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*** ***elNémo ID: 19101015332028693Job options:ID = 19101015332028693 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:ATOM 1 N SER A 2 -0.987 160.287 265.459 1.00 67.14 A N ANISOU 1 N SER A 2 6284 8832 10394 2128 289 307 A N ATOM 2 CA SER A 2 -1.482 161.553 264.932 1.00 71.83 A C ANISOU 2 CA SER A 2 6937 9324 11032 2369 266 335 A C ATOM 3 C SER A 2 -0.334 162.461 264.498 1.00 70.02 A C ANISOU 3 C SER A 2 6977 8746 10883 2404 250 349 A C ATOM 4 O SER A 2 -0.520 163.656 264.268 1.00 72.20 A O ANISOU 4 O SER A 2 7370 8861 11203 2607 244 349 A O ATOM 5 CB SER A 2 -2.357 162.254 265.971 1.00 77.81 A C ANISOU 5 CB SER A 2 7641 10132 11792 2589 347 221 A C ATOM 6 OG SER A 2 -3.214 161.327 266.617 1.00 80.46 A O ANISOU 6 OG SER A 2 7745 10759 12067 2503 394 203 A O ATOM 7 N THR A 3 0.858 161.883 264.396 1.00 64.33 A N ANISOU 7 N THR A 3 6353 7897 10193 2188 242 357 A N ATOM 8 CA THR A 3 2.001 162.585 263.841 1.00 60.55 A C ANISOU 8 CA THR A 3 6103 7100 9804 2150 218 387 A C ATOM 9 C THR A 3 2.329 161.809 262.582 1.00 48.54 A C ANISOU 9 C THR A 3 4523 5649 8270 1971 128 528 A C ATOM 10 O THR A 3 2.337 160.578 262.603 1.00 41.66 A O ANISOU 10 O THR A 3 3519 4959 7349 1793 103 534 A O ATOM 11 CB THR A 3 3.198 162.575 264.800 1.00 63.79 A C ANISOU 11 CB THR A 3 6670 7295 10272 2029 273 251 A C ATOM 12 CG2 THR A 3 4.352 163.393 264.226 1.00 62.71 A C ANISOU 12 CG2 THR A 3 6765 6832 10232 1970 245 277 A C ATOM 13 OG1 THR A 3 2.798 163.140 266.056 1.00 67.88 A O ANISOU 13 OG1 THR A 3 7228 7798 10766 2194 355 103 A O ATOM 14 N GLU A 4 2.624 162.510 261.494 1.00 42.90 A N ANISOU 14 N GLU A 4 3921 4789 7591 2014 78 638 A N ATOM 15 CA GLU A 4 2.815 161.835 260.216 1.00 44.72 A C ANISOU 15 CA GLU A 4 4094 5114 7782 1880 -11 774 A C ATOM 16 C GLU A 4 4.189 162.065 259.623 1.00 43.03 A C ANISOU 16 C GLU A 4 4058 4655 7636 1748 -28 824 A C ATOM 17 O GLU A 4 4.739 163.164 259.686 1.00 48.57 A O ANISOU 17 O GLU A 4 4945 5095 8413 1815 7 817 A O ATOM 18 CB GLU A 4 1.735 162.204 259.195 1.00 51.35 A C ANISOU 18 CB GLU A 4 4847 6104 8560 2035 -76 890 A C ATOM 19 CG GLU A 4 0.402 161.517 259.422 1.00 63.57 A C ANISOU 19 CG GLU A 4 6153 7979 10021 2071 -98 868 A C ATOM 20 CD GLU A 4 -0.357 161.298 258.127 1.00 73.17 A C ANISOU 20 CD GLU A 4 7257 9383 11162 2091 -202 988 A C ATOM 21 OE1 GLU A 4 0.142 161.729 257.065 1.00 77.75 A O ANISOU 21 OE1 GLU A 4 7952 9843 11747 2103 -250 1094 A O ATOM 22 OE2 GLU A 4 -1.446 160.689 258.169 1.00 74.69 A O1- ANISOU 22 OE2 GLU A 4 7245 9844 11290 2083 -235 975 A O1- ATOM 23 N ILE A 5 4.726 161.005 259.036 1.00 39.36 A N ANISOU 23 N ILE A 5 3538 4282 7134 1554 -85 872 A N ATOM 24 CA ILE A 5 6.021 161.061 258.399 1.00 40.81 A C ANISOU 24 CA ILE A 5 3857 4286 7362 1419 -105 928 A C ATOM 25 C ILE A 5 5.882 160.455 257.012 1.00 40.01 A C ANISOU 25 C ILE A 5 3689 4349 7165 1365 -197 1068 A C ATOM 26 O ILE A 5 5.054 159.567 256.781 1.00 38.88 A O ANISOU 26 O ILE A 5 3389 4459 6926 1342 -253 1075 A O ATOM 27 CB ILE A 5 7.032 160.193 259.220 1.00 58.08 A C ANISOU 27 CB ILE A 5 6054 6428 9585 1223 -87 811 A C ATOM 28 CG1 ILE A 5 7.342 160.840 260.571 1.00 59.10 A C ANISOU 28 CG1 ILE A 5 6279 6376 9799 1263 -2 655 A C ATOM 29 CG2 ILE A 5 8.325 159.914 258.455 1.00 55.37 A C ANISOU 29 CG2 ILE A 5 5799 5983 9257 1064 -125 876 A C ATOM 30 CD1 ILE A 5 8.102 159.930 261.526 1.00 55.29 A C ANISOU 30 CD1 ILE A 5 5780 5900 9328 1101 15 520 A C ATOM 31 N LYS A 6 6.709 160.940 256.096 1.00 41.72 A N ANISOU 31 N LYS A 6 4031 4424 7398 1334 -211 1173 A N ATOM 32 CA LYS A 6 6.779 160.414 254.752 1.00 47.55 A C ANISOU 32 CA LYS A 6 4736 5298 8032 1283 -291 1299 A C ATOM 33 C LYS A 6 8.240 160.076 254.568 1.00 45.41 A C ANISOU 33 C LYS A 6 4561 4905 7790 1109 -284 1309 A C ATOM 34 O LYS A 6 9.113 160.905 254.834 1.00 46.32 A O ANISOU 34 O LYS A 6 4814 4785 8003 1087 -223 1306 A O ATOM 35 CB LYS A 6 6.347 161.470 253.738 1.00 53.56 A C ANISOU 35 CB LYS A 6 5562 6019 8767 1445 -304 1437 A C ATOM 36 CG LYS A 6 6.432 161.008 252.292 1.00 59.86 A C ANISOU 36 CG LYS A 6 6341 6963 9441 1408 -384 1566 A C ATOM 37 CD LYS A 6 6.014 162.113 251.332 1.00 68.04 A C ANISOU 37 CD LYS A 6 7450 7951 10450 1578 -393 1703 A C ATOM 38 CE LYS A 6 6.290 161.723 249.883 1.00 73.29 A C ANISOU 38 CE LYS A 6 8122 8740 10985 1537 -462 1830 A C ATOM 39 NZ LYS A 6 5.465 160.564 249.437 1.00 76.08 A N1+ ANISOU 39 NZ LYS A 6 8314 9389 11204 1509 -565 1797 A N1+ ATOM 40 N THR A 7 8.510 158.865 254.101 1.00 39.81 A N ANISOU 40 N THR A 7 3783 4359 6986 982 -352 1314 A N ATOM 41 CA THR A 7 9.880 158.429 253.892 1.00 33.98 A C ANISOU 41 CA THR A 7 3118 3543 6252 833 -352 1323 A C ATOM 42 C THR A 7 9.919 157.531 252.669 1.00 34.55 A C ANISOU 42 C THR A 7 3151 3809 6167 783 -441 1403 A C ATOM 43 O THR A 7 8.871 157.094 252.182 1.00 33.98 A O ANISOU 43 O THR A 7 2989 3930 5992 832 -509 1415 A O ATOM 44 CB THR A 7 10.439 157.700 255.137 1.00 34.71 A C ANISOU 44 CB THR A 7 3206 3609 6373 697 -323 1149 A C ATOM 45 CG2 THR A 7 9.672 156.405 255.405 1.00 32.89 A C ANISOU 45 CG2 THR A 7 2849 3606 6042 641 -382 1070 A C ATOM 46 OG1 THR A 7 11.829 157.406 254.952 1.00 35.10 A O ANISOU 46 OG1 THR A 7 3352 3596 6388 549 -308 1134 A O ATOM 47 N GLN A 8 11.115 157.279 252.150 1.00 32.79 A N ANISOU 47 N GLN A 8 3001 3544 5915 689 -442 1452 A N ATOM 48 CA GLN A 8 11.252 156.330 251.054 1.00 32.44 A C ANISOU 48 CA GLN A 8 2938 3687 5701 644 -525 1501 A C ATOM 49 C GLN A 8 11.159 154.899 251.571 1.00 30.83 A C ANISOU 49 C GLN A 8 2682 3620 5413 521 -580 1349 A C ATOM 50 O GLN A 8 10.324 154.116 251.114 1.00 31.40 A O ANISOU 50 O GLN A 8 2676 3871 5385 524 -673 1342 A O ATOM 51 CB GLN A 8 12.570 156.551 250.299 1.00 31.30 A C ANISOU 51 CB GLN A 8 2896 3478 5516 590 -490 1596 A C ATOM 52 CG GLN A 8 12.611 157.859 249.490 1.00 34.19 A C ANISOU 52 CG GLN A 8 3334 3744 5911 688 -439 1761 A C ATOM 53 CD GLN A 8 13.917 158.040 248.728 1.00 35.70 A C ANISOU 53 CD GLN A 8 3607 3899 6059 621 -396 1875 A C ATOM 54 NE2 GLN A 8 13.866 157.843 247.416 1.00 37.28 A N ANISOU 54 NE2 GLN A 8 3816 4254 6095 670 -434 1981 A N ATOM 55 OE1 GLN A 8 14.957 158.356 249.312 1.00 36.40 A O ANISOU 55 OE1 GLN A 8 3746 3833 6250 523 -325 1859 A O ATOM 56 N VAL A 9 12.000 154.571 252.548 1.00 28.23 A N ANISOU 56 N VAL A 9 2408 3202 5118 406 -522 1221 A N ATOM 57 CA VAL A 9 12.048 153.220 253.091 1.00 25.18 A C ANISOU 57 CA VAL A 9 2006 2915 4648 287 -562 1082 A C ATOM 58 C VAL A 9 11.760 153.190 254.582 1.00 27.26 A C ANISOU 58 C VAL A 9 2240 3115 5001 251 -506 949 A C ATOM 59 O VAL A 9 12.351 153.957 255.340 1.00 30.82 A O ANISOU 59 O VAL A 9 2744 3413 5553 252 -424 910 A O ATOM 60 CB VAL A 9 13.447 152.593 252.886 1.00 25.57 A C ANISOU 60 CB VAL A 9 2152 2952 4609 188 -550 1045 A C ATOM 61 CG1 VAL A 9 13.498 151.183 253.462 1.00 22.02 A C ANISOU 61 CG1 VAL A 9 1712 2582 4072 84 -592 906 A C ATOM 62 CG2 VAL A 9 13.839 152.611 251.406 1.00 23.92 A C ANISOU 62 CG2 VAL A 9 1978 2821 4290 232 -591 1176 A C ATOM 63 N VAL A 10 10.863 152.298 255.002 1.00 25.36 A N ANISOU 63 N VAL A 10 1918 3000 4719 212 -553 881 A N ATOM 64 CA VAL A 10 10.710 152.007 256.423 1.00 22.73 A C ANISOU 64 CA VAL A 10 1566 2638 4433 158 -498 754 A C ATOM 65 C VAL A 10 11.134 150.559 256.678 1.00 25.45 A C ANISOU 65 C VAL A 10 1955 3048 4667 17 -540 664 A C ATOM 66 O VAL A 10 10.750 149.641 255.947 1.00 28.24 A O ANISOU 66 O VAL A 10 2291 3518 4921 -33 -631 684 A O ATOM 67 CB VAL A 10 9.278 152.295 256.945 1.00 23.13 A C ANISOU 67 CB VAL A 10 1477 2768 4542 236 -489 757 A C ATOM 68 CG1 VAL A 10 8.232 151.406 256.263 1.00 23.52 A C ANISOU 68 CG1 VAL A 10 1413 3017 4506 200 -593 799 A C ATOM 69 CG2 VAL A 10 9.221 152.153 258.463 1.00 23.20 A C ANISOU 69 CG2 VAL A 10 1479 2742 4594 199 -410 632 A C ATOM 70 N VAL A 11 11.921 150.354 257.728 1.00 23.14 A N ANISOU 70 N VAL A 11 1730 2676 4388 -43 -478 561 A N ATOM 71 CA VAL A 11 12.400 149.018 258.066 1.00 22.84 A C ANISOU 71 CA VAL A 11 1755 2677 4246 -157 -509 479 A C ATOM 72 C VAL A 11 11.783 148.635 259.395 1.00 24.59 A C ANISOU 72 C VAL A 11 1933 2920 4492 -199 -467 396 A C ATOM 73 O VAL A 11 11.934 149.352 260.389 1.00 20.21 A O ANISOU 73 O VAL A 11 1374 2292 4012 -159 -385 343 A O ATOM 74 CB VAL A 11 13.933 148.986 258.193 1.00 19.90 A C ANISOU 74 CB VAL A 11 1496 2222 3844 -184 -476 435 A C ATOM 75 CG1 VAL A 11 14.408 147.593 258.582 1.00 17.46 A C ANISOU 75 CG1 VAL A 11 1263 1950 3422 -271 -508 353 A C ATOM 76 CG2 VAL A 11 14.594 149.448 256.892 1.00 21.45 A C ANISOU 76 CG2 VAL A 11 1725 2412 4014 -141 -498 534 A C ATOM 77 N LEU A 12 11.074 147.511 259.408 1.00 24.16 A N ANISOU 77 N LEU A 12 1847 2964 4367 -283 -524 386 A N ATOM 78 CA LEU A 12 10.403 147.066 260.616 1.00 18.75 A C ANISOU 78 CA LEU A 12 1111 2321 3692 -336 -478 331 A C ATOM 79 C LEU A 12 11.251 146.025 261.342 1.00 26.36 A C ANISOU 79 C LEU A 12 2204 3240 4570 -425 -467 250 A C ATOM 80 O LEU A 12 11.295 144.852 260.952 1.00 22.26 A O ANISOU 80 O LEU A 12 1765 2747 3945 -509 -531 243 A O ATOM 81 CB LEU A 12 9.019 146.522 260.268 1.00 19.85 A C ANISOU 81 CB LEU A 12 1165 2599 3779 -379 -524 373 A C ATOM 82 CG LEU A 12 8.128 146.072 261.424 1.00 32.71 A C ANISOU 82 CG LEU A 12 2728 4307 5395 -435 -465 339 A C ATOM 83 CD1 LEU A 12 7.859 147.247 262.352 1.00 31.48 A C ANISOU 83 CD1 LEU A 12 2469 4139 5352 -317 -364 328 A C ATOM 84 CD2 LEU A 12 6.825 145.490 260.904 1.00 28.68 A C ANISOU 84 CD2 LEU A 12 2126 3942 4829 -499 -520 380 A C ATOM 85 N GLY A 13 11.933 146.469 262.399 1.00 23.42 A N ANISOU 85 N GLY A 13 1869 2798 4232 -393 -386 181 A N ATOM 86 CA GLY A 13 12.816 145.602 263.161 1.00 18.38 A C ANISOU 86 CA GLY A 13 1345 2124 3512 -451 -373 108 A C ATOM 87 C GLY A 13 14.262 146.042 263.040 1.00 17.48 A C ANISOU 87 C GLY A 13 1319 1930 3391 -407 -361 69 A C ATOM 88 O GLY A 13 14.730 146.327 261.934 1.00 19.90 A O ANISOU 88 O GLY A 13 1642 2221 3697 -382 -401 119 A O ATOM 89 N ALA A 14 14.970 146.122 264.166 1.00 18.66 A N ANISOU 89 N ALA A 14 1515 2045 3530 -400 -306 -13 A N ATOM 90 CA ALA A 14 16.359 146.579 264.145 1.00 14.81 A C ANISOU 90 CA ALA A 14 1085 1502 3040 -374 -296 -55 A C ATOM 91 C ALA A 14 17.375 145.486 264.494 1.00 17.28 A C ANISOU 91 C ALA A 14 1500 1834 3232 -400 -320 -104 A C ATOM 92 O ALA A 14 18.457 145.773 265.027 1.00 19.66 A O ANISOU 92 O ALA A 14 1829 2119 3521 -382 -298 -166 A O ATOM 93 CB ALA A 14 16.537 147.784 265.069 1.00 17.86 A C ANISOU 93 CB ALA A 14 1439 1829 3517 -331 -227 -121 A C ATOM 94 N GLY A 15 17.052 144.240 264.159 1.00 14.05 A N ANISOU 94 N GLY A 15 1150 1456 2732 -440 -371 -78 A N ATOM 95 CA GLY A 15 18.012 143.162 264.305 1.00 13.63 A C ANISOU 95 CA GLY A 15 1215 1408 2558 -439 -401 -114 A C ATOM 96 C GLY A 15 19.029 143.206 263.178 1.00 15.68 A C ANISOU 96 C GLY A 15 1505 1677 2777 -395 -440 -90 A C ATOM 97 O GLY A 15 18.996 144.118 262.352 1.00 19.87 A O ANISOU 97 O GLY A 15 1967 2206 3378 -379 -437 -40 A O ATOM 98 N PRO A 16 19.933 142.214 263.134 1.00 17.79 A N ANISOU 98 N PRO A 16 1878 1959 2922 -365 -471 -119 A N ATOM 99 CA PRO A 16 21.010 142.126 262.136 1.00 18.56 A C ANISOU 99 CA PRO A 16 2003 2095 2952 -303 -498 -101 A C ATOM 100 C PRO A 16 20.510 142.407 260.720 1.00 13.41 A C ANISOU 100 C PRO A 16 1322 1454 2319 -303 -535 -25 A C ATOM 101 O PRO A 16 21.053 143.255 259.991 1.00 22.98 A O ANISOU 101 O PRO A 16 2471 2696 3564 -272 -516 21 A O ATOM 102 CB PRO A 16 21.461 140.664 262.234 1.00 22.79 A C ANISOU 102 CB PRO A 16 2687 2631 3341 -264 -543 -136 A C ATOM 103 CG PRO A 16 21.082 140.235 263.591 1.00 17.94 A C ANISOU 103 CG PRO A 16 2110 1983 2724 -301 -519 -178 A C ATOM 104 CD PRO A 16 19.869 141.018 263.996 1.00 16.64 A C ANISOU 104 CD PRO A 16 1840 1797 2684 -379 -483 -157 A C ATOM 105 N ALA A 17 19.449 141.701 260.353 1.00 16.01 A N ANISOU 105 N ALA A 17 1695 1764 2625 -347 -591 -7 A N ATOM 106 CA ALA A 17 18.834 141.866 259.049 1.00 20.22 A C ANISOU 106 CA ALA A 17 2202 2323 3158 -348 -644 59 A C ATOM 107 C ALA A 17 18.322 143.297 258.863 1.00 19.05 A C ANISOU 107 C ALA A 17 1913 2179 3146 -349 -600 122 A C ATOM 108 O ALA A 17 18.659 143.969 257.879 1.00 19.83 A O ANISOU 108 O ALA A 17 1976 2307 3252 -303 -600 186 A O ATOM 109 CB ALA A 17 17.707 140.870 258.875 1.00 14.65 A C ANISOU 109 CB ALA A 17 1553 1600 2415 -422 -719 54 A C ATOM 110 N GLY A 18 17.503 143.747 259.810 1.00 19.44 A N ANISOU 110 N GLY A 18 1891 2200 3296 -390 -560 108 A N ATOM 111 CA GLY A 18 16.892 145.067 259.745 1.00 14.72 A C ANISOU 111 CA GLY A 18 1177 1589 2828 -371 -519 159 A C ATOM 112 C GLY A 18 17.869 146.224 259.705 1.00 22.11 A C ANISOU 112 C GLY A 18 2085 2486 3830 -328 -461 173 A C ATOM 113 O GLY A 18 17.786 147.096 258.829 1.00 19.94 A O ANISOU 113 O GLY A 18 1764 2203 3608 -293 -458 256 A O ATOM 114 N TYR A 19 18.792 146.263 260.661 1.00 22.02 A N ANISOU 114 N TYR A 19 2099 2450 3816 -336 -417 97 A N ATOM 115 CA TYR A 19 19.715 147.389 260.687 1.00 26.09 A C ANISOU 115 CA TYR A 19 2581 2926 4407 -325 -368 104 A C ATOM 116 C TYR A 19 20.708 147.297 259.537 1.00 26.27 A C ANISOU 116 C TYR A 19 2619 3002 4359 -304 -384 170 A C ATOM 117 O TYR A 19 21.131 148.333 259.016 1.00 22.62 A O ANISOU 117 O TYR A 19 2115 2512 3970 -304 -352 237 A O ATOM 118 CB TYR A 19 20.392 147.593 262.058 1.00 21.88 A C ANISOU 118 CB TYR A 19 2052 2364 3895 -347 -325 -3 A C ATOM 119 CG TYR A 19 21.566 146.691 262.381 1.00 25.51 A C ANISOU 119 CG TYR A 19 2565 2892 4236 -344 -341 -60 A C ATOM 120 CD1 TYR A 19 22.797 146.860 261.755 1.00 25.38 A C ANISOU 120 CD1 TYR A 19 2534 2924 4185 -336 -340 -32 A C ATOM 121 CD2 TYR A 19 21.450 145.688 263.338 1.00 19.19 A C ANISOU 121 CD2 TYR A 19 1823 2115 3352 -342 -352 -133 A C ATOM 122 CE1 TYR A 19 23.866 146.039 262.054 1.00 25.90 A C ANISOU 122 CE1 TYR A 19 2634 3074 4135 -309 -354 -82 A C ATOM 123 CE2 TYR A 19 22.516 144.867 263.642 1.00 22.15 A C ANISOU 123 CE2 TYR A 19 2252 2552 3612 -314 -369 -180 A C ATOM 124 CZ TYR A 19 23.718 145.051 262.998 1.00 30.06 A C ANISOU 124 CZ TYR A 19 3230 3613 4580 -290 -372 -158 A C ATOM 125 OH TYR A 19 24.785 144.242 263.300 1.00 44.47 A O ANISOU 125 OH TYR A 19 5094 5520 6283 -239 -388 -203 A O ATOM 126 N SER A 20 21.063 146.078 259.111 1.00 21.67 A N ANISOU 126 N SER A 20 2106 2494 3635 -281 -431 157 A N ATOM 127 CA SER A 20 21.949 145.990 257.948 1.00 21.13 A C ANISOU 127 CA SER A 20 2048 2499 3482 -237 -440 221 A C ATOM 128 C SER A 20 21.257 146.545 256.707 1.00 22.03 A C ANISOU 128 C SER A 20 2132 2619 3620 -216 -458 335 A C ATOM 129 O SER A 20 21.860 147.303 255.928 1.00 25.62 A O ANISOU 129 O SER A 20 2547 3097 4089 -199 -425 425 A O ATOM 130 CB SER A 20 22.440 144.563 257.712 1.00 16.36 A C ANISOU 130 CB SER A 20 1543 1965 2709 -189 -489 174 A C ATOM 131 OG SER A 20 23.171 144.110 258.843 1.00 18.72 A O ANISOU 131 OG SER A 20 1867 2268 2978 -189 -470 83 A O ATOM 132 N ALA A 21 19.981 146.197 256.554 1.00 15.20 A N ANISOU 132 N ALA A 21 1276 1741 2759 -222 -511 340 A N ATOM 133 CA ALA A 21 19.172 146.700 255.447 1.00 16.20 A C ANISOU 133 CA ALA A 21 1365 1888 2903 -192 -542 445 A C ATOM 134 C ALA A 21 19.069 148.224 255.485 1.00 20.18 A C ANISOU 134 C ALA A 21 1791 2319 3557 -186 -478 523 A C ATOM 135 O ALA A 21 19.266 148.899 254.469 1.00 21.50 A O ANISOU 135 O ALA A 21 1940 2504 3726 -147 -467 638 A O ATOM 136 CB ALA A 21 17.784 146.085 255.491 1.00 16.05 A C ANISOU 136 CB ALA A 21 1341 1881 2877 -217 -612 424 A C ATOM 137 N ALA A 22 18.770 148.758 256.664 1.00 19.82 A N ANISOU 137 N ALA A 22 1714 2186 3632 -217 -434 463 A N ATOM 138 CA ALA A 22 18.596 150.196 256.842 1.00 21.94 A C ANISOU 138 CA ALA A 22 1934 2350 4050 -204 -377 515 A C ATOM 139 C ALA A 22 19.871 150.973 256.542 1.00 25.95 A C ANISOU 139 C ALA A 22 2448 2820 4592 -228 -324 566 A C ATOM 140 O ALA A 22 19.843 151.998 255.841 1.00 23.04 A O ANISOU 140 O ALA A 22 2065 2395 4295 -206 -297 683 A O ATOM 141 CB ALA A 22 18.141 150.490 258.257 1.00 16.83 A C ANISOU 141 CB ALA A 22 1271 1626 3500 -224 -341 411 A C ATOM 142 N PHE A 23 20.985 150.485 257.082 1.00 20.67 A N ANISOU 142 N PHE A 23 1796 2186 3870 -275 -308 486 A N ATOM 143 CA PHE A 23 22.276 151.135 256.884 1.00 21.43 A C ANISOU 143 CA PHE A 23 1873 2276 3994 -320 -259 527 A C ATOM 144 C PHE A 23 22.670 151.065 255.408 1.00 25.38 A C ANISOU 144 C PHE A 23 2369 2873 4402 -282 -261 667 A C ATOM 145 O PHE A 23 23.228 152.023 254.857 1.00 26.88 A O ANISOU 145 O PHE A 23 2530 3030 4652 -311 -212 778 A O ATOM 146 CB PHE A 23 23.359 150.496 257.766 1.00 18.69 A C ANISOU 146 CB PHE A 23 1525 1989 3587 -362 -253 410 A C ATOM 147 CG PHE A 23 23.196 150.765 259.245 1.00 22.08 A C ANISOU 147 CG PHE A 23 1957 2331 4102 -404 -241 278 A C ATOM 148 CD1 PHE A 23 22.165 151.567 259.724 1.00 21.43 A C ANISOU 148 CD1 PHE A 23 1876 2120 4144 -398 -227 264 A C ATOM 149 CD2 PHE A 23 24.073 150.190 260.158 1.00 20.84 A C ANISOU 149 CD2 PHE A 23 1799 2234 3884 -431 -245 166 A C ATOM 150 CE1 PHE A 23 22.019 151.804 261.081 1.00 18.17 A C ANISOU 150 CE1 PHE A 23 1472 1642 3790 -420 -212 135 A C ATOM 151 CE2 PHE A 23 23.935 150.416 261.519 1.00 20.06 A C ANISOU 151 CE2 PHE A 23 1707 2073 3841 -460 -237 42 A C ATOM 152 CZ PHE A 23 22.909 151.226 261.982 1.00 23.49 A C ANISOU 152 CZ PHE A 23 2150 2380 4396 -456 -219 23 A C ATOM 153 N ARG A 24 22.369 149.942 254.758 1.00 17.55 A N ANISOU 153 N ARG A 24 1412 1995 3260 -219 -318 665 A N ATOM 154 CA ARG A 24 22.681 149.836 253.335 1.00 21.36 A C ANISOU 154 CA ARG A 24 1900 2585 3630 -162 -324 788 A C ATOM 155 C ARG A 24 21.834 150.832 252.525 1.00 20.52 A C ANISOU 155 C ARG A 24 1777 2422 3598 -131 -321 929 A C ATOM 156 O ARG A 24 22.349 151.523 251.640 1.00 22.21 A O ANISOU 156 O ARG A 24 1972 2659 3806 -120 -277 1069 A O ATOM 157 CB ARG A 24 22.485 148.401 252.836 1.00 22.39 A C ANISOU 157 CB ARG A 24 2095 2833 3577 -97 -399 733 A C ATOM 158 CG ARG A 24 22.978 148.167 251.413 1.00 22.71 A C ANISOU 158 CG ARG A 24 2154 3011 3465 -20 -404 834 A C ATOM 159 CD ARG A 24 24.435 147.736 251.383 1.00 23.71 A C ANISOU 159 CD ARG A 24 2273 3247 3489 0 -357 813 A C ATOM 160 NE ARG A 24 24.928 147.633 250.013 1.00 26.98 A N ANISOU 160 NE ARG A 24 2692 3807 3751 85 -343 922 A N ATOM 161 CZ ARG A 24 25.634 148.580 249.402 1.00 28.94 A C ANISOU 161 CZ ARG A 24 2866 4105 4023 70 -261 1067 A C ATOM 162 NH1 ARG A 24 25.946 149.698 250.046 1.00 21.93 A N1+ ANISOU 162 NH1 ARG A 24 1904 3111 3315 -39 -194 1112 A N1+ ATOM 163 NH2 ARG A 24 26.037 148.406 248.151 1.00 30.20 A N ANISOU 163 NH2 ARG A 24 3034 4420 4022 161 -244 1168 A N ATOM 164 N CYS A 25 20.549 150.937 252.856 1.00 20.68 A N ANISOU 164 N CYS A 25 1795 2375 3687 -111 -362 903 A N ATOM 165 CA CYS A 25 19.682 151.932 252.226 1.00 23.98 A C ANISOU 165 CA CYS A 25 2191 2735 4184 -59 -361 1032 A C ATOM 166 C CYS A 25 20.240 153.343 252.394 1.00 26.41 A C ANISOU 166 C CYS A 25 2490 2902 4644 -97 -276 1117 A C ATOM 167 O CYS A 25 20.272 154.120 251.441 1.00 26.45 A O ANISOU 167 O CYS A 25 2498 2891 4660 -61 -252 1278 A O ATOM 168 CB CYS A 25 18.269 151.878 252.814 1.00 22.81 A C ANISOU 168 CB CYS A 25 2018 2544 4103 -32 -407 973 A C ATOM 169 SG CYS A 25 17.235 150.551 252.169 1.00 28.04 A S ANISOU 169 SG CYS A 25 2681 3364 4611 6 -525 942 A S ATOM 170 N ALA A 26 20.669 153.675 253.610 1.00 25.43 A N ANISOU 170 N ALA A 26 2363 2668 4630 -175 -235 1008 A N ATOM 171 CA ALA A 26 21.224 155.000 253.868 1.00 26.90 A C ANISOU 171 CA ALA A 26 2556 2696 4970 -236 -165 1064 A C ATOM 172 C ALA A 26 22.483 155.249 253.053 1.00 26.43 A C ANISOU 172 C ALA A 26 2482 2695 4865 -294 -117 1183 A C ATOM 173 O ALA A 26 22.636 156.319 252.456 1.00 27.24 A O ANISOU 173 O ALA A 26 2598 2704 5049 -309 -70 1334 A O ATOM 174 CB ALA A 26 21.510 155.185 255.349 1.00 29.29 A C ANISOU 174 CB ALA A 26 2861 2892 5374 -312 -146 899 A C ATOM 175 N ASP A 27 23.370 154.257 253.008 1.00 26.54 A N ANISOU 175 N ASP A 27 2470 2871 4744 -318 -124 1126 A N ATOM 176 CA ASP A 27 24.615 154.388 252.248 1.00 28.38 A C ANISOU 176 CA ASP A 27 2664 3207 4913 -364 -70 1236 A C ATOM 177 C ASP A 27 24.335 154.510 250.753 1.00 26.79 A C ANISOU 177 C ASP A 27 2475 3090 4613 -277 -65 1423 A C ATOM 178 O ASP A 27 25.147 155.050 250.000 1.00 27.47 A O ANISOU 178 O ASP A 27 2532 3221 4683 -313 0 1574 A O ATOM 179 CB ASP A 27 25.535 153.185 252.504 1.00 28.70 A C ANISOU 179 CB ASP A 27 2673 3427 4806 -365 -83 1127 A C ATOM 180 CG ASP A 27 26.145 153.189 253.902 1.00 29.32 A C ANISOU 180 CG ASP A 27 2723 3451 4966 -460 -77 971 A C ATOM 181 OD1 ASP A 27 26.037 154.216 254.608 1.00 26.86 A O ANISOU 181 OD1 ASP A 27 2413 2967 4827 -546 -54 951 A O ATOM 182 OD2 ASP A 27 26.735 152.157 254.293 1.00 27.60 A O1- ANISOU 182 OD2 ASP A 27 2490 3364 4632 -439 -98 865 A O1- ATOM 183 N LEU A 28 23.174 154.027 250.326 1.00 23.27 A N ANISOU 183 N LEU A 28 2067 2678 4099 -166 -135 1420 A N ATOM 184 CA LEU A 28 22.819 154.088 248.914 1.00 26.61 A C ANISOU 184 CA LEU A 28 2504 3198 4407 -69 -148 1584 A C ATOM 185 C LEU A 28 22.006 155.333 248.598 1.00 29.04 A C ANISOU 185 C LEU A 28 2832 3354 4846 -36 -132 1727 A C ATOM 186 O LEU A 28 21.542 155.511 247.467 1.00 28.72 A O ANISOU 186 O LEU A 28 2807 3383 4721 60 -150 1876 A O ATOM 187 CB LEU A 28 22.071 152.821 248.482 1.00 25.97 A C ANISOU 187 CB LEU A 28 2452 3262 4155 31 -248 1505 A C ATOM 188 CG LEU A 28 22.990 151.601 248.358 1.00 29.50 A C ANISOU 188 CG LEU A 28 2908 3875 4427 41 -258 1413 A C ATOM 189 CD1 LEU A 28 22.203 150.319 248.193 1.00 21.95 A C ANISOU 189 CD1 LEU A 28 2006 3003 3332 111 -368 1296 A C ATOM 190 CD2 LEU A 28 23.943 151.799 247.194 1.00 32.01 A C ANISOU 190 CD2 LEU A 28 3208 4335 4618 79 -195 1567 A C ATOM 191 N GLY A 29 21.838 156.192 249.602 1.00 27.48 A N ANISOU 191 N GLY A 29 2644 2950 4846 -102 -102 1679 A N ATOM 192 CA GLY A 29 21.261 157.507 249.388 1.00 27.25 A C ANISOU 192 CA GLY A 29 2653 2739 4960 -70 -72 1817 A C ATOM 193 C GLY A 29 19.760 157.564 249.542 1.00 29.83 A C ANISOU 193 C GLY A 29 2990 3022 5324 53 -138 1786 A C ATOM 194 O GLY A 29 19.130 158.525 249.113 1.00 33.28 A O ANISOU 194 O GLY A 29 3460 3348 5837 134 -127 1922 A O ATOM 195 N LEU A 30 19.180 156.545 250.167 1.00 29.43 A N ANISOU 195 N LEU A 30 2906 3057 5217 71 -204 1615 A N ATOM 196 CA LEU A 30 17.733 156.505 250.363 1.00 28.77 A C ANISOU 196 CA LEU A 30 2801 2970 5161 175 -267 1581 A C ATOM 197 C LEU A 30 17.336 157.052 251.734 1.00 28.92 A C ANISOU 197 C LEU A 30 2824 2815 5350 156 -238 1456 A C ATOM 198 O LEU A 30 18.035 156.822 252.727 1.00 31.19 A O ANISOU 198 O LEU A 30 3118 3054 5677 51 -208 1318 A O ATOM 199 CB LEU A 30 17.229 155.065 250.206 1.00 27.23 A C ANISOU 199 CB LEU A 30 2566 2973 4805 193 -358 1480 A C ATOM 200 CG LEU A 30 17.607 154.387 248.885 1.00 28.95 A C ANISOU 200 CG LEU A 30 2796 3374 4829 226 -399 1568 A C ATOM 201 CD1 LEU A 30 17.331 152.886 248.912 1.00 28.00 A C ANISOU 201 CD1 LEU A 30 2670 3409 4561 212 -489 1429 A C ATOM 202 CD2 LEU A 30 16.860 155.042 247.741 1.00 34.99 A C ANISOU 202 CD2 LEU A 30 3556 4176 5562 349 -428 1749 A C ATOM 203 N GLU A 31 16.209 157.758 251.793 1.00 31.08 A N ANISOU 203 N GLU A 31 3091 3010 5709 271 -248 1501 A N ATOM 204 CA GLU A 31 15.686 158.228 253.074 1.00 34.27 A C ANISOU 204 CA GLU A 31 3496 3273 6251 288 -222 1373 A C ATOM 205 C GLU A 31 15.089 157.036 253.810 1.00 33.45 A C ANISOU 205 C GLU A 31 3320 3316 6074 270 -271 1212 A C ATOM 206 O GLU A 31 14.188 156.372 253.294 1.00 34.31 A O ANISOU 206 O GLU A 31 3362 3586 6090 332 -340 1237 A O ATOM 207 CB GLU A 31 14.602 159.287 252.862 1.00 36.72 A C ANISOU 207 CB GLU A 31 3815 3479 6658 450 -218 1474 A C ATOM 208 CG GLU A 31 15.029 160.472 252.013 1.00 54.41 A C ANISOU 208 CG GLU A 31 6147 5579 8948 479 -171 1651 A C ATOM 209 CD GLU A 31 13.852 161.351 251.608 1.00 66.36 A C ANISOU 209 CD GLU A 31 7679 7072 10462 652 -175 1721 A C ATOM 210 OE1 GLU A 31 12.699 160.989 251.934 1.00 69.57 A O ANISOU 210 OE1 GLU A 31 8003 7584 10847 757 -219 1658 A O ATOM 211 OE2 GLU A 31 14.077 162.398 250.962 1.00 68.48 A O1- ANISOU 211 OE2 GLU A 31 8044 7230 10747 682 -134 1841 A O1- ATOM 212 N THR A 32 15.576 156.776 255.021 1.00 36.20 A N ANISOU 212 N THR A 32 3682 3611 6461 180 -239 1050 A N ATOM 213 CA THR A 32 15.294 155.512 255.698 1.00 30.91 A C ANISOU 213 CA THR A 32 2963 3080 5703 132 -277 911 A C ATOM 214 C THR A 32 14.909 155.745 257.150 1.00 28.00 A C ANISOU 214 C THR A 32 2587 2629 5421 136 -237 766 A C ATOM 215 O THR A 32 15.550 156.524 257.854 1.00 26.52 A O ANISOU 215 O THR A 32 2459 2286 5332 103 -182 707 A O ATOM 216 CB THR A 32 16.533 154.585 255.671 1.00 30.59 A C ANISOU 216 CB THR A 32 2953 3112 5558 13 -284 855 A C ATOM 217 CG2 THR A 32 16.198 153.200 256.227 1.00 21.98 A C ANISOU 217 CG2 THR A 32 1836 2152 4363 -26 -331 734 A C ATOM 218 OG1 THR A 32 17.013 154.453 254.326 1.00 30.92 A O ANISOU 218 OG1 THR A 32 3008 3232 5508 21 -307 988 A O ATOM 219 N VAL A 33 13.878 155.037 257.600 1.00 24.07 A N ANISOU 219 N VAL A 33 2016 2249 4882 168 -265 705 A N ATOM 220 CA VAL A 33 13.434 155.096 258.986 1.00 24.13 A C ANISOU 220 CA VAL A 33 2005 2225 4940 180 -222 571 A C ATOM 221 C VAL A 33 13.364 153.677 259.533 1.00 24.36 A C ANISOU 221 C VAL A 33 2000 2398 4857 91 -251 478 A C ATOM 222 O VAL A 33 12.841 152.777 258.872 1.00 20.76 A O ANISOU 222 O VAL A 33 1494 2081 4311 71 -316 526 A O ATOM 223 CB VAL A 33 12.030 155.753 259.102 1.00 30.71 A C ANISOU 223 CB VAL A 33 2762 3067 5841 330 -209 607 A C ATOM 224 CG1 VAL A 33 11.496 155.666 260.530 1.00 30.55 A C ANISOU 224 CG1 VAL A 33 2706 3059 5843 353 -158 469 A C ATOM 225 CG2 VAL A 33 12.055 157.205 258.616 1.00 28.84 A C ANISOU 225 CG2 VAL A 33 2584 2655 5721 441 -178 703 A C ATOM 226 N ILE A 34 13.883 153.475 260.740 1.00 24.39 A N ANISOU 226 N ILE A 34 2041 2363 4862 35 -210 346 A N ATOM 227 CA ILE A 34 13.791 152.169 261.385 1.00 22.56 A C ANISOU 227 CA ILE A 34 1794 2249 4527 -41 -228 266 A C ATOM 228 C ILE A 34 12.727 152.203 262.468 1.00 25.97 A C ANISOU 228 C ILE A 34 2159 2723 4984 8 -184 202 A C ATOM 229 O ILE A 34 12.674 153.152 263.245 1.00 27.15 A O ANISOU 229 O ILE A 34 2322 2778 5214 77 -123 141 A O ATOM 230 CB ILE A 34 15.113 151.788 262.074 1.00 23.15 A C ANISOU 230 CB ILE A 34 1952 2286 4559 -125 -212 167 A C ATOM 231 CG1 ILE A 34 16.269 151.792 261.081 1.00 28.85 A C ANISOU 231 CG1 ILE A 34 2724 2988 5251 -169 -240 229 A C ATOM 232 CG2 ILE A 34 15.002 150.416 262.722 1.00 29.61 A C ANISOU 232 CG2 ILE A 34 2775 3212 5265 -189 -231 101 A C ATOM 233 CD1 ILE A 34 17.607 151.426 261.707 1.00 29.21 A C ANISOU 233 CD1 ILE A 34 2825 3025 5248 -242 -229 139 A C ATOM 234 N VAL A 35 11.893 151.168 262.536 1.00 21.59 A N ANISOU 234 N VAL A 35 1536 2311 4357 -31 -214 213 A N ATOM 235 CA VAL A 35 10.929 151.046 263.623 1.00 23.19 A C ANISOU 235 CA VAL A 35 1661 2589 4563 -3 -161 160 A C ATOM 236 C VAL A 35 11.355 149.874 264.499 1.00 24.05 A C ANISOU 236 C VAL A 35 1819 2746 4575 -113 -154 82 A C ATOM 237 O VAL A 35 11.614 148.784 263.993 1.00 23.67 A O ANISOU 237 O VAL A 35 1806 2744 4443 -210 -217 109 A O ATOM 238 CB VAL A 35 9.493 150.830 263.092 1.00 25.07 A C ANISOU 238 CB VAL A 35 1753 2971 4802 30 -192 250 A C ATOM 239 CG1 VAL A 35 8.523 150.604 264.240 1.00 21.62 A C ANISOU 239 CG1 VAL A 35 1216 2644 4356 46 -126 206 A C ATOM 240 CG2 VAL A 35 9.052 152.019 262.250 1.00 22.00 A C ANISOU 240 CG2 VAL A 35 1318 2540 4501 168 -200 336 A C ATOM 241 N GLU A 36 11.457 150.101 265.805 1.00 19.12 A N ANISOU 241 N GLU A 36 1212 2102 3950 -86 -80 -16 A N ATOM 242 CA GLU A 36 11.859 149.034 266.721 1.00 18.43 A C ANISOU 242 CA GLU A 36 1179 2062 3761 -173 -67 -80 A C ATOM 243 C GLU A 36 11.139 149.177 268.047 1.00 25.06 A C ANISOU 243 C GLU A 36 1965 2968 4589 -123 20 -140 A C ATOM 244 O GLU A 36 11.137 150.254 268.643 1.00 25.36 A O ANISOU 244 O GLU A 36 2004 2946 4684 -17 78 -209 A O ATOM 245 CB GLU A 36 13.384 149.033 266.929 1.00 22.45 A C ANISOU 245 CB GLU A 36 1815 2476 4239 -205 -81 -154 A C ATOM 246 CG GLU A 36 13.879 148.145 268.081 1.00 22.84 A C ANISOU 246 CG GLU A 36 1929 2567 4182 -254 -59 -232 A C ATOM 247 CD GLU A 36 13.607 146.658 267.861 1.00 26.53 A C ANISOU 247 CD GLU A 36 2418 3112 4550 -348 -101 -174 A C ATOM 248 OE1 GLU A 36 12.979 146.040 268.747 1.00 26.65 A O ANISOU 248 OE1 GLU A 36 2415 3200 4509 -376 -59 -180 A O ATOM 249 OE2 GLU A 36 14.020 146.106 266.814 1.00 27.23 A O1- ANISOU 249 OE2 GLU A 36 2550 3183 4611 -394 -174 -123 A O1- ATOM 250 N ARG A 37 10.551 148.079 268.516 1.00 24.77 A N ANISOU 250 N ARG A 37 1892 3048 4470 -201 31 -114 A N ATOM 251 CA ARG A 37 9.716 148.113 269.710 1.00 22.61 A C ANISOU 251 CA ARG A 37 1544 2879 4169 -158 124 -144 A C ATOM 252 C ARG A 37 10.560 148.220 270.965 1.00 26.04 A C ANISOU 252 C ARG A 37 2081 3271 4541 -127 179 -263 A C ATOM 253 O ARG A 37 10.104 148.725 271.984 1.00 32.56 A O ANISOU 253 O ARG A 37 2869 4149 5355 -37 264 -323 A O ATOM 254 CB ARG A 37 8.802 146.884 269.771 1.00 25.85 A C ANISOU 254 CB ARG A 37 1876 3430 4514 -277 121 -58 A C ATOM 255 CG ARG A 37 9.540 145.559 269.885 1.00 23.86 A C ANISOU 255 CG ARG A 37 1754 3149 4163 -414 75 -54 A C ATOM 256 CD ARG A 37 8.595 144.358 269.894 1.00 22.23 A C ANISOU 256 CD ARG A 37 1486 3053 3906 -555 65 39 A C ATOM 257 NE ARG A 37 9.364 143.121 269.773 1.00 25.54 A N ANISOU 257 NE ARG A 37 2064 3399 4241 -673 3 46 A N ATOM 258 CZ ARG A 37 8.840 141.908 269.610 1.00 29.99 A C ANISOU 258 CZ ARG A 37 2641 3995 4759 -826 -35 121 A C ATOM 259 NH1 ARG A 37 7.520 141.737 269.557 1.00 25.15 A N1+ ANISOU 259 NH1 ARG A 37 1868 3511 4178 -904 -18 200 A N1+ ATOM 260 NH2 ARG A 37 9.645 140.859 269.503 1.00 25.94 A N ANISOU 260 NH2 ARG A 37 2304 3386 4167 -901 -93 115 A N ATOM 261 N TYR A 38 11.799 147.754 270.893 1.00 26.61 A N ANISOU 261 N TYR A 38 2281 3266 4565 -190 127 -301 A N ATOM 262 CA TYR A 38 12.663 147.845 272.061 1.00 35.04 A C ANISOU 262 CA TYR A 38 3440 4312 5564 -161 162 -417 A C ATOM 263 C TYR A 38 13.598 149.054 272.009 1.00 34.79 A C ANISOU 263 C TYR A 38 3462 4151 5606 -98 146 -515 A C ATOM 264 O TYR A 38 13.722 149.701 270.968 1.00 31.62 A O ANISOU 264 O TYR A 38 3047 3662 5304 -90 107 -474 A O ATOM 265 CB TYR A 38 13.345 146.505 272.347 1.00 43.02 A C ANISOU 265 CB TYR A 38 4545 5352 6450 -255 128 -404 A C ATOM 266 CG TYR A 38 12.301 145.472 272.719 1.00 54.06 A C ANISOU 266 CG TYR A 38 5897 6864 7781 -320 166 -318 A C ATOM 267 CD1 TYR A 38 11.170 145.857 273.434 1.00 57.29 A C ANISOU 267 CD1 TYR A 38 6194 7377 8197 -268 258 -311 A C ATOM 268 CD2 TYR A 38 12.428 144.134 272.360 1.00 54.76 A C ANISOU 268 CD2 TYR A 38 6053 6955 7799 -434 114 -243 A C ATOM 269 CE1 TYR A 38 10.195 144.953 273.783 1.00 58.54 A C ANISOU 269 CE1 TYR A 38 6288 7656 8299 -346 301 -219 A C ATOM 270 CE2 TYR A 38 11.449 143.208 272.713 1.00 57.34 A C ANISOU 270 CE2 TYR A 38 6341 7372 8076 -522 148 -156 A C ATOM 271 CZ TYR A 38 10.335 143.631 273.426 1.00 64.53 A C ANISOU 271 CZ TYR A 38 7119 8402 8999 -486 245 -139 A C ATOM 272 OH TYR A 38 9.346 142.745 273.792 1.00 73.75 A O ANISOU 272 OH TYR A 38 8225 9676 10120 -590 288 -40 A O ATOM 273 N ASN A 39 14.230 149.367 273.137 1.00 33.09 A N ANISOU 273 N ASN A 39 3309 3924 5337 -59 176 -641 A N ATOM 274 CA ASN A 39 14.966 150.622 273.279 1.00 38.94 A C ANISOU 274 CA ASN A 39 4099 4540 6157 -9 166 -752 A C ATOM 275 C ASN A 39 16.391 150.606 272.749 1.00 35.74 A C ANISOU 275 C ASN A 39 3759 4058 5762 -88 89 -771 A C ATOM 276 O ASN A 39 17.044 151.648 272.688 1.00 41.13 A O ANISOU 276 O ASN A 39 4474 4626 6528 -82 71 -844 A O ATOM 277 CB ASN A 39 14.995 151.017 274.755 1.00 51.34 A C ANISOU 277 CB ASN A 39 5705 6143 7657 68 223 -898 A C ATOM 278 CG ASN A 39 15.501 149.887 275.642 1.00 62.54 A C ANISOU 278 CG ASN A 39 7172 7678 8913 25 221 -922 A C ATOM 279 ND2 ASN A 39 16.071 150.241 276.787 1.00 68.21 A N ANISOU 279 ND2 ASN A 39 7949 8410 9557 71 233 -1066 A N ATOM 280 OD1 ASN A 39 15.379 148.707 275.295 1.00 62.03 A O ANISOU 280 OD1 ASN A 39 7100 7684 8786 -46 205 -813 A O ATOM 281 N THR A 40 16.880 149.429 272.376 1.00 33.25 A N ANISOU 281 N THR A 40 3466 3807 5363 -162 45 -706 A N ATOM 282 CA THR A 40 18.193 149.328 271.742 1.00 29.37 A C ANISOU 282 CA THR A 40 3014 3275 4871 -222 -23 -705 A C ATOM 283 C THR A 40 18.079 148.621 270.396 1.00 25.72 A C ANISOU 283 C THR A 40 2537 2823 4414 -267 -66 -569 A C ATOM 284 O THR A 40 17.100 147.914 270.142 1.00 26.58 A O ANISOU 284 O THR A 40 2621 2983 4496 -274 -58 -490 A O ATOM 285 CB THR A 40 19.238 148.623 272.642 1.00 35.90 A C ANISOU 285 CB THR A 40 3900 4176 5565 -237 -46 -785 A C ATOM 286 CG2 THR A 40 19.340 149.317 273.991 1.00 39.97 A C ANISOU 286 CG2 THR A 40 4434 4696 6056 -189 -13 -932 A C ATOM 287 OG1 THR A 40 18.863 147.254 272.846 1.00 42.19 A O ANISOU 287 OG1 THR A 40 4726 5063 6241 -246 -42 -720 A O ATOM 288 N LEU A 41 19.091 148.802 269.551 1.00 25.39 A N ANISOU 288 N LEU A 41 2507 2742 4397 -303 -113 -546 A N ATOM 289 CA LEU A 41 19.174 148.132 268.260 1.00 26.59 A C ANISOU 289 CA LEU A 41 2661 2913 4530 -332 -159 -433 A C ATOM 290 C LEU A 41 19.903 146.794 268.437 1.00 25.10 A C ANISOU 290 C LEU A 41 2538 2803 4196 -347 -195 -439 A C ATOM 291 O LEU A 41 20.385 146.490 269.529 1.00 23.36 A O ANISOU 291 O LEU A 41 2352 2622 3900 -334 -185 -521 A O ATOM 292 CB LEU A 41 19.919 149.023 267.258 1.00 25.95 A C ANISOU 292 CB LEU A 41 2558 2766 4536 -349 -178 -394 A C ATOM 293 CG LEU A 41 19.443 150.484 267.146 1.00 29.68 A C ANISOU 293 CG LEU A 41 2996 3124 5158 -327 -144 -393 A C ATOM 294 CD1 LEU A 41 20.279 151.282 266.147 1.00 27.01 A C ANISOU 294 CD1 LEU A 41 2649 2716 4898 -364 -160 -333 A C ATOM 295 CD2 LEU A 41 17.968 150.568 266.782 1.00 25.00 A C ANISOU 295 CD2 LEU A 41 2360 2530 4610 -275 -125 -320 A C ATOM 296 N GLY A 42 19.953 145.985 267.382 1.00 23.93 A N ANISOU 296 N GLY A 42 2416 2675 4001 -360 -240 -356 A N ATOM 297 CA GLY A 42 20.705 144.738 267.413 1.00 22.14 A C ANISOU 297 CA GLY A 42 2272 2502 3638 -352 -278 -360 A C ATOM 298 C GLY A 42 19.839 143.503 267.544 1.00 20.44 A C ANISOU 298 C GLY A 42 2124 2297 3345 -372 -292 -321 A C ATOM 299 O GLY A 42 20.299 142.386 267.313 1.00 19.98 A O ANISOU 299 O GLY A 42 2159 2252 3178 -361 -333 -306 A O ATOM 300 N GLY A 43 18.580 143.707 267.918 1.00 21.07 A N ANISOU 300 N GLY A 43 2155 2371 3481 -402 -256 -301 A N ATOM 301 CA GLY A 43 17.621 142.621 267.997 1.00 19.24 A C ANISOU 301 CA GLY A 43 1963 2151 3195 -455 -266 -249 A C ATOM 302 C GLY A 43 18.018 141.458 268.891 1.00 14.65 A C ANISOU 302 C GLY A 43 1499 1583 2486 -457 -266 -269 A C ATOM 303 O GLY A 43 18.774 141.606 269.873 1.00 16.50 A O ANISOU 303 O GLY A 43 1757 1843 2669 -406 -238 -336 A O ATOM 304 N VAL A 44 17.518 140.283 268.522 1.00 16.85 A N ANISOU 304 N VAL A 44 1858 1837 2708 -517 -306 -210 A N ATOM 305 CA VAL A 44 17.723 139.086 269.318 1.00 16.90 A C ANISOU 305 CA VAL A 44 1997 1828 2595 -526 -305 -205 A C ATOM 306 C VAL A 44 19.201 138.720 269.363 1.00 19.59 A C ANISOU 306 C VAL A 44 2440 2165 2837 -428 -339 -253 A C ATOM 307 O VAL A 44 19.745 138.473 270.439 1.00 21.36 A O ANISOU 307 O VAL A 44 2717 2420 2981 -376 -311 -288 A O ATOM 308 CB VAL A 44 16.905 137.905 268.777 1.00 18.83 A C ANISOU 308 CB VAL A 44 2327 2017 2811 -629 -354 -131 A C ATOM 309 CG1 VAL A 44 17.417 136.588 269.350 1.00 15.82 A C ANISOU 309 CG1 VAL A 44 2134 1578 2299 -619 -371 -121 A C ATOM 310 CG2 VAL A 44 15.420 138.095 269.091 1.00 16.12 A C ANISOU 310 CG2 VAL A 44 1868 1715 2542 -736 -309 -76 A C ATOM 311 N ACYS A 45 19.858 138.730 268.206 0.45 19.31 A N ANISOU 311 N ACYS A 45 2422 2114 2801 -390 -396 -254 A N ATOM 312 N BCYS A 45 19.830 138.698 268.187 0.55 19.36 A N ANISOU 312 N BCYS A 45 2431 2118 2807 -393 -397 -252 A N ATOM 313 CA ACYS A 45 21.261 138.330 268.125 0.45 19.10 A C ANISOU 313 CA ACYS A 45 2475 2110 2674 -285 -427 -292 A C ATOM 314 CA BCYS A 45 21.252 138.390 268.035 0.55 18.28 A C ANISOU 314 CA BCYS A 45 2364 2006 2577 -286 -428 -291 A C ATOM 315 C ACYS A 45 22.144 139.089 269.107 0.45 22.23 A C ANISOU 315 C ACYS A 45 2799 2583 3062 -223 -388 -362 A C ATOM 316 C BCYS A 45 22.133 139.090 269.063 0.55 21.81 A C ANISOU 316 C BCYS A 45 2746 2529 3011 -224 -389 -360 A C ATOM 317 O ACYS A 45 22.909 138.484 269.860 0.45 22.23 A O ANISOU 317 O ACYS A 45 2878 2618 2950 -149 -394 -391 A O ATOM 318 O BCYS A 45 22.881 138.445 269.801 0.55 22.57 A O ANISOU 318 O BCYS A 45 2925 2657 2994 -151 -396 -387 A O ATOM 319 CB ACYS A 45 21.796 138.510 266.705 0.45 18.38 A C ANISOU 319 CB ACYS A 45 2367 2024 2592 -249 -475 -279 A C ATOM 320 CB BCYS A 45 21.707 138.769 266.625 0.55 17.95 A C ANISOU 320 CB BCYS A 45 2281 1974 2565 -259 -469 -278 A C ATOM 321 SG ACYS A 45 23.439 137.801 266.451 0.45 23.82 A S ANISOU 321 SG ACYS A 45 3152 2764 3136 -101 -512 -312 A S ATOM 322 SG BCYS A 45 23.491 138.999 266.416 0.55 27.61 A S ANISOU 322 SG BCYS A 45 3486 3288 3717 -133 -479 -323 A S ATOM 323 N LEU A 46 22.032 140.413 269.113 1.00 21.78 A N ANISOU 323 N LEU A 46 2603 2550 3121 -250 -354 -391 A N ATOM 324 CA LEU A 46 22.850 141.203 270.016 1.00 22.07 A C ANISOU 324 CA LEU A 46 2575 2650 3160 -212 -330 -474 A C ATOM 325 C LEU A 46 22.369 141.154 271.467 1.00 18.90 A C ANISOU 325 C LEU A 46 2191 2270 2719 -212 -284 -514 A C ATOM 326 O LEU A 46 23.183 141.009 272.381 1.00 17.02 A O ANISOU 326 O LEU A 46 1979 2100 2389 -153 -288 -574 A O ATOM 327 CB LEU A 46 22.936 142.654 269.533 1.00 25.61 A C ANISOU 327 CB LEU A 46 2894 3088 3749 -247 -314 -496 A C ATOM 328 CG LEU A 46 23.828 143.571 270.371 1.00 24.44 A C ANISOU 328 CG LEU A 46 2679 2989 3618 -234 -303 -594 A C ATOM 329 CD1 LEU A 46 25.166 142.893 270.653 1.00 24.17 A C ANISOU 329 CD1 LEU A 46 2679 3053 3453 -166 -344 -627 A C ATOM 330 CD2 LEU A 46 24.047 144.897 269.657 1.00 23.10 A C ANISOU 330 CD2 LEU A 46 2409 2778 3590 -281 -297 -596 A C ATOM 331 N ASN A 47 21.064 141.269 271.691 1.00 17.45 A N ANISOU 331 N ASN A 47 1985 2053 2593 -271 -239 -479 A N ATOM 332 CA ASN A 47 20.592 141.475 273.065 1.00 19.06 A C ANISOU 332 CA ASN A 47 2178 2300 2764 -262 -178 -522 A C ATOM 333 C ASN A 47 20.355 140.209 273.878 1.00 20.00 A C ANISOU 333 C ASN A 47 2414 2438 2746 -254 -163 -476 A C ATOM 334 O ASN A 47 20.648 140.168 275.077 1.00 20.52 A O ANISOU 334 O ASN A 47 2507 2569 2720 -202 -134 -523 A O ATOM 335 CB ASN A 47 19.337 142.354 273.075 1.00 18.96 A C ANISOU 335 CB ASN A 47 2063 2271 2871 -305 -121 -513 A C ATOM 336 CG ASN A 47 19.602 143.757 272.542 1.00 21.25 A C ANISOU 336 CG ASN A 47 2256 2524 3292 -296 -125 -567 A C ATOM 337 ND2 ASN A 47 19.305 143.976 271.265 1.00 19.07 A N ANISOU 337 ND2 ASN A 47 1942 2198 3108 -330 -153 -500 A N ATOM 338 OD1 ASN A 47 20.091 144.621 273.264 1.00 20.28 A O ANISOU 338 OD1 ASN A 47 2105 2416 3184 -261 -109 -666 A O ATOM 339 N VAL A 48 19.807 139.186 273.228 1.00 16.38 A N ANISOU 339 N VAL A 48 2032 1918 2272 -310 -186 -381 A N ATOM 340 CA VAL A 48 19.430 137.952 273.907 1.00 19.01 A C ANISOU 340 CA VAL A 48 2493 2237 2495 -331 -169 -313 A C ATOM 341 C VAL A 48 19.761 136.709 273.075 1.00 22.32 A C ANISOU 341 C VAL A 48 3063 2563 2855 -338 -241 -253 A C ATOM 342 O VAL A 48 19.103 135.676 273.218 1.00 26.04 A O ANISOU 342 O VAL A 48 3642 2971 3282 -408 -237 -173 A O ATOM 343 CB VAL A 48 17.911 137.938 274.220 1.00 22.35 A C ANISOU 343 CB VAL A 48 2854 2667 2971 -438 -102 -243 A C ATOM 344 CG1 VAL A 48 17.545 139.074 275.171 1.00 18.88 A C ANISOU 344 CG1 VAL A 48 2288 2323 2564 -400 -21 -308 A C ATOM 345 CG2 VAL A 48 17.101 138.058 272.935 1.00 16.55 A C ANISOU 345 CG2 VAL A 48 2051 1879 2356 -532 -137 -194 A C ATOM 346 N GLY A 49 20.784 136.798 272.221 1.00 18.60 A N ANISOU 346 N GLY A 49 2605 2083 2378 -266 -303 -293 A N ATOM 347 CA GLY A 49 21.106 135.697 271.318 1.00 20.98 A C ANISOU 347 CA GLY A 49 3054 2298 2619 -248 -373 -253 A C ATOM 348 C GLY A 49 22.586 135.380 271.143 1.00 20.98 A C ANISOU 348 C GLY A 49 3123 2333 2516 -97 -420 -298 A C ATOM 349 O GLY A 49 23.260 135.049 272.118 1.00 22.12 A O ANISOU 349 O GLY A 49 3325 2527 2554 -6 -410 -317 A O ATOM 350 N ACYS A 50 23.077 135.515 269.913 0.01 18.65 A N ANISOU 350 N ACYS A 50 1692 2610 2784 -4 -155 -414 A N ATOM 351 N BCYS A 50 23.086 135.477 269.906 0.99 15.76 A N ANISOU 351 N BCYS A 50 1326 2246 2416 -3 -153 -416 A N ATOM 352 CA ACYS A 50 24.451 135.172 269.549 0.01 19.26 A C ANISOU 352 CA ACYS A 50 1798 2769 2751 28 -110 -280 A C ATOM 353 CA BCYS A 50 24.475 135.124 269.570 0.99 20.96 A C ANISOU 353 CA BCYS A 50 2015 2983 2965 26 -107 -282 A C ATOM 354 C ACYS A 50 25.509 135.697 270.513 0.01 20.16 A C ANISOU 354 C ACYS A 50 1929 2813 2917 -58 -61 -145 A C ATOM 355 C BCYS A 50 25.537 135.694 270.510 0.99 21.33 A C ANISOU 355 C BCYS A 50 2078 2962 3064 -57 -60 -142 A C ATOM 356 O ACYS A 50 26.292 134.931 271.073 0.01 20.87 A O ANISOU 356 O ACYS A 50 2050 2893 2989 -93 -5 -140 A O ATOM 357 O BCYS A 50 26.369 134.957 271.044 0.99 21.92 A O ANISOU 357 O BCYS A 50 2183 3029 3118 -91 -4 -130 A O ATOM 358 CB ACYS A 50 24.757 135.711 268.152 0.01 19.52 A C ANISOU 358 CB ACYS A 50 1813 2956 2649 164 -148 -154 A C ATOM 359 CB BCYS A 50 24.834 135.571 268.142 0.99 18.80 A C ANISOU 359 CB BCYS A 50 1724 2871 2548 166 -143 -160 A C ATOM 360 SG ACYS A 50 23.311 135.871 267.089 0.01 33.83 A S ANISOU 360 SG ACYS A 50 3590 4854 4411 295 -262 -294 A S ATOM 361 SG BCYS A 50 23.486 135.600 266.972 0.99 33.50 A S ANISOU 361 SG BCYS A 50 3552 4840 4338 312 -254 -304 A S ATOM 362 N ILE A 51 25.519 137.013 270.697 1.00 16.68 A N ANISOU 362 N ILE A 51 1456 2315 2568 -80 -101 -51 A N ATOM 363 CA ILE A 51 26.579 137.676 271.449 1.00 15.34 A C ANISOU 363 CA ILE A 51 1266 2071 2491 -137 -93 55 A C ATOM 364 C ILE A 51 26.716 137.281 272.931 1.00 13.46 A C ANISOU 364 C ILE A 51 1058 1769 2287 -205 -72 -60 A C ATOM 365 O ILE A 51 27.801 136.866 273.357 1.00 17.22 A O ANISOU 365 O ILE A 51 1552 2253 2739 -218 -39 -14 A O ATOM 366 CB ILE A 51 26.535 139.212 271.249 1.00 19.74 A C ANISOU 366 CB ILE A 51 1745 2546 3209 -137 -162 171 A C ATOM 367 CG1 ILE A 51 26.671 139.541 269.764 1.00 19.72 A C ANISOU 367 CG1 ILE A 51 1712 2644 3137 -41 -151 367 A C ATOM 368 CG2 ILE A 51 27.649 139.872 272.032 1.00 18.34 A C ANISOU 368 CG2 ILE A 51 1512 2263 3193 -190 -180 239 A C ATOM 369 CD1 ILE A 51 27.930 138.935 269.118 1.00 15.60 A C ANISOU 369 CD1 ILE A 51 1193 2243 2491 7 -64 520 A C ATOM 370 N PRO A 52 25.640 137.429 273.728 1.00 14.60 A N ANISOU 370 N PRO A 52 1202 1870 2476 -229 -89 -202 A N ATOM 371 CA PRO A 52 25.786 137.025 275.134 1.00 20.30 A C ANISOU 371 CA PRO A 52 1952 2585 3178 -253 -51 -283 A C ATOM 372 C PRO A 52 26.095 135.538 275.295 1.00 18.44 A C ANISOU 372 C PRO A 52 1774 2394 2838 -255 46 -270 A C ATOM 373 O PRO A 52 26.908 135.143 276.160 1.00 23.39 A O ANISOU 373 O PRO A 52 2432 3038 3418 -252 76 -246 A O ATOM 374 CB PRO A 52 24.409 137.339 275.744 1.00 22.71 A C ANISOU 374 CB PRO A 52 2232 2872 3525 -257 -56 -422 A C ATOM 375 CG PRO A 52 23.486 137.511 274.594 1.00 20.91 A C ANISOU 375 CG PRO A 52 1976 2632 3336 -247 -89 -435 A C ATOM 376 CD PRO A 52 24.316 138.023 273.464 1.00 16.52 A C ANISOU 376 CD PRO A 52 1410 2085 2783 -219 -139 -287 A C ATOM 377 N SER A 53 25.474 134.716 274.453 1.00 15.22 A N ANISOU 377 N SER A 53 1369 2000 2416 -247 77 -298 A N ATOM 378 CA SER A 53 25.719 133.287 274.549 1.00 20.82 A C ANISOU 378 CA SER A 53 2105 2713 3094 -248 153 -299 A C ATOM 379 C SER A 53 27.187 133.002 274.247 1.00 21.27 A C ANISOU 379 C SER A 53 2190 2808 3083 -227 152 -200 A C ATOM 380 O SER A 53 27.822 132.242 274.966 1.00 19.07 A O ANISOU 380 O SER A 53 1942 2521 2781 -233 202 -167 A O ATOM 381 CB SER A 53 24.751 132.466 273.673 1.00 20.23 A C ANISOU 381 CB SER A 53 1992 2621 3075 -230 154 -399 A C ATOM 382 OG SER A 53 24.919 132.726 272.294 1.00 34.09 A O ANISOU 382 OG SER A 53 3734 4447 4774 -164 79 -405 A O ATOM 383 N LYS A 54 27.748 133.665 273.240 1.00 18.69 A N ANISOU 383 N LYS A 54 1842 2530 2729 -194 103 -130 A N ATOM 384 CA LYS A 54 29.163 133.469 272.924 1.00 19.75 A C ANISOU 384 CA LYS A 54 1980 2709 2814 -171 117 -25 A C ATOM 385 C LYS A 54 30.098 134.010 274.028 1.00 23.66 A C ANISOU 385 C LYS A 54 2476 3159 3357 -206 104 27 A C ATOM 386 O LYS A 54 31.166 133.438 274.294 1.00 21.22 A O ANISOU 386 O LYS A 54 2179 2862 3020 -198 126 68 A O ATOM 387 CB LYS A 54 29.501 134.031 271.534 1.00 23.41 A C ANISOU 387 CB LYS A 54 2401 3263 3230 -106 99 76 A C ATOM 388 CG LYS A 54 29.562 132.971 270.402 1.00 26.96 A C ANISOU 388 CG LYS A 54 2852 3831 3561 -13 116 28 A C ATOM 389 CD LYS A 54 28.203 132.696 269.733 1.00 27.61 A C ANISOU 389 CD LYS A 54 2923 3943 3623 41 67 -119 A C ATOM 390 CE LYS A 54 27.432 131.578 270.419 1.00 27.47 A C ANISOU 390 CE LYS A 54 2914 3819 3704 -8 75 -288 A C ATOM 391 NZ LYS A 54 26.062 131.373 269.849 1.00 28.07 A N1+ ANISOU 391 NZ LYS A 54 2949 3890 3827 34 15 -454 A N1+ ATOM 392 N ALA A 55 29.700 135.093 274.690 1.00 19.98 A N ANISOU 392 N ALA A 55 1982 2639 2971 -229 50 -5 A N ATOM 393 CA ALA A 55 30.487 135.576 275.832 1.00 18.98 A C ANISOU 393 CA ALA A 55 1839 2477 2895 -233 3 -24 A C ATOM 394 C ALA A 55 30.552 134.539 276.973 1.00 18.42 A C ANISOU 394 C ALA A 55 1837 2444 2718 -211 51 -79 A C ATOM 395 O ALA A 55 31.650 134.164 277.485 1.00 18.14 A O ANISOU 395 O ALA A 55 1814 2426 2654 -186 42 -52 A O ATOM 396 CB ALA A 55 29.918 136.896 276.344 1.00 16.97 A C ANISOU 396 CB ALA A 55 1526 2161 2762 -238 -86 -102 A C ATOM 397 N LEU A 56 29.368 134.065 277.362 1.00 12.65 A N ANISOU 397 N LEU A 56 1137 1727 1940 -213 108 -137 A N ATOM 398 CA LEU A 56 29.288 133.070 278.431 1.00 13.79 A C ANISOU 398 CA LEU A 56 1333 1912 1995 -182 186 -132 A C ATOM 399 C LEU A 56 30.005 131.766 278.051 1.00 21.17 A C ANISOU 399 C LEU A 56 2301 2836 2908 -182 244 -49 A C ATOM 400 O LEU A 56 30.650 131.115 278.892 1.00 27.98 A O ANISOU 400 O LEU A 56 3199 3725 3705 -140 272 0 A O ATOM 401 CB LEU A 56 27.825 132.825 278.825 1.00 11.95 A C ANISOU 401 CB LEU A 56 1094 1683 1763 -189 264 -175 A C ATOM 402 CG LEU A 56 27.117 134.076 279.368 1.00 18.89 A C ANISOU 402 CG LEU A 56 1934 2588 2654 -168 205 -282 A C ATOM 403 CD1 LEU A 56 25.672 133.790 279.766 1.00 19.28 A C ANISOU 403 CD1 LEU A 56 1962 2654 2710 -171 302 -319 A C ATOM 404 CD2 LEU A 56 27.880 134.660 280.548 1.00 18.67 A C ANISOU 404 CD2 LEU A 56 1911 2638 2547 -86 136 -333 A C ATOM 405 N LEU A 57 29.908 131.401 276.776 1.00 18.20 A N ANISOU 405 N LEU A 57 1905 2431 2578 -207 248 -45 A N ATOM 406 CA LEU A 57 30.557 130.194 276.274 1.00 18.51 A C ANISOU 406 CA LEU A 57 1955 2458 2619 -193 282 -10 A C ATOM 407 C LEU A 57 32.074 130.329 276.301 1.00 19.60 A C ANISOU 407 C LEU A 57 2097 2630 2720 -168 243 49 A C ATOM 408 O LEU A 57 32.788 129.353 276.591 1.00 14.89 A O ANISOU 408 O LEU A 57 1523 2024 2112 -143 268 85 A O ATOM 409 CB LEU A 57 30.088 129.868 274.856 1.00 13.12 A C ANISOU 409 CB LEU A 57 1234 1778 1973 -186 269 -69 A C ATOM 410 CG LEU A 57 28.705 129.230 274.726 1.00 19.18 A C ANISOU 410 CG LEU A 57 1971 2480 2836 -202 300 -158 A C ATOM 411 CD1 LEU A 57 28.212 129.298 273.282 1.00 19.59 A C ANISOU 411 CD1 LEU A 57 1977 2573 2895 -161 238 -261 A C ATOM 412 CD2 LEU A 57 28.770 127.785 275.201 1.00 12.19 A C ANISOU 412 CD2 LEU A 57 1078 1509 2046 -204 364 -141 A C ATOM 413 N HIS A 58 32.573 131.528 276.006 1.00 16.92 A N ANISOU 413 N HIS A 58 1719 2310 2399 -174 181 67 A N ATOM 414 CA HIS A 58 34.008 131.756 276.117 1.00 19.66 A C ANISOU 414 CA HIS A 58 2038 2668 2764 -156 144 121 A C ATOM 415 C HIS A 58 34.437 131.593 277.579 1.00 21.81 A C ANISOU 415 C HIS A 58 2346 2940 3002 -122 113 93 A C ATOM 416 O HIS A 58 35.462 130.938 277.888 1.00 20.32 A O ANISOU 416 O HIS A 58 2169 2762 2792 -87 108 122 A O ATOM 417 CB HIS A 58 34.405 133.138 275.603 1.00 22.49 A C ANISOU 417 CB HIS A 58 2312 3010 3224 -174 89 167 A C ATOM 418 CG HIS A 58 35.839 133.471 275.852 1.00 26.34 A C ANISOU 418 CG HIS A 58 2734 3476 3796 -164 45 211 A C ATOM 419 CD2 HIS A 58 36.973 133.038 275.248 1.00 28.13 A C ANISOU 419 CD2 HIS A 58 2921 3733 4035 -147 78 290 A C ATOM 420 ND1 HIS A 58 36.243 134.339 276.847 1.00 30.71 A N ANISOU 420 ND1 HIS A 58 3237 3972 4459 -159 -55 148 A N ATOM 421 CE1 HIS A 58 37.559 134.429 276.839 1.00 32.68 A C ANISOU 421 CE1 HIS A 58 3411 4197 4808 -148 -87 186 A C ATOM 422 NE2 HIS A 58 38.027 133.652 275.880 1.00 29.96 A N ANISOU 422 NE2 HIS A 58 3074 3908 4403 -146 4 287 A N ATOM 423 N VAL A 59 33.652 132.176 278.484 1.00 21.54 A N ANISOU 423 N VAL A 59 2325 2914 2946 -110 89 28 A N ATOM 424 CA VAL A 59 33.946 131.949 279.909 1.00 23.07 A C ANISOU 424 CA VAL A 59 2557 3165 3045 -31 65 -3 A C ATOM 425 C VAL A 59 34.033 130.455 280.283 1.00 22.49 A C ANISOU 425 C VAL A 59 2552 3111 2884 4 159 87 A C ATOM 426 O VAL A 59 35.019 129.992 280.912 1.00 21.57 A O ANISOU 426 O VAL A 59 2455 3027 2712 72 129 116 A O ATOM 427 CB VAL A 59 32.913 132.669 280.807 1.00 24.15 A C ANISOU 427 CB VAL A 59 2694 3352 3130 7 47 -94 A C ATOM 428 CG1 VAL A 59 32.954 132.136 282.221 1.00 21.60 A C ANISOU 428 CG1 VAL A 59 2425 3146 2636 126 70 -92 A C ATOM 429 CG2 VAL A 59 33.149 134.177 280.772 1.00 22.67 A C ANISOU 429 CG2 VAL A 59 2418 3125 3069 4 -92 -207 A C ATOM 430 N ALA A 60 33.025 129.699 279.853 1.00 20.68 A N ANISOU 430 N ALA A 60 2337 2840 2679 -40 262 128 A N ATOM 431 CA ALA A 60 32.984 128.254 280.103 1.00 19.46 A C ANISOU 431 CA ALA A 60 2214 2651 2528 -20 356 227 A C ATOM 432 C ALA A 60 34.230 127.522 279.567 1.00 18.40 A C ANISOU 432 C ALA A 60 2078 2482 2433 -10 324 256 A C ATOM 433 O ALA A 60 34.852 126.679 280.264 1.00 21.98 A O ANISOU 433 O ALA A 60 2561 2936 2853 51 342 338 A O ATOM 434 CB ALA A 60 31.719 127.675 279.482 1.00 17.21 A C ANISOU 434 CB ALA A 60 1900 2284 2355 -83 442 225 A C ATOM 435 N LYS A 61 34.593 127.861 278.330 1.00 15.95 A N ANISOU 435 N LYS A 61 1723 2156 2180 -53 282 200 A N ATOM 436 CA LYS A 61 35.763 127.277 277.679 1.00 17.87 A C ANISOU 436 CA LYS A 61 1943 2392 2454 -33 258 210 A C ATOM 437 C LYS A 61 37.037 127.535 278.469 1.00 19.89 A C ANISOU 437 C LYS A 61 2205 2684 2668 18 193 235 A C ATOM 438 O LYS A 61 37.839 126.609 278.712 1.00 16.67 A O ANISOU 438 O LYS A 61 1809 2260 2266 65 191 273 A O ATOM 439 CB LYS A 61 35.918 127.832 276.257 1.00 17.99 A C ANISOU 439 CB LYS A 61 1900 2442 2495 -58 240 169 A C ATOM 440 CG LYS A 61 37.130 127.285 275.506 1.00 20.03 A C ANISOU 440 CG LYS A 61 2117 2730 2765 -19 232 175 A C ATOM 441 CD LYS A 61 37.173 127.781 274.054 1.00 19.53 A C ANISOU 441 CD LYS A 61 1990 2752 2680 -6 243 164 A C ATOM 442 CE LYS A 61 38.400 127.241 273.335 1.00 18.59 A C ANISOU 442 CE LYS A 61 1815 2699 2551 55 253 172 A C ATOM 443 NZ LYS A 61 38.549 127.799 271.969 1.00 19.29 A N1+ ANISOU 443 NZ LYS A 61 1832 2921 2576 101 287 203 A N1+ ATOM 444 N VAL A 62 37.238 128.789 278.866 1.00 16.86 A N ANISOU 444 N VAL A 62 1796 2338 2274 19 122 195 A N ATOM 445 CA VAL A 62 38.428 129.089 279.660 1.00 14.58 A C ANISOU 445 CA VAL A 62 1487 2076 1978 83 29 174 A C ATOM 446 C VAL A 62 38.429 128.317 280.989 1.00 15.48 A C ANISOU 446 C VAL A 62 1677 2238 1965 183 30 207 A C ATOM 447 O VAL A 62 39.464 127.771 281.386 1.00 18.71 A O ANISOU 447 O VAL A 62 2091 2659 2358 251 -15 227 A O ATOM 448 CB VAL A 62 38.641 130.597 279.871 1.00 21.64 A C ANISOU 448 CB VAL A 62 2304 2968 2948 76 -75 91 A C ATOM 449 CG1 VAL A 62 39.815 130.843 280.816 1.00 19.80 A C ANISOU 449 CG1 VAL A 62 2033 2758 2732 164 -202 20 A C ATOM 450 CG2 VAL A 62 38.886 131.274 278.535 1.00 18.20 A C ANISOU 450 CG2 VAL A 62 1776 2485 2655 -5 -58 130 A C ATOM 451 N ILE A 63 37.281 128.257 281.670 1.00 18.16 A N ANISOU 451 N ILE A 63 2070 2618 2213 206 92 232 A N ATOM 452 CA ILE A 63 37.213 127.477 282.921 1.00 20.93 A C ANISOU 452 CA ILE A 63 2489 3044 2420 325 130 323 A C ATOM 453 C ILE A 63 37.659 126.016 282.732 1.00 25.08 A C ANISOU 453 C ILE A 63 3038 3495 2998 334 196 455 A C ATOM 454 O ILE A 63 38.564 125.491 283.449 1.00 26.61 A O ANISOU 454 O ILE A 63 3258 3732 3122 442 150 510 A O ATOM 455 CB ILE A 63 35.786 127.475 283.518 1.00 19.48 A C ANISOU 455 CB ILE A 63 2337 2914 2152 340 240 377 A C ATOM 456 CG1 ILE A 63 35.421 128.864 284.054 1.00 19.32 A C ANISOU 456 CG1 ILE A 63 2294 2997 2049 384 153 227 A C ATOM 457 CG2 ILE A 63 35.669 126.446 284.642 1.00 20.13 A C ANISOU 457 CG2 ILE A 63 2476 3071 2102 465 334 555 A C ATOM 458 CD1 ILE A 63 33.961 128.990 284.501 1.00 19.89 A C ANISOU 458 CD1 ILE A 63 2377 3129 2049 392 267 257 A C ATOM 459 N GLU A 64 37.056 125.366 281.741 1.00 23.93 A N ANISOU 459 N GLU A 64 2869 3231 2992 234 281 485 A N ATOM 460 CA GLU A 64 37.419 123.974 281.490 1.00 28.33 A C ANISOU 460 CA GLU A 64 3422 3686 3658 242 325 576 A C ATOM 461 C GLU A 64 38.883 123.788 281.068 1.00 27.64 A C ANISOU 461 C GLU A 64 3308 3590 3602 270 230 523 A C ATOM 462 O GLU A 64 39.521 122.810 281.458 1.00 28.39 A O ANISOU 462 O GLU A 64 3416 3647 3726 336 226 606 A O ATOM 463 CB GLU A 64 36.429 123.290 280.544 1.00 32.74 A C ANISOU 463 CB GLU A 64 3933 4111 4395 152 406 567 