TITLE STRUCTURE OF COVID-19 MAIN PROTEASE BOUND TO POTENT TITLE 2 BROAD-SPECTRUM NON-COVALENT INHIBITOR X77 EXPDTA X-RAY DIFFRACTION REMARK 2 RESOLUTION. 2.10 ANGSTROMS REMARK 4 6W63 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 200 TEMPERATURE (KELVIN) : 100.00 REMARK 200 PH : NULL REMARK 888 REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC) ATOM 1 N SER A 1 15.647 37.895 -22.389 1.00 39.55 N1+ ANISOU 1 N SER A 1 5046 4997 4984 -235 -442 334 ATOM 2 CA SER A 1 15.172 37.375 -21.062 1.00 26.86 C ANISOU 2 CA SER A 1 3450 3368 3388 -178 -402 288 ATOM 3 C SER A 1 13.627 37.513 -21.030 1.00 25.13 C ANISOU 3 C SER A 1 3248 3113 3188 -148 -405 251 ATOM 4 O SER A 1 12.995 37.975 -21.985 1.00 21.95 O ANISOU 4 O SER A 1 2847 2702 2791 -168 -431 257 ATOM 5 CB SER A 1 15.917 38.038 -19.879 1.00 43.51 C ANISOU 5 CB SER A 1 5575 5450 5507 -164 -432 291 ATOM 6 OG SER A 1 15.710 39.435 -19.819 1.00 44.46 O ANISOU 6 OG SER A 1 5718 5530 5646 -181 -509 307 ATOM 7 N GLY A 2 13.046 37.053 -19.912 1.00 21.77 N ANISOU 7 N GLY A 2 2831 2671 2770 -101 -376 213 ATOM 8 CA GLY A 2 11.613 36.869 -19.710 1.00 26.23 C ANISOU 8 CA GLY A 2 3404 3215 3347 -68 -365 174 ATOM 9 C GLY A 2 11.261 35.393 -19.946 1.00 21.76 C ANISOU 9 C GLY A 2 2821 2678 2769 -54 -296 156 ATOM 10 O GLY A 2 12.053 34.624 -20.501 1.00 26.30 O ANISOU 10 O GLY A 2 3378 3288 3328 -70 -260 171 ATOM 11 N PHE A 3 10.049 35.003 -19.526 1.00 24.77 N ANISOU 11 N PHE A 3 3207 3046 3158 -22 -279 122 ATOM 12 CA PHE A 3 9.530 33.655 -19.733 1.00 29.60 C ANISOU 12 CA PHE A 3 3806 3680 3762 -10 -220 106 ATOM 13 C PHE A 3 8.000 33.738 -19.785 1.00 28.96 C ANISOU 13 C PHE A 3 3727 3584 3690 9 -220 79 ATOM 14 O PHE A 3 7.371 34.192 -18.829 1.00 33.78 O ANISOU 14 O PHE A 3 4348 4176 4311 37 -239 55 ATOM 15 CB PHE A 3 10.060 32.699 -18.639 1.00 28.47 C ANISOU 15 CB PHE A 3 3658 3547 3612 16 -179 94 ATOM 16 CG PHE A 3 10.041 31.236 -19.042 1.00 33.75 C ANISOU 16 CG PHE A 3 4310 4241 4271 16 -126 91 ATOM 17 CD1 PHE A 3 10.984 30.758 -19.979 1.00 29.96 C ANISOU 17 CD1 PHE A 3 3817 3787 3780 -8 -112 111 ATOM 18 CD2 PHE A 3 9.014 30.378 -18.602 1.00 24.72 C ANISOU 18 CD2 PHE A 3 3165 3097 3130 39 -93 69 ATOM 19 CE1 PHE A 3 10.917 29.445 -20.427 1.00 36.09 C ANISOU 19 CE1 PHE A 3 4580 4583 4549 -4 -69 103 ATOM 20 CE2 PHE A 3 8.977 29.064 -19.049 1.00 28.56 C ANISOU 20 CE2 PHE A 3 3640 3600 3611 38 -52 66 ATOM 21 CZ PHE A 3 9.914 28.603 -19.964 1.00 24.59 C ANISOU 21 CZ PHE A 3 3126 3118 3100 19 -41 81 ATOM 22 N ARG A 4 7.446 33.314 -20.928 1.00 25.67 N ANISOU 22 N ARG A 4 3302 3181 3271 -7 -200 81 ATOM 23 CA ARG A 4 6.027 33.349 -21.265 1.00 23.55 C ANISOU 23 CA ARG A 4 3035 2901 3012 6 -201 59 ATOM 24 C ARG A 4 5.569 31.955 -21.697 1.00 27.05 C ANISOU 24 C ARG A 4 3465 3365 3447 7 -149 51 ATOM 25 O ARG A 4 6.376 31.150 -22.162 1.00 18.26 O ANISOU 25 O ARG A 4 2342 2274 2323 -10 -122 64 ATOM 26 CB ARG A 4 5.830 34.343 -22.433 1.00 25.69 C ANISOU 26 CB ARG A 4 3312 3156 3292 -20 -251 72 ATOM 27 CG ARG A 4 5.884 35.823 -22.018 1.00 36.07 C ANISOU 27 CG ARG A 4 4644 4438 4622 -16 -315 73 ATOM 28 CD ARG A 4 4.565 36.292 -21.389 1.00 40.40 C ANISOU 28 CD ARG A 4 5199 4963 5188 16 -338 39 ATOM 29 NE ARG A 4 4.637 37.655 -20.851 1.00 48.64 N ANISOU 29 NE ARG A 4 6261 5970 6251 22 -410 35 ATOM 30 CZ ARG A 4 3.573 38.379 -20.457 1.00 33.50 C ANISOU 30 CZ ARG A 4 4350 4030 4348 60 -439 -2 ATOM 31 NH1 ARG A 4 2.329 37.881 -20.514 1.00 42.15 N ANISOU 31 NH1 ARG A 4 5434 5143 5439 91 -400 -35 ATOM 32 NH2 ARG A 4 3.759 39.621 -19.995 1.00 30.56 N1+ ANISOU 32 NH2 ARG A 4 3996 3621 3996 66 -511 -7 ATOM 33 N LYS A 5 4.254 31.721 -21.596 1.00 22.11 N ANISOU 33 N LYS A 5 2838 2734 2828 27 -139 28 ATOM 34 CA LYS A 5 3.598 30.560 -22.184 1.00 25.57 C ANISOU 34 CA LYS A 5 3267 3186 3263 22 -102 23 ATOM 35 C LYS A 5 3.441 30.796 -23.694 1.00 18.74 C ANISOU 35 C LYS A 5 2400 2324 2397 -10 -117 38 ATOM 36 O LYS A 5 2.589 31.581 -24.110 1.00 30.86 O ANISOU 36 O LYS A 5 3940 3843 3942 -15 -151 35 ATOM 37 CB LYS A 5 2.288 30.294 -21.432 1.00 37.63 C ANISOU 37 CB LYS A 5 4792 4711 4796 47 -92 -2 ATOM 38 CG LYS A 5 1.627 28.969 -21.834 1.00 53.53 C ANISOU 38 CG LYS A 5 6795 6740 6804 48 -46 -5 ATOM 39 CD LYS A 5 0.781 28.349 -20.716 1.00 55.62 C ANISOU 39 CD LYS A 5 7054 7012 7065 74 -28 -20 ATOM 40 CE LYS A 5 1.628 27.630 -19.650 1.00 52.04 C ANISOU 40 CE LYS A 5 6598 6569 6605 76 2 -11 ATOM 41 NZ LYS A 5 0.770 26.921 -18.688 1.00 60.07 N1+ ANISOU 41 NZ LYS A 5 7608 7599 7616 97 15 -22 ATOM 42 N MET A 6 4.361 30.183 -24.453 1.00 21.91 N ANISOU 42 N MET A 6 2793 2747 2786 -30 -97 52 ATOM 43 CA MET A 6 4.643 30.503 -25.844 1.00 22.60 C ANISOU 43 CA MET A 6 2874 2847 2865 -64 -112 71 ATOM 44 C MET A 6 4.167 29.361 -26.746 1.00 29.08 C ANISOU 44 C MET A 6 3685 3684 3679 -68 -76 61 ATOM 45 O MET A 6 4.647 28.234 -26.617 1.00 20.25 O ANISOU 45 O MET A 6 2560 2579 2555 -55 -40 51 ATOM 46 CB MET A 6 6.162 30.755 -25.963 1.00 23.13 C ANISOU 46 CB MET A 6 2934 2936 2917 -85 -119 95 ATOM 47 CG MET A 6 6.646 31.156 -27.367 1.00 33.71 C ANISOU 47 CG MET A 6 4264 4302 4241 -125 -135 118 ATOM 48 SD MET A 6 8.434 31.440 -27.485 1.00 49.44 S ANISOU 48 SD MET A 6 6245 6325 6215 -151 -150 150 ATOM 49 CE MET A 6 8.586 32.999 -26.571 1.00 37.49 C ANISOU 49 CE MET A 6 4753 4769 4722 -143 -200 160 ATOM 50 N ALA A 7 3.250 29.694 -27.665 1.00 21.87 N ANISOU 50 N ALA A 7 2772 2768 2768 -85 -91 62 ATOM 51 CA ALA A 7 2.795 28.796 -28.718 1.00 22.69 C ANISOU 51 CA ALA A 7 2868 2888 2866 -91 -64 53 ATOM 52 C ALA A 7 3.710 28.871 -29.953 1.00 21.13 C ANISOU 52 C ALA A 7 2659 2724 2647 -124 -67 70 ATOM 53 O ALA A 7 4.395 29.874 -30.164 1.00 18.97 O ANISOU 53 O ALA A 7 2383 2459 2365 -149 -97 94 ATOM 54 CB ALA A 7 1.355 29.175 -29.089 1.00 18.47 C ANISOU 54 CB ALA A 7 2339 2333 2344 -90 -76 44 ATOM 55 N PHE A 8 3.656 27.813 -30.776 1.00 17.58 N ANISOU 55 N PHE A 8 2199 2294 2186 -125 -38 58 ATOM 56 CA PHE A 8 4.195 27.782 -32.135 1.00 17.77 C ANISOU 56 CA PHE A 8 2208 2358 2186 -156 -40 70 ATOM 57 C PHE A 8 3.409 28.745 -33.056 1.00 18.67 C ANISOU 57 C PHE A 8 2325 2468 2300 -186 -73 86 ATOM 58 O PHE A 8 2.192 28.852 -32.882 1.00 20.71 O ANISOU 58 O PHE A 8 2595 2694 2578 -178 -83 78 ATOM 59 CB PHE A 8 4.097 26.347 -32.698 1.00 19.90 C ANISOU 59 CB PHE A 8 2467 2650 2445 -144 -4 46 ATOM 60 CG PHE A 8 5.026 25.341 -32.047 1.00 22.94 C ANISOU 60 CG PHE A 8 2844 3045 2825 -120 22 33 ATOM 61 CD1 PHE A 8 6.414 25.391 -32.291 1.00 23.40 C ANISOU 61 CD1 PHE A 8 2885 3146 2860 -130 23 42 ATOM 62 CD2 PHE A 8 4.530 24.418 -31.103 1.00 23.46 C ANISOU 62 CD2 PHE A 8 2920 3083 2910 -89 42 13 ATOM 63 CE1 PHE A 8 7.262 24.511 -31.632 1.00 27.87 C ANISOU 63 CE1 PHE A 8 3444 3720 3424 -105 45 28 ATOM 64 CE2 PHE A 8 5.398 23.557 -30.447 1.00 26.87 C ANISOU 64 CE2 PHE A 8 3347 3521 3340 -67 61 2 ATOM 65 CZ PHE A 8 6.758 23.599 -30.714 1.00 27.04 C ANISOU 65 CZ PHE A 8 3352 3580 3341 -73 62 7 ATOM 66 N PRO A 9 4.090 29.393 -34.035 1.00 19.39 N ANISOU 66 N PRO A 9 2404 2594 2370 -223 -94 112 ATOM 67 CA PRO A 9 3.422 30.144 -35.122 1.00 21.45 C ANISOU 67 CA PRO A 9 2667 2854 2629 -257 -127 130 ATOM 68 C PRO A 9 2.362 29.304 -35.860 1.00 23.50 C ANISOU 68 C PRO A 9 2925 3116 2888 -251 -102 107 ATOM 69 O PRO A 9 2.692 28.240 -36.381 1.00 18.95 O ANISOU 69 O PRO A 9 2338 2566 2297 -238 -66 86 ATOM 70 CB PRO A 9 4.578 30.554 -36.055 1.00 26.70 C ANISOU 70 CB PRO A 9 3313 3571 3262 -300 -144 162 ATOM 71 CG PRO A 9 5.811 30.553 -35.173 1.00 26.92 C ANISOU 71 CG PRO A 9 3331 3619 3280 -286 -127 163 ATOM 72 CD PRO A 9 5.545 29.409 -34.206 1.00 29.21 C ANISOU 72 CD PRO A 9 3628 3889 3584 -238 -84 124 ATOM 73 N SER A 10 1.105 29.766 -35.836 1.00 16.47 N ANISOU 73 N SER A 10 2047 2195 2017 -256 -125 108 ATOM 74 CA SER A 10 -0.058 29.014 -36.312 1.00 21.27 C ANISOU 74 CA SER A 10 2657 2792 2631 -245 -105 86 ATOM 75 C SER A 10 -0.312 29.065 -37.833 1.00 19.53 C ANISOU 75 C SER A 10 2428 2600 2392 -282 -116 97 ATOM 76 O SER A 10 -1.194 28.337 -38.280 1.00 19.13 O ANISOU 76 O SER A 10 2380 2541 2348 -276 -104 81 ATOM 77 CB SER A 10 -1.286 29.443 -35.482 1.00 17.87 C ANISOU 77 CB SER A 10 2244 2314 2234 -224 -120 76 ATOM 78 OG SER A 10 -1.560 30.827 -35.593 1.00 22.78 O ANISOU 78 OG SER A 10 2872 2918 2866 -248 -171 98 ATOM 79 N GLY A 11 0.442 29.883 -38.593 1.00 30.99 N ANISOU 79 N GLY A 11 3868 4087 3820 -321 -140 127 ATOM 80 CA GLY A 11 0.254 30.162 -40.028 1.00 26.35 C ANISOU 80 CA GLY A 11 3272 3527 3214 -360 -157 143 ATOM 81 C GLY A 11 0.129 28.921 -40.934 1.00 26.35 C ANISOU 81 C GLY A 11 3259 3560 3192 -353 -117 116 ATOM 82 O GLY A 11 -0.725 28.913 -41.821 1.00 20.58 O ANISOU 82 O GLY A 11 2531 2828 2461 -367 -122 113 ATOM 83 N LYS A 12 0.938 27.871 -40.699 1.00 18.26 N ANISOU 83 N LYS A 12 2223 2565 2151 -330 -80 94 ATOM 84 CA LYS A 12 0.885 26.599 -41.433 1.00 21.27 C ANISOU 84 CA LYS A 12 2592 2977 2512 -319 -48 63 ATOM 85 C LYS A 12 -0.415 25.801 -41.210 1.00 30.63 C ANISOU 85 C LYS A 12 3796 4114 3728 -290 -34 36 ATOM 86 O LYS A 12 -0.853 25.108 -42.129 1.00 25.47 O ANISOU 86 O LYS A 12 3140 3473 3065 -295 -26 20 ATOM 87 CB LYS A 12 2.102 25.725 -41.070 1.00 20.96 C ANISOU 87 CB LYS A 12 2536 2975 2452 -295 -17 42 ATOM 88 CG LYS A 12 3.434 26.208 -41.667 1.00 27.15 C ANISOU 88 CG LYS A 12 3293 3825 3197 -324 -25 65 ATOM 89 CD LYS A 12 4.597 25.283 -41.267 1.00 40.52 C ANISOU 89 CD LYS A 12 4973 5545 4879 -290 5 39 ATOM 90 CE LYS A 12 5.947 25.634 -41.906 1.00 52.09 C ANISOU 90 CE LYS A 12 6401 7094 6295 -315 6 52 ATOM 91 NZ LYS A 12 6.415 26.974 -41.521 1.00 67.84 N1+ ANISOU 91 NZ LYS A 12 8394 9094 8289 -344 -20 96 ATOM 92 N VAL A 13 -1.003 25.915 -40.009 1.00 25.17 N ANISOU 92 N VAL A 13 3121 3371 3070 -263 -33 32 ATOM 93 CA VAL A 13 -2.235 25.227 -39.626 1.00 24.53 C ANISOU 93 CA VAL A 13 3055 3249 3016 -240 -22 11 ATOM 94 C VAL A 13 -3.490 26.028 -40.020 1.00 15.82 C ANISOU 94 C VAL A 13 1961 2124 1928 -260 -50 25 ATOM 95 O VAL A 13 -4.479 25.400 -40.389 1.00 18.69 O ANISOU 95 O VAL A 13 2328 2473 2299 -257 -43 12 ATOM 96 CB VAL A 13 -2.259 24.926 -38.102 1.00 16.34 C ANISOU 96 CB VAL A 13 2028 2175 2004 -205 -9 2 ATOM 97 CG1 VAL A 13 -3.554 24.253 -37.596 1.00 20.96 C ANISOU 97 CG1 VAL A 13 2623 2726 2612 -186 1 -14 ATOM 98 CG2 VAL A 13 -1.051 24.053 -37.730 1.00 18.24 C ANISOU 98 CG2 VAL A 13 2261 2435 2233 -185 14 -12 ATOM 99 N GLU A 14 -3.417 27.374 -39.995 1.00 21.12 N ANISOU 99 N GLU A 14 2635 2785 2604 -280 -85 52 ATOM 100 CA GLU A 14 -4.472 28.299 -40.436 1.00 23.94 C ANISOU 100 CA GLU A 14 3000 3120 2976 -300 -118 66 ATOM 101 C GLU A 14 -4.949 28.056 -41.880 1.00 22.29 C ANISOU 101 C GLU A 14 2784 2938 2748 -328 -117 66 ATOM 102 O GLU A 14 -6.156 28.064 -42.117 1.00 17.00 O ANISOU 102 O GLU A 14 2120 2245 2092 -327 -122 60 ATOM 103 CB GLU A 14 -3.988 29.758 -40.299 1.00 25.55 C ANISOU 103 CB GLU A 14 3207 3316 3185 -325 -165 98 ATOM 104 CG GLU A 14 -3.902 30.280 -38.854 1.00 25.20 C ANISOU 104 CG GLU A 14 3173 3238 3164 -296 -174 94 ATOM 105 CD GLU A 14 -3.294 31.681 -38.800 1.00 23.31 C ANISOU 105 CD GLU A 14 2938 2991 2929 -320 -225 125 ATOM 106 OE1 GLU A 14 -3.846 32.575 -39.479 1.00 23.02 O ANISOU 106 OE1 GLU A 14 2905 2941 2899 -348 -269 145 ATOM 107 OE2 GLU A 14 -2.278 31.831 -38.089 1.00 19.24 O1- ANISOU 107 OE2 GLU A 14 2422 2478 2411 -311 -225 131 ATOM 108 N GLY A 15 -3.999 27.798 -42.799 1.00 22.53 N ANISOU 108 N GLY A 15 2798 3020 2742 -353 -112 75 ATOM 109 CA GLY A 15 -4.266 27.512 -44.212 1.00 25.97 C ANISOU 109 CA GLY A 15 3226 3486 3155 -378 -111 74 ATOM 110 C GLY A 15 -4.843 26.104 -44.450 1.00 20.83 C ANISOU 110 C GLY A 15 2578 2830 2508 -352 -79 38 ATOM 111 O GLY A 15 -5.200 25.796 -45.587 1.00 19.92 O ANISOU 111 O GLY A 15 2457 2736 2375 -370 -78 32 ATOM 112 N CYS A 16 -4.943 25.267 -43.401 1.00 18.12 N ANISOU 112 N CYS A 16 2243 2456 2186 -312 -55 14 ATOM 113 CA CYS A 16 -5.528 23.927 -43.435 1.00 20.80 C ANISOU 113 CA CYS A 16 2587 2782 2533 -289 -30 -16 ATOM 114 C CYS A 16 -6.941 23.898 -42.829 1.00 20.19 C ANISOU 114 C CYS A 16 2524 2654 2491 -276 -35 -18 ATOM 115 O CYS A 16 -7.620 22.891 -43.005 1.00 20.59 O ANISOU 115 O CYS A 16 2581 2691 2552 -260 -19 -38 ATOM 116 CB CYS A 16 -4.636 22.900 -42.708 1.00 20.56 C ANISOU 116 CB CYS A 16 2553 2758 2499 -256 -2 -40 ATOM 117 SG CYS A 16 -3.029 22.775 -43.531 1.00 23.56 S ANISOU 117 SG CYS A 16 2910 3206 2834 -263 9 -48 ATOM 118 N MET A 17 -7.384 24.959 -42.132 1.00 24.47 N ANISOU 118 N MET A 17 3074 3171 3055 -279 -57 0 ATOM 119 CA MET A 17 -8.696 24.976 -41.484 1.00 20.50 C ANISOU 119 CA MET A 17 2578 2627 2582 -261 -58 -5 ATOM 120 C MET A 17 -9.832 25.240 -42.476 1.00 16.51 C ANISOU 120 C MET A 17 2076 2116 2084 -282 -76 0 ATOM 121 O MET A 17 -9.792 26.221 -43.219 1.00 18.75 O ANISOU 121 O MET A 17 2357 2409 2358 -311 -104 19 ATOM 122 CB MET A 17 -8.725 25.975 -40.313 1.00 20.11 C ANISOU 122 CB MET A 17 2532 2555 2553 -247 -75 5 ATOM 123 CG MET A 17 -7.684 25.673 -39.225 1.00 22.29 C ANISOU 123 CG MET A 17 2808 2836 2826 -225 -57 1 ATOM 124 SD MET A 17 -7.555 23.943 -38.668 1.00 20.86 S ANISOU 124 SD MET A 17 2627 2652 2647 -197 -17 -23 ATOM 125 CE MET A 17 -9.231 23.641 -38.040 1.00 19.22 C ANISOU 125 CE MET A 17 2423 2414 2467 -184 -18 -26 ATOM 126 N VAL A 18 -10.825 24.343 -42.433 1.00 19.40 N ANISOU 126 N VAL A 18 2445 2464 2463 -270 -63 -14 ATOM 127 CA VAL A 18 -12.067 24.417 -43.190 1.00 23.22 C ANISOU 127 CA VAL A 18 2930 2937 2956 -286 -79 -10 ATOM 128 C VAL A 18 -13.249 24.209 -42.232 1.00 17.34 C ANISOU 128 C VAL A 18 2186 2163 2240 -265 -76 -14 ATOM 129 O VAL A 18 -13.082 23.689 -41.128 1.00 16.32 O ANISOU 129 O VAL A 18 2055 2026 2118 -240 -58 -21 ATOM 130 CB VAL A 18 -12.124 23.348 -44.323 1.00 17.86 C ANISOU 130 CB VAL A 18 2251 2274 2259 -301 -68 -22 ATOM 131 CG1 VAL A 18 -10.993 23.563 -45.340 1.00 22.05 C ANISOU 131 CG1 VAL A 18 2775 2846 2756 -324 -71 -18 ATOM 132 CG2 VAL A 18 -12.155 21.877 -43.861 1.00 23.32 C ANISOU 132 CG2 VAL A 18 2946 2957 2955 -276 -40 -43 ATOM 133 N GLN A 19 -14.429 24.638 -42.685 1.00 17.02 N ANISOU 133 N GLN A 19 2144 2111 2210 -277 -93 -10 ATOM 134 CA GLN A 19 -15.711 24.430 -42.029 1.00 26.25 C ANISOU 134 CA GLN A 19 3310 3262 3403 -261 -92 -13 ATOM 135 C GLN A 19 -16.329 23.158 -42.617 1.00 21.80 C ANISOU 135 C GLN A 19 2748 2697 2838 -269 -78 -20 ATOM 136 O GLN A 19 -16.288 22.993 -43.835 1.00 26.80 O ANISOU 136 O GLN A 19 3386 3337 3460 -292 -85 -19 ATOM 137 CB GLN A 19 -16.568 25.666 -42.352 1.00 27.13 C ANISOU 137 CB GLN A 19 3418 3362 3529 -270 -127 -4 ATOM 138 CG GLN A 19 -17.921 25.751 -41.626 1.00 30.46 C ANISOU 138 CG GLN A 19 3831 3773 3972 -253 -131 -10 ATOM 139 CD GLN A 19 -18.703 27.014 -42.010 1.00 34.59 C ANISOU 139 CD GLN A 19 4351 4283 4510 -256 -171 -5 ATOM 140 OE1 GLN A 19 -18.178 27.928 -42.644 1.00 43.90 O ANISOU 140 OE1 GLN A 19 5537 5458 5684 -278 -200 7 ATOM 141 NE2 GLN A 19 -19.974 27.077 -41.619 1.00 38.23 N ANISOU 141 NE2 GLN A 19 4799 4738 4990 -237 -177 -13 ATOM 142 N VAL A 20 -16.902 22.302 -41.760 1.00 27.63 N ANISOU 142 N VAL A 20 3483 3428 3588 -252 -60 -24 ATOM 143 CA VAL A 20 -17.637 21.109 -42.174 1.00 18.93 C ANISOU 143 CA VAL A 20 2384 2319 2490 -260 -52 -28 ATOM 144 C VAL A 20 -19.023 21.168 -41.520 1.00 25.29 C ANISOU 144 C VAL A 20 3177 3118 3314 -255 -57 -20 ATOM 145 O VAL A 20 -19.120 21.247 -40.295 1.00 22.69 O ANISOU 145 O VAL A 20 2837 2792 2992 -236 -50 -18 ATOM 146 CB VAL A 20 -16.936 19.786 -41.747 1.00 23.84 C ANISOU 146 CB VAL A 20 3012 2939 3108 -249 -32 -36 ATOM 147 CG1 VAL A 20 -17.722 18.524 -42.169 1.00 18.90 C ANISOU 147 CG1 VAL A 20 2392 2301 2489 -259 -32 -39 ATOM 148 CG2 VAL A 20 -15.500 19.703 -42.291 1.00 19.54 C ANISOU 148 CG2 VAL A 20 2474 2407 2542 -249 -27 -47 ATOM 149 N THR A 21 -20.061 21.126 -42.363 1.00 25.76 N ANISOU 149 N THR A 21 3237 3173 3379 -273 -69 -16 ATOM 150 CA THR A 21 -21.462 21.153 -41.968 1.00 28.18 C ANISOU 150 CA THR A 21 3528 3478 3701 -272 -75 -9 ATOM 151 C THR A 21 -22.144 19.881 -42.491 1.00 35.75 C ANISOU 151 C THR A 21 4492 4430 4664 -288 -71 -5 ATOM 152 O THR A 21 -21.933 19.496 -43.642 1.00 28.71 O ANISOU 152 O THR A 21 3614 3530 3764 -305 -76 -10 ATOM 153 CB THR A 21 -22.187 22.393 -42.561 1.00 34.23 C ANISOU 153 CB THR A 21 4289 4243 4475 -279 -101 -7 ATOM 154 OG1 THR A 21 -21.598 23.574 -42.048 1.00 32.58 O ANISOU 154 OG1 THR A 21 4076 4036 4266 -262 -112 -10 ATOM 155 CG2 THR A 21 -23.702 22.467 -42.284 1.00 35.79 C ANISOU 155 CG2 THR A 21 4469 4444 4688 -276 -107 -2 ATOM 156 N CYS A 22 -22.966 19.269 -41.628 1.00 35.75 N ANISOU 156 N CYS A 22 4477 4433 4672 -283 -64 4 ATOM 157 CA CYS A 22 -23.780 18.106 -41.949 1.00 24.56 C ANISOU 157 CA CYS A 22 3062 3008 3262 -300 -65 14 ATOM 158 C CYS A 22 -25.072 18.237 -41.137 1.00 43.34 C ANISOU 158 C CYS A 22 5415 5404 5650 -299 -67 28 ATOM 159 O CYS A 22 -25.024 18.164 -39.907 1.00 39.66 O ANISOU 159 O CYS A 22 4932 4956 5182 -283 -55 33 ATOM 160 CB CYS A 22 -23.020 16.784 -41.707 1.00 26.48 C ANISOU 160 CB CYS A 22 3318 3242 3504 -298 -54 14 ATOM 161 SG CYS A 22 -23.967 15.349 -42.284 1.00 54.57 S ANISOU 161 SG CYS A 22 6890 6775 7069 -321 -67 19 ATOM 162 N GLY A 23 -26.190 18.486 -41.840 1.00 43.87 N ANISOU 162 N GLY A 23 5475 5471 5724 -314 -82 33 ATOM 163 CA GLY A 23 -27.472 18.835 -41.229 1.00 36.29 C ANISOU 163 CA GLY A 23 4485 4533 4771 -310 -86 42 ATOM 164 C GLY A 23 -27.387 20.254 -40.645 1.00 50.69 C ANISOU 164 C GLY A 23 6292 6374 6594 -281 -87 29 ATOM 165 O GLY A 23 -26.871 21.163 -41.299 1.00 62.11 O ANISOU 165 O GLY A 23 7747 7808 8042 -276 -102 17 ATOM 166 N THR A 24 -27.900 20.431 -39.416 1.00 60.68 N ANISOU 166 N THR A 24 7532 7669 7855 -263 -76 31 ATOM 167 CA THR A 24 -27.795 21.679 -38.653 1.00 71.42 C ANISOU 167 CA THR A 24 8874 9047 9214 -230 -80 14 ATOM 168 C THR A 24 -26.435 21.838 -37.930 1.00 59.80 C ANISOU 168 C THR A 24 7415 7574 7735 -212 -67 5 ATOM 169 O THR A 24 -26.072 22.966 -37.593 1.00 61.06 O ANISOU 169 O THR A 24 7566 7738 7894 -185 -76 -12 ATOM 170 CB THR A 24 -28.964 21.824 -37.630 1.00 78.55 C ANISOU 170 CB THR A 24 9737 9994 10114 -217 -74 16 ATOM 171 OG1 THR A 24 -28.894 23.047 -36.919 1.00 69.96 O ANISOU 171 OG1 THR A 24 8630 8925 9025 -179 -82 -8 ATOM 172 CG2 THR A 24 -29.066 20.710 -36.571 1.00 86.10 C ANISOU 172 CG2 THR A 24 10683 10973 11057 -226 -51 36 ATOM 173 N THR A 25 -25.703 20.730 -37.707 1.00 40.45 N ANISOU 173 N THR A 25 4981 5112 5277 -224 -50 15 ATOM 174 CA THR A 25 -24.429 20.746 -36.991 1.00 39.03 C ANISOU 174 CA THR A 25 4810 4932 5089 -207 -38 9 ATOM 175 C THR A 25 -23.287 21.249 -37.892 1.00 24.50 C ANISOU 175 C THR A 25 2996 3064 3248 -209 -47 -2 ATOM 176 O THR A 25 -23.061 20.676 -38.957 1.00 30.92 O ANISOU 176 O THR A 25 3829 3858 4062 -230 -51 1 ATOM 177 CB THR A 25 -24.017 19.349 -36.458 1.00 42.61 C ANISOU 177 CB THR A 25 5269 5384 5537 -219 -20 25 ATOM 178 OG1 THR A 25 -25.101 18.776 -35.750 1.00 44.66 O ANISOU 178 OG1 THR A 25 5503 5671 5794 -228 -15 42 ATOM 179 CG2 THR A 25 -22.804 19.395 -35.501 1.00 44.59 C ANISOU 179 CG2 THR A 25 5525 5638 5779 -199 -7 18 ATOM 180 N THR A 26 -22.585 22.287 -37.416 1.00 23.62 N ANISOU 180 N THR A 26 2885 2955 3135 -187 -52 -14 ATOM 181 CA THR A 26 -21.360 22.807 -38.014 1.00 20.81 C ANISOU 181 CA THR A 26 2552 2580 2775 -191 -59 -19 ATOM 182 C THR A 26 -20.214 22.678 -37.002 1.00 23.60 C ANISOU 182 C THR A 26 2910 2938 3119 -176 -42 -22 ATOM 183 O THR A 26 -20.405 22.944 -35.815 1.00 28.11 O ANISOU 183 O THR A 26 3465 3525 3688 -154 -34 -25 ATOM 184 CB THR A 26 -21.501 24.307 -38.374 1.00 30.43 C ANISOU 184 CB THR A 26 3770 3792 4001 -185 -89 -28 ATOM 185 OG1 THR A 26 -22.488 24.434 -39.378 1.00 41.56 O ANISOU 185 OG1 THR A 26 5180 5192 5418 -205 -107 -23 ATOM 186 CG2 THR A 26 -20.220 24.984 -38.897 1.00 42.31 C ANISOU 186 CG2 THR A 26 5294 5284 5499 -191 -97 -28 ATOM 187 N LEU A 27 -19.035 22.310 -37.514 1.00 17.17 N ANISOU 187 N LEU A 27 2114 2112 2296 -186 -36 -22 ATOM 188 CA LEU A 27 -17.781 22.258 -36.773 1.00 23.77 C ANISOU 188 CA LEU A 27 2956 2951 3125 -170 -24 -25 ATOM 189 C LEU A 27 -16.603 22.451 -37.742 1.00 20.27 C ANISOU 189 C LEU A 27 2529 2500 2671 -183 -28 -27 ATOM 190 O LEU A 27 -16.818 22.784 -38.910 1.00 22.31 O ANISOU 190 O LEU A 27 2794 2755 2928 -202 -43 -26 ATOM 191 CB LEU A 27 -17.765 21.021 -35.830 1.00 22.20 C ANISOU 191 CB LEU A 27 2753 2758 2924 -165 -2 -19 ATOM 192 CG LEU A 27 -17.185 19.667 -36.311 1.00 26.84 C ANISOU 192 CG LEU A 27 3354 3334 3511 -179 8 -15 ATOM 193 CD1 LEU A 27 -17.673 18.542 -35.372 1.00 29.43 C ANISOU 193 CD1 LEU A 27 3671 3666 3844 -184 16 -1 ATOM 194 CD2 LEU A 27 -17.453 19.320 -37.786 1.00 18.72 C ANISOU 194 CD2 LEU A 27 2337 2293 2482 -199 -1 -19 ATOM 195 N ASN A 28 -15.376 22.284 -37.240 1.00 11.52 N ANISOU 195 N ASN A 28 1427 1394 1555 -173 -16 -29 ATOM 196 CA ASN A 28 -14.148 22.495 -38.010 1.00 16.88 C ANISOU 196 CA ASN A 28 2117 2076 2220 -184 -20 -31 ATOM 197 C ASN A 28 -13.634 21.169 -38.595 1.00 14.10 C ANISOU 197 C ASN A 28 1773 1725 1858 -190 -4 -38 ATOM 198 O ASN A 28 -13.952 20.095 -38.082 1.00 16.55 O ANISOU 198 O ASN A 28 2084 2029 2174 -181 10 -40 ATOM 199 CB ASN A 28 -13.069 23.127 -37.104 1.00 20.59 C ANISOU 199 CB ASN A 28 2587 2551 2685 -169 -20 -31 ATOM 200 CG ASN A 28 -13.533 24.409 -36.410 1.00 22.12 C ANISOU 200 CG ASN A 28 2774 2740 2889 -157 -41 -30 ATOM 201 OD1 ASN A 28 -13.654 25.457 -37.038 1.00 17.98 O ANISOU 201 OD1 ASN A 28 2252 2212 2368 -168 -68 -25 ATOM 202 ND2 ASN A 28 -13.793 24.324 -35.105 1.00 17.98 N ANISOU 202 ND2 ASN A 28 2242 2220 2371 -133 -31 -34 ATOM 203 N GLY A 29 -12.817 21.284 -39.649 1.00 21.65 N ANISOU 203 N GLY A 29 2734 2693 2799 -205 -10 -42 ATOM 204 CA GLY A 29 -12.083 20.177 -40.244 1.00 20.18 C ANISOU 204 CA GLY A 29 2553 2513 2600 -206 2 -55 ATOM 205 C GLY A 29 -10.672 20.658 -40.596 1.00 19.23 C ANISOU 205 C GLY A 29 2430 2418 2457 -209 4 -59 ATOM 206 O GLY A 29 -10.428 21.856 -40.753 1.00 23.71 O ANISOU 206 O GLY A 29 2995 2996 3018 -220 -10 -46 ATOM 207 N LEU A 30 -9.753 19.694 -40.749 1.00 11.79 N ANISOU 207 N LEU A 30 1490 1485 1504 -198 17 -76 ATOM 208 CA LEU A 30 -8.365 19.894 -41.148 1.00 19.36 C ANISOU 208 CA LEU A 30 2442 2475 2438 -198 21 -83 ATOM 209 C LEU A 30 -8.183 19.314 -42.557 1.00 19.48 C ANISOU 209 C LEU A 30 2454 2516 2431 -210 20 -101 ATOM 210 O LEU A 30 -8.329 18.109 -42.734 1.00 22.66 O ANISOU 210 O LEU A 30 2863 2909 2838 -198 25 -122 ATOM 211 CB LEU A 30 -7.442 19.189 -40.126 1.00 17.94 C ANISOU 211 CB LEU A 30 2263 2292 2262 -172 37 -94 ATOM 212 CG LEU A 30 -5.943 19.519 -40.309 1.00 20.32 C ANISOU 212 CG LEU A 30 2554 2628 2538 -168 43 -100 ATOM 213 CD1 LEU A 30 -5.618 20.948 -39.850 1.00 18.23 C ANISOU 213 CD1 LEU A 30 2285 2370 2270 -177 36 -76 ATOM 214 CD2 LEU A 30 -5.036 18.499 -39.603 1.00 26.50 C ANISOU 214 CD2 LEU A 30 3338 3404 3326 -140 56 -118 ATOM 215 N TRP A 31 -7.861 20.182 -43.522 1.00 17.25 N ANISOU 215 N TRP A 31 2162 2270 2123 -233 12 -92 ATOM 216 CA TRP A 31 -7.692 19.868 -44.936 1.00 12.37 C ANISOU 216 CA TRP A 31 1537 1686 1477 -250 9 -105 ATOM 217 C TRP A 31 -6.195 19.718 -45.250 1.00 20.01 C ANISOU 217 C TRP A 31 2488 2704 2410 -244 19 -120 ATOM 218 O TRP A 31 -5.468 20.710 -45.231 1.00 20.48 O ANISOU 218 O TRP A 31 2536 2794 2452 -261 14 -100 ATOM 219 CB TRP A 31 -8.364 21.007 -45.732 1.00 14.92 C ANISOU 219 CB TRP A 31 1858 2019 1793 -286 -12 -79 ATOM 220 CG TRP A 31 -8.429 20.917 -47.229 1.00 22.50 C ANISOU 220 CG TRP A 31 2809 3016 2723 -308 -18 -88 ATOM 221 CD1 TRP A 31 -8.496 19.786 -47.972 1.00 24.34 C ANISOU 221 CD1 TRP A 31 3042 3265 2943 -297 -8 -120 ATOM 222 CD2 TRP A 31 -8.523 22.024 -48.177 1.00 23.96 C ANISOU 222 CD2 TRP A 31 2986 3230 2888 -348 -38 -62 ATOM 223 NE1 TRP A 31 -8.588 20.120 -49.309 1.00 24.90 N ANISOU 223 NE1 TRP A 31 3102 3376 2981 -327 -18 -119 ATOM 224 CE2 TRP A 31 -8.606 21.486 -49.498 1.00 18.22 C ANISOU 224 CE2 TRP A 31 2252 2541 2131 -361 -37 -80 ATOM 225 CE3 TRP A 31 -8.514 23.435 -48.058 1.00 31.10 C ANISOU 225 CE3 TRP A 31 3889 4131 3796 -375 -63 -25 ATOM 226 CZ2 TRP A 31 -8.670 22.306 -50.639 1.00 21.87 C ANISOU 226 CZ2 TRP A 31 2703 3041 2565 -402 -55 -60 ATOM 227 CZ3 TRP A 31 -8.562 24.265 -49.197 1.00 33.76 C ANISOU 227 CZ3 TRP A 31 4218 4500 4110 -416 -85 -4 ATOM 228 CH2 TRP A 31 -8.638 23.704 -50.487 1.00 30.19 C ANISOU 228 CH2 TRP A 31 3756 4089 3625 -431 -80 -19 ATOM 229 N LEU A 32 -5.769 18.474 -45.514 1.00 18.33 N ANISOU 229 N LEU A 32 2274 2501 2189 -221 30 -156 ATOM 230 CA LEU A 32 -4.401 18.111 -45.889 1.00 20.76 C ANISOU 230 CA LEU A 32 2563 2861 2464 -208 41 -180 ATOM 231 C LEU A 32 -4.493 17.253 -47.148 1.00 19.67 C ANISOU 231 C LEU A 32 2419 2753 2302 -205 40 -216 ATOM 232 O LEU A 32 -5.229 16.264 -47.142 1.00 17.96 O ANISOU 232 O LEU A 32 2217 2498 2107 -188 36 -238 ATOM 233 CB LEU A 32 -3.732 17.285 -44.772 1.00 19.44 C ANISOU 233 CB LEU A 32 2399 2671 2314 -170 53 -198 ATOM 234 CG LEU A 32 -3.582 17.974 -43.402 1.00 23.44 C ANISOU 234 CG LEU A 32 2913 3147 2846 -167 55 -168 ATOM 235 CD1 LEU A 32 -3.223 16.935 -42.326 1.00 24.13 C ANISOU 235 CD1 LEU A 32 3008 3206 2954 -130 64 -187 ATOM 236 CD2 LEU A 32 -2.585 19.148 -43.424 1.00 22.71 C ANISOU 236 CD2 LEU A 32 2804 3095 2728 -188 54 -142 ATOM 237 N ASP A 33 -3.789 17.669 -48.216 1.00 25.44 N ANISOU 237 N ASP A 33 3125 3554 2987 -221 42 -221 ATOM 238 CA ASP A 33 -3.961 17.146 -49.577 1.00 26.35 C ANISOU 238 CA ASP A 33 3230 3711 3071 -224 39 -252 ATOM 239 C ASP A 33 -5.442 17.266 -49.988 1.00 23.96 C ANISOU 239 C ASP A 33 2948 3364 2792 -245 25 -238 ATOM 240 O ASP A 33 -6.029 18.323 -49.755 1.00 23.48 O ANISOU 240 O ASP A 33 2893 3287 2743 -277 15 -195 ATOM 241 CB ASP A 33 -3.344 15.735 -49.811 1.00 21.40 C ANISOU 241 CB ASP A 33 2600 3091 2441 -178 46 -309 ATOM 242 CG ASP A 33 -1.868 15.608 -49.421 1.00 27.99 C ANISOU 242 CG ASP A 33 3409 3978 3249 -158 60 -324 ATOM 243 OD1 ASP A 33 -1.143 16.620 -49.532 1.00 27.33 O ANISOU 243 OD1 ASP A 33 3304 3945 3134 -187 64 -294 ATOM 244 OD2 ASP A 33 -1.461 14.467 -49.113 1.00 36.80 O1- ANISOU 244 OD2 ASP A 33 4526 5082 4374 -114 63 -366 ATOM 245 N ASP A 34 -6.030 16.198 -50.542 1.00 21.58 N ANISOU 245 N ASP A 34 2659 3039 2501 -227 20 -271 ATOM 246 CA ASP A 34 -7.426 16.147 -50.971 1.00 28.28 C ANISOU 246 CA ASP A 34 3525 3850 3369 -248 6 -257 ATOM 247 C ASP A 34 -8.347 15.484 -49.920 1.00 26.63 C ANISOU 247 C ASP A 34 3342 3564 3213 -228 1 -256 ATOM 248 O ASP A 34 -9.424 15.033 -50.301 1.00 21.69 O ANISOU 248 O ASP A 34 2732 2907 2604 -231 -11 -263 ATOM 249 CB ASP A 34 -7.568 15.493 -52.371 1.00 19.06 C ANISOU 249 CB ASP A 34 2352 2718 2172 -253 -2 -290 ATOM 250 CG ASP A 34 -7.020 14.067 -52.531 1.00 29.74 C ANISOU 250 CG ASP A 34 3706 4070 3523 -208 -2 -348 ATOM 251 OD1 ASP A 34 -6.421 13.527 -51.574 1.00 24.77 O ANISOU 251 OD1 ASP A 34 3079 3424 2910 -174 5 -365 ATOM 252 OD2 ASP A 34 -7.231 13.515 -53.632 1.00 28.70 O1- ANISOU 252 OD2 ASP A 34 3575 3954 3374 -206 -12 -380 ATOM 253 N VAL A 35 -7.940 15.425 -48.637 1.00 16.12 N ANISOU 253 N VAL A 35 2015 2205 1905 -210 9 -245 ATOM 254 CA VAL A 35 -8.721 14.808 -47.559 1.00 21.24 C ANISOU 254 CA VAL A 35 2684 2788 2598 -195 5 -238 ATOM 255 C VAL A 35 -8.962 15.831 -46.437 1.00 18.70 C ANISOU 255 C VAL A 35 2363 2446 2295 -208 10 -196 ATOM 256 O VAL A 35 -8.017 16.479 -45.987 1.00 18.67 O ANISOU 256 O VAL A 35 2349 2467 2278 -209 18 -184 ATOM 257 CB VAL A 35 -7.999 13.574 -46.940 1.00 24.41 C ANISOU 257 CB VAL A 35 3090 3172 3012 -157 7 -269 ATOM 258 CG1 VAL A 35 -8.791 12.900 -45.793 1.00 23.92 C ANISOU 258 CG1 VAL A 35 3048 3046 2993 -149 -2 -257 ATOM 259 CG2 VAL A 35 -7.667 12.519 -48.012 1.00 24.37 C ANISOU 259 CG2 VAL A 35 3082 3190 2986 -138 -1 -318 ATOM 260 N VAL A 36 -10.221 15.912 -45.985 1.00 20.13 N ANISOU 260 N VAL A 36 2557 2584 2507 -215 2 -177 ATOM 261 CA VAL A 36 -10.649 16.719 -44.848 1.00 22.13 C ANISOU 261 CA VAL A 36 2812 2816 2782 -219 5 -144 ATOM 262 C VAL A 36 -10.988 15.785 -43.674 1.00 16.74 C ANISOU 262 C VAL A 36 2138 2093 2128 -198 8 -146 ATOM 263 O VAL A 36 -11.923 14.990 -43.765 1.00 21.11 O ANISOU 263 O VAL A 36 2702 2620 2698 -197 -1 -153 ATOM 264 CB VAL A 36 -11.878 17.599 -45.201 1.00 19.91 C ANISOU 264 CB VAL A 36 2531 2526 2510 -246 -8 -120 ATOM 265 CG1 VAL A 36 -12.518 18.317 -43.992 1.00 17.96 C ANISOU 265 CG1 VAL A 36 2283 2256 2286 -242 -8 -95 ATOM 266 CG2 VAL A 36 -11.497 18.627 -46.279 1.00 18.55 C ANISOU 266 CG2 VAL A 36 2349 2392 2308 -271 -15 -113 ATOM 267 N TYR A 37 -10.205 15.916 -42.596 1.00 20.53 N ANISOU 267 N TYR A 37 2616 2571 2614 -184 18 -137 ATOM 268 CA TYR A 37 -10.343 15.180 -41.342 1.00 18.11 C ANISOU 268 CA TYR A 37 2316 2232 2332 -167 20 -133 ATOM 269 C TYR A 37 -11.210 16.005 -40.382 1.00 17.27 C ANISOU 269 C TYR A 37 2207 2115 2242 -174 22 -103 ATOM 270 O TYR A 37 -10.926 17.187 -40.208 1.00 22.54 O ANISOU 270 O TYR A 37 2865 2798 2899 -177 25 -92 ATOM 271 CB TYR A 37 -8.942 14.952 -40.732 1.00 14.42 C ANISOU 271 CB TYR A 37 1848 1773 1860 -143 29 -146 ATOM 272 CG TYR A 37 -7.976 14.176 -41.614 1.00 23.07 C ANISOU 272 CG TYR A 37 2940 2889 2935 -129 28 -182 ATOM 273 CD1 TYR A 37 -7.227 14.841 -42.610 1.00 22.17 C ANISOU 273 CD1 TYR A 37 2813 2822 2789 -138 33 -191 ATOM 274 CD2 TYR A 37 -7.817 12.786 -41.441 1.00 22.51 C ANISOU 274 CD2 TYR A 37 2880 2796 2879 -106 19 -206 ATOM 275 CE1 TYR A 37 -6.345 14.126 -43.438 1.00 20.49 C ANISOU 275 CE1 TYR A 37 2593 2639 2553 -123 33 -226 ATOM 276 CE2 TYR A 37 -6.922 12.071 -42.260 1.00 28.02 C ANISOU 276 CE2 TYR A 37 3572 3516 3558 -87 16 -246 ATOM 277 CZ TYR A 37 -6.187 12.740 -43.259 1.00 19.48 C ANISOU 277 CZ TYR A 37 2474 2488 2440 -94 25 -257 ATOM 278 OH TYR A 37 -5.314 12.048 -44.047 1.00 26.42 O ANISOU 278 OH TYR A 37 3344 3400 3296 -73 23 -300 ATOM 279 N CYS A 38 -12.220 15.389 -39.752 1.00 18.89 N ANISOU 279 N CYS A 38 2416 2295 2468 -177 17 -91 ATOM 280 CA CYS A 38 -13.084 16.046 -38.762 1.00 22.30 C ANISOU 280 CA CYS A 38 2838 2724 2910 -179 21 -68 ATOM 281 C CYS A 38 -13.618 15.003 -37.756 1.00 26.51 C ANISOU 281 C CYS A 38 3374 3238 3462 -178 19 -55 ATOM 282 O CYS A 38 -13.556 13.813 -38.059 1.00 23.10 O ANISOU 282 O CYS A 38 2952 2786 3038 -179 9 -62 ATOM 283 CB CYS A 38 -14.189 16.907 -39.433 1.00 20.50 C ANISOU 283 CB CYS A 38 2605 2503 2683 -197 12 -58 ATOM 284 SG CYS A 38 -15.556 15.926 -40.125 1.00 23.89 S ANISOU 284 SG CYS A 38 3040 2914 3125 -215 0 -56 ATOM 285 N PRO A 39 -14.175 15.435 -36.599 1.00 21.33 N ANISOU 285 N PRO A 39 2706 2588 2812 -176 25 -35 ATOM 286 CA PRO A 39 -14.880 14.522 -35.675 1.00 16.06 C ANISOU 286 CA PRO A 39 2036 1910 2157 -181 22 -17 ATOM 287 C PRO A 39 -16.125 13.898 -36.326 1.00 20.18 C ANISOU 287 C PRO A 39 2559 2420 2690 -202 8 -8 ATOM 288 O PRO A 39 -16.907 14.628 -36.942 1.00 28.43 O ANISOU 288 O PRO A 39 3597 3473 3731 -212 5 -8 ATOM 289 CB PRO A 39 -15.249 15.414 -34.473 1.00 21.77 C ANISOU 289 CB PRO A 39 2740 2654 2876 -174 33 -2 ATOM 290 CG PRO A 39 -14.311 16.605 -34.565 1.00 16.94 C ANISOU 290 CG PRO A 39 2128 2055 2252 -159 40 -16 ATOM 291 CD PRO A 39 -14.158 16.797 -36.068 1.00 17.10 C ANISOU 291 CD PRO A 39 2158 2071 2268 -169 31 -30 ATOM 292 N ARG A 40 -16.276 12.568 -36.192 1.00 18.60 N ANISOU 292 N ARG A 40 2368 2198 2502 -210 -5 1 ATOM 293 CA ARG A 40 -17.410 11.820 -36.744 1.00 22.36 C ANISOU 293 CA ARG A 40 2846 2659 2990 -232 -23 12 ATOM 294 C ARG A 40 -18.767 12.224 -36.149 1.00 21.47 C ANISOU 294 C ARG A 40 2712 2569 2878 -248 -19 40 ATOM 295 O ARG A 40 -19.768 12.036 -36.833 1.00 24.59 O ANISOU 295 O ARG A 40 3103 2962 3277 -266 -30 47 ATOM 296 CB ARG A 40 -17.183 10.293 -36.640 1.00 26.60 C ANISOU 296 CB ARG A 40 3400 3163 3544 -239 -46 16 ATOM 297 CG ARG A 40 -17.441 9.677 -35.248 1.00 28.94 C ANISOU 297 CG ARG A 40 3689 3459 3847 -244 -48 46 ATOM 298 CD ARG A 40 -17.309 8.158 -35.237 1.00 18.83 C ANISOU 298 CD ARG A 40 2427 2138 2589 -258 -83 56 ATOM 299 NE ARG A 40 -17.319 7.631 -33.868 1.00 19.31 N ANISOU 299 NE ARG A 40 2482 2198 2656 -268 -90 88 ATOM 300 CZ ARG A 40 -17.396 6.336 -33.525 1.00 24.25 C ANISOU 300 CZ ARG A 40 3120 2789 3302 -286 -125 108 ATOM 301 NH1 ARG A 40 -17.479 5.380 -34.461 1.00 26.14 N ANISOU 301 NH1 ARG A 40 3383 2990 3561 -291 -158 94 ATOM 302 NH2 ARG A 40 -17.385 6.004 -32.229 1.00 24.82 N1+ ANISOU 302 NH2 ARG A 40 3184 2868 3377 -299 -131 143 ATOM 303 N HIS A 41 -18.782 12.782 -34.919 1.00 19.20 N ANISOU 303 N HIS A 41 2406 2307 2582 -239 -4 53 ATOM 304 CA HIS A 41 -19.986 