***  6et7_20240709  ***
Job options:
ID = 2407091543422795003
JOBID = 6et7_20240709
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:
HEADER 6et7_20240709
ATOM 1 N ILE A 24 16.264 51.492 480.418 1.00 64.81 A N
ANISOU 1 N ILE A 24 9688 5401 9534 1358 -1227 -839 A N
ATOM 2 CA ILE A 24 15.863 52.743 479.787 1.00 48.90 A C
ANISOU 2 CA ILE A 24 7559 3295 7725 1250 -1085 -899 A C
ATOM 3 C ILE A 24 17.105 53.542 479.408 1.00 60.92 A C
ANISOU 3 C ILE A 24 8850 4666 9632 1122 -1320 -1098 A C
ATOM 4 O ILE A 24 17.331 54.625 479.964 1.00 80.78 A O
ANISOU 4 O ILE A 24 11442 7064 12186 1148 -1479 -1321 A O
ATOM 5 CB ILE A 24 14.931 53.537 480.715 1.00 50.51 A C
ANISOU 5 CB ILE A 24 8058 3485 7649 1394 -1001 -986 A C
ATOM 6 CG1 ILE A 24 15.437 53.479 482.160 1.00 58.86 A C
ANISOU 6 CG1 ILE A 24 9433 4541 8392 1580 -1301 -1176 A C
ATOM 7 CG2 ILE A 24 13.530 52.995 480.642 1.00 49.14 A C
ANISOU 7 CG2 ILE A 24 7978 3417 7277 1451 -638 -761 A C
ATOM 8 CD1 ILE A 24 14.921 54.556 483.030 1.00 56.24 A C
ANISOU 8 CD1 ILE A 24 9379 4135 7854 1703 -1294 -1362 A C
ATOM 9 N PRO A 25 17.937 53.065 478.478 1.00 53.34 A N
ANISOU 9 N PRO A 25 7601 3679 8987 981 -1328 -1039 A N
ATOM 10 CA PRO A 25 19.104 53.846 478.068 1.00 52.73 A C
ANISOU 10 CA PRO A 25 7265 3425 9344 842 -1482 -1220 A C
ATOM 11 C PRO A 25 18.801 54.904 477.021 1.00 54.79 A C
ANISOU 11 C PRO A 25 7403 3557 9859 687 -1224 -1177 A C
ATOM 12 O PRO A 25 19.695 55.685 476.684 1.00 61.03 A O
ANISOU 12 O PRO A 25 7990 4181 11016 557 -1285 -1312 A O
ATOM 13 CB PRO A 25 20.025 52.774 477.484 1.00 49.71 A C
ANISOU 13 CB PRO A 25 6640 3066 9183 774 -1517 -1143 A C
ATOM 14 CG PRO A 25 19.085 51.820 476.856 1.00 46.83 A C
ANISOU 14 CG PRO A 25 6346 2847 8599 779 -1218 -869 A C
ATOM 15 CD PRO A 25 17.879 51.778 477.757 1.00 47.62 A C
ANISOU 15 CD PRO A 25 6770 3060 8265 939 -1172 -818 A C
ATOM 16 N ASN A 26 17.571 54.977 476.530 1.00 56.59 A N
ANISOU 16 N ASN A 26 7745 3856 9902 703 -940 -987 A N
ATOM 17 CA ASN A 26 17.202 55.907 475.460 1.00 72.41 A C
ANISOU 17 CA ASN A 26 9669 5756 12088 583 -699 -898 A C
ATOM 18 C ASN A 26 18.178 55.843 474.277 1.00 66.99 A C
ANISOU 18 C ASN A 26 8730 5068 11656 391 -578 -818 A C
ATOM 19 O ASN A 26 18.502 56.859 473.646 1.00 56.19 A O
ANISOU 19 O ASN A 26 7276 3622 10451 273 -461 -820 A O
ATOM 20 CB ASN A 26 17.060 57.328 476.011 1.00 70.43 A C
ANISOU 20 CB ASN A 26 9508 5384 11867 604 -754 -1069 A C
ATOM 21 CG ASN A 26 15.699 57.563 476.640 1.00 84.45 A C
ANISOU 21 CG ASN A 26 11534 7185 13367 776 -676 -1051 A C
ATOM 22 ND2 ASN A 26 15.261 58.819 476.678 1.00100.81 A N
ANISOU 22 ND2 ASN A 26 13671 9150 15482 783 -597 -1114 A N
ATOM 23 OD1 ASN A 26 15.039 56.616 477.071 1.00 88.07 A O
ANISOU 23 OD1 ASN A 26 12109 7826 13525 887 -633 -946 A O
ATOM 24 N ALA A 27 18.608 54.619 473.948 1.00 53.55 A N
ANISOU 24 N ALA A 27 6930 3444 9973 373 -575 -736 A N
ATOM 25 CA ALA A 27 19.521 54.361 472.842 1.00 45.26 A C
ANISOU 25 CA ALA A 27 5661 2395 9139 220 -424 -663 A C
ATOM 26 C ALA A 27 19.419 52.890 472.453 1.00 49.45 A C
ANISOU 26 C ALA A 27 6185 3041 9565 246 -359 -524 A C
ATOM 27 O ALA A 27 18.959 52.048 473.234 1.00 55.18 A O
ANISOU 27 O ALA A 27 7026 3817 10122 378 -493 -518 A O
ATOM 28 CB ALA A 27 20.965 54.732 473.209 1.00 47.90 A C
ANISOU 28 CB ALA A 27 5754 2611 9835 147 -603 -868 A C
ATOM 29 N ILE A 28 19.845 52.590 471.223 1.00 42.97 A N
ANISOU 29 N ILE A 28 5252 2246 8830 128 -135 -411 A N
ATOM 30 CA ILE A 28 19.812 51.231 470.705 1.00 41.59 A C
ANISOU 30 CA ILE A 28 5069 2165 8568 136 -45 -295 A C
ATOM 31 C ILE A 28 21.164 50.892 470.085 1.00 42.94 A C
ANISOU 31 C ILE A 28 5000 2280 9034 39 44 -335 A C
ATOM 32 O ILE A 28 21.931 51.772 469.697 1.00 44.68 A O
ANISOU 32 O ILE A 28 5076 2404 9496 -58 133 -397 A O
ATOM 33 CB ILE A 28 18.695 51.025 469.670 1.00 39.73 A C
ANISOU 33 CB ILE A 28 4998 2027 8070 118 168 -106 A C
ATOM 34 CG1 ILE A 28 18.936 51.932 468.462 1.00 40.48 A C
ANISOU 34 CG1 ILE A 28 5092 2067 8221 9 380 -49 A C
ATOM 35 CG2 ILE A 28 17.348 51.265 470.306 1.00 38.74 A C
ANISOU 35 CG2 ILE A 28 5048 1949 7722 224 95 -67 A C
ATOM 36 CD1 ILE A 28 18.390 51.372 467.130 1.00 39.47 A C
ANISOU 36 CD1 ILE A 28 5092 2006 7899 -20 573 111 A C
ATOM 37 N GLN A 29 21.448 49.586 469.999 1.00 42.40 A N
ANISOU 37 N GLN A 29 4881 2261 8969 72 44 -298 A N
ATOM 38 CA GLN A 29 22.569 49.117 469.205 1.00 43.58 A C
ANISOU 38 CA GLN A 29 4819 2364 9378 -7 207 -308 A C
ATOM 39 C GLN A 29 22.237 49.255 467.721 1.00 42.93 A C
ANISOU 39 C GLN A 29 4850 2313 9150 -97 551 -166 A C
ATOM 40 O GLN A 29 21.094 49.036 467.327 1.00 41.10 A O
ANISOU 40 O GLN A 29 4850 2174 8593 -70 602 -47 A O
ATOM 41 CB GLN A 29 22.879 47.663 469.526 1.00 43.33 A C
ANISOU 41 CB GLN A 29 4729 2362 9371 74 113 -303 A C
ATOM 42 CG GLN A 29 22.919 47.299 471.008 1.00 43.88 A C
ANISOU 42 CG GLN A 29 4809 2412 9450 222 -261 -399 A C
ATOM 43 CD GLN A 29 23.439 45.868 471.232 1.00 44.26 A C
ANISOU 43 CD GLN A 29 4779 2463 9576 314 -346 -382 A C
ATOM 44 NE2 GLN A 29 22.582 45.006 471.777 1.00 45.87 A N
ANISOU 44 NE2 GLN A 29 5203 2745 9481 435 -427 -282 A N
ATOM 45 OE1 GLN A 29 24.587 45.539 470.887 1.00 45.98 A O
ANISOU 45 OE1 GLN A 29 4734 2603 10135 279 -310 -449 A O
ATOM 46 N PRO A 30 23.221 49.585 466.864 1.00 49.54 A N
ANISOU 46 N PRO A 30 5532 3059 10234 -190 788 -182 A N
ATOM 47 CA PRO A 30 22.902 49.917 465.464 1.00 48.05 A C
ANISOU 47 CA PRO A 30 5521 2865 9872 -252 1107 -51 A C
ATOM 48 C PRO A 30 22.614 48.751 464.520 1.00 43.91 A C
ANISOU 48 C PRO A 30 5142 2403 9140 -239 1279 44 A C
ATOM 49 O PRO A 30 22.699 48.939 463.300 1.00 59.20 A O
ANISOU 49 O PRO A 30 7206 4291 10997 -286 1563 122 A O
ATOM 50 CB PRO A 30 24.163 50.658 464.999 1.00 47.80 A C
ANISOU 50 CB PRO A 30 5264 2683 10215 -342 1329 -113 A C
ATOM 51 CG PRO A 30 25.246 50.083 465.806 1.00 49.14 A C
ANISOU 51 CG PRO A 30 5093 2802 10774 -326 1178 -263 A C
ATOM 52 CD PRO A 30 24.634 49.875 467.176 1.00 54.34 A C
ANISOU 52 CD PRO A 30 5797 3535 11314 -235 768 -329 A C
ATOM 53 N PHE A 31 22.302 47.552 465.011 1.00 47.04 A N
ANISOU 53 N PHE A 31 5544 2883 9444 -173 1129 38 A N
ATOM 54 CA PHE A 31 21.945 46.506 464.057 1.00 42.93 A C
ANISOU 54 CA PHE A 31 5185 2405 8720 -169 1290 114 A C
ATOM 55 C PHE A 31 20.468 46.552 463.657 1.00 40.12 A C
ANISOU 55 C PHE A 31 5124 2133 7986 -147 1231 219 A C
ATOM 56 O PHE A 31 19.943 45.615 463.041 1.00 41.63 A O
ANISOU 56 O PHE A 31 5463 2361 7994 -137 1279 264 A O
ATOM 57 CB PHE A 31 22.386 45.121 464.567 1.00 41.64 A C
ANISOU 57 CB PHE A 31 4887 2263 8670 -115 1207 64 A C
ATOM 58 CG PHE A 31 21.705 44.633 465.821 1.00 40.08 A C
ANISOU 58 CG PHE A 31 4709 2147 8372 -27 901 61 A C
ATOM 59 CD1 PHE A 31 22.176 45.001 467.068 1.00 40.70 A C
ANISOU 59 CD1 PHE A 31 4627 2189 8649 26 663 -25 A C
ATOM 60 CD2 PHE A 31 20.663 43.706 465.744 1.00 43.85 A C
ANISOU 60 CD2 PHE A 31 5369 2713 8581 11 860 135 A C
ATOM 61 CE1 PHE A 31 21.584 44.506 468.219 1.00 39.77 A C
ANISOU 61 CE1 PHE A 31 4580 2121 8410 134 413 -17 A C
ATOM 62 CE2 PHE A 31 20.061 43.205 466.885 1.00 37.51 A C
ANISOU 62 CE2 PHE A 31 4593 1964 7696 98 642 150 A C
ATOM 63 CZ PHE A 31 20.522 43.602 468.129 1.00 38.17 A C
ANISOU 63 CZ PHE A 31 4564 2008 7929 170 431 85 A C
ATOM 64 N GLY A 32 19.820 47.670 463.941 1.00 43.78 A N
ANISOU 64 N GLY A 32 5663 2604 8369 -141 1133 249 A N
ATOM 65 CA GLY A 32 18.491 47.933 463.437 1.00 51.09 A C
ANISOU 65 CA GLY A 32 6832 3570 9011 -117 1090 350 A C
ATOM 66 C GLY A 32 18.115 49.365 463.732 1.00 49.73 A C
ANISOU 66 C GLY A 32 6693 3362 8842 -108 1026 368 A C
ATOM 67 O GLY A 32 18.942 50.160 464.185 1.00 57.14 A O
ANISOU 67 O GLY A 32 7485 4233 9994 -140 1045 298 A O
ATOM 68 N ALA A 33 16.842 49.683 463.502 1.00 49.53 A N
ANISOU 68 N ALA A 33 6843 3364 8612 -59 938 452 A N
ATOM 69 CA ALA A 33 16.292 50.996 463.838 1.00 49.83 A C
ANISOU 69 CA ALA A 33 6923 3364 8646 -25 862 474 A C
ATOM 70 C ALA A 33 15.070 50.790 464.712 1.00 37.24 A C
ANISOU 70 C ALA A 33 5328 1855 6966 64 669 476 A C
ATOM 71 O ALA A 33 14.490 49.707 464.741 1.00 47.06 A O
ANISOU 71 O ALA A 33 6580 3174 8127 88 616 497 A O
ATOM 72 CB ALA A 33 15.916 51.815 462.588 1.00 40.01 A C
ANISOU 72 CB ALA A 33 5901 2028 7274 -27 973 596 A C
ATOM 73 N MET A 34 14.675 51.820 465.430 1.00 37.44 A N
ANISOU 73 N MET A 34 5338 1854 7032 113 587 451 A N
ATOM 74 CA MET A 34 13.556 51.703 466.349 1.00 36.54 A C
ANISOU 74 CA MET A 34 5210 1805 6868 210 455 446 A C
ATOM 75 C MET A 34 12.615 52.891 466.198 1.00 58.59 A C
ANISOU 75 C MET A 34 8088 4544 9630 280 424 500 A C
ATOM 76 O MET A 34 13.059 54.036 466.047 1.00 49.63 A O
ANISOU 76 O MET A 34 6988 3312 8558 259 467 485 A O
ATOM 77 CB MET A 34 14.039 51.603 467.795 1.00 36.38 A C
ANISOU 77 CB MET A 34 5080 1796 6948 243 371 324 A C
ATOM 78 CG MET A 34 12.909 51.418 468.781 1.00 35.87 A C
ANISOU 78 CG MET A 34 5030 1779 6820 356 294 327 A C
ATOM 79 SD MET A 34 13.392 51.540 470.513 1.00 36.48 A S
ANISOU 79 SD MET A 34 5087 1810 6962 441 184 181 A S
ATOM 80 CE MET A 34 13.868 49.835 470.852 1.00 35.78 A C
ANISOU 80 CE MET A 34 4956 1786 6853 442 155 198 A C
ATOM 81 N LEU A 35 11.311 52.608 466.238 1.00 49.65 A N
ANISOU 81 N LEU A 35 6969 3460 8436 364 353 562 A N
ATOM 82 CA LEU A 35 10.275 53.626 466.344 1.00 44.62 A C
ANISOU 82 CA LEU A 35 6363 2778 7813 467 303 600 A C
ATOM 83 C LEU A 35 9.504 53.403 467.630 1.00 37.22 A C
ANISOU 83 C LEU A 35 5322 1897 6922 557 268 543 A C
ATOM 84 O LEU A 35 9.285 52.263 468.032 1.00 36.40 A O
ANISOU 84 O LEU A 35 5152 1871 6809 553 269 541 A O
ATOM 85 CB LEU A 35 9.285 53.601 465.170 1.00 38.30 A C
ANISOU 85 CB LEU A 35 5650 1947 6954 519 243 734 A C
ATOM 86 CG LEU A 35 9.684 53.867 463.720 1.00 39.39 A C
ANISOU 86 CG LEU A 35 5985 1988 6993 481 278 837 A C
ATOM 87 CD1 LEU A 35 8.461 53.688 462.849 1.00 40.35 A C
ANISOU 87 CD1 LEU A 35 6187 2072 7072 582 134 958 A C
ATOM 88 CD2 LEU A 35 10.243 55.269 463.561 1.00 40.71 A C
ANISOU 88 CD2 LEU A 35 6247 2041 7180 475 351 847 A C
ATOM 89 N ILE A 36 9.122 54.505 468.277 1.00 38.11 A N
ANISOU 89 N ILE A 36 5443 1951 7086 642 265 498 A N
ATOM 90 CA ILE A 36 8.213 54.509 469.416 1.00 38.39 A C
ANISOU 90 CA ILE A 36 5419 2007 7162 760 282 453 A C
ATOM 91 C ILE A 36 7.015 55.370 469.056 1.00 47.91 A C
ANISOU 91 C ILE A 36 6604 3168 8431 868 264 515 A C
ATOM 92 O ILE A 36 7.165 56.571 468.782 1.00 46.19 A O
ANISOU 92 O ILE A 36 6462 2856 8232 891 251 509 A O
ATOM 93 CB ILE A 36 8.876 55.013 470.706 1.00 45.50 A C
ANISOU 93 CB ILE A 36 6367 2850 8072 793 298 305 A C
ATOM 94 CG1 ILE A 36 10.056 54.111 471.084 1.00 38.09 A C
ANISOU 94 CG1 ILE A 36 5427 1939 7105 712 266 242 A C
ATOM 95 CG2 ILE A 36 7.834 55.092 471.832 1.00 39.70 A C
ANISOU 95 CG2 ILE A 36 5627 2109 7347 945 372 266 A C
ATOM 96 CD1 ILE A 36 10.777 54.540 472.321 1.00 39.03 A C
ANISOU 96 CD1 ILE A 36 5607 1973 7249 760 211 76 A C
ATOM 97 N VAL A 37 5.828 54.757 469.114 1.00 49.94 A N
ANISOU 97 N VAL A 37 6741 3477 8759 940 267 571 A N
ATOM 98 CA VAL A 37 4.566 55.330 468.666 1.00 52.87 A C
ANISOU 98 CA VAL A 37 7027 3812 9249 1054 213 637 A C
ATOM 99 C VAL A 37 3.628 55.426 469.857 1.00 54.94 A C
ANISOU 99 C VAL A 37 7168 4078 9628 1175 342 579 A C
ATOM 100 O VAL A 37 3.538 54.494 470.659 1.00 41.79 A O
ANISOU 100 O VAL A 37 5452 2482 7946 1160 456 548 A O
ATOM 101 CB VAL A 37 3.913 54.477 467.556 1.00 52.90 A C
ANISOU 101 CB VAL A 37 6944 3846 9308 1035 81 744 A C
ATOM 102 CG1 VAL A 37 2.651 55.166 467.012 1.00 43.42 A C
ANISOU 102 CG1 VAL A 37 5643 2593 8263 1174 -46 806 A C
ATOM 103 CG2 VAL A 37 4.902 54.198 466.452 1.00 49.22 A C
ANISOU 103 CG2 VAL A 37 6645 3368 8690 920 11 795 A C
ATOM 104 N GLU A 38 2.936 56.556 469.980 1.00 53.57 A N
ANISOU 104 N GLU A 38 6971 3835 9548 1298 350 564 A N
ATOM 105 CA GLU A 38 1.897 56.685 470.991 1.00 52.94 A C
ANISOU 105 CA GLU A 38 6762 3746 9605 1429 511 513 A C
ATOM 106 C GLU A 38 0.665 55.922 470.526 1.00 53.76 A C
ANISOU 106 C GLU A 38 6606 3893 9928 1463 481 595 A C
ATOM 107 O GLU A 38 0.175 56.149 469.418 1.00 54.02 A O
ANISOU 107 O GLU A 38 6559 3908 10057 1485 278 673 A O
ATOM 108 CB GLU A 38 1.577 58.158 471.251 1.00 47.21 A C
ANISOU 108 CB GLU A 38 6088 2921 8929 1551 533 457 A C
ATOM 109 CG GLU A 38 2.608 58.803 472.153 1.00 47.00 A C
ANISOU 109 CG GLU A 38 6277 2829 8751 1536 606 321 A C
ATOM 110 CD GLU A 38 2.135 60.057 472.854 1.00 69.28 A C
ANISOU 110 CD GLU A 38 9146 5543 11636 1676 699 221 A C
ATOM 111 OE1 GLU A 38 1.240 60.762 472.319 1.00 70.30 A O
ANISOU 111 OE1 GLU A 38 9172 5626 11914 1771 659 280 A O
ATOM 112 OE2 GLU A 38 2.680 60.333 473.952 1.00 73.05 A O1-
ANISOU 112 OE2 GLU A 38 9779 5968 12008 1703 796 71 A O1-
ATOM 113 N LYS A 39 0.178 55.004 471.369 1.00 46.55 A N
ANISOU 113 N LYS A 39 5572 3031 9085 1464 676 574 A N
ATOM 114 CA LYS A 39 -0.936 54.141 470.980 1.00 47.64 A C
ANISOU 114 CA LYS A 39 5424 3220 9458 1448 656 627 A C
ATOM 115 C LYS A 39 -2.183 54.950 470.620 1.00 58.38 A C
ANISOU 115 C LYS A 39 6546 4492 11145 1601 590 644 A C
ATOM 116 O LYS A 39 -2.831 54.681 469.601 1.00 51.19 A O
ANISOU 116 O LYS A 39 5445 3586 10421 1597 349 696 A O
ATOM 117 CB LYS A 39 -1.240 53.140 472.099 1.00 56.09 A C
ANISOU 117 CB LYS A 39 6430 4346 10536 1416 952 604 A C
ATOM 118 CG LYS A 39 -2.291 52.084 471.736 1.00 58.22 A C
ANISOU 118 CG LYS A 39 6380 4646 11095 1354 961 647 A C
ATOM 119 CD LYS A 39 -2.771 51.282 472.941 1.00 63.78 A C
ANISOU 119 CD LYS A 39 7016 5352 11866 1350 1344 645 A C
ATOM 120 CE LYS A 39 -3.705 50.132 472.500 1.00 88.33 A C
ANISOU 120 CE LYS A 39 9788 8463 15310 1246 1347 681 A C
ATOM 121 NZ LYS A 39 -2.990 48.874 472.001 1.00 89.56 A N1+
ANISOU 121 NZ LYS A 39 10032 8690 15306 1062 1215 710 A N1+
ATOM 122 N ASP A 40 -2.532 55.951 471.440 1.00 62.12 A N
ANISOU 122 N ASP A 40 7044 4918 11640 1725 770 580 A N
ATOM 123 CA ASP A 40 -3.790 56.680 471.242 1.00 63.31 A C
ANISOU 123 CA ASP A 40 6948 5023 12083 1858 737 580 A C
ATOM 124 C ASP A 40 -3.762 57.570 470.002 1.00 68.82 A C
ANISOU 124 C ASP A 40 7705 5682 12762 1906 390 639 A C
ATOM 125 O ASP A 40 -4.684 57.519 469.175 1.00 70.42 A O
ANISOU 125 O ASP A 40 7674 5878 13203 1960 169 687 A O
ATOM 126 CB ASP A 40 -4.138 57.515 472.481 1.00 66.20 A C
ANISOU 126 CB ASP A 40 7360 5334 12459 1982 1050 487 A C
ATOM 127 CG ASP A 40 -2.968 58.342 472.979 1.00 90.72 A C
ANISOU 127 CG ASP A 40 10835 8399 15235 1987 1078 414 A C
ATOM 128 OD1 ASP A 40 -1.829 58.078 472.533 1.00 99.05 A O
ANISOU 128 OD1 ASP A 40 12088 9482 16066 1869 920 437 A O
ATOM 129 OD2 ASP A 40 -3.191 59.265 473.798 1.00101.76 A O1-
ANISOU 129 OD2 ASP A 40 12314 9727 16623 2102 1253 321 A O1-
ATOM 130 N THR A 41 -2.731 58.413 469.865 1.00 68.91 A N
ANISOU 130 N THR A 41 8031 5651 12501 1894 338 636 A N
ATOM 131 CA THR A 41 -2.678 59.358 468.755 1.00 55.52 A C
ANISOU 131 CA THR A 41 6449 3886 10759 1956 77 713 A C
ATOM 132 C THR A 41 -2.082 58.740 467.501 1.00 57.69 A C
ANISOU 132 C THR A 41 6844 4191 10883 1854 -177 814 A C
ATOM 133 O THR A 41 -2.223 59.313 466.416 1.00 80.08 A O
ANISOU 133 O THR A 41 9774 6969 13682 1924 -413 907 A O
ATOM 134 CB THR A 41 -1.885 60.603 469.159 1.00 54.62 A C
ANISOU 134 CB THR A 41 6608 3677 10468 1983 172 662 A C
ATOM 135 CG2 THR A 41 -2.319 61.052 470.508 1.00 55.87 A C
ANISOU 135 CG2 THR A 41 6704 3803 10720 2071 440 536 A C
ATOM 136 OG1 THR A 41 -0.500 60.292 469.289 1.00 62.07 A O
ANISOU 136 OG1 THR A 41 7785 4640 11157 1828 214 635 A O
ATOM 137 N GLN A 42 -1.436 57.584 467.635 1.00 51.13 A N
ANISOU 137 N GLN A 42 6038 3437 9952 1705 -124 801 A N
ATOM 138 CA GLN A 42 -0.753 56.897 466.538 1.00 68.96 A C
ANISOU 138 CA GLN A 42 8439 5716 12044 1595 -318 878 A C
ATOM 139 C GLN A 42 0.325 57.764 465.899 1.00 49.26 A C
ANISOU 139 C GLN A 42 6279 3150 9290 1565 -353 932 A C
ATOM 140 O GLN A 42 0.571 57.703 464.690 1.00 66.38 A O
ANISOU 140 O GLN A 42 8606 5283 11332 1554 -542 1033 A O
ATOM 141 CB GLN A 42 -1.737 56.348 465.504 1.00 74.67 A C
ANISOU 141 CB GLN A 42 8985 6447 12940 1647 -620 940 A C
ATOM 142 CG GLN A 42 -2.679 55.315 466.108 1.00 72.62 A C
ANISOU 142 CG GLN A 42 8362 6244 12987 1628 -553 875 A C
ATOM 143 CD GLN A 42 -3.159 54.302 465.103 1.00 71.06 A C
ANISOU 143 CD GLN A 42 8048 6118 12835 1557 -847 877 A C
ATOM 144 NE2 GLN A 42 -3.602 53.156 465.598 1.00 90.24 A N
ANISOU 144 NE2 GLN A 42 10228 8623 15436 1448 -736 807 A N
ATOM 145 OE1 GLN A 42 -3.136 54.538 463.896 1.00 54.16 A O
ANISOU 145 OE1 GLN A 42 6062 3949 10569 1602 -1169 939 A O
ATOM 146 N GLN A 43 0.983 58.568 466.724 1.00 48.73 A N
ANISOU 146 N GLN A 43 6328 3041 9144 1552 -162 858 A N
ATOM 147 CA GLN A 43 2.090 59.399 466.287 1.00 48.43 A C
ANISOU 147 CA GLN A 43 6567 2913 8920 1496 -141 884 A C
ATOM 148 C GLN A 43 3.415 58.754 466.651 1.00 46.11 A C
ANISOU 148 C GLN A 43 6369 2670 8480 1316 -24 817 A C
ATOM 149 O GLN A 43 3.575 58.251 467.767 1.00 45.04 A O
ANISOU 149 O GLN A 43 6142 2602 8368 1280 96 708 A O
ATOM 150 CB GLN A 43 2.053 60.789 466.911 1.00 49.81 A C
ANISOU 150 CB GLN A 43 6803 2978 9146 1584 -47 821 A C
ATOM 151 CG GLN A 43 1.753 61.869 465.937 1.00 52.03 A C
ANISOU 151 CG GLN A 43 7223 3126 9420 1696 -163 938 A C
ATOM 152 CD GLN A 43 2.042 63.186 466.549 1.00 70.61 A C
ANISOU 152 CD GLN A 43 9675 5347 11806 1735 -50 862 A C
ATOM 153 NE2 GLN A 43 1.903 64.251 465.771 1.00 73.56 A N
ANISOU 153 NE2 GLN A 43 10209 5570 12170 1830 -120 965 A N
ATOM 154 OE1 GLN A 43 2.418 63.252 467.721 1.00 65.44 A O
ANISOU 154 OE1 GLN A 43 8978 4708 11178 1686 93 708 A O
ATOM 155 N ILE A 44 4.354 58.764 465.703 1.00 45.72 A N
ANISOU 155 N ILE A 44 6513 2575 8283 1219 -50 886 A N
ATOM 156 CA ILE A 44 5.738 58.461 466.040 1.00 48.72 A C
ANISOU 156 CA ILE A 44 6968 2975 8569 1056 69 808 A C
ATOM 157 C ILE A 44 6.248 59.545 466.973 1.00 46.30 A C
ANISOU 157 C ILE A 44 6690 2588 8313 1057 163 688 A C
ATOM 158 O ILE A 44 6.230 60.733 466.631 1.00 48.19 A O
ANISOU 158 O ILE A 44 7035 2696 8579 1105 161 721 A O
ATOM 159 CB ILE A 44 6.597 58.346 464.778 1.00 44.23 A C
ANISOU 159 CB ILE A 44 6591 2349 7867 959 68 907 A C
ATOM 160 CG1 ILE A 44 6.177 57.106 463.979 1.00 54.51 A C
ANISOU 160 CG1 ILE A 44 7882 3720 9108 952 -34 991 A C
ATOM 161 CG2 ILE A 44 8.066 58.316 465.148 1.00 43.30 A C
ANISOU 161 CG2 ILE A 44 6499 2225 7727 799 201 811 A C
ATOM 162 CD1 ILE A 44 6.555 57.129 462.530 1.00 44.86 A C
ANISOU 162 CD1 ILE A 44 6912 2400 7732 935 -65 1130 A C
ATOM 163 N VAL A 45 6.635 59.159 468.185 1.00 48.44 A N
ANISOU 163 N VAL A 45 6885 2916 8604 1022 228 548 A N
ATOM 164 CA VAL A 45 7.190 60.116 469.122 1.00 55.43 A C
ANISOU 164 CA VAL A 45 7818 3706 9537 1025 281 406 A C
ATOM 165 C VAL A 45 8.696 59.951 469.278 1.00 60.79 A C
ANISOU 165 C VAL A 45 8533 4363 10199 869 298 318 A C
ATOM 166 O VAL A 45 9.390 60.939 469.549 1.00 45.09 A O
ANISOU 166 O VAL A 45 6599 2248 8283 831 314 226 A O
ATOM 167 CB VAL A 45 6.491 60.058 470.494 1.00 54.72 A C
ANISOU 167 CB VAL A 45 7666 3641 9485 1145 332 286 A C
ATOM 168 CG1 VAL A 45 5.062 60.558 470.362 1.00 46.30 A C
ANISOU 168 CG1 VAL A 45 6527 2556 8509 1305 342 352 A C
ATOM 169 CG2 VAL A 45 6.578 58.665 471.103 1.00 43.38 A C
ANISOU 169 CG2 VAL A 45 6164 2331 7989 1117 359 260 A C
ATOM 170 N TYR A 46 9.230 58.745 469.087 1.00 61.31 A N
ANISOU 170 N TYR A 46 8552 4536 10207 778 291 337 A N
ATOM 171 CA TYR A 46 10.675 58.569 469.092 1.00 56.85 A C
ANISOU 171 CA TYR A 46 7980 3946 9673 636 305 263 A C
ATOM 172 C TYR A 46 11.105 57.751 467.887 1.00 41.25 A C
ANISOU 172 C TYR A 46 6010 2027 7636 536 340 383 A C
ATOM 173 O TYR A 46 10.352 56.927 467.374 1.00 40.40 A O
ANISOU 173 O TYR A 46 5902 2008 7441 572 318 485 A O
ATOM 174 CB TYR A 46 11.178 57.888 470.370 1.00 41.53 A C
ANISOU 174 CB TYR A 46 5986 2049 7744 640 257 110 A C
ATOM 175 CG TYR A 46 10.943 58.659 471.653 1.00 42.81 A C
ANISOU 175 CG TYR A 46 6201 2126 7941 745 223 -49 A C
ATOM 176 CD1 TYR A 46 11.753 59.729 472.011 1.00 44.45 A C
ANISOU 176 CD1 TYR A 46 6439 2190 8260 700 188 -191 A C
ATOM 177 CD2 TYR A 46 9.936 58.289 472.536 1.00 42.76 A C
ANISOU 177 CD2 TYR A 46 6220 2165 7864 891 246 -72 A C
ATOM 178 CE1 TYR A 46 11.534 60.434 473.206 1.00 45.98 A C
ANISOU 178 CE1 TYR A 46 6719 2289 8463 806 145 -369 A C
ATOM 179 CE2 TYR A 46 9.722 58.984 473.726 1.00 44.33 A C
ANISOU 179 CE2 TYR A 46 6515 2267 8063 1010 245 -237 A C
ATOM 180 CZ TYR A 46 10.526 60.050 474.050 1.00 45.91 A C
ANISOU 180 CZ TYR A 46 6774 2325 8343 969 176 -395 A C
ATOM 181 OH TYR A 46 10.314 60.711 475.226 1.00 47.75 A O
ANISOU 181 OH TYR A 46 7137 2453 8553 1093 162 -586 A O
ATOM 182 N ALA A 47 12.299 58.039 467.395 1.00 41.91 A N
ANISOU 182 N ALA A 47 6101 2039 7786 414 408 366 A N
ATOM 183 CA ALA A 47 12.929 57.219 466.377 1.00 41.46 A C
ANISOU 183 CA ALA A 47 6053 2019 7680 317 483 447 A C
ATOM 184 C ALA A 47 14.413 57.159 466.691 1.00 45.97 A C
ANISOU 184 C ALA A 47 6506 2550 8412 196 539 330 A C
ATOM 185 O ALA A 47 14.996 58.143 467.149 1.00 50.14 A O
ANISOU 185 O ALA A 47 6991 2965 9096 161 545 234 A O
ATOM 186 CB ALA A 47 12.694 57.748 464.952 1.00 42.68 A C
ANISOU 186 CB ALA A 47 6376 2088 7754 314 561 611 A C
ATOM 187 N SER A 48 15.014 55.998 466.475 1.00 47.81 A N
ANISOU 187 N SER A 48 6667 2863 8637 137 570 326 A N
ATOM 188 CA SER A 48 16.447 55.895 466.654 1.00 48.38 A C
ANISOU 188 CA SER A 48 6585 2885 8911 32 625 222 A C
ATOM 189 C SER A 48 17.160 56.713 465.585 1.00 43.94 A C
ANISOU 189 C SER A 48 6054 2194 8446 -60 823 286 A C
ATOM 190 O SER A 48 16.681 56.852 464.456 1.00 44.27 A O
ANISOU 190 O SER A 48 6274 2214 8335 -48 933 438 A O
ATOM 191 CB SER A 48 16.882 54.441 466.583 1.00 56.84 A C
ANISOU 191 CB SER A 48 7574 4058 9963 8 629 216 A C
ATOM 192 OG SER A 48 16.638 53.905 465.290 1.00 61.29 A O
ANISOU 192 OG SER A 48 8258 4651 10379 -14 765 353 A O
ATOM 193 N ALA A 49 18.332 57.240 465.955 1.00 45.65 A N
ANISOU 193 N ALA A 49 6098 2308 8938 -147 866 165 A N
ATOM 194 CA ALA A 49 19.025 58.228 465.129 1.00 54.21 A C
ANISOU 194 CA ALA A 49 7188 3236 10176 -234 1081 212 A C
ATOM 195 C ALA A 49 19.298 57.722 463.717 1.00 56.38 A C
ANISOU 195 C ALA A 49 7566 3505 10350 -273 1332 362 A C
ATOM 196 O ALA A 49 19.422 58.521 462.783 1.00 50.67 A O
ANISOU 196 O ALA A 49 6975 2657 9622 -303 1535 474 A O
ATOM 197 CB ALA A 49 20.329 58.638 465.805 1.00 52.52 A C
ANISOU 197 CB ALA A 49 6700 2917 10340 -329 1077 33 A C
ATOM 198 N ASN A 50 19.394 56.412 463.539 1.00 47.24 A N
ANISOU 198 N ASN A 50 6379 2465 9105 -266 1333 367 A N
ATOM 199 CA ASN A 50 19.638 55.820 462.237 1.00 58.82 A C
ANISOU 199 CA ASN A 50 7973 3922 10452 -291 1574 485 A C
ATOM 200 C ASN A 50 18.356 55.419 461.526 1.00 59.57 A C
ANISOU 200 C ASN A 50 8360 4087 10188 -203 1505 630 A C
ATOM 201 O ASN A 50 18.404 54.553 460.644 1.00 56.93 A O
ANISOU 201 O ASN A 50 8147 3777 9707 -204 1630 695 A O
ATOM 202 CB ASN A 50 20.507 54.574 462.382 1.00 58.49 A C
ANISOU 202 CB ASN A 50 7736 3944 10543 -327 1625 397 A C
ATOM 203 CG ASN A 50 19.835 53.509 463.232 1.00 58.18 A C
ANISOU 203 CG ASN A 50 7664 4063 10379 -258 1359 346 A C
ATOM 204 ND2 ASN A 50 20.091 52.252 462.912 1.00 68.38 A N
ANISOU 204 ND2 ASN A 50 8933 5419 11630 -258 1416 345 A N
ATOM 205 OD1 ASN A 50 19.041 53.814 464.119 1.00 60.45 A O
ANISOU 205 OD1 ASN A 50 7969 4401 10598 -197 1132 315 A O
ATOM 206 N SER A 51 17.206 55.977 461.920 1.00 45.79 A N
ANISOU 206 N SER A 51 6716 2362 8318 -118 1302 668 A N
ATOM 207 CA SER A 51 15.940 55.457 461.402 1.00 51.72 A C
ANISOU 207 CA SER A 51 7675 3181 8795 -23 1180 779 A C
ATOM 208 C SER A 51 15.803 55.678 459.905 1.00 56.37 A C
ANISOU 208 C SER A 51 8556 3671 9191 -7 1342 947 A C
ATOM 209 O SER A 51 15.112 54.903 459.224 1.00 55.55 A O
ANISOU 209 O SER A 51 8633 3607 8867 50 1285 1025 A O
ATOM 210 CB SER A 51 14.752 56.063 462.152 1.00 57.16 A C
ANISOU 210 CB SER A 51 8374 3894 9451 80 953 779 A C
ATOM 211 OG SER A 51 14.736 55.648 463.511 1.00 60.53 A O
ANISOU 211 OG SER A 51 8593 4421 9983 91 817 636 A O
ATOM 212 N ALA A 52 16.467 56.705 459.371 1.00 49.16 A N
ANISOU 212 N ALA A 52 7712 2614 8354 -50 1553 1003 A N
ATOM 213 CA ALA A 52 16.303 57.010 457.960 1.00 51.61 A C
ANISOU 213 CA ALA A 52 8356 2815 8436 -9 1724 1181 A C
ATOM 214 C ALA A 52 16.753 55.848 457.081 1.00 67.15 A C
ANISOU 214 C ALA A 52 10456 4811 10247 -35 1911 1198 A C
ATOM 215 O ALA A 52 16.032 55.446 456.158 1.00 68.81 A O
ANISOU 215 O ALA A 52 10982 5015 10146 50 1873 1311 A O
ATOM 216 CB ALA A 52 17.075 58.278 457.615 1.00 77.17 A C
ANISOU 216 CB ALA A 52 11623 5879 11816 -62 1974 1231 A C
ATOM 217 N GLU A 53 17.911 55.251 457.380 1.00 63.97 A N
ANISOU 217 N GLU A 53 9818 4431 10056 -136 2093 1073 A N
ATOM 218 CA GLU A 53 18.445 54.265 456.446 1.00 64.45 A C
ANISOU 218 CA GLU A 53 10024 4479 9984 -154 2342 1087 A C
ATOM 219 C GLU A 53 17.632 52.983 456.407 1.00 72.53 A C
ANISOU 219 C GLU A 53 11143 5619 10794 -102 2134 1067 A C
ATOM 220 O GLU A 53 17.699 52.265 455.407 1.00 85.49 A O
ANISOU 220 O GLU A 53 13053 7224 12207 -82 2299 1108 A O
ATOM 221 CB GLU A 53 19.901 53.933 456.769 1.00 61.72 A C
ANISOU 221 CB GLU A 53 9366 4110 9974 -258 2595 955 A C
ATOM 222 CG GLU A 53 20.100 53.204 458.070 1.00 75.17 A C
ANISOU 222 CG GLU A 53 10702 5947 11912 -288 2357 792 A C
ATOM 223 CD GLU A 53 21.568 53.033 458.423 1.00 78.48 A C
ANISOU 223 CD GLU A 53 10785 6316 12719 -371 2567 664 A C
ATOM 224 OE1 GLU A 53 22.134 51.939 458.166 1.00 70.93 A O
ANISOU 224 OE1 GLU A 53 9762 5379 11809 -381 2706 610 A O
ATOM 225 OE2 GLU A 53 22.153 54.011 458.947 1.00 83.15 A O1-
ANISOU 225 OE2 GLU A 53 11170 6828 13594 -420 2590 612 A O1-
ATOM 226 N TYR A 54 16.849 52.682 457.440 1.00 72.46 A N
ANISOU 226 N TYR A 54 10953 5732 10846 -73 1799 1002 A N
ATOM 227 CA TYR A 54 16.000 51.495 457.366 1.00 66.60 A C
ANISOU 227 CA TYR A 54 10301 5073 9930 -24 1614 989 A C
ATOM 228 C TYR A 54 14.635 51.820 456.762 1.00 72.89 A C
ANISOU 228 C TYR A 54 11405 5833 10455 94 1408 1120 A C
ATOM 229 O TYR A 54 14.142 51.069 455.914 1.00 68.18 A O
ANISOU 229 O TYR A 54 11097 5211 9597 143 1373 1159 A O
ATOM 230 CB TYR A 54 15.836 50.846 458.743 1.00 43.72 A C
ANISOU 230 CB TYR A 54 7069 2313 7229 -41 1395 859 A C
ATOM 231 CG TYR A 54 17.093 50.214 459.272 1.00 49.36 A C
ANISOU 231 CG TYR A 54 7517 3065 8171 -121 1533 733 A C
ATOM 232 CD1 TYR A 54 18.110 50.996 459.807 1.00 60.87 A C
ANISOU 232 CD1 TYR A 54 8758 4483 9886 -175 1636 673 A C
ATOM 233 CD2 TYR A 54 17.273 48.837 459.249 1.00 53.35 A C
ANISOU 233 CD2 TYR A 54 7980 3625 8665 -135 1546 668 A C
ATOM 234 CE1 TYR A 54 19.271 50.427 460.290 1.00 55.44 A C
ANISOU 234 CE1 TYR A 54 7808 3807 9451 -229 1731 558 A C
ATOM 235 CE2 TYR A 54 18.440 48.255 459.740 1.00 50.44 A C
ANISOU 235 CE2 TYR A 54 7357 3275 8533 -183 1654 561 A C
ATOM 236 CZ TYR A 54 19.428 49.061 460.261 1.00 52.49 A C
ANISOU 236 CZ TYR A 54 7393 3492 9057 -224 1735 509 A C
ATOM 237 OH TYR A 54 20.584 48.513 460.747 1.00 61.36 A O
ANISOU 237 OH TYR A 54 8243 4609 10461 -257 1813 402 A O
ATOM 238 N PHE A 55 13.987 52.905 457.215 1.00 70.03 A N
ANISOU 238 N PHE A 55 10994 5458 10155 154 1243 1174 A N
ATOM 239 CA PHE A 55 12.662 53.202 456.688 1.00 47.99 A C
ANISOU 239 CA PHE A 55 8456 2629 7148 296 1009 1297 A C
ATOM 240 C PHE A 55 12.696 53.859 455.325 1.00 62.95 A C
ANISOU 240 C PHE A 55 10766 4398 8753 364 1129 1456 A C
ATOM 241 O PHE A 55 11.641 53.973 454.693 1.00 69.35 A O
ANISOU 241 O PHE A 55 11855 5179 9317 507 894 1559 A O
ATOM 242 CB PHE A 55 11.872 54.039 457.674 1.00 46.94 A C
ANISOU 242 CB PHE A 55 8115 2520 7198 361 792 1293 A C
ATOM 243 CG PHE A 55 11.490 53.273 458.877 1.00 44.27 A C
ANISOU 243 CG PHE A 55 7476 2304 7039 345 646 1164 A C
ATOM 244 CD1 PHE A 55 10.406 52.412 458.839 1.00 48.41 A C
ANISOU 244 CD1 PHE A 55 8007 2898 7487 418 427 1159 A C
ATOM 245 CD2 PHE A 55 12.252 53.343 460.024 1.00 46.70 A C
ANISOU 245 CD2 PHE A 55 7495 2686 7563 256 713 1030 A C
ATOM 246 CE1 PHE A 55 10.059 51.665 459.943 1.00 41.60 A C
ANISOU 246 CE1 PHE A 55 6838 2186 6784 389 322 1040 A C
ATOM 247 CE2 PHE A 55 11.911 52.609 461.144 1.00 44.35 A C
ANISOU 247 CE2 PHE A 55 6964 2511 7377 257 595 924 A C
ATOM 248 CZ PHE A 55 10.811 51.767 461.105 1.00 47.32 A C
ANISOU 248 CZ PHE A 55 7339 2927 7714 324 440 950 A C
ATOM 249 N SER A 56 13.869 54.288 454.850 1.00 61.11 A N
ANISOU 249 N SER A 56 10591 4087 8539 281 1477 1476 A N
ATOM 250 CA SER A 56 13.970 54.689 453.453 1.00 56.65 A C
ANISOU 250 CA SER A 56 10487 3402 7637 351 1654 1626 A C
ATOM 251 C SER A 56 13.592 53.540 452.532 1.00 66.48 A C
ANISOU 251 C SER A 56 12100 4655 8506 415 1594 1632 A C
ATOM 252 O SER A 56 13.230 53.774 451.373 1.00 60.75 A O
ANISOU 252 O SER A 56 11851 3849 7382 534 1582 1758 A O
ATOM 253 CB SER A 56 15.382 55.183 453.140 1.00 58.58 A C
ANISOU 253 CB SER A 56 10700 3548 8011 241 2105 1625 A C
ATOM 254 OG SER A 56 16.301 54.115 453.051 1.00 58.14 A O
ANISOU 254 OG SER A 56 10560 3519 8011 146 2349 1509 A O
ATOM 255 N VAL A 57 13.687 52.306 453.036 1.00 63.77 A N
ANISOU 255 N VAL A 57 11566 4396 8266 344 1543 1488 A N
ATOM 256 CA VAL A 57 13.367 51.110 452.266 1.00 67.54 A C
ANISOU 256 CA VAL A 57 12381 4858 8423 384 1472 1453 A C
ATOM 257 C VAL A 57 11.855 50.936 452.109 1.00 74.09 A C
ANISOU 257 C VAL A 57 13332 5777 9040 521 953 1460 A C
ATOM 258 O VAL A 57 11.372 50.513 451.051 1.00 58.66 A O
ANISOU 258 O VAL A 57 11769 3835 6684 613 784 1463 A O
ATOM 259 CB VAL A 57 14.020 49.897 452.946 1.00 66.99 A C
ANISOU 259 CB VAL A 57 11992 4856 8606 252 1590 1277 A C
ATOM 260 CG1 VAL A 57 13.830 48.685 452.109 1.00 71.32 A C
ANISOU 260 CG1 VAL A 57 12813 5443 8841 270 1534 1187 A C
ATOM 261 CG2 VAL A 57 15.506 50.162 453.213 1.00 53.58 A C
ANISOU 261 CG2 VAL A 57 10017 3149 7193 129 2005 1227 A C
ATOM 262 N ALA A 58 11.089 51.224 453.168 1.00 78.78 A N
ANISOU 262 N ALA A 58 13533 6481 9918 536 668 1424 A N
ATOM 263 CA ALA A 58 9.629 51.218 453.075 1.00 67.21 A C
ANISOU 263 CA ALA A 58 12054 5128 8354 666 175 1415 A C
ATOM 264 C ALA A 58 9.113 52.425 452.314 1.00 70.11 A C
ANISOU 264 C ALA A 58 12779 5365 8493 840 51 1608 A C
ATOM 265 O ALA A 58 8.049 52.361 451.691 1.00 85.34 A O
ANISOU 265 O ALA A 58 14882 7342 10200 983 -357 1620 A O
ATOM 266 CB ALA A 58 8.999 51.198 454.467 1.00 51.40 A C
ANISOU 266 CB ALA A 58 9525 3256 6747 636 -11 1326 A C
ATOM 267 N ASP A 59 9.846 53.531 452.362 1.00 70.71 A N
ANISOU 267 N ASP A 59 12949 5269 8648 832 377 1754 A N
ATOM 268 CA ASP A 59 9.328 54.809 451.892 1.00 72.86 A C
ANISOU 268 CA ASP A 59 13390 5482 8811 978 262 1913 A C
ATOM 269 C ASP A 59 10.512 55.559 451.287 1.00 72.51 A C
ANISOU 269 C ASP A 59 13530 5334 8688 905 729 2005 A C
ATOM 270 O ASP A 59 11.272 56.200 452.020 1.00 76.48 A O
ANISOU 270 O ASP A 59 13712 5812 9534 780 989 1979 A O
ATOM 271 CB ASP A 59 8.708 55.569 453.056 1.00 71.77 A C
ANISOU 271 CB ASP A 59 12824 5378 9066 1004 98 1900 A C
ATOM 272 CG ASP A 59 7.750 56.638 452.604 1.00 80.51 A C
ANISOU 272 CG ASP A 59 14078 6436 10076 1202 -171 2043 A C
ATOM 273 OD1 ASP A 59 7.901 57.129 451.460 1.00 84.30 A O
ANISOU 273 OD1 ASP A 59 14973 6835 10221 1285 -111 2180 A O
ATOM 274 OD2 ASP A 59 6.851 56.991 453.401 1.00 86.88 A O1-
ANISOU 274 OD2 ASP A 59 14583 7280 11149 1282 -423 2016 A O1-
ATOM 275 N ASN A 60 10.658 55.501 449.957 1.00 66.62 A N
ANISOU 275 N ASN A 60 13309 4515 7488 990 815 2100 A N
ATOM 276 CA ASN A 60 11.899 56.106 449.442 1.00 81.78 A C
ANISOU 276 CA ASN A 60 15367 6320 9386 902 1337 2166 A C
ATOM 277 C ASN A 60 11.904 57.655 449.525 1.00 88.63 A C
ANISOU 277 C ASN A 60 16179 7087 10409 941 1413 2305 A C
ATOM 278 O ASN A 60 12.851 58.294 449.034 1.00 96.18 A O
ANISOU 278 O ASN A 60 17271 7917 11355 884 1830 2375 A O
ATOM 279 CB ASN A 60 12.217 55.625 448.009 1.00 72.73 A C
ANISOU 279 CB ASN A 60 14825 5102 7709 977 1518 2216 A C
ATOM 280 CG ASN A 60 11.010 55.668 447.063 1.00 90.71 A C
ANISOU 280 CG ASN A 60 17589 7385 9492 1214 1059 2308 A C
ATOM 281 ND2 ASN A 60 11.235 56.109 445.833 1.00 80.85 A N
ANISOU 281 ND2 ASN A 60 16880 6028 7810 1327 1232 2425 A N
ATOM 282 OD1 ASN A 60 9.898 55.298 447.435 1.00 97.58 A O
ANISOU 282 OD1 ASN A 60 18338 8352 10385 1302 543 2258 A O
ATOM 283 N THR A 61 10.909 58.273 450.165 1.00 87.01 A N
ANISOU 283 N THR A 61 15761 6914 10383 1031 1050 2337 A N
ATOM 284 CA THR A 61 10.943 59.707 450.405 1.00 70.79 A C
ANISOU 284 CA THR A 61 13608 4747 8542 1048 1127 2444 A C
ATOM 285 C THR A 61 11.650 60.052 451.709 1.00 67.63 A C
ANISOU 285 C THR A 61 12691 4350 8654 861 1300 2312 A C
ATOM 286 O THR A 61 12.062 61.203 451.893 1.00 74.46 A O
ANISOU 286 O THR A 61 13485 5089 9718 821 1468 2365 A O
ATOM 287 CB THR A 61 9.524 60.279 450.414 1.00 71.82 A C
ANISOU 287 CB THR A 61 13772 4889 8626 1258 663 2538 A C
ATOM 288 CG2 THR A 61 8.863 60.005 449.084 1.00 75.68 A C
ANISOU 288 CG2 THR A 61 14791 5377 8585 1458 430 2648 A C
ATOM 289 OG1 THR A 61 8.750 59.669 451.449 1.00 68.17 A O
ANISOU 289 OG1 THR A 61 12927 4562 8414 1263 343 2401 A O
ATOM 290 N ILE A 62 11.837 59.074 452.591 1.00 63.87 A N
ANISOU 290 N ILE A 62 11884 4005 8379 750 1254 2133 A N
ATOM 291 CA ILE A 62 12.615 59.260 453.813 1.00 76.08 A C
ANISOU 291 CA ILE A 62 12979 5573 10355 579 1390 1976 A C
ATOM 292 C ILE A 62 14.081 59.410 453.415 1.00 75.11 A C
ANISOU 292 C ILE A 62 12882 5360 10298 435 1846 1959 A C
ATOM 293 O ILE A 62 14.707 58.460 452.933 1.00 63.29 A O
ANISOU 293 O ILE A 62 11473 3898 8678 378 2046 1914 A O
ATOM 294 CB ILE A 62 12.424 58.087 454.787 1.00 71.11 A C
ANISOU 294 CB ILE A 62 12036 5110 9872 521 1217 1798 A C
ATOM 295 CG1 ILE A 62 10.946 57.916 455.179 1.00 73.39 A C
ANISOU 295 CG1 ILE A 62 12277 5472 10138 673 804 1811 A C
ATOM 296 CG2 ILE A 62 13.336 58.230 455.991 1.00 60.12 A C
ANISOU 296 CG2 ILE A 62 10237 3751 8855 363 1341 1625 A C
ATOM 297 CD1 ILE A 62 10.296 59.197 455.704 1.00 72.83 A C
ANISOU 297 CD1 ILE A 62 12095 5329 10249 762 656 1860 A C
ATOM 298 N HIS A 63 14.632 60.608 453.609 1.00 74.41 A N
ANISOU 298 N HIS A 63 12710 5136 10428 380 2023 1986 A N
ATOM 299 CA HIS A 63 16.036 60.881 453.335 1.00 66.54 A C
ANISOU 299 CA HIS A 63 11666 4027 9587 244 2467 1958 A C
ATOM 300 C HIS A 63 16.801 61.179 454.617 1.00 76.68 A C
ANISOU 300 C HIS A 63 12479 5324 11332 96 2489 1767 A C
ATOM 301 O HIS A 63 17.764 60.483 454.948 1.00 78.95 A O
ANISOU 301 O HIS A 63 12527 5664 11806 -21 2655 1626 A O
ATOM 302 CB HIS A 63 16.153 62.030 452.341 1.00 71.07 A C
ANISOU 302 CB HIS A 63 12585 4397 10023 307 2702 2154 A C
ATOM 303 CG HIS A 63 15.759 61.657 450.946 1.00 73.93 A C
ANISOU 303 CG HIS A 63 13471 4731 9887 448 2770 2322 A C
ATOM 304 CD2 HIS A 63 16.503 61.417 449.840 1.00 85.06 A C
ANISOU 304 CD2 HIS A 63 15209 6047 11063 448 3172 2390 A C
ATOM 305 ND1 HIS A 63 14.444 61.528 450.555 1.00 74.04 A N
ANISOU 305 ND1 HIS A 63 13756 4808 9569 632 2386 2430 A N
ATOM 306 CE1 HIS A 63 14.395 61.209 449.273 1.00 77.33 A C
ANISOU 306 CE1 HIS A 63 14669 5180 9533 740 2509 2550 A C
ATOM 307 NE2 HIS A 63 15.631 61.141 448.814 1.00 81.71 A N
ANISOU 307 NE2 HIS A 63 15287 5636 10124 632 3006 2529 A N
ATOM 308 N GLU A 64 16.405 62.202 455.353 1.00 82.94 A N
ANISOU 308 N GLU A 64 13143 6058 12312 111 2316 1750 A N
ATOM 309 CA GLU A 64 16.977 62.420 456.669 1.00 86.07 A C
ANISOU 309 CA GLU A 64 13136 6480 13086 -3 2259 1544 A C
ATOM 310 C GLU A 64 16.057 61.858 457.744 1.00 68.37 A C
ANISOU 310 C GLU A 64 10723 4414 10839 56 1870 1425 A C
ATOM 311 O GLU A 64 14.963 61.355 457.477 1.00 64.97 A O
ANISOU 311 O GLU A 64 10446 4072 10168 177 1650 1504 A O
ATOM 312 CB GLU A 64 17.236 63.910 456.905 1.00 82.60 A C
ANISOU 312 CB GLU A 64 12665 5844 12875 -33 2350 1561 A C
ATOM 313 CG GLU A 64 18.037 64.559 455.813 1.00 84.00 A C
ANISOU 313 CG GLU A 64 13036 5820 13059 -75 2761 1701 A C
ATOM 314 CD GLU A 64 17.156 65.246 454.781 1.00102.35 A C
ANISOU 314 CD GLU A 64 15787 8030 15072 76 2748 1950 A C
ATOM 315 OE1 GLU A 64 16.112 65.842 455.159 1.00101.12 A O
ANISOU 315 OE1 GLU A 64 15675 7864 14881 184 2443 1991 A O
ATOM 316 OE2 GLU A 64 17.515 65.173 453.583 1.00104.34 A O1-
ANISOU 316 OE2 GLU A 64 16340 8195 15109 101 3050 2102 A O1-
ATOM 317 N LEU A 65 16.516 61.969 458.987 1.00 68.74 A N
ANISOU 317 N LEU A 65 10453 4498 11166 -23 1794 1230 A N
ATOM 318 CA LEU A 65 15.671 61.642 460.122 1.00 64.60 A C
ANISOU 318 CA LEU A 65 9789 4112 10646 44 1476 1111 A C
ATOM 319 C LEU A 65 14.475 62.576 460.199 1.00 59.12 A C
ANISOU 319 C LEU A 65 9237 3348 9877 182 1292 1195 A C
ATOM 320 O LEU A 65 13.410 62.183 460.684 1.00 56.97 A O
ANISOU 320 O LEU A 65 8947 3185 9513 293 1052 1173 A O
ATOM 321 CB LEU A 65 16.489 61.703 461.409 1.00 68.58 A C
ANISOU 321 CB LEU A 65 9980 4639 11440 -53 1449 888 A C
ATOM 322 CG LEU A 65 15.820 61.224 462.687 1.00 51.00 A C
ANISOU 322 CG LEU A 65 7613 2559 9207 12 1178 745 A C
ATOM 323 CD1 LEU A 65 15.316 59.840 462.464 1.00 50.33 A C
ANISOU 323 CD1 LEU A 65 7555 2646 8922 57 1093 782 A C
ATOM 324 CD2 LEU A 65 16.821 61.235 463.810 1.00 50.93 A C
ANISOU 324 CD2 LEU A 65 7337 2548 9466 -82 1160 534 A C
ATOM 325 N SER A 66 14.637 63.823 459.761 1.00 58.02 A N
ANISOU 325 N SER A 66 9222 3016 9808 184 1415 1287 A N
ATOM 326 CA SER A 66 13.551 64.779 459.917 1.00 58.88 A C
ANISOU 326 CA SER A 66 9440 3038 9892 324 1238 1352 A C
ATOM 327 C SER A 66 12.318 64.371 459.123 1.00 58.83 A C
ANISOU 327 C SER A 66 9647 3086 9621 491 1052 1526 A C
ATOM 328 O SER A 66 11.196 64.657 459.548 1.00 72.15 A O
ANISOU 328 O SER A 66 11322 4785 11305 634 819 1525 A O
ATOM 329 CB SER A 66 14.010 66.171 459.492 1.00 68.62 A C
ANISOU 329 CB SER A 66 10786 4030 11255 293 1424 1437 A C
ATOM 330 OG SER A 66 14.765 66.105 458.298 1.00 73.15 A O
ANISOU 330 OG SER A 66 11528 4521 11744 228 1707 1585 A O
ATOM 331 N ASP A 67 12.492 63.654 458.010 1.00 59.50 A N
ANISOU 331 N ASP A 67 9914 3202 9490 487 1148 1659 A N
ATOM 332 CA ASP A 67 11.340 63.251 457.210 1.00 60.00 A C
ANISOU 332 CA ASP A 67 10190 3307 9299 655 942 1820 A C
ATOM 333 C ASP A 67 10.391 62.341 457.970 1.00 59.49 A C
ANISOU 333 C ASP A 67 9943 3413 9246 730 660 1717 A C
ATOM 334 O ASP A 67 9.218 62.239 457.600 1.00 71.20 A O
ANISOU 334 O ASP A 67 11515 4912 10625 899 420 1821 A O
ATOM 335 CB ASP A 67 11.786 62.555 455.933 1.00 67.32 A C
ANISOU 335 CB ASP A 67 11386 4245 9949 638 1116 1947 A C
ATOM 336 CG ASP A 67 12.616 63.440 455.065 1.00 72.45 A C
ANISOU 336 CG ASP A 67 12262 4712 10553 593 1435 2075 A C
ATOM 337 OD1 ASP A 67 12.335 64.649 455.035 1.00 71.39 A O
ANISOU 337 OD1 ASP A 67 12199 4427 10501 655 1416 2164 A O
ATOM 338 OD2 ASP A 67 13.540 62.930 454.406 1.00 86.32 A O1-
ANISOU 338 OD2 ASP A 67 14130 6463 12204 502 1726 2088 A O1-
ATOM 339 N ILE A 68 10.875 61.646 458.996 1.00 54.22 A N
ANISOU 339 N ILE A 68 9022 2872 8709 620 688 1520 A N
ATOM 340 CA ILE A 68 9.985 60.810 459.784 1.00 67.48 A C
ANISOU 340 CA ILE A 68 10535 4701 10404 693 471 1424 A C
ATOM 341 C ILE A 68 8.869 61.660 460.371 1.00 70.16 A C
ANISOU 341 C ILE A 68 10825 4995 10838 851 288 1417 A C
ATOM 342 O ILE A 68 7.729 61.201 460.520 1.00 73.91 A O
ANISOU 342 O ILE A 68 11250 5541 11292 990 88 1428 A O
ATOM 343 CB ILE A 68 10.784 60.080 460.876 1.00 55.73 A C
ANISOU 343 CB ILE A 68 8796 3342 9037 557 558 1220 A C
ATOM 344 CG1 ILE A 68 11.831 59.188 460.233 1.00 55.46 A C
ANISOU 344 CG1 ILE A 68 8797 3345 8931 425 735 1227 A C
ATOM 345 CG2 ILE A 68 9.866 59.182 461.684 1.00 47.04 A C
ANISOU 345 CG2 ILE A 68 7537 2394 7942 634 387 1138 A C
ATOM 346 CD1 ILE A 68 11.228 58.034 459.495 1.00 58.17 A C
ANISOU 346 CD1 ILE A 68 9261 3764 9078 480 642 1307 A C
ATOM 347 N LYS A 69 9.169 62.915 460.685 1.00 53.77 A N
ANISOU 347 N LYS A 69 8759 2786 8886 841 369 1394 A N
ATOM 348 CA LYS A 69 8.158 63.800 461.241 1.00 56.13 A C
ANISOU 348 CA LYS A 69 9026 3023 9278 1001 233 1375 A C
ATOM 349 C LYS A 69 6.984 63.981 460.278 1.00 56.71 A C
ANISOU 349 C LYS A 69 9258 3031 9257 1196 13 1567 A C
ATOM 350 O LYS A 69 5.829 64.043 460.710 1.00 80.16 A O
ANISOU 350 O LYS A 69 12151 6036 12270 1372 -153 1537 A O
ATOM 351 CB LYS A 69 8.819 65.121 461.619 1.00 56.29 A C
ANISOU 351 CB LYS A 69 9059 2878 9451 941 375 1322 A C
ATOM 352 CG LYS A 69 7.985 66.037 462.438 1.00 57.10 A C
ANISOU 352 CG LYS A 69 9103 2917 9676 1082 292 1247 A C
ATOM 353 CD LYS A 69 8.829 67.204 462.906 1.00 75.44 A C
ANISOU 353 CD LYS A 69 11424 5072 12167 986 445 1159 A C
ATOM 354 CE LYS A 69 8.027 68.202 463.721 1.00 78.25 A C
ANISOU 354 CE LYS A 69 11745 5338 12649 1131 385 1074 A C
ATOM 355 NZ LYS A 69 8.957 68.977 464.575 1.00 78.86 A N1+
ANISOU 355 NZ LYS A 69 11755 5303 12904 1007 516 902 A N1+
ATOM 356 N GLN A 70 7.246 64.018 458.972 1.00 58.70 A N
ANISOU 356 N GLN A 70 9722 3204 9376 1186 34 1768 A N
ATOM 357 CA GLN A 70 6.161 64.105 457.997 1.00 61.09 A C
ANISOU 357 CA GLN A 70 10144 3468 9598 1384 -188 1978 A C
ATOM 358 C GLN A 70 5.439 62.778 457.781 1.00 59.82 A C
ANISOU 358 C GLN A 70 9898 3478 9354 1462 -350 1993 A C
ATOM 359 O GLN A 70 4.414 62.753 457.097 1.00 61.91 A O
ANISOU 359 O GLN A 70 10234 3768 9520 1669 -537 2128 A O
ATOM 360 CB GLN A 70 6.685 64.591 456.646 1.00 64.24 A C
ANISOU 360 CB GLN A 70 10880 3753 9776 1383 -48 2192 A C
ATOM 361 CG GLN A 70 7.679 65.708 456.739 1.00 72.49 A C
ANISOU 361 CG GLN A 70 12004 4626 10911 1261 209 2185 A C
ATOM 362 CD GLN A 70 8.265 66.055 455.386 1.00 85.62 A C
ANISOU 362 CD GLN A 70 14028 6177 12328 1254 407 2394 A C
ATOM 363 NE2 GLN A 70 9.341 66.843 455.392 1.00 99.70 A N
ANISOU 363 NE2 GLN A 70 15862 7813 14207 1112 710 2384 A N
ATOM 364 OE1 GLN A 70 7.762 65.620 454.343 1.00 79.71 A O
ANISOU 364 OE1 GLN A 70 13530 5471 11285 1384 296 2551 A O
ATOM 365 N ALA A 71 5.958 61.677 458.312 1.00 69.98 A N
ANISOU 365 N ALA A 71 11075 4893 10621 1321 -277 1842 A N
ATOM 366 CA ALA A 71 5.432 60.369 457.966 1.00 65.24 A C
ANISOU 366 CA ALA A 71 10466 4434 9889 1377 -394 1850 A C
ATOM 367 C ALA A 71 4.192 60.004 458.779 1.00 71.06 A C
ANISOU 367 C ALA A 71 10949 5283 10768 1527 -571 1750 A C
ATOM 368 O ALA A 71 3.920 60.554 459.848 1.00 75.62 A O
ANISOU 368 O ALA A 71 11356 5869 11508 1560 -509 1628 A O
ATOM 369 CB ALA A 71 6.504 59.300 458.173 1.00 65.94 A C
ANISOU 369 CB ALA A 71 10547 4606 9900 1168 -219 1730 A C
ATOM 370 N ASN A 72 3.433 59.061 458.229 1.00 75.77 A N
ANISOU 370 N ASN A 72 11542 5986 11262 1581 -888 1741 A N
ATOM 371 CA ASN A 72 2.302 58.400 458.857 1.00 57.09 A C
ANISOU 371 CA ASN A 72 8824 3752 9117 1635 -1134 1621 A C
ATOM 372 C ASN A 72 2.695 56.939 459.059 1.00 52.76 A C
ANISOU 372 C ASN A 72 8171 3343 8531 1457 -1108 1501 A C
ATOM 373 O ASN A 72 3.369 56.358 458.210 1.00 62.02 A O
ANISOU 373 O ASN A 72 9606 4531 9427 1371 -1082 1528 A O
ATOM 374 CB ASN A 72 1.067 58.539 457.959 1.00 58.50 A C
ANISOU 374 CB ASN A 72 9029 3939 9259 1835 -1542 1693 A C
ATOM 375 CG ASN A 72 -0.184 57.971 458.573 1.00 77.86 A C
ANISOU 375 CG ASN A 72 11042 6502 12038 1893 -1777 1568 A C
ATOM 376 ND2 ASN A 72 -1.135 58.844 458.897 1.00 72.13 A N
ANISOU 376 ND2 ASN A 72 10113 5760 11532 2054 -1848 1573 A N
ATOM 377 OD1 ASN A 72 -0.316 56.758 458.730 1.00 82.93 A O
ANISOU 377 OD1 ASN A 72 11513 7256 12740 1782 -1854 1459 A O
ATOM 378 N ILE A 73 2.254 56.321 460.156 1.00 51.02 A N
ANISOU 378 N ILE A 73 7576 3253 8555 1400 -1067 1359 A N
ATOM 379 CA ILE A 73 2.774 54.988 460.475 1.00 55.92 A C
ANISOU 379 CA ILE A 73 8101 4022 9124 1214 -955 1244 A C
ATOM 380 C ILE A 73 2.328 53.954 459.446 1.00 74.81 A C
ANISOU 380 C ILE A 73 10561 6499 11366 1195 -1219 1224 A C
ATOM 381 O ILE A 73 2.974 52.908 459.282 1.00 48.61 A O
ANISOU 381 O ILE A 73 7301 3255 7914 1048 -1129 1159 A O
ATOM 382 CB ILE A 73 2.382 54.562 461.904 1.00 48.93 A C
ANISOU 382 CB ILE A 73 6850 3233 8508 1172 -825 1121 A C
ATOM 383 CG1 ILE A 73 0.878 54.377 462.017 1.00 62.79 A C
ANISOU 383 CG1 ILE A 73 8310 5034 10514 1284 -1045 1090 A C
ATOM 384 CG2 ILE A 73 2.856 55.563 462.916 1.00 46.24 A C
ANISOU 384 CG2 ILE A 73 6493 2805 8272 1199 -593 1108 A C
ATOM 385 CD1 ILE A 73 0.395 54.231 463.441 1.00 68.85 A C
ANISOU 385 CD1 ILE A 73 8759 5849 11553 1282 -847 1001 A C
ATOM 386 N ASN A 74 1.213 54.208 458.761 1.00 69.58 A N
ANISOU 386 N ASN A 74 9884 5815 10739 1351 -1568 1263 A N
ATOM 387 CA ASN A 74 0.763 53.319 457.697 1.00 62.53 A C
ANISOU 387 CA ASN A 74 9093 4980 9684 1350 -1888 1221 A C
ATOM 388 C ASN A 74 1.703 53.333 456.498 1.00 67.00 A C
ANISOU 388 C ASN A 74 10170 5482 9804 1333 -1858 1307 A C
ATOM 389 O ASN A 74 1.734 52.365 455.732 1.00 79.35 A O
ANISOU 389 O ASN A 74 11881 7104 11166 1275 -2008 1235 A O
ATOM 390 CB ASN A 74 -0.665 53.697 457.288 1.00 58.05 A C
ANISOU 390 CB ASN A 74 8368 4389 9299 1544 -2319 1231 A C
ATOM 391 CG ASN A 74 -1.640 53.595 458.453 1.00 61.75 A C
ANISOU 391 CG ASN A 74 8303 4906 10254 1555 -2292 1136 A C
ATOM 392 ND2 ASN A 74 -1.725 54.656 459.243 1.00 59.50 A N
ANISOU 392 ND2 ASN A 74 7911 4545 10153 1652 -2106 1198 A N
ATOM 393 OD1 ASN A 74 -2.284 52.570 458.656 1.00 57.93 A O
ANISOU 393 OD1 ASN A 74 7517 4509 9984 1473 -2402 1006 A O
ATOM 394 N SER A 75 2.469 54.405 456.317 1.00 68.50 A N
ANISOU 394 N SER A 75 10643 5534 9850 1381 -1643 1454 A N
ATOM 395 CA SER A 75 3.423 54.460 455.217 1.00 56.87 A C
ANISOU 395 CA SER A 75 9666 3970 7970 1361 -1517 1553 A C
ATOM 396 C SER A 75 4.649 53.603 455.476 1.00 58.01 A C
ANISOU 396 C SER A 75 9822 4164 8055 1145 -1158 1467 A C
ATOM 397 O SER A 75 5.329 53.208 454.528 1.00 74.84 A O
ANISOU 397 O SER A 75 12314 6256 9865 1106 -1062 1494 A O
ATOM 398 CB SER A 75 3.849 55.904 454.983 1.00 58.25 A C
ANISOU 398 CB SER A 75 10115 3944 8075 1469 -1351 1748 A C
ATOM 399 OG SER A 75 2.706 56.714 454.802 1.00 74.27 A O
ANISOU 399 OG SER A 75 12114 5913 10193 1691 -1690 1832 A O
ATOM 400 N LEU A 76 4.980 53.349 456.736 1.00 51.15 A N
ANISOU 400 N LEU A 76 8592 3363 7478 1023 -947 1370 A N
ATOM 401 CA LEU A 76 6.190 52.617 457.067 1.00 48.89 A C
ANISOU 401 CA LEU A 76 8290 3106 7180 842 -626 1295 A C
ATOM 402 C LEU A 76 5.933 51.206 457.558 1.00 54.15 A C
ANISOU 402 C LEU A 76 8691 3931 7953 735 -694 1136 A C
ATOM 403 O LEU A 76 6.761 50.324 457.326 1.00 68.89 A O
ANISOU 403 O LEU A 76 10643 5818 9715 618 -532 1076 A O
ATOM 404 CB LEU A 76 6.996 53.365 458.130 1.00 50.67 A C
ANISOU 404 CB LEU A 76 8358 3264 7631 782 -332 1300 A C
ATOM 405 CG LEU A 76 7.138 54.871 457.938 1.00 48.58 A C
ANISOU 405 CG LEU A 76 8268 2813 7378 879 -251 1441 A C
ATOM 406 CD1 LEU A 76 7.603 55.499 459.232 1.00 46.82 A C
ANISOU 406 CD1 LEU A 76 7795 2548 7446 827 -64 1379 A C
ATOM 407 CD2 LEU A 76 8.092 55.165 456.801 1.00 50.42 A C
ANISOU 407 CD2 LEU A 76 8909 2890 7357 853 -35 1563 A C
ATOM 408 N LEU A 77 4.847 50.983 458.217 1.00 46.97 A N
ANISOU 408 N LEU A 77 7469 3109 7270 773 -892 1074 A N
ATOM 409 CA LEU A 77 4.586 49.708 458.860 1.00 45.53 A C
ANISOU 409 CA LEU A 77 7010 3043 7246 665 -898 941 A C
ATOM 410 C LEU A 77 3.622 48.866 458.026 1.00 55.08 A C
ANISOU 410 C LEU A 77 8220 4298 8409 680 -1232 867 A C
ATOM 411 O LEU A 77 2.711 49.406 457.385 1.00 61.32 A O
ANISOU 411 O LEU A 77 9063 5061 9176 813 -1538 904 A O
ATOM 412 CB LEU A 77 3.999 49.944 460.256 1.00 44.60 A C
ANISOU 412 CB LEU A 77 6527 2971 7449 685 -836 913 A C
ATOM 413 CG LEU A 77 4.914 50.712 461.229 1.00 42.80 A C
ANISOU 413 CG LEU A 77 6286 2699 7278 670 -552 940 A C
ATOM 414 CD1 LEU A 77 4.612 50.374 462.669 1.00 41.05 A C
ANISOU 414 CD1 LEU A 77 5770 2546 7280 650 -437 871 A C
ATOM 415 CD2 LEU A 77 6.389 50.481 460.948 1.00 41.39 A C
ANISOU 415 CD2 LEU A 77 6307 2478 6940 562 -334 941 A C
ATOM 416 N PRO A 78 3.788 47.541 458.020 1.00 48.98 A N
ANISOU 416 N PRO A 78 7385 3581 7645 553 -1207 751 A N
ATOM 417 CA PRO A 78 2.842 46.682 457.293 1.00 49.80 A C
ANISOU 417 CA PRO A 78 7454 3710 7757 547 -1546 641 A C
ATOM 418 C PRO A 78 1.466 46.645 457.941 1.00 50.13 A C
ANISOU 418 C PRO A 78 7076 3786 8185 584 -1749 593 A C
ATOM 419 O PRO A 78 1.314 46.830 459.150 1.00 54.58 A O
ANISOU 419 O PRO A 78 7349 4373 9016 569 -1543 617 A O
ATOM 420 CB PRO A 78 3.507 45.302 457.340 1.00 48.00 A C
ANISOU 420 CB PRO A 78 7239 3503 7497 387 -1384 529 A C
ATOM 421 CG PRO A 78 4.945 45.584 457.652 1.00 45.77 A C
ANISOU 421 CG PRO A 78 7115 3193 7081 344 -1003 603 A C
ATOM 422 CD PRO A 78 4.952 46.787 458.514 1.00 44.61 A C
ANISOU 422 CD PRO A 78 6836 3041 7072 417 -889 711 A C
ATOM 423 N GLU A 79 0.455 46.373 457.117 1.00 53.21 A N
ANISOU 423 N GLU A 79 7438 4168 8614 636 -2158 512 A N
ATOM 424 CA GLU A 79 -0.900 46.266 457.643 1.00 54.74 A C
ANISOU 424 CA GLU A 79 7178 4371 9251 662 -2357 447 A C
ATOM 425 C GLU A 79 -0.963 45.223 458.747 1.00 62.89 A C
ANISOU 425 C GLU A 79 7868 5429 10599 498 -2084 372 A C
ATOM 426 O GLU A 79 -1.575 45.461 459.795 1.00 65.46 A O
ANISOU 426 O GLU A 79 7844 5757 11270 515 -1935 398 A O
ATOM 427 CB GLU A 79 -1.888 45.940 456.525 1.00 58.77 A C
ANISOU 427 CB GLU A 79 7693 4856 9780 720 -2886 330 A C
ATOM 428 CG GLU A 79 -3.339 45.874 456.975 1.00 77.28 A C
ANISOU 428 CG GLU A 79 9513 7185 12665 752 -3120 249 A C
ATOM 429 CD GLU A 79 -3.977 44.504 456.744 1.00 92.98 A C
ANISOU 429 CD GLU A 79 11258 9154 14916 601 -3332 41 A C
ATOM 430 OE1 GLU A 79 -3.237 43.507 456.568 1.00 85.86 A O
ANISOU 430 OE1 GLU A 79 10545 8256 13820 449 -3187 -33 A O
ATOM 431 OE2 GLU A 79 -5.226 44.430 456.738 1.00106.30 A O1-
ANISOU 431 OE2 GLU A 79 12544 10803 17044 635 -3641 -57 A O1-
ATOM 432 N HIS A 80 -0.305 44.073 458.540 1.00 52.04 A N
ANISOU 432 N HIS A 80 6620 4057 9096 351 -1982 289 A N
ATOM 433 CA HIS A 80 -0.354 42.987 459.518 1.00 50.78 A C
ANISOU 433 CA HIS A 80 6181 3894 9217 202 -1730 234 A C
ATOM 434 C HIS A 80 0.220 43.426 460.862 1.00 61.84 A C
ANISOU 434 C HIS A 80 7505 5326 10667 214 -1318 356 A C
ATOM 435 O HIS A 80 -0.314 43.066 461.921 1.00 47.73 A O
ANISOU 435 O HIS A 80 5415 3529 9190 174 -1131 360 A O
ATOM 436 CB HIS A 80 0.403 41.761 458.983 1.00 79.46 A C
ANISOU 436 CB HIS A 80 10025 7502 12664 67 -1687 135 A C
ATOM 437 CG HIS A 80 -0.079 41.289 457.642 1.00 96.32 A C
ANISOU 437 CG HIS A 80 12306 9599 14692 59 -2101 -16 A C
ATOM 438 CD2 HIS A 80 -0.871 40.243 457.295 1.00102.78 A C
ANISOU 438 CD2 HIS A 80 12943 10358 15750 -43 -2343 -194 A C
ATOM 439 ND1 HIS A 80 0.233 41.939 456.465 1.00104.40 A N
ANISOU 439 ND1 HIS A 80 13730 10625 15310 172 -2327 -1 A N
ATOM 440 CE1 HIS A 80 -0.342 41.311 455.452 1.00109.23 A C
ANISOU 440 CE1 HIS A 80 14432 11196 15872 155 -2716 -169 A C
ATOM 441 NE2 HIS A 80 -1.018 40.280 455.928 1.00105.90 A N
ANISOU 441 NE2 HIS A 80 13640 10735 15861 18 -2749 -303 A N
ATOM 442 N LEU A 81 1.300 44.221 460.841 1.00 53.14 A N
ANISOU 442 N LEU A 81 6684 4243 9263 271 -1169 450 A N
ATOM 443 CA LEU A 81 1.874 44.735 462.083 1.00 43.71 A C
ANISOU 443 CA LEU A 81 5441 3070 8097 295 -844 537 A C
ATOM 444 C LEU A 81 0.914 45.695 462.793 1.00 52.34 A C
ANISOU 444 C LEU A 81 6299 4160 9427 412 -844 583 A C
ATOM 445 O LEU A 81 0.761 45.636 464.020 1.00 43.79 A O
ANISOU 445 O LEU A 81 5044 3086 8510 412 -597 604 A O
ATOM 446 CB LEU A 81 3.199 45.438 461.791 1.00 42.17 A C
ANISOU 446 CB LEU A 81 5562 2867 7592 321 -726 601 A C
ATOM 447 CG LEU A 81 3.937 45.973 463.015 1.00 40.12 A C
ANISOU 447 CG LEU A 81 5278 2618 7350 342 -448 655 A C
ATOM 448 CD1 LEU A 81 4.167 44.829 463.984 1.00 49.59 A C
ANISOU 448 CD1 LEU A 81 6350 3841 8652 256 -260 623 A C
ATOM 449 CD2 LEU A 81 5.224 46.692 462.662 1.00 39.15 A C
ANISOU 449 CD2 LEU A 81 5414 2457 7006 350 -346 699 A C
ATOM 450 N ILE A 82 0.261 46.590 462.050 1.00 46.46 A N
ANISOU 450 N ILE A 82 5569 3392 8692 529 -1108 603 A N
ATOM 451 CA ILE A 82 -0.648 47.528 462.698 1.00 57.73 A C
ANISOU 451 CA ILE A 82 6761 4797 10377 658 -1097 641 A C
ATOM 452 C ILE A 82 -1.861 46.805 463.270 1.00 49.25 A C
ANISOU 452 C ILE A 82 5276 3714 9723 620 -1082 573 A C
ATOM 453 O ILE A 82 -2.201 46.986 464.441 1.00 49.02 A O
ANISOU 453 O ILE A 82 5051 3676 9899 649 -806 596 A O
ATOM 454 CB ILE A 82 -1.046 48.673 461.750 1.00 60.67 A C
ANISOU 454 CB ILE A 82 7252 5123 10675 817 -1397 694 A C
ATOM 455 CG1 ILE A 82 0.199 49.439 461.326 1.00 58.72 A C
ANISOU 455 CG1 ILE A 82 7408 4851 10053 842 -1307 783 A C
ATOM 456 CG2 ILE A 82 -2.007 49.621 462.437 1.00 50.90 A C
ANISOU 456 CG2 ILE A 82 5745 3845 9749 964 -1374 724 A C
ATOM 457 CD1 ILE A 82 -0.098 50.675 460.491 1.00 72.71 A C
ANISOU 457 CD1 ILE A 82 9356 6544 11726 1014 -1539 875 A C
ATOM 458 N SER A 83 -2.530 45.975 462.476 1.00 51.35 A N
ANISOU 458 N SER A 83 5411 3964 10134 554 -1360 479 A N
ATOM 459 CA SER A 83 -3.703 45.294 463.023 1.00 62.29 A C
ANISOU 459 CA SER A 83 6357 5308 12002 499 -1320 408 A C
ATOM 460 C SER A 83 -3.320 44.395 464.199 1.00 62.45 A C
ANISOU 460 C SER A 83 6315 5327 12087 373 -885 427 A C
ATOM 461 O SER A 83 -4.011 44.380 465.229 1.00 68.70 A O
ANISOU 461 O SER A 83 6828 6079 13196 387 -615 449 A O
ATOM 462 CB SER A 83 -4.439 44.515 461.930 1.00 56.37 A C
ANISOU 462 CB SER A 83 5472 4521 11424 433 -1737 272 A C
ATOM 463 OG SER A 83 -3.549 43.827 461.079 1.00 62.91 A O
ANISOU 463 OG SER A 83 6647 5372 11883 338 -1858 223 A O
ATOM 464 N GLY A 84 -2.193 43.683 464.088 1.00 53.55 A N
ANISOU 464 N GLY A 84 5469 4228 10649 268 -788 431 A N
ATOM 465 CA GLY A 84 -1.734 42.863 465.200 1.00 47.96 A C
ANISOU 465 CA GLY A 84 4757 3509 9956 180 -404 471 A C
ATOM 466 C GLY A 84 -1.474 43.654 466.474 1.00 63.59 A C
ANISOU 466 C GLY A 84 6778 5513 11872 286 -79 569 A C
ATOM 467 O GLY A 84 -1.717 43.157 467.579 1.00 47.02 A O
ANISOU 467 O GLY A 84 4572 3379 9915 263 241 608 A O
ATOM 468 N LEU A 85 -0.905 44.867 466.345 1.00 53.53 A N
ANISOU 468 N LEU A 85 5705 4281 10355 402 -142 608 A N
ATOM 469 CA LEU A 85 -0.695 45.712 467.526 1.00 52.14 A C
ANISOU 469 CA LEU A 85 5580 4112 10118 511 124 665 A C
ATOM 470 C LEU A 85 -2.009 46.244 468.081 1.00 53.85 A C
ANISOU 470 C LEU A 85 5498 4280 10682 610 224 665 A C
ATOM 471 O LEU A 85 -2.181 46.340 469.301 1.00 62.33 A O
ANISOU 471 O LEU A 85 6542 5334 11805 661 554 696 A O
ATOM 472 CB LEU A 85 0.263 46.861 467.211 1.00 43.14 A C
ANISOU 472 CB LEU A 85 4712 2994 8683 590 31 688 A C
ATOM 473 CG LEU A 85 1.765 46.520 467.167 1.00 40.78 A C
ANISOU 473 CG LEU A 85 4696 2726 8072 517 79 694 A C
ATOM 474 CD1 LEU A 85 2.561 47.645 466.611 1.00 39.99 A C
ANISOU 474 CD1 LEU A 85 4807 2611 7774 572 -24 711 A C
ATOM 475 CD2 LEU A 85 2.306 46.156 468.527 1.00 39.83 A C
ANISOU 475 CD2 LEU A 85 4636 2619 7880 520 353 709 A C
ATOM 476 N ALA A 86 -2.940 46.613 467.202 1.00 62.43 A N
ANISOU 476 N ALA A 86 6375 5338 12009 654 -58 629 A N
ATOM 477 CA ALA A 86 -4.231 47.128 467.657 1.00 65.73 A C
ANISOU 477 CA ALA A 86 6450 5693 12833 759 25 619 A C
ATOM 478 C ALA A 86 -5.004 46.079 468.440 1.00 62.37 A C
ANISOU 478 C ALA A 86 5730 5209 12758 666 322 605 A C
ATOM 479 O ALA A 86 -5.728 46.409 469.385 1.00 72.23 A O
ANISOU 479 O ALA A 86 6786 6400 14258 747 633 624 A O
ATOM 480 CB ALA A 86 -5.059 47.612 466.470 1.00 54.31 A C
ANISOU 480 CB ALA A 86 4818 4217 11600 832 -409 576 A C
ATOM 481 N SER A 87 -4.903 44.817 468.035 1.00 61.10 A N
ANISOU 481 N SER A 87 5533 5040 12644 497 254 570 A N
ATOM 482 CA SER A 87 -5.663 43.769 468.700 1.00 55.77 A C
ANISOU 482 CA SER A 87 4571 4272 12349 389 548 565 A C
ATOM 483 C SER A 87 -5.024 43.292 470.005 1.00 71.40 A C
ANISOU 483 C SER A 87 6776 6244 14108 371 1024 663 A C
ATOM 484 O SER A 87 -5.704 42.651 470.811 1.00 82.45 A O
ANISOU 484 O SER A 87 7980 7543 15805 324 1387 699 A O
ATOM 485 CB SER A 87 -5.856 42.594 467.745 1.00 56.76 A C
ANISOU 485 CB SER A 87 4564 4356 12645 212 277 473 A C
ATOM 486 OG SER A 87 -4.614 41.995 467.407 1.00 61.20 A O
ANISOU 486 OG SER A 87 5499 4978 12778 128 212 484 A O
ATOM 487 N ALA A 88 -3.736 43.553 470.222 1.00 71.56 A N
ANISOU 487 N ALA A 88 7204 6351 13633 409 1029 708 A N
ATOM 488 CA ALA A 88 -3.044 43.021 471.393 1.00 69.89 A C
ANISOU 488 CA ALA A 88 7244 6134 13177 408 1393 794 A C
ATOM 489 C ALA A 88 -3.454 43.769 472.657 1.00 77.93 A C
ANISOU 489 C ALA A 88 8290 7124 14196 559 1762 844 A C
ATOM 490 O ALA A 88 -3.326 44.994 472.734 1.00 91.50 A O
ANISOU 490 O ALA A 88 10094 8886 15785 694 1688 817 A O
ATOM 491 CB ALA A 88 -1.534 43.117 471.206 1.00 64.38 A C
ANISOU 491 CB ALA A 88 6930 5529 12005 412 1235 803 A C
ATOM 492 N ILE A 89 -3.917 43.028 473.662 1.00 70.87 A N
ANISOU 492 N ILE A 89 7360 6138 13430 540 2185 918 A N
ATOM 493 CA ILE A 89 -4.272 43.611 474.952 1.00 69.56 A C
ANISOU 493 CA ILE A 89 7294 5930 13206 693 2604 969 A C
ATOM 494 C ILE A 89 -3.181 43.349 475.981 1.00 68.93 A C
ANISOU 494 C ILE A 89 7689 5883 12619 758 2787 1046 A C
ATOM 495 O ILE A 89 -2.959 44.176 476.873 1.00 81.53 A O
ANISOU 495 O ILE A 89 9531 7497 13949 919 2949 1042 A O
ATOM 496 CB ILE A 89 -5.645 43.104 475.445 1.00 79.12 A C
ANISOU 496 CB ILE A 89 8154 6989 14920 660 3019 1009 A C
ATOM 497 CG1 ILE A 89 -5.781 41.589 475.252 1.00 72.55 A C
ANISOU 497 CG1 ILE A 89 7203 6062 14302 466 3108 1061 A C
ATOM 498 CG2 ILE A 89 -6.773 43.875 474.760 1.00 87.86 A C
ANISOU 498 CG2 ILE A 89 8803 8063 16516 694 2860 914 A C
ATOM 499 CD1 ILE A 89 -7.127 41.043 475.658 1.00 65.44 A C
ANISOU 499 CD1 ILE A 89 5907 4977 13980 400 3527 1094 A C
ATOM 500 N ARG A 90 -2.510 42.201 475.880 1.00 66.66 A N
ANISOU 500 N ARG A 90 7539 5589 12201 647 2747 1104 A N
ATOM 501 CA ARG A 90 -1.350 41.935 476.728 1.00 58.84 A C
ANISOU 501 CA ARG A 90 6996 4634 10728 724 2811 1169 A C
ATOM 502 C ARG A 90 -0.153 42.786 476.323 1.00 58.58 A C
ANISOU 502 C ARG A 90 7169 4729 10360 779 2422 1079 A C
ATOM 503 O ARG A 90 0.089 43.015 475.138 1.00 70.40 A O
ANISOU 503 O ARG A 90 8517 6281 11951 694 2079 1005 A O
ATOM 504 CB ARG A 90 -0.958 40.464 476.663 1.00 53.15 A C
ANISOU 504 CB ARG A 90 6340 3848 10005 602 2856 1258 A C
ATOM 505 CG ARG A 90 -1.340 39.698 477.895 1.00 67.46 A C
ANISOU 505 CG ARG A 90 8323 5530 11779 652 3345 1411 A C
ATOM 506 CD ARG A 90 -1.367 38.199 477.661 1.00 87.09 A C
ANISOU 506 CD ARG A 90 10744 7892 14453 497 3440 1503 A C
ATOM 507 NE ARG A 90 -2.411 37.782 476.726 1.00 98.88 A N
ANISOU 507 NE ARG A 90 11761 9301 16509 312 3414 1438 A N
ATOM 508 CZ ARG A 90 -2.346 36.678 475.986 1.00 97.92 A C
ANISOU 508 CZ ARG A 90 11500 9099 16605 137 3290 1425 A C
ATOM 509 NH1 ARG A 90 -1.283 35.883 476.071 1.00103.73 A N1+
ANISOU 509 NH1 ARG A 90 12530 9827 17054 132 3211 1489 A N1+
ATOM 510 NH2 ARG A 90 -3.340 36.364 475.163 1.00 85.47 A N
ANISOU 510 NH2 ARG A 90 9485 7438 15550 -25 3225 1334 A N
ATOM 511 N GLU A 91 0.592 43.272 477.312 1.00 48.85 A N
ANISOU 511 N GLU A 91 6292 3529 8741 925 2480 1080 A N
ATOM 512 CA GLU A 91 1.810 44.023 477.027 1.00 62.94 A C
ANISOU 512 CA GLU A 91 8256 5405 10254 963 2131 987 A C
ATOM 513 C GLU A 91 3.020 43.102 476.879 1.00 44.88 A C
ANISOU 513 C GLU A 91 6135 3141 7776 905 1951 1018 A C
ATOM 514 O GLU A 91 3.061 41.997 477.413 1.00 45.93 A O
ANISOU 514 O GLU A 91 6379 3219 7853 898 2126 1124 A O
ATOM 515 CB GLU A 91 2.078 45.055 478.119 1.00 47.46 A C
ANISOU 515 CB GLU A 91 6577 3453 8003 1146 2213 928 A C
ATOM 516 CG GLU A 91 1.076 46.176 478.098 1.00 60.22 A C
ANISOU 516 CG GLU A 91 8025 5042 9815 1216 2329 866 A C
ATOM 517 CD GLU A 91 1.362 47.225 479.127 1.00 67.85 A C
ANISOU 517 CD GLU A 91 9288 6000 10494 1395 2399 777 A C
ATOM 518 OE1 GLU A 91 2.545 47.594 479.293 1.00 64.37 A O
ANISOU 518 OE1 GLU A 91 9084 5601 9774 1427 2140 696 A O
ATOM 519 OE2 GLU A 91 0.391 47.668 479.776 1.00 85.45 A O1-
ANISOU 519 OE2 GLU A 91 11501 8164 12800 1504 2723 774 A O1-
ATOM 520 N ASN A 92 4.026 43.597 476.163 1.00 42.66 A N
ANISOU 520 N ASN A 92 5873 2923 7412 872 1622 929 A N
ATOM 521 CA ASN A 92 5.351 42.966 476.080 1.00 52.40 A C
ANISOU 521 CA ASN A 92 7258 4176 8476 848 1434 928 A C
ATOM 522 C ASN A 92 5.335 41.580 475.420 1.00 51.94 A C
ANISOU 522 C ASN A 92 7086 4077 8571 715 1448 1000 A C
ATOM 523 O ASN A 92 6.157 40.721 475.751 1.00 40.95 A O
ANISOU 523 O ASN A 92 5844 2660 7053 731 1422 1048 A O
ATOM 524 CB ASN A 92 6.006 42.893 477.468 1.00 42.71 A C
ANISOU 524 CB ASN A 92 6365 2940 6925 1007 1487 949 A C
ATOM 525 CG ASN A 92 6.234 44.283 478.084 1.00 48.79 A C
ANISOU 525 CG ASN A 92 7280 3737 7520 1135 1409 830 A C
ATOM 526 ND2 ASN A 92 7.265 44.969 477.606 1.00 51.22 A N
ANISOU 526 ND2 ASN A 92 7573 4075 7812 1110 1114 712 A N
ATOM 527 OD1 ASN A 92 5.495 44.730 478.973 1.00 48.41 A O
ANISOU 527 OD1 ASN A 92 7356 3664 7373 1251 1635 836 A O
ATOM 528 N GLU A 93 4.413 41.345 474.480 1.00 59.91 A N
ANISOU 528 N GLU A 93 7833 5067 9864 591 1465 996 A N
ATOM 529 CA GLU A 93 4.390 40.137 473.660 1.00 44.35 A C
ANISOU 529 CA GLU A 93 5743 3046 8062 448 1428 1017 A C
ATOM 530 C GLU A 93 4.755 40.525 472.231 1.00 46.32 A C
ANISOU 530 C GLU A 93 5885 3344 8369 357 1145 914 A C
ATOM 531 O GLU A 93 3.870 40.792 471.409 1.00 59.29 A O
ANISOU 531 O GLU A 93 7332 4987 10208 293 1069 871 A O
ATOM 532 CB GLU A 93 3.018 39.467 473.708 1.00 55.44 A C
ANISOU 532 CB GLU A 93 6936 4361 9766 372 1654 1070 A C
ATOM 533 CG GLU A 93 2.781 38.625 474.943 1.00 73.33 A C
ANISOU 533 CG GLU A 93 9343 6530 11990 425 1994 1207 A C
ATOM 534 CD GLU A 93 1.511 37.776 474.834 1.00 91.80 A C
ANISOU 534 CD GLU A 93 11427 8738 14716 303 2238 1256 A C
ATOM 535 OE1 GLU A 93 0.808 37.878 473.802 1.00 93.26 A O
ANISOU 535 OE1 GLU A 93 11309 8921 15204 186 2085 1160 A O
ATOM 536 OE2 GLU A 93 1.207 37.021 475.784 1.00 83.84 A O1-
ANISOU 536 OE2 GLU A 93 10525 7612 13717 329 2579 1390 A O1-
ATOM 537 N PRO A 94 6.034 40.545 471.870 1.00 38.61 A N
ANISOU 537 N PRO A 94 5037 2395 7236 356 985 874 A N
ATOM 538 CA PRO A 94 6.412 41.019 470.536 1.00 44.12 A C
ANISOU 538 CA PRO A 94 5688 3124 7952 285 777 792 A C
ATOM 539 C PRO A 94 5.809 40.196 469.412 1.00 42.74 A C
ANISOU 539 C PRO A 94 5388 2910 7941 157 713 761 A C
ATOM 540 O PRO A 94 5.473 39.025 469.568 1.00 59.85 A O
ANISOU 540 O PRO A 94 7506 5010 10225 94 813 789 A O
ATOM 541 CB PRO A 94 7.935 40.922 470.549 1.00 35.26 A C
ANISOU 541 CB PRO A 94 4709 2004 6685 305 703 765 A C
ATOM 542 CG PRO A 94 8.283 41.154 471.969 1.00 35.75 A C
ANISOU 542 CG PRO A 94 4894 2076 6616 432 774 802 A C
ATOM 543 CD PRO A 94 7.212 40.415 472.742 1.00 37.23 A C
ANISOU 543 CD PRO A 94 5065 2224 6856 450 981 895 A C
ATOM 544 N ILE A 95 5.616 40.870 468.288 1.00 36.62 A N
ANISOU 544 N ILE A 95 4579 2162 7173 127 538 700 A N
ATOM 545 CA ILE A 95 4.979 40.355 467.087 1.00 37.51 A C
ANISOU 545 CA ILE A 95 4608 2247 7399 28 394 638 A C
ATOM 546 C ILE A 95 5.976 40.513 465.948 1.00 40.84 A C
ANISOU 546 C ILE A 95 5201 2674 7641 1 267 583 A C
ATOM 547 O ILE A 95 6.613 41.563 465.817 1.00 35.89 A O
ANISOU 547 O ILE A 95 4679 2079 6880 61 241 595 A O
ATOM 548 CB ILE A 95 3.664 41.099 466.795 1.00 44.75 A C
ANISOU 548 CB ILE A 95 5351 3178 8475 56 283 623 A C
ATOM 549 CG1 ILE A 95 2.601 40.680 467.807 1.00 50.26 A C
ANISOU 549 CG1 ILE A 95 5840 3834 9421 57 471 666 A C
ATOM 550 CG2 ILE A 95 3.201 40.890 465.370 1.00 40.03 A C
ANISOU 550 CG2 ILE A 95 4730 2563 7916 -11 24 536 A C
ATOM 551 CD1 ILE A 95 1.633 41.820 468.152 1.00 71.21 A C
ANISOU 551 CD1 ILE A 95 8342 6510 12206 157 477 682 A C
ATOM 552 N TRP A 96 6.179 39.443 465.193 1.00 42.64 A N
ANISOU 552 N TRP A 96 5472 2850 7878 -90 230 523 A N
ATOM 553 CA TRP A 96 7.202 39.370 464.163 1.00 36.78 A C
ANISOU 553 CA TRP A 96 4920 2089 6964 -116 189 469 A C
ATOM 554 C TRP A 96 6.522 39.368 462.801 1.00 44.48 A C
ANISOU 554 C TRP A 96 5957 3051 7891 -158 -22 385 A C
ATOM 555 O TRP A 96 5.727 38.470 462.511 1.00 47.65 A O
ANISOU 555 O TRP A 96 6268 3408 8429 -232 -114 313 A O
ATOM 556 CB TRP A 96 8.044 38.115 464.379 1.00 36.50 A C
ANISOU 556 CB TRP A 96 4928 1987 6955 -162 321 450 A C
ATOM 557 CG TRP A 96 9.066 37.882 463.385 1.00 36.52 A C
ANISOU 557 CG TRP A 96 5101 1948 6828 -188 339 384 A C
ATOM 558 CD1 TRP A 96 9.573 38.783 462.494 1.00 43.39 A C
ANISOU 558 CD1 TRP A 96 6122 2834 7531 -164 309 368 A C
ATOM 559 CD2 TRP A 96 9.712 36.643 463.117 1.00 38.22 A C
ANISOU 559 CD2 TRP A 96 5373 2072 7076 -236 429 327 A C
ATOM 560 CE2 TRP A 96 10.607 36.862 462.055 1.00 37.23 A C
ANISOU 560 CE2 TRP A 96 5426 1918 6799 -238 468 266 A C
ATOM 561 CE3 TRP A 96 9.629 35.367 463.680 1.00 38.15 A C
ANISOU 561 CE3 TRP A 96 5292 1982 7220 -272 508 328 A C
ATOM 562 NE1 TRP A 96 10.494 38.178 461.686 1.00 43.39 A N
ANISOU 562 NE1 TRP A 96 6272 2763 7453 -197 403 302 A N
ATOM 563 CZ2 TRP A 96 11.417 35.860 461.548 1.00 37.89 A C
ANISOU 563 CZ2 TRP A 96 5603 1903 6888 -268 584 191 A C
ATOM 564 CZ3 TRP A 96 10.426 34.374 463.170 1.00 45.22 A C
ANISOU 564 CZ3 TRP A 96 6279 2806 8096 -298 584 255 A C
ATOM 565 CH2 TRP A 96 11.312 34.625 462.113 1.00 38.15 A C
ANISOU 565 CH2 TRP A 96 5549 1862 7085 -296 630 181 A C
ATOM 566 N VAL A 97 6.823 40.368 461.970 1.00 38.45 A N
ANISOU 566 N VAL A 97 5362 2310 6938 -108 -107 392 A N
ATOM 567 CA VAL A 97 6.188 40.516 460.662 1.00 45.48 A C
ANISOU 567 CA VAL A 97 6380 3187 7712 -108 -347 327 A C
ATOM 568 C VAL A 97 7.259 40.918 459.664 1.00 48.11 A C
ANISOU 568 C VAL A 97 7030 3489 7761 -86 -281 329 A C
ATOM 569 O VAL A 97 7.961 41.906 459.880 1.00 59.09 A O
ANISOU 569 O VAL A 97 8484 4884 9083 -33 -152 415 A O
ATOM 570 CB VAL A 97 5.045 41.565 460.677 1.00 50.31 A C
ANISOU 570 CB VAL A 97 6877 3841 8398 -25 -547 370 A C
ATOM 571 CG1 VAL A 97 4.633 41.940 459.264 1.00 43.58 A C
ANISOU 571 CG1 VAL A 97 6240 2971 7347 19 -827 326 A C
ATOM 572 CG2 VAL A 97 3.818 41.068 461.474 1.00 42.06 A C
ANISOU 572 CG2 VAL A 97 5497 2800 7683 -56 -596 347 A C
ATOM 573 N GLU A 98 7.361 40.192 458.554 1.00 53.91 A N
ANISOU 573 N GLU A 98 7973 4173 8338 -127 -355 228 A N
ATOM 574 CA GLU A 98 8.400 40.452 457.561 1.00 52.02 A C
ANISOU 574 CA GLU A 98 8068 3879 7817 -106 -221 228 A C
ATOM 575 C GLU A 98 7.821 40.954 456.240 1.00 45.47 A C
ANISOU 575 C GLU A 98 7541 3034 6701 -41 -461 207 A C
ATOM 576 O GLU A 98 6.716 40.586 455.840 1.00 60.92 A O
ANISOU 576 O GLU A 98 9468 5004 8674 -41 -779 118 A O
ATOM 577 CB GLU A 98 9.231 39.186 457.305 1.00 42.98 A C
ANISOU 577 CB GLU A 98 7007 2663 6662 -180 -41 125 A C
ATOM 578 CG GLU A 98 9.969 38.673 458.522 1.00 40.85 A C
ANISOU 578 CG GLU A 98 6495 2389 6638 -214 183 159 A C
ATOM 579 CD GLU A 98 10.710 37.372 458.268 1.00 55.41 A C
ANISOU 579 CD GLU A 98 8401 4140 8511 -269 340 58 A C
ATOM 580 OE1 GLU A 98 10.127 36.464 457.633 1.00 55.49 A O
ANISOU 580 OE1 GLU A 98 8496 4103 8485 -320 210 -66 A O
ATOM 581 OE2 GLU A 98 11.877 37.265 458.710 1.00 58.94 A O1-
ANISOU 581 OE2 GLU A 98 8801 4550 9045 -257 579 91 A O1-
ATOM 582 N THR A 99 8.597 41.773 455.549 1.00 46.15 A N
ANISOU 582 N THR A 99 7928 3073 6533 18 -309 287 A N
ATOM 583 CA THR A 99 8.357 42.159 454.170 1.00 50.68 A C
ANISOU 583 CA THR A 99 8919 3601 6737 98 -462 284 A C
ATOM 584 C THR A 99 9.463 41.549 453.318 1.00 54.50 A C
ANISOU 584 C THR A 99 9739 3991 6978 67 -179 222 A C
ATOM 585 O THR A 99 10.219 40.677 453.769 1.00 61.24 A O
ANISOU 585 O THR A 99 10450 4820 7999 -18 61 154 A O
ATOM 586 CB THR A 99 8.282 43.687 454.016 1.00 49.63 A C
ANISOU 586 CB THR A 99 8912 3453 6491 211 -475 457 A C
ATOM 587 CG2 THR A 99 7.430 44.304 455.100 1.00 48.02 A C
ANISOU 587 CG2 THR A 99 8323 3325 6596 238 -639 517 A C
ATOM 588 OG1 THR A 99 9.591 44.252 454.070 1.00 60.34 A O
ANISOU 588 OG1 THR A 99 10380 4731 7815 195 -64 557 A O
ATOM 589 N ASP A 100 9.554 41.989 452.066 1.00 54.42 A N
ANISOU 589 N ASP A 100 10199 3914 6563 153 -196 248 A N
ATOM 590 CA ASP A 100 10.589 41.432 451.201 1.00 71.70 A C
ANISOU 590 CA ASP A 100 12747 5996 8500 137 128 186 A C
ATOM 591 C ASP A 100 11.976 41.960 451.563 1.00 71.63 A C
ANISOU 591 C ASP A 100 12682 5909 8624 105 636 306 A C
ATOM 592 O ASP A 100 12.985 41.292 451.297 1.00 72.00 A O
ANISOU 592 O ASP A 100 12817 5871 8670 59 981 237 A O
ATOM 593 CB ASP A 100 10.265 41.716 449.730 1.00 79.39 A C
ANISOU 593 CB ASP A 100 14311 6906 8946 255 -22 179 A C
ATOM 594 CG ASP A 100 9.910 43.170 449.472 1.00 90.74 A C
ANISOU 594 CG ASP A 100 15926 8334 10215 380 -124 384 A C
ATOM 595 OD1 ASP A 100 9.283 43.812 450.351 1.00 92.67 A O
ANISOU 595 OD1 ASP A 100 15801 8657 10751 388 -317 467 A O
ATOM 596 OD2 ASP A 100 10.254 43.660 448.377 1.00 92.82 A O1-
ANISOU 596 OD2 ASP A 100 16728 8495 10046 480 8 465 A O1-
ATOM 597 N ARG A 101 12.060 43.158 452.136 1.00 63.44 A N
ANISOU 597 N ARG A 101 11494 4882 7730 132 691 469 A N
ATOM 598 CA ARG A 101 13.348 43.716 452.499 1.00 64.44 A C
ANISOU 598 CA ARG A 101 11525 4915 8044 89 1134 561 A C
ATOM 599 C ARG A 101 13.529 43.965 453.980 1.00 61.36 A C
ANISOU 599 C ARG A 101 10626 4592 8096 32 1129 582 A C
ATOM 600 O ARG A 101 14.678 44.047 454.426 1.00 65.15 A O
ANISOU 600 O ARG A 101 10939 5001 8815 -23 1448 591 A O
ATOM 601 CB ARG A 101 13.606 45.042 451.760 1.00 69.38 A C
ANISOU 601 CB ARG A 101 12496 5422 8442 166 1308 737 A C
ATOM 602 CG ARG A 101 13.705 44.942 450.229 1.00 76.38 A C
ANISOU 602 CG ARG A 101 13995 6201 8824 245 1426 751 A C
ATOM 603 CD ARG A 101 13.770 46.340 449.623 1.00 84.49 A C
ANISOU 603 CD ARG A 101 15367 7106 9631 338 1557 967 A C
ATOM 604 NE ARG A 101 13.425 46.425 448.207 1.00100.39 A N
ANISOU 604 NE ARG A 101 18033 9042 11067 470 1502 1015 A N
ATOM 605 CZ ARG A 101 12.185 46.557 447.743 1.00105.85 A C
ANISOU 605 CZ ARG A 101 18948 9810 11458 597 987 1016 A C
ATOM 606 NH1 ARG A 101 11.161 46.604 448.590 1.00106.48 A N1+
ANISOU 606 NH1 ARG A 101 18609 10040 11809 597 529 973 A N1+
ATOM 607 NH2 ARG A 101 11.967 46.643 446.434 1.00102.43 A N
ANISOU 607 NH2 ARG A 101 19165 9293 10460 736 930 1057 A N
ATOM 608 N LEU A 102 12.452 44.045 454.760 1.00 60.75 A N
ANISOU 608 N LEU A 102 10299 4638 8144 49 781 578 A N
ATOM 609 CA LEU A 102 12.548 44.423 456.164 1.00 58.80 A C
ANISOU 609 CA LEU A 102 9649 4449 8245 22 775 607 A C
ATOM 610 C LEU A 102 11.832 43.432 457.066 1.00 55.45 A C
ANISOU 610 C LEU A 102 8928 4139 8003 -11 561 515 A C
ATOM 611 O LEU A 102 10.836 42.816 456.682 1.00 50.19 A O
ANISOU 611 O LEU A 102 8309 3521 7239 -5 314 452 A O
ATOM 612 CB LEU A 102 11.990 45.823 456.407 1.00 43.84 A C
ANISOU 612 CB LEU A 102 7743 2556 6359 93 655 729 A C
ATOM 613 CG LEU A 102 12.806 46.929 455.771 1.00 45.45 A C
ANISOU 613 CG LEU A 102 8188 2610 6469 113 923 846 A C
ATOM 614 CD1 LEU A 102 11.996 48.207 455.749 1.00 47.07 A C
ANISOU 614 CD1 LEU A 102 8468 2799 6619 209 744 969 A C
ATOM 615 CD2 LEU A 102 14.078 47.102 456.577 1.00 44.20 A C
ANISOU 615 CD2 LEU A 102 7780 2386 6631 31 1218 826 A C
ATOM 616 N SER A 103 12.353 43.320 458.289 1.00 52.89 A N
ANISOU 616 N SER A 103 8303 3840 7953 -43 656 511 A N
ATOM 617 CA SER A 103 11.865 42.410 459.317 1.00 51.36 A C
ANISOU 617 CA SER A 103 7844 3726 7943 -67 538 457 A C
ATOM 618 C SER A 103 11.518 43.214 460.565 1.00 50.79 A C
ANISOU 618 C SER A 103 7546 3715 8035 -26 468 518 A C
ATOM 619 O SER A 103 12.388 43.887 461.137 1.00 39.54 A O
ANISOU 619 O SER A 103 6050 2258 6716 -17 596 544 A O
ATOM 620 CB SER A 103 12.919 41.343 459.627 1.00 42.87 A C
ANISOU 620 CB SER A 103 6685 2604 6998 -115 727 391 A C
ATOM 621 OG SER A 103 12.380 40.297 460.405 1.00 45.70 A O
ANISOU 621 OG SER A 103 6869 3009 7487 -134 625 353 A O
ATOM 622 N PHE A 104 10.250 43.142 460.974 1.00 49.34 A N
ANISOU 622 N PHE A 104 7247 3606 7893 -2 269 523 A N
ATOM 623 CA PHE A 104 9.675 43.937 462.054 1.00 45.78 A C
ANISOU 623 CA PHE A 104 6622 3207 7565 56 210 573 A C
ATOM 624 C PHE A 104 9.376 43.098 463.290 1.00 41.07 A C
ANISOU 624 C PHE A 104 5819 2659 7127 46 230 556 A C
ATOM 625 O PHE A 104 8.868 41.976 463.184 1.00 49.00 A O
ANISOU 625 O PHE A 104 6774 3667 8177 -3 191 517 A O
ATOM 626 CB PHE A 104 8.374 44.609 461.604 1.00 37.37 A C
ANISOU 626 CB PHE A 104 5568 2166 6463 115 5 606 A C
ATOM 627 CG PHE A 104 8.568 45.696 460.586 1.00 42.97 A C
ANISOU 627 CG PHE A 104 6511 2814 7000 166 -22 666 A C
ATOM 628 CD1 PHE A 104 8.883 46.989 460.979 1.00 43.47 A C
ANISOU 628 CD1 PHE A 104 6579 2834 7101 221 52 735 A C
ATOM 629 CD2 PHE A 104 8.415 45.435 459.234 1.00 43.50 A C
ANISOU 629 CD2 PHE A 104 6826 2848 6855 167 -120 653 A C
ATOM 630 CE1 PHE A 104 9.046 47.989 460.038 1.00 39.73 A C
ANISOU 630 CE1 PHE A 104 6344 2273 6479 271 56 814 A C
ATOM 631 CE2 PHE A 104 8.588 46.432 458.295 1.00 41.91 A C
ANISOU 631 CE2 PHE A 104 6899 2572 6454 232 -123 737 A C
ATOM 632 CZ PHE A 104 8.897 47.706 458.692 1.00 41.58 A C
ANISOU 632 CZ PHE A 104 6850 2475 6475 282 -22 829 A C
ATOM 633 N LEU A 105 9.658 43.681 464.459 1.00 34.42 A N
ANISOU 633 N LEU A 105 4884 1836 6360 98 290 583 A N
ATOM 634 CA LEU A 105 9.278 43.161 465.772 1.00 34.48 A C
ANISOU 634 CA LEU A 105 4756 1883 6462 127 325 595 A C
ATOM 635 C LEU A 105 8.625 44.292 466.574 1.00 35.80 A C
ANISOU 635 C LEU A 105 4865 2079 6658 214 306 624 A C
ATOM 636 O LEU A 105 9.281 45.279 466.904 1.00 39.35 A O
ANISOU 636 O LEU A 105 5360 2509 7083 258 322 615 A O
ATOM 637 CB LEU A 105 10.512 42.627 466.502 1.00 38.43 A C
ANISOU 637 CB LEU A 105 5262 2361 6980 133 417 578 A C
ATOM 638 CG LEU A 105 10.345 41.840 467.794 1.00 39.84 A C
ANISOU 638 CG LEU A 105 5385 2557 7196 178 465 608 A C
ATOM 639 CD1 LEU A 105 9.725 40.481 467.546 1.00 33.86 A C
ANISOU 639 CD1 LEU A 105 4592 1774 6500 115 501 622 A C
ATOM 640 CD2 LEU A 105 11.681 41.746 468.526 1.00 34.06 A C
ANISOU 640 CD2 LEU A 105 4677 1824 6440 225 470 581 A C
ATOM 641 N GLY A 106 7.350 44.166 466.900 1.00 34.76 A N
ANISOU 641 N GLY A 106 4620 1976 6612 239 287 646 A N
ATOM 642 CA GLY A 106 6.660 45.210 467.624 1.00 35.19 A C
ANISOU 642 CA GLY A 106 4616 2043 6712 334 302 665 A C
ATOM 643 C GLY A 106 5.875 44.686 468.807 1.00 35.81 A C
ANISOU 643 C GLY A 106 4589 2139 6880 373 435 690 A C
ATOM 644 O GLY A 106 5.305 43.605 468.774 1.00 36.40 A O
ANISOU 644 O GLY A 106 4570 2205 7055 314 478 705 A O
ATOM 645 N TRP A 107 5.799 45.510 469.843 1.00 38.97 A N
ANISOU 645 N TRP A 107 5017 2543 7249 476 519 690 A N
ATOM 646 CA TRP A 107 5.040 45.130 471.018 1.00 37.15 A C
ANISOU 646 CA TRP A 107 4736 2312 7066 535 704 724 A C
ATOM 647 C TRP A 107 4.431 46.369 471.651 1.00 38.09 A C
ANISOU 647 C TRP A 107 4845 2420 7206 656 769 705 A C
ATOM 648 O TRP A 107 4.849 47.492 471.393 1.00 43.66 A O
ANISOU 648 O TRP A 107 5615 3111 7861 698 665 662 A O
ATOM 649 CB TRP A 107 5.928 44.371 472.009 1.00 36.88 A C
ANISOU 649 CB TRP A 107 4856 2279 6877 556 798 741 A C
ATOM 650 CG TRP A 107 7.031 45.194 472.612 1.00 36.42 A C
ANISOU 650 CG TRP A 107 4964 2227 6647 635 727 682 A C
ATOM 651 CD1 TRP A 107 7.008 45.843 473.810 1.00 44.41 A C
ANISOU 651 CD1 TRP A 107 6102 3236 7537 760 798 652 A C
ATOM 652 CD2 TRP A 107 8.330 45.458 472.041 1.00 37.47 A C
ANISOU 652 CD2 TRP A 107 5148 2351 6739 589 570 624 A C
ATOM 653 CE2 TRP A 107 9.030 46.271 472.951 1.00 35.74 A C
ANISOU 653 CE2 TRP A 107 5047 2118 6413 680 521 551 A C
ATOM 654 CE3 TRP A 107 8.962 45.085 470.851 1.00 34.39 A C
ANISOU 654 CE3 TRP A 107 4718 1947 6403 482 486 617 A C
ATOM 655 NE1 TRP A 107 8.204 46.501 474.017 1.00 49.37 A N
ANISOU 655 NE1 TRP A 107 6843 3854 8063 790 647 563 A N
ATOM 656 CZ2 TRP A 107 10.327 46.707 472.715 1.00 35.80 A C
ANISOU 656 CZ2 TRP A 107 5081 2092 6431 652 384 470 A C
ATOM 657 CZ3 TRP A 107 10.252 45.534 470.616 1.00 33.94 A C
ANISOU 657 CZ3 TRP A 107 4706 1857 6334 463 403 555 A C
ATOM 658 CH2 TRP A 107 10.920 46.331 471.543 1.00 34.41 A C
ANISOU 658 CH2 TRP A 107 4830 1896 6349 540 348 482 A C
ATOM 659 N ARG A 108 3.444 46.144 472.497 1.00 39.64 A N
ANISOU 659 N ARG A 108 4964 2600 7496 714 975 738 A N
ATOM 660 CA ARG A 108 2.759 47.198 473.219 1.00 41.01 A C
ANISOU 660 CA ARG A 108 5127 2748 7708 845 1102 715 A C
ATOM 661 C ARG A 108 3.361 47.310 474.615 1.00 41.48 A C
ANISOU 661 C ARG A 108 5442 2806 7514 948 1254 694 A C
ATOM 662 O ARG A 108 3.452 46.317 475.346 1.00 52.71 A O
ANISOU 662 O ARG A 108 6961 4227 8838 949 1410 752 A O
ATOM 663 CB ARG A 108 1.262 46.890 473.292 1.00 43.29 A C
ANISOU 663 CB ARG A 108 5160 2999 8290 854 1278 755 A C
ATOM 664 CG ARG A 108 0.483 47.765 474.225 1.00 55.07 A C
ANISOU 664 CG ARG A 108 6636 4445 9843 1002 1507 736 A C
ATOM 665 CD ARG A 108 -0.943 47.279 474.322 1.00 66.74 A C
ANISOU 665 CD ARG A 108 7813 5866 11679 994 1726 779 A C
ATOM 666 NE ARG A 108 -1.738 48.108 475.221 1.00 69.08 A N
ANISOU 666 NE ARG A 108 8079 6102 12066 1149 2005 758 A N
ATOM 667 CZ ARG A 108 -3.067 48.090 475.253 1.00 88.66 A C
ANISOU 667 CZ ARG A 108 10235 8509 14942 1176 2198 771 A C
ATOM 668 NH1 ARG A 108 -3.735 47.292 474.429 1.00100.89 A N1+
ANISOU 668 NH1 ARG A 108 11458 10040 16835 1049 2093 793 A N1+
ATOM 669 NH2 ARG A 108 -3.735 48.867 476.098 1.00 92.56 A N
ANISOU 669 NH2 ARG A 108 10716 8935 15518 1331 2492 745 A N
ATOM 670 N HIS A 109 3.776 48.514 474.986 1.00 45.41 A N
ANISOU 670 N HIS A 109 6071 3285 7896 1042 1195 609 A N
ATOM 671 CA HIS A 109 4.272 48.779 476.332 1.00 50.19 A C
ANISOU 671 CA HIS A 109 6948 3881 8243 1164 1292 552 A C
ATOM 672 C HIS A 109 3.595 50.035 476.850 1.00 54.55 A C
ANISOU 672 C HIS A 109 7525 4375 8825 1297 1409 476 A C
ATOM 673 O HIS A 109 3.917 51.143 476.407 1.00 53.10 A O
ANISOU 673 O HIS A 109 7334 4153 8688 1307 1245 395 A O
ATOM 674 CB HIS A 109 5.795 48.946 476.373 1.00 49.81 A C
ANISOU 674 CB HIS A 109 7072 3845 8008 1141 1045 470 A C
ATOM 675 CG HIS A 109 6.324 49.175 477.758 1.00 56.82 A C
ANISOU 675 CG HIS A 109 8256 4719 8614 1279 1067 388 A C
ATOM 676 CD2 HIS A 109 6.621 50.318 478.425 1.00 52.29 A C
ANISOU 676 CD2 HIS A 109 7849 4099 7922 1384 1006 243 A C
ATOM 677 ND1 HIS A 109 6.557 48.143 478.644 1.00 43.97 A N
ANISOU 677 ND1 HIS A 109 6820 3114 6772 1336 1151 449 A N
ATOM 678 CE1 HIS A 109 6.991 48.638 479.790 1.00 49.36 A C
