 15.82 C ANISOU 446 CB ALA A 62 2048 2107 1855 94 -72 -156 C ATOM 447 N ASP A 63 -20.037 12.475 14.262 1.00 13.54 N ANISOU 447 N ASP A 63 1725 1832 1586 99 -46 -151 N ATOM 448 CA ASP A 63 -21.029 13.150 15.135 1.00 14.25 C ANISOU 448 CA ASP A 63 1798 1926 1689 96 -37 -148 C ATOM 449 C ASP A 63 -20.314 14.223 15.951 1.00 13.48 C ANISOU 449 C ASP A 63 1699 1834 1587 103 -25 -153 C ATOM 450 O ASP A 63 -19.069 14.186 16.116 1.00 14.19 O ANISOU 450 O ASP A 63 1797 1929 1666 107 -23 -159 O ATOM 451 CB ASP A 63 -21.796 12.166 16.014 1.00 16.03 C ANISOU 451 CB ASP A 63 2024 2152 1915 81 -30 -146 C ATOM 452 CG ASP A 63 -22.953 11.486 15.307 1.00 18.20 C ANISOU 452 CG ASP A 63 2289 2426 2198 65 -39 -145 C ATOM 453 OD1 ASP A 63 -23.065 11.654 14.054 1.00 22.55 O ANISOU 453 OD1 ASP A 63 2838 2972 2755 73 -58 -144 O ATOM 454 OD2 ASP A 63 -23.772 10.825 16.011 1.00 20.87 O1- ANISOU 454 OD2 ASP A 63 2623 2768 2535 39 -27 -147 O1- ATOM 455 N CYS A 64 -21.080 15.208 16.394 1.00 13.10 N ANISOU 455 N CYS A 64 1639 1787 1549 108 -20 -154 N ATOM 456 CA CYS A 64 -20.566 16.257 17.288 1.00 12.76 C ANISOU 456 CA CYS A 64 1600 1747 1501 113 -10 -158 C ATOM 457 C CYS A 64 -20.721 15.746 18.717 1.00 12.65 C ANISOU 457 C CYS A 64 1583 1738 1485 109 5 -158 C ATOM 458 O CYS A 64 -21.844 15.482 19.166 1.00 13.25 O ANISOU 458 O CYS A 64 1645 1820 1569 102 15 -162 O ATOM 459 CB CYS A 64 -21.305 17.563 17.066 1.00 13.45 C ANISOU 459 CB CYS A 64 1687 1828 1595 126 -18 -163 C ATOM 460 SG CYS A 64 -20.561 18.943 17.962 1.00 13.38 S ANISOU 460 SG CYS A 64 1697 1814 1573 130 -10 -165 S ATOM 461 N PRO A 65 -19.607 15.528 19.443 1.00 12.02 N ANISOU 461 N PRO A 65 1519 1657 1391 110 8 -159 N ATOM 462 CA PRO A 65 -19.676 14.905 20.763 1.00 11.99 C ANISOU 462 CA PRO A 65 1531 1648 1377 104 16 -158 C ATOM 463 C PRO A 65 -20.332 15.798 21.818 1.00 12.45 C ANISOU 463 C PRO A 65 1584 1708 1435 101 36 -161 C ATOM 464 O PRO A 65 -20.527 16.999 21.578 1.00 12.88 O ANISOU 464 O PRO A 65 1624 1768 1499 112 37 -165 O ATOM 465 CB PRO A 65 -18.207 14.627 21.121 1.00 12.02 C ANISOU 465 CB PRO A 65 1552 1647 1366 116 1 -165 C ATOM 466 CG PRO A 65 -17.462 15.720 20.374 1.00 11.82 C ANISOU 466 CG PRO A 65 1509 1635 1347 120 1 -172 C ATOM 467 CD PRO A 65 -18.241 15.925 19.090 1.00 11.81 C ANISOU 467 CD PRO A 65 1496 1634 1356 114 1 -166 C ATOM 468 N ARG A 66 -20.671 15.226 22.975 1.00 13.09 N ANISOU 468 N ARG A 66 1685 1785 1502 86 51 -161 N ATOM 469 CA ARG A 66 -21.192 16.016 24.115 1.00 13.63 C ANISOU 469 CA ARG A 66 1753 1858 1567 81 75 -168 C ATOM 470 C ARG A 66 -20.435 15.684 25.404 1.00 14.72 C ANISOU 470 C ARG A 66 1937 1977 1677 76 75 -164 C ATOM 471 O ARG A 66 -20.075 14.513 25.587 1.00 15.48 O ANISOU 471 O ARG A 66 2070 2056 1754 66 62 -159 O ATOM 472 CB ARG A 66 -22.685 15.779 24.355 1.00 13.77 C ANISOU 472 CB ARG A 66 1747 1892 1590 58 103 -180 C ATOM 473 CG ARG A 66 -23.534 16.038 23.130 1.00 14.32 C ANISOU 473 CG ARG A 66 1771 1980 1688 68 94 -190 C ATOM 474 CD ARG A 66 -24.990 15.862 23.462 1.00 15.51 C ANISOU 474 CD ARG A 66 1886 2159 1848 46 123 -214 C ATOM 475 NE ARG A 66 -25.853 16.111 22.321 1.00 15.68 N ANISOU 475 NE ARG A 66 1859 2198 1898 62 106 -230 N ATOM 476 CZ ARG A 66 -26.466 17.257 22.071 1.00 16.80 C ANISOU 476 CZ ARG A 66 1966 2354 2063 98 95 -253 C ATOM 477 NH1 ARG A 66 -26.187 18.335 22.773 1.00 17.15 N1+ ANISOU 477 NH1 ARG A 66 2020 2393 2101 123 99 -259 N1+ ATOM 478 NH2 ARG A 66 -27.313 17.330 21.066 1.00 17.97 N ANISOU 478 NH2 ARG A 66 2076 2516 2235 114 72 -272 N ATOM 479 N TYR A 67 -20.189 16.717 26.209 1.00 16.12 N ANISOU 479 N TYR A 67 2119 2154 1850 85 83 -168 N ATOM 480 CA TYR A 67 -19.604 16.624 27.570 1.00 18.67 C ANISOU 480 CA TYR A 67 2489 2458 2146 81 82 -167 C ATOM 481 C TYR A 67 -20.694 16.137 28.511 1.00 22.26 C ANISOU 481 C TYR A 67 2966 2910 2580 46 117 -171 C ATOM 482 O TYR A 67 -21.854 16.591 28.391 1.00 24.22 O ANISOU 482 O TYR A 67 3175 3183 2843 36 148 -184 O ATOM 483 CB TYR A 67 -19.065 17.970 28.051 1.00 18.33 C ANISOU 483 CB TYR A 67 2442 2415 2104 99 81 -171 C ATOM 484 CG TYR A 67 -17.768 18.376 27.407 1.00 18.66 C ANISOU 484 CG TYR A 67 2474 2460 2155 118 51 -172 C ATOM 485 CD1 TYR A 67 -16.651 17.571 27.531 1.00 19.34 C ANISOU 485 CD1 TYR A 67 2579 2537 2232 126 21 -177 C ATOM 486 CD2 TYR A 67 -17.684 19.486 26.581 1.00 18.63 C ANISOU 486 CD2 TYR A 67 2443 2466 2166 125 50 -175 C ATOM 487 CE1 TYR A 67 -15.470 17.870 26.884 1.00 19.51 C ANISOU 487 CE1 TYR A 67 2578 2572 2262 138 0 -188 C ATOM 488 CE2 TYR A 67 -16.504 19.791 25.908 1.00 20.97 C ANISOU 488 CE2 TYR A 67 2731 2771 2466 127 31 -180 C ATOM 489 CZ TYR A 67 -15.374 19.018 26.122 1.00 20.93 C ANISOU 489 CZ TYR A 67 2730 2767 2454 132 9 -190 C ATOM 490 OH TYR A 67 -14.213 19.261 25.456 1.00 22.31 O ANISOU 490 OH TYR A 67 2883 2960 2633 130 -4 -206 O ATOM 491 N HIS A 68 -20.377 15.137 29.317 1.00 25.32 N ANISOU 491 N HIS A 68 3417 3270 2933 27 110 -165 N ATOM 492 CA HIS A 68 -21.373 14.536 30.238 1.00 28.70 C ANISOU 492 CA HIS A 68 3883 3691 3329 -22 148 -169 C ATOM 493 C HIS A 68 -20.685 14.015 31.492 1.00 30.93 C ANISOU 493 C HIS A 68 4256 3930 3563 -33 133 -162 C ATOM 494 O HIS A 68 -19.470 14.090 31.614 1.00 29.01 O ANISOU 494 O HIS A 68 4038 3666 3318 4 87 -158 O ATOM 495 CB HIS A 68 -22.109 13.430 29.503 1.00 28.31 C ANISOU 495 CB HIS A 68 3829 3647 3279 -55 156 -168 C ATOM 496 CG HIS A 68 -21.201 12.332 29.073 1.00 28.29 C ANISOU 496 CG HIS A 68 3875 3612 3262 -41 108 -154 C ATOM 497 CD2 HIS A 68 -20.941 11.125 29.629 1.00 26.61 C ANISOU 497 CD2 HIS A 68 3751 3355 3003 -64 88 -146 C ATOM 498 ND1 HIS A 68 -20.430 12.423 27.922 1.00 27.41 N ANISOU 498 ND1 HIS A 68 3725 3507 3181 2 71 -151 N ATOM 499 CE1 HIS A 68 -19.758 11.291 27.773 1.00 25.90 C ANISOU 499 CE1 HIS A 68 3587 3285 2968 10 32 -146 C ATOM 500 NE2 HIS A 68 -20.066 10.475 28.802 1.00 27.87 N ANISOU 500 NE2 HIS A 68 3919 3500 3171 -26 37 -142 N ATOM 501 OXT HIS A 68 -21.391 13.532 32.366 1.00 34.10 O1- ANISOU 501 OXT HIS A 68 4708 4319 3927 -83 166 -165 O1- HETATM 989 O HOH D 1 -14.346 14.586 13.221 1.00 13.87 O HETATM 990 O HOH D 2 -16.418 14.200 15.979 1.00 13.76 O HETATM 991 O HOH D 3 -25.403 4.934 14.386 1.00 23.70 O HETATM 992 O HOH D 4 -24.620 22.399 15.997 1.00 17.87 O HETATM 993 O HOH D 5 -20.306 6.075 22.911 1.00 12.15 O HETATM 994 O HOH D 6 -14.549 2.651 15.454 1.00 15.20 O HETATM 995 O HOH D 7 -15.778 18.925 22.456 1.00 15.94 O HETATM 996 O HOH D 8 -19.637 6.466 19.651 1.00 15.30 O HETATM 997 O HOH D 9 -15.295 3.313 3.323 1.00 24.66 O HETATM 998 O HOH D 10 -7.450 -1.899 20.032 1.00 21.60 O HETATM 999 O HOH D 11 -24.925 24.638 17.543 1.00 17.16 O HETATM 1000 O HOH D 12 -12.854 6.224 13.330 1.00 18.83 O HETATM 1001 O HOH D 13 -23.148 13.294 20.178 1.00 17.85 O HETATM 1002 O HOH D 14 -19.020 8.607 12.665 1.00 19.45 O HETATM 1003 O HOH D 15 -14.829 -1.565 10.147 1.00 22.95 O HETATM 1004 O HOH D 16 -18.237 6.739 10.395 1.00 16.79 O HETATM 1005 O HOH D 17 -17.837 17.578 23.749 1.00 17.43 O HETATM 1006 O HOH D 18 -14.096 17.039 21.107 1.00 19.36 O HETATM 1007 O HOH D 19 -8.892 14.113 18.550 1.00 19.80 O HETATM 1008 O HOH D 20 -25.778 13.515 21.123 1.00 17.76 O HETATM 1009 O HOH D 21 -14.066 4.700 18.367 1.00 21.37 O HETATM 1010 O HOH D 22 -18.203 0.243 3.478 1.00 