13.255 -34.233 1.00 25.48 C ANISOU 304 CA HIS A 41 3175 3133 3374 -251 -1 75 ATOM 305 C HIS A 41 -20.775 14.348 -34.975 1.00 19.14 C ANISOU 305 C HIS A 41 2361 2343 2566 -248 1 63 ATOM 306 O HIS A 41 -21.924 14.578 -34.609 1.00 23.61 O ANISOU 306 O HIS A 41 2905 2935 3132 -257 1 77 ATOM 307 CB HIS A 41 -19.702 13.587 -32.754 1.00 23.31 C ANISOU 307 CB HIS A 41 2881 2888 3088 -240 14 88 ATOM 308 CG HIS A 41 -18.897 14.826 -32.451 1.00 19.51 C ANISOU 308 CG HIS A 41 2396 2422 2596 -211 30 66 ATOM 309 ND1 HIS A 41 -19.323 16.114 -32.796 1.00 23.40 N ANISOU 309 ND1 HIS A 41 2877 2930 3082 -200 33 51 ATOM 310 CD2 HIS A 41 -17.706 14.927 -31.764 1.00 22.30 C ANISOU 310 CD2 HIS A 41 2754 2775 2943 -193 40 60 ATOM 311 CE1 HIS A 41 -18.382 16.922 -32.338 1.00 22.79 C ANISOU 311 CE1 HIS A 41 2800 2860 2997 -176 41 36 ATOM 312 NE2 HIS A 41 -17.396 16.271 -31.730 1.00 21.37 N ANISOU 312 NE2 HIS A 41 2630 2673 2817 -172 47 42 ATOM 313 N VAL A 42 -20.194 14.949 -36.031 1.00 22.29 N ANISOU 313 N VAL A 42 2776 2728 2963 -240 0 39 ATOM 314 CA VAL A 42 -20.862 15.861 -36.962 1.00 26.59 C ANISOU 314 CA VAL A 42 3314 3280 3507 -244 -6 31 ATOM 315 C VAL A 42 -22.118 15.274 -37.650 1.00 29.50 C ANISOU 315 C VAL A 42 3680 3642 3885 -268 -20 45 ATOM 316 O VAL A 42 -22.961 16.062 -38.071 1.00 24.90 O ANISOU 316 O VAL A 42 3086 3071 3304 -273 -25 45 ATOM 317 CB VAL A 42 -19.875 16.373 -38.054 1.00 28.83 C ANISOU 317 CB VAL A 42 3617 3551 3785 -239 -8 9 ATOM 318 CG1 VAL A 42 -19.532 15.345 -39.149 1.00 21.31 C ANISOU 318 CG1 VAL A 42 2685 2575 2836 -252 -19 0 ATOM 319 CG2 VAL A 42 -20.325 17.703 -38.695 1.00 29.59 C ANISOU 319 CG2 VAL A 42 3704 3658 3880 -240 -16 4 ATOM 320 N ILE A 43 -22.234 13.932 -37.731 1.00 29.07 N ANISOU 320 N ILE A 43 3638 3568 3840 -284 -30 57 ATOM 321 CA ILE A 43 -23.398 13.225 -38.282 1.00 34.71 C ANISOU 321 CA ILE A 43 4351 4273 4563 -310 -47 71 ATOM 322 C ILE A 43 -24.476 12.896 -37.219 1.00 31.74 C ANISOU 322 C ILE A 43 3950 3922 4189 -325 -47 104 ATOM 323 O ILE A 43 -25.539 12.410 -37.605 1.00 34.03 O ANISOU 323 O ILE A 43 4235 4208 4487 -350 -63 123 ATOM 324 CB ILE A 43 -22.997 11.915 -39.031 1.00 26.64 C ANISOU 324 CB ILE A 43 3358 3213 3553 -321 -66 64 ATOM 325 CG1 ILE A 43 -22.618 10.718 -38.117 1.00 32.34 C ANISOU 325 CG1 ILE A 43 4088 3919 4283 -323 -74 78 ATOM 326 CG2 ILE A 43 -21.932 12.225 -40.102 1.00 23.24 C ANISOU 326 CG2 ILE A 43 2947 2770 3114 -306 -64 30 ATOM 327 CD1 ILE A 43 -22.099 9.487 -38.871 1.00 34.58 C ANISOU 327 CD1 ILE A 43 4399 4158 4580 -332 -102 68 ATOM 328 N CYS A 44 -24.219 13.185 -35.927 1.00 38.89 N ANISOU 328 N CYS A 44 4835 4858 5084 -311 -31 111 ATOM 329 CA CYS A 44 -25.219 13.105 -34.855 1.00 35.26 C ANISOU 329 CA CYS A 44 4342 4437 4618 -324 -28 140 ATOM 330 C CYS A 44 -26.189 14.288 -34.950 1.00 36.52 C ANISOU 330 C CYS A 44 4473 4632 4771 -318 -23 135 ATOM 331 O CYS A 44 -25.755 15.421 -35.165 1.00 43.68 O ANISOU 331 O CYS A 44 5383 5536 5677 -296 -19 108 ATOM 332 CB CYS A 44 -24.611 13.147 -33.436 1.00 42.15 C ANISOU 332 CB CYS A 44 5201 5336 5478 -310 -12 147 ATOM 333 SG CYS A 44 -23.666 11.650 -33.091 1.00 52.07 S ANISOU 333 SG CYS A 44 6478 6564 6742 -325 -23 167 ATOM 334 N THR A 45 -27.471 14.002 -34.702 1.00 34.90 N ANISOU 334 N THR A 45 4238 4462 4561 -337 -26 162 ATOM 335 CA THR A 45 -28.484 15.003 -34.376 1.00 45.23 C ANISOU 335 CA THR A 45 5509 5817 5859 -325 -19 157 ATOM 336 C THR A 45 -28.661 15.062 -32.841 1.00 47.05 C ANISOU 336 C THR A 45 5702 6106 6069 -318 -4 171 ATOM 337 O THR A 45 -28.061 14.266 -32.112 1.00 40.95 O ANISOU 337 O THR A 45 4932 5335 5290 -330 -1 192 ATOM 338 CB THR A 45 -29.843 14.643 -35.039 1.00 43.87 C ANISOU 338 CB THR A 45 5324 5650 5694 -353 -34 175 ATOM 339 OG1 THR A 45 -30.466 13.513 -34.456 1.00 52.10 O ANISOU 339 OG1 THR A 45 6364 6694 6738 -390 -45 215 ATOM 340 CG2 THR A 45 -29.739 14.446 -36.560 1.00 50.21 C ANISOU 340 CG2 THR A 45 6159 6405 6515 -356 -48 156 ATOM 341 N SER A 46 -29.513 15.993 -32.378 1.00 56.71 N ANISOU 341 N SER A 46 6887 7378 7280 -298 2 158 ATOM 342 CA SER A 46 -29.942 16.110 -30.979 1.00 63.97 C ANISOU 342 CA SER A 46 7764 8368 8175 -289 17 167 ATOM 343 C SER A 46 -30.670 14.865 -30.426 1.00 60.82 C ANISOU 343 C SER A 46 7343 8001 7766 -332 13 216 ATOM 344 O SER A 46 -30.694 14.681 -29.208 1.00 68.84 O ANISOU 344 O SER A 46 8329 9071 8758 -336 25 234 ATOM 345 CB SER A 46 -30.782 17.395 -30.824 1.00 80.22 C ANISOU 345 CB SER A 46 9784 10474 10223 -256 20 138 ATOM 346 OG SER A 46 -32.010 17.322 -31.524 1.00 88.08 O ANISOU 346 OG SER A 46 10761 11481 11224 -275 9 149 ATOM 347 N GLU A 47 -31.217 14.034 -31.330 1.00 52.97 N ANISOU 347 N GLU A 47 6363 6975 6788 -368 -5 239 ATOM 348 CA GLU A 47 -31.914 12.783 -31.038 1.00 61.43 C ANISOU 348 CA GLU A 47 7419 8067 7854 -415 -17 291 ATOM 349 C GLU A 47 -30.946 11.593 -30.826 1.00 57.40 C ANISOU 349 C GLU A 47 6946 7507 7356 -440 -31 315 ATOM 350 O GLU A 47 -31.379 10.575 -30.288 1.00 56.08 O ANISOU 350 O GLU A 47 6772 7347 7189 -483 -48 361 ATOM 351 CB GLU A 47 -32.888 12.456 -32.204 1.00 62.74 C ANISOU 351 CB GLU A 47 7582 8221 8034 -443 -36 306 ATOM 352 CG GLU A 47 -33.609 13.637 -32.909 1.00 66.76 C ANISOU 352 CG GLU A 47 8085 8732 8550 -415 -34 268 ATOM 353 CD GLU A 47 -34.503 14.524 -32.034 1.00 81.02 C ANISOU 353 CD GLU A 47 9831 10620 10331 -396 -21 261 ATOM 354 OE1 GLU A 47 -34.697 14.193 -30.843 1.00 83.49 O ANISOU 354 OE1 GLU A 47 10106 10998 10618 -403 -9 283 ATOM 355 OE2 GLU A 47 -34.984 15.536 -32.589 1.00 83.63 O1- ANISOU 355 OE2 GLU A 47 10153 10954 10669 -373 -24 232 ATOM 356 N ASP A 48 -29.684 11.722 -31.278 1.00 63.79 N ANISOU 356 N ASP A 48 7794 8268 8177 -413 -25 285 ATOM 357 CA ASP A 48 -28.692 10.638 -31.356 1.00 58.36 C ANISOU 357 CA ASP A 48 7148 7520 7507 -430 -43 297 ATOM 358 C ASP A 48 -27.621 10.652 -30.258 1.00 40.67 C ANISOU 358 C ASP A 48 4913 5282 5258 -415 -32 296 ATOM 359 O ASP A 48 -26.942 9.635 -30.120 1.00 47.62 O ANISOU 359 O ASP A 48 5824 6115 6153 -429 -49 308 ATOM 360 CB ASP A 48 -27.962 10.617 -32.722 1.00 67.42 C ANISOU 360 CB ASP A 48 8339 8599 8677 -414 -52 262 ATOM 361 CG ASP A 48 -28.882 10.406 -33.919 1.00 68.75 C ANISOU 361 CG ASP A 48 8519 8741 8863 -442 -76 272 ATOM 362 OD1 ASP A 48 -29.529 9.335 -33.951 1.00 59.84 O ANISOU 362 OD1 ASP A 48 7393 7600 7742 -480 -101 310 ATOM 363 OD2 ASP A 48 -28.852 11.271 -34.822 1.00 74.49 O1- ANISOU 363 OD2 ASP A 48 9252 9457 9594 -427 -72 244 ATOM 364 N MET A 49 -27.440 11.773 -29.538 1.00 46.14 N ANISOU 364 N MET A 49 5577 6025 5927 -387 -6 281 ATOM 365 CA MET A 49 -26.262 12.030 -28.696 1.00 37.64 C ANISOU 365 CA MET A 49 4515 4940 4846 -362 7 266 ATOM 366 C MET A 49 -25.955 10.993 -27.598 1.00 28.93 C ANISOU 366 C MET A 49 3406 3850 3735 -390 -1 307 ATOM 367 O MET A 49 -24.777 10.778 -27.325 1.00 34.15 O ANISOU 367 O MET A 49 4092 4480 4402 -380 -2 301 ATOM 368 CB MET A 49 -26.328 13.445 -28.089 1.00 60.39 C ANISOU 368 CB MET A 49 7369 7869 7706 -322 32 233 ATOM 369 CG MET A 49 -26.454 14.562 -29.139 1.00 67.51 C ANISOU 369 CG MET A 49 8277 8755 8617 -295 34 194 ATOM 370 SD MET A 49 -26.026 16.215 -28.528 1.00 70.01 S ANISOU 370 SD MET A 49 8577 9105 8918 -242 52 150 ATOM 371 CE MET A 49 -27.544 16.658 -27.646 1.00 80.92 C ANISOU 371 CE MET A 49 9909 10551 10287 -233 53 143 ATOM 372 N LEU A 50 -26.988 10.372 -27.001 1.00 29.31 N ANISOU 372 N LEU A 50 3420 3948 3768 -428 -9 352 ATOM 373 CA LEU A 50 -26.856 9.437 -25.876 1.00 35.44 C ANISOU 373 CA LEU A 50 4186 4745 4534 -459 -19 397 ATOM 374 C LEU A 50 -26.108 8.133 -26.215 1.00 35.70 C ANISOU 374 C LEU A 50 4266 4701 4599 -484 -54 417 ATOM 375 O LEU A 50 -25.265 7.706 -25.424 1.00 34.99 O ANISOU 375 O LEU A 50 4190 4595 4512 -486 -60 429 ATOM 376 CB LEU A 50 -28.252 9.155 -25.262 1.00 44.51 C ANISOU 376 CB LEU A 50 5284 5971 5657 -498 -23 444 ATOM 377 CG LEU A 50 -28.369 9.518 -23.765 1.00 71.91 C ANISOU 377 CG LEU A 50 8706 9533 9085 -496 0 458 ATOM 378 CD1 LEU A 50 -28.159 11.022 -23.494 1.00 83.43 C ANISOU 378 CD1 LEU A 50 10153 11018 10527 -436 34 401 ATOM 379 CD2 LEU A 50 -29.707 9.031 -23.184 1.00 72.91 C ANISOU 379 CD2 LEU A 50 8776 9745 9183 -530 -1 497 ATOM 380 N ASN A 51 -26.419 7.535 -27.378 1.00 36.15 N ANISOU 380 N ASN A 51 4346 4706 4681 -502 -80 420 ATOM 381 CA ASN A 51 -25.810 6.287 -27.839 1.00 46.18 C ANISOU 381 CA ASN A 51 5662 5900 5985 -520 -118 431 ATOM 382 C ASN A 51 -25.931 6.182 -29.378 1.00 46.80 C ANISOU 382 C ASN A 51 5771 5921 6089 -512 -133 401 ATOM 383 O ASN A 51 -26.737 5.388 -29.865 1.00 51.38 O ANISOU 383 O ASN A 51 6360 6477 6686 -547 -166 427 ATOM 384 CB ASN A 51 -26.389 5.059 -27.078 1.00 59.59 C ANISOU 384 CB ASN A 51 7349 7607 7685 -577 -155 497 ATOM 385 CG ASN A 51 -25.381 3.912 -26.921 1.00 58.09 C ANISOU 385 CG ASN A 51 7193 7362 7517 -587 -187 512 ATOM 386 OD1 ASN A 51 -24.587 3.636 -27.818 1.00 68.94 O ANISOU 386 OD1 ASN A 51 8549 8766 8878 -616 -197 556 ATOM 387 ND2 ASN A 51 -25.418 3.225 -25.777 1.00 49.79 N ANISOU 387 ND2 ASN A 51 6188 6233 6497 -562 -204 473 ATOM 388 N PRO A 52 -25.161 7.009 -30.125 1.00 46.77 N ANISOU 388 N PRO A 52 5788 5895 6089 -468 -111 347 ATOM 389 CA PRO A 52 -25.228 7.038 -31.596 1.00 42.13 C ANISOU 389 CA PRO A 52 5227 5261 5521 -461 -123 318 ATOM 390 C PRO A 52 -24.640 5.770 -32.240 1.00 29.65 C ANISOU 390 C PRO A 52 3686 3609 3969 -473 -164 319 ATOM 391 O PRO A 52 -23.513 5.391 -31.921 1.00 35.71 O ANISOU 391 O PRO A 52 4474 4350 4746 -465 -175 317 ATOM 392 CB PRO A 52 -24.423 8.294 -31.969 1.00 40.68 C ANISOU 392 CB PRO A 52 5050 5078 5329 -414 -91 266 ATOM 393 CG PRO A 52 -23.428 8.471 -30.836 1.00 45.80 C ANISOU 393 CG PRO A 52 5693 5742 5965 -396 -74 265 ATOM 394 CD PRO A 52 -24.176 7.967 -29.614 1.00 39.98 C ANISOU 394 CD PRO A 52 4924 5052 5214 -426 -78 314 ATOM 395 N ASN A 53 -25.411 5.155 -33.150 1.00 32.49 N ANISOU 395 N ASN A 53 4060 3939 4345 -492 -191 321 ATOM 396 CA ASN A 53 -24.933 4.095 -34.036 1.00 39.90 C ANISOU 396 CA ASN A 53 5040 4807 5313 -497 -233 310 ATOM 397 C ASN A 53 -24.307 4.776 -35.264 1.00 30.57 C ANISOU 397 C ASN A 53 3880 3604 4132 -458 -216 251 ATOM 398 O ASN A 53 -25.014 5.067 -36.227 1.00 33.19 O ANISOU 398 O ASN A 53 4211 3936 4462 -460 -215 237 ATOM 399 CB ASN A 53 -26.109 3.153 -34.395 1.00 39.06 C ANISOU 399 CB ASN A 53 4934 4683 5222 -542 -275 348 ATOM 400 CG ASN A 53 -25.704 1.867 -35.132 1.00 42.66 C ANISOU 400 CG ASN A 53 5434 5063 5710 -545 -326 334 ATOM 401 OD1 ASN A 53 -24.623 1.762 -35.709 1.00 37.99 O ANISOU 401 OD1 ASN A 53 4872 4435 5128 -508 -326 285 ATOM 402 ND2 ASN A 53 -26.598 0.877 -35.141 1.00 43.63 N ANISOU 402 ND2 ASN A 53 5562 5164 5852 -589 -373 376 ATOM 403 N TYR A 54 -22.996 5.048 -35.183 1.00 24.24 N ANISOU 403 N TYR A 54 3093 2788 3329 -423 -203 217 ATOM 404 CA TYR A 54 -22.236 5.783 -36.194 1.00 27.24 C ANISOU 404 CA TYR A 54 3483 3166 3699 -388 -179 166 ATOM 405 C TYR A 54 -22.172 5.113 -37.570 1.00 29.59 C ANISOU 405 C TYR A 54 3810 3421 4013 -387 -208 138 ATOM 406 O TYR A 54 -22.193 5.833 -38.568 1.00 20.22 O ANISOU 406 O TYR A 54 2622 2244 2816 -378 -194 113 ATOM 407 CB TYR A 54 -20.824 6.077 -35.665 1.00 28.58 C ANISOU 407 CB TYR A 54 3660 3336 3862 -353 -160 139 ATOM 408 CG TYR A 54 -20.794 7.200 -34.655 1.00 31.67 C ANISOU 408 CG TYR A 54 4024 3779 4232 -343 -121 149 ATOM 409 CD1 TYR A 54 -21.109 8.500 -35.090 1.00 25.68 C ANISOU 409 CD1 TYR A 54 3249 3053 3455 -329 -92 131 ATOM 410 CD2 TYR A 54 -20.450 6.970 -33.306 1.00 28.90 C ANISOU 410 CD2 TYR A 54 3662 3443 3878 -347 -118 175 ATOM 411 CE1 TYR A 54 -21.084 9.568 -34.185 1.00 26.40 C ANISOU 411 CE1 TYR A 54 3314 3188 3528 -317 -62 136 ATOM 412 CE2 TYR A 54 -20.380 8.055 -32.409 1.00 30.99 C ANISOU 412 CE2 TYR A 54 3900 3756 4120 -335 -84 180 ATOM 413 CZ TYR A 54 -20.700 9.356 -32.848 1.00 29.20 C ANISOU 413 CZ TYR A 54 3659 3559 3878 -318 -57 159 ATOM 414 OH TYR A 54 -20.648 10.409 -31.984 1.00 31.43 O ANISOU 414 OH TYR A 54 3915 3885 4140 -303 -30 160 ATOM 415 N GLU A 55 -22.134 3.771 -37.609 1.00 23.18 N ANISOU 415 N GLU A 55 3022 2560 3224 -395 -252 142 ATOM 416 CA GLU A 55 -22.189 2.983 -38.840 1.00 31.05 C ANISOU 416 CA GLU A 55 4046 3514 4237 -394 -286 114 ATOM 417 C GLU A 55 -23.520 3.180 -39.584 1.00 30.00 C ANISOU 417 C GLU A 55 3904 3391 4103 -423 -292 132 ATOM 418 O GLU A 55 -23.500 3.438 -40.787 1.00 33.78 O ANISOU 418 O GLU A 55 4392 3864 4577 -413 -290 99 ATOM 419 CB GLU A 55 -21.952 1.480 -38.555 1.00 29.48 C ANISOU 419 CB GLU A 55 3874 3258 4069 -402 -341 122 ATOM 420 CG GLU A 55 -20.507 1.082 -38.181 1.00 34.59 C ANISOU 420 CG GLU A 55 4538 3885 4722 -365 -344 87 ATOM 421 CD GLU A 55 -20.023 1.512 -36.792 1.00 32.76 C ANISOU 421 CD GLU A 55 4290 3673 4486 -369 -328 120 ATOM 422 OE1 GLU A 55 -18.787 1.586 -36.630 1.00 37.13 O ANISOU 422 OE1 GLU A 55 4851 4219 5038 -337 -320 92 ATOM 423 OE2 GLU A 55 -20.874 1.742 -35.905 1.00 44.55 O1- ANISOU 423 OE2 GLU A 55 5762 5192 5974 -404 -324 173 ATOM 424 N ASP A 56 -24.637 3.088 -38.840 1.00 32.82 N ANISOU 424 N ASP A 56 4240 3766 4462 -460 -299 185 ATOM 425 CA ASP A 56 -25.997 3.269 -39.347 1.00 43.59 C ANISOU 425 CA ASP A 56 5594 5141 5826 -488 -306 204 ATOM 426 C ASP A 56 -26.272 4.724 -39.785 1.00 51.62 C ANISOU 426 C ASP A 56 6590 6204 6820 -472 -260 183 ATOM 427 O ASP A 56 -26.861 4.926 -40.847 1.00 47.17 O ANISOU 427 O ASP A 56 6033 5636 6256 -475 -264 167 ATOM 428 CB ASP A 56 -27.036 2.787 -38.310 1.00 54.90 C ANISOU 428 CB ASP A 56 7004 6593 7264 -534 -323 268 ATOM 429 CG ASP A 56 -28.478 2.801 -38.818 1.00 65.48 C ANISOU 429 CG ASP A 56 8330 7945 8604 -566 -334 291 ATOM 430 OD1 ASP A 56 -29.323 3.417 -38.130 1.00 57.17 O ANISOU 430 OD1 ASP A 56 7240 6948 7532 -578 -305 315 ATOM 431 OD2 ASP A 56 -28.726 2.180 -39.873 1.00 64.01 O1- ANISOU 431 OD2 ASP A 56 8171 7712 8437 -577 -373 282 ATOM 432 N LEU A 57 -25.822 5.704 -38.980 1.00 38.15 N ANISOU 432 N LEU A 57 4860 4540 5094 -454 -220 184 ATOM 433 CA LEU A 57 -25.949 7.135 -39.269 1.00 39.31 C ANISOU 433 CA LEU A 57 4988 4726 5222 -438 -184 165 ATOM 434 C LEU A 57 -25.210 7.545 -40.552 1.00 31.04 C ANISOU 434 C LEU A 57 3964 3660 4170 -413 -180 117 ATOM 435 O LEU A 57 -25.792 8.270 -41.359 1.00 38.82 O ANISOU 435 O LEU A 57 4944 4658 5148 -414 -171 106 ATOM 436 CB LEU A 57 -25.438 7.974 -38.075 1.00 38.75 C ANISOU 436 CB LEU A 57 4893 4697 5134 -419 -150 170 ATOM 437 CG LEU A 57 -26.384 8.031 -36.857 1.00 41.28 C ANISOU 437 CG LEU A 57 5179 5059 5447 -441 -144 214 ATOM 438 CD1 LEU A 57 -25.653 8.571 -35.605 1.00 39.75 C ANISOU 438 CD1 LEU A 57 4968 4897 5236 -418 -115 212 ATOM 439 CD2 LEU A 57 -27.681 8.809 -37.170 1.00 48.18 C ANISOU 439 CD2 LEU A 57 6024 5969 6313 -455 -137 226 ATOM 440 N LEU A 58 -23.971 7.051 -40.724 1.00 28.04 N ANISOU 440 N LEU A 58 3608 3251 3794 -392 -187 89 ATOM 441 CA LEU A 58 -23.124 7.313 -41.888 1.00 28.57 C ANISOU 441 CA LEU A 58 3691 3312 3851 -368 -180 42 ATOM 442 C LEU A 58 -23.649 6.666 -43.184 1.00 38.80 C ANISOU 442 C LEU A 58 5005 4584 5155 -381 -208 29 ATOM 443 O LEU A 58 -23.420 7.229 -44.254 1.00 29.21 O ANISOU 443 O LEU A 58 3792 3380 3925 -373 -198 1 ATOM 444 CB LEU A 58 -21.673 6.880 -41.567 1.00 33.94 C ANISOU 444 CB LEU A 58 4388 3974 4532 -340 -183 14 ATOM 445 CG LEU A 58 -20.615 7.252 -42.633 1.00 38.14 C ANISOU 445 CG LEU A 58 4930 4517 5046 -313 -168 -32 ATOM 446 CD1 LEU A 58 -20.536 8.780 -42.841 1.00 41.31 C ANISOU 446 CD1 LEU A 58 5310 4961 5426 -306 -131 -31 ATOM 447 CD2 LEU A 58 -19.242 6.637 -42.294 1.00 31.95 C ANISOU 447 CD2 LEU A 58 4160 3713 4266 -285 -177 -60 ATOM 448 N ILE A 59 -24.352 5.522 -43.077 1.00 46.00 N ANISOU 448 N ILE A 59 5927 5462 6088 -404 -244 51 ATOM 449 CA ILE A 59 -24.920 4.797 -44.221 1.00 43.39 C ANISOU 449 CA ILE A 59 5616 5100 5768 -416 -278 37 ATOM 450 C ILE A 59 -26.020 5.595 -44.957 1.00 37.96 C ANISOU 450 C ILE A 59 4915 4439 5070 -434 -266 46 ATOM 451 O ILE A 59 -26.099 5.504 -46.182 1.00 49.77 O ANISOU 451 O ILE A 59 6422 5930 6558 -430 -272 16 ATOM 452 CB ILE A 59 -25.431 3.369 -43.810 1.00 51.64 C ANISOU 452 CB ILE A 59 6675 6104 6841 -441 -325 68 ATOM 453 CG1 ILE A 59 -24.834 2.275 -44.722 1.00 48.19 C ANISOU 453 CG1 ILE A 59 6273 5617 6419 -427 -368 28 ATOM 454 CG2 ILE A 59 -26.964 3.167 -43.735 1.00 51.42 C ANISOU 454 CG2 ILE A 59 6630 6086 6820 -483 -336 116 ATOM 455 CD1 ILE A 59 -23.332 2.036 -44.511 1.00 50.08 C ANISOU 455 CD1 ILE A 59 6526 5847 6655 -386 -363 -15 ATOM 456 N ARG A 60 -26.808 6.391 -44.209 1.00 49.16 N ANISOU 456 N ARG A 60 6305 5887 6486 -453 -250 85 ATOM 457 CA ARG A 60 -27.831 7.285 -44.757 1.00 57.55 C ANISOU 457 CA ARG A 60 7349 6975 7541 -468 -240 95 ATOM 458 C ARG A 60 -27.265 8.608 -45.315 1.00 64.56 C ANISOU 458 C ARG A 60 8231 7892 8408 -445 -208 65 ATOM 459 O ARG A 60 -28.042 9.372 -45.890 1.00 68.03 O ANISOU 459 O ARG A 60 8654 8352 8842 -455 -200 73 ATOM 460 CB ARG A 60 -28.923 7.545 -43.696 1.00 64.60 C ANISOU 460 CB ARG A 60 8209 7899 8436 -489 -231 142 ATOM 461 CG ARG A 60 -29.780 6.303 -43.389 1.00 66.44 C ANISOU 461 CG ARG A 60 8444 8113 8688 -524 -267 182 ATOM 462 CD ARG A 60 -31.020 6.609 -42.529 1.00 67.49 C ANISOU 462 CD ARG A 60 8538 8288 8816 -550 -258 226 ATOM 463 NE ARG A 60 -30.677 6.872 -41.124 1.00 68.26 N ANISOU 463 NE ARG A 60 8609 8424 8903 -543 -235 246 ATOM 464 CZ ARG A 60 -30.451 5.918 -40.205 1.00 77.89 C ANISOU 464 CZ ARG A 60 9829 9636 10130 -558 -250 274 ATOM 465 NH1 ARG A 60 -30.570 4.621 -40.514 1.00 83.44 N ANISOU 465 NH1 ARG A 60 10561 10290 10854 -579 -293 286 ATOM 466 NH2 ARG A 60 -30.093 6.256 -38.960 1.00 78.98 N1+ ANISOU 466 NH2 ARG A 60 9940 9814 10253 -551 -226 291 ATOM 467 N LYS A 61 -25.952 8.862 -45.164 1.00 45.93 N ANISOU 467 N LYS A 61 5882 5531 6036 -417 -194 33 ATOM 468 CA LYS A 61 -25.289 10.041 -45.721 1.00 42.21 C ANISOU 468 CA LYS A 61 5404 5088 5545 -400 -169 12 ATOM 469 C LYS A 61 -24.735 9.751 -47.120 1.00 23.68 C ANISOU 469 C LYS A 61 3078 2735 3186 -394 -177 -26 ATOM 470 O LYS A 61 -24.036 8.758 -47.320 1.00 27.42 O ANISOU 470 O LYS A 61 3570 3187 3661 -382 -192 -50 ATOM 471 CB LYS A 61 -24.152 10.528 -44.796 1.00 44.72 C ANISOU 471 CB LYS A 61 5714 5422 5854 -376 -144 7 ATOM 472 CG LYS A 61 -24.584 10.907 -43.369 1.00 41.19 C ANISOU 472 CG LYS A 61 5243 4992 5413 -379 -132 40 ATOM 473 CD LYS A 61 -25.748 11.907 -43.313 1.00 37.40 C ANISOU 473 CD LYS A 61 4740 4546 4927 -380 -117 49 ATOM 474 CE LYS A 61 -26.107 12.332 -41.886 1.00 43.22 C ANISOU 474 CE LYS A 61 5448 5305 5666 -383 -108 79 ATOM 475 NZ LYS A 61 -27.255 13.249 -41.905 1.00 51.46 N1+ ANISOU 475 NZ LYS A 61 6466 6378 6707 -384 -102 86 ATOM 476 N SER A 62 -25.014 10.690 -48.033 1.00 38.70 N ANISOU 476 N SER A 62 4973 4657 5074 -401 -171 -31 ATOM 477 CA SER A 62 -24.339 10.860 -49.315 1.00 45.57 C ANISOU 477 CA SER A 62 5855 5536 5923 -397 -174 -64 ATOM 478 C SER A 62 -23.159 11.837 -49.146 1.00 34.61 C ANISOU 478 C SER A 62 4459 4179 4513 -380 -150 -77 ATOM 479 O SER A 62 -23.069 12.520 -48.122 1.00 27.18 O ANISOU 479 O SER A 62 3502 3250 3574 -374 -134 -59 ATOM 480 CB SER A 62 -25.384 11.357 -50.342 1.00 38.53 C ANISOU 480 CB SER A 62 4961 4651 5028 -422 -185 -57 ATOM 481 OG SER A 62 -25.775 12.704 -50.137 1.00 34.07 O ANISOU 481 OG SER A 62 4375 4105 4466 -429 -173 -31 ATOM 482 N ASN A 63 -22.298 11.928 -50.175 1.00 30.60 N ANISOU 482 N ASN A 63 3959 3686 3982 -371 -150 -110 ATOM 483 CA ASN A 63 -21.236 12.943 -50.262 1.00 33.89 C ANISOU 483 CA ASN A 63 4366 4138 4373 -362 -130 -118 ATOM 484 C ASN A 63 -21.792 14.377 -50.246 1.00 38.59 C ANISOU 484 C ASN A 63 4946 4748 4968 -380 -126 -90 ATOM 485 O ASN A 63 -21.185 15.253 -49.632 1.00 29.96 O ANISOU 485 O ASN A 63 3842 3669 3872 -371 -112 -80 ATOM 486 CB ASN A 63 -20.408 12.768 -51.552 1.00 22.04 C ANISOU 486 CB ASN A 63 2870 2663 2841 -361 -134 -152 ATOM 487 CG ASN A 63 -19.657 11.446 -51.659 1.00 26.17 C ANISOU 487 CG ASN A 63 3404 3176 3362 -334 -139 -188 ATOM 488 OD1 ASN A 63 -19.093 10.964 -50.680 1.00 37.53 O ANISOU 488 OD1 ASN A 63 4847 4596 4818 -315 -134 -186 ATOM 489 ND2 ASN A 63 -19.619 10.869 -52.860 1.00 23.93 N ANISOU 489 ND2 ASN A 63 3128 2909 3057 -331 -150 -223 ATOM 490 N HIS A 64 -22.951 14.573 -50.899 1.00 35.15 N ANISOU 490 N HIS A 64 4510 4308 4539 -403 -141 -78 ATOM 491 CA HIS A 64 -23.655 15.848 -50.997 1.00 31.69 C ANISOU 491 CA HIS A 64 4058 3880 4102 -418 -144 -55 ATOM 492 C HIS A 64 -24.207 16.368 -49.653 1.00 24.17 C ANISOU 492 C HIS A 64 3092 2919 3173 -409 -137 -32 ATOM 493 O HIS A 64 -24.345 17.584 -49.522 1.00 26.60 O ANISOU 493 O HIS A 64 3387 3236 3483 -411 -140 -19 ATOM 494 CB HIS A 64 -24.745 15.736 -52.081 1.00 40.71 C ANISOU 494 CB HIS A 64 5204 5019 5246 -444 -164 -50 ATOM 495 CG HIS A 64 -25.271 17.067 -52.563 1.00 49.13 C ANISOU 495 CG HIS A 64 6259 6097 6309 -462 -174 -32 ATOM 496 ND1 HIS A 64 -26.330 17.726 -51.963 1.00 47.96 N ANISOU 496 ND1 HIS A 64 6100 5938 6185 -469 -183 -10 ATOM 497 CD2 HIS A 64 -24.877 17.874 -53.607 1.00 44.36 C ANISOU 497 CD2 HIS A 64 5653 5518 5683 -476 -180 -32 ATOM 498 CE1 HIS A 64 -26.499 18.879 -52.619 1.00 45.09 C ANISOU 498 CE1 HIS A 64 5730 5585 5817 -483 -197 0 ATOM 499 NE2 HIS A 64 -25.645 19.041 -53.623 1.00 45.49 N ANISOU 499 NE2 HIS A 64 5787 5656 5841 -490 -196 -10 ATOM 500 N ASN A 65 -24.461 15.479 -48.669 1.00 28.85 N ANISOU 500 N ASN A 65 3685 3496 3781 -397 -131 -28 ATOM 501 CA ASN A 65 -24.851 15.856 -47.297 1.00 33.12 C ANISOU 501 CA ASN A 65 4208 4038 4336 -386 -122 -9 ATOM 502 C ASN A 65 -23.728 16.547 -46.501 1.00 30.58 C ANISOU 502 C ASN A 65 3883 3732 4006 -365 -105 -15 ATOM 503 O ASN A 65 -24.037 17.189 -45.497 1.00 31.99 O ANISOU 503 O ASN A 65 4045 3917 4192 -353 -98 -3 ATOM 504 CB ASN A 65 -25.366 14.625 -46.508 1.00 37.62 C ANISOU 504 CB ASN A 65 4779 4593 4922 -386 -122 2 ATOM 505 CG ASN A 65 -26.697 14.066 -47.017 1.00 43.02 C ANISOU 505 CG ASN A 65 5461 5266 5621 -409 -140 18 ATOM 506 OD1 ASN A 65 -26.789 12.891 -47.357 1.00 51.95 O ANISOU 506 OD1 ASN A 65 6605 6374 6758 -418 -153 18 ATOM 507 ND2 ASN A 65 -27.742 14.895 -47.054 1.00 41.99 N ANISOU 507 ND2 ASN A 65 5313 5148 5495 -418 -144 32 ATOM 508 N PHE A 66 -22.469 16.424 -46.953 1.00 25.30 N ANISOU 508 N PHE A 66 3224 3070 3318 -359 -100 -34 ATOM 509 CA PHE A 66 -21.313 17.087 -46.361 1.00 28.62 C ANISOU 509 CA PHE A 66 3641 3504 3729 -341 -86 -38 ATOM 510 C PHE A 66 -20.998 18.370 -47.142 1.00 23.47 C ANISOU 510 C PHE A 66 2985 2870 3063 -352 -94 -36 ATOM 511 O PHE A 66 -20.362 18.308 -48.194 1.00 28.09 O ANISOU 511 O PHE A 66 3577 3468 3630 -367 -101 -45 ATOM 512 CB PHE A 66 -20.112 16.121 -46.352 1.00 19.34 C ANISOU 512 CB PHE A 66 2477 2329 2543 -326 -76 -58 ATOM 513 CG PHE A 66 -20.313 14.889 -45.490 1.00 22.67 C ANISOU 513 CG PHE A 66 2904 2729 2982 -316 -74 -56 ATOM 514 CD1 PHE A 66 -20.316 15.003 -44.083 1.00 34.43 C ANISOU 514 CD1 PHE A 66 4383 4216 4482 -303 -62 -42 ATOM 515 CD2 PHE A 66 -20.626 13.648 -46.081 1.00 21.08 C ANISOU 515 CD2 PHE A 66 2716 2508 2786 -322 -87 -67 ATOM 516 CE1 PHE A 66 -20.577 13.886 -43.300 1.00 33.68 C ANISOU 516 CE1 PHE A 66 4292 4102 4401 -300 -64 -34 ATOM 517 CE2 PHE A 66 -20.875 12.541 -45.280 1.00 26.55 C ANISOU 517 CE2 PHE A 66 3414 3176 3496 -317 -92 -60 ATOM 518 CZ PHE A 66 -20.847 12.659 -43.895 1.00 36.82 C ANISOU 518 CZ PHE A 66 4704 4477 4807 -308 -81 -42 ATOM 519 N LEU A 67 -21.434 19.515 -46.594 1.00 29.54 N ANISOU 519 N LEU A 67 3742 3642 3841 -345 -98 -23 ATOM 520 CA LEU A 67 -21.032 20.843 -47.050 1.00 30.19 C ANISOU 520 CA LEU A 67 3821 3735 3913 -356 -113 -17 ATOM 521 C LEU A 67 -19.685 21.187 -46.398 1.00 22.59 C ANISOU 521 C LEU A 67 2859 2785 2940 -341 -103 -21 ATOM 522 O LEU A 67 -19.624 21.289 -45.174 1.00 26.73 O ANISOU 522 O LEU A 67 3377 3303 3475 -319 -94 -19 ATOM 523 CB LEU A 67 -22.145 21.861 -46.716 1.00 30.10 C ANISOU 523 CB LEU A 67 3798 3715 3922 -355 -132 -4 ATOM 524 CG LEU A 67 -21.802 23.350 -46.983 1.00 39.66 C ANISOU 524 CG LEU A 67 5008 4930 5131 -364 -157 4 ATOM 525 CD1 LEU A 67 -21.506 23.628 -48.474 1.00 40.92 C ANISOU 525 CD1 LEU A 67 5174 5098 5274 -399 -176 11 ATOM 526 CD2 LEU A 67 -22.890 24.276 -46.401 1.00 38.25 C ANISOU 526 CD2 LEU A 67 4817 4740 4977 -350 -177 10 ATOM 527 N VAL A 68 -18.644 21.364 -47.223 1.00 27.89 N ANISOU 527 N VAL A 68 3535 3477 3587 -353 -103 -26 ATOM 528 CA VAL A 68 -17.304 21.734 -46.776 1.00 22.00 C ANISOU 528 CA VAL A 68 2787 2746 2825 -344 -95 -28 ATOM 529 C VAL A 68 -16.940 23.071 -47.437 1.00 28.60 C ANISOU 529 C VAL A 68 3619 3596 3650 -366 -120 -11 ATOM 530 O VAL A 68 -17.088 23.193 -48.653 1.00 30.28 O ANISOU 530 O VAL A 68 3833 3826 3847 -394 -133 -6 ATOM 531 CB VAL A 68 -16.246 20.666 -47.168 1.00 22.40 C ANISOU 531 CB VAL A 68 2842 2816 2853 -338 -76 -48 ATOM 532 CG1 VAL A 68 -14.803 21.062 -46.798 1.00 22.12 C ANISOU 532 CG1 VAL A 68 2802 2800 2803 -327 -67 -48 ATOM 533 CG2 VAL A 68 -16.568 19.297 -46.540 1.00 28.34 C ANISOU 533 CG2 VAL A 68 3601 3548 3620 -318 -62 -62 ATOM 534 N GLN A 69 -16.482 24.038 -46.626 1.00 21.81 N ANISOU 534 N GLN A 69 2757 2731 2800 -356 -128 -1 ATOM 535 CA GLN A 69 -16.126 25.385 -47.072 1.00 23.71 C ANISOU 535 CA GLN A 69 2996 2979 3034 -379 -160 19 ATOM 536 C GLN A 69 -14.730 25.752 -46.556 1.00 20.56 C ANISOU 536 C GLN A 69 2595 2597 2620 -375 -155 23 ATOM 537 O GLN A 69 -14.514 25.765 -45.345 1.00 21.73 O ANISOU 537 O GLN A 69 2743 2734 2780 -346 -142 16 ATOM 538 CB GLN A 69 -17.173 26.406 -46.578 1.00 26.42 C ANISOU 538 CB GLN A 69 3338 3293 3408 -374 -189 29 ATOM 539 CG GLN A 69 -18.593 26.176 -47.123 1.00 40.95 C ANISOU 539 CG GLN A 69 5177 5120 5262 -382 -199 28 ATOM 540 CD GLN A 69 -19.586 27.156 -46.502 1.00 49.38 C ANISOU 540 CD GLN A 69 6239 6161 6361 -365 -224 30 ATOM 541 OE1 GLN A 69 -19.717 28.290 -46.959 1.00 48.81 O ANISOU 541 OE1 GLN A 69 6160 6081 6305 -336 -208 18 ATOM 542 NE2 GLN A 69 -20.286 26.720 -45.453 1.00 50.36 N ANISOU 542 NE2 GLN A 69 6365 6276 6494 -382 -267 45 ATOM 543 N ALA A 70 -13.831 26.085 -47.492 1.00 19.93 N ANISOU 543 N ALA A 70 2512 2550 2512 -404 -165 35 ATOM 544 CA ALA A 70 -12.527 26.688 -47.239 1.00 26.71 C ANISOU 544 CA ALA A 70 3367 3429 3354 -408 -168 47 ATOM 545 C ALA A 70 -12.666 28.193 -47.493 1.00 33.59 C ANISOU 545 C ALA A 70 4239 4290 4234 -436 -216 77 ATOM 546 O ALA A 70 -12.635 28.621 -48.649 1.00 28.34 O ANISOU 546 O ALA A 70 3572 3644 3553 -475 -240 96 ATOM 547 CB ALA A 70 -11.495 26.049 -48.184 1.00 29.91 C ANISOU 547 CB ALA A 70 3762 3885 3717 -424 -150 41 ATOM 548 N GLY A 71 -12.882 28.967 -46.416 1.00 27.59 N ANISOU 548 N GLY A 71 3484 3500 3500 -416 -234 81 ATOM 549 CA GLY A 71 -13.289 30.370 -46.500 1.00 36.78 C ANISOU 549 CA GLY A 71 4652 4639 4683 -434 -287 104 ATOM 550 C GLY A 71 -14.718 30.426 -47.060 1.00 32.11 C ANISOU 550 C GLY A 71 4063 4026 4111 -440 -304 102 ATOM 551 O GLY A 71 -15.615 29.779 -46.520 1.00 47.56 O ANISOU 551 O GLY A 71 6020 5964 6087 -409 -284 79 ATOM 552 N ASN A 72 -14.911 31.184 -48.150 1.00 48.17 N ANISOU 552 N ASN A 72 6098 6066 6138 -482 -342 127 ATOM 553 CA ASN A 72 -16.169 31.229 -48.901 1.00 67.04 C ANISOU 553 CA ASN A 72 8490 8440 8544 -493 -360 128 ATOM 554 C ASN A 72 -16.256 30.134 -49.991 1.00 64.35 C ANISOU 554 C ASN A 72 8145 8133 8172 -516 -333 124 ATOM 555 O ASN A 72 -17.357 29.866 -50.471 1.00 74.45 O ANISOU 555 O ASN A 72 9425 9400 9461 -526 -344 124 ATOM 556 CB ASN A 72 -16.327 32.631 -49.539 1.00 88.61 C ANISOU 556 CB ASN A 72 11227 11151 11290 -525 -427 158 ATOM 557 CG ASN A 72 -17.788 33.022 -49.783 1.00115.38 C ANISOU 557 CG ASN A 72 14619 14513 14707 -526 -453 156 ATOM 558 OD1 ASN A 72 -18.477 33.465 -48.868 1.00128.52 O ANISOU 558 OD1 ASN A 72 16282 16195 16356 -555 -449 164 ATOM 559 ND2 ASN A 72 -18.265 32.866 -51.021 1.00115.28 N ANISOU 559 ND2 ASN A 72 14609 14458 14734 -494 -480 144 ATOM 560 N VAL A 73 -15.117 29.538 -50.387 1.00 45.17 N ANISOU 560 N VAL A 73 5710 5746 5707 -522 -300 119 ATOM 561 CA VAL A 73 -15.037 28.564 -51.478 1.00 33.12 C ANISOU 561 CA VAL A 73 4179 4257 4149 -541 -277 111 ATOM 562 C VAL A 73 -15.523 27.182 -51.005 1.00 34.98 C ANISOU 562 C VAL A 73 4418 4480 4395 -504 -235 76 ATOM 563 O VAL A 73 -14.905 26.604 -50.111 1.00 26.56 O ANISOU 563 O VAL A 73 3350 3410 3331 -471 -205 57 ATOM 564 CB VAL A 73 -13.582 28.413 -52.013 1.00 39.48 C ANISOU 564 CB VAL A 73 4972 5120 4907 -563 -264 117 ATOM 565 CG1 VAL A 73 -13.429 27.353 -53.127 1.00 43.24 C ANISOU 565 CG1 VAL A 73 5442 5638 5349 -580 -244 103 ATOM 566 CG2 VAL A 73 -13.020 29.758 -52.505 1.00 57.08 C ANISOU 566 CG2 VAL A 73 7198 7364 7127 -604 -308 158 ATOM 567 N GLN A 74 -16.590 26.666 -51.638 1.00 32.60 N ANISOU 567 N GLN A 74 4118 4171 4096 -513 -236 69 ATOM 568 CA GLN A 74 -17.064 25.301 -51.412 1.00 40.43 C ANISOU 568 CA GLN A 74 5114 5154 5095 -485 -202 40 ATOM 569 C GLN A 74 -16.104 24.274 -52.036 1.00 30.74 C ANISOU 569 C GLN A 74 3882 3966 3830 -485 -174 20 ATOM 570 O GLN A 74 -15.717 24.425 -53.196 1.00 29.85 O ANISOU 570 O GLN A 74 3763 3895 3683 -516 -182 27 ATOM 571 CB GLN A 74 -18.509 25.138 -51.933 1.00 48.87 C ANISOU 571 CB GLN A 74 6187 6200 6182 -494 -215 41 ATOM 572 CG GLN A 74 -19.082 23.715 -51.720 1.00 64.67 C ANISOU 572 CG GLN A 74 8193 8195 8186 -476 -186 15 ATOM 573 CD GLN A 74 -20.564 23.570 -52.064 1.00 63.14 C ANISOU 573 CD GLN A 74 8000 7970 8018 -478 -199 18 ATOM 574 OE1 GLN A 74 -21.227 24.518 -52.479 1.00 65.42 O ANISOU 574 OE1 GLN A 74 8288 8247 8323 -494 -229 37 ATOM 575 NE2 GLN A 74 -21.095 22.358 -51.885 1.00 52.46 N ANISOU 575 NE2 GLN A 74 6653 6606 6675 -462 -179 1 ATOM 576 N LEU A 75 -15.785 23.236 -51.252 1.00 29.31 N ANISOU 576 N LEU A 75 3705 3777 3655 -451 -144 -6 ATOM 577 CA LEU A 75 -15.040 22.060 -51.684 1.00 28.99 C ANISOU 577 CA LEU A 75 3661 3766 3586 -442 -120 -34 ATOM 578 C LEU A 75 -16.052 20.924 -51.841 1.00 30.30 C ANISOU 578 C LEU A 75 3838 3907 3768 -430 -114 -54 ATOM 579 O LEU A 75 -16.648 20.508 -50.847 1.00 36.30 O ANISOU 579 O LEU A 75 4604 4626 4561 -411 -110 -52 ATOM 580 CB LEU A 75 -13.987 21.681 -50.619 1.00 26.15 C ANISOU 580 CB LEU A 75 3300 3413 3224 -411 -97 -49 ATOM 581 CG LEU A 75 -12.989 22.793 -50.245 1.00 35.02 C ANISOU 581 CG LEU A 75 4414 4557 4335 -417 -101 -30 ATOM 582 CD1 LEU A 75 -12.132 22.359 -49.044 1.00 34.22 C ANISOU 582 CD1 LEU A 75 4314 4448 4242 -381 -76 -47 ATOM 583 CD2 LEU A 75 -12.119 23.228 -51.436 1.00 34.80 C ANISOU 583 CD2 LEU A 75 4371 4588 4261 -448 -108 -23 ATOM 584 N ARG A 76 -16.233 20.442 -53.079 1.00 33.53 N ANISOU 584 N ARG A 76 4246 4342 4152 -442 -114 -71 ATOM 585 CA ARG A 76 -17.076 19.290 -53.383 1.00 28.26 C ANISOU 585 CA ARG A 76 3590 3648 3498 -435 -114 -89 ATOM 586 C ARG A 76 -16.468 18.011 -52.795 1.00 22.90 C ANISOU 586 C ARG A 76 2917 2959 2824 -399 -96 -121 ATOM 587 O ARG A 76 -15.359 17.645 -53.178 1.00 26.21 O ANISOU 587 O ARG A 76 3330 3413 3215 -387 -84 -144 ATOM 588 CB ARG A 76 -17.264 19.195 -54.910 1.00 27.45 C ANISOU 588 CB ARG A 76 3486 3577 3367 -462 -127 -96 ATOM 589 CG ARG A 76 -17.956 17.911 -55.406 1.00 24.58 C ANISOU 589 CG ARG A 76 3134 3197 3009 -451 -127 -125 ATOM 590 CD ARG A 76 -18.094 17.866 -56.931 1.00 30.30 C ANISOU 590 CD ARG A 76 3855 3961 3698 -479 -139 -134 ATOM 591 NE ARG A 76 -18.932 16.737 -57.356 1.00 30.39 N ANISOU 591 NE ARG A 76 3879 3949 3718 -472 -147 -157 ATOM 592 CZ ARG A 76 -20.271 16.685 -57.273 1.00 39.88 C ANISOU 592 CZ ARG A 76 5092 5106 4953 -482 -161 -140 ATOM 593 NH1 ARG A 76 -20.987 17.709 -56.783 1.00 36.34 N ANISOU 593 NH1 ARG A 76 4641 4636 4531 -495 -167 -104 ATOM 594 NH2 ARG A 76 -20.907 15.585 -57.692 1.00 42.39 N1+ ANISOU 594 NH2 ARG A 76 5422 5404 5278 -479 -171 -160 ATOM 595 N VAL A 77 -17.234 17.345 -51.918 1.00 19.96 N ANISOU 595 N VAL A 77 2556 2542 2488 -384 -95 -121 ATOM 596 CA VAL A 77 -16.908 16.025 -51.388 1.00 25.45 C ANISOU 596 CA VAL A 77 3259 3216 3194 -354 -86 -146 ATOM 597 C VAL A 77 -17.273 14.968 -52.449 1.00 34.57 C ANISOU 597 C VAL A 77 4425 4371 4341 -353 -96 -175 ATOM 598 O VAL A 77 -18.343 15.051 -53.053 1.00 28.23 O ANISOU 598 O VAL A 77 3628 3551 3548 -372 -111 -165 ATOM 599 CB VAL A 77 -17.667 15.745 -50.060 1.00 31.74 C ANISOU 599 CB VAL A 77 4061 3969 4029 -343 -84 -127 ATOM 600 CG1 VAL A 77 -17.409 14.349 -49.461 1.00 24.28 C ANISOU 600 CG1 VAL A 77 3127 3000 3099 -317 -81 -148 ATOM 601 CG2 VAL A 77 -17.329 16.814 -49.003 1.00 29.72 C ANISOU 601 CG2 VAL A 77 3795 3717 3780 -339 -75 -104 ATOM 602 N ILE A 78 -16.350 14.026 -52.674 1.00 28.26 N ANISOU 602 N ILE A 78 3627 3588 