ANISOU 678 CE1 HIS A 109 7796 3776 7182 1482 1116 345 A C
ATOM 679 NE2 HIS A 109 7.039 49.955 479.684 1.00 56.06 A N
ANISOU 679 NE2 HIS A 109 8627 4583 8092 1507 1024 204 A N
ATOM 680 N GLU A 110 2.662 49.857 477.781 1.00 46.48 A N
ANISOU 680 N GLU A 110 6543 3325 7792 1401 1724 508 A N
ATOM 681 CA GLU A 110 1.949 50.957 478.432 1.00 51.63 A C
ANISOU 681 CA GLU A 110 7242 3907 8468 1553 1909 429 A C
ATOM 682 C GLU A 110 1.296 51.808 477.355 1.00 53.93 A C
ANISOU 682 C GLU A 110 7238 4159 9092 1531 1796 421 A C
ATOM 683 O GLU A 110 0.497 51.275 476.563 1.00 57.29 A O
ANISOU 683 O GLU A 110 7368 4596 9802 1455 1804 510 A O
ATOM 684 CB GLU A 110 2.932 51.706 479.324 1.00 52.87 A C
ANISOU 684 CB GLU A 110 7751 4042 8294 1656 1806 284 A C
ATOM 685 CG GLU A 110 3.458 50.918 480.489 1.00 65.59 A C
ANISOU 685 CG GLU A 110 9698 5682 9543 1727 1897 293 A C
ATOM 686 CD GLU A 110 4.306 51.778 481.394 1.00 81.99 A C
ANISOU 686 CD GLU A 110 12120 7723 11308 1851 1750 110 A C
ATOM 687 OE1 GLU A 110 4.323 53.017 481.169 1.00 81.26 A O
ANISOU 687 OE1 GLU A 110 11986 7566 11324 1877 1651 -23 A O
ATOM 688 OE2 GLU A 110 4.976 51.215 482.298 1.00 86.38 A O1-
ANISOU 688 OE2 GLU A 110 12993 8303 11524 1925 1704 95 A O1-
ATOM 689 N ASN A 111 1.622 53.096 477.263 1.00 67.03 A N
ANISOU 689 N ASN A 111 8974 5757 10738 1597 1663 314 A N
ATOM 690 CA ASN A 111 1.048 54.025 476.307 1.00 48.31 A C
ANISOU 690 CA ASN A 111 6383 3321 8650 1614 1548 318 A C
ATOM 691 C ASN A 111 1.559 53.814 474.890 1.00 50.09 A C
ANISOU 691 C ASN A 111 6490 3584 8957 1468 1240 387 A C
ATOM 692 O ASN A 111 1.008 54.417 473.970 1.00 46.40 A O
ANISOU 692 O ASN A 111 5855 3067 8707 1487 1120 425 A O
ATOM 693 CB ASN A 111 1.361 55.453 476.772 1.00 60.48 A C
ANISOU 693 CB ASN A 111 8105 4753 10124 1733 1529 180 A C
ATOM 694 CG ASN A 111 0.526 56.513 476.052 1.00 93.11 A C
ANISOU 694 CG ASN A 111 12035 8778 14563 1814 1491 194 A C
ATOM 695 ND2 ASN A 111 0.927 57.778 476.213 1.00 93.48 A N
ANISOU 695 ND2 ASN A 111 12231 8725 14564 1877 1417 82 A N
ATOM 696 OD1 ASN A 111 -0.471 56.209 475.376 1.00101.03 A O
ANISOU 696 OD1 ASN A 111 12751 9794 15841 1815 1500 294 A O
ATOM 697 N TYR A 112 2.613 53.023 474.686 1.00 47.50 A N
ANISOU 697 N TYR A 112 6269 3329 8451 1342 1110 403 A N
ATOM 698 CA TYR A 112 3.301 52.998 473.401 1.00 42.40 A C
ANISOU 698 CA TYR A 112 5584 2692 7832 1219 857 444 A C
ATOM 699 C TYR A 112 3.186 51.666 472.660 1.00 41.36 A C
ANISOU 699 C TYR A 112 5326 2646 7743 1093 802 536 A C
ATOM 700 O TYR A 112 2.836 50.629 473.219 1.00 47.94 A O
ANISOU 700 O TYR A 112 6119 3528 8567 1074 948 569 A O
ATOM 701 CB TYR A 112 4.777 53.360 473.581 1.00 41.35 A C
ANISOU 701 CB TYR A 112 5656 2534 7520 1170 736 360 A C
ATOM 702 CG TYR A 112 5.029 54.598 474.388 1.00 42.61 A C
ANISOU 702 CG TYR A 112 5963 2593 7633 1275 762 231 A C
ATOM 703 CD1 TYR A 112 4.947 55.853 473.807 1.00 56.75 A C
ANISOU 703 CD1 TYR A 112 7738 4260 9564 1307 694 212 A C
ATOM 704 CD2 TYR A 112 5.414 54.513 475.714 1.00 43.54 A C
ANISOU 704 CD2 TYR A 112 6272 2721 7552 1348 837 121 A C
ATOM 705 CE1 TYR A 112 5.194 57.010 474.542 1.00 44.55 A C
ANISOU 705 CE1 TYR A 112 6332 2593 8003 1397 717 72 A C
ATOM 706 CE2 TYR A 112 5.669 55.646 476.453 1.00 60.28 A C
ANISOU 706 CE2 TYR A 112 8551 4735 9617 1444 833 -33 A C
ATOM 707 CZ TYR A 112 5.568 56.904 475.864 1.00 56.00 A C
ANISOU 707 CZ TYR A 112 7961 4059 9256 1459 777 -67 A C
ATOM 708 OH TYR A 112 5.837 58.051 476.598 1.00 54.13 A O
ANISOU 708 OH TYR A 112 7886 3688 8992 1547 771 -241 A O
ATOM 709 N TYR A 113 3.509 51.742 471.368 1.00 40.41 A N
ANISOU 709 N TYR A 113 5174 2520 7660 1010 600 577 A N
ATOM 710 CA TYR A 113 3.907 50.626 470.523 1.00 39.21 A C
ANISOU 710 CA TYR A 113 4999 2428 7471 876 499 624 A C
ATOM 711 C TYR A 113 5.392 50.852 470.258 1.00 37.86 A C
ANISOU 711 C TYR A 113 5004 2236 7146 807 420 591 A C
ATOM 712 O TYR A 113 5.789 51.916 469.768 1.00 37.99 A O
ANISOU 712 O TYR A 113 5094 2173 7169 824 349 581 A O
ATOM 713 CB TYR A 113 3.186 50.612 469.172 1.00 39.77 A C
ANISOU 713 CB TYR A 113 4949 2490 7670 851 325 681 A C
ATOM 714 CG TYR A 113 1.692 50.492 469.162 1.00 44.40 A C
ANISOU 714 CG TYR A 113 5292 3075 8504 913 332 700 A C
ATOM 715 CD1 TYR A 113 1.005 49.827 470.166 1.00 43.68 A C
ANISOU 715 CD1 TYR A 113 5061 3002 8532 926 549 692 A C
ATOM 716 CD2 TYR A 113 0.958 51.057 468.124 1.00 42.92 A C
ANISOU 716 CD2 TYR A 113 5011 2847 8450 967 120 731 A C
ATOM 717 CE1 TYR A 113 -0.386 49.734 470.138 1.00 44.63 A C
ANISOU 717 CE1 TYR A 113 4900 3096 8963 973 582 701 A C
ATOM 718 CE2 TYR A 113 -0.421 50.974 468.084 1.00 45.07 A C
ANISOU 718 CE2 TYR A 113 5004 3103 9017 1031 86 732 A C
ATOM 719 CZ TYR A 113 -1.093 50.316 469.092 1.00 53.63 A C
ANISOU 719 CZ TYR A 113 5897 4201 10280 1025 331 710 A C
ATOM 720 OH TYR A 113 -2.472 50.229 469.039 1.00 49.36 A O
ANISOU 720 OH TYR A 113 5023 3621 10111 1079 323 702 A O
ATOM 721 N ILE A 114 6.220 49.877 470.579 1.00 44.04 A N
ANISOU 721 N ILE A 114 5841 3065 7826 735 445 576 A N
ATOM 722 CA ILE A 114 7.633 49.938 470.250 1.00 43.84 A C
ANISOU 722 CA ILE A 114 5920 3011 7728 662 376 539 A C
ATOM 723 C ILE A 114 7.861 48.975 469.102 1.00 39.97 A C
ANISOU 723 C ILE A 114 5405 2547 7236 551 329 591 A C
ATOM 724 O ILE A 114 7.374 47.841 469.145 1.00 38.41 A O
ANISOU 724 O ILE A 114 5141 2405 7049 520 358 621 A O
ATOM 725 CB ILE A 114 8.507 49.612 471.467 1.00 37.16 A C
ANISOU 725 CB ILE A 114 5156 2179 6783 688 403 465 A C
ATOM 726 CG1 ILE A 114 8.034 50.449 472.661 1.00 37.13 A C
ANISOU 726 CG1 ILE A 114 5220 2154 6734 819 463 401 A C
ATOM 727 CG2 ILE A 114 9.974 49.824 471.116 1.00 35.44 A C
ANISOU 727 CG2 ILE A 114 4978 1905 6581 616 317 405 A C
ATOM 728 CD1 ILE A 114 8.877 50.303 473.892 1.00 39.36 A C
ANISOU 728 CD1 ILE A 114 5644 2440 6872 877 433 309 A C
ATOM 729 N ILE A 115 8.532 49.452 468.054 1.00 35.11 A N
ANISOU 729 N ILE A 115 4859 1870 6610 496 279 601 A N
ATOM 730 CA ILE A 115 8.795 48.690 466.843 1.00 34.87 A C
ANISOU 730 CA ILE A 115 4866 1844 6538 406 251 638 A C
ATOM 731 C ILE A 115 10.286 48.703 466.561 1.00 34.51 A C
ANISOU 731 C ILE A 115 4892 1754 6466 332 309 599 A C
ATOM 732 O ILE A 115 10.887 49.774 466.417 1.00 45.44 A O
ANISOU 732 O ILE A 115 6327 3088 7851 328 329 577 A O
ATOM 733 CB ILE A 115 8.033 49.242 465.633 1.00 35.85 A C
ANISOU 733 CB ILE A 115 5049 1935 6638 427 156 702 A C
ATOM 734 CG1 ILE A 115 6.531 49.110 465.826 1.00 36.64 A C
ANISOU 734 CG1 ILE A 115 5011 2088 6823 494 69 720 A C
ATOM 735 CG2 ILE A 115 8.485 48.557 464.367 1.00 37.06 A C
ANISOU 735 CG2 ILE A 115 5322 2075 6684 346 138 720 A C
ATOM 736 CD1 ILE A 115 5.882 50.384 466.243 1.00 39.58 A C
ANISOU 736 CD1 ILE A 115 5346 2413 7279 611 55 736 A C
ATOM 737 N GLU A 116 10.877 47.522 466.457 1.00 34.00 A N
ANISOU 737 N GLU A 116 4812 1722 6386 269 344 579 A N
ATOM 738 CA GLU A 116 12.260 47.368 466.056 1.00 34.03 A C
ANISOU 738 CA GLU A 116 4839 1706 6386 198 412 533 A C
ATOM 739 C GLU A 116 12.267 46.803 464.643 1.00 49.72 A C
ANISOU 739 C GLU A 116 6934 3652 8305 137 464 573 A C
ATOM 740 O GLU A 116 11.478 45.907 464.333 1.00 46.77 A O
ANISOU 740 O GLU A 116 6572 3286 7914 132 420 598 A O
ATOM 741 CB GLU A 116 13.004 46.437 467.015 1.00 33.61 A C
ANISOU 741 CB GLU A 116 4697 1689 6382 202 411 476 A C
ATOM 742 CG GLU A 116 13.094 46.935 468.443 1.00 39.69 A C
ANISOU 742 CG GLU A 116 5429 2455 7198 284 344 429 A C
ATOM 743 CD GLU A 116 13.856 45.983 469.350 1.00 47.44 A C
ANISOU 743 CD GLU A 116 6370 3435 8222 319 306 392 A C
ATOM 744 OE1 GLU A 116 14.159 44.860 468.896 1.00 61.94 A O
ANISOU 744 OE1 GLU A 116 8186 5291 10059 276 348 412 A O
ATOM 745 OE2 GLU A 116 14.156 46.348 470.514 1.00 60.27 A O1-
ANISOU 745 OE2 GLU A 116 8004 5026 9871 404 218 336 A O1-
ATOM 746 N VAL A 117 13.125 47.339 463.770 1.00 35.25 A N
ANISOU 746 N VAL A 117 5195 1753 6446 91 568 576 A N
ATOM 747 CA VAL A 117 13.184 46.875 462.388 1.00 36.16 A C
ANISOU 747 CA VAL A 117 5487 1793 6457 51 653 616 A C
ATOM 748 C VAL A 117 14.626 46.562 462.022 1.00 36.75 A C
ANISOU 748 C VAL A 117 5544 1842 6576 -15 837 562 A C
ATOM 749 O VAL A 117 15.551 47.271 462.430 1.00 50.20 A O
ANISOU 749 O VAL A 117 7138 3535 8402 -35 905 526 A O
ATOM 750 CB VAL A 117 12.563 47.890 461.399 1.00 37.46 A C
ANISOU 750 CB VAL A 117 5868 1855 6508 93 641 717 A C
ATOM 751 CG1 VAL A 117 13.357 49.191 461.332 1.00 38.31 A C
ANISOU 751 CG1 VAL A 117 5996 1916 6645 79 750 733 A C
ATOM 752 CG2 VAL A 117 12.446 47.257 460.024 1.00 41.93 A C
ANISOU 752 CG2 VAL A 117 6678 2392 6860 76 672 739 A C
ATOM 753 N GLU A 118 14.811 45.481 461.270 1.00 37.18 A N
ANISOU 753 N GLU A 118 5691 1866 6569 -48 923 545 A N
ATOM 754 CA GLU A 118 16.116 45.016 460.816 1.00 53.30 A C
ANISOU 754 CA GLU A 118 7708 3868 8676 -97 1135 491 A C
ATOM 755 C GLU A 118 16.047 44.686 459.329 1.00 44.31 A C
ANISOU 755 C GLU A 118 6871 2617 7347 -114 1297 521 A C
ATOM 756 O GLU A 118 15.006 44.244 458.838 1.00 40.46 A O
ANISOU 756 O GLU A 118 6581 2094 6698 -93 1185 544 A O
ATOM 757 CB GLU A 118 16.575 43.756 461.604 1.00 51.59 A C
ANISOU 757 CB GLU A 118 7298 3716 8590 -96 1099 412 A C
ATOM 758 CG GLU A 118 16.697 43.963 463.104 1.00 46.89 A C
ANISOU 758 CG GLU A 118 6480 3201 8134 -56 943 384 A C
ATOM 759 CD GLU A 118 17.286 42.769 463.824 1.00 46.51 A C
ANISOU 759 CD GLU A 118 6285 3180 8205 -32 917 331 A C
ATOM 760 OE1 GLU A 118 18.244 42.176 463.289 1.00 62.86 A O
ANISOU 760 OE1 GLU A 118 8317 5197 10370 -55 1068 287 A O
ATOM 761 OE2 GLU A 118 16.800 42.422 464.926 1.00 45.51 A O1-
ANISOU 761 OE2 GLU A 118 6096 3113 8084 21 765 341 A O1-
ATOM 762 N ARG A 119 17.153 44.896 458.606 1.00 51.98 A N
ANISOU 762 N ARG A 119 7902 3510 8340 -147 1574 514 A N
ATOM 763 CA ARG A 119 17.215 44.382 457.239 1.00 56.23 A C
ANISOU 763 CA ARG A 119 8776 3929 8661 -151 1779 523 A C
ATOM 764 C ARG A 119 17.187 42.859 457.263 1.00 43.69 A C
ANISOU 764 C ARG A 119 7165 2349 7087 -162 1757 421 A C
ATOM 765 O ARG A 119 17.651 42.221 458.209 1.00 42.03 A O
ANISOU 765 O ARG A 119 6645 2222 7102 -169 1698 356 A O
ATOM 766 CB ARG A 119 18.456 44.877 456.497 1.00 45.75 A C
ANISOU 766 CB ARG A 119 7506 2500 7379 -180 2156 536 A C
ATOM 767 CG ARG A 119 18.457 46.369 456.246 1.00 52.12 A C
ANISOU 767 CG ARG A 119 8401 3260 8142 -174 2220 645 A C
ATOM 768 CD ARG A 119 19.494 46.769 455.202 1.00 58.01 A C
ANISOU 768 CD ARG A 119 9314 3864 8863 -196 2657 679 A C
ATOM 769 NE ARG A 119 19.773 48.194 455.255 1.00 70.02 A N
ANISOU 769 NE ARG A 119 10786 5342 10476 -207 2738 758 A N
ATOM 770 CZ ARG A 119 20.598 48.737 456.146 1.00 82.86 A C
ANISOU 770 CZ ARG A 119 12018 6990 12475 -259 2755 695 A C
ATOM 771 NH1 ARG A 119 21.210 47.962 457.044 1.00 78.58 A N1+
ANISOU 771 NH1 ARG A 119 11120 6520 12219 -285 2678 567 A N1+
ATOM 772 NH2 ARG A 119 20.815 50.048 456.146 1.00 83.85 A N
ANISOU 772 NH2 ARG A 119 12122 7048 12688 -276 2831 756 A N
ATOM 773 N TYR A 120 16.658 42.273 456.195 1.00 57.62 A N
ANISOU 773 N TYR A 120 9287 4025 8583 -153 1785 402 A N
ATOM 774 CA TYR A 120 16.283 40.868 456.253 1.00 66.51 A C
ANISOU 774 CA TYR A 120 10382 5200 9690 -164 1659 289 A C
ATOM 775 C TYR A 120 16.444 40.187 454.896 1.00 69.44 A C
ANISOU 775 C TYR A 120 11123 5480 9782 -160 1824 209 A C
ATOM 776 O TYR A 120 16.117 40.753 453.846 1.00 62.23 A O
ANISOU 776 O TYR A 120 10579 4532 8534 -124 1841 251 A O
ATOM 777 CB TYR A 120 14.847 40.726 456.756 1.00 58.31 A C
ANISOU 777 CB TYR A 120 9265 4301 8591 -152 1264 290 A C
ATOM 778 CG TYR A 120 14.168 39.472 456.280 1.00 66.58 A C
ANISOU 778 CG TYR A 120 10420 5360 9517 -173 1117 173 A C
ATOM 779 CD1 TYR A 120 14.544 38.232 456.787 1.00 68.57 A C
ANISOU 779 CD1 TYR A 120 10502 5582 9968 -207 1179 88 A C
ATOM 780 CD2 TYR A 120 13.126 39.520 455.350 1.00 66.64 A C
ANISOU 780 CD2 TYR A 120 10695 5392 9234 -152 884 140 A C
ATOM 781 CE1 TYR A 120 13.923 37.064 456.374 1.00 69.55 A C
ANISOU 781 CE1 TYR A 120 10716 5686 10024 -240 1052 -34 A C
ATOM 782 CE2 TYR A 120 12.495 38.357 454.929 1.00 75.35 A C
ANISOU 782 CE2 TYR A 120 11876 6486 10267 -185 715 -2 A C
ATOM 783 CZ TYR A 120 12.900 37.125 455.450 1.00 79.36 A C
ANISOU 783 CZ TYR A 120 12205 6950 10999 -239 818 -91 A C
ATOM 784 OH TYR A 120 12.288 35.947 455.054 1.00 84.95 A O
ANISOU 784 OH TYR A 120 12981 7617 11679 -286 665 -244 A O
ATOM 785 N HIS A 121 16.955 38.958 454.942 1.00 75.80 A N
ANISOU 785 N HIS A 121 11854 6235 10713 -181 1941 94 A N
ATOM 786 CA HIS A 121 17.252 38.173 453.753 1.00 84.07 A C
ANISOU 786 CA HIS A 121 13240 7173 11532 -173 2141 -17 A C
ATOM 787 C HIS A 121 16.565 36.815 453.850 1.00 76.22 A C
ANISOU 787 C HIS A 121 12222 6206 10532 -196 1912 -158 A C
ATOM 788 O HIS A 121 16.683 36.125 454.871 1.00 75.37 A O
ANISOU 788 O HIS A 121 11779 6118 10738 -218 1849 -177 A O
ATOM 789 CB HIS A 121 18.765 37.998 453.597 1.00 82.41 A C
ANISOU 789 CB HIS A 121 12958 6808 11544 -175 2611 -39 A C
ATOM 790 CG HIS A 121 19.168 37.407 452.285 1.00 89.51 A C
ANISOU 790 CG HIS A 121 14263 7570 12176 -151 2913 -141 A C
ATOM 791 CD2 HIS A 121 19.777 36.234 451.985 1.00 96.02 A C
ANISOU 791 CD2 HIS A 121 15113 8282 13087 -143 3135 -285 A C
ATOM 792 ND1 HIS A 121 18.939 38.041 451.080 1.00 88.60 A N
ANISOU 792 ND1 HIS A 121 14638 7406 11621 -113 3026 -101 A N
ATOM 793 CE1 HIS A 121 19.393 37.284 450.096 1.00 96.15 A C
ANISOU 793 CE1 HIS A 121 15925 8232 12377 -85 3315 -223 A C
ATOM 794 NE2 HIS A 121 19.907 36.183 450.618 1.00 97.44 A N
ANISOU 794 NE2 HIS A 121 15800 8352 12872 -106 3393 -344 A N
ATOM 795 N VAL A 122 15.855 36.429 452.788 1.00 62.70 A N
ANISOU 795 N VAL A 122 10884 4476 8464 -186 1778 -259 A N
ATOM 796 CA VAL A 122 15.152 35.151 452.797 1.00 74.93 A C
ANISOU 796 CA VAL A 122 12416 6020 10034 -226 1549 -418 A C
ATOM 797 C VAL A 122 16.157 34.005 452.743 1.00 73.03 A C
ANISOU 797 C VAL A 122 12144 5636 9968 -234 1862 -535 A C
ATOM 798 O VAL A 122 17.103 34.017 451.943 1.00 55.85 A O
ANISOU 798 O VAL A 122 10207 3342 7673 -196 2229 -572 A O
ATOM 799 CB VAL A 122 14.147 35.064 451.636 1.00 73.60 A C
ANISOU 799 CB VAL A 122 12661 5855 9449 -209 1272 -531 A C
ATOM 800 CG1 VAL A 122 13.086 36.142 451.754 1.00 53.83 A C
ANISOU 800 CG1 VAL A 122 10136 3483 6834 -182 920 -416 A C
ATOM 801 CG2 VAL A 122 14.852 35.141 450.290 1.00 72.74 A C
ANISOU 801 CG2 VAL A 122 13062 5624 8953 -147 1574 -591 A C
ATOM 802 N GLN A 123 15.966 33.015 453.616 1.00 79.98 A N
ANISOU 802 N GLN A 123 12729 6509 11151 -273 1747 -581 A N
ATOM 803 CA GLN A 123 16.685 31.746 453.542 1.00 92.43 A C
ANISOU 803 CA GLN A 123 14290 7931 12898 -271 1969 -711 A C
ATOM 804 C GLN A 123 15.700 30.683 453.073 1.00 82.00 A C
ANISOU 804 C GLN A 123 13136 6557 11465 -327 1720 -893 A C
ATOM 805 O GLN A 123 14.796 30.281 453.821 1.00 67.88 A O
ANISOU 805 O GLN A 123 11119 4816 9857 -386 1436 -882 A O
ATOM 806 CB GLN A 123 17.316 31.347 454.881 1.00100.70 A C
ANISOU 806 CB GLN A 123 14865 9035 14359 -252 2003 -609 A C
ATOM 807 CG GLN A 123 18.617 32.076 455.226 1.00 99.46 A C
ANISOU 807 CG GLN A 123 14490 8945 14357 -191 2252 -495 A C
ATOM 808 CD GLN A 123 18.360 33.339 456.021 1.00 90.31 A C
ANISOU 808 CD GLN A 123 13150 7921 13244 -193 2096 -337 A C
ATOM 809 NE2 GLN A 123 18.970 34.453 455.602 1.00 86.57 A N
ANISOU 809 NE2 GLN A 123 12746 7435 12711 -180 2298 -276 A N
ATOM 810 OE1 GLN A 123 17.604 33.316 456.996 1.00 83.55 A O
ANISOU 810 OE1 GLN A 123 12105 7167 12474 -207 1819 -271 A O
ATOM 811 N THR A 124 15.868 30.241 451.833 1.00 77.95 A N
ANISOU 811 N THR A 124 13028 5927 10660 -310 1840 -1070 A N
ATOM 812 CA THR A 124 15.161 29.066 451.346 1.00 71.40 A C
ANISOU 812 CA THR A 124 12363 4995 9771 -364 1643 -1295 A C
ATOM 813 C THR A 124 16.100 27.884 451.512 1.00 75.03 A C
ANISOU 813 C THR A 124 12732 5283 10495 -347 1953 -1387 A C
ATOM 814 O THR A 124 16.952 27.634 450.654 1.00 96.45 A O
ANISOU 814 O THR A 124 15686 7919 13041 -283 2262 -1478 A O
ATOM 815 CB THR A 124 14.773 29.241 449.885 1.00 77.59 A C
ANISOU 815 CB THR A 124 13690 5749 10041 -335 1549 -1460 A C
ATOM 816 CG2 THR A 124 14.108 27.988 449.354 1.00 86.74 A C
ANISOU 816 CG2 THR A 124 15025 6776 11155 -395 1327 -1739 A C
ATOM 817 OG1 THR A 124 13.891 30.356 449.753 1.00 88.21 A O
ANISOU 817 OG1 THR A 124 15097 7259 11159 -325 1222 -1354 A O
ATOM 818 N SER A 125 15.942 27.145 452.604 1.00 58.12 A N
ANISOU 818 N SER A 125 10170 3185 8728 -380 1829 -1317 A N
ATOM 819 CA SER A 125 16.689 25.903 452.753 1.00 74.72 A C
ANISOU 819 CA SER A 125 12124 5226 11041 -342 1997 -1368 A C
ATOM 820 C SER A 125 16.119 25.145 453.936 1.00 70.25 A C
ANISOU 820 C SER A 125 11201 4692 10799 -388 1772 -1280 A C
ATOM 821 O SER A 125 15.379 25.705 454.752 1.00 55.37 A O
ANISOU 821 O SER A 125 9129 2908 9000 -431 1562 -1145 A O
ATOM 822 CB SER A 125 18.196 26.150 452.929 1.00 67.76 A C
ANISOU 822 CB SER A 125 11081 4387 10277 -236 2365 -1251 A C
ATOM 823 OG SER A 125 18.507 26.494 454.260 1.00 67.90 A O
ANISOU 823 OG SER A 125 10678 4545 10575 -206 2297 -1035 A O
ATOM 824 N ASN A 126 16.486 23.871 454.030 1.00 59.10 A N
ANISOU 824 N ASN A 126 9714 3185 9554 -368 1846 -1344 A N
ATOM 825 CA ASN A 126 16.067 23.064 455.161 1.00 58.07 A C
ANISOU 825 CA ASN A 126 9294 3067 9702 -393 1696 -1233 A C
ATOM 826 C ASN A 126 17.122 23.016 456.258 1.00 56.49 A C
ANISOU 826 C ASN A 126 8795 2966 9704 -279 1838 -1022 A C
ATOM 827 O ASN A 126 16.965 22.257 457.222 1.00 60.55 A O
ANISOU 827 O ASN A 126 9122 3477 10410 -268 1764 -916 A O
ATOM 828 CB ASN A 126 15.679 21.657 454.698 1.00 60.91 A C
ANISOU 828 CB ASN A 126 9767 3240 10137 -448 1645 -1422 A C
ATOM 829 CG ASN A 126 16.779 20.971 453.940 1.00 63.42 A C
ANISOU 829 CG ASN A 126 10229 3445 10421 -362 1921 -1551 A C
ATOM 830 ND2 ASN A 126 16.429 19.926 453.220 1.00 66.43 A N
ANISOU 830 ND2 ASN A 126 10803 3651 10788 -409 1879 -1773 A N
ATOM 831 OD1 ASN A 126 17.933 21.381 453.992 1.00 67.12 A O
ANISOU 831 OD1 ASN A 126 10628 3976 10899 -256 2174 -1462 A O
ATOM 832 N TRP A 127 18.151 23.858 456.158 1.00 55.85 A N
ANISOU 832 N TRP A 127 8673 2963 9583 -196 2029 -960 A N
ATOM 833 CA TRP A 127 19.216 23.890 457.153 1.00 54.84 A C
ANISOU 833 CA TRP A 127 8254 2912 9670 -85 2121 -797 A C
ATOM 834 C TRP A 127 18.668 23.957 458.572 1.00 52.63 A C
ANISOU 834 C TRP A 127 7757 2743 9496 -80 1893 -610 A C
ATOM 835 O TRP A 127 19.150 23.253 459.460 1.00 52.84 A O
ANISOU 835 O TRP A 127 7619 2754 9704 0 1891 -515 A O
ATOM 836 CB TRP A 127 20.122 25.090 456.888 1.00 54.32 A C
ANISOU 836 CB TRP A 127 8150 2924 9566 -37 2300 -756 A C
ATOM 837 CG TRP A 127 21.346 25.130 457.739 1.00 54.09 A C
ANISOU 837 CG TRP A 127 7816 2936 9800 74 2390 -643 A C
ATOM 838 CD1 TRP A 127 22.531 24.530 457.489 1.00 56.28 A C
ANISOU 838 CD1 TRP A 127 7998 3113 10272 155 2628 -693 A C
ATOM 839 CD2 TRP A 127 21.485 25.780 459.006 1.00 61.16 A C
ANISOU 839 CD2 TRP A 127 8462 3966 10810 121 2215 -475 A C
ATOM 840 CE2 TRP A 127 22.796 25.538 459.452 1.00 53.11 A C
ANISOU 840 CE2 TRP A 127 7206 2909 10065 231 2327 -443 A C
ATOM 841 CE3 TRP A 127 20.629 26.551 459.804 1.00 49.50 A C
ANISOU 841 CE3 TRP A 127 6948 2625 9237 86 1974 -359 A C
ATOM 842 NE1 TRP A 127 23.413 24.777 458.501 1.00 55.73 A N
ANISOU 842 NE1 TRP A 127 7617 3099 10460 246 2589 -572 A N
ATOM 843 CZ2 TRP A 127 23.276 26.035 460.661 1.00 52.01 A C
ANISOU 843 CZ2 TRP A 127 6818 2854 10090 308 2168 -314 A C
ATOM 844 CZ3 TRP A 127 21.109 27.049 460.997 1.00 48.32 A C
ANISOU 844 CZ3 TRP A 127 6573 2567 9221 164 1856 -227 A C
ATOM 845 CH2 TRP A 127 22.420 26.789 461.416 1.00 49.62 A C
ANISOU 845 CH2 TRP A 127 6528 2682 9643 275 1935 -212 A C
ATOM 846 N PHE A 128 17.652 24.791 458.805 1.00 44.64 A N
ANISOU 846 N PHE A 128 7588 2811 6560 561 482 -752 A N
ATOM 847 CA PHE A 128 17.139 24.997 460.162 1.00 42.33 A C
ANISOU 847 CA PHE A 128 7035 2577 6474 451 304 -674 A C
ATOM 848 C PHE A 128 16.365 23.787 460.678 1.00 47.00 A C
ANISOU 848 C PHE A 128 7685 3075 7099 359 98 -743 A C
ATOM 849 O PHE A 128 16.512 23.392 461.843 1.00 41.32 A O
ANISOU 849 O PHE A 128 6799 2326 6573 331 49 -704 A O
ATOM 850 CB PHE A 128 16.252 26.236 460.186 1.00 41.11 A C
ANISOU 850 CB PHE A 128 6791 2562 6265 358 185 -583 A C
ATOM 851 CG PHE A 128 17.003 27.493 459.986 1.00 43.69 A C
ANISOU 851 CG PHE A 128 7008 2968 6624 425 369 -487 A C
ATOM 852 CD1 PHE A 128 17.313 27.932 458.712 1.00 48.39 A C
ANISOU 852 CD1 PHE A 128 7797 3568 7020 497 523 -486 A C
ATOM 853 CD2 PHE A 128 17.410 28.255 461.076 1.00 44.90 A C
ANISOU 853 CD2 PHE A 128 6879 3179 7001 410 390 -394 A C
ATOM 854 CE1 PHE A 128 18.037 29.097 458.533 1.00 42.43 A C
ANISOU 854 CE1 PHE A 128 6933 2869 6319 547 713 -379 A C
ATOM 855 CE2 PHE A 128 18.121 29.427 460.898 1.00 39.04 A C
ANISOU 855 CE2 PHE A 128 6025 2487 6319 457 550 -305 A C
ATOM 856 CZ PHE A 128 18.435 29.842 459.627 1.00 40.68 A C
ANISOU 856 CZ PHE A 128 6406 2695 6357 521 720 -291 A C
ATOM 857 N GLU A 129 15.535 23.185 459.830 1.00 43.84 A N
ANISOU 857 N GLU A 129 7530 2615 6512 306 -36 -842 A N
ATOM 858 CA GLU A 129 14.791 22.013 460.261 1.00 44.23 A C
ANISOU 858 CA GLU A 129 7635 2552 6617 203 -230 -906 A C
ATOM 859 C GLU A 129 15.735 20.856 460.550 1.00 45.15 A C
ANISOU 859 C GLU A 129 7805 2505 6844 300 -117 -971 A C
ATOM 860 O GLU A 129 15.554 20.131 461.539 1.00 44.62 A O
ANISOU 860 O GLU A 129 7647 2365 6944 237 -213 -946 A O
ATOM 861 CB GLU A 129 13.750 21.634 459.210 1.00 46.02 A C
ANISOU 861 CB GLU A 129 8118 2732 6634 121 -423 -1010 A C
ATOM 862 CG GLU A 129 12.661 22.690 458.992 1.00 49.55 A C
ANISOU 862 CG GLU A 129 8490 3325 7012 18 -593 -938 A C
ATOM 863 CD GLU A 129 13.134 23.925 458.211 1.00 53.47 A C
ANISOU 863 CD GLU A 129 9030 3937 7350 119 -447 -882 A C
ATOM 864 OE1 GLU A 129 14.338 24.029 457.897 1.00 60.27 A O
ANISOU 864 OE1 GLU A 129 9948 4778 8173 260 -186 -888 A O
ATOM 865 OE2 GLU A 129 12.293 24.804 457.924 1.00 62.14 A O1-
ANISOU 865 OE2 GLU A 129 10093 5137 8381 56 -590 -821 A O1-
ATOM 866 N ILE A 130 16.754 20.682 459.702 1.00 46.75 A N
ANISOU 866 N ILE A 130 8158 2644 6962 461 101 -1046 A N
ATOM 867 CA ILE A 130 17.749 19.636 459.921 1.00 47.93 A C
ANISOU 867 CA ILE A 130 8339 2628 7245 586 234 -1108 A C
ATOM 868 C ILE A 130 18.504 19.880 461.223 1.00 46.26 A C
ANISOU 868 C ILE A 130 7814 2451 7313 622 284 -982 A C
ATOM 869 O ILE A 130 18.645 18.979 462.062 1.00 46.31 A O
ANISOU 869 O ILE A 130 7773 2339 7483 618 207 -975 A O
ATOM 870 CB ILE A 130 18.709 19.569 458.722 1.00 50.22 A C
ANISOU 870 CB ILE A 130 8826 2858 7395 767 506 -1206 A C
ATOM 871 CG1 ILE A 130 17.940 19.181 457.473 1.00 52.30 A C
ANISOU 871 CG1 ILE A 130 9463 3062 7346 733 418 -1350 A C
ATOM 872 CG2 ILE A 130 19.832 18.604 458.995 1.00 51.54 A C
ANISOU 872 CG2 ILE A 130 8971 2859 7753 924 671 -1259 A C
ATOM 873 CD1 ILE A 130 18.771 19.175 456.254 1.00 54.83 A C
ANISOU 873 CD1 ILE A 130 10029 3335 7470 907 701 -1447 A C
ATOM 874 N GLN A 131 18.968 21.116 461.429 1.00 44.96 A N
ANISOU 874 N GLN A 131 7443 2437 7203 649 390 -875 A N
ATOM 875 CA GLN A 131 19.656 21.444 462.674 1.00 45.86 A C
ANISOU 875 CA GLN A 131 7269 2586 7570 672 396 -762 A C
ATOM 876 C GLN A 131 18.795 21.108 463.877 1.00 42.18 A C
ANISOU 876 C GLN A 131 6728 2123 7175 531 160 -703 A C
ATOM 877 O GLN A 131 19.276 20.525 464.853 1.00 42.13 A O
ANISOU 877 O GLN A 131 6628 2037 7342 561 115 -660 A O
ATOM 878 CB GLN A 131 20.051 22.929 462.718 1.00 42.41 A C
ANISOU 878 CB GLN A 131 6635 2309 7171 682 497 -662 A C
ATOM 879 CG GLN A 131 21.217 23.346 461.803 1.00 52.48 A C
ANISOU 879 CG GLN A 131 7902 3575 8463 832 787 -674 A C
ATOM 880 CD GLN A 131 22.236 22.235 461.510 1.00 46.13 A C
ANISOU 880 CD GLN A 131 7157 2604 7768 994 952 -758 A C
ATOM 881 NE2 GLN A 131 22.320 21.844 460.241 1.00 48.23 A N
ANISOU 881 NE2 GLN A 131 7681 2805 7839 1076 1123 -866 A N
ATOM 882 OE1 GLN A 131 22.949 21.770 462.395 1.00 46.17 A O
ANISOU 882 OE1 GLN A 131 6987 2534 8022 1053 926 -726 A O
ATOM 883 N PHE A 132 17.518 21.484 463.821 1.00 41.29 A N
ANISOU 883 N PHE A 132 6656 2099 6935 381 12 -690 A N
ATOM 884 CA PHE A 132 16.610 21.299 464.948 1.00 46.59 A C
ANISOU 884 CA PHE A 132 7240 2790 7671 238 -169 -620 A C
ATOM 885 C PHE A 132 16.372 19.823 465.233 1.00 41.37 A C
ANISOU 885 C PHE A 132 6713 1948 7060 202 -262 -665 A C
ATOM 886 O PHE A 132 16.355 19.404 466.399 1.00 41.12 A O
ANISOU 886 O PHE A 132 6593 1915 7115 158 -317 -577 A O
ATOM 887 CB PHE A 132 15.296 22.045 464.682 1.00 39.38 A C
ANISOU 887 CB PHE A 132 6318 2003 6642 99 -282 -601 A C
ATOM 888 CG PHE A 132 14.581 22.472 465.923 1.00 37.93 A C
ANISOU 888 CG PHE A 132 5959 1906 6545 -14 -378 -497 A C
ATOM 889 CD1 PHE A 132 15.265 23.093 466.947 1.00 36.76 A C
ANISOU 889 CD1 PHE A 132 5644 1821 6504 33 -325 -412 A C
ATOM 890 CD2 PHE A 132 13.222 22.265 466.059 1.00 38.03 A C
ANISOU 890 CD2 PHE A 132 5977 1933 6539 -168 -519 -488 A C
ATOM 891 CE1 PHE A 132 14.614 23.494 468.099 1.00 35.73 A C
ANISOU 891 CE1 PHE A 132 5392 1765 6418 -60 -393 -327 A C
ATOM 892 CE2 PHE A 132 12.539 22.672 467.205 1.00 38.25 A C
ANISOU 892 CE2 PHE A 132 5847 2041 6644 -263 -562 -391 A C
ATOM 893 CZ PHE A 132 13.237 23.281 468.230 1.00 50.96 A C
ANISOU 893 CZ PHE A 132 7331 3713 8319 -204 -491 -315 A C
ATOM 894 N GLN A 133 16.128 19.028 464.188 1.00 43.11 A N
ANISOU 894 N GLN A 133 7159 2048 7172 209 -275 -791 A N
ATOM 895 CA GLN A 133 15.935 17.601 464.402 1.00 44.55 A C
ANISOU 895 CA GLN A 133 7453 2088 7386 168 -333 -827 A C
ATOM 896 C GLN A 133 17.172 16.975 465.019 1.00 56.97 A C
ANISOU 896 C GLN A 133 8973 3593 9080 308 -215 -786 A C
ATOM 897 O GLN A 133 17.070 16.158 465.948 1.00 61.49 A O
ANISOU 897 O GLN A 133 9518 4130 9715 257 -274 -712 A O
ATOM 898 CB GLN A 133 15.585 16.908 463.098 1.00 46.64 A C
ANISOU 898 CB GLN A 133 7973 2241 7508 166 -360 -989 A C
ATOM 899 CG GLN A 133 15.604 15.431 463.200 1.00 48.49 A C
ANISOU 899 CG GLN A 133 8298 2334 7793 151 -376 -1037 A C
ATOM 900 CD GLN A 133 14.732 14.792 462.157 1.00 64.48 A C
ANISOU 900 CD GLN A 133 10537 4283 9678 60 -500 -1177 A C
ATOM 901 NE2 GLN A 133 15.198 13.676 461.588 1.00 62.58 A N
ANISOU 901 NE2 GLN A 133 10460 3890 9427 141 -446 -1298 A N
ATOM 902 OE1 GLN A 133 13.639 15.285 461.865 1.00 50.09 A O
ANISOU 902 OE1 GLN A 133 8729 2535 7769 -80 -659 -1178 A O
ATOM 903 N ARG A 134 18.353 17.357 464.525 1.00 45.51 A N
ANISOU 903 N ARG A 134 7507 2120 7665 490 -54 -824 A N
ATOM 904 CA ARG A 134 19.582 16.789 465.056 1.00 46.37 A C
ANISOU 904 CA ARG A 134 7548 2180 7893 639 21 -780 A C
ATOM 905 C ARG A 134 19.765 17.160 466.529 1.00 44.87 A C
ANISOU 905 C ARG A 134 7135 2107 7808 595 -68 -619 A C
ATOM 906 O ARG A 134 20.116 16.308 467.356 1.00 45.61 A O
ANISOU 906 O ARG A 134 7220 2139 7970 618 -122 -557 A O
ATOM 907 CB ARG A 134 20.760 17.255 464.213 1.00 47.32 A C
ANISOU 907 CB ARG A 134 7623 2300 8055 831 212 -843 A C
ATOM 908 CG ARG A 134 22.110 16.921 464.816 1.00 78.83 A C
ANISOU 908 CG ARG A 134 11447 6284 12221 983 275 -780 A C
ATOM 909 CD ARG A 134 23.231 17.027 463.788 1.00 83.15 A C
ANISOU 909 CD ARG A 134 11966 6807 12821 1170 515 -863 A C
ATOM 910 NE ARG A 134 23.740 18.392 463.668 1.00 78.94 A N
ANISOU 910 NE ARG A 134 11221 6417 12355 1190 659 -799 A N
ATOM 911 CZ ARG A 134 24.369 19.029 464.650 1.00 73.52 A C
ANISOU 911 CZ ARG A 134 10260 5831 11843 1189 612 -673 A C
ATOM 912 NH1 ARG A 134 24.544 18.422 465.816 1.00 72.89 A N1+
ANISOU 912 NH1 ARG A 134 10108 5730 11858 1175 433 -598 A N1+
ATOM 913 NH2 ARG A 134 24.812 20.271 464.474 1.00 74.16 A N
ANISOU 913 NH2 ARG A 134 10156 6023 11997 1196 738 -621 A N
ATOM 914 N ALA A 135 19.515 18.427 466.879 1.00 43.00 A N
ANISOU 914 N ALA A 135 6737 2024 7575 534 -90 -553 A N
ATOM 915 CA ALA A 135 19.622 18.862 468.270 1.00 41.77 A C
ANISOU 915 CA ALA A 135 6408 1973 7488 490 -183 -421 A C
ATOM 916 C ALA A 135 18.669 18.093 469.174 1.00 41.73 A C
ANISOU 916 C ALA A 135 6480 1939 7438 352 -314 -359 A C
ATOM 917 O ALA A 135 19.049 17.661 470.269 1.00 42.05 A O
ANISOU 917 O ALA A 135 6482 1960 7534 369 -379 -269 A O
ATOM 918 CB ALA A 135 19.359 20.360 468.378 1.00 39.98 A C
ANISOU 918 CB ALA A 135 6033 1900 7256 439 -177 -383 A C
ATOM 919 N PHE A 136 17.414 17.926 468.741 1.00 41.71 A N
ANISOU 919 N PHE A 136 6578 1926 7342 212 -358 -399 A N
ATOM 920 CA PHE A 136 16.458 17.170 469.547 1.00 41.92 A C
ANISOU 920 CA PHE A 136 6657 1919 7352 68 -454 -333 A C
ATOM 921 C PHE A 136 16.882 15.729 469.733 1.00 43.79 A C
ANISOU 921 C PHE A 136 7012 1995 7631 114 -458 -333 A C
ATOM 922 O PHE A 136 16.754 15.177 470.832 1.00 44.18 A O
ANISOU 922 O PHE A 136 7065 2011 7710 68 -515 -227 A O
ATOM 923 CB PHE A 136 15.078 17.192 468.919 1.00 41.92 A C
ANISOU 923 CB PHE A 136 6714 1930 7284 -90 -509 -384 A C
ATOM 924 CG PHE A 136 14.224 18.274 469.424 1.00 42.73 A C
ANISOU 924 CG PHE A 136 6686 2174 7375 -198 -550 -316 A C
ATOM 925 CD1 PHE A 136 14.689 19.578 469.467 1.00 38.93 A C
ANISOU 925 CD1 PHE A 136 6079 1811 6900 -128 -507 -300 A C
ATOM 926 CD2 PHE A 136 12.954 17.991 469.881 1.00 48.18 A C
ANISOU 926 CD2 PHE A 136 7366 2870 8070 -370 -617 -265 A C
ATOM 927 CE1 PHE A 136 13.896 20.581 469.954 1.00 37.71 A C
ANISOU 927 CE1 PHE A 136 5808 1775 6746 -218 -535 -244 A C
ATOM 928 CE2 PHE A 136 12.153 18.992 470.355 1.00 51.94 A C
ANISOU 928 CE2 PHE A 136 7712 3465 8556 -458 -632 -204 A C
ATOM 929 CZ PHE A 136 12.626 20.294 470.390 1.00 48.74 A C
ANISOU 929 CZ PHE A 136 7198 3174 8147 -377 -592 -198 A C
ATOM 930 N GLN A 137 17.351 15.082 468.667 1.00 45.22 A N
ANISOU 930 N GLN A 137 7312 2057 7811 206 -390 -451 A N
ATOM 931 CA GLN A 137 17.769 13.696 468.829 1.00 54.48 A C
ANISOU 931 CA GLN A 137 8598 3060 9041 260 -385 -455 A C
ATOM 932 C GLN A 137 18.933 13.593 469.810 1.00 49.31 A C
ANISOU 932 C GLN A 137 7852 2400 8486 395 -391 -352 A C
ATOM 933 O GLN A 137 18.916 12.760 470.734 1.00 49.46 A O
ANISOU 933 O GLN A 137 7906 2339 8549 371 -460 -260 A O
ATOM 934 CB GLN A 137 18.083 13.087 467.457 1.00 49.94 A C
ANISOU 934 CB GLN A 137 8180 2350 8445 347 -291 -619 A C
ATOM 935 CG GLN A 137 16.814 12.453 466.832 1.00 68.04 A C
ANISOU 935 CG GLN A 137 10603 4574 10676 179 -366 -705 A C
ATOM 936 CD GLN A 137 16.810 12.393 465.296 1.00 80.27 A C
ANISOU 936 CD GLN A 137 12295 6056 12150 228 -309 -896 A C
ATOM 937 NE2 GLN A 137 15.612 12.318 464.716 1.00 68.31 A N
ANISOU 937 NE2 GLN A 137 10859 4550 10547 69 -434 -966 A N
ATOM 938 OE1 GLN A 137 17.862 12.406 464.646 1.00 87.77 A O
ANISOU 938 OE1 GLN A 137 13285 6944 13120 409 -160 -979 A O
ATOM 939 N LYS A 138 19.907 14.492 469.686 1.00 46.75 A N
ANISOU 939 N LYS A 138 7393 2162 8208 526 -337 -356 A N
ATOM 940 CA LYS A 138 21.080 14.400 470.543 1.00 49.36 A C
ANISOU 940 CA LYS A 138 7606 2485 8662 658 -371 -271 A C
ATOM 941 C LYS A 138 20.730 14.699 471.995 1.00 48.63 A C
ANISOU 941 C LYS A 138 7446 2467 8563 564 -507 -128 A C
ATOM 942 O LYS A 138 21.186 13.995 472.897 1.00 66.08 A O
ANISOU 942 O LYS A 138 9674 4598 10835 609 -592 -40 A O
ATOM 943 CB LYS A 138 22.166 15.329 470.013 1.00 48.74 A C
ANISOU 943 CB LYS A 138 7364 2486 8669 801 -278 -311 A C
ATOM 944 CG LYS A 138 22.724 14.828 468.681 1.00 48.78 A C
ANISOU 944 CG LYS A 138 7465 2382 8688 938 -124 -445 A C
ATOM 945 CD LYS A 138 23.945 15.597 468.216 1.00 80.37 A C
ANISOU 945 CD LYS A 138 11273 6446 12817 1094 0 -469 A C
ATOM 946 CE LYS A 138 24.486 15.016 466.909 1.00 81.75 A C
ANISOU 946 CE LYS A 138 11564 6504 12994 1243 174 -607 A C
ATOM 947 NZ LYS A 138 25.386 15.968 466.190 1.00 85.49 A N1+
ANISOU 947 NZ LYS A 138 11855 7065 13563 1353 362 -640 A N1+
ATOM 948 N LEU A 139 19.891 15.699 472.249 1.00 44.56 A N
ANISOU 948 N LEU A 139 6878 2088 7966 437 -532 -102 A N
ATOM 949 CA LEU A 139 19.493 15.950 473.631 1.00 44.03 A C
ANISOU 949 CA LEU A 139 6791 2070 7867 352 -643 26 A C
ATOM 950 C LEU A 139 18.658 14.805 474.187 1.00 46.49 A C
ANISOU 950 C LEU A 139 7261 2267 8135 243 -686 93 A C
ATOM 951 O LEU A 139 18.859 14.385 475.337 1.00 47.70 A O
ANISOU 951 O LEU A 139 7459 2368 8298 249 -773 212 A O
ATOM 952 CB LEU A 139 18.734 17.270 473.746 1.00 42.04 A C
ANISOU 952 CB LEU A 139 6456 1974 7544 248 -637 31 A C
ATOM 953 CG LEU A 139 19.585 18.471 473.354 1.00 41.06 A C
ANISOU 953 CG LEU A 139 6164 1957 7479 345 -599 -13 A C
ATOM 954 CD1 LEU A 139 18.746 19.713 473.095 1.00 39.29 A C
ANISOU 954 CD1 LEU A 139 5875 1865 7187 249 -565 -36 A C
ATOM 955 CD2 LEU A 139 20.645 18.713 474.404 1.00 41.56 A C
ANISOU 955 CD2 LEU A 139 6132 2027 7631 438 -702 64 A C
ATOM 956 N ARG A 140 17.732 14.272 473.382 1.00 45.47 A N
ANISOU 956 N ARG A 140 7225 2087 7966 140 -634 23 A N
ATOM 957 CA ARG A 140 16.946 13.125 473.821 1.00 46.91 A C
ANISOU 957 CA ARG A 140 7539 2143 8139 26 -663 84 A C
ATOM 958 C ARG A 140 17.831 11.934 474.197 1.00 48.98 A C
ANISOU 958 C ARG A 140 7888 2242 8481 141 -694 128 A C
ATOM 959 O ARG A 140 17.459 11.146 475.070 1.00 54.97 A O
ANISOU 959 O ARG A 140 8739 2904 9242 73 -741 241 A O
ATOM 960 CB ARG A 140 15.939 12.742 472.733 1.00 47.24 A C
ANISOU 960 CB ARG A 140 7646 2146 8156 -94 -625 -24 A C
ATOM 961 CG ARG A 140 14.580 13.446 472.856 1.00 46.10 A C
ANISOU 961 CG ARG A 140 7445 2113 7959 -279 -637 2 A C
ATOM 962 CD ARG A 140 13.553 13.054 471.769 1.00 46.80 A C
ANISOU 962 CD ARG A 140 7581 2159 8041 -405 -646 -106 A C
ATOM 963 NE ARG A 140 13.530 11.622 471.466 1.00 68.76 A N
ANISOU 963 NE ARG A 140 10500 4753 10872 -421 -659 -143 A N
ATOM 964 CZ ARG A 140 12.667 10.751 471.984 1.00 76.86 A C
ANISOU 964 CZ ARG A 140 11577 5681 11944 -571 -687 -70 A C
ATOM 965 NH1 ARG A 140 11.730 11.153 472.841 1.00 81.18 A N1+
ANISOU 965 NH1 ARG A 140 12051 6302 12494 -718 -686 50 A N1+
ATOM 966 NH2 ARG A 140 12.739 9.473 471.636 1.00 84.67 A N
ANISOU 966 NH2 ARG A 140 12694 6488 12990 -573 -701 -117 A N
ATOM 967 N ASN A 141 19.015 11.802 473.592 1.00 49.60 A N
ANISOU 967 N ASN A 141 7933 2278 8634 320 -661 53 A N
ATOM 968 CA ASN A 141 19.893 10.688 473.944 1.00 52.35 A C
ANISOU 968 CA ASN A 141 8345 2464 9081 446 -695 95 A C
ATOM 969 C ASN A 141 20.622 10.852 475.274 1.00 52.18 A C
ANISOU 969 C ASN A 141 8265 2461 9100 519 -819 241 A C
ATOM 970 O ASN A 141 21.152 9.867 475.789 1.00 88.67 A O
ANISOU 970 O ASN A 141 12957 6941 13795 597 -881 312 A O
ATOM 971 CB ASN A 141 20.910 10.448 472.829 1.00 76.15 A C
ANISOU 971 CB ASN A 141 11344 5411 12177 624 -601 -35 A C
ATOM 972 CG ASN A 141 20.340 9.615 471.704 1.00 87.14 A C
ANISOU 972 CG ASN A 141 12893 6675 13542 579 -512 -165 A C
ATOM 973 ND2 ASN A 141 20.826 9.843 470.482 1.00 84.04 A N
ANISOU 973 ND2 ASN A 141 12511 6273 13147 687 -394 -309 A N
ATOM 974 OD1 ASN A 141 19.447 8.789 471.926 1.00 94.61 A O
ANISOU 974 OD1 ASN A 141 13956 7524 14469 444 -550 -137 A O
ATOM 975 N CYS A 142 20.663 12.046 475.842 1.00 51.38 A N
ANISOU 975 N CYS A 142 8049 2517 8954 498 -870 287 A N
ATOM 976 CA CYS A 142 21.346 12.272 477.112 1.00 51.10 A C
ANISOU 976 CA CYS A 142 7978 2496 8942 562 -1019 415 A C
ATOM 977 C CYS A 142 20.609 11.663 478.305 1.00 52.13 A C
ANISOU 977 C CYS A 142 8278 2550 8978 452 -1101 569 A C
ATOM 978 O CYS A 142 19.449 11.985 478.565 1.00 60.01 A O
ANISOU 978 O CYS A 142 9339 3600 9861 289 -1057 605 A O
ATOM 979 CB CYS A 142 21.504 13.768 477.330 1.00 49.17 A C
ANISOU 979 CB CYS A 142 7585 2429 8669 556 -1050 403 A C
ATOM 980 SG CYS A 142 22.564 14.539 476.135 1.00 48.48 A S
ANISOU 980 SG CYS A 142 7281 2421 8716 696 -958 263 A S
ATOM 981 N LYS A 143 21.305 10.842 479.086 1.00 73.01 A N
ANISOU 981 N LYS A 143 10994 5071 11675 544 -1220 674 A N
ATOM 982 CA LYS A 143 20.705 10.240 480.271 1.00 66.70 A C
ANISOU 982 CA LYS A 143 10382 4186 10774 452 -1295 843 A C
ATOM 983 C LYS A 143 21.227 10.847 481.568 1.00 56.19 A C
ANISOU 983 C LYS A 143 9076 2906 9368 499 -1479 968 A C
ATOM 984 O LYS A 143 20.733 10.501 482.643 1.00 57.47 A O
ANISOU 984 O LYS A 143 9425 3010 9402 424 -1540 1123 A O
ATOM 985 CB LYS A 143 20.898 8.714 480.245 1.00 65.51 A C
ANISOU 985 CB LYS A 143 10354 3827 10708 498 -1300 889 A C
ATOM 986 CG LYS A 143 20.355 8.065 478.974 1.00 64.83 A C
ANISOU 986 CG LYS A 143 10281 3668 10683 445 -1140 754 A C
ATOM 987 CD LYS A 143 21.343 7.138 478.299 1.00 64.89 A C
ANISOU 987 CD LYS A 143 10280 3529 10847 615 -1131 679 A C
ATOM 988 CE LYS A 143 20.929 6.882 476.848 1.00 65.29 A C
ANISOU 988 CE LYS A 143 10334 3547 10925 583 -973 499 A C
ATOM 989 NZ LYS A 143 21.666 5.761 476.189 1.00 69.74 A N1+
ANISOU 989 NZ LYS A 143 10956 3920 11623 727 -933 426 A N1+
ATOM 990 N THR A 144 22.170 11.781 481.485 1.00 61.46 A N
ANISOU 990 N THR A 144 9571 3678 10104 610 -1567 904 A N
ATOM 991 CA THR A 144 22.868 12.352 482.629 1.00 56.21 A C
ANISOU 991 CA THR A 144 8915 3048 9396 674 -1789 996 A C
ATOM 992 C THR A 144 22.932 13.871 482.514 1.00 57.53 A C
ANISOU 992 C THR A 144 8935 3385 9541 655 -1798 913 A C
ATOM 993 O THR A 144 22.953 14.421 481.410 1.00 52.25 A O
ANISOU 993 O THR A 144 8088 2801 8964 659 -1656 776 A O
ATOM 994 CB THR A 144 24.281 11.777 482.725 1.00 58.43 A C
ANISOU 994 CB THR A 144 9099 3241 9862 858 -1946 1008 A C
ATOM 995 CG2 THR A 144 25.155 12.552 483.700 1.00 82.86 A C
ANISOU 995 CG2 THR A 144 12139 6389 12955 930 -2207 1061 A C
ATOM 996 OG1 THR A 144 24.191 10.423 483.142 1.00 60.83 A O
ANISOU 996 OG1 THR A 144 9583 3374 10157 874 -1979 1119 A O
ATOM 997 N HIS A 145 22.908 14.544 483.671 1.00 54.40 A N
ANISOU 997 N HIS A 145 8643 3027 8999 629 -1964 1000 A N
ATOM 998 CA HIS A 145 23.228 15.966 483.767 1.00 53.01 A C
ANISOU 998 CA HIS A 145 8336 2980 8826 638 -2039 930 A C
ATOM 999 C HIS A 145 24.461 16.365 482.943 1.00 52.78 A C
ANISOU 999 C HIS A 145 8001 2996 9058 766 -2065 812 A C
ATOM 1000 O HIS A 145 24.376 17.218 482.055 1.00 61.66 A O
ANISOU 1000 O HIS A 145 8950 4225 10253 745 -1924 696 A O
ATOM 1001 CB HIS A 145 23.415 16.309 485.253 1.00 54.64 A C
ANISOU 1001 CB HIS A 145 8740 3167 8855 642 -2292 1047 A C
ATOM 1002 CG HIS A 145 23.906 17.700 485.514 1.00 64.59 A C
ANISOU 1002 CG HIS A 145 9888 4524 10128 666 -2434 976 A C
ATOM 1003 CD2 HIS A 145 25.150 18.172 485.772 1.00 55.02 A C
ANISOU 1003 CD2 HIS A 145 8516 3322 9069 771 -2672 941 A C
ATOM 1004 ND1 HIS A 145 23.068 18.798 485.543 1.00 59.32 A N
ANISOU 1004 ND1 HIS A 145 9267 3947 9325 566 -2338 929 A N
ATOM 1005 CE1 HIS A 145 23.775 19.884 485.798 1.00 51.95 A C
ANISOU 1005 CE1 HIS A 145 8221 3067 8451 614 -2510 864 A C
ATOM 1006 NE2 HIS A 145 25.041 19.534 485.940 1.00 57.25 A N
ANISOU 1006 NE2 HIS A 145 8756 3693 9303 730 -2719 871 A N
ATOM 1007 N ASN A 146 25.606 15.726 483.192 1.00 58.67 A N
ANISOU 1007 N ASN A 146 8677 3657 9959 897 -2228 848 A N
ATOM 1008 CA ASN A 146 26.840 16.041 482.468 1.00 55.40 A C
ANISOU 1008 CA ASN A 146 7957 3270 9822 1018 -2239 754 A C
ATOM 1009 C ASN A 146 26.662 15.952 480.960 1.00 53.86 A C
ANISOU 1009 C ASN A 146 7628 3108 9729 1025 -1943 632 A C
ATOM 1010 O ASN A 146 27.033 16.863 480.215 1.00 52.66 A O
ANISOU 1010 O ASN A 146 7263 3052 9694 1039 -1848 535 A O
ATOM 1011 CB ASN A 146 27.958 15.094 482.909 1.00 58.50 A C
ANISOU 1011 CB ASN A 146 8312 3537 10377 1156 -2427 822 A C
ATOM 1012 CG ASN A 146 28.537 15.455 484.258 1.00 72.43 A C
ANISOU 1012 CG ASN A 146 10132 5287 12101 1179 -2773 911 A C
ATOM 1013 ND2 ASN A 146 29.029 14.449 484.976 1.00 70.59 A N
ANISOU 1013 ND2 ASN A 146 10009 4927 11883 1257 -2960 1019 A N
ATOM 1014 OD1 ASN A 146 28.537 16.624 484.659 1.00 82.57 A O
ANISOU 1014 OD1 ASN A 146 11379 6662 13331 1127 -2884 881 A O
ATOM 1015 N ASP A 147 26.157 14.824 480.486 1.00 58.77 A N
ANISOU 1015 N ASP A 147 8383 3636 10310 1019 -1804 636 A N
ATOM 1016 CA ASP A 147 26.016 14.635 479.051 1.00 57.19 A C
ANISOU 1016 CA ASP A 147 8107 3444 10178 1035 -1549 514 A C
ATOM 1017 C ASP A 147 25.113 15.694 478.454 1.00 50.54 A C
ANISOU 1017 C ASP A 147 7243 2740 9219 914 -1401 436 A C
ATOM 1018 O ASP A 147 25.347 16.164 477.334 1.00 57.93 A O
ANISOU 1018 O ASP A 147 8040 3736 10235 946 -1240 328 A O
ATOM 1019 CB ASP A 147 25.490 13.232 478.773 1.00 59.64 A C
ANISOU 1019 CB ASP A 147 8611 3610 10440 1027 -1462 531 A C
ATOM 1020 CG ASP A 147 26.365 12.182 479.399 1.00 76.15 A C
ANISOU 1020 CG ASP A 147 10732 5553 12650 1153 -1613 619 A C
ATOM 1021 OD1 ASP A 147 27.527 12.027 478.949 1.00 84.38 A O1-
ANISOU 1021 OD1 ASP A 147 11596 6558 13906 1307 -1613 572 A O1-
ATOM 1022 OD2 ASP A 147 25.905 11.550 480.375 1.00 86.11 A O1-
ANISOU 1022 OD2 ASP A 147 12191 6733 13796 1100 -1732 744 A O1-
ATOM 1023 N LEU A 148 24.058 16.071 479.175 1.00 52.31 A N
ANISOU 1023 N LEU A 148 7615 3011 9252 777 -1442 494 A N
ATOM 1024 CA LEU A 148 23.154 17.080 478.645 1.00 47.03 A C
ANISOU 1024 CA LEU A 148 6918 2467 8484 663 -1310 425 A C
ATOM 1025 C LEU A 148 23.838 18.437 478.551 1.00 52.44 A C
ANISOU 1025 C LEU A 148 7394 3269 9262 702 -1345 373 A C
ATOM 1026 O LEU A 148 23.768 19.093 477.511 1.00 67.84 A O
ANISOU 1026 O LEU A 148 9224 5301 11253 695 -1189 279 A O
ATOM 1027 CB LEU A 148 21.896 17.164 479.485 1.00 46.44 A C
ANISOU 1027 CB LEU A 148 7037 2401 8208 515 -1332 506 A C
ATOM 1028 CG LEU A 148 20.941 18.177 478.871 1.00 56.33 A C
ANISOU 1028 CG LEU A 148 8240 3777 9386 404 -1192 430 A C
ATOM 1029 CD1 LEU A 148 19.598 17.561 478.686 1.00 51.25 A C
ANISOU 1029 CD1 LEU A 148 7742 3098 8633 265 -1081 449 A C
ATOM 1030 CD2 LEU A 148 20.824 19.405 479.742 1.00 43.44 A C
ANISOU 1030 CD2 LEU A 148 6596 2227 7681 367 -1287 460 A C
ATOM 1031 N ILE A 149 24.514 18.883 479.611 1.00 47.04 A N
ANISOU 1031 N ILE A 149 6672 2585 8615 742 -1559 435 A N
ATOM 1032 CA ILE A 149 25.102 20.219 479.537 1.00 46.30 A C
ANISOU 1032 CA ILE A 149 6377 2590 8626 757 -1601 381 A C
ATOM 1033 C ILE A 149 26.225 20.271 478.496 1.00 46.89 A C
ANISOU 1033 C ILE A 149 6196 2671 8949 866 -1499 309 A C
ATOM 1034 O ILE A 149 26.374 21.272 477.777 1.00 45.76 A O
ANISOU 1034 O ILE A 149 5888 2616 8881 851 -1382 239 A O
ATOM 1035 CB ILE A 149 25.578 20.696 480.919 1.00 47.52 A C
ANISOU 1035 CB ILE A 149 6567 2725 8762 768 -1889 450 A C
ATOM 1036 CG1 ILE A 149 26.766 19.865 481.425 1.00 52.09 A C
ANISOU 1036 CG1 ILE A 149 7093 3201 9497 889 -2089 509 A C
ATOM 1037 CG2 ILE A 149 24.407 20.708 481.894 1.00 47.12 A C
ANISOU 1037 CG2 ILE A 149 6806 2663 8436 662 -1944 523 A C
ATOM 1038 CD1 ILE A 149 27.431 20.432 482.667 1.00 51.79 A C
ANISOU 1038 CD1 ILE A 149 7062 3145 9471 909 -2417 558 A C
ATOM 1039 N ASN A 150 27.004 19.195 478.352 1.00 48.85 A N
ANISOU 1039 N ASN A 150 6414 2817 9330 976 -1517 328 A N
ATOM 1040 CA ASN A 150 28.034 19.221 477.316 1.00 49.70 A C
ANISOU 1040 CA ASN A 150 6289 2920 9674 1084 -1378 260 A C
ATOM 1041 C ASN A 150 27.430 19.148 475.913 1.00 48.38 A C
ANISOU 1041 C ASN A 150 6165 2781 9434 1066 -1087 169 A C
ATOM 1042 O ASN A 150 27.844 19.895 475.014 1.00 47.97 A O
ANISOU 1042 O ASN A 150 5946 2792 9491 1090 -930 106 A O
ATOM 1043 CB ASN A 150 29.019 18.078 477.525 1.00 62.72 A C
ANISOU 1043 CB ASN A 150 7896 4442 11493 1219 -1465 300 A C
ATOM 1044 CG ASN A 150 29.819 18.235 478.793 1.00 68.69 A C
ANISOU 1044 CG ASN A 150 8573 5167 12359 1251 -1778 382 A C
ATOM 1045 ND2 ASN A 150 29.866 17.171 479.599 1.00 65.80 A N
ANISOU 1045 ND2 ASN A 150 8366 4689 11944 1294 -1945 468 A N
ATOM 1046 OD1 ASN A 150 30.385 19.301 479.057 1.00 70.71 A O
ANISOU 1046 OD1 ASN A 150 8638 5487 12740 1233 -1884 370 A O
ATOM 1047 N THR A 151 26.438 18.271 475.705 1.00 47.92 A N
ANISOU 1047 N THR A 151 6343 2670 9195 1016 -1018 164 A N
ATOM 1048 CA THR A 151 25.773 18.219 474.408 1.00 46.87 A C
ANISOU 1048 CA THR A 151 6285 2553 8971 986 -789 70 A C
ATOM 1049 C THR A 151 25.192 19.576 474.045 1.00 58.63 A C
ANISOU 1049 C THR A 151 7711 4181 10383 889 -716 33 A C
ATOM 1050 O THR A 151 25.338 20.035 472.904 1.00 54.21 A O
ANISOU 1050 O THR A 151 7082 3658 9856 918 -536 -42 A O
ATOM 1051 CB THR A 151 24.661 17.169 474.401 1.00 46.79 A C
ANISOU 1051 CB THR A 151 6533 2460 8784 908 -776 75 A C
ATOM 1052 CG2 THR A 151 23.946 17.158 473.056 1.00 45.95 A C
ANISOU 1052 CG2 THR A 151 6517 2361 8581 867 -585 -34 A C
ATOM 1053 OG1 THR A 151 25.192 15.865 474.644 1.00 48.98 A O
ANISOU 1053 OG1 THR A 151 6883 2588 9138 1003 -826 107 A O
ATOM 1054 N LEU A 152 24.567 20.253 475.016 1.00 43.52 A N
ANISOU 1054 N LEU A 152 5829 2337 8369 784 -848 89 A N
ATOM 1055 CA LEU A 152 23.950 21.543 474.738 1.00 41.61 A C
ANISOU 1055 CA LEU A 152 5537 2218 8057 694 -785 56 A C
ATOM 1056 C LEU A 152 24.988 22.593 474.386 1.00 43.33 A C
ANISOU 1056 C LEU A 152 5514 2493 8458 755 -746 32 A C
ATOM 1057 O LEU A 152 24.794 23.367 473.438 1.00 44.88 A O
ANISOU 1057 O LEU A 152 5650 2753 8648 734 -587 -19 A O
ATOM 1058 CB LEU A 152 23.115 22.012 475.924 1.00 64.32 A C
ANISOU 1058 CB LEU A 152 8510 5135 10795 585 -926 117 A C
ATOM 1059 CG LEU A 152 22.527 23.421 475.720 1.00 38.97 A C
ANISOU 1059 CG LEU A 152 5234 2042 7531 504 -870 82 A C
ATOM 1060 CD1 LEU A 152 21.505 23.449 474.592 1.00 37.80 A C
ANISOU 1060 CD1 LEU A 152 5150 1933 7279 438 -697 24 A C
ATOM 1061 CD2 LEU A 152 21.944 23.972 476.999 1.00 38.58 A C
ANISOU 1061 CD2 LEU A 152 5271 2014 7374 427 -1012 134 A C
ATOM 1062 N THR A 153 26.091 22.650 475.135 1.00 49.71 A N
ANISOU 1062 N THR A 153 6177 3269 9442 824 -897 75 A N
ATOM 1063 CA THR A 153 27.129 23.611 474.776 1.00 46.76 A C
ANISOU 1063 CA THR A 153 5542 2934 9292 867 -856 56 A C
ATOM 1064 C THR A 153 27.651 23.361 473.359 1.00 44.47 A C
ANISOU 1064 C THR A 153 5163 2623 9111 952 -595 2 A C
ATOM 1065 O THR A 153 27.786 24.303 472.560 1.00 43.96 A O
ANISOU 1065 O THR A 153 4983 2616 9105 936 -434 -26 A O
ATOM 1066 CB THR A 153 28.256 23.581 475.809 1.00 52.21 A C
ANISOU 1066 CB THR A 153 6080 3571 10184 923 -1094 108 A C
ATOM 1067 CG2 THR A 153 29.273 24.610 475.493 1.00 65.57 A C
ANISOU 1067 CG2 THR A 153 7484 5292 12138 940 -1064 94 A C
ATOM 1068 OG1 THR A 153 27.726 23.881 477.104 1.00 46.44 A O
ANISOU 1068 OG1 THR A 153 5482 2849 9314 850 -1335 152 A O
ATOM 1069 N ARG A 154 27.897 22.095 473.007 1.00 48.78 A N
ANISOU 1069 N ARG A 154 5790 3074 9668 1043 -538 -13 A N
ATOM 1070 CA ARG A 154 28.418 21.799 471.671 1.00 62.84 A C
ANISOU 1070 CA ARG A 154 7523 4818 11537 1142 -279 -75 A C
ATOM 1071 C ARG A 154 27.408 22.172 470.575 1.00 45.37 A C
ANISOU 1071 C ARG A 154 5468 2650 9121 1081 -87 -140 A C
ATOM 1072 O ARG A 154 27.765 22.818 469.584 1.00 45.65 A O
ANISOU 1072 O ARG A 154 5411 2713 9222 1113 123 -172 A O
ATOM 1073 CB ARG A 154 28.829 20.319 471.603 1.00 48.93 A C
ANISOU 1073 CB ARG A 154 5848 2927 9816 1258 -277 -88 A C
ATOM 1074 CG ARG A 154 28.958 19.716 470.198 1.00 59.78 A C
ANISOU 1074 CG ARG A 154 7306 4235 11172 1357 -9 -179 A C
ATOM 1075 CD ARG A 154 29.490 18.270 470.199 1.00 64.12 A C
ANISOU 1075 CD ARG A 154 7929 4641 11794 1489 -17 -196 A C
ATOM 1076 NE ARG A 154 28.796 17.360 471.126 1.00 75.95 A N
ANISOU 1076 NE ARG A 154 9627 6072 13160 1437 -227 -150 A N
ATOM 1077 CZ ARG A 154 27.576 16.843 470.934 1.00 74.70 A C
ANISOU 1077 CZ ARG A 154 9740 5879 12763 1347 -228 -183 A C
ATOM 1078 NH1 ARG A 154 26.865 17.146 469.845 1.00 71.86 A N1+
ANISOU 1078 NH1 ARG A 154 9502 5547 12254 1301 -65 -272 A N1+
ATOM 1079 NH2 ARG A 154 27.060 16.018 471.839 1.00 66.84 A N
ANISOU 1079 NH2 ARG A 154 8894 4814 11687 1295 -398 -120 A N
ATOM 1080 N LEU A 155 26.132 21.796 470.756 1.00 70.03 A N
ANISOU 1080 N LEU A 155 8826 5776 12006 986 -158 -151 A N
ATOM 1081 CA LEU A 155 25.082 22.126 469.785 1.00 45.42 A C
ANISOU 1081 CA LEU A 155 5862 2692 8703 916 -28 -212 A C
ATOM 1082 C LEU A 155 24.936 23.632 469.605 1.00 41.31 A C
ANISOU 1082 C LEU A 155 5218 2285 8193 851 22 -195 A C
ATOM 1083 O LEU A 155 24.803 24.122 468.479 1.00 41.25 A O
ANISOU 1083 O LEU A 155 5235 2289 8147 863 206 -238 A O
ATOM 1084 CB LEU A 155 23.744 21.536 470.221 1.00 41.59 A C
ANISOU 1084 CB LEU A 155 5596 2192 8013 800 -151 -209 A C
ATOM 1085 CG LEU A 155 23.450 20.056 470.070 1.00 42.75 A C
ANISOU 1085 CG LEU A 155 5941 2211 8093 823 -167 -242 A C
ATOM 1086 CD1 LEU A 155 22.199 19.760 470.846 1.00 41.71 A C
ANISOU 1086 CD1 LEU A 155 5946 2088 7814 676 -305 -198 A C
ATOM 1087 CD2 LEU A 155 23.296 19.623 468.628 1.00 43.61 A C
ANISOU 1087 CD2 LEU A 155 6192 2244 8134 874 3 -354 A C
ATOM 1088 N ILE A 156 24.878 24.378 470.713 1.00 40.37 A N
ANISOU 1088 N ILE A 156 4997 2236 8106 779 -144 -134 A N
ATOM 1089 CA ILE A 156 24.747 25.825 470.610 1.00 39.26 A C
ANISOU 1089 CA ILE A 156 4744 2187 7986 717 -110 -119 A C
ATOM 1090 C ILE A 156 25.916 26.400 469.821 1.00 47.98 A C
ANISOU 1090 C ILE A 156 5649 3280 9301 799 68 -119 A C
ATOM 1091 O ILE A 156 25.738 27.310 469.004 1.00 40.09 A O
ANISOU 1091 O ILE A 156 4628 2317 8286 776 222 -123 A O
ATOM 1092 CB ILE A 156 24.606 26.459 472.004 1.00 42.01 A C
ANISOU 1092 CB ILE A 156 5035 2586 8342 643 -329 -70 A C
ATOM 1093 CG1 ILE A 156 23.312 25.965 472.678 1.00 37.42 A C
ANISOU 1093 CG1 ILE A 156 4662 2015 7542 555 -441 -62 A C
ATOM 1094 CG2 ILE A 156 24.662 28.002 471.929 1.00 37.75 A C
ANISOU 1094 CG2 ILE A 156 4359 2119 7864 591 -301 -61 A C
ATOM 1095 CD1 ILE A 156 22.016 26.287 471.916 1.00 36.06 A C
ANISOU 1095 CD1 ILE A 156 4611 1891 7198 471 -341 -96 A C
ATOM 1096 N GLN A 157 27.129 25.867 470.035 1.00 61.87 A N
ANISOU 1096 N GLN A 157 7256 4980 11274 896 62 -103 A N
ATOM 1097 CA GLN A 157 28.273 26.301 469.229 1.00 44.09 A C
ANISOU 1097 CA GLN A 157 4794 2706 9253 974 272 -97 A C
ATOM 1098 C GLN A 157 28.123 25.938 467.754 1.00 44.78 A C
ANISOU 1098 C GLN A 157 5018 2756 9242 1045 568 -153 A C
ATOM 1099 O GLN A 157 28.442 26.747 466.873 1.00 49.75 A O
ANISOU 1099 O GLN A 157 5569 3397 9936 1058 794 -141 A O
ATOM 1100 CB GLN A 157 29.560 25.691 469.750 1.00 46.32 A C
ANISOU 1100 CB GLN A 157 4875 2924 9800 1065 200 -71 A C
ATOM 1101 CG GLN A 157 30.669 25.887 468.757 1.00 48.49 A C
ANISOU 1101 CG GLN A 157 4952 3163 10310 1154 477 -69 A C
ATOM 1102 CD GLN A 157 32.001 25.794 469.375 1.00 60.32 A C
ANISOU 1102 CD GLN A 157 6157 4614 12146 1203 381 -24 A C
ATOM 1103 NE2 GLN A 157 32.475 24.570 469.572 1.00 60.22 A N
ANISOU 1103 NE2 GLN A 157 6161 4527 12192 1308 332 -38 A N
ATOM 1104 OE1 GLN A 157 32.621 26.811 469.684 1.00 73.34 A O
ANISOU 1104 OE1 GLN A 157 7562 6280 14022 1144 337 24 A O
ATOM 1105 N GLU A 158 27.681 24.715 467.461 1.00 45.10 A N
ANISOU 1105 N GLU A 158 5276 2733 9129 1095 574 -214 A N
ATOM 1106 CA GLU A 158 27.531 24.294 466.072 1.00 46.12 A C
ANISOU 1106 CA GLU A 158 5579 2805 9138 1170 834 -290 A C
ATOM 1107 C GLU A 158 26.495 25.160 465.345 1.00 58.09 A C
ANISOU 1107 C GLU A 158 7250 4369 10450 1085 917 -305 A C
ATOM 1108 O GLU A 158 26.650 25.465 464.157 1.00 54.17 A O
ANISOU 1108 O GLU A 158 6826 3849 9905 1142 1182 -332 A O
ATOM 1109 CB GLU A 158 27.174 22.800 466.037 1.00 52.24 A C
ANISOU 1109 CB GLU A 158 6576 3485 9789 1222 768 -362 A C
ATOM 1110 CG GLU A 158 28.380 21.885 466.390 1.00 58.45 A C
ANISOU 1110 CG GLU A 158 7222 4194 10793 1352 765 -354 A C
ATOM 1111 CD GLU A 158 28.031 20.407 466.730 1.00 63.99 A C
ANISOU 1111 CD GLU A 158 8124 4787 11402 1389 627 -397 A C
ATOM 1112 OE1 GLU A 158 26.843 20.053 466.876 1.00 58.26 A O
ANISOU 1112 OE1 GLU A 158 7627 4048 10460 1291 502 -422 A O
ATOM 1113 OE2 GLU A 158 28.971 19.588 466.872 1.00 76.70 A O1-
ANISOU 1113 OE2 GLU A 158 9651 6315 13177 1513 642 -398 A O1-
ATOM 1114 N ILE A 159 25.436 25.567 466.046 1.00 42.44 A N
ANISOU 1114 N ILE A 159 5331 2449 8344 955 704 -281 A N
ATOM 1115 CA ILE A 159 24.392 26.391 465.444 1.00 41.14 A C
ANISOU 1115 CA ILE A 159 5298 2324 8007 871 744 -288 A C
ATOM 1116 C ILE A 159 24.810 27.853 465.349 1.00 40.85 A C
ANISOU 1116 C ILE A 159 5079 2352 8092 846 837 -213 A C
ATOM 1117 O ILE A 159 24.691 28.481 464.295 1.00 41.29 A O
ANISOU 1117 O ILE A 159 5212 2452 8024 845 1019 -204 A O
ATOM 1118 CB ILE A 159 23.088 26.235 466.241 1.00 39.26 A C
ANISOU 1118 CB ILE A 159 5173 2128 7618 742 494 -289 A C
ATOM 1119 CG1 ILE A 159 22.665 24.771 466.229 1.00 39.86 A C
ANISOU 1119 CG1 ILE A 159 5439 2117 7591 754 422 -355 A C
ATOM 1120 CG2 ILE A 159 22.015 27.110 465.671 1.00 38.15 A C
ANISOU 1120 CG2 ILE A 159 5133 2095 7265 643 495 -282 A C
ATOM 1121 CD1 ILE A 159 21.356 24.500 466.902 1.00 38.49 A C
ANISOU 1121 CD1 ILE A 159 5373 1967 7283 620 217 -349 A C
ATOM 1122 N SER A 160 25.252 28.439 466.456 1.00 40.27 A N
ANISOU 1122 N SER A 160 4787 2334 8180 799 680 -152 A N
ATOM 1123 CA SER A 160 25.499 29.877 466.482 1.00 47.12 A C
ANISOU 1123 CA SER A 160 5493 3249 9163 748 722 -87 A C
ATOM 1124 C SER A 160 26.802 30.255 465.794 1.00 59.92 A C
ANISOU 1124 C SER A 160 6925 4822 11020 830 973 -47 A C
ATOM 1125 O SER A 160 26.958 31.404 465.360 1.00 54.68 A O
ANISOU 1125 O SER A 160 6180 4167 10427 798 1100 12 A O
ATOM 1126 CB SER A 160 25.512 30.387 467.915 1.00 38.92 A C
ANISOU 1126 CB SER A 160 4314 2268 8207 666 457 -55 A C
ATOM 1127 OG SER A 160 26.703 29.969 468.544 1.00 48.04 A O
ANISOU 1127 OG SER A 160 5276 3386 9591 721 393 -41 A O
ATOM 1128 N GLY A 161 27.754 29.332 465.733 1.00 43.79 A N
ANISOU 1128 N GLY A 161 4796 2726 9115 930 1049 -67 A N
ATOM 1129 CA GLY A 161 29.022 29.608 465.117 1.00 46.15 A C
ANISOU 1129 CA GLY A 161 4885 2981 9668 1008 1308 -26 A C
ATOM 1130 C GLY A 161 29.991 30.373 465.977 1.00 46.82 A C
ANISOU 1130 C GLY A 161 4633 3073 10084 958 1192 45 A C
ATOM 1131 O GLY A 161 31.051 30.766 465.480 1.00 48.97 A O
ANISOU 1131 O GLY A 161 4687 3304 10617 996 1414 97 A O
ATOM 1132 N TYR A 162 29.679 30.560 467.255 1.00 45.38 A N
ANISOU 1132 N TYR A 162 4407 2929 9904 874 856 45 A N
ATOM 1133 CA TYR A 162 30.500 31.380 468.131 1.00 48.75 A C
ANISOU 1133 CA TYR A 162 4549 3347 10628 812 696 95 A C
ATOM 1134 C TYR A 162 31.746 30.635 468.577 1.00 51.77 A C
ANISOU 1134 C TYR A 162 4709 3671 11292 882 633 103 A C
ATOM 1135 O TYR A 162 31.725 29.420 468.793 1.00 48.67 A O
ANISOU 1135 O TYR A 162 4420 3262 10812 957 563 64 A O
ATOM 1136 CB TYR A 162 29.714 31.814 469.363 1.00 51.02 A C
ANISOU 1136 CB TYR A 162 4914 3685 10784 710 360 79 A C
ATOM 1137 CG TYR A 162 28.900 33.031 469.122 1.00 42.58 A C
ANISOU 1137 CG TYR A 162 3924 2659 9596 619 393 94 A C
ATOM 1138 CD1 TYR A 162 27.785 32.968 468.316 1.00 58.35 A C
ANISOU 1138 CD1 TYR A 162 6171 4695 11303 616 526 76 A C
ATOM 1139 CD2 TYR A 162 29.251 34.253 469.673 1.00 42.82 A C
ANISOU 1139 CD2 TYR A 162 3780 2674 9815 535 280 125 A C
ATOM 1140 CE1 TYR A 162 27.013 34.081 468.080 1.00 59.60 A C
ANISOU 1140 CE1 TYR A 162 6403 4888 11354 538 545 99 A C
ATOM 1141 CE2 TYR A 162 28.490 35.381 469.429 1.00 52.47 A C
ANISOU 1141 CE2 TYR A 162 5086 3926 10924 457 315 141 A C
ATOM 1142 CZ TYR A 162 27.362 35.273 468.631 1.00 40.18 A C
ANISOU 1142 CZ TYR A 162 3778 2420 9069 462 450 132 A C
ATOM 1143 OH TYR A 162 26.567 36.337 468.357 1.00 53.41 A O
ANISOU 1143 OH TYR A 162 5542 4124 10626 393 474 155 A O
ATOM 1144 N ASP A 163 32.830 31.396 468.752 1.00 55.62 A N
ANISOU 1144 N ASP A 163 4884 4112 12139 847 640 159 A N
ATOM 1145 CA ASP A 163 34.122 30.803 469.083 1.00 60.59 A C
ANISOU 1145 CA ASP A 163 5260 4672 13091 905 593 177 A C
ATOM 1146 C ASP A 163 34.122 30.140 470.458 1.00 65.59 A C
ANISOU 1146 C ASP A 163 5918 5297 13706 904 191 149 A C
ATOM 1147 O ASP A 163 34.868 29.175 470.671 1.00 66.92 A O
ANISOU 1147 O ASP A 163 5999 5413 14015 990 142 149 A O
ATOM 1148 CB ASP A 163 35.215 31.864 469.000 1.00 60.53 A C
ANISOU 1148 CB ASP A 163 4908 4600 13492 836 665 248 A C
ATOM 1149 CG ASP A 163 35.600 32.179 467.568 1.00 74.65 A C
ANISOU 1149 CG ASP A 163 6637 6363 15363 876 1128 299 A C
ATOM 1150 OD1 ASP A 163 35.401 31.302 466.693 1.00 72.65 A O
ANISOU 1150 OD1 ASP A 163 6558 6125 14920 991 1382 268 A O
ATOM 1151 OD2 ASP A 163 36.106 33.299 467.321 1.00 79.47 A O1-
ANISOU 1151 OD2 ASP A 163 7044 6927 16224 793 1242 372 A O1-
ATOM 1152 N ARG A 164 33.320 30.639 471.405 1.00 50.67 A N
ANISOU 1152 N ARG A 164 4157 3450 11646 815 -91 131 A N
ATOM 1153 CA ARG A 164 33.272 30.046 472.736 1.00 50.65 A C
ANISOU 1153 CA ARG A 164 4221 3432 11592 817 -462 115 A C
ATOM 1154 C ARG A 164 31.857 30.067 473.284 1.00 57.18 A C
ANISOU 1154 C ARG A 164 5365 4329 12032 765 -600 82 A C
ATOM 1155 O ARG A 164 31.167 31.086 473.197 1.00 53.42 A O
ANISOU 1155 O ARG A 164 4953 3901 11445 681 -573 73 A O
ATOM 1156 CB ARG A 164 34.193 30.782 473.699 1.00 53.82 A C
ANISOU 1156 CB ARG A 164 4372 3768 12311 752 -747 136 A C
ATOM 1157 CG ARG A 164 34.077 30.329 475.127 1.00 52.55 A C
ANISOU 1157 CG ARG A 164 4324 3583 12060 750 -1156 122 A C
ATOM 1158 CD ARG A 164 35.202 30.942 475.874 1.00 67.60 A C
ANISOU 1158 CD ARG A 164 5962 5397 14328 700 -1423 136 A C
ATOM 1159 NE ARG A 164 35.091 32.391 475.807 1.00 82.56 A N
ANISOU 1159 NE ARG A 164 7764 7287 16319 586 -1421 124 A N
ATOM 1160 CZ ARG A 164 36.041 33.226 476.224 1.00 89.38 A C
ANISOU 1160 CZ ARG A 164 8372 8049 17538 509 -1602 131 A C
ATOM 1161 NH1 ARG A 164 37.178 32.725 476.719 1.00 75.82 A N1+
ANISOU 1161 NH1 ARG A 164 6469 6234 16106 536 -1798 150 A N1+
ATOM 1162 NH2 ARG A 164 35.860 34.552 476.133 1.00 77.22 A N
ANISOU 1162 NH2 ARG A 164 6771 6488 16081 405 -1593 119 A N
ATOM 1163 N VAL A 165 31.451 28.957 473.901 1.00 48.47 A N
ANISOU 1163 N VAL A 165 4455 3219 10742 812 -750 72 A N
ATOM 1164 CA VAL A 165 30.107 28.800 474.451 1.00 50.46 A C
ANISOU 1164 CA VAL A 165 5011 3523 10638 761 -857 53 A C
ATOM 1165 C VAL A 165 30.234 28.149 475.820 1.00 54.67 A C
ANISOU 1165 C VAL A 165 5629 4007 11138 778 -1186 74 A C
ATOM 1166 O VAL A 165 30.943 27.149 475.972 1.00 47.90 A O
ANISOU 1166 O VAL A 165 4719 3084 10397 864 -1246 98 A O
ATOM 1167 CB VAL A 165 29.197 27.964 473.526 1.00 44.02 A C
ANISOU 1167 CB VAL A 165 4417 2736 9571 793 -626 29 A C
ATOM 1168 CG1 VAL A 165 27.900 27.617 474.211 1.00 42.27 A C
ANISOU 1168 CG1 VAL A 165 4477 2547 9035 733 -751 23 A C
ATOM 1169 CG2 VAL A 165 28.922 28.713 472.226 1.00 43.22 A C
ANISOU 1169 CG2 VAL A 165 4292 2680 9449 772 -333 11 A C
ATOM 1170 N MET A 166 29.546 28.716 476.810 1.00 45.14 A N
ANISOU 1170 N MET A 166 4569 2819 9763 704 -1394 69 A N
ATOM 1171 CA MET A 166 29.644 28.308 478.199 1.00 46.20 A C
ANISOU 1171 CA MET A 166 4820 2894 9838 714 -1727 96 A C
ATOM 1172 C MET A 166 28.250 28.233 478.798 1.00 44.42 A C
ANISOU 1172 C MET A 166 4919 2704 9254 655 -1762 95 A C
ATOM 1173 O MET A 166 27.319 28.886 478.327 1.00 52.72 A O
ANISOU 1173 O MET A 166 6045 3828 10158 587 -1592 61 A O
ATOM 1174 CB MET A 166 30.499 29.298 478.991 1.00 61.35 A C
ANISOU 1174 CB MET A 166 6567 4763 11978 682 -2002 85 A C
ATOM 1175 CG MET A 166 31.966 29.252 478.646 1.00 61.41 A C
ANISOU 1175 CG MET A 166 6237 4711 12385 728 -2022 100 A C
ATOM 1176 SD MET A 166 32.693 30.902 478.672 1.00 75.40 A S
ANISOU 1176 SD MET A 166 7728 6450 14469 636 -2113 68 A S
ATOM 1177 CE MET A 166 32.359 31.410 480.344 1.00 79.42 A C
ANISOU 1177 CE MET A 166 8457 6905 14813 590 -2576 38 A C
ATOM 1178 N ILE A 167 28.102 27.403 479.822 1.00 45.32 A N
ANISOU 1178 N ILE A 167 5226 2758 9234 681 -1972 141 A N
ATOM 1179 CA ILE A 167 26.899 27.369 480.646 1.00 44.32 A C
ANISOU 1179 CA ILE A 167 5413 2636 8792 621 -2037 157 A C
ATOM 1180 C ILE A 167 27.262 27.825 482.048 1.00 47.47 A C
ANISOU 1180 C ILE A 167 5914 2964 9160 620 -2392 171 A C
ATOM 1181 O ILE A 167 28.147 27.240 482.691 1.00 48.15 A O
ANISOU 1181 O ILE A 167 5977 2972 9345 685 -2637 218 A O
ATOM 1182 CB ILE A 167 26.242 25.979 480.657 1.00 44.20 A C
ANISOU 1182 CB ILE A 167 5606 2592 8598 638 -1958 215 A C
ATOM 1183 CG1 ILE A 167 25.655 25.683 479.282 1.00 42.56 A C
ANISOU 1183 CG1 ILE A 167 5354 2445 8369 621 -1632 178 A C
ATOM 1184 CG2 ILE A 167 25.193 25.873 481.741 1.00 44.01 A C
ANISOU 1184 CG2 ILE A 167 5900 2538 8283 577 -2062 261 A C
ATOM 1185 CD1 ILE A 167 24.775 24.447 479.223 1.00 53.89 A C
ANISOU 1185 CD1 ILE A 167 7008 3846 9624 605 -1544 219 A C
ATOM 1186 N TYR A 168 26.602 28.884 482.509 1.00 45.11 A N
ANISOU 1186 N TYR A 168 5738 2682 8722 550 -2430 124 A N
ATOM 1187 CA TYR A 168 26.762 29.363 483.873 1.00 46.74 A C
ANISOU 1187 CA TYR A 168 6119 2858 8782 532 -2739 113 A C
ATOM 1188 C TYR A 168 25.631 28.809 484.712 1.00 46.59 A C
ANISOU 1188 C TYR A 168 6470 2879 8353 492 -2706 158 A C
ATOM 1189 O TYR A 168 24.464 28.941 484.331 1.00 59.22 A O
ANISOU 1189 O TYR A 168 8158 4575 9766 424 -2431 140 A O
ATOM 1190 CB TYR A 168 26.675 30.876 484.004 1.00 59.43 A C
ANISOU 1190 CB TYR A 168 7673 4524 10383 457 -2756 11 A C
ATOM 1191 CG TYR A 168 27.485 31.717 483.096 1.00 59.72 A C
ANISOU 1191 CG TYR A 168 7362 4543 10786 454 -2702 -36 A C
ATOM 1192 CD1 TYR A 168 28.828 31.483 482.903 1.00 58.64 A C
ANISOU 1192 CD1 TYR A 168 6952 4304 11023 521 -2866 -6 A C
ATOM 1193 CD2 TYR A 168 26.897 32.803 482.457 1.00 62.77 A C
ANISOU 1193 CD2 TYR A 168 7685 5010 11153 381 -2481 -102 A C
ATOM 1194 CE1 TYR A 168 29.568 32.304 482.060 1.00 75.42 A C
ANISOU 1194 CE1 TYR A 168 8742 6444 13472 493 -2762 -40 A C
ATOM 1195 CE2 TYR A 168 27.615 33.617 481.614 1.00 65.84 A C
ANISOU 1195 CE2 TYR A 168 7773 5374 11870 367 -2408 -127 A C
ATOM 1196 CZ TYR A 168 28.955 33.374 481.418 1.00 77.27 A C
ANISOU 1196 CZ TYR A 168 8945 6739 13674 418 -2537 -94 A C
ATOM 1197 OH TYR A 168 29.674 34.204 480.582 1.00 80.66 A O
ANISOU 1197 OH TYR A 168 9063 7169 14417 385 -2421 -107 A O
ATOM 1198 N GLN A 169 25.963 28.189 485.838 1.00 48.80 A N
ANISOU 1198 N GLN A 169 6962 3079 8501 534 -2982 227 A N
ATOM 1199 CA GLN A 169 24.938 27.800 486.787 1.00 49.19 A C
ANISOU 1199 CA GLN A 169 7391 3161 8139 490 -2949 279 A C
ATOM 1200 C GLN A 169 25.010 28.721 487.993 1.00 50.87 A C
ANISOU 1200 C GLN A 169 7815 3386 8128 466 -3182 219 A C
ATOM 1201 O GLN A 169 26.080 28.883 488.592 1.00 70.45 A O
ANISOU 1201 O GLN A 169 10272 5776 10720 518 -3542 213 A O
ATOM 1202 CB GLN A 169 25.069 26.346 487.221 1.00 50.71 A C
ANISOU 1202 CB GLN A 169 7757 3247 8266 549 -3054 419 A C
ATOM 1203 CG GLN A 169 23.877 25.925 488.030 1.00 51.02 A C
ANISOU 1203 CG GLN A 169 8169 3324 7892 483 -2929 490 A C
ATOM 1204 CD GLN A 169 24.043 24.581 488.629 1.00 70.06 A C
ANISOU 1204 CD GLN A 169 10797 5610 10213 534 -3066 644 A C
ATOM 1205 NE2 GLN A 169 23.025 24.146 489.351 1.00 81.27 A N
ANISOU 1205 NE2 GLN A 169 12547 7049 11282 471 -2937 730 A N
ATOM 1206 OE1 GLN A 169 25.070 23.921 488.449 1.00 71.56 A O
ANISOU 1206 OE1 GLN A 169 10854 5677 10659 633 -3275 696 A O
ATOM 1207 N PHE A 170 23.867 29.318 488.338 1.00 50.15 A N
ANISOU 1207 N PHE A 170 7926 3396 7732 392 -2980 169 A N
ATOM 1208 CA PHE A 170 23.761 30.183 489.502 1.00 51.78 A C
ANISOU 1208 CA PHE A 170 8395 3614 7664 373 -3148 95 A C
ATOM 1209 C PHE A 170 23.573 29.344 490.751 1.00 61.72 A C
ANISOU 1209 C PHE A 170 10062 4822 8568 398 -3295 202 A C
ATOM 1210 O PHE A 170 22.864 28.335 490.731 1.00 53.93 A O
ANISOU 1210 O PHE A 170 9206 3843 7442 385 -3098 321 A O
ATOM 1211 CB PHE A 170 22.590 31.149 489.366 1.00 50.20 A C
ANISOU 1211 CB PHE A 170 8250 3533 7291 303 -2840 -3 A C
ATOM 1212 CG PHE A 170 22.806 32.223 488.348 1.00 48.35 A C
ANISOU 1212 CG PHE A 170 7681 3334 7355 279 -2748 -113 A C
ATOM 1213 CD1 PHE A 170 23.769 33.187 488.536 1.00 49.48 A C
ANISOU 1213 CD1 PHE A 170 7713 3417 7672 287 -3014 -212 A C
ATOM 1214 CD2 PHE A 170 22.025 32.282 487.207 1.00 55.85 A C
ANISOU 1214 CD2 PHE A 170 8441 4368 8412 242 -2406 -113 A C
ATOM 1215 CE1 PHE A 170 23.966 34.184 487.597 1.00 48.00 A C
ANISOU 1215 CE1 PHE A 170 7228 3247 7765 256 -2912 -295 A C
ATOM 1216 CE2 PHE A 170 22.220 33.276 486.264 1.00 44.27 A C
ANISOU 1216 CE2 PHE A 170 6697 2926 7197 223 -2320 -196 A C
ATOM 1217 CZ PHE A 170 23.191 34.226 486.463 1.00 45.39 A C
ANISOU 1217 CZ PHE A 170 6731 3002 7514 229 -2558 -280 A C
ATOM 1218 N ASP A 171 24.181 29.792 491.841 1.00 62.94 A N
ANISOU 1218 N ASP A 171 10432 4917 8564 427 -3643 160 A N
ATOM 1219 CA ASP A 171 24.027 29.219 493.168 1.00 64.54 A C
ANISOU 1219 CA ASP A 171 11093 5071 8359 453 -3815 249 A C
ATOM 1220 C ASP A 171 22.983 30.007 493.944 1.00 74.89 A C
ANISOU 1220 C ASP A 171 12741 6467 9246 404 -3622 164 A C
ATOM 1221 O ASP A 171 22.502 31.045 493.475 1.00 73.36 A O
ANISOU 1221 O ASP A 171 12400 6355 9118 360 -3412 26 A O
ATOM 1222 CB ASP A 171 25.385 29.210 493.887 1.00 63.03 A C
ANISOU 1222 CB ASP A 171 10950 4749 8249 525 -4358 252 A C
ATOM 1223 CG ASP A 171 25.723 30.541 494.560 1.00 75.77 A C
ANISOU 1223 CG ASP A 171 12675 6356 9756 506 -4607 78 A C
ATOM 1224 OD1 ASP A 171 25.098 31.572 494.248 1.00 74.47 A O1-
ANISOU 1224 OD1 ASP A 171 12450 6278 9565 447 -4361 -60 A O1-
ATOM 1225 OD2 ASP A 171 26.639 30.552 495.411 1.00 79.09 A O1-
ANISOU 1225 OD2 ASP A 171 13248 6670 10131 553 -5078 77 A O1-
ATOM 1226 N PRO A 172 22.584 29.540 495.139 1.00 80.05 A N
ANISOU 1226 N PRO A 172 13864 7098 9453 418 -3666 247 A N
ATOM 1227 CA PRO A 172 21.463 30.206 495.831 1.00 72.35 A C
ANISOU 1227 CA PRO A 172 13214 6209 8067 381 -3389 172 A C
ATOM 1228 C PRO A 172 21.675 31.688 496.080 1.00 64.38 A C
ANISOU 1228 C PRO A 172 12215 5214 7033 380 -3510 -49 A C
ATOM 1229 O PRO A 172 20.692 32.428 496.192 1.00 79.39 A O
ANISOU 1229 O PRO A 172 14217 7198 8749 352 -3191 -147 A O
ATOM 1230 CB PRO A 172 21.357 29.424 497.146 1.00 67.50 A C
ANISOU 1230 CB PRO A 172 13126 5534 6988 413 -3513 310 A C
ATOM 1231 CG PRO A 172 21.845 28.091 496.810 1.00 67.40 A C
ANISOU 1231 CG PRO A 172 13003 5438 7167 438 -3632 502 A C
ATOM 1232 CD PRO A 172 22.964 28.296 495.832 1.00 65.67 A C
ANISOU 1232 CD PRO A 172 12305 5174 7473 468 -3885 434 A C
ATOM 1233 N GLU A 173 22.922 32.142 496.188 1.00 80.67 A N
ANISOU 1233 N GLU A 173 14171 7183 9295 411 -3965 -130 A N
ATOM 1234 CA GLU A 173 23.247 33.549 496.399 1.00 73.14 A C
ANISOU 1234 CA GLU A 173 13210 6210 8369 399 -4132 -344 A C
ATOM 1235 C GLU A 173 23.487 34.304 495.095 1.00 63.23 A C
ANISOU 1235 C GLU A 173 11430 4981 7611 358 -4019 -437 A C
ATOM 1236 O GLU A 173 23.940 35.449 495.135 1.00 63.83 A O
ANISOU 1236 O GLU A 173 11432 5012 7810 340 -4197 -602 A O
ATOM 1237 CB GLU A 173 24.465 33.680 497.325 1.00 70.06 A C
ANISOU 1237 CB GLU A 173 13014 5686 7921 440 -4727 -386 A C
ATOM 1238 CG GLU A 173 24.223 33.174 498.746 1.00 83.97 A C
ANISOU 1238 CG GLU A 173 15385 7411 9108 484 -4873 -321 A C
ATOM 1239 CD GLU A 173 25.362 33.508 499.694 1.00 97.01 A C
ANISOU 1239 CD GLU A 173 17263 8926 10668 521 -5499 -397 A C
ATOM 1240 OE1 GLU A 173 26.350 34.129 499.247 1.00100.46 A O
ANISOU 1240 OE1 GLU A 173 17347 9293 11532 503 -5818 -500 A O
ATOM 1241 OE2 GLU A 173 25.265 33.147 500.888 1.00111.69 A O1-
ANISOU 1241 OE2 GLU A 173 19660 10744 12032 563 -5676 -349 A O1-
ATOM 1242 N TRP A 174 23.250 33.670 493.944 1.00 72.36 A N
ANISOU 1242 N TRP A 174 12241 6195 9056 343 -3748 -330 A N
ATOM 1243 CA TRP A 174 23.374 34.263 492.606 1.00 68.23 A C
ANISOU 1243 CA TRP A 174 11250 5708 8969 308 -3582 -388 A C
ATOM 1244 C TRP A 174 24.817 34.438 492.154 1.00 67.98 A C
ANISOU 1244 C TRP A 174 10882 5575 9373 320 -3933 -405 A C
ATOM 1245 O TRP A 174 25.087 35.193 491.222 1.00 56.06 A O
ANISOU 1245 O TRP A 174 9026 4070 8205 287 -3851 -474 A O
ATOM 1246 CB TRP A 174 22.614 35.586 492.501 1.00 72.85 A C
ANISOU 1246 CB TRP A 174 11847 6348 9483 270 -3357 -548 A C
ATOM 1247 CG TRP A 174 21.171 35.316 492.604 1.00 65.82 A C
ANISOU 1247 CG TRP A 174 11144 5566 8297 261 -2936 -508 A C
ATOM 1248 CD1 TRP A 174 20.357 35.570 493.670 1.00 57.31 A C
ANISOU 1248 CD1 TRP A 174 10474 4514 6787 274 -2821 -558 A C
ATOM 1249 CD2 TRP A 174 20.370 34.656 491.627 1.00 52.68 A C
ANISOU 1249 CD2 TRP A 174 9270 3992 6754 235 -2574 -401 A C
ATOM 1250 CE2 TRP A 174 19.067 34.570 492.146 1.00 53.06 A C
ANISOU 1250 CE2 TRP A 174 9573 4117 6470 225 -2252 -386 A C
ATOM 1251 CE3 TRP A 174 20.624 34.145 490.356 1.00 50.22 A C
ANISOU 1251 CE3 TRP A 174 8588 3697 6798 221 -2488 -324 A C
ATOM 1252 NE1 TRP A 174 19.085 35.135 493.398 1.00 55.92 A N
ANISOU 1252 NE1 TRP A 174 10313 4441 6493 255 -2387 -481 A N
ATOM 1253 CZ2 TRP A 174 18.018 33.986 491.435 1.00 51.07 A C
ANISOU 1253 CZ2 TRP A 174 9185 3952 6266 189 -1882 -292 A C
ATOM 1254 CZ3 TRP A 174 19.582 33.574 489.648 1.00 59.61 A C
ANISOU 1254 CZ3 TRP A 174 9685 4972 7992 189 -2132 -244 A C
ATOM 1255 CH2 TRP A 174 18.296 33.493 490.191 1.00 48.66 A C
ANISOU 1255 CH2 TRP A 174 8529 3656 6304 168 -1850 -226 A C
ATOM 1256 N ASN A 175 25.746 33.728 492.783 1.00 72.75 A N
ANISOU 1256 N ASN A 175 11573 6081 9988 370 -4316 -329 A N
ATOM 1257 CA ASN A 175 27.049 33.521 492.182 1.00 66.93 A C
ANISOU 1257 CA ASN A 175 10445 5254 9732 396 -4577 -293 A C
ATOM 1258 C ASN A 175 26.914 32.536 491.026 1.00 57.97 A C
ANISOU 1258 C ASN A 175 9027 4161 8838 421 -4280 -164 A C
ATOM 1259 O ASN A 175 25.962 31.753 490.951 1.00 56.70 A O
ANISOU 1259 O ASN A 175 9034 4068 8443 422 -3995 -76 A O
ATOM 1260 CB ASN A 175 28.027 32.969 493.216 1.00 64.20 A C
ANISOU 1260 CB ASN A 175 10277 4784 9334 457 -5088 -237 A C
ATOM 1261 CG ASN A 175 28.289 33.933 494.338 1.00 72.43 A C
ANISOU 1261 CG ASN A 175 11607 5763 10148 434 -5444 -379 A C
ATOM 1262 ND2 ASN A 175 28.058 33.483 495.561 1.00 75.79 A N
ANISOU 1262 ND2 ASN A 175 12523 6163 10112 472 -5639 -340 A N
ATOM 1263 OD1 ASN A 175 28.669 35.082 494.114 1.00 76.48 A O
ANISOU 1263 OD1 ASN A 175 11933 6245 10882 379 -5537 -525 A O
ATOM 1264 N GLY A 176 27.897 32.544 490.132 1.00 57.55 A N
ANISOU 1264 N GLY A 176 8548 4054 9265 440 -4350 -153 A N
ATOM 1265 CA GLY A 176 27.856 31.703 488.951 1.00 59.10 A C
ANISOU 1265 CA GLY A 176 8475 4277 9705 472 -4066 -58 A C
ATOM 1266 C GLY A 176 29.095 30.835 488.833 1.00 63.93 A C
ANISOU 1266 C GLY A 176 8866 4768 10658 563 -4329 35 A C
ATOM 1267 O GLY A 176 30.193 31.230 489.234 1.00 66.42 A O
ANISOU 1267 O GLY A 176 9040 4985 11212 584 -4702 4 A O
ATOM 1268 N ARG A 177 28.909 29.650 488.250 1.00 56.18 A N
ANISOU 1268 N ARG A 177 7840 3782 9724 620 -4135 145 A N
ATOM 1269 CA ARG A 177 30.004 28.741 487.935 1.00 62.60 A C
ANISOU 1269 CA ARG A 177 8409 4475 10899 727 -4302 234 A C
ATOM 1270 C ARG A 177 29.910 28.327 486.478 1.00 55.35 A C
ANISOU 1270 C ARG A 177 7194 3632 10206 729 -3881 237 A C
ATOM 1271 O ARG A 177 28.827 27.959 486.012 1.00 53.09 A O
ANISOU 1271 O ARG A 177 7054 3400 9718 705 -3571 258 A O
ATOM 1272 CB ARG A 177 29.964 27.498 488.835 1.00 72.63 A C
ANISOU 1272 CB ARG A 177 9981 5688 11925 787 -4485 355 A C
ATOM 1273 CG ARG A 177 31.200 26.628 488.715 1.00 82.93 A C
ANISOU 1273 CG ARG A 177 11025 6953 13529 847 -4624 397 A C
ATOM 1274 CD ARG A 177 31.252 25.527 489.767 1.00 84.41 A C
ANISOU 1274 CD ARG A 177 11531 7072 13468 899 -4858 511 A C
ATOM 1275 NE ARG A 177 30.422 24.367 489.484 1.00 79.72 A N
ANISOU 1275 NE ARG A 177 11112 6491 12686 919 -4577 613 A N
ATOM 1276 CZ ARG A 177 30.686 23.158 489.969 1.00 82.65 A C
ANISOU 1276 CZ ARG A 177 11619 6796 12989 976 -4686 722 A C
ATOM 1277 NH1 ARG A 177 31.745 22.984 490.748 1.00 89.68 A N1+
ANISOU 1277 NH1 ARG A 177 12489 7610 13976 1022 -5065 740 A N1+
ATOM 1278 NH2 ARG A 177 29.903 22.130 489.684 1.00 76.63 A N
ANISOU 1278 NH2 ARG A 177 11009 6030 12076 981 -4424 811 A N
ATOM 1279 N VAL A 178 31.036 28.362 485.766 1.00 56.21 A N
ANISOU 1279 N VAL A 178 6902 3743 10713 749 -3862 214 A N
ATOM 1280 CA VAL A 178 31.082 27.826 484.406 1.00 64.65 A C
ANISOU 1280 CA VAL A 178 7729 4879 11957 769 -3473 221 A C
ATOM 1281 C VAL A 178 31.228 26.311 484.517 1.00 60.14 A C
ANISOU 1281 C VAL A 178 7249 4270 11331 849 -3471 309 A C
ATOM 1282 O VAL A 178 32.270 25.806 484.933 1.00 58.48 A O
ANISOU 1282 O VAL A 178 6924 3987 11308 906 -3704 342 A O
ATOM 1283 CB VAL A 178 32.224 28.437 483.587 1.00 55.52 A C
ANISOU 1283 CB VAL A 178 6138 3722 11235 761 -3409 175 A C
ATOM 1284 CG1 VAL A 178 32.276 27.818 482.208 1.00 54.34 A C
ANISOU 1284 CG1 VAL A 178 5804 3630 11212 799 -3004 186 A C
ATOM 1285 CG2 VAL A 178 32.044 29.911 483.481 1.00 54.57 A C
ANISOU 1285 CG2 VAL A 178 5941 3621 11174 676 -3406 98 A C
ATOM 1286 N ILE A 179 30.192 25.586 484.106 1.00 55.19 A N
ANISOU 1286 N ILE A 179 6816 3682 10471 847 -3205 342 A N
ATOM 1287 CA ILE A 179 30.101 24.149 484.334 1.00 58.67 A C
ANISOU 1287 CA ILE A 179 7417 4067 10806 910 -3209 430 A C
ATOM 1288 C ILE A 179 30.218 23.330 483.054 1.00 64.83 A C
ANISOU 1288 C ILE A 179 8028 4867 11739 960 -2883 420 A C
ATOM 1289 O ILE A 179 30.340 22.097 483.128 1.00 55.29 A O
ANISOU 1289 O ILE A 179 6904 3591 10513 1026 -2885 483 A O
ATOM 1290 CB ILE A 179 28.800 23.808 485.081 1.00 53.99 A C
ANISOU 1290 CB ILE A 179 7240 3465 9807 859 -3206 493 A C
ATOM 1291 CG1 ILE A 179 27.601 24.268 484.243 1.00 50.86 A C
ANISOU 1291 CG1 ILE A 179 6883 3158 9284 775 -2859 439 A C
ATOM 1292 CG2 ILE A 179 28.839 24.441 486.462 1.00 55.59 A C
ANISOU 1292 CG2 ILE A 179 7672 3622 9827 840 -3563 513 A C
ATOM 1293 CD1 ILE A 179 26.267 23.865 484.785 1.00 50.07 A C
ANISOU 1293 CD1 ILE A 179 7144 3044 8836 709 -2780 503 A C
ATOM 1294 N ALA A 180 30.201 23.971 481.897 1.00 69.96 A N
ANISOU 1294 N ALA A 180 8466 5593 12523 935 -2610 344 A N
ATOM 1295 CA ALA A 180 30.390 23.333 480.611 1.00 52.00 A C
ANISOU 1295 CA ALA A 180 6048 3330 10378 990 -2302 319 A C
ATOM 1296 C ALA A 180 30.862 24.414 479.653 1.00 61.51 A C
ANISOU 1296 C ALA A 180 6967 4602 11804 966 -2123 248 A C
ATOM 1297 O ALA A 180 30.601 25.604 479.853 1.00 50.28 A O
ANISOU 1297 O ALA A 180 5518 3230 10355 885 -2170 215 A O
ATOM 1298 CB ALA A 180 29.109 22.676 480.101 1.00 49.99 A C
ANISOU 1298 CB ALA A 180 6038 3101 9855 954 -2062 319 A C
ATOM 1299 N GLU A 181 31.606 23.988 478.645 1.00 53.73 A N
ANISOU 1299 N GLU A 181 5775 3598 11040 1042 -1919 230 A N
ATOM 1300 CA GLU A 181 32.258 24.910 477.736 1.00 52.34 A C
ANISOU 1300 CA GLU A 181 5312 3462 11113 1029 -1737 187 A C
ATOM 1301 C GLU A 181 32.553 24.146 476.460 1.00 60.01 A C
ANISOU 1301 C GLU A 181 6213 4417 12172 1121 -1415 166 A C
ATOM 1302 O GLU A 181 32.764 22.933 476.489 1.00 65.31 A O
ANISOU 1302 O GLU A 181 6956 5016 12841 1215 -1423 186 A O
ATOM 1303 CB GLU A 181 33.540 25.463 478.360 1.00 54.89 A C
ANISOU 1303 CB GLU A 181 5357 3728 11771 1031 -1987 204 A C
ATOM 1304 CG GLU A 181 34.369 26.374 477.503 1.00 55.66 A C
ANISOU 1304 CG GLU A 181 5124 3835 12187 1007 -1805 180 A C
ATOM 1305 CD GLU A 181 35.742 26.624 478.120 1.00 83.47 A C
ANISOU 1305 CD GLU A 181 8358 7267 16088 1011 -2062 202 A C
ATOM 1306 OE1 GLU A 181 36.286 25.691 478.770 1.00 84.84 A O
ANISOU 1306 OE1 GLU A 181 8542 7365 16329 1087 -2274 237 A O
ATOM 1307 OE2 GLU A 181 36.280 27.747 477.952 1.00 89.94 A O1-
ANISOU 1307 OE2 GLU A 181 8945 8078 17151 932 -2058 188 A O1-
ATOM 1308 N SER A 182 32.569 24.864 475.343 1.00 57.68 A N
ANISOU 1308 N SER A 182 5796 4176 11943 1099 -1131 127 A N
ATOM 1309 CA SER A 182 32.919 24.275 474.054 1.00 52.87 A C
ANISOU 1309 CA SER A 182 5130 3544 11412 1193 -806 99 A C
ATOM 1310 C SER A 182 33.604 25.410 473.310 1.00 53.47 A C
ANISOU 1310 C SER A 182 4935 3650 11733 1161 -616 95 A C
ATOM 1311 O SER A 182 32.945 26.360 472.874 1.00 51.58 A O
ANISOU 1311 O SER A 182 4744 3481 11373 1077 -497 79 A O
ATOM 1312 CB SER A 182 31.680 23.751 473.324 1.00 50.80 A C
ANISOU 1312 CB SER A 182 5170 3312 10818 1187 -612 55 A C
ATOM 1313 OG SER A 182 31.980 23.052 472.138 1.00 51.92 A O
ANISOU 1313 OG SER A 182 5319 3409 10998 1292 -329 12 A O
ATOM 1314 N VAL A 183 34.928 25.322 473.201 1.00 56.36 A N
ANISOU 1314 N VAL A 183 5009 3949 12455 1224 -593 120 A N
ATOM 1315 CA VAL A 183 35.762 26.474 472.880 1.00 64.51 A C
ANISOU 1315 CA VAL A 183 5735 4980 13798 1164 -502 143 A C
ATOM 1316 C VAL A 183 36.877 26.051 471.937 1.00 72.30 A C
ANISOU 1316 C VAL A 183 6494 5902 15073 1268 -216 154 A C
ATOM 1317 O VAL A 183 37.617 25.107 472.235 1.00101.49 A O
ANISOU 1317 O VAL A 183 10107 9524 18932 1368 -303 164 A O
ATOM 1318 CB VAL A 183 36.346 27.143 474.143 1.00 64.21 A C
ANISOU 1318 CB VAL A 183 5521 4902 13972 1081 -886 172 A C
ATOM 1319 CG1 VAL A 183 37.118 26.151 475.008 1.00 65.68 A C
ANISOU 1319 CG1 VAL A 183 5645 5001 14310 1162 -1158 197 A C
ATOM 1320 CG2 VAL A 183 37.226 28.323 473.768 1.00 62.34 A C
ANISOU 1320 CG2 VAL A 183 4961 4634 14090 1003 -787 198 A C
ATOM 1321 N ARG A 184 36.938 26.670 470.765 1.00 70.31 A N
ANISOU 1321 N ARG A 184 6178 5675 14862 1258 146 154 A N
ATOM 1322 CA ARG A 184 38.110 26.516 469.914 1.00 70.94 A C
ANISOU 1322 CA ARG A 184 6006 5688 15258 1338 440 179 A C
ATOM 1323 C ARG A 184 39.298 27.163 470.624 1.00 83.32 A C
ANISOU 1323 C ARG A 184 7209 7185 17265 1268 243 239 A C
ATOM 1324 O ARG A 184 39.136 28.152 471.343 1.00 88.15 A O
ANISOU 1324 O ARG A 184 7763 7808 17921 1135 3 256 A O
ATOM 1325 CB ARG A 184 37.831 27.182 468.579 1.00 63.32 A C
ANISOU 1325 CB ARG A 184 5090 4764 14207 1324 862 181 A C
ATOM 1326 CG ARG A 184 36.450 26.778 468.109 1.00 60.36 A C
ANISOU 1326 CG ARG A 184 5108 4457 13370 1348 941 115 A C
ATOM 1327 CD ARG A 184 35.958 27.556 466.931 1.00 62.71 A C
ANISOU 1327 CD ARG A 184 5511 4798 13520 1319 1286 119 A C
ATOM 1328 NE ARG A 184 34.621 27.100 466.582 1.00 71.68 A N
ANISOU 1328 NE ARG A 184 7029 5980 14225 1335 1297 48 A N
ATOM 1329 CZ ARG A 184 33.906 27.598 465.582 1.00 81.84 A C
ANISOU 1329 CZ ARG A 184 8506 7302 15287 1320 1545 35 A C
ATOM 1330 NH1 ARG A 184 34.409 28.578 464.836 1.00 92.16 A N1+
ANISOU 1330 NH1 ARG A 184 9664 8604 16747 1295 1826 99 A N1+
ATOM 1331 NH2 ARG A 184 32.692 27.126 465.338 1.00 53.80 A N
ANISOU 1331 NH2 ARG A 184 5298 3776 11369 1323 1506 -35 A N
ATOM 1332 N GLN A 185 40.527 26.609 470.422 1.00 93.24 A N
ANISOU 1332 N GLN A 185 8214 8348 18865 1360 336 266 A N
ATOM 1333 CA GLN A 185 41.659 27.166 471.211 1.00 86.81 A C
ANISOU 1333 CA GLN A 185 7057 7440 18486 1285 85 319 A C
ATOM 1334 C GLN A 185 42.065 28.589 470.738 1.00 92.23 A C
ANISOU 1334 C GLN A 185 7527 8103 19414 1151 260 372 A C