24.34 O HETATM 1011 O HOH D 23 -24.157 19.193 24.694 1.00 24.94 O HETATM 1012 O HOH D 24 -21.455 19.261 25.575 1.00 22.49 O HETATM 1013 O HOH D 25 -12.895 4.846 15.764 1.00 21.24 O HETATM 1014 O HOH D 26 -29.709 11.636 19.616 1.00 25.16 O HETATM 1015 O HOH D 27 -21.215 21.573 27.003 1.00 26.77 O HETATM 1016 O HOH D 28 -13.129 -8.850 10.120 1.00 25.87 O HETATM 1017 O HOH D 29 -41.913 18.790 27.497 1.00 26.26 O HETATM 1018 O HOH D 30 -17.923 12.302 18.268 1.00 25.24 O HETATM 1019 O HOH D 31 -27.890 10.226 3.993 1.00 25.58 O HETATM 1020 O HOH D 32 -22.223 22.564 23.258 1.00 26.44 O HETATM 1021 O HOH D 33 -18.411 31.797 31.693 1.00 25.94 O HETATM 1022 O HOH D 34 -35.807 9.810 17.243 1.00 24.59 O HETATM 1023 O HOH D 35 -23.983 11.248 18.524 1.00 21.78 O HETATM 1024 O HOH D 36 -19.807 1.629 11.762 1.00 26.33 O HETATM 1025 O HOH D 37 -14.345 2.884 28.435 1.00 21.56 O HETATM 1026 O HOH D 38 -17.071 -3.709 13.294 1.00 24.32 O HETATM 1027 O HOH D 39 -32.282 11.213 31.255 1.00 34.42 O HETATM 1028 O HOH D 40 -36.657 23.638 19.162 1.00 24.17 O HETATM 1029 O HOH D 41 -10.252 6.899 12.893 1.00 28.70 O HETATM 1030 O HOH D 42 -10.646 12.608 7.876 1.00 31.65 O HETATM 1031 O HOH D 43 -22.103 8.155 8.072 1.00 28.96 O HETATM 1032 O HOH D 44 -21.908 0.679 27.299 1.00 22.99 O HETATM 1033 O HOH D 45 -23.701 -5.262 13.306 1.00 28.36 O HETATM 1034 O HOH D 46 -24.451 21.923 24.217 1.00 30.19 O HETATM 1035 O HOH D 47 -26.483 17.482 17.359 1.00 36.87 O HETATM 1036 O HOH D 48 -12.722 20.054 8.884 1.00 32.44 O HETATM 1037 O HOH D 49 -17.009 15.136 24.694 1.00 21.88 O HETATM 1038 O HOH D 50 -23.942 0.227 21.920 1.00 24.38 O HETATM 1039 O HOH D 51 -12.015 -7.420 12.971 1.00 25.89 O HETATM 1040 O HOH D 52 -25.834 7.465 14.154 1.00 35.01 O HETATM 1041 O HOH D 53 -29.098 16.527 28.432 1.00 31.44 O HETATM 1042 O HOH D 54 -14.435 8.395 -0.844 1.00 31.12 O HETATM 1043 O HOH D 55 -30.920 4.107 16.665 1.00 28.80 O HETATM 1044 O HOH D 56 -29.039 2.727 -2.138 1.00 24.93 O HETATM 1045 O HOH D 57 -28.179 14.939 19.542 1.00 33.37 O HETATM 1046 O HOH D 58 -25.420 -1.467 18.911 1.00 33.73 O HETATM 1047 O HOH D 59 -25.603 13.861 4.849 1.00 23.65 O HETATM 1048 O HOH D 60 -17.270 29.812 23.491 1.00 26.07 O HETATM 1049 O HOH D 61 -14.228 10.238 18.345 1.00 23.29 O HETATM 1050 O HOH D 62 -24.441 16.173 28.164 1.00 33.20 O HETATM 1051 O HOH D 63 -24.477 -3.110 14.489 1.00 28.83 O HETATM 1052 O HOH D 64 -20.487 29.491 22.239 1.00 24.32 O HETATM 1053 O HOH D 65 -22.877 7.803 29.595 1.00 32.53 O HETATM 1054 O HOH D 66 -12.893 4.238 5.885 1.00 38.38 O HETATM 1055 O HOH D 67 -20.143 21.213 12.081 1.00 26.42 O HETATM 1056 O HOH D 68 -16.331 1.292 5.269 1.00 28.80 O HETATM 1057 O HOH D 69 -12.582 5.637 8.793 1.00 28.28 O HETATM 1058 O HOH D 70 -13.185 -2.588 23.531 0.50 25.03 O HETATM 1059 O HOH D 71 -19.570 19.158 8.970 1.00 32.43 O HETATM 1060 O HOH D 72 -28.439 14.750 -3.165 1.00 30.92 O HETATM 1061 O HOH D 73 -15.220 26.991 23.192 1.00 30.51 O HETATM 1062 O HOH D 74 -26.741 6.561 -0.331 1.00 24.97 O HETATM 1063 O HOH D 75 -29.470 4.682 2.057 1.00 33.42 O HETATM 1064 O HOH D 76 -28.981 1.786 20.089 1.00 30.83 O HETATM 1065 O HOH D 77 -41.724 17.079 20.270 1.00 29.32 O HETATM 1066 O HOH D 78 -26.031 15.167 8.310 1.00 37.44 O HETATM 1067 O HOH D 79 -16.630 5.792 28.047 1.00 24.54 O HETATM 1068 O HOH D 80 -13.394 8.123 25.059 1.00 29.46 O HETATM 1069 O HOH D 81 -34.091 19.503 28.258 1.00 27.60 O HETATM 1070 O HOH D 82 -30.875 19.667 25.882 1.00 35.35 O HETATM 1071 O HOH D 83 -18.687 7.580 28.077 1.00 32.84 O HETATM 1072 O HOH D 84 -26.569 20.354 17.560 1.00 28.58 O HETATM 1073 O HOH D 85 -13.548 7.141 27.800 1.00 35.80 O HETATM 1074 O HOH D 86 -11.959 28.561 19.933 1.00 25.13 O HETATM 1075 O HOH D 87 -11.617 26.554 16.948 1.00 34.51 O HETATM 1076 O HOH D 88 -34.507 13.945 32.641 1.00 39.43 O HETATM 1077 O HOH D 89 -27.023 27.775 20.210 1.00 43.56 O HETATM 1078 O HOH D 90 -13.401 25.850 15.302 1.00 20.77 O HETATM 1079 O HOH D 91 -27.480 3.976 -0.082 1.00 24.68 O HETATM 1080 O HOH D 92 -14.664 -4.701 24.661 1.00 23.89 O HETATM 1081 O HOH D 93 -26.388 -1.248 23.007 1.00 36.84 O HETATM 1082 O HOH D 94 -39.269 16.169 20.785 1.00 33.72 O HETATM 1083 O HOH D 95 -18.925 21.856 8.304 1.00 31.09 O HETATM 1084 O HOH D 96 -26.827 28.684 17.434 1.00 39.13 O HETATM 1085 O HOH D 97 -41.261 15.840 27.533 1.00 23.38 O HETATM 1086 O HOH D 98 -39.356 22.840 28.328 1.00 22.81 O HETATM 1087 O HOH D 99 -24.514 0.526 8.209 1.00 31.60 O HETATM 1088 O HOH D 100 -23.882 -12.884 6.093 1.00 25.75 O HETATM 1089 O HOH D 101 -18.705 29.886 25.850 1.00 27.18 O HETATM 1090 O HOH D 102 -25.618 26.953 16.085 1.00 26.56 O HETATM 1091 O HOH D 103 -14.669 12.480 22.085 1.00 34.86 O HETATM 1092 O HOH D 104 -38.612 13.533 20.876 1.00 25.86 O HETATM 1093 O HOH D 105 -21.076 7.660 -4.941 1.00 30.07 O HETATM 1094 O HOH D 106 -17.217 13.516 -3.125 1.00 32.41 O HETATM 1095 O HOH D 107 -24.272 -8.487 6.578 1.00 34.25 O HETATM 1096 O HOH D 108 -8.900 22.502 14.896 1.00 38.76 O HETATM 1097 O HOH D 109 -9.207 -6.782 13.756 1.00 40.76 O HETATM 1098 O HOH D 110 -24.517 15.222 15.126 1.00 30.25 O END A second structure was input as follows:HEADER ---- 15-MAR-20 xxxx TITLE --- COMPND --- REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU, REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.44 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 99.29 REMARK 3 NUMBER OF REFLECTIONS : 7541 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.21226 REMARK 3 R VALUE (WORKING SET) : 0.21003 REMARK 3 FREE R VALUE : 0.25472 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.3 REMARK 3 FREE R VALUE TEST SET COUNT : 419 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.804 REMARK 3 BIN RESOLUTION RANGE LOW : 1.851 REMARK 3 REFLECTION IN BIN (WORKING SET) : 538 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.88 REMARK 3 BIN R VALUE (WORKING SET) : 0.261 REMARK 3 BIN FREE R VALUE SET COUNT : 21 REMARK 3 BIN FREE R VALUE : 0.340 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 796 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.851 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.93 REMARK 3 B22 (A**2) : 0.93 REMARK 3 B33 (A**2) : -3.03 REMARK 3 B12 (A**2) : 0.47 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : -0.00 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.165 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.493 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 783 ; 0.009 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 669 ; 0.001 ; 0.018 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1050 ; 1.461 ; 1.688 REMARK 3 BOND ANGLES OTHERS (DEGREES): 1580 ; 1.333 ; 1.616 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 96 ; 6.889 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 48 ;32.679 ;21.667 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 141 ;14.555 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;10.857 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 96 ; 0.087 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 887 ; 0.014 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 161 ; 0.002 ; 0.020 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 390 ; 1.789 ; 2.179 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 