HEADER PROTEIN BINDING 06-JUL-20 6ZN6 TITLE PROTEIN POLYBROMO-1 (PB1 BD2) BOUND TO MW278 EXPDTA X-RAY DIFFRACTION REMARK 2 RESOLUTION. 2.02 ANGSTROMS REMARK 3 R VALUE : 0.218000 REMARK 3 FREE R VALUE : 0.278000 REMARK 4 6ZN6 COMPLIES WITH FORMAT V. 3.30, REMARK 200 TEMPERATURE (KELVIN) : 100.00 REMARK 200 PH : 5.50 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.000000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.000000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.000000 REMARK 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.000000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.000000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.000000 REMARK 888 REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC) CRYST1 70.525 73.193 105.024 90.00 90.00 90.00 C 2 2 21 16 ATOM 1 N MET A 177 39.117 26.362 4.103 1.00 37.11 N ANISOU 1 N MET A 177 5167 4326 4607 548 -129 -460 ATOM 2 CA MET A 177 38.451 25.127 3.654 1.00 37.78 C ANISOU 2 CA MET A 177 5204 4456 4696 540 -68 -429 ATOM 3 C MET A 177 37.096 25.535 3.033 1.00 34.64 C ANISOU 3 C MET A 177 4818 4035 4310 565 -78 -436 ATOM 4 O MET A 177 36.182 25.942 3.755 1.00 35.05 O ANISOU 4 O MET A 177 4875 4036 4408 535 -120 -434 ATOM 5 CB MET A 177 38.345 24.081 4.797 1.00 42.45 C ANISOU 5 CB MET A 177 5741 5055 5332 468 -50 -390 ATOM 6 CG MET A 177 37.381 22.905 4.542 1.00 42.22 C ANISOU 6 CG MET A 177 5664 5072 5307 456 6 -358 ATOM 7 SD MET A 177 37.767 21.376 5.441 1.00 48.17 S ANISOU 7 SD MET A 177 6365 5856 6082 395 38 -321 ATOM 8 CE MET A 177 37.344 21.877 7.130 1.00 46.76 C ANISOU 8 CE MET A 177 6195 5627 5945 349 -13 -320 ATOM 9 H1 MET A 177 39.981 26.144 4.580 1.00 0.00 H ATOM 10 H2 MET A 177 39.376 26.937 3.314 1.00 0.00 H ATOM 11 HA MET A 177 39.061 24.664 2.874 1.00 0.00 H ATOM 12 HB3 MET A 177 38.022 24.583 5.712 1.00 0.00 H ATOM 13 HB2 MET A 177 39.339 23.689 5.017 1.00 0.00 H ATOM 14 HG3 MET A 177 37.358 22.662 3.480 1.00 0.00 H ATOM 15 HG2 MET A 177 36.367 23.212 4.801 1.00 0.00 H ATOM 16 HE1 MET A 177 37.496 21.045 7.817 1.00 0.00 H ATOM 17 HE2 MET A 177 37.968 22.711 7.451 1.00 0.00 H ATOM 18 HE3 MET A 177 36.299 22.182 7.185 1.00 0.00 H ATOM 19 N SER A 178 36.993 25.400 1.698 1.00 37.80 N ANISOU 19 N SER A 178 5220 4473 4670 622 -39 -440 ATOM 20 CA SER A 178 35.770 25.629 0.923 1.00 33.41 C ANISOU 20 CA SER A 178 4675 3898 4122 651 -45 -447 ATOM 21 C SER A 178 34.702 24.536 1.182 1.00 23.20 C ANISOU 21 C SER A 178 3328 2610 2875 596 -22 -408 ATOM 22 O SER A 178 35.063 23.454 1.650 1.00 23.48 O ANISOU 22 O SER A 178 3319 2679 2922 552 12 -377 ATOM 23 CB SER A 178 36.156 25.750 -0.571 1.00 31.13 C ANISOU 23 CB SER A 178 4396 3655 3776 730 -4 -455 ATOM 24 OG SER A 178 36.460 24.499 -1.163 1.00 32.75 O ANISOU 24 OG SER A 178 4545 3926 3974 720 62 -414 ATOM 25 H SER A 178 37.782 25.053 1.172 1.00 0.00 H ATOM 26 HA SER A 178 35.393 26.597 1.254 1.00 0.00 H ATOM 27 HB3 SER A 178 37.009 26.419 -0.695 1.00 0.00 H ATOM 28 HB2 SER A 178 35.339 26.196 -1.137 1.00 0.00 H ATOM 29 HG SER A 178 36.763 24.653 -2.062 1.00 0.00 H ATOM 30 N PRO A 179 33.419 24.799 0.826 1.00 15.83 N ANISOU 30 N PRO A 179 2404 1641 1969 599 -45 -410 ATOM 31 CA PRO A 179 32.353 23.775 0.881 1.00 15.46 C ANISOU 31 CA PRO A 179 2310 1608 1957 559 -19 -373 ATOM 32 C PRO A 179 32.605 22.521 0.021 1.00 20.96 C ANISOU 32 C PRO A 179 2964 2370 2630 568 45 -346 ATOM 33 O PRO A 179 32.227 21.429 0.440 1.00 21.96 O ANISOU 33 O PRO A 179 3048 2517 2778 520 69 -314 ATOM 34 CB PRO A 179 31.087 24.521 0.424 1.00 15.83 C ANISOU 34 CB PRO A 179 2381 1614 2019 587 -49 -386 ATOM 35 CG PRO A 179 31.384 25.987 0.685 1.00 21.57 C ANISOU 35 CG PRO A 179 3166 2283 2747 607 -114 -425 ATOM 36 CD PRO A 179 32.876 26.090 0.399 1.00 20.55 C ANISOU 36 CD PRO A 179 3058 2182 2569 638 -103 -446 ATOM 37 HA PRO A 179 32.239 23.478 1.926 1.00 0.00 H ATOM 38 HB3 PRO A 179 30.191 24.184 0.946 1.00 0.00 H ATOM 39 HB2 PRO A 179 30.914 24.379 -0.645 1.00 0.00 H ATOM 40 HG3 PRO A 179 31.200 26.211 1.737 1.00 0.00 H ATOM 41 HG2 PRO A 179 30.779 26.668 0.085 1.00 0.00 H ATOM 42 HD2 PRO A 179 33.049 26.214 -0.671 1.00 0.00 H ATOM 43 HD3 PRO A 179 33.296 26.949 0.922 1.00 0.00 H ATOM 44 N ALA A 180 33.254 22.703 -1.144 1.00 20.28 N ANISOU 44 N ALA A 180 2888 2316 2500 632 72 -355 ATOM 45 CA ALA A 180 33.641 21.631 -2.061 1.00 20.26 C ANISOU 45 CA ALA A 180 2841 2375 2482 641 128 -321 ATOM 46 C ALA A 180 34.775 20.751 -1.510 1.00 16.33 C ANISOU 46 C ALA A 180 2314 1912 1979 604 151 -301 ATOM 47 O ALA A 180 34.694 19.530 -1.645 1.00 19.80 O ANISOU 47 O ALA A 180 2708 2380 2435 570 179 -266 ATOM 48 CB ALA A 180 34.033 22.240 -3.416 1.00 23.12 C ANISOU 48 CB ALA A 180 3220 2768 2798 723 152 -330 ATOM 49 H ALA A 180 33.532 23.636 -1.414 1.00 0.00 H ATOM 50 HA ALA A 180 32.770 20.992 -2.219 1.00 0.00 H ATOM 51 HB1 ALA A 180 34.318 21.465 -4.129 1.00 0.00 H ATOM 52 HB2 ALA A 180 33.201 22.794 -3.851 1.00 0.00 H ATOM 53 HB3 ALA A 180 34.874 22.928 -3.318 1.00 0.00 H ATOM 54 N TYR A 181 35.784 21.375 -0.874 1.00 16.90 N ANISOU 54 N TYR A 181 2414 1977 2031 611 134 -324 ATOM 55 CA TYR A 181 36.895 20.672 -0.228 1.00 21.30 C ANISOU 55 CA TYR A 181 2947 2561 2586 576 150 -308 ATOM 56 C TYR A 181 36.444 19.919 1.035 1.00 23.47 C ANISOU 56 C TYR A 181 3197 2816 2906 504 139 -290 ATOM 57 O TYR A 181 36.867 18.781 1.230 1.00 25.06 O ANISOU 57 O TYR A 181 3359 3046 3115 472 165 -262 ATOM 58 CB TYR A 181 38.047 21.654 0.069 1.00 30.75 C ANISOU 58 CB TYR A 181 4184 3747 3752 599 127 -338 ATOM 59 CG TYR A 181 39.318 20.987 0.573 1.00 44.50 C ANISOU 59 CG TYR A 181 5902 5525 5483 577 150 -320 ATOM 60 CD1 TYR A 181 40.232 20.431 -0.347 1.00 46.56 C ANISOU 60 CD1 TYR A 181 6141 5842 5708 613 192 -299 ATOM 61 CD2 TYR A 181 39.578 20.886 1.957 1.00 47.62 C ANISOU 61 CD2 TYR A 181 6290 5898 5904 521 129 -320 ATOM 62 CE1 TYR A 181 41.392 19.777 0.113 1.00 48.39 C ANISOU 62 CE1 TYR A 181 6349 6104 5932 590 209 -279 ATOM 63 CE2 TYR A 181 40.733 20.228 2.418 1.00 48.45 C ANISOU 63 CE2 TYR A 181 6374 6034 6001 502 148 -303 ATOM 64 CZ TYR A 181 41.641 19.672 1.497 1.00 46.28 C ANISOU 64 CZ TYR A 181 6081 5812 5692 535 186 -284 ATOM 65 OH TYR A 181 42.759 19.031 1.946 1.00 48.01 O ANISOU 65 OH TYR A 181 6278 6058 5906 513 200 -266 ATOM 66 H TYR A 181 35.786 22.384 -0.800 1.00 0.00 H ATOM 67 HA TYR A 181 37.269 19.928 -0.936 1.00 0.00 H ATOM 68 HB3 TYR A 181 37.725 22.409 0.789 1.00 0.00 H ATOM 69 HB2 TYR A 181 38.300 22.200 -0.841 1.00 0.00 H ATOM 70 HD1 TYR A 181 40.040 20.493 -1.408 1.00 0.00 H ATOM 71 HD2 TYR A 181 38.881 21.292 2.670 1.00 0.00 H ATOM 72 HE1 TYR A 181 42.082 19.349 -0.599 1.00 0.00 H ATOM 73 HE2 TYR A 181 40.917 20.146 3.480 1.00 0.00 H ATOM 74 HH TYR A 181 43.303 18.679 1.237 1.00 0.00 H ATOM 75 N LEU A 182 35.564 20.544 1.838 1.00 20.30 N ANISOU 75 N LEU A 182 2816 2364 2533 480 99 -305 ATOM 76 CA LEU A 182 34.923 19.936 3.006 1.00 22.75 C ANISOU 76 CA LEU A 182 3102 2660 2883 420 92 -284 ATOM 77 C LEU A 182 34.073 18.712 2.631 1.00 18.28 C ANISOU 77 C LEU A 182 2499 2118 2330 403 122 -254 ATOM 78 O LEU A 182 34.137 17.713 3.340 1.00 16.48 O ANISOU 78 O LEU A 182 2242 1907 2111 367 138 -233 ATOM 79 CB LEU A 182 34.100 21.008 3.759 1.00 17.95 C ANISOU 79 CB LEU A 182 2517 1997 2308 403 44 -296 ATOM 80 CG LEU A 182 33.335 20.542 5.024 1.00 21.57 C ANISOU 80 CG LEU A 182 2947 2442 2806 348 39 -267 ATOM 81 CD1 LEU A 182 34.233 19.883 6.095 1.00 27.50 C ANISOU 81 CD1 LEU A 182 3681 3210 3557 317 49 -256 ATOM 82 CD2 LEU A 182 32.497 21.696 5.606 1.00 16.08 C ANISOU 82 CD2 LEU A 182 2269 1692 2148 334 -10 -269 ATOM 83 H LEU A 182 35.275 21.489 1.618 1.00 0.00 H ATOM 84 HA LEU A 182 35.728 19.589 3.655 1.00 0.00 H ATOM 85 HB3 LEU A 182 33.382 21.440 3.060 1.00 0.00 H ATOM 86 HB2 LEU A 182 34.761 21.827 4.037 1.00 0.00 H ATOM 87 HG LEU A 182 32.615 19.791 4.704 1.00 0.00 H ATOM 88 HD11 LEU A 182 34.139 20.357 7.071 1.00 0.00 H ATOM 89 HD12 LEU A 182 33.971 18.834 6.229 1.00 0.00 H ATOM 90 HD13 LEU A 182 35.288 19.916 5.833 1.00 0.00 H ATOM 91 HD21 LEU A 182 31.523 21.336 5.933 1.00 0.00 H ATOM 92 HD22 LEU A 182 32.982 22.166 6.462 1.00 0.00 H ATOM 93 HD23 LEU A 182 32.321 22.486 4.874 1.00 0.00 H ATOM 94 N LYS A 183 33.335 18.791 1.510 1.00 19.24 N ANISOU 94 N LYS A 183 2622 2239 2450 432 126 -254 ATOM 95 CA LYS A 183 32.530 17.692 0.978 1.00 20.62 C ANISOU 95 CA LYS A 183 2764 2433 2637 419 149 -225 ATOM 96 C LYS A 183 33.364 16.451 0.606 1.00 20.42 C ANISOU 96 C LYS A 183 2707 2454 2599 411 182 -201 ATOM 97 O LYS A 183 32.931 15.351 0.939 1.00 16.34 O ANISOU 97 O LYS A 183 2164 1946 2098 376 189 -179 ATOM 98 CB LYS A 183 31.638 18.213 -0.166 1.00 20.10 C ANISOU 98 CB LYS A 183 2706 2364 2567 461 151 -229 ATOM 99 CG LYS A 183 30.745 17.149 -0.825 1.00 17.96 C ANISOU 99 CG LYS A 183 2404 2105 2314 449 166 -199 ATOM 100 CD LYS A 183 29.648 17.778 -1.700 1.00 19.20 C ANISOU 100 CD LYS A 183 2580 2237 2479 481 152 -210 ATOM 101 CE LYS A 183 28.766 16.744 -2.417 1.00 28.50 C ANISOU 101 CE LYS A 183 3729 3430 3668 483 168 -182 ATOM 102 NZ LYS A 183 29.437 16.123 -3.573 1.00 31.97 N1+ ANISOU 102 NZ LYS A 183 4131 3917 4099 478 200 -151 ATOM 103 H LYS A 183 33.324 19.651 0.977 1.00 0.00 H ATOM 104 HA LYS A 183 31.861 17.387 1.786 1.00 0.00 H ATOM 105 HB3 LYS A 183 32.249 18.688 -0.935 1.00 0.00 H ATOM 106 HB2 LYS A 183 31.000 19.000 0.240 1.00 0.00 H ATOM 107 HG3 LYS A 183 30.281 16.531 -0.054 1.00 0.00 H ATOM 108 HG2 LYS A 183 31.360 16.478 -1.427 1.00 0.00 H ATOM 109 HD3 LYS A 183 30.094 18.465 -2.421 1.00 0.00 H ATOM 110 HD2 LYS A 183 29.006 18.392 -1.065 1.00 0.00 H ATOM 111 HE3 LYS A 183 27.854 17.221 -2.775 1.00 0.00 H ATOM 112 HE2 LYS A 183 28.473 15.959 -1.720 1.00 0.00 H ATOM 113 HZ1 LYS A 183 30.244 15.603 -3.249 1.00 0.00 H ATOM 114 HZ2 LYS A 183 28.798 15.477 -4.016 1.00 0.00 H ATOM 115 HZ3 LYS A 183 29.725 16.830 -4.234 1.00 0.00 H ATOM 116 N GLU A 184 34.559 16.641 0.014 1.00 13.69 N ANISOU 116 N GLU A 184 1855 1629 1716 446 199 -204 ATOM 117 CA GLU A 184 35.532 15.567 -0.232 1.00 16.81 C ANISOU 117 CA GLU A 184 2217 2066 2106 435 225 -176 ATOM 118 C GLU A 184 36.051 14.901 1.055 1.00 20.43 C ANISOU 118 C GLU A 184 2668 2517 2577 386 216 -174 ATOM 119 O GLU A 184 36.208 13.682 1.068 1.00 25.22 O ANISOU 119 O GLU A 184 3249 3137 3198 357 223 -149 ATOM 120 CB GLU A 184 36.725 16.075 -1.065 1.00 21.65 C ANISOU 120 CB GLU A 184 2832 2712 2683 481 245 -176 ATOM 121 CG GLU A 184 36.370 16.444 -2.521 1.00 33.38 C ANISOU 121 CG GLU A 184 4299 4228 4155 526 270 -154 ATOM 122 CD GLU A 184 37.559 16.907 -3.384 1.00 50.32 C ANISOU 122 CD GLU A 184 6440 6416 6262 575 296 -144 ATOM 123 OE1 GLU A 184 37.318 17.107 -4.595 1.00 57.48 O ANISOU 123 OE1 GLU A 184 7336 7352 7152 625 321 -126 ATOM 124 OE2 GLU A 184 38.682 17.059 -2.852 1.00 59.13 O1- ANISOU 124 OE2 GLU A 184 7563 7538 7364 564 294 -152 ATOM 125 H GLU A 184 34.854 17.576 -0.232 1.00 0.00 H ATOM 126 HA GLU A 184 35.026 14.793 -0.812 1.00 0.00 H ATOM 127 HB3 GLU A 184 37.509 15.315 -1.074 1.00 0.00 H ATOM 128 HB2 GLU A 184 37.160 16.946 -0.573 1.00 0.00 H ATOM 129 HG3 GLU A 184 35.615 17.230 -2.531 1.00 0.00 H ATOM 130 HG2 GLU A 184 35.915 15.579 -3.005 1.00 0.00 H ATOM 131 N ILE A 185 36.292 15.700 2.109 1.00 21.13 N ANISOU 131 N ILE A 185 2783 2582 2664 378 196 -198 ATOM 132 CA ILE A 185 36.742 15.220 3.418 1.00 24.41 C ANISOU 132 CA ILE A 185 3192 2991 3093 336 190 -195 ATOM 133 C ILE A 185 35.676 14.379 4.151 1.00 18.55 C ANISOU 133 C ILE A 185 2436 2237 2376 303 186 -180 ATOM 134 O ILE A 185 36.021 13.335 4.705 1.00 12.46 O ANISOU 134 O ILE A 185 1646 1478 1609 279 193 -164 ATOM 135 CB ILE A 185 37.228 16.396 4.324 1.00 24.29 C ANISOU 135 CB ILE A 185 3205 2948 3077 333 165 -220 ATOM 136 CG1 ILE A 185 38.511 17.063 3.772 1.00 26.63 C ANISOU 136 CG1 ILE A 185 3514 3261 3341 364 169 -233 ATOM 137 CG2 ILE A 185 37.390 16.049 5.819 1.00 21.76 C ANISOU 137 CG2 ILE A 185 2874 2615 2777 290 157 -211 ATOM 138 CD1 ILE A 185 39.725 16.139 3.595 1.00 30.23 C ANISOU 138 CD1 ILE A 185 3942 3759 3783 363 197 -210 ATOM 139 H ILE A 185 36.149 16.697 2.021 1.00 0.00 H ATOM 140 HA ILE A 185 37.584 14.550 3.238 1.00 0.00 H ATOM 141 HB ILE A 185 36.467 17.175 4.288 1.00 0.00 H ATOM 142 HG13 ILE A 185 38.785 17.911 4.402 1.00 0.00 H ATOM 143 HG12 ILE A 185 38.294 17.498 2.800 1.00 0.00 H ATOM 144 HG21 ILE A 185 37.917 16.838 6.354 1.00 0.00 H ATOM 145 HG22 ILE A 185 36.423 15.930 6.307 1.00 0.00 H ATOM 146 HG23 ILE A 185 37.939 15.120 5.958 1.00 0.00 H ATOM 147 HD11 ILE A 185 40.639 16.634 3.925 1.00 0.00 H ATOM 148 HD12 ILE A 185 39.629 15.211 4.156 1.00 0.00 H ATOM 149 HD13 ILE A 185 39.858 15.874 2.546 1.00 0.00 H ATOM 150 N LEU A 186 34.405 14.815 4.108 1.00 15.99 N ANISOU 150 N LEU A 186 2123 1887 2066 304 172 -184 ATOM 151 CA LEU A 186 33.276 14.087 4.693 1.00 19.23 C ANISOU 151 CA LEU A 186 2522 2288 2496 276 169 -168 ATOM 152 C LEU A 186 32.907 12.822 3.892 1.00 17.42 C ANISOU 152 C LEU A 186 2273 2082 2266 275 184 -148 ATOM 153 O LEU A 186 32.463 11.847 4.499 1.00 16.77 O ANISOU 153 O LEU A 186 2181 2002 2188 252 184 -135 ATOM 154 CB LEU A 186 32.054 15.017 4.843 1.00 19.22 C ANISOU 154 CB LEU A 186 2534 2255 2513 279 150 -172 ATOM 155 CG LEU A 186 32.270 16.281 5.707 1.00 17.78 C ANISOU 155 CG LEU A 186 2374 2042 2341 278 124 -189 ATOM 156 CD1 LEU A 186 31.070 17.238 5.584 1.00 16.95 C ANISOU 156 CD1 LEU A 186 2280 1901 2259 280 98 -188 ATOM 157 CD2 LEU A 186 32.625 15.969 7.174 1.00 18.51 C ANISOU 157 CD2 LEU A 186 2459 2133 2442 248 121 -180 ATOM 158 H LEU A 186 34.190 15.687 3.641 1.00 0.00 H ATOM 159 HA LEU A 186 33.576 13.751 5.686 1.00 0.00 H ATOM 160 HB3 LEU A 186 31.237 14.443 5.276 1.00 0.00 H ATOM 161 HB2 LEU A 186 31.723 15.323 3.848 1.00 0.00 H ATOM 162 HG LEU A 186 33.127 16.818 5.318 1.00 0.00 H ATOM 163 HD11 LEU A 186 30.901 17.812 6.495 1.00 0.00 H ATOM 164 HD12 LEU A 186 31.234 17.956 4.781 1.00 0.00 H ATOM 165 HD13 LEU A 186 30.151 16.703 5.349 1.00 0.00 H ATOM 166 HD21 LEU A 186 31.930 16.423 7.880 1.00 0.00 H ATOM 167 HD22 LEU A 186 32.634 14.903 7.384 1.00 0.00 H ATOM 168 HD23 LEU A 186 33.622 16.341 7.407 1.00 0.00 H ATOM 169 N GLU A 187 33.138 12.838 2.565 1.00 12.68 N ANISOU 169 N GLU A 187 1665 1496 1657 301 194 -143 ATOM 170 CA GLU A 187 33.035 11.669 1.688 1.00 14.92 C ANISOU 170 CA GLU A 187 1924 1801 1945 298 202 -118 ATOM 171 C GLU A 187 34.097 10.598 1.984 1.00 19.90 C ANISOU 171 C GLU A 187 2540 2450 2573 278 206 -105 ATOM 172 O GLU A 187 33.746 9.423 1.941 1.00 20.97 O ANISOU 172 O GLU A 187 2664 2587 2717 259 198 -88 ATOM 173 CB GLU A 187 33.072 12.097 0.207 1.00 16.03 C ANISOU 173 CB GLU A 187 2055 1959 2078 334 216 -109 ATOM 174 CG GLU A 187 31.727 12.675 -0.286 1.00 21.92 C ANISOU 174 CG GLU A 187 2813 2685 2833 352 209 -116 ATOM 175 CD GLU A 187 31.740 13.294 -1.694 1.00 29.35 C ANISOU 175 CD GLU A 187 3747 3643 3762 397 224 -110 ATOM 176 OE1 GLU A 187 32.832 13.561 -2.244 1.00 31.47 O ANISOU 176 OE1 GLU A 187 4009 3937 4010 423 241 -107 ATOM 177 OE2 GLU A 187 30.622 13.511 -2.207 1.00 26.61 O1- ANISOU 177 OE2 GLU A 187 3400 3284 3425 411 220 -107 ATOM 178 H GLU A 187 33.469 13.688 2.128 1.00 0.00 H ATOM 179 HA GLU A 187 32.065 11.203 1.876 1.00 0.00 H ATOM 180 HB3 GLU A 187 33.351 11.254 -0.430 1.00 0.00 H ATOM 181 HB2 GLU A 187 33.861 12.837 0.080 1.00 0.00 H ATOM 182 HG3 GLU A 187 31.380 13.442 0.404 1.00 0.00 H ATOM 183 HG2 GLU A 187 30.974 11.886 -0.257 1.00 0.00 H ATOM 184 N GLN A 188 35.336 11.000 2.324 1.00 12.51 N ANISOU 184 N GLN A 188 1607 1524 1624 284 212 -114 ATOM 185 CA GLN A 188 36.405 10.098 2.781 1.00 22.13 C ANISOU 185 CA GLN A 188 2812 2756 2842 264 211 -102 ATOM 186 C GLN A 188 36.097 9.427 4.130 1.00 19.78 C ANISOU 186 C GLN A 188 2524 2439 2551 236 198 -110 ATOM 187 O GLN A 188 36.406 8.247 4.298 1.00 23.37 O ANISOU 187 O GLN A 188 2971 2897 3011 219 190 -97 ATOM 188 CB GLN A 188 37.748 10.848 2.871 1.00 21.82 C ANISOU 188 CB GLN A 188 2775 2729 2787 276 220 -111 ATOM 189 CG GLN A 188 38.388 11.150 1.508 1.00 32.34 C ANISOU 189 CG GLN A 188 4095 4089 4103 310 237 -99 ATOM 190 CD GLN A 188 39.612 12.052 1.669 1.00 34.52 C ANISOU 190 CD GLN A 188 4380 4378 4359 321 243 -109 ATOM 191 OE1 GLN A 188 40.602 11.656 2.282 1.00 30.26 O ANISOU 191 OE1 GLN A 188 3866 3830 3801 346 242 -135 ATOM 192 NE2 GLN A 188 39.552 13.266 1.118 1.00 36.90 N ANISOU 192 NE2 GLN A 188 4661 4695 4664 303 244 -89 ATOM 193 H GLN A 188 35.558 11.987 2.312 1.00 0.00 H ATOM 194 HA GLN A 188 36.509 9.304 2.038 1.00 0.00 H ATOM 195 HB3 GLN A 188 38.461 10.264 3.459 1.00 0.00 H ATOM 196 HB2 GLN A 188 37.608 11.778 3.424 1.00 0.00 H ATOM 197 HG3 GLN A 188 37.668 11.613 0.835 1.00 0.00 H ATOM 198 HG2 GLN A 188 38.697 10.220 1.028 1.00 0.00 H ATOM 199 HE22 GLN A 188 40.338 13.896 1.190 1.00 0.00 H ATOM 200 HE21 GLN A 188 38.722 13.561 0.624 1.00 0.00 H ATOM 201 N LEU A 189 35.485 10.191 5.051 1.00 16.24 N ANISOU 201 N LEU A 189 2095 1973 2104 233 195 -128 ATOM 202 CA LEU A 189 35.052 9.732 6.370 1.00 19.16 C ANISOU 202 CA LEU A 189 2471 2331 2477 213 188 -129 ATOM 203 C LEU A 189 33.907 8.713 6.296 1.00 15.55 C ANISOU 203 C LEU A 189 2012 1871 2024 207 183 -116 ATOM 204 O LEU A 189 33.956 7.713 7.013 1.00 16.32 O ANISOU 204 O LEU A 189 2111 1971 2118 197 176 -112 ATOM 205 CB LEU A 189 34.633 10.951 7.217 1.00 12.57 C ANISOU 205 CB LEU A 189 1650 1478 1649 211 185 -140 ATOM 206 CG LEU A 189 35.811 11.811 7.713 1.00 19.38 C ANISOU 206 CG LEU A 189 2518 2340 2506 215 183 -154 ATOM 207 CD1 LEU A 189 35.347 13.212 8.153 1.00 20.03 C ANISOU 207 CD1 LEU A 189 2614 2397 2600 216 169 -163 ATOM 208 CD2 LEU A 189 36.602 11.097 8.824 1.00 15.22 C ANISOU 208 CD2 LEU A 189 1985 1821 1975 201 186 -152 ATOM 209 H LEU A 189 35.289 11.158 4.832 1.00 0.00 H ATOM 210 HA LEU A 189 35.895 9.230 6.845 1.00 0.00 H ATOM 211 HB3 LEU A 189 34.050 10.629 8.079 1.00 0.00 H ATOM 212 HB2 LEU A 189 33.954 11.569 6.630 1.00 0.00 H ATOM 213 HG LEU A 189 36.498 11.954 6.878 1.00 0.00 H ATOM 214 HD11 LEU A 189 35.808 13.513 9.091 1.00 0.00 H ATOM 215 HD12 LEU A 189 35.619 13.962 7.410 1.00 0.00 H ATOM 216 HD13 LEU A 189 34.267 13.266 8.286 1.00 0.00 H ATOM 217 HD21 LEU A 189 37.671 11.179 8.638 1.00 0.00 H ATOM 218 HD22 LEU A 189 36.402 11.522 9.805 1.00 0.00 H ATOM 219 HD23 LEU A 189 36.361 10.037 8.902 1.00 0.00 H ATOM 220 N LEU A 190 32.919 8.971 5.421 1.00 14.84 N ANISOU 220 N LEU A 190 1923 1775 1940 216 182 -112 ATOM 221 CA LEU A 190 31.799 8.065 5.174 1.00 18.37 C ANISOU 221 CA LEU A 190 2370 2220 2390 212 174 -100 ATOM 222 C LEU A 190 32.228 6.832 4.362 1.00 22.25 C ANISOU 222 C LEU A 190 2850 2722 2882 208 165 -86 ATOM 223 O LEU A 190 31.758 5.740 4.673 1.00 15.55 O ANISOU 223 O LEU A 190 2009 1870 2030 200 150 -81 ATOM 224 CB LEU A 190 30.639 8.829 4.498 1.00 18.99 C ANISOU 224 CB LEU A 190 2448 2290 2477 223 174 -96 ATOM 225 CG LEU A 190 29.318 8.029 4.392 1.00 17.80 C ANISOU 225 CG LEU A 190 2299 2137 2328 219 165 -81 ATOM 226 CD1 LEU A 190 28.741 7.646 5.774 1.00 15.27 C ANISOU 226 CD1 LEU A 190 1991 1811 1998 211 163 -81 ATOM 227 CD2 LEU A 190 28.289 8.779 3.528 1.00 12.42 C