ATOM 1335 O GLN A 185 43.122 29.152 471.106 1.00102.51 A O
ANISOU 1335 O GLN A 185 8520 9299 21132 1084 142 422 A O
ATOM 1336 CB GLN A 185 42.872 26.231 471.186 1.00 92.64 A C
ANISOU 1336 CB GLN A 185 7566 8072 19559 1416 113 340 A C
ATOM 1337 CG GLN A 185 43.952 26.550 472.250 1.00102.84 A C
ANISOU 1337 CG GLN A 185 8552 9252 21270 1353 -264 385 A C
ATOM 1338 CD GLN A 185 45.286 25.844 471.978 1.00 95.65 A C
ANISOU 1338 CD GLN A 185 7344 8224 20774 1476 -150 420 A C
ATOM 1339 NE2 GLN A 185 45.751 25.055 472.940 1.00 86.61 A N
ANISOU 1339 NE2 GLN A 185 6148 7008 19753 1544 -511 423 A N
ATOM 1340 OE1 GLN A 185 45.884 26.013 470.917 1.00 88.63 A O
ANISOU 1340 OE1 GLN A 185 6283 7304 20090 1513 263 448 A O
ATOM 1341 N LEU A 186 41.186 29.175 469.926 1.00 95.14 A N
ANISOU 1341 N LEU A 186 8077 8555 19515 1111 530 365 A N
ATOM 1342 CA LEU A 186 41.196 30.588 469.579 1.00106.31 A C
ANISOU 1342 CA LEU A 186 9385 9960 21048 973 655 415 A C
ATOM 1343 C LEU A 186 40.924 31.473 470.811 1.00101.97 A C
ANISOU 1343 C LEU A 186 8819 9396 20530 827 207 404 A C
ATOM 1344 O LEU A 186 41.006 32.708 470.718 1.00 82.33 A O
ANISOU 1344 O LEU A 186 6227 6868 18187 703 235 442 A O
ATOM 1345 CB LEU A 186 40.128 30.832 468.496 1.00102.73 A C
ANISOU 1345 CB LEU A 186 9201 9607 20226 988 1004 403 A C
ATOM 1346 CG LEU A 186 40.195 29.995 467.204 1.00 85.85 A C
ANISOU 1346 CG LEU A 186 7174 7482 17961 1137 1455 392 A C
ATOM 1347 CD1 LEU A 186 38.913 30.167 466.385 1.00 69.53 A C
ANISOU 1347 CD1 LEU A 186 5452 5513 15453 1148 1672 358 A C
ATOM 1348 CD2 LEU A 186 41.428 30.307 466.356 1.00 77.95 A C
ANISOU 1348 CD2 LEU A 186 5898 6388 17333 1156 1820 473 A C
ATOM 1349 N PHE A 187 40.624 30.828 471.947 1.00102.47 A N
ANISOU 1349 N PHE A 187 9001 9477 20455 850 -196 353 A N
ATOM 1350 CA PHE A 187 40.331 31.416 473.248 1.00 89.67 A C
ANISOU 1350 CA PHE A 187 7428 7840 18801 743 -659 323 A C
ATOM 1351 C PHE A 187 40.896 30.488 474.330 1.00 92.36 A C
ANISOU 1351 C PHE A 187 7736 8119 19236 806 -1036 310 A C
ATOM 1352 O PHE A 187 41.173 29.307 474.077 1.00 97.26 A O
ANISOU 1352 O PHE A 187 8368 8740 19848 939 -938 315 A O
ATOM 1353 CB PHE A 187 38.822 31.608 473.440 1.00 76.77 A C
ANISOU 1353 CB PHE A 187 6136 6331 16700 716 -719 273 A C
ATOM 1354 CG PHE A 187 38.324 32.970 473.044 1.00 89.00 A C
ANISOU 1354 CG PHE A 187 7688 7901 18226 599 -596 282 A C
ATOM 1355 CD1 PHE A 187 38.853 34.125 473.624 1.00 98.79 A C
ANISOU 1355 CD1 PHE A 187 8747 9039 19749 473 -812 293 A C
ATOM 1356 CD2 PHE A 187 37.289 33.099 472.119 1.00 91.20 A C
ANISOU 1356 CD2 PHE A 187 8177 8283 18192 619 -288 277 A C
ATOM 1357 CE1 PHE A 187 38.378 35.389 473.261 1.00 91.05 A C
ANISOU 1357 CE1 PHE A 187 7779 8060 18757 372 -700 304 A C
ATOM 1358 CE2 PHE A 187 36.804 34.358 471.755 1.00 86.33 A C
ANISOU 1358 CE2 PHE A 187 7570 7677 17553 521 -180 294 A C
ATOM 1359 CZ PHE A 187 37.351 35.501 472.327 1.00 84.54 A C
ANISOU 1359 CZ PHE A 187 7146 7349 17626 399 -380 311 A C
ATOM 1360 N THR A 188 41.108 31.034 475.532 1.00 90.43 A N
ANISOU 1360 N THR A 188 7462 7806 19090 716 -1475 293 A N
ATOM 1361 CA THR A 188 41.551 30.227 476.671 1.00 98.11 A C
ANISOU 1361 CA THR A 188 8454 8716 20106 770 -1883 285 A C
ATOM 1362 C THR A 188 40.365 29.535 477.357 1.00 99.79 A C
ANISOU 1362 C THR A 188 9046 9028 19842 818 -2075 248 A C
ATOM 1363 O THR A 188 39.228 30.020 477.314 1.00 96.89 A O
ANISOU 1363 O THR A 188 8908 8756 19151 767 -2025 216 A O
ATOM 1364 CB THR A 188 42.307 31.098 477.675 1.00 92.34 A C
ANISOU 1364 CB THR A 188 7570 7849 19664 660 -2289 279 A C
ATOM 1365 CG2 THR A 188 42.916 30.234 478.793 1.00 89.18 A C
ANISOU 1365 CG2 THR A 188 7178 7366 19342 726 -2710 283 A C
ATOM 1366 OG1 THR A 188 43.383 31.764 477.003 1.00 95.28 A O
ANISOU 1366 OG1 THR A 188 7597 8111 20491 612 -2087 326 A O
ATOM 1367 N SER A 189 40.639 28.383 477.989 1.00 90.38 A N
ANISOU 1367 N SER A 189 7922 7799 18619 920 -2287 262 A N
ATOM 1368 CA SER A 189 39.598 27.591 478.651 1.00 89.05 A C
ANISOU 1368 CA SER A 189 8122 7696 18018 973 -2452 250 A C
ATOM 1369 C SER A 189 39.084 28.250 479.929 1.00 87.05 A C
ANISOU 1369 C SER A 189 8068 7435 17571 880 -2870 223 A C
ATOM 1370 O SER A 189 39.859 28.500 480.860 1.00 90.53 A O
ANISOU 1370 O SER A 189 8417 7769 18210 846 -3244 224 A O
ATOM 1371 CB SER A 189 40.119 26.199 478.986 1.00 94.58 A C
ANISOU 1371 CB SER A 189 8836 8332 18768 1109 -2566 288 A C
ATOM 1372 OG SER A 189 39.141 25.480 479.718 1.00 83.58 A O
ANISOU 1372 OG SER A 189 7810 6976 16969 1146 -2743 294 A O
ATOM 1373 N MET A 190 37.759 28.446 479.996 1.00 81.05 A N
ANISOU 1373 N MET A 190 7613 6778 16406 852 -2813 197 A N
ATOM 1374 CA MET A 190 37.058 29.066 481.119 1.00 76.67 A C
ANISOU 1374 CA MET A 190 7309 6228 15595 780 -3147 165 A C
ATOM 1375 C MET A 190 36.359 28.068 482.037 1.00 62.73 A C
ANISOU 1375 C MET A 190 5902 4470 13463 846 -3356 194 A C
ATOM 1376 O MET A 190 35.664 28.489 482.961 1.00 61.94 A O
ANISOU 1376 O MET A 190 6068 4377 13091 801 -3598 175 A O
ATOM 1377 CB MET A 190 36.009 30.065 480.605 1.00 74.25 A C
ANISOU 1377 CB MET A 190 7105 6016 15091 703 -2930 122 A C
ATOM 1378 CG MET A 190 36.558 31.334 479.991 1.00 79.16 A C
ANISOU 1378 CG MET A 190 7437 6610 16032 608 -2807 98 A C
ATOM 1379 SD MET A 190 37.543 32.262 481.174 1.00 89.38 A S
ANISOU 1379 SD MET A 190 8597 7748 17616 516 -3298 63 A S
ATOM 1380 CE MET A 190 36.360 32.443 482.505 1.00 83.40 A C
ANISOU 1380 CE MET A 190 8286 7021 16382 507 -3656 13 A C
ATOM 1381 N LEU A 191 36.507 26.769 481.803 1.00 63.40 A N
ANISOU 1381 N LEU A 191 6020 4543 13527 953 -3257 244 A N
ATOM 1382 CA LEU A 191 35.786 25.771 482.585 1.00 63.02 A C
ANISOU 1382 CA LEU A 191 6326 4488 13130 1009 -3406 291 A C
ATOM 1383 C LEU A 191 36.130 25.846 484.074 1.00 74.67 A C
ANISOU 1383 C LEU A 191 7947 5879 14546 993 -3903 311 A C
ATOM 1384 O LEU A 191 37.302 25.943 484.453 1.00 75.09 A O
ANISOU 1384 O LEU A 191 7782 5839 14909 999 -4149 313 A O
ATOM 1385 CB LEU A 191 36.086 24.378 482.033 1.00 69.78 A C
ANISOU 1385 CB LEU A 191 7150 5313 14050 1130 -3226 338 A C
ATOM 1386 CG LEU A 191 35.407 23.156 482.660 1.00 70.84 A C
ANISOU 1386 CG LEU A 191 7629 5417 13870 1194 -3318 403 A C
ATOM 1387 CD1 LEU A 191 33.929 23.400 482.923 1.00 71.34 A C
ANISOU 1387 CD1 LEU A 191 8044 5553 13510 1121 -3254 401 A C
ATOM 1388 CD2 LEU A 191 35.585 21.989 481.719 1.00 64.17 A C
ANISOU 1388 CD2 LEU A 191 6723 4546 13111 1304 -3029 420 A C
ATOM 1389 N ASN A 192 35.087 25.798 484.911 1.00 76.20 A N
ANISOU 1389 N ASN A 192 8531 6094 14327 972 -4043 329 A N
ATOM 1390 CA ASN A 192 35.104 25.798 486.381 1.00 66.26 A C
ANISOU 1390 CA ASN A 192 7549 4764 12862 963 -4490 355 A C
ATOM 1391 C ASN A 192 35.470 27.123 487.027 1.00 78.48 A C
ANISOU 1391 C ASN A 192 9058 6274 14485 876 -4792 278 A C
ATOM 1392 O ASN A 192 35.740 27.151 488.236 1.00 69.96 A O
ANISOU 1392 O ASN A 192 8187 5116 13277 872 -5201 286 A O
ATOM 1393 CB ASN A 192 36.013 24.723 486.968 1.00 71.73 A C
ANISOU 1393 CB ASN A 192 8226 5354 13676 1048 -4740 428 A C
ATOM 1394 CG ASN A 192 35.243 23.496 487.370 1.00 85.93 A C
ANISOU 1394 CG ASN A 192 10375 7144 15130 1113 -4707 524 A C
ATOM 1395 ND2 ASN A 192 34.527 23.589 488.486 1.00 95.43 A N
ANISOU 1395 ND2 ASN A 192 11984 8335 15939 1081 -4935 559 A N
ATOM 1396 OD1 ASN A 192 35.255 22.487 486.669 1.00 93.35 A O
ANISOU 1396 OD1 ASN A 192 11243 8081 16146 1187 -4462 567 A O
ATOM 1397 N HIS A 193 35.469 28.219 486.280 1.00 72.45 A N
ANISOU 1397 N HIS A 193 8065 5554 13908 804 -4609 202 A N
ATOM 1398 CA HIS A 193 35.656 29.525 486.877 1.00 66.77 A C
ANISOU 1398 CA HIS A 193 7349 4787 13234 716 -4880 120 A C
ATOM 1399 C HIS A 193 34.341 29.990 487.496 1.00 64.75 A C
ANISOU 1399 C HIS A 193 7510 4580 12514 695 -4926 96 A C
ATOM 1400 O HIS A 193 33.262 29.691 486.978 1.00 70.30 A O
ANISOU 1400 O HIS A 193 8362 5370 12980 713 -4603 124 A O
ATOM 1401 CB HIS A 193 36.156 30.497 485.813 1.00 66.10 A C
ANISOU 1401 CB HIS A 193 6864 4712 13540 646 -4642 64 A C
ATOM 1402 CG HIS A 193 35.697 31.908 486.009 1.00 85.83 A C
ANISOU 1402 CG HIS A 193 9424 7208 15979 555 -4719 -23 A C
ATOM 1403 CD2 HIS A 193 34.581 32.548 485.580 1.00 78.88 A C
ANISOU 1403 CD2 HIS A 193 8668 6416 14888 529 -4483 -56 A C
ATOM 1404 ND1 HIS A 193 36.435 32.843 486.706 1.00 81.60 A N
ANISOU 1404 ND1 HIS A 193 8827 6551 15625 482 -5067 -91 A N
ATOM 1405 CE1 HIS A 193 35.787 33.994 486.704 1.00 92.87 A C
ANISOU 1405 CE1 HIS A 193 10338 7997 16950 417 -5050 -167 A C
ATOM 1406 NE2 HIS A 193 34.656 33.840 486.033 1.00 84.56 A N
ANISOU 1406 NE2 HIS A 193 9390 7071 15667 450 -4704 -144 A N
ATOM 1407 N HIS A 194 34.430 30.622 488.666 1.00 68.46 A N
ANISOU 1407 N HIS A 194 8207 4978 12826 661 -5332 46 A N
ATOM 1408 CA HIS A 194 33.289 31.220 489.351 1.00 65.52 A C
ANISOU 1408 CA HIS A 194 8246 4633 12016 647 -5409 10 A C
ATOM 1409 C HIS A 194 33.328 32.745 489.227 1.00 65.20 A C
ANISOU 1409 C HIS A 194 8079 4577 12118 566 -5474 -113 A C
ATOM 1410 O HIS A 194 34.402 33.351 489.254 1.00 67.45 A O
ANISOU 1410 O HIS A 194 8094 4781 12753 503 -5660 -176 A O
ATOM 1411 CB HIS A 194 33.273 30.868 490.843 1.00 74.91 A C
ANISOU 1411 CB HIS A 194 9871 5760 12830 672 -5821 31 A C
ATOM 1412 CG HIS A 194 33.236 29.403 491.147 1.00 93.27 A C
ANISOU 1412 CG HIS A 194 12367 8080 14991 747 -5809 162 A C
ATOM 1413 CD2 HIS A 194 32.233 28.610 491.593 1.00 99.73 A C
ANISOU 1413 CD2 HIS A 194 13593 8929 15371 789 -5710 259 A C
ATOM 1414 ND1 HIS A 194 34.348 28.591 491.043 1.00102.94 A N
ANISOU 1414 ND1 HIS A 194 13341 9243 16530 783 -5908 210 A N
ATOM 1415 CE1 HIS A 194 34.027 27.359 491.397 1.00103.07 A C
ANISOU 1415 CE1 HIS A 194 13596 9257 16308 851 -5885 326 A C
ATOM 1416 NE2 HIS A 194 32.752 27.345 491.741 1.00103.84 A N
ANISOU 1416 NE2 HIS A 194 14096 9409 15950 847 -5761 362 A N
ATOM 1417 N PHE A 195 32.149 33.370 489.137 1.00 63.36 A N
ANISOU 1417 N PHE A 195 8079 4451 11543 500 -5191 -182 A N
ATOM 1418 CA PHE A 195 32.020 34.828 489.215 1.00 62.62 A C
ANISOU 1418 CA PHE A 195 7973 4365 11455 391 -5208 -328 A C
ATOM 1419 C PHE A 195 31.063 35.226 490.336 1.00 63.02 A C
ANISOU 1419 C PHE A 195 8541 4460 10945 356 -5281 -414 A C
ATOM 1420 O PHE A 195 30.119 34.486 490.646 1.00 92.30 A O
ANISOU 1420 O PHE A 195 12574 8250 14247 390 -5096 -354 A O
ATOM 1421 CB PHE A 195 31.540 35.461 487.894 1.00 73.77 A C
ANISOU 1421 CB PHE A 195 9131 5862 13035 333 -4731 -355 A C
ATOM 1422 CG PHE A 195 30.125 35.064 487.461 1.00 70.06 A C
ANISOU 1422 CG PHE A 195 8888 5539 12193 336 -4284 -327 A C
ATOM 1423 CD1 PHE A 195 29.020 35.812 487.860 1.00 55.11 A C
ANISOU 1423 CD1 PHE A 195 7292 3722 9927 277 -4145 -419 A C
ATOM 1424 CD2 PHE A 195 29.921 33.972 486.611 1.00 64.79 A C
ANISOU 1424 CD2 PHE A 195 8113 4919 11586 398 -4005 -216 A C
ATOM 1425 CE1 PHE A 195 27.750 35.459 487.455 1.00 63.16 A C
ANISOU 1425 CE1 PHE A 195 8468 4867 10664 276 -3754 -388 A C
ATOM 1426 CE2 PHE A 195 28.648 33.612 486.192 1.00 61.49 A C
ANISOU 1426 CE2 PHE A 195 7876 4621 10867 387 -3632 -193 A C
ATOM 1427 CZ PHE A 195 27.558 34.355 486.611 1.00 68.25 A C
ANISOU 1427 CZ PHE A 195 8995 5556 11379 323 -3509 -273 A C
ATOM 1428 N PRO A 196 31.280 36.381 490.959 1.00 64.80 A N
ANISOU 1428 N PRO A 196 8856 4623 11141 286 -5536 -557 A N
ATOM 1429 CA PRO A 196 30.398 36.828 492.044 1.00 70.34 A C
ANISOU 1429 CA PRO A 196 10070 5356 11299 265 -5587 -660 A C
ATOM 1430 C PRO A 196 29.093 37.432 491.537 1.00 70.90 A C
ANISOU 1430 C PRO A 196 10238 5552 11147 221 -5094 -722 A C
ATOM 1431 O PRO A 196 29.004 37.980 490.435 1.00 62.85 A O
ANISOU 1431 O PRO A 196 8894 4565 10421 178 -4811 -735 A O
ATOM 1432 CB PRO A 196 31.238 37.891 492.754 1.00 72.89 A C
ANISOU 1432 CB PRO A 196 10402 5539 11754 207 -6056 -807 A C
ATOM 1433 CG PRO A 196 32.052 38.478 491.650 1.00 74.76 A C
ANISOU 1433 CG PRO A 196 10082 5725 12597 154 -5986 -805 A C
ATOM 1434 CD PRO A 196 32.385 37.325 490.728 1.00 66.58 A C
ANISOU 1434 CD PRO A 196 8721 4728 11848 222 -5796 -634 A C
ATOM 1435 N ALA A 197 28.083 37.380 492.410 1.00 74.13 A N
ANISOU 1435 N ALA A 197 11116 6022 11029 237 -5006 -760 A N
ATOM 1436 CA ALA A 197 26.754 37.861 492.043 1.00 60.27 A C
ANISOU 1436 CA ALA A 197 9469 4384 9049 211 -4541 -810 A C
ATOM 1437 C ALA A 197 26.773 39.312 491.596 1.00 59.75 A C
ANISOU 1437 C ALA A 197 9228 4280 9195 144 -4483 -960 A C
ATOM 1438 O ALA A 197 25.932 39.717 490.788 1.00 57.10 A O
ANISOU 1438 O ALA A 197 8779 4029 8888 125 -4086 -969 A O
ATOM 1439 CB ALA A 197 25.785 37.686 493.212 1.00 61.61 A C
ANISOU 1439 CB ALA A 197 10174 4600 8636 241 -4484 -841 A C
ATOM 1440 N SER A 198 27.722 40.106 492.105 1.00 87.31 A N
ANISOU 1440 N SER A 198 12693 7630 12849 106 -4893 -1075 A N
ATOM 1441 CA SER A 198 27.821 41.518 491.749 1.00 75.93 A C
ANISOU 1441 CA SER A 198 11099 6117 11634 32 -4877 -1219 A C
ATOM 1442 C SER A 198 28.053 41.739 490.258 1.00 77.51 A C
ANISOU 1442 C SER A 198 10803 6340 12307 -7 -4601 -1140 A C
ATOM 1443 O SER A 198 27.744 42.824 489.749 1.00 81.36 A O
ANISOU 1443 O SER A 198 11170 6851 12893 -44 -4388 -1195 A O
ATOM 1444 CB SER A 198 28.958 42.151 492.539 1.00 66.22 A C
ANISOU 1444 CB SER A 198 9862 4776 10524 20 -5335 -1284 A C
ATOM 1445 OG SER A 198 30.216 41.782 491.996 1.00 66.91 A O
ANISOU 1445 OG SER A 198 9518 4810 11095 19 -5519 -1165 A O
ATOM 1446 N ASP A 199 28.571 40.727 489.552 1.00 75.02 A N
ANISOU 1446 N ASP A 199 10205 6063 12238 24 -4546 -981 A N
ATOM 1447 CA ASP A 199 28.987 40.846 488.157 1.00 56.89 A C
ANISOU 1447 CA ASP A 199 7449 3773 10395 -4 -4312 -898 A C
ATOM 1448 C ASP A 199 27.827 40.819 487.183 1.00 60.19 A C
ANISOU 1448 C ASP A 199 7849 4329 10692 6 -3808 -850 A C
ATOM 1449 O ASP A 199 28.011 41.182 486.013 1.00 52.01 A O
ANISOU 1449 O ASP A 199 6495 3296 9969 -24 -3585 -803 A O
ATOM 1450 CB ASP A 199 29.998 39.751 487.812 1.00 65.53 A C
ANISOU 1450 CB ASP A 199 8270 4842 11787 45 -4438 -761 A C
ATOM 1451 CG ASP A 199 31.413 40.105 488.264 1.00 73.64 A C
ANISOU 1451 CG ASP A 199 9084 5717 13178 17 -4892 -789 A C
ATOM 1452 OD1 ASP A 199 31.607 41.180 488.897 1.00 78.22 A O
ANISOU 1452 OD1 ASP A 199 9758 6265 13695 -9 -5056 -880 A O
ATOM 1453 OD2 ASP A 199 32.335 39.311 487.980 1.00 74.74 A O1-
ANISOU 1453 OD2 ASP A 199 8952 5803 13645 56 -5025 -690 A O1-
ATOM 1454 N ILE A 200 26.679 40.307 487.605 1.00 67.78 A N
ANISOU 1454 N ILE A 200 9131 5400 11223 50 -3628 -843 A N
ATOM 1455 CA ILE A 200 25.420 40.472 486.893 1.00 60.26 A C
ANISOU 1455 CA ILE A 200 8207 4566 10123 52 -3200 -828 A C
ATOM 1456 C ILE A 200 24.402 41.065 487.861 1.00 56.57 A C
ANISOU 1456 C ILE A 200 8115 4121 9258 59 -3161 -948 A C
ATOM 1457 O ILE A 200 23.878 40.372 488.735 1.00 57.57 A O
ANISOU 1457 O ILE A 200 8552 4297 9026 99 -3175 -935 A O
ATOM 1458 CB ILE A 200 24.921 39.151 486.279 1.00 47.57 A C
ANISOU 1458 CB ILE A 200 6565 3073 8436 98 -2952 -686 A C
ATOM 1459 CG1 ILE A 200 26.069 38.417 485.598 1.00 47.75 A C
ANISOU 1459 CG1 ILE A 200 6280 3049 8814 118 -3044 -584 A C
ATOM 1460 CG2 ILE A 200 23.870 39.422 485.239 1.00 44.92 A C
ANISOU 1460 CG2 ILE A 200 6143 2838 8086 86 -2555 -663 A C
ATOM 1461 CD1 ILE A 200 25.657 37.101 484.988 1.00 56.42 A C
ANISOU 1461 CD1 ILE A 200 7359 4229 9847 166 -2823 -461 A C
ATOM 1462 N PRO A 201 24.129 42.364 487.761 1.00 59.13 A N
ANISOU 1462 N PRO A 201 8431 4396 9639 25 -3106 -1066 A N
ATOM 1463 CA PRO A 201 23.211 42.998 488.711 1.00 59.61 A C
ANISOU 1463 CA PRO A 201 8852 4459 9340 47 -3060 -1201 A C
ATOM 1464 C PRO A 201 21.812 42.422 488.591 1.00 51.65 A C
ANISOU 1464 C PRO A 201 7981 3601 8045 94 -2680 -1140 A C
ATOM 1465 O PRO A 201 21.443 41.819 487.583 1.00 52.55 A O
ANISOU 1465 O PRO A 201 7883 3808 8276 94 -2437 -1015 A O
ATOM 1466 CB PRO A 201 23.238 44.475 488.305 1.00 62.33 A C
ANISOU 1466 CB PRO A 201 9073 4706 9904 5 -3033 -1316 A C
ATOM 1467 CG PRO A 201 24.506 44.629 487.536 1.00 64.35 A C
ANISOU 1467 CG PRO A 201 8942 4917 10592 -51 -3176 -1237 A C
ATOM 1468 CD PRO A 201 24.720 43.336 486.828 1.00 49.97 A C
ANISOU 1468 CD PRO A 201 6944 3154 8888 -34 -3092 -1081 A C
ATOM 1469 N ALA A 202 21.032 42.597 489.658 1.00 54.21 A N
ANISOU 1469 N ALA A 202 8671 3940 7987 133 -2633 -1232 A N
ATOM 1470 CA ALA A 202 19.702 42.008 489.677 1.00 49.97 A C
ANISOU 1470 CA ALA A 202 8261 3537 7190 171 -2273 -1167 A C
ATOM 1471 C ALA A 202 18.916 42.448 488.457 1.00 47.41 A C
ANISOU 1471 C ALA A 202 7661 3278 7076 164 -1949 -1133 A C
ATOM 1472 O ALA A 202 18.197 41.653 487.848 1.00 62.65 A O
ANISOU 1472 O ALA A 202 9489 5318 8995 167 -1703 -1013 A O
ATOM 1473 CB ALA A 202 18.978 42.383 490.967 1.00 52.36 A C
ANISOU 1473 CB ALA A 202 8984 3830 7080 219 -2223 -1290 A C
ATOM 1474 N GLN A 203 19.075 43.708 488.066 1.00 68.36 A N
ANISOU 1474 N GLN A 203 10191 5847 9933 153 -1970 -1233 A N
ATOM 1475 CA GLN A 203 18.351 44.241 486.923 1.00 45.38 A C
ANISOU 1475 CA GLN A 203 7044 2981 7218 155 -1695 -1198 A C
ATOM 1476 C GLN A 203 18.718 43.512 485.633 1.00 48.90 A C
ANISOU 1476 C GLN A 203 7176 3487 7917 119 -1634 -1038 A C
ATOM 1477 O GLN A 203 17.861 43.300 484.771 1.00 56.71 A O
ANISOU 1477 O GLN A 203 8038 4568 8943 129 -1378 -959 A O
ATOM 1478 CB GLN A 203 18.624 45.736 486.832 1.00 67.22 A C
ANISOU 1478 CB GLN A 203 9766 5612 10164 146 -1776 -1328 A C
ATOM 1479 CG GLN A 203 17.515 46.511 486.180 1.00 85.95 A C
ANISOU 1479 CG GLN A 203 12051 8009 12598 186 -1485 -1341 A C
ATOM 1480 CD GLN A 203 17.777 47.995 486.209 1.00 96.74 A C
ANISOU 1480 CD GLN A 203 13416 9213 14129 183 -1576 -1475 A C
ATOM 1481 NE2 GLN A 203 18.746 48.408 487.027 1.00101.37 A N
ANISOU 1481 NE2 GLN A 203 14139 9664 14713 147 -1884 -1594 A N
ATOM 1482 OE1 GLN A 203 17.101 48.769 485.528 1.00 97.58 A O
ANISOU 1482 OE1 GLN A 203 13408 9301 14366 212 -1390 -1473 A O
ATOM 1483 N ALA A 204 19.979 43.098 485.491 1.00 51.79 A N
ANISOU 1483 N ALA A 204 7421 3797 8460 84 -1870 -991 A N
ATOM 1484 CA ALA A 204 20.409 42.396 484.285 1.00 41.64 A C
ANISOU 1484 CA ALA A 204 5857 2555 7408 64 -1796 -852 A C
ATOM 1485 C ALA A 204 19.955 40.945 484.282 1.00 40.72 A C
ANISOU 1485 C ALA A 204 5806 2547 7120 85 -1691 -745 A C
ATOM 1486 O ALA A 204 19.589 40.412 483.233 1.00 40.24 A O
ANISOU 1486 O ALA A 204 5589 2557 7143 83 -1501 -650 A O
ATOM 1487 CB ALA A 204 21.928 42.462 484.134 1.00 42.67 A C
ANISOU 1487 CB ALA A 204 5805 2578 7829 29 -2057 -839 A C
ATOM 1488 N ARG A 205 20.030 40.267 485.421 1.00 42.66 A N
ANISOU 1488 N ARG A 205 6293 2790 7127 102 -1830 -755 A N
ATOM 1489 CA ARG A 205 19.448 38.934 485.503 1.00 41.54 A C
ANISOU 1489 CA ARG A 205 6244 2733 6805 115 -1708 -648 A C
ATOM 1490 C ARG A 205 17.952 38.966 485.223 1.00 40.37 A C
ANISOU 1490 C ARG A 205 6133 2687 6518 116 -1384 -635 A C
ATOM 1491 O ARG A 205 17.419 38.074 484.553 1.00 50.52 A O
ANISOU 1491 O ARG A 205 7334 4042 7818 103 -1221 -535 A O
ATOM 1492 CB ARG A 205 19.759 38.335 486.880 1.00 43.74 A C
ANISOU 1492 CB ARG A 205 6819 2976 6823 135 -1917 -654 A C
ATOM 1493 CG ARG A 205 21.251 38.035 487.067 1.00 45.01 A C
ANISOU 1493 CG ARG A 205 6902 3037 7164 140 -2266 -636 A C
ATOM 1494 CD ARG A 205 21.608 37.275 488.343 1.00 67.04 A C
ANISOU 1494 CD ARG A 205 9989 5784 9697 168 -2511 -611 A C
ATOM 1495 NE ARG A 205 21.508 38.077 489.560 1.00 77.81 A N
ANISOU 1495 NE ARG A 205 11662 7102 10799 176 -2664 -740 A N
ATOM 1496 CZ ARG A 205 20.407 38.225 490.290 1.00 70.32 A C
ANISOU 1496 CZ ARG A 205 11014 6209 9494 190 -2470 -781 A C
ATOM 1497 NH1 ARG A 205 19.269 37.628 489.938 1.00 74.65 A N1+
ANISOU 1497 NH1 ARG A 205 11566 6863 9934 187 -2120 -695 A N1+
ATOM 1498 NH2 ARG A 205 20.444 38.972 491.383 1.00 52.82 A N
ANISOU 1498 NH2 ARG A 205 9099 3934 7037 208 -2625 -914 A N
ATOM 1499 N ALA A 206 17.278 40.029 485.644 1.00 41.02 A N
ANISOU 1499 N ALA A 206 6314 2766 6505 132 -1294 -740 A N
ATOM 1500 CA ALA A 206 15.838 40.129 485.438 1.00 44.13 A C
ANISOU 1500 CA ALA A 206 6714 3248 6804 144 -991 -730 A C
ATOM 1501 C ALA A 206 15.460 40.289 483.967 1.00 42.88 A C
ANISOU 1501 C ALA A 206 6269 3135 6890 128 -842 -669 A C
ATOM 1502 O ALA A 206 14.331 39.955 483.590 1.00 37.48 A O
ANISOU 1502 O ALA A 206 5539 2532 6170 125 -624 -618 A O
ATOM 1503 CB ALA A 206 15.281 41.292 486.256 1.00 48.43 A C
ANISOU 1503 CB ALA A 206 7431 3759 7213 186 -931 -870 A C
ATOM 1504 N MET A 207 16.362 40.814 483.126 1.00 47.46 A N
ANISOU 1504 N MET A 207 6659 3657 7718 116 -954 -669 A N
ATOM 1505 CA MET A 207 16.003 41.026 481.724 1.00 41.79 A C
ANISOU 1505 CA MET A 207 5716 2975 7189 107 -812 -607 A C
ATOM 1506 C MET A 207 15.691 39.717 481.030 1.00 34.63 A C
ANISOU 1506 C MET A 207 4744 2146 6268 86 -721 -495 A C
ATOM 1507 O MET A 207 14.865 39.693 480.119 1.00 50.20 A O
ANISOU 1507 O MET A 207 6609 4175 8288 81 -570 -449 A O
ATOM 1508 CB MET A 207 17.114 41.740 480.951 1.00 41.45 A C
ANISOU 1508 CB MET A 207 5497 2847 7403 92 -923 -607 A C
ATOM 1509 CG MET A 207 17.403 43.189 481.325 1.00 63.46 A C
ANISOU 1509 CG MET A 207 8302 5531 10279 98 -1007 -712 A C
ATOM 1510 SD MET A 207 16.100 44.409 481.031 1.00 60.06 A S
ANISOU 1510 SD MET A 207 7867 5103 9850 139 -814 -761 A S
ATOM 1511 CE MET A 207 15.247 44.455 482.627 1.00 56.90 A C
ANISOU 1511 CE MET A 207 7748 4719 9152 186 -777 -884 A C
ATOM 1512 N TYR A 208 16.325 38.615 481.448 1.00 46.20 A N
ANISOU 1512 N TYR A 208 6282 3601 7671 75 -829 -451 A N
ATOM 1513 CA TYR A 208 16.060 37.323 480.807 1.00 34.06 A C
ANISOU 1513 CA TYR A 208 4702 2112 6129 55 -751 -354 A C
ATOM 1514 C TYR A 208 14.599 36.907 480.936 1.00 33.92 A C
ANISOU 1514 C TYR A 208 4745 2173 5970 32 -565 -326 A C
ATOM 1515 O TYR A 208 14.058 36.253 480.041 1.00 37.04 A O
ANISOU 1515 O TYR A 208 5050 2609 6415 5 -470 -264 A O
ATOM 1516 CB TYR A 208 16.986 36.251 481.383 1.00 34.82 A C
ANISOU 1516 CB TYR A 208 4885 2160 6188 60 -911 -313 A C
ATOM 1517 CG TYR A 208 18.419 36.433 480.964 1.00 38.16 A C
ANISOU 1517 CG TYR A 208 5167 2506 6827 81 -1072 -316 A C
ATOM 1518 CD1 TYR A 208 18.810 36.197 479.646 1.00 36.50 A C
ANISOU 1518 CD1 TYR A 208 4769 2293 6805 86 -997 -270 A C
ATOM 1519 CD2 TYR A 208 19.377 36.860 481.868 1.00 36.47 A C
ANISOU 1519 CD2 TYR A 208 5005 2215 6637 96 -1294 -367 A C
ATOM 1520 CE1 TYR A 208 20.122 36.379 479.246 1.00 34.45 A C
ANISOU 1520 CE1 TYR A 208 4356 1961 6773 107 -1099 -265 A C
ATOM 1521 CE2 TYR A 208 20.684 37.044 481.481 1.00 36.94 A C
ANISOU 1521 CE2 TYR A 208 4890 2196 6947 108 -1438 -364 A C
ATOM 1522 CZ TYR A 208 21.056 36.799 480.172 1.00 45.91 A C
ANISOU 1522 CZ TYR A 208 5819 3336 8290 115 -1320 -308 A C
ATOM 1523 OH TYR A 208 22.372 36.974 479.795 1.00 44.15 A O
ANISOU 1523 OH TYR A 208 5400 3032 8341 129 -1425 -296 A O
ATOM 1524 N SER A 209 13.937 37.293 482.020 1.00 35.07 A N
ANISOU 1524 N SER A 209 5041 2334 5950 42 -506 -373 A N
ATOM 1525 CA SER A 209 12.523 37.001 482.149 1.00 35.28 A C
ANISOU 1525 CA SER A 209 5085 2432 5889 21 -297 -342 A C
ATOM 1526 C SER A 209 11.668 37.813 481.176 1.00 38.14 A C
ANISOU 1526 C SER A 209 5257 2833 6400 31 -173 -356 A C
ATOM 1527 O SER A 209 10.594 37.343 480.780 1.00 37.25 A O
ANISOU 1527 O SER A 209 5066 2778 6310 -2 -37 -303 A O
ATOM 1528 CB SER A 209 12.095 37.235 483.593 1.00 37.13 A C
ANISOU 1528 CB SER A 209 5544 2666 5899 43 -232 -390 A C
ATOM 1529 OG SER A 209 12.661 36.243 484.429 1.00 38.10 A O
ANISOU 1529 OG SER A 209 5861 2757 5857 26 -335 -340 A O
ATOM 1530 N ILE A 210 12.146 38.976 480.719 1.00 34.08 A N
ANISOU 1530 N ILE A 210 4660 2280 6010 69 -237 -415 A N
ATOM 1531 CA ILE A 210 11.411 39.740 479.708 1.00 33.44 A C
ANISOU 1531 CA ILE A 210 4410 2222 6074 87 -149 -409 A C
ATOM 1532 C ILE A 210 11.708 39.209 478.310 1.00 35.41 A C
ANISOU 1532 C ILE A 210 4526 2485 6443 56 -190 -331 A C
ATOM 1533 O ILE A 210 10.801 38.975 477.508 1.00 49.85 A O
ANISOU 1533 O ILE A 210 6258 4363 8321 40 -118 -284 A O
ATOM 1534 CB ILE A 210 11.727 41.248 479.821 1.00 33.90 A C
ANISOU 1534 CB ILE A 210 4456 2211 6212 141 -187 -495 A C
ATOM 1535 CG1 ILE A 210 11.147 41.851 481.099 1.00 35.49 A C
ANISOU 1535 CG1 ILE A 210 4803 2398 6283 186 -105 -591 A C
ATOM 1536 CG2 ILE A 210 11.148 41.994 478.656 1.00 43.49 A C
ANISOU 1536 CG2 ILE A 210 5505 3432 7589 164 -130 -464 A C
ATOM 1537 CD1 ILE A 210 12.166 42.181 482.103 1.00 36.51 A C
ANISOU 1537 CD1 ILE A 210 5108 2449 6315 196 -253 -679 A C
ATOM 1538 N ASN A 211 12.961 39.003 477.997 1.00 31.70 A N
ANISOU 1538 N ASN A 211 4054 1968 6024 52 -307 -320 A N
ATOM 1539 CA ASN A 211 13.351 38.404 476.727 1.00 30.80 A C
ANISOU 1539 CA ASN A 211 3852 1858 5993 34 -320 -255 A C
ATOM 1540 C ASN A 211 14.475 37.408 477.000 1.00 30.87 A C
ANISOU 1540 C ASN A 211 3913 1828 5989 26 -414 -238 A C
ATOM 1541 O ASN A 211 15.518 37.764 477.553 1.00 49.54 A O
ANISOU 1541 O ASN A 211 6293 4133 8399 44 -519 -270 A O
ATOM 1542 CB ASN A 211 13.768 39.481 475.720 1.00 30.49 A C
ANISOU 1542 CB ASN A 211 3708 1784 6095 60 -322 -248 A C
ATOM 1543 CG ASN A 211 14.052 38.915 474.332 1.00 29.90 A C
ANISOU 1543 CG ASN A 211 3578 1718 6065 52 -299 -181 A C
ATOM 1544 ND2 ASN A 211 13.885 39.742 473.302 1.00 29.81 A N
ANISOU 1544 ND2 ASN A 211 3504 1700 6123 70 -261 -149 A N
ATOM 1545 OD1 ASN A 211 14.425 37.755 474.189 1.00 29.74 A O
ANISOU 1545 OD1 ASN A 211 3592 1701 6007 36 -314 -160 A O
ATOM 1546 N PRO A 212 14.284 36.138 476.660 1.00 34.37 A N
ANISOU 1546 N PRO A 212 4382 2289 6388 -1 -395 -189 A N
ATOM 1547 CA PRO A 212 15.278 35.123 477.030 1.00 38.98 A C
ANISOU 1547 CA PRO A 212 5024 2821 6966 5 -486 -169 A C
ATOM 1548 C PRO A 212 16.608 35.256 476.315 1.00 39.27 A C
ANISOU 1548 C PRO A 212 4964 2800 7158 43 -539 -165 A C
ATOM 1549 O PRO A 212 17.577 34.615 476.744 1.00 40.07 A O
ANISOU 1549 O PRO A 212 5083 2843 7299 66 -637 -155 A O
ATOM 1550 CB PRO A 212 14.586 33.806 476.659 1.00 38.53 A C
ANISOU 1550 CB PRO A 212 5013 2782 6846 -35 -433 -122 A C
ATOM 1551 CG PRO A 212 13.496 34.190 475.711 1.00 30.29 A C
ANISOU 1551 CG PRO A 212 3893 1796 5819 -61 -339 -118 A C
ATOM 1552 CD PRO A 212 13.062 35.552 476.096 1.00 30.36 A C
ANISOU 1552 CD PRO A 212 3860 1836 5839 -41 -307 -155 A C
ATOM 1553 N ILE A 213 16.703 36.062 475.263 1.00 33.83 A N
ANISOU 1553 N ILE A 213 4170 2116 6567 55 -473 -162 A N
ATOM 1554 CA ILE A 213 17.931 36.178 474.488 1.00 40.75 A C
ANISOU 1554 CA ILE A 213 4944 2936 7602 88 -468 -143 A C
ATOM 1555 C ILE A 213 18.426 37.614 474.561 1.00 39.03 A C
ANISOU 1555 C ILE A 213 4636 2682 7511 90 -490 -162 A C
ATOM 1556 O ILE A 213 17.628 38.558 474.583 1.00 49.40 A O
ANISOU 1556 O ILE A 213 5960 4021 8787 77 -457 -180 A O
ATOM 1557 CB ILE A 213 17.750 35.740 473.024 1.00 41.81 A C
ANISOU 1557 CB ILE A 213 5064 3089 7731 98 -346 -106 A C
ATOM 1558 CG1 ILE A 213 19.112 35.663 472.350 1.00 41.98 A C
ANISOU 1558 CG1 ILE A 213 4992 3046 7912 143 -302 -84 A C
ATOM 1559 CG2 ILE A 213 16.846 36.726 472.271 1.00 32.16 A C
ANISOU 1559 CG2 ILE A 213 3830 1915 6476 84 -274 -94 A C
ATOM 1560 CD1 ILE A 213 19.257 34.472 471.465 1.00 33.17 A C
ANISOU 1560 CD1 ILE A 213 3927 1918 6759 175 -222 -71 A C
ATOM 1561 N ARG A 214 19.745 37.768 474.661 1.00 31.85 A N
ANISOU 1561 N ARG A 214 3627 1722 6753 104 -550 -158 A N
ATOM 1562 CA ARG A 214 20.415 39.059 474.616 1.00 32.51 A C
ANISOU 1562 CA ARG A 214 3597 1777 6978 90 -569 -164 A C
ATOM 1563 C ARG A 214 21.506 38.995 473.562 1.00 39.61 A C
ANISOU 1563 C ARG A 214 4346 2652 8050 106 -470 -104 A C
ATOM 1564 O ARG A 214 22.321 38.066 473.568 1.00 62.12 A O
ANISOU 1564 O ARG A 214 7146 5474 10983 137 -491 -90 A O
ATOM 1565 CB ARG A 214 20.992 39.407 475.990 1.00 33.53 A C
ANISOU 1565 CB ARG A 214 3738 1844 7157 78 -771 -227 A C
ATOM 1566 CG ARG A 214 21.673 40.747 476.119 1.00 34.53 A C
ANISOU 1566 CG ARG A 214 3756 1920 7443 48 -831 -250 A C
ATOM 1567 CD ARG A 214 20.775 41.928 475.801 1.00 34.07 A C
ANISOU 1567 CD ARG A 214 3734 1884 7328 33 -737 -264 A C
ATOM 1568 NE ARG A 214 21.317 43.158 476.365 1.00 43.59 A N
ANISOU 1568 NE ARG A 214 4892 3018 8652 2 -850 -316 A N
ATOM 1569 CZ ARG A 214 21.186 44.358 475.813 1.00 43.16 A C
ANISOU 1569 CZ ARG A 214 4783 2947 8669 -16 -772 -297 A C
ATOM 1570 NH1 ARG A 214 20.536 44.483 474.665 1.00 37.12 A N1+
ANISOU 1570 NH1 ARG A 214 4010 2232 7862 -1 -592 -222 A N1+
ATOM 1571 NH2 ARG A 214 21.720 45.428 476.403 1.00 49.56 A N
ANISOU 1571 NH2 ARG A 214 5560 3677 9594 -49 -893 -353 A N
ATOM 1572 N ILE A 215 21.530 39.966 472.653 1.00 38.36 A N
ANISOU 1572 N ILE A 215 4124 2489 7961 92 -349 -63 A N
ATOM 1573 CA ILE A 215 22.495 39.970 471.555 1.00 45.40 A C
ANISOU 1573 CA ILE A 215 4890 3337 9022 108 -200 7 A C
ATOM 1574 C ILE A 215 23.283 41.280 471.546 1.00 50.60 A C
ANISOU 1574 C ILE A 215 5399 3932 9896 66 -202 33 A C
ATOM 1575 O ILE A 215 22.695 42.370 471.554 1.00 57.00 A O
ANISOU 1575 O ILE A 215 6248 4748 10663 35 -207 31 A O
ATOM 1576 CB ILE A 215 21.798 39.748 470.206 1.00 33.58 A C
ANISOU 1576 CB ILE A 215 3493 1863 7403 134 -13 62 A C
ATOM 1577 CG1 ILE A 215 20.915 38.511 470.300 1.00 40.30 A C
ANISOU 1577 CG1 ILE A 215 4492 2764 8059 158 -45 25 A C
ATOM 1578 CG2 ILE A 215 22.817 39.616 469.102 1.00 50.18 A C
ANISOU 1578 CG2 ILE A 215 5504 3898 9662 166 179 133 A C
ATOM 1579 CD1 ILE A 215 19.613 38.679 469.597 1.00 46.28 A C
ANISOU 1579 CD1 ILE A 215 5376 3557 8652 152 6 40 A C
ATOM 1580 N ILE A 216 24.609 41.164 471.504 1.00 47.73 A N
ANISOU 1580 N ILE A 216 4850 3495 9791 66 -194 60 A N
ATOM 1581 CA ILE A 216 25.525 42.292 471.364 1.00 45.50 A C
ANISOU 1581 CA ILE A 216 4380 3127 9779 16 -174 100 A C
ATOM 1582 C ILE A 216 26.425 42.021 470.167 1.00 39.61 A C
ANISOU 1582 C ILE A 216 3495 2318 9238 41 75 199 A C
ATOM 1583 O ILE A 216 27.454 41.358 470.332 1.00 50.11 A O
ANISOU 1583 O ILE A 216 4660 3591 10788 67 63 204 A O
ATOM 1584 CB ILE A 216 26.362 42.481 472.631 1.00 39.55 A C
ANISOU 1584 CB ILE A 216 3498 2312 9216 -17 -432 35 A C
ATOM 1585 CG1 ILE A 216 25.470 42.738 473.820 1.00 38.63 A C
ANISOU 1585 CG1 ILE A 216 3564 2240 8875 -30 -645 -65 A C
ATOM 1586 CG2 ILE A 216 27.311 43.623 472.481 1.00 65.16 A C
ANISOU 1586 CG2 ILE A 216 6530 5458 12769 -77 -427 75 A C
ATOM 1587 CD1 ILE A 216 26.243 42.758 475.091 1.00 40.01 A C
ANISOU 1587 CD1 ILE A 216 3673 2342 9186 -49 -927 -136 A C
ATOM 1588 N PRO A 217 26.070 42.454 468.950 1.00 39.63 A N
ANISOU 1588 N PRO A 217 3569 2314 9175 46 311 285 A N
ATOM 1589 CA PRO A 217 26.853 42.048 467.763 1.00 41.05 A C
ANISOU 1589 CA PRO A 217 3670 2420 9506 90 601 382 A C
ATOM 1590 C PRO A 217 28.209 42.713 467.642 1.00 45.86 A C
ANISOU 1590 C PRO A 217 3997 2910 10517 45 697 455 A C
ATOM 1591 O PRO A 217 29.016 42.286 466.804 1.00 45.04 A O
ANISOU 1591 O PRO A 217 3789 2728 10596 91 959 533 A O
ATOM 1592 CB PRO A 217 25.941 42.430 466.588 1.00 40.55 A C
ANISOU 1592 CB PRO A 217 3820 2372 9214 104 794 457 A C
ATOM 1593 CG PRO A 217 24.552 42.427 467.191 1.00 38.42 A C
ANISOU 1593 CG PRO A 217 3740 2209 8649 97 582 373 A C
ATOM 1594 CD PRO A 217 24.743 42.973 468.573 1.00 38.27 A C
ANISOU 1594 CD PRO A 217 3607 2204 8728 41 330 291 A C
ATOM 1595 N ASP A 218 28.471 43.772 468.398 1.00 51.43 A N
ANISOU 1595 N ASP A 218 4578 3589 11373 -37 515 434 A N
ATOM 1596 CA ASP A 218 29.730 44.489 468.251 1.00 50.25 A C
ANISOU 1596 CA ASP A 218 4143 3322 11629 -91 596 508 A C
ATOM 1597 C ASP A 218 29.905 45.383 469.469 1.00 54.69 A C
ANISOU 1597 C ASP A 218 4614 3868 12299 -159 272 426 A C
ATOM 1598 O ASP A 218 29.183 46.378 469.606 1.00 54.34 A O
ANISOU 1598 O ASP A 218 4703 3851 12092 -198 204 408 A O
ATOM 1599 CB ASP A 218 29.717 45.290 466.960 1.00 47.70 A C
ANISOU 1599 CB ASP A 218 3856 2955 11312 -112 916 650 A C
ATOM 1600 CG ASP A 218 31.082 45.702 466.525 1.00 50.73 A C
ANISOU 1600 CG ASP A 218 3942 3220 12112 -144 1110 756 A C
ATOM 1601 OD1 ASP A 218 31.997 45.748 467.369 1.00 52.08 A O
ANISOU 1601 OD1 ASP A 218 3855 3335 12599 -166 920 708 A O
ATOM 1602 OD2 ASP A 218 31.240 45.930 465.313 1.00 51.99 A O1-
ANISOU 1602 OD2 ASP A 218 4140 3342 12273 -137 1458 892 A O1-
ATOM 1603 N VAL A 219 30.835 45.026 470.356 1.00 51.99 A N
ANISOU 1603 N VAL A 219 4062 3467 12224 -163 63 372 A N
ATOM 1604 CA VAL A 219 31.107 45.880 471.507 1.00 58.27 A C
ANISOU 1604 CA VAL A 219 4793 4221 13125 -217 -259 291 A C
ATOM 1605 C VAL A 219 31.507 47.288 471.091 1.00 61.79 A C
ANISOU 1605 C VAL A 219 5134 4590 13755 -280 -172 360 A C
ATOM 1606 O VAL A 219 31.355 48.229 471.874 1.00 65.91 A O
ANISOU 1606 O VAL A 219 5705 5086 14254 -327 -398 288 A O
ATOM 1607 CB VAL A 219 32.194 45.270 472.416 1.00 50.95 A C
ANISOU 1607 CB VAL A 219 3643 3214 12502 -201 -512 243 A C
ATOM 1608 CG1 VAL A 219 31.744 43.927 472.945 1.00 63.75 A C
ANISOU 1608 CG1 VAL A 219 5404 4903 13915 -142 -634 174 A C
ATOM 1609 CG2 VAL A 219 33.513 45.167 471.672 1.00 53.64 A C
ANISOU 1609 CG2 VAL A 219 3656 3435 13290 -184 -307 357 A C
ATOM 1610 N ASN A 220 32.043 47.457 469.888 1.00 63.20 A N
ANISOU 1610 N ASN A 220 5186 4716 14112 -280 160 499 A N
ATOM 1611 CA ASN A 220 32.538 48.752 469.458 1.00 69.29 A C
ANISOU 1611 CA ASN A 220 5851 5396 15080 -339 259 584 A C
ATOM 1612 C ASN A 220 31.586 49.457 468.513 1.00 67.04 A C
ANISOU 1612 C ASN A 220 5789 5154 14529 -358 480 663 A C
ATOM 1613 O ASN A 220 31.902 50.557 468.045 1.00 55.43 A O
ANISOU 1613 O ASN A 220 4265 3605 13192 -409 587 750 A O
ATOM 1614 CB ASN A 220 33.903 48.594 468.800 1.00 57.62 A C
ANISOU 1614 CB ASN A 220 4078 3806 14010 -325 485 701 A C
ATOM 1615 CG ASN A 220 34.917 48.050 469.748 1.00 61.04 A C
ANISOU 1615 CG ASN A 220 4278 4160 14754 -301 228 634 A C
ATOM 1616 ND2 ASN A 220 35.655 47.046 469.305 1.00 85.68 A N
ANISOU 1616 ND2 ASN A 220 7238 7237 18080 -235 407 689 A N
ATOM 1617 OD1 ASN A 220 35.020 48.499 470.886 1.00 59.59 A O
ANISOU 1617 OD1 ASN A 220 4084 3943 14612 -336 -136 531 A O
ATOM 1618 N ALA A 221 30.418 48.882 468.250 1.00 50.96 A N
ANISOU 1618 N ALA A 221 4013 3227 12124 -314 528 638 A N
ATOM 1619 CA ALA A 221 29.417 49.625 467.503 1.00 60.40 A C
ANISOU 1619 CA ALA A 221 5438 4450 13061 -322 657 703 A C
ATOM 1620 C ALA A 221 28.954 50.827 468.326 1.00 58.90 A C
ANISOU 1620 C ALA A 221 5313 4237 12831 -372 411 622 A C
ATOM 1621 O ALA A 221 28.840 50.756 469.556 1.00 49.43 A O
ANISOU 1621 O ALA A 221 4117 3057 11608 -376 122 479 A O
ATOM 1622 CB ALA A 221 28.241 48.732 467.134 1.00 47.55 A C
ANISOU 1622 CB ALA A 221 4071 2933 11062 -254 711 682 A C
ATOM 1623 N GLU A 222 28.725 51.943 467.632 1.00 61.79 A N
ANISOU 1623 N GLU A 222 5743 4544 13190 -406 537 721 A N
ATOM 1624 CA GLU A 222 28.342 53.202 468.259 1.00 51.53 A C
ANISOU 1624 CA GLU A 222 4504 3188 11886 -451 348 661 A C
ATOM 1625 C GLU A 222 26.843 53.204 468.502 1.00 49.08 A C
ANISOU 1625 C GLU A 222 4462 2965 11221 -401 252 584 A C
ATOM 1626 O GLU A 222 26.074 53.132 467.534 1.00 52.35 A O
ANISOU 1626 O GLU A 222 5036 3415 11439 -361 421 679 A O
ATOM 1627 CB GLU A 222 28.715 54.372 467.353 1.00 57.27 A C
ANISOU 1627 CB GLU A 222 5194 3801 12767 -506 534 813 A C
ATOM 1628 CG GLU A 222 28.568 55.767 467.969 1.00 71.37 A C
ANISOU 1628 CG GLU A 222 7004 5483 14629 -563 351 760 A C
ATOM 1629 CD GLU A 222 28.666 56.889 466.928 1.00 89.02 A C
ANISOU 1629 CD GLU A 222 9268 7609 16948 -609 554 930 A C
ATOM 1630 OE1 GLU A 222 28.162 56.706 465.792 1.00 82.18 A O
ANISOU 1630 OE1 GLU A 222 8545 6777 15904 -571 786 1067 A O
ATOM 1631 OE2 GLU A 222 29.242 57.960 467.248 1.00103.11 A O1-
ANISOU 1631 OE2 GLU A 222 10949 9260 18967 -683 471 930 A O1-
ATOM 1632 N PRO A 223 26.378 53.285 469.752 1.00 48.15 A N
ANISOU 1632 N PRO A 223 4410 2873 11011 -393 -10 420 A N
ATOM 1633 CA PRO A 223 24.927 53.270 469.982 1.00 46.10 A C
ANISOU 1633 CA PRO A 223 4386 2692 10440 -333 -68 352 A C
ATOM 1634 C PRO A 223 24.267 54.455 469.312 1.00 62.14 A C
ANISOU 1634 C PRO A 223 6526 4656 12429 -333 16 434 A C
ATOM 1635 O PRO A 223 24.873 55.514 469.139 1.00 87.56 A O
ANISOU 1635 O PRO A 223 9665 7753 15850 -393 34 489 A O
ATOM 1636 CB PRO A 223 24.796 53.339 471.509 1.00 45.88 A C
ANISOU 1636 CB PRO A 223 4392 2664 10378 -335 -338 168 A C
ATOM 1637 CG PRO A 223 26.102 53.821 472.008 1.00 48.20 A C
ANISOU 1637 CG PRO A 223 4493 2848 10972 -408 -455 148 A C
ATOM 1638 CD PRO A 223 27.143 53.403 471.003 1.00 49.25 A C
ANISOU 1638 CD PRO A 223 4425 2961 11327 -432 -260 295 A C
ATOM 1639 N GLN A 224 23.020 54.258 468.904 1.00 52.45 A N
ANISOU 1639 N GLN A 224 5478 3497 10953 -263 61 450 A N
ATOM 1640 CA GLN A 224 22.237 55.326 468.290 1.00 47.21 A C
ANISOU 1640 CA GLN A 224 4936 2767 10236 -242 111 529 A C
ATOM 1641 C GLN A 224 21.177 55.800 469.271 1.00 49.93 A C
ANISOU 1641 C GLN A 224 5391 3116 10464 -193 -56 385 A C
ATOM 1642 O GLN A 224 20.374 54.984 469.743 1.00 53.51 A O
ANISOU 1642 O GLN A 224 5918 3677 10738 -133 -111 296 A O
ATOM 1643 CB GLN A 224 21.591 54.862 466.991 1.00 45.14 A C
ANISOU 1643 CB GLN A 224 4795 2552 9806 -187 277 673 A C
ATOM 1644 CG GLN A 224 22.575 54.220 466.035 1.00 55.63 A C
ANISOU 1644 CG GLN A 224 6049 3878 11211 -218 481 805 A C
ATOM 1645 CD GLN A 224 23.663 55.165 465.587 1.00 70.97 A C
ANISOU 1645 CD GLN A 224 7872 5692 13402 -297 598 920 A C
ATOM 1646 NE2 GLN A 224 24.906 54.734 465.743 1.00 78.81 A N
ANISOU 1646 NE2 GLN A 224 8667 6671 14606 -348 660 920 A N
ATOM 1647 OE1 GLN A 224 23.398 56.260 465.091 1.00 82.49 A O
ANISOU 1647 OE1 GLN A 224 9407 7056 14879 -308 635 1015 A O
ATOM 1648 N PRO A 225 21.158 57.074 469.646 1.00 55.80 A N
ANISOU 1648 N PRO A 225 6149 3738 11315 -215 -128 352 A N
ATOM 1649 CA PRO A 225 20.156 57.552 470.606 1.00 63.14 A C
ANISOU 1649 CA PRO A 225 7193 4653 12143 -156 -257 207 A C
ATOM 1650 C PRO A 225 18.778 57.717 469.984 1.00 45.59 A C
ANISOU 1650 C PRO A 225 5096 2457 9768 -59 -198 265 A C
ATOM 1651 O PRO A 225 18.628 57.908 468.778 1.00 45.98 A O
ANISOU 1651 O PRO A 225 5173 2485 9812 -47 -86 430 A O
ATOM 1652 CB PRO A 225 20.716 58.906 471.054 1.00 52.89 A C
ANISOU 1652 CB PRO A 225 5870 3187 11039 -214 -338 168 A C
ATOM 1653 CG PRO A 225 21.606 59.317 469.949 1.00 50.16 A C
ANISOU 1653 CG PRO A 225 5424 2766 10867 -286 -209 348 A C
ATOM 1654 CD PRO A 225 22.191 58.084 469.369 1.00 49.07 A C
ANISOU 1654 CD PRO A 225 5194 2741 10709 -301 -99 428 A C
ATOM 1655 N LEU A 226 17.760 57.639 470.845 1.00 44.80 A N
ANISOU 1655 N LEU A 226 5076 2395 9550 17 -276 129 A N
ATOM 1656 CA LEU A 226 16.390 57.950 470.437 1.00 59.11 A C
ANISOU 1656 CA LEU A 226 6976 4212 11272 121 -248 164 A C
ATOM 1657 C LEU A 226 16.178 59.461 470.354 1.00 64.43 A C
ANISOU 1657 C LEU A 226 7695 4723 12063 140 -267 184 A C
ATOM 1658 O LEU A 226 16.466 60.198 471.306 1.00 66.75 A O
ANISOU 1658 O LEU A 226 8005 4918 12439 119 -344 58 A O
ATOM 1659 CB LEU A 226 15.377 57.332 471.406 1.00 43.39 A C
ANISOU 1659 CB LEU A 226 5031 2307 9148 200 -294 16 A C
ATOM 1660 CG LEU A 226 15.465 55.826 471.674 1.00 53.88 A C
ANISOU 1660 CG LEU A 226 6334 3783 10354 186 -290 -22 A C
ATOM 1661 CD1 LEU A 226 14.472 55.391 472.729 1.00 45.56 A C
ANISOU 1661 CD1 LEU A 226 5336 2781 9193 260 -319 -167 A C
ATOM 1662 CD2 LEU A 226 15.222 55.056 470.397 1.00 40.52 A C
ANISOU 1662 CD2 LEU A 226 4627 2172 8597 198 -210 130 A C
ATOM 1663 N HIS A 227 15.666 59.916 469.218 1.00 47.27 A N
ANISOU 1663 N HIS A 227 5561 2507 9891 184 -207 343 A N
ATOM 1664 CA HIS A 227 15.358 61.315 469.008 1.00 49.34 A C
ANISOU 1664 CA HIS A 227 5879 2607 10260 217 -222 386 A C
ATOM 1665 C HIS A 227 13.864 61.564 469.091 1.00 57.10 A C
ANISOU 1665 C HIS A 227 6920 3596 11181 358 -253 354 A C
ATOM 1666 O HIS A 227 13.054 60.726 468.679 1.00 48.05 A O
ANISOU 1666 O HIS A 227 5769 2568 9920 425 -241 395 A O
ATOM 1667 CB HIS A 227 15.892 61.797 467.665 1.00 72.60 A C
ANISOU 1667 CB HIS A 227 8844 5470 13270 170 -138 605 A C
ATOM 1668 CG HIS A 227 17.377 61.933 467.641 1.00 72.14 A C
ANISOU 1668 CG HIS A 227 8702 5357 13352 33 -93 639 A C
ATOM 1669 CD2 HIS A 227 18.353 61.038 467.368 1.00 74.07 A C
ANISOU 1669 CD2 HIS A 227 8858 5682 13604 -47 -20 683 A C
ATOM 1670 ND1 HIS A 227 18.013 63.113 467.950 1.00 53.77 A N
ANISOU 1670 ND1 HIS A 227 6358 2862 11212 -32 -125 623 A N
ATOM 1671 CE1 HIS A 227 19.318 62.942 467.864 1.00 65.49 A C
ANISOU 1671 CE1 HIS A 227 7727 4329 12825 -151 -79 662 A C
ATOM 1672 NE2 HIS A 227 19.552 61.693 467.511 1.00 67.68 A N
ANISOU 1672 NE2 HIS A 227 7957 4759 13001 -156 -8 699 A N
ATOM 1673 N MET A 228 13.500 62.720 469.632 1.00 51.08 A N
ANISOU 1673 N MET A 228 6202 2694 10513 407 -295 279 A N
ATOM 1674 CA MET A 228 12.092 63.075 469.684 1.00 54.22 A C
ANISOU 1674 CA MET A 228 6631 3076 10893 556 -311 255 A C
ATOM 1675 C MET A 228 11.632 63.529 468.305 1.00 52.62 A C
ANISOU 1675 C MET A 228 6464 2820 10711 607 -304 470 A C
ATOM 1676 O MET A 228 12.269 64.365 467.671 1.00 54.22 A O
ANISOU 1676 O MET A 228 6714 2890 10999 553 -289 591 A O
ATOM 1677 CB MET A 228 11.852 64.149 470.729 1.00 53.38 A C
ANISOU 1677 CB MET A 228 6577 2825 10879 606 -345 96 A C
ATOM 1678 CG MET A 228 10.426 64.586 470.846 1.00 54.32 A C
ANISOU 1678 CG MET A 228 6710 2914 11014 773 -343 64 A C
ATOM 1679 SD MET A 228 10.188 65.525 472.367 1.00 67.29 A S
ANISOU 1679 SD MET A 228 8439 4409 12718 841 -350 -182 A S
ATOM 1680 CE MET A 228 10.899 64.434 473.591 1.00 74.22 A C
ANISOU 1680 CE MET A 228 9331 5406 13465 752 -355 -366 A C
ATOM 1681 N ILE A 229 10.569 62.916 467.810 1.00 56.03 A N
ANISOU 1681 N ILE A 229 6876 3352 11061 705 -319 528 A N
ATOM 1682 CA ILE A 229 10.049 63.247 466.495 1.00 53.02 A C
ANISOU 1682 CA ILE A 229 6550 2924 10673 768 -347 735 A C
ATOM 1683 C ILE A 229 8.906 64.224 466.712 1.00 58.37 A C
ANISOU 1683 C ILE A 229 7226 3499 11451 912 -404 706 A C
ATOM 1684 O ILE A 229 8.959 65.390 466.300 1.00 57.10 A O
ANISOU 1684 O ILE A 229 7138 3171 11385 939 -422 794 A O
ATOM 1685 CB ILE A 229 9.570 61.987 465.764 1.00 51.48 A C
ANISOU 1685 CB ILE A 229 6335 2885 10338 791 -366 821 A C
ATOM 1686 CG1 ILE A 229 10.717 60.998 465.630 1.00 49.77 A C
ANISOU 1686 CG1 ILE A 229 6121 2760 10031 659 -293 833 A C
ATOM 1687 CG2 ILE A 229 9.027 62.336 464.394 1.00 53.03 A C
ANISOU 1687 CG2 ILE A 229 6623 3021 10503 863 -427 1041 A C
ATOM 1688 CD1 ILE A 229 11.829 61.496 464.764 1.00 67.89 A C
ANISOU 1688 CD1 ILE A 229 8499 4954 12344 567 -223 992 A C
ATOM 1689 N HIS A 230 7.856 63.734 467.348 1.00 62.37 A N
ANISOU 1689 N HIS A 230 7645 4102 11952 1010 -422 588 A N
ATOM 1690 CA HIS A 230 6.736 64.539 467.784 1.00 56.05 A C
ANISOU 1690 CA HIS A 230 6809 3221 11267 1159 -447 521 A C
ATOM 1691 C HIS A 230 6.731 64.545 469.303 1.00 64.59 A C
ANISOU 1691 C HIS A 230 7865 4307 12369 1168 -380 279 A C
ATOM 1692 O HIS A 230 7.363 63.711 469.958 1.00 64.48 A O
ANISOU 1692 O HIS A 230 7845 4392 12263 1075 -340 175 A O
ATOM 1693 CB HIS A 230 5.431 63.990 467.216 1.00 56.14 A C
ANISOU 1693 CB HIS A 230 6725 3331 11276 1278 -514 597 A C
ATOM 1694 CG HIS A 230 5.324 64.151 465.735 1.00 57.13 A C
ANISOU 1694 CG HIS A 230 6918 3419 11369 1296 -611 836 A C
ATOM 1695 CD2 HIS A 230 5.038 65.231 464.974 1.00 59.61 A C
ANISOU 1695 CD2 HIS A 230 7309 3584 11757 1373 -679 979 A C
ATOM 1696 ND1 HIS A 230 5.578 63.119 464.856 1.00 55.74 A N
ANISOU 1696 ND1 HIS A 230 6771 3356 11052 1234 -647 958 A N
ATOM 1697 CE1 HIS A 230 5.422 63.550 463.618 1.00 57.40 A C
ANISOU 1697 CE1 HIS A 230 7086 3489 11233 1276 -736 1167 A C
ATOM 1698 NE2 HIS A 230 5.091 64.828 463.663 1.00 59.74 A N
ANISOU 1698 NE2 HIS A 230 7410 3629 11661 1359 -760 1188 A N
ATOM 1699 N LYS A 231 5.982 65.414 469.843 1.00 64.88 A N
ANISOU 1699 N LYS A 231 7900 4238 12514 1291 -369 194 A N
ATOM 1700 CA LYS A 231 6.062 65.579 471.284 1.00 60.03 A C
ANISOU 1700 CA LYS A 231 7320 3589 11900 1308 -298 -37 A C
ATOM 1701 C LYS A 231 5.141 64.583 471.990 1.00 63.42 A C
ANISOU 1701 C LYS A 231 7647 4173 12277 1384 -228 -151 A C
ATOM 1702 O LYS A 231 3.981 64.420 471.588 1.00 57.56 A O
ANISOU 1702 O LYS A 231 6786 3483 11601 1499 -232 -90 A O
ATOM 1703 CB LYS A 231 5.697 67.005 471.652 1.00 60.90 A C
ANISOU 1703 CB LYS A 231 7499 3493 12146 1417 -293 -99 A C
ATOM 1704 CG LYS A 231 6.214 67.474 472.981 1.00 72.33 A C
ANISOU 1704 CG LYS A 231 9064 4836 13582 1400 -247 -320 A C
ATOM 1705 CD LYS A 231 5.143 67.256 474.029 1.00 80.44 A C
ANISOU 1705 CD LYS A 231 10064 5902 14595 1551 -145 -497 A C
ATOM 1706 CE LYS A 231 5.317 68.130 475.257 1.00 90.82 A C
ANISOU 1706 CE LYS A 231 11542 7045 15919 1605 -98 -713 A C
ATOM 1707 NZ LYS A 231 4.098 68.029 476.128 1.00 96.34 A N1+
ANISOU 1707 NZ LYS A 231 12216 7770 16620 1790 38 -863 A N1+
ATOM 1708 N PRO A 232 5.636 63.860 472.988 1.00 55.57 A N
ANISOU 1708 N PRO A 232 6690 3252 11173 1317 -171 -302 A N
ATOM 1709 CA PRO A 232 4.779 62.949 473.744 1.00 62.21 A C
ANISOU 1709 CA PRO A 232 7451 4219 11967 1389 -77 -413 A C
ATOM 1710 C PRO A 232 4.066 63.584 474.928 1.00 57.12 A C
ANISOU 1710 C PRO A 232 6853 3484 11366 1531 35 -602 A C
ATOM 1711 O PRO A 232 4.572 64.478 475.602 1.00 58.58 A O
ANISOU 1711 O PRO A 232 7190 3518 11550 1538 38 -721 A O
ATOM 1712 CB PRO A 232 5.774 61.882 474.228 1.00 52.65 A C
ANISOU 1712 CB PRO A 232 6294 3112 10600 1247 -75 -475 A C
ATOM 1713 CG PRO A 232 7.034 62.594 474.371 1.00 53.05 A C
ANISOU 1713 CG PRO A 232 6474 3041 10641 1143 -139 -500 A C
ATOM 1714 CD PRO A 232 7.060 63.640 473.283 1.00 54.38 A C
ANISOU 1714 CD PRO A 232 6634 3093 10933 1155 -202 -341 A C
ATOM 1715 N GLN A 233 2.874 63.056 475.200 1.00 57.52 A N
ANISOU 1715 N GLN A 233 6771 3628 11456 1646 136 -634 A N
ATOM 1716 CA GLN A 233 2.130 63.434 476.396 1.00 68.97 A C
ANISOU 1716 CA GLN A 233 8258 5021 12926 1791 295 -822 A C
ATOM 1717 C GLN A 233 2.837 63.030 477.680 1.00 59.17 A C
ANISOU 1717 C GLN A 233 7200 3776 11505 1740 371 -1018 A C
ATOM 1718 O GLN A 233 2.486 63.531 478.747 1.00 73.21 A O
ANISOU 1718 O GLN A 233 9095 5464 13255 1854 496 -1199 A O
ATOM 1719 CB GLN A 233 0.736 62.816 476.366 1.00 72.59 A C
ANISOU 1719 CB GLN A 233 8497 5602 13484 1906 407 -796 A C
ATOM 1720 CG GLN A 233 0.180 62.717 474.972 1.00 86.17 A C
ANISOU 1720 CG GLN A 233 10026 7377 15338 1906 275 -579 A C
ATOM 1721 CD GLN A 233 -1.272 62.319 474.955 1.00 88.23 A C
ANISOU 1721 CD GLN A 233 10046 7728 15751 2027 362 -555 A C
ATOM 1722 NE2 GLN A 233 -1.568 61.151 474.367 1.00 78.96 A N
ANISOU 1722 NE2 GLN A 233 8714 6709 14578 1953 310 -446 A N
ATOM 1723 OE1 GLN A 233 -2.128 63.059 475.454 1.00 86.30 A O
ANISOU 1723 OE1 GLN A 233 9748 7408 15634 2185 473 -632 A O
ATOM 1724 N ASN A 234 3.780 62.101 477.612 1.00 82.93 A N
ANISOU 1724 N ASN A 234 10248 6878 14384 1581 302 -991 A N
ATOM 1725 CA ASN A 234 4.548 61.647 478.764 1.00 67.36 A C
ANISOU 1725 CA ASN A 234 8461 4900 12233 1519 331 -1161 A C
ATOM 1726 C ASN A 234 6.023 61.762 478.435 1.00 60.87 A C
ANISOU 1726 C ASN A 234 7733 4034 11360 1345 157 -1113 A C
ATOM 1727 O ASN A 234 6.472 61.275 477.391 1.00 67.89 A O
ANISOU 1727 O ASN A 234 8510 5010 12275 1238 67 -941 A O
ATOM 1728 CB ASN A 234 4.208 60.206 479.147 1.00 75.16 A C
ANISOU 1728 CB ASN A 234 9383 6055 13121 1499 433 -1182 A C
ATOM 1729 CG ASN A 234 5.250 59.600 480.070 1.00 84.69 A C
ANISOU 1729 CG ASN A 234 10785 7260 14132 1396 399 -1310 A C
ATOM 1730 ND2 ASN A 234 5.996 58.594 479.568 1.00 81.22 A N
ANISOU 1730 ND2 ASN A 234 10294 6930 13637 1252 298 -1207 A N
ATOM 1731 OD1 ASN A 234 5.391 60.029 481.219 1.00 71.32 A O
ANISOU 1731 OD1 ASN A 234 9303 5463 12332 1450 453 -1503 A O
ATOM 1732 N THR A 235 6.768 62.427 479.303 1.00 56.35 A N
ANISOU 1732 N THR A 235 7365 3321 10726 1319 113 -1264 A N
ATOM 1733 CA THR A 235 8.155 62.748 479.007 1.00 55.84 A C
ANISOU 1733 CA THR A 235 7357 3191 10670 1156 -52 -1218 A C
ATOM 1734 C THR A 235 9.165 61.753 479.578 1.00 57.68 A C
ANISOU 1734 C THR A 235 7659 3500 10756 1023 -126 -1278 A C
ATOM 1735 O THR A 235 10.361 61.893 479.308 1.00 53.92 A O
ANISOU 1735 O THR A 235 7186 2991 10311 880 -262 -1228 A O
ATOM 1736 CB THR A 235 8.456 64.153 479.530 1.00 58.62 A C
ANISOU 1736 CB THR A 235 7874 3320 11079 1186 -95 -1336 A C
ATOM 1737 CG2 THR A 235 7.314 65.077 479.163 1.00 73.88 A C
ANISOU 1737 CG2 THR A 235 9755 5169 13146 1352 -5 -1305 A C
ATOM 1738 OG1 THR A 235 8.539 64.115 480.958 1.00 60.92 A O
ANISOU 1738 OG1 THR A 235 8385 3544 11217 1225 -61 -1572 A O
ATOM 1739 N GLU A 236 8.726 60.752 480.338 1.00 53.69 A N
ANISOU 1739 N GLU A 236 7200 3092 10109 1066 -37 -1375 A N
ATOM 1740 CA GLU A 236 9.656 59.796 480.932 1.00 61.44 A C
ANISOU 1740 CA GLU A 236 8265 4132 10946 951 -122 -1433 A C
ATOM 1741 C GLU A 236 10.193 58.798 479.911 1.00 62.09 A C
ANISOU 1741 C GLU A 236 8166 4367 11057 831 -186 -1244 A C
ATOM 1742 O GLU A 236 9.532 58.463 478.922 1.00 77.77 A O
ANISOU 1742 O GLU A 236 9984 6451 13116 860 -121 -1093 A O
ATOM 1743 CB GLU A 236 8.995 59.040 482.078 1.00 65.57 A C
ANISOU 1743 CB GLU A 236 8921 4694 11297 1041 8 -1597 A C
ATOM 1744 CG GLU A 236 8.424 59.932 483.146 1.00 76.80 A C
ANISOU 1744 CG GLU A 236 10555 5971 12653 1179 110 -1803 A C
ATOM 1745 CD GLU A 236 7.456 59.198 484.045 1.00 90.04 A C
ANISOU 1745 CD GLU A 236 12317 7711 14185 1304 324 -1932 A C
ATOM 1746 OE1 GLU A 236 7.608 57.962 484.193 1.00 93.85 A O
ANISOU 1746 OE1 GLU A 236 12779 8311 14568 1243 336 -1911 A O
ATOM 1747 OE2 GLU A 236 6.541 59.859 484.590 1.00 92.42 A O1-
ANISOU 1747 OE2 GLU A 236 12698 7940 14478 1465 496 -2049 A O1-
ATOM 1748 N ALA A 237 11.415 58.326 480.174 1.00 62.73 A N
ANISOU 1748 N ALA A 237 8292 4461 11081 699 -323 -1257 A N
ATOM 1749 CA ALA A 237 12.124 57.429 479.266 1.00 53.42 A C
ANISOU 1749 CA ALA A 237 6960 3408 9929 585 -382 -1092 A C
ATOM 1750 C ALA A 237 11.350 56.134 479.072 1.00 54.34 A C
ANISOU 1750 C ALA A 237 7005 3675 9966 624 -279 -1040 A C
ATOM 1751 O ALA A 237 10.798 55.565 480.019 1.00 59.86 A O
ANISOU 1751 O ALA A 237 7805 4389 10548 685 -209 -1165 A O
ATOM 1752 CB ALA A 237 13.515 57.107 479.816 1.00 47.02 A C
ANISOU 1752 CB ALA A 237 6205 2578 9081 460 -545 -1143 A C
ATOM 1753 N VAL A 238 11.348 55.649 477.863 1.00 51.88 A N
ANISOU 1753 N VAL A 238 6535 3464 9713 584 -267 -863 A N
ATOM 1754 CA VAL A 238 10.558 54.473 477.558 1.00 42.10 A C
ANISOU 1754 CA VAL A 238 5217 2354 8425 614 -180 -804 A C
ATOM 1755 C VAL A 238 11.419 53.245 477.806 1.00 56.57 A C
ANISOU 1755 C VAL A 238 7071 4263 10159 519 -244 -801 A C
ATOM 1756 O VAL A 238 12.621 53.231 477.524 1.00 67.36 A O
ANISOU 1756 O VAL A 238 8420 5627 11547 421 -348 -753 A O
ATOM 1757 CB VAL A 238 10.027 54.533 476.116 1.00 41.39 A C
ANISOU 1757 CB VAL A 238 4975 2321 8430 629 -153 -624 A C
ATOM 1758 CG1 VAL A 238 9.105 53.381 475.844 1.00 52.52 A C
ANISOU 1758 CG1 VAL A 238 6299 3844 9812 662 -82 -576 A C
ATOM 1759 CG2 VAL A 238 9.294 55.823 475.886 1.00 43.04 A C
ANISOU 1759 CG2 VAL A 238 5169 2435 8749 724 -123 -619 A C
ATOM 1760 N ASN A 239 10.798 52.227 478.381 1.00 55.19 A N
ANISOU 1760 N ASN A 239 6928 4146 9896 552 -172 -855 A N
ATOM 1761 CA ASN A 239 11.433 50.953 478.669 1.00 49.57 A C
ANISOU 1761 CA ASN A 239 6248 3498 9087 477 -226 -851 A C
ATOM 1762 C ASN A 239 11.592 50.171 477.368 1.00 49.76 A C
ANISOU 1762 C ASN A 239 6128 3630 9149 421 -228 -677 A C
ATOM 1763 O ASN A 239 10.623 49.997 476.625 1.00 60.92 A O
ANISOU 1763 O ASN A 239 7444 5091 10610 465 -147 -597 A O
ATOM 1764 CB ASN A 239 10.545 50.216 479.680 1.00 39.52 A C
ANISOU 1764 CB ASN A 239 5069 2288 7657 529 -110 -940 A C
ATOM 1765 CG ASN A 239 11.185 48.995 480.280 1.00 38.89 A C
ANISOU 1765 CG ASN A 239 5083 2300 7393 453 -173 -941 A C
ATOM 1766 ND2 ASN A 239 10.951 48.792 481.556 1.00 40.14 A N
ANISOU 1766 ND2 ASN A 239 5425 2471 7355 481 -130 -1055 A N
ATOM 1767 OD1 ASN A 239 11.890 48.252 479.616 1.00 37.54 A O
ANISOU 1767 OD1 ASN A 239 4834 2179 7249 378 -253 -839 A O
ATOM 1768 N LEU A 240 12.808 49.710 477.076 1.00 36.67 A N
ANISOU 1768 N LEU A 240 4454 2001 7478 330 -323 -622 A N
ATOM 1769 CA LEU A 240 13.077 49.013 475.822 1.00 39.98 A C
ANISOU 1769 CA LEU A 240 4766 2506 7918 286 -308 -473 A C
ATOM 1770 C LEU A 240 13.381 47.516 475.970 1.00 34.31 A C
ANISOU 1770 C LEU A 240 4062 1858 7115 244 -324 -458 A C
ATOM 1771 O LEU A 240 13.778 46.882 474.984 1.00 39.90 A O
ANISOU 1771 O LEU A 240 4705 2625 7829 208 -313 -353 A O
ATOM 1772 CB LEU A 240 14.238 49.690 475.099 1.00 35.67 A C
ANISOU 1772 CB LEU A 240 4160 1930 7464 228 -356 -398 A C
ATOM 1773 CG LEU A 240 14.369 51.198 475.033 1.00 37.02 A C
ANISOU 1773 CG LEU A 240 4328 2000 7738 238 -371 -408 A C
ATOM 1774 CD1 LEU A 240 15.689 51.530 474.367 1.00 37.38 A C
ANISOU 1774 CD1 LEU A 240 4296 2015 7891 159 -404 -324 A C
ATOM 1775 CD2 LEU A 240 13.184 51.787 474.250 1.00 40.90 A C
ANISOU 1775 CD2 LEU A 240 4792 2487 8262 313 -293 -340 A C
ATOM 1776 N SER A 241 13.198 46.930 477.152 1.00 34.57 A N
ANISOU 1776 N SER A 241 4198 1893 7043 251 -339 -556 A N
ATOM 1777 CA SER A 241 13.773 45.620 477.456 1.00 50.57 A C
ANISOU 1777 CA SER A 241 6261 3994 8958 200 -388 -537 A C
ATOM 1778 C SER A 241 13.124 44.438 476.729 1.00 44.12 A C
ANISOU 1778 C SER A 241 5394 3302 8067 187 -307 -441 A C
ATOM 1779 O SER A 241 13.687 43.340 476.770 1.00 61.68 A O
ANISOU 1779 O SER A 241 7639 5566 10230 148 -347 -411 A O
ATOM 1780 CB SER A 241 13.719 45.361 478.964 1.00 55.45 A C
ANISOU 1780 CB SER A 241 7044 4614 9411 210 -427 -648 A C
ATOM 1781 OG SER A 241 12.437 45.572 479.502 1.00 56.68 A O
ANISOU 1781 OG SER A 241 7258 4811 9466 265 -292 -697 A O
ATOM 1782 N SER A 242 11.968 44.604 476.093 1.00 32.65 A N
ANISOU 1782 N SER A 242 3877 1898 6631 218 -215 -398 A N
ATOM 1783 CA SER A 242 11.285 43.470 475.471 1.00 31.93 A C
ANISOU 1783 CA SER A 242 3745 1911 6475 193 -169 -323 A C
ATOM 1784 C SER A 242 11.836 43.058 474.101 1.00 37.67 A C
ANISOU 1784 C SER A 242 4421 2646 7244 165 -200 -228 A C
ATOM 1785 O SER A 242 11.581 41.924 473.664 1.00 35.92 A O
ANISOU 1785 O SER A 242 4204 2491 6951 132 -194 -186 A O
ATOM 1786 CB SER A 242 9.796 43.778 475.344 1.00 32.46 A C
ANISOU 1786 CB SER A 242 3743 2022 6567 234 -85 -314 A C
ATOM 1787 OG SER A 242 9.145 43.437 476.555 1.00 46.52 A O
ANISOU 1787 OG SER A 242 5579 3840 8255 241 -2 -378 A O
ATOM 1788 N GLY A 243 12.524 43.955 473.392 1.00 31.30 A N
ANISOU 1788 N GLY A 243 3581 1764 6547 177 -219 -193 A N
ATOM 1789 CA GLY A 243 13.121 43.655 472.108 1.00 30.96 A C
ANISOU 1789 CA GLY A 243 3518 1720 6524 160 -211 -102 A C
ATOM 1790 C GLY A 243 14.560 43.170 472.234 1.00 51.66 A C
ANISOU 1790 C GLY A 243 6142 4304 9183 127 -230 -105 A C
ATOM 1791 O GLY A 243 15.003 42.678 473.278 1.00 44.55 A O
ANISOU 1791 O GLY A 243 5268 3401 8257 111 -284 -169 A O
ATOM 1792 N VAL A 244 15.299 43.296 471.136 1.00 35.77 A N
ANISOU 1792 N VAL A 244 4102 2267 7222 123 -182 -27 A N
ATOM 1793 CA VAL A 244 16.705 42.916 471.121 1.00 36.76 A C
ANISOU 1793 CA VAL A 244 4185 2380 7403 100 -174 -17 A C
ATOM 1794 C VAL A 244 17.657 44.085 470.927 1.00 35.81 A C
ANISOU 1794 C VAL A 244 3983 2201 7421 83 -154 15 A C
ATOM 1795 O VAL A 244 18.859 43.920 471.195 1.00 46.25 A O
ANISOU 1795 O VAL A 244 5228 3497 8849 60 -172 9 A O
ATOM 1796 CB VAL A 244 16.974 41.841 470.055 1.00 41.16 A C
ANISOU 1796 CB VAL A 244 4771 2944 7923 110 -95 41 A C
ATOM 1797 CG1 VAL A 244 16.204 40.580 470.404 1.00 30.39 A C
ANISOU 1797 CG1 VAL A 244 3479 1657 6411 106 -136 -2 A C
ATOM 1798 CG2 VAL A 244 16.580 42.385 468.696 1.00 49.04 A C
ANISOU 1798 CG2 VAL A 244 5810 3936 8889 128 -9 130 A C
ATOM 1799 N LEU A 245 17.174 45.258 470.484 1.00 41.50 A N
ANISOU 1799 N LEU A 245 4707 2888 8172 93 -126 55 A N
ATOM 1800 CA LEU A 245 18.045 46.374 470.109 1.00 33.81 A C
ANISOU 1800 CA LEU A 245 3662 1842 7343 66 -87 109 A C
ATOM 1801 C LEU A 245 18.517 47.231 471.276 1.00 34.53 A C
ANISOU 1801 C LEU A 245 3703 1886 7532 36 -196 22 A C
ATOM 1802 O LEU A 245 19.441 48.014 471.078 1.00 35.69 A O
ANISOU 1802 O LEU A 245 3764 1962 7835 -3 -182 59 A O
ATOM 1803 CB LEU A 245 17.336 47.274 469.112 1.00 34.27 A C
ANISOU 1803 CB LEU A 245 3768 1861 7391 92 -23 201 A C
ATOM 1804 CG LEU A 245 17.071 46.707 467.723 1.00 34.25 A C
ANISOU 1804 CG LEU A 245 3841 1858 7313 120 80 314 A C
ATOM 1805 CD1 LEU A 245 16.412 47.756 466.863 1.00 35.08 A C
ANISOU 1805 CD1 LEU A 245 4008 1904 7418 150 104 416 A C
ATOM 1806 CD2 LEU A 245 18.372 46.273 467.099 1.00 34.92 A C
ANISOU 1806 CD2 LEU A 245 3884 1907 7476 94 206 377 A C
ATOM 1807 N ARG A 246 17.920 47.104 472.466 1.00 46.19 A N
ANISOU 1807 N ARG A 246 5241 3383 8926 52 -298 -91 A N
ATOM 1808 CA ARG A 246 18.253 47.957 473.608 1.00 35.14 A C
ANISOU 1808 CA ARG A 246 3847 1917 7589 33 -414 -190 A C
ATOM 1809 C ARG A 246 19.762 48.071 473.829 1.00 46.24 A C
ANISOU 1809 C ARG A 246 5140 3265 9164 -25 -488 -189 A C
ATOM 1810 O ARG A 246 20.498 47.086 473.762 1.00 45.43 A O
ANISOU 1810 O ARG A 246 4978 3190 9096 -37 -497 -167 A O
ATOM 1811 CB ARG A 246 17.569 47.421 474.867 1.00 34.78 A C
ANISOU 1811 CB ARG A 246 3914 1891 7408 62 -493 -309 A C
ATOM 1812 CG ARG A 246 18.011 48.055 476.171 1.00 39.38 A C
ANISOU 1812 CG ARG A 246 4554 2391 8017 46 -636 -433 A C
ATOM 1813 CD ARG A 246 17.266 47.446 477.345 1.00 41.02 A C
ANISOU 1813 CD ARG A 246 4916 2604 8066 83 -681 -543 A C
ATOM 1814 NE ARG A 246 17.335 45.989 477.332 1.00 49.29 A N
ANISOU 1814 NE ARG A 246 5972 3719 9036 79 -679 -506 A N
ATOM 1815 CZ ARG A 246 18.274 45.260 477.933 1.00 64.54 A C
ANISOU 1815 CZ ARG A 246 7916 5634 10973 52 -809 -527 A C
ATOM 1816 NH1 ARG A 246 19.249 45.837 478.620 1.00 36.73 A N1+
ANISOU 1816 NH1 ARG A 246 4388 2033 7536 21 -973 -589 A N1+
ATOM 1817 NH2 ARG A 246 18.229 43.934 477.852 1.00 57.63 A N
ANISOU 1817 NH2 ARG A 246 7057 4810 10028 56 -794 -484 A N
ATOM 1818 N ALA A 247 20.215 49.289 474.115 1.00 45.87 A N
ANISOU 1818 N ALA A 247 5056 3126 9248 -57 -548 -216 A N
ATOM 1819 CA ALA A 247 21.643 49.544 474.227 1.00 47.55 A C
ANISOU 1819 CA ALA A 247 5123 3265 9679 -119 -623 -203 A C
ATOM 1820 C ALA A 247 22.229 48.858 475.448 1.00 39.46 A C
ANISOU 1820 C ALA A 247 4109 2232 8653 -130 -816 -306 A C
ATOM 1821 O ALA A 247 21.544 48.586 476.438 1.00 42.43 A O
ANISOU 1821 O ALA A 247 4642 2624 8854 -99 -908 -411 A O
ATOM 1822 CB ALA A 247 21.932 51.045 474.314 1.00 40.74 A C
ANISOU 1822 CB ALA A 247 4228 2289 8964 -158 -664 -214 A C
ATOM 1823 N VAL A 248 23.531 48.625 475.371 1.00 40.58 A N
ANISOU 1823 N VAL A 248 4078 2329 9011 -171 -877 -270 A N
ATOM 1824 CA VAL A 248 24.297 47.885 476.369 1.00 41.31 A C
ANISOU 1824 CA VAL A 248 4144 2398 9154 -179 -1084 -339 A C
ATOM 1825 C VAL A 248 24.984 48.898 477.265 1.00 43.48 A C
ANISOU 1825 C VAL A 248 4390 2557 9575 -228 -1303 -425 A C
ATOM 1826 O VAL A 248 25.506 49.910 476.783 1.00 44.78 A O
ANISOU 1826 O VAL A 248 4423 2647 9942 -273 -1265 -380 A O
ATOM 1827 CB VAL A 248 25.339 46.953 475.706 1.00 41.57 A C
ANISOU 1827 CB VAL A 248 3976 2436 9383 -181 -1027 -245 A C
ATOM 1828 CG1 VAL A 248 26.023 46.079 476.731 1.00 42.34 A C
ANISOU 1828 CG1 VAL A 248 4056 2504 9528 -172 -1263 -307 A C
ATOM 1829 CG2 VAL A 248 24.728 46.137 474.609 1.00 39.83 A C
ANISOU 1829 CG2 VAL A 248 3792 2308 9032 -138 -787 -156 A C
ATOM 1830 N SER A 249 24.997 48.620 478.563 1.00 57.31 A N
ANISOU 1830 N SER A 249 6277 4279 11218 -219 -1537 -546 A N
ATOM 1831 CA SER A 249 25.751 49.410 479.530 1.00 54.25 A C
ANISOU 1831 CA SER A 249 5885 3772 10954 -263 -1801 -643 A C
ATOM 1832 C SER A 249 27.221 49.515 479.113 1.00 55.20 A C
ANISOU 1832 C SER A 249 5705 3820 11448 -313 -1875 -563 A C
ATOM 1833 O SER A 249 27.884 48.476 478.934 1.00 51.09 A O
ANISOU 1833 O SER A 249 5045 3320 11046 -297 -1900 -503 A O
ATOM 1834 CB SER A 249 25.635 48.759 480.908 1.00 58.18 A C
ANISOU 1834 CB SER A 249 6595 4257 11255 -237 -2049 -767 A C
ATOM 1835 OG SER A 249 26.621 49.236 481.796 1.00 63.81 A O
ANISOU 1835 OG SER A 249 7281 4855 12110 -277 -2356 -844 A O
ATOM 1836 N PRO A 250 27.764 50.731 478.958 1.00 57.75 A N
ANISOU 1836 N PRO A 250 5914 4042 11985 -369 -1906 -557 A N
ATOM 1837 CA PRO A 250 29.173 50.868 478.543 1.00 52.37 A C
ANISOU 1837 CA PRO A 250 4923 3275 11700 -414 -1953 -470 A C
ATOM 1838 C PRO A 250 30.155 50.180 479.464 1.00 54.13 A C
ANISOU 1838 C PRO A 250 5063 3442 12062 -408 -2264 -518 A C
ATOM 1839 O PRO A 250 31.215 49.726 478.997 1.00 55.28 A O
ANISOU 1839 O PRO A 250 4931 3547 12524 -409 -2252 -423 A O
ATOM 1840 CB PRO A 250 29.375 52.384 478.529 1.00 54.31 A C
ANISOU 1840 CB PRO A 250 5141 3406 12090 -477 -1981 -490 A C
ATOM 1841 CG PRO A 250 28.007 52.925 478.265 1.00 53.79 A C
ANISOU 1841 CG PRO A 250 5304 3394 11738 -453 -1800 -516 A C
ATOM 1842 CD PRO A 250 27.078 52.031 479.012 1.00 55.60 A C
ANISOU 1842 CD PRO A 250 5777 3720 11627 -388 -1857 -611 A C
ATOM 1843 N LEU A 251 29.808 50.043 480.749 1.00 57.99 A N
ANISOU 1843 N LEU A 251 5797 3918 12317 -392 -2533 -658 A N
ATOM 1844 CA LEU A 251 30.607 49.235 481.669 1.00 69.36 A C
ANISOU 1844 CA LEU A 251 7216 5311 13826 -372 -2855 -698 A C
ATOM 1845 C LEU A 251 30.792 47.820 481.151 1.00 54.70 A C
ANISOU 1845 C LEU A 251 5238 3527 12020 -320 -2752 -601 A C
ATOM 1846 O LEU A 251 31.910 47.299 481.104 1.00 56.36 A O
ANISOU 1846 O LEU A 251 5206 3669 12537 -309 -2877 -540 A O
ATOM 1847 CB LEU A 251 29.954 49.185 483.052 1.00 69.73 A C
ANISOU 1847 CB LEU A 251 7627 5351 13514 -352 -3105 -856 A C
ATOM 1848 CG LEU A 251 30.787 48.375 484.056 1.00 70.52 A C
ANISOU 1848 CG LEU A 251 7747 5390 13657 -327 -3482 -890 A C
ATOM 1849 CD1 LEU A 251 32.123 49.053 484.267 1.00 74.62 A C
ANISOU 1849 CD1 LEU A 251 8032 5766 14555 -370 -3730 -881 A C
ATOM 1850 CD2 LEU A 251 30.081 48.183 485.391 1.00 70.85 A C
ANISOU 1850 CD2 LEU A 251 8202 5434 13285 -298 -3702 -1036 A C
ATOM 1851 N HIS A 252 29.697 47.186 480.744 1.00 60.08 A N
ANISOU 1851 N HIS A 252 6082 4330 12415 -282 -2519 -584 A N
ATOM 1852 CA HIS A 252 29.777 45.796 480.323 1.00 59.46 A C
ANISOU 1852 CA HIS A 252 5935 4310 12346 -232 -2429 -507 A C
ATOM 1853 C HIS A 252 30.458 45.644 478.965 1.00 57.55 A C
ANISOU 1853 C HIS A 252 5373 4068 12426 -233 -2163 -368 A C
ATOM 1854 O HIS A 252 31.199 44.674 478.749 1.00 61.66 A O
ANISOU 1854 O HIS A 252 5714 4561 13153 -198 -2182 -308 A O
ATOM 1855 CB HIS A 252 28.387 45.177 480.310 1.00 62.05 A C
ANISOU 1855 CB HIS A 252 6546 4757 12275 -189 -2260 -530 A C
ATOM 1856 CG HIS A 252 28.379 43.793 479.765 1.00 61.85 A C
ANISOU 1856 CG HIS A 252 6471 4789 12241 -136 -2132 -447 A C
ATOM 1857 CD2 HIS A 252 27.734 43.259 478.702 1.00 55.00 A C
ANISOU 1857 CD2 HIS A 252 5607 4018 11271 -105 -1816 -369 A C
ATOM 1858 ND1 HIS A 252 29.155 42.786 480.294 1.00 50.89 A N
ANISOU 1858 ND1 HIS A 252 5022 3341 10974 -104 -2352 -438 A N
ATOM 1859 CE1 HIS A 252 28.963 41.682 479.596 1.00 46.20 A C
ANISOU 1859 CE1 HIS A 252 4401 2805 10346 -51 -2156 -361 A C
ATOM 1860 NE2 HIS A 252 28.112 41.943 478.620 1.00 44.21 A N
ANISOU 1860 NE2 HIS A 252 4194 2654 9951 -52 -1831 -322 A N
ATOM 1861 N MET A 253 30.224 46.582 478.036 1.00 50.08 A N
ANISOU 1861 N MET A 253 4362 3137 11529 -268 -1908 -313 A N
ATOM 1862 CA MET A 253 31.027 46.605 476.816 1.00 62.93 A C
ANISOU 1862 CA MET A 253 5695 4731 13485 -275 -1662 -180 A C
ATOM 1863 C MET A 253 32.511 46.595 477.169 1.00 70.14 A C
ANISOU 1863 C MET A 253 6319 5507 14825 -281 -1866 -158 A C
ATOM 1864 O MET A 253 33.303 45.844 476.581 1.00 54.72 A O
ANISOU 1864 O MET A 253 4132 3516 13145 -244 -1752 -70 A O
ATOM 1865 CB MET A 253 30.689 47.835 475.957 1.00 50.75 A C
ANISOU 1865 CB MET A 253 4148 3187 11950 -321 -1427 -125 A C
ATOM 1866 CG MET A 253 29.272 47.902 475.392 1.00 48.05 A C
ANISOU 1866 CG MET A 253 4053 2961 11244 -302 -1204 -119 A C
ATOM 1867 SD MET A 253 28.843 46.590 474.213 1.00 45.95 A S
ANISOU 1867 SD MET A 253 3808 2801 10852 -239 -893 -20 A S
ATOM 1868 CE MET A 253 28.050 47.426 472.850 1.00 45.04 A C
ANISOU 1868 CE MET A 253 3779 2722 10614 -250 -567 82 A C
ATOM 1869 N GLN A 254 32.901 47.397 478.162 1.00 71.38 A N
ANISOU 1869 N GLN A 254 6502 5574 15047 -319 -2174 -241 A N
ATOM 1870 CA GLN A 254 34.299 47.385 478.573 1.00 71.85 A C
ANISOU 1870 CA GLN A 254 6307 5486 15507 -317 -2406 -220 A C
ATOM 1871 C GLN A 254 34.691 46.036 479.165 1.00 59.53 A C
ANISOU 1871 C GLN A 254 4729 3910 13979 -248 -2616 -233 A C
ATOM 1872 O GLN A 254 35.819 45.568 478.954 1.00 61.64 A O
ANISOU 1872 O GLN A 254 4732 4066 14623 -214 -2641 -159 A O
ATOM 1873 CB GLN A 254 34.576 48.518 479.561 1.00 75.17 A C
ANISOU 1873 CB GLN A 254 6803 5805 15954 -375 -2719 -318 A C
ATOM 1874 CG GLN A 254 36.059 48.766 479.807 1.00 65.50 A C
ANISOU 1874 CG GLN A 254 5297 4403 15187 -390 -2923 -279 A C
ATOM 1875 CD GLN A 254 36.850 48.775 478.512 1.00 70.29 A C
ANISOU 1875 CD GLN A 254 5571 4956 16180 -389 -2583 -123 A C
ATOM 1876 NE2 GLN A 254 37.930 47.997 478.467 1.00 68.48 A N
ANISOU 1876 NE2 GLN A 254 5109 4624 16286 -344 -2635 -59 A N
ATOM 1877 OE1 GLN A 254 36.502 49.488 477.567 1.00 67.87 A O
ANISOU 1877 OE1 GLN A 254 5237 4685 15866 -428 -2269 -58 A O
ATOM 1878 N TYR A 255 33.787 45.400 479.921 1.00 60.57 A N
ANISOU 1878 N TYR A 255 5156 4131 13728 -224 -2762 -320 A N
ATOM 1879 CA TYR A 255 34.115 44.095 480.491 1.00 58.05 A C
ANISOU 1879 CA TYR A 255 4846 3788 13424 -160 -2975 -323 A C
ATOM 1880 C TYR A 255 34.462 43.108 479.381 1.00 59.77 A C
ANISOU 1880 C TYR A 255 4826 4015 13868 -109 -2684 -207 A C
ATOM 1881 O TYR A 255 35.495 42.430 479.435 1.00 59.33 A O
ANISOU 1881 O TYR A 255 4564 3838 14141 -60 -2790 -157 A O
ATOM 1882 CB TYR A 255 32.959 43.566 481.353 1.00 60.82 A C
ANISOU 1882 CB TYR A 255 5588 4231 13288 -147 -3106 -420 A C
ATOM 1883 CG TYR A 255 33.356 42.370 482.209 1.00 57.18 A C
ANISOU 1883 CG TYR A 255 5189 3714 12823 -89 -3424 -431 A C
ATOM 1884 CD1 TYR A 255 33.393 41.080 481.707 1.00 56.12 A C
ANISOU 1884 CD1 TYR A 255 4972 3596 12755 -33 -3305 -359 A C
ATOM 1885 CD2 TYR A 255 33.727 42.561 483.528 1.00 59.60 A C
ANISOU 1885 CD2 TYR A 255 5655 3934 13056 -88 -3854 -512 A C
ATOM 1886 CE1 TYR A 255 33.802 40.015 482.508 1.00 76.43 A C
ANISOU 1886 CE1 TYR A 255 7599 6092 15348 21 -3625 -361 A C
ATOM 1887 CE2 TYR A 255 34.125 41.519 484.336 1.00 69.54 A C
ANISOU 1887 CE2 TYR A 255 6996 5129 14297 -32 -4173 -509 A C
ATOM 1888 CZ TYR A 255 34.169 40.245 483.835 1.00 75.35 A C
ANISOU 1888 CZ TYR A 255 7630 5879 15123 22 -4069 -431 A C
ATOM 1889 OH TYR A 255 34.585 39.226 484.685 1.00 76.71 A O
ANISOU 1889 OH TYR A 255 7896 5982 15267 83 -4409 -420 A O
ATOM 1890 N LEU A 256 33.630 43.065 478.334 1.00 54.71 A N
ANISOU 1890 N LEU A 256 4238 3495 13055 -119 -2297 -164 A N
ATOM 1891 CA LEU A 256 33.874 42.176 477.200 1.00 54.10 A C
ANISOU 1891 CA LEU A 256 3977 3430 13148 -74 -1978 -64 A C
ATOM 1892 C LEU A 256 35.137 42.555 476.432 1.00 56.72 A C
ANISOU 1892 C LEU A 256 3952 3623 13974 -63 -1814 37 A C
ATOM 1893 O LEU A 256 35.832 41.681 475.907 1.00 57.70 A O
ANISOU 1893 O LEU A 256 3915 3655 14354 -16 -1669 105 A O
ATOM 1894 CB LEU A 256 32.668 42.187 476.268 1.00 51.12 A C
ANISOU 1894 CB LEU A 256 3811 3198 12412 -81 -1610 -42 A C
ATOM 1895 CG LEU A 256 31.387 41.618 476.875 1.00 49.85 A C
ANISOU 1895 CG LEU A 256 4032 3154 11755 -51 -1684 -117 A C
ATOM 1896 CD1 LEU A 256 30.213 41.854 475.940 1.00 46.15 A C
ANISOU 1896 CD1 LEU A 256 3750 2811 10973 -51 -1350 -90 A C
ATOM 1897 CD2 LEU A 256 31.563 40.128 477.207 1.00 48.57 A C
ANISOU 1897 CD2 LEU A 256 3910 2989 11555 34 -1778 -110 A C
ATOM 1898 N ARG A 257 35.417 43.851 476.291 1.00 58.01 A N
ANISOU 1898 N ARG A 257 4054 3744 14243 -122 -1781 52 A N
ATOM 1899 CA ARG A 257 36.675 44.261 475.679 1.00 61.03 A C
ANISOU 1899 CA ARG A 257 4146 3972 15072 -128 -1634 150 A C
ATOM 1900 C ARG A 257 37.871 43.669 476.418 1.00 64.00 A C
ANISOU 1900 C ARG A 257 4374 4185 15760 -106 -1916 143 A C
ATOM 1901 O ARG A 257 38.769 43.088 475.798 1.00 65.79 A O
ANISOU 1901 O ARG A 257 4397 4321 16280 -93 -1722 225 A O
ATOM 1902 CB ARG A 257 36.768 45.784 475.630 1.00 62.25 A C
ANISOU 1902 CB ARG A 257 4276 4097 15282 -208 -1634 154 A C
ATOM 1903 CG ARG A 257 35.998 46.410 474.509 1.00 60.47 A C
ANISOU 1903 CG ARG A 257 4123 3971 14882 -241 -1252 217 A C
ATOM 1904 CD ARG A 257 36.246 47.903 474.446 1.00 62.24 A C
ANISOU 1904 CD ARG A 257 4300 4125 15222 -323 -1259 235 A C
ATOM 1905 NE ARG A 257 35.066 48.568 473.913 1.00 59.86 A N
ANISOU 1905 NE ARG A 257 4221 3939 14585 -361 -1066 236 A N
ATOM 1906 CZ ARG A 257 34.147 49.156 474.678 1.00 67.41 A C
ANISOU 1906 CZ ARG A 257 5427 4953 15234 -397 -1269 123 A C
ATOM 1907 NH1 ARG A 257 34.297 49.163 476.000 1.00 64.37 A N1+
ANISOU 1907 NH1 ARG A 257 5111 4528 14820 -403 -1662 0 A N1+
ATOM 1908 NH2 ARG A 257 33.083 49.738 474.131 1.00 56.56 A N
ANISOU 1908 NH2 ARG A 257 4253 3660 13578 -421 -1079 135 A N
ATOM 1909 N ASN A 258 37.906 43.824 477.747 1.00 64.88 A N
ANISOU 1909 N ASN A 258 4604 4263 15784 -117 -2368 44 A N
ATOM 1910 CA ASN A 258 39.030 43.316 478.527 1.00 68.05 A C
ANISOU 1910 CA ASN A 258 4890 4511 16454 -107 -2681 35 A C
ATOM 1911 C ASN A 258 39.192 41.811 478.403 1.00 67.60 A C
ANISOU 1911 C ASN A 258 4821 4464 16401 -59 -2629 59 A C
ATOM 1912 O ASN A 258 40.287 41.285 478.617 1.00 77.31 A O
ANISOU 1912 O ASN A 258 5871 5584 17919 -55 -2743 88 A O
ATOM 1913 CB ASN A 258 38.855 43.716 479.990 1.00 68.92 A C
ANISOU 1913 CB ASN A 258 5208 4602 16375 -121 -3176 -82 A C
ATOM 1914 CG ASN A 258 38.860 45.210 480.172 1.00 70.07 A C
ANISOU 1914 CG ASN A 258 5356 4723 16543 -194 -3246 -119 A C
ATOM 1915 ND2 ASN A 258 38.640 45.657 481.400 1.00 92.93 A N
ANISOU 1915 ND2 ASN A 258 8471 7605 19234 -216 -3643 -234 A N
ATOM 1916 OD1 ASN A 258 39.058 45.962 479.217 1.00 70.38 A O
ANISOU 1916 OD1 ASN A 258 5222 4750 16769 -234 -2940 -46 A O
ATOM 1917 N PHE A 259 38.127 41.123 478.050 1.00 67.99 A N
ANISOU 1917 N PHE A 259 5043 4654 16134 -29 -2458 45 A N
ATOM 1918 CA PHE A 259 38.072 39.687 477.891 1.00 63.44 A C
ANISOU 1918 CA PHE A 259 4486 4154 15462 7 -2383 57 A C
ATOM 1919 C PHE A 259 38.436 39.231 476.481 1.00 67.45 A C
ANISOU 1919 C PHE A 259 4800 4710 16118 26 -1894 156 A C
ATOM 1920 O PHE A 259 38.487 38.022 476.230 1.00 69.76 A O
ANISOU 1920 O PHE A 259 5094 5094 16316 99 -1784 174 A O
ATOM 1921 CB PHE A 259 36.657 39.230 478.249 1.00 59.95 A C
ANISOU 1921 CB PHE A 259 4344 3874 14560 29 -2450 -10 A C
ATOM 1922 CG PHE A 259 36.566 37.814 478.725 1.00 67.09 A C
ANISOU 1922 CG PHE A 259 5365 4872 15254 114 -2574 -17 A C
ATOM 1923 CD1 PHE A 259 37.701 37.049 478.928 1.00 65.25 A C
ANISOU 1923 CD1 PHE A 259 4970 4560 15261 152 -2675 19 A C
ATOM 1924 CD2 PHE A 259 35.324 37.241 478.952 1.00 62.79 A C
ANISOU 1924 CD2 PHE A 259 5125 4479 14254 181 -2565 -47 A C
ATOM 1925 CE1 PHE A 259 37.604 35.743 479.346 1.00 71.48 A C
ANISOU 1925 CE1 PHE A 259 5886 5418 15855 248 -2781 24 A C
ATOM 1926 CE2 PHE A 259 35.218 35.938 479.371 1.00 56.67 A C
ANISOU 1926 CE2 PHE A 259 4503 3758 13270 277 -2653 -34 A C
ATOM 1927 CZ PHE A 259 36.357 35.191 479.577 1.00 74.13 A C
ANISOU 1927 CZ PHE A 259 6538 5892 15735 310 -2772 0 A C
ATOM 1928 N GLY A 260 38.669 40.153 475.549 1.00 70.34 A N
ANISOU 1928 N GLY A 260 5031 5023 16673 -8 -1587 225 A N
ATOM 1929 CA GLY A 260 38.932 39.761 474.179 1.00 64.31 A C
ANISOU 1929 CA GLY A 260 4137 4305 15993 22 -1100 321 A C
ATOM 1930 C GLY A 260 37.704 39.391 473.380 1.00 79.73 A C
ANISOU 1930 C GLY A 260 6285 6439 17569 57 -802 322 A C
ATOM 1931 O GLY A 260 37.831 38.781 472.312 1.00 78.66 A O
ANISOU 1931 O GLY A 260 6113 6367 17407 122 -420 384 A O
ATOM 1932 N VAL A 261 36.514 39.747 473.859 1.00 58.05 A N
ANISOU 1932 N VAL A 261 3761 3777 14517 31 -962 252 A N
ATOM 1933 CA VAL A 261 35.253 39.398 473.218 1.00 54.87 A C
ANISOU 1933 CA VAL A 261 3595 3557 13697 91 -726 245 A C
ATOM 1934 C VAL A 261 34.762 40.607 472.425 1.00 63.37 A C
ANISOU 1934 C VAL A 261 4673 4624 14781 32 -485 294 A C
ATOM 1935 O VAL A 261 34.751 41.733 472.939 1.00 54.55 A O
ANISOU 1935 O VAL A 261 3505 3461 13759 -20 -674 272 A O
ATOM 1936 CB VAL A 261 34.211 38.974 474.265 1.00 52.56 A C
ANISOU 1936 CB VAL A 261 3612 3367 12992 126 -1033 146 A C
ATOM 1937 CG1 VAL A 261 32.949 38.499 473.600 1.00 49.65 A C
ANISOU 1937 CG1 VAL A 261 3560 3149 12156 185 -784 142 A C
ATOM 1938 CG2 VAL A 261 34.774 37.944 475.192 1.00 53.80 A C
ANISOU 1938 CG2 VAL A 261 3753 3500 13187 175 -1325 113 A C
ATOM 1939 N SER A 262 34.388 40.388 471.164 1.00 59.00 A N
ANISOU 1939 N SER A 262 4211 4137 14068 90 -72 362 A N
ATOM 1940 CA SER A 262 33.868 41.452 470.318 1.00 52.67 A C
ANISOU 1940 CA SER A 262 3485 3329 13197 39 177 425 A C
ATOM 1941 C SER A 262 32.358 41.368 470.113 1.00 66.51 A C
ANISOU 1941 C SER A 262 5645 5238 14387 57 212 379 A C
ATOM 1942 O SER A 262 31.727 42.373 469.765 1.00 72.82 A O
ANISOU 1942 O SER A 262 6565 6069 15032 -7 286 404 A O
ATOM 1943 CB SER A 262 34.573 41.430 468.957 1.00 57.29 A C
ANISOU 1943 CB SER A 262 3896 3845 14029 84 638 555 A C
ATOM 1944 OG SER A 262 35.886 41.967 469.030 1.00 57.88 A O
ANISOU 1944 OG SER A 262 3688 3776 14528 30 637 616 A O
ATOM 1945 N ALA A 263 31.764 40.201 470.315 1.00 59.81 A N
ANISOU 1945 N ALA A 263 5000 4491 13234 142 155 316 A N
ATOM 1946 CA ALA A 263 30.324 40.061 470.219 1.00 45.15 A C
ANISOU 1946 CA ALA A 263 3492 2765 10899 152 154 271 A C
ATOM 1947 C ALA A 263 29.918 38.929 471.132 1.00 43.98 A C
ANISOU 1947 C ALA A 263 3485 2689 10535 203 -79 185 A C
ATOM 1948 O ALA A 263 30.737 38.078 471.473 1.00 45.23 A O
ANISOU 1948 O ALA A 263 3508 2810 10869 258 -157 178 A O
ATOM 1949 CB ALA A 263 29.864 39.792 468.788 1.00 54.46 A C
ANISOU 1949 CB ALA A 263 4817 3972 11902 211 516 336 A C
ATOM 1950 N SER A 264 28.690 38.988 471.620 1.00 41.88 A N
ANISOU 1950 N SER A 264 3478 2517 9916 180 -204 126 A N
ATOM 1951 CA SER A 264 28.201 37.907 472.457 1.00 53.64 A C
ANISOU 1951 CA SER A 264 5129 4063 11187 223 -390 64 A C
ATOM 1952 C SER A 264 26.710 37.737 472.230 1.00 50.19 A C
ANISOU 1952 C SER A 264 4975 3732 10363 220 -327 38 A C
ATOM 1953 O SER A 264 26.031 38.605 471.668 1.00 50.55 A O
ANISOU 1953 O SER A 264 5090 3810 10308 180 -214 56 A O
ATOM 1954 CB SER A 264 28.477 38.126 473.949 1.00 63.89 A C
ANISOU 1954 CB SER A 264 6404 5320 12549 187 -740 4 A C
ATOM 1955 OG SER A 264 27.831 39.279 474.446 1.00 66.54 A O
ANISOU 1955 OG SER A 264 6834 5674 12773 113 -839 -39 A O
ATOM 1956 N THR A 265 26.224 36.584 472.677 1.00 46.00 A N
ANISOU 1956 N THR A 265 4595 3242 9642 262 -409 5 A N
ATOM 1957 CA THR A 265 24.816 36.252 472.784 1.00 37.78 A C
ANISOU 1957 CA THR A 265 3797 2282 8277 249 -411 -24 A C
ATOM 1958 C THR A 265 24.640 35.507 474.093 1.00 39.04 A C
ANISOU 1958 C THR A 265 4058 2435 8340 256 -639 -62 A C
ATOM 1959 O THR A 265 25.503 34.719 474.459 1.00 37.16 A O
ANISOU 1959 O THR A 265 3747 2144 8229 304 -733 -53 A O
ATOM 1960 CB THR A 265 24.386 35.333 471.640 1.00 49.28 A C
ANISOU 1960 CB THR A 265 5356 3762 9608 298 -210 -5 A C
ATOM 1961 CG2 THR A 265 22.874 35.153 471.630 1.00 55.55 A C
ANISOU 1961 CG2 THR A 265 6361 4623 10121 266 -216 -29 A C
ATOM 1962 OG1 THR A 265 24.809 35.882 470.390 1.00 60.68 A O
ANISOU 1962 OG1 THR A 265 6715 5175 11164 314 16 42 A O
ATOM 1963 N SER A 266 23.559 35.743 474.824 1.00 38.65 A N
ANISOU 1963 N SER A 266 4178 2426 8081 215 -725 -98 A N
ATOM 1964 CA SER A 266 23.315 34.858 475.956 1.00 35.16 A C
ANISOU 1964 CA SER A 266 3878 1960 7521 228 -897 -114 A C
ATOM 1965 C SER A 266 21.838 34.501 476.002 1.00 33.82 A C
ANISOU 1965 C SER A 266 3905 1846 7099 198 -825 -123 A C
ATOM 1966 O SER A 266 20.981 35.291 475.599 1.00 32.93 A O
ANISOU 1966 O SER A 266 3816 1784 6912 161 -725 -137 A O
ATOM 1967 CB SER A 266 23.756 35.455 477.293 1.00 37.38 A C
ANISOU 1967 CB SER A 266 4172 2177 7854 209 -1149 -154 A C
ATOM 1968 OG SER A 266 23.332 36.786 477.409 1.00 44.87 A O
ANISOU 1968 OG SER A 266 5124 3142 8781 157 -1138 -198 A O
ATOM 1969 N ILE A 267 21.557 33.280 476.458 1.00 40.51 A N
ANISOU 1969 N ILE A 267 4880 2669 7844 214 -877 -105 A N
ATOM 1970 CA ILE A 267 20.199 32.763 476.603 1.00 35.39 A C
ANISOU 1970 CA ILE A 267 4398 2079 6968 171 -811 -100 A C
ATOM 1971 C ILE A 267 19.991 32.345 478.050 1.00 33.82 A C
ANISOU 1971 C ILE A 267 4358 1866 6624 157 -958 -93 A C
ATOM 1972 O ILE A 267 20.878 31.738 478.661 1.00 42.00 A O
ANISOU 1972 O ILE A 267 5411 2827 7720 200 -1112 -69 A O
ATOM 1973 CB ILE A 267 19.918 31.582 475.649 1.00 32.74 A C
ANISOU 1973 CB ILE A 267 4095 1734 6610 185 -697 -74 A C
ATOM 1974 CG1 ILE A 267 20.152 31.997 474.217 1.00 32.37 A C
ANISOU 1974 CG1 ILE A 267 3939 1709 6650 206 -544 -81 A C
ATOM 1975 CG2 ILE A 267 18.494 31.130 475.758 1.00 32.11 A C
ANISOU 1975 CG2 ILE A 267 4150 1712 6337 119 -638 -66 A C
ATOM 1976 CD1 ILE A 267 20.586 30.886 473.361 1.00 32.84 A C
ANISOU 1976 CD1 ILE A 267 4008 1733 6737 257 -464 -74 A C
ATOM 1977 N GLY A 268 18.824 32.682 478.598 1.00 33.44 A N
ANISOU 1977 N GLY A 268 4430 1886 6390 105 -906 -107 A N
ATOM 1978 CA GLY A 268 18.489 32.263 479.949 1.00 34.41 A C
ANISOU 1978 CA GLY A 268 4745 2001 6328 90 -995 -90 A C
ATOM 1979 C GLY A 268 17.964 30.835 479.977 1.00 39.88 A C
ANISOU 1979 C GLY A 268 5550 2676 6928 69 -946 -19 A C
ATOM 1980 O GLY A 268 17.253 30.387 479.076 1.00 39.08 A O
ANISOU 1980 O GLY A 268 5407 2602 6839 35 -808 -5 A O
ATOM 1981 N ILE A 269 18.349 30.111 481.017 1.00 43.15 A N
ANISOU 1981 N ILE A 269 6115 3028 7252 86 -1082 29 A N
ATOM 1982 CA ILE A 269 17.868 28.758 481.250 1.00 36.45 A C
ANISOU 1982 CA ILE A 269 5405 2136 6307 59 -1049 112 A C
ATOM 1983 C ILE A 269 16.870 28.833 482.390 1.00 37.27 A C
ANISOU 1983 C ILE A 269 5711 2285 6167 2 -989 143 A C
ATOM 1984 O ILE A 269 17.248 29.042 483.548 1.00 38.66 A O
ANISOU 1984 O ILE A 269 6046 2437 6206 28 -1120 151 A O
ATOM 1985 CB ILE A 269 19.000 27.798 481.602 1.00 37.74 A C
ANISOU 1985 CB ILE A 269 5614 2179 6546 129 -1236 168 A C