389 ; 1.787 ; 2.179 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 484 ; 2.646 ; 3.246 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2) : 485 ; 2.644 ; 3.247 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 391 ; 2.610 ; 2.694 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2) : 387 ; 2.608 ; 2.686 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2) : 560 ; 4.265 ; 3.873 REMARK 3 LONG RANGE B REFINED ATOMS (A**2) : 800 ; 5.404 ;25.904 REMARK 3 LONG RANGE B OTHER ATOMS (A**2) : 798 ; 5.400 ;25.859 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 TWIN DETAILS REMARK 3 NUMBER OF TWIN DOMAINS : NULL REMARK 3 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A -1 A 45 REMARK 3 ORIGIN FOR THE GROUP (A): -19.6654 7.4936 19.1712 REMARK 3 T TENSOR REMARK 3 T11: 0.0522 T22: 0.1454 REMARK 3 T33: 0.0114 T12: 0.0300 REMARK 3 T13: 0.0016 T23: 0.0365 REMARK 3 L TENSOR REMARK 3 L11: 0.8743 L22: 0.4437 REMARK 3 L33: 3.6703 L12: -0.2875 REMARK 3 L13: 1.6694 L23: -0.1640 REMARK 3 S TENSOR REMARK 3 S11: 0.0164 S12: -0.1958 S13: -0.0704 REMARK 3 S21: 0.0146 S22: 0.1306 S23: 0.0177 REMARK 3 S31: -0.0043 S32: -0.3629 S33: -0.1471 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B -1 B 49 REMARK 3 ORIGIN FOR THE GROUP (A): -13.3755 6.9430 3.3376 REMARK 3 T TENSOR REMARK 3 T11: 0.0457 T22: 0.0268 REMARK 3 T33: 0.0541 T12: -0.0163 REMARK 3 T13: 0.0041 T23: -0.0060 REMARK 3 L TENSOR REMARK 3 L11: 0.7388 L22: 0.1677 REMARK 3 L33: 1.2617 L12: -0.2228 REMARK 3 L13: 0.4568 L23: -0.4412 REMARK 3 S TENSOR REMARK 3 S11: 0.0074 S12: -0.0175 S13: -0.0585 REMARK 3 S21: -0.0041 S22: 0.0093 S23: -0.0032 REMARK 3 S31: -0.0254 S32: -0.0042 S33: -0.0166 REMARK 3 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : WITH TLS ADDED REMARK 3 SSBOND 1 CYS A 2 CYS A 11 SSBOND 2 CYS A 7 CYS A 32 SSBOND 3 CYS A 8 CYS A 37 SSBOND 4 CYS A 20 CYS A 39 SSBOND 5 CYS B 2 CYS B 11 SSBOND 6 CYS B 7 CYS B 32 SSBOND 7 CYS B 8 CYS B 37 SSBOND 8 CYS B 20 CYS B 39 LINKR GLU B 3 GLY B 5 gap CRYST1 33.906 33.906 121.172 90.00 90.00 120.00 P 32 2 1 SCALE1 0.029493 0.017028 0.000000 0.00000 SCALE2 -0.000000 0.034056 0.000000 0.00000 SCALE3 0.000000 -0.000000 0.008253 0.00000 ATOM 1 N GLU A -1 -8.526 5.278 40.669 1.00 42.47 N ANISOU 1 N GLU A -1 5575 6010 4551 898 -303 18 N ATOM 2 CA GLU A -1 -8.322 6.675 40.175 1.00 38.63 C ANISOU 2 CA GLU A -1 5080 5508 4088 942 -276 -45 C ATOM 3 CB GLU A -1 -6.963 6.740 39.487 1.00 43.49 C ANISOU 3 CB GLU A -1 5700 6039 4783 909 -308 -129 C ATOM 4 CG GLU A -1 -6.548 8.122 39.045 1.00 50.20 C ANISOU 4 CG GLU A -1 6561 6861 5651 913 -307 -182 C ATOM 5 CD GLU A -1 -5.620 8.054 37.853 1.00 57.52 C ANISOU 5 CD GLU A -1 7450 7764 6640 837 -315 -224 C ATOM 6 OE1 GLU A -1 -6.012 7.403 36.841 1.00 59.94 O ANISOU 6 OE1 GLU A -1 7721 8083 6969 795 -290 -197 O ATOM 7 OE2 GLU A -1 -4.478 8.552 37.970 1.00 67.43 O ANISOU 7 OE2 GLU A -1 8704 9006 7911 818 -351 -282 O ATOM 8 C GLU A -1 -9.503 7.057 39.278 1.00 30.60 C ANISOU 8 C GLU A -1 4021 4552 3051 922 -227 7 C ATOM 9 O GLU A -1 -10.550 7.433 39.829 1.00 27.94 O ANISOU 9 O GLU A -1 3662 4321 2629 980 -198 55 O ATOM 10 N PHE A 0 -9.386 6.895 37.955 1.00 27.03 N ANISOU 10 N PHE A 0 3550 4057 2661 853 -218 0 N ATOM 11 CA PHE A 0 -10.494 7.180 37.013 1.00 26.53 C ANISOU 11 CA PHE A 0 3448 4046 2583 829 -176 48 C ATOM 12 CB PHE A 0 -10.044 8.149 35.925 1.00 26.39 C ANISOU 12 CB PHE A 0 3445 3965 2617 819 -170 -10 C ATOM 13 CG PHE A 0 -9.706 9.513 36.448 1.00 28.74 C ANISOU 13 CG PHE A 0 3801 4231 2886 893 -192 -66 C ATOM 14 CD1 PHE A 0 -10.705 10.376 36.884 1.00 30.65 C ANISOU 14 CD1 PHE A 0 4067 4532 3046 995 -184 -54 C ATOM 15 CE1 PHE A 0 -10.388 11.619 37.419 1.00 30.29 C ANISOU 15 CE1 PHE A 0 4115 4432 2962 1080 -233 -113 C ATOM 16 CZ PHE A 0 -9.074 12.010 37.517 1.00 30.54 C ANISOU 16 CZ PHE A 0 4204 4357 3042 1028 -288 -169 C ATOM 17 CD2 PHE A 0 -8.390 9.920 36.556 1.00 29.76 C ANISOU 17 CD2 PHE A 0 3966 4283 3055 867 -235 -132 C ATOM 18 CE2 PHE A 0 -8.081 11.181 37.051 1.00 31.31 C ANISOU 18 CE2 PHE A 0 4245 4430 3220 915 -281 -175 C ATOM 19 C PHE A 0 -10.991 5.876 36.400 1.00 26.12 C ANISOU 19 C PHE A 0 3371 4006 2545 735 -182 120 C ATOM 20 O PHE A 0 -10.219 4.922 36.347 1.00 25.40 O ANISOU 20 O PHE A 0 3313 3843 2492 696 -230 102 O ATOM 21 N GLU A 1 -12.262 5.852 36.027 1.00 25.58 N ANISOU 21 N GLU A 1 3255 4032 2431 708 -149 198 N ATOM 22 CA GLU A 1 -12.876 4.805 35.187 1.00 26.49 C ANISOU 22 CA GLU A 1 3354 4151 2557 599 -165 273 C ATOM 23 CB GLU A 1 -14.386 4.712 35.422 1.00 28.10 C ANISOU 23 CB GLU A 1 3485 4524 2667 566 -134 387 C ATOM 24 CG GLU A 1 -14.987 3.401 34.919 1.00 29.44 C ANISOU 24 CG GLU A 1 3658 4698 2829 418 -182 491 C ATOM 25 CD GLU A 1 -14.700 2.151 35.741 1.00 30.20 C ANISOU 25 CD GLU A 1 3823 4750 2899 334 -263 551 C ATOM 26 OE1 GLU A 1 -14.451 2.239 36.973 1.00 28.72 O ANISOU 26 OE1 GLU A 1 3641 4607 2665 380 -262 552 O ATOM 27 OE2 GLU A 1 -14.725 1.073 35.143 1.00 33.40 O ANISOU 27 OE2 GLU A 1 4295 5068 3325 225 -340 595 O ATOM 28 C GLU A 1 -12.536 5.147 33.747 1.00 28.17 C ANISOU 28 C GLU A 1 3571 4288 2844 584 -154 218 C ATOM 29 O GLU A 1 -13.022 6.181 33.240 1.00 30.17 O ANISOU 29 O GLU A 1 3794 4579 3088 622 -109 205 O ATOM 30 N CYS A 2 -11.639 4.377 33.157 1.00 27.04 N ANISOU 30 N CYS A 2 3469 4044 2760 548 -200 176 N ATOM 31 CA CYS A 2 -11.056 4.713 31.845 1.00 27.59 C ANISOU 31 CA CYS A 2 3533 4058 2889 544 -189 111 C ATOM 32 CB CYS A 2 -9.580 5.019 31.948 1.00 29.29 C ANISOU 32 CB CYS A 2 3758 4229 3139 587 -205 12 C ATOM 33 SG CYS A 2 -9.238 6.574 32.807 1.00 31.66 S ANISOU 33 SG CYS A 2 4056 4548 3422 641 -175 -27 S ATOM 34 C CYS A 2 -11.299 3.572 30.874 1.00 27.80 C ANISOU 34 C CYS A 2 3585 4043 2933 483 -234 141 C ATOM 35 O CYS A 2 -11.119 2.407 31.250 1.00 29.66 O ANISOU 35 O CYS A 2 3880 4231 3156 462 -309 161 O ATOM 36 N GLU A 3 -11.769 3.918 29.697 1.00 28.30 N ANISOU 36 N GLU A 3 3620 4115 3016 457 -203 148 N ATOM 37 CA GLU A 3 -11.969 2.958 28.598 1.00 28.98 C ANISOU 37 CA GLU A 3 3738 4152 3118 409 -251 164 C ATOM 38 CB GLU A 3 -13.426 2.498 28.604 1.00 35.44 C ANISOU 38 CB GLU A 3 4550 5018 3897 324 -262 283 C ATOM 39 CG GLU A 3 -13.792 1.598 27.447 1.00 39.80 C ANISOU 39 CG GLU A 3 5149 5511 4461 262 -323 311 C ATOM 40 CD GLU A 3 -15.147 0.926 27.594 1.00 45.19 C ANISOU 40 CD GLU A 3 5834 6243 5093 142 -364 446 C ATOM 41 OE1 GLU A 3 -15.688 0.908 28.736 1.00 50.61 O ANISOU 41 OE1 GLU A 3 6487 7019 5722 104 -356 523 O ATOM 42 OE2 GLU A 3 -15.645 0.395 26.580 1.00 50.16 O ANISOU 42 OE2 GLU A 3 6494 6835 5728 80 -409 480 O ATOM 43 C GLU A 3 -11.530 3.680 27.333 1.00 28.02 C ANISOU 43 C GLU A 3 3583 4027 3034 429 -209 100 C ATOM 44 O GLU A 3 -11.599 4.920 27.307 1.00 28.52 O ANISOU 44 O GLU A 3 3606 4128 3099 444 -146 86 O ATOM 45 N SER A 4 -11.121 2.942 26.321 1.00 25.01 N ANISOU 45 N SER A 4 3230 3602 2668 431 -253 65 N ATOM 46 CA SER A 4 -10.755 3.527 25.016 1.00 24.80 C ANISOU 46 CA SER A 4 3164 3593 2662 439 -214 16 C ATOM 47 CB SER A 4 -9.312 3.277 24.700 1.00 27.08 C ANISOU 47 CB SER A 4 3441 3898 2948 503 -238 -81 C ATOM 48 OG SER A 4 -9.075 1.905 24.522 1.00 27.51 O ANISOU 48 OG SER A 4 3566 3900 2984 551 -333 -106 O ATOM 49 C SER A 4 -11.721 3.025 23.937 1.00 25.50 C ANISOU 