A C ATOM 464 CG GLU A 64 35.019 123.257 281.135 1.00 44.44 A C ANISOU 464 CG GLU A 64 5419 5579 5886 134 519 652 A C ATOM 465 CD GLU A 64 34.905 122.327 282.348 1.00 54.80 A C ANISOU 465 CD GLU A 64 6757 6879 7188 220 618 875 A C ATOM 466 OE1 GLU A 64 35.813 121.493 282.567 1.00 56.21 A O ANISOU 466 OE1 GLU A 64 6943 7011 7401 281 594 960 A O ATOM 467 OE2 GLU A 64 33.914 122.448 283.099 1.00 58.64 A O1- ANISOU 467 OE2 GLU A 64 7246 7411 7622 241 727 984 A O1- ATOM 468 N GLU A 65 39.422 124.714 280.280 1.00 21.66 A N ANISOU 468 N GLU A 65 2502 2867 2859 224 162 404 A N ATOM 469 CA GLU A 65 40.837 124.605 279.908 1.00 22.46 A C ANISOU 469 CA GLU A 65 2555 2973 3005 252 89 364 A C ATOM 470 C GLU A 65 41.762 124.743 281.121 1.00 22.11 A C ANISOU 470 C GLU A 65 2533 2988 2879 360 -5 377 A C ATOM 471 O GLU A 65 42.736 123.976 281.294 1.00 28.85 A O ANISOU 471 O GLU A 65 3380 3822 3761 425 -46 401 A O ATOM 472 CB GLU A 65 41.194 125.645 278.838 1.00 23.38 A C ANISOU 472 CB GLU A 65 2590 3120 3173 188 64 284 A C ATOM 473 CG GLU A 65 40.632 125.295 277.469 1.00 36.89 A C ANISOU 473 CG GLU A 65 4268 4814 4934 135 136 259 A C ATOM 474 CD GLU A 65 41.103 126.230 276.380 1.00 49.65 A C ANISOU 474 CD GLU A 65 5798 6494 6574 106 136 237 A C ATOM 475 OE1 GLU A 65 41.394 125.735 275.269 1.00 51.88 A O ANISOU 475 OE1 GLU A 65 6030 6816 6868 127 173 213 A O ATOM 476 OE2 GLU A 65 41.171 127.456 276.631 1.00 55.05 A O1- ANISOU 476 OE2 GLU A 65 6450 7193 7273 76 101 249 A O1- ATOM 477 N ALA A 66 41.441 125.725 281.962 1.00 21.32 A N ANISOU 477 N ALA A 66 2452 2970 2678 397 -56 336 A N ATOM 478 CA ALA A 66 42.189 125.959 283.188 1.00 26.15 A C ANISOU 478 CA ALA A 66 3079 3675 3182 538 -174 302 A C ATOM 479 C ALA A 66 42.226 124.683 283.997 1.00 27.92 A C ANISOU 479 C ALA A 66 3383 3919 3306 651 -129 453 A C ATOM 480 O ALA A 66 43.298 124.244 284.422 1.00 30.91 A O ANISOU 480 O ALA A 66 3757 4317 3670 751 -215 456 A O ATOM 481 CB ALA A 66 41.557 127.079 284.005 1.00 25.51 A C ANISOU 481 CB ALA A 66 3007 3697 2990 590 -230 212 A C ATOM 482 N LYS A 67 41.058 124.070 284.187 1.00 27.02 A N ANISOU 482 N LYS A 67 3326 3788 3152 636 11 593 A N ATOM 483 CA LYS A 67 41.018 122.792 284.907 1.00 29.13 A C ANISOU 483 CA LYS A 67 3647 4043 3379 736 84 798 A C ATOM 484 C LYS A 67 41.824 121.683 284.209 1.00 28.08 A C ANISOU 484 C LYS A 67 3479 3759 3432 705 76 835 A C ATOM 485 O LYS A 67 42.510 120.894 284.860 1.00 29.16 A O ANISOU 485 O LYS A 67 3640 3899 3540 825 45 945 A O ATOM 486 CB LYS A 67 39.571 122.371 285.148 1.00 35.35 A C ANISOU 486 CB LYS A 67 4461 4806 4165 706 256 960 A C ATOM 487 CG LYS A 67 38.884 123.292 286.140 1.00 48.95 A C ANISOU 487 CG LYS A 67 6222 6722 5654 798 267 948 A C ATOM 488 CD LYS A 67 37.421 122.948 286.366 1.00 58.07 A C ANISOU 488 CD LYS A 67 7381 7862 6821 765 456 1113 A C ATOM 489 CE LYS A 67 36.809 123.927 287.366 1.00 61.47 A C ANISOU 489 CE LYS A 67 7841 8525 6991 884 460 1070 A C ATOM 490 NZ LYS A 67 35.328 123.807 287.472 1.00 64.08 A N1+ ANISOU 490 NZ LYS A 67 8151 8846 7349 834 647 1195 A N1+ ATOM 491 N ALA A 68 41.747 121.628 282.884 1.00 25.79 A N ANISOU 491 N ALA A 68 3126 3354 3320 567 96 734 A N ATOM 492 CA ALA A 68 42.451 120.594 282.125 1.00 26.99 A C ANISOU 492 CA ALA A 68 3226 3379 3650 552 83 723 A C ATOM 493 C ALA A 68 43.974 120.721 282.217 1.00 27.63 A C ANISOU 493 C ALA A 68 3278 3509 3713 625 -45 644 A C ATOM 494 O ALA A 68 44.700 119.750 281.981 1.00 23.27 A O ANISOU 494 O ALA A 68 2693 2872 3277 663 -71 660 A O ATOM 495 CB ALA A 68 42.011 120.616 280.670 1.00 25.01 A C ANISOU 495 CB ALA A 68 2907 3054 3542 429 121 598 A C ATOM 496 N LEU A 69 44.460 121.916 282.537 1.00 23.36 A N ANISOU 496 N LEU A 69 2725 3085 3065 647 -135 542 A N ATOM 497 CA LEU A 69 45.909 122.099 282.704 1.00 26.17 A C ANISOU 497 CA LEU A 69 3026 3476 3443 720 -267 454 A C ATOM 498 C LEU A 69 46.528 121.305 283.876 1.00 27.76 A C ANISOU 498 C LEU A 69 3282 3709 3558 891 -341 550 A C ATOM 499 O LEU A 69 47.747 121.069 283.905 1.00 23.20 A O ANISOU 499 O LEU A 69 2652 3124 3041 957 -446 488 A O ATOM 500 CB LEU A 69 46.230 123.585 282.882 1.00 24.70 A C ANISOU 500 CB LEU A 69 2784 3376 3226 711 -365 313 A C ATOM 501 CG LEU A 69 46.462 124.405 281.609 1.00 31.08 A C ANISOU 501 CG LEU A 69 3478 4146 4187 576 -340 222 A C ATOM 502 CD1 LEU A 69 47.229 125.692 281.912 1.00 29.22 A C ANISOU 502 CD1 LEU A 69 3137 3939 4025 591 -470 95 A C ATOM 503 CD2 LEU A 69 47.172 123.582 280.537 1.00 31.51 A C ANISOU 503 CD2 LEU A 69 3465 4141 4364 544 -292 226 A C ATOM 504 N ALA A 70 45.703 120.895 284.838 1.00 22.32 A N ANISOU 504 N ALA A 70 2688 3067 2726 976 -278 716 A N ATOM 505 CA ALA A 70 46.218 120.306 286.073 1.00 32.96 A C ANISOU 505 CA ALA A 70 4095 4498 3932 1178 -344 840 A C ATOM 506 C ALA A 70 47.068 119.049 285.877 1.00 39.27 A C ANISOU 506 C ALA A 70 4869 5169 4881 1223 -368 922 A C ATOM 507 O ALA A 70 48.075 118.872 286.564 1.00 37.33 A O ANISOU 507 O ALA A 70 4629 4992 4564 1379 -499 914 A O ATOM 508 CB ALA A 70 45.074 120.033 287.058 1.00 33.88 A C ANISOU 508 CB ALA A 70 4304 4703 3865 1269 -223 1062 A C ATOM 509 N GLU A 71 46.681 118.185 284.943 1.00 41.99 A N ANISOU 509 N GLU A 71 5177 5329 5449 1101 -264 975 A N ATOM 510 CA GLU A 71 47.442 116.956 284.727 1.00 47.14 A C ANISOU 510 CA GLU A 71 5789 5839 6284 1148 -297 1032 A C ATOM 511 C GLU A 71 48.762 117.190 283.993 1.00 40.81 A C ANISOU 511 C GLU A 71 4894 5034 5577 1131 -420 809 A C ATOM 512 O GLU A 71 49.601 116.293 283.914 1.00 38.61 A O ANISOU 512 O GLU A 71 4574 4667 5430 1198 -481 818 A O ATOM 513 CB GLU A 71 46.613 115.882 284.023 1.00 58.08 A C ANISOU 513 CB GLU A 71 7137 7011 7921 1051 -173 1126 A C ATOM 514 CG GLU A 71 46.218 116.208 282.604 1.00 66.87 A C ANISOU 514 CG GLU A 71 8174 8067 9168 886 -135 921 A C ATOM 515 CD GLU A 71 45.384 115.102 281.989 1.00 77.81 A C ANISOU 515 CD GLU A 71 9502 9237 10827 821 -51 968 A C ATOM 516 OE1 GLU A 71 45.313 114.006 282.591 1.00 81.80 A O ANISOU 516 OE1 GLU A 71 10003 9595 11483 891 -28 1167 A O ATOM 517 OE2 GLU A 71 44.808 115.325 280.902 1.00 81.06 A O1- ANISOU 517 OE2 GLU A 71 9857 9619 11323 712 -17 807 A O1- ATOM 518 N HIS A 72 48.947 118.394 283.461 1.00 33.37 A N ANISOU 518 N HIS A 72 3902 4182 4594 1047 -449 626 A N ATOM 519 CA HIS A 72 50.174 118.708 282.741 1.00 28.74 A C ANISOU 519 CA HIS A 72 3199 3601 4119 1026 -533 446 A C ATOM 520 C HIS A 72 51.121 119.535 283.603 1.00 26.48 A C ANISOU 520 C HIS A 72 2888 3430 3744 1133 -690 356 A C ATOM 521 O HIS A 72 52.141 120.025 283.117 1.00 31.11 A O ANISOU 521 O HIS A 72 3351 4022 4447 1111 -761 208 A O ATOM 522 CB HIS A 72 49.858 119.443 281.437 1.00 31.54 A C ANISOU 522 CB HIS A 72 3476 3964 4545 870 -448 330 A C ATOM 523 CG HIS A 72 48.937 118.691 280.530 1.00 34.02 A C ANISOU 523 CG HIS A 72 3795 4186 4945 791 -328 357 A C ATOM 524 CD2 HIS A 72 48.028 119.125 279.621 1.00 31.16 A C ANISOU 524 CD2 HIS A 72 3420 3837 4583 681 -232 315 A C ATOM 525 ND1 HIS A 72 48.862 117.312 280.516 1.00 32.05 A N ANISOU 525 ND1 HIS A 72 3551 3803 4822 837 -317 420 A N ATOM 526 CE1 HIS A 72 47.962 116.932 279.630 1.00 32.79 A C ANISOU 526 CE1 HIS A 72 3622 3826 5012 759 -231 385 A C ATOM 527 NE2 HIS A 72 47.441 118.009 279.071 1.00 35.31 A N ANISOU 527 NE2 HIS A 72 3937 4247 5233 670 -179 320 A N ATOM 528 N GLY A 73 50.768 119.714 284.874 1.00 30.02 A N ANISOU 528 N GLY A 73 3435 3978 3994 1262 -746 435 A N ATOM 529 CA GLY A 73 51.652 120.376 285.821 1.00 29.99 A C ANISOU 529 CA GLY A 73 3404 4096 3896 1415 -935 315 A C ATOM 530 C GLY A 73 51.287 121.798 286.223 1.00 32.34 A C ANISOU 530 C GLY A 73 3684 4507 4097 1411 -999 176 A C ATOM 531 O GLY A 73 52.045 122.451 286.941 1.00 35.80 A O ANISOU 531 O GLY A 73 4063 5033 4504 1541 -1188 13 A O ATOM 532 N ILE A 74 50.137 122.287 285.770 1.00 24.71 A N ANISOU 532 N ILE A 74 2750 3530 3108 1274 -864 213 A N ATOM 533 CA ILE A 74 49.662 123.609 286.180 1.00 29.92 A C ANISOU 533 CA ILE A 74 3393 4284 3692 1276 -925 83 A C ATOM 534 C ILE A 74 48.348 123.511 286.944 1.00 24.93 A C ANISOU 534 C ILE A 74 2899 3762 2812 1341 -832 218 A C ATOM 535 O ILE A 74 47.291 123.314 286.345 1.00 26.15 A O ANISOU 535 O ILE A 74 3096 3851 2987 1204 -659 333 A O ATOM 536 CB ILE A 74 49.443 124.520 284.963 1.00 30.66 A C ANISOU 536 CB ILE A 74 3380 4279 3989 1063 -854 1 A C ATOM 537 CG1 ILE A 74 50.615 124.391 283.984 1.00 38.32 A C ANISOU 537 CG1 ILE A 74 4209 5147 5203 985 -866 -55 A C ATOM 538 CG2 ILE A 74 49.207 125.965 285.406 1.00 28.51 A C ANISOU 538 CG2 ILE A 74 3046 4064 3721 1075 -963 -167 A C ATOM 539 CD1 ILE A 74 51.393 125.666 283.781 1.00 44.87 A C ANISOU 539 CD1 ILE A 74 4859 5946 6245 945 -979 -226 A C ATOM 540 N VAL A 75 48.406 123.687 288.261 1.00 27.60 A N ANISOU 540 N VAL A 75 3290 4284 2912 1566 -950 190 A N ATOM 541 CA VAL A 75 47.237 123.446 289.102 1.00 29.49 A C ANISOU 541 CA VAL A 75 3655 4670 2881 1672 -838 361 A C ATOM 542 C VAL A 75 46.643 124.746 289.637 1.00 34.43 A C ANISOU 542 C VAL A 75 4263 5446 3373 1728 -914 174 A C ATOM 543 O VAL A 75 47.189 125.361 290.551 1.00 37.09 A O ANISOU 543 O VAL A 75 4577 5907 3610 1870 -1068 -28 A O ATOM 544 CB VAL A 75 47.570 122.508 290.287 1.00 33.31 A C ANISOU 544 CB VAL A 75 4230 5281 3145 1893 -847 520 A C ATOM 545 CG1 VAL A 75 46.337 122.269 291.144 1.00 33.71 A C ANISOU 545 CG1 VAL A 75 4384 5477 2948 1971 -673 720 A C ATOM 546 CG2 VAL A 75 48.133 121.182 289.783 1.00 32.45 A C ANISOU 546 CG2 VAL A 75 4126 5007 3197 1861 -795 711 A C ATOM 547 N PHE A 76 45.527 125.165 289.053 1.00 36.80 A N ANISOU 547 N PHE A 76 4570 5684 3727 1557 -769 205 A N ATOM 548 CA PHE A 76 44.750 126.266 289.599 1.00 40.31 A C ANISOU 548 CA PHE A 76 5008 6270 4037 1616 -812 59 A C ATOM 549 C PHE A 76 43.837 125.634 290.642 1.00 48.94 A C ANISOU 549 C PHE A 76 6224 7572 4800 1798 -680 278 A C ATOM 550 O PHE A 76 43.523 124.448 290.553 1.00 52.22 A O ANISOU 550 O PHE A 76 6710 7928 5204 1773 -503 571 A O ATOM 551 CB PHE A 76 43.896 126.913 288.504 1.00 38.25 A C ANISOU 551 CB PHE A 76 4703 5854 3977 1363 -700 29 A C ATOM 552 CG PHE A 76 44.681 127.736 287.507 1.00 36.40 A C ANISOU 552 CG PHE A 76 4329 5447 4055 1203 -806 -152 A C ATOM 553 CD1 PHE A 76 45.077 129.034 287.809 1.00 39.72 A C ANISOU 553 CD1 PHE A 76 4630 5887 4574 1251 -1003 -418 A C ATOM 554 CD2 PHE A 76 45.002 127.216 286.258 1.00 34.00 A C ANISOU 554 CD2 PHE A 76 3991 4963 3963 1018 -703 -51 A C ATOM 555 CE1 PHE A 76 45.791 129.794 286.889 1.00 40.38 A C ANISOU 555 CE1 PHE A 76 4558 5792 4994 1100 -1073 -531 A C ATOM 556 CE2 PHE A 76 45.713 127.970 285.334 1.00 36.75 A C ANISOU 556 CE2 PHE A 76 4199 5183 4581 889 -763 -166 A C ATOM 557 CZ PHE A 76 46.108 129.259 285.649 1.00 38.97 A C ANISOU 557 CZ PHE A 76 4356 5462 4989 921 -936 -381 A C ATOM 558 N GLY A 77 43.401 126.401 291.632 1.00 56.60 A N ANISOU 558 N GLY A 77 7200 8739 5565 1943 -723 132 A N ATOM 559 CA GLY A 77 42.424 125.872 292.566 1.00 62.54 A C ANISOU 559 CA GLY A 77 8037 9662 6064 2065 -526 342 A C ATOM 560 C GLY A 77 41.089 125.706 291.861 1.00 58.15 A C ANISOU 560 C GLY A 77 7506 9030 5557 1903 -320 540 A C ATOM 561 O GLY A 77 41.006 125.784 290.630 1.00 48.26 A O ANISOU 561 O GLY A 77 6217 7551 4570 1667 -298 524 A O ATOM 562 N GLU A 78 40.034 125.455 292.624 1.00 57.59 A N ANISOU 562 N GLU A 78 7467 9091 5324 1979 -131 699 A N ATOM 563 CA GLU A 78 38.704 125.595 292.067 1.00 56.81 A C ANISOU 563 CA GLU A 78 7366 8932 5287 1829 43 803 A C ATOM 564 C GLU A 78 38.453 127.094 292.084 1.00 45.56 A C ANISOU 564 C GLU A 78 5889 7610 3811 1850 -116 466 A C ATOM 565 O GLU A 78 38.768 127.766 293.064 1.00 46.08 A O ANISOU 565 O GLU A 78 5921 7853 3735 2042 -248 250 A O ATOM 566 CB GLU A 78 37.671 124.825 292.887 1.00 70.42 A C ANISOU 566 CB GLU A 78 9097 10734 6924 1895 291 1079 A C ATOM 567 CG GLU A 78 36.463 124.381 292.080 1.00 78.20 A C ANISOU 567 CG GLU A 78 10066 11534 8114 1680 508 1274 A C ATOM 568 CD GLU A 78 35.161 124.901 292.647 1.00 88.79 A C ANISOU 568 CD GLU A 78 11368 13008 9359 1719 625 1269 A C ATOM 569 OE1 GLU A 78 35.146 125.338 293.820 1.00 94.76 A O ANISOU 569 OE1 GLU A 78 12113 14016 9875 1943 579 1191 A O ATOM 570 OE2 GLU A 78 34.153 124.888 291.910 1.00 89.48 A O1- ANISOU 570 OE2 GLU A 78 11426 12948 9624 1534 755 1326 A O1- ATOM 571 N PRO A 79 37.884 127.631 291.004 1.00 43.37 A N ANISOU 571 N PRO A 79 5570 7148 3760 1615 -91 383 A N ATOM 572 CA PRO A 79 37.687 129.082 290.932 1.00 44.66 A C ANISOU 572 CA PRO A 79 5657 7339 3972 1600 -251 54 A C ATOM 573 C PRO A 79 36.658 129.606 291.932 1.00 46.47 A C ANISOU 573 C PRO A 79 5893 7842 3923 1788 -203 0 A C ATOM 574 O PRO A 79 35.725 128.896 292.304 1.00 47.31 A O ANISOU 574 O PRO A 79 6035 8002 3938 1801 33 256 A O ATOM 575 CB PRO A 79 37.199 129.291 289.496 1.00 38.35 A C ANISOU 575 CB PRO A 79 4815 6250 3506 1288 -175 60 A C ATOM 576 CG PRO A 79 36.562 128.005 289.123 1.00 39.71 A C ANISOU 576 CG PRO A 79 5045 6327 3716 1187 69 377 A C ATOM 577 CD PRO A 79 37.372 126.940 289.808 1.00 41.06 A C ANISOU 577 CD PRO A 79 5275 6581 3746 1345 82 560 A C ATOM 578 N LYS A 80 36.852 130.837 292.389 1.00 45.96 A N ANISOU 578 N LYS A 80 5745 7857 3861 1892 -413 -344 A N ATOM 579 CA LYS A 80 35.835 131.498 293.190 1.00 50.23 A C ANISOU 579 CA LYS A 80 6241 8562 4282 2012 -370 -446 A C ATOM 580 C LYS A 80 34.993 132.326 292.225 1.00 47.96 A C ANISOU 580 C LYS A 80 5913 8146 4165 1815 -373 -573 A C ATOM 581 O LYS A 80 35.510 133.206 291.534 1.00 46.79 A O ANISOU 581 O LYS A 80 5684 7818 4277 1697 -567 -808 A O ATOM 582 CB LYS A 80 36.481 132.354 294.284 1.00 59.15 A C ANISOU 582 CB LYS A 80 7280 9836 5357 2259 -588 -759 A C ATOM 583 CG LYS A 80 35.503 132.976 295.277 1.00 67.04 A C ANISOU 583 CG LYS A 80 8215 11054 6204 2444 -564 -859 A C ATOM 584 CD LYS A 80 36.241 133.680 296.415 1.00 74.74 A C ANISOU 584 CD LYS A 80 9093 12190 7113 2736 -773 -1163 A C ATOM 585 CE LYS A 80 35.316 133.971 297.594 1.00 78.54 A C ANISOU 585 CE LYS A 80 9516 12966 7358 2986 -725 -1185 A C ATOM 586 NZ LYS A 80 34.258 134.967 297.265 1.00 77.72 A N1+ ANISOU 586 NZ LYS A 80 9332 12821 7377 2891 -752 -1340 A N1+ ATOM 587 N THR A 81 33.703 132.015 292.147 1.00 45.71 A N ANISOU 587 N THR A 81 5655 7889 3822 1748 -141 -389 A N ATOM 588 CA THR A 81 32.854 132.596 291.114 1.00 39.41 A C ANISOU 588 CA THR A 81 4811 6888 3275 1512 -97 -451 A C ATOM 589 C THR A 81 31.791 133.544 291.678 1.00 40.35 A C ANISOU 589 C THR A 81 4868 7171 3290 1619 -110 -644 A C ATOM 590 O THR A 81 31.142 133.246 292.685 1.00 39.82 A O ANISOU 590 O THR A 81 4801 7283 3045 1762 3 -521 A O ATOM 591 CB THR A 81 32.169 131.481 290.298 1.00 42.54 A C ANISOU 591 CB THR A 81 5255 7104 3802 1299 168 -118 A C ATOM 592 CG2 THR A 81 31.420 132.059 289.105 1.00 42.44 A C ANISOU 592 CG2 THR A 81 5187 6852 4085 1051 181 -193 A C ATOM 593 OG1 THR A 81 33.159 130.555 289.828 1.00 45.27 A O ANISOU 593 OG1 THR A 81 5648 7308 4245 1223 171 42 A O ATOM 594 N ASP A 82 31.636 134.691 291.021 1.00 38.91 A N ANISOU 594 N ASP A 82 4597 6818 3367 1494 -264 -897 A N ATOM 595 CA ASP A 82 30.627 135.685 291.377 1.00 34.30 A C ANISOU 595 CA ASP A 82 3934 6324 2774 1559 -304 -1106 A C ATOM 596 C ASP A 82 29.732 135.909 290.159 1.00 33.91 A C ANISOU 596 C ASP A 82 3860 6017 3006 1287 -205 -1044 A C ATOM 597 O ASP A 82 30.122 136.607 289.218 1.00 33.98 A O ANISOU 597 O ASP A 82 3809 5771 3330 1119 -348 -1151 A O ATOM 598 CB ASP A 82 31.308 136.989 291.808 1.00 33.80 A C ANISOU 598 CB ASP A 82 3740 6233 2869 1670 -619 -1464 A C ATOM 599 CG ASP A 82 30.320 138.056 292.271 1.00 39.84 A C ANISOU 599 CG ASP A 82 4391 7057 3688 1741 -684 -1661 A C ATOM 600 OD1 ASP A 82 29.108 137.935 291.992 1.00 42.64 A O ANISOU 600 OD1 ASP A 82 4771 7423 4007 1650 -513 -1557 A O ATOM 601 OD2 ASP A 82 30.765 139.025 292.924 1.00 43.71 A O1- ANISOU 601 OD2 ASP A 82 4750 7572 4287 1899 -903 -1927 A O1- ATOM 602 N ILE A 83 28.534 135.327 290.193 1.00 28.30 A N ANISOU 602 N ILE A 83 3523 4206 3026 1010 214 -1116 A N ATOM 603 CA ILE A 83 27.622 135.329 289.049 1.00 34.03 A C ANISOU 603 CA ILE A 83 4082 4990 3857 872 280 -985 A C ATOM 604 C ILE A 83 27.176 136.743 288.664 1.00 31.12 A C ANISOU 604 C ILE A 83 3734 4577 3513 986 240 -1033 A C ATOM 605 O ILE A 83 26.999 137.053 287.477 1.00 26.29 A O ANISOU 605 O ILE A 83 3026 3926 3039 823 209 -1002 A O ATOM 606 CB ILE A 83 26.370 134.468 289.354 1.00 39.51 A C ANISOU 606 CB ILE A 83 4623 5902 4487 875 430 -735 A C ATOM 607 CG1 ILE A 83 26.789 133.053 289.748 1.00 41.46 A C ANISOU 607 CG1 ILE A 83 4913 6150 4691 752 442 -688 A C ATOM 608 CG2 ILE A 83 25.436 134.416 288.158 1.00 42.83 A C ANISOU 608 CG2 ILE A 83 4870 6380 5022 660 424 -543 A C ATOM 609 CD1 ILE A 83 27.610 132.347 288.686 1.00 33.94 A C ANISOU 609 CD1 ILE A 83 4061 5017 3818 507 356 -740 A C ATOM 610 N ASP A 84 27.019 137.599 289.671 1.00 29.81 A N ANISOU 610 N ASP A 84 3760 4389 3178 1294 234 -1114 A N ATOM 611 CA ASP A 84 26.641 138.990 289.444 1.00 36.69 A C ANISOU 611 CA ASP A 84 4773 5164 4004 1472 185 -1176 A C ATOM 612 C ASP A 84 27.680 139.709 288.582 1.00 33.59 A C ANISOU 612 C ASP A 84 4450 4530 3780 1230 -58 -1320 A C ATOM 613 O ASP A 84 27.332 140.514 287.708 1.00 35.59 A O ANISOU 613 O ASP A 84 4673 4733 4118 1199 -82 -1314 A O ATOM 614 CB ASP A 84 26.457 139.724 290.778 1.00 47.52 A C ANISOU 614 CB ASP A 84 6477 6444 5133 1781 162 -1171 A C ATOM 615 CG ASP A 84 25.297 139.177 291.596 1.00 56.86 A C ANISOU 615 CG ASP A 84 7549 7890 6166 2030 417 -920 A C ATOM 616 OD1 ASP A 84 24.266 138.808 290.994 1.00 55.52 A O ANISOU 616 OD1 ASP A 84 7057 7978 6058 2037 608 -695 A O ATOM 617 OD2 ASP A 84 25.411 139.132 292.842 1.00 65.38 A O1- ANISOU 617 OD2 ASP A 84 8845 8931 7064 2214 405 -904 A O1- ATOM 618 N LYS A 85 28.954 139.406 288.818 1.00 33.61 A N ANISOU 618 N LYS A 85 4510 4420 3840 1060 -233 -1397 A N ATOM 619 CA LYS A 85 30.031 140.002 288.029 1.00 33.21 A C ANISOU 619 CA LYS A 85 4441 4209 3970 815 -463 -1421 A C ATOM 620 C LYS A 85 30.096 139.483 286.590 1.00 27.92 A C ANISOU 620 C LYS A 85 3484 3622 3504 600 -354 -1309 A C ATOM 621 O LYS A 85 30.324 140.255 285.657 1.00 24.05 A O ANISOU 621 O LYS A 85 2947 3045 3145 487 -449 -1292 A O ATOM 622 CB LYS A 85 31.393 139.875 288.732 1.00 26.69 A C ANISOU 622 CB LYS A 85 3701 3292 3146 702 -699 -1429 A C ATOM 623 CG LYS A 85 31.626 140.923 289.812 1.00 37.99 A C ANISOU 623 CG LYS A 85 5550 4489 4394 816 -994 -1552 A C ATOM 624 CD LYS A 85 33.108 141.049 290.142 1.00 43.52 A C ANISOU 624 CD LYS A 85 6275 5081 5178 557 -1352 -1472 A C ATOM 625 CE LYS A 85 33.362 142.189 291.114 1.00 55.86 A C ANISOU 625 CE LYS A 85 8324 6340 6560 584 -1713 -1526 A C ATOM 626 NZ LYS A 85 33.173 141.794 292.539 1.00 59.73 A N1+ ANISOU 626 NZ LYS A 85 9075 6819 6800 818 -1656 -1574 A N1+ ATOM 627 N ILE A 86 29.902 138.180 286.415 1.00 27.57 A N ANISOU 627 N ILE A 86 3310 3713 3453 557 -174 -1225 A N ATOM 628 CA ILE A 86 29.823 137.603 285.078 1.00 25.61 A C ANISOU 628 CA ILE A 86 2932 3487 3310 403 -84 -1128 A C ATOM 629 C ILE A 86 28.693 138.277 284.295 1.00 25.84 A C ANISOU 629 C ILE A 86 2905 3528 3384 388 -49 -1106 A C ATOM 630 O ILE A 86 28.887 138.726 283.151 1.00 28.62 A O ANISOU 630 O ILE A 86 3207 3815 3853 284 -88 -1084 A O ATOM 631 CB ILE A 86 29.584 136.076 285.135 1.00 22.70 A C ANISOU 631 CB ILE A 86 2576 3193 2855 366 52 -1046 A C ATOM 632 CG1 ILE A 86 30.669 135.394 285.973 1.00 26.53 A C ANISOU 632 CG1 ILE A 86 3113 3689 3278 425 45 -1055 A C ATOM 633 CG2 ILE A 86 29.532 135.479 283.727 1.00 18.21 A C ANISOU 633 CG2 ILE A 86 2033 2565 2322 231 93 -959 A C ATOM 634 CD1 ILE A 86 30.518 133.879 286.051 1.00 30.54 A C ANISOU 634 CD1 ILE A 86 3708 4225 3673 407 163 -980 A C ATOM 635 N ARG A 87 27.524 138.361 284.929 1.00 24.09 A N ANISOU 635 N ARG A 87 2672 3421 3062 523 38 -1067 A N ATOM 636 CA ARG A 87 26.358 138.996 284.321 1.00 28.99 A C ANISOU 636 CA ARG A 87 3192 4116 3708 554 93 -974 A C ATOM 637 C ARG A 87 26.686 140.450 283.947 1.00 28.10 A C ANISOU 637 C ARG A 87 3174 3851 3651 621 -21 -1095 A C ATOM 638 O ARG A 87 26.391 140.907 282.832 1.00 29.25 A O ANISOU 638 O ARG A 87 3234 3974 3907 519 -33 -1054 A O ATOM 639 CB ARG A 87 25.161 138.933 285.282 1.00 30.41 A C ANISOU 639 CB ARG A 87 3309 4506 3740 786 239 -829 A C ATOM 640 CG ARG A 87 23.824 139.293 284.654 1.00 34.04 A C ANISOU 640 CG ARG A 87 3562 5145 4227 810 330 -598 A C ATOM 641 CD ARG A 87 22.712 139.434 285.696 1.00 35.80 A C ANISOU 641 CD ARG A 87 3688 5638 4277 1157 522 -372 A C ATOM 642 NE ARG A 87 22.628 138.277 286.585 1.00 40.38 A N ANISOU 642 NE ARG A 87 4202 6358 4781 1140 588 -244 A N ATOM 643 CZ ARG A 87 22.932 138.296 287.882 1.00 41.17 A C ANISOU 643 CZ ARG A 87 4479 6465 4700 1443 665 -336 A C ATOM 644 NH1 ARG A 87 23.324 139.423 288.463 1.00 41.87 A N1+ ANISOU 644 NH1 ARG A 87 4883 6391 4636 1782 648 -559 A N1+ ATOM 645 NH2 ARG A 87 22.827 137.188 288.603 1.00 38.21 A N ANISOU 645 NH2 ARG A 87 4017 6229 4273 1401 728 -196 A N ATOM 646 N THR A 88 27.334 141.158 284.867 1.00 27.89 A N ANISOU 646 N THR A 88 3369 3690 3538 766 -144 -1234 A N ATOM 647 CA THR A 88 27.722 142.545 284.620 1.00 31.08 A C ANISOU 647 CA THR A 88 3953 3885 3971 788 -333 -1335 A C ATOM 648 C THR A 88 28.639 142.656 283.394 1.00 28.90 A C ANISOU 648 C THR A 88 3529 3530 3924 496 -451 -1298 A C ATOM 649 O THR A 88 28.473 143.554 282.562 1.00 26.92 A O ANISOU 649 O THR A 88 3273 3196 3759 454 -510 -1295 A O ATOM 650 CB THR A 88 28.410 143.166 285.858 1.00 31.74 A C ANISOU 650 CB THR A 88 4396 3768 3895 917 -552 -1470 A C ATOM 651 CG2 THR A 88 28.931 144.566 285.548 1.00 29.85 A C ANISOU 651 CG2 THR A 88 4407 3245 3689 847 -848 -1543 A C ATOM 652 OG1 THR A 88 27.469 143.251 286.937 1.00 35.00 A O ANISOU 652 OG1 THR A 88 5019 4243 4038 1299 -408 -1492 A O ATOM 653 N TRP A 89 29.579 141.725 283.262 1.00 27.74 A N ANISOU 653 N TRP A 89 3259 3429 3853 341 -452 -1237 A N ATOM 654 CA TRP A 89 30.469 141.718 282.100 1.00 27.55 A C ANISOU 654 CA TRP A 89 3076 3386 4004 158 -495 -1127 A C ATOM 655 C TRP A 89 29.723 141.462 280.781 1.00 21.28 A C ANISOU 655 C TRP A 89 2175 2647 3265 115 -338 -1070 A C ATOM 656 O TRP A 89 29.936 142.166 279.778 1.00 27.10 A O ANISOU 656 O TRP A 89 2849 3327 4121 40 -389 -1021 A O ATOM 657 CB TRP A 89 31.586 140.692 282.289 1.00 26.09 A C ANISOU 657 CB TRP A 89 2803 3279 3831 111 -467 -1018 A C ATOM 658 CG TRP A 89 32.407 140.502 281.053 1.00 31.08 A C ANISOU 658 CG TRP A 89 3272 3953 4583 40 -415 -834 A C ATOM 659 CD1 TRP A 89 33.241 141.419 280.466 1.00 30.91 A C ANISOU 659 CD1 TRP A 89 3120 3904 4720 -64 -565 -683 A C ATOM 660 CD2 TRP A 89 32.472 139.323 280.244 1.00 28.89 A C ANISOU 660 CD2 TRP A 89 2990 3745 4241 105 -197 -743 A C ATOM 661 CE2 TRP A 89 33.366 139.592 279.187 1.00 28.84 A C ANISOU 661 CE2 TRP A 89 2851 3774 4334 112 -173 -537 A C ATOM 662 CE3 TRP A 89 31.862 138.069 280.311 1.00 30.73 A C ANISOU 662 CE3 TRP A 89 3368 3990 4317 163 -45 -790 A C ATOM 663 NE1 TRP A 89 33.818 140.875 279.341 1.00 33.86 A N ANISOU 663 NE1 TRP A 89 3357 4377 5132 -16 -398 -480 A N ATOM 664 CZ2 TRP A 89 33.657 138.650 278.206 1.00 35.23 A C ANISOU 664 CZ2 TRP A 89 3729 4617 5040 256 36 -406 A C ATOM 665 CZ3 TRP A 89 32.154 137.138 279.336 1.00 34.26 A C ANISOU 665 CZ3 TRP A 89 3931 4419 4668 240 99 -682 A C ATOM 666 CH2 TRP A 89 33.045 137.429 278.300 1.00 35.65 A C ANISOU 666 CH2 TRP A 89 4031 4617 4897 326 157 -505 A C ATOM 667 N LYS A 90 28.850 140.457 280.792 1.00 20.93 A N ANISOU 667 N LYS A 90 2124 2701 3126 135 -186 -1049 A N ATOM 668 CA LYS A 90 27.998 140.158 279.633 1.00 25.05 A C ANISOU 668 CA LYS A 90 2602 3248 3667 46 -112 -972 A C ATOM 669 C LYS A 90 27.257 141.418 279.172 1.00 19.58 A C ANISOU 669 C LYS A 90 1855 2542 3044 74 -149 -984 A C ATOM 670 O LYS A 90 27.245 141.798 277.968 1.00 20.58 A O ANISOU 670 O LYS A 90 1942 2618 3259 -11 -166 -945 A O ATOM 671 CB LYS A 90 26.968 139.099 280.033 1.00 26.25 A C ANISOU 671 CB LYS A 90 2759 3509 3707 14 -38 -892 A C ATOM 672 CG LYS A 90 26.118 138.593 278.888 1.00 24.52 A C ANISOU 672 CG LYS A 90 2545 3286 3486 -161 -53 -761 A C ATOM 673 CD LYS A 90 24.743 138.123 279.362 1.00 28.86 A C ANISOU 673 CD LYS A 90 2983 4005 3980 -231 -47 -579 A C ATOM 674 CE LYS A 90 23.858 139.291 279.783 1.00 27.79 A C ANISOU 674 CE LYS A 90 2649 4035 3876 -57 18 -519 A C ATOM 675 NZ LYS A 90 22.428 138.886 279.923 1.00 28.86 A N1+ ANISOU 675 NZ LYS A 90 2573 4410 3982 -132 37 -202 A N1+ ATOM 676 N GLU A 91 26.637 142.060 280.158 1.00 18.88 A N ANISOU 676 N GLU A 91 1801 2494 2877 244 -145 -1030 A N ATOM 677 CA GLU A 91 25.923 143.303 279.925 1.00 31.75 A C ANISOU 677 CA GLU A 91 3447 4105 4512 367 -156 -1037 A C ATOM 678 C GLU A 91 26.853 144.372 279.366 1.00 31.10 A C ANISOU 678 C GLU A 91 3448 3821 4545 297 -323 -1120 A C ATOM 679 O GLU A 91 26.429 145.181 278.553 1.00 28.68 A O ANISOU 679 O GLU A 91 3117 3479 4302 296 -334 -1098 A O ATOM 680 CB GLU A 91 25.214 143.784 281.197 1.00 33.72 A C ANISOU 680 CB GLU A 91 3822 4414 4576 680 -93 -1055 A C ATOM 681 CG GLU A 91 24.033 142.902 281.593 1.00 37.49 A C ANISOU 681 CG GLU A 91 4113 5169 4964 761 96 -850 A C ATOM 682 CD GLU A 91 23.521 143.172 282.997 1.00 44.69 A C ANISOU 682 CD GLU A 91 5155 6175 5649 1147 211 -826 A C ATOM 683 OE1 GLU A 91 24.113 144.012 283.712 1.00 47.99 A O ANISOU 683 OE1 GLU A 91 5907 6383 5944 1351 111 -1021 A O ATOM 684 OE2 GLU A 91 22.524 142.529 283.388 1.00 46.95 A O1- ANISOU 684 OE2 GLU A 91 5235 6742 5863 1246 381 -577 A O1- ATOM 685 N LYS A 92 28.111 144.383 279.805 1.00 28.42 A N ANISOU 685 N LYS A 92 3185 3371 4243 219 -470 -1165 A N ATOM 686 CA LYS A 92 29.074 145.357 279.294 1.00 30.87 A C ANISOU 686 CA LYS A 92 3520 3519 4690 87 -678 -1143 A C ATOM 687 C LYS A 92 29.391 145.140 277.814 1.00 28.28 A C ANISOU 687 C LYS A 92 2980 3246 4518 -55 -603 -1012 A C ATOM 688 O LYS A 92 29.388 146.100 277.029 1.00 24.59 A O ANISOU 688 O LYS A 92 2497 2694 4151 -107 -682 -980 A O ATOM 689 CB LYS A 92 30.361 145.356 280.122 1.00 32.97 A C ANISOU 689 CB LYS A 92 3853 3701 4973 -12 -894 -1116 A C ATOM 690 CG LYS A 92 31.384 146.387 279.659 1.00 40.76 A C ANISOU 690 CG LYS A 92 4824 4540 6122 -217 -1179 -991 A C ATOM 691 CD LYS A 92 32.643 146.345 280.515 1.00 50.68 A C ANISOU 691 CD LYS A 92 6100 5747 7408 -373 -1450 -875 A C ATOM 692 CE LYS A 92 33.630 147.425 280.094 1.00 60.05 A C ANISOU 692 CE LYS A 92 7268 6843 8704 -597 -1693 -608 A C ATOM 693 NZ LYS A 92 34.911 147.344 280.858 1.00 64.90 A N1+ ANISOU 693 NZ LYS A 92 7848 7475 9334 -770 -1916 -380 A N1+ ATOM 694 N VAL A 93 29.662 143.894 277.417 1.00 24.75 A N ANISOU 694 N VAL A 93 2430 2916 4058 -82 -451 -931 A N ATOM 695 CA VAL A 93 29.874 143.647 275.980 1.00 26.58 A C ANISOU 695 CA VAL A 93 2570 3172 4358 -130 -357 -808 A C ATOM 696 C VAL A 93 28.634 144.044 275.151 1.00 25.82 A C ANISOU 696 C VAL A 93 2486 3064 4259 -139 -311 -847 A C ATOM 697 O VAL A 93 28.742 144.746 274.104 1.00 27.52 A O ANISOU 697 O VAL A 93 2649 3235 4573 -176 -333 -787 A O ATOM 698 CB VAL A 93 30.467 142.226 275.642 1.00 28.46 A C ANISOU 698 CB VAL A 93 2833 3480 4503 -82 -206 -705 A C ATOM 699 CG1 VAL A 93 30.954 141.517 276.889 1.00 30.72 A C ANISOU 699 CG1 VAL A 93 3143 3814 4713 -41 -210 -729 A C ATOM 700 CG2 VAL A 93 29.494 141.375 274.859 1.00 19.19 A C ANISOU 700 CG2 VAL A 93 1802 2286 3204 -89 -103 -724 A C ATOM 701 N ILE A 94 27.458 143.630 275.635 1.00 25.37 A N ANISOU 701 N ILE A 94 2463 3077 4099 -106 -253 -896 A N ATOM 702 CA ILE A 94 26.226 144.012 274.941 1.00 24.44 A C ANISOU 702 CA ILE A 94 2296 3004 3986 -123 -226 -854 A C ATOM 703 C ILE A 94 26.074 145.542 274.798 1.00 27.50 A C ANISOU 703 C ILE A 94 2676 3320 4451 -44 -293 -898 A C ATOM 704 O ILE A 94 25.885 146.050 273.696 1.00 26.55 A O ANISOU 704 O ILE A 94 2509 3168 4409 -97 -301 -851 A O ATOM 705 CB ILE A 94 24.981 143.433 275.638 1.00 24.95 A C ANISOU 705 CB ILE A 94 2313 3225 3943 -92 -164 -785 A C ATOM 706 CG1 ILE A 94 24.973 141.905 275.544 1.00 25.43 A C ANISOU 706 CG1 ILE A 94 2434 3307 3920 -237 -156 -710 A C ATOM 707 CG2 ILE A 94 23.711 143.985 275.013 1.00 21.81 A C ANISOU 707 CG2 ILE A 94 1791 2932 3565 -93 -146 -656 A C ATOM 708 CD1 ILE A 94 23.847 141.264 276.334 1.00 25.73 A C ANISOU 708 CD1 ILE A 94 2379 3524 3875 -257 -129 -567 A C ATOM 709 N ASN A 95 26.193 146.270 275.903 1.00 23.52 A N ANISOU 709 N ASN A 95 2287 2754 3897 95 -360 -991 A N ATOM 710 CA ASN A 95 26.032 147.730 275.909 1.00 24.39 A C ANISOU 710 CA ASN A 95 2528 2724 4014 204 -461 -1047 A C ATOM 711 C ASN A 95 27.051 148.412 275.004 1.00 28.07 A C ANISOU 711 C ASN A 95 2973 3040 4651 29 -613 -1014 A C ATOM 712 O ASN A 95 26.743 149.402 274.336 1.00 31.40 A O ANISOU 712 O ASN A 95 3425 3379 5125 44 -659 -1005 A O ATOM 713 CB ASN A 95 26.101 148.300 277.332 1.00 28.11 A C ANISOU 713 CB ASN A 95 3282 3074 4323 408 -558 -1163 A C ATOM 714 CG ASN A 95 24.914 147.876 278.199 1.00 38.27 A C ANISOU 714 CG ASN A 95 4577 4551 5414 685 -357 -1130 A C ATOM 715 ND2 ASN A 95 25.070 147.990 279.520 1.00 35.29 A N ANISOU 715 ND2 ASN A 95 4464 4094 4852 892 -400 -1223 A N ATOM 716 OD1 ASN A 95 23.877 147.450 277.689 1.00 43.14 A O ANISOU 716 OD1 ASN A 95 4961 5392 6038 708 -183 -979 A O ATOM 717 N GLN A 96 28.278 147.894 275.008 1.00 25.94 A N ANISOU 717 N GLN A 96 2629 2762 4466 -118 -683 -949 A N ATOM 718 CA GLN A 96 29.293 148.377 274.079 1.00 31.67 A C ANISOU 718 CA GLN A 96 3236 3433 5364 -273 -786 -800 A C ATOM 719 C GLN A 96 28.791 148.253 272.638 1.00 30.37 A C ANISOU 719 C GLN A 96 2949 3342 5247 -272 -626 -731 A C ATOM 720 O GLN A 96 28.804 149.234 271.867 1.00 31.83 A O ANISOU 720 O GLN A 96 3133 3459 5503 -301 -681 -663 A O ATOM 721 CB GLN A 96 30.602 147.605 274.270 1.00 34.91 A C ANISOU 721 CB GLN A 96 3516 3927 5820 -356 -798 -638 A C ATOM 722 CG GLN A 96 31.799 148.211 273.553 1.00 49.45 A C ANISOU 722 CG GLN A 96 5231 5786 7773 -468 -882 -350 A C ATOM 723 CD GLN A 96 33.105 147.542 273.948 1.00 63.39 A C ANISOU 723 CD GLN A 96 6829 7680 9575 -517 -905 -122 A C ATOM 724 NE2 GLN A 96 34.151 147.781 273.166 1.00 72.64 A N ANISOU 724 NE2 GLN A 96 7807 8962 10831 -560 -891 210 A N ATOM 725 OE1 GLN A 96 33.171 146.819 274.947 1.00 63.48 A O ANISOU 725 OE1 GLN A 96 6872 7715 9534 -494 -922 -215 A O ATOM 726 N LEU A 97 28.311 147.061 272.280 1.00 24.67 A N ANISOU 726 N LEU A 97 2201 2739 4431 -236 -446 -728 A N ATOM 727 CA LEU A 97 27.843 146.874 270.899 1.00 24.90 A C ANISOU 727 CA LEU A 97 2206 2794 4461 -251 -349 -660 A C ATOM 728 C LEU A 97 26.594 147.699 270.504 1.00 26.65 A C ANISOU 728 C LEU A 97 2423 3009 4695 -238 -364 -704 A C ATOM 729 O LEU A 97 26.539 148.271 269.400 1.00 25.43 A O ANISOU 729 O LEU A 97 2233 2819 4609 -262 -365 -642 A O ATOM 730 CB LEU A 97 27.664 145.384 270.592 1.00 25.30 A C ANISOU 730 CB LEU A 97 2355 2895 4363 -246 -236 -632 A C ATOM 731 CG LEU A 97 29.019 144.660 270.585 1.00 31.15 A C ANISOU 731 CG LEU A 97 3114 3651 5072 -171 -165 -526 A C ATOM 732 CD1 LEU A 97 28.878 143.159 270.750 1.00 28.53 A C ANISOU 732 CD1 LEU A 97 2984 3318 4539 -130 -83 -541 A C ATOM 733 CD2 LEU A 97 29.789 144.992 269.310 1.00 31.39 A C ANISOU 733 CD2 LEU A 97 3100 3677 5149 -96 -96 -347 A C ATOM 734 N THR A 98 25.610 147.780 271.400 1.00 21.32 A N ANISOU 734 N THR A 98 1769 2395 3938 -161 -353 -769 A N ATOM 735 CA THR A 98 24.400 148.562 271.145 1.00 24.49 A C ANISOU 735 CA THR A 98 2132 2849 4325 -76 -328 -740 A C ATOM 736 C THR A 98 24.747 150.046 271.020 1.00 27.50 A C ANISOU 736 C THR A 98 2600 3068 4781 -4 -425 -795 A C ATOM 737 O THR A 98 24.155 150.773 270.208 1.00 21.51 A O ANISOU 737 O THR A 98 1805 2307 4060 27 -411 -748 A O ATOM 738 CB THR A 98 23.318 148.366 272.236 1.00 24.88 A C ANISOU 738 CB THR A 98 2158 3054 4241 85 -248 -710 A C ATOM 739 CG2 THR A 98 22.823 146.930 272.259 1.00 24.79 A C ANISOU 739 CG2 THR A 98 2047 3202 4172 -54 -204 -592 A C ATOM 740 OG1 THR A 98 23.864 148.690 273.519 1.00 32.55 A O ANISOU 740 OG1 THR A 98 3295 3932 5140 233 -288 -837 A O ATOM 741 N GLY A 99 25.692 150.489 271.849 1.00 26.37 A N ANISOU 741 N GLY A 99 2599 2770 4648 1 -562 -874 A N ATOM 742 CA GLY A 99 26.214 151.840 271.756 1.00 28.94 A C ANISOU 742 CA GLY A 99 3078 2874 5043 -15 -753 -894 A C ATOM 743 C GLY A 99 26.804 152.055 270.376 1.00 28.94 A C ANISOU 743 C GLY A 99 2906 2867 5221 -186 -770 -762 A C ATOM 744 O GLY A 99 26.550 153.083 269.726 1.00 24.54 A O ANISOU 744 O GLY A 99 2393 2212 4720 -175 -827 -740 A O ATOM 745 N GLY A 100 27.585 151.074 269.918 1.00 23.43 A N ANISOU 745 N GLY A 100 2061 2291 4551 -277 -680 -637 A N ATOM 746 CA GLY A 100 28.117 151.135 268.567 1.00 19.98 A C ANISOU 746 CA GLY A 100 1530 1901 4159 -318 -604 -454 A C ATOM 747 C GLY A 100 27.056 151.296 267.487 1.00 23.59 A C ANISOU 747 C GLY A 100 1964 2387 4611 -278 -508 -476 A C ATOM 748 O GLY A 100 27.167 152.168 266.604 1.00 25.98 A O ANISOU 748 O GLY A 100 2245 2638 4989 -293 -537 -393 A O ATOM 749 N LEU A 101 26.002 150.484 267.571 1.00 21.61 A N ANISOU 749 N LEU A 101 1710 2228 4273 -250 -420 -552 A N ATOM 750 CA LEU A 101 24.938 150.537 266.569 1.00 19.35 A C ANISOU 750 CA LEU A 101 1393 1996 3964 -255 -371 -514 A C ATOM 751 C LEU A 101 24.206 151.879 266.587 1.00 24.42 A C ANISOU 751 C LEU A 101 2002 2598 4680 -178 -420 -547 A C ATOM 752 O LEU A 101 23.900 152.450 265.530 1.00 23.55 A O ANISOU 752 O LEU A 101 1852 2473 4622 -188 -415 -484 A O ATOM 753 CB LEU A 101 23.935 149.397 266.766 1.00 20.50 A C ANISOU 753 CB LEU A 101 1528 2265 3995 -304 -336 -500 A C ATOM 754 CG LEU A 101 24.403 147.973 266.443 1.00 22.90 A C ANISOU 754 CG LEU A 101 1949 2550 4200 -388 -320 -474 A C ATOM 755 CD1 LEU A 101 23.290 146.995 266.721 1.00 20.71 A C ANISOU 755 CD1 LEU A 101 1700 2367 3803 -501 -366 -414 A C ATOM 756 CD2 LEU A 101 24.871 147.833 265.008 1.00 23.58 A C ANISOU 756 CD2 LEU A 101 2154 2548 4256 -388 -300 -401 A C ATOM 757 N ALA A 102 23.915 152.379 267.784 1.00 23.68 A N ANISOU 757 N ALA A 102 1996 2474 4525 -45 -450 -631 A N ATOM 758 CA ALA A 102 23.269 153.682 267.902 1.00 26.97 A C ANISOU 758 CA ALA A 102 2519 2816 4913 133 -473 -653 A C ATOM 759 C ALA A 102 24.146 154.754 267.262 1.00 24.24 A C ANISOU 759 C ALA A 102 2258 2250 4701 41 -622 -651 A C ATOM 760 O ALA A 102 23.655 155.639 266.542 1.00 28.25 A O ANISOU 760 O ALA A 102 2783 2715 5236 105 -619 -614 A O ATOM 761 CB ALA A 102 22.992 154.017 269.358 1.00 25.52 A C ANISOU 761 CB ALA A 102 2548 2580 4569 365 -484 -747 A C ATOM 762 N GLY A 103 25.445 154.672 267.538 1.00 22.94 A N ANISOU 762 N GLY A 103 2120 1967 4629 -119 -764 -641 A N ATOM 763 CA GLY A 103 26.399 155.598 266.953 1.00 24.48 A C ANISOU 763 CA GLY A 103 2326 1993 4983 -272 -944 -535 A C ATOM 764 C GLY A 103 26.371 155.565 265.436 1.00 29.47 A C ANISOU 764 C GLY A 103 2772 2743 5683 -302 -808 -388 A C ATOM 765 O GLY A 103 26.360 156.615 264.787 1.00 27.40 A O ANISOU 765 O GLY A 103 2539 2368 5503 -324 -891 -329 A O ATOM 766 N MET A 104 26.335 154.362 264.865 1.00 25.34 A N ANISOU 766 N MET A 104 2143 2411 5075 -283 -613 -331 A N ATOM 767 CA MET A 104 26.327 154.234 263.406 1.00 26.34 A C ANISOU 767 CA MET A 104 2201 2604 5202 -277 -501 -207 A C ATOM 768 C MET A 104 25.028 154.716 262.769 1.00 26.38 A C ANISOU 768 C MET A 104 2188 2616 5219 -235 -478 -262 A C ATOM 769 O MET A 104 25.041 155.299 261.682 1.00 27.78 A O ANISOU 769 O MET A 104 2335 2769 5452 -235 -465 -172 A O ATOM 770 CB MET A 104 26.651 152.799 262.973 1.00 25.96 A C ANISOU 770 CB MET A 104 2127 2664 5073 -266 -371 -155 A C ATOM 771 CG MET A 104 28.145 152.524 262.984 1.00 32.07 A C ANISOU 771 CG MET A 104 2807 3468 5911 -268 -351 27 A C ATOM 772 SD MET A 104 28.608 150.993 262.169 1.00 30.75 A S ANISOU 772 SD MET A 104 2654 3391 5640 -126 -149 143 A S ATOM 773 CE MET A 104 27.806 149.783 263.226 1.00 27.85 A C ANISOU 773 CE MET A 104 2465 3019 5097 -164 -164 -88 A C ATOM 774 N ALA A 105 23.910 154.463 263.439 1.00 24.84 A N ANISOU 774 N ALA A 105 1976 2490 4972 -184 -464 -364 A N ATOM 775 CA ALA A 105 22.628 154.957 262.965 1.00 24.25 A C ANISOU 775 CA ALA A 105 1864 2494 4855 -100 -423 -329 A C ATOM 776 C ALA A 105 22.665 156.477 262.953 1.00 28.52 A C ANISOU 776 C ALA A 105 2499 2878 5459 5 -490 -351 A C ATOM 777 O ALA A 105 22.224 157.116 261.993 1.00 21.24 A O ANISOU 777 O ALA A 105 1537 1957 4574 31 -472 -282 A O ATOM 778 CB ALA A 105 21.498 154.456 263.845 1.00 20.22 A C ANISOU 778 CB ALA A 105 1307 2158 4217 -7 -363 -319 A C ATOM 779 N LYS A 106 23.189 157.056 264.027 1.00 21.97 A N ANISOU 779 N LYS A 106 1852 1879 4616 59 -600 -444 A N ATOM 780 CA LYS A 106 23.284 158.503 264.096 1.00 37.00 A C ANISOU 780 CA LYS A 106 3981 3544 6534 142 -735 -471 A C ATOM 781 C LYS A 106 24.159 159.026 262.952 1.00 35.50 A C ANISOU 781 C LYS A 106 3701 3254 6535 -56 -832 -347 A C ATOM 782 O LYS A 106 23.795 159.981 262.272 1.00 28.07 A O ANISOU 782 O LYS A 106 2815 2228 5621 1 -852 -308 A O ATOM 783 CB LYS A 106 23.864 158.931 265.437 1.00 39.80 A C ANISOU 783 CB LYS A 106 4652 3661 6811 175 -926 -582 A C ATOM 784 CG LYS A 106 23.933 160.419 265.609 1.00 47.49 A C ANISOU 784 CG LYS A 106 6013 4299 7733 259 -1137 -620 A C ATOM 785 CD LYS A 106 24.581 160.758 266.922 1.00 57.55 A C ANISOU 785 CD LYS A 106 7697 5277 8893 245 -1406 -724 A C ATOM 786 CE LYS A 106 26.069 160.993 266.739 1.00 64.64 A C ANISOU 786 CE LYS A 106 8520 6121 9921 -155 -1667 -547 A C ATOM 787 NZ LYS A 106 26.301 162.403 266.276 1.00 70.07 A N1+ ANISOU 787 NZ LYS A 106 9447 6603 10573 -225 -1873 -452 A N1+ ATOM 788 N GLY A 107 25.311 158.391 262.744 1.00 37.11 A N ANISOU 788 N GLY A 107 3749 3493 6857 -253 -869 -243 A N ATOM 789 CA GLY A 107 26.239 158.800 261.700 1.00 30.96 A C ANISOU 789 CA GLY A 107 2858 2718 6188 -366 -898 -25 A C ATOM 790 C GLY A 107 25.674 158.724 260.294 1.00 25.28 A C ANISOU 790 C GLY A 107 2007 2108 5492 -308 -733 40 A C ATOM 791 O GLY A 107 26.035 159.517 259.421 1.00 27.90 A O ANISOU 791 O GLY A 107 2303 2388 5910 -341 -769 187 A O ATOM 792 N ARG A 108 24.772 157.776 260.074 1.00 22.44 A N ANISOU 792 N ARG A 108 1599 1901 5026 -232 -579 -44 A N ATOM 793 CA ARG A 108 24.159 157.592 258.761 1.00 22.68 A C ANISOU 793 CA ARG A 108 1577 2026 5014 -192 -468 22 A C ATOM 794 C ARG A 108 22.853 158.376 258.658 1.00 26.14 A C ANISOU 794 C ARG A 108 2031 2474 5428 -99 -474 -30 A C ATOM 795 O ARG A 108 22.128 158.266 257.665 1.00 27.57 A O ANISOU 795 O ARG A 108 2161 2746 5566 -84 -418 35 A O ATOM 796 CB ARG A 108 23.922 156.104 258.474 1.00 20.67 A C ANISOU 796 CB ARG A 108 1345 1902 4607 -200 -371 16 A C ATOM 797 CG ARG A 108 25.197 155.336 258.114 1.00 23.89 A C ANISOU 797 CG ARG A 108 1739 2316 5021 -192 -301 131 A C ATOM 798 CD ARG A 108 24.937 153.846 258.039 1.00 19.43 A C ANISOU 798 CD ARG A 108 1334 1802 4247 -173 -243 88 A C ATOM 799 NE ARG A 108 25.924 153.137 257.227 1.00 21.88 A N ANISOU 799 NE ARG A 108 1755 2111 4446 -35 -117 233 A N ATOM 800 CZ ARG A 108 26.956 152.461 257.723 1.00 25.63 A C ANISOU 800 CZ ARG A 108 2227 2626 4887 47 -33 308 A C ATOM 801 NH1 ARG A 108 27.153 152.404 259.036 1.00 26.79 A N1+ ANISOU 801 NH1 ARG A 108 2264 2795 5122 -52 -101 224 A N1+ ATOM 802 NH2 ARG A 108 27.787 151.831 256.907 1.00 21.94 A N ANISOU 802 NH2 ARG A 108 1887 2182 4266 273 132 490 A N ATOM 803 N LYS A 109 22.547 159.134 259.710 1.00 28.93 A N ANISOU 803 N LYS A 109 2840 2714 5439 -299 -1068 806 A N ATOM 804 CA LYS A 109 21.362 159.992 259.749 1.00 30.38 A C ANISOU 804 CA LYS A 109 3002 2824 5717 -226 -1086 791 A C ATOM 805 C LYS A 109 20.083 159.194 259.588 1.00 30.31 A C ANISOU 805 C LYS A 109 2951 2915 5650 -180 -1026 741 A C ATOM 806 O LYS A 109 19.123 159.655 258.967 1.00 33.01 A O ANISOU 806 O LYS A 109 3238 3256 6049 -133 -1046 783 A O ATOM 807 CB LYS A 109 21.441 161.068 258.663 1.00 30.26 A C ANISOU 807 CB LYS A 109 2941 2761 5796 -230 -1160 938 A C ATOM 808 CG LYS A 109 22.639 162.010 258.799 1.00 29.13 A C ANISOU 808 CG LYS A 109 2829 2500 5741 -279 -1227 1001 A C ATOM 809 CD LYS A 109 22.751 162.920 257.571 1.00 32.08 A C ANISOU 809 CD LYS A 109 3150 2848 6190 -294 -1291 1172 A C ATOM 810 CE LYS A 109 23.884 163.921 257.723 1.00 40.11 A C ANISOU 810 CE LYS A 109 4185 3770 7283 -350 -1344 1215 A C ATOM 811 NZ LYS A 109 25.198 163.236 257.813 1.00 45.18 A N1+ ANISOU 811 NZ LYS A 109 4838 4477 7852 -422 -1324 1229 A N1+ ATOM 812 N VAL A 110 20.055 158.006 260.177 1.00 26.96 A N ANISOU 812 N VAL A 110 2551 2570 5122 -194 -958 651 A N ATOM 813 CA VAL A 110 18.862 157.184 260.118 1.00 24.28 A C ANISOU 813 CA VAL A 110 2168 2320 4736 -158 -900 599 A C ATOM 814 C VAL A 110 18.017 157.397 261.362 1.00 24.78 A C ANISOU 814 C VAL A 110 2260 2316 4841 -96 -851 474 A C ATOM 815 O VAL A 110 18.478 157.164 262.479 1.00 27.19 A O ANISOU 815 O VAL A 110 2637 2584 5109 -104 -818 385 A O ATOM 816 CB VAL A 110 19.204 155.687 259.993 1.00 26.73 A C ANISOU 816 CB VAL A 110 2484 2760 4914 -208 -851 577 A C ATOM 817 CG1 VAL A 110 17.936 154.846 260.120 1.00 24.03 A C ANISOU 817 CG1 VAL A 110 2098 2491 4539 -175 -791 513 A C ATOM 818 CG2 VAL A 110 19.894 155.409 258.665 1.00 21.86 A C ANISOU 818 CG2 VAL A 110 1831 2229 4245 -256 -889 695 A C ATOM 819 N LYS A 111 16.783 157.845 261.154 1.00 26.33 A N ANISOU 819 N LYS A 111 2396 2499 5110 -31 -846 469 A N ATOM 820 CA LYS A 111 15.836 158.075 262.236 1.00 28.35 A C ANISOU 820 CA LYS A 111 2661 2701 5409 40 -789 355 A C ATOM 821 C LYS A 111 15.307 156.762 262.800 1.00 24.54 A C ANISOU 821 C LYS A 111 2174 2320 4832 32 -693 275 A C ATOM 822 O LYS A 111 14.904 155.868 262.058 1.00 23.33 A O ANISOU 822 O LYS A 111 1959 2275 4630 6 -679 313 A O ATOM 823 CB LYS A 111 14.658 158.893 261.692 1.00 29.31 A C ANISOU 823 CB LYS A 111 2701 2790 5646 113 -816 386 A C ATOM 824 CG LYS A 111 13.485 159.094 262.651 1.00 33.90 A C ANISOU 824 CG LYS A 111 3265 3335 6280 198 -746 275 A C ATOM 825 CD LYS A 111 13.788 159.949 263.866 1.00 38.48 A C ANISOU 825 CD LYS A 111 3931 3786 6904 243 -739 181 A C ATOM 826 CE LYS A 111 12.480 160.347 264.541 1.00 43.26 A C ANISOU 826 CE LYS A 111 4497 4358 7582 345 -677 89 A C ATOM 827 NZ LYS A 111 12.694 161.041 265.840 1.00 48.58 A N1+ ANISOU 827 NZ LYS A 111 5264 4919 8274 400 -655 -26 A N1+ ATOM 828 N VAL A 112 15.277 156.673 264.125 1.00 22.39 A N ANISOU 828 N VAL A 112 1968 2005 4533 56 -631 165 A N ATOM 829 CA VAL A 112 14.738 155.509 264.806 1.00 25.02 A C ANISOU 829 CA VAL A 112 2303 2421 4783 51 -532 91 A C ATOM 830 C VAL A 112 13.461 155.884 265.547 1.00 27.31 A C ANISOU 830 C VAL A 112 2560 2683 5133 136 -460 11 A C ATOM 831 O VAL A 112 13.474 156.753 266.419 1.00 26.87 A O ANISOU 831 O VAL A 112 2562 2530 5119 192 -453 -58 A O ATOM 832 CB VAL A 112 15.738 154.936 265.828 1.00 27.01 A C ANISOU 832 CB VAL A 112 2665 2665 4933 8 -504 28 A C ATOM 833 CG1 VAL A 112 15.129 153.747 266.559 1.00 26.16 A C ANISOU 833 CG1 VAL A 112 2561 2638 4741 3 -400 -38 A C ATOM 834 CG2 VAL A 112 17.033 154.531 265.146 1.00 24.70 A C ANISOU 834 CG2 VAL A 112 2397 2403 4586 -73 -569 102 A C ATOM 835 N VAL A 113 12.363 155.231 265.181 1.00 23.02 A N ANISOU 835 N VAL A 113 1922 2224 4599 147 -410 19 A N ATOM 836 CA VAL A 113 11.085 155.375 265.871 1.00 25.42 A C ANISOU 836 CA VAL A 113 2176 2525 4956 223 -323 -54 A C ATOM 837 C VAL A 113 10.851 154.149 266.752 1.00 29.16 A C ANISOU 837 C VAL A 113 2673 3076 5329 195 -212 -116 A C ATOM 838 O VAL A 113 10.893 152.994 266.287 1.00 28.22 A O ANISOU 838 O VAL A 113 2524 3050 5150 127 -203 -78 A O ATOM 839 CB VAL A 113 9.909 155.576 264.890 1.00 26.21 A C ANISOU 839 CB VAL A 113 2139 2659 5160 261 -345 0 A C ATOM 840 CG1 VAL A 113 8.590 155.680 265.640 1.00 28.60 A C ANISOU 840 CG1 VAL A 113 2377 2964 5524 340 -245 -76 A C ATOM 841 CG2 VAL A 113 10.140 156.814 264.027 1.00 25.03 A C ANISOU 841 CG2 VAL A 113 1973 2429 5109 290 -458 71 A C ATOM 842 N ASN A 114 10.673 154.404 268.043 1.00 27.54 A N ANISOU 842 N ASN A 114 2532 2829 5103 245 -131 -211 A N ATOM 843 CA ASN A 114 10.502 153.327 269.003 1.00 32.58 A C ANISOU 843 CA ASN A 114 3208 3532 5640 221 -21 -266 A C ATOM 844 C ASN A 114 9.038 153.005 269.288 1.00 31.58 A C ANISOU 844 C ASN A 114 2977 3462 5559 268 89 -294 A C ATOM 845 O ASN A 114 8.268 153.879 269.677 1.00 32.70 A O ANISOU 845 O ASN A 114 3085 3558 5781 358 129 -342 A O ATOM 846 CB ASN A 114 11.302 153.609 270.274 1.00 38.48 A C ANISOU 846 CB ASN A 114 4102 4216 6304 237 4 -348 A C ATOM 847 CG ASN A 114 12.804 153.470 270.049 1.00 44.45 A C ANISOU 847 CG ASN A 114 4950 4944 6995 164 -92 -314 A C ATOM 848 ND2 ASN A 114 13.488 154.598 269.897 1.00 42.28 A N ANISOU 848 ND2 ASN A 114 4719 4569 6775 186 -183 -310 A N ATOM 849 OD1 ASN A 114 13.336 152.360 269.996 1.00 45.78 A O ANISOU 849 OD1 ASN A 114 5145 5178 7073 89 -85 -289 A O ATOM 850 N GLY A 115 8.654 151.749 269.073 1.00 28.15 A N ANISOU 850 N GLY A 115 2487 3124 5084 207 136 -263 A N ATOM 851 CA GLY A 115 7.284 151.337 269.314 1.00 28.26 A C ANISOU 851 CA GLY A 115 2390 3197 5151 237 240 -279 A C ATOM 852 C GLY A 115 6.886 150.139 268.475 1.00 26.65 A C ANISOU 852 C GLY A 115 2091 3084 4952 160 227 -213 A C ATOM 853 O GLY A 115 7.698 149.581 267.734 1.00 26.64 A O ANISOU 853 O GLY A 115 2119 3104 4899 87 142 -162 A O ATOM 854 N LEU A 116 5.632 149.728 268.615 1.00 28.19 A N ANISOU 854 N LEU A 116 2170 3331 5211 178 313 -218 A N ATOM 855 CA LEU A 116 5.107 148.589 267.879 1.00 26.09 A C ANISOU 855 CA LEU A 116 1802 3144 4965 108 300 -163 A C ATOM 856 C LEU A 116 4.603 149.032 266.512 1.00 26.19 A C ANISOU 856 C LEU A 116 1698 3161 5093 125 190 -106 A C ATOM 857 O LEU A 116 3.670 149.829 266.424 1.00 26.41 A O ANISOU 857 O LEU A 116 1631 3167 5236 201 204 -115 A O ATOM 858 CB LEU A 116 3.934 147.975 268.644 1.00 28.00 A C ANISOU 858 CB LEU A 116 1959 3439 5242 117 441 -186 A C ATOM 859 CG LEU A 116 4.078 146.581 269.242 1.00 33.51 A C ANISOU 859 CG LEU A 116 2693 4192 5846 33 516 -181 A C ATOM 860 CD1 LEU A 116 2.708 146.044 269.611 1.00 26.98 A C ANISOU 860 CD1 LEU A 116 1731 3420 5099 37 633 -177 A C ATOM 861 CD2 LEU A 116 4.788 145.647 268.282 1.00 24.55 A C ANISOU 861 CD2 LEU A 116 1577 3085 4666 -62 404 -128 A C ATOM 862 N GLY A 117 5.190 148.502 265.445 1.00 27.21 A N ANISOU 862 N GLY A 117 1833 3319 5188 58 81 -48 A N ATOM 863 CA GLY A 117 4.748 148.866 264.112 1.00 31.14 A C ANISOU 863 CA GLY A 117 2230 3826 5774 72 -31 10 A C ATOM 864 C GLY A 117 3.780 147.837 263.550 1.00 34.48 A C ANISOU 864 C GLY A 117 2527 4324 6249 29 -34 36 A C ATOM 865 O GLY A 117 4.003 146.628 263.673 1.00 31.47 A O ANISOU 865 O GLY A 117 2168 3990 5799 -46 -12 36 A O ATOM 866 N LYS A 118 2.692 148.314 262.950 1.00 34.95 A N ANISOU 866 N LYS A 118 2476 4389 6416 78 -67 56 A N ATOM 867 CA LYS A 118 1.748 147.444 262.247 1.00 35.16 A C ANISOU 867 CA LYS A 118 2459 4478 6422 39 -96 81 A C ATOM 868 C LYS A 118 1.252 148.125 260.979 1.00 34.63 A C ANISOU 868 C LYS A 118 2365 4407 6386 76 -213 125 A C ATOM 869 O LYS A 118 1.015 149.338 260.965 1.00 35.40 A O ANISOU 869 O LYS A 118 2431 4451 6567 152 -228 128 A O ATOM 870 CB LYS A 118 0.587 147.032 263.159 1.00 36.64 A C ANISOU 870 CB LYS A 118 2559 4688 6673 50 30 47 A C ATOM 871 CG LYS A 118 1.032 146.062 264.250 1.00 41.94 A C ANISOU 871 CG LYS A 118 3267 5379 7287 -8 141 17 A C ATOM 872 CD LYS A 118 -0.015 145.804 265.306 1.00 44.64 A C ANISOU 872 CD LYS A 118 3532 5743 7687 10 289 -12 A C ATOM 873 CE LYS A 118 0.500 144.779 266.312 1.00 45.91 A C ANISOU 873 CE LYS A 118 3746 5925 7774 -57 395 -30 A C ATOM 874 NZ LYS A 118 -0.332 144.733 267.549 1.00 51.05 A N1+ ANISOU 874 NZ LYS A 118 4339 6591 8465 -26 568 -60 A N1+ ATOM 875 N PHE A 119 1.114 147.347 259.910 1.00 30.67 A N ANISOU 875 N PHE A 119 1881 3959 5815 26 -296 157 A N ATOM 876 CA PHE A 119 0.644 147.900 258.647 1.00 35.85 A C ANISOU 876 CA PHE A 119 2515 4618 6488 57 -406 199 A C ATOM 877 C PHE A 119 -0.822 148.285 258.761 1.00 36.28 A C ANISOU 877 C PHE A 119 2455 4668 6662 109 -379 189 A C ATOM 878 O PHE A 119 -1.597 147.622 259.454 1.00 39.05 A O ANISOU 878 O PHE A 119 2743 5044 7050 92 -294 159 A O ATOM 879 CB PHE A 119 0.845 146.902 257.501 1.00 33.33 A C ANISOU 879 CB PHE A 119 2242 4361 6062 -3 -493 221 A C ATOM 880 CG PHE A 119 2.288 146.694 257.117 1.00 28.67 A C ANISOU 880 CG PHE A 119 1763 3778 5350 -40 -537 238 A C ATOM 881 CD1 PHE A 119 2.902 147.523 256.190 1.00 29.75 A C ANISOU 881 CD1 PHE A 119 1948 3902 5456 -14 -623 285 A C ATOM 882 CD2 PHE A 119 3.028 145.664 257.683 1.00 28.23 A C ANISOU 882 CD2 PHE A 119 1766 3744 5216 -101 -490 210 A C ATOM 883 CE1 PHE A 119 4.236 147.332 255.833 1.00 27.97 A C ANISOU 883 CE1 PHE A 119 1819 3689 5119 -48 -655 305 A C ATOM 884 CE2 PHE A 119 4.356 145.466 257.336 1.00 31.12 A C ANISOU 884 CE2 PHE A 119 2231 4119 5472 -132 -527 223 A C ATOM 885 CZ PHE A 119 4.962 146.305 256.409 1.00 31.08 A C ANISOU 885 CZ PHE A 119 2268 4106 5437 -105 -607 270 A C ATOM 886 N THR A 120 -1.184 149.374 258.092 1.00 36.92 A N ANISOU 886 N THR A 120 2509 4716 6805 171 -449 219 A N ATOM 887 CA THR A 120 -2.570 149.808 258.005 1.00 36.28 A C ANISOU 887 CA THR A 120 2318 4629 6836 224 -445 215 A C ATOM 888 C THR A 120 -2.948 149.905 256.535 1.00 37.01 A C ANISOU 888 C THR A 120 2406 4745 6911 224 -578 263 A C ATOM 889 O THR A 120 -4.126 149.944 256.191 1.00 43.17 A O ANISOU 889 O THR A 120 3098 5538 7765 247 -600 265 A O ATOM 890 CB THR A 120 -2.798 151.169 258.699 1.00 34.69 A C ANISOU 890 CB THR A 120 2078 4354 6747 316 -399 198 A C ATOM 891 CG2 THR A 120 -2.629 151.041 260.200 1.00 31.42 A C ANISOU 891 CG2 THR A 120 1656 3925 6357 328 -253 138 A C ATOM 892 OG1 THR A 120 -1.846 152.118 258.207 1.00 37.74 A O ANISOU 892 OG1 THR A 120 2541 4687 7112 341 -478 234 A O ATOM 893 N GLY A 121 -1.938 149.958 255.668 1.00 36.25 A N ANISOU 893 N GLY A 121 2404 4655 6715 199 -664 302 A N ATOM 894 CA GLY A 121 -2.197 149.982 254.237 1.00 34.35 A C ANISOU 894 CA GLY A 121 2171 4446 6437 198 -785 346 A C ATOM 895 C GLY A 121 -0.989 149.574 253.410 1.00 36.00 A C ANISOU 895 C GLY A 121 2489 4688 6503 152 -850 375 A C ATOM 896 O GLY A 121 0.116 149.435 253.948 1.00 35.84 A O ANISOU 896 O GLY A 121 2540 4657 6421 124 -807 368 A O ATOM 897 N ALA A 122 -1.178 149.458 252.096 1.00 32.81 A N ANISOU 897 N ALA A 122 2097 4324 6047 149 -953 410 A N ATOM 898 CA ALA A 122 -0.119 148.996 251.200 1.00 33.47 A C ANISOU 898 CA ALA A 122 2276 4452 5987 111 -1012 434 A C ATOM 899 C ALA A 122 1.078 149.937 251.213 1.00 31.98 A C ANISOU 899 C ALA A 122 2164 4222 5765 126 -1018 481 A C ATOM 900 O ALA A 122 2.188 149.554 250.833 1.00 33.19 A O ANISOU 900 O ALA A 122 2402 4407 5803 90 -1032 496 A O ATOM 901 CB ALA A 122 -0.653 148.854 249.788 1.00 33.54 A C ANISOU 901 CB ALA A 122 2275 4509 5960 121 -1121 461 A C ATOM 902 N ASN A 123 0.849 151.162 251.672 1.00 28.99 A N ANISOU 902 N ASN A 123 1753 3770 5493 179 -1006 503 A N ATOM 903 CA ASN A 123 1.918 152.142 251.779 1.00 35.30 A C ANISOU 903 CA ASN A 123 2616 4513 6283 193 -1014 551 A C ATOM 904 C ASN A 123 1.885 152.836 253.130 1.00 33.28 A C ANISOU 904 C ASN A 123 2330 4175 6139 228 -935 518 A C ATOM 905 O ASN A 123 2.418 153.938 253.278 1.00 32.60 A O ANISOU 905 O ASN A 123 2271 4017 6098 260 -951 554 A O ATOM 906 CB ASN A 123 1.851 153.179 250.651 1.00 36.39 A C ANISOU 906 CB ASN A 123 2766 4631 6430 232 -1113 631 A C ATOM 907 CG ASN A 123 2.178 152.583 249.299 1.00 39.48 A C ANISOU 907 CG ASN A 123 3205 5104 6690 202 -1189 668 A C ATOM 908 ND2 ASN A 123 3.451 152.643 248.917 1.00 39.06 A N ANISOU 908 ND2 ASN A 123 3240 5066 6537 173 -1202 713 A N ATOM 909 OD1 ASN A 123 1.308 152.030 248.627 1.00 40.09 A O ANISOU 909 OD1 ASN A 123 3242 5234 6757 205 -1234 652 A O ATOM 910 N THR A 124 1.254 152.202 254.117 1.00 31.22 A N ANISOU 910 N THR A 124 2011 3923 5926 223 -848 448 A N ATOM 911 CA THR A 124 1.159 152.848 255.425 1.00 38.03 A C ANISOU 911 CA THR A 124 2840 4714 6895 266 -764 407 A C ATOM 912 C THR A 124 1.402 151.903 256.591 1.00 36.60 A C ANISOU 912 C THR A 124 2661 4556 6691 227 -656 341 A C ATOM 913 O THR A 124 0.738 150.856 256.714 1.00 37.89 A O ANISOU 913 O THR A 124 2783 4777 6836 193 -617 309 A O ATOM 914 CB THR A 124 -0.199 153.566 255.620 1.00 42.68 A C ANISOU 914 CB THR A 124 3327 5267 7623 340 -753 390 A C ATOM 915 CG2 THR A 124 -0.175 154.414 256.877 1.00 42.63 A C ANISOU 915 CG2 THR A 124 3298 5178 7720 401 -672 344 A C ATOM 916 OG1 THR A 124 -0.455 154.423 254.500 1.00 47.42 A O ANISOU 916 OG1 THR A 124 3928 5847 8245 374 -860 454 A O ATOM 917 N LEU A 125 2.343 152.304 257.447 1.00 32.29 A N ANISOU 917 N LEU A 125 2162 3957 6151 233 -612 324 A N ATOM 918 CA LEU A 125 2.681 151.564 258.660 1.00 31.10 A C ANISOU 918 CA LEU A 125 2018 3816 5984 202 -506 263 A C ATOM 919 C LEU A 125 2.428 152.461 259.868 1.00 28.27 A C ANISOU 919 C LEU A 125 1617 3380 5745 278 -424 210 A C ATOM 920 O LEU A 125 2.859 153.608 259.894 1.00 27.89 A O ANISOU 920 O LEU A 125 1592 3253 5751 330 -463 225 A O ATOM 921 CB LEU A 125 4.154 151.142 258.637 1.00 27.64 A C ANISOU 921 