ATOM 1986 CG1 ILE A 269 20.114 27.905 480.576 1.00 37.34 A C
ANISOU 1986 CG1 ILE A 269 5341 2085 6761 202 -1274 128 A C
ATOM 1987 CG2 ILE A 269 18.436 26.381 481.661 1.00 40.75 A C
ANISOU 1987 CG2 ILE A 269 6133 2496 6854 94 -1180 257 A C
ATOM 1988 CD1 ILE A 269 21.358 27.152 480.998 1.00 41.65 A C
ANISOU 1988 CD1 ILE A 269 5884 2506 7433 293 -1481 175 A C
ATOM 1989 N PHE A 270 15.605 28.615 482.093 1.00 47.41 A N
ANISOU 1989 N PHE A 270 6997 3624 7394 -74 -793 164 A N
ATOM 1990 CA PHE A 270 14.576 28.802 483.090 1.00 37.74 A C
ANISOU 1990 CA PHE A 270 5926 2449 5964 -125 -674 191 A C
ATOM 1991 C PHE A 270 14.047 27.460 483.550 1.00 49.92 A C
ANISOU 1991 C PHE A 270 7625 3932 7412 -186 -615 311 A C
ATOM 1992 O PHE A 270 13.693 26.601 482.731 1.00 45.81 A O
ANISOU 1992 O PHE A 270 7026 3375 7006 -235 -558 348 A O
ATOM 1993 CB PHE A 270 13.465 29.683 482.550 1.00 36.77 A C
ANISOU 1993 CB PHE A 270 5665 2428 5877 -167 -484 135 A C
ATOM 1994 CG PHE A 270 13.841 31.110 482.520 1.00 46.11 A C
ANISOU 1994 CG PHE A 270 6771 3656 7094 -111 -527 32 A C
ATOM 1995 CD1 PHE A 270 13.677 31.899 483.642 1.00 42.32 A C
ANISOU 1995 CD1 PHE A 270 6435 3198 6447 -89 -516 -12 A C
ATOM 1996 CD2 PHE A 270 14.430 31.656 481.397 1.00 46.95 A C
ANISOU 1996 CD2 PHE A 270 6684 3764 7391 -79 -579 -21 A C
ATOM 1997 CE1 PHE A 270 14.049 33.211 483.622 1.00 37.10 A C
ANISOU 1997 CE1 PHE A 270 5713 2551 5832 -41 -571 -115 A C
ATOM 1998 CE2 PHE A 270 14.816 32.974 481.376 1.00 34.58 A C
ANISOU 1998 CE2 PHE A 270 5048 2215 5877 -38 -622 -104 A C
ATOM 1999 CZ PHE A 270 14.625 33.747 482.488 1.00 35.67 A C
ANISOU 1999 CZ PHE A 270 5318 2364 5870 -21 -629 -155 A C
ATOM 2000 N ASN A 271 14.032 27.292 484.864 1.00 52.72 A N
ANISOU 2000 N ASN A 271 8220 4262 7547 -183 -640 371 A N
ATOM 2001 CA ASN A 271 13.304 26.237 485.545 1.00 42.36 A C
ANISOU 2001 CA ASN A 271 7095 2903 6095 -255 -526 502 A C
ATOM 2002 C ASN A 271 11.991 26.882 485.983 1.00 42.89 A C
ANISOU 2002 C ASN A 271 7178 3072 6046 -316 -264 492 A C
ATOM 2003 O ASN A 271 11.947 27.661 486.943 1.00 44.00 A O
ANISOU 2003 O ASN A 271 7473 3256 5988 -277 -236 456 A O
ATOM 2004 CB ASN A 271 14.114 25.694 486.712 1.00 63.92 A C
ANISOU 2004 CB ASN A 271 10106 5542 8638 -204 -708 586 A C
ATOM 2005 CG ASN A 271 13.428 24.535 487.398 1.00 66.17 A C
ANISOU 2005 CG ASN A 271 10607 5756 8778 -281 -587 748 A C
ATOM 2006 ND2 ASN A 271 14.167 23.833 488.245 1.00 65.86 A N
ANISOU 2006 ND2 ASN A 271 10815 5609 8599 -235 -770 849 A N
ATOM 2007 OD1 ASN A 271 12.241 24.280 487.178 1.00 63.99 A O
ANISOU 2007 OD1 ASN A 271 10272 5514 8527 -384 -338 790 A O
ATOM 2008 N GLU A 272 10.937 26.611 485.222 1.00 52.72 A N
ANISOU 2008 N GLU A 272 8250 4349 7434 -405 -81 510 A N
ATOM 2009 CA GLU A 272 9.663 27.315 485.351 1.00 61.64 A C
ANISOU 2009 CA GLU A 272 9292 5577 8551 -453 171 487 A C
ATOM 2010 C GLU A 272 10.018 28.787 485.192 1.00 61.28 A C
ANISOU 2010 C GLU A 272 9157 5611 8518 -360 118 342 A C
ATOM 2011 O GLU A 272 10.544 29.155 484.124 1.00 52.03 A O
ANISOU 2011 O GLU A 272 7798 4447 7525 -327 -8 269 A O
ATOM 2012 CB GLU A 272 8.952 26.924 486.650 1.00 70.75 A C
ANISOU 2012 CB GLU A 272 10679 6722 9481 -501 370 596 A C
ATOM 2013 CG GLU A 272 8.723 25.403 486.840 1.00 71.87 A C
ANISOU 2013 CG GLU A 272 10933 6753 9620 -600 404 762 A C
ATOM 2014 CD GLU A 272 7.994 24.735 485.672 1.00 77.10 A C
ANISOU 2014 CD GLU A 272 11342 7390 10562 -709 461 784 A C
ATOM 2015 OE1 GLU A 272 6.957 25.257 485.198 1.00 82.96 A O
ANISOU 2015 OE1 GLU A 272 11864 8214 11443 -761 628 744 A O
ATOM 2016 OE2 GLU A 272 8.481 23.681 485.218 1.00 74.90 A O1-
ANISOU 2016 OE2 GLU A 272 11090 6998 10372 -738 319 836 A O1-
ATOM 2017 N ASP A 273 9.795 29.640 486.192 1.00 62.14 A N
ANISOU 2017 N ASP A 273 9407 5765 8439 -315 210 298 A N
ATOM 2018 CA ASP A 273 10.123 31.059 486.080 1.00 57.40 A C
ANISOU 2018 CA ASP A 273 8736 5213 7860 -231 153 155 A C
ATOM 2019 C ASP A 273 11.457 31.416 486.716 1.00 60.64 A C
ANISOU 2019 C ASP A 273 9327 5570 8142 -152 -104 99 A C
ATOM 2020 O ASP A 273 11.843 32.583 486.673 1.00 56.57 A O
ANISOU 2020 O ASP A 273 8768 5071 7656 -92 -180 -22 A O
ATOM 2021 CB ASP A 273 9.023 31.922 486.707 1.00 60.68 A C
ANISOU 2021 CB ASP A 273 9179 5697 8180 -218 413 108 A C
ATOM 2022 CG ASP A 273 7.663 31.649 486.110 1.00 79.87 A C
ANISOU 2022 CG ASP A 273 11386 8178 10783 -295 657 164 A C
ATOM 2023 OD1 ASP A 273 7.587 31.314 484.906 1.00 76.16 A O1-
ANISOU 2023 OD1 ASP A 273 10686 7708 10543 -340 584 179 A O1-
ATOM 2024 OD2 ASP A 273 6.665 31.773 486.851 1.00 96.04 A O1-
ANISOU 2024 OD2 ASP A 273 13492 10261 12739 -309 922 191 A O1-
ATOM 2025 N GLU A 274 12.170 30.452 487.302 1.00 67.09 A N
ANISOU 2025 N GLU A 274 10342 6311 8840 -152 -257 186 A N
ATOM 2026 CA GLU A 274 13.427 30.733 487.986 1.00 60.43 A C
ANISOU 2026 CA GLU A 274 9669 5407 7886 -78 -540 142 A C
ATOM 2027 C GLU A 274 14.600 30.651 487.018 1.00 56.15 A C
ANISOU 2027 C GLU A 274 8914 4815 7606 -46 -779 115 A C
ATOM 2028 O GLU A 274 14.737 29.667 486.280 1.00 45.11 A O
ANISOU 2028 O GLU A 274 7403 3379 6356 -72 -790 192 A O
ATOM 2029 CB GLU A 274 13.648 29.748 489.127 1.00 66.39 A C
ANISOU 2029 CB GLU A 274 10751 6092 8382 -81 -613 262 A C
ATOM 2030 CG GLU A 274 12.579 29.778 490.190 1.00 88.82 A C
ANISOU 2030 CG GLU A 274 13849 8972 10929 -108 -351 305 A C
ATOM 2031 CD GLU A 274 13.005 29.018 491.426 1.00105.23 A C
ANISOU 2031 CD GLU A 274 16314 10971 12698 -91 -472 416 A C
ATOM 2032 OE1 GLU A 274 14.232 28.907 491.652 1.00103.96 A O
ANISOU 2032 OE1 GLU A 274 16239 10735 12527 -31 -817 406 A O
ATOM 2033 OE2 GLU A 274 12.125 28.498 492.145 1.00112.21 A O1-
ANISOU 2033 OE2 GLU A 274 17408 11862 13366 -139 -225 525 A O1-
ATOM 2034 N LEU A 275 15.474 31.659 487.069 1.00 56.89 A N
ANISOU 2034 N LEU A 275 8964 4895 7758 12 -967 4 A N
ATOM 2035 CA LEU A 275 16.689 31.669 486.265 1.00 49.06 A C
ANISOU 2035 CA LEU A 275 7766 3849 7026 47 -1180 -18 A C
ATOM 2036 C LEU A 275 17.708 30.724 486.899 1.00 79.90 A C
ANISOU 2036 C LEU A 275 11815 7655 10889 85 -1438 61 A C
ATOM 2037 O LEU A 275 18.237 30.983 487.989 1.00 71.55 A O
ANISOU 2037 O LEU A 275 10970 6553 9662 121 -1641 41 A O
ATOM 2038 CB LEU A 275 17.255 33.076 486.140 1.00 41.18 A C
ANISOU 2038 CB LEU A 275 6658 2852 6136 79 -1287 -149 A C
ATOM 2039 CG LEU A 275 18.473 33.161 485.210 1.00 40.93 A C
ANISOU 2039 CG LEU A 275 6370 2767 6415 107 -1454 -162 A C
ATOM 2040 CD1 LEU A 275 18.088 32.811 483.778 1.00 42.61 A C
ANISOU 2040 CD1 LEU A 275 6349 3021 6820 84 -1263 -127 A C
ATOM 2041 CD2 LEU A 275 19.188 34.510 485.278 1.00 40.60 A C
ANISOU 2041 CD2 LEU A 275 6241 2694 6493 125 -1601 -277 A C
ATOM 2042 N TRP A 276 17.944 29.605 486.233 1.00 42.41 A N
ANISOU 2042 N TRP A 276 6969 2859 6285 84 -1438 151 A N
ATOM 2043 CA TRP A 276 18.832 28.578 486.726 1.00 43.94 A C
ANISOU 2043 CA TRP A 276 7278 2943 6475 131 -1665 243 A C
ATOM 2044 C TRP A 276 20.273 28.831 486.309 1.00 52.45 A C
ANISOU 2044 C TRP A 276 8151 3953 7825 205 -1920 198 A C
ATOM 2045 O TRP A 276 21.208 28.504 487.054 1.00 45.91 A O
ANISOU 2045 O TRP A 276 7424 3033 6985 263 -2202 236 A O
ATOM 2046 CB TRP A 276 18.335 27.230 486.202 1.00 43.53 A C
ANISOU 2046 CB TRP A 276 7221 2851 6465 96 -1526 355 A C
ATOM 2047 CG TRP A 276 19.092 26.050 486.679 1.00 45.23 A C
ANISOU 2047 CG TRP A 276 7570 2935 6680 148 -1728 468 A C
ATOM 2048 CD1 TRP A 276 18.815 25.299 487.775 1.00 47.32 A C
ANISOU 2048 CD1 TRP A 276 8143 3142 6694 135 -1771 589 A C
ATOM 2049 CD2 TRP A 276 20.248 25.464 486.069 1.00 45.27 A C
ANISOU 2049 CD2 TRP A 276 7407 2838 6957 230 -1904 483 A C
ATOM 2050 CE2 TRP A 276 20.615 24.365 486.850 1.00 47.39 A C
ANISOU 2050 CE2 TRP A 276 7888 2983 7137 269 -2071 611 A C
ATOM 2051 CE3 TRP A 276 21.005 25.764 484.933 1.00 57.73 A C
ANISOU 2051 CE3 TRP A 276 8678 4410 8845 279 -1916 405 A C
ATOM 2052 NE1 TRP A 276 19.720 24.280 487.884 1.00 48.60 A N
ANISOU 2052 NE1 TRP A 276 8344 3165 6958 205 -1989 681 A N
ATOM 2053 CZ2 TRP A 276 21.707 23.565 486.538 1.00 52.43 A C
ANISOU 2053 CZ2 TRP A 276 8422 3489 8012 367 -2263 656 A C
ATOM 2054 CZ3 TRP A 276 22.083 24.965 484.623 1.00 44.85 A C
ANISOU 2054 CZ3 TRP A 276 6944 2656 7441 372 -2074 446 A C
ATOM 2055 CH2 TRP A 276 22.425 23.883 485.419 1.00 46.93 A C
ANISOU 2055 CH2 TRP A 276 7403 2794 7635 420 -2252 566 A C
ATOM 2056 N GLY A 277 20.455 29.404 485.129 1.00 45.26 A N
ANISOU 2056 N GLY A 277 6952 3079 7164 203 -1821 127 A N
ATOM 2057 CA GLY A 277 21.771 29.627 484.572 1.00 51.27 A C
ANISOU 2057 CA GLY A 277 7474 3776 8229 266 -1992 95 A C
ATOM 2058 C GLY A 277 21.654 30.398 483.276 1.00 53.79 A C
ANISOU 2058 C GLY A 277 7530 4159 8751 245 -1800 26 A C
ATOM 2059 O GLY A 277 20.603 30.963 482.959 1.00 57.12 A O
ANISOU 2059 O GLY A 277 7965 4672 9067 188 -1593 -12 A O
ATOM 2060 N ILE A 278 22.750 30.420 482.519 1.00 40.85 A N
ANISOU 2060 N ILE A 278 5647 2462 7411 297 -1864 17 A N
ATOM 2061 CA ILE A 278 22.783 31.114 481.238 1.00 42.70 A C
ANISOU 2061 CA ILE A 278 5646 2740 7836 285 -1678 -30 A C
ATOM 2062 C ILE A 278 23.611 30.310 480.245 1.00 42.81 A C
ANISOU 2062 C ILE A 278 5476 2688 8100 353 -1628 7 A C
ATOM 2063 O ILE A 278 24.565 29.621 480.622 1.00 55.13 A O
ANISOU 2063 O ILE A 278 7000 4151 9795 423 -1806 48 A O
ATOM 2064 CB ILE A 278 23.351 32.547 481.431 1.00 41.90 A C
ANISOU 2064 CB ILE A 278 5425 2637 7859 268 -1783 -105 A C
ATOM 2065 CG1 ILE A 278 22.298 33.434 482.083 1.00 45.22 A C
ANISOU 2065 CG1 ILE A 278 6023 3131 8030 208 -1735 -164 A C
ATOM 2066 CG2 ILE A 278 23.843 33.185 480.128 1.00 38.48 A C
ANISOU 2066 CG2 ILE A 278 4718 2205 7696 271 -1635 -123 A C
ATOM 2067 CD1 ILE A 278 22.870 34.417 483.037 1.00 53.60 A C
ANISOU 2067 CD1 ILE A 278 7127 4143 9095 202 -1968 -237 A C
ATOM 2068 N VAL A 279 23.257 30.408 478.966 1.00 37.57 A N
ANISOU 2068 N VAL A 279 4705 2071 7500 342 -1388 -9 A N
ATOM 2069 CA VAL A 279 24.131 29.971 477.885 1.00 37.90 A C
ANISOU 2069 CA VAL A 279 4551 2118 7732 401 -1273 1 A C
ATOM 2070 C VAL A 279 24.806 31.209 477.303 1.00 41.41 A C
ANISOU 2070 C VAL A 279 4772 2590 8371 392 -1218 -31 A C
ATOM 2071 O VAL A 279 24.156 32.022 476.638 1.00 44.84 A O
ANISOU 2071 O VAL A 279 5198 3091 8749 343 -1060 -56 A O
ATOM 2072 CB VAL A 279 23.363 29.194 476.812 1.00 36.82 A C
ANISOU 2072 CB VAL A 279 4482 2022 7488 396 -1045 4 A C
ATOM 2073 CG1 VAL A 279 24.312 28.796 475.694 1.00 37.51 A C
ANISOU 2073 CG1 VAL A 279 4404 2095 7754 471 -911 0 A C
ATOM 2074 CG2 VAL A 279 22.707 27.948 477.422 1.00 38.21 A C
ANISOU 2074 CG2 VAL A 279 4869 2148 7501 387 -1103 45 A C
ATOM 2075 N ALA A 280 26.109 31.369 477.544 1.00 44.96 A N
ANISOU 2075 N ALA A 280 5032 2979 9074 435 -1355 -23 A N
ATOM 2076 CA ALA A 280 26.861 32.524 477.067 1.00 40.14 A C
ANISOU 2076 CA ALA A 280 4186 2364 8702 413 -1314 -40 A C
ATOM 2077 C ALA A 280 27.699 32.147 475.852 1.00 46.78 A C
ANISOU 2077 C ALA A 280 4820 3198 9756 470 -1101 -12 A C
ATOM 2078 O ALA A 280 28.390 31.126 475.857 1.00 49.40 A O
ANISOU 2078 O ALA A 280 5094 3484 10191 545 -1130 12 A O
ATOM 2079 CB ALA A 280 27.742 33.098 478.170 1.00 41.93 A C
ANISOU 2079 CB ALA A 280 4318 2504 9111 404 -1625 -55 A C
ATOM 2080 N CYS A 281 27.638 32.976 474.818 1.00 40.32 A N
ANISOU 2080 N CYS A 281 3906 2414 8998 440 -878 -11 A N
ATOM 2081 CA CYS A 281 28.360 32.775 473.573 1.00 41.20 A C
ANISOU 2081 CA CYS A 281 3854 2509 9292 493 -625 18 A C
ATOM 2082 C CYS A 281 29.196 34.022 473.320 1.00 59.02 A C
ANISOU 2082 C CYS A 281 5859 4722 11845 449 -586 40 A C
ATOM 2083 O CYS A 281 28.646 35.117 473.160 1.00 49.48 A O
ANISOU 2083 O CYS A 281 4686 3541 10573 377 -544 35 A O
ATOM 2084 CB CYS A 281 27.395 32.533 472.411 1.00 39.73 A C
ANISOU 2084 CB CYS A 281 3840 2382 8874 500 -362 12 A C
ATOM 2085 SG CYS A 281 26.086 31.328 472.730 1.00 38.21 A S
ANISOU 2085 SG CYS A 281 3956 2231 8332 504 -421 -17 A S
ATOM 2086 N HIS A 282 30.516 33.855 473.293 1.00 60.85 A N
ANISOU 2086 N HIS A 282 5829 4876 12417 487 -601 69 A N
ATOM 2087 CA HIS A 282 31.453 34.918 472.974 1.00 46.27 A C
ANISOU 2087 CA HIS A 282 3697 2959 10925 439 -538 105 A C
ATOM 2088 C HIS A 282 32.119 34.609 471.642 1.00 47.59 A C
ANISOU 2088 C HIS A 282 3720 3104 11259 502 -175 158 A C
ATOM 2089 O HIS A 282 32.361 33.440 471.313 1.00 48.19 A O
ANISOU 2089 O HIS A 282 3829 3185 11297 597 -78 154 A O
ATOM 2090 CB HIS A 282 32.504 35.063 474.067 1.00 49.87 A C
ANISOU 2090 CB HIS A 282 3936 3321 11691 416 -861 99 A C
ATOM 2091 CG HIS A 282 31.926 35.318 475.425 1.00 64.50 A C
ANISOU 2091 CG HIS A 282 5966 5174 13365 373 -1226 42 A C
ATOM 2092 CD2 HIS A 282 30.660 35.603 475.815 1.00 45.41 A C
ANISOU 2092 CD2 HIS A 282 3838 2828 10589 338 -1274 -1 A C
ATOM 2093 ND1 HIS A 282 32.676 35.240 476.582 1.00 61.36 A N
ANISOU 2093 ND1 HIS A 282 5475 4689 13149 367 -1594 23 A N
ATOM 2094 CE1 HIS A 282 31.902 35.504 477.622 1.00 52.98 A C
ANISOU 2094 CE1 HIS A 282 4659 3636 11834 339 -1847 -30 A C
ATOM 2095 NE2 HIS A 282 30.674 35.727 477.183 1.00 46.05 A N
ANISOU 2095 NE2 HIS A 282 4009 2858 10631 318 -1639 -46 A N
ATOM 2096 N HIS A 283 32.392 35.663 470.874 1.00 48.23 A N
ANISOU 2096 N HIS A 283 3663 3148 11516 454 37 210 A N
ATOM 2097 CA HIS A 283 33.102 35.585 469.602 1.00 67.32 A C
ANISOU 2097 CA HIS A 283 5936 5525 14118 508 420 276 A C
ATOM 2098 C HIS A 283 34.224 36.616 469.599 1.00 67.92 A C
ANISOU 2098 C HIS A 283 5668 5490 14648 430 452 345 A C
ATOM 2099 O HIS A 283 34.108 37.694 470.189 1.00 73.62 A O
ANISOU 2099 O HIS A 283 6327 6171 15473 327 260 343 A O
ATOM 2100 CB HIS A 283 32.171 35.843 468.394 1.00 54.98 A C
ANISOU 2100 CB HIS A 283 4607 4008 12274 531 734 297 A C
ATOM 2101 CG HIS A 283 32.660 35.254 467.103 1.00 57.21 A C
ANISOU 2101 CG HIS A 283 4879 4268 12590 635 1132 335 A C
ATOM 2102 CD2 HIS A 283 32.894 35.823 465.896 1.00 68.53 A C
ANISOU 2102 CD2 HIS A 283 6287 5660 14091 657 1512 413 A C
ATOM 2103 ND1 HIS A 283 33.015 33.928 466.970 1.00 60.91 A N
ANISOU 2103 ND1 HIS A 283 5380 4744 13019 742 1182 293 A N
ATOM 2104 CE1 HIS A 283 33.405 33.697 465.729 1.00 52.82 A C
ANISOU 2104 CE1 HIS A 283 4365 3691 12012 826 1576 327 A C
ATOM 2105 NE2 HIS A 283 33.352 34.833 465.058 1.00 78.76 A N
ANISOU 2105 NE2 HIS A 283 7618 6949 15357 777 1792 405 A N
ATOM 2106 N THR A 284 35.309 36.290 468.919 1.00 72.03 A N
ANISOU 2106 N THR A 284 5976 5949 15443 474 702 403 A N
ATOM 2107 CA THR A 284 36.488 37.149 468.949 1.00 77.71 A C
ANISOU 2107 CA THR A 284 6363 6538 16625 386 728 477 A C
ATOM 2108 C THR A 284 36.468 38.249 467.879 1.00 72.14 A C
ANISOU 2108 C THR A 284 5615 5788 16009 338 1085 576 A C
ATOM 2109 O THR A 284 37.404 39.053 467.818 1.00 67.34 A O
ANISOU 2109 O THR A 284 4767 5049 15771 259 1134 651 A O
ATOM 2110 CB THR A 284 37.751 36.274 468.829 1.00 72.56 A C
ANISOU 2110 CB THR A 284 5504 5820 16247 451 810 501 A C
ATOM 2111 CG2 THR A 284 37.802 35.571 467.476 1.00 61.89 A C
ANISOU 2111 CG2 THR A 284 4239 4508 14768 574 1278 535 A C
ATOM 2112 OG1 THR A 284 38.926 37.074 469.024 1.00 83.71 A O
ANISOU 2112 OG1 THR A 284 6612 7078 18116 362 768 567 A O
ATOM 2113 N LYS A 285 35.434 38.306 467.048 1.00 56.62 A N
ANISOU 2113 N LYS A 285 3904 3905 13704 391 1320 583 A N
ATOM 2114 CA LYS A 285 35.185 39.418 466.146 1.00 68.52 A C
ANISOU 2114 CA LYS A 285 5424 5374 15236 351 1612 681 A C
ATOM 2115 C LYS A 285 33.679 39.633 466.104 1.00 69.93 A C
ANISOU 2115 C LYS A 285 5978 5643 14949 349 1520 632 A C
ATOM 2116 O LYS A 285 32.913 38.745 466.495 1.00 55.24 A O
ANISOU 2116 O LYS A 285 4346 3864 12781 410 1346 534 A O
ATOM 2117 CB LYS A 285 35.724 39.179 464.726 1.00 67.55 A C
ANISOU 2117 CB LYS A 285 5295 5236 15135 428 2129 777 A C
ATOM 2118 CG LYS A 285 35.339 37.873 464.077 1.00 82.24 A C
ANISOU 2118 CG LYS A 285 7406 7181 16662 582 2313 714 A C
ATOM 2119 CD LYS A 285 36.266 37.552 462.894 1.00 94.72 A C
ANISOU 2119 CD LYS A 285 8922 8720 18350 656 2787 794 A C
ATOM 2120 CE LYS A 285 35.929 36.194 462.269 1.00 95.07 A C
ANISOU 2120 CE LYS A 285 9230 8829 18062 817 2954 708 A C
ATOM 2121 NZ LYS A 285 35.942 35.083 463.272 1.00 94.53 A N1+
ANISOU 2121 NZ LYS A 285 9147 8795 17976 853 2592 590 A N1+
ATOM 2122 N PRO A 286 33.220 40.793 465.623 1.00 70.21 A N
ANISOU 2122 N PRO A 286 6114 5678 14884 250 1623 704 A N
ATOM 2123 CA PRO A 286 31.773 41.029 465.564 1.00 61.25 A C
ANISOU 2123 CA PRO A 286 5348 4645 13279 225 1514 663 A C
ATOM 2124 C PRO A 286 31.075 39.907 464.813 1.00 52.91 A C
ANISOU 2124 C PRO A 286 4585 3692 11826 341 1668 621 A C
ATOM 2125 O PRO A 286 31.678 39.212 463.991 1.00 56.60 A O
ANISOU 2125 O PRO A 286 5025 4146 12334 437 1964 650 A O
ATOM 2126 CB PRO A 286 31.654 42.367 464.825 1.00 67.25 A C
ANISOU 2126 CB PRO A 286 6137 5359 14056 132 1706 786 A C
ATOM 2127 CG PRO A 286 33.059 42.737 464.396 1.00 54.67 A C
ANISOU 2127 CG PRO A 286 4202 3644 12926 106 1969 901 A C
ATOM 2128 CD PRO A 286 33.978 42.011 465.304 1.00 55.61 A C
ANISOU 2128 CD PRO A 286 4023 3717 13391 142 1779 827 A C
ATOM 2129 N ARG A 287 29.802 39.713 465.136 1.00 46.69 A N
ANISOU 2129 N ARG A 287 4073 2998 10668 333 1459 545 A N
ATOM 2130 CA ARG A 287 29.056 38.558 464.649 1.00 45.56 A C
ANISOU 2130 CA ARG A 287 4201 2941 10168 425 1511 480 A C
ATOM 2131 C ARG A 287 27.575 38.845 464.779 1.00 44.08 A C
ANISOU 2131 C ARG A 287 4285 2843 9619 376 1331 442 A C
ATOM 2132 O ARG A 287 27.092 39.091 465.891 1.00 46.13 A O
ANISOU 2132 O ARG A 287 4526 3119 9882 319 1040 384 A O
ATOM 2133 CB ARG A 287 29.427 37.308 465.432 1.00 53.67 A C
ANISOU 2133 CB ARG A 287 5149 3957 11286 498 1352 388 A C
ATOM 2134 CG ARG A 287 28.626 36.083 465.066 1.00 59.89 A C
ANISOU 2134 CG ARG A 287 6215 4809 11731 577 1363 311 A C
ATOM 2135 CD ARG A 287 29.434 34.819 465.358 1.00 61.42 A C
ANISOU 2135 CD ARG A 287 6295 4942 12098 686 1365 259 A C
ATOM 2136 NE ARG A 287 28.825 33.628 464.771 1.00 45.02 A N
ANISOU 2136 NE ARG A 287 4488 2894 9725 768 1441 188 A N
ATOM 2137 CZ ARG A 287 28.941 33.302 463.490 1.00 46.44 A C
ANISOU 2137 CZ ARG A 287 4810 3065 9769 846 1758 194 A C
ATOM 2138 NH1 ARG A 287 29.638 34.082 462.676 1.00 61.03 A N1+
ANISOU 2138 NH1 ARG A 287 6555 4888 11747 852 2054 284 A N1+
ATOM 2139 NH2 ARG A 287 28.365 32.205 463.019 1.00 46.22 A N
ANISOU 2139 NH2 ARG A 287 5044 3045 9472 913 1785 109 A N
ATOM 2140 N ALA A 288 26.860 38.792 463.660 1.00 43.04 A N
ANISOU 2140 N ALA A 288 4409 2765 9179 403 1500 472 A N
ATOM 2141 CA ALA A 288 25.414 38.949 463.648 1.00 41.09 A C
ANISOU 2141 CA ALA A 288 4406 2602 8604 370 1335 440 A C
ATOM 2142 C ALA A 288 24.714 37.599 463.618 1.00 44.87 A C
ANISOU 2142 C ALA A 288 5077 3143 8830 426 1252 340 A C
ATOM 2143 O ALA A 288 25.209 36.621 463.060 1.00 69.08 A O
ANISOU 2143 O ALA A 288 8191 6188 11867 507 1410 312 A O
ATOM 2144 CB ALA A 288 24.958 39.760 462.438 1.00 52.68 A C
ANISOU 2144 CB ALA A 288 6053 4080 9882 360 1512 542 A C
ATOM 2145 N ILE A 289 23.536 37.565 464.210 1.00 45.61 A N
ANISOU 2145 N ILE A 289 5277 3300 8751 381 1015 285 A N
ATOM 2146 CA ILE A 289 22.702 36.379 464.251 1.00 37.22 A C
ANISOU 2146 CA ILE A 289 4390 2287 7463 404 908 199 A C
ATOM 2147 C ILE A 289 21.287 36.798 463.871 1.00 36.25 A C
ANISOU 2147 C ILE A 289 4451 2235 7086 360 808 206 A C
ATOM 2148 O ILE A 289 20.708 37.677 464.523 1.00 44.78 A O
ANISOU 2148 O ILE A 289 5471 3340 8205 302 668 221 A O
ATOM 2149 CB ILE A 289 22.744 35.759 465.653 1.00 50.54 A C
ANISOU 2149 CB ILE A 289 5971 3969 9262 387 694 129 A C
ATOM 2150 CG1 ILE A 289 23.947 34.846 465.803 1.00 50.63 A C
ANISOU 2150 CG1 ILE A 289 5866 3908 9463 462 769 107 A C
ATOM 2151 CG2 ILE A 289 21.469 35.043 466.007 1.00 57.48 A C
ANISOU 2151 CG2 ILE A 289 7013 4908 9919 357 524 66 A C
ATOM 2152 CD1 ILE A 289 23.857 34.075 467.104 1.00 65.98 A C
ANISOU 2152 CD1 ILE A 289 7772 5842 11456 454 537 49 A C
ATOM 2153 N GLY A 290 20.732 36.176 462.816 1.00 47.45 A N
ANISOU 2153 N GLY A 290 6096 3678 8255 392 868 189 A N
ATOM 2154 CA GLY A 290 19.395 36.520 462.347 1.00 36.32 A C
ANISOU 2154 CA GLY A 290 4852 2328 6621 355 747 200 A C
ATOM 2155 C GLY A 290 18.289 36.009 463.267 1.00 50.83 A C
ANISOU 2155 C GLY A 290 6681 4215 8418 301 506 127 A C
ATOM 2156 O GLY A 290 18.519 35.224 464.195 1.00 43.76 A O
ANISOU 2156 O GLY A 290 5706 3306 7614 294 439 66 A O
ATOM 2157 N ARG A 291 17.047 36.438 462.970 1.00 32.88 A N
ANISOU 2157 N ARG A 291 3371 2436 6687 771 1393 -291 A N
ATOM 2158 CA ARG A 291 15.916 36.040 463.807 1.00 32.73 A C
ANISOU 2158 CA ARG A 291 3387 2451 6596 809 1387 -284 A C
ATOM 2159 C ARG A 291 15.717 34.527 463.827 1.00 31.85 A C
ANISOU 2159 C ARG A 291 3265 2380 6458 809 1254 -271 A C
ATOM 2160 O ARG A 291 15.387 33.968 464.875 1.00 34.70 A O
ANISOU 2160 O ARG A 291 3645 2751 6788 822 1205 -291 A O
ATOM 2161 CB ARG A 291 14.629 36.735 463.351 1.00 33.27 A C
ANISOU 2161 CB ARG A 291 3476 2548 6618 872 1505 -207 A C
ATOM 2162 CG ARG A 291 14.621 38.238 463.447 1.00 34.52 A C
ANISOU 2162 CG ARG A 291 3693 2654 6768 918 1642 -219 A C
ATOM 2163 CD ARG A 291 13.184 38.766 463.496 1.00 47.24 A C
ANISOU 2163 CD ARG A 291 5347 4316 8288 1042 1754 -141 A C
ATOM 2164 NE ARG A 291 13.068 40.203 463.245 1.00 41.29 A N
ANISOU 2164 NE ARG A 291 4674 3508 7506 1119 1895 -133 A N
ATOM 2165 CZ ARG A 291 13.386 41.156 464.117 1.00 49.31 A C
ANISOU 2165 CZ ARG A 291 5806 4446 8484 1183 1955 -217 A C
ATOM 2166 NH1 ARG A 291 13.868 40.855 465.316 1.00 49.33 A N1+
ANISOU 2166 NH1 ARG A 291 5852 4421 8472 1175 1885 -317 A N1+
ATOM 2167 NH2 ARG A 291 13.254 42.426 463.771 1.00 55.38 A N
ANISOU 2167 NH2 ARG A 291 6672 5149 9222 1266 2079 -209 A N
ATOM 2168 N ARG A 292 15.995 33.838 462.725 1.00 32.18 A N
ANISOU 2168 N ARG A 292 3299 2429 6497 816 1186 -245 A N
ATOM 2169 CA ARG A 292 15.749 32.398 462.695 1.00 42.87 A C
ANISOU 2169 CA ARG A 292 4693 3792 7804 849 1046 -240 A C
ATOM 2170 C ARG A 292 16.777 31.656 463.537 1.00 49.80 A C
ANISOU 2170 C ARG A 292 5605 4644 8674 854 942 -301 A C
ATOM 2171 O ARG A 292 16.440 30.661 464.191 1.00 52.67 A O
ANISOU 2171 O ARG A 292 6021 4994 9000 871 843 -306 A O
ATOM 2172 CB ARG A 292 15.719 31.880 461.258 1.00 42.43 A C
ANISOU 2172 CB ARG A 292 4677 3736 7710 904 994 -209 A C
ATOM 2173 CG ARG A 292 14.440 32.296 460.598 1.00 47.61 A C
ANISOU 2173 CG ARG A 292 5302 4421 8365 908 1064 -137 A C
ATOM 2174 CD ARG A 292 14.314 31.965 459.137 1.00 41.95 A C
ANISOU 2174 CD ARG A 292 4629 3702 7607 970 1022 -110 A C
ATOM 2175 NE ARG A 292 12.923 32.204 458.732 1.00 48.59 A N
ANISOU 2175 NE ARG A 292 5428 4579 8455 977 1069 -29 A N
ATOM 2176 CZ ARG A 292 12.432 33.414 458.451 1.00 52.01 A C
ANISOU 2176 CZ ARG A 292 5800 5048 8912 967 1224 30 A C
ATOM 2177 NH1 ARG A 292 13.224 34.475 458.495 1.00 50.76 A N1+
ANISOU 2177 NH1 ARG A 292 5636 4868 8783 936 1330 6 A N1+
ATOM 2178 NH2 ARG A 292 11.160 33.562 458.096 1.00 52.91 A N
ANISOU 2178 NH2 ARG A 292 5871 5214 9019 1004 1263 124 A N
ATOM 2179 N ILE A 293 18.037 32.113 463.515 1.00 43.60 A N
ANISOU 2179 N ILE A 293 4793 3844 7927 849 959 -335 A N
ATOM 2180 CA ILE A 293 19.061 31.505 464.362 1.00 46.80 A C
ANISOU 2180 CA ILE A 293 5220 4232 8330 870 871 -380 A C
ATOM 2181 C ILE A 293 18.775 31.801 465.837 1.00 40.40 A C
ANISOU 2181 C ILE A 293 4399 3412 7538 817 886 -425 A C
ATOM 2182 O ILE A 293 18.938 30.942 466.702 1.00 49.62 A O
ANISOU 2182 O ILE A 293 5614 4568 8672 837 793 -448 A O
ATOM 2183 CB ILE A 293 20.454 32.061 463.971 1.00 40.17 A C
ANISOU 2183 CB ILE A 293 4327 3386 7549 886 899 -383 A C
ATOM 2184 CG1 ILE A 293 21.028 31.411 462.717 1.00 32.54 A C
ANISOU 2184 CG1 ILE A 293 3411 2434 6520 1008 856 -341 A C
ATOM 2185 CG2 ILE A 293 21.478 31.728 465.047 1.00 32.25 A C
ANISOU 2185 CG2 ILE A 293 3317 2369 6567 900 831 -423 A C
ATOM 2186 CD1 ILE A 293 21.503 30.014 462.886 1.00 35.42 A C
ANISOU 2186 CD1 ILE A 293 3895 2789 6773 1143 724 -349 A C
ATOM 2187 N ARG A 294 18.317 33.009 466.146 1.00 41.25 A N
ANISOU 2187 N ARG A 294 4480 3515 7678 778 1003 -437 A N
ATOM 2188 CA ARG A 294 17.898 33.322 467.508 1.00 35.47 A C
ANISOU 2188 CA ARG A 294 3787 2771 6921 779 1026 -483 A C
ATOM 2189 C ARG A 294 16.818 32.377 467.989 1.00 31.31 A C
ANISOU 2189 C ARG A 294 3291 2273 6331 811 980 -447 A C
ATOM 2190 O ARG A 294 16.903 31.829 469.091 1.00 31.25 A O
ANISOU 2190 O ARG A 294 3324 2254 6296 824 917 -479 A O
ATOM 2191 CB ARG A 294 17.403 34.761 467.595 1.00 45.64 A C
ANISOU 2191 CB ARG A 294 5100 4038 8205 794 1167 -495 A C
ATOM 2192 CG ARG A 294 18.428 35.765 467.284 1.00 33.12 A C
ANISOU 2192 CG ARG A 294 3500 2395 6691 761 1208 -534 A C
ATOM 2193 CD ARG A 294 17.764 37.060 467.106 1.00 48.08 A C
ANISOU 2193 CD ARG A 294 5454 4255 8557 801 1344 -530 A C
ATOM 2194 NE ARG A 294 18.608 37.989 466.377 1.00 48.32 A N
ANISOU 2194 NE ARG A 294 5458 4228 8674 764 1391 -536 A N
ATOM 2195 CZ ARG A 294 18.156 39.123 465.877 1.00 35.47 A C
ANISOU 2195 CZ ARG A 294 3883 2559 7033 800 1511 -517 A C
ATOM 2196 NH1 ARG A 294 16.881 39.436 466.048 1.00 39.53 A N1+
ANISOU 2196 NH1 ARG A 294 4478 3099 7445 892 1594 -488 A N1+
ATOM 2197 NH2 ARG A 294 18.964 39.927 465.211 1.00 35.97 A N
ANISOU 2197 NH2 ARG A 294 3919 2561 7187 763 1551 -517 A N
ATOM 2198 N ARG A 295 15.769 32.207 467.181 1.00 47.93 A N
ANISOU 2198 N ARG A 295 5378 4412 8421 828 1010 -370 A N
ATOM 2199 CA ARG A 295 14.670 31.343 467.582 1.00 37.15 A C
ANISOU 2199 CA ARG A 295 4022 3071 7022 860 965 -311 A C
ATOM 2200 C ARG A 295 15.150 29.906 467.717 1.00 30.36 A C
ANISOU 2200 C ARG A 295 3224 2161 6150 852 794 -319 A C
ATOM 2201 O ARG A 295 14.758 29.209 468.656 1.00 30.26 A O
ANISOU 2201 O ARG A 295 3250 2130 6118 865 731 -301 A O
ATOM 2202 CB ARG A 295 13.512 31.429 466.582 1.00 45.18 A C
ANISOU 2202 CB ARG A 295 4994 4131 8041 884 1015 -212 A C
ATOM 2203 CG ARG A 295 12.940 32.831 466.227 1.00 31.92 A C
ANISOU 2203 CG ARG A 295 3283 2496 6349 923 1186 -179 A C
ATOM 2204 CD ARG A 295 12.261 33.466 467.367 1.00 50.70 A C
ANISOU 2204 CD ARG A 295 5670 4927 8667 1015 1288 -170 A C
ATOM 2205 NE ARG A 295 11.397 34.582 466.984 1.00 64.12 A N
ANISOU 2205 NE ARG A 295 7359 6687 10319 1108 1441 -103 A N
ATOM 2206 CZ ARG A 295 11.831 35.812 466.714 1.00 59.72 A C
ANISOU 2206 CZ ARG A 295 6866 6075 9750 1124 1537 -151 A C
ATOM 2207 NH1 ARG A 295 13.124 36.096 466.753 1.00 56.48 A N1+
ANISOU 2207 NH1 ARG A 295 6502 5567 9391 1039 1496 -255 A N1+
ATOM 2208 NH2 ARG A 295 10.967 36.765 466.417 1.00 60.25 A N
ANISOU 2208 NH2 ARG A 295 6944 6194 9756 1238 1674 -81 A N
ATOM 2209 N LEU A 296 15.975 29.433 466.771 1.00 30.37 A N
ANISOU 2209 N LEU A 296 3263 2132 6143 859 718 -334 A N
ATOM 2210 CA LEU A 296 16.494 28.068 466.842 1.00 30.48 A C
ANISOU 2210 CA LEU A 296 3407 2075 6100 900 555 -339 A C
ATOM 2211 C LEU A 296 17.325 27.829 468.092 1.00 37.83 A C
ANISOU 2211 C LEU A 296 4364 2987 7023 899 514 -390 A C
ATOM 2212 O LEU A 296 17.141 26.826 468.793 1.00 42.25 A O
ANISOU 2212 O LEU A 296 5033 3482 7539 909 407 -372 A O
ATOM 2213 CB LEU A 296 17.344 27.796 465.607 1.00 30.93 A C
ANISOU 2213 CB LEU A 296 3527 2113 6111 970 513 -347 A C
ATOM 2214 CG LEU A 296 18.213 26.533 465.496 1.00 40.46 A C
ANISOU 2214 CG LEU A 296 4929 3236 7209 1083 372 -355 A C
ATOM 2215 CD1 LEU A 296 17.467 25.215 465.674 1.00 34.58 A C
ANISOU 2215 CD1 LEU A 296 4406 2359 6375 1097 227 -311 A C
ATOM 2216 CD2 LEU A 296 18.917 26.536 464.151 1.00 34.38 A C
ANISOU 2216 CD2 LEU A 296 4218 2469 6377 1202 376 -354 A C
ATOM 2217 N LEU A 297 18.144 28.799 468.460 1.00 30.75 A N
ANISOU 2217 N LEU A 297 3382 2127 6174 877 594 -445 A N
ATOM 2218 CA LEU A 297 18.910 28.717 469.696 1.00 30.93 A C
ANISOU 2218 CA LEU A 297 3422 2131 6199 876 558 -497 A C
ATOM 2219 C LEU A 297 17.982 28.621 470.910 1.00 30.77 A C
ANISOU 2219 C LEU A 297 3434 2102 6155 860 565 -498 A C
ATOM 2220 O LEU A 297 18.115 27.722 471.748 1.00 38.21 A O
ANISOU 2220 O LEU A 297 4460 2998 7058 876 470 -496 A O
ATOM 2221 CB LEU A 297 19.868 29.914 469.803 1.00 32.10 A C
ANISOU 2221 CB LEU A 297 3485 2294 6417 847 635 -551 A C
ATOM 2222 CG LEU A 297 21.075 29.991 468.838 1.00 31.65 A C
ANISOU 2222 CG LEU A 297 3382 2245 6398 882 624 -536 A C
ATOM 2223 CD1 LEU A 297 21.876 31.240 469.084 1.00 35.35 A C
ANISOU 2223 CD1 LEU A 297 3768 2701 6964 833 692 -577 A C
ATOM 2224 CD2 LEU A 297 21.972 28.778 468.816 1.00 32.03 A C
ANISOU 2224 CD2 LEU A 297 3501 2280 6387 989 510 -513 A C
ATOM 2225 N VAL A 298 17.074 29.588 471.054 1.00 30.82 A N
ANISOU 2225 N VAL A 298 3392 2149 6171 855 688 -494 A N
ATOM 2226 CA VAL A 298 16.233 29.638 472.247 1.00 31.25 A C
ANISOU 2226 CA VAL A 298 3456 2195 6221 886 737 -492 A C
ATOM 2227 C VAL A 298 15.359 28.397 472.357 1.00 33.23 A C
ANISOU 2227 C VAL A 298 3658 2366 6602 869 691 -400 A C
ATOM 2228 O VAL A 298 15.221 27.820 473.442 1.00 32.63 A O
ANISOU 2228 O VAL A 298 3564 2202 6632 864 675 -394 A O
ATOM 2229 CB VAL A 298 15.385 30.923 472.235 1.00 31.72 A C
ANISOU 2229 CB VAL A 298 3492 2320 6239 944 897 -486 A C
ATOM 2230 CG1 VAL A 298 14.358 30.898 473.332 1.00 33.16 A C
ANISOU 2230 CG1 VAL A 298 3618 2484 6495 1018 1025 -452 A C
ATOM 2231 CG2 VAL A 298 16.272 32.119 472.354 1.00 32.25 A C
ANISOU 2231 CG2 VAL A 298 3606 2359 6290 937 946 -582 A C
ATOM 2232 N ARG A 299 14.838 27.908 471.227 1.00 39.70 A N
ANISOU 2232 N ARG A 299 4470 3179 7435 852 644 -318 A N
ATOM 2233 CA ARG A 299 14.009 26.704 471.252 1.00 38.14 A C
ANISOU 2233 CA ARG A 299 4243 2837 7414 809 556 -196 A C
ATOM 2234 C ARG A 299 14.847 25.520 471.710 1.00 42.08 A C
ANISOU 2234 C ARG A 299 4905 3211 7874 776 361 -225 A C
ATOM 2235 O ARG A 299 14.346 24.601 472.372 1.00 33.73 A O
ANISOU 2235 O ARG A 299 3859 1992 6965 707 255 -125 A O
ATOM 2236 CB ARG A 299 13.394 26.404 469.887 1.00 35.18 A C
ANISOU 2236 CB ARG A 299 3875 2437 7056 790 504 -107 A C
ATOM 2237 CG ARG A 299 12.430 27.398 469.315 1.00 32.20 A C
ANISOU 2237 CG ARG A 299 3332 2172 6729 827 685 -34 A C
ATOM 2238 CD ARG A 299 11.122 27.498 470.043 1.00 33.80 A C
ANISOU 2238 CD ARG A 299 3297 2374 7172 861 837 168 A C
ATOM 2239 NE ARG A 299 11.229 28.475 471.123 1.00 35.51 A N
ANISOU 2239 NE ARG A 299 3490 2724 7276 953 1020 88 A N
ATOM 2240 CZ ARG A 299 11.147 29.791 470.909 1.00 42.44 A C
ANISOU 2240 CZ ARG A 299 4406 3760 7959 1031 1159 19 A C
ATOM 2241 NH1 ARG A 299 10.965 30.234 469.665 1.00 33.23 A N1+
ANISOU 2241 NH1 ARG A 299 3256 2651 6716 1021 1154 30 A N1+
ATOM 2242 NH2 ARG A 299 11.253 30.662 471.908 1.00 34.42 A N
ANISOU 2242 NH2 ARG A 299 3442 2817 6818 1125 1274 -59 A N
ATOM 2243 N THR A 300 16.113 25.488 471.284 1.00 37.02 A N
ANISOU 2243 N THR A 300 4403 2632 7030 828 303 -316 A N
ATOM 2244 CA THR A 300 16.996 24.400 471.674 1.00 36.11 A C
ANISOU 2244 CA THR A 300 4461 2420 6840 849 157 -328 A C
ATOM 2245 C THR A 300 17.273 24.427 473.173 1.00 32.83 A C
ANISOU 2245 C THR A 300 3976 1969 6528 824 166 -371 A C
ATOM 2246 O THR A 300 17.145 23.404 473.852 1.00 33.82 A O
ANISOU 2246 O THR A 300 4188 1950 6712 782 38 -322 A O
ATOM 2247 CB THR A 300 18.295 24.515 470.888 1.00 31.59 A C
ANISOU 2247 CB THR A 300 3996 1939 6066 958 155 -373 A C
ATOM 2248 CG2 THR A 300 19.251 23.439 471.266 1.00 32.42 A C
ANISOU 2248 CG2 THR A 300 4275 1953 6088 1035 57 -366 A C
ATOM 2249 OG1 THR A 300 18.007 24.422 469.496 1.00 31.67 A O
ANISOU 2249 OG1 THR A 300 4055 1940 6039 991 148 -342 A O
ATOM 2250 N VAL A 301 17.598 25.599 473.721 1.00 45.58 A N
ANISOU 2250 N VAL A 301 5469 3689 8160 838 298 -455 A N
ATOM 2251 CA VAL A 301 17.815 25.694 475.167 1.00 41.80 A C
ANISOU 2251 CA VAL A 301 4951 3160 7771 827 313 -514 A C
ATOM 2252 C VAL A 301 16.548 25.294 475.914 1.00 34.35 A C
ANISOU 2252 C VAL A 301 3943 2112 6996 793 335 -430 A C
ATOM 2253 O VAL A 301 16.599 24.601 476.933 1.00 41.42 A O
ANISOU 2253 O VAL A 301 4868 2892 7977 768 249 -413 A O
ATOM 2254 CB VAL A 301 18.275 27.110 475.570 1.00 39.86 A C
ANISOU 2254 CB VAL A 301 4647 2998 7500 844 445 -621 A C
ATOM 2255 CG1 VAL A 301 18.250 27.252 477.075 1.00 34.48 A C
ANISOU 2255 CG1 VAL A 301 3961 2241 6899 848 476 -696 A C
ATOM 2256 CG2 VAL A 301 19.650 27.446 475.009 1.00 32.81 A C
ANISOU 2256 CG2 VAL A 301 3768 2157 6542 855 404 -661 A C
ATOM 2257 N GLU A 302 15.386 25.644 475.367 1.00 37.03 A N
ANISOU 2257 N GLU A 302 4179 2477 7415 795 443 -335 A N
ATOM 2258 CA GLU A 302 14.138 25.304 476.035 1.00 35.82 A C
ANISOU 2258 CA GLU A 302 3897 2224 7490 790 500 -159 A C
ATOM 2259 C GLU A 302 13.887 23.807 476.025 1.00 36.68 A C
ANISOU 2259 C GLU A 302 4120 2233 7585 598 217 26 A C
ATOM 2260 O GLU A 302 13.422 23.254 477.028 1.00 38.07 A O
ANISOU 2260 O GLU A 302 4284 2563 7620 455 138 181 A O
ATOM 2261 CB GLU A 302 12.980 26.034 475.368 1.00 36.03 A C
ANISOU 2261 CB GLU A 302 3745 2361 7585 862 698 -29 A C
ATOM 2262 CG GLU A 302 12.862 27.434 475.830 1.00 36.22 A C
ANISOU 2262 CG GLU A 302 3720 2577 7463 1006 959 -134 A C
ATOM 2263 CD GLU A 302 11.943 28.231 474.979 1.00 50.88 A C
ANISOU 2263 CD GLU A 302 5463 4598 9269 1079 1128 -32 A C
ATOM 2264 OE1 GLU A 302 11.567 27.740 473.898 1.00 57.56 A O
ANISOU 2264 OE1 GLU A 302 6251 5404 10214 1007 1041 83 A O
ATOM 2265 OE2 GLU A 302 11.639 29.370 475.377 1.00 57.04 A O1-
ANISOU 2265 OE2 GLU A 302 6260 5534 9880 1210 1323 -74 A O1-
ATOM 2266 N PHE A 303 14.149 23.131 474.903 1.00 41.47 A N
ANISOU 2266 N PHE A 303 4882 2684 8191 560 46 30 A N
ATOM 2267 CA PHE A 303 13.994 21.681 474.919 1.00 37.44 A C
ANISOU 2267 CA PHE A 303 4590 1994 7643 371 -263 193 A C
ATOM 2268 C PHE A 303 15.031 21.047 475.816 1.00 49.76 A C
ANISOU 2268 C PHE A 303 6313 3495 9099 403 -374 90 A C
ATOM 2269 O PHE A 303 14.735 20.081 476.527 1.00 51.93 A O
ANISOU 2269 O PHE A 303 6704 3738 9291 223 -569 249 A O
ATOM 2270 CB PHE A 303 14.093 21.083 473.528 1.00 37.30 A C
ANISOU 2270 CB PHE A 303 4793 1930 7450 349 -400 188 A C
ATOM 2271 CG PHE A 303 13.824 19.604 473.509 1.00 43.04 A C
ANISOU 2271 CG PHE A 303 5823 2473 8057 132 -723 356 A C
ATOM 2272 CD1 PHE A 303 12.547 19.118 473.708 1.00 45.62 A C
ANISOU 2272 CD1 PHE A 303 6116 2759 8457 -200 -924 680 A C
ATOM 2273 CD2 PHE A 303 14.857 18.690 473.327 1.00 39.45 A C
ANISOU 2273 CD2 PHE A 303 5685 1951 7352 233 -807 240 A C
ATOM 2274 CE1 PHE A 303 12.305 17.748 473.699 1.00 50.85 A C
ANISOU 2274 CE1 PHE A 303 7107 3299 8915 -458 -1252 839 A C
ATOM 2275 CE2 PHE A 303 14.611 17.342 473.319 1.00 41.51 A C
ANISOU 2275 CE2 PHE A 303 6255 2056 7463 53 -1073 372 A C
ATOM 2276 CZ PHE A 303 13.335 16.869 473.509 1.00 43.38 A C
ANISOU 2276 CZ PHE A 303 6504 2243 7733 -304 -1315 649 A C
ATOM 2277 N ALA A 304 16.233 21.622 475.847 1.00 52.44 A N
ANISOU 2277 N ALA A 304 6644 3971 9308 582 -243 -130 A N
ATOM 2278 CA ALA A 304 17.302 21.059 476.663 1.00 49.04 A C
ANISOU 2278 CA ALA A 304 6331 3505 8796 633 -336 -199 A C
ATOM 2279 C ALA A 304 17.003 21.252 478.139 1.00 45.70 A C
ANISOU 2279 C ALA A 304 5788 3028 8548 583 -327 -184 A C
ATOM 2280 O ALA A 304 17.260 20.362 478.956 1.00 44.32 A O
ANISOU 2280 O ALA A 304 5737 2823 8277 514 -491 -120 A O
ATOM 2281 CB ALA A 304 18.643 21.697 476.305 1.00 49.08 A C
ANISOU 2281 CB ALA A 304 6310 3670 8668 790 -220 -350 A C
ATOM 2282 N ALA A 305 16.418 22.394 478.490 1.00 37.50 A N
ANISOU 2282 N ALA A 305 4542 2164 7543 600 -103 -215 A N
ATOM 2283 CA ALA A 305 16.104 22.661 479.884 1.00 44.45 A C
ANISOU 2283 CA ALA A 305 5347 3256 8287 549 -31 -185 A C
ATOM 2284 C ALA A 305 15.060 21.683 480.422 1.00 47.31 A C
ANISOU 2284 C ALA A 305 5719 3759 8498 340 -162 99 A C
ATOM 2285 O ALA A 305 15.291 21.035 481.448 1.00 61.65 A O
ANISOU 2285 O ALA A 305 7608 5621 10195 268 -276 150 A O
ATOM 2286 CB ALA A 305 15.626 24.107 480.045 1.00 38.46 A C
ANISOU 2286 CB ALA A 305 4436 2645 7531 663 253 -266 A C
ATOM 2287 N GLU A 306 13.925 21.525 479.728 1.00 40.66 A N
ANISOU 2287 N GLU A 306 4798 2998 7653 218 -168 315 A N
ATOM 2288 CA GLU A 306 12.948 20.515 480.145 1.00 43.23 A C
ANISOU 2288 CA GLU A 306 5124 3465 7837 -47 -342 641 A C
ATOM 2289 C GLU A 306 13.578 19.127 480.321 1.00 43.68 A C
ANISOU 2289 C GLU A 306 5473 3281 7841 -181 -653 672 A C
ATOM 2290 O GLU A 306 13.298 18.427 481.303 1.00 44.93 A O
ANISOU 2290 O GLU A 306 5661 3550 7859 -337 -766 845 A O
ATOM 2291 CB GLU A 306 11.799 20.413 479.129 1.00 43.27 A C
ANISOU 2291 CB GLU A 306 5029 3552 7859 -210 -380 885 A C
ATOM 2292 CG GLU A 306 11.026 21.716 478.876 1.00 74.57 A C
ANISOU 2292 CG GLU A 306 8701 7783 11848 -56 -67 914 A C
ATOM 2293 CD GLU A 306 10.362 22.326 480.100 1.00 74.90 A C
ANISOU 2293 CD GLU A 306 8526 8202 11731 30 157 1044 A C
ATOM 2294 OE1 GLU A 306 9.398 21.744 480.618 1.00 72.61 A O
ANISOU 2294 OE1 GLU A 306 8100 8194 11295 -169 84 1395 A O
ATOM 2295 OE2 GLU A 306 10.796 23.426 480.523 1.00 71.64 A O1-
ANISOU 2295 OE2 GLU A 306 8096 7806 11321 303 407 808 A O1-
ATOM 2296 N ARG A 307 14.504 18.756 479.437 1.00 42.25 A N
ANISOU 2296 N ARG A 307 5524 2778 7753 -74 -772 503 A N
ATOM 2297 CA ARG A 307 15.207 17.480 479.570 1.00 43.14 A C
ANISOU 2297 CA ARG A 307 5969 2635 7787 -111 -1041 515 A C
ATOM 2298 C ARG A 307 16.016 17.434 480.863 1.00 44.19 A C
ANISOU 2298 C ARG A 307 6087 2851 7853 -14 -1013 419 A C
ATOM 2299 O ARG A 307 15.967 16.447 481.610 1.00 44.92 A O
ANISOU 2299 O ARG A 307 6337 2921 7809 -149 -1195 561 A O
ATOM 2300 CB ARG A 307 16.077 17.242 478.336 1.00 44.11 A C
ANISOU 2300 CB ARG A 307 6331 2435 7993 86 -1115 354 A C
ATOM 2301 CG ARG A 307 16.734 15.873 478.192 1.00 43.56 A C
ANISOU 2301 CG ARG A 307 6652 2189 7711 114 -1327 369 A C
ATOM 2302 CD ARG A 307 15.808 14.727 477.978 1.00 45.77 A C
ANISOU 2302 CD ARG A 307 7197 2363 7832 -189 -1591 607 A C
ATOM 2303 NE ARG A 307 16.512 13.468 478.137 1.00 47.42 A N
ANISOU 2303 NE ARG A 307 7751 2455 7810 -121 -1738 593 A N
ATOM 2304 CZ ARG A 307 15.915 12.302 478.320 1.00 61.97 A C
ANISOU 2304 CZ ARG A 307 9871 4201 9474 -383 -1999 784 A C
ATOM 2305 NH1 ARG A 307 14.600 12.241 478.367 1.00 67.96 A N1+
ANISOU 2305 NH1 ARG A 307 10565 5011 10244 -767 -2145 1037 A N1+
ATOM 2306 NH2 ARG A 307 16.632 11.195 478.475 1.00 72.91 A N
ANISOU 2306 NH2 ARG A 307 11579 5466 10657 -272 -2112 750 A N
ATOM 2307 N LEU A 308 16.778 18.493 481.132 1.00 42.72 A N
ANISOU 2307 N LEU A 308 5729 2752 7751 201 -805 186 A N
ATOM 2308 CA LEU A 308 17.620 18.547 482.324 1.00 42.33 A C
ANISOU 2308 CA LEU A 308 5663 2790 7632 283 -793 82 A C
ATOM 2309 C LEU A 308 16.785 18.463 483.598 1.00 43.78 A C
ANISOU 2309 C LEU A 308 5751 3225 7659 125 -769 245 A C
ATOM 2310 O LEU A 308 17.219 17.866 484.589 1.00 44.81 A O
ANISOU 2310 O LEU A 308 5965 3387 7673 106 -874 272 A O
ATOM 2311 CB LEU A 308 18.462 19.817 482.310 1.00 50.33 A C
ANISOU 2311 CB LEU A 308 6515 3853 8754 471 -599 -170 A C
ATOM 2312 CG LEU A 308 19.516 19.943 483.398 1.00 47.08 A C
ANISOU 2312 CG LEU A 308 6092 3519 8277 542 -622 -290 A C
ATOM 2313 CD1 LEU A 308 20.389 18.704 483.365 1.00 42.27 A C
ANISOU 2313 CD1 LEU A 308 5675 2767 7619 607 -838 -237 A C
ATOM 2314 CD2 LEU A 308 20.352 21.213 483.167 1.00 40.69 A C
ANISOU 2314 CD2 LEU A 308 5149 2725 7585 663 -477 -511 A C
ATOM 2315 N TRP A 309 15.642 19.156 483.637 1.00 44.03 A N
ANISOU 2315 N TRP A 309 5585 3473 7671 58 -602 356 A N
ATOM 2316 CA TRP A 309 14.781 19.044 484.809 1.00 45.82 A C
ANISOU 2316 CA TRP A 309 5702 3986 7721 -54 -559 563 A C
ATOM 2317 C TRP A 309 14.220 17.634 484.945 1.00 54.58 A C
ANISOU 2317 C TRP A 309 6937 5070 8731 -321 -818 867 A C
ATOM 2318 O TRP A 309 14.041 17.148 486.066 1.00 49.14 A O
ANISOU 2318 O TRP A 309 6249 4535 7890 -405 -871 1010 A O
ATOM 2319 CB TRP A 309 13.640 20.070 484.795 1.00 49.89 A C
ANISOU 2319 CB TRP A 309 5970 4785 8201 -11 -302 667 A C
ATOM 2320 CG TRP A 309 13.981 21.514 484.412 1.00 44.79 A C
ANISOU 2320 CG TRP A 309 5253 4113 7650 232 -49 397 A C
ATOM 2321 CD1 TRP A 309 13.145 22.390 483.807 1.00 44.65 A C
ANISOU 2321 CD1 TRP A 309 5080 4223 7663 315 160 451 A C
ATOM 2322 CD2 TRP A 309 15.231 22.206 484.576 1.00 43.65 A C
ANISOU 2322 CD2 TRP A 309 5204 3808 7575 394 -3 66 A C
ATOM 2323 CE2 TRP A 309 15.058 23.495 484.055 1.00 42.93 A C
ANISOU 2323 CE2 TRP A 309 5040 3720 7552 549 228 -71 A C
ATOM 2324 CE3 TRP A 309 16.473 21.861 485.114 1.00 43.49 A C
ANISOU 2324 CE3 TRP A 309 5312 3659 7552 411 -144 -98 A C
ATOM 2325 NE1 TRP A 309 13.775 23.578 483.593 1.00 56.56 A N
ANISOU 2325 NE1 TRP A 309 6618 5622 9250 524 336 161 A N
ATOM 2326 CZ2 TRP A 309 16.074 24.445 484.054 1.00 47.53 A C
ANISOU 2326 CZ2 TRP A 309 5696 4160 8205 675 299 -363 A C
ATOM 2327 CZ3 TRP A 309 17.481 22.797 485.112 1.00 42.76 A C
ANISOU 2327 CZ3 TRP A 309 5244 3472 7530 534 -74 -367 A C
ATOM 2328 CH2 TRP A 309 17.277 24.077 484.586 1.00 45.90 A C
ANISOU 2328 CH2 TRP A 309 5589 3852 8000 643 136 -497 A C
ATOM 2329 N LEU A 310 13.878 16.977 483.828 1.00 58.53 A N
ANISOU 2329 N LEU A 310 7567 5376 9296 -474 -992 986 A N
ATOM 2330 CA LEU A 310 13.465 15.577 483.926 1.00 49.69 A C
ANISOU 2330 CA LEU A 310 6665 4149 8065 -764 -1294 1263 A C
ATOM 2331 C LEU A 310 14.591 14.711 484.480 1.00 49.98 A C
ANISOU 2331 C LEU A 310 6997 3954 8040 -680 -1465 1149 A C
ATOM 2332 O LEU A 310 14.350 13.779 485.256 1.00 51.96 A O
ANISOU 2332 O LEU A 310 7371 4225 8147 -865 -1637 1359 A O
ATOM 2333 CB LEU A 310 13.007 15.049 482.564 1.00 49.98 A C
ANISOU 2333 CB LEU A 310 6880 3953 8159 -941 -1486 1375 A C
ATOM 2334 CG LEU A 310 12.588 13.567 482.508 1.00 60.51 A C
ANISOU 2334 CG LEU A 310 8546 5085 9359 -1288 -1858 1660 A C
ATOM 2335 CD1 LEU A 310 11.504 13.214 483.538 1.00 55.14 A C
ANISOU 2335 CD1 LEU A 310 7664 4755 8533 -1605 -1907 2046 A C
ATOM 2336 CD2 LEU A 310 12.102 13.219 481.120 1.00 59.00 A C
ANISOU 2336 CD2 LEU A 310 8550 4662 9204 -1466 -2047 1748 A C
ATOM 2337 N ILE A 311 15.833 15.011 484.110 1.00 51.71 A N
ANISOU 2337 N ILE A 311 7314 3980 8355 -395 -1415 847 A N
ATOM 2338 CA ILE A 311 16.946 14.193 484.574 1.00 48.83 A C
ANISOU 2338 CA ILE A 311 7205 3432 7916 -268 -1564 767 A C
ATOM 2339 C ILE A 311 17.178 14.420 486.060 1.00 55.29 A C
ANISOU 2339 C ILE A 311 7867 4510 8633 -239 -1480 755 A C
ATOM 2340 O ILE A 311 17.385 13.466 486.817 1.00 67.99 A O
ANISOU 2340 O ILE A 311 9652 6077 10104 -301 -1643 873 A O
ATOM 2341 CB ILE A 311 18.201 14.462 483.731 1.00 47.30 A C
ANISOU 2341 CB ILE A 311 7103 3034 7836 45 -1525 507 A C
ATOM 2342 CG1 ILE A 311 18.022 13.833 482.358 1.00 47.52 A C
ANISOU 2342 CG1 ILE A 311 7424 2743 7889 32 -1677 556 A C
ATOM 2343 CG2 ILE A 311 19.431 13.964 484.407 1.00 47.89 A C
ANISOU 2343 CG2 ILE A 311 7303 3061 7831 244 -1595 424 A C
ATOM 2344 CD1 ILE A 311 19.039 14.265 481.351 1.00 46.07 A C
ANISOU 2344 CD1 ILE A 311 7269 2415 7822 355 -1588 339 A C
ATOM 2345 N HIS A 312 17.121 15.680 486.505 1.00 48.39 A N
ANISOU 2345 N HIS A 312 6698 3889 7801 -142 -1231 618 A N
ATOM 2346 CA HIS A 312 17.236 15.976 487.932 1.00 58.84 A C
ANISOU 2346 CA HIS A 312 7906 5459 8990 -113 -1150 605 A C
ATOM 2347 C HIS A 312 16.112 15.320 488.727 1.00 57.56 A C
ANISOU 2347 C HIS A 312 7716 5490 8664 -342 -1211 928 A C
ATOM 2348 O HIS A 312 16.341 14.745 489.796 1.00 52.74 A O
ANISOU 2348 O HIS A 312 7172 4957 7909 -369 -1294 1006 A O
ATOM 2349 CB HIS A 312 17.261 17.487 488.191 1.00 48.29 A C
ANISOU 2349 CB HIS A 312 6347 4311 7690 31 -883 403 A C
ATOM 2350 CG HIS A 312 18.484 18.168 487.664 1.00 50.98 A C
ANISOU 2350 CG HIS A 312 6692 4508 8169 214 -843 112 A C
ATOM 2351 CD2 HIS A 312 19.634 17.663 487.150 1.00 59.79 A C
ANISOU 2351 CD2 HIS A 312 7928 5429 9362 317 -978 19 A C
ATOM 2352 ND1 HIS A 312 18.605 19.537 487.607 1.00 45.92 A N
ANISOU 2352 ND1 HIS A 312 5922 3940 7587 317 -642 -85 A N
ATOM 2353 CE1 HIS A 312 19.786 19.847 487.097 1.00 63.13 A C
ANISOU 2353 CE1 HIS A 312 8113 5984 9887 424 -674 -274 A C
ATOM 2354 NE2 HIS A 312 20.428 18.729 486.808 1.00 45.12 A N
ANISOU 2354 NE2 HIS A 312 5957 3568 7619 448 -864 -205 A N
ATOM 2355 N SER A 313 14.880 15.439 488.246 1.00 51.88 A N
ANISOU 2355 N SER A 313 6866 4892 7955 -511 -1164 1147 A N
ATOM 2356 CA SER A 313 13.761 14.888 488.992 1.00 54.29 A C
ANISOU 2356 CA SER A 313 7076 5455 8099 -745 -1211 1515 A C
ATOM 2357 C SER A 313 13.890 13.373 489.150 1.00 64.66 A C
ANISOU 2357 C SER A 313 8680 6557 9331 -971 -1533 1716 A C
ATOM 2358 O SER A 313 13.565 12.829 490.213 1.00 75.71 A O
ANISOU 2358 O SER A 313 10063 8134 10569 -1091 -1590 1935 A O
ATOM 2359 CB SER A 313 12.451 15.268 488.306 1.00 54.85 A C
ANISOU 2359 CB SER A 313 6920 5723 8197 -896 -1122 1758 A C
ATOM 2360 OG SER A 313 11.358 15.219 489.211 1.00 64.11 A O
ANISOU 2360 OG SER A 313 7857 7308 9194 -1022 -1044 2112 A O
ATOM 2361 N ARG A 314 14.384 12.670 488.119 1.00 66.14 A N
ANISOU 2361 N ARG A 314 9177 6351 9604 -1008 -1745 1647 A N
ATOM 2362 CA ARG A 314 14.572 11.222 488.262 1.00 65.88 A C
ANISOU 2362 CA ARG A 314 9521 6051 9459 -1184 -2060 1819 A C
ATOM 2363 C ARG A 314 15.729 10.907 489.207 1.00 68.60 A C
ANISOU 2363 C ARG A 314 9998 6345 9724 -957 -2075 1658 A C
ATOM 2364 O ARG A 314 15.714 9.870 489.887 1.00 78.27 A O
ANISOU 2364 O ARG A 314 11434 7504 10802 -1092 -2265 1850 A O
ATOM 2365 CB ARG A 314 14.849 10.649 486.872 1.00 57.53 A C
ANISOU 2365 CB ARG A 314 8822 4560 8475 -1202 -2260 1754 A C
ATOM 2366 CG ARG A 314 13.598 10.362 486.060 1.00 58.99 A C
ANISOU 2366 CG ARG A 314 9026 4725 8662 -1573 -2408 2040 A C
ATOM 2367 CD ARG A 314 13.980 10.127 484.590 1.00 66.25 A C
ANISOU 2367 CD ARG A 314 10282 5228 9662 -1497 -2542 1886 A C
ATOM 2368 NE ARG A 314 12.864 9.690 483.754 1.00 78.48 A N
ANISOU 2368 NE ARG A 314 11942 6694 11184 -1893 -2760 2163 A N
ATOM 2369 CZ ARG A 314 12.888 9.715 482.420 1.00 71.31 A C
ANISOU 2369 CZ ARG A 314 11178 5618 10298 -1820 -2790 2004 A C
ATOM 2370 NH1 ARG A 314 13.961 10.165 481.775 1.00 58.71 A N1+
ANISOU 2370 NH1 ARG A 314 9655 3862 8789 -1396 -2630 1644 A N1+
ATOM 2371 NH2 ARG A 314 11.825 9.333 481.727 1.00 75.38 A N
ANISOU 2371 NH2 ARG A 314 11695 6230 10716 -2144 -2944 2193 A N
ATOM 2372 N ASN A 315 16.705 11.820 489.299 1.00 64.46 A N
ANISOU 2372 N ASN A 315 9333 5876 9283 -635 -1882 1332 A N
ATOM 2373 CA ASN A 315 17.818 11.683 490.237 1.00 55.58 A C
ANISOU 2373 CA ASN A 315 8259 4780 8078 -426 -1885 1190 A C
ATOM 2374 C ASN A 315 17.343 11.817 491.677 1.00 56.94 A C
ANISOU 2374 C ASN A 315 8249 5291 8095 -510 -1808 1324 A C
ATOM 2375 O ASN A 315 17.829 11.114 492.564 1.00 65.21 A O
ANISOU 2375 O ASN A 315 9428 6341 9008 -484 -1918 1381 A O
ATOM 2376 CB ASN A 315 18.928 12.685 489.914 1.00 53.47 A C
ANISOU 2376 CB ASN A 315 7860 4520 7938 -129 -1728 852 A C
ATOM 2377 CG ASN A 315 19.765 12.261 488.716 1.00 70.55 A C
ANISOU 2377 CG ASN A 315 10255 6357 10195 46 -1830 744 A C
ATOM 2378 ND2 ASN A 315 20.572 13.188 488.184 1.00 52.08 A N
ANISOU 2378 ND2 ASN A 315 7758 4039 7991 261 -1690 505 A N
ATOM 2379 OD1 ASN A 315 19.684 11.108 488.269 1.00 75.54 A O
ANISOU 2379 OD1 ASN A 315 11230 6713 10757 -7 -2038 889 A O
ATOM 2380 N VAL A 316 16.384 12.710 491.918 1.00 56.85 A N
ANISOU 2380 N VAL A 316 7945 5577 8079 -578 -1607 1390 A N
ATOM 2381 CA VAL A 316 15.755 12.822 493.231 1.00 58.61 A C
ANISOU 2381 CA VAL A 316 8002 6150 8117 -633 -1514 1569 A C
ATOM 2382 C VAL A 316 15.105 11.499 493.600 1.00 81.67 A C
ANISOU 2382 C VAL A 316 11062 9058 10912 -918 -1735 1950 A C
ATOM 2383 O VAL A 316 15.210 11.030 494.742 1.00 81.48 A O
ANISOU 2383 O VAL A 316 11066 9170 10722 -928 -1778 2065 A O
ATOM 2384 CB VAL A 316 14.742 13.983 493.249 1.00 59.99 A C
ANISOU 2384 CB VAL A 316 7868 6644 8282 -603 -1242 1616 A C
ATOM 2385 CG1 VAL A 316 14.037 14.062 494.587 1.00 60.77 A C
ANISOU 2385 CG1 VAL A 316 7809 7132 8150 -608 -1126 1840 A C
ATOM 2386 CG2 VAL A 316 15.428 15.299 492.915 1.00 56.33 A C
ANISOU 2386 CG2 VAL A 316 7335 6141 7926 -338 -1045 1233 A C
ATOM 2387 N GLU A 317 14.432 10.873 492.632 1.00 77.26 A N
ANISOU 2387 N GLU A 317 10614 8322 10418 -1175 -1901 2160 A N
ATOM 2388 CA GLU A 317 13.820 9.569 492.860 1.00 74.20 A C
ANISOU 2388 CA GLU A 317 10423 7861 9911 -1516 -2168 2542 A C
ATOM 2389 C GLU A 317 14.871 8.538 493.254 1.00 65.23 A C
ANISOU 2389 C GLU A 317 9674 6416 8695 -1432 -2378 2465 A C
ATOM 2390 O GLU A 317 14.720 7.838 494.263 1.00 72.20 A O
ANISOU 2390 O GLU A 317 10617 7401 9416 -1547 -2473 2687 A O
ATOM 2391 CB GLU A 317 13.124 9.119 491.578 1.00 80.23 A C
ANISOU 2391 CB GLU A 317 11326 8396 10760 -1806 -2357 2716 A C
ATOM 2392 CG GLU A 317 11.623 9.179 491.552 1.00 87.06 A C
ANISOU 2392 CG GLU A 317 11903 9599 11577 -2159 -2354 3140 A C
ATOM 2393 CD GLU A 317 11.098 8.793 490.182 1.00 87.77 A C
ANISOU 2393 CD GLU A 317 12166 9425 11756 -2442 -2571 3260 A C
ATOM 2394 OE1 GLU A 317 10.830 7.585 489.961 1.00 95.43 A O
ANISOU 2394 OE1 GLU A 317 13491 10124 12643 -2800 -2921 3518 A O
ATOM 2395 OE2 GLU A 317 10.994 9.699 489.319 1.00 71.01 A O1-
ANISOU 2395 OE2 GLU A 317 9868 7338 9775 -2305 -2404 3084 A O1-
ATOM 2396 N ARG A 318 15.955 8.441 492.480 1.00 63.62 A N
ANISOU 2396 N ARG A 318 9726 5859 8587 -1198 -2438 2172 A N
ATOM 2397 CA ARG A 318 16.995 7.476 492.825 1.00 77.09 A C
ANISOU 2397 CA ARG A 318 11799 7300 10193 -1047 -2614 2117 A C
ATOM 2398 C ARG A 318 17.617 7.775 494.186 1.00 77.27 A C
ANISOU 2398 C ARG A 318 11640 7607 10112 -850 -2487 2028 A C
ATOM 2399 O ARG A 318 17.986 6.845 494.918 1.00 79.05 A O
ANISOU 2399 O ARG A 318 12091 7757 10187 -846 -2635 2149 A O
ATOM 2400 CB ARG A 318 18.064 7.441 491.735 1.00 78.28 A C
ANISOU 2400 CB ARG A 318 12197 7100 10444 -756 -2651 1842 A C
ATOM 2401 CG ARG A 318 17.534 6.898 490.430 1.00 79.42 A C
ANISOU 2401 CG ARG A 318 12655 6889 10633 -937 -2834 1939 A C
ATOM 2402 CD ARG A 318 18.600 6.765 489.363 1.00 83.68 A C
ANISOU 2402 CD ARG A 318 13488 7081 11227 -595 -2866 1695 A C
ATOM 2403 NE ARG A 318 17.965 6.423 488.095 1.00 95.73 A N
ANISOU 2403 NE ARG A 318 15293 8294 12786 -779 -3023 1772 A N
ATOM 2404 CZ ARG A 318 17.526 7.320 487.211 1.00 92.96 A C
ANISOU 2404 CZ ARG A 318 14696 8024 12601 -815 -2890 1675 A C
ATOM 2405 NH1 ARG A 318 17.675 8.620 487.448 1.00 90.27 A N1+
ANISOU 2405 NH1 ARG A 318 13856 8038 12407 -666 -2593 1491 A N1+
ATOM 2406 NH2 ARG A 318 16.944 6.916 486.083 1.00 83.24 A N
ANISOU 2406 NH2 ARG A 318 13686 6594 11346 -985 -3018 1720 A N
ATOM 2407 N TYR A 319 17.721 9.056 494.551 1.00 67.76 A N
ANISOU 2407 N TYR A 319 10067 6715 8965 -694 -2227 1825 A N
ATOM 2408 CA TYR A 319 18.263 9.419 495.857 1.00 66.65 A C
ANISOU 2408 CA TYR A 319 9781 6845 8700 -532 -2124 1733 A C
ATOM 2409 C TYR A 319 17.343 8.985 496.992 1.00 80.86 A C
ANISOU 2409 C TYR A 319 11505 8908 10311 -732 -2135 2054 A C
ATOM 2410 O TYR A 319 17.820 8.524 498.035 1.00 84.66 A O
ANISOU 2410 O TYR A 319 12057 9471 10638 -661 -2191 2093 A O
ATOM 2411 CB TYR A 319 18.503 10.923 495.929 1.00 64.43 A C
ANISOU 2411 CB TYR A 319 9203 6784 8494 -351 -1872 1447 A C
ATOM 2412 CG TYR A 319 19.026 11.393 497.267 1.00 68.33 A C
ANISOU 2412 CG TYR A 319 9589 7542 8831 -207 -1786 1336 A C
ATOM 2413 CD1 TYR A 319 20.360 11.214 497.617 1.00 72.50 A C
ANISOU 2413 CD1 TYR A 319 10209 8009 9327 -24 -1878 1163 A C
ATOM 2414 CD2 TYR A 319 18.181 12.016 498.185 1.00 71.73 A C
ANISOU 2414 CD2 TYR A 319 9832 8306 9117 -237 -1616 1426 A C
ATOM 2415 CE1 TYR A 319 20.843 11.647 498.843 1.00 81.39 A C
ANISOU 2415 CE1 TYR A 319 11252 9379 10293 75 -1832 1067 A C
ATOM 2416 CE2 TYR A 319 18.649 12.455 499.419 1.00 77.42 A C
ANISOU 2416 CE2 TYR A 319 10513 9246 9659 -98 -1552 1313 A C
ATOM 2417 CZ TYR A 319 19.982 12.270 499.744 1.00 84.28 A C
ANISOU 2417 CZ TYR A 319 11485 10029 10509 32 -1676 1125 A C
ATOM 2418 OH TYR A 319 20.460 12.706 500.967 1.00 85.30 A O
ANISOU 2418 OH TYR A 319 11590 10376 10445 140 -1646 1017 A O
ATOM 2419 N MET A 320 16.026 9.137 496.824 1.00 81.58 A N
ANISOU 2419 N MET A 320 11424 9174 10400 -972 -2076 2313 A N
ATOM 2420 CA MET A 320 15.112 8.674 497.864 1.00 84.05 A C
ANISOU 2420 CA MET A 320 11631 9782 10523 -1169 -2086 2686 A C
ATOM 2421 C MET A 320 15.129 7.154 497.993 1.00 84.05 A C
ANISOU 2421 C MET A 320 11971 9528 10434 -1405 -2394 2962 A C
ATOM 2422 O MET A 320 15.054 6.616 499.111 1.00 87.27 A O
ANISOU 2422 O MET A 320 12394 10100 10664 -1450 -2437 3161 A O
ATOM 2423 CB MET A 320 13.691 9.173 497.581 1.00 94.04 A C
ANISOU 2423 CB MET A 320 12591 11345 11795 -1366 -1952 2961 A C
ATOM 2424 CG MET A 320 13.438 10.652 497.889 1.00103.48 A C
ANISOU 2424 CG MET A 320 13456 12891 12970 -1102 -1606 2784 A C
ATOM 2425 SD MET A 320 14.289 11.243 499.381 1.00121.13 A S
ANISOU 2425 SD MET A 320 15678 15333 15011 -759 -1448 2529 A S
ATOM 2426 CE MET A 320 13.481 10.298 500.688 1.00112.21 A C
ANISOU 2426 CE MET A 320 14486 14533 13615 -936 -1507 3016 A C
ATOM 2427 N VAL A 321 15.264 6.446 496.868 1.00 79.10 A N
ANISOU 2427 N VAL A 321 11668 8477 9910 -1537 -2617 2971 A N
ATOM 2428 CA VAL A 321 15.463 5.000 496.931 1.00 79.94 A C
ANISOU 2428 CA VAL A 321 12225 8241 9908 -1706 -2929 3177 A C
ATOM 2429 C VAL A 321 16.738 4.664 497.699 1.00 84.45 A C
ANISOU 2429 C VAL A 321 12976 8730 10382 -1378 -2943 2980 A C
ATOM 2430 O VAL A 321 16.755 3.757 498.542 1.00 83.66 A O
ANISOU 2430 O VAL A 321 13059 8613 10113 -1466 -3083 3200 A O
ATOM 2431 CB VAL A 321 15.469 4.395 495.517 1.00 75.19 A C
ANISOU 2431 CB VAL A 321 12019 7151 9401 -1839 -3159 3166 A C
ATOM 2432 CG1 VAL A 321 15.948 2.961 495.564 1.00 78.12 A C
ANISOU 2432 CG1 VAL A 321 12973 7083 9627 -1893 -3470 3290 A C
ATOM 2433 CG2 VAL A 321 14.078 4.475 494.913 1.00 76.53 A C
ANISOU 2433 CG2 VAL A 321 12033 7428 9618 -2266 -3220 3473 A C
ATOM 2434 N THR A 322 17.815 5.409 497.443 1.00 83.46 A N
ANISOU 2434 N THR A 322 12773 8584 10352 -1008 -2800 2590 A N
ATOM 2435 CA THR A 322 19.067 5.193 498.165 1.00 78.40 A C
ANISOU 2435 CA THR A 322 12231 7941 9616 -692 -2808 2423 A C
ATOM 2436 C THR A 322 18.907 5.409 499.670 1.00 77.40 A C
ANISOU 2436 C THR A 322 11867 8215 9326 -691 -2705 2518 A C
ATOM 2437 O THR A 322 19.375 4.598 500.482 1.00 81.61 A O
ANISOU 2437 O THR A 322 12585 8725 9699 -630 -2821 2624 A O
ATOM 2438 CB THR A 322 20.136 6.135 497.603 1.00 71.79 A C
ANISOU 2438 CB THR A 322 11254 7103 8921 -357 -2665 2037 A C
ATOM 2439 CG2 THR A 322 21.423 6.050 498.406 1.00 79.49 A C
ANISOU 2439 CG2 THR A 322 12236 8176 9791 -54 -2667 1896 A C
ATOM 2440 OG1 THR A 322 20.402 5.797 496.240 1.00 67.95 A O
ANISOU 2440 OG1 THR A 322 11033 6236 8551 -298 -2764 1965 A O
ATOM 2441 N VAL A 323 18.236 6.492 500.061 1.00 73.17 A N
ANISOU 2441 N VAL A 323 10952 8047 8804 -729 -2483 2488 A N
ATOM 2442 CA VAL A 323 18.012 6.758 501.478 1.00 77.58 A C
ANISOU 2442 CA VAL A 323 11313 8995 9171 -694 -2368 2579 A C
ATOM 2443 C VAL A 323 17.235 5.611 502.110 1.00 89.18 A C
ANISOU 2443 C VAL A 323 12906 10499 10480 -962 -2519 3014 A C
ATOM 2444 O VAL A 323 17.547 5.161 503.224 1.00 89.43 A O
ANISOU 2444 O VAL A 323 12987 10664 10330 -894 -2554 3106 A O
ATOM 2445 CB VAL A 323 17.303 8.113 501.672 1.00 76.18 A C
ANISOU 2445 CB VAL A 323 10774 9173 8999 -652 -2091 2497 A C
ATOM 2446 CG1 VAL A 323 16.672 8.203 503.061 1.00 81.09 A C
ANISOU 2446 CG1 VAL A 323 11232 10204 9376 -655 -1975 2715 A C
ATOM 2447 CG2 VAL A 323 18.272 9.267 501.437 1.00 69.84 A C
ANISOU 2447 CG2 VAL A 323 9886 8359 8290 -377 -1961 2057 A C
ATOM 2448 N GLN A 324 16.243 5.078 501.387 1.00 96.28 A N
ANISOU 2448 N GLN A 324 13876 11269 11439 -1294 -2637 3307 A N
ATOM 2449 CA GLN A 324 15.456 3.999 501.974 1.00 99.44 A C
ANISOU 2449 CA GLN A 324 14386 11713 11685 -1616 -2808 3769 A C
ATOM 2450 C GLN A 324 16.249 2.702 502.058 1.00 99.09 A C
ANISOU 2450 C GLN A 324 14828 11262 11560 -1608 -3082 3812 A C
ATOM 2451 O GLN A 324 16.048 1.914 502.991 1.00102.70 A O
ANISOU 2451 O GLN A 324 15382 11799 11839 -1732 -3185 4100 A O
ATOM 2452 CB GLN A 324 14.189 3.764 501.153 1.00106.46 A C
ANISOU 2452 CB GLN A 324 15224 12578 12646 -2034 -2906 4107 A C
ATOM 2453 CG GLN A 324 13.192 4.905 501.229 1.00121.18 A C
ANISOU 2453 CG GLN A 324 16584 14928 14531 -2049 -2626 4195 A C
ATOM 2454 CD GLN A 324 12.749 5.205 502.642 1.00131.42 A C
ANISOU 2454 CD GLN A 324 17577 16743 15612 -1959 -2431 4398 A C
ATOM 2455 NE2 GLN A 324 12.217 6.407 502.850 1.00133.13 A N
ANISOU 2455 NE2 GLN A 324 17406 17373 15802 -1773 -2119 4346 A N
ATOM 2456 OE1 GLN A 324 12.903 4.378 503.544 1.00133.14 A O
ANISOU 2456 OE1 GLN A 324 17934 16983 15670 -2020 -2550 4596 A O
ATOM 2457 N ALA A 325 17.179 2.481 501.130 1.00 98.25 A N
ANISOU 2457 N ALA A 325 15037 10735 11560 -1421 -3186 3540 A N
ATOM 2458 CA ALA A 325 18.033 1.303 501.215 1.00101.13 A C
ANISOU 2458 CA ALA A 325 15893 10720 11811 -1305 -3412 3563 A C
ATOM 2459 C ALA A 325 18.988 1.391 502.402 1.00105.46 A C
ANISOU 2459 C ALA A 325 16347 11500 12224 -974 -3317 3433 A C
ATOM 2460 O ALA A 325 19.285 0.374 503.046 1.00102.55 A O
ANISOU 2460 O ALA A 325 16272 11008 11684 -962 -3473 3614 A O
ATOM 2461 CB ALA A 325 18.802 1.126 499.903 1.00 98.44 A C
ANISOU 2461 CB ALA A 325 15894 9922 11586 -1105 -3506 3314 A C
ATOM 2462 N ALA A 326 19.479 2.603 502.702 1.00105.18 A N
ANISOU 2462 N ALA A 326 15925 11788 12249 -719 -3079 3128 A N
ATOM 2463 CA ALA A 326 20.316 2.825 503.886 1.00 94.50 A C
ANISOU 2463 CA ALA A 326 14443 10710 10752 -453 -2999 3009 A C
ATOM 2464 C ALA A 326 19.563 2.607 505.201 1.00 95.22 A C
ANISOU 2464 C ALA A 326 14400 11134 10646 -615 -2965 3299 A C
ATOM 2465 O ALA A 326 20.105 2.001 506.131 1.00 90.70 A O
ANISOU 2465 O ALA A 326 13949 10616 9897 -496 -3038 3377 A O
ATOM 2466 CB ALA A 326 20.922 4.228 503.847 1.00 84.14 A C
ANISOU 2466 CB ALA A 326 12793 9639 9538 -218 -2791 2630 A C
ATOM 2467 N ARG A 327 18.346 3.154 505.338 1.00103.70 A N
ANISOU 2467 N ARG A 327 15191 12482 11726 -843 -2832 3470 A N
ATOM 2468 CA ARG A 327 17.635 2.965 506.608 1.00105.33 A C
ANISOU 2468 CA ARG A 327 15244 13057 11718 -952 -2774 3780 A C
ATOM 2469 C ARG A 327 17.292 1.498 506.872 1.00110.45 A C
ANISOU 2469 C ARG A 327 16206 13508 12252 -1215 -3023 4193 A C
ATOM 2470 O ARG A 327 17.177 1.089 508.035 1.00112.90 A O
ANISOU 2470 O ARG A 327 16488 14049 12358 -1217 -3023 4412 A O
ATOM 2471 CB ARG A 327 16.392 3.853 506.668 1.00104.20 A C
ANISOU 2471 CB ARG A 327 14719 13295 11578 -1087 -2556 3924 A C
ATOM 2472 CG ARG A 327 16.784 5.309 506.553 1.00102.68 A C
ANISOU 2472 CG ARG A 327 14293 13271 11451 -798 -2315 3508 A C
ATOM 2473 CD ARG A 327 15.690 6.299 506.893 1.00105.01 A C
ANISOU 2473 CD ARG A 327 14238 13996 11664 -790 -2047 3620 A C
ATOM 2474 NE ARG A 327 15.065 6.019 508.179 1.00114.02 A N
ANISOU 2474 NE ARG A 327 15259 15526 12536 -803 -1973 3955 A N
ATOM 2475 CZ ARG A 327 13.819 6.355 508.495 1.00115.65 A C
ANISOU 2475 CZ ARG A 327 15182 16135 12625 -877 -1791 4289 A C
ATOM 2476 NH1 ARG A 327 13.058 6.997 507.616 1.00112.13 A N1+
ANISOU 2476 NH1 ARG A 327 14540 15755 12311 -948 -1666 4325 A N1+
ATOM 2477 NH2 ARG A 327 13.341 6.065 509.698 1.00118.23 A N
ANISOU 2477 NH2 ARG A 327 15403 16833 12686 -850 -1719 4607 A N
ATOM 2478 N GLU A 328 17.107 0.698 505.819 1.00111.32 A N
ANISOU 2478 N GLU A 328 16649 13178 12470 -1445 -3246 4313 A N
ATOM 2479 CA GLU A 328 16.879 -0.733 506.004 1.00114.00 A C
ANISOU 2479 CA GLU A 328 17398 13233 12684 -1705 -3526 4685 A C
ATOM 2480 C GLU A 328 18.176 -1.436 506.394 1.00113.47 A C
ANISOU 2480 C GLU A 328 17696 12913 12503 -1374 -3635 4528 A C
ATOM 2481 O GLU A 328 18.180 -2.359 507.223 1.00117.46 A O
ANISOU 2481 O GLU A 328 18414 13394 12822 -1442 -3763 4798 A O
ATOM 2482 CB GLU A 328 16.292 -1.350 504.734 1.00116.73 A C
ANISOU 2482 CB GLU A 328 18067 13142 13144 -2061 -3762 4848 A C
ATOM 2483 CG GLU A 328 15.944 -2.831 504.886 1.00130.07 A C
ANISOU 2483 CG GLU A 328 20201 14512 14708 -2382 -4046 5191 A C
ATOM 2484 CD GLU A 328 16.752 -3.741 503.972 1.00133.06 A C
ANISOU 2484 CD GLU A 328 21137 14287 15132 -2226 -4201 4905 A C
ATOM 2485 OE1 GLU A 328 17.028 -3.340 502.816 1.00137.70 A O
ANISOU 2485 OE1 GLU A 328 21820 14635 15864 -2119 -4201 4649 A O
ATOM 2486 OE2 GLU A 328 17.110 -4.856 504.418 1.00124.08 A O1-
ANISOU 2486 OE2 GLU A 328 20341 12936 13868 -2184 -4304 4940 A O1-
ATOM 2487 N GLN A 329 19.290 -0.977 505.823 1.00106.95 A N
ANISOU 2487 N GLN A 329 16916 11942 11779 -1000 -3573 4118 A N
ATOM 2488 CA GLN A 329 20.609 -1.484 506.181 1.00105.69 A C
ANISOU 2488 CA GLN A 329 17010 11643 11507 -615 -3635 3968 A C
ATOM 2489 C GLN A 329 20.907 -1.288 507.662 1.00107.48 A C
ANISOU 2489 C GLN A 329 16985 12301 11551 -466 -3527 3998 A C
ATOM 2490 O GLN A 329 21.431 -2.198 508.310 1.00114.99 A O
ANISOU 2490 O GLN A 329 18207 13160 12324 -343 -3648 4135 A O
ATOM 2491 CB GLN A 329 21.665 -0.808 505.305 1.00105.89 A C
ANISOU 2491 CB GLN A 329 16987 11566 11682 -258 -3549 3560 A C
ATOM 2492 CG GLN A 329 23.099 -1.174 505.627 1.00116.47 A C
ANISOU 2492 CG GLN A 329 18483 12864 12905 184 -3582 3417 A C
ATOM 2493 CD GLN A 329 23.429 -2.614 505.285 1.00127.47 A C
ANISOU 2493 CD GLN A 329 20501 13770 14163 274 -3812 3610 A C
ATOM 2494 NE2 GLN A 329 23.227 -2.984 504.022 1.00123.82 A N
ANISOU 2494 NE2 GLN A 329 20397 12858 13789 212 -3924 3601 A N
ATOM 2495 OE1 GLN A 329 23.835 -3.398 506.157 1.00129.37 A O
ANISOU 2495 OE1 GLN A 329 20938 14021 14197 404 -3894 3771 A O
ATOM 2496 N LEU A 330 20.622 -0.105 508.208 1.00104.87 A N
ANISOU 2496 N LEU A 330 16180 12426 11239 -442 -3301 3861 A N
ATOM 2497 CA LEU A 330 20.807 0.119 509.643 1.00104.60 A C
ANISOU 2497 CA LEU A 330 15940 12806 10998 -312 -3204 3895 A C
ATOM 2498 C LEU A 330 20.074 -0.941 510.461 1.00109.75 A C
ANISOU 2498 C LEU A 330 16748 13489 11462 -548 -3317 4347 A C
ATOM 2499 O LEU A 330 20.633 -1.522 511.406 1.00115.71 A O
ANISOU 2499 O LEU A 330 17623 14317 12024 -395 -3377 4432 A O
ATOM 2500 CB LEU A 330 20.309 1.522 510.001 1.00102.80 A C
ANISOU 2500 CB LEU A 330 15267 13005 10786 -298 -2952 3731 A C
ATOM 2501 CG LEU A 330 20.709 2.268 511.272 1.00100.98 A C
ANISOU 2501 CG LEU A 330 14807 13201 10358 -74 -2810 3583 A C
ATOM 2502 CD1 LEU A 330 20.300 3.724 511.102 1.00 95.70 A C
ANISOU 2502 CD1 LEU A 330 13834 12772 9756 -36 -2584 3341 A C
ATOM 2503 CD2 LEU A 330 20.080 1.677 512.534 1.00106.75 A C
ANISOU 2503 CD2 LEU A 330 15524 14202 10834 -160 -2805 3944 A C
ATOM 2504 N SER A 331 18.817 -1.218 510.094 1.00114.83 A N
ANISOU 2504 N SER A 331 17383 14093 12156 -941 -3359 4671 A N
ATOM 2505 CA SER A 331 18.037 -2.223 510.807 1.00118.22 A C
ANISOU 2505 CA SER A 331 17939 14565 12414 -1237 -3487 5160 A C
ATOM 2506 C SER A 331 18.659 -3.609 510.673 1.00123.78 A C
ANISOU 2506 C SER A 331 19214 14779 13038 -1234 -3767 5288 A C
ATOM 2507 O SER A 331 18.622 -4.405 511.621 1.00134.82 A O
ANISOU 2507 O SER A 331 20754 16235 14237 -1279 -3853 5572 A O
ATOM 2508 CB SER A 331 16.597 -2.231 510.292 1.00119.47 A C
ANISOU 2508 CB SER A 331 17954 14785 12654 -1701 -3509 5513 A C
ATOM 2509 OG SER A 331 15.862 -3.299 510.867 1.00130.50 A O
ANISOU 2509 OG SER A 331 19502 16187 13896 -2053 -3682 6037 A O
ATOM 2510 N THR A 332 19.222 -3.924 509.499 1.00118.92 A N
ANISOU 2510 N THR A 332 18961 13671 12553 -1155 -3905 5095 A N
ATOM 2511 CA THR A 332 19.889 -5.215 509.325 1.00122.74 A C
ANISOU 2511 CA THR A 332 20033 13665 12936 -1051 -4127 5159 A C
ATOM 2512 C THR A 332 21.162 -5.314 510.169 1.00122.38 A C
ANISOU 2512 C THR A 332 20035 13742 12721 -574 -4091 5012 A C
ATOM 2513 O THR A 332 21.458 -6.374 510.739 1.00122.29 A O
ANISOU 2513 O THR A 332 20315 13590 12561 -501 -4167 5153 A O
ATOM 2514 CB THR A 332 20.193 -5.453 507.844 1.00118.43 A C
ANISOU 2514 CB THR A 332 19802 12624 12571 -996 -4190 4901 A C
ATOM 2515 CG2 THR A 332 20.498 -6.922 507.589 1.00118.94 A C
ANISOU 2515 CG2 THR A 332 20386 12227 12579 -961 -4301 4893 A C
ATOM 2516 OG1 THR A 332 19.054 -5.078 507.059 1.00118.76 A O
ANISOU 2516 OG1 THR A 332 19681 12656 12785 -1412 -4192 4978 A O
ATOM 2517 N THR A 333 21.920 -4.215 510.261 1.00119.15 A N
ANISOU 2517 N THR A 333 19234 13651 12387 -240 -3886 4634 A N
ATOM 2518 CA THR A 333 23.174 -4.173 511.015 1.00120.79 A C
ANISOU 2518 CA THR A 333 19387 14051 12455 198 -3838 4462 A C
ATOM 2519 C THR A 333 22.951 -4.295 512.521 1.00122.46 A C
ANISOU 2519 C THR A 333 19422 14659 12449 166 -3792 4666 A C
ATOM 2520 O THR A 333 23.788 -4.884 513.223 1.00117.67 A O
ANISOU 2520 O THR A 333 18974 14080 11657 436 -3853 4709 A O
ATOM 2521 CB THR A 333 23.942 -2.889 510.681 1.00114.95 A C
ANISOU 2521 CB THR A 333 18258 13561 11857 462 -3665 4039 A C
ATOM 2522 CG2 THR A 333 25.235 -2.800 511.480 1.00115.27 A C
ANISOU 2522 CG2 THR A 333 18194 13859 11743 861 -3644 3897 A C
ATOM 2523 OG1 THR A 333 24.262 -2.873 509.282 1.00115.39 A O
ANISOU 2523 OG1 THR A 333 18501 13247 12094 545 -3707 3870 A O
ATOM 2524 N ALA A 334 21.847 -3.739 513.036 1.00122.72 A N
ANISOU 2524 N ALA A 334 19122 15028 12479 -124 -3672 4808 A N
ATOM 2525 CA ALA A 334 21.594 -3.790 514.477 1.00127.96 A C
ANISOU 2525 CA ALA A 334 19604 16103 12911 -122 -3603 5007 A C
ATOM 2526 C ALA A 334 21.629 -5.222 515.019 1.00130.51 A C
ANISOU 2526 C ALA A 334 20339 16204 13045 -181 -3800 5378 A C
ATOM 2527 O ALA A 334 22.102 -5.463 516.139 1.00123.87 A O
ANISOU 2527 O ALA A 334 19472 15604 11990 16 -3785 5443 A O
ATOM 2528 CB ALA A 334 20.243 -3.140 514.780 1.00122.77 A C
ANISOU 2528 CB ALA A 334 18586 15799 12262 -423 -3446 5194 A C
ATOM 2529 N ASP A 335 21.155 -6.183 514.231 1.00131.78 A N
ANISOU 2529 N ASP A 335 20920 15885 13264 -454 -4001 5623 A N
ATOM 2530 CA ASP A 335 21.082 -7.578 514.652 1.00129.84 A C
ANISOU 2530 CA ASP A 335 21032 15387 12914 -530 -4099 5864 A C
ATOM 2531 C ASP A 335 22.473 -8.206 514.736 1.00124.40 A C
ANISOU 2531 C ASP A 335 20668 14477 12120 -61 -4152 5688 A C
ATOM 2532 O ASP A 335 23.081 -8.248 515.810 1.00124.14 A O
ANISOU 2532 O ASP A 335 20559 14729 11879 198 -4130 5734 A O
ATOM 2533 CB ASP A 335 20.188 -8.370 513.687 1.00133.75 A C
ANISOU 2533 CB ASP A 335 21774 15448 13595 -936 -4181 5964 A C
ATOM 2534 CG ASP A 335 18.860 -7.667 513.401 1.00131.44 A C
ANISOU 2534 CG ASP A 335 21109 15399 13433 -1374 -4122 6124 A C
ATOM 2535 OD1 ASP A 335 18.311 -7.026 514.326 1.00133.76 A O
ANISOU 2535 OD1 ASP A 335 20988 16217 13617 -1441 -3994 6316 A O
ATOM 2536 OD2 ASP A 335 18.368 -7.749 512.252 1.00118.09 A O1-
ANISOU 2536 OD2 ASP A 335 19527 13405 11936 -1626 -4190 6060 A O1-
ATOM 2537 N LYS A 337 25.672 -6.774 515.973 1.00127.52 A N
ANISOU 2537 N LYS A 337 20598 15619 12233 1110 -4017 5076 A N
ATOM 2538 CA LYS A 337 26.364 -5.799 516.810 1.00125.98 A C
ANISOU 2538 CA LYS A 337 19944 15959 11963 1337 -3886 4836 A C
ATOM 2539 C LYS A 337 25.701 -5.729 518.176 1.00131.26 A C
ANISOU 2539 C LYS A 337 20421 17016 12438 1181 -3824 5037 A C
ATOM 2540 O LYS A 337 24.494 -5.956 518.313 1.00130.96 A O
ANISOU 2540 O LYS A 337 20407 16947 12405 832 -3812 5301 A O
ATOM 2541 CB LYS A 337 26.376 -4.410 516.158 1.00121.36 A C
ANISOU 2541 CB LYS A 337 18968 15543 11600 1296 -3749 4470 A C
ATOM 2542 CG LYS A 337 26.764 -4.417 514.692 1.00127.51 A C
ANISOU 2542 CG LYS A 337 19914 15936 12598 1384 -3788 4303 A C
ATOM 2543 CD LYS A 337 28.033 -5.227 514.456 1.00132.74 A C
ANISOU 2543 CD LYS A 337 20866 16416 13152 1810 -3894 4320 A C
ATOM 2544 CE LYS A 337 28.366 -5.308 512.973 1.00132.57 A C
ANISOU 2544 CE LYS A 337 21060 15998 13312 1939 -3921 4187 A C
ATOM 2545 NZ LYS A 337 29.422 -6.325 512.724 1.00138.47 A N1+
ANISOU 2545 NZ LYS A 337 22203 16509 13899 2389 -4017 4293 A N1+
ATOM 2546 N HIS A 338 26.510 -5.412 519.187 1.00134.15 A N
ANISOU 2546 N HIS A 338 20585 17774 12613 1445 -3792 4934 A N
ATOM 2547 CA HIS A 338 26.055 -5.302 520.565 1.00138.18 A C
ANISOU 2547 CA HIS A 338 20923 18689 12891 1383 -3727 5093 A C
ATOM 2548 C HIS A 338 25.930 -3.859 521.040 1.00139.50 A C
ANISOU 2548 C HIS A 338 20663 19302 13039 1375 -3567 4806 A C
ATOM 2549 O HIS A 338 25.369 -3.626 522.118 1.00142.46 A O
ANISOU 2549 O HIS A 338 20898 20018 13211 1323 -3479 4926 A O
ATOM 2550 CB HIS A 338 27.018 -6.058 521.491 1.00135.63 A C
ANISOU 2550 CB HIS A 338 20740 18487 12305 1690 -3826 5215 A C
ATOM 2551 CG HIS A 338 26.480 -6.306 522.868 1.00139.52 A C
ANISOU 2551 CG HIS A 338 21173 19302 12534 1623 -3788 5475 A C
ATOM 2552 CD2 HIS A 338 26.695 -5.661 524.040 1.00143.69 A C
ANISOU 2552 CD2 HIS A 338 21433 20320 12841 1742 -3715 5385 A C
ATOM 2553 ND1 HIS A 338 25.629 -7.350 523.158 1.00145.95 A N
ANISOU 2553 ND1 HIS A 338 22250 19937 13268 1412 -3842 5900 A N
ATOM 2554 CE1 HIS A 338 25.337 -7.335 524.448 1.00148.53 A C
ANISOU 2554 CE1 HIS A 338 22434 20657 13344 1424 -3779 6073 A C
ATOM 2555 NE2 HIS A 338 25.971 -6.320 525.006 1.00147.84 A N
ANISOU 2555 NE2 HIS A 338 22042 20973 13159 1639 -3699 5754 A N
ATOM 2556 N SER A 339 26.430 -2.893 520.272 1.00132.12 A N
ANISOU 2556 N SER A 339 19552 18360 12286 1436 -3528 4441 A N
ATOM 2557 CA SER A 339 26.474 -1.501 520.696 1.00128.60 A C
ANISOU 2557 CA SER A 339 18785 18279 11796 1450 -3411 4136 A C
ATOM 2558 C SER A 339 25.921 -0.593 519.608 1.00127.22 A C
ANISOU 2558 C SER A 339 18483 17963 11892 1282 -3303 3920 A C
ATOM 2559 O SER A 339 25.745 -0.987 518.451 1.00132.47 A O
ANISOU 2559 O SER A 339 19278 18262 12793 1189 -3338 3956 A O
ATOM 2560 CB SER A 339 27.902 -1.060 521.046 1.00127.46 A C
ANISOU 2560 CB SER A 339 18526 18354 11550 1706 -3506 3881 A C
ATOM 2561 OG SER A 339 28.017 0.354 520.987 1.00121.08 A O
ANISOU 2561 OG SER A 339 17482 17742 10781 1662 -3436 3532 A O
ATOM 2562 N SER A 340 25.661 0.652 520.007 1.00122.47 A N
ANISOU 2562 N SER A 340 17659 17647 11226 1264 -3174 3689 A N
ATOM 2563 CA SER A 340 25.211 1.669 519.067 1.00121.02 A C
ANISOU 2563 CA SER A 340 17344 17370 11269 1146 -3057 3453 A C
ATOM 2564 C SER A 340 26.376 2.247 518.270 1.00119.56 A C
ANISOU 2564 C SER A 340 17095 17078 11256 1248 -3142 3116 A C
ATOM 2565 O SER A 340 26.252 2.484 517.062 1.00106.03 A O
ANISOU 2565 O SER A 340 15366 15108 9813 1168 -3114 3008 A O
ATOM 2566 CB SER A 340 24.472 2.772 519.826 1.00120.57 A C
ANISOU 2566 CB SER A 340 17139 17639 11032 1134 -2877 3350 A C
ATOM 2567 OG SER A 340 24.189 3.878 518.987 1.00119.06 A O
ANISOU 2567 OG SER A 340 16839 17373 11028 1069 -2764 3082 A O
ATOM 2568 N HIS A 341 27.516 2.475 518.931 1.00127.08 A N
ANISOU 2568 N HIS A 341 17990 18251 12045 1415 -3255 2974 A N
ATOM 2569 CA HIS A 341 28.708 2.987 518.266 1.00119.16 A C
ANISOU 2569 CA HIS A 341 16876 17225 11176 1500 -3357 2721 A C
ATOM 2570 C HIS A 341 29.335 1.973 517.322 1.00114.85 A C
ANISOU 2570 C HIS A 341 16440 16400 10798 1629 -3450 2857 A C
ATOM 2571 O HIS A 341 30.213 2.343 516.537 1.00109.58 A O
ANISOU 2571 O HIS A 341 15662 15695 10279 1713 -3503 2694 A O
ATOM 2572 CB HIS A 341 29.734 3.435 519.312 1.00124.92 A C
ANISOU 2572 CB HIS A 341 17500 18314 11648 1606 -3484 2600 A C
ATOM 2573 CG HIS A 341 29.371 4.718 519.993 1.00128.49 A C
ANISOU 2573 CG HIS A 341 17896 18983 11941 1502 -3421 2357 A C
ATOM 2574 CD2 HIS A 341 28.469 4.990 520.966 1.00127.00 A C
ANISOU 2574 CD2 HIS A 341 17785 18956 11514 1482 -3306 2398 A C
ATOM 2575 ND1 HIS A 341 29.952 5.924 519.663 1.00127.83 A N
ANISOU 2575 ND1 HIS A 341 17702 18951 11917 1424 -3475 2039 A N
ATOM 2576 CE1 HIS A 341 29.428 6.882 520.408 1.00124.59 A C
ANISOU 2576 CE1 HIS A 341 17358 18682 11298 1364 -3407 1872 A C
ATOM 2577 NE2 HIS A 341 28.524 6.342 521.205 1.00123.29 A N
ANISOU 2577 NE2 HIS A 341 17300 18602 10943 1426 -3289 2084 A N
ATOM 2578 N GLU A 342 28.907 0.711 517.380 1.00125.47 A N
ANISOU 2578 N GLU A 342 18027 17545 12101 1658 -3474 3166 A N
ATOM 2579 CA GLU A 342 29.444 -0.292 516.470 1.00120.17 A C
ANISOU 2579 CA GLU A 342 17568 16548 11543 1821 -3562 3296 A C
ATOM 2580 C GLU A 342 28.875 -0.083 515.076 1.00108.74 A C
ANISOU 2580 C GLU A 342 16181 14746 10389 1683 -3497 3208 A C
ATOM 2581 O GLU A 342 29.584 -0.221 514.075 1.00109.48 A O
ANISOU 2581 O GLU A 342 16324 14650 10622 1848 -3537 3136 A O
ATOM 2582 CB GLU A 342 29.068 -1.685 516.985 1.00126.86 A C
ANISOU 2582 CB GLU A 342 18739 17235 12228 1857 -3627 3655 A C
ATOM 2583 CG GLU A 342 29.885 -2.194 518.183 1.00124.27 A C
ANISOU 2583 CG GLU A 342 18414 17195 11607 2088 -3717 3786 A C
ATOM 2584 CD GLU A 342 31.215 -2.797 517.814 1.00128.50 A C
ANISOU 2584 CD GLU A 342 19031 17692 12103 2451 -3823 3825 A C
ATOM 2585 OE1 GLU A 342 31.459 -3.029 516.610 1.00131.43 A O
ANISOU 2585 OE1 GLU A 342 19536 17750 12653 2555 -3827 3791 A O
ATOM 2586 OE2 GLU A 342 32.017 -3.044 518.741 1.00135.99 A O1-
ANISOU 2586 OE2 GLU A 342 19906 18946 12817 2659 -3896 3908 A O1-
ATOM 2587 N ILE A 343 27.577 0.218 515.013 1.00112.95 A N
ANISOU 2587 N ILE A 343 16706 15214 10997 1400 -3392 3246 A N
ATOM 2588 CA ILE A 343 26.840 0.451 513.770 1.00114.16 A C
ANISOU 2588 CA ILE A 343 16899 15064 11412 1219 -3329 3191 A C
ATOM 2589 C ILE A 343 27.336 1.698 513.029 1.00107.67 A C
ANISOU 2589 C ILE A 343 15823 14309 10776 1254 -3258 2840 A C
ATOM 2590 O ILE A 343 27.452 1.705 511.797 1.00 97.72 A O
ANISOU 2590 O ILE A 343 14625 12773 9733 1268 -3260 2760 A O
ATOM 2591 CB ILE A 343 25.337 0.545 514.105 1.00113.51 A C
ANISOU 2591 CB ILE A 343 16787 15029 11311 918 -3227 3369 A C
ATOM 2592 CG1 ILE A 343 24.792 -0.833 514.506 1.00122.90 A C
ANISOU 2592 CG1 ILE A 343 18273 16053 12371 814 -3332 3773 A C
ATOM 2593 CG2 ILE A 343 24.551 1.152 512.955 1.00100.37 A C
ANISOU 2593 CG2 ILE A 343 15050 13185 9902 720 -3133 3270 A C
ATOM 2594 CD1 ILE A 343 23.432 -0.788 515.175 1.00125.36 A C
ANISOU 2594 CD1 ILE A 343 18480 16561 12588 543 -3237 4032 A C
ATOM 2595 N VAL A 344 27.588 2.782 513.772 1.00114.99 A N
ANISOU 2595 N VAL A 344 16497 15587 11606 1253 -3203 2632 A N
ATOM 2596 CA VAL A 344 28.106 4.045 513.229 1.00106.08 A C
ANISOU 2596 CA VAL A 344 15145 14542 10617 1250 -3161 2305 A C
ATOM 2597 C VAL A 344 29.460 3.877 512.546 1.00102.24 A C
ANISOU 2597 C VAL A 344 14612 14013 10222 1458 -3274 2236 A C
ATOM 2598 O VAL A 344 29.708 4.458 511.481 1.00104.29 A O
ANISOU 2598 O VAL A 344 14774 14152 10699 1450 -3240 2070 A O
ATOM 2599 CB VAL A 344 28.175 5.113 514.340 1.00 99.27 A C
ANISOU 2599 CB VAL A 344 14125 14038 9555 1207 -3131 2126 A C
ATOM 2600 CG1 VAL A 344 28.867 6.372 513.832 1.00 91.81 A C
ANISOU 2600 CG1 VAL A 344 13000 13157 8727 1178 -3142 1804 A C
ATOM 2601 CG2 VAL A 344 26.785 5.431 514.871 1.00102.62 A C
ANISOU 2601 CG2 VAL A 344 14576 14529 9884 1065 -2968 2193 A C
ATOM 2602 N ILE A 345 30.361 3.100 513.148 1.00102.96 A N
ANISOU 2602 N ILE A 345 14751 14237 10134 1670 -3398 2385 A N
ATOM 2603 CA ILE A 345 31.682 2.877 512.564 1.00100.06 A C
ANISOU 2603 CA ILE A 345 14305 13905 9807 1929 -3489 2387 A C
ATOM 2604 C ILE A 345 31.595 2.146 511.226 1.00 99.68 A C
ANISOU 2604 C ILE A 345 14480 13451 9943 2061 -3463 2474 A C
ATOM 2605 O ILE A 345 32.399 2.400 510.318 1.00 96.53 A O
ANISOU 2605 O ILE A 345 13966 13040 9671 2224 -3467 2397 A O
ATOM 2606 CB ILE A 345 32.555 2.126 513.597 1.00100.71 A C
ANISOU 2606 CB ILE A 345 14402 14248 9615 2155 -3614 2578 A C
ATOM 2607 CG1 ILE A 345 33.109 3.097 514.640 1.00 98.27 A C
ANISOU 2607 CG1 ILE A 345 13811 14385 9142 2057 -3687 2432 A C
ATOM 2608 CG2 ILE A 345 33.703 1.383 512.941 1.00112.17 A C
ANISOU 2608 CG2 ILE A 345 15884 15669 11065 2519 -3680 2721 A C
ATOM 2609 CD1 ILE A 345 33.885 2.422 515.743 1.00101.29 A C
ANISOU 2609 CD1 ILE A 345 14184 15063 9237 2249 -3814 2624 A C
ATOM 2610 N GLU A 346 30.611 1.261 511.065 1.00104.78 A N
ANISOU 2610 N GLU A 346 15457 13762 10594 1978 -3448 2646 A N
ATOM 2611 CA GLU A 346 30.491 0.451 509.853 1.00103.39 A C
ANISOU 2611 CA GLU A 346 15601 13143 10539 2093 -3463 2741 A C
ATOM 2612 C GLU A 346 29.957 1.228 508.644 1.00 93.01 A C
ANISOU 2612 C GLU A 346 14207 11632 9500 1922 -3371 2549 A C
ATOM 2613 O GLU A 346 30.386 0.963 507.517 1.00 93.93 A O
ANISOU 2613 O GLU A 346 14458 11507 9725 2114 -3377 2532 A O
ATOM 2614 CB GLU A 346 29.617 -0.772 510.140 1.00107.51 A C
ANISOU 2614 CB GLU A 346 16544 13358 10946 1995 -3528 3016 A C
ATOM 2615 CG GLU A 346 29.373 -1.679 508.949 1.00109.19 A C
ANISOU 2615 CG GLU A 346 17204 13045 11237 2063 -3588 3125 A C
ATOM 2616 CD GLU A 346 28.856 -3.039 509.367 1.00121.39 A C
ANISOU 2616 CD GLU A 346 19231 14292 12602 2015 -3713 3435 A C
ATOM 2617 OE1 GLU A 346 28.206 -3.125 510.432 1.00124.42 A O
ANISOU 2617 OE1 GLU A 346 19544 14854 12876 1784 -3719 3571 A O
ATOM 2618 OE2 GLU A 346 29.079 -4.019 508.624 1.00129.47 A O1-
ANISOU 2618 OE2 GLU A 346 20732 14886 13574 2210 -3809 3553 A O1-
ATOM 2619 N HIS A 347 29.050 2.191 508.835 1.00 91.01 A N
ANISOU 2619 N HIS A 347 13751 11487 9343 1608 -3273 2411 A N
ATOM 2620 CA HIS A 347 28.301 2.788 507.726 1.00 98.58 A C
ANISOU 2620 CA HIS A 347 14682 12229 10547 1423 -3180 2281 A C
ATOM 2621 C HIS A 347 28.546 4.278 507.488 1.00 99.18 A C
ANISOU 2621 C HIS A 347 14396 12526 10762 1354 -3078 1985 A C
ATOM 2622 O HIS A 347 27.941 4.842 506.563 1.00 96.69 A O
ANISOU 2622 O HIS A 347 14041 12047 10649 1219 -2988 1871 A O
ATOM 2623 CB HIS A 347 26.788 2.554 507.897 1.00104.96 A C
ANISOU 2623 CB HIS A 347 15611 12906 11361 1104 -3141 2433 A C
ATOM 2624 CG HIS A 347 26.388 1.109 507.888 1.00116.07 A C
ANISOU 2624 CG HIS A 347 17430 14005 12668 1077 -3270 2740 A C
ATOM 2625 CD2 HIS A 347 25.312 0.478 508.416 1.00120.59 A C
ANISOU 2625 CD2 HIS A 347 18154 14520 13146 820 -3309 3007 A C
ATOM 2626 ND1 HIS A 347 27.126 0.134 507.249 1.00119.01 A N
ANISOU 2626 ND1 HIS A 347 18144 14066 13009 1332 -3389 2821 A N
ATOM 2627 CE1 HIS A 347 26.531 -1.037 507.396 1.00116.92 A C
ANISOU 2627 CE1 HIS A 347 18277 13518 12630 1220 -3512 3100 A C
ATOM 2628 NE2 HIS A 347 25.430 -0.857 508.104 1.00121.82 A N
ANISOU 2628 NE2 HIS A 347 18767 14299 13221 881 -3474 3230 A N
ATOM 2629 N ALA A 348 29.429 4.931 508.256 1.00 99.69 A N
ANISOU 2629 N ALA A 348 14219 12941 10716 1429 -3107 1866 A N
ATOM 2630 CA ALA A 348 29.514 6.392 508.203 1.00 90.60 A C