49 C SER A 4 3276 3658 2754 395 -233 65 C ATOM 50 O SER A 4 -12.547 2.141 24.199 1.00 26.35 O ANISOU 50 O SER A 4 3433 3732 2844 349 -290 136 O ATOM 51 N GLY A 5 -11.771 3.740 22.835 1.00 23.18 N ANISOU 51 N GLY A 5 2943 3389 2473 388 -183 47 N ATOM 52 CA GLY A 5 -12.714 3.482 21.755 1.00 23.30 C ANISOU 52 CA GLY A 5 2972 3389 2492 348 -191 90 C ATOM 53 C GLY A 5 -12.869 4.724 20.903 1.00 23.15 C ANISOU 53 C GLY A 5 2904 3409 2482 337 -116 81 C ATOM 54 O GLY A 5 -12.382 5.797 21.246 1.00 21.51 O ANISOU 54 O GLY A 5 2670 3229 2272 345 -70 54 O ATOM 55 N PRO A 6 -13.562 4.584 19.760 1.00 24.65 N ANISOU 55 N PRO A 6 3101 3589 2675 311 -118 105 N ATOM 56 CA PRO A 6 -13.752 5.696 18.832 1.00 22.62 C ANISOU 56 CA PRO A 6 2817 3356 2420 298 -60 98 C ATOM 57 CB PRO A 6 -14.756 5.136 17.817 1.00 23.13 C ANISOU 57 CB PRO A 6 2898 3401 2487 270 -84 141 C ATOM 58 CG PRO A 6 -14.556 3.633 17.878 1.00 24.45 C ANISOU 58 CG PRO A 6 3119 3517 2652 276 -172 138 C ATOM 59 CD PRO A 6 -14.158 3.317 19.302 1.00 23.26 C ANISOU 59 CD PRO A 6 2977 3363 2495 288 -194 141 C ATOM 60 C PRO A 6 -14.345 6.952 19.482 1.00 23.55 C ANISOU 60 C PRO A 6 2923 3498 2525 298 -14 127 C ATOM 61 O PRO A 6 -14.127 8.028 18.974 1.00 21.77 O ANISOU 61 O PRO A 6 2705 3273 2293 292 15 107 O ATOM 62 N CYS A 7 -15.198 6.796 20.492 1.00 22.50 N ANISOU 62 N CYS A 7 2782 3393 2372 307 -19 179 N ATOM 63 CA CYS A 7 -15.968 7.932 21.081 1.00 24.02 C ANISOU 63 CA CYS A 7 2966 3633 2527 349 13 200 C ATOM 64 CB CYS A 7 -17.445 7.576 21.177 1.00 24.17 C ANISOU 64 CB CYS A 7 2942 3734 2508 343 12 277 C ATOM 65 SG CYS A 7 -18.226 7.524 19.545 1.00 26.26 S ANISOU 65 SG CYS A 7 3201 3992 2784 307 13 299 S ATOM 66 C CYS A 7 -15.387 8.346 22.439 1.00 23.90 C ANISOU 66 C CYS A 7 2961 3622 2495 391 12 176 C ATOM 67 O CYS A 7 -16.077 9.043 23.187 1.00 23.66 O ANISOU 67 O CYS A 7 2929 3644 2416 452 23 192 O ATOM 68 N CYS A 8 -14.133 7.987 22.709 1.00 24.41 N ANISOU 68 N CYS A 8 3038 3647 2590 377 -3 130 N ATOM 69 CA CYS A 8 -13.382 8.392 23.919 1.00 23.29 C ANISOU 69 CA CYS A 8 2910 3500 2436 410 -10 98 C ATOM 70 CB CYS A 8 -13.277 7.263 24.930 1.00 25.32 C ANISOU 70 CB CYS A 8 3156 3769 2693 416 -36 117 C ATOM 71 SG CYS A 8 -14.855 6.978 25.757 1.00 27.26 S ANISOU 71 SG CYS A 8 3371 4105 2882 427 -30 210 S ATOM 72 C CYS A 8 -11.987 8.858 23.530 1.00 23.63 C ANISOU 72 C CYS A 8 2964 3514 2500 380 -16 37 C ATOM 73 O CYS A 8 -11.421 8.332 22.557 1.00 23.07 O ANISOU 73 O CYS A 8 2867 3448 2448 347 -17 15 O ATOM 74 N ARG A 9 -11.451 9.758 24.333 1.00 22.14 N ANISOU 74 N ARG A 9 2806 3310 2294 394 -27 12 N ATOM 75 CA ARG A 9 -10.063 10.247 24.192 1.00 24.85 C ANISOU 75 CA ARG A 9 3148 3652 2641 340 -43 -31 C ATOM 76 CB ARG A 9 -10.053 11.463 23.260 1.00 27.25 C ANISOU 76 CB ARG A 9 3499 3929 2925 276 -48 -24 C ATOM 77 CG ARG A 9 -8.663 11.957 22.906 1.00 31.89 C ANISOU 77 CG ARG A 9 4067 4549 3499 176 -68 -45 C ATOM 78 CD ARG A 9 -7.972 11.035 21.931 1.00 34.71 C ANISOU 78 CD ARG A 9 4321 5001 3863 148 -40 -64 C ATOM 79 NE ARG A 9 -6.662 11.560 21.564 1.00 39.27 N ANISOU 79 NE ARG A 9 4849 5666 4404 43 -54 -74 N ATOM 80 CZ ARG A 9 -5.476 11.053 21.925 1.00 41.12 C ANISOU 80 CZ ARG A 9 4992 6007 4621 42 -60 -113 C ATOM 81 NH1 ARG A 9 -5.387 9.969 22.690 1.00 39.92 N ANISOU 81 NH1 ARG A 9 4813 5862 4493 151 -63 -154 N ATOM 82 NH2 ARG A 9 -4.372 11.629 21.477 1.00 40.98 N ANISOU 82 NH2 ARG A 9 4910 6107 4552 -74 -72 -107 N ATOM 83 C ARG A 9 -9.545 10.563 25.587 1.00 24.77 C ANISOU 83 C ARG A 9 3164 3629 2617 371 -70 -52 C ATOM 84 O ARG A 9 -10.217 11.334 26.270 1.00 23.32 O ANISOU 84 O ARG A 9 3044 3412 2404 421 -84 -39 O ATOM 85 N ASN A 10 -8.458 9.908 26.003 1.00 24.10 N ANISOU 85 N ASN A 10 3032 3578 2544 364 -83 -87 N ATOM 86 CA ASN A 10 -7.747 10.182 27.276 1.00 28.54 C ANISOU 86 CA ASN A 10 3613 4133 3095 385 -114 -114 C ATOM 87 CB ASN A 10 -7.001 11.515 27.201 1.00 33.40 C ANISOU 87 CB ASN A 10 4271 4731 3687 305 -149 -123 C ATOM 88 CG ASN A 10 -5.818 11.465 26.254 1.00 37.40 C ANISOU 88 CG ASN A 10 4696 5324 4187 205 -148 -140 C ATOM 89 OD1 ASN A 10 -5.151 10.438 26.138 1.00 40.75 O ANISOU 89 OD1 ASN A 10 5031 5833 4619 233 -135 -174 O ATOM 90 ND2 ASN A 10 -5.549 12.569 25.576 1.00 40.49 N ANISOU 90 ND2 ASN A 10 5125 5708 4551 93 -172 -116 N ATOM 91 C ASN A 10 -8.754 10.128 28.433 1.00 27.01 C ANISOU 91 C ASN A 10 3465 3910 2884 470 -115 -88 C ATOM 92 O ASN A 10 -8.805 11.066 29.233 1.00 24.22 O ANISOU 92 O ASN A 10 3176 3525 2501 502 -141 -95 O ATOM 93 N CYS A 11 -9.629 9.126 28.409 1.00 27.53 N ANISOU 93 N CYS A 11 3504 3997 2956 502 -94 -51 N ATOM 94 CA CYS A 11 -10.539 8.790 29.518 1.00 27.83 C ANISOU 94 CA CYS A 11 3553 4060 2962 564 -91 -11 C ATOM 95 CB CYS A 11 -9.740 8.801 30.811 1.00 32.31 C ANISOU 95 CB CYS A 11 4139 4618 3518 600 -120 -44 C ATOM 96 SG CYS A 11 -10.615 7.947 32.132 1.00 35.76 S ANISOU 96 SG CYS A 11 4568 5108 3908 653 -120 13 S ATOM 97 C CYS A 11 -11.727 9.770 29.562 1.00 27.59 C ANISOU 97 C CYS A 11 3547 4053 2880 617 -74 17 C ATOM 98 O CYS A 11 -12.446 9.824 30.570 1.00 27.93 O ANISOU 98 O CYS A 11 3590 4154 2869 689 -71 43 O ATOM 99 N LYS A 12 -11.936 10.534 28.506 1.00 25.54 N ANISOU 99 N LYS A 12 3311 3767 2625 594 -69 11 N ATOM 100 CA LYS A 12 -13.077 11.467 28.402 1.00 27.85 C ANISOU 100 CA LYS A 12 3640 4081 2858 669 -66 26 C ATOM 101 CB LYS A 12 -12.537 12.887 28.265 1.00 30.33 C ANISOU 101 CB LYS A 12 4065 4305 3153 677 -117 -19 C ATOM 102 CG LYS A 12 -11.535 13.277 29.343 1.00 31.98 C ANISOU 102 CG LYS A 12 4329 4467 3355 685 -164 -59 C ATOM 103 CD LYS A 12 -11.068 14.715 29.249 1.00 35.94 C ANISOU 103 CD LYS A 12 4970 4862 3823 673 -245 -92 C ATOM 104 CE LYS A 12 -10.489 15.055 27.898 1.00 39.51 C ANISOU 104 CE LYS A 12 5435 5267 4308 532 -255 -82 C ATOM 105 NZ LYS A 12 -9.383 14.141 27.520 1.00 41.55 N ANISOU 105 NZ LYS A 12 5579 5578 4627 416 -218 -80 N ATOM 106 C LYS A 12 -13.963 11.031 27.243 1.00 26.85 C ANISOU 106 C LYS A 12 3465 3992 2744 634 -33 69 C ATOM 107 O LYS A 12 -13.456 10.363 26.343 1.00 25.70 O ANISOU 107 O LYS A 12 3290 3818 2654 548 -24 69 O ATOM 108 N PHE A 13 -15.253 11.339 27.307 1.00 28.71 N ANISOU 108 N PHE A 13 3683 4308 2915 712 -19 100 N ATOM 109 CA PHE A 13 -16.244 11.005 26.261 1.00 28.16 C ANISOU 109 CA PHE A 13 3563 4292 2844 685 6 145 C ATOM 110 CB PHE A 13 -17.588 10.670 26.908 1.00 30.52 C ANISOU 110 CB PHE A 13 3777 4757 3059 749 27 206 C ATOM 111 CG PHE A 13 -17.516 9.394 27.686 1.00 32.90 C ANISOU 111 CG PHE A 13 4015 5115 3369 679 31 264 C ATOM 112 CD1 PHE A 13 -17.007 9.398 28.974 1.00 34.82 C ANISOU 112 CD1 PHE A 13 4274 5367 3588 723 21 247 C ATOM 113 CE1 PHE A 13 -16.790 8.209 29.649 1.00 38.67 C ANISOU 113 CE1 PHE A 13 4729 5876 4085 648 10 297 C ATOM 114 CZ PHE A 13 -17.087 7.009 29.047 1.00 37.48 C ANISOU 114 CZ PHE A 13 4550 5726 3965 526 -4 364 C ATOM 115 CD2 PHE A 13 -17.698 8.178 27.052 1.00 33.58 C ANISOU 115 CD2 PHE A 13 4062 5198 3497 558 26 323 C ATOM 116 CE2 PHE A 13 -17.504 6.988 27.737 1.00 36.38 C ANISOU 116 CE2 PHE A 13 4401 5564 3856 482 0 374 C ATOM 117 C PHE A 13 -16.326 12.152 25.251 1.00 29.80 C ANISOU 117 C PHE A 13 3847 4430 3045 706 -11 109 C ATOM 118 O PHE A 13 -16.470 13.334 25.669 1.00 29.07 O ANISOU 118 O PHE A 13 3843 4311 2890 808 -49 70 O ATOM 119 