CB LEU A 125 1680 3386 5435 141 -526 278 A C ATOM 922 CG LEU A 125 4.685 150.351 259.839 1.00 29.53 A C ANISOU 922 CG LEU A 125 1941 3634 5644 101 -429 220 A C ATOM 923 CD1 LEU A 125 4.252 148.902 259.737 1.00 32.67 A C ANISOU 923 CD1 LEU A 125 2331 4113 5968 36 -397 202 A C ATOM 924 CD2 LEU A 125 6.193 150.422 259.936 1.00 30.57 A C ANISOU 924 CD2 LEU A 125 2166 3744 5706 64 -459 236 A C ATOM 925 N GLU A 126 1.738 151.933 260.871 1.00 29.81 A N ANISOU 925 N GLU A 126 1753 3596 5978 285 -308 148 A N ATOM 926 CA GLU A 126 1.375 152.713 262.049 1.00 32.45 A C ANISOU 926 CA GLU A 126 2046 3868 6416 370 -209 83 A C ATOM 927 C GLU A 126 2.153 152.216 263.261 1.00 34.65 A C ANISOU 927 C GLU A 126 2397 4144 6625 342 -103 23 A C ATOM 928 O GLU A 126 2.184 151.016 263.539 1.00 27.47 A O ANISOU 928 O GLU A 126 1492 3301 5645 271 -47 15 A O ATOM 929 CB GLU A 126 -0.132 152.621 262.305 1.00 33.71 A C ANISOU 929 CB GLU A 126 2100 4058 6652 410 -138 56 A C ATOM 930 CG GLU A 126 -0.644 153.553 263.385 1.00 39.94 A C ANISOU 930 CG GLU A 126 2846 4785 7543 515 -37 -13 A C ATOM 931 CD GLU A 126 -2.155 153.699 263.362 1.00 47.89 A C ANISOU 931 CD GLU A 126 3744 5818 8633 563 3 -23 A C ATOM 932 OE1 GLU A 126 -2.800 153.365 264.379 1.00 53.21 A O ANISOU 932 OE1 GLU A 126 4368 6522 9330 586 143 -78 A O ATOM 933 OE2 GLU A 126 -2.700 154.133 262.325 1.00 47.97 A O1- ANISOU 933 OE2 GLU A 126 3720 5824 8684 577 -103 27 A O1- ATOM 934 N VAL A 127 2.804 153.138 263.967 1.00 32.80 A N ANISOU 934 N VAL A 127 2268 3829 6366 390 -80 -18 A N ATOM 935 CA VAL A 127 3.643 152.765 265.099 1.00 32.77 A C ANISOU 935 CA VAL A 127 2396 3816 6237 359 6 -76 A C ATOM 936 C VAL A 127 3.046 153.261 266.407 1.00 37.82 A C ANISOU 936 C VAL A 127 3041 4422 6909 442 138 -165 A C ATOM 937 O VAL A 127 2.688 154.436 266.529 1.00 36.03 A O ANISOU 937 O VAL A 127 2794 4122 6774 536 127 -193 A O ATOM 938 CB VAL A 127 5.060 153.337 264.970 1.00 29.66 A C ANISOU 938 CB VAL A 127 2144 3357 5769 338 -77 -60 A C ATOM 939 CG1 VAL A 127 5.944 152.821 266.107 1.00 26.25 A C ANISOU 939 CG1 VAL A 127 1847 2923 5205 299 0 -118 A C ATOM 940 CG2 VAL A 127 5.655 152.982 263.619 1.00 27.75 A C ANISOU 940 CG2 VAL A 127 1896 3152 5497 269 -202 32 A C ATOM 941 N GLU A 128 2.900 152.356 267.371 1.00 37.92 A N ANISOU 941 N GLU A 128 3077 4488 6845 411 263 -209 A N ATOM 942 CA GLU A 128 2.396 152.735 268.684 1.00 38.74 A C ANISOU 942 CA GLU A 128 3198 4572 6949 489 403 -296 A C ATOM 943 C GLU A 128 3.566 152.666 269.671 1.00 37.05 A C ANISOU 943 C GLU A 128 3166 4325 6585 467 435 -347 A C ATOM 944 O GLU A 128 4.103 151.585 269.944 1.00 34.97 A O ANISOU 944 O GLU A 128 2965 4114 6209 382 463 -334 A O ATOM 945 CB GLU A 128 1.264 151.788 269.072 1.00 39.91 A C ANISOU 945 CB GLU A 128 3229 4810 7126 474 530 -299 A C ATOM 946 CG GLU A 128 0.554 152.092 270.368 1.00 48.94 A C ANISOU 946 CG GLU A 128 4364 5956 8274 559 695 -380 A C ATOM 947 CD GLU A 128 -0.733 151.297 270.488 1.00 53.75 A C ANISOU 947 CD GLU A 128 4812 6652 8958 548 807 -361 A C ATOM 948 OE1 GLU A 128 -0.965 150.404 269.642 1.00 54.21 A O ANISOU 948 OE1 GLU A 128 4783 6764 9049 463 749 -290 A O ATOM 949 OE2 GLU A 128 -1.517 151.575 271.415 1.00 54.25 A O1- ANISOU 949 OE2 GLU A 128 4832 6729 9050 625 950 -418 A O1- ATOM 950 N GLY A 129 3.992 153.826 270.167 1.00 36.02 A N ANISOU 950 N GLY A 129 3124 4103 6460 543 417 -405 A N ATOM 951 CA GLY A 129 5.161 153.899 271.028 1.00 32.87 A C ANISOU 951 CA GLY A 129 2901 3659 5931 526 419 -455 A C ATOM 952 C GLY A 129 5.182 155.021 272.050 1.00 33.24 A C ANISOU 952 C GLY A 129 3030 3619 5980 633 462 -556 A C ATOM 953 O GLY A 129 4.150 155.607 272.385 1.00 31.45 A O ANISOU 953 O GLY A 129 2728 3383 5840 730 536 -605 A O ATOM 954 N GLU A 130 6.387 155.309 272.542 1.00 30.16 A N ANISOU 954 N GLU A 130 2797 3165 5497 615 409 -591 A N ATOM 955 CA GLU A 130 6.620 156.315 273.573 1.00 35.49 A C ANISOU 955 CA GLU A 130 3581 3748 6153 708 430 -696 A C ATOM 956 C GLU A 130 6.075 157.681 273.159 1.00 36.69 A C ANISOU 956 C GLU A 130 3669 3808 6462 809 373 -716 A C ATOM 957 O GLU A 130 5.594 158.445 273.998 1.00 33.04 A O ANISOU 957 O GLU A 130 3234 3296 6024 919 437 -815 A O ATOM 958 CB GLU A 130 8.106 156.416 273.941 1.00 40.36 A C ANISOU 958 CB GLU A 130 4367 4302 6667 657 344 -715 A C ATOM 959 CG GLU A 130 9.036 156.691 272.771 1.00 54.05 A C ANISOU 959 CG GLU A 130 6098 5988 8452 588 182 -624 A C ATOM 960 CD GLU A 130 10.502 156.459 273.120 1.00 67.83 A C ANISOU 960 CD GLU A 130 7987 7698 10086 517 113 -629 A C ATOM 961 OE1 GLU A 130 10.802 156.156 274.299 1.00 70.46 A O ANISOU 961 OE1 GLU A 130 8433 8036 10304 527 179 -707 A O ATOM 962 OE2 GLU A 130 11.356 156.581 272.214 1.00 69.36 A O1- ANISOU 962 OE2 GLU A 130 8181 7864 10309 452 -7 -551 A O1- ATOM 963 N ASN A 131 6.167 157.990 271.869 1.00 32.62 A N ANISOU 963 N ASN A 131 3075 3268 6050 777 250 -623 A N ATOM 964 CA ASN A 131 5.721 159.286 271.380 1.00 36.43 A C ANISOU 964 CA ASN A 131 3500 3653 6687 866 177 -625 A C ATOM 965 C ASN A 131 4.308 159.201 270.830 1.00 39.27 A C ANISOU 965 C ASN A 131 3681 4072 7166 914 227 -595 A C ATOM 966 O ASN A 131 3.921 160.012 269.987 1.00 43.03 A O ANISOU 966 O ASN A 131 4077 4492 7780 958 138 -551 A O ATOM 967 CB ASN A 131 6.636 159.749 270.240 1.00 38.66 A C ANISOU 967 CB ASN A 131 3799 3872 7017 804 8 -528 A C ATOM 968 CG ASN A 131 8.056 160.041 270.696 1.00 45.80 A C ANISOU 968 CG ASN A 131 4864 4698 7840 762 -62 -552 A C ATOM 969 ND2 ASN A 131 8.972 160.131 269.740 1.00 41.70 A N ANISOU 969 ND2 ASN A 131 4359 4154 7333 683 -187 -454 A N ATOM 970 OD1 ASN A 131 8.331 160.161 271.889 1.00 53.31 A O ANISOU 970 OD1 ASN A 131 5925 5616 8716 800 -4 -656 A O ATOM 971 N GLY A 132 3.528 158.232 271.304 1.00 38.25 A N ANISOU 971 N GLY A 132 3488 4053 6991 905 364 -614 A N ATOM 972 CA GLY A 132 2.154 158.117 270.852 1.00 33.97 A C ANISOU 972 CA GLY A 132 2767 3569 6573 949 416 -589 A C ATOM 973 C GLY A 132 2.087 157.331 269.558 1.00 39.10 A C ANISOU 973 C GLY A 132 3318 4288 7250 851 333 -469 A C ATOM 974 O GLY A 132 2.827 156.358 269.360 1.00 37.79 A O ANISOU 974 O GLY A 132 3208 4178 6973 741 313 -423 A O ATOM 975 N LYS A 133 1.185 157.757 268.679 1.00 36.68 A N ANISOU 975 N LYS A 133 2867 3978 7093 895 280 -423 A N ATOM 976 CA LYS A 133 0.940 157.071 267.422 1.00 38.82 A C ANISOU 976 CA LYS A 133 3033 4317 7401 817 197 -317 A C ATOM 977 C LYS A 133 1.680 157.845 266.337 1.00 39.97 A C ANISOU 977 C LYS A 133 3217 4388 7583 803 24 -242 A C ATOM 978 O LYS A 133 1.549 159.068 266.242 1.00 40.44 A O ANISOU 978 O LYS A 133 3274 4347 7743 890 -33 -256 A O ATOM 979 CB LYS A 133 -0.563 157.088 267.122 1.00 40.83 A C ANISOU 979 CB LYS A 133 3098 4613 7803 880 238 -310 A C ATOM 980 CG LYS A 133 -0.955 156.594 265.733 1.00 43.23 A C ANISOU 980 CG LYS A 133 3282 4972 8170 820 127 -206 A C ATOM 981 CD LYS A 133 -2.466 156.671 265.553 1.00 53.10 A C ANISOU 981 CD LYS A 133 4418 6267 9489 858 162 -202 A C ATOM 982 CE LYS A 133 -3.182 155.785 266.563 1.00 57.16 A C ANISOU 982 CE LYS A 133 4878 6864 9978 851 334 -255 A C ATOM 983 NZ LYS A 133 -4.660 155.809 266.379 1.00 60.21 A N1+ ANISOU 983 NZ LYS A 133 5143 7297 10436 883 365 -244 A N1+ ATOM 984 N THR A 134 2.426 157.132 265.498 1.00 31.04 A N ANISOU 984 N THR A 134 2116 3304 6373 697 -59 -161 A N ATOM 985 CA THR A 134 3.156 157.757 264.398 1.00 33.50 A C ANISOU 985 CA THR A 134 2460 3562 6705 673 -214 -74 A C ATOM 986 C THR A 134 2.764 157.065 263.106 1.00 36.90 A C ANISOU 986 C THR A 134 2788 4079 7154 616 -291 21 A C ATOM 987 O THR A 134 2.960 155.853 262.965 1.00 32.98 A O ANISOU 987 O THR A 134 2293 3674 6564 530 -266 38 A O ATOM 988 CB THR A 134 4.688 157.620 264.563 1.00 33.78 A C ANISOU 988 CB THR A 134 2653 3573 6610 596 -252 -63 A C ATOM 989 CG2 THR A 134 5.413 158.365 263.458 1.00 29.04 A C ANISOU 989 CG2 THR A 134 2079 2915 6041 577 -400 33 A C ATOM 990 OG1 THR A 134 5.102 158.153 265.829 1.00 33.52 A O ANISOU 990 OG1 THR A 134 2727 3464 6545 643 -185 -160 A O ATOM 991 N VAL A 135 2.256 157.834 262.147 1.00 35.69 A N ANISOU 991 N VAL A 135 2553 3889 7117 663 -395 84 A N ATOM 992 CA VAL A 135 1.843 157.261 260.874 1.00 35.45 A C ANISOU 992 CA VAL A 135 2489 3945 7037 598 -470 168 A C ATOM 993 C VAL A 135 2.959 157.463 259.859 1.00 35.84 A C ANISOU 993 C VAL A 135 2622 3983 7014 539 -592 260 A C ATOM 994 O VAL A 135 3.364 158.594 259.572 1.00 35.28 A O ANISOU 994 O VAL A 135 2592 3821 6991 576 -666 298 A O ATOM 995 CB VAL A 135 0.549 157.908 260.353 1.00 38.86 A C ANISOU 995 CB VAL A 135 2842 4366 7556 659 -500 182 A C ATOM 996 CG1 VAL A 135 0.178 157.324 259.000 1.00 32.01 A C ANISOU 996 CG1 VAL A 135 1955 3581 6626 596 -586 261 A C ATOM 997 CG2 VAL A 135 -0.582 157.687 261.339 1.00 38.09 A C ANISOU 997 CG2 VAL A 135 2656 4291 7524 715 -371 96 A C ATOM 998 N ILE A 136 3.470 156.354 259.336 1.00 33.36 A N ANISOU 998 N ILE A 136 2337 3759 6580 447 -607 295 A N ATOM 999 CA ILE A 136 4.581 156.396 258.404 1.00 31.59 A C ANISOU 999 CA ILE A 136 2195 3543 6265 387 -702 380 A C ATOM 1000 C ILE A 136 4.118 155.983 257.019 1.00 32.95 A C ANISOU 1000 C ILE A 136 2357 3795 6368 351 -773 447 A C ATOM 1001 O ILE A 136 3.752 154.820 256.798 1.00 31.74 A O ANISOU 1001 O ILE A 136 2185 3733 6142 304 -747 429 A O ATOM 1002 CB ILE A 136 5.724 155.455 258.847 1.00 34.54 A C ANISOU 1002 CB ILE A 136 2629 3957 6537 313 -668 363 A C ATOM 1003 CG1 ILE A 136 6.215 155.814 260.251 1.00 29.03 A C ANISOU 1003 CG1 ILE A 136 2000 3185 5847 338 -583 279 A C ATOM 1004 CG2 ILE A 136 6.878 155.498 257.854 1.00 29.50 A C ANISOU 1004 CG2 ILE A 136 2075 3336 5800 253 -756 451 A C ATOM 1005 CD1 ILE A 136 7.428 155.010 260.698 1.00 27.48 A C ANISOU 1005 CD1 ILE A 136 1916 3019 5506 256 -547 259 A C ATOM 1006 N ASN A 137 4.147 156.945 256.096 1.00 35.75 A N ANISOU 1006 N ASN A 137 2730 4108 6745 374 -864 522 A N ATOM 1007 CA ASN A 137 3.829 156.708 254.695 1.00 33.66 A C ANISOU 1007 CA ASN A 137 2467 3912 6411 349 -942 591 A C ATOM 1008 C ASN A 137 5.140 156.417 253.969 1.00 34.05 A C ANISOU 1008 C ASN A 137 2607 3998 6331 282 -987 658 A C ATOM 1009 O ASN A 137 6.067 157.224 254.014 1.00 32.60 A O ANISOU 1009 O ASN A 137 2478 3748 6160 280 -1015 705 A O ATOM 1010 CB ASN A 137 3.166 157.950 254.087 1.00 36.93 A C ANISOU 1010 CB ASN A 137 2852 4261 6919 412 -1014 641 A C ATOM 1011 CG ASN A 137 1.844 158.307 254.757 1.00 43.85 A C ANISOU 1011 CG ASN A 137 3634 5101 7928 485 -969 575 A C ATOM 1012 ND2 ASN A 137 1.733 159.545 255.228 1.00 44.95 A N ANISOU 1012 ND2 ASN A 137 3766 5131 8183 554 -976 568 A N ATOM 1013 OD1 ASN A 137 0.943 157.475 254.864 1.00 48.89 A O ANISOU 1013 OD1 ASN A 137 4205 5806 8563 481 -927 529 A O ATOM 1014 N PHE A 138 5.213 155.272 253.294 1.00 33.31 A N ANISOU 1014 N PHE A 138 2532 4010 6117 229 -993 660 A N ATOM 1015 CA PHE A 138 6.462 154.825 252.680 1.00 31.41 A C ANISOU 1015 CA PHE A 138 2374 3818 5742 168 -1017 708 A C ATOM 1016 C PHE A 138 6.296 154.493 251.198 1.00 31.45 A C ANISOU 1016 C PHE A 138 2394 3904 5651 154 -1087 763 A C ATOM 1017 O PHE A 138 5.181 154.238 250.729 1.00 34.75 A O ANISOU 1017 O PHE A 138 2757 4356 6088 177 -1113 746 A O ATOM 1018 CB PHE A 138 7.023 153.607 253.423 1.00 25.29 A C ANISOU 1018 CB PHE A 138 1625 3092 4892 115 -945 641 A C ATOM 1019 CG PHE A 138 6.075 152.444 253.480 1.00 25.30 A C ANISOU 1019 CG PHE A 138 1579 3164 4869 102 -911 575 A C ATOM 1020 CD1 PHE A 138 5.996 151.539 252.428 1.00 25.17 A C ANISOU 1020 CD1 PHE A 138 1581 3238 4745 71 -950 584 A C ATOM 1021 CD2 PHE A 138 5.269 152.245 254.595 1.00 25.53 A C ANISOU 1021 CD2 PHE A 138 1543 3169 4989 123 -837 503 A C ATOM 1022 CE1 PHE A 138 5.115 150.467 252.480 1.00 33.61 A C ANISOU 1022 CE1 PHE A 138 2606 4361 5802 56 -927 525 A C ATOM 1023 CE2 PHE A 138 4.396 151.171 254.663 1.00 25.64 A C ANISOU 1023 CE2 PHE A 138 1511 3244 4988 103 -803 452 A C ATOM 1024 CZ PHE A 138 4.318 150.279 253.603 1.00 31.37 A C ANISOU 1024 CZ PHE A 138 2256 4050 5612 67 -854 464 A C ATOM 1025 N ASP A 139 7.407 154.508 250.465 1.00 27.98 A N ANISOU 1025 N ASP A 139 2025 3495 5109 118 -1119 830 A N ATOM 1026 CA ASP A 139 7.423 153.999 249.099 1.00 31.36 A C ANISOU 1026 CA ASP A 139 2478 4016 5423 103 -1175 870 A C ATOM 1027 C ASP A 139 7.772 152.516 249.140 1.00 31.71 A C ANISOU 1027 C ASP A 139 2547 4147 5353 57 -1136 804 A C ATOM 1028 O ASP A 139 7.241 151.717 248.367 1.00 33.40 A O ANISOU 1028 O ASP A 139 2750 4436 5502 55 -1167 781 A O ATOM 1029 CB ASP A 139 8.441 154.757 248.248 1.00 38.11 A C ANISOU 1029 CB ASP A 139 3391 4866 6223 91 -1221 979 A C ATOM 1030 CG ASP A 139 8.137 156.243 248.156 1.00 47.29 A C ANISOU 1030 CG ASP A 139 4535 5933 7500 133 -1266 1051 A C ATOM 1031 OD1 ASP A 139 6.958 156.621 248.327 1.00 49.79 A O ANISOU 1031 OD1 ASP A 139 4790 6211 7916 181 -1284 1023 A O ATOM 1032 OD2 ASP A 139 9.082 157.033 247.935 1.00 48.34 A O1- ANISOU 1032 OD2 ASP A 139 4713 6026 7629 116 -1283 1136 A O1- ATOM 1033 N ASN A 140 8.671 152.163 250.051 1.00 32.08 A N ANISOU 1033 N ASN A 140 2630 4178 5380 21 -1073 772 A N ATOM 1034 CA ASN A 140 9.071 150.777 250.258 1.00 34.99 A C ANISOU 1034 CA ASN A 140 3028 4615 5652 -23 -1030 704 A C ATOM 1035 C ASN A 140 9.139 150.425 251.737 1.00 33.80 A C ANISOU 1035 C ASN A 140 2867 4421 5555 -40 -951 632 A C ATOM 1036 O ASN A 140 9.522 151.256 252.563 1.00 30.96 A O ANISOU 1036 O ASN A 140 2509 3984 5272 -29 -928 644 A O ATOM 1037 CB ASN A 140 10.430 150.504 249.612 1.00 32.81 A C ANISOU 1037 CB ASN A 140 2826 4388 5251 -58 -1040 749 A C ATOM 1038 CG ASN A 140 10.406 150.671 248.108 1.00 33.78 A C ANISOU 1038 CG ASN A 140 2962 4571 5300 -42 -1111 816 A C ATOM 1039 ND2 ASN A 140 9.906 149.661 247.410 1.00 31.52 A N ANISOU 1039 ND2 ASN A 140 2671 4363 4941 -41 -1137 769 A N ATOM 1040 OD1 ASN A 140 10.829 151.699 247.580 1.00 37.54 A O ANISOU 1040 OD1 ASN A 140 3455 5023 5786 -31 -1146 910 A O ATOM 1041 N ALA A 141 8.760 149.194 252.068 1.00 33.66 A N ANISOU 1041 N ALA A 141 2839 4450 5500 -65 -913 556 A N ATOM 1042 CA ALA A 141 8.864 148.705 253.437 1.00 30.35 A C ANISOU 1042 CA ALA A 141 2415 4002 5114 -88 -834 490 A C ATOM 1043 C ALA A 141 9.723 147.447 253.477 1.00 30.46 A C ANISOU 1043 C ALA A 141 2492 4072 5010 -141 -808 452 A C ATOM 1044 O ALA A 141 9.637 146.596 252.596 1.00 28.59 A O ANISOU 1044 O ALA A 141 2270 3904 4691 -155 -839 440 A O ATOM 1045 CB ALA A 141 7.488 148.419 254.005 1.00 22.54 A C ANISOU 1045 CB ALA A 141 1345 3005 4213 -70 -799 437 A C ATOM 1046 N ILE A 142 10.530 147.318 254.521 1.00 28.46 A N ANISOU 1046 N ILE A 142 2274 3785 4753 -168 -754 427 A N ATOM 1047 CA ILE A 142 11.336 146.126 254.703 1.00 23.94 A C ANISOU 1047 CA ILE A 142 1761 3255 4079 -216 -726 385 A C ATOM 1048 C ILE A 142 10.948 145.488 256.028 1.00 23.17 A C ANISOU 1048 C ILE A 142 1645 3135 4025 -239 -654 319 A C ATOM 1049 O ILE A 142 11.191 146.047 257.102 1.00 21.25 A O ANISOU 1049 O ILE A 142 1397 2830 3846 -236 -614 310 A O ATOM 1050 CB ILE A 142 12.858 146.423 254.669 1.00 26.58 A C ANISOU 1050 CB ILE A 142 2168 3581 4351 -236 -732 421 A C ATOM 1051 CG1 ILE A 142 13.252 147.129 253.369 1.00 26.16 A C ANISOU 1051 CG1 ILE A 142 2128 3552 4261 -217 -795 501 A C ATOM 1052 CG2 ILE A 142 13.658 145.137 254.801 1.00 17.89 A C ANISOU 1052 CG2 ILE A 142 1127 2525 3147 -278 -706 373 A C ATOM 1053 CD1 ILE A 142 14.760 147.454 253.268 1.00 18.61 A C ANISOU 1053 CD1 ILE A 142 1232 2590 3249 -240 -796 549 A C ATOM 1054 N ILE A 143 10.299 144.333 255.934 1.00 19.16 A N ANISOU 1054 N ILE A 143 1121 2672 3488 -260 -641 274 A N ATOM 1055 CA ILE A 143 9.860 143.591 257.101 1.00 19.06 A C ANISOU 1055 CA ILE A 143 1088 2645 3510 -288 -570 221 A C ATOM 1056 C ILE A 143 10.987 142.716 257.633 1.00 23.13 A C ANISOU 1056 C ILE A 143 1682 3166 3940 -336 -543 192 A C ATOM 1057 O ILE A 143 11.478 141.819 256.940 1.00 23.51 A O ANISOU 1057 O ILE A 143 1777 3261 3895 -356 -572 179 A O ATOM 1058 CB ILE A 143 8.644 142.711 256.765 1.00 25.95 A C ANISOU 1058 CB ILE A 143 1905 3556 4398 -296 -573 194 A C ATOM 1059 CG1 ILE A 143 7.476 143.586 256.291 1.00 20.67 A C ANISOU 1059 CG1 ILE A 143 1153 2878 3821 -247 -601 220 A C ATOM 1060 CG2 ILE A 143 8.223 141.895 257.973 1.00 21.29 A C ANISOU 1060 CG2 ILE A 143 1294 2952 3841 -333 -494 151 A C ATOM 1061 CD1 ILE A 143 6.300 142.802 255.746 1.00 21.37 A C ANISOU 1061 CD1 ILE A 143 1187 3008 3926 -254 -624 201 A C ATOM 1062 N ALA A 144 11.394 142.978 258.870 1.00 24.39 A N ANISOU 1062 N ALA A 144 1854 3276 4137 -349 -488 177 A N ATOM 1063 CA ALA A 144 12.486 142.232 259.478 1.00 22.48 A C ANISOU 1063 CA ALA A 144 1690 3031 3822 -393 -466 151 A C ATOM 1064 C ALA A 144 12.190 142.011 260.953 1.00 21.00 A C ANISOU 1064 C ALA A 144 1485 2801 3694 -417 -388 114 A C ATOM 1065 O ALA A 144 13.032 142.278 261.811 1.00 21.77 A O ANISOU 1065 O ALA A 144 1633 2854 3782 -430 -363 102 A O ATOM 1066 CB ALA A 144 13.791 142.997 259.301 1.00 16.59 A C ANISOU 1066 CB ALA A 144 1003 2262 3038 -387 -499 183 A C ATOM 1067 N ALA A 145 11.000 141.489 261.237 1.00 19.33 A N ANISOU 1067 N ALA A 145 1209 2603 3533 -422 -344 95 A N ATOM 1068 CA ALA A 145 10.497 141.446 262.607 1.00 18.11 A C ANISOU 1068 CA ALA A 145 1019 2412 3451 -433 -248 65 A C ATOM 1069 C ALA A 145 10.845 140.152 263.342 1.00 22.63 A C ANISOU 1069 C ALA A 145 1650 2990 3957 -493 -203 38 A C ATOM 1070 O ALA A 145 10.361 139.916 264.451 1.00 18.15 A O ANISOU 1070 O ALA A 145 1091 2407 3400 -499 -107 14 A O ATOM 1071 CB ALA A 145 8.990 141.692 262.631 1.00 19.14 A C ANISOU 1071 CB ALA A 145 1039 2550 3682 -400 -206 65 A C ATOM 1072 N GLY A 146 11.650 139.300 262.711 1.00 22.05 A N ANISOU 1072 N GLY A 146 1642 2946 3790 -526 -265 40 A N ATOM 1073 CA GLY A 146 12.266 138.179 263.409 1.00 17.95 A C ANISOU 1073 CA GLY A 146 1190 2419 3210 -581 -240 18 A C ATOM 1074 C GLY A 146 11.404 137.013 263.876 1.00 17.51 A C ANISOU 1074 C GLY A 146 1108 2375 3172 -623 -190 7 A C ATOM 1075 O GLY A 146 10.322 136.745 263.343 1.00 17.69 A O ANISOU 1075 O GLY A 146 1063 2427 3230 -615 -195 14 A O ATOM 1076 N SER A 147 11.900 136.328 264.905 1.00 16.88 A N ANISOU 1076 N SER A 147 1084 2266 3063 -669 -142 -7 A N ATOM 1077 CA SER A 147 11.241 135.147 265.447 1.00 20.01 A C ANISOU 1077 CA SER A 147 1465 2664 3474 -721 -93 -7 A C ATOM 1078 C SER A 147 11.213 135.209 266.976 1.00 22.84 A C ANISOU 1078 C SER A 147 1886 2991 3802 -724 24 -14 A C ATOM 1079 O SER A 147 11.676 136.184 267.579 1.00 22.71 A O ANISOU 1079 O SER A 147 1933 2951 3744 -678 59 -30 A O ATOM 1080 CB SER A 147 11.969 133.875 264.988 1.00 20.42 A C ANISOU 1080 CB SER A 147 1596 2728 3435 -755 -160 -17 A C ATOM 1081 OG SER A 147 13.327 133.853 265.425 1.00 22.90 A O ANISOU 1081 OG SER A 147 2006 3013 3683 -767 -179 -29 A O ATOM 1082 N ARG A 148 10.690 134.151 267.591 1.00 23.43 A N ANISOU 1082 N ARG A 148 1952 3064 3889 -777 79 -3 A N ATOM 1083 CA ARG A 148 10.556 134.074 269.043 1.00 26.94 A C ANISOU 1083 CA ARG A 148 2460 3488 4288 -782 199 -2 A C ATOM 1084 C ARG A 148 10.576 132.599 269.449 1.00 28.81 A C ANISOU 1084 C ARG A 148 2726 3714 4505 -858 209 20 A C ATOM 1085 O ARG A 148 10.312 131.732 268.622 1.00 27.64 A O ANISOU 1085 O ARG A 148 2514 3574 4413 -904 139 32 A O ATOM 1086 CB ARG A 148 9.247 134.747 269.469 1.00 19.77 A C ANISOU 1086 CB ARG A 148 1455 2597 3458 -746 305 6 A C ATOM 1087 CG ARG A 148 8.014 133.981 269.018 1.00 30.04 A C ANISOU 1087 CG ARG A 148 2616 3924 4873 -793 316 37 A C ATOM 1088 CD ARG A 148 6.720 134.701 269.359 1.00 29.72 A C ANISOU 1088 CD ARG A 148 2462 3904 4924 -751 419 45 A C ATOM 1089 NE ARG A 148 5.557 133.893 268.991 1.00 33.15 A N ANISOU 1089 NE ARG A 148 2777 4365 5455 -795 421 79 A N ATOM 1090 CZ ARG A 148 5.010 133.883 267.776 1.00 36.38 A C ANISOU 1090 CZ ARG A 148 3129 4798 5894 -776 311 81 A C ATOM 1091 NH1 ARG A 148 5.523 134.629 266.803 1.00 31.23 A N1+ ANISOU 1091 NH1 ARG A 148 2493 4148 5227 -729 211 60 A N1+ ATOM 1092 NH2 ARG A 148 3.956 133.119 267.527 1.00 33.93 A N ANISOU 1092 NH2 ARG A 148 2754 4510 5628 -805 305 105 A N ATOM 1093 N PRO A 149 10.872 132.308 270.727 1.00 30.47 A N ANISOU 1093 N PRO A 149 3036 3903 4637 -872 291 26 A N ATOM 1094 CA PRO A 149 10.949 130.903 271.167 1.00 24.02 A C ANISOU 1094 CA PRO A 149 2258 3068 3801 -946 297 56 A C ATOM 1095 C PRO A 149 9.619 130.148 271.150 1.00 26.27 A C ANISOU 1095 C PRO A 149 2423 3367 4191 -1000 353 99 A C ATOM 1096 O PRO A 149 8.563 130.735 271.378 1.00 24.77 A O ANISOU 1096 O PRO A 149 2141 3204 4065 -976 443 110 A O ATOM 1097 CB PRO A 149 11.466 131.015 272.607 1.00 25.47 A C ANISOU 1097 CB PRO A 149 2575 3230 3870 -935 383 57 A C ATOM 1098 CG PRO A 149 12.142 132.361 272.677 1.00 27.56 A C ANISOU 1098 CG PRO A 149 2899 3493 4082 -858 368 11 A C ATOM 1099 CD PRO A 149 11.340 133.244 271.768 1.00 26.71 A C ANISOU 1099 CD PRO A 149 2661 3413 4076 -817 359 2 A C ATOM 1100 N ILE A 150 9.682 128.846 270.882 1.00 24.92 A N ANISOU 1100 N ILE A 150 2249 3173 4046 -1073 296 121 A N ATOM 1101 CA ILE A 150 8.502 127.993 270.939 1.00 23.96 A C ANISOU 1101 CA ILE A 150 2031 3058 4015 -1130 337 168 A C ATOM 1102 C ILE A 150 8.076 127.740 272.384 1.00 29.42 A C ANISOU 1102 C ILE A 150 2751 3742 4684 -1163 492 218 A C ATOM 1103 O ILE A 150 8.906 127.434 273.241 1.00 26.76 A O ANISOU 1103 O ILE A 150 2553 3381 4235 -1170 513 225 A O ATOM 1104 CB ILE A 150 8.747 126.634 270.238 1.00 26.29 A C ANISOU 1104 CB ILE A 150 2363 3334 4290 -1174 215 162 A C ATOM 1105 CG1 ILE A 150 8.790 126.816 268.715 1.00 30.11 A C ANISOU 1105 CG1 ILE A 150 2816 3848 4776 -1124 91 105 A C ATOM 1106 CG2 ILE A 150 7.664 125.629 270.607 1.00 22.99 A C ANISOU 1106 CG2 ILE A 150 1894 2913 3926 -1233 265 208 A C ATOM 1107 CD1 ILE A 150 9.182 125.563 267.933 1.00 23.84 A C ANISOU 1107 CD1 ILE A 150 2070 3030 3959 -1141 -12 67 A C ATOM 1108 N GLN A 151 6.784 127.905 272.657 1.00 31.05 A N ANISOU 1108 N GLN A 151 2846 3983 4971 -1165 593 253 A N ATOM 1109 CA GLN A 151 6.215 127.516 273.940 1.00 31.78 A C ANISOU 1109 CA GLN A 151 2948 4080 5048 -1201 748 313 A C ATOM 1110 C GLN A 151 5.278 126.332 273.716 1.00 36.21 A C ANISOU 1110 C GLN A 151 3443 4649 5668 -1262 712 367 A C ATOM 1111 O GLN A 151 4.701 126.196 272.633 1.00 33.96 A O ANISOU 1111 O GLN A 151 3075 4380 5448 -1255 611 342 A O ATOM 1112 CB GLN A 151 5.458 128.691 274.561 1.00 30.17 A C ANISOU 1112 CB GLN A 151 2691 3925 4849 -1132 895 304 A C ATOM 1113 CG GLN A 151 6.345 129.611 275.393 1.00 37.62 A C ANISOU 1113 CG GLN A 151 3788 4870 5636 -1054 938 259 A C ATOM 1114 CD GLN A 151 5.630 130.865 275.869 1.00 39.48 A C ANISOU 1114 CD GLN A 151 3974 5149 5878 -968 1061 233 A C ATOM 1115 NE2 GLN A 151 6.403 131.878 276.243 1.00 39.94 A N ANISOU 1115 NE2 GLN A 151 4145 5200 5828 -889 1057 173 A N ATOM 1116 OE1 GLN A 151 4.401 130.923 275.898 1.00 42.68 A O ANISOU 1116 OE1 GLN A 151 4237 5590 6389 -972 1155 263 A O ATOM 1117 N LEU A 152 5.136 125.479 274.732 1.00 39.45 A N ANISOU 1117 N LEU A 152 3898 5043 6047 -1323 797 434 A N ATOM 1118 CA LEU A 152 4.212 124.344 274.684 1.00 39.92 A C ANISOU 1118 CA LEU A 152 3899 5105 6165 -1392 784 483 A C ATOM 1119 C LEU A 152 3.072 124.550 275.687 1.00 45.12 A C ANISOU 1119 C LEU A 152 4486 5814 6844 -1393 957 546 A C ATOM 1120 O LEU A 152 3.308 124.983 276.815 1.00 46.15 A O ANISOU 1120 O LEU A 152 4680 5959 6897 -1372 1098 575 A O ATOM 1121 CB LEU A 152 4.936 123.016 274.950 1.00 38.98 A C ANISOU 1121 CB LEU A 152 3888 4921 6002 -1470 725 512 A C ATOM 1122 CG LEU A 152 6.031 122.617 273.951 1.00 38.83 A C ANISOU 1122 CG LEU A 152 3941 4850 5962 -1466 557 439 A C ATOM 1123 CD1 LEU A 152 6.698 121.308 274.350 1.00 38.51 A C ANISOU 1123 CD1 LEU A 152 4009 4731 5891 -1529 523 458 A C ATOM 1124 CD2 LEU A 152 5.487 122.531 272.529 1.00 36.40 A C ANISOU 1124 CD2 LEU A 152 3544 4557 5731 -1441 439 375 A C ATOM 1125 N PRO A 153 1.828 124.265 275.262 1.00 48.33 A N ANISOU 1125 N PRO A 153 4766 6249 7349 -1412 952 558 A N ATOM 1126 CA PRO A 153 0.607 124.505 276.045 1.00 49.97 A C ANISOU 1126 CA PRO A 153 4879 6513 7593 -1407 1107 610 A C ATOM 1127 C PRO A 153 0.559 123.795 277.399 1.00 45.98 A C ANISOU 1127 C PRO A 153 4439 6012 7020 -1465 1238 698 A C ATOM 1128 O PRO A 153 -0.024 124.338 278.340 1.00 48.22 A O ANISOU 1128 O PRO A 153 4695 6352 7274 -1430 1402 732 A O ATOM 1129 CB PRO A 153 -0.506 123.955 275.142 1.00 53.99 A C ANISOU 1129 CB PRO A 153 5260 7027 8228 -1441 1027 605 A C ATOM 1130 CG PRO A 153 0.071 123.943 273.776 1.00 54.53 A C ANISOU 1130 CG PRO A 153 5345 7059 8316 -1423 846 530 A C ATOM 1131 CD PRO A 153 1.530 123.669 273.947 1.00 50.01 A C ANISOU 1131 CD PRO A 153 4922 6438 7641 -1435 794 515 A C ATOM 1132 N PHE A 154 1.158 122.612 277.502 1.00 42.76 A N ANISOU 1132 N PHE A 154 4121 5543 6581 -1545 1170 731 A N ATOM 1133 CA PHE A 154 1.050 121.823 278.731 1.00 44.81 A C ANISOU 1133 CA PHE A 154 4444 5802 6779 -1609 1281 826 A C ATOM 1134 C PHE A 154 2.125 122.185 279.755 1.00 45.63 A C ANISOU 1134 C PHE A 154 4702 5901 6736 -1577 1360 850 A C ATOM 1135 O PHE A 154 2.188 121.603 280.837 1.00 47.26 A O ANISOU 1135 O PHE A 154 4987 6108 6863 -1618 1451 932 A O ATOM 1136 CB PHE A 154 1.065 120.316 278.427 1.00 45.06 A C ANISOU 1136 CB PHE A 154 4501 5761 6859 -1712 1180 852 A C ATOM 1137 CG PHE A 154 2.357 119.817 277.827 1.00 42.42 A C ANISOU 1137 CG PHE A 154 4284 5344 6490 -1725 1029 800 A C ATOM 1138 CD1 PHE A 154 3.402 119.395 278.640 1.00 40.29 A C ANISOU 1138 CD1 PHE A 154 4168 5029 6112 -1751 1045 841 A C ATOM 1139 CD2 PHE A 154 2.513 119.742 276.450 1.00 40.77 A C ANISOU 1139 CD2 PHE A 154 4034 5102 6353 -1704 872 711 A C ATOM 1140 CE1 PHE A 154 4.586 118.927 278.093 1.00 37.69 A C ANISOU 1140 CE1 PHE A 154 3943 4616 5762 -1755 913 782 A C ATOM 1141 CE2 PHE A 154 3.693 119.272 275.896 1.00 41.82 A C ANISOU 1141 CE2 PHE A 154 4271 5163 6455 -1703 743 654 A C ATOM 1142 CZ PHE A 154 4.731 118.864 276.720 1.00 40.85 A C ANISOU 1142 CZ PHE A 154 4292 4987 6241 -1726 766 686 A C ATOM 1143 N ILE A 155 2.980 123.135 279.392 1.00 42.73 A N ANISOU 1143 N ILE A 155 4383 5522 6329 -1502 1324 775 A N ATOM 1144 CA ILE A 155 4.042 123.601 280.276 1.00 42.60 A C ANISOU 1144 CA ILE A 155 4528 5489 6168 -1463 1399 767 A C ATOM 1145 C ILE A 155 3.666 124.921 280.961 1.00 43.52 A C ANISOU 1145 C ILE A 155 4639 5674 6221 -1370 1569 731 A C ATOM 1146 O ILE A 155 3.206 125.859 280.306 1.00 43.84 A O ANISOU 1146 O ILE A 155 4574 5747 6338 -1309 1563 667 A O ATOM 1147 CB ILE A 155 5.365 123.774 279.493 1.00 43.71 A C ANISOU 1147 CB ILE A 155 4756 5564 6289 -1451 1253 686 A C ATOM 1148 CG1 ILE A 155 5.819 122.432 278.915 1.00 44.34 A C ANISOU 1148 CG1 ILE A 155 4858 5573 6416 -1530 1089 717 A C ATOM 1149 CG2 ILE A 155 6.455 124.365 280.376 1.00 44.70 A C ANISOU 1149 CG2 ILE A 155 5071 5685 6229 -1398 1297 646 A C ATOM 1150 CD1 ILE A 155 7.188 122.482 278.240 1.00 41.05 A C ANISOU 1150 CD1 ILE A 155 4539 5094 5962 -1518 946 639 A C ATOM 1151 N PRO A 156 3.863 125.001 282.284 1.00 42.90 A N ANISOU 1151 N PRO A 156 4685 5620 5995 -1353 1714 767 A N ATOM 1152 CA PRO A 156 3.574 126.258 282.983 1.00 43.28 A C ANISOU 1152 CA PRO A 156 4750 5732 5961 -1255 1874 718 A C ATOM 1153 C PRO A 156 4.665 127.293 282.735 1.00 42.83 A C ANISOU 1153 C PRO A 156 4810 5652 5812 -1170 1788 601 A C ATOM 1154 O PRO A 156 5.492 127.521 283.620 1.00 43.86 A O ANISOU 1154 O PRO A 156 5122 5779 5765 -1128 1803 578 A O ATOM 1155 CB PRO A 156 3.569 125.843 284.457 1.00 45.26 A C ANISOU 1155 CB PRO A 156 5128 6016 6051 -1261 2012 792 A C ATOM 1156 CG PRO A 156 4.452 124.643 284.513 1.00 46.22 A C ANISOU 1156 CG PRO A 156 5366 6064 6131 -1350 1903 849 A C ATOM 1157 CD PRO A 156 4.249 123.921 283.210 1.00 46.19 A C ANISOU 1157 CD PRO A 156 5227 6012 6313 -1418 1736 858 A C ATOM 1158 N HIS A 157 4.652 127.928 281.562 1.00 43.89 A N ANISOU 1158 N HIS A 157 4844 5775 6058 -1135 1677 529 A N ATOM 1159 CA HIS A 157 5.724 128.839 281.169 1.00 42.92 A C ANISOU 1159 CA HIS A 157 4821 5625 5862 -1058 1554 427 A C ATOM 1160 C HIS A 157 5.691 130.122 281.987 1.00 46.95 A C ANISOU 1160 C HIS A 157 5399 6175 6264 -945 1661 363 A C ATOM 1161 O HIS A 157 6.541 130.999 281.816 1.00 48.89 A O ANISOU 1161 O HIS A 157 5732 6397 6446 -875 1574 278 A O ATOM 1162 CB HIS A 157 5.582 129.221 279.690 1.00 43.81 A C ANISOU 1162 CB HIS A 157 4798 5723 6126 -1049 1423 380 A C ATOM 1163 CG HIS A 157 6.084 128.189 278.728 1.00 44.03 A C ANISOU 1163 CG HIS A 157 4809 5697 6222 -1132 1261 400 A C ATOM 1164 CD2 HIS A 157 5.427 127.248 278.004 1.00 43.47 A C ANISOU 1164 CD2 HIS A 157 4608 5612 6296 -1216 1219 452 A C ATOM 1165 ND1 HIS A 157 7.418 128.059 278.402 1.00 39.66 A N ANISOU 1165 ND1 HIS A 157 4383 5095 5590 -1129 1116 358 A N ATOM 1166 CE1 HIS A 157 7.561 127.084 277.521 1.00 40.39 A C ANISOU 1166 CE1 HIS A 157 4428 5151 5769 -1201 997 380 A C ATOM 1167 NE2 HIS A 157 6.370 126.573 277.266 1.00 43.16 A N ANISOU 1167 NE2 HIS A 157 4627 5518 6254 -1256 1051 435 A N ATOM 1168 N GLU A 158 4.733 130.213 282.901 1.00 45.95 A N ANISOU 1168 N GLU A 158 5236 6109 6116 -927 1851 403 A N ATOM 1169 CA GLU A 158 4.608 131.373 283.768 1.00 52.07 A C ANISOU 1169 CA GLU A 158 6077 6925 6782 -815 1969 338 A C ATOM 1170 C GLU A 158 5.350 131.195 285.088 1.00 50.76 A C ANISOU 1170 C GLU A 158 6125 6762 6400 -798 2024 344 A C ATOM 1171 O GLU A 158 5.538 132.157 285.829 1.00 53.15 A O ANISOU 1171 O GLU A 158 6527 7085 6582 -699 2086 272 A O ATOM 1172 CB GLU A 158 3.131 131.756 283.975 1.00 63.09 A C ANISOU 1172 CB GLU A 158 7304 8393 8274 -781 2149 360 A C ATOM 1173 CG GLU A 158 2.267 130.716 284.690 1.00 73.60 A C ANISOU 1173 CG GLU A 158 8578 9770 9614 -859 2309 479 A C ATOM 1174 CD GLU A 158 1.882 129.547 283.785 1.00 79.80 A C ANISOU 1174 CD GLU A 158 9229 10526 10564 -979 2208 563 A C ATOM 1175 OE1 GLU A 158 2.201 129.595 282.577 1.00 81.92 A O ANISOU 1175 OE1 GLU A 158 9432 10745 10948 -1002 2058 526 A O ATOM 1176 OE2 GLU A 158 1.246 128.587 284.273 1.00 82.35 A O1- ANISOU 1176 OE2 GLU A 158 9518 10880 10892 -1040 2251 661 A O1- ATOM 1177 N ASP A 159 5.790 129.971 285.366 1.00 45.32 A N ANISOU 1177 N ASP A 159 5512 6046 5662 -892 1990 426 A N ATOM 1178 CA ASP A 159 6.629 129.716 286.531 1.00 41.02 A C ANISOU 1178 CA ASP A 159 5182 5494 4910 -882 2008 436 A C ATOM 1179 C ASP A 159 8.031 130.205 286.194 1.00 40.84 A C ANISOU 1179 C ASP A 159 5292 5406 4821 -843 1822 345 A C ATOM 1180 O ASP A 159 8.532 129.957 285.096 1.00 42.60 A O ANISOU 1180 O ASP A 159 5461 5577 5147 -883 1664 331 A O ATOM 1181 CB ASP A 159 6.647 128.226 286.874 1.00 38.97 A C ANISOU 1181 CB ASP A 159 4954 5217 4636 -997 2019 560 A C ATOM 1182 CG ASP A 159 7.262 127.944 288.235 1.00 43.03 A C ANISOU 1182 CG ASP A 159 5681 5738 4930 -985 2075 590 A C ATOM 1183 OD1 ASP A 159 6.508 127.631 289.184 1.00 47.84 A O ANISOU 1183 OD1 ASP A 159 6298 6409 5472 -996 2256 669 A O ATOM 1184 OD2 ASP A 159 8.502 128.039 288.354 1.00 39.96 A O1- ANISOU 1184 OD2 ASP A 159 5451 5298 4436 -964 1938 539 A O1- ATOM 1185 N PRO A 160 8.669 130.915 287.134 1.00 38.69 A N ANISOU 1185 N PRO A 160 5190 5138 4374 -762 1840 282 A N ATOM 1186 CA PRO A 160 9.985 131.501 286.856 1.00 39.14 A C ANISOU 1186 CA PRO A 160 5363 5132 4377 -721 1667 192 A C ATOM 1187 C PRO A 160 11.074 130.453 286.655 1.00 40.59 A C ANISOU 1187 C PRO A 160 5636 5253 4533 -800 1517 235 A C ATOM 1188 O PRO A 160 12.144 130.771 286.129 1.00 39.97 A O ANISOU 1188 O PRO A 160 5610 5121 4457 -785 1357 174 A O ATOM 1189 CB PRO A 160 10.284 132.300 288.130 1.00 40.43 A C ANISOU 1189 CB PRO A 160 5696 5316 4348 -627 1740 130 A C ATOM 1190 CG PRO A 160 8.956 132.490 288.798 1.00 39.59 A C ANISOU 1190 CG PRO A 160 5520 5293 4229 -592 1960 159 A C ATOM 1191 CD PRO A 160 8.177 131.266 288.476 1.00 35.27 A C ANISOU 1191 CD PRO A 160 4845 4768 3790 -701 2022 284 A C ATOM 1192 N ARG A 161 10.801 129.217 287.056 1.00 39.14 A N ANISOU 1192 N ARG A 161 5463 5075 4332 -884 1569 341 A N ATOM 1193 CA ARG A 161 11.782 128.154 286.905 1.00 34.22 A C ANISOU 1193 CA ARG A 161 4923 4388 3689 -957 1429 385 A C ATOM 1194 C ARG A 161 11.707 127.477 285.535 1.00 33.72 A C ANISOU 1194 C ARG A 161 4713 4287 3812 -1031 1319 409 A C ATOM 1195 O ARG A 161 12.531 126.619 285.214 1.00 32.23 A O ANISOU 1195 O ARG A 161 4574 4041 3632 -1086 1189 432 A O ATOM 1196 CB ARG A 161 11.628 127.130 288.032 1.00 33.35 A C ANISOU 1196 CB ARG A 161 4917 4290 3464 -1011 1522 490 A C ATOM 1197 CG ARG A 161 11.924 127.698 289.420 1.00 32.56 A C ANISOU 1197 CG ARG A 161 5000 4222 3148 -936 1604 463 A C ATOM 1198 CD ARG A 161 11.388 126.777 290.502 1.00 37.57 A C ANISOU 1198 CD ARG A 161 5700 4893 3681 -986 1745 584 A C ATOM 1199 NE ARG A 161 9.933 126.671 290.437 1.00 38.38 A N ANISOU 1199 NE ARG A 161 5637 5063 3883 -1012 1925 649 A N ATOM 1200 CZ ARG A 161 9.200 125.889 291.222 1.00 41.52 A C ANISOU 1200 CZ ARG A 161 6039 5503 4235 -1065 2077 769 A C ATOM 1201 NH1 ARG A 161 9.781 125.126 292.137 1.00 39.05 A N1+ ANISOU 1201 NH1 ARG A 161 5897 5171 3770 -1099 2069 842 A N1+ ATOM 1202 NH2 ARG A 161 7.882 125.862 291.080 1.00 43.45 A N ANISOU 1202 NH2 ARG A 161 6112 5808 4590 -1087 2237 823 A N ATOM 1203 N ILE A 162 10.726 127.869 284.727 1.00 28.80 A N ANISOU 1203 N ILE A 162 3910 3697 3335 -1027 1366 398 A N ATOM 1204 CA ILE A 162 10.659 127.418 283.341 1.00 33.04 A C ANISOU 1204 CA ILE A 162 4308 4202 4042 -1080 1249 400 A C ATOM 1205 C ILE A 162 11.276 128.503 282.469 1.00 31.27 A C ANISOU 1205 C ILE A 162 4065 3965 3851 -1011 1136 298 A C ATOM 1206 O ILE A 162 10.736 129.605 282.360 1.00 33.39 A O ANISOU 1206 O ILE A 162 4270 4270 4149 -943 1197 247 A O ATOM 1207 CB ILE A 162 9.209 127.160 282.884 1.00 35.74 A C ANISOU 1207 CB ILE A 162 4456 4584 4538 -1122 1350 454 A C ATOM 1208 CG1 ILE A 162 8.530 126.135 283.798 1.00 38.05 A C ANISOU 1208 CG1 ILE A 162 4758 4893 4805 -1195 1480 568 A C ATOM 1209 CG2 ILE A 162 9.181 126.695 281.429 1.00 30.07 A C ANISOU 1209 CG2 ILE A 162 3608 3832 3986 -1173 1212 448 A C ATOM 1210 CD1 ILE A 162 9.236 124.796 283.850 1.00 36.27 A C ANISOU 1210 CD1 ILE A 162 4618 4602 4562 -1282 1380 633 A C ATOM 1211 N TRP A 163 12.410 128.184 281.851 1.00 32.28 A N ANISOU 1211 N TRP A 163 4246 4039 3979 -1029 972 271 A N ATOM 1212 CA TRP A 163 13.199 129.170 281.121 1.00 30.73 A C ANISOU 1212 CA TRP A 163 4054 3827 3795 -968 859 184 A C ATOM 1213 C TRP A 163 13.086 129.024 279.607 1.00 29.45 A C ANISOU 1213 C TRP A 163 3750 3657 3782 -994 757 173 A C ATOM 1214 O TRP A 163 12.942 127.912 279.087 1.00 26.46 A O ANISOU 1214 O TRP A 163 3319 3260 3474 -1066 711 219 A O ATOM 1215 CB TRP A 163 14.679 129.001 281.469 1.00 33.19 A C ANISOU 1215 CB TRP A 163 4525 4088 3997 -961 743 158 A C ATOM 1216 CG TRP A 163 15.046 129.275 282.892 1.00 32.75 A C ANISOU 1216 CG TRP A 163 4633 4032 3778 -924 805 152 A C ATOM 1217 CD1 TRP A 163 14.229 129.728 283.887 1.00 33.31 A C ANISOU 1217 CD1 TRP A 163 4731 4149 3777 -887 960 160 A C ATOM 1218 CD2 TRP A 163 16.347 129.129 283.472 1.00 30.93 A C ANISOU 1218 CD2 TRP A 163 4565 3757 3431 -914 708 132 A C ATOM 1219 CE2 TRP A 163 16.243 129.499 284.827 1.00 31.40 A C ANISOU 1219 CE2 TRP A 163 4752 3835 3343 -872 804 128 A C ATOM 1220 CE3 TRP A 163 17.587 128.713 282.977 1.00 27.81 A C ANISOU 1220 CE3 TRP A 163 4216 3308 3041 -933 548 115 A C ATOM 1221 NE1 TRP A 163 14.943 129.863 285.057 1.00 31.10 A N ANISOU 1221 NE1 TRP A 163 4631 3856 3332 -854 963 144 A N ATOM 1222 CZ2 TRP A 163 17.338 129.471 285.690 1.00 35.12 A C ANISOU 1222 CZ2 TRP A 163 5400 4270 3675 -851 735 108 A C ATOM 1223 CZ3 TRP A 163 18.668 128.685 283.833 1.00 26.41 A C ANISOU 1223 CZ3 TRP A 163 4202 3094 2737 -914 483 99 A C ATOM 1224 CH2 TRP A 163 18.538 129.061 285.174 1.00 32.52 A C ANISOU 1224 CH2 TRP A 163 5105 3884 3367 -875 571 96 A C ATOM 1225 N ASP A 164 13.170 130.149 278.900 1.00 22.02 A N ANISOU 1225 N ASP A 164 2755 2727 2886 -933 717 111 A N ATOM 1226 CA ASP A 164 13.576 130.114 277.500 1.00 23.58 A C ANISOU 1226 CA ASP A 164 2873 2911 3176 -945 583 88 A C ATOM 1227 C ASP A 164 15.011 130.625 277.425 1.00 20.99 A C ANISOU 1227 C ASP A 164 2653 2548 2774 -907 472 36 A C ATOM 1228 O ASP A 164 15.632 130.864 278.463 1.00 21.50 A O ANISOU 1228 O ASP A 164 2851 2594 2725 -881 490 21 A O ATOM 1229 CB ASP A 164 12.625 130.896 276.582 1.00 32.25 A C ANISOU 1229 CB ASP A 164 3815 4044 4394 -914 603 71 A C ATOM 1230 CG ASP A 164 12.528 132.374 276.940 1.00 35.60 A C ANISOU 1230 CG ASP A 164 4255 4482 4790 -827 655 19 A C ATOM 1231 OD1 ASP A 164 13.406 132.894 277.661 1.00 36.36 A O ANISOU 1231 OD1 ASP A 164 4483 4554 4780 -787 641 -17 A O ATOM 1232 OD2 ASP A 164 11.565 133.024 276.478 1.00 36.94 A O1- ANISOU 1232 OD2 ASP A 164 4303 4682 5052 -796 701 13 A O1- ATOM 1233 N SER A 165 15.534 130.786 276.215 1.00 21.48 A N ANISOU 1233 N SER A 165 2210 2546 3404 -273 634 -91 A N ATOM 1234 CA SER A 165 16.924 131.193 276.039 1.00 22.86 A C ANISOU 1234 CA SER A 165 2554 2689 3443 -249 546 -113 A C ATOM 1235 C SER A 165 17.254 132.544 276.690 1.00 24.41 A C ANISOU 1235 C SER A 165 2832 2880 3565 -155 579 -167 A C ATOM 1236 O SER A 165 18.351 132.733 277.218 1.00 18.61 A O ANISOU 1236 O SER A 165 2241 2142 2687 -158 572 -177 A O ATOM 1237 CB SER A 165 17.290 131.213 274.552 1.00 21.14 A C ANISOU 1237 CB SER A 165 2324 2455 3254 -272 371 -120 A C ATOM 1238 OG SER A 165 16.343 131.960 273.813 1.00 23.19 A O ANISOU 1238 OG SER A 165 2456 2720 3634 -233 309 -128 A O ATOM 1239 N THR A 166 16.314 133.483 276.640 1.00 25.69 A N ANISOU 1239 N THR A 166 2899 3031 3831 -69 602 -207 A N ATOM 1240 CA THR A 166 16.521 134.792 277.262 1.00 22.78 A C ANISOU 1240 CA THR A 166 2621 2618 3417 32 628 -284 A C ATOM 1241 C THR A 166 16.708 134.671 278.778 1.00 26.88 A C ANISOU 1241 C THR A 166 3228 3192 3795 47 792 -328 A C ATOM 1242 O THR A 166 17.663 135.227 279.350 1.00 23.98 A O ANISOU 1242 O THR A 166 3023 2799 3291 53 772 -377 A O ATOM 1243 CB THR A 166 15.361 135.761 276.918 1.00 26.58 A C ANISOU 1243 CB THR A 166 2972 3062 4066 155 622 -325 A C ATOM 1244 CG2 THR A 166 15.544 137.114 277.607 1.00 21.81 A C ANISOU 1244 CG2 THR A 166 2484 2369 3433 277 647 -430 A C ATOM 1245 OG1 THR A 166 15.333 135.963 275.499 1.00 25.86 A O ANISOU 1245 OG1 THR A 166 2828 2928 4069 134 443 -266 A O ATOM 1246 N ASP A 167 15.817 133.912 279.414 1.00 31.72 A N ANISOU 1246 N ASP A 167 3728 3895 4428 34 945 -300 A N ATOM 1247 CA ASP A 167 15.912 133.637 280.846 1.00 34.33 A C ANISOU 1247 CA ASP A 167 4129 4316 4597 31 1113 -312 A C ATOM 1248 C ASP A 167 17.269 133.027 281.192 1.00 33.08 A C ANISOU 1248 C ASP A 167 4146 4156 4267 -55 1054 -258 A C ATOM 1249 O ASP A 167 17.909 133.419 282.170 1.00 32.88 A O ANISOU 1249 O ASP A 167 4258 4169 4067 -35 1095 -307 A O ATOM 1250 CB ASP A 167 14.796 132.686 281.285 1.00 38.10 A C ANISOU 1250 CB ASP A 167 4443 4906 5130 -19 1273 -236 A C ATOM 1251 CG ASP A 167 13.412 133.252 281.034 1.00 40.83 A C ANISOU 1251 CG ASP A 167 4572 5295 5646 76 1345 -287 A C ATOM 1252 OD1 ASP A 167 13.190 134.444 281.332 1.00 44.94 A O ANISOU 1252 OD1 ASP A 167 5105 5802 6167 228 1381 -413 A O ATOM 1253 OD2 ASP A 167 12.549 132.504 280.524 1.00 38.13 A O1- ANISOU 1253 OD2 ASP A 167 4044 4994 5448 1 1354 -205 A O1- ATOM 1254 N ALA A 168 17.696 132.061 280.383 1.00 26.96 A N ANISOU 1254 N ALA A 168 3359 3343 3540 -143 950 -166 A N ATOM 1255 CA ALA A 168 18.970 131.394 280.594 1.00 23.26 A C ANISOU 1255 CA ALA A 168 3026 2874 2938 -199 883 -108 A C ATOM 1256 C ALA A 168 20.111 132.398 280.504 1.00 25.57 A C ANISOU 1256 C ALA A 168 3440 3146 3130 -169 772 -177 A C ATOM 1257 O ALA A 168 21.049 132.368 281.306 1.00 21.13 A O ANISOU 1257 O ALA A 168 2997 2630 2401 -183 766 -171 A O ATOM 1258 CB ALA A 168 19.162 130.300 279.566 1.00 23.30 A C ANISOU 1258 CB ALA A 168 2988 2824 3041 -265 783 -37 A C ATOM 1259 N LEU A 169 20.026 133.299 279.531 1.00 22.30 A N ANISOU 1259 N LEU A 169 2990 2666 2815 -140 674 -229 A N ATOM 1260 CA LEU A 169 21.100 134.266 279.338 1.00 25.07 A C ANISOU 1260 CA LEU A 169 3449 2986 3092 -146 556 -272 A C ATOM 1261 C LEU A 169 21.066 135.365 280.401 1.00 28.04 A C ANISOU 1261 C LEU A 169 3924 3344 3385 -95 612 -380 A C ATOM 1262 O LEU A 169 22.028 136.117 280.555 1.00 31.84 A O ANISOU 1262 O LEU A 169 4519 3800 3779 -126 521 -421 A O ATOM 1263 CB LEU A 169 21.057 134.861 277.928 1.00 16.20 A C ANISOU 1263 CB LEU A 169 2269 1796 2090 -151 424 -262 A C ATOM 1264 CG LEU A 169 21.357 133.862 276.807 1.00 23.61 A C ANISOU 1264 CG LEU A 169 3138 2771 3061 -206 345 -189 A C ATOM 1265 CD1 LEU A 169 21.078 134.485 275.443 1.00 26.74 A C ANISOU 1265 CD1 LEU A 169 3470 3132 3558 -209 228 -173 A C ATOM 1266 CD2 LEU A 169 22.789 133.357 276.885 1.00 22.55 A C ANISOU 1266 CD2 LEU A 169 3078 2702 2788 -254 290 -157 A C ATOM 1267 N GLU A 170 19.968 135.462 281.141 1.00 28.01 A N ANISOU 1267 N GLU A 170 3875 3363 3405 -21 763 -435 A N ATOM 1268 CA GLU A 170 19.932 136.424 282.247 1.00 36.17 A C ANISOU 1268 CA GLU A 170 5017 4394 4332 45 834 -570 A C ATOM 1269 C GLU A 170 20.798 135.998 283.444 1.00 35.77 A C ANISOU 1269 C GLU A 170 5095 4456 4040 -10 872 -568 A C ATOM 1270 O GLU A 170 21.152 136.831 284.287 1.00 27.85 A O ANISOU 1270 O GLU A 170 4222 3453 2906 13 877 -692 A O ATOM 1271 CB GLU A 170 18.495 136.720 282.679 1.00 41.00 A C ANISOU 1271 CB GLU A 170 5523 5028 5027 166 999 -648 A C ATOM 1272 CG GLU A 170 17.775 137.670 281.730 1.00 49.64 A C ANISOU 1272 CG GLU A 170 6534 5987 6339 263 929 -698 A C ATOM 1273 CD GLU A 170 16.327 137.889 282.116 1.00 60.24 A C ANISOU 1273 CD GLU A 170 7728 7378 7782 403 1095 -771 A C ATOM 1274 OE1 GLU A 170 15.910 137.373 283.177 1.00 61.62 A O ANISOU 1274 OE1 GLU A 170 7872 7704 7835 414 1281 -792 A O ATOM 1275 OE2 GLU A 170 15.603 138.567 281.353 1.00 66.67 A O1- ANISOU 1275 OE2 GLU A 170 8443 8096 8792 505 1040 -794 A O1- ATOM 1276 N LEU A 171 21.140 134.710 283.505 1.00 34.37 A N ANISOU 1276 N LEU A 171 4890 4364 3807 -80 884 -429 A N ATOM 1277 CA LEU A 171 22.029 134.188 284.544 1.00 36.05 A C ANISOU 1277 CA LEU A 171 5214 4687 3795 -130 890 -385 A C ATOM 1278 C LEU A 171 21.498 134.524 285.939 1.00 38.67 A C ANISOU 1278 C LEU A 171 5613 5125 3957 -84 1048 -474 A C ATOM 1279 O LEU A 171 22.196 135.136 286.752 1.00 34.80 A O ANISOU 1279 O LEU A 171 5261 4680 3280 -91 1012 -566 A O ATOM 1280 CB LEU A 171 23.429 134.791 284.374 1.00 39.76 A C ANISOU 1280 CB LEU A 171 5788 5135 4183 -182 713 -418 A C ATOM 1281 CG LEU A 171 24.575 133.894 283.904 1.00 41.30 A C ANISOU 1281 CG LEU A 171 5970 5373 4351 -244 591 -287 A C ATOM 1282 CD1 LEU A 171 25.895 134.651 284.004 1.00 39.15 A C ANISOU 1282 CD1 LEU A 171 5780 5126 3967 -304 440 -333 A C ATOM 1283 CD2 LEU A 171 24.631 132.592 284.679 1.00 40.40 A C ANISOU 1283 CD2 LEU A 171 5865 5355 4130 -249 661 -160 A C ATOM 1284 N LYS A 172 20.259 134.126 286.207 1.00 41.31 A N ANISOU 1284 N LYS A 172 5839 5514 4343 -45 1225 -451 A N ATOM 1285 CA LYS A 172 19.599 134.454 287.466 1.00 40.14 A C ANISOU 1285 CA LYS A 172 5722 5501 4028 13 1411 -544 A C ATOM 1286 C LYS A 172 20.215 133.679 288.626 1.00 38.17 A C ANISOU 1286 C LYS A 172 5581 5415 3507 -59 1453 -442 A C ATOM 1287 O LYS A 172 20.294 134.181 289.749 1.00 38.62 A O ANISOU 1287 O LYS A 172 5747 5595 3331 -29 1531 -551 A O ATOM 1288 CB LYS A 172 18.105 134.140 287.368 1.00 44.08 A C ANISOU 1288 CB LYS A 172 6031 6052 4666 59 1596 -517 A C ATOM 1289 CG LYS A 172 17.392 134.888 286.248 1.00 51.13 A C ANISOU 1289 CG LYS A 172 6796 6803 5828 147 1547 -602 A C ATOM 1290 CD LYS A 172 15.887 134.698 286.329 1.00 58.25 A C ANISOU 1290 CD LYS A 172 7487 7799 6846 206 1738 -597 A C ATOM 1291 CE LYS A 172 15.507 133.246 286.092 1.00 59.21 A C ANISOU 1291 CE LYS A 172 7483 7981 7032 70 1781 -380 A C ATOM 1292 NZ LYS A 172 14.036 133.021 286.225 1.00 63.88 A N1+ ANISOU 1292 NZ LYS A 172 7841 8696 7733 95 1971 -357 A N1+ ATOM 1293 N GLU A 173 20.653 132.456 288.337 1.00 33.79 A N ANISOU 1293 N GLU A 173 5005 4855 2980 -146 1391 -235 A N ATOM 1294 CA GLU A 173 21.243 131.572 289.335 1.00 34.67 A C ANISOU 1294 CA GLU A 173 5213 5099 2863 -210 1405 -86 A C ATOM 1295 C GLU A 173 21.895 130.394 288.629 1.00 33.10 A C ANISOU 1295 C GLU A 173 4992 4805 2781 -270 1272 107 A C ATOM 1296 O GLU A 173 21.771 130.238 287.417 1.00 36.37 A O ANISOU 1296 O GLU A 173 5311 5076 3431 -268 1197 109 A O ATOM 1297 CB GLU A 173 20.180 131.017 290.283 1.00 36.32 A C ANISOU 1297 CB GLU A 173 5352 5464 2983 -222 1607 4 A C ATOM 1298 CG GLU A 173 19.204 130.065 289.596 1.00 44.07 A C ANISOU 1298 CG GLU A 173 6182 6380 4181 -283 1709 151 A C ATOM 1299 CD GLU A 173 18.117 129.562 290.530 1.00 58.57 A C ANISOU 1299 CD GLU A 173 7907 8395 5954 -310 1877 255 A C ATOM 1300 OE1 GLU A 173 18.432 129.250 291.700 1.00 63.38 A O ANISOU 1300 OE1 GLU A 173 8585 9164 6331 -326 1883 344 A O ATOM 1301 OE2 GLU A 173 16.950 129.468 290.094 1.00 62.34 A O1- ANISOU 1301 OE2 GLU A 173 8210 8870 6606 -321 1996 258 A O1- ATOM 1302 N VAL A 174 22.615 129.582 289.391 1.00 31.19 A N ANISOU 1302 N VAL A 174 4843 4645 2363 -312 1233 261 A N ATOM 1303 CA VAL A 174 23.145 128.330 288.881 1.00 31.06 A C ANISOU 1303 CA VAL A 174 4815 4530 2455 -344 1126 451 A C ATOM 1304 C VAL A 174 22.330 127.207 289.504 1.00 32.40 A C ANISOU 1304 C VAL A 174 4970 4733 2607 -411 1267 654 A C ATOM 1305 O VAL A 174 22.565 126.828 290.648 1.00 35.30 A O ANISOU 1305 O VAL A 174 5399 5236 2777 -426 1277 771 A O ATOM 1306 CB VAL A 174 24.646 128.184 289.209 1.00 32.27 A C ANISOU 1306 CB VAL A 174 5074 4731 2455 -328 948 502 A C ATOM 1307 CG1 VAL A 174 25.203 126.864 288.686 1.00 32.73 A C ANISOU 1307 CG1 VAL A 174 5120 4676 2642 -321 839 685 A C ATOM 1308 CG2 VAL A 174 25.426 129.369 288.638 1.00 26.33 A C ANISOU 1308 CG2 VAL A 174 4323 3964 1716 -298 818 312 A C ATOM 1309 N PRO A 175 21.341 126.689 288.758 1.00 32.70 A N ANISOU 1309 N PRO A 175 4884 4657 2883 -451 1335 695 A N ATOM 1310 CA PRO A 175 20.506 125.610 289.296 1.00 35.16 A C ANISOU 1310 CA PRO A 175 5168 4986 3205 -552 1466 905 A C ATOM 1311 C PRO A 175 21.340 124.358 289.532 1.00 35.96 A C ANISOU 1311 C PRO A 175 5382 4999 3283 -585 1346 1130 A C ATOM 1312 O PRO A 175 22.191 124.023 288.708 1.00 33.46 A O ANISOU 1312 O PRO A 175 5089 4530 3095 -530 1169 1115 A O ATOM 1313 CB PRO A 175 19.462 125.380 288.193 1.00 31.75 A C ANISOU 1313 CB PRO A 175 4570 4420 3073 -595 1501 872 A C ATOM 1314 CG PRO A 175 20.044 125.985 286.967 1.00 34.77 A C ANISOU 1314 CG PRO A 175 4930 4681 3601 -511 1338 700 A C ATOM 1315 CD PRO A 175 20.909 127.118 287.418 1.00 29.48 A C ANISOU 1315 CD PRO A 175 4353 4116 2732 -424 1290 559 A C ATOM 1316 N GLU A 176 21.096 123.682 290.648 1.00 39.04 A N ANISOU 1316 N GLU A 176 5783 5502 3547 -646 1386 1316 A N ATOM 1317 CA GLU A 176 21.845 122.485 290.987 1.00 42.13 A C ANISOU 1317 CA GLU A 176 6279 5805 3923 -669 1259 1550 A C ATOM 1318 C GLU A 176 21.585 121.427 289.926 1.00 40.72 A C ANISOU 1318 C GLU A 176 6096 5337 4041 -722 1211 1643 A C ATOM 1319 O GLU A 176 22.506 120.753 289.460 1.00 33.27 A O ANISOU 1319 O GLU A 176 5250 4211 3179 -656 1062 1713 A O ATOM 1320 CB GLU A 176 21.412 121.984 292.362 1.00 44.92 A C ANISOU 1320 CB GLU A 176 6624 6334 4110 -742 1326 1734 A C ATOM 1321 CG GLU A 176 22.182 120.792 292.888 1.00 52.39 A C ANISOU 1321 CG GLU A 176 7856 7038 5010 -733 1261 1893 A C ATOM 1322 CD GLU A 176 21.675 120.370 294.253 1.00 65.00 A C ANISOU 1322 CD GLU A 176 9527 8739 6433 -778 1400 2046 A C ATOM 1323 OE1 GLU A 176 20.684 120.973 294.721 1.00 68.44 A O ANISOU 1323 OE1 GLU A 176 9880 9332 6793 -814 1595 1964 A O ATOM 1324 OE2 GLU A 176 22.258 119.443 294.854 1.00 67.42 A O1- ANISOU 1324 OE2 GLU A 176 9973 8974 6670 -778 1311 2250 A O1- ATOM 1325 N ARG A 177 20.327 121.328 289.510 1.00 39.12 A N ANISOU 1325 N ARG A 177 5761 5094 4007 -824 1330 1623 A N ATOM 1326 CA ARG A 177 19.946 120.385 288.474 1.00 39.36 A C ANISOU 1326 CA ARG A 177 5764 4854 4336 -893 1276 1678 A C ATOM 1327 C ARG A 177 19.102 121.065 287.405 1.00 41.10 A C ANISOU 1327 C ARG A 177 5820 5053 4743 -901 1335 1474 A C ATOM 1328 O ARG A 177 18.016 121.580 287.686 1.00 40.63 A O ANISOU 1328 O ARG A 177 5622 5148 4667 -965 1492 1435 A O ATOM 1329 CB ARG A 177 19.177 119.215 289.083 1.00 43.02 A C ANISOU 1329 CB ARG A 177 6228 5270 4847 -1073 1296 1897 A C ATOM 1330 CG ARG A 177 19.131 117.999 288.194 1.00 51.62 A C ANISOU 1330 CG ARG A 177 7365 6027 6221 -1135 1173 1969 A C ATOM 1331 CD ARG A 177 18.454 116.831 288.880 1.00 62.89 A C ANISOU 1331 CD ARG A 177 8881 7347 7667 -1306 1222 2150 A C ATOM 1332 NE ARG A 177 18.441 115.653 288.019 1.00 68.80 A N ANISOU 1332 NE ARG A 177 9690 7752 8698 -1346 1093 2187 A N ATOM 1333 CZ ARG A 177 17.514 114.701 288.063 1.00 73.84 A C ANISOU 1333 CZ ARG A 177 10327 8247 9482 -1510 1141 2277 A C ATOM 1334 NH1 ARG A 177 16.515 114.777 288.936 1.00 74.35 A N1+ ANISOU 1334 NH1 ARG A 177 10317 8492 9442 -1648 1331 2361 A N1+ ATOM 1335 NH2 ARG A 177 17.589 113.668 287.234 1.00 75.16 A N ANISOU 1335 NH2 ARG A 177 10562 8094 9902 -1530 1002 2272 A N ATOM 1336 N LEU A 178 19.613 121.044 286.174 1.00 36.38 A N ANISOU 1336 N LEU A 178 5212 4290 4319 -823 1172 1328 A N ATOM 1337 CA LEU A 178 18.964 121.688 285.037 1.00 30.28 A C ANISOU 1337 CA LEU A 178 4288 3501 3717 -815 1166 1129 A C ATOM 1338 C LEU A 178 18.597 120.704 283.925 1.00 34.23 A C ANISOU 1338 C LEU A 178 4752 3767 4489 -890 1060 1130 A C ATOM 1339 O LEU A 178 19.430 119.895 283.486 1.00 32.49 A O ANISOU 1339 O LEU A 178 4642 3364 4337 -843 912 1150 A O ATOM 1340 CB LEU A 178 19.866 122.789 284.470 1.00 30.80 A C ANISOU 1340 CB LEU A 178 4366 3625 3710 -661 1068 924 A C ATOM 1341 CG LEU A 178 19.454 123.394 283.126 1.00 29.71 A C ANISOU 1341 CG LEU A 178 4102 3445 3742 -636 1009 738 A C ATOM 1342 CD1 LEU A 178 18.151 124.167 283.245 1.00 30.20 A C ANISOU 1342 CD1 LEU A 178 4008 3626 3841 -678 1155 683 A C ATOM 1343 CD2 LEU A 178 20.558 124.279 282.550 1.00 31.24 A C ANISOU 1343 CD2 LEU A 178 4335 3673 3861 -509 890 589 A C ATOM 1344 N LEU A 179 17.345 120.783 283.476 1.00 34.31 A N ANISOU 1344 N LEU A 179 4598 3789 4650 -1001 1132 1096 A N ATOM 1345 CA LEU A 179 16.893 120.046 282.298 1.00 34.68 A C ANISOU 1345 CA LEU A 179 4588 3639 4948 -1083 1018 1046 A C ATOM 1346 C LEU A 179 16.836 120.952 281.068 1.00 33.44 A C ANISOU 1346 C LEU A 179 4325 3524 4857 -994 936 816 A C ATOM 1347 O LEU A 179 16.229 122.025 281.099 1.00 32.11 A O ANISOU 1347 O LEU A 179 4024 3526 4652 -964 1025 737 A O ATOM 1348 CB LEU A 179 15.519 119.429 282.530 1.00 32.84 A C ANISOU 1348 CB LEU A 179 4226 3394 4858 -1296 1121 1178 A C ATOM 1349 CG LEU A 179 14.934 118.706 281.311 1.00 36.30 A C ANISOU 1349 CG LEU A 179 4595 3638 5560 -1411 990 1109 A C ATOM 1350 CD1 LEU A 179 15.777 117.492 280.931 1.00 36.31 A C ANISOU 1350 CD1 LEU A 179 4796 3345 5655 -1407 821 1139 A C ATOM 1351 CD2 LEU A 179 13.487 118.290 281.558 1.00 35.20 A C ANISOU 1351 CD2 LEU A 179 4298 3584 5491 -1610 1048 1189 A C ATOM 1352 N VAL A 180 17.493 120.518 279.998 1.00 30.54 A N ANISOU 1352 N VAL A 180 4024 3003 4577 -940 766 712 A N ATOM 1353 CA VAL A 180 17.404 121.180 278.698 1.00 27.52 A C ANISOU 1353 CA VAL A 180 3548 2651 4259 -884 670 519 A C ATOM 1354 C VAL A 180 16.503 120.358 277.783 1.00 29.33 A C ANISOU 1354 C VAL A 180 3698 2743 4704 -1024 590 486 A C ATOM 1355 O VAL A 180 16.813 119.206 277.460 1.00 32.52 A O ANISOU 1355 O VAL A 180 4211 2940 5205 -1066 490 497 A O ATOM 1356 CB VAL A 180 18.791 121.339 278.043 1.00 28.83 A C ANISOU 1356 CB VAL A 180 3825 2792 4338 -728 540 405 A C ATOM 1357 CG1 VAL A 180 18.662 121.973 276.671 1.00 27.82 A C ANISOU 1357 CG1 VAL A 180 3604 2710 4255 -694 444 233 A C ATOM 1358 CG2 VAL A 180 19.720 122.178 278.932 1.00 26.91 A C ANISOU 1358 CG2 VAL A 180 3650 2690 3886 -614 596 434 A C ATOM 1359 N MET A 181 15.372 120.934 277.390 1.00 26.81 A N ANISOU 1359 N MET A 181 3189 2531 4467 -1094 624 442 A N ATOM 1360 CA MET A 181 14.480 120.266 276.449 1.00 29.16 A C ANISOU 1360 CA MET A 181 3386 2731 4961 -1240 526 394 A C ATOM 1361 C MET A 181 14.850 120.686 275.040 1.00 30.69 A C ANISOU 1361 C MET A 181 3573 2936 5153 -1149 365 202 A C ATOM 1362 O MET A 181 14.676 121.853 274.665 1.00 26.19 A O ANISOU 1362 O MET A 181 2896 2529 4524 -1065 370 135 A O ATOM 1363 CB MET A 181 13.013 120.609 276.714 1.00 30.44 A C ANISOU 1363 CB MET A 181 3312 3030 5223 -1368 632 458 A C ATOM 1364 CG MET A 181 12.466 120.068 278.014 1.00 31.43 A C ANISOU 1364 CG MET A 181 3414 3174 5353 -1501 800 661 A C ATOM 1365 SD MET A 181 10.744 120.537 278.269 1.00 42.47 A S ANISOU 1365 SD MET A 181 4516 4823 6796 -1599 909 700 A S ATOM 1366 CE MET A 181 10.004 119.972 276.739 1.00 33.25 A C ANISOU 1366 CE MET A 181 3253 3570 5809 -1719 686 578 A C ATOM 1367 N GLY A 182 15.387 119.741 274.275 1.00 28.16 A N ANISOU 1367 N GLY A 182 3375 2440 4885 -1158 224 116 A N ATOM 1368 CA GLY A 182 15.824 120.014 272.922 1.00 26.28 A C ANISOU 1368 CA GLY A 182 3146 2231 4609 -1074 77 -70 A C ATOM 1369 C GLY A 182 17.325 