ANISOU 2630 CA ALA A 348 12794 11974 9656 1292 -3036 1594 A C
ATOM 2631 C ALA A 348 30.106 6.896 506.884 1.00 96.80 A C
ANISOU 2631 C ALA A 348 13461 12643 10677 1362 -3012 1457 A C
ATOM 2632 O ALA A 348 29.822 8.029 506.487 1.00 97.38 A O
ANISOU 2632 O ALA A 348 13387 12726 10885 1206 -2926 1248 A O
ATOM 2633 CB ALA A 348 30.334 6.920 509.381 1.00 85.98 A C
ANISOU 2633 CB ALA A 348 12036 11770 8861 1307 -3125 1520 A C
ATOM 2634 N ALA A 349 30.961 6.113 506.218 1.00 97.00 A N
ANISOU 2634 N ALA A 349 13551 12574 10729 1626 -3078 1578 A N
ATOM 2635 CA ALA A 349 31.440 6.506 504.892 1.00 87.27 A C
ANISOU 2635 CA ALA A 349 12221 11226 9710 1727 -3034 1485 A C
ATOM 2636 C ALA A 349 30.293 6.557 503.884 1.00 85.24 A C
ANISOU 2636 C ALA A 349 12131 10605 9649 1584 -2927 1430 A C
ATOM 2637 O ALA A 349 30.188 7.501 503.080 1.00 84.97 A O
ANISOU 2637 O ALA A 349 11941 10535 9810 1491 -2842 1253 A O
ATOM 2638 CB ALA A 349 32.528 5.543 504.421 1.00 89.72 A C
ANISOU 2638 CB ALA A 349 12614 11521 9955 2116 -3103 1669 A C
ATOM 2639 N ASP A 350 29.377 5.584 503.968 1.00 88.78 A N
ANISOU 2639 N ASP A 350 12892 10799 10040 1526 -2945 1597 A N
ATOM 2640 CA ASP A 350 28.161 5.643 503.167 1.00 88.09 A C
ANISOU 2640 CA ASP A 350 12939 10421 10110 1317 -2872 1586 A C
ATOM 2641 C ASP A 350 27.346 6.869 503.526 1.00 88.73 A C
ANISOU 2641 C ASP A 350 12778 10679 10255 1050 -2745 1425 A C
ATOM 2642 O ASP A 350 26.782 7.522 502.638 1.00 88.21 A O
ANISOU 2642 O ASP A 350 12648 10490 10376 937 -2645 1311 A O
ATOM 2643 CB ASP A 350 27.319 4.380 503.366 1.00 89.84 A C
ANISOU 2643 CB ASP A 350 13528 10385 10223 1230 -2957 1843 A C
ATOM 2644 CG ASP A 350 27.941 3.153 502.730 1.00 99.33 A C
ANISOU 2644 CG ASP A 350 15104 11277 11360 1507 -3077 1989 A C
ATOM 2645 OD1 ASP A 350 28.361 3.250 501.559 1.00106.93 A O
ANISOU 2645 OD1 ASP A 350 16121 12058 12449 1676 -3055 1902 A O
ATOM 2646 OD2 ASP A 350 27.988 2.088 503.389 1.00 98.76 A O1-
ANISOU 2646 OD2 ASP A 350 15304 11129 11093 1577 -3187 2199 A O1-
ATOM 2647 N TRP A 351 27.207 7.161 504.826 1.00 87.70 A N
ANISOU 2647 N TRP A 351 12548 10827 9947 969 -2738 1428 A N
ATOM 2648 CA TRP A 351 26.425 8.337 505.195 1.00 89.25 A C
ANISOU 2648 CA TRP A 351 12578 11181 10151 783 -2600 1278 A C
ATOM 2649 C TRP A 351 27.065 9.615 504.657 1.00 89.18 A C
ANISOU 2649 C TRP A 351 12365 11241 10280 794 -2550 999 A C
ATOM 2650 O TRP A 351 26.355 10.531 504.228 1.00 88.32 A O
ANISOU 2650 O TRP A 351 12186 11091 10281 676 -2414 865 A O
ATOM 2651 CB TRP A 351 26.280 8.407 506.711 1.00 90.77 A C
ANISOU 2651 CB TRP A 351 12748 11659 10080 754 -2609 1326 A C
ATOM 2652 CG TRP A 351 25.573 7.223 507.277 1.00 92.29 A C
ANISOU 2652 CG TRP A 351 13121 11809 10137 711 -2650 1626 A C
ATOM 2653 CD1 TRP A 351 24.886 6.271 506.584 1.00 92.34 A C
ANISOU 2653 CD1 TRP A 351 13315 11537 10232 627 -2682 1843 A C
ATOM 2654 CD2 TRP A 351 25.496 6.849 508.656 1.00 99.88 A C
ANISOU 2654 CD2 TRP A 351 14114 13002 10834 725 -2685 1761 A C
ATOM 2655 CE2 TRP A 351 24.744 5.660 508.724 1.00102.36 A C
ANISOU 2655 CE2 TRP A 351 14618 13171 11103 639 -2730 2077 A C
ATOM 2656 CE3 TRP A 351 25.986 7.408 509.840 1.00102.48 A C
ANISOU 2656 CE3 TRP A 351 14352 13639 10945 786 -2698 1653 A C
ATOM 2657 NE1 TRP A 351 24.386 5.327 507.444 1.00 94.98 A N
ANISOU 2657 NE1 TRP A 351 13792 11913 10382 562 -2743 2120 A N
ATOM 2658 CZ2 TRP A 351 24.469 5.019 509.928 1.00108.49 A C
ANISOU 2658 CZ2 TRP A 351 15464 14120 11639 628 -2766 2298 A C
ATOM 2659 CZ3 TRP A 351 25.712 6.770 511.036 1.00110.76 A C
ANISOU 2659 CZ3 TRP A 351 15478 14860 11745 801 -2728 1855 A C
ATOM 2660 CH2 TRP A 351 24.960 5.589 511.071 1.00114.44 A C
ANISOU 2660 CH2 TRP A 351 16101 15194 12185 729 -2751 2180 A C
ATOM 2661 N CYS A 352 28.403 9.659 504.598 1.00 85.04 A N
ANISOU 2661 N CYS A 352 11739 10822 9751 937 -2660 941 A N
ATOM 2662 CA CYS A 352 29.095 10.825 504.056 1.00 78.85 A C
ANISOU 2662 CA CYS A 352 10750 10111 9097 908 -2645 723 A C
ATOM 2663 C CYS A 352 28.776 10.983 502.585 1.00 78.39 A C
ANISOU 2663 C CYS A 352 10692 9791 9300 920 -2548 675 A C
ATOM 2664 O CYS A 352 28.635 12.108 502.087 1.00 76.04 A O
ANISOU 2664 O CYS A 352 10278 9479 9135 812 -2461 486 A O
ATOM 2665 CB CYS A 352 30.599 10.737 504.277 1.00 80.00 A C
ANISOU 2665 CB CYS A 352 10739 10483 9174 1044 -2799 753 A C
ATOM 2666 SG CYS A 352 31.043 11.185 505.941 1.00 88.77 A S
ANISOU 2666 SG CYS A 352 11787 11946 9994 937 -2924 705 A S
ATOM 2667 N LYS A 353 28.644 9.863 501.874 1.00 81.58 A N
ANISOU 2667 N LYS A 353 11271 9964 9762 1052 -2570 844 A N
ATOM 2668 CA LYS A 353 28.206 9.982 500.495 1.00 79.18 A C
ANISOU 2668 CA LYS A 353 11012 9392 9679 1050 -2486 802 A C
ATOM 2669 C LYS A 353 26.762 10.458 500.499 1.00 79.05 A C
ANISOU 2669 C LYS A 353 11025 9296 9713 815 -2360 765 A C
ATOM 2670 O LYS A 353 26.422 11.467 499.872 1.00 97.11 A O
ANISOU 2670 O LYS A 353 13192 11554 12151 729 -2243 604 A O
ATOM 2671 CB LYS A 353 28.283 8.617 499.793 1.00 80.16 A C
ANISOU 2671 CB LYS A 353 11418 9238 9800 1236 -2563 996 A C
ATOM 2672 CG LYS A 353 29.652 7.931 499.695 1.00 79.20 A C
ANISOU 2672 CG LYS A 353 11320 9182 9588 1570 -2662 1095 A C
ATOM 2673 CD LYS A 353 30.786 8.806 499.214 1.00 86.57 A C
ANISOU 2673 CD LYS A 353 11937 10333 10621 1694 -2635 982 A C
ATOM 2674 CE LYS A 353 32.043 7.956 498.998 1.00 94.77 A C
ANISOU 2674 CE LYS A 353 13005 11456 11548 2089 -2711 1159 A C
ATOM 2675 NZ LYS A 353 33.279 8.767 498.778 1.00 96.47 A N1+
ANISOU 2675 NZ LYS A 353 12829 12012 11814 2190 -2712 1131 A N1+
ATOM 2676 N LEU A 354 25.920 9.760 501.265 1.00 77.16 A N
ANISOU 2676 N LEU A 354 10927 9061 9328 719 -2379 942 A N
ATOM 2677 CA LEU A 354 24.506 10.083 501.435 1.00 78.13 A C
ANISOU 2677 CA LEU A 354 11041 9199 9447 516 -2258 997 A C
ATOM 2678 C LEU A 354 24.253 11.550 501.788 1.00 85.41 A C
ANISOU 2678 C LEU A 354 11772 10318 10361 460 -2104 780 A C
ATOM 2679 O LEU A 354 23.272 12.145 501.324 1.00 75.85 A O
ANISOU 2679 O LEU A 354 10508 9076 9235 366 -1958 760 A O
ATOM 2680 CB LEU A 354 23.911 9.152 502.487 1.00 78.03 A C
ANISOU 2680 CB LEU A 354 11155 9268 9226 441 -2319 1250 A C
ATOM 2681 CG LEU A 354 22.398 9.004 502.441 1.00 82.13 A C
ANISOU 2681 CG LEU A 354 11686 9778 9741 228 -2236 1453 A C
ATOM 2682 CD1 LEU A 354 21.973 8.493 501.091 1.00 82.75 A C
ANISOU 2682 CD1 LEU A 354 11898 9537 10006 135 -2288 1541 A C
ATOM 2683 CD2 LEU A 354 21.985 8.021 503.517 1.00 89.37 A C
ANISOU 2683 CD2 LEU A 354 12716 10798 10443 155 -2319 1737 A C
ATOM 2684 N PHE A 355 25.125 12.158 502.600 1.00101.12 A N
ANISOU 2684 N PHE A 355 13684 12506 12230 519 -2144 625 A N
ATOM 2685 CA PHE A 355 24.867 13.501 503.111 1.00104.61 A C
ANISOU 2685 CA PHE A 355 14057 13098 12593 468 -2027 421 A C
ATOM 2686 C PHE A 355 25.774 14.538 502.474 1.00107.35 A C
ANISOU 2686 C PHE A 355 14303 13406 13079 467 -2045 173 A C
ATOM 2687 O PHE A 355 25.654 15.727 502.791 1.00111.29 A O
ANISOU 2687 O PHE A 355 14806 13967 13511 415 -1972 -21 A O
ATOM 2688 CB PHE A 355 25.114 13.579 504.630 1.00107.17 A C
ANISOU 2688 CB PHE A 355 14429 13670 12622 486 -2086 415 A C
ATOM 2689 CG PHE A 355 24.269 12.651 505.464 1.00105.98 A C
ANISOU 2689 CG PHE A 355 14360 13616 12292 485 -2065 674 A C
ATOM 2690 CD1 PHE A 355 22.896 12.600 505.321 1.00100.78 A C
ANISOU 2690 CD1 PHE A 355 13701 12956 11635 425 -1904 831 A C
ATOM 2691 CD2 PHE A 355 24.861 11.903 506.480 1.00101.08 A C
ANISOU 2691 CD2 PHE A 355 13795 13136 11476 539 -2207 783 A C
ATOM 2692 CE1 PHE A 355 22.144 11.749 506.103 1.00 97.89 A C
ANISOU 2692 CE1 PHE A 355 13378 12717 11098 394 -1898 1116 A C
ATOM 2693 CE2 PHE A 355 24.110 11.068 507.278 1.00 98.97 A C
ANISOU 2693 CE2 PHE A 355 13601 12967 11036 527 -2192 1038 A C
ATOM 2694 CZ PHE A 355 22.748 10.993 507.092 1.00102.64 A C
ANISOU 2694 CZ PHE A 355 14055 13427 11515 443 -2040 1213 A C
ATOM 2695 N ARG A 356 26.631 14.122 501.550 1.00104.55 A N
ANISOU 2695 N ARG A 356 13881 12943 12901 534 -2135 193 A N
ATOM 2696 CA ARG A 356 27.570 14.995 500.861 1.00 97.88 A C
ANISOU 2696 CA ARG A 356 12896 12094 12200 526 -2165 23 A C
ATOM 2697 C ARG A 356 28.295 15.901 501.857 1.00 88.55 A C
ANISOU 2697 C ARG A 356 11675 11124 10848 430 -2264 -128 A C
ATOM 2698 O ARG A 356 28.308 17.127 501.737 1.00 88.16 A O
ANISOU 2698 O ARG A 356 11619 11053 10824 316 -2224 -325 A O
ATOM 2699 CB ARG A 356 26.821 15.794 499.793 1.00 94.33 A C
ANISOU 2699 CB ARG A 356 12429 11462 11952 472 -1996 -94 A C
ATOM 2700 CG ARG A 356 26.241 14.864 498.738 1.00 98.30 A C
ANISOU 2700 CG ARG A 356 12986 11750 12613 540 -1950 62 A C
ATOM 2701 CD ARG A 356 25.618 15.538 497.525 1.00102.74 A C
ANISOU 2701 CD ARG A 356 13508 12138 13389 504 -1803 -28 A C
ATOM 2702 NE ARG A 356 24.266 15.013 497.313 1.00109.89 A N
ANISOU 2702 NE ARG A 356 14509 12943 14299 446 -1716 122 A N
ATOM 2703 CZ ARG A 356 23.946 14.094 496.401 1.00106.40 A C
ANISOU 2703 CZ ARG A 356 14163 12298 13965 462 -1757 270 A C
ATOM 2704 NH1 ARG A 356 24.877 13.604 495.587 1.00101.69 A N1+
ANISOU 2704 NH1 ARG A 356 13604 11564 13470 602 -1851 270 A N1+
ATOM 2705 NH2 ARG A 356 22.690 13.674 496.290 1.00 97.35 A N
ANISOU 2705 NH2 ARG A 356 13086 11098 12805 341 -1711 439 A N
ATOM 2706 N CYS A 357 28.908 15.271 502.857 1.00 88.00 A N
ANISOU 2706 N CYS A 357 11611 11244 10583 468 -2413 -25 A N
ATOM 2707 CA CYS A 357 29.664 15.968 503.888 1.00 96.08 A C
ANISOU 2707 CA CYS A 357 12619 12484 11405 357 -2561 -135 A C
ATOM 2708 C CYS A 357 31.022 15.294 504.036 1.00103.76 A C
ANISOU 2708 C CYS A 357 13419 13661 12342 431 -2763 17 A C
ATOM 2709 O CYS A 357 31.206 14.137 503.646 1.00108.41 A O
ANISOU 2709 O CYS A 357 13981 14221 12988 623 -2766 214 A O
ATOM 2710 CB CYS A 357 28.929 15.997 505.242 1.00 92.06 A C
ANISOU 2710 CB CYS A 357 12301 12070 10606 337 -2534 -153 A C
ATOM 2711 SG CYS A 357 28.559 14.388 505.978 1.00 88.35 A S
ANISOU 2711 SG CYS A 357 11895 11683 9993 486 -2551 131 A S
ATOM 2712 N ASP A 358 31.986 16.037 504.585 1.00104.92 A N
ANISOU 2712 N ASP A 358 13470 14018 12377 280 -2942 -61 A N
ATOM 2713 CA ASP A 358 33.352 15.541 504.729 1.00103.77 A C
ANISOU 2713 CA ASP A 358 13094 14149 12184 337 -3142 117 A C
ATOM 2714 C ASP A 358 33.603 14.745 506.008 1.00 99.32 A C
ANISOU 2714 C ASP A 358 12585 13804 11347 410 -3266 249 A C
ATOM 2715 O ASP A 358 34.613 14.036 506.081 1.00 97.32 A O
ANISOU 2715 O ASP A 358 12147 13782 11046 548 -3394 458 A O
ATOM 2716 CB ASP A 358 34.341 16.706 504.641 1.00108.61 A C
ANISOU 2716 CB ASP A 358 13530 14925 12811 84 -3315 27 A C
ATOM 2717 CG ASP A 358 34.093 17.577 503.425 1.00109.12 A C
ANISOU 2717 CG ASP A 358 13555 14772 13135 -4 -3194 -106 A C
ATOM 2718 OD1 ASP A 358 34.519 17.177 502.320 1.00107.00 A O
ANISOU 2718 OD1 ASP A 358 13082 14500 13074 154 -3136 30 A O
ATOM 2719 OD2 ASP A 358 33.455 18.644 503.566 1.00108.10 A O1-
ANISOU 2719 OD2 ASP A 358 13624 14468 12980 -196 -3144 -340 A O1-
ATOM 2720 N GLY A 359 32.724 14.832 507.005 1.00 98.96 A N
ANISOU 2720 N GLY A 359 12779 13716 11105 355 -3220 158 A N
ATOM 2721 CA GLY A 359 32.962 14.152 508.268 1.00 94.23 A C
ANISOU 2721 CA GLY A 359 12237 13335 10230 416 -3340 279 A C
ATOM 2722 C GLY A 359 31.720 14.091 509.130 1.00 91.91 A C
ANISOU 2722 C GLY A 359 12213 12954 9757 424 -3210 222 A C
ATOM 2723 O GLY A 359 30.793 14.895 508.987 1.00 89.26 A O
ANISOU 2723 O GLY A 359 12023 12450 9443 346 -3060 48 A O
ATOM 2724 N ILE A 360 31.717 13.110 510.032 1.00101.73 A N
ANISOU 2724 N ILE A 360 13510 14337 10805 548 -3259 399 A N
ATOM 2725 CA ILE A 360 30.610 12.865 510.954 1.00103.13 A C
ANISOU 2725 CA ILE A 360 13903 14502 10780 585 -3142 424 A C
ATOM 2726 C ILE A 360 31.143 12.555 512.352 1.00 98.81 A C
ANISOU 2726 C ILE A 360 13402 14235 9906 607 -3309 494 A C
ATOM 2727 O ILE A 360 32.183 11.905 512.497 1.00 99.02 A O
ANISOU 2727 O ILE A 360 13284 14437 9901 676 -3478 643 A O
ATOM 2728 CB ILE A 360 29.704 11.722 510.431 1.00 99.34 A C
ANISOU 2728 CB ILE A 360 13474 13836 10435 718 -2983 640 A C
ATOM 2729 CG1 ILE A 360 28.797 12.237 509.316 1.00 94.96 A C
ANISOU 2729 CG1 ILE A 360 12931 13024 10124 660 -2792 546 A C
ATOM 2730 CG2 ILE A 360 28.884 11.077 511.543 1.00103.04 A C
ANISOU 2730 CG2 ILE A 360 14094 14398 10660 773 -2926 797 A C
ATOM 2731 CD1 ILE A 360 28.287 11.152 508.406 1.00 98.48 A C
ANISOU 2731 CD1 ILE A 360 13400 13252 10767 739 -2719 751 A C
ATOM 2732 N GLY A 361 30.441 13.043 513.383 1.00 98.28 A N
ANISOU 2732 N GLY A 361 13541 14229 9573 577 -3256 397 A N
ATOM 2733 CA GLY A 361 30.742 12.617 514.740 1.00100.54 A C
ANISOU 2733 CA GLY A 361 13905 14767 9531 628 -3384 488 A C
ATOM 2734 C GLY A 361 29.442 12.244 515.432 1.00101.94 A C
ANISOU 2734 C GLY A 361 14260 14936 9535 744 -3182 590 A C
ATOM 2735 O GLY A 361 28.450 12.973 515.353 1.00103.07 A O
ANISOU 2735 O GLY A 361 14534 14976 9653 739 -2994 472 A O
ATOM 2736 N TYR A 362 29.445 11.087 516.100 1.00105.73 A N
ANISOU 2736 N TYR A 362 14736 15547 9889 863 -3215 843 A N
ATOM 2737 CA TYR A 362 28.340 10.573 516.909 1.00103.88 A C
ANISOU 2737 CA TYR A 362 14633 15380 9457 963 -3058 1019 A C
ATOM 2738 C TYR A 362 28.695 10.474 518.386 1.00103.45 A C
ANISOU 2738 C TYR A 362 14687 15607 9015 1029 -3178 1048 A C
ATOM 2739 O TYR A 362 29.658 9.788 518.741 1.00109.70 A O
ANISOU 2739 O TYR A 362 15398 16534 9748 1062 -3370 1161 A O
ATOM 2740 CB TYR A 362 27.897 9.208 516.373 1.00109.62 A C
ANISOU 2740 CB TYR A 362 15304 15977 10371 1020 -2992 1334 A C
ATOM 2741 CG TYR A 362 26.872 8.463 517.202 1.00109.17 A C
ANISOU 2741 CG TYR A 362 15340 16020 10120 1083 -2873 1606 A C
ATOM 2742 CD1 TYR A 362 25.584 8.957 517.361 1.00104.97 A C
ANISOU 2742 CD1 TYR A 362 14853 15519 9513 1076 -2648 1634 A C
ATOM 2743 CD2 TYR A 362 27.182 7.239 517.782 1.00109.98 A C
ANISOU 2743 CD2 TYR A 362 15473 16200 10114 1160 -2977 1872 A C
ATOM 2744 CE1 TYR A 362 24.641 8.264 518.094 1.00110.94 A C
ANISOU 2744 CE1 TYR A 362 15643 16417 10091 1123 -2537 1940 A C
ATOM 2745 CE2 TYR A 362 26.249 6.540 518.514 1.00112.38 A C
ANISOU 2745 CE2 TYR A 362 15850 16599 10249 1187 -2879 2155 A C
ATOM 2746 CZ TYR A 362 24.980 7.052 518.669 1.00115.82 A C
ANISOU 2746 CZ TYR A 362 16292 17099 10616 1156 -2661 2200 A C
ATOM 2747 OH TYR A 362 24.054 6.351 519.413 1.00122.51 A O
ANISOU 2747 OH TYR A 362 17167 18098 11284 1175 -2562 2536 A O
ATOM 2748 N LEU A 363 27.943 11.158 519.246 1.00101.87 A N
ANISOU 2748 N LEU A 363 14675 15506 8526 1079 -3062 957 A N
ATOM 2749 CA LEU A 363 28.244 11.185 520.672 1.00104.60 A C
ANISOU 2749 CA LEU A 363 15170 16111 8462 1154 -3176 954 A C
ATOM 2750 C LEU A 363 27.074 10.526 521.389 1.00104.20 A C
ANISOU 2750 C LEU A 363 15185 16182 8226 1318 -2962 1222 A C
ATOM 2751 O LEU A 363 25.913 10.848 521.114 1.00103.90 A O
ANISOU 2751 O LEU A 363 15178 16083 8214 1372 -2711 1261 A O
ATOM 2752 CB LEU A 363 28.427 12.607 521.199 1.00106.43 A C
ANISOU 2752 CB LEU A 363 15648 16364 8425 1105 -3244 615 A C
ATOM 2753 CG LEU A 363 29.838 13.142 521.403 1.00110.11 A C
ANISOU 2753 CG LEU A 363 16123 16902 8813 921 -3585 419 A C
ATOM 2754 CD1 LEU A 363 30.702 12.870 520.179 1.00110.63 A C
ANISOU 2754 CD1 LEU A 363 15883 16867 9286 778 -3702 453 A C
ATOM 2755 CD2 LEU A 363 29.783 14.621 521.738 1.00112.10 A C
ANISOU 2755 CD2 LEU A 363 16709 17067 8818 836 -3636 76 A C
ATOM 2756 N ARG A 364 27.373 9.628 522.328 1.00106.65 A N
ANISOU 2756 N ARG A 364 15498 16694 8331 1400 -3059 1433 A N
ATOM 2757 CA ARG A 364 26.300 8.961 523.062 1.00112.62 A C
ANISOU 2757 CA ARG A 364 16295 17598 8896 1538 -2869 1732 A C
ATOM 2758 C ARG A 364 26.819 8.581 524.452 1.00118.79 A C
ANISOU 2758 C ARG A 364 17179 18658 9298 1649 -3009 1810 A C
ATOM 2759 O ARG A 364 27.507 7.565 524.609 1.00117.09 A O
ANISOU 2759 O ARG A 364 16874 18492 9123 1648 -3166 1995 A O
ATOM 2760 CB ARG A 364 25.763 7.762 522.288 1.00107.28 A C
ANISOU 2760 CB ARG A 364 15465 16775 8521 1482 -2788 2070 A C
ATOM 2761 CG ARG A 364 24.905 6.855 523.134 1.00115.49 A C
ANISOU 2761 CG ARG A 364 16522 17999 9358 1567 -2673 2451 A C
ATOM 2762 CD ARG A 364 23.438 7.227 522.986 1.00113.59 A C
ANISOU 2762 CD ARG A 364 16249 17811 9100 1586 -2385 2591 A C
ATOM 2763 NE ARG A 364 22.567 6.259 523.645 1.00119.72 A N
ANISOU 2763 NE ARG A 364 16984 18777 9729 1616 -2281 3037 A N
ATOM 2764 CZ ARG A 364 21.243 6.256 523.551 1.00118.12 A C
ANISOU 2764 CZ ARG A 364 16681 18689 9510 1607 -2045 3312 A C
ATOM 2765 NH1 ARG A 364 20.630 7.169 522.807 1.00112.20 A N1+
ANISOU 2765 NH1 ARG A 364 15873 17875 8883 1602 -1876 3171 A N1+
ATOM 2766 NH2 ARG A 364 20.537 5.338 524.202 1.00116.40 A N
ANISOU 2766 NH2 ARG A 364 16406 18675 9146 1600 -1982 3758 A N
ATOM 2767 N GLY A 365 26.490 9.398 525.448 1.00119.75 A N
ANISOU 2767 N GLY A 365 17517 18955 9029 1773 -2949 1671 A N
ATOM 2768 CA GLY A 365 27.029 9.214 526.788 1.00128.64 A C
ANISOU 2768 CA GLY A 365 18779 20346 9755 1877 -3102 1693 A C
ATOM 2769 C GLY A 365 28.537 9.402 526.867 1.00130.01 A C
ANISOU 2769 C GLY A 365 18936 20544 9917 1736 -3451 1492 A C
ATOM 2770 O GLY A 365 29.054 10.502 526.634 1.00124.85 A O
ANISOU 2770 O GLY A 365 18394 19800 9242 1608 -3584 1164 A O
ATOM 2771 N GLU A 366 29.270 8.344 527.222 1.00135.88 A N
ANISOU 2771 N GLU A 366 19544 21430 10655 1754 -3615 1712 A N
ATOM 2772 CA GLU A 366 30.720 8.448 527.349 1.00142.94 A C
ANISOU 2772 CA GLU A 366 20361 22435 11513 1639 -3948 1597 A C
ATOM 2773 C GLU A 366 31.489 8.156 526.062 1.00145.93 A C
ANISOU 2773 C GLU A 366 20474 22652 12319 1516 -4046 1613 A C
ATOM 2774 O GLU A 366 32.715 8.323 526.044 1.00146.53 A O
ANISOU 2774 O GLU A 366 20427 22861 12387 1414 -4314 1547 A O
ATOM 2775 CB GLU A 366 31.201 7.466 528.420 1.00145.32 A C
ANISOU 2775 CB GLU A 366 20642 23019 11554 1772 -4074 1847 A C
ATOM 2776 CG GLU A 366 30.767 7.788 529.836 1.00149.80 A C
ANISOU 2776 CG GLU A 366 21475 23813 11630 1903 -4050 1818 A C
ATOM 2777 CD GLU A 366 30.320 6.545 530.594 1.00152.91 A C
ANISOU 2777 CD GLU A 366 21841 24375 11881 2102 -3939 2196 A C
ATOM 2778 OE1 GLU A 366 30.104 5.498 529.945 1.00146.90 A O
ANISOU 2778 OE1 GLU A 366 20910 23488 11418 2121 -3845 2471 A O
ATOM 2779 OE2 GLU A 366 30.210 6.608 531.840 1.00159.50 A O1-
ANISOU 2779 OE2 GLU A 366 22854 25455 12291 2236 -3962 2223 A O1-
ATOM 2780 N GLU A 367 30.814 7.698 525.013 1.00143.47 A N
ANISOU 2780 N GLU A 367 20067 22089 12356 1530 -3843 1729 A N
ATOM 2781 CA GLU A 367 31.429 7.300 523.750 1.00137.35 A C
ANISOU 2781 CA GLU A 367 19080 21137 11968 1476 -3898 1775 A C
ATOM 2782 C GLU A 367 31.383 8.407 522.695 1.00133.87 A C
ANISOU 2782 C GLU A 367 18604 20487 11776 1310 -3862 1493 A C
ATOM 2783 O GLU A 367 30.381 9.120 522.573 1.00129.92 A O
ANISOU 2783 O GLU A 367 18239 19853 11272 1279 -3672 1355 A O
ATOM 2784 CB GLU A 367 30.787 6.020 523.215 1.00136.82 A C
ANISOU 2784 CB GLU A 367 18989 20886 12109 1584 -3740 2089 A C
ATOM 2785 CG GLU A 367 31.031 4.794 524.069 1.00138.67 A C
ANISOU 2785 CG GLU A 367 19258 21284 12148 1746 -3807 2398 A C
ATOM 2786 CD GLU A 367 32.240 4.007 523.593 1.00138.44 A C
ANISOU 2786 CD GLU A 367 19096 21265 12239 1852 -3978 2531 A C
ATOM 2787 OE1 GLU A 367 32.882 4.438 522.610 1.00128.65 A O
ANISOU 2787 OE1 GLU A 367 17712 19936 11234 1796 -4040 2392 A O
ATOM 2788 OE2 GLU A 367 32.558 2.968 524.209 1.00147.24 A O1-
ANISOU 2788 OE2 GLU A 367 20251 22496 13199 2016 -4042 2791 A O1-
ATOM 2789 N LEU A 368 32.478 8.545 521.936 1.00133.23 A N
ANISOU 2789 N LEU A 368 18326 20400 11894 1224 -4034 1436 A N
ATOM 2790 CA LEU A 368 32.574 9.497 520.830 1.00123.55 A C
ANISOU 2790 CA LEU A 368 17030 18978 10935 1061 -4018 1207 A C
ATOM 2791 C LEU A 368 33.218 8.752 519.667 1.00117.11 A C
ANISOU 2791 C LEU A 368 15976 18068 10451 1127 -4039 1368 A C
ATOM 2792 O LEU A 368 34.300 8.179 519.816 1.00118.97 A O
ANISOU 2792 O LEU A 368 16047 18517 10640 1209 -4217 1527 A O
ATOM 2793 CB LEU A 368 33.403 10.731 521.213 1.00132.51 A C
ANISOU 2793 CB LEU A 368 18193 20259 11898 846 -4259 947 A C
ATOM 2794 CG LEU A 368 33.128 11.418 522.566 1.00144.40 A C
ANISOU 2794 CG LEU A 368 19999 21901 12966 808 -4331 789 A C
ATOM 2795 CD1 LEU A 368 33.772 10.690 523.763 1.00137.44 A C
ANISOU 2795 CD1 LEU A 368 19098 21353 11770 897 -4519 973 A C
ATOM 2796 CD2 LEU A 368 33.584 12.877 522.533 1.00150.37 A C
ANISOU 2796 CD2 LEU A 368 20900 22608 13627 540 -4519 466 A C
ATOM 2797 N THR A 369 32.566 8.798 518.506 1.00118.06 A N
ANISOU 2797 N THR A 369 16087 17887 10883 1115 -3856 1333 A N
ATOM 2798 CA THR A 369 33.046 8.221 517.251 1.00117.47 A C
ANISOU 2798 CA THR A 369 15850 17662 11122 1198 -3845 1447 A C
ATOM 2799 C THR A 369 33.181 9.255 516.139 1.00121.01 A C
ANISOU 2799 C THR A 369 16190 17958 11829 1043 -3820 1224 A C
ATOM 2800 O THR A 369 32.279 10.078 515.953 1.00122.48 A O
ANISOU 2800 O THR A 369 16498 17976 12065 920 -3681 1030 A O
ATOM 2801 CB THR A 369 32.104 7.104 516.781 1.00112.08 A C
ANISOU 2801 CB THR A 369 15298 16711 10576 1331 -3664 1659 A C
ATOM 2802 CG2 THR A 369 32.606 6.505 515.478 1.00108.83 A C
ANISOU 2802 CG2 THR A 369 14803 16106 10443 1453 -3661 1760 A C
ATOM 2803 OG1 THR A 369 32.061 6.063 517.761 1.00122.10 A O
ANISOU 2803 OG1 THR A 369 16671 18108 11613 1472 -3702 1902 A O
ATOM 2804 N THR A 370 34.308 9.236 515.411 1.00121.71 A N
ANISOU 2804 N THR A 370 16046 18134 12065 1069 -3945 1271 A N
ATOM 2805 CA THR A 370 34.523 10.195 514.332 1.00115.99 A C
ANISOU 2805 CA THR A 370 15194 17289 11589 918 -3931 1091 A C
ATOM 2806 C THR A 370 34.873 9.437 513.055 1.00101.66 A C
ANISOU 2806 C THR A 370 13245 15336 10046 1119 -3859 1256 A C
ATOM 2807 O THR A 370 35.491 8.370 513.087 1.00103.84 A O
ANISOU 2807 O THR A 370 13462 15723 10270 1366 -3910 1506 A O
ATOM 2808 CB THR A 370 35.660 11.193 514.648 1.00121.04 A C
ANISOU 2808 CB THR A 370 15653 18216 12121 698 -4185 985 A C
ATOM 2809 CG2 THR A 370 35.419 11.880 515.978 1.00122.92 A C
ANISOU 2809 CG2 THR A 370 16101 18575 12028 523 -4297 822 A C
ATOM 2810 OG1 THR A 370 36.916 10.499 514.705 1.00126.84 A O
ANISOU 2810 OG1 THR A 370 16119 19269 12804 838 -4356 1242 A O
ATOM 2811 N TYR A 371 34.446 10.001 511.926 1.00 97.16 A N
ANISOU 2811 N TYR A 371 12663 14512 9744 1041 -3731 1116 A N
ATOM 2812 CA TYR A 371 34.818 9.565 510.585 1.00 99.97 A C
ANISOU 2812 CA TYR A 371 12901 14725 10356 1211 -3666 1219 A C
ATOM 2813 C TYR A 371 35.126 10.729 509.657 1.00 98.11 A C
ANISOU 2813 C TYR A 371 12489 14455 10332 1034 -3664 1039 A C
ATOM 2814 O TYR A 371 34.369 11.704 509.607 1.00 97.56 A O
ANISOU 2814 O TYR A 371 12524 14228 10318 813 -3588 802 A O
ATOM 2815 CB TYR A 371 33.726 8.721 509.923 1.00100.83 A C
ANISOU 2815 CB TYR A 371 13250 14455 10607 1341 -3476 1290 A C
ATOM 2816 CG TYR A 371 34.089 8.394 508.496 1.00 96.19 A C
ANISOU 2816 CG TYR A 371 12601 13687 10259 1517 -3415 1356 A C
ATOM 2817 CD1 TYR A 371 35.080 7.471 508.200 1.00 97.16 A C
ANISOU 2817 CD1 TYR A 371 12663 13916 10337 1836 -3480 1589 A C
ATOM 2818 CD2 TYR A 371 33.476 9.063 507.443 1.00 91.06 A C
ANISOU 2818 CD2 TYR A 371 11960 12784 9857 1398 -3286 1190 A C
ATOM 2819 CE1 TYR A 371 35.422 7.192 506.891 1.00 96.39 A C
ANISOU 2819 CE1 TYR A 371 12544 13659 10421 2051 -3411 1653 A C
ATOM 2820 CE2 TYR A 371 33.819 8.799 506.135 1.00 92.74 A C
ANISOU 2820 CE2 TYR A 371 12130 12837 10268 1573 -3230 1245 A C
ATOM 2821 CZ TYR A 371 34.787 7.860 505.864 1.00 93.14 A C
ANISOU 2821 CZ TYR A 371 12148 12984 10255 1907 -3291 1474 A C
ATOM 2822 OH TYR A 371 35.132 7.598 504.561 1.00 91.77 A O
ANISOU 2822 OH TYR A 371 11969 12658 10243 2136 -3221 1535 A O
ATOM 2823 N GLY A 372 36.204 10.614 508.884 1.00 96.03 A N
ANISOU 2823 N GLY A 372 11967 14341 10179 1159 -3730 1172 A N
ATOM 2824 CA GLY A 372 36.490 11.711 507.990 1.00 96.93 A C
ANISOU 2824 CA GLY A 372 11902 14431 10496 975 -3729 1029 A C
ATOM 2825 C GLY A 372 37.090 12.909 508.693 1.00100.88 A C
ANISOU 2825 C GLY A 372 12272 15190 10869 628 -3940 901 A C
ATOM 2826 O GLY A 372 37.620 12.819 509.803 1.00105.35 A O
ANISOU 2826 O GLY A 372 12803 16045 11180 563 -4126 972 A O
ATOM 2827 N GLU A 373 37.039 14.047 508.006 1.00100.38 A N
ANISOU 2827 N GLU A 373 12156 15011 10973 390 -3928 718 A N
ATOM 2828 CA GLU A 373 37.703 15.236 508.511 1.00111.61 A C
ANISOU 2828 CA GLU A 373 13489 16635 12281 17 -4167 609 A C
ATOM 2829 C GLU A 373 36.863 15.797 509.647 1.00111.66 A C
ANISOU 2829 C GLU A 373 13865 16507 12054 -167 -4190 362 A C
ATOM 2830 O GLU A 373 35.718 16.211 509.440 1.00104.42 A O
ANISOU 2830 O GLU A 373 13216 15257 11202 -176 -3992 151 A O
ATOM 2831 CB GLU A 373 37.828 16.276 507.397 1.00113.54 A C
ANISOU 2831 CB GLU A 373 13622 16746 12773 -179 -4138 493 A C
ATOM 2832 CG GLU A 373 38.456 15.783 506.101 1.00111.72 A C
ANISOU 2832 CG GLU A 373 13064 16595 12790 57 -4048 718 A C
ATOM 2833 CD GLU A 373 39.959 15.609 506.193 1.00119.86 A C
ANISOU 2833 CD GLU A 373 13670 18131 13739 56 -4275 1030 A C
ATOM 2834 OE1 GLU A 373 40.558 15.998 507.223 1.00123.46 A O
ANISOU 2834 OE1 GLU A 373 14066 18876 13967 -211 -4542 1060 A O
ATOM 2835 OE2 GLU A 373 40.541 15.082 505.223 1.00120.34 A O1-
ANISOU 2835 OE2 GLU A 373 13458 18320 13945 337 -4187 1265 A O1-
ATOM 2836 N THR A 374 37.436 15.825 510.840 1.00118.22 A N
ANISOU 2836 N THR A 374 14710 17618 12589 -292 -4428 406 A N
ATOM 2837 CA THR A 374 36.747 16.371 511.993 1.00115.95 A C
ANISOU 2837 CA THR A 374 14801 17234 12021 -433 -4469 182 A C
ATOM 2838 C THR A 374 37.733 17.141 512.857 1.00128.19 A C
ANISOU 2838 C THR A 374 16341 19057 13310 -778 -4837 153 A C
ATOM 2839 O THR A 374 38.937 16.861 512.840 1.00137.39 A O
ANISOU 2839 O THR A 374 17148 20588 14465 -845 -5060 395 A O
ATOM 2840 CB THR A 374 36.139 15.196 512.782 1.00111.55 A C
ANISOU 2840 CB THR A 374 14370 16708 11305 -138 -4344 303 A C
ATOM 2841 CG2 THR A 374 35.528 15.599 514.096 1.00112.70 A C
ANISOU 2841 CG2 THR A 374 14874 16840 11107 -215 -4384 134 A C
ATOM 2842 OG1 THR A 374 35.135 14.554 511.990 1.00117.42 A O
ANISOU 2842 OG1 THR A 374 15173 17168 12275 106 -4038 332 A O
ATOM 2843 N PRO A 375 37.246 18.102 513.640 1.00128.21 A N
ANISOU 2843 N PRO A 375 16747 18899 13066 -992 -4917 -120 A N
ATOM 2844 CA PRO A 375 38.070 18.717 514.685 1.00128.85 A C
ANISOU 2844 CA PRO A 375 16930 19211 12816 -1322 -5301 -155 A C
ATOM 2845 C PRO A 375 38.429 17.683 515.740 1.00125.10 A C
ANISOU 2845 C PRO A 375 16362 19073 12098 -1150 -5401 53 A C
ATOM 2846 O PRO A 375 37.893 16.574 515.776 1.00120.48 A O
ANISOU 2846 O PRO A 375 15726 18485 11568 -781 -5160 184 A O
ATOM 2847 CB PRO A 375 37.180 19.829 515.241 1.00126.39 A C
ANISOU 2847 CB PRO A 375 17197 18553 12270 -1457 -5276 -518 A C
ATOM 2848 CG PRO A 375 36.294 20.182 514.103 1.00121.46 A C
ANISOU 2848 CG PRO A 375 16630 17567 11951 -1338 -4955 -653 A C
ATOM 2849 CD PRO A 375 36.025 18.890 513.385 1.00120.75 A C
ANISOU 2849 CD PRO A 375 16188 17540 12154 -979 -4683 -414 A C
ATOM 2850 N ASP A 376 39.364 18.031 516.606 1.00128.52 A N
ANISOU 2850 N ASP A 376 16779 19803 12250 -1438 -5779 103 A N
ATOM 2851 CA ASP A 376 39.713 17.004 517.565 1.00130.95 A C
ANISOU 2851 CA ASP A 376 16972 20448 12334 -1244 -5858 321 A C
ATOM 2852 C ASP A 376 38.611 16.935 518.633 1.00129.49 A C
ANISOU 2852 C ASP A 376 17279 20068 11854 -1076 -5716 119 A C
ATOM 2853 O ASP A 376 37.717 17.784 518.694 1.00129.62 A O
ANISOU 2853 O ASP A 376 17716 19736 11796 -1131 -5599 -179 A O
ATOM 2854 CB ASP A 376 41.116 17.252 518.125 1.00135.07 A C
ANISOU 2854 CB ASP A 376 17244 21427 12651 -1583 -6311 507 A C
ATOM 2855 CG ASP A 376 41.223 18.544 518.901 1.00144.09 A C
ANISOU 2855 CG ASP A 376 18806 22466 13475 -2049 -6643 241 A C
ATOM 2856 OD1 ASP A 376 40.246 19.323 518.900 1.00143.28 A O
ANISOU 2856 OD1 ASP A 376 19194 21920 13324 -2076 -6499 -99 A O
ATOM 2857 OD2 ASP A 376 42.291 18.780 519.508 1.00151.01 A O1-
ANISOU 2857 OD2 ASP A 376 19541 23709 14128 -2383 -7059 386 A O1-
ATOM 2858 N GLN A 377 38.668 15.887 519.459 1.00125.62 A N
ANISOU 2858 N GLN A 377 16724 19821 11185 -830 -5706 311 A N
ATOM 2859 CA GLN A 377 37.605 15.587 520.424 1.00125.43 A C
ANISOU 2859 CA GLN A 377 17084 19671 10902 -600 -5524 205 A C
ATOM 2860 C GLN A 377 37.242 16.805 521.278 1.00135.70 A C
ANISOU 2860 C GLN A 377 18906 20813 11841 -823 -5665 -121 A C
ATOM 2861 O GLN A 377 36.056 17.076 521.529 1.00138.35 A O
ANISOU 2861 O GLN A 377 19620 20880 12067 -643 -5407 -307 A O
ATOM 2862 CB GLN A 377 38.028 14.382 521.269 1.00125.81 A C
ANISOU 2862 CB GLN A 377 16962 20070 10771 -382 -5589 489 A C
ATOM 2863 CG GLN A 377 37.183 14.084 522.487 1.00127.13 A C
ANISOU 2863 CG GLN A 377 17489 20220 10595 -190 -5484 432 A C
ATOM 2864 CD GLN A 377 37.293 12.618 522.914 1.00124.86 A C
ANISOU 2864 CD GLN A 377 16998 20167 10275 127 -5405 757 A C
ATOM 2865 NE2 GLN A 377 38.295 11.921 522.388 1.00124.56 A N
ANISOU 2865 NE2 GLN A 377 16547 20366 10415 179 -5509 1026 A N
ATOM 2866 OE1 GLN A 377 36.488 12.126 523.702 1.00121.20 A O
ANISOU 2866 OE1 GLN A 377 16757 19679 9613 340 -5246 785 A O
ATOM 2867 N THR A 378 38.254 17.555 521.721 1.00141.02 A N
ANISOU 2867 N THR A 378 19622 21657 12303 -1209 -6082 -172 A N
ATOM 2868 CA THR A 378 38.043 18.716 522.586 1.00140.06 A C
ANISOU 2868 CA THR A 378 20079 21360 11776 -1444 -6284 -484 A C
ATOM 2869 C THR A 378 37.181 19.768 521.898 1.00144.20 A C
ANISOU 2869 C THR A 378 20968 21415 12408 -1479 -6086 -790 A C
ATOM 2870 O THR A 378 36.238 20.301 522.498 1.00146.42 A O
ANISOU 2870 O THR A 378 21789 21444 12400 -1328 -5943 -1033 A O
ATOM 2871 CB THR A 378 39.383 19.338 522.953 1.00134.01 A C
ANISOU 2871 CB THR A 378 19252 20844 10821 -1943 -6817 -446 A C
ATOM 2872 CG2 THR A 378 39.194 20.352 524.066 1.00138.06 A C
ANISOU 2872 CG2 THR A 378 20453 21181 10820 -2155 -7070 -750 A C
ATOM 2873 OG1 THR A 378 40.273 18.313 523.384 1.00134.65 A O
ANISOU 2873 OG1 THR A 378 18881 21417 10863 -1887 -6981 -102 A O
ATOM 2874 N THR A 379 37.495 20.078 520.633 1.00138.78 A N
ANISOU 2874 N THR A 379 19989 20623 12118 -1644 -6062 -762 A N
ATOM 2875 CA THR A 379 36.702 21.039 519.873 1.00127.94 A C
ANISOU 2875 CA THR A 379 18919 18811 10880 -1662 -5859 -1027 A C
ATOM 2876 C THR A 379 35.265 20.554 519.749 1.00123.31 A C
ANISOU 2876 C THR A 379 18458 18029 10365 -1187 -5367 -1067 A C
ATOM 2877 O THR A 379 34.324 21.356 519.781 1.00123.88 A O
ANISOU 2877 O THR A 379 18984 17780 10305 -1084 -5181 -1317 A O
ATOM 2878 CB THR A 379 37.317 21.248 518.489 1.00122.08 A C
ANISOU 2878 CB THR A 379 17751 18050 10583 -1876 -5891 -928 A C
ATOM 2879 CG2 THR A 379 36.535 22.290 517.714 1.00119.72 A C
ANISOU 2879 CG2 THR A 379 17779 17299 10412 -1908 -5699 -1202 A C
ATOM 2880 OG1 THR A 379 38.664 21.710 518.628 1.00128.35 A O
ANISOU 2880 OG1 THR A 379 18382 19090 11295 -2349 -6364 -832 A O
ATOM 2881 N ILE A 380 35.080 19.243 519.581 1.00118.91 A N
ANISOU 2881 N ILE A 380 17506 17665 10007 -894 -5158 -797 A N
ATOM 2882 CA ILE A 380 33.736 18.681 519.497 1.00114.87 A C
ANISOU 2882 CA ILE A 380 17071 17015 9558 -498 -4729 -767 A C
ATOM 2883 C ILE A 380 32.986 18.961 520.795 1.00114.89 A C
ANISOU 2883 C ILE A 380 17564 17006 9083 -324 -4669 -900 A C
ATOM 2884 O ILE A 380 31.780 19.256 520.792 1.00112.33 A O
ANISOU 2884 O ILE A 380 17505 16490 8687 -77 -4351 -999 A O
ATOM 2885 CB ILE A 380 33.810 17.173 519.193 1.00113.26 A C
ANISOU 2885 CB ILE A 380 16417 17016 9602 -274 -4596 -430 A C
ATOM 2886 CG1 ILE A 380 34.096 16.937 517.712 1.00112.05 A C
ANISOU 2886 CG1 ILE A 380 15881 16766 9925 -310 -4511 -330 A C
ATOM 2887 CG2 ILE A 380 32.515 16.476 519.578 1.00107.41 A C
ANISOU 2887 CG2 ILE A 380 15798 16226 8785 73 -4254 -339 A C
ATOM 2888 CD1 ILE A 380 34.176 15.475 517.350 1.00111.80 A C
ANISOU 2888 CD1 ILE A 380 15505 16869 10107 -68 -4392 -14 A C
ATOM 2889 N ASN A 381 33.705 18.936 521.924 1.00121.53 A N
ANISOU 2889 N ASN A 381 18540 18074 9563 -441 -4979 -894 A N
ATOM 2890 CA ASN A 381 33.069 19.241 523.204 1.00120.85 A C
ANISOU 2890 CA ASN A 381 18961 17984 8972 -258 -4942 -1027 A C
ATOM 2891 C ASN A 381 32.773 20.735 523.345 1.00122.89 A C
ANISOU 2891 C ASN A 381 19826 17914 8953 -371 -5007 -1389 A C
ATOM 2892 O ASN A 381 31.755 21.114 523.942 1.00124.14 A O
ANISOU 2892 O ASN A 381 20435 17946 8787 -67 -4775 -1519 A O
ATOM 2893 CB ASN A 381 33.953 18.754 524.355 1.00124.04 A C
ANISOU 2893 CB ASN A 381 19344 18728 9059 -351 -5272 -911 A C
ATOM 2894 CG ASN A 381 34.082 17.232 524.401 1.00122.25 A C
ANISOU 2894 CG ASN A 381 18628 18803 9016 -143 -5163 -550 A C
ATOM 2895 ND2 ASN A 381 34.497 16.708 525.551 1.00125.17 A N
ANISOU 2895 ND2 ASN A 381 19038 19465 9058 -95 -5340 -434 A N
ATOM 2896 OD1 ASN A 381 33.808 16.542 523.422 1.00118.24 A O
ANISOU 2896 OD1 ASN A 381 17755 18248 8922 -23 -4931 -380 A O
ATOM 2897 N LYS A 382 33.646 21.602 522.813 1.00124.65 A N
ANISOU 2897 N LYS A 382 20090 17999 9272 -791 -5321 -1534 A N
ATOM 2898 CA LYS A 382 33.326 23.030 522.746 1.00132.58 A C
ANISOU 2898 CA LYS A 382 21703 18611 10061 -906 -5368 -1875 A C
ATOM 2899 C LYS A 382 32.072 23.303 521.914 1.00137.47 A C
ANISOU 2899 C LYS A 382 22394 18952 10887 -580 -4895 -1951 A C
ATOM 2900 O LYS A 382 31.257 24.161 522.274 1.00145.06 A O
ANISOU 2900 O LYS A 382 23944 19652 11519 -370 -4742 -2181 A O
ATOM 2901 CB LYS A 382 34.500 23.813 522.152 1.00134.70 A C
ANISOU 2901 CB LYS A 382 21915 18792 10474 -1464 -5788 -1952 A C
ATOM 2902 CG LYS A 382 35.875 23.395 522.619 1.00141.12 A C
ANISOU 2902 CG LYS A 382 22410 19979 11232 -1837 -6251 -1763 A C
ATOM 2903 CD LYS A 382 36.951 24.273 521.990 1.00143.82 A C
ANISOU 2903 CD LYS A 382 22691 20250 11705 -2417 -6660 -1802 A C
ATOM 2904 CE LYS A 382 38.303 24.063 522.663 1.00151.98 A C
ANISOU 2904 CE LYS A 382 23506 21681 12559 -2831 -7181 -1615 A C
ATOM 2905 NZ LYS A 382 39.304 25.079 522.233 1.00156.15 A N1+
ANISOU 2905 NZ LYS A 382 23958 22124 13250 -3372 -7472 -1634 A N1+
ATOM 2906 N LEU A 383 31.905 22.594 520.793 1.00130.71 A N
ANISOU 2906 N LEU A 383 20965 18150 10548 -515 -4664 -1750 A N
ATOM 2907 CA LEU A 383 30.706 22.747 519.968 1.00126.46 A C
ANISOU 2907 CA LEU A 383 20428 17398 10225 -222 -4225 -1775 A C
ATOM 2908 C LEU A 383 29.459 22.310 520.724 1.00128.45 A C
ANISOU 2908 C LEU A 383 20854 17745 10206 252 -3867 -1691 A C
ATOM 2909 O LEU A 383 28.482 23.064 520.823 1.00132.54 A O
ANISOU 2909 O LEU A 383 21785 18071 10503 516 -3614 -1841 A O
ATOM 2910 CB LEU A 383 30.849 21.990 518.646 1.00123.13 A C
ANISOU 2910 CB LEU A 383 19372 17025 10385 -272 -4095 -1560 A C
ATOM 2911 CG LEU A 383 31.766 22.680 517.633 1.00126.58 A C
ANISOU 2911 CG LEU A 383 19669 17312 11114 -662 -4327 -1654 A C
ATOM 2912 CD1 LEU A 383 31.895 21.859 516.362 1.00119.27 A C
ANISOU 2912 CD1 LEU A 383 18145 16452 10721 -643 -4180 -1429 A C
ATOM 2913 CD2 LEU A 383 31.255 24.082 517.312 1.00130.12 A C
ANISOU 2913 CD2 LEU A 383 20617 17372 11449 -701 -4257 -1957 A C
ATOM 2914 N VAL A 384 29.460 21.067 521.219 1.00123.97 A N
ANISOU 2914 N VAL A 384 19952 17493 9656 385 -3826 -1416 A N
ATOM 2915 CA VAL A 384 28.313 20.541 521.962 1.00120.92 A C
ANISOU 2915 CA VAL A 384 19662 17259 9023 806 -3499 -1265 A C
ATOM 2916 C VAL A 384 27.914 21.527 523.051 1.00128.88 A C
ANISOU 2916 C VAL A 384 21348 18180 9439 998 -3499 -1504 A C
ATOM 2917 O VAL A 384 26.763 21.981 523.122 1.00128.37 A O
ANISOU 2917 O VAL A 384 21553 18035 9187 1356 -3155 -1538 A O
ATOM 2918 CB VAL A 384 28.638 19.157 522.551 1.00122.34 A C
ANISOU 2918 CB VAL A 384 19483 17778 9222 846 -3566 -959 A C
ATOM 2919 CG1 VAL A 384 27.596 18.756 523.585 1.00126.82 A C
ANISOU 2919 CG1 VAL A 384 20228 18535 9424 1237 -3302 -811 A C
ATOM 2920 CG2 VAL A 384 28.739 18.118 521.449 1.00120.79 A C
ANISOU 2920 CG2 VAL A 384 18711 17621 9564 777 -3479 -702 A C
ATOM 2921 N GLU A 385 28.875 21.868 523.917 1.00140.72 A N
ANISOU 2921 N GLU A 385 23147 19711 10611 777 -3893 -1656 A N
ATOM 2922 CA GLU A 385 28.622 22.813 525.001 1.00141.44 A C
ANISOU 2922 CA GLU A 385 23976 19681 10084 941 -3956 -1909 A C
ATOM 2923 C GLU A 385 28.068 24.144 524.479 1.00142.41 A C
ANISOU 2923 C GLU A 385 24601 19400 10107 1023 -3820 -2197 A C
ATOM 2924 O GLU A 385 27.134 24.696 525.072 1.00143.40 A O
ANISOU 2924 O GLU A 385 25244 19444 9799 1446 -3567 -2297 A O
ATOM 2925 CB GLU A 385 29.873 22.982 525.871 1.00142.17 A C
ANISOU 2925 CB GLU A 385 24292 19846 9879 586 -4476 -2024 A C
ATOM 2926 CG GLU A 385 30.233 21.664 526.603 1.00148.07 A C
ANISOU 2926 CG GLU A 385 24627 21022 10612 636 -4545 -1725 A C
ATOM 2927 CD GLU A 385 31.514 21.720 527.441 1.00153.51 A C
ANISOU 2927 CD GLU A 385 25442 21857 11029 276 -5070 -1782 A C
ATOM 2928 OE1 GLU A 385 31.911 22.826 527.870 1.00152.38 A O
ANISOU 2928 OE1 GLU A 385 25894 21488 10517 63 -5372 -2076 A O
ATOM 2929 OE2 GLU A 385 32.114 20.647 527.690 1.00151.75 A O1-
ANISOU 2929 OE2 GLU A 385 24746 21975 10937 207 -5189 -1519 A O1-
ATOM 2930 N TRP A 386 28.645 24.704 523.404 1.00141.60 A N
ANISOU 2930 N TRP A 386 24389 19048 10363 652 -3984 -2324 A N
ATOM 2931 CA TRP A 386 28.116 25.976 522.900 1.00141.37 A C
ANISOU 2931 CA TRP A 386 24868 18614 10233 739 -3853 -2593 A C
ATOM 2932 C TRP A 386 26.675 25.844 522.412 1.00139.27 A C
ANISOU 2932 C TRP A 386 24480 18365 10071 1247 -3289 -2462 A C
ATOM 2933 O TRP A 386 25.877 26.783 522.573 1.00140.49 A O
ANISOU 2933 O TRP A 386 25203 18295 9883 1584 -3068 -2638 A O
ATOM 2934 CB TRP A 386 29.004 26.476 521.752 1.00136.44 A C
ANISOU 2934 CB TRP A 386 24045 17762 10034 231 -4118 -2694 A C
ATOM 2935 CG TRP A 386 28.580 27.777 521.105 1.00135.12 A C
ANISOU 2935 CG TRP A 386 24372 17148 9818 257 -4018 -2961 A C
ATOM 2936 CD1 TRP A 386 28.956 29.043 521.459 1.00135.32 A C
ANISOU 2936 CD1 TRP A 386 25165 16797 9455 62 -4308 -3284 A C
ATOM 2937 CD2 TRP A 386 27.727 27.920 519.959 1.00132.90 A C
ANISOU 2937 CD2 TRP A 386 23863 16740 9892 474 -3620 -2915 A C
ATOM 2938 CE2 TRP A 386 27.616 29.299 519.688 1.00131.94 A C
ANISOU 2938 CE2 TRP A 386 24390 16171 9572 436 -3663 -3218 A C
ATOM 2939 CE3 TRP A 386 27.037 27.015 519.144 1.00128.05 A C
ANISOU 2939 CE3 TRP A 386 22593 16336 9724 686 -3248 -2640 A C
ATOM 2940 NE1 TRP A 386 28.374 29.962 520.618 1.00136.51 A N
ANISOU 2940 NE1 TRP A 386 25594 16582 9690 177 -4092 -3443 A N
ATOM 2941 CZ2 TRP A 386 26.843 29.793 518.639 1.00127.30 A C
ANISOU 2941 CZ2 TRP A 386 23773 15371 9223 633 -3324 -3248 A C
ATOM 2942 CZ3 TRP A 386 26.271 27.509 518.103 1.00125.50 A C
ANISOU 2942 CZ3 TRP A 386 22238 15812 9636 850 -2934 -2670 A C
ATOM 2943 CH2 TRP A 386 26.180 28.884 517.860 1.00124.00 A C
ANISOU 2943 CH2 TRP A 386 22661 15206 9248 838 -2962 -2968 A C
ATOM 2944 N LEU A 387 26.303 24.688 521.862 1.00135.58 A N
ANISOU 2944 N LEU A 387 23312 18174 10030 1325 -3055 -2135 A N
ATOM 2945 CA LEU A 387 24.921 24.507 521.433 1.00134.81 A C
ANISOU 2945 CA LEU A 387 23055 18148 10019 1759 -2551 -1955 A C
ATOM 2946 C LEU A 387 24.000 24.472 522.643 1.00140.05 A C
ANISOU 2946 C LEU A 387 24066 19016 10129 2266 -2298 -1869 A C
ATOM 2947 O LEU A 387 23.062 25.272 522.759 1.00140.76 A O
ANISOU 2947 O LEU A 387 24574 19003 9906 2675 -1998 -1951 A O
ATOM 2948 CB LEU A 387 24.768 23.247 520.588 1.00126.03 A C
ANISOU 2948 CB LEU A 387 21166 17257 9463 1669 -2416 -1613 A C
ATOM 2949 CG LEU A 387 25.239 23.501 519.167 1.00122.25 A C
ANISOU 2949 CG LEU A 387 20405 16543 9502 1345 -2498 -1692 A C
ATOM 2950 CD1 LEU A 387 25.399 22.194 518.425 1.00117.84 A C
ANISOU 2950 CD1 LEU A 387 19160 16170 9445 1204 -2476 -1386 A C
ATOM 2951 CD2 LEU A 387 24.253 24.427 518.476 1.00127.06 A C
ANISOU 2951 CD2 LEU A 387 21232 16929 10115 1588 -2173 -1796 A C
ATOM 2952 N GLU A 388 24.277 23.549 523.572 1.00140.84 A N
ANISOU 2952 N GLU A 388 24006 19426 10080 2274 -2409 -1688 A N
ATOM 2953 CA GLU A 388 23.459 23.412 524.771 1.00144.48 A C
ANISOU 2953 CA GLU A 388 24749 20135 10011 2756 -2176 -1565 A C
ATOM 2954 C GLU A 388 23.473 24.675 525.624 1.00144.79 A C
ANISOU 2954 C GLU A 388 25669 19933 9409 2974 -2258 -1915 A C
ATOM 2955 O GLU A 388 22.631 24.814 526.517 1.00150.13 A O
ANISOU 2955 O GLU A 388 26687 20771 9584 3487 -1989 -1842 A O
ATOM 2956 CB GLU A 388 23.929 22.200 525.589 1.00148.93 A C
ANISOU 2956 CB GLU A 388 24992 21046 10548 2661 -2340 -1324 A C
ATOM 2957 CG GLU A 388 24.024 20.888 524.784 1.00144.97 A C
ANISOU 2957 CG GLU A 388 23706 20730 10645 2434 -2308 -986 A C
ATOM 2958 CD GLU A 388 24.169 19.640 525.658 1.00145.36 A C
ANISOU 2958 CD GLU A 388 23482 21140 10607 2471 -2363 -684 A C
ATOM 2959 OE1 GLU A 388 24.933 19.673 526.650 1.00144.52 A O
ANISOU 2959 OE1 GLU A 388 23642 21103 10165 2402 -2649 -801 A O
ATOM 2960 OE2 GLU A 388 23.509 18.622 525.346 1.00143.36 A O1-
ANISOU 2960 OE2 GLU A 388 22761 21095 10614 2554 -2134 -318 A O1-
ATOM 2961 N GLU A 389 24.404 25.597 525.365 1.00144.06 A N
ANISOU 2961 N GLU A 389 25977 19457 9302 2599 -2630 -2274 A N
ATOM 2962 CA GLU A 389 24.410 26.883 526.055 1.00153.50 A C
ANISOU 2962 CA GLU A 389 28113 20325 9884 2770 -2739 -2634 A C
ATOM 2963 C GLU A 389 23.503 27.895 525.367 1.00154.75 A C
ANISOU 2963 C GLU A 389 28623 20191 9984 3106 -2397 -2763 A C
ATOM 2964 O GLU A 389 22.774 28.636 526.039 1.00155.42 A O
ANISOU 2964 O GLU A 389 29247 20166 9640 3575 -2146 -2836 A O
ATOM 2965 CB GLU A 389 25.833 27.436 526.137 1.00156.44 A C
ANISOU 2965 CB GLU A 389 28798 20411 10229 2158 -3342 -2933 A C
ATOM 2966 CG GLU A 389 26.601 27.043 527.381 1.00158.51 A C
ANISOU 2966 CG GLU A 389 29179 20861 10185 1993 -3682 -2926 A C
ATOM 2967 CD GLU A 389 27.978 27.671 527.412 1.00159.18 A C
ANISOU 2967 CD GLU A 389 29402 20692 10387 1324 -4224 -3137 A C
ATOM 2968 OE1 GLU A 389 28.372 28.273 526.387 1.00159.06 A O
ANISOU 2968 OE1 GLU A 389 29346 20391 10697 976 -4356 -3263 A O
ATOM 2969 OE2 GLU A 389 28.665 27.562 528.452 1.00158.15 A O1-
ANISOU 2969 OE2 GLU A 389 29390 20671 10028 1141 -4511 -3149 A O1-
ATOM 2970 N ASN A 390 23.539 27.947 524.030 1.00152.00 A N
ANISOU 2970 N ASN A 390 27837 19706 10209 2852 -2339 -2737 A N
ATOM 2971 CA ASN A 390 22.708 28.905 523.305 1.00148.07 A C
ANISOU 2971 CA ASN A 390 27640 18936 9683 3159 -2018 -2848 A C
ATOM 2972 C ASN A 390 21.214 28.665 523.486 1.00148.98 A C
ANISOU 2972 C ASN A 390 27640 19363 9601 3857 -1433 -2561 A C
ATOM 2973 O ASN A 390 20.417 29.477 523.002 1.00150.44 A O
ANISOU 2973 O ASN A 390 28106 19377 9679 4216 -1119 -2620 A O
ATOM 2974 CB ASN A 390 23.035 28.867 521.812 1.00140.67 A C
ANISOU 2974 CB ASN A 390 26166 17849 9432 2745 -2061 -2830 A C
ATOM 2975 CG ASN A 390 23.933 30.007 521.379 1.00139.30 A C
ANISOU 2975 CG ASN A 390 26497 17173 9259 2323 -2436 -3204 A C
ATOM 2976 ND2 ASN A 390 23.909 30.320 520.084 1.00136.75 A N
ANISOU 2976 ND2 ASN A 390 25900 16658 9402 2141 -2359 -3222 A N
ATOM 2977 OD1 ASN A 390 24.642 30.599 522.195 1.00135.69 A O
ANISOU 2977 OD1 ASN A 390 26662 16501 8393 2136 -2804 -3455 A O
ATOM 2978 N GLY A 391 20.813 27.590 524.164 1.00149.69 A N
ANISOU 2978 N GLY A 391 27321 19924 9630 4058 -1278 -2225 A N
ATOM 2979 CA GLY A 391 19.438 27.142 524.123 1.00149.27 A C
ANISOU 2979 CA GLY A 391 26915 20261 9539 4594 -743 -1836 A C
ATOM 2980 C GLY A 391 19.024 26.523 522.806 1.00142.25 A C
ANISOU 2980 C GLY A 391 25233 19496 9321 4402 -557 -1562 A C
ATOM 2981 O GLY A 391 17.886 26.052 522.686 1.00143.36 A O
ANISOU 2981 O GLY A 391 24984 20001 9486 4761 -146 -1179 A O
ATOM 2982 N LYS A 392 19.912 26.505 521.818 1.00134.01 A N
ANISOU 2982 N LYS A 392 23937 18178 8801 3844 -855 -1722 A N
ATOM 2983 CA LYS A 392 19.640 25.941 520.507 1.00133.00 A C
ANISOU 2983 CA LYS A 392 23116 18110 9307 3629 -727 -1504 A C
ATOM 2984 C LYS A 392 19.793 24.427 520.463 1.00132.13 A C
ANISOU 2984 C LYS A 392 22294 18341 9570 3379 -797 -1148 A C
ATOM 2985 O LYS A 392 19.708 23.851 519.370 1.00127.79 A O
ANISOU 2985 O LYS A 392 21198 17805 9552 3142 -759 -978 A O
ATOM 2986 CB LYS A 392 20.567 26.580 519.469 1.00131.30 A C
ANISOU 2986 CB LYS A 392 22963 17460 9466 3167 -1015 -1819 A C
ATOM 2987 CG LYS A 392 20.397 28.085 519.323 1.00135.38 A C
ANISOU 2987 CG LYS A 392 24189 17577 9674 3367 -953 -2160 A C
ATOM 2988 CD LYS A 392 20.932 28.539 517.977 1.00133.24 A C
ANISOU 2988 CD LYS A 392 23757 16970 9899 2965 -1095 -2324 A C
ATOM 2989 CE LYS A 392 20.584 29.985 517.659 1.00132.16 A C
ANISOU 2989 CE LYS A 392 24276 16432 9506 3194 -970 -2609 A C
ATOM 2990 NZ LYS A 392 21.079 30.370 516.296 1.00118.77 A N1+
ANISOU 2990 NZ LYS A 392 22364 14439 8324 2794 -1093 -2730 A N1+
ATOM 2991 N LYS A 393 20.004 23.771 521.611 1.00138.60 A N
ANISOU 2991 N LYS A 393 23145 19413 10104 3438 -900 -1031 A N
ATOM 2992 CA LYS A 393 20.332 22.346 521.594 1.00139.55 A C
ANISOU 2992 CA LYS A 393 22669 19788 10564 3161 -1028 -729 A C
ATOM 2993 C LYS A 393 19.150 21.506 521.132 1.00143.13 A C
ANISOU 2993 C LYS A 393 22585 20556 11243 3326 -673 -268 A C
ATOM 2994 O LYS A 393 19.318 20.603 520.308 1.00146.32 A O
ANISOU 2994 O LYS A 393 22478 20975 12143 3010 -751 -78 A O
ATOM 2995 CB LYS A 393 20.830 21.884 522.972 1.00136.46 A C
ANISOU 2995 CB LYS A 393 22469 19595 9784 3202 -1221 -709 A C
ATOM 2996 CG LYS A 393 19.838 21.105 523.845 1.00138.88 A C
ANISOU 2996 CG LYS A 393 22607 20350 9812 3581 -927 -301 A C
ATOM 2997 CD LYS A 393 20.556 20.228 524.876 1.00139.62 A C
ANISOU 2997 CD LYS A 393 22654 20641 9753 3454 -1187 -213 A C
ATOM 2998 CE LYS A 393 19.604 19.656 525.930 1.00137.97 A C
ANISOU 2998 CE LYS A 393 22400 20868 9153 3872 -903 158 A C
ATOM 2999 NZ LYS A 393 20.324 18.939 527.029 1.00134.34 A N1+
ANISOU 2999 NZ LYS A 393 21985 20584 8476 3787 -1158 206 A N1+
ATOM 3000 N SER A 394 17.940 21.815 521.612 1.00139.44 A N
ANISOU 3000 N SER A 394 22238 20341 10402 3821 -288 -67 A N
ATOM 3001 CA SER A 394 16.802 20.941 521.346 1.00135.28 A C
ANISOU 3001 CA SER A 394 21170 20199 10032 3945 19 450 A C
ATOM 3002 C SER A 394 16.332 21.031 519.898 1.00138.81 A C
ANISOU 3002 C SER A 394 21264 20527 10951 3793 150 532 A C
ATOM 3003 O SER A 394 15.789 20.057 519.364 1.00139.34 A O
ANISOU 3003 O SER A 394 20799 20803 11343 3633 228 926 A O
ATOM 3004 CB SER A 394 15.661 21.273 522.298 1.00134.22 A C
ANISOU 3004 CB SER A 394 21228 20440 9330 4544 403 691 A C
ATOM 3005 OG SER A 394 16.091 21.120 523.635 1.00140.22 A O
ANISOU 3005 OG SER A 394 22310 21318 9649 4685 277 630 A O
ATOM 3006 N LEU A 395 16.515 22.179 519.254 1.00136.37 A N
ANISOU 3006 N LEU A 395 21266 19877 10672 3829 162 179 A N
ATOM 3007 CA LEU A 395 16.156 22.308 517.853 1.00134.47 A C
ANISOU 3007 CA LEU A 395 20710 19502 10882 3676 265 227 A C
ATOM 3008 C LEU A 395 17.239 21.676 516.990 1.00124.88 A C
ANISOU 3008 C LEU A 395 19215 18020 10213 3116 -94 102 A C
ATOM 3009 O LEU A 395 18.344 21.391 517.461 1.00118.04 A O
ANISOU 3009 O LEU A 395 18466 17040 9346 2875 -422 -81 A O
ATOM 3010 CB LEU A 395 15.968 23.780 517.476 1.00142.60 A C
ANISOU 3010 CB LEU A 395 22198 20252 11731 3936 416 -98 A C
ATOM 3011 CG LEU A 395 14.645 24.411 517.920 1.00148.50 A C
ANISOU 3011 CG LEU A 395 23125 21285 12012 4567 872 108 A C
ATOM 3012 CD1 LEU A 395 14.629 25.913 517.647 1.00149.57 A C
ANISOU 3012 CD1 LEU A 395 23856 21063 11912 4844 978 -273 A C
ATOM 3013 CD2 LEU A 395 13.467 23.716 517.248 1.00144.93 A C
ANISOU 3013 CD2 LEU A 395 22027 21229 11812 4622 1168 632 A C
ATOM 3014 N PHE A 396 16.931 21.478 515.708 1.00123.91 A N
ANISOU 3014 N PHE A 396 18727 17814 10540 2933 -29 213 A N
ATOM 3015 CA PHE A 396 18.018 21.088 514.836 1.00121.18 A C
ANISOU 3015 CA PHE A 396 18205 17177 10661 2478 -349 43 A C
ATOM 3016 C PHE A 396 18.811 22.358 514.599 1.00122.39 A C
ANISOU 3016 C PHE A 396 18779 16961 10763 2430 -485 -426 A C
ATOM 3017 O PHE A 396 18.250 23.457 514.607 1.00133.44 A O
ANISOU 3017 O PHE A 396 20508 18277 11915 2722 -272 -567 A O
ATOM 3018 CB PHE A 396 17.404 20.545 513.550 1.00123.97 A C
ANISOU 3018 CB PHE A 396 18104 17538 11460 2326 -236 296 A C
ATOM 3019 CG PHE A 396 16.039 21.149 513.265 1.00135.86 A C
ANISOU 3019 CG PHE A 396 19567 19222 12832 2657 153 483 A C
ATOM 3020 CD1 PHE A 396 15.909 22.351 512.574 1.00139.38 A C
ANISOU 3020 CD1 PHE A 396 20225 19438 13297 2788 283 226 A C
ATOM 3021 CD2 PHE A 396 14.885 20.542 513.765 1.00138.75 A C
ANISOU 3021 CD2 PHE A 396 19686 20021 13011 2862 394 946 A C
ATOM 3022 CE1 PHE A 396 14.644 22.913 512.348 1.00140.57 A C
ANISOU 3022 CE1 PHE A 396 20332 19790 13287 3148 660 425 A C
ATOM 3023 CE2 PHE A 396 13.630 21.098 513.551 1.00142.30 A C
ANISOU 3023 CE2 PHE A 396 20054 20713 13303 3199 763 1172 A C
ATOM 3024 CZ PHE A 396 13.507 22.281 512.839 1.00143.99 A C
ANISOU 3024 CZ PHE A 396 20476 20699 13536 3362 904 909 A C
ATOM 3025 N TRP A 397 20.098 22.230 514.300 1.00115.53 A N
ANISOU 3025 N TRP A 397 17895 15867 10135 2062 -836 -643 A N
ATOM 3026 CA TRP A 397 20.819 23.444 513.959 1.00117.01 A C
ANISOU 3026 CA TRP A 397 18445 15708 10306 1949 -983 -1041 A C
ATOM 3027 C TRP A 397 21.818 23.248 512.825 1.00109.41 A C
ANISOU 3027 C TRP A 397 17202 14532 9836 1543 -1230 -1136 A C
ATOM 3028 O TRP A 397 22.519 22.233 512.794 1.00106.73 A O
ANISOU 3028 O TRP A 397 16557 14289 9709 1318 -1439 -1008 A O
ATOM 3029 CB TRP A 397 21.441 24.013 515.241 1.00123.96 A C
ANISOU 3029 CB TRP A 397 19842 16548 10708 1996 -1183 -1281 A C
ATOM 3030 CG TRP A 397 21.983 25.374 515.096 1.00122.67 A C
ANISOU 3030 CG TRP A 397 20182 16023 10406 1911 -1324 -1669 A C
ATOM 3031 CD1 TRP A 397 21.295 26.531 515.312 1.00124.16 A C
ANISOU 3031 CD1 TRP A 397 20893 16051 10230 2246 -1111 -1840 A C
ATOM 3032 CD2 TRP A 397 23.317 25.753 514.778 1.00122.46 A C
ANISOU 3032 CD2 TRP A 397 20232 15752 10546 1474 -1717 -1913 A C
ATOM 3033 CE2 TRP A 397 23.360 27.161 514.785 1.00127.73 A C
ANISOU 3033 CE2 TRP A 397 21493 16082 10956 1512 -1747 -2233 A C
ATOM 3034 CE3 TRP A 397 24.477 25.043 514.468 1.00120.73 A C
ANISOU 3034 CE3 TRP A 397 19636 15583 10654 1067 -2043 -1864 A C
ATOM 3035 NE1 TRP A 397 22.107 27.611 515.109 1.00128.84 A N
ANISOU 3035 NE1 TRP A 397 21925 16260 10767 2014 -1364 -2196 A N
ATOM 3036 CZ2 TRP A 397 24.516 27.870 514.497 1.00130.46 A C
ANISOU 3036 CZ2 TRP A 397 22047 16142 11379 1092 -2118 -2489 A C
ATOM 3037 CZ3 TRP A 397 25.622 25.748 514.182 1.00122.21 A C
ANISOU 3037 CZ3 TRP A 397 19978 15543 10914 692 -2384 -2098 A C
ATOM 3038 CH2 TRP A 397 25.636 27.148 514.199 1.00126.47 A C
ANISOU 3038 CH2 TRP A 397 21093 15749 11210 673 -2433 -2401 A C
ATOM 3039 N HIS A 398 21.894 24.202 511.899 1.00106.80 A N
ANISOU 3039 N HIS A 398 16984 13924 9670 1477 -1199 -1343 A N
ATOM 3040 CA HIS A 398 22.736 24.018 510.724 1.00103.80 A C
ANISOU 3040 CA HIS A 398 16300 13377 9761 1138 -1384 -1390 A C
ATOM 3041 C HIS A 398 23.212 25.388 510.252 1.00108.32 A C
ANISOU 3041 C HIS A 398 17211 13620 10326 1019 -1473 -1717 A C
ATOM 3042 O HIS A 398 22.513 26.393 510.404 1.00112.60 A O
ANISOU 3042 O HIS A 398 18147 14030 10607 1261 -1276 -1855 A O
ATOM 3043 CB HIS A 398 22.032 23.222 509.616 1.00100.78 A C
ANISOU 3043 CB HIS A 398 15456 13062 9773 1158 -1185 -1125 A C
ATOM 3044 CG HIS A 398 20.897 23.940 508.956 1.00105.07 A C
ANISOU 3044 CG HIS A 398 16053 13538 10332 1386 -857 -1114 A C
ATOM 3045 CD2 HIS A 398 20.796 24.523 507.739 1.00 99.84 A C
ANISOU 3045 CD2 HIS A 398 15318 12665 9950 1328 -774 -1205 A C
ATOM 3046 ND1 HIS A 398 19.654 24.057 509.540 1.00111.58 A N
ANISOU 3046 ND1 HIS A 398 16975 14569 10851 1742 -551 -949 A N
ATOM 3047 CE1 HIS A 398 18.845 24.709 508.725 1.00106.34 A C
ANISOU 3047 CE1 HIS A 398 16301 13832 10271 1901 -295 -941 A C
ATOM 3048 NE2 HIS A 398 19.512 24.999 507.623 1.00100.81 A N
ANISOU 3048 NE2 HIS A 398 15509 12864 9931 1648 -428 -1106 A N
ATOM 3049 N SER A 399 24.423 25.406 509.688 1.00108.85 A N
ANISOU 3049 N SER A 399 17129 13568 10662 654 -1772 -1813 A N
ATOM 3050 CA SER A 399 25.084 26.601 509.175 1.00108.20 A C
ANISOU 3050 CA SER A 399 17306 13183 10624 432 -1930 -2080 A C
ATOM 3051 C SER A 399 26.105 26.213 508.106 1.00105.72 A C
ANISOU 3051 C SER A 399 16551 12852 10766 101 -2131 -2017 A C
ATOM 3052 O SER A 399 26.754 25.170 508.216 1.00 98.28 A O
ANISOU 3052 O SER A 399 15259 12122 9959 -12 -2290 -1843 A O
ATOM 3053 CB SER A 399 25.765 27.384 510.304 1.00106.72 A C
ANISOU 3053 CB SER A 399 17643 12896 10008 300 -2212 -2312 A C
ATOM 3054 OG SER A 399 26.695 28.319 509.789 1.00106.29 A O
ANISOU 3054 OG SER A 399 17752 12582 10050 -57 -2477 -2509 A O
ATOM 3055 N HIS A 400 26.219 27.040 507.062 1.00110.41 A N
ANISOU 3055 N HIS A 400 17169 13203 11579 -14 -2103 -2139 A N
ATOM 3056 CA HIS A 400 27.276 26.927 506.057 1.00111.08 A C
ANISOU 3056 CA HIS A 400 16898 13263 12045 -325 -2304 -2098 A C
ATOM 3057 C HIS A 400 28.310 28.048 506.200 1.00115.10 A C
ANISOU 3057 C HIS A 400 17698 13593 12440 -682 -2626 -2301 A C
ATOM 3058 O HIS A 400 29.027 28.360 505.243 1.00115.51 A O
ANISOU 3058 O HIS A 400 17537 13570 12781 -929 -2745 -2291 A O
ATOM 3059 CB HIS A 400 26.725 26.885 504.630 1.00108.72 A C
ANISOU 3059 CB HIS A 400 16323 12857 12128 -228 -2054 -2028 A C
ATOM 3060 CG HIS A 400 25.904 28.075 504.244 1.00108.46 A C
ANISOU 3060 CG HIS A 400 16640 12554 12017 -92 -1834 -2207 A C
ATOM 3061 CD2 HIS A 400 26.229 29.167 503.513 1.00104.46 A C
ANISOU 3061 CD2 HIS A 400 16299 11780 11613 -255 -1881 -2373 A C
ATOM 3062 ND1 HIS A 400 24.572 28.214 504.566 1.00107.86 A N
ANISOU 3062 ND1 HIS A 400 16768 12483 11733 271 -1511 -2195 A N
ATOM 3063 CE1 HIS A 400 24.119 29.351 504.069 1.00105.97 A C
ANISOU 3063 CE1 HIS A 400 16825 11985 11455 359 -1360 -2357 A C
ATOM 3064 NE2 HIS A 400 25.105 29.948 503.425 1.00104.13 A N
ANISOU 3064 NE2 HIS A 400 16594 11559 11412 32 -1586 -2479 A N
ATOM 3065 N MET A 401 28.390 28.656 507.382 1.00115.33 A N
ANISOU 3065 N MET A 401 18230 13554 12036 -722 -2781 -2468 A N
ATOM 3066 CA MET A 401 29.386 29.667 507.719 1.00123.46 A C
ANISOU 3066 CA MET A 401 19613 14413 12885 -1121 -3159 -2645 A C
ATOM 3067 C MET A 401 29.559 29.737 509.233 1.00122.19 A C
ANISOU 3067 C MET A 401 19878 14313 12234 -1137 -3368 -2740 A C
ATOM 3068 O MET A 401 29.061 30.648 509.906 1.00123.06 A O
ANISOU 3068 O MET A 401 20647 14170 11941 -1021 -3344 -2966 A O
ATOM 3069 CB MET A 401 28.957 31.030 507.156 1.00130.63 A C
ANISOU 3069 CB MET A 401 20981 14908 13745 -1128 -3060 -2873 A C
ATOM 3070 CG MET A 401 29.782 32.243 507.624 1.00147.01 A C
ANISOU 3070 CG MET A 401 23614 16707 15536 -1540 -3454 -3088 A C
ATOM 3071 SD MET A 401 31.585 32.288 507.523 1.00162.51 A S
ANISOU 3071 SD MET A 401 25270 18826 17649 -2230 -4023 -2969 A S
ATOM 3072 CE MET A 401 31.793 33.046 505.919 1.00150.55 A C
ANISOU 3072 CE MET A 401 23565 17079 16557 -2437 -3963 -2959 A C
ATOM 3073 N LEU A 402 30.236 28.712 509.768 1.00115.14 A N
ANISOU 3073 N LEU A 402 18622 13767 11360 -1234 -3555 -2553 A N
ATOM 3074 CA LEU A 402 30.507 28.622 511.199 1.00123.47 A C
ANISOU 3074 CA LEU A 402 20001 14939 11972 -1267 -3780 -2605 A C
ATOM 3075 C LEU A 402 31.215 29.847 511.757 1.00129.23 A C
ANISOU 3075 C LEU A 402 21314 15422 12366 -1650 -4170 -2838 A C
ATOM 3076 O LEU A 402 30.886 30.298 512.857 1.00133.13 A O
ANISOU 3076 O LEU A 402 22410 15796 12377 -1538 -4228 -3014 A O
ATOM 3077 CB LEU A 402 31.316 27.362 511.493 1.00126.70 A C
ANISOU 3077 CB LEU A 402 19864 15764 12511 -1365 -3955 -2340 A C
ATOM 3078 CG LEU A 402 30.419 26.127 511.517 1.00117.37 A C
ANISOU 3078 CG LEU A 402 18365 14789 11443 -939 -3603 -2143 A C
ATOM 3079 CD1 LEU A 402 31.233 24.860 511.355 1.00109.06 A C
ANISOU 3079 CD1 LEU A 402 16721 14079 10637 -1012 -3730 -1858 A C
ATOM 3080 CD2 LEU A 402 29.631 26.108 512.818 1.00120.11 A C
ANISOU 3080 CD2 LEU A 402 19144 15166 11324 -651 -3494 -2219 A C
ATOM 3081 N LYS A 403 32.208 30.387 511.041 1.00132.83 A N
ANISOU 3081 N LYS A 403 21623 15804 13043 -2116 -4463 -2824 A N
ATOM 3082 CA LYS A 403 32.977 31.471 511.649 1.00138.46 A C
ANISOU 3082 CA LYS A 403 22890 16302 13415 -2573 -4914 -3003 A C
ATOM 3083 C LYS A 403 32.138 32.733 511.851 1.00140.01 A C
ANISOU 3083 C LYS A 403 23949 15986 13265 -2419 -4798 -3333 A C
ATOM 3084 O LYS A 403 32.401 33.490 512.793 1.00144.74 A O
ANISOU 3084 O LYS A 403 25182 16383 13429 -2596 -5069 -3506 A O
ATOM 3085 CB LYS A 403 34.259 31.763 510.863 1.00143.16 A C
ANISOU 3085 CB LYS A 403 23100 16982 14313 -3150 -5278 -2855 A C
ATOM 3086 CG LYS A 403 35.265 30.609 510.923 1.00146.68 A C
ANISOU 3086 CG LYS A 403 22798 17968 14965 -3304 -5469 -2520 A C
ATOM 3087 CD LYS A 403 36.596 30.947 510.262 1.00149.69 A C
ANISOU 3087 CD LYS A 403 22788 18510 15577 -3874 -5852 -2321 A C
ATOM 3088 CE LYS A 403 37.540 29.747 510.259 1.00145.84 A C
ANISOU 3088 CE LYS A 403 21526 18603 15284 -3915 -5977 -1949 A C
ATOM 3089 NZ LYS A 403 38.927 30.134 509.858 1.00148.31 A N1+
ANISOU 3089 NZ LYS A 403 21473 19161 15718 -4498 -6409 -1707 A N1+
ATOM 3090 N GLU A 404 31.140 32.990 510.996 1.00138.39 A N
ANISOU 3090 N GLU A 404 23761 15573 13247 -2060 -4370 -3391 A N
ATOM 3091 CA GLU A 404 30.238 34.119 511.233 1.00136.72 A C
ANISOU 3091 CA GLU A 404 24379 14905 12663 -1791 -4196 -3679 A C
ATOM 3092 C GLU A 404 28.958 33.759 511.988 1.00135.20 A C
ANISOU 3092 C GLU A 404 24436 14784 12151 -1134 -3783 -3713 A C
ATOM 3093 O GLU A 404 28.444 34.596 512.740 1.00142.26 A O
ANISOU 3093 O GLU A 404 26127 15383 12542 -905 -3747 -3940 A O
ATOM 3094 CB GLU A 404 29.864 34.807 509.918 1.00134.69 A C
ANISOU 3094 CB GLU A 404 24093 14362 12722 -1764 -3975 -3727 A C
ATOM 3095 CG GLU A 404 30.959 35.715 509.380 1.00144.14 A C
ANISOU 3095 CG GLU A 404 25286 15369 14112 -2353 -4316 -3712 A C
ATOM 3096 CD GLU A 404 30.575 36.420 508.089 1.00147.86 A C
ANISOU 3096 CD GLU A 404 25715 15569 14896 -2301 -4072 -3738 A C
ATOM 3097 OE1 GLU A 404 29.410 36.282 507.648 1.00145.06 A O
ANISOU 3097 OE1 GLU A 404 25433 15126 14557 -1806 -3658 -3811 A O
ATOM 3098 OE2 GLU A 404 31.435 37.141 507.536 1.00150.29 A O1-
ANISOU 3098 OE2 GLU A 404 25919 15769 15415 -2748 -4290 -3665 A O1-
ATOM 3099 N ASP A 405 28.439 32.532 511.867 1.00130.77 A N
ANISOU 3099 N ASP A 405 23238 14616 11834 -818 -3479 -3469 A N
ATOM 3100 CA ASP A 405 27.248 32.180 512.642 1.00130.11 A C
ANISOU 3100 CA ASP A 405 23354 14655 11426 -231 -3109 -3446 A C
ATOM 3101 C ASP A 405 27.628 31.868 514.085 1.00133.47 A C
ANISOU 3101 C ASP A 405 24063 15242 11409 -255 -3358 -3474 A C
ATOM 3102 O ASP A 405 27.078 32.456 515.022 1.00137.10 A O
ANISOU 3102 O ASP A 405 25219 15542 11329 50 -3290 -3646 A O
ATOM 3103 CB ASP A 405 26.490 31.010 511.999 1.00121.36 A C
ANISOU 3103 CB ASP A 405 21510 13887 10715 73 -2717 -3152 A C
ATOM 3104 CG ASP A 405 25.523 31.462 510.911 1.00118.50 A C
ANISOU 3104 CG ASP A 405 21100 13356 10568 349 -2325 -3151 A C
ATOM 3105 OD1 ASP A 405 25.034 32.607 510.996 1.00112.02 A O
ANISOU 3105 OD1 ASP A 405 20914 12206 9441 542 -2218 -3367 A O
ATOM 3106 OD2 ASP A 405 25.234 30.674 509.984 1.00125.16 A O1-
ANISOU 3106 OD2 ASP A 405 21308 14389 11859 392 -2127 -2932 A O1-
ATOM 3107 N ALA A 406 28.534 30.911 514.286 1.00131.20 A N
ANISOU 3107 N ALA A 406 23245 15286 11318 -563 -3624 -3289 A N
ATOM 3108 CA ALA A 406 29.126 30.621 515.590 1.00135.13 A C
ANISOU 3108 CA ALA A 406 23958 15955 11432 -686 -3940 -3303 A C
ATOM 3109 C ALA A 406 30.499 31.291 515.683 1.00138.39 A C
ANISOU 3109 C ALA A 406 24573 16223 11785 -1329 -4510 -3419 A C
ATOM 3110 O ALA A 406 31.529 30.636 515.451 1.00137.28 A O
ANISOU 3110 O ALA A 406 23850 16372 11938 -1708 -4784 -3220 A O
ATOM 3111 CB ALA A 406 29.245 29.108 515.791 1.00131.72 A C
ANISOU 3111 CB ALA A 406 22815 16006 11228 -598 -3871 -2992 A C
ATOM 3112 N PRO A 407 30.584 32.578 516.030 1.00142.79 A N
ANISOU 3112 N PRO A 407 25938 16354 11960 -1477 -4713 -3703 A N
ATOM 3113 CA PRO A 407 31.892 33.247 516.001 1.00147.71 A C
ANISOU 3113 CA PRO A 407 26502 16894 12727 -2116 -5143 -3671 A C
ATOM 3114 C PRO A 407 32.859 32.680 517.035 1.00150.53 A C
ANISOU 3114 C PRO A 407 26690 17587 12918 -2410 -5525 -3547 A C
ATOM 3115 O PRO A 407 32.476 32.352 518.161 1.00153.50 A O
ANISOU 3115 O PRO A 407 27351 18069 12904 -2117 -5475 -3590 A O
ATOM 3116 CB PRO A 407 31.543 34.713 516.290 1.00154.58 A C
ANISOU 3116 CB PRO A 407 28110 17266 13356 -2044 -5060 -3874 A C
ATOM 3117 CG PRO A 407 30.312 34.632 517.116 1.00154.50 A C
ANISOU 3117 CG PRO A 407 28571 17210 12921 -1384 -4695 -3987 A C
ATOM 3118 CD PRO A 407 29.527 33.494 516.503 1.00146.75 A C
ANISOU 3118 CD PRO A 407 27128 16521 12108 -1004 -4375 -3886 A C
ATOM 3119 N GLY A 408 34.129 32.587 516.642 1.00148.19 A N
ANISOU 3119 N GLY A 408 25903 17487 12916 -2974 -5892 -3365 A N
ATOM 3120 CA GLY A 408 35.200 32.181 517.535 1.00147.03 A C
ANISOU 3120 CA GLY A 408 25544 17676 12646 -3311 -6278 -3210 A C
ATOM 3121 C GLY A 408 35.203 30.730 517.976 1.00147.84 A C
ANISOU 3121 C GLY A 408 25202 18265 12704 -3105 -6282 -3032 A C
ATOM 3122 O GLY A 408 35.014 30.440 519.160 1.00135.51 A O
ANISOU 3122 O GLY A 408 23914 16811 10761 -2909 -6306 -3073 A O
ATOM 3123 N LEU A 409 35.429 29.801 517.040 1.00151.02 A N
ANISOU 3123 N LEU A 409 24927 18966 13486 -3133 -6265 -2812 A N
ATOM 3124 CA LEU A 409 35.548 28.394 517.410 1.00147.64 A C
ANISOU 3124 CA LEU A 409 23916 19019 13160 -2891 -6163 -2543 A C
ATOM 3125 C LEU A 409 36.686 27.694 516.668 1.00145.85 A C
ANISOU 3125 C LEU A 409 22855 19199 13362 -3186 -6347 -2200 A C
ATOM 3126 O LEU A 409 36.651 26.467 516.517 1.00142.72 A O
ANISOU 3126 O LEU A 409 21890 19139 13199 -2893 -6134 -1952 A O
ATOM 3127 CB LEU A 409 34.216 27.660 517.178 1.00135.17 A C
ANISOU 3127 CB LEU A 409 22205 17429 11724 -2245 -5575 -2520 A C
ATOM 3128 CG LEU A 409 33.171 27.906 518.274 1.00128.80 A C
ANISOU 3128 CG LEU A 409 22067 16458 10414 -1838 -5380 -2727 A C
ATOM 3129 CD1 LEU A 409 31.781 27.539 517.796 1.00124.39 A C
ANISOU 3129 CD1 LEU A 409 21418 15828 10016 -1277 -4802 -2701 A C
ATOM 3130 CD2 LEU A 409 33.524 27.139 519.538 1.00125.79 A C
ANISOU 3130 CD2 LEU A 409 21662 16419 9713 -1791 -5561 -2614 A C
ATOM 3131 N LEU A 410 37.691 28.443 516.216 1.00144.99 A N
ANISOU 3131 N LEU A 410 22681 19072 13337 -3746 -6737 -2159 A N
ATOM 3132 CA LEU A 410 38.881 27.892 515.566 1.00134.13 A C
ANISOU 3132 CA LEU A 410 20519 18137 12306 -4039 -6946 -1793 A C
ATOM 3133 C LEU A 410 39.511 26.758 516.369 1.00128.43 A C
ANISOU 3133 C LEU A 410 19379 17942 11475 -3962 -7088 -1520 A C
ATOM 3134 O LEU A 410 40.707 26.781 516.655 1.00131.04 A O
ANISOU 3134 O LEU A 410 19373 18601 11814 -4304 -7389 -1293 A O
ATOM 3135 CB LEU A 410 39.917 28.999 515.350 1.00142.83 A C
ANISOU 3135 CB LEU A 410 21595 19166 13507 -4575 -7209 -1740 A C
ATOM 3136 CG LEU A 410 39.482 30.220 514.537 1.00142.28 A C
ANISOU 3136 CG LEU A 410 21908 18582 13571 -4695 -7084 -1960 A C
ATOM 3137 CD1 LEU A 410 40.286 31.448 514.958 1.00146.80 A C
ANISOU 3137 CD1 LEU A 410 22793 18969 14014 -5180 -7373 -1983 A C
ATOM 3138 CD2 LEU A 410 39.634 29.959 513.047 1.00128.76 A C
ANISOU 3138 CD2 LEU A 410 19618 16974 12333 -4713 -6957 -1776 A C
ATOM 3139 N ARG A 415 39.121 26.184 510.383 1.00117.36 A N
ANISOU 3139 N ARG A 415 16174 16361 12056 -3430 -5940 -1048 A N
ATOM 3140 CA ARG A 415 39.290 25.541 509.089 1.00117.48 A C
ANISOU 3140 CA ARG A 415 15609 16523 12505 -3204 -5694 -814 A C
ATOM 3141 C ARG A 415 37.951 25.065 508.478 1.00124.97 A C
ANISOU 3141 C ARG A 415 16664 17164 13654 -2695 -5190 -958 A C
ATOM 3142 O ARG A 415 37.717 25.242 507.275 1.00126.08 A O
ANISOU 3142 O ARG A 415 16640 17151 14114 -2613 -4980 -951 A O
ATOM 3143 CB ARG A 415 40.261 24.366 509.178 1.00119.47 A C
ANISOU 3143 CB ARG A 415 15252 17327 12814 -3084 -5793 -420 A C
ATOM 3144 CG ARG A 415 40.235 23.561 507.901 1.00116.79 A C
ANISOU 3144 CG ARG A 415 14436 17075 12865 -2712 -5475 -212 A C
ATOM 3145 CD ARG A 415 40.563 22.106 508.117 1.00117.43 A C
ANISOU 3145 CD ARG A 415 14147 17524 12947 -2320 -5387 75 A C
ATOM 3146 NE ARG A 415 40.427 21.378 506.861 1.00116.77 A N
ANISOU 3146 NE ARG A 415 13738 17430 13200 -1935 -5074 231 A N
ATOM 3147 CZ ARG A 415 40.445 20.055 506.753 1.00119.18 A C
ANISOU 3147 CZ ARG A 415 13825 17904 13552 -1491 -4901 441 A C
ATOM 3148 NH1 ARG A 415 40.597 19.301 507.837 1.00117.83 A N1+
ANISOU 3148 NH1 ARG A 415 13689 17950 13132 -1373 -4999 534 A N1+
ATOM 3149 NH2 ARG A 415 40.302 19.491 505.557 1.00118.83 A N
ANISOU 3149 NH2 ARG A 415 13574 17788 13786 -1157 -4637 555 A N
ATOM 3150 N PHE A 416 37.104 24.453 509.302 1.00125.66 A N
ANISOU 3150 N PHE A 416 17003 17196 13547 -2375 -5013 -1056 A N
ATOM 3151 CA PHE A 416 35.847 23.873 508.847 1.00110.47 A C
ANISOU 3151 CA PHE A 416 15136 15057 11779 -1926 -4573 -1122 A C
ATOM 3152 C PHE A 416 34.795 24.972 508.754 1.00109.62 A C
ANISOU 3152 C PHE A 416 15549 14512 11591 -1923 -4402 -1444 A C
ATOM 3153 O PHE A 416 34.834 25.954 509.497 1.00116.51 A O
ANISOU 3153 O PHE A 416 16886 15227 12154 -2157 -4601 -1653 A O
ATOM 3154 CB PHE A 416 35.351 22.773 509.804 1.00101.68 A C
ANISOU 3154 CB PHE A 416 14068 14093 10474 -1607 -4463 -1048 A C
ATOM 3155 CG PHE A 416 36.263 21.563 509.916 1.00103.76 A C
ANISOU 3155 CG PHE A 416 13865 14765 10795 -1513 -4581 -722 A C
ATOM 3156 CD1 PHE A 416 37.420 21.595 510.685 1.00114.56 A C
ANISOU 3156 CD1 PHE A 416 15105 16470 11954 -1775 -4955 -592 A C
ATOM 3157 CD2 PHE A 416 35.913 20.364 509.302 1.00 95.34 A C
ANISOU 3157 CD2 PHE A 416 12531 13738 9955 -1145 -4321 -536 A C
ATOM 3158 CE1 PHE A 416 38.246 20.463 510.809 1.00111.57 A C
ANISOU 3158 CE1 PHE A 416 14295 16496 11600 -1628 -5039 -266 A C
ATOM 3159 CE2 PHE A 416 36.729 19.235 509.422 1.00 94.15 A C
ANISOU 3159 CE2 PHE A 416 12022 13932 9818 -997 -4412 -235 A C
ATOM 3160 CZ PHE A 416 37.896 19.287 510.174 1.00103.78 A C
ANISOU 3160 CZ PHE A 416 13080 15519 10833 -1214 -4755 -95 A C
ATOM 3161 N ALA A 417 33.851 24.806 507.831 1.00 99.21 A N
ANISOU 3161 N ALA A 417 14178 12990 10526 -1642 -4037 -1475 A N
ATOM 3162 CA ALA A 417 32.870 25.852 507.593 1.00 99.34 A C
ANISOU 3162 CA ALA A 417 14632 12623 10488 -1595 -3844 -1740 A C
ATOM 3163 C ALA A 417 31.413 25.428 507.724 1.00108.86 A C
ANISOU 3163 C ALA A 417 16003 13715 11646 -1171 -3453 -1786 A C
ATOM 3164 O ALA A 417 30.574 26.294 508.004 1.00118.18 A O
ANISOU 3164 O ALA A 417 17641 14643 12618 -1076 -3314 -2001 A O
ATOM 3165 CB ALA A 417 33.078 26.451 506.198 1.00 92.64 A C
ANISOU 3165 CB ALA A 417 13599 11610 9988 -1726 -3785 -1746 A C
ATOM 3166 N GLY A 418 31.082 24.152 507.582 1.00102.27 A N
ANISOU 3166 N GLY A 418 14840 13060 10957 -915 -3284 -1574 A N
ATOM 3167 CA GLY A 418 29.698 23.695 507.646 1.00 91.83 A C
ANISOU 3167 CA GLY A 418 13612 11672 9606 -568 -2936 -1551 A C
ATOM 3168 C GLY A 418 29.417 22.775 508.814 1.00 88.98 A C
ANISOU 3168 C GLY A 418 13288 11531 8988 -398 -2933 -1427 A C
ATOM 3169 O GLY A 418 30.244 21.936 509.159 1.00 89.51 A O
ANISOU 3169 O GLY A 418 13119 11829 9061 -459 -3126 -1264 A O
ATOM 3170 N LEU A 419 28.256 22.966 509.438 1.00 91.13 A N
ANISOU 3170 N LEU A 419 13859 11752 9015 -164 -2706 -1486 A N
ATOM 3171 CA LEU A 419 27.841 22.143 510.565 1.00 97.93 A C
ANISOU 3171 CA LEU A 419 14770 12828 9612 21 -2666 -1351 A C
ATOM 3172 C LEU A 419 26.335 21.915 510.550 1.00101.56 A C
ANISOU 3172 C LEU A 419 15282 13282 10025 332 -2297 -1251 A C
ATOM 3173 O LEU A 419 25.560 22.864 510.407 1.00106.66 A O
ANISOU 3173 O LEU A 419 16191 13772 10564 457 -2102 -1396 A O
ATOM 3174 CB LEU A 419 28.246 22.772 511.902 1.00105.09 A C
ANISOU 3174 CB LEU A 419 16079 13781 10069 -49 -2877 -1517 A C
ATOM 3175 CG LEU A 419 27.662 22.058 513.126 1.00109.39 A C
ANISOU 3175 CG LEU A 419 16728 14544 10289 191 -2790 -1389 A C
ATOM 3176 CD1 LEU A 419 28.117 20.599 513.183 1.00105.04 A C
ANISOU 3176 CD1 LEU A 419 15764 14241 9906 186 -2873 -1103 A C
ATOM 3177 CD2 LEU A 419 27.998 22.790 514.410 1.00119.14 A C
ANISOU 3177 CD2 LEU A 419 18435 15790 11044 148 -2990 -1584 A C
ATOM 3178 N LEU A 420 25.937 20.648 510.664 1.00100.54 A N
ANISOU 3178 N LEU A 420 14896 13332 9971 450 -2209 -977 A N
ATOM 3179 CA LEU A 420 24.562 20.219 510.912 1.00102.16 A C
ANISOU 3179 CA LEU A 420 15102 13637 10075 704 -1911 -789 A C
ATOM 3180 C LEU A 420 24.536 19.338 512.154 1.00110.24 A C
ANISOU 3180 C LEU A 420 16143 14917 10826 795 -1970 -609 A C
ATOM 3181 O LEU A 420 25.185 18.288 512.181 1.00109.90 A O
ANISOU 3181 O LEU A 420 15880 14968 10910 700 -2136 -448 A O
ATOM 3182 CB LEU A 420 23.954 19.464 509.735 1.00 93.84 A C
ANISOU 3182 CB LEU A 420 13724 12536 9394 711 -1753 -572 A C
ATOM 3183 CG LEU A 420 22.582 18.839 510.054 1.00 92.47 A C
ANISOU 3183 CG LEU A 420 13487 12535 9115 903 -1497 -289 A C
ATOM 3184 CD1 LEU A 420 21.616 19.779 510.786 1.00 94.04 A C
ANISOU 3184 CD1 LEU A 420 13956 12825 8952 1153 -1259 -351 A C
ATOM 3185 CD2 LEU A 420 21.940 18.313 508.795 1.00 95.98 A C
ANISOU 3185 CD2 LEU A 420 13668 12890 9911 856 -1371 -104 A C
ATOM 3186 N ALA A 421 23.807 19.766 513.184 1.00112.92 A N
ANISOU 3186 N ALA A 421 16762 15372 10772 1009 -1828 -629 A N
ATOM 3187 CA ALA A 421 23.829 19.113 514.487 1.00110.71 A C
ANISOU 3187 CA ALA A 421 16554 15341 10171 1109 -1890 -491 A C
ATOM 3188 C ALA A 421 22.407 18.669 514.805 1.00110.84 A C
ANISOU 3188 C ALA A 421 16507 15553 10053 1372 -1570 -205 A C
ATOM 3189 O ALA A 421 21.503 19.503 514.920 1.00109.15 A O
ANISOU 3189 O ALA A 421 16490 15348 9635 1602 -1321 -255 A O
ATOM 3190 CB ALA A 421 24.360 20.058 515.565 1.00109.47 A C
ANISOU 3190 CB ALA A 421 16830 15174 9590 1132 -2046 -764 A C
ATOM 3191 N ILE A 422 22.228 17.358 514.956 1.00112.54 A N
ANISOU 3191 N ILE A 422 16457 15938 10364 1342 -1583 120 A N
ATOM 3192 CA ILE A 422 20.942 16.742 515.270 1.00111.12 A C
ANISOU 3192 CA ILE A 422 16148 15994 10078 1515 -1327 479 A C
ATOM 3193 C ILE A 422 20.950 16.364 516.752 1.00110.01 A C
ANISOU 3193 C ILE A 422 16150 16122 9527 1666 -1358 592 A C
ATOM 3194 O ILE A 422 21.718 15.471 517.141 1.00106.87 A O
ANISOU 3194 O ILE A 422 15675 15771 9161 1537 -1582 674 A O
ATOM 3195 CB ILE A 422 20.693 15.494 514.415 1.00106.30 A C
ANISOU 3195 CB ILE A 422 15193 15357 9838 1334 -1350 794 A C
ATOM 3196 CG1 ILE A 422 21.085 15.751 512.970 1.00100.61 A C
ANISOU 3196 CG1 ILE A 422 14359 14340 9529 1158 -1409 635 A C
ATOM 3197 CG2 ILE A 422 19.235 15.066 514.501 1.00108.53 A C
ANISOU 3197 CG2 ILE A 422 15316 15872 10048 1445 -1084 1185 A C
ATOM 3198 CD1 ILE A 422 20.734 14.621 512.067 1.00104.37 A C
ANISOU 3198 CD1 ILE A 422 14582 14744 10327 1003 -1425 925 A C
ATOM 3199 N PRO A 423 20.118 16.978 517.583 1.00113.79 A N
ANISOU 3199 N PRO A 423 16837 16792 9606 1968 -1130 621 A N
ATOM 3200 CA PRO A 423 20.070 16.561 518.984 1.00116.65 A C
ANISOU 3200 CA PRO A 423 17325 17432 9566 2137 -1142 761 A C
ATOM 3201 C PRO A 423 19.321 15.251 519.143 1.00119.28 A C
ANISOU 3201 C PRO A 423 17326 18025 9969 2120 -1043 1252 A C
ATOM 3202 O PRO A 423 18.298 15.009 518.497 1.00122.92 A O
ANISOU 3202 O PRO A 423 17543 18568 10594 2125 -832 1533 A O
ATOM 3203 CB PRO A 423 19.311 17.705 519.654 1.00120.68 A C
ANISOU 3203 CB PRO A 423 18182 18049 9621 2521 -885 650 A C
ATOM 3204 CG PRO A 423 18.382 18.170 518.577 1.00122.07 A C
ANISOU 3204 CG PRO A 423 18204 18164 10011 2589 -620 724 A C
ATOM 3205 CD PRO A 423 19.176 18.072 517.304 1.00116.62 A C
ANISOU 3205 CD PRO A 423 17341 17140 9829 2219 -834 547 A C
ATOM 3206 N LEU A 424 19.854 14.399 520.007 1.00118.54 A N
ANISOU 3206 N LEU A 424 17231 18064 9746 2074 -1217 1373 A N
ATOM 3207 CA LEU A 424 19.266 13.106 520.312 1.00121.44 A C
ANISOU 3207 CA LEU A 424 17345 18660 10138 2031 -1171 1844 A C
ATOM 3208 C LEU A 424 19.010 13.054 521.811 1.00126.49 A C
ANISOU 3208 C LEU A 424 18145 19634 10281 2299 -1091 1974 A C
ATOM 3209 O LEU A 424 19.852 13.487 522.604 1.00129.63 A O
ANISOU 3209 O LEU A 424 18825 20013 10415 2380 -1249 1689 A O
ATOM 3210 CB LEU A 424 20.165 11.958 519.841 1.00116.86 A C
ANISOU 3210 CB LEU A 424 16615 17896 9892 1731 -1459 1913 A C
ATOM 3211 CG LEU A 424 20.498 12.022 518.343 1.00108.71 A C
ANISOU 3211 CG LEU A 424 15457 16526 9322 1505 -1540 1770 A C
ATOM 3212 CD1 LEU A 424 21.629 11.064 517.975 1.00103.36 A C
ANISOU 3212 CD1 LEU A 424 14719 15661 8890 1306 -1833 1764 A C
ATOM 3213 CD2 LEU A 424 19.261 11.772 517.484 1.00103.77 A C
ANISOU 3213 CD2 LEU A 424 14613 15913 8904 1439 -1333 2068 A C
ATOM 3214 N LYS A 425 17.850 12.543 522.209 1.00125.61 A N
ANISOU 3214 N LYS A 425 17854 19848 10023 2431 -855 2421 A N
ATOM 3215 CA LYS A 425 17.465 12.588 523.612 1.00131.88 A C
ANISOU 3215 CA LYS A 425 18795 21005 10311 2750 -721 2575 A C
ATOM 3216 C LYS A 425 16.983 11.225 524.079 1.00124.93 A C
ANISOU 3216 C LYS A 425 17644 20394 9429 2651 -717 3108 A C
ATOM 3217 O LYS A 425 16.092 10.631 523.466 1.00123.80 A O
ANISOU 3217 O LYS A 425 17190 20347 9504 2501 -602 3508 A O
ATOM 3218 CB LYS A 425 16.384 13.649 523.845 1.00143.18 A C
ANISOU 3218 CB LYS A 425 20334 22660 11409 3152 -355 2608 A C
ATOM 3219 CG LYS A 425 16.822 15.066 523.462 1.00146.12 A C
ANISOU 3219 CG LYS A 425 21065 22731 11722 3275 -357 2077 A C
ATOM 3220 CD LYS A 425 15.911 16.129 524.073 1.00149.90 A C
ANISOU 3220 CD LYS A 425 21814 23437 11705 3794 -8 2073 A C
ATOM 3221 CE LYS A 425 16.409 17.541 523.774 1.00144.88 A C
ANISOU 3221 CE LYS A 425 21642 22441 10964 3908 -48 1527 A C
ATOM 3222 NZ LYS A 425 15.632 18.575 524.518 1.00147.62 A N1+
ANISOU 3222 NZ LYS A 425 22384 22968 10736 4482 273 1489 A N1+
ATOM 3223 N SER A 426 17.573 10.739 525.164 1.00128.95 A N
ANISOU 3223 N SER A 426 18287 21025 9683 2712 -859 3126 A N
ATOM 3224 CA SER A 426 17.116 9.518 525.813 1.00134.25 A C
ANISOU 3224 CA SER A 426 18763 21978 10270 2663 -845 3636 A C
ATOM 3225 C SER A 426 17.564 9.576 527.271 1.00130.74 A C
ANISOU 3225 C SER A 426 18567 21758 9349 2928 -885 3567 A C
ATOM 3226 O SER A 426 17.786 10.662 527.818 1.00128.10 A O
ANISOU 3226 O SER A 426 18547 21447 8677 3214 -827 3219 A O
ATOM 3227 CB SER A 426 17.646 8.278 525.074 1.00137.04 A C
ANISOU 3227 CB SER A 426 18947 22060 11060 2251 -1114 3782 A C
ATOM 3228 OG SER A 426 19.022 8.063 525.348 1.00139.33 A O
ANISOU 3228 OG SER A 426 19423 22148 11369 2187 -1411 3473 A O
ATOM 3229 N ASP A 427 17.711 8.413 527.891 1.00131.99 A N
ANISOU 3229 N ASP A 427 18626 22057 9467 2829 -1000 3892 A N
ATOM 3230 CA ASP A 427 18.154 8.336 529.275 1.00135.15 A C
ANISOU 3230 CA ASP A 427 19241 22684 9426 3063 -1056 3863 A C
ATOM 3231 C ASP A 427 19.675 8.442 529.387 1.00127.53 A C
ANISOU 3231 C ASP A 427 18504 21446 8505 2949 -1406 3413 A C
ATOM 3232 O ASP A 427 20.369 8.708 528.404 1.00122.62 A O
ANISOU 3232 O ASP A 427 17880 20480 8230 2728 -1577 3108 A O
ATOM 3233 CB ASP A 427 17.668 7.032 529.912 1.00146.32 A C
ANISOU 3233 CB ASP A 427 20447 24379 10768 3004 -1031 4432 A C
ATOM 3234 CG ASP A 427 16.191 6.767 529.649 1.00154.04 A C
ANISOU 3234 CG ASP A 427 21110 25645 11774 3002 -737 4969 A C
ATOM 3235 OD1 ASP A 427 15.519 7.643 529.056 1.00151.35 A O
ANISOU 3235 OD1 ASP A 427 20713 25329 11465 3114 -520 4896 A O
ATOM 3236 OD2 ASP A 427 15.704 5.682 530.045 1.00160.26 A O1-
ANISOU 3236 OD2 ASP A 427 21702 26650 12539 2881 -729 5490 A O1-
ATOM 3237 N SER A 432 24.125 11.900 522.722 1.00110.66 A N
ANISOU 3237 N SER A 432 16378 17258 8410 1731 -2323 1284 A N
ATOM 3238 CA SER A 432 22.962 12.770 522.652 1.00112.62 A C
ANISOU 3238 CA SER A 432 16736 17528 8526 1904 -2025 1250 A C
ATOM 3239 C SER A 432 23.121 13.793 521.525 1.00116.81 A C
ANISOU 3239 C SER A 432 17303 17770 9310 1794 -2017 938 A C
ATOM 3240 O SER A 432 22.533 14.874 521.569 1.00123.92 A O
ANISOU 3240 O SER A 432 18417 18640 10025 1955 -1839 766 A O
ATOM 3241 CB SER A 432 22.726 13.466 524.005 1.00116.78 A C
ANISOU 3241 CB SER A 432 17601 18270 8500 2176 -1955 1147 A C
ATOM 3242 OG SER A 432 23.918 14.005 524.555 1.00113.19 A O
ANISOU 3242 OG SER A 432 17399 17756 7850 2096 -2253 819 A O
ATOM 3243 N TYR A 433 23.907 13.435 520.508 1.00113.77 A N
ANISOU 3243 N TYR A 433 16723 17175 9330 1551 -2197 883 A N
ATOM 3244 CA TYR A 433 24.145 14.310 519.365 1.00111.03 A C
ANISOU 3244 CA TYR A 433 16370 16558 9257 1423 -2206 616 A C
ATOM 3245 C TYR A 433 24.612 13.494 518.162 1.00105.34 A C
ANISOU 3245 C TYR A 433 15356 15665 9004 1227 -2308 726 A C
ATOM 3246 O TYR A 433 25.226 12.433 518.311 1.00106.36 A O
ANISOU 3246 O TYR A 433 15361 15849 9202 1173 -2469 901 A O
ATOM 3247 CB TYR A 433 25.187 15.388 519.691 1.00107.28 A C
ANISOU 3247 CB TYR A 433 16153 16000 8610 1336 -2437 232 A C
ATOM 3248 CG TYR A 433 24.619 16.706 520.169 1.00109.00 A C
ANISOU 3248 CG TYR A 433 16757 16176 8482 1506 -2298 -12 A C
ATOM 3249 CD1 TYR A 433 23.949 17.554 519.297 1.00109.40 A C
ANISOU 3249 CD1 TYR A 433 16863 16033 8670 1554 -2091 -135 A C
ATOM 3250 CD2 TYR A 433 24.777 17.113 521.485 1.00116.85 A C
ANISOU 3250 CD2 TYR A 433 18103 17308 8986 1642 -2379 -123 A C
ATOM 3251 CE1 TYR A 433 23.434 18.765 519.731 1.00115.14 A C
ANISOU 3251 CE1 TYR A 433 18005 16697 9045 1764 -1952 -355 A C
ATOM 3252 CE2 TYR A 433 24.269 18.319 521.928 1.00121.23 A C
ANISOU 3252 CE2 TYR A 433 19101 17785 9174 1845 -2253 -356 A C
ATOM 3253 CZ TYR A 433 23.601 19.141 521.049 1.00120.67 A C
ANISOU 3253 CZ TYR A 433 19098 17511 9239 1918 -2035 -469 A C
ATOM 3254 OH TYR A 433 23.100 20.341 521.497 1.00123.22 A O
ANISOU 3254 OH TYR A 433 19921 17737 9162 2171 -1900 -696 A O
ATOM 3255 N LEU A 434 24.313 14.005 516.967 1.00 99.96 A N
ANISOU 3255 N LEU A 434 14597 14768 8617 1154 -2204 623 A N
ATOM 3256 CA LEU A 434 24.930 13.534 515.727 1.00101.35 A C
ANISOU 3256 CA LEU A 434 14563 14738 9209 987 -2318 634 A C
ATOM 3257 C LEU A 434 25.281 14.753 514.890 1.00104.22 A C
ANISOU 3257 C LEU A 434 14971 14902 9727 896 -2329 315 A C
ATOM 3258 O LEU A 434 24.402 15.558 514.566 1.00106.26 A O
ANISOU 3258 O LEU A 434 15314 15085 9976 964 -2116 228 A O
ATOM 3259 CB LEU A 434 24.014 12.593 514.935 1.00 98.68 A C
ANISOU 3259 CB LEU A 434 14051 14319 9122 968 -2170 938 A C