ANISOU 227 CD2 LEU A 190 1615 1447 1658 230 164 -76 ATOM 228 H LEU A 190 32.937 9.825 4.878 1.00 0.00 H ATOM 229 HA LEU A 190 31.453 7.712 6.148 1.00 0.00 H ATOM 230 HB3 LEU A 190 30.962 9.141 3.503 1.00 0.00 H ATOM 231 HB2 LEU A 190 30.441 9.753 5.043 1.00 0.00 H ATOM 232 HG LEU A 190 29.524 7.100 3.859 1.00 0.00 H ATOM 233 HD11 LEU A 190 27.662 7.786 5.833 1.00 0.00 H ATOM 234 HD12 LEU A 190 28.936 6.595 5.995 1.00 0.00 H ATOM 235 HD13 LEU A 190 29.182 8.235 6.580 1.00 0.00 H ATOM 236 HD21 LEU A 190 27.834 8.109 2.798 1.00 0.00 H ATOM 237 HD22 LEU A 190 27.489 9.205 4.132 1.00 0.00 H ATOM 238 HD23 LEU A 190 28.740 9.599 2.969 1.00 0.00 H ATOM 239 N GLU A 191 33.133 7.015 3.379 1.00 23.36 N ANISOU 239 N GLU A 191 2972 2876 3026 215 170 -78 ATOM 240 CA GLU A 191 33.743 5.942 2.588 1.00 22.87 C ANISOU 240 CA GLU A 191 2893 2824 2974 208 157 -56 ATOM 241 C GLU A 191 34.462 4.915 3.470 1.00 21.73 C ANISOU 241 C GLU A 191 2756 2673 2826 190 140 -59 ATOM 242 O GLU A 191 34.187 3.727 3.329 1.00 17.26 O ANISOU 242 O GLU A 191 2194 2099 2267 180 115 -49 ATOM 243 CB GLU A 191 34.659 6.506 1.481 1.00 16.13 C ANISOU 243 CB GLU A 191 2014 1992 2124 221 171 -39 ATOM 244 CG GLU A 191 35.407 5.436 0.652 1.00 27.80 C ANISOU 244 CG GLU A 191 3465 3479 3617 209 155 -7 ATOM 245 CD GLU A 191 36.243 6.060 -0.469 1.00 36.84 C ANISOU 245 CD GLU A 191 4578 4654 4767 227 174 21 ATOM 246 OE1 GLU A 191 37.328 6.590 -0.146 1.00 41.99 O ANISOU 246 OE1 GLU A 191 5224 5320 5411 230 184 23 ATOM 247 OE2 GLU A 191 35.787 5.988 -1.633 1.00 42.22 O1- ANISOU 247 OE2 GLU A 191 5240 5345 5457 241 179 45 ATOM 248 H GLU A 191 33.451 7.951 3.163 1.00 0.00 H ATOM 249 HA GLU A 191 32.932 5.429 2.073 1.00 0.00 H ATOM 250 HB3 GLU A 191 35.378 7.196 1.921 1.00 0.00 H ATOM 251 HB2 GLU A 191 34.049 7.099 0.797 1.00 0.00 H ATOM 252 HG3 GLU A 191 34.692 4.726 0.233 1.00 0.00 H ATOM 253 HG2 GLU A 191 36.079 4.851 1.282 1.00 0.00 H ATOM 254 N ALA A 192 35.311 5.405 4.391 1.00 22.93 N ANISOU 254 N ALA A 192 2915 2828 2970 189 151 -74 ATOM 255 CA ALA A 192 36.037 4.610 5.382 1.00 25.43 C ANISOU 255 CA ALA A 192 3241 3139 3283 177 136 -79 ATOM 256 C ALA A 192 35.123 3.713 6.228 1.00 23.76 C ANISOU 256 C ALA A 192 3054 2912 3062 176 122 -88 ATOM 257 O ALA A 192 35.441 2.537 6.390 1.00 19.13 O ANISOU 257 O ALA A 192 2478 2316 2474 171 98 -88 ATOM 258 CB ALA A 192 36.857 5.543 6.282 1.00 20.39 C ANISOU 258 CB ALA A 192 2606 2504 2636 177 152 -94 ATOM 259 H ALA A 192 35.474 6.404 4.424 1.00 0.00 H ATOM 260 HA ALA A 192 36.731 3.969 4.836 1.00 0.00 H ATOM 261 HB1 ALA A 192 37.477 4.980 6.980 1.00 0.00 H ATOM 262 HB2 ALA A 192 37.518 6.162 5.679 1.00 0.00 H ATOM 263 HB3 ALA A 192 36.222 6.212 6.864 1.00 0.00 H ATOM 264 N ILE A 193 33.995 4.273 6.700 1.00 21.94 N ANISOU 264 N ILE A 193 2834 2678 2824 185 135 -95 ATOM 265 CA ILE A 193 32.959 3.561 7.448 1.00 21.31 C ANISOU 265 CA ILE A 193 2777 2591 2730 190 127 -99 ATOM 266 C ILE A 193 32.292 2.438 6.631 1.00 20.41 C ANISOU 266 C ILE A 193 2668 2469 2618 189 99 -89 ATOM 267 O ILE A 193 32.202 1.319 7.137 1.00 16.65 O ANISOU 267 O ILE A 193 2215 1983 2128 194 76 -94 ATOM 268 CB ILE A 193 31.873 4.535 8.003 1.00 16.80 C ANISOU 268 CB ILE A 193 2210 2020 2154 198 147 -100 ATOM 269 CG1 ILE A 193 32.461 5.441 9.108 1.00 11.96 C ANISOU 269 CG1 ILE A 193 1594 1409 1540 198 165 -106 ATOM 270 CG2 ILE A 193 30.585 3.848 8.515 1.00 12.18 C ANISOU 270 CG2 ILE A 193 1644 1433 1551 210 140 -95 ATOM 271 CD1 ILE A 193 31.611 6.688 9.402 1.00 12.00 C ANISOU 271 CD1 ILE A 193 1596 1412 1552 200 178 -98 ATOM 272 H ILE A 193 33.808 5.247 6.504 1.00 0.00 H ATOM 273 HA ILE A 193 33.442 3.087 8.304 1.00 0.00 H ATOM 274 HB ILE A 193 31.574 5.193 7.187 1.00 0.00 H ATOM 275 HG13 ILE A 193 33.461 5.774 8.830 1.00 0.00 H ATOM 276 HG12 ILE A 193 32.596 4.862 10.024 1.00 0.00 H ATOM 277 HG21 ILE A 193 29.929 4.548 9.028 1.00 0.00 H ATOM 278 HG22 ILE A 193 30.001 3.410 7.705 1.00 0.00 H ATOM 279 HG23 ILE A 193 30.825 3.054 9.219 1.00 0.00 H ATOM 280 HD11 ILE A 193 32.186 7.599 9.240 1.00 0.00 H ATOM 281 HD12 ILE A 193 30.727 6.754 8.768 1.00 0.00 H ATOM 282 HD13 ILE A 193 31.278 6.687 10.439 1.00 0.00 H ATOM 283 N VAL A 194 31.838 2.750 5.403 1.00 18.97 N ANISOU 283 N VAL A 194 2468 2289 2452 186 98 -75 ATOM 284 CA VAL A 194 31.042 1.822 4.595 1.00 22.42 C ANISOU 284 CA VAL A 194 2909 2717 2894 185 70 -62 ATOM 285 C VAL A 194 31.851 0.726 3.868 1.00 24.91 C ANISOU 285 C VAL A 194 3214 3025 3226 172 36 -47 ATOM 286 O VAL A 194 31.256 -0.295 3.522 1.00 12.79 O ANISOU 286 O VAL A 194 1685 1477 1698 167 2 -36 ATOM 287 CB VAL A 194 30.099 2.535 3.589 1.00 19.87 C ANISOU 287 CB VAL A 194 2569 2398 2583 189 82 -49 ATOM 288 CG1 VAL A 194 29.122 3.484 4.309 1.00 12.42 C ANISOU 288 CG1 VAL A 194 1636 1454 1627 199 106 -60 ATOM 289 CG2 VAL A 194 30.809 3.237 2.420 1.00 22.05 C ANISOU 289 CG2 VAL A 194 2813 2687 2878 189 96 -36 ATOM 290 H VAL A 194 31.952 3.687 5.039 1.00 0.00 H ATOM 291 HA VAL A 194 30.396 1.299 5.290 1.00 0.00 H ATOM 292 HB VAL A 194 29.469 1.764 3.141 1.00 0.00 H ATOM 293 HG11 VAL A 194 28.388 3.896 3.617 1.00 0.00 H ATOM 294 HG12 VAL A 194 28.578 2.958 5.094 1.00 0.00 H ATOM 295 HG13 VAL A 194 29.634 4.321 4.780 1.00 0.00 H ATOM 296 HG21 VAL A 194 30.097 3.758 1.780 1.00 0.00 H ATOM 297 HG22 VAL A 194 31.514 3.971 2.795 1.00 0.00 H ATOM 298 HG23 VAL A 194 31.358 2.536 1.791 1.00 0.00 H ATOM 299 N VAL A 195 33.169 0.922 3.684 1.00 19.98 N ANISOU 299 N VAL A 195 2571 2407 2612 163 41 -42 ATOM 300 CA VAL A 195 34.075 -0.095 3.130 1.00 25.41 C ANISOU 300 CA VAL A 195 3246 3086 3321 148 4 -22 ATOM 301 C VAL A 195 34.771 -0.931 4.227 1.00 32.38 C ANISOU 301 C VAL A 195 4157 3953 4193 145 -20 -40 ATOM 302 O VAL A 195 35.362 -1.957 3.885 1.00 37.33 O ANISOU 302 O VAL A 195 4782 4563 4838 131 -63 -26 ATOM 303 CB VAL A 195 35.178 0.517 2.216 1.00 23.17 C ANISOU 303 CB VAL A 195 2921 2824 3060 142 21 5 ATOM 304 CG1 VAL A 195 34.583 1.309 1.036 1.00 17.36 C ANISOU 304 CG1 VAL A 195 2159 2106 2331 154 48 23 ATOM 305 CG2 VAL A 195 36.298 1.293 2.943 1.00 22.99 C ANISOU 305 CG2 VAL A 195 2899 2813 3024 145 48 -12 ATOM 306 H VAL A 195 33.590 1.801 3.956 1.00 0.00 H ATOM 307 HA VAL A 195 33.505 -0.793 2.516 1.00 0.00 H ATOM 308 HB VAL A 195 35.684 -0.324 1.736 1.00 0.00 H ATOM 309 HG11 VAL A 195 35.365 1.681 0.374 1.00 0.00 H ATOM 310 HG12 VAL A 195 33.925 0.677 0.439 1.00 0.00 H ATOM 311 HG13 VAL A 195 33.997 2.166 1.364 1.00 0.00 H ATOM 312 HG21 VAL A 195 36.902 1.870 2.244 1.00 0.00 H ATOM 313 HG22 VAL A 195 35.900 1.979 3.686 1.00 0.00 H ATOM 314 HG23 VAL A 195 36.976 0.617 3.466 1.00 0.00 H ATOM 315 N ALA A 196 34.701 -0.501 5.504 1.00 32.59 N ANISOU 315 N ALA A 196 4207 3983 4193 159 4 -68 ATOM 316 CA ALA A 196 35.305 -1.205 6.637 1.00 33.09 C ANISOU 316 CA ALA A 196 4296 4033 4242 163 -13 -87 ATOM 317 C ALA A 196 34.644 -2.564 6.894 1.00 35.29 C ANISOU 317 C ALA A 196 4611 4286 4512 170 -62 -94 ATOM 318 O ALA A 196 33.427 -2.631 7.073 1.00 23.59 O ANISOU 318 O ALA A 196 3149 2802 3012 184 -64 -100 ATOM 319 CB ALA A 196 35.255 -0.342 7.907 1.00 24.67 C ANISOU 319 CB ALA A 196 3244 2980 3151 180 26 -108 ATOM 320 H ALA A 196 34.196 0.347 5.721 1.00 0.00 H ATOM 321 HA ALA A 196 36.357 -1.371 6.396 1.00 0.00 H ATOM 322 HB1 ALA A 196 35.561 -0.913 8.785 1.00 0.00 H ATOM 323 HB2 ALA A 196 35.941 0.499 7.828 1.00 0.00 H ATOM 324 HB3 ALA A 196 34.256 0.046 8.101 1.00 0.00 H ATOM 325 N THR A 197 35.486 -3.605 6.926 1.00 46.87 N ANISOU 325 N THR A 197 6087 5731 5990 162 -105 -94 ATOM 326 CA THR A 197 35.108 -4.970 7.267 1.00 49.25 C ANISOU 326 CA THR A 197 6430 6000 6282 171 -162 -106 ATOM 327 C THR A 197 35.689 -5.343 8.641 1.00 50.95 C ANISOU 327 C THR A 197 6682 6205 6471 193 -169 -135 ATOM 328 O THR A 197 36.736 -4.827 9.040 1.00 53.53 O ANISOU 328 O THR A 197 6991 6542 6803 187 -145 -136 ATOM 329 CB THR A 197 35.670 -5.984 6.231 1.00 46.30 C ANISOU 329 CB THR A 197 6039 5601 5950 143 -223 -77 ATOM 330 OG1 THR A 197 37.087 -6.025 6.199 1.00 51.13 O ANISOU 330 OG1 THR A 197 6620 6217 6590 123 -221 -60 ATOM 331 CG2 THR A 197 35.147 -5.762 4.806 1.00 39.85 C ANISOU 331 CG2 THR A 197 5189 4795 5159 127 -220 -45 ATOM 332 H THR A 197 36.471 -3.458 6.758 1.00 0.00 H ATOM 333 HA THR A 197 34.024 -5.058 7.303 1.00 0.00 H ATOM 334 HB THR A 197 35.349 -6.979 6.537 1.00 0.00 H ATOM 335 HG1 THR A 197 37.404 -6.327 7.055 1.00 0.00 H ATOM 336 HG21 THR A 197 35.540 -6.517 4.123 1.00 0.00 H ATOM 337 HG22 THR A 197 34.060 -5.839 4.783 1.00 0.00 H ATOM 338 HG23 THR A 197 35.428 -4.783 4.417 1.00 0.00 H ATOM 339 N ASN A 198 35.016 -6.293 9.306 1.00 45.36 N ANISOU 339 N ASN A 198 6026 5477 5730 222 -201 -159 ATOM 340 CA ASN A 198 35.511 -6.992 10.496 1.00 46.51 C ANISOU 340 CA ASN A 198 6214 5612 5845 253 -210 -188 ATOM 341 C ASN A 198 36.580 -8.061 10.112 1.00 52.76 C ANISOU 341 C ASN A 198 7015 6366 6667 236 -277 -187 ATOM 342 O ASN A 198 36.848 -8.225 8.919 1.00 46.20 O ANISOU 342 O ASN A 198 6149 5522 5882 198 -307 -158 ATOM 343 CB ASN A 198 34.285 -7.511 11.304 1.00 40.67 C ANISOU 343 CB ASN A 198 5528 4872 5054 299 -215 -212 ATOM 344 CG ASN A 198 33.498 -8.685 10.702 1.00 38.32 C ANISOU 344 CG ASN A 198 5260 4541 4758 298 -282 -212 ATOM 345 OD1 ASN A 198 33.769 -9.152 9.599 1.00 37.64 O ANISOU 345 OD1 ASN A 198 5158 4428 4716 263 -333 -194 ATOM 346 ND2 ASN A 198 32.506 -9.177 11.444 1.00 34.06 N ANISOU 346 ND2 ASN A 198 4764 4005 4171 338 -283 -229 ATOM 347 H ASN A 198 34.160 -6.657 8.907 1.00 0.00 H ATOM 348 HA ASN A 198 36.030 -6.272 11.129 1.00 0.00 H ATOM 349 HB3 ASN A 198 33.588 -6.686 11.454 1.00 0.00 H ATOM 350 HB2 ASN A 198 34.579 -7.797 12.310 1.00 0.00 H ATOM 351 HD22 ASN A 198 31.967 -9.961 11.106 1.00 0.00 H ATOM 352 HD21 ASN A 198 32.299 -8.779 12.349 1.00 0.00 H ATOM 353 N PRO A 199 37.149 -8.812 11.089 1.00 62.98 N ANISOU 353 N PRO A 199 8352 7639 7937 265 -301 -216 ATOM 354 CA PRO A 199 38.092 -9.915 10.792 1.00 61.41 C ANISOU 354 CA PRO A 199 8166 7396 7771 247 -376 -214 ATOM 355 C PRO A 199 37.544 -11.080 9.939 1.00 54.41 C ANISOU 355 C PRO A 199 7304 6468 6902 237 -455 -207 ATOM 356 O PRO A 199 38.342 -11.775 9.311 1.00 53.74 O ANISOU 356 O PRO A 199 7202 6350 6867 201 -516 -183 ATOM 357 CB PRO A 199 38.556 -10.397 12.177 1.00 63.80 C ANISOU 357 CB PRO A 199 8520 7685 8036 292 -384 -251 ATOM 358 CG PRO A 199 38.348 -9.198 13.086 1.00 66.04 C ANISOU 358 CG PRO A 199 8794 8017 8281 320 -299 -260 ATOM 359 CD PRO A 199 37.072 -8.582 12.533 1.00 67.48 C ANISOU 359 CD PRO A 199 8956 8227 8456 313 -262 -245 ATOM 360 HA PRO A 199 38.943 -9.476 10.269 1.00 0.00 H ATOM 361 HB3 PRO A 199 39.591 -10.741 12.177 1.00 0.00 H ATOM 362 HB2 PRO A 199 37.936 -11.225 12.527 1.00 0.00 H ATOM 363 HG3 PRO A 199 39.175 -8.498 12.962 1.00 0.00 H ATOM 364 HG2 PRO A 199 38.281 -9.460 14.143 1.00 0.00 H ATOM 365 HD2 PRO A 199 36.212 -9.120 12.932 1.00 0.00 H ATOM 366 HD3 PRO A 199 36.991 -7.530 12.810 1.00 0.00 H ATOM 367 N SER A 200 36.210 -11.257 9.912 1.00 46.30 N ANISOU 367 N SER A 200 6312 5443 5838 265 -458 -223 ATOM 368 CA SER A 200 35.511 -12.259 9.103 1.00 48.53 C ANISOU 368 CA SER A 200 6624 5685 6132 259 -537 -219 ATOM 369 C SER A 200 35.271 -11.809 7.640 1.00 57.96 C ANISOU 369 C SER A 200 7758 6886 7378 209 -540 -172 ATOM 370 O SER A 200 34.869 -12.640 6.826 1.00 61.27 O ANISOU 370 O SER A 200 8188 7268 7822 193 -613 -158 ATOM 371 CB SER A 200 34.193 -12.622 9.822 1.00 47.39 C ANISOU 371 CB SER A 200 6540 5543 5922 312 -535 -252 ATOM 372 OG SER A 200 33.543 -13.726 9.225 1.00 49.81 O ANISOU 372 OG SER A 200 6888 5803 6233 313 -624 -257 ATOM 373 H SER A 200 35.620 -10.638 10.449 1.00 0.00 H ATOM 374 HA SER A 200 36.127 -13.160 9.066 1.00 0.00 H ATOM 375 HB3 SER A 200 33.505 -11.776 9.830 1.00 0.00 H ATOM 376 HB2 SER A 200 34.390 -12.877 10.865 1.00 0.00 H ATOM 377 HG SER A 200 33.378 -13.521 8.300 1.00 0.00 H ATOM 378 N GLY A 201 35.517 -10.524 7.325 1.00 61.27 N ANISOU 378 N GLY A 201 8116 7351 7813 188 -465 -146 ATOM 379 CA GLY A 201 35.378 -9.957 5.981 1.00 54.70 C ANISOU 379 CA GLY A 201 7227 6534 7023 152 -455 -102 ATOM 380 C GLY A 201 33.980 -9.366 5.716 1.00 59.66 C ANISOU 380 C GLY A 201 7852 7191 7624 166 -409 -104 ATOM 381 O GLY A 201 33.749 -8.876 4.611 1.00 68.01 O ANISOU 381 O GLY A 201 8863 8266 8714 141 -392 -69 ATOM 382 H GLY A 201 35.852 -9.897 8.045 1.00 0.00 H ATOM 383 HA3 GLY A 201 35.604 -10.703 5.217 1.00 0.00 H ATOM 384 HA2 GLY A 201 36.118 -9.165 5.868 1.00 0.00 H ATOM 385 N ARG A 202 33.063 -9.388 6.700 1.00 55.71 N ANISOU 385 N ARG A 202 7400 6700 7068 208 -386 -140 ATOM 386 CA ARG A 202 31.727 -8.794 6.611 1.00 50.84 C ANISOU 386 CA ARG A 202 6782 6109 6427 222 -346 -139 ATOM 387 C ARG A 202 31.784 -7.276 6.857 1.00 48.79 C ANISOU 387 C ARG A 202 6475 5894 6170 215 -262 -128 ATOM 388 O ARG A 202 32.390 -6.848 7.839 1.00 46.68 O ANISOU 388 O ARG A 202 6196 5641 5899 217 -226 -136 ATOM 389 CB ARG A 202 30.797 -9.495 7.630 1.00 43.73 C ANISOU 389 CB ARG A 202 5947 5206 5463 272 -350 -175 ATOM 390 CG ARG A 202 29.352 -8.944 7.673 1.00 37.55 C ANISOU 390 CG ARG A 202 5168 4443 4656 286 -325 -169 ATOM 391 CD ARG A 202 28.443 -9.605 8.726 1.00 37.07 C ANISOU 391 CD ARG A 202 5170 4389 4528 342 -319 -199 ATOM 392 NE ARG A 202 28.831 -9.273 10.111 1.00 40.79 N ANISOU 392 NE ARG A 202 5647 4884 4967 372 -268 -216 ATOM 393 CZ ARG A 202 28.571 -8.139 10.792 1.00 39.76 C ANISOU 393 CZ ARG A 202 5497 4796 4816 388 -196 -208 ATOM 394 NH1 ARG A 202 27.868 -7.120 10.272 1.00 39.75 N ANISOU 394 NH1 ARG A 202 5471 4815 4819 378 -166 -187 ATOM 395 NH2 ARG A 202 29.036 -8.020 12.040 1.00 33.50 N1+ ANISOU 395 NH2 ARG A 202 4708 4022 3999 413 -156 -219 ATOM 396 H ARG A 202 33.319 -9.768 7.601 1.00 0.00 H ATOM 397 HA ARG A 202 31.327 -8.976 5.611 1.00 0.00 H ATOM 398 HB3 ARG A 202 31.236 -9.414 8.625 1.00 0.00 H ATOM 399 HB2 ARG A 202 30.765 -10.562 7.405 1.00 0.00 H ATOM 400 HG3 ARG A 202 28.877 -8.966 6.692 1.00 0.00 H ATOM 401 HG2 ARG A 202 29.416 -7.888 7.935 1.00 0.00 H ATOM 402 HD3 ARG A 202 28.585 -10.684 8.663 1.00 0.00 H ATOM 403 HD2 ARG A 202 27.386 -9.433 8.525 1.00 0.00 H ATOM 404 HE ARG A 202 29.376 -9.982 10.578 1.00 0.00 H ATOM 405 HH12 ARG A 202 27.692 -6.292 10.827 1.00 0.00 H ATOM 406 HH11 ARG A 202 27.524 -7.167 9.324 1.00 0.00 H ATOM 407 HH22 ARG A 202 28.866 -7.163 12.559 1.00 0.00 H ATOM 408 HH21 ARG A 202 29.553 -8.768 12.478 1.00 0.00 H ATOM 409 N LEU A 203 31.085 -6.513 5.999 1.00 45.09 N ANISOU 409 N LEU A 203 5981 5443 5707 208 -235 -110 ATOM 410 CA LEU A 203 30.851 -5.072 6.137 1.00 39.46 C ANISOU 410 CA LEU A 203 5228 4766 4999 203 -165 -100 ATOM 411 C LEU A 203 29.982 -4.773 7.372 1.00 39.47 C ANISOU 411 C LEU A 203 5255 4787 4954 236 -123 -120 ATOM 412 O LEU A 203 28.818 -5.177 7.410 1.00 41.06 O ANISOU 412 O LEU A 203 5473 4992 5138 250 -124 -118 ATOM 413 CB LEU A 203 30.171 -4.541 4.853 1.00 30.96 C ANISOU 413 CB LEU A 203 4112 3697 3953 183 -159 -70 ATOM 414 CG LEU A 203 31.084 -4.514 3.606 1.00 36.20 C ANISOU 414 CG LEU A 203 4730 4360 4665 153 -171 -39 ATOM 415 CD1 LEU A 203 30.254 -4.340 2.314 1.00 43.28 C ANISOU 415 CD1 LEU A 203 5601 5251 5591 138 -195 -6 ATOM 416 CD2 LEU A 203 32.201 -3.456 3.733 1.00 36.57 C ANISOU 416 CD2 LEU A 203 4740 4436 4718 150 -112 -35 ATOM 417 H LEU A 203 30.614 -6.954 5.222 1.00 0.00 H ATOM 418 HA LEU A 203 31.816 -4.581 6.258 1.00 0.00 H ATOM 419 HB3 LEU A 203 29.785 -3.533 5.021 1.00 0.00 H ATOM 420 HB2 LEU A 203 29.294 -5.158 4.649 1.00 0.00 H ATOM 421 HG LEU A 203 31.570 -5.488 3.528 1.00 0.00 H ATOM 422 HD11 LEU A 203 30.529 -3.453 1.744 1.00 0.00 H ATOM 423 HD12 LEU A 203 30.385 -5.199 1.653 1.00 0.00 H ATOM 424 HD13 LEU A 203 29.187 -4.255 2.520 1.00 0.00 H ATOM 425 HD21 LEU A 203 32.250 -2.788 2.875 1.00 0.00 H ATOM 426 HD22 LEU A 203 32.074 -2.827 4.615 1.00 0.00 H ATOM 427 HD23 LEU A 203 33.178 -3.927 3.812 1.00 0.00 H ATOM 428 N ILE A 204 30.573 -4.078 8.359 1.00 36.62 N ANISOU 428 N ILE A 204 4894 4441 4579 247 -86 -132 ATOM 429 CA ILE A 204 29.936 -3.730 9.635 1.00 33.33 C ANISOU 429 CA ILE A 204 4496 4044 4122 279 -47 -142 ATOM 430 C ILE A 204 28.855 -2.631 9.530 1.00 27.61 C ANISOU 430 C ILE A 204 3746 3342 3403 275 -5 -125 ATOM 431 O ILE A 204 27.995 -2.554 10.405 1.00 25.92 O ANISOU 431 O ILE A 204 3546 3144 3159 300 21 -124 ATOM 432 CB ILE A 204 30.988 -3.273 10.686 1.00 40.36 C ANISOU 432 CB ILE A 204 5387 4946 5004 289 -20 -154 ATOM 433 CG1 ILE A 204 31.817 -2.030 10.264 1.00 35.19 C ANISOU 433 CG1 ILE A 204 4685 4302 4384 259 11 -142 ATOM 434 CG2 ILE A 204 31.897 -4.452 11.082 1.00 44.35 C ANISOU 434 CG2 ILE A 204 5922 5425 5503 297 -66 -173 ATOM 435 CD1 ILE A 204 32.654 -1.428 11.397 1.00 37.88 C ANISOU 435 CD1 ILE A 204 5020 4657 4716 268 45 -148 ATOM 436 H ILE A 204 31.531 -3.777 8.246 1.00 0.00 H ATOM 437 HA ILE A 204 29.441 -4.624 10.017 1.00 0.00 H ATOM 438 HB ILE A 204 30.443 -2.996 11.590 1.00 0.00 H ATOM 439 HG13 ILE A 204 31.176 -1.238 9.880 1.00 0.00 H ATOM 440 HG12 ILE A 204 32.482 -2.297 9.444 1.00 0.00 H ATOM 441 HG21 ILE A 204 32.541 -4.195 11.923 1.00 0.00 H ATOM 442 HG22 ILE A 204 31.308 -5.319 11.383 1.00 0.00 H ATOM 443 HG23 ILE A 204 32.537 -4.757 10.253 1.00 0.00 H ATOM 444 HD11 ILE A 204 32.958 -0.408 11.159 1.00 0.00 H ATOM 445 HD12 ILE A 204 32.085 -1.392 12.325 1.00 0.00 H ATOM 446 HD13 ILE A 204 33.559 -2.009 11.573 1.00 0.00 H ATOM 447 N SER A 205 28.924 -1.815 8.467 1.00 24.40 N ANISOU 447 N SER A 205 3302 2937 3034 247 3 -109 ATOM 448 CA SER A 205 28.069 -0.657 8.212 1.00 19.58 C ANISOU 448 CA SER A 205 2668 2342 2430 245 40 -96 ATOM 449 C SER A 205 26.638 -0.983 7.762 1.00 18.71 C ANISOU 449 C SER A 205 2573 2230 2307 255 27 -86 ATOM 450 O SER A 205 25.792 -0.094 7.843 1.00 14.06 O ANISOU 450 O SER A 205 1975 1654 1714 261 56 -76 ATOM 451 CB SER A 205 28.773 0.198 7.143 1.00 22.82 C ANISOU 451 CB SER A 205 3039 2754 2877 220 51 -85 ATOM 452 OG SER A 205 28.775 -0.451 5.881 1.00 22.24 O ANISOU 452 OG SER A 205 2956 2669 2826 206 17 -73 ATOM 453 H SER A 205 29.654 -1.965 7.785 1.00 0.00 H ATOM 454 HA SER A 205 28.007 -0.072 9.131 1.00 0.00 H ATOM 455 HB3 SER A 205 29.797 0.411 7.445 1.00 0.00 H ATOM 456 HB2 SER A 205 28.274 1.162 7.034 1.00 0.00 H ATOM 457 HG SER A 205 27.906 -0.359 5.482 1.00 0.00 H ATOM 458 N GLU A 206 26.414 -2.199 7.230 1.00 19.28 N ANISOU 458 N GLU A 206 2665 2284 2375 255 -19 -88 ATOM 459 CA GLU A 206 25.251 -2.529 6.405 1.00 21.02 C ANISOU 459 CA GLU A 206 2892 2500 2594 257 -36 -76 ATOM 460 C GLU A 206 23.904 -2.495 7.155 1.00 21.00 C ANISOU 460 C GLU A 206 2910 2513 2554 285 -12 -73 ATOM 461 O GLU A 206 22.902 -2.103 6.558 1.00 19.10 O ANISOU 461 O GLU A 206 2654 2280 2322 282 4 -56 ATOM 462 CB GLU A 206 25.508 -3.872 5.685 1.00 26.14 C ANISOU 462 CB GLU A 206 3566 3123 3243 255 -98 -79 ATOM 463 CG GLU A 206 24.543 -4.169 4.512 1.00 42.47 C ANISOU 463 CG GLU A 206 5617 5183 5336 239 -119 -57 ATOM 464 CD GLU A 206 24.653 -3.167 3.348 1.00 43.98 C ANISOU 464 CD GLU A 206 5754 5383 5572 214 -94 -36 ATOM 465 OE1 GLU A 206 23.588 -2.681 2.906 1.00 42.74 O ANISOU 465 OE1 GLU A 206 5578 5239 5420 216 -60 -27 ATOM 466 OE2 GLU A 206 25.796 -2.895 2.915 1.00 41.86 O1- ANISOU 466 OE2 GLU A 206 5464 5108 5333 196 -109 -29 ATOM 467 H GLU A 206 27.167 -2.872 7.216 1.00 0.00 H ATOM 468 HA GLU A 206 25.206 -1.749 5.644 1.00 0.00 H ATOM 469 HB3 GLU A 206 25.435 -4.685 6.409 1.00 0.00 H ATOM 470 HB2 GLU A 206 26.538 -3.910 5.326 1.00 0.00 H ATOM 471 HG3 GLU A 206 23.515 -4.217 4.875 1.00 0.00 H ATOM 472 HG2 GLU A 206 24.761 -5.161 4.115 1.00 0.00 H ATOM 473 N LEU A 207 23.911 -2.848 8.453 1.00 17.81 N ANISOU 473 N LEU A 207 2540 2117 2110 315 -8 -87 ATOM 474 CA LEU A 207 22.758 -2.723 9.352 1.00 17.10 C ANISOU 474 CA LEU A 207 2468 2049 1981 347 18 -77 ATOM 475 C LEU A 207 22.394 -1.253 9.653 1.00 17.33 C ANISOU 475 C LEU A 207 2457 2098 2031 337 67 -54 ATOM 476 O LEU A 207 21.216 -0.951 9.839 1.00 18.12 O ANISOU 476 O LEU A 207 2555 2212 2120 348 84 -33 ATOM 477 CB LEU A 207 23.030 -3.568 10.624 1.00 19.30 C ANISOU 477 CB LEU A 207 2785 2337 2210 389 21 -93 ATOM 478 CG LEU A 207 21.938 -3.510 11.724 1.00 29.11 C ANISOU 478 CG LEU A 207 4039 3612 3410 428 57 -74 ATOM 479 CD1 LEU A 207 21.817 -4.854 12.467 1.00 27.76 C ANISOU 479 CD1 LEU A 207 3928 3442 3177 478 30 -91 ATOM 480 CD2 LEU A 207 22.159 -2.342 12.711 1.00 26.25 C ANISOU 480 CD2 LEU A 207 3649 3276 3049 435 110 -58 ATOM 481 H LEU A 207 24.776 -3.153 8.876 1.00 0.00 H ATOM 482 HA LEU A 207 21.897 -3.164 8.846 1.00 0.00 H ATOM 483 HB3 LEU A 207 24.002 -3.319 11.052 1.00 0.00 H ATOM 484 HB2 LEU A 207 23.126 -4.603 10.290 1.00 0.00 H ATOM 485 HG LEU A 207 20.975 -3.352 11.237 1.00 0.00 H ATOM 486 HD11 LEU A 207 21.382 -4.740 13.461 1.00 0.00 H ATOM 487 HD12 LEU A 207 21.169 -5.538 11.919 1.00 0.00 H ATOM 488 HD13 LEU A 207 22.786 -5.342 12.581 1.00 0.00 H ATOM 489 HD21 LEU A 207 22.123 -2.656 13.754 1.00 0.00 H ATOM 490 HD22 LEU A 207 23.118 -1.849 12.558 1.00 0.00 H ATOM 491 HD23 LEU A 207 21.393 -1.581 12.579 1.00 0.00 H ATOM 492 N PHE A 208 23.408 -0.374 9.675 1.00 16.91 N ANISOU 492 N PHE A 208 2373 2044 2008 314 87 -56 ATOM 493 CA PHE A 208 23.285 1.048 10.000 1.00 15.62 C ANISOU 493 CA PHE A 208 2176 1892 1866 304 125 -37 ATOM 494 C PHE A 208 22.906 1.929 8.795 1.00 15.45 C ANISOU 494 C PHE A 208 2127 1859 1883 279 123 -27 ATOM 495 O PHE A 208 22.658 3.117 9.000 1.00 18.42 O ANISOU 495 O PHE A 208 2479 2238 2282 269 145 -14 ATOM 496 CB PHE A 208 24.588 1.540 10.655 1.00 15.06 C ANISOU 496 CB PHE A 208 2092 1825 1806 297 143 -46 ATOM 497 CG PHE A 208 24.983 0.750 11.887 1.00 13.45 C ANISOU 497 CG PHE A 208 1912 1633 1565 327 151 -53 ATOM 498 CD1 PHE A 208 24.361 0.991 13.129 1.00 24.23 C ANISOU 498 CD1 PHE A 208 3282 3023 2903 356 178 -31 ATOM 499 CD2 PHE A 208 25.827 -0.372 11.752 1.00 16.81 C ANISOU 499 CD2 PHE A 208 2356 2049 1984 329 130 -78 ATOM 500 CE1 PHE A 208 24.658 0.181 14.216 1.00 28.46 C ANISOU 500 CE1 PHE A 208 3840 3575 3399 391 189 -36 ATOM 501 CE2 PHE A 208 26.108 -1.169 12.849 1.00 19.99 C ANISOU 501 CE2 PHE A 208 2784 2462 2351 361 136 -87 ATOM 502 CZ PHE A 208 25.541 -0.883 14.082 1.00 21.74 C ANISOU 502 CZ PHE A 208 3011 2710 2540 395 167 -67 ATOM 503 H PHE A 208 24.343 -0.697 9.474 1.00 0.00 H ATOM 504 HA PHE A 208 22.498 1.153 10.741 1.00 0.00 H ATOM 505 HB3 PHE A 208 24.489 2.590 10.937 1.00 0.00 H ATOM 506 HB2 PHE A 208 25.410 1.495 9.941 1.00 0.00 H ATOM 507 HD1 PHE A 208 23.648 1.797 13.235 1.00 0.00 H ATOM 508 HD2 PHE A 208 26.255 -0.614 10.791 1.00 0.00 H ATOM 509 HE1 PHE A 208 24.186 0.361 15.166 1.00 0.00 H ATOM 510 HE2 PHE A 208 26.752 -2.026 12.735 1.00 0.00 H ATOM 511 HZ PHE A 208 25.764 -1.512 14.929 1.00 0.00 H ATOM 512 N GLN A 209 22.858 1.348 7.579 1.00 13.21 N ANISOU 512 N GLN A 209 1847 1562 1609 270 93 -32 ATOM 513 CA GLN A 209 22.461 2.024 6.341 1.00 13.12 C ANISOU 513 CA GLN A 209 1810 1542 1634 252 93 -21 ATOM 514 C GLN A 209 21.032 2.571 6.346 1.00 20.26 C ANISOU 514 C GLN A 209 2708 2451 2538 258 107 0 ATOM 515 O GLN A 209 20.819 3.660 5.816 1.00 16.92 O ANISOU 515 O GLN A 209 2262 2024 2141 248 122 9 ATOM 516 CB GLN A 209 22.682 1.106 5.116 1.00 19.52 C ANISOU 516 CB GLN A 209 2621 2339 2455 243 58 -22 ATOM 517 CG GLN A 209 24.158 0.901 4.717 1.00 23.79 C ANISOU 517 CG GLN A 209 3151 2874 3014 229 45 -32 ATOM 518 CD GLN A 209 24.919 2.167 4.304 1.00 25.11 C ANISOU 518 CD GLN A 209 3286 3046 3209 219 70 -32 ATOM 519 OE1 GLN A 209 26.131 2.229 4.476 1.00 18.06 O ANISOU 519 OE1 GLN A 209 2381 2155 2327 221 92 -27 ATOM 520 NE2 GLN A 209 24.236 3.177 3.756 1.00 25.04 N ANISOU 520 NE2 GLN A 209 3266 3036 3211 210 63 -36 ATOM 521 H GLN A 209 23.089 0.367 7.495 1.00 0.00 H ATOM 522 HA GLN A 209 23.098 2.896 6.240 1.00 0.00 H ATOM 523 HB3 GLN A 209 22.141 1.495 4.251 1.00 0.00 H ATOM 524 HB2 GLN A 209 22.231 0.133 5.312 1.00 0.00 H ATOM 525 HG3 GLN A 209 24.218 0.187 3.894 1.00 0.00 H ATOM 526 HG2 GLN A 209 24.691 0.448 5.550 1.00 0.00 H ATOM 527 HE22 GLN A 209 24.720 4.017 3.472 1.00 0.00 H ATOM 528 HE21 GLN A 209 23.239 3.106 3.614 1.00 0.00 H ATOM 529 N LYS A 210 20.098 1.818 6.944 1.00 16.26 N ANISOU 529 N LYS A 210 2224 1952 2001 276 98 10 ATOM 530 CA LYS A 210 18.695 2.194 7.070 1.00 16.01 C ANISOU 530 CA LYS A 210 2188 1926 1971 280 106 36 ATOM 531 C LYS A 210 18.188 1.817 8.465 1.00 18.83 C ANISOU 531 C LYS A 210 2562 2304 2287 308 123 51 ATOM 532 O LYS A 210 18.461 0.712 8.937 1.00 16.54 O ANISOU 532 O LYS A 210 2304 2022 1957 330 112 39 ATOM 533 CB LYS A 210 17.860 1.539 5.947 1.00 0.00 C ATOM 534 CG LYS A 210 18.103 2.177 4.563 1.00 0.00 C ATOM 535 CD LYS A 210 17.229 1.611 3.433 1.00 0.00 C ATOM 536 CE LYS A 210 17.584 0.161 3.058 1.00 0.00 C ATOM 537 NZ LYS A 210 16.801 -0.313 1.903 1.00 0.00 N1+ ATOM 538 H LYS A 210 20.359 0.942 7.377 1.00 0.00 H ATOM 539 HA LYS A 210 18.609 3.272 6.962 1.00 0.00 H ATOM 540 HB2 LYS A 210 18.052 0.465 5.923 1.00 0.00 H ATOM 541 HB3 LYS A 210 16.801 1.653 6.183 1.00 0.00 H ATOM 542 HG2 LYS A 210 17.929 3.251 4.635 1.00 0.00 H ATOM 543 HG3 LYS A 210 19.148 2.063 4.277 1.00 0.00 H ATOM 544 HD2 LYS A 210 16.181 1.673 3.728 1.00 0.00 H ATOM 545 HD3 LYS A 210 17.335 2.258 2.560 1.00 0.00 H ATOM 546 HE2 LYS A 210 18.643 0.084 2.810 1.00 0.00 H ATOM 547 HE3 LYS A 210 17.401 -0.510 3.898 1.00 0.00 H ATOM 548 HZ1 LYS A 210 16.989 0.274 1.102 1.00 0.00 H ATOM 549 HZ2 LYS A 210 17.062 -1.266 1.688 1.00 0.00 H ATOM 550 HZ3 LYS A 210 15.816 -0.277 2.123 1.00 0.00 H ATOM 551 N LEU A 211 17.436 2.746 9.079 1.00 17.82 N ANISOU 551 N LEU A 211 2413 2188 2171 307 149 80 ATOM 552 CA LEU A 211 16.718 2.587 10.348 1.00 21.01 C ANISOU 552 CA LEU A 211 2823 2620 2541 335 173 109 ATOM 553 C LEU A 211 15.710 1.417 10.277 1.00 18.46 C ANISOU 553 C LEU A 211 2534 2308 2170 364 159 112 ATOM 554 O LEU A 211 15.102 1.221 9.222 1.00 14.61 O ANISOU 554 O LEU A 211 2055 1805 1691 354 131 106 ATOM 555 CB LEU A 211 15.954 3.902 10.637 1.00 23.96 C ANISOU 555 CB LEU A 211 3162 2996 2946 323 193 150 ATOM 556 CG LEU A 211 16.824 5.042 11.211 1.00 21.27 C ANISOU 556 CG LEU A 211 2790 2648 2643 303 208 158 ATOM 557 CD1 LEU A 211 16.147 6.410 11.017 1.00 18.34 C ANISOU 557 CD1 LEU A 211 2389 2260 2319 281 205 189 ATOM 558 CD2 LEU A 211 17.219 4.812 12.681 1.00 16.62 C ANISOU 558 CD2 LEU A 211 2198 2089 2029 325 237 179 ATOM 559 H LEU A 211 17.305 3.641 8.621 1.00 0.00 H ATOM 560 HA LEU A 211 17.469 2.409 11.115 1.00 0.00 H ATOM 561 HB3 LEU A 211 15.141 3.719 11.340 1.00 0.00 H ATOM 562 HB2 LEU A 211 15.467 4.226 9.716 1.00 0.00 H ATOM 563 HG LEU A 211 17.745 5.079 10.638 1.00 0.00 H ATOM 564 HD11 LEU A 211 16.886 7.210 10.997 1.00 0.00 H ATOM 565 HD12 LEU A 211 15.596 6.462 10.078 1.00 0.00 H ATOM 566 HD13 LEU A 211 15.442 6.621 11.818 1.00 0.00 H ATOM 567 HD21 LEU A 211 17.192 5.733 13.260 1.00 0.00 H ATOM 568 HD22 LEU A 211 16.555 4.109 13.179 1.00 0.00 H ATOM 569 HD23 LEU A 211 18.232 4.418 12.756 1.00 0.00 H ATOM 570 N PRO A 212 15.530 0.673 11.396 1.00 19.25 N ANISOU 570 N PRO A 212 2658 2438 2219 403 175 122 ATOM 571 CA PRO A 212 14.530 -0.407 11.470 1.00 23.01 C ANISOU 571 CA PRO A 212 3172 2927 2644 438 160 126 ATOM 572 C PRO A 212 13.102 0.153 11.352 1.00 23.99 C ANISOU 572 C PRO A 212 3277 3062 2777 436 169 169 ATOM 573 O PRO A 212 12.836 1.220 11.901 1.00 19.75 O ANISOU 573 O PRO A 212 2701 2536 2268 424 199 207 ATOM 574 CB PRO A 212 14.801 -1.041 12.843 1.00 21.43 C ANISOU 574 CB PRO A 212 2998 2759 2386 487 183 128 ATOM 575 CG PRO A 212 15.351 0.085 13.698 1.00 19.96 C ANISOU 575 CG PRO A 212 2770 2585 2228 475 223 151 ATOM 576 CD PRO A 212 16.156 0.906 12.700 1.00 19.98 C ANISOU 576 CD PRO A 212 2741 2554 2297 422 209 133 ATOM 577 HA PRO A 212 14.702 -1.142 10.681 1.00 0.00 H ATOM 578 HB3 PRO A 212 15.559 -1.815 12.735 1.00 0.00 H ATOM 579 HB2 PRO A 212 13.926 -1.504 13.295 1.00 0.00 H ATOM 580 HG3 PRO A 212 15.940 -0.263 14.548 1.00 0.00 H ATOM 581 HG2 PRO A 212 14.526 0.685 14.085 1.00 0.00 H ATOM 582 HD2 PRO A 212 16.159 1.954 12.994 1.00 0.00 H ATOM 583 HD3 PRO A 212 17.184 0.558 12.658 1.00 0.00 H ATOM 584 N SER A 213 12.236 -0.542 10.596 1.00 18.34 N ANISOU 584 N SER A 213 2589 2340 2038 445 140 164 ATOM 585 CA SER A 213 10.861 -0.126 10.295 1.00 23.20 C ANISOU 585 CA SER A 213 3189 2962 2662 442 143 204 ATOM 586 C SER A 213 10.030 0.185 11.556 1.00 22.65 C ANISOU 586 C SER A 213 3108 2936 2564 474 185 254 ATOM 587 O SER A 213 10.111 -0.561 12.530 1.00 16.42 O ANISOU 587 O SER A 213 2346 2177 1716 520 202 255 ATOM 588 CB SER A 213 10.196 -1.229 9.447 1.00 32.20 C ANISOU 588 CB SER A 213 4370 4094 3771 457 102 189 ATOM 589 OG SER A 213 8.861 -0.909 9.102 1.00 34.88 O ANISOU 589 OG SER A 213 4711 4458 4082 480 113 231 ATOM 590 H SER A 213 12.540 -1.404 10.166 1.00 0.00 H ATOM 591 HA SER A 213 10.924 0.783 9.693 1.00 0.00 H ATOM 592 HB3 SER A 213 10.199 -2.176 9.987 1.00 0.00 H ATOM 593 HB2 SER A 213 10.758 -1.389 8.526 1.00 0.00 H ATOM 594 HG SER A 213 8.446 -1.698 8.737 1.00 0.00 H ATOM 595 N LYS A 214 9.228 1.262 11.493 1.00 16.17 N ANISOU 595 N LYS A 214 2245 2117 1784 453 200 300 ATOM 596 CA LYS A 214 8.286 1.672 12.543 1.00 25.80 C ANISOU 596 CA LYS A 214 3442 3377 2983 479 239 363 ATOM 597 C LYS A 214 7.184 0.633 12.820 1.00 26.11 C ANISOU 597 C LYS A 214 3517 3448 2955 526 238 382 ATOM 598 O LYS A 214 6.714 0.555 13.955 1.00 23.22 O ANISOU 598 O LYS A 214 3148 3129 2546 568 275 427 ATOM 599 CB LYS A 214 7.657 3.028 12.157 1.00 31.18 C ANISOU 599 CB LYS A 214 4070 4045 3733 439 245 409 ATOM 600 CG LYS A 214 8.631 4.214 12.247 1.00 41.03 C ANISOU 600 CG LYS A 214 5284 5260 5047 396 242 394 ATOM 601 CD LYS A 214 8.023 5.525 11.718 1.00 49.00 C ANISOU 601 CD LYS A 214 6253 6241 6123 357 229 427 ATOM 602 CE LYS A 214 8.933 6.755 11.893 1.00 51.94 C ANISOU 602 CE LYS A 214 6591 6590 6555 325 232 431 ATOM 603 NZ LYS A 214 9.026 7.194 13.298 1.00 50.84 N1+ ANISOU 603 NZ LYS A 214 6420 6483 6414 337 264 491 ATOM 604 H LYS A 214 9.219 1.820 10.652 1.00 0.00 H ATOM 605 HA LYS A 214 8.850 1.796 13.469 1.00 0.00 H ATOM 606 HB3 LYS A 214 6.818 3.244 12.821 1.00 0.00 H ATOM 607 HB2 LYS A 214 7.235 2.963 11.152 1.00 0.00 H ATOM 608 HG3 LYS A 214 9.544 3.992 11.693 1.00 0.00 H ATOM 609 HG2 LYS A 214 8.923 4.342 13.288 1.00 0.00 H ATOM 610 HD3 LYS A 214 7.056 5.703 12.192 1.00 0.00 H ATOM 611 HD2 LYS A 214 7.808 5.404 10.655 1.00 0.00 H ATOM 612 HE3 LYS A 214 8.535 7.588 11.311 1.00 0.00 H ATOM 613 HE2 LYS A 214 9.933 6.549 11.509 1.00 0.00 H ATOM 614 HZ1 LYS A 214 9.428 6.453 13.856 1.00 0.00 H ATOM 615 HZ2 LYS A 214 9.612 8.014 13.357 1.00 0.00 H ATOM 616 HZ3 LYS A 214 8.104 7.415 13.646 1.00 0.00 H ATOM 617 N VAL A 215 6.809 -0.142 11.788 1.00 17.04 N ANISOU 617 N VAL A 215 2402 2278 1796 522 198 352 ATOM 618 CA VAL A 215 5.795 -1.192 11.852 1.00 21.55 C ANISOU 618 CA VAL A 215 3015 2875 2299 569 189 365 ATOM 619 C VAL A 215 6.313 -2.454 12.574 1.00 24.20 C ANISOU 619 C VAL A 215 3406 3233 2556 626 190 332 ATOM 620 O VAL A 215 5.616 -2.958 13.455 1.00 26.11 O ANISOU 620 O VAL A 215 3666 3522 2732 683 220 363 ATOM 621 CB VAL A 215 5.289 -1.564 10.426 1.00 22.74 C ANISOU 621 CB VAL A 215 3183 2991 2465 545 139 342 ATOM 622 CG1 VAL A 215 4.381 -2.811 10.357 1.00 25.40 C ANISOU 622 CG1 VAL A 215 3571 3350 2728 593 121 348 ATOM 623 CG2 VAL A 215 4.574 -0.370 9.766 1.00 19.57 C ANISOU 623 CG2 VAL A 215 2728 2569 2137 497 140 377 ATOM 624 H VAL A 215 7.261 -0.020 10.892 1.00 0.00 H ATOM 625 HA VAL A 215 4.947 -0.808 12.423 1.00 0.00 H ATOM 626 HB VAL A 215 6.160 -1.777 9.806 1.00 0.00 H ATOM 627 HG11 VAL A 215 3.982 -2.950 9.352 1.00 0.00 H ATOM 628 HG12 VAL A 215 4.917 -3.728 10.605 1.00 0.00 H ATOM 629 HG13 VAL A 215 3.535 -2.720 11.039 1.00 0.00 H ATOM 630 HG21 VAL A 215 4.237 -0.620 8.759 1.00 0.00 H ATOM 631 HG22 VAL A 215 3.700 -0.067 10.342 1.00 0.00 H ATOM 632 HG23 VAL A 215 5.231 0.496 9.678 1.00 0.00 H ATOM 633 N GLN A 216 7.518 -2.927 12.205 1.00 20.99 N ANISOU 633 N GLN A 216 3026 2794 2154 614 160 272 ATOM 634 CA GLN A 216 8.145 -4.113 12.800 1.00 27.91 C ANISOU 634 CA GLN A 216 3962 3682 2959 668 150 236 ATOM 635 C GLN A 216 8.814 -3.845 14.160 1.00 34.49 C ANISOU 635 C GLN A 216 4780 4550 3773 699 202 251 ATOM 636 O GLN A 216 8.862 -4.759 14.982 1.00 33.57 O ANISOU 636 O GLN A 216 4708 4466 3581 765 214 245 ATOM 637 CB GLN A 216 9.168 -4.737 11.823 1.00 33.46 C ANISOU 637 CB GLN A 216 4696 4336 3682 642 94 172 ATOM 638 CG GLN A 216 8.557 -5.468 10.608 1.00 48.18 C ANISOU 638 CG GLN A 216 6594 6170 5544 632 34 152 ATOM 639 CD GLN A 216 8.591 -4.637 9.323 1.00 60.27 C ANISOU 639 CD GLN A 216 8077 7664 7158 563 16 154 ATOM 640 OE1 GLN A 216 7.829 -3.687 9.171 1.00 68.29 O ANISOU 640 OE1 GLN A 216 9052 8687 8208 541 37 193 ATOM 641 NE2 GLN A 216 9.472 -4.994 8.386 1.00 59.88 N ANISOU 641 NE2 GLN A 216 8033 7576 7144 532 -23 115 ATOM 642 H GLN A 216 8.032 -2.466 11.468 1.00 0.00 H ATOM 643 HA GLN A 216 7.366 -4.857 12.981 1.00 0.00 H ATOM 644 HB3 GLN A 216 9.752 -5.480 12.371 1.00 0.00 H ATOM 645 HB2 GLN A 216 9.897 -3.990 11.506 1.00 0.00 H ATOM 646 HG3 GLN A 216 7.532 -5.777 10.812 1.00 0.00 H ATOM 647 HG2 GLN A 216 9.114 -6.391 10.434 1.00 0.00 H ATOM 648 HE22 GLN A 216 9.522 -4.484 7.516 1.00 0.00 H ATOM 649 HE21 GLN A 216 10.084 -5.784 8.532 1.00 0.00 H ATOM 650 N TYR A 217 9.331 -2.621 14.361 1.00 31.23 N ANISOU 650 N TYR A 217 4309 4133 3426 655 231 270 ATOM 651 CA TYR A 217 10.134 -2.226 15.520 1.00 29.93 C ANISOU 651 CA TYR A 217 4125 3993 3253 675 273 282 ATOM 652 C TYR A 217 9.674 -0.864 16.085 1.00 33.36 C ANISOU 652 C TYR A 217 4492 4455 3729 658 321 353 ATOM 653 O TYR A 217 10.461 0.084 16.064 1.00 31.65 O ANISOU 653 O TYR A 217 4232 4223 3572 617 332 358 ATOM 654 CB TYR A 217 11.637 -2.227 15.144 1.00 30.25 C ANISOU 654 CB TYR A 217 4166 3995 3333 639 251 229 ATOM 655 CG TYR A 217 12.163 -3.560 14.643 1.00 26.30 C ANISOU 655 CG TYR A 217 3730 3469 2792 659 202 167 ATOM 656 CD1 TYR A 217 12.446 -4.593 15.561 1.00 22.69 C ANISOU 656 CD1 TYR A 217 3323 3031 2267 721 206 145 ATOM 657 CD2 TYR A 217 12.332 -3.786 13.260 1.00 16.76 C ANISOU 657 CD2 TYR A 217 2536 2217 1616 620 148 134 ATOM 658 CE1 TYR A 217 12.874 -5.852 15.098 1.00 24.33 C ANISOU 658 CE1 TYR A 217 3595 3209 2441 739 151 89 ATOM 659 CE2 TYR A 217 12.765 -5.043 12.797 1.00 23.61 C ANISOU 659 CE2 TYR A 217 3461 3057 2453 635 95 84 ATOM 660 CZ TYR A 217 13.027 -6.080 13.715 1.00 22.67 C ANISOU 660 CZ TYR A 217 3393 2952 2268 694 93 60 ATOM 661 OH TYR A 217 13.428 -7.304 13.264 1.00 25.57 O ANISOU 661 OH TYR A 217 3820 3285 2610 708 31 10 ATOM 662 H TYR A 217 9.257 -1.925 13.629 1.00 0.00 H ATOM 663 HA TYR A 217 10.006 -2.950 16.326 1.00 0.00 H ATOM 664 HB3 TYR A 217 12.236 -1.941 16.011 1.00 0.00 H ATOM 665 HB2 TYR A 217 11.832 -1.469 14.384 1.00 0.00 H ATOM 666 HD1 TYR A 217 12.314 -4.427 16.621 1.00 0.00 H ATOM 667 HD2 TYR A 217 12.109 -3.002 12.550 1.00 0.00 H ATOM 668 HE1 TYR A 217 13.076 -6.641 15.808 1.00 0.00 H ATOM 669 HE2 TYR A 217 12.883 -5.216 11.737 1.00 0.00 H ATOM 670 HH TYR A 217 13.535 -7.948 13.968 1.00 0.00 H ATOM 671 N PRO A 218 8.424 -0.769 16.601 1.00 31.62 N ANISOU 671 N PRO A 218 4260 4275 3478 690 347 413 ATOM 672 CA PRO A 218 7.952 0.447 17.296 1.00 29.90 C ANISOU 672 CA PRO A 218 3973 4084 3304 674 390 491 ATOM 673 C PRO A 218 8.661 0.722 18.640 1.00 29.49 C ANISOU 673 C PRO A 218 3897 4060 3246 696 431 512 ATOM 674 O PRO A 218 8.697 1.875 19.069 1.00 28.26 O ANISOU 674 O PRO A 218 3680 3902 3154 658 449 556 ATOM 675 CB PRO A 218 6.450 0.189 17.490 1.00 28.52 C ANISOU 675 CB PRO A 218 3801 3954 3080 717 410 550 ATOM 676 CG PRO A 218 6.342 -1.323 17.610 1.00 32.52 C ANISOU 676 CG PRO A 218 4385 4477 3494 782 396 504 ATOM 677 CD PRO A 218 7.405 -1.822 16.638 1.00 28.07 C ANISOU 677 CD PRO A 218 3861 3854 2950 748 341 417 ATOM 678 HA PRO A 218 8.089 1.322 16.656 1.00 0.00 H ATOM 679 HB3 PRO A 218 5.908 0.527 16.606 1.00 0.00 H ATOM 680 HB2 PRO A 218 6.021 0.706 18.350 1.00 0.00 H ATOM 681 HG3 PRO A 218 5.345 -1.706 17.392 1.00 0.00 H ATOM 682 HG2 PRO A 218 6.603 -1.628 18.625 1.00 0.00 H ATOM 683 HD2 PRO A 218 7.792 -2.794 16.947 1.00 0.00 H ATOM 684 HD3 PRO A 218 6.975 -1.922 15.641 1.00 0.00 H ATOM 685 N ASP A 219 9.233 -0.333 19.251 1.00 26.83 N ANISOU 685 N ASP A 219 3608 3749 2836 757 443 481 ATOM 686 CA ASP A 219 10.047 -0.303 20.469 1.00 27.50 C ANISOU 686 CA ASP A 219 3672 3865 2914 784 484 502 ATOM 687 C ASP A 219 11.348 0.508 20.313 1.00 29.89 C ANISOU 687 C ASP A 219 3941 4122 3293 719 470 474 ATOM 688 O ASP A 219 11.779 1.114 21.293 1.00 32.53 O ANISOU 688 O ASP A 219 4223 4473 3665 708 501 521 ATOM 689 CB ASP A 219 10.360 -1.715 21.044 1.00 38.18 C ANISOU 689 CB ASP A 219 5091 5243 4173 864 491 461 ATOM 690 CG ASP A 219 11.074 -2.748 20.143 1.00 49.30 C ANISOU 690 CG ASP A 219 6571 6602 5558 858 429 371 ATOM 691 OD1 ASP A 219 11.052 -2.616 18.898 1.00 43.60 O ANISOU 691 OD1 ASP A 219 5870 5857 4839 838 392 356 ATOM 692 OD2 ASP A 219 11.578 -3.733 20.725 1.00 50.53 O1- ANISOU 692 OD2 ASP A 219 6762 6743 5696 875 416 318 ATOM 693 H ASP A 219 9.171 -1.242 18.811 1.00 0.00 H ATOM 694 HA ASP A 219 9.446 0.215 21.219 1.00 0.00 H ATOM 695 HB3 ASP A 219 9.412 -2.173 21.326 1.00 0.00 H ATOM 696 HB2 ASP A 219 10.914 -1.608 21.980 1.00 0.00 H ATOM 697 N TYR A 220 11.925 0.539 19.094 1.00 29.48 N ANISOU 697 N TYR A 220 3917 4016 3269 676 421 404 ATOM 698 CA TYR A 220 13.085 1.366 18.756 1.00 24.52 C ANISOU 698 CA TYR A 220 3259 3347 2712 617 406 378 ATOM 699 C TYR A 220 12.781 2.864 18.920 1.00 24.68 C ANISOU 699 C TYR A 220 3211 3361 2805 569 418 438 ATOM 700 O TYR A 220 13.559 3.563 19.560 1.00 24.75 O ANISOU 700 O TYR A 220 3180 3368 2854 548 434 457 ATOM 701 CB TYR A 220 13.604 1.024 17.338 1.00 19.04 C ANISOU 701 CB TYR A 220 2597 2600 2039 578 354 308 ATOM 702 CG TYR A 220 14.858 1.781 16.920 1.00 22.70 C ANISOU 702 CG TYR A 220 3038 3026 2561 528 341 276 ATOM 703 CD1 TYR A 220 14.762 3.055 16.318 1.00 22.63 C ANISOU 703 CD1 TYR A 220 2983 2991 2625 473 335 294 ATOM 704 CD2 TYR A 220 16.130 1.223 17.159 1.00 25.77 C ANISOU 704 CD2 TYR A 220 3456 3407 2931 540 333 228 ATOM 705 CE1 TYR A 220 15.927 3.780 16.002 1.00 31.27 C ANISOU 705 CE1 TYR A 220 4061 4053 3765 434 322 264 ATOM 706 CE2 TYR A 220 17.297 1.941 16.831 1.00 25.70 C ANISOU 706 