N LEU A 14 -16.220 11.822 23.960 1.00 25.68 N ANISOU 119 N LEU A 14 3311 3868 2575 617 2 120 N ATOM 120 CA LEU A 14 -16.394 12.818 22.881 1.00 29.14 C ANISOU 120 CA LEU A 14 3823 4245 3001 620 -15 100 C ATOM 121 CB LEU A 14 -16.133 12.162 21.514 1.00 29.03 C ANISOU 121 CB LEU A 14 3772 4206 3050 511 7 116 C ATOM 122 CG LEU A 14 -14.665 11.844 21.166 1.00 30.49 C ANISOU 122 CG LEU A 14 3957 4338 3290 411 5 89 C ATOM 123 CD1 LEU A 14 -14.541 11.424 19.705 1.00 28.50 C ANISOU 123 CD1 LEU A 14 3678 4080 3069 340 22 96 C ATOM 124 CD2 LEU A 14 -13.738 13.019 21.420 1.00 34.48 C ANISOU 124 CD2 LEU A 14 4550 4775 3775 385 -34 55 C ATOM 125 C LEU A 14 -17.809 13.414 22.979 1.00 27.68 C ANISOU 125 C LEU A 14 3643 4143 2732 750 -20 110 C ATOM 126 O LEU A 14 -18.774 12.662 23.305 1.00 29.37 O ANISOU 126 O LEU A 14 3749 4495 2916 779 12 159 O ATOM 127 N LYS A 15 -17.916 14.731 22.783 1.00 30.99 N ANISOU 127 N LYS A 15 4187 4490 3096 828 -74 67 N ATOM 128 CA LYS A 15 -19.202 15.485 22.776 1.00 33.31 C ANISOU 128 CA LYS A 15 4509 4858 3287 993 -99 54 C ATOM 129 CB LYS A 15 -19.007 16.825 22.061 1.00 36.10 C ANISOU 129 CB LYS A 15 5047 5060 3608 1023 -182 7 C ATOM 130 CG LYS A 15 -20.062 17.876 22.349 1.00 37.95 C ANISOU 130 CG LYS A 15 5375 5333 3710 1244 -250 -39 C ATOM 131 CD LYS A 15 -19.945 18.465 23.732 1.00 39.41 C ANISOU 131 CD LYS A 15 5638 5522 3813 1393 -308 -88 C ATOM 132 CE LYS A 15 -21.050 19.455 24.030 1.00 41.29 C ANISOU 132 CE LYS A 15 5966 5826 3894 1660 -385 -149 C ATOM 133 NZ LYS A 15 -22.312 18.766 24.395 1.00 40.27 N ANISOU 133 NZ LYS A 15 5626 5982 3692 1784 -303 -121 N ATOM 134 C LYS A 15 -20.286 14.642 22.095 1.00 32.32 C ANISOU 134 C LYS A 15 4244 4871 3163 976 -42 109 C ATOM 135 O LYS A 15 -20.046 14.157 20.959 1.00 30.62 O ANISOU 135 O LYS A 15 4011 4599 3024 850 -21 133 O ATOM 136 N GLU A 16 -21.449 14.500 22.724 1.00 34.29 N ANISOU 136 N GLU A 16 4396 5311 3320 1096 -25 132 N ATOM 137 CA GLU A 16 -22.612 13.820 22.104 1.00 39.11 C ANISOU 137 CA GLU A 16 4870 6081 3907 1076 14 195 C ATOM 138 CB GLU A 16 -23.855 13.843 22.991 1.00 45.09 C ANISOU 138 CB GLU A 16 5504 7102 4526 1223 28 220 C ATOM 139 CG GLU A 16 -24.474 15.215 23.166 1.00 50.67 C ANISOU 139 CG GLU A 16 6296 7855 5101 1468 -24 140 C ATOM 140 CD GLU A 16 -25.578 15.242 24.217 1.00 54.37 C ANISOU 140 CD GLU A 16 6623 8629 5405 1644 -8 154 C ATOM 141 OE1 GLU A 16 -26.761 15.298 23.820 1.00 53.73 O ANISOU 141 OE1 GLU A 16 6432 8755 5227 1731 2 174 O ATOM 142 OE2 GLU A 16 -25.253 15.139 25.431 1.00 56.54 O ANISOU 142 OE2 GLU A 16 6880 8959 5643 1686 -2 152 O ATOM 143 C GLU A 16 -22.915 14.499 20.760 1.00 39.05 C ANISOU 143 C GLU A 16 4942 5990 3904 1093 -11 166 C ATOM 144 O GLU A 16 -22.735 15.738 20.655 1.00 38.99 O ANISOU 144 O GLU A 16 5088 5873 3850 1203 -73 97 O ATOM 145 N GLY A 17 -23.341 13.708 19.779 1.00 37.08 N ANISOU 145 N GLY A 17 4609 5774 3703 984 19 220 N ATOM 146 CA GLY A 17 -23.617 14.177 18.408 1.00 38.69 C ANISOU 146 CA GLY A 17 4876 5901 3920 979 0 202 C ATOM 147 C GLY A 17 -22.401 14.140 17.493 1.00 38.17 C ANISOU 147 C GLY A 17 4909 5629 3962 836 -4 186 C ATOM 148 O GLY A 17 -22.619 14.345 16.285 1.00 41.65 O ANISOU 148 O GLY A 17 5387 6017 4418 807 -12 184 O ATOM 149 N THR A 18 -21.175 13.906 18.006 1.00 34.79 N ANISOU 149 N THR A 18 4513 5110 3594 754 0 174 N ATOM 150 CA THR A 18 -19.916 13.846 17.195 1.00 34.29 C ANISOU 150 CA THR A 18 4513 4904 3611 620 -2 160 C ATOM 151 CB THR A 18 -18.669 13.756 18.090 1.00 34.64 C ANISOU 151 CB THR A 18 4577 4897 3688 571 -6 140 C ATOM 152 OG1 THR A 18 -18.600 14.861 18.995 1.00 36.59 O ANISOU 152 OG1 THR A 18 4923 5107 3871 668 -55 103 O ATOM 153 CG2 THR A 18 -17.384 13.705 17.291 1.00 35.18 C ANISOU 153 CG2 THR A 18 4677 4878 3811 441 -5 128 C ATOM 154 C THR A 18 -19.979 12.649 16.225 1.00 28.61 C ANISOU 154 C THR A 18 3708 4207 2956 516 32 199 C ATOM 155 O THR A 18 -20.295 11.526 16.666 1.00 29.80 O ANISOU 155 O THR A 18 3762 4434 3124 487 50 239 O ATOM 156 N ILE A 19 -19.763 12.853 14.917 1.00 27.60 N ANISOU 156 N ILE A 19 3624 4012 2850 460 29 191 N ATOM 157 CA ILE A 19 -19.863 11.736 13.941 1.00 23.87 C ANISOU 157 CA ILE A 19 3087 3554 2426 384 48 219 C ATOM 158 CB ILE A 19 -19.796 12.236 12.483 1.00 25.47 C ANISOU 158 CB ILE A 19 3348 3697 2629 351 43 207 C ATOM 159 CG1 ILE A 19 -20.105 11.108 11.497 1.00 25.00 C ANISOU 159 CG1 ILE A 19 3234 3657 2607 303 50 231 C ATOM 160 CG2 ILE A 19 -18.474 12.941 12.174 1.00 26.06 C ANISOU 160 CG2 ILE A 19 3496 3698 2706 285 37 177 C ATOM 161 CD1 ILE A 19 -20.284 11.589 10.056 1.00 26.10 C ANISOU 161 CD1 ILE A 19 3423 3756 2736 286 47 224 C ATOM 162 C ILE A 19 -18.764 10.715 14.271 1.00 23.49 C ANISOU 162 C ILE A 19 3003 3491 2430 316 56 211 C ATOM 163 O ILE A 19 -17.616 11.128 14.498 1.00 23.07 O ANISOU 163 O ILE A 19 2983 3396 2384 290 57 177 O ATOM 164 N CYS A 20 -19.084 9.426 14.227 1.00 22.11 N ANISOU 164 N CYS A 20 2771 3346 2280 285 47 243 N ATOM 165 CA CYS A 20 -18.070 8.374 14.423 1.00 22.41 C ANISOU 165 CA CYS A 20 2799 3358 2355 246 31 225 C ATOM 166 CB CYS A 20 -18.180 7.767 15.818 1.00 21.80 C ANISOU 166 CB CYS A 20 2693 3315 2274 252 16 252 C ATOM 167 SG CYS A 20 -19.760 6.988 16.225 1.00 24.94 S ANISOU 167 SG CYS A 20 3036 3799 2641 224 -10 346 S ATOM 168 C CYS A 20 -18.075 7.362 13.275 1.00 22.16 C ANISOU 168 C CYS A 20 2774 3300 2344 214 2 226 C ATOM 169 O CYS A 20 -17.045 6.701 13.081 1.00 20.26 O ANISOU 169 O CYS A 20 2544 3036 2116 214 -16 184 O ATOM 170 N LYS A 21 -19.113 7.309 12.449 1.00 23.74 N ANISOU 170 N LYS A 21 2972 3508 2537 203 -7 261 N ATOM 171 CA LYS A 21 -19.098 6.431 11.258 1.00 24.03 C ANISOU 171 CA LYS A 21 3036 3507 2588 181 -46 255 C ATOM 172 CB LYS A 21 -19.373 4.980 11.622 1.00 27.86 C ANISOU 172 CB LYS A 21 3537 3967 3080 146 -125 291 C ATOM 173 CG LYS A 21 -19.087 3.978 10.519 1.00 31.26 C ANISOU 173 CG LYS A 21 4031 4332 3514 150 -194 263 C ATOM 174 CD LYS A 21 -18.869 2.583 11.057 1.00 37.42 C ANISOU 174 CD LYS A 21 4876 5051 4291 134 -297 274 C ATOM 175 CE LYS A 21 -18.282 1.635 10.041 1.00 40.00 C ANISOU 175 CE LYS A 21 5292 5302 4603 188 -383 214 C ATOM 176 NZ LYS A 21 -19.295 1.227 9.046 1.00 44.73 N ANISOU 176 NZ LYS A 21 5934 5860 5198 141 -443 259 N ATOM 177 C LYS A 21 -20.107 6.947 10.237 1.00 24.72 C ANISOU 177 C LYS A 21 3124 3606 2662 177 -37 279 C ATOM 178 O LYS A 21 -21.295 7.019 10.526 1.00 25.57 O ANISOU 178 O LYS A 21 3197 3767 2752 169 -44 335 O ATOM 179 N ARG A 22 -19.609 7.305 9.070 1.00 22.53 N ANISOU 179 N ARG A 22 2876 3300 2383 186 -21 239 N ATOM 180 CA ARG A 22 -20.437 7.838 7.987 1.00 21.14 C ANISOU 180 CA ARG A 22 2715 3122 2193 188 -15 254 C ATOM 181 CB ARG A 22 -19.541 8.548 6.979 1.00 20.89 C ANISOU 181 CB ARG A 22 2718 3073 2146 188 15 209 C ATOM 182 CG ARG A 22 -20.310 9.269 5.893 1.00 22.97 C ANISOU 182 CG ARG A 22 3015 3323 2389 191 20 221 C ATOM 183 CD ARG A 22 -19.487 10.336 5.219 1.00 23.39 C ANISOU 183 CD ARG A 22 3113 3365 2408 166 50 198 C ATOM 184 NE ARG A 22 -18.783 11.221 6.130 1.00 24.06 N ANISOU 184 NE ARG A 22 3215 3447 2477 146 65 191 N ATOM 185 CZ ARG A 22 -19.285 12.316 6.699 1.00 25.61 C ANISOU 185 CZ ARG A 22 3469 3610 2651 169 54 202 C ATOM 186 NH1 ARG A 22 -20.523 12.701 6.441 1.00 26.52 N ANISOU 186 NH1 ARG A 22 3613 