HEADER 1.10.135.10 1m15A01 ATOM 1 N VAL A 2 46.175 -11.953 27.067 1.00 30.64 N ANISOU 1 N VAL A 2 3069 3602 4971 790 -168 -429 N ATOM 2 CA VAL A 2 46.461 -10.521 27.206 1.00 33.03 C ANISOU 2 CA VAL A 2 3945 3796 4811 238 1913 -997 C ATOM 3 C VAL A 2 47.921 -10.222 26.919 1.00 35.31 C ANISOU 3 C VAL A 2 4206 4773 4439 -184 2199 -1253 C ATOM 4 O VAL A 2 48.841 -10.999 27.193 1.00 47.91 O ANISOU 4 O VAL A 2 3698 4730 9776 -300 2265 -891 O ATOM 5 CB VAL A 2 46.057 -10.074 28.619 1.00 32.64 C ANISOU 5 CB VAL A 2 3471 4280 4650 173 1977 -603 C ATOM 6 CG1 VAL A 2 46.370 -8.617 28.895 1.00 46.72 C ANISOU 6 CG1 VAL A 2 4280 5129 8345 222 2076 -3300 C ATOM 7 CG2 VAL A 2 44.569 -10.362 28.803 1.00 36.60 C ANISOU 7 CG2 VAL A 2 3219 4753 5935 817 1982 -253 C ATOM 8 N ASP A 3 48.177 -9.062 26.317 1.00 35.68 N ANISOU 8 N ASP A 3 4820 4809 3927 -1095 1611 -1613 N ATOM 9 CA ASP A 3 49.524 -8.661 25.933 1.00 39.57 C ANISOU 9 CA ASP A 3 4664 5204 5169 -857 1815 -1042 C ATOM 10 C ASP A 3 50.329 -8.284 27.169 1.00 38.74 C ANISOU 10 C ASP A 3 3565 6213 4942 -806 2464 -1506 C ATOM 11 O ASP A 3 49.770 -7.803 28.150 1.00 39.69 O ANISOU 11 O ASP A 3 4577 6351 4152 829 2376 -278 O ATOM 12 CB ASP A 3 49.447 -7.499 24.944 1.00 45.17 C ANISOU 12 CB ASP A 3 3847 6401 6916 -932 1583 375 C ATOM 13 CG ASP A 3 48.756 -6.265 25.486 1.00 53.46 C ANISOU 13 CG ASP A 3 5218 5913 9182 -309 256 -13 C ATOM 14 OD1 ASP A 3 49.472 -5.301 25.835 1.00 59.00 O ANISOU 14 OD1 ASP A 3 5688 4559 12170 -182 -974 1575 O ATOM 15 OD2 ASP A 3 47.503 -6.241 25.548 1.00 56.53 O ANISOU 15 OD2 ASP A 3 5209 5752 10517 1394 -2774 -1999 O ATOM 16 N GLN A 4 51.644 -8.443 27.136 1.00 45.33 N ANISOU 16 N GLN A 4 3773 7071 6379 -12 2219 -2087 N ATOM 17 CA GLN A 4 52.520 -8.115 28.252 1.00 45.64 C ANISOU 17 CA GLN A 4 3373 7194 6775 575 1973 -2092 C ATOM 18 C GLN A 4 52.377 -6.677 28.727 1.00 43.82 C ANISOU 18 C GLN A 4 3796 7060 5793 81 2053 -1817 C ATOM 19 O GLN A 4 52.552 -6.375 29.904 1.00 40.99 O ANISOU 19 O GLN A 4 3091 6851 5632 858 1749 -1389 O ATOM 20 CB GLN A 4 53.989 -8.365 27.864 1.00 54.07 C ANISOU 20 CB GLN A 4 3377 8137 9031 371 2436 -2433 C ATOM 21 CG GLN A 4 54.924 -8.297 29.070 1.00 54.91 C ANISOU 21 CG GLN A 4 2788 8482 9594 628 2275 -2206 C ATOM 22 CD GLN A 4 54.597 -9.406 30.057 1.00 57.18 C ANISOU 22 CD GLN A 4 3243 8380 10103 14 1218 -1920 C ATOM 23 OE1 GLN A 4 54.327 -10.541 29.649 1.00 67.15 O ANISOU 23 OE1 GLN A 4 4953 9392 11170 -2069 575 -2157 O ATOM 24 NE2 GLN A 4 54.561 -9.074 31.340 1.00 58.61 N ANISOU 24 NE2 GLN A 4 3241 9008 10021 -1069 2166 -1716 N ATOM 25 N ALA A 5 52.174 -5.745 27.800 1.00 39.17 N ANISOU 25 N ALA A 5 3294 6671 4919 -1234 1753 -2231 N ATOM 26 CA ALA A 5 52.109 -4.341 28.214 1.00 38.69 C ANISOU 26 CA ALA A 5 3138 6664 4898 -1223 1431 -2273 C ATOM 27 C ALA A 5 50.939 -4.119 29.161 1.00 37.38 C ANISOU 27 C ALA A 5 2690 6964 4551 -631 809 -2215 C ATOM 28 O ALA A 5 51.003 -3.289 30.077 1.00 36.91 O ANISOU 28 O ALA A 5 3076 7146 3802 87 306 -1911 O ATOM 29 CB ALA A 5 51.980 -3.445 26.991 1.00 44.59 C ANISOU 29 CB ALA A 5 3544 7264 6136 -1042 1863 -1182 C ATOM 30 N THR A 6 49.838 -4.813 28.866 1.00 35.72 N ANISOU 30 N THR A 6 3279 5921 4374 -1319 1197 -770 N ATOM 31 CA THR A 6 48.647 -4.695 29.707 1.00 33.07 C ANISOU 31 CA THR A 6 2759 5861 3944 -240 613 35 C ATOM 32 C THR A 6 48.886 -5.428 31.023 1.00 28.07 C ANISOU 32 C THR A 6 2246 4594 3826 442 547 -572 C ATOM 33 O THR A 6 48.572 -4.928 32.102 1.00 24.79 O ANISOU 33 O THR A 6 1790 3748 3882 96 616 -410 O ATOM 34 CB THR A 6 47.449 -5.347 28.989 1.00 30.69 C ANISOU 34 CB THR A 6 2498 5880 3284 407 792 -445 C ATOM 35 OG1 THR A 6 47.071 -4.549 27.859 1.00 33.07 O ANISOU 35 OG1 THR A 6 4042 4496 4028 217 13 -532 O ATOM 36 CG2 THR A 6 46.295 -5.443 29.968 1.00 38.90 C ANISOU 36 CG2 THR A 6 2064 8466 4252 552 993 -466 C ATOM 37 N LEU A 7 49.582 -6.574 30.972 1.00 31.25 N ANISOU 37 N LEU A 7 2262 4512 5100 364 1035 -920 N ATOM 38 CA LEU A 7 49.887 -7.277 32.219 1.00 28.36 C ANISOU 38 CA LEU A 7 1819 3291 5667 357 574 -986 C ATOM 39 C LEU A 7 50.787 -6.419 33.101 1.00 28.85 C ANISOU 39 C LEU A 7 1731 3920 5310 165 1073 -1413 C ATOM 40 O LEU A 7 50.666 -6.373 34.316 1.00 30.62 O ANISOU 40 O LEU A 7 2064 4298 5273 778 977 -1303 O ATOM 41 CB LEU A 7 50.463 -8.664 31.990 1.00 36.77 C ANISOU 41 CB LEU A 7 3009 3225 7736 382 1268 -1388 C ATOM 42 CG LEU A 7 49.611 -9.706 31.271 1.00 38.98 C ANISOU 42 CG LEU A 7 3231 3500 8080 -91 1932 -1787 C ATOM 43 CD1 LEU A 7 50.402 -10.997 31.026 1.00 45.34 C ANISOU 43 CD1 LEU A 7 3974 3787 9466 45 2949 -2421 C ATOM 44 CD2 LEU A 7 48.348 -10.015 32.052 1.00 40.78 C ANISOU 44 CD2 LEU A 7 2817 4998 7681 -3 1727 -2434 C ATOM 45 N ASP A 8 51.797 -5.807 32.488 1.00 30.24 N ANISOU 45 N ASP A 8 2010 3873 5606 -82 655 -766 N ATOM 46 CA ASP A 8 52.684 -4.871 33.173 1.00 31.54 C ANISOU 46 CA ASP A 8 1757 4946 5280 -194 997 -1549 C ATOM 47 C ASP A 8 51.923 -3.753 33.873 1.00 31.07 C ANISOU 47 C ASP A 8 2227 5308 4272 308 662 -1395 C ATOM 48 O ASP A 8 52.177 -3.434 35.043 1.00 29.47 O ANISOU 48 O ASP A 8 1574 5226 4397 -140 382 -1268 O ATOM 49 CB ASP A 8 53.674 -4.249 32.175 1.00 33.52 C ANISOU 49 CB ASP A 8 1882 4739 6116 -347 1410 -1687 C ATOM 50 CG ASP A 8 54.656 -5.224 31.573 1.00 39.60 C ANISOU 50 CG ASP A 8 3368 5882 5798 307 1995 -2050 C ATOM 51 OD1 ASP A 8 54.892 -6.311 32.139 1.00 38.60 O ANISOU 51 OD1 ASP A 8 2916 7359 4393 2178 -232 -2293 O ATOM 52 OD2 ASP A 8 55.258 -4.880 30.522 1.00 53.87 O ANISOU 52 OD2 ASP A 8 5135 9878 5456 1267 2455 -1403 O ATOM 53 N LYS A 9 51.043 -3.098 33.121 1.00 26.73 N ANISOU 53 N LYS A 9 2523 4079 3554 -381 818 -1158 N ATOM 54 CA LYS A 9 50.203 -2.038 33.676 1.00 26.30 C ANISOU 54 CA LYS A 9 3127 3606 3259 -129 742 -587 C ATOM 55 C LYS A 9 49.317 -2.575 34.785 1.00 22.64 C ANISOU 55 C LYS A 9 2381 3206 3016 263 409 -597 C ATOM 56 O LYS A 9 49.081 -1.960 35.828 1.00 24.85 O ANISOU 56 O LYS A 9 1982 4204 3256 -5 368 -1169 O ATOM 57 CB LYS A 9 49.368 -1.369 32.577 1.00 27.05 C ANISOU 57 CB LYS A 9 2832 4130 3317 -649 692 -102 C ATOM 58 CG LYS A 9 50.194 -0.462 31.650 1.00 30.93 C ANISOU 58 CG LYS A 9 3453 4806 3495 -627 1349 36 C ATOM 59 CD LYS A 9 49.377 -0.066 30.425 1.00 38.37 C ANISOU 59 CD LYS A 9 4247 5870 4463 -1143 778 1360 C ATOM 60 CE LYS A 9 48.841 -1.294 29.709 1.00 48.79 C ANISOU 60 CE LYS A 9 5757 7441 5341 -128 -1000 -474 C ATOM 61 NZ LYS A 9 48.608 -1.085 28.254 1.00 56.29 N ANISOU 61 NZ LYS A 9 8422 7360 5608 3742 -1575 -741 N ATOM 62 N LEU A 10 48.842 -3.817 34.611 1.00 22.20 N ANISOU 62 N LEU A 10 1295 3352 3788 239 53 -636 N ATOM 63 CA LEU A 10 48.012 -4.364 35.689 1.00 24.15 C ANISOU 63 CA LEU A 10 1652 3692 3832 -32 155 -610 C ATOM 64 C LEU A 10 48.810 -4.560 36.973 1.00 24.65 C ANISOU 64 C LEU A 10 1609 3837 3922 475 90 -426 C ATOM 65 O LEU A 10 48.341 -4.280 38.076 1.00 22.57 O ANISOU 65 O LEU A 10 1758 2978 3839 486 103 -231 O ATOM 66 CB LEU A 10 47.400 -5.691 35.228 1.00 23.66 C ANISOU 66 CB LEU A 10 1445 3322 4224 306 260 -535 C ATOM 67 CG LEU A 10 46.161 -5.509 34.340 1.00 22.79 C ANISOU 67 CG LEU A 10 1362 3528 3768 452 365 -1227 C ATOM 68 CD1 LEU A 10 45.793 -6.813 33.660 1.00 22.88 C ANISOU 68 CD1 LEU A 10 1874 2921 3898 437 313 -704 C ATOM 69 CD2 LEU A 10 45.021 -4.952 35.196 1.00 19.35 C ANISOU 69 CD2 LEU A 10 1403 3194 2757 251 568 -285 C ATOM 70 N GLU A 11 49.985 -5.188 36.877 1.00 26.33 N ANISOU 70 N GLU A 11 1653 3676 4675 449 640 183 N ATOM 71 CA GLU A 11 50.818 -5.400 38.062 1.00 29.90 C ANISOU 71 CA GLU A 11 2275 3288 5798 1234 -161 316 C ATOM 72 C GLU A 11 51.144 -4.080 38.749 1.00 28.15 C ANISOU 72 C GLU A 11 2168 3373 5154 1349 -580 421 C ATOM 73 O GLU A 11 51.120 -3.922 39.969 1.00 28.25 O ANISOU 73 O GLU A 11 1723 3897 5113 1001 -3 559 O ATOM 74 CB GLU A 11 52.108 -6.134 37.689 1.00 33.39 C ANISOU 74 CB GLU A 11 2650 4292 5746 1605 248 -156 C ATOM 75 CG GLU A 11 51.870 -7.513 37.078 1.00 36.07 C ANISOU 75 CG GLU A 11 2978 4909 5818 1296 1100 -889 C ATOM 76 CD GLU A 11 51.381 -8.547 38.075 1.00 31.43 C ANISOU 76 CD GLU A 11 2407 4198 5337 1277 341 -1193 C ATOM 77 OE1 GLU A 11 51.467 -8.322 39.304 1.00 32.17 O ANISOU 77 OE1 GLU A 11 2550 4340 5335 1239 -627 -846 O ATOM 78 OE2 GLU A 11 50.927 -9.612 37.605 1.00 40.48 O ANISOU 78 OE2 GLU A 11 4535 5056 5789 182 -2363 -503 O ATOM 79 N ALA A 12 51.410 -3.048 37.944 1.00 26.78 N ANISOU 79 N ALA A 12 1920 3489 4765 787 45 -19 N ATOM 80 CA ALA A 12 51.701 -1.730 38.523 1.00 27.56 C ANISOU 80 CA ALA A 12 1277 3981 5214 -52 379 -289 C ATOM 81 C ALA A 12 50.453 -1.121 39.154 1.00 26.25 C ANISOU 81 C ALA A 12 1488 3986 4502 257 -152 -774 C ATOM 82 O ALA A 12 50.516 -0.500 40.225 1.00 24.37 O ANISOU 82 O ALA A 12 2331 3121 3808 -6 -288 31 O ATOM 83 CB ALA A 12 52.275 -0.808 37.445 1.00 26.99 C ANISOU 83 CB ALA A 12 1753 4411 4091 -699 -452 -482 C ATOM 84 N GLY A 13 49.287 -1.333 38.527 1.00 23.07 N ANISOU 84 N GLY A 13 1385 2930 4452 271 -145 -440 N ATOM 85 CA GLY A 13 48.081 -0.793 39.171 1.00 22.96 C ANISOU 85 CA GLY A 13 1563 2490 4672 564 105 251 C ATOM 86 C GLY A 13 47.794 -1.531 40.474 1.00 22.12 C ANISOU 86 C GLY A 13 1265 2647 4491 458 -256 303 C ATOM 87 O GLY A 13 47.321 -0.924 41.460 1.00 21.44 O ANISOU 87 O GLY A 13 1076 2556 4515 406 -305 238 O ATOM 88 N PHE A 14 47.951 -2.861 40.467 1.00 21.77 N ANISOU 88 N PHE A 14 1417 2599 4255 110 -122 147 N ATOM 89 CA PHE A 14 47.671 -3.622 41.702 1.00 20.55 C ANISOU 89 CA PHE A 14 1874 2068 3868 60 -304 -324 C ATOM 90 C PHE A 14 48.587 -3.093 42.802 1.00 22.81 C ANISOU 90 C PHE A 14 2211 2361 4094 -450 -257 -499 C ATOM 91 O PHE A 14 48.180 -2.838 43.939 1.00 22.32 O ANISOU 91 O PHE A 14 2090 2705 3685 640 -737 33 O ATOM 92 CB PHE A 14 47.891 -5.121 41.452 1.00 20.25 C ANISOU 92 CB PHE A 14 2104 2189 3400 241 94 -552 C ATOM 93 CG PHE A 14 47.736 -5.998 42.682 1.00 22.56 C ANISOU 93 CG PHE A 14 2037 2309 4227 276 -197 56 C