119.881 272.794 1.00 28.82 A C ANISOU 1369 C GLY A 182 3641 2514 4797 -904 37 -135 A C ATOM 1370 O GLY A 182 18.087 120.594 273.457 1.00 31.69 A O ANISOU 1370 O GLY A 182 4041 2983 5018 -787 116 -79 A O ATOM 1371 N GLY A 183 17.746 118.982 271.911 1.00 33.27 A N ANISOU 1371 N GLY A 183 4299 2938 5403 -888 -92 -269 A N ATOM 1372 CA GLY A 183 19.154 118.735 271.673 1.00 31.10 A C ANISOU 1372 CA GLY A 183 4161 2637 5017 -712 -133 -351 A C ATOM 1373 C GLY A 183 19.641 119.508 270.464 1.00 28.03 A C ANISOU 1373 C GLY A 183 3724 2434 4491 -616 -204 -510 A C ATOM 1374 O GLY A 183 20.527 119.052 269.735 1.00 27.88 A O ANISOU 1374 O GLY A 183 3786 2396 4410 -504 -276 -651 A O ATOM 1375 N GLY A 184 19.021 120.659 270.222 1.00 27.49 A N ANISOU 1375 N GLY A 184 3518 2548 4378 -658 -184 -485 A N ATOM 1376 CA GLY A 184 19.495 121.584 269.207 1.00 29.37 A C ANISOU 1376 CA GLY A 184 3710 2982 4467 -580 -240 -577 A C ATOM 1377 C GLY A 184 20.659 122.435 269.695 1.00 25.92 A C ANISOU 1377 C GLY A 184 3305 2674 3870 -453 -171 -518 A C ATOM 1378 O GLY A 184 21.154 122.263 270.814 1.00 28.91 A O ANISOU 1378 O GLY A 184 3747 2995 4242 -410 -89 -422 A O ATOM 1379 N ILE A 185 21.073 123.389 268.871 1.00 21.78 A N ANISOU 1379 N ILE A 185 2732 2332 3212 -409 -211 -559 A N ATOM 1380 CA ILE A 185 22.266 124.175 269.163 1.00 19.06 A C ANISOU 1380 CA ILE A 185 2411 2117 2715 -315 -168 -514 A C ATOM 1381 C ILE A 185 22.121 125.061 270.414 1.00 18.14 A C ANISOU 1381 C ILE A 185 2283 2007 2602 -327 -72 -376 A C ATOM 1382 O ILE A 185 22.999 125.066 271.277 1.00 20.33 A O ANISOU 1382 O ILE A 185 2621 2290 2814 -268 -19 -323 A O ATOM 1383 CB ILE A 185 22.709 124.993 267.922 1.00 24.50 A C ANISOU 1383 CB ILE A 185 3048 3003 3257 -297 -238 -569 A C ATOM 1384 CG1 ILE A 185 23.172 124.036 266.815 1.00 23.21 A C ANISOU 1384 CG1 ILE A 185 2917 2868 3035 -249 -309 -733 A C ATOM 1385 CG2 ILE A 185 23.796 126.007 268.288 1.00 19.42 A C ANISOU 1385 CG2 ILE A 185 2405 2497 2477 -249 -196 -489 A C ATOM 1386 CD1 ILE A 185 23.547 124.713 265.510 1.00 24.03 A C ANISOU 1386 CD1 ILE A 185 2968 3198 2963 -246 -372 -785 A C ATOM 1387 N ILE A 186 21.011 125.790 270.512 1.00 18.31 A N ANISOU 1387 N ILE A 186 2225 2036 2697 -394 -56 -329 A N ATOM 1388 CA ILE A 186 20.780 126.709 271.625 1.00 19.69 A C ANISOU 1388 CA ILE A 186 2389 2222 2869 -390 39 -235 A C ATOM 1389 C ILE A 186 20.795 125.972 272.973 1.00 19.92 A C ANISOU 1389 C ILE A 186 2483 2159 2928 -394 142 -167 A C ATOM 1390 O ILE A 186 21.495 126.368 273.926 1.00 20.65 A O ANISOU 1390 O ILE A 186 2638 2284 2923 -350 201 -116 A O ATOM 1391 CB ILE A 186 19.436 127.453 271.430 1.00 24.22 A C ANISOU 1391 CB ILE A 186 2845 2810 3547 -434 39 -215 A C ATOM 1392 CG1 ILE A 186 19.569 128.499 270.321 1.00 23.63 A C ANISOU 1392 CG1 ILE A 186 2729 2835 3413 -416 -63 -232 A C ATOM 1393 CG2 ILE A 186 18.967 128.098 272.730 1.00 17.38 A C ANISOU 1393 CG2 ILE A 186 1966 1931 2705 -418 165 -148 A C ATOM 1394 CD1 ILE A 186 18.247 129.133 269.932 1.00 26.99 A C ANISOU 1394 CD1 ILE A 186 3026 3273 3957 -438 -99 -211 A C ATOM 1395 N GLY A 187 20.047 124.874 273.027 1.00 20.86 A N ANISOU 1395 N GLY A 187 2591 2164 3173 -461 149 -161 A N ATOM 1396 CA GLY A 187 20.015 124.026 274.205 1.00 23.17 A C ANISOU 1396 CA GLY A 187 2951 2356 3498 -487 234 -68 A C ATOM 1397 C GLY A 187 21.378 123.507 274.633 1.00 24.47 A C ANISOU 1397 C GLY A 187 3243 2494 3561 -396 219 -48 A C ATOM 1398 O GLY A 187 21.743 123.584 275.807 1.00 22.24 A O ANISOU 1398 O GLY A 187 3019 2228 3204 -374 293 50 A O ATOM 1399 N LEU A 188 22.135 122.967 273.685 1.00 22.11 A N ANISOU 1399 N LEU A 188 2979 2171 3249 -333 120 -145 A N ATOM 1400 CA LEU A 188 23.465 122.452 273.996 1.00 24.61 A C ANISOU 1400 CA LEU A 188 3387 2480 3485 -217 97 -136 A C ATOM 1401 C LEU A 188 24.425 123.548 274.453 1.00 24.75 A C ANISOU 1401 C LEU A 188 3396 2674 3337 -155 120 -102 A C ATOM 1402 O LEU A 188 25.249 123.323 275.346 1.00 16.64 A O ANISOU 1402 O LEU A 188 2429 1657 2237 -93 135 -27 A O ATOM 1403 CB LEU A 188 24.048 121.697 272.799 1.00 22.87 A C ANISOU 1403 CB LEU A 188 3186 2223 3281 -140 -2 -279 A C ATOM 1404 CG LEU A 188 23.303 120.413 272.429 1.00 26.52 A C ANISOU 1404 CG LEU A 188 3698 2464 3913 -196 -50 -332 A C ATOM 1405 CD1 LEU A 188 23.865 119.814 271.151 1.00 23.85 A C ANISOU 1405 CD1 LEU A 188 3382 2113 3564 -104 -147 -521 A C ATOM 1406 CD2 LEU A 188 23.396 119.414 273.570 1.00 27.87 A C ANISOU 1406 CD2 LEU A 188 3978 2444 4168 -190 -21 -201 A C ATOM 1407 N GLU A 189 24.339 124.721 273.830 1.00 16.69 A N ANISOU 1407 N GLU A 189 2301 1784 2257 -180 106 -149 A N ATOM 1408 CA GLU A 189 25.190 125.843 274.222 1.00 15.16 A C ANISOU 1408 CA GLU A 189 2103 1735 1924 -155 113 -119 A C ATOM 1409 C GLU A 189 24.894 126.279 275.659 1.00 17.50 A C ANISOU 1409 C GLU A 189 2443 2018 2186 -185 198 -28 A C ATOM 1410 O GLU A 189 25.812 126.459 276.485 1.00 24.13 A O ANISOU 1410 O GLU A 189 3333 2924 2913 -150 201 19 A O ATOM 1411 CB GLU A 189 25.054 127.011 273.228 1.00 16.64 A C ANISOU 1411 CB GLU A 189 2219 2027 2078 -194 70 -166 A C ATOM 1412 CG GLU A 189 25.669 126.720 271.834 1.00 19.01 A C ANISOU 1412 CG GLU A 189 2476 2414 2331 -159 -9 -251 A C ATOM 1413 CD GLU A 189 25.580 127.908 270.872 1.00 26.94 A C ANISOU 1413 CD GLU A 189 3419 3538 3280 -213 -58 -256 A C ATOM 1414 OE1 GLU A 189 25.016 128.961 271.254 1.00 34.11 A O ANISOU 1414 OE1 GLU A 189 4321 4425 4212 -264 -43 -201 A O ATOM 1415 OE2 GLU A 189 26.083 127.797 269.732 1.00 22.78 A O1- ANISOU 1415 OE2 GLU A 189 2852 3126 2677 -197 -112 -313 A O1- ATOM 1416 N MET A 190 23.607 126.436 275.963 1.00 16.26 A N ANISOU 1416 N MET A 190 2259 1799 2118 -249 267 -9 A N ATOM 1417 CA MET A 190 23.218 126.815 277.320 1.00 19.59 A C ANISOU 1417 CA MET A 190 2718 2234 2491 -270 371 59 A C ATOM 1418 C MET A 190 23.633 125.749 278.337 1.00 22.84 A C ANISOU 1418 C MET A 190 3216 2601 2859 -257 404 160 A C ATOM 1419 O MET A 190 24.094 126.062 279.449 1.00 26.02 A O ANISOU 1419 O MET A 190 3684 3075 3129 -243 444 216 A O ATOM 1420 CB MET A 190 21.714 127.051 277.375 1.00 23.01 A C ANISOU 1420 CB MET A 190 3070 2633 3039 -328 452 58 A C ATOM 1421 CG MET A 190 21.276 128.239 276.544 1.00 20.19 A C ANISOU 1421 CG MET A 190 2634 2316 2722 -321 413 -17 A C ATOM 1422 SD MET A 190 22.104 129.764 277.040 1.00 31.70 A S ANISOU 1422 SD MET A 190 4157 3851 4037 -279 402 -50 A S ATOM 1423 CE MET A 190 23.363 129.927 275.777 1.00 25.96 A C ANISOU 1423 CE MET A 190 3434 3176 3255 -273 255 -76 A C ATOM 1424 N GLY A 191 23.484 124.489 277.937 1.00 20.97 A N ANISOU 1424 N GLY A 191 2993 2242 2734 -262 371 184 A N ATOM 1425 CA GLY A 191 23.915 123.374 278.758 1.00 23.88 A C ANISOU 1425 CA GLY A 191 3457 2528 3089 -240 374 299 A C ATOM 1426 C GLY A 191 25.401 123.457 279.050 1.00 20.83 A C ANISOU 1426 C GLY A 191 3122 2228 2565 -132 304 311 A C ATOM 1427 O GLY A 191 25.840 123.183 280.163 1.00 21.42 A O ANISOU 1427 O GLY A 191 3270 2325 2542 -111 321 427 A O ATOM 1428 N THR A 192 26.173 123.838 278.040 1.00 18.25 A N ANISOU 1428 N THR A 192 2742 1972 2218 -69 224 202 A N ATOM 1429 CA THR A 192 27.618 123.991 278.174 1.00 25.89 A C ANISOU 1429 CA THR A 192 3712 3062 3063 27 154 205 A C ATOM 1430 C THR A 192 27.940 125.080 279.197 1.00 23.74 A C ANISOU 1430 C THR A 192 3457 2931 2631 -14 181 249 A C ATOM 1431 O THR A 192 28.749 124.884 280.141 1.00 20.72 A O ANISOU 1431 O THR A 192 3122 2613 2137 29 152 334 A O ATOM 1432 CB THR A 192 28.253 124.314 276.801 1.00 22.08 A C ANISOU 1432 CB THR A 192 3141 2668 2579 74 86 79 A C ATOM 1433 CG2 THR A 192 29.772 124.431 276.908 1.00 16.45 A C ANISOU 1433 CG2 THR A 192 2391 2113 1747 168 21 88 A C ATOM 1434 OG1 THR A 192 27.912 123.279 275.865 1.00 22.77 A O ANISOU 1434 OG1 THR A 192 3229 2624 2797 115 58 6 A O ATOM 1435 N VAL A 193 27.283 126.226 279.017 1.00 23.55 A N ANISOU 1435 N VAL A 193 3401 2948 2600 -93 225 187 A N ATOM 1436 CA VAL A 193 27.479 127.343 279.936 1.00 24.28 A C ANISOU 1436 CA VAL A 193 3528 3144 2555 -135 247 189 A C ATOM 1437 C VAL A 193 27.194 126.944 281.383 1.00 23.40 A C ANISOU 1437 C VAL A 193 3505 3031 2354 -146 319 288 A C ATOM 1438 O VAL A 193 28.036 127.133 282.267 1.00 21.69 A O ANISOU 1438 O VAL A 193 3341 2919 1982 -133 281 331 A O ATOM 1439 CB VAL A 193 26.590 128.550 279.584 1.00 20.10 A C ANISOU 1439 CB VAL A 193 2967 2602 2067 -197 291 105 A C ATOM 1440 CG1 VAL A 193 26.662 129.596 280.700 1.00 19.08 A C ANISOU 1440 CG1 VAL A 193 2906 2540 1804 -229 325 85 A C ATOM 1441 CG2 VAL A 193 27.009 129.149 278.260 1.00 16.69 A C ANISOU 1441 CG2 VAL A 193 2462 2204 1674 -205 207 38 A C ATOM 1442 N TYR A 194 26.006 126.406 281.632 1.00 25.87 A N ANISOU 1442 N TYR A 194 3826 3248 2753 -182 420 333 A N ATOM 1443 CA TYR A 194 25.630 126.100 283.011 1.00 27.22 A C ANISOU 1443 CA TYR A 194 4075 3450 2816 -211 511 441 A C ATOM 1444 C TYR A 194 26.403 124.934 283.611 1.00 27.28 A C ANISOU 1444 C TYR A 194 4158 3438 2770 -167 453 592 A C ATOM 1445 O TYR A 194 26.642 124.892 284.820 1.00 24.03 A O ANISOU 1445 O TYR A 194 3825 3116 2189 -176 478 690 A O ATOM 1446 CB TYR A 194 24.123 125.910 283.141 1.00 26.47 A C ANISOU 1446 CB TYR A 194 3941 3294 2821 -281 650 463 A C ATOM 1447 CG TYR A 194 23.407 127.228 283.216 1.00 27.17 A C ANISOU 1447 CG TYR A 194 3983 3453 2886 -296 731 341 A C ATOM 1448 CD1 TYR A 194 23.223 127.866 284.437 1.00 24.54 A C ANISOU 1448 CD1 TYR A 194 3708 3238 2379 -302 829 332 A C ATOM 1449 CD2 TYR A 194 22.956 127.862 282.063 1.00 24.36 A C ANISOU 1449 CD2 TYR A 194 3533 3047 2673 -291 699 229 A C ATOM 1450 CE1 TYR A 194 22.584 129.084 284.512 1.00 26.16 A C ANISOU 1450 CE1 TYR A 194 3881 3484 2575 -287 900 197 A C ATOM 1451 CE2 TYR A 194 22.316 129.083 282.128 1.00 20.92 A C ANISOU 1451 CE2 TYR A 194 3061 2648 2237 -280 758 124 A C ATOM 1452 CZ TYR A 194 22.134 129.686 283.355 1.00 25.50 A C ANISOU 1452 CZ TYR A 194 3702 3320 2664 -269 860 99 A C ATOM 1453 OH TYR A 194 21.496 130.897 283.436 1.00 24.72 A O ANISOU 1453 OH TYR A 194 3578 3235 2579 -231 917 -28 A O ATOM 1454 N HIS A 195 26.795 123.983 282.773 1.00 25.92 A N ANISOU 1454 N HIS A 195 3966 3146 2735 -108 370 607 A N ATOM 1455 CA HIS A 195 27.636 122.904 283.261 1.00 25.96 A C ANISOU 1455 CA HIS A 195 4042 3109 2714 -28 291 744 A C ATOM 1456 C HIS A 195 28.958 123.467 283.738 1.00 27.29 A C ANISOU 1456 C HIS A 195 4210 3457 2702 38 198 743 A C ATOM 1457 O HIS A 195 29.455 123.074 284.794 1.00 27.45 A O ANISOU 1457 O HIS A 195 4303 3534 2593 65 164 883 A O ATOM 1458 CB HIS A 195 27.889 121.830 282.206 1.00 25.72 A C ANISOU 1458 CB HIS A 195 3994 2905 2873 54 210 718 A C ATOM 1459 CG HIS A 195 28.755 120.717 282.699 1.00 26.87 A C ANISOU 1459 CG HIS A 195 4215 2977 3017 169 118 857 A C ATOM 1460 CD2 HIS A 195 28.454 119.585 283.382 1.00 27.30 A C ANISOU 1460 CD2 HIS A 195 4377 2867 3128 162 117 1038 A C ATOM 1461 ND1 HIS A 195 30.124 120.710 282.532 1.00 30.55 A N ANISOU 1461 ND1 HIS A 195 4641 3545 3423 313 4 832 A N ATOM 1462 CE1 HIS A 195 30.625 119.618 283.077 1.00 32.74 A C ANISOU 1462 CE1 HIS A 195 4995 3717 3727 416 -70 983 A C ATOM 1463 NE2 HIS A 195 29.635 118.919 283.600 1.00 35.29 A N ANISOU 1463 NE2 HIS A 195 5422 3864 4121 323 -7 1117 A N ATOM 1464 N ALA A 196 29.540 124.379 282.961 1.00 27.70 A N ANISOU 1464 N ALA A 196 4175 3609 2740 51 146 601 A N ATOM 1465 CA ALA A 196 30.793 124.977 283.420 1.00 29.69 A C ANISOU 1465 CA ALA A 196 4406 4047 2826 81 50 601 A C ATOM 1466 C ALA A 196 30.640 125.691 284.770 1.00 29.64 A C ANISOU 1466 C ALA A 196 4485 4159 2617 0 87 639 A C ATOM 1467 O ALA A 196 31.595 125.773 285.546 1.00 29.51 A O ANISOU 1467 O ALA A 196 4489 4283 2440 22 -3 699 A O ATOM 1468 CB ALA A 196 31.333 125.926 282.391 1.00 27.75 A C ANISOU 1468 CB ALA A 196 4053 3893 2598 64 1 462 A C ATOM 1469 N LEU A 197 29.449 126.220 285.039 1.00 32.29 A N ANISOU 1469 N LEU A 197 4498 5360 2410 -638 -27 144 A N ATOM 1470 CA LEU A 197 29.185 126.915 286.302 1.00 30.49 A C ANISOU 1470 CA LEU A 197 4316 5249 2020 -725 43 77 A C ATOM 1471 C LEU A 197 28.831 126.009 287.483 1.00 33.01 A C ANISOU 1471 C LEU A 197 4684 5640 2219 -661 101 217 A C ATOM 1472 O LEU A 197 28.682 126.487 288.607 1.00 33.08 A O ANISOU 1472 O LEU A 197 4731 5774 2062 -722 156 172 A O ATOM 1473 CB LEU A 197 28.112 127.989 286.105 1.00 28.76 A C ANISOU 1473 CB LEU A 197 4139 4868 1921 -818 149 -63 A C ATOM 1474 CG LEU A 197 28.581 129.083 285.144 1.00 31.17 A C ANISOU 1474 CG LEU A 197 4415 5130 2297 -892 105 -206 A C ATOM 1475 CD1 LEU A 197 27.532 130.179 284.966 1.00 31.67 A C ANISOU 1475 CD1 LEU A 197 4533 5029 2473 -956 223 -330 A C ATOM 1476 CD2 LEU A 197 29.897 129.666 285.646 1.00 29.04 A C ANISOU 1476 CD2 LEU A 197 4119 5096 1819 -978 27 -284 A C ATOM 1477 N GLY A 198 28.687 124.710 287.240 1.00 32.52 A N ANISOU 1477 N GLY A 198 4631 5490 2234 -541 100 385 A N ATOM 1478 CA GLY A 198 28.440 123.785 288.334 1.00 32.02 A C ANISOU 1478 CA GLY A 198 4624 5488 2053 -469 161 542 A C ATOM 1479 C GLY A 198 27.113 123.055 288.264 1.00 34.07 A C ANISOU 1479 C GLY A 198 4942 5519 2485 -451 284 626 A C ATOM 1480 O GLY A 198 26.847 122.180 289.086 1.00 32.20 A O ANISOU 1480 O GLY A 198 4762 5297 2175 -391 352 775 A O ATOM 1481 N SER A 199 26.261 123.424 287.311 1.00 29.08 A N ANISOU 1481 N SER A 199 4292 4686 2073 -508 319 533 A N ATOM 1482 CA SER A 199 24.979 122.740 287.156 1.00 33.09 A C ANISOU 1482 CA SER A 199 4829 4993 2751 -511 429 599 A C ATOM 1483 C SER A 199 25.161 121.313 286.657 1.00 33.47 A C ANISOU 1483 C SER A 199 4905 4921 2890 -418 410 751 A C ATOM 1484 O SER A 199 26.050 121.028 285.848 1.00 33.03 A O ANISOU 1484 O SER A 199 4826 4863 2862 -354 305 759 A O ATOM 1485 CB SER A 199 24.044 123.499 286.209 1.00 33.03 A C ANISOU 1485 CB SER A 199 4773 4832 2943 -586 459 464 A C ATOM 1486 OG SER A 199 23.646 124.743 286.757 1.00 35.73 A O ANISOU 1486 OG SER A 199 5115 5241 3220 -660 520 338 A O ATOM 1487 N GLN A 200 24.312 120.422 287.150 1.00 31.06 A N ANISOU 1487 N GLN A 200 4659 4510 2632 -414 524 870 A N ATOM 1488 CA GLN A 200 24.206 119.081 286.604 1.00 34.15 A C ANISOU 1488 CA GLN A 200 5100 4724 3153 -355 543 994 A C ATOM 1489 C GLN A 200 23.205 119.137 285.449 1.00 30.54 A C ANISOU 1489 C GLN A 200 4595 4068 2941 -442 563 895 A C ATOM 1490 O GLN A 200 22.107 119.679 285.603 1.00 30.53 A O ANISOU 1490 O GLN A 200 4555 4036 3008 -537 644 825 A O ATOM 1491 CB GLN A 200 23.767 118.121 287.705 1.00 42.63 A C ANISOU 1491 CB GLN A 200 6268 5774 4156 -327 670 1169 A C ATOM 1492 CG GLN A 200 23.808 116.655 287.343 1.00 53.34 A C ANISOU 1492 CG GLN A 200 7711 6942 5613 -255 709 1321 A C ATOM 1493 CD GLN A 200 23.259 115.799 288.462 1.00 65.60 A C ANISOU 1493 CD GLN A 200 9366 8455 7104 -243 859 1497 A C ATOM 1494 NE2 GLN A 200 22.605 114.700 288.103 1.00 69.34 A N ANISOU 1494 NE2 GLN A 200 9914 8688 7743 -270 956 1580 A N ATOM 1495 OE1 GLN A 200 23.402 116.134 289.640 1.00 67.72 A O ANISOU 1495 OE1 GLN A 200 9649 8909 7172 -219 894 1553 A O ATOM 1496 N ILE A 201 23.595 118.609 284.291 1.00 29.29 A N ANISOU 1496 N ILE A 201 4430 3794 2904 -402 487 884 A N ATOM 1497 CA ILE A 201 22.826 118.807 283.061 1.00 30.76 A C ANISOU 1497 CA ILE A 201 4552 3839 3295 -479 472 768 A C ATOM 1498 C ILE A 201 22.166 117.524 282.537 1.00 32.05 A C ANISOU 1498 C ILE A 201 4765 3789 3622 -507 533 830 A C ATOM 1499 O ILE A 201 22.841 116.524 282.285 1.00 33.23 A O ANISOU 1499 O ILE A 201 4996 3857 3774 -424 512 918 A O ATOM 1500 CB ILE A 201 23.717 119.393 281.931 1.00 29.55 A C ANISOU 1500 CB ILE A 201 4341 3726 3163 -437 332 664 A C ATOM 1501 CG1 ILE A 201 24.454 120.651 282.399 1.00 28.21 A C ANISOU 1501 CG1 ILE A 201 4129 3755 2835 -433 274 592 A C ATOM 1502 CG2 ILE A 201 22.893 119.680 280.674 1.00 24.84 A C ANISOU 1502 CG2 ILE A 201 3672 3011 2756 -508 313 546 A C ATOM 1503 CD1 ILE A 201 23.545 121.809 282.751 1.00 26.12 A C ANISOU 1503 CD1 ILE A 201 3820 3524 2581 -527 339 487 A C ATOM 1504 N ASP A 202 20.844 117.559 282.383 1.00 28.26 A N ANISOU 1504 N ASP A 202 4238 3223 3275 -625 615 782 A N ATOM 1505 CA ASP A 202 20.128 116.510 281.655 1.00 28.84 A C ANISOU 1505 CA ASP A 202 4333 3101 3524 -696 659 791 A C ATOM 1506 C ASP A 202 19.635 117.120 280.340 1.00 31.43 A C ANISOU 1506 C ASP A 202 4541 3411 3989 -757 581 632 A C ATOM 1507 O ASP A 202 19.211 118.271 280.318 1.00 33.76 A O ANISOU 1507 O ASP A 202 4735 3815 4277 -784 567 544 A O ATOM 1508 CB ASP A 202 18.938 115.992 282.471 1.00 33.06 A C ANISOU 1508 CB ASP A 202 4885 3571 4106 -802 817 863 A C ATOM 1509 CG ASP A 202 19.349 115.021 283.579 1.00 40.81 A C ANISOU 1509 CG ASP A 202 6013 4513 4981 -741 911 1047 A C ATOM 1510 OD1 ASP A 202 20.562 114.793 283.774 1.00 41.41 A O ANISOU 1510 OD1 ASP A 202 6165 4634 4935 -602 848 1123 A O ATOM 1511 OD2 ASP A 202 18.446 114.493 284.268 1.00 41.79 A O1- ANISOU 1511 OD2 ASP A 202 6168 4572 5138 -827 1053 1126 A O1- ATOM 1512 N VAL A 203 19.716 116.376 279.240 1.00 28.32 A N ANISOU 1512 N VAL A 203 4166 2886 3711 -769 533 596 A N ATOM 1513 CA VAL A 203 19.172 116.857 277.964 1.00 26.47 A C ANISOU 1513 CA VAL A 203 3814 2646 3597 -829 460 453 A C ATOM 1514 C VAL A 203 18.166 115.847 277.424 1.00 32.40 A C ANISOU 1514 C VAL A 203 4562 3246 4503 -960 518 429 A C ATOM 1515 O VAL A 203 18.497 114.674 277.247 1.00 35.10 A O ANISOU 1515 O VAL A 203 5023 3432 4881 -959 543 478 A O ATOM 1516 CB VAL A 203 20.281 117.087 276.912 1.00 25.21 A C ANISOU 1516 CB VAL A 203 3656 2505 3416 -729 322 392 A C ATOM 1517 CG1 VAL A 203 19.684 117.567 275.583 1.00 24.37 A C ANISOU 1517 CG1 VAL A 203 3433 2406 3421 -784 250 255 A C ATOM 1518 CG2 VAL A 203 21.312 118.079 277.429 1.00 24.27 A C ANISOU 1518 CG2 VAL A 203 3533 2545 3144 -626 266 407 A C ATOM 1519 N VAL A 204 16.939 116.294 277.166 1.00 27.76 A N ANISOU 1519 N VAL A 204 3839 2704 4004 -1075 546 352 A N ATOM 1520 CA VAL A 204 15.933 115.399 276.589 1.00 30.62 A C ANISOU 1520 CA VAL A 204 4169 2955 4511 -1229 591 307 A C ATOM 1521 C VAL A 204 15.648 115.778 275.130 1.00 35.43 A C ANISOU 1521 C VAL A 204 4655 3608 5200 -1258 474 161 A C ATOM 1522 O VAL A 204 15.391 116.944 274.819 1.00 39.68 A O ANISOU 1522 O VAL A 204 5061 4296 5720 -1217 418 101 A O ATOM 1523 CB VAL A 204 14.633 115.355 277.449 1.00 34.14 A C ANISOU 1523 CB VAL A 204 4541 3431 5001 -1360 730 346 A C ATOM 1524 CG1 VAL A 204 13.973 116.725 277.520 1.00 30.48 A C ANISOU 1524 CG1 VAL A 204 3905 3158 4517 -1342 716 288 A C ATOM 1525 CG2 VAL A 204 13.657 114.299 276.927 1.00 34.68 A C ANISOU 1525 CG2 VAL A 204 4583 3380 5215 -1549 787 303 A C ATOM 1526 N GLU A 205 15.750 114.800 274.233 1.00 29.92 A N ANISOU 1526 N GLU A 205 4013 2776 4577 -1315 442 108 A N ATOM 1527 CA GLU A 205 15.583 115.051 272.801 1.00 29.55 A C ANISOU 1527 CA GLU A 205 3865 2777 4584 -1336 324 -31 A C ATOM 1528 C GLU A 205 14.807 113.928 272.118 1.00 37.11 A C ANISOU 1528 C GLU A 205 4823 3616 5661 -1516 351 -112 A C ATOM 1529 O GLU A 205 15.112 112.749 272.305 1.00 34.19 A O ANISOU 1529 O GLU A 205 4617 3050 5323 -1559 419 -74 A O ATOM 1530 CB GLU A 205 16.941 115.246 272.119 1.00 31.20 A C ANISOU 1530 CB GLU A 205 4152 2979 4722 -1177 211 -48 A C ATOM 1531 CG GLU A 205 16.893 115.207 270.597 1.00 32.98 A C ANISOU 1531 CG GLU A 205 4316 3220 4996 -1198 100 -183 A C ATOM 1532 CD GLU A 205 16.070 116.342 270.014 1.00 38.48 A C ANISOU 1532 CD GLU A 205 4811 4105 5707 -1217 37 -261 A C ATOM 1533 OE1 GLU A 205 16.286 117.505 270.422 1.00 41.28 A O ANISOU 1533 OE1 GLU A 205 5110 4579 5995 -1115 24 -222 A O ATOM 1534 OE2 GLU A 205 15.212 116.072 269.145 1.00 36.68 A O1- ANISOU 1534 OE2 GLU A 205 4480 3907 5550 -1331 3 -362 A O1- ATOM 1535 N MET A 206 13.808 114.302 271.326 1.00 39.99 A N ANISOU 1535 N MET A 206 5005 4101 6087 -1619 301 -224 A N ATOM 1536 CA MET A 206 12.936 113.339 270.663 1.00 45.86 A C ANISOU 1536 CA MET A 206 5713 4775 6937 -1824 319 -325 A C ATOM 1537 C MET A 206 13.643 112.623 269.513 1.00 41.79 A C ANISOU 1537 C MET A 206 5308 4138 6431 -1815 237 -423 A C ATOM 1538 O MET A 206 13.353 111.465 269.217 1.00 35.82 A O ANISOU 1538 O MET A 206 4639 3220 5751 -1970 288 -483 A O ATOM 1539 CB MET A 206 11.698 114.061 270.126 1.00 54.20 A C ANISOU 1539 CB MET A 206 6510 6051 8031 -1916 273 -414 A C ATOM 1540 CG MET A 206 10.862 113.249 269.149 1.00 62.59 A C ANISOU 1540 CG MET A 206 7495 7109 9178 -2121 242 -554 A C ATOM 1541 SD MET A 206 9.645 112.231 269.989 1.00136.44 A S ANISOU 1541 SD MET A 206 16838 16403 18602 -2310 378 -497 A S ATOM 1542 CE MET A 206 8.503 113.510 270.499 1.00 75.33 A C ANISOU 1542 CE MET A 206 8818 8948 10857 -2307 403 -463 A C ATOM 1543 N PHE A 207 14.605 113.292 268.890 1.00 39.78 A N ANISOU 1543 N PHE A 207 5064 3951 6098 -1636 121 -439 A N ATOM 1544 CA PHE A 207 15.274 112.701 267.741 1.00 34.39 A C ANISOU 1544 CA PHE A 207 4474 3179 5414 -1612 43 -537 A C ATOM 1545 C PHE A 207 16.345 111.727 268.230 1.00 32.44 A C ANISOU 1545 C PHE A 207 4474 2701 5151 -1530 116 -452 A C ATOM 1546 O PHE A 207 16.625 111.654 269.430 1.00 36.03 A O ANISOU 1546 O PHE A 207 5010 3099 5579 -1475 208 -310 A O ATOM 1547 CB PHE A 207 15.877 113.817 266.886 1.00 31.90 A C ANISOU 1547 CB PHE A 207 4067 3036 5018 -1449 -97 -576 A C ATOM 1548 CG PHE A 207 16.112 113.436 265.453 1.00 34.44 A C ANISOU 1548 CG PHE A 207 4398 3349 5337 -1462 -196 -715 A C ATOM 1549 CD1 PHE A 207 15.048 113.121 264.614 1.00 34.36 A C ANISOU 1549 CD1 PHE A 207 4270 3404 5382 -1638 -233 -855 A C ATOM 1550 CD2 PHE A 207 17.399 113.425 264.934 1.00 33.19 A C ANISOU 1550 CD2 PHE A 207 4355 3144 5110 -1297 -254 -711 A C ATOM 1551 CE1 PHE A 207 15.268 112.781 263.285 1.00 34.92 A C ANISOU 1551 CE1 PHE A 207 4353 3484 5433 -1652 -326 -994 A C ATOM 1552 CE2 PHE A 207 17.627 113.093 263.608 1.00 33.69 A C ANISOU 1552 CE2 PHE A 207 4432 3209 5161 -1300 -338 -841 A C ATOM 1553 CZ PHE A 207 16.561 112.771 262.782 1.00 34.38 A C ANISOU 1553 CZ PHE A 207 4414 3353 5295 -1478 -375 -986 A C ATOM 1554 N ASP A 208 16.927 110.962 267.311 1.00 31.49 A N ANISOU 1554 N ASP A 208 4472 2453 5039 -1514 81 -535 A N ATOM 1555 CA ASP A 208 17.867 109.913 267.700 1.00 38.81 A C ANISOU 1555 CA ASP A 208 5641 3144 5961 -1429 166 -455 A C ATOM 1556 C ASP A 208 19.286 110.443 267.735 1.00 36.10 A C ANISOU 1556 C ASP A 208 5348 2860 5506 -1175 100 -370 A C ATOM 1557 O ASP A 208 20.240 109.679 267.894 1.00 31.12 A O ANISOU 1557 O ASP A 208 4899 2074 4851 -1054 148 -302 A O ATOM 1558 CB ASP A 208 17.790 108.711 266.750 1.00 36.30 A C ANISOU 1558 CB ASP A 208 5453 2626 5712 -1539 189 -589 A C ATOM 1559 CG ASP A 208 18.347 109.015 265.363 1.00 42.20 A C ANISOU 1559 CG ASP A 208 6164 3461 6409 -1454 52 -722 A C ATOM 1560 OD1 ASP A 208 18.316 110.190 264.930 1.00 41.40 A O ANISOU 1560 OD1 ASP A 208 5881 3600 6249 -1390 -68 -748 A O ATOM 1561 OD2 ASP A 208 18.845 108.071 264.712 1.00 50.46 A O1- ANISOU 1561 OD2 ASP A 208 7376 4327 7471 -1441 75 -794 A O1- ATOM 1562 N GLN A 209 19.410 111.757 267.579 1.00 30.61 A N ANISOU 1562 N GLN A 209 4492 2395 4745 -1094 -2 -374 A N ATOM 1563 CA GLN A 209 20.705 112.405 267.481 1.00 28.94 A C ANISOU 1563 CA GLN A 209 4294 2275 4427 -884 -76 -317 A C ATOM 1564 C GLN A 209 20.553 113.864 267.892 1.00 27.65 A C ANISOU 1564 C GLN A 209 3969 2330 4206 -845 -127 -282 A C ATOM 1565 O GLN A 209 19.532 114.477 267.587 1.00 29.94 A O ANISOU 1565 O GLN A 209 4112 2727 4536 -947 -154 -352 A O ATOM 1566 CB GLN A 209 21.121 112.349 266.013 1.00 30.44 A C ANISOU 1566 CB GLN A 209 4477 2483 4606 -843 -175 -446 A C ATOM 1567 CG GLN A 209 22.525 112.780 265.698 1.00 31.62 A C ANISOU 1567 CG GLN A 209 4656 2704 4656 -637 -242 -404 A C ATOM 1568 CD GLN A 209 22.665 113.200 264.243 1.00 33.42 A C ANISOU 1568 CD GLN A 209 4807 3031 4861 -614 -353 -534 A C ATOM 1569 NE2 GLN A 209 22.933 114.484 264.022 1.00 25.77 A N ANISOU 1569 NE2 GLN A 209 3707 2256 3827 -541 -434 -522 A N ATOM 1570 OE1 GLN A 209 22.537 112.380 263.329 1.00 31.61 A O ANISOU 1570 OE1 GLN A 209 4644 2699 4666 -663 -360 -645 A O ATOM 1571 N VAL A 210 21.549 114.426 268.580 1.00 24.40 A N ANISOU 1571 N VAL A 210 3583 1990 3697 -699 -136 -177 A N ATOM 1572 CA VAL A 210 21.593 115.876 268.783 1.00 22.88 A C ANISOU 1572 CA VAL A 210 3260 1990 3443 -655 -189 -168 A C ATOM 1573 C VAL A 210 22.040 116.551 267.488 1.00 24.57 A C ANISOU 1573 C VAL A 210 3402 2303 3631 -589 -303 -257 A C ATOM 1574 O VAL A 210 22.614 115.884 266.623 1.00 26.77 A O ANISOU 1574 O VAL A 210 3747 2515 3910 -543 -340 -304 A O ATOM 1575 CB VAL A 210 22.523 116.293 269.938 1.00 29.64 A C ANISOU 1575 CB VAL A 210 4163 2907 4192 -546 -164 -45 A C ATOM 1576 CG1 VAL A 210 22.079 115.644 271.239 1.00 24.96 A C ANISOU 1576 CG1 VAL A 210 3646 2231 3608 -599 -47 56 A C ATOM 1577 CG2 VAL A 210 23.972 115.960 269.611 1.00 22.09 A C ANISOU 1577 CG2 VAL A 210 3289 1944 3159 -395 -212 -9 A C ATOM 1578 N ILE A 211 21.774 117.856 267.364 1.00 25.53 A N ANISOU 1578 N ILE A 211 3398 2575 3726 -579 -344 -277 A N ATOM 1579 CA ILE A 211 22.048 118.620 266.138 1.00 24.46 A C ANISOU 1579 CA ILE A 211 3185 2542 3566 -522 -440 -350 A C ATOM 1580 C ILE A 211 21.684 117.774 264.913 1.00 26.56 A C ANISOU 1580 C ILE A 211 3455 2751 3885 -572 -485 -454 A C ATOM 1581 O ILE A 211 22.568 117.352 264.151 1.00 23.17 A O ANISOU 1581 O ILE A 211 3092 2290 3421 -495 -530 -483 A O ATOM 1582 CB ILE A 211 23.517 119.084 266.053 1.00 25.28 A C ANISOU 1582 CB ILE A 211 3332 2701 3573 -386 -484 -307 A C ATOM 1583 CG1 ILE A 211 24.017 119.549 267.419 1.00 25.41 A C ANISOU 1583 CG1 ILE A 211 3377 2754 3524 -357 -432 -209 A C ATOM 1584 CG2 ILE A 211 23.670 120.201 265.014 1.00 23.50 A C ANISOU 1584 CG2 ILE A 211 3014 2597 3317 -338 -558 -358 A C ATOM 1585 CD1 ILE A 211 25.484 119.964 267.426 1.00 19.27 A C ANISOU 1585 CD1 ILE A 211 2624 2055 2643 -244 -475 -168 A C ATOM 1586 N PRO A 212 20.382 117.477 264.756 1.00 27.73 A N ANISOU 1586 N PRO A 212 3532 2893 4112 -708 -467 -516 A N ATOM 1587 CA PRO A 212 19.894 116.480 263.793 1.00 30.12 A C ANISOU 1587 CA PRO A 212 3849 3128 4468 -803 -493 -629 A C ATOM 1588 C PRO A 212 20.304 116.706 262.340 1.00 33.88 A C ANISOU 1588 C PRO A 212 4292 3683 4896 -738 -598 -721 A C ATOM 1589 O PRO A 212 20.444 115.730 261.603 1.00 32.83 A O ANISOU 1589 O PRO A 212 4238 3460 4777 -774 -613 -808 A O ATOM 1590 CB PRO A 212 18.362 116.554 263.934 1.00 29.44 A C ANISOU 1590 CB PRO A 212 3628 3102 4455 -961 -468 -672 A C ATOM 1591 CG PRO A 212 18.076 117.773 264.708 1.00 33.60 A C ANISOU 1591 CG PRO A 212 4058 3750 4961 -910 -444 -589 A C ATOM 1592 CD PRO A 212 19.284 118.093 265.523 1.00 28.78 A C ANISOU 1592 CD PRO A 212 3557 3096 4282 -784 -415 -485 A C ATOM 1593 N ALA A 213 20.493 117.952 261.923 1.00 33.93 A N ANISOU 1593 N ALA A 213 4197 3848 4846 -645 -659 -703 A N ATOM 1594 CA ALA A 213 20.875 118.198 260.533 1.00 30.74 A C ANISOU 1594 CA ALA A 213 3762 3531 4386 -577 -752 -777 A C ATOM 1595 C ALA A 213 22.323 117.808 260.235 1.00 29.90 A C ANISOU 1595 C ALA A 213 3785 3355 4219 -456 -763 -761 A C ATOM 1596 O ALA A 213 22.672 117.554 259.084 1.00 32.01 A O ANISOU 1596 O ALA A 213 4067 3648 4446 -417 -822 -839 A O ATOM 1597 CB ALA A 213 20.634 119.656 260.161 1.00 26.78 A C ANISOU 1597 CB ALA A 213 3125 3207 3842 -505 -798 -747 A C ATOM 1598 N ALA A 214 23.147 117.688 261.271 1.00 26.86 A N ANISOU 1598 N ALA A 214 3491 2895 3821 -396 -704 -660 A N ATOM 1599 CA ALA A 214 24.564 117.406 261.058 1.00 24.16 A C ANISOU 1599 CA ALA A 214 3244 2522 3412 -263 -713 -627 A C ATOM 1600 C ALA A 214 24.801 115.917 260.868 1.00 22.36 A C ANISOU 1600 C ALA A 214 3158 2122 3214 -271 -676 -671 A C ATOM 1601 O ALA A 214 24.021 115.086 261.349 1.00 24.60 A O ANISOU 1601 O ALA A 214 3496 2278 3575 -385 -616 -691 A O ATOM 1602 CB ALA A 214 25.392 117.935 262.210 1.00 23.48 A C ANISOU 1602 CB ALA A 214 3178 2463 3281 -189 -675 -502 A C ATOM 1603 N ASP A 215 25.876 115.594 260.151 1.00 27.06 A N ANISOU 1603 N ASP A 215 3821 2711 3751 -148 -699 -688 A N ATOM 1604 CA ASP A 215 26.233 114.213 259.813 1.00 29.90 A C ANISOU 1604 CA ASP A 215 4333 2897 4129 -123 -655 -737 A C ATOM 1605 C ASP A 215 26.516 113.328 261.030 1.00 33.70 A C ANISOU 1605 C ASP A 215 4947 3213 4646 -99 -553 -633 A C ATOM 1606 O ASP A 215 26.924 113.819 262.088 1.00 31.47 A O ANISOU 1606 O ASP A 215 4637 2987 4332 -45 -532 -505 A O ATOM 1607 CB ASP A 215 27.440 114.200 258.870 1.00 28.00 A C ANISOU 1607 CB ASP A 215 4125 2711 3804 37 -693 -756 A C ATOM 1608 CG ASP A 215 27.047 114.366 257.404 1.00 32.62 A C ANISOU 1608 CG ASP A 215 4657 3374 4362 0 -768 -900 A C ATOM 1609 OD1 ASP A 215 25.909 113.993 257.030 1.00 32.34 A O ANISOU 1609 OD1 ASP A 215 4609 3298 4382 -150 -779 -1011 A O ATOM 1610 OD2 ASP A 215 27.885 114.881 256.629 1.00 26.57 A O1- ANISOU 1610 OD2 ASP A 215 3855 2729 3513 119 -815 -900 A O1- ATOM 1611 N LYS A 216 26.313 112.024 260.857 1.00 29.98 A N ANISOU 1611 N LYS A 216 4624 2536 4231 -139 -486 -690 A N ATOM 1612 CA ALYS A 216 26.528 111.039 261.916 0.39 33.85 A C ANISOU 1612 CA ALYS A 216 5266 2837 4758 -109 -372 -586 A C ATOM 1613 CA BLYS A 216 26.519 111.066 261.938 0.61 32.84 A C ANISOU 1613 CA BLYS A 216 5134 2712 4630 -110 -373 -584 A C ATOM 1614 C LYS A 216 27.952 111.048 262.460 1.00 31.95 A C ANISOU 1614 C LYS A 216 5072 2635 4431 113 -354 -440 A C ATOM 1615 O LYS A 216 28.162 111.068 263.665 1.00 29.78 A O ANISOU 1615 O LYS A 216 4814 2360 4141 153 -305 -300 A O ATOM 1616 CB ALYS A 216 26.209 109.631 261.407 0.39 39.48 A C ANISOU 1616 CB ALYS A 216 6157 3302 5543 -174 -295 -688 A C ATOM 1617 CB BLYS A 216 26.121 109.657 261.499 0.61 39.79 A C ANISOU 1617 CB BLYS A 216 6190 3342 5588 -187 -292 -683 A C ATOM 1618 CG ALYS A 216 24.787 109.442 260.906 0.39 45.31 A C ANISOU 1618 CG ALYS A 216 6850 4000 6364 -419 -306 -844 A C ATOM 1619 CG BLYS A 216 24.678 109.535 261.045 0.61 47.66 A C ANISOU 1619 CG BLYS A 216 7131 4310 6666 -434 -306 -832 A C ATOM 1620 CD ALYS A 216 23.769 109.725 261.999 0.39 47.92 A C ANISOU 1620 CD ALYS A 216 7105 4343 6759 -569 -266 -776 A C ATOM 1621 CD BLYS A 216 23.704 109.630 262.213 0.61 49.06 A C ANISOU 1621 CD BLYS A 216 7264 4463 6915 -580 -246 -757 A C ATOM 1622 CE ALYS A 216 22.350 109.481 261.503 0.39 47.37 A C ANISOU 1622 CE ALYS A 216 6971 4256 6770 -819 -274 -929 A C ATOM 1623 CE BLYS A 216 22.261 109.582 261.720 0.61 47.31 A C ANISOU 1623 CE BLYS A 216 6947 4260 6767 -827 -268 -906 A C ATOM 1624 NZ ALYS A 216 21.345 109.856 262.533 0.39 44.56 A N1+ ANISOU 1624 NZ ALYS A 216 6514 3946 6471 -955 -235 -860 A N1+ ATOM 1625 NZ BLYS A 216 22.181 109.071 260.318 0.61 44.50 A N1+ ANISOU 1625 NZ BLYS A 216 6630 3872 6407 -881 -317 -1095 A N1+ ATOM 1626 N ASP A 217 28.933 111.004 261.562 1.00 33.22 A N ANISOU 1626 N ASP A 217 5249 2846 4528 259 -391 -473 A N ATOM 1627 CA ASP A 217 30.338 110.888 261.980 1.00 26.03 A C ANISOU 1627 CA ASP A 217 4372 1986 3530 481 -371 -339 A C ATOM 1628 C ASP A 217 30.860 112.111 262.770 1.00 24.42 A C ANISOU 1628 C ASP A 217 4014 2018 3246 523 -428 -224 A C ATOM 1629 O ASP A 217 31.611 111.959 263.731 1.00 30.25 A O ANISOU 1629 O ASP A 217 4774 2791 3927 640 -393 -82 A O ATOM 1630 CB ASP A 217 31.243 110.470 260.802 1.00 30.02 A C ANISOU 1630 CB ASP A 217 4933 2487 3988 630 -383 -405 A C ATOM 1631 CG ASP A 217 31.106 111.385 259.581 1.00 35.10 A C ANISOU 1631 CG ASP A 217 5444 3297 4596 578 -488 -531 A C ATOM 1632 OD1 ASP A 217 30.213 112.264 259.561 1.00 32.90 A O ANISOU 1632 OD1 ASP A 217 5044 3115 4343 425 -549 -576 A O ATOM 1633 OD2 ASP A 217 31.865 111.179 258.608 1.00 35.40 A O1- ANISOU 1633 OD2 ASP A 217 5507 3363 4578 699 -501 -583 A O1- ATOM 1634 N ILE A 218 30.453 113.311 262.368 1.00 23.80 A N ANISOU 1634 N ILE A 218 3786 2101 3156 427 -512 -287 A N ATOM 1635 CA ILE A 218 30.770 114.544 263.099 1.00 25.11 A C ANISOU 1635 CA ILE A 218 3820 2463 3258 424 -555 -206 A C ATOM 1636 C ILE A 218 30.194 114.551 264.537 1.00 23.92 A C ANISOU 1636 C ILE A 218 3682 2276 3129 347 -501 -116 A C ATOM 1637 O ILE A 218 30.893 114.756 265.586 1.00 27.61 A O ANISOU 1637 O ILE A 218 4136 2834 3521 420 -486 5 A O ATOM 1638 CB ILE A 218 30.165 115.743 262.324 1.00 23.83 A C ANISOU 1638 CB ILE A 218 3525 2424 3104 320 -630 -302 A C ATOM 1639 CG1 ILE A 218 30.703 115.790 260.886 1.00 23.11 A C ANISOU 1639 CG1 ILE A 218 3418 2386 2977 394 -682 -385 A C ATOM 1640 CG2 ILE A 218 30.397 117.048 263.057 1.00 20.22 A C ANISOU 1640 CG2 ILE A 218 2955 2135 2593 297 -657 -236 A C ATOM 1641 CD1 ILE A 218 32.176 116.156 260.787 1.00 26.23 A C ANISOU 1641 CD1 ILE A 218 3772 2925 3270 547 -702 -314 A C ATOM 1642 N VAL A 219 28.884 114.321 264.558 1.00 26.61 A N ANISOU 1642 N VAL A 219 4041 2501 3567 193 -471 -181 A N ATOM 1643 CA VAL A 219 28.087 114.348 265.771 1.00 27.93 A C ANISOU 1643 CA VAL A 219 4214 2630 3769 92 -413 -118 A C ATOM 1644 C VAL A 219 28.486 113.212 266.696 1.00 29.73 A C ANISOU 1644 C VAL A 219 4585 2722 3988 172 -320 2 A C ATOM 1645 O VAL A 219 28.237 113.276 267.873 1.00 33.43 A O ANISOU 1645 O VAL A 219 5061 3199 4441 143 -270 97 A O ATOM 1646 CB VAL A 219 26.566 114.312 265.438 1.00 31.02 A C ANISOU 1646 CB VAL A 219 4573 2945 4269 -95 -401 -223 A C ATOM 1647 CG1 VAL A 219 25.715 114.204 266.689 1.00 29.59 A C ANISOU 1647 CG1 VAL A 219 4403 2711 4128 -198 -322 -154 A C ATOM 1648 CG2 VAL A 219 26.178 115.559 264.679 1.00 31.22 A C ANISOU 1648 CG2 VAL A 219 4447 3131 4286 -144 -488 -307 A C ATOM 1649 N LYS A 220 29.082 112.158 266.155 1.00 25.69 A N ANISOU 1649 N LYS A 220 4197 2080 3485 282 -287 1 A N ATOM 1650 CA LYS A 220 29.556 111.047 266.975 1.00 26.35 A C ANISOU 1650 CA LYS A 220 4433 2025 3555 396 -188 134 A C ATOM 1651 C LYS A 220 30.736 111.495 267.841 1.00 35.19 A C ANISOU 1651 C LYS A 220 5497 3335 4539 561 -212 284 A C ATOM 1652 O LYS A 220 30.789 111.199 269.034 1.00 26.77 A O ANISOU 1652 O LYS A 220 4478 2259 3434 597 -151 419 A O ATOM 1653 CB LYS A 220 29.916 109.827 266.111 1.00 27.88 A C ANISOU 1653 CB LYS A 220 4786 2017 3791 487 -134 88 A C ATOM 1654 CG LYS A 220 30.288 108.584 266.917 1.00 31.86 A C ANISOU 1654 CG LYS A 220 5477 2330 4297 612 -6 232 A C ATOM 1655 CD LYS A 220 30.678 107.419 266.014 1.00 38.23 A C ANISOU 1655 CD LYS A 220 6459 2920 5146 715 60 176 A C ATOM 1656 CE LYS A 220 31.014 106.166 266.827 1.00 43.84 A C ANISOU 1656 CE LYS A 220 7379 3413 5866 855 209 334 A C ATOM 1657 NZ LYS A 220 31.467 105.039 265.960 1.00 47.99 A N1+ ANISOU 1657 NZ LYS A 220 8095 3710 6430 979 291 281 A N1+ ATOM 1658 N VAL A 221 31.689 112.194 267.228 1.00 33.90 A N ANISOU 1658 N VAL A 221 5227 3356 4295 656 -300 259 A N ATOM 1659 CA VAL A 221 32.808 112.764 267.969 1.00 31.88 A C ANISOU 1659 CA VAL A 221 4882 3327 3903 780 -339 377 A C ATOM 1660 C VAL A 221 32.250 113.709 269.020 1.00 28.74 A C ANISOU 1660 C VAL A 221 4397 3048 3475 647 -354 403 A C ATOM 1661 O VAL A 221 32.577 113.612 270.245 1.00 27.65 A O ANISOU 1661 O VAL A 221 4269 2983 3252 701 -323 534 A O ATOM 1662 CB VAL A 221 33.777 113.509 267.029 1.00 32.67 A C ANISOU 1662 CB VAL A 221 4862 3614 3936 853 -430 321 A C ATOM 1663 CG1 VAL A 221 34.888 114.190 267.823 1.00 32.87 A C ANISOU 1663 CG1 VAL A 221 4771 3901 3816 940 -475 427 A C ATOM 1664 CG2 VAL A 221 34.359 112.542 266.007 1.00 24.86 A C ANISOU 1664 CG2 VAL A 221 3966 2515 2966 1001 -404 295 A C ATOM 1665 N PHE A 222 31.367 114.599 268.560 1.00 27.95 A N ANISOU 1665 N PHE A 222 4217 2965 3438 482 -394 282 A N ATOM 1666 CA PHE A 222 30.810 115.541 269.535 1.00 26.13 A C ANISOU 1666 CA PHE A 222 3912 2836 3180 364 -395 297 A C ATOM 1667 C PHE A 222 30.112 114.851 270.726 1.00 25.37 A C ANISOU 1667 C PHE A 222 3907 2627 3103 323 -300 389 A C ATOM 1668 O PHE A 222 30.336 115.204 271.877 1.00 30.31 A O ANISOU 1668 O PHE A 222 4511 3370 3637 332 -286 477 A O ATOM 1669 CB PHE A 222 29.868 116.557 268.886 1.00 27.38 A C ANISOU 1669 CB PHE A 222 3979 3014 3409 213 -434 167 A C ATOM 1670 CG PHE A 222 29.142 117.408 269.886 1.00 27.07 A C ANISOU 1670 CG PHE A 222 3888 3039 3358 99 -409 178 A C ATOM 1671 CD1 PHE A 222 27.786 117.230 270.119 1.00 26.42 A C ANISOU 1671 CD1 PHE A 222 3823 2843 3374 -25 -352 146 A C ATOM 1672 CD2 PHE A 222 29.825 118.367 270.617 1.00 30.06 A C ANISOU 1672 CD2 PHE A 222 4200 3601 3623 112 -436 214 A C ATOM 1673 CE1 PHE A 222 27.123 118.005 271.055 1.00 34.13 A C ANISOU 1673 CE1 PHE A 222 4753 3882 4334 -114 -317 158 A C ATOM 1674 CE2 PHE A 222 29.170 119.145 271.556 1.00 29.94 A C ANISOU 1674 CE2 PHE A 222 4151 3635 3588 11 -402 213 A C ATOM 1675 CZ PHE A 222 27.817 118.964 271.775 1.00 34.07 A C ANISOU 1675 CZ PHE A 222 4695 4039 4209 -91 -339 189 A C ATOM 1676 N THR A 223 29.300 113.848 270.434 1.00 31.94 A N ANISOU 1676 N THR A 223 4847 3237 4050 273 -231 366 A N ATOM 1677 CA THR A 223 28.498 113.127 271.417 1.00 31.58 A C ANISOU 1677 CA THR A 223 4898 3053 4047 209 -124 445 A C ATOM 1678 C THR A 223 29.390 112.375 272.382 1.00 32.48 A C ANISOU 1678 C THR A 223 5109 3170 4061 375 -69 621 A C ATOM 1679 O THR A 223 29.125 112.341 273.582 1.00 35.57 A O ANISOU 1679 O THR A 223 5524 3589 4403 357 -10 725 A O ATOM 1680 CB THR A 223 27.519 112.132 270.730 1.00 33.10 A C ANISOU 1680 CB THR A 223 5192 2995 4390 105 -58 367 A C ATOM 1681 CG2 THR A 223 26.767 111.307 271.754 1.00 34.76 A C ANISOU 1681 CG2 THR A 223 5513 3048 4645 36 71 462 A C ATOM 1682 OG1 THR A 223 26.565 112.861 269.945 1.00 36.55 A O ANISOU 1682 OG1 THR A 223 5516 3465 4905 -53 -111 215 A O ATOM 1683 N LYS A 224 30.443 111.763 271.848 1.00 29.26 A N ANISOU 1683 N LYS A 224 4755 2745 3617 550 -83 659 A N ATOM 1684 CA LYS A 224 31.419 111.073 272.675 1.00 36.38 A C ANISOU 1684 CA LYS A 224 5732 3683 4409 749 -39 839 A C ATOM 1685 C LYS A 224 31.989 112.058 273.665 1.00 40.63 A C ANISOU 1685 C LYS A 224 6139 4509 4790 772 -102 909 A C ATOM 1686 O LYS A 224 32.129 111.749 274.853 1.00 41.72 A O ANISOU 1686 O LYS A 224 6320 4694 4837 835 -49 1056 A O ATOM 1687 CB LYS A 224 32.539 110.493 271.810 1.00 41.81 A C ANISOU 1687 CB LYS A 224 6457 4357 5071 947 -59 852 A C ATOM 1688 CG LYS A 224 33.612 109.724 272.576 1.00 55.35 A C ANISOU 1688 CG LYS A 224 8241 6122 6667 1193 -12 1052 A C ATOM 1689 CD LYS A 224 33.032 108.750 273.589 1.00 70.00 A C ANISOU 1689 CD LYS A 224 10263 7785 8547 1206 124 1193 A C ATOM 1690 CE LYS A 224 34.096 107.792 274.134 1.00 75.94 A C ANISOU 1690 CE LYS A 224 11116 8543 9196 1491 189 1402 A C ATOM 1691 NZ LYS A 224 35.094 108.435 275.045 1.00 77.81 A N1+ ANISOU 1691 NZ LYS A 224 11204 9132 9230 1620 108 1529 A N1+ ATOM 1692 N ARG A 225 32.281 113.266 273.196 1.00 42.30 A N ANISOU 1692 N ARG A 225 6196 4911 4964 710 -208 802 A N ATOM 1693 CA ARG A 225 32.782 114.252 274.147 1.00 43.60 A C ANISOU 1693 CA ARG A 225 6244 5342 4980 699 -262 843 A C ATOM 1694 C ARG A 225 31.738 114.704 275.184 1.00 41.98 A C ANISOU 1694 C ARG A 225 6042 5132 4776 545 -213 845 A C ATOM 1695 O ARG A 225 32.044 114.845 276.365 1.00 40.97 A O ANISOU 1695 O ARG A 225 5903 5149 4515 577 -201 946 A O ATOM 1696 CB ARG A 225 33.389 115.448 273.411 1.00 49.17 A C ANISOU 1696 CB ARG A 225 6799 6236 5647 659 -371 729 A C ATOM 1697 CG ARG A 225 34.033 116.469 274.336 1.00 62.42 A C ANISOU 1697 CG ARG A 225 8361 8193 7164 632 -426 752 A C ATOM 1698 CD ARG A 225 34.980 115.807 275.352 1.00 73.86 A C ANISOU 1698 CD ARG A 225 9822 9787 8454 801 -417 925 A C ATOM 1699 NE ARG A 225 36.360 115.707 274.882 1.00 79.85 A N ANISOU 1699 NE ARG A 225 10499 10721 9121 958 -484 965 A N ATOM 1700 CZ ARG A 225 37.128 114.629 275.016 1.00 86.42 A C ANISOU 1700 CZ ARG A 225 11380 11562 9895 1178 -458 1111 A C ATOM 1701 NH1 ARG A 225 36.658 113.527 275.587 1.00 88.22 A N1+ ANISOU 1701 NH1 ARG A 225 11760 11608 10152 1264 -360 1233 A N1+ ATOM 1702 NH2 ARG A 225 38.374 114.652 274.566 1.00 88.21 A N ANISOU 1702 NH2 ARG A 225 11505 11979 10034 1318 -520 1140 A N ATOM 1703 N ILE A 226 30.507 114.916 274.737 1.00 43.15 A N ANISOU 1703 N ILE A 226 6200 5130 5066 384 -182 735 A N ATOM 1704 CA ILE A 226 29.472 115.541 275.558 1.00 43.73 A C ANISOU 1704 CA ILE A 226 6248 5219 5148 233 -138 712 A C ATOM 1705 C ILE A 226 28.745 114.602 276.533 1.00 43.47 A C ANISOU 1705 C ILE A 226 6333 5049 5136 217 -17 827 A C ATOM 1706 O ILE A 226 28.121 115.057 277.492 1.00 42.17 A O ANISOU 1706 O ILE A 226 6150 4942 4931 130 29 846 A O ATOM 1707 CB ILE A 226 28.438 116.271 274.647 1.00 43.85 A C ANISOU 1707 CB ILE A 226 6196 5167 5299 78 -159 550 A C ATOM 1708 CG1 ILE A 226 27.923 117.547 275.301 1.00 48.78 A C ANISOU 1708 CG1 ILE A 226 6733 5921 5879 -34 -160 497 A C ATOM 1709 CG2 ILE A 226 27.262 115.380 274.304 1.00 43.11 A C ANISOU 1709 CG2 ILE A 226 6178 4843 5358 -8 -80 527 A C ATOM 1710 CD1 ILE A 226 28.988 118.541 275.616 1.00 53.59 A C ANISOU 1710 CD1 ILE A 226 7266 6753 6343 5 -233 489 A C ATOM 1711 N ASER A 227 28.825 113.298 276.281 0.52 43.14 A N ANISOU 1711 N ASER A 227 6420 4815 5155 301 47 903 A N ATOM 1712 N BSER A 227 28.832 113.298 276.280 0.48 43.13 A N ANISOU 1712 N BSER A 227 6418 4815 5153 302 46 904 A N ATOM 1713 CA ASER A 227 28.166 112.308 277.129 0.52 43.83 A C ANISOU 1713 CA ASER A 227 6641 4740 5273 286 180 1024 A C ATOM 1714 CA BSER A 227 28.170 112.308 277.123 0.48 43.78 A C ANISOU 1714 CA BSER A 227 6634 4733 5267 286 179 1024 A C ATOM 1715 C ASER A 227 28.874 112.139 278.470 0.52 44.84 A C ANISOU 1715 C ASER A 227 6802 5014 5222 418 209 1206 A C ATOM 1716 C BSER A 227 28.866 112.154 278.469 0.48 44.89 A C ANISOU 1716 C BSER A 227 6806 5022 5228 416 208 1204 A C ATOM 1717 O ASER A 227 28.351 111.502 279.383 0.52 44.61 A O ANISOU 1717 O ASER A 227 6872 4894 5184 407 323 1326 A O ATOM 1718 O BSER A 227 28.323 111.545 279.387 0.48 44.74 A O ANISOU 1718 O BSER A 227 6883 4914 5200 401 321 1321 A O ATOM 1719 CB ASER A 227 28.027 110.963 276.409 0.52 42.56 A C ANISOU 1719 CB ASER A 227 6630 4300 5240 325 255 1041 A C ATOM 1720 CB BSER A 227 28.092 110.952 276.414 0.48 42.64 A C ANISOU 1720 CB BSER A 227 6641 4315 5244 335 253 1046 A C ATOM 1721 OG ASER A 227 29.294 110.406 276.105 0.52 40.90 A O ANISOU 1721 OG ASER A 227 6474 4108 4959 540 226 1120 A O ATOM 1722 OG BSER A 227 26.990 110.896 275.527 0.48 40.31 A O ANISOU 1722 OG BSER A 227 6340 3858 5119 155 269 894 A O ATOM 1723 N LYS A 228 30.071 112.704 278.581 1.00 49.88 A N ANISOU 1723 N LYS A 228 7350 5892 5709 540 108 1229 A N ATOM 1724 CA LYS A 228 30.819 112.635 279.826 1.00 59.80 A C ANISOU 1724 CA LYS A 228 8608 7346 6767 668 113 1391 A C ATOM 1725 C LYS A 228 30.298 113.688 280.788 1.00 58.37 A C ANISOU 1725 C LYS A 228 8346 7335 6496 528 107 1349 A C ATOM 1726 O LYS A 228 30.356 113.512 282.006 1.00 62.82 A O ANISOU 1726 O LYS A 228 8945 8002 6922 573 156 1480 A O ATOM 1727 CB LYS A 228 32.314 112.845 279.565 1.00 66.47 A C ANISOU 1727 CB LYS A 228 9365 8416 7477 839 2 1423 A C ATOM 1728 CG LYS A 228 32.907 111.774 278.666 1.00 69.68 A C ANISOU 1728 CG LYS A 228 9858 8663 7955 1010 20 1475 A C ATOM 1729 CD LYS A 228 34.350 112.045 278.259 1.00 74.90 A C ANISOU 1729 CD LYS A 228 10404 9558 8495 1172 -90 1490 A C ATOM 1730 CE LYS A 228 34.879 110.846 277.468 1.00 84.78 A C ANISOU 1730 CE LYS A 228 11769 10629 9816 1370 -42 1561 A C ATOM 1731 NZ LYS A 228 36.263 111.005 276.930 1.00 89.55 A N1+ ANISOU 1731 NZ LYS A 228 12258 11447 10320 1544 -135 1577 A N1+ ATOM 1732 N LYS A 229 29.795 114.787 280.237 1.00 49.60 A N ANISOU 1732 N LYS A 229 7134 6257 5456 369 52 1169 A N ATOM 1733 CA LYS A 229 29.280 115.867 281.072 1.00 46.21 A C ANISOU 1733 CA LYS A 229 6636 5971 4949 239 57 1108 A C ATOM 1734 C LYS A 229 27.749 116.014 281.125 1.00 37.47 A C ANISOU 1734 C LYS A 229 5551 4700 3984 72 151 1040 A C ATOM 1735 O LYS A 229 27.210 116.453 282.140 1.00 38.69 A O ANISOU 1735 O LYS A 229 5702 4934 4066 2 209 1055 A O ATOM 1736 CB LYS A 229 30.031 117.195 280.855 1.00 46.00 A C ANISOU 1736 CB LYS A 229 6476 6175 4828 203 -61 986 A C ATOM 1737 CG LYS A 229 29.979 117.836 279.485 1.00 48.76 A C ANISOU 1737 CG LYS A 229 6755 6464 5309 139 -129 829 A C ATOM 1738 CD LYS A 229 30.717 119.183 279.559 1.00 54.61 A C ANISOU 1738 CD LYS A 229 7381 7435 5931 88 -217 729 A C ATOM 1739 CE LYS A 229 30.857 119.866 278.208 1.00 60.49 A C ANISOU 1739 CE LYS A 229 8057 8144 6782 44 -285 594 A C ATOM 1740 NZ LYS A 229 31.700 121.098 278.292 1.00 63.85 A N1+ ANISOU 1740 NZ LYS A 229 8387 8784 7090 -9 -358 510 A N1+ ATOM 1741 N PHE A 230 27.050 115.649 280.051 1.00 30.92 A N ANISOU 1741 N PHE A 230 4736 3664 3346 9 168 963 A N ATOM 1742 CA PHE A 230 25.588 115.739 280.060 1.00 33.08 A C ANISOU 1742 CA PHE A 230 5006 3809 3754 -149 254 901 A C ATOM 1743 C PHE A 230 24.985 114.337 280.148 1.00 38.27 A C ANISOU 1743 C PHE A 230 5791 4238 4514 -157 369 1002 A C ATOM 1744 O PHE A 230 25.577 113.369 279.667 1.00 41.63 A O ANISOU 1744 O PHE A 230 6304 4544 4968 -56 368 1062 A O ATOM 1745 CB PHE A 230 25.036 116.421 278.794 1.00 30.83 A C ANISOU 1745 CB PHE A 230 4626 3476 3611 -245 193 728 A C ATOM 1746 CG PHE A 230 25.583 117.806 278.528 1.00 30.37 A C ANISOU 1746 CG PHE A 230 4460 3600 3480 -246 94 623 A C ATOM 1747 CD1 PHE A 230 26.320 118.491 279.482 1.00 28.04 A C ANISOU 1747 CD1 PHE A 230 4145 3500 3009 -210 71 655 A C ATOM 1748 CD2 PHE A 230 25.324 118.434 277.313 1.00 32.39 A C ANISOU 1748 CD2 PHE A 230 4637 3829 3841 -294 30 490 A C ATOM 1749 CE1 PHE A 230 26.817 119.767 279.218 1.00 27.91 A C ANISOU 1749 CE1 PHE A 230 4043 3629 2934 -235 -7 547 A C ATOM 1750 CE2 PHE A 230 25.815 119.708 277.047 1.00 29.52 A C ANISOU 1750 CE2 PHE A 230 4191 3606 3418 -299 -43 401 A C ATOM 1751 CZ PHE A 230 26.559 120.373 278.003 1.00 27.77 A C ANISOU 1751 CZ PHE A 230 3961 3557 3034 -279 -56 426 A C ATOM 1752 N ASN A 231 23.805 114.235 280.757 1.00 38.56 A N ANISOU 1752 N ASN A 231 5839 4207 4605 -281 481 1018 A N ATOM 1753 CA ASN A 231 22.998 113.015 280.690 1.00 40.13 A C ANISOU 1753 CA ASN A 231 6143 4167 4936 -349 602 1077 A C ATOM 1754 C ASN A 231 22.044 113.083 279.502 1.00 37.48 A C ANISOU 1754 C ASN A 231 5737 3713 4791 -499 585 917 A C ATOM 1755 O ASN A 231 20.969 113.683 279.597 1.00 38.18 A O ANISOU 1755 O ASN A 231 5727 3841 4938 -635 617 842 A O ATOM 1756 CB ASN A 231 22.227 112.797 282.001 1.00 43.55 A C ANISOU 1756 CB ASN A 231 6622 4602 5324 -412 743 1191 A C ATOM 1757 CG ASN A 231 21.301 111.580 281.956 1.00 47.02 A C ANISOU 1757 CG ASN A 231 7166 4788 5911 -519 886 1248 A C ATOM 1758 ND2 ASN A 231 20.264 111.598 282.784 1.00 43.32 A N ANISOU 1758 ND2 ASN A 231 6685 4319 5456 -639 1008 1289 A N ATOM 1759 OD1 ASN A 231 21.528 110.634 281.204 1.00 53.53 A O ANISOU 1759 OD1 ASN A 231 8087 5420 6834 -498 896 1251 A O ATOM 1760 N LEU A 232 22.435 112.469 278.388 1.00 33.19 A N ANISOU 1760 N LEU A 232 5239 3040 4333 -466 536 865 A N ATOM 1761 CA LEU A 232 21.665 112.582 277.153 1.00 36.20 A C ANISOU 1761 CA LEU A 232 5541 3347 4867 -595 494 700 A C ATOM 1762 C LEU A 232 20.556 111.550 277.087 1.00 35.76 A C ANISOU 1762 C LEU A 232 5551 3082 4955 -754 616 698 A C ATOM 1763 O LEU A 232 20.802 110.349 277.204 1.00 34.16 A O ANISOU 1763 O LEU A 232 5512 2686 4782 -725 700 785 A O ATOM 1764 CB LEU A 232 22.556 112.406 275.921 1.00 39.04 A C ANISOU 1764 CB LEU A 232 5917 3671 5244 -500 387 626 A C ATOM 1765 CG LEU A 232 23.655 113.416 275.630 1.00 40.33 A C ANISOU 1765 CG LEU A 232 5998 4032 5294 -370 255 594 A C ATOM 1766 CD1 LEU A 232 24.466 112.967 274.420 1.00 39.62 A C ANISOU 1766 CD1 LEU A 232 5947 3874 5233 -277 180 538 A C ATOM 1767 CD2 LEU A 232 23.042 114.780 275.388 1.00 40.69 A C ANISOU 1767 CD2 LEU A 232 5881 4231 5350 -461 195 477 A C ATOM 1768 N MET A 233 19.330 112.031 276.918 1.00 33.76 A N ANISOU 1768 N MET A 233 5167 2871 4788 -923 633 601 A N ATOM 1769 CA MET A 233 18.185 111.146 276.778 1.00 35.87 A C ANISOU 1769 CA MET A 233 5460 2973 5197 -1112 741 574 A C ATOM 1770 C MET A 233 17.568 111.325 275.394 1.00 33.83 A C ANISOU 1770 C MET A 233 5082 2717 5054 -1230 654 388 A C ATOM 1771 O MET A 233 16.711 112.183 275.182 1.00 33.06 A O ANISOU 1771 O MET A 233 4806 2767 4987 -1318 619 301 A O ATOM 1772 CB MET A 233 17.174 111.391 277.897 1.00 36.02 A C ANISOU 1772 CB MET A 233 5420 3055 5212 -1219 859 642 A C ATOM 1773 CG MET A 233 17.686 110.941 279.263 1.00 40.16 A C ANISOU 1773 CG MET A 233 6088 3548 5622 -1121 967 838 A C ATOM 1774 SD MET A 233 16.584 111.357 280.624 1.00 51.22 A S ANISOU 1774 SD MET A 233 7417 5057 6987 -1226 1107 918 A S ATOM 1775 CE MET A 233 17.023 113.073 280.882 1.00 33.32 A C ANISOU 1775 CE MET A 233 5004 3080 4577 -1107 985 858 A C ATOM 1776 N LEU A 234 18.045 110.521 274.451 1.00 34.07 A N ANISOU 1776 N LEU A 234 5213 2596 5137 -1215 621 329 A N ATOM 1777 CA LEU A 234 17.575 110.576 273.073 1.00 34.34 A C ANISOU 1777 CA LEU A 234 5153 2636 5261 -1319 532 148 A C ATOM 1778 C LEU A 234 16.334 109.715 272.851 1.00 36.24 A C ANISOU 1778 C LEU A 234 5388 2743 5638 -1564 625 76 A C ATOM 1779 O LEU A 234 16.043 108.815 273.643 1.00 42.69 A O ANISOU 1779 O LEU A 234 6333 3394 6495 -1642 772 172 A O ATOM 1780 CB LEU A 234 18.695 110.193 272.098 1.00 34.60 A C ANISOU 1780 CB LEU A 234 5288 2588 5269 -1186 448 100 A C ATOM 1781 CG LEU A 234 19.897 111.150 272.125 1.00 38.59 A C ANISOU 1781 CG LEU A 234 5757 3262 5643 -969 338 145 A C ATOM 1782 CD1 LEU A 234 21.063 110.630 271.294 1.00 36.06 A C ANISOU 1782 CD1 LEU A 234 5549 2856 5294 -825 281 124 A C ATOM 1783 CD2 LEU A 234 19.472 112.522 271.634 1.00 28.37 A C ANISOU 1783 CD2 LEU A 234 4255 2192 4333 -993 229 47 A C ATOM 1784 N GLU A 235 15.605 110.024 271.780 1.00 35.83 A N ANISOU 1784 N GLU A 235 5182 2781 5650 -1689 540 -91 A N ATOM 1785 CA GLU A 235 14.359 109.349 271.428 1.00 37.94 A C ANISOU 1785 CA GLU A 235 5395 2982 6041 -1949 602 -193 A C ATOM 1786 C GLU A 235 13.417 109.292 272.623 1.00 41.99 A C ANISOU 1786 C GLU A 235 5852 3526 6577 -2053 731 -88 A C ATOM 1787 O GLU A 235 12.761 108.279 272.868 1.00 43.75 A O ANISOU 1787 O GLU A 235 6123 3644 6857 -2169 811 -71 A O ATOM 1788 CB GLU A 235 14.670 107.939 270.924 1.00 38.42 A C ANISOU 1788 CB GLU A 235 5644 2811 6145 -1970 632 -226 A C ATOM 1789 CG GLU A 235 15.510 107.940 269.655 1.00 42.19 A C ANISOU 1789 CG GLU A 235 6169 3262 6599 -1878 513 -347 A C ATOM 1790 CD GLU A 235 15.818 106.550 269.140 1.00 51.14 A C ANISOU 1790 CD GLU A 235 7490 4170 7770 -1884 550 -387 A C ATOM 1791 OE1 GLU A 235 16.774 105.934 269.654 1.00 58.65 A O ANISOU 1791 OE1 GLU A 235 8653 4936 8696 -1743 633 -269 A O ATOM 1792 OE2 GLU A 235 15.127 106.087 268.209 1.00 51.28 A O1- ANISOU 1792 OE2 GLU A 235 7445 4206 7834 -2017 497 -534 A O1- ATOM 1793 N THR A 236 13.364 110.396 273.362 1.00 38.28 A N ANISOU 1793 N THR A 236 5272 3235 6038 -1968 728 -13 A N ATOM 1794 CA THR A 236 12.566 110.503 274.578 1.00 43.23 A C ANISOU 1794 CA THR A 236 5849 3908 6670 -2047 862 92 A C ATOM 1795 C THR A 236 11.781 111.812 274.515 1.00 42.05 A C ANISOU 1795 C THR A 236 5445 4032 6502 -2047 801 38 A C ATOM 1796 O THR A 236 12.288 112.790 273.966 1.00 35.76 A O ANISOU 1796 O THR A 236 4573 3371 5642 -1900 670 -10 A O ATOM 1797 CB THR A 236 13.490 110.515 275.814 1.00 43.58 A C ANISOU 1797 CB THR A 236 6055 3904 6601 -1870 932 277 A C ATOM 1798 CG2 THR A 236 12.691 110.697 277.095 1.00 42.24 A C ANISOU 1798 CG2 THR A 236 5834 3800 6414 -1938 1072 387 A C ATOM 1799 OG1 THR A 236 14.224 109.283 275.879 1.00 46.11 A O ANISOU 1799 OG1 THR A 236 6615 3970 6935 -1840 999 347 A O ATOM 1800 N LYS A 237 10.556 111.847 275.044 1.00 41.28 A N ANISOU 1800 N LYS A 237 5213 4013 6460 -2203 902 50 A N ATOM 1801 CA LYS A 237 9.798 113.102 275.023 1.00 47.32 A C ANISOU 1801 CA LYS A 237 5737 5038 7205 -2173 860 11 A C ATOM 1802 C LYS A 237 9.176 113.428 276.377 1.00 48.49 A C ANISOU 1802 C LYS A 237 5841 5260 7322 -2187 1006 128 A C ATOM 1803 O LYS A 237 8.871 112.531 277.165 1.00 48.85 A O ANISOU 1803 O LYS A 237 5982 5185 7394 -2291 1141 216 A O ATOM 1804 CB LYS A 237 8.681 113.103 273.973 1.00 50.42 A C ANISOU 1804 CB LYS A 237 5913 5563 7680 -2316 788 -127 A C ATOM 1805 CG LYS A 237 7.442 112.295 274.328 1.00 55.02 A C ANISOU 1805 CG LYS A 237 6424 6154 8325 -2482 870 -107 A C ATOM 1806 CD LYS A 237 6.534 112.139 273.116 1.00 62.48 A C ANISOU 1806 CD LYS A 237 7187 7228 9324 -2588 757 -244 A C ATOM 1807 CE LYS A 237 5.123 111.760 273.526 1.00 69.76 A C ANISOU 1807 CE LYS A 237 7958 8246 10302 -2744 837 -224 A C ATOM 1808 NZ LYS A 237 4.453 112.938 274.160 1.00 69.54 A N1+ ANISOU 1808 NZ LYS A 237 7730 8446 10247 -2680 888 -170 A N1+ ATOM 1809 N VAL A 238 8.966 114.719 276.622 1.00 42.47 A N ANISOU 1809 N VAL A 238 4941 4699 6495 -2064 977 130 A N ATOM 1810 CA VAL A 238 8.290 115.179 277.829 1.00 43.78 A C ANISOU 1810 CA VAL A 238 5042 4967 6624 -2065 1114 220 A C ATOM 1811 C VAL A 238 6.778 115.149 277.608 1.00 45.84 A C ANISOU 1811 C VAL A 238 5066 5364 6987 -2241 1174 165 A C ATOM 1812 O VAL A 238 6.279 115.676 276.610 1.00 47.63 A O ANISOU 1812 O VAL A 238 5106 5736 7255 -2245 1071 58 A O ATOM 1813 CB VAL A 238 8.722 116.613 278.202 1.00 40.68 A C ANISOU 1813 CB VAL A 238 4619 4721 6117 -1855 1072 234 A C ATOM 1814 CG1 