3713 2748 226 35 216 N ATOM 187 NH2 ARG A 22 -18.498 13.093 7.414 1.00 25.84 N ANISOU 187 NH2 ARG A 22 3537 3620 2660 139 50 193 N ATOM 188 C ARG A 22 -21.249 6.687 7.410 1.00 21.57 C ANISOU 188 C ARG A 22 2771 3164 2257 161 -76 290 C ATOM 189 O ARG A 22 -20.680 5.608 7.169 1.00 20.17 O ANISOU 189 O ARG A 22 2627 2945 2091 156 -127 270 O ATOM 190 N ALA A 23 -22.537 6.947 7.180 1.00 25.72 N ANISOU 190 N ALA A 23 3272 3731 2767 153 -83 339 N ATOM 191 CA ALA A 23 -23.541 5.999 6.658 1.00 27.27 C ANISOU 191 CA ALA A 23 3464 3933 2962 102 -151 394 C ATOM 192 CB ALA A 23 -24.921 6.579 6.874 1.00 29.54 C ANISOU 192 CB ALA A 23 3680 4330 3213 104 -138 451 C ATOM 193 C ALA A 23 -23.301 5.757 5.167 1.00 25.52 C ANISOU 193 C ALA A 23 3305 3643 2749 113 -176 357 C ATOM 194 O ALA A 23 -22.796 6.666 4.498 1.00 21.34 O ANISOU 194 O ALA A 23 2795 3101 2210 156 -122 310 O ATOM 195 N ARG A 24 -23.813 4.645 4.655 1.00 25.68 N ANISOU 195 N ARG A 24 3358 3625 2771 66 -264 390 N ATOM 196 CA ARG A 24 -23.960 4.370 3.208 1.00 28.53 C ANISOU 196 CA ARG A 24 3778 3933 3129 79 -304 368 C ATOM 197 CB ARG A 24 -23.877 2.850 2.990 1.00 34.93 C ANISOU 197 CB ARG A 24 4674 4655 3940 45 -433 377 C ATOM 198 CG ARG A 24 -22.793 2.172 3.826 1.00 41.37 C ANISOU 198 CG ARG A 24 5530 5427 4759 71 -463 339 C ATOM 199 CD ARG A 24 -22.640 0.669 3.623 1.00 48.42 C ANISOU 199 CD ARG A 24 6552 6206 5637 61 -621 335 C ATOM 200 NE ARG A 24 -22.086 0.343 2.312 1.00 57.01 N ANISOU 200 NE ARG A 24 7723 7237 6699 161 -663 253 N ATOM 201 CZ ARG A 24 -22.780 -0.134 1.267 1.00 61.87 C ANISOU 201 CZ ARG A 24 8412 7792 7302 144 -751 269 C ATOM 202 NH1 ARG A 24 -24.078 -0.372 1.370 1.00 65.11 N ANISOU 202 NH1 ARG A 24 8817 8196 7723 12 -812 373 N ATOM 203 NH2 ARG A 24 -22.161 -0.383 0.120 1.00 58.65 N ANISOU 203 NH2 ARG A 24 8076 7349 6858 260 -782 182 N ATOM 204 C ARG A 24 -25.284 4.995 2.734 1.00 27.62 C ANISOU 204 C ARG A 24 3615 3880 2998 60 -291 417 C ATOM 205 O ARG A 24 -26.253 4.992 3.515 1.00 27.51 O ANISOU 205 O ARG A 24 3528 3956 2968 12 -300 488 O ATOM 206 N GLY A 25 -25.326 5.544 1.526 1.00 26.15 N ANISOU 206 N GLY A 25 3461 3670 2803 103 -269 382 N ATOM 207 CA GLY A 25 -26.576 6.008 0.893 1.00 28.08 C ANISOU 207 CA GLY A 25 3676 3965 3027 99 -276 419 C ATOM 208 C GLY A 25 -27.217 7.132 1.700 1.00 29.20 C ANISOU 208 C GLY A 25 3741 4213 3139 137 -214 438 C ATOM 209 O GLY A 25 -26.479 8.042 2.121 1.00 26.72 O ANISOU 209 O GLY A 25 3444 3885 2820 191 -152 394 O ATOM 210 N ASP A 26 -28.526 7.037 1.976 1.00 27.64 N ANISOU 210 N ASP A 26 3459 4132 2909 112 -243 504 N ATOM 211 CA ASP A 26 -29.310 8.142 2.584 1.00 28.29 C ANISOU 211 CA ASP A 26 3466 4349 2934 194 -197 509 C ATOM 212 CB ASP A 26 -30.703 8.285 1.975 1.00 28.64 C ANISOU 212 CB ASP A 26 3443 4510 2927 208 -229 547 C ATOM 213 CG ASP A 26 -31.356 9.610 2.347 1.00 29.68 C ANISOU 213 CG ASP A 26 3532 4762 2982 353 -190 517 C ATOM 214 OD1 ASP A 26 -30.628 10.602 2.399 1.00 26.69 O ANISOU 214 OD1 ASP A 26 3248 4289 2603 441 -154 448 O ATOM 215 OD2 ASP A 26 -32.586 9.637 2.566 1.00 30.60 O ANISOU 215 OD2 ASP A 26 3526 5072 3027 377 -209 563 O ATOM 216 C ASP A 26 -29.434 7.936 4.097 1.00 29.07 C ANISOU 216 C ASP A 26 3473 4560 3009 175 -185 552 C ATOM 217 O ASP A 26 -30.178 8.716 4.738 1.00 28.39 O ANISOU 217 O ASP A 26 3307 4622 2855 258 -157 559 O ATOM 218 N ASP A 27 -28.716 6.967 4.673 1.00 30.00 N ANISOU 218 N ASP A 27 3609 4618 3169 88 -208 573 N ATOM 219 CA ASP A 27 -28.932 6.579 6.091 1.00 30.17 C ANISOU 219 CA ASP A 27 3544 4754 3164 43 -209 632 C ATOM 220 CB ASP A 27 -28.257 5.256 6.447 1.00 33.02 C ANISOU 220 CB ASP A 27 3958 5018 3569 -71 -272 664 C ATOM 221 CG ASP A 27 -29.016 4.055 5.931 1.00 37.96 C ANISOU 221 CG ASP A 27 4590 5645 4188 -210 -382 750 C ATOM 222 OD1 ASP A 27 -30.273 4.128 5.894 1.00 40.19 O ANISOU 222 OD1 ASP A 27 4766 6092 4413 -257 -398 826 O ATOM 223 OD2 ASP A 27 -28.350 3.070 5.548 1.00 40.63 O ANISOU 223 OD2 ASP A 27 5045 5826 4566 -264 -461 738 O ATOM 224 C ASP A 27 -28.451 7.687 7.036 1.00 30.98 C ANISOU 224 C ASP A 27 3637 4888 3244 160 -134 577 C ATOM 225 O ASP A 27 -27.623 8.542 6.664 1.00 26.37 O ANISOU 225 O ASP A 27 3144 4192 2683 237 -96 497 O ATOM 226 N MET A 28 -28.933 7.623 8.267 1.00 31.68 N ANISOU 226 N MET A 28 3625 5131 3280 157 -125 627 N ATOM 227 CA MET A 28 -28.419 8.450 9.369 1.00 30.69 C ANISOU 227 CA MET A 28 3500 5029 3131 259 -72 581 C ATOM 228 CB MET A 28 -29.315 8.292 10.591 1.00 33.10 C ANISOU 228 CB MET A 28 3660 5566 3348 261 -68 652 C ATOM 229 CG MET A 28 -29.143 9.407 11.571 1.00 33.31 C ANISOU 229 CG MET A 28 3683 5653 3317 420 -22 593 C ATOM 230 SD MET A 28 -30.128 9.112 13.025 1.00 34.97 S ANISOU 230 SD MET A 28 3707 6173 3407 427 -13 679 S ATOM 231 CE MET A 28 -31.769 8.992 12.314 1.00 33.12 C ANISOU 231 CE MET A 28 3320 6189 3075 417 -37 751 C ATOM 232 C MET A 28 -27.001 7.976 9.693 1.00 28.70 C ANISOU 232 C MET A 28 3336 4611 2956 207 -70 547 C ATOM 233 O MET A 28 -26.796 6.755 9.727 1.00 27.04 O ANISOU 233 O MET A 28 3132 4359 2780 91 -118 594 O ATOM 234 N ASP A 29 -26.064 8.914 9.827 1.00 28.00 N ANISOU 234 N ASP A 29 3325 4429 2884 289 -30 468 N ATOM 235 CA ASP A 29 -24.678 8.630 10.269 1.00 29.22 C ANISOU 235 CA ASP A 29 3540 4468 3094 257 -21 430 C ATOM 236 CB ASP A 29 -23.802 9.871 10.096 1.00 28.89 C ANISOU 236 CB ASP A 29 3584 4338 3052 326 10 355 C ATOM 237 CG ASP A 29 -23.674 10.305 8.642 1.00 28.48 C ANISOU 237 CG ASP A 29 3601 4207 3012 322 8 326 C ATOM 238 OD1 ASP A 29 -23.376 9.454 7.798 1.00 28.55 O ANISOU 238 OD1 ASP A 29 3618 4171 3059 260 -7 330 O ATOM 239 OD2 ASP A 29 -23.955 11.477 8.365 1.00 31.78 O ANISOU 239 OD2 ASP A 29 4074 4613 3388 391 10 300 O ATOM 240 C ASP A 29 -24.741 8.124 11.712 1.00 29.92 C ANISOU 240 C ASP A 29 3564 4642 3163 236 -23 473 C ATOM 241 O ASP A 29 -25.741 8.383 12.385 1.00 33.24 O ANISOU 241 O ASP A 29 3896 5218 3513 275 -15 516 O ATOM 242 N ASP A 30 -23.783 7.298 12.098 1.00 30.91 N ANISOU 242 N ASP A 30 3722 4686 3335 177 -42 467 N ATOM 243 CA ASP A 30 -23.521 6.927 13.514 1.00 30.34 C ANISOU 243 CA ASP A 30 3617 4660 3250 163 -42 492 C ATOM 244 CB ASP A 30 -22.718 5.635 13.582 1.00 30.76 C ANISOU 244 CB ASP A 30 3723 4613 3350 81 -98 498 C ATOM 245 CG ASP A 30 -23.373 4.434 12.928 1.00 33.87 C ANISOU 245 CG ASP A 30 4133 4990 3746 -22 -182 565 C ATOM 246 OD1 ASP A 30 -24.597 4.486 12.657 1.00 36.43 O ANISOU 246 OD1 ASP A 30 4391 5420 4029 -61 -191 633 O ATOM 247 OD2 ASP A 30 -22.668 3.438 12.739 1.00 34.00 O ANISOU 247 OD2 ASP A 30 4232 4892 3792 -59 -250 549 O ATOM 248 C ASP A 30 -22.804 8.090 14.209 1.00 29.82 C ANISOU 248 C ASP A 30 3578 4575 3174 261 6 425 C ATOM 249 O ASP A 30 -21.858 8.667 13.611 1.00 28.73 O ANISOU 249 O ASP A 30 3513 4330 3070 281 21 358 O ATOM 250 N TYR A 31 -23.198 8.382 15.455 1.00 30.03 N ANISOU 250 N TYR A 31 3550 4711 3148 308 21 447 N ATOM 251 CA TYR A 31 -22.695 9.525 16.248 1.00 29.87 C ANISOU 251 CA TYR A 31 3568 4680 3101 414 48 387 C ATOM 252 CB TYR A 31 -23.699 10.681 16.273 1.00 32.67 C ANISOU 252 CB TYR A 31 3909 5134 3368 545 55 372 C ATOM 253 CG TYR A 31 -24.062 11.236 14.916 1.00 38.41 C ANISOU 253 CG TYR A 31 4685 5808 4097 565 46 349 C ATOM 254 CD1 TYR A 31 -23.309 12.239 14.327 1.00 41.34 C ANISOU 254 CD1 TYR A 31 5185 6036 