ATOM 94 CD1 PHE A 14 46.485 -6.425 43.080 1.00 23.99 C ANISOU 94 CD1 PHE A 14 2197 2913 4007 -229 -528 430 C ATOM 95 CD2 PHE A 14 48.793 -6.377 43.471 1.00 22.62 C ANISOU 95 CD2 PHE A 14 2029 2503 4062 632 -44 -128 C ATOM 96 CE1 PHE A 14 46.276 -7.158 44.229 1.00 25.48 C ANISOU 96 CE1 PHE A 14 2292 3293 4097 991 175 669 C ATOM 97 CE2 PHE A 14 48.598 -7.071 44.650 1.00 25.72 C ANISOU 97 CE2 PHE A 14 2526 2483 4764 225 -385 526 C ATOM 98 CZ PHE A 14 47.348 -7.459 45.055 1.00 25.09 C ANISOU 98 CZ PHE A 14 2464 3236 3835 703 -67 360 C ATOM 99 N LYS A 15 49.867 -2.920 42.470 1.00 22.18 N ANISOU 99 N LYS A 15 1990 2361 4078 -117 -606 419 N ATOM 100 CA LYS A 15 50.844 -2.379 43.411 1.00 24.20 C ANISOU 100 CA LYS A 15 2028 2758 4411 77 -831 144 C ATOM 101 C LYS A 15 50.436 -0.998 43.920 1.00 24.89 C ANISOU 101 C LYS A 15 2221 3070 4165 420 -1374 -89 C ATOM 102 O LYS A 15 50.523 -0.686 45.123 1.00 24.07 O ANISOU 102 O LYS A 15 1942 3208 3996 -139 -973 78 O ATOM 103 CB LYS A 15 52.225 -2.326 42.772 1.00 28.95 C ANISOU 103 CB LYS A 15 1616 3778 5607 375 -909 144 C ATOM 104 CG LYS A 15 53.371 -1.810 43.634 1.00 35.79 C ANISOU 104 CG LYS A 15 1905 4545 7151 433 -1378 -810 C ATOM 105 CD LYS A 15 54.705 -2.012 42.900 1.00 44.25 C ANISOU 105 CD LYS A 15 1371 6381 9062 893 -1155 850 C ATOM 106 CE LYS A 15 55.724 -0.953 43.299 1.00 54.67 C ANISOU 106 CE LYS A 15 2156 7376 11240 -70 -613 169 C ATOM 107 NZ LYS A 15 56.915 -0.900 42.401 1.00 57.54 N ANISOU 107 NZ LYS A 15 2437 9339 10088 -791 -890 1266 N ATOM 108 N LYS A 16 50.031 -0.154 42.966 1.00 21.52 N ANISOU 108 N LYS A 16 1660 2486 4030 -255 -1159 -123 N ATOM 109 CA LYS A 16 49.623 1.192 43.367 1.00 21.91 C ANISOU 109 CA LYS A 16 2440 2312 3574 -522 -460 146 C ATOM 110 C LYS A 16 48.456 1.107 44.334 1.00 25.97 C ANISOU 110 C LYS A 16 2603 3220 4045 -828 -148 -603 C ATOM 111 O LYS A 16 48.400 1.880 45.309 1.00 21.40 O ANISOU 111 O LYS A 16 2261 2129 3742 66 -737 59 O ATOM 112 CB LYS A 16 49.232 1.968 42.108 1.00 24.04 C ANISOU 112 CB LYS A 16 2759 2391 3984 -576 -1251 220 C ATOM 113 CG LYS A 16 48.796 3.397 42.385 1.00 28.55 C ANISOU 113 CG LYS A 16 3067 2207 5575 -674 -1216 336 C ATOM 114 CD LYS A 16 48.830 4.217 41.099 1.00 38.04 C ANISOU 114 CD LYS A 16 4980 2670 6803 -637 -279 1448 C ATOM 115 CE LYS A 16 48.262 5.608 41.313 1.00 41.85 C ANISOU 115 CE LYS A 16 5284 3661 6958 854 -855 1600 C ATOM 116 NZ LYS A 16 47.325 6.008 40.225 1.00 46.45 N ANISOU 116 NZ LYS A 16 3657 4647 9344 -1373 -1810 3087 N ATOM 117 N LEU A 17 47.473 0.236 44.109 1.00 20.50 N ANISOU 117 N LEU A 17 2092 2195 3504 -129 -355 84 N ATOM 118 CA LEU A 17 46.355 0.121 45.052 1.00 19.89 C ANISOU 118 CA LEU A 17 1822 2855 2882 -1 -786 99 C ATOM 119 C LEU A 17 46.795 -0.371 46.430 1.00 22.23 C ANISOU 119 C LEU A 17 2098 3325 3023 239 -997 155 C ATOM 120 O LEU A 17 46.334 0.145 47.460 1.00 20.91 O ANISOU 120 O LEU A 17 2599 2486 2860 -403 -809 293 O ATOM 121 CB LEU A 17 45.322 -0.872 44.516 1.00 19.20 C ANISOU 121 CB LEU A 17 1975 2810 2511 -230 -473 134 C ATOM 122 CG LEU A 17 44.432 -0.384 43.370 1.00 18.95 C ANISOU 122 CG LEU A 17 1801 2607 2792 336 -658 -455 C ATOM 123 CD1 LEU A 17 43.812 -1.600 42.710 1.00 19.61 C ANISOU 123 CD1 LEU A 17 1455 2688 3309 109 -454 -583 C ATOM 124 CD2 LEU A 17 43.451 0.683 43.783 1.00 16.67 C ANISOU 124 CD2 LEU A 17 1910 2240 2185 -86 349 98 C ATOM 125 N GLN A 18 47.701 -1.353 46.436 1.00 23.20 N ANISOU 125 N GLN A 18 1630 3501 3686 148 -1081 374 N ATOM 126 CA GLN A 18 48.171 -1.887 47.710 1.00 22.34 C ANISOU 126 CA GLN A 18 2419 2284 3784 -228 -1207 360 C ATOM 127 C GLN A 18 48.907 -0.809 48.499 1.00 23.05 C ANISOU 127 C GLN A 18 3066 2166 3526 -375 -1246 520 C ATOM 128 O GLN A 18 48.805 -0.784 49.728 1.00 24.83 O ANISOU 128 O GLN A 18 2950 2990 3494 -11 -1187 317 O ATOM 129 CB GLN A 18 49.166 -3.035 47.493 1.00 27.23 C ANISOU 129 CB GLN A 18 3537 2602 4206 494 -1736 28 C ATOM 130 CG GLN A 18 48.581 -4.268 46.828 1.00 24.77 C ANISOU 130 CG GLN A 18 3149 2411 3852 -436 60 302 C ATOM 131 CD GLN A 18 47.093 -4.427 47.027 1.00 26.75 C ANISOU 131 CD GLN A 18 3003 3808 3355 -149 -304 937 C ATOM 132 OE1 GLN A 18 46.293 -4.120 46.140 1.00 39.93 O ANISOU 132 OE1 GLN A 18 3995 7163 4013 476 -1035 1333 O ATOM 133 NE2 GLN A 18 46.699 -4.989 48.155 1.00 30.42 N ANISOU 133 NE2 GLN A 18 3530 4500 3528 -555 130 979 N ATOM 134 N GLU A 19 49.668 0.033 47.773 1.00 22.20 N ANISOU 134 N GLU A 19 2331 2027 4079 -98 -1312 683 N ATOM 135 CA GLU A 19 50.471 1.039 48.461 1.00 22.62 C ANISOU 135 CA GLU A 19 1821 2639 4136 -141 -841 118 C ATOM 136 C GLU A 19 49.631 2.194 48.986 1.00 23.22 C ANISOU 136 C GLU A 19 1913 3060 3848 47 -875 -118 C ATOM 137 O GLU A 19 50.098 3.004 49.807 1.00 24.15 O ANISOU 137 O GLU A 19 2911 2854 3413 -242 -828 172 O ATOM 138 CB GLU A 19 51.556 1.538 47.505 1.00 22.98 C ANISOU 138 CB GLU A 19 1825 2726 4180 67 -718 249 C ATOM 139 CG GLU A 19 52.667 0.517 47.288 1.00 25.64 C ANISOU 139 CG GLU A 19 1903 3217 4621 255 -933 -509 C ATOM 140 CD GLU A 19 53.613 0.908 46.163 1.00 31.79 C ANISOU 140 CD GLU A 19 2196 3665 6219 525 17 92 C ATOM 141 OE1 GLU A 19 53.441 1.974 45.532 1.00 31.99 O ANISOU 141 OE1 GLU A 19 3001 3008 6145 -139 116 -257 O ATOM 142 OE2 GLU A 19 54.548 0.109 45.894 1.00 41.44 O ANISOU 142 OE2 GLU A 19 4263 4248 7235 1533 1407 55 O ATOM 143 N ALA A 20 48.450 2.405 48.416 1.00 22.08 N ANISOU 143 N ALA A 20 1934 3013 3442 68 -609 757 N ATOM 144 CA ALA A 20 47.619 3.561 48.764 1.00 21.32 C ANISOU 144 CA ALA A 20 2152 3095 2854 200 -543 870 C ATOM 145 C ALA A 20 46.906 3.248 50.077 1.00 20.55 C ANISOU 145 C ALA A 20 2423 2885 2499 -525 -792 383 C ATOM 146 O ALA A 20 45.801 2.702 50.036 1.00 23.06 O ANISOU 146 O ALA A 20 2636 3168 2958 -772 -655 613 O ATOM 147 CB ALA A 20 46.564 3.861 47.705 1.00 20.67 C ANISOU 147 CB ALA A 20 1981 3449 2423 385 -407 320 C ATOM 148 N SER A 21 47.574 3.494 51.185 1.00 26.33 N ANISOU 148 N SER A 21 2729 4467 2807 44 -1227 88 N ATOM 149 CA SER A 21 47.118 3.090 52.508 1.00 31.08 C ANISOU 149 CA SER A 21 3091 6087 2631 -246 -1505 381 C ATOM 150 C SER A 21 45.801 3.717 52.899 1.00 29.33 C ANISOU 150 C SER A 21 2942 5857 2345 -577 -1164 732 C ATOM 151 O SER A 21 44.996 3.166 53.659 1.00 33.57 O ANISOU 151 O SER A 21 3726 6507 2521 -1208 -858 677 O ATOM 152 CB SER A 21 48.218 3.457 53.530 1.00 38.73 C ANISOU 152 CB SER A 21 3379 7973 3364 -554 -2170 727 C ATOM 153 OG SER A 21 49.407 2.788 53.132 1.00 51.98 O ANISOU 153 OG SER A 21 2785 9302 7664 -293 -1485 1862 O ATOM 154 N ASP A 22 45.499 4.907 52.376 1.00 28.24 N ANISOU 154 N ASP A 22 2974 5247 2510 -683 -1203 129 N ATOM 155 CA ASP A 22 44.216 5.448 52.853 1.00 32.49 C ANISOU 155 CA ASP A 22 3338 6210 2798 -147 -1358 -834 C ATOM 156 C ASP A 22 43.133 5.377 51.783 1.00 31.15 C ANISOU 156 C ASP A 22 2956 6085 2795 -309 -1110 -807 C ATOM 157 O ASP A 22 42.075 6.005 51.911 1.00 39.34 O ANISOU 157 O ASP A 22 4258 7598 3091 1388 -1881 -1208 O ATOM 158 CB ASP A 22 44.404 6.886 53.317 1.00 44.71 C ANISOU 158 CB ASP A 22 5780 7481 3727 -475 -900 -2914 C ATOM 159 CG ASP A 22 45.312 7.030 54.519 1.00 54.03 C ANISOU 159 CG ASP A 22 6510 9319 4702 -1957 -1693 -2634 C ATOM 160 OD1 ASP A 22 45.226 6.219 55.469 1.00 61.10 O ANISOU 160 OD1 ASP A 22 8212 10757 4248 -1609 -2195 -2190 O ATOM 161 OD2 ASP A 22 46.160 7.955 54.505 1.00 70.60 O ANISOU 161 OD2 ASP A 22 8192 10400 8234 -3316 -2319 -3007 O ATOM 162 N CYS A 23 43.359 4.636 50.701 1.00 25.03 N ANISOU 162 N CYS A 23 2377 4951 2181 -1193 -663 28 N ATOM 163 CA CYS A 23 42.318 4.455 49.683 1.00 20.59 C ANISOU 163 CA CYS A 23 2102 3550 2173 -784 -638 378 C ATOM 164 C CYS A 23 41.230 3.543 50.230 1.00 21.81 C ANISOU 164 C CYS A 23 2141 4029 2117 -790 -882 1135 C ATOM 165 O CYS A 23 41.466 2.511 50.870 1.00 24.53 O ANISOU 165 O CYS A 23 2549 4223 2549 -393 -665 1373 O ATOM 166 CB CYS A 23 43.018 3.832 48.479 1.00 21.91 C ANISOU 166 CB CYS A 23 2359 3940 2026 -694 -707 288 C ATOM 167 SG CYS A 23 41.874 3.217 47.216 1.00 19.23 S ANISOU 167 SG CYS A 23 1928 3224 2156 -434 -600 426 S ATOM 168 N LYS A 24 39.990 3.973 49.985 1.00 19.70 N ANISOU 168 N LYS A 24 2109 3110 2267 -867 -843 546 N ATOM 169 CA LYS A 24 38.836 3.298 50.563 1.00 19.32 C ANISOU 169 CA LYS A 24 2258 3058 2024 -727 -237 -164 C ATOM 170 C LYS A 24 37.898 2.775 49.487 1.00 15.80 C ANISOU 170 C LYS A 24 1741 2387 1876 -390 -430 378 C ATOM 171 O LYS A 24 36.741 2.414 49.765 1.00 19.49 O ANISOU 171 O LYS A 24 2009 3025 2370 -742 -184 336 O ATOM 172 CB LYS A 24 38.103 4.266 51.503 1.00 26.60 C ANISOU 172 CB LYS A 24 3278 4197 2633 119 -416 -876 C ATOM 173 CG LYS A 24 38.907 4.621 52.745 1.00 32.69 C ANISOU 173 CG LYS A 24 4065 4782 3573 -316 -845 -1924 C ATOM 174 CD LYS A 24 38.134 5.374 53.809 1.00 41.05 C ANISOU 174 CD LYS A 24 5078 7295 3226 165 -490 -2182 C ATOM 175 CE LYS A 24 38.912 5.458 55.110 1.00 45.70 C ANISOU 175 CE LYS A 24 5550 8882 2933 1047 -514 -1675 C ATOM 176 NZ LYS A 24 38.063 5.270 56.326 1.00 54.13 N ANISOU 176 NZ LYS A 24 5762 11335 3471 2232 -448 1052 N ATOM 177 N SER A 25 38.378 2.619 48.256 1.00 16.47 N ANISOU 177 N SER A 25 1890 2450 1918 -356 -397 249 N ATOM 178 CA SER A 25 37.498 2.146 47.197 1.00 15.02 C ANISOU 178 CA SER A 25 1637 2257 1815 -216 -375 385 C ATOM 179 C SER A 25 37.143 0.681 47.403 1.00 15.51 C ANISOU 179 C SER A 25 1408 2316 2169 -308 -519 625 C ATOM 180 O SER A 25 37.910 -0.141 47.937 1.00 16.27 O ANISOU 180 O SER A 25 1736 2504 1942 -187 -514 664 O ATOM 181 CB SER A 25 38.106 2.306 45.804 1.00 15.16 C ANISOU 181 CB SER A 25 1399 2475 1886 22 -204 461 C ATOM 182 OG SER A 25 39.270 1.492 45.675 1.00 16.30 O ANISOU 182 OG SER A 25 1567 2228 2398 71 -431 232 O ATOM 183 N LEU A 26 35.992 0.280 46.869 1.00 14.44 N ANISOU 183 N LEU A 26 1495 2378 1614 -235 -256 288 N ATOM 184 CA LEU A 26 35.640 -1.133 46.861 1.00 13.69 C ANISOU 184 CA LEU A 26 1330 2401 1471 -259 -224 196 C ATOM 185 