CE2 TYR A 220 3426 3367 2972 497 322 202 ATOM 707 CZ TYR A 220 17.195 3.226 16.261 1.00 27.90 C ANISOU 707 CZ TYR A 220 3661 3624 3317 446 319 219 ATOM 708 OH TYR A 220 18.317 3.942 15.963 1.00 17.94 O ANISOU 708 OH TYR A 220 2384 2334 2099 409 308 192 ATOM 709 H TYR A 220 11.523 -0.004 18.343 1.00 0.00 H ATOM 710 HA TYR A 220 13.875 1.123 19.467 1.00 0.00 H ATOM 711 HB3 TYR A 220 12.828 1.215 16.597 1.00 0.00 H ATOM 712 HB2 TYR A 220 13.815 -0.045 17.278 1.00 0.00 H ATOM 713 HD1 TYR A 220 13.794 3.494 16.123 1.00 0.00 H ATOM 714 HD2 TYR A 220 16.213 0.245 17.605 1.00 0.00 H ATOM 715 HE1 TYR A 220 15.844 4.765 15.566 1.00 0.00 H ATOM 716 HE2 TYR A 220 18.263 1.505 17.035 1.00 0.00 H ATOM 717 HH TYR A 220 19.129 3.441 16.083 1.00 0.00 H ATOM 718 N TYR A 221 11.644 3.311 18.367 1.00 24.48 N ANISOU 718 N TYR A 221 3171 3330 2800 551 408 468 ATOM 719 CA TYR A 221 11.197 4.707 18.386 1.00 26.26 C ANISOU 719 CA TYR A 221 3336 3541 3100 504 408 523 ATOM 720 C TYR A 221 10.619 5.157 19.736 1.00 32.74 C ANISOU 720 C TYR A 221 4110 4412 3919 529 452 612 ATOM 721 O TYR A 221 10.617 6.358 20.004 1.00 36.70 O ANISOU 721 O TYR A 221 4556 4900 4488 490 452 661 ATOM 722 CB TYR A 221 10.188 4.919 17.245 1.00 26.08 C ANISOU 722 CB TYR A 221 3315 3491 3103 476 378 523 ATOM 723 CG TYR A 221 10.805 4.677 15.882 1.00 21.67 C ANISOU 723 CG TYR A 221 2792 2885 2558 447 336 444 ATOM 724 CD1 TYR A 221 11.511 5.713 15.240 1.00 21.19 C ANISOU 724 CD1 TYR A 221 2709 2778 2563 396 313 420 ATOM 725 CD2 TYR A 221 10.732 3.403 15.286 1.00 22.07 C ANISOU 725 CD2 TYR A 221 2897 2936 2553 474 318 395 ATOM 726 CE1 TYR A 221 12.140 5.479 14.003 1.00 17.21 C ANISOU 726 CE1 TYR A 221 2232 2237 2070 375 280 355 ATOM 727 CE2 TYR A 221 11.375 3.162 14.059 1.00 19.52 C ANISOU 727 CE2 TYR A 221 2598 2570 2247 447 280 332 ATOM 728 CZ TYR A 221 12.073 4.203 13.412 1.00 17.73 C ANISOU 728 CZ TYR A 221 2344 2306 2087 398 266 315 ATOM 729 OH TYR A 221 12.677 3.986 12.211 1.00 15.21 O ANISOU 729 OH TYR A 221 2043 1952 1785 375 234 261 ATOM 730 H TYR A 221 11.044 2.661 17.880 1.00 0.00 H ATOM 731 HA TYR A 221 12.066 5.340 18.190 1.00 0.00 H ATOM 732 HB3 TYR A 221 9.802 5.940 17.269 1.00 0.00 H ATOM 733 HB2 TYR A 221 9.325 4.264 17.375 1.00 0.00 H ATOM 734 HD1 TYR A 221 11.574 6.686 15.706 1.00 0.00 H ATOM 735 HD2 TYR A 221 10.194 2.606 15.776 1.00 0.00 H ATOM 736 HE1 TYR A 221 12.679 6.274 13.510 1.00 0.00 H ATOM 737 HE2 TYR A 221 11.311 2.179 13.619 1.00 0.00 H ATOM 738 HH TYR A 221 12.673 3.055 11.960 1.00 0.00 H ATOM 739 N ALA A 222 10.177 4.199 20.570 1.00 21.98 N ANISOU 739 N ALA A 222 2768 3104 2478 597 488 637 ATOM 740 CA ALA A 222 9.773 4.437 21.956 1.00 37.32 C ANISOU 740 CA ALA A 222 4663 5103 4413 631 538 724 ATOM 741 C ALA A 222 10.966 4.743 22.881 1.00 37.12 C ANISOU 741 C ALA A 222 4610 5075 4419 619 552 726 ATOM 742 O ALA A 222 10.786 5.458 23.866 1.00 32.89 O ANISOU 742 O ALA A 222 4010 4557 3929 606 575 804 ATOM 743 CB ALA A 222 8.997 3.212 22.462 1.00 32.64 C ANISOU 743 CB ALA A 222 4110 4574 3720 718 575 739 ATOM 744 H ALA A 222 10.180 3.235 20.266 1.00 0.00 H ATOM 745 HA ALA A 222 9.102 5.299 21.975 1.00 0.00 H ATOM 746 HB1 ALA A 222 8.616 3.376 23.471 1.00 0.00 H ATOM 747 HB2 ALA A 222 8.142 2.996 21.821 1.00 0.00 H ATOM 748 HB3 ALA A 222 9.626 2.321 22.488 1.00 0.00 H ATOM 749 N ILE A 223 12.150 4.205 22.541 1.00 36.85 N ANISOU 749 N ILE A 223 4620 5017 4366 620 536 644 ATOM 750 CA ILE A 223 13.392 4.344 23.302 1.00 33.81 C ANISOU 750 CA ILE A 223 4216 4633 3998 619 551 640 ATOM 751 C ILE A 223 14.286 5.476 22.748 1.00 35.37 C ANISOU 751 C ILE A 223 4388 4771 4279 543 514 613 ATOM 752 O ILE A 223 14.890 6.197 23.543 1.00 32.39 O ANISOU 752 O ILE A 223 3964 4394 3949 522 524 652 ATOM 753 CB ILE A 223 14.166 2.984 23.319 1.00 32.99 C ANISOU 753 CB ILE A 223 4176 4540 3820 672 556 571 ATOM 754 CG1 ILE A 223 13.396 1.945 24.172 1.00 39.90 C ANISOU 754 CG1 ILE A 223 5074 5479 4605 760 598 605 ATOM 755 CG2 ILE A 223 15.636 3.059 23.789 1.00 26.73 C ANISOU 755 CG2 ILE A 223 3367 3740 3050 662 563 556 ATOM 756 CD1 ILE A 223 13.809 0.485 23.932 1.00 42.43 C ANISOU 756 CD1 ILE A 223 5476 5798 4846 813 583 526 ATOM 757 H ILE A 223 12.204 3.626 21.714 1.00 0.00 H ATOM 758 HA ILE A 223 13.153 4.601 24.336 1.00 0.00 H ATOM 759 HB ILE A 223 14.184 2.609 22.293 1.00 0.00 H ATOM 760 HG13 ILE A 223 12.326 2.015 23.977 1.00 0.00 H ATOM 761 HG12 ILE A 223 13.513 2.184 25.230 1.00 0.00 H ATOM 762 HG21 ILE A 223 16.100 2.073 23.817 1.00 0.00 H ATOM 763 HG22 ILE A 223 16.249 3.655 23.118 1.00 0.00 H ATOM 764 HG23 ILE A 223 15.711 3.489 24.788 1.00 0.00 H ATOM 765 HD11 ILE A 223 13.097 -0.195 24.400 1.00 0.00 H ATOM 766 HD12 ILE A 223 13.829 0.248 22.869 1.00 0.00 H ATOM 767 HD13 ILE A 223 14.791 0.265 24.349 1.00 0.00 H ATOM 768 N ILE A 224 14.352 5.615 21.413 1.00 29.66 N ANISOU 768 N ILE A 224 3695 3998 3576 505 470 549 ATOM 769 CA ILE A 224 15.239 6.543 20.711 1.00 28.25 C ANISOU 769 CA ILE A 224 3508 3766 3462 445 434 508 ATOM 770 C ILE A 224 14.463 7.795 20.262 1.00 30.33 C ANISOU 770 C ILE A 224 3728 3998 3797 395 411 550 ATOM 771 O ILE A 224 13.577 7.698 19.412 1.00 21.97 O ANISOU 771 O ILE A 224 2682 2921 2745 382 390 541 ATOM 772 CB ILE A 224 15.899 5.856 19.475 1.00 24.24 C ANISOU 772 CB ILE A 224 3054 3223 2934 437 401 419 ATOM 773 CG1 ILE A 224 16.742 4.621 19.885 1.00 15.95 C ANISOU 773 CG1 ILE A 224 2047 2194 1819 483 414 377 ATOM 774 CG2 ILE A 224 16.726 6.810 18.589 1.00 26.27 C ANISOU 774 CG2 ILE A 224 3300 3428 3252 381 368 381 ATOM 775 CD1 ILE A 224 17.838 4.903 20.921 1.00 22.04 C ANISOU 775 CD1 ILE A 224 2796 2985 2594 496 442 396 ATOM 776 H ILE A 224 13.822 4.987 20.821 1.00 0.00 H ATOM 777 HA ILE A 224 16.033 6.874 21.381 1.00 0.00 H ATOM 778 HB ILE A 224 15.103 5.479 18.832 1.00 0.00 H ATOM 779 HG13 ILE A 224 17.192 4.171 19.000 1.00 0.00 H ATOM 780 HG12 ILE A 224 16.089 3.849 20.291 1.00 0.00 H ATOM 781 HG21 ILE A 224 17.254 6.266 17.806 1.00 0.00 H ATOM 782 HG22 ILE A 224 16.093 7.539 18.087 1.00 0.00 H ATOM 783 HG23 ILE A 224 17.459 7.362 19.175 1.00 0.00 H ATOM 784 HD11 ILE A 224 18.468 4.025 21.056 1.00 0.00 H ATOM 785 HD12 ILE A 224 18.469 5.735 20.618 1.00 0.00 H ATOM 786 HD13 ILE A 224 17.424 5.148 21.898 1.00 0.00 H ATOM 787 N LYS A 225 14.836 8.945 20.850 1.00 30.77 N ANISOU 787 N LYS A 225 3735 4046 3911 366 411 596 ATOM 788 CA LYS A 225 14.240 10.259 20.593 1.00 37.78 C ANISOU 788 CA LYS A 225 4583 4900 4874 319 381 641 ATOM 789 C LYS A 225 14.724 10.935 19.297 1.00 35.09 C ANISOU 789 C LYS A 225 4265 4496 4572 276 332 575 ATOM 790 O LYS A 225 13.993 11.778 18.777 1.00 27.78 O ANISOU 790 O LYS A 225 3330 3541 3686 250 304 591 ATOM 791 CB LYS A 225 14.507 11.188 21.796 1.00 0.00 C ATOM 792 CG LYS A 225 13.709 10.814 23.056 1.00 0.00 C ATOM 793 CD LYS A 225 13.895 11.842 24.182 1.00 0.00 C ATOM 794 CE LYS A 225 13.017 11.544 25.408 1.00 0.00 C ATOM 795 NZ LYS A 225 13.201 12.551 26.469 1.00 0.00 N1+ ATOM 796 H LYS A 225 15.569 8.924 21.545 1.00 0.00 H ATOM 797 HA LYS A 225 13.161 10.127 20.498 1.00 0.00 H ATOM 798 HB2 LYS A 225 15.574 11.222 22.019 1.00 0.00 H ATOM 799 HB3 LYS A 225 14.226 12.208 21.525 1.00 0.00 H ATOM 800 HG2 LYS A 225 12.650 10.742 22.803 1.00 0.00 H ATOM 801 HG3 LYS A 225 14.009 9.825 23.406 1.00 0.00 H ATOM 802 HD2 LYS A 225 14.946 11.860 24.475 1.00 0.00 H ATOM 803 HD3 LYS A 225 13.667 12.839 23.799 1.00 0.00 H ATOM 804 HE2 LYS A 225 11.965 11.529 25.122 1.00 0.00 H ATOM 805 HE3 LYS A 225 13.254 10.559 25.813 1.00 0.00 H ATOM 806 HZ1 LYS A 225 12.959 13.465 26.114 1.00 0.00 H ATOM 807 HZ2 LYS A 225 12.605 12.327 27.253 1.00 0.00 H ATOM 808 HZ3 LYS A 225 14.165 12.552 26.771 1.00 0.00 H ATOM 809 N GLU A 226 15.918 10.568 18.797 1.00 30.38 N ANISOU 809 N GLU A 226 3700 3880 3964 270 322 503 ATOM 810 CA GLU A 226 16.521 11.139 17.586 1.00 28.08 C ANISOU 810 CA GLU A 226 3430 3535 3704 237 280 443 ATOM 811 C GLU A 226 17.049 10.027 16.653 1.00 27.73 C ANISOU 811 C GLU A 226 3434 3492 3609 255 282 370 ATOM 812 O GLU A 226 18.265 9.840 16.591 1.00 26.53 O ANISOU 812 O GLU A 226 3298 3334 3447 254 280 324 ATOM 813 CB GLU A 226 17.632 12.146 17.970 1.00 33.51 C ANISOU 813 CB GLU A 226 4101 4192 4440 206 259 434 ATOM 814 CG GLU A 226 17.143 13.385 18.748 1.00 45.62 C ANISOU 814 CG GLU A 226 5588 5707 6039 177 240 504 ATOM 815 CD GLU A 226 18.284 14.372 19.023 1.00 55.06 C ANISOU 815 CD GLU A 226 6774 6866 7281 147 210 489 ATOM 816 OE1 GLU A 226 18.720 14.434 20.194 1.00 61.42 O ANISOU 816 OE1 GLU A 226 7548 7689 8098 146 224 532 ATOM 817 OE2 GLU A 226 18.705 15.050 18.058 1.00 55.54 O1- ANISOU 817 OE2 GLU A 226 6860 6881 7363 127 172 436 ATOM 818 H GLU A 226 16.461 9.862 19.274 1.00 0.00 H ATOM 819 HA GLU A 226 15.777 11.694 17.012 1.00 0.00 H ATOM 820 HB3 GLU A 226 18.147 12.472 17.064 1.00 0.00 H ATOM 821 HB2 GLU A 226 18.383 11.634 18.574 1.00 0.00 H ATOM 822 HG3 GLU A 226 16.686 13.084 19.692 1.00 0.00 H ATOM 823 HG2 GLU A 226 16.363 13.895 18.181 1.00 0.00 H ATOM 824 N PRO A 227 16.148 9.302 15.942 1.00 25.41 N ANISOU 824 N PRO A 227 3161 3206 3286 271 281 361 ATOM 825 CA PRO A 227 16.537 8.282 14.943 1.00 24.33 C ANISOU 825 CA PRO A 227 3068 3067 3109 284 273 298 ATOM 826 C PRO A 227 17.374 8.852 13.783 1.00 14.36 C ANISOU 826 C PRO A 227 1813 1762 1879 254 244 247 ATOM 827 O PRO A 227 17.004 9.884 13.220 1.00 18.91 O ANISOU 827 O PRO A 227 2376 2307 2501 230 222 254 ATOM 828 CB PRO A 227 15.191 7.729 14.432 1.00 14.91 C ANISOU 828 CB PRO A 227 1888 1884 1891 300 271 311 ATOM 829 CG PRO A 227 14.173 8.099 15.489 1.00 29.96 C ANISOU 829 CG PRO A 227 3764 3820 3799 312 294 383 ATOM 830 CD PRO A 227 14.692 9.424 16.011 1.00 31.39 C ANISOU 830 CD PRO A 227 3904 3980 4042 280 287 415 ATOM 831 HA PRO A 227 17.084 7.493 15.464 1.00 0.00 H ATOM 832 HB3 PRO A 227 15.215 6.653 14.255 1.00 0.00 H ATOM 833 HB2 PRO A 227 14.901 8.206 13.494 1.00 0.00 H ATOM 834 HG3 PRO A 227 14.186 7.357 16.290 1.00 0.00 H ATOM 835 HG2 PRO A 227 13.158 8.172 15.102 1.00 0.00 H ATOM 836 HD2 PRO A 227 14.376 10.248 15.369 1.00 0.00 H ATOM 837 HD3 PRO A 227 14.292 9.592 17.006 1.00 0.00 H ATOM 838 N ILE A 228 18.478 8.167 13.452 1.00 19.57 N ANISOU 838 N ILE A 228 2498 2422 2516 260 242 198 ATOM 839 CA ILE A 228 19.378 8.544 12.362 1.00 17.53 C ANISOU 839 CA ILE A 228 2249 2132 2279 240 219 152 ATOM 840 C ILE A 228 20.118 7.305 11.821 1.00 21.97 C ANISOU 840 C ILE A 228 2841 2702 2803 254 217 111 ATOM 841 O ILE A 228 20.419 6.390 12.589 1.00 20.98 O ANISOU 841 O ILE A 228 2731 2602 2640 277 230 111 ATOM 842 CB ILE A 228 20.395 9.638 12.809 1.00 13.65 C ANISOU 842 CB ILE A 228 1742 1622 1822 220 214 145 ATOM 843 CG1 ILE A 228 21.232 10.190 11.632 1.00 15.06 C ANISOU 843 CG1 ILE A 228 1929 1769 2024 205 190 105 ATOM 844 CG2 ILE A 228 21.304 9.200 13.978 1.00 15.42 C ANISOU 844 CG2 ILE A 228 1970 1868 2022 231 233 136 ATOM 845 CD1 ILE A 228 21.764 11.603 11.880 1.00 14.30 C ANISOU 845 CD1 ILE A 228 1823 1650 1960 188 178 98 ATOM 846 H ILE A 228 18.721 7.320 13.947 1.00 0.00 H ATOM 847 HA ILE A 228 18.771 8.940 11.543 1.00 0.00 H ATOM 848 HB ILE A 228 19.798 10.473 13.181 1.00 0.00 H ATOM 849 HG13 ILE A 228 20.619 10.226 10.732 1.00 0.00 H ATOM 850 HG12 ILE A 228 22.061 9.518 11.405 1.00 0.00 H ATOM 851 HG21 ILE A 228 21.957 10.007 14.307 1.00 0.00 H ATOM 852 HG22 ILE A 228 20.718 8.892 14.843 1.00 0.00 H ATOM 853 HG23 ILE A 228 21.938 8.364 13.696 1.00 0.00 H ATOM 854 HD11 ILE A 228 22.325 11.961 11.016 1.00 0.00 H ATOM 855 HD12 ILE A 228 20.948 12.304 12.058 1.00 0.00 H ATOM 856 HD13 ILE A 228 22.422 11.636 12.746 1.00 0.00 H ATOM 857 N ASP A 229 20.388 7.321 10.506 1.00 16.34 N ANISOU 857 N ASP A 229 2137 1970 2102 244 197 79 ATOM 858 CA ASP A 229 21.052 6.264 9.735 1.00 18.19 C ANISOU 858 CA ASP A 229 2393 2207 2311 251 187 47 ATOM 859 C ASP A 229 22.171 6.866 8.864 1.00 12.98 C ANISOU 859 C ASP A 229 1728 1528 1676 235 176 19 ATOM 860 O ASP A 229 22.225 8.086 8.688 1.00 19.15 O ANISOU 860 O ASP A 229 2494 2293 2487 223 174 19 ATOM 861 CB ASP A 229 20.052 5.406 8.899 1.00 25.25 C ANISOU 861 CB ASP A 229 3303 3104 3185 262 174 51 ATOM 862 CG ASP A 229 18.923 6.149 8.150 1.00 23.91 C ANISOU 862 CG ASP A 229 3121 2918 3045 251 164 64 ATOM 863 OD1 ASP A 229 19.164 7.280 7.684 1.00 16.40 O ANISOU 863 OD1 ASP A 229 2153 1948 2128 236 161 58 ATOM 864 OD2 ASP A 229 17.867 5.528 7.911 1.00 22.92 O1- ANISOU 864 OD2 ASP A 229 3004 2798 2906 260 156 78 ATOM 865 H ASP A 229 20.106 8.122 9.958 1.00 0.00 H ATOM 866 HA ASP A 229 21.561 5.597 10.426 1.00 0.00 H ATOM 867 HB3 ASP A 229 19.620 4.650 9.554 1.00 0.00 H ATOM 868 HB2 ASP A 229 20.598 4.834 8.151 1.00 0.00 H ATOM 869 N LEU A 230 23.038 5.994 8.317 1.00 12.87 N ANISOU 869 N LEU A 230 1726 1515 1647 237 165 -4 ATOM 870 CA LEU A 230 24.107 6.373 7.385 1.00 13.75 C ANISOU 870 CA LEU A 230 1828 1616 1778 226 159 -24 ATOM 871 C LEU A 230 23.586 6.910 6.036 1.00 12.72 C ANISOU 871 C LEU A 230 1688 1474 1672 223 150 -22 ATOM 872 O LEU A 230 24.322 7.646 5.383 1.00 20.77 O ANISOU 872 O LEU A 230 2698 2486 2708 220 152 -34 ATOM 873 CB LEU A 230 25.083 5.197 7.157 1.00 17.33 C ANISOU 873 CB LEU A 230 2292 2075 2218 226 147 -41 ATOM 874 CG LEU A 230 25.943 4.799 8.375 1.00 18.14 C ANISOU 874 CG LEU A 230 2407 2187 2300 232 154 -49 ATOM 875 CD1 LEU A 230 26.690 3.482 8.100 1.00 12.58 C ANISOU 875 CD1 LEU A 230 1715 1480 1583 232 131 -62 ATOM 876 CD2 LEU A 230 26.916 5.917 8.804 1.00 12.43 C ANISOU 876 CD2 LEU A 230 1669 1463 1592 223 169 -55 ATOM 877 H LEU A 230 22.941 5.004 8.511 1.00 0.00 H ATOM 878 HA LEU A 230 24.657 7.188 7.852 1.00 0.00 H ATOM 879 HB3 LEU A 230 25.761 5.434 6.334 1.00 0.00 H ATOM 880 HB2 LEU A 230 24.517 4.335 6.820 1.00 0.00 H ATOM 881 HG LEU A 230 25.265 4.604 9.208 1.00 0.00 H ATOM 882 HD11 LEU A 230 27.006 3.009 9.030 1.00 0.00 H ATOM 883 HD12 LEU A 230 26.066 2.765 7.565 1.00 0.00 H ATOM 884 HD13 LEU A 230 27.581 3.649 7.495 1.00 0.00 H ATOM 885 HD21 LEU A 230 27.948 5.574 8.829 1.00 0.00 H ATOM 886 HD22 LEU A 230 26.890 6.775 8.131 1.00 0.00 H ATOM 887 HD23 LEU A 230 26.681 6.280 9.804 1.00 0.00 H ATOM 888 N LYS A 231 22.335 6.581 5.665 1.00 15.06 N ANISOU 888 N LYS A 231 1988 1770 1966 227 141 -8 ATOM 889 CA LYS A 231 21.600 7.175 4.544 1.00 19.15 C ANISOU 889 CA LYS A 231 2495 2276 2506 227 134 -4 ATOM 890 C LYS A 231 21.336 8.681 4.742 1.00 19.20 C ANISOU 890 C LYS A 231 2493 2266 2536 226 139 -1 ATOM 891 O LYS A 231 21.619 9.455 3.832 1.00 16.55 O ANISOU 891 O LYS A 231 2151 1918 2218 231 136 -11 ATOM 892 CB LYS A 231 20.314 6.352 4.291 1.00 22.25 C ANISOU 892 CB LYS A 231 2893 2669 2892 231 120 12 ATOM 893 CG LYS A 231 19.219 7.022 3.439 1.00 31.50 C ANISOU 893 CG LYS A 231 4053 3827 4087 232 116 24 ATOM 894 CD LYS A 231 17.970 6.135 3.306 1.00 28.60 C ANISOU 894 CD LYS A 231 3694 3462 3710 235 106 46 ATOM 895 CE LYS A 231 16.750 6.859 2.710 1.00 40.16 C ANISOU 895 CE LYS A 231 5147 4911 5201 236 103 61 ATOM 896 NZ LYS A 231 16.197 7.877 3.626 1.00 43.99 N1+ ANISOU 896 NZ LYS A 231 5626 5386 5700 232 112 69 ATOM 897 H LYS A 231 21.801 5.953 6.250 1.00 0.00 H ATOM 898 HA LYS A 231 22.230 7.072 3.658 1.00 0.00 H ATOM 899 HB3 LYS A 231 19.863 6.115 5.254 1.00 0.00 H ATOM 900 HB2 LYS A 231 20.587 5.394 3.846 1.00 0.00 H ATOM 901 HG3 LYS A 231 19.611 7.266 2.451 1.00 0.00 H ATOM 902 HG2 LYS A 231 18.927 7.967 3.896 1.00 0.00 H ATOM 903 HD3 LYS A 231 17.710 5.711 4.278 1.00 0.00 H ATOM 904 HD2 LYS A 231 18.214 5.281 2.672 1.00 0.00 H ATOM 905 HE3 LYS A 231 15.963 6.133 2.503 1.00 0.00 H ATOM 906 HE2 LYS A 231 17.008 7.328 1.760 1.00 0.00 H ATOM 907 HZ1 LYS A 231 16.897 8.589 3.790 1.00 0.00 H ATOM 908 HZ2 LYS A 231 15.382 8.302 3.208 1.00 0.00 H ATOM 909 HZ3 LYS A 231 15.944 7.445 4.504 1.00 0.00 H ATOM 910 N THR A 232 20.814 9.069 5.919 1.00 13.05 N ANISOU 910 N THR A 232 1715 1488 1757 222 145 16 ATOM 911 CA THR A 232 20.545 10.462 6.295 1.00 14.76 C ANISOU 911 CA THR A 232 1923 1684 2002 216 141 24 ATOM 912 C THR A 232 21.840 11.278 6.464 1.00 22.50 C ANISOU 912 C THR A 232 2903 2654 2990 214 141 0 ATOM 913 O THR A 232 21.852 12.452 6.095 1.00 13.14 O ANISOU 913 O THR A 232 1718 1446 1826 216 129 -11 ATOM 914 CB THR A 232 19.717 10.550 7.609 1.00 22.75 C ANISOU 914 CB THR A 232 2928 2704 3014 211 148 57 ATOM 915 OG1 THR A 232 18.416 10.064 7.350 1.00 19.88 O ANISOU 915 OG1 THR A 232 2567 2352 2633 218 150 78 ATOM 916 CG2 THR A 232 19.561 11.940 8.250 1.00 21.85 C ANISOU 916 CG2 THR A 232 2802 2562 2937 200 135 73 ATOM 917 H THR A 232 20.577 8.370 6.614 1.00 0.00 H ATOM 918 HA THR A 232 19.966 10.919 5.490 1.00 0.00 H ATOM 919 HB THR A 232 20.161 9.887 8.353 1.00 0.00 H ATOM 920 HG1 THR A 232 18.470 9.101 7.289 1.00 0.00 H ATOM 921 HG21 THR A 232 18.863 11.908 9.088 1.00 0.00 H ATOM 922 HG22 THR A 232 20.506 12.310 8.649 1.00 0.00 H ATOM 923 HG23 THR A 232 19.185 12.668 7.531 1.00 0.00 H ATOM 924 N ILE A 233 22.912 10.637 6.960 1.00 12.90 N ANISOU 924 N ILE A 233 1690 1456 1756 211 152 -9 ATOM 925 CA ILE A 233 24.250 11.225 7.048 1.00 12.80 C ANISOU 925 CA ILE A 233 1678 1437 1747 209 152 -31 ATOM 926 C ILE A 233 24.881 11.441 5.655 1.00 12.77 C ANISOU 926 C ILE A 233 1677 1429 1744 221 148 -53 ATOM 927 O ILE A 233 25.493 12.486 5.443 1.00 18.48 O ANISOU 927 O ILE A 233 2406 2137 2479 228 140 -69 ATOM 928 CB ILE A 233 25.181 10.383 7.973 1.00 13.91 C ANISOU 928 CB ILE A 233 1820 1597 1866 206 165 -35 ATOM 929 CG1 ILE A 233 24.659 10.439 9.432 1.00 12.75 C ANISOU 929 CG1 ILE A 233 1667 1457 1719 201 173 -9 ATOM 930 CG2 ILE A 233 26.681 10.762 7.925 1.00 14.95 C ANISOU 930 CG2 ILE A 233 1954 1729 1999 205 165 -60 ATOM 931 CD1 ILE A 233 25.306 9.431 10.391 1.00 19.69 C ANISOU 931 CD1 ILE A 233 2550 2357 2576 204 187 -12 ATOM 932 H ILE A 233 22.824 9.674 7.258 1.00 0.00 H ATOM 933 HA ILE A 233 24.135 12.212 7.499 1.00 0.00 H ATOM 934 HB ILE A 233 25.111 9.349 7.639 1.00 0.00 H ATOM 935 HG13 ILE A 233 23.582 10.278 9.458 1.00 0.00 H ATOM 936 HG12 ILE A 233 24.808 11.441 9.829 1.00 0.00 H ATOM 937 HG21 ILE A 233 27.265 10.160 8.621 1.00 0.00 H ATOM 938 HG22 ILE A 233 27.119 10.596 6.940 1.00 0.00 H ATOM 939 HG23 ILE A 233 26.834 11.808 8.189 1.00 0.00 H ATOM 940 HD11 ILE A 233 24.589 9.095 11.141 1.00 0.00 H ATOM 941 HD12 ILE A 233 25.677 8.550 9.868 1.00 0.00 H ATOM 942 HD13 ILE A 233 26.138 9.890 10.924 1.00 0.00 H ATOM 943 N ALA A 234 24.659 10.502 4.715 1.00 12.73 N ANISOU 943 N ALA A 234 1670 1438 1728 227 151 -52 ATOM 944 CA ALA A 234 25.047 10.623 3.306 1.00 12.76 C ANISOU 944 CA ALA A 234 1669 1444 1734 242 151 -62 ATOM 945 C ALA A 234 24.298 11.744 2.569 1.00 21.68 C ANISOU 945 C ALA A 234 2802 2555 2882 256 143 -64 ATOM 946 O ALA A 234 24.936 12.495 1.836 1.00 20.77 O ANISOU 946 O ALA A 234 2690 2436 2768 276 144 -81 ATOM 947 CB ALA A 234 24.864 9.278 2.585 1.00 13.55 C ANISOU 947 CB ALA A 234 1762 1561 1826 240 149 -50 ATOM 948 H ALA A 234 24.162 9.657 4.964 1.00 0.00 H ATOM 949 HA ALA A 234 26.107 10.875 3.278 1.00 0.00 H ATOM 950 HB1 ALA A 234 25.232 9.332 1.559 1.00 0.00 H ATOM 951 HB2 ALA A 234 25.414 8.481 3.084 1.00 0.00 H ATOM 952 HB3 ALA A 234 23.819 8.975 2.543 1.00 