4487 595 36 284 C ATOM 255 CE1 TYR A 31 -23.646 12.759 13.085 1.00 40.53 C ANISOU 255 CE1 TYR A 31 5138 5883 4378 607 22 268 C ATOM 256 CZ TYR A 31 -24.753 12.278 12.413 1.00 44.08 C ANISOU 256 CZ TYR A 31 5510 6428 4810 602 22 309 C ATOM 257 OH TYR A 31 -25.093 12.796 11.194 1.00 46.88 O ANISOU 257 OH TYR A 31 5924 6731 5157 621 6 291 O ATOM 258 CE2 TYR A 31 -25.510 11.264 12.975 1.00 42.36 C ANISOU 258 CE2 TYR A 31 5158 6361 4576 563 29 378 C ATOM 259 CD2 TYR A 31 -25.161 10.758 14.217 1.00 42.88 C ANISOU 259 CD2 TYR A 31 5175 6475 4642 538 40 401 C ATOM 260 C TYR A 31 -22.407 9.030 17.663 1.00 28.10 C ANISOU 260 C TYR A 31 3305 4507 2862 404 48 411 C ATOM 261 O TYR A 31 -23.129 8.133 18.159 1.00 26.84 O ANISOU 261 O TYR A 31 3062 4464 2671 343 34 491 O ATOM 262 N CYS A 32 -21.399 9.617 18.296 1.00 28.32 N ANISOU 262 N CYS A 32 3394 4458 2905 450 56 351 N ATOM 263 CA CYS A 32 -21.077 9.385 19.733 1.00 27.50 C ANISOU 263 CA CYS A 32 3267 4400 2781 468 58 360 C ATOM 264 CB CYS A 32 -19.770 10.067 20.102 1.00 27.92 C ANISOU 264 CB CYS A 32 3407 4333 2867 497 57 285 C ATOM 265 SG CYS A 32 -18.365 9.495 19.119 1.00 26.55 S ANISOU 265 SG CYS A 32 3282 4018 2786 395 48 247 S ATOM 266 C CYS A 32 -22.231 9.918 20.593 1.00 31.12 C ANISOU 266 C CYS A 32 3652 5040 3131 574 71 389 C ATOM 267 O CYS A 32 -22.823 10.936 20.218 1.00 29.54 O ANISOU 267 O CYS A 32 3472 4875 2876 683 72 355 O ATOM 268 N ASN A 33 -22.528 9.263 21.722 1.00 32.16 N ANISOU 268 N ASN A 33 3706 5294 3218 554 74 447 N ATOM 269 CA ASN A 33 -23.696 9.599 22.579 1.00 37.49 C ANISOU 269 CA ASN A 33 4273 6208 3763 652 90 487 C ATOM 270 CB ASN A 33 -24.444 8.341 23.019 1.00 38.86 C ANISOU 270 CB ASN A 33 4320 6550 3893 518 84 612 C ATOM 271 CG ASN A 33 -23.526 7.374 23.722 1.00 37.71 C ANISOU 271 CG ASN A 33 4219 6301 3807 405 60 638 C ATOM 272 OD1 ASN A 33 -22.489 7.786 24.225 1.00 38.96 O ANISOU 272 OD1 ASN A 33 4460 6334 4008 467 65 561 O ATOM 273 ND2 ASN A 33 -23.819 6.093 23.627 1.00 38.42 N ANISOU 273 ND2 ASN A 33 4279 6413 3906 233 18 739 N ATOM 274 C ASN A 33 -23.218 10.418 23.787 1.00 39.04 C ANISOU 274 C ASN A 33 4513 6410 3910 791 94 425 C ATOM 275 O ASN A 33 -24.076 10.913 24.541 1.00 42.34 O ANISOU 275 O ASN A 33 4856 7028 4200 926 105 432 O ATOM 276 N GLY A 34 -21.904 10.568 23.955 1.00 37.31 N ANISOU 276 N GLY A 34 4406 5994 3775 769 81 364 N ATOM 277 CA GLY A 34 -21.303 11.332 25.062 1.00 39.15 C ANISOU 277 CA GLY A 34 4704 6196 3972 882 69 302 C ATOM 278 C GLY A 34 -21.415 10.576 26.378 1.00 39.22 C ANISOU 278 C GLY A 34 4628 6336 3935 865 82 358 C ATOM 279 O GLY A 34 -21.246 11.217 27.431 1.00 40.63 O ANISOU 279 O GLY A 34 4836 6550 4050 990 75 316 O ATOM 280 N LYS A 35 -21.642 9.255 26.318 1.00 38.22 N ANISOU 280 N LYS A 35 4423 6262 3835 710 87 451 N ATOM 281 CA LYS A 35 -21.866 8.380 27.503 1.00 40.62 C ANISOU 281 CA LYS A 35 4649 6701 4083 653 88 532 C ATOM 282 CB LYS A 35 -23.336 7.949 27.592 1.00 45.82 C ANISOU 282 CB LYS A 35 5152 7633 4625 615 102 645 C ATOM 283 CG LYS A 35 -24.330 9.084 27.785 1.00 49.31 C ANISOU 283 CG LYS A 35 5515 8288 4931 813 133 614 C ATOM 284 CD LYS A 35 -25.745 8.615 28.073 1.00 54.77 C ANISOU 284 CD LYS A 35 6012 9320 5477 776 152 734 C ATOM 285 CE LYS A 35 -26.432 8.021 26.861 1.00 57.84 C ANISOU 285 CE LYS A 35 6346 9732 5895 630 139 808 C ATOM 286 NZ LYS A 35 -27.739 7.419 27.218 1.00 61.02 N ANISOU 286 NZ LYS A 35 6547 10486 6151 541 147 951 N ATOM 287 C LYS A 35 -20.959 7.141 27.465 1.00 38.47 C ANISOU 287 C LYS A 35 4432 6272 3910 489 51 561 C ATOM 288 O LYS A 35 -20.585 6.721 28.559 1.00 38.63 O ANISOU 288 O LYS A 35 4455 6312 3910 475 40 581 O ATOM 289 N THR A 36 -20.605 6.610 26.278 1.00 35.91 N ANISOU 289 N THR A 36 4161 5804 3679 393 25 554 N ATOM 290 CA THR A 36 -19.923 5.293 26.046 1.00 34.01 C ANISOU 290 CA THR A 36 3983 5427 3509 257 -34 581 C ATOM 291 CB THR A 36 -20.937 4.197 25.707 1.00 38.36 C ANISOU 291 CB THR A 36 4490 6060 4022 107 -81 706 C ATOM 292 OG1 THR A 36 -21.551 4.461 24.446 1.00 40.94 O ANISOU 292 OG1 THR A 36 4795 6394 4364 98 -71 706 O ATOM 293 CG2 THR A 36 -22.013 4.074 26.766 1.00 43.87 C ANISOU 293 CG2 THR A 36 5071 7000 4597 74 -68 817 C ATOM 294 C THR A 36 -18.853 5.410 24.938 1.00 32.30 C ANISOU 294 C THR A 36 3856 5020 3395 267 -44 487 C ATOM 295 O THR A 36 -18.926 6.387 24.183 1.00 26.87 O ANISOU 295 O THR A 36 3169 4319 2719 330 -7 435 O ATOM 296 N CYS A 37 -17.851 4.510 24.899 1.00 28.10 N ANISOU 296 N CYS A 37 3398 4359 2918 221 -97 459 N ATOM 297 CA CYS A 37 -16.608 4.691 24.095 1.00 28.51 C ANISOU 297 CA CYS A 37 3510 4279 3042 257 -100 357 C ATOM 298 CB CYS A 37 -15.371 4.087 24.741 1.00 27.51 C ANISOU 298 CB CYS A 37 3437 4075 2939 274 -142 305 C ATOM 299 SG CYS A 37 -14.834 4.971 26.231 1.00 28.76 S ANISOU 299 SG CYS A 37 3577 4274 3075 349 -103 270 S ATOM 300 C CYS A 37 -16.773 4.090 22.699 1.00 29.80 C ANISOU 300 C CYS A 37 3701 4383 3235 207 -134 361 C ATOM 301 O CYS A 37 -15.994 4.459 21.809 1.00 30.60 O ANISOU 301 O CYS A 37 3823 4428 3376 242 -119 285 O ATOM 302 N ASP A 38 -17.758 3.216 22.513 1.00 31.03 N ANISOU 302 N ASP A 38 3857 4566 3365 119 -185 452 N ATOM 303 CA ASP A 38 -18.000 2.558 21.209 1.00 34.24 C ANISOU 303 CA ASP A 38 4309 4906 3794 69 -238 461 C ATOM 304 CB ASP A 38 -18.591 1.156 21.398 1.00 37.68 C ANISOU 304 CB ASP A 38 4806 5312 4199 -50 -352 558 C ATOM 305 CG ASP A 38 -17.540 0.099 21.797 1.00 52.16 C ANISOU 305 CG ASP A 38 6762 7012 6042 -37 -452 515 C ATOM 306 OD1 ASP A 38 -16.328 0.340 21.558 1.00 50.97 O ANISOU 306 OD1 ASP A 38 6636 6803 5928 73 -433 399 O ATOM 307 OD2 ASP A 38 -17.923 -0.959 22.384 1.00 51.00 O ANISOU 307 OD2 ASP A 38 6688 6834 5855 -139 -559 602 O ATOM 308 C ASP A 38 -18.772 3.541 20.320 1.00 30.40 C ANISOU 308 C ASP A 38 3758 4486 3306 89 -170 464 C ATOM 309 O ASP A 38 -19.293 4.580 20.804 1.00 27.03 O ANISOU 309 O ASP A 38 3262 4163 2845 137 -102 473 O ATOM 310 N CYS A 39 -18.678 3.332 19.023 1.00 30.11 N ANISOU 310 N CYS A 39 3759 4381 3299 82 -191 435 N ATOM 311 CA CYS A 39 -19.476 4.059 18.023 1.00 31.25 C ANISOU 311 CA CYS A 39 3862 4571 3440 88 -148 445 C ATOM 312 CB CYS A 39 -18.689 4.189 16.731 1.00 28.93 C ANISOU 312 CB CYS A 39 3616 4187 3186 125 -145 365 C ATOM 313 SG CYS A 39 -19.611 5.104 15.481 1.00 28.18 S ANISOU 313 SG CYS A 39 3489 4131 3085 133 -100 374 S ATOM 314 C CYS A 39 -20.783 3.292 17.816 1.00 34.71 C ANISOU 314 C CYS A 39 4276 5068 3841 -14 -204 553 C ATOM 315 O CYS A 39 -20.756 2.185 17.283 1.00 37.05 O ANISOU 315 O CYS A 39 4648 5279 4151 -84 -296 577 O ATOM 316 N PRO A 40 -21.909 3.726 18.422 1.00 37.62 N ANISOU 316 N PRO A 40 4545 5598 4149 -32 -169 629 N ATOM 317 CA PRO A 40 -23.113 2.904 18.424 1.00 39.56 C ANISOU 317 CA PRO A 40 4745 5942 4341 -163 -229 754 C ATOM 318 CB PRO A 40 -24.074 3.636 19.374 1.00 41.55 C ANISOU 318 CB PRO A 40 4856 6426 4504 -130 -164 811 C ATOM 319 CG PRO A 40 -23.571 5.080 19.431 1.00 40.07 C ANISOU 319 CG PRO A 40 4666 6229 4330 47 -74 697 C ATOM 320 CD PRO A 40 -22.107 5.045 19.050 1.00 35.88 C ANISOU 320 CD PRO A 40 4254 5487 3892 79 -82 597 C ATOM 321 C PRO A 40 -23.678 2.787 16.994 1.00 42.28 C ANISOU 321 C PRO A 40 5106 6255 4705 -197 -257 762 C ATOM 322 O PRO A 40 -23.830 3.816 16.329 1.00 37.25 O ANISOU 322 O PRO A 40 4434 