3524 -330 -92 -212 ATOM 603 CA ILE A 78 -16.445 12.962 -53.677 1.00 28.49 C ANISOU 603 CA ILE A 78 3665 3617 3544 -322 -106 -248 ATOM 604 C ILE A 78 -16.250 11.559 -53.061 1.00 32.68 C ANISOU 604 C ILE A 78 4210 4108 4099 -290 -113 -274 ATOM 605 O ILE A 78 -16.413 10.567 -53.771 1.00 31.61 O ANISOU 605 O ILE A 78 4086 3963 3962 -280 -131 -307 ATOM 606 CB ILE A 78 -15.406 13.175 -54.817 1.00 24.34 C ANISOU 606 CB ILE A 78 3124 3156 2968 -324 -101 -277 ATOM 607 CG1 ILE A 78 -13.934 13.167 -54.337 1.00 28.49 C ANISOU 607 CG1 ILE A 78 3638 3714 3475 -298 -83 -295 ATOM 608 CG2 ILE A 78 -15.734 14.449 -55.622 1.00 25.65 C ANISOU 608 CG2 ILE A 78 3279 3355 3113 -363 -102 -244 ATOM 609 CD1 ILE A 78 -12.902 13.107 -55.471 1.00 33.58 C ANISOU 609 CD1 ILE A 78 4262 4431 4066 -295 -78 -329 ATOM 610 N GLY A 79 -15.945 11.495 -51.755 1.00 32.54 N ANISOU 610 N GLY A 79 4194 4066 4104 -275 -104 -259 ATOM 611 CA GLY A 79 -15.867 10.253 -51.001 1.00 23.16 C ANISOU 611 CA GLY A 79 3020 2833 2945 -250 -116 -274 ATOM 612 C GLY A 79 -15.991 10.593 -49.513 1.00 19.09 C ANISOU 612 C GLY A 79 2503 2293 2456 -249 -105 -238 ATOM 613 O GLY A 79 -15.679 11.705 -49.088 1.00 21.77 O ANISOU 613 O GLY A 79 2829 2653 2788 -259 -86 -212 ATOM 614 N HIS A 80 -16.419 9.606 -48.716 1.00 23.07 N ANISOU 614 N HIS A 80 3021 2752 2991 -240 -121 -235 ATOM 615 CA HIS A 80 -16.494 9.696 -47.261 1.00 24.64 C ANISOU 615 CA HIS A 80 3216 2932 3212 -238 -111 -203 ATOM 616 C HIS A 80 -16.252 8.311 -46.651 1.00 31.58 C ANISOU 616 C HIS A 80 4111 3769 4117 -220 -133 -213 ATOM 617 O HIS A 80 -16.733 7.308 -47.181 1.00 32.79 O ANISOU 617 O HIS A 80 4281 3893 4285 -222 -163 -227 ATOM 618 CB HIS A 80 -17.833 10.320 -46.806 1.00 35.21 C ANISOU 618 CB HIS A 80 4550 4263 4567 -265 -109 -160 ATOM 619 CG HIS A 80 -19.076 9.518 -47.104 1.00 35.54 C ANISOU 619 CG HIS A 80 4602 4272 4628 -284 -134 -150 ATOM 620 ND1 HIS A 80 -19.782 9.633 -48.287 1.00 38.52 N ANISOU 620 ND1 HIS A 80 4982 4657 4997 -302 -144 -155 ATOM 621 CD2 HIS A 80 -19.760 8.586 -46.356 1.00 39.33 C ANISOU 621 CD2 HIS A 80 5091 4715 5137 -291 -155 -132 ATOM 622 CE1 HIS A 80 -20.815 8.793 -48.215 1.00 45.13 C ANISOU 622 CE1 HIS A 80 5830 5461 5857 -318 -169 -142 ATOM 623 NE2 HIS A 80 -20.858 8.114 -47.074 1.00 41.00 N ANISOU 623 NE2 HIS A 80 5311 4911 5357 -312 -176 -126 ATOM 624 N SER A 81 -15.529 8.294 -45.526 1.00 25.42 N ANISOU 624 N SER A 81 3328 2986 3345 -204 -122 -206 ATOM 625 CA SER A 81 -15.232 7.097 -44.748 1.00 23.31 C ANISOU 625 CA SER A 81 3075 2678 3104 -191 -145 -208 ATOM 626 C SER A 81 -14.963 7.482 -43.290 1.00 28.99 C ANISOU 626 C SER A 81 3785 3398 3833 -190 -128 -176 ATOM 627 O SER A 81 -14.629 8.631 -43.004 1.00 24.11 O ANISOU 627 O SER A 81 3151 2812 3198 -193 -98 -161 ATOM 628 CB SER A 81 -14.065 6.311 -45.394 1.00 23.28 C ANISOU 628 CB SER A 81 3079 2672 3093 -156 -159 -261 ATOM 629 OG SER A 81 -12.808 6.933 -45.201 1.00 31.08 O ANISOU 629 OG SER A 81 4052 3703 4054 -136 -130 -277 ATOM 630 N MET A 82 -15.094 6.490 -42.403 1.00 33.19 N ANISOU 630 N MET A 82 4328 3891 4391 -187 -151 -165 ATOM 631 CA MET A 82 -14.847 6.614 -40.974 1.00 28.79 C ANISOU 631 CA MET A 82 3764 3332 3844 -189 -140 -132 ATOM 632 C MET A 82 -13.615 5.776 -40.604 1.00 23.41 C ANISOU 632 C MET A 82 3093 2632 3171 -159 -153 -157 ATOM 633 O MET A 82 -13.542 4.607 -40.980 1.00 31.49 O ANISOU 633 O MET A 82 4134 3618 4213 -149 -189 -179 ATOM 634 CB MET A 82 -16.132 6.173 -40.247 1.00 33.88 C ANISOU 634 CB MET A 82 4410 3952 4512 -220 -159 -87 ATOM 635 CG MET A 82 -16.060 6.139 -38.715 1.00 27.97 C ANISOU 635 CG MET A 82 3652 3204 3772 -225 -152 -51 ATOM 636 SD MET A 82 -17.692 6.046 -37.929 1.00 33.82 S ANISOU 636 SD MET A 82 4377 3955 4520 -267 -153 5 ATOM 637 CE MET A 82 -18.264 4.418 -38.477 1.00 38.45 C ANISOU 637 CE MET A 82 4986 4486 5137 -289 -210 18 ATOM 638 N GLN A 83 -12.683 6.394 -39.865 1.00 22.65 N ANISOU 638 N GLN A 83 2984 2558 3062 -145 -126 -155 ATOM 639 CA GLN A 83 -11.547 5.732 -39.235 1.00 26.72 C ANISOU 639 CA GLN A 83 3506 3057 3588 -118 -137 -171 ATOM 640 C GLN A 83 -11.627 6.073 -37.746 1.00 29.57 C ANISOU 640 C GLN A 83 3859 3419 3957 -129 -124 -128 ATOM 641 O GLN A 83 -11.305 7.199 -37.361 1.00 24.21 O ANISOU 641 O GLN A 83 3164 2776 3259 -128 -91 -117 ATOM 642 CB GLN A 83 -10.218 6.204 -39.864 1.00 24.27 C ANISOU 642 CB GLN A 83 3189 2782 3253 -87 -118 -214 ATOM 643 CG GLN A 83 -8.993 5.459 -39.281 1.00 27.87 C ANISOU 643 CG GLN A 83 3649 3221 3720 -57 -130 -234 ATOM 644 CD GLN A 83 -7.642 6.053 -39.680 1.00 32.75 C ANISOU 644 CD GLN A 83 4252 3882 4309 -28 -106 -270 ATOM 645 OE1 GLN A 83 -7.558 6.979 -40.485 1.00 31.64 O ANISOU 645 OE1 GLN A 83 4098 3786 4139 -35 -79 -274 ATOM 646 NE2 GLN A 83 -6.563 5.512 -39.112 1.00 36.51 N ANISOU 646 NE2 GLN A 83 4732 4347 4794 2 -118 -293 ATOM 647 N ASN A 84 -12.076 5.088 -36.950 1.00 22.74 N ANISOU 647 N ASN A 84 3005 2516 3118 -140 -154 -104 ATOM 648 CA ASN A 84 -12.294 5.177 -35.502 1.00 29.20 C ANISOU 648 CA ASN A 84 3813 3340 3941 -155 -145 -60 ATOM 649 C ASN A 84 -13.326 6.284 -35.208 1.00 23.69 C ANISOU 649 C ASN A 84 3096 2681 3226 -177 -114 -32 ATOM 650 O ASN A 84 -14.455 6.161 -35.682 1.00 24.19 O ANISOU 650 O ASN A 84 3159 2742 3292 -198 -122 -22 ATOM 651 CB ASN A 84 -10.941 5.305 -34.753 1.00 22.67 C ANISOU 651 CB ASN A 84 2985 2520 3110 -127 -132 -75 ATOM 652 CG ASN A 84 -10.014 4.105 -34.984 1.00 25.26 C ANISOU 652 CG ASN A 84 3333 2806 3461 -104 -171 -104 ATOM 653 OD1 ASN A 84 -10.386 2.965 -34.713 1.00 26.35 O ANISOU 653 OD1 ASN A 84 3485 2901 3626 -118 -212 -87 ATOM 654 ND2 ASN A 84 -8.799 4.357 -35.475 1.00 28.48 N ANISOU 654 ND2 ASN A 84 3739 3226 3857 -68 -162 -149 ATOM 655 N CYS A 85 -12.936 7.338 -34.475 1.00 27.54 N ANISOU 655 N CYS A 85 3566 3202 3695 -172 -81 -21 ATOM 656 CA CYS A 85 -13.810 8.462 -34.132 1.00 21.86 C ANISOU 656 CA CYS A 85 2827 2518 2962 -189 -57 4 ATOM 657 C CYS A 85 -13.720 9.641 -35.122 1.00 22.89 C ANISOU 657 C CYS A 85 2951 2676 3072 -179 -35 -20 ATOM 658 O CYS A 85 -14.441 10.614 -34.927 1.00 19.37 O ANISOU 658 O CYS A 85 2487 2257 2614 -185 -16 -7 ATOM 659 CB CYS A 85 -13.594 8.933 -32.683 1.00 30.38 C ANISOU 659 CB CYS A 85 3890 3618 4034 -189 -41 30 ATOM 660 SG CYS A 85 -13.963 7.567 -31.545 1.00 23.70 S ANISOU 660 SG CYS A 85 3048 2748 3208 -211 -70 70 ATOM 661 N VAL A 86 -12.883 9.558 -36.170 1.00 17.40 N ANISOU 661 N VAL A 86 2266 1974 2372 -164 -39 -56 ATOM 662 CA VAL A 86 -12.699 10.627 -37.158 1.00 19.62 C ANISOU 662 CA VAL A 86 2540 2282 2631 -160 -22 -75 ATOM 663 C VAL A 86 -13.332 10.250 -38.511 1.00 30.78 C ANISOU 663 C VAL A 86 3962 3687 4047 -171 -37 -89 ATOM 664 O VAL A 86 -13.184 9.120 -38.973 1.00 27.96 O ANISOU 664 O VAL A 86 3619 3300 3704 -170 -62 -102 ATOM 665 CB VAL A 86 -11.182 10.969 -37.307 1.00 22.35 C ANISOU 665 CB VAL A 86 2886 2644 2963 -135 -10 -102 ATOM 666 CG1 VAL A 86 -10.722 11.593 -38.641 1.00 36.01 C ANISOU 666 CG1 VAL A 86 4614 4396 4672 -133 -6 -128 ATOM 667 CG2 VAL A 86 -10.751 11.900 -36.158 1.00 24.67 C ANISOU 667 CG2 VAL A 86 3167 2959 3248 -130 12 -84 ATOM 668 N LEU A 87 -14.001 11.239 -39.126 1.00 28.49 N ANISOU 668 N LEU A 87 3663 3420 3743 -183 -27 -86 ATOM 669 CA LEU A 87 -14.457 11.238 -40.515 1.00 26.81 C ANISOU 669 CA LEU A 87 3455 3207 3524 -194 -37 -102 ATOM 670 C LEU A 87 -13.326 11.723 -41.428 1.00 22.41 C ANISOU 670 C LEU A 87 2896 2677 2942 -181 -28 -133 ATOM 671 O LEU A 87 -12.652 12.696 -41.096 1.00 23.69 O ANISOU 671 O LEU A 87 3048 2864 3089 -175 -11 -130 ATOM 672 CB LEU A 87 -15.663 12.197 -40.663 1.00 36.83 C ANISOU 672 CB LEU A 87 4714 4488 4792 -216 -34 -80 ATOM 673 CG LEU A 87 -17.028 11.492 -40.726 1.00 40.58 C ANISOU 673 CG LEU A 87 5188 4946 5284 -238 -49 -58 ATOM 674 CD1 LEU A 87 -18.162 12.533 -40.677 1.00 43.63 C ANISOU 674 CD1 LEU A 87 5560 5353 5663 -252 -42 -45 ATOM 675 CD2 LEU A 87 -17.144 10.562 -41.953 1.00 46.92 C ANISOU 675 CD2 LEU A 87 6009 5722 6096 -243 -73 -74 ATOM 676 N LYS A 88 -13.192 11.065 -42.585 1.00 22.86 N ANISOU 676 N LYS A 88 2962 2731 2994 -178 -42 -162 ATOM 677 CA LYS A 88 -12.261 11.402 -43.656 1.00 21.99 C ANISOU 677 CA LYS A 88 2847 2656 2854 -170 -36 -192 ATOM 678 C LYS A 88 -13.099 11.640 -44.912 1.00 19.88 C ANISOU 678 C LYS A 88 2579 2399 2575 -192 -43 -194 ATOM 679 O LYS A 88 -13.639 10.685 -45.466 1.00 22.81 O ANISOU 679 O LYS A 88 2962 2747 2958 -195 -63 -206 ATOM 680 CB LYS A 88 -11.258 10.244 -43.831 1.00 23.88 C ANISOU 680 CB LYS A 88 3093 2890 3090 -141 -47 -233 ATOM 681 CG LYS A 88 -10.294 10.133 -42.637 1.00 27.86 C ANISOU 681 CG LYS A 88 3594 3394 3599 -118 -37 -234 ATOM 682 CD LYS A 88 -9.502 8.823 -42.564 1.00 38.78 C ANISOU 682 CD LYS A 88 4988 4748 4997 -92 -59 -264 ATOM 683 CE LYS A 88 -8.468 8.636 -43.681 1.00 41.45 C ANISOU 683 CE LYS A 88 5317 5121 5310 -63 -54 -308 ATOM 684 NZ LYS A 88 -7.692 7.402 -43.468 1.00 44.77 N1+ ANISOU 684 NZ LYS A 88 5750 5505 5754 -33 -78 -334 ATOM 685 N LEU A 89 -13.215 12.914 -45.310 1.00 26.54 N ANISOU 685 N LEU A 89 3410 3275 3399 -207 -32 -182 ATOM 686 CA LEU A 89 -13.990 13.352 -46.464 1.00 27.99 C ANISOU 686 CA LEU A 89 3592 3470 3571 -231 -40 -180 ATOM 687 C LEU A 89 -13.005 13.674 -47.591 1.00 27.33 C ANISOU 687 C LEU A 89 3500 3434 3450 -230 -36 -206 ATOM 688 O LEU A 89 -12.349 14.714 -47.533 1.00 20.20 O ANISOU 688 O LEU A 89 2585 2563 2528 -230 -23 -200 ATOM 689 CB LEU A 89 -14.835 14.597 -46.090 1.00 22.77 C ANISOU 689 CB LEU A 89 2924 2810 2917 -253 -37 -144 ATOM 690 CG LEU A 89 -15.768 14.424 -44.871 1.00 28.23 C ANISOU 690 CG LEU A 89 3617 3470 3639 -252 -38 -119 ATOM 691 CD1 LEU A 89 -16.437 15.766 -44.506 1.00 30.77 C ANISOU 691 CD1 LEU A 89 3927 3800 3963 -266 -36 -92 ATOM 692 CD2 LEU A 89 -16.792 13.292 -45.084 1.00 29.16 C ANISOU 692 CD2 LEU A 89 3746 3557 3776 -260 -54 -119 ATOM 693 N LYS A 90 -12.912 12.786 -48.596 1.00 24.21 N ANISOU 693 N LYS A 90 3110 3044 3043 -227 -48 -237 ATOM 694 CA LYS A 90 -12.169 13.070 -49.822 1.00 20.63 C ANISOU 694 CA LYS A 90 2644 2646 2549 -228 -44 -263 ATOM 695 C LYS A 90 -12.923 14.129 -50.643 1.00 21.54 C ANISOU 695 C LYS A 90 2753 2785 2648 -265 -47 -238 ATOM 696 O LYS A 90 -14.094 13.922 -50.954 1.00 25.68 O ANISOU 696 O LYS A 90 3287 3281 3190 -283 -60 -224 ATOM 697 CB LYS A 90 -11.904 11.776 -50.621 1.00 30.74 C ANISOU 697 CB LYS A 90 3932 3928 3821 -207 -58 -312 ATOM 698 CG LYS A 90 -11.127 12.013 -51.937 1.00 39.80 C ANISOU 698 CG LYS A 90 5060 5146 4918 -206 -52 -342 ATOM 699 CD LYS A 90 -10.763 10.716 -52.681 1.00 52.82 C ANISOU 699 CD LYS A 90 6713 6801 6556 -175 -67 -401 ATOM 700 CE LYS A 90 -9.425 10.107 -52.239 1.00 64.41 C ANISOU 700 CE LYS A 90 8165 8301 8006 -137 -56 -436 ATOM 701 NZ LYS A 90 -8.283 10.857 -52.788 1.00 57.63 N1+ ANISOU 701 NZ LYS A 90 7275 7530 7090 -144 -40 -451 ATOM 702 N VAL A 91 -12.230 15.227 -50.965 1.00 24.95 N ANISOU 702 N VAL A 91 3167 3266 3048 -279 -38 -228 ATOM 703 CA VAL A 91 -12.718 16.323 -51.798 1.00 24.59 C ANISOU 703 CA VAL A 91 3114 3240 2988 -318 -47 -199 ATOM 704 C VAL A 91 -11.983 16.327 -53.154 1.00 31.77 C ANISOU 704 C VAL A 91 4007 4215 3848 -330 -47 -220 ATOM 705 O VAL A 91 -10.940 15.689 -53.280 1.00 30.34 O ANISOU 705 O VAL A 91 3816 4069 3641 -307 -37 -255 ATOM 706 CB VAL A 91 -12.520 17.693 -51.089 1.00 26.64 C ANISOU 706 CB VAL A 91 3368 3500 3256 -333 -45 -159 ATOM 707 CG1 VAL A 91 -13.506 17.869 -49.920 1.00 21.84 C ANISOU 707 CG1 VAL A 91 2772 2833 2693 -323 -47 -139 ATOM 708 CG2 VAL A 91 -11.080 17.962 -50.614 1.00 23.47 C ANISOU 708 CG2 VAL A 91 2951 3134 2832 -322 -32 -162 ATOM 709 N ASP A 92 -12.558 17.003 -54.165 1.00 23.34 N ANISOU 709 N ASP A 92 2935 3167 2764 -367 -60 -199 ATOM 710 CA ASP A 92 -12.026 17.030 -55.539 1.00 30.56 C ANISOU 710 CA ASP A 92 3834 4149 3629 -384 -62 -217 ATOM 711 C ASP A 92 -10.776 17.920 -55.713 1.00 32.61 C ANISOU 711 C ASP A 92 4069 4472 3850 -405 -57 -197 ATOM 712 O ASP A 92 -10.110 17.809 -56.743 1.00 28.28 O ANISOU 712 O ASP A 92 3501 3991 3253 -423 -58 -208 ATOM 713 CB ASP A 92 -13.090 17.408 -56.603 1.00 27.43 C ANISOU 713 CB ASP A 92 3443 3747 3231 -416 -81 -204 ATOM 714 CG ASP A 92 -13.796 18.762 -56.439 1.00 34.62 C ANISOU 714 CG ASP A 92 4354 4648 4153 -456 -96 -152 ATOM 715 OD1 ASP A 92 -13.456 19.524 -55.505 1.00 38.97 O ANISOU 715 OD1 ASP A 92 4899 5195 4712 -459 -94 -125 ATOM 716 OD2 ASP A 92 -14.675 19.026 -57.287 1.00 43.21 O1- ANISOU 716 OD2 ASP A 92 5446 5729 5242 -483 -113 -138 ATOM 717 N THR A 93 -10.504 18.794 -54.733 1.00 27.85 N ANISOU 717 N THR A 93 3466 3852 3265 -404 -53 -169 ATOM 718 CA THR A 93 -9.434 19.781 -54.780 1.00 29.33 C ANISOU 718 CA THR A 93 3631 4094 3419 -425 -51 -146 ATOM 719 C THR A 93 -8.457 19.514 -53.627 1.00 30.96 C ANISOU 719 C THR A 93 3835 4292 3637 -390 -34 -156 ATOM 720 O THR A 93 -8.874 19.485 -52.468 1.00 22.78 O ANISOU 720 O THR A 93 2817 3195 2645 -370 -31 -149 ATOM 721 CB THR A 93 -10.006 21.214 -54.620 1.00 27.27 C ANISOU 721 CB THR A 93 3372 3818 3170 -467 -75 -91 ATOM 722 OG1 THR A 93 -10.947 21.454 -55.650 1.00 32.88 O ANISOU 722 OG1 THR A 93 4088 4526 3878 -497 -94 -81 ATOM 723 CG2 THR A 93 -8.958 22.340 -54.686 1.00 27.72 C ANISOU 723 CG2 THR A 93 3406 3937 3189 -498 -81 -63 ATOM 724 N ALA A 94 -7.170 19.348 -53.967 1.00 25.01 N ANISOU 724 N ALA A 94 3058 3605 2841 -384 -21 -174 ATOM 725 CA ALA A 94 -6.088 19.270 -52.993 1.00 29.83 C ANISOU 725 CA ALA A 94 3662 4216 3457 -356 -6 -180 ATOM 726 C ALA A 94 -5.733 20.672 -52.486 1.00 18.82 C ANISOU 726 C ALA A 94 2261 2825 2064 -387 -16 -129 ATOM 727 O ALA A 94 -5.668 21.597 -53.296 1.00 21.25 O ANISOU 727 O ALA A 94 2555 3175 2342 -431 -32 -97 ATOM 728 CB ALA A 94 -4.869 18.587 -53.626 1.00 26.79 C ANISOU 728 CB ALA A 94 3249 3905 3024 -336 10 -221 ATOM 729 N ASN A 95 -5.504 20.804 -51.167 1.00 18.28 N ANISOU 729 N ASN A 95 2204 2712 2029 -363 -10 -122 ATOM 730 CA ASN A 95 -5.141 22.064 -50.517 1.00 15.05 C ANISOU 730 CA ASN A 95 1794 2300 1627 -386 -23 -78 ATOM 731 C ASN A 95 -3.768 22.546 -51.036 1.00 14.00 C ANISOU 731 C ASN A 95 1631 2247 1444 -410 -22 -66 ATOM 732 O ASN A 95 -2.777 21.858 -50.782 1.00 23.29 O ANISOU 732 O ASN A 95 2792 3453 2603 -383 -2 -90 ATOM 733 CB ASN A 95 -5.128 21.852 -48.981 1.00 19.87 C ANISOU 733 CB ASN A 95 2420 2853 2278 -351 -13 -80 ATOM 734 CG ASN A 95 -4.854 23.122 -48.157 1.00 17.44 C ANISOU 734 CG ASN A 95 2114 2532 1982 -370 -31 -38 ATOM 735 OD1 ASN A 95 -4.843 24.236 -48.676 1.00 17.62 O ANISOU 735 OD1 ASN A 95 2125 2588 1982 -411 -52 -6 ATOM 736 ND2 ASN A 95 -4.636 22.966 -46.854 1.00 22.23 N ANISOU 736 ND2 ASN A 95 2734 3089 2624 -342 -25 -38 ATOM 737 N PRO A 96 -3.722 23.707 -51.735 1.00 20.82 N ANISOU 737 N PRO A 96 2482 3146 2283 -461 -46 -25 ATOM 738 CA PRO A 96 -2.447 24.266 -52.221 1.00 23.02 C ANISOU 738 CA PRO A 96 2729 3506 2512 -489 -48 -5 ATOM 739 C PRO A 96 -1.513 24.783 -51.106 1.00 29.09 C ANISOU 739 C PRO A 96 3497 4263 3293 -478 -47 12 ATOM 740 O PRO A 96 -0.345 25.042 -51.391 1.00 22.63 O ANISOU 740 O PRO A 96 2651 3514 2435 -495 -44 24 ATOM 741 CB PRO A 96 -2.892 25.385 -53.177 1.00 23.24 C ANISOU 741 CB PRO A 96 2752 3557 2522 -552 -84 44 ATOM 742 CG PRO A 96 -4.212 25.871 -52.601 1.00 26.14 C ANISOU 742 CG PRO A 96 3153 3835 2945 -551 -106 59 ATOM 743 CD PRO A 96 -4.846 24.593 -52.065 1.00 25.63 C ANISOU 743 CD PRO A 96 3108 3717 2914 -496 -78 11 ATOM 744 N LYS A 97 -2.033 24.900 -49.871 1.00 26.37 N ANISOU 744 N LYS A 97 3180 3839 3002 -452 -49 14 ATOM 745 CA LYS A 97 -1.318 25.346 -48.681 1.00 28.69 C ANISOU 745 CA LYS A 97 3474 4117 3308 -441 -50 30 ATOM 746 C LYS A 97 -0.993 24.193 -47.711 1.00 23.30 C ANISOU 746 C LYS A 97 2798 3412 2644 -385 -17 -11 ATOM 747 O LYS A 97 -0.649 24.492 -46.568 1.00 26.85 O ANISOU 747 O LYS A 97 3256 3829 3118 -368 -16 -3 ATOM 748 CB LYS A 97 -2.149 26.440 -47.976 1.00 24.78 C ANISOU 748 CB LYS A 97 3004 3554 2857 -454 -82 66 ATOM 749 CG LYS A 97 -2.359 27.704 -48.821 1.00 37.90 C ANISOU 749 CG LYS A 97 4660 5236 4504 -512 -124 114 ATOM 750 CD LYS A 97 -3.039 28.818 -48.015 1.00 42.19 C ANISOU 750 CD LYS A 97 5227 5711 5092 -520 -162 144 ATOM 751 CE LYS A 97 -3.307 30.064 -48.867 1.00 47.80 C ANISOU 751 CE LYS A 97 5935 6436 5792 -578 -210 191 ATOM 752 NZ LYS A 97 -3.974 31.112 -48.076 1.00 57.45 N1+ ANISOU 752 NZ LYS A 97 7182 7584 7063 -579 -252 211 ATOM 753 N THR A 98 -1.074 22.918 -48.148 1.00 20.43 N ANISOU 753 N THR A 98 2429 3063 2270 -357 6 -56 ATOM 754 CA THR A 98 -0.692 21.760 -47.324 1.00 20.80 C ANISOU 754 CA THR A 98 2482 3084 2336 -305 30 -96 ATOM 755 C THR A 98 0.808 21.839 -46.955 1.00 24.25 C ANISOU 755 C THR A 98 2898 3566 2750 -296 40 -95 ATOM 756 O THR A 98 1.637 21.775 -47.866 1.00 25.20 O ANISOU 756 O THR A 98 2987 3766 2822 -307 46 -104 ATOM 757 CB THR A 98 -0.882 20.399 -48.056 1.00 25.61 C ANISOU 757 CB THR A 98 3089 3706 2934 -279 43 -145 ATOM 758 OG1 THR A 98 -2.226 20.233 -48.421 1.00 19.07 O ANISOU 758 OG1 THR A 98 2283 2834 2130 -288 32 -143 ATOM 759 CG2 THR A 98 -0.508 19.166 -47.206 1.00 23.03 C ANISOU 759 CG2 THR A 98 2771 3349 2631 -227 60 -184 ATOM 760 N PRO A 99 1.143 22.003 -45.652 1.00 20.83 N ANISOU 760 N PRO A 99 2476 3092 2347 -274 44 -88 ATOM 761 CA PRO A 99 2.548 21.983 -45.221 1.00 21.38 C ANISOU 761 CA PRO A 99 2525 3202 2395 -263 55 -90 ATOM 762 C PRO A 99 3.107 20.552 -45.263 1.00 23.75 C ANISOU 762 C PRO A 99 2816 3516 2690 -216 78 -143 ATOM 763 O PRO A 99 2.336 19.598 -45.368 1.00 25.82 O ANISOU 763 O PRO A 99 3096 3741 2975 -190 82 -175 ATOM 764 CB PRO A 99 2.465 22.523 -43.781 1.00 29.73 C ANISOU 764 CB PRO A 99 3604 4199 3492 -256 48 -64 ATOM 765 CG PRO A 99 1.131 22.013 -43.261 1.00 25.91 C ANISOU 765 CG PRO A 99 3151 3642 3053 -233 49 -79 ATOM 766 CD PRO A 99 0.239 22.079 -44.498 1.00 23.15 C ANISOU 766 CD PRO A 99 2802 3302 2692 -258 39 -79 ATOM 767 N LYS A 100 4.429 20.412 -45.086 1.00 28.47 N ANISOU 767 N LYS A 100 3388 4167 3262 -204 89 -153 ATOM 768 CA LYS A 100 5.006 19.137 -44.655 1.00 27.04 C ANISOU 768 CA LYS A 100 3204 3984 3088 -151 106 -203 ATOM 769 C LYS A 100 4.437 18.789 -43.269 1.00 22.09 C ANISOU 769 C LYS A 100 2611 3268 2516 -126 105 -199 ATOM 770 O LYS A 100 4.403 19.662 -42.401 1.00 22.18 O ANISOU 770 O LYS A 100 2632 3250 2545 -141 99 -161 ATOM 771 CB LYS A 100 6.543 19.221 -44.645 1.00 20.68 C ANISOU 771 CB LYS A 100 2361 3251 2244 -143 116 -211 ATOM 772 CG LYS A 100 7.217 17.886 -44.276 1.00 26.11 C ANISOU 772 CG LYS A 100 3045 3933 2944 -86 128 -263 ATOM 773 CD LYS A 100 8.745 17.966 -44.287 1.00 44.95 C ANISOU 773 CD LYS A 100 5391 6397 5291 -77 139 -272 ATOM 774 CE LYS A 100 9.394 16.608 -43.986 1.00 48.98 C ANISOU 774 CE LYS A 100 5895 6903 5812 -15 147 -332 ATOM 775 NZ LYS A 100 10.860 16.719 -43.970 1.00 53.69 N1+ ANISOU 775 NZ LYS A 100 6448 7584 6367 -4 157 -345 ATOM 776 N TYR A 101 3.941 17.557 -43.112 1.00 22.17 N ANISOU 776 N TYR A 101 2638 3234 2553 -89 108 -237 ATOM 777 CA TYR A 101 3.224 17.161 -41.908 1.00 23.94 C ANISOU 777 CA TYR A 101 2893 3377 2826 -73 105 -228 ATOM 778 C TYR A 101 3.401 15.671 -41.624 1.00 26.17 C ANISOU 778 C TYR A 101 3184 3631 3130 -27 106 -272 ATOM 779 O TYR A 101 3.780 14.903 -42.509 1.00 29.50 O ANISOU 779 O TYR A 101 3592 4086 3532 -7 106 -315 ATOM 780 CB TYR A 101 1.727 17.559 -42.026 1.00 18.33 C ANISOU 780 CB TYR A 101 2207 2619 2140 -96 95 -205 ATOM 781 CG TYR A 101 0.832 16.606 -42.809 1.00 20.27 C ANISOU 781 CG TYR A 101 2459 2854 2388 -87 90 -236 ATOM 782 CD1 TYR A 101 0.689 16.747 -44.205 1.00 21.84 C ANISOU 782 CD1 TYR A 101 2643 3102 2553 -108 88 -244 ATOM 783 CD2 TYR A 101 0.170 15.548 -42.148 1.00 19.72 C ANISOU 783 CD2 TYR A 101 2411 2726 2354 -60 86 -256 ATOM 784 CE1 TYR A 101 -0.095 15.836 -44.936 1.00 28.12 C ANISOU 784 CE1 TYR A 101 3447 3886 3352 -99 82 -276 ATOM 785 CE2 TYR A 101 -0.590 14.618 -42.881 1.00 27.10 C ANISOU 785 CE2 TYR A 101 3356 3647 3296 -53 77 -284 ATOM 786 CZ TYR A 101 -0.730 14.767 -44.275 1.00 31.73 C ANISOU 786 CZ TYR A 101 3929 4280 3849 -70 76 -296 ATOM 787 OH TYR A 101 -1.483 13.878 -44.984 1.00 33.67 O ANISOU 787 OH TYR A 101 4185 4507 4102 -61 65 -326 ATOM 788 N LYS A 102 3.020 15.296 -40.398 1.00 27.91 N ANISOU 788 N LYS A 102 3426 3789 3390 -11 104 -262 ATOM 789 CA LYS A 102 2.794 13.915 -39.995 1.00 21.49 C ANISOU 789 CA LYS A 102 2629 2928 2607 22 96 -294 ATOM 790 C LYS A 102 1.836 13.880 -38.799 1.00 19.29 C ANISOU 790 C LYS A 102 2378 2581 2369 16 90 -264 ATOM 791 O LYS A 102 1.626 14.895 -38.134 1.00 19.80 O ANISOU 791 O LYS A 102 2448 2639 2438 -8 95 -225 ATOM 792 CB LYS A 102 4.139 13.190 -39.763 1.00 34.75 C ANISOU 792 CB LYS A 102 4296 4622 4284 60 97 -326 ATOM 793 CG LYS A 102 5.027 13.753 -38.640 1.00 36.46 C ANISOU 793 CG LYS A 102 4505 4850 4499 59 106 -300 ATOM 794 CD LYS A 102 6.481 13.282 -38.806 1.00 47.09 C ANISOU 794 CD LYS A 102 5823 6249 5821 88 111 -335 ATOM 795 CE LYS A 102 7.390 13.611 -37.616 1.00 49.55 C ANISOU 795 CE LYS A 102 6134 6545 6146 102 115 -320 ATOM 796 NZ LYS A 102 7.092 12.754 -36.455 1.00 60.05 N1+ ANISOU 796 NZ LYS A 102 7487 7809 7519 133 100 -337 ATOM 797 N PHE A 103 1.251 12.697 -38.577 1.00 16.89 N ANISOU 797 N PHE A 103 2092 2230 2094 36 77 -282 ATOM 798 CA PHE A 103 0.346 12.415 -37.469 1.00 21.50 C ANISOU 798 CA PHE A 103 2698 2754 2715 30 70 -256 ATOM 799 C PHE A 103 1.119 11.611 -36.421 1.00 28.33 C ANISOU 799 C PHE A 103 3570 3594 3602 56 65 -262 ATOM 800 O PHE A 103 1.657 10.553 -36.748 1.00 24.22 O ANISOU 800 O PHE A 103 3049 3069 3087 85 52 -298 ATOM 801 CB PHE A 103 -0.874 11.624 -37.992 1.00 19.50 C ANISOU 801 CB PHE A 103 2463 2465 2482 26 53 -265 ATOM 802 CG PHE A 103 -1.751 12.314 -39.031 1.00 16.70 C ANISOU 802 CG PHE A 103 2106 2127 2112 -2 56 -257 ATOM 803 CD1 PHE A 103 -1.821 13.722 -39.130 1.00 19.52 C ANISOU 803 CD1 PHE A 103 2452 2516 2448 -27 69 -231 ATOM 804 CD2 PHE A 103 -2.648 11.541 -39.799 1.00 18.20 C ANISOU 804 CD2 PHE A 103 2307 2298 2311 -2 40 -276 ATOM 805 CE1 PHE A 103 -2.715 14.323 -40.004 1.00 20.63 C ANISOU 805 CE1 PHE A 103 2592 2670 2577 -53 66 -223 ATOM 806 CE2 PHE A 103 -3.532 12.160 -40.673 1.00 18.40 C ANISOU 806 CE2 PHE A 103 2332 2338 2324 -28 41 -268 ATOM 807 CZ PHE A 103 -3.563 13.545 -40.778 1.00 25.72 C ANISOU 807 CZ PHE A 103 3247 3296 3230 -54 54 -241 ATOM 808 N VAL A 104 1.163 12.137 -35.188 1.00 28.12 N ANISOU 808 N VAL A 104 3549 3548 3588 48 71 -228 ATOM 809 CA VAL A 104 1.826 11.506 -34.048 1.00 22.86 C ANISOU 809 CA VAL A 104 2888 2856 2941 69 64 -228 ATOM 810 C VAL A 104 0.843 11.405 -32.874 1.00 29.59 C ANISOU 810 C VAL A 104 3756 3666 3819 54 60 -193 ATOM 811 O VAL A 104 0.026 12.302 -32.681 1.00 23.96 O ANISOU 811 O VAL A 104 3044 2955 3103 30 68 -166 ATOM 812 CB VAL A 104 3.073 12.318 -33.583 1.00 25.62 C ANISOU 812 CB VAL A 104 3222 3241 3274 78 79 -223 ATOM 813 CG1 VAL A 104 4.115 12.446 -34.707 1.00 36.18 C ANISOU 813 CG1 VAL A 104 4536 4633 4576 86 86 -253 ATOM 814 CG2 VAL A 104 2.787 13.702 -32.964 1.00 39.65 C ANISOU 814 CG2 VAL A 104 4998 5023 5044 53 92 -184 ATOM 815 N ARG A 105 0.962 10.328 -32.086 1.00 30.91 N ANISOU 815 N ARG A 105 3935 3798 4012 68 44 -193 ATOM 816 CA ARG A 105 0.251 10.189 -30.822 1.00 26.15 C ANISOU 816 CA ARG A 105 3342 3163 3429 53 39 -157 ATOM 817 C ARG A 105 1.219 10.569 -29.695 1.00 23.75 C ANISOU 817 C ARG A 105 3034 2867 3123 62 49 -143 ATOM 818 O ARG A 105 2.165 9.823 -29.437 1.00 29.93 O ANISOU 818 O ARG A 105 3816 3644 3913 85 39 -161 ATOM 819 CB ARG A 105 -0.326 8.767 -30.691 1.00 19.42 C ANISOU 819 CB ARG A 105 2506 2264 2607 56 8 -159 ATOM 820 CG ARG A 105 -1.164 8.572 -29.417 1.00 28.24 C ANISOU 820 CG ARG A 105 3632 3357 3741 35 2 -117 ATOM 821 CD ARG A 105 -1.794 7.181 -29.331 1.00 26.73 C ANISOU 821 CD ARG A 105 3456 3119 3579 28 -34 -113 ATOM 822 NE ARG A 105 -2.695 7.064 -28.177 1.00 32.02 N ANISOU 822 NE ARG A 105 4129 3778 4259 0 -38 -67 ATOM 823 CZ ARG A 105 -3.983 7.440 -28.136 1.00 22.15 C ANISOU 823 CZ ARG A 105 2876 2534 3005 -27 -33 -42 ATOM 824 NH1 ARG A 105 -4.602 7.966 -29.200 1.00 22.89 N ANISOU 824 NH1 ARG A 105 2968 2641 3089 -32 -25 -56 ATOM 825 NH2 ARG A 105 -4.665 7.270 -26.999 1.00 24.11 N1+ ANISOU 825 NH2 ARG A 105 3122 2782 3258 -51 -37 -1 ATOM 826 N ILE A 106 0.982 11.736 -29.073 1.00 27.20 N ANISOU 826 N ILE A 106 3467 3318 3550 46 65 -113 ATOM 827 CA ILE A 106 1.817 12.254 -27.990 1.00 23.88 C ANISOU 827 CA ILE A 106 3041 2907 3124 54 74 -101 ATOM 828 C ILE A 106 1.593 11.517 -26.660 1.00 25.30 C ANISOU 828 C ILE A 106 3230 3057 3325 53 62 -79 ATOM 829 O ILE A 106 0.493 11.044 -26.379 1.00 24.72 O ANISOU 829 O ILE A 106 3166 2958 3268 40 48 -67 ATOM 830 CB ILE A 106 1.607 13.773 -27.739 1.00 17.03 C ANISOU 830 CB ILE A 106 2165 2068 2237 42 92 -84 ATOM 831 CG1 ILE A 106 0.128 14.179 -27.532 1.00 18.92 C ANISOU 831 CG1 ILE A 106 2408 2299 2481 22 92 -61 ATOM 832 CG2 ILE A 106 2.308 14.599 -28.833 1.00 32.09 C ANISOU 832 CG2 ILE A 106 4062 4007 4124 41 98 -102 ATOM 833 CD1 ILE A 106 -0.043 15.589 -26.964 1.00 38.62 C ANISOU 833 CD1 ILE A 106 4897 4816 4961 15 103 -48 ATOM 834 N GLN A 107 2.662 11.466 -25.858 1.00 29.78 N ANISOU 834 N GLN A 107 3795 3629 3892 64 66 -73 ATOM 835 CA GLN A 107 2.645 10.937 -24.500 1.00 30.12 C ANISOU 835 CA GLN A 107 3845 3650 3950 63 55 -50 ATOM 836 C GLN A 107 2.047 11.966 -23.520 1.00 22.45 C ANISOU 836 C GLN A 107 2868 2696 2965 48 71 -21 ATOM 837 O GLN A 107 2.185 13.168 -23.757 1.00 20.88 O ANISOU 837 O GLN A 107 2661 2524 2747 49 87 -24 ATOM 838 CB GLN A 107 4.097 10.591 -24.098 1.00 43.16 C ANISOU 838 CB GLN A 107 5494 5299 5606 86 49 -65 ATOM 839 CG GLN A 107 4.745 9.452 -24.913 1.00 51.69 C ANISOU 839 CG GLN A 107 6577 6363 6701 109 30 -101 ATOM 840 CD GLN A 107 4.015 8.117 -24.760 1.00 51.49 C ANISOU 840 CD GLN A 107 6568 6291 6706 106 -3 -94 ATOM 841 OE1 GLN A 107 3.157 7.772 -25.571 1.00 60.43 O ANISOU 841 OE1 GLN A 107 7706 7400 7854 107 -20 -77 ATOM 842 NE2 GLN A 107 4.351 7.363 -23.711 1.00 50.45 N ANISOU 842 NE2 GLN A 107 6444 6143 6584 99 -17 -105 ATOM 843 N PRO A 108 1.439 11.497 -22.407 1.00 26.30 N ANISOU 843 N PRO A 108 3360 3171 3462 33 62 6 ATOM 844 CA PRO A 108 1.102 12.385 -21.281 1.00 30.85 C ANISOU 844 CA PRO A 108 3929 3769 4024 24 75 31 ATOM 845 C PRO A 108 2.352 13.044 -20.666 1.00 20.67 C ANISOU 845 C PRO A 108 2636 2495 2724 40 85 26 ATOM 846 O PRO A 108 3.396 12.401 -20.545 1.00 26.43 O ANISOU 846 O PRO A 108 3369 3211 3463 54 77 17 ATOM 847 CB PRO A 108 0.347 11.476 -20.302 1.00 37.73 C ANISOU 847 CB PRO A 108 4803 4625 4908 8 59 61 ATOM 848 CG PRO A 108 0.817 10.067 -20.620 1.00 37.90 C ANISOU 848 CG PRO A 108 4835 4613 4951 2 36 55 ATOM 849 CD PRO A 108 1.107 10.102 -22.114 1.00 23.27 C ANISOU 849 CD PRO A 108 2986 2752 3103 26 35 16 ATOM 850 N GLY A 109 2.216 14.341 -20.362 1.00 23.27 N ANISOU 850 N GLY A 109 2958 2849 3034 39 100 30 ATOM 851 CA GLY A 109 3.279 15.222 -19.890 1.00 20.47 C ANISOU 851 CA GLY A 109 2601 2508 2670 52 106 27 ATOM 852 C GLY A 109 3.843 16.088 -21.028 1.00 27.02 C ANISOU 852 C GLY A 109 3426 3351 3489 58 111 8 ATOM 853 O GLY A 109 4.472 17.104 -20.736 1.00 25.84 O ANISOU 853 O GLY A 109 3273 3216 3327 63 115 9 ATOM 854 N GLN A 110 3.612 15.721 -22.304 1.00 20.19 N ANISOU 854 N GLN A 110 2562 2483 2627 56 110 -9 ATOM 855 CA GLN A 110 4.025 16.498 -23.477 1.00 27.39 C ANISOU 855 CA GLN A 110 3468 3414 3526 56 113 -23 ATOM 856 C GLN A 110 3.053 17.643 -23.769 1.00 19.20 C ANISOU 856 C GLN A 110 2428 2388 2479 43 115 -17 ATOM 857 O GLN A 110 1.885 17.577 -23.389 1.00 21.19 O ANISOU 857 O GLN A 110 2683 2634 2736 36 115 -9 ATOM 858 CB GLN A 110 4.146 15.578 -24.709 1.00 30.43 C ANISOU 858 CB GLN A 110 3851 3796 3914 60 110 -46 ATOM 859 CG GLN A 110 5.202 14.467 -24.565 1.00 52.83 C ANISOU 859 CG GLN A 110 6688 6624 6762 78 103 -60 ATOM 860 CD GLN A 110 6.611 14.999 -24.298 1.00 69.11 C ANISOU 860 CD GLN A 110 8742 8705 8814 89 108 -59 ATOM 861 OE1 GLN A 110 7.228 15.612 -25.167 1.00 86.67 O ANISOU 861 OE1 GLN A 110 10970 10918 11044 93 106 -44 ATOM 862 NE2 GLN A 110 7.123 14.763 -23.090 1.00 64.73 N ANISOU 862 NE2 GLN A 110 8173 8181 8240 90 113 -72 ATOM 863 N THR A 111 3.580 18.666 -24.454 1.00 21.02 N ANISOU 863 N THR A 111 2654 2637 2696 39 113 -22 ATOM 864 CA THR A 111 2.902 19.923 -24.745 1.00 26.85 C ANISOU 864 CA THR A 111 3392 3383 3428 27 107 -16 ATOM 865 C THR A 111 2.790 20.155 -26.259 1.00 28.29 C ANISOU 865 C THR A 111 3570 3575 3602 14 104 -25 ATOM 866 O THR A 111 3.522 19.557 -27.045 1.00 25.30 O ANISOU 866 O THR A 111 3186 3208 3218 16 107 -37 ATOM 867 CB THR A 111 3.697 21.102 -24.135 1.00 29.91 C ANISOU 867 CB THR A 111 3778 3780 3806 28 99 -7 ATOM 868 OG1 THR A 111 5.009 21.112 -24.658 1.00 26.27 O ANISOU 868 OG1 THR A 111 3311 3335 3336 28 99 -9 ATOM 869 CG2 THR A 111 3.744 21.090 -22.598 1.00 31.51 C ANISOU 869 CG2 THR A 111 3984 3974 4012 41 100 2 ATOM 870 N PHE A 112 1.838 21.024 -26.622 1.00 20.71 N ANISOU 870 N PHE A 112 2612 2615 2643 3 96 -22 ATOM 871 CA PHE A 112 1.457 21.323 -27.997 1.00 20.16 C ANISOU 871 CA PHE A 112 2539 2556 2565 -13 89 -26 ATOM 872 C PHE A 112 0.633 22.615 -28.027 1.00 20.92 C ANISOU 872 C PHE A 112 2638 2650 2662 -23 72 -17 ATOM 873 O PHE A 112 -0.040 22.941 -27.049 1.00 16.41 O ANISOU 873 O PHE A 112 2069 2067 2098 -14 68 -14 ATOM 874 CB PHE A 112 0.687 20.124 -28.600 1.00 16.77 C ANISOU 874 CB PHE A 112 2110 2118 2142 -15 96 -38 ATOM 875 CG PHE A 112 -0.613 19.733 -27.917 1.00 25.14 C ANISOU 875 CG PHE A 112 3176 3159 3218 -12 99 -34 ATOM 876 CD1 PHE A 112 -0.596 18.875 -26.795 1.00 26.66 C ANISOU 876 CD1 PHE A 112 3372 3338 3420 -1 105 -31 ATOM 877 CD2 PHE A 112 -1.832 20.322 -28.309 1.00 20.56 C ANISOU 877 CD2 PHE A 112 2595 2576 2639 -22 92 -32 ATOM 878 CE1 PHE A 112 -1.780 18.547 -26.153 1.00 25.51 C ANISOU 878 CE1 PHE A 112 3226 3182 3283 -4 106 -22 ATOM 879 CE2 PHE A 112 -3.007 19.965 -27.667 1.00 23.61 C ANISOU 879 CE2 PHE A 112 2982 2953 3036 -21 95 -27 ATOM 880 CZ PHE A 112 -2.979 19.079 -26.602 1.00 20.34 C ANISOU 880 CZ PHE A 112 2568 2530 2629 -13 102 -21 ATOM 881 N SER A 113 0.679 23.307 -29.173 1.00 13.38 N ANISOU 881 N SER A 113 1679 1706 1697 -42 60 -15 ATOM 882 CA SER A 113 -0.115 24.499 -29.446 1.00 19.72 C ANISOU 882 CA SER A 113 2485 2503 2504 -54 37 -7 ATOM 883 C SER A 113 -1.462 24.099 -30.041 1.00 17.01 C ANISOU 883 C SER A 113 2143 2151 2170 -59 39 -14 ATOM 884 O SER A 113 -1.482 23.319 -30.987 1.00 14.61 O ANISOU 884 O SER A 113 1836 1852 1862 -65 52 -22 ATOM 885 CB SER A 113 0.620 25.387 -30.458 1.00 14.42 C ANISOU 885 CB SER A 113 1810 1849 1820 -78 16 6 ATOM 886 OG SER A 113 1.795 25.873 -29.867 1.00 17.36 O ANISOU 886 OG SER A 113 2180 2233 2183 -78 12 16 ATOM 887 N VAL A 114 -2.543 24.679 -29.513 1.00 20.37 N ANISOU 887 N VAL A 114 2571 2564 2606 -56 24 -14 ATOM 888 CA VAL A 114 -3.899 24.543 -30.025 1.00 17.74 C ANISOU 888 CA VAL A 114 2237 2223 2280 -60 22 -19 ATOM 889 C VAL A 114 -4.263 25.828 -30.774 1.00 20.84 C ANISOU 889 C VAL A 114 2631 2612 2675 -76 -8 -13 ATOM 890 O VAL A 114 -4.182 26.898 -30.175 1.00 16.28 O ANISOU 890 O VAL A 114 2056 2027 2102 -71 -33 -9 ATOM 891 CB VAL A 114 -4.908 24.371 -28.854 1.00 24.19 C ANISOU 891 CB VAL A 114 3050 3033 3107 -40 30 -25 ATOM 892 CG1 VAL A 114 -6.389 24.490 -29.265 1.00 20.28 C ANISOU 892 CG1 VAL A 114 2552 2534 2620 -46 25 -29 ATOM 893 CG2 VAL A 114 -4.688 23.031 -28.137 1.00 29.23 C ANISOU 893 CG2 VAL A 114 3688 3673 3745 -30 56 -25 ATOM 894 N LEU A 115 -4.712 25.688 -32.032 1.00 18.82 N ANISOU 894 N LEU A 115 2375 2361 2417 -96 -11 -12 ATOM 895 CA LEU A 115 -5.360 26.759 -32.785 1.00 18.44 C ANISOU 895 CA LEU A 115 2328 2307 2373 -113 -42 -6 ATOM 896 C LEU A 115 -6.877 26.563 -32.641 1.00 17.40 C ANISOU 896 C LEU A 115 2194 2162 2256 -103 -42 -16 ATOM 897 O LEU A 115 -7.453 25.751 -33.361 1.00 25.67 O ANISOU 897 O LEU A 115 3240 3213 3303 -112 -28 -20 ATOM 898 CB LEU A 115 -4.871 26.730 -34.256 1.00 12.92 C ANISOU 898 CB LEU A 115 1627 1625 1658 -144 -46 4 ATOM 899 CG LEU A 115 -5.507 27.800 -35.178 1.00 15.66 C ANISOU 899 CG LEU A 115 1975 1965 2009 -168 -82 15 ATOM 900 CD1 LEU A 115 -5.087 29.230 -34.782 1.00 20.34 C ANISOU 900 CD1 LEU A 115 2572 2547 2608 -172 -119 29 ATOM 901 CD2 LEU A 115 -5.203 27.507 -36.655 1.00 16.08 C ANISOU 901 CD2 LEU A 115 2024 2044 2042 -200 -81 24 ATOM 902 N ALA A 116 -7.502 27.297 -31.707 1.00 14.94 N ANISOU 902 N ALA A 116 1881 1840 1957 -83 -58 -23 ATOM 903 CA ALA A 116 -8.955 27.315 -31.546 1.00 17.96 C ANISOU 903 CA ALA A 116 2255 2218 