0.00 H ATOM 953 N GLN A 235 22.982 11.874 2.815 1.00 17.02 N ANISOU 953 N GLN A 235 2211 1951 2303 251 134 -48 ATOM 954 CA GLN A 235 22.139 12.965 2.314 1.00 15.85 C ANISOU 954 CA GLN A 235 2068 1779 2176 264 120 -49 ATOM 955 C GLN A 235 22.608 14.355 2.778 1.00 16.61 C ANISOU 955 C GLN A 235 2177 1851 2283 269 108 -68 ATOM 956 O GLN A 235 22.630 15.275 1.965 1.00 17.42 O ANISOU 956 O GLN A 235 2291 1938 2391 293 99 -87 ATOM 957 CB GLN A 235 20.670 12.729 2.721 1.00 23.87 C ANISOU 957 CB GLN A 235 3080 2784 3207 252 111 -24 ATOM 958 CG GLN A 235 19.968 11.606 1.926 1.00 37.89 C ANISOU 958 CG GLN A 235 4848 4572 4976 255 113 -7 ATOM 959 CD GLN A 235 18.627 11.151 2.521 1.00 44.32 C ANISOU 959 CD GLN A 235 5660 5385 5793 241 108 22 ATOM 960 OE1 GLN A 235 18.122 10.092 2.154 1.00 49.31 O ANISOU 960 OE1 GLN A 235 6290 6030 6414 241 107 35 ATOM 961 NE2 GLN A 235 18.032 11.928 3.431 1.00 38.77 N ANISOU 961 NE2 GLN A 235 4957 4668 5105 231 102 35 ATOM 962 H GLN A 235 22.525 11.197 3.413 1.00 0.00 H ATOM 963 HA GLN A 235 22.200 12.950 1.223 1.00 0.00 H ATOM 964 HB3 GLN A 235 20.099 13.650 2.590 1.00 0.00 H ATOM 965 HB2 GLN A 235 20.640 12.506 3.787 1.00 0.00 H ATOM 966 HG3 GLN A 235 20.614 10.731 1.858 1.00 0.00 H ATOM 967 HG2 GLN A 235 19.800 11.933 0.900 1.00 0.00 H ATOM 968 HE22 GLN A 235 17.149 11.655 3.836 1.00 0.00 H ATOM 969 HE21 GLN A 235 18.460 12.796 3.718 1.00 0.00 H ATOM 970 N ARG A 236 23.009 14.468 4.056 1.00 14.72 N ANISOU 970 N ARG A 236 1938 1608 2047 248 106 -62 ATOM 971 CA ARG A 236 23.542 15.690 4.664 1.00 14.49 C ANISOU 971 CA ARG A 236 1920 1551 2034 247 86 -75 ATOM 972 C ARG A 236 24.954 16.065 4.169 1.00 13.42 C ANISOU 972 C ARG A 236 1798 1421 1880 267 89 -107 ATOM 973 O ARG A 236 25.294 17.246 4.236 1.00 13.65 O ANISOU 973 O ARG A 236 1846 1422 1917 284 67 -128 ATOM 974 CB ARG A 236 23.478 15.557 6.202 1.00 14.35 C ANISOU 974 CB ARG A 236 1892 1535 2024 220 85 -54 ATOM 975 CG ARG A 236 22.032 15.618 6.725 1.00 19.96 C ANISOU 975 CG ARG A 236 2591 2238 2756 205 79 -16 ATOM 976 CD ARG A 236 21.886 15.349 8.233 1.00 21.85 C ANISOU 976 CD ARG A 236 2814 2489 3000 185 87 16 ATOM 977 NE ARG A 236 20.461 15.293 8.610 1.00 25.34 N ANISOU 977 NE ARG A 236 3241 2929 3458 176 84 57 ATOM 978 CZ ARG A 236 19.925 15.144 9.837 1.00 27.56 C ANISOU 978 CZ ARG A 236 3502 3221 3748 163 91 99 ATOM 979 NH1 ARG A 236 20.670 15.034 10.944 1.00 23.38 N ANISOU 979 NH1 ARG A 236 2964 2703 3215 156 100 104 ATOM 980 NH2 ARG A 236 18.592 15.107 9.958 1.00 31.39 N1+ ANISOU 980 NH2 ARG A 236 3973 3707 4246 159 89 139 ATOM 981 H ARG A 236 22.956 13.660 4.662 1.00 0.00 H ATOM 982 HA ARG A 236 22.896 16.520 4.372 1.00 0.00 H ATOM 983 HB3 ARG A 236 24.046 16.359 6.676 1.00 0.00 H ATOM 984 HB2 ARG A 236 23.956 14.627 6.513 1.00 0.00 H ATOM 985 HG3 ARG A 236 21.352 14.992 6.145 1.00 0.00 H ATOM 986 HG2 ARG A 236 21.701 16.642 6.541 1.00 0.00 H ATOM 987 HD3 ARG A 236 22.296 16.201 8.776 1.00 0.00 H ATOM 988 HD2 ARG A 236 22.445 14.468 8.552 1.00 0.00 H ATOM 989 HE ARG A 236 19.822 15.374 7.833 1.00 0.00 H ATOM 990 HH12 ARG A 236 20.240 14.933 11.851 1.00 0.00 H ATOM 991 HH11 ARG A 236 21.684 15.025 10.887 1.00 0.00 H ATOM 992 HH22 ARG A 236 18.167 14.995 10.867 1.00 0.00 H ATOM 993 HH21 ARG A 236 18.000 15.189 9.145 1.00 0.00 H ATOM 994 N ILE A 237 25.724 15.101 3.634 1.00 13.19 N ANISOU 994 N ILE A 237 1761 1425 1827 268 113 -111 ATOM 995 CA ILE A 237 26.993 15.359 2.945 1.00 17.55 C ANISOU 995 CA ILE A 237 2320 1988 2359 291 121 -135 ATOM 996 C ILE A 237 26.762 15.876 1.509 1.00 13.44 C ANISOU 996 C ILE A 237 1807 1464 1836 327 120 -145 ATOM 997 O ILE A 237 27.443 16.817 1.101 1.00 14.73 O ANISOU 997 O ILE A 237 1991 1615 1991 356 111 -168 ATOM 998 CB ILE A 237 27.910 14.096 2.920 1.00 20.50 C ANISOU 998 CB ILE A 237 2678 2399 2713 284 145 -128 ATOM 999 CG1 ILE A 237 28.378 13.762 4.352 1.00 12.77 C ANISOU 999 CG1 ILE A 237 1696 1423 1733 256 147 -123 ATOM 1000 CG2 ILE A 237 29.136 14.183 1.982 1.00 21.37 C ANISOU 1000 CG2 ILE A 237 2789 2526 2803 311 157 -142 ATOM 1001 CD1 ILE A 237 28.870 12.323 4.543 1.00 18.14 C ANISOU 1001 CD1 ILE A 237 2363 2132 2398 246 162 -114 ATOM 1002 H ILE A 237 25.398 14.144 3.628 1.00 0.00 H ATOM 1003 HA ILE A 237 27.528 16.141 3.489 1.00 0.00 H ATOM 1004 HB ILE A 237 27.306 13.258 2.574 1.00 0.00 H ATOM 1005 HG13 ILE A 237 27.564 13.921 5.050 1.00 0.00 H ATOM 1006 HG12 ILE A 237 29.148 14.468 4.653 1.00 0.00 H ATOM 1007 HG21 ILE A 237 29.756 13.291 2.066 1.00 0.00 H ATOM 1008 HG22 ILE A 237 28.855 14.260 0.931 1.00 0.00 H ATOM 1009 HG23 ILE A 237 29.762 15.042 2.224 1.00 0.00 H ATOM 1010 HD11 ILE A 237 28.940 12.076 5.602 1.00 0.00 H ATOM 1011 HD12 ILE A 237 28.182 11.612 4.091 1.00 0.00 H ATOM 1012 HD13 ILE A 237 29.853 12.169 4.101 1.00 0.00 H ATOM 1013 N GLN A 238 25.793 15.279 0.788 1.00 18.21 N ANISOU 1013 N GLN A 238 2396 2078 2445 329 128 -126 ATOM 1014 CA GLN A 238 25.434 15.661 -0.583 1.00 23.77 C ANISOU 1014 CA GLN A 238 3102 2783 3146 366 132 -131 ATOM 1015 C GLN A 238 24.720 17.019 -0.687 1.00 22.66 C ANISOU 1015 C GLN A 238 2986 2602 3020 385 104 -148 ATOM 1016 O GLN A 238 24.984 17.754 -1.638 1.00 24.90 O ANISOU 1016 O GLN A 238 3285 2882 3293 428 104 -165 ATOM 1017 CB GLN A 238 24.619 14.538 -1.269 1.00 30.83 C ANISOU 1017 CB GLN A 238 3972 3694 4046 359 142 -103 ATOM 1018 CG GLN A 238 25.361 13.200 -1.501 1.00 13.47 C ANISOU 1018 CG GLN A 238 1750 1532 1834 350 162 -87 ATOM 1019 CD GLN A 238 26.755 13.341 -2.117 1.00 23.87 C ANISOU 1019 CD GLN A 238 3064 2872 3132 377 179 -96 ATOM 1020 OE1 GLN A 238 26.922 13.992 -3.147 1.00 30.91 O ANISOU 1020 OE1 GLN A 238 3955 3772 4018 416 189 -98 ATOM 1021 NE2 GLN A 238 27.761 12.731 -1.487 1.00 18.34 N ANISOU 1021 NE2 GLN A 238 2363 2184 2421 359 184 -101 ATOM 1022 H GLN A 238 25.278 14.506 1.187 1.00 0.00 H ATOM 1023 HA GLN A 238 26.362 15.797 -1.132 1.00 0.00 H ATOM 1024 HB3 GLN A 238 24.274 14.900 -2.239 1.00 0.00 H ATOM 1025 HB2 GLN A 238 23.714 14.341 -0.693 1.00 0.00 H ATOM 1026 HG3 GLN A 238 24.762 12.559 -2.148 1.00 0.00 H ATOM 1027 HG2 GLN A 238 25.454 12.664 -0.560 1.00 0.00 H ATOM 1028 HE22 GLN A 238 28.708 12.819 -1.841 1.00 0.00 H ATOM 1029 HE21 GLN A 238 27.596 12.199 -0.646 1.00 0.00 H ATOM 1030 N ASN A 239 23.872 17.344 0.304 1.00 20.00 N ANISOU 1030 N ASN A 239 2656 2234 2709 357 80 -140 ATOM 1031 CA ASN A 239 23.186 18.637 0.428 1.00 16.65 C ANISOU 1031 CA ASN A 239 2255 1764 2307 369 44 -152 ATOM 1032 C ASN A 239 24.081 19.730 1.046 1.00 15.01 C ANISOU 1032 C ASN A 239 2075 1528 2099 376 16 -179 ATOM 1033 O ASN A 239 23.687 20.896 1.005 1.00 17.38 O ANISOU 1033 O ASN A 239 2400 1783 2422 385 -24 -191 ATOM 1034 CB ASN A 239 21.895 18.456 1.267 1.00 18.58 C ANISOU 1034 CB ASN A 239 2488 1987 2586 334 25 -122 ATOM 1035 CG ASN A 239 20.815 17.598 0.593 1.00 20.57 C ANISOU 1035 CG ASN A 239 2724 2248 2843 339 36 -102 ATOM 1036 OD1 ASN A 239 20.758 17.488 -0.630 1.00 19.98 O ANISOU 1036 OD1 ASN A 239 2655 2174 2761 374 40 -114 ATOM 1037 ND2 ASN A 239 19.933 17.000 1.396 1.00 19.82 N ANISOU 1037 ND2 ASN A 239 2610 2161 2758 307 40 -69 ATOM 1038 H ASN A 239 23.681 16.667 1.031 1.00 0.00 H ATOM 1039 HA ASN A 239 22.909 18.966 -0.576 1.00 0.00 H ATOM 1040 HB3 ASN A 239 21.437 19.428 1.454 1.00 0.00 H ATOM 1041 HB2 ASN A 239 22.141 18.039 2.246 1.00 0.00 H ATOM 1042 HD22 ASN A 239 19.198 16.434 0.998 1.00 0.00 H ATOM 1043 HD21 ASN A 239 19.992 17.109 2.397 1.00 0.00 H ATOM 1044 N GLY A 240 25.251 19.360 1.600 1.00 18.49 N ANISOU 1044 N GLY A 240 2514 1991 2520 369 32 -188 ATOM 1045 CA GLY A 240 26.207 20.290 2.206 1.00 19.22 C ANISOU 1045 CA GLY A 240 2633 2056 2613 372 2 -212 ATOM 1046 C GLY A 240 25.707 20.864 3.543 1.00 24.95 C ANISOU 1046 C GLY A 240 3355 2748 3376 329 -31 -192 ATOM 1047 O GLY A 240 26.135 21.952 3.927 1.00 23.11 O ANISOU 1047 O GLY A 240 3147 2480 3155 329 -70 -209 ATOM 1048 H GLY A 240 25.515 18.384 1.580 1.00 0.00 H ATOM 1049 HA3 GLY A 240 26.427 21.103 1.511 1.00 0.00 H ATOM 1050 HA2 GLY A 240 27.143 19.759 2.382 1.00 0.00 H ATOM 1051 N SER A 241 24.795 20.152 4.232 1.00 20.94 N ANISOU 1051 N SER A 241 2817 2254 2887 294 -17 -155 ATOM 1052 CA SER A 241 24.193 20.527 5.516 1.00 22.74 C ANISOU 1052 CA SER A 241 3033 2455 3153 256 -44 -125 ATOM 1053 C SER A 241 25.212 20.626 6.666 1.00 27.05 C ANISOU 1053 C SER A 241 3574 3005 3698 235 -46 -123 ATOM 1054 O SER A 241 25.038 21.470 7.546 1.00 27.51 O ANISOU 1054 O SER A 241 3629 3031 3792 210 -80 -103 ATOM 1055 CB SER A 241 23.087 19.513 5.865 1.00 21.52 C ANISOU 1055 CB SER A 241 2846 2323 3007 232 -20 -83 ATOM 1056 OG SER A 241 21.972 19.678 5.013 1.00 26.92 O ANISOU 1056 OG SER A 241 3532 3002 3694 249 -20 -81 ATOM 1057 H SER A 241 24.518 19.252 3.865 1.00 0.00 H ATOM 1058 HA SER A 241 23.743 21.515 5.401 1.00 0.00 H ATOM 1059 HB3 SER A 241 22.740 19.659 6.890 1.00 0.00 H ATOM 1060 HB2 SER A 241 23.453 18.490 5.799 1.00 0.00 H ATOM 1061 HG SER A 241 22.246 19.513 4.108 1.00 0.00 H ATOM 1062 N TYR A 242 26.269 19.796 6.613 1.00 19.37 N ANISOU 1062 N TYR A 242 2598 2070 2690 242 -12 -138 ATOM 1063 CA TYR A 242 27.421 19.864 7.508 1.00 22.97 C ANISOU 1063 CA TYR A 242 3050 2531 3144 225 -13 -138 ATOM 1064 C TYR A 242 28.347 21.014 7.091 1.00 22.18 C ANISOU 1064 C TYR A 242 2986 2405 3037 247 -45 -176 ATOM 1065 O TYR A 242 28.818 21.032 5.953 1.00 18.14 O ANISOU 1065 O TYR A 242 2493 1904 2493 284 -34 -207 ATOM 1066 CB TYR A 242 28.177 18.520 7.479 1.00 26.58 C ANISOU 1066 CB TYR A 242 3491 3039 3570 222 33 -135 ATOM 1067 CG TYR A 242 27.383 17.302 7.921 1.00 18.60 C ANISOU 1067 CG TYR A 242 2453 2054 2559 205 60 -102 ATOM 1068 CD1 TYR A 242 26.542 17.363 9.052 1.00 21.46 C ANISOU 1068 CD1 TYR A 242 2797 2411 2948 180 55 -64 ATOM 1069 CD2 TYR A 242 27.503 16.089 7.210 1.00 14.36 C ANISOU 1069 CD2 TYR A 242 1910 1549 1996 217 90 -106 ATOM 1070 CE1 TYR A 242 25.821 16.230 9.461 1.00 19.52 C ANISOU 1070 CE1 TYR A 242 2531 2192 2694 173 81 -35 ATOM 1071 CE2 TYR A 242 26.793 14.949 7.631 1.00 14.63 C ANISOU 1071 CE2 TYR A 242 1929 1605 2026 206 109 -80 ATOM 1072 CZ TYR A 242 25.948 15.021 8.751 1.00 19.78 C ANISOU 1072 CZ TYR A 242 2567 2253 2696 187 106 -47 ATOM 1073 OH TYR A 242 25.258 13.916 9.143 1.00 13.02 O ANISOU 1073 OH TYR A 242 1699 1420 1826 185 127 -24 ATOM 1074 H TYR A 242 26.336 19.129 5.857 1.00 0.00 H ATOM 1075 HA TYR A 242 27.071 20.058 8.523 1.00 0.00 H ATOM 1076 HB3 TYR A 242 29.061 18.576 8.114 1.00 0.00 H ATOM 1077 HB2 TYR A 242 28.541 18.340 6.466 1.00 0.00 H ATOM 1078 HD1 TYR A 242 26.442 18.273 9.624 1.00 0.00 H ATOM 1079 HD2 TYR A 242 28.148 16.022 6.347 1.00 0.00 H ATOM 1080 HE1 TYR A 242 25.186 16.300 10.330 1.00 0.00 H ATOM 1081 HE2 TYR A 242 26.896 14.014 7.105 1.00 0.00 H ATOM 1082 HH TYR A 242 24.729 14.072 9.936 1.00 0.00 H ATOM 1083 N LYS A 243 28.581 21.943 8.030 1.00 24.72 N ANISOU 1083 N LYS A 243 3314 2692 3387 227 -85 -170 ATOM 1084 CA LYS A 243 29.424 23.129 7.842 1.00 24.75 C ANISOU 1084 CA LYS A 243 3356 2663 3384 248 -125 -207 ATOM 1085 C LYS A 243 30.824 22.956 8.462 1.00 24.52 C ANISOU 1085 C LYS A 243 3327 2658 3333 243 -112 -217 ATOM 1086 O LYS A 243 31.624 23.889 8.399 1.00 25.05 O ANISOU 1086 O LYS A 243 3427 2701 3391 259 -146 -246 ATOM 1087 CB LYS A 243 28.694 24.363 8.423 1.00 20.37 C ANISOU 1087 CB LYS A 243 2816 2045 2879 230 -193 -197 ATOM 1088 CG LYS A 243 27.273 24.600 7.868 1.00 24.35 C ANISOU 1088 CG LYS A 243 3326 2520 3407 239 -215 -190 ATOM 1089 CD LYS A 243 27.192 24.681 6.333 1.00 23.59 C ANISOU 1089 CD LYS A 243 3260 2435 3268 292 -198 -232 ATOM 1090 CE LYS A 243 25.769 24.982 5.840 1.00 27.76 C ANISOU 1090 CE LYS A 243 3798 2929 3822 303 -224 -228 ATOM 1091 NZ LYS A 243 25.698 25.017 4.368 1.00 30.95 N1+ ANISOU 1091 NZ LYS A 243 4211 3363 4184 349 -185 -253 ATOM 1092 H LYS A 243 28.135 21.859 8.932 1.00 0.00 H ATOM 1093 HA LYS A 243 29.597 23.304 6.779 1.00 0.00 H ATOM 1094 HB3 LYS A 243 29.292 25.256 8.235 1.00 0.00 H ATOM 1095 HB2 LYS A 243 28.628 24.271 9.509 1.00 0.00 H ATOM 1096 HG3 LYS A 243 26.885 25.525 8.296 1.00 0.00 H ATOM 1097 HG2 LYS A 243 26.608 23.812 8.224 1.00 0.00 H ATOM 1098 HD3 LYS A 243 27.520 23.736 5.898 1.00 0.00 H ATOM 1099 HD2 LYS A 243 27.884 25.444 5.974 1.00 0.00 H ATOM 1100 HE3 LYS A 243 25.426 25.940 6.232 1.00 0.00 H ATOM 1101 HE2 LYS A 243 25.077 24.219 6.200 1.00 0.00 H ATOM 1102 HZ1 LYS A 243 25.967 24.111 4.004 1.00 0.00 H ATOM 1103 HZ2 LYS A 243 24.752 25.224 4.080 1.00 0.00 H ATOM 1104 HZ3 LYS A 243 26.323 25.725 4.012 1.00 0.00 H ATOM 1105 N SER A 244 31.106 21.767 9.020 1.00 22.08 N ANISOU 1105 N SER A 244 2984 2392 3015 222 -67 -194 ATOM 1106 CA SER A 244 32.389 21.368 9.590 1.00 23.13 C ANISOU 1106 CA SER A 244 3113 2550 3127 218 -51 -201 ATOM 1107 C SER A 244 32.467 19.834 9.668 1.00 23.83 C ANISOU 1107 C SER A 244 3169 2688 3199 206 3 -180 ATOM 1108 O SER A 244 31.459 19.148 9.487 1.00 24.68 O ANISOU 1108 O SER A 244 3257 2805 3314 199 21 -158 ATOM 1109 CB SER A 244 32.603 22.053 10.963 1.00 24.03 C ANISOU 1109 CB SER A 244 3223 2633 3275 187 -89 -185 ATOM 1110 OG SER A 244 31.740 21.543 11.962 1.00 26.37 O ANISOU 1110 OG SER A 244 3480 2935 3604 153 -78 -137 ATOM 1111 H SER A 244 30.404 21.042 9.006 1.00 0.00 H ATOM 1112 HA SER A 244 33.176 21.699 8.909 1.00 0.00 H ATOM 1113 HB3 SER A 244 32.469 23.133 10.893 1.00 0.00 H ATOM 1114 HB2 SER A 244 33.629 21.897 11.299 1.00 0.00 H ATOM 1115 HG SER A 244 30.860 21.898 11.809 1.00 0.00 H ATOM 1116 N ILE A 245 33.671 19.326 9.979 1.00 14.40 N ANISOU 1116 N ILE A 245 1970 1520 1981 206 23 -188 ATOM 1117 CA ILE A 245 33.911 17.909 10.266 1.00 21.59 C ANISOU 1117 CA ILE A 245 2854 2470 2880 194 64 -170 ATOM 1118 C ILE A 245 33.252 17.474 11.597 1.00 22.99 C ANISOU 1118 C ILE A 245 3006 2643 3085 165 65 -133 ATOM 1119 O ILE A 245 32.765 16.346 11.685 1.00 20.07 O ANISOU 1119 O ILE A 245 2619 2298 2710 161 92 -114 ATOM 1120 CB ILE A 245 35.433 17.572 10.302 1.00 22.61 C ANISOU 1120 CB ILE A 245 2983 2622 2984 198 78 -184 ATOM 1121 CG1 ILE A 245 36.118 17.927 8.958 1.00 34.14 C ANISOU 1121 CG1 ILE A 245 4467 4090 4415 231 78 -213 ATOM 1122 CG2 ILE A 245 35.718 16.096 10.655 1.00 20.27 C ANISOU 1122 CG2 ILE A 245 2664 2361 2676 188 113 -168 ATOM 1123 CD1 ILE A 245 37.653 17.916 9.014 1.00 31.60 C ANISOU 1123 CD1 ILE A 245 4142 3797 4068 236 96 -220 ATOM 1124 H ILE A 245 34.462 19.943 10.095 1.00 0.00 H ATOM 1125 HA ILE A 245 33.452 17.323 9.472 1.00 0.00 H ATOM 1126 HB ILE A 245 35.893 18.190 11.075 1.00 0.00 H ATOM 1127 HG13 ILE A 245 35.814 18.916 8.616 1.00 0.00 H ATOM 1128 HG12 ILE A 245 35.779 17.235 8.186 1.00 0.00 H ATOM 1129 HG21 ILE A 245 36.779 15.860 10.594 1.00 0.00 H ATOM 1130 HG22 ILE A 245 35.401 15.836 11.663 1.00 0.00 H ATOM 1131 HG23 ILE A 245 35.187 15.439 9.970 1.00 0.00 H ATOM 1132 HD11 ILE A 245 38.073 18.502 8.196 1.00 0.00 H ATOM 1133 HD12 ILE A 245 38.022 18.346 9.945 1.00 0.00 H ATOM 1134 HD13 ILE A 245 38.050 16.904 8.929 1.00 0.00 H ATOM 1135 N HIS A 246 33.200 18.397 12.576 1.00 17.13 N ANISOU 1135 N HIS A 246 2262 1874 2373 148 34 -120 ATOM 1136 CA HIS A 246 32.527 18.227 13.865 1.00 18.24 C ANISOU 1136 CA HIS A 246 2373 2015 2542 123 37 -76 ATOM 1137 C HIS A 246 30.993 18.097 13.750 1.00 24.37 C ANISOU 1137 C HIS A 246 3136 2789 3333 122 42 -49 ATOM 1138 O HIS A 246 30.391 17.432 14.593 1.00 22.29 O ANISOU 1138 O HIS A 246 2850 2551 3070 116 69 -16 ATOM 1139 CB HIS A 246 32.937 19.383 14.801 1.00 24.77 C ANISOU 1139 CB HIS A 246 3198 2807 3408 103 -6 -62 ATOM 1140 CG HIS A 246 32.410 19.269 16.213 1.00 34.48 C ANISOU 1140 CG HIS A 246 4390 4040 4672 80 -3 -6 ATOM 1141 ND1 HIS A 246 31.397 20.073 16.705 1.00 31.97 N ANISOU 1141 ND1 HIS A 246 4046 3757 4342 77 34 16 ATOM 1142 CD2 HIS A 246 32.760 18.434 17.252 1.00 33.90 C ANISOU 1142 CD2 HIS A 246 4296 3939 4644 61 -31 37 ATOM 1143 CE1 HIS A 246 31.174 19.697 17.968 1.00 34.54 C ANISOU 1143 CE1 HIS A 246 4339 4084 4702 61 33 71 ATOM 1144 NE2 HIS A 246 31.964 18.708 18.368 1.00 33.61 N ANISOU 1144 NE2 HIS A 246 4220 3928 4621 48 -6 88 ATOM 1145 H HIS A 246 33.606 19.307 12.411 1.00 0.00 H ATOM 1146 HA HIS A 246 32.908 17.302 14.299 1.00 0.00 H ATOM 1147 HB3 HIS A 246 32.616 20.338 14.383 1.00 0.00 H ATOM 1148 HB2 HIS A 246 34.024 19.432 14.866 1.00 0.00 H ATOM 1149 HD1 HIS A 246 30.911 20.803 16.205 1.00 0.00 H ATOM 1150 HD2 HIS A 246 33.510 17.658 17.282 1.00 0.00 H ATOM 1151 HE1 HIS A 246 30.426 20.151 18.602 1.00 0.00 H ATOM 1152 N ALA A 247 30.394 18.701 12.706 1.00 17.25 N ANISOU 1152 N ALA A 247 2254 1860 2442 130 16 -63 ATOM 1153 CA ALA A 247 28.964 18.602 12.410 1.00 18.91 C ANISOU 1153 CA ALA A 247 2454 2067 2666 130 20 -39 ATOM 1154 C ALA A 247 28.543 17.187 11.974 1.00 23.13 C ANISOU 1154 C ALA A 247 2979 2643 3165 142 65 -38 ATOM 1155 O ALA A 247 27.482 16.732 12.402 1.00 18.54 O ANISOU 1155 O ALA A 247 2378 2077 2588 136 82 -4 ATOM 1156 CB ALA A 247 28.578 19.653 11.357 1.00 18.73 C ANISOU 1156 CB ALA A 247 2457 2007 2653 144 -15 -64 ATOM 1157 H ALA A 247 30.952 19.234 12.053 1.00 0.00 H ATOM 1158 HA ALA A 247 28.423 18.841 13.329 1.00 0.00 H ATOM 1159 HB1 ALA A 247 27.497 19.689 11.221 1.00 0.00 H ATOM 1160 HB2 ALA A 247 28.899 20.650 11.659 1.00 0.00 H ATOM 1161 HB3 ALA A 247 29.025 19.438 10.388 1.00 0.00 H ATOM 1162 N MET A 248 29.395 16.502 11.185 1.00 17.34 N ANISOU 1162 N MET A 248 2261 1929 2397 159 83 -73 ATOM 1163 CA MET A 248 29.236 15.080 10.864 1.00 16.00 C ANISOU 1163 CA MET A 248 2086 1794 2200 168 116 -71 ATOM 1164 C MET A 248 29.528 14.181 12.077 1.00 16.52 C ANISOU 1164 C MET A 248 2136 1886 2256 160 139 -51 ATOM 1165 O MET A 248 28.806 13.206 12.275 1.00 21.29 O ANISOU 1165 O MET A 248 2733 2510 2848 164 158 -33 ATOM 1166 CB MET A 248 30.100 14.690 9.641 1.00 14.69 C ANISOU 1166 CB MET A 248 1933 1640 2006 186 125 -104 ATOM 1167 CG MET A 248 30.010 13.195 9.264 1.00 12.44 C ANISOU 1167 CG MET A 248 1642 1387 1699 191 150 -101 ATOM 1168 SD MET A 248 30.946 12.700 7.797 1.00 19.65 S ANISOU 1168 SD MET A 248 2561 2317 2589 209 159 -124 ATOM 1169 CE MET A 248 30.730 10.905 7.903 1.00 13.80 C ANISOU 1169 CE MET A 248 1811 1600 1832 204 174 -110 ATOM 1170 H MET A 248 30.248 16.941 10.871 1.00 0.00 H ATOM 1171 HA MET A 248 28.193 14.914 10.589 1.00 0.00 H ATOM 1172 HB3 MET A 248 31.143 14.940 9.837 1.00 0.00 H ATOM 1173 HB2 MET A 248 29.805 15.294 8.782 1.00 0.00 H ATOM 1174 HG3 MET A 248 28.968 12.917 9.109 1.00 0.00 H ATOM 1175 HG2 MET A 248 30.380 12.576 10.081 1.00 0.00 H ATOM 1176 HE1 MET A 248 31.306 10.417 7.121 1.00 0.00 H ATOM 1177 HE2 MET A 248 31.075 10.529 8.866 1.00 0.00 H ATOM 1178 HE3 MET A 248 29.681 10.638 7.780 1.00 0.00 H ATOM 1179 N ALA A 249 30.569 14.528 12.859 1.00 15.36 N ANISOU 1179 N ALA A 249 1986 1739 2112 152 137 -54 ATOM 1180 CA ALA A 249 31.015 13.786 14.040 1.00 18.75 C ANISOU 1180 CA ALA A 249 2401 2192 2532 149 158 -34 ATOM 1181 C ALA A 249 29.938 13.644 15.124 1.00 22.98 C ANISOU 1181 C ALA A 249 2916 2733 3084 145 166 12 ATOM 1182 O ALA A 249 29.829 12.563 15.697 1.00 18.58 O ANISOU 1182 O ALA A 249 2352 2203 2505 157 192 28 ATOM 1183 CB ALA A 249 32.279 14.437 14.620 1.00 14.65 C ANISOU 