C LEU A 26 36.611 -1.909 45.974 1.00 14.54 C ANISOU 185 C LEU A 26 1271 2290 1965 32 25 613 C ATOM 186 O LEU A 26 36.859 -3.097 46.267 1.00 15.45 O ANISOU 186 O LEU A 26 1708 2119 2042 -127 -435 512 O ATOM 187 CB LEU A 26 34.181 -1.271 46.366 1.00 13.99 C ANISOU 187 CB LEU A 26 1260 2537 1519 67 -254 -106 C ATOM 188 CG LEU A 26 33.097 -0.730 47.302 1.00 13.65 C ANISOU 188 CG LEU A 26 1438 2237 1512 87 -149 -21 C ATOM 189 CD1 LEU A 26 31.702 -0.974 46.728 1.00 17.70 C ANISOU 189 CD1 LEU A 26 1326 3139 2259 98 -176 176 C ATOM 190 CD2 LEU A 26 33.248 -1.287 48.699 1.00 18.15 C ANISOU 190 CD2 LEU A 26 1879 3430 1588 633 121 262 C ATOM 191 N LEU A 27 37.182 -1.283 44.957 1.00 13.76 N ANISOU 191 N LEU A 27 1206 2211 1813 -166 -15 350 N ATOM 192 CA LEU A 27 38.233 -1.935 44.157 1.00 13.95 C ANISOU 192 CA LEU A 27 1253 2449 1598 87 -162 514 C ATOM 193 C LEU A 27 39.402 -2.363 45.026 1.00 14.99 C ANISOU 193 C LEU A 27 1510 2357 1828 176 -413 475 C ATOM 194 O LEU A 27 39.828 -3.521 45.061 1.00 16.80 O ANISOU 194 O LEU A 27 1593 2398 2394 308 -195 467 O ATOM 195 CB LEU A 27 38.730 -0.942 43.091 1.00 13.08 C ANISOU 195 CB LEU A 27 1402 1963 1605 200 -72 428 C ATOM 196 CG LEU A 27 39.997 -1.365 42.337 1.00 13.61 C ANISOU 196 CG LEU A 27 1289 2206 1675 148 -116 311 C ATOM 197 CD1 LEU A 27 39.811 -2.691 41.612 1.00 16.66 C ANISOU 197 CD1 LEU A 27 1629 2359 2342 417 -255 -44 C ATOM 198 CD2 LEU A 27 40.403 -0.256 41.369 1.00 16.02 C ANISOU 198 CD2 LEU A 27 1314 2661 2113 209 65 743 C ATOM 199 N LYS A 28 39.958 -1.440 45.815 1.00 16.22 N ANISOU 199 N LYS A 28 1629 2448 2087 248 -659 439 N ATOM 200 CA LYS A 28 41.076 -1.821 46.671 1.00 16.70 C ANISOU 200 CA LYS A 28 1396 2912 2036 38 -605 805 C ATOM 201 C LYS A 28 40.632 -2.881 47.666 1.00 16.19 C ANISOU 201 C LYS A 28 1504 2952 1695 -24 -597 612 C ATOM 202 O LYS A 28 41.412 -3.796 47.998 1.00 19.31 O ANISOU 202 O LYS A 28 2061 3067 2209 311 -602 876 O ATOM 203 CB ALYS A 28 41.604 -0.617 47.452 0.50 20.81 C ANISOU 203 CB ALYS A 28 1877 3068 2961 -238 -1220 767 C ATOM 204 CB BLYS A 28 41.639 -0.618 47.416 0.50 21.22 C ANISOU 204 CB BLYS A 28 1983 3147 2932 -345 -1213 812 C ATOM 205 CG ALYS A 28 42.699 -0.991 48.475 0.50 22.94 C ANISOU 205 CG ALYS A 28 2497 3464 2756 -746 -1481 1250 C ATOM 206 CG BLYS A 28 42.780 -0.981 48.391 0.50 23.30 C ANISOU 206 CG BLYS A 28 2540 3692 2623 -701 -1432 1211 C ATOM 207 CD ALYS A 28 43.188 0.289 49.142 0.50 27.18 C ANISOU 207 CD ALYS A 28 3067 4409 2853 -1440 -1222 673 C ATOM 208 CD BLYS A 28 43.222 0.317 49.059 0.50 25.65 C ANISOU 208 CD BLYS A 28 2410 4150 3185 -872 -1414 806 C ATOM 209 CE ALYS A 28 43.980 0.033 50.406 0.50 29.77 C ANISOU 209 CE ALYS A 28 3633 4732 2945 -812 -1441 325 C ATOM 210 CE BLYS A 28 44.107 0.071 50.262 0.50 27.59 C ANISOU 210 CE BLYS A 28 3079 4632 2772 -311 -1380 304 C ATOM 211 NZ ALYS A 28 43.540 0.890 51.547 0.50 26.52 N ANISOU 211 NZ ALYS A 28 2990 4545 2540 -222 -1226 1049 N ATOM 212 NZ BLYS A 28 45.360 -0.634 49.896 0.50 24.63 N ANISOU 212 NZ BLYS A 28 3549 3370 2440 113 -974 2160 N ATOM 213 N LYS A 29 39.459 -2.740 48.251 1.00 17.29 N ANISOU 213 N LYS A 29 1448 2593 2527 -332 -493 779 N ATOM 214 CA LYS A 29 39.018 -3.697 49.281 1.00 16.08 C ANISOU 214 CA LYS A 29 1787 2368 1953 -8 -293 490 C ATOM 215 C LYS A 29 38.876 -5.101 48.732 1.00 16.84 C ANISOU 215 C LYS A 29 2217 2335 1847 6 -319 607 C ATOM 216 O LYS A 29 39.232 -6.102 49.380 1.00 20.33 O ANISOU 216 O LYS A 29 2560 2341 2825 -45 -1154 628 O ATOM 217 CB LYS A 29 37.643 -3.224 49.797 1.00 18.13 C ANISOU 217 CB LYS A 29 1868 3073 1949 -71 -122 95 C ATOM 218 CG LYS A 29 36.983 -4.176 50.792 1.00 18.67 C ANISOU 218 CG LYS A 29 1904 3640 1549 -159 -275 211 C ATOM 219 CD LYS A 29 35.674 -3.561 51.295 1.00 19.79 C ANISOU 219 CD LYS A 29 2173 3513 1834 -102 46 495 C ATOM 220 CE LYS A 29 34.995 -4.442 52.324 1.00 22.68 C ANISOU 220 CE LYS A 29 2206 4560 1850 -442 -96 889 C ATOM 221 NZ LYS A 29 33.705 -3.859 52.793 1.00 27.60 N ANISOU 221 NZ LYS A 29 1590 6609 2288 -512 -239 966 N ATOM 222 N HIS A 30 38.406 -5.261 47.498 1.00 16.34 N ANISOU 222 N HIS A 30 1745 2338 2124 177 -484 414 N ATOM 223 CA HIS A 30 38.011 -6.570 47.004 1.00 17.39 C ANISOU 223 CA HIS A 30 1489 2527 2590 38 -304 200 C ATOM 224 C HIS A 30 38.972 -7.160 45.999 1.00 16.59 C ANISOU 224 C HIS A 30 1653 2300 2351 148 -350 375 C ATOM 225 O HIS A 30 38.887 -8.372 45.787 1.00 17.90 O ANISOU 225 O HIS A 30 1915 2305 2580 212 -438 425 O ATOM 226 CB HIS A 30 36.587 -6.533 46.381 1.00 17.19 C ANISOU 226 CB HIS A 30 1557 2749 2224 -124 -257 581 C ATOM 227 CG HIS A 30 35.596 -6.404 47.509 1.00 16.52 C ANISOU 227 CG HIS A 30 1432 2445 2399 85 -285 823 C ATOM 228 ND1 HIS A 30 35.341 -7.414 48.403 1.00 19.06 N ANISOU 228 ND1 HIS A 30 2015 2681 2547 -103 -101 957 N ATOM 229 CD2 HIS A 30 34.825 -5.362 47.886 1.00 17.52 C ANISOU 229 CD2 HIS A 30 1897 2813 1948 249 -309 632 C ATOM 230 CE1 HIS A 30 34.465 -7.014 49.304 1.00 18.07 C ANISOU 230 CE1 HIS A 30 1598 3064 2203 -240 -455 764 C ATOM 231 NE2 HIS A 30 34.089 -5.778 48.977 1.00 16.58 N ANISOU 231 NE2 HIS A 30 1948 2829 1522 -317 -486 262 N ATOM 232 N LEU A 31 39.885 -6.375 45.435 1.00 17.03 N ANISOU 232 N LEU A 31 1512 2394 2565 308 -302 550 N ATOM 233 CA LEU A 31 40.887 -6.945 44.535 1.00 17.25 C ANISOU 233 CA LEU A 31 1633 2362 2561 406 -267 738 C ATOM 234 C LEU A 31 42.059 -7.501 45.343 1.00 18.36 C ANISOU 234 C LEU A 31 1831 2533 2611 728 -376 378 C ATOM 235 O LEU A 31 43.092 -6.851 45.510 1.00 21.59 O ANISOU 235 O LEU A 31 1766 3316 3120 560 -604 841 O ATOM 236 CB LEU A 31 41.387 -5.847 43.583 1.00 17.67 C ANISOU 236 CB LEU A 31 2184 1824 2706 500 128 439 C ATOM 237 CG LEU A 31 42.303 -6.389 42.472 1.00 17.36 C ANISOU 237 CG LEU A 31 1415 2284 2896 472 31 376 C ATOM 238 CD1 LEU A 31 41.607 -7.418 41.604 1.00 20.66 C ANISOU 238 CD1 LEU A 31 1685 2632 3532 391 465 -359 C ATOM 239 CD2 LEU A 31 42.837 -5.230 41.627 1.00 25.65 C ANISOU 239 CD2 LEU A 31 2348 2535 4863 297 1384 771 C ATOM 240 N THR A 32 41.814 -8.699 45.876 1.00 19.21 N ANISOU 240 N THR A 32 2388 2357 2556 919 -608 370 N ATOM 241 CA THR A 32 42.904 -9.403 46.575 1.00 20.44 C ANISOU 241 CA THR A 32 2156 2764 2846 811 -610 539 C ATOM 242 C THR A 32 43.880 -9.978 45.568 1.00 20.00 C ANISOU 242 C THR A 32 2044 2539 3018 687 -687 318 C ATOM 243 O THR A 32 43.561 -10.109 44.375 1.00 20.95 O ANISOU 243 O THR A 32 2444 2611 2906 628 -515 462 O ATOM 244 CB THR A 32 42.334 -10.579 47.394 1.00 21.22 C ANISOU 244 CB THR A 32 3213 2468 2382 974 -556 389 C ATOM 245 OG1 THR A 32 41.727 -11.526 46.518 1.00 22.52 O ANISOU 245 OG1 THR A 32 2913 2482 3163 911 -1037 348 O ATOM 246 CG2 THR A 32 41.312 -10.090 48.398 1.00 28.53 C ANISOU 246 CG2 THR A 32 4709 4404 1726 1558 129 980 C ATOM 247 N LYS A 33 45.079 -10.329 46.046 1.00 22.13 N ANISOU 247 N LYS A 33 2234 2584 3591 925 -783 329 N ATOM 248 CA LYS A 33 46.061 -10.965 45.164 1.00 22.68 C ANISOU 248 CA LYS A 33 2275 3125 3218 1132 -1024 145 C ATOM 249 C LYS A 33 45.449 -12.191 44.482 1.00 23.21 C ANISOU 249 C LYS A 33 2020 3039 3761 1228 -1118 33 C ATOM 250 O LYS A 33 45.651 -12.358 43.270 1.00 25.22 O ANISOU 250 O LYS A 33 3088 2593 3903 860 -924 -165 O ATOM 251 CB LYS A 33 47.349 -11.351 45.885 1.00 31.60 C ANISOU 251 CB LYS A 33 2142 5043 4823 1310 -1590 -656 C ATOM 252 CG LYS A 33 48.440 -11.931 44.994 1.00 39.10 C ANISOU 252 CG LYS A 33 2502 5917 6439 2013 -1244 -1036 C ATOM 253 CD LYS A 33 49.732 -12.191 45.748 1.00 45.33 C ANISOU 253 CD LYS A 33 2602 6743 7879 2172 -1670 -625 C ATOM 254 CE LYS A 33 50.306 -13.577 45.466 1.00 45.21 C ANISOU 254 CE LYS A 33 3007 7171 7001 2661 -1716 -742 C ATOM 255 NZ LYS A 33 51.731 -13.526 45.063 1.00 43.55 N ANISOU 255 NZ LYS A 33 4387 6842 5318 2370 760 200 N ATOM 256 N ASP A 34 44.698 -13.008 45.209 1.00 24.66 N ANISOU 256 N ASP A 34 2556 2729 4084 1332 -894 150 N ATOM 257 CA ASP A 34 44.073 -14.183 44.608 1.00 28.46 C ANISOU 257 CA ASP A 34 3532 2699 4582 981 -1348 429 C ATOM 258 C ASP A 34 43.108 -13.807 43.493 1.00 24.46 C ANISOU 258 C ASP A 34 2806 2654 3833 1003 -697 116 C ATOM 259 O ASP A 34 43.110 -14.414 42.412 1.00 26.68 O ANISOU 259 O ASP A 34 2876 2897 4363 923 -761 -490 O ATOM 260 CB ASP A 34 43.339 -15.028 45.651 1.00 39.65 C ANISOU 260 CB ASP A 34 4737 3644 6685 389 -2092 2708 C ATOM 261 CG ASP A 34 42.814 -16.330 45.076 1.00 52.74 C ANISOU 261 CG ASP A 34 6686 3169 10183 36 -2422 2612 C ATOM 262 OD1 ASP A 34 41.608 -16.433 44.750 1.00 73.00 O ANISOU 262 OD1 ASP A 34 7079 6559 14097 -2070 -3014 1102 O ATOM 263 OD2 ASP A 34 43.614 -17.291 44.962 1.00 86.86 O ANISOU 263 OD2 ASP A 34 11526 4331 17148 2610 -3010 714 O ATOM 264 N VAL A 35 42.201 -12.868 43.817 1.00 21.91 N ANISOU 264 N VAL A 35 2608 2577 3140 709 -528 249 N ATOM 265 CA VAL A 35 41.240 -12.461 42.800 1.00 20.47 C ANISOU 265 CA VAL A 35 2274 2359 3146 656 -341 336 C ATOM 266 C VAL A 35 41.968 -11.925 41.577 1.00 18.60 C ANISOU 266 C VAL A 35 1595 2484 2987 668 -462 47 C ATOM 267 O VAL A 35 41.642 -12.295 40.441 1.00 20.91 O ANISOU 267 O VAL A 35 2308 2623 3015 754 -554 -29 O ATOM 268 CB VAL A 35 40.233 -11.436 43.345 1.00 21.31 C ANISOU 268 CB VAL A 35 2613 2619 2866 881 158 883 C ATOM 269 CG1 VAL A 35 39.392 -10.856 42.204 1.00 19.29 C ANISOU 269 CG1 VAL A 35 2402 2381 2548 795 -82 239 C ATOM 270 CG2 VAL A 35 39.340 -12.114 44.378 1.00 22.44 C ANISOU 270 CG2 VAL A 35 2060 3133 3334 314 -187 1173 C ATOM 271 N PHE A 36 42.916 -11.015 41.818 1.00 20.02 N ANISOU 271 N PHE A 36 1394 2659 3554 685 -381 26 N ATOM 272 CA PHE A 36 43.719 -10.436 40.734 1.00 19.91 C ANISOU 272 CA PHE A 36 1917 2414 3234 355 -193 -550 C ATOM 273 C PHE A 36 44.402 -11.504 39.904 1.00 21.03 C ANISOU 273 C PHE A 36 2528 2459 3002 879 -467 -426 C ATOM 274 O PHE A 36 44.258 -11.521 38.674 1.00 20.83 O ANISOU 274 O PHE A 36 2006 2824 3086 770 -544 -595 O ATOM 275 CB PHE A 36 44.771 -9.520 41.371 1.00 