VAL A 238 7.885 117.144 279.347 1.00 39.18 A C ANISOU 1814 CG1 VAL A 238 4344 4652 5892 -1859 1219 302 A C ATOM 1815 CG2 VAL A 238 10.199 116.654 278.554 1.00 37.73 A C ANISOU 1815 CG2 VAL A 238 4459 4247 5630 -1701 1021 292 A C ATOM 1816 N THR A 239 6.063 114.512 278.534 1.00 44.51 A N ANISOU 1816 N THR A 239 4906 5168 6838 -2351 1318 252 A N ATOM 1817 CA THR A 239 4.610 114.385 278.463 1.00 46.90 A C ANISOU 1817 CA THR A 239 4993 5619 7207 -2471 1348 229 A C ATOM 1818 C THR A 239 3.894 115.255 279.492 1.00 52.49 A C ANISOU 1818 C THR A 239 5573 6502 7867 -2418 1476 300 A C ATOM 1819 O THR A 239 2.709 115.567 279.334 1.00 56.34 A O ANISOU 1819 O THR A 239 5832 7176 8398 -2465 1488 273 A O ATOM 1820 CB THR A 239 4.169 112.930 278.688 1.00 46.75 A C ANISOU 1820 CB THR A 239 5064 5450 7250 -2637 1407 271 A C ATOM 1821 CG2 THR A 239 4.719 112.033 277.594 1.00 47.38 A C ANISOU 1821 CG2 THR A 239 5257 5362 7382 -2695 1291 182 A C ATOM 1822 OG1 THR A 239 4.656 112.480 279.958 1.00 47.64 A O ANISOU 1822 OG1 THR A 239 5376 5424 7302 -2606 1544 417 A O ATOM 1823 N ALA A 240 4.598 115.605 280.566 1.00 52.03 A N ANISOU 1823 N ALA A 240 5668 6391 7712 -2314 1575 396 A N ATOM 1824 CA ALA A 240 4.027 116.463 281.600 1.00 51.41 A C ANISOU 1824 CA ALA A 240 5499 6468 7566 -2243 1706 458 A C ATOM 1825 C ALA A 240 5.090 117.252 282.362 1.00 49.35 A C ANISOU 1825 C ALA A 240 5404 6186 7160 -2049 1718 510 A C ATOM 1826 O ALA A 240 6.202 116.773 282.583 1.00 48.35 A O ANISOU 1826 O ALA A 240 5497 5904 6970 -2000 1680 559 A O ATOM 1827 CB ALA A 240 3.186 115.638 282.565 1.00 47.07 A C ANISOU 1827 CB ALA A 240 4953 5909 7025 -2353 1840 564 A C ATOM 1828 N VAL A 241 4.731 118.474 282.747 1.00 48.80 A N ANISOU 1828 N VAL A 241 5231 6285 7026 -1916 1752 495 A N ATOM 1829 CA VAL A 241 5.586 119.353 283.538 1.00 44.35 A C ANISOU 1829 CA VAL A 241 4812 5733 6308 -1731 1758 525 A C ATOM 1830 C VAL A 241 4.706 120.005 284.601 1.00 46.91 A C ANISOU 1830 C VAL A 241 5047 6202 6574 -1697 1930 567 A C ATOM 1831 O VAL A 241 3.732 120.679 284.272 1.00 46.82 A O ANISOU 1831 O VAL A 241 4830 6341 6621 -1676 1959 517 A O ATOM 1832 CB VAL A 241 6.239 120.449 282.661 1.00 39.83 A C ANISOU 1832 CB VAL A 241 4226 5199 5710 -1569 1599 424 A C ATOM 1833 CG1 VAL A 241 7.094 121.392 283.501 1.00 38.29 A C ANISOU 1833 CG1 VAL A 241 4176 5017 5353 -1407 1614 436 A C ATOM 1834 CG2 VAL A 241 7.076 119.832 281.552 1.00 35.64 A C ANISOU 1834 CG2 VAL A 241 3768 4541 5231 -1595 1433 377 A C ATOM 1835 N GLU A 242 5.045 119.802 285.870 1.00 50.51 A N ANISOU 1835 N GLU A 242 5657 6626 6907 -1680 2046 664 A N ATOM 1836 CA GLU A 242 4.230 120.292 286.978 1.00 56.74 A C ANISOU 1836 CA GLU A 242 6384 7547 7628 -1657 2228 712 A C ATOM 1837 C GLU A 242 5.077 121.105 287.937 1.00 58.27 A C ANISOU 1837 C GLU A 242 6748 7762 7629 -1500 2250 722 A C ATOM 1838 O GLU A 242 6.115 120.639 288.409 1.00 58.30 A O ANISOU 1838 O GLU A 242 6949 7673 7529 -1482 2214 780 A O ATOM 1839 CB GLU A 242 3.581 119.135 287.742 1.00 60.91 A C ANISOU 1839 CB GLU A 242 6919 8042 8181 -1820 2382 832 A C ATOM 1840 CG GLU A 242 2.753 119.586 288.947 1.00 66.88 A C ANISOU 1840 CG GLU A 242 7620 8947 8844 -1771 2541 890 A C ATOM 1841 CD GLU A 242 2.042 118.438 289.658 1.00 72.80 A C ANISOU 1841 CD GLU A 242 8368 9681 9612 -1901 2630 1012 A C ATOM 1842 OE1 GLU A 242 2.172 117.279 289.210 1.00 72.64 A O ANISOU 1842 OE1 GLU A 242 8398 9518 9683 -2031 2573 1049 A O ATOM 1843 OE2 GLU A 242 1.360 118.698 290.676 1.00 72.34 A O1- ANISOU 1843 OE2 GLU A 242 8266 9745 9473 -1872 2763 1069 A O1- ATOM 1844 N ALA A 243 4.629 122.322 288.224 1.00 57.61 A N ANISOU 1844 N ALA A 243 6588 7808 7495 -1383 2313 662 A N ATOM 1845 CA ALA A 243 5.333 123.193 289.155 1.00 56.01 A C ANISOU 1845 CA ALA A 243 6541 7637 7105 -1251 2349 644 A C ATOM 1846 C ALA A 243 4.962 122.865 290.597 1.00 57.82 A C ANISOU 1846 C ALA A 243 6833 7925 7210 -1284 2539 745 A C ATOM 1847 O ALA A 243 3.794 122.946 290.980 1.00 58.55 A O ANISOU 1847 O ALA A 243 6785 8118 7342 -1315 2696 771 A O ATOM 1848 CB ALA A 243 5.012 124.644 288.849 1.00 54.84 A C ANISOU 1848 CB ALA A 243 6310 7573 6954 -1109 2354 530 A C ATOM 1849 N LYS A 244 5.958 122.482 291.392 1.00 58.38 A N ANISOU 1849 N LYS A 244 7107 7951 7124 -1271 2527 809 A N ATOM 1850 CA LYS A 244 5.748 122.266 292.818 1.00 58.45 A C ANISOU 1850 CA LYS A 244 7200 8033 6976 -1279 2700 907 A C ATOM 1851 C LYS A 244 6.758 123.101 293.596 1.00 58.72 A C ANISOU 1851 C LYS A 244 7406 8123 6784 -1159 2671 855 A C ATOM 1852 O LYS A 244 7.749 123.572 293.027 1.00 58.49 A O ANISOU 1852 O LYS A 244 7444 8049 6729 -1098 2508 769 A O ATOM 1853 CB LYS A 244 5.943 120.787 293.151 1.00 60.97 A C ANISOU 1853 CB LYS A 244 7605 8258 7302 -1387 2718 1065 A C ATOM 1854 CG LYS A 244 5.003 119.850 292.408 1.00 67.02 A C ANISOU 1854 CG LYS A 244 8221 8957 8287 -1527 2714 1102 A C ATOM 1855 CD LYS A 244 5.246 118.398 292.800 1.00 74.32 A C ANISOU 1855 CD LYS A 244 9264 9764 9213 -1615 2721 1252 A C ATOM 1856 CE LYS A 244 4.372 117.436 292.001 1.00 76.27 A C ANISOU 1856 CE LYS A 244 9380 9927 9674 -1775 2706 1266 A C ATOM 1857 NZ LYS A 244 4.682 116.011 292.326 1.00 74.43 A N1+ ANISOU 1857 NZ LYS A 244 9291 9542 9448 -1855 2717 1404 A N1+ ATOM 1858 N GLU A 245 6.563 123.211 294.907 1.00 60.11 A N ANISOU 1858 N GLU A 245 7652 8400 6785 -1136 2819 909 A N ATOM 1859 CA GLU A 245 7.336 124.161 295.699 1.00 59.96 A C ANISOU 1859 CA GLU A 245 7775 8467 6539 -1037 2817 828 A C ATOM 1860 C GLU A 245 8.819 123.799 295.720 1.00 54.52 A C ANISOU 1860 C GLU A 245 7247 7741 5727 -1021 2653 852 A C ATOM 1861 O GLU A 245 9.682 124.679 295.679 1.00 51.26 A O ANISOU 1861 O GLU A 245 6911 7360 5207 -956 2553 732 A O ATOM 1862 CB GLU A 245 6.816 124.249 297.134 1.00 66.79 A C ANISOU 1862 CB GLU A 245 8668 9467 7244 -999 2944 880 A C ATOM 1863 CG GLU A 245 5.389 124.775 297.278 1.00 78.93 A C ANISOU 1863 CG GLU A 245 10041 11078 8870 -976 3080 844 A C ATOM 1864 CD GLU A 245 5.022 125.019 298.733 1.00 89.39 A C ANISOU 1864 CD GLU A 245 11415 12546 10003 -927 3201 872 A C ATOM 1865 OE1 GLU A 245 5.941 124.998 299.583 1.00 93.14 A O ANISOU 1865 OE1 GLU A 245 12051 13072 10266 -898 3168 888 A O ATOM 1866 OE2 GLU A 245 3.819 125.187 299.036 1.00 91.77 A O1- ANISOU 1866 OE2 GLU A 245 11585 12926 10359 -918 3325 883 A O1- ATOM 1867 N ASP A 246 9.111 122.502 295.729 1.00 53.66 A N ANISOU 1867 N ASP A 246 7184 7561 5643 -1078 2626 1006 A N ATOM 1868 CA ASP A 246 10.491 122.059 295.846 1.00 56.68 A C ANISOU 1868 CA ASP A 246 7710 7930 5894 -1040 2485 1058 A C ATOM 1869 C ASP A 246 11.102 121.861 294.473 1.00 51.79 A C ANISOU 1869 C ASP A 246 7058 7180 5440 -1044 2295 1006 A C ATOM 1870 O ASP A 246 12.242 121.407 294.366 1.00 51.66 A O ANISOU 1870 O ASP A 246 7138 7140 5350 -1007 2168 1053 A O ATOM 1871 CB ASP A 246 10.576 120.734 296.618 1.00 63.28 A C ANISOU 1871 CB ASP A 246 8641 8747 6654 -1070 2568 1271 A C ATOM 1872 CG ASP A 246 9.900 119.581 295.884 1.00 69.08 A C ANISOU 1872 CG ASP A 246 9305 9314 7629 -1170 2595 1370 A C ATOM 1873 OD1 ASP A 246 10.370 118.430 296.016 1.00 72.65 A O ANISOU 1873 OD1 ASP A 246 9851 9679 8075 -1175 2569 1518 A O ATOM 1874 OD2 ASP A 246 8.909 119.822 295.164 1.00 72.89 A O1- ANISOU 1874 OD2 ASP A 246 9634 9755 8305 -1239 2632 1293 A O1- ATOM 1875 N GLY A 247 10.366 122.209 293.420 1.00 50.25 A N ANISOU 1875 N GLY A 247 6720 6916 5456 -1077 2275 913 A N ATOM 1876 CA GLY A 247 10.936 122.093 292.090 1.00 45.15 A C ANISOU 1876 CA GLY A 247 6042 6161 4953 -1076 2096 854 A C ATOM 1877 C GLY A 247 9.958 121.802 290.971 1.00 42.21 A C ANISOU 1877 C GLY A 247 5509 5700 4828 -1151 2094 826 A C ATOM 1878 O GLY A 247 8.750 121.727 291.175 1.00 42.57 A O ANISOU 1878 O GLY A 247 5443 5778 4953 -1210 2233 849 A O ATOM 1879 N ILE A 248 10.503 121.616 289.776 1.00 45.50 A N ANISOU 1879 N ILE A 248 5908 6022 5358 -1150 1933 777 A N ATOM 1880 CA ILE A 248 9.704 121.333 288.600 1.00 41.31 A C ANISOU 1880 CA ILE A 248 5227 5423 5046 -1223 1901 736 A C ATOM 1881 C ILE A 248 9.775 119.843 288.297 1.00 42.51 A C ANISOU 1881 C ILE A 248 5422 5438 5291 -1324 1890 840 A C ATOM 1882 O ILE A 248 10.853 119.305 288.023 1.00 41.55 A O ANISOU 1882 O ILE A 248 5421 5230 5136 -1290 1781 872 A O ATOM 1883 CB ILE A 248 10.248 122.099 287.385 1.00 38.02 A C ANISOU 1883 CB ILE A 248 4767 4987 4693 -1157 1732 607 A C ATOM 1884 CG1 ILE A 248 10.400 123.587 287.713 1.00 36.87 A C ANISOU 1884 CG1 ILE A 248 4628 4940 4442 -1051 1745 505 A C ATOM 1885 CG2 ILE A 248 9.381 121.852 286.157 1.00 39.56 A C ANISOU 1885 CG2 ILE A 248 4793 5144 5093 -1226 1693 560 A C ATOM 1886 CD1 ILE A 248 9.090 124.289 288.002 1.00 39.67 A C ANISOU 1886 CD1 ILE A 248 4851 5382 4839 -1041 1892 472 A C ATOM 1887 N TYR A 249 8.620 119.184 288.315 1.00 41.10 A N ANISOU 1887 N TYR A 249 5145 5239 5234 -1451 2009 888 A N ATOM 1888 CA TYR A 249 8.565 117.745 288.084 1.00 46.13 A C ANISOU 1888 CA TYR A 249 5837 5722 5969 -1573 2033 981 A C ATOM 1889 C TYR A 249 8.193 117.430 286.648 1.00 48.17 A C ANISOU 1889 C TYR A 249 5975 5906 6422 -1663 1930 886 A C ATOM 1890 O TYR A 249 7.142 117.846 286.157 1.00 50.89 A O ANISOU 1890 O TYR A 249 6125 6338 6874 -1726 1953 809 A O ATOM 1891 CB TYR A 249 7.603 117.084 289.067 1.00 47.43 A C ANISOU 1891 CB TYR A 249 5989 5897 6135 -1686 2241 1102 A C ATOM 1892 CG TYR A 249 8.194 116.948 290.446 1.00 48.84 A C ANISOU 1892 CG TYR A 249 6342 6107 6110 -1606 2333 1234 A C ATOM 1893 CD1 TYR A 249 8.301 118.045 291.290 1.00 47.88 A C ANISOU 1893 CD1 TYR A 249 6224 6151 5818 -1494 2368 1202 A C ATOM 1894 CD2 TYR A 249 8.624 115.713 290.914 1.00 49.47 A C ANISOU 1894 CD2 TYR A 249 6583 6056 6159 -1635 2381 1389 A C ATOM 1895 CE1 TYR A 249 8.842 117.921 292.550 1.00 51.43 A C ANISOU 1895 CE1 TYR A 249 6824 6656 6060 -1425 2445 1315 A C ATOM 1896 CE2 TYR A 249 9.161 115.578 292.172 1.00 53.77 A C ANISOU 1896 CE2 TYR A 249 7270 6660 6501 -1539 2440 1516 A C ATOM 1897 CZ TYR A 249 9.267 116.685 292.987 1.00 55.35 A C ANISOU 1897 CZ TYR A 249 7465 7045 6522 -1446 2480 1480 A C ATOM 1898 OH TYR A 249 9.804 116.554 294.244 1.00 58.37 A O ANISOU 1898 OH TYR A 249 7979 7514 6686 -1354 2523 1596 A O ATOM 1899 N AVAL A 250 9.050 116.666 285.983 0.24 45.44 A N ANISOU 1899 N AVAL A 250 5741 5410 6113 -1666 1822 894 A N ATOM 1900 N BVAL A 250 9.068 116.681 285.978 0.76 45.31 A N ANISOU 1900 N BVAL A 250 5726 5394 6095 -1663 1819 893 A N ATOM 1901 CA AVAL A 250 8.858 116.385 284.571 0.24 44.28 A C ANISOU 1901 CA AVAL A 250 5502 5195 6127 -1741 1708 788 A C ATOM 1902 CA BVAL A 250 8.939 116.405 284.551 0.76 43.33 A C ANISOU 1902 CA BVAL A 250 5390 5073 6001 -1732 1699 787 A C ATOM 1903 C AVAL A 250 8.757 114.893 284.310 0.24 47.45 A C ANISOU 1903 C AVAL A 250 5991 5402 6635 -1890 1755 848 A C ATOM 1904 C BVAL A 250 8.793 114.908 284.273 0.76 47.48 A C ANISOU 1904 C BVAL A 250 5995 5405 6638 -1885 1748 844 A C ATOM 1905 O AVAL A 250 9.539 114.087 284.817 0.24 49.02 A O ANISOU 1905 O AVAL A 250 6387 5466 6772 -1855 1788 961 A O ATOM 1906 O BVAL A 250 9.616 114.106 284.717 0.76 49.41 A O ANISOU 1906 O BVAL A 250 6438 5511 6823 -1847 1772 952 A O ATOM 1907 CB AVAL A 250 9.941 117.036 283.677 0.24 39.04 A C ANISOU 1907 CB AVAL A 250 4870 4535 5430 -1603 1515 694 A C ATOM 1908 CB BVAL A 250 10.170 116.933 283.784 0.76 39.83 A C ANISOU 1908 CB BVAL A 250 5010 4616 5508 -1588 1512 712 A C ATOM 1909 CG1AVAL A 250 10.025 118.529 283.944 0.24 37.59 A C ANISOU 1909 CG1AVAL A 250 4619 4517 5147 -1472 1488 631 A C ATOM 1910 CG1BVAL A 250 10.052 116.625 282.299 0.76 37.38 A C ANISOU 1910 CG1BVAL A 250 4618 4240 5344 -1653 1390 603 A C ATOM 1911 CG2AVAL A 250 11.284 116.389 283.899 0.24 38.97 A C ANISOU 1911 CG2AVAL A 250 5070 4406 5330 -1520 1462 774 A C ATOM 1912 CG2BVAL A 250 10.338 118.431 284.007 0.76 34.92 A C ANISOU 1912 CG2BVAL A 250 4327 4157 4785 -1454 1473 645 A C ATOM 1913 N THR A 251 7.747 114.532 283.539 1.00 49.09 A N ANISOU 1913 N THR A 251 6049 5603 7001 -2058 1767 771 A N ATOM 1914 CA THR A 251 7.547 113.146 283.169 1.00 50.42 A C ANISOU 1914 CA THR A 251 6289 5592 7276 -2200 1781 791 A C ATOM 1915 C THR A 251 7.959 112.953 281.726 1.00 51.74 A C ANISOU 1915 C THR A 251 6445 5679 7534 -2224 1627 661 A C ATOM 1916 O THR A 251 7.594 113.738 280.845 1.00 48.08 A O ANISOU 1916 O THR A 251 5803 5347 7120 -2233 1535 533 A O ATOM 1917 CB THR A 251 6.084 112.707 283.347 1.00 51.22 A C ANISOU 1917 CB THR A 251 6231 5765 7465 -2356 1855 790 A C ATOM 1918 CG2 THR A 251 5.892 111.270 282.849 1.00 49.83 A C ANISOU 1918 CG2 THR A 251 6135 5401 7395 -2496 1840 786 A C ATOM 1919 OG1 THR A 251 5.734 112.783 284.735 1.00 54.10 A O ANISOU 1919 OG1 THR A 251 6623 6194 7738 -2330 2005 921 A O ATOM 1920 N MET A 252 8.750 111.912 281.500 1.00 53.91 A N ANISOU 1920 N MET A 252 6918 5744 7821 -2217 1603 699 A N ATOM 1921 CA MET A 252 9.231 111.607 280.172 1.00 50.96 A C ANISOU 1921 CA MET A 252 6566 5277 7521 -2230 1465 579 A C ATOM 1922 C MET A 252 8.771 110.215 279.794 1.00 56.96 A C ANISOU 1922 C MET A 252 7388 5875 8381 -2367 1481 564 A C ATOM 1923 O MET A 252 8.542 109.363 280.651 1.00 57.26 A O ANISOU 1923 O MET A 252 7532 5810 8415 -2410 1601 681 A O ATOM 1924 CB MET A 252 10.753 111.727 280.102 1.00 48.13 A C ANISOU 1924 CB MET A 252 6389 4832 7065 -2041 1388 620 A C ATOM 1925 CG MET A 252 11.257 113.125 280.427 1.00 46.23 A C ANISOU 1925 CG MET A 252 6078 4797 6691 -1849 1301 616 A C ATOM 1926 SD MET A 252 13.049 113.222 280.619 1.00 57.28 A S ANISOU 1926 SD MET A 252 7671 6153 7939 -1610 1202 688 A S ATOM 1927 CE MET A 252 13.202 113.170 282.403 1.00 57.65 A C ANISOU 1927 CE MET A 252 7829 6239 7836 -1545 1353 876 A C ATOM 1928 N GLU A 253 8.635 109.992 278.498 1.00 60.43 A N ANISOU 1928 N GLU A 253 7761 6295 8902 -2435 1361 416 A N ATOM 1929 CA GLU A 253 8.313 108.681 277.988 1.00 64.79 A C ANISOU 1929 CA GLU A 253 8390 6683 9544 -2564 1366 374 A C ATOM 1930 C GLU A 253 9.244 108.451 276.815 1.00 62.35 A C ANISOU 1930 C GLU A 253 8178 6264 9247 -2501 1239 271 A C ATOM 1931 O GLU A 253 9.566 109.387 276.084 1.00 62.19 A O ANISOU 1931 O GLU A 253 8057 6370 9204 -2430 1120 179 A O ATOM 1932 CB GLU A 253 6.839 108.694 277.580 1.00 70.49 A C ANISOU 1932 CB GLU A 253 8877 7557 10349 -2747 1353 279 A C ATOM 1933 CG GLU A 253 6.418 107.774 276.471 1.00 78.99 A C ANISOU 1933 CG GLU A 253 9944 8553 11516 -2893 1285 147 A C ATOM 1934 CD GLU A 253 4.970 108.013 276.084 1.00 85.75 A C ANISOU 1934 CD GLU A 253 10532 9618 12432 -3052 1259 60 A C ATOM 1935 OE1 GLU A 253 4.161 108.342 276.981 1.00 86.33 A O ANISOU 1935 OE1 GLU A 253 10485 9814 12501 -3093 1357 143 A O ATOM 1936 OE2 GLU A 253 4.646 107.884 274.885 1.00 88.34 A O1- ANISOU 1936 OE2 GLU A 253 10762 10000 12801 -3128 1142 -87 A O1- ATOM 1937 N GLY A 254 9.677 107.211 276.630 1.00 62.35 A N ANISOU 1937 N GLY A 254 8376 6032 9281 -2518 1271 286 A N ATOM 1938 CA GLY A 254 10.600 106.898 275.557 1.00 59.09 A C ANISOU 1938 CA GLY A 254 8075 5503 8875 -2444 1168 194 A C ATOM 1939 C GLY A 254 11.764 106.041 276.022 1.00 58.49 A C ANISOU 1939 C GLY A 254 8277 5186 8759 -2305 1241 319 A C ATOM 1940 O GLY A 254 11.799 105.572 277.164 1.00 56.61 A O ANISOU 1940 O GLY A 254 8153 4866 8492 -2277 1372 480 A O ATOM 1941 N LYS A 255 12.725 105.852 275.125 1.00 60.61 A N ANISOU 1941 N LYS A 255 8651 5359 9019 -2203 1155 251 A N ATOM 1942 CA LYS A 255 13.798 104.876 275.297 1.00 65.35 A C ANISOU 1942 CA LYS A 255 9511 5724 9595 -2063 1214 346 A C ATOM 1943 C LYS A 255 14.699 105.084 276.512 1.00 66.30 A C ANISOU 1943 C LYS A 255 9760 5824 9605 -1869 1293 558 A C ATOM 1944 O LYS A 255 15.193 104.119 277.100 1.00 64.88 A O ANISOU 1944 O LYS A 255 9775 5471 9404 -1780 1392 691 A O ATOM 1945 CB LYS A 255 14.658 104.834 274.031 1.00 66.49 A C ANISOU 1945 CB LYS A 255 9710 5812 9739 -1973 1095 221 A C ATOM 1946 CG LYS A 255 13.909 104.343 272.803 1.00 70.98 A C ANISOU 1946 CG LYS A 255 10202 6369 10397 -2146 1026 21 A C ATOM 1947 CD LYS A 255 14.841 104.157 271.613 1.00 72.44 A C ANISOU 1947 CD LYS A 255 10475 6480 10569 -2040 928 -90 A C ATOM 1948 CE LYS A 255 14.153 103.381 270.494 1.00 75.51 A C ANISOU 1948 CE LYS A 255 10840 6818 11033 -2209 888 -272 A C ATOM 1949 NZ LYS A 255 13.100 104.186 269.810 1.00 76.45 A N1+ ANISOU 1949 NZ LYS A 255 10695 7184 11170 -2362 771 -415 A N1+ ATOM 1950 N LYS A 256 14.910 106.337 276.897 1.00 67.19 A N ANISOU 1950 N LYS A 256 9765 6126 9640 -1798 1250 592 A N ATOM 1951 CA LYS A 256 15.873 106.618 277.946 1.00 69.61 A C ANISOU 1951 CA LYS A 256 10190 6445 9815 -1602 1302 783 A C ATOM 1952 C LYS A 256 15.154 107.306 279.094 1.00 69.27 A C ANISOU 1952 C LYS A 256 10036 6565 9719 -1658 1379 870 A C ATOM 1953 O LYS A 256 15.787 107.872 279.986 1.00 68.80 A O ANISOU 1953 O LYS A 256 10007 6614 9521 -1504 1389 1000 A O ATOM 1954 CB LYS A 256 16.961 107.549 277.405 1.00 69.93 A C ANISOU 1954 CB LYS A 256 10189 6620 9761 -1415 1147 741 A C ATOM 1955 CG LYS A 256 17.942 106.888 276.436 1.00 72.02 A C ANISOU 1955 CG LYS A 256 10593 6727 10043 -1301 1088 694 A C ATOM 1956 CD LYS A 256 18.609 105.640 276.990 1.00 78.43 A C ANISOU 1956 CD LYS A 256 11658 7303 10837 -1185 1217 861 A C ATOM 1957 CE LYS A 256 19.594 105.952 278.097 1.00 80.57 A C ANISOU 1957 CE LYS A 256 11987 7687 10937 -948 1226 1065 A C ATOM 1958 NZ LYS A 256 20.387 104.737 278.430 1.00 82.74 A N1+ ANISOU 1958 NZ LYS A 256 12486 7768 11184 -781 1317 1217 A N1+ ATOM 1959 N ALA A 257 13.827 107.246 279.072 1.00 70.26 A N ANISOU 1959 N ALA A 257 10014 6745 9934 -1858 1413 793 A N ATOM 1960 CA ALA A 257 13.022 107.864 280.116 1.00 68.36 A C ANISOU 1960 CA ALA A 257 9655 6665 9652 -1916 1495 863 A C ATOM 1961 C ALA A 257 13.143 107.088 281.420 1.00 70.71 A C ANISOU 1961 C ALA A 257 10109 6876 9881 -1859 1638 1064 A C ATOM 1962 O ALA A 257 13.158 105.857 281.418 1.00 73.02 A O ANISOU 1962 O ALA A 257 10542 6976 10226 -1882 1697 1108 A O ATOM 1963 CB ALA A 257 11.569 107.941 279.682 1.00 67.17 A C ANISOU 1963 CB ALA A 257 9298 6609 9616 -2131 1489 733 A C ATOM 1964 N PRO A 258 13.226 107.811 282.543 1.00 67.34 A N ANISOU 1964 N PRO A 258 9661 6597 9327 -1779 1696 1183 A N ATOM 1965 CA PRO A 258 13.186 107.200 283.875 1.00 62.72 A C ANISOU 1965 CA PRO A 258 9191 5982 8659 -1732 1830 1373 A C ATOM 1966 C PRO A 258 11.771 106.756 284.212 1.00 64.04 A C ANISOU 1966 C PRO A 258 9260 6151 8921 -1934 1929 1358 A C ATOM 1967 O PRO A 258 10.821 107.230 283.590 1.00 60.24 A O ANISOU 1967 O PRO A 258 8586 5765 8536 -2086 1889 1212 A O ATOM 1968 CB PRO A 258 13.614 108.347 284.800 1.00 61.00 A C ANISOU 1968 CB PRO A 258 8937 5975 8265 -1603 1837 1458 A C ATOM 1969 CG PRO A 258 14.288 109.350 283.892 1.00 61.27 A C ANISOU 1969 CG PRO A 258 8897 6102 8281 -1528 1685 1331 A C ATOM 1970 CD PRO A 258 13.536 109.248 282.609 1.00 62.68 A C ANISOU 1970 CD PRO A 258 8960 6211 8644 -1705 1633 1147 A C ATOM 1971 N ALA A 259 11.630 105.863 285.186 1.00 67.78 A N ANISOU 1971 N ALA A 259 9857 6534 9362 -1929 2055 1513 A N ATOM 1972 CA ALA A 259 10.315 105.356 285.550 1.00 69.95 A C ANISOU 1972 CA ALA A 259 10052 6800 9723 -2125 2160 1514 A C ATOM 1973 C ALA A 259 9.499 106.461 286.204 1.00 70.91 A C ANISOU 1973 C ALA A 259 9980 7173 9790 -2172 2194 1508 A C ATOM 1974 O ALA A 259 8.320 106.646 285.895 1.00 72.31 A O ANISOU 1974 O ALA A 259 9974 7435 10068 -2346 2204 1409 A O ATOM 1975 CB ALA A 259 10.443 104.163 286.483 1.00 70.90 A C ANISOU 1975 CB ALA A 259 10367 6761 9811 -2094 2295 1694 A C ATOM 1976 N GLU A 260 10.139 107.203 287.102 1.00 68.28 A N ANISOU 1976 N GLU A 260 9683 6972 9287 -2007 2209 1612 A N ATOM 1977 CA GLU A 260 9.452 108.224 287.881 1.00 67.30 A C ANISOU 1977 CA GLU A 260 9405 7080 9084 -2024 2262 1620 A C ATOM 1978 C GLU A 260 9.692 109.617 287.321 1.00 62.01 A C ANISOU 1978 C GLU A 260 8600 6577 8384 -1967 2158 1490 A C ATOM 1979 O GLU A 260 10.710 109.863 286.673 1.00 58.53 A O ANISOU 1979 O GLU A 260 8227 6091 7919 -1863 2053 1448 A O ATOM 1980 CB GLU A 260 9.915 108.171 289.341 1.00 72.79 A C ANISOU 1980 CB GLU A 260 10227 7838 9590 -1887 2357 1811 A C ATOM 1981 CG GLU A 260 9.565 106.889 290.076 1.00 78.53 A C ANISOU 1981 CG GLU A 260 11078 8426 10333 -1941 2482 1957 A C ATOM 1982 CD GLU A 260 8.067 106.643 290.130 1.00 84.22 A C ANISOU 1982 CD GLU A 260 11650 9171 11179 -2160 2572 1914 A C ATOM 1983 OE1 GLU A 260 7.298 107.629 290.187 1.00 83.34 A O ANISOU 1983 OE1 GLU A 260 11342 9259 11066 -2216 2575 1832 A O ATOM 1984 OE2 GLU A 260 7.658 105.463 290.127 1.00 89.87 A O1- ANISOU 1984 OE2 GLU A 260 12445 9712 11991 -2271 2646 1963 A O1- ATOM 1985 N PRO A 261 8.749 110.537 287.576 1.00 60.06 A N ANISOU 1985 N PRO A 261 8161 6524 8135 -2028 2194 1428 A N ATOM 1986 CA PRO A 261 8.936 111.951 287.235 1.00 55.45 A C ANISOU 1986 CA PRO A 261 7455 6110 7503 -1958 2123 1318 A C ATOM 1987 C PRO A 261 10.183 112.496 287.920 1.00 54.98 A C ANISOU 1987 C PRO A 261 7541 6102 7246 -1770 2111 1401 A C ATOM 1988 O PRO A 261 10.446 112.148 289.070 1.00 59.60 A O ANISOU 1988 O PRO A 261 8244 6705 7696 -1698 2194 1549 A O ATOM 1989 CB PRO A 261 7.681 112.618 287.798 1.00 55.90 A C ANISOU 1989 CB PRO A 261 7322 6355 7561 -2026 2215 1294 A C ATOM 1990 CG PRO A 261 6.650 111.537 287.821 1.00 59.26 A C ANISOU 1990 CG PRO A 261 7703 6703 8109 -2193 2283 1327 A C ATOM 1991 CD PRO A 261 7.382 110.246 288.045 1.00 60.28 A C ANISOU 1991 CD PRO A 261 8062 6612 8228 -2178 2303 1446 A C ATOM 1992 N GLN A 262 10.940 113.338 287.228 1.00 47.23 A N ANISOU 1992 N GLN A 262 6140 5441 6362 -1246 1572 1604 A N ATOM 1993 CA GLN A 262 12.192 113.842 287.774 1.00 49.07 A C ANISOU 1993 CA GLN A 262 6416 5744 6483 -1095 1584 1606 A C ATOM 1994 C GLN A 262 12.050 115.275 288.259 1.00 43.84 A C ANISOU 1994 C GLN A 262 5643 5297 5718 -1037 1618 1523 A C ATOM 1995 O GLN A 262 11.356 116.079 287.640 1.00 42.31 A O ANISOU 1995 O GLN A 262 5359 5149 5570 -1070 1603 1418 A O ATOM 1996 CB GLN A 262 13.294 113.769 286.718 1.00 53.15 A C ANISOU 1996 CB GLN A 262 7027 6110 7058 -1006 1516 1540 A C ATOM 1997 CG GLN A 262 13.624 112.364 286.266 1.00 58.31 A C ANISOU 1997 CG GLN A 262 7801 6548 7806 -1036 1477 1607 A C ATOM 1998 CD GLN A 262 14.183 111.530 287.394 1.00 64.69 A C ANISOU 1998 CD GLN A 262 8679 7356 8543 -1000 1512 1757 A C ATOM 1999 NE2 GLN A 262 13.585 110.368 287.626 1.00 63.73 A N ANISOU 1999 NE2 GLN A 262 8598 7133 8484 -1107 1520 1861 A N ATOM 2000 OE1 GLN A 262 15.144 111.928 288.055 1.00 67.93 A O ANISOU 2000 OE1 GLN A 262 9107 7859 8843 -879 1529 1781 A O ATOM 2001 N ARG A 263 12.712 115.587 289.370 1.00 42.87 A N ANISOU 2001 N ARG A 263 5527 5305 5455 -947 1657 1566 A N ATOM 2002 CA ARG A 263 12.680 116.937 289.922 1.00 45.69 A C ANISOU 2002 CA ARG A 263 5789 5865 5705 -881 1685 1476 A C ATOM 2003 C ARG A 263 13.881 117.758 289.440 1.00 45.62 A C ANISOU 2003 C ARG A 263 5812 5853 5669 -749 1636 1384 A C ATOM 2004 O ARG A 263 15.030 117.329 289.551 1.00 47.61 A O ANISOU 2004 O ARG A 263 6159 6045 5887 -665 1614 1434 A O ATOM 2005 CB ARG A 263 12.641 116.889 291.456 1.00 49.46 A C ANISOU 2005 CB ARG A 263 6251 6504 6038 -863 1755 1555 A C ATOM 2006 CG ARG A 263 12.347 118.233 292.119 1.00 51.88 A C ANISOU 2006 CG ARG A 263 6451 7023 6238 -815 1791 1448 A C ATOM 2007 CD ARG A 263 12.796 118.252 293.572 1.00 55.41 A C ANISOU 2007 CD ARG A 263 6915 7612 6527 -751 1841 1506 A C ATOM 2008 NE ARG A 263 14.208 117.908 293.670 1.00 59.35 A N ANISOU 2008 NE ARG A 263 7515 8055 6980 -647 1794 1558 A N ATOM 2009 CZ ARG A 263 15.205 118.767 293.475 1.00 63.93 A C ANISOU 2009 CZ ARG A 263 8102 8675 7515 -533 1746 1466 A C ATOM 2010 NH1 ARG A 263 14.951 120.032 293.157 1.00 61.84 A N1+ ANISOU 2010 NH1 ARG A 263 7754 8494 7248 -510 1735 1316 A N1+ ATOM 2011 NH2 ARG A 263 16.462 118.355 293.582 1.00 67.00 A N ANISOU 2011 NH2 ARG A 263 8578 9014 7864 -443 1706 1522 A N ATOM 2012 N TYR A 264 13.599 118.938 288.898 1.00 41.49 A N ANISOU 2012 N TYR A 264 5206 5395 5163 -730 1619 1252 A N ATOM 2013 CA TYR A 264 14.634 119.860 288.442 1.00 36.75 A C ANISOU 2013 CA TYR A 264 4621 4805 4536 -616 1576 1154 A C ATOM 2014 C TYR A 264 14.467 121.219 289.107 1.00 36.73 A C ANISOU 2014 C TYR A 264 4517 5001 4436 -564 1595 1055 A C ATOM 2015 O TYR A 264 13.362 121.583 289.511 1.00 34.45 A O ANISOU 2015 O TYR A 264 4132 4818 4140 -625 1634 1028 A O ATOM 2016 CB TYR A 264 14.591 119.996 286.921 1.00 34.29 A C ANISOU 2016 CB TYR A 264 4324 4345 4359 -639 1522 1071 A C ATOM 2017 CG TYR A 264 14.957 118.729 286.195 1.00 35.87 A C ANISOU 2017 CG TYR A 264 4639 4340 4650 -670 1492 1137 A C ATOM 2018 CD1 TYR A 264 16.282 118.433 285.910 1.00 32.72 A C ANISOU 2018 CD1 TYR A 264 4344 3854 4235 -575 1461 1150 A C ATOM 2019 CD2 TYR A 264 13.988 117.801 285.847 1.00 37.18 A C ANISOU 2019 CD2 TYR A 264 4807 4404 4915 -792 1490 1184 A C ATOM 2020 CE1 TYR A 264 16.628 117.270 285.253 1.00 32.58 A C ANISOU 2020 CE1 TYR A 264 4431 3647 4299 -593 1431 1197 A C ATOM 2021 CE2 TYR A 264 14.326 116.635 285.202 1.00 41.26 A C ANISOU 2021 CE2 TYR A 264 5431 4730 5516 -818 1455 1229 A C ATOM 2022 CZ TYR A 264 15.643 116.370 284.905 1.00 42.12 A C ANISOU 2022 CZ TYR A 264 5645 4750 5610 -715 1427 1233 A C ATOM 2023 OH TYR A 264 15.967 115.195 284.259 1.00 42.27 A O ANISOU 2023 OH TYR A 264 5771 4577 5715 -733 1390 1266 A O ATOM 2024 N ASP A 265 15.568 121.951 289.250 1.00 35.84 A N ANISOU 2024 N ASP A 265 4426 4940 4250 -452 1566 997 A N ATOM 2025 CA ASP A 265 15.512 123.286 289.829 1.00 38.48 A C ANISOU 2025 CA ASP A 265 4674 5446 4501 -397 1571 881 A C ATOM 2026 C ASP A 265 15.146 124.306 288.751 1.00 39.57 A C ANISOU 2026 C ASP A 265 4745 5557 4733 -399 1533 751 A C ATOM 2027 O ASP A 265 14.656 125.402 289.048 1.00 39.64 A O ANISOU 2027 O ASP A 265 4659 5689 4715 -381 1538 646 A O ATOM 2028 CB ASP A 265 16.845 123.634 290.492 1.00 42.07 A C ANISOU 2028 CB ASP A 265 5177 5969 4838 -284 1546 870 A C ATOM 2029 CG ASP A 265 17.237 122.635 291.566 1.00 49.23 A C ANISOU 2029 CG ASP A 265 6149 6905 5653 -273 1577 1004 A C ATOM 2030 OD1 ASP A 265 16.640 122.670 292.664 1.00 57.00 A O ANISOU 2030 OD1 ASP A 265 7090 8012 6554 -297 1630 1024 A O ATOM 2031 OD2 ASP A 265 18.150 121.818 291.311 1.00 49.02 A O1- ANISOU 2031 OD2 ASP A 265 6215 6773 5637 -235 1549 1090 A O1- ATOM 2032 N ALA A 266 15.387 123.930 287.498 1.00 38.59 A N ANISOU 2032 N ALA A 266 4675 5267 4722 -418 1494 753 A N ATOM 2033 CA ALA A 266 14.994 124.743 286.351 1.00 37.57 A C ANISOU 2033 CA ALA A 266 4492 5086 4696 -432 1454 642 A C ATOM 2034 C ALA A 266 14.897 123.879 285.099 1.00 33.61 A C ANISOU 2034 C ALA A 266 4056 4392 4320 -498 1426 672 A C ATOM 2035 O ALA A 266 15.623 122.895 284.956 1.00 32.71 A O ANISOU 2035 O ALA A 266 4050 4170 4209 -489 1421 750 A O ATOM 2036 CB ALA A 266 15.989 125.878 286.127 1.00 37.31 A C ANISOU 2036 CB ALA A 266 4458 5089 4628 -330 1410 540 A C ATOM 2037 N VAL A 267 14.014 124.268 284.184 1.00 31.40 A N ANISOU 2037 N VAL A 267 3713 4072 4144 -559 1399 599 A N ATOM 2038 CA VAL A 267 13.868 123.586 282.904 1.00 30.67 A C ANISOU 2038 CA VAL A 267 3675 3809 4170 -626 1358 596 A C ATOM 2039 C VAL A 267 13.968 124.616 281.787 1.00 30.56 A C ANISOU 2039 C VAL A 267 3625 3770 4217 -603 1301 473 A C ATOM 2040 O VAL A 267 13.206 125.585 281.766 1.00 28.77 A O ANISOU 2040 O VAL A 267 3289 3632 4010 -608 1291 399 A O ATOM 2041 CB VAL A 267 12.514 122.837 282.798 1.00 33.18 A C ANISOU 2041 CB VAL A 267 3947 4097 4562 -748 1365 638 A C ATOM 2042 CG1 VAL A 267 12.318 122.257 281.399 1.00 27.91 A C ANISOU 2042 CG1 VAL A 267 3328 3265 4013 -816 1303 605 A C ATOM 2043 CG2 VAL A 267 12.407 121.744 283.858 1.00 31.61 A C ANISOU 2043 CG2 VAL A 267 3787 3911 4310 -783 1419 771 A C ATOM 2044 N LEU A 268 14.921 124.416 280.878 1.00 23.04 A N ANISOU 2044 N LEU A 268 2762 2703 3291 -573 1264 455 A N ATOM 2045 CA LEU A 268 15.064 125.281 279.717 1.00 24.43 A C ANISOU 2045 CA LEU A 268 2913 2850 3521 -556 1193 348 A C ATOM 2046 C LEU A 268 14.314 124.651 278.553 1.00 31.70 A C ANISOU 2046 C LEU A 268 3843 3651 4549 -655 1152 330 A C ATOM 2047 O LEU A 268 14.642 123.544 278.119 1.00 31.68 A O ANISOU 2047 O LEU A 268 3942 3523 4573 -685 1144 373 A O ATOM 2048 CB LEU A 268 16.545 125.461 279.347 1.00 24.07 A C ANISOU 2048 CB LEU A 268 2954 2770 3422 -455 1141 327 A C ATOM 2049 CG LEU A 268 16.837 126.119 277.985 1.00 22.80 A C ANISOU 2049 CG LEU A 268 2792 2562 3308 -436 1049 233 A C ATOM 2050 CD1 LEU A 268 16.323 127.544 277.922 1.00 20.10 A C ANISOU 2050 CD1 LEU A 268 2335 2316 2986 -420 1021 149 A C ATOM 2051 CD2 LEU A 268 18.316 126.075 277.627 1.00 18.57 A C ANISOU 2051 CD2 LEU A 268 2345 1990 2721 -345 1010 232 A C ATOM 2052 N VAL A 269 13.303 125.356 278.051 1.00 26.58 A N ANISOU 2052 N VAL A 269 3091 3046 3962 -700 1119 261 A N ATOM 2053 CA VAL A 269 12.546 124.874 276.906 1.00 26.13 A C ANISOU 2053 CA VAL A 269 3032 2903 3995 -786 1055 230 A C ATOM 2054 C VAL A 269 13.179 125.444 275.638 1.00 27.48 A C ANISOU 2054 C VAL A 269 3231 3024 4187 -747 976 149 A C ATOM 2055 O VAL A 269 12.985 126.612 275.302 1.00 27.49 A O ANISOU 2055 O VAL A 269 3151 3096 4197 -711 934 83 A O ATOM 2056 CB VAL A 269 11.054 125.267 276.996 1.00 24.76 A C ANISOU 2056 CB VAL A 269 2728 2813 3866 -848 1042 207 A C ATOM 2057 CG1 VAL A 269 10.300 124.742 275.802 1.00 26.81 A C ANISOU 2057 CG1 VAL A 269 2985 2994 4206 -934 967 175 A C ATOM 2058 CG2 VAL A 269 10.431 124.730 278.277 1.00 27.80 A C ANISOU 2058 CG2 VAL A 269 3080 3267 4215 -882 1116 292 A C ATOM 2059 N ALA A 270 13.961 124.622 274.948 1.00 27.27 A N ANISOU 2059 N ALA A 270 3323 2883 4156 -738 944 156 A N ATOM 2060 CA ALA A 270 14.663 125.082 273.757 1.00 24.58 A C ANISOU 2060 CA ALA A 270 3018 2512 3807 -685 860 87 A C ATOM 2061 C ALA A 270 14.315 124.201 272.569 1.00 22.56 A C ANISOU 2061 C ALA A 270 2816 2143 3611 -760 809 56 A C ATOM 2062 O ALA A 270 15.200 123.647 271.912 1.00 23.66 A O ANISOU 2062 O ALA A 270 3061 2202 3727 -722 779 42 A O ATOM 2063 CB ALA A 270 16.157 125.098 273.997 1.00 20.77 A C ANISOU 2063 CB ALA A 270 2624 2024 3244 -575 865 107 A C ATOM 2064 N ILE A 271 13.016 124.113 272.286 1.00 26.54 A N ANISOU 2064 N ILE A 271 3242 2654 4188 -862 793 36 A N ATOM 2065 CA ILE A 271 12.470 123.250 271.234 1.00 31.01 A C ANISOU 2065 CA ILE A 271 3845 3139 4799 -936 723 0 A C ATOM 2066 C ILE A 271 12.722 123.827 269.843 1.00 31.86 A C ANISOU 2066 C ILE A 271 3954 3242 4908 -917 640 -85 A C ATOM 2067 O ILE A 271 12.896 123.088 268.870 1.00 35.41 A O ANISOU 2067 O ILE A 271 4482 3608 5364 -940 587 -126 A O ATOM 2068 CB ILE A 271 10.947 123.046 271.445 1.00 44.48 A C ANISOU 2068 CB ILE A 271 5452 4891 6556 -1031 711 14 A C ATOM 2069 CG1 ILE A 271 10.704 122.230 272.708 1.00 45.99 A C ANISOU 2069 CG1 ILE A 271 5657 5072 6743 -1064 789 107 A C ATOM 2070 CG2 ILE A 271 10.316 122.304 270.282 1.00 46.73 A C ANISOU 2070 CG2 ILE A 271 5759 5108 6888 -1112 627 -34 A C ATOM 2071 CD1 ILE A 271 11.537 120.966 272.757 1.00 47.97 A C ANISOU 2071 CD1 ILE A 271 6051 5190 6985 -1058 806 149 A C ATOM 2072 N GLY A 272 12.754 125.150 269.754 1.00 28.40 A N ANISOU 2072 N GLY A 272 3432 2903 4457 -864 620 -111 A N ATOM 2073 CA GLY A 272 12.962 125.815 268.482 1.00 26.57 A C ANISOU 2073 CA GLY A 272 3190 2693 4211 -832 531 -174 A C ATOM 2074 C GLY A 272 12.365 127.204 268.517 1.00 28.02 A C ANISOU 2074 C GLY A 272 3243 2988 4416 -810 505 -189 A C ATOM 2075 O GLY A 272 11.986 127.693 269.585 1.00 28.21 A O ANISOU 2075 O GLY A 272 3193 3072 4453 -799 561 -161 A O ATOM 2076 N ARG A 273 12.272 127.833 267.348 1.00 24.22 A N ANISOU 2076 N ARG A 273 2733 2534 3936 -798 420 -234 A N ATOM 2077 CA ARG A 273 11.777 129.203 267.234 1.00 27.08 A C ANISOU 2077 CA ARG A 273 2977 2988 4325 -764 383 -245 A C ATOM 2078 C ARG A 273 10.772 129.323 266.085 1.00 27.91 A C ANISOU 2078 C ARG A 273 3015 3116 4475 -827 297 -284 A C ATOM 2079 O ARG A 273 10.872 128.603 265.091 1.00 29.75 A O ANISOU 2079 O ARG A 273 3313 3303 4688 -866 246 -314 A O ATOM 2080 CB ARG A 273 12.949 130.178 267.045 1.00 26.08 A C ANISOU 2080 CB ARG A 273 2878 2887 4143 -656 363 -240 A C ATOM 2081 CG ARG A 273 13.902 130.239 268.244 1.00 21.16 A C ANISOU 2081 CG ARG A 273 2300 2263 3476 -590 440 -206 A C ATOM 2082 CD ARG A 273 15.123 131.124 267.980 1.00 23.34 A C ANISOU 2082 CD ARG A 273 2605 2561 3704 -495 414 -203 A C ATOM 2083 NE ARG A 273 14.770 132.528 267.764 1.00 21.14 A N ANISOU 2083 NE ARG A 273 2227 2340 3465 -463 369 -216 A N ATOM 2084 CZ ARG A 273 14.461 133.387 268.732 1.00 20.55 A C ANISOU 2084 CZ ARG A 273 2075 2310 3424 -434 400 -219 A C ATOM 2085 NH1 ARG A 273 14.460 132.995 270.002 1.00 16.29 A N1+ ANISOU 2085 NH1 ARG A 273 1541 1781 2867 -433 479 -209 A N1+ ATOM 2086 NH2 ARG A 273 14.163 134.649 268.431 1.00 15.49 A N ANISOU 2086 NH2 ARG A 273 1352 1703 2831 -400 353 -234 A N ATOM 2087 N VAL A 274 9.789 130.207 266.248 1.00 29.35 A N ANISOU 2087 N VAL A 274 3069 3374 4708 -829 278 -284 A N ATOM 2088 CA VAL A 274 8.764 130.448 265.233 1.00 25.47 A C ANISOU 2088 CA VAL A 274 2506 2928 4243 -868 188 -306 A C ATOM 2089 C VAL A 274 8.755 131.922 264.802 1.00 26.28 A C ANISOU 2089 C VAL A 274 2527 3096 4363 -792 133 -305 A C ATOM 2090 O VAL A 274 9.028 132.810 265.616 1.00 22.46 A O ANISOU 2090 O VAL A 274 2008 2637 3889 -721 175 -288 A O ATOM 2091 CB VAL A 274 7.367 130.043 265.747 1.00 25.66 A C ANISOU 2091 CB VAL A 274 2456 2993 4302 -933 201 -291 A C ATOM 2092 CG1 VAL A 274 7.278 128.531 265.916 1.00 29.91 A C ANISOU 2092 CG1 VAL A 274 3074 3455 4834 -1020 231 -286 A C ATOM 2093 CG2 VAL A 274 7.064 130.744 267.057 1.00 23.87 A C ANISOU 2093 CG2 VAL A 274 2157 2821 4090 -882 273 -262 A C ATOM 2094 N PRO A 275 8.460 132.183 263.514 1.00 22.23 A N ANISOU 2094 N PRO A 275 1986 2609 3852 -807 37 -323 A N ATOM 2095 CA PRO A 275 8.476 133.542 262.946 1.00 22.36 A C ANISOU 2095 CA PRO A 275 1932 2677 3886 -736 -26 -307 A C ATOM 2096 C PRO A 275 7.327 134.440 263.431 1.00 26.48 A C ANISOU 2096 C PRO A 275 2339 3268 4455 -704 -30 -289 A C ATOM 2097 O PRO A 275 6.246 133.942 263.754 1.00 18.72 A O ANISOU 2097 O PRO A 275 1310 2314 3489 -759 -17 -293 A O ATOM 2098 CB PRO A 275 8.341 133.291 261.442 1.00 17.88 A C ANISOU 2098 CB PRO A 275 1377 2128 3288 -774 -127 -326 A C ATOM 2099 CG PRO A 275 7.586 131.998 261.361 1.00 18.80 A C ANISOU 2099 CG PRO A 275 1511 2225 3408 -880 -126 -363 A C ATOM 2100 CD PRO A 275 8.101 131.169 262.503 1.00 19.59 A C ANISOU 2100 CD PRO A 275 1690 2253 3501 -894 -22 -359 A C ATOM 2101 N ASN A 276 7.552 135.753 263.425 1.00 22.77 A N ANISOU 2101 N ASN A 276 1825 2819 4008 -616 -52 -268 A N ATOM 2102 CA ASN A 276 6.569 136.718 263.919 1.00 21.66 A C ANISOU 2102 CA ASN A 276 1585 2731 3915 -567 -51 -259 A C ATOM 2103 C ASN A 276 5.679 137.295 262.812 1.00 25.82 A C ANISOU 2103 C ASN A 276 2033 3312 4465 -565 -149 -244 A C ATOM 2104 O ASN A 276 5.143 138.398 262.952 1.00 28.24 A O ANISOU 2104 O ASN A 276 2267 3648 4815 -497 -166 -229 A O ATOM 2105 CB ASN A 276 7.284 137.875 264.631 1.00 20.74 A C ANISOU 2105 CB ASN A 276 1470 2592 3818 -468 -19 -251 A C ATOM 2106 CG ASN A 276 7.936 137.450 265.930 1.00 22.32 A C ANISOU 2106 CG ASN A 276 1722 2763 3996 -462 81 -268 A C ATOM 2107 ND2 ASN A 276 9.094 138.034 266.234 1.00 16.47 A N ANISOU 2107 ND2 ASN A 276 1027 1985 3246 -402 99 -266 A N ATOM 2108 OD1 ASN A 276 7.408 136.605 266.650 1.00 25.43 A O ANISOU 2108 OD1 ASN A 276 2112 3171 4379 -513 139 -278 A O ATOM 2109 N GLY A 277 5.511 136.553 261.720 1.00 20.91 A N ANISOU 2109 N GLY A 277 1427 2704 3814 -635 -214 -252 A N ATOM 2110 CA GLY A 277 4.808 137.083 260.563 1.00 23.52 A C ANISOU 2110 CA GLY A 277 1688 3097 4153 -631 -316 -234 A C ATOM 2111 C GLY A 277 3.330 137.356 260.772 1.00 28.10 A C ANISOU 2111 C GLY A 277 2157 3746 4773 -638 -326 -232 A C ATOM 2112 O GLY A 277 2.733 138.151 260.042 1.00 30.61 A O ANISOU 2112 O GLY A 277 2402 4118 5110 -601 -400 -208 A O ATOM 2113 N LYS A 278 2.735 136.721 261.777 1.00 27.14 A N ANISOU 2113 N LYS A 278 2018 3629 4665 -683 -253 -252 A N ATOM 2114 CA LYS A 278 1.300 136.848 261.992 1.00 26.26 A C ANISOU 2114 CA LYS A 278 1794 3593 4591 -702 -259 -249 A C ATOM 2115 C LYS A 278 0.953 138.032 262.883 1.00 29.68 A C ANISOU 2115 C LYS A 278 2159 4044 5074 -603 -216 -239 A C ATOM 2116 O LYS A 278 -0.224 138.277 263.152 1.00 37.11 A O ANISOU 2116 O LYS A 278 2997 5052 6050 -602 -214 -237 A O ATOM 2117 CB LYS A 278 0.730 135.580 262.636 1.00 26.67 A C ANISOU 2117 CB LYS A 278 1848 3648 4637 -806 -203 -265 A C ATOM 2118 CG LYS A 278 0.793 134.332 261.776 1.00 28.55 A C ANISOU 2118 CG LYS A 278 2145 3864 4837 -917 -250 -286 A C ATOM 2119 CD LYS A 278 0.091 133.177 262.476 1.00 31.23 A C ANISOU 2119 CD LYS A 278 2477 4201 5189 -1018 -197 -289 A C ATOM 2120 CE LYS A 278 0.207 131.885 261.676 1.00 33.96 A C ANISOU 2120 CE LYS A 278 2898 4500 5504 -1130 -244 -317 A C ATOM 2121 NZ LYS A 278 -0.491 130.756 262.356 1.00 36.59 A N1+ ANISOU 2121 NZ LYS A 278 3225 4816 5860 -1233 -197 -308 A N1+ ATOM 2122 N ASN A 279 1.963 138.775 263.326 1.00 24.92 A N ANISOU 2122 N ASN A 279 1610 3382 4476 -520 -184 -236 A N ATOM 2123 CA ASN A 279 1.747 139.808 264.337 1.00 28.52 A C ANISOU 2123 CA ASN A 279 2021 3839 4978 -429 -134 -243 A C ATOM 2124 C ASN A 279 1.902 141.234 263.816 1.00 26.86 A C ANISOU 2124 C ASN A 279 1785 3610 4809 -329 -193 -221 A C ATOM 2125 O ASN A 279 2.065 142.165 264.601 1.00 25.33 A O ANISOU 2125 O ASN A 279 1584 3387 4653 -248 -156 -234 A O ATOM 2126 CB ASN A 279 2.698 139.603 265.522 1.00 33.63 A C ANISOU 2126 CB ASN A 279 2743 4432 5604 -412 -41 -264 A C ATOM 2127 CG ASN A 279 2.521 138.253 266.190 1.00 39.33 A C ANISOU 2127 CG ASN A 279 3487 5166 6290 -503 28 -275 A C ATOM 2128 ND2 ASN A 279 3.618 137.691 266.687 1.00 41.74 A N ANISOU 2128 ND2 ASN A 279 3889 5415 6556 -515 82 -281 A N ATOM 2129 OD1 ASN A 279 1.410 137.729 266.272 1.00 35.78 A O ANISOU 2129 OD1 ASN A 279 2968 4775 5851 -562 33 -271 A O ATOM 2130 N LEU A 280 1.837 141.406 262.500 1.00 26.39 A N ANISOU 2130 N LEU A 280 1716 3568 4744 -336 -288 -187 A N ATOM 2131 CA LEU A 280 2.165 142.689 261.890 1.00 27.18 A C ANISOU 2131 CA LEU A 280 1810 3637 4879 -247 -349 -148 A C ATOM 2132 C LEU A 280 0.980 143.352 261.184 1.00 30.24 A C ANISOU 2132 C LEU A 280 2093 4090 5306 -216 -422 -121 A C ATOM 2133 O LEU A 280 1.126 144.453 260.641 1.00 31.04 A O ANISOU 2133 O LEU A 280 2184 4165 5445 -140 -476 -78 A O ATOM 2134 CB LEU A 280 3.302 142.505 260.882 1.00 27.91 A C ANISOU 2134 CB LEU A 280 1985 3695 4925 -265 -402 -114 A C ATOM 2135 CG LEU A 280 4.476 141.644 261.353 1.00 28.51 A C ANISOU 2135 CG LEU A 280 2162 3719 4952 -308 -341 -138 A C ATOM 2136 CD1 LEU A 280 5.506 141.449 260.245 1.00 25.35 A C ANISOU 2136 CD1 LEU A 280 1827 3301 4503 -325 -401 -102 A C ATOM 2137 CD2 LEU A 280 5.118 142.233 262.603 1.00 30.67 A C ANISOU 2137 CD2 LEU A 280 2469 3931 5254 -246 -262 -159 A C ATOM 2138 N ASP A 281 -0.184 142.697 261.207 1.00 29.40 A N ANISOU 2138 N ASP A 281 1908 4067 5195 -274 -422 -140 A N ATOM 2139 CA ASP A 281 -1.310 143.072 260.343 1.00 32.94 A C ANISOU 2139 CA ASP A 281 2253 4598 5663 -264 -503 -114 A C ATOM 2140 C ASP A 281 -0.837 143.211 258.895 1.00 35.08 A C ANISOU 2140 C ASP A 281 2556 4876 5897 -266 -605 -67 A C ATOM 2141 O ASP A 281 -1.244 144.132 258.186 1.00 34.16 A O ANISOU 2141 O ASP A 281 2386 4784 5808 -201 -676 -22 A O ATOM 2142 CB ASP A 281 -1.953 144.389 260.801 1.00 35.91 A C ANISOU 2142 CB ASP A 281 2553 4973 6119 -154 -498 -104 A C ATOM 2143 CG ASP A 281 -2.760 144.240 262.076 1.00 42.94 A C ANISOU 2143 CG ASP A 281 3377 5898 7039 -153 -411 -148 A C ATOM 2144 OD1 ASP A 281 -3.142 143.100 262.416 1.00 47.15 A O ANISOU 2144 OD1 ASP A 281 3897 6482 7536 -247 -372 -172 A O ATOM 2145 OD2 ASP A 281 -3.009 145.268 262.741 1.00 46.68 A O1- ANISOU 2145 OD2 ASP A 281 3814 6349 7574 -59 -383 -159 A O1- ATOM 2146 N ALA A 282 0.013 142.286 258.459 1.00 33.31 A N ANISOU 2146 N ALA A 282 2417 4632 5606 -338 -612 -77 A N ATOM 2147 CA ALA A 282 0.599 142.355 257.123 1.00 30.81 A C ANISOU 2147 CA ALA A 282 2138 4328 5240 -340 -704 -34 A C ATOM 2148 C ALA A 282 -0.456 142.245 256.023 1.00 29.42 A C ANISOU 2148 C ALA A 282 1876 4261 5040 -368 -802 -23 A C ATOM 2149 O ALA A 282 -0.289 142.801 254.928 1.00 26.56 A O ANISOU 2149 O ALA A 282 1510 3928 4653 -329 -890 32 A O ATOM 2150 CB ALA A 282 1.659 141.280 256.961 1.00 26.63 A C ANISOU 2150 CB ALA A 282 1713 3763 4643 -415 -687 -61 A C ATOM 2151 N GLY A 283 -1.542 141.536 256.325 1.00 27.56 A N ANISOU 2151 N GLY A 283 1570 4092 4810 -436 -786 -68 A N ATOM 2152 CA GLY A 283 -2.657 141.395 255.404 1.00 30.56 A C ANISOU 2152 CA GLY A 283 1853 4587 5170 -468 -874 -68 A C ATOM 2153 C GLY A 283 -3.270 142.725 254.997 1.00 34.01 A C ANISOU 2153 C GLY A 283 2204 5062 5654 -359 -931 -11 A C ATOM 2154 O GLY A 283 -3.806 142.862 253.895 1.00 38.49 A O ANISOU 2154 O GLY A 283 2716 5716 6191 -356 -1029 11 A O ATOM 2155 N LYS A 284 -3.203 143.712 255.887 1.00 33.19 A N ANISOU 2155 N LYS A 284 2092 4892 5627 -265 -872 10 A N ATOM 2156 CA LYS A 284 -3.754 145.030 255.578 1.00 39.43 A C ANISOU 2156 CA LYS A 284 2810 5696 6475 -155 -921 65 A C ATOM 2157 C LYS A 284 -2.935 145.736 254.503 1.00 36.63 A C ANISOU 2157 C LYS A 284 2514 5308 6095 -100 -1000 141 A C ATOM 2158 O LYS A 284 -3.410 146.676 253.865 1.00 35.02 A O ANISOU 2158 O LYS A 284 2255 5132 5920 -23 -1068 201 A O ATOM 2159 CB LYS A 284 -3.871 145.901 256.837 1.00 39.05 A C ANISOU 2159 CB LYS A 284 2745 5577 6518 -71 -838 56 A C ATOM 2160 CG LYS A 284 -4.860 145.359 257.865 1.00 40.27 A C ANISOU 2160 CG LYS A 284 2818 5787 6696 -110 -766 -4 A C ATOM 2161 CD LYS A 284 -5.056 146.307 259.041 1.00 45.82 A C ANISOU 2161 CD LYS A 284 3494 6435 7482 -14 -693 -18 A C ATOM 2162 CE LYS A 284 -5.989 145.682 260.069 1.00 48.48 A C ANISOU 2162 CE LYS A 284 3751 6841 7828 -59 -616 -69 A C ATOM 2163 NZ LYS A 284 -7.310 145.368 259.465 1.00 50.50 A N1+ ANISOU 2163 NZ LYS A 284 3877 7231 8078 -96 -673 -61 A N1+ ATOM 2164 N ALA A 285 -1.714 145.259 254.283 1.00 36.77 A N ANISOU 2164 N ALA A 285 2642 5272 6056 -140 -990 146 A N ATOM 2165 CA ALA A 285 -0.874 145.805 253.231 1.00 34.91 A C ANISOU 2165 CA ALA A 285 2465 5019 5781 -101 -1061 227 A C ATOM 2166 C ALA A 285 -0.939 144.879 252.031 1.00 34.32 A C ANISOU 2166 C ALA A 285 2394 5048 5600 -177 -1145 218 A C ATOM 2167 O ALA A 285 -0.272 145.103 251.021 1.00 34.30 A O ANISOU 2167 O ALA A 285 2440 5060 5534 -161 -1211 283 A O ATOM 2168 CB ALA A 285 0.549 145.947 253.715 1.00 34.00 A C ANISOU 2168 CB ALA A 285 2462 4789 5667 -89 -1002 242 A C ATOM 2169 N GLY A 286 -1.735 143.821 252.165 1.00 35.73 A N ANISOU 2169 N GLY A 286 2524 5298 5755 -265 -1140 137 A N ATOM 2170 CA GLY A 286 -1.913 142.854 251.097 1.00 33.37 A C ANISOU 2170 CA GLY A 286 2225 5096 5359 -348 -1221 102 A C ATOM 2171 C GLY A 286 -0.852 141.769 251.106 1.00 32.09 A C ANISOU 2171 C GLY A 286 2173 4891 5129 -431 -1192 55 A C ATOM 2172 O GLY A 286 -0.815 140.923 250.214 1.00 35.01 A O ANISOU 2172 O GLY A 286 2565 5326 5411 -501 -1259 16 A O ATOM 2173 N VAL A 287 0.006 141.777 252.121 1.00 31.70 A N ANISOU 2173 N VAL A 287 2195 4731 5118 -422 -1095 51 A N ATOM 2174 CA VAL A 287 1.111 140.825 252.179 1.00 31.62 A C ANISOU 2174 CA VAL A 287 2293 4670 5050 -487 -1064 13 A C ATOM 2175 C VAL A 287 0.628 139.457 252.660 1.00 33.35 A C ANISOU 2175 C VAL A 287 2516 4896 5261 -604 -1023 -86 A C ATOM 2176 O VAL A 287 -0.146 139.358 253.621 1.00 29.29 A O ANISOU 2176 O VAL A 287 1948 4372 4810 -620 -956 -114 A O ATOM 2177 CB VAL A 287 2.268 141.345 253.056 1.00 35.23 A C ANISOU 2177 CB VAL A 287 2825 5011 5549 -431 -980 46 A C ATOM 2178 CG1 VAL A 287 3.311 140.258 253.285 1.00 34.74 A C ANISOU 2178 CG1 VAL A 287 2865 4896 5438 -501 -937 -5 A C ATOM 2179 CG2 VAL A 287 2.911 142.564 252.408 1.00 31.39 A C ANISOU 2179 CG2 VAL A 287 2354 4512 5060 -337 -1028 150 A C ATOM 2180 N GLU A 288 1.042 138.413 251.944 1.00 31.48 A N ANISOU 2180 N GLU A 288 2342 4678 4942 -685 -1067 -136 A N ATOM 2181 CA GLU A 288 0.674 137.043 252.287 1.00 31.13 A C ANISOU 2181 CA GLU A 288 2320 4621 4886 -806 -1034 -229 A C ATOM 2182 C GLU A 288 1.576 136.473 253.373 1.00 27.91 A C ANISOU 2182 C GLU A 288 2009 4092 4504 -828 -924 -253 A C ATOM 2183 O GLU A 288 2.809 136.531 253.277 1.00 29.32 A O ANISOU 2183 O GLU A 288 2275 4213 4653 -796 -915 -238 A O ATOM 2184 CB GLU A 288 0.731 136.150 251.045 1.00 37.75 A C ANISOU 2184 CB GLU A 288 3197 5522 5626 -882 -1132 -289 A C ATOM 2185 CG GLU A 288 -0.322 136.471 249.990 1.00 48.96 A C ANISOU 2185 CG GLU A 288 4516 7072 7014 -875 -1241 -289 A C ATOM 2186 CD GLU A 288 -0.167 135.632 248.729 1.00 57.71 A C ANISOU 2186 CD GLU A 288 5673 8239 8014 -934 -1344 -361 A C ATOM 2187 OE1 GLU A 288 0.859 134.928 248.600 1.00 62.32 A O ANISOU 2187 OE1 GLU A 288 6377 8765 8538 -970 -1335 -398 A O ATOM 2188 OE2 GLU A 288 -1.074 135.674 247.870 1.00 58.34 A O1- ANISOU 2188 OE2 GLU A 288 5676 8418 8072 -938 -1438 -387 A O1- ATOM 2189 N VAL A 289 0.956 135.911 254.402 1.00 26.55 A N ANISOU 2189 N VAL A 289 1818 3888 4382 -882 -843 -284 A N ATOM 2190 CA VAL A 289 1.688 135.255 255.472 1.00 31.28 A C ANISOU 2190 CA VAL A 289 2507 4379 5000 -906 -737 -308 A C ATOM 2191 C VAL A 289 1.250 133.803 255.497 1.00 33.56 A C ANISOU 2191 C VAL A 289 2833 4647 5270 -1034 -729 -372 A C ATOM 2192 O VAL A 289 0.053 133.522 255.495 1.00 34.19 A O ANISOU 2192 O VAL A 289 2835 4786 5370 -1095 -748 -379 A O ATOM 2193 CB VAL A 289 1.354 135.878 256.838 1.00 32.73 A C ANISOU 2193 CB VAL A 289 2643 4536 5256 -850 -638 -275 A C ATOM 2194 CG1 VAL A 289 2.192 135.234 257.938 1.00 27.55 A C ANISOU 2194 CG1 VAL A 289 2083 3779 4607 -865 -530 -294 A C ATOM 2195 CG2 VAL A 289 1.576 137.386 256.806 1.00 31.22 A C ANISOU 2195 CG2 VAL A 289 2407 4357 5096 -725 -653 -215 A C ATOM 2196 N ASP A 290 2.198 132.873 255.488 1.00 33.73 A N ANISOU 2196 N ASP A 290 2976 4583 5256 -1076 -704 -416 A N ATOM 2197 CA ASP A 290 1.805 131.469 255.491 1.00 31.25 A C ANISOU 2197 CA ASP A 290 2714 4226 4933 -1195 -699 -474 A C ATOM 2198 C ASP A 290 1.314 130.992 256.856 1.00 31.19 A C ANISOU 2198 C ASP A 290 2696 4165 4987 -1231 -594 -453 A C ATOM 2199 O ASP A 290 1.359 131.737 257.840 1.00 32.63 A O ANISOU 2199 O ASP A 290 2839 4348 5210 -1160 -519 -406 A O ATOM 2200 CB ASP A 290 2.865 130.548 254.861 1.00 34.01 A C ANISOU 2200 CB ASP A 290 3200 4503 5219 -1227 -721 -543 A C ATOM 2201 CG ASP A 290 4.032 130.229 255.789 1.00 32.21 A C ANISOU 2201 CG ASP A 290 3077 4160 5001 -1192 -612 -545 A C ATOM 2202 OD1 ASP A 290 3.999 130.538 256.999 1.00 33.21 A O ANISOU 2202 OD1 ASP A 290 3182 4257 5181 -1159 -517 -494 A O ATOM 2203 OD2 ASP A 290 4.997 129.620 255.285 1.00 34.25 A O1- ANISOU 2203 OD2 ASP A 290 3445 4365 5203 -1198 -621 -604 A O1- ATOM 2204 N ASP A 291 0.887 129.737 256.906 1.00 31.93 A N ANISOU 2204 N ASP A 291 2833 4212 5088 -1339 -593 -488 A N ATOM 2205 CA ASP A 291 0.221 129.171 258.073 1.00 32.01 A C ANISOU 2205 CA ASP A 291 2818 4188 5155 -1392 -512 -459 A C ATOM 2206 C ASP A 291 1.140 129.050 259.278 1.00 27.85 A C ANISOU 2206 C ASP A 291 2368 3573 4639 -1344 -393 -436 A C ATOM 2207 O ASP A 291 0.680 129.005 260.418 1.00 30.73 A O ANISOU 2207 O ASP A 291 2691 3939 5046 -1349 -313 -395 A O ATOM 2208 CB ASP A 291 -0.326 127.793 257.696 1.00 45.55 A C ANISOU 2208 CB ASP A 291 4575 5855 6878 -1521 -553 -499 A C ATOM 2209 CG ASP A 291 -1.669 127.878 257.015 1.00 61.36 A C ANISOU 2209 CG ASP A 291 6458 7958 8896 -1586 -647 -499 A C ATOM 2210 OD1 ASP A 291 -2.265 128.978 257.040 1.00 66.91 A O ANISOU 2210 OD1 ASP A 291 7040 8772 9610 -1529 -659 -459 A O ATOM 2211 OD2 ASP A 291 -2.100 126.873 256.406 1.00 69.01 A O1- ANISOU 2211 OD2 ASP A 291 7457 8895 9869 -1687 -713 -542 A O1- ATOM 2212 N ARG A 292 2.440 129.020 259.016 1.00 24.71 A N ANISOU 2212 N ARG A 292 2078 3112 4200 -1295 -382 -461 A N ATOM 2213 CA ARG A 292 3.442 128.870 260.059 1.00 28.89 A C ANISOU 2213 CA ARG A 292 2689 3559 4730 -1247 -276 -441 A C ATOM 2214 C ARG A 292 4.002 130.214 260.500 1.00 29.71 A C ANISOU 2214 C ARG A 292 2751 3700 4836 -1130 -242 -404 A C ATOM 2215 O ARG A 292 4.873 130.281 261.366 1.00 35.01 A O ANISOU 2215 O ARG A 292 3479 4319 5504 -1079 -160 -386 A O ATOM 2216 CB ARG A 292 4.550 127.954 259.539 1.00 26.18 A C ANISOU 2216 CB ARG A 292 2490 3117 4340 -1265 -281 -494 A C ATOM 2217 CG ARG A 292 4.053 126.512 259.357 1.00 35.96 A C ANISOU 2217 CG ARG A 292 3787 4286 5589 -1375 -298 -530 A C ATOM 2218 CD ARG A 292 5.034 125.643 258.591 1.00 39.16 A C ANISOU 2218 CD ARG A 292 4333 4601 5943 -1386 -322 -602 A C ATOM 2219 NE ARG A 292 6.292 125.432 259.294 1.00 37.33 A N ANISOU 2219 NE ARG A 292 4206 4283 5693 -1325 -230 -589 A N ATOM 2220 CZ ARG A 292 7.483 125.541 258.715 1.00 35.13 A C ANISOU 2220 CZ ARG A 292 4013 3978 5356 -1268 -235 -634 A C ATOM 2221 NH1 ARG A 292 7.564 125.848 257.427 1.00 28.34 A N1+ ANISOU 2221 NH1 ARG A 292 3145 3178 4443 -1265 -329 -697 A N1+ ATOM 2222 NH2 ARG A 292 8.590 125.338 259.417 1.00 41.32 A N ANISOU 2222 NH2 ARG A 292 4886 4687 6125 -1213 -148 -615 A N ATOM 2223 N GLY A 293 3.505 131.288 259.902 1.00 28.28 A N ANISOU 2223 N GLY A 293 2474 3608 4663 -1085 -309 -390 A N ATOM 2224 CA GLY A 293 3.878 132.617 260.345 1.00 25.44 A C ANISOU 2224 CA GLY A 293 2069 3277 4322 -973 -284 -351 A C ATOM 2225 C GLY A 293 5.043 133.159 259.550 1.00 28.00 A C ANISOU 2225 C GLY A 293 2445 3583 4611 -912 -329 -353 A C ATOM 2226 O GLY A 293 5.606 134.199 259.894 1.00 24.95 A O ANISOU 2226 O GLY A 293 2044 3197 4240 -821 -308 -317 A O ATOM 2227 N PHE A 294 5.438 132.447 258.500 1.00 26.44 A N ANISOU 2227 N PHE A 294 2311 3369 4367 -963 -391 -396 A N ATOM 2228 CA PHE A 294 6.499 132.956 257.641 1.00 27.60 A C ANISOU 2228 CA PHE A 294 2508 3520 4458 -900 -441 -388 A C ATOM 2229 C PHE A 294 5.948 133.920 256.605 1.00 30.14 A C ANISOU 2229 C PHE A 294 2736 3938 4777 -868 -551 -357 A C ATOM 2230 O PHE A 294 4.820 133.764 256.127 1.00 30.39 A O ANISOU 2230 O PHE A 294 2691 4034 4823 -922 -613 -373 A O ATOM 2231 CB PHE A 294 7.242 131.816 256.945 1.00 27.94 A C ANISOU 2231 CB PHE A 294 2692 3521 4405 -937 -451 -441 A C ATOM 2232 CG PHE A 294 8.103 131.009 257.865 1.00 25.45 A C ANISOU 2232 CG PHE A 294 2488 3104 4077 -936 -346 -453 A C ATOM 2233 CD1 PHE A 294 7.717 129.734 258.255 1.00 20.75 A C ANISOU 2233 CD1 PHE A 294 1932 2440 3512 -1031 -311 -503 A C ATOM 2234 CD2 PHE A 294 9.297 131.525 258.347 1.00 20.16 A C ANISOU 2234 CD2 PHE A 294 1881 2407 3371 -843 -285 -408 A C ATOM 2235 CE1 PHE A 294 8.505 128.985 259.104 1.00 20.84 A C ANISOU 2235 CE1 PHE A 294 2047 2357 3515 -1024 -217 -502 A C ATOM 2236 CE2 PHE A 294 10.096 130.780 259.205 1.00 21.31 A C ANISOU 2236 CE2 PHE A 294 2125 2469 3504 -836 -193 -414 A C ATOM 2237 CZ PHE A 294 9.695 129.510 259.585 1.00 26.70 A C ANISOU 2237 CZ PHE A 294 2848 3082 4212 -922 -158 -457 A C ATOM 2238 N ILE A 295 6.759 134.909 256.251 1.00 26.49 A N ANISOU 2238 N ILE A 295 2297 3492 4276 -773 -566 -297 A N ATOM 2239 CA ILE A 295 6.447 135.778 255.129 1.00 26.22 A C ANISOU 2239 CA ILE A 295 2199 3545 4218 -735 -673 -251 A C ATOM 2240 C ILE A 295 7.416 135.425 254.011 1.00 30.10 A C ANISOU 2240 C ILE A 295 2805 4059 4573 -722 -711 -253 A C ATOM 2241 O ILE A 295 8.585 135.805 254.051 1.00 29.24 A O ANISOU 2241 O ILE A 295 2773 3922 4415 -656 -670 -211 A O ATOM 2242 CB ILE A 295 6.576 137.259 255.508 1.00 25.68 A C ANISOU 2242 CB ILE A 295 2061 3477 4217 -637 -667 -169 A C ATOM 2243 CG1 ILE A 295 5.585 137.594 256.626 1.00 29.98 A C ANISOU 2243 CG1 ILE A 295 2515 4013 4863 -631 -611 -177 A C ATOM 2244 CG2 ILE A 295 6.321 138.135 254.294 1.00 26.28 A C ANISOU 2244 CG2 ILE A 295 2080 3637 4267 -594 -780 -103 A C ATOM 2245 CD1 ILE A 295 5.616 139.040 257.083 1.00 30.80 A C ANISOU 2245 CD1 ILE A 295 2573 4107 5024 -525 -593 -115 A C ATOM 2246 N ARG A 296 6.932 134.653 253.043 1.00 30.23 A N ANISOU 2246 N ARG A 296 2832 4130 4526 -789 -787 -309 A N ATOM 2247 CA ARG A 296 7.777 134.107 251.988 1.00 31.49 A C ANISOU 2247 CA ARG A 296 3104 4318 4544 -784 -818 -336 A C ATOM 2248 C ARG A 296 8.118 135.161 250.936 1.00 31.02 A C ANISOU 2248 C ARG A 296 3022 4354 4410 -710 -891 -250 A C ATOM 2249 O ARG A 296 7.287 136.010 250.603 1.00 32.86 A O ANISOU 2249 O ARG A 296 3140 4656 4689 -695 -966 -194 A O ATOM 2250 CB ARG A 296 7.073 132.915 251.339 1.00 29.61 A C ANISOU 2250 CB ARG A 296 2881 4105 4266 -885 -878 -440 A C ATOM 2251 CG ARG A 296 6.698 131.824 252.338 1.00 32.91 A C ANISOU 2251 CG ARG A 296 3321 4419 4764 -970 -808 -515 A C ATOM 2252 CD ARG A 296 7.933 131.278 253.041 1.00 36.65 A C ANISOU 2252 CD ARG A 296 3929 4785 5212 -936 -697 -525 A C ATOM 2253 NE ARG A 296 7.613 130.140 253.898 1.00 40.63 A N ANISOU 2253 NE ARG A 296 4466 5188 5783 -1020 -634 -587 A N ATOM 2254 CZ ARG A 296 8.519 129.391 254.516 1.00 36.84 A C ANISOU 2254 CZ ARG A 296 4103 4605 5287 -1008 -545 -607 A C ATOM 2255 NH1 ARG A 296 9.814 129.633 254.350 1.00 28.21 A N1+ ANISOU 2255 NH1 ARG A 296 3102 3506 