ATOM 3260 CG LEU A 434 24.552 12.126 513.572 1.00 90.16 A C
ANISOU 3260 CG LEU A 434 12822 12989 8445 840 -2268 941 A C
ATOM 3261 CD1 LEU A 434 25.802 11.268 513.720 1.00 90.94 A C
ANISOU 3261 CD1 LEU A 434 12877 13101 8573 828 -2517 996 A C
ATOM 3262 CD2 LEU A 434 23.488 11.379 512.793 1.00 88.93 A C
ANISOU 3262 CD2 LEU A 434 12575 12722 8491 791 -2130 1216 A C
ATOM 3263 N LEU A 435 26.556 14.880 514.533 1.00104.02 A N
ANISOU 3263 N LEU A 435 14876 14813 9834 753 -2572 172 A N
ATOM 3264 CA LEU A 435 27.074 16.076 513.889 1.00104.63 A C
ANISOU 3264 CA LEU A 435 15007 14728 10018 622 -2638 -121 A C
ATOM 3265 C LEU A 435 27.598 15.751 512.496 1.00103.24 A C
ANISOU 3265 C LEU A 435 14572 14394 10260 520 -2682 -84 A C
ATOM 3266 O LEU A 435 28.131 14.664 512.251 1.00102.02 A O
ANISOU 3266 O LEU A 435 14235 14286 10242 536 -2781 114 A O
ATOM 3267 CB LEU A 435 28.189 16.712 514.737 1.00103.59 A C
ANISOU 3267 CB LEU A 435 15025 14704 9631 498 -2919 -313 A C
ATOM 3268 CG LEU A 435 27.956 16.760 516.252 1.00104.71 A C
ANISOU 3268 CG LEU A 435 15431 15038 9317 611 -2948 -318 A C
ATOM 3269 CD1 LEU A 435 29.115 17.436 516.966 1.00108.39 A C
ANISOU 3269 CD1 LEU A 435 16062 15581 9541 427 -3276 -515 A C
ATOM 3270 CD2 LEU A 435 26.639 17.441 516.604 1.00106.13 A C
ANISOU 3270 CD2 LEU A 435 15886 15167 9271 812 -2661 -389 A C
ATOM 3271 N LEU A 436 27.434 16.709 511.583 1.00 98.25 A N
ANISOU 3271 N LEU A 436 13957 13567 9806 448 -2599 -270 A N
ATOM 3272 CA LEU A 436 27.931 16.609 510.217 1.00 89.40 A C
ANISOU 3272 CA LEU A 436 12615 12293 9062 365 -2627 -266 A C
ATOM 3273 C LEU A 436 28.795 17.829 509.930 1.00 87.12 A C
ANISOU 3273 C LEU A 436 12364 11938 8799 181 -2778 -518 A C
ATOM 3274 O LEU A 436 28.378 18.958 510.201 1.00 87.07 A O
ANISOU 3274 O LEU A 436 12610 11836 8636 145 -2718 -733 A O
ATOM 3275 CB LEU A 436 26.781 16.522 509.211 1.00 92.16 A C
ANISOU 3275 CB LEU A 436 12917 12459 9641 435 -2368 -200 A C
ATOM 3276 CG LEU A 436 25.747 15.400 509.344 1.00 92.98 A C
ANISOU 3276 CG LEU A 436 12988 12603 9738 547 -2223 83 A C
ATOM 3277 CD1 LEU A 436 24.686 15.725 510.380 1.00 95.82 A C
ANISOU 3277 CD1 LEU A 436 13513 13108 9786 655 -2055 118 A C
ATOM 3278 CD2 LEU A 436 25.097 15.132 507.997 1.00 87.23 A C
ANISOU 3278 CD2 LEU A 436 12141 11675 9326 532 -2084 174 A C
ATOM 3279 N PHE A 437 29.991 17.601 509.389 1.00 87.84 A N
ANISOU 3279 N PHE A 437 12223 12087 9066 74 -2975 -469 A N
ATOM 3280 CA PHE A 437 30.969 18.654 509.144 1.00 90.62 A C
ANISOU 3280 CA PHE A 437 12553 12434 9443 -160 -3172 -637 A C
ATOM 3281 C PHE A 437 31.270 18.765 507.656 1.00 92.40 A C
ANISOU 3281 C PHE A 437 12539 12528 10042 -192 -3117 -614 A C
ATOM 3282 O PHE A 437 31.452 17.753 506.972 1.00 89.71 A O
ANISOU 3282 O PHE A 437 11971 12212 9903 -48 -3071 -415 A O
ATOM 3283 CB PHE A 437 32.267 18.385 509.899 1.00 94.05 A C
ANISOU 3283 CB PHE A 437 12865 13155 9715 -282 -3487 -545 A C
ATOM 3284 CG PHE A 437 32.080 18.169 511.366 1.00102.50 A C
ANISOU 3284 CG PHE A 437 14155 14380 10409 -238 -3564 -547 A C
ATOM 3285 CD1 PHE A 437 31.382 19.087 512.135 1.00108.17 A C
ANISOU 3285 CD1 PHE A 437 15263 14989 10846 -267 -3515 -768 A C
ATOM 3286 CD2 PHE A 437 32.595 17.040 511.982 1.00109.00 A C
ANISOU 3286 CD2 PHE A 437 14825 15456 11135 -131 -3673 -320 A C
ATOM 3287 CE1 PHE A 437 31.212 18.890 513.501 1.00109.01 A C
ANISOU 3287 CE1 PHE A 437 15593 15250 10577 -195 -3579 -765 A C
ATOM 3288 CE2 PHE A 437 32.422 16.834 513.344 1.00112.46 A C
ANISOU 3288 CE2 PHE A 437 15464 16048 11219 -83 -3741 -313 A C
ATOM 3289 CZ PHE A 437 31.731 17.762 514.104 1.00109.65 A C
ANISOU 3289 CZ PHE A 437 15487 15594 10583 -118 -3694 -536 A C
ATOM 3290 N ARG A 438 31.347 19.999 507.163 1.00 98.97 A N
ANISOU 3290 N ARG A 438 13458 13204 10940 -369 -3128 -816 A N
ATOM 3291 CA ARG A 438 31.588 20.268 505.752 1.00 97.02 A C
ANISOU 3291 CA ARG A 438 13003 12827 11032 -407 -3064 -811 A C
ATOM 3292 C ARG A 438 32.720 21.278 505.627 1.00105.08 A C
ANISOU 3292 C ARG A 438 13962 13908 12055 -714 -3317 -894 A C
ATOM 3293 O ARG A 438 32.728 22.300 506.321 1.00107.10 A O
ANISOU 3293 O ARG A 438 14514 14095 12085 -917 -3440 -1089 A O
ATOM 3294 CB ARG A 438 30.314 20.777 505.071 1.00 91.81 A C
ANISOU 3294 CB ARG A 438 12507 11884 10493 -310 -2773 -941 A C
ATOM 3295 CG ARG A 438 29.950 20.065 503.773 1.00 93.01 A C
ANISOU 3295 CG ARG A 438 12438 11928 10972 -153 -2594 -804 A C
ATOM 3296 CD ARG A 438 28.447 20.154 503.517 1.00 95.57 A C
ANISOU 3296 CD ARG A 438 12921 12070 11320 -16 -2308 -844 A C
ATOM 3297 NE ARG A 438 28.079 19.876 502.129 1.00 97.71 A N
ANISOU 3297 NE ARG A 438 13038 12184 11905 61 -2158 -776 A N
ATOM 3298 CZ ARG A 438 26.824 19.831 501.688 1.00 94.43 A C
ANISOU 3298 CZ ARG A 438 12684 11641 11555 161 -1927 -752 A C
ATOM 3299 NH1 ARG A 438 25.822 20.038 502.531 1.00 85.52 A N1+
ANISOU 3299 NH1 ARG A 438 11739 10555 10200 227 -1797 -766 A N1+
ATOM 3300 NH2 ARG A 438 26.569 19.577 500.408 1.00 90.27 A N
ANISOU 3300 NH2 ARG A 438 12028 10969 11301 207 -1827 -691 A N
ATOM 3301 N VAL A 439 33.676 20.981 504.748 1.00106.79 A N
ANISOU 3301 N VAL A 439 13814 14258 12503 -744 -3404 -724 A N
ATOM 3302 CA VAL A 439 34.884 21.784 504.588 1.00104.33 A C
ANISOU 3302 CA VAL A 439 13339 14094 12208 -1061 -3673 -703 A C
ATOM 3303 C VAL A 439 34.569 23.038 503.779 1.00105.99 A C
ANISOU 3303 C VAL A 439 13690 14017 12563 -1241 -3602 -901 A C
ATOM 3304 O VAL A 439 33.735 23.026 502.867 1.00110.00 A O
ANISOU 3304 O VAL A 439 14220 14292 13281 -1059 -3328 -960 A O
ATOM 3305 CB VAL A 439 35.985 20.927 503.927 1.00105.56 A C
ANISOU 3305 CB VAL A 439 13015 14555 12536 -952 -3750 -389 A C
ATOM 3306 CG1 VAL A 439 37.119 21.784 503.393 1.00119.37 A C
ANISOU 3306 CG1 VAL A 439 14504 16470 14383 -1265 -3968 -306 A C
ATOM 3307 CG2 VAL A 439 36.524 19.898 504.918 1.00101.63 A C
ANISOU 3307 CG2 VAL A 439 12411 14377 11827 -831 -3893 -192 A C
ATOM 3308 N SER A 481 30.835 27.200 503.788 1.00105.42 A N
ANISOU 3308 N SER A 481 15298 12633 12125 -1254 -3009 -1929 A N
ATOM 3309 CA SER A 481 30.724 25.837 503.306 1.00100.10 A C
ANISOU 3309 CA SER A 481 14180 12166 11689 -1027 -2868 -1692 A C
ATOM 3310 C SER A 481 29.667 25.748 502.214 1.00 95.69 A C
ANISOU 3310 C SER A 481 13546 11433 11378 -782 -2523 -1687 A C
ATOM 3311 O SER A 481 28.878 26.671 501.993 1.00 98.69 A O
ANISOU 3311 O SER A 481 14214 11573 11711 -725 -2351 -1858 A O
ATOM 3312 CB SER A 481 30.369 24.887 504.444 1.00 98.65 A C
ANISOU 3312 CB SER A 481 14046 12172 11267 -844 -2855 -1607 A C
ATOM 3313 OG SER A 481 29.848 23.672 503.946 1.00 93.55 A O
ANISOU 3313 OG SER A 481 13115 11613 10818 -587 -2655 -1410 A O
ATOM 3314 N GLN A 482 29.679 24.625 501.513 1.00 95.48 A N
ANISOU 3314 N GLN A 482 13151 11526 11600 -631 -2433 -1480 A N
ATOM 3315 CA GLN A 482 28.583 24.300 500.622 1.00 93.29 A C
ANISOU 3315 CA GLN A 482 12810 11119 11517 -401 -2132 -1437 A C
ATOM 3316 C GLN A 482 27.281 24.334 501.415 1.00 94.23 A C
ANISOU 3316 C GLN A 482 13207 11204 11393 -211 -1930 -1487 A C
ATOM 3317 O GLN A 482 27.200 23.703 502.480 1.00 92.42 A O
ANISOU 3317 O GLN A 482 13038 11138 10940 -151 -1988 -1415 A O
ATOM 3318 CB GLN A 482 28.796 22.916 500.013 1.00 92.41 A C
ANISOU 3318 CB GLN A 482 12363 11131 11616 -266 -2118 -1197 A C
ATOM 3319 CG GLN A 482 27.954 22.654 498.796 1.00 91.30 A C
ANISOU 3319 CG GLN A 482 12127 10835 11727 -113 -1882 -1143 A C
ATOM 3320 CD GLN A 482 28.397 23.493 497.631 1.00 82.78 A C
ANISOU 3320 CD GLN A 482 10946 9623 10882 -206 -1866 -1223 A C
ATOM 3321 NE2 GLN A 482 29.680 23.834 497.611 1.00 78.71 A N
ANISOU 3321 NE2 GLN A 482 10299 9213 10395 -387 -2085 -1215 A N
ATOM 3322 OE1 GLN A 482 27.604 23.832 496.754 1.00 78.88 A O
ANISOU 3322 OE1 GLN A 482 10472 8960 10537 -125 -1664 -1266 A O
ATOM 3323 N PRO A 483 26.260 25.061 500.960 1.00100.85 A N
ANISOU 3323 N PRO A 483 14206 11867 12245 -92 -1685 -1584 A N
ATOM 3324 CA PRO A 483 25.034 25.141 501.755 1.00102.54 A C
ANISOU 3324 CA PRO A 483 14658 12115 12188 130 -1475 -1586 A C
ATOM 3325 C PRO A 483 24.339 23.792 501.803 1.00 99.62 A C
ANISOU 3325 C PRO A 483 14055 11923 11873 277 -1366 -1323 A C
ATOM 3326 O PRO A 483 24.437 22.973 500.882 1.00 93.08 A O
ANISOU 3326 O PRO A 483 12945 11091 11328 257 -1369 -1173 A O
ATOM 3327 CB PRO A 483 24.189 26.193 501.019 1.00 92.38 A C
ANISOU 3327 CB PRO A 483 13528 10625 10947 244 -1229 -1704 A C
ATOM 3328 CG PRO A 483 24.975 26.565 499.770 1.00 93.63 A C
ANISOU 3328 CG PRO A 483 13507 10628 11440 57 -1319 -1761 A C
ATOM 3329 CD PRO A 483 26.029 25.524 499.584 1.00 97.96 A C
ANISOU 3329 CD PRO A 483 13725 11326 12171 -85 -1542 -1613 A C
ATOM 3330 N TRP A 484 23.600 23.584 502.886 1.00 93.19 A N
ANISOU 3330 N TRP A 484 13395 11254 10760 428 -1273 -1258 A N
ATOM 3331 CA TRP A 484 22.908 22.323 503.107 1.00 90.40 A C
ANISOU 3331 CA TRP A 484 12854 11084 10410 527 -1195 -978 A C
ATOM 3332 C TRP A 484 21.631 22.328 502.281 1.00 95.13 A C
ANISOU 3332 C TRP A 484 13342 11666 11136 654 -923 -841 A C
ATOM 3333 O TRP A 484 20.625 22.920 502.678 1.00 92.53 A O
ANISOU 3333 O TRP A 484 13154 11411 10592 843 -698 -827 A O
ATOM 3334 CB TRP A 484 22.608 22.120 504.589 1.00 91.60 A C
ANISOU 3334 CB TRP A 484 13186 11436 10183 638 -1196 -926 A C
ATOM 3335 CG TRP A 484 23.814 22.081 505.496 1.00 99.15 A C
ANISOU 3335 CG TRP A 484 14254 12443 10976 506 -1480 -1039 A C
ATOM 3336 CD1 TRP A 484 24.343 23.126 506.201 1.00105.77 A C
ANISOU 3336 CD1 TRP A 484 15414 13214 11560 453 -1597 -1286 A C
ATOM 3337 CD2 TRP A 484 24.652 20.947 505.779 1.00 99.01 A C
ANISOU 3337 CD2 TRP A 484 14046 12554 11020 404 -1699 -895 A C
ATOM 3338 CE2 TRP A 484 25.656 21.380 506.671 1.00 95.48 A C
ANISOU 3338 CE2 TRP A 484 13765 12159 10355 288 -1937 -1049 A C
ATOM 3339 CE3 TRP A 484 24.649 19.609 505.367 1.00 92.55 A C
ANISOU 3339 CE3 TRP A 484 12972 11797 10396 406 -1727 -645 A C
ATOM 3340 NE1 TRP A 484 25.443 22.711 506.917 1.00101.29 A N
ANISOU 3340 NE1 TRP A 484 14828 12759 10897 296 -1886 -1291 A N
ATOM 3341 CZ2 TRP A 484 26.644 20.527 507.153 1.00 93.73 A C
ANISOU 3341 CZ2 TRP A 484 13401 12097 10114 197 -2179 -941 A C
ATOM 3342 CZ3 TRP A 484 25.634 18.763 505.850 1.00 89.26 A C
ANISOU 3342 CZ3 TRP A 484 12468 11499 9948 347 -1956 -555 A C
ATOM 3343 CH2 TRP A 484 26.616 19.226 506.732 1.00 91.63 A C
ANISOU 3343 CH2 TRP A 484 12878 11898 10040 254 -2168 -694 A C
ATOM 3344 N ARG A 485 21.669 21.673 501.120 1.00 95.40 A N
ANISOU 3344 N ARG A 485 13132 11617 11498 570 -942 -723 A N
ATOM 3345 CA ARG A 485 20.451 21.478 500.349 1.00 92.64 A C
ANISOU 3345 CA ARG A 485 12648 11284 11266 643 -731 -539 A C
ATOM 3346 C ARG A 485 19.462 20.647 501.164 1.00 97.98 A C
ANISOU 3346 C ARG A 485 13274 12210 11744 716 -648 -246 A C
ATOM 3347 O ARG A 485 19.844 19.870 502.042 1.00 94.06 A O
ANISOU 3347 O ARG A 485 12798 11823 11116 678 -791 -157 A O
ATOM 3348 CB ARG A 485 20.768 20.821 498.998 1.00 92.67 A C
ANISOU 3348 CB ARG A 485 12454 11131 11625 525 -816 -469 A C
ATOM 3349 CG ARG A 485 21.671 21.685 498.100 1.00100.63 A C
ANISOU 3349 CG ARG A 485 13468 11933 12837 469 -866 -714 A C
ATOM 3350 CD ARG A 485 22.503 20.884 497.072 1.00104.85 A C
ANISOU 3350 CD ARG A 485 13840 12347 13652 385 -1024 -660 A C
ATOM 3351 NE ARG A 485 23.730 21.602 496.688 1.00111.00 A N
ANISOU 3351 NE ARG A 485 14603 13032 14541 316 -1138 -857 A N
ATOM 3352 CZ ARG A 485 24.476 21.327 495.614 1.00108.23 A C
ANISOU 3352 CZ ARG A 485 14108 12583 14433 296 -1216 -843 A C
ATOM 3353 NH1 ARG A 485 24.130 20.348 494.785 1.00114.26 A N1+
ANISOU 3353 NH1 ARG A 485 14793 13276 15345 353 -1202 -677 A N1+
ATOM 3354 NH2 ARG A 485 25.570 22.037 495.360 1.00 92.88 A N
ANISOU 3354 NH2 ARG A 485 12114 10614 12563 216 -1319 -976 A N
ATOM 3355 N THR A 486 18.172 20.838 500.877 1.00108.64 A N
ANISOU 3355 N THR A 486 14538 13678 13061 821 -413 -67 A N
ATOM 3356 CA THR A 486 17.113 20.360 501.765 1.00108.90 A C
ANISOU 3356 CA THR A 486 14516 14019 12842 922 -284 235 A C
ATOM 3357 C THR A 486 16.992 18.836 501.748 1.00107.89 A C
ANISOU 3357 C THR A 486 14222 13959 12814 728 -449 547 A C
ATOM 3358 O THR A 486 16.701 18.222 502.782 1.00110.09 A O
ANISOU 3358 O THR A 486 14502 14456 12872 749 -465 750 A O
ATOM 3359 CB THR A 486 15.780 21.017 501.401 1.00103.43 A C
ANISOU 3359 CB THR A 486 13731 13489 12080 1099 18 390 A C
ATOM 3360 CG2 THR A 486 14.763 20.729 502.464 1.00 96.92 A C
ANISOU 3360 CG2 THR A 486 12849 13045 10931 1259 178 706 A C
ATOM 3361 OG1 THR A 486 15.950 22.437 501.340 1.00107.84 A O
ANISOU 3361 OG1 THR A 486 14514 13917 12542 1295 161 81 A O
ATOM 3362 N ALA A 487 17.190 18.209 500.582 1.00 97.31 A N
ANISOU 3362 N ALA A 487 12776 12418 11780 547 -575 598 A N
ATOM 3363 CA ALA A 487 17.069 16.756 500.497 1.00 91.65 A C
ANISOU 3363 CA ALA A 487 11994 11693 11135 358 -755 888 A C
ATOM 3364 C ALA A 487 18.065 16.037 501.393 1.00 92.45 A C
ANISOU 3364 C ALA A 487 12219 11777 11132 338 -960 845 A C
ATOM 3365 O ALA A 487 17.773 14.933 501.861 1.00106.29 A O
ANISOU 3365 O ALA A 487 13967 13613 12807 238 -1063 1124 A O
ATOM 3366 CB ALA A 487 17.256 16.295 499.052 1.00 92.65 A C
ANISOU 3366 CB ALA A 487 12085 11543 11574 209 -871 890 A C
ATOM 3367 N GLN A 488 19.253 16.604 501.613 1.00 90.83 A N
ANISOU 3367 N GLN A 488 12118 11469 10924 410 -1040 530 A N
ATOM 3368 CA GLN A 488 20.210 15.926 502.487 1.00 93.02 A C
ANISOU 3368 CA GLN A 488 12482 11777 11084 402 -1238 517 A C
ATOM 3369 C GLN A 488 19.848 16.083 503.968 1.00 95.65 A C
ANISOU 3369 C GLN A 488 12885 12382 11075 501 -1168 580 A C
ATOM 3370 O GLN A 488 20.013 15.135 504.744 1.00 98.40 A O
ANISOU 3370 O GLN A 488 13260 12830 11296 472 -1288 753 A O
ATOM 3371 CB GLN A 488 21.633 16.399 502.201 1.00 99.06 A C
ANISOU 3371 CB GLN A 488 13287 12395 11955 412 -1378 223 A C
ATOM 3372 CG GLN A 488 22.034 16.256 500.747 1.00 97.62 A C
ANISOU 3372 CG GLN A 488 13033 11972 12085 364 -1427 175 A C
ATOM 3373 CD GLN A 488 21.998 17.576 500.025 1.00104.22 A C
ANISOU 3373 CD GLN A 488 13840 12719 13041 384 -1293 -57 A C
ATOM 3374 NE2 GLN A 488 21.510 17.563 498.781 1.00105.76 A N
ANISOU 3374 NE2 GLN A 488 13959 12763 13461 359 -1216 -13 A N
ATOM 3375 OE1 GLN A 488 22.403 18.608 500.579 1.00 99.39 A O
ANISOU 3375 OE1 GLN A 488 13304 12155 12305 413 -1272 -272 A O
ATOM 3376 N LEU A 489 19.336 17.254 504.373 1.00 95.14 A N
ANISOU 3376 N LEU A 489 12882 12432 10834 645 -969 452 A N
ATOM 3377 CA LEU A 489 18.947 17.476 505.769 1.00 99.49 A C
ANISOU 3377 CA LEU A 489 13544 13243 11015 798 -877 507 A C
ATOM 3378 C LEU A 489 17.969 16.416 506.253 1.00106.08 A C
ANISOU 3378 C LEU A 489 14247 14318 11742 773 -826 927 A C
ATOM 3379 O LEU A 489 18.120 15.865 507.352 1.00102.18 A O
ANISOU 3379 O LEU A 489 13809 13989 11025 805 -896 1039 A O
ATOM 3380 CB LEU A 489 18.354 18.874 505.983 1.00107.99 A C
ANISOU 3380 CB LEU A 489 14757 14382 11892 1016 -632 344 A C
ATOM 3381 CG LEU A 489 19.014 20.196 505.596 1.00110.58 A C
ANISOU 3381 CG LEU A 489 15281 14480 12253 1055 -632 -50 A C
ATOM 3382 CD1 LEU A 489 18.067 21.344 505.868 1.00113.44 A C
ANISOU 3382 CD1 LEU A 489 15814 14930 12359 1331 -343 -101 A C
ATOM 3383 CD2 LEU A 489 20.240 20.391 506.465 1.00105.59 A C
ANISOU 3383 CD2 LEU A 489 14861 13796 11460 1001 -864 -288 A C
ATOM 3384 N TYR A 490 16.928 16.142 505.467 1.00111.03 A N
ANISOU 3384 N TYR A 490 14690 14987 12508 699 -711 1187 A N
ATOM 3385 CA TYR A 490 15.890 15.236 505.949 1.00109.50 A C
ANISOU 3385 CA TYR A 490 14350 15066 12188 636 -663 1638 A C
ATOM 3386 C TYR A 490 16.403 13.801 505.932 1.00104.57 A C
ANISOU 3386 C TYR A 490 13747 14306 11680 402 -939 1808 A C
ATOM 3387 O TYR A 490 16.027 12.996 506.795 1.00105.43 A O
ANISOU 3387 O TYR A 490 13833 14618 11610 358 -976 2108 A O
ATOM 3388 CB TYR A 490 14.641 15.332 505.067 1.00109.39 A C
ANISOU 3388 CB TYR A 490 14115 15160 12289 571 -500 1910 A C
ATOM 3389 CG TYR A 490 13.812 16.595 505.213 1.00118.01 A C
ANISOU 3389 CG TYR A 490 15159 16487 13194 859 -175 1883 A C
ATOM 3390 CD1 TYR A 490 13.007 16.831 506.321 1.00126.59 A C
ANISOU 3390 CD1 TYR A 490 16205 17976 13916 1098 41 2113 A C
ATOM 3391 CD2 TYR A 490 13.781 17.529 504.180 1.00114.47 A C
ANISOU 3391 CD2 TYR A 490 14709 15862 12920 920 -67 1659 A C
ATOM 3392 CE1 TYR A 490 12.225 17.995 506.418 1.00125.37 A C
ANISOU 3392 CE1 TYR A 490 16046 18037 13553 1436 365 2106 A C
ATOM 3393 CE2 TYR A 490 13.001 18.673 504.269 1.00110.93 A C
ANISOU 3393 CE2 TYR A 490 14255 15610 12284 1221 242 1648 A C
ATOM 3394 CZ TYR A 490 12.233 18.911 505.378 1.00112.98 A C
ANISOU 3394 CZ TYR A 490 14506 16260 12163 1496 461 1867 A C
ATOM 3395 OH TYR A 490 11.476 20.063 505.450 1.00108.93 A O
ANISOU 3395 OH TYR A 490 14030 15934 11425 1866 788 1860 A O
ATOM 3396 N ALA A 491 17.272 13.475 504.966 1.00 96.06 A N
ANISOU 3396 N ALA A 491 12735 12885 10879 280 -1127 1630 A N
ATOM 3397 CA ALA A 491 18.037 12.237 505.029 1.00 95.37 A C
ANISOU 3397 CA ALA A 491 12759 12626 10852 157 -1387 1711 A C
ATOM 3398 C ALA A 491 18.778 12.119 506.357 1.00102.39 A C
ANISOU 3398 C ALA A 491 13750 13660 11495 281 -1457 1635 A C
ATOM 3399 O ALA A 491 18.883 11.023 506.925 1.00110.19 A O
ANISOU 3399 O ALA A 491 14800 14676 12393 212 -1596 1861 A O
ATOM 3400 CB ALA A 491 19.016 12.174 503.859 1.00 94.93 A C
ANISOU 3400 CB ALA A 491 12775 12219 11074 126 -1530 1475 A C
ATOM 3401 N ALA A 492 19.289 13.242 506.876 1.00107.06 A N
ANISOU 3401 N ALA A 492 14388 14332 11957 452 -1376 1326 A N
ATOM 3402 CA ALA A 492 20.056 13.201 508.122 1.00105.54 A C
ANISOU 3402 CA ALA A 492 14310 14275 11516 553 -1470 1232 A C
ATOM 3403 C ALA A 492 19.155 13.009 509.338 1.00101.79 A C
ANISOU 3403 C ALA A 492 13829 14125 10720 640 -1343 1490 A C
ATOM 3404 O ALA A 492 19.460 12.194 510.219 1.00 98.13 A O
ANISOU 3404 O ALA A 492 13417 13767 10099 637 -1462 1636 A O
ATOM 3405 CB ALA A 492 20.902 14.466 508.272 1.00104.34 A C
ANISOU 3405 CB ALA A 492 14258 14081 11306 654 -1472 830 A C
ATOM 3406 N ARG A 493 18.044 13.752 509.415 1.00104.08 A N
ANISOU 3406 N ARG A 493 14053 14604 10889 751 -1087 1572 A N
ATOM 3407 CA ARG A 493 17.121 13.532 510.528 1.00113.90 A C
ANISOU 3407 CA ARG A 493 15254 16211 11812 869 -938 1880 A C
ATOM 3408 C ARG A 493 16.548 12.117 510.513 1.00112.28 A C
ANISOU 3408 C ARG A 493 14909 16080 11671 651 -1034 2340 A C
ATOM 3409 O ARG A 493 16.327 11.528 511.578 1.00107.10 A O
ANISOU 3409 O ARG A 493 14256 15662 10773 687 -1040 2584 A O
ATOM 3410 CB ARG A 493 15.988 14.565 510.514 1.00115.39 A C
ANISOU 3410 CB ARG A 493 15373 16622 11847 1078 -619 1937 A C
ATOM 3411 CG ARG A 493 15.055 14.473 511.729 1.00115.65 A C
ANISOU 3411 CG ARG A 493 15357 17092 11491 1284 -423 2266 A C
ATOM 3412 CD ARG A 493 13.791 15.287 511.532 1.00117.90 A C
ANISOU 3412 CD ARG A 493 15507 17646 11645 1505 -88 2442 A C
ATOM 3413 NE ARG A 493 13.097 14.901 510.307 1.00121.37 A N
ANISOU 3413 NE ARG A 493 15672 18043 12401 1261 -82 2693 A N
ATOM 3414 CZ ARG A 493 12.142 15.622 509.726 1.00119.42 A C
ANISOU 3414 CZ ARG A 493 15268 17953 12151 1393 169 2809 A C
ATOM 3415 NH1 ARG A 493 11.764 16.779 510.258 1.00118.71 A N1+
ANISOU 3415 NH1 ARG A 493 15300 18055 11748 1810 454 2690 A N1+
ATOM 3416 NH2 ARG A 493 11.569 15.191 508.607 1.00110.58 A N
ANISOU 3416 NH2 ARG A 493 13902 16791 11321 1125 128 3046 A N
ATOM 3417 N ASP A 494 16.325 11.545 509.323 1.00105.15 A N
ANISOU 3417 N ASP A 494 13919 14956 11076 411 -1128 2466 A N
ATOM 3418 CA ASP A 494 15.764 10.199 509.253 1.00 97.61 A C
ANISOU 3418 CA ASP A 494 12903 14015 10170 151 -1262 2910 A C
ATOM 3419 C ASP A 494 16.792 9.139 509.614 1.00 95.87 A C
ANISOU 3419 C ASP A 494 12878 13591 9957 79 -1530 2889 A C
ATOM 3420 O ASP A 494 16.462 8.161 510.295 1.00 99.06 A O
ANISOU 3420 O ASP A 494 13298 14115 10224 -28 -1612 3235 A O
ATOM 3421 CB ASP A 494 15.190 9.931 507.867 1.00 98.46 A C
ANISOU 3421 CB ASP A 494 12923 13922 10566 -96 -1309 3047 A C
ATOM 3422 CG ASP A 494 13.790 10.459 507.720 1.00106.67 A C
ANISOU 3422 CG ASP A 494 13698 15293 11538 -102 -1070 3336 A C
ATOM 3423 OD1 ASP A 494 13.579 11.654 508.019 1.00110.75 A O1-
ANISOU 3423 OD1 ASP A 494 14151 16013 11915 184 -816 3156 A O1-
ATOM 3424 OD2 ASP A 494 12.897 9.675 507.332 1.00110.60 A O1-
ANISOU 3424 OD2 ASP A 494 14068 15859 12098 -391 -1143 3766 A O1-
ATOM 3425 N ILE A 495 18.041 9.298 509.169 1.00 97.92 A N
ANISOU 3425 N ILE A 495 13279 13563 10363 146 -1666 2521 A N
ATOM 3426 CA ILE A 495 19.064 8.350 509.604 1.00 97.60 A C
ANISOU 3426 CA ILE A 495 13410 13389 10283 152 -1893 2516 A C
ATOM 3427 C ILE A 495 19.241 8.438 511.112 1.00 92.88 A C
ANISOU 3427 C ILE A 495 12830 13101 9360 310 -1854 2541 A C
ATOM 3428 O ILE A 495 19.313 7.414 511.803 1.00 91.80 A O
ANISOU 3428 O ILE A 495 12772 13014 9093 266 -1972 2790 A O
ATOM 3429 CB ILE A 495 20.392 8.588 508.860 1.00 91.62 A C
ANISOU 3429 CB ILE A 495 12743 12352 9718 235 -2022 2155 A C
ATOM 3430 CG1 ILE A 495 20.285 8.129 507.404 1.00 90.94 A C
ANISOU 3430 CG1 ILE A 495 12707 11924 9923 93 -2103 2195 A C
ATOM 3431 CG2 ILE A 495 21.523 7.842 509.545 1.00 88.88 A C
ANISOU 3431 CG2 ILE A 495 12530 11983 9256 332 -2212 2139 A C
ATOM 3432 CD1 ILE A 495 20.206 6.619 507.223 1.00 87.53 A C
ANISOU 3432 CD1 ILE A 495 12477 11275 9506 -50 -2303 2506 A C
ATOM 3433 N ALA A 496 19.251 9.668 511.649 1.00 94.83 A N
ANISOU 3433 N ALA A 496 13039 13548 9444 498 -1689 2295 A N
ATOM 3434 CA ALA A 496 19.426 9.880 513.087 1.00 94.90 A C
ANISOU 3434 CA ALA A 496 13112 13843 9103 675 -1652 2280 A C
ATOM 3435 C ALA A 496 18.267 9.301 513.888 1.00 96.49 A C
ANISOU 3435 C ALA A 496 13226 14353 9084 664 -1530 2721 A C
ATOM 3436 O ALA A 496 18.461 8.816 515.008 1.00 96.54 A O
ANISOU 3436 O ALA A 496 13295 14543 8842 740 -1579 2848 A O
ATOM 3437 CB ALA A 496 19.580 11.371 513.385 1.00 91.34 A C
ANISOU 3437 CB ALA A 496 12722 13482 8500 872 -1509 1921 A C
ATOM 3438 N ARG A 497 17.053 9.362 513.339 1.00 98.64 A N
ANISOU 3438 N ARG A 497 13327 14719 9431 570 -1370 2986 A N
ATOM 3439 CA ARG A 497 15.885 8.837 514.037 1.00100.48 A C
ANISOU 3439 CA ARG A 497 13413 15307 9458 535 -1248 3476 A C
ATOM 3440 C ARG A 497 16.056 7.351 514.325 1.00104.39 A C
ANISOU 3440 C ARG A 497 13972 15719 9971 310 -1479 3801 A C
ATOM 3441 O ARG A 497 15.842 6.893 515.454 1.00110.57 A O
ANISOU 3441 O ARG A 497 14750 16774 10486 373 -1458 4053 A O
ATOM 3442 CB ARG A 497 14.639 9.093 513.184 1.00100.31 A C
ANISOU 3442 CB ARG A 497 13158 15392 9563 415 -1083 3736 A C
ATOM 3443 CG ARG A 497 13.325 8.655 513.790 1.00107.90 A C
ANISOU 3443 CG ARG A 497 13884 16795 10316 361 -937 4310 A C
ATOM 3444 CD ARG A 497 12.864 9.632 514.849 1.00114.82 A C
ANISOU 3444 CD ARG A 497 14708 18110 10811 768 -629 4301 A C
ATOM 3445 NE ARG A 497 11.711 9.127 515.588 1.00124.70 A N
ANISOU 3445 NE ARG A 497 15713 19851 11817 759 -486 4898 A N
ATOM 3446 CZ ARG A 497 11.257 9.662 516.719 1.00131.90 A C
ANISOU 3446 CZ ARG A 497 16586 21204 12326 1131 -228 5015 A C
ATOM 3447 NH1 ARG A 497 11.848 10.733 517.239 1.00131.82 A N1+
ANISOU 3447 NH1 ARG A 497 16825 21159 12101 1526 -104 4549 A N1+
ATOM 3448 NH2 ARG A 497 10.198 9.139 517.323 1.00134.46 A N
ANISOU 3448 NH2 ARG A 497 16639 22009 12441 1108 -99 5618 A N
ATOM 3449 N ASP A 498 16.496 6.590 513.321 1.00104.92 A N
ANISOU 3449 N ASP A 498 14145 15389 10330 75 -1705 3786 A N
ATOM 3450 CA ASP A 498 16.724 5.161 513.506 1.00111.63 A C
ANISOU 3450 CA ASP A 498 15151 16076 11187 -121 -1944 4070 A C
ATOM 3451 C ASP A 498 17.891 4.906 514.449 1.00115.28 A C
ANISOU 3451 C ASP A 498 15784 16534 11481 83 -2054 3881 A C
ATOM 3452 O ASP A 498 17.884 3.931 515.207 1.00120.86 A O
ANISOU 3452 O ASP A 498 16580 17306 12035 28 -2159 4170 A O
ATOM 3453 CB ASP A 498 16.963 4.500 512.154 1.00117.47 A C
ANISOU 3453 CB ASP A 498 16044 16351 12239 -356 -2151 4055 A C
ATOM 3454 CG ASP A 498 15.752 4.584 511.255 1.00127.67 A C
ANISOU 3454 CG ASP A 498 17174 17657 13679 -619 -2089 4312 A C
ATOM 3455 OD1 ASP A 498 14.972 5.549 511.408 1.00123.96 A O1-
ANISOU 3455 OD1 ASP A 498 16439 17527 13134 -524 -1838 4338 A O1-
ATOM 3456 OD2 ASP A 498 15.580 3.695 510.395 1.00138.34 A O1-
ANISOU 3456 OD2 ASP A 498 18683 18681 15199 -907 -2296 4495 A O1-
ATOM 3457 N LEU A 499 18.916 5.758 514.395 1.00113.35 A N
ANISOU 3457 N LEU A 499 15587 16220 11261 297 -2050 3418 A N
ATOM 3458 CA LEU A 499 20.052 5.616 515.297 1.00113.85 A C
ANISOU 3458 CA LEU A 499 15775 16334 11148 480 -2166 3245 A C
ATOM 3459 C LEU A 499 19.616 5.747 516.750 1.00116.32 A C
ANISOU 3459 C LEU A 499 16048 17053 11096 619 -2047 3406 A C
ATOM 3460 O LEU A 499 19.937 4.896 517.590 1.00116.33 A O
ANISOU 3460 O LEU A 499 16140 17132 10930 643 -2159 3590 A O
ATOM 3461 CB LEU A 499 21.105 6.668 514.949 1.00113.20 A C
ANISOU 3461 CB LEU A 499 15705 16158 11147 627 -2185 2758 A C
ATOM 3462 CG LEU A 499 22.560 6.465 515.365 1.00116.12 A C
ANISOU 3462 CG LEU A 499 16178 16490 11453 753 -2381 2555 A C
ATOM 3463 CD1 LEU A 499 23.160 5.259 514.676 1.00116.33 A C
ANISOU 3463 CD1 LEU A 499 16319 16220 11663 696 -2575 2689 A C
ATOM 3464 CD2 LEU A 499 23.336 7.718 515.000 1.00115.73 A C
ANISOU 3464 CD2 LEU A 499 16088 16410 11473 827 -2379 2126 A C
ATOM 3465 N LEU A 500 18.860 6.802 517.058 1.00108.55 A N
ANISOU 3465 N LEU A 500 15232 16906 9106 288 663 693 A N
ATOM 3466 CA LEU A 500 18.372 6.991 518.417 1.00109.17 A C
ANISOU 3466 CA LEU A 500 14980 17078 9423 547 614 769 A C
ATOM 3467 C LEU A 500 17.479 5.831 518.845 1.00116.67 A C
ANISOU 3467 C LEU A 500 15816 18182 10333 440 422 846 A C
ATOM 3468 O LEU A 500 17.558 5.370 519.989 1.00118.40 A O
ANISOU 3468 O LEU A 500 15859 18398 10730 583 458 752 A O
ATOM 3469 CB LEU A 500 17.638 8.329 518.527 1.00107.50 A C
ANISOU 3469 CB LEU A 500 14598 16965 9283 738 543 1041 A C
ATOM 3470 CG LEU A 500 17.145 8.713 519.922 1.00104.89 A C
ANISOU 3470 CG LEU A 500 13954 16701 9199 1025 543 1124 A C
ATOM 3471 CD1 LEU A 500 18.328 8.844 520.862 1.00106.23 A C
ANISOU 3471 CD1 LEU A 500 14109 16690 9562 1190 780 836 A C
ATOM 3472 CD2 LEU A 500 16.349 10.006 519.888 1.00104.37 A C
ANISOU 3472 CD2 LEU A 500 13753 16713 9190 1207 499 1421 A C
ATOM 3473 N ILE B 24 8.127 -4.652 454.057 1.00 35.43 B N
ANISOU 3473 N ILE B 24 5293 1932 6237 1016 390 -412 B N
ATOM 3474 CA ILE B 24 8.611 -4.925 452.707 1.00 36.27 B C
ANISOU 3474 CA ILE B 24 5361 1993 6425 934 530 -533 B C
ATOM 3475 C ILE B 24 7.441 -5.187 451.771 1.00 35.93 B C
ANISOU 3475 C ILE B 24 5408 1931 6313 789 556 -618 B C
ATOM 3476 O ILE B 24 7.367 -6.268 451.176 1.00 62.28 B O
ANISOU 3476 O ILE B 24 8720 5203 9738 764 722 -709 B O
ATOM 3477 CB ILE B 24 9.572 -6.118 452.705 1.00 45.09 B C
ANISOU 3477 CB ILE B 24 6353 3040 7738 1042 717 -565 B C
ATOM 3478 CG1 ILE B 24 9.019 -7.222 453.613 1.00 50.54 B C
ANISOU 3478 CG1 ILE B 24 7055 3703 8446 1138 724 -505 B C
ATOM 3479 CG2 ILE B 24 10.955 -5.695 453.153 1.00 39.50 B C
ANISOU 3479 CG2 ILE B 24 5506 2333 7170 1153 728 -512 B C
ATOM 3480 CD1 ILE B 24 9.547 -8.574 453.324 1.00 41.63 B C
ANISOU 3480 CD1 ILE B 24 5849 2483 7487 1200 930 -555 B C
ATOM 3481 N PRO B 25 6.543 -4.224 451.550 1.00 46.03 B N
ANISOU 3481 N PRO B 25 6784 3249 7457 682 418 -597 B N
ATOM 3482 CA PRO B 25 5.410 -4.464 450.652 1.00 34.41 B C
ANISOU 3482 CA PRO B 25 5386 1751 5939 546 424 -672 B C
ATOM 3483 C PRO B 25 5.719 -4.281 449.176 1.00 43.22 B C
ANISOU 3483 C PRO B 25 6509 2807 7106 385 553 -810 B C
ATOM 3484 O PRO B 25 4.820 -4.498 448.360 1.00 40.96 B O
ANISOU 3484 O PRO B 25 6293 2493 6777 255 561 -889 B O
ATOM 3485 CB PRO B 25 4.393 -3.434 451.124 1.00 32.85 B C
ANISOU 3485 CB PRO B 25 5263 1600 5618 509 252 -577 B C
ATOM 3486 CG PRO B 25 5.223 -2.301 451.544 1.00 41.02 B C
ANISOU 3486 CG PRO B 25 6305 2681 6599 543 177 -503 B C
ATOM 3487 CD PRO B 25 6.476 -2.878 452.147 1.00 35.33 B C
ANISOU 3487 CD PRO B 25 5479 1955 5990 681 260 -497 B C
ATOM 3488 N ASN B 26 6.952 -3.911 448.803 1.00 47.23 B N
ANISOU 3488 N ASN B 26 6949 3289 7708 375 673 -855 B N
ATOM 3489 CA ASN B 26 7.314 -3.670 447.398 1.00 45.08 B C
ANISOU 3489 CA ASN B 26 6708 2964 7455 192 835 -1008 B C
ATOM 3490 C ASN B 26 6.304 -2.766 446.695 1.00 46.06 B C
ANISOU 3490 C ASN B 26 6965 3101 7434 10 678 -1011 B C
ATOM 3491 O ASN B 26 5.960 -2.975 445.533 1.00 58.70 B O
ANISOU 3491 O ASN B 26 8651 4675 8979 -174 779 -1149 B O
ATOM 3492 CB ASN B 26 7.463 -4.978 446.631 1.00 53.00 B C
ANISOU 3492 CB ASN B 26 7703 3908 8526 145 1101 -1170 B C
ATOM 3493 CG ASN B 26 8.808 -5.618 446.833 1.00 53.19 B C
ANISOU 3493 CG ASN B 26 7589 3891 8731 263 1321 -1203 B C
ATOM 3494 ND2 ASN B 26 9.221 -6.439 445.888 1.00 44.03 B N
ANISOU 3494 ND2 ASN B 26 6428 2671 7631 177 1604 -1374 B N
ATOM 3495 OD1 ASN B 26 9.468 -5.375 447.836 1.00 72.91 B O
ANISOU 3495 OD1 ASN B 26 9981 6411 11311 427 1237 -1078 B O
ATOM 3496 N ALA B 27 5.818 -1.759 447.415 1.00 47.11 B N
ANISOU 3496 N ALA B 27 7127 3281 7491 51 433 -857 B N
ATOM 3497 CA ALA B 27 4.887 -0.781 446.878 1.00 34.47 B C
ANISOU 3497 CA ALA B 27 5633 1681 5781 -101 253 -818 B C
ATOM 3498 C ALA B 27 4.914 0.433 447.785 1.00 50.29 B C
ANISOU 3498 C ALA B 27 7664 3732 7711 -32 76 -648 B C
ATOM 3499 O ALA B 27 5.350 0.361 448.938 1.00 50.03 B O
ANISOU 3499 O ALA B 27 7584 3750 7676 133 82 -570 B O
ATOM 3500 CB ALA B 27 3.469 -1.327 446.776 1.00 36.85 B C
ANISOU 3500 CB ALA B 27 5991 1980 6029 -133 160 -821 B C
ATOM 3501 N ILE B 28 4.458 1.558 447.240 1.00 43.91 B N
ANISOU 3501 N ILE B 28 6939 2922 6822 -178 -46 -592 B N
ATOM 3502 CA ILE B 28 4.441 2.816 447.968 1.00 43.65 B C
ANISOU 3502 CA ILE B 28 6937 2984 6666 -158 -24 -441 B C
ATOM 3503 C ILE B 28 3.077 3.453 447.786 1.00 41.36 B C
ANISOU 3503 C ILE B 28 6576 2744 6395 -245 81 -384 B C
ATOM 3504 O ILE B 28 2.318 3.103 446.882 1.00 41.25 B O
ANISOU 3504 O ILE B 28 6537 2691 6446 -369 95 -458 B O
ATOM 3505 CB ILE B 28 5.552 3.786 447.508 1.00 38.76 B C
ANISOU 3505 CB ILE B 28 6300 2311 6114 -258 -35 -446 B C
ATOM 3506 CG1 ILE B 28 5.390 4.151 446.034 1.00 43.40 B C
ANISOU 3506 CG1 ILE B 28 6827 2842 6821 -472 -168 -510 B C
ATOM 3507 CG2 ILE B 28 6.932 3.210 447.755 1.00 34.26 B C
ANISOU 3507 CG2 ILE B 28 5605 1688 5725 -161 35 -533 B C
ATOM 3508 CD1 ILE B 28 5.999 5.511 445.704 1.00 46.87 B C
ANISOU 3508 CD1 ILE B 28 7222 3261 7325 -612 -55 -464 B C
ATOM 3509 N GLN B 29 2.758 4.364 448.694 1.00 36.35 B N
ANISOU 3509 N GLN B 29 5851 2174 5788 -158 40 -269 B N
ATOM 3510 CA GLN B 29 1.623 5.234 448.485 1.00 32.81 B C
ANISOU 3510 CA GLN B 29 5345 1746 5373 -205 -73 -190 B C
ATOM 3511 C GLN B 29 1.970 6.253 447.402 1.00 42.79 B C
ANISOU 3511 C GLN B 29 6632 2978 6648 -359 -228 -158 B C
ATOM 3512 O GLN B 29 3.120 6.684 447.285 1.00 54.58 B O
ANISOU 3512 O GLN B 29 8140 4446 8151 -395 -217 -167 B O
ATOM 3513 CB GLN B 29 1.254 5.952 449.774 1.00 27.64 B C
ANISOU 3513 CB GLN B 29 4626 1192 4682 -74 -95 -87 B C
ATOM 3514 CG GLN B 29 1.218 5.065 450.984 1.00 27.39 B C
ANISOU 3514 CG GLN B 29 4593 1173 4642 67 -47 -100 B C
ATOM 3515 CD GLN B 29 0.634 5.784 452.180 1.00 38.69 B C
ANISOU 3515 CD GLN B 29 5945 2661 6092 151 -138 -26 B C
ATOM 3516 NE2 GLN B 29 1.392 5.841 453.269 1.00 27.82 B N
ANISOU 3516 NE2 GLN B 29 4550 1311 4711 236 -125 -16 B N
ATOM 3517 OE1 GLN B 29 -0.508 6.258 452.134 1.00 27.07 B O
ANISOU 3517 OE1 GLN B 29 4441 1201 4642 134 -214 15 B O
ATOM 3518 N PRO B 30 1.014 6.634 446.593 1.00 39.01 B N
ANISOU 3518 N PRO B 30 6193 2493 6135 -463 -390 -104 B N
ATOM 3519 CA PRO B 30 1.338 7.466 445.433 1.00 37.84 B C
ANISOU 3519 CA PRO B 30 6161 2316 5902 -650 -551 -45 B C
ATOM 3520 C PRO B 30 1.524 8.955 445.707 1.00 42.10 B C
ANISOU 3520 C PRO B 30 6680 2896 6418 -630 -649 106 B C
ATOM 3521 O PRO B 30 1.507 9.728 444.745 1.00 60.70 B O
ANISOU 3521 O PRO B 30 9152 5235 8676 -791 -795 205 B O
ATOM 3522 CB PRO B 30 0.143 7.219 444.504 1.00 33.37 B C
ANISOU 3522 CB PRO B 30 5686 1733 5259 -785 -713 -22 B C
ATOM 3523 CG PRO B 30 -0.965 6.899 445.418 1.00 32.20 B C
ANISOU 3523 CG PRO B 30 5411 1615 5208 -619 -687 -5 B C
ATOM 3524 CD PRO B 30 -0.349 6.089 446.515 1.00 35.86 B C
ANISOU 3524 CD PRO B 30 5784 2096 5746 -458 -436 -106 B C
ATOM 3525 N PHE B 31 1.713 9.407 446.951 1.00 46.75 B N
ANISOU 3525 N PHE B 31 7157 3541 7065 -465 -568 129 B N
ATOM 3526 CA PHE B 31 2.030 10.825 447.118 1.00 30.51 B C
ANISOU 3526 CA PHE B 31 5095 1505 4994 -475 -637 235 B C
ATOM 3527 C PHE B 31 3.542 11.133 446.914 1.00 41.60 B C
ANISOU 3527 C PHE B 31 6535 2868 6403 -559 -587 204 B C
ATOM 3528 O PHE B 31 4.026 12.213 447.300 1.00 32.87 B O
ANISOU 3528 O PHE B 31 5409 1773 5309 -555 -603 262 B O
ATOM 3529 CB PHE B 31 1.528 11.348 448.471 1.00 29.17 B C
ANISOU 3529 CB PHE B 31 4823 1406 4852 -314 -583 260 B C
ATOM 3530 CG PHE B 31 2.213 10.765 449.700 1.00 51.23 B C
ANISOU 3530 CG PHE B 31 7564 4240 7659 -197 -434 176 B C
ATOM 3531 CD1 PHE B 31 1.770 9.569 450.274 1.00 59.84 B C
ANISOU 3531 CD1 PHE B 31 8631 5349 8756 -108 -361 117 B C
ATOM 3532 CD2 PHE B 31 3.255 11.439 450.314 1.00 28.23 B C
ANISOU 3532 CD2 PHE B 31 4640 1331 4755 -187 -416 173 B C
ATOM 3533 CE1 PHE B 31 2.369 9.044 451.414 1.00 38.49 B C
ANISOU 3533 CE1 PHE B 31 5901 2664 6060 -7 -302 74 B C
ATOM 3534 CE2 PHE B 31 3.850 10.929 451.443 1.00 33.23 B C
ANISOU 3534 CE2 PHE B 31 5240 1989 5397 -91 -358 120 B C
ATOM 3535 CZ PHE B 31 3.405 9.721 451.996 1.00 36.23 B C
ANISOU 3535 CZ PHE B 31 5602 2386 5778 3 -312 79 B C
ATOM 3536 N GLY B 32 4.267 10.207 446.293 1.00 43.02 B N
ANISOU 3536 N GLY B 32 6770 2991 6586 -649 -518 100 B N
ATOM 3537 CA GLY B 32 5.634 10.438 445.880 1.00 37.04 B C
ANISOU 3537 CA GLY B 32 6056 2178 5838 -773 -468 63 B C
ATOM 3538 C GLY B 32 6.118 9.314 444.989 1.00 43.85 B C
ANISOU 3538 C GLY B 32 7009 2976 6676 -902 -379 -75 B C
ATOM 3539 O GLY B 32 5.341 8.463 444.556 1.00 54.57 B O
ANISOU 3539 O GLY B 32 8416 4332 7987 -920 -380 -134 B O
ATOM 3540 N ALA B 33 7.416 9.329 444.704 1.00 35.06 B N
ANISOU 3540 N ALA B 33 5928 1809 5584 -1013 -285 -142 B N
ATOM 3541 CA ALA B 33 8.048 8.257 443.948 1.00 36.43 B C
ANISOU 3541 CA ALA B 33 6198 1941 5702 -1135 -100 -317 B C
ATOM 3542 C ALA B 33 9.277 7.751 444.697 1.00 55.30 B C
ANISOU 3542 C ALA B 33 8404 4321 8286 -989 59 -424 B C
ATOM 3543 O ALA B 33 9.822 8.434 445.572 1.00 35.69 B O
ANISOU 3543 O ALA B 33 5816 1812 5933 -903 -18 -354 B O
ATOM 3544 CB ALA B 33 8.433 8.710 442.545 1.00 43.41 B C
ANISOU 3544 CB ALA B 33 7195 2958 6342 -1402 -14 -309 B C
ATOM 3545 N MET B 34 9.704 6.529 444.357 1.00 51.20 B N
ANISOU 3545 N MET B 34 7841 3817 7794 -960 279 -595 B N
ATOM 3546 CA MET B 34 10.819 5.890 445.047 1.00 46.88 B C
ANISOU 3546 CA MET B 34 7098 3253 7463 -794 431 -686 B C
ATOM 3547 C MET B 34 11.765 5.197 444.074 1.00 50.41 B C
ANISOU 3547 C MET B 34 7501 3772 7879 -896 730 -851 B C
ATOM 3548 O MET B 34 11.326 4.569 443.107 1.00 55.77 B O
ANISOU 3548 O MET B 34 8316 4470 8406 -1023 856 -960 B O
ATOM 3549 CB MET B 34 10.325 4.892 446.078 1.00 36.30 B C
ANISOU 3549 CB MET B 34 5698 1822 6271 -540 392 -704 B C
ATOM 3550 CG MET B 34 11.440 4.271 446.861 1.00 48.45 B C
ANISOU 3550 CG MET B 34 7031 3341 8035 -349 512 -754 B C
ATOM 3551 SD MET B 34 10.808 2.918 447.844 1.00 35.83 B S
ANISOU 3551 SD MET B 34 5394 1788 6432 -73 466 -725 B S
ATOM 3552 CE MET B 34 10.368 3.804 449.339 1.00 33.76 B C
ANISOU 3552 CE MET B 34 5138 1607 6081 60 184 -530 B C
ATOM 3553 N LEU B 35 13.068 5.335 444.334 1.00 49.94 B N
ANISOU 3553 N LEU B 35 7249 3756 7968 -852 847 -876 B N
ATOM 3554 CA LEU B 35 14.126 4.591 443.664 1.00 54.61 B C
ANISOU 3554 CA LEU B 35 7735 4390 8623 -889 1165 -1039 B C
ATOM 3555 C LEU B 35 14.928 3.805 444.696 1.00 57.21 B C
ANISOU 3555 C LEU B 35 7813 4657 9269 -619 1235 -1073 B C
ATOM 3556 O LEU B 35 15.157 4.277 445.815 1.00 42.16 B O
ANISOU 3556 O LEU B 35 5777 2741 7500 -475 1038 -955 B O
ATOM 3557 CB LEU B 35 15.072 5.515 442.911 1.00 44.92 B C
ANISOU 3557 CB LEU B 35 6471 3285 7310 -1101 1269 -1028 B C
ATOM 3558 CG LEU B 35 14.487 6.425 441.841 1.00 45.37 B C
ANISOU 3558 CG LEU B 35 6770 3420 7049 -1380 1208 -958 B C
ATOM 3559 CD1 LEU B 35 15.623 7.253 441.250 1.00 47.35 B C
ANISOU 3559 CD1 LEU B 35 6950 3772 7269 -1563 1355 -948 B C
ATOM 3560 CD2 LEU B 35 13.740 5.623 440.778 1.00 55.77 B C
ANISOU 3560 CD2 LEU B 35 8301 4748 8140 -1511 1334 -1080 B C
ATOM 3561 N ILE B 36 15.360 2.610 444.318 1.00 44.93 B N
ANISOU 3561 N ILE B 36 6192 3055 7825 -554 1515 -1231 B N
ATOM 3562 CA ILE B 36 16.273 1.814 445.122 1.00 45.78 B C
ANISOU 3562 CA ILE B 36 6038 3104 8252 -301 1621 -1256 B C
ATOM 3563 C ILE B 36 17.503 1.571 444.271 1.00 53.65 B C
ANISOU 3563 C ILE B 36 6886 4160 9337 -390 1950 -1393 B C
ATOM 3564 O ILE B 36 17.401 0.998 443.173 1.00 50.26 B O
ANISOU 3564 O ILE B 36 6587 3718 8793 -532 2219 -1557 B O
ATOM 3565 CB ILE B 36 15.649 0.486 445.571 1.00 52.98 B C
ANISOU 3565 CB ILE B 36 6987 3856 9288 -94 1685 -1311 B C
ATOM 3566 CG1 ILE B 36 14.375 0.732 446.376 1.00 49.68 B C
ANISOU 3566 CG1 ILE B 36 6721 3375 8781 -23 1386 -1182 B C
ATOM 3567 CG2 ILE B 36 16.649 -0.298 446.406 1.00 51.25 B C
ANISOU 3567 CG2 ILE B 36 6488 3574 9410 182 1784 -1299 B C
ATOM 3568 CD1 ILE B 36 13.655 -0.550 446.766 1.00 42.28 B C
ANISOU 3568 CD1 ILE B 36 5810 2457 7798 140 1376 -1160 B C
ATOM 3569 N VAL B 37 18.658 1.979 444.792 1.00 49.67 B N
ANISOU 3569 N VAL B 37 6108 3722 9041 -312 1937 -1334 B N
ATOM 3570 CA VAL B 37 19.923 1.961 444.071 1.00 65.11 B C
ANISOU 3570 CA VAL B 37 7876 5749 11115 -404 2235 -1441 B C
ATOM 3571 C VAL B 37 20.884 1.040 444.810 1.00 64.51 B C
ANISOU 3571 C VAL B 37 7470 5611 11429 -119 2349 -1455 B C
ATOM 3572 O VAL B 37 20.988 1.114 446.039 1.00 69.21 B O
ANISOU 3572 O VAL B 37 7912 6200 12185 91 2091 -1312 B O
ATOM 3573 CB VAL B 37 20.494 3.388 443.956 1.00 52.78 B C
ANISOU 3573 CB VAL B 37 6250 4330 9472 -597 2116 -1350 B C
ATOM 3574 CG1 VAL B 37 21.753 3.417 443.142 1.00 55.94 B C
ANISOU 3574 CG1 VAL B 37 6465 4806 9985 -722 2447 -1464 B C
ATOM 3575 CG2 VAL B 37 19.468 4.275 443.322 1.00 51.28 B C
ANISOU 3575 CG2 VAL B 37 6387 4177 8918 -841 1975 -1296 B C
ATOM 3576 N GLU B 38 21.577 0.170 444.066 1.00 56.95 B N
ANISOU 3576 N GLU B 38 6408 4607 10623 -110 2738 -1623 B N
ATOM 3577 CA GLU B 38 22.649 -0.639 444.651 1.00 64.96 B C
ANISOU 3577 CA GLU B 38 7065 5565 12053 158 2878 -1625 B C
ATOM 3578 C GLU B 38 23.890 0.221 444.863 1.00 60.69 B C
ANISOU 3578 C GLU B 38 6205 5174 11679 117 2834 -1557 B C
ATOM 3579 O GLU B 38 24.415 0.794 443.906 1.00 62.27 B O
ANISOU 3579 O GLU B 38 6404 5464 11791 -127 3039 -1649 B O
ATOM 3580 CB GLU B 38 23.020 -1.817 443.748 1.00 69.42 B C
ANISOU 3580 CB GLU B 38 7610 6009 12756 177 3347 -1839 B C
ATOM 3581 CG GLU B 38 22.130 -3.038 443.798 1.00 71.94 B C
ANISOU 3581 CG GLU B 38 8115 6134 13083 315 3444 -1917 B C
ATOM 3582 CD GLU B 38 22.845 -4.320 443.326 1.00 77.65 B C
ANISOU 3582 CD GLU B 38 8701 6758 14045 409 3832 -2046 B C
ATOM 3583 OE1 GLU B 38 23.793 -4.249 442.509 1.00 69.21 B O
ANISOU 3583 OE1 GLU B 38 7495 5718 13084 301 4170 -2191 B O
ATOM 3584 OE2 GLU B 38 22.448 -5.411 443.791 1.00 87.82 B O1-
ANISOU 3584 OE2 GLU B 38 10034 7991 15343 550 3738 -1947 B O1-
ATOM 3585 N LYS B 39 24.392 0.275 446.100 1.00 73.38 B N
ANISOU 3585 N LYS B 39 7539 6810 13532 347 2579 -1401 B N
ATOM 3586 CA LYS B 39 25.554 1.114 446.403 1.00 74.20 B C
ANISOU 3586 CA LYS B 39 7318 7067 13807 300 2491 -1335 B C
ATOM 3587 C LYS B 39 26.773 0.709 445.578 1.00 78.31 B C
ANISOU 3587 C LYS B 39 7561 7600 14593 268 2907 -1475 B C
ATOM 3588 O LYS B 39 27.462 1.561 445.006 1.00 80.91 B O
ANISOU 3588 O LYS B 39 7791 8051 14901 42 3007 -1517 B O
ATOM 3589 CB LYS B 39 25.882 1.048 447.896 1.00 61.92 B C
ANISOU 3589 CB LYS B 39 5512 5543 12472 569 2146 -1152 B C
ATOM 3590 CG LYS B 39 27.032 1.949 448.307 1.00 63.64 B C
ANISOU 3590 CG LYS B 39 5388 5935 12859 505 2001 -1085 B C
ATOM 3591 CD LYS B 39 27.509 1.676 449.737 1.00 64.30 B C
ANISOU 3591 CD LYS B 39 5182 6062 13188 787 1686 -915 B C
ATOM 3592 CE LYS B 39 28.607 2.659 450.148 1.00 69.77 B C
ANISOU 3592 CE LYS B 39 5539 6946 14023 682 1505 -861 B C
ATOM 3593 NZ LYS B 39 28.059 3.971 450.578 1.00 82.72 B N1+
ANISOU 3593 NZ LYS B 39 7390 8676 15365 472 1176 -803 B N1+
ATOM 3594 N ASP B 40 27.052 -0.591 445.500 1.00 76.71 B N
ANISOU 3594 N ASP B 40 7231 7257 14656 492 3177 -1552 B N
ATOM 3595 CA ASP B 40 28.276 -1.044 444.848 1.00 79.86 B C
ANISOU 3595 CA ASP B 40 7317 7649 15379 508 3585 -1679 B C
ATOM 3596 C ASP B 40 28.235 -0.800 443.339 1.00 89.69 B C
ANISOU 3596 C ASP B 40 8787 8906 16385 181 3976 -1891 B C
ATOM 3597 O ASP B 40 29.196 -0.282 442.761 1.00105.03 B O
ANISOU 3597 O ASP B 40 10533 10948 18427 20 4188 -1956 B O
ATOM 3598 CB ASP B 40 28.537 -2.513 445.191 1.00 80.97 B C
ANISOU 3598 CB ASP B 40 7273 7605 15887 852 3781 -1696 B C
ATOM 3599 CG ASP B 40 27.304 -3.379 445.035 1.00 94.89 B C
ANISOU 3599 CG ASP B 40 9453 9212 17388 873 3785 -1732 B C
ATOM 3600 OD1 ASP B 40 26.204 -2.803 444.888 1.00110.29 B O1-
ANISOU 3600 OD1 ASP B 40 11733 11171 19001 719 3641 -1755 B O1-
ATOM 3601 OD2 ASP B 40 27.423 -4.626 445.071 1.00 93.15 B O1-
ANISOU 3601 OD2 ASP B 40 9263 8893 17238 1001 3868 -1702 B O1-
ATOM 3602 N THR B 41 27.148 -1.181 442.678 1.00 86.76 B N
ANISOU 3602 N THR B 41 8826 8441 15697 69 4080 -2000 B N
ATOM 3603 CA THR B 41 27.049 -1.023 441.232 1.00 83.67 B C
ANISOU 3603 CA THR B 41 8688 8071 15034 -249 4440 -2201 B C
ATOM 3604 C THR B 41 26.556 0.356 440.803 1.00 74.78 B C
ANISOU 3604 C THR B 41 7823 7102 13489 -576 4230 -2132 B C
ATOM 3605 O THR B 41 26.685 0.698 439.622 1.00 75.66 B O
ANISOU 3605 O THR B 41 8103 7270 13375 -865 4510 -2261 B O
ATOM 3606 CB THR B 41 26.119 -2.098 440.654 1.00 82.57 B C
ANISOU 3606 CB THR B 41 8872 7768 14734 -245 4652 -2366 B C
ATOM 3607 CG2 THR B 41 26.574 -3.473 441.085 1.00 74.71 B C
ANISOU 3607 CG2 THR B 41 7641 6586 14162 81 4863 -2416 B C
ATOM 3608 OG1 THR B 41 24.776 -1.874 441.114 1.00 68.89 B O
ANISOU 3608 OG1 THR B 41 7446 6025 12703 -253 4269 -2253 B O
ATOM 3609 N GLN B 42 26.006 1.148 441.728 1.00 73.55 B N
ANISOU 3609 N GLN B 42 7711 7008 13227 -538 3760 -1931 B N
ATOM 3610 CA GLN B 42 25.392 2.453 441.436 1.00 80.92 B C
ANISOU 3610 CA GLN B 42 8910 8054 13782 -815 3525 -1838 B C
ATOM 3611 C GLN B 42 24.254 2.314 440.429 1.00 81.96 B C
ANISOU 3611 C GLN B 42 9488 8153 13500 -1020 3613 -1930 B C
ATOM 3612 O GLN B 42 23.922 3.267 439.711 1.00 85.48 B O
ANISOU 3612 O GLN B 42 10168 8692 13620 -1304 3574 -1898 B O
ATOM 3613 CB GLN B 42 26.424 3.468 440.925 1.00 73.99 B C
ANISOU 3613 CB GLN B 42 7871 7309 12933 -1045 3658 -1839 B C
ATOM 3614 CG GLN B 42 27.590 3.717 441.865 1.00 73.91 B C
ANISOU 3614 CG GLN B 42 7397 7360 13327 -887 3550 -1754 B C
ATOM 3615 CD GLN B 42 27.197 4.492 443.103 1.00 81.37 B C
ANISOU 3615 CD GLN B 42 8315 8349 14251 -802 3046 -1555 B C
ATOM 3616 NE2 GLN B 42 26.640 3.797 444.091 1.00 78.26 B N
ANISOU 3616 NE2 GLN B 42 7916 7876 13943 -522 2812 -1481 B N
ATOM 3617 OE1 GLN B 42 27.402 5.707 443.176 1.00 91.08 B O
ANISOU 3617 OE1 GLN B 42 9538 9676 15391 -993 2885 -1474 B O
ATOM 3618 N GLN B 43 23.606 1.152 440.421 1.00 64.61 B N
ANISOU 3618 N GLN B 43 7413 5824 11311 -878 3703 -2027 B N
ATOM 3619 CA GLN B 43 22.564 0.836 439.457 1.00 64.27 B C
ANISOU 3619 CA GLN B 43 7766 5750 10902 -1069 3803 -2145 B C
ATOM 3620 C GLN B 43 21.189 0.979 440.101 1.00 60.67 B C
ANISOU 3620 C GLN B 43 7533 5257 10263 -1004 3399 -2009 B C
ATOM 3621 O GLN B 43 20.942 0.441 441.187 1.00 59.12 B O
ANISOU 3621 O GLN B 43 7216 4962 10284 -726 3221 -1932 B O
ATOM 3622 CB GLN B 43 22.790 -0.584 438.934 1.00 66.75 B C
ANISOU 3622 CB GLN B 43 8069 5929 11365 -987 4222 -2380 B C
ATOM 3623 CG GLN B 43 23.408 -0.619 437.540 1.00 74.91 B C
ANISOU 3623 CG GLN B 43 9190 7015 12258 -1259 4676 -2589 B C
ATOM 3624 CD GLN B 43 23.561 -2.024 436.986 1.00 76.83 B C
ANISOU 3624 CD GLN B 43 9457 7102 12633 -1196 5116 -2851 B C
ATOM 3625 NE2 GLN B 43 24.083 -2.130 435.768 1.00 79.37 B N
ANISOU 3625 NE2 GLN B 43 9876 7459 12821 -1438 5549 -3060 B N
ATOM 3626 OE1 GLN B 43 23.249 -3.003 437.657 1.00 85.17 B O
ANISOU 3626 OE1 GLN B 43 10446 7997 13919 -936 5088 -2867 B O
ATOM 3627 N ILE B 44 20.290 1.693 439.424 1.00 59.61 B N
ANISOU 3627 N ILE B 44 7719 5199 9731 -1258 3262 -1971 B N
ATOM 3628 CA ILE B 44 18.902 1.693 439.858 1.00 56.69 B C
ANISOU 3628 CA ILE B 44 7569 4781 9191 -1213 2936 -1875 B C
ATOM 3629 C ILE B 44 18.363 0.283 439.705 1.00 59.20 B C
ANISOU 3629 C ILE B 44 7979 4960 9553 -1111 3114 -2046 B C
ATOM 3630 O ILE B 44 18.270 -0.243 438.588 1.00 61.90 B O
ANISOU 3630 O ILE B 44 8499 5305 9717 -1299 3400 -2240 B O
ATOM 3631 CB ILE B 44 18.077 2.680 439.040 1.00 56.08 B C
ANISOU 3631 CB ILE B 44 7800 4812 8695 -1508 2776 -1798 B C
ATOM 3632 CG1 ILE B 44 18.538 4.101 439.268 1.00 55.57 B C
ANISOU 3632 CG1 ILE B 44 7658 4849 8609 -1599 2594 -1615 B C
ATOM 3633 CG2 ILE B 44 16.638 2.576 439.426 1.00 53.49 B C
ANISOU 3633 CG2 ILE B 44 7668 4427 8228 -1456 2472 -1715 B C
ATOM 3634 CD1 ILE B 44 18.133 4.983 438.123 1.00 56.45 B C
ANISOU 3634 CD1 ILE B 44 8049 5070 8329 -1926 2585 -1568 B C
ATOM 3635 N VAL B 45 17.995 -0.337 440.822 1.00 57.94 B N
ANISOU 3635 N VAL B 45 7716 4675 9624 -828 2956 -1980 B N
ATOM 3636 CA VAL B 45 17.451 -1.678 440.783 1.00 55.84 B C
ANISOU 3636 CA VAL B 45 7533 4248 9434 -720 3119 -2128 B C
ATOM 3637 C VAL B 45 15.945 -1.706 441.013 1.00 53.35 B C
ANISOU 3637 C VAL B 45 7461 3891 8919 -744 2840 -2066 B C
ATOM 3638 O VAL B 45 15.277 -2.610 440.501 1.00 54.08 B O
ANISOU 3638 O VAL B 45 7725 3894 8929 -805 2985 -2228 B O
ATOM 3639 CB VAL B 45 18.170 -2.610 441.770 1.00 56.45 B C
ANISOU 3639 CB VAL B 45 7319 4180 9949 -374 3225 -2118 B C
ATOM 3640 CG1 VAL B 45 19.560 -2.902 441.285 1.00 59.72 B C
ANISOU 3640 CG1 VAL B 45 7503 4604 10584 -364 3595 -2242 B C
ATOM 3641 CG2 VAL B 45 18.217 -2.003 443.153 1.00 54.11 B C
ANISOU 3641 CG2 VAL B 45 6848 3908 9804 -159 2855 -1870 B C
ATOM 3642 N TYR B 46 15.377 -0.749 441.734 1.00 50.69 B N
ANISOU 3642 N TYR B 46 7143 3610 8507 -714 2460 -1851 B N
ATOM 3643 CA TYR B 46 13.924 -0.697 441.815 1.00 48.69 B C
ANISOU 3643 CA TYR B 46 7114 3326 8060 -766 2216 -1797 B C
ATOM 3644 C TYR B 46 13.431 0.719 441.561 1.00 51.51 B C
ANISOU 3644 C TYR B 46 7598 3825 8150 -958 1932 -1633 B C
ATOM 3645 O TYR B 46 14.072 1.705 441.932 1.00 46.95 B O
ANISOU 3645 O TYR B 46 6899 3324 7617 -948 1818 -1499 B O
ATOM 3646 CB TYR B 46 13.407 -1.212 443.165 1.00 46.63 B C
ANISOU 3646 CB TYR B 46 6749 2972 7996 -468 2014 -1664 B C
ATOM 3647 CG TYR B 46 13.686 -2.678 443.417 1.00 59.20 B C
ANISOU 3647 CG TYR B 46 8206 4536 9751 -274 2198 -1718 B C
ATOM 3648 CD1 TYR B 46 12.877 -3.676 442.861 1.00 48.70 B C
ANISOU 3648 CD1 TYR B 46 7003 3217 8285 -339 2278 -1809 B C
ATOM 3649 CD2 TYR B 46 14.769 -3.073 444.194 1.00 59.40 B C
ANISOU 3649 CD2 TYR B 46 7972 4525 10073 -40 2282 -1665 B C
ATOM 3650 CE1 TYR B 46 13.138 -5.027 443.097 1.00 50.14 B C
ANISOU 3650 CE1 TYR B 46 7069 3357 8625 -185 2444 -1838 B C
ATOM 3651 CE2 TYR B 46 15.040 -4.410 444.426 1.00 50.28 B C
ANISOU 3651 CE2 TYR B 46 6700 3341 9061 120 2431 -1677 B C
ATOM 3652 CZ TYR B 46 14.223 -5.391 443.880 1.00 66.81 B C
ANISOU 3652 CZ TYR B 46 8937 5429 11019 42 2518 -1763 B C
ATOM 3653 OH TYR B 46 14.516 -6.726 444.141 1.00 52.63 B O
ANISOU 3653 OH TYR B 46 7032 3581 9382 187 2665 -1763 B O
ATOM 3654 N ALA B 47 12.275 0.810 440.925 1.00 50.40 B N
ANISOU 3654 N ALA B 47 7696 3711 7742 -1136 1816 -1643 B N
ATOM 3655 CA ALA B 47 11.619 2.089 440.753 1.00 45.86 B C
ANISOU 3655 CA ALA B 47 7246 3239 6941 -1284 1520 -1458 B C
ATOM 3656 C ALA B 47 10.127 1.904 440.942 1.00 44.33 B C
ANISOU 3656 C ALA B 47 7195 2989 6661 -1277 1289 -1408 B C
ATOM 3657 O ALA B 47 9.562 0.915 440.472 1.00 67.43 B O
ANISOU 3657 O ALA B 47 10224 5868 9528 -1332 1403 -1566 B O
ATOM 3658 CB ALA B 47 11.901 2.675 439.369 1.00 60.99 B C
ANISOU 3658 CB ALA B 47 9319 5310 8547 -1598 1629 -1497 B C
ATOM 3659 N SER B 48 9.495 2.857 441.630 1.00 56.20 B N
ANISOU 3659 N SER B 48 8696 4487 8171 -1216 978 -1197 B N
ATOM 3660 CA SER B 48 8.049 2.820 441.790 1.00 40.98 B C
ANISOU 3660 CA SER B 48 6882 2511 6177 -1217 751 -1129 B C
ATOM 3661 C SER B 48 7.365 3.120 440.463 1.00 42.56 B C
ANISOU 3661 C SER B 48 7288 2836 6045 -1510 688 -1139 B C
ATOM 3662 O SER B 48 7.847 3.917 439.662 1.00 52.81 B O
ANISOU 3662 O SER B 48 8657 4261 7145 -1697 702 -1085 B O
ATOM 3663 CB SER B 48 7.587 3.822 442.844 1.00 38.68 B C
ANISOU 3663 CB SER B 48 6521 2188 5986 -1072 457 -901 B C
ATOM 3664 OG SER B 48 7.804 5.145 442.428 1.00 38.96 B O
ANISOU 3664 OG SER B 48 6615 2308 5882 -1225 340 -760 B O
ATOM 3665 N ALA B 49 6.203 2.499 440.255 1.00 56.21 B N
ANISOU 3665 N ALA B 49 9114 4533 7711 -1555 603 -1193 B N
ATOM 3666 CA ALA B 49 5.566 2.537 438.944 1.00 49.27 B C
ANISOU 3666 CA ALA B 49 8430 3789 6503 -1845 553 -1238 B C
ATOM 3667 C ALA B 49 5.323 3.963 438.468 1.00 44.85 B C
ANISOU 3667 C ALA B 49 7952 3354 5734 -1990 308 -1001 B C
ATOM 3668 O ALA B 49 5.253 4.206 437.258 1.00 47.12 B O
ANISOU 3668 O ALA B 49 8407 3792 5705 -2253 307 -1012 B O
ATOM 3669 CB ALA B 49 4.262 1.748 438.978 1.00 44.49 B C
ANISOU 3669 CB ALA B 49 7854 3145 5906 -1838 437 -1295 B C
ATOM 3670 N ASN B 50 5.210 4.916 439.392 1.00 42.78 B N
ANISOU 3670 N ASN B 50 7589 3026 5639 -1828 111 -787 B N
ATOM 3671 CA ASN B 50 4.961 6.320 439.066 1.00 58.91 B C
ANISOU 3671 CA ASN B 50 9699 5143 7541 -1934 -115 -542 B C
ATOM 3672 C ASN B 50 6.234 7.178 438.974 1.00 50.37 B C
ANISOU 3672 C ASN B 50 8586 4107 6446 -1975 2 -480 B C
ATOM 3673 O ASN B 50 6.145 8.405 439.067 1.00 43.15 B O
ANISOU 3673 O ASN B 50 7687 3194 5513 -1997 -171 -264 B O
ATOM 3674 CB ASN B 50 4.003 6.906 440.099 1.00 40.76 B C
ANISOU 3674 CB ASN B 50 7321 2725 5443 -1750 -384 -354 B C
ATOM 3675 CG ASN B 50 4.538 6.781 441.501 1.00 38.55 B C
ANISOU 3675 CG ASN B 50 6855 2318 5473 -1471 -312 -373 B C
ATOM 3676 ND2 ASN B 50 4.068 7.638 442.398 1.00 36.91 B N
ANISOU 3676 ND2 ASN B 50 6502 2114 5410 -1283 -473 -196 B N
ATOM 3677 OD1 ASN B 50 5.349 5.892 441.784 1.00 56.20 B O
ANISOU 3677 OD1 ASN B 50 9027 4512 7814 -1395 -88 -549 B O
ATOM 3678 N SER B 51 7.412 6.566 438.793 1.00 49.75 B N
ANISOU 3678 N SER B 51 8452 4053 6397 -1986 304 -666 B N
ATOM 3679 CA SER B 51 8.662 7.321 438.874 1.00 50.71 B C
ANISOU 3679 CA SER B 51 8491 4203 6572 -2002 425 -619 B C
ATOM 3680 C SER B 51 8.801 8.341 437.744 1.00 56.66 B C
ANISOU 3680 C SER B 51 9411 5087 7029 -2270 396 -488 B C
ATOM 3681 O SER B 51 9.449 9.385 437.923 1.00 46.89 B O
ANISOU 3681 O SER B 51 8126 3849 5840 -2290 379 -354 B O
ATOM 3682 CB SER B 51 9.856 6.363 438.851 1.00 45.84 B C
ANISOU 3682 CB SER B 51 7758 3586 6075 -1956 769 -850 B C
ATOM 3683 OG SER B 51 9.894 5.510 439.972 1.00 44.16 B O
ANISOU 3683 OG SER B 51 7377 3243 6158 -1689 799 -934 B O
ATOM 3684 N ALA B 52 8.195 8.058 436.584 1.00 58.33 B N
ANISOU 3684 N ALA B 52 9825 5411 6926 -2488 386 -521 B N
ATOM 3685 CA ALA B 52 8.376 8.909 435.414 1.00 51.35 B C
ANISOU 3685 CA ALA B 52 9129 4666 5716 -2760 384 -398 B C
ATOM 3686 C ALA B 52 7.839 10.308 435.657 1.00 56.83 B C
ANISOU 3686 C ALA B 52 9850 5326 6417 -2749 84 -82 B C
ATOM 3687 O ALA B 52 8.464 11.300 435.262 1.00 72.03 B O
ANISOU 3687 O ALA B 52 11829 7289 8252 -2873 125 55 B O
ATOM 3688 CB ALA B 52 7.700 8.285 434.198 1.00 60.29 B C
ANISOU 3688 CB ALA B 52 10485 5936 6488 -2994 386 -490 B C
ATOM 3689 N GLU B 53 6.667 10.414 436.280 1.00 53.69 B N
ANISOU 3689 N GLU B 53 9419 4844 6136 -2606 -201 38 B N
ATOM 3690 CA GLU B 53 6.062 11.730 436.398 1.00 62.15 B C
ANISOU 3690 CA GLU B 53 10530 5869 7213 -2603 -474 341 B C
ATOM 3691 C GLU B 53 6.823 12.619 437.368 1.00 67.95 B C
ANISOU 3691 C GLU B 53 11124 6476 8217 -2465 -444 425 B C
ATOM 3692 O GLU B 53 6.660 13.845 437.312 1.00 68.06 B O
ANISOU 3692 O GLU B 53 11191 6446 8223 -2507 -589 664 B O
ATOM 3693 CB GLU B 53 4.593 11.626 436.800 1.00 47.44 B C
ANISOU 3693 CB GLU B 53 8648 3941 5434 -2485 -767 444 B C
ATOM 3694 CG GLU B 53 4.326 11.114 438.187 1.00 75.88 B C
ANISOU 3694 CG GLU B 53 12063 7384 9386 -2206 -783 352 B C
ATOM 3695 CD GLU B 53 2.834 10.929 438.438 1.00 85.43 B C
ANISOU 3695 CD GLU B 53 13257 8540 10661 -2122 -1040 438 B C
ATOM 3696 OE1 GLU B 53 2.277 9.891 437.986 1.00 89.58 B O
ANISOU 3696 OE1 GLU B 53 13822 9136 11079 -2188 -1033 293 B O
ATOM 3697 OE2 GLU B 53 2.226 11.831 439.071 1.00 74.59 B O1-
ANISOU 3697 OE2 GLU B 53 11831 7050 9460 -2000 -1236 643 B O1-
ATOM 3698 N TYR B 54 7.637 12.039 438.258 1.00 45.56 B N
ANISOU 3698 N TYR B 54 8111 3577 5622 -2305 -268 240 B N
ATOM 3699 CA TYR B 54 8.476 12.869 439.113 1.00 58.17 B C
ANISOU 3699 CA TYR B 54 9574 5083 7444 -2213 -237 297 B C
ATOM 3700 C TYR B 54 9.838 13.138 438.494 1.00 60.03 B C
ANISOU 3700 C TYR B 54 9803 5408 7597 -2382 17 236 B C
ATOM 3701 O TYR B 54 10.258 14.292 438.380 1.00 71.61 B O
ANISOU 3701 O TYR B 54 11296 6853 9058 -2480 -3 389 B O
ATOM 3702 CB TYR B 54 8.660 12.230 440.484 1.00 42.20 B C
ANISOU 3702 CB TYR B 54 7352 2955 5727 -1951 -219 165 B C
ATOM 3703 CG TYR B 54 7.415 12.228 441.310 1.00 40.23 B C
ANISOU 3703 CG TYR B 54 7093 2586 5608 -1774 -454 251 B C
ATOM 3704 CD1 TYR B 54 6.399 11.309 441.052 1.00 64.29 B C
ANISOU 3704 CD1 TYR B 54 10195 5647 8585 -1748 -515 192 B C
ATOM 3705 CD2 TYR B 54 7.239 13.125 442.344 1.00 38.81 B C
ANISOU 3705 CD2 TYR B 54 6753 2383 5610 -1569 -560 356 B C
ATOM 3706 CE1 TYR B 54 5.242 11.281 441.809 1.00 51.05 B C
ANISOU 3706 CE1 TYR B 54 8405 3956 7037 -1526 -674 254 B C
ATOM 3707 CE2 TYR B 54 6.081 13.110 443.112 1.00 46.20 B C
ANISOU 3707 CE2 TYR B 54 7580 3332 6641 -1341 -682 397 B C
ATOM 3708 CZ TYR B 54 5.086 12.177 442.836 1.00 46.88 B C
ANISOU 3708 CZ TYR B 54 7710 3430 6673 -1319 -736 353 B C
ATOM 3709 OH TYR B 54 3.932 12.129 443.576 1.00 46.98 B O
ANISOU 3709 OH TYR B 54 7606 3466 6778 -1117 -821 387 B O
ATOM 3710 N PHE B 55 10.518 12.095 438.042 1.00 64.10 B N
ANISOU 3710 N PHE B 55 10287 6013 8057 -2429 274 14 B N
ATOM 3711 CA PHE B 55 11.864 12.315 437.552 1.00 58.59 B C
ANISOU 3711 CA PHE B 55 9543 5387 7332 -2571 546 -59 B C
ATOM 3712 C PHE B 55 11.904 12.948 436.177 1.00 65.02 B C
ANISOU 3712 C PHE B 55 10587 6315 7804 -2866 609 51 B C
ATOM 3713 O PHE B 55 12.986 13.374 435.758 1.00 67.57 B O
ANISOU 3713 O PHE B 55 10886 6685 8103 -3008 829 33 B O
ATOM 3714 CB PHE B 55 12.640 11.000 437.554 1.00 57.66 B C
ANISOU 3714 CB PHE B 55 9294 5305 7307 -2508 833 -335 B C
ATOM 3715 CG PHE B 55 12.931 10.515 438.923 1.00 52.57 B C
ANISOU 3715 CG PHE B 55 8403 4556 7014 -2227 803 -414 B C
ATOM 3716 CD1 PHE B 55 12.134 9.547 439.518 1.00 54.56 B C
ANISOU 3716 CD1 PHE B 55 8631 4739 7360 -2037 712 -490 B C
ATOM 3717 CD2 PHE B 55 13.964 11.078 439.648 1.00 47.58 B C
ANISOU 3717 CD2 PHE B 55 7568 3898 6614 -2162 844 -397 B C
ATOM 3718 CE1 PHE B 55 12.387 9.129 440.804 1.00 44.23 B C
ANISOU 3718 CE1 PHE B 55 7117 3336 6353 -1778 674 -535 B C
ATOM 3719 CE2 PHE B 55 14.217 10.677 440.928 1.00 45.83 B C
ANISOU 3719 CE2 PHE B 55 7130 3598 6684 -1912 782 -448 B C
ATOM 3720 CZ PHE B 55 13.427 9.708 441.514 1.00 48.64 B C
ANISOU 3720 CZ PHE B 55 7482 3885 7113 -1715 697 -508 B C
ATOM 3721 N SER B 56 10.771 13.050 435.474 1.00 52.99 B N
ANISOU 3721 N SER B 56 9279 4839 6015 -2968 418 178 B N
ATOM 3722 CA SER B 56 10.793 13.798 434.222 1.00 68.81 B C
ANISOU 3722 CA SER B 56 11517 6953 7677 -3247 439 335 B C
ATOM 3723 C SER B 56 11.241 15.240 434.438 1.00 83.25 B C
ANISOU 3723 C SER B 56 13331 8701 9599 -3290 387 564 B C
ATOM 3724 O SER B 56 11.774 15.865 433.512 1.00 82.89 B O
ANISOU 3724 O SER B 56 13429 8730 9335 -3522 522 659 B O
ATOM 3725 CB SER B 56 9.420 13.771 433.543 1.00 63.02 B C
ANISOU 3725 CB SER B 56 10995 6285 6665 -3330 171 478 B C
ATOM 3726 OG SER B 56 8.494 14.644 434.159 1.00 55.15 B O
ANISOU 3726 OG SER B 56 9976 5170 5808 -3200 -158 733 B O
ATOM 3727 N VAL B 57 11.062 15.766 435.656 1.00 86.55 B N
ANISOU 3727 N VAL B 57 13586 8961 10337 -3079 215 643 B N
ATOM 3728 CA VAL B 57 11.463 17.136 435.949 1.00 66.68 B C
ANISOU 3728 CA VAL B 57 11052 6340 7941 -3119 170 838 B C
ATOM 3729 C VAL B 57 12.979 17.220 436.045 1.00 71.25 B C
ANISOU 3729 C VAL B 57 11483 6943 8646 -3194 468 694 B C
ATOM 3730 O VAL B 57 13.589 18.217 435.641 1.00 68.85 B O
ANISOU 3730 O VAL B 57 11235 6624 8303 -3365 560 820 B O
ATOM 3731 CB VAL B 57 10.774 17.620 437.237 1.00 62.14 B C
ANISOU 3731 CB VAL B 57 10363 5586 7662 -2882 -87 933 B C
ATOM 3732 CG1 VAL B 57 10.996 19.108 437.420 1.00 57.92 B C
ANISOU 3732 CG1 VAL B 57 9813 4967 7229 -2893 -145 1130 B C
ATOM 3733 CG2 VAL B 57 9.300 17.264 437.203 1.00 50.37 B C
ANISOU 3733 CG2 VAL B 57 8964 4082 6094 -2783 -345 1023 B C
ATOM 3734 N ALA B 58 13.607 16.180 436.599 1.00 64.28 B N
ANISOU 3734 N ALA B 58 10395 6089 7938 -3063 625 436 B N
ATOM 3735 CA ALA B 58 15.062 16.104 436.595 1.00 62.95 B C
ANISOU 3735 CA ALA B 58 10054 5966 7898 -3134 922 285 B C
ATOM 3736 C ALA B 58 15.626 15.786 435.209 1.00 62.26 B C
ANISOU 3736 C ALA B 58 10109 6024 7524 -3387 1223 210 B C
ATOM 3737 O ALA B 58 16.697 16.290 434.848 1.00 64.63 B O
ANISOU 3737 O ALA B 58 10356 6353 7847 -3546 1456 199 B O
ATOM 3738 CB ALA B 58 15.518 15.047 437.599 1.00 53.44 B C
ANISOU 3738 CB ALA B 58 8581 4746 6980 -2897 984 57 B C
ATOM 3739 N ASP B 59 14.897 15.024 434.390 1.00 59.10 B N
ANISOU 3739 N ASP B 59 9905 5714 6836 -3451 1226 163 B N
ATOM 3740 CA ASP B 59 15.490 14.428 433.193 1.00 73.17 B C
ANISOU 3740 CA ASP B 59 11805 7636 8358 -3668 1557 12 B C
ATOM 3741 C ASP B 59 14.433 14.437 432.090 1.00 63.65 B C
ANISOU 3741 C ASP B 59 10937 6529 6717 -3848 1427 133 B C
ATOM 3742 O ASP B 59 13.537 13.593 432.079 1.00 75.95 B O
ANISOU 3742 O ASP B 59 12558 8112 8189 -3769 1295 53 B O
ATOM 3743 CB ASP B 59 15.991 13.019 433.499 1.00 80.84 B C
ANISOU 3743 CB ASP B 59 12591 8624 9503 -3526 1784 -298 B C
ATOM 3744 CG ASP B 59 16.975 12.488 432.454 1.00 90.38 B C
ANISOU 3744 CG ASP B 59 13842 9941 10557 -3731 2219 -494 B C
ATOM 3745 OD1 ASP B 59 16.902 12.925 431.281 1.00 97.39 B O
ANISOU 3745 OD1 ASP B 59 14999 10930 11075 -4007 2312 -412 B O
ATOM 3746 OD2 ASP B 59 17.813 11.621 432.804 1.00 82.57 B O1-
ANISOU 3746 OD2 ASP B 59 12620 8934 9818 -3614 2473 -726 B O1-
ATOM 3747 N ASN B 60 14.540 15.394 431.171 1.00 66.24 B N
ANISOU 3747 N ASN B 60 11482 6916 6772 -4096 1456 332 B N
ATOM 3748 CA ASN B 60 13.493 15.525 430.159 1.00 67.98 B C
ANISOU 3748 CA ASN B 60 12023 7240 6566 -4266 1272 497 B C
ATOM 3749 C ASN B 60 13.517 14.416 429.155 1.00 83.89 B C
ANISOU 3749 C ASN B 60 14203 9418 8254 -4434 1492 267 B C
ATOM 3750 O ASN B 60 12.784 14.467 428.155 1.00 89.25 B O
ANISOU 3750 O ASN B 60 15171 10225 8515 -4630 1374 378 B O
ATOM 3751 CB ASN B 60 13.605 16.865 429.427 1.00 72.96 B C
ANISOU 3751 CB ASN B 60 12860 7885 6977 -4487 1242 804 B C
ATOM 3752 CG ASN B 60 15.006 17.138 428.890 1.00 78.40 B C
ANISOU 3752 CG ASN B 60 13542 8616 7632 -4689 1657 719 B C
ATOM 3753 ND2 ASN B 60 15.071 17.740 427.714 1.00 77.51 B N
ANISOU 3753 ND2 ASN B 60 13719 8601 7130 -4974 1745 892 B N
ATOM 3754 OD1 ASN B 60 16.011 16.846 429.538 1.00 83.73 B O
ANISOU 3754 OD1 ASN B 60 13946 9234 8634 -4590 1889 517 B O
ATOM 3755 N THR B 61 14.377 13.428 429.373 1.00 88.63 B N
ANISOU 3755 N THR B 61 14628 10017 9030 -4371 1819 -50 B N
ATOM 3756 CA THR B 61 14.383 12.220 428.562 1.00 96.79 B C
ANISOU 3756 CA THR B 61 15795 11167 9815 -4497 2058 -324 B C
ATOM 3757 C THR B 61 13.501 11.123 429.140 1.00 80.58 B C
ANISOU 3757 C THR B 61 13664 9069 7884 -4294 1888 -480 B C
ATOM 3758 O THR B 61 13.172 10.172 428.424 1.00 71.41 B O
ANISOU 3758 O THR B 61 12664 8000 6470 -4418 2000 -678 B O
ATOM 3759 CB THR B 61 15.819 11.715 428.387 1.00 73.83 B C
ANISOU 3759 CB THR B 61 12742 8263 7045 -4547 2554 -588 B C
ATOM 3760 CG2 THR B 61 16.634 12.712 427.603 1.00 76.85 B C
ANISOU 3760 CG2 THR B 61 13248 8711 7242 -4805 2767 -453 B C
ATOM 3761 OG1 THR B 61 16.421 11.513 429.669 1.00 71.05 B O
ANISOU 3761 OG1 THR B 61 12015 7769 7211 -4255 2578 -673 B O
ATOM 3762 N ILE B 62 13.121 11.241 430.409 1.00 69.93 B N
ANISOU 3762 N ILE B 62 12085 7577 6908 -4003 1635 -403 B N
ATOM 3763 CA ILE B 62 12.222 10.297 431.066 1.00 70.29 B C
ANISOU 3763 CA ILE B 62 12050 7558 7098 -3798 1456 -515 B C
ATOM 3764 C ILE B 62 10.792 10.537 430.586 1.00 76.18 B C
ANISOU 3764 C ILE B 62 13020 8374 7549 -3892 1093 -333 B C
ATOM 3765 O ILE B 62 10.170 11.541 430.944 1.00 69.03 B O
ANISOU 3765 O ILE B 62 12117 7420 6690 -3831 775 -46 B O
ATOM 3766 CB ILE B 62 12.309 10.426 432.590 1.00 60.14 B C
ANISOU 3766 CB ILE B 62 10463 6103 6286 -3470 1314 -473 B C
ATOM 3767 CG1 ILE B 62 13.758 10.285 433.072 1.00 60.23 B C
ANISOU 3767 CG1 ILE B 62 10226 6063 6593 -3384 1631 -620 B C
ATOM 3768 CG2 ILE B 62 11.411 9.419 433.241 1.00 57.99 B C
ANISOU 3768 CG2 ILE B 62 10122 5758 6153 -3271 1168 -587 B C
ATOM 3769 CD1 ILE B 62 14.475 9.063 432.570 1.00 62.12 B C
ANISOU 3769 CD1 ILE B 62 10438 6343 6823 -3430 2024 -932 B C
ATOM 3770 N HIS B 63 10.239 9.589 429.823 1.00 80.76 B N
ANISOU 3770 N HIS B 63 13772 9059 7854 -4033 1132 -507 B N
ATOM 3771 CA HIS B 63 8.837 9.656 429.419 1.00 78.65 B C
ANISOU 3771 CA HIS B 63 13676 8871 7337 -4113 766 -362 B C
ATOM 3772 C HIS B 63 8.004 8.547 430.058 1.00 71.99 B C
ANISOU 3772 C HIS B 63 12721 7951 6682 -3938 657 -538 B C
ATOM 3773 O HIS B 63 7.086 8.836 430.834 1.00 68.52 B O
ANISOU 3773 O HIS B 63 12172 7423 6439 -3755 331 -372 B O
ATOM 3774 CB HIS B 63 8.688 9.597 427.896 1.00 70.34 B C
ANISOU 3774 CB HIS B 63 12957 8035 5735 -4477 827 -379 B C
ATOM 3775 CG HIS B 63 9.113 10.842 427.172 1.00 83.47 B C
ANISOU 3775 CG HIS B 63 14790 9785 7140 -4673 824 -110 B C
ATOM 3776 CD2 HIS B 63 8.386 11.855 426.641 1.00 82.81 B C
ANISOU 3776 CD2 HIS B 63 14884 9784 6795 -4796 499 236 B C
ATOM 3777 ND1 HIS B 63 10.432 11.130 426.883 1.00 84.02 B N
ANISOU 3777 ND1 HIS B 63 14860 9858 7206 -4771 1201 -179 B N
ATOM 3778 CE1 HIS B 63 10.498 12.264 426.207 1.00 83.17 B C
ANISOU 3778 CE1 HIS B 63 14939 9827 6835 -4957 1120 108 B C
ATOM 3779 NE2 HIS B 63 9.270 12.725 426.047 1.00 83.34 B N
ANISOU 3779 NE2 HIS B 63 15076 9895 6693 -4969 691 372 B N
ATOM 3780 N GLU B 64 8.296 7.276 429.765 1.00 65.18 B N
ANISOU 3780 N GLU B 64 11880 7103 5783 -3990 943 -875 B N
ATOM 3781 CA GLU B 64 7.659 6.164 430.456 1.00 76.57 B C
ANISOU 3781 CA GLU B 64 13199 8437 7459 -3811 901 -1061 B C
ATOM 3782 C GLU B 64 8.571 5.671 431.579 1.00 70.67 B C
ANISOU 3782 C GLU B 64 12174 7507 7171 -3523 1145 -1203 B C
ATOM 3783 O GLU B 64 9.707 6.128 431.740 1.00 61.01 B O
ANISOU 3783 O GLU B 64 10850 6261 6070 -3486 1350 -1185 B O
ATOM 3784 CB GLU B 64 7.331 5.004 429.501 1.00 80.88 B C
ANISOU 3784 CB GLU B 64 13940 9081 7710 -4038 1058 -1352 B C
ATOM 3785 CG GLU B 64 6.599 5.364 428.221 1.00 87.11 B C
ANISOU 3785 CG GLU B 64 15031 10093 7972 -4376 860 -1255 B C
ATOM 3786 CD GLU B 64 7.541 5.433 427.026 1.00112.85 B C
ANISOU 3786 CD GLU B 64 18522 13502 10855 -4674 1195 -1372 B C
ATOM 3787 OE1 GLU B 64 8.458 4.588 426.954 1.00118.04 B O
ANISOU 3787 OE1 GLU B 64 19144 14097 11607 -4674 1626 -1680 B O
ATOM 3788 OE2 GLU B 64 7.384 6.334 426.170 1.00125.74 B O1-
ANISOU 3788 OE2 GLU B 64 20367 15302 12106 -4901 1043 -1149 B O1-
ATOM 3789 N LEU B 65 8.082 4.664 432.315 1.00 64.03 B N
ANISOU 3789 N LEU B 65 11211 6538 6578 -3333 1133 -1354 B N
ATOM 3790 CA LEU B 65 8.889 4.027 433.352 1.00 60.11 B C
ANISOU 3790 CA LEU B 65 10465 5873 6502 -3057 1358 -1491 B C
ATOM 3791 C LEU B 65 10.133 3.377 432.774 1.00 68.37 B C
ANISOU 3791 C LEU B 65 11510 6933 7533 -3145 1817 -1747 B C
ATOM 3792 O LEU B 65 11.201 3.405 433.392 1.00 77.25 B O
ANISOU 3792 O LEU B 65 12423 7978 8952 -2974 2010 -1769 B O
ATOM 3793 CB LEU B 65 8.063 2.961 434.068 1.00 63.41 B C
ANISOU 3793 CB LEU B 65 10803 6156 7134 -2877 1290 -1612 B C
ATOM 3794 CG LEU B 65 8.712 2.305 435.285 1.00 60.52 B C
ANISOU 3794 CG LEU B 65 10181 5602 7212 -2557 1455 -1698 B C
ATOM 3795 CD1 LEU B 65 9.077 3.357 436.344 1.00 59.90 B C
ANISOU 3795 CD1 LEU B 65 9916 5474 7369 -2349 1271 -1450 B C
ATOM 3796 CD2 LEU B 65 7.840 1.185 435.839 1.00 52.64 B C
ANISOU 3796 CD2 LEU B 65 9151 4468 6383 -2420 1418 -1822 B C
ATOM 3797 N SER B 66 10.015 2.792 431.584 1.00 70.07 B N
ANISOU 3797 N SER B 66 11957 7254 7412 -3417 2001 -1946 B N
ATOM 3798 CA SER B 66 11.130 2.055 431.011 1.00 65.55 B C
ANISOU 3798 CA SER B 66 11393 6673 6840 -3502 2482 -2226 B C
ATOM 3799 C SER B 66 12.331 2.953 430.733 1.00 83.45 B C
ANISOU 3799 C SER B 66 13609 9009 9088 -3571 2666 -2133 B C
ATOM 3800 O SER B 66 13.466 2.466 430.715 1.00100.65 B O
ANISOU 3800 O SER B 66 15657 11130 11457 -3520 3058 -2317 B O
ATOM 3801 CB SER B 66 10.648 1.332 429.757 1.00 82.96 B C
ANISOU 3801 CB SER B 66 13898 8987 8637 -3817 2620 -2461 B C
ATOM 3802 OG SER B 66 9.756 2.157 429.024 1.00 87.77 B O
ANISOU 3802 OG SER B 66 14744 9782 8822 -4060 2284 -2262 B O
ATOM 3803 N ASP B 67 12.113 4.262 430.529 1.00 82.03 B N
ANISOU 3803 N ASP B 67 13515 8940 8714 -3679 2400 -1844 B N
ATOM 3804 CA ASP B 67 13.231 5.171 430.267 1.00 67.61 B C
ANISOU 3804 CA ASP B 67 11643 7169 6877 -3763 2576 -1746 B C
ATOM 3805 C ASP B 67 14.185 5.270 431.452 1.00 77.39 B C
ANISOU 3805 C ASP B 67 12525 8269 8612 -3469 2663 -1724 B C
ATOM 3806 O ASP B 67 15.372 5.552 431.265 1.00 80.67 B O
ANISOU 3806 O ASP B 67 12833 8702 9117 -3514 2949 -1766 B O
ATOM 3807 CB ASP B 67 12.716 6.568 429.906 1.00 67.64 B C
ANISOU 3807 CB ASP B 67 11809 7284 6608 -3916 2250 -1414 B C
ATOM 3808 CG ASP B 67 11.850 6.577 428.656 1.00 97.15 B C
ANISOU 3808 CG ASP B 67 15902 11192 9818 -4230 2139 -1396 B C
ATOM 3809 OD1 ASP B 67 12.145 5.833 427.686 1.00 93.82 B O
ANISOU 3809 OD1 ASP B 67 15660 10857 9131 -4449 2450 -1648 B O
ATOM 3810 OD2 ASP B 67 10.853 7.326 428.654 1.00 99.31 B O1-
ANISOU 3810 OD2 ASP B 67 16274 11514 9944 -4257 1735 -1129 B O1-
ATOM 3811 N ILE B 68 13.694 5.046 432.671 1.00 62.19 B N
ANISOU 3811 N ILE B 68 10410 6213 7006 -3176 2421 -1658 B N
ATOM 3812 CA ILE B 68 14.557 5.099 433.853 1.00 65.35 B C
ANISOU 3812 CA ILE B 68 10477 6497 7855 -2897 2465 -1632 B C
ATOM 3813 C ILE B 68 15.693 4.082 433.768 1.00 70.24 B C
ANISOU 3813 C ILE B 68 10929 7061 8696 -2828 2908 -1898 B C
ATOM 3814 O ILE B 68 16.808 4.323 434.261 1.00 62.41 B O
ANISOU 3814 O ILE B 68 9681 6041 7991 -2713 3050 -1887 B O
ATOM 3815 CB ILE B 68 13.698 4.932 435.130 1.00 56.81 B C
ANISOU 3815 CB ILE B 68 9272 5291 7021 -2614 2132 -1526 B C
ATOM 3816 CG1 ILE B 68 12.795 6.156 435.297 1.00 55.17 B C
ANISOU 3816 CG1 ILE B 68 9173 5120 6666 -2662 1729 -1239 B C
ATOM 3817 CG2 ILE B 68 14.543 4.704 436.364 1.00 55.29 B C
ANISOU 3817 CG2 ILE B 68 8753 4984 7271 -2318 2187 -1535 B C
ATOM 3818 CD1 ILE B 68 11.494 5.862 435.855 1.00 52.98 B C
ANISOU 3818 CD1 ILE B 68 8938 4774 6419 -2535 1434 -1176 B C
ATOM 3819 N LYS B 69 15.440 2.936 433.146 1.00 74.89 B N
ANISOU 3819 N LYS B 69 11650 7629 9177 -2900 3136 -2145 B N
ATOM 3820 CA LYS B 69 16.494 1.941 433.002 1.00 75.35 B C
ANISOU 3820 CA LYS B 69 11557 7610 9462 -2833 3591 -2406 B C
ATOM 3821 C LYS B 69 17.662 2.490 432.200 1.00 80.79 B C
ANISOU 3821 C LYS B 69 12233 8401 10064 -3031 3914 -2447 B C
ATOM 3822 O LYS B 69 18.822 2.153 432.463 1.00 75.46 B O
ANISOU 3822 O LYS B 69 11293 7662 9715 -2905 4217 -2552 B O
ATOM 3823 CB LYS B 69 15.935 0.677 432.354 1.00 67.88 B C
ANISOU 3823 CB LYS B 69 10804 6614 8372 -2922 3795 -2679 B C
ATOM 3824 CG LYS B 69 16.906 -0.465 432.372 1.00 69.97 B C
ANISOU 3824 CG LYS B 69 10894 6744 8946 -2795 4259 -2946 B C
ATOM 3825 CD LYS B 69 16.279 -1.725 431.829 1.00 81.21 B C
ANISOU 3825 CD LYS B 69 12515 8085 10255 -2875 4452 -3224 B C
ATOM 3826 CE LYS B 69 17.295 -2.849 431.802 1.00 93.49 B C
ANISOU 3826 CE LYS B 69 13897 9478 12146 -2744 4958 -3493 B C
ATOM 3827 NZ LYS B 69 16.643 -4.182 431.765 1.00 97.37 B N1+
ANISOU 3827 NZ LYS B 69 14432 9862 12702 -2682 5012 -3625 B N1+
ATOM 3828 N GLN B 70 17.369 3.315 431.202 1.00 70.60 B N
ANISOU 3828 N GLN B 70 11221 7266 8338 -3343 3860 -2359 B N
ATOM 3829 CA GLN B 70 18.377 3.938 430.368 1.00 73.59 B C
ANISOU 3829 CA GLN B 70 11634 7748 8579 -3570 4159 -2373 B C
ATOM 3830 C GLN B 70 19.027 5.145 431.021 1.00 72.25 B C
ANISOU 3830 C GLN B 70 11243 7591 8618 -3495 4007 -2128 B C
ATOM 3831 O GLN B 70 20.071 5.599 430.546 1.00 88.24 B O
ANISOU 3831 O GLN B 70 13202 9670 10655 -3633 4294 -2150 B O
ATOM 3832 CB GLN B 70 17.717 4.314 429.049 1.00 85.07 B C
ANISOU 3832 CB GLN B 70 13507 9364 9452 -3940 4138 -2355 B C
ATOM 3833 CG GLN B 70 16.399 3.553 428.863 1.00 93.61 B C
ANISOU 3833 CG GLN B 70 14812 10444 10311 -3968 3931 -2438 B C
ATOM 3834 CD GLN B 70 16.577 2.096 428.424 1.00 87.95 B C
ANISOU 3834 CD GLN B 70 14143 9654 9619 -3991 4327 -2813 B C
ATOM 3835 NE2 GLN B 70 15.474 1.469 428.003 1.00 86.48 B N
ANISOU 3835 NE2 GLN B 70 14203 9495 9161 -4107 4194 -2919 B N
ATOM 3836 OE1 GLN B 70 17.668 1.528 428.519 1.00 78.98 B O
ANISOU 3836 OE1 GLN B 70 12806 8426 8777 -3893 4738 -3003 B O
ATOM 3837 N ALA B 71 18.461 5.657 432.104 1.00 79.46 B N
ANISOU 3837 N ALA B 71 12037 8448 9705 -3289 3587 -1912 B N
ATOM 3838 CA ALA B 71 18.962 6.882 432.704 1.00 86.04 B C
ANISOU 3838 CA ALA B 71 12701 9291 10698 -3252 3414 -1683 B C
ATOM 3839 C ALA B 71 20.127 6.594 433.651 1.00 83.10 B C
ANISOU 3839 C ALA B 71 11915 8838 10821 -3010 3565 -1755 B C
ATOM 3840 O ALA B 71 20.364 5.458 434.080 1.00 79.73 B O
ANISOU 3840 O ALA B 71 11316 8322 10654 -2803 3715 -1929 B O
ATOM 3841 CB ALA B 71 17.850 7.633 433.443 1.00 84.09 B C
ANISOU 3841 CB ALA B 71 12520 9014 10416 -3153 2912 -1427 B C
ATOM 3842 N ASN B 72 20.844 7.665 433.979 1.00 75.67 B N
ANISOU 3842 N ASN B 72 10814 7925 10013 -3044 3510 -1605 B N
ATOM 3843 CA ASN B 72 21.936 7.694 434.938 1.00 75.17 B C
ANISOU 3843 CA ASN B 72 10343 7816 10402 -2846 3563 -1617 B C
ATOM 3844 C ASN B 72 21.482 8.421 436.200 1.00 76.29 B C
ANISOU 3844 C ASN B 72 10375 7908 10702 -2667 3113 -1406 B C
ATOM 3845 O ASN B 72 20.660 9.336 436.134 1.00 83.77 B O
ANISOU 3845 O ASN B 72 11542 8868 11419 -2774 2835 -1221 B O
ATOM 3846 CB ASN B 72 23.140 8.408 434.316 1.00 75.60 B C
ANISOU 3846 CB ASN B 72 10293 7946 10485 -3062 3861 -1628 B C
ATOM 3847 CG ASN B 72 24.334 8.452 435.234 1.00 86.26 B C
ANISOU 3847 CG ASN B 72 11193 9272 12312 -2885 3917 -1647 B C
ATOM 3848 ND2 ASN B 72 25.153 9.488 435.085 1.00 88.03 B N
ANISOU 3848 ND2 ASN B 72 11304 9550 12592 -3056 3991 -1565 B N
ATOM 3849 OD1 ASN B 72 24.524 7.570 436.067 1.00 97.18 B O
ANISOU 3849 OD1 ASN B 72 12327 10586 14011 -2603 3891 -1726 B O
ATOM 3850 N ILE B 73 21.982 7.996 437.366 1.00 62.63 B N
ANISOU 3850 N ILE B 73 8316 6117 9365 -2391 3037 -1430 B N
ATOM 3851 CA ILE B 73 21.460 8.595 438.594 1.00 59.55 B C
ANISOU 3851 CA ILE B 73 7860 5678 9089 -2224 2616 -1252 B C
ATOM 3852 C ILE B 73 21.919 10.041 438.749 1.00 79.13 B C
ANISOU 3852 C ILE B 73 10288 8200 11578 -2378 2492 -1097 B C
ATOM 3853 O ILE B 73 21.207 10.866 439.341 1.00 68.80 B O
ANISOU 3853 O ILE B 73 9080 6853 10210 -2359 2159 -929 B O
ATOM 3854 CB ILE B 73 21.831 7.767 439.839 1.00 63.30 B C
ANISOU 3854 CB ILE B 73 8022 6087 9942 -1894 2539 -1300 B C
ATOM 3855 CG1 ILE B 73 23.335 7.796 440.085 1.00 65.08 B C
ANISOU 3855 CG1 ILE B 73 7870 6359 10499 -1860 2737 -1361 B C
ATOM 3856 CG2 ILE B 73 21.335 6.351 439.705 1.00 77.43 B C
ANISOU 3856 CG2 ILE B 73 9877 7804 11739 -1742 2671 -1443 B C
ATOM 3857 CD1 ILE B 73 23.789 6.794 441.133 1.00 69.32 B C
ANISOU 3857 CD1 ILE B 73 8093 6842 11405 -1532 2710 -1411 B C
ATOM 3858 N ASN B 74 23.083 10.395 438.198 1.00 76.42 B N
ANISOU 3858 N ASN B 74 9798 7922 11315 -2544 2775 -1153 B N
ATOM 3859 CA ASN B 74 23.504 11.788 438.265 1.00 70.61 B C
ANISOU 3859 CA ASN B 74 9034 7212 10583 -2722 2683 -1012 B C
ATOM 3860 C ASN B 74 22.560 12.677 437.477 1.00 67.29 B C
ANISOU 3860 C ASN B 74 9005 6790 9773 -2948 2572 -854 B C
ATOM 3861 O ASN B 74 22.437 13.870 437.772 1.00 87.72 B O
ANISOU 3861 O ASN B 74 11638 9345 12345 -3039 2373 -686 B O
ATOM 3862 CB ASN B 74 24.933 11.933 437.750 1.00 82.56 B C
ANISOU 3862 CB ASN B 74 10309 8794 12265 -2873 3046 -1112 B C
ATOM 3863 CG ASN B 74 25.929 11.128 438.564 1.00 93.74 B C
ANISOU 3863 CG ASN B 74 11291 10216 14110 -2639 3133 -1240 B C
ATOM 3864 ND2 ASN B 74 27.216 11.423 438.378 1.00106.78 B N
ANISOU 3864 ND2 ASN B 74 12656 11925 15990 -2747 3380 -1301 B N
ATOM 3865 OD1 ASN B 74 25.550 10.252 439.352 1.00 82.56 B O
ANISOU 3865 OD1 ASN B 74 9789 8752 12829 -2363 2980 -1272 B O
ATOM 3866 N SER B 75 21.877 12.111 436.485 1.00 63.44 B N
ANISOU 3866 N SER B 75 8801 6331 8974 -3041 2689 -901 B N
ATOM 3867 CA SER B 75 20.864 12.853 435.757 1.00 63.24 B C
ANISOU 3867 CA SER B 75 9146 6315 8568 -3230 2535 -729 B C
ATOM 3868 C SER B 75 19.604 13.044 436.584 1.00 72.41 B C
ANISOU 3868 C SER B 75 10405 7392 9715 -3054 2114 -586 B C
ATOM 3869 O SER B 75 18.822 13.954 436.292 1.00 89.34 B O
ANISOU 3869 O SER B 75 12783 9515 11646 -3171 1912 -387 B O
ATOM 3870 CB SER B 75 20.523 12.143 434.451 1.00 71.96 B C
ANISOU 3870 CB SER B 75 10520 7498 9324 -3397 2772 -836 B C
ATOM 3871 OG SER B 75 21.692 11.931 433.672 1.00 99.05 B O
ANISOU 3871 OG SER B 75 13869 10998 12768 -3561 3205 -986 B O
ATOM 3872 N LEU B 76 19.386 12.202 437.599 1.00 71.52 B N
ANISOU 3872 N LEU B 76 10119 7223 9833 -2775 1991 -674 B N
ATOM 3873 CA LEU B 76 18.144 12.200 438.364 1.00 54.68 B C
ANISOU 3873 CA LEU B 76 8081 5006 7688 -2601 1637 -567 B C
ATOM 3874 C LEU B 76 18.268 12.832 439.743 1.00 62.05 B C
ANISOU 3874 C LEU B 76 8822 5859 8896 -2432 1387 -477 B C
ATOM 3875 O LEU B 76 17.331 13.501 440.192 1.00 50.87 B O
ANISOU 3875 O LEU B 76 7534 4367 7427 -2393 1104 -321 B O
ATOM 3876 CB LEU B 76 17.634 10.763 438.528 1.00 61.29 B C
ANISOU 3876 CB LEU B 76 8911 5823 8553 -2416 1672 -723 B C
ATOM 3877 CG LEU B 76 17.655 9.868 437.284 1.00 61.17 B C
ANISOU 3877 CG LEU B 76 9049 5880 8313 -2563 1969 -887 B C
ATOM 3878 CD1 LEU B 76 17.529 8.413 437.674 1.00 64.75 B C
ANISOU 3878 CD1 LEU B 76 9401 6279 8923 -2349 2066 -1075 B C
ATOM 3879 CD2 LEU B 76 16.545 10.242 436.305 1.00 56.34 B C
ANISOU 3879 CD2 LEU B 76 8790 5318 7300 -2767 1846 -778 B C
ATOM 3880 N LEU B 77 19.372 12.692 440.378 1.00 73.82 B N
ANISOU 3880 N LEU B 77 10019 7365 10665 -2347 1482 -566 B N
ATOM 3881 CA LEU B 77 19.575 13.121 441.753 1.00 63.15 B C
ANISOU 3881 CA LEU B 77 8469 5958 9567 -2183 1249 -515 B C
ATOM 3882 C LEU B 77 20.303 14.457 441.833 1.00 52.94 B C
ANISOU 3882 C LEU B 77 7103 4670 8343 -2363 1231 -430 B C
ATOM 3883 O LEU B 77 21.116 14.786 440.967 1.00 55.45 B O
ANISOU 3883 O LEU B 77 7394 5051 8623 -2573 1477 -457 B O
ATOM 3884 CB LEU B 77 20.379 12.072 442.519 1.00 51.87 B C
ANISOU 3884 CB LEU B 77 6729 4555 8426 -1961 1329 -659 B C
ATOM 3885 CG LEU B 77 19.657 10.749 442.692 1.00 50.52 B C
ANISOU 3885 CG LEU B 77 6610 4341 8244 -1749 1327 -737 B C
ATOM 3886 CD1 LEU B 77 20.174 10.059 443.926 1.00 52.42 B C
ANISOU 3886 CD1 LEU B 77 6567 4565 8787 -1479 1250 -785 B C
ATOM 3887 CD2 LEU B 77 18.146 10.966 442.812 1.00 48.12 B C
ANISOU 3887 CD2 LEU B 77 6588 3958 7738 -1721 1077 -624 B C
ATOM 3888 N PRO B 78 20.008 15.250 442.853 1.00 51.41 B N
ANISOU 3888 N PRO B 78 6888 4399 8248 -2298 960 -334 B N
ATOM 3889 CA PRO B 78 20.780 16.475 443.084 1.00 52.74 B C
ANISOU 3889 CA PRO B 78 6955 4555 8528 -2463 943 -281 B C
ATOM 3890 C PRO B 78 22.192 16.133 443.534 1.00 54.43 B C
ANISOU 3890 C PRO B 78 6800 4863 9018 -2433 1069 -418 B C
ATOM 3891 O PRO B 78 22.450 15.058 444.067 1.00 54.00 B O
ANISOU 3891 O PRO B 78 6556 4853 9110 -2221 1075 -521 B O
ATOM 3892 CB PRO B 78 20.000 17.188 444.198 1.00 50.57 B C
ANISOU 3892 CB PRO B 78 6756 4161 8297 -2362 619 -181 B C
ATOM 3893 CG PRO B 78 18.638 16.560 444.195 1.00 50.67 B C
ANISOU 3893 CG PRO B 78 6980 4116 8155 -2202 490 -133 B C
ATOM 3894 CD PRO B 78 18.865 15.133 443.770 1.00 48.61 B C
ANISOU 3894 CD PRO B 78 6637 3948 7886 -2098 673 -269 B C
ATOM 3895 N GLU B 79 23.125 17.062 443.297 1.00 63.66 B N
ANISOU 3895 N GLU B 79 7857 6057 10276 -2651 1177 -410 B N
ATOM 3896 CA GLU B 79 24.511 16.847 443.720 1.00 58.65 B C
ANISOU 3896 CA GLU B 79 6833 5520 9933 -2645 1284 -532 B C
ATOM 3897 C GLU B 79 24.614 16.600 445.224 1.00 58.03 B C
ANISOU 3897 C GLU B 79 6538 5447 10062 -2418 999 -563 B C
ATOM 3898 O GLU B 79 25.324 15.687 445.675 1.00 59.80 B O
ANISOU 3898 O GLU B 79 6469 5759 10494 -2252 1036 -660 B O
ATOM 3899 CB GLU B 79 25.371 18.051 443.333 1.00 80.67 B C
ANISOU 3899 CB GLU B 79 9550 8314 12787 -2937 1406 -505 B C
ATOM 3900 CG GLU B 79 25.947 18.042 441.912 1.00 93.91 B C
ANISOU 3900 CG GLU B 79 11270 10045 14366 -3163 1790 -531 B C
ATOM 3901 CD GLU B 79 26.748 19.319 441.584 1.00103.19 B C
ANISOU 3901 CD GLU B 79 12390 11203 15613 -3466 1910 -486 B C
ATOM 3902 OE1 GLU B 79 26.473 20.396 442.176 1.00 98.12 B O
ANISOU 3902 OE1 GLU B 79 11825 10463 14991 -3541 1690 -393 B O
ATOM 3903 OE2 GLU B 79 27.654 19.241 440.728 1.00109.66 B O1-
ANISOU 3903 OE2 GLU B 79 13094 12095 16477 -3635 2246 -552 B O1-
ATOM 3904 N HIS B 80 23.932 17.425 446.024 1.00 67.63 B N
ANISOU 3904 N HIS B 80 7897 6570 11230 -2412 719 -478 B N
ATOM 3905 CA HIS B 80 24.077 17.303 447.470 1.00 66.68 B C
ANISOU 3905 CA HIS B 80 7596 6466 11273 -2235 451 -512 B C
ATOM 3906 C HIS B 80 23.548 15.963 447.969 1.00 56.37 B C
ANISOU 3906 C HIS B 80 6277 5176 9967 -1928 375 -537 B C
ATOM 3907 O HIS B 80 24.121 15.371 448.887 1.00 53.37 B O
ANISOU 3907 O HIS B 80 5639 4872 9768 -1758 267 -589 B O
ATOM 3908 CB HIS B 80 23.396 18.467 448.191 1.00 66.89 B C
ANISOU 3908 CB HIS B 80 7814 6370 11232 -2303 203 -434 B C
ATOM 3909 CG HIS B 80 23.825 18.612 449.621 1.00 81.55 B C