19.73 C ANISOU 275 CB PHE A 36 2042 2508 2945 288 -403 -275 C ATOM 276 CG PHE A 36 45.723 -8.854 40.414 1.00 20.53 C ANISOU 276 CG PHE A 36 1721 2515 3563 472 -333 -15 C ATOM 277 CD1 PHE A 36 45.295 -7.905 39.498 1.00 21.56 C ANISOU 277 CD1 PHE A 36 2027 2925 3241 723 3 103 C ATOM 278 CD2 PHE A 36 47.064 -9.213 40.412 1.00 25.46 C ANISOU 278 CD2 PHE A 36 2059 3290 4326 1181 183 214 C ATOM 279 CE1 PHE A 36 46.195 -7.345 38.609 1.00 20.17 C ANISOU 279 CE1 PHE A 36 1778 3120 2765 792 42 -295 C ATOM 280 CE2 PHE A 36 47.959 -8.616 39.548 1.00 24.79 C ANISOU 280 CE2 PHE A 36 1570 4267 3582 778 -385 136 C ATOM 281 CZ PHE A 36 47.547 -7.644 38.675 1.00 20.21 C ANISOU 281 CZ PHE A 36 1806 3174 2700 786 -249 -721 C ATOM 282 N ASP A 37 45.127 -12.444 40.532 1.00 23.15 N ANISOU 282 N ASP A 37 2314 3005 3478 995 -875 -520 N ATOM 283 CA ASP A 37 45.811 -13.468 39.724 1.00 26.23 C ANISOU 283 CA ASP A 37 1899 2994 5074 1097 -949 -890 C ATOM 284 C ASP A 37 44.808 -14.327 38.961 1.00 23.63 C ANISOU 284 C ASP A 37 2337 2352 4291 679 -520 -516 C ATOM 285 O ASP A 37 45.096 -14.793 37.852 1.00 26.86 O ANISOU 285 O ASP A 37 2883 2459 4865 833 -118 -983 O ATOM 286 CB ASP A 37 46.691 -14.376 40.580 1.00 31.27 C ANISOU 286 CB ASP A 37 2227 3371 6282 1146 -1342 -349 C ATOM 287 CG ASP A 37 47.906 -13.648 41.127 1.00 30.98 C ANISOU 287 CG ASP A 37 2193 3230 6349 1360 -1522 -386 C ATOM 288 OD1 ASP A 37 48.281 -12.555 40.651 1.00 29.83 O ANISOU 288 OD1 ASP A 37 2543 3224 5569 1151 -1123 -829 O ATOM 289 OD2 ASP A 37 48.530 -14.235 42.046 1.00 31.69 O ANISOU 289 OD2 ASP A 37 2978 3872 5191 1331 -1406 -695 O ATOM 290 N SER A 38 43.621 -14.529 39.526 1.00 22.22 N ANISOU 290 N SER A 38 2352 2106 3983 630 -651 -141 N ATOM 291 CA SER A 38 42.646 -15.398 38.878 1.00 21.48 C ANISOU 291 CA SER A 38 2989 2143 3031 11 -49 -75 C ATOM 292 C SER A 38 42.096 -14.803 37.591 1.00 21.54 C ANISOU 292 C SER A 38 2525 2539 3120 834 -147 -382 C ATOM 293 O SER A 38 41.613 -15.536 36.721 1.00 26.53 O ANISOU 293 O SER A 38 3536 2727 3816 1111 -1005 -607 O ATOM 294 CB SER A 38 41.519 -15.746 39.852 1.00 23.63 C ANISOU 294 CB SER A 38 3108 2164 3707 260 474 -263 C ATOM 295 OG SER A 38 40.627 -14.660 40.079 1.00 29.00 O ANISOU 295 OG SER A 38 2818 3457 4745 1168 -234 -82 O ATOM 296 N ILE A 39 42.116 -13.473 37.437 1.00 18.99 N ANISOU 296 N ILE A 39 1736 2671 2808 613 48 -53 N ATOM 297 CA ILE A 39 41.443 -12.891 36.280 1.00 19.07 C ANISOU 297 CA ILE A 39 1677 2721 2848 639 -105 -229 C ATOM 298 C ILE A 39 42.317 -11.966 35.469 1.00 17.56 C ANISOU 298 C ILE A 39 1557 2592 2524 817 -123 -239 C ATOM 299 O ILE A 39 41.912 -11.575 34.375 1.00 20.91 O ANISOU 299 O ILE A 39 1870 3577 2499 1016 -6 -145 O ATOM 300 CB ILE A 39 40.169 -12.147 36.715 1.00 18.22 C ANISOU 300 CB ILE A 39 1598 2496 2828 421 0 -38 C ATOM 301 CG1 ILE A 39 40.477 -11.020 37.707 1.00 22.25 C ANISOU 301 CG1 ILE A 39 1725 3115 3613 310 466 -800 C ATOM 302 CG2 ILE A 39 39.182 -13.121 37.329 1.00 21.13 C ANISOU 302 CG2 ILE A 39 2350 2273 3407 525 689 159 C ATOM 303 CD1 ILE A 39 39.291 -10.252 38.213 1.00 17.77 C ANISOU 303 CD1 ILE A 39 1583 2580 2589 802 -138 204 C ATOM 304 N LYS A 40 43.556 -11.682 35.844 1.00 18.72 N ANISOU 304 N LYS A 40 1675 2455 2984 697 -118 -251 N ATOM 305 CA LYS A 40 44.342 -10.691 35.123 1.00 19.21 C ANISOU 305 CA LYS A 40 1951 2376 2973 540 -279 -192 C ATOM 306 C LYS A 40 44.759 -11.115 33.720 1.00 20.72 C ANISOU 306 C LYS A 40 1638 2862 3372 413 210 -338 C ATOM 307 O LYS A 40 45.055 -10.236 32.886 1.00 21.45 O ANISOU 307 O LYS A 40 1936 3005 3209 757 241 -213 O ATOM 308 CB LYS A 40 45.578 -10.336 35.962 1.00 21.56 C ANISOU 308 CB LYS A 40 1798 2495 3901 616 -453 -420 C ATOM 309 CG LYS A 40 46.516 -11.547 36.142 1.00 23.35 C ANISOU 309 CG LYS A 40 2219 3014 3641 1097 -429 -173 C ATOM 310 CD LYS A 40 47.626 -11.163 37.119 1.00 26.44 C ANISOU 310 CD LYS A 40 2504 3684 3860 1376 -718 -515 C ATOM 311 CE LYS A 40 48.654 -12.291 37.243 1.00 26.41 C ANISOU 311 CE LYS A 40 2539 3648 3847 1383 -727 -432 C ATOM 312 NZ LYS A 40 49.541 -12.037 38.419 1.00 29.25 N ANISOU 312 NZ LYS A 40 2383 5080 3652 1498 -566 -331 N ATOM 313 N ASN A 41 44.726 -12.408 33.414 1.00 20.91 N ANISOU 313 N ASN A 41 1710 2803 3432 964 87 -441 N ATOM 314 CA ASN A 41 45.083 -12.873 32.068 1.00 23.24 C ANISOU 314 CA ASN A 41 2118 3343 3369 1555 178 -294 C ATOM 315 C ASN A 41 43.837 -13.098 31.208 1.00 21.37 C ANISOU 315 C ASN A 41 2173 3079 2867 1020 477 -282 C ATOM 316 O ASN A 41 43.915 -13.679 30.117 1.00 25.70 O ANISOU 316 O ASN A 41 2874 4153 2739 1251 667 -480 O ATOM 317 CB ASN A 41 45.862 -14.200 32.130 1.00 25.70 C ANISOU 317 CB ASN A 41 2841 3206 3719 1600 -27 -666 C ATOM 318 CG ASN A 41 47.157 -14.091 32.903 1.00 27.93 C ANISOU 318 CG ASN A 41 2568 3293 4750 1579 -161 454 C ATOM 319 OD1 ASN A 41 47.283 -14.639 34.004 1.00 34.37 O ANISOU 319 OD1 ASN A 41 3979 5445 3636 1818 -273 -164 O ATOM 320 ND2 ASN A 41 48.099 -13.326 32.370 1.00 34.75 N ANISOU 320 ND2 ASN A 41 2610 3656 6938 1474 992 -19 N ATOM 321 N LYS A 42 42.657 -12.711 31.709 1.00 20.87 N ANISOU 321 N LYS A 42 1898 3213 2818 657 380 -560 N ATOM 322 CA LYS A 42 41.431 -12.986 30.945 1.00 22.31 C ANISOU 322 CA LYS A 42 2161 3865 2452 658 225 -374 C ATOM 323 C LYS A 42 41.066 -11.806 30.054 1.00 23.24 C ANISOU 323 C LYS A 42 2429 4103 2300 978 619 -249 C ATOM 324 O LYS A 42 41.433 -10.656 30.299 1.00 23.45 O ANISOU 324 O LYS A 42 1990 4009 2912 1195 82 -83 O ATOM 325 CB LYS A 42 40.267 -13.303 31.886 1.00 20.01 C ANISOU 325 CB LYS A 42 1976 3013 2614 488 137 -488 C ATOM 326 CG LYS A 42 40.465 -14.586 32.683 1.00 23.05 C ANISOU 326 CG LYS A 42 2513 3836 2408 922 -168 13 C ATOM 327 CD LYS A 42 39.155 -14.957 33.367 1.00 32.98 C ANISOU 327 CD LYS A 42 4791 2870 4872 860 2628 -231 C ATOM 328 CE LYS A 42 39.284 -16.179 34.257 1.00 45.67 C ANISOU 328 CE LYS A 42 7098 3824 6431 656 2528 1043 C ATOM 329 NZ LYS A 42 40.229 -17.188 33.702 1.00 54.90 N ANISOU 329 NZ LYS A 42 9375 4116 7371 2456 3327 2533 N ATOM 330 N LYS A 43 40.318 -12.133 29.006 1.00 25.07 N ANISOU 330 N LYS A 43 3069 3712 2743 1631 24 -524 N ATOM 331 CA LYS A 43 39.906 -11.127 28.025 1.00 23.50 C ANISOU 331 CA LYS A 43 2170 3862 2898 1259 399 -126 C ATOM 332 C LYS A 43 38.531 -11.466 27.479 1.00 23.54 C ANISOU 332 C LYS A 43 2339 3899 2706 1012 369 -89 C ATOM 333 O LYS A 43 38.167 -12.633 27.357 1.00 23.36 O ANISOU 333 O LYS A 43 2786 3889 2201 1097 180 -293 O ATOM 334 CB LYS A 43 40.985 -11.103 26.935 1.00 32.60 C ANISOU 334 CB LYS A 43 2826 5415 4147 511 1352 -7 C ATOM 335 CG LYS A 43 40.998 -9.886 26.030 1.00 31.30 C ANISOU 335 CG LYS A 43 3674 5233 2986 -494 903 -615 C ATOM 336 CD LYS A 43 42.124 -9.990 25.005 1.00 29.24 C ANISOU 336 CD LYS A 43 2950 4850 3310 -830 641 -998 C ATOM 337 CE LYS A 43 41.640 -10.823 23.838 1.00 31.08 C ANISOU 337 CE LYS A 43 3294 4601 3916 -495 944 -1640 C ATOM 338 NZ LYS A 43 42.685 -10.892 22.776 1.00 31.94 N ANISOU 338 NZ LYS A 43 3959 4793 3386 -197 1075 -795 N ATOM 339 N THR A 44 37.693 -10.460 27.233 1.00 20.99 N ANISOU 339 N THR A 44 2087 3809 2081 927 226 -604 N ATOM 340 CA THR A 44 36.376 -10.734 26.660 1.00 20.02 C ANISOU 340 CA THR A 44 2374 3345 1889 826 79 -920 C ATOM 341 C THR A 44 36.448 -10.915 25.141 1.00 23.25 C ANISOU 341 C THR A 44 2320 4651 1862 1329 358 -887 C ATOM 342 O THR A 44 37.502 -10.636 24.565 1.00 30.84 O ANISOU 342 O THR A 44 2710 5937 3071 1695 1278 -756 O ATOM 343 CB THR A 44 35.354 -9.638 26.980 1.00 18.10 C ANISOU 343 CB THR A 44 2000 3116 1762 673 351 -555 C ATOM 344 OG1 THR A 44 35.676 -8.422 26.307 1.00 19.86 O ANISOU 344 OG1 THR A 44 2247 3439 1859 675 521 -290 O ATOM 345 CG2 THR A 44 35.363 -9.390 28.483 1.00 19.44 C ANISOU 345 CG2 THR A 44 3547 2053 1788 756 214 -511 C ATOM 346 N GLY A 45 35.314 -11.279 24.564 1.00 25.03 N ANISOU 346 N GLY A 45 3066 4668 1778 1264 -290 -782 N ATOM 347 CA GLY A 45 35.209 -11.439 23.112 1.00 29.24 C ANISOU 347 CA GLY A 45 3361 6001 1749 1860 8 -993 C ATOM 348 C GLY A 45 35.438 -10.104 22.433 1.00 28.99 C ANISOU 348 C GLY A 45 2776 6722 1517 1543 424 -502 C ATOM 349 O GLY A 45 35.832 -10.117 21.270 1.00 40.50 O ANISOU 349 O GLY A 45 4406 8987 1996 1927 1373 -289 O ATOM 350 N MET A 46 35.226 -8.971 23.083 1.00 30.26 N ANISOU 350 N MET A 46 3049 6046 2403 1459 792 -92 N ATOM 351 CA MET A 46 35.446 -7.644 22.516 1.00 30.92 C ANISOU 351 CA MET A 46 3080 6591 2077 1737 503 550 C ATOM 352 C MET A 46 36.841 -7.106 22.842 1.00 29.11 C ANISOU 352 C MET A 46 3130 6175 1755 1481 968 777 C ATOM 353 O MET A 46 37.199 -5.973 22.509 1.00 37.88 O ANISOU 353 O MET A 46 2905 7177 4310 1569 1456 2785 O ATOM 354 CB AMET A 46 34.442 -6.669 23.149 0.50 32.50 C ANISOU 354 CB AMET A 46 2973 5697 3680 904 1060 -16 C ATOM 355 CB BMET A 46 34.360 -6.670 22.967 0.50 32.34 C ANISOU 355 CB BMET A 46 3057 5840 3393 1175 663 -67 C ATOM 356 CG AMET A 46 32.978 -7.025 22.969 0.50 35.01 C ANISOU 356 CG AMET A 46 2901 6013 4387 1100 787 -46 C ATOM 357 CG BMET A 46 33.116 -6.564 22.098 0.50 34.88 C ANISOU 357 CG BMET A 46 2848 5737 4670 1376 381 -63 C ATOM 358 SD AMET A 46 32.081 -5.601 22.292 0.50 35.74 S ANISOU 358 SD AMET A 46 3748 6212 3619 2273 1249 -940 S ATOM 359 SD BMET A 46 31.769 -5.713 22.965 0.50 43.76 S ANISOU 359 SD BMET A 46 3432 7233 5964 1795 1151 -245 S ATOM 360 CE AMET A 46 33.147 -5.251 20.885 0.50 35.78 C ANISOU 360 CE AMET A 46 2280 10057 1256 2654 -934 275 C ATOM 361 CE BMET A 46 30.616 -5.400 21.637 0.50 47.23 C ANISOU 361 CE BMET A 46 3402 8143 6402 2851 1211 -19 C ATOM 362 N GLY A 47 37.620 -7.881 23.582 1.00 25.27 N ANISOU 362 N GLY A 47 2663 5083 1856 1003 724 298 N ATOM 363 CA GLY A 47 38.998 -7.543 23.901 1.00 25.74 C ANISOU 363 CA GLY A 47 2783 4608 2391 724 814 312 C ATOM 364 C GLY A 47 39.168 -6.739 25.170 1.00 26.32 C ANISOU 364 C GLY A 47 2830 4991 2179 541 641 455 C ATOM 365 O GLY A 47 40.229 -6.156 25.423 1.00 25.93 