4112 -917 -509 -579 A N1+ ATOM 2256 NH2 ARG A 296 8.133 128.378 255.284 1.00 39.62 A N ANISOU 2256 NH2 ARG A 296 4479 4865 5708 -1088 -493 -650 A N ATOM 2257 N VAL A 297 9.337 135.091 250.407 1.00 23.52 A N ANISOU 2257 N VAL A 297 2178 3413 3346 -663 -869 -234 A N ATOM 2258 CA VAL A 297 9.831 136.091 249.467 1.00 24.60 A C ANISOU 2258 CA VAL A 297 2303 3638 3407 -592 -922 -135 A C ATOM 2259 C VAL A 297 10.571 135.415 248.322 1.00 32.44 A C ANISOU 2259 C VAL A 297 3396 4702 4229 -591 -948 -174 A C ATOM 2260 O VAL A 297 10.911 134.232 248.411 1.00 35.49 A O ANISOU 2260 O VAL A 297 3874 5041 4567 -629 -907 -278 A O ATOM 2261 CB VAL A 297 10.795 137.072 250.146 1.00 27.05 A C ANISOU 2261 CB VAL A 297 2624 3890 3765 -513 -850 -40 A C ATOM 2262 CG1 VAL A 297 10.065 137.906 251.187 1.00 25.33 A C ANISOU 2262 CG1 VAL A 297 2301 3614 3709 -500 -833 -2 A C ATOM 2263 CG2 VAL A 297 11.949 136.312 250.781 1.00 27.26 A C ANISOU 2263 CG2 VAL A 297 2767 3834 3755 -506 -745 -89 A C ATOM 2264 N ASP A 298 10.820 136.166 247.251 1.00 31.19 A N ANISOU 2264 N ASP A 298 3219 4655 3977 -543 -1013 -89 A N ATOM 2265 CA ASP A 298 11.593 135.652 246.126 1.00 30.49 A C ANISOU 2265 CA ASP A 298 3220 4656 3710 -528 -1031 -117 A C ATOM 2266 C ASP A 298 13.079 135.950 246.305 1.00 29.40 A C ANISOU 2266 C ASP A 298 3159 4490 3524 -458 -941 -56 A C ATOM 2267 O ASP A 298 13.511 136.339 247.397 1.00 26.33 A O ANISOU 2267 O ASP A 298 2767 3996 3242 -435 -862 -18 A O ATOM 2268 CB ASP A 298 11.072 136.206 244.789 1.00 33.49 A C ANISOU 2268 CB ASP A 298 3539 5196 3990 -517 -1151 -57 A C ATOM 2269 CG ASP A 298 11.201 137.730 244.671 1.00 36.13 A C ANISOU 2269 CG ASP A 298 3796 5564 4368 -449 -1173 118 A C ATOM 2270 OD1 ASP A 298 11.951 138.368 245.446 1.00 33.61 A O ANISOU 2270 OD1 ASP A 298 3488 5156 4127 -404 -1093 191 A O ATOM 2271 OD2 ASP A 298 10.543 138.298 243.773 1.00 40.15 A O1- ANISOU 2271 OD2 ASP A 298 4232 6189 4833 -440 -1276 186 A O1- ATOM 2272 N LYS A 299 13.848 135.798 245.229 1.00 29.49 A N ANISOU 2272 N LYS A 299 3230 4605 3370 -425 -954 -46 A N ATOM 2273 CA LYS A 299 15.300 135.967 245.292 1.00 35.09 A C ANISOU 2273 CA LYS A 299 4009 5307 4018 -363 -868 6 A C ATOM 2274 C LYS A 299 15.739 137.431 245.373 1.00 34.27 A C ANISOU 2274 C LYS A 299 3841 5216 3964 -310 -862 177 A C ATOM 2275 O LYS A 299 16.925 137.727 245.544 1.00 34.81 A O ANISOU 2275 O LYS A 299 3947 5271 4007 -265 -790 236 A O ATOM 2276 CB LYS A 299 15.979 135.227 244.135 1.00 37.76 A C ANISOU 2276 CB LYS A 299 4431 5759 4158 -344 -875 -53 A C ATOM 2277 CG LYS A 299 15.933 133.709 244.320 1.00 42.40 A C ANISOU 2277 CG LYS A 299 5110 6282 4719 -383 -847 -231 A C ATOM 2278 CD LYS A 299 16.362 132.951 243.080 1.00 49.84 A C ANISOU 2278 CD LYS A 299 6128 7344 5465 -366 -873 -315 A C ATOM 2279 CE LYS A 299 16.042 131.469 243.228 1.00 58.05 A C ANISOU 2279 CE LYS A 299 7249 8302 6504 -418 -868 -502 A C ATOM 2280 NZ LYS A 299 17.287 130.652 243.188 1.00 61.34 A N1+ ANISOU 2280 NZ LYS A 299 7781 8693 6833 -361 -780 -574 A N1+ ATOM 2281 N GLN A 300 14.776 138.342 245.273 1.00 32.03 A N ANISOU 2281 N GLN A 300 3457 4953 3762 -317 -938 257 A N ATOM 2282 CA GLN A 300 15.058 139.756 245.496 1.00 32.82 A C ANISOU 2282 CA GLN A 300 3493 5030 3947 -271 -936 414 A C ATOM 2283 C GLN A 300 14.431 140.211 246.806 1.00 32.18 A C ANISOU 2283 C GLN A 300 3349 4812 4064 -280 -912 407 A C ATOM 2284 O GLN A 300 14.335 141.412 247.078 1.00 30.77 A O ANISOU 2284 O GLN A 300 3103 4597 3991 -247 -927 518 A O ATOM 2285 CB GLN A 300 14.555 140.607 244.335 1.00 33.04 A C ANISOU 2285 CB GLN A 300 3452 5185 3917 -252 -1040 533 A C ATOM 2286 CG GLN A 300 15.352 140.401 243.065 1.00 34.83 A C ANISOU 2286 CG GLN A 300 3734 5560 3940 -229 -1052 571 A C ATOM 2287 CD GLN A 300 15.052 141.450 242.027 1.00 36.96 A C ANISOU 2287 CD GLN A 300 3935 5950 4159 -201 -1141 731 A C ATOM 2288 NE2 GLN A 300 16.100 142.089 241.519 1.00 32.76 A N ANISOU 2288 NE2 GLN A 300 3421 5475 3553 -161 -1109 862 A N ATOM 2289 OE1 GLN A 300 13.892 141.698 241.690 1.00 40.46 A O ANISOU 2289 OE1 GLN A 300 4305 6437 4632 -214 -1239 745 A O ATOM 2290 N LEU A 301 14.012 139.228 247.604 1.00 28.51 A N ANISOU 2290 N LEU A 301 2911 4274 3648 -325 -874 275 A N ATOM 2291 CA LEU A 301 13.435 139.445 248.931 1.00 27.73 A C ANISOU 2291 CA LEU A 301 2761 4057 3718 -338 -836 248 A C ATOM 2292 C LEU A 301 12.090 140.178 248.899 1.00 25.90 A C ANISOU 2292 C LEU A 301 2409 3843 3591 -343 -918 286 A C ATOM 2293 O LEU A 301 11.659 140.730 249.909 1.00 23.51 A O ANISOU 2293 O LEU A 301 2045 3456 3432 -332 -892 294 A O ATOM 2294 CB LEU A 301 14.427 140.165 249.866 1.00 27.84 A C ANISOU 2294 CB LEU A 301 2791 3979 3809 -292 -753 307 A C ATOM 2295 CG LEU A 301 15.738 139.456 250.246 1.00 27.45 A C ANISOU 2295 CG LEU A 301 2845 3893 3690 -282 -659 264 A C ATOM 2296 CD1 LEU A 301 15.509 137.987 250.595 1.00 21.36 A C ANISOU 2296 CD1 LEU A 301 2139 3090 2885 -329 -623 126 A C ATOM 2297 CD2 LEU A 301 16.809 139.596 249.170 1.00 30.95 A C ANISOU 2297 CD2 LEU A 301 3337 4428 3993 -248 -662 332 A C ATOM 2298 N ARG A 302 11.422 140.158 247.749 1.00 28.16 A N ANISOU 2298 N ARG A 302 2657 4244 3798 -357 -1018 304 A N ATOM 2299 CA ARG A 302 10.097 140.760 247.621 1.00 31.75 A C ANISOU 2299 CA ARG A 302 2990 4732 4342 -360 -1106 338 A C ATOM 2300 C ARG A 302 9.000 139.826 248.115 1.00 32.53 A C ANISOU 2300 C ARG A 302 3052 4813 4495 -431 -1114 212 A C ATOM 2301 O ARG A 302 9.025 138.632 247.828 1.00 29.53 A O ANISOU 2301 O ARG A 302 2737 4457 4026 -490 -1111 106 A O ATOM 2302 CB ARG A 302 9.789 141.107 246.163 1.00 30.45 A C ANISOU 2302 CB ARG A 302 2792 4714 4064 -346 -1219 415 A C ATOM 2303 CG ARG A 302 10.700 142.135 245.505 1.00 34.84 A C ANISOU 2303 CG ARG A 302 3364 5309 4565 -280 -1228 569 A C ATOM 2304 CD ARG A 302 10.209 142.429 244.081 1.00 36.96 A C ANISOU 2304 CD ARG A 302 3588 5738 4717 -269 -1348 647 A C ATOM 2305 NE ARG A 302 11.223 143.090 243.265 1.00 39.55 A N ANISOU 2305 NE ARG A 302 3955 6132 4941 -222 -1347 784 A N ATOM 2306 CZ ARG A 302 11.362 144.409 243.168 1.00 42.49 A C ANISOU 2306 CZ ARG A 302 4280 6476 5390 -165 -1363 944 A C ATOM 2307 NH1 ARG A 302 10.546 145.215 243.837 1.00 42.93 A N1+ ANISOU 2307 NH1 ARG A 302 4268 6423 5622 -137 -1362 962 A N1+ ATOM 2308 NH2 ARG A 302 12.312 144.921 242.398 1.00 40.19 A N ANISOU 2308 NH2 ARG A 302 4036 6239 4998 -132 -1344 1061 A N ATOM 2309 N THR A 303 8.030 140.372 248.843 1.00 32.44 A N ANISOU 2309 N THR A 303 2933 4761 4633 -427 -1125 223 A N ATOM 2310 CA THR A 303 6.817 139.619 249.144 1.00 34.38 A C ANISOU 2310 CA THR A 303 3113 5018 4931 -498 -1150 125 A C ATOM 2311 C THR A 303 5.962 139.577 247.882 1.00 32.76 A C ANISOU 2311 C THR A 303 2843 4952 4652 -521 -1282 137 A C ATOM 2312 O THR A 303 6.399 140.001 246.810 1.00 32.64 A O ANISOU 2312 O THR A 303 2851 5022 4528 -483 -1342 213 A O ATOM 2313 CB THR A 303 5.979 140.283 250.254 1.00 30.88 A C ANISOU 2313 CB THR A 303 2556 4510 4665 -478 -1123 137 A C ATOM 2314 CG2 THR A 303 6.817 140.508 251.500 1.00 22.43 A C ANISOU 2314 CG2 THR A 303 1541 3317 3665 -444 -1002 133 A C ATOM 2315 OG1 THR A 303 5.460 141.534 249.783 1.00 28.70 A O ANISOU 2315 OG1 THR A 303 2205 4275 4424 -399 -1177 234 A O ATOM 2316 N ASN A 304 4.733 139.088 248.016 1.00 30.69 A N ANISOU 2316 N ASN A 304 2495 4720 4447 -584 -1324 65 A N ATOM 2317 CA ASN A 304 3.782 139.077 246.910 1.00 33.93 A C ANISOU 2317 CA ASN A 304 2848 5254 4789 -591 -1426 56 A C ATOM 2318 C ASN A 304 3.378 140.488 246.493 1.00 39.43 A C ANISOU 2318 C ASN A 304 3473 5989 5519 -486 -1464 178 A C ATOM 2319 O ASN A 304 2.893 140.706 245.380 1.00 38.18 A O ANISOU 2319 O ASN A 304 3285 5940 5282 -467 -1557 207 A O ATOM 2320 CB ASN A 304 2.555 138.246 247.277 1.00 33.69 A C ANISOU 2320 CB ASN A 304 2755 5228 4818 -670 -1425 -61 A C ATOM 2321 CG ASN A 304 1.827 138.799 248.479 1.00 31.51 A C ANISOU 2321 CG ASN A 304 2395 4884 4691 -640 -1344 -52 A C ATOM 2322 ND2 ASN A 304 0.599 139.257 248.272 1.00 31.10 A N ANISOU 2322 ND2 ASN A 304 2234 4902 4681 -618 -1386 -45 A N ATOM 2323 OD1 ASN A 304 2.362 138.803 249.589 1.00 31.63 A O ANISOU 2323 OD1 ASN A 304 2447 4794 4777 -635 -1244 -54 A O ATOM 2324 N VAL A 305 3.560 141.435 247.411 1.00 40.76 A N ANISOU 2324 N VAL A 305 3620 6059 5806 -418 -1391 241 A N ATOM 2325 CA VAL A 305 3.421 142.854 247.109 1.00 36.83 A C ANISOU 2325 CA VAL A 305 3081 5562 5350 -315 -1414 364 A C ATOM 2326 C VAL A 305 4.813 143.408 246.804 1.00 36.40 A C ANISOU 2326 C VAL A 305 3112 5476 5243 -271 -1398 467 A C ATOM 2327 O VAL A 305 5.644 143.544 247.701 1.00 38.17 A O ANISOU 2327 O VAL A 305 3380 5595 5528 -261 -1316 472 A O ATOM 2328 CB VAL A 305 2.806 143.623 248.293 1.00 35.09 A C ANISOU 2328 CB VAL A 305 2796 5248 5287 -265 -1343 364 A C ATOM 2329 CG1 VAL A 305 2.609 145.074 247.926 1.00 36.67 A C ANISOU 2329 CG1 VAL A 305 2960 5438 5535 -163 -1376 483 A C ATOM 2330 CG2 VAL A 305 1.482 142.994 248.718 1.00 31.48 A C ANISOU 2330 CG2 VAL A 305 2254 4831 4877 -317 -1341 262 A C ATOM 2331 N PRO A 306 5.066 143.738 245.528 1.00 38.63 A N ANISOU 2331 N PRO A 306 3415 5856 5408 -243 -1474 553 A N ATOM 2332 CA PRO A 306 6.408 143.996 244.981 1.00 38.64 A C ANISOU 2332 CA PRO A 306 3502 5870 5311 -220 -1464 646 A C ATOM 2333 C PRO A 306 7.211 145.093 245.683 1.00 37.01 A C ANISOU 2333 C PRO A 306 3316 5537 5210 -157 -1391 742 A C ATOM 2334 O PRO A 306 8.440 144.987 245.730 1.00 31.76 A O ANISOU 2334 O PRO A 306 2723 4852 4494 -162 -1348 776 A O ATOM 2335 CB PRO A 306 6.123 144.399 243.527 1.00 41.59 A C ANISOU 2335 CB PRO A 306 3866 6373 5562 -188 -1556 728 A C ATOM 2336 CG PRO A 306 4.786 143.788 243.224 1.00 44.54 A C ANISOU 2336 CG PRO A 306 4169 6826 5928 -226 -1626 631 A C ATOM 2337 CD PRO A 306 4.018 143.903 244.506 1.00 42.26 A C ANISOU 2337 CD PRO A 306 3812 6431 5815 -229 -1572 568 A C ATOM 2338 N HIS A 307 6.551 146.113 246.224 1.00 36.29 A N ANISOU 2338 N HIS A 307 3165 5364 5259 -101 -1376 777 A N ATOM 2339 CA HIS A 307 7.281 147.188 246.898 1.00 32.27 A C ANISOU 2339 CA HIS A 307 2681 4725 4857 -47 -1310 854 A C ATOM 2340 C HIS A 307 7.492 146.902 248.386 1.00 32.81 A C ANISOU 2340 C HIS A 307 2757 4674 5035 -63 -1218 757 A C ATOM 2341 O HIS A 307 8.118 147.691 249.100 1.00 30.50 A O ANISOU 2341 O HIS A 307 2489 4266 4833 -26 -1159 793 A O ATOM 2342 CB HIS A 307 6.598 148.546 246.698 1.00 35.88 A C ANISOU 2342 CB HIS A 307 3085 5143 5405 28 -1341 945 A C ATOM 2343 CG HIS A 307 5.268 148.665 247.369 1.00 39.22 A C ANISOU 2343 CG HIS A 307 3423 5543 5937 46 -1342 869 A C ATOM 2344 CD2 HIS A 307 4.895 149.306 248.504 1.00 38.28 A C ANISOU 2344 CD2 HIS A 307 3272 5310 5965 85 -1285 835 A C ATOM 2345 ND1 HIS A 307 4.124 148.068 246.876 1.00 43.34 A N ANISOU 2345 ND1 HIS A 307 3878 6177 6413 23 -1407 813 A N ATOM 2346 CE1 HIS A 307 3.106 148.354 247.667 1.00 40.54 A C ANISOU 2346 CE1 HIS A 307 3449 5783 6173 48 -1385 757 A C ATOM 2347 NE2 HIS A 307 3.547 149.095 248.667 1.00 38.19 A N ANISOU 2347 NE2 HIS A 307 3173 5349 5988 88 -1311 768 A N ATOM 2348 N ILE A 308 6.980 145.765 248.847 1.00 28.08 A N ANISOU 2348 N ILE A 308 2140 4102 4425 -124 -1204 633 A N ATOM 2349 CA ILE A 308 7.209 145.345 250.223 1.00 26.61 A C ANISOU 2349 CA ILE A 308 1969 3818 4322 -147 -1110 540 A C ATOM 2350 C ILE A 308 8.117 144.116 250.292 1.00 28.56 A C ANISOU 2350 C ILE A 308 2286 4082 4485 -217 -1085 481 A C ATOM 2351 O ILE A 308 7.822 143.077 249.703 1.00 33.50 A O ANISOU 2351 O ILE A 308 2918 4794 5018 -282 -1131 424 A O ATOM 2352 CB ILE A 308 5.881 145.094 250.975 1.00 27.02 A C ANISOU 2352 CB ILE A 308 1947 3864 4454 -160 -1088 445 A C ATOM 2353 CG1 ILE A 308 5.066 146.393 251.047 1.00 26.32 A C ANISOU 2353 CG1 ILE A 308 1793 3749 4461 -79 -1106 502 A C ATOM 2354 CG2 ILE A 308 6.153 144.548 252.378 1.00 25.71 A C ANISOU 2354 CG2 ILE A 308 1807 3612 4349 -189 -984 351 A C ATOM 2355 CD1 ILE A 308 3.746 146.271 251.799 1.00 26.85 A C ANISOU 2355 CD1 ILE A 308 1777 3824 4603 -81 -1082 420 A C ATOM 2356 N PHE A 309 9.226 144.258 251.016 1.00 28.98 A N ANISOU 2356 N PHE A 309 2396 4048 4567 -204 -1009 489 A N ATOM 2357 CA PHE A 309 10.258 143.233 251.120 1.00 23.28 A C ANISOU 2357 CA PHE A 309 1795 3319 3731 -244 -936 424 A C ATOM 2358 C PHE A 309 10.222 142.585 252.502 1.00 27.57 A C ANISOU 2358 C PHE A 309 2359 3776 4342 -272 -839 315 A C ATOM 2359 O PHE A 309 9.608 143.122 253.427 1.00 26.53 A O ANISOU 2359 O PHE A 309 2152 3585 4341 -250 -819 300 A O ATOM 2360 CB PHE A 309 11.639 143.850 250.889 1.00 25.70 A C ANISOU 2360 CB PHE A 309 2169 3600 3995 -202 -904 514 A C ATOM 2361 CG PHE A 309 11.850 144.390 249.498 1.00 27.75 A C ANISOU 2361 CG PHE A 309 2423 3956 4164 -179 -985 634 A C ATOM 2362 CD1 PHE A 309 12.708 143.751 248.617 1.00 29.24 A C ANISOU 2362 CD1 PHE A 309 2697 4228 4184 -196 -978 640 A C ATOM 2363 CD2 PHE A 309 11.207 145.548 249.080 1.00 28.79 A C ANISOU 2363 CD2 PHE A 309 2464 4098 4377 -135 -1066 745 A C ATOM 2364 CE1 PHE A 309 12.912 144.246 247.341 1.00 31.18 A C ANISOU 2364 CE1 PHE A 309 2937 4579 4332 -174 -1048 756 A C ATOM 2365 CE2 PHE A 309 11.397 146.045 247.803 1.00 30.31 A C ANISOU 2365 CE2 PHE A 309 2654 4385 4477 -113 -1137 868 A C ATOM 2366 CZ PHE A 309 12.257 145.397 246.934 1.00 31.61 A C ANISOU 2366 CZ PHE A 309 2900 4646 4464 -135 -1130 878 A C ATOM 2367 N ALA A 310 10.880 141.437 252.646 1.00 21.73 A N ANISOU 2367 N ALA A 310 1718 3029 3509 -315 -779 239 A N ATOM 2368 CA ALA A 310 10.987 140.780 253.945 1.00 18.46 A C ANISOU 2368 CA ALA A 310 1335 2535 3144 -339 -683 152 A C ATOM 2369 C ALA A 310 12.305 140.028 254.016 1.00 20.56 A C ANISOU 2369 C ALA A 310 1726 2777 3308 -344 -614 126 A C ATOM 2370 O ALA A 310 12.746 139.450 253.019 1.00 24.78 A O ANISOU 2370 O ALA A 310 2323 3371 3720 -358 -641 124 A O ATOM 2371 CB ALA A 310 9.799 139.833 254.172 1.00 18.97 A C ANISOU 2371 CB ALA A 310 1359 2619 3232 -409 -693 62 A C ATOM 2372 N ILE A 311 12.938 140.034 255.187 1.00 19.15 A N ANISOU 2372 N ILE A 311 1580 2519 3175 -327 -526 104 A N ATOM 2373 CA ILE A 311 14.282 139.481 255.336 1.00 16.89 A C ANISOU 2373 CA ILE A 311 1403 2210 2806 -316 -460 93 A C ATOM 2374 C ILE A 311 14.485 138.832 256.708 1.00 17.59 A C ANISOU 2374 C ILE A 311 1527 2225 2932 -329 -367 25 A C ATOM 2375 O ILE A 311 13.740 139.105 257.648 1.00 17.64 A O ANISOU 2375 O ILE A 311 1469 2197 3038 -334 -345 1 A O ATOM 2376 CB ILE A 311 15.336 140.590 255.181 1.00 16.25 A C ANISOU 2376 CB ILE A 311 1326 2122 2728 -258 -457 185 A C ATOM 2377 CG1 ILE A 311 15.019 141.743 256.141 1.00 15.49 A C ANISOU 2377 CG1 ILE A 311 1151 1960 2773 -225 -448 210 A C ATOM 2378 CG2 ILE A 311 15.374 141.103 253.755 1.00 16.47 A C ANISOU 2378 CG2 ILE A 311 1337 2232 2689 -245 -538 269 A C ATOM 2379 CD1 ILE A 311 16.094 142.830 256.168 1.00 24.11 A C ANISOU 2379 CD1 ILE A 311 2249 3021 3890 -178 -440 292 A C ATOM 2380 N GLY A 312 15.494 137.975 256.823 1.00 14.82 A N ANISOU 2380 N GLY A 312 1275 1857 2499 -328 -310 -3 A N ATOM 2381 CA GLY A 312 15.838 137.379 258.104 1.00 16.91 A C ANISOU 2381 CA GLY A 312 1581 2057 2788 -331 -223 -50 A C ATOM 2382 C GLY A 312 14.992 136.186 258.516 1.00 21.98 A C ANISOU 2382 C GLY A 312 2237 2674 3441 -394 -200 -124 A C ATOM 2383 O GLY A 312 14.381 135.512 257.669 1.00 21.57 A O ANISOU 2383 O GLY A 312 2193 2650 3351 -442 -248 -158 A O ATOM 2384 N ASP A 313 14.943 135.946 259.829 1.00 23.48 A N ANISOU 2384 N ASP A 313 2426 2813 3681 -398 -127 -148 A N ATOM 2385 CA ASP A 313 14.231 134.803 260.406 1.00 22.61 A C ANISOU 2385 CA ASP A 313 2332 2670 3590 -461 -89 -204 A C ATOM 2386 C ASP A 313 12.795 134.687 259.912 1.00 23.87 A C ANISOU 2386 C ASP A 313 2411 2861 3797 -525 -149 -228 A C ATOM 2387 O ASP A 313 12.295 133.588 259.671 1.00 27.39 A O ANISOU 2387 O ASP A 313 2887 3292 4229 -594 -154 -275 A O ATOM 2388 CB ASP A 313 14.189 134.922 261.936 1.00 20.12 A C ANISOU 2388 CB ASP A 313 1993 2320 3333 -450 -9 -207 A C ATOM 2389 CG ASP A 313 15.504 134.558 262.599 1.00 26.38 A C ANISOU 2389 CG ASP A 313 2877 3078 4071 -406 60 -198 A C ATOM 2390 OD1 ASP A 313 16.521 134.414 261.887 1.00 26.28 A O ANISOU 2390 OD1 ASP A 313 2932 3068 3984 -374 46 -184 A O ATOM 2391 OD2 ASP A 313 15.510 134.418 263.846 1.00 25.90 A O1- ANISOU 2391 OD2 ASP A 313 2811 2994 4034 -402 127 -204 A O1- ATOM 2392 N ILE A 314 12.151 135.834 259.727 1.00 19.23 A N ANISOU 2392 N ILE A 314 1720 2315 3271 -502 -199 -196 A N ATOM 2393 CA ILE A 314 10.729 135.877 259.431 1.00 22.19 A C ANISOU 2393 CA ILE A 314 1994 2730 3707 -553 -254 -213 A C ATOM 2394 C ILE A 314 10.444 135.342 258.031 1.00 21.52 A C ANISOU 2394 C ILE A 314 1930 2691 3556 -597 -339 -230 A C ATOM 2395 O ILE A 314 9.303 135.037 257.688 1.00 24.26 A O ANISOU 2395 O ILE A 314 2209 3073 3937 -658 -389 -259 A O ATOM 2396 CB ILE A 314 10.196 137.318 259.573 1.00 22.32 A C ANISOU 2396 CB ILE A 314 1894 2775 3809 -498 -288 -170 A C ATOM 2397 CG1 ILE A 314 8.706 137.323 259.921 1.00 22.46 A C ANISOU 2397 CG1 ILE A 314 1792 2825 3917 -541 -302 -196 A C ATOM 2398 CG2 ILE A 314 10.465 138.123 258.311 1.00 23.54 A C ANISOU 2398 CG2 ILE A 314 2040 2974 3930 -458 -377 -113 A C ATOM 2399 CD1 ILE A 314 8.227 138.676 260.474 1.00 22.83 A C ANISOU 2399 CD1 ILE A 314 1749 2883 4043 -465 -300 -165 A C ATOM 2400 N VAL A 315 11.501 135.188 257.243 1.00 19.87 A N ANISOU 2400 N VAL A 315 1813 2489 3248 -566 -353 -218 A N ATOM 2401 CA VAL A 315 11.362 134.794 255.848 1.00 17.68 A C ANISOU 2401 CA VAL A 315 1560 2271 2887 -593 -436 -236 A C ATOM 2402 C VAL A 315 11.516 133.280 255.640 1.00 27.08 A C ANISOU 2402 C VAL A 315 2850 3424 4016 -654 -417 -318 A C ATOM 2403 O VAL A 315 11.023 132.705 254.661 1.00 21.40 A O ANISOU 2403 O VAL A 315 2138 2746 3247 -704 -486 -366 A O ATOM 2404 CB VAL A 315 12.383 135.622 255.022 1.00 26.17 A C ANISOU 2404 CB VAL A 315 2666 3393 3886 -519 -465 -167 A C ATOM 2405 CG1 VAL A 315 13.242 134.766 254.118 1.00 22.34 A C ANISOU 2405 CG1 VAL A 315 2291 2929 3268 -519 -469 -201 A C ATOM 2406 CG2 VAL A 315 11.674 136.752 254.293 1.00 21.58 A C ANISOU 2406 CG2 VAL A 315 1981 2885 3334 -498 -555 -102 A C ATOM 2407 N GLY A 316 12.173 132.620 256.582 1.00 25.18 A N ANISOU 2407 N GLY A 316 2684 3101 3780 -650 -326 -338 A N ATOM 2408 CA GLY A 316 12.332 131.187 256.483 1.00 17.88 A C ANISOU 2408 CA GLY A 316 1858 2119 2816 -702 -303 -411 A C ATOM 2409 C GLY A 316 13.624 130.738 257.116 1.00 22.47 A C ANISOU 2409 C GLY A 316 2546 2634 3359 -649 -215 -405 A C ATOM 2410 O GLY A 316 14.418 131.562 257.570 1.00 24.04 A O ANISOU 2410 O GLY A 316 2738 2842 3554 -576 -178 -345 A O ATOM 2411 N GLN A 317 13.834 129.429 257.143 1.00 21.74 A N ANISOU 2411 N GLN A 317 2549 2469 3242 -685 -187 -466 A N ATOM 2412 CA GLN A 317 15.074 128.839 257.635 1.00 26.53 A C ANISOU 2412 CA GLN A 317 3263 3010 3805 -629 -110 -464 A C ATOM 2413 C GLN A 317 16.195 128.906 256.595 1.00 23.49 A C ANISOU 2413 C GLN A 317 2947 2673 3305 -557 -130 -470 A C ATOM 2414 O GLN A 317 15.922 128.942 255.393 1.00 25.25 A O ANISOU 2414 O GLN A 317 3165 2961 3469 -571 -204 -503 A O ATOM 2415 CB GLN A 317 14.818 127.401 258.119 1.00 36.30 A C ANISOU 2415 CB GLN A 317 4575 4139 5077 -692 -70 -520 A C ATOM 2416 CG GLN A 317 13.919 127.355 259.344 1.00 45.93 A C ANISOU 2416 CG GLN A 317 5729 5319 6404 -753 -25 -493 A C ATOM 2417 CD GLN A 317 13.857 125.986 259.986 1.00 62.22 A C ANISOU 2417 CD GLN A 317 7873 7266 8504 -807 30 -520 A C ATOM 2418 NE2 GLN A 317 13.512 125.950 261.272 1.00 66.85 A N ANISOU 2418 NE2 GLN A 317 8422 7820 9158 -831 99 -471 A N ATOM 2419 OE1 GLN A 317 14.138 124.972 259.346 1.00 68.65 A O ANISOU 2419 OE1 GLN A 317 8782 8017 9285 -824 14 -582 A O ATOM 2420 N PRO A 318 17.463 128.888 257.047 1.00 24.56 A N ANISOU 2420 N PRO A 318 3144 2786 3401 -479 -64 -439 A N ATOM 2421 CA PRO A 318 17.899 128.825 258.450 1.00 27.22 A C ANISOU 2421 CA PRO A 318 3492 3060 3791 -454 20 -400 A C ATOM 2422 C PRO A 318 17.822 130.176 259.150 1.00 29.96 A C ANISOU 2422 C PRO A 318 3742 3454 4190 -429 28 -328 A C ATOM 2423 O PRO A 318 18.115 131.217 258.556 1.00 27.86 A O ANISOU 2423 O PRO A 318 3429 3259 3897 -390 -11 -287 A O ATOM 2424 CB PRO A 318 19.356 128.376 258.338 1.00 23.17 A C ANISOU 2424 CB PRO A 318 3074 2533 3196 -372 66 -398 A C ATOM 2425 CG PRO A 318 19.799 128.924 257.010 1.00 25.01 A C ANISOU 2425 CG PRO A 318 3300 2862 3340 -334 11 -397 A C ATOM 2426 CD PRO A 318 18.601 128.832 256.111 1.00 22.95 A C ANISOU 2426 CD PRO A 318 3004 2631 3084 -408 -69 -446 A C ATOM 2427 N MET A 319 17.432 130.149 260.419 1.00 26.44 A N ANISOU 2427 N MET A 319 3266 2964 3817 -449 80 -311 A N ATOM 2428 CA MET A 319 17.314 131.369 261.204 1.00 25.13 A C ANISOU 2428 CA MET A 319 3011 2833 3704 -423 93 -262 A C ATOM 2429 C MET A 319 18.682 131.715 261.783 1.00 22.10 A C ANISOU 2429 C MET A 319 2664 2450 3281 -343 143 -223 A C ATOM 2430 O MET A 319 18.987 131.387 262.931 1.00 24.23 A O ANISOU 2430 O MET A 319 2957 2686 3566 -329 208 -214 A O ATOM 2431 CB MET A 319 16.263 131.183 262.312 1.00 25.20 A C ANISOU 2431 CB MET A 319 2966 2812 3797 -477 129 -268 A C ATOM 2432 CG MET A 319 14.809 131.034 261.801 1.00 29.02 A C ANISOU 2432 CG MET A 319 3382 3311 4335 -561 75 -300 A C ATOM 2433 SD MET A 319 13.552 130.948 263.114 1.00 32.66 A S ANISOU 2433 SD MET A 319 3754 3759 4895 -623 126 -298 A S ATOM 2434 CE MET A 319 12.048 130.747 262.155 1.00 29.54 A C ANISOU 2434 CE MET A 319 3281 3395 4549 -717 43 -337 A C ATOM 2435 N LEU A 320 19.511 132.368 260.973 1.00 16.83 A N ANISOU 2435 N LEU A 320 2000 1833 2562 -293 112 -196 A N ATOM 2436 CA LEU A 320 20.873 132.720 261.378 1.00 20.47 A C ANISOU 2436 CA LEU A 320 2487 2306 2984 -222 152 -158 A C ATOM 2437 C LEU A 320 21.154 134.179 261.046 1.00 20.89 A C ANISOU 2437 C LEU A 320 2467 2415 3055 -193 113 -106 A C ATOM 2438 O LEU A 320 20.559 134.736 260.126 1.00 22.46 A O ANISOU 2438 O LEU A 320 2620 2650 3263 -214 50 -94 A O ATOM 2439 CB LEU A 320 21.899 131.818 260.688 1.00 22.91 A C ANISOU 2439 CB LEU A 320 2891 2615 3199 -183 168 -173 A C ATOM 2440 CG LEU A 320 21.765 130.313 260.947 1.00 24.56 A C ANISOU 2440 CG LEU A 320 3187 2749 3395 -202 205 -224 A C ATOM 2441 CD1 LEU A 320 22.600 129.501 259.948 1.00 27.03 A C ANISOU 2441 CD1 LEU A 320 3586 3066 3617 -161 204 -255 A C ATOM 2442 CD2 LEU A 320 22.150 129.977 262.381 1.00 17.34 A C ANISOU 2442 CD2 LEU A 320 2293 1788 2508 -180 275 -203 A C ATOM 2443 N ALA A 321 22.046 134.800 261.809 1.00 20.53 A N ANISOU 2443 N ALA A 321 2408 2374 3019 -148 146 -74 A N ATOM 2444 CA ALA A 321 22.295 136.228 261.666 1.00 18.33 A C ANISOU 2444 CA ALA A 321 2058 2126 2780 -129 111 -25 A C ATOM 2445 C ALA A 321 22.883 136.606 260.303 1.00 17.74 A C ANISOU 2445 C ALA A 321 1987 2106 2646 -113 67 21 A C ATOM 2446 O ALA A 321 22.423 137.554 259.655 1.00 15.82 A O ANISOU 2446 O ALA A 321 1684 1887 2439 -124 11 61 A O ATOM 2447 CB ALA A 321 23.202 136.711 262.791 1.00 19.90 A C ANISOU 2447 CB ALA A 321 2247 2318 2997 -91 153 -11 A C ATOM 2448 N HIS A 322 23.876 135.846 259.854 1.00 15.15 A N ANISOU 2448 N HIS A 322 1727 1802 2226 -82 95 20 A N ATOM 2449 CA HIS A 322 24.572 136.179 258.616 1.00 18.24 A C ANISOU 2449 CA HIS A 322 2121 2264 2546 -60 67 68 A C ATOM 2450 C HIS A 322 23.651 136.135 257.394 1.00 19.54 A C ANISOU 2450 C HIS A 322 2276 2465 2684 -93 5 63 A C ATOM 2451 O HIS A 322 23.784 136.962 256.459 1.00 21.39 A O ANISOU 2451 O HIS A 322 2471 2761 2896 -88 -40 127 A O ATOM 2452 CB HIS A 322 25.808 135.288 258.425 1.00 15.98 A C ANISOU 2452 CB HIS A 322 1906 2003 2162 -10 118 57 A C ATOM 2453 CG HIS A 322 25.621 133.873 258.873 1.00 21.07 A C ANISOU 2453 CG HIS A 322 2630 2592 2785 -9 158 -17 A C ATOM 2454 CD2 HIS A 322 25.432 132.730 258.165 1.00 17.27 A C ANISOU 2454 CD2 HIS A 322 2219 2102 2238 -10 158 -74 A C ATOM 2455 ND1 HIS A 322 25.657 133.493 260.202 1.00 16.43 A N ANISOU 2455 ND1 HIS A 322 2057 1943 2243 -4 205 -36 A N ATOM 2456 CE1 HIS A 322 25.487 132.189 260.290 1.00 17.41 A C ANISOU 2456 CE1 HIS A 322 2258 2018 2339 -5 233 -90 A C ATOM 2457 NE2 HIS A 322 25.350 131.700 259.070 1.00 17.84 A N ANISOU 2457 NE2 HIS A 322 2350 2097 2333 -9 204 -120 A N ATOM 2458 N LYS A 323 22.710 135.185 257.414 1.00 20.41 A N ANISOU 2458 N LYS A 323 2418 2540 2796 -130 -2 -8 A N ATOM 2459 CA LYS A 323 21.704 135.096 256.360 1.00 21.21 A C ANISOU 2459 CA LYS A 323 2504 2678 2878 -170 -69 -26 A C ATOM 2460 C LYS A 323 20.927 136.399 256.282 1.00 18.47 A C ANISOU 2460 C LYS A 323 2058 2346 2612 -187 -126 32 A C ATOM 2461 O LYS A 323 20.750 136.966 255.201 1.00 20.61 A O ANISOU 2461 O LYS A 323 2298 2684 2849 -188 -186 80 A O ATOM 2462 CB LYS A 323 20.712 133.958 256.610 1.00 17.38 A C ANISOU 2462 CB LYS A 323 2053 2139 2412 -222 -68 -112 A C ATOM 2463 CG LYS A 323 19.776 133.734 255.419 1.00 19.37 A C ANISOU 2463 CG LYS A 323 2293 2439 2627 -265 -144 -143 A C ATOM 2464 CD LYS A 323 18.510 132.963 255.793 1.00 25.38 A C ANISOU 2464 CD LYS A 323 3048 3146 3450 -336 -158 -213 A C ATOM 2465 CE LYS A 323 17.543 133.902 256.494 1.00 26.97 A C ANISOU 2465 CE LYS A 323 3144 3336 3766 -361 -176 -178 A C ATOM 2466 NZ LYS A 323 16.156 133.404 256.535 1.00 25.17 A N1+ ANISOU 2466 NZ LYS A 323 2877 3092 3593 -436 -210 -230 A N1+ ATOM 2467 N GLY A 324 20.449 136.849 257.440 1.00 19.53 A N ANISOU 2467 N GLY A 324 2145 2422 2853 -198 -107 28 A N ATOM 2468 CA GLY A 324 19.691 138.084 257.547 1.00 21.29 A C ANISOU 2468 CA GLY A 324 2274 2643 3173 -204 -154 72 A C ATOM 2469 C GLY A 324 20.470 139.305 257.095 1.00 21.94 A C ANISOU 2469 C GLY A 324 2322 2753 3261 -168 -178 164 A C ATOM 2470 O GLY A 324 19.930 140.173 256.410 1.00 27.49 A O ANISOU 2470 O GLY A 324 2965 3481 3997 -170 -242 220 A O ATOM 2471 N VAL A 325 21.736 139.387 257.496 1.00 16.95 A N ANISOU 2471 N VAL A 325 1723 2114 2602 -136 -128 185 A N ATOM 2472 CA VAL A 325 22.583 140.498 257.080 1.00 18.72 A C ANISOU 2472 CA VAL A 325 1915 2364 2835 -112 -146 277 A C ATOM 2473 C VAL A 325 22.671 140.544 255.555 1.00 19.55 A C ANISOU 2473 C VAL A 325 2025 2554 2848 -112 -194 338 A C ATOM 2474 O VAL A 325 22.371 141.589 254.919 1.00 17.32 A O ANISOU 2474 O VAL A 325 1685 2291 2604 -114 -251 421 A O ATOM 2475 CB VAL A 325 24.004 140.367 257.674 1.00 19.71 A C ANISOU 2475 CB VAL A 325 2076 2486 2928 -83 -83 283 A C ATOM 2476 CG1 VAL A 325 24.947 141.384 257.038 1.00 17.31 A C ANISOU 2476 CG1 VAL A 325 1738 2221 2618 -70 -101 386 A C ATOM 2477 CG2 VAL A 325 23.968 140.553 259.174 1.00 18.25 A C ANISOU 2477 CG2 VAL A 325 1874 2230 2829 -79 -45 236 A C ATOM 2478 N HIS A 326 23.021 139.405 254.950 1.00 19.49 A N ANISOU 2478 N HIS A 326 2087 2599 2720 -108 -172 295 A N ATOM 2479 CA HIS A 326 23.149 139.412 253.485 1.00 20.59 A C ANISOU 2479 CA HIS A 326 2234 2839 2752 -103 -214 344 A C ATOM 2480 C HIS A 326 21.824 139.705 252.752 1.00 22.47 A C ANISOU 2480 C HIS A 326 2427 3105 3007 -133 -297 355 A C ATOM 2481 O HIS A 326 21.788 140.475 251.765 1.00 25.50 A O ANISOU 2481 O HIS A 326 2771 3556 3360 -128 -351 448 A O ATOM 2482 CB HIS A 326 23.800 138.118 252.991 1.00 14.43 A C ANISOU 2482 CB HIS A 326 1539 2108 1835 -84 -173 280 A C ATOM 2483 CG HIS A 326 25.265 138.038 253.284 1.00 19.88 A C ANISOU 2483 CG HIS A 326 2257 2813 2483 -41 -105 305 A C ATOM 2484 CD2 HIS A 326 25.938 137.977 254.463 1.00 18.10 A C ANISOU 2484 CD2 HIS A 326 2040 2525 2313 -24 -47 289 A C ATOM 2485 ND1 HIS A 326 26.229 138.055 252.296 1.00 17.10 A N ANISOU 2485 ND1 HIS A 326 1918 2564 2015 -9 -92 357 A N ATOM 2486 CE1 HIS A 326 27.426 137.985 252.850 1.00 22.36 A C ANISOU 2486 CE1 HIS A 326 2595 3227 2674 26 -28 371 A C ATOM 2487 NE2 HIS A 326 27.279 137.933 254.161 1.00 22.25 A N ANISOU 2487 NE2 HIS A 326 2579 3112 2761 17 -4 329 A N ATOM 2488 N GLU A 327 20.731 139.139 253.265 1.00 21.16 A N ANISOU 2488 N GLU A 327 2257 2888 2894 -165 -309 271 A N ATOM 2489 CA GLU A 327 19.410 139.409 252.698 1.00 22.00 A C ANISOU 2489 CA GLU A 327 2307 3021 3031 -195 -390 275 A C ATOM 2490 C GLU A 327 19.061 140.897 252.774 1.00 22.73 A C ANISOU 2490 C GLU A 327 2309 3094 3232 -180 -435 375 A C ATOM 2491 O GLU A 327 18.522 141.463 251.825 1.00 22.54 A O ANISOU 2491 O GLU A 327 2240 3132 3194 -180 -509 442 A O ATOM 2492 CB GLU A 327 18.329 138.573 253.394 1.00 17.45 A C ANISOU 2492 CB GLU A 327 1731 2390 2511 -237 -385 170 A C ATOM 2493 CG GLU A 327 18.344 137.097 253.013 1.00 24.92 A C ANISOU 2493 CG GLU A 327 2759 3353 3356 -263 -369 73 A C ATOM 2494 CD GLU A 327 17.361 136.273 253.828 1.00 33.86 A C ANISOU 2494 CD GLU A 327 3891 4417 4559 -315 -354 -18 A C ATOM 2495 OE1 GLU A 327 16.915 136.761 254.891 1.00 35.37 A O ANISOU 2495 OE1 GLU A 327 4027 4548 4864 -320 -331 -10 A O ATOM 2496 OE2 GLU A 327 17.044 135.135 253.415 1.00 36.82 A O1- ANISOU 2496 OE2 GLU A 327 4318 4796 4875 -352 -364 -100 A O1- ATOM 2497 N GLY A 328 19.363 141.518 253.910 1.00 18.46 A N ANISOU 2497 N GLY A 328 1745 2468 2801 -165 -393 383 A N ATOM 2498 CA GLY A 328 19.122 142.943 254.100 1.00 23.74 A C ANISOU 2498 CA GLY A 328 2336 3095 3590 -147 -431 465 A C ATOM 2499 C GLY A 328 19.894 143.792 253.112 1.00 24.71 A C ANISOU 2499 C GLY A 328 2448 3268 3672 -128 -462 593 A C ATOM 2500 O GLY A 328 19.356 144.764 252.520 1.00 18.52 A O ANISOU 2500 O GLY A 328 1603 2493 2941 -119 -531 684 A O ATOM 2501 N HIS A 329 21.170 143.440 252.939 1.00 22.57 A N ANISOU 2501 N HIS A 329 2233 3032 3309 -120 -410 610 A N ATOM 2502 CA HIS A 329 21.975 144.145 251.943 1.00 24.72 A C ANISOU 2502 CA HIS A 329 2496 3372 3526 -108 -430 738 A C ATOM 2503 C HIS A 329 21.345 144.038 250.556 1.00 28.37 A C ANISOU 2503 C HIS A 329 2948 3942 3889 -112 -500 787 A C ATOM 2504 O HIS A 329 21.188 145.056 249.846 1.00 26.65 A O ANISOU 2504 O HIS A 329 2679 3750 3696 -105 -557 913 A O ATOM 2505 CB HIS A 329 23.410 143.620 251.919 1.00 26.08 A C ANISOU 2505 CB HIS A 329 2724 3588 3599 -96 -358 737 A C ATOM 2506 CG HIS A 329 24.216 144.018 253.112 1.00 26.33 A C ANISOU 2506 CG HIS A 329 2750 3533 3723 -91 -304 727 A C ATOM 2507 CD2 HIS A 329 23.894 144.773 254.191 1.00 29.26 A C ANISOU 2507 CD2 HIS A 329 3079 3795 4245 -95 -308 710 A C ATOM 2508 ND1 HIS A 329 25.526 143.633 253.293 1.00 29.41 A N ANISOU 2508 ND1 HIS A 329 3175 3953 4047 -78 -239 726 A N ATOM 2509 CE1 HIS A 329 25.976 144.128 254.428 1.00 28.79 A C ANISOU 2509 CE1 HIS A 329 3077 3791 4072 -79 -210 711 A C ATOM 2510 NE2 HIS A 329 25.008 144.822 254.997 1.00 31.85 A N ANISOU 2510 NE2 HIS A 329 3421 4092 4590 -89 -250 697 A N ATOM 2511 N VAL A 330 20.959 142.821 250.171 1.00 24.68 A N ANISOU 2511 N VAL A 330 2529 3535 3312 -123 -499 690 A N ATOM 2512 CA VAL A 330 20.370 142.663 248.841 1.00 23.81 A C ANISOU 2512 CA VAL A 330 2412 3541 3093 -129 -571 722 A C ATOM 2513 C VAL A 330 19.060 143.447 248.686 1.00 24.93 A C ANISOU 2513 C VAL A 330 2472 3666 3334 -136 -659 768 A C ATOM 2514 O VAL A 330 18.847 144.113 247.679 1.00 24.62 A O ANISOU 2514 O VAL A 330 2395 3705 3256 -125 -726 879 A O ATOM 2515 CB VAL A 330 20.131 141.190 248.478 1.00 23.46 A C ANISOU 2515 CB VAL A 330 2436 3554 2925 -145 -562 590 A C ATOM 2516 CG1 VAL A 330 19.444 141.097 247.110 1.00 24.97 A C ANISOU 2516 CG1 VAL A 330 2612 3874 3002 -153 -648 615 A C ATOM 2517 CG2 VAL A 330 21.448 140.449 248.436 1.00 19.82 A C ANISOU 2517 CG2 VAL A 330 2052 3123 2354 -123 -482 556 A C ATOM 2518 N ALA A 331 18.184 143.373 249.682 1.00 23.08 A N ANISOU 2518 N ALA A 331 2207 3337 3225 -149 -659 689 A N ATOM 2519 CA ALA A 331 16.909 144.083 249.607 1.00 24.15 A C ANISOU 2519 CA ALA A 331 2256 3458 3463 -148 -738 723 A C ATOM 2520 C ALA A 331 17.144 145.583 249.431 1.00 24.57 A C ANISOU 2520 C ALA A 331 2252 3477 3608 -114 -772 874 A C ATOM 2521 O ALA A 331 16.536 146.229 248.553 1.00 26.41 A O ANISOU 2521 O ALA A 331 2431 3765 3839 -100 -855 972 A O ATOM 2522 CB ALA A 331 16.082 143.818 250.847 1.00 18.38 A C ANISOU 2522 CB ALA A 331 1497 2631 2857 -162 -713 616 A C ATOM 2523 N ALA A 332 18.057 146.123 250.239 1.00 21.72 A N ANISOU 2523 N ALA A 332 1903 3024 3325 -102 -711 896 A N ATOM 2524 CA ALA A 332 18.387 147.538 250.112 1.00 22.59 A C ANISOU 2524 CA ALA A 332 1966 3082 3535 -77 -740 1037 A C ATOM 2525 C ALA A 332 18.880 147.855 248.704 1.00 27.20 A C ANISOU 2525 C ALA A 332 2555 3781 4000 -74 -780 1180 A C ATOM 2526 O ALA A 332 18.411 148.816 248.082 1.00 25.23 A O ANISOU 2526 O ALA A 332 2249 3537 3801 -55 -853 1306 A O ATOM 2527 CB ALA A 332 19.435 147.934 251.138 1.00 18.42 A C ANISOU 2527 CB ALA A 332 1458 2451 3088 -76 -667 1026 A C ATOM 2528 N GLU A 333 19.784 147.021 248.186 1.00 27.99 A N ANISOU 2528 N GLU A 333 2720 3979 3937 -86 -733 1163 A N ATOM 2529 CA GLU A 333 20.347 147.250 246.851 1.00 25.74 A C ANISOU 2529 CA GLU A 333 2441 3824 3514 -81 -759 1295 A C ATOM 2530 C GLU A 333 19.301 147.201 245.731 1.00 25.19 A C ANISOU 2530 C GLU A 333 2341 3867 3363 -75 -853 1336 A C ATOM 2531 O GLU A 333 19.384 147.960 244.765 1.00 28.36 A O ANISOU 2531 O GLU A 333 2711 4341 3723 -62 -904 1493 A O ATOM 2532 CB GLU A 333 21.483 146.261 246.563 1.00 28.83 A C ANISOU 2532 CB GLU A 333 2907 4307 3740 -86 -683 1244 A C ATOM 2533 CG GLU A 333 22.761 146.543 247.349 1.00 30.97 A C ANISOU 2533 CG GLU A 333 3194 4505 4068 -88 -600 1261 A C ATOM 2534 CD GLU A 333 23.567 145.284 247.618 1.00 33.81 A C ANISOU 2534 CD GLU A 333 3628 4907 4314 -85 -518 1139 A C ATOM 2535 OE1 GLU A 333 23.331 144.276 246.916 1.00 33.34 A O ANISOU 2535 OE1 GLU A 333 3611 4949 4107 -80 -524 1068 A O ATOM 2536 OE2 GLU A 333 24.419 145.295 248.539 1.00 32.64 A O1- ANISOU 2536 OE2 GLU A 333 3492 4686 4225 -85 -451 1110 A O1- ATOM 2537 N VAL A 334 18.338 146.290 245.853 1.00 27.10 A N ANISOU 2537 N VAL A 334 2590 4129 3579 -88 -878 1200 A N ATOM 2538 CA VAL A 334 17.259 146.159 244.874 1.00 30.93 A C ANISOU 2538 CA VAL A 334 3039 4724 3990 -89 -975 1216 A C ATOM 2539 C VAL A 334 16.368 147.393 244.932 1.00 33.56 A C ANISOU 2539 C VAL A 334 3281 4993 4477 -64 -1051 1325 A C ATOM 2540 O VAL A 334 15.990 147.944 243.892 1.00 35.91 A O ANISOU 2540 O VAL A 334 3567 5359 4718 -49 -1095 1411 A O ATOM 2541 CB VAL A 334 16.410 144.883 245.102 1.00 29.75 A C ANISOU 2541 CB VAL A 334 2912 4594 3799 -120 -983 1035 A C ATOM 2542 CG1 VAL A 334 15.155 144.908 244.247 1.00 25.44 A C ANISOU 2542 CG1 VAL A 334 2306 4146 3215 -124 -1096 1051 A C ATOM 2543 CG2 VAL A 334 17.224 143.637 244.804 1.00 30.07 A C ANISOU 2543 CG2 VAL A 334 3048 4706 3673 -136 -922 932 A C ATOM 2544 N ILE A 335 16.032 147.829 246.146 1.00 31.33 A N ANISOU 2544 N ILE A 335 2965 4556 4382 -57 -1026 1278 A N ATOM 2545 CA ILE A 335 15.233 149.050 246.292 1.00 29.72 A C ANISOU 2545 CA ILE A 335 2714 4253 4325 -27 -1050 1330 A C ATOM 2546 C ILE A 335 15.956 150.245 245.659 1.00 30.91 A C ANISOU 2546 C ILE A 335 2878 4383 4484 -13 -1037 1487 A C ATOM 2547 O ILE A 335 15.328 151.119 245.062 1.00 34.10 A O ANISOU 2547 O ILE A 335 3250 4782 4924 9 -1082 1568 A O ATOM 2548 CB ILE A 335 14.873 149.337 247.769 1.00 29.23 A C ANISOU 2548 CB ILE A 335 2625 4032 4451 -18 -1010 1239 A C ATOM 2549 CG1 ILE A 335 13.866 148.301 248.264 1.00 30.50 A C ANISOU 2549 CG1 ILE A 335 2755 4219 4615 -37 -1027 1096 A C ATOM 2550 CG2 ILE A 335 14.283 150.735 247.930 1.00 26.80 A C ANISOU 2550 CG2 ILE A 335 2279 3615 4290 19 -1025 1301 A C ATOM 2551 CD1 ILE A 335 13.515 148.429 249.733 1.00 31.95 A C ANISOU 2551 CD1 ILE A 335 2915 4268 4956 -29 -972 993 A C ATOM 2552 N ALA A 336 17.284 150.253 245.754 1.00 32.06 A N ANISOU 2552 N ALA A 336 3325 4338 4520 947 34 1631 A N ATOM 2553 CA ALA A 336 18.073 151.335 245.175 1.00 32.15 A C ANISOU 2553 CA ALA A 336 3393 4274 4546 1038 199 1732 A C ATOM 2554 C ALA A 336 18.118 151.238 243.653 1.00 37.22 A C ANISOU 2554 C ALA A 336 4160 4993 4988 1151 140 1840 A C ATOM 2555 O ALA A 336 18.577 152.165 242.980 1.00 42.81 A O ANISOU 2555 O ALA A 336 4919 5652 5696 1257 277 1967 A O ATOM 2556 CB ALA A 336 19.473 151.318 245.738 1.00 31.77 A C ANISOU 2556 CB ALA A 336 3385 4125 4562 973 338 1643 A C ATOM 2557 N GLY A 337 17.636 150.120 243.115 1.00 35.89 A N ANISOU 2557 N GLY A 337 4054 4935 4647 1134 -63 1791 A N ATOM 2558 CA GLY A 337 17.519 149.961 241.677 1.00 38.65 A C ANISOU 2558 CA GLY A 337 4556 5361 4769 1254 -160 1878 A C ATOM 2559 C GLY A 337 18.567 149.067 241.043 1.00 38.36 A C ANISOU 2559 C GLY A 337 4710 5335 4530 1265 -143 1809 A C ATOM 2560 O GLY A 337 18.642 148.982 239.822 1.00 41.63 A O ANISOU 2560 O GLY A 337 5298 5796 4724 1389 -186 1882 A O ATOM 2561 N LYS A 338 19.364 148.390 241.863 1.00 39.28 A N ANISOU 2561 N LYS A 338 4807 5407 4712 1149 -78 1674 A N ATOM 2562 CA LYS A 338 20.373 147.468 241.347 1.00 39.91 A C ANISOU 2562 CA LYS A 338 5054 5487 4623 1157 -46 1609 A C ATOM 2563 C LYS A 338 19.767 146.097 241.075 1.00 44.23 A C ANISOU 2563 C LYS A 338 5682 6122 5002 1106 -294 1490 A C ATOM 2564 O LYS A 338 18.903 145.642 241.820 1.00 42.76 A O ANISOU 2564 O LYS A 338 5365 5966 4917 996 -446 1412 A O ATOM 2565 CB LYS A 338 21.534 147.347 242.337 1.00 36.17 A C ANISOU 2565 CB LYS A 338 4513 4918 4312 1059 123 1528 A C ATOM 2566 CG LYS A 338 22.265 148.656 242.568 1.00 41.51 A C ANISOU 2566 CG LYS A 338 5115 5479 5176 1099 352 1634 A C ATOM 2567 CD LYS A 338 23.335 148.531 243.640 1.00 47.31 A C ANISOU 2567 CD LYS A 338 5767 6114 6096 986 463 1542 A C ATOM 2568 CE LYS A 338 23.953 149.893 243.938 1.00 51.96 A C ANISOU 2568 CE LYS A 338 6264 6566 6911 1009 653 1638 A C ATOM 2569 NZ LYS A 338 25.040 150.267 242.983 1.00 55.03 A N1+ ANISOU 2569 NZ LYS A 338 6729 6886 7292 1117 846 1774 A N1+ ATOM 2570 N LYS A 339 20.218 145.429 240.019 1.00 49.41 A N ANISOU 2570 N LYS A 339 6559 6805 5410 1189 -326 1479 A N ATOM 2571 CA LYS A 339 19.669 144.112 239.712 1.00 51.39 A C ANISOU 2571 CA LYS A 339 6909 7118 5499 1139 -577 1353 A C ATOM 2572 C LYS A 339 20.427 143.009 240.445 1.00 46.01 A C ANISOU 2572 C LYS A 339 6224 6399 4859 1018 -533 1202 A C ATOM 2573 O LYS A 339 21.220 142.274 239.850 1.00 48.11 A O ANISOU 2573 O LYS A 339 6682 6650 4950 1066 -487 1156 A O ATOM 2574 CB LYS A 339 19.577 143.872 238.196 1.00 61.19 A C ANISOU 2574 CB LYS A 339 8423 8405 6420 1297 -685 1396 A C ATOM 2575 CG LYS A 339 18.850 142.578 237.780 1.00 72.44 A C ANISOU 2575 CG LYS A 339 9965 9881 7678 1248 -1001 1259 A C ATOM 2576 CD LYS A 339 18.565 142.541 236.265 1.00 80.38 A C ANISOU 2576 CD LYS A 339 11257 10931 8351 1423 -1152 1308 A C ATOM 2577 CE LYS A 339 19.635 141.761 235.489 1.00 83.78 A C ANISOU 2577 CE LYS A 339 11976 11316 8540 1493 -1032 1231 A C ATOM 2578 NZ LYS A 339 19.553 140.286 235.725 1.00 85.42 A N1+ ANISOU 2578 NZ LYS A 339 12251 11514 8693 1378 -1215 1038 A N1+ ATOM 2579 N HIS A 340 20.185 142.917 241.750 1.00 39.94 A N ANISOU 2579 N HIS A 340 5246 5610 4320 875 -533 1136 A N ATOM 2580 CA HIS A 340 20.881 141.954 242.586 1.00 37.47 A C ANISOU 2580 CA HIS A 340 4907 5260 4070 761 -487 1007 A C ATOM 2581 C HIS A 340 19.905 140.896 243.079 1.00 35.95 A C ANISOU 2581 C HIS A 340 4642 5106 3912 642 -712 895 A C ATOM 2582 O HIS A 340 18.695 141.131 243.158 1.00 32.24 A O ANISOU 2582 O HIS A 340 4061 4676 3514 622 -866 929 A O ATOM 2583 CB HIS A 340 21.538 142.656 243.781 1.00 35.90 A C ANISOU 2583 CB HIS A 340 4548 4991 4102 700 -293 1018 A C ATOM 2584 CG HIS A 340 22.698 143.518 243.402 1.00 36.39 A C ANISOU 2584 CG HIS A 340 4660 4984 4183 790 -65 1116 A C ATOM 2585 CD2 HIS A 340 23.263 143.763 242.196 1.00 37.23 A C ANISOU 2585 CD2 HIS A 340 4929 5083 4133 929 32 1213 A C ATOM 2586 ND1 HIS A 340 23.396 144.284 244.314 1.00 40.81 A N ANISOU 2586 ND1 HIS A 340 5092 5457 4956 746 95 1134 A N ATOM 2587 CE1 HIS A 340 24.352 144.943 243.688 1.00 41.94 A C ANISOU 2587 CE1 HIS A 340 5292 5537 5107 840 277 1241 A C ATOM 2588 NE2 HIS A 340 24.294 144.648 242.404 1.00 39.91 A N ANISOU 2588 NE2 HIS A 340 5212 5329 4625 959 262 1300 A N ATOM 2589 N TYR A 341 20.445 139.730 243.408 1.00 35.44 A N ANISOU 2589 N TYR A 341 4627 5020 3818 567 -721 776 A N ATOM 2590 CA TYR A 341 19.640 138.605 243.836 1.00 35.25 A C ANISOU 2590 CA TYR A 341 4543 5013 3836 454 -917 671 A C ATOM 2591 C TYR A 341 20.332 137.968 245.025 1.00 32.16 A C ANISOU 2591 C TYR A 341 4073 4577 3569 351 -803 586 A C ATOM 2592 O TYR A 341 21.556 138.012 245.131 1.00 32.52 A O ANISOU 2592 O TYR A 341 4181 4582 3594 376 -627 581 A O ATOM 2593 CB TYR A 341 19.501 137.597 242.694 1.00 36.03 A C ANISOU 2593 CB TYR A 341 4854 5128 3710 488 -1100 600 A C ATOM 2594 CG TYR A 341 18.827 138.178 241.477 1.00 38.01 A C ANISOU 2594 CG TYR A 341 5214 5424 3803 603 -1243 679 A C ATOM 2595 CD1 TYR A 341 19.571 138.770 240.463 1.00 40.72 A C ANISOU 2595 CD1 TYR A 341 5758 5768 3946 760 -1116 756 A C ATOM 2596 CD2 TYR A 341 17.444 138.152 241.348 1.00 38.20 A C ANISOU 2596 CD2 TYR A 341 5135 5487 3893 564 -1501 694 A C ATOM 2597 CE1 TYR A 341 18.956 139.318 239.350 1.00 37.42 A C ANISOU 2597 CE1 TYR A 341 5460 5395 3363 883 -1248 838 A C ATOM 2598 CE2 TYR A 341 16.821 138.696 240.238 1.00 39.88 A C ANISOU 2598 CE2 TYR A 341 5448 5743 3961 674 -1657 773 A C ATOM 2599 CZ TYR A 341 17.583 139.275 239.242 1.00 41.34 A C ANISOU 2599 CZ TYR A 341 5858 5936 3914 838 -1532 841 A C ATOM 2600 OH TYR A 341 16.973 139.818 238.132 1.00 46.74 A O ANISOU 2600 OH TYR A 341 6663 6666 4430 965 -1687 928 A O ATOM 2601 N PHE A 342 19.545 137.378 245.917 1.00 28.84 A N ANISOU 2601 N PHE A 342 3509 4158 3289 243 -901 535 A N ATOM 2602 CA PHE A 342 20.091 136.587 247.005 1.00 23.47 A C ANISOU 2602 CA PHE A 342 2776 3441 2701 152 -824 452 A C ATOM 2603 C PHE A 342 19.957 135.119 246.643 1.00 27.20 A C ANISOU 2603 C PHE A 342 3337 3905 3093 97 -970 349 A C ATOM 2604 O PHE A 342 18.858 134.559 246.662 1.00 28.40 A O ANISOU 2604 O PHE A 342 3415 4065 3309 35 -1151 328 A O ATOM 2605 CB PHE A 342 19.374 136.891 248.319 1.00 22.52 A C ANISOU 2605 CB PHE A 342 2455 3314 2786 87 -796 474 A C ATOM 2606 CG PHE A 342 19.899 136.105 249.484 1.00 24.35 A C ANISOU 2606 CG PHE A 342 2647 3510 3095 10 -719 399 A C ATOM 2607 CD1 PHE A 342 21.114 136.430 250.067 1.00 20.40 A C ANISOU 2607 CD1 PHE A 342 2175 2973 2603 20 -557 383 A C ATOM 2608 CD2 PHE A 342 19.172 135.038 249.999 1.00 23.25 A C ANISOU 2608 CD2 PHE A 342 2434 3365 3035 -72 -816 354 A C ATOM 2609 CE1 PHE A 342 21.603 135.703 251.138 1.00 24.32 A C ANISOU 2609 CE1 PHE A 342 2643 3439 3158 -41 -504 320 A C ATOM 2610 CE2 PHE A 342 19.651 134.308 251.072 1.00 25.38 A C ANISOU 2610 CE2 PHE A 342 2677 3602 3365 -129 -737 299 A C ATOM 2611 CZ PHE A 342 20.870 134.637 251.642 1.00 25.61 A C ANISOU 2611 CZ PHE A 342 2751 3606 3374 -110 -586 279 A C ATOM 2612 N ASP A 343 21.078 134.516 246.267 1.00 31.85 A N ANISOU 2612 N ASP A 343 4081 4463 3556 123 -888 294 A N ATOM 2613 CA ASP A 343 21.095 133.127 245.830 1.00 35.72 A C ANISOU 2613 CA ASP A 343 4696 4927 3949 87 -1006 188 A C ATOM 2614 C ASP A 343 22.434 132.493 246.172 1.00 29.26 A C ANISOU 2614 C ASP A 343 3951 4061 3107 86 -836 141 A C ATOM 2615 O ASP A 343 23.189 132.107 245.280 1.00 29.58 A O ANISOU 2615 O ASP A 343 4185 4075 2978 161 -789 118 A O ATOM 2616 CB ASP A 343 20.841 133.052 244.320 1.00 41.02 A C ANISOU 2616 CB ASP A 343 5578 5612 4397 177 -1147 179 A C ATOM 2617 CG ASP A 343 20.398 131.671 243.864 1.00 48.78 A C ANISOU 2617 CG ASP A 343 6675 6558 5303 123 -1354 56 A C ATOM 2618 OD1 ASP A 343 19.787 130.941 244.674 1.00 51.23 A O ANISOU 2618 OD1 ASP A 343 6835 6844 5784 0 -1445 7 A O ATOM 2619 OD2 ASP A 343 20.647 131.324 242.688 1.00 54.66 A O1- ANISOU 2619 OD2 ASP A 343 7668 7287 5814 210 -1424 11 A O1- ATOM 2620 N PRO A 344 22.745 132.394 247.471 1.00 24.91 A N ANISOU 2620 N PRO A 344 3250 3493 2720 12 -738 135 A N ATOM 2621 CA PRO A 344 24.047 131.848 247.860 1.00 26.04 A C ANISOU 2621 CA PRO A 344 3439 3590 2865 13 -587 106 A C ATOM 2622 C PRO A 344 24.080 130.348 247.604 1.00 29.44 A C ANISOU 2622 C PRO A 344 3974 3982 3228 -26 -664 7 A C ATOM 2623 O PRO A 344 23.050 129.684 247.729 1.00 23.31 A O ANISOU 2623 O PRO A 344 3156 3206 2495 -99 -828 -44 A O ATOM 2624 CB PRO A 344 24.089 132.104 249.364 1.00 21.42 A C ANISOU 2624 CB PRO A 344 2674 3003 2464 -58 -521 118 A C ATOM 2625 CG PRO A 344 22.663 132.020 249.782 1.00 22.77 A C ANISOU 2625 CG PRO A 344 2731 3201 2719 -119 -658 115 A C ATOM 2626 CD PRO A 344 21.870 132.610 248.638 1.00 25.67 A C ANISOU 2626 CD PRO A 344 3147 3605 3001 -67 -773 153 A C ATOM 2627 N LYS A 345 25.235 129.823 247.218 1.00 31.15 A N ANISOU 2627 N LYS A 345 4322 4154 3359 26 -544 -11 A N ATOM 2628 CA LYS A 345 25.379 128.379 247.096 1.00 29.44 A C ANISOU 2628 CA LYS A 345 4207 3883 3095 -7 -590 -106 A C ATOM 2629 C LYS A 345 25.311 127.724 248.468 1.00 26.36 A C ANISOU 2629 C LYS A 345 3656 3478 2883 -115 -582 -133 A C ATOM 2630 O LYS A 345 24.765 126.628 248.613 1.00 33.27 A O ANISOU 2630 O LYS A 345 4538 4317 3785 -184 -688 -207 A O ATOM 2631 CB LYS A 345 26.681 128.013 246.388 1.00 33.99 A C ANISOU 2631 CB LYS A 345 4961 4406 3548 93 -427 -101 A C ATOM 2632 CG LYS A 345 26.553 127.983 244.878 1.00 42.24 A C ANISOU 2632 CG LYS A 345 6256 5439 4354 205 -476 -120 A C ATOM 2633 CD LYS A 345 27.794 127.412 244.214 1.00 50.57 A C ANISOU 2633 CD LYS A 345 7506 6422 5285 317 -291 -116 A C ATOM 2634 CE LYS A 345 27.811 127.803 242.749 1.00 55.33 A C ANISOU 2634 CE LYS A 345 8366 7023 5635 472 -278 -92 A C ATOM 2635 NZ LYS A 345 27.666 129.282 242.613 1.00 55.56 A N1+ ANISOU 2635 NZ LYS A 345 8302 7117 5692 521 -232 30 A N1+ ATOM 2636 N VAL A 346 25.908 128.377 249.464 1.00 22.51 A N ANISOU 2636 N VAL A 346 3033 3005 2514 -123 -456 -72 A N ATOM 2637 CA VAL A 346 25.984 127.814 250.811 1.00 24.08 A C ANISOU 2637 CA VAL A 346 3106 3189 2853 -199 -431 -87 A C ATOM 2638 C VAL A 346 25.694 128.823 251.915 1.00 26.20 A C ANISOU 2638 C VAL A 346 3218 3495 3240 -221 -405 -33 A C ATOM 2639 O VAL A 346 25.914 130.027 251.757 1.00 26.74 A O ANISOU 2639 O VAL A 346 3266 3585 3309 -175 -357 22 A O ATOM 2640 CB VAL A 346 27.356 127.170 251.085 1.00 22.63 A C ANISOU 2640 CB VAL A 346 2962 2956 2681 -177 -298 -88 A C ATOM 2641 CG1 VAL A 346 27.623 126.053 250.097 1.00 21.78 A C ANISOU 2641 CG1 VAL A 346 3025 2794 2455 -147 -304 -148 A C ATOM 2642 CG2 VAL A 346 28.461 128.219 251.011 1.00 19.35 A C ANISOU 2642 CG2 VAL A 346 2528 2539 2286 -110 -165 -11 A C ATOM 2643 N ILE A 347 25.189 128.310 253.031 1.00 21.91 A N ANISOU 2643 N ILE A 347 2579 2949 2797 -283 -427 -46 A N ATOM 2644 CA ILE A 347 25.035 129.085 254.253 1.00 19.27 A C ANISOU 2644 CA ILE A 347 2134 2635 2555 -289 -382 -5 A C ATOM 2645 C ILE A 347 25.591 128.254 255.405 1.00 18.25 A C ANISOU 2645 C ILE A 347 1979 2476 2478 -315 -330 -21 A C ATOM 2646 O ILE A 347 25.083 127.177 255.691 1.00 21.34 A O ANISOU 2646 O ILE A 347 2356 2849 2903 -357 -360 -43 A O ATOM 2647 CB ILE A 347 23.558 129.415 254.545 1.00 19.96 A C ANISOU 2647 CB ILE A 347 2128 2749 2707 -313 -451 22 A C ATOM 2648 CG1 ILE A 347 22.914 130.118 253.345 1.00 22.11 A C ANISOU 2648 CG1 ILE A 347 2422 3050 2927 -287 -532 43 A C ATOM 2649 CG2 ILE A 347 23.439 130.268 255.807 1.00 16.06 A C ANISOU 2649 CG2 ILE A 347 1558 2263 2283 -294 -379 62 A C ATOM 2650 CD1 ILE A 347 21.445 130.437 253.524 1.00 27.34 A C ANISOU 2650 CD1 ILE A 347 2972 3735 3682 -307 -609 88 A C ATOM 2651 N PRO A 348 26.647 128.754 256.063 1.00 17.17 A N ANISOU 2651 N PRO A 348 1834 2328 2361 -289 -261 -6 A N ATOM 2652 CA PRO A 348 27.318 128.029 257.145 1.00 19.35 A C ANISOU 2652 CA PRO A 348 2099 2579 2675 -300 -226 -14 A C ATOM 2653 C PRO A 348 26.464 127.940 258.404 1.00 19.49 A C ANISOU 2653 C PRO A 348 2067 2607 2730 -310 -230 -3 A C ATOM 2654 O PRO A 348 25.598 128.790 258.629 1.00 18.54 A O ANISOU 2654 O PRO A 348 1911 2510 2624 -297 -238 19 A O ATOM 2655 CB PRO A 348 28.559 128.887 257.418 1.00 21.00 A C ANISOU 2655 CB PRO A 348 2300 2767 2911 -269 -190 6 A C ATOM 2656 CG PRO A 348 28.169 130.264 256.988 1.00 19.65 A C ANISOU 2656 CG PRO A 348 2114 2613 2739 -247 -197 28 A C ATOM 2657 CD PRO A 348 27.285 130.056 255.790 1.00 20.59 A C ANISOU 2657 CD PRO A 348 2266 2761 2798 -248 -226 26 A C ATOM 2658 N SER A 349 26.695 126.896 259.195 1.00 14.69 A N ANISOU 2658 N SER A 349 1462 1979 2141 -319 -207 -5 A N ATOM 2659 CA SER A 349 26.042 126.739 260.490 1.00 14.54 A C ANISOU 2659 CA SER A 349 1418 1961 2144 -304 -179 22 A C ATOM 2660 C SER A 349 27.110 126.341 261.503 1.00 20.24 A C ANISOU 2660 C SER A 349 2177 2664 2848 -276 -157 22 A C ATOM 2661 O SER A 349 27.998 125.541 261.179 1.00 17.30 A O ANISOU 2661 O SER A 349 1821 2270 2484 -290 -155 12 A O ATOM 2662 CB SER A 349 24.965 125.655 260.431 1.00 20.16 A C ANISOU 2662 CB SER A 349 2087 2657 2915 -341 -174 40 A C ATOM 2663 OG SER A 349 23.939 125.982 259.520 1.00 32.52 A O ANISOU 2663 OG SER A 349 3608 4235 4514 -371 -228 42 A O ATOM 2664 N ILE A 350 27.050 126.921 262.703 1.00 18.25 A N ANISOU 2664 N ILE A 350 1950 2416 2566 -228 -146 35 A N ATOM 2665 CA ILE A 350 27.992 126.589 263.778 1.00 18.64 A C ANISOU 2665 CA ILE A 350 2050 2448 2583 -191 -156 36 A C ATOM 2666 C ILE A 350 27.310 126.431 265.144 1.00 21.09 A C ANISOU 2666 C ILE A 350 2412 2758 2841 -126 -106 69 A C ATOM 2667 O ILE A 350 26.510 127.272 265.552 1.00 22.36 A O ANISOU 2667 O ILE A 350 2595 2925 2973 -85 -77 77 A O ATOM 2668 CB ILE A 350 29.101 127.644 263.937 1.00 19.31 A C ANISOU 2668 CB ILE A 350 2158 2517 2660 -177 -230 5 A C ATOM 2669 CG1 ILE A 350 29.850 127.870 262.625 1.00 17.03 A C ANISOU 2669 CG1 ILE A 350 1818 2218 2434 -220 -245 -2 A C ATOM 2670 CG2 ILE A 350 30.081 127.244 265.061 1.00 14.42 A C ANISOU 2670 CG2 ILE A 350 1587 1876 2014 -140 -281 6 A C ATOM 2671 CD1 ILE A 350 30.882 128.996 262.711 1.00 16.78 A C ANISOU 2671 CD1 ILE A 350 1776 2152 2449 -214 -309 -15 A C ATOM 2672 N ALA A 351 27.621 125.333 265.827 1.00 17.85 A N ANISOU 2672 N ALA A 351 2028 2335 2418 -104 -79 99 A N ATOM 2673 CA ALA A 351 27.298 125.142 267.229 1.00 16.38 A C ANISOU 2673 CA ALA A 351 1924 2143 2155 -16 -27 140 A C ATOM 2674 C ALA A 351 28.566 125.439 268.009 1.00 17.30 A C ANISOU 2674 C ALA A 351 2129 2251 2192 28 -127 108 A C ATOM 2675 O ALA A 351 29.580 124.744 267.833 1.00 17.64 A O ANISOU 2675 O ALA A 351 2146 2286 2273 1 -176 110 A O ATOM 2676 CB ALA A 351 26.855 123.708 267.481 1.00 15.98 A C ANISOU 2676 CB ALA A 351 1845 2075 2150 -13 66 208 A C ATOM 2677 N TYR A 352 28.505 126.465 268.861 1.00 17.74 A N ANISOU 2677 N TYR A 352 2290 2301 2149 98 -165 79 A N ATOM 2678 CA TYR A 352 29.669 126.940 269.602 1.00 18.93 A C ANISOU 2678 CA TYR A 352 2531 2429 2232 133 -308 31 A C ATOM 2679 C TYR A 352 29.799 126.186 270.919 1.00 22.63 A C ANISOU 2679 C TYR A 352 3126 2895 2579 234 -299 71 A C ATOM 2680 O TYR A 352 30.111 126.760 271.969 1.00 23.23 A O ANISOU 2680 O TYR A 352 3355 2950 2522 318 -387 35 A O ATOM 2681 CB TYR A 352 29.580 128.451 269.841 1.00 18.34 A C ANISOU 2681 CB TYR A 352 2531 2328 2107 158 -377 -37 A C ATOM 2682 CG TYR A 352 29.561 129.273 268.564 1.00 18.80 A C ANISOU 2682 CG TYR A 352 2471 2385 2285 70 -389 -66 A C ATOM 2683 CD1 TYR A 352 28.374 129.491 267.877 1.00 17.79 A C ANISOU 2683 CD1 TYR A 352 2285 2283 2192 54 -273 -38 A C ATOM 2684 CD2 TYR A 352 30.723 129.841 268.060 1.00 23.28 A C ANISOU 2684 CD2 TYR A 352 2981 2919 2943 11 -514 -105 A C ATOM 2685 CE1 TYR A 352 28.344 130.240 266.720 1.00 18.52 A C ANISOU 2685 CE1 TYR A 352 2287 2377 2374 -10 -286 -55 A C ATOM 2686 CE2 TYR A 352 30.703 130.596 266.899 1.00 21.44 A C ANISOU 2686 CE2 TYR A 352 2653 2681 2814 -51 -502 -114 A C ATOM 2687 CZ TYR A 352 29.511 130.788 266.236 1.00 23.72 A C ANISOU 2687 CZ TYR A 352 2908 3005 3102 -57 -390 -91 A C ATOM 2688 OH TYR A 352 29.481 131.536 265.084 1.00 24.30 A O ANISOU 2688 OH TYR A 352 2901 3075 3258 -104 -380 -91 A O ATOM 2689 N THR A 353 29.549 124.884 270.846 1.00 19.91 A N ANISOU 2689 N THR A 353 2728 2562 2274 230 -196 146 A N ATOM 2690 CA THR A 353 29.792 123.986 271.959 1.00 21.42 A C ANISOU 2690 CA THR A 353 3019 2749 2370 324 -175 206 A C ATOM 2691 C THR A 353 31.295 123.724 272.003 1.00 22.92 A C ANISOU 2691 C THR A 353 3191 2930 2588 298 -341 184 A C ATOM 2692 O THR A 353 32.050 124.271 271.196 1.00 22.16 A O ANISOU 2692 O THR A 353 3001 2823 2595 213 -447 131 A O ATOM 2693 CB THR A 353 29.061 122.658 271.740 1.00 24.60 A C ANISOU 2693 CB THR A 353 3343 3150 2853 313 -5 300 A C ATOM 2694 CG2 THR A 353 27.562 122.839 271.934 1.00 24.01 A C ANISOU 2694 CG2 THR A 353 3277 3071 2775 357 162 352 A C ATOM 2695 OG1 THR A 353 29.305 122.197 270.405 1.00 24.52 A O ANISOU 2695 OG1 THR A 353 3175 3136 3004 188 -13 281 A O ATOM 2696 N GLU A 354 31.729 122.884 272.935 1.00 24.85 A N ANISOU 2696 N GLU A 354 3515 3173 2755 379 -356 241 A N ATOM 2697 CA GLU A 354 33.125 122.470 273.007 1.00 27.63 A C ANISOU 2697 CA GLU A 354 3827 3513 3160 362 -506 248 A C ATOM 2698 C GLU A 354 33.222 120.947 273.048 1.00 31.63 A C ANISOU 2698 C GLU A 354 4284 4018 3716 380 -396 348 A C ATOM 2699 O GLU A 354 32.856 120.329 274.045 1.00 33.36 A O ANISOU 2699 O GLU A 354 4618 4242 3817 487 -326 417 A O ATOM 2700 CB GLU A 354 33.833 123.104 274.206 1.00 36.51 A C ANISOU 2700 