1183 CB ALA A 249 1878 1668 2020 139 150 -40 ATOM 1184 H ALA A 249 31.119 15.340 12.614 1.00 0.00 H ATOM 1185 HA ALA A 249 31.274 12.781 13.701 1.00 0.00 H ATOM 1186 HB1 ALA A 249 32.740 13.789 15.364 1.00 0.00 H ATOM 1187 HB2 ALA A 249 33.025 14.628 13.849 1.00 0.00 H ATOM 1188 HB3 ALA A 249 32.053 15.381 15.115 1.00 0.00 H ATOM 1189 N LYS A 250 29.132 14.700 15.334 1.00 17.37 N ANISOU 1189 N LYS A 250 2195 1996 2410 131 141 35 ATOM 1190 CA LYS A 250 27.973 14.707 16.229 1.00 19.74 C ANISOU 1190 CA LYS A 250 2469 2303 2728 127 149 88 ATOM 1191 C LYS A 250 26.901 13.669 15.843 1.00 19.00 C ANISOU 1191 C LYS A 250 2380 2233 2606 145 173 93 ATOM 1192 O LYS A 250 26.340 13.035 16.736 1.00 24.05 O ANISOU 1192 O LYS A 250 3005 2902 3230 157 199 126 ATOM 1193 CB LYS A 250 27.396 16.141 16.297 1.00 0.00 C ATOM 1194 CG LYS A 250 26.148 16.288 17.190 1.00 0.00 C ATOM 1195 CD LYS A 250 25.640 17.732 17.292 1.00 0.00 C ATOM 1196 CE LYS A 250 24.362 17.824 18.142 1.00 0.00 C ATOM 1197 NZ LYS A 250 23.846 19.203 18.215 1.00 0.00 N1+ ATOM 1198 H LYS A 250 29.302 15.557 14.824 1.00 0.00 H ATOM 1199 HA LYS A 250 28.338 14.444 17.224 1.00 0.00 H ATOM 1200 HB2 LYS A 250 28.173 16.816 16.660 1.00 0.00 H ATOM 1201 HB3 LYS A 250 27.150 16.481 15.289 1.00 0.00 H ATOM 1202 HG2 LYS A 250 25.336 15.673 16.801 1.00 0.00 H ATOM 1203 HG3 LYS A 250 26.371 15.906 18.188 1.00 0.00 H ATOM 1204 HD2 LYS A 250 26.422 18.358 17.723 1.00 0.00 H ATOM 1205 HD3 LYS A 250 25.453 18.117 16.288 1.00 0.00 H ATOM 1206 HE2 LYS A 250 23.583 17.187 17.721 1.00 0.00 H ATOM 1207 HE3 LYS A 250 24.554 17.468 19.155 1.00 0.00 H ATOM 1208 HZ1 LYS A 250 23.631 19.531 17.284 1.00 0.00 H ATOM 1209 HZ2 LYS A 250 23.006 19.218 18.777 1.00 0.00 H ATOM 1210 HZ3 LYS A 250 24.541 19.805 18.632 1.00 0.00 H ATOM 1211 N ASP A 251 26.651 13.506 14.533 1.00 18.50 N ANISOU 1211 N ASP A 251 2337 2159 2533 151 164 62 ATOM 1212 CA ASP A 251 25.684 12.548 13.989 1.00 22.73 C ANISOU 1212 CA ASP A 251 2879 2713 3043 166 180 67 ATOM 1213 C ASP A 251 26.207 11.101 13.963 1.00 23.26 C ANISOU 1213 C ASP A 251 2958 2810 3068 184 204 50 ATOM 1214 O ASP A 251 25.391 10.186 14.065 1.00 17.31 O ANISOU 1214 O ASP A 251 2208 2080 2290 200 220 67 ATOM 1215 CB ASP A 251 25.131 12.968 12.607 1.00 20.74 C ANISOU 1215 CB ASP A 251 2643 2441 2798 167 162 41 ATOM 1216 CG ASP A 251 24.225 14.217 12.585 1.00 22.48 C ANISOU 1216 CG ASP A 251 2854 2635 3054 157 140 67 ATOM 1217 OD1 ASP A 251 24.043 14.883 13.630 1.00 16.63 O ANISOU 1217 OD1 ASP A 251 2091 1890 2339 145 136 108 ATOM 1218 OD2 ASP A 251 23.707 14.494 11.483 1.00 23.12 O1- ANISOU 1218 OD2 ASP A 251 2946 2699 3140 162 126 51 ATOM 1219 H ASP A 251 27.152 14.065 13.857 1.00 0.00 H ATOM 1220 HA ASP A 251 24.834 12.533 14.671 1.00 0.00 H ATOM 1221 HB3 ASP A 251 24.595 12.137 12.149 1.00 0.00 H ATOM 1222 HB2 ASP A 251 25.973 13.179 11.944 1.00 0.00 H ATOM 1223 N ILE A 252 27.537 10.909 13.885 1.00 23.22 N ANISOU 1223 N ILE A 252 2964 2806 3052 183 203 17 ATOM 1224 CA ILE A 252 28.191 9.610 14.085 1.00 20.38 C ANISOU 1224 CA ILE A 252 2616 2469 2658 198 218 3 ATOM 1225 C ILE A 252 28.138 9.171 15.566 1.00 24.35 C ANISOU 1225 C ILE A 252 3109 2994 3149 210 239 32 ATOM 1226 O ILE A 252 27.889 7.993 15.825 1.00 12.83 O ANISOU 1226 O ILE A 252 1663 1556 1657 233 252 34 ATOM 1227 CB ILE A 252 29.664 9.609 13.570 1.00 12.38 C ANISOU 1227 CB ILE A 252 1611 1450 1643 191 210 -31 ATOM 1228 CG1 ILE A 252 29.736 9.788 12.032 1.00 14.35 C ANISOU 1228 CG1 ILE A 252 1869 1687 1896 188 196 -55 ATOM 1229 CG2 ILE A 252 30.525 8.402 14.018 1.00 12.29 C ANISOU 1229 CG2 ILE A 252 1612 1457 1601 204 220 -44 ATOM 1230 CD1 ILE A 252 29.142 8.639 11.201 1.00 12.70 C ANISOU 1230 CD1 ILE A 252 1671 1486 1668 199 196 -59 ATOM 1231 H ILE A 252 28.147 11.707 13.772 1.00 0.00 H ATOM 1232 HA ILE A 252 27.630 8.864 13.520 1.00 0.00 H ATOM 1233 HB ILE A 252 30.150 10.491 13.988 1.00 0.00 H ATOM 1234 HG13 ILE A 252 30.773 9.940 11.735 1.00 0.00 H ATOM 1235 HG12 ILE A 252 29.225 10.707 11.747 1.00 0.00 H ATOM 1236 HG21 ILE A 252 31.496 8.409 13.527 1.00 0.00 H ATOM 1237 HG22 ILE A 252 30.722 8.416 15.090 1.00 0.00 H ATOM 1238 HG23 ILE A 252 30.046 7.451 13.782 1.00 0.00 H ATOM 1239 HD11 ILE A 252 29.440 8.727 10.156 1.00 0.00 H ATOM 1240 HD12 ILE A 252 29.469 7.663 11.556 1.00 0.00 H ATOM 1241 HD13 ILE A 252 28.054 8.649 11.229 1.00 0.00 H ATOM 1242 N ASP A 253 28.306 10.130 16.499 1.00 17.19 N ANISOU 1242 N ASP A 253 2179 2082 2269 198 240 57 ATOM 1243 CA ASP A 253 28.105 9.942 17.942 1.00 18.00 C ANISOU 1243 CA ASP A 253 2265 2210 2365 213 263 95 ATOM 1244 C ASP A 253 26.650 9.598 18.286 1.00 23.06 C ANISOU 1244 C ASP A 253 2898 2870 2994 230 279 134 ATOM 1245 O ASP A 253 26.442 8.693 19.090 1.00 22.57 O ANISOU 1245 O ASP A 253 2842 2838 2895 262 304 148 ATOM 1246 CB ASP A 253 28.555 11.140 18.823 1.00 13.24 C ANISOU 1246 CB ASP A 253 1634 1595 1803 191 255 123 ATOM 1247 CG ASP A 253 30.014 11.607 18.695 1.00 22.16 C ANISOU 1247 CG ASP A 253 2771 2711 2938 178 242 88 ATOM 1248 OD1 ASP A 253 30.859 10.826 18.208 1.00 22.05 O ANISOU 1248 OD1 ASP A 253 2781 2702 2896 187 244 48 ATOM 1249 OD2 ASP A 253 30.294 12.707 19.217 1.00 23.65 O1- ANISOU 1249 OD2 ASP A 253 2940 2883 3161 158 227 105 ATOM 1250 H ASP A 253 28.548 11.069 16.207 1.00 0.00 H ATOM 1251 HA ASP A 253 28.705 9.075 18.230 1.00 0.00 H ATOM 1252 HB3 ASP A 253 28.396 10.891 19.874 1.00 0.00 H ATOM 1253 HB2 ASP A 253 27.923 12.002 18.608 1.00 0.00 H ATOM 1254 N LEU A 254 25.684 10.300 17.662 1.00 17.92 N ANISOU 1254 N LEU A 254 2236 2201 2372 214 264 152 ATOM 1255 CA LEU A 254 24.246 10.083 17.828 1.00 19.82 C ANISOU 1255 CA LEU A 254 2467 2458 2604 228 277 193 ATOM 1256 C LEU A 254 23.819 8.679 17.372 1.00 21.85 C ANISOU 1256 C LEU A 254 2756 2736 2809 258 289 169 ATOM 1257 O LEU A 254 23.189 7.975 18.157 1.00 25.86 O ANISOU 1257 O LEU A 254 3265 3276 3285 289 313 198 ATOM 1258 CB LEU A 254 23.457 11.199 17.099 1.00 16.29 C ANISOU 1258 CB LEU A 254 2010 1980 2197 203 250 204 ATOM 1259 CG LEU A 254 21.916 11.158 17.251 1.00 14.12 C ANISOU 1259 CG LEU A 254 1727 1722 1916 215 260 245 ATOM 1260 CD1 LEU A 254 21.462 11.312 18.719 1.00 14.53 C ANISOU 1260 CD1 LEU A 254 1743 1805 1973 227 286 316 ATOM 1261 CD2 LEU A 254 21.239 12.184 16.314 1.00 14.17 C ANISOU 1261 CD2 LEU A 254 1729 1692 1961 192 229 248 ATOM 1262 H LEU A 254 25.949 11.051 17.038 1.00 0.00 H ATOM 1263 HA LEU A 254 24.042 10.158 18.897 1.00 0.00 H ATOM 1264 HB3 LEU A 254 23.698 11.143 16.038 1.00 0.00 H ATOM 1265 HB2 LEU A 254 23.815 12.173 17.435 1.00 0.00 H ATOM 1266 HG LEU A 254 21.571 10.181 16.912 1.00 0.00 H ATOM 1267 HD11 LEU A 254 21.045 10.376 19.091 1.00 0.00 H ATOM 1268 HD12 LEU A 254 22.286 11.589 19.376 1.00 0.00 H ATOM 1269 HD13 LEU A 254 20.696 12.076 18.847 1.00 0.00 H ATOM 1270 HD21 LEU A 254 20.468 11.705 15.710 1.00 0.00 H ATOM 1271 HD22 LEU A 254 20.763 13.002 16.856 1.00 0.00 H ATOM 1272 HD23 LEU A 254 21.949 12.638 15.622 1.00 0.00 H ATOM 1273 N LEU A 255 24.207 8.296 16.142 1.00 13.43 N ANISOU 1273 N LEU A 255 1716 1652 1734 251 270 120 ATOM 1274 CA LEU A 255 23.940 6.992 15.527 1.00 15.82 C ANISOU 1274 CA LEU A 255 2049 1966 1994 274 270 98 ATOM 1275 C LEU A 255 24.467 5.815 16.363 1.00 18.70 C ANISOU 1275 C LEU A 255 2432 2356 2317 306 286 91 ATOM 1276 O LEU A 255 23.721 4.866 16.610 1.00 16.95 O ANISOU 1276 O LEU A 255 2229 2157 2055 340 298 102 ATOM 1277 CB LEU A 255 24.514 6.994 14.090 1.00 16.26 C ANISOU 1277 CB LEU A 255 2123 1999 2058 258 244 54 ATOM 1278 CG LEU A 255 24.182 5.744 13.239 1.00 25.59 C ANISOU 1278 CG LEU A 255 3332 3182 3208 273 232 34 ATOM 1279 CD1 LEU A 255 24.123 6.113 11.752 1.00 25.00 C ANISOU 1279 CD1 LEU A 255 3257 3085 3157 253 211 16 ATOM 1280 CD2 LEU A 255 25.159 4.570 13.465 1.00 28.42 C ANISOU 1280 CD2 LEU A 255 3716 3547 3537 288 227 6 ATOM 1281 H LEU A 255 24.725 8.950 15.568 1.00 0.00 H ATOM 1282 HA LEU A 255 22.855 6.890 15.462 1.00 0.00 H ATOM 1283 HB3 LEU A 255 25.592 7.165 14.103 1.00 0.00 H ATOM 1284 HB2 LEU A 255 24.107 7.869 13.583 1.00 0.00 H ATOM 1285 HG LEU A 255 23.180 5.409 13.507 1.00 0.00 H ATOM 1286 HD11 LEU A 255 23.875 5.246 11.138 1.00 0.00 H ATOM 1287 HD12 LEU A 255 23.364 6.874 11.571 1.00 0.00 H ATOM 1288 HD13 LEU A 255 25.077 6.510 11.408 1.00 0.00 H ATOM 1289 HD21 LEU A 255 25.529 4.153 12.528 1.00 0.00 H ATOM 1290 HD22 LEU A 255 26.034 4.866 14.044 1.00 0.00 H ATOM 1291 HD23 LEU A 255 24.670 3.762 14.009 1.00 0.00 H ATOM 1292 N ALA A 256 25.735 5.919 16.793 1.00 18.51 N ANISOU 1292 N ALA A 256 2405 2328 2299 300 288 74 ATOM 1293 CA ALA A 256 26.408 4.917 17.612 1.00 16.08 C ANISOU 1293 CA ALA A 256 2117 2040 1953 332 300 63 ATOM 1294 C ALA A 256 25.847 4.824 19.040 1.00 13.82 C ANISOU 1294 C ALA A 256 1815 1787 1647 365 334 110 ATOM 1295 O ALA A 256 25.746 3.715 19.557 1.00 25.42 O ANISOU 1295 O ALA A 256 3310 3280 3068 409 347 108 ATOM 1296 CB ALA A 256 27.912 5.201 17.627 1.00 13.86 C ANISOU 1296 CB ALA A 256 1833 1746 1688 316 293 37 ATOM 1297 H ALA A 256 26.284 6.730 16.538 1.00 0.00 H ATOM 1298 HA ALA A 256 26.254 3.950 17.131 1.00 0.00 H ATOM 1299 HB1 ALA A 256 28.445 4.473 18.240 1.00 0.00 H ATOM 1300 HB2 ALA A 256 28.328 5.148 16.620 1.00 0.00 H ATOM 1301 HB3 ALA A 256 28.122 6.197 18.020 1.00 0.00 H ATOM 1302 N LYS A 257 25.458 5.967 19.636 1.00 17.77 N ANISOU 1302 N LYS A 257 2275 2292 2186 347 346 156 ATOM 1303 CA LYS A 257 24.805 6.040 20.945 1.00 19.59 C ANISOU 1303 CA LYS A 257 2482 2560 2402 379 381 213 ATOM 1304 C LYS A 257 23.415 5.382 20.943 1.00 21.03 C ANISOU 1304 C LYS A 257 2674 2765 2551 409 394 238 ATOM 1305 O LYS A 257 23.108 4.680 21.902 1.00 18.09 O ANISOU 1305 O LYS A 257 2308 2432 2133 459 424 264 ATOM 1306 CB LYS A 257 24.743 7.508 21.421 1.00 19.04 C ANISOU 1306 CB LYS A 257 2361 2483 2390 346 384 262 ATOM 1307 CG LYS A 257 24.088 7.727 22.803 1.00 25.07 C ANISOU 1307 CG LYS A 257 3090 3288 3145 378 422 330 ATOM 1308 CD LYS A 257 23.920 9.211 23.187 1.00 29.46 C ANISOU 1308 CD LYS A 257 3591 3835 3766 341 416 391 ATOM 1309 CE LYS A 257 23.016 10.047 22.253 1.00 43.54 C ANISOU 1309 CE LYS A 257 5369 5587 5587 305 386 397 ATOM 1310 NZ LYS A 257 21.645 9.510 22.141 1.00 50.02 N1+ ANISOU 1310 NZ LYS A 257 6211 6424 6370 330 395 398 ATOM 1311 H LYS A 257 25.587 6.848 19.154 1.00 0.00 H ATOM 1312 HA LYS A 257 25.431 5.490 21.650 1.00 0.00 H ATOM 1313 HB3 LYS A 257 24.210 8.086 20.667 1.00 0.00 H ATOM 1314 HB2 LYS A 257 25.754 7.913 21.460 1.00 0.00 H ATOM 1315 HG3 LYS A 257 24.698 7.235 23.561 1.00 0.00 H ATOM 1316 HG2 LYS A 257 23.115 7.242 22.860 1.00 0.00 H ATOM 1317 HD3 LYS A 257 24.905 9.677 23.224 1.00 0.00 H ATOM 1318 HD2 LYS A 257 23.535 9.270 24.206 1.00 0.00 H ATOM 1319 HE3 LYS A 257 23.447 10.118 21.255 1.00 0.00 H ATOM 1320 HE2 LYS A 257 22.950 11.068 22.629 1.00 0.00 H ATOM 1321 HZ1 LYS A 257 21.674 8.581 21.742 1.00 0.00 H ATOM 1322 HZ2 LYS A 257 21.219 9.470 23.057 1.00 0.00 H ATOM 1323 HZ3 LYS A 257 21.096 10.109 21.541 1.00 0.00 H ATOM 1324 N ASN A 258 22.619 5.597 19.878 1.00 18.38 N ANISOU 1324 N ASN A 258 2342 2408 2234 384 372 232 ATOM 1325 CA ASN A 258 21.286 5.003 19.701 1.00 16.28 C ANISOU 1325 CA ASN A 258 2092 2161 1934 411 378 249 ATOM 1326 C ASN A 258 21.345 3.473 19.573 1.00 17.89 C ANISOU 1326 C ASN A 258 2348 2378 2072 456 377 209 ATOM 1327 O ASN A 258 20.524 2.784 20.176 1.00 16.90 O ANISOU 1327 O ASN A 258 2237 2290 1896 507 401 233 ATOM 1328 CB ASN A 258 20.587 5.589 18.454 1.00 14.61 C ANISOU 1328 CB ASN A 258 1879 1917 1755 374 349 237 ATOM 1329 CG ASN A 258 20.265 7.084 18.523 1.00 24.01 C ANISOU 1329 CG ASN A 258 3023 3096 3005 340 346 287 ATOM 1330 OD1 ASN A 258 20.235 7.695 19.592 1.00 17.43 O ANISOU 1330 OD1 ASN A 258 2154 2283 2187 345 368 342 ATOM 1331 ND2 ASN A 258 20.001 7.672 17.356 1.00 14.53 N ANISOU 1331 ND2 ASN A 258 1822 1861 1839 307 317 272 ATOM 1332 H ASN A 258 22.937 6.205 19.134 1.00 0.00 H ATOM 1333 HA ASN A 258 20.714 5.254 20.595 1.00 0.00 H ATOM 1334 HB3 ASN A 258 19.636 5.077 18.300 1.00 0.00 H ATOM 1335 HB2 ASN A 258 21.185 5.396 17.562 1.00 0.00 H ATOM 1336 HD22 ASN A 258 19.728 8.646 17.319 1.00 0.00 H ATOM 1337 HD21 ASN A 258 20.036 7.139 16.499 1.00 0.00 H ATOM 1338 N ALA A 259 22.341 2.977 18.824 1.00 20.61 N ANISOU 1338 N ALA A 259 2722 2693 2414 441 347 150 ATOM 1339 CA ALA A 259 22.653 1.558 18.689 1.00 23.66 C ANISOU 1339 CA ALA A 259 3161 3082 2745 480 333 110 ATOM 1340 C ALA A 259 23.121 0.916 20.007 1.00 19.11 C ANISOU 1340 C ALA A 259 2596 2538 2127 531 362 120 ATOM 1341 O ALA A 259 22.739 -0.218 20.287 1.00 19.22 O ANISOU 1341 O ALA A 259 2649 2572 2080 586 366 113 ATOM 1342 CB ALA A 259 23.717 1.408 17.600 1.00 14.24 C ANISOU 1342 CB ALA A 259 1987 1852 1571 449 295 55 ATOM 1343 H ALA A 259 22.961 3.614 18.341 1.00 0.00 H ATOM 1344 HA ALA A 259 21.751 1.038 18.362 1.00 0.00 H ATOM 1345 HB1 ALA A 259 24.004 0.365 17.464 1.00 0.00 H ATOM 1346 HB2 ALA A 259 23.343 1.785 16.647 1.00 0.00 H ATOM 1347 HB3 ALA A 259 24.615 1.974 17.841 1.00 0.00 H ATOM 1348 N LYS A 260 23.898 1.663 20.806 1.00 18.19 N ANISOU 1348 N LYS A 260 2447 2427 2039 519 381 136 ATOM 1349 CA LYS A 260 24.377 1.247 22.125 1.00 19.22 C ANISOU 1349 CA LYS A 260 2584 2587 2133 568 410 145 ATOM 1350 C LYS A 260 23.325 1.370 23.249 1.00 23.19 C ANISOU 1350 C LYS A 260 3062 3139 2609 613 456 212 ATOM 1351 O LYS A 260 23.541 0.794 24.314 1.00 21.76 O ANISOU 1351 O LYS A 260 2890 2992 2388 668 486 225 ATOM 1352 CB LYS A 260 25.655 2.037 22.467 1.00 14.90 C ANISOU 1352 CB LYS A 260 2008 2026 1628 537 411 140 ATOM 1353 CG LYS A 260 26.883 1.610 21.637 1.00 16.05 C ANISOU 1353 CG LYS A 260 2183 2131 1784 509 370 76 ATOM 1354 CD LYS A 260 28.069 2.581 21.757 1.00 23.11 C ANISOU 1354 CD LYS A 260 3044 3008 2731 464 366 74 ATOM 1355 CE LYS A 260 28.646 2.673 23.181 1.00 25.73 C ANISOU 1355 CE LYS A 260 3358 3364 3054 493 397 99 ATOM 1356 NZ LYS A 260 29.772 3.619 23.255 1.00 22.74 N1+ ANISOU 1356 NZ LYS A 260 2946 2967 2726 449 391 99 ATOM 1357 H LYS A 260 24.186 2.583 20.499 1.00 0.00 H ATOM 1358 HA LYS A 260 24.640 0.193 22.051 1.00 0.00 H ATOM 1359 HB3 LYS A 260 25.897 1.899 23.521 1.00 0.00 H ATOM 1360 HB2 LYS A 260 25.464 3.104 22.341 1.00 0.00 H ATOM 1361 HG3 LYS A 260 26.611 1.514 20.586 1.00 0.00 H ATOM 1362 HG2 LYS A 260 27.203 0.613 21.940 1.00 0.00 H ATOM 1363 HD3 LYS A 260 27.753 3.570 21.422 1.00 0.00 H ATOM 1364 HD2 LYS A 260 28.843 2.264 21.058 1.00 0.00 H ATOM 1365 HE3 LYS A 260 28.991 1.692 23.511 1.00 0.00 H ATOM 1366 HE2 LYS A 260 27.886 3.004 23.888 1.00 0.00 H ATOM 1367 HZ1 LYS A 260 29.464 4.539 22.972 1.00 0.00 H ATOM 1368 HZ2 LYS A 260 30.123 3.655 24.201 1.00 0.00 H ATOM 1369 HZ3 LYS A 260 30.508 3.301 22.636 1.00 0.00 H ATOM 1370 N THR A 261 22.224 2.102 23.004 1.00 22.88 N ANISOU 1370 N THR A 261 2992 3107 2594 593 463 256 ATOM 1371 CA THR A 261 21.116 2.282 23.947 1.00 28.47 C ANISOU 1371 CA THR A 261 3674 3864 3279 633 505 326 ATOM 1372 C THR A 261 20.034 1.208 23.734 1.00 30.12 C ANISOU 1372 C THR A 261 3933 4093 3418 687 505 315 ATOM 1373 O THR A 261 19.558 0.643 24.718 1.00 31.68 O ANISOU 1373 O THR A 261 4143 4338 3556 756 541 344 ATOM 1374 CB THR A 261 20.456 3.683 23.791 1.00 28.93 C ANISOU 1374 CB THR A 261 3674 3915 3402 582 506 383 ATOM 1375 OG1 THR A 261 21.396 4.677 24.144 1.00 25.40 O ANISOU 1375 OG1 THR A 261 3183 3449 3018 538 503 399 ATOM 1376 CG2 THR A 261 19.195 3.938 24.638 1.00 21.59 C ANISOU 1376 CG2 THR A 261 2716 3039 2450 623 548 464 ATOM 1377 H THR A 261 22.128 2.563 22.110 1.00 0.00 H ATOM 1378 HA THR A 261 21.486 2.191 24.971 1.00 0.00 H ATOM 1379 HB THR A 261 20.205 3.849 22.743 1.00 0.00 H ATOM 1380 HG1 THR A 261 22.124 4.637 23.516 1.00 0.00 H ATOM 1381 HG21 THR A 261 18.850 4.967 24.529 1.00 0.00 H ATOM 1382 HG22 THR A 261 18.369 3.295 24.340 1.00 0.00 H ATOM 1383 HG23 THR A 261 19.388 3.763 25.697 1.00 0.00 H ATOM 1384 N TYR A 262 19.674 0.942 22.464 1.00 21.58 N ANISOU 1384 N TYR A 262 2880 2978 2342 658 465 275 ATOM 1385 CA TYR A 262 18.661 -0.047 22.089 1.00 21.70 C ANISOU 1385 CA TYR A 262 2942 3007 2295 702 457 265 ATOM 1386 C TYR A 262 19.137 -1.506 22.254 1.00 18.65 C ANISOU 1386 C TYR A 262 2626 2619 1842 757 439 208 ATOM 1387 O TYR A 262 18.304 -2.372 22.519 1.00 25.08 O ANISOU 1387 O TYR A 262 3484 3457 2588 817 442 207 ATOM 1388 CB TYR A 262 18.174 0.249 20.652 1.00 22.79 C ANISOU 1388 CB TYR A 262 3084 3107 2468 651 417 245 ATOM 1389 CG TYR A 262 17.092 -0.684 20.130 1.00 28.16 C ANISOU 1389 CG TYR A 262 3808 3797 3093 688 403 238 ATOM 1390 CD1 TYR A 262 15.777 -0.588 20.626 1.00 32.40 C ANISOU 1390 CD1 TYR A 262 4328 4376 3604 720 436 300 ATOM 1391 CD2 TYR A 262 17.398 -1.662 19.161 1.00 24.51 C ANISOU 1391 CD2 TYR A 262 3404 3303 2608 690 355 176 ATOM 1392 CE1 TYR A 262 14.774 -1.459 20.156 1.00 31.99 C ANISOU 1392 CE1 TYR A 262 4320 4335 3500 754 421 294 ATOM 1393 CE2 TYR A 262 16.394 -2.524 18.680 1.00 27.83 C ANISOU 1393 CE2 TYR A 262 3867 3729 2980 722 335 169 ATOM 1394 CZ TYR A 262 15.081 -2.422 19.173 1.00 36.45 C ANISOU 1394 CZ TYR A 262 4944 4863 4041 755 370 226 ATOM 1395 OH TYR A 262 14.118 -3.260 18.692 1.00 45.95 O ANISOU 1395 OH TYR A 262 6193 6073 5193 790 349 220 ATOM 1396 H TYR A 262 20.102 1.453 21.703 1.00 0.00 H ATOM 1397 HA TYR A 262 17.807 0.088 22.757 1.00 0.00 H ATOM 1398 HB3 TYR A 262 19.022 0.223 19.964 1.00 0.00 H ATOM 1399 HB2 TYR A 262 17.786 1.268 20.603 1.00 0.00 H ATOM 1400 HD1 TYR A 262 15.537 0.157 21.371 1.00 0.00 H ATOM 1401 HD2 TYR A 262 18.402 -1.754 18.782 1.00 0.00 H ATOM 1402 HE1 TYR A 262 13.770 -1.379 20.545 1.00 0.00 H ATOM 1403 HE2 TYR A 262 16.631 -3.266 17.932 1.00 0.00 H ATOM 1404 HH TYR A 262 13.254 -3.146 19.103 1.00 0.00 H ATOM 1405 N ASN A 263 20.450 -1.747 22.102 1.00 16.55 N ANISOU 1405 N ASN A 263 2373 2322 1592 740 417 160 ATOM 1406 CA ASN A 263 21.066 -3.074 22.200 1.00 27.38 C ANISOU 1406 CA ASN A 263 3811 3680 2910 784 388 102 ATOM 1407 C ASN A 263 22.029 -3.107 23.395 1.00 27.11 C ANISOU 1407 C ASN A 263 3772 3668 2861 821 419 107 ATOM 1408 O ASN A 263 22.639 -2.087 23.716 1.00 26.19 O ANISOU 1408 O ASN A 263 3599 3557 2794 787 446 138 ATOM 1409 CB ASN A 263 21.835 -3.429 20.907 1.00 24.49 C ANISOU 1409 CB ASN A 263 3468 3256 2580 730 327 42 ATOM 1410 CG ASN A 263 20.997 -3.302 19.634 1.00 33.10 C ANISOU 1410 CG ASN A 263 4556 4326 3695 690 299 42 ATOM 1411 OD1 ASN A 263 20.305 -4.235 19.237 1.00 29.92 O ANISOU 1411 OD1 ASN A 263 4201 3916 3251 716 269 23 ATOM 1412 ND2 ASN A 263 21.071 -2.141 18.987 1.00 39.45 N ANISOU 1412 ND2 ASN A 263 5306 5118 4565 628 307 65 ATOM 1413 H ASN A 263 21.082 -0.980 21.919 1.00 0.00 H ATOM 1414 HA ASN A 263 20.321 -3.853 22.381 1.00 0.00 H ATOM 1415 HB3 ASN A 263 22.174 -4.462 20.967 1.00 0.00 H ATOM 1416 HB2 ASN A 263 22.733 -2.818 20.806 1.00 0.00 H ATOM 1417 HD22 ASN A 263 20.554 -1.999 18.130 1.00 0.00 H ATOM 1418 HD21 ASN A 263 21.655 -1.397 19.350 1.00 0.00 H ATOM 1419 N GLU A 264 22.152 -4.289 24.019 1.00 30.30 N ANISOU 1419 N GLU A 264 4238 4081 3194 893 412 75 ATOM 1420 CA GLU A 264 22.966 -4.525 25.214 1.00 23.91 C ANISOU 1420 CA GLU A 264 3431 3298 2357 946 