O ANISOU 365 O GLY A 47 2758 3951 3145 918 419 393 O ATOM 366 N ALA A 48 38.102 -6.667 25.967 1.00 23.72 N ANISOU 366 N ALA A 48 2558 3913 2541 1231 448 105 N ATOM 367 CA ALA A 48 38.205 -5.964 27.238 1.00 22.03 C ANISOU 367 CA ALA A 48 2307 3540 2522 902 483 298 C ATOM 368 C ALA A 48 39.054 -6.779 28.201 1.00 19.26 C ANISOU 368 C ALA A 48 1637 3130 2553 300 702 652 C ATOM 369 O ALA A 48 38.895 -8.002 28.324 1.00 21.79 O ANISOU 369 O ALA A 48 1955 2993 3331 374 662 373 O ATOM 370 CB ALA A 48 36.835 -5.743 27.845 1.00 20.22 C ANISOU 370 CB ALA A 48 1770 3806 2106 532 -46 -115 C ATOM 371 N THR A 49 39.975 -6.068 28.850 1.00 18.92 N ANISOU 371 N THR A 49 1824 3001 2363 432 801 338 N ATOM 372 CA THR A 49 40.831 -6.742 29.825 1.00 18.65 C ANISOU 372 CA THR A 49 1943 2723 2422 345 577 202 C ATOM 373 C THR A 49 40.529 -6.227 31.220 1.00 17.40 C ANISOU 373 C THR A 49 1916 2255 2440 160 523 208 C ATOM 374 O THR A 49 39.800 -5.251 31.425 1.00 18.62 O ANISOU 374 O THR A 49 1767 2698 2609 353 358 14 O ATOM 375 CB THR A 49 42.329 -6.505 29.526 1.00 22.40 C ANISOU 375 CB THR A 49 1821 3795 2896 318 557 -780 C ATOM 376 OG1 THR A 49 42.565 -5.122 29.853 1.00 23.15 O ANISOU 376 OG1 THR A 49 1802 3520 3473 69 1011 -172 O ATOM 377 CG2 THR A 49 42.601 -6.660 28.038 1.00 24.06 C ANISOU 377 CG2 THR A 49 1418 4969 2756 482 484 -361 C ATOM 378 N LEU A 50 41.190 -6.795 32.219 1.00 18.50 N ANISOU 378 N LEU A 50 1728 2860 2440 471 490 114 N ATOM 379 CA LEU A 50 41.035 -6.300 33.587 1.00 17.52 C ANISOU 379 CA LEU A 50 1708 2492 2458 446 562 194 C ATOM 380 C LEU A 50 41.468 -4.855 33.721 1.00 17.93 C ANISOU 380 C LEU A 50 1225 2590 2998 429 536 73 C ATOM 381 O LEU A 50 40.940 -4.094 34.541 1.00 18.98 O ANISOU 381 O LEU A 50 1677 2467 3069 674 617 190 O ATOM 382 CB LEU A 50 41.820 -7.183 34.562 1.00 18.32 C ANISOU 382 CB LEU A 50 1694 2729 2538 442 163 28 C ATOM 383 CG LEU A 50 41.663 -6.812 36.035 1.00 16.58 C ANISOU 383 CG LEU A 50 1400 2255 2644 490 79 -171 C ATOM 384 CD1 LEU A 50 40.205 -7.022 36.470 1.00 19.89 C ANISOU 384 CD1 LEU A 50 1715 2430 3411 497 686 392 C ATOM 385 CD2 LEU A 50 42.588 -7.670 36.897 1.00 18.65 C ANISOU 385 CD2 LEU A 50 1932 2460 2696 567 117 268 C ATOM 386 N LEU A 51 42.439 -4.434 32.926 1.00 17.69 N ANISOU 386 N LEU A 51 1282 2759 2679 291 330 197 N ATOM 387 CA LEU A 51 42.872 -3.045 32.967 1.00 17.24 C ANISOU 387 CA LEU A 51 1212 2745 2595 278 331 88 C ATOM 388 C LEU A 51 41.730 -2.104 32.590 1.00 18.26 C ANISOU 388 C LEU A 51 1754 3014 2169 734 452 188 C ATOM 389 O LEU A 51 41.533 -1.037 33.195 1.00 18.73 O ANISOU 389 O LEU A 51 1886 2672 2557 338 950 324 O ATOM 390 CB LEU A 51 44.080 -2.807 32.057 1.00 20.53 C ANISOU 390 CB LEU A 51 1752 2498 3550 323 1034 58 C ATOM 391 CG LEU A 51 44.706 -1.415 32.175 1.00 21.39 C ANISOU 391 CG LEU A 51 1901 3239 2987 -393 924 -456 C ATOM 392 CD1 LEU A 51 45.136 -1.119 33.606 1.00 23.57 C ANISOU 392 CD1 LEU A 51 1945 3784 3226 293 13 100 C ATOM 393 CD2 LEU A 51 45.856 -1.283 31.189 1.00 23.09 C ANISOU 393 CD2 LEU A 51 1606 3138 4028 85 1322 -267 C ATOM 394 N ASP A 52 40.961 -2.451 31.552 1.00 17.95 N ANISOU 394 N ASP A 52 1766 3102 1953 694 460 512 N ATOM 395 CA ASP A 52 39.829 -1.627 31.168 1.00 17.78 C ANISOU 395 CA ASP A 52 1408 3121 2227 453 575 629 C ATOM 396 C ASP A 52 38.841 -1.536 32.330 1.00 18.35 C ANISOU 396 C ASP A 52 2262 2567 2144 746 863 504 C ATOM 397 O ASP A 52 38.196 -0.508 32.597 1.00 22.09 O ANISOU 397 O ASP A 52 2189 2856 3349 1058 1007 739 O ATOM 398 CB ASP A 52 39.158 -2.250 29.931 1.00 19.09 C ANISOU 398 CB ASP A 52 1763 3353 2138 1118 445 238 C ATOM 399 CG ASP A 52 40.156 -2.314 28.780 1.00 20.17 C ANISOU 399 CG ASP A 52 1780 3164 2718 435 790 -100 C ATOM 400 OD1 ASP A 52 40.702 -1.248 28.470 1.00 20.44 O ANISOU 400 OD1 ASP A 52 2135 3190 2442 592 243 555 O ATOM 401 OD2 ASP A 52 40.398 -3.380 28.198 1.00 23.45 O ANISOU 401 OD2 ASP A 52 2975 3326 2608 609 1072 -160 O ATOM 402 N VAL A 53 38.658 -2.643 33.046 1.00 15.48 N ANISOU 402 N VAL A 53 1473 2472 1935 301 481 276 N ATOM 403 CA VAL A 53 37.731 -2.685 34.171 1.00 14.52 C ANISOU 403 CA VAL A 53 1216 2542 1760 289 231 337 C ATOM 404 C VAL A 53 38.182 -1.796 35.316 1.00 14.14 C ANISOU 404 C VAL A 53 1206 2364 1803 331 339 327 C ATOM 405 O VAL A 53 37.386 -1.033 35.894 1.00 15.45 O ANISOU 405 O VAL A 53 1419 2120 2333 549 424 355 O ATOM 406 CB VAL A 53 37.544 -4.141 34.652 1.00 13.75 C ANISOU 406 CB VAL A 53 1348 2427 1451 482 140 245 C ATOM 407 CG1 VAL A 53 36.779 -4.204 35.968 1.00 14.27 C ANISOU 407 CG1 VAL A 53 1451 2160 1812 437 543 123 C ATOM 408 CG2 VAL A 53 36.874 -4.987 33.578 1.00 16.38 C ANISOU 408 CG2 VAL A 53 1684 2672 1869 323 218 -142 C ATOM 409 N ILE A 54 39.464 -1.877 35.678 1.00 15.19 N ANISOU 409 N ILE A 54 1364 2337 2069 381 75 169 N ATOM 410 CA ILE A 54 39.942 -1.257 36.914 1.00 13.92 C ANISOU 410 CA ILE A 54 1299 1970 2021 485 108 226 C ATOM 411 C ILE A 54 40.658 0.070 36.724 1.00 15.02 C ANISOU 411 C ILE A 54 1263 2193 2252 344 -127 442 C ATOM 412 O ILE A 54 40.973 0.740 37.730 1.00 15.48 O ANISOU 412 O ILE A 54 1138 2331 2412 248 -243 370 O ATOM 413 CB ILE A 54 40.830 -2.178 37.791 1.00 15.22 C ANISOU 413 CB ILE A 54 1230 2343 2212 260 128 641 C ATOM 414 CG1 ILE A 54 42.255 -2.329 37.210 1.00 18.41 C ANISOU 414 CG1 ILE A 54 1128 3133 2734 532 160 579 C ATOM 415 CG2 ILE A 54 40.179 -3.540 37.995 1.00 15.74 C ANISOU 415 CG2 ILE A 54 1671 2092 2216 292 127 426 C ATOM 416 CD1 ILE A 54 43.206 -3.099 38.122 1.00 21.65 C ANISOU 416 CD1 ILE A 54 1592 3058 3578 589 -348 697 C ATOM 417 N GLN A 55 40.982 0.474 35.505 1.00 15.31 N ANISOU 417 N GLN A 55 1190 2276 2351 165 109 327 N ATOM 418 CA GLN A 55 41.876 1.637 35.345 1.00 16.25 C ANISOU 418 CA GLN A 55 1495 1950 2730 243 90 290 C ATOM 419 C GLN A 55 41.311 2.884 36.019 1.00 15.64 C ANISOU 419 C GLN A 55 1356 2336 2252 217 77 163 C ATOM 420 O GLN A 55 42.055 3.699 36.608 1.00 15.36 O ANISOU 420 O GLN A 55 1406 2301 2130 189 46 217 O ATOM 421 CB GLN A 55 42.118 1.881 33.858 1.00 22.29 C ANISOU 421 CB GLN A 55 2599 2766 3105 102 1523 68 C ATOM 422 CG GLN A 55 43.024 3.053 33.524 1.00 26.12 C ANISOU 422 CG GLN A 55 2228 4735 2962 -899 -348 1445 C ATOM 423 CD GLN A 55 43.249 3.069 32.018 1.00 37.06 C ANISOU 423 CD GLN A 55 3598 7147 3337 1283 999 3015 C ATOM 424 OE1 GLN A 55 42.382 3.553 31.281 1.00 52.25 O ANISOU 424 OE1 GLN A 55 4595 12442 2814 2923 341 2277 O ATOM 425 NE2 GLN A 55 44.382 2.515 31.618 1.00 38.36 N ANISOU 425 NE2 GLN A 55 4278 5569 4729 1233 1135 1608 N ATOM 426 N SER A 56 39.988 3.080 36.019 1.00 14.60 N ANISOU 426 N SER A 56 1291 2305 1951 268 127 235 N ATOM 427 CA SER A 56 39.484 4.334 36.601 1.00 12.85 C ANISOU 427 CA SER A 56 1134 2045 1704 -35 -190 211 C ATOM 428 C SER A 56 39.745 4.386 38.106 1.00 12.99 C ANISOU 428 C SER A 56 870 2365 1701 -81 -27 316 C ATOM 429 O SER A 56 40.084 5.428 38.696 1.00 14.68 O ANISOU 429 O SER A 56 1371 2408 1800 -113 -380 269 O ATOM 430 CB SER A 56 37.973 4.412 36.377 1.00 13.79 C ANISOU 430 CB SER A 56 1184 2240 1817 317 -236 192 C ATOM 431 OG SER A 56 37.439 5.595 36.972 1.00 12.91 O ANISOU 431 OG SER A 56 1186 1859 1860 -61 -122 102 O ATOM 432 N GLY A 57 39.646 3.232 38.758 1.00 13.36 N ANISOU 432 N GLY A 57 1050 2326 1702 46 -207 383 N ATOM 433 CA GLY A 57 39.871 3.156 40.180 1.00 13.21 C ANISOU 433 CA GLY A 57 1009 2342 1669 58 -211 283 C ATOM 434 C GLY A 57 41.359 3.202 40.517 1.00 15.02 C ANISOU 434 C GLY A 57 1029 2750 1928 -107 -218 668 C ATOM 435 O GLY A 57 41.699 3.578 41.635 1.00 16.20 O ANISOU 435 O GLY A 57 1317 2587 2253 -162 -576 442 O ATOM 436 N VAL A 58 42.214 2.737 39.616 1.00 16.45 N ANISOU 436 N VAL A 58 1003 2868 2378 -25 -53 583 N ATOM 437 CA VAL A 58 43.658 2.833 39.827 1.00 16.97 C ANISOU 437 CA VAL A 58 1071 2993 2383 -64 -168 325 C ATOM 438 C VAL A 58 44.093 4.293 39.715 1.00 18.02 C ANISOU 438 C VAL A 58 1011 3002 2833 -48 -35 334 C ATOM 439 O VAL A 58 44.880 4.809 40.498 1.00 20.10 O ANISOU 439 O VAL A 58 1282 2837 3518 -143 -565 689 O ATOM 440 CB VAL A 58 44.408 1.956 38.830 1.00 16.44 C ANISOU 440 CB VAL A 58 961 2855 2431 -89 26 577 C ATOM 441 CG1 VAL A 58 45.894 2.267 38.826 1.00 24.11 C ANISOU 441 CG1 VAL A 58 760 4181 4221 204 112 1530 C ATOM 442 CG2 VAL A 58 44.136 0.484 39.143 1.00 19.76 C ANISOU 442 CG2 VAL A 58 1823 2741 2946 206 -414 764 C ATOM 443 N GLU A 59 43.558 5.001 38.735 1.00 17.44 N ANISOU 443 N GLU A 59 1417 2679 2531 41 -15 120 N ATOM 444 CA GLU A 59 44.009 6.362 38.449 1.00 17.28 C ANISOU 444 CA GLU A 59 1079 2719 2767 -177 -92 -2 C ATOM 445 C GLU A 59 43.360 7.344 39.421 1.00 16.32 C ANISOU 445 C GLU A 59 1254 2665 2283 -312 -86 86 C ATOM 446 O GLU A 59 43.898 8.413 39.704 1.00 18.48 O ANISOU 446 O GLU A 59 1736 2551 2735 -451 219 176 O ATOM 447 CB GLU A 59 43.686 6.746 36.997 1.00 18.54 C ANISOU 447 CB GLU A 59 1892 2670 2482 -312 564 33 C ATOM 448 CG GLU A 59 44.397 5.879 35.947 1.00 21.79 C ANISOU 448 CG GLU A 59 1989 3097 3192 -390 499 -718 C ATOM 449 CD GLU A 59 45.893 5.888 36.159 1.00 26.19 C ANISOU 449 CD GLU A 59 1815 3412 4726 -435 973 -465 C ATOM 450 OE1 GLU A 59 46.479 4.790 36.106 1.00 33.56 O ANISOU 450 OE1 GLU A 59 2310 3975 6466 236 1361 -122 O ATOM 451 OE2 GLU A 59 46.444 6.996 36.378 1.00 33.35 O ANISOU 451 OE2 GLU A 59 2246 4240 6185 -1151 1294 -1235 O ATOM 452 N ASN A 60 42.127 7.047 39.820 1.00 14.90 N ANISOU 452 N ASN A 60 1180 2511 1970 -100 -208 411 N ATOM 453 CA ASN A 60 41.385 7.922 40.745 1.00 14.20 C ANISOU 453 CA ASN A 60 999 2508 1889 -177 -247 566 C ATOM 454 C ASN A 60 41.265 7.190 42.072 1.00 14.42 C ANISOU 454 C ASN A 60 1263 2382 1834 -169 -331 455 C ATOM 455 O ASN A 60 40.306 6.450 42.322 1.00 14.22 O ANISOU 455 O ASN A 60 1222 2370 1811 -148 -194 546 O ATOM 456 CB ASN A 60 39.972 8.242 40.234 1.00 16.49 C ANISOU 456 CB ASN A 60 935 3248 2083 -113 -246 905 C ATOM 457 CG ASN A 60 40.066 9.029 38.925 1.00 15.53 C ANISOU 457 