CB GLU A 354 5112 4624 4136 452 -706 209 A C ATOM 2701 CG GLU A 354 35.357 122.934 274.209 1.00 44.79 A C ANISOU 2701 CG GLU A 354 6083 5649 5286 418 -911 212 A C ATOM 2702 CD GLU A 354 36.055 123.703 273.093 1.00 48.71 A C ANISOU 2702 CD GLU A 354 6409 6115 5981 291 -999 159 A C ATOM 2703 OE1 GLU A 354 35.395 124.504 272.401 1.00 50.64 A O ANISOU 2703 OE1 GLU A 354 6625 6362 6253 237 -931 105 A O ATOM 2704 OE2 GLU A 354 37.273 123.502 272.909 1.00 50.92 A O1- ANISOU 2704 OE2 GLU A 354 6578 6366 6403 254 -1127 187 A O1- ATOM 2705 N PRO A 355 33.705 120.333 271.957 1.00 29.43 A N ANISOU 2705 N PRO A 355 3848 3724 3611 284 -364 361 A N ATOM 2706 CA PRO A 355 34.214 120.973 270.737 1.00 23.21 A C ANISOU 2706 CA PRO A 355 2936 2925 2959 177 -419 300 A C ATOM 2707 C PRO A 355 33.110 121.609 269.910 1.00 21.55 A C ANISOU 2707 C PRO A 355 2700 2729 2762 119 -329 250 A C ATOM 2708 O PRO A 355 31.935 121.284 270.101 1.00 19.00 A O ANISOU 2708 O PRO A 355 2412 2416 2393 143 -204 274 A O ATOM 2709 CB PRO A 355 34.807 119.799 269.958 1.00 22.42 A C ANISOU 2709 CB PRO A 355 2723 2796 2998 134 -346 354 A C ATOM 2710 CG PRO A 355 33.984 118.625 270.391 1.00 25.88 A C ANISOU 2710 CG PRO A 355 3205 3230 3398 178 -199 419 A C ATOM 2711 CD PRO A 355 33.711 118.864 271.852 1.00 25.88 A C ANISOU 2711 CD PRO A 355 3349 3254 3229 291 -240 447 A C ATOM 2712 N GLU A 356 33.490 122.510 269.010 1.00 20.26 A N ANISOU 2712 N GLU A 356 2465 2559 2675 50 -391 194 A N ATOM 2713 CA GLU A 356 32.518 123.173 268.153 1.00 21.95 A C ANISOU 2713 CA GLU A 356 2651 2787 2902 0 -324 151 A C ATOM 2714 C GLU A 356 32.088 122.200 267.064 1.00 17.91 A C ANISOU 2714 C GLU A 356 2064 2268 2474 -58 -206 171 A C ATOM 2715 O GLU A 356 32.854 121.315 266.669 1.00 21.26 A O ANISOU 2715 O GLU A 356 2444 2665 2970 -74 -188 200 A O ATOM 2716 CB GLU A 356 33.108 124.464 267.554 1.00 18.15 A C ANISOU 2716 CB GLU A 356 2127 2294 2476 -44 -422 97 A C ATOM 2717 CG GLU A 356 33.683 125.424 268.619 1.00 19.02 A C ANISOU 2717 CG GLU A 356 2315 2386 2527 2 -578 60 A C ATOM 2718 CD GLU A 356 34.154 126.768 268.063 1.00 24.92 A C ANISOU 2718 CD GLU A 356 3012 3101 3357 -46 -669 10 A C ATOM 2719 OE1 GLU A 356 34.066 126.986 266.832 1.00 20.83 A O ANISOU 2719 OE1 GLU A 356 2400 2583 2930 -104 -597 14 A O ATOM 2720 OE2 GLU A 356 34.648 127.598 268.864 1.00 22.82 A O1- ANISOU 2720 OE2 GLU A 356 2807 2799 3063 -22 -820 -34 A O1- ATOM 2721 N VAL A 357 30.854 122.337 266.600 1.00 19.37 A N ANISOU 2721 N VAL A 357 2238 2465 2654 -85 -133 158 A N ATOM 2722 CA VAL A 357 30.405 121.537 265.466 1.00 19.34 A C ANISOU 2722 CA VAL A 357 2178 2442 2728 -149 -64 155 A C ATOM 2723 C VAL A 357 29.997 122.503 264.368 1.00 20.70 A C ANISOU 2723 C VAL A 357 2320 2632 2914 -197 -89 105 A C ATOM 2724 O VAL A 357 29.064 123.266 264.547 1.00 16.55 A O ANISOU 2724 O VAL A 357 1798 2131 2359 -190 -87 98 A O ATOM 2725 CB VAL A 357 29.204 120.644 265.827 1.00 17.72 A C ANISOU 2725 CB VAL A 357 1969 2221 2543 -145 29 197 A C ATOM 2726 CG1 VAL A 357 28.659 119.950 264.582 1.00 15.27 A C ANISOU 2726 CG1 VAL A 357 1607 1876 2320 -224 56 171 A C ATOM 2727 CG2 VAL A 357 29.601 119.618 266.872 1.00 19.41 A C ANISOU 2727 CG2 VAL A 357 2219 2413 2744 -86 75 263 A C ATOM 2728 N ALA A 358 30.700 122.480 263.239 1.00 15.00 A N ANISOU 2728 N ALA A 358 1573 1892 2232 -232 -99 81 A N ATOM 2729 CA ALA A 358 30.481 123.472 262.196 1.00 15.01 A C ANISOU 2729 CA ALA A 358 1561 1910 2232 -259 -121 46 A C ATOM 2730 C ALA A 358 30.354 122.788 260.854 1.00 19.81 A C ANISOU 2730 C ALA A 358 2179 2493 2856 -294 -87 23 A C ATOM 2731 O ALA A 358 31.106 121.871 260.556 1.00 20.67 A O ANISOU 2731 O ALA A 358 2303 2560 2991 -289 -49 32 A O ATOM 2732 CB ALA A 358 31.649 124.451 262.146 1.00 13.87 A C ANISOU 2732 CB ALA A 358 1399 1760 2112 -242 -167 48 A C ATOM 2733 N TRP A 359 29.422 123.239 260.025 1.00 13.96 A N ANISOU 2733 N TRP A 359 1441 1770 2093 -320 -108 -5 A N ATOM 2734 CA TRP A 359 29.338 122.671 258.681 1.00 17.45 A C ANISOU 2734 CA TRP A 359 1929 2181 2518 -342 -103 -41 A C ATOM 2735 C TRP A 359 28.764 123.644 257.662 1.00 18.23 A C ANISOU 2735 C TRP A 359 2044 2311 2572 -346 -145 -62 A C ATOM 2736 O TRP A 359 28.063 124.599 258.015 1.00 24.24 A O ANISOU 2736 O TRP A 359 2761 3115 3336 -348 -178 -49 A O ATOM 2737 CB TRP A 359 28.559 121.350 258.674 1.00 17.02 A C ANISOU 2737 CB TRP A 359 1886 2084 2497 -382 -105 -61 A C ATOM 2738 CG TRP A 359 27.085 121.503 258.829 1.00 19.88 A C ANISOU 2738 CG TRP A 359 2196 2462 2894 -422 -156 -60 A C ATOM 2739 CD1 TRP A 359 26.149 121.417 257.843 1.00 20.70 A C ANISOU 2739 CD1 TRP A 359 2309 2552 3004 -465 -231 -100 A C ATOM 2740 CD2 TRP A 359 26.369 121.751 260.047 1.00 18.52 A C ANISOU 2740 CD2 TRP A 359 1955 2313 2767 -412 -132 -7 A C ATOM 2741 CE2 TRP A 359 25.001 121.807 259.719 1.00 20.61 A C ANISOU 2741 CE2 TRP A 359 2163 2574 3094 -454 -179 -3 A C ATOM 2742 CE3 TRP A 359 26.754 121.937 261.376 1.00 21.54 A C ANISOU 2742 CE3 TRP A 359 2331 2715 3139 -362 -79 40 A C ATOM 2743 NE1 TRP A 359 24.892 121.600 258.369 1.00 24.37 A N ANISOU 2743 NE1 TRP A 359 2682 3029 3548 -493 -259 -64 A N ATOM 2744 CZ2 TRP A 359 24.014 122.042 260.677 1.00 21.62 A C ANISOU 2744 CZ2 TRP A 359 2214 2712 3290 -441 -139 64 A C ATOM 2745 CZ3 TRP A 359 25.776 122.171 262.324 1.00 16.92 A C ANISOU 2745 CZ3 TRP A 359 1705 2142 2581 -340 -43 92 A C ATOM 2746 CH2 TRP A 359 24.419 122.217 261.971 1.00 17.18 A C ANISOU 2746 CH2 TRP A 359 1668 2167 2693 -377 -56 111 A C ATOM 2747 N VAL A 360 29.083 123.404 256.395 1.00 18.54 A N ANISOU 2747 N VAL A 360 2161 2323 2559 -334 -136 -90 A N ATOM 2748 CA VAL A 360 28.633 124.275 255.315 1.00 19.91 A C ANISOU 2748 CA VAL A 360 2374 2524 2666 -320 -175 -102 A C ATOM 2749 C VAL A 360 28.454 123.476 254.021 1.00 25.78 A C ANISOU 2749 C VAL A 360 3244 3225 3327 -314 -200 -157 A C ATOM 2750 O VAL A 360 29.192 122.514 253.763 1.00 19.21 A O ANISOU 2750 O VAL A 360 2484 2334 2480 -294 -140 -175 A O ATOM 2751 CB VAL A 360 29.606 125.470 255.116 1.00 16.37 A C ANISOU 2751 CB VAL A 360 1913 2091 2217 -267 -116 -54 A C ATOM 2752 CG1 VAL A 360 30.943 125.005 254.586 1.00 16.11 A C ANISOU 2752 CG1 VAL A 360 1933 2004 2185 -218 -16 -30 A C ATOM 2753 CG2 VAL A 360 29.000 126.532 254.203 1.00 15.09 A C ANISOU 2753 CG2 VAL A 360 1777 1964 1994 -246 -151 -47 A C ATOM 2754 N GLY A 361 27.476 123.882 253.212 1.00 27.07 A N ANISOU 2754 N GLY A 361 3442 3411 3431 -324 -297 -184 A N ATOM 2755 CA GLY A 361 27.138 123.153 252.003 1.00 22.51 A C ANISOU 2755 CA GLY A 361 3009 2788 2755 -319 -367 -254 A C ATOM 2756 C GLY A 361 26.386 121.867 252.290 1.00 22.84 A C ANISOU 2756 C GLY A 361 3040 2771 2867 -396 -452 -312 A C ATOM 2757 O GLY A 361 25.693 121.746 253.312 1.00 19.24 A O ANISOU 2757 O GLY A 361 2444 2328 2539 -456 -478 -285 A O ATOM 2758 N LEU A 362 26.505 120.902 251.382 1.00 22.56 A N ANISOU 2758 N LEU A 362 3161 2659 2751 -387 -488 -390 A N ATOM 2759 CA LEU A 362 25.788 119.643 251.537 1.00 25.15 A C ANISOU 2759 CA LEU A 362 3487 2906 3164 -467 -583 -454 A C ATOM 2760 C LEU A 362 26.387 118.780 252.638 1.00 25.22 A C ANISOU 2760 C LEU A 362 3423 2874 3287 -485 -461 -422 A C ATOM 2761 O LEU A 362 27.611 118.663 252.748 1.00 19.32 A O ANISOU 2761 O LEU A 362 2723 2118 2502 -421 -319 -394 A O ATOM 2762 CB LEU A 362 25.778 118.848 250.233 1.00 29.03 A C ANISOU 2762 CB LEU A 362 4199 3306 3524 -446 -669 -564 A C ATOM 2763 CG LEU A 362 24.958 119.418 249.079 1.00 35.15 A C ANISOU 2763 CG LEU A 362 5076 4101 4177 -435 -849 -616 A C ATOM 2764 CD1 LEU A 362 25.104 118.541 247.838 1.00 35.86 A C ANISOU 2764 CD1 LEU A 362 5437 4087 4102 -395 -929 -738 A C ATOM 2765 CD2 LEU A 362 23.501 119.590 249.472 1.00 38.14 A C ANISOU 2765 CD2 LEU A 362 5279 4499 4713 -541 -1033 -605 A C ATOM 2766 N THR A 363 25.518 118.187 253.453 1.00 21.70 A N ANISOU 2766 N THR A 363 2852 2399 2996 -566 -512 -410 A N ATOM 2767 CA THR A 363 25.927 117.108 254.350 1.00 23.91 A C ANISOU 2767 CA THR A 363 3091 2615 3379 -582 -415 -386 A C ATOM 2768 C THR A 363 25.916 115.788 253.571 1.00 28.30 A C ANISOU 2768 C THR A 363 3784 3040 3930 -609 -465 -484 A C ATOM 2769 O THR A 363 25.344 115.707 252.483 1.00 28.01 A O ANISOU 2769 O THR A 363 3856 2960 3827 -631 -610 -574 A O ATOM 2770 CB THR A 363 24.957 116.976 255.526 1.00 20.99 A C ANISOU 2770 CB THR A 363 2541 2252 3183 -643 -425 -318 A C ATOM 2771 CG2 THR A 363 24.863 118.295 256.314 1.00 21.91 A C ANISOU 2771 CG2 THR A 363 2550 2484 3290 -608 -379 -233 A C ATOM 2772 OG1 THR A 363 23.660 116.632 255.027 1.00 20.85 A O ANISOU 2772 OG1 THR A 363 2486 2176 3261 -726 -581 -360 A O ATOM 2773 N GLU A 364 26.532 114.752 254.131 1.00 30.40 A N ANISOU 2773 N GLU A 364 4369 3014 4167 -986 -612 -385 A N ATOM 2774 CA GLU A 364 26.512 113.433 253.501 1.00 31.59 A C ANISOU 2774 CA GLU A 364 4638 3081 4282 -1008 -641 -421 A C ATOM 2775 C GLU A 364 25.091 112.871 253.382 1.00 29.93 A C ANISOU 2775 C GLU A 364 4357 2877 4137 -1113 -698 -426 A C ATOM 2776 O GLU A 364 24.768 112.190 252.409 1.00 32.27 A O ANISOU 2776 O GLU A 364 4724 3135 4403 -1141 -764 -472 A O ATOM 2777 CB GLU A 364 27.446 112.448 254.215 1.00 30.73 A C ANISOU 2777 CB GLU A 364 4629 2885 4160 -976 -566 -409 A C ATOM 2778 CG GLU A 364 27.719 111.183 253.413 1.00 33.16 A C ANISOU 2778 CG GLU A 364 5077 3097 4426 -969 -591 -459 A C ATOM 2779 CD GLU A 364 28.722 110.256 254.080 1.00 39.76 A C ANISOU 2779 CD GLU A 364 6009 3840 5257 -920 -518 -440 A C ATOM 2780 OE1 GLU A 364 28.804 109.076 253.664 1.00 41.74 A O ANISOU 2780 OE1 GLU A 364 6356 3998 5505 -926 -532 -475 A O ATOM 2781 OE2 GLU A 364 29.456 110.717 254.984 1.00 38.81 A O1- ANISOU 2781 OE2 GLU A 364 5871 3740 5138 -872 -451 -393 A O1- ATOM 2782 N LYS A 365 24.259 113.131 254.389 1.00 26.72 A N ANISOU 2782 N LYS A 365 3814 2519 3820 -1171 -667 -381 A N ATOM 2783 CA LYS A 365 22.857 112.715 254.346 1.00 34.27 A C ANISOU 2783 CA LYS A 365 4682 3493 4848 -1270 -713 -379 A C ATOM 2784 C LYS A 365 22.198 113.269 253.078 1.00 31.47 A C ANISOU 2784 C LYS A 365 4297 3190 4471 -1278 -816 -413 A C ATOM 2785 O LYS A 365 21.557 112.539 252.288 1.00 30.69 A O ANISOU 2785 O LYS A 365 4232 3061 4367 -1336 -890 -449 A O ATOM 2786 CB LYS A 365 22.111 113.260 255.568 1.00 34.95 A C ANISOU 2786 CB LYS A 365 4604 3652 5021 -1312 -655 -326 A C ATOM 2787 CG LYS A 365 22.611 112.770 256.917 1.00 36.58 A C ANISOU 2787 CG LYS A 365 4825 3828 5247 -1319 -558 -278 A C ATOM 2788 CD LYS A 365 21.877 113.492 258.048 1.00 38.73 A C ANISOU 2788 CD LYS A 365 4928 4196 5591 -1355 -499 -234 A C ATOM 2789 CE LYS A 365 22.356 113.016 259.413 1.00 42.88 A C ANISOU 2789 CE LYS A 365 5469 4705 6119 -1372 -406 -175 A C ATOM 2790 NZ LYS A 365 21.579 113.621 260.531 1.00 41.72 A N1+ ANISOU 2790 NZ LYS A 365 5157 4663 6033 -1414 -341 -135 A N1+ ATOM 2791 N GLU A 366 22.373 114.577 252.898 1.00 25.88 A N ANISOU 2791 N GLU A 366 3524 2558 3752 -1222 -826 -399 A N ATOM 2792 CA GLU A 366 21.799 115.278 251.761 1.00 24.98 A C ANISOU 2792 CA GLU A 366 3372 2501 3619 -1221 -927 -411 A C ATOM 2793 C GLU A 366 22.392 114.770 250.466 1.00 24.22 A C ANISOU 2793 C GLU A 366 3437 2356 3410 -1198 -994 -463 A C ATOM 2794 O GLU A 366 21.670 114.580 249.490 1.00 27.60 A O ANISOU 2794 O GLU A 366 3870 2801 3815 -1241 -1091 -489 A O ATOM 2795 CB GLU A 366 22.011 116.797 251.885 1.00 22.36 A C ANISOU 2795 CB GLU A 366 2945 2245 3307 -1156 -919 -376 A C ATOM 2796 CG GLU A 366 21.250 117.432 253.039 1.00 35.54 A C ANISOU 2796 CG GLU A 366 4438 3979 5088 -1174 -860 -339 A C ATOM 2797 CD GLU A 366 21.739 118.831 253.369 1.00 41.87 A C ANISOU 2797 CD GLU A 366 5164 4829 5917 -1095 -828 -314 A C ATOM 2798 OE1 GLU A 366 22.800 119.237 252.844 1.00 38.68 A O ANISOU 2798 OE1 GLU A 366 4849 4398 5448 -1030 -841 -318 A O ATOM 2799 OE2 GLU A 366 21.046 119.538 254.130 1.00 46.60 A O1- ANISOU 2799 OE2 GLU A 366 5611 5492 6605 -1097 -790 -292 A O1- ATOM 2800 N ALA A 367 23.698 114.514 250.462 1.00 24.80 A N ANISOU 2800 N ALA A 367 3642 2372 3408 -1129 -940 -481 A N ATOM 2801 CA ALA A 367 24.343 114.038 249.240 1.00 27.07 A C ANISOU 2801 CA ALA A 367 4090 2619 3578 -1095 -987 -537 A C ATOM 2802 C ALA A 367 23.782 112.681 248.822 1.00 31.60 A C ANISOU 2802 C ALA A 367 4728 3127 4150 -1164 -1028 -590 A C ATOM 2803 O ALA A 367 23.482 112.466 247.640 1.00 30.82 A O ANISOU 2803 O ALA A 367 4691 3037 3983 -1183 -1117 -640 A O ATOM 2804 CB ALA A 367 25.851 113.965 249.414 1.00 27.92 A C ANISOU 2804 CB ALA A 367 4317 2677 3615 -1002 -905 -547 A C ATOM 2805 N LYS A 368 23.633 111.770 249.781 1.00 33.52 A N ANISOU 2805 N LYS A 368 4961 3306 4469 -1205 -968 -580 A N ATOM 2806 CA LYS A 368 23.050 110.465 249.469 1.00 37.65 A C ANISOU 2806 CA LYS A 368 5537 3754 5013 -1280 -1008 -627 A C ATOM 2807 C LYS A 368 21.606 110.594 248.998 1.00 34.94 A C ANISOU 2807 C LYS A 368 5088 3469 4718 -1375 -1106 -632 A C ATOM 2808 O LYS A 368 21.226 109.938 248.026 1.00 33.10 A O ANISOU 2808 O LYS A 368 4921 3208 4447 -1418 -1187 -695 A O ATOM 2809 CB LYS A 368 23.288 109.389 250.543 1.00 46.30 A C ANISOU 2809 CB LYS A 368 6661 4752 6178 -1303 -928 -606 A C ATOM 2810 CG LYS A 368 22.836 109.701 251.949 1.00 54.17 A C ANISOU 2810 CG LYS A 368 7523 5783 7275 -1340 -861 -526 A C ATOM 2811 CD LYS A 368 23.648 108.870 252.948 1.00 57.01 A C ANISOU 2811 CD LYS A 368 7952 6052 7657 -1317 -771 -494 A C ATOM 2812 CE LYS A 368 23.964 107.486 252.392 1.00 57.46 A C ANISOU 2812 CE LYS A 368 8152 5982 7699 -1326 -791 -550 A C ATOM 2813 NZ LYS A 368 24.837 106.676 253.287 1.00 60.07 A N1+ ANISOU 2813 NZ LYS A 368 8557 6216 8052 -1290 -710 -513 A N1+ ATOM 2814 N GLU A 369 20.790 111.414 249.667 1.00 27.90 A N ANISOU 2814 N GLU A 369 4031 2659 3910 -1406 -1098 -571 A N ATOM 2815 CA GLU A 369 19.432 111.586 249.128 1.00 35.28 A C ANISOU 2815 CA GLU A 369 4860 3656 4889 -1486 -1196 -574 A C ATOM 2816 C GLU A 369 19.400 112.194 247.713 1.00 40.19 A C ANISOU 2816 C GLU A 369 5522 4335 5414 -1459 -1306 -606 A C ATOM 2817 O GLU A 369 18.560 111.803 246.896 1.00 43.96 A O ANISOU 2817 O GLU A 369 5994 4825 5885 -1526 -1406 -643 A O ATOM 2818 CB GLU A 369 18.508 112.410 250.039 1.00 37.91 A C ANISOU 2818 CB GLU A 369 4999 4076 5331 -1515 -1166 -507 A C ATOM 2819 CG GLU A 369 17.080 112.496 249.461 1.00 43.22 A C ANISOU 2819 CG GLU A 369 5558 4810 6054 -1596 -1268 -510 A C ATOM 2820 CD GLU A 369 16.066 113.126 250.386 1.00 52.02 A C ANISOU 2820 CD GLU A 369 6477 6004 7285 -1630 -1229 -452 A C ATOM 2821 OE1 GLU A 369 16.257 113.039 251.618 1.00 60.67 A O ANISOU 2821 OE1 GLU A 369 7530 7086 8434 -1628 -1119 -418 A O ATOM 2822 OE2 GLU A 369 15.104 113.754 249.873 1.00 49.12 A O1- ANISOU 2822 OE2 GLU A 369 5995 5717 6950 -1651 -1309 -438 A O1- ATOM 2823 N LYS A 370 20.335 113.093 247.399 1.00 31.38 A N ANISOU 2823 N LYS A 370 4453 3252 4220 -1366 -1292 -592 A N ATOM 2824 CA LYS A 370 20.341 113.724 246.081 1.00 28.91 A C ANISOU 2824 CA LYS A 370 4179 2999 3806 -1339 -1396 -608 A C ATOM 2825 C LYS A 370 20.742 112.737 244.995 1.00 33.85 A C ANISOU 2825 C LYS A 370 4977 3570 4314 -1345 -1445 -696 A C ATOM 2826 O LYS A 370 20.402 112.917 243.827 1.00 36.85 A O ANISOU 2826 O LYS A 370 5388 4000 4611 -1357 -1551 -724 A O ATOM 2827 CB LYS A 370 21.342 114.888 246.060 1.00 27.39 A C ANISOU 2827 CB LYS A 370 4004 2845 3559 -1240 -1361 -567 A C ATOM 2828 CG LYS A 370 21.010 115.998 245.059 1.00 30.01 A C ANISOU 2828 CG LYS A 370 4292 3270 3840 -1220 -1468 -533 A C ATOM 2829 CD LYS A 370 22.064 117.111 245.099 1.00 30.92 A C ANISOU 2829 CD LYS A 370 4426 3409 3911 -1127 -1431 -488 A C ATOM 2830 CE LYS A 370 21.632 118.315 244.274 1.00 35.89 A C ANISOU 2830 CE LYS A 370 4984 4132 4522 -1109 -1538 -429 A C ATOM 2831 NZ LYS A 370 22.740 119.311 244.118 1.00 40.44 A N1+ ANISOU 2831 NZ LYS A 370 5603 4723 5039 -1025 -1517 -388 A N1+ ATOM 2832 N GLY A 371 21.449 111.685 245.386 1.00 38.43 A N ANISOU 2832 N GLY A 371 5666 4047 4887 -1333 -1368 -740 A N ATOM 2833 CA GLY A 371 21.828 110.625 244.468 1.00 42.91 A C ANISOU 2833 CA GLY A 371 6394 4548 5362 -1335 -1399 -835 A C ATOM 2834 C GLY A 371 22.946 110.935 243.488 1.00 45.17 A C ANISOU 2834 C GLY A 371 6823 4852 5489 -1240 -1397 -875 A C ATOM 2835 O GLY A 371 23.100 110.232 242.487 1.00 48.11 A O ANISOU 2835 O GLY A 371 7317 5200 5764 -1241 -1441 -962 A O ATOM 2836 N ILE A 372 23.754 111.945 243.796 1.00 44.72 A N ANISOU 2836 N ILE A 372 6754 4836 5403 -1157 -1339 -817 A N ATOM 2837 CA ILE A 372 24.902 112.305 242.966 1.00 43.75 A C ANISOU 2837 CA ILE A 372 6761 4734 5127 -1061 -1319 -844 A C ATOM 2838 C ILE A 372 26.097 111.468 243.393 1.00 43.77 A C ANISOU 2838 C ILE A 372 6880 4638 5112 -991 -1201 -885 A C ATOM 2839 O ILE A 372 26.206 111.091 244.556 1.00 44.23 A O ANISOU 2839 O ILE A 372 6893 4633 5280 -998 -1126 -853 A O ATOM 2840 CB ILE A 372 25.260 113.816 243.020 1.00 66.60 A C ANISOU 2840 CB ILE A 372 9591 7716 7997 -1006 -1317 -762 A C ATOM 2841 CG1 ILE A 372 25.784 114.231 244.400 1.00 60.76 A C ANISOU 2841 CG1 ILE A 372 8779 6945 7363 -971 -1211 -701 A C ATOM 2842 CG2 ILE A 372 24.091 114.671 242.535 1.00 69.62 A C ANISOU 2842 CG2 ILE A 372 9853 8197 8403 -1064 -1441 -713 A C ATOM 2843 CD1 ILE A 372 27.262 114.593 244.392 1.00 53.30 A C ANISOU 2843 CD1 ILE A 372 7935 5987 6330 -862 -1122 -700 A C ATOM 2844 N SER A 373 26.997 111.172 242.464 1.00 48.21 A N ANISOU 2844 N SER A 373 7590 5193 5536 -918 -1180 -950 A N ATOM 2845 CA SER A 373 28.195 110.437 242.829 1.00 44.95 A C ANISOU 2845 CA SER A 373 7278 4692 5110 -834 -1064 -984 A C ATOM 2846 C SER A 373 29.096 111.357 243.629 1.00 36.92 A C ANISOU 2846 C SER A 373 6222 3697 4109 -756 -973 -906 A C ATOM 2847 O SER A 373 29.616 112.337 243.095 1.00 40.71 A O ANISOU 2847 O SER A 373 6722 4254 4492 -697 -971 -883 A O ATOM 2848 CB SER A 373 28.945 109.994 241.574 1.00 45.09 A C ANISOU 2848 CB SER A 373 7451 4714 4969 -764 -1054 -1076 A C ATOM 2849 OG SER A 373 28.257 108.966 240.891 1.00 55.01 A O ANISOU 2849 OG SER A 373 8759 5930 6213 -832 -1126 -1168 A O ATOM 2850 N TYR A 374 29.256 111.046 244.918 1.00 29.59 A N ANISOU 2850 N TYR A 374 5237 2705 3302 -759 -901 -863 A N ATOM 2851 CA TYR A 374 30.045 111.877 245.826 1.00 25.96 A C ANISOU 2851 CA TYR A 374 4727 2262 2874 -694 -817 -792 A C ATOM 2852 C TYR A 374 31.080 111.010 246.540 1.00 32.07 A C ANISOU 2852 C TYR A 374 5563 2945 3676 -623 -707 -798 A C ATOM 2853 O TYR A 374 30.947 109.783 246.609 1.00 25.46 A O ANISOU 2853 O TYR A 374 4777 2022 2875 -646 -703 -840 A O ATOM 2854 CB TYR A 374 29.154 112.518 246.893 1.00 25.57 A C ANISOU 2854 CB TYR A 374 4515 2247 2955 -769 -837 -716 A C ATOM 2855 CG TYR A 374 28.667 111.544 247.952 1.00 29.46 A C ANISOU 2855 CG TYR A 374 4961 2667 3566 -829 -806 -702 A C ATOM 2856 CD1 TYR A 374 29.342 111.413 249.164 1.00 27.66 A C ANISOU 2856 CD1 TYR A 374 4712 2399 3397 -790 -710 -655 A C ATOM 2857 CD2 TYR A 374 27.538 110.759 247.746 1.00 30.16 A C ANISOU 2857 CD2 TYR A 374 5026 2729 3703 -927 -875 -731 A C ATOM 2858 CE1 TYR A 374 28.909 110.530 250.136 1.00 28.52 A C ANISOU 2858 CE1 TYR A 374 4787 2446 3604 -847 -685 -631 A C ATOM 2859 CE2 TYR A 374 27.097 109.870 248.719 1.00 31.95 A C ANISOU 2859 CE2 TYR A 374 5214 2887 4037 -985 -845 -710 A C ATOM 2860 CZ TYR A 374 27.790 109.766 249.912 1.00 28.95 A C ANISOU 2860 CZ TYR A 374 4821 2471 3707 -945 -750 -657 A C ATOM 2861 OH TYR A 374 27.371 108.891 250.887 1.00 34.87 A O ANISOU 2861 OH TYR A 374 5540 3155 4555 -1005 -721 -625 A O ATOM 2862 N GLU A 375 32.109 111.655 247.076 1.00 31.93 A N ANISOU 2862 N GLU A 375 5538 2943 3649 -538 -623 -754 A N ATOM 2863 CA GLU A 375 33.102 110.979 247.903 1.00 30.60 A C ANISOU 2863 CA GLU A 375 5404 2701 3520 -465 -521 -739 A C ATOM 2864 C GLU A 375 33.494 111.869 249.069 1.00 28.94 A C ANISOU 2864 C GLU A 375 5100 2524 3373 -442 -464 -659 A C ATOM 2865 O GLU A 375 33.689 113.074 248.885 1.00 25.15 A O ANISOU 2865 O GLU A 375 4582 2116 2859 -419 -467 -635 A O ATOM 2866 CB GLU A 375 34.317 110.600 247.058 1.00 34.21 A C ANISOU 2866 CB GLU A 375 5986 3141 3870 -347 -458 -793 A C ATOM 2867 CG GLU A 375 35.433 109.874 247.799 1.00 38.12 A C ANISOU 2867 CG GLU A 375 6514 3564 4407 -256 -355 -777 A C ATOM 2868 CD GLU A 375 36.562 109.476 246.859 1.00 41.31 A C ANISOU 2868 CD GLU A 375 7026 3960 4710 -136 -291 -835 A C ATOM 2869 OE1 GLU A 375 37.709 109.308 247.324 1.00 36.21 A O ANISOU 2869 OE1 GLU A 375 6388 3292 4078 -33 -197 -808 A O ATOM 2870 OE2 GLU A 375 36.298 109.346 245.643 1.00 46.79 A O1- ANISOU 2870 OE2 GLU A 375 7791 4680 5309 -145 -335 -907 A O1- ATOM 2871 N THR A 376 33.587 111.292 250.267 1.00 23.35 A N ANISOU 2871 N THR A 376 4355 1761 2754 -453 -418 -618 A N ATOM 2872 CA THR A 376 34.019 112.059 251.426 1.00 23.88 A C ANISOU 2872 CA THR A 376 4340 1861 2873 -430 -361 -548 A C ATOM 2873 C THR A 376 35.506 111.862 251.656 1.00 21.54 A C ANISOU 2873 C THR A 376 4106 1534 2544 -303 -266 -537 A C ATOM 2874 O THR A 376 36.078 110.846 251.267 1.00 23.39 A O ANISOU 2874 O THR A 376 4432 1705 2752 -246 -238 -572 A O ATOM 2875 CB THR A 376 33.268 111.659 252.715 1.00 26.52 A C ANISOU 2875 CB THR A 376 4592 2172 3313 -516 -362 -496 A C ATOM 2876 CG2 THR A 376 31.765 111.795 252.526 1.00 25.34 A C ANISOU 2876 CG2 THR A 376 4362 2058 3209 -636 -446 -502 A C ATOM 2877 OG1 THR A 376 33.582 110.302 253.049 1.00 30.08 A O ANISOU 2877 OG1 THR A 376 5116 2525 3788 -502 -332 -497 A O ATOM 2878 N ALA A 377 36.122 112.836 252.310 1.00 22.92 A N ANISOU 2878 N ALA A 377 4169 1801 2739 -247 -208 -472 A N ATOM 2879 CA ALA A 377 37.519 112.733 252.704 1.00 24.88 A C ANISOU 2879 CA ALA A 377 4428 2049 2976 -129 -118 -441 A C ATOM 2880 C ALA A 377 37.647 113.347 254.084 1.00 26.18 A C ANISOU 2880 C ALA A 377 4461 2277 3210 -136 -84 -365 A C ATOM 2881 O ALA A 377 37.271 114.511 254.297 1.00 21.79 A O ANISOU 2881 O ALA A 377 3788 1816 2676 -166 -97 -339 A O ATOM 2882 CB ALA A 377 38.413 113.459 251.712 1.00 19.21 A C ANISOU 2882 CB ALA A 377 3716 1402 2181 -34 -79 -451 A C ATOM 2883 N THR A 378 38.171 112.575 255.030 1.00 24.98 A N ANISOU 2883 N THR A 378 4329 2072 3091 -108 -43 -329 A N ATOM 2884 CA THR A 378 38.275 113.073 256.401 1.00 26.34 A C ANISOU 2884 CA THR A 378 4385 2311 3311 -119 -16 -260 A C ATOM 2885 C THR A 378 39.709 113.076 256.924 1.00 26.04 A C ANISOU 2885 C THR A 378 4331 2297 3265 -6 51 -216 A C ATOM 2886 O THR A 378 40.526 112.244 256.540 1.00 28.48 A O ANISOU 2886 O THR A 378 4732 2533 3554 75 81 -225 A O ATOM 2887 CB THR A 378 37.367 112.287 257.372 1.00 26.64 A C ANISOU 2887 CB THR A 378 4425 2296 3399 -215 -39 -230 A C ATOM 2888 CG2 THR A 378 35.939 112.246 256.856 1.00 25.14 A C ANISOU 2888 CG2 THR A 378 4238 2085 3228 -333 -109 -271 A C ATOM 2889 OG1 THR A 378 37.847 110.945 257.490 1.00 36.95 A O ANISOU 2889 OG1 THR A 378 5846 3481 4711 -181 -23 -220 A O ATOM 2890 N PHE A 379 40.008 114.043 257.784 1.00 25.00 A N ANISOU 2890 N PHE A 379 4077 2268 3153 2 71 -174 A N ATOM 2891 CA PHE A 379 41.272 114.080 258.496 1.00 22.49 A C ANISOU 2891 CA PHE A 379 3722 1986 2836 91 120 -124 A C ATOM 2892 C PHE A 379 40.985 114.089 259.991 1.00 21.48 A C ANISOU 2892 C PHE A 379 3525 1902 2735 41 117 -72 A C ATOM 2893 O PHE A 379 40.366 115.032 260.507 1.00 23.01 A O ANISOU 2893 O PHE A 379 3621 2178 2943 -20 103 -77 A O ATOM 2894 CB PHE A 379 42.085 115.315 258.104 1.00 17.40 A C ANISOU 2894 CB PHE A 379 2993 1436 2183 149 145 -125 A C ATOM 2895 CG PHE A 379 43.463 115.337 258.695 1.00 23.05 A C ANISOU 2895 CG PHE A 379 3664 2190 2903 242 189 -77 A C ATOM 2896 CD1 PHE A 379 43.722 116.019 259.871 1.00 22.82 A C ANISOU 2896 CD1 PHE A 379 3526 2246 2897 228 188 -41 A C ATOM 2897 CD2 PHE A 379 44.503 114.671 258.070 1.00 19.44 A C ANISOU 2897 CD2 PHE A 379 3272 1687 2427 346 231 -73 A C ATOM 2898 CE1 PHE A 379 44.997 116.031 260.414 1.00 21.73 A C ANISOU 2898 CE1 PHE A 379 3342 2151 2765 309 216 4 A C ATOM 2899 CE2 PHE A 379 45.782 114.678 258.610 1.00 20.35 A C ANISOU 2899 CE2 PHE A 379 3333 1843 2555 435 269 -23 A C ATOM 2900 CZ PHE A 379 46.027 115.360 259.784 1.00 19.53 A C ANISOU 2900 CZ PHE A 379 3116 1827 2476 412 255 18 A C ATOM 2901 N PRO A 380 41.433 113.036 260.690 1.00 19.62 A N ANISOU 2901 N PRO A 380 3340 1611 2502 72 131 -21 A N ATOM 2902 CA PRO A 380 41.244 112.893 262.136 1.00 16.94 A C ANISOU 2902 CA PRO A 380 2950 1318 2169 31 132 43 A C ATOM 2903 C PRO A 380 42.258 113.754 262.891 1.00 21.66 A C ANISOU 2903 C PRO A 380 3445 2032 2753 91 151 73 A C ATOM 2904 O PRO A 380 43.432 113.787 262.510 1.00 23.63 A O ANISOU 2904 O PRO A 380 3695 2283 2999 189 172 81 A O ATOM 2905 CB PRO A 380 41.511 111.401 262.371 1.00 19.47 A C ANISOU 2905 CB PRO A 380 3379 1520 2501 59 137 95 A C ATOM 2906 CG PRO A 380 42.503 111.032 261.313 1.00 21.43 A C ANISOU 2906 CG PRO A 380 3697 1698 2746 171 158 65 A C ATOM 2907 CD PRO A 380 42.173 111.899 260.108 1.00 19.32 A C ANISOU 2907 CD PRO A 380 3418 1462 2462 156 151 -19 A C ATOM 2908 N TRP A 381 41.816 114.457 263.931 1.00 17.46 A N ANISOU 2908 N TRP A 381 2822 1601 2213 32 144 83 A N ATOM 2909 CA TRP A 381 42.710 115.364 264.646 1.00 19.57 A C ANISOU 2909 CA TRP A 381 2989 1981 2466 75 151 94 A C ATOM 2910 C TRP A 381 43.725 114.617 265.519 1.00 20.37 A C ANISOU 2910 C TRP A 381 3103 2093 2544 140 157 174 A C ATOM 2911 O TRP A 381 44.707 115.208 265.981 1.00 16.54 A O ANISOU 2911 O TRP A 381 2544 1693 2049 192 155 188 A O ATOM 2912 CB TRP A 381 41.909 116.388 265.467 1.00 19.99 A C ANISOU 2912 CB TRP A 381 2944 2137 2513 -5 143 61 A C ATOM 2913 CG TRP A 381 41.233 117.440 264.622 1.00 22.96 A C ANISOU 2913 CG TRP A 381 3275 2521 2926 -41 134 -14 A C ATOM 2914 CD1 TRP A 381 40.932 117.357 263.289 1.00 24.70 A C ANISOU 2914 CD1 TRP A 381 3549 2665 3169 -37 126 -44 A C ATOM 2915 CD2 TRP A 381 40.774 118.729 265.054 1.00 18.69 A C ANISOU 2915 CD2 TRP A 381 2630 2067 2405 -82 130 -65 A C ATOM 2916 CE2 TRP A 381 40.215 119.376 263.930 1.00 19.41 A C ANISOU 2916 CE2 TRP A 381 2712 2123 2540 -98 117 -112 A C ATOM 2917 CE3 TRP A 381 40.787 119.403 266.282 1.00 15.05 A C ANISOU 2917 CE3 TRP A 381 2085 1707 1925 -104 134 -80 A C ATOM 2918 NE1 TRP A 381 40.322 118.516 262.866 1.00 20.08 A N ANISOU 2918 NE1 TRP A 381 2896 2118 2618 -73 112 -96 A N ATOM 2919 CZ2 TRP A 381 39.668 120.663 263.998 1.00 16.20 A C ANISOU 2919 CZ2 TRP A 381 2212 1768 2176 -131 108 -166 A C ATOM 2920 CZ3 TRP A 381 40.241 120.684 266.347 1.00 17.49 A C ANISOU 2920 CZ3 TRP A 381 2305 2066 2273 -137 130 -150 A C ATOM 2921 CH2 TRP A 381 39.689 121.296 265.212 1.00 17.26 A C ANISOU 2921 CH2 TRP A 381 2266 1989 2304 -148 118 -188 A C ATOM 2922 N ALA A 382 43.523 113.312 265.699 1.00 22.70 A N ANISOU 2922 N ALA A 382 3491 2296 2837 139 157 231 A N ATOM 2923 CA ALA A 382 44.520 112.491 266.378 1.00 23.30 A C ANISOU 2923 CA ALA A 382 3590 2362 2902 216 158 320 A C ATOM 2924 C ALA A 382 45.827 112.508 265.593 1.00 22.99 A C ANISOU 2924 C ALA A 382 3549 2298 2887 338 174 313 A C ATOM 2925 O ALA A 382 46.897 112.260 266.147 1.00 28.69 A O ANISOU 2925 O ALA A 382 4242 3054 3606 417 171 378 A O ATOM 2926 CB ALA A 382 44.023 111.059 266.529 1.00 25.14 A C ANISOU 2926 CB ALA A 382 3934 2469 3149 194 156 382 A C ATOM 2927 N ALA A 383 45.737 112.822 264.305 1.00 19.21 A N ANISOU 2927 N ALA A 383 3097 1773 2430 352 191 240 A N ATOM 2928 CA ALA A 383 46.913 112.900 263.447 1.00 22.71 A C ANISOU 2928 CA ALA A 383 3535 2204 2890 464 221 228 A C ATOM 2929 C ALA A 383 47.418 114.334 263.298 1.00 24.10 A C ANISOU 2929 C ALA A 383 3591 2499 3068 468 225 196 A C ATOM 2930 O ALA A 383 48.371 114.587 262.560 1.00 29.83 A O ANISOU 2930 O ALA A 383 4292 3233 3808 549 256 189 A O ATOM 2931 CB ALA A 383 46.594 112.312 262.076 1.00 18.28 A C ANISOU 2931 CB ALA A 383 3086 1524 2338 484 243 171 A C ATOM 2932 N SER A 384 46.783 115.270 263.997 1.00 23.25 A N ANISOU 2932 N SER A 384 3406 2477 2949 380 198 175 A N ATOM 2933 CA SER A 384 47.167 116.679 263.897 1.00 21.69 A C ANISOU 2933 CA SER A 384 3098 2376 2768 372 196 138 A C ATOM 2934 C SER A 384 48.140 117.084 264.990 1.00 21.18 A C ANISOU 2934 C SER A 384 2934 2412 2699 400 177 179 A C ATOM 2935 O SER A 384 47.807 117.035 266.177 1.00 21.93 A O ANISOU 2935 O SER A 384 3008 2563 2761 354 148 197 A O ATOM 2936 CB SER A 384 45.933 117.573 263.981 1.00 21.22 A C ANISOU 2936 CB SER A 384 3005 2345 2711 268 176 78 A C ATOM 2937 OG SER A 384 46.320 118.921 264.190 1.00 22.62 A O ANISOU 2937 OG SER A 384 3071 2610 2914 256 167 49 A O ATOM 2938 N GLY A 385 49.335 117.501 264.583 1.00 23.54 A N ANISOU 2938 N GLY A 385 3171 2745 3029 472 192 192 A N ATOM 2939 CA GLY A 385 50.330 117.997 265.518 1.00 22.93 A C ANISOU 2939 CA GLY A 385 2985 2770 2956 494 164 224 A C ATOM 2940 C GLY A 385 49.815 119.125 266.393 1.00 21.34 A C ANISOU 2940 C GLY A 385 2705 2658 2745 402 124 173 A C ATOM 2941 O GLY A 385 50.082 119.162 267.594 1.00 25.55 A O ANISOU 2941 O GLY A 385 3193 3273 3244 388 85 194 A O ATOM 2942 N AARG A 386 49.099 120.070 265.786 0.50 19.91 A N ANISOU 2942 N AARG A 386 2507 2464 2593 344 132 105 A N ATOM 2943 N BARG A 386 49.064 120.046 265.795 0.15 20.22 A N ANISOU 2943 N BARG A 386 2550 2502 2631 343 132 104 A N ATOM 2944 N CARG A 386 49.055 120.036 265.790 0.35 19.77 A N ANISOU 2944 N CARG A 386 2493 2444 2574 343 133 104 A N ATOM 2945 CA AARG A 386 48.548 121.196 266.534 0.50 20.15 A C ANISOU 2945 CA AARG A 386 2466 2563 2628 264 102 41 A C ATOM 2946 CA BARG A 386 48.540 121.187 266.535 0.15 20.04 A C ANISOU 2946 CA BARG A 386 2452 2549 2613 264 102 41 A C ATOM 2947 CA CARG A 386 48.528 121.192 266.505 0.35 20.12 A C ANISOU 2947 CA CARG A 386 2463 2556 2624 264 102 40 A C ATOM 2948 C AARG A 386 47.493 120.761 267.552 0.50 20.25 A C ANISOU 2948 C AARG A 386 2517 2598 2578 204 88 30 A C ATOM 2949 C BARG A 386 47.495 120.756 267.552 0.15 20.21 A C ANISOU 2949 C BARG A 386 2513 2594 2574 204 88 30 A C ATOM 2950 C CARG A 386 47.475 120.786 267.530 0.35 20.21 A C ANISOU 2950 C CARG A 386 2512 2592 2575 202 88 28 A C ATOM 2951 O AARG A 386 47.499 121.219 268.700 0.50 20.52 A O ANISOU 2951 O AARG A 386 2496 2722 2578 168 59 7 A O ATOM 2952 O BARG A 386 47.517 121.197 268.702 0.15 20.50 A O ANISOU 2952 O BARG A 386 2495 2721 2576 169 59 8 A O ATOM 2953 O CARG A 386 47.474 121.272 268.665 0.35 20.38 A O ANISOU 2953 O CARG A 386 2477 2704 2564 166 59 3 A O ATOM 2954 CB AARG A 386 47.961 122.262 265.602 0.50 19.76 A C ANISOU 2954 CB AARG A 386 2392 2479 2637 223 114 -20 A C ATOM 2955 CB BARG A 386 47.932 122.219 265.586 0.15 19.92 A C ANISOU 2955 CB BARG A 386 2416 2497 2655 224 114 -19 A C ATOM 2956 CB CARG A 386 47.932 122.193 265.513 0.35 18.77 A C ANISOU 2956 CB CARG A 386 2274 2346 2510 226 116 -18 A C ATOM 2957 CG AARG A 386 47.494 123.493 266.367 0.50 21.80 A C ANISOU 2957 CG AARG A 386 2568 2796 2917 153 84 -94 A C ATOM 2958 CG BARG A 386 47.511 123.499 266.284 0.15 21.23 A C ANISOU 2958 CG BARG A 386 2497 2719 2848 155 85 -92 A C ATOM 2959 CG CARG A 386 47.309 123.420 266.160 0.35 20.87 A C ANISOU 2959 CG CARG A 386 2467 2662 2802 152 90 -94 A C ATOM 2960 CD AARG A 386 48.692 124.265 266.910 0.50 22.47 A C ANISOU 2960 CD AARG A 386 2552 2953 3034 166 55 -98 A C ATOM 2961 CD BARG A 386 48.726 124.235 266.831 0.15 22.88 A C ANISOU 2961 CD BARG A 386 2606 3001 3087 170 57 -94 A C ATOM 2962 CD CARG A 386 48.313 124.198 267.002 0.35 22.22 A C ANISOU 2962 CD CARG A 386 2537 2917 2991 152 56 -109 A C ATOM 2963 NE AARG A 386 48.317 125.494 267.610 0.50 24.94 A N ANISOU 2963 NE AARG A 386 2790 3310 3376 102 24 -185 A N ATOM 2964 NE BARG A 386 48.350 125.402 267.622 0.15 23.88 A N ANISOU 2964 NE BARG A 386 2660 3177 3237 105 25 -179 A N ATOM 2965 NE CARG A 386 48.039 125.633 266.954 0.35 25.08 A N ANISOU 2965 NE CARG A 386 2822 3283 3423 101 40 -185 A N ATOM 2966 CZ AARG A 386 47.953 126.639 267.032 0.50 24.03 A C ANISOU 2966 CZ AARG A 386 2632 3156 3344 68 25 -238 A C ATOM 2967 CZ BARG A 386 47.950 126.558 267.102 0.15 23.50 A C ANISOU 2967 CZ BARG A 386 2568 3092 3269 69 25 -236 A C ATOM 2968 CZ CARG A 386 48.296 126.488 267.941 0.35 24.82 A C ANISOU 2968 CZ CARG A 386 2712 3318 3402 65 2 -246 A C ATOM 2969 NH1AARG A 386 47.882 126.755 265.710 0.50 20.84 A N1+ ANISOU 2969 NH1AARG A 386 2251 2678 2991 88 54 -206 A N1+ ATOM 2970 NH1BARG A 386 47.861 126.705 265.785 0.15 22.59 A N1+ ANISOU 2970 NH1BARG A 386 2475 2903 3207 87 53 -207 A N1+ ATOM 2971 NH1CARG A 386 48.830 126.059 269.080 0.35 13.75 A N1+ ANISOU 2971 NH1CARG A 386 1295 2001 1929 71 -28 -235 A N1+ ATOM 2972 NH2AARG A 386 47.644 127.681 267.793 0.50 22.97 A N ANISOU 2972 NH2AARG A 386 2435 3055 3239 17 -3 -325 A N ATOM 2973 NH2BARG A 386 47.629 127.568 267.898 0.15 23.68 A N ANISOU 2973 NH2BARG A 386 2529 3151 3316 17 -3 -323 A N ATOM 2974 NH2CARG A 386 48.008 127.776 267.792 0.35 22.84 A N ANISOU 2974 NH2CARG A 386 2401 3046 3233 23 -9 -318 A N ATOM 2975 N ALA A 387 46.581 119.900 267.122 1.00 13.51 A N ANISOU 2975 N ALA A 387 1759 1667 1709 187 109 44 A N ATOM 2976 CA ALA A 387 45.504 119.440 267.983 1.00 13.71 A C ANISOU 2976 CA ALA A 387 1819 1709 1683 123 106 45 A C ATOM 2977 C ALA A 387 46.050 118.675 269.176 1.00 15.58 A C ANISOU 2977 C ALA A 387 2063 2003 1853 144 89 117 A C ATOM 2978 O ALA A 387 45.561 118.827 270.302 1.00 20.50 A O ANISOU 2978 O ALA A 387 2661 2709 2418 92 79 109 A O ATOM 2979 CB ALA A 387 44.543 118.575 267.203 1.00 17.73 A C ANISOU 2979 CB ALA A 387 2425 2112 2200 100 127 56 A C ATOM 2980 N ILE A 388 47.069 117.857 268.937 1.00 17.32 A N ANISOU 2980 N ILE A 388 2315 2186 2079 227 88 190 A N ATOM 2981 CA ILE A 388 47.688 117.124 270.032 1.00 25.41 A C ANISOU 2981 CA ILE A 388 3343 3265 3047 259 62 275 A C ATOM 2982 C ILE A 388 48.436 118.084 270.945 1.00 26.30 A C ANISOU 2982 C ILE A 388 3347 3515 3131 255 21 252 A C ATOM 2983 O ILE A 388 48.237 118.062 272.155 1.00 23.27 A O ANISOU 2983 O ILE A 388 2947 3225 2668 217 -4 268 A O ATOM 2984 CB ILE A 388 48.617 116.005 269.527 1.00 28.46 A C ANISOU 2984 CB ILE A 388 3784 3569 3461 360 70 361 A C ATOM 2985 CG1 ILE A 388 47.791 114.932 268.823 1.00 31.23 A C ANISOU 2985 CG1 ILE A 388 4256 3779 3830 352 102 378 A C ATOM 2986 CG2 ILE A 388 49.379 115.373 270.683 1.00 28.53 A C ANISOU 2986 CG2 ILE A 388 3777 3643 3419 403 33 459 A C ATOM 2987 CD1 ILE A 388 48.618 113.947 268.074 1.00 39.53 A C ANISOU 2987 CD1 ILE A 388 5369 4726 4924 458 121 429 A C ATOM 2988 N ALA A 389 49.255 118.959 270.363 1.00 23.19 A N ANISOU 2988 N ALA A 389 2879 3136 2798 287 14 210 A N ATOM 2989 CA ALA A 389 49.997 119.938 271.156 1.00 22.24 A C ANISOU 2989 CA ALA A 389 2650 3135 2666 274 -34 176 A C ATOM 2990 C ALA A 389 49.076 120.912 271.896 1.00 19.91 A C ANISOU 2990 C ALA A 389 2320 2911 2334 182 -45 79 A C ATOM 2991 O ALA A 389 49.467 121.482 272.917 1.00 22.07 A O ANISOU 2991 O ALA A 389 2528 3296 2560 158 -90 48 A O ATOM 2992 CB ALA A 389 50.989 120.707 270.284 1.00 19.54 A C ANISOU 2992 CB ALA A 389 2229 2780 2414 315 -33 155 A C ATOM 2993 N SER A 390 47.864 121.120 271.388 1.00 20.84 A N ANISOU 2993 N SER A 390 2478 2968 2474 131 -5 24 A N ATOM 2994 CA SER A 390 46.928 122.022 272.068 1.00 27.00 A C ANISOU 2994 CA SER A 390 3222 3809 3227 54 -6 -72 A C ATOM 2995 C SER A 390 45.924 121.261 272.922 1.00 26.67 A C ANISOU 2995 C SER A 390 3237 3804 3093 10 15 -44 A C ATOM 2996 O SER A 390 44.964 121.852 273.420 1.00 25.51 A O ANISOU 2996 O SER A 390 3068 3703 2922 -51 32 -121 A O ATOM 2997 CB SER A 390 46.160 122.891 271.064 1.00 18.95 A C ANISOU 2997 CB SER A 390 2188 2715 2299 23 22 -151 A C ATOM 2998 OG SER A 390 47.036 123.750 270.361 1.00 22.59 A O ANISOU 2998 OG SER A 390 2586 3152 2844 51 6 -176 A O ATOM 2999 N ASP A 391 46.150 119.960 273.091 1.00 28.88 A N ANISOU 2999 N ASP A 391 3587 4060 3328 43 16 68 A N ATOM 3000 CA ASP A 391 45.272 119.127 273.908 1.00 22.45 A C ANISOU 3000 CA ASP A 391 2828 3274 2427 -2 37 121 A C ATOM 3001 C ASP A 391 43.815 119.157 273.435 1.00 24.03 A C ANISOU 3001 C ASP A 391 3057 3413 2660 -67 86 76 A C ATOM 3002 O ASP A 391 42.893 119.268 274.244 1.00 21.69 A O ANISOU 3002 O ASP A 391 2749 3189 2302 -130 110 53 A O ATOM 3003 CB ASP A 391 45.351 119.560 275.372 1.00 26.68 A C ANISOU 3003 CB ASP A 391 3316 3971 2851 -34 13 99 A C ATOM 3004 CG ASP A 391 45.065 118.428 276.332 1.00 32.93 A C ANISOU 3004 CG ASP A 391 4166 4812 3534 -50 20 212 A C ATOM 3005 OD1 ASP A 391 44.959 117.272 275.875 1.00 35.84 A O ANISOU 3005 OD1 ASP A 391 4612 5076 3931 -29 35 315 A O ATOM 3006 OD2 ASP A 391 44.942 118.700 277.543 1.00 38.51 A O1- ANISOU 3006 OD2 ASP A 391 4846 5660 4125 -85 10 198 A O1- ATOM 3007 N CYS A 392 43.603 119.043 272.127 1.00 26.68 A N ANISOU 3007 N CYS A 392 3426 3625 3087 -52 100 65 A N ATOM 3008 CA CYS A 392 42.243 118.995 271.594 1.00 27.32 A C ANISOU 3008 CA CYS A 392 3531 3644 3205 -113 133 31 A C ATOM 3009 C CYS A 392 42.151 118.001 270.443 1.00 28.72 A C ANISOU 3009 C CYS A 392 3798 3680 3436 -91 139 84 A C ATOM 3010 O CYS A 392 41.580 118.308 269.395 1.00 25.94 A O ANISOU 3010 O CYS A 392 3452 3256 3147 -107 145 35 A O ATOM 3011 CB CYS A 392 41.765 120.390 271.152 1.00 31.78 A C ANISOU 3011 CB CYS A 392 4020 4222 3833 -138 137 -85 A C ATOM 3012 SG CYS A 392 42.795 121.227 269.905 1.00 28.75 A S ANISOU 3012 SG CYS A 392 3605 3777 3542 -74 113 -122 A S ATOM 3013 N ALA A 393 42.694 116.803 270.666 1.00 30.30 A N ANISOU 3013 N ALA A 393 4068 3839 3606 -54 134 183 A N ATOM 3014 CA ALA A 393 42.868 115.810 269.610 1.00 27.68 A C ANISOU 3014 CA ALA A 393 3828 3367 3324 -13 137 225 A C ATOM 3015 C ALA A 393 41.584 115.109 269.182 1.00 28.72 A C ANISOU 3015 C ALA A 393 4026 3406 3479 -86 152 229 A C ATOM 3016 O ALA A 393 41.558 114.413 268.164 1.00 31.72 A O ANISOU 3016 O ALA A 393 4485 3663 3904 -66 151 234 A O ATOM 3017 CB ALA A 393 43.897 114.776 270.037 1.00 24.19 A C ANISOU 3017 CB ALA A 393 3435 2902 2857 59 125 329 A C ATOM 3018 N ASP A 394 40.523 115.287 269.953 1.00 29.05 A N ANISOU 3018 N ASP A 394 4033 3513 3491 -173 167 223 A N ATOM 3019 CA ASP A 394 39.237 114.711 269.593 1.00 32.19 A C ANISOU 3019 CA ASP A 394 4472 3837 3921 -255 179 226 A C ATOM 3020 C ASP A 394 38.513 115.670 268.661 1.00 35.24 A C ANISOU 3020 C ASP A 394 4810 4214 4364 -285 174 125 A C ATOM 3021 O ASP A 394 37.787 116.574 269.093 1.00 36.34 A O ANISOU 3021 O ASP A 394 4864 4441 4502 -333 188 70 A O ATOM 3022 CB ASP A 394 38.444 114.359 270.845 1.00 34.04 A C ANISOU 3022 CB ASP A 394 4687 4149 4099 -333 206 283 A C ATOM 3023 CG ASP A 394 39.170 113.334 271.701 1.00 47.07 A C ANISOU 3023 CG ASP A 394 6393 5799 5692 -302 203 404 A C ATOM 3024 OD1 ASP A 394 39.515 112.267 271.143 1.00 51.06 A O ANISOU 3024 OD1 ASP A 394 6992 6170 6239 -270 189 464 A O ATOM 3025 OD2 ASP A 394 39.455 113.603 272.888 1.00 48.33 A O1- ANISOU 3025 OD2 ASP A 394 6508 6089 5767 -301 211 437 A O1- ATOM 3026 N GLY A 395 38.757 115.476 267.371 1.00 26.03 A N ANISOU 3026 N GLY A 395 3700 2943 3246 -249 155 101 A N ATOM 3027 CA GLY A 395 38.152 116.302 266.354 1.00 24.17 A C ANISOU 3027 CA GLY A 395 3431 2691 3061 -269 141 21 A C ATOM 3028 C GLY A 395 38.309 115.652 265.000 1.00 25.30 A C ANISOU 3028 C GLY A 395 3670 2710 3233 -241 120 14 A C ATOM 3029 O GLY A 395 39.041 114.668 264.846 1.00 26.73 A O ANISOU 3029 O GLY A 395 3938 2818 3402 -190 123 59 A O ATOM 3030 N MET A 396 37.636 116.216 264.008 1.00 16.42 A N ANISOU 3030 N MET A 396 2530 1565 2144 -269 98 -45 A N ATOM 3031 CA MET A 396 37.701 115.686 262.660 1.00 18.24 A C ANISOU 3031 CA MET A 396 2853 1693 2385 -248 74 -66 A C ATOM 3032 C MET A 396 37.358 116.800 261.697 1.00 16.32 A C ANISOU 3032 C MET A 396 2558 1476 2165 -251 51 -124 A C ATOM 3033 O MET A 396 36.491 117.628 261.991 1.00 18.46 A O ANISOU 3033 O MET A 396 2740 1807 2468 -305 42 -148 A O ATOM 3034 CB MET A 396 36.718 114.521 262.507 1.00 17.89 A C ANISOU 3034 CB MET A 396 2884 1556 2355 -328 53 -52 A C ATOM 3035 CG MET A 396 36.591 113.996 261.082 1.00 30.66 A C ANISOU 3035 CG MET A 396 4601 3070 3977 -322 18 -94 A C ATOM 3036 SD MET A 396 35.598 112.495 260.948 1.00 71.74 A S ANISOU 3036 SD MET A 396 9906 8143 9208 -418 -16 -82 A S ATOM 3037 CE MET A 396 33.974 113.114 261.366 1.00 34.49 A C ANISOU 3037 CE MET A 396 5071 3499 4534 -548 -40 -89 A C ATOM 3038 N THR A 397 38.034 116.816 260.553 1.00 23.60 A N ANISOU 3038 N THR A 397 3537 2356 3072 -188 45 -141 A N ATOM 3039 CA THR A 397 37.711 117.739 259.472 1.00 21.13 A C ANISOU 3039 CA THR A 397 3197 2060 2773 -190 18 -180 A C ATOM 3040 C THR A 397 37.230 116.911 258.306 1.00 23.34 A C ANISOU 3040 C THR A 397 3584 2254 3030 -211 -18 -205 A C ATOM 3041 O THR A 397 37.871 115.926 257.931 1.00 21.74 A O ANISOU 3041 O THR A 397 3487 1981 2793 -165 -4 -203 A O ATOM 3042 CB THR A 397 38.940 118.545 259.037 1.00 19.51 A C ANISOU 3042 CB THR A 397 2964 1892 2557 -101 45 -175 A C ATOM 3043 CG2 THR A 397 38.618 119.410 257.809 1.00 19.60 A C ANISOU 3043 CG2 THR A 397 2960 1912 2574 -103 16 -198 A C ATOM 3044 OG1 THR A 397 39.343 119.407 260.108 1.00 19.38 A O ANISOU 3044 OG1 THR A 397 2842 1954 2567 -92 66 -165 A O ATOM 3045 N LYS A 398 36.088 117.287 257.744 1.00 21.40 A N ANISOU 3045 N LYS A 398 3312 2013 2807 -280 -69 -233 A N ATOM 3046 CA LYS A 398 35.475 116.474 256.700 1.00 18.54 A C ANISOU 3046 CA LYS A 398 3050 1575 2420 -320 -119 -265 A C ATOM 3047 C LYS A 398 35.126 117.315 255.482 1.00 22.52 A C ANISOU 3047 C LYS A 398 3538 2110 2909 -319 -166 -291 A C ATOM 3048 O LYS A 398 34.521 118.379 255.609 1.00 23.60 A O ANISOU 3048 O LYS A 398 3566 2309 3092 -347 -187 -284 A O ATOM 3049 CB LYS A 398 34.226 115.781 257.252 1.00 16.53 A C ANISOU 3049 CB LYS A 398 2786 1286 2207 -429 -153 -264 A C ATOM 3050 CG LYS A 398 33.417 114.986 256.230 1.00 16.03 A C ANISOU 3050 CG LYS A 398 2813 1145 2133 -493 -222 -305 A C ATOM 3051 CD LYS A 398 32.359 114.144 256.927 1.00 21.26 A C ANISOU 3051 CD LYS A 398 3467 1762 2849 -603 -244 -290 A C ATOM 3052 CE LYS A 398 31.221 113.777 256.002 1.00 23.96 A C ANISOU 3052 CE LYS A 398 3839 2061 3205 -696 -333 -333 A C ATOM 3053 NZ LYS A 398 30.137 113.049 256.726 1.00 24.63 A N1+ ANISOU 3053 NZ LYS A 398 3891 2111 3357 -816 -351 -309 A N1+ ATOM 3054 N LEU A 399 35.532 116.839 254.308 1.00 22.43 A N ANISOU 3054 N LEU A 399 3637 2055 2829 -282 -180 -319 A N ATOM 3055 CA LEU A 399 35.157 117.468 253.048 1.00 20.78 A C ANISOU 3055 CA LEU A 399 3436 1876 2584 -286 -232 -337 A C ATOM 3056 C LEU A 399 34.350 116.503 252.196 1.00 25.58 A C ANISOU 3056 C LEU A 399 4148 2419 3151 -349 -304 -389 A C ATOM 3057 O LEU A 399 34.594 115.296 252.207 1.00 24.18 A O ANISOU 3057 O LEU A 399 4082 2157 2950 -348 -293 -420 A O ATOM 3058 CB LEU A 399 36.392 117.955 252.275 1.00 18.12 A C ANISOU 3058 CB LEU A 399 3130 1573 2182 -185 -184 -324 A C ATOM 3059 CG LEU A 399 37.200 119.099 252.893 1.00 20.68 A C ANISOU 3059 CG LEU A 399 3341 1964 2550 -130 -128 -273 A C ATOM 3060 CD1 LEU A 399 38.406 119.458 252.020 1.00 20.37 A C ANISOU 3060 CD1 LEU A 399 3336 1955 2448 -39 -79 -254 A C ATOM 3061 CD2 LEU A 399 36.299 120.311 253.074 1.00 16.98 A C ANISOU 3061 CD2 LEU A 399 2750 1548 2153 -182 -173 -254 A C ATOM 3062 N ILE A 400 33.381 117.038 251.462 1.00 23.61 A N ANISOU 3062 N ILE A 400 3865 2205 2900 -406 -384 -398 A N ATOM 3063 CA ILE A 400 32.571 116.223 250.565 1.00 26.35 A C ANISOU 3063 CA ILE A 400 4305 2503 3204 -474 -469 -453 A C ATOM 3064 C ILE A 400 32.749 116.723 249.134 1.00 26.27 A C ANISOU 3064 C ILE A 400 4348 2541 3094 -436 -510 -467 A C ATOM 3065 O ILE A 400 32.594 117.911 248.866 1.00 24.86 A O ANISOU 3065 O ILE A 400 4076 2442 2928 -422 -528 -420 A O ATOM 3066 CB ILE A 400 31.083 116.230 250.954 1.00 25.56 A C ANISOU 3066 CB ILE A 400 4117 2406 3188 -593 -548 -450 A C ATOM 3067 CG1 ILE A 400 30.906 115.783 252.408 1.00 28.38 A C ANISOU 3067 CG1 ILE A 400 4417 2733 3633 -632 -496 -424 A C ATOM 3068 CG2 ILE A 400 30.290 115.315 250.024 1.00 24.57 A C ANISOU 3068 CG2 ILE A 400 4090 2224 3021 -674 -646 -513 A C ATOM 3069 CD1 ILE A 400 29.472 115.830 252.895 1.00 31.11 A C ANISOU 3069 CD1 ILE A 400 4655 3095 4068 -747 -552 -413 A C ATOM 3070 N PHE A 401 33.108 115.816 248.231 1.00 25.29 A N ANISOU 3070 N PHE A 401 4375 2366 2869 -415 -521 -531 A N ATOM 3071 CA PHE A 401 33.401 116.168 246.847 1.00 25.61 A C ANISOU 3071 CA PHE A 401 4485 2460 2785 -371 -546 -549 A C ATOM 3072 C PHE A 401 32.440 115.501 245.879 1.00 31.93 A C ANISOU 3072 C PHE A 401 5377 3235 3519 -453 -663 -622 A C ATOM 3073 O PHE A 401 31.982 114.385 246.128 1.00 31.26 A O ANISOU 3073 O PHE A 401 5360 3055 3461 -517 -696 -685 A O ATOM 3074 CB PHE A 401 34.823 115.725 246.485 1.00 21.23 A C ANISOU 3074 CB PHE A 401 4038 1887 2141 -257 -445 -573 A C ATOM 3075 CG PHE A 401 35.896 116.452 247.240 1.00 22.28 A C ANISOU 3075 CG PHE A 401 4081 2060 2324 -172 -339 -500 A C ATOM 3076 CD1 PHE A 401 36.472 115.888 248.364 1.00 18.39 A C ANISOU 3076 CD1 PHE A 401 3578 1509 1902 -143 -269 -493 A C ATOM 3077 CD2 PHE A 401 36.332 117.701 246.815 1.00 21.69 A C ANISOU 3077 CD2 PHE A 401 3932 2082 2227 -125 -315 -433 A C ATOM 3078 CE1 PHE A 401 37.462 116.558 249.058 1.00 23.02 A C ANISOU 3078 CE1 PHE A 401 4078 2139 2531 -71 -184 -430 A C ATOM 3079 CE2 PHE A 401 37.312 118.380 247.508 1.00 24.38 A C ANISOU 3079 CE2 PHE A 401 4186 2455 2623 -58 -226 -370 A C ATOM 3080 CZ PHE A 401 37.884 117.807 248.628 1.00 25.44 A C ANISOU 3080 CZ PHE A 401 4308 2538 2821 -31 -163 -373 A C ATOM 3081 N ASP A 402 32.131 116.188 244.781 1.00 30.61 A N ANISOU 3081 N ASP A 402 5213 3153 3266 -455 -729 -611 A N ATOM 3082 CA ASP A 402 31.457 115.552 243.651 1.00 29.16 A C ANISOU 3082 CA ASP A 402 5142 2961 2977 -515 -839 -691 A C ATOM 3083 C ASP A 402 32.452 114.611 242.993 1.00 32.66 A C ANISOU 3083 C ASP A 402 5763 3354 3291 -441 -777 -779 A C ATOM 3084 O ASP A 402 33.538 115.032 242.606 1.00 29.90 A O ANISOU 3084 O ASP A 402 5441 3058 2861 -333 -685 -753 A O ATOM 3085 CB ASP A 402 30.991 116.594 242.632 1.00 33.62 A C ANISOU 3085 CB ASP A 402 5664 3644 3468 -522 -923 -640 A C ATOM 3086 CG ASP A 402 30.221 115.975 241.471 1.00 37.03 A C ANISOU 3086 CG ASP A 402 6205 4083 3780 -593 -1055 -724 A C ATOM 3087 OD1 ASP A 402 28.975 115.949 241.506 1.00 35.93 A O ANISOU 3087 OD1 ASP A 402 5992 3949 3711 -696 -1171 -722 A O ATOM 3088 OD2 ASP A 402 30.872 115.510 240.514 1.00 43.63 A O1- ANISOU 3088 OD2 ASP A 402 7191 4929 4456 -540 -1034 -790 A O1- ATOM 3089 N LYS A 403 32.104 113.337 242.878 1.00 39.20 A N ANISOU 3089 N LYS A 403 6653 4106 4137 -479 -795 -856 A N ATOM 3090 CA LYS A 403 33.090 112.353 242.446 1.00 43.24 A C ANISOU 3090 CA LYS A 403 7287 4566 4576 -392 -707 -926 A C ATOM 3091 C LYS A 403 33.607 112.557 241.021 1.00 42.88 A C ANISOU 3091 C LYS A 403 7347 4603 4345 -326 -704 -971 A C ATOM 3092 O LYS A 403 34.771 112.280 240.725 1.00 47.29 A O ANISOU 3092 O LYS A 403 7981 5156 4829 -216 -596 -998 A O ATOM 3093 CB LYS A 403 32.539 110.936 242.555 1.00 50.61 A C ANISOU 3093 CB LYS A 403 8248 5401 5579 -450 -733 -994 A C ATOM 3094 CG LYS A 403 33.621 109.895 242.365 1.00 55.59 A C ANISOU 3094 CG LYS A 403 8986 5959 6176 -353 -636 -1059 A C ATOM 3095 CD LYS A 403 33.072 108.497 242.406 1.00 60.81 A C ANISOU 3095 CD LYS A 403 9685 6513 6907 -413 -670 -1131 A C ATOM 3096 CE LYS A 403 34.192 107.486 242.361 1.00 65.28 A C ANISOU 3096 CE LYS A 403 10345 6995 7464 -311 -571 -1188 A C ATOM 3097 NZ LYS A 403 33.661 106.120 242.157 1.00 71.04 A N1+ ANISOU 3097 NZ LYS A 403 11131 7617 8245 -369 -615 -1276 A N1+ ATOM 3098 N GLU A 404 32.751 113.074 240.150 1.00 41.37 A N ANISOU 3098 N GLU A 404 7146 4497 4078 -389 -817 -969 A N ATOM 3099 CA GLU A 404 33.093 113.195 238.742 1.00 45.26 A C ANISOU 3099 CA GLU A 404 7734 5081 4381 -340 -824 -1008 A C ATOM 3100 C GLU A 404 33.838 114.479 238.431 1.00 42.21 A C ANISOU 3100 C GLU A 404 7345 4804 3888 -263 -777 -923 A C ATOM 3101 O GLU A 404 34.847 114.461 237.725 1.00 43.58 A O ANISOU 3101 O GLU A 404 7598 5030 3931 -164 -683 -939 A O ATOM 3102 CB GLU A 404 31.815 113.165 237.909 1.00 51.99 A C ANISOU 3102 CB GLU A 404 8573 5988 5193 -443 -975 -1034 A C ATOM 3103 CG GLU A 404 31.114 111.822 237.883 1.00 65.62 A C ANISOU 3103 CG GLU A 404 10325 7621 6985 -515 -1023 -1134 A C ATOM 3104 CD GLU A 404 29.889 111.833 236.989 1.00 78.61 A C ANISOU 3104 CD GLU A 404 11954 9334 8581 -612 -1173 -1163 A C ATOM 3105 OE1 GLU A 404 29.499 112.930 236.527 1.00 83.02 A O ANISOU 3105 OE1 GLU A 404 12462 10007 9075 -628 -1247 -1088 A O ATOM 3106 OE2 GLU A 404 29.306 110.750 236.761 1.00 82.44 A O1- ANISOU 3106 OE2 GLU A 404 12471 9756 9096 -674 -1221 -1255 A O1- ATOM 3107 N SER A 405 33.303 115.594 238.912 1.00 37.08 A N ANISOU 3107 N SER A 405 6577 4201 3310 -309 -836 -819 A N ATOM 3108 CA SER A 405 33.872 116.905 238.638 1.00 31.89 A C ANISOU 3108 CA SER A 405 5832 3663 2623 -241 -779 -689 A C ATOM 3109 C SER A 405 35.038 117.210 239.563 1.00 30.94 A C ANISOU 3109 C SER A 405 5640 3516 2598 -150 -623 -629 A C ATOM 3110 O SER A 405 35.863 118.072 239.258 1.00 32.88 A O ANISOU 3110 O SER A 405 5846 3846 2802 -74 -542 -541 A O ATOM 3111 CB SER A 405 32.802 117.979 238.807 1.00 35.50 A C ANISOU 3111 CB SER A 405 6137 4176 3175 -316 -890 -585 A C ATOM 3112 OG SER A 405 32.453 118.123 240.174 1.00 37.09 A O ANISOU 3112 OG SER A 405 6206 4307 3581 -353 -875 -551 A O ATOM 3113 N HIS A 406 35.084 116.497 240.690 1.00 33.23 A N ANISOU 3113 N HIS A 406 5913 3694 3020 -163 -587 -670 A N ATOM 3114 CA HIS A 406 36.028 116.742 241.791 1.00 33.65 A C ANISOU 3114 CA HIS A 406 5880 3717 3189 -95 -462 -611 A C ATOM 3115 C HIS A 406 35.769 118.046 242.554 1.00 26.32 A C ANISOU 3115 C HIS A 406 4769 2837 2395 -117 -468 -490 A C ATOM 3116 O HIS A 406 36.596 118.446 243.371 1.00 24.80 A O ANISOU 3116 O HIS A 406 4497 2641 2284 -61 -372 -435 A O ATOM 3117 CB HIS A 406 37.491 116.735 241.322 1.00 35.96 A C ANISOU 3117 CB HIS A 406 6231 4049 3383 31 -326 -605 A C ATOM 3118 CG HIS A 406 37.927 115.421 240.731 1.00 41.67 A C ANISOU 3118 CG HIS A 406 7131 4710 3993 78 -292 -735 A C ATOM 3119 CD2 HIS A 406 39.107 115.085 240.142 1.00 44.64 A C ANISOU 3119 CD2 HIS A 406 7593 5110 4259 193 -176 -769 A C ATOM 3120 ND1 HIS A 406 37.135 114.317 240.708 1.00 40.94 A N ANISOU 3120 ND1 HIS A 406 7137 4516 3900 8 -376 -847 A N ATOM 3121 CE1 HIS A 406 37.798 113.316 240.119 1.00 45.43 A C ANISOU 3121 CE1 HIS A 406 7822 5050 4390 77 -312 -938 A C ATOM 3122 NE2 HIS A 406 38.978 113.759 239.777 1.00 48.35 A N ANISOU 3122 NE2 HIS A 406 8207 5489 4675 193 -193 -905 A N ATOM 3123 N ARG A 407 34.646 118.716 242.303 1.00 23.30 A N ANISOU 3123 N ARG A 407 4316 2498 2039 -195 -582 -450 A N ATOM 3124 CA ARG A 407 34.353 119.945 243.052 1.00 28.13 A C ANISOU 3124 CA ARG A 407 4755 3142 2792 -210 -586 -347 A C ATOM 3125 C ARG A 407 33.940 119.694 244.488 1.00 23.71 A C ANISOU 3125 C ARG A 407 4107 2510 2393 -255 -577 -360 A C ATOM 3126 O ARG A 407 33.215 118.738 244.782 1.00 21.88 A O ANISOU 3126 O ARG A 407 3915 2213 2184 -324 -629 -429 A O ATOM 3127 CB ARG A 407 33.264 120.774 242.397 1.00 38.19 A C ANISOU 3127 CB ARG A 407 5967 4481 4063 -269 -709 -293 A C ATOM 3128 CG ARG A 407 33.667 121.396 241.107 1.00 56.67 A C ANISOU 3128 CG ARG A 407 8356 6914 6260 -222 -716 -237 A C ATOM 3129 CD ARG A 407 32.619 122.379 240.681 1.00 72.73 A C ANISOU 3129 CD ARG A 407 10297 9007 8331 -272 -836 -156 A C ATOM 3130 NE ARG A 407 31.372 121.673 240.433 1.00 87.63 A N ANISOU 3130 NE ARG A 407 12215 10877 10202 -365 -971 -227 A N ATOM 3131 CZ ARG A 407 31.091 121.071 239.290 1.00 97.02 A C ANISOU 3131 CZ ARG A 407 13533 12106 11225 -389 -1050 -284 A C ATOM 3132 NH1 ARG A 407 32.014 121.039 238.338 1.00 99.20 A N1+ ANISOU 3132 NH1 ARG A 407 13923 12441 11327 -320 -991 -282 A N1+ ATOM 3133 NH2 ARG A 407 29.929 120.450 239.132 1.00 99.74 A N ANISOU 3133 NH2 ARG A 407 13892 12431 11574 -485 -1182 -350 A N ATOM 3134 N VAL A 408 34.403 120.562 245.380 1.00 18.71 A N ANISOU 3134 N VAL A 408 3352 1891 1868 -221 -510 -292 A N ATOM 3135 CA VAL A 408 33.974 120.514 246.766 1.00 17.81 A C ANISOU 3135 CA VAL A 408 3140 1731 1895 -263 -499 -295 A C ATOM 3136 C VAL A 408 32.526 121.018 246.826 1.00 24.77 A C ANISOU 3136 C VAL A 408 3924 2631 2856 -348 -607 -278 A C ATOM 3137 O VAL A 408 32.190 122.058 246.252 1.00 24.23 A O ANISOU 3137 O VAL A 408 3791 2620 2797 -344 -655 -219 A O ATOM 3138 CB VAL A 408 34.945 121.300 247.692 1.00 21.43 A C ANISOU 3138 CB VAL A 408 3504 2205 2435 -200 -399 -240 A C ATOM 3139 CG1 VAL A 408 34.985 122.786 247.335 1.00 21.54 A C ANISOU 3139 CG1 VAL A 408 3417 2281 2487 -178 -410 -158 A C ATOM 3140 CG2 VAL A 408 34.581 121.101 249.158 1.00 18.01 A C ANISOU 3140 CG2 VAL A 408 2989 1733 2120 -238 -381 -255 A C ATOM 3141 N ILE A 409 31.659 120.244 247.472 1.00 24.68 A N ANISOU 3141 N ILE A 409 3903 2571 2905 -426 -646 -326 A N ATOM 3142 CA ILE A 409 30.237 120.566 247.546 1.00 23.71 A C ANISOU 3142 CA ILE A 409 3681 2467 2862 -511 -746 -316 A C ATOM 3143 C ILE A 409 29.766 120.700 248.992 1.00 22.69 A C ANISOU 3143 C ILE A 409 3428 2320 2873 -546 -709 -308 A C ATOM 3144 O ILE A 409 28.640 