ANISOU 3909 CG HIS B 80 9472 8267 13247 -2214 -46 -490 B C
ATOM 3910 CD2 HIS B 80 24.489 19.607 450.259 1.00 89.33 B C
ANISOU 3910 CD2 HIS B 80 10331 9259 14350 -2377 -160 -528 B C
ATOM 3911 ND1 HIS B 80 23.593 17.637 450.572 1.00 82.02 B N
ANISOU 3911 ND1 HIS B 80 9449 8371 13343 -1941 -210 -515 B N
ATOM 3912 CE1 HIS B 80 24.090 18.029 451.733 1.00 82.21 B C
ANISOU 3912 CE1 HIS B 80 9314 8444 13477 -1938 -428 -558 B C
ATOM 3913 NE2 HIS B 80 24.636 19.222 451.571 1.00 85.34 B N
ANISOU 3913 NE2 HIS B 80 9679 8821 13927 -2206 -405 -578 B N
ATOM 3914 N LEU B 81 22.458 15.467 447.381 1.00 51.20 B N
ANISOU 3914 N LEU B 81 5894 4449 9112 -1859 423 -493 B N
ATOM 3915 CA LEU B 81 21.937 14.167 447.794 1.00 49.67 B C
ANISOU 3915 CA LEU B 81 5696 4250 8927 -1584 382 -523 B C
ATOM 3916 C LEU B 81 22.931 13.047 447.490 1.00 51.55 B C
ANISOU 3916 C LEU B 81 5657 4587 9343 -1488 606 -631 B C
ATOM 3917 O LEU B 81 23.119 12.135 448.300 1.00 54.51 B O
ANISOU 3917 O LEU B 81 5859 4984 9867 -1248 529 -658 B O
ATOM 3918 CB LEU B 81 20.597 13.897 447.117 1.00 47.80 B C
ANISOU 3918 CB LEU B 81 5793 3922 8449 -1569 404 -468 B C
ATOM 3919 CG LEU B 81 20.036 12.554 447.560 1.00 46.35 B C
ANISOU 3919 CG LEU B 81 5609 3713 8288 -1300 375 -507 B C
ATOM 3920 CD1 LEU B 81 19.977 12.507 449.075 1.00 45.22 B C
ANISOU 3920 CD1 LEU B 81 5362 3551 8270 -1103 115 -480 B C
ATOM 3921 CD2 LEU B 81 18.664 12.298 446.939 1.00 50.22 B C
ANISOU 3921 CD2 LEU B 81 6411 4118 8552 -1299 372 -461 B C
ATOM 3922 N ILE B 82 23.581 13.111 446.329 1.00 53.67 B N
ANISOU 3922 N ILE B 82 5881 4906 9604 -1672 899 -686 B N
ATOM 3923 CA ILE B 82 24.548 12.093 445.937 1.00 55.84 B C
ANISOU 3923 CA ILE B 82 5891 5257 10070 -1595 1165 -800 B C
ATOM 3924 C ILE B 82 25.743 12.088 446.891 1.00 67.58 B C
ANISOU 3924 C ILE B 82 6967 6835 11875 -1505 1070 -826 B C
ATOM 3925 O ILE B 82 26.176 11.030 447.376 1.00 74.62 B O
ANISOU 3925 O ILE B 82 7623 7757 12972 -1269 1088 -866 B O
ATOM 3926 CB ILE B 82 24.992 12.333 444.485 1.00 58.04 B C
ANISOU 3926 CB ILE B 82 6234 5569 10251 -1850 1514 -856 B C
ATOM 3927 CG1 ILE B 82 23.780 12.332 443.553 1.00 56.62 B C
ANISOU 3927 CG1 ILE B 82 6466 5322 9726 -1946 1565 -816 B C
ATOM 3928 CG2 ILE B 82 26.016 11.288 444.076 1.00 60.60 B C
ANISOU 3928 CG2 ILE B 82 6272 5954 10798 -1770 1830 -992 B C
ATOM 3929 CD1 ILE B 82 24.121 12.479 442.085 1.00 58.95 B C
ANISOU 3929 CD1 ILE B 82 6878 5659 9862 -2202 1909 -866 B C
ATOM 3930 N SER B 83 26.327 13.264 447.141 1.00 58.68 B N
ANISOU 3930 N SER B 83 5737 5752 10806 -1699 973 -801 B N
ATOM 3931 CA SER B 83 27.467 13.300 448.054 1.00 76.84 B C
ANISOU 3931 CA SER B 83 7632 8161 13403 -1638 851 -828 B C
ATOM 3932 C SER B 83 27.046 12.870 449.455 1.00 70.71 B C
ANISOU 3932 C SER B 83 6824 7382 12661 -1377 508 -774 B C
ATOM 3933 O SER B 83 27.779 12.142 450.146 1.00 70.14 B O
ANISOU 3933 O SER B 83 6430 7396 12825 -1185 439 -787 B O
ATOM 3934 CB SER B 83 28.126 14.692 448.070 1.00 72.73 B C
ANISOU 3934 CB SER B 83 7022 7680 12930 -1927 805 -825 B C
ATOM 3935 OG SER B 83 27.190 15.756 448.138 1.00 76.06 B O
ANISOU 3935 OG SER B 83 7790 7995 13115 -2071 647 -749 B O
ATOM 3936 N GLY B 84 25.859 13.308 449.885 1.00 56.16 B N
ANISOU 3936 N GLY B 84 5312 5439 10586 -1364 297 -705 B N
ATOM 3937 CA GLY B 84 25.361 12.934 451.199 1.00 59.81 B C
ANISOU 3937 CA GLY B 84 5794 5888 11042 -1133 -4 -653 B C
ATOM 3938 C GLY B 84 25.179 11.439 451.363 1.00 62.79 B C
ANISOU 3938 C GLY B 84 6110 6254 11495 -834 57 -651 B C
ATOM 3939 O GLY B 84 25.544 10.875 452.398 1.00 70.15 B O
ANISOU 3939 O GLY B 84 6843 7244 12566 -627 -121 -619 B O
ATOM 3940 N LEU B 85 24.645 10.768 450.331 1.00 60.16 B N
ANISOU 3940 N LEU B 85 5945 5843 11070 -815 313 -683 B N
ATOM 3941 CA LEU B 85 24.481 9.314 450.402 1.00 64.69 B C
ANISOU 3941 CA LEU B 85 6468 6377 11733 -546 415 -698 B C
ATOM 3942 C LEU B 85 25.825 8.602 450.437 1.00 61.87 B C
ANISOU 3942 C LEU B 85 5695 6114 11698 -433 555 -743 B C
ATOM 3943 O LEU B 85 26.005 7.644 451.199 1.00 57.94 B O
ANISOU 3943 O LEU B 85 5035 5615 11364 -163 475 -702 B O
ATOM 3944 CB LEU B 85 23.656 8.806 449.217 1.00 57.58 B C
ANISOU 3944 CB LEU B 85 5842 5378 10657 -595 672 -750 B C
ATOM 3945 CG LEU B 85 22.141 8.993 449.281 1.00 49.14 B C
ANISOU 3945 CG LEU B 85 5156 4196 9318 -595 531 -692 B C
ATOM 3946 CD1 LEU B 85 21.505 8.643 447.960 1.00 48.84 B C
ANISOU 3946 CD1 LEU B 85 5354 4103 9101 -709 779 -753 B C
ATOM 3947 CD2 LEU B 85 21.561 8.154 450.387 1.00 47.67 B C
ANISOU 3947 CD2 LEU B 85 4988 3946 9177 -312 353 -638 B C
ATOM 3948 N ALA B 86 26.787 9.067 449.632 1.00 77.93 B N
ANISOU 3948 N ALA B 86 7542 8224 13842 -634 769 -815 B N
ATOM 3949 CA ALA B 86 28.110 8.451 449.649 1.00 71.20 B C
ANISOU 3949 CA ALA B 86 6255 7462 13338 -532 916 -858 B C
ATOM 3950 C ALA B 86 28.770 8.600 451.012 1.00 71.69 B C
ANISOU 3950 C ALA B 86 6012 7635 13591 -402 576 -775 B C
ATOM 3951 O ALA B 86 29.445 7.680 451.483 1.00 65.04 B O
ANISOU 3951 O ALA B 86 4858 6834 13020 -163 572 -747 B O
ATOM 3952 CB ALA B 86 28.992 9.060 448.560 1.00 73.43 B C
ANISOU 3952 CB ALA B 86 6399 7805 13695 -804 1212 -951 B C
ATOM 3953 N SER B 87 28.550 9.737 451.681 1.00 80.96 B N
ANISOU 3953 N SER B 87 7285 8855 14622 -552 279 -731 B N
ATOM 3954 CA SER B 87 29.215 10.016 452.953 1.00 86.10 B C
ANISOU 3954 CA SER B 87 7664 9636 15414 -487 -60 -672 B C
ATOM 3955 C SER B 87 28.624 9.259 454.150 1.00 79.26 B C
ANISOU 3955 C SER B 87 6871 8747 14495 -191 -337 -565 B C
ATOM 3956 O SER B 87 29.297 9.138 455.183 1.00 75.95 B O
ANISOU 3956 O SER B 87 6180 8455 14224 -75 -597 -501 B O
ATOM 3957 CB SER B 87 29.169 11.522 453.226 1.00 63.19 B C
ANISOU 3957 CB SER B 87 4871 6772 12366 -778 -252 -688 B C
ATOM 3958 OG SER B 87 29.140 11.782 454.619 1.00 63.13 B O
ANISOU 3958 OG SER B 87 4824 6838 12325 -702 -644 -627 B O
ATOM 3959 N ALA B 88 27.395 8.755 454.046 1.00 81.58 B N
ANISOU 3959 N ALA B 88 7524 8892 14582 -75 -293 -539 B N
ATOM 3960 CA ALA B 88 26.728 8.142 455.193 1.00 82.23 B C
ANISOU 3960 CA ALA B 88 7723 8936 14583 177 -542 -434 B C
ATOM 3961 C ALA B 88 27.327 6.774 455.494 1.00 91.65 B C
ANISOU 3961 C ALA B 88 8635 10145 16042 487 -486 -371 B C
ATOM 3962 O ALA B 88 27.379 5.898 454.619 1.00 96.71 B O
ANISOU 3962 O ALA B 88 9241 10697 16808 576 -167 -420 B O
ATOM 3963 CB ALA B 88 25.225 8.014 454.931 1.00 65.28 B C
ANISOU 3963 CB ALA B 88 6024 6616 12164 194 -485 -430 B C
ATOM 3964 N ILE B 89 27.787 6.588 456.728 1.00 85.92 B N
ANISOU 3964 N ILE B 89 7715 9528 15402 648 -793 -260 B N
ATOM 3965 CA ILE B 89 28.240 5.282 457.185 1.00 84.00 B C
ANISOU 3965 CA ILE B 89 7232 9284 15401 978 -791 -152 B C
ATOM 3966 C ILE B 89 27.196 4.626 458.078 1.00 76.51 B C
ANISOU 3966 C ILE B 89 6568 8228 14273 1203 -951 -34 B C
ATOM 3967 O ILE B 89 26.972 3.418 457.999 1.00 73.44 B O
ANISOU 3967 O ILE B 89 6185 7716 14003 1455 -795 22 B O
ATOM 3968 CB ILE B 89 29.606 5.395 457.905 1.00 82.69 B C
ANISOU 3968 CB ILE B 89 6595 9329 15493 1026 -1022 -80 B C
ATOM 3969 CG1 ILE B 89 29.605 6.548 458.920 1.00 89.50 B C
ANISOU 3969 CG1 ILE B 89 7517 10341 16147 848 -1423 -59 B C
ATOM 3970 CG2 ILE B 89 30.736 5.585 456.893 1.00 71.02 B C
ANISOU 3970 CG2 ILE B 89 4759 7919 14305 887 -756 -188 B C
ATOM 3971 CD1 ILE B 89 30.926 6.740 459.639 1.00 79.96 B C
ANISOU 3971 CD1 ILE B 89 5847 9366 15167 855 -1691 1 B C
ATOM 3972 N ARG B 90 26.514 5.432 458.885 1.00 69.56 B N
ANISOU 3972 N ARG B 90 5945 7376 13110 1100 -1227 -8 B N
ATOM 3973 CA ARG B 90 25.405 4.941 459.683 1.00 64.78 B C
ANISOU 3973 CA ARG B 90 5654 6657 12301 1273 -1347 88 B C
ATOM 3974 C ARG B 90 24.216 4.638 458.791 1.00 62.20 B C
ANISOU 3974 C ARG B 90 5665 6121 11847 1248 -1067 12 B C
ATOM 3975 O ARG B 90 23.925 5.379 457.851 1.00 68.10 B O
ANISOU 3975 O ARG B 90 6541 6835 12499 1009 -917 -109 B O
ATOM 3976 CB ARG B 90 25.028 5.972 460.734 1.00 63.95 B C
ANISOU 3976 CB ARG B 90 5731 6635 11932 1140 -1683 109 B C
ATOM 3977 CG ARG B 90 25.479 5.657 462.150 1.00 68.75 B C
ANISOU 3977 CG ARG B 90 6209 7380 12534 1315 -2022 260 B C
ATOM 3978 CD ARG B 90 25.524 6.955 462.914 1.00 79.90 B C
ANISOU 3978 CD ARG B 90 7707 8922 13730 1079 -2316 210 B C
ATOM 3979 NE ARG B 90 26.589 7.815 462.393 1.00 95.61 B N
ANISOU 3979 NE ARG B 90 9403 11054 15871 840 -2321 104 B N
ATOM 3980 CZ ARG B 90 26.547 9.147 462.370 1.00 97.15 B C
ANISOU 3980 CZ ARG B 90 9700 11286 15925 535 -2403 -17 B C
ATOM 3981 NH1 ARG B 90 25.466 9.797 462.805 1.00 91.57 B N1+
ANISOU 3981 NH1 ARG B 90 9386 10476 14929 439 -2476 -53 B N1+
ATOM 3982 NH2 ARG B 90 27.578 9.832 461.885 1.00 92.82 B N
ANISOU 3982 NH2 ARG B 90 8859 10860 15548 326 -2386 -105 B N
ATOM 3983 N GLU B 91 23.522 3.546 459.094 1.00 65.26 B N
ANISOU 3983 N GLU B 91 6198 6369 12230 1489 -1006 92 B N
ATOM 3984 CA GLU B 91 22.361 3.174 458.297 1.00 65.65 B C
ANISOU 3984 CA GLU B 91 6555 6225 12166 1466 -759 18 B C
ATOM 3985 C GLU B 91 21.098 3.882 458.774 1.00 56.51 B C
ANISOU 3985 C GLU B 91 5766 5002 10704 1364 -909 23 B C
ATOM 3986 O GLU B 91 21.013 4.386 459.896 1.00 74.01 B O
ANISOU 3986 O GLU B 91 8039 7288 12794 1375 -1186 99 B O
ATOM 3987 CB GLU B 91 22.144 1.665 458.333 1.00 62.20 B C
ANISOU 3987 CB GLU B 91 6109 5639 11884 1752 -587 82 B C
ATOM 3988 CG GLU B 91 23.240 0.880 457.632 1.00 64.60 B C
ANISOU 3988 CG GLU B 91 6079 5950 12517 1854 -346 49 B C
ATOM 3989 CD GLU B 91 22.918 -0.586 457.571 1.00 80.41 B C
ANISOU 3989 CD GLU B 91 8224 7890 14438 1998 -126 87 B C
ATOM 3990 OE1 GLU B 91 21.742 -0.907 457.273 1.00 81.08 B O
ANISOU 3990 OE1 GLU B 91 8651 7882 14274 1934 -9 37 B O
ATOM 3991 OE2 GLU B 91 23.826 -1.410 457.838 1.00 88.92 B O1-
ANISOU 3991 OE2 GLU B 91 9078 9031 15678 2160 -85 168 B O1-
ATOM 3992 N ASN B 92 20.127 3.967 457.872 1.00 49.40 B N
ANISOU 3992 N ASN B 92 5113 3970 9686 1248 -719 -66 B N
ATOM 3993 CA ASN B 92 18.764 4.389 458.203 1.00 50.78 B C
ANISOU 3993 CA ASN B 92 5633 4038 9623 1196 -802 -55 B C
ATOM 3994 C ASN B 92 18.719 5.806 458.799 1.00 49.36 B C
ANISOU 3994 C ASN B 92 5531 3944 9278 1012 -1043 -56 B C
ATOM 3995 O ASN B 92 17.843 6.119 459.604 1.00 56.47 B O
ANISOU 3995 O ASN B 92 6657 4783 10016 1032 -1182 -13 B O
ATOM 3996 CB ASN B 92 18.102 3.367 459.139 1.00 42.62 B C
ANISOU 3996 CB ASN B 92 4740 2974 8479 1406 -819 52 B C
ATOM 3997 CG ASN B 92 18.067 1.953 458.538 1.00 64.11 B C
ANISOU 3997 CG ASN B 92 7450 5692 11218 1509 -534 41 B C
ATOM 3998 ND2 ASN B 92 18.696 0.999 459.229 1.00 77.76 B N
ANISOU 3998 ND2 ASN B 92 9046 7484 13016 1706 -544 143 B N
ATOM 3999 OD1 ASN B 92 17.514 1.728 457.467 1.00 50.27 B O
ANISOU 3999 OD1 ASN B 92 5810 3877 9413 1408 -324 -57 B O
ATOM 4000 N GLU B 93 19.650 6.682 458.395 1.00 57.46 B N
ANISOU 4000 N GLU B 93 6378 5099 10355 822 -1071 -115 B N
ATOM 4001 CA GLU B 93 19.669 8.105 458.753 1.00 53.19 B C
ANISOU 4001 CA GLU B 93 5909 4619 9683 604 -1252 -145 B C
ATOM 4002 C GLU B 93 19.271 8.909 457.523 1.00 48.56 B C
ANISOU 4002 C GLU B 93 5451 3970 9030 365 -1089 -226 B C
ATOM 4003 O GLU B 93 20.131 9.273 456.710 1.00 43.79 B O
ANISOU 4003 O GLU B 93 4671 3446 8522 214 -981 -284 B O
ATOM 4004 CB GLU B 93 21.047 8.569 459.241 1.00 64.49 B C
ANISOU 4004 CB GLU B 93 7033 6241 11228 539 -1417 -148 B C
ATOM 4005 CG GLU B 93 21.427 8.282 460.688 1.00 87.76 B C
ANISOU 4005 CG GLU B 93 9891 9292 14163 698 -1692 -57 B C
ATOM 4006 CD GLU B 93 22.687 9.053 461.123 1.00 96.82 B C
ANISOU 4006 CD GLU B 93 10759 10641 15387 555 -1893 -84 B C
ATOM 4007 OE1 GLU B 93 23.261 9.790 460.288 1.00 99.63 B O
ANISOU 4007 OE1 GLU B 93 10988 11040 15827 336 -1792 -176 B O
ATOM 4008 OE2 GLU B 93 23.109 8.920 462.295 1.00 93.46 B O1-
ANISOU 4008 OE2 GLU B 93 10241 10337 14932 650 -2154 -12 B O1-
ATOM 4009 N PRO B 94 17.991 9.200 457.328 1.00 57.18 B N
ANISOU 4009 N PRO B 94 6840 4921 9965 323 -1063 -221 B N
ATOM 4010 CA PRO B 94 17.581 9.934 456.127 1.00 50.94 B C
ANISOU 4010 CA PRO B 94 6177 4075 9103 106 -926 -267 B C
ATOM 4011 C PRO B 94 18.227 11.305 456.008 1.00 40.30 B C
ANISOU 4011 C PRO B 94 4770 2795 7747 -137 -998 -298 B C
ATOM 4012 O PRO B 94 18.481 11.991 456.997 1.00 40.87 B O
ANISOU 4012 O PRO B 94 4824 2905 7799 -172 -1194 -295 B O
ATOM 4013 CB PRO B 94 16.064 10.054 456.298 1.00 50.22 B C
ANISOU 4013 CB PRO B 94 6390 3826 8865 139 -959 -228 B C
ATOM 4014 CG PRO B 94 15.700 8.800 457.069 1.00 55.73 B C
ANISOU 4014 CG PRO B 94 7097 4482 9597 402 -972 -186 B C
ATOM 4015 CD PRO B 94 16.832 8.636 458.052 1.00 64.66 B C
ANISOU 4015 CD PRO B 94 8006 5745 10818 497 -1115 -163 B C
ATOM 4016 N ILE B 95 18.454 11.682 454.752 1.00 40.71 B N
ANISOU 4016 N ILE B 95 4814 2854 7801 -319 -824 -333 B N
ATOM 4017 CA ILE B 95 19.103 12.903 454.288 1.00 41.97 B C
ANISOU 4017 CA ILE B 95 4917 3058 7969 -577 -813 -361 B C
ATOM 4018 C ILE B 95 18.095 13.634 453.410 1.00 51.76 B C
ANISOU 4018 C ILE B 95 6432 4174 9061 -729 -741 -324 B C
ATOM 4019 O ILE B 95 17.578 13.066 452.442 1.00 56.24 B O
ANISOU 4019 O ILE B 95 7097 4706 9565 -720 -584 -316 B O
ATOM 4020 CB ILE B 95 20.381 12.592 453.487 1.00 44.24 B C
ANISOU 4020 CB ILE B 95 4930 3473 8406 -652 -632 -419 B C
ATOM 4021 CG1 ILE B 95 21.533 12.195 454.401 1.00 46.22 B C
ANISOU 4021 CG1 ILE B 95 4860 3862 8839 -541 -747 -438 B C
ATOM 4022 CG2 ILE B 95 20.755 13.733 452.557 1.00 49.88 B C
ANISOU 4022 CG2 ILE B 95 5667 4194 9092 -943 -524 -437 B C
ATOM 4023 CD1 ILE B 95 22.468 11.206 453.758 1.00 59.93 B C
ANISOU 4023 CD1 ILE B 95 6326 5684 10762 -461 -537 -478 B C
ATOM 4024 N TRP B 96 17.831 14.888 453.735 1.00 54.13 B N
ANISOU 4024 N TRP B 96 6852 4406 9309 -874 -857 -299 B N
ATOM 4025 CA TRP B 96 16.784 15.686 453.113 1.00 39.32 B C
ANISOU 4025 CA TRP B 96 5238 2390 7313 -989 -834 -230 B C
ATOM 4026 C TRP B 96 17.453 16.740 452.238 1.00 40.98 B C
ANISOU 4026 C TRP B 96 5420 2617 7533 -1256 -737 -224 B C
ATOM 4027 O TRP B 96 18.231 17.557 452.740 1.00 42.37 B O
ANISOU 4027 O TRP B 96 5489 2821 7789 -1380 -805 -264 B O
ATOM 4028 CB TRP B 96 15.935 16.325 454.209 1.00 38.18 B C
ANISOU 4028 CB TRP B 96 5254 2174 7079 -918 -989 -198 B C
ATOM 4029 CG TRP B 96 14.864 17.193 453.778 1.00 37.29 B C
ANISOU 4029 CG TRP B 96 5348 2080 6739 -946 -902 -116 B C
ATOM 4030 CD1 TRP B 96 14.315 17.271 452.538 1.00 61.41 B C
ANISOU 4030 CD1 TRP B 96 8508 5136 9689 -1009 -771 -50 B C
ATOM 4031 CD2 TRP B 96 14.191 18.154 454.578 1.00 36.86 B C
ANISOU 4031 CD2 TRP B 96 5403 2033 6567 -915 -934 -96 B C
ATOM 4032 CE2 TRP B 96 13.229 18.776 453.758 1.00 36.32 B C
ANISOU 4032 CE2 TRP B 96 5469 1968 6363 -937 -812 -12 B C
ATOM 4033 CE3 TRP B 96 14.316 18.565 455.906 1.00 37.15 B C
ANISOU 4033 CE3 TRP B 96 5434 2064 6619 -880 -1051 -148 B C
ATOM 4034 NE1 TRP B 96 13.338 18.229 452.509 1.00 36.47 B N
ANISOU 4034 NE1 TRP B 96 5489 1985 6384 -1000 -735 20 B N
ATOM 4035 CZ2 TRP B 96 12.382 19.759 454.227 1.00 36.01 B C
ANISOU 4035 CZ2 TRP B 96 5524 1919 6241 -903 -783 19 B C
ATOM 4036 CZ3 TRP B 96 13.474 19.528 456.373 1.00 36.81 B C
ANISOU 4036 CZ3 TRP B 96 5516 2011 6458 -865 -1005 -127 B C
ATOM 4037 CH2 TRP B 96 12.509 20.114 455.537 1.00 37.30 B C
ANISOU 4037 CH2 TRP B 96 5681 2071 6422 -868 -861 -44 B C
ATOM 4038 N VAL B 97 17.177 16.709 450.936 1.00 41.08 B N
ANISOU 4038 N VAL B 97 5534 2617 7459 -1358 -576 -178 B N
ATOM 4039 CA VAL B 97 17.803 17.629 449.994 1.00 42.88 B C
ANISOU 4039 CA VAL B 97 5756 2860 7676 -1616 -451 -154 B C
ATOM 4040 C VAL B 97 16.740 18.108 449.024 1.00 55.50 B C
ANISOU 4040 C VAL B 97 7626 4350 9113 -1706 -414 -29 B C
ATOM 4041 O VAL B 97 16.048 17.287 448.417 1.00 48.90 B O
ANISOU 4041 O VAL B 97 6886 3525 8168 -1624 -360 -7 B O
ATOM 4042 CB VAL B 97 18.967 16.977 449.229 1.00 44.72 B C
ANISOU 4042 CB VAL B 97 5773 3248 7971 -1678 -241 -234 B C
ATOM 4043 CG1 VAL B 97 19.346 17.845 448.049 1.00 46.47 B C
ANISOU 4043 CG1 VAL B 97 6061 3468 8129 -1949 -73 -187 B C
ATOM 4044 CG2 VAL B 97 20.153 16.810 450.144 1.00 46.03 B C
ANISOU 4044 CG2 VAL B 97 5634 3524 8332 -1632 -299 -330 B C
ATOM 4045 N GLU B 98 16.620 19.427 448.854 1.00 53.17 B N
ANISOU 4045 N GLU B 98 7445 4013 8745 -1845 -410 47 B N
ATOM 4046 CA GLU B 98 15.573 19.993 448.016 1.00 53.35 B C
ANISOU 4046 CA GLU B 98 7682 4012 8577 -1853 -353 175 B C
ATOM 4047 C GLU B 98 16.141 20.674 446.775 1.00 52.73 B C
ANISOU 4047 C GLU B 98 7644 3914 8478 -2116 -211 252 B C
ATOM 4048 O GLU B 98 17.276 21.146 446.763 1.00 55.67 B O
ANISOU 4048 O GLU B 98 7899 4285 8967 -2307 -143 207 B O
ATOM 4049 CB GLU B 98 14.719 20.997 448.800 1.00 41.92 B C
ANISOU 4049 CB GLU B 98 6313 2542 7072 -1721 -419 217 B C
ATOM 4050 CG GLU B 98 14.027 20.381 449.970 1.00 39.93 B C
ANISOU 4050 CG GLU B 98 6045 2326 6799 -1477 -527 164 B C
ATOM 4051 CD GLU B 98 13.208 21.373 450.774 1.00 59.24 B C
ANISOU 4051 CD GLU B 98 8558 4750 9201 -1373 -555 191 B C
ATOM 4052 OE1 GLU B 98 13.689 22.505 451.007 1.00 40.80 B O
ANISOU 4052 OE1 GLU B 98 6225 2358 6918 -1493 -532 180 B O
ATOM 4053 OE2 GLU B 98 12.086 21.001 451.208 1.00 63.49 B O1-
ANISOU 4053 OE2 GLU B 98 9135 5324 9665 -1181 -582 213 B O1-
ATOM 4054 N THR B 99 15.335 20.687 445.726 1.00 55.86 B N
ANISOU 4054 N THR B 99 8195 4314 8714 -2128 -175 377 B N
ATOM 4055 CA THR B 99 15.497 21.519 444.548 1.00 63.78 B C
ANISOU 4055 CA THR B 99 9300 5313 9619 -2327 -75 510 B C
ATOM 4056 C THR B 99 14.364 22.539 444.579 1.00 46.71 B C
ANISOU 4056 C THR B 99 7251 3099 7397 -2202 -160 652 B C
ATOM 4057 O THR B 99 13.693 22.718 445.610 1.00 49.40 B O
ANISOU 4057 O THR B 99 7564 3415 7791 -1999 -252 613 B O
ATOM 4058 CB THR B 99 15.466 20.688 443.261 1.00 60.97 B C
ANISOU 4058 CB THR B 99 9069 5032 9065 -2466 34 543 B C
ATOM 4059 CG2 THR B 99 16.299 19.409 443.420 1.00 47.69 B C
ANISOU 4059 CG2 THR B 99 7247 3428 7444 -2477 157 349 B C
ATOM 4060 OG1 THR B 99 14.110 20.358 442.914 1.00 61.27 B O
ANISOU 4060 OG1 THR B 99 9254 5081 8946 -2327 -82 637 B O
ATOM 4061 N ASP B 100 14.175 23.263 443.475 1.00 57.04 B N
ANISOU 4061 N ASP B 100 8691 4396 8585 -2333 -113 819 B N
ATOM 4062 CA ASP B 100 13.062 24.212 443.478 1.00 68.14 B C
ANISOU 4062 CA ASP B 100 10191 5741 9959 -2209 -197 964 B C
ATOM 4063 C ASP B 100 11.723 23.520 443.254 1.00 65.69 B C
ANISOU 4063 C ASP B 100 9962 5481 9516 -2049 -325 1026 B C
ATOM 4064 O ASP B 100 10.685 24.059 443.646 1.00 72.05 B O
ANISOU 4064 O ASP B 100 10783 6249 10345 -1884 -408 1091 B O
ATOM 4065 CB ASP B 100 13.260 25.346 442.461 1.00 64.07 B C
ANISOU 4065 CB ASP B 100 9788 5176 9381 -2383 -122 1144 B C
ATOM 4066 CG ASP B 100 13.694 24.863 441.103 1.00 78.85 B C
ANISOU 4066 CG ASP B 100 11779 7139 11043 -2606 -34 1221 B C
ATOM 4067 OD1 ASP B 100 14.487 23.898 441.050 1.00 87.12 B O
ANISOU 4067 OD1 ASP B 100 12764 8262 12075 -2705 58 1080 B O
ATOM 4068 OD2 ASP B 100 13.223 25.447 440.101 1.00 79.56 B O1-
ANISOU 4068 OD2 ASP B 100 12033 7227 10970 -2685 -41 1417 B O1-
ATOM 4069 N ARG B 101 11.716 22.356 442.604 1.00 58.50 B N
ANISOU 4069 N ARG B 101 9105 4653 8469 -2113 -326 998 B N
ATOM 4070 CA ARG B 101 10.477 21.651 442.297 1.00 75.38 B C
ANISOU 4070 CA ARG B 101 11323 6840 10479 -1999 -450 1050 B C
ATOM 4071 C ARG B 101 10.340 20.276 442.959 1.00 62.91 B C
ANISOU 4071 C ARG B 101 9657 5299 8945 -1865 -471 879 B C
ATOM 4072 O ARG B 101 9.226 19.737 442.995 1.00 46.67 B O
ANISOU 4072 O ARG B 101 7625 3272 6836 -1731 -577 897 B O
ATOM 4073 CB ARG B 101 10.321 21.529 440.771 1.00 47.77 B C
ANISOU 4073 CB ARG B 101 8026 3402 6721 -2214 -444 1193 B C
ATOM 4074 CG ARG B 101 10.261 22.910 440.169 1.00 59.24 B C
ANISOU 4074 CG ARG B 101 9568 4810 8132 -2303 -444 1393 B C
ATOM 4075 CD ARG B 101 10.369 23.000 438.659 1.00 54.84 B C
ANISOU 4075 CD ARG B 101 9224 4325 7289 -2555 -403 1550 B C
ATOM 4076 NE ARG B 101 10.856 24.343 438.327 1.00 63.34 B N
ANISOU 4076 NE ARG B 101 10331 5335 8399 -2650 -324 1690 B N
ATOM 4077 CZ ARG B 101 10.540 25.039 437.234 1.00 80.26 B C
ANISOU 4077 CZ ARG B 101 12648 7495 10352 -2773 -348 1913 B C
ATOM 4078 NH1 ARG B 101 9.712 24.532 436.325 1.00 83.26 B N1+
ANISOU 4078 NH1 ARG B 101 13194 7974 10466 -2834 -474 2028 B N1+
ATOM 4079 NH2 ARG B 101 11.071 26.251 437.041 1.00 82.46 B N
ANISOU 4079 NH2 ARG B 101 12936 7690 10703 -2847 -247 2024 B N
ATOM 4080 N LEU B 102 11.422 19.692 443.467 1.00 47.51 B N
ANISOU 4080 N LEU B 102 7600 3347 7105 -1900 -374 719 B N
ATOM 4081 CA LEU B 102 11.372 18.373 444.073 1.00 41.47 B C
ANISOU 4081 CA LEU B 102 6759 2602 6398 -1770 -380 565 B C
ATOM 4082 C LEU B 102 12.021 18.436 445.449 1.00 56.94 B C
ANISOU 4082 C LEU B 102 8550 4531 8553 -1647 -377 442 B C
ATOM 4083 O LEU B 102 12.867 19.300 445.718 1.00 43.26 B O
ANISOU 4083 O LEU B 102 6760 2767 6908 -1746 -338 437 B O
ATOM 4084 CB LEU B 102 12.061 17.308 443.195 1.00 42.50 B C
ANISOU 4084 CB LEU B 102 6955 2760 6433 -1957 -249 476 B C
ATOM 4085 CG LEU B 102 11.437 16.988 441.840 1.00 43.70 B C
ANISOU 4085 CG LEU B 102 7317 2968 6320 -2113 -230 555 B C
ATOM 4086 CD1 LEU B 102 12.411 16.239 440.975 1.00 45.39 B C
ANISOU 4086 CD1 LEU B 102 7536 3294 6415 -2285 20 416 B C
ATOM 4087 CD2 LEU B 102 10.183 16.149 442.035 1.00 48.49 B C
ANISOU 4087 CD2 LEU B 102 7949 3582 6893 -1934 -362 538 B C
ATOM 4088 N SER B 103 11.559 17.549 446.332 1.00 38.60 B N
ANISOU 4088 N SER B 103 6164 2229 6275 -1438 -425 351 B N
ATOM 4089 CA SER B 103 12.045 17.398 447.699 1.00 45.49 B C
ANISOU 4089 CA SER B 103 6914 3101 7268 -1308 -453 245 B C
ATOM 4090 C SER B 103 12.433 15.941 447.897 1.00 38.10 B C
ANISOU 4090 C SER B 103 5911 2164 6401 -1236 -432 130 B C
ATOM 4091 O SER B 103 11.579 15.055 447.790 1.00 39.32 B O
ANISOU 4091 O SER B 103 6108 2342 6491 -1113 -431 118 B O
ATOM 4092 CB SER B 103 10.971 17.825 448.702 1.00 45.30 B C
ANISOU 4092 CB SER B 103 6893 3115 7205 -1103 -523 274 B C
ATOM 4093 OG SER B 103 11.471 17.922 450.016 1.00 35.71 B O
ANISOU 4093 OG SER B 103 5597 1907 6064 -1022 -566 195 B O
ATOM 4094 N PHE B 104 13.707 15.698 448.195 1.00 43.15 B N
ANISOU 4094 N PHE B 104 6413 2773 7210 -1305 -414 43 B N
ATOM 4095 CA PHE B 104 14.285 14.359 448.251 1.00 38.17 B C
ANISOU 4095 CA PHE B 104 5638 2182 6683 -1209 -330 -78 B C
ATOM 4096 C PHE B 104 14.578 13.947 449.690 1.00 37.38 B C
ANISOU 4096 C PHE B 104 5391 2073 6738 -1006 -440 -135 B C
ATOM 4097 O PHE B 104 15.016 14.762 450.512 1.00 38.11 B O
ANISOU 4097 O PHE B 104 5421 2150 6910 -1032 -552 -127 B O
ATOM 4098 CB PHE B 104 15.578 14.282 447.426 1.00 40.35 B C
ANISOU 4098 CB PHE B 104 5771 2586 6975 -1360 -122 -151 B C
ATOM 4099 CG PHE B 104 15.359 14.404 445.939 1.00 41.47 B C
ANISOU 4099 CG PHE B 104 6069 2764 6925 -1555 26 -114 B C
ATOM 4100 CD1 PHE B 104 15.365 15.651 445.321 1.00 42.53 B C
ANISOU 4100 CD1 PHE B 104 6323 2871 6966 -1771 19 2 B C
ATOM 4101 CD2 PHE B 104 15.144 13.280 445.158 1.00 41.74 B C
ANISOU 4101 CD2 PHE B 104 6144 2853 6861 -1532 176 -192 B C
ATOM 4102 CE1 PHE B 104 15.148 15.771 443.953 1.00 53.72 B C
ANISOU 4102 CE1 PHE B 104 7906 4333 8172 -1956 141 58 B C
ATOM 4103 CE2 PHE B 104 14.940 13.386 443.793 1.00 43.07 B C
ANISOU 4103 CE2 PHE B 104 6479 3073 6813 -1730 304 -165 B C
ATOM 4104 CZ PHE B 104 14.933 14.628 443.186 1.00 50.02 B C
ANISOU 4104 CZ PHE B 104 7486 3944 7578 -1941 278 -30 B C
ATOM 4105 N LEU B 105 14.310 12.678 449.987 1.00 36.58 B N
ANISOU 4105 N LEU B 105 5251 1979 6668 -813 -410 -190 B N
ATOM 4106 CA LEU B 105 14.688 12.046 451.242 1.00 44.30 B C
ANISOU 4106 CA LEU B 105 6083 2970 7778 -607 -489 -233 B C
ATOM 4107 C LEU B 105 15.354 10.726 450.906 1.00 45.38 B C
ANISOU 4107 C LEU B 105 6061 3184 7998 -502 -316 -320 B C
ATOM 4108 O LEU B 105 14.704 9.837 450.355 1.00 54.84 B O
ANISOU 4108 O LEU B 105 7351 4342 9143 -445 -211 -347 B O
ATOM 4109 CB LEU B 105 13.464 11.811 452.124 1.00 48.42 B C
ANISOU 4109 CB LEU B 105 6740 3498 8160 -423 -584 -176 B C
ATOM 4110 CG LEU B 105 13.744 11.405 453.566 1.00 51.70 B C
ANISOU 4110 CG LEU B 105 7055 3930 8659 -236 -697 -186 B C
ATOM 4111 CD1 LEU B 105 14.365 12.582 454.309 1.00 55.50 B C
ANISOU 4111 CD1 LEU B 105 7487 4396 9204 -334 -850 -183 B C
ATOM 4112 CD2 LEU B 105 12.462 10.940 454.237 1.00 52.72 B C
ANISOU 4112 CD2 LEU B 105 7304 4156 8572 -76 -679 -135 B C
ATOM 4113 N GLY B 106 16.630 10.585 451.235 1.00 38.78 B N
ANISOU 4113 N GLY B 106 4979 2449 7307 -478 -282 -368 B N
ATOM 4114 CA GLY B 106 17.359 9.375 450.911 1.00 40.07 B C
ANISOU 4114 CA GLY B 106 4962 2669 7593 -368 -95 -446 B C
ATOM 4115 C GLY B 106 18.082 8.839 452.127 1.00 50.13 B C
ANISOU 4115 C GLY B 106 6012 3988 9047 -159 -202 -436 B C
ATOM 4116 O GLY B 106 18.456 9.586 453.019 1.00 41.02 B O
ANISOU 4116 O GLY B 106 4785 2879 7922 -175 -396 -398 B O
ATOM 4117 N TRP B 107 18.218 7.513 452.188 1.00 41.22 B N
ANISOU 4117 N TRP B 107 4791 2839 8033 39 -83 -467 B N
ATOM 4118 CA TRP B 107 18.987 6.929 453.279 1.00 48.51 B C
ANISOU 4118 CA TRP B 107 5481 3811 9138 252 -184 -430 B C
ATOM 4119 C TRP B 107 19.635 5.630 452.826 1.00 44.08 B C
ANISOU 4119 C TRP B 107 4733 3246 8768 399 54 -486 B C
ATOM 4120 O TRP B 107 19.215 5.007 451.849 1.00 47.58 B O
ANISOU 4120 O TRP B 107 5288 3617 9175 368 286 -563 B O
ATOM 4121 CB TRP B 107 18.127 6.666 454.520 1.00 47.94 B C
ANISOU 4121 CB TRP B 107 5547 3660 9006 438 -391 -342 B C
ATOM 4122 CG TRP B 107 17.138 5.592 454.313 1.00 40.09 B C
ANISOU 4122 CG TRP B 107 4718 2530 7984 576 -269 -347 B C
ATOM 4123 CD1 TRP B 107 17.275 4.282 454.639 1.00 40.26 B C
ANISOU 4123 CD1 TRP B 107 4652 2496 8148 808 -178 -333 B C
ATOM 4124 CD2 TRP B 107 15.846 5.736 453.731 1.00 42.56 B C
ANISOU 4124 CD2 TRP B 107 5304 2736 8131 483 -227 -364 B C
ATOM 4125 CE2 TRP B 107 15.247 4.461 453.730 1.00 58.92 B C
ANISOU 4125 CE2 TRP B 107 7445 4777 10167 634 -102 -367 B C
ATOM 4126 CE3 TRP B 107 15.136 6.821 453.205 1.00 45.53 B C
ANISOU 4126 CE3 TRP B 107 5866 3096 8338 275 -283 -359 B C
ATOM 4127 NE1 TRP B 107 16.143 3.590 454.292 1.00 55.42 B N
ANISOU 4127 NE1 TRP B 107 6790 4337 9929 833 -65 -350 B N
ATOM 4128 CZ2 TRP B 107 13.966 4.232 453.216 1.00 35.65 B C
ANISOU 4128 CZ2 TRP B 107 4734 1872 6941 559 -42 -369 B C
ATOM 4129 CZ3 TRP B 107 13.864 6.595 452.694 1.00 53.92 B C
ANISOU 4129 CZ3 TRP B 107 7150 4155 9181 237 -227 -349 B C
ATOM 4130 CH2 TRP B 107 13.293 5.303 452.704 1.00 46.62 B C
ANISOU 4130 CH2 TRP B 107 6276 3268 8170 373 -112 -358 B C
ATOM 4131 N ARG B 108 20.641 5.202 453.581 1.00 45.96 B N
ANISOU 4131 N ARG B 108 4687 3557 9216 564 -10 -444 B N
ATOM 4132 CA ARG B 108 21.360 3.970 453.290 1.00 61.21 B C
ANISOU 4132 CA ARG B 108 6399 5469 11388 740 211 -479 B C
ATOM 4133 C ARG B 108 20.819 2.834 454.138 1.00 57.87 B C
ANISOU 4133 C ARG B 108 6031 4932 11026 1028 159 -395 B C
ATOM 4134 O ARG B 108 20.732 2.951 455.368 1.00 47.18 B O
ANISOU 4134 O ARG B 108 4668 3606 9652 1157 -108 -275 B O
ATOM 4135 CB ARG B 108 22.855 4.108 453.561 1.00 69.95 B C
ANISOU 4135 CB ARG B 108 7115 6723 12740 768 182 -463 B C
ATOM 4136 CG ARG B 108 23.599 2.780 453.483 1.00 62.95 B C
ANISOU 4136 CG ARG B 108 5969 5796 12153 1008 385 -466 B C
ATOM 4137 CD ARG B 108 25.002 2.991 453.924 1.00 66.41 B C
ANISOU 4137 CD ARG B 108 5998 6391 12844 1051 292 -421 B C
ATOM 4138 NE ARG B 108 25.809 1.793 453.808 1.00 73.80 B N
ANISOU 4138 NE ARG B 108 6642 7285 14113 1285 498 -414 B N
ATOM 4139 CZ ARG B 108 27.140 1.831 453.809 1.00100.89 B C
ANISOU 4139 CZ ARG B 108 9663 10839 17833 1311 530 -407 B C
ATOM 4140 NH1 ARG B 108 27.756 3.007 453.916 1.00112.97 B N1+
ANISOU 4140 NH1 ARG B 108 11051 12541 19333 1097 364 -418 B N1+
ATOM 4141 NH2 ARG B 108 27.858 0.718 453.675 1.00102.97 B N
ANISOU 4141 NH2 ARG B 108 9648 11042 18434 1543 740 -395 B N
ATOM 4142 N HIS B 109 20.483 1.731 453.479 1.00 61.26 B N
ANISOU 4142 N HIS B 109 6523 5228 11523 1118 425 -464 B N
ATOM 4143 CA HIS B 109 20.040 0.521 454.160 1.00 67.81 B C
ANISOU 4143 CA HIS B 109 7395 5923 12445 1391 438 -390 B C
ATOM 4144 C HIS B 109 20.773 -0.680 453.568 1.00 76.91 B C
ANISOU 4144 C HIS B 109 8377 7066 13780 1489 736 -447 B C
ATOM 4145 O HIS B 109 20.461 -1.119 452.457 1.00 50.16 B O
ANISOU 4145 O HIS B 109 5102 3601 10355 1383 1015 -589 B O
ATOM 4146 CB HIS B 109 18.529 0.365 454.052 1.00 61.08 B C
ANISOU 4146 CB HIS B 109 6928 5053 11225 1289 424 -393 B C
ATOM 4147 CG HIS B 109 18.001 -0.826 454.785 1.00 62.47 B C
ANISOU 4147 CG HIS B 109 7229 5283 11223 1436 411 -295 B C
ATOM 4148 CD2 HIS B 109 17.636 -2.054 454.351 1.00 56.71 B C
ANISOU 4148 CD2 HIS B 109 6591 4526 10433 1472 606 -337 B C
ATOM 4149 ND1 HIS B 109 17.783 -0.819 456.145 1.00 64.92 B N
ANISOU 4149 ND1 HIS B 109 7600 5672 11397 1554 180 -146 B N
ATOM 4150 CE1 HIS B 109 17.311 -1.996 456.517 1.00 62.78 B C
ANISOU 4150 CE1 HIS B 109 7453 5412 10987 1662 245 -99 B C
ATOM 4151 NE2 HIS B 109 17.214 -2.762 455.448 1.00 61.21 B N
ANISOU 4151 NE2 HIS B 109 7266 5146 10844 1614 486 -212 B N
ATOM 4152 N GLU B 110 21.728 -1.220 454.324 1.00 73.80 B N
ANISOU 4152 N GLU B 110 7727 6752 13561 1679 666 -331 B N
ATOM 4153 CA GLU B 110 22.553 -2.359 453.910 1.00 65.56 B C
ANISOU 4153 CA GLU B 110 6498 5698 12714 1789 921 -356 B C
ATOM 4154 C GLU B 110 23.225 -1.999 452.592 1.00 58.45 B C
ANISOU 4154 C GLU B 110 5420 4751 12037 1654 1229 -549 B C
ATOM 4155 O GLU B 110 24.024 -1.049 452.569 1.00 58.75 B O
ANISOU 4155 O GLU B 110 5207 4880 12236 1591 1158 -564 B O
ATOM 4156 CB GLU B 110 21.738 -3.655 453.886 1.00 70.78 B C
ANISOU 4156 CB GLU B 110 7420 6297 13175 1842 1040 -345 B C
ATOM 4157 CG GLU B 110 21.325 -4.176 455.243 1.00 78.60 B C
ANISOU 4157 CG GLU B 110 8531 7345 13989 2006 795 -160 B C
ATOM 4158 CD GLU B 110 20.733 -5.564 455.152 1.00 84.26 B C
ANISOU 4158 CD GLU B 110 9432 7992 14591 2067 947 -166 B C
ATOM 4159 OE1 GLU B 110 20.773 -6.152 454.051 1.00 84.79 B O
ANISOU 4159 OE1 GLU B 110 9499 7971 14745 1990 1234 -306 B O
ATOM 4160 OE2 GLU B 110 20.243 -6.076 456.178 1.00 87.17 B O1-
ANISOU 4160 OE2 GLU B 110 9942 8389 14789 2185 790 -41 B O1-
ATOM 4161 N ASN B 111 23.012 -2.753 451.518 1.00 68.53 B N
ANISOU 4161 N ASN B 111 6816 5936 13286 1576 1568 -696 B N
ATOM 4162 CA ASN B 111 23.615 -2.502 450.217 1.00 71.11 B C
ANISOU 4162 CA ASN B 111 7022 6225 13772 1427 1922 -904 B C
ATOM 4163 C ASN B 111 22.927 -1.396 449.443 1.00 63.33 B C
ANISOU 4163 C ASN B 111 6290 5282 12492 1122 1908 -1011 B C
ATOM 4164 O ASN B 111 23.414 -1.020 448.377 1.00 69.96 B O
ANISOU 4164 O ASN B 111 7101 6187 13296 906 2140 -1147 B O
ATOM 4165 CB ASN B 111 23.623 -3.778 449.367 1.00 82.30 B C
ANISOU 4165 CB ASN B 111 8529 7561 15182 1412 2267 -1016 B C
ATOM 4166 CG ASN B 111 24.582 -3.676 448.186 1.00 92.37 B C
ANISOU 4166 CG ASN B 111 9617 8828 16652 1289 2656 -1211 B C
ATOM 4167 ND2 ASN B 111 24.437 -4.602 447.240 1.00 96.29 B N
ANISOU 4167 ND2 ASN B 111 10258 9237 17091 1206 2980 -1355 B N
ATOM 4168 OD1 ASN B 111 25.444 -2.782 448.122 1.00 84.42 B O
ANISOU 4168 OD1 ASN B 111 8333 7908 15837 1251 2672 -1236 B O
ATOM 4169 N TYR B 112 21.782 -0.917 449.897 1.00 59.06 B N
ANISOU 4169 N TYR B 112 6029 4731 11680 1067 1644 -937 B N
ATOM 4170 CA TYR B 112 20.980 -0.041 449.068 1.00 51.74 B C
ANISOU 4170 CA TYR B 112 5392 3850 10417 766 1628 -1011 B C
ATOM 4171 C TYR B 112 21.013 1.397 449.561 1.00 50.38 B C
ANISOU 4171 C TYR B 112 5223 3824 10094 625 1310 -901 B C
ATOM 4172 O TYR B 112 21.361 1.692 450.708 1.00 70.96 B O
ANISOU 4172 O TYR B 112 7677 6487 12796 761 1048 -768 B O
ATOM 4173 CB TYR B 112 19.535 -0.547 449.007 1.00 49.52 B C
ANISOU 4173 CB TYR B 112 5441 3429 9945 774 1608 -1033 B C
ATOM 4174 CG TYR B 112 19.420 -1.987 448.583 1.00 61.28 B C
ANISOU 4174 CG TYR B 112 6957 4796 11532 882 1894 -1133 B C
ATOM 4175 CD1 TYR B 112 19.395 -2.319 447.238 1.00 69.88 B C
ANISOU 4175 CD1 TYR B 112 8154 5833 12565 704 2234 -1343 B C
ATOM 4176 CD2 TYR B 112 19.341 -3.023 449.515 1.00 56.98 B C
ANISOU 4176 CD2 TYR B 112 6367 4290 10992 1089 1780 -985 B C
ATOM 4177 CE1 TYR B 112 19.287 -3.640 446.818 1.00 66.06 B C
ANISOU 4177 CE1 TYR B 112 7711 5328 12061 734 2443 -1404 B C
ATOM 4178 CE2 TYR B 112 19.234 -4.351 449.102 1.00 52.73 B C
ANISOU 4178 CE2 TYR B 112 5876 3714 10445 1122 1992 -1040 B C
ATOM 4179 CZ TYR B 112 19.211 -4.651 447.744 1.00 58.21 B C
ANISOU 4179 CZ TYR B 112 6655 4347 11113 944 2321 -1251 B C
ATOM 4180 OH TYR B 112 19.107 -5.952 447.279 1.00 75.00 B O
ANISOU 4180 OH TYR B 112 8832 6420 13243 953 2539 -1322 B O
ATOM 4181 N TYR B 113 20.660 2.278 448.641 1.00 49.64 B N
ANISOU 4181 N TYR B 113 5316 3789 9758 340 1347 -962 B N
ATOM 4182 CA TYR B 113 20.222 3.635 448.911 1.00 56.26 B C
ANISOU 4182 CA TYR B 113 6286 4704 10386 172 1073 -871 B C
ATOM 4183 C TYR B 113 18.756 3.679 448.517 1.00 45.52 B C
ANISOU 4183 C TYR B 113 5279 3257 8759 83 1025 -875 B C
ATOM 4184 O TYR B 113 18.404 3.316 447.387 1.00 60.06 B O
ANISOU 4184 O TYR B 113 7273 5070 10478 -51 1246 -987 B O
ATOM 4185 CB TYR B 113 20.994 4.657 448.073 1.00 53.58 B C
ANISOU 4185 CB TYR B 113 5876 4488 9995 -95 1170 -915 B C
ATOM 4186 CG TYR B 113 22.469 4.757 448.358 1.00 61.31 B C
ANISOU 4186 CG TYR B 113 6479 5568 11247 -52 1222 -919 B C
ATOM 4187 CD1 TYR B 113 22.975 4.560 449.638 1.00 52.20 B C
ANISOU 4187 CD1 TYR B 113 5086 4445 10302 171 1005 -821 B C
ATOM 4188 CD2 TYR B 113 23.372 4.975 447.321 1.00 54.23 B C
ANISOU 4188 CD2 TYR B 113 5456 4742 10406 -234 1503 -1021 B C
ATOM 4189 CE1 TYR B 113 24.341 4.636 449.885 1.00 69.94 B C
ANISOU 4189 CE1 TYR B 113 6954 6801 12818 207 1032 -819 B C
ATOM 4190 CE2 TYR B 113 24.736 5.042 447.553 1.00 56.88 B C
ANISOU 4190 CE2 TYR B 113 5412 5172 11027 -198 1566 -1030 B C
ATOM 4191 CZ TYR B 113 25.217 4.872 448.832 1.00 62.85 B C
ANISOU 4191 CZ TYR B 113 5911 5966 12003 25 1319 -927 B C
ATOM 4192 OH TYR B 113 26.572 4.943 449.055 1.00 60.15 B O
ANISOU 4192 OH TYR B 113 5163 5731 11959 56 1358 -929 B O
ATOM 4193 N ILE B 114 17.898 4.099 449.426 1.00 43.29 B N
ANISOU 4193 N ILE B 114 5127 2936 8386 148 745 -761 B N
ATOM 4194 CA ILE B 114 16.498 4.296 449.097 1.00 41.24 B C
ANISOU 4194 CA ILE B 114 5171 2603 7897 56 670 -747 B C
ATOM 4195 C ILE B 114 16.249 5.793 449.007 1.00 40.33 B C
ANISOU 4195 C ILE B 114 5160 2550 7614 -146 484 -667 B C
ATOM 4196 O ILE B 114 16.623 6.549 449.910 1.00 40.05 B O
ANISOU 4196 O ILE B 114 5030 2554 7635 -115 290 -585 B O
ATOM 4197 CB ILE B 114 15.592 3.616 450.131 1.00 46.18 B C
ANISOU 4197 CB ILE B 114 5879 3106 8561 280 535 -683 B C
ATOM 4198 CG1 ILE B 114 16.090 2.181 450.376 1.00 40.98 B C
ANISOU 4198 CG1 ILE B 114 5071 2375 8125 507 718 -735 B C
ATOM 4199 CG2 ILE B 114 14.150 3.656 449.646 1.00 37.91 B C
ANISOU 4199 CG2 ILE B 114 5109 1980 7314 181 501 -689 B C
ATOM 4200 CD1 ILE B 114 15.238 1.365 451.311 1.00 39.75 B C
ANISOU 4200 CD1 ILE B 114 5011 2258 7836 684 598 -631 B C
ATOM 4201 N ILE B 115 15.649 6.225 447.906 1.00 40.17 B N
ANISOU 4201 N ILE B 115 5337 2538 7387 -361 546 -689 B N
ATOM 4202 CA ILE B 115 15.378 7.634 447.669 1.00 39.63 B C
ANISOU 4202 CA ILE B 115 5385 2507 7166 -558 398 -597 B C
ATOM 4203 C ILE B 115 13.891 7.799 447.393 1.00 37.98 B C
ANISOU 4203 C ILE B 115 5437 2220 6772 -607 282 -538 B C
ATOM 4204 O ILE B 115 13.359 7.224 446.437 1.00 38.36 B O
ANISOU 4204 O ILE B 115 5616 2265 6695 -689 406 -602 B O
ATOM 4205 CB ILE B 115 16.197 8.197 446.500 1.00 41.65 B C
ANISOU 4205 CB ILE B 115 5616 2864 7344 -802 579 -641 B C
ATOM 4206 CG1 ILE B 115 17.686 8.075 446.781 1.00 43.54 B C
ANISOU 4206 CG1 ILE B 115 5558 3182 7804 -759 697 -699 B C
ATOM 4207 CG2 ILE B 115 15.844 9.658 446.281 1.00 41.21 B C
ANISOU 4207 CG2 ILE B 115 5700 2817 7140 -996 424 -521 B C
ATOM 4208 CD1 ILE B 115 18.302 6.926 446.080 1.00 45.40 B C
ANISOU 4208 CD1 ILE B 115 5688 3435 8127 -723 1003 -841 B C
ATOM 4209 N GLU B 116 13.240 8.612 448.210 1.00 36.42 B N
ANISOU 4209 N GLU B 116 5311 1964 6563 -568 47 -422 B N
ATOM 4210 CA GLU B 116 11.855 9.016 448.051 1.00 35.04 B C
ANISOU 4210 CA GLU B 116 5348 1711 6254 -612 -91 -337 B C
ATOM 4211 C GLU B 116 11.831 10.484 447.624 1.00 51.12 B C
ANISOU 4211 C GLU B 116 7470 3767 8187 -810 -187 -229 B C
ATOM 4212 O GLU B 116 12.597 11.302 448.140 1.00 59.22 B O
ANISOU 4212 O GLU B 116 8399 4811 9290 -839 -239 -199 B O
ATOM 4213 CB GLU B 116 11.097 8.826 449.373 1.00 33.26 B C
ANISOU 4213 CB GLU B 116 5131 1560 5945 -383 -212 -267 B C
ATOM 4214 CG GLU B 116 10.943 7.386 449.888 1.00 36.53 B C
ANISOU 4214 CG GLU B 116 5495 1988 6396 -181 -136 -325 B C
ATOM 4215 CD GLU B 116 10.215 7.312 451.240 1.00 43.05 B C
ANISOU 4215 CD GLU B 116 6332 2919 7107 -5 -213 -241 B C
ATOM 4216 OE1 GLU B 116 10.053 8.375 451.865 1.00 51.94 B O
ANISOU 4216 OE1 GLU B 116 7458 4096 8182 -25 -308 -171 B O
ATOM 4217 OE2 GLU B 116 9.764 6.217 451.664 1.00 55.70 B O1-
ANISOU 4217 OE2 GLU B 116 7945 4553 8664 131 -155 -252 B O1-
ATOM 4218 N VAL B 117 10.975 10.823 446.670 1.00 48.68 B N
ANISOU 4218 N VAL B 117 7339 3451 7707 -953 -214 -164 B N
ATOM 4219 CA VAL B 117 10.882 12.187 446.170 1.00 36.13 B C
ANISOU 4219 CA VAL B 117 5835 1887 6008 -1125 -283 -35 B C
ATOM 4220 C VAL B 117 9.427 12.629 446.171 1.00 35.09 B C
ANISOU 4220 C VAL B 117 5754 1829 5749 -1037 -379 77 B C
ATOM 4221 O VAL B 117 8.522 11.866 445.808 1.00 40.24 B O
ANISOU 4221 O VAL B 117 6456 2498 6336 -996 -385 59 B O
ATOM 4222 CB VAL B 117 11.493 12.335 444.757 1.00 38.25 B C
ANISOU 4222 CB VAL B 117 6169 2246 6118 -1371 -128 -50 B C
ATOM 4223 CG1 VAL B 117 10.705 11.551 443.719 1.00 54.53 B C
ANISOU 4223 CG1 VAL B 117 8376 4352 7989 -1442 -74 -85 B C
ATOM 4224 CG2 VAL B 117 11.553 13.785 444.358 1.00 39.13 B C
ANISOU 4224 CG2 VAL B 117 6371 2342 6155 -1550 -201 104 B C
ATOM 4225 N GLU B 118 9.211 13.880 446.555 1.00 46.16 B N
ANISOU 4225 N GLU B 118 7139 3265 7137 -1021 -451 184 B N
ATOM 4226 CA GLU B 118 7.893 14.482 446.597 1.00 47.29 B C
ANISOU 4226 CA GLU B 118 7308 3458 7202 -941 -540 295 B C
ATOM 4227 C GLU B 118 7.983 15.794 445.843 1.00 35.71 B C
ANISOU 4227 C GLU B 118 5920 1972 5675 -1099 -588 430 B C
ATOM 4228 O GLU B 118 9.026 16.434 445.867 1.00 59.07 B O
ANISOU 4228 O GLU B 118 8865 4896 8682 -1206 -541 427 B O
ATOM 4229 CB GLU B 118 7.428 14.716 448.037 1.00 51.20 B C
ANISOU 4229 CB GLU B 118 7705 4005 7742 -734 -549 277 B C
ATOM 4230 CG GLU B 118 7.266 13.453 448.859 1.00 44.38 B C
ANISOU 4230 CG GLU B 118 6781 3179 6904 -575 -496 178 B C
ATOM 4231 CD GLU B 118 6.701 13.714 450.262 1.00 51.42 B C
ANISOU 4231 CD GLU B 118 7610 4142 7787 -410 -498 180 B C
ATOM 4232 OE1 GLU B 118 5.802 14.575 450.403 1.00 69.97 B O
ANISOU 4232 OE1 GLU B 118 9965 6517 10106 -389 -527 250 B O
ATOM 4233 OE2 GLU B 118 7.136 13.049 451.228 1.00 40.57 B O1-
ANISOU 4233 OE2 GLU B 118 6188 2790 6436 -310 -469 116 B O1-
ATOM 4234 N ARG B 119 6.919 16.164 445.131 1.00 50.46 B N
ANISOU 4234 N ARG B 119 7873 3858 7442 -1127 -684 556 B N
ATOM 4235 CA ARG B 119 6.845 17.513 444.589 1.00 39.95 B C
ANISOU 4235 CA ARG B 119 6611 2504 6064 -1230 -734 712 B C
ATOM 4236 C ARG B 119 6.756 18.497 445.738 1.00 43.15 B C
ANISOU 4236 C ARG B 119 6915 2894 6585 -1088 -716 708 B C
ATOM 4237 O ARG B 119 6.223 18.194 446.808 1.00 54.84 B O
ANISOU 4237 O ARG B 119 8306 4410 8122 -907 -704 632 B O
ATOM 4238 CB ARG B 119 5.634 17.681 443.667 1.00 54.47 B C
ANISOU 4238 CB ARG B 119 8557 4361 7778 -1273 -873 862 B C
ATOM 4239 CG ARG B 119 5.712 16.882 442.390 1.00 50.00 B C
ANISOU 4239 CG ARG B 119 8158 3815 7025 -1483 -899 881 B C
ATOM 4240 CD ARG B 119 4.670 17.326 441.408 1.00 50.42 B C
ANISOU 4240 CD ARG B 119 8343 3888 6925 -1576 -1070 1074 B C
ATOM 4241 NE ARG B 119 4.496 16.378 440.309 1.00 66.93 B N
ANISOU 4241 NE ARG B 119 10617 6018 8795 -1784 -1111 1069 B N
ATOM 4242 CZ ARG B 119 3.771 15.260 440.385 1.00 84.86 B C
ANISOU 4242 CZ ARG B 119 12883 8298 11061 -1734 -1163 971 B C
ATOM 4243 NH1 ARG B 119 3.148 14.926 441.517 1.00 75.18 B N1+
ANISOU 4243 NH1 ARG B 119 11466 7058 10041 -1470 -1171 885 B N1+
ATOM 4244 NH2 ARG B 119 3.663 14.472 439.322 1.00 88.16 B N
ANISOU 4244 NH2 ARG B 119 13500 8750 11248 -1973 -1182 946 B N
ATOM 4245 N TYR B 120 7.288 19.685 445.510 1.00 65.56 B N
ANISOU 4245 N TYR B 120 9787 5680 9441 -1192 -693 787 B N
ATOM 4246 CA TYR B 120 7.512 20.621 446.596 1.00 67.15 B C
ANISOU 4246 CA TYR B 120 9920 5846 9750 -1111 -645 748 B C
ATOM 4247 C TYR B 120 7.494 22.033 446.033 1.00 70.20 B C
ANISOU 4247 C TYR B 120 10375 6156 10141 -1208 -643 891 B C
ATOM 4248 O TYR B 120 8.043 22.280 444.950 1.00 63.34 B O
ANISOU 4248 O TYR B 120 9591 5266 9209 -1392 -634 984 B O
ATOM 4249 CB TYR B 120 8.833 20.292 447.292 1.00 37.65 B C
ANISOU 4249 CB TYR B 120 6114 2103 6090 -1152 -575 606 B C
ATOM 4250 CG TYR B 120 9.501 21.453 447.943 1.00 38.46 B C
ANISOU 4250 CG TYR B 120 6194 2143 6277 -1200 -532 586 B C
ATOM 4251 CD1 TYR B 120 9.008 21.991 449.110 1.00 37.70 B C
ANISOU 4251 CD1 TYR B 120 6068 2037 6218 -1068 -533 544 B C
ATOM 4252 CD2 TYR B 120 10.643 22.013 447.385 1.00 54.89 B C
ANISOU 4252 CD2 TYR B 120 8286 4171 8397 -1404 -476 600 B C
ATOM 4253 CE1 TYR B 120 9.634 23.056 449.716 1.00 41.11 B C
ANISOU 4253 CE1 TYR B 120 6499 2397 6724 -1136 -493 509 B C
ATOM 4254 CE2 TYR B 120 11.268 23.088 447.969 1.00 51.26 B C
ANISOU 4254 CE2 TYR B 120 7805 3645 8028 -1469 -433 569 B C
ATOM 4255 CZ TYR B 120 10.759 23.608 449.139 1.00 49.93 B C
ANISOU 4255 CZ TYR B 120 7622 3456 7892 -1335 -450 519 B C
ATOM 4256 OH TYR B 120 11.384 24.678 449.749 1.00 67.74 B O
ANISOU 4256 OH TYR B 120 9873 5632 10232 -1421 -406 470 B O
ATOM 4257 N HIS B 121 6.839 22.943 446.762 1.00 73.72 B N
ANISOU 4257 N HIS B 121 10798 6558 10654 -1094 -630 909 B N
ATOM 4258 CA HIS B 121 6.825 24.370 446.456 1.00 63.09 B C
ANISOU 4258 CA HIS B 121 9510 5108 9353 -1158 -597 1027 B C
ATOM 4259 C HIS B 121 7.612 25.127 447.512 1.00 50.18 B C
ANISOU 4259 C HIS B 121 7838 3402 7825 -1170 -496 915 B C
ATOM 4260 O HIS B 121 7.450 24.873 448.708 1.00 45.90 B O
ANISOU 4260 O HIS B 121 7239 2888 7313 -1052 -477 788 B O
ATOM 4261 CB HIS B 121 5.399 24.936 446.432 1.00 71.76 B C
ANISOU 4261 CB HIS B 121 10626 6176 10463 -1030 -643 1136 B C
ATOM 4262 CG HIS B 121 4.633 24.617 445.190 1.00 99.84 B C
ANISOU 4262 CG HIS B 121 14244 9770 13919 -1069 -774 1299 B C
ATOM 4263 CD2 HIS B 121 3.758 23.618 444.911 1.00104.62 B C
ANISOU 4263 CD2 HIS B 121 14831 10462 14457 -1009 -885 1306 B C
ATOM 4264 ND1 HIS B 121 4.707 25.393 444.050 1.00114.88 B N
ANISOU 4264 ND1 HIS B 121 16256 11621 15772 -1200 -812 1490 B N
ATOM 4265 CE1 HIS B 121 3.921 24.878 443.119 1.00111.13 B C
ANISOU 4265 CE1 HIS B 121 15834 11208 15183 -1227 -961 1614 B C
ATOM 4266 NE2 HIS B 121 3.335 23.801 443.615 1.00111.60 B N
ANISOU 4266 NE2 HIS B 121 15816 11346 15240 -1117 -1010 1498 B N
ATOM 4267 N VAL B 122 8.436 26.075 447.067 1.00 52.43 B N
ANISOU 4267 N VAL B 122 8168 3596 8157 -1328 -431 968 B N
ATOM 4268 CA VAL B 122 9.108 26.985 447.990 1.00 60.48 B C
ANISOU 4268 CA VAL B 122 9169 4523 9287 -1369 -340 870 B C
ATOM 4269 C VAL B 122 8.089 27.943 448.596 1.00 65.87 B C
ANISOU 4269 C VAL B 122 9894 5113 10020 -1244 -297 902 B C
ATOM 4270 O VAL B 122 7.282 28.549 447.880 1.00 77.40 B O
ANISOU 4270 O VAL B 122 11420 6512 11477 -1216 -302 1061 B O
ATOM 4271 CB VAL B 122 10.219 27.762 447.270 1.00 54.22 B C
ANISOU 4271 CB VAL B 122 8406 3647 8547 -1588 -262 922 B C
ATOM 4272 CG1 VAL B 122 10.928 28.632 448.241 1.00 47.44 B C
ANISOU 4272 CG1 VAL B 122 7522 2693 7809 -1652 -177 799 B C
ATOM 4273 CG2 VAL B 122 11.187 26.834 446.593 1.00 46.66 B C
ANISOU 4273 CG2 VAL B 122 7411 2778 7540 -1730 -273 896 B C
ATOM 4274 N GLN B 123 8.149 28.121 449.914 1.00 60.09 B N
ANISOU 4274 N GLN B 123 9137 4361 9334 -1184 -252 757 B N
ATOM 4275 CA GLN B 123 7.175 28.934 450.637 1.00 65.84 B C
ANISOU 4275 CA GLN B 123 9919 4997 10102 -1072 -181 759 B C
ATOM 4276 C GLN B 123 7.874 29.611 451.814 1.00 74.39 B C
ANISOU 4276 C GLN B 123 11019 5990 11255 -1141 -103 610 B C
ATOM 4277 O GLN B 123 8.293 28.927 452.754 1.00 89.27 B O
ANISOU 4277 O GLN B 123 12847 7959 13113 -1123 -139 468 B O
ATOM 4278 CB GLN B 123 6.017 28.048 451.106 1.00 64.17 B C
ANISOU 4278 CB GLN B 123 9666 4878 9837 -895 -284 755 B C
ATOM 4279 CG GLN B 123 4.785 28.774 451.637 1.00 84.11 B C
ANISOU 4279 CG GLN B 123 12243 7292 12424 -786 -284 805 B C
ATOM 4280 CD GLN B 123 4.001 27.929 452.648 1.00 87.90 B C
ANISOU 4280 CD GLN B 123 12666 7853 12877 -646 -336 722 B C
ATOM 4281 NE2 GLN B 123 3.304 28.598 453.574 1.00 81.69 B N
ANISOU 4281 NE2 GLN B 123 11932 6951 12154 -582 -284 692 B N
ATOM 4282 OE1 GLN B 123 4.040 26.692 452.604 1.00 88.20 B O
ANISOU 4282 OE1 GLN B 123 12628 8044 12841 -603 -403 681 B O
ATOM 4283 N THR B 124 7.964 30.950 451.786 1.00 56.25 B N
ANISOU 4283 N THR B 124 8812 3513 9049 -1225 -1 643 B N
ATOM 4284 CA THR B 124 8.891 31.727 452.620 1.00 57.52 B C
ANISOU 4284 CA THR B 124 8999 3571 9285 -1363 98 496 B C
ATOM 4285 C THR B 124 8.123 32.602 453.613 1.00 55.14 B C
ANISOU 4285 C THR B 124 8796 3129 9027 -1301 142 458 B C
ATOM 4286 O THR B 124 7.522 33.608 453.220 1.00 60.61 B O
ANISOU 4286 O THR B 124 9594 3672 9764 -1290 201 569 B O
ATOM 4287 CB THR B 124 9.796 32.614 451.761 1.00 73.63 B C
ANISOU 4287 CB THR B 124 11061 5503 11411 -1555 165 555 B C
ATOM 4288 CG2 THR B 124 10.782 33.376 452.644 1.00 76.36 B C
ANISOU 4288 CG2 THR B 124 11397 5786 11830 -1710 221 384 B C
ATOM 4289 OG1 THR B 124 10.547 31.815 450.844 1.00 76.49 B O
ANISOU 4289 OG1 THR B 124 11340 5978 11745 -1641 84 602 B O
ATOM 4290 N SER B 125 8.150 32.242 454.894 1.00 48.71 B N
ANISOU 4290 N SER B 125 7959 2357 8192 -1265 117 304 B N
ATOM 4291 CA SER B 125 7.535 33.076 455.923 1.00 55.23 B C
ANISOU 4291 CA SER B 125 8885 3055 9045 -1229 181 240 B C
ATOM 4292 C SER B 125 8.020 32.617 457.291 1.00 66.55 B C
ANISOU 4292 C SER B 125 10269 4560 10457 -1250 160 45 B C
ATOM 4293 O SER B 125 8.733 31.619 457.415 1.00 86.50 B O
ANISOU 4293 O SER B 125 12691 7230 12944 -1272 77 -22 B O
ATOM 4294 CB SER B 125 6.013 33.026 455.872 1.00 49.95 B C
ANISOU 4294 CB SER B 125 8282 2335 8362 -1048 159 359 B C
ATOM 4295 OG SER B 125 5.557 31.896 456.565 1.00 49.09 B O
ANISOU 4295 OG SER B 125 8102 2348 8200 -927 91 303 B O
ATOM 4296 N ASN B 126 7.644 33.376 458.321 1.00 61.24 B N
ANISOU 4296 N ASN B 126 9688 3776 9802 -1252 238 -46 B N
ATOM 4297 CA ASN B 126 7.965 33.026 459.699 1.00 53.38 B C
ANISOU 4297 CA ASN B 126 8652 2830 8799 -1270 229 -229 B C
ATOM 4298 C ASN B 126 6.862 32.215 460.384 1.00 49.01 B C
ANISOU 4298 C ASN B 126 8103 2325 8194 -1085 200 -214 B C
ATOM 4299 O ASN B 126 6.867 32.082 461.617 1.00 49.18 B O
ANISOU 4299 O ASN B 126 8114 2352 8221 -1083 221 -354 B O
ATOM 4300 CB ASN B 126 8.289 34.283 460.512 1.00 59.39 B C
ANISOU 4300 CB ASN B 126 9494 3450 9621 -1404 353 -370 B C
ATOM 4301 CG ASN B 126 7.168 35.315 460.521 1.00 55.10 B C
ANISOU 4301 CG ASN B 126 9201 2723 9013 -1352 448 -283 B C
ATOM 4302 ND2 ASN B 126 7.494 36.502 460.970 1.00 57.79 B N
ANISOU 4302 ND2 ASN B 126 9761 2920 9275 -1508 501 -364 B N
ATOM 4303 OD1 ASN B 126 6.029 35.038 460.180 1.00 54.37 B O
ANISOU 4303 OD1 ASN B 126 9183 2616 8861 -1192 398 -143 B O
ATOM 4304 N TRP B 127 5.920 31.678 459.606 1.00 64.96 B N
ANISOU 4304 N TRP B 127 10124 4380 10179 -941 155 -54 B N
ATOM 4305 CA TRP B 127 4.814 30.914 460.173 1.00 55.76 B C
ANISOU 4305 CA TRP B 127 8955 3263 8968 -774 138 -35 B C
ATOM 4306 C TRP B 127 5.287 29.798 461.096 1.00 60.32 B C
ANISOU 4306 C TRP B 127 9442 3971 9505 -755 75 -151 B C
ATOM 4307 O TRP B 127 4.772 29.641 462.211 1.00 45.11 B O
ANISOU 4307 O TRP B 127 7536 2032 7571 -695 122 -229 B O
ATOM 4308 CB TRP B 127 3.945 30.328 459.061 1.00 45.46 B C
ANISOU 4308 CB TRP B 127 7616 2010 7647 -652 67 137 B C
ATOM 4309 CG TRP B 127 2.725 29.736 459.644 1.00 58.03 B C
ANISOU 4309 CG TRP B 127 9214 3629 9205 -498 66 151 B C
ATOM 4310 CD1 TRP B 127 1.603 30.405 460.001 1.00 46.29 B C
ANISOU 4310 CD1 TRP B 127 7844 2020 7724 -426 120 181 B C
ATOM 4311 CD2 TRP B 127 2.485 28.353 459.949 1.00 71.54 B C
ANISOU 4311 CD2 TRP B 127 10829 5493 10861 -403 3 135 B C
ATOM 4312 CE2 TRP B 127 1.184 28.271 460.495 1.00 66.71 B C
ANISOU 4312 CE2 TRP B 127 10265 4845 10236 -284 45 153 B C
ATOM 4313 CE3 TRP B 127 3.231 27.174 459.800 1.00 56.50 B C
ANISOU 4313 CE3 TRP B 127 8796 3780 8893 -405 -108 110 B C
ATOM 4314 NE1 TRP B 127 0.674 29.542 460.521 1.00 45.26 B N
ANISOU 4314 NE1 TRP B 127 7684 1958 7553 -299 104 179 B N
ATOM 4315 CZ2 TRP B 127 0.619 27.061 460.899 1.00 48.43 B C
ANISOU 4315 CZ2 TRP B 127 7884 2646 7873 -180 18 145 B C
ATOM 4316 CZ3 TRP B 127 2.669 25.986 460.199 1.00 48.09 B C
ANISOU 4316 CZ3 TRP B 127 7668 2835 7769 -293 -150 107 B C
ATOM 4317 CH2 TRP B 127 1.376 25.936 460.742 1.00 39.59 B C
ANISOU 4317 CH2 TRP B 127 6639 1701 6702 -187 -78 123 B C
ATOM 4318 N PHE B 128 6.275 29.015 460.651 1.00 43.40 B N
ANISOU 4318 N PHE B 128 7182 1889 7421 40 -196 -156 B N
ATOM 4319 CA PHE B 128 6.660 27.841 461.425 1.00 41.51 B C
ANISOU 4319 CA PHE B 128 6696 1842 7235 26 -250 -192 B C
ATOM 4320 C PHE B 128 7.394 28.242 462.688 1.00 42.12 B C
ANISOU 4320 C PHE B 128 6708 1898 7398 -51 -302 -298 B C
ATOM 4321 O PHE B 128 7.248 27.588 463.730 1.00 41.02 B O
ANISOU 4321 O PHE B 128 6370 1891 7325 29 -371 -354 B O
ATOM 4322 CB PHE B 128 7.516 26.882 460.605 1.00 40.66 B C
ANISOU 4322 CB PHE B 128 6506 1804 7138 -131 -184 -132 B C
ATOM 4323 CG PHE B 128 6.795 26.213 459.473 1.00 39.85 B C
ANISOU 4323 CG PHE B 128 6445 1748 6948 -58 -150 -41 B C
ATOM 4324 CD1 PHE B 128 6.732 26.804 458.232 1.00 41.20 B C
ANISOU 4324 CD1 PHE B 128 6868 1764 7022 -119 -63 27 B C
ATOM 4325 CD2 PHE B 128 6.208 24.979 459.649 1.00 37.97 B C
ANISOU 4325 CD2 PHE B 128 5995 1696 6736 56 -186 -27 B C
ATOM 4326 CE1 PHE B 128 6.093 26.188 457.188 1.00 40.70 B C
ANISOU 4326 CE1 PHE B 128 6838 1730 6895 -62 -28 105 B C
ATOM 4327 CE2 PHE B 128 5.564 24.346 458.601 1.00 44.84 B C
ANISOU 4327 CE2 PHE B 128 6910 2600 7528 103 -165 48 B C
ATOM 4328 CZ PHE B 128 5.509 24.966 457.367 1.00 46.54 B C
ANISOU 4328 CZ PHE B 128 7383 2657 7643 47 -99 112 B C
ATOM 4329 N GLU B 129 8.216 29.294 462.605 1.00 44.08 B N
ANISOU 4329 N GLU B 129 7126 1972 7650 -224 -264 -329 B N
ATOM 4330 CA GLU B 129 8.915 29.782 463.789 1.00 45.06 B C
ANISOU 4330 CA GLU B 129 7211 2057 7853 -317 -330 -441 B C
ATOM 4331 C GLU B 129 7.929 30.268 464.844 1.00 47.56 B C
ANISOU 4331 C GLU B 129 7565 2359 8148 -112 -411 -526 B C
ATOM 4332 O GLU B 129 8.040 29.886 466.015 1.00 53.41 B O
ANISOU 4332 O GLU B 129 8165 3186 8943 -81 -496 -611 B O
ATOM 4333 CB GLU B 129 9.873 30.910 463.403 1.00 47.47 B C
ANISOU 4333 CB GLU B 129 7719 2165 8155 -557 -260 -461 B C
ATOM 4334 CG GLU B 129 11.064 30.540 462.533 1.00 47.83 B C
ANISOU 4334 CG GLU B 129 7725 2220 8227 -812 -185 -404 B C
ATOM 4335 CD GLU B 129 10.735 30.192 461.081 1.00 56.34 B C
ANISOU 4335 CD GLU B 129 8925 3285 9198 -802 -86 -283 B C
ATOM 4336 OE1 GLU B 129 9.551 30.100 460.701 1.00 59.57 B O
ANISOU 4336 OE1 GLU B 129 9397 3699 9539 -586 -64 -236 B O
ATOM 4337 OE2 GLU B 129 11.688 30.008 460.298 1.00 68.32 B O1-
ANISOU 4337 OE2 GLU B 129 10450 4792 10716 -1021 -49 -233 B O1-
ATOM 4338 N ILE B 130 6.911 31.045 464.433 1.00 50.59 B N
ANISOU 4338 N ILE B 130 8114 2640 8466 43 -386 -504 B N
ATOM 4339 CA ILE B 130 5.881 31.495 465.373 1.00 46.82 B C
ANISOU 4339 CA ILE B 130 7657 2157 7975 258 -452 -589 B C
ATOM 4340 C ILE B 130 5.129 30.299 465.968 1.00 44.77 B C
ANISOU 4340 C ILE B 130 7177 2116 7718 426 -498 -598 B C
ATOM 4341 O ILE B 130 4.878 30.250 467.181 1.00 44.89 B O
ANISOU 4341 O ILE B 130 7137 2174 7745 508 -550 -705 B O
ATOM 4342 CB ILE B 130 4.938 32.505 464.692 1.00 48.48 B C
ANISOU 4342 CB ILE B 130 8035 2224 8159 400 -432 -552 B C
ATOM 4343 CG1 ILE B 130 5.716 33.765 464.329 1.00 54.01 B C
ANISOU 4343 CG1 ILE B 130 8939 2691 8891 226 -392 -565 B C
ATOM 4344 CG2 ILE B 130 3.792 32.879 465.602 1.00 49.20 B C
ANISOU 4344 CG2 ILE B 130 8122 2329 8244 644 -490 -643 B C
ATOM 4345 CD1 ILE B 130 4.926 34.805 463.579 1.00 52.92 B C
ANISOU 4345 CD1 ILE B 130 8959 2390 8756 349 -411 -516 B C
ATOM 4346 N GLN B 131 4.752 29.326 465.132 1.00 43.11 B N
ANISOU 4346 N GLN B 131 6848 2036 7494 468 -472 -493 B N
ATOM 4347 CA GLN B 131 4.191 28.074 465.645 1.00 41.23 B C
ANISOU 4347 CA GLN B 131 6381 2006 7277 578 -498 -496 B C
ATOM 4348 C GLN B 131 5.094 27.422 466.693 1.00 52.81 B C
ANISOU 4348 C GLN B 131 7699 3548 8819 472 -536 -562 B C
ATOM 4349 O GLN B 131 4.619 26.999 467.751 1.00 40.16 B O
ANISOU 4349 O GLN B 131 5998 2033 7230 578 -572 -636 B O
ATOM 4350 CB GLN B 131 3.959 27.090 464.495 1.00 57.27 B C
ANISOU 4350 CB GLN B 131 8322 4146 9291 572 -461 -375 B C
ATOM 4351 CG GLN B 131 2.747 27.377 463.659 1.00 55.84 B C
ANISOU 4351 CG GLN B 131 8214 3947 9054 727 -465 -317 B C
ATOM 4352 CD GLN B 131 1.610 27.907 464.481 1.00 53.09 B C
ANISOU 4352 CD GLN B 131 7855 3604 8712 936 -507 -399 B C
ATOM 4353 NE2 GLN B 131 1.309 29.209 464.320 1.00 52.77 B N
ANISOU 4353 NE2 GLN B 131 7998 3392 8660 1002 -518 -420 B N
ATOM 4354 OE1 GLN B 131 1.015 27.164 465.282 1.00 43.78 B O
ANISOU 4354 OE1 GLN B 131 6503 2574 7557 1036 -518 -448 B O
ATOM 4355 N PHE B 132 6.401 27.337 466.416 1.00 43.78 B N
ANISOU 4355 N PHE B 132 6532 2366 7735 261 -527 -542 B N
ATOM 4356 CA PHE B 132 7.322 26.699 467.354 1.00 43.30 B C
ANISOU 4356 CA PHE B 132 6300 2372 7781 159 -586 -600 B C
ATOM 4357 C PHE B 132 7.344 27.435 468.692 1.00 42.89 B C
ANISOU 4357 C PHE B 132 6336 2240 7721 178 -675 -741 B C
ATOM 4358 O PHE B 132 7.210 26.816 469.758 1.00 41.23 B O
ANISOU 4358 O PHE B 132 6021 2112 7535 241 -741 -808 B O
ATOM 4359 CB PHE B 132 8.747 26.672 466.779 1.00 49.78 B C
ANISOU 4359 CB PHE B 132 7066 3152 8695 -78 -558 -567 B C
ATOM 4360 CG PHE B 132 9.066 25.473 465.918 1.00 58.33 B C
ANISOU 4360 CG PHE B 132 7969 4360 9836 -114 -483 -465 B C
ATOM 4361 CD1 PHE B 132 9.104 24.182 466.454 1.00 58.47 B C
ANISOU 4361 CD1 PHE B 132 7755 4526 9936 -56 -511 -456 B C
ATOM 4362 CD2 PHE B 132 9.394 25.646 464.565 1.00 67.46 B C
ANISOU 4362 CD2 PHE B 132 9212 5464 10956 -216 -379 -384 B C
ATOM 4363 CE1 PHE B 132 9.421 23.083 465.638 1.00 60.55 B C
ANISOU 4363 CE1 PHE B 132 7867 4888 10252 -85 -428 -369 B C
ATOM 4364 CE2 PHE B 132 9.709 24.552 463.742 1.00 67.12 B C
ANISOU 4364 CE2 PHE B 132 9023 5524 10957 -250 -295 -306 B C
ATOM 4365 CZ PHE B 132 9.723 23.269 464.276 1.00 57.48 B C
ANISOU 4365 CZ PHE B 132 7559 4453 9826 -180 -316 -301 B C
ATOM 4366 N GLN B 133 7.497 28.763 468.656 1.00 43.59 B N
ANISOU 4366 N GLN B 133 6645 2155 7763 122 -675 -794 B N
ATOM 4367 CA GLN B 133 7.559 29.522 469.901 1.00 46.42 B C
ANISOU 4367 CA GLN B 133 7119 2423 8096 125 -757 -944 B C
ATOM 4368 C GLN B 133 6.275 29.363 470.702 1.00 49.18 B C
ANISOU 4368 C GLN B 133 7479 2834 8375 371 -759 -1013 B C
ATOM 4369 O GLN B 133 6.309 29.113 471.913 1.00 45.37 B O
ANISOU 4369 O GLN B 133 6974 2383 7880 396 -833 -1128 B O
ATOM 4370 CB GLN B 133 7.821 31.006 469.619 1.00 47.56 B C
ANISOU 4370 CB GLN B 133 7518 2356 8196 33 -731 -982 B C
ATOM 4371 CG GLN B 133 7.664 31.884 470.860 1.00 51.73 B C
ANISOU 4371 CG GLN B 133 8206 2779 8671 68 -799 -1146 B C
ATOM 4372 CD GLN B 133 8.402 33.191 470.750 1.00 83.75 B C
ANISOU 4372 CD GLN B 133 12470 6631 12722 -118 -795 -1198 B C
ATOM 4373 NE2 GLN B 133 7.788 34.260 471.246 1.00 81.07 B N
ANISOU 4373 NE2 GLN B 133 12337 6150 12316 -13 -786 -1299 B N
ATOM 4374 OE1 GLN B 133 9.516 33.248 470.224 1.00100.98 B O
ANISOU 4374 OE1 GLN B 133 14618 8780 14968 -359 -789 -1155 B O
ATOM 4375 N ARG B 134 5.129 29.496 470.031 1.00 45.70 B N
ANISOU 4375 N ARG B 134 7070 2410 7884 550 -680 -952 B N
ATOM 4376 CA ARG B 134 3.850 29.418 470.718 1.00 45.85 B C
ANISOU 4376 CA ARG B 134 7075 2492 7853 784 -657 -1025 B C
ATOM 4377 C ARG B 134 3.601 28.023 471.270 1.00 45.93 B C
ANISOU 4377 C ARG B 134 6871 2693 7889 836 -664 -1023 B C
ATOM 4378 O ARG B 134 3.171 27.870 472.418 1.00 50.61 B O
ANISOU 4378 O ARG B 134 7463 3319 8445 934 -674 -1146 B O
ATOM 4379 CB ARG B 134 2.734 29.835 469.766 1.00 59.11 B C
ANISOU 4379 CB ARG B 134 8795 4157 9508 948 -591 -950 B C
ATOM 4380 CG ARG B 134 1.327 29.534 470.264 1.00 74.48 B C
ANISOU 4380 CG ARG B 134 10647 6215 11437 1192 -551 -1005 B C
ATOM 4381 CD ARG B 134 0.279 30.318 469.487 1.00 85.73 B C
ANISOU 4381 CD ARG B 134 12139 7576 12858 1358 -521 -965 B C
ATOM 4382 NE ARG B 134 -1.081 29.943 469.867 1.00 92.72 B N
ANISOU 4382 NE ARG B 134 12881 8593 13753 1585 -478 -1013 B N
ATOM 4383 CZ ARG B 134 -1.768 28.960 469.295 1.00 92.14 B C
ANISOU 4383 CZ ARG B 134 12615 8689 13706 1645 -469 -926 B C
ATOM 4384 NH1 ARG B 134 -1.221 28.251 468.308 1.00 81.69 B N1+
ANISOU 4384 NH1 ARG B 134 11239 7413 12386 1503 -499 -788 B N1+
ATOM 4385 NH2 ARG B 134 -3.004 28.690 469.710 1.00 94.29 B N
ANISOU 4385 NH2 ARG B 134 12743 9081 14000 1841 -422 -987 B N
ATOM 4386 N ALA B 135 3.846 26.987 470.464 1.00 43.38 B N
ANISOU 4386 N ALA B 135 6379 2485 7617 773 -647 -889 B N
ATOM 4387 CA ALA B 135 3.636 25.630 470.952 1.00 39.80 B C
ANISOU 4387 CA ALA B 135 5731 2194 7195 811 -645 -874 B C
ATOM 4388 C ALA B 135 4.503 25.361 472.156 1.00 46.44 B C
ANISOU 4388 C ALA B 135 6567 3013 8066 720 -739 -973 B C
ATOM 4389 O ALA B 135 4.027 24.830 473.169 1.00 48.46 B O
ANISOU 4389 O ALA B 135 6794 3335 8284 812 -747 -1052 B O
ATOM 4390 CB ALA B 135 3.935 24.612 469.864 1.00 37.96 B C
ANISOU 4390 CB ALA B 135 5345 2065 7012 732 -610 -719 B C
ATOM 4391 N PHE B 136 5.775 25.762 472.078 1.00 56.23 B N
ANISOU 4391 N PHE B 136 7843 4160 9361 531 -816 -977 B N
ATOM 4392 CA PHE B 136 6.685 25.519 473.187 1.00 41.56 B C
ANISOU 4392 CA PHE B 136 5972 2295 7526 422 -946 -1065 B C
ATOM 4393 C PHE B 136 6.250 26.274 474.432 1.00 43.39 B C
ANISOU 4393 C PHE B 136 6391 2489 7605 490 -982 -1228 B C
ATOM 4394 O PHE B 136 6.258 25.711 475.533 1.00 47.13 B O
ANISOU 4394 O PHE B 136 6846 3110 7950 494 -1016 -1265 B O
ATOM 4395 CB PHE B 136 8.103 25.890 472.789 1.00 42.24 B C
ANISOU 4395 CB PHE B 136 6032 2291 7727 193 -1023 -1049 B C
ATOM 4396 CG PHE B 136 8.832 24.783 472.097 1.00 46.91 B C
ANISOU 4396 CG PHE B 136 6386 2995 8443 105 -1004 -919 B C
ATOM 4397 CD1 PHE B 136 8.127 23.845 471.331 1.00 40.86 B C
ANISOU 4397 CD1 PHE B 136 5509 2332 7683 219 -892 -800 B C
ATOM 4398 CD2 PHE B 136 10.212 24.667 472.203 1.00 41.63 B C
ANISOU 4398 CD2 PHE B 136 5594 2348 7877 -89 -1091 -918 B C
ATOM 4399 CE1 PHE B 136 8.795 22.818 470.662 1.00 40.45 B C
ANISOU 4399 CE1 PHE B 136 5262 2363 7746 148 -861 -692 B C
ATOM 4400 CE2 PHE B 136 10.887 23.641 471.546 1.00 40.61 B C
ANISOU 4400 CE2 PHE B 136 5234 2323 7875 -145 -1053 -810 B C
ATOM 4401 CZ PHE B 136 10.181 22.716 470.776 1.00 38.69 B C
ANISOU 4401 CZ PHE B 136 4915 2150 7636 -23 -932 -699 B C
ATOM 4402 N GLN B 137 5.860 27.543 474.284 1.00 44.81 B N
ANISOU 4402 N GLN B 137 6772 2496 7760 541 -956 -1312 B N
ATOM 4403 CA GLN B 137 5.414 28.304 475.445 1.00 46.82 B C
ANISOU 4403 CA GLN B 137 7233 2672 7884 625 -978 -1497 B C
ATOM 4404 C GLN B 137 4.176 27.665 476.063 1.00 46.48 B C
ANISOU 4404 C GLN B 137 7134 2795 7730 832 -866 -1530 B C
ATOM 4405 O GLN B 137 4.089 27.513 477.290 1.00 47.56 B O
ANISOU 4405 O GLN B 137 7342 3029 7701 835 -870 -1627 B O
ATOM 4406 CB GLN B 137 5.157 29.762 475.054 1.00 50.44 B C
ANISOU 4406 CB GLN B 137 7889 2975 8300 647 -916 -1530 B C
ATOM 4407 CG GLN B 137 4.771 30.706 476.205 1.00 59.75 B C
ANISOU 4407 CG GLN B 137 9307 4052 9344 722 -919 -1729 B C
ATOM 4408 CD GLN B 137 5.851 30.855 477.287 1.00 76.25 B C
ANISOU 4408 CD GLN B 137 11516 6089 11366 528 -1084 -1858 B C
ATOM 4409 NE2 GLN B 137 5.804 29.991 478.298 1.00 75.81 B N
ANISOU 4409 NE2 GLN B 137 11423 6177 11206 548 -1133 -1917 B N
ATOM 4410 OE1 GLN B 137 6.697 31.751 477.222 1.00 80.77 B O
ANISOU 4410 OE1 GLN B 137 12209 6530 11948 347 -1150 -1885 B O
ATOM 4411 N LYS B 138 3.230 27.235 475.226 1.00 45.15 B N
ANISOU 4411 N LYS B 138 6835 2683 7638 984 -761 -1443 B N
ATOM 4412 CA LYS B 138 1.996 26.676 475.762 1.00 45.16 B C
ANISOU 4412 CA LYS B 138 6754 2856 7548 1162 -632 -1478 B C
ATOM 4413 C LYS B 138 2.239 25.366 476.484 1.00 44.21 B C
ANISOU 4413 C LYS B 138 6505 2972 7321 1071 -620 -1410 B C
ATOM 4414 O LYS B 138 1.652 25.132 477.545 1.00 54.83 B O
ANISOU 4414 O LYS B 138 7892 4437 8506 1131 -540 -1495 B O
ATOM 4415 CB LYS B 138 0.938 26.515 474.671 1.00 44.24 B C
ANISOU 4415 CB LYS B 138 6503 2769 7539 1322 -542 -1391 B C
ATOM 4416 CG LYS B 138 0.339 27.840 474.301 1.00 45.96 B C
ANISOU 4416 CG LYS B 138 6855 2879 7730 1429 -493 -1424 B C
ATOM 4417 CD LYS B 138 -0.919 27.734 473.518 1.00 45.81 B C
ANISOU 4417 CD LYS B 138 6702 2955 7749 1600 -403 -1350 B C
ATOM 4418 CE LYS B 138 -1.502 29.140 473.314 1.00 76.79 B C
ANISOU 4418 CE LYS B 138 10780 6740 11658 1728 -373 -1401 B C
ATOM 4419 NZ LYS B 138 -1.729 29.954 474.589 1.00 50.57 B N1+
ANISOU 4419 NZ LYS B 138 7621 3332 8261 1823 -321 -1613 B N1+
ATOM 4420 N LEU B 139 3.112 24.513 475.953 1.00 42.53 B N
ANISOU 4420 N LEU B 139 6155 2820 7186 928 -693 -1261 B N
ATOM 4421 CA LEU B 139 3.431 23.284 476.674 1.00 41.95 B C
ANISOU 4421 CA LEU B 139 5991 2938 7011 849 -711 -1191 B C
ATOM 4422 C LEU B 139 4.189 23.562 477.972 1.00 43.70 B C
ANISOU 4422 C LEU B 139 6371 3160 7075 745 -828 -1289 B C
ATOM 4423 O LEU B 139 3.871 22.971 479.006 1.00 44.40 B O
ANISOU 4423 O LEU B 139 6505 3383 6980 755 -798 -1310 B O
ATOM 4424 CB LEU B 139 4.196 22.335 475.759 1.00 40.04 B C
ANISOU 4424 CB LEU B 139 5568 2739 6908 747 -762 -1022 B C
ATOM 4425 CG LEU B 139 3.322 21.896 474.579 1.00 38.49 B C
ANISOU 4425 CG LEU B 139 5238 2566 6819 845 -647 -927 B C
ATOM 4426 CD1 LEU B 139 4.116 21.327 473.405 1.00 37.45 B C
ANISOU 4426 CD1 LEU B 139 4978 2407 6843 747 -682 -789 B C
ATOM 4427 CD2 LEU B 139 2.277 20.902 475.051 1.00 38.15 B C
ANISOU 4427 CD2 LEU B 139 5113 2708 6675 925 -533 -898 B C
ATOM 4428 N ARG B 140 5.169 24.479 477.961 1.00 44.73 B N
ANISOU 4428 N ARG B 140 6603 3135 7257 631 -963 -1354 B N
ATOM 4429 CA ARG B 140 5.847 24.823 479.216 1.00 47.63 B C
ANISOU 4429 CA ARG B 140 7137 3496 7464 525 -1099 -1464 B C
ATOM 4430 C ARG B 140 4.885 25.360 480.258 1.00 48.60 B C
ANISOU 4430 C ARG B 140 7473 3620 7374 640 -998 -1627 B C
ATOM 4431 O ARG B 140 5.166 25.263 481.457 1.00 51.83 B O
ANISOU 4431 O ARG B 140 8028 4088 7579 575 -1074 -1700 B O
ATOM 4432 CB ARG B 140 6.974 25.846 479.025 1.00 48.66 B C
ANISOU 4432 CB ARG B 140 7349 3447 7694 366 -1255 -1530 B C
ATOM 4433 CG ARG B 140 8.311 25.203 478.781 1.00 60.10 B C
ANISOU 4433 CG ARG B 140 8615 4956 9264 191 -1416 -1422 B C
ATOM 4434 CD ARG B 140 9.467 26.171 478.787 1.00 66.11 B C
ANISOU 4434 CD ARG B 140 9438 5570 10111 -3 -1576 -1505 B C
ATOM 4435 NE ARG B 140 9.103 27.551 478.520 1.00 62.73 B N
ANISOU 4435 NE ARG B 140 9223 4918 9694 9 -1519 -1627 B N
ATOM 4436 CZ ARG B 140 8.936 28.036 477.298 1.00 71.37 B C
ANISOU 4436 CZ ARG B 140 10294 5871 10951 25 -1420 -1578 B C
ATOM 4437 NH1 ARG B 140 9.085 27.225 476.254 1.00 71.40 B N1+
ANISOU 4437 NH1 ARG B 140 10069 5954 11107 25 -1355 -1418 B N1+
ATOM 4438 NH2 ARG B 140 8.624 29.322 477.119 1.00 65.78 B N
ANISOU 4438 NH2 ARG B 140 9818 4932 10243 43 -1391 -1688 B N
ATOM 4439 N ASN B 141 3.772 25.962 479.831 1.00 57.18 B N
ANISOU 4439 N ASN B 141 8589 4636 8501 815 -834 -1694 B N
ATOM 4440 CA ASN B 141 2.813 26.481 480.798 1.00 50.77 B C
ANISOU 4440 CA ASN B 141 7956 3829 7505 947 -703 -1868 B C
ATOM 4441 C ASN B 141 1.955 25.404 481.448 1.00 50.61 B C
ANISOU 4441 C ASN B 141 7858 4040 7331 1011 -549 -1835 B C
ATOM 4442 O ASN B 141 1.356 25.670 482.495 1.00 52.86 B O
ANISOU 4442 O ASN B 141 8308 4363 7412 1071 -438 -1981 B O
ATOM 4443 CB ASN B 141 1.914 27.515 480.143 1.00 56.01 B C
ANISOU 4443 CB ASN B 141 8662 4333 8288 1138 -589 -1962 B C
ATOM 4444 CG ASN B 141 2.591 28.848 480.014 1.00 56.86 B C
ANISOU 4444 CG ASN B 141 8986 4174 8446 1078 -712 -2069 B C
ATOM 4445 ND2 ASN B 141 2.148 29.651 479.049 1.00 60.11 B N
ANISOU 4445 ND2 ASN B 141 9416 4404 9021 1204 -678 -2077 B N
ATOM 4446 OD1 ASN B 141 3.499 29.165 480.782 1.00 60.02 B O
ANISOU 4446 OD1 ASN B 141 9550 4522 8734 913 -847 -2143 B O
ATOM 4447 N CYS B 142 1.898 24.204 480.875 1.00 50.80 B N
ANISOU 4447 N CYS B 142 7658 4210 7436 986 -528 -1653 B N
ATOM 4448 CA CYS B 142 1.125 23.117 481.467 1.00 48.44 B C
ANISOU 4448 CA CYS B 142 7296 4119 6990 1011 -382 -1605 B C
ATOM 4449 C CYS B 142 1.770 22.607 482.742 1.00 49.74 B C
ANISOU 4449 C CYS B 142 7633 4364 6903 874 -478 -1608 B C
ATOM 4450 O CYS B 142 2.946 22.228 482.751 1.00 49.19 B O
ANISOU 4450 O CYS B 142 7558 4279 6855 738 -691 -1513 B O
ATOM 4451 CB CYS B 142 0.992 21.972 480.487 1.00 45.97 B C
ANISOU 4451 CB CYS B 142 6729 3907 6829 1000 -359 -1409 B C
ATOM 4452 SG CYS B 142 0.020 22.445 479.136 1.00 44.93 B S
ANISOU 4452 SG CYS B 142 6423 3715 6934 1166 -246 -1407 B S
ATOM 4453 N LYS B 143 0.987 22.577 483.816 1.00 52.74 B N
ANISOU 4453 N LYS B 143 8163 4834 7043 913 -318 -1718 B N
ATOM 4454 CA LYS B 143 1.473 22.114 485.099 1.00 59.08 B C
ANISOU 4454 CA LYS B 143 9182 5709 7555 786 -400 -1725 B C
ATOM 4455 C LYS B 143 0.888 20.767 485.475 1.00 59.48 B C
ANISOU 4455 C LYS B 143 9183 5950 7468 754 -266 -1599 B C
ATOM 4456 O LYS B 143 1.310 20.177 486.476 1.00 54.51 B O
ANISOU 4456 O LYS B 143 8741 5382 6588 640 -350 -1560 B O
ATOM 4457 CB LYS B 143 1.124 23.145 486.180 1.00 59.06 B C
ANISOU 4457 CB LYS B 143 9470 5647 7323 822 -317 -1960 B C
ATOM 4458 CG LYS B 143 1.546 24.554 485.823 1.00 66.38 B C
ANISOU 4458 CG LYS B 143 10480 6359 8380 860 -420 -2103 B C
ATOM 4459 CD LYS B 143 2.741 25.020 486.626 1.00 76.52 B C
ANISOU 4459 CD LYS B 143 12014 7549 9510 697 -680 -2171 B C
ATOM 4460 CE LYS B 143 3.350 26.245 485.971 1.00 85.92 B C
ANISOU 4460 CE LYS B 143 13230 8516 10902 688 -815 -2256 B C
ATOM 4461 NZ LYS B 143 2.304 27.262 485.649 1.00 80.94 B N1+
ANISOU 4461 NZ LYS B 143 12645 7765 10345 884 -599 -2416 B N1+
ATOM 4462 N THR B 144 -0.049 20.264 484.683 1.00 56.15 B N
ANISOU 4462 N THR B 144 8526 5610 7199 838 -76 -1530 B N
ATOM 4463 CA THR B 144 -0.842 19.095 485.015 1.00 51.88 B C
ANISOU 4463 CA THR B 144 7936 5241 6533 802 107 -1439 B C
ATOM 4464 C THR B 144 -0.907 18.188 483.811 1.00 49.17 B C
ANISOU 4464 C THR B 144 7316 4935 6431 801 92 -1254 B C
ATOM 4465 O THR B 144 -1.035 18.669 482.686 1.00 47.63 B O
ANISOU 4465 O THR B 144 6934 4670 6494 893 80 -1256 B O
ATOM 4466 CB THR B 144 -2.266 19.510 485.434 1.00 66.85 B C
ANISOU 4466 CB THR B 144 9827 7227 8345 910 430 -1605 B C
ATOM 4467 CG2 THR B 144 -3.233 18.330 485.419 1.00 78.97 B C
ANISOU 4467 CG2 THR B 144 11218 8945 9844 868 652 -1504 B C
ATOM 4468 OG1 THR B 144 -2.229 20.112 486.734 1.00 56.71 B O
ANISOU 4468 OG1 THR B 144 8851 5930 6768 885 479 -1772 B O
ATOM 4469 N HIS B 145 -0.869 16.880 484.067 1.00 59.89 B N
ANISOU 4469 N HIS B 145 8677 6391 7685 695 98 -1097 B N
ATOM 4470 CA HIS B 145 -1.146 15.866 483.055 1.00 46.76 B C
ANISOU 4470 CA HIS B 145 6784 4778 6206 682 133 -933 B C
ATOM 4471 C HIS B 145 -2.340 16.231 482.159 1.00 51.51 B C
ANISOU 4471 C HIS B 145 7147 5423 7003 800 331 -998 B C
ATOM 4472 O HIS B 145 -2.221 16.246 480.925 1.00 44.13 B O
ANISOU 4472 O HIS B 145 6022 4429 6314 848 259 -932 B O
ATOM 4473 CB HIS B 145 -1.359 14.543 483.784 1.00 47.62 B C
ANISOU 4473 CB HIS B 145 6999 4994 6102 557 203 -809 B C
ATOM 4474 CG HIS B 145 -1.815 13.433 482.906 1.00 46.00 B C
ANISOU 4474 CG HIS B 145 6596 4842 6041 523 277 -658 B C
ATOM 4475 CD2 HIS B 145 -3.053 12.937 482.675 1.00 46.27 B C
ANISOU 4475 CD2 HIS B 145 6491 4994 6096 508 519 -655 B C
ATOM 4476 ND1 HIS B 145 -0.947 12.689 482.136 1.00 44.07 B N
ANISOU 4476 ND1 HIS B 145 6275 4523 5947 493 89 -496 B N
ATOM 4477 CE1 HIS B 145 -1.633 11.784 481.461 1.00 54.37 B C
ANISOU 4477 CE1 HIS B 145 7431 5884 7344 460 210 -400 B C
ATOM 4478 NE2 HIS B 145 -2.913 11.915 481.767 1.00 65.58 B N
ANISOU 4478 NE2 HIS B 145 8802 7424 8690 458 461 -491 B N
ATOM 4479 N ASN B 146 -3.498 16.537 482.760 1.00 54.91 B N
ANISOU 4479 N ASN B 146 7583 5957 7325 851 578 -1133 B N
ATOM 4480 CA ASN B 146 -4.664 16.954 481.974 1.00 63.80 B C
ANISOU 4480 CA ASN B 146 8459 7132 8650 987 745 -1212 B C
ATOM 4481 C ASN B 146 -4.338 18.139 481.073 1.00 47.09 B C
ANISOU 4481 C ASN B 146 6281 4855 6755 1133 605 -1281 B C
ATOM 4482 O ASN B 146 -4.542 18.087 479.855 1.00 45.44 B O
ANISOU 4482 O ASN B 146 5872 4616 6776 1190 556 -1211 B O
ATOM 4483 CB ASN B 146 -5.843 17.331 482.885 1.00 70.61 B C
ANISOU 4483 CB ASN B 146 9339 8120 9371 1045 1032 -1390 B C
ATOM 4484 CG ASN B 146 -6.565 16.129 483.468 1.00 68.24 B C
ANISOU 4484 CG ASN B 146 9016 8003 8910 900 1244 -1322 B C
ATOM 4485 ND2 ASN B 146 -7.185 16.324 484.636 1.00 64.09 B N
ANISOU 4485 ND2 ASN B 146 8624 7575 8151 881 1480 -1461 B N
ATOM 4486 OD1 ASN B 146 -6.577 15.046 482.881 1.00 72.34 B O
ANISOU 4486 OD1 ASN B 146 9415 8566 9504 796 1211 -1151 B O
ATOM 4487 N ASP B 147 -3.834 19.226 481.657 1.00 48.31 B N
ANISOU 4487 N ASP B 147 6635 4892 6828 1182 537 -1417 B N
ATOM 4488 CA ASP B 147 -3.568 20.403 480.839 1.00 56.69 B C
ANISOU 4488 CA ASP B 147 7675 5778 8086 1308 419 -1485 B C
ATOM 4489 C ASP B 147 -2.597 20.076 479.716 1.00 53.33 B C
ANISOU 4489 C ASP B 147 7169 5256 7838 1236 206 -1316 B C
ATOM 4490 O ASP B 147 -2.821 20.472 478.568 1.00 44.08 B O
ANISOU 4490 O ASP B 147 5865 4006 6878 1326 171 -1292 B O
ATOM 4491 CB ASP B 147 -3.027 21.569 481.682 1.00 49.61 B C
ANISOU 4491 CB ASP B 147 7045 4747 7060 1332 357 -1652 B C
ATOM 4492 CG ASP B 147 -3.986 22.016 482.771 1.00 75.91 B C
ANISOU 4492 CG ASP B 147 10479 8153 10209 1421 591 -1850 B C
ATOM 4493 OD1 ASP B 147 -4.046 21.345 483.823 1.00 87.84 B O1-
ANISOU 4493 OD1 ASP B 147 12112 9791 11471 1308 688 -1849 B O1-
ATOM 4494 OD2 ASP B 147 -4.669 23.050 482.591 1.00 72.41 B O1-
ANISOU 4494 OD2 ASP B 147 10015 7634 9865 1608 683 -2009 B O1-
ATOM 4495 N LEU B 148 -1.558 19.284 480.000 1.00 44.24 B N
ANISOU 4495 N LEU B 148 6089 4115 6604 1078 71 -1193 B N
ATOM 4496 CA LEU B 148 -0.589 18.988 478.956 1.00 42.07 B C
ANISOU 4496 CA LEU B 148 5726 3752 6506 1015 -105 -1052 B C
ATOM 4497 C LEU B 148 -1.223 18.217 477.814 1.00 40.39 B C
ANISOU 4497 C LEU B 148 5292 3599 6454 1041 -36 -933 B C
ATOM 4498 O LEU B 148 -1.049 18.580 476.651 1.00 39.16 B O
ANISOU 4498 O LEU B 148 5049 3344 6485 1080 -102 -895 B O
ATOM 4499 CB LEU B 148 0.604 18.214 479.507 1.00 44.59 B C
ANISOU 4499 CB LEU B 148 6133 4083 6728 868 -263 -950 B C
ATOM 4500 CG LEU B 148 1.549 17.917 478.334 1.00 43.06 B C
ANISOU 4500 CG LEU B 148 5808 3805 6747 821 -405 -821 B C
ATOM 4501 CD1 LEU B 148 2.937 18.354 478.612 1.00 47.35 B C
ANISOU 4501 CD1 LEU B 148 6436 4251 7303 735 -610 -835 B C
ATOM 4502 CD2 LEU B 148 1.536 16.461 477.971 1.00 38.51 B C
ANISOU 4502 CD2 LEU B 148 5118 3318 6196 767 -386 -656 B C
ATOM 4503 N ILE B 149 -1.959 17.147 478.116 1.00 40.51 B N
ANISOU 4503 N ILE B 149 5236 3770 6387 1001 95 -872 B N
ATOM 4504 CA ILE B 149 -2.475 16.324 477.026 1.00 39.02 B C
ANISOU 4504 CA ILE B 149 4850 3631 6343 994 135 -756 B C
ATOM 4505 C ILE B 149 -3.539 17.072 476.221 1.00 45.83 B C
ANISOU 4505 C ILE B 149 5566 4489 7358 1141 210 -836 B C
ATOM 4506 O ILE B 149 -3.607 16.936 474.990 1.00 43.84 B O
ANISOU 4506 O ILE B 149 5195 4191 7270 1161 151 -758 B O
ATOM 4507 CB ILE B 149 -2.987 14.978 477.552 1.00 44.00 B C
ANISOU 4507 CB ILE B 149 5455 4413 6848 889 252 -670 B C
ATOM 4508 CG1 ILE B 149 -4.199 15.188 478.447 1.00 41.54 B C
ANISOU 4508 CG1 ILE B 149 5136 4237 6409 928 468 -796 B C
ATOM 4509 CG2 ILE B 149 -1.858 14.233 478.259 1.00 39.23 B C
ANISOU 4509 CG2 ILE B 149 5014 3784 6106 768 132 -572 B C
ATOM 4510 CD1 ILE B 149 -4.905 13.922 478.780 1.00 56.63 B C
ANISOU 4510 CD1 ILE B 149 6996 6298 8223 808 619 -714 B C
ATOM 4511 N ASN B 150 -4.364 17.897 476.873 1.00 41.26 B N
ANISOU 4511 N ASN B 150 5004 3947 6728 1258 331 -996 B N
ATOM 4512 CA ASN B 150 -5.336 18.650 476.087 1.00 41.83 B C
ANISOU 4512 CA ASN B 150 4927 3998 6968 1431 368 -1073 B C
ATOM 4513 C ASN B 150 -4.653 19.740 475.264 1.00 43.49 B C
ANISOU 4513 C ASN B 150 5227 3991 7305 1509 199 -1083 B C
ATOM 4514 O ASN B 150 -4.952 19.911 474.078 1.00 46.48 B O
ANISOU 4514 O ASN B 150 5502 4311 7846 1578 132 -1030 B O
ATOM 4515 CB ASN B 150 -6.433 19.197 476.999 1.00 44.47 B C
ANISOU 4515 CB ASN B 150 5231 4432 7233 1555 562 -1253 B C
ATOM 4516 CG ASN B 150 -7.348 18.089 477.550 1.00 45.37 B C
ANISOU 4516 CG ASN B 150 5204 4776 7259 1467 765 -1235 B C
ATOM 4517 ND2 ASN B 150 -7.516 18.051 478.870 1.00 47.26 B N
ANISOU 4517 ND2 ASN B 150 5567 5102 7289 1423 925 -1331 B N
ATOM 4518 OD1 ASN B 150 -7.877 17.275 476.794 1.00 44.55 B O
ANISOU 4518 OD1 ASN B 150 4902 4762 7262 1419 778 -1135 B O
ATOM 4519 N THR B 151 -3.694 20.449 475.858 1.00 41.55 B N
ANISOU 4519 N THR B 151 5190 3619 6978 1476 118 -1142 B N
ATOM 4520 CA THR B 151 -2.898 21.424 475.111 1.00 41.04 B C
ANISOU 4520 CA THR B 151 5234 3338 7023 1497 -37 -1140 B C
ATOM 4521 C THR B 151 -2.212 20.768 473.916 1.00 39.96 B C
ANISOU 4521 C THR B 151 5022 3159 7001 1389 -143 -966 B C
ATOM 4522 O THR B 151 -2.114 21.362 472.834 1.00 42.00 B O
ANISOU 4522 O THR B 151 5291 3278 7389 1435 -221 -935 B O
ATOM 4523 CB THR B 151 -1.858 22.064 476.035 1.00 41.89 B C
ANISOU 4523 CB THR B 151 5564 3342 7011 1418 -114 -1221 B C
ATOM 4524 CG2 THR B 151 -1.003 23.080 475.302 1.00 41.67 B C
ANISOU 4524 CG2 THR B 151 5653 3084 7095 1402 -259 -1223 B C
ATOM 4525 OG1 THR B 151 -2.523 22.721 477.113 1.00 52.38 B O
ANISOU 4525 OG1 THR B 151 6994 4692 8216 1524 -1 -1399 B O
ATOM 4526 N LEU B 152 -1.719 19.548 474.096 1.00 37.62 B N
ANISOU 4526 N LEU B 152 4673 2971 6650 1247 -144 -854 B N
ATOM 4527 CA LEU B 152 -1.080 18.858 472.991 1.00 49.56 B C
ANISOU 4527 CA LEU B 152 6116 4447 8268 1154 -219 -705 B C
ATOM 4528 C LEU B 152 -2.084 18.573 471.877 1.00 52.62 B C
ANISOU 4528 C LEU B 152 6361 4869 8763 1226 -180 -651 B C
ATOM 4529 O LEU B 152 -1.813 18.849 470.699 1.00 36.70 B O
ANISOU 4529 O LEU B 152 4352 2737 6855 1227 -253 -591 B O
ATOM 4530 CB LEU B 152 -0.442 17.570 473.505 1.00 34.98 B C
ANISOU 4530 CB LEU B 152 4249 2701 6341 1018 -225 -607 B C
ATOM 4531 CG LEU B 152 0.194 16.729 472.423 1.00 33.29 B C
ANISOU 4531 CG LEU B 152 3959 2456 6234 934 -275 -466 B C
ATOM 4532 CD1 LEU B 152 1.344 17.519 471.848 1.00 33.01 B C
ANISOU 4532 CD1 LEU B 152 3987 2259 6294 892 -380 -468 B C
ATOM 4533 CD2 LEU B 152 0.656 15.405 472.989 1.00 40.68 B C
ANISOU 4533 CD2 LEU B 152 4881 3483 7094 836 -277 -374 B C
ATOM 4534 N THR B 153 -3.274 18.086 472.239 1.00 35.96 B N
ANISOU 4534 N THR B 153 4128 2916 6617 1281 -66 -681 B N
ATOM 4535 CA THR B 153 -4.299 17.810 471.238 1.00 35.84 B C
ANISOU 4535 CA THR B 153 3954 2953 6709 1345 -50 -642 B C
ATOM 4536 C THR B 153 -4.690 19.073 470.452 1.00 54.85 B C
ANISOU 4536 C THR B 153 6390 5221 9231 1508 -130 -701 B C
ATOM 4537 O THR B 153 -4.774 19.051 469.210 1.00 50.94 B O
ANISOU 4537 O THR B 153 5886 4692 8778 1490 -211 -606 B O
ATOM 4538 CB THR B 153 -5.503 17.180 471.929 1.00 41.90 B C
ANISOU 4538 CB THR B 153 4567 3926 7426 1362 99 -690 B C
ATOM 4539 CG2 THR B 153 -6.453 16.697 470.933 1.00 59.52 B C
ANISOU 4539 CG2 THR B 153 6615 6232 9770 1385 93 -639 B C
ATOM 4540 OG1 THR B 153 -5.064 16.024 472.638 1.00 58.85 B O
ANISOU 4540 OG1 THR B 153 6745 6166 9450 1200 159 -618 B O
ATOM 4541 N ARG B 154 -4.908 20.196 471.147 1.00 40.11 B N
ANISOU 4541 N ARG B 154 4603 3292 7345 1640 -110 -841 B N
ATOM 4542 CA ARG B 154 -5.273 21.409 470.429 1.00 47.41 B C
ANISOU 4542 CA ARG B 154 5614 4130 8268 1749 -181 -850 B C
ATOM 4543 C ARG B 154 -4.133 21.892 469.548 1.00 40.71 B C
ANISOU 4543 C ARG B 154 4957 3137 7373 1622 -291 -740 B C
ATOM 4544 O ARG B 154 -4.358 22.300 468.403 1.00 38.38 B O
ANISOU 4544 O ARG B 154 4706 2804 7072 1633 -358 -659 B O
ATOM 4545 CB ARG B 154 -5.695 22.501 471.399 1.00 52.09 B C
ANISOU 4545 CB ARG B 154 6282 4678 8830 1907 -119 -1019 B C
ATOM 4546 CG ARG B 154 -7.012 22.248 472.106 1.00 73.43 B C
ANISOU 4546 CG ARG B 154 8778 7545 11576 2058 25 -1148 B C
ATOM 4547 CD ARG B 154 -7.317 23.430 473.015 1.00 96.76 B C
ANISOU 4547 CD ARG B 154 11850 10434 14478 2214 98 -1323 B C
ATOM 4548 NE ARG B 154 -8.375 23.178 473.989 1.00108.11 B N
ANISOU 4548 NE ARG B 154 13110 12040 15928 2336 293 -1488 B N
ATOM 4549 CZ ARG B 154 -8.811 24.091 474.855 1.00103.26 B C
ANISOU 4549 CZ ARG B 154 12574 11400 15259 2485 403 -1663 B C
ATOM 4550 NH1 ARG B 154 -8.273 25.310 474.865 1.00102.53 B N1+
ANISOU 4550 NH1 ARG B 154 12743 11103 15112 2529 317 -1687 B N1+
ATOM 4551 NH2 ARG B 154 -9.775 23.788 475.716 1.00 96.62 B N
ANISOU 4551 NH2 ARG B 154 11556 10740 14414 2574 621 -1817 B N
ATOM 4552 N LEU B 155 -2.901 21.868 470.063 1.00 43.66 B N
ANISOU 4552 N LEU B 155 5441 3428 7718 1498 -310 -745 B N
ATOM 4553 CA LEU B 155 -1.758 22.302 469.260 1.00 36.80 B C
ANISOU 4553 CA LEU B 155 4718 2443 6822 1359 -384 -656 B C
ATOM 4554 C LEU B 155 -1.621 21.473 467.986 1.00 61.52 B C
ANISOU 4554 C LEU B 155 7785 5628 9961 1257 -402 -510 B C
ATOM 4555 O LEU B 155 -1.523 22.031 466.884 1.00 35.44 B O
ANISOU 4555 O LEU B 155 4581 2253 6630 1235 -442 -445 B O
ATOM 4556 CB LEU B 155 -0.470 22.224 470.081 1.00 43.50 B C
ANISOU 4556 CB LEU B 155 5634 3223 7670 1235 -410 -692 B C
ATOM 4557 CG LEU B 155 -0.183 23.311 471.114 1.00 42.37 B C
ANISOU 4557 CG LEU B 155 5644 2957 7496 1277 -432 -839 B C
ATOM 4558 CD1 LEU B 155 0.963 22.916 472.014 1.00 37.84 B C
ANISOU 4558 CD1 LEU B 155 5096 2343 6939 1155 -489 -881 B C
ATOM 4559 CD2 LEU B 155 0.093 24.643 470.429 1.00 46.92 B C
ANISOU 4559 CD2 LEU B 155 6397 3387 8044 1262 -469 -828 B C
ATOM 4560 N ILE B 156 -1.631 20.136 468.119 1.00 34.07 B N
ANISOU 4560 N ILE B 156 4165 2262 6519 1198 -367 -462 B N
ATOM 4561 CA ILE B 156 -1.500 19.264 466.955 1.00 43.00 B C