443 80 ATOM 1421 C GLU A 264 24.486 -4.467 24.937 1.00 18.42 C ANISOU 1421 C GLU A 264 2731 2559 1708 900 414 38 ATOM 1422 O GLU A 264 24.898 -4.811 23.828 1.00 16.71 O ANISOU 1422 O GLU A 264 2535 2293 1522 850 360 -8 ATOM 1423 CB GLU A 264 22.608 -5.904 25.802 1.00 30.22 C ANISOU 1423 CB GLU A 264 4307 4115 3061 1043 437 52 ATOM 1424 CG GLU A 264 21.140 -6.021 26.256 1.00 34.17 C ANISOU 1424 CG GLU A 264 4814 4665 3503 1101 472 97 ATOM 1425 CD GLU A 264 20.870 -7.345 26.980 1.00 45.86 C ANISOU 1425 CD GLU A 264 6358 6183 4885 1215 490 86 ATOM 1426 OE1 GLU A 264 20.894 -8.392 26.294 1.00 36.99 O ANISOU 1426 OE1 GLU A 264 5318 5031 3706 1255 437 26 ATOM 1427 OE2 GLU A 264 20.644 -7.291 28.209 1.00 58.02 O1- ANISOU 1427 OE2 GLU A 264 7863 7778 6403 1266 554 140 ATOM 1428 H GLU A 264 21.623 -5.083 23.687 1.00 0.00 H ATOM 1429 HA GLU A 264 22.673 -3.759 25.930 1.00 0.00 H ATOM 1430 HB3 GLU A 264 23.260 -6.123 26.650 1.00 0.00 H ATOM 1431 HB2 GLU A 264 22.818 -6.678 25.061 1.00 0.00 H ATOM 1432 HG3 GLU A 264 20.468 -5.948 25.400 1.00 0.00 H ATOM 1433 HG2 GLU A 264 20.889 -5.184 26.911 1.00 0.00 H ATOM 1434 N PRO A 265 25.300 -4.116 25.964 1.00 20.08 N ANISOU 1434 N PRO A 265 2914 2789 1926 917 448 58 ATOM 1435 CA PRO A 265 26.765 -4.314 25.949 1.00 19.15 C ANISOU 1435 CA PRO A 265 2802 2632 1840 886 418 14 ATOM 1436 C PRO A 265 27.221 -5.736 25.569 1.00 24.22 C ANISOU 1436 C PRO A 265 3525 3238 2440 919 361 -55 ATOM 1437 O PRO A 265 26.777 -6.705 26.185 1.00 21.87 O ANISOU 1437 O PRO A 265 3284 2957 2070 995 358 -68 ATOM 1438 CB PRO A 265 27.201 -3.941 27.377 1.00 17.38 C ANISOU 1438 CB PRO A 265 2546 2448 1610 926 470 52 ATOM 1439 CG PRO A 265 26.149 -2.957 27.848 1.00 23.52 C ANISOU 1439 CG PRO A 265 3270 3279 2388 940 528 130 ATOM 1440 CD PRO A 265 24.873 -3.502 27.223 1.00 22.22 C ANISOU 1440 CD PRO A 265 3140 3122 2182 962 517 128 ATOM 1441 HA PRO A 265 27.182 -3.592 25.252 1.00 0.00 H ATOM 1442 HB3 PRO A 265 28.205 -3.517 27.410 1.00 0.00 H ATOM 1443 HB2 PRO A 265 27.191 -4.815 28.032 1.00 0.00 H ATOM 1444 HG3 PRO A 265 26.364 -1.971 27.432 1.00 0.00 H ATOM 1445 HG2 PRO A 265 26.095 -2.862 28.932 1.00 0.00 H ATOM 1446 HD2 PRO A 265 24.426 -4.267 27.861 1.00 0.00 H ATOM 1447 HD3 PRO A 265 24.154 -2.693 27.088 1.00 0.00 H ATOM 1448 N GLY A 266 28.091 -5.818 24.551 1.00 29.01 N ANISOU 1448 N GLY A 266 4137 3792 3092 860 310 -97 ATOM 1449 CA GLY A 266 28.687 -7.070 24.082 1.00 29.09 C ANISOU 1449 CA GLY A 266 4218 3759 3077 879 245 -158 ATOM 1450 C GLY A 266 27.882 -7.734 22.954 1.00 23.08 C ANISOU 1450 C GLY A 266 3498 2972 2300 871 196 -181 ATOM 1451 O GLY A 266 28.386 -8.692 22.366 1.00 22.09 O ANISOU 1451 O GLY A 266 3424 2800 2169 870 129 -228 ATOM 1452 H GLY A 266 28.389 -4.970 24.090 1.00 0.00 H ATOM 1453 HA3 GLY A 266 28.808 -7.779 24.904 1.00 0.00 H ATOM 1454 HA2 GLY A 266 29.688 -6.850 23.711 1.00 0.00 H ATOM 1455 N SER A 267 26.679 -7.229 22.613 1.00 19.32 N ANISOU 1455 N SER A 267 3002 2523 1817 868 221 -147 ATOM 1456 CA SER A 267 25.929 -7.630 21.416 1.00 18.22 C ANISOU 1456 CA SER A 267 2890 2356 1676 847 174 -164 ATOM 1457 C SER A 267 26.635 -7.143 20.136 1.00 20.89 C ANISOU 1457 C SER A 267 3197 2651 2091 758 135 -177 ATOM 1458 O SER A 267 27.408 -6.186 20.196 1.00 15.73 O ANISOU 1458 O SER A 267 2488 1998 1490 711 159 -161 ATOM 1459 CB SER A 267 24.474 -7.121 21.514 1.00 20.08 C ANISOU 1459 CB SER A 267 3100 2632 1897 855 215 -118 ATOM 1460 OG SER A 267 24.357 -5.743 21.222 1.00 22.69 O ANISOU 1460 OG SER A 267 3355 2976 2292 794 254 -76 ATOM 1461 H SER A 267 26.302 -6.451 23.136 1.00 0.00 H ATOM 1462 HA SER A 267 25.900 -8.722 21.399 1.00 0.00 H ATOM 1463 HB3 SER A 267 24.060 -7.316 22.505 1.00 0.00 H ATOM 1464 HB2 SER A 267 23.847 -7.663 20.805 1.00 0.00 H ATOM 1465 HG SER A 267 24.581 -5.251 22.021 1.00 0.00 H ATOM 1466 N GLN A 268 26.367 -7.807 19.000 1.00 19.61 N ANISOU 1466 N GLN A 268 3068 2450 1933 739 73 -204 ATOM 1467 CA GLN A 268 27.064 -7.527 17.742 1.00 15.69 C ANISOU 1467 CA GLN A 268 2540 1914 1506 662 36 -213 ATOM 1468 C GLN A 268 26.804 -6.110 17.194 1.00 23.10 C ANISOU 1468 C GLN A 268 3408 2871 2496 607 80 -174 ATOM 1469 O GLN A 268 27.740 -5.505 16.680 1.00 14.79 O ANISOU 1469 O GLN A 268 2315 1807 1499 555 81 -172 ATOM 1470 CB GLN A 268 26.744 -8.625 16.703 1.00 24.74 C ANISOU 1470 CB GLN A 268 3729 3020 2651 652 -36 -236 ATOM 1471 CG GLN A 268 27.682 -8.636 15.475 1.00 25.27 C ANISOU 1471 CG GLN A 268 3774 3044 2784 586 -85 -247 ATOM 1472 CD GLN A 268 29.141 -8.923 15.853 1.00 31.01 C ANISOU 1472 CD GLN A 268 4507 3751 3524 585 -101 -268 ATOM 1473 OE1 GLN A 268 29.435 -9.939 16.480 1.00 30.70 O ANISOU 1473 OE1 GLN A 268 4417 3713 3534 539 -81 -256 ATOM 1474 NE2 GLN A 268 30.063 -8.032 15.485 1.00 26.50 N ANISOU 1474 NE2 GLN A 268 4000 3162 2907 638 -138 -300 ATOM 1475 H GLN A 268 25.717 -8.580 18.999 1.00 0.00 H ATOM 1476 HA GLN A 268 28.126 -7.576 17.977 1.00 0.00 H ATOM 1477 HB3 GLN A 268 25.711 -8.524 16.369 1.00 0.00 H ATOM 1478 HB2 GLN A 268 26.799 -9.603 17.187 1.00 0.00 H ATOM 1479 HG3 GLN A 268 27.610 -7.695 14.929 1.00 0.00 H ATOM 1480 HG2 GLN A 268 27.360 -9.413 14.781 1.00 0.00 H ATOM 1481 HE22 GLN A 268 31.034 -8.186 15.714 1.00 0.00 H ATOM 1482 HE21 GLN A 268 29.806 -7.174 15.006 1.00 0.00 H ATOM 1483 N VAL A 269 25.579 -5.586 17.371 1.00 22.83 N ANISOU 1483 N VAL A 269 3361 2869 2446 620 114 -143 ATOM 1484 CA VAL A 269 25.201 -4.227 16.971 1.00 18.51 C ANISOU 1484 CA VAL A 269 2750 2332 1949 570 149 -108 ATOM 1485 C VAL A 269 25.842 -3.145 17.872 1.00 14.72 C ANISOU 1485 C VAL A 269 2226 1871 1496 557 193 -89 ATOM 1486 O VAL A 269 26.214 -2.091 17.358 1.00 20.06 O ANISOU 1486 O VAL A 269 2859 2535 2226 505 198 -82 ATOM 1487 CB VAL A 269 23.658 -4.043 16.972 1.00 17.60 C ANISOU 1487 CB VAL A 269 2629 2245 1812 589 174 -74 ATOM 1488 CG1 VAL A 269 23.201 -2.628 16.565 1.00 14.78 C ANISOU 1488 CG1 VAL A 269 2211 1892 1514 535 199 -42 ATOM 1489 CG2 VAL A 269 22.964 -5.072 16.061 1.00 19.60 C ANISOU 1489 CG2 VAL A 269 2929 2480 2036 603 127 -93 ATOM 1490 H VAL A 269 24.861 -6.136 17.822 1.00 0.00 H ATOM 1491 HA VAL A 269 25.562 -4.066 15.952 1.00 0.00 H ATOM 1492 HB VAL A 269 23.293 -4.222 17.985 1.00 0.00 H ATOM 1493 HG11 VAL A 269 22.123 -2.594 16.428 1.00 0.00 H ATOM 1494 HG12 VAL A 269 23.448 -1.881 17.318 1.00 0.00 H ATOM 1495 HG13 VAL A 269 23.651 -2.325 15.621 1.00 0.00 H ATOM 1496 HG21 VAL A 269 21.884 -4.923 16.044 1.00 0.00 H ATOM 1497 HG22 VAL A 269 23.328 -4.993 15.036 1.00 0.00 H ATOM 1498 HG23 VAL A 269 23.138 -6.095 16.397 1.00 0.00 H ATOM 1499 N PHE A 270 26.010 -3.436 19.177 1.00 16.08 N ANISOU 1499 N PHE A 270 2406 2074 1629 609 228 -76 ATOM 1500 CA PHE A 270 26.732 -2.589 20.135 1.00 14.91 C ANISOU 1500 CA PHE A 270 2217 1944 1505 602 268 -54 ATOM 1501 C PHE A 270 28.232 -2.489 19.791 1.00 20.52 C ANISOU 1501 C PHE A 270 2922 2622 2252 564 241 -85 ATOM 1502 O PHE A 270 28.792 -1.395 19.855 1.00 18.82 O ANISOU 1502 O PHE A 270 2662 2403 2087 518 253 -72 ATOM 1503 CB PHE A 270 26.486 -3.129 21.566 1.00 15.42 C ANISOU 1503 CB PHE A 270 2300 2046 1511 674 303 -38 ATOM 1504 CG PHE A 270 27.060 -2.339 22.735 1.00 22.92 C ANISOU 1504 CG PHE A 270 3203 3024 2483 675 350 -1 ATOM 1505 CD1 PHE A 270 28.442 -2.352 23.024 1.00 21.02 C ANISOU 1505 CD1 PHE A 270 2958 2767 2261 664 342 -23 ATOM 1506 CD2 PHE A 270 26.211 -1.530 23.520 1.00 24.92 C ANISOU 1506 CD2 PHE A 270 3414 3318 2736 690 399 59 ATOM 1507 CE1 PHE A 270 28.943 -1.584 24.068 1.00 25.49 C ANISOU 1507 CE1 PHE A 270 3481 3357 2848 666 382 13 ATOM 1508 CE2 PHE A 270 26.729 -0.773 24.563 1.00 21.64 C ANISOU 1508 CE2 PHE A 270 2952 2927 2344 691 438 100 ATOM 1509 CZ PHE A 270 28.090 -0.798 24.833 1.00 20.38 C ANISOU 1509 CZ PHE A 270 2791 2750 2203 679 430 75 ATOM 1510 H PHE A 270 25.687 -4.327 19.529 1.00 0.00 H ATOM 1511 HA PHE A 270 26.306 -1.584 20.077 1.00 0.00 H ATOM 1512 HB3 PHE A 270 26.862 -4.148 21.649 1.00 0.00 H ATOM 1513 HB2 PHE A 270 25.409 -3.203 21.719 1.00 0.00 H ATOM 1514 HD1 PHE A 270 29.117 -2.963 22.442 1.00 0.00 H ATOM 1515 HD2 PHE A 270 25.150 -1.514 23.331 1.00 0.00 H ATOM 1516 HE1 PHE A 270 29.999 -1.603 24.291 1.00 0.00 H ATOM 1517 HE2 PHE A 270 26.069 -0.168 25.166 1.00 0.00 H ATOM 1518 HZ PHE A 270 28.486 -0.208 25.647 1.00 0.00 H ATOM 1519 N LYS A 271 28.843 -3.628 19.415 1.00 22.79 N ANISOU 1519 N LYS A 271 3257 2884 2516 582 198 -126 ATOM 1520 CA LYS A 271 30.244 -3.728 19.005 1.00 21.36 C ANISOU 1520 CA LYS A 271 3073 2673 2371 548 170 -152 ATOM 1521 C LYS A 271 30.522 -3.049 17.655 1.00 19.81 C ANISOU 1521 C LYS A 271 2844 2452 2229 482 148 -153 ATOM 1522 O LYS A 271 31.489 -2.296 17.572 1.00 14.83 O ANISOU 1522 O LYS A 271 2180 1815 1638 444 154 -151 ATOM 1523 CB LYS A 271 30.692 -5.204 18.990 1.00 29.00 C ANISOU 1523 CB LYS A 271 4100 3612 3305 581 119 -193 ATOM 1524 CG LYS A 271 30.808 -5.820 20.399 1.00 26.22 C ANISOU 1524 CG LYS A 271 3785 3281 2895 655 137 -199 ATOM 1525 CD LYS A 271 31.326 -7.270 20.414 1.00 33.18 C ANISOU 1525 CD LYS A 271 4723 4124 3762 676 78 -244 ATOM 1526 CE LYS A 271 30.459 -8.252 19.606 1.00 28.91 C ANISOU 1526 CE LYS A 271 4244 3558 3183 705 23 -271 ATOM 1527 NZ LYS A 271 30.898 -9.649 19.772 1.00 30.37 N1+ ANISOU 1527 NZ LYS A 271 4486 3695 3358 723 -47 -314 ATOM 1528 H LYS A 271 28.313 -4.490 19.399 1.00 0.00 H ATOM 1529 HA LYS A 271 30.837 -3.204 19.758 1.00 0.00 H ATOM 1530 HB3 LYS A 271 31.671 -5.276 18.514 1.00 0.00 H ATOM 1531 HB2 LYS A 271 30.007 -5.782 18.369 1.00 0.00 H ATOM 1532 HG3 LYS A 271 29.847 -5.776 20.910 1.00 0.00 H ATOM 1533 HG2 LYS A 271 31.483 -5.207 20.997 1.00 0.00 H ATOM 1534 HD3 LYS A 271 31.383 -7.600 21.453 1.00 0.00 H ATOM 1535 HD2 LYS A 271 32.350 -7.285 20.037 1.00 0.00 H ATOM 1536 HE3 LYS A 271 30.493 -8.012 18.544 1.00 0.00 H ATOM 1537 HE2 LYS A 271 29.419 -8.184 19.921 1.00 0.00 H ATOM 1538 HZ1 LYS A 271 30.814 -9.915 20.743 1.00 0.00 H ATOM 1539 HZ2 LYS A 271 30.315 -10.250 19.208 1.00 0.00 H ATOM 1540 HZ3 LYS A 271 31.859 -9.743 19.476 1.00 0.00 H ATOM 1541 N ASP A 272 29.660 -3.280 16.646 1.00 16.24 N ANISOU 1541 N ASP A 272 2404 1990 1777 471 124 -154 ATOM 1542 CA ASP A 272 29.729 -2.630 15.328 1.00 16.70 C ANISOU 1542 CA ASP A 272 2430 2030 1884 416 109 -150 ATOM 1543 C ASP A 272 29.532 -1.105 15.391 1.00 21.51 C ANISOU 1543 C ASP A 272 2989 2657 2525 389 152 -122 ATOM 1544 O ASP A 272 30.138 -0.403 14.584 1.00 15.66 O ANISOU 1544 O ASP A 272 2219 1906 1826 348 148 -122 ATOM 1545 CB ASP A 272 28.756 -3.219 14.277 1.00 15.76 C ANISOU 1545 CB ASP A 272 2331 1899 1757 415 77 -152 ATOM 1546 CG ASP A 272 28.937 -4.695 13.884 1.00 19.68 C ANISOU 1546 CG ASP A 272 2871 2363 2242 424 17 -179 ATOM 1547 OD1 ASP A 272 30.013 -5.276 14.149 1.00 23.87 O ANISOU 1547 OD1 ASP A 272 3415 2878 2775 427 -3 -198 ATOM 1548 OD2 ASP A 272 28.014 -5.207 13.214 1.00 29.49 O1- ANISOU 1548 OD2 ASP A 272 4135 3594 3478 425 -16 -180 ATOM 1549 H ASP A 272 28.900 -3.935 16.776 1.00 0.00 H ATOM 1550 HA ASP A 272 30.742 -2.793 14.958 1.00 0.00 H ATOM 1551 HB3 ASP A 272 28.829 -2.639 13.355 1.00 0.00 H ATOM 1552 HB2 ASP A 272 27.736 -3.106 14.647 1.00 0.00 H ATOM 1553 N ALA A 273 28.731 -0.617 16.355 1.00 13.54 N ANISOU 1553 N ALA A 273 1969 1676 1498 412 190 -96 ATOM 1554 CA ALA A 273 28.542 0.808 16.626 1.00 13.35 C ANISOU 1554 CA ALA A 273 1900 1664 1510 386 222 -67 ATOM 1555 C ALA A 273 29.824 1.500 17.120 1.00 13.15 C ANISOU 1555 C ALA A 273 1851 1636 1510 368 233 -70 ATOM 1556 O ALA A 273 30.136 2.579 16.621 1.00 24.30 O ANISOU 1556 O ALA A 273 3234 3037 2960 331 234 -66 ATOM 1557 CB ALA A 273 27.390 0.992 17.621 1.00 13.64 C ANISOU 1557 CB ALA A 273 1927 1731 1525 415 258 -29 ATOM 1558 H ALA A 273 28.241 -1.257 16.966 1.00 0.00 H ATOM 1559 HA ALA A 273 28.249 1.287 15.689 1.00 0.00 H ATOM 1560 HB1 ALA A 273 27.255 2.040 17.884 1.00 0.00 H ATOM 1561 HB2 ALA A 273 26.457 0.634 17.190 1.00 0.00 H ATOM 1562 HB3 ALA A 273 27.558 0.444 18.547 1.00 0.00 H ATOM 1563 N ASN A 274 30.565 0.846 18.036 1.00 17.96 N ANISOU 1563 N ASN A 274 2476 2253 2095 396 239 -77 ATOM 1564 CA ASN A 274 31.889 1.283 18.503 1.00 17.19 C ANISOU 1564 CA ASN A 274 2358 2152 2022 378 245 -81 ATOM 1565 C ASN A 274 32.957 1.195 17.403 1.00 16.24 C ANISOU 1565 C ASN A 274 2238 2004 1927 342 213 -108 ATOM 1566 O ASN A 274 33.789 2.096 17.327 1.00 18.94 O ANISOU 1566 O ASN A 274 2552 2341 2302 311 217 -105 ATOM 1567 CB ASN A 274 32.322 0.450 19.730 1.00 15.62 C ANISOU 1567 CB ASN A 274 2177 1966 1791 420 257 -84 ATOM 1568 CG ASN A 274 31.585 0.830 21.014 1.00 24.78 C ANISOU 1568 CG ASN A 274 3313 3160 2944 445 301 -43 ATOM 1569 OD1 ASN A 274 31.605 1.990 21.422 1.00 21.37 O ANISOU 1569 OD1 ASN A 274 2840 2732 2548 416 318 -14 ATOM 1570 ND2 ASN A 274 30.955 -0.145 21.670 1.00 25.91 N ANISOU 1570 ND2 ASN A 274 3482 3325 3040 502 317 -38 ATOM 1571 H ASN A 274 30.239 -0.044 18.388 1.00 0.00 H ATOM 1572 HA ASN A 274 31.766 2.328 18.800 1.00 0.00 H ATOM 1573 HB3 ASN A 274 33.380 0.621 19.936 1.00 0.00 H ATOM 1574 HB2 ASN A 274 32.224 -0.618 19.529 1.00 0.00 H ATOM 1575 HD22 ASN A 274 30.466 0.049 22.531 1.00 0.00 H ATOM 1576 HD21 ASN A 274 30.936 -1.082 21.293 1.00 0.00 H ATOM 1577 N SER A 275 32.907 0.148 16.560 1.00 19.62 N ANISOU 1577 N SER A 275 2698 2415 2342 348 177 -131 ATOM 1578 CA SER A 275 33.818 -0.038 15.428 1.00 18.63 C ANISOU 1578 CA SER A 275 2567 2266 2244 315 145 -147 ATOM 1579 C SER A 275 33.648 1.042 14.340 1.00 20.83 C ANISOU 1579 C SER A 275 2814 2544 2555 280 152 -135 ATOM 1580 O SER A 275 34.644 1.440 13.741 1.00 12.26 O ANISOU 1580 O SER A 275 1711 1453 1496 254 146 -138 ATOM 1581 CB SER A 275 33.626 -1.439 14.823 1.00 13.84 C ANISOU 1581 CB SER A 275 1996 1639 1623 324 100 -164 ATOM 1582 OG SER A 275 33.990 -2.452 15.736 1.00 17.65 O ANISOU 1582 OG SER A 275 2516 2116 2074 360 85 -182 ATOM 1583 H SER A 275 32.219 -0.581 16.701 1.00 0.00 H ATOM 1584 HA SER A 275 34.840 0.035 15.805 1.00 0.00 H ATOM 1585 HB3 SER A 275 34.240 -1.560 13.930 1.00 0.00 H ATOM 1586 HB2 SER A 275 32.592 -1.592 14.525 1.00 0.00 H ATOM 1587 HG SER A 275 34.906 -2.327 16.001 1.00 0.00 H ATOM 1588 N ILE A 276 32.410 1.525 14.132 1.00 15.89 N ANISOU 1588 N ILE A 276 2184 1925 1927 282 163 -122 ATOM 1589 CA ILE A 276 32.083 2.630 13.225 1.00 20.61 C ANISOU 1589 CA ILE A 276 2756 2521 2554 256 169 -112 ATOM 1590 C ILE A 276 32.571 3.999 13.744 1.00 19.18 C ANISOU 1590 C ILE A 276 2549 2345 2394 242 191 -105 ATOM 1591 O ILE A 276 33.036 4.797 12.930 1.00 20.19 O ANISOU 1591 O ILE A 276 2662 2467 2544 221 188 -109 ATOM 1592 CB ILE A 276 30.561 2.658 12.886 1.00 24.84 C ANISOU 1592 CB ILE A 276 3294 3061 3084 264 174 -98 ATOM 1593 CG1 ILE A 276 30.239 1.493 11.922 1.00 36.61 C ANISOU 1593 CG1 ILE A 276 4808 4542 4562 270 143 -106 ATOM 1594 CG2 ILE A 276 30.015 3.991 12.317 1.00 20.82 C ANISOU 1594 CG2 ILE A 276 2758 2548 2604 242 183 -88 ATOM 1595 CD1 ILE A 276 28.746 1.196 11.758 1.00 39.72 C ANISOU 1595 CD1 ILE A 276 5196 4934 4962 266 142 -93 ATOM 1596 H ILE A 276 31.632 1.129 14.643 1.00 0.00 H ATOM 1597 HA ILE A 276 32.623 2.448 12.292 1.00 0.00 H ATOM 1598 HB ILE A 276 30.019 2.469 13.815 1.00 0.00 H ATOM 1599 HG13 ILE A 276 30.724 0.580 12.263 1.00 0.00 H ATOM 1600 HG12 ILE A 276 30.675 1.691 10.945 1.00 0.00 H ATOM 1601 HG21 ILE A 276 28.964 3.909 12.042 1.00 0.00 H ATOM 1602 HG22 ILE A 276 30.074 4.804 13.041 1.00 0.00 H ATOM 1603 HG23 ILE A 276 30.564 4.296 11.427 1.00 0.00 H ATOM 1604 HD11 ILE A 276 28.599 0.140 11.530 1.00 0.00 H ATOM 1605 HD12 ILE A 276 28.186 1.417 12.667 1.00 0.00 H ATOM 1606 HD13 ILE A 276 28.312 1.776 10.943 1.00 0.00 H ATOM 1607 N LYS A 277 32.524 4.224 15.075 1.00 23.23 N ANISOU 1607 N LYS A 277 3058 2871 2899 256 213 -90 ATOM 1608 CA LYS A 277 33.163 5.379 15.718 1.00 21.84 C ANISOU 1608 CA LYS A 277 2858 2696 2745 242 227 -80 ATOM 1609 C LYS A 277 34.688 5.346 15.560 1.00 22.48 C ANISOU 1609 C LYS A 277 2937 2770 2833 230 218 -98 ATOM 1610 O LYS A 277 35.270 6.365 15.196 1.00 19.34 O ANISOU 1610 O LYS A 277 2525 2366 2458 210 215 -101 ATOM 1611 CB LYS A 277 32.829 5.466 17.222 1.00 24.14 C ANISOU 1611 CB LYS A 277 3142 3005 3027 262 251 -53 ATOM 1612 CG LYS A 277 31.358 5.749 17.548 1.00 29.17 C ANISOU 1612 CG LYS A 277 3761 3647 3674 262 264 -21 ATOM 1613 CD LYS A 277 31.152 6.209 19.002 1.00 26.85 C ANISOU 1613 CD LYS A 277 3448 3373 3380 277 289 14 ATOM 1614 CE LYS A 277 31.536 7.685 19.190 1.00 20.70 C ANISOU 1614 CE LYS A 277 2641 2584 2642 250 287 29 ATOM 1615 NZ LYS A 277 31.261 8.179 20.549 1.00 23.69 N1+ ANISOU 1615 NZ LYS A 277 2991 2982 3027 263 310 78 ATOM 1616 H LYS A 277 32.121 3.528 15.688 1.00 0.00 H ATOM 1617 HA LYS A 277 32.792 6.284 15.231 1.00 0.00 H ATOM 1618 HB3 LYS A 277 33.431 6.274 17.639 1.00 0.00 H ATOM 1619 HB2 LYS A 277 33.149 4.566 17.747 1.00 0.00 H ATOM 1620 HG3 LYS A 277 30.783 4.843 17.381 1.00 0.00 H ATOM 1621 HG2 LYS A 277 30.950 6.492 16.860 1.00 0.00 H ATOM 1622 HD3 LYS A 277 31.747 5.581 19.668 1.00 0.00 H ATOM 1623 HD2 LYS A 277 30.113 6.050 19.291 1.00 0.00 H ATOM 1624 HE3 LYS A 277 30.962 8.278 18.482 1.00 0.00 H ATOM 1625 HE2 LYS A 277 32.588 7.855 18.970 1.00 0.00 H ATOM 1626 HZ1 LYS A 277 31.821 7.671 21.219 1.00 0.00 H ATOM 1627 HZ2 LYS A 277 31.496 9.162 20.590 1.00 0.00 H ATOM 1628 HZ3 LYS A 277 30.281 8.064 20.761 1.00 0.00 H ATOM 1629 N LYS A 278 35.291 4.173 15.820 1.00 15.20 N ANISOU 1629 N LYS A 278 2034 1849 1891 245 209 -111 ATOM 1630 CA LYS A 278 36.728 3.922 15.751 1.00 17.75 C ANISOU 1630 CA LYS A 278 2355 2166 2223 233 198 -125 ATOM 1631 C LYS A 278 37.307 4.226 14.364 1.00 18.04 C ANISOU 1631 C LYS A 278 2383 2194 2278 209 182 -132 ATOM 1632 O LYS A 278 38.255 4.999 14.274 1.00 18.04 O ANISOU 1632 O LYS A 278 2367 2193 2292 194 184 -134 ATOM 1633 CB LYS A 278 37.004 2.467 16.183 1.00 20.41 C ANISOU 1633 CB LYS A 278 2718 2498 2537 254 181 -138 ATOM 1634 CG LYS A 278 38.482 2.163 16.475 1.00 18.30 C ANISOU 1634 CG LYS A 278 2449 2226 2279 247 173 -148 ATOM 1635 CD LYS A 278 38.768 0.674 16.728 1.00 18.75 C ANISOU 1635 CD LYS A 278 2535 2268 2320 264 143 -164 ATOM 1636 CE LYS A 278 38.726 -0.187 15.453 1.00 21.21 C ANISOU 1636 CE LYS A 278 2851 2563 2644 245 108 -169 ATOM 1637 NZ LYS A 278 39.048 -1.598 15.738 1.00 31.31 N1+ ANISOU 1637 NZ LYS A 278 4166 3824 3907 264 70 -183 ATOM 1638 H LYS A 278 34.726 3.390 16.124 1.00 0.00 H ATOM 1639 HA LYS A 278 37.213 4.602 16.450 1.00 0.00 H ATOM 1640 HB3 LYS A 278 36.617 1.783 15.429 1.00 0.00 H ATOM 1641 HB2 LYS A 278 36.443 2.249 17.089 1.00 0.00 H ATOM 1642 HG3 LYS A 278 38.774 2.733 17.357 1.00 0.00 H ATOM 1643 HG2 LYS A 278 39.115 2.517 15.663 1.00 0.00 H ATOM 1644 HD3 LYS A 278 38.039 0.296 17.444 1.00 0.00 H ATOM 1645 HD2 LYS A 278 39.743 0.580 17.209 1.00 0.00 H ATOM 1646 HE3 LYS A 278 39.438 0.192 14.719 1.00 0.00 H ATOM 1647 HE2 LYS A 278 37.738 -0.151 14.993 1.00 0.00 H ATOM 1648 HZ1 LYS A 278 38.366 -1.973 16.387 1.00 0.00 H ATOM 1649 HZ2 LYS A 278 39.021 -2.135 14.883 1.00 0.00 H ATOM 1650 HZ3 LYS A 278 39.968 -1.663 16.149 1.00 0.00 H ATOM 1651 N ILE A 279 36.684 3.663 13.318 1.00 15.44 N ANISOU 1651 N ILE A 279 2062 1860 1946 209 