2349 -72 -57 -34 ATOM 904 C ALA A 116 -9.626 28.009 -32.740 1.00 21.35 C ANISOU 904 C ALA A 116 2687 2639 2787 -92 -83 -30 ATOM 905 O ALA A 116 -9.178 29.081 -33.146 1.00 27.80 O ANISOU 905 O ALA A 116 3510 3446 3605 -104 -117 -22 ATOM 906 CB ALA A 116 -9.325 28.006 -30.230 1.00 20.31 C ANISOU 906 CB ALA A 116 2548 2514 2656 -41 -68 -47 ATOM 907 N CYS A 117 -10.662 27.360 -33.288 1.00 16.95 N ANISOU 907 N CYS A 117 2125 2084 2233 -98 -71 -33 ATOM 908 CA CYS A 117 -11.370 27.762 -34.503 1.00 15.88 C ANISOU 908 CA CYS A 117 1990 1941 2103 -118 -95 -29 ATOM 909 C CYS A 117 -12.878 27.628 -34.274 1.00 15.25 C ANISOU 909 C CYS A 117 1899 1860 2036 -105 -95 -40 ATOM 910 O CYS A 117 -13.304 26.784 -33.487 1.00 17.17 O ANISOU 910 O CYS A 117 2132 2113 2277 -89 -69 -46 ATOM 911 CB CYS A 117 -10.982 26.876 -35.704 1.00 29.02 C ANISOU 911 CB CYS A 117 3658 3613 3754 -147 -83 -19 ATOM 912 SG CYS A 117 -9.239 27.073 -36.135 1.00 29.36 S ANISOU 912 SG CYS A 117 3709 3671 3777 -166 -84 -6 ATOM 913 N TYR A 118 -13.661 28.438 -35.002 1.00 21.22 N ANISOU 913 N TYR A 118 2655 2605 2803 -115 -127 -39 ATOM 914 CA TYR A 118 -15.123 28.381 -35.037 1.00 22.17 C ANISOU 914 CA TYR A 118 2763 2726 2936 -106 -131 -49 ATOM 915 C TYR A 118 -15.561 28.685 -36.468 1.00 17.04 C ANISOU 915 C TYR A 118 2120 2066 2290 -136 -152 -38 ATOM 916 O TYR A 118 -15.127 29.692 -37.024 1.00 21.84 O ANISOU 916 O TYR A 118 2737 2661 2899 -154 -185 -28 ATOM 917 CB TYR A 118 -15.742 29.397 -34.051 1.00 21.54 C ANISOU 917 CB TYR A 118 2672 2642 2869 -72 -158 -68 ATOM 918 CG TYR A 118 -15.339 29.161 -32.610 1.00 19.65 C ANISOU 918 CG TYR A 118 2426 2420 2621 -44 -135 -78 ATOM 919 CD1 TYR A 118 -14.227 29.841 -32.074 1.00 25.53 C ANISOU 919 CD1 TYR A 118 3181 3156 3364 -35 -148 -79 ATOM 920 CD2 TYR A 118 -16.017 28.202 -31.834 1.00 25.61 C ANISOU 920 CD2 TYR A 118 3164 3199 3368 -33 -101 -83 ATOM 921 CE1 TYR A 118 -13.753 29.520 -30.789 1.00 17.75 C ANISOU 921 CE1 TYR A 118 2189 2186 2368 -12 -125 -87 ATOM 922 CE2 TYR A 118 -15.558 27.898 -30.539 1.00 20.61 C ANISOU 922 CE2 TYR A 118 2523 2583 2723 -12 -80 -88 ATOM 923 CZ TYR A 118 -14.412 28.538 -30.027 1.00 21.32 C ANISOU 923 CZ TYR A 118 2624 2664 2812 -1 -91 -91 ATOM 924 OH TYR A 118 -13.930 28.201 -28.796 1.00 17.37 O ANISOU 924 OH TYR A 118 2118 2183 2301 18 -70 -95 ATOM 925 N ASN A 119 -16.405 27.811 -37.038 1.00 15.22 N ANISOU 925 N ASN A 119 1882 1840 2059 -146 -136 -38 ATOM 926 CA ASN A 119 -16.931 27.881 -38.411 1.00 22.42 C ANISOU 926 CA ASN A 119 2800 2746 2974 -175 -152 -28 ATOM 927 C ASN A 119 -15.806 27.882 -39.471 1.00 28.30 C ANISOU 927 C ASN A 119 3558 3491 3703 -206 -158 -13 ATOM 928 O ASN A 119 -15.897 28.601 -40.467 1.00 19.79 O ANISOU 928 O ASN A 119 2486 2407 2627 -230 -190 -2 ATOM 929 CB ASN A 119 -17.915 29.072 -38.599 1.00 26.58 C ANISOU 929 CB ASN A 119 3321 3257 3520 -170 -195 -33 ATOM 930 CG ASN A 119 -19.034 29.127 -37.555 1.00 32.77 C ANISOU 930 CG ASN A 119 4086 4049 4316 -137 -191 -51 ATOM 931 OD1 ASN A 119 -19.005 29.960 -36.651 1.00 41.09 O ANISOU 931 OD1 ASN A 119 5129 5116 5368 -138 -168 -52 ATOM 932 ND2 ASN A 119 -20.026 28.244 -37.674 1.00 35.17 N ANISOU 932 ND2 ASN A 119 4385 4348 4631 -107 -216 -67 ATOM 933 N GLY A 120 -14.744 27.097 -39.216 1.00 27.44 N ANISOU 933 N GLY A 120 3453 3396 3577 -206 -129 -12 ATOM 934 CA GLY A 120 -13.549 26.991 -40.053 1.00 19.89 C ANISOU 934 CA GLY A 120 2504 2451 2601 -232 -130 -1 ATOM 935 C GLY A 120 -12.600 28.197 -39.952 1.00 30.50 C ANISOU 935 C GLY A 120 3852 3794 3942 -239 -159 11 ATOM 936 O GLY A 120 -11.614 28.220 -40.688 1.00 20.97 O ANISOU 936 O GLY A 120 2648 2605 2715 -263 -161 24 ATOM 937 N SER A 121 -12.884 29.189 -39.088 1.00 22.15 N ANISOU 937 N SER A 121 2795 2718 2903 -218 -184 7 ATOM 938 CA SER A 121 -12.131 30.439 -38.975 1.00 23.60 C ANISOU 938 CA SER A 121 2985 2894 3088 -226 -220 21 ATOM 939 C SER A 121 -11.331 30.445 -37.653 1.00 23.86 C ANISOU 939 C SER A 121 3018 2928 3119 -199 -205 13 ATOM 940 O SER A 121 -11.960 30.394 -36.595 1.00 22.34 O ANISOU 940 O SER A 121 2820 2730 2938 -165 -192 -6 ATOM 941 CB SER A 121 -13.134 31.614 -38.988 1.00 27.42 C ANISOU 941 CB SER A 121 3471 3350 3596 -224 -273 22 ATOM 942 OG SER A 121 -13.704 31.762 -40.274 1.00 41.37 O ANISOU 942 OG SER A 121 5239 5115 5364 -254 -292 34 ATOM 943 N PRO A 122 -9.978 30.518 -37.723 1.00 32.39 N ANISOU 943 N PRO A 122 4102 4020 4184 -215 -209 28 ATOM 944 CA PRO A 122 -9.092 30.747 -36.556 1.00 28.41 C ANISOU 944 CA PRO A 122 3600 3515 3680 -190 -200 23 ATOM 945 C PRO A 122 -9.477 31.934 -35.650 1.00 32.81 C ANISOU 945 C PRO A 122 4161 4046 4260 -166 -238 14 ATOM 946 O PRO A 122 -9.696 33.039 -36.149 1.00 34.02 O ANISOU 946 O PRO A 122 4320 4179 4428 -177 -288 22 ATOM 947 CB PRO A 122 -7.703 30.937 -37.191 1.00 32.16 C ANISOU 947 CB PRO A 122 4076 4010 4133 -220 -205 46 ATOM 948 CG PRO A 122 -7.761 30.131 -38.475 1.00 51.40 C ANISOU 948 CG PRO A 122 6507 6472 6550 -250 -188 52 ATOM 949 CD PRO A 122 -9.187 30.360 -38.947 1.00 30.87 C ANISOU 949 CD PRO A 122 3909 3852 3967 -254 -208 49 ATOM 950 N SER A 123 -9.560 31.653 -34.340 1.00 21.30 N ANISOU 950 N SER A 123 2700 2588 2805 -130 -218 -4 ATOM 951 CA SER A 123 -9.905 32.599 -33.277 1.00 25.92 C ANISOU 951 CA SER A 123 3287 3153 3409 -100 -252 -20 ATOM 952 C SER A 123 -8.664 33.037 -32.479 1.00 22.46 C ANISOU 952 C SER A 123 2855 2715 2966 -88 -255 -18 ATOM 953 O SER A 123 -8.525 34.227 -32.197 1.00 22.91 O ANISOU 953 O SER A 123 2919 2749 3036 -78 -301 -20 ATOM 954 CB SER A 123 -10.965 31.945 -32.364 1.00 34.13 C ANISOU 954 CB SER A 123 4314 4198 4457 -64 -233 -48 ATOM 955 OG SER A 123 -11.281 32.748 -31.243 1.00 56.82 O ANISOU 955 OG SER A 123 7183 7076 7328 -30 -224 -65 ATOM 956 N GLY A 124 -7.793 32.081 -32.122 1.00 23.05 N ANISOU 956 N GLY A 124 2926 2809 3021 -88 -210 -14 ATOM 957 CA GLY A 124 -6.612 32.366 -31.318 1.00 23.19 C ANISOU 957 CA GLY A 124 2948 2828 3034 -75 -210 -12 ATOM 958 C GLY A 124 -5.792 31.088 -31.148 1.00 20.56 C ANISOU 958 C GLY A 124 2612 2519 2682 -82 -162 -5 ATOM 959 O GLY A 124 -6.255 29.989 -31.457 1.00 18.32 O ANISOU 959 O GLY A 124 2321 2249 2391 -87 -127 -8 ATOM 960 N VAL A 125 -4.563 31.260 -30.638 1.00 19.57 N ANISOU 960 N VAL A 125 2489 2397 2548 -81 -163 4 ATOM 961 CA VAL A 125 -3.606 30.185 -30.402 1.00 18.71 C ANISOU 961 CA VAL A 125 2377 2310 2423 -84 -123 9 ATOM 962 C VAL A 125 -3.079 30.248 -28.955 1.00 17.27 C ANISOU 962 C VAL A 125 2197 2125 2242 -56 -116 1 ATOM 963 O VAL A 125 -2.818 31.337 -28.439 1.00 16.85 O ANISOU 963 O VAL A 125 2150 2056 2196 -48 -150 2 ATOM 964 CB VAL A 125 -2.433 30.232 -31.426 1.00 25.02 C ANISOU 964 CB VAL A 125 3176 3126 3206 -119 -131 32 ATOM 965 CG1 VAL A 125 -1.503 31.454 -31.289 1.00 33.08 C ANISOU 965 CG1 VAL A 125 4204 4135 4230 -131 -177 50 ATOM 966 CG2 VAL A 125 -1.608 28.929 -31.436 1.00 26.34 C ANISOU 966 CG2 VAL A 125 3336 3318 3355 -117 -90 32 ATOM 967 N TYR A 126 -2.938 29.069 -28.329 1.00 24.54 N ANISOU 967 N TYR A 126 3112 3058 3155 -42 -74 -7 ATOM 968 CA TYR A 126 -2.454 28.912 -26.958 1.00 18.87 C ANISOU 968 CA TYR A 126 2394 2341 2436 -19 -65 -12 ATOM 969 C TYR A 126 -1.797 27.540 -26.772 1.00 22.64 C ANISOU 969 C TYR A 126 2868 2833 2903 -19 -25 -9 ATOM 970 O TYR A 126 -2.109 26.600 -27.500 1.00 19.00 O ANISOU 970 O TYR A 126 2403 2379 2438 -30 -5 -9 ATOM 971 CB TYR A 126 -3.599 29.156 -25.948 1.00 20.51 C ANISOU 971 CB TYR A 126 2598 2544 2652 11 -68 -32 ATOM 972 CG TYR A 126 -4.793 28.222 -26.067 1.00 22.18 C ANISOU 972 CG TYR A 126 2800 2765 2864 14 -42 -40 ATOM 973 CD1 TYR A 126 -5.898 28.592 -26.862 1.00 26.00 C ANISOU 973 CD1 TYR A 126 3280 3244 3356 10 -56 -47 ATOM 974 CD2 TYR A 126 -4.803 26.983 -25.391 1.00 27.91 C ANISOU 974 CD2 TYR A 126 3519 3504 3582 20 -6 -39 ATOM 975 CE1 TYR A 126 -7.003 27.729 -26.987 1.00 22.43 C ANISOU 975 CE1 TYR A 126 2817 2802 2904 10 -33 -52 ATOM 976 CE2 TYR A 126 -5.905 26.121 -25.529 1.00 35.34 C ANISOU 976 CE2 TYR A 126 4450 4452 4524 19 13 -42 ATOM 977 CZ TYR A 126 -7.001 26.487 -26.326 1.00 26.64 C ANISOU 977 CZ TYR A 126 3344 3348 3429 14 0 -48 ATOM 978 OH TYR A 126 -8.054 25.630 -26.445 1.00 27.53 O ANISOU 978 OH TYR A 126 3447 3471 3543 11 18 -49 ATOM 979 N GLN A 127 -0.906 27.460 -25.776 1.00 16.03 N ANISOU 979 N GLN A 127 2032 1998 2062 -5 -18 -8 ATOM 980 CA GLN A 127 -0.142 26.264 -25.436 1.00 17.56 C ANISOU 980 CA GLN A 127 2222 2200 2248 -2 13 -5 ATOM 981 C GLN A 127 -0.900 25.428 -24.385 1.00 22.16 C ANISOU 981 C GLN A 127 2801 2784 2834 18 34 -13 ATOM 982 O GLN A 127 -1.451 25.989 -23.436 1.00 20.52 O ANISOU 982 O GLN A 127 2593 2577 2629 34 26 -20 ATOM 983 CB GLN A 127 1.232 26.750 -24.927 1.00 30.57 C ANISOU 983 CB GLN A 127 3873 3852 3889 -3 3 6 ATOM 984 CG GLN A 127 2.320 25.677 -24.743 1.00 36.30 C ANISOU 984 CG GLN A 127 4595 4588 4608 0 28 8 ATOM 985 CD GLN A 127 2.894 25.113 -26.048 1.00 30.50 C ANISOU 985 CD GLN A 127 3854 3870 3864 -18 36 11 ATOM 986 OE1 GLN A 127 2.426 25.411 -27.143 1.00 31.33 O ANISOU 986 OE1 GLN A 127 3956 3981 3965 -36 25 13 ATOM 987 NE2 GLN A 127 3.932 24.287 -25.927 1.00 31.84 N ANISOU 987 NE2 GLN A 127 4018 4050 4028 -12 53 10 ATOM 988 N CYS A 128 -0.889 24.101 -24.575 1.00 27.22 N ANISOU 988 N CYS A 128 3440 3428 3475 15 58 -12 ATOM 989 CA CYS A 128 -1.515 23.082 -23.726 1.00 29.97 C ANISOU 989 CA CYS A 128 3784 3777 3826 24 76 -13 ATOM 990 C CYS A 128 -0.480 22.027 -23.320 1.00 31.33 C ANISOU 990 C CYS A 128 3958 3947 3998 26 91 -7 ATOM 991 O CYS A 128 0.592 21.959 -23.918 1.00 23.75 O ANISOU 991 O CYS A 128 3001 2987 3036 22 92 -7 ATOM 992 CB CYS A 128 -2.655 22.360 -24.484 1.00 26.57 C ANISOU 992 CB CYS A 128 3350 3344 3400 13 82 -15 ATOM 993 SG CYS A 128 -4.199 23.264 -24.274 1.00 52.45 S ANISOU 993 SG CYS A 128 6621 6626 6681 14 70 -22 ATOM 994 N ALA A 129 -0.875 21.178 -22.356 1.00 27.80 N ANISOU 994 N ALA A 129 3508 3502 3554 30 102 -1 ATOM 995 CA ALA A 129 -0.258 19.882 -22.094 1.00 29.41 C ANISOU 995 CA ALA A 129 3715 3696 3762 30 111 4 ATOM 996 C ALA A 129 -1.319 18.783 -22.158 1.00 23.72 C ANISOU 996 C ALA A 129 2993 2970 3050 21 116 11 ATOM 997 O ALA A 129 -2.453 18.991 -21.722 1.00 26.32 O ANISOU 997 O ALA A 129 3314 3311 3376 17 116 16 ATOM 998 CB ALA A 129 0.426 19.877 -20.718 1.00 26.48 C ANISOU 998 CB ALA A 129 3344 3329 3386 41 113 12 ATOM 999 N MET A 130 -0.902 17.598 -22.630 1.00 24.22 N ANISOU 999 N MET A 130 3062 3016 3123 18 115 10 ATOM 1000 CA MET A 130 -1.616 16.348 -22.400 1.00 20.11 C ANISOU 1000 CA MET A 130 2542 2484 2614 8 112 22 ATOM 1001 C MET A 130 -1.395 15.963 -20.933 1.00 22.76 C ANISOU 1001 C MET A 130 2875 2826 2948 9 113 41 ATOM 1002 O MET A 130 -0.269 15.645 -20.558 1.00 21.64 O ANISOU 1002 O MET A 130 2739 2676 2809 17 112 42 ATOM 1003 CB MET A 130 -1.104 15.267 -23.375 1.00 19.47 C ANISOU 1003 CB MET A 130 2470 2380 2547 8 105 11 ATOM 1004 CG MET A 130 -1.837 13.913 -23.293 1.00 22.77 C ANISOU 1004 CG MET A 130 2892 2778 2980 -5 93 23 ATOM 1005 SD MET A 130 -3.628 13.957 -23.587 1.00 29.92 S ANISOU 1005 SD MET A 130 3791 3692 3884 -25 93 34 ATOM 1006 CE MET A 130 -3.691 14.637 -25.267 1.00 32.56 C ANISOU 1006 CE MET A 130 4130 4024 4218 -22 93 6 ATOM 1007 N ARG A 131 -2.456 16.059 -20.123 1.00 21.24 N ANISOU 1007 N ARG A 131 2672 2653 2747 0 116 55 ATOM 1008 CA ARG A 131 -2.410 15.736 -18.700 1.00 17.38 C ANISOU 1008 CA ARG A 131 2176 2177 2250 -3 117 76 ATOM 1009 C ARG A 131 -2.197 14.220 -18.485 1.00 21.14 C ANISOU 1009 C ARG A 131 2660 2630 2742 -16 105 95 ATOM 1010 O ARG A 131 -2.594 13.438 -19.349 1.00 24.90 O ANISOU 1010 O ARG A 131 3144 3083 3234 -26 94 93 ATOM 1011 CB ARG A 131 -3.717 16.211 -18.031 1.00 14.12 C ANISOU 1011 CB ARG A 131 1745 1801 1820 -10 123 86 ATOM 1012 CG ARG A 131 -3.995 17.729 -18.109 1.00 18.45 C ANISOU 1012 CG ARG A 131 2284 2372 2354 8 129 65 ATOM 1013 CD ARG A 131 -2.827 18.621 -17.667 1.00 27.48 C ANISOU 1013 CD ARG A 131 3435 3514 3493 27 129 54 ATOM 1014 NE ARG A 131 -2.332 18.248 -16.336 1.00 22.29 N ANISOU 1014 NE ARG A 131 2774 2870 2825 28 131 69 ATOM 1015 CZ ARG A 131 -1.340 18.844 -15.661 1.00 29.60 C ANISOU 1015 CZ ARG A 131 3706 3796 3747 43 130 64 ATOM 1016 NH1 ARG A 131 -0.750 19.955 -16.120 1.00 24.79 N ANISOU 1016 NH1 ARG A 131 3105 3175 3140 57 125 45 ATOM 1017 NH2 ARG A 131 -0.930 18.317 -14.503 1.00 20.88 N1+ ANISOU 1017 NH2 ARG A 131 2598 2704 2633 41 132 80 ATOM 1018 N PRO A 132 -1.612 13.820 -17.333 1.00 22.64 N ANISOU 1018 N PRO A 132 2849 2825 2929 -18 102 113 ATOM 1019 CA PRO A 132 -1.569 12.410 -16.889 1.00 26.91 C ANISOU 1019 CA PRO A 132 3396 3341 3486 -35 83 136 ATOM 1020 C PRO A 132 -2.893 11.617 -16.910 1.00 21.49 C ANISOU 1020 C PRO A 132 2703 2658 2803 -62 73 159 ATOM 1021 O PRO A 132 -2.852 10.421 -17.193 1.00 29.37 O ANISOU 1021 O PRO A 132 3713 3622 3823 -76 49 171 ATOM 1022 CB PRO A 132 -0.957 12.500 -15.488 1.00 29.53 C ANISOU 1022 CB PRO A 132 3724 3689 3808 -35 84 156 ATOM 1023 CG PRO A 132 -0.009 13.680 -15.601 1.00 26.14 C ANISOU 1023 CG PRO A 132 3296 3270 3367 -9 99 131 ATOM 1024 CD PRO A 132 -0.788 14.664 -16.462 1.00 15.61 C ANISOU 1024 CD PRO A 132 1954 1953 2022 -3 111 111 ATOM 1025 N ASN A 133 -4.035 12.288 -16.675 1.00 22.12 N ANISOU 1025 N ASN A 133 2766 2777 2863 -70 86 163 ATOM 1026 CA ASN A 133 -5.380 11.707 -16.804 1.00 20.77 C ANISOU 1026 CA ASN A 133 2584 2614 2692 -99 76 186 ATOM 1027 C ASN A 133 -5.952 11.738 -18.245 1.00 24.32 C ANISOU 1027 C ASN A 133 3041 3045 3155 -97 75 166 ATOM 1028 O ASN A 133 -7.136 11.456 -18.424 1.00 21.13 O ANISOU 1028 O ASN A 133 2627 2653 2749 -118 71 180 ATOM 1029 CB ASN A 133 -6.330 12.341 -15.761 1.00 22.13 C ANISOU 1029 CB ASN A 133 2728 2846 2834 -110 90 204 ATOM 1030 CG ASN A 133 -6.724 13.807 -15.989 1.00 21.32 C ANISOU 1030 CG ASN A 133 2613 2774 2714 -86 111 173 ATOM 1031 OD1 ASN A 133 -6.253 14.475 -16.908 1.00 20.29 O ANISOU 1031 OD1 ASN A 133 2496 2620 2594 -66 114 143 ATOM 1032 ND2 ASN A 133 -7.607 14.313 -15.132 1.00 27.33 N ANISOU 1032 ND2 ASN A 133 3347 3590 3446 -88 122 180 ATOM 1033 N PHE A 134 -5.117 12.089 -19.239 1.00 27.48 N ANISOU 1033 N PHE A 134 3457 3419 3566 -74 78 134 ATOM 1034 CA PHE A 134 -5.400 12.139 -20.679 1.00 25.35 C ANISOU 1034 CA PHE A 134 3195 3130 3308 -72 75 112 ATOM 1035 C PHE A 134 -6.383 13.231 -21.140 1.00 25.48 C ANISOU 1035 C PHE A 134 3197 3176 3308 -72 90 104 ATOM 1036 O PHE A 134 -6.756 13.243 -22.313 1.00 27.32 O ANISOU 1036 O PHE A 134 3433 3398 3549 -79 85 95 ATOM 1037 CB PHE A 134 -5.796 10.755 -21.221 1.00 27.12 C ANISOU 1037 CB PHE A 134 3429 3321 3553 -93 50 126 ATOM 1038 CG PHE A 134 -4.710 9.703 -21.164 1.00 27.63 C ANISOU 1038 CG PHE A 134 3512 3347 3639 -86 29 125 ATOM 1039 CD1 PHE A 134 -3.677 9.704 -22.124 1.00 31.93 C ANISOU 1039 CD1 PHE A 134 4069 3867 4194 -62 27 90 ATOM 1040 CD2 PHE A 134 -4.649 8.801 -20.081 1.00 33.61 C ANISOU 1040 CD2 PHE A 134 4271 4095 4406 -105 8 158 ATOM 1041 CE1 PHE A 134 -2.652 8.773 -22.032 1.00 33.59 C ANISOU 1041 CE1 PHE A 134 4294 4044 4425 -51 5 83 ATOM 1042 CE2 PHE A 134 -3.617 7.878 -20.008 1.00 33.42 C ANISOU 1042 CE2 PHE A 134 4263 4031 4404 -97 -17 155 ATOM 1043 CZ PHE A 134 -2.628 7.859 -20.984 1.00 32.85 C ANISOU 1043 CZ PHE A 134 4203 3933 4343 -67 -18 115 ATOM 1044 N THR A 135 -6.754 14.155 -20.242 1.00 24.61 N ANISOU 1044 N THR A 135 3070 3103 3177 -65 104 106 ATOM 1045 CA THR A 135 -7.483 15.373 -20.596 1.00 22.49 C ANISOU 1045 CA THR A 135 2790 2860 2897 -56 113 89 ATOM 1046 C THR A 135 -6.495 16.482 -21.001 1.00 19.00 C ANISOU 1046 C THR A 135 2356 2411 2452 -32 118 62 ATOM 1047 O THR A 135 -5.281 16.314 -20.881 1.00 22.39 O ANISOU 1047 O THR A 135 2796 2826 2884 -22 118 59 ATOM 1048 CB THR A 135 -8.352 15.879 -19.411 1.00 26.86 C ANISOU 1048 CB THR A 135 3316 3461 3427 -58 122 100 ATOM 1049 OG1 THR A 135 -7.612 16.495 -18.371 1.00 23.86 O ANISOU 1049 OG1 THR A 135 2935 3098 3035 -42 128 99 ATOM 1050 CG2 THR A 135 -9.254 14.788 -18.827 1.00 25.91 C ANISOU 1050 CG2 THR A 135 3185 3355 3306 -87 116 134 ATOM 1051 N ILE A 136 -7.045 17.606 -21.470 1.00 15.86 N ANISOU 1051 N ILE A 136 1952 2024 2049 -24 119 46 ATOM 1052 CA ILE A 136 -6.305 18.840 -21.692 1.00 24.11 C ANISOU 1052 CA ILE A 136 3002 3068 3090 -5 118 26 ATOM 1053 C ILE A 136 -7.141 19.960 -21.054 1.00 21.71 C ANISOU 1053 C ILE A 136 2682 2795 2773 8 117 17 ATOM 1054 O ILE A 136 -8.372 19.921 -21.114 1.00 24.73 O ANISOU 1054 O ILE A 136 3049 3196 3152 2 118 19 ATOM 1055 CB ILE A 136 -6.002 19.105 -23.209 1.00 25.25 C ANISOU 1055 CB ILE A 136 3160 3190 3244 -6 112 11 ATOM 1056 CG1 ILE A 136 -7.044 19.894 -24.046 1.00 33.34 C ANISOU 1056 CG1 ILE A 136 4177 4220 4268 -10 105 2 ATOM 1057 CG2 ILE A 136 -5.605 17.801 -23.939 1.00 22.50 C ANISOU 1057 CG2 ILE A 136 2824 2818 2908 -18 111 15 ATOM 1058 CD1 ILE A 136 -6.469 20.444 -25.362 1.00 30.22 C ANISOU 1058 CD1 ILE A 136 3795 3809 3880 -16 97 -9 ATOM 1059 N LYS A 137 -6.457 20.937 -20.445 1.00 21.08 N ANISOU 1059 N LYS A 137 2603 2720 2686 28 113 5 ATOM 1060 CA LYS A 137 -7.078 22.107 -19.830 1.00 24.48 C ANISOU 1060 CA LYS A 137 3020 3178 3105 48 106 -12 ATOM 1061 C LYS A 137 -7.010 23.272 -20.823 1.00 22.86 C ANISOU 1061 C LYS A 137 2824 2953 2910 54 87 -30 ATOM 1062 O LYS A 137 -6.215 24.196 -20.653 1.00 28.03 O ANISOU 1062 O LYS A 137 3488 3596 3566 66 73 -40 ATOM 1063 CB LYS A 137 -6.417 22.390 -18.463 1.00 33.72 C ANISOU 1063 CB LYS A 137 4186 4365 4262 65 108 -14 ATOM 1064 CG LYS A 137 -6.706 21.264 -17.452 1.00 43.24 C ANISOU 1064 CG LYS A 137 5383 5588 5457 52 123 10 ATOM 1065 CD LYS A 137 -6.380 21.611 -15.992 1.00 57.66 C ANISOU 1065 CD LYS A 137 7193 7455 7261 68 127 7 ATOM 1066 CE LYS A 137 -4.883 21.671 -15.670 1.00 61.62 C ANISOU 1066 CE LYS A 137 7709 7942 7762 84 121 0 ATOM 1067 NZ LYS A 137 -4.661 21.740 -14.215 1.00 57.87 N1+ ANISOU 1067 NZ LYS A 137 7228 7490 7272 80 131 19 ATOM 1068 N GLY A 138 -7.836 23.159 -21.875 1.00 25.21 N ANISOU 1068 N GLY A 138 3119 3245 3215 43 84 -31 ATOM 1069 CA GLY A 138 -7.910 24.109 -22.977 1.00 28.90 C ANISOU 1069 CA GLY A 138 3595 3693 3693 42 64 -43 ATOM 1070 C GLY A 138 -8.925 25.218 -22.682 1.00 29.17 C ANISOU 1070 C GLY A 138 3616 3741 3726 62 46 -63 ATOM 1071 O GLY A 138 -9.465 25.334 -21.579 1.00 24.79 O ANISOU 1071 O GLY A 138 3043 3216 3159 81 50 -73 ATOM 1072 N SER A 139 -9.172 26.030 -23.716 1.00 25.49 N ANISOU 1072 N SER A 139 3158 3256 3272 58 23 -71 ATOM 1073 CA SER A 139 -10.149 27.108 -23.745 1.00 20.66 C ANISOU 1073 CA SER A 139 2535 2651 2665 76 0 -92 ATOM 1074 C SER A 139 -10.957 26.918 -25.034 1.00 26.70 C ANISOU 1074 C SER A 139 3301 3405 3440 56 -4 -87 ATOM 1075 O SER A 139 -10.489 27.280 -26.115 1.00 21.83 O ANISOU 1075 O SER A 139 2700 2761 2832 38 -18 -79 ATOM 1076 CB SER A 139 -9.408 28.458 -23.662 1.00 22.88 C ANISOU 1076 CB SER A 139 2827 2912 2952 94 -36 -107 ATOM 1077 OG SER A 139 -10.306 29.549 -23.663 1.00 24.15 O ANISOU 1077 OG SER A 139 2978 3074 3122 112 -66 -130 ATOM 1078 N PHE A 140 -12.129 26.289 -24.886 1.00 22.32 N ANISOU 1078 N PHE A 140 2726 2872 2881 55 9 -88 ATOM 1079 CA PHE A 140 -12.976 25.835 -25.982 1.00 16.63 C ANISOU 1079 CA PHE A 140 2006 2144 2170 34 9 -80 ATOM 1080 C PHE A 140 -14.448 26.116 -25.647 1.00 19.94 C ANISOU 1080 C PHE A 140 2400 2590 2588 48 4 -94 ATOM 1081 O PHE A 140 -14.896 25.771 -24.553 1.00 24.17 O ANISOU 1081 O PHE A 140 2913 3163 3108 60 20 -96 ATOM 1082 CB PHE A 140 -12.740 24.322 -26.184 1.00 16.09 C ANISOU 1082 CB PHE A 140 1941 2074 2098 7 37 -57 ATOM 1083 CG PHE A 140 -11.430 23.879 -26.822 1.00 20.51 C ANISOU 1083 CG PHE A 140 2524 2610 2660 -8 42 -46 ATOM 1084 CD1 PHE A 140 -10.995 24.409 -28.056 1.00 30.45 C ANISOU 1084 CD1 PHE A 140 3798 3846 3925 -23 29 -46 ATOM 1085 CD2 PHE A 140 -10.717 22.800 -26.261 1.00 32.52 C ANISOU 1085 CD2 PHE A 140 4048 4134 4174 -9 62 -35 ATOM 1086 CE1 PHE A 140 -9.898 23.853 -28.703 1.00 22.99 C ANISOU 1086 CE1 PHE A 140 2868 2889 2978 -35 36 -38 ATOM 1087 CE2 PHE A 140 -9.617 22.265 -26.912 1.00 27.10 C ANISOU 1087 CE2 PHE A 140 3379 3428 3490 -20 67 -28 ATOM 1088 CZ PHE A 140 -9.220 22.778 -28.138 1.00 22.03 C ANISOU 1088 CZ PHE A 140 2749 2770 2852 -31 56 -32 ATOM 1089 N LEU A 141 -15.170 26.705 -26.613 1.00 17.26 N ANISOU 1089 N LEU A 141 2061 2236 2261 43 -17 -101 ATOM 1090 CA LEU A 141 -16.610 26.970 -26.564 1.00 21.63 C ANISOU 1090 CA LEU A 141 2589 2814 2814 56 -24 -115 ATOM 1091 C LEU A 141 -17.340 25.999 -27.507 1.00 21.49 C ANISOU 1091 C LEU A 141 2570 2794 2802 25 -12 -95 ATOM 1092 O LEU A 141 -16.703 25.163 -28.149 1.00 25.23 O ANISOU 1092 O LEU A 141 3064 3244 3279 -2 -2 -76 ATOM 1093 CB LEU A 141 -16.882 28.435 -26.992 1.00 21.56 C ANISOU 1093 CB LEU A 141 2581 2789 2821 78 -66 -140 ATOM 1094 CG LEU A 141 -16.126 29.513 -26.188 1.00 22.67 C ANISOU 1094 CG LEU A 141 2729 2923 2962 109 -89 -161 ATOM 1095 CD1 LEU A 141 -16.329 30.900 -26.817 1.00 23.34 C ANISOU 1095 CD1 LEU A 141 2823 2976 3068 121 -139 -179 ATOM 1096 CD2 LEU A 141 -16.482 29.514 -24.688 1.00 25.13 C ANISOU 1096 CD2 LEU A 141 3012 3282 3256 144 -78 -184 ATOM 1097 N ASN A 142 -18.673 26.130 -27.598 1.00 18.13 N ANISOU 1097 N ASN A 142 2119 2396 2375 31 -13 -102 ATOM 1098 CA ASN A 142 -19.496 25.357 -28.531 1.00 22.90 C ANISOU 1098 CA ASN A 142 2722 2995 2985 1 -6 -84 ATOM 1099 C ASN A 142 -19.107 25.640 -29.997 1.00 13.00 C ANISOU 1099 C ASN A 142 1497 1696 1748 -19 -25 -80 ATOM 1100 O ASN A 142 -19.006 26.803 -30.390 1.00 25.67 O ANISOU 1100 O ASN A 142 3110 3280 3362 -7 -54 -95 ATOM 1101 CB ASN A 142 -20.990 25.653 -28.277 1.00 24.05 C ANISOU 1101 CB ASN A 142 2836 3174 3130 13 -13 -96 ATOM 1102 CG ASN A 142 -21.545 24.966 -27.023 1.00 46.25 C ANISOU 1102 CG ASN A 142 5612 6043 5918 24 9 -94 ATOM 1103 OD1 ASN A 142 -21.570 23.738 -26.936 1.00 46.79 O ANISOU 1103 OD1 ASN A 142 5674 6128 5976 -2 32 -66 ATOM 1104 ND2 ASN A 142 -22.024 25.751 -26.057 1.00 50.76 N ANISOU 1104 ND2 ASN A 142 6159 6647 6479 63 -1 -124 ATOM 1105 N GLY A 143 -18.886 24.561 -30.763 1.00 18.39 N ANISOU 1105 N GLY A 143 2193 2362 2431 -50 -11 -59 ATOM 1106 CA GLY A 143 -18.481 24.627 -32.170 1.00 24.68 C ANISOU 1106 CA GLY A 143 3014 3127 3238 -71 -25 -55 ATOM 1107 C GLY A 143 -16.958 24.622 -32.354 1.00 23.10 C ANISOU 1107 C GLY A 143 2836 2907 3033 -77 -22 -51 ATOM 1108 O GLY A 143 -16.503 24.698 -33.495 1.00 23.33 O ANISOU 1108 O GLY A 143 2882 2917 3065 -96 -34 -46 ATOM 1109 N SER A 144 -16.169 24.516 -31.268 1.00 18.71 N ANISOU 1109 N SER A 144 2280 2361 2469 -62 -9 -52 ATOM 1110 CA SER A 144 -14.710 24.390 -31.314 1.00 20.23 C ANISOU 1110 CA SER A 144 2491 2540 2657 -66 -4 -47 ATOM 1111 C SER A 144 -14.203 23.042 -31.854 1.00 12.41 C ANISOU 1111 C SER A 144 1511 1542 1663 -87 16 -36 ATOM 1112 O SER A 144 -13.028 22.949 -32.192 1.00 21.01 O ANISOU 1112 O SER A 144 2614 2620 2747 -94 17 -34 ATOM 1113 CB SER A 144 -14.116 24.662 -29.925 1.00 20.17 C ANISOU 1113 CB SER A 144 2479 2544 2642 -42 2 -53 ATOM 1114 OG SER A 144 -14.497 23.662 -29.008 1.00 23.18 O ANISOU 1114 OG SER A 144 2845 2947 3016 -38 25 -47 ATOM 1115 N CYS A 145 -15.081 22.030 -31.904 1.00 14.82 N ANISOU 1115 N CYS A 145 1808 1854 1970 -95 28 -28 ATOM 1116 CA CYS A 145 -14.808 20.656 -32.322 1.00 18.35 C ANISOU 1116 CA CYS A 145 2266 2289 2417 -112 40 -19 ATOM 1117 C CYS A 145 -14.148 20.608 -33.710 1.00 14.24 C ANISOU 1117 C CYS A 145 1762 1752 1895 -126 32 -25 ATOM 1118 O CYS A 145 -14.607 21.290 -34.624 1.00 19.82 O ANISOU 1118 O CYS A 145 2470 2456 2604 -135 17 -28 ATOM 1119 CB CYS A 145 -16.101 19.829 -32.307 1.00 17.11 C ANISOU 1119 CB CYS A 145 2098 2138 2265 -126 41 -8 ATOM 1120 SG CYS A 145 -16.813 19.881 -30.643 1.00 23.42 S ANISOU 1120 SG CYS A 145 2867 2973 3059 -114 49 0 ATOM 1121 N GLY A 146 -13.059 19.839 -33.814 1.00 16.04 N ANISOU 1121 N GLY A 146 2003 1973 2119 -127 41 -27 ATOM 1122 CA GLY A 146 -12.234 19.743 -35.013 1.00 22.91 C ANISOU 1122 CA GLY A 146 2885 2840 2982 -137 37 -35 ATOM 1123 C GLY A 146 -11.036 20.704 -34.989 1.00 19.06 C ANISOU 1123 C GLY A 146 2399 2360 2484 -131 34 -38 ATOM 1124 O GLY A 146 -10.205 20.615 -35.892 1.00 16.14 O ANISOU 1124 O GLY A 146 2035 1996 2103 -138 34 -44 ATOM 1125 N SER A 147 -10.918 21.594 -33.981 1.00 20.39 N ANISOU 1125 N SER A 147 2562 2532 2654 -118 29 -35 ATOM 1126 CA SER A 147 -9.717 22.399 -33.724 1.00 22.90 C ANISOU 1126 CA SER A 147 2883 2856 2963 -111 26 -35 ATOM 1127 C SER A 147 -8.561 21.479 -33.322 1.00 12.98 C ANISOU 1127 C SER A 147 1630 1601 1700 -104 44 -38 ATOM 1128 O SER A 147 -8.761 20.624 -32.457 1.00 17.81 O ANISOU 1128 O SER A 147 2242 2206 2318 -97 56 -38 ATOM 1129 CB SER A 147 -9.969 23.402 -32.584 1.00 21.90 C ANISOU 1129 CB SER A 147 2750 2729 2841 -93 18 -34 ATOM 1130 OG SER A 147 -10.804 24.447 -33.028 1.00 19.41 O ANISOU 1130 OG SER A 147 2431 2410 2533 -97 -6 -35 ATOM 1131 N VAL A 148 -7.395 21.653 -33.959 1.00 10.07 N ANISOU 1131 N VAL A 148 1265 1243 1319 -107 43 -39 ATOM 1132 CA VAL A 148 -6.275 20.734 -33.799 1.00 17.01 C ANISOU 1132 CA VAL A 148 2145 2126 2192 -98 58 -47 ATOM 1133 C VAL A 148 -5.154 21.310 -32.925 1.00 12.55 C ANISOU 1133 C VAL A 148 1579 1568 1621 -87 59 -42 ATOM 1134 O VAL A 148 -4.908 22.519 -32.917 1.00 20.27 O ANISOU 1134 O VAL A 148 2556 2551 2596 -91 45 -33 ATOM 1135 CB VAL A 148 -5.686 20.270 -35.161 1.00 11.60 C ANISOU 1135 CB VAL A 148 1460 1456 1492 -110 58 -58 ATOM 1136 CG1 VAL A 148 -6.741 19.503 -35.977 1.00 20.67 C ANISOU 1136 CG1 VAL A 148 2612 2595 2647 -119 57 -66 ATOM 1137 CG2 VAL A 148 -5.015 21.365 -36.011 1.00 15.37 C ANISOU 1137 CG2 VAL A 148 1932 1956 1952 -128 45 -50 ATOM 1138 N GLY A 149 -4.496 20.379 -32.222 1.00 18.49 N ANISOU 1138 N GLY A 149 2333 2319 2374 -73 73 -47 ATOM 1139 CA GLY A 149 -3.271 20.591 -31.479 1.00 16.13 C ANISOU 1139 CA GLY A 149 2032 2027 2068 -62 76 -44 ATOM 1140 C GLY A 149 -2.104 20.083 -32.330 1.00 22.11 C ANISOU 1140 C GLY A 149 2786 2803 2812 -62 81 -56 ATOM 1141 O GLY A 149 -2.240 19.103 -33.066 1.00 17.41 O ANISOU 1141 O GLY A 149 2192 2207 2217 -60 86 -71 ATOM 1142 N PHE A 150 -0.950 20.753 -32.210 1.00 15.33 N ANISOU 1142 N PHE A 150 1922 1963 1940 -63 79 -50 ATOM 1143 CA PHE A 150 0.219 20.519 -33.049 1.00 17.47 C ANISOU 1143 CA PHE A 150 2182 2263 2191 -65 83 -60 ATOM 1144 C PHE A 150 1.498 21.027 -32.375 1.00 18.69 C ANISOU 1144 C PHE A 150 2331 2432 2338 -58 84 -51 ATOM 1145 O PHE A 150 1.466 21.982 -31.599 1.00 20.47 O ANISOU 1145 O PHE A 150 2561 2647 2569 -59 76 -35 ATOM 1146 CB PHE A 150 0.013 21.192 -34.435 1.00 19.01 C ANISOU 1146 CB PHE A 150 2369 2486 2366 -91 73 -56 ATOM 1147 CG PHE A 150 -0.057 22.716 -34.433 1.00 21.44 C ANISOU 1147 CG PHE A 150 2678 2795 2672 -111 53 -32 ATOM 1148 CD1 PHE A 150 -1.256 23.369 -34.072 1.00 21.73 C ANISOU 1148 CD1 PHE A 150 2724 2805 2726 -115 40 -24 ATOM 1149 CD2 PHE A 150 1.104 23.493 -34.636 1.00 23.04 C ANISOU 1149 CD2 PHE A 150 2871 3027 2856 -125 42 -16 ATOM 1150 CE1 PHE A 150 -1.293 24.753 -33.963 1.00 21.32 C ANISOU 1150 CE1 PHE A 150 2675 2749 2676 -129 15 -5 ATOM 1151 CE2 PHE A 150 1.045 24.877 -34.529 1.00 17.92 C ANISOU 1151 CE2 PHE A 150 2225 2374 2209 -146 16 8 ATOM 1152 CZ PHE A 150 -0.148 25.504 -34.195 1.00 16.52 C ANISOU 1152 CZ PHE A 150 2061 2165 2052 -146 0 12 ATOM 1153 N ASN A 151 2.616 20.410 -32.771 1.00 23.18 N ANISOU 1153 N ASN A 151 2888 3027 2891 -51 92 -65 ATOM 1154 CA ASN A 151 3.968 20.936 -32.600 1.00 24.68 C ANISOU 1154 CA ASN A 151 3066 3246 3064 -52 92 -56 ATOM 1155 C ASN A 151 4.526 21.211 -34.000 1.00 32.07 C ANISOU 1155 C ASN A 151 3983 4233 3970 -72 89 -59 ATOM 1156 O ASN A 151 4.115 20.553 -34.957 1.00 21.92 O ANISOU 1156 O ASN A 151 2694 2960 2676 -75 93 -76 ATOM 1157 CB ASN A 151 4.867 19.917 -31.863 1.00 16.52 C ANISOU 1157 CB ASN A 151 2031 2209 2038 -24 104 -71 ATOM 1158 CG ASN A 151 4.430 19.660 -30.416 1.00 26.81 C ANISOU 1158 CG ASN A 151 3349 3472 3364 -11 104 -60 ATOM 1159 OD1 ASN A 151 3.390 19.055 -30.173 1.00 29.13 O ANISOU 1159 OD1 ASN A 151 3644 3766 3658 -13 100 -43 ATOM 1160 ND2 ASN A 151 5.226 20.093 -29.442 1.00 22.47 N ANISOU 1160 ND2 ASN A 151 2810 2891 2834 0 108 -69 ATOM 1161 N ILE A 152 5.469 22.158 -34.093 1.00 21.94 N ANISOU 1161 N ILE A 152 2687 2981 2667 -88 82 -40 ATOM 1162 CA ILE A 152 6.217 22.398 -35.324 1.00 26.17 C ANISOU 1162 CA ILE A 152 3198 3578 3167 -108 80 -38 ATOM 1163 C ILE A 152 7.685 22.104 -35.029 1.00 35.85 C ANISOU 1163 C ILE A 152 4404 4840 4377 -93 91 -46 ATOM 1164 O ILE A 152 8.271 22.752 -34.164 1.00 38.95 O ANISOU 1164 O ILE A 152 4801 5220 4779 -89 87 -29 ATOM 1165 CB ILE A 152 6.087 23.852 -35.861 1.00 26.41 C ANISOU 1165 CB ILE A 152 3226 3623 3185 -150 55 -1 ATOM 1166 CG1 ILE A 152 4.595 24.189 -36.073 1.00 23.53 C ANISOU 1166 CG1 ILE A 152 2882 3214 2843 -159 41 5 ATOM 1167 CG2 ILE A 152 6.894 24.056 -37.169 1.00 33.89 C ANISOU 1167 CG2 ILE A 152 4144 4641 4090 -177 54 2 ATOM 1168 CD1 ILE A 152 4.315 25.546 -36.725 1.00 39.07 C ANISOU 1168 CD1 ILE A 152 4848 5198 4799 -201 12 35 ATOM 1169 N ASP A 153 8.240 21.150 -35.785 1.00 36.16 N ANISOU 1169 N ASP A 153 4421 4924 4392 -82 104 -74 ATOM 1170 CA ASP A 153 9.659 20.838 -35.813 1.00 45.70 C ANISOU 1170 CA ASP A 153 5604 6183 5579 -68 114 -87 ATOM 1171 C ASP A 153 10.163 21.179 -37.215 1.00 57.91 C ANISOU 1171 C ASP A 153 7117 7807 7078 -97 112 -82 ATOM 1172 O ASP A 153 9.899 20.441 -38.166 1.00 48.96 O ANISOU 1172 O ASP A 153 5972 6704 5928 -89 120 -113 ATOM 1173 CB ASP A 153 9.992 19.381 -35.416 1.00 73.84 C ANISOU 1173 CB ASP A 153 9168 9730 9157 -21 128 -132 ATOM 1174 CG ASP A 153 9.412 18.963 -34.063 1.00 94.44 C ANISOU 1174 CG ASP A 153 11807 12267 11809 1 127 -128 ATOM 1175 OD1 ASP A 153 10.042 19.319 -33.043 1.00 99.30 O ANISOU 1175 OD1 ASP A 153 12422 12878 12430 6 127 -113 ATOM 1176 OD2 ASP A 153 8.361 18.286 -34.072 1.00 88.25 O1- ANISOU 1176 OD2 ASP A 153 11045 11434 11051 11 126 -139 ATOM 1177 N TYR A 154 10.926 22.281 -37.290 1.00 65.83 N ANISOU 1177 N TYR A 154 8106 8846 8059 -132 99 -42 ATOM 1178 CA TYR A 154 11.702 22.737 -38.447 1.00 60.79 C ANISOU 1178 CA TYR A 154 7429 8299 7371 -163 97 -32 ATOM 1179 C TYR A 154 10.742 23.318 -39.512 1.00 49.56 C ANISOU 1179 C TYR A 154 6009 6885 5936 -197 85 -20 ATOM 1180 O TYR A 154 10.289 24.449 -39.334 1.00 47.59 O ANISOU 1180 O TYR A 154 5775 6610 5696 -234 60 22 ATOM 1181 CB TYR A 154 12.718 21.647 -38.934 1.00 78.99 C ANISOU 1181 CB TYR A 154 9700 10661 9649 -126 120 -79 ATOM 1182 CG TYR A 154 13.195 20.646 -37.873 1.00116.72 C ANISOU 1182 CG TYR A 154 14494 15392 14462 -73 133 -113 ATOM 1183 CD1 TYR A 154 13.638 21.078 -36.601 1.00125.93 C ANISOU 1183 CD1 TYR A 154 15683 16501 15662 -68 126 -89 ATOM 1184 CD2 TYR A 154 13.074 19.261 -38.122 1.00129.31 C ANISOU 1184 CD2 TYR A 154 16080 16995 16058 -28 146 -169 ATOM 1185 CE1 TYR A 154 13.878 20.142 -35.573 1.00126.56 C ANISOU 1185 CE1 TYR A 154 15777 16536 15772 -23 135 -116 ATOM 1186 CE2 TYR A 154 13.332 18.324 -37.101 1.00132.58 C ANISOU 1186 CE2 TYR A 154 16509 17360 16506 17 151 -196 ATOM 1187 CZ TYR A 154 13.710 18.765 -35.819 1.00128.01 C ANISOU 1187 CZ TYR A 154 15952 16728 15958 18 146 -167 ATOM 1188 OH TYR A 154 13.891 17.858 -34.813 1.00121.55 O ANISOU 1188 OH TYR A 154 15148 15864 15172 58 148 -190 ATOM 1189 N ASP A 155 10.411 22.540 -40.556 1.00 44.57 N ANISOU 1189 N ASP A 155 5364 6285 5284 -185 99 -57 ATOM 1190 CA ASP A 155 9.387 22.847 -41.564 1.00 65.15 C ANISOU 1190 CA ASP A 155 7977 8892 7883 -215 88 -48 ATOM 1191 C ASP A 155 8.140 21.946 -41.410 1.00 50.27 C ANISOU 1191 C ASP A 155 6123 6942 6034 -185 95 -82 ATOM 1192 O ASP A 155 7.107 22.262 -42.001 1.00 38.48 O ANISOU 1192 O ASP A 155 4640 5438 4541 -207 85 -75 ATOM 1193 CB ASP A 155 9.918 22.741 -43.022 1.00 58.66 C ANISOU 1193 CB ASP A 155 7114 8171 7003 -238 92 -55 ATOM 1194 CG ASP A 155 10.600 21.420 -43.428 1.00 57.34 C ANISOU 1194 CG ASP A 155 6923 8047 6817 -190 118 -116 ATOM 1195 OD1 ASP A 155 10.946 20.612 -42.537 1.00 51.37 O ANISOU 1195 OD1 ASP A 155 6178 7250 6089 -144 129 -146 ATOM 1196 OD2 ASP A 155 10.786 21.247 -44.651 1.00 63.60 O1- ANISOU 1196 OD2 ASP A 155 7685 8916 7565 -199 124 -136 ATOM 1197 N CYS A 156 8.260 20.836 -40.659 1.00 30.29 N ANISOU 1197 N CYS A 156 3608 4367 3535 -138 108 -114 ATOM 1198 CA CYS A 156 7.233 19.810 -40.498 1.00 36.37 C ANISOU 1198 CA CYS A 156 4402 5083 4335 -108 114 -148 ATOM 1199 C CYS A 156 6.280 20.168 -39.345 1.00 34.20 C ANISOU 1199 C CYS A 156 4163 4723 4107 -104 106 -129 ATOM 1200 O CYS A 156 6.751 20.537 -38.271 1.00 