CG ASN A 60 1030 2776 2095 -205 -288 807 C ATOM 458 OD1 ASN A 60 40.356 10.231 38.921 1.00 18.69 O ANISOU 458 OD1 ASN A 60 1215 2929 2959 -456 -668 1036 O ATOM 459 ND2 ASN A 60 39.795 8.298 37.864 1.00 17.73 N ANISOU 459 ND2 ASN A 60 1498 3119 2120 215 -123 544 N ATOM 460 N LEU A 61 42.285 7.360 42.904 1.00 15.64 N ANISOU 460 N LEU A 61 1469 2512 1963 -59 -530 423 N ATOM 461 CA LEU A 61 42.317 6.598 44.156 1.00 15.15 C ANISOU 461 CA LEU A 61 1505 2280 1973 -220 -582 393 C ATOM 462 C LEU A 61 41.233 7.036 45.124 1.00 14.75 C ANISOU 462 C LEU A 61 1717 2101 1786 -285 -585 377 C ATOM 463 O LEU A 61 40.931 6.278 46.032 1.00 18.69 O ANISOU 463 O LEU A 61 2027 3002 2071 -45 -403 1004 O ATOM 464 CB LEU A 61 43.723 6.682 44.761 1.00 16.04 C ANISOU 464 CB LEU A 61 1704 2079 2313 -28 -919 61 C ATOM 465 CG LEU A 61 44.767 5.888 43.945 1.00 15.45 C ANISOU 465 CG LEU A 61 1597 2080 2194 -186 -654 214 C ATOM 466 CD1 LEU A 61 46.150 6.169 44.532 1.00 19.90 C ANISOU 466 CD1 LEU A 61 1480 2780 3303 -583 -726 718 C ATOM 467 CD2 LEU A 61 44.486 4.385 44.020 1.00 17.50 C ANISOU 467 CD2 LEU A 61 1526 2014 3111 -82 -577 156 C ATOM 468 N ASP A 62 40.615 8.182 44.864 1.00 15.46 N ANISOU 468 N ASP A 62 1729 2090 2054 -211 -512 272 N ATOM 469 CA ASP A 62 39.497 8.678 45.671 1.00 15.61 C ANISOU 469 CA ASP A 62 1813 2401 1717 -229 -513 48 C ATOM 470 C ASP A 62 38.166 8.052 45.267 1.00 15.31 C ANISOU 470 C ASP A 62 1636 2444 1737 124 -682 86 C ATOM 471 O ASP A 62 37.104 8.428 45.782 1.00 16.91 O ANISOU 471 O ASP A 62 1837 2751 1839 -65 -187 299 O ATOM 472 CB ASP A 62 39.424 10.203 45.586 1.00 18.09 C ANISOU 472 CB ASP A 62 1698 2500 2676 -19 -484 9 C ATOM 473 CG ASP A 62 39.236 10.724 44.171 1.00 17.73 C ANISOU 473 CG ASP A 62 1432 2251 3053 -572 -792 448 C ATOM 474 OD1 ASP A 62 39.608 10.018 43.211 1.00 19.45 O ANISOU 474 OD1 ASP A 62 2103 2709 2578 -329 -168 954 O ATOM 475 OD2 ASP A 62 38.914 11.929 44.051 1.00 24.50 O ANISOU 475 OD2 ASP A 62 2183 2532 4593 -84 -87 954 O ATOM 476 N SER A 63 38.168 7.135 44.285 1.00 13.80 N ANISOU 476 N SER A 63 1650 1774 1819 -287 -434 384 N ATOM 477 CA SER A 63 36.960 6.416 43.871 1.00 14.19 C ANISOU 477 CA SER A 63 1417 2513 1460 -320 -290 293 C ATOM 478 C SER A 63 36.266 5.769 45.064 1.00 13.37 C ANISOU 478 C SER A 63 1334 2354 1392 -187 -296 203 C ATOM 479 O SER A 63 36.922 5.184 45.925 1.00 14.40 O ANISOU 479 O SER A 63 1488 2456 1529 -322 -435 398 O ATOM 480 CB SER A 63 37.312 5.337 42.842 1.00 14.17 C ANISOU 480 CB SER A 63 1273 2638 1475 -469 -141 174 C ATOM 481 OG SER A 63 37.787 5.881 41.634 1.00 13.82 O ANISOU 481 OG SER A 63 1354 2320 1576 -62 -145 452 O ATOM 482 N GLY A 64 34.938 5.739 45.049 1.00 13.25 N ANISOU 482 N GLY A 64 1377 2091 1568 -142 -226 302 N ATOM 483 CA GLY A 64 34.223 4.920 46.018 1.00 13.23 C ANISOU 483 CA GLY A 64 1470 2124 1433 -351 -332 167 C ATOM 484 C GLY A 64 34.118 3.468 45.568 1.00 11.78 C ANISOU 484 C GLY A 64 1198 2016 1262 -63 -448 364 C ATOM 485 O GLY A 64 34.120 2.573 46.432 1.00 14.04 O ANISOU 485 O GLY A 64 1543 2239 1551 -96 -459 561 O ATOM 486 N VAL A 65 34.046 3.231 44.276 1.00 11.95 N ANISOU 486 N VAL A 65 1434 1780 1328 33 -166 238 N ATOM 487 CA VAL A 65 33.863 1.879 43.750 1.00 11.40 C ANISOU 487 CA VAL A 65 1110 1776 1447 28 -231 316 C ATOM 488 C VAL A 65 35.075 1.518 42.909 1.00 12.08 C ANISOU 488 C VAL A 65 1204 1797 1590 111 -100 281 C ATOM 489 O VAL A 65 35.879 0.670 43.318 1.00 14.29 O ANISOU 489 O VAL A 65 1438 2145 1846 337 -147 508 O ATOM 490 CB VAL A 65 32.549 1.815 42.946 1.00 12.74 C ANISOU 490 CB VAL A 65 1191 2000 1648 191 -335 -52 C ATOM 491 CG1 VAL A 65 32.296 0.436 42.358 1.00 13.47 C ANISOU 491 CG1 VAL A 65 1430 1788 1899 -100 -282 188 C ATOM 492 CG2 VAL A 65 31.408 2.258 43.862 1.00 16.63 C ANISOU 492 CG2 VAL A 65 1140 2980 2198 74 -210 -512 C ATOM 493 N GLY A 66 35.281 2.227 41.790 1.00 12.51 N ANISOU 493 N GLY A 66 1310 2007 1438 67 -49 238 N ATOM 494 CA GLY A 66 36.541 2.132 41.058 1.00 13.38 C ANISOU 494 CA GLY A 66 1136 2156 1793 10 -29 139 C ATOM 495 C GLY A 66 36.563 1.224 39.861 1.00 13.13 C ANISOU 495 C GLY A 66 1070 2382 1538 107 -120 176 C ATOM 496 O GLY A 66 37.649 1.074 39.277 1.00 14.40 O ANISOU 496 O GLY A 66 1023 2565 1882 178 -175 -55 O ATOM 497 N ILE A 67 35.463 0.565 39.516 1.00 12.68 N ANISOU 497 N ILE A 67 1096 2233 1489 135 -131 222 N ATOM 498 CA ILE A 67 35.465 -0.332 38.364 1.00 12.59 C ANISOU 498 CA ILE A 67 1291 1958 1534 148 -32 246 C ATOM 499 C ILE A 67 34.238 -0.071 37.495 1.00 11.61 C ANISOU 499 C ILE A 67 1292 1940 1179 187 97 308 C ATOM 500 O ILE A 67 33.227 0.481 37.958 1.00 12.60 O ANISOU 500 O ILE A 67 1168 2236 1385 187 23 101 O ATOM 501 CB ILE A 67 35.495 -1.826 38.752 1.00 13.11 C ANISOU 501 CB ILE A 67 1123 2061 1796 318 -40 429 C ATOM 502 CG1 ILE A 67 34.209 -2.300 39.480 1.00 12.92 C ANISOU 502 CG1 ILE A 67 1441 1756 1714 117 65 169 C ATOM 503 CG2 ILE A 67 36.714 -2.170 39.578 1.00 16.04 C ANISOU 503 CG2 ILE A 67 1521 2664 1908 418 -431 316 C ATOM 504 CD1 ILE A 67 34.151 -3.797 39.701 1.00 15.80 C ANISOU 504 CD1 ILE A 67 2088 1774 2142 -28 -564 477 C ATOM 505 N TYR A 68 34.373 -0.433 36.235 1.00 12.56 N ANISOU 505 N TYR A 68 1287 2088 1397 5 30 -31 N ATOM 506 CA TYR A 68 33.252 -0.349 35.279 1.00 12.10 C ANISOU 506 CA TYR A 68 1326 1644 1627 63 -212 -20 C ATOM 507 C TYR A 68 33.333 -1.580 34.373 1.00 11.46 C ANISOU 507 C TYR A 68 1166 1858 1329 160 71 -78 C ATOM 508 O TYR A 68 34.408 -2.196 34.254 1.00 13.05 O ANISOU 508 O TYR A 68 1217 2240 1500 225 153 -127 O ATOM 509 CB TYR A 68 33.429 0.891 34.413 1.00 13.04 C ANISOU 509 CB TYR A 68 1216 1727 2011 170 146 176 C ATOM 510 CG TYR A 68 33.276 2.226 35.085 1.00 11.52 C ANISOU 510 CG TYR A 68 1143 1739 1496 96 38 239 C ATOM 511 CD1 TYR A 68 34.392 2.881 35.595 1.00 12.15 C ANISOU 511 CD1 TYR A 68 1182 2145 1291 144 40 39 C ATOM 512 CD2 TYR A 68 32.030 2.837 35.206 1.00 12.14 C ANISOU 512 CD2 TYR A 68 1225 1894 1492 267 -89 82 C ATOM 513 CE1 TYR A 68 34.219 4.122 36.185 1.00 12.32 C ANISOU 513 CE1 TYR A 68 1119 2171 1390 25 109 -28 C ATOM 514 CE2 TYR A 68 31.870 4.096 35.738 1.00 12.57 C ANISOU 514 CE2 TYR A 68 1245 2209 1324 161 -83 -297 C ATOM 515 CZ TYR A 68 32.989 4.724 36.271 1.00 11.46 C ANISOU 515 CZ TYR A 68 1165 2164 1026 210 -95 -36 C ATOM 516 OH TYR A 68 32.883 5.969 36.844 1.00 12.60 O ANISOU 516 OH TYR A 68 1295 2043 1451 -51 -53 -52 O ATOM 517 N ALA A 69 32.238 -1.922 33.719 1.00 12.94 N ANISOU 517 N ALA A 69 1286 1934 1697 13 -70 -208 N ATOM 518 CA ALA A 69 32.233 -3.022 32.763 1.00 12.67 C ANISOU 518 CA ALA A 69 1363 1867 1586 -97 149 -139 C ATOM 519 C ALA A 69 32.363 -2.464 31.341 1.00 12.89 C ANISOU 519 C ALA A 69 1176 2027 1694 48 404 6 C ATOM 520 O ALA A 69 31.442 -1.789 30.880 1.00 14.10 O ANISOU 520 O ALA A 69 1685 2080 1591 359 342 -116 O ATOM 521 CB ALA A 69 30.900 -3.771 32.900 1.00 13.09 C ANISOU 521 CB ALA A 69 1451 1788 1734 -181 293 -86 C ATOM 522 N PRO A 70 33.418 -2.796 30.595 1.00 14.24 N ANISOU 522 N PRO A 70 1465 2069 1878 231 506 -124 N ATOM 523 CA PRO A 70 33.515 -2.303 29.205 1.00 15.45 C ANISOU 523 CA PRO A 70 1492 2553 1825 122 622 -100 C ATOM 524 C PRO A 70 32.482 -2.911 28.276 1.00 14.35 C ANISOU 524 C PRO A 70 1550 2095 1808 474 456 -1 C ATOM 525 O PRO A 70 32.041 -2.237 27.316 1.00 16.52 O ANISOU 525 O PRO A 70 2134 2649 1495 295 531 189 O ATOM 526 CB PRO A 70 34.936 -2.617 28.756 1.00 18.69 C ANISOU 526 CB PRO A 70 1505 3384 2212 94 686 -226 C ATOM 527 CG PRO A 70 35.671 -2.712 30.054 1.00 19.66 C ANISOU 527 CG PRO A 70 1510 3728 2234 503 671 69 C ATOM 528 CD PRO A 70 34.707 -3.346 31.033 1.00 16.51 C ANISOU 528 CD PRO A 70 1488 2428 2356 527 543 -69 C ATOM 529 N ASP A 71 32.115 -4.158 28.590 1.00 14.97 N ANISOU 529 N ASP A 71 1967 1999 1722 390 514 -243 N ATOM 530 CA ASP A 71 31.064 -4.839 27.834 1.00 16.32 C ANISOU 530 CA ASP A 71 2177 2472 1552 5 712 -375 C ATOM 531 C ASP A 71 30.292 -5.724 28.799 1.00 15.47 C ANISOU 531 C ASP A 71 1740 2338 1801 361 377 39 C ATOM 532 O ASP A 71 30.701 -5.859 29.973 1.00 16.45 O ANISOU 532 O ASP A 71 2358 2347 1544 416 497 -184 O ATOM 533 CB ASP A 71 31.656 -5.620 26.658 1.00 18.36 C ANISOU 533 CB ASP A 71 2370 3081 1524 649 410 -542 C ATOM 534 CG ASP A 71 32.705 -6.629 27.024 1.00 18.92 C ANISOU 534 CG ASP A 71 2213 3367 1608 643 812 -106 C ATOM 535 OD1 ASP A 71 33.337 -7.184 26.095 1.00 18.86 O ANISOU 535 OD1 ASP A 71 2216 3248 1703 560 604 -445 O ATOM 536 OD2 ASP A 71 32.837 -7.019 28.207 1.00 17.55 O ANISOU 536 OD2 ASP A 71 2500 2410 1758 549 997 -55 O ATOM 537 N ALA A 72 29.182 -6.304 28.343 1.00 16.13 N ANISOU 537 N ALA A 72 1694 2343 2092 276 587 -203 N ATOM 538 CA ALA A 72 28.379 -7.118 29.261 1.00 16.76 C ANISOU 538 CA ALA A 72 1956 2170 2244 285 535 62 C ATOM 539 C ALA A 72 29.124 -8.347 29.761 1.00 15.95 C ANISOU 539 C ALA A 72 1961 2363 1737 435 479 -275 C ATOM 540 O ALA A 72 28.995 -8.770 30.890 1.00 14.76 O ANISOU 540 O ALA A 72 1929 1942 1739 206 520 -275 O ATOM 541 CB ALA A 72 27.072 -7.537 28.593 1.00 18.55 C ANISOU 541 CB ALA A 72 1576 2502 2972 354 566 107 C ATOM 542 N GLU A 73 29.885 -8.930 28.837 1.00 16.27 N ANISOU 542 N GLU A 73 1867 2468 1846 359 520 -470 N ATOM 543 CA GLU A 73 30.611 -10.153 29.107 1.00 16.78 C ANISOU 543 CA GLU A 73 2394 2351 1629 429 315 -703 C ATOM 544 C GLU A 73 31.531 -9.936 30.310 1.00 14.94 C ANISOU 544 C GLU A 73 2176 1963 1539 125 482 -372 C ATOM 545 O GLU A 73 31.791 -10.827 31.121 1.00 16.15 O ANISOU 545 O GLU A 73 2164 2058 1914 492 559 -155 O ATOM 546 CB GLU A 73 31.435 -10.524 27.852 1.00 17.35 C ANISOU 546 CB GLU A 73 2760 2276 1555 828 602 -167 C ATOM 547 CG GLU A 73 32.072 -11.923 28.054 1.00 21.71 C ANISOU 547 CG GLU A 73 3604 2222 2422 1040 742 -354 C ATOM 548 CD GLU A 73 32.885 -12.357 26.852 1.00 26.03 C ANISOU 548 CD GLU A 73 4469 3047 2375 1645 649 -793 C ATOM 549 OE1 GLU A 73 32.923 -11.649 25.813 1.00 23.74 O ANISOU 549 OE1 