167 -134 ATOM 1652 CA ILE A 279 37.028 3.886 11.915 1.00 17.59 C ANISOU 1652 CA ILE A 279 2321 2129 2235 192 156 -134 ATOM 1653 C ILE A 279 36.848 5.351 11.458 1.00 14.17 C ANISOU 1653 C ILE A 279 1870 1699 1814 184 172 -130 ATOM 1654 O ILE A 279 37.700 5.845 10.719 1.00 14.67 O ANISOU 1654 O ILE A 279 1922 1766 1887 175 172 -132 ATOM 1655 CB ILE A 279 36.219 2.916 11.004 1.00 18.63 C ANISOU 1655 CB ILE A 279 2461 2253 2364 194 136 -131 ATOM 1656 CG1 ILE A 279 36.706 1.453 11.159 1.00 22.42 C ANISOU 1656 CG1 ILE A 279 2963 2722 2835 201 106 -138 ATOM 1657 CG2 ILE A 279 36.119 3.299 9.514 1.00 13.04 C ANISOU 1657 CG2 ILE A 279 1733 1548 1675 181 131 -122 ATOM 1658 CD1 ILE A 279 38.144 1.177 10.689 1.00 22.31 C ANISOU 1658 CD1 ILE A 279 2940 2704 2834 188 93 -139 ATOM 1659 H ILE A 279 35.904 3.041 13.486 1.00 0.00 H ATOM 1660 HA ILE A 279 38.091 3.660 11.810 1.00 0.00 H ATOM 1661 HB ILE A 279 35.191 2.924 11.372 1.00 0.00 H ATOM 1662 HG13 ILE A 279 36.020 0.784 10.639 1.00 0.00 H ATOM 1663 HG12 ILE A 279 36.648 1.160 12.207 1.00 0.00 H ATOM 1664 HG21 ILE A 279 35.606 2.512 8.967 1.00 0.00 H ATOM 1665 HG22 ILE A 279 35.542 4.212 9.361 1.00 0.00 H ATOM 1666 HG23 ILE A 279 37.096 3.442 9.054 1.00 0.00 H ATOM 1667 HD11 ILE A 279 38.241 0.153 10.325 1.00 0.00 H ATOM 1668 HD12 ILE A 279 38.458 1.838 9.882 1.00 0.00 H ATOM 1669 HD13 ILE A 279 38.851 1.301 11.509 1.00 0.00 H ATOM 1670 N PHE A 280 35.786 6.027 11.938 1.00 11.75 N ANISOU 1670 N PHE A 280 1564 1392 1509 189 184 -124 ATOM 1671 CA PHE A 280 35.545 7.452 11.698 1.00 16.30 C ANISOU 1671 CA PHE A 280 2129 1964 2099 183 191 -122 ATOM 1672 C PHE A 280 36.624 8.360 12.313 1.00 16.05 C ANISOU 1672 C PHE A 280 2091 1931 2075 175 194 -126 ATOM 1673 O PHE A 280 37.174 9.194 11.597 1.00 14.41 O ANISOU 1673 O PHE A 280 1880 1722 1874 172 191 -134 ATOM 1674 CB PHE A 280 34.113 7.848 12.127 1.00 17.35 C ANISOU 1674 CB PHE A 280 2262 2093 2236 187 198 -109 ATOM 1675 CG PHE A 280 33.797 9.338 12.081 1.00 16.38 C ANISOU 1675 CG PHE A 280 2132 1958 2132 181 196 -106 ATOM 1676 CD1 PHE A 280 33.507 9.966 10.851 1.00 13.14 C ANISOU 1676 CD1 PHE A 280 1724 1541 1728 183 189 -112 ATOM 1677 CD2 PHE A 280 33.965 10.137 13.232 1.00 17.12 C ANISOU 1677 CD2 PHE A 280 2219 2046 2240 174 197 -96 ATOM 1678 CE1 PHE A 280 33.331 11.344 10.798 1.00 20.47 C ANISOU 1678 CE1 PHE A 280 2652 2453 2673 182 181 -114 ATOM 1679 CE2 PHE A 280 33.803 11.514 13.154 1.00 18.59 C ANISOU 1679 CE2 PHE A 280 2402 2214 2447 167 184 -95 ATOM 1680 CZ PHE A 280 33.481 12.114 11.943 1.00 20.35 C ANISOU 1680 CZ PHE A 280 2633 2426 2673 172 175 -107 ATOM 1681 H PHE A 280 35.123 5.556 12.539 1.00 0.00 H ATOM 1682 HA PHE A 280 35.597 7.603 10.617 1.00 0.00 H ATOM 1683 HB3 PHE A 280 33.907 7.481 13.134 1.00 0.00 H ATOM 1684 HB2 PHE A 280 33.402 7.338 11.478 1.00 0.00 H ATOM 1685 HD1 PHE A 280 33.424 9.379 9.949 1.00 0.00 H ATOM 1686 HD2 PHE A 280 34.234 9.682 14.174 1.00 0.00 H ATOM 1687 HE1 PHE A 280 33.092 11.822 9.861 1.00 0.00 H ATOM 1688 HE2 PHE A 280 33.935 12.118 14.039 1.00 0.00 H ATOM 1689 HZ PHE A 280 33.354 13.186 11.887 1.00 0.00 H ATOM 1690 N TYR A 281 36.904 8.176 13.616 1.00 17.86 N ANISOU 1690 N TYR A 281 2320 2164 2302 176 201 -120 ATOM 1691 CA TYR A 281 37.871 8.976 14.370 1.00 14.72 C ANISOU 1691 CA TYR A 281 1914 1763 1916 167 201 -120 ATOM 1692 C TYR A 281 39.341 8.693 14.010 1.00 15.98 C ANISOU 1692 C TYR A 281 2073 1926 2070 162 194 -134 ATOM 1693 O TYR A 281 40.153 9.611 14.131 1.00 18.31 O ANISOU 1693 O TYR A 281 2366 2220 2373 156 190 -139 ATOM 1694 CB TYR A 281 37.591 8.871 15.887 1.00 15.62 C ANISOU 1694 CB TYR A 281 2021 1881 2032 171 212 -103 ATOM 1695 CG TYR A 281 36.444 9.758 16.349 1.00 18.45 C ANISOU 1695 CG TYR A 281 2370 2234 2406 170 215 -81 ATOM 1696 CD1 TYR A 281 36.604 11.159 16.319 1.00 19.73 C ANISOU 1696 CD1 TYR A 281 2525 2379 2591 155 201 -78 ATOM 1697 CD2 TYR A 281 35.223 9.210 16.794 1.00 21.62 C ANISOU 1697 CD2 TYR A 281 2772 2646 2798 184 228 -62 ATOM 1698 CE1 TYR A 281 35.545 12.007 16.695 1.00 18.88 C ANISOU 1698 CE1 TYR A 281 2407 2262 2505 150 197 -53 ATOM 1699 CE2 TYR A 281 34.162 10.057 17.168 1.00 17.18 C ANISOU 1699 CE2 TYR A 281 2196 2080 2253 181 230 -35 ATOM 1700 CZ TYR A 281 34.320 11.456 17.114 1.00 16.40 C ANISOU 1700 CZ TYR A 281 2086 1960 2184 162 213 -29 ATOM 1701 OH TYR A 281 33.300 12.288 17.470 1.00 19.56 O ANISOU 1701 OH TYR A 281 2472 2351 2609 155 208 2 ATOM 1702 H TYR A 281 36.403 7.469 14.140 1.00 0.00 H ATOM 1703 HA TYR A 281 37.689 10.011 14.084 1.00 0.00 H ATOM 1704 HB3 TYR A 281 38.462 9.213 16.447 1.00 0.00 H ATOM 1705 HB2 TYR A 281 37.432 7.834 16.188 1.00 0.00 H ATOM 1706 HD1 TYR A 281 37.542 11.586 15.998 1.00 0.00 H ATOM 1707 HD2 TYR A 281 35.092 8.143 16.861 1.00 0.00 H ATOM 1708 HE1 TYR A 281 35.674 13.079 16.660 1.00 0.00 H ATOM 1709 HE2 TYR A 281 33.228 9.628 17.496 1.00 0.00 H ATOM 1710 HH TYR A 281 32.495 11.827 17.739 1.00 0.00 H ATOM 1711 N MET A 282 39.656 7.475 13.531 1.00 18.02 N ANISOU 1711 N MET A 282 2338 2191 2319 166 190 -137 ATOM 1712 CA MET A 282 40.958 7.132 12.950 1.00 17.21 C ANISOU 1712 CA MET A 282 2231 2093 2217 160 182 -142 ATOM 1713 C MET A 282 41.192 7.844 11.608 1.00 18.29 C ANISOU 1713 C MET A 282 2360 2234 2354 158 181 -143 ATOM 1714 O MET A 282 42.270 8.403 11.421 1.00 20.05 O ANISOU 1714 O MET A 282 2579 2463 2578 156 182 -146 ATOM 1715 CB MET A 282 41.094 5.606 12.775 1.00 18.82 C ANISOU 1715 CB MET A 282 2442 2295 2415 162 168 -141 ATOM 1716 CG MET A 282 41.388 4.856 14.082 1.00 19.43 C ANISOU 1716 CG MET A 282 2528 2368 2485 169 166 -145 ATOM 1717 SD MET A 282 41.348 3.050 13.918 1.00 19.47 S ANISOU 1717 SD MET A 282 2551 2363 2484 176 138 -149 ATOM 1718 CE MET A 282 42.925 2.775 13.068 1.00 20.35 C ANISOU 1718 CE MET A 282 2645 2474 2612 155 121 -142 ATOM 1719 H MET A 282 38.948 6.754 13.494 1.00 0.00 H ATOM 1720 HA MET A 282 41.742 7.468 13.634 1.00 0.00 H ATOM 1721 HB3 MET A 282 41.909 5.394 12.082 1.00 0.00 H ATOM 1722 HB2 MET A 282 40.197 5.199 12.305 1.00 0.00 H ATOM 1723 HG3 MET A 282 40.688 5.146 14.864 1.00 0.00 H ATOM 1724 HG2 MET A 282 42.371 5.142 14.448 1.00 0.00 H ATOM 1725 HE1 MET A 282 43.111 1.706 12.960 1.00 0.00 H ATOM 1726 HE2 MET A 282 42.912 3.224 12.075 1.00 0.00 H ATOM 1727 HE3 MET A 282 43.746 3.211 13.637 1.00 0.00 H ATOM 1728 N LYS A 283 40.180 7.842 10.720 1.00 15.97 N ANISOU 1728 N LYS A 283 2068 1940 2061 164 181 -140 ATOM 1729 CA LYS A 283 40.219 8.537 9.429 1.00 15.92 C ANISOU 1729 CA LYS A 283 2054 1942 2054 171 184 -138 ATOM 1730 C LYS A 283 40.220 10.073 9.581 1.00 16.68 C ANISOU 1730 C LYS A 283 2157 2032 2149 177 188 -150 ATOM 1731 O LYS A 283 40.862 10.749 8.780 1.00 17.15 O ANISOU 1731 O LYS A 283 2216 2100 2200 188 190 -154 ATOM 1732 CB LYS A 283 39.067 8.024 8.532 1.00 17.16 C ANISOU 1732 CB LYS A 283 2208 2098 2212 177 182 -131 ATOM 1733 CG LYS A 283 38.987 8.635 7.113 1.00 21.04 C ANISOU 1733 CG LYS A 283 2692 2600 2702 190 189 -126 ATOM 1734 CD LYS A 283 40.236 8.449 6.227 1.00 26.17 C ANISOU 1734 CD LYS A 283 3324 3270 3349 192 190 -112 ATOM 1735 CE LYS A 283 40.545 6.981 5.876 1.00 27.20 C ANISOU 1735 CE LYS A 283 3441 3402 3492 179 176 -91 ATOM 1736 NZ LYS A 283 41.716 6.862 4.990 1.00 31.83 N1+ ANISOU 1736 NZ LYS A 283 4002 4011 4083 182 178 -64 ATOM 1737 H LYS A 283 39.321 7.355 10.939 1.00 0.00 H ATOM 1738 HA LYS A 283 41.158 8.254 8.951 1.00 0.00 H ATOM 1739 HB3 LYS A 283 38.117 8.204 9.036 1.00 0.00 H ATOM 1740 HB2 LYS A 283 39.144 6.939 8.442 1.00 0.00 H ATOM 1741 HG3 LYS A 283 38.767 9.700 7.186 1.00 0.00 H ATOM 1742 HG2 LYS A 283 38.125 8.213 6.598 1.00 0.00 H ATOM 1743 HD3 LYS A 283 41.101 8.907 6.708 1.00 0.00 H ATOM 1744 HD2 LYS A 283 40.084 9.015 5.306 1.00 0.00 H ATOM 1745 HE3 LYS A 283 39.696 6.531 5.365 1.00 0.00 H ATOM 1746 HE2 LYS A 283 40.733 6.397 6.777 1.00 0.00 H ATOM 1747 HZ1 LYS A 283 42.537 7.199 5.479 1.00 0.00 H ATOM 1748 HZ2 LYS A 283 41.860 5.892 4.746 1.00 0.00 H ATOM 1749 HZ3 LYS A 283 41.573 7.406 4.151 1.00 0.00 H ATOM 1750 N LYS A 284 39.540 10.591 10.621 1.00 17.80 N ANISOU 1750 N LYS A 284 2306 2159 2299 173 186 -152 ATOM 1751 CA LYS A 284 39.520 12.006 11.000 1.00 26.02 C ANISOU 1751 CA LYS A 284 3356 3186 3346 175 178 -161 ATOM 1752 C LYS A 284 40.908 12.489 11.450 1.00 26.11 C ANISOU 1752 C LYS A 284 3368 3200 3353 171 173 -167 ATOM 1753 O LYS A 284 41.373 13.510 10.950 1.00 24.63 O ANISOU 1753 O LYS A 284 3191 3007 3161 181 164 -180 ATOM 1754 CB LYS A 284 38.442 12.223 12.084 1.00 19.93 C ANISOU 1754 CB LYS A 284 2584 2398 2591 166 174 -151 ATOM 1755 CG LYS A 284 38.273 13.671 12.574 1.00 13.75 C ANISOU 1755 CG LYS A 284 1807 1593 1824 161 155 -154 ATOM 1756 CD LYS A 284 37.054 13.826 13.502 1.00 17.18 C ANISOU 1756 CD LYS A 284 2233 2014 2281 151 151 -132 ATOM 1757 CE LYS A 284 36.898 15.211 14.160 1.00 23.59 C ANISOU 1757 CE LYS A 284 3048 2797 3118 142 123 -129 ATOM 1758 NZ LYS A 284 37.983 15.520 15.108 1.00 29.10 N1+ ANISOU 1758 NZ LYS A 284 3737 3493 3826 128 117 -120 ATOM 1759 H LYS A 284 39.002 9.970 11.211 1.00 0.00 H ATOM 1760 HA LYS A 284 39.234 12.582 10.117 1.00 0.00 H ATOM 1761 HB3 LYS A 284 38.674 11.600 12.945 1.00 0.00 H ATOM 1762 HB2 LYS A 284 37.483 11.873 11.709 1.00 0.00 H ATOM 1763 HG3 LYS A 284 38.176 14.340 11.719 1.00 0.00 H ATOM 1764 HG2 LYS A 284 39.177 13.973 13.101 1.00 0.00 H ATOM 1765 HD3 LYS A 284 37.083 13.055 14.271 1.00 0.00 H ATOM 1766 HD2 LYS A 284 36.152 13.621 12.924 1.00 0.00 H ATOM 1767 HE3 LYS A 284 35.953 15.249 14.704 1.00 0.00 H ATOM 1768 HE2 LYS A 284 36.859 15.996 13.407 1.00 0.00 H ATOM 1769 HZ1 LYS A 284 38.859 15.570 14.601 1.00 0.00 H ATOM 1770 HZ2 LYS A 284 37.810 16.417 15.540 1.00 0.00 H ATOM 1771 HZ3 LYS A 284 38.041 14.804 15.818 1.00 0.00 H ATOM 1772 N ALA A 285 41.555 11.718 12.342 1.00 25.31 N ANISOU 1772 N ALA A 285 3258 3105 3253 160 177 -161 ATOM 1773 CA ALA A 285 42.918 11.951 12.821 1.00 19.84 C ANISOU 1773 CA ALA A 285 2565 2416 2559 155 172 -165 ATOM 1774 C ALA A 285 43.994 11.838 11.727 1.00 23.68 C ANISOU 1774 C ALA A 285 3050 2921 3029 165 176 -167 ATOM 1775 O ALA A 285 44.986 12.563 11.790 1.00 21.92 O ANISOU 1775 O ALA A 285 2832 2701 2797 169 170 -174 ATOM 1776 CB ALA A 285 43.221 10.961 13.952 1.00 19.62 C ANISOU 1776 CB ALA A 285 2528 2389 2537 143 175 -155 ATOM 1777 H ALA A 285 41.097 10.893 12.707 1.00 0.00 H ATOM 1778 HA ALA A 285 42.964 12.963 13.227 1.00 0.00 H ATOM 1779 HB1 ALA A 285 44.262 11.039 14.259 1.00 0.00 H ATOM 1780 HB2 ALA A 285 42.599 11.154 14.827 1.00 0.00 H ATOM 1781 HB3 ALA A 285 43.050 9.929 13.643 1.00 0.00 H ATOM 1782 N GLU A 286 43.768 10.947 10.747 1.00 24.71 N ANISOU 1782 N GLU A 286 3171 3064 3155 169 183 -158 ATOM 1783 CA GLU A 286 44.615 10.747 9.573 1.00 24.69 C ANISOU 1783 CA GLU A 286 3158 3083 3140 179 189 -149 ATOM 1784 C GLU A 286 44.577 11.950 8.611 1.00 34.30 C ANISOU 1784 C GLU A 286 4386 4306 4341 204 193 -159 ATOM 1785 O GLU A 286 45.628 12.355 8.117 1.00 34.67 O ANISOU 1785 O GLU A 286 4432 4369 4370 219 197 -158 ATOM 1786 CB GLU A 286 44.197 9.429 8.892 1.00 14.52 C ANISOU 1786 CB GLU A 286 1855 1803 1859 176 190 -131 ATOM 1787 CG GLU A 286 45.032 9.025 7.656 1.00 23.75 C ANISOU 1787 CG GLU A 286 3005 2997 3024 182 195 -109 ATOM 1788 CD GLU A 286 44.640 7.679 7.022 1.00 36.22 C ANISOU 1788 CD GLU A 286 4567 4576 4618 174 186 -86 ATOM 1789 OE1 GLU A 286 43.731 6.994 7.545 1.00 32.17 O ANISOU 1789 OE1 GLU A 286 4064 4046 4113 167 178 -94 ATOM 1790 OE2 GLU A 286 45.257 7.353 5.984 1.00 40.79 O1- ANISOU 1790 OE2 GLU A 286 5122 5174 5202 174 186 -58 ATOM 1791 H GLU A 286 42.940 10.368 10.794 1.00 0.00 H ATOM 1792 HA GLU A 286 45.639 10.626 9.924 1.00 0.00 H ATOM 1793 HB3 GLU A 286 43.150 9.497 8.600 1.00 0.00 H ATOM 1794 HB2 GLU A 286 44.246 8.631 9.632 1.00 0.00 H ATOM 1795 HG3 GLU A 286 46.085 8.975 7.935 1.00 0.00 H ATOM 1796 HG2 GLU A 286 44.952 9.791 6.883 1.00 0.00 H ATOM 1797 N ILE A 287 43.371 12.497 8.387 1.00 33.30 N ANISOU 1797 N ILE A 287 4270 4164 4218 212 191 -168 ATOM 1798 CA ILE A 287 43.113 13.662 7.537 1.00 31.65 C ANISOU 1798 CA ILE A 287 4077 3956 3992 242 191 -181 ATOM 1799 C ILE A 287 43.616 14.984 8.156 1.00 33.95 C ANISOU 1799 C ILE A 287 4393 4231 4277 247 173 -202 ATOM 1800 O ILE A 287 44.248 15.770 7.451 1.00 36.67 O ANISOU 1800 O ILE A 287 4752 4586 4597 275 173 -213 ATOM 1801 CB ILE A 287 41.593 13.767 7.188 1.00 32.91 C ANISOU 1801 CB ILE A 287 4241 4100 4162 247 190 -183 ATOM 1802 CG1 ILE A 287 41.205 12.692 6.141 1.00 24.56 C ANISOU 1802 CG1 ILE A 287 3162 3064 3107 249 204 -161 ATOM 1803 CG2 ILE A 287 41.113 15.161 6.720 1.00 38.17 C ANISOU 1803 CG2 ILE A 287 4933 4754 4816 276 180 -204 ATOM 1804 CD1 ILE A 287 39.693 12.450 6.008 1.00 18.59 C ANISOU 1804 CD1 ILE A 287 2406 2293 2365 246 201 -159 ATOM 1805 H ILE A 287 42.557 12.087 8.825 1.00 0.00 H ATOM 1806 HA ILE A 287 43.664 13.515 6.606 1.00 0.00 H ATOM 1807 HB ILE A 287 41.039 13.541 8.100 1.00 0.00 H ATOM 1808 HG13 ILE A 287 41.679 11.741 6.387 1.00 0.00 H ATOM 1809 HG12 ILE A 287 41.608 12.973 5.167 1.00 0.00 H ATOM 1810 HG21 ILE A 287 40.062 15.142 6.455 1.00 0.00 H ATOM 1811 HG22 ILE A 287 41.204 15.920 7.497 1.00 0.00 H ATOM 1812 HG23 ILE A 287 41.672 15.499 5.847 1.00 0.00 H ATOM 1813 HD11 ILE A 287 39.494 11.442 5.645 1.00 0.00 H ATOM 1814 HD12 ILE A 287 39.177 12.564 6.962 1.00 0.00 H ATOM 1815 HD13 ILE A 287 39.241 13.140 5.296 1.00 0.00 H ATOM 1816 N GLU A 288 43.314 15.207 9.448 1.00 34.39 N ANISOU 1816 N GLU A 288 4452 4260 4354 223 157 -206 ATOM 1817 CA GLU A 288 43.601 16.447 10.179 1.00 38.58 C ANISOU 1817 CA GLU A 288 5005 4767 4888 222 130 -222 ATOM 1818 C GLU A 288 45.087 16.695 10.500 1.00 43.79 C ANISOU 1818 C GLU A 288 5668 5438 5535 221 126 -225 ATOM 1819 O GLU A 288 45.420 17.812 10.897 1.00 40.49 O ANISOU 1819 O GLU A 288 5269 4997 5118 221 99 -238 ATOM 1820 CB GLU A 288 42.749 16.487 11.466 1.00 35.70 C ANISOU 1820 CB GLU A 288 4633 4374 4556 194 116 -213 ATOM 1821 CG GLU A 288 41.249 16.749 11.191 1.00 34.00 C ANISOU 1821 CG GLU A 288 4423 4139 4355 197 109 -212 ATOM 1822 CD GLU A 288 40.334 16.717 12.429 1.00 37.56 C ANISOU 1822 CD GLU A 288 4862 4568 4840 171 97 -194 ATOM 1823 OE1 GLU A 288 39.158 17.105 12.259 1.00 41.94 O ANISOU 1823 OE1 GLU A 288 5422 5101 5411 171 82 -190 ATOM 1824 OE2 GLU A 288 40.786 16.300 13.521 1.00 40.58 O1- ANISOU 1824 OE2 GLU A 288 5228 4957 5232 152 103 -179 ATOM 1825 H GLU A 288 42.780 14.513 9.957 1.00 0.00 H ATOM 1826 HA GLU A 288 43.291 17.282 9.547 1.00 0.00 H ATOM 1827 HB3 GLU A 288 43.121 17.253 12.150 1.00 0.00 H ATOM 1828 HB2 GLU A 288 42.870 15.539 11.993 1.00 0.00 H ATOM 1829 HG3 GLU A 288 40.866 16.026 10.471 1.00 0.00 H ATOM 1830 HG2 GLU A 288 41.144 17.726 10.716 1.00 0.00 H ATOM 1831 N HIS A 289 45.948 15.674 10.342 1.00 48.36 N ANISOU 1831 N HIS A 289 6227 6046 6101 220 147 -211 ATOM 1832 CA HIS A 289 47.372 15.722 10.707 1.00 45.27 C ANISOU 1832 CA HIS A 289 5834 5665 5700 216 143 -210 ATOM 1833 C HIS A 289 48.185 15.116 9.574 1.00 42.44 C ANISOU 1833 C HIS A 289 5465 5344 5315 236 164 -197 ATOM 1834 O HIS A 289 47.725 14.700 8.510 1.00 45.87 O ANISOU 1834 O HIS A 289 5888 5797 5743 250 182 -185 ATOM 1835 CB HIS A 289 47.610 14.941 12.018 1.00 41.06 C ANISOU 1835 CB HIS A 289 5284 5126 5193 182 142 -197 ATOM 1836 CG HIS A 289 46.820 15.429 13.209 1.00 35.30 C ANISOU 1836 CG HIS A 289 4556 4365 4490 164 126 -198 ATOM 1837 ND1 HIS A 289 45.698 14.772 13.681 1.00 38.48 N ANISOU 1837 ND1 HIS A 289 4973 4745 4901 159 98 -206 ATOM 1838 CD2 HIS A 289 46.979 16.524 14.029 1.00 37.94 C ANISOU 1838 CD2 HIS A 289 4879 4690 4845 151 132 -187 ATOM 1839 CE1 HIS A 289 45.233 15.475 14.717 1.00 40.15 C ANISOU 1839 CE1 HIS A 289 5178 4935 5144 140 88 -195 ATOM 1840 NE2 HIS A 289 45.966 16.549 14.990 1.00 38.13 N ANISOU 1840 NE2 HIS A 289 4906 4690 4893 137 111 -183 ATOM 1841 H HIS A 289 45.598 14.779 10.026 1.00 0.00 H ATOM 1842 HA HIS A 289 47.713 16.751 10.844 1.00 0.00 H ATOM 1843 HXT HIS A 289 49.257 15.077 9.771 1.00 0.00 H ATOM 1844 HB3 HIS A 289 48.666 14.959 12.293 1.00 0.00 H ATOM 1845 HB2 HIS A 289 47.343 13.897 11.862 1.00 0.00 H ATOM 1846 HD1 HIS A 289 45.292 13.933 13.285 1.00 0.00 H ATOM 1847 HD2 HIS A 289 47.729 17.298 13.990 1.00 0.00 H ATOM 1848 HE1 HIS A 289 44.353 15.197 15.278 1.00 0.00 H TER 1849 HIS A 289 HETATM 1850 O1 UNK 900 20.935 0.321 16.309 1.00 0.00 O HETATM 1851 C1 UNK 900 20.337 0.155 15.253 1.00 0.00 C HETATM 1852 N1 UNK 900 19.642 -0.969 15.021 1.00 0.00 N HETATM 1853 C2 UNK 900 18.737 -1.144 13.895 1.00 0.00 C HETATM 1854 C3 UNK 900 18.213 -2.570 13.774 1.00 0.00 C HETATM 1855 C4 UNK 900 18.390 -3.331 12.596 1.00 0.00 C HETATM 1856 C5 UNK 900 17.854 -4.629 12.501 1.00 0.00 C HETATM 1857 C6 UNK 900 17.131 -5.178 13.577 1.00 0.00 C HETATM 1858 C7 UNK 900 16.950 -4.431 14.757 1.00 0.00 C HETATM 1859 C8 UNK 900 16.168 -5.023 15.913 1.00 0.00 C HETATM 1860 C9 UNK 900 17.494 -3.132 14.855 1.00 0.00 C HETATM 1861 N2 UNK 900 19.336 -0.569 12.691 1.00 0.00 N HETATM 1862 C10 UNK 900 19.912 0.698 12.835 1.00 0.00 C HETATM 1863 C11 UNK 900 20.031 1.510 11.695 1.00 0.00 C HETATM 1864 C12 UNK 900 20.538 2.809 11.805 1.00 0.00 C HETATM 1865 C13 UNK 900 20.941 3.288 13.059 1.00 0.00 C HETATM 1866 C14 UNK 900 20.855 2.476 14.205 1.00 0.00 C HETATM 1867 CL1 UNK 900 21.337 3.206 15.688 1.00 0.00 Cl HETATM 1868 C15 UNK 900 20.358 1.145 14.104 1.00 0.00 C HETATM 1869 H1 UNK 900 19.652 -1.695 15.720 1.00 0.00 H HETATM 1870 H2 UNK 900 17.870 -0.542 14.152 1.00 0.00 H HETATM 1871 H3 UNK 900 18.936 -2.933 11.753 1.00 0.00 H HETATM 1872 H4 UNK 900 17.990 -5.204 11.598 1.00 0.00 H HETATM 1873 H5 UNK 900 16.720 -6.174 13.488 1.00 0.00 H HETATM 1874 H6 UNK 900 15.725 -5.982 15.635 1.00 0.00 H HETATM 1875 H7 UNK 900 15.361 -4.355 16.220 1.00 0.00 H HETATM 1876 H8 UNK 900 16.823 -5.191 16.770 1.00 0.00 H HETATM 1877 H9 UNK 900 17.348 -2.557 15.758 1.00 0.00 H HETATM 1878 H10 UNK 900 18.927 -0.804 11.799 1.00 0.00 H HETATM 1879 H11 UNK 900 19.737 1.137 10.727 1.00 0.00 H HETATM 1880 H12 UNK 900 20.627 3.430 10.928 1.00 0.00 H HETATM 1881 H13 UNK 900 21.333 4.291 13.142 1.00 0.00 H CONECT 1833 1843 CONECT 1843 1833 CONECT 1850 1851 CONECT 1850 1851 CONECT 1851 1850 1868 1852 CONECT 1851 1850 CONECT 1852 1851 1853 1869 CONECT 1853 1852 1854 1861 1870 CONECT 1854 1853 1860 1855 CONECT 1854 1855 CONECT 1855 1854 1856 1871 CONECT 1855 1854 CONECT 1856 1855 1857 1872 CONECT 1856 1857 CONECT 1857 1856 1858 1873 CONECT 1857 1856 CONECT 1858 1857 1859 1860 CONECT 1858 1860 CONECT 1859 1858 1874 1875 1876 CONECT 1860 1854 1858 1877 CONECT 1860 1858 CONECT 1861 1853 1862 1878 CONECT 1862 1861 1868 1863 CONECT 1862 1863 CONECT 1863 1862 1864 1879 CONECT 1863 1862 CONECT 1864 1863 1865 1880 CONECT 1864 1865 CONECT 1865 1864 1866 1881 CONECT 1865 1864 CONECT 1866 1865 1867 1868 CONECT 1866 1868 CONECT 1867 1866 CONECT 1868 1851 1862 1866 CONECT 1868 1866 CONECT 1869 1852 CONECT 1870 1853 CONECT 1871 1855 CONECT 1872 1856 CONECT 1873 1857 CONECT 1874 1859 CONECT 1875 1859 CONECT 1876 1859 CONECT 1877 1860 CONECT 1878 1861 CONECT 1879 1863 CONECT 1880 1864 CONECT 1881 1865 END