20.92 O ANISOU 1200 O CYS A 156 2489 3015 2444 -91 108 -118 ATOM 1201 CB CYS A 156 7.884 18.422 -40.303 1.00 21.27 C ANISOU 1201 CB CYS A 156 2478 3179 2423 -59 127 -199 ATOM 1202 SG CYS A 156 6.674 17.070 -40.181 1.00 32.04 S ANISOU 1202 SG CYS A 156 3873 4476 3826 -25 126 -238 ATOM 1203 N VAL A 157 4.967 20.017 -39.579 1.00 28.53 N ANISOU 1203 N VAL A 157 3466 3968 3408 -114 99 -126 ATOM 1204 CA VAL A 157 3.925 20.189 -38.569 1.00 21.25 C ANISOU 1204 CA VAL A 157 2574 2973 2528 -108 94 -112 ATOM 1205 C VAL A 157 3.447 18.799 -38.112 1.00 23.96 C ANISOU 1205 C VAL A 157 2931 3277 2897 -72 103 -146 ATOM 1206 O VAL A 157 2.716 18.125 -38.839 1.00 24.75 O ANISOU 1206 O VAL A 157 3031 3376 2994 -66 103 -170 ATOM 1207 CB VAL A 157 2.699 20.974 -39.119 1.00 26.40 C ANISOU 1207 CB VAL A 157 3238 3608 3187 -139 79 -91 ATOM 1208 CG1 VAL A 157 1.595 21.177 -38.060 1.00 21.37 C ANISOU 1208 CG1 VAL A 157 2627 2904 2590 -130 73 -78 ATOM 1209 CG2 VAL A 157 3.109 22.339 -39.693 1.00 25.01 C ANISOU 1209 CG2 VAL A 157 3049 3468 2986 -178 62 -57 ATOM 1210 N SER A 158 3.852 18.402 -36.899 1.00 17.71 N ANISOU 1210 N SER A 158 2150 2449 2130 -50 106 -143 ATOM 1211 CA SER A 158 3.343 17.208 -36.235 1.00 21.93 C ANISOU 1211 CA SER A 158 2702 2938 2694 -22 108 -165 ATOM 1212 C SER A 158 1.990 17.518 -35.581 1.00 19.53 C ANISOU 1212 C SER A 158 2419 2584 2418 -33 102 -142 ATOM 1213 O SER A 158 1.970 18.058 -34.476 1.00 24.80 O ANISOU 1213 O SER A 158 3093 3232 3097 -36 102 -118 ATOM 1214 CB SER A 158 4.374 16.693 -35.210 1.00 26.24 C ANISOU 1214 CB SER A 158 3246 3476 3250 6 113 -172 ATOM 1215 OG SER A 158 5.272 15.806 -35.843 1.00 33.01 O ANISOU 1215 OG SER A 158 4079 4379 4082 22 117 -201 ATOM 1216 N PHE A 159 0.890 17.169 -36.267 1.00 19.14 N ANISOU 1216 N PHE A 159 2378 2517 2377 -38 97 -151 ATOM 1217 CA PHE A 159 -0.457 17.182 -35.693 1.00 16.92 C ANISOU 1217 CA PHE A 159 2114 2195 2121 -47 92 -133 ATOM 1218 C PHE A 159 -0.587 16.030 -34.689 1.00 22.28 C ANISOU 1218 C PHE A 159 2804 2834 2826 -26 92 -138 ATOM 1219 O PHE A 159 -0.159 14.916 -34.996 1.00 22.27 O ANISOU 1219 O PHE A 159 2805 2826 2830 -8 89 -162 ATOM 1220 CB PHE A 159 -1.518 17.036 -36.797 1.00 19.82 C ANISOU 1220 CB PHE A 159 2484 2560 2486 -63 86 -139 ATOM 1221 CG PHE A 159 -1.569 18.170 -37.800 1.00 22.20 C ANISOU 1221 CG PHE A 159 2775 2896 2763 -89 81 -128 ATOM 1222 CD1 PHE A 159 -2.132 19.408 -37.431 1.00 18.00 C ANISOU 1222 CD1 PHE A 159 2246 2355 2236 -109 73 -100 ATOM 1223 CD2 PHE A 159 -0.946 18.044 -39.060 1.00 18.93 C ANISOU 1223 CD2 PHE A 159 2347 2526 2320 -95 82 -146 ATOM 1224 CE1 PHE A 159 -2.126 20.466 -38.330 1.00 23.34 C ANISOU 1224 CE1 PHE A 159 2915 3060 2894 -136 62 -86 ATOM 1225 CE2 PHE A 159 -0.958 19.115 -39.947 1.00 16.63 C ANISOU 1225 CE2 PHE A 159 2045 2270 2005 -125 76 -130 ATOM 1226 CZ PHE A 159 -1.551 20.318 -39.586 1.00 25.67 C ANISOU 1226 CZ PHE A 159 3196 3398 3159 -147 63 -98 ATOM 1227 N CYS A 160 -1.155 16.325 -33.513 1.00 24.31 N ANISOU 1227 N CYS A 160 3068 3069 3098 -28 93 -114 ATOM 1228 CA CYS A 160 -1.213 15.371 -32.408 1.00 21.10 C ANISOU 1228 CA CYS A 160 2671 2630 2714 -14 92 -111 ATOM 1229 C CYS A 160 -2.579 15.266 -31.747 1.00 20.80 C ANISOU 1229 C CYS A 160 2641 2567 2693 -26 88 -92 ATOM 1230 O CYS A 160 -2.856 14.226 -31.158 1.00 23.36 O ANISOU 1230 O CYS A 160 2973 2867 3036 -20 82 -87 ATOM 1231 CB CYS A 160 -0.101 15.614 -31.378 1.00 26.97 C ANISOU 1231 CB CYS A 160 3412 3378 3457 -1 98 -102 ATOM 1232 SG CYS A 160 -0.280 17.203 -30.510 1.00 23.69 S ANISOU 1232 SG CYS A 160 2993 2975 3034 -12 102 -76 ATOM 1233 N TYR A 161 -3.399 16.313 -31.844 1.00 18.20 N ANISOU 1233 N TYR A 161 2310 2246 2360 -41 88 -79 ATOM 1234 CA TYR A 161 -4.699 16.351 -31.203 1.00 21.68 C ANISOU 1234 CA TYR A 161 2752 2673 2814 -50 87 -61 ATOM 1235 C TYR A 161 -5.712 16.913 -32.197 1.00 17.94 C ANISOU 1235 C TYR A 161 2276 2205 2336 -66 82 -60 ATOM 1236 O TYR A 161 -5.371 17.758 -33.021 1.00 16.60 O ANISOU 1236 O TYR A 161 2102 2053 2154 -72 80 -62 ATOM 1237 CB TYR A 161 -4.574 17.156 -29.893 1.00 19.18 C ANISOU 1237 CB TYR A 161 2430 2362 2494 -44 92 -45 ATOM 1238 CG TYR A 161 -5.839 17.332 -29.073 1.00 17.53 C ANISOU 1238 CG TYR A 161 2216 2152 2292 -49 92 -29 ATOM 1239 CD1 TYR A 161 -6.229 16.335 -28.154 1.00 20.60 C ANISOU 1239 CD1 TYR A 161 2605 2532 2691 -50 93 -15 ATOM 1240 CD2 TYR A 161 -6.608 18.509 -29.200 1.00 17.78 C ANISOU 1240 CD2 TYR A 161 2241 2195 2318 -54 89 -26 ATOM 1241 CE1 TYR A 161 -7.371 16.521 -27.353 1.00 20.07 C ANISOU 1241 CE1 TYR A 161 2527 2475 2623 -57 94 0 ATOM 1242 CE2 TYR A 161 -7.756 18.688 -28.406 1.00 14.78 C ANISOU 1242 CE2 TYR A 161 1852 1822 1941 -55 89 -16 ATOM 1243 CZ TYR A 161 -8.137 17.697 -27.479 1.00 15.02 C ANISOU 1243 CZ TYR A 161 1878 1851 1976 -57 94 -3 ATOM 1244 OH TYR A 161 -9.241 17.877 -26.698 1.00 15.24 O ANISOU 1244 OH TYR A 161 1892 1896 2002 -60 96 8 ATOM 1245 N MET A 162 -6.945 16.430 -32.070 1.00 17.49 N ANISOU 1245 N MET A 162 2220 2134 2291 -75 78 -52 ATOM 1246 CA MET A 162 -8.145 17.014 -32.632 1.00 20.07 C ANISOU 1246 CA MET A 162 2543 2465 2618 -90 72 -47 ATOM 1247 C MET A 162 -9.144 17.045 -31.480 1.00 27.35 C ANISOU 1247 C MET A 162 3458 3387 3548 -92 74 -29 ATOM 1248 O MET A 162 -9.296 16.036 -30.792 1.00 14.99 O ANISOU 1248 O MET A 162 1892 1811 1991 -94 74 -19 ATOM 1249 CB MET A 162 -8.629 16.185 -33.838 1.00 17.26 C ANISOU 1249 CB MET A 162 2192 2099 2265 -102 64 -58 ATOM 1250 CG MET A 162 -9.979 16.653 -34.402 1.00 18.23 C ANISOU 1250 CG MET A 162 2311 2225 2391 -118 58 -50 ATOM 1251 SD MET A 162 -10.408 15.949 -36.014 1.00 27.07 S ANISOU 1251 SD MET A 162 3439 3335 3511 -133 47 -64 ATOM 1252 CE MET A 162 -9.468 17.059 -37.097 1.00 30.70 C ANISOU 1252 CE MET A 162 3896 3821 3948 -136 47 -78 ATOM 1253 N HIS A 163 -9.787 18.202 -31.277 1.00 21.66 N ANISOU 1253 N HIS A 163 2727 2679 2823 -92 72 -26 ATOM 1254 CA HIS A 163 -10.786 18.390 -30.236 1.00 25.14 C ANISOU 1254 CA HIS A 163 3155 3131 3266 -88 75 -14 ATOM 1255 C HIS A 163 -12.111 17.727 -30.628 1.00 11.66 C ANISOU 1255 C HIS A 163 1443 1422 1567 -104 71 -5 ATOM 1256 O HIS A 163 -12.559 17.906 -31.761 1.00 16.62 O ANISOU 1256 O HIS A 163 2073 2045 2197 -115 63 -10 ATOM 1257 CB HIS A 163 -10.969 19.894 -29.977 1.00 16.61 C ANISOU 1257 CB HIS A 163 2067 2066 2180 -78 69 -19 ATOM 1258 CG HIS A 163 -11.873 20.160 -28.807 1.00 16.69 C ANISOU 1258 CG HIS A 163 2059 2095 2188 -69 72 -13 ATOM 1259 ND1 HIS A 163 -11.618 19.655 -27.526 1.00 16.01 N ANISOU 1259 ND1 HIS A 163 1967 2020 2098 -62 83 -3 ATOM 1260 CD2 HIS A 163 -13.075 20.827 -28.796 1.00 12.53 C ANISOU 1260 CD2 HIS A 163 1517 1582 1661 -66 65 -16 ATOM 1261 CE1 HIS A 163 -12.665 20.033 -26.806 1.00 14.24 C ANISOU 1261 CE1 HIS A 163 1722 1822 1868 -57 85 0 ATOM 1262 NE2 HIS A 163 -13.554 20.732 -27.506 1.00 17.54 N ANISOU 1262 NE2 HIS A 163 2133 2242 2288 -56 74 -10 ATOM 1263 N HIS A 164 -12.711 16.990 -29.681 1.00 19.03 N ANISOU 1263 N HIS A 164 2368 2360 2502 -109 75 12 ATOM 1264 CA HIS A 164 -14.003 16.339 -29.876 1.00 17.82 C ANISOU 1264 CA HIS A 164 2206 2210 2354 -127 69 25 ATOM 1265 C HIS A 164 -15.057 16.877 -28.917 1.00 17.76 C ANISOU 1265 C HIS A 164 2173 2236 2338 -125 74 36 ATOM 1266 O HIS A 164 -16.178 17.085 -29.364 1.00 18.54 O ANISOU 1266 O HIS A 164 2259 2347 2438 -133 69 38 ATOM 1267 CB HIS A 164 -13.886 14.810 -29.737 1.00 16.64 C ANISOU 1267 CB HIS A 164 2067 2041 2216 -143 62 40 ATOM 1268 CG HIS A 164 -13.326 14.139 -30.963 1.00 24.15 C ANISOU 1268 CG HIS A 164 3039 2960 3177 -146 51 25 ATOM 1269 ND1 HIS A 164 -14.005 13.120 -31.634 1.00 21.79 N ANISOU 1269 ND1 HIS A 164 2747 2643 2890 -165 36 29 ATOM 1270 CD2 HIS A 164 -12.151 14.397 -31.634 1.00 16.48 C ANISOU 1270 CD2 HIS A 164 2082 1976 2204 -133 52 4 ATOM 1271 CE1 HIS A 164 -13.228 12.826 -32.667 1.00 21.10 C ANISOU 1271 CE1 HIS A 164 2678 2534 2807 -159 29 8 ATOM 1272 NE2 HIS A 164 -12.125 13.563 -32.731 1.00 16.09 N ANISOU 1272 NE2 HIS A 164 2046 1905 2163 -140 39 -8 ATOM 1273 N MET A 165 -14.736 17.059 -27.628 1.00 16.24 N ANISOU 1273 N MET A 165 1970 2066 2136 -114 83 43 ATOM 1274 CA MET A 165 -15.770 17.339 -26.633 1.00 23.66 C ANISOU 1274 CA MET A 165 2881 3047 3064 -114 87 52 ATOM 1275 C MET A 165 -15.180 17.874 -25.329 1.00 13.37 C ANISOU 1275 C MET A 165 1565 1771 1745 -94 97 51 ATOM 1276 O MET A 165 -14.012 17.651 -25.022 1.00 22.88 O ANISOU 1276 O MET A 165 2785 2960 2950 -86 100 49 ATOM 1277 CB MET A 165 -16.611 16.058 -26.382 1.00 29.61 C ANISOU 1277 CB MET A 165 3624 3809 3818 -142 84 82 ATOM 1278 CG MET A 165 -15.835 14.924 -25.697 1.00 29.54 C ANISOU 1278 CG MET A 165 3626 3786 3812 -153 83 102 ATOM 1279 SD MET A 165 -16.672 13.326 -25.705 1.00 38.85 S ANISOU 1279 SD MET A 165 4803 4959 5002 -193 66 141 ATOM 1280 CE MET A 165 -15.487 12.459 -24.650 1.00 40.09 C ANISOU 1280 CE MET A 165 4966 5108 5157 -198 63 163 ATOM 1281 N GLU A 166 -16.064 18.513 -24.560 1.00 14.10 N ANISOU 1281 N GLU A 166 1628 1909 1822 -87 101 51 ATOM 1282 CA GLU A 166 -15.849 18.925 -23.184 1.00 22.51 C ANISOU 1282 CA GLU A 166 2675 3011 2868 -67 110 47 ATOM 1283 C GLU A 166 -16.536 17.907 -22.259 1.00 23.20 C ANISOU 1283 C GLU A 166 2738 3137 2938 -89 118 78 ATOM 1284 O GLU A 166 -17.663 17.493 -22.528 1.00 24.71 O ANISOU 1284 O GLU A 166 2913 3346 3129 -111 115 96 ATOM 1285 CB GLU A 166 -16.415 20.351 -23.038 1.00 26.20 C ANISOU 1285 CB GLU A 166 3124 3505 3326 -36 106 16 ATOM 1286 CG GLU A 166 -16.156 21.002 -21.670 1.00 31.17 C ANISOU 1286 CG GLU A 166 3735 4174 3934 -10 112 4 ATOM 1287 CD GLU A 166 -16.606 22.459 -21.651 1.00 39.82 C ANISOU 1287 CD GLU A 166 4819 5284 5028 26 99 -34 ATOM 1288 OE1 GLU A 166 -17.704 22.709 -21.110 1.00 38.66 O ANISOU 1288 OE1 GLU A 166 4637 5185 4865 38 100 -45 ATOM 1289 OE2 GLU A 166 -15.851 23.301 -22.185 1.00 32.92 O1- ANISOU 1289 OE2 GLU A 166 3967 4374 4166 43 85 -54 ATOM 1290 N LEU A 167 -15.848 17.535 -21.172 1.00 23.16 N ANISOU 1290 N LEU A 167 2732 3148 2922 -87 125 89 ATOM 1291 CA LEU A 167 -16.403 16.747 -20.071 1.00 33.58 C ANISOU 1291 CA LEU A 167 4024 4515 4221 -109 130 122 ATOM 1292 C LEU A 167 -17.191 17.683 -19.128 1.00 38.94 C ANISOU 1292 C LEU A 167 4662 5265 4867 -87 140 106 ATOM 1293 O LEU A 167 -16.836 18.859 -19.047 1.00 35.92 O ANISOU 1293 O LEU A 167 4280 4886 4482 -50 141 69 ATOM 1294 CB LEU A 167 -15.245 16.070 -19.298 1.00 25.03 C ANISOU 1294 CB LEU A 167 2956 3417 3138 -120 130 144 ATOM 1295 CG LEU A 167 -14.352 15.126 -20.139 1.00 26.19 C ANISOU 1295 CG LEU A 167 3142 3493 3315 -131 118 149 ATOM 1296 CD1 LEU A 167 -13.235 14.511 -19.273 1.00 38.94 C ANISOU 1296 CD1 LEU A 167 4769 5097 4929 -134 116 166 ATOM 1297 CD2 LEU A 167 -15.157 14.041 -20.879 1.00 29.35 C ANISOU 1297 CD2 LEU A 167 3548 3873 3731 -165 103 174 ATOM 1298 N PRO A 168 -18.194 17.164 -18.380 1.00 54.25 N ANISOU 1298 N PRO A 168 6566 7266 6783 -109 145 134 ATOM 1299 CA PRO A 168 -18.885 17.919 -17.307 1.00 55.96 C ANISOU 1299 CA PRO A 168 6738 7561 6963 -84 156 115 ATOM 1300 C PRO A 168 -18.011 18.669 -16.273 1.00 51.07 C ANISOU 1300 C PRO A 168 6121 6954 6329 -51 162 91 ATOM 1301 O PRO A 168 -18.484 19.653 -15.706 1.00 57.32 O ANISOU 1301 O PRO A 168 6888 7788 7102 -14 165 53 ATOM 1302 CB PRO A 168 -19.761 16.858 -16.627 1.00 67.74 C ANISOU 1302 CB PRO A 168 8194 9116 8429 -125 160 161 ATOM 1303 CG PRO A 168 -20.077 15.868 -17.735 1.00 65.70 C ANISOU 1303 CG PRO A 168 7955 8809 8199 -163 147 191 ATOM 1304 CD PRO A 168 -18.800 15.844 -18.567 1.00 54.98 C ANISOU 1304 CD PRO A 168 6651 7360 6878 -156 138 179 ATOM 1305 N THR A 169 -16.755 18.227 -16.081 1.00 42.74 N ANISOU 1305 N THR A 169 5094 5861 5284 -62 162 108 ATOM 1306 CA THR A 169 -15.739 18.881 -15.248 1.00 39.30 C ANISOU 1306 CA THR A 169 4666 5429 4838 -31 165 85 ATOM 1307 C THR A 169 -15.192 20.220 -15.811 1.00 42.66 C ANISOU 1307 C THR A 169 5112 5814 5282 10 156 38 ATOM 1308 O THR A 169 -14.503 20.936 -15.084 1.00 35.37 O ANISOU 1308 O THR A 169 4193 4897 4350 40 155 14 ATOM 1309 CB THR A 169 -14.499 17.969 -14.994 1.00 44.53 C ANISOU 1309 CB THR A 169 5358 6050 5513 -52 163 114 ATOM 1310 OG1 THR A 169 -14.784 16.597 -15.187 1.00 51.00 O ANISOU 1310 OG1 THR A 169 6184 6848 6347 -96 156 156 ATOM 1311 CG2 THR A 169 -13.959 18.091 -13.560 1.00 64.00 C ANISOU 1311 CG2 THR A 169 7803 8567 7946 -50 172 124 ATOM 1312 N GLY A 170 -15.482 20.522 -17.090 1.00 39.05 N ANISOU 1312 N GLY A 170 4671 5316 4850 9 147 27 ATOM 1313 CA GLY A 170 -15.017 21.711 -17.811 1.00 40.61 C ANISOU 1313 CA GLY A 170 4892 5471 5067 38 133 -9 ATOM 1314 C GLY A 170 -13.666 21.482 -18.511 1.00 45.22 C ANISOU 1314 C GLY A 170 5517 5990 5674 32 129 -3 ATOM 1315 O GLY A 170 -13.173 22.398 -19.170 1.00 30.93 O ANISOU 1315 O GLY A 170 3726 4149 3877 53 116 -28 ATOM 1316 N VAL A 171 -13.076 20.280 -18.385 1.00 35.01 N ANISOU 1316 N VAL A 171 4237 4678 4386 4 136 29 ATOM 1317 CA VAL A 171 -11.851 19.867 -19.069 1.00 37.27 C ANISOU 1317 CA VAL A 171 4558 4908 4694 -2 132 33 ATOM 1318 C VAL A 171 -12.199 19.130 -20.373 1.00 26.44 C ANISOU 1318 C VAL A 171 3200 3501 3344 -25 126 42 ATOM 1319 O VAL A 171 -13.338 18.704 -20.557 1.00 21.83 O ANISOU 1319 O VAL A 171 2601 2935 2759 -39 126 51 ATOM 1320 CB VAL A 171 -10.985 18.945 -18.169 1.00 35.62 C ANISOU 1320 CB VAL A 171 4357 4696 4481 -14 138 58 ATOM 1321 CG1 VAL A 171 -10.621 19.666 -16.860 1.00 38.72 C ANISOU 1321 CG1 VAL A 171 4734 5127 4850 8 143 48 ATOM 1322 CG2 VAL A 171 -11.576 17.546 -17.902 1.00 24.24 C ANISOU 1322 CG2 VAL A 171 2906 3267 3039 -49 139 94 ATOM 1323 N HIS A 172 -11.215 19.046 -21.273 1.00 22.22 N ANISOU 1323 N HIS A 172 2695 2920 2828 -27 121 38 ATOM 1324 CA HIS A 172 -11.433 18.724 -22.680 1.00 23.01 C ANISOU 1324 CA HIS A 172 2809 2988 2945 -41 114 36 ATOM 1325 C HIS A 172 -10.819 17.378 -23.058 1.00 20.49 C ANISOU 1325 C HIS A 172 2508 2636 2640 -61 112 53 ATOM 1326 O HIS A 172 -9.782 16.996 -22.515 1.00 24.68 O ANISOU 1326 O HIS A 172 3049 3157 3172 -58 114 60 ATOM 1327 CB HIS A 172 -10.878 19.891 -23.511 1.00 21.06 C ANISOU 1327 CB HIS A 172 2575 2722 2705 -25 106 12 ATOM 1328 CG HIS A 172 -11.576 21.183 -23.167 1.00 20.59 C ANISOU 1328 CG HIS A 172 2498 2688 2636 -4 99 -7 ATOM 1329 ND1 HIS A 172 -10.948 22.226 -22.478 1.00 19.06 N ANISOU 1329 ND1 HIS A 172 2306 2499 2436 20 93 -23 ATOM 1330 CD2 HIS A 172 -12.894 21.521 -23.381 1.00 21.15 C ANISOU 1330 CD2 HIS A 172 2550 2783 2704 -1 95 -14 ATOM 1331 CE1 HIS A 172 -11.905 23.126 -22.287 1.00 21.96 C ANISOU 1331 CE1 HIS A 172 2657 2889 2799 39 83 -42 ATOM 1332 NE2 HIS A 172 -13.080 22.755 -22.790 1.00 25.50 N ANISOU 1332 NE2 HIS A 172 3091 3351 3248 28 85 -38 ATOM 1333 N ALA A 173 -11.502 16.691 -23.984 1.00 23.99 N ANISOU 1333 N ALA A 173 2957 3064 3096 -79 105 58 ATOM 1334 CA ALA A 173 -11.160 15.364 -24.470 1.00 22.08 C ANISOU 1334 CA ALA A 173 2733 2788 2869 -94 97 69 ATOM 1335 C ALA A 173 -11.226 15.319 -26.001 1.00 16.24 C ANISOU 1335 C ALA A 173 2007 2021 2142 -100 89 54 ATOM 1336 O ALA A 173 -12.069 15.978 -26.615 1.00 15.81 O ANISOU 1336 O ALA A 173 1945 1975 2086 -104 88 48 ATOM 1337 CB ALA A 173 -12.105 14.330 -23.838 1.00 29.49 C ANISOU 1337 CB ALA A 173 3660 3736 3808 -120 90 101 ATOM 1338 N GLY A 174 -10.320 14.529 -26.585 1.00 19.75 N ANISOU 1338 N GLY A 174 2472 2434 2599 -100 81 48 ATOM 1339 CA GLY A 174 -10.159 14.451 -28.025 1.00 22.39 C ANISOU 1339 CA GLY A 174 2819 2747 2941 -102 74 29 ATOM 1340 C GLY A 174 -9.263 13.269 -28.383 1.00 17.46 C ANISOU 1340 C GLY A 174 2213 2092 2330 -99 62 21 ATOM 1341 O GLY A 174 -8.893 12.450 -27.539 1.00 17.82 O ANISOU 1341 O GLY A 174 2261 2125 2383 -101 54 35 ATOM 1342 N THR A 175 -8.959 13.188 -29.682 1.00 20.16 N ANISOU 1342 N THR A 175 2565 2423 2674 -94 58 -3 ATOM 1343 CA THR A 175 -8.303 12.062 -30.332 1.00 22.74 C ANISOU 1343 CA THR A 175 2906 2722 3012 -89 43 -20 ATOM 1344 C THR A 175 -6.998 12.505 -31.002 1.00 19.12 C ANISOU 1344 C THR A 175 2451 2273 2543 -69 50 -48 ATOM 1345 O THR A 175 -6.798 13.697 -31.221 1.00 20.80 O ANISOU 1345 O THR A 175 2654 2509 2738 -66 64 -52 ATOM 1346 CB THR A 175 -9.233 11.507 -31.451 1.00 17.89 C ANISOU 1346 CB THR A 175 2299 2093 2407 -104 28 -25 ATOM 1347 OG1 THR A 175 -9.379 12.389 -32.553 1.00 16.28 O ANISOU 1347 OG1 THR A 175 2091 1908 2188 -104 38 -42 ATOM 1348 CG2 THR A 175 -10.630 11.097 -30.972 1.00 13.34 C ANISOU 1348 CG2 THR A 175 1716 1516 1838 -127 21 6 ATOM 1349 N ASP A 176 -6.176 11.520 -31.401 1.00 18.82 N ANISOU 1349 N ASP A 176 2423 2216 2513 -56 38 -68 ATOM 1350 CA ASP A 176 -5.154 11.693 -32.439 1.00 18.49 C ANISOU 1350 CA ASP A 176 2380 2189 2458 -39 42 -100 ATOM 1351 C ASP A 176 -5.833 11.832 -33.824 1.00 20.03 C ANISOU 1351 C ASP A 176 2575 2390 2646 -49 38 -116 ATOM 1352 O ASP A 176 -7.046 11.653 -33.941 1.00 21.56 O ANISOU 1352 O ASP A 176 2772 2573 2848 -68 32 -102 ATOM 1353 CB ASP A 176 -4.087 10.564 -32.421 1.00 20.39 C ANISOU 1353 CB ASP A 176 2627 2411 2708 -16 28 -123 ATOM 1354 CG ASP A 176 -4.609 9.124 -32.444 1.00 24.07 C ANISOU 1354 CG ASP A 176 3108 2838 3200 -18 -1 -128 ATOM 1355 OD1 ASP A 176 -5.671 8.889 -33.058 1.00 25.27 O ANISOU 1355 OD1 ASP A 176 3264 2983 3355 -34 -10 -128 ATOM 1356 OD2 ASP A 176 -3.875 8.256 -31.922 1.00 27.44 O1- ANISOU 1356 OD2 ASP A 176 3544 3239 3645 -5 -20 -132 ATOM 1357 N LEU A 177 -5.050 12.121 -34.872 1.00 23.36 N ANISOU 1357 N LEU A 177 2991 2834 3049 -39 43 -143 ATOM 1358 CA LEU A 177 -5.570 12.263 -36.237 1.00 15.10 C ANISOU 1358 CA LEU A 177 1945 1800 1993 -51 39 -156 ATOM 1359 C LEU A 177 -5.936 10.926 -36.926 1.00 27.78 C ANISOU 1359 C LEU A 177 3563 3379 3612 -45 17 -180 ATOM 1360 O LEU A 177 -6.471 10.970 -38.035 1.00 27.09 O ANISOU 1360 O LEU A 177 3475 3301 3515 -53 13 -194 ATOM 1361 CB LEU A 177 -4.619 13.158 -37.064 1.00 26.34 C ANISOU 1361 CB LEU A 177 3355 3267 3386 -48 52 -173 ATOM 1362 CG LEU A 177 -4.854 14.676 -36.866 1.00 20.52 C ANISOU 1362 CG LEU A 177 2609 2554 2636 -66 64 -147 ATOM 1363 CD1 LEU A 177 -6.212 15.131 -37.435 1.00 24.02 C ANISOU 1363 CD1 LEU A 177 3053 2994 3078 -90 58 -136 ATOM 1364 CD2 LEU A 177 -4.646 15.151 -35.414 1.00 26.39 C ANISOU 1364 CD2 LEU A 177 3352 3284 3389 -64 70 -121 ATOM 1365 N GLU A 178 -5.727 9.782 -36.245 1.00 31.47 N ANISOU 1365 N GLU A 178 4042 3812 4104 -32 -1 -182 ATOM 1366 CA GLU A 178 -6.287 8.474 -36.609 1.00 29.66 C ANISOU 1366 CA GLU A 178 3828 3546 3896 -32 -31 -194 ATOM 1367 C GLU A 178 -7.667 8.207 -35.971 1.00 23.84 C ANISOU 1367 C GLU A 178 3098 2780 3180 -59 -42 -155 ATOM 1368 O GLU A 178 -8.281 7.195 -36.306 1.00 30.79 O ANISOU 1368 O GLU A 178 3993 3625 4082 -65 -72 -156 ATOM 1369 CB GLU A 178 -5.291 7.357 -36.239 1.00 21.58 C ANISOU 1369 CB GLU A 178 2813 2496 2889 -3 -54 -220 ATOM 1370 CG GLU A 178 -3.971 7.441 -37.030 1.00 36.96 C ANISOU 1370 CG GLU A 178 4750 4477 4815 27 -44 -263 ATOM 1371 CD GLU A 178 -3.022 6.266 -36.775 1.00 61.35 C ANISOU 1371 CD GLU A 178 7846 7538 7924 61 -72 -293 ATOM 1372 OE1 GLU A 178 -3.261 5.501 -35.814 1.00 67.87 O ANISOU 1372 OE1 GLU A 178 8687 8320 8781 57 -94 -271 ATOM 1373 OE2 GLU A 178 -2.056 6.155 -37.560 1.00 59.40 O1- ANISOU 1373 OE2 GLU A 178 7590 7317 7661 90 -73 -339 ATOM 1374 N GLY A 179 -8.139 9.102 -35.088 1.00 20.52 N ANISOU 1374 N GLY A 179 2668 2376 2754 -76 -21 -121 ATOM 1375 CA GLY A 179 -9.455 9.031 -34.461 1.00 18.33 C ANISOU 1375 CA GLY A 179 2390 2086 2490 -102 -28 -84 ATOM 1376 C GLY A 179 -9.478 8.176 -33.185 1.00 14.60 C ANISOU 1376 C GLY A 179 1922 1590 2036 -108 -43 -57 ATOM 1377 O GLY A 179 -10.566 7.875 -32.705 1.00 21.64 O ANISOU 1377 O GLY A 179 2812 2473 2938 -134 -54 -24 ATOM 1378 N ASN A 180 -8.323 7.793 -32.618 1.00 19.03 N ANISOU 1378 N ASN A 180 2486 2144 2601 -88 -45 -66 ATOM 1379 CA ASN A 180 -8.252 7.107 -31.324 1.00 23.13 C ANISOU 1379 CA ASN A 180 3010 2642 3138 -95 -62 -37 ATOM 1380 C ASN A 180 -8.207 8.155 -30.207 1.00 26.26 C ANISOU 1380 C ASN A 180 3390 3071 3518 -99 -33 -11 ATOM 1381 O ASN A 180 -7.268 8.950 -30.179 1.00 23.18 O ANISOU 1381 O ASN A 180 2994 2701 3113 -79 -12 -28 ATOM 1382 CB ASN A 180 -7.000 6.205 -31.248 1.00 26.01 C ANISOU 1382 CB ASN A 180 3388 2978 3518 -69 -84 -62 ATOM 1383 CG ASN A 180 -6.971 5.097 -32.298 1.00 27.89 C ANISOU 1383 CG ASN A 180 3643 3179 3775 -60 -120 -92 ATOM 1384 OD1 ASN A 180 -6.071 5.052 -33.131 1.00 27.48 O ANISOU 1384 OD1 ASN A 180 3601 3099 3742 -82 -148 -74 ATOM 1385 ND2 ASN A 180 -7.943 4.187 -32.251 1.00 34.89 N ANISOU 1385 ND2 ASN A 180 4531 4068 4656 -26 -121 -139 ATOM 1386 N PHE A 181 -9.194 8.119 -29.294 1.00 19.18 N ANISOU 1386 N PHE A 181 2485 2181 2623 -125 -35 28 ATOM 1387 CA PHE A 181 -9.241 8.953 -28.089 1.00 20.10 C ANISOU 1387 CA PHE A 181 2582 2332 2721 -127 -10 50 ATOM 1388 C PHE A 181 -8.004 8.792 -27.202 1.00 19.51 C ANISOU 1388 C PHE A 181 2511 2252 2648 -110 -8 48 ATOM 1389 O PHE A 181 -7.578 7.666 -26.942 1.00 19.31 O ANISOU 1389 O PHE A 181 2501 2195 2642 -105 -33 46 ATOM 1390 CB PHE A 181 -10.523 8.700 -27.258 1.00 20.79 C ANISOU 1390 CB PHE A 181 2657 2434 2808 -158 -15 93 ATOM 1391 CG PHE A 181 -11.694 9.606 -27.594 1.00 21.91 C ANISOU 1391 CG PHE A 181 2782 2606 2935 -169 1 97 ATOM 1392 CD1 PHE A 181 -11.777 10.893 -27.018 1.00 22.91 C ANISOU 1392 CD1 PHE A 181 2889 2775 3041 -160 28 97 ATOM 1393 CD2 PHE A 181 -12.629 9.239 -28.583 1.00 23.70 C ANISOU 1393 CD2 PHE A 181 3014 2820 3172 -185 -13 96 ATOM 1394 CE1 PHE A 181 -12.809 11.750 -27.376 1.00 26.87 C ANISOU 1394 CE1 PHE A 181 3376 3303 3532 -165 39 96 ATOM 1395 CE2 PHE A 181 -13.657 10.109 -28.923 1.00 20.18 C ANISOU 1395 CE2 PHE A 181 2552 2402 2714 -193 0 98 ATOM 1396 CZ PHE A 181 -13.750 11.356 -28.318 1.00 22.29 C ANISOU 1396 CZ PHE A 181 2799 2710 2961 -182 26 97 ATOM 1397 N TYR A 182 -7.499 9.930 -26.707 1.00 15.54 N ANISOU 1397 N TYR A 182 1997 1782 2126 -98 19 47 ATOM 1398 CA TYR A 182 -6.645 9.972 -25.529 1.00 16.03 C ANISOU 1398 CA TYR A 182 2057 1848 2185 -88 23 56 ATOM 1399 C TYR A 182 -7.519 9.697 -24.304 1.00 17.98 C ANISOU 1399 C TYR A 182 2292 2110 2429 -112 19 97 ATOM 1400 O TYR A 182 -8.528 10.374 -24.119 1.00 26.40 O ANISOU 1400 O TYR A 182 3342 3208 3480 -124 33 111 ATOM 1401 CB TYR A 182 -5.956 11.342 -25.429 1.00 20.68 C ANISOU 1401 CB TYR A 182 2637 2466 2754 -68 50 40 ATOM 1402 CG TYR A 182 -4.936 11.588 -26.514 1.00 16.41 C ANISOU 1402 CG TYR A 182 2104 1919 2211 -47 53 5 ATOM 1403 CD1 TYR A 182 -3.666 10.987 -26.417 1.00 24.97 C ANISOU 1403 CD1 TYR A 182 3196 2990 3302 -28 47 -9 ATOM 1404 CD2 TYR A 182 -5.248 12.414 -27.614 1.00 19.95 C ANISOU 1404 CD2 TYR A 182 2550 2380 2650 -47 61 -13 ATOM 1405 CE1 TYR A 182 -2.708 11.219 -27.417 1.00 24.28 C ANISOU 1405 CE1 TYR A 182 3110 2908 3209 -10 51 -41 ATOM 1406 CE2 TYR A 182 -4.283 12.653 -28.607 1.00 15.97 C ANISOU 1406 CE2 TYR A 182 2048 1880 2139 -32 65 -42 ATOM 1407 CZ TYR A 182 -3.013 12.056 -28.505 1.00 23.77 C ANISOU 1407 CZ TYR A 182 3041 2861 3131 -13 60 -56 ATOM 1408 OH TYR A 182 -2.070 12.288 -29.455 1.00 25.27 O ANISOU 1408 OH TYR A 182 3227 3064 3309 1 64 -84 ATOM 1409 N GLY A 183 -7.124 8.701 -23.502 1.00 28.08 N ANISOU 1409 N GLY A 183 3580 3368 3723 -120 -2 118 ATOM 1410 CA GLY A 183 -7.851 8.315 -22.300 1.00 36.88 C ANISOU 1410 CA GLY A 183 4681 4502 4832 -148 -9 161 ATOM 1411 C GLY A 183 -9.023 7.376 -22.623 1.00 40.57 C ANISOU 1411 C GLY A 183 5148 4956 5310 -181 -34 187 ATOM 1412 O GLY A 183 -9.216 6.978 -23.774 1.00 31.58 O ANISOU 1412 O GLY A 183 4023 3789 4187 -180 -48 169 ATOM 1413 N PRO A 184 -9.815 7.019 -21.590 1.00 35.69 N ANISOU 1413 N PRO A 184 4513 4364 4682 -213 -40 232 ATOM 1414 CA PRO A 184 -10.944 6.079 -21.711 1.00 35.71 C ANISOU 1414 CA PRO A 184 4515 4357 4697 -251 -70 266 ATOM 1415 C PRO A 184 -12.239 6.682 -22.304 1.00 37.04 C ANISOU 1415 C PRO A 184 4664 4558 4850 -263 -54 267 ATOM 1416 O PRO A 184 -13.270 6.012 -22.262 1.00 45.37 O ANISOU 1416 O PRO A 184 5710 5620 5907 -299 -74 302 ATOM 1417 CB PRO A 184 -11.139 5.620 -20.253 1.00 36.39 C ANISOU 1417 CB PRO A 184 4586 4468 4772 -283 -82 317 ATOM 1418 CG PRO A 184 -10.768 6.840 -19.423 1.00 37.09 C ANISOU 1418 CG PRO A 184 4655 4608 4830 -261 -42 306 ATOM 1419 CD PRO A 184 -9.605 7.438 -20.200 1.00 31.18 C ANISOU 1419 CD PRO A 184 3925 3832 4089 -216 -26 255 ATOM 1420 N PHE A 185 -12.184 7.922 -22.820 1.00 28.83 N ANISOU 1420 N PHE A 185 3619 3538 3797 -235 -22 230 ATOM 1421 CA PHE A 185 -13.355 8.697 -23.227 1.00 27.84 C ANISOU 1421 CA PHE A 185 3472 3452 3655 -243 -6 231 ATOM 1422 C PHE A 185 -13.929 8.236 -24.580 1.00 31.30 C ANISOU 1422 C PHE A 185 3924 3857 4112 -252 -23 221 ATOM 1423 O PHE A 185 -13.195 7.706 -25.414 1.00 27.75 O ANISOU 1423 O PHE A 185 3501 3358 3683 -239 -39 196 ATOM 1424 CB PHE A 185 -12.981 10.193 -23.259 1.00 36.20 C ANISOU 1424 CB PHE A 185 4519 4544 4693 -210 29 198 ATOM 1425 CG PHE A 185 -12.267 10.693 -22.014 1.00 26.33 C ANISOU 1425 CG PHE A 185 3260 3317 3426 -196 44 201 ATOM 1426 CD1 PHE A 185 -12.860 10.565 -20.740 1.00 26.03 C ANISOU 1426 CD1 PHE A 185 3195 3327 3366 -214 48 234 ATOM 1427 CD2 PHE A 185 -10.979 11.256 -22.120 1.00 16.96 C ANISOU 1427 CD2 PHE A 185 2090 2110 2244 -166 52 172 ATOM 1428 CE1 PHE A 185 -12.155 10.958 -19.610 1.00 16.75 C ANISOU 1428 CE1 PHE A 185 2013 2176 2176 -201 61 235 ATOM 1429 CE2 PHE A 185 -10.292 11.644 -20.979 1.00 24.35 C ANISOU 1429 CE2 PHE A 185 3019 3067 3165 -153 64 176 ATOM 1430 CZ PHE A 185 -10.876 11.488 -19.728 1.00 27.08 C ANISOU 1430 CZ PHE A 185 3342 3457 3492 -170 68 206 ATOM 1431 N VAL A 186 -15.241 8.452 -24.751 1.00 29.77 N ANISOU 1431 N VAL A 186 3709 3694 3908 -272 -19 237 ATOM 1432 CA VAL A 186 -16.048 8.029 -25.897 1.00 20.61 C ANISOU 1432 CA VAL A 186 2558 2510 2763 -287 -36 235 ATOM 1433 C VAL A 186 -16.920 9.190 -26.414 1.00 26.24 C ANISOU 1433 C VAL A 186 3252 3260 3460 -277 -12 217 ATOM 1434 O VAL A 186 -17.420 9.976 -25.610 1.00 23.45 O ANISOU 1434 O VAL A 186 2871 2958 3083 -270 12 220 ATOM 1435 CB VAL A 186 -16.991 6.850 -25.505 1.00 28.96 C ANISOU 1435 CB VAL A 186 3609 3565 3829 -333 -69 284 ATOM 1436 CG1 VAL A 186 -16.213 5.535 -25.329 1.00 26.77 C ANISOU 1436 CG1 VAL A 186 3358 3238 3576 -341 -104 298 ATOM 1437 CG2 VAL A 186 -17.874 7.112 -24.264 1.00 30.81 C ANISOU 1437 CG2 VAL A 186 3802 3872 4033 -354 -52 321 ATOM 1438 N ASP A 187 -17.108 9.270 -27.745 1.00 19.59 N ANISOU 1438 N ASP A 187 2424 2389 2630 -276 -20 196 ATOM 1439 CA ASP A 187 -17.878 10.328 -28.422 1.00 29.32 C ANISOU 1439 CA ASP A 187 3641 3647 3850 -266 -1 176 ATOM 1440 C ASP A 187 -19.400 10.091 -28.328 1.00 21.21 C ANISOU 1440 C ASP A 187 2592 2647 2820 -297 -9 206 ATOM 1441 O ASP A 187 -20.058 9.827 -29.335 1.00 24.41 O ANISOU 1441 O ASP A 187 3004 3035 3236 -308 -21 202 ATOM 1442 CB ASP A 187 -17.423 10.612 -29.882 1.00 17.11 C ANISOU 1442 CB ASP A 187 2119 2066 2314 -247 -2 138 ATOM 1443 CG ASP A 187 -17.258 9.405 -30.817 1.00 21.98 C ANISOU 1443 CG ASP A 187 2762 2635 2954 -261 -32 136 ATOM 1444 OD1 ASP A 187 -17.661 8.281 -30.451 1.00 26.23 O ANISOU 1444 OD1 ASP A 187 3305 3156 3505 -285 -56 165 ATOM 1445 OD2 ASP A 187 -16.773 9.640 -31.942 1.00 24.07 O1- ANISOU 1445 OD2 ASP A 187 3043 2880 3224 -249 -33 105 ATOM 1446 N ARG A 188 -19.941 10.206 -27.111 1.00 19.81 N ANISOU 1446 N ARG A 188 2384 2519 2624 -310 -1 236 ATOM 1447 CA ARG A 188 -21.368 10.134 -26.828 1.00 26.70 C ANISOU 1447 CA ARG A 188 3225 3435 3485 -338 -4 266 ATOM 1448 C ARG A 188 -21.635 10.849 -25.496 1.00 30.69 C ANISOU 1448 C ARG A 188 3691 4011 3959 -331 19 276 ATOM 1449 O ARG A 188 -20.742 10.940 -24.651 1.00 30.76 O ANISOU 1449 O ARG A 188 3701 4029 3958 -314 30 271 ATOM 1450 CB ARG A 188 -21.859 8.662 -26.849 1.00 27.46 C ANISOU 1450 CB ARG A 188 3328 3509 3596 -383 -38 311 ATOM 1451 CG ARG A 188 -21.495 7.822 -25.611 1.00 25.27 C ANISOU 1451 CG ARG A 188 3048 3238 3315 -403 -51 347 ATOM 1452 CD ARG A 188 -21.886 6.341 -25.708 1.00 33.80 C ANISOU 1452 CD ARG A 188 4142 4284 4417 -451 -96 394 ATOM 1453 NE ARG A 188 -20.952 5.549 -26.521 1.00 56.61 N ANISOU 1453 NE ARG A 188 7077 7092 7340 -440 -125 372 ATOM 1454 CZ ARG A 188 -20.152 4.566 -26.072 1.00 63.12 C ANISOU 1454 CZ ARG A 188 7925 7876 8184 -449 -154 388 ATOM 1455 NH1 ARG A 188 -20.175 4.166 -24.791 1.00 63.63 N ANISOU 1455 NH1 ARG A 188 7972 7970 8236 -474 -161 431 ATOM 1456 NH2 ARG A 188 -19.315 3.966 -26.926 1.00 70.45 N1+ ANISOU 1456 NH2 ARG A 188 8892 8734 9141 -432 -179 358 ATOM 1457 N GLN A 189 -22.878 11.315 -25.326 1.00 26.10 N ANISOU 1457 N GLN A 189 3073 3485 3360 -342 26 288 ATOM 1458 CA GLN A 189 -23.375 11.930 -24.102 1.00 29.92 C ANISOU 1458 CA GLN A 189 3514 4046 3810 -330 48 290 ATOM 1459 C GLN A 189 -23.734 10.832 -23.088 1.00 32.62 C ANISOU 1459 C GLN A 189 3833 4425 4135 -371 37 344 ATOM 1460 O GLN A 189 -24.847 10.310 -23.100 1.00 31.83 O ANISOU 1460 O GLN A 189 3704 4366 4025 -406 28 380 ATOM 1461 CB GLN A 189 -24.548 12.866 -24.455 1.00 24.04 C ANISOU 1461 CB GLN A 189 2734 3350 3051 -319 58 274 ATOM 1462 CG GLN A 189 -25.133 13.611 -23.241 1.00 37.53 C ANISOU 1462 CG GLN A 189 4397 5138 4723 -295 80 263 ATOM 1463 CD GLN A 189 -26.093 14.714 -23.677 1.00 47.85 C ANISOU 1463 CD GLN A 189 5671 6487 6020 -275 87 237 ATOM 1464 OE1 GLN A 189 -25.678 15.847 -23.913 1.00 61.38 O ANISOU 1464 OE1 GLN A 189 7358 8236 7727 -302 81 262 ATOM 1465 NE2 GLN A 189 -27.382 14.388 -23.781 1.00 58.23 N ANISOU 1465 NE2 GLN A 189 6990 7798 7336 -227 96 188 ATOM 1466 N THR A 190 -22.755 10.489 -22.247 1.00 33.11 N ANISOU 1466 N THR A 190 3907 4479 4195 -369 38 352 ATOM 1467 CA THR A 190 -22.860 9.465 -21.215 1.00 44.99 C ANISOU 1467 CA THR A 190 5396 6012 5687 -411 23 407 ATOM 1468 C THR A 190 -21.976 9.878 -20.025 1.00 41.64 C ANISOU 1468 C THR A 190 4966 5613 5243 -391 40 400 ATOM 1469 O THR A 190 -21.109 10.741 -20.185 1.00 39.99 O ANISOU 1469 O THR A 190 4774 5384 5038 -346 57 355 ATOM 1470 CB THR A 190 -22.432 8.074 -21.774 1.00 45.96 C ANISOU 1470 CB THR A 190 5558 6061 5846 -447 -16 438 ATOM 1471 OG1 THR A 190 -22.716 7.037 -20.854 1.00 56.36 O ANISOU 1471 OG1 THR A 190 6854 7411 7150 -500 -39 501 ATOM 1472 CG2 THR A 190 -20.933 7.946 -22.122 1.00 36.75 C ANISOU 1472 CG2 THR A 190 4435 4825 4703 -421 -22 412 ATOM 1473 N ALA A 191 -22.206 9.257 -18.853 1.00 48.83 N ANISOU 1473 N ALA A 191 5853 6570 6132 -426 32 448 ATOM 1474 CA ALA A 191 -21.385 9.447 -17.659 1.00 43.37 C ANISOU 1474 CA ALA A 191 5152 5908 5417 -411 47 446 ATOM 1475 C ALA A 191 -19.957 8.937 -17.897 1.00 45.78 C ANISOU 1475 C ALA A 191 5508 6129 5756 -401 31 437 ATOM 1476 O ALA A 191 -19.744 7.733 -18.039 1.00 58.95 O ANISOU 1476 O ALA A 191 7202 7744 7451 -434 -3 470 ATOM 1477 CB ALA A 191 -22.032 8.746 -16.455 1.00 50.74 C ANISOU 1477 CB ALA A 191 6044 6918 6315 -458 40 505 ATOM 1478 N GLN A 192 -19.025 9.892 -17.959 1.00 39.76 N ANISOU 1478 N GLN A 192 4760 5353 4994 -354 53 391 ATOM 1479 CA GLN A 192 -17.604 9.663 -18.146 1.00 40.71 C ANISOU 1479 CA GLN A 192 4922 5404 5141 -340 42 380 ATOM 1480 C GLN A 192 -16.887 10.852 -17.509 1.00 50.42 C ANISOU 1480 C GLN A 192 6148 6657 6352 -295 70 342 ATOM 1481 O GLN A 192 -17.157 12.003 -17.857 1.00 50.99 O ANISOU 1481 O GLN A 192 6210 6748 6415 -261 91 301 ATOM 1482 CB GLN A 192 -17.265 9.446 -19.640 1.00 37.67 C ANISOU 1482 CB GLN A 192 4578 4940 4795 -327 28 353 ATOM 1483 CG GLN A 192 -17.508 10.664 -20.558 1.00 37.08 C ANISOU 1483 CG GLN A 192 4500 4869 4718 -293 49 306 ATOM 1484 CD GLN A 192 -17.345 10.318 -22.033 1.00 28.70 C ANISOU 1484 CD GLN A 192 3474 3740 3691 -289 34 286 ATOM 1485 OE1 GLN A 192 -16.406 9.626 -22.405 1.00 26.60 O ANISOU 1485 OE1 GLN A 192 3241 3417 3448 -284 19 278 ATOM 1486 NE2 GLN A 192 -18.232 10.830 -22.885 1.00 31.28 N ANISOU 1486 NE2 GLN A 192 3792 4075 4018 -291 37 275 ATOM 1487 N ALA A 193 -16.003 10.531 -16.563 1.00 42.39 N ANISOU 1487 N ALA A 193 5137 5639 5331 -298 67 356 ATOM 1488 CA ALA A 193 -15.179 11.486 -15.847 1.00 43.65 C ANISOU 1488 CA ALA A 193 5291 5825 5471 -260 91 326 ATOM 1489 C ALA A 193 -13.729 11.032 -15.944 1.00 36.72 C ANISOU 1489 C ALA A 193 4451 4884 4617 -249 80 320 ATOM 1490 O ALA A 193 -13.447 9.831 -15.977 1.00 37.10 O ANISOU 1490 O ALA A 193 4519 4889 4688 -276 54 350 ATOM 1491 CB ALA A 193 -15.641 11.557 -14.383 1.00 48.80 C ANISOU 1491 CB ALA A 193 5900 6564 6079 -274 102 352 ATOM 1492 N ALA A 194 -12.830 12.021 -15.965 1.00 41.24 N ANISOU 1492 N ALA A 194 5032 5450 5186 -208 98 280 ATOM 1493 CA ALA A 194 -11.396 11.793 -15.922 1.00 37.11 C ANISOU 1493 CA ALA A 194 4540 4877 4682 -192 92 270 ATOM 1494 C ALA A 194 -10.968 11.222 -14.565 1.00 35.62 C ANISOU 1494 C ALA A 194 4344 4707 4481 -212 84 306 ATOM 1495 O ALA A 194 -11.551 11.577 -13.538 1.00 41.92 O ANISOU 1495 O ALA A 194 5111 5573 5245 -221 95 323 ATOM 1496 CB ALA A 194 -10.697 13.126 -16.199 1.00 37.38 C ANISOU 1496 CB ALA A 194 4581 4910 4712 -148 111 224 ATOM 1497 N GLY A 195 -9.916 10.391 -14.592 1.00 38.55 N ANISOU 1497 N GLY A 195 4746 5023 4880 -217 64 315 ATOM 1498 CA GLY A 195 -9.215 9.931 -13.396 1.00 37.72 C ANISOU 1498 CA GLY A 195 4640 4927 4766 -226 57 341 ATOM 1499 C GLY A 195 -8.562 11.122 -12.680 1.00 38.46 C ANISOU 1499 C GLY A 195 4723 5055 4834 -192 84 312 ATOM 1500 O GLY A 195 -8.398 12.199 -13.261 1.00 29.10 O ANISOU 1500 O GLY A 195 3539 3874 3645 -158 103 271 ATOM 1501 N THR A 196 -8.183 10.925 -11.409 1.00 37.36 N ANISOU 1501 N THR A 196 4576 4942 4678 -203 81 338 ATOM 1502 CA THR A 196 -7.501 11.939 -10.606 1.00 31.85 C ANISOU 1502 CA THR A 196 3871 4273 3957 -171 102 312 ATOM 1503 C THR A 196 -6.152 12.313 -11.241 1.00 19.94 C ANISOU 1503 C THR A 196 2395 2703 2477 -137 103 276 ATOM 1504 O THR A 196 -5.296 11.441 -11.404 1.00 30.60 O ANISOU 1504 O THR A 196 3771 3997 3857 -143 84 284 ATOM 1505 CB THR A 196 -7.236 11.442 -9.164 1.00 45.48 C ANISOU 1505 CB THR A 196 5585 6035 5662 -192 96 349 ATOM 1506 OG1 THR A 196 -8.471 11.116 -8.560 1.00 35.43 O ANISOU 1506 OG1 THR A 196 4277 4824 4359 -231 94 389 ATOM 1507 CG2 THR A 196 -6.515 12.446 -8.246 1.00 38.99 C ANISOU 1507 CG2 THR A 196 4753 5249 4812 -157 118 319 ATOM 1508 N ASP A 197 -6.020 13.592 -11.628 1.00 25.75 N ANISOU 1508 N ASP A 197 3129 3451 3203 -102 121 236 ATOM 1509 CA ASP A 197 -4.817 14.114 -12.265 1.00 22.50 C ANISOU 1509 CA ASP A 197 2744 2992 2812 -73 122 206 ATOM 1510 C ASP A 197 -3.674 14.229 -11.242 1.00 34.26 C ANISOU 1510 C ASP A 197 4240 4482 4295 -65 121 213 ATOM 1511 O ASP A 197 -3.918 14.259 -10.036 1.00 30.92 O ANISOU 1511 O ASP A 197 3799 4100 3848 -78 122 236 ATOM 1512 CB ASP A 197 -5.083 15.481 -12.942 1.00 28.56 C ANISOU 1512 CB ASP A 197 3509 3770 3573 -43 135 165 ATOM 1513 CG ASP A 197 -4.117 15.795 -14.089 1.00 27.05 C ANISOU 1513 CG ASP A 197 3344 3526 3408 -26 131 141 ATOM 1514 OD1 ASP A 197 -3.619 14.837 -14.721 1.00 25.50 O ANISOU 1514 OD1 ASP A 197 3164 3289 3236 -38 120 151 ATOM 1515 OD2 ASP A 197 -3.934 17.002 -14.354 1.00 26.24 O1- ANISOU 1515 OD2 ASP A 197 3244 3426 3302 -1 137 112 ATOM 1516 N THR A 198 -2.449 14.299 -11.766 1.00 25.18 N ANISOU 1516 N THR A 198 3113 3288 3166 -45 118 193 ATOM 1517 CA THR A 198 -1.212 14.418 -11.007 1.00 26.29 C ANISOU 1517 CA THR A 198 3263 3421 3306 -34 116 195 ATOM 1518 C THR A 198 -0.293 15.441 -11.695 1.00 24.45 C ANISOU 1518 C THR A 198 3041 3170 3078 -2 123 159 ATOM 1519 O THR A 198 -0.459 15.723 -12.885 1.00 23.16 O ANISOU 1519 O THR A 198 2882 2994 2923 7 126 136 ATOM 1520 CB THR A 198 -0.542 13.022 -10.824 1.00 32.30 C ANISOU 1520 CB THR A 198 4040 4142 4092 -51 96 220 ATOM 1521 OG1 THR A 198 0.761 13.091 -10.282 1.00 48.28 O ANISOU 1521 OG1 THR A 198 6076 6145 6122 -32 94 211 ATOM 1522 CG2 THR A 198 -0.412 12.198 -12.110 1.00 36.25 C ANISOU 1522 CG2 THR A 198 4554 4596 4622 -55 83 213 ATOM 1523 N THR A 199 0.618 16.027 -10.907 1.00 17.80 N ANISOU 1523 N THR A 199 2205 2330 2230 11 123 157 ATOM 1524 CA THR A 199 1.544 17.057 -11.357 1.00 18.06 C ANISOU 1524 CA THR A 199 2248 2349 2267 37 126 129 ATOM 1525 C THR A 199 2.744 16.432 -12.087 1.00 22.62 C ANISOU 1525 C THR A 199 2843 2883 2870 40 118 126 ATOM 1526 O THR A 199 3.329 15.471 -11.582 1.00 17.75 O ANISOU 1526 O THR A 199 2232 2249 2264 32 110 144 ATOM 1527 CB THR A 199 2.066 17.891 -10.165 1.00 21.85 C ANISOU 1527 CB THR A 199 2722 2855 2724 51 128 126 ATOM 1528 OG1 THR A 199 0.964 18.407 -9.446 1.00 23.60 O ANISOU 1528 OG1 THR A 199 2925 3122 2922 54 135 118 ATOM 1529 CG2 THR A 199 2.965 19.073 -10.564 1.00 21.08 C ANISOU 1529 CG2 THR A 199 2637 2741 2633 72 125 103 ATOM 1530 N ILE A 200 3.077 16.992 -13.262 1.00 22.07 N ANISOU 1530 N ILE A 200 2781 2797 2809 52 120 103 ATOM 1531 CA ILE A 200 4.131 16.486 -14.140 1.00 21.46 C ANISOU 1531 CA ILE A 200 2714 2689 2751 58 114 95 ATOM 1532 C ILE A 200 5.492 17.007 -13.631 1.00 18.32 C ANISOU 1532 C ILE A 200 2320 2290 2350 71 112 93 ATOM 1533 O ILE A 200 5.865 18.148 -13.903 1.00 18.74 O ANISOU 1533 O ILE A 200 2374 2349 2396 81 114 80 ATOM 1534 CB ILE A 200 3.913 16.915 -15.623 1.00 18.20 C ANISOU 1534 CB ILE A 200 2303 2268 2344 61 116 73 ATOM 1535 CG1 ILE A 200 2.497 16.576 -16.156 1.00 19.82 C ANISOU 1535 CG1 ILE A 200 2505 2476 2552 48 117 75 ATOM 1536 CG2 ILE A 200 4.976 16.309 -16.565 1.00 20.58 C ANISOU 1536 CG2 ILE A 200 2612 2548 2662 67 111 63 ATOM 1537 CD1 ILE A 200 1.978 17.605 -17.174 1.00 24.72 C ANISOU 1537 CD1 ILE A 200 3122 3107 3165 50 121 58 ATOM 1538 N THR A 201 6.171 16.168 -12.837 1.00 18.32 N ANISOU 1538 N THR A 201 2323 2281 2357 68 106 110 ATOM 1539 CA THR A 201 7.342 16.515 -12.025 1.00 17.71 C ANISOU 1539 CA THR A 201 2248 2205 2274 78 104 114 ATOM 1540 C THR A 201 8.572 16.983 -12.821 1.00 16.75 C ANISOU 1540 C THR A 201 2130 2076 2160 92 103 96 ATOM 1541 O THR A 201 9.223 17.940 -12.403 1.00 21.72 O ANISOU 1541 O THR A 201 2759 2716 2778 100 103 93 ATOM 1542 CB THR A 201 7.773 15.302 -11.169 1.00 14.31 C ANISOU 1542 CB THR A 201 1821 1761 1856 71 93 136 ATOM 1543 OG1 THR A 201 6.645 14.845 -10.466 1.00 22.19 O ANISOU 1543 OG1 THR A 201 2813 2774 2844 52 92 158 ATOM 1544 CG2 THR A 201 8.915 15.550 -10.173 1.00 18.92 C ANISOU 1544 CG2 THR A 201 2406 2347 2434 81 90 141 ATOM 1545 N VAL A 202 8.841 16.323 -13.960 1.00 22.51 N ANISOU 1545 N VAL A 202 2860 2787 2905 94 100 85 ATOM 1546 CA VAL A 202 9.921 16.669 -14.886 1.00 20.62 C ANISOU 1546 CA VAL A 202 2618 2549 2666 106 101 68 ATOM 1547 C VAL A 202 9.733 18.052 -15.553 1.00 18.89 C ANISOU 1547 C VAL A 202 2397 2350 2433 104 106 60 ATOM 1548 O VAL A 202 10.730 18.724 -15.820 1.00 17.12 O ANISOU 1548 O VAL A 202 2169 2136 2201 108 103 57 ATOM 1549 CB VAL A 202 10.097 15.565 -15.970 1.00 17.14 C ANISOU 1549 CB VAL A 202 2176 2093 2242 112 96 52 ATOM 1550 CG1 VAL A 202 8.882 15.385 -16.903 1.00 16.72 C ANISOU 1550 CG1 VAL A 202 2124 2039 2191 104 99 42 ATOM 1551 CG2 VAL A 202 11.374 15.741 -16.812 1.00 16.82 C ANISOU 1551 CG2 VAL A 202 2127 2066 2198 124 97 36 ATOM 1552 N ASN A 203 8.470 18.475 -15.747 1.00 15.35 N ANISOU 1552 N ASN A 203 1948 1905 1979 96 109 58 ATOM 1553 CA ASN A 203 8.114 19.800 -16.259 1.00 18.53 C ANISOU 1553 CA ASN A 203 2350 2320 2370 93 107 51 ATOM 1554 C ASN A 203 8.285 20.887 -15.188 1.00 24.85 C ANISOU 1554 C ASN A 203 3152 3130 3159 98 100 57 ATOM 1555 O ASN A 203 8.751 21.971 -15.535 1.00 19.27 O ANISOU 1555 O ASN A 203 2447 2429 2447 98 90 55 ATOM 1556 CB ASN A 203 6.671 19.808 -16.812 1.00 13.26 C ANISOU 1556 CB ASN A 203 1681 1654 1703 85 110 45 ATOM 1557 CG ASN A 203 6.460 19.002 -18.096 1.00 18.46 C ANISOU 1557 CG ASN A 203 2339 2304 2371 80 113 35 ATOM 1558 OD1 ASN A 203 7.326 18.248 -18.528 1.00 20.96 O ANISOU 1558 OD1 ASN A 203 2654 2617 2694 85 112 29 ATOM 1559 ND2 ASN A 203 5.286 19.149 -18.711 1.00 18.06 N ANISOU 1559 ND2 ASN A 203 2288 2254 2322 72 114 30 ATOM 1560 N VAL A 204 7.952 20.591 -13.915 1.00 18.24 N ANISOU 1560 N VAL A 204 2316 2297 2318 101 102 66 ATOM 1561 CA VAL A 204 8.186 21.509 -12.793 1.00 13.01 C ANISOU 1561 CA VAL A 204 1656 1646 1643 109 95 68 ATOM 1562 C VAL A 204 9.686 21.774 -12.572 1.00 17.00 C ANISOU 1562 C VAL A 204 2164 2145 2150 113 87 74 ATOM 1563 O VAL A 204 10.062 22.931 -12.403 1.00 20.11 O ANISOU 1563 O VAL A 204 2561 2542 2537 116 74 71 ATOM 1564 CB VAL A 204 7.552 21.027 -11.454 1.00 15.49 C ANISOU 1564 CB VAL A 204 1965 1972 1947 110 100 78 ATOM 1565 CG1 VAL A 204 7.866 21.945 -10.253 1.00 19.04 C ANISOU 1565 CG1 VAL A 204 2417 2434 2383 121 91 77 ATOM 1566 CG2 VAL A 204 6.028 20.880 -11.565 1.00 16.06 C ANISOU 1566 CG2 VAL A 204 2030 2060 2013 106 106 72 ATOM 1567 N LEU A 205 10.509 20.714 -12.651 1.00 18.14 N ANISOU 1567 N LEU A 205 2307 2281 2304 112 93 81 ATOM 1568 CA LEU A 205 11.970 20.785 -12.604 1.00 13.94 C ANISOU 1568 CA LEU A 205 1776 1748 1775 116 87 86 ATOM 1569 C LEU A 205 12.567 21.607 -13.757 1.00 18.77 C ANISOU 1569 C LEU A 205 2383 2367 2383 112 81 79 ATOM 1570 O LEU A 205 13.451 22.421 -13.496 1.00 16.74 O ANISOU 1570 O LEU A 205 2126 2116 2120 111 69 86 ATOM 1571 CB LEU A 205 12.554 19.358 -12.591 1.00 13.19 C ANISOU 1571 CB LEU A 205 1677 1641 1692 120 91 90 ATOM 1572 CG LEU A 205 12.402 18.642 -11.232 1.00 17.37 C ANISOU 1572 CG LEU A 205 2210 2163 2225 119 90 105 ATOM 1573 CD1 LEU A 205 12.735 17.148 -11.359 1.00 20.88 C ANISOU 1573 CD1 LEU A 205 2655 2589 2690 122 87 108 ATOM 1574 CD2 LEU A 205 13.252 19.302 -10.131 1.00 26.41 C ANISOU 1574 CD2 LEU A 205 3358 3315 3360 124 84 116 ATOM 1575 N ALA A 206 12.048 21.424 -14.986 1.00 16.29 N ANISOU 1575 N ALA A 206 2064 2053 2071 106 86 69 ATOM 1576 CA ALA A 206 12.426 22.199 -16.171 1.00 14.02 C ANISOU 1576 CA ALA A 206 1770 1779 1777 97 79 66 ATOM 1577 C ALA A 206 12.154 23.700 -16.023 1.00 13.58 C ANISOU 1577 C ALA A 206 1722 1725 1714 90 60 72 ATOM 1578 O ALA A 206 12.992 24.512 -16.407 1.00 17.71 O ANISOU 1578 O ALA A 206 2243 2256 2231 81 45 81 ATOM 1579 CB ALA A 206 11.687 21.659 -17.400 1.00 25.60 C ANISOU 1579 CB ALA A 206 3232 3248 3246 91 87 54 ATOM 1580 N TRP A 207 10.995 24.030 -15.441 1.00 16.95 N ANISOU 1580 N TRP A 207 2155 2143 2140 95 58 66 ATOM 1581 CA TRP A 207 10.570 25.392 -15.157 1.00 14.35 C ANISOU 1581 CA TRP A 207 1834 1811 1807 95 35 64 ATOM 1582 C TRP A 207 11.355 26.067 -14.014 1.00 24.24 C ANISOU 1582 C TRP A 207 3093 3063 3056 102 20 72 ATOM 1583 O TRP A 207 11.540 27.282 -14.070 1.00 17.52 O ANISOU 1583 O TRP A 207 2248 2208 2203 97 -7 76 ATOM 1584 CB TRP A 207 9.053 25.366 -14.943 1.00 17.16 C ANISOU 1584 CB TRP A 207 2191 2165 2163 104 40 51 ATOM 1585 CG TRP A 207 8.403 26.644 -14.534 1.00 18.05 C ANISOU 1585 CG TRP A 207 2310 2275 2272 112 16 41 ATOM 1586 CD1 TRP A 207 8.015 27.636 -15.368 1.00 29.42 C ANISOU 1586 CD1 TRP A 207 3754 3709 3717 105 -6 35 ATOM 1587 CD2 TRP A 207 8.107 27.104 -13.185 1.00 17.59 C ANISOU 1587 CD2 TRP A 207 2255 2222 2207 130 8 32 ATOM 1588 NE1 TRP A 207 7.444 28.652 -14.631 1.00 21.21 N ANISOU 1588 NE1 TRP A 207 2720 2665 2675 121 -31 20 ATOM 1589 CE2 TRP A 207 7.460 28.370 -13.281 1.00 28.55 C ANISOU 1589 CE2 TRP A 207 3648 3604 3596 138 -21 16 ATOM 1590 CE3 TRP A 207 8.300 26.570 -11.889 1.00 19.13 C ANISOU 1590 CE3 TRP A 207 2448 2428 2394 140 21 35 ATOM 1591 CZ2 TRP A 207 6.972 29.045 -12.155 1.00 25.43 C ANISOU 1591 CZ2 TRP A 207 3255 3215 3193 160 -37 -1 ATOM 1592 CZ3 TRP A 207 7.835 27.255 -10.751 1.00 21.81 C ANISOU 1592 CZ3 TRP A 207 2788 2777 2721 159 8 20 ATOM 1593 CH2 TRP A 207 7.141 28.471 -10.883 1.00 20.52 C ANISOU 1593 CH2 TRP A 207 2629 2610 2559 171 -20 0 ATOM 1594 N LEU A 208 11.859 25.286 -13.038 1.00 16.75 N ANISOU 1594 N LEU A 208 2144 2115 2106 111 33 77 ATOM 1595 CA LEU A 208 12.808 25.772 -12.029 1.00 14.86 C ANISOU 1595 CA LEU A 208 1910 1875 1862 117 18 85 ATOM 1596 C LEU A 208 14.192 26.082 -12.635 1.00 14.01 C ANISOU 1596 C LEU A 208 1799 1770 1756 104 7 99 ATOM 1597 O LEU A 208 14.842 27.012 -12.162 1.00 19.36 O ANISOU 1597 O LEU A 208 2482 2444 2430 101 -18 107 ATOM 1598 CB LEU A 208 12.941 24.775 -10.855 1.00 17.63 C ANISOU 1598 CB LEU A 208 2259 2227 2211 126 34 91 ATOM 1599 CG LEU A 208 11.708 24.635 -9.934 1.00 19.66 C ANISOU 1599 CG LEU A 208 2517 2492 2461 135 42 82 ATOM 1600 CD1 LEU A 208 11.901 23.470 -8.934 1.00 15.02 C ANISOU 1600 CD1 LEU A 208 1928 1909 1871 138 54 95 ATOM 1601 CD2 LEU A 208 11.320 25.956 -9.233 1.00 19.27 C ANISOU 1601 CD2 LEU A 208 2473 2447 2401 147 22 68 ATOM 1602 N TYR A 209 14.606 25.355 -13.691 1.00 16.45 N ANISOU 1602 N TYR A 209 2095 2087 2066 97 23 102 ATOM 1603 CA TYR A 209 15.789 25.701 -14.488 1.00 15.54 C ANISOU 1603 CA TYR A 209 1971 1988 1948 83 13 115 ATOM 1604 C TYR A 209 15.589 26.972 -15.329 1.00 13.05 C ANISOU 1604 C TYR A 209 1658 1674 1628 64 -13 121 ATOM 1605 O TYR A 209 16.520 27.771 -15.405 1.00 16.75 O ANISOU 1605 O TYR A 209 2126 2149 2091 51 -36 138 ATOM 1606 CB TYR A 209 16.220 24.531 -15.391 1.00 12.86 C ANISOU 1606 CB TYR A 209 1614 1664 1608 83 35 109 ATOM 1607 CG TYR A 209 16.955 23.410 -14.686 1.00 19.12 C ANISOU 1607 CG TYR A 209 2402 2455 2408 98 49 109 ATOM 1608 CD1 TYR A 209 18.246 23.651 -14.184 1.00 13.58 C ANISOU 1608 CD1 TYR A 209 1693 1765 1702 98 42 121 ATOM 1609 CD2 TYR A 209 16.391 22.122 -14.574 1.00 23.31 C ANISOU 1609 CD2 TYR A 209 2936 2972 2950 111 65 97 ATOM 1610 CE1 TYR A 209 18.969 22.616 -13.571 1.00 16.25 C ANISOU 1610 CE1 TYR A 209 2027 2100 2049 112 51 120 ATOM 1611 CE2 TYR A 209 17.110 21.086 -13.946 1.00 17.62 C ANISOU 1611 CE2 TYR A 209 2212 2245 2238 123 70 98 ATOM 1612 CZ TYR A 209 18.402 21.338 -13.451 1.00 16.05 C ANISOU 1612 CZ TYR A 209 2005 2057 2036 126 64 108 ATOM 1613 OH TYR A 209 19.124 20.345 -12.867 1.00 16.33 O ANISOU 1613 OH TYR A 209 2037 2084 2082 139 67 108 ATOM 1614 N ALA A 210 14.386 27.157 -15.905 1.00 19.41 N ANISOU 1614 N ALA A 210 2466 2474 2435 62 -12 110 ATOM 1615 CA ALA A 210 13.990 28.360 -16.649 1.00 22.55 C ANISOU 1615 CA ALA A 210 2867 2869 2830 43 -42 117 ATOM 1616 C ALA A 210 14.039 29.630 -15.785 1.00 25.83 C ANISOU 1616 C ALA A 210 3299 3267 3250 47 -78 122 ATOM 1617 O ALA A 210 14.456 30.680 -16.275 1.00 19.69 O ANISOU 1617 O ALA A 210 2523 2487 2470 27 -112 139 ATOM 1618 CB ALA A 210 12.574 28.175 -17.215 1.00 19.75 C ANISOU 1618 CB ALA A 210 2514 2508 2480 43 -36 102 ATOM 1619 N ALA A 211 13.648 29.483 -14.507 1.00 21.14 N ANISOU 1619 N ALA A 211 2714 2659 2658 71 -73 106 ATOM 1620 CA ALA A 211 13.718 30.507 -13.475 1.00 19.20 C ANISOU 1620 CA ALA A 211 2484 2398 2415 80 -107 105 ATOM 1621 C ALA A 211 15.157 30.937 -13.165 1.00 19.43 C ANISOU 1621 C ALA A 211 2512 2429 2440 67 -125 128 ATOM 1622 O ALA A 211 15.421 32.136 -13.184 1.00 23.17 O ANISOU 1622 O ALA A 211 2995 2890 2917 55 -168 140 ATOM 1623 CB ALA A 211 12.995 30.007 -12.219 1.00 26.07 C ANISOU 1623 CB ALA A 211 3357 3266 3281 108 -91 85 ATOM 1624 N VAL A 212 16.061 29.964 -12.941 1.00 13.79 N ANISOU 1624 N VAL A 212 1787 1731 1722 68 -96 137 ATOM 1625 CA VAL A 212 17.490 30.199 -12.699 1.00 22.88 C ANISOU 1625 CA VAL A 212 2935 2888 2869 57 -110 160 ATOM 1626 C VAL A 212 18.211 30.873 -13.885 1.00 22.61 C ANISOU 1626 C VAL A 212 2891 2868 2831 26 -134 183 ATOM 1627 O VAL A 212 19.032 31.759 -13.647 1.00 22.60 O ANISOU 1627 O VAL A 212 2895 2861 2829 10 -171 204 ATOM 1628 CB VAL A 212 18.235 28.884 -12.319 1.00 25.35 C ANISOU 1628 CB VAL A 212 3235 3217 3180 67 -74 161 ATOM 1629 CG1 VAL A 212 19.778 28.957 -12.370 1.00 21.81 C ANISOU 1629 CG1 VAL A 212 2777 2784 2727 54 -84 184 ATOM 1630 CG2 VAL A 212 17.801 28.400 -10.926 1.00 21.03 C ANISOU 1630 CG2 VAL A 212 2698 2656 2634 92 -62 147 ATOM 1631 N ILE A 213 17.868 30.474 -15.124 1.00 23.54 N ANISOU 1631 N ILE A 213 2994 3005 2944 13 -115 182 ATOM 1632 CA ILE A 213 18.368 31.075 -16.369 1.00 22.61 C ANISOU 1632 CA ILE A 213 2864 2909 2818 -21 -136 206 ATOM 1633 C ILE A 213 17.958 32.560 -16.520 1.00 20.78 C ANISOU 1633 C ILE A 213 2651 2652 2594 -37 -188 217 ATOM 1634 O ILE A 213 18.756 33.351 -17.021 1.00 27.23 O ANISOU 1634 O ILE A 213 3464 3477 3405 -68 -224 247 ATOM 1635 CB ILE A 213 17.925 30.242 -17.616 1.00 27.86 C ANISOU 1635 CB ILE A 213 3512 3599 3476 -26 -105 196 ATOM 1636 CG1 ILE A 213 18.648 28.873 -17.639 1.00 22.72 C ANISOU 1636 CG1 ILE A 213 2842 2973 2819 -11 -66 187 ATOM 1637 CG2 ILE A 213 18.099 30.941 -18.985 1.00 35.23 C ANISOU 1637 CG2 ILE A 213 4432 4558 4397 -63 -127 219 ATOM 1638 CD1 ILE A 213 17.982 27.809 -18.526 1.00 20.80 C ANISOU 1638 CD1 ILE A 213 2584 2747 2572 -5 -34 168 ATOM 1639 N ASN A 214 16.761 32.915 -16.019 1.00 23.54 N ANISOU 1639 N ASN A 214 3019 2970 2955 -16 -197 192 ATOM 1640 CA ASN A 214 16.246 34.288 -15.917 1.00 25.47 C ANISOU 1640 CA ASN A 214 3282 3185 3211 -25 -253 196 ATOM 1641 C ASN A 214 16.693 35.026 -14.638 1.00 28.27 C ANISOU 1641 C ASN A 214 3656 3514 3573 -12 -290 196 ATOM 1642 O ASN A 214 16.335 36.194 -14.487 1.00 34.59 O ANISOU 1642 O ASN A 214 4474 4284 4385 -16 -344 196 ATOM 1643 CB ASN A 214 14.707 34.228 -16.037 1.00 30.89 C ANISOU 1643 CB ASN A 214 3978 3853 3907 -5 -250 166 ATOM 1644 CG ASN A 214 14.269 34.224 -17.500 1.00 41.95 C ANISOU 1644 CG ASN A 214 5373 5260 5308 -32 -261 177 ATOM 1645 OD1 ASN A 214 14.333 35.262 -18.150 1.00 47.26 O ANISOU 1645 OD1 ASN A 214 6055 5914 5987 -53 -314 192 ATOM 1646 ND2 ASN A 214 13.840 33.078 -18.028 1.00 46.53 N ANISOU 1646 ND2 ASN A 214 5936 5866 5878 -34 -215 170 ATOM 1647 N GLY A 215 17.482 34.381 -13.763 1.00 20.59 N ANISOU 1647 N GLY A 215 2680 2548 2594 3 -268 196 ATOM 1648 CA GLY A 215 18.095 35.012 -12.594 1.00 23.82 C ANISOU 1648 CA GLY A 215 3106 2936 3008 13 -303 196 ATOM 1649 C GLY A 215 17.199 35.010 -11.346 1.00 21.69 C ANISOU 1649 C GLY A 215 2851 2649 2742 55 -297 160 ATOM 1650 O GLY A 215 17.526 35.705 -10.383 1.00 30.29 O ANISOU 1650 O GLY A 215 3956 3719 3834 67 -331 155 ATOM 1651 N ASP A 216 16.107 34.227 -11.337 1.00 35.96 N ANISOU 1651 N ASP A 216 4651 4465 4545 75 -255 134 ATOM 1652 CA ASP A 216 15.240 33.996 -10.182 1.00 30.56 C ANISOU 1652 CA ASP A 216 3974 3779 3859 112 -243 101 ATOM 1653 C ASP A 216 15.768 32.723 -9.488 1.00 29.63 C ANISOU 1653 C ASP A 216 3845 3682 3730 120 -197 106 ATOM 1654 O ASP A 216 15.575 31.622 -10.003 1.00 32.14 O ANISOU 1654 O ASP A 216 4151 4017 4046 119 -154 104 ATOM 1655 CB ASP A 216 13.759 33.871 -10.637 1.00 38.88 C ANISOU 1655 CB ASP A 216 5023 4835 4914 124 -228 76 ATOM 1656 CG ASP A 216 12.731 34.487 -9.683 1.00 44.78 C ANISOU 1656 CG ASP A 216 5781 5570 5662 158 -254 39 ATOM 1657 OD1 ASP A 216 13.117 34.937 -8.582 1.00 48.03 O ANISOU 1657 OD1 ASP A 216 6203 5974 6071 174 -280 30 ATOM 1658 OD2 ASP A 216 11.548 34.497 -10.084 1.00 41.42 O1- ANISOU 1658 OD2 ASP A 216 5351 5148 5239 168 -248 18 ATOM 1659 N ARG A 217 16.511 32.914 -8.384 1.00 22.91 N ANISOU 1659 N ARG A 217 3001 2827 2875 127 -211 112 ATOM 1660 CA ARG A 217 17.406 31.906 -7.799 1.00 27.60 C ANISOU 1660 CA ARG A 217 3587 3437 3462 127 -176 124 ATOM 1661 C ARG A 217 17.190 31.670 -6.292 1.00 26.82 C ANISOU 1661 C ARG A 217 3494 3343 3354 153 -169 108 ATOM 1662 O ARG A 217 17.900 30.833 -5.735 1.00 25.13 O ANISOU 1662 O ARG A 217 3274 3139 3135 152 -148 121 ATOM 1663 CB ARG A 217 18.865 32.355 -8.054 1.00 30.65 C ANISOU 1663 CB ARG A 217 3971 3823 3851 105 -194 156 ATOM 1664 CG ARG A 217 19.301 32.274 -9.528 1.00 41.20 C ANISOU 1664 CG ARG A 217 5295 5168 5190 75 -197 178 ATOM 1665 CD ARG A 217 20.741 32.748 -9.777 1.00 46.70 C ANISOU 1665 CD ARG A 217 5988 5871 5886 49 -223 212 ATOM 1666 NE ARG A 217 20.898 34.199 -9.578 1.00 51.01 N ANISOU 1666 NE ARG A 217 6551 6392 6438 38 -283 220 ATOM 1667 CZ ARG A 217 21.279 34.840 -8.459 1.00 64.49 C ANISOU 1667 CZ ARG A 217 8274 8081 8147 46 -316 222 ATOM 1668 NH1 ARG A 217 21.619 34.179 -7.341 1.00 67.00 N ANISOU 1668 NH1 ARG A 217 8592 8405 8459 64 -293 217 ATOM 1669 NH2 ARG A 217 21.324 36.178 -8.467 1.00 77.03 N1+ ANISOU 1669 NH2 ARG A 217 9881 9643 9745 36 -376 229 ATOM 1670 N TRP A 218 16.259 32.392 -5.642 1.00 21.03 N ANISOU 1670 N TRP A 218 2769 2607 2616 176 -187 78 ATOM 1671 CA TRP A 218 16.073 32.382 -4.180 1.00 21.91 C ANISOU 1671 CA TRP A 218 2883 2728 2712 199 -187 63 ATOM 1672 C TRP A 218 15.755 31.004 -3.557 1.00 15.62 C ANISOU 1672 C TRP A 218 2073 1959 1902 203 -138 65 ATOM 1673 O TRP A 218 16.128 30.770 -2.408 1.00 19.13 O ANISOU 1673 O TRP A 218 2518 2416 2334 212 -133 65 ATOM 1674 CB TRP A 218 14.996 33.414 -3.788 1.00 28.59 C ANISOU 1674 CB TRP A 218 3738 3571 3552 227 -218 25 ATOM 1675 CG TRP A 218 13.592 33.135 -4.248 1.00 24.11 C ANISOU 1675 CG TRP A 218 3160 3018 2984 236 -198 4 ATOM 1676 CD1 TRP A 218 13.036 33.599 -5.390 1.00 28.40 C ANISOU 1676 CD1 TRP A 218 3705 3545 3541 230 -214 -1 ATOM 1677 CD2 TRP A 218 12.593 32.254 -3.645 1.00 27.48 C ANISOU 1677 CD2 TRP A 218 3570 3479 3392 249 -159 -10 ATOM 1678 NE1 TRP A 218 11.761 33.093 -5.522 1.00 21.52 N ANISOU 1678 NE1 TRP A 218 2820 2695 2662 241 -186 -21 ATOM 1679 CE2 TRP A 218 11.437 32.246 -4.483 1.00 26.98 C ANISOU 1679 CE2 TRP A 218 3499 3418 3333 252 -152 -26 ATOM 1680 CE3 TRP A 218 12.545 31.450 -2.479 1.00 26.27 C ANISOU 1680 CE3 TRP A 218 3408 3357 3218 256 -131 -8 ATOM 1681 CZ2 TRP A 218 10.299 31.480 -4.182 1.00 26.39 C ANISOU 1681 CZ2 TRP A 218 3408 3377 3244 261 -119 -38 ATOM 1682 CZ3 TRP A 218 11.420 30.655 -2.182 1.00 22.02 C ANISOU 1682 CZ3 TRP A 218 2852 2852 2663 263 -100 -19 ATOM 1683 CH2 TRP A 218 10.301 30.668 -3.034 1.00 23.90 C ANISOU 1683 CH2 TRP A 218 3082 3093 2906 265 -94 -34 ATOM 1684 N PHE A 219 15.066 30.137 -4.317 1.00 22.98 N ANISOU 1684 N PHE A 219 2993 2899 2838 194 -106 68 ATOM 1685 CA PHE A 219 14.619 28.807 -3.897 1.00 15.78 C ANISOU 1685 CA PHE A 219 2069 2011 1917 195 -68 72 ATOM 1686 C PHE A 219 15.720 27.729 -3.919 1.00 15.97 C ANISOU 1686 C PHE A 219 2089 2032 1949 179 -48 100 ATOM 1687 O PHE A 219 15.443 26.604 -3.509 1.00 23.23 O ANISOU 1687 O PHE A 219 3000 2965 2863 177 -22 108 ATOM 1688 CB PHE A 219 13.394 28.393 -4.746 1.00 28.63 C ANISOU 1688 CB PHE A 219 3687 3645 3548 193 -48 62 ATOM 1689 CG PHE A 219 13.630 28.362 -6.249 1.00 21.32 C ANISOU 1689 CG PHE A 219 2761 2701 2640 175 -49 72 ATOM 1690 CD1 PHE A 219 14.243 27.246 -6.861 1.00 17.84 C ANISOU 1690 CD1 PHE A 219 2312 2258 2208 160 -24 92 ATOM 1691 CD2 PHE A 219 13.410 29.527 -7.014 1.00 22.36 C ANISOU 1691 CD2 PHE A 219 2899 2818 2778 175 -78 62 ATOM 1692 CE1 PHE A 219 14.584 27.293 -8.206 1.00 24.12 C ANISOU 1692 CE1 PHE A 219 3105 3045 3015 145 -25 98 ATOM 1693 CE2 PHE A 219 13.736 29.545 -8.362 1.00 32.68 C ANISOU 1693 CE2 PHE A 219 4204 4114 4097 155 -79 74 ATOM 1694 CZ PHE A 219 14.327 28.437 -8.952 1.00 30.17 C ANISOU 1694 CZ PHE A 219 3877 3802 3785 141 -51 92 ATOM 1695 N LEU A 220 16.929 28.053 -4.403 1.00 17.10 N ANISOU 1695 N LEU A 220 2235 2159 2103 168 -61 117 ATOM 1696 CA LEU A 220 18.054 27.120 -4.451 1.00 20.91 C ANISOU 1696 CA LEU A 220 2712 2641 2593 157 -46 140 ATOM 1697 C LEU A 220 18.670 26.957 -3.052 1.00 26.38 C ANISOU 1697 C LEU A 220 3408 3338 3276 163 -49 148 ATOM 1698 O LEU A 220 19.311 27.890 -2.565 1.00 24.67 O ANISOU 1698 O LEU A 220 3202 3116 3056 167 -75 149 ATOM 1699 CB LEU A 220 19.101 27.606 -5.474 1.00 20.42 C ANISOU 1699 CB LEU A 220 2648 2571 2541 143 -60 154 ATOM 1700 CG LEU A 220 18.593 27.771 -6.925 1.00 24.02 C ANISOU 1700 CG LEU A 220 3096 3026 3004 132 -57 150 ATOM 1701 CD1 LEU A 220 19.658 28.464 -7.794 1.00 26.30 C ANISOU 1701 CD1 LEU A 220 3382 3315 3296 115 -78 168 ATOM 1702 CD2 LEU A 220 18.118 26.452 -7.561 1.00 25.34 C ANISOU 1702 CD2 LEU A 220 3251 3200 3178 131 -24 149 ATOM 1703 N ASN A 221 18.459 25.780 -2.438 1.00 19.86 N ANISOU 1703 N ASN A 221 2576 2521 2449 162 -26 158 ATOM 1704 CA ASN A 221 19.032 25.422 -1.136 1.00 25.29 C ANISOU 1704 CA ASN A 221 3267 3215 3128 165 -29 169 ATOM 1705 C ASN A 221 20.436 24.801 -1.276 1.00 23.97 C ANISOU 1705 C ASN A 221 3096 3036 2976 156 -28 192 ATOM 1706 O ASN A 221 20.927 24.613 -2.390 1.00 26.31 O ANISOU 1706 O ASN A 221 3385 3324 3287 151 -23 196 ATOM 1707 CB ASN A 221 18.031 24.567 -0.314 1.00 23.54 C ANISOU 1707 CB ASN A 221 3039 3013 2892 166 -12 169 ATOM 1708 CG ASN A 221 17.659 23.179 -0.854 1.00 23.01 C ANISOU 1708 CG ASN A 221 2963 2941 2839 154 9 182 ATOM 1709 OD1 ASN A 221 18.375 22.562 -1.638 1.00 22.64 O ANISOU 1709 OD1 ASN A 221 2914 2875 2813 149 12 191 ATOM 1710 ND2 ASN A 221 16.525 22.663 -0.388 1.00 25.66 N ANISOU 1710 ND2 ASN A 221 3292 3295 3163 150 21 184 ATOM 1711 N ARG A 222 21.065 24.509 -0.129 1.00 27.50 N ANISOU 1711 N ARG A 222 3546 3486 3417 157 -33 205 ATOM 1712 CA ARG A 222 22.425 23.972 -0.033 1.00 25.69 C ANISOU 1712 CA ARG A 222 3314 3247 3202 152 -36 225 ATOM 1713 C ARG A 222 22.514 22.437 -0.169 1.00 24.30 C ANISOU 1713 C ARG A 222 3128 3064 3039 148 -20 237 ATOM 1714 O ARG A 222 23.627 21.911 -0.137 1.00 32.28 O ANISOU 1714 O ARG A 222 4135 4067 4063 147 -24 251 ATOM 1715 CB ARG A 222 23.028 24.465 1.302 1.00 40.12 C ANISOU 1715 CB ARG A 222 5149 5077 5016 154 -54 235 ATOM 1716 CG ARG A 222 22.427 23.849 2.586 1.00 42.06 C ANISOU 1716 CG ARG A 222 5397 5338 5245 155 -47 238 ATOM 1717 CD ARG A 222 23.031 24.487 3.845 1.00 42.72 C ANISOU 1717 CD ARG A 222 5490 5431 5309 160 -66 239 ATOM 1718 NE ARG A 222 22.420 24.002 5.090 1.00 51.01 N ANISOU 1718 NE ARG A 222 6539 6503 6340 157 -59 247 ATOM 1719 CZ ARG A 222 21.290 24.454 5.658 1.00 59.00 C ANISOU 1719 CZ ARG A 222 7549 7545 7324 163 -56 230 ATOM 1720 NH1 ARG A 222 20.526 25.384 5.067 1.00 58.06 N ANISOU 1720 NH1 ARG A 222 7431 7432 7197 177 -60 201 ATOM 1721 NH2 ARG A 222 20.924 23.968 6.852 1.00 56.42 N1+ ANISOU 1721 NH2 ARG A 222 7216 7245 6976 156 -49 243 ATOM 1722 N PHE A 223 21.367 21.746 -0.263 1.00 21.14 N ANISOU 1722 N PHE A 223 2725 2667 2638 146 -5 232 ATOM 1723 CA PHE A 223 21.273 20.292 -0.137 1.00 17.82 C ANISOU 1723 CA PHE A 223 2300 2238 2232 140 1 245 ATOM 1724 C PHE A 223 21.278 19.565 -1.488 1.00 26.61 C ANISOU 1724 C PHE A 223 3406 3337 3368 142 9 236 ATOM 1725 O PHE A 223 20.980 20.158 -2.524 1.00 21.08 O ANISOU 1725 O PHE A 223 2703 2639 2668 145 15 220 ATOM 1726 CB PHE A 223 19.976 19.958 0.627 1.00 28.00 C ANISOU 1726 CB PHE A 223 3590 3542 3505 131 7 251 ATOM 1727 CG PHE A 223 19.899 20.547 2.024 1.00 27.93 C ANISOU 1727 CG PHE A 223 3587 3557 3470 131 0 256 ATOM 1728 CD1 PHE A 223 20.827 20.166 3.016 1.00 20.88 C ANISOU 1728 CD1 PHE A 223 2696 2660 2577 127 -11 276 ATOM 1729 CD2 PHE A 223 18.918 21.512 2.331 1.00 31.40 C ANISOU 1729 CD2 PHE A 223 4025 4022 3884 136 4 238 ATOM 1730 CE1 PHE A 223 20.746 20.721 4.286 1.00 23.03 C ANISOU 1730 CE1 PHE A 223 2972 2957 2822 127 -18 278 ATOM 1731 CE2 PHE A 223 18.854 22.055 3.606 1.00 38.15 C ANISOU 1731 CE2 PHE A 223 4883 4902 4712 141 -4 236 ATOM 1732 CZ PHE A 223 19.759 21.653 4.580 1.00 42.20 C ANISOU 1732 CZ PHE A 223 5399 5413 5222 135 -14 257 ATOM 1733 N THR A 224 21.541 18.255 -1.410 1.00 24.19 N ANISOU 1733 N THR A 224 3097 3014 3080 140 6 247 ATOM 1734 CA THR A 224 21.269 17.280 -2.462 1.00 24.36 C ANISOU 1734 CA THR A 224 3113 3021 3123 143 10 238 ATOM 1735 C THR A 224 20.284 16.227 -1.899 1.00 24.06 C ANISOU 1735 C THR A 224 3079 2975 3088 130 7 252 ATOM 1736 O THR A 224 19.976 16.242 -0.703 1.00 24.12 O ANISOU 1736 O THR A 224 3090 2996 3077 117 5 269 ATOM 1737 CB THR A 224 22.590 16.606 -2.939 1.00 26.96 C ANISOU 1737 CB THR A 224 3433 3335 3474 156 1 234 ATOM 1738 OG1 THR A 224 22.387 15.884 -4.141 1.00 23.92 O ANISOU 1738 OG1 THR A 224 3041 2941 3106 164 5 214 ATOM 1739 CG2 THR A 224 23.250 15.645 -1.929 1.00 33.79 C ANISOU 1739 CG2 THR A 224 4302 4182 4354 154 -16 254 ATOM 1740 N THR A 225 19.796 15.337 -2.770 1.00 24.49 N ANISOU 1740 N THR A 225 3132 3011 3164 131 5 244 ATOM 1741 CA THR A 225 18.955 14.206 -2.392 1.00 25.51 C ANISOU 1741 CA THR A 225 3264 3128 3301 115 -4 261 ATOM 1742 C THR A 225 19.188 13.046 -3.365 1.00 21.62 C ANISOU 1742 C THR A 225 2771 2604 2841 125 -16 249 ATOM 1743 O THR A 225 19.517 13.278 -4.527 1.00 24.93 O ANISOU 1743 O THR A 225 3183 3021 3268 143 -10 222 ATOM 1744 CB THR A 225 17.442 14.583 -2.363 1.00 32.57 C ANISOU 1744 CB THR A 225 4158 4045 4173 101 11 261 ATOM 1745 OG1 THR A 225 16.625 13.474 -2.032 1.00 29.52 O ANISOU 1745 OG1 THR A 225 3773 3651 3793 80 -1 284 ATOM 1746 CG2 THR A 225 16.880 15.135 -3.682 1.00 27.50 C ANISOU 1746 CG2 THR A 225 3512 3401 3535 111 24 233 ATOM 1747 N THR A 226 18.961 11.814 -2.890 1.00 20.46 N ANISOU 1747 N THR A 226 2629 2434 2711 111 -37 269 ATOM 1748 CA THR A 226 18.829 10.649 -3.760 1.00 19.62 C ANISOU 1748 CA THR A 226 2524 2293 2637 120 -55 256 ATOM 1749 C THR A 226 17.484 10.698 -4.523 1.00 21.93 C ANISOU 1749 C THR A 226 2817 2592 2924 110 -44 248 ATOM 1750 O THR A 226 16.538 11.338 -4.055 1.00 23.53 O ANISOU 1750 O THR A 226 3018 2820 3100 90 -29 262 ATOM 1751 CB THR A 226 18.937 9.324 -2.955 1.00 27.91 C ANISOU 1751 CB THR A 226 3582 3309 3713 107 -92 283 ATOM 1752 OG1 THR A 226 17.723 8.897 -2.366 1.00 23.03 O ANISOU 1752 OG1 THR A 226 2968 2701 3082 73 -96 316 ATOM 1753 CG2 THR A 226 20.069 9.297 -1.915 1.00 27.29 C ANISOU 1753 CG2 THR A 226 3504 3228 3637 111 -104 298 ATOM 1754 N LEU A 227 17.423 10.019 -5.681 1.00 21.09 N ANISOU 1754 N LEU A 227 2711 2463 2841 124 -52 223 ATOM 1755 CA LEU A 227 16.221 9.923 -6.515 1.00 22.15 C ANISOU 1755 CA LEU A 227 2846 2598 2974 115 -45 215 ATOM 1756 C LEU A 227 15.047 9.245 -5.782 1.00 28.65 C ANISOU 1756 C LEU A 227 3676 3415 3796 82 -60 252 ATOM 1757 O LEU A 227 13.916 9.709 -5.911 1.00 22.40 O ANISOU 1757 O LEU A 227 2881 2648 2982 64 -43 259 ATOM 1758 CB LEU A 227 16.578 9.209 -7.842 1.00 21.40 C ANISOU 1758 CB LEU A 227 2750 2474 2906 137 -59 183 ATOM 1759 CG LEU A 227 15.462 9.197 -8.915 1.00 29.52 C ANISOU 1759 CG LEU A 227 3778 3506 3930 132 -48 167 ATOM 1760 CD1 LEU A 227 15.009 10.615 -9.318 1.00 29.57 C ANISOU 1760 CD1 LEU A 227 3778 3554 3905 130 -11 158 ATOM 1761 CD2 LEU A 227 15.882 8.369 -10.147 1.00 30.30 C ANISOU 1761 CD2 LEU A 227 3876 3581 4055 159 -63 130 ATOM 1762 N ASN A 228 15.354 8.204 -4.986 1.00 27.30 N ANISOU 1762 N ASN A 228 3512 3215 3646 71 -94 278 ATOM 1763 CA ASN A 228 14.394 7.479 -4.152 1.00 31.11 C ANISOU 1763 CA ASN A 228 3999 3694 4128 34 -114 319 ATOM 1764 C ASN A 228 13.796 8.353 -3.038 1.00 25.06 C ANISOU 1764 C ASN A 228 3224 2979 3320 10 -90 346 ATOM 1765 O ASN A 228 12.573 8.393 -2.931 1.00 26.81 O ANISOU 1765 O ASN A 228 3440 3224 3522 -16 -83 363 ATOM 1766 CB ASN A 228 15.043 6.200 -3.577 1.00 38.75 C ANISOU 1766 CB ASN A 228 4976 4617 5129 25 -162 343 ATOM 1767 CG ASN A 228 15.342 5.102 -4.605 1.00 49.61 C ANISOU 1767 CG ASN A 228 6362 5940 6549 43 -197 320 ATOM 1768 OD1 ASN A 228 14.834 5.113 -5.726 1.00 44.67 O ANISOU 1768 OD1 ASN A 228 5736 5312 5927 51 -188 295 ATOM 1769 ND2 ASN A 228 16.168 4.128 -4.216 1.00 47.58 N ANISOU 1769 ND2 ASN A 228 6113 5639 6327 52 -240 324 ATOM 1770 N ASP A 229 14.637 9.064 -2.267 1.00 27.30 N ANISOU 1770 N ASP A 229 3504 3283 3586 19 -78 347 ATOM 1771 CA ASP A 229 14.194 9.980 -1.203 1.00 27.60 C ANISOU 1771 CA ASP A 229 3533 3371 3581 1 -58 366 ATOM 1772 C ASP A 229 13.412 11.198 -1.718 1.00 21.84 C ANISOU 1772 C ASP A 229 2796 2678 2825 11 -23 339 ATOM 1773 O ASP A 229 12.517 11.662 -1.013 1.00 26.45 O ANISOU 1773 O ASP A 229 3370 3304 3377 -7 -10 352 ATOM 1774 CB ASP A 229 15.329 10.437 -0.259 1.00 40.17 C ANISOU 1774 CB ASP A 229 5126 4972 5163 12 -56 369 ATOM 1775 CG ASP A 229 16.069 9.299 0.449 1.00 57.06 C ANISOU 1775 CG ASP A 229 7272 7083 7324 -3 -92 402 ATOM 1776 OD1 ASP A 229 17.207 9.562 0.894 1.00 63.46 O ANISOU 1776 OD1 ASP A 229 8086 7884 8143 12 -98 399 ATOM 1777 OD2 ASP A 229 15.478 8.207 0.601 1.00 47.78 O1- ANISOU 1777 OD2 ASP A 229 6100 5895 6161 -32 -117 433 ATOM 1778 N PHE A 230 13.712 11.668 -2.942 1.00 14.31 N ANISOU 1778 N PHE A 230 1844 1711 1882 38 -10 302 ATOM 1779 CA PHE A 230 12.903 12.676 -3.622 1.00 18.13 C ANISOU 1779 CA PHE A 230 2321 2222 2345 45 16 279 ATOM 1780 C PHE A 230 11.482 12.185 -3.952 1.00 22.71 C ANISOU 1780 C PHE A 230 2898 2808 2924 24 15 289 ATOM 1781 O PHE A 230 10.523 12.893 -3.652 1.00 22.75 O ANISOU 1781 O PHE A 230 2893 2852 2901 16 31 291 ATOM 1782 CB PHE A 230 13.641 13.242 -4.852 1.00 21.49 C ANISOU 1782 CB PHE A 230 2749 2632 2784 72 25 243 ATOM 1783 CG PHE A 230 12.790 14.155 -5.717 1.00 25.46 C ANISOU 1783 CG PHE A 230 3247 3155 3271 76 45 222 ATOM 1784 CD1 PHE A 230 12.415 15.427 -5.235 1.00 17.51 C ANISOU 1784 CD1 PHE A 230 2236 2182 2236 80 60 214 ATOM 1785 CD2 PHE A 230 12.208 13.672 -6.907 1.00 21.00 C ANISOU 1785 CD2 PHE A 230 2682 2576 2721 75 46 209 ATOM 1786 CE1 PHE A 230 11.524 16.211 -5.955 1.00 22.93 C ANISOU 1786 CE1 PHE A 230 2918 2883 2910 84 73 195 ATOM 1787 CE2 PHE A 230 11.314 14.468 -7.607 1.00 30.31 C ANISOU 1787 CE2 PHE A 230 3858 3774 3887 77 62 192 ATOM 1788 CZ PHE A 230 10.975 15.730 -7.136 1.00 22.21 C ANISOU 1788 CZ PHE A 230 2826 2778 2833 82 75 185 ATOM 1789 N ASN A 231 11.386 10.987 -4.552 1.00 20.17 N ANISOU 1789 N ASN A 231 2583 2448 2634 18 -7 295 ATOM 1790 CA ASN A 231 10.127 10.376 -4.986 1.00 23.96 C ANISOU 1790 CA ASN A 231 3059 2930 3114 -2 -9 303 ATOM 1791 