5642 4075 -103 -188 705 O ATOM 323 N ARG A 41 -23.902 1.553 16.519 1.00 45.94 N ANISOU 323 N ARG A 41 5644 6639 5172 -326 -371 825 N ATOM 324 CA ARG A 41 -24.594 1.302 15.227 1.00 48.67 C ANISOU 324 CA ARG A 41 6006 6963 5523 -379 -418 852 C ATOM 325 CB ARG A 41 -24.441 -0.159 14.773 1.00 53.77 C ANISOU 325 CB ARG A 41 6800 7449 6179 -499 -577 892 C ATOM 326 CG ARG A 41 -25.546 -1.115 15.204 1.00 60.13 C ANISOU 326 CG ARG A 41 7592 8338 6913 -709 -690 1058 C ATOM 327 CD ARG A 41 -25.430 -2.477 14.532 1.00 65.02 C ANISOU 327 CD ARG A 41 8405 8759 7539 -821 -878 1090 C ATOM 328 NE ARG A 41 -25.353 -2.388 13.073 1.00 68.19 N ANISOU 328 NE ARG A 41 8869 9056 7984 -749 -894 1014 N ATOM 329 CZ ARG A 41 -26.400 -2.271 12.253 1.00 72.85 C ANISOU 329 CZ ARG A 41 9400 9725 8555 -824 -906 1076 C ATOM 330 NH1 ARG A 41 -27.631 -2.238 12.737 1.00 75.49 N ANISOU 330 NH1 ARG A 41 9596 10266 8820 -975 -905 1218 N ATOM 331 NH2 ARG A 41 -26.214 -2.194 10.947 1.00 71.99 N ANISOU 331 NH2 ARG A 41 9359 9507 8484 -744 -920 996 N ATOM 332 C ARG A 41 -26.025 1.830 15.384 1.00 46.34 C ANISOU 332 C ARG A 41 5551 6903 5152 -422 -373 945 C ATOM 333 O ARG A 41 -26.738 1.391 16.298 1.00 46.22 O ANISOU 333 O ARG A 41 5457 7042 5063 -534 -402 1060 O ATOM 334 N ASN A 42 -26.300 2.937 14.709 1.00 46.78 N ANISOU 334 N ASN A 42 5549 7011 5211 -304 -289 882 N ATOM 335 CA ASN A 42 -27.605 3.639 14.696 1.00 49.35 C ANISOU 335 CA ASN A 42 5723 7570 5455 -281 -241 936 C ATOM 336 CB ASN A 42 -27.659 4.593 13.504 1.00 50.58 C ANISOU 336 CB ASN A 42 5900 7675 5640 -160 -193 848 C ATOM 337 CG ASN A 42 -28.675 5.690 13.679 1.00 51.87 C ANISOU 337 CG ASN A 42 5933 8059 5714 -46 -129 849 C ATOM 338 OD1 ASN A 42 -29.874 5.431 13.634 1.00 53.17 O ANISOU 338 OD1 ASN A 42 5975 8425 5800 -111 -152 941 O ATOM 339 ND2 ASN A 42 -28.196 6.916 13.841 1.00 52.40 N ANISOU 339 ND2 ASN A 42 6034 8092 5783 126 -63 745 N ATOM 340 C ASN A 42 -28.736 2.612 14.618 1.00 50.96 C ANISOU 340 C ASN A 42 5863 7902 5596 -477 -332 1086 C ATOM 341 O ASN A 42 -28.703 1.737 13.755 1.00 52.75 O ANISOU 341 O ASN A 42 6191 7986 5864 -587 -429 1112 O ATOM 342 N PRO A 43 -29.778 2.697 15.482 1.00 49.51 N ANISOU 342 N PRO A 43 5510 8003 5298 -528 -313 1191 N ATOM 343 CA PRO A 43 -30.908 1.768 15.414 1.00 52.92 C ANISOU 343 CA PRO A 43 5857 8599 5650 -747 -405 1355 C ATOM 344 CB PRO A 43 -31.652 2.007 16.748 1.00 53.56 C ANISOU 344 CB PRO A 43 5741 9015 5594 -763 -354 1448 C ATOM 345 CG PRO A 43 -31.282 3.424 17.162 1.00 52.36 C ANISOU 345 CG PRO A 43 5545 8911 5435 -483 -223 1307 C ATOM 346 CD PRO A 43 -29.909 3.676 16.573 1.00 50.25 C ANISOU 346 CD PRO A 43 5482 8292 5317 -379 -213 1161 C ATOM 347 C PRO A 43 -31.805 2.022 14.184 1.00 55.51 C ANISOU 347 C PRO A 43 6130 8995 5964 -748 -415 1364 C ATOM 348 O PRO A 43 -32.333 1.056 13.603 1.00 50.75 O ANISOU 348 O PRO A 43 5558 8370 5353 -946 -530 1467 O ATOM 349 N HIS A 44 -31.882 3.286 13.746 1.00 54.41 N ANISOU 349 N HIS A 44 5945 8900 5828 -531 -314 1251 N ATOM 350 CA HIS A 44 -32.926 3.804 12.818 1.00 56.38 C ANISOU 350 CA HIS A 44 6096 9298 6027 -484 -303 1255 C ATOM 351 CB HIS A 44 -33.212 5.287 13.118 1.00 59.40 C ANISOU 351 CB HIS A 44 6381 9847 6340 -225 -193 1158 C ATOM 352 CG HIS A 44 -33.544 5.566 14.549 1.00 66.38 C ANISOU 352 CG HIS A 44 7117 10996 7106 -170 -144 1198 C ATOM 353 ND1 HIS A 44 -34.193 4.643 15.355 1.00 67.91 N ANISOU 353 ND1 HIS A 44 7174 11422 7206 -368 -186 1357 N ATOM 354 CE1 HIS A 44 -34.343 5.150 16.564 1.00 68.94 C ANISOU 354 CE1 HIS A 44 7185 11776 7231 -255 -123 1357 C ATOM 355 NE2 HIS A 44 -33.819 6.385 16.568 1.00 69.59 N ANISOU 355 NE2 HIS A 44 7341 11761 7338 15 -53 1196 N ATOM 356 CD2 HIS A 44 -33.323 6.655 15.322 1.00 68.62 C ANISOU 356 CD2 HIS A 44 7377 11356 7337 55 -68 1104 C ATOM 357 C HIS A 44 -32.506 3.578 11.356 1.00 51.80 C ANISOU 357 C HIS A 44 5676 8447 5556 -497 -352 1193 C ATOM 358 O HIS A 44 -32.337 4.584 10.637 1.00 47.70 O ANISOU 358 O HIS A 44 5192 7865 5067 -320 -290 1080 O ATOM 359 N LYS A 45 -32.341 2.313 10.939 1.00 50.99 N ANISOU 359 N LYS A 45 5683 8189 5499 -692 -472 1264 N ATOM 360 CA LYS A 45 -32.041 1.927 9.527 1.00 52.78 C ANISOU 360 CA LYS A 45 6063 8181 5809 -710 -541 1215 C ATOM 361 CB LYS A 45 -30.628 2.369 9.131 1.00 52.62 C ANISOU 361 CB LYS A 45 6198 7902 5891 -549 -488 1060 C ATOM 362 CG LYS A 45 -29.490 1.665 9.858 1.00 57.34 C ANISOU 362 CG LYS A 45 6913 8338 6534 -581 -526 1040 C ATOM 363 CD LYS A 45 -28.136 2.334 9.661 1.00 56.02 C ANISOU 363 CD LYS A 45 6839 8005 6441 -409 -448 891 C ATOM 364 CE LYS A 45 -27.060 1.745 10.546 1.00 58.32 C ANISOU 364 CE LYS A 45 7213 8186 6760 -420 -474 869 C ATOM 365 NZ LYS A 45 -25.907 2.666 10.686 1.00 62.03 N ANISOU 365 NZ LYS A 45 7705 8588 7273 -261 -373 745 N ATOM 366 C LYS A 45 -32.215 0.415 9.351 1.00 51.58 C ANISOU 366 C LYS A 45 6012 7928 5657 -951 -710 1331 C ATOM 367 O LYS A 45 -32.069 -0.316 10.330 1.00 55.57 O ANISOU 367 O LYS A 45 6533 8445 6133 -1079 -769 1413 O TER 368 LYS A 45 HETATM 761 S SO4 C 1 -9.495 0.366 13.117 1.00 35.34 S HETATM 762 O1 SO4 C 1 -10.757 -0.126 13.610 1.00 32.33 O HETATM 763 O2 SO4 C 1 -9.449 0.229 11.686 1.00 39.00 O HETATM 764 O3 SO4 C 1 -9.339 1.761 13.475 1.00 32.87 O HETATM 765 O4 SO4 C 1 -8.426 -0.394 13.690 1.00 36.18 O HETATM 766 O HOH E 1 -10.063 -7.090 13.949 1.00 21.68 O HETATM 767 O HOH E 2 -14.745 9.950 -1.758 1.00 19.40 O HETATM 768 O HOH E 3 -8.435 6.596 5.352 1.00 19.35 O HETATM 769 O HOH E 4 -23.919 5.896 -0.957 1.00 23.22 O HETATM 770 O HOH E 5 -13.222 7.011 -0.306 1.00 18.75 O HETATM 771 O HOH E 6 -9.771 -6.100 17.691 1.00 21.03 O HETATM 772 O HOH E 7 -10.887 8.793 19.842 1.00 28.24 O HETATM 773 O HOH E 8 -8.176 15.886 -3.521 1.00 22.24 O HETATM 774 O HOH E 9 -27.530 17.593 24.103 1.00 25.59 O HETATM 775 O HOH E 10 -9.355 15.612 6.934 1.00 29.03 O HETATM 776 O HOH E 11 -13.812 8.645 32.587 1.00 23.96 O HETATM 777 O HOH E 12 -10.022 1.673 -0.391 1.00 37.05 O HETATM 778 O HOH E 13 -13.060 6.552 29.178 1.00 25.67 O HETATM 779 O HOH E 14 -20.427 8.920 -11.004 1.00 27.78 O HETATM 780 O HOH E 15 -20.664 6.793 21.959 1.00 27.10 O HETATM 781 O HOH E 16 -24.048 7.186 -4.650 1.00 26.95 O HETATM 782 O HOH E 17 -17.716 15.963 2.361 1.00 33.19 O HETATM 783 O HOH E 18 -20.637 6.813 -7.263 1.00 31.89 O HETATM 784 O HOH E 19 -31.293 5.510 8.333 1.00 29.79 O HETATM 785 O HOH E 20 -16.068 4.484 14.684 1.00 27.08 O HETATM 786 O HOH E 21 -8.925 2.373 16.152 1.00 32.48 O HETATM 787 O HOH E 22 -19.084 9.877 23.545 1.00 26.09 O HETATM 788 O HOH E 23 -17.737 4.642 7.062 1.00 25.25 O HETATM 789 O HOH E 24 -9.466 -0.444 22.684 1.00 30.03 O HETATM 790 O HOH E 25 -9.520 -0.188 3.540 1.00 33.70 O HETATM 791 O HOH E 26 -30.031 4.758 1.547 1.00 32.90 O HETATM 792 O HOH E 27 -14.354 15.784 7.736 1.00 26.00 O HETATM 793 O HOH E 28 -20.418 15.634 9.016 1.00 37.73 O HETATM 794 O HOH E 29 -6.144 -2.883 16.116 1.00 37.44 O HETATM 795 O HOH E 30 -2.748 5.338 13.632 1.00 26.12 O HETATM 796 O HOH E 31 -11.829 15.921 10.682 1.00 43.86 O HETATM 797 O HOH E 32 -16.024 3.288 -5.868 1.00 33.79 O HETATM 798 O HOH E 33 -20.806 2.030 14.107 1.00 33.42 O END If you find results from this site helpful for your research, please cite one of our papers:
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