121.141 249.249 1.00 23.97 A O ANISOU 3144 O ILE A 409 3475 2507 3126 -604 -769 -292 A O ATOM 3145 CB ILE A 409 29.371 119.498 246.839 1.00 22.16 A C ANISOU 3145 CB ILE A 409 3575 2239 2604 -596 -849 -380 A C ATOM 3146 CG1 ILE A 409 29.617 118.123 247.467 1.00 25.43 A C ANISOU 3146 CG1 ILE A 409 4082 2562 3019 -624 -804 -447 A C ATOM 3147 CG2 ILE A 409 29.667 119.462 245.347 1.00 22.29 A C ANISOU 3147 CG2 ILE A 409 3710 2292 2467 -567 -901 -394 A C ATOM 3148 CD1 ILE A 409 28.780 116.998 246.861 1.00 23.88 A C ANISOU 3148 CD1 ILE A 409 3979 2314 2782 -719 -906 -520 A C ATOM 3149 N GLY A 410 30.624 120.311 249.931 1.00 20.49 A N ANISOU 3149 N GLY A 410 3169 2008 2608 -509 -608 -318 A N ATOM 3150 CA GLY A 410 30.283 120.382 251.340 1.00 21.84 A C ANISOU 3150 CA GLY A 410 3237 2175 2888 -538 -563 -312 A C ATOM 3151 C GLY A 410 31.480 120.153 252.245 1.00 23.46 A C ANISOU 3151 C GLY A 410 3467 2361 3085 -476 -455 -308 A C ATOM 3152 O GLY A 410 32.500 119.592 251.826 1.00 23.58 A O ANISOU 3152 O GLY A 410 3595 2347 3018 -421 -416 -320 A O ATOM 3153 N GLY A 411 31.368 120.606 253.488 1.00 21.89 A N ANISOU 3153 N GLY A 411 3161 2186 2969 -481 -406 -294 A N ATOM 3154 CA GLY A 411 32.433 120.405 254.451 1.00 14.34 A C ANISOU 3154 CA GLY A 411 2218 1224 2007 -430 -317 -287 A C ATOM 3155 C GLY A 411 31.930 120.503 255.873 1.00 15.64 A C ANISOU 3155 C GLY A 411 2283 1414 2245 -470 -281 -285 A C ATOM 3156 O GLY A 411 30.870 121.101 256.126 1.00 17.64 A O ANISOU 3156 O GLY A 411 2430 1703 2571 -517 -311 -287 A O ATOM 3157 N ALA A 412 32.685 119.917 256.799 1.00 15.59 A N ANISOU 3157 N ALA A 412 2309 1395 2217 -447 -216 -278 A N ATOM 3158 CA ALA A 412 32.327 119.940 258.218 1.00 17.75 A C ANISOU 3158 CA ALA A 412 2502 1707 2536 -481 -174 -272 A C ATOM 3159 C ALA A 412 33.556 119.788 259.120 1.00 21.25 A C ANISOU 3159 C ALA A 412 2966 2164 2945 -420 -105 -255 A C ATOM 3160 O ALA A 412 34.557 119.181 258.734 1.00 21.35 A O ANISOU 3160 O ALA A 412 3074 2135 2904 -366 -89 -243 A O ATOM 3161 CB ALA A 412 31.304 118.864 258.529 1.00 14.40 A C ANISOU 3161 CB ALA A 412 2098 1248 2124 -574 -194 -269 A C ATOM 3162 N ILE A 413 33.485 120.381 260.305 1.00 18.33 A N ANISOU 3162 N ILE A 413 2500 1859 2605 -424 -65 -257 A N ATOM 3163 CA ILE A 413 34.524 120.237 261.308 1.00 17.37 A C ANISOU 3163 CA ILE A 413 2386 1767 2448 -379 -11 -239 A C ATOM 3164 C ILE A 413 33.862 119.985 262.662 1.00 20.27 A C ANISOU 3164 C ILE A 413 2698 2186 2819 -435 22 -233 A C ATOM 3165 O ILE A 413 32.893 120.657 263.025 1.00 16.40 A O ANISOU 3165 O ILE A 413 2110 1745 2376 -477 23 -261 A O ATOM 3166 CB ILE A 413 35.414 121.505 261.419 1.00 25.03 A C ANISOU 3166 CB ILE A 413 3288 2786 3436 -312 7 -256 A C ATOM 3167 CG1 ILE A 413 35.957 121.944 260.051 1.00 19.51 A C ANISOU 3167 CG1 ILE A 413 2624 2051 2739 -264 -19 -252 A C ATOM 3168 CG2 ILE A 413 36.551 121.285 262.412 1.00 12.06 A C ANISOU 3168 CG2 ILE A 413 1653 1178 1751 -268 49 -237 A C ATOM 3169 CD1 ILE A 413 35.100 122.994 259.367 1.00 24.02 A C ANISOU 3169 CD1 ILE A 413 3125 2629 3372 -285 -60 -271 A C ATOM 3170 N VAL A 414 34.373 119.012 263.407 1.00 18.00 A N ANISOU 3170 N VAL A 414 2469 1890 2481 -433 51 -191 A N ATOM 3171 CA VAL A 414 34.070 118.941 264.830 1.00 19.01 A C ANISOU 3171 CA VAL A 414 2541 2093 2588 -468 94 -175 A C ATOM 3172 C VAL A 414 35.404 119.112 265.544 1.00 20.75 A C ANISOU 3172 C VAL A 414 2769 2358 2757 -397 120 -160 A C ATOM 3173 O VAL A 414 36.373 118.428 265.223 1.00 20.87 A O ANISOU 3173 O VAL A 414 2867 2320 2742 -346 115 -123 A O ATOM 3174 CB VAL A 414 33.348 117.623 265.236 1.00 18.43 A C ANISOU 3174 CB VAL A 414 2520 1982 2501 -544 101 -121 A C ATOM 3175 CG1 VAL A 414 34.063 116.390 264.683 1.00 14.74 A C ANISOU 3175 CG1 VAL A 414 2187 1405 2007 -518 83 -75 A C ATOM 3176 CG2 VAL A 414 33.207 117.528 266.746 1.00 21.13 A C ANISOU 3176 CG2 VAL A 414 2812 2416 2799 -572 155 -89 A C ATOM 3177 N GLY A 415 35.477 120.067 266.469 1.00 14.20 A N ANISOU 3177 N GLY A 415 1848 1625 1921 -389 145 -196 A N ATOM 3178 CA GLY A 415 36.728 120.314 267.163 1.00 16.23 A C ANISOU 3178 CA GLY A 415 2101 1935 2131 -329 157 -189 A C ATOM 3179 C GLY A 415 36.813 121.701 267.779 1.00 20.50 A C ANISOU 3179 C GLY A 415 2537 2562 2689 -317 167 -262 A C ATOM 3180 O GLY A 415 35.998 122.584 267.478 1.00 17.41 A O ANISOU 3180 O GLY A 415 2079 2175 2362 -338 164 -321 A O ATOM 3181 N THR A 416 37.797 121.882 268.658 1.00 16.97 A N ANISOU 3181 N THR A 416 2077 2183 2189 -282 173 -261 A N ATOM 3182 CA THR A 416 38.075 123.190 269.248 1.00 21.13 A C ANISOU 3182 CA THR A 416 2514 2782 2731 -268 174 -341 A C ATOM 3183 C THR A 416 38.403 124.159 268.128 1.00 17.41 A C ANISOU 3183 C THR A 416 2015 2248 2353 -234 147 -378 A C ATOM 3184 O THR A 416 39.116 123.796 267.185 1.00 13.85 A O ANISOU 3184 O THR A 416 1616 1732 1915 -196 129 -330 A O ATOM 3185 CB THR A 416 39.267 123.129 270.222 1.00 19.49 A C ANISOU 3185 CB THR A 416 2306 2650 2448 -234 167 -326 A C ATOM 3186 CG2 THR A 416 39.556 124.501 270.815 1.00 25.98 A C ANISOU 3186 CG2 THR A 416 3040 3540 3292 -228 160 -425 A C ATOM 3187 OG1 THR A 416 38.947 122.236 271.292 1.00 20.21 A O ANISOU 3187 OG1 THR A 416 2426 2808 2444 -266 192 -278 A O ATOM 3188 N ASN A 417 37.837 125.365 268.206 1.00 17.18 A N ANISOU 3188 N ASN A 417 1903 2235 2390 -246 149 -459 A N ATOM 3189 CA ASN A 417 38.010 126.383 267.174 1.00 17.38 A C ANISOU 3189 CA ASN A 417 1893 2196 2514 -221 122 -485 A C ATOM 3190 C ASN A 417 37.539 125.946 265.782 1.00 17.94 A C ANISOU 3190 C ASN A 417 2014 2181 2620 -223 104 -434 A C ATOM 3191 O ASN A 417 37.908 126.568 264.781 1.00 19.17 A O ANISOU 3191 O ASN A 417 2164 2285 2835 -196 81 -425 A O ATOM 3192 CB ASN A 417 39.473 126.843 267.086 1.00 21.82 A C ANISOU 3192 CB ASN A 417 2449 2758 3085 -176 104 -478 A C ATOM 3193 CG ASN A 417 39.937 127.581 268.328 1.00 25.91 A C ANISOU 3193 CG ASN A 417 2904 3355 3587 -179 104 -549 A C ATOM 3194 ND2 ASN A 417 41.245 127.568 268.562 1.00 30.26 A N ANISOU 3194 ND2 ASN A 417 3455 3930 4111 -150 85 -527 A N ATOM 3195 OD1 ASN A 417 39.138 128.170 269.058 1.00 24.26 A O ANISOU 3195 OD1 ASN A 417 2642 3186 3388 -205 121 -628 A O ATOM 3196 N GLY A 418 36.729 124.892 265.715 1.00 19.73 A N ANISOU 3196 N GLY A 418 2291 2396 2808 -260 111 -399 A N ATOM 3197 CA GLY A 418 36.326 124.337 264.435 1.00 17.54 A C ANISOU 3197 CA GLY A 418 2074 2042 2547 -267 84 -358 A C ATOM 3198 C GLY A 418 35.590 125.302 263.519 1.00 16.50 A C ANISOU 3198 C GLY A 418 1889 1876 2503 -273 54 -384 A C ATOM 3199 O GLY A 418 35.853 125.332 262.312 1.00 22.29 A O ANISOU 3199 O GLY A 418 2665 2556 3249 -250 24 -353 A O ATOM 3200 N GLY A 419 34.686 126.099 264.087 1.00 15.38 A N ANISOU 3200 N GLY A 419 1655 1770 2420 -296 63 -438 A N ATOM 3201 CA GLY A 419 33.917 127.071 263.319 1.00 14.32 A C ANISOU 3201 CA GLY A 419 1455 1601 2383 -295 31 -459 A C ATOM 3202 C GLY A 419 34.787 128.003 262.486 1.00 22.23 A C ANISOU 3202 C GLY A 419 2453 2559 3434 -247 5 -446 A C ATOM 3203 O GLY A 419 34.459 128.336 261.335 1.00 29.95 A O ANISOU 3203 O GLY A 419 3435 3490 4456 -240 -35 -414 A O ATOM 3204 N GLU A 420 35.929 128.386 263.046 1.00 21.13 A N ANISOU 3204 N GLU A 420 2307 2439 3282 -216 26 -462 A N ATOM 3205 CA GLU A 420 36.814 129.337 262.377 1.00 23.43 A C ANISOU 3205 CA GLU A 420 2580 2691 3631 -178 9 -445 A C ATOM 3206 C GLU A 420 37.377 128.785 261.071 1.00 25.31 A C ANISOU 3206 C GLU A 420 2900 2890 3827 -156 -8 -366 A C ATOM 3207 O GLU A 420 37.945 129.534 260.269 1.00 21.29 A O ANISOU 3207 O GLU A 420 2378 2348 3363 -130 -21 -333 A O ATOM 3208 CB GLU A 420 37.949 129.774 263.310 1.00 21.42 A C ANISOU 3208 CB GLU A 420 2296 2472 3371 -159 29 -480 A C ATOM 3209 CG GLU A 420 37.488 130.483 264.590 1.00 22.38 A C ANISOU 3209 CG GLU A 420 2339 2638 3529 -175 46 -577 A C ATOM 3210 CD GLU A 420 36.804 131.828 264.337 1.00 26.47 A C ANISOU 3210 CD GLU A 420 2773 3105 4179 -171 29 -626 A C ATOM 3211 OE1 GLU A 420 36.750 132.271 263.168 1.00 21.49 A O ANISOU 3211 OE1 GLU A 420 2143 2408 3615 -157 -1 -572 A O ATOM 3212 OE2 GLU A 420 36.319 132.443 265.318 1.00 23.44 A O1- ANISOU 3212 OE2 GLU A 420 2325 2750 3831 -177 48 -719 A O1- ATOM 3213 N LEU A 421 37.179 127.487 260.843 1.00 18.50 A N ANISOU 3213 N LEU A 421 2122 2028 2878 -169 -5 -337 A N ATOM 3214 CA LEU A 421 37.670 126.860 259.623 1.00 17.30 A C ANISOU 3214 CA LEU A 421 2060 1842 2673 -145 -16 -279 A C ATOM 3215 C LEU A 421 36.683 126.958 258.465 1.00 19.49 A C ANISOU 3215 C LEU A 421 2353 2084 2967 -165 -62 -259 A C ATOM 3216 O LEU A 421 37.045 126.662 257.321 1.00 18.72 A O ANISOU 3216 O LEU A 421 2326 1965 2823 -144 -75 -217 A O ATOM 3217 CB LEU A 421 38.020 125.382 259.873 1.00 20.53 A C ANISOU 3217 CB LEU A 421 2563 2251 2986 -142 5 -262 A C ATOM 3218 CG LEU A 421 39.398 125.036 260.451 1.00 21.11 A C ANISOU 3218 CG LEU A 421 2654 2348 3018 -96 42 -244 A C ATOM 3219 CD1 LEU A 421 39.667 125.736 261.772 1.00 21.20 A C ANISOU 3219 CD1 LEU A 421 2579 2415 3063 -103 56 -283 A C ATOM 3220 CD2 LEU A 421 39.539 123.528 260.616 1.00 24.28 A C ANISOU 3220 CD2 LEU A 421 3153 2731 3341 -91 57 -221 A C ATOM 3221 N LEU A 422 35.434 127.323 258.758 1.00 19.72 A N ANISOU 3221 N LEU A 422 2317 2118 3056 -205 -87 -291 A N ATOM 3222 CA LEU A 422 34.391 127.319 257.725 1.00 24.13 A C ANISOU 3222 CA LEU A 422 2884 2654 3631 -231 -144 -270 A C ATOM 3223 C LEU A 422 34.650 128.271 256.546 1.00 24.54 A C ANISOU 3223 C LEU A 422 2925 2682 3717 -198 -178 -222 A C ATOM 3224 O LEU A 422 34.355 127.933 255.391 1.00 27.37 A O ANISOU 3224 O LEU A 422 3343 3027 4028 -204 -222 -184 A O ATOM 3225 CB LEU A 422 33.017 127.624 258.328 1.00 25.14 A C ANISOU 3225 CB LEU A 422 2920 2798 3834 -274 -161 -309 A C ATOM 3226 CG LEU A 422 32.285 126.502 259.057 1.00 23.38 A C ANISOU 3226 CG LEU A 422 2714 2597 3570 -329 -146 -332 A C ATOM 3227 CD1 LEU A 422 30.867 126.944 259.380 1.00 23.28 A C ANISOU 3227 CD1 LEU A 422 2596 2607 3645 -368 -164 -359 A C ATOM 3228 CD2 LEU A 422 32.270 125.206 258.244 1.00 13.94 A C ANISOU 3228 CD2 LEU A 422 1638 1371 2289 -356 -175 -301 A C ATOM 3229 N GLY A 423 35.202 129.448 256.841 1.00 19.56 A N ANISOU 3229 N GLY A 423 2221 2044 3165 -168 -161 -222 A N ATOM 3230 CA GLY A 423 35.428 130.462 255.822 1.00 22.40 A C ANISOU 3230 CA GLY A 423 2559 2375 3576 -142 -190 -162 A C ATOM 3231 C GLY A 423 36.026 129.893 254.546 1.00 23.81 A C ANISOU 3231 C GLY A 423 2840 2557 3650 -124 -198 -97 A C ATOM 3232 O GLY A 423 35.383 129.930 253.481 1.00 26.70 A O ANISOU 3232 O GLY A 423 3231 2918 3995 -132 -252 -55 A O ATOM 3233 N GLU A 424 37.193 129.262 254.688 1.00 19.81 A N ANISOU 3233 N GLU A 424 2394 2065 3069 -98 -144 -94 A N ATOM 3234 CA GLU A 424 37.900 128.685 253.557 1.00 20.83 A C ANISOU 3234 CA GLU A 424 2620 2202 3092 -68 -132 -43 A C ATOM 3235 C GLU A 424 36.953 127.758 252.805 1.00 18.30 A C ANISOU 3235 C GLU A 424 2382 1879 2690 -97 -182 -53 A C ATOM 3236 O GLU A 424 36.712 127.938 251.596 1.00 22.99 A O ANISOU 3236 O GLU A 424 3015 2479 3240 -93 -221 -7 A O ATOM 3237 CB GLU A 424 39.146 127.916 254.030 1.00 14.07 A C ANISOU 3237 CB GLU A 424 1810 1362 2175 -33 -65 -54 A C ATOM 3238 CG GLU A 424 40.028 127.387 252.882 1.00 18.54 A C ANISOU 3238 CG GLU A 424 2468 1941 2637 13 -34 -7 A C ATOM 3239 CD GLU A 424 41.218 126.560 253.360 1.00 24.81 A C ANISOU 3239 CD GLU A 424 3299 2747 3382 58 32 -17 A C ATOM 3240 OE1 GLU A 424 41.541 126.597 254.572 1.00 19.41 A O ANISOU 3240 OE1 GLU A 424 2559 2069 2748 54 50 -45 A O ATOM 3241 OE2 GLU A 424 41.831 125.868 252.517 1.00 25.87 A O1- ANISOU 3241 OE2 GLU A 424 3518 2888 3422 101 66 1 A O1- ATOM 3242 N ILE A 425 36.348 126.829 253.543 1.00 13.72 A N ANISOU 3242 N ILE A 425 1823 1293 2095 -132 -186 -110 A N ATOM 3243 CA ILE A 425 35.493 125.838 252.907 1.00 16.94 A C ANISOU 3243 CA ILE A 425 2313 1691 2433 -170 -236 -127 A C ATOM 3244 C ILE A 425 34.383 126.569 252.168 1.00 22.19 A C ANISOU 3244 C ILE A 425 2928 2361 3142 -200 -316 -102 A C ATOM 3245 O ILE A 425 34.165 126.330 250.967 1.00 26.14 A O ANISOU 3245 O ILE A 425 3498 2868 3565 -203 -364 -77 A O ATOM 3246 CB ILE A 425 34.963 124.802 253.920 1.00 18.85 A C ANISOU 3246 CB ILE A 425 2570 1919 2675 -214 -227 -181 A C ATOM 3247 CG1 ILE A 425 36.143 124.088 254.591 1.00 14.22 A C ANISOU 3247 CG1 ILE A 425 2034 1327 2043 -174 -155 -189 A C ATOM 3248 CG2 ILE A 425 34.088 123.763 253.229 1.00 16.23 A C ANISOU 3248 CG2 ILE A 425 2321 1563 2282 -264 -286 -201 A C ATOM 3249 CD1 ILE A 425 35.734 123.112 255.693 1.00 12.56 A C ANISOU 3249 CD1 ILE A 425 1836 1103 1834 -215 -140 -223 A C ATOM 3250 N GLY A 426 33.764 127.534 252.850 1.00 18.15 A N ANISOU 3250 N GLY A 426 2295 1850 2751 -213 -328 -106 A N ATOM 3251 CA GLY A 426 32.682 128.288 252.248 1.00 18.05 A C ANISOU 3251 CA GLY A 426 2216 1839 2802 -232 -405 -76 A C ATOM 3252 C GLY A 426 33.172 128.915 250.955 1.00 21.15 A C ANISOU 3252 C GLY A 426 2643 2237 3154 -196 -432 2 A C ATOM 3253 O GLY A 426 32.564 128.740 249.881 1.00 18.72 A O ANISOU 3253 O GLY A 426 2378 1946 2789 -214 -505 34 A O ATOM 3254 N LEU A 427 34.317 129.593 251.044 1.00 16.88 A N ANISOU 3254 N LEU A 427 2089 1691 2634 -150 -373 36 A N ATOM 3255 CA LEU A 427 34.799 130.321 249.886 1.00 25.59 A C ANISOU 3255 CA LEU A 427 3210 2802 3711 -119 -387 126 A C ATOM 3256 C LEU A 427 35.028 129.293 248.792 1.00 26.47 A C ANISOU 3256 C LEU A 427 3456 2948 3654 -116 -398 137 A C ATOM 3257 O LEU A 427 34.599 129.485 247.644 1.00 15.77 A O ANISOU 3257 O LEU A 427 2134 1617 2241 -121 -462 192 A O ATOM 3258 CB LEU A 427 36.079 131.089 250.198 1.00 18.93 A C ANISOU 3258 CB LEU A 427 2330 1946 2917 -79 -314 161 A C ATOM 3259 CG LEU A 427 36.619 131.926 249.033 1.00 22.52 A C ANISOU 3259 CG LEU A 427 2792 2410 3357 -52 -320 273 A C ATOM 3260 CD1 LEU A 427 35.614 132.986 248.570 1.00 18.07 A C ANISOU 3260 CD1 LEU A 427 2155 1821 2891 -63 -402 335 A C ATOM 3261 CD2 LEU A 427 37.945 132.581 249.403 1.00 21.35 A C ANISOU 3261 CD2 LEU A 427 2601 2248 3263 -24 -243 305 A C ATOM 3262 N ALA A 428 35.624 128.167 249.185 1.00 14.59 A N ANISOU 3262 N ALA A 428 2029 1443 2070 -110 -343 77 A N ATOM 3263 CA ALA A 428 35.987 127.143 248.219 1.00 20.43 A C ANISOU 3263 CA ALA A 428 2904 2204 2653 -97 -338 68 A C ATOM 3264 C ALA A 428 34.746 126.721 247.458 1.00 21.27 A C ANISOU 3264 C ALA A 428 3055 2321 2707 -147 -440 53 A C ATOM 3265 O ALA A 428 34.795 126.546 246.238 1.00 23.45 A O ANISOU 3265 O ALA A 428 3415 2631 2864 -137 -472 80 A O ATOM 3266 CB ALA A 428 36.615 125.945 248.910 1.00 14.67 A C ANISOU 3266 CB ALA A 428 2243 1454 1877 -84 -273 -2 A C ATOM 3267 N ILE A 429 33.623 126.579 248.163 1.00 19.91 A N ANISOU 3267 N ILE A 429 2820 2126 2619 -202 -492 10 A N ATOM 3268 CA ILE A 429 32.441 126.080 247.476 1.00 18.37 A C ANISOU 3268 CA ILE A 429 2659 1942 2380 -258 -595 -8 A C ATOM 3269 C ILE A 429 31.889 127.151 246.547 1.00 21.41 A C ANISOU 3269 C ILE A 429 2990 2361 2782 -255 -676 75 A C ATOM 3270 O ILE A 429 31.444 126.842 245.443 1.00 18.90 A O ANISOU 3270 O ILE A 429 2742 2078 2361 -275 -755 88 A O ATOM 3271 CB ILE A 429 31.349 125.565 248.431 1.00 19.70 A C ANISOU 3271 CB ILE A 429 2768 2084 2635 -325 -628 -69 A C ATOM 3272 CG1 ILE A 429 31.860 124.372 249.244 1.00 21.70 A C ANISOU 3272 CG1 ILE A 429 3091 2300 2854 -333 -559 -137 A C ATOM 3273 CG2 ILE A 429 30.119 125.142 247.638 1.00 17.33 A C ANISOU 3273 CG2 ILE A 429 2486 1799 2299 -390 -747 -79 A C ATOM 3274 CD1 ILE A 429 30.909 123.939 250.351 1.00 19.89 A C ANISOU 3274 CD1 ILE A 429 2792 2050 2715 -398 -569 -180 A C ATOM 3275 N GLU A 430 31.951 128.412 246.975 1.00 20.49 A N ANISOU 3275 N GLU A 430 2756 2236 2796 -227 -659 132 A N ATOM 3276 CA GLU A 430 31.353 129.484 246.181 1.00 17.68 A C ANISOU 3276 CA GLU A 430 2336 1898 2482 -221 -740 223 A C ATOM 3277 C GLU A 430 32.132 129.685 244.893 1.00 19.58 A C ANISOU 3277 C GLU A 430 2668 2183 2589 -185 -737 303 A C ATOM 3278 O GLU A 430 31.562 130.042 243.857 1.00 21.96 A O ANISOU 3278 O GLU A 430 2979 2523 2842 -192 -828 372 A O ATOM 3279 CB GLU A 430 31.330 130.793 246.983 1.00 17.27 A C ANISOU 3279 CB GLU A 430 2142 1806 2614 -194 -714 259 A C ATOM 3280 CG GLU A 430 30.311 130.814 248.111 1.00 26.07 A C ANISOU 3280 CG GLU A 430 3147 2895 3865 -225 -729 191 A C ATOM 3281 CD GLU A 430 28.880 130.984 247.625 1.00 32.06 A C ANISOU 3281 CD GLU A 430 3842 3671 4670 -259 -846 216 A C ATOM 3282 OE1 GLU A 430 28.677 131.262 246.425 1.00 36.90 A O ANISOU 3282 OE1 GLU A 430 4486 4313 5220 -253 -926 296 A O ATOM 3283 OE2 GLU A 430 27.955 130.851 248.455 1.00 36.43 A O1- ANISOU 3283 OE2 GLU A 430 4306 4216 5321 -290 -858 159 A O1- ATOM 3284 N MET A 431 33.435 129.420 244.949 1.00 17.92 A N ANISOU 3284 N MET A 431 2524 1975 2312 -145 -633 297 A N ATOM 3285 CA MET A 431 34.291 129.638 243.786 1.00 19.52 A C ANISOU 3285 CA MET A 431 2803 2227 2385 -105 -606 377 A C ATOM 3286 C MET A 431 34.343 128.402 242.898 1.00 24.29 A C ANISOU 3286 C MET A 431 3561 2879 2791 -113 -622 321 A C ATOM 3287 O MET A 431 34.996 128.409 241.857 1.00 29.27 A O ANISOU 3287 O MET A 431 4274 3566 3282 -79 -596 372 A O ATOM 3288 CB MET A 431 35.709 130.014 244.214 1.00 18.75 A C ANISOU 3288 CB MET A 431 2689 2118 2318 -56 -483 404 A C ATOM 3289 CG MET A 431 35.807 131.315 244.995 1.00 25.78 A C ANISOU 3289 CG MET A 431 3439 2957 3400 -49 -467 456 A C ATOM 3290 SD MET A 431 35.194 132.718 244.048 1.00 29.83 A S ANISOU 3290 SD MET A 431 3885 3474 3974 -48 -553 602 A S ATOM 3291 CE MET A 431 36.394 132.800 242.720 1.00 60.29 A C ANISOU 3291 CE MET A 431 7838 7405 7664 -11 -492 713 A C ATOM 3292 N GLY A 432 33.670 127.337 243.316 1.00 21.42 A N ANISOU 3292 N GLY A 432 3237 2489 2414 -157 -659 215 A N ATOM 3293 CA GLY A 432 33.665 126.114 242.538 1.00 21.35 A C ANISOU 3293 CA GLY A 432 3377 2503 2231 -169 -680 142 A C ATOM 3294 C GLY A 432 35.010 125.414 242.516 1.00 21.15 A C ANISOU 3294 C GLY A 432 3451 2477 2110 -110 -558 102 A C ATOM 3295 O GLY A 432 35.351 124.776 241.527 1.00 21.52 A O ANISOU 3295 O GLY A 432 3625 2563 1988 -89 -551 74 A O ATOM 3296 N CYS A 433 35.774 125.524 243.602 1.00 21.32 A N ANISOU 3296 N CYS A 433 3411 2455 2235 -79 -462 95 A N ATOM 3297 CA CYS A 433 37.074 124.857 243.688 1.00 24.89 A C ANISOU 3297 CA CYS A 433 3937 2903 2617 -17 -345 61 A C ATOM 3298 C CYS A 433 36.957 123.343 243.637 1.00 25.90 A C ANISOU 3298 C CYS A 433 4193 2993 2653 -26 -348 -55 A C ATOM 3299 O CYS A 433 35.952 122.782 244.088 1.00 23.71 A O ANISOU 3299 O CYS A 433 3917 2670 2423 -91 -422 -115 A O ATOM 3300 CB CYS A 433 37.795 125.238 244.978 1.00 27.65 A C ANISOU 3300 CB CYS A 433 4185 3216 3106 8 -263 73 A C ATOM 3301 SG CYS A 433 38.290 126.953 245.078 1.00 33.58 A S ANISOU 3301 SG CYS A 433 4797 3991 3971 28 -235 197 A S ATOM 3302 N ASP A 434 37.981 122.689 243.083 1.00 23.18 A N ANISOU 3302 N ASP A 434 3955 2666 2188 40 -265 -84 A N ATOM 3303 CA ASP A 434 38.088 121.232 243.183 1.00 27.47 A C ANISOU 3303 CA ASP A 434 4619 3149 2669 48 -247 -198 A C ATOM 3304 C ASP A 434 39.111 120.849 244.243 1.00 26.71 A C ANISOU 3304 C ASP A 434 4493 3005 2650 104 -140 -210 A C ATOM 3305 O ASP A 434 39.781 121.717 244.804 1.00 21.96 A O ANISOU 3305 O ASP A 434 3782 2428 2133 135 -82 -136 A O ATOM 3306 CB ASP A 434 38.454 120.585 241.842 1.00 26.45 A C ANISOU 3306 CB ASP A 434 4643 3060 2346 90 -232 -247 A C ATOM 3307 CG ASP A 434 39.781 121.087 241.281 1.00 31.35 A C ANISOU 3307 CG ASP A 434 5263 3755 2892 185 -112 -181 A C ATOM 3308 OD1 ASP A 434 40.617 121.627 242.044 1.00 31.86 A O ANISOU 3308 OD1 ASP A 434 5226 3818 3061 225 -29 -119 A O ATOM 3309 OD2 ASP A 434 40.003 120.912 240.063 1.00 34.94 A O1- ANISOU 3309 OD2 ASP A 434 5821 4276 3178 217 -100 -194 A O1- ATOM 3310 N ALA A 435 39.258 119.551 244.489 1.00 27.32 A N ANISOU 3310 N ALA A 435 4669 3011 2700 118 -119 -301 A N ATOM 3311 CA ALA A 435 40.166 119.078 245.528 1.00 23.72 A C ANISOU 3311 CA ALA A 435 4188 2506 2318 172 -31 -308 A C ATOM 3312 C ALA A 435 41.606 119.537 245.307 1.00 24.55 A C ANISOU 3312 C ALA A 435 4262 2670 2397 272 85 -251 A C ATOM 3313 O ALA A 435 42.311 119.868 246.258 1.00 27.47 A O ANISOU 3313 O ALA A 435 4536 3039 2864 301 141 -207 A O ATOM 3314 CB ALA A 435 40.107 117.561 245.626 1.00 24.45 A C ANISOU 3314 CB ALA A 435 4408 2503 2377 179 -30 -408 A C ATOM 3315 N GLU A 436 42.028 119.569 244.048 1.00 21.61 A N ANISOU 3315 N GLU A 436 3966 2358 1888 320 119 -251 A N ATOM 3316 CA GLU A 436 43.386 119.961 243.703 1.00 19.91 A C ANISOU 3316 CA GLU A 436 3720 2208 1637 414 237 -194 A C ATOM 3317 C GLU A 436 43.667 121.414 244.094 1.00 24.35 A C ANISOU 3317 C GLU A 436 4125 2828 2300 396 248 -74 A C ATOM 3318 O GLU A 436 44.740 121.724 244.623 1.00 24.94 A O ANISOU 3318 O GLU A 436 4117 2920 2440 448 332 -26 A O ATOM 3319 CB GLU A 436 43.620 119.747 242.206 1.00 27.57 A C ANISOU 3319 CB GLU A 436 4807 3245 2423 459 268 -216 A C ATOM 3320 CG GLU A 436 44.998 120.137 241.722 1.00 31.61 A C ANISOU 3320 CG GLU A 436 5286 3840 2884 555 401 -152 A C ATOM 3321 CD GLU A 436 45.158 119.983 240.218 1.00 38.80 A C ANISOU 3321 CD GLU A 436 6313 4835 3594 596 435 -171 A C ATOM 3322 OE1 GLU A 436 45.318 121.012 239.530 1.00 43.79 A O ANISOU 3322 OE1 GLU A 436 6895 5566 4176 589 451 -67 A O ATOM 3323 OE2 GLU A 436 45.141 118.836 239.725 1.00 44.78 A O1- ANISOU 3323 OE2 GLU A 436 7213 5558 4242 636 449 -290 A O1- ATOM 3324 N ASP A 437 42.700 122.296 243.843 1.00 23.06 A N ANISOU 3324 N ASP A 437 3917 2687 2159 321 158 -29 A N ATOM 3325 CA ASP A 437 42.818 123.702 244.223 1.00 23.03 A C ANISOU 3325 CA ASP A 437 3767 2714 2268 297 155 77 A C ATOM 3326 C ASP A 437 43.112 123.872 245.711 1.00 20.68 A C ANISOU 3326 C ASP A 437 3361 2367 2128 289 173 75 A C ATOM 3327 O ASP A 437 43.977 124.658 246.102 1.00 24.44 A O ANISOU 3327 O ASP A 437 3736 2869 2682 312 229 141 A O ATOM 3328 CB ASP A 437 41.539 124.469 243.881 1.00 24.77 A C ANISOU 3328 CB ASP A 437 3959 2942 2511 219 40 112 A C ATOM 3329 CG ASP A 437 41.358 124.673 242.397 1.00 28.61 A C ANISOU 3329 CG ASP A 437 4523 3501 2846 226 18 152 A C ATOM 3330 OD1 ASP A 437 42.374 124.832 241.687 1.00 31.49 A O ANISOU 3330 OD1 ASP A 437 4911 3930 3123 287 109 202 A O ATOM 3331 OD2 ASP A 437 40.192 124.703 241.948 1.00 32.42 A O1- ANISOU 3331 OD2 ASP A 437 5037 3985 3295 168 -92 139 A O1- ATOM 3332 N ILE A 438 42.377 123.133 246.533 1.00 19.67 A N ANISOU 3332 N ILE A 438 3256 2174 2045 249 122 -1 A N ATOM 3333 CA ILE A 438 42.528 123.215 247.979 1.00 17.42 A C ANISOU 3333 CA ILE A 438 2879 1852 1888 235 130 -9 A C ATOM 3334 C ILE A 438 43.839 122.576 248.431 1.00 23.79 A C ANISOU 3334 C ILE A 438 3692 2656 2691 314 224 -16 A C ATOM 3335 O ILE A 438 44.606 123.185 249.179 1.00 23.39 A O ANISOU 3335 O ILE A 438 3536 2625 2725 331 263 27 A O ATOM 3336 CB ILE A 438 41.344 122.531 248.684 1.00 19.08 A C ANISOU 3336 CB ILE A 438 3115 2002 2134 169 56 -77 A C ATOM 3337 CG1 ILE A 438 40.023 123.142 248.210 1.00 16.36 A C ANISOU 3337 CG1 ILE A 438 2750 1665 1801 95 -41 -69 A C ATOM 3338 CG2 ILE A 438 41.485 122.611 250.203 1.00 15.80 A C ANISOU 3338 CG2 ILE A 438 2609 1563 1832 154 69 -83 A C ATOM 3339 CD1 ILE A 438 38.788 122.366 248.652 1.00 19.32 A C ANISOU 3339 CD1 ILE A 438 3157 1988 2195 24 -115 -135 A C ATOM 3340 N ALA A 439 44.103 121.364 247.951 1.00 23.93 A N ANISOU 3340 N ALA A 439 3831 2648 2612 363 257 -72 A N ATOM 3341 CA ALA A 439 45.288 120.611 248.355 1.00 21.34 A C ANISOU 3341 CA ALA A 439 3517 2308 2285 448 342 -82 A C ATOM 3342 C ALA A 439 46.582 121.328 247.998 1.00 19.25 A C ANISOU 3342 C ALA A 439 3175 2118 2020 516 432 -9 A C ATOM 3343 O ALA A 439 47.514 121.351 248.794 1.00 23.42 A O ANISOU 3343 O ALA A 439 3625 2655 2619 557 481 19 A O ATOM 3344 CB ALA A 439 45.273 119.215 247.741 1.00 20.32 A C ANISOU 3344 CB ALA A 439 3541 2125 2054 494 361 -164 A C ATOM 3345 N LEU A 440 46.641 121.913 246.806 1.00 17.38 A N ANISOU 3345 N LEU A 440 2957 1942 1705 523 451 31 A N ATOM 3346 CA LEU A 440 47.874 122.551 246.346 1.00 24.38 A C ANISOU 3346 CA LEU A 440 3773 2906 2584 583 546 110 A C ATOM 3347 C LEU A 440 48.100 123.935 246.966 1.00 24.16 A C ANISOU 3347 C LEU A 440 3588 2905 2688 534 532 198 A C ATOM 3348 O LEU A 440 49.201 124.483 246.881 1.00 26.22 A O ANISOU 3348 O LEU A 440 3762 3219 2982 572 606 269 A O ATOM 3349 CB LEU A 440 47.943 122.612 244.816 1.00 27.59 A C ANISOU 3349 CB LEU A 440 4263 3377 2843 613 586 128 A C ATOM 3350 CG LEU A 440 48.047 121.250 244.120 1.00 34.56 A C ANISOU 3350 CG LEU A 440 5301 4241 3588 683 627 32 A C ATOM 3351 CD1 LEU A 440 48.265 121.410 242.625 1.00 32.39 A C ANISOU 3351 CD1 LEU A 440 5101 4055 3152 719 680 53 A C ATOM 3352 CD2 LEU A 440 49.144 120.396 244.731 1.00 38.07 A C ANISOU 3352 CD2 LEU A 440 5735 4659 4072 777 715 2 A C ATOM 3353 N THR A 441 47.058 124.511 247.561 1.00 20.51 A N ANISOU 3353 N THR A 441 3085 2404 2305 450 437 191 A N ATOM 3354 CA THR A 441 47.242 125.726 248.348 1.00 24.35 A C ANISOU 3354 CA THR A 441 3427 2893 2930 405 418 247 A C ATOM 3355 C THR A 441 48.055 125.339 249.577 1.00 25.01 A C ANISOU 3355 C THR A 441 3447 2966 3088 434 448 224 A C ATOM 3356 O THR A 441 47.748 124.344 250.242 1.00 21.58 A O ANISOU 3356 O THR A 441 3068 2490 2641 442 428 156 A O ATOM 3357 CB THR A 441 45.894 126.336 248.785 1.00 27.63 A C ANISOU 3357 CB THR A 441 3817 3267 3417 320 314 228 A C ATOM 3358 CG2 THR A 441 46.115 127.565 249.666 1.00 27.94 A C ANISOU 3358 CG2 THR A 441 3713 3298 3606 280 298 266 A C ATOM 3359 OG1 THR A 441 45.154 126.740 247.626 1.00 25.68 A O ANISOU 3359 OG1 THR A 441 3618 3036 3104 295 275 262 A O ATOM 3360 N ILE A 442 49.110 126.096 249.867 1.00 18.10 A N ANISOU 3360 N ILE A 442 2457 2129 2292 448 494 287 A N ATOM 3361 CA ILE A 442 49.966 125.769 251.008 1.00 17.13 A C ANISOU 3361 CA ILE A 442 2265 2010 2236 477 515 273 A C ATOM 3362 C ILE A 442 49.351 126.302 252.304 1.00 21.40 A C ANISOU 3362 C ILE A 442 2735 2516 2879 405 436 237 A C ATOM 3363 O ILE A 442 49.280 127.515 252.508 1.00 20.64 A O ANISOU 3363 O ILE A 442 2545 2421 2874 351 407 267 A O ATOM 3364 CB ILE A 442 51.408 126.312 250.836 1.00 19.67 A C ANISOU 3364 CB ILE A 442 2478 2392 2602 518 592 352 A C ATOM 3365 CG1 ILE A 442 52.031 125.788 249.542 1.00 22.22 A C ANISOU 3365 CG1 ILE A 442 2867 2763 2814 596 686 386 A C ATOM 3366 CG2 ILE A 442 52.274 125.914 252.023 1.00 15.88 A C ANISOU 3366 CG2 ILE A 442 1924 1923 2186 549 599 337 A C ATOM 3367 CD1 ILE A 442 53.441 126.301 249.282 1.00 22.76 A C ANISOU 3367 CD1 ILE A 442 2820 2902 2926 637 775 473 A C ATOM 3368 N HIS A 443 48.888 125.393 253.163 1.00 18.14 A N ANISOU 3368 N HIS A 443 2371 2072 2450 404 403 171 A N ATOM 3369 CA HIS A 443 48.309 125.775 254.444 1.00 22.75 A C ANISOU 3369 CA HIS A 443 2896 2638 3109 342 340 131 A C ATOM 3370 C HIS A 443 49.404 125.807 255.500 1.00 23.59 A C ANISOU 3370 C HIS A 443 2912 2780 3271 365 355 142 A C ATOM 3371 O HIS A 443 50.272 124.938 255.515 1.00 22.56 A O ANISOU 3371 O HIS A 443 2801 2667 3102 436 400 158 A O ATOM 3372 CB HIS A 443 47.216 124.779 254.851 1.00 20.14 A C ANISOU 3372 CB HIS A 443 2660 2263 2729 320 299 67 A C ATOM 3373 CG HIS A 443 46.051 124.738 253.912 1.00 22.78 A C ANISOU 3373 CG HIS A 443 3074 2566 3017 286 266 50 A C ATOM 3374 CD2 HIS A 443 44.746 125.066 254.093 1.00 20.75 A C ANISOU 3374 CD2 HIS A 443 2817 2283 2785 217 203 17 A C ATOM 3375 ND1 HIS A 443 46.156 124.324 252.597 1.00 19.82 A N ANISOU 3375 ND1 HIS A 443 2785 2191 2554 324 297 66 A N ATOM 3376 CE1 HIS A 443 44.975 124.398 252.017 1.00 20.35 A C ANISOU 3376 CE1 HIS A 443 2905 2235 2592 276 243 46 A C ATOM 3377 NE2 HIS A 443 44.099 124.842 252.902 1.00 19.31 A N ANISOU 3377 NE2 HIS A 443 2716 2085 2535 211 186 19 A N ATOM 3378 N ALA A 444 49.359 126.793 256.393 1.00 19.63 A N ANISOU 3378 N ALA A 444 2309 2289 2859 309 312 128 A N ATOM 3379 CA ALA A 444 50.391 126.912 257.423 1.00 22.46 A C ANISOU 3379 CA ALA A 444 2575 2691 3267 321 311 134 A C ATOM 3380 C ALA A 444 50.399 125.715 258.373 1.00 23.05 A C ANISOU 3380 C ALA A 444 2697 2773 3288 351 299 104 A C ATOM 3381 O ALA A 444 49.347 125.164 258.711 1.00 21.56 A O ANISOU 3381 O ALA A 444 2583 2552 3058 325 271 60 A O ATOM 3382 CB ALA A 444 50.215 128.195 258.205 1.00 19.06 A C ANISOU 3382 CB ALA A 444 2042 2263 2937 249 259 105 A C ATOM 3383 N HIS A 445 51.597 125.326 258.799 1.00 22.64 A N ANISOU 3383 N HIS A 445 2595 2765 3243 406 321 138 A N ATOM 3384 CA HIS A 445 51.792 124.224 259.738 1.00 22.09 A C ANISOU 3384 CA HIS A 445 2558 2706 3130 443 308 132 A C ATOM 3385 C HIS A 445 52.605 124.739 260.922 1.00 25.96 A C ANISOU 3385 C HIS A 445 2929 3262 3672 427 268 137 A C ATOM 3386 O HIS A 445 53.561 125.490 260.737 1.00 26.95 A O ANISOU 3386 O HIS A 445 2952 3427 3862 431 279 169 A O ATOM 3387 CB HIS A 445 52.544 123.081 259.057 1.00 20.61 A C ANISOU 3387 CB HIS A 445 2429 2506 2895 545 370 175 A C ATOM 3388 CG HIS A 445 52.844 121.924 259.958 1.00 27.74 A C ANISOU 3388 CG HIS A 445 3363 3407 3768 595 357 185 A C ATOM 3389 CD2 HIS A 445 53.949 121.618 260.684 1.00 31.59 A C ANISOU 3389 CD2 HIS A 445 3778 3946 4279 650 352 229 A C ATOM 3390 ND1 HIS A 445 51.946 120.898 260.186 1.00 28.46 A N ANISOU 3390 ND1 HIS A 445 3572 3438 3804 591 342 160 A N ATOM 3391 CE1 HIS A 445 52.485 120.016 261.007 1.00 28.47 A C ANISOU 3391 CE1 HIS A 445 3576 3446 3794 643 332 193 A C ATOM 3392 NE2 HIS A 445 53.699 120.426 261.324 1.00 29.74 A N ANISOU 3392 NE2 HIS A 445 3622 3678 4000 683 335 235 A N ATOM 3393 N PRO A 446 52.217 124.365 262.149 1.00 26.51 A N ANISOU 3393 N PRO A 446 3009 3351 3712 401 218 105 A N ATOM 3394 CA PRO A 446 51.081 123.509 262.493 1.00 24.05 A C ANISOU 3394 CA PRO A 446 2806 2999 3333 383 205 76 A C ATOM 3395 C PRO A 446 49.847 124.313 262.905 1.00 22.26 A C ANISOU 3395 C PRO A 446 2575 2765 3120 291 168 7 A C ATOM 3396 O PRO A 446 49.883 125.080 263.870 1.00 16.15 A O ANISOU 3396 O PRO A 446 1723 2041 2372 245 128 -31 A O ATOM 3397 CB PRO A 446 51.616 122.722 263.686 1.00 23.24 A C ANISOU 3397 CB PRO A 446 2693 2943 3195 414 178 103 A C ATOM 3398 CG PRO A 446 52.552 123.695 264.378 1.00 23.00 A C ANISOU 3398 CG PRO A 446 2528 2994 3216 395 141 101 A C ATOM 3399 CD PRO A 446 53.058 124.659 263.326 1.00 24.28 A C ANISOU 3399 CD PRO A 446 2625 3145 3453 394 172 110 A C ATOM 3400 N THR A 447 48.753 124.126 262.171 1.00 20.20 A N ANISOU 3400 N THR A 447 2393 2443 2839 268 180 -14 A N ATOM 3401 CA THR A 447 47.492 124.789 262.482 1.00 19.33 A C ANISOU 3401 CA THR A 447 2277 2322 2747 191 150 -75 A C ATOM 3402 C THR A 447 46.378 123.766 262.466 1.00 18.44 A C ANISOU 3402 C THR A 447 2265 2166 2576 174 151 -84 A C ATOM 3403 O THR A 447 46.563 122.652 261.981 1.00 16.37 A O ANISOU 3403 O THR A 447 2087 1865 2267 219 173 -49 A O ATOM 3404 CB THR A 447 47.137 125.862 261.434 1.00 20.68 A C ANISOU 3404 CB THR A 447 2420 2457 2980 167 153 -84 A C ATOM 3405 CG2 THR A 447 48.204 126.925 261.370 1.00 11.95 A C ANISOU 3405 CG2 THR A 447 1211 1380 1948 173 154 -66 A C ATOM 3406 OG1 THR A 447 47.010 125.242 260.145 1.00 18.81 A O ANISOU 3406 OG1 THR A 447 2268 2174 2705 203 184 -48 A O ATOM 3407 N LEU A 448 45.216 124.142 262.984 1.00 19.99 A N ANISOU 3407 N LEU A 448 2449 2366 2780 108 128 -135 A N ATOM 3408 CA LEU A 448 44.044 123.285 262.870 1.00 17.00 A C ANISOU 3408 CA LEU A 448 2152 1945 2362 76 126 -142 A C ATOM 3409 C LEU A 448 43.478 123.363 261.453 1.00 22.58 A C ANISOU 3409 C LEU A 448 2907 2590 3083 73 127 -142 A C ATOM 3410 O LEU A 448 42.974 122.368 260.921 1.00 19.70 A O ANISOU 3410 O LEU A 448 2634 2174 2677 72 129 -132 A O ATOM 3411 CB LEU A 448 42.977 123.696 263.887 1.00 20.29 A C ANISOU 3411 CB LEU A 448 2526 2399 2786 8 109 -194 A C ATOM 3412 CG LEU A 448 43.417 123.638 265.356 1.00 22.63 A C ANISOU 3412 CG LEU A 448 2780 2773 3044 3 105 -202 A C ATOM 3413 CD1 LEU A 448 42.336 124.173 266.291 1.00 18.18 A C ANISOU 3413 CD1 LEU A 448 2169 2257 2481 -61 101 -265 A C ATOM 3414 CD2 LEU A 448 43.781 122.198 265.736 1.00 19.88 A C ANISOU 3414 CD2 LEU A 448 2510 2420 2625 32 115 -137 A C ATOM 3415 N HIS A 449 43.575 124.538 260.832 1.00 16.97 A N ANISOU 3415 N HIS A 449 2137 1881 2430 70 121 -150 A N ATOM 3416 CA HIS A 449 42.925 124.721 259.538 1.00 17.98 A C ANISOU 3416 CA HIS A 449 2305 1964 2564 61 112 -144 A C ATOM 3417 C HIS A 449 43.636 124.004 258.387 1.00 17.34 A C ANISOU 3417 C HIS A 449 2306 1856 2428 120 141 -102 A C ATOM 3418 O HIS A 449 43.025 123.751 257.347 1.00 19.11 A O ANISOU 3418 O HIS A 449 2596 2044 2621 112 130 -102 A O ATOM 3419 CB HIS A 449 42.666 126.210 259.212 1.00 19.42 A C ANISOU 3419 CB HIS A 449 2401 2148 2830 36 92 -154 A C ATOM 3420 CG HIS A 449 43.863 126.946 258.699 1.00 17.21 A C ANISOU 3420 CG HIS A 449 2075 1880 2585 75 114 -112 A C ATOM 3421 CD2 HIS A 449 44.374 127.048 257.445 1.00 14.98 A C ANISOU 3421 CD2 HIS A 449 1821 1585 2286 109 135 -58 A C ATOM 3422 ND1 HIS A 449 44.695 127.687 259.514 1.00 17.76 A N ANISOU 3422 ND1 HIS A 449 2054 1983 2711 75 116 -121 A N ATOM 3423 CE1 HIS A 449 45.662 128.219 258.783 1.00 19.67 A C ANISOU 3423 CE1 HIS A 449 2264 2227 2983 104 138 -69 A C ATOM 3424 NE2 HIS A 449 45.494 127.844 257.528 1.00 16.23 A N ANISOU 3424 NE2 HIS A 449 1900 1768 2500 128 156 -26 A N ATOM 3425 N GLU A 450 44.906 123.646 258.574 1.00 15.45 A N ANISOU 3425 N GLU A 450 2062 1638 2172 180 177 -70 A N ATOM 3426 CA GLU A 450 45.610 122.906 257.528 1.00 21.08 A C ANISOU 3426 CA GLU A 450 2851 2327 2830 248 218 -39 A C ATOM 3427 C GLU A 450 44.937 121.563 257.253 1.00 20.47 A C ANISOU 3427 C GLU A 450 2898 2190 2688 249 212 -61 A C ATOM 3428 O GLU A 450 45.065 121.009 256.157 1.00 21.11 A O ANISOU 3428 O GLU A 450 3064 2239 2717 287 234 -61 A O ATOM 3429 CB GLU A 450 47.106 122.736 257.844 1.00 23.10 A C ANISOU 3429 CB GLU A 450 3065 2621 3093 321 261 1 A C ATOM 3430 CG GLU A 450 47.427 121.774 258.975 1.00 30.23 A C ANISOU 3430 CG GLU A 450 3982 3526 3979 344 257 5 A C ATOM 3431 CD GLU A 450 48.926 121.553 259.143 1.00 34.76 A C ANISOU 3431 CD GLU A 450 4510 4138 4562 426 295 52 A C ATOM 3432 OE1 GLU A 450 49.589 121.179 258.148 1.00 32.68 A O ANISOU 3432 OE1 GLU A 450 4282 3859 4275 496 346 75 A O ATOM 3433 OE2 GLU A 450 49.440 121.764 260.265 1.00 33.01 A O1- ANISOU 3433 OE2 GLU A 450 4210 3966 4367 422 273 64 A O1- ATOM 3434 N SER A 451 44.187 121.072 258.238 1.00 19.89 A N ANISOU 3434 N SER A 451 2835 2103 2619 200 183 -82 A N ATOM 3435 CA SER A 451 43.397 119.860 258.068 1.00 20.96 A C ANISOU 3435 CA SER A 451 3080 2171 2713 179 169 -101 A C ATOM 3436 C SER A 451 42.514 119.949 256.819 1.00 22.56 A C ANISOU 3436 C SER A 451 3340 2339 2893 145 142 -129 A C ATOM 3437 O SER A 451 42.339 118.947 256.116 1.00 24.07 A O ANISOU 3437 O SER A 451 3642 2469 3034 159 142 -148 A O ATOM 3438 CB SER A 451 42.586 119.537 259.334 1.00 17.98 A C ANISOU 3438 CB SER A 451 2683 1797 2351 113 143 -108 A C ATOM 3439 OG SER A 451 41.628 120.543 259.623 1.00 15.87 A O ANISOU 3439 OG SER A 451 2337 1567 2126 42 113 -136 A O ATOM 3440 N VAL A 452 42.007 121.150 256.520 1.00 24.51 A N ANISOU 3440 N VAL A 452 3514 2622 3177 106 116 -133 A N ATOM 3441 CA VAL A 452 41.209 121.355 255.306 1.00 12.47 A C ANISOU 3441 CA VAL A 452 2033 1079 1627 78 81 -147 A C ATOM 3442 C VAL A 452 42.023 120.889 254.102 1.00 17.67 A C ANISOU 3442 C VAL A 452 2779 1725 2211 148 117 -138 A C ATOM 3443 O VAL A 452 41.619 119.943 253.387 1.00 20.52 A O ANISOU 3443 O VAL A 452 3253 2037 2508 145 102 -171 A O ATOM 3444 CB VAL A 452 40.767 122.836 255.156 1.00 18.08 A C ANISOU 3444 CB VAL A 452 2640 1830 2401 44 53 -135 A C ATOM 3445 CG1 VAL A 452 40.068 123.073 253.818 1.00 12.52 A C ANISOU 3445 CG1 VAL A 452 1978 1116 1662 26 11 -131 A C ATOM 3446 CG2 VAL A 452 39.844 123.213 256.297 1.00 15.20 A C ANISOU 3446 CG2 VAL A 452 2196 1476 2105 -19 23 -161 A C ATOM 3447 N GLY A 453 43.211 121.471 253.949 1.00 17.63 A N ANISOU 3447 N GLY A 453 2724 1763 2213 211 168 -99 A N ATOM 3448 CA GLY A 453 44.117 121.055 252.896 1.00 20.27 A C ANISOU 3448 CA GLY A 453 3127 2100 2474 288 222 -86 A C ATOM 3449 C GLY A 453 44.358 119.557 252.966 1.00 21.21 A C ANISOU 3449 C GLY A 453 3356 2158 2544 332 246 -122 A C ATOM 3450 O GLY A 453 44.316 118.850 251.945 1.00 23.19 A O ANISOU 3450 O GLY A 453 3719 2376 2716 362 257 -155 A O ATOM 3451 N LEU A 454 44.561 119.050 254.179 1.00 17.43 A N ANISOU 3451 N LEU A 454 2853 1659 2110 335 248 -117 A N ATOM 3452 CA LEU A 454 44.963 117.659 254.285 1.00 21.97 A C ANISOU 3452 CA LEU A 454 3526 2167 2655 390 275 -135 A C ATOM 3453 C LEU A 454 43.807 116.791 253.826 1.00 21.55 A C ANISOU 3453 C LEU A 454 3590 2033 2565 333 227 -191 A C ATOM 3454 O LEU A 454 44.025 115.787 253.137 1.00 18.74 A O ANISOU 3454 O LEU A 454 3351 1611 2158 382 248 -229 A O ATOM 3455 CB LEU A 454 45.463 117.318 255.693 1.00 22.28 A C ANISOU 3455 CB LEU A 454 3511 2207 2746 407 283 -100 A C ATOM 3456 CG LEU A 454 46.780 118.035 256.029 1.00 25.34 A C ANISOU 3456 CG LEU A 454 3790 2673 3166 472 328 -49 A C ATOM 3457 CD1 LEU A 454 47.133 117.945 257.501 1.00 23.46 A C ANISOU 3457 CD1 LEU A 454 3480 2461 2973 468 314 -14 A C ATOM 3458 CD2 LEU A 454 47.913 117.461 255.190 1.00 20.02 A C ANISOU 3458 CD2 LEU A 454 3163 1988 2456 585 398 -41 A C ATOM 3459 N ALA A 455 42.581 117.234 254.113 1.00 19.26 A N ANISOU 3459 N ALA A 455 3265 1748 2303 232 163 -202 A N ATOM 3460 CA ALA A 455 41.428 116.430 253.727 1.00 18.77 A C ANISOU 3460 CA ALA A 455 3299 1614 2220 163 107 -252 A C ATOM 3461 C ALA A 455 41.433 116.353 252.218 1.00 22.50 A C ANISOU 3461 C ALA A 455 3860 2079 2608 190 103 -293 A C ATOM 3462 O ALA A 455 41.234 115.274 251.641 1.00 22.54 A O ANISOU 3462 O ALA A 455 3991 2006 2566 195 92 -348 A O ATOM 3463 CB ALA A 455 40.137 117.050 254.232 1.00 20.41 A C ANISOU 3463 CB ALA A 455 3431 1847 2478 55 44 -251 A C ATOM 3464 N ALA A 456 41.743 117.483 251.581 1.00 19.00 A N ANISOU 3464 N ALA A 456 3356 1718 2145 210 116 -265 A N ATOM 3465 CA ALA A 456 41.743 117.529 250.128 1.00 20.18 A C ANISOU 3465 CA ALA A 456 3585 1885 2199 233 114 -291 A C ATOM 3466 C ALA A 456 42.762 116.526 249.616 1.00 23.89 A C ANISOU 3466 C ALA A 456 4161 2315 2601 333 185 -326 A C ATOM 3467 O ALA A 456 42.486 115.774 248.667 1.00 27.18 A O ANISOU 3467 O ALA A 456 4705 2690 2933 340 171 -394 A O ATOM 3468 CB ALA A 456 42.067 118.931 249.634 1.00 20.33 A C ANISOU 3468 CB ALA A 456 3510 1998 2215 246 128 -231 A C ATOM 3469 N GLU A 457 43.913 116.468 250.288 1.00 21.78 A N ANISOU 3469 N GLU A 457 3842 2060 2376 412 259 -286 A N ATOM 3470 CA GLU A 457 44.961 115.544 249.867 1.00 22.12 A C ANISOU 3470 CA GLU A 457 3967 2066 2370 523 337 -314 A C ATOM 3471 C GLU A 457 44.478 114.097 249.955 1.00 23.95 A C ANISOU 3471 C GLU A 457 4332 2171 2595 515 309 -386 A C ATOM 3472 O GLU A 457 44.815 113.268 249.098 1.00 25.35 A O ANISOU 3472 O GLU A 457 4630 2298 2702 580 344 -452 A O ATOM 3473 CB GLU A 457 46.245 115.738 250.681 1.00 21.75 A C ANISOU 3473 CB GLU A 457 3821 2056 2386 605 409 -249 A C ATOM 3474 CG GLU A 457 47.025 117.000 250.333 1.00 30.92 A C ANISOU 3474 CG GLU A 457 4869 3332 3548 635 457 -184 A C ATOM 3475 CD GLU A 457 48.322 117.119 251.121 1.00 45.74 A C ANISOU 3475 CD GLU A 457 6643 5245 5490 712 520 -125 A C ATOM 3476 OE1 GLU A 457 48.860 116.073 251.553 1.00 51.34 A O ANISOU 3476 OE1 GLU A 457 7396 5897 6216 782 550 -138 A O ATOM 3477 OE2 GLU A 457 48.814 118.257 251.292 1.00 48.97 A O1- ANISOU 3477 OE2 GLU A 457 6927 5736 5941 703 535 -62 A O1- ATOM 3478 N VAL A 458 43.663 113.804 250.967 1.00 23.57 A N ANISOU 3478 N VAL A 458 4264 2069 2621 431 248 -377 A N ATOM 3479 CA VAL A 458 43.165 112.445 251.129 1.00 21.08 A C ANISOU 3479 CA VAL A 458 4068 1622 2318 409 218 -432 A C ATOM 3480 C VAL A 458 42.378 112.107 249.872 1.00 24.58 A C ANISOU 3480 C VAL A 458 4631 2031 2678 365 168 -522 A C ATOM 3481 O VAL A 458 42.515 111.007 249.324 1.00 25.29 A O ANISOU 3481 O VAL A 458 4842 2032 2734 401 177 -592 A O ATOM 3482 CB VAL A 458 42.278 112.291 252.381 1.00 23.87 A C ANISOU 3482 CB VAL A 458 4371 1941 2759 307 159 -394 A C ATOM 3483 CG1 VAL A 458 41.548 110.950 252.355 1.00 24.26 A C ANISOU 3483 CG1 VAL A 458 4547 1848 2822 256 115 -449 A C ATOM 3484 CG2 VAL A 458 43.129 112.389 253.648 1.00 19.89 A C ANISOU 3484 CG2 VAL A 458 3774 1464 2319 358 205 -314 A C ATOM 3485 N PHE A 459 41.604 113.074 249.377 1.00 22.04 A N ANISOU 3485 N PHE A 459 4259 1790 2324 290 113 -516 A N ATOM 3486 CA PHE A 459 40.860 112.843 248.146 1.00 26.45 A C ANISOU 3486 CA PHE A 459 4923 2336 2790 246 54 -595 A C ATOM 3487 C PHE A 459 41.802 112.715 246.961 1.00 25.87 A C ANISOU 3487 C PHE A 459 4937 2295 2600 355 124 -639 A C ATOM 3488 O PHE A 459 41.603 111.858 246.100 1.00 30.04 A O ANISOU 3488 O PHE A 459 5599 2765 3051 361 106 -733 A O ATOM 3489 CB PHE A 459 39.832 113.947 247.885 1.00 23.11 A C ANISOU 3489 CB PHE A 459 4417 1999 2365 148 -27 -564 A C ATOM 3490 CG PHE A 459 39.049 113.751 246.612 1.00 21.98 A C ANISOU 3490 CG PHE A 459 4375 1859 2119 99 -102 -637 A C ATOM 3491 CD1 PHE A 459 37.892 112.986 246.601 1.00 25.12 A C ANISOU 3491 CD1 PHE A 459 4835 2174 2536 -4 -198 -700 A C ATOM 3492 CD2 PHE A 459 39.469 114.338 245.428 1.00 21.23 A C ANISOU 3492 CD2 PHE A 459 4308 1854 1903 152 -80 -639 A C ATOM 3493 CE1 PHE A 459 37.168 112.804 245.419 1.00 26.32 A C ANISOU 3493 CE1 PHE A 459 5079 2335 2588 -55 -282 -773 A C ATOM 3494 CE2 PHE A 459 38.752 114.169 244.249 1.00 26.60 A C ANISOU 3494 CE2 PHE A 459 5086 2550 2472 106 -158 -706 A C ATOM 3495 CZ PHE A 459 37.598 113.401 244.246 1.00 25.83 A C ANISOU 3495 CZ PHE A 459 5050 2370 2393 2 -264 -778 A C ATOM 3496 N GLU A 460 42.854 113.530 246.937 1.00 24.93 A N ANISOU 3496 N GLU A 460 4731 2271 2471 439 208 -572 A N ATOM 3497 CA GLU A 460 43.728 113.560 245.769 1.00 27.80 A C ANISOU 3497 CA GLU A 460 5158 2692 2715 539 286 -600 A C ATOM 3498 C GLU A 460 44.594 112.306 245.711 1.00 31.07 A C ANISOU 3498 C GLU A 460 5675 3013 3116 649 364 -667 A C ATOM 3499 O GLU A 460 45.108 111.943 244.652 1.00 29.85 A O ANISOU 3499 O GLU A 460 5579 2893 2868 713 412 -714 A O ATOM 3500 CB GLU A 460 44.611 114.816 245.781 1.00 27.28 A C ANISOU 3500 CB GLU A 460 4956 2754 2657 589 357 -496 A C ATOM 3501 CG GLU A 460 43.869 116.092 245.387 1.00 26.97 A C ANISOU 3501 CG GLU A 460 4841 2807 2599 504 291 -438 A C ATOM 3502 CD GLU A 460 43.513 116.107 243.907 1.00 39.22 A C ANISOU 3502 CD GLU A 460 6499 4408 3994 500 269 -486 A C ATOM 3503 OE1 GLU A 460 44.393 116.434 243.081 1.00 43.27 A O ANISOU 3503 OE1 GLU A 460 7023 5004 4415 581 355 -462 A O ATOM 3504 OE2 GLU A 460 42.358 115.767 243.566 1.00 41.18 A O1- ANISOU 3504 OE2 GLU A 460 6820 4618 4208 416 166 -546 A O1- ATOM 3505 N GLY A 461 44.745 111.652 246.857 1.00 28.19 A N ANISOU 3505 N GLY A 461 5270 2567 2873 649 362 -640 A N ATOM 3506 CA GLY A 461 45.580 110.473 246.962 1.00 28.90 A C ANISOU 3506 CA GLY A 461 5384 2596 3002 733 415 -658 A C ATOM 3507 C GLY A 461 47.043 110.831 247.132 1.00 27.75 A C ANISOU 3507 C GLY A 461 5156 2518 2870 862 528 -596 A C ATOM 3508 O GLY A 461 47.921 110.009 246.869 1.00 30.89 A O ANISOU 3508 O GLY A 461 5571 2893 3272 953 589 -617 A O ATOM 3509 N SER A 462 47.311 112.046 247.604 1.00 28.15 A N ANISOU 3509 N SER A 462 5107 2650 2939 869 555 -519 A N ATOM 3510 CA SER A 462 48.689 112.504 247.737 1.00 29.31 A C ANISOU 3510 CA SER A 462 5152 2879 3106 980 658 -451 A C ATOM 3511 C SER A 462 49.101 112.627 249.195 1.00 27.28 A C ANISOU 3511 C SER A 462 4782 2608 2974 988 654 -369 A C ATOM 3512 O SER A 462 50.273 112.868 249.491 1.00 26.70 A O ANISOU 3512 O SER A 462 4611 2593 2940 1077 727 -308 A O ATOM 3513 CB SER A 462 48.850 113.877 247.085 1.00 28.67 A C ANISOU 3513 CB SER A 462 4990 2937 2966 964 685 -398 A C ATOM 3514 OG SER A 462 47.978 114.816 247.688 1.00 28.19 A O ANISOU 3514 OG SER A 462 4841 2910 2962 840 596 -344 A O ATOM 3515 N ILE A 463 48.135 112.452 250.093 1.00 22.56 A N ANISOU 3515 N ILE A 463 4185 1949 2439 885 564 -362 A N ATOM 3516 CA ILE A 463 48.346 112.623 251.529 1.00 24.26 A C ANISOU 3516 CA ILE A 463 4290 2172 2758 866 542 -281 A C ATOM 3517 C ILE A 463 49.531 111.797 252.038 1.00 25.20 A C ANISOU 3517 C ILE A 463 4401 2247 2926 993 606 -252 A C ATOM 3518 O ILE A 463 49.683 110.622 251.684 1.00 24.89 A O ANISOU 3518 O ILE A 463 4441 2135 2882 1028 612 -295 A O ATOM 3519 CB ILE A 463 47.068 112.225 252.305 1.00 28.10 A C ANISOU 3519 CB ILE A 463 4813 2579 3285 746 447 -292 A C ATOM 3520 CG1 ILE A 463 47.244 112.397 253.816 1.00 28.24 A C ANISOU 3520 CG1 ILE A 463 4723 2619 3389 723 426 -210 A C ATOM 3521 CG2 ILE A 463 46.653 110.800 251.962 1.00 25.79 A C ANISOU 3521 CG2 ILE A 463 4677 2142 2980 754 431 -366 A C ATOM 3522 CD1 ILE A 463 46.944 113.796 254.315 1.00 22.61 A C ANISOU 3522 CD1 ILE A 463 3872 2022 2698 643 394 -164 A C ATOM 3523 N THR A 464 50.392 112.424 252.838 1.00 23.39 A N ANISOU 3523 N THR A 464 4028 2103 2756 1027 628 -166 A N ATOM 3524 CA THR A 464 51.501 111.702 253.459 1.00 25.61 A C ANISOU 3524 CA THR A 464 4270 2364 3096 1134 668 -119 A C ATOM 3525 C THR A 464 51.473 111.797 254.988 1.00 27.87 A C ANISOU 3525 C THR A 464 4474 2655 3458 1099 614 -40 A C ATOM 3526 O THR A 464 52.249 111.122 255.673 1.00 30.88 A O ANISOU 3526 O THR A 464 4830 3012 3893 1177 627 10 A O ATOM 3527 CB THR A 464 52.890 112.162 252.928 1.00 31.34 A C ANISOU 3527 CB THR A 464 4893 3197 3818 1235 755 -83 A C ATOM 3528 CG2 THR A 464 53.073 111.784 251.451 1.00 22.28 A C ANISOU 3528 CG2 THR A 464 3829 2049 2586 1278 813 -155 A C ATOM 3529 OG1 THR A 464 53.028 113.579 253.095 1.00 23.96 A O ANISOU 3529 OG1 THR A 464 3835 2376 2894 1198 759 -32 A O ATOM 3530 N ASP A 465 50.581 112.626 255.523 1.00 26.52 A N ANISOU 3530 N ASP A 465 4251 2535 3290 969 547 -28 A N ATOM 3531 CA ASP A 465 50.414 112.724 256.976 1.00 35.47 A C ANISOU 3531 CA ASP A 465 5312 3692 4475 915 490 35 A C ATOM 3532 C ASP A 465 49.425 111.690 257.527 1.00 31.54 A C ANISOU 3532 C ASP A 465 4920 3079 3986 855 439 26 A C ATOM 3533 O ASP A 465 49.255 111.573 258.737 1.00 32.32 A O ANISOU 3533 O ASP A 465 4977 3189 4115 815 398 84 A O ATOM 3534 CB ASP A 465 50.027 114.144 257.408 1.00 43.69 A C ANISOU 3534 CB ASP A 465 6233 4846 5521 815 451 51 A C ATOM 3535 CG ASP A 465 51.236 114.995 257.783 1.00 53.94 A C ANISOU 3535 CG ASP A 465 7383 6256 6854 865 476 108 A C ATOM 3536 OD1 ASP A 465 52.352 114.445 257.910 1.00 56.28 A O ANISOU 3536 OD1 ASP A 465 7656 6553 7176 975 517 148 A O ATOM 3537 OD2 ASP A 465 51.067 116.218 257.965 1.00 60.72 A O1- ANISOU 3537 OD2 ASP A 465 8146 7199 7726 795 453 112 A O1- ATOM 3538 N LEU A 466 48.773 110.958 256.625 1.00 27.86 A N ANISOU 3538 N LEU A 466 4590 2505 3490 844 440 -46 A N ATOM 3539 CA LEU A 466 47.976 109.785 256.983 1.00 25.94 A C ANISOU 3539 CA LEU A 466 4461 2126 3268 800 401 -57 A C ATOM 3540 C LEU A 466 48.413 108.624 256.122 1.00 28.92 A C ANISOU 3540 C LEU A 466 4948 2397 3643 887 437 -110 A C ATOM 3541 O LEU A 466 49.036 108.836 255.077 1.00 28.74 A O ANISOU 3541 O LEU A 466 4922 2421 3579 953 487 -157 A O ATOM 3542 CB LEU A 466 46.488 110.020 256.727 1.00 23.68 A C ANISOU 3542 CB LEU A 466 4219 1821 2959 656 340 -109 A C ATOM 3543 CG LEU A 466 45.771 111.076 257.545 1.00 25.30 A C ANISOU 3543 CG LEU A 466 4310 2133 3171 543 295 -73 A C ATOM 3544 CD1 LEU A 466 44.349 111.232 257.038 1.00 22.95 A C ANISOU 3544 CD1 LEU A 466 4057 1809 2854 421 243 -132 A C ATOM 3545 CD2 LEU A 466 45.783 110.632 258.988 1.00 23.62 A C ANISOU 3545 CD2 LEU A 466 4062 1914 2999 523 275 9 A C ATOM 3546 N PRO A 467 48.066 107.390 256.536 1.00 30.57 A N ANISOU 3546 N PRO A 467 5228 2490 3896 864 404 -101 A N ATOM 3547 CA PRO A 467 48.211 106.262 255.614 1.00 31.78 A C ANISOU 3547 CA PRO A 467 5471 2554 4051 903 417 -173 A C ATOM 3548 C PRO A 467 47.383 106.558 254.369 1.00 32.04 A C ANISOU 3548 C PRO A 467 5568 2594 4011 835 401 -279 A C ATOM 3549 O PRO A 467 46.333 107.195 254.488 1.00 33.21 A O ANISOU 3549 O PRO A 467 5716 2765 4139 723 352 -287 A O ATOM 3550 CB PRO A 467 47.613 105.089 256.401 1.00 34.23 A C ANISOU 3550 CB PRO A 467 5841 2735 4431 849 367 -139 A C ATOM 3551 CG PRO A 467 47.800 105.467 257.835 1.00 30.57 A C ANISOU 3551 CG PRO A 467 5302 2311 4003 845 354 -18 A C ATOM 3552 CD PRO A 467 47.606 106.960 257.870 1.00 28.79 A C ANISOU 3552 CD PRO A 467 5003 2211 3725 809 359 -17 A C ATOM 3553 N ASN A 468 47.880 106.175 253.196 1.00 29.04 A N ANISOU 3553 N ASN A 468 5238 2208 3588 904 442 -355 A N ATOM 3554 CA ASN A 468 47.249 106.563 251.938 1.00 30.01 A C ANISOU 3554 CA ASN A 468 5419 2362 3623 855 430 -448 A C ATOM 3555 C ASN A 468 46.734 105.339 251.189 1.00 32.66 A C ANISOU 3555 C ASN A 468 5871 2583 3956 829 400 -543 A C ATOM 3556 O ASN A 468 47.503 104.650 250.517 1.00 37.48 A O ANISOU 3556 O ASN A 468 6522 3162 4556 925 451 -593 A O ATOM 3557 CB ASN A 468 48.244 107.339 251.076 1.00 24.35 A C ANISOU 3557 CB ASN A 468 4660 1759 2835 953 510 -460 A C ATOM 3558 CG ASN A 468 47.632 107.845 249.785 1.00 30.89 A C ANISOU 3558 CG ASN A 468 5547 2633 3555 908 499 -541 A C ATOM 3559 ND2 ASN A 468 48.477 108.334 248.886 1.00 33.22 A N ANISOU 3559 ND2 ASN A 468 5825 3018 3779 994 574 -555 A N ATOM 3560 OD1 ASN A 468 46.413 107.820 249.605 1.00 34.66 A O ANISOU 3560 OD1 ASN A 468 6080 3074 4014 794 421 -583 A O ATOM 3561 N PRO A 469 45.433 105.040 251.326 1.00 34.05 A N ANISOU 3561 N PRO A 469 6094 2694 4150 699 318 -568 A N ATOM 3562 CA PRO A 469 44.918 103.848 250.638 1.00 41.38 A C ANISOU 3562 CA PRO A 469 7127 3508 5089 668 283 -661 A C ATOM 3563 C PRO A 469 44.811 104.025 249.125 1.00 37.23 A C ANISOU 3563 C PRO A 469 6666 3027 4453 678 290 -772 A C ATOM 3564 O PRO A 469 44.553 103.052 248.425 1.00 36.63 A O ANISOU 3564 O PRO A 469 6679 2865 4376 671 271 -864 A O ATOM 3565 CB PRO A 469 43.504 103.700 251.219 1.00 40.77 A C ANISOU 3565 CB PRO A 469 7054 3377 5059 513 193 -644 A C ATOM 3566 CG PRO A 469 43.532 104.457 252.513 1.00 38.26 A C ANISOU 3566 CG PRO A 469 6641 3114 4781 491 195 -528 A C ATOM 3567 CD PRO A 469 44.459 105.605 252.272 1.00 32.35 A C ANISOU 3567 CD PRO A 469 5830 2494 3969 581 258 -506 A C ATOM 3568 N LYS A 470 45.034 105.234 248.623 1.00 36.70 A N ANISOU 3568 N LYS A 470 6558 3092 4296 697 318 -762 A N ATOM 3569 CA LYS A 470 45.013 105.452 247.179 1.00 38.65 A C ANISOU 3569 CA LYS A 470 6868 3395 4422 715 330 -855 A C ATOM 3570 C LYS A 470 46.398 105.237 246.572 1.00 39.27 A C ANISOU 3570 C LYS A 470 6951 3507 4461 866 437 -877 A C ATOM 3571 O LYS A 470 46.602 105.395 245.367 1.00 40.52 A O ANISOU 3571 O LYS A 470 7158 3726 4512 903 469 -949 A O ATOM 3572 CB LYS A 470 44.465 106.840 246.844 1.00 36.15 A C ANISOU 3572 CB LYS A 470 6512 3198 4023 653 302 -832 A C ATOM 3573 CG LYS A 470 42.994 107.021 247.220 1.00 37.12 A C ANISOU 3573 CG LYS A 470 6633 3295 4178 499 192 -829 A C ATOM 3574 CD LYS A 470 42.402 108.283 246.589 1.00 38.81 A C ANISOU 3574 CD LYS A 470 6828 3618 4299 443 155 -829 A C ATOM 3575 CE LYS A 470 40.900 108.378 246.847 1.00 41.71 A C ANISOU 3575 CE LYS A 470 7185 3960 4703 290 40 -834 A C ATOM 3576 NZ LYS A 470 40.573 108.168 248.283 1.00 49.08 A N1+ ANISOU 3576 NZ LYS A 470 8050 4836 5764 236 22 -761 A N1+ ATOM 3577 N ALA A 471 47.349 104.890 247.430 1.00 37.33 A N ANISOU 3577 N ALA A 471 6647 3232 4304 953 490 -811 A N ATOM 3578 CA ALA A 471 48.717 104.637 247.008 1.00 41.83 A C ANISOU 3578 CA ALA A 471 7199 3833 4862 1098 592 -819 A C ATOM 3579 C ALA A 471 48.800 103.364 246.181 1.00 52.97 A C ANISOU 3579 C ALA A 471 8716 5143 6266 1140 603 -938 A C ATOM 3580 O ALA A 471 47.869 102.555 246.172 1.00 53.68 A O ANISOU 3580 O ALA A 471 8885 5119 6391 1057 528 -999 A O ATOM 3581 CB ALA A 471 49.624 104.527 248.213 1.00 40.15 A C ANISOU 3581 CB ALA A 471 6891 3608 4757 1171 629 -714 A C ATOM 3582 N LYS A 472 49.903 103.206 245.460 1.00 59.79 A N ANISOU 3582 N LYS A 472 9577 6051 7089 1264 697 -974 A N ATOM 3583 CA LYS A 472 50.219 101.918 244.863 1.00 66.25 A C ANISOU 3583 CA LYS A 472 10481 6762 7928 1330 723 -1083 A C ATOM 3584 C LYS A 472 51.725 101.699 244.871 1.00 66.90 A C ANISOU 3584 C LYS A 472 10498 6874 8045 1488 833 -1057 A C ATOM 3585 O LYS A 472 52.341 101.654 245.936 1.00 68.51 A O ANISOU 3585 O LYS A 472 10616 7062 8354 1535 847 -955 A O ATOM 3586 CB LYS A 472 49.658 101.777 243.452 1.00 69.61 A C ANISOU 3586 CB LYS A 472 11014 7207 8228 1296 711 -1221 A C ATOM 3587 CG LYS A 472 49.956 100.411 242.864 1.00 73.86 A C ANISOU 3587 CG LYS A 472 11644 7624 8796 1363 737 -1349 A C ATOM 3588 CD LYS A 472 49.628 99.312 243.874 1.00 71.44 A C ANISOU 3588 CD LYS A 472 11356 7136 8652 1334 678 -1333 A C ATOM 3589 CE LYS A 472 50.436 98.062 243.603 1.00 71.54 A C ANISOU 3589 CE LYS A 472 11415 7031 8737 1453 737 -1418 A C ATOM 3590 NZ LYS A 472 50.281 97.639 242.188 1.00 76.28 A N1+ ANISOU 3590 NZ LYS A 472 12120 7630 9231 1465 757 -1587 A N1+ TER END If you find results from this site helpful for your research, please cite one of our papers:
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