C ASN A 231 9.207 9.962 -3.825 1.00 25.06 C ANISOU 1791 C ASN A 231 3189 3102 3231 -39 -16 346 ATOM 1792 O ASN A 231 7.993 10.004 -4.017 1.00 20.49 O ANISOU 1792 O ASN A 231 2599 2553 2632 -54 -4 351 ATOM 1793 CB ASN A 231 10.427 9.192 -5.933 1.00 25.50 C ANISOU 1793 CB ASN A 231 3266 3073 3350 2 -36 296 ATOM 1794 CG ASN A 231 10.911 9.615 -7.326 1.00 29.45 C ANISOU 1794 CG ASN A 231 3768 3560 3861 34 -22 250 ATOM 1795 OD1 ASN A 231 10.602 10.704 -7.806 1.00 27.03 O ANISOU 1795 OD1 ASN A 231 3455 3282 3533 40 6 232 ATOM 1796 ND2 ASN A 231 11.649 8.734 -8.001 1.00 24.09 N ANISOU 1796 ND2 ASN A 231 3097 2843 3214 53 -42 232 ATOM 1797 N LEU A 232 9.763 9.635 -2.643 1.00 21.36 N ANISOU 1797 N LEU A 232 2721 2636 2758 -54 -32 376 ATOM 1798 CA LEU A 232 8.987 9.404 -1.417 1.00 30.53 C ANISOU 1798 CA LEU A 232 3868 3841 3890 -91 -36 418 ATOM 1799 C LEU A 232 8.243 10.670 -0.956 1.00 29.82 C ANISOU 1799 C LEU A 232 3760 3816 3754 -84 -1 403 ATOM 1800 O LEU A 232 7.069 10.571 -0.600 1.00 36.38 O ANISOU 1800 O LEU A 232 4574 4693 4557 -108 6 422 ATOM 1801 CB LEU A 232 9.899 8.893 -0.279 1.00 32.60 C ANISOU 1801 CB LEU A 232 4134 4099 4153 -108 -60 453 ATOM 1802 CG LEU A 232 10.394 7.438 -0.428 1.00 32.53 C ANISOU 1802 CG LEU A 232 4142 4029 4190 -119 -104 475 ATOM 1803 CD1 LEU A 232 11.461 7.111 0.641 1.00 40.36 C ANISOU 1803 CD1 LEU A 232 5134 5029 5173 -138 -124 513 ATOM 1804 CD2 LEU A 232 9.244 6.410 -0.441 1.00 41.35 C ANISOU 1804 CD2 LEU A 232 5261 5125 5324 -150 -132 502 ATOM 1805 N VAL A 233 8.923 11.830 -1.001 1.00 32.34 N ANISOU 1805 N VAL A 233 4082 4142 4063 -52 18 371 ATOM 1806 CA VAL A 233 8.323 13.126 -0.680 1.00 36.45 C ANISOU 1806 CA VAL A 233 4587 4717 4544 -40 45 350 ATOM 1807 C VAL A 233 7.310 13.554 -1.757 1.00 27.43 C ANISOU 1807 C VAL A 233 3439 3579 3402 -32 59 325 ATOM 1808 O VAL A 233 6.182 13.881 -1.398 1.00 38.56 O ANISOU 1808 O VAL A 233 4831 5037 4783 -43 71 329 ATOM 1809 CB VAL A 233 9.378 14.253 -0.484 1.00 40.52 C ANISOU 1809 CB VAL A 233 5111 5231 5055 -8 54 323 ATOM 1810 CG1 VAL A 233 8.750 15.643 -0.240 1.00 31.09 C ANISOU 1810 CG1 VAL A 233 3904 4085 3825 10 74 294 ATOM 1811 CG2 VAL A 233 10.322 13.919 0.686 1.00 39.85 C ANISOU 1811 CG2 VAL A 233 5030 5146 4967 -19 39 350 ATOM 1812 N ALA A 234 7.712 13.502 -3.042 1.00 28.85 N ANISOU 1812 N ALA A 234 3635 3714 3614 -14 58 301 ATOM 1813 CA ALA A 234 6.903 13.877 -4.206 1.00 37.88 C ANISOU 1813 CA ALA A 234 4774 4860 4758 -5 72 276 ATOM 1814 C ALA A 234 5.555 13.135 -4.287 1.00 38.35 C ANISOU 1814 C ALA A 234 4822 4934 4813 -34 67 299 ATOM 1815 O ALA A 234 4.540 13.772 -4.562 1.00 31.16 O ANISOU 1815 O ALA A 234 3898 4056 3884 -34 82 286 ATOM 1816 CB ALA A 234 7.737 13.663 -5.480 1.00 36.17 C ANISOU 1816 CB ALA A 234 4573 4594 4576 14 68 251 ATOM 1817 N MET A 235 5.556 11.829 -3.962 1.00 29.16 N ANISOU 1817 N MET A 235 3664 3747 3670 -61 43 334 ATOM 1818 CA MET A 235 4.368 10.973 -3.885 1.00 33.22 C ANISOU 1818 CA MET A 235 4167 4276 4179 -96 33 365 ATOM 1819 C MET A 235 3.251 11.517 -2.972 1.00 23.66 C ANISOU 1819 C MET A 235 2928 3141 2921 -110 51 376 ATOM 1820 O MET A 235 2.085 11.427 -3.355 1.00 21.01 O ANISOU 1820 O MET A 235 2577 2832 2573 -123 58 378 ATOM 1821 CB MET A 235 4.804 9.542 -3.498 1.00 35.25 C ANISOU 1821 CB MET A 235 4434 4500 4460 -127 -4 408 ATOM 1822 CG MET A 235 3.657 8.544 -3.257 1.00 44.95 C ANISOU 1822 CG MET A 235 5650 5750 5681 -172 -21 452 ATOM 1823 SD MET A 235 4.186 6.820 -3.071 1.00 55.64 S ANISOU 1823 SD MET A 235 7023 7041 7078 -207 -78 499 ATOM 1824 CE MET A 235 4.515 6.406 -4.806 1.00 51.90 C ANISOU 1824 CE MET A 235 6574 6492 6655 -175 -90 455 ATOM 1825 N LYS A 236 3.623 12.099 -1.815 1.00 25.33 N ANISOU 1825 N LYS A 236 3131 3391 3103 -105 59 380 ATOM 1826 CA LYS A 236 2.687 12.724 -0.874 1.00 26.91 C ANISOU 1826 CA LYS A 236 3300 3671 3253 -116 75 387 ATOM 1827 C LYS A 236 1.969 13.970 -1.412 1.00 25.83 C ANISOU 1827 C LYS A 236 3152 3564 3099 -86 99 343 ATOM 1828 O LYS A 236 0.838 14.212 -0.996 1.00 24.75 O ANISOU 1828 O LYS A 236 2986 3492 2925 -96 111 346 ATOM 1829 CB LYS A 236 3.391 13.069 0.454 1.00 33.79 C ANISOU 1829 CB LYS A 236 4167 4575 4097 -111 77 393 ATOM 1830 CG LYS A 236 3.601 11.846 1.351 1.00 58.07 C ANISOU 1830 CG LYS A 236 7238 7660 7168 -152 55 447 ATOM 1831 CD LYS A 236 4.056 12.213 2.775 1.00 71.55 C ANISOU 1831 CD LYS A 236 8923 9437 8824 -155 64 455 ATOM 1832 CE LYS A 236 3.404 11.338 3.857 1.00 80.31 C ANISOU 1832 CE LYS A 236 10010 10598 9906 -210 49 515 ATOM 1833 NZ LYS A 236 3.661 9.904 3.632 1.00 76.01 N1+ ANISOU 1833 NZ LYS A 236 9485 9992 9405 -247 12 563 ATOM 1834 N TYR A 237 2.624 14.726 -2.306 1.00 29.44 N ANISOU 1834 N TYR A 237 3627 3980 3578 -51 106 303 ATOM 1835 CA TYR A 237 2.092 15.961 -2.891 1.00 18.20 C ANISOU 1835 CA TYR A 237 2196 2579 2141 -22 122 261 ATOM 1836 C TYR A 237 1.424 15.736 -4.256 1.00 26.46 C ANISOU 1836 C TYR A 237 3247 3596 3211 -24 123 250 ATOM 1837 O TYR A 237 1.121 16.719 -4.932 1.00 23.28 O ANISOU 1837 O TYR A 237 2844 3192 2808 2 132 214 ATOM 1838 CB TYR A 237 3.207 17.025 -2.937 1.00 27.84 C ANISOU 1838 CB TYR A 237 3432 3780 3365 14 124 227 ATOM 1839 CG TYR A 237 3.704 17.375 -1.547 1.00 22.76 C ANISOU 1839 CG TYR A 237 2781 3174 2694 17 124 234 ATOM 1840 CD1 TYR A 237 4.890 16.797 -1.057 1.00 25.33 C ANISOU 1840 CD1 TYR A 237 3120 3473 3031 5 112 260 ATOM 1841 CD2 TYR A 237 2.941 18.216 -0.711 1.00 23.90 C ANISOU 1841 CD2 TYR A 237 2903 3380 2797 33 133 213 ATOM 1842 CE1 TYR A 237 5.289 17.019 0.274 1.00 32.20 C ANISOU 1842 CE1 TYR A 237 3984 4378 3874 6 111 268 ATOM 1843 CE2 TYR A 237 3.350 18.454 0.616 1.00 35.87 C ANISOU 1843 CE2 TYR A 237 4411 4933 4283 37 131 217 ATOM 1844 CZ TYR A 237 4.519 17.843 1.113 1.00 29.28 C ANISOU 1844 CZ TYR A 237 3593 4072 3462 22 121 247 ATOM 1845 OH TYR A 237 4.907 18.044 2.405 1.00 33.76 O ANISOU 1845 OH TYR A 237 4152 4674 3999 24 118 252 ATOM 1846 N ASN A 238 1.176 14.465 -4.630 1.00 20.31 N ANISOU 1846 N ASN A 238 2473 2791 2453 -54 110 282 ATOM 1847 CA ASN A 238 0.528 14.052 -5.879 1.00 22.12 C ANISOU 1847 CA ASN A 238 2708 2991 2706 -59 108 276 ATOM 1848 C ASN A 238 1.352 14.465 -7.120 1.00 25.37 C ANISOU 1848 C ASN A 238 3144 3346 3150 -32 108 243 ATOM 1849 O ASN A 238 0.792 14.894 -8.128 1.00 17.24 O ANISOU 1849 O ASN A 238 2116 2307 2128 -23 114 221 ATOM 1850 CB ASN A 238 -0.942 14.552 -5.909 1.00 17.10 C ANISOU 1850 CB ASN A 238 2048 2406 2044 -58 123 263 ATOM 1851 CG ASN A 238 -1.843 13.865 -6.940 1.00 20.10 C ANISOU 1851 CG ASN A 238 2429 2766 2444 -78 117 273 ATOM 1852 OD1 ASN A 238 -1.641 12.709 -7.306 1.00 29.19 O ANISOU 1852 OD1 ASN A 238 3591 3881 3619 -105 97 303 ATOM 1853 ND2 ASN A 238 -2.851 14.598 -7.412 1.00 31.10 N ANISOU 1853 ND2 ASN A 238 3810 4180 3828 -66 129 248 ATOM 1854 N TYR A 239 2.679 14.321 -7.008 1.00 24.67 N ANISOU 1854 N TYR A 239 3072 3225 3077 -21 100 241 ATOM 1855 CA TYR A 239 3.629 14.451 -8.107 1.00 22.04 C ANISOU 1855 CA TYR A 239 2758 2842 2772 -1 98 216 ATOM 1856 C TYR A 239 3.950 13.046 -8.620 1.00 29.41 C ANISOU 1856 C TYR A 239 3706 3730 3740 -14 77 231 ATOM 1857 O TYR A 239 4.051 12.110 -7.822 1.00 24.03 O ANISOU 1857 O TYR A 239 3025 3040 3064 -35 60 263 ATOM 1858 CB TYR A 239 4.908 15.147 -7.596 1.00 23.23 C ANISOU 1858 CB TYR A 239 2918 2987 2922 21 99 204 ATOM 1859 CG TYR A 239 4.912 16.662 -7.626 1.00 23.70 C ANISOU 1859 CG TYR A 239 2972 3070 2961 43 111 176 ATOM 1860 CD1 TYR A 239 3.886 17.396 -7.001 1.00 25.59 C ANISOU 1860 CD1 TYR A 239 3195 3358 3170 45 120 172 ATOM 1861 CD2 TYR A 239 5.964 17.346 -8.267 1.00 17.25 C ANISOU 1861 CD2 TYR A 239 2168 2231 2156 64 111 153 ATOM 1862 CE1 TYR A 239 3.890 18.801 -7.051 1.00 21.93 C ANISOU 1862 CE1 TYR A 239 2729 2911 2692 69 124 143 ATOM 1863 CE2 TYR A 239 5.984 18.750 -8.303 1.00 14.87 C ANISOU 1863 CE2 TYR A 239 1864 1945 1840 82 114 130 ATOM 1864 CZ TYR A 239 4.942 19.476 -7.701 1.00 17.57 C ANISOU 1864 CZ TYR A 239 2192 2326 2156 86 118 124 ATOM 1865 OH TYR A 239 4.945 20.836 -7.768 1.00 19.64 O ANISOU 1865 OH TYR A 239 2456 2597 2409 107 114 97 ATOM 1866 N GLU A 240 4.137 12.934 -9.945 1.00 27.60 N ANISOU 1866 N GLU A 240 3486 3470 3531 -2 77 207 ATOM 1867 CA GLU A 240 4.558 11.698 -10.602 1.00 29.89 C ANISOU 1867 CA GLU A 240 3789 3714 3853 -6 56 209 ATOM 1868 C GLU A 240 5.981 11.266 -10.188 1.00 26.29 C ANISOU 1868 C GLU A 240 3344 3231 3414 6 42 210 ATOM 1869 O GLU A 240 6.792 12.130 -9.848 1.00 22.40 O ANISOU 1869 O GLU A 240 2850 2751 2910 24 54 198 ATOM 1870 CB GLU A 240 4.479 11.868 -12.131 1.00 40.34 C ANISOU 1870 CB GLU A 240 5119 5018 5191 9 60 177 ATOM 1871 CG GLU A 240 3.033 11.984 -12.632 1.00 60.24 C ANISOU 1871 CG GLU A 240 7634 7544 7710 -8 61 182 ATOM 1872 CD GLU A 240 2.962 11.951 -14.152 1.00 66.60 C ANISOU 1872 CD GLU A 240 8448 8328 8532 4 61 152 ATOM 1873 OE1 GLU A 240 2.538 10.902 -14.683 1.00 76.35 O ANISOU 1873 OE1 GLU A 240 9688 9537 9785 -8 43 157 ATOM 1874 OE2 GLU A 240 3.352 12.969 -14.763 1.00 44.06 O1- ANISOU 1874 OE2 GLU A 240 5592 5481 5669 24 76 125 ATOM 1875 N PRO A 241 6.287 9.950 -10.266 1.00 27.07 N ANISOU 1875 N PRO A 241 3453 3293 3541 -2 13 224 ATOM 1876 CA PRO A 241 7.668 9.454 -10.115 1.00 24.71 C ANISOU 1876 CA PRO A 241 3164 2964 3262 15 -3 218 ATOM 1877 C PRO A 241 8.645 10.081 -11.124 1.00 24.12 C ANISOU 1877 C PRO A 241 3090 2884 3192 48 11 177 ATOM 1878 O PRO A 241 8.371 10.066 -12.326 1.00 25.60 O ANISOU 1878 O PRO A 241 3277 3066 3383 57 17 151 ATOM 1879 CB PRO A 241 7.543 7.934 -10.326 1.00 25.95 C ANISOU 1879 CB PRO A 241 3332 3075 3453 2 -42 232 ATOM 1880 CG PRO A 241 6.089 7.609 -10.042 1.00 27.98 C ANISOU 1880 CG PRO A 241 3583 3348 3699 -35 -48 266 ATOM 1881 CD PRO A 241 5.359 8.849 -10.534 1.00 24.98 C ANISOU 1881 CD PRO A 241 3192 3009 3292 -28 -10 246 ATOM 1882 N LEU A 242 9.759 10.624 -10.614 1.00 27.37 N ANISOU 1882 N LEU A 242 3501 3301 3599 63 15 172 ATOM 1883 CA LEU A 242 10.878 11.054 -11.441 1.00 22.29 C ANISOU 1883 CA LEU A 242 2855 2655 2960 91 23 140 ATOM 1884 C LEU A 242 11.766 9.836 -11.740 1.00 26.97 C ANISOU 1884 C LEU A 242 3454 3210 3584 106 -5 129 ATOM 1885 O LEU A 242 12.381 9.285 -10.826 1.00 25.56 O ANISOU 1885 O LEU A 242 3279 3014 3417 104 -25 149 ATOM 1886 CB LEU A 242 11.648 12.199 -10.757 1.00 27.19 C ANISOU 1886 CB LEU A 242 3470 3301 3560 100 38 142 ATOM 1887 CG LEU A 242 12.684 12.887 -11.677 1.00 25.91 C ANISOU 1887 CG LEU A 242 3302 3147 3396 122 48 113 ATOM 1888 CD1 LEU A 242 12.003 13.828 -12.689 1.00 21.62 C ANISOU 1888 CD1 LEU A 242 2754 2623 2837 121 66 96 ATOM 1889 CD2 LEU A 242 13.753 13.633 -10.863 1.00 23.79 C ANISOU 1889 CD2 LEU A 242 3031 2894 3114 128 53 122 ATOM 1890 N THR A 243 11.795 9.442 -13.018 1.00 27.89 N ANISOU 1890 N THR A 243 3569 3316 3713 125 -9 97 ATOM 1891 CA THR A 243 12.590 8.338 -13.548 1.00 27.91 C ANISOU 1891 CA THR A 243 3574 3284 3745 146 -38 76 ATOM 1892 C THR A 243 13.987 8.836 -13.971 1.00 20.19 C ANISOU 1892 C THR A 243 2584 2325 2762 177 -27 46 ATOM 1893 O THR A 243 14.211 10.045 -14.056 1.00 21.10 O ANISOU 1893 O THR A 243 2689 2477 2850 177 1 42 ATOM 1894 CB THR A 243 11.877 7.726 -14.788 1.00 26.51 C ANISOU 1894 CB THR A 243 3402 3086 3584 150 -51 54 ATOM 1895 OG1 THR A 243 11.973 8.546 -15.943 1.00 23.08 O ANISOU 1895 OG1 THR A 243 2956 2682 3131 166 -26 20 ATOM 1896 CG2 THR A 243 10.405 7.356 -14.538 1.00 35.81 C ANISOU 1896 CG2 THR A 243 4588 4259 4759 117 -54 83 ATOM 1897 N GLN A 244 14.899 7.893 -14.258 1.00 27.68 N ANISOU 1897 N GLN A 244 3533 3249 3736 202 -54 25 ATOM 1898 CA GLN A 244 16.230 8.203 -14.782 1.00 24.24 C ANISOU 1898 CA GLN A 244 3080 2837 3293 232 -45 -5 ATOM 1899 C GLN A 244 16.192 8.799 -16.204 1.00 21.94 C ANISOU 1899 C GLN A 244 2775 2580 2982 243 -22 -39 ATOM 1900 O GLN A 244 17.025 9.654 -16.488 1.00 20.83 O ANISOU 1900 O GLN A 244 2616 2480 2819 252 -1 -50 ATOM 1901 CB GLN A 244 17.137 6.958 -14.694 1.00 34.89 C ANISOU 1901 CB GLN A 244 4429 4153 4674 261 -81 -25 ATOM 1902 CG GLN A 244 18.629 7.188 -15.037 1.00 30.01 C ANISOU 1902 CG GLN A 244 3789 3567 4048 294 -74 -57 ATOM 1903 CD GLN A 244 19.303 8.258 -14.170 1.00 24.60 C ANISOU 1903 CD GLN A 244 3096 2907 3342 283 -54 -29 ATOM 1904 OE1 GLN A 244 19.732 9.298 -14.665 1.00 34.21 O ANISOU 1904 OE1 GLN A 244 4327 4105 4568 265 -63 6 ATOM 1905 NE2 GLN A 244 19.400 8.010 -12.862 1.00 23.86 N ANISOU 1905 NE2 GLN A 244 2982 2863 3221 291 -27 -43 ATOM 1906 N ASP A 245 15.204 8.415 -17.039 1.00 23.09 N ANISOU 1906 N ASP A 245 2926 2713 3133 238 -27 -51 ATOM 1907 CA ASP A 245 14.951 9.054 -18.341 1.00 21.20 C ANISOU 1907 CA ASP A 245 2674 2509 2872 243 -5 -78 ATOM 1908 C ASP A 245 14.593 10.541 -18.211 1.00 26.08 C ANISOU 1908 C ASP A 245 3287 3164 3458 219 27 -55 ATOM 1909 O ASP A 245 15.117 11.334 -18.989 1.00 26.47 O ANISOU 1909 O ASP A 245 3320 3254 3485 224 45 -70 ATOM 1910 CB ASP A 245 13.905 8.355 -19.244 1.00 25.05 C ANISOU 1910 CB ASP A 245 3172 2974 3372 238 -17 -92 ATOM 1911 CG ASP A 245 14.236 6.933 -19.703 1.00 47.59 C ANISOU 1911 CG ASP A 245 6023 5810 6248 273 -46 -137 ATOM 1912 OD1 ASP A 245 15.203 6.334 -19.182 1.00 38.94 O ANISOU 1912 OD1 ASP A 245 4922 4706 5169 300 -65 -153 ATOM 1913 OD2 ASP A 245 13.476 6.451 -20.571 1.00 51.29 O1- ANISOU 1913 OD2 ASP A 245 6494 6274 6719 276 -51 -160 ATOM 1914 N HIS A 246 13.769 10.905 -17.211 1.00 22.79 N ANISOU 1914 N HIS A 246 2884 2735 3040 193 31 -19 ATOM 1915 CA HIS A 246 13.453 12.300 -16.890 1.00 16.50 C ANISOU 1915 CA HIS A 246 2084 1968 2216 175 55 -1 ATOM 1916 C HIS A 246 14.684 13.117 -16.461 1.00 17.53 C ANISOU 1916 C HIS A 246 2203 2125 2334 183 63 2 ATOM 1917 O HIS A 246 14.797 14.275 -16.864 1.00 18.59 O ANISOU 1917 O HIS A 246 2327 2292 2446 179 77 -2 ATOM 1918 CB HIS A 246 12.354 12.374 -15.812 1.00 23.97 C ANISOU 1918 CB HIS A 246 3043 2902 3162 152 55 33 ATOM 1919 CG HIS A 246 11.003 11.824 -16.199 1.00 19.41 C ANISOU 1919 CG HIS A 246 2473 2308 2592 137 50 36 ATOM 1920 ND1 HIS A 246 10.476 11.933 -17.490 1.00 20.11 N ANISOU 1920 ND1 HIS A 246 2571 2380 2689 118 40 64 ATOM 1921 CD2 HIS A 246 10.073 11.187 -15.401 1.00 21.01 C ANISOU 1921 CD2 HIS A 246 2675 2514 2795 137 54 16 ATOM 1922 CE1 HIS A 246 9.288 11.347 -17.425 1.00 25.30 C ANISOU 1922 CE1 HIS A 246 3232 3029 3351 107 37 62 ATOM 1923 NE2 HIS A 246 8.993 10.891 -16.209 1.00 22.51 N ANISOU 1923 NE2 HIS A 246 2874 2684 2993 118 45 32 ATOM 1924 N VAL A 247 15.596 12.491 -15.696 1.00 16.47 N ANISOU 1924 N VAL A 247 2070 1975 2212 194 49 9 ATOM 1925 CA VAL A 247 16.873 13.072 -15.277 1.00 19.62 C ANISOU 1925 CA VAL A 247 2458 2397 2601 202 54 12 ATOM 1926 C VAL A 247 17.836 13.294 -16.464 1.00 27.07 C ANISOU 1926 C VAL A 247 3378 3374 3531 219 61 -17 ATOM 1927 O VAL A 247 18.436 14.367 -16.545 1.00 24.33 O ANISOU 1927 O VAL A 247 3019 3063 3163 213 73 -11 ATOM 1928 CB VAL A 247 17.564 12.206 -14.179 1.00 15.88 C ANISOU 1928 CB VAL A 247 1990 1897 2149 213 34 22 ATOM 1929 CG1 VAL A 247 19.016 12.606 -13.846 1.00 21.45 C ANISOU 1929 CG1 VAL A 247 2682 2626 2842 222 39 26 ATOM 1930 CG2 VAL A 247 16.729 12.172 -12.885 1.00 23.45 C ANISOU 1930 CG2 VAL A 247 2967 2830 3114 192 27 55 ATOM 1931 N ASP A 248 17.932 12.312 -17.379 1.00 25.67 N ANISOU 1931 N ASP A 248 3195 3191 3368 240 51 -49 ATOM 1932 CA ASP A 248 18.708 12.395 -18.625 1.00 24.42 C ANISOU 1932 CA ASP A 248 3011 3075 3193 257 58 -80 ATOM 1933 C ASP A 248 18.198 13.484 -19.586 1.00 20.34 C ANISOU 1933 C ASP A 248 2487 2594 2648 235 78 -76 ATOM 1934 O ASP A 248 19.015 14.190 -20.178 1.00 24.95 O ANISOU 1934 O ASP A 248 3048 3224 3206 232 88 -78 ATOM 1935 CB ASP A 248 18.827 11.044 -19.374 1.00 29.45 C ANISOU 1935 CB ASP A 248 3644 3696 3849 286 41 -121 ATOM 1936 CG ASP A 248 19.403 9.890 -18.544 1.00 31.70 C ANISOU 1936 CG ASP A 248 3934 3945 4165 311 14 -128 ATOM 1937 OD1 ASP A 248 20.204 10.173 -17.626 1.00 29.05 O ANISOU 1937 OD1 ASP A 248 3596 3614 3830 310 13 -108 ATOM 1938 OD2 ASP A 248 19.094 8.731 -18.900 1.00 33.85 O1- ANISOU 1938 OD2 ASP A 248 4214 4184 4464 331 -11 -153 ATOM 1939 N ILE A 249 16.866 13.627 -19.688 1.00 24.63 N ANISOU 1939 N ILE A 249 3047 3115 3194 218 80 -68 ATOM 1940 CA ILE A 249 16.185 14.653 -20.483 1.00 22.35 C ANISOU 1940 CA ILE A 249 2756 2853 2883 196 94 -63 ATOM 1941 C ILE A 249 16.385 16.087 -19.927 1.00 23.15 C ANISOU 1941 C ILE A 249 2856 2973 2966 175 101 -33 ATOM 1942 O ILE A 249 16.400 17.033 -20.715 1.00 20.54 O ANISOU 1942 O ILE A 249 2516 2676 2614 160 107 -29 ATOM 1943 CB ILE A 249 14.670 14.310 -20.631 1.00 24.85 C ANISOU 1943 CB ILE A 249 3092 3138 3213 184 93 -60 ATOM 1944 CG1 ILE A 249 14.467 13.060 -21.520 1.00 32.90 C ANISOU 1944 CG1 ILE A 249 4109 4149 4244 202 84 -94 ATOM 1945 CG2 ILE A 249 13.779 15.443 -21.174 1.00 29.98 C ANISOU 1945 CG2 ILE A 249 3744 3804 3844 159 104 -45 ATOM 1946 CD1 ILE A 249 13.104 12.376 -21.333 1.00 42.50 C ANISOU 1946 CD1 ILE A 249 5345 5322 5479 192 75 -87 ATOM 1947 N LEU A 250 16.590 16.219 -18.602 1.00 25.24 N ANISOU 1947 N LEU A 250 3133 3218 3240 174 96 -11 ATOM 1948 CA LEU A 250 16.952 17.467 -17.914 1.00 22.26 C ANISOU 1948 CA LEU A 250 2756 2854 2847 158 98 14 ATOM 1949 C LEU A 250 18.450 17.831 -18.026 1.00 28.24 C ANISOU 1949 C LEU A 250 3492 3646 3591 163 96 15 ATOM 1950 O LEU A 250 18.837 18.885 -17.521 1.00 27.53 O ANISOU 1950 O LEU A 250 3403 3568 3490 149 93 37 ATOM 1951 CB LEU A 250 16.516 17.356 -16.432 1.00 15.51 C ANISOU 1951 CB LEU A 250 1920 1968 2003 155 93 36 ATOM 1952 CG LEU A 250 15.008 17.584 -16.213 1.00 17.77 C ANISOU 1952 CG LEU A 250 2222 2235 2293 144 95 41 ATOM 1953 CD1 LEU A 250 14.577 17.079 -14.826 1.00 19.99 C ANISOU 1953 CD1 LEU A 250 2517 2492 2585 143 91 58 ATOM 1954 CD2 LEU A 250 14.625 19.064 -16.406 1.00 20.92 C ANISOU 1954 CD2 LEU A 250 2624 2650 2676 127 96 50 ATOM 1955 N GLY A 251 19.257 16.978 -18.683 1.00 20.32 N ANISOU 1955 N GLY A 251 2469 2663 2589 183 98 -10 ATOM 1956 CA GLY A 251 20.701 17.123 -18.883 1.00 22.91 C ANISOU 1956 CA GLY A 251 2773 3030 2904 190 97 -11 ATOM 1957 C GLY A 251 21.152 18.453 -19.523 1.00 20.78 C ANISOU 1957 C GLY A 251 2488 2803 2604 164 99 9 ATOM 1958 O GLY A 251 22.088 19.045 -18.987 1.00 18.95 O ANISOU 1958 O GLY A 251 2249 2587 2363 156 94 30 ATOM 1959 N PRO A 252 20.521 18.961 -20.613 1.00 17.60 N ANISOU 1959 N PRO A 252 2079 2421 2185 147 104 4 ATOM 1960 CA PRO A 252 20.879 20.262 -21.221 1.00 21.15 C ANISOU 1960 CA PRO A 252 2514 2914 2607 117 99 28 ATOM 1961 C PRO A 252 20.712 21.482 -20.297 1.00 23.78 C ANISOU 1961 C PRO A 252 2870 3222 2945 95 85 62 ATOM 1962 O PRO A 252 21.563 22.370 -20.320 1.00 23.29 O ANISOU 1962 O PRO A 252 2796 3186 2867 77 74 86 ATOM 1963 CB PRO A 252 19.972 20.361 -22.461 1.00 23.78 C ANISOU 1963 CB PRO A 252 2845 3263 2929 104 104 17 ATOM 1964 CG PRO A 252 19.628 18.921 -22.799 1.00 24.25 C ANISOU 1964 CG PRO A 252 2903 3309 3003 134 114 -22 ATOM 1965 CD PRO A 252 19.525 18.267 -21.427 1.00 28.04 C ANISOU 1965 CD PRO A 252 3404 3739 3513 157 110 -24 ATOM 1966 N LEU A 253 19.642 21.486 -19.488 1.00 23.16 N ANISOU 1966 N LEU A 253 2820 3095 2885 98 83 65 ATOM 1967 CA LEU A 253 19.341 22.542 -18.522 1.00 20.23 C ANISOU 1967 CA LEU A 253 2469 2702 2517 84 68 91 ATOM 1968 C LEU A 253 20.273 22.500 -17.300 1.00 22.38 C ANISOU 1968 C LEU A 253 2742 2967 2794 94 63 102 ATOM 1969 O LEU A 253 20.677 23.556 -16.814 1.00 17.79 O ANISOU 1969 O LEU A 253 2163 2390 2205 78 46 125 ATOM 1970 CB LEU A 253 17.871 22.422 -18.086 1.00 23.18 C ANISOU 1970 CB LEU A 253 2868 3036 2905 86 69 86 ATOM 1971 CG LEU A 253 16.844 22.587 -19.227 1.00 20.49 C ANISOU 1971 CG LEU A 253 2525 2703 2558 74 72 76 ATOM 1972 CD1 LEU A 253 15.412 22.361 -18.708 1.00 17.97 C ANISOU 1972 CD1 LEU A 253 2227 2349 2252 79 74 70 ATOM 1973 CD2 LEU A 253 16.980 23.942 -19.948 1.00 21.32 C ANISOU 1973 CD2 LEU A 253 2626 2830 2647 46 53 96 ATOM 1974 N SER A 254 20.628 21.281 -16.860 1.00 22.24 N ANISOU 1974 N SER A 254 2723 2937 2791 118 73 88 ATOM 1975 CA SER A 254 21.600 21.021 -15.801 1.00 14.81 C ANISOU 1975 CA SER A 254 1781 1991 1854 127 67 99 ATOM 1976 C SER A 254 23.023 21.466 -16.185 1.00 19.36 C ANISOU 1976 C SER A 254 2332 2612 2414 119 62 109 ATOM 1977 O SER A 254 23.713 22.048 -15.349 1.00 21.82 O ANISOU 1977 O SER A 254 2644 2924 2720 108 49 132 ATOM 1978 CB SER A 254 21.520 19.528 -15.423 1.00 20.79 C ANISOU 1978 CB SER A 254 2541 2726 2633 154 74 81 ATOM 1979 OG SER A 254 22.417 19.197 -14.385 1.00 29.10 O ANISOU 1979 OG SER A 254 3594 3772 3691 161 66 94 ATOM 1980 N ALA A 255 23.409 21.224 -17.450 1.00 18.99 N ANISOU 1980 N ALA A 255 2257 2606 2353 122 71 93 ATOM 1981 CA ALA A 255 24.687 21.630 -18.029 1.00 25.77 C ANISOU 1981 CA ALA A 255 3083 3519 3189 111 67 104 ATOM 1982 C ALA A 255 24.822 23.152 -18.202 1.00 26.01 C ANISOU 1982 C ALA A 255 3117 3564 3202 73 49 139 ATOM 1983 O ALA A 255 25.904 23.679 -17.945 1.00 21.88 O ANISOU 1983 O ALA A 255 2584 3061 2670 59 36 164 ATOM 1984 CB ALA A 255 24.883 20.910 -19.372 1.00 25.66 C ANISOU 1984 CB ALA A 255 3036 3556 3157 120 80 77 ATOM 1985 N GLN A 256 23.733 23.828 -18.615 1.00 24.88 N ANISOU 1985 N GLN A 256 2989 3408 3057 55 44 142 ATOM 1986 CA GLN A 256 23.697 25.278 -18.829 1.00 23.55 C ANISOU 1986 CA GLN A 256 2824 3249 2875 18 19 175 ATOM 1987 C GLN A 256 23.832 26.082 -17.522 1.00 24.18 C ANISOU 1987 C GLN A 256 2928 3290 2967 14 -3 197 ATOM 1988 O GLN A 256 24.608 27.036 -17.487 1.00 28.12 O ANISOU 1988 O GLN A 256 3422 3806 3456 -10 -27 227 ATOM 1989 CB GLN A 256 22.427 25.661 -19.624 1.00 22.22 C ANISOU 1989 CB GLN A 256 2669 3067 2707 3 15 172 ATOM 1990 CG GLN A 256 22.308 27.174 -19.929 1.00 38.93 C ANISOU 1990 CG GLN A 256 4784 5199 4808 -38 -17 206 ATOM 1991 CD GLN A 256 21.082 27.555 -20.762 1.00 43.87 C ANISOU 1991 CD GLN A 256 5423 5809 5436 -53 -25 203 ATOM 1992 OE1 GLN A 256 20.379 26.703 -21.301 1.00 42.66 O ANISOU 1992 OE1 GLN A 256 5270 5653 5286 -38 -2 176 ATOM 1993 NE2 GLN A 256 20.826 28.861 -20.878 1.00 48.04 N ANISOU 1993 NE2 GLN A 256 5966 6323 5965 -82 -62 231 ATOM 1994 N THR A 257 23.070 25.688 -16.489 1.00 26.45 N ANISOU 1994 N THR A 257 3242 3530 3276 37 3 183 ATOM 1995 CA THR A 257 23.019 26.376 -15.195 1.00 19.77 C ANISOU 1995 CA THR A 257 2421 2650 2440 36 -18 198 ATOM 1996 C THR A 257 24.108 25.912 -14.204 1.00 23.31 C ANISOU 1996 C THR A 257 2866 3099 2893 50 -16 204 ATOM 1997 O THR A 257 24.377 26.639 -13.247 1.00 22.41 O ANISOU 1997 O THR A 257 2768 2967 2782 45 -37 221 ATOM 1998 CB THR A 257 21.645 26.163 -14.511 1.00 12.87 C ANISOU 1998 CB THR A 257 1575 1734 1581 52 -13 181 ATOM 1999 OG1 THR A 257 21.420 24.801 -14.186 1.00 17.36 O ANISOU 1999 OG1 THR A 257 2143 2293 2161 78 13 162 ATOM 2000 CG2 THR A 257 20.477 26.693 -15.356 1.00 23.51 C ANISOU 2000 CG2 THR A 257 2927 3081 2926 40 -15 174 ATOM 2001 N GLY A 258 24.707 24.730 -14.433 1.00 21.09 N ANISOU 2001 N GLY A 258 2565 2835 2613 69 6 190 ATOM 2002 CA GLY A 258 25.714 24.132 -13.556 1.00 26.19 C ANISOU 2002 CA GLY A 258 3209 3476 3268 85 7 193 ATOM 2003 C GLY A 258 25.108 23.463 -12.308 1.00 29.40 C ANISOU 2003 C GLY A 258 3640 3838 3693 106 14 182 ATOM 2004 O GLY A 258 25.868 23.051 -11.432 1.00 33.57 O ANISOU 2004 O GLY A 258 4167 4358 4228 119 13 187 ATOM 2005 N ILE A 259 23.773 23.353 -12.217 1.00 24.99 N ANISOU 2005 N ILE A 259 3100 3255 3142 110 20 170 ATOM 2006 CA ILE A 259 23.063 22.746 -11.092 1.00 17.91 C ANISOU 2006 CA ILE A 259 2223 2324 2258 124 25 165 ATOM 2007 C ILE A 259 22.652 21.324 -11.491 1.00 19.75 C ANISOU 2007 C ILE A 259 2450 2549 2504 141 42 144 ATOM 2008 O ILE A 259 21.878 21.164 -12.435 1.00 23.87 O ANISOU 2008 O ILE A 259 2970 3074 3026 140 51 130 ATOM 2009 CB ILE A 259 21.784 23.556 -10.729 1.00 19.23 C ANISOU 2009 CB ILE A 259 2412 2472 2423 117 19 164 ATOM 2010 CG1 ILE A 259 22.145 24.988 -10.286 1.00 21.23 C ANISOU 2010 CG1 ILE A 259 2674 2727 2666 104 -7 182 ATOM 2011 CG2 ILE A 259 20.880 22.881 -9.670 1.00 19.99 C ANISOU 2011 CG2 ILE A 259 2522 2544 2527 129 26 160 ATOM 2012 CD1 ILE A 259 20.970 25.958 -10.401 1.00 23.51 C ANISOU 2012 CD1 ILE A 259 2977 3005 2952 96 -20 177 ATOM 2013 N ALA A 260 23.152 20.324 -10.745 1.00 18.70 N ANISOU 2013 N ALA A 260 2316 2405 2384 156 43 144 ATOM 2014 CA ALA A 260 22.778 18.913 -10.874 1.00 22.03 C ANISOU 2014 CA ALA A 260 2737 2809 2824 172 50 127 ATOM 2015 C ALA A 260 21.273 18.697 -10.644 1.00 20.11 C ANISOU 2015 C ALA A 260 2512 2543 2585 167 54 125 ATOM 2016 O ALA A 260 20.688 19.389 -9.810 1.00 21.16 O ANISOU 2016 O ALA A 260 2660 2668 2710 157 52 138 ATOM 2017 CB ALA A 260 23.598 18.094 -9.866 1.00 26.22 C ANISOU 2017 CB ALA A 260 3269 3324 3369 185 41 135 ATOM 2018 N VAL A 261 20.669 17.752 -11.384 1.00 16.73 N ANISOU 2018 N VAL A 261 2082 2106 2169 174 60 107 ATOM 2019 CA VAL A 261 19.234 17.453 -11.311 1.00 16.85 C ANISOU 2019 CA VAL A 261 2112 2103 2188 167 64 106 ATOM 2020 C VAL A 261 18.777 17.001 -9.912 1.00 18.52 C ANISOU 2020 C VAL A 261 2338 2294 2406 163 58 125 ATOM 2021 O VAL A 261 17.717 17.438 -9.471 1.00 17.03 O ANISOU 2021 O VAL A 261 2159 2106 2206 152 61 134 ATOM 2022 CB VAL A 261 18.789 16.410 -12.373 1.00 22.58 C ANISOU 2022 CB VAL A 261 2832 2821 2928 176 66 84 ATOM 2023 CG1 VAL A 261 17.308 15.989 -12.260 1.00 12.99 C ANISOU 2023 CG1 VAL A 261 1631 1584 1718 166 68 88 ATOM 2024 CG2 VAL A 261 19.054 16.925 -13.801 1.00 24.95 C ANISOU 2024 CG2 VAL A 261 3116 3149 3214 176 75 66 ATOM 2025 N LEU A 262 19.611 16.212 -9.217 1.00 19.16 N ANISOU 2025 N LEU A 262 2418 2360 2501 172 47 131 ATOM 2026 CA LEU A 262 19.391 15.804 -7.831 1.00 15.64 C ANISOU 2026 CA LEU A 262 1985 1899 2059 163 39 154 ATOM 2027 C LEU A 262 19.533 16.946 -6.803 1.00 22.36 C ANISOU 2027 C LEU A 262 2841 2766 2889 155 41 170 ATOM 2028 O LEU A 262 18.906 16.857 -5.750 1.00 22.70 O ANISOU 2028 O LEU A 262 2893 2809 2923 144 41 184 ATOM 2029 CB LEU A 262 20.317 14.621 -7.492 1.00 20.08 C ANISOU 2029 CB LEU A 262 2546 2439 2644 174 22 158 ATOM 2030 CG LEU A 262 19.880 13.267 -8.102 1.00 24.97 C ANISOU 2030 CG LEU A 262 3166 3033 3287 180 12 145 ATOM 2031 CD1 LEU A 262 20.863 12.151 -7.699 1.00 25.19 C ANISOU 2031 CD1 LEU A 262 3193 3037 3341 194 -12 146 ATOM 2032 CD2 LEU A 262 18.425 12.877 -7.765 1.00 24.18 C ANISOU 2032 CD2 LEU A 262 3078 2922 3189 161 10 159 ATOM 2033 N ASP A 263 20.289 18.011 -7.120 1.00 25.71 N ANISOU 2033 N ASP A 263 3260 3206 3304 159 41 167 ATOM 2034 CA ASP A 263 20.313 19.247 -6.324 1.00 26.09 C ANISOU 2034 CA ASP A 263 3315 3266 3333 152 38 177 ATOM 2035 C ASP A 263 19.041 20.083 -6.533 1.00 18.54 C ANISOU 2035 C ASP A 263 2365 2317 2362 145 43 170 ATOM 2036 O ASP A 263 18.491 20.577 -5.550 1.00 20.47 O ANISOU 2036 O ASP A 263 2617 2568 2592 143 41 175 ATOM 2037 CB ASP A 263 21.581 20.113 -6.511 1.00 22.43 C ANISOU 2037 CB ASP A 263 2843 2815 2863 154 31 178 ATOM 2038 CG ASP A 263 22.906 19.423 -6.163 1.00 26.27 C ANISOU 2038 CG ASP A 263 3324 3299 3358 160 23 190 ATOM 2039 OD1 ASP A 263 22.889 18.233 -5.776 1.00 30.86 O ANISOU 2039 OD1 ASP A 263 3907 3864 3954 166 21 193 ATOM 2040 OD2 ASP A 263 23.936 20.121 -6.284 1.00 33.51 O1- ANISOU 2040 OD2 ASP A 263 4235 4229 4267 158 15 196 ATOM 2041 N MET A 264 18.552 20.178 -7.785 1.00 16.28 N ANISOU 2041 N MET A 264 2073 2034 2077 144 50 155 ATOM 2042 CA MET A 264 17.276 20.828 -8.104 1.00 21.27 C ANISOU 2042 CA MET A 264 2710 2672 2698 139 53 146 ATOM 2043 C MET A 264 16.058 20.086 -7.510 1.00 24.39 C ANISOU 2043 C MET A 264 3109 3064 3093 136 61 149 ATOM 2044 O MET A 264 15.078 20.738 -7.155 1.00 16.58 O ANISOU 2044 O MET A 264 2123 2085 2090 135 61 145 ATOM 2045 CB MET A 264 17.150 21.042 -9.631 1.00 15.59 C ANISOU 2045 CB MET A 264 1984 1957 1982 136 58 132 ATOM 2046 CG MET A 264 16.003 21.986 -10.040 1.00 15.93 C ANISOU 2046 CG MET A 264 2032 2005 2015 131 57 124 ATOM 2047 SD MET A 264 16.191 23.702 -9.483 1.00 20.57 S ANISOU 2047 SD MET A 264 2628 2598 2589 130 35 127 ATOM 2048 CE MET A 264 17.199 24.350 -10.838 1.00 26.01 C ANISOU 2048 CE MET A 264 3308 3295 3280 118 27 128 ATOM 2049 N CYS A 265 16.164 18.753 -7.362 1.00 22.36 N ANISOU 2049 N CYS A 265 2851 2794 2852 135 62 156 ATOM 2050 CA CYS A 265 15.199 17.895 -6.670 1.00 16.44 C ANISOU 2050 CA CYS A 265 2103 2043 2102 126 65 166 ATOM 2051 C CYS A 265 15.125 18.194 -5.163 1.00 13.78 C ANISOU 2051 C CYS A 265 1769 1720 1747 122 61 182 ATOM 2052 O CYS A 265 14.027 18.160 -4.613 1.00 17.05 O ANISOU 2052 O CYS A 265 2181 2151 2145 115 66 186 ATOM 2053 CB CYS A 265 15.509 16.401 -6.866 1.00 18.33 C ANISOU 2053 CB CYS A 265 2342 2258 2364 124 58 173 ATOM 2054 SG CYS A 265 15.116 15.887 -8.556 1.00 21.98 S ANISOU 2054 SG CYS A 265 2801 2708 2844 129 62 151 ATOM 2055 N ALA A 266 16.270 18.505 -4.528 1.00 21.30 N ANISOU 2055 N ALA A 266 2724 2671 2699 127 53 190 ATOM 2056 CA ALA A 266 16.341 18.901 -3.119 1.00 19.01 C ANISOU 2056 CA ALA A 266 2436 2396 2389 124 48 203 ATOM 2057 C ALA A 266 15.704 20.278 -2.865 1.00 18.43 C ANISOU 2057 C ALA A 266 2364 2346 2292 131 50 187 ATOM 2058 O ALA A 266 15.088 20.471 -1.817 1.00 24.75 O ANISOU 2058 O ALA A 266 3162 3171 3072 128 52 189 ATOM 2059 CB ALA A 266 17.803 18.890 -2.659 1.00 19.82 C ANISOU 2059 CB ALA A 266 2543 2490 2499 128 37 215 ATOM 2060 N SER A 267 15.832 21.190 -3.844 1.00 15.39 N ANISOU 2060 N SER A 267 1982 1957 1910 139 46 170 ATOM 2061 CA SER A 267 15.197 22.507 -3.840 1.00 14.99 C ANISOU 2061 CA SER A 267 1933 1920 1842 147 41 152 ATOM 2062 C SER A 267 13.675 22.414 -4.044 1.00 18.08 C ANISOU 2062 C SER A 267 2318 2327 2225 145 52 142 ATOM 2063 O SER A 267 12.934 23.074 -3.318 1.00 19.54 O ANISOU 2063 O SER A 267 2499 2536 2388 152 50 132 ATOM 2064 CB SER A 267 15.868 23.391 -4.902 1.00 21.33 C ANISOU 2064 CB SER A 267 2741 2711 2653 150 28 142 ATOM 2065 OG SER A 267 17.189 23.684 -4.498 1.00 24.66 O ANISOU 2065 OG SER A 267 3165 3124 3079 150 17 155 ATOM 2066 N LEU A 268 13.224 21.548 -4.972 1.00 23.51 N ANISOU 2066 N LEU A 268 3002 3003 2928 137 62 142 ATOM 2067 CA LEU A 268 11.805 21.247 -5.185 1.00 24.08 C ANISOU 2067 CA LEU A 268 3066 3090 2992 133 72 135 ATOM 2068 C LEU A 268 11.154 20.562 -3.967 1.00 21.87 C ANISOU 2068 C LEU A 268 2778 2834 2696 124 78 152 ATOM 2069 O LEU A 268 10.023 20.908 -3.637 1.00 24.44 O ANISOU 2069 O LEU A 268 3094 3190 3000 125 83 144 ATOM 2070 CB LEU A 268 11.621 20.433 -6.488 1.00 19.95 C ANISOU 2070 CB LEU A 268 2542 2548 2489 124 80 135 ATOM 2071 CG LEU A 268 10.161 20.029 -6.818 1.00 23.56 C ANISOU 2071 CG LEU A 268 2991 3017 2942 116 90 134 ATOM 2072 CD1 LEU A 268 9.190 21.226 -6.845 1.00 20.82 C ANISOU 2072 CD1 LEU A 268 2640 2696 2576 125 90 114 ATOM 2073 CD2 LEU A 268 10.083 19.217 -8.123 1.00 23.34 C ANISOU 2073 CD2 LEU A 268 2964 2966 2936 109 94 131 ATOM 2074 N LYS A 269 11.885 19.654 -3.294 1.00 17.93 N ANISOU 2074 N LYS A 269 2282 2325 2205 113 76 176 ATOM 2075 CA LYS A 269 11.485 19.004 -2.041 1.00 16.99 C ANISOU 2075 CA LYS A 269 2155 2234 2068 99 77 197 ATOM 2076 C LYS A 269 11.125 20.013 -0.935 1.00 20.18 C ANISOU 2076 C LYS A 269 2553 2677 2438 111 76 185 ATOM 2077 O LYS A 269 10.078 19.862 -0.309 1.00 20.27 O ANISOU 2077 O LYS A 269 2549 2728 2423 105 83 186 ATOM 2078 CB LYS A 269 12.587 18.008 -1.603 1.00 24.74 C ANISOU 2078 CB LYS A 269 3142 3193 3065 89 67 224 ATOM 2079 CG LYS A 269 12.451 17.433 -0.175 1.00 43.50 C ANISOU 2079 CG LYS A 269 5511 5598 5417 74 63 249 ATOM 2080 CD LYS A 269 13.633 16.583 0.297 1.00 43.25 C ANISOU 2080 CD LYS A 269 5488 5541 5405 65 49 275 ATOM 2081 CE LYS A 269 13.911 15.344 -0.561 1.00 46.89 C ANISOU 2081 CE LYS A 269 5953 5965 5899 52 39 290 ATOM 2082 NZ LYS A 269 14.962 14.525 0.059 1.00 52.84 N1+ ANISOU 2082 NZ LYS A 269 6715 6688 6676 50 20 308 ATOM 2083 N GLU A 270 11.986 21.025 -0.736 1.00 20.12 N ANISOU 2083 N GLU A 270 2554 2660 2429 128 67 172 ATOM 2084 CA GLU A 270 11.773 22.087 0.246 1.00 17.26 C ANISOU 2084 CA GLU A 270 2188 2333 2036 143 61 155 ATOM 2085 C GLU A 270 10.596 23.017 -0.118 1.00 24.99 C ANISOU 2085 C GLU A 270 3159 3335 3002 158 63 124 ATOM 2086 O GLU A 270 9.856 23.401 0.786 1.00 20.80 O ANISOU 2086 O GLU A 270 2614 2849 2439 167 65 112 ATOM 2087 CB GLU A 270 13.102 22.826 0.494 1.00 25.39 C ANISOU 2087 CB GLU A 270 3233 3342 3072 156 44 149 ATOM 2088 CG GLU A 270 13.015 23.997 1.500 1.00 37.70 C ANISOU 2088 CG GLU A 270 4791 4934 4601 174 33 131 ATOM 2089 CD GLU A 270 14.340 24.730 1.707 1.00 40.26 C ANISOU 2089 CD GLU A 270 5130 5234 4932 184 12 129 ATOM 2090 OE1 GLU A 270 15.367 24.035 1.869 