GLU A 73 2938 3443 2639 683 1009 -537 O ATOM 550 OE2 GLU A 73 33.538 -13.422 26.956 1.00 31.47 O ANISOU 550 OE2 GLU A 73 4886 3615 3456 2259 446 -1034 O ATOM 551 N SER A 74 32.107 -8.743 30.420 1.00 14.50 N ANISOU 551 N SER A 74 1708 2057 1744 166 662 -404 N ATOM 552 CA SER A 74 33.020 -8.421 31.518 1.00 15.27 C ANISOU 552 CA SER A 74 1694 2333 1775 -9 578 -284 C ATOM 553 C SER A 74 32.439 -8.735 32.894 1.00 12.84 C ANISOU 553 C SER A 74 1575 1465 1840 312 501 39 C ATOM 554 O SER A 74 33.176 -9.115 33.821 1.00 14.51 O ANISOU 554 O SER A 74 1584 1839 2089 301 285 4 O ATOM 555 CB SER A 74 33.355 -6.912 31.486 1.00 16.70 C ANISOU 555 CB SER A 74 2355 2526 1463 -646 305 207 C ATOM 556 OG SER A 74 34.259 -6.614 30.445 1.00 19.02 O ANISOU 556 OG SER A 74 2281 2715 2231 -278 875 -172 O ATOM 557 N TYR A 75 31.141 -8.579 33.109 1.00 13.01 N ANISOU 557 N TYR A 75 1489 1754 1699 167 455 -115 N ATOM 558 CA TYR A 75 30.558 -8.839 34.430 1.00 14.11 C ANISOU 558 CA TYR A 75 1593 1887 1883 321 629 86 C ATOM 559 C TYR A 75 30.782 -10.277 34.872 1.00 14.14 C ANISOU 559 C TYR A 75 1630 1828 1913 211 512 -5 C ATOM 560 O TYR A 75 30.880 -10.547 36.070 1.00 15.78 O ANISOU 560 O TYR A 75 2095 2043 1858 455 298 93 O ATOM 561 CB TYR A 75 29.045 -8.548 34.401 1.00 13.57 C ANISOU 561 CB TYR A 75 1527 2028 1600 309 317 -401 C ATOM 562 CG TYR A 75 28.750 -7.074 34.600 1.00 12.96 C ANISOU 562 CG TYR A 75 1387 1905 1631 188 243 -123 C ATOM 563 CD1 TYR A 75 28.084 -6.322 33.642 1.00 13.61 C ANISOU 563 CD1 TYR A 75 1491 2059 1621 72 -95 -206 C ATOM 564 CD2 TYR A 75 29.105 -6.458 35.811 1.00 12.94 C ANISOU 564 CD2 TYR A 75 1589 1894 1433 626 180 -162 C ATOM 565 CE1 TYR A 75 27.783 -4.985 33.833 1.00 12.85 C ANISOU 565 CE1 TYR A 75 1394 2055 1432 170 64 -57 C ATOM 566 CE2 TYR A 75 28.836 -5.118 35.996 1.00 12.62 C ANISOU 566 CE2 TYR A 75 1634 1814 1346 438 102 27 C ATOM 567 CZ TYR A 75 28.153 -4.392 35.020 1.00 11.96 C ANISOU 567 CZ TYR A 75 1290 1810 1444 285 57 30 C ATOM 568 OH TYR A 75 27.922 -3.056 35.263 1.00 12.28 O ANISOU 568 OH TYR A 75 1306 1780 1579 315 -22 -4 O ATOM 569 N ARG A 76 30.910 -11.191 33.925 1.00 15.53 N ANISOU 569 N ARG A 76 1839 1978 2085 470 431 -125 N ATOM 570 CA ARG A 76 31.202 -12.593 34.215 1.00 15.29 C ANISOU 570 CA ARG A 76 1834 1894 2081 373 399 -313 C ATOM 571 C ARG A 76 32.651 -12.943 33.993 1.00 15.23 C ANISOU 571 C ARG A 76 1776 1717 2293 324 412 -88 C ATOM 572 O ARG A 76 33.208 -13.664 34.832 1.00 17.75 O ANISOU 572 O ARG A 76 2264 2499 1981 708 136 -190 O ATOM 573 CB ARG A 76 30.247 -13.500 33.438 1.00 17.74 C ANISOU 573 CB ARG A 76 1790 2158 2794 640 27 -730 C ATOM 574 CG ARG A 76 28.830 -13.404 33.999 1.00 18.74 C ANISOU 574 CG ARG A 76 2048 2867 2207 -40 478 -486 C ATOM 575 CD ARG A 76 27.867 -14.300 33.231 1.00 19.84 C ANISOU 575 CD ARG A 76 1885 2992 2662 200 217 -687 C ATOM 576 NE ARG A 76 26.535 -14.254 33.835 1.00 18.14 N ANISOU 576 NE ARG A 76 1929 2556 2406 271 234 -104 N ATOM 577 CZ ARG A 76 25.614 -13.319 33.686 1.00 18.41 C ANISOU 577 CZ ARG A 76 2289 1960 2745 277 684 -251 C ATOM 578 NH1 ARG A 76 25.801 -12.238 32.943 1.00 18.07 N ANISOU 578 NH1 ARG A 76 2314 2182 2369 -25 322 -209 N ATOM 579 NH2 ARG A 76 24.431 -13.412 34.286 1.00 18.52 N ANISOU 579 NH2 ARG A 76 2304 2667 2065 645 523 244 N ATOM 580 N THR A 77 33.284 -12.466 32.919 1.00 16.01 N ANISOU 580 N THR A 77 1811 2043 2230 527 492 -170 N ATOM 581 CA THR A 77 34.714 -12.761 32.735 1.00 16.70 C ANISOU 581 CA THR A 77 1763 2306 2275 305 522 -441 C ATOM 582 C THR A 77 35.492 -12.331 33.974 1.00 15.37 C ANISOU 582 C THR A 77 1890 2103 1847 598 482 -60 C ATOM 583 O THR A 77 36.414 -13.009 34.442 1.00 19.56 O ANISOU 583 O THR A 77 2116 2427 2890 849 227 -20 O ATOM 584 CB THR A 77 35.218 -11.980 31.512 1.00 17.23 C ANISOU 584 CB THR A 77 1838 3031 1677 779 448 -436 C ATOM 585 OG1 THR A 77 34.487 -12.440 30.358 1.00 19.78 O ANISOU 585 OG1 THR A 77 2132 3063 2322 393 58 -491 O ATOM 586 CG2 THR A 77 36.702 -12.287 31.335 1.00 20.68 C ANISOU 586 CG2 THR A 77 1706 3701 2452 499 517 481 C ATOM 587 N PHE A 78 35.119 -11.148 34.496 1.00 16.42 N ANISOU 587 N PHE A 78 1699 2313 2228 533 395 -433 N ATOM 588 CA PHE A 78 35.814 -10.649 35.682 1.00 14.61 C ANISOU 588 CA PHE A 78 1501 1998 2051 623 323 -86 C ATOM 589 C PHE A 78 34.917 -10.751 36.905 1.00 14.63 C ANISOU 589 C PHE A 78 1624 1854 2081 497 312 18 C ATOM 590 O PHE A 78 35.037 -9.980 37.848 1.00 15.83 O ANISOU 590 O PHE A 78 1935 2139 1941 306 366 -26 O ATOM 591 CB PHE A 78 36.274 -9.196 35.439 1.00 14.70 C ANISOU 591 CB PHE A 78 1655 2125 1804 490 396 20 C ATOM 592 CG PHE A 78 37.112 -9.125 34.176 1.00 15.12 C ANISOU 592 CG PHE A 78 1599 2444 1704 446 357 -207 C ATOM 593 CD1 PHE A 78 36.592 -8.636 32.983 1.00 17.49 C ANISOU 593 CD1 PHE A 78 2634 2266 1747 419 271 11 C ATOM 594 CD2 PHE A 78 38.399 -9.621 34.161 1.00 18.04 C ANISOU 594 CD2 PHE A 78 1578 2730 2546 460 527 -432 C ATOM 595 CE1 PHE A 78 37.349 -8.576 31.831 1.00 16.70 C ANISOU 595 CE1 PHE A 78 2041 2363 1943 60 218 35 C ATOM 596 CE2 PHE A 78 39.194 -9.510 33.026 1.00 18.82 C ANISOU 596 CE2 PHE A 78 1729 2847 2575 662 616 14 C ATOM 597 CZ PHE A 78 38.629 -9.089 31.827 1.00 20.05 C ANISOU 597 CZ PHE A 78 2274 2771 2575 427 167 -295 C ATOM 598 N GLY A 79 34.037 -11.747 36.878 1.00 16.78 N ANISOU 598 N GLY A 79 1768 2142 2467 261 481 -123 N ATOM 599 CA GLY A 79 33.138 -12.049 37.970 1.00 17.28 C ANISOU 599 CA GLY A 79 1629 2687 2250 409 215 420 C ATOM 600 C GLY A 79 33.817 -12.087 39.320 1.00 15.13 C ANISOU 600 C GLY A 79 1596 1792 2360 469 72 -98 C ATOM 601 O GLY A 79 33.245 -11.567 40.300 1.00 16.79 O ANISOU 601 O GLY A 79 2040 1929 2412 481 449 97 O ATOM 602 N PRO A 80 34.978 -12.719 39.481 1.00 15.68 N ANISOU 602 N PRO A 80 1732 2010 2217 523 45 -36 N ATOM 603 CA PRO A 80 35.578 -12.794 40.828 1.00 15.70 C ANISOU 603 CA PRO A 80 1887 1812 2267 243 -112 169 C ATOM 604 C PRO A 80 35.851 -11.417 41.430 1.00 15.71 C ANISOU 604 C PRO A 80 1847 1847 2275 35 -84 268 C ATOM 605 O PRO A 80 35.957 -11.291 42.675 1.00 16.10 O ANISOU 605 O PRO A 80 1953 1967 2197 240 -204 192 O ATOM 606 CB PRO A 80 36.867 -13.600 40.586 1.00 19.26 C ANISOU 606 CB PRO A 80 2521 2430 2366 934 -325 170 C ATOM 607 CG PRO A 80 36.499 -14.527 39.448 1.00 18.37 C ANISOU 607 CG PRO A 80 2092 1842 3047 496 -146 57 C ATOM 608 CD PRO A 80 35.666 -13.621 38.541 1.00 17.57 C ANISOU 608 CD PRO A 80 1690 2342 2645 794 -253 -449 C ATOM 609 N LEU A 81 35.936 -10.360 40.650 1.00 14.41 N ANISOU 609 N LEU A 81 1582 1738 2154 144 115 136 N ATOM 610 CA LEU A 81 36.042 -8.996 41.167 1.00 15.23 C ANISOU 610 CA LEU A 81 1368 1753 2665 191 158 47 C ATOM 611 C LEU A 81 34.662 -8.339 41.196 1.00 14.96 C ANISOU 611 C LEU A 81 1311 2106 2269 273 93 3 C ATOM 612 O LEU A 81 34.293 -7.726 42.222 1.00 14.07 O ANISOU 612 O LEU A 81 1470 2058 1817 325 57 311 O ATOM 613 CB LEU A 81 36.985 -8.141 40.292 1.00 15.53 C ANISOU 613 CB LEU A 81 1236 2065 2601 -218 -66 67 C ATOM 614 CG LEU A 81 37.138 -6.684 40.754 1.00 15.27 C ANISOU 614 CG LEU A 81 1434 2085 2284 -150 -214 175 C ATOM 615 CD1 LEU A 81 37.612 -6.681 42.212 1.00 15.98 C ANISOU 615 CD1 LEU A 81 1694 2159 2218 485 -176 79 C ATOM 616 CD2 LEU A 81 38.077 -5.903 39.849 1.00 15.42 C ANISOU 616 CD2 LEU A 81 1537 1797 2526 52 106 175 C ATOM 617 N PHE A 82 33.855 -8.467 40.133 1.00 14.45 N ANISOU 617 N PHE A 82 1531 1921 2038 366 126 85 N ATOM 618 CA PHE A 82 32.538 -7.803 40.163 1.00 13.11 C ANISOU 618 CA PHE A 82 1419 2005 1559 179 66 300 C ATOM 619 C PHE A 82 31.641 -8.323 41.276 1.00 12.24 C ANISOU 619 C PHE A 82 1536 1775 1339 246 7 113 C ATOM 620 O PHE A 82 30.926 -7.583 41.940 1.00 13.64 O ANISOU 620 O PHE A 82 1558 2142 1483 372 43 -62 O ATOM 621 CB PHE A 82 31.816 -7.934 38.813 1.00 14.10 C ANISOU 621 CB PHE A 82 1864 2110 1384 203 36 181 C ATOM 622 CG PHE A 82 32.302 -6.882 37.818 1.00 12.86 C ANISOU 622 CG PHE A 82 1441 1903 1541 335 62 153 C ATOM 623 CD1 PHE A 82 33.191 -7.203 36.794 1.00 15.47 C ANISOU 623 CD1 PHE A 82 1957 2042 1878 311 481 173 C ATOM 624 CD2 PHE A 82 31.806 -5.573 37.878 1.00 13.88 C ANISOU 624 CD2 PHE A 82 1467 1862 1945 248 -49 49 C ATOM 625 CE1 PHE A 82 33.551 -6.292 35.816 1.00 14.64 C ANISOU 625 CE1 PHE A 82 1993 1782 1787 46 277 8 C ATOM 626 CE2 PHE A 82 32.229 -4.648 36.951 1.00 14.14 C ANISOU 626 CE2 PHE A 82 1558 1830 1985 285 -63 116 C ATOM 627 CZ PHE A 82 33.070 -5.000 35.911 1.00 14.22 C ANISOU 627 CZ PHE A 82 1579 1972 1852 323 -109 45 C ATOM 628 N ASP A 83 31.610 -9.649 41.442 1.00 13.43 N ANISOU 628 N ASP A 83 1421 1750 1931 104 -91 342 N ATOM 629 CA ASP A 83 30.642 -10.268 42.343 1.00 14.19 C ANISOU 629 CA ASP A 83 1606 1860 1924 -91 177 -66 C ATOM 630 C ASP A 83 30.791 -9.751 43.764 1.00 13.77 C ANISOU 630 C ASP A 83 1649 1730 1853 535 -114 122 C ATOM 631 O ASP A 83 29.776 -9.349 44.361 1.00 13.48 O ANISOU 631 O ASP A 83 1627 1767 1727 179 49 120 O ATOM 632 CB ASP A 83 30.718 -11.800 42.305 1.00 14.76 C ANISOU 632 CB ASP A 83 1806 1834 1967 -237 80 96 C ATOM 633 CG ASP A 83 30.152 -12.401 41.021 1.00 15.19 C ANISOU 633 CG ASP A 83 1606 1849 2315 -217 19 -100 C ATOM 634 OD1 ASP A 83 29.410 -11.705 40.302 1.00 16.42 O ANISOU 634 OD1 ASP A 83 2199 2261 1780 201 65 -110 O ATOM 635 OD2 ASP A 83 30.504 -13.561 40.689 1.00 19.51 O ANISOU 635 OD2 ASP A 83 2736 1890 2786 121 -189 -248 O ATOM 636 N PRO A 84 31.990 -9.714 44.336 1.00 14.31 N ANISOU 636 N PRO A 84 1679 1840 1918 402 -52 195 N ATOM 637 CA PRO A 84 32.055 -9.240 45.740 1.00 13.33 C ANISOU 637 CA PRO A 84 1637 1631 1797 245 -166 446 C ATOM 638 C PRO A 84 31.779 -7.756 45.819 1.00 12.84 C ANISOU 638 C PRO A 84 1688 1744 1446 270 -95 405 C ATOM 639 O PRO A 84 31.257 -7.297 46.845 1.00 13.47 O ANISOU 639 O PRO A 84 1724 1831 1564 94 -53 244 O ATOM 640 CB PRO A 84 33.465 -9.621 46.186 1.00 15.52 C ANISOU 640 CB PRO A 84 1423 2457 2018 441 26 440 C ATOM 641 CG PRO A 84 34.233 -9.714 44.901 1.00 16.63 C ANISOU 641 CG PRO A 84 1695 2837 1787 288 -41 418 C ATOM 642 CD PRO A 84 33.254 -10.371 43.956 1.00 15.84 C ANISOU 642 CD PRO A 84 1517 2379 2121 475 -41 308 C ATOM 643 N ILE A 85 32.147 -6.974 44.811 1.00 13.10 N ANISOU 643 N ILE A 85 1486 1725 1765 333 -111 615 N ATOM 644 CA ILE A 85 31.901 -5.528 44.843 1.00 13.54 C ANISOU 644 CA ILE A 85 1438 1746 1960 80 -257 570 C ATOM 645 C ILE A 85 30.425 -5.233 44.749 1.00 11.63 C ANISOU 645 C ILE A 85 1515 1526 1379 219 -201 326 C ATOM 646 O ILE A 85 29.885 -4.397 45.490 1.00 13.21 O ANISOU 646 O ILE A 85 1784 1862 1372 79 1 61 O ATOM 647 CB ILE A 85 32.717 -4.833 43.724 1.00 14.14 C ANISOU 647 CB ILE A 85 1427 1922 2025 47 -144 645 C ATOM 648 CG1 ILE A 85 34.190 -4.795 44.162 1.00 14.15 C ANISOU 648 CG1 ILE A 85 1448 2144 1784 9 -221 422 C ATOM 649 CG2 ILE A 85 32.154 -3.433 43.496 1.00 13.45 C ANISOU 649 CG2 ILE A 85 1605 1720 1785 62 -66 366 C ATOM 650 CD1 ILE A 85 35.183 -4.222 43.176 1.00 14.96 C ANISOU 650 CD1 ILE A 85 1340 2318 2028 59 20 174 C ATOM 651 N ILE A 86 29.732 -5.977 43.881 1.00 13.04 N ANISOU 651 N ILE A 86 1405 1761 1787 7 -150 31 N ATOM 652 CA ILE A 86 28.277 -5.810 43.747 1.00 13.42 C ANISOU 652 CA ILE A 86 1450 2497 1152 201 -111 112 C ATOM 653 C ILE A 86 27.603 -6.229 45.050 1.00 12.21 C ANISOU 653 C ILE A 86 1557 1780 1301 219 -64 -17 C ATOM 654 O ILE A 86 26.675 -5.527 45.495 1.00 12.49 O ANISOU 654 O ILE A 86 1362 2033 1351 259 -72 -32 O ATOM 655 CB ILE A 86 27.858 -6.687 42.534 1.00 13.60 C ANISOU 655 CB ILE A 86 1523 2465 1179 -79 -160 248 C ATOM 656 CG1 ILE A 86 28.207 -5.968 41.216 1.00 12.82 C ANISOU 656 CG1 ILE A 86 1784 1950 1139 65 30 87 C ATOM 657 CG2 ILE A 86 26.397 -7.041 42.608 1.00 15.34 C ANISOU 657 CG2 ILE A 86 1523 2230 2077 -125 171 -70 C ATOM 658 CD1 ILE A 86 28.068 -6.911 40.020 1.00 15.49 C ANISOU 658 CD1 ILE A 86 2033 2519 1332 83 -53 -202 C ATOM 659 N ASP A 87 28.014 -7.347 45.621 1.00 13.31 N ANISOU 659 N ASP A 87 1505 1862 1691 141 -117 264 N ATOM 660 CA ASP A 87 27.406 -7.780 46.897 1.00 13.33 C ANISOU 660 CA ASP A 87 1705 1745 1614 267 -48 106 C ATOM 661 C ASP A 87 27.609 -6.717 47.953 1.00 13.23 C ANISOU 661 C ASP A 87 1421 1882 1724 314 -158 57 C ATOM 662 O ASP A 87 26.721 -6.411 48.749 1.00 13.66 O ANISOU 662 O ASP A 87 1844 1779 1568 91 -23 28 O ATOM 663 CB ASP A 87 28.060 -9.105 47.313 1.00 14.20 C ANISOU 663 CB ASP A 87 1944 1708 1742 206 -65 266 C ATOM 664 CG ASP A 87 27.742 -9.475 48.734 1.00 16.08 C ANISOU 664 CG ASP A 87 1942 2293 1876 -199 -220 558 C ATOM 665 OD1 ASP A 87 26.579 -9.831 49.012 1.00 16.24 O ANISOU 665 OD1 ASP A 87 1683 2540 1949 247 -136 472 O ATOM 666 OD2 ASP A 87 28.668 -9.531 49.594 1.00 22.42 O ANISOU 666 OD2 ASP A 87 1866 4633 2021 -269 -218 1038 O ATOM 667 N ASP A 88 28.792 -6.113 48.022 1.00 13.73 N ANISOU 667 N ASP A 88 1731 1836 1649 64 -395 311 N ATOM 668 CA ASP A 88 29.057 -5.103 49.057 1.00 13.53 C ANISOU 668 CA ASP A 88 1679 1876 1587 100 -404 350 C ATOM 669 C ASP A 88 28.235 -3.832 48.836 1.00 12.90 C ANISOU 669 C ASP A 88 1789 1989 1124 172 -300 213 C ATOM 670 O ASP A 88 27.468 -3.363 49.676 1.00 13.64 O ANISOU 670 O ASP A 88 1838 2027 1316 176 -180 330 O ATOM 671 CB ASP A 88 30.569 -4.784 48.982 1.00 15.41 C ANISOU 671 CB ASP A 88 1654 2429 1771 30 -562 145 C ATOM 672 CG ASP A 88 31.082 -4.015 50.170 1.00 16.83 C ANISOU 672 CG ASP A 88 2164 2255 1977 23 -757 64 C ATOM 673 OD1 ASP A 88 30.272 -3.345 50.845 1.00 21.19 O ANISOU 673 OD1 ASP A 88 2428 3174 2450 -49 -414 -574 O ATOM 674 OD2 ASP A 88 32.315 -4.154 50.423 1.00 18.96 O ANISOU 674 OD2 ASP A 88 1892 3564 1749 -409 -526 236 O ATOM 675 N TYR A 89 28.331 -3.266 47.623 1.00 12.17 N ANISOU 675 N TYR A 89 1561 1773 1289 143 -268 301 N ATOM 676 CA TYR A 89 27.693 -1.989 47.354 1.00 11.62 C ANISOU 676 CA TYR A 89 1351 1754 1310 195 -216 155 C ATOM 677 C TYR A 89 26.183 -2.127 47.555 1.00 11.91 C ANISOU 677 C TYR A 89 1519 1659 1347 143 -127 102 C ATOM 678 O TYR A 89 25.558 -1.210 48.072 1.00 11.90 O ANISOU 678 O TYR A 89 1499 1683 1341 232 -171 78 O ATOM 679 CB TYR A 89 28.012 -1.532 45.895 1.00 11.75 C ANISOU 679 CB TYR A 89 1528 1612 1323 183 -176 164 C ATOM 680 CG TYR A 89 27.227 -0.279 45.567 1.00 11.54 C ANISOU 680 CG TYR A 89 1565 1599 1221 153 -104 130 C ATOM 681 CD1 TYR A 89 27.732 0.964 45.952 1.00 10.98 C ANISOU 681 CD1 TYR A 89 1485 1604 1083 202 -201 119 C ATOM 682 CD2 TYR A 89 25.971 -0.315 44.931 1.00 11.26 C ANISOU 682 CD2 TYR A 89 1582 1723 972 146 -174 88 C ATOM 683 CE1 TYR A 89 27.031 2.123 45.727 1.00 11.04 C ANISOU 683 CE1 TYR A 89 1320 1656 1218 160 -157 278 C ATOM 684 CE2 TYR A 89 25.237 0.840 44.769 1.00 10.62 C ANISOU 684 CE2 TYR A 89 1467 1686 882 121 -20 80 C ATOM 685 CZ TYR A 89 25.780 2.055 45.134 1.00 10.22 C ANISOU 685 CZ TYR A 89 1306 1668 908 70 -65 315 C ATOM 686 OH TYR A 89 25.062 3.200 44.952 1.00 10.90 O ANISOU 686 OH TYR A 89 1324 1720 1099 190 -103 190 O ATOM 687 N HIS A 90 25.559 -3.150 47.015 1.00 11.45 N ANISOU 687 N HIS A 90 1539 1587 1224 14 -120 236 N ATOM 688 CA HIS A 90 24.103 -3.192 47.007 1.00 11.15 C ANISOU 688 CA HIS A 90 1560 1732 944 82 99 75 C ATOM 689 C HIS A 90 23.549 -3.770 48.316 1.00 12.55 C ANISOU 689 C HIS A 90 1509 2224 1037 556 230 243 C ATOM 690 O HIS A 90 22.338 -3.996 48.418 1.00 12.97 O ANISOU 690 O HIS A 90 1530 2228 1170 262 224 180 O ATOM 691 CB HIS A 90 23.577 -3.998 45.808 1.00 11.02 C ANISOU 691 CB HIS A 90 1464 1703 1021 113 -54 173 C ATOM 692 CG HIS A 90 23.839 -3.281 44.513 1.00 9.86 C ANISOU 692 CG HIS A 90 1222 1525 999 95 -106 127 C ATOM 693 ND1 HIS A 90 23.064 -2.237 44.085 1.00 9.90 N ANISOU 693 ND1 HIS A 90 1274 1516 973 -1 -32 146 N ATOM 694 CD2 HIS A 90 24.783 -3.523 43.564 1.00 10.86 C ANISOU 694 CD2 HIS A 90 1472 1684 970 135 -68 188 C ATOM 695 CE1 HIS A 90 23.526 -1.822 42.927 1.00 9.71 C ANISOU 695 CE1 HIS A 90 1204 1598 887 57 -65 34 C ATOM 696 NE2 HIS A 90 24.576 -2.577 42.590 1.00 10.60 N ANISOU 696 NE2 HIS A 90 1437 1446 1144 130 20 163 N ATOM 697 N GLY A 91 24.392 -3.975 49.328 1.00 12.68 N ANISOU 697 N GLY A 91 1921 1832 1066 86 -49 270 N ATOM 698 CA GLY A 91 23.859 -4.350 50.632 1.00 13.18 C ANISOU 698 CA GLY A 91 2154 1806 1049 -94 115 108 C ATOM 699 C GLY A 91 23.383 -5.796 50.635 1.00 11.99 C ANISOU 699 C GLY A 91 1717 1911 926 -234 -69 -29 C ATOM 700 O GLY A 91 22.496 -6.151 51.412 1.00 14.87 O ANISOU 700 O GLY A 91 2135 1984 1530 -120 278 192 O ATOM 701 N GLY A 92 24.042 -6.642 49.839 1.00 12.72 N ANISOU 701 N GLY A 92 1989 1638 1207 210 -172 250 N ATOM 702 CA GLY A 92 23.765 -8.066 49.857 1.00 13.93 C ANISOU 702 CA GLY A 92 2352 1677 1264 284 -194 371 C ATOM 703 C GLY A 92 23.277 -8.555 48.506 1.00 14.32 C ANISOU 703 C GLY A 92 1901 1969 1572 -10 -123 19 C ATOM 704 O GLY A 92 22.161 -8.242 48.091 1.00 15.36 O ANISOU 704 O GLY A 92 1829 2405 1602 37 -95 117 O ATOM 705 N PHE A 93 24.111 -9.328 47.813 1.00 15.43 N ANISOU 705 N PHE A 93 2213 2166 1483 361 -340 14 N ATOM 706 CA PHE A 93 23.681 -9.886 46.532 1.00 13.61 C ANISOU 706 CA PHE A 93 1632 2064 1474 18 -90 94 C ATOM 707 C PHE A 93 24.633 -11.065 46.318 1.00 13.91 C ANISOU 707 C PHE A 93 1523 2194 1570 84 -132 -23 C ATOM 708 O PHE A 93 25.784 -10.867 45.928 1.00 17.69 O ANISOU 708 O PHE A 93 1487 3165 2068 -84 -5 -433 O ATOM 709 CB PHE A 93 23.818 -8.856 45.395 1.00 14.14 C ANISOU 709 CB PHE A 93 1831 2086 1455 -175 -232 138 C ATOM 710 CG PHE A 93 23.067 -9.349 44.151 1.00 13.38 C ANISOU 710 CG PHE A 93 1742 1852 1490 -83 -91 128 C ATOM 711 CD1 PHE A 93 21.690 -9.357 44.035 1.00 13.28 C ANISOU 711 CD1 PHE A 93 1748 1536 1761 31 -337 227 C ATOM 712 CD2 PHE A 93 23.808 -9.853 43.088 1.00 15.15 C ANISOU 712 CD2 PHE A 93 2134 2095 1528 103 -29 -49 C ATOM 713 CE1 PHE A 93 21.009 -9.832 42.934 1.00 14.49 C ANISOU 713 CE1 PHE A 93 1805 1957 1745 119 -256 -18 C ATOM 714 CE2 PHE A 93 23.163 -10.310 41.965 1.00 14.47 C ANISOU 714 CE2 PHE A 93 1921 2120 1456 6 -44 109 C ATOM 715 CZ PHE A 93 21.769 -10.273 41.858 1.00 14.32 C ANISOU 715 CZ PHE A 93 1896 1693 1852 204 -36 178 C ATOM 716 N LYS A 94 24.157 -12.242 46.681 1.00 15.97 N ANISOU 716 N LYS A 94 2153 2133 1783 354 35 302 N ATOM 717 CA LYS A 94 24.956 -13.450 46.696 1.00 18.08 C ANISOU 717 CA LYS A 94 2543 2434 1892 798 39 215 C ATOM 718 C LYS A 94 25.138 -14.028 45.305 1.00 16.18 C ANISOU 718 C LYS A 94 1832 2298 2016 278 85 116 C ATOM 719 O LYS A 94 24.489 -13.639 44.351 1.00 17.68 O ANISOU 719 O LYS A 94 2584 2260 1875 370 66 191 O ATOM 720 CB LYS A 94 24.317 -14.506 47.599 1.00 20.82 C ANISOU 720 CB LYS A 94 3724 2236 1952 1038 311 354 C ATOM 721 CG LYS A 94 24.250 -14.154 49.070 1.00 27.40 C ANISOU 721 CG LYS A 94 5723 2727 1962 2034 820 387 C ATOM 722 CD LYS A 94 23.510 -15.281 49.797 1.00 35.14 C ANISOU 722 CD LYS A 94 6139 4849 2364 1130 655 1469 C ATOM 723 CE LYS A 94 22.671 -14.775 50.958 1.00 40.81 C ANISOU 723 CE LYS A 94 6587 6945 1975 1432 734 1637 C ATOM 724 NZ LYS A 94 21.216 -14.692 50.627 1.00 55.34 N ANISOU 724 NZ LYS A 94 6813 7568 6646 4033 356 724 N ATOM 725 N LEU A 95 26.076 -14.948 45.159 1.00 20.23 N ANISOU 725 N LEU A 95 2811 2496 2378 872 154 61 N ATOM 726 CA LEU A 95 26.427 -15.580 43.897 1.00 19.89 C ANISOU 726 CA LEU A 95 2853 2380 2323 965 11 77 C ATOM 727 C LEU A 95 25.166 -16.258 43.363 1.00 19.90 C ANISOU 727 C LEU A 95 2770 2420 2371 1034 58 65 C ATOM 728 O LEU A 95 24.998 -16.315 42.149 1.00 24.78 O ANISOU 728 O LEU A 95 3800 3212 2402 1144 -242 -527 O ATOM 729 CB LEU A 95 27.528 -16.631 44.080 1.00 20.95 C ANISOU 729 CB LEU A 95 2446 2619 2896 847 522 333 C ATOM 730 CG LEU A 95 28.917 -16.058 44.343 1.00 24.74 C ANISOU 730 CG LEU A 95 2268 3823 3309 587 945 769 C ATOM 731 CD1 LEU A 95 29.214 -14.900 43.415 1.00 33.55 C ANISOU 731 CD1 LEU A 95 2924 4804 5020 47 1026 1878 C ATOM 732 CD2 LEU A 95 29.083 -15.684 45.797 1.00 46.39 C ANISOU 732 CD2 LEU A 95 6400 7498 3730 -1954 -1134 630 C TER END