1.00 42.28 O ANISOU 2090 OE1 GLU A 270 5392 5466 5204 171 11 154 ATOM 2091 OE2 GLU A 270 14.305 25.981 1.709 1.00 45.51 O1- ANISOU 2091 OE2 GLU A 270 5802 5904 5587 204 -7 102 ATOM 2092 N LEU A 271 10.403 23.313 -1.418 1.00 20.66 N ANISOU 2092 N LEU A 271 2617 2760 2474 162 62 111 ATOM 2093 CA LEU A 271 9.254 24.073 -1.932 1.00 21.83 C ANISOU 2093 CA LEU A 271 2757 2925 2613 176 61 82 ATOM 2094 C LEU A 271 7.912 23.345 -1.735 1.00 19.28 C ANISOU 2094 C LEU A 271 2413 2640 2271 165 79 88 ATOM 2095 O LEU A 271 6.918 24.015 -1.465 1.00 21.58 O ANISOU 2095 O LEU A 271 2690 2971 2539 179 79 65 ATOM 2096 CB LEU A 271 9.459 24.419 -3.425 1.00 21.39 C ANISOU 2096 CB LEU A 271 2711 2832 2583 177 55 72 ATOM 2097 CG LEU A 271 10.523 25.507 -3.693 1.00 23.08 C ANISOU 2097 CG LEU A 271 2942 3017 2810 187 31 63 ATOM 2098 CD1 LEU A 271 10.949 25.511 -5.178 1.00 25.52 C ANISOU 2098 CD1 LEU A 271 3259 3294 3145 177 29 68 ATOM 2099 CD2 LEU A 271 10.069 26.899 -3.195 1.00 28.79 C ANISOU 2099 CD2 LEU A 271 3667 3753 3518 213 8 30 ATOM 2100 N LEU A 272 7.900 22.005 -1.844 1.00 17.18 N ANISOU 2100 N LEU A 272 2145 2365 2017 139 90 120 ATOM 2101 CA LEU A 272 6.729 21.170 -1.564 1.00 19.98 C ANISOU 2101 CA LEU A 272 2480 2756 2356 122 103 133 ATOM 2102 C LEU A 272 6.393 21.122 -0.064 1.00 24.00 C ANISOU 2102 C LEU A 272 2970 3321 2826 119 106 141 ATOM 2103 O LEU A 272 5.219 21.216 0.292 1.00 20.18 O ANISOU 2103 O LEU A 272 2464 2890 2314 118 115 134 ATOM 2104 CB LEU A 272 6.957 19.734 -2.091 1.00 25.87 C ANISOU 2104 CB LEU A 272 3231 3473 3127 94 107 166 ATOM 2105 CG LEU A 272 6.922 19.575 -3.625 1.00 28.34 C ANISOU 2105 CG LEU A 272 3555 3740 3472 94 107 157 ATOM 2106 CD1 LEU A 272 7.420 18.173 -4.048 1.00 27.10 C ANISOU 2106 CD1 LEU A 272 3404 3552 3340 71 104 186 ATOM 2107 CD2 LEU A 272 5.532 19.904 -4.203 1.00 28.49 C ANISOU 2107 CD2 LEU A 272 3564 3775 3485 100 113 136 ATOM 2108 N GLN A 273 7.425 20.970 0.779 1.00 25.71 N ANISOU 2108 N GLN A 273 3196 3534 3040 116 99 156 ATOM 2109 CA GLN A 273 7.297 20.819 2.227 1.00 26.29 C ANISOU 2109 CA GLN A 273 3252 3662 3075 108 101 170 ATOM 2110 C GLN A 273 6.947 22.117 2.974 1.00 31.00 C ANISOU 2110 C GLN A 273 3838 4301 3638 140 97 130 ATOM 2111 O GLN A 273 6.200 22.047 3.950 1.00 37.30 O ANISOU 2111 O GLN A 273 4611 5167 4396 140 105 127 ATOM 2112 CB GLN A 273 8.582 20.172 2.780 1.00 19.56 C ANISOU 2112 CB GLN A 273 2414 2784 2234 93 92 200 ATOM 2113 CG GLN A 273 8.692 18.671 2.420 1.00 22.55 C ANISOU 2113 CG GLN A 273 2796 3135 2638 59 91 243 ATOM 2114 CD GLN A 273 10.021 18.008 2.800 1.00 26.65 C ANISOU 2114 CD GLN A 273 3331 3616 3178 49 78 269 ATOM 2115 OE1 GLN A 273 10.083 16.785 2.911 1.00 35.13 O ANISOU 2115 OE1 GLN A 273 4420 4666 4261 69 71 254 ATOM 2116 NE2 GLN A 273 11.093 18.781 2.985 1.00 31.86 N ANISOU 2116 NE2 GLN A 273 3990 4267 3848 18 70 309 ATOM 2117 N ASN A 274 7.496 23.261 2.525 1.00 31.61 N ANISOU 2117 N ASN A 274 3934 4344 3731 169 83 98 ATOM 2118 CA ASN A 274 7.394 24.549 3.225 1.00 24.65 C ANISOU 2118 CA ASN A 274 3049 3491 2825 204 70 57 ATOM 2119 C ASN A 274 6.522 25.577 2.482 1.00 37.13 C ANISOU 2119 C ASN A 274 4626 5072 4408 232 62 14 ATOM 2120 O ASN A 274 6.110 26.546 3.118 1.00 25.91 O ANISOU 2120 O ASN A 274 3197 3687 2963 263 50 -25 ATOM 2121 CB ASN A 274 8.806 25.155 3.450 1.00 25.68 C ANISOU 2121 CB ASN A 274 3206 3581 2971 215 50 54 ATOM 2122 CG ASN A 274 9.790 24.307 4.273 1.00 34.72 C ANISOU 2122 CG ASN A 274 4354 4728 4112 192 54 92 ATOM 2123 OD1 ASN A 274 10.998 24.496 4.165 1.00 39.08 O ANISOU 2123 OD1 ASN A 274 4888 5320 4642 170 68 118 ATOM 2124 ND2 ASN A 274 9.302 23.397 5.121 1.00 46.74 N ANISOU 2124 ND2 ASN A 274 5898 6207 5655 195 38 98 ATOM 2125 N GLY A 275 6.262 25.384 1.177 1.00 25.96 N ANISOU 2125 N GLY A 275 3219 3622 3023 223 66 18 ATOM 2126 CA GLY A 275 5.610 26.383 0.322 1.00 30.92 C ANISOU 2126 CA GLY A 275 3847 4240 3659 249 53 -22 ATOM 2127 C GLY A 275 6.628 27.439 -0.141 1.00 26.75 C ANISOU 2127 C GLY A 275 3346 3662 3154 267 23 -39 ATOM 2128 O GLY A 275 7.835 27.259 0.023 1.00 23.20 O ANISOU 2128 O GLY A 275 2913 3186 2715 259 16 -20 ATOM 2129 N MET A 276 6.130 28.535 -0.741 1.00 22.50 N ANISOU 2129 N MET A 276 2812 3110 2626 291 2 -74 ATOM 2130 CA MET A 276 6.945 29.661 -1.219 1.00 37.41 C ANISOU 2130 CA MET A 276 4726 4948 4539 304 -34 -88 ATOM 2131 C MET A 276 7.012 30.840 -0.235 1.00 38.50 C ANISOU 2131 C MET A 276 4867 5099 4661 341 -68 -128 ATOM 2132 O MET A 276 7.869 31.702 -0.417 1.00 32.52 O ANISOU 2132 O MET A 276 4133 4298 3924 349 -104 -136 ATOM 2133 CB MET A 276 6.420 30.183 -2.569 1.00 27.22 C ANISOU 2133 CB MET A 276 3443 3626 3275 303 -46 -98 ATOM 2134 CG MET A 276 6.397 29.150 -3.697 1.00 39.71 C ANISOU 2134 CG MET A 276 5025 5186 4876 271 -21 -65 ATOM 2135 SD MET A 276 6.194 29.922 -5.324 1.00 49.63 S ANISOU 2135 SD MET A 276 6295 6397 6163 269 -46 -74 ATOM 2136 CE MET A 276 5.870 28.435 -6.288 1.00 30.74 C ANISOU 2136 CE MET A 276 3888 4016 3775 244 -6 -54 ATOM 2137 N ASN A 277 6.120 30.878 0.771 1.00 38.88 N ANISOU 2137 N ASN A 277 4893 5208 4674 363 -60 -155 ATOM 2138 CA ASN A 277 6.061 31.902 1.822 1.00 43.96 C ANISOU 2138 CA ASN A 277 5535 5873 5296 403 -91 -198 ATOM 2139 C ASN A 277 5.768 33.327 1.291 1.00 37.03 C ANISOU 2139 C ASN A 277 4674 4956 4441 434 -139 -240 ATOM 2140 O ASN A 277 6.344 34.301 1.778 1.00 40.17 O ANISOU 2140 O ASN A 277 5090 5330 4844 456 -181 -262 ATOM 2141 CB ASN A 277 7.324 31.824 2.727 1.00 56.37 C ANISOU 2141 CB ASN A 277 7122 7434 6862 396 -98 -180 ATOM 2142 CG ASN A 277 6.970 31.719 4.211 1.00 71.81 C ANISOU 2142 CG ASN A 277 9054 9459 8770 412 -87 -196 ATOM 2143 OD1 ASN A 277 6.589 30.651 4.685 1.00 85.06 O ANISOU 2143 OD1 ASN A 277 10711 11182 10425 388 -49 -167 ATOM 2144 ND2 ASN A 277 7.091 32.827 4.944 1.00 78.01 N ANISOU 2144 ND2 ASN A 277 9843 10257 9540 452 -122 -243 ATOM 2145 N GLY A 278 4.865 33.416 0.298 1.00 33.18 N ANISOU 2145 N GLY A 278 4178 4461 3966 436 -138 -251 ATOM 2146 CA GLY A 278 4.427 34.671 -0.320 1.00 35.43 C ANISOU 2146 CA GLY A 278 4476 4709 4274 464 -187 -289 ATOM 2147 C GLY A 278 5.330 35.111 -1.485 1.00 34.77 C ANISOU 2147 C GLY A 278 4426 4552 4235 438 -214 -261 ATOM 2148 O GLY A 278 4.984 36.074 -2.171 1.00 29.87 O ANISOU 2148 O GLY A 278 3815 3897 3636 452 -255 -284 ATOM 2149 N ARG A 279 6.458 34.420 -1.730 1.00 34.82 N ANISOU 2149 N ARG A 279 4444 4535 4251 402 -195 -213 ATOM 2150 CA ARG A 279 7.346 34.670 -2.864 1.00 32.77 C ANISOU 2150 CA ARG A 279 4209 4216 4026 375 -218 -184 ATOM 2151 C ARG A 279 6.827 34.024 -4.157 1.00 38.00 C ANISOU 2151 C ARG A 279 4864 4870 4703 349 -192 -163 ATOM 2152 O ARG A 279 5.959 33.152 -4.116 1.00 40.72 O ANISOU 2152 O ARG A 279 5188 5251 5034 347 -154 -164 ATOM 2153 CB ARG A 279 8.765 34.184 -2.529 1.00 25.85 C ANISOU 2153 CB ARG A 279 3345 3324 3152 349 -209 -144 ATOM 2154 CG ARG A 279 9.385 34.929 -1.333 1.00 32.48 C ANISOU 2154 CG ARG A 279 4192 4173 3976 374 -235 -165 ATOM 2155 CD ARG A 279 10.917 34.898 -1.334 1.00 30.39 C ANISOU 2155 CD ARG A 279 3948 3874 3726 352 -251 -131 ATOM 2156 NE ARG A 279 11.447 35.677 -2.465 1.00 45.36 N ANISOU 2156 NE ARG A 279 5861 5720 5653 333 -287 -116 ATOM 2157 CZ ARG A 279 12.726 36.030 -2.657 1.00 44.56 C ANISOU 2157 CZ ARG A 279 5776 5587 5567 310 -310 -84 ATOM 2158 NH1 ARG A 279 13.668 35.761 -1.743 1.00 30.26 N ANISOU 2158 NH1 ARG A 279 3968 3784 3746 305 -300 -68 ATOM 2159 NH2 ARG A 279 13.069 36.670 -3.782 1.00 42.61 N1+ ANISOU 2159 NH2 ARG A 279 5542 5303 5345 288 -343 -67 ATOM 2160 N THR A 280 7.380 34.490 -5.285 1.00 33.36 N ANISOU 2160 N THR A 280 4294 4236 4144 326 -216 -142 ATOM 2161 CA THR A 280 7.024 34.048 -6.630 1.00 30.68 C ANISOU 2161 CA THR A 280 3950 3886 3819 303 -200 -126 ATOM 2162 C THR A 280 8.281 33.597 -7.391 1.00 16.05 C ANISOU 2162 C THR A 280 2107 2011 1981 264 -187 -80 ATOM 2163 O THR A 280 9.389 34.045 -7.093 1.00 27.27 O ANISOU 2163 O THR A 280 3541 3414 3406 255 -207 -64 ATOM 2164 CB THR A 280 6.357 35.198 -7.434 1.00 32.46 C ANISOU 2164 CB THR A 280 4185 4085 4065 314 -246 -149 ATOM 2165 OG1 THR A 280 7.214 36.320 -7.574 1.00 27.96 O ANISOU 2165 OG1 THR A 280 3638 3474 3511 312 -302 -145 ATOM 2166 CG2 THR A 280 5.032 35.667 -6.814 1.00 29.37 C ANISOU 2166 CG2 THR A 280 3779 3721 3659 356 -255 -199 ATOM 2167 N ILE A 281 8.059 32.710 -8.369 1.00 24.36 N ANISOU 2167 N ILE A 281 3150 3066 3038 241 -156 -62 ATOM 2168 CA ILE A 281 9.065 32.172 -9.277 1.00 22.58 C ANISOU 2168 CA ILE A 281 2930 2827 2824 207 -144 -26 ATOM 2169 C ILE A 281 8.516 32.382 -10.700 1.00 23.42 C ANISOU 2169 C ILE A 281 3036 2917 2945 190 -153 -21 ATOM 2170 O ILE A 281 7.428 31.890 -10.992 1.00 22.17 O ANISOU 2170 O ILE A 281 2867 2771 2785 192 -131 -31 ATOM 2171 CB ILE A 281 9.292 30.650 -9.033 1.00 24.86 C ANISOU 2171 CB ILE A 281 3205 3136 3103 196 -93 -7 ATOM 2172 CG1 ILE A 281 9.759 30.362 -7.588 1.00 24.09 C ANISOU 2172 CG1 ILE A 281 3107 3054 2991 210 -86 -7 ATOM 2173 CG2 ILE A 281 10.266 30.015 -10.047 1.00 20.63 C ANISOU 2173 CG2 ILE A 281 2671 2589 2579 168 -84 23 ATOM 2174 CD1 ILE A 281 9.778 28.872 -7.214 1.00 24.74 C ANISOU 2174 CD1 ILE A 281 3177 3158 3063 202 -43 9 ATOM 2175 N LEU A 282 9.238 33.157 -11.532 1.00 22.94 N ANISOU 2175 N LEU A 282 2987 2833 2897 170 -188 -4 ATOM 2176 CA LEU A 282 8.833 33.595 -12.883 1.00 29.26 C ANISOU 2176 CA LEU A 282 3788 3620 3710 150 -204 3 ATOM 2177 C LEU A 282 7.443 34.278 -12.916 1.00 26.31 C ANISOU 2177 C LEU A 282 3414 3240 3341 173 -223 -30 ATOM 2178 O LEU A 282 6.666 34.056 -13.847 1.00 24.17 O ANISOU 2178 O LEU A 282 3136 2974 3074 166 -210 -33 ATOM 2179 CB LEU A 282 8.944 32.433 -13.910 1.00 25.53 C ANISOU 2179 CB LEU A 282 3303 3165 3234 128 -159 22 ATOM 2180 CG LEU A 282 10.380 31.957 -14.203 1.00 26.06 C ANISOU 2180 CG LEU A 282 3366 3238 3298 103 -146 52 ATOM 2181 CD1 LEU A 282 10.358 30.665 -15.049 1.00 24.26 C ANISOU 2181 CD1 LEU A 282 3123 3028 3066 90 -101 60 ATOM 2182 CD2 LEU A 282 11.235 33.066 -14.860 1.00 26.39 C ANISOU 2182 CD2 LEU A 282 3415 3265 3346 77 -191 74 ATOM 2183 N GLY A 283 7.151 35.087 -11.883 1.00 25.87 N ANISOU 2183 N GLY A 283 3366 3178 3285 204 -256 -57 ATOM 2184 CA GLY A 283 5.897 35.822 -11.724 1.00 30.80 C ANISOU 2184 CA GLY A 283 3988 3801 3913 233 -279 -95 ATOM 2185 C GLY A 283 4.705 34.948 -11.290 1.00 32.18 C ANISOU 2185 C GLY A 283 4142 4012 4072 252 -232 -116 ATOM 2186 O GLY A 283 3.587 35.461 -11.295 1.00 34.94 O ANISOU 2186 O GLY A 283 4486 4366 4425 274 -247 -146 ATOM 2187 N SER A 284 4.912 33.669 -10.923 1.00 23.09 N ANISOU 2187 N SER A 284 2979 2889 2905 244 -181 -100 ATOM 2188 CA SER A 284 3.857 32.761 -10.465 1.00 22.13 C ANISOU 2188 CA SER A 284 2836 2805 2766 256 -141 -114 ATOM 2189 C SER A 284 4.063 32.391 -8.989 1.00 26.60 C ANISOU 2189 C SER A 284 3394 3403 3309 276 -124 -124 ATOM 2190 O SER A 284 5.181 32.075 -8.585 1.00 23.38 O ANISOU 2190 O SER A 284 2995 2990 2899 269 -122 -107 ATOM 2191 CB SER A 284 3.839 31.502 -11.354 1.00 31.87 C ANISOU 2191 CB SER A 284 4062 4045 4002 225 -97 -85 ATOM 2192 OG SER A 284 2.768 30.656 -10.988 1.00 37.51 O ANISOU 2192 OG SER A 284 4756 4796 4699 232 -61 -92 ATOM 2193 N ALA A 285 2.950 32.378 -8.238 1.00 20.85 N ANISOU 2193 N ALA A 285 2645 2713 2562 300 -112 -151 ATOM 2194 CA ALA A 285 2.867 31.910 -6.852 1.00 25.74 C ANISOU 2194 CA ALA A 285 3251 3376 3154 318 -94 -162 ATOM 2195 C ALA A 285 2.660 30.384 -6.732 1.00 25.69 C ANISOU 2195 C ALA A 285 3227 3400 3132 294 -44 -133 ATOM 2196 O ALA A 285 2.613 29.881 -5.608 1.00 31.44 O ANISOU 2196 O ALA A 285 3940 4169 3834 300 -26 -134 ATOM 2197 CB ALA A 285 1.727 32.674 -6.159 1.00 28.27 C ANISOU 2197 CB ALA A 285 3554 3732 3457 359 -112 -210 ATOM 2198 N LEU A 286 2.541 29.684 -7.874 1.00 25.56 N ANISOU 2198 N LEU A 286 3214 3364 3133 265 -25 -107 ATOM 2199 CA LEU A 286 2.371 28.234 -7.980 1.00 23.18 C ANISOU 2199 CA LEU A 286 2901 3083 2825 240 14 -79 ATOM 2200 C LEU A 286 3.516 27.635 -8.813 1.00 25.65 C ANISOU 2200 C LEU A 286 3230 3357 3159 212 22 -47 ATOM 2201 O LEU A 286 4.124 28.330 -9.628 1.00 25.37 O ANISOU 2201 O LEU A 286 3210 3287 3142 208 1 -46 ATOM 2202 CB LEU A 286 1.024 27.930 -8.676 1.00 22.37 C ANISOU 2202 CB LEU A 286 2781 2998 2722 236 28 -86 ATOM 2203 CG LEU A 286 -0.238 28.381 -7.906 1.00 33.19 C ANISOU 2203 CG LEU A 286 4126 4414 4069 263 25 -118 ATOM 2204 CD1 LEU A 286 -1.499 28.165 -8.762 1.00 32.43 C ANISOU 2204 CD1 LEU A 286 4018 4323 3980 252 36 -118 ATOM 2205 CD2 LEU A 286 -0.374 27.722 -6.517 1.00 35.84 C ANISOU 2205 CD2 LEU A 286 4442 4806 4372 265 46 -112 ATOM 2206 N LEU A 287 3.765 26.334 -8.604 1.00 18.64 N ANISOU 2206 N LEU A 287 2337 2477 2268 192 49 -20 ATOM 2207 CA LEU A 287 4.704 25.531 -9.383 1.00 15.48 C ANISOU 2207 CA LEU A 287 1949 2045 1888 171 57 4 ATOM 2208 C LEU A 287 4.027 25.103 -10.700 1.00 18.23 C ANISOU 2208 C LEU A 287 2296 2382 2250 157 64 5 ATOM 2209 O LEU A 287 3.089 24.305 -10.669 1.00 25.04 O ANISOU 2209 O LEU A 287 3145 3263 3107 153 78 5 ATOM 2210 CB LEU A 287 5.162 24.321 -8.531 1.00 17.50 C ANISOU 2210 CB LEU A 287 2202 2308 2139 158 75 29 ATOM 2211 CG LEU A 287 5.981 24.703 -7.270 1.00 20.44 C ANISOU 2211 CG LEU A 287 2576 2695 2496 171 67 29 ATOM 2212 CD1 LEU A 287 6.179 23.496 -6.338 1.00 27.74 C ANISOU 2212 CD1 LEU A 287 3495 3630 3413 156 83 55 ATOM 2213 CD2 LEU A 287 7.342 25.323 -7.624 1.00 31.67 C ANISOU 2213 CD2 LEU A 287 4016 4090 3929 177 46 26 ATOM 2214 N GLU A 288 4.496 25.675 -11.823 1.00 20.20 N ANISOU 2214 N GLU A 288 2556 2602 2515 149 52 7 ATOM 2215 CA GLU A 288 3.997 25.419 -13.181 1.00 24.62 C ANISOU 2215 CA GLU A 288 3116 3151 3088 137 56 6 ATOM 2216 C GLU A 288 4.512 24.068 -13.705 1.00 20.97 C ANISOU 2216 C GLU A 288 2654 2678 2634 119 75 24 ATOM 2217 O GLU A 288 5.692 23.782 -13.507 1.00 19.63 O ANISOU 2217 O GLU A 288 2491 2500 2470 116 76 35 ATOM 2218 CB GLU A 288 4.494 26.549 -14.110 1.00 25.21 C ANISOU 2218 CB GLU A 288 3201 3206 3172 135 30 -1 ATOM 2219 CG GLU A 288 4.033 27.975 -13.739 1.00 47.07 C ANISOU 2219 CG GLU A 288 5972 5976 5936 155 0 -22 ATOM 2220 CD GLU A 288 2.530 28.211 -13.875 1.00 53.93 C ANISOU 2220 CD GLU A 288 6832 6855 6806 164 -4 -42 ATOM 2221 OE1 GLU A 288 1.997 28.956 -13.028 1.00 55.36 O ANISOU 2221 OE1 GLU A 288 7010 7044 6980 188 -25 -66 ATOM 2222 OE2 GLU A 288 1.939 27.674 -14.836 1.00 46.04 O1- ANISOU 2222 OE2 GLU A 288 5827 5854 5811 150 12 -36 ATOM 2223 N ASP A 289 3.655 23.296 -14.399 1.00 17.94 N ANISOU 2223 N ASP A 289 2264 2297 2255 109 88 25 ATOM 2224 CA ASP A 289 3.983 21.945 -14.883 1.00 27.58 C ANISOU 2224 CA ASP A 289 3487 3505 3487 96 101 38 ATOM 2225 C ASP A 289 3.648 21.728 -16.379 1.00 24.15 C ANISOU 2225 C ASP A 289 3054 3060 3063 85 102 31 ATOM 2226 O ASP A 289 3.598 20.570 -16.794 1.00 17.32 O ANISOU 2226 O ASP A 289 2188 2186 2207 76 111 36 ATOM 2227 CB ASP A 289 3.368 20.825 -14.002 1.00 19.46 C ANISOU 2227 CB ASP A 289 2451 2487 2455 90 113 51 ATOM 2228 CG ASP A 289 1.849 20.631 -14.079 1.00 22.93 C ANISOU 2228 CG ASP A 289 2880 2939 2892 82 118 49 ATOM 2229 OD1 ASP A 289 1.132 21.543 -14.546 1.00 22.90 O ANISOU 2229 OD1 ASP A 289 2874 2941 2886 87 113 34 ATOM 2230 OD2 ASP A 289 1.416 19.540 -13.657 1.00 22.88 O1- ANISOU 2230 OD2 ASP A 289 2869 2938 2886 69 125 66 ATOM 2231 N GLU A 290 3.430 22.795 -17.169 1.00 19.63 N ANISOU 2231 N GLU A 290 2483 2486 2490 86 89 21 ATOM 2232 CA GLU A 290 3.136 22.686 -18.607 1.00 22.38 C ANISOU 2232 CA GLU A 290 2832 2827 2846 73 90 16 ATOM 2233 C GLU A 290 4.202 23.362 -19.484 1.00 25.39 C ANISOU 2233 C GLU A 290 3216 3204 3226 66 80 17 ATOM 2234 O GLU A 290 3.875 23.868 -20.557 1.00 25.58 O ANISOU 2234 O GLU A 290 3239 3228 3252 55 74 13 ATOM 2235 CB GLU A 290 1.693 23.127 -18.934 1.00 25.47 C ANISOU 2235 CB GLU A 290 3219 3223 3236 73 83 6 ATOM 2236 CG GLU A 290 0.625 22.371 -18.117 1.00 23.21 C ANISOU 2236 CG GLU A 290 2923 2948 2947 74 97 9 ATOM 2237 CD GLU A 290 -0.802 22.500 -18.658 1.00 35.48 C ANISOU 2237 CD GLU A 290 4470 4506 4503 68 98 3 ATOM 2238 OE1 GLU A 290 -1.032 23.321 -19.573 1.00 23.02 O ANISOU 2238 OE1 GLU A 290 2896 2920 2930 64 86 -6 ATOM 2239 OE2 GLU A 290 -1.654 21.730 -18.163 1.00 25.69 O1- ANISOU 2239 OE2 GLU A 290 3222 3279 3262 63 109 10 ATOM 2240 N PHE A 291 5.465 23.296 -19.038 1.00 19.65 N ANISOU 2240 N PHE A 291 2491 2478 2497 70 78 24 ATOM 2241 CA PHE A 291 6.658 23.547 -19.840 1.00 18.55 C ANISOU 2241 CA PHE A 291 2350 2344 2355 62 73 28 ATOM 2242 C PHE A 291 7.529 22.295 -19.737 1.00 22.49 C ANISOU 2242 C PHE A 291 2845 2845 2857 67 89 29 ATOM 2243 O PHE A 291 8.082 22.036 -18.667 1.00 18.75 O ANISOU 2243 O PHE A 291 2373 2367 2385 77 92 35 ATOM 2244 CB PHE A 291 7.448 24.764 -19.314 1.00 16.50 C ANISOU 2244 CB PHE A 291 2093 2086 2089 61 53 37 ATOM 2245 CG PHE A 291 6.731 26.094 -19.383 1.00 24.63 C ANISOU 2245 CG PHE A 291 3128 3110 3119 58 28 34 ATOM 2246 CD1 PHE A 291 6.734 26.833 -20.583 1.00 27.11 C ANISOU 2246 CD1 PHE A 291 3442 3426 3432 40 10 38 ATOM 2247 CD2 PHE A 291 5.958 26.546 -18.292 1.00 28.82 C ANISOU 2247 CD2 PHE A 291 3665 3635 3651 74 18 27 ATOM 2248 CE1 PHE A 291 6.061 28.045 -20.643 1.00 24.08 C ANISOU 2248 CE1 PHE A 291 3066 3032 3053 38 -20 36 ATOM 2249 CE2 PHE A 291 5.281 27.755 -18.378 1.00 33.65 C ANISOU 2249 CE2 PHE A 291 4281 4238 4265 77 -10 19 ATOM 2250 CZ PHE A 291 5.343 28.507 -19.545 1.00 20.76 C ANISOU 2250 CZ PHE A 291 2651 2601 2636 58 -32 24 ATOM 2251 N THR A 292 7.669 21.558 -20.851 1.00 16.82 N ANISOU 2251 N THR A 292 2119 2132 2138 61 96 21 ATOM 2252 CA THR A 292 8.623 20.452 -20.956 1.00 21.40 C ANISOU 2252 CA THR A 292 2695 2714 2723 71 104 15 ATOM 2253 C THR A 292 10.079 20.978 -20.941 1.00 18.14 C ANISOU 2253 C THR A 292 2274 2319 2300 71 100 21 ATOM 2254 O THR A 292 10.294 22.149 -21.264 1.00 17.02 O ANISOU 2254 O THR A 292 2129 2190 2146 58 88 31 ATOM 2255 CB THR A 292 8.403 19.586 -22.235 1.00 18.73 C ANISOU 2255 CB THR A 292 2351 2379 2386 70 110 -1 ATOM 2256 OG1 THR A 292 8.905 20.177 -23.419 1.00 21.95 O ANISOU 2256 OG1 THR A 292 2748 2814 2779 58 107 -4 ATOM 2257 CG2 THR A 292 6.951 19.153 -22.452 1.00 20.25 C ANISOU 2257 CG2 THR A 292 2550 2556 2588 65 112 -5 ATOM 2258 N PRO A 293 11.060 20.102 -20.620 1.00 17.69 N ANISOU 2258 N PRO A 293 2211 2264 2247 84 105 17 ATOM 2259 CA PRO A 293 12.494 20.408 -20.786 1.00 18.19 C ANISOU 2259 CA PRO A 293 2262 2352 2298 84 102 21 ATOM 2260 C PRO A 293 12.907 20.974 -22.160 1.00 28.17 C ANISOU 2260 C PRO A 293 3511 3650 3544 69 99 18 ATOM 2261 O PRO A 293 13.727 21.889 -22.195 1.00 22.92 O ANISOU 2261 O PRO A 293 2838 3006 2865 54 89 34 ATOM 2262 CB PRO A 293 13.190 19.077 -20.458 1.00 18.45 C ANISOU 2262 CB PRO A 293 2290 2380 2342 105 107 9 ATOM 2263 CG PRO A 293 12.234 18.375 -19.503 1.00 22.03 C ANISOU 2263 CG PRO A 293 2758 2798 2813 111 108 11 ATOM 2264 CD PRO A 293 10.861 18.792 -19.994 1.00 24.10 C ANISOU 2264 CD PRO A 293 3028 3054 3076 99 110 11 ATOM 2265 N PHE A 294 12.288 20.475 -23.246 1.00 23.58 N ANISOU 2265 N PHE A 294 2923 3074 2961 69 106 0 ATOM 2266 CA PHE A 294 12.534 20.946 -24.608 1.00 21.04 C ANISOU 2266 CA PHE A 294 2585 2790 2618 52 104 -2 ATOM 2267 C PHE A 294 11.910 22.323 -24.904 1.00 16.99 C ANISOU 2267 C PHE A 294 2080 2277 2099 26 89 20 ATOM 2268 O PHE A 294 12.528 23.078 -25.649 1.00 20.26 O ANISOU 2268 O PHE A 294 2481 2724 2495 5 78 34 ATOM 2269 CB PHE A 294 12.096 19.874 -25.622 1.00 28.91 C ANISOU 2269 CB PHE A 294 3578 3792 3616 58 114 -28 ATOM 2270 CG PHE A 294 12.492 20.146 -27.065 1.00 55.58 C ANISOU 2270 CG PHE A 294 6931 7220 6966 45 115 -36 ATOM 2271 CD1 PHE A 294 11.521 20.442 -28.043 1.00 69.90 C ANISOU 2271 CD1 PHE A 294 8744 9043 8770 28 113 -39 ATOM 2272 CD2 PHE A 294 13.856 20.161 -27.426 1.00 60.36 C ANISOU 2272 CD2 PHE A 294 7511 7870 7551 49 117 -38 ATOM 2273 CE1 PHE A 294 11.912 20.694 -29.352 1.00 76.13 C ANISOU 2273 CE1 PHE A 294 9509 9885 9531 14 114 -44 ATOM 2274 CE2 PHE A 294 14.226 20.428 -28.738 1.00 66.21 C ANISOU 2274 CE2 PHE A 294 8226 8670 8262 35 119 -43 ATOM 2275 CZ PHE A 294 13.255 20.683 -29.699 1.00 76.15 C ANISOU 2275 CZ PHE A 294 9485 9938 9510 16 118 -46 ATOM 2276 N ASP A 295 10.753 22.648 -24.294 1.00 23.20 N ANISOU 2276 N ASP A 295 2886 3029 2901 26 84 23 ATOM 2277 CA ASP A 295 10.118 23.977 -24.363 1.00 26.32 C ANISOU 2277 CA ASP A 295 3289 3418 3294 6 64 39 ATOM 2278 C ASP A 295 10.982 25.077 -23.741 1.00 22.54 C ANISOU 2278 C ASP A 295 2811 2945 2810 -2 44 60 ATOM 2279 O ASP A 295 11.075 26.160 -24.320 1.00 18.71 O ANISOU 2279 O ASP A 295 2324 2470 2316 -26 21 78 ATOM 2280 CB ASP A 295 8.716 24.059 -23.715 1.00 24.38 C ANISOU 2280 CB ASP A 295 3061 3139 3065 15 62 35 ATOM 2281 CG ASP A 295 7.723 23.006 -24.182 1.00 28.83 C ANISOU 2281 CG ASP A 295 3625 3695 3635 18 76 19 ATOM 2282 OD1 ASP A 295 7.841 22.542 -25.336 1.00 27.16 O ANISOU 2282 OD1 ASP A 295 3403 3502 3414 10 81 11 ATOM 2283 OD2 ASP A 295 6.808 22.716 -23.384 1.00 23.94 O1- ANISOU 2283 OD2 ASP A 295 3015 3053 3028 29 80 14 ATOM 2284 N VAL A 296 11.594 24.774 -22.583 1.00 21.00 N ANISOU 2284 N VAL A 296 2620 2738 2621 16 50 61 ATOM 2285 CA VAL A 296 12.487 25.683 -21.871 1.00 20.37 C ANISOU 2285 CA VAL A 296 2541 2660 2537 9 31 81 ATOM 2286 C VAL A 296 13.779 25.936 -22.665 1.00 18.27 C ANISOU 2286 C VAL A 296 2254 2435 2251 -10 25 94 ATOM 2287 O VAL A 296 14.160 27.097 -22.795 1.00 21.43 O ANISOU 2287 O VAL A 296 2654 2846 2644 -35 -1 117 ATOM 2288 CB VAL A 296 12.844 25.160 -20.453 1.00 12.22 C ANISOU 2288 CB VAL A 296 1517 1612 1515 32 39 78 ATOM 2289 CG1 VAL A 296 13.882 26.031 -19.710 1.00 21.56 C ANISOU 2289 CG1 VAL A 296 2700 2798 2692 24 18 99 ATOM 2290 CG2 VAL A 296 11.576 25.030 -19.592 1.00 14.99 C ANISOU 2290 CG2 VAL A 296 1884 1933 1879 46 42 69 ATOM 2291 N VAL A 297 14.380 24.870 -23.228 1.00 25.24 N ANISOU 2291 N VAL A 297 3120 3345 3127 0 48 80 ATOM 2292 CA VAL A 297 15.528 24.949 -24.137 1.00 41.07 C ANISOU 2292 CA VAL A 297 5098 5400 5107 -17 47 90 ATOM 2293 C VAL A 297 15.222 25.805 -25.384 1.00 38.43 C ANISOU 2293 C VAL A 297 4756 5089 4756 -51 30 105 ATOM 2294 O VAL A 297 15.982 26.727 -25.659 1.00 26.94 O ANISOU 2294 O VAL A 297 3288 3663 3283 -80 9 132 ATOM 2295 CB VAL A 297 16.036 23.536 -24.564 1.00 38.19 C ANISOU 2295 CB VAL A 297 4713 5061 4737 6 73 62 ATOM 2296 CG1 VAL A 297 16.972 23.503 -25.795 1.00 44.39 C ANISOU 2296 CG1 VAL A 297 5464 5910 5490 -12 74 66 ATOM 2297 CG2 VAL A 297 16.736 22.826 -23.390 1.00 35.15 C ANISOU 2297 CG2 VAL A 297 4330 4659 4365 34 81 54 ATOM 2298 N ARG A 298 14.098 25.523 -26.065 1.00 36.47 N ANISOU 2298 N ARG A 298 4515 4828 4513 -50 36 90 ATOM 2299 CA ARG A 298 13.587 26.237 -27.242 1.00 34.80 C ANISOU 2299 CA ARG A 298 4296 4642 4286 -83 21 103 ATOM 2300 C ARG A 298 13.382 27.747 -27.027 1.00 38.43 C ANISOU 2300 C ARG A 298 4771 5079 4752 -109 -18 133 ATOM 2301 O ARG A 298 13.800 28.524 -27.884 1.00 31.77 O ANISOU 2301 O ARG A 298 3916 4265 3891 -146 -42 160 ATOM 2302 CB ARG A 298 12.321 25.497 -27.741 1.00 48.34 C ANISOU 2302 CB ARG A 298 6017 6342 6008 -74 36 78 ATOM 2303 CG ARG A 298 11.229 26.309 -28.459 1.00 60.26 C ANISOU 2303 CG ARG A 298 7536 7844 7518 -102 13 92 ATOM 2304 CD ARG A 298 10.115 25.387 -28.973 1.00 61.50 C ANISOU 2304 CD ARG A 298 7700 7986 7684 -91 30 67 ATOM 2305 NE ARG A 298 8.821 26.080 -29.015 1.00 62.01 N ANISOU 2305 NE ARG A 298 7785 8006 7768 -93 12 71 ATOM 2306 CZ ARG A 298 7.768 25.798 -28.226 1.00 65.30 C ANISOU 2306 CZ ARG A 298 8218 8387 8207 -69 25 52 ATOM 2307 NH1 ARG A 298 6.678 26.569 -28.293 1.00 64.30 N ANISOU 2307 NH1 ARG A 298 8107 8230 8096 -71 8 55 ATOM 2308 NH2 ARG A 298 7.782 24.765 -27.372 1.00 61.55 N1+ ANISOU 2308 NH2 ARG A 298 7741 7906 7738 -43 52 31 ATOM 2309 N GLN A 299 12.751 28.131 -25.905 1.00 30.01 N ANISOU 2309 N GLN A 299 3730 3962 3710 -92 -27 129 ATOM 2310 CA GLN A 299 12.475 29.529 -25.572 1.00 24.98 C ANISOU 2310 CA GLN A 299 3109 3299 3082 -110 -69 151 ATOM 2311 C GLN A 299 13.715 30.301 -25.085 1.00 29.44 C ANISOU 2311 C GLN A 299 3672 3873 3642 -125 -95 178 ATOM 2312 O GLN A 299 13.811 31.498 -25.357 1.00 37.09 O ANISOU 2312 O GLN A 299 4648 4833 4612 -152 -138 205 ATOM 2313 CB GLN A 299 11.289 29.589 -24.590 1.00 31.10 C ANISOU 2313 CB GLN A 299 3909 4024 3883 -83 -72 132 ATOM 2314 CG GLN A 299 10.934 31.010 -24.099 1.00 26.19 C ANISOU 2314 CG GLN A 299 3305 3371 3273 -92 -121 146 ATOM 2315 CD GLN A 299 9.585 31.143 -23.391 1.00 31.63 C ANISOU 2315 CD GLN A 299 4013 4021 3983 -65 -126 123 ATOM 2316 OE1 GLN A 299 9.240 32.240 -22.961 1.00 27.83 O ANISOU 2316 OE1 GLN A 299 3548 3513 3515 -63 -166 126 ATOM 2317 NE2 GLN A 299 8.804 30.069 -23.267 1.00 21.94 N ANISOU 2317 NE2 GLN A 299 2784 2794 2759 -44 -89 99 ATOM 2318 N CYS A 300 14.642 29.606 -24.404 1.00 38.23 N ANISOU 2318 N CYS A 300 4776 4999 4751 -107 -73 174 ATOM 2319 CA CYS A 300 15.886 30.177 -23.882 1.00 41.43 C ANISOU 2319 CA CYS A 300 5175 5417 5148 -122 -95 201 ATOM 2320 C CYS A 300 17.055 30.109 -24.896 1.00 46.32 C ANISOU 2320 C CYS A 300 5761 6101 5737 -147 -87 219 ATOM 2321 O CYS A 300 18.137 30.594 -24.562 1.00 51.50 O ANISOU 2321 O CYS A 300 6406 6777 6384 -157 -97 240 ATOM 2322 CB CYS A 300 16.282 29.532 -22.534 1.00 43.54 C ANISOU 2322 CB CYS A 300 5454 5662 5429 -89 -80 188 ATOM 2323 SG CYS A 300 15.032 29.896 -21.261 1.00 50.38 S ANISOU 2323 SG CYS A 300 6353 6467 6322 -58 -88 167 ATOM 2324 N SER A 301 16.835 29.545 -26.101 1.00 44.88 N ANISOU 2324 N SER A 301 5560 5956 5538 -158 -69 210 ATOM 2325 CA SER A 301 17.817 29.474 -27.195 1.00 39.56 C ANISOU 2325 CA SER A 301 4849 5353 4829 -184 -64 226 ATOM 2326 C SER A 301 17.304 30.075 -28.520 1.00 48.26 C ANISOU 2326 C SER A 301 5939 6487 5911 -223 -80 242 ATOM 2327 O SER A 301 18.122 30.301 -29.411 1.00 47.01 O ANISOU 2327 O SER A 301 5747 6396 5719 -254 -82 263 ATOM 2328 CB SER A 301 18.336 28.029 -27.371 1.00 60.12 C ANISOU 2328 CB SER A 301 7431 7991 7423 -150 -19 190 ATOM 2329 OG SER A 301 17.400 27.179 -28.001 1.00 69.72 O ANISOU 2329 OG SER A 301 8644 9212 8636 -140 1 162 ATOM 2330 N GLY A 302 15.993 30.356 -28.625 1.00 49.68 N ANISOU 2330 N GLY A 302 6141 6625 6108 -224 -91 235 ATOM 2331 CA GLY A 302 15.387 31.052 -29.761 1.00 60.09 C ANISOU 2331 CA GLY A 302 7453 7966 7411 -267 -116 258 ATOM 2332 C GLY A 302 15.296 30.181 -31.024 1.00 56.42 C ANISOU 2332 C GLY A 302 6965 7550 6922 -268 -85 238 ATOM 2333 O GLY A 302 15.597 30.679 -32.109 1.00 45.65 O ANISOU 2333 O GLY A 302 5581 6232 5531 -311 -102 263 ATOM 2334 N VAL A 303 14.889 28.902 -30.898 1.00 58.09 N ANISOU 2334 N VAL A 303 7177 7752 7141 -224 -44 193 ATOM 2335 CA VAL A 303 14.644 27.999 -32.033 1.00 55.29 C ANISOU 2335 CA VAL A 303 6801 7440 6765 -221 -17 167 ATOM 2336 C VAL A 303 13.467 28.509 -32.895 1.00 51.73 C ANISOU 2336 C VAL A 303 6363 6973 6317 -247 -37 177 ATOM 2337 O VAL A 303 12.358 28.664 -32.381 1.00 31.57 O ANISOU 2337 O VAL A 303 3842 4356 3797 -236 -48 172 ATOM 2338 CB VAL A 303 14.331 26.543 -31.571 1.00 42.96 C ANISOU 2338 CB VAL A 303 5247 5856 5221 -168 21 118 ATOM 2339 CG1 VAL A 303 13.941 25.578 -32.715 1.00 45.56 C ANISOU 2339 CG1 VAL A 303 5555 6227 5528 -161 45 87 ATOM 2340 CG2 VAL A 303 15.510 25.942 -30.788 1.00 35.53 C ANISOU 2340 CG2 VAL A 303 4294 4924 4280 -142 36 110 ATOM 2341 N THR A 304 13.753 28.761 -34.183 1.00 61.25 N ANISOU 2341 N THR A 304 7542 8242 7488 -282 -40 190 ATOM 2342 CA THR A 304 12.809 29.274 -35.178 1.00 57.22 C ANISOU 2342 CA THR A 304 7038 7728 6974 -314 -61 203 ATOM 2343 C THR A 304 12.397 28.162 -36.164 1.00 54.69 C ANISOU 2343 C THR A 304 6704 7438 6637 -298 -28 166 ATOM 2344 O THR A 304 12.997 27.084 -36.181 1.00 43.33 O ANISOU 2344 O THR A 304 5246 6034 5184 -266 7 131 ATOM 2345 CB THR A 304 13.450 30.435 -35.990 1.00 50.83 C ANISOU 2345 CB THR A 304 6208 6969 6134 -376 -99 257 ATOM 2346 OG1 THR A 304 14.530 30.001 -36.799 1.00 52.36 O ANISOU 2346 OG1 THR A 304 6358 7254 6281 -387 -79 258 ATOM 2347 CG2 THR A 304 13.910 31.614 -35.122 1.00 24.87 C ANISOU 2347 CG2 THR A 304 2941 3640 2869 -394 -143 295 ATOM 2348 N PHE A 305 11.344 28.451 -36.950 1.00 50.82 N ANISOU 2348 N PHE A 305 6225 6934 6151 -319 -42 171 ATOM 2349 CA PHE A 305 10.682 27.492 -37.840 1.00 59.54 C ANISOU 2349 CA PHE A 305 7321 8061 7242 -306 -16 136 ATOM 2350 C PHE A 305 10.543 28.245 -39.140 1.00 60.66 C ANISOU 2350 C PHE A 305 7447 8247 7353 -357 -38 163 ATOM 2351 O PHE A 305 10.820 27.741 -40.227 1.00 55.63 O ANISOU 2351 O PHE A 305 6774 7690 6672 -373 -25 159 ATOM 2352 CB PHE A 305 9.306 27.068 -37.258 1.00 55.24 C ANISOU 2352 CB PHE A 305 6810 7439 6740 -268 -5 105 ATOM 2353 CG PHE A 305 9.381 26.608 -35.810 1.00 56.82 C ANISOU 2353 CG PHE A 305 7029 7588 6972 -229 6 91 ATOM 2354 CD1 PHE A 305 9.974 25.366 -35.504 1.00 54.28 C ANISOU 2354 CD1 PHE A 305 6700 7273 6652 -188 39 54 ATOM 2355 CD2 PHE A 305 9.120 27.523 -34.767 1.00 54.86 C ANISOU 2355 CD2 PHE A 305 6804 7287 6752 -232 -20 114 ATOM 2356 CE1 PHE A 305 10.298 25.060 -34.189 1.00 54.15 C ANISOU 2356 CE1 PHE A 305 6700 7211 6663 -155 47 46 ATOM 2357 CE2 PHE A 305 9.444 27.194 -33.458 1.00 49.82 C ANISOU 2357 CE2 PHE A 305 6181 6608 6138 -198 -9 102 ATOM 2358 CZ PHE A 305 10.046 25.975 -33.176 1.00 53.30 C ANISOU 2358 CZ PHE A 305 6614 7057 6579 -162 24 71 TER 2359 PHE A 305 HETATM 2360 N1 UNK 900 -20.791 20.451 -28.960 1.00 0.00 N HETATM 2361 C1 UNK 900 -21.289 19.426 -28.164 1.00 0.00 C HETATM 2362 N2 UNK 900 -20.474 18.959 -27.116 1.00 0.00 N HETATM 2363 C2 UNK 900 -19.244 19.514 -26.893 1.00 0.00 C HETATM 2364 N3 UNK 900 -18.825 20.504 -27.750 1.00 0.00 N HETATM 2365 C3 UNK 900 -19.591 21.017 -28.761 1.00 0.00 C HETATM 2366 O1 UNK 900 -19.220 21.928 -29.503 1.00 0.00 O HETATM 2367 O2 UNK 900 -18.521 19.122 -25.974 1.00 0.00 O HETATM 2368 C4 UNK 900 -17.421 20.979 -27.637 1.00 0.00 C HETATM 2369 N4 UNK 900 -22.460 18.907 -28.388 1.00 0.00 N HETATM 2370 C5 UNK 900 -23.204 19.310 -29.504 1.00 0.00 C HETATM 2371 C6 UNK 900 -20.965 17.820 -26.304 1.00 0.00 C HETATM 2372 C7 UNK 900 -20.928 16.466 -27.014 1.00 0.00 C HETATM 2373 C8 UNK 900 -21.984 15.546 -26.825 1.00 0.00 C HETATM 2374 C9 UNK 900 -21.965 14.295 -27.473 1.00 0.00 C HETATM 2375 C10 UNK 900 -20.884 13.946 -28.306 1.00 0.00 C HETATM 2376 C11 UNK 900 -19.825 14.854 -28.495 1.00 0.00 C HETATM 2377 C12 UNK 900 -19.851 16.110 -27.858 1.00 0.00 C HETATM 2378 F1 UNK 900 -18.779 14.521 -29.287 1.00 0.00 F HETATM 2379 F2 UNK 900 -20.863 12.740 -28.923 1.00 0.00 F HETATM 2380 F3 UNK 900 -22.987 13.424 -27.295 1.00 0.00 F HETATM 2381 C13 UNK 900 -17.120 22.012 -26.546 1.00 0.00 C HETATM 2382 N5 UNK 900 -18.142 22.592 -25.899 1.00 0.00 N HETATM 2383 O3 UNK 900 -15.941 22.268 -26.308 1.00 0.00 O HETATM 2384 C14 UNK 900 -17.986 23.570 -24.831 1.00 0.00 C HETATM 2385 C15 UNK 900 -23.262 18.436 -30.609 1.00 0.00 C HETATM 2386 C16 UNK 900 -23.968 18.793 -31.772 1.00 0.00 C HETATM 2387 C17 UNK 900 -24.625 20.036 -31.860 1.00 0.00 C HETATM 2388 C18 UNK 900 -24.589 20.905 -30.739 1.00 0.00 C HETATM 2389 C19 UNK 900 -23.904 20.544 -29.559 1.00 0.00 C HETATM 2390 C20 UNK 900 -23.931 21.498 -28.375 1.00 0.00 C HETATM 2391 O4 UNK 900 -25.243 20.335 -33.057 1.00 0.00 O HETATM 2392 C21 UNK 900 -25.964 21.482 -33.183 1.00 0.00 C HETATM 2393 F4 UNK 900 -25.136 22.542 -33.354 1.00 0.00 F HETATM 2394 F5 UNK 900 -26.744 21.408 -34.286 1.00 0.00 F CONECT 2360 2361 2365 CONECT 2361 2360 2362 2369 CONECT 2361 2369 CONECT 2362 2361 2363 2371 CONECT 2363 2362 2367 2364 CONECT 2363 2367 CONECT 2364 2363 2365 2368 CONECT 2365 2360 2364 2366 CONECT 2365 2366 CONECT 2366 2365 CONECT 2366 2365 CONECT 2367 2363 CONECT 2367 2363 CONECT 2368 2364 2381 CONECT 2369 2361 2370 CONECT 2369 2361 CONECT 2370 2369 2385 2389 CONECT 2370 2385 CONECT 2371 2362 2372 CONECT 2372 2371 2373 2377 CONECT 2372 2373 CONECT 2373 2372 2374 CONECT 2373 2372 CONECT 2374 2373 2375 2380 CONECT 2374 2375 CONECT 2375 2374 2376 2379 CONECT 2375 2374 CONECT 2376 2375 2377 2378 CONECT 2376 2377 CONECT 2377 2372 2376 CONECT 2377 2376 CONECT 2378 2376 CONECT 2379 2375 CONECT 2380 2374 CONECT 2381 2368 2382 2383 CONECT 2381 2383 CONECT 2382 2381 2384 CONECT 2383 2381 CONECT 2383 2381 CONECT 2384 2382 CONECT 2385 2370 2386 CONECT 2385 2370 CONECT 2386 2385 2387 CONECT 2386 2387 CONECT 2387 2386 2388 2391 CONECT 2387 2386 CONECT 2388 2387 2389 CONECT 2388 2389 CONECT 2389 2370 2388 2390 CONECT 2389 2388 CONECT 2390 2389 CONECT 2391 2387 2392 CONECT 2392 2391 2393 2394 CONECT 2393 2392 CONECT 2394 2392 END