ANISOU 4561 CA ILE B 156 5250 3436 7652 1100 -375 -339 B C
ATOM 4562 C ILE B 156 -2.623 19.522 465.948 1.00 52.50 B C
ANISOU 4562 C ILE B 156 6436 4658 8855 1190 -411 -313 B C
ATOM 4563 O ILE B 156 -2.381 19.616 464.737 1.00 33.11 B O
ANISOU 4563 O ILE B 156 4064 2149 6367 1130 -451 -234 B O
ATOM 4564 CB ILE B 156 -1.482 17.787 467.393 1.00 31.76 B C
ANISOU 4564 CB ILE B 156 3687 2111 6271 1042 -326 -301 B C
ATOM 4565 CG1 ILE B 156 -0.272 17.480 468.274 1.00 40.26 B C
ANISOU 4565 CG1 ILE B 156 4791 3152 7354 957 -326 -308 B C
ATOM 4566 CG2 ILE B 156 -1.396 16.891 466.171 1.00 30.68 B C
ANISOU 4566 CG2 ILE B 156 3524 2002 6131 946 -329 -190 B C
ATOM 4567 CD1 ILE B 156 1.086 17.672 467.604 1.00 36.41 B C
ANISOU 4567 CD1 ILE B 156 4382 2597 6855 825 -357 -252 B C
ATOM 4568 N GLN B 157 -3.866 19.674 466.428 1.00 34.61 B N
ANISOU 4568 N GLN B 157 4057 2464 6631 1342 -399 -386 B N
ATOM 4569 CA GLN B 157 -4.960 19.902 465.489 1.00 43.58 B C
ANISOU 4569 CA GLN B 157 5145 3623 7792 1440 -463 -364 B C
ATOM 4570 C GLN B 157 -4.802 21.223 464.753 1.00 53.98 B C
ANISOU 4570 C GLN B 157 6657 4799 9055 1490 -537 -348 B C
ATOM 4571 O GLN B 157 -5.064 21.302 463.545 1.00 56.50 B O
ANISOU 4571 O GLN B 157 7030 5076 9363 1487 -617 -272 B O
ATOM 4572 CB GLN B 157 -6.302 19.849 466.202 1.00 42.46 B C
ANISOU 4572 CB GLN B 157 4803 3605 7724 1599 -423 -461 B C
ATOM 4573 CG GLN B 157 -7.463 20.265 465.324 1.00 38.59 B C
ANISOU 4573 CG GLN B 157 4244 3140 7278 1728 -515 -454 B C
ATOM 4574 CD GLN B 157 -8.764 19.680 465.822 1.00 49.83 B C
ANISOU 4574 CD GLN B 157 5381 4746 8805 1824 -462 -528 B C
ATOM 4575 NE2 GLN B 157 -9.329 18.742 465.062 1.00 39.80 B N
ANISOU 4575 NE2 GLN B 157 3959 3558 7604 1770 -517 -468 B N
ATOM 4576 OE1 GLN B 157 -9.238 20.036 466.902 1.00 59.34 B O
ANISOU 4576 OE1 GLN B 157 6496 6019 10031 1934 -358 -648 B O
ATOM 4577 N GLU B 158 -4.418 22.284 465.469 1.00 53.90 B N
ANISOU 4577 N GLU B 158 6769 4697 9015 1540 -515 -420 B N
ATOM 4578 CA GLU B 158 -4.237 23.577 464.819 1.00 44.93 B C
ANISOU 4578 CA GLU B 158 5837 3399 7835 1579 -572 -400 B C
ATOM 4579 C GLU B 158 -3.074 23.565 463.835 1.00 44.96 B C
ANISOU 4579 C GLU B 158 6001 3300 7782 1399 -586 -299 B C
ATOM 4580 O GLU B 158 -3.159 24.168 462.766 1.00 38.56 B O
ANISOU 4580 O GLU B 158 5328 2384 6939 1408 -641 -235 B O
ATOM 4581 CB GLU B 158 -4.085 24.667 465.868 1.00 48.88 B C
ANISOU 4581 CB GLU B 158 6436 3809 8325 1660 -536 -511 B C
ATOM 4582 CG GLU B 158 -5.443 24.961 466.482 1.00 77.59 B C
ANISOU 4582 CG GLU B 158 9942 7523 12014 1879 -516 -610 B C
ATOM 4583 CD GLU B 158 -5.378 25.808 467.725 1.00 93.48 B C
ANISOU 4583 CD GLU B 158 12033 9470 14017 1967 -450 -748 B C
ATOM 4584 OE1 GLU B 158 -4.250 26.035 468.223 1.00 93.93 B O
ANISOU 4584 OE1 GLU B 158 12228 9431 14029 1841 -437 -771 B O
ATOM 4585 OE2 GLU B 158 -6.459 26.263 468.181 1.00 87.08 B O1-
ANISOU 4585 OE2 GLU B 158 11141 8698 13247 2161 -414 -842 B O1-
ATOM 4586 N ILE B 159 -1.996 22.854 464.145 1.00 36.15 B N
ANISOU 4586 N ILE B 159 4863 2213 6658 1239 -533 -282 B N
ATOM 4587 CA ILE B 159 -0.869 22.826 463.223 1.00 35.46 B C
ANISOU 4587 CA ILE B 159 4902 2042 6528 1072 -520 -201 B C
ATOM 4588 C ILE B 159 -1.219 22.025 461.982 1.00 34.81 B C
ANISOU 4588 C ILE B 159 4798 2001 6430 1036 -540 -108 B C
ATOM 4589 O ILE B 159 -1.064 22.507 460.855 1.00 38.07 B O
ANISOU 4589 O ILE B 159 5372 2303 6791 1002 -561 -45 B O
ATOM 4590 CB ILE B 159 0.370 22.253 463.924 1.00 53.51 B C
ANISOU 4590 CB ILE B 159 7133 4359 8840 927 -467 -218 B C
ATOM 4591 CG1 ILE B 159 0.741 23.134 465.120 1.00 54.30 B C
ANISOU 4591 CG1 ILE B 159 7287 4389 8957 953 -473 -319 B C
ATOM 4592 CG2 ILE B 159 1.511 22.061 462.931 1.00 46.62 B C
ANISOU 4592 CG2 ILE B 159 6342 3427 7944 757 -430 -143 B C
ATOM 4593 CD1 ILE B 159 2.000 22.716 465.825 1.00 49.00 B C
ANISOU 4593 CD1 ILE B 159 6564 3723 8330 815 -458 -341 B C
ATOM 4594 N SER B 160 -1.707 20.791 462.170 1.00 33.76 B N
ANISOU 4594 N SER B 160 4481 2008 6338 1038 -532 -100 B N
ATOM 4595 CA SER B 160 -1.974 19.889 461.055 1.00 37.70 B C
ANISOU 4595 CA SER B 160 4960 2536 6829 984 -552 -21 B C
ATOM 4596 C SER B 160 -3.275 20.213 460.327 1.00 48.85 B C
ANISOU 4596 C SER B 160 6373 3934 8256 1117 -665 -5 B C
ATOM 4597 O SER B 160 -3.418 19.892 459.139 1.00 52.82 B O
ANISOU 4597 O SER B 160 6948 4391 8728 1074 -717 68 B O
ATOM 4598 CB SER B 160 -2.073 18.458 461.549 1.00 31.86 B C
ANISOU 4598 CB SER B 160 4032 1929 6145 934 -506 -18 B C
ATOM 4599 OG SER B 160 -3.324 18.317 462.211 1.00 38.58 B O
ANISOU 4599 OG SER B 160 4722 2870 7067 1067 -540 -72 B O
ATOM 4600 N GLY B 161 -4.250 20.792 461.016 1.00 48.06 B N
ANISOU 4600 N GLY B 161 6182 3873 8207 1282 -709 -75 B N
ATOM 4601 CA GLY B 161 -5.500 21.059 460.351 1.00 37.31 B C
ANISOU 4601 CA GLY B 161 4779 2515 6883 1422 -835 -66 B C
ATOM 4602 C GLY B 161 -6.402 19.860 460.215 1.00 55.48 B C
ANISOU 4602 C GLY B 161 6859 4950 9270 1432 -879 -61 B C
ATOM 4603 O GLY B 161 -7.399 19.937 459.484 1.00 52.87 B O
ANISOU 4603 O GLY B 161 6480 4627 8981 1528 -1016 -44 B O
ATOM 4604 N TYR B 162 -6.087 18.762 460.899 1.00 47.13 B N
ANISOU 4604 N TYR B 162 5667 3991 8250 1335 -778 -74 B N
ATOM 4605 CA TYR B 162 -6.862 17.542 460.765 1.00 44.04 B C
ANISOU 4605 CA TYR B 162 5073 3706 7955 1315 -804 -62 B C
ATOM 4606 C TYR B 162 -8.201 17.676 461.479 1.00 36.93 B C
ANISOU 4606 C TYR B 162 3926 2943 7161 1475 -821 -153 B C
ATOM 4607 O TYR B 162 -8.324 18.367 462.490 1.00 61.55 B O
ANISOU 4607 O TYR B 162 7011 6098 10277 1573 -747 -239 B O
ATOM 4608 CB TYR B 162 -6.057 16.359 461.304 1.00 41.62 B C
ANISOU 4608 CB TYR B 162 4722 3438 7655 1162 -676 -39 B C
ATOM 4609 CG TYR B 162 -5.188 15.733 460.248 1.00 41.08 B C
ANISOU 4609 CG TYR B 162 4806 3281 7522 1007 -674 54 B C
ATOM 4610 CD1 TYR B 162 -4.076 16.393 459.750 1.00 53.30 B C
ANISOU 4610 CD1 TYR B 162 6571 4727 8955 939 -642 85 B C
ATOM 4611 CD2 TYR B 162 -5.518 14.506 459.703 1.00 31.95 B C
ANISOU 4611 CD2 TYR B 162 3578 2137 6424 929 -695 104 B C
ATOM 4612 CE1 TYR B 162 -3.284 15.815 458.764 1.00 53.37 B C
ANISOU 4612 CE1 TYR B 162 6712 4671 8896 801 -606 154 B C
ATOM 4613 CE2 TYR B 162 -4.741 13.922 458.717 1.00 32.64 B C
ANISOU 4613 CE2 TYR B 162 3826 2139 6436 791 -673 176 B C
ATOM 4614 CZ TYR B 162 -3.623 14.580 458.252 1.00 50.90 B C
ANISOU 4614 CZ TYR B 162 6342 4376 8621 733 -618 195 B C
ATOM 4615 OH TYR B 162 -2.854 14.004 457.268 1.00 50.27 B O
ANISOU 4615 OH TYR B 162 6412 4231 8458 604 -562 248 B O
ATOM 4616 N ASP B 163 -9.228 17.033 460.915 1.00 61.47 B N
ANISOU 4616 N ASP B 163 6856 6131 10367 1500 -921 -142 B N
ATOM 4617 CA ASP B 163 -10.581 17.199 461.448 1.00 67.97 B C
ANISOU 4617 CA ASP B 163 7407 7118 11299 1649 -935 -236 B C
ATOM 4618 C ASP B 163 -10.712 16.648 462.868 1.00 70.64 B C
ANISOU 4618 C ASP B 163 7546 7601 11691 1630 -740 -320 B C
ATOM 4619 O ASP B 163 -11.481 17.199 463.661 1.00 41.32 B O
ANISOU 4619 O ASP B 163 3685 3998 8015 1765 -675 -426 B O
ATOM 4620 CB ASP B 163 -11.607 16.525 460.523 1.00 78.56 B C
ANISOU 4620 CB ASP B 163 8567 8539 12745 1647 -1096 -206 B C
ATOM 4621 CG ASP B 163 -11.942 17.354 459.282 1.00 70.05 B C
ANISOU 4621 CG ASP B 163 7639 7351 11625 1743 -1320 -156 B C
ATOM 4622 OD1 ASP B 163 -11.815 18.582 459.340 1.00 60.67 B O1-
ANISOU 4622 OD1 ASP B 163 6606 6076 10369 1864 -1333 -175 B O1-
ATOM 4623 OD2 ASP B 163 -12.343 16.776 458.248 1.00 62.41 B O1-
ANISOU 4623 OD2 ASP B 163 6647 6374 10693 1694 -1494 -95 B O1-
ATOM 4624 N ARG B 164 -9.954 15.593 463.217 1.00 37.69 B N
ANISOU 4624 N ARG B 164 3384 3420 7518 1470 -635 -274 B N
ATOM 4625 CA ARG B 164 -9.996 14.974 464.537 1.00 37.52 B C
ANISOU 4625 CA ARG B 164 3239 3542 7473 1401 -438 -329 B C
ATOM 4626 C ARG B 164 -8.583 14.596 464.950 1.00 42.17 B C
ANISOU 4626 C ARG B 164 4040 4031 7950 1265 -356 -268 B C
ATOM 4627 O ARG B 164 -7.782 14.152 464.123 1.00 48.50 B O
ANISOU 4627 O ARG B 164 4990 4722 8716 1155 -411 -170 B O
ATOM 4628 CB ARG B 164 -10.901 13.728 464.580 1.00 38.15 B C
ANISOU 4628 CB ARG B 164 3099 3827 7570 1259 -375 -316 B C
ATOM 4629 CG ARG B 164 -10.831 12.970 465.895 1.00 54.10 B C
ANISOU 4629 CG ARG B 164 5068 5979 9510 1135 -159 -343 B C
ATOM 4630 CD ARG B 164 -11.901 11.911 466.041 1.00 53.25 B C
ANISOU 4630 CD ARG B 164 4727 6076 9429 997 -75 -351 B C
ATOM 4631 NE ARG B 164 -11.782 10.842 465.058 1.00 69.89 B N
ANISOU 4631 NE ARG B 164 6884 8152 11518 817 -160 -242 B N
ATOM 4632 CZ ARG B 164 -12.686 9.878 464.888 1.00 75.74 B C
ANISOU 4632 CZ ARG B 164 7448 9040 12291 665 -134 -236 B C
ATOM 4633 NH1 ARG B 164 -13.792 9.857 465.626 1.00 77.11 B N1+
ANISOU 4633 NH1 ARG B 164 7351 9419 12529 667 -13 -330 B N1+
ATOM 4634 NH2 ARG B 164 -12.496 8.941 463.973 1.00 70.35 B N
ANISOU 4634 NH2 ARG B 164 6856 8298 11577 500 -218 -144 B N
ATOM 4635 N VAL B 165 -8.278 14.815 466.228 1.00 41.04 B N
ANISOU 4635 N VAL B 165 3912 3927 7754 1282 -228 -335 B N
ATOM 4636 CA VAL B 165 -6.972 14.544 466.816 1.00 34.00 B C
ANISOU 4636 CA VAL B 165 3195 2958 6766 1176 -172 -294 B C
ATOM 4637 C VAL B 165 -7.162 13.918 468.190 1.00 41.22 B C
ANISOU 4637 C VAL B 165 4050 4022 7592 1107 -14 -333 B C
ATOM 4638 O VAL B 165 -7.920 14.440 469.014 1.00 36.09 B O
ANISOU 4638 O VAL B 165 3304 3469 6939 1205 71 -445 B O
ATOM 4639 CB VAL B 165 -6.135 15.828 466.928 1.00 40.49 B C
ANISOU 4639 CB VAL B 165 4186 3609 7590 1277 -230 -338 B C
ATOM 4640 CG1 VAL B 165 -4.923 15.580 467.801 1.00 34.35 B C
ANISOU 4640 CG1 VAL B 165 3533 2796 6723 1176 -176 -324 B C
ATOM 4641 CG2 VAL B 165 -5.707 16.291 465.533 1.00 33.34 B C
ANISOU 4641 CG2 VAL B 165 3427 2583 6660 1250 -356 -260 B C
ATOM 4642 N MET B 166 -6.447 12.822 468.456 1.00 33.35 B N
ANISOU 4642 N MET B 166 3129 3030 6513 946 28 -245 B N
ATOM 4643 CA MET B 166 -6.612 12.077 469.695 1.00 33.97 B C
ANISOU 4643 CA MET B 166 3195 3233 6480 855 165 -254 B C
ATOM 4644 C MET B 166 -5.268 11.700 470.300 1.00 32.93 B C
ANISOU 4644 C MET B 166 3247 3014 6250 777 148 -193 B C
ATOM 4645 O MET B 166 -4.250 11.591 469.617 1.00 31.77 B O
ANISOU 4645 O MET B 166 3191 2738 6144 752 53 -123 B O
ATOM 4646 CB MET B 166 -7.451 10.811 469.503 1.00 40.51 B C
ANISOU 4646 CB MET B 166 3903 4187 7303 715 238 -198 B C
ATOM 4647 CG MET B 166 -8.921 11.096 469.257 1.00 39.68 B C
ANISOU 4647 CG MET B 166 3561 4225 7290 776 277 -281 B C
ATOM 4648 SD MET B 166 -9.727 9.863 468.240 1.00 60.70 B S
ANISOU 4648 SD MET B 166 6085 6963 10014 616 249 -203 B S
ATOM 4649 CE MET B 166 -8.697 9.872 466.770 1.00 61.11 B C
ANISOU 4649 CE MET B 166 6309 6803 10106 621 57 -102 B C
ATOM 4650 N ILE B 167 -5.288 11.484 471.606 1.00 33.86 B N
ANISOU 4650 N ILE B 167 3415 3211 6238 740 243 -223 B N
ATOM 4651 CA ILE B 167 -4.163 10.911 472.320 1.00 33.36 B C
ANISOU 4651 CA ILE B 167 3516 3093 6067 658 212 -155 B C
ATOM 4652 C ILE B 167 -4.589 9.503 472.705 1.00 43.79 B C
ANISOU 4652 C ILE B 167 4842 4499 7296 513 305 -70 B C
ATOM 4653 O ILE B 167 -5.536 9.308 473.477 1.00 41.92 B O
ANISOU 4653 O ILE B 167 4561 4397 6969 469 447 -115 B O
ATOM 4654 CB ILE B 167 -3.806 11.727 473.558 1.00 34.39 B C
ANISOU 4654 CB ILE B 167 3758 3228 6081 711 223 -246 B C
ATOM 4655 CG1 ILE B 167 -3.357 13.123 473.142 1.00 40.86 B C
ANISOU 4655 CG1 ILE B 167 4596 3934 6994 836 127 -330 B C
ATOM 4656 CG2 ILE B 167 -2.733 11.009 474.333 1.00 35.92 B C
ANISOU 4656 CG2 ILE B 167 4113 3382 6155 623 163 -165 B C
ATOM 4657 CD1 ILE B 167 -2.060 13.142 472.444 1.00 36.44 B C
ANISOU 4657 CD1 ILE B 167 4100 3230 6515 809 -12 -257 B C
ATOM 4658 N TYR B 168 -3.913 8.518 472.144 1.00 32.76 B N
ANISOU 4658 N TYR B 168 3504 3018 5925 434 240 48 B N
ATOM 4659 CA TYR B 168 -4.196 7.121 472.413 1.00 38.30 B C
ANISOU 4659 CA TYR B 168 4254 3754 6545 290 309 143 B C
ATOM 4660 C TYR B 168 -3.110 6.582 473.338 1.00 33.44 B C
ANISOU 4660 C TYR B 168 3831 3065 5807 260 249 217 B C
ATOM 4661 O TYR B 168 -1.934 6.552 472.967 1.00 38.83 B O
ANISOU 4661 O TYR B 168 4570 3626 6557 307 121 262 B O
ATOM 4662 CB TYR B 168 -4.255 6.385 471.077 1.00 32.24 B C
ANISOU 4662 CB TYR B 168 3435 2921 5893 237 269 213 B C
ATOM 4663 CG TYR B 168 -4.670 4.958 471.148 1.00 48.40 B C
ANISOU 4663 CG TYR B 168 5533 4980 7878 77 338 303 B C
ATOM 4664 CD1 TYR B 168 -5.950 4.616 471.538 1.00 46.46 B C
ANISOU 4664 CD1 TYR B 168 5197 4878 7578 -31 474 277 B C
ATOM 4665 CD2 TYR B 168 -3.782 3.935 470.800 1.00 32.23 B C
ANISOU 4665 CD2 TYR B 168 3620 2791 5833 31 274 410 B C
ATOM 4666 CE1 TYR B 168 -6.343 3.293 471.590 1.00 52.35 B C
ANISOU 4666 CE1 TYR B 168 6008 5620 8263 -209 542 362 B C
ATOM 4667 CE2 TYR B 168 -4.165 2.632 470.852 1.00 33.00 B C
ANISOU 4667 CE2 TYR B 168 3798 2870 5871 -117 332 492 B C
ATOM 4668 CZ TYR B 168 -5.452 2.308 471.240 1.00 46.08 B C
ANISOU 4668 CZ TYR B 168 5383 4662 7462 -251 465 472 B C
ATOM 4669 OH TYR B 168 -5.850 0.989 471.299 1.00 48.05 B O
ANISOU 4669 OH TYR B 168 5730 4880 7646 -431 530 557 B O
ATOM 4670 N GLN B 169 -3.496 6.113 474.513 1.00 34.98 B N
ANISOU 4670 N GLN B 169 4129 3336 5826 177 340 233 B N
ATOM 4671 CA GLN B 169 -2.528 5.605 475.473 1.00 38.11 B C
ANISOU 4671 CA GLN B 169 4735 3663 6082 155 256 311 B C
ATOM 4672 C GLN B 169 -2.611 4.091 475.614 1.00 40.14 B C
ANISOU 4672 C GLN B 169 5119 3875 6257 21 287 448 B C
ATOM 4673 O GLN B 169 -3.694 3.531 475.844 1.00 38.71 B O
ANISOU 4673 O GLN B 169 4931 3783 5995 -109 446 459 B O
ATOM 4674 CB GLN B 169 -2.700 6.247 476.845 1.00 37.21 B C
ANISOU 4674 CB GLN B 169 4729 3633 5777 161 309 236 B C
ATOM 4675 CG GLN B 169 -1.578 5.863 477.739 1.00 37.89 B C
ANISOU 4675 CG GLN B 169 5034 3635 5727 157 162 314 B C
ATOM 4676 CD GLN B 169 -1.856 6.215 479.136 1.00 39.91 B C
ANISOU 4676 CD GLN B 169 5454 3970 5739 120 228 260 B C
ATOM 4677 NE2 GLN B 169 -0.912 5.911 480.030 1.00 40.91 B N
ANISOU 4677 NE2 GLN B 169 5801 4029 5714 114 73 329 B N
ATOM 4678 OE1 GLN B 169 -2.927 6.749 479.437 1.00 54.53 B O
ANISOU 4678 OE1 GLN B 169 7239 5946 7533 101 416 152 B O
ATOM 4679 N PHE B 170 -1.451 3.451 475.536 1.00 35.84 B N
ANISOU 4679 N PHE B 170 4693 3189 5736 54 136 547 B N
ATOM 4680 CA PHE B 170 -1.353 2.012 475.647 1.00 36.61 B C
ANISOU 4680 CA PHE B 170 4950 3196 5766 -44 132 685 B C
ATOM 4681 C PHE B 170 -1.394 1.584 477.104 1.00 38.73 B C
ANISOU 4681 C PHE B 170 5454 3480 5779 -120 146 746 B C
ATOM 4682 O PHE B 170 -0.843 2.261 477.979 1.00 39.35 B O
ANISOU 4682 O PHE B 170 5612 3581 5757 -52 58 710 B O
ATOM 4683 CB PHE B 170 -0.047 1.536 475.010 1.00 35.70 B C
ANISOU 4683 CB PHE B 170 4862 2913 5791 56 -39 755 B C
ATOM 4684 CG PHE B 170 -0.016 1.642 473.525 1.00 34.01 B C
ANISOU 4684 CG PHE B 170 4478 2655 5788 94 -27 719 B C
ATOM 4685 CD1 PHE B 170 -0.849 0.859 472.741 1.00 33.89 B C
ANISOU 4685 CD1 PHE B 170 4445 2628 5805 -15 77 748 B C
ATOM 4686 CD2 PHE B 170 0.855 2.516 472.907 1.00 32.77 B C
ANISOU 4686 CD2 PHE B 170 4201 2465 5785 218 -118 657 B C
ATOM 4687 CE1 PHE B 170 -0.819 0.949 471.365 1.00 32.56 B C
ANISOU 4687 CE1 PHE B 170 4157 2414 5802 12 78 714 B C
ATOM 4688 CE2 PHE B 170 0.882 2.618 471.528 1.00 31.46 B C
ANISOU 4688 CE2 PHE B 170 3916 2252 5783 239 -94 628 B C
ATOM 4689 CZ PHE B 170 0.044 1.827 470.758 1.00 31.35 B C
ANISOU 4689 CZ PHE B 170 3904 2226 5783 141 -1 657 B C
ATOM 4690 N ASP B 171 -2.052 0.460 477.358 1.00 40.04 B N
ANISOU 4690 N ASP B 171 5756 3630 5829 -278 254 840 B N
ATOM 4691 CA ASP B 171 -2.008 -0.209 478.651 1.00 43.28 B C
ANISOU 4691 CA ASP B 171 6458 4010 5977 -373 258 938 B C
ATOM 4692 C ASP B 171 -1.013 -1.371 478.582 1.00 42.72 B C
ANISOU 4692 C ASP B 171 6589 3729 5915 -338 79 1095 B C
ATOM 4693 O ASP B 171 -0.412 -1.620 477.534 1.00 41.24 B O
ANISOU 4693 O ASP B 171 6291 3435 5942 -241 -16 1108 B O
ATOM 4694 CB ASP B 171 -3.432 -0.631 479.077 1.00 44.04 B C
ANISOU 4694 CB ASP B 171 6588 4225 5920 -592 520 934 B C
ATOM 4695 CG ASP B 171 -3.869 -1.990 478.555 1.00 58.89 B C
ANISOU 4695 CG ASP B 171 8549 6006 7819 -753 586 1048 B C
ATOM 4696 OD1 ASP B 171 -3.244 -2.558 477.645 1.00 57.26 B O1-
ANISOU 4696 OD1 ASP B 171 8333 5649 7775 -685 458 1107 B O1-
ATOM 4697 OD2 ASP B 171 -4.891 -2.485 479.079 1.00 63.98 B O1-
ANISOU 4697 OD2 ASP B 171 9271 6727 8310 -963 789 1069 B O1-
ATOM 4698 N PRO B 172 -0.722 -2.036 479.704 1.00 44.92 B N
ANISOU 4698 N PRO B 172 7175 3931 5962 -390 13 1212 B N
ATOM 4699 CA PRO B 172 0.341 -3.061 479.674 1.00 48.02 B C
ANISOU 4699 CA PRO B 172 7757 4105 6383 -304 -200 1358 B C
ATOM 4700 C PRO B 172 0.095 -4.205 478.698 1.00 60.69 B C
ANISOU 4700 C PRO B 172 9375 5570 8114 -367 -141 1433 B C
ATOM 4701 O PRO B 172 1.062 -4.851 478.261 1.00 45.15 B O
ANISOU 4701 O PRO B 172 7460 3420 6275 -234 -311 1505 B O
ATOM 4702 CB PRO B 172 0.391 -3.542 481.124 1.00 48.44 B C
ANISOU 4702 CB PRO B 172 8174 4116 6115 -386 -252 1473 B C
ATOM 4703 CG PRO B 172 -0.056 -2.356 481.907 1.00 48.74 B C
ANISOU 4703 CG PRO B 172 8164 4352 6003 -419 -158 1348 B C
ATOM 4704 CD PRO B 172 -1.114 -1.714 481.089 1.00 47.05 B C
ANISOU 4704 CD PRO B 172 7642 4298 5935 -482 83 1206 B C
ATOM 4705 N GLU B 173 -1.161 -4.493 478.358 1.00 56.63 B N
ANISOU 4705 N GLU B 173 8813 5133 7571 -566 91 1409 B N
ATOM 4706 CA GLU B 173 -1.485 -5.563 477.422 1.00 45.23 B C
ANISOU 4706 CA GLU B 173 7395 3557 6232 -658 150 1466 B C
ATOM 4707 C GLU B 173 -1.564 -5.075 475.986 1.00 42.76 B C
ANISOU 4707 C GLU B 173 6770 3289 6186 -586 174 1350 B C
ATOM 4708 O GLU B 173 -1.940 -5.851 475.106 1.00 42.61 B O
ANISOU 4708 O GLU B 173 6754 3182 6255 -677 234 1369 B O
ATOM 4709 CB GLU B 173 -2.816 -6.218 477.806 1.00 65.43 B C
ANISOU 4709 CB GLU B 173 10073 6170 8617 -948 378 1505 B C
ATOM 4710 CG GLU B 173 -2.802 -6.889 479.163 1.00 77.04 B C
ANISOU 4710 CG GLU B 173 11920 7562 9790 -1063 380 1644 B C
ATOM 4711 CD GLU B 173 -3.004 -5.888 480.290 1.00 89.18 B C
ANISOU 4711 CD GLU B 173 13458 9290 11138 -1065 436 1579 B C
ATOM 4712 OE1 GLU B 173 -3.941 -5.061 480.192 1.00 83.98 B O
ANISOU 4712 OE1 GLU B 173 12550 8853 10504 -1140 631 1440 B O
ATOM 4713 OE2 GLU B 173 -2.226 -5.922 481.269 1.00 99.70 B O1-
ANISOU 4713 OE2 GLU B 173 15043 10544 12294 -983 276 1661 B O1-
ATOM 4714 N TRP B 174 -1.257 -3.798 475.748 1.00 48.92 B N
ANISOU 4714 N TRP B 174 7311 4198 7079 -442 131 1229 B N
ATOM 4715 CA TRP B 174 -1.243 -3.127 474.443 1.00 46.48 B C
ANISOU 4715 CA TRP B 174 6727 3933 6999 -358 138 1119 B C
ATOM 4716 C TRP B 174 -2.643 -2.867 473.902 1.00 38.55 B C
ANISOU 4716 C TRP B 174 5549 3082 6017 -511 317 1037 B C
ATOM 4717 O TRP B 174 -2.812 -2.597 472.720 1.00 37.15 B O
ANISOU 4717 O TRP B 174 5197 2914 6004 -484 322 971 B O
ATOM 4718 CB TRP B 174 -0.379 -3.880 473.423 1.00 40.93 B C
ANISOU 4718 CB TRP B 174 6057 3033 6462 -265 40 1163 B C
ATOM 4719 CG TRP B 174 1.059 -3.801 473.857 1.00 43.35 B C
ANISOU 4719 CG TRP B 174 6425 3235 6811 -67 -151 1203 B C
ATOM 4720 CD1 TRP B 174 1.804 -4.795 474.398 1.00 39.96 B C
ANISOU 4720 CD1 TRP B 174 6224 2629 6328 -11 -273 1324 B C
ATOM 4721 CD2 TRP B 174 1.884 -2.627 473.875 1.00 52.76 B C
ANISOU 4721 CD2 TRP B 174 7444 4500 8104 92 -254 1119 B C
ATOM 4722 CE2 TRP B 174 3.126 -3.000 474.409 1.00 38.30 B C
ANISOU 4722 CE2 TRP B 174 5715 2547 6292 235 -442 1189 B C
ATOM 4723 CE3 TRP B 174 1.691 -1.299 473.482 1.00 35.71 B C
ANISOU 4723 CE3 TRP B 174 5060 2485 6025 126 -214 992 B C
ATOM 4724 NE1 TRP B 174 3.049 -4.328 474.723 1.00 39.97 B N
ANISOU 4724 NE1 TRP B 174 6174 2605 6408 184 -457 1317 B N
ATOM 4725 CZ2 TRP B 174 4.173 -2.103 474.558 1.00 37.89 B C
ANISOU 4725 CZ2 TRP B 174 5523 2530 6342 386 -584 1130 B C
ATOM 4726 CZ3 TRP B 174 2.740 -0.412 473.624 1.00 43.25 B C
ANISOU 4726 CZ3 TRP B 174 5912 3453 7069 270 -345 940 B C
ATOM 4727 CH2 TRP B 174 3.963 -0.819 474.160 1.00 36.32 B C
ANISOU 4727 CH2 TRP B 174 5117 2469 6214 387 -525 1005 B C
ATOM 4728 N ASN B 175 -3.656 -2.955 474.753 1.00 40.16 B N
ANISOU 4728 N ASN B 175 5796 3408 6056 -677 465 1039 B N
ATOM 4729 CA ASN B 175 -4.932 -2.331 474.479 1.00 40.18 B C
ANISOU 4729 CA ASN B 175 5560 3612 6095 -773 623 927 B C
ATOM 4730 C ASN B 175 -4.774 -0.834 474.729 1.00 52.89 B C
ANISOU 4730 C ASN B 175 6998 5354 7742 -605 597 805 B C
ATOM 4731 O ASN B 175 -3.802 -0.388 475.352 1.00 45.70 B O
ANISOU 4731 O ASN B 175 6188 4395 6779 -472 482 815 B O
ATOM 4732 CB ASN B 175 -6.027 -2.915 475.366 1.00 49.94 B C
ANISOU 4732 CB ASN B 175 6883 4943 7148 -1010 818 958 B C
ATOM 4733 CG ASN B 175 -6.235 -4.403 475.140 1.00 46.96 B C
ANISOU 4733 CG ASN B 175 6704 4415 6724 -1207 849 1080 B C
ATOM 4734 ND2 ASN B 175 -6.262 -5.171 476.222 1.00 46.06 B N
ANISOU 4734 ND2 ASN B 175 6874 4236 6390 -1344 911 1190 B N
ATOM 4735 OD1 ASN B 175 -6.396 -4.850 474.014 1.00 58.66 B O
ANISOU 4735 OD1 ASN B 175 8108 5829 8350 -1245 820 1074 B O
ATOM 4736 N GLY B 176 -5.704 -0.047 474.206 1.00 52.24 B N
ANISOU 4736 N GLY B 176 6658 5428 7763 -605 684 686 B N
ATOM 4737 CA GLY B 176 -5.591 1.398 474.279 1.00 58.48 B C
ANISOU 4737 CA GLY B 176 7295 6313 8613 -434 654 564 B C
ATOM 4738 C GLY B 176 -6.830 2.096 474.794 1.00 51.66 B C
ANISOU 4738 C GLY B 176 6262 5658 7710 -475 829 446 B C
ATOM 4739 O GLY B 176 -7.942 1.585 474.709 1.00 62.76 B O
ANISOU 4739 O GLY B 176 7565 7168 9115 -634 974 436 B O
ATOM 4740 N ARG B 177 -6.617 3.273 475.361 1.00 56.35 B N
ANISOU 4740 N ARG B 177 6824 6309 8277 -332 820 349 B N
ATOM 4741 CA ARG B 177 -7.718 4.161 475.724 1.00 58.73 B C
ANISOU 4741 CA ARG B 177 6936 6797 8584 -307 979 205 B C
ATOM 4742 C ARG B 177 -7.428 5.533 475.139 1.00 39.29 B C
ANISOU 4742 C ARG B 177 4336 4320 6274 -89 867 96 B C
ATOM 4743 O ARG B 177 -6.279 5.979 475.159 1.00 54.53 B O
ANISOU 4743 O ARG B 177 6388 6128 8204 21 715 114 B O
ATOM 4744 CB ARG B 177 -7.902 4.264 477.243 1.00 54.01 B C
ANISOU 4744 CB ARG B 177 6492 6282 7748 -365 1129 173 B C
ATOM 4745 CG ARG B 177 -9.189 4.946 477.649 1.00 68.99 B C
ANISOU 4745 CG ARG B 177 8181 8384 9649 -368 1352 19 B C
ATOM 4746 CD ARG B 177 -9.426 4.881 479.156 1.00 81.16 B C
ANISOU 4746 CD ARG B 177 9909 10007 10919 -466 1545 -9 B C
ATOM 4747 NE ARG B 177 -8.615 5.863 479.872 1.00 87.08 B N
ANISOU 4747 NE ARG B 177 10819 10703 11562 -309 1457 -76 B N
ATOM 4748 CZ ARG B 177 -8.937 6.380 481.054 1.00 98.53 B C
ANISOU 4748 CZ ARG B 177 12375 12247 12813 -315 1624 -180 B C
ATOM 4749 NH1 ARG B 177 -10.062 6.011 481.665 1.00 95.53 B N1+
ANISOU 4749 NH1 ARG B 177 11943 12030 12324 -470 1914 -228 B N1+
ATOM 4750 NH2 ARG B 177 -8.135 7.270 481.628 1.00104.75 B N
ANISOU 4750 NH2 ARG B 177 13325 12966 13507 -181 1511 -243 B N
ATOM 4751 N VAL B 178 -8.439 6.176 474.564 1.00 39.72 B N
ANISOU 4751 N VAL B 178 4136 4488 6468 -30 926 -11 B N
ATOM 4752 CA VAL B 178 -8.301 7.571 474.147 1.00 38.98 B C
ANISOU 4752 CA VAL B 178 3941 4374 6498 182 836 -121 B C
ATOM 4753 C VAL B 178 -8.487 8.486 475.355 1.00 46.92 B C
ANISOU 4753 C VAL B 178 4986 5456 7386 266 951 -246 B C
ATOM 4754 O VAL B 178 -9.559 8.508 475.971 1.00 46.45 B O
ANISOU 4754 O VAL B 178 4810 5558 7280 224 1150 -332 B O
ATOM 4755 CB VAL B 178 -9.293 7.938 473.041 1.00 39.14 B C
ANISOU 4755 CB VAL B 178 3691 4465 6714 242 819 -183 B C
ATOM 4756 CG1 VAL B 178 -9.157 9.425 472.717 1.00 39.27 B C
ANISOU 4756 CG1 VAL B 178 3649 4435 6837 471 725 -291 B C
ATOM 4757 CG2 VAL B 178 -9.064 7.098 471.815 1.00 37.72 B C
ANISOU 4757 CG2 VAL B 178 3510 4196 6626 156 696 -71 B C
ATOM 4758 N ILE B 179 -7.451 9.257 475.683 1.00 39.72 B N
ANISOU 4758 N ILE B 179 4233 4430 6430 378 833 -269 B N
ATOM 4759 CA ILE B 179 -7.446 10.062 476.896 1.00 41.27 B C
ANISOU 4759 CA ILE B 179 4534 4667 6478 441 921 -385 B C
ATOM 4760 C ILE B 179 -7.576 11.553 476.615 1.00 52.40 B C
ANISOU 4760 C ILE B 179 5857 6046 8009 648 878 -532 B C
ATOM 4761 O ILE B 179 -7.757 12.333 477.569 1.00 42.97 B O
ANISOU 4761 O ILE B 179 4733 4888 6706 718 975 -662 B O
ATOM 4762 CB ILE B 179 -6.186 9.788 477.739 1.00 47.35 B C
ANISOU 4762 CB ILE B 179 5592 5334 7066 388 814 -309 B C
ATOM 4763 CG1 ILE B 179 -4.924 10.217 476.989 1.00 53.03 B C
ANISOU 4763 CG1 ILE B 179 6355 5883 7909 476 575 -264 B C
ATOM 4764 CG2 ILE B 179 -6.081 8.315 478.037 1.00 41.22 B C
ANISOU 4764 CG2 ILE B 179 4932 4562 6167 203 845 -156 B C
ATOM 4765 CD1 ILE B 179 -3.658 10.125 477.815 1.00 38.87 B C
ANISOU 4765 CD1 ILE B 179 4797 4000 5973 449 438 -214 B C
ATOM 4766 N ALA B 180 -7.496 11.981 475.350 1.00 48.71 B N
ANISOU 4766 N ALA B 180 5266 5496 7745 746 740 -519 B N
ATOM 4767 CA ALA B 180 -7.704 13.379 474.978 1.00 48.74 B C
ANISOU 4767 CA ALA B 180 5203 5445 7871 946 689 -645 B C
ATOM 4768 C ALA B 180 -8.080 13.438 473.505 1.00 39.20 B C
ANISOU 4768 C ALA B 180 3824 4200 6871 1005 578 -602 B C
ATOM 4769 O ALA B 180 -7.679 12.582 472.718 1.00 48.74 B O
ANISOU 4769 O ALA B 180 5040 5363 8116 897 492 -471 B O
ATOM 4770 CB ALA B 180 -6.470 14.246 475.258 1.00 39.45 B C
ANISOU 4770 CB ALA B 180 4239 4102 6648 1009 552 -669 B C
ATOM 4771 N GLU B 181 -8.843 14.463 473.143 1.00 40.33 B N
ANISOU 4771 N GLU B 181 3833 4351 7139 1184 573 -717 B N
ATOM 4772 CA GLU B 181 -9.457 14.525 471.825 1.00 49.77 B C
ANISOU 4772 CA GLU B 181 4855 5539 8516 1249 466 -686 B C
ATOM 4773 C GLU B 181 -9.780 15.982 471.475 1.00 56.94 B C
ANISOU 4773 C GLU B 181 5734 6357 9543 1492 386 -800 B C
ATOM 4774 O GLU B 181 -9.963 16.829 472.356 1.00 42.66 B O
ANISOU 4774 O GLU B 181 3962 4552 7697 1615 476 -937 B O
ATOM 4775 CB GLU B 181 -10.715 13.646 471.806 1.00 41.49 B C
ANISOU 4775 CB GLU B 181 3555 4699 7511 1164 591 -692 B C
ATOM 4776 CG GLU B 181 -11.511 13.629 470.525 1.00 41.78 B C
ANISOU 4776 CG GLU B 181 3384 4763 7728 1218 468 -672 B C
ATOM 4777 CD GLU B 181 -12.879 12.956 470.702 1.00 81.16 B C
ANISOU 4777 CD GLU B 181 8074 9985 12778 1144 608 -722 B C
ATOM 4778 OE1 GLU B 181 -13.470 13.084 471.796 1.00 82.38 B O
ANISOU 4778 OE1 GLU B 181 8136 10281 12885 1157 817 -835 B O
ATOM 4779 OE2 GLU B 181 -13.374 12.304 469.753 1.00 75.90 B O1-
ANISOU 4779 OE2 GLU B 181 7269 9365 12205 1059 516 -656 B O1-
ATOM 4780 N SER B 182 -9.800 16.270 470.175 1.00 49.19 B N
ANISOU 4780 N SER B 182 4726 5273 8691 1558 210 -741 B N
ATOM 4781 CA SER B 182 -10.112 17.601 469.660 1.00 41.55 B C
ANISOU 4781 CA SER B 182 3761 4185 7842 1791 96 -821 B C
ATOM 4782 C SER B 182 -10.713 17.415 468.274 1.00 54.26 B C
ANISOU 4782 C SER B 182 5245 5793 9579 1821 -63 -745 B C
ATOM 4783 O SER B 182 -10.012 16.955 467.369 1.00 58.14 B O
ANISOU 4783 O SER B 182 5855 6184 10052 1701 -177 -615 B O
ATOM 4784 CB SER B 182 -8.862 18.484 469.609 1.00 50.06 B C
ANISOU 4784 CB SER B 182 5123 5028 8871 1818 -3 -807 B C
ATOM 4785 OG SER B 182 -9.156 19.813 469.213 1.00 64.31 B O
ANISOU 4785 OG SER B 182 7031 6750 10654 1968 -93 -842 B O
ATOM 4786 N VAL B 183 -11.984 17.770 468.088 1.00 56.95 B N
ANISOU 4786 N VAL B 183 5385 6263 9989 1947 -73 -811 B N
ATOM 4787 CA VAL B 183 -12.746 17.354 466.907 1.00 59.98 B C
ANISOU 4787 CA VAL B 183 5621 6714 10456 1928 -218 -739 B C
ATOM 4788 C VAL B 183 -13.433 18.584 466.313 1.00 63.22 B C
ANISOU 4788 C VAL B 183 6059 7085 10876 2128 -356 -764 B C
ATOM 4789 O VAL B 183 -14.521 18.957 466.755 1.00 72.16 B O
ANISOU 4789 O VAL B 183 6982 8359 12077 2267 -291 -869 B O
ATOM 4790 CB VAL B 183 -13.777 16.284 467.274 1.00 52.91 B C
ANISOU 4790 CB VAL B 183 4372 6060 9670 1849 -90 -789 B C
ATOM 4791 CG1 VAL B 183 -13.127 14.976 467.421 1.00 43.55 B C
ANISOU 4791 CG1 VAL B 183 3264 4903 8381 1579 -7 -684 B C
ATOM 4792 CG2 VAL B 183 -14.410 16.626 468.621 1.00 66.33 B C
ANISOU 4792 CG2 VAL B 183 5920 7910 11372 1940 142 -951 B C
ATOM 4793 N ARG B 184 -12.861 19.153 465.238 1.00 56.62 B N
ANISOU 4793 N ARG B 184 5467 6064 9982 2136 -541 -663 B N
ATOM 4794 CA ARG B 184 -13.499 20.289 464.569 1.00 64.10 B C
ANISOU 4794 CA ARG B 184 6462 6949 10945 2320 -686 -666 B C
ATOM 4795 C ARG B 184 -14.812 19.902 463.903 1.00 87.37 B C
ANISOU 4795 C ARG B 184 9127 10054 14017 2379 -799 -670 B C
ATOM 4796 O ARG B 184 -15.885 20.388 464.288 1.00102.78 B O
ANISOU 4796 O ARG B 184 10873 12126 16052 2546 -766 -763 B O
ATOM 4797 CB ARG B 184 -12.569 20.961 463.551 1.00 46.83 B C
ANISOU 4797 CB ARG B 184 4611 4526 8656 2289 -837 -553 B C
ATOM 4798 CG ARG B 184 -11.308 21.534 464.120 1.00 45.34 B C
ANISOU 4798 CG ARG B 184 4691 4183 8352 2231 -746 -552 B C
ATOM 4799 CD ARG B 184 -10.405 22.049 463.030 1.00 51.87 B C
ANISOU 4799 CD ARG B 184 5817 4807 9086 2154 -867 -437 B C
ATOM 4800 NE ARG B 184 -9.217 22.714 463.570 1.00 62.27 B N
ANISOU 4800 NE ARG B 184 7370 5985 10305 2091 -783 -444 B N
ATOM 4801 CZ ARG B 184 -8.279 23.316 462.831 1.00 66.20 B C
ANISOU 4801 CZ ARG B 184 8134 6304 10715 2007 -836 -362 B C
ATOM 4802 NH1 ARG B 184 -8.388 23.342 461.503 1.00 55.70 B N1+
ANISOU 4802 NH1 ARG B 184 6895 4902 9366 1984 -968 -265 B N1+
ATOM 4803 NH2 ARG B 184 -7.239 23.916 463.418 1.00 60.51 B N
ANISOU 4803 NH2 ARG B 184 7590 5474 9926 1941 -756 -384 B N
ATOM 4804 N GLN B 185 -14.753 19.068 462.872 1.00 81.36 B N
ANISOU 4804 N GLN B 185 8352 9285 13274 2248 -940 -573 B N
ATOM 4805 CA GLN B 185 -15.965 18.770 462.126 1.00 77.53 B C
ANISOU 4805 CA GLN B 185 7620 8934 12904 2296 -1094 -573 B C
ATOM 4806 C GLN B 185 -16.869 17.849 462.942 1.00 75.93 B C
ANISOU 4806 C GLN B 185 7033 9002 12814 2233 -934 -666 B C
ATOM 4807 O GLN B 185 -16.519 17.400 464.037 1.00 86.97 B O
ANISOU 4807 O GLN B 185 8382 10469 14192 2149 -705 -720 B O
ATOM 4808 CB GLN B 185 -15.604 18.187 460.766 1.00 80.02 B C
ANISOU 4808 CB GLN B 185 8067 9142 13194 2169 -1306 -447 B C
ATOM 4809 CG GLN B 185 -14.680 19.113 459.996 1.00 90.95 B C
ANISOU 4809 CG GLN B 185 9844 10265 14448 2204 -1421 -359 B C
ATOM 4810 CD GLN B 185 -15.045 19.236 458.532 1.00 98.34 B C
ANISOU 4810 CD GLN B 185 10872 11115 15377 2228 -1700 -272 B C
ATOM 4811 NE2 GLN B 185 -14.389 20.163 457.831 1.00 86.87 B N
ANISOU 4811 NE2 GLN B 185 9758 9441 13805 2267 -1795 -198 B N
ATOM 4812 OE1 GLN B 185 -15.907 18.504 458.033 1.00107.77 B O
ANISOU 4812 OE1 GLN B 185 11842 12441 16665 2198 -1832 -271 B O
ATOM 4813 N LEU B 186 -18.054 17.573 462.402 1.00 66.82 B N
ANISOU 4813 N LEU B 186 5605 8009 11775 2263 -1054 -683 B N
ATOM 4814 CA LEU B 186 -18.961 16.613 463.020 1.00 69.28 B C
ANISOU 4814 CA LEU B 186 5537 8594 12193 2151 -905 -760 B C
ATOM 4815 C LEU B 186 -18.350 15.215 462.977 1.00 68.06 B C
ANISOU 4815 C LEU B 186 5382 8454 12024 1870 -843 -697 B C
ATOM 4816 O LEU B 186 -18.181 14.618 461.909 1.00 68.48 B O
ANISOU 4816 O LEU B 186 5492 8441 12086 1754 -1038 -602 B O
ATOM 4817 CB LEU B 186 -20.332 16.659 462.348 1.00 75.69 B C
ANISOU 4817 CB LEU B 186 6059 9569 13132 2229 -1075 -785 B C
ATOM 4818 CG LEU B 186 -21.089 18.005 462.419 1.00 75.62 B C
ANISOU 4818 CG LEU B 186 5999 9557 13176 2527 -1131 -848 B C
ATOM 4819 CD1 LEU B 186 -22.281 18.050 461.474 1.00 74.56 B C
ANISOU 4819 CD1 LEU B 186 5627 9537 13165 2606 -1375 -840 B C
ATOM 4820 CD2 LEU B 186 -21.568 18.286 463.843 1.00 68.66 B C
ANISOU 4820 CD2 LEU B 186 4921 8833 12335 2611 -830 -986 B C
ATOM 4821 N PHE B 187 -17.996 14.732 464.166 1.00 75.10 B N
ANISOU 4821 N PHE B 187 6228 9416 12889 1767 -570 -748 B N
ATOM 4822 CA PHE B 187 -17.446 13.423 464.487 1.00 73.80 B C
ANISOU 4822 CA PHE B 187 6042 9279 12719 1506 -434 -701 B C
ATOM 4823 C PHE B 187 -18.049 13.041 465.828 1.00 73.77 B C
ANISOU 4823 C PHE B 187 5796 9499 12735 1434 -128 -814 B C
ATOM 4824 O PHE B 187 -18.341 13.917 466.648 1.00 76.73 B O
ANISOU 4824 O PHE B 187 6147 9920 13087 1607 -0 -920 B O
ATOM 4825 CB PHE B 187 -15.911 13.449 464.676 1.00 68.72 B C
ANISOU 4825 CB PHE B 187 5799 8409 11904 1447 -387 -610 B C
ATOM 4826 CG PHE B 187 -15.089 12.903 463.536 1.00 75.99 B C
ANISOU 4826 CG PHE B 187 6982 9161 12731 1303 -555 -460 B C
ATOM 4827 CD1 PHE B 187 -15.238 11.589 463.110 1.00 82.83 B C
ANISOU 4827 CD1 PHE B 187 7819 10098 13554 1045 -553 -386 B C
ATOM 4828 CD2 PHE B 187 -14.062 13.661 462.982 1.00 81.14 B C
ANISOU 4828 CD2 PHE B 187 7941 9571 13319 1402 -675 -397 B C
ATOM 4829 CE1 PHE B 187 -14.415 11.051 462.093 1.00 72.38 B C
ANISOU 4829 CE1 PHE B 187 6764 8607 12129 913 -675 -262 B C
ATOM 4830 CE2 PHE B 187 -13.241 13.136 461.966 1.00 77.98 B C
ANISOU 4830 CE2 PHE B 187 7791 9019 12820 1258 -784 -270 B C
ATOM 4831 CZ PHE B 187 -13.422 11.826 461.523 1.00 64.42 B C
ANISOU 4831 CZ PHE B 187 6040 7375 11062 1024 -781 -207 B C
ATOM 4832 N THR B 188 -18.196 11.745 466.085 1.00 67.45 B N
ANISOU 4832 N THR B 188 4927 8823 11878 1139 10 -769 B N
ATOM 4833 CA THR B 188 -18.592 11.352 467.426 1.00 60.89 B C
ANISOU 4833 CA THR B 188 3959 8174 11003 1030 333 -855 B C
ATOM 4834 C THR B 188 -17.352 11.338 468.304 1.00 64.78 B C
ANISOU 4834 C THR B 188 4817 8520 11277 982 479 -804 B C
ATOM 4835 O THR B 188 -16.232 11.097 467.834 1.00 71.43 B O
ANISOU 4835 O THR B 188 5972 9163 12004 919 361 -676 B O
ATOM 4836 CB THR B 188 -19.267 9.975 467.447 1.00 73.01 B C
ANISOU 4836 CB THR B 188 5311 9890 12539 708 439 -822 B C
ATOM 4837 CG2 THR B 188 -19.688 9.593 468.871 1.00 71.96 B C
ANISOU 4837 CG2 THR B 188 5065 9942 12337 577 800 -907 B C
ATOM 4838 OG1 THR B 188 -20.433 9.983 466.610 1.00 83.28 B O
ANISOU 4838 OG1 THR B 188 6245 11341 14055 739 274 -877 B O
ATOM 4839 N SER B 189 -17.550 11.635 469.580 1.00 52.09 B N
ANISOU 4839 N SER B 189 3164 7014 9615 1021 735 -913 B N
ATOM 4840 CA SER B 189 -16.437 11.650 470.515 1.00 50.27 B C
ANISOU 4840 CA SER B 189 3271 6660 9168 976 859 -876 B C
ATOM 4841 C SER B 189 -15.990 10.223 470.804 1.00 55.07 B C
ANISOU 4841 C SER B 189 4039 7275 9611 655 956 -744 B C
ATOM 4842 O SER B 189 -16.798 9.374 471.182 1.00 77.87 B O
ANISOU 4842 O SER B 189 6749 10342 12496 458 1126 -759 B O
ATOM 4843 CB SER B 189 -16.852 12.357 471.796 1.00 52.48 B C
ANISOU 4843 CB SER B 189 3477 7049 9413 1099 1106 -1041 B C
ATOM 4844 OG SER B 189 -15.828 12.311 472.760 1.00 70.16 B O
ANISOU 4844 OG SER B 189 6047 9185 11424 1032 1213 -1008 B O
ATOM 4845 N MET B 190 -14.714 9.948 470.586 1.00 51.22 B N
ANISOU 4845 N MET B 190 3879 6585 8998 602 844 -616 B N
ATOM 4846 CA MET B 190 -14.101 8.686 470.981 1.00 56.00 B C
ANISOU 4846 CA MET B 190 4692 7150 9434 345 924 -489 B C
ATOM 4847 C MET B 190 -13.445 8.791 472.347 1.00 52.30 B C
ANISOU 4847 C MET B 190 4446 6657 8769 332 1084 -502 B C
ATOM 4848 O MET B 190 -12.693 7.895 472.741 1.00 63.60 B O
ANISOU 4848 O MET B 190 6112 8009 10043 166 1109 -387 B O
ATOM 4849 CB MET B 190 -13.064 8.230 469.931 1.00 53.41 B C
ANISOU 4849 CB MET B 190 4582 6618 9095 299 710 -345 B C
ATOM 4850 CG MET B 190 -13.650 7.861 468.576 1.00 46.70 B C
ANISOU 4850 CG MET B 190 3581 5779 8384 251 550 -312 B C
ATOM 4851 SD MET B 190 -14.796 6.476 468.732 1.00 59.45 B S
ANISOU 4851 SD MET B 190 4998 7584 10005 -48 695 -299 B S
ATOM 4852 CE MET B 190 -15.586 6.442 467.117 1.00 77.26 B C
ANISOU 4852 CE MET B 190 7040 9868 12448 -44 453 -302 B C
ATOM 4853 N LEU B 191 -13.708 9.875 473.063 1.00 46.41 B N
ANISOU 4853 N LEU B 191 3644 5966 8025 511 1179 -643 B N
ATOM 4854 CA LEU B 191 -13.060 10.126 474.340 1.00 46.57 B C
ANISOU 4854 CA LEU B 191 3902 5952 7842 514 1303 -672 B C
ATOM 4855 C LEU B 191 -13.390 9.017 475.326 1.00 48.08 B C
ANISOU 4855 C LEU B 191 4151 6263 7855 263 1533 -631 B C
ATOM 4856 O LEU B 191 -14.561 8.678 475.513 1.00 60.12 B O
ANISOU 4856 O LEU B 191 5433 7981 9431 168 1720 -698 B O
ATOM 4857 CB LEU B 191 -13.533 11.472 474.886 1.00 48.37 B C
ANISOU 4857 CB LEU B 191 4031 6232 8115 748 1391 -860 B C
ATOM 4858 CG LEU B 191 -12.884 11.918 476.178 1.00 48.81 B C
ANISOU 4858 CG LEU B 191 4349 6242 7954 771 1502 -917 B C
ATOM 4859 CD1 LEU B 191 -11.376 11.754 476.090 1.00 46.09 B C
ANISOU 4859 CD1 LEU B 191 4323 5689 7499 730 1304 -783 B C
ATOM 4860 CD2 LEU B 191 -13.272 13.334 476.508 1.00 74.74 B C
ANISOU 4860 CD2 LEU B 191 7561 9531 11306 1028 1553 -1110 B C
ATOM 4861 N ASN B 192 -12.356 8.458 475.964 1.00 54.59 B N
ANISOU 4861 N ASN B 192 5299 6972 8472 153 1515 -521 B N
ATOM 4862 CA ASN B 192 -12.468 7.405 476.974 1.00 54.31 B C
ANISOU 4862 CA ASN B 192 5418 6999 8217 -87 1705 -455 B C
ATOM 4863 C ASN B 192 -12.934 6.079 476.396 1.00 59.76 B C
ANISOU 4863 C ASN B 192 6034 7722 8951 -321 1726 -338 B C
ATOM 4864 O ASN B 192 -13.371 5.196 477.155 1.00 59.12 B O
ANISOU 4864 O ASN B 192 6024 7723 8717 -547 1925 -297 B O
ATOM 4865 CB ASN B 192 -13.400 7.789 478.123 1.00 53.74 B C
ANISOU 4865 CB ASN B 192 5262 7117 8041 -105 2004 -605 B C
ATOM 4866 CG ASN B 192 -12.660 8.358 479.283 1.00 78.08 B C
ANISOU 4866 CG ASN B 192 8639 10135 10894 -39 2041 -647 B C
ATOM 4867 ND2 ASN B 192 -12.419 9.664 479.246 1.00 78.77 B N
ANISOU 4867 ND2 ASN B 192 8701 10172 11055 208 1962 -775 B N
ATOM 4868 OD1 ASN B 192 -12.293 7.635 480.215 1.00 99.53 B O
ANISOU 4868 OD1 ASN B 192 11628 12832 13357 -212 2128 -563 B O
ATOM 4869 N HIS B 193 -12.928 5.937 475.078 1.00 46.98 B N
ANISOU 4869 N HIS B 193 4282 6042 7525 -288 1539 -291 B N
ATOM 4870 CA HIS B 193 -13.228 4.659 474.462 1.00 52.34 B C
ANISOU 4870 CA HIS B 193 4940 6713 8233 -516 1526 -179 B C
ATOM 4871 C HIS B 193 -11.980 3.774 474.464 1.00 45.67 B C
ANISOU 4871 C HIS B 193 4444 5654 7255 -599 1402 -9 B C
ATOM 4872 O HIS B 193 -10.858 4.245 474.248 1.00 43.03 B O
ANISOU 4872 O HIS B 193 4263 5165 6921 -439 1228 24 B O
ATOM 4873 CB HIS B 193 -13.771 4.868 473.043 1.00 46.42 B C
ANISOU 4873 CB HIS B 193 3925 5987 7727 -450 1368 -209 B C
ATOM 4874 CG HIS B 193 -15.169 5.408 473.004 1.00 55.84 B C
ANISOU 4874 CG HIS B 193 4735 7409 9074 -412 1485 -360 B C
ATOM 4875 CD2 HIS B 193 -16.195 5.170 472.153 1.00 62.92 B C
ANISOU 4875 CD2 HIS B 193 5325 8427 10153 -478 1446 -398 B C
ATOM 4876 ND1 HIS B 193 -15.648 6.307 473.934 1.00 70.70 B N
ANISOU 4876 ND1 HIS B 193 6501 9424 10937 -284 1663 -505 B N
ATOM 4877 CE1 HIS B 193 -16.909 6.596 473.660 1.00 53.16 B C
ANISOU 4877 CE1 HIS B 193 3898 7401 8899 -258 1739 -628 B C
ATOM 4878 NE2 HIS B 193 -17.266 5.919 472.585 1.00 52.89 B N
ANISOU 4878 NE2 HIS B 193 3733 7369 8992 -378 1596 -562 B N
ATOM 4879 N HIS B 194 -12.184 2.482 474.701 1.00 46.15 B N
ANISOU 4879 N HIS B 194 4622 5701 7213 -851 1493 95 B N
ATOM 4880 CA HIS B 194 -11.099 1.515 474.668 1.00 44.84 B C
ANISOU 4880 CA HIS B 194 4777 5322 6939 -924 1375 258 B C
ATOM 4881 C HIS B 194 -11.058 0.848 473.311 1.00 43.60 B C
ANISOU 4881 C HIS B 194 4572 5064 6930 -979 1231 320 B C
ATOM 4882 O HIS B 194 -12.097 0.595 472.698 1.00 44.68 B O
ANISOU 4882 O HIS B 194 4485 5312 7180 -1099 1279 276 B O
ATOM 4883 CB HIS B 194 -11.256 0.431 475.728 1.00 46.91 B C
ANISOU 4883 CB HIS B 194 5270 5578 6978 -1165 1543 352 B C
ATOM 4884 CG HIS B 194 -11.239 0.946 477.125 1.00 55.09 B C
ANISOU 4884 CG HIS B 194 6424 6694 7812 -1143 1692 304 B C
ATOM 4885 CD2 HIS B 194 -10.282 0.889 478.080 1.00 48.45 B C
ANISOU 4885 CD2 HIS B 194 5905 5742 6761 -1104 1643 377 B C
ATOM 4886 ND1 HIS B 194 -12.310 1.606 477.688 1.00 56.28 B N
ANISOU 4886 ND1 HIS B 194 6358 7069 7958 -1160 1918 158 B N
ATOM 4887 CE1 HIS B 194 -12.009 1.944 478.929 1.00 63.66 B C
ANISOU 4887 CE1 HIS B 194 7500 8019 8669 -1140 2020 138 B C
ATOM 4888 NE2 HIS B 194 -10.787 1.515 479.193 1.00 60.71 B N
ANISOU 4888 NE2 HIS B 194 7460 7445 8161 -1112 1841 275 B N
ATOM 4889 N PHE B 195 -9.850 0.559 472.856 1.00 41.59 B N
ANISOU 4889 N PHE B 195 4526 4601 6675 -896 1056 413 B N
ATOM 4890 CA PHE B 195 -9.595 -0.177 471.639 1.00 40.48 B C
ANISOU 4890 CA PHE B 195 4422 4324 6636 -946 929 479 B C
ATOM 4891 C PHE B 195 -8.763 -1.401 471.961 1.00 40.53 B C
ANISOU 4891 C PHE B 195 4747 4133 6518 -1045 904 623 B C
ATOM 4892 O PHE B 195 -7.938 -1.373 472.883 1.00 44.02 B O
ANISOU 4892 O PHE B 195 5386 4504 6836 -973 888 676 B O
ATOM 4893 CB PHE B 195 -8.865 0.684 470.601 1.00 47.01 B C
ANISOU 4893 CB PHE B 195 5188 5068 7605 -725 747 441 B C
ATOM 4894 CG PHE B 195 -9.672 1.856 470.124 1.00 49.80 B C
ANISOU 4894 CG PHE B 195 5257 5575 8090 -611 733 314 B C
ATOM 4895 CD1 PHE B 195 -10.031 2.873 470.999 1.00 39.10 B C
ANISOU 4895 CD1 PHE B 195 3788 4357 6712 -503 821 217 B C
ATOM 4896 CD2 PHE B 195 -10.079 1.936 468.812 1.00 37.86 B C
ANISOU 4896 CD2 PHE B 195 3611 4058 6716 -605 624 288 B C
ATOM 4897 CE1 PHE B 195 -10.775 3.918 470.578 1.00 39.50 B C
ANISOU 4897 CE1 PHE B 195 3588 4528 6894 -376 801 100 B C
ATOM 4898 CE2 PHE B 195 -10.828 2.996 468.385 1.00 50.50 B C
ANISOU 4898 CE2 PHE B 195 4965 5786 8438 -483 583 182 B C
ATOM 4899 CZ PHE B 195 -11.175 3.991 469.266 1.00 39.10 B C
ANISOU 4899 CZ PHE B 195 3399 4469 6990 -358 671 87 B C
ATOM 4900 N PRO B 196 -8.972 -2.490 471.237 1.00 40.88 B N
ANISOU 4900 N PRO B 196 4862 4079 6593 -1205 888 685 B N
ATOM 4901 CA PRO B 196 -8.220 -3.718 471.495 1.00 41.25 B C
ANISOU 4901 CA PRO B 196 5230 3908 6534 -1287 860 821 B C
ATOM 4902 C PRO B 196 -6.826 -3.676 470.885 1.00 39.23 B C
ANISOU 4902 C PRO B 196 5101 3455 6350 -1079 685 860 B C
ATOM 4903 O PRO B 196 -6.553 -2.945 469.938 1.00 37.57 B O
ANISOU 4903 O PRO B 196 4746 3252 6278 -936 594 791 B O
ATOM 4904 CB PRO B 196 -9.089 -4.785 470.826 1.00 49.10 B C
ANISOU 4904 CB PRO B 196 6225 4876 7555 -1541 914 843 B C
ATOM 4905 CG PRO B 196 -9.700 -4.044 469.675 1.00 49.79 B C
ANISOU 4905 CG PRO B 196 6014 5086 7815 -1489 853 728 B C
ATOM 4906 CD PRO B 196 -9.960 -2.657 470.161 1.00 41.31 B C
ANISOU 4906 CD PRO B 196 4711 4210 6776 -1324 884 627 B C
ATOM 4907 N ALA B 197 -5.937 -4.497 471.450 1.00 39.69 B N
ANISOU 4907 N ALA B 197 5438 3330 6312 -1065 640 974 B N
ATOM 4908 CA ALA B 197 -4.554 -4.562 470.970 1.00 38.26 B C
ANISOU 4908 CA ALA B 197 5362 2963 6213 -864 487 1009 B C
ATOM 4909 C ALA B 197 -4.456 -4.952 469.496 1.00 37.35 B C
ANISOU 4909 C ALA B 197 5215 2737 6238 -865 442 982 B C
ATOM 4910 O ALA B 197 -3.507 -4.562 468.817 1.00 35.90 B O
ANISOU 4910 O ALA B 197 5003 2472 6165 -686 350 955 B O
ATOM 4911 CB ALA B 197 -3.748 -5.530 471.828 1.00 39.52 B C
ANISOU 4911 CB ALA B 197 5824 2938 6253 -854 436 1140 B C
ATOM 4912 N SER B 198 -5.422 -5.708 468.981 1.00 38.39 B N
ANISOU 4912 N SER B 198 5359 2867 6361 -1078 512 983 B N
ATOM 4913 CA SER B 198 -5.409 -6.134 467.586 1.00 37.86 B C
ANISOU 4913 CA SER B 198 5300 2691 6396 -1106 467 952 B C
ATOM 4914 C SER B 198 -5.398 -4.965 466.612 1.00 45.76 B C
ANISOU 4914 C SER B 198 6073 3795 7518 -974 407 846 B C
ATOM 4915 O SER B 198 -5.061 -5.151 465.437 1.00 35.50 B O
ANISOU 4915 O SER B 198 4814 2385 6291 -944 355 819 B O
ATOM 4916 CB SER B 198 -6.616 -7.026 467.314 1.00 39.62 B C
ANISOU 4916 CB SER B 198 5548 2930 6576 -1393 544 957 B C
ATOM 4917 OG SER B 198 -7.790 -6.246 467.218 1.00 54.48 B O
ANISOU 4917 OG SER B 198 7144 5061 8494 -1479 588 869 B O
ATOM 4918 N ASP B 199 -5.760 -3.764 467.068 1.00 45.42 B N
ANISOU 4918 N ASP B 199 5819 3948 7489 -895 417 785 B N
ATOM 4919 CA ASP B 199 -5.945 -2.658 466.136 1.00 49.15 B C
ANISOU 4919 CA ASP B 199 6095 4513 8068 -792 354 692 B C
ATOM 4920 C ASP B 199 -4.627 -2.087 465.660 1.00 32.76 B C
ANISOU 4920 C ASP B 199 4067 2321 6060 -584 276 684 B C
ATOM 4921 O ASP B 199 -4.573 -1.542 464.555 1.00 39.99 B O
ANISOU 4921 O ASP B 199 4920 3224 7048 -529 222 631 B O
ATOM 4922 CB ASP B 199 -6.780 -1.560 466.792 1.00 47.80 B C
ANISOU 4922 CB ASP B 199 5695 4568 7898 -760 394 622 B C
ATOM 4923 CG ASP B 199 -8.237 -1.915 466.847 1.00 47.67 B C
ANISOU 4923 CG ASP B 199 5536 4704 7871 -963 471 591 B C
ATOM 4924 OD1 ASP B 199 -8.583 -3.041 466.425 1.00 56.72 B O
ANISOU 4924 OD1 ASP B 199 6783 5774 8996 -1152 486 632 B O
ATOM 4925 OD2 ASP B 199 -9.019 -1.099 467.360 1.00 50.54 B O1-
ANISOU 4925 OD2 ASP B 199 5691 5260 8252 -938 524 520 B O1-
ATOM 4926 N ILE B 200 -3.574 -2.199 466.467 1.00 39.71 B N
ANISOU 4926 N ILE B 200 5057 3117 6914 -477 264 735 B N
ATOM 4927 CA ILE B 200 -2.200 -1.938 466.037 1.00 37.46 B C
ANISOU 4927 CA ILE B 200 4820 2703 6711 -306 201 734 B C
ATOM 4928 C ILE B 200 -1.345 -3.133 466.443 1.00 34.06 B C
ANISOU 4928 C ILE B 200 4591 2092 6256 -289 191 821 B C
ATOM 4929 O ILE B 200 -0.932 -3.212 467.610 1.00 32.84 B O
ANISOU 4929 O ILE B 200 4496 1939 6041 -241 164 874 B O
ATOM 4930 CB ILE B 200 -1.640 -0.650 466.664 1.00 39.03 B C
ANISOU 4930 CB ILE B 200 4904 2989 6935 -154 158 693 B C
ATOM 4931 CG1 ILE B 200 -2.719 0.430 466.692 1.00 44.92 B C
ANISOU 4931 CG1 ILE B 200 5474 3918 7675 -173 178 617 B C
ATOM 4932 CG2 ILE B 200 -0.405 -0.170 465.899 1.00 29.62 B C
ANISOU 4932 CG2 ILE B 200 3699 1696 5859 -13 109 665 B C
ATOM 4933 CD1 ILE B 200 -2.299 1.703 467.365 1.00 48.90 B C
ANISOU 4933 CD1 ILE B 200 5894 4496 8189 -39 143 567 B C
ATOM 4934 N PRO B 201 -1.055 -4.068 465.535 1.00 46.57 B N
ANISOU 4934 N PRO B 201 6303 3529 7860 -316 201 828 B N
ATOM 4935 CA PRO B 201 -0.229 -5.228 465.883 1.00 33.63 B C
ANISOU 4935 CA PRO B 201 4868 1774 6138 -264 175 874 B C
ATOM 4936 C PRO B 201 1.202 -4.822 466.203 1.00 37.53 B C
ANISOU 4936 C PRO B 201 5322 2275 6663 -50 103 853 B C
ATOM 4937 O PRO B 201 1.659 -3.730 465.861 1.00 37.38 B O
ANISOU 4937 O PRO B 201 5139 2355 6710 43 87 783 B O
ATOM 4938 CB PRO B 201 -0.262 -6.083 464.618 1.00 33.99 B C
ANISOU 4938 CB PRO B 201 5032 1756 6127 -318 200 818 B C
ATOM 4939 CG PRO B 201 -1.425 -5.594 463.839 1.00 52.12 B C
ANISOU 4939 CG PRO B 201 7219 4130 8455 -463 234 775 B C
ATOM 4940 CD PRO B 201 -1.509 -4.133 464.140 1.00 54.36 B C
ANISOU 4940 CD PRO B 201 7279 4533 8841 -385 218 754 B C
ATOM 4941 N ALA B 202 1.917 -5.741 466.858 1.00 34.54 B N
ANISOU 4941 N ALA B 202 5102 1786 6237 19 53 915 B N
ATOM 4942 CA ALA B 202 3.275 -5.452 467.308 1.00 35.39 B C
ANISOU 4942 CA ALA B 202 5156 1898 6394 214 -34 904 B C
ATOM 4943 C ALA B 202 4.162 -4.956 466.174 1.00 40.64 B C
ANISOU 4943 C ALA B 202 5682 2629 7130 316 -10 789 B C
ATOM 4944 O ALA B 202 4.952 -4.025 466.353 1.00 42.30 B O
ANISOU 4944 O ALA B 202 5731 2923 7417 415 -52 750 B O
ATOM 4945 CB ALA B 202 3.880 -6.697 467.939 1.00 36.60 B C
ANISOU 4945 CB ALA B 202 5521 1898 6489 284 -96 983 B C
ATOM 4946 N GLN B 203 4.020 -5.548 464.994 1.00 47.12 B N
ANISOU 4946 N GLN B 203 6574 3406 7922 269 62 737 B N
ATOM 4947 CA GLN B 203 4.857 -5.180 463.863 1.00 42.60 B C
ANISOU 4947 CA GLN B 203 5906 2870 7408 344 108 641 B C
ATOM 4948 C GLN B 203 4.693 -3.710 463.512 1.00 41.62 B C
ANISOU 4948 C GLN B 203 5595 2891 7329 322 128 588 B C
ATOM 4949 O GLN B 203 5.638 -3.060 463.055 1.00 50.12 B O
ANISOU 4949 O GLN B 203 6551 4015 8478 397 147 530 B O
ATOM 4950 CB GLN B 203 4.491 -6.054 462.665 1.00 41.03 B C
ANISOU 4950 CB GLN B 203 5857 2584 7147 267 177 602 B C
ATOM 4951 CG GLN B 203 5.584 -6.199 461.638 1.00 54.96 B C
ANISOU 4951 CG GLN B 203 7601 4313 8969 365 234 523 B C
ATOM 4952 CD GLN B 203 5.117 -6.997 460.427 1.00 72.36 B C
ANISOU 4952 CD GLN B 203 9974 6420 11100 274 292 481 B C
ATOM 4953 NE2 GLN B 203 3.950 -7.683 460.557 1.00 58.01 B N
ANISOU 4953 NE2 GLN B 203 8312 4544 9184 127 263 526 B N
ATOM 4954 OE1 GLN B 203 5.781 -6.979 459.371 1.00 64.57 B O
ANISOU 4954 OE1 GLN B 203 8977 5407 10150 318 367 407 B O
ATOM 4955 N ALA B 204 3.477 -3.192 463.662 1.00 66.93 B N
ANISOU 4955 N ALA B 204 8777 6152 10502 211 130 607 B N
ATOM 4956 CA ALA B 204 3.174 -1.790 463.387 1.00 39.42 B C
ANISOU 4956 CA ALA B 204 5141 2782 7055 199 133 562 B C
ATOM 4957 C ALA B 204 3.572 -0.886 464.537 1.00 29.56 B C
ANISOU 4957 C ALA B 204 3774 1593 5863 272 67 578 B C
ATOM 4958 O ALA B 204 4.069 0.209 464.304 1.00 50.83 B O
ANISOU 4958 O ALA B 204 6352 4359 8603 314 60 524 B O
ATOM 4959 CB ALA B 204 1.688 -1.615 463.088 1.00 34.28 B C
ANISOU 4959 CB ALA B 204 4495 2149 6381 68 150 573 B C
ATOM 4960 N ARG B 205 3.333 -1.290 465.784 1.00 30.23 B N
ANISOU 4960 N ARG B 205 3910 1637 5940 274 15 655 B N
ATOM 4961 CA ARG B 205 3.849 -0.485 466.881 1.00 30.26 B C
ANISOU 4961 CA ARG B 205 3832 1679 5988 353 -68 666 B C
ATOM 4962 C ARG B 205 5.348 -0.354 466.767 1.00 37.72 B C
ANISOU 4962 C ARG B 205 4707 2634 6991 465 -114 625 B C
ATOM 4963 O ARG B 205 5.928 0.653 467.177 1.00 43.12 B O
ANISOU 4963 O ARG B 205 5276 3375 7734 513 -171 591 B O
ATOM 4964 CB ARG B 205 3.504 -1.085 468.227 1.00 31.35 B C
ANISOU 4964 CB ARG B 205 4083 1740 6090 339 -125 774 B C
ATOM 4965 CG ARG B 205 2.039 -1.167 468.511 1.00 35.83 B C
ANISOU 4965 CG ARG B 205 4693 2320 6602 198 -55 816 B C
ATOM 4966 CD ARG B 205 1.855 -1.471 469.960 1.00 39.66 B C
ANISOU 4966 CD ARG B 205 5290 2843 6937 168 -97 884 B C
ATOM 4967 NE ARG B 205 2.395 -2.784 470.295 1.00 52.04 B N
ANISOU 4967 NE ARG B 205 7048 4246 8480 187 -149 989 B N
ATOM 4968 CZ ARG B 205 1.764 -3.936 470.122 1.00 52.55 B C
ANISOU 4968 CZ ARG B 205 7270 4219 8478 67 -84 1053 B C
ATOM 4969 NH1 ARG B 205 0.545 -3.957 469.608 1.00 61.70 B N1+
ANISOU 4969 NH1 ARG B 205 8392 5456 9595 -96 35 1020 B N1+
ATOM 4970 NH2 ARG B 205 2.360 -5.066 470.466 1.00 37.69 B N
ANISOU 4970 NH2 ARG B 205 5584 2159 6579 112 -149 1150 B N
ATOM 4971 N ALA B 206 5.991 -1.366 466.205 1.00 45.97 B N
ANISOU 4971 N ALA B 206 5815 3612 8038 504 -86 623 B N
ATOM 4972 CA ALA B 206 7.429 -1.336 466.064 1.00 42.11 B C
ANISOU 4972 CA ALA B 206 5230 3120 7649 614 -115 585 B C
ATOM 4973 C ALA B 206 7.874 -0.276 465.068 1.00 35.70 B C
ANISOU 4973 C ALA B 206 4274 2382 6910 591 -41 496 B C
ATOM 4974 O ALA B 206 9.024 0.164 465.134 1.00 32.43 B O
ANISOU 4974 O ALA B 206 3724 1982 6616 656 -68 461 B O
ATOM 4975 CB ALA B 206 7.923 -2.726 465.671 1.00 33.44 B C
ANISOU 4975 CB ALA B 206 4246 1911 6550 674 -89 600 B C
ATOM 4976 N MET B 207 6.987 0.165 464.170 1.00 42.21 B N
ANISOU 4976 N MET B 207 5126 3242 7670 496 43 466 B N
ATOM 4977 CA MET B 207 7.385 1.139 463.157 1.00 44.28 B C
ANISOU 4977 CA MET B 207 5300 3546 7980 468 116 398 B C
ATOM 4978 C MET B 207 7.777 2.472 463.786 1.00 45.42 B C
ANISOU 4978 C MET B 207 5312 3752 8194 479 53 375 B C
ATOM 4979 O MET B 207 8.729 3.128 463.343 1.00 29.59 B O
ANISOU 4979 O MET B 207 3200 1746 6296 486 89 328 B O
ATOM 4980 CB MET B 207 6.257 1.340 462.149 1.00 49.89 B C
ANISOU 4980 CB MET B 207 6098 4270 8589 374 179 383 B C
ATOM 4981 CG MET B 207 6.144 0.228 461.133 1.00 49.24 B C
ANISOU 4981 CG MET B 207 6145 4109 8455 347 256 376 B C
ATOM 4982 SD MET B 207 7.642 -0.013 460.140 1.00 54.62 B S
ANISOU 4982 SD MET B 207 6787 4725 9239 404 370 316 B S
ATOM 4983 CE MET B 207 7.131 -1.255 458.967 1.00 59.24 B C
ANISOU 4983 CE MET B 207 7580 5207 9721 355 450 302 B C
ATOM 4984 N TYR B 208 7.062 2.885 464.826 1.00 28.89 B N
ANISOU 4984 N TYR B 208 3228 1693 6055 475 -32 404 B N
ATOM 4985 CA TYR B 208 7.324 4.195 465.406 1.00 34.36 B C
ANISOU 4985 CA TYR B 208 3827 2428 6800 481 -95 371 B C
ATOM 4986 C TYR B 208 8.773 4.318 465.851 1.00 30.32 B C
ANISOU 4986 C TYR B 208 3196 1895 6430 541 -160 353 B C
ATOM 4987 O TYR B 208 9.339 5.418 465.831 1.00 44.80 B O
ANISOU 4987 O TYR B 208 4931 3738 8354 525 -178 303 B O
ATOM 4988 CB TYR B 208 6.360 4.445 466.566 1.00 28.51 B C
ANISOU 4988 CB TYR B 208 3132 1703 5999 486 -171 403 B C
ATOM 4989 CG TYR B 208 4.939 4.525 466.100 1.00 35.46 B C
ANISOU 4989 CG TYR B 208 4070 2601 6803 429 -108 408 B C
ATOM 4990 CD1 TYR B 208 4.498 5.609 465.354 1.00 31.91 B C
ANISOU 4990 CD1 TYR B 208 3594 2189 6343 398 -75 355 B C
ATOM 4991 CD2 TYR B 208 4.044 3.496 466.358 1.00 36.67 B C
ANISOU 4991 CD2 TYR B 208 4306 2717 6911 400 -89 470 B C
ATOM 4992 CE1 TYR B 208 3.194 5.704 464.911 1.00 26.69 B C
ANISOU 4992 CE1 TYR B 208 2961 1536 5643 363 -45 358 B C
ATOM 4993 CE2 TYR B 208 2.736 3.573 465.905 1.00 42.76 B C
ANISOU 4993 CE2 TYR B 208 5091 3494 7661 339 -40 472 B C
ATOM 4994 CZ TYR B 208 2.318 4.689 465.176 1.00 46.12 B C
ANISOU 4994 CZ TYR B 208 5464 3966 8094 332 -27 413 B C
ATOM 4995 OH TYR B 208 1.024 4.795 464.700 1.00 43.45 B O
ANISOU 4995 OH TYR B 208 5116 3625 7770 290 -6 413 B O
ATOM 4996 N SER B 209 9.395 3.204 466.241 1.00 39.75 B N
ANISOU 4996 N SER B 209 4396 3047 7661 613 -204 391 B N
ATOM 4997 CA SER B 209 10.803 3.233 466.613 1.00 32.27 B C
ANISOU 4997 CA SER B 209 3304 2079 6879 687 -284 372 B C
ATOM 4998 C SER B 209 11.737 3.438 465.433 1.00 32.72 B C
ANISOU 4998 C SER B 209 3233 2114 7086 672 -160 307 B C
ATOM 4999 O SER B 209 12.857 3.906 465.627 1.00 42.49 B O
ANISOU 4999 O SER B 209 4295 3342 8508 701 -208 267 B O
ATOM 5000 CB SER B 209 11.139 1.982 467.364 1.00 33.60 B C
ANISOU 5000 CB SER B 209 3530 2200 7036 787 -382 436 B C
ATOM 5001 OG SER B 209 10.483 2.102 468.598 1.00 48.12 B O
ANISOU 5001 OG SER B 209 5464 4044 8776 793 -510 494 B O
ATOM 5002 N ILE B 210 11.314 3.106 464.221 1.00 32.10 B N
ANISOU 5002 N ILE B 210 3234 2018 6946 623 -3 294 B N
ATOM 5003 CA ILE B 210 12.111 3.448 463.057 1.00 32.64 B C
ANISOU 5003 CA ILE B 210 3203 2048 7150 594 143 232 B C
ATOM 5004 C ILE B 210 11.815 4.871 462.603 1.00 31.73 B C
ANISOU 5004 C ILE B 210 3075 1952 7031 494 190 198 B C
ATOM 5005 O ILE B 210 12.725 5.671 462.367 1.00 44.32 B O
ANISOU 5005 O ILE B 210 4524 3509 8806 469 234 148 B O
ATOM 5006 CB ILE B 210 11.866 2.443 461.926 1.00 42.96 B C
ANISOU 5006 CB ILE B 210 4630 3305 8389 592 288 228 B C
ATOM 5007 CG1 ILE B 210 12.434 1.070 462.298 1.00 34.18 B C
ANISOU 5007 CG1 ILE B 210 3523 2142 7323 710 251 248 B C
ATOM 5008 CG2 ILE B 210 12.445 2.990 460.634 1.00 33.20 B C
ANISOU 5008 CG2 ILE B 210 3337 2021 7257 536 471 165 B C
ATOM 5009 CD1 ILE B 210 11.404 0.051 462.588 1.00 33.68 B C
ANISOU 5009 CD1 ILE B 210 3663 2060 7072 716 203 309 B C
ATOM 5010 N ASN B 211 10.549 5.217 462.490 1.00 30.33 B N
ANISOU 5010 N ASN B 211 3044 1817 6663 440 179 221 B N
ATOM 5011 CA ASN B 211 10.156 6.562 462.093 1.00 30.11 B C
ANISOU 5011 CA ASN B 211 3042 1802 6598 365 200 194 B C
ATOM 5012 C ASN B 211 8.955 6.999 462.926 1.00 28.63 B C
ANISOU 5012 C ASN B 211 2934 1676 6268 365 88 218 B C
ATOM 5013 O ASN B 211 7.905 6.349 462.888 1.00 27.99 B O
ANISOU 5013 O ASN B 211 2957 1624 6055 367 84 253 B O
ATOM 5014 CB ASN B 211 9.844 6.574 460.597 1.00 29.46 B C
ANISOU 5014 CB ASN B 211 3072 1686 6435 304 342 182 B C
ATOM 5015 CG ASN B 211 9.554 7.951 460.069 1.00 33.91 B C
ANISOU 5015 CG ASN B 211 3695 2240 6951 234 359 161 B C
ATOM 5016 ND2 ASN B 211 9.783 8.144 458.784 1.00 40.13 B N
ANISOU 5016 ND2 ASN B 211 4563 2966 7718 174 492 144 B N
ATOM 5017 OD1 ASN B 211 9.115 8.832 460.800 1.00 45.13 B O
ANISOU 5017 OD1 ASN B 211 5114 3693 8340 235 257 161 B O
ATOM 5018 N PRO B 212 9.058 8.087 463.692 1.00 28.68 B N
ANISOU 5018 N PRO B 212 2892 1690 6316 363 3 194 B N
ATOM 5019 CA PRO B 212 7.979 8.421 464.638 1.00 28.08 B C
ANISOU 5019 CA PRO B 212 2880 1658 6132 385 -90 206 B C
ATOM 5020 C PRO B 212 6.677 8.853 463.988 1.00 28.81 B C
ANISOU 5020 C PRO B 212 3079 1776 6091 358 -52 207 B C
ATOM 5021 O PRO B 212 5.652 8.906 464.682 1.00 27.74 B O
ANISOU 5021 O PRO B 212 2976 1670 5893 386 -100 216 B O
ATOM 5022 CB PRO B 212 8.587 9.555 465.477 1.00 28.68 B C
ANISOU 5022 CB PRO B 212 2888 1706 6305 390 -182 161 B C
ATOM 5023 CG PRO B 212 9.718 10.051 464.692 1.00 29.37 B C
ANISOU 5023 CG PRO B 212 2889 1733 6539 340 -119 125 B C
ATOM 5024 CD PRO B 212 10.248 8.921 463.900 1.00 29.65 B C
ANISOU 5024 CD PRO B 212 2884 1760 6623 347 -19 148 B C
ATOM 5025 N ILE B 213 6.665 9.151 462.698 1.00 27.12 B N
ANISOU 5025 N ILE B 213 2919 1539 5847 311 28 197 B N
ATOM 5026 CA ILE B 213 5.469 9.647 462.037 1.00 32.06 B C
ANISOU 5026 CA ILE B 213 3646 2172 6362 298 28 200 B C
ATOM 5027 C ILE B 213 5.077 8.688 460.916 1.00 26.52 B C
ANISOU 5027 C ILE B 213 3024 1458 5596 267 93 228 B C
ATOM 5028 O ILE B 213 5.934 8.169 460.190 1.00 26.91 B O
ANISOU 5028 O ILE B 213 3083 1468 5673 239 176 225 B O
ATOM 5029 CB ILE B 213 5.687 11.092 461.525 1.00 33.24 B C
ANISOU 5029 CB ILE B 213 3847 2273 6508 273 27 167 B C
ATOM 5030 CG1 ILE B 213 4.375 11.704 461.059 1.00 38.02 B C
ANISOU 5030 CG1 ILE B 213 4554 2876 7016 294 -16 172 B C
ATOM 5031 CG2 ILE B 213 6.665 11.141 460.386 1.00 27.55 B C
ANISOU 5031 CG2 ILE B 213 3160 1488 5818 208 128 164 B C
ATOM 5032 CD1 ILE B 213 4.223 13.123 461.470 1.00 27.24 B C
ANISOU 5032 CD1 ILE B 213 3221 1478 5651 324 -75 135 B C
ATOM 5033 N ARG B 214 3.779 8.436 460.797 1.00 26.22 B N
ANISOU 5033 N ARG B 214 3031 1436 5494 272 56 248 B N
ATOM 5034 CA ARG B 214 3.223 7.627 459.722 1.00 29.21 B C
ANISOU 5034 CA ARG B 214 3503 1783 5812 229 90 270 B C
ATOM 5035 C ARG B 214 2.112 8.418 459.059 1.00 34.28 B C
ANISOU 5035 C ARG B 214 4212 2403 6412 228 29 271 B C
ATOM 5036 O ARG B 214 1.204 8.894 459.751 1.00 37.95 B O
ANISOU 5036 O ARG B 214 4607 2895 6915 276 -44 268 B O
ATOM 5037 CB ARG B 214 2.694 6.279 460.261 1.00 26.22 B C
ANISOU 5037 CB ARG B 214 3103 1417 5442 225 88 302 B C
ATOM 5038 CG ARG B 214 2.143 5.338 459.202 1.00 26.49 B C
ANISOU 5038 CG ARG B 214 3247 1401 5419 164 117 318 B C
ATOM 5039 CD ARG B 214 3.156 4.976 458.088 1.00 26.91 B C
ANISOU 5039 CD ARG B 214 3400 1397 5427 135 208 297 B C
ATOM 5040 NE ARG B 214 2.734 3.760 457.394 1.00 27.35 B N
ANISOU 5040 NE ARG B 214 3573 1395 5426 80 235 307 B N
ATOM 5041 CZ ARG B 214 2.940 3.456 456.112 1.00 27.97 B C
ANISOU 5041 CZ ARG B 214 3798 1396 5431 28 291 288 B C
ATOM 5042 NH1 ARG B 214 3.573 4.278 455.295 1.00 28.26 B N1+
ANISOU 5042 NH1 ARG B 214 3892 1400 5445 18 338 265 B N1+
ATOM 5043 NH2 ARG B 214 2.487 2.299 455.635 1.00 41.57 B N
ANISOU 5043 NH2 ARG B 214 5636 3058 7101 -29 301 292 B N
ATOM 5044 N ILE B 215 2.158 8.545 457.731 1.00 26.80 B N
ANISOU 5044 N ILE B 215 3402 1388 5394 182 54 275 B N
ATOM 5045 CA ILE B 215 1.188 9.367 457.012 1.00 36.76 B C
ANISOU 5045 CA ILE B 215 4750 2599 6617 191 -31 286 B C
ATOM 5046 C ILE B 215 0.497 8.521 455.956 1.00 27.73 B C
ANISOU 5046 C ILE B 215 3717 1394 5425 131 -48 311 B C
ATOM 5047 O ILE B 215 1.151 7.871 455.134 1.00 41.18 B O
ANISOU 5047 O ILE B 215 5543 3048 7057 64 38 309 B O
ATOM 5048 CB ILE B 215 1.827 10.605 456.353 1.00 28.29 B C
ANISOU 5048 CB ILE B 215 3801 1459 5489 181 -17 277 B C
ATOM 5049 CG1 ILE B 215 2.712 11.362 457.313 1.00 35.67 B C
ANISOU 5049 CG1 ILE B 215 4641 2431 6482 208 8 246 B C
ATOM 5050 CG2 ILE B 215 0.773 11.583 455.921 1.00 36.09 B C
ANISOU 5050 CG2 ILE B 215 4866 2392 6453 230 -137 292 B C
ATOM 5051 CD1 ILE B 215 3.935 11.865 456.605 1.00 45.28 B C
ANISOU 5051 CD1 ILE B 215 5952 3574 7677 139 98 237 B C
ATOM 5052 N ILE B 216 -0.821 8.578 455.953 1.00 28.09 B N
ANISOU 5052 N ILE B 216 3718 1430 5526 153 -170 330 B N
ATOM 5053 CA ILE B 216 -1.671 7.960 454.953 1.00 28.87 B C
ANISOU 5053 CA ILE B 216 3912 1452 5607 87 -243 356 B C
ATOM 5054 C ILE B 216 -2.535 9.093 454.403 1.00 45.33 B C
ANISOU 5054 C ILE B 216 6036 3478 7710 147 -412 373 B C
ATOM 5055 O ILE B 216 -3.581 9.395 454.991 1.00 41.90 B O
ANISOU 5055 O ILE B 216 5440 3072 7407 227 -546 372 B O
ATOM 5056 CB ILE B 216 -2.496 6.838 455.599 1.00 28.83 B C
ANISOU 5056 CB ILE B 216 3770 1478 5708 49 -273 367 B C
ATOM 5057 CG1 ILE B 216 -1.546 5.785 456.193 1.00 28.13 B C
ANISOU 5057 CG1 ILE B 216 3675 1435 5579 15 -121 357 B C
ATOM 5058 CG2 ILE B 216 -3.502 6.271 454.620 1.00 33.54 B C
ANISOU 5058 CG2 ILE B 216 4442 2014 6287 -44 -391 386 B C
ATOM 5059 CD1 ILE B 216 -2.197 4.743 457.041 1.00 28.18 B C
ANISOU 5059 CD1 ILE B 216 3572 1462 5672 -29 -122 377 B C
ATOM 5060 N PRO B 217 -2.117 9.804 453.344 1.00 37.34 B N
ANISOU 5060 N PRO B 217 5236 2377 6576 128 -412 388 B N
ATOM 5061 CA PRO B 217 -2.875 10.997 452.921 1.00 42.90 B C
ANISOU 5061 CA PRO B 217 5996 3023 7282 213 -593 412 B C
ATOM 5062 C PRO B 217 -4.176 10.676 452.235 1.00 37.41 B C
ANISOU 5062 C PRO B 217 5321 2268 6626 210 -830 446 B C
ATOM 5063 O PRO B 217 -5.035 11.562 452.110 1.00 39.68 B O
ANISOU 5063 O PRO B 217 5582 2566 6930 323 -1022 454 B O
ATOM 5064 CB PRO B 217 -1.913 11.710 451.963 1.00 32.13 B C
ANISOU 5064 CB PRO B 217 4891 1558 5760 161 -493 429 B C
ATOM 5065 CG PRO B 217 -0.554 11.216 452.363 1.00 39.45 B C
ANISOU 5065 CG PRO B 217 5802 2530 6659 95 -262 392 B C
ATOM 5066 CD PRO B 217 -0.781 9.777 452.729 1.00 41.03 B C
ANISOU 5066 CD PRO B 217 5880 2796 6912 54 -233 378 B C
ATOM 5067 N ASP B 218 -4.359 9.435 451.807 1.00 42.70 B N
ANISOU 5067 N ASP B 218 6020 2964 7242 84 -806 444 B N
ATOM 5068 CA ASP B 218 -5.536 9.061 451.031 1.00 43.76 B C
ANISOU 5068 CA ASP B 218 6178 3145 7304 37 -1008 453 B C
ATOM 5069 C ASP B 218 -5.703 7.558 451.188 1.00 41.00 B C
ANISOU 5069 C ASP B 218 5762 2864 6952 -101 -928 429 B C
ATOM 5070 O ASP B 218 -4.940 6.784 450.603 1.00 37.28 B O
ANISOU 5070 O ASP B 218 5485 2288 6392 -216 -796 429 B O
ATOM 5071 CB ASP B 218 -5.365 9.449 449.563 1.00 43.57 B C
ANISOU 5071 CB ASP B 218 6490 2963 7102 -20 -1099 497 B C
ATOM 5072 CG ASP B 218 -6.671 9.462 448.791 1.00 46.48 B C
ANISOU 5072 CG ASP B 218 6879 3378 7402 -24 -1389 513 B C
ATOM 5073 OD1 ASP B 218 -7.685 8.872 449.244 1.00 38.26 B O
ANISOU 5073 OD1 ASP B 218 5589 2500 6450 -31 -1492 479 B O
ATOM 5074 OD2 ASP B 218 -6.649 10.030 447.682 1.00 46.28 B O1-
ANISOU 5074 OD2 ASP B 218 7138 3223 7225 -37 -1513 560 B O1-
ATOM 5075 N VAL B 219 -6.700 7.168 451.981 1.00 38.21 B N
ANISOU 5075 N VAL B 219 5141 2679 6698 -90 -995 402 B N
ATOM 5076 CA VAL B 219 -7.037 5.771 452.199 1.00 34.42 B C
ANISOU 5076 CA VAL B 219 4594 2264 6218 -237 -940 383 B C
ATOM 5077 C VAL B 219 -7.357 5.057 450.891 1.00 42.16 B C
ANISOU 5077 C VAL B 219 5791 3170 7056 -391 -1043 386 B C
ATOM 5078 O VAL B 219 -7.087 3.853 450.752 1.00 49.95 B O
ANISOU 5078 O VAL B 219 6875 4109 7995 -533 -937 373 B O
ATOM 5079 CB VAL B 219 -8.213 5.726 453.193 1.00 43.49 B C
ANISOU 5079 CB VAL B 219 5413 3618 7493 -206 -1010 352 B C
ATOM 5080 CG1 VAL B 219 -8.964 4.438 453.090 1.00 44.00 B C
ANISOU 5080 CG1 VAL B 219 5421 3755 7542 -391 -1034 336 B C
ATOM 5081 CG2 VAL B 219 -7.721 5.979 454.610 1.00 33.53 B C
ANISOU 5081 CG2 VAL B 219 3992 2415 6334 -110 -843 340 B C
ATOM 5082 N ASN B 220 -7.872 5.777 449.890 1.00 37.29 B N
ANISOU 5082 N ASN B 220 5292 2520 6354 -364 -1254 404 B N
ATOM 5083 CA ASN B 220 -8.277 5.143 448.633 1.00 38.98 B C
ANISOU 5083 CA ASN B 220 5730 2672 6409 -518 -1390 404 B C
ATOM 5084 C ASN B 220 -7.287 5.352 447.505 1.00 43.10 B C
ANISOU 5084 C ASN B 220 6641 2990 6745 -559 -1317 429 B C
ATOM 5085 O ASN B 220 -7.563 4.942 446.374 1.00 40.80 B O
ANISOU 5085 O ASN B 220 6593 2626 6283 -684 -1432 427 B O
ATOM 5086 CB ASN B 220 -9.644 5.636 448.184 1.00 41.14 B C
ANISOU 5086 CB ASN B 220 5887 3053 6690 -487 -1716 407 B C
ATOM 5087 CG ASN B 220 -10.726 5.261 449.141 1.00 48.81 B C
ANISOU 5087 CG ASN B 220 6468 4240 7837 -491 -1774 365 B C
ATOM 5088 ND2 ASN B 220 -11.583 6.221 449.462 1.00 53.92 B N
ANISOU 5088 ND2 ASN B 220 6870 5010 8605 -329 -1952 359 B N
ATOM 5089 OD1 ASN B 220 -10.799 4.115 449.598 1.00 51.32 B O
ANISOU 5089 OD1 ASN B 220 6708 4608 8184 -640 -1651 336 B O
ATOM 5090 N ALA B 221 -6.140 5.967 447.783 1.00 46.98 B N
ANISOU 5090 N ALA B 221 7200 3390 7259 -472 -1121 445 B N
ATOM 5091 CA ALA B 221 -5.122 6.092 446.755 1.00 53.15 B C
ANISOU 5091 CA ALA B 221 8336 3986 7872 -535 -994 458 B C
ATOM 5092 C ALA B 221 -4.582 4.717 446.388 1.00 38.18 B C
ANISOU 5092 C ALA B 221 6591 2016 5900 -685 -810 411 B C
ATOM 5093 O ALA B 221 -4.351 3.864 447.250 1.00 37.03 B O
ANISOU 5093 O ALA B 221 6273 1920 5877 -693 -671 380 B O
ATOM 5094 CB ALA B 221 -4.001 7.020 447.215 1.00 36.90 B C
ANISOU 5094 CB ALA B 221 6272 1863 5885 -430 -810 476 B C
ATOM 5095 N GLU B 222 -4.347 4.529 445.107 1.00 46.10 B N
ANISOU 5095 N GLU B 222 7942 2883 6689 -798 -806 405 B N
ATOM 5096 CA GLU B 222 -3.918 3.245 444.582 1.00 57.73 B C
ANISOU 5096 CA GLU B 222 9559 4320 8054 -920 -627 338 B C
ATOM 5097 C GLU B 222 -2.410 3.097 444.765 1.00 63.16 B C
ANISOU 5097 C GLU B 222 10185 5021 8793 -847 -267 297 B C
ATOM 5098 O GLU B 222 -1.651 3.940 444.270 1.00 65.34 B O
ANISOU 5098 O GLU B 222 10553 5271 9003 -810 -165 311 B O
ATOM 5099 CB GLU B 222 -4.307 3.161 443.110 1.00 69.52 B C
ANISOU 5099 CB GLU B 222 11420 5719 9277 -1053 -766 334 B C
ATOM 5100 CG GLU B 222 -4.182 1.802 442.436 1.00 76.81 B C
ANISOU 5100 CG GLU B 222 12524 6602 10059 -1194 -656 255 B C
ATOM 5101 CD GLU B 222 -4.357 1.915 440.906 1.00 83.46 B C
ANISOU 5101 CD GLU B 222 13784 7340 10587 -1319 -763 249 B C
ATOM 5102 OE1 GLU B 222 -3.895 2.935 440.321 1.00 74.23 B O
ANISOU 5102 OE1 GLU B 222 12779 6128 9298 -1275 -735 292 B O
ATOM 5103 OE2 GLU B 222 -4.951 0.991 440.296 1.00 83.19 B O1-
ANISOU 5103 OE2 GLU B 222 13930 7264 10415 -1472 -878 203 B O1-
ATOM 5104 N PRO B 223 -1.937 2.095 445.506 1.00 51.15 B N
ANISOU 5104 N PRO B 223 8491 3535 7407 -825 -103 255 B N
ATOM 5105 CA PRO B 223 -0.489 1.949 445.685 1.00 37.60 B C
ANISOU 5105 CA PRO B 223 6690 1830 5766 -746 147 221 B C
ATOM 5106 C PRO B 223 0.219 1.701 444.358 1.00 50.05 B C
ANISOU 5106 C PRO B 223 8546 3333 7138 -817 291 170 B C
ATOM 5107 O PRO B 223 -0.343 1.133 443.418 1.00 47.81 B O
ANISOU 5107 O PRO B 223 8515 2986 6667 -933 234 141 B O
ATOM 5108 CB PRO B 223 -0.362 0.746 446.627 1.00 40.19 B C
ANISOU 5108 CB PRO B 223 6844 2192 6234 -719 197 196 B C
ATOM 5109 CG PRO B 223 -1.651 0.032 446.548 1.00 37.48 B C
ANISOU 5109 CG PRO B 223 6569 1830 5842 -834 53 194 B C
ATOM 5110 CD PRO B 223 -2.698 1.041 446.195 1.00 49.12 B C
ANISOU 5110 CD PRO B 223 8123 3307 7233 -880 -177 241 B C
ATOM 5111 N GLN B 224 1.466 2.159 444.284 1.00 46.14 B N
ANISOU 5111 N GLN B 224 8023 2843 6665 -762 482 152 B N
ATOM 5112 CA GLN B 224 2.314 1.950 443.122 1.00 47.11 B C
ANISOU 5112 CA GLN B 224 8402 2890 6608 -827 692 91 B C
ATOM 5113 C GLN B 224 3.384 0.919 443.452 1.00 41.07 B C
ANISOU 5113 C GLN B 224 7541 2122 5940 -767 920 13 B C
ATOM 5114 O GLN B 224 4.188 1.142 444.367 1.00 46.92 B O
ANISOU 5114 O GLN B 224 8041 2926 6862 -664 1000 16 B O
ATOM 5115 CB GLN B 224 2.944 3.280 442.706 1.00 48.84 B C
ANISOU 5115 CB GLN B 224 8690 3097 6768 -831 772 122 B C
ATOM 5116 CG GLN B 224 1.920 4.370 442.435 1.00 41.68 B C
ANISOU 5116 CG GLN B 224 7888 2178 5771 -860 529 208 B C
ATOM 5117 CD GLN B 224 1.092 4.073 441.199 1.00 69.71 B C
ANISOU 5117 CD GLN B 224 11804 5642 9039 -986 409 206 B C
ATOM 5118 NE2 GLN B 224 -0.225 3.961 441.379 1.00 64.61 B N
ANISOU 5118 NE2 GLN B 224 11157 5004 8387 -1002 125 246 B N
ATOM 5119 OE1 GLN B 224 1.632 3.894 440.101 1.00 67.56 B O
ANISOU 5119 OE1 GLN B 224 11827 5294 8548 -1080 569 162 B O
ATOM 5120 N PRO B 225 3.430 -0.220 442.774 1.00 47.53 B N
ANISOU 5120 N PRO B 225 8552 2865 6644 -823 1021 -59 B N
ATOM 5121 CA PRO B 225 4.461 -1.214 443.089 1.00 55.37 B C
ANISOU 5121 CA PRO B 225 9464 3832 7743 -743 1243 -135 B C
ATOM 5122 C PRO B 225 5.833 -0.818 442.562 1.00 54.04 B C
ANISOU 5122 C PRO B 225 9351 3617 7564 -726 1559 -197 B C
ATOM 5123 O PRO B 225 5.984 -0.035 441.617 1.00 45.32 B O
ANISOU 5123 O PRO B 225 8458 2470 6292 -818 1647 -199 B O
ATOM 5124 CB PRO B 225 3.951 -2.493 442.411 1.00 44.46 B C
ANISOU 5124 CB PRO B 225 8313 2360 6218 -822 1241 -197 B C
ATOM 5125 CG PRO B 225 3.028 -2.020 441.348 1.00 45.60 B C
ANISOU 5125 CG PRO B 225 8743 2468 6116 -970 1107 -177 B C
ATOM 5126 CD PRO B 225 2.397 -0.764 441.875 1.00 44.00 B C
ANISOU 5126 CD PRO B 225 8380 2351 5985 -953 893 -74 B C
ATOM 5127 N LEU B 226 6.848 -1.372 443.215 1.00 44.01 B N
ANISOU 5127 N LEU B 226 7889 2347 6486 -609 1736 -246 B N
ATOM 5128 CA LEU B 226 8.212 -1.235 442.739 1.00 45.64 B C
ANISOU 5128 CA LEU B 226 8119 2488 6736 -591 2090 -329 B C
ATOM 5129 C LEU B 226 8.444 -2.198 441.586 1.00 53.43 B C
ANISOU 5129 C LEU B 226 9412 3338 7551 -654 2314 -434 B C
ATOM 5130 O LEU B 226 8.159 -3.397 441.697 1.00 48.61 B O
ANISOU 5130 O LEU B 226 8841 2684 6945 -615 2266 -469 B O
ATOM 5131 CB LEU B 226 9.200 -1.510 443.864 1.00 44.98 B C
ANISOU 5131 CB LEU B 226 7702 2440 6947 -433 2189 -347 B C
ATOM 5132 CG LEU B 226 8.923 -0.719 445.127 1.00 42.52 B C
ANISOU 5132 CG LEU B 226 7105 2264 6785 -369 1952 -251 B C
ATOM 5133 CD1 LEU B 226 9.921 -1.098 446.177 1.00 42.30 B C
ANISOU 5133 CD1 LEU B 226 6783 2261 7027 -219 2042 -273 B C
ATOM 5134 CD2 LEU B 226 8.980 0.761 444.827 1.00 42.25 B C
ANISOU 5134 CD2 LEU B 226 7090 2265 6697 -451 1955 -209 B C
ATOM 5135 N HIS B 227 8.964 -1.669 440.484 1.00 50.21 B N
ANISOU 5135 N HIS B 227 9243 2853 6980 -760 2564 -487 B N
ATOM 5136 CA HIS B 227 9.294 -2.452 439.310 1.00 53.06 B C
ANISOU 5136 CA HIS B 227 9934 3076 7150 -835 2830 -600 B C
ATOM 5137 C HIS B 227 10.799 -2.676 439.291 1.00 68.97 B C
ANISOU 5137 C HIS B 227 11826 5019 9359 -758 3253 -710 B C
ATOM 5138 O HIS B 227 11.567 -1.819 439.733 1.00 70.28 B O
ANISOU 5138 O HIS B 227 11765 5226 9711 -729 3380 -699 B O
ATOM 5139 CB HIS B 227 8.850 -1.728 438.041 1.00 54.59 B C
ANISOU 5139 CB HIS B 227 10524 3220 6999 -1024 2845 -589 B C
ATOM 5140 CG HIS B 227 7.365 -1.676 437.855 1.00 60.66 B C
ANISOU 5140 CG HIS B 227 11448 4027 7572 -1105 2448 -502 B C
ATOM 5141 CD2 HIS B 227 6.438 -0.812 438.332 1.00 68.81 B C
ANISOU 5141 CD2 HIS B 227 12365 5159 8621 -1112 2108 -381 B C
ATOM 5142 ND1 HIS B 227 6.671 -2.600 437.104 1.00 70.19 B N
ANISOU 5142 ND1 HIS B 227 12956 5156 8555 -1192 2377 -548 B N
ATOM 5143 CE1 HIS B 227 5.385 -2.302 437.117 1.00 65.63 B C
ANISOU 5143 CE1 HIS B 227 12433 4630 7872 -1258 2009 -458 B C
ATOM 5144 NE2 HIS B 227 5.217 -1.222 437.855 1.00 65.20 B N
ANISOU 5144 NE2 HIS B 227 12125 4680 7967 -1203 1848 -357 B N
ATOM 5145 N MET B 228 11.222 -3.847 438.838 1.00 65.37 B N
ANISOU 5145 N MET B 228 11494 4453 8891 -719 3465 -821 B N
ATOM 5146 CA MET B 228 12.650 -4.091 438.717 1.00 61.75 B C
ANISOU 5146 CA MET B 228 10911 3915 8634 -641 3888 -940 B C
ATOM 5147 C MET B 228 13.192 -3.384 437.489 1.00 61.70 B C
ANISOU 5147 C MET B 228 11193 3822 8429 -816 4252 -1014 B C
ATOM 5148 O MET B 228 12.657 -3.534 436.386 1.00 78.35 B O
ANISOU 5148 O MET B 228 13726 5856 10189 -967 4281 -1037 B O
ATOM 5149 CB MET B 228 12.979 -5.572 438.633 1.00 60.99 B C
ANISOU 5149 CB MET B 228 10843 3726 8604 -522 3997 -1037 B C
ATOM 5150 CG MET B 228 14.460 -5.765 438.445 1.00 73.09 B C
ANISOU 5150 CG MET B 228 12217 5188 10365 -433 4428 -1167 B C
ATOM 5151 SD MET B 228 15.041 -7.422 438.764 1.00 80.78 B S
ANISOU 5151 SD MET B 228 13070 6084 11540 -207 4482 -1260 B S
ATOM 5152 CE MET B 228 14.302 -7.692 440.378 1.00 71.81 B C
ANISOU 5152 CE MET B 228 11637 5064 10583 -59 3986 -1113 B C
ATOM 5153 N ILE B 229 14.240 -2.594 437.688 1.00 62.29 B N
ANISOU 5153 N ILE B 229 11049 3901 8716 -814 4526 -1050 B N
ATOM 5154 CA ILE B 229 14.838 -1.846 436.596 1.00 64.93 B C
ANISOU 5154 CA ILE B 229 11645 4145 8879 -1005 4912 -1122 B C
ATOM 5155 C ILE B 229 16.058 -2.600 436.084 1.00 81.52 B C
ANISOU 5155 C ILE B 229 13711 6139 11123 -964 5390 -1294 B C
ATOM 5156 O ILE B 229 16.031 -3.182 434.991 1.00 82.17 B O
ANISOU 5156 O ILE B 229 14163 6115 10944 -1060 5589 -1372 B O
ATOM 5157 CB ILE B 229 15.198 -0.425 437.057 1.00 63.75 B C
ANISOU 5157 CB ILE B 229 11295 4061 8866 -1069 4924 -1059 B C
ATOM 5158 CG1 ILE B 229 13.936 0.307 437.533 1.00 60.51 B C
ANISOU 5158 CG1 ILE B 229 10905 3782 8306 -1089 4402 -879 B C
ATOM 5159 CG2 ILE B 229 15.882 0.324 435.964 1.00 66.79 B C
ANISOU 5159 CG2 ILE B 229 11957 4339 9081 -1287 5353 -1140 B C
ATOM 5160 CD1 ILE B 229 12.904 0.538 436.444 1.00 61.21 B C
ANISOU 5160 CD1 ILE B 229 11480 3840 7937 -1256 4238 -825 B C
ATOM 5161 N HIS B 230 17.098 -2.676 436.907 1.00 80.00 B N
ANISOU 5161 N HIS B 230 13050 5991 11356 -803 5527 -1348 B N
ATOM 5162 CA HIS B 230 18.283 -3.465 436.616 1.00 72.11 B C
ANISOU 5162 CA HIS B 230 11888 4944 10566 -706 5882 -1498 B C
ATOM 5163 C HIS B 230 18.239 -4.688 437.511 1.00 74.08 B C
ANISOU 5163 C HIS B 230 11876 5233 11038 -438 5624 -1487 B C
ATOM 5164 O HIS B 230 17.428 -4.768 438.435 1.00 76.08 B O
ANISOU 5164 O HIS B 230 12028 5557 11320 -351 5221 -1366 B O
ATOM 5165 CB HIS B 230 19.574 -2.672 436.868 1.00 80.42 B C
ANISOU 5165 CB HIS B 230 12561 6047 11948 -716 6181 -1571 B C
ATOM 5166 CG HIS B 230 19.853 -1.607 435.848 1.00 84.24 B C
ANISOU 5166 CG HIS B 230 13324 6465 12218 -999 6523 -1613 B C
ATOM 5167 CD2 HIS B 230 19.145 -0.512 435.479 1.00 84.82 B C
ANISOU 5167 CD2 HIS B 230 13736 6496 11995 -1219 6481 -1532 B C
ATOM 5168 ND1 HIS B 230 20.990 -1.604 435.071 1.00 85.16 B N
ANISOU 5168 ND1 HIS B 230 13402 6551 12403 -1084 6939 -1750 B N
ATOM 5169 CE1 HIS B 230 20.969 -0.556 434.266 1.00 87.96 B C
ANISOU 5169 CE1 HIS B 230 14072 6842 12506 -1361 7143 -1746 B C
ATOM 5170 NE2 HIS B 230 19.859 0.123 434.492 1.00 77.67 B N
ANISOU 5170 NE2 HIS B 230 13022 5521 10970 -1447 6887 -1615 B N
ATOM 5171 N LYS B 231 19.061 -5.659 437.211 1.00 74.36 B N
ANISOU 5171 N LYS B 231 11833 5218 11203 -315 5840 -1610 B N
ATOM 5172 CA LYS B 231 18.852 -6.787 438.108 1.00 73.30 B C
ANISOU 5172 CA LYS B 231 11519 5103 11230 -71 5539 -1578 B C
ATOM 5173 C LYS B 231 19.767 -6.652 439.319 1.00 89.50 B C
ANISOU 5173 C LYS B 231 13017 7268 13719 135 5458 -1569 B C
ATOM 5174 O LYS B 231 20.959 -6.364 439.153 1.00 96.70 B O
ANISOU 5174 O LYS B 231 13672 8213 14858 160 5744 -1671 B O
ATOM 5175 CB LYS B 231 19.098 -8.117 437.421 1.00 78.55 B C
ANISOU 5175 CB LYS B 231 12379 5648 11820 18 5685 -1697 B C
ATOM 5176 CG LYS B 231 18.341 -9.230 438.110 1.00 81.79 B C
ANISOU 5176 CG LYS B 231 12825 6032 12218 175 5316 -1634 B C
ATOM 5177 CD LYS B 231 18.913 -10.608 437.864 1.00 91.65 B C
ANISOU 5177 CD LYS B 231 14102 7172 13551 360 5429 -1758 B C
ATOM 5178 CE LYS B 231 18.175 -11.620 438.749 1.00 92.37 B C
ANISOU 5178 CE LYS B 231 14200 7234 13662 510 5032 -1679 B C
ATOM 5179 NZ LYS B 231 18.894 -12.928 438.905 1.00 98.95 B N1+
ANISOU 5179 NZ LYS B 231 14953 7968 14677 762 5077 -1786 B N1+
ATOM 5180 N PRO B 232 19.245 -6.803 440.536 1.00 73.52 B N
ANISOU 5180 N PRO B 232 10802 5320 11812 266 5060 -1447 B N
ATOM 5181 CA PRO B 232 20.094 -6.759 441.730 1.00 71.43 B C
ANISOU 5181 CA PRO B 232 10043 5164 11935 467 4935 -1430 B C
ATOM 5182 C PRO B 232 20.699 -8.114 442.059 1.00 71.95 B C
ANISOU 5182 C PRO B 232 9978 5189 12170 726 4888 -1499 B C
ATOM 5183 O PRO B 232 20.142 -9.171 441.762 1.00 72.46 B O
ANISOU 5183 O PRO B 232 10322 5145 12062 776 4812 -1512 B O
ATOM 5184 CB PRO B 232 19.118 -6.307 442.826 1.00 65.30 B C
ANISOU 5184 CB PRO B 232 9207 4474 11132 463 4518 -1260 B C
ATOM 5185 CG PRO B 232 17.811 -6.855 442.379 1.00 63.94 B C
ANISOU 5185 CG PRO B 232 9454 4227 10614 373 4352 -1206 B C
ATOM 5186 CD PRO B 232 17.812 -6.814 440.881 1.00 66.30 B C
ANISOU 5186 CD PRO B 232 10115 4417 10658 199 4690 -1309 B C
ATOM 5187 N GLN B 233 21.875 -8.055 442.687 1.00 73.66 B N
ANISOU 5187 N GLN B 233 9764 5493 12731 893 4920 -1547 B N
ATOM 5188 CA GLN B 233 22.556 -9.253 443.146 1.00 76.15 B C
ANISOU 5188 CA GLN B 233 9912 5782 13239 1175 4837 -1608 B C
ATOM 5189 C GLN B 233 21.763 -10.019 444.190 1.00 80.06 B C
ANISOU 5189 C GLN B 233 10471 6255 13692 1315 4412 -1484 B C
ATOM 5190 O GLN B 233 22.015 -11.213 444.390 1.00 94.77 B O
ANISOU 5190 O GLN B 233 12363 8035 15613 1528 4331 -1529 B O
ATOM 5191 CB GLN B 233 23.911 -8.887 443.739 1.00 78.29 B C
ANISOU 5191 CB GLN B 233 9683 6184 13881 1316 4885 -1666 B C
ATOM 5192 CG GLN B 233 24.569 -7.700 443.081 1.00100.19 B C
ANISOU 5192 CG GLN B 233 12313 9032 16723 1115 5218 -1739 B C
ATOM 5193 CD GLN B 233 25.989 -7.501 443.566 1.00103.33 B C
ANISOU 5193 CD GLN B 233 12207 9563 17490 1257 5274 -1823 B C
ATOM 5194 NE2 GLN B 233 26.242 -6.368 444.218 1.00 80.99 B N
ANISOU 5194 NE2 GLN B 233 9090 6869 14814 1161 5177 -1763 B N
ATOM 5195 OE1 GLN B 233 26.853 -8.361 443.354 1.00114.82 B O
ANISOU 5195 OE1 GLN B 233 13533 11003 19091 1455 5394 -1948 B O
ATOM 5196 N ASN B 234 20.838 -9.363 444.880 1.00 70.84 B N
ANISOU 5196 N ASN B 234 9331 5157 12428 1205 4140 -1332 B N
ATOM 5197 CA ASN B 234 19.989 -10.020 445.865 1.00 67.48 B C
ANISOU 5197 CA ASN B 234 8992 4718 11930 1294 3746 -1208 B C
ATOM 5198 C ASN B 234 18.549 -9.638 445.565 1.00 73.20 B C
ANISOU 5198 C ASN B 234 10041 5431 12341 1066 3629 -1112 B C
ATOM 5199 O ASN B 234 18.210 -8.449 445.568 1.00 82.96 B O
ANISOU 5199 O ASN B 234 11233 6758 13529 902 3629 -1052 B O
ATOM 5200 CB ASN B 234 20.394 -9.612 447.285 1.00 77.64 B C
ANISOU 5200 CB ASN B 234 9913 6140 13447 1421 3474 -1115 B C
ATOM 5201 CG ASN B 234 19.364 -10.003 448.325 1.00 87.77 B C
ANISOU 5201 CG ASN B 234 11315 7428 14606 1444 3080 -967 B C
ATOM 5202 ND2 ASN B 234 18.654 -9.001 448.879 1.00 90.72 B N
ANISOU 5202 ND2 ASN B 234 11646 7914 14910 1299 2911 -849 B N
ATOM 5203 OD1 ASN B 234 19.193 -11.186 448.621 1.00 64.37 B O
ANISOU 5203 OD1 ASN B 234 8492 4361 11605 1585 2937 -964 B O
ATOM 5204 N THR B 235 17.700 -10.635 445.343 1.00 64.21 B N
ANISOU 5204 N THR B 235 9219 4182 10997 1057 3507 -1100 B N
ATOM 5205 CA THR B 235 16.333 -10.404 444.896 1.00 61.90 B C
ANISOU 5205 CA THR B 235 9245 3880 10395 836 3396 -1031 B C
ATOM 5206 C THR B 235 15.344 -10.349 446.049 1.00 58.68 B C
ANISOU 5206 C THR B 235 8800 3552 9942 821 3001 -878 B C
ATOM 5207 O THR B 235 14.137 -10.229 445.813 1.00 56.85 B O
ANISOU 5207 O THR B 235 8793 3332 9474 652 2854 -816 B O
ATOM 5208 CB THR B 235 15.914 -11.465 443.881 1.00 80.06 B C
ANISOU 5208 CB THR B 235 11920 6018 12480 790 3498 -1116 B C
ATOM 5209 CG2 THR B 235 14.796 -10.933 442.987 1.00 78.26 B C
ANISOU 5209 CG2 THR B 235 12012 5795 11929 527 3497 -1088 B C
ATOM 5210 OG1 THR B 235 17.033 -11.761 443.046 1.00 92.12 B O
ANISOU 5210 OG1 THR B 235 13436 7464 14101 870 3857 -1270 B O
ATOM 5211 N GLU B 236 15.817 -10.482 447.282 1.00 58.25 B N
ANISOU 5211 N GLU B 236 8478 3557 10099 992 2819 -820 B N
ATOM 5212 CA GLU B 236 14.924 -10.371 448.423 1.00 55.41 B C
ANISOU 5212 CA GLU B 236 8089 3279 9686 966 2472 -677 B C
ATOM 5213 C GLU B 236 14.507 -8.913 448.626 1.00 54.78 B C
ANISOU 5213 C GLU B 236 7887 3356 9573 819 2420 -600 B C
ATOM 5214 O GLU B 236 15.284 -7.976 448.389 1.00 52.98 B O
ANISOU 5214 O GLU B 236 7469 3185 9476 808 2604 -640 B O
ATOM 5215 CB GLU B 236 15.608 -10.982 449.649 1.00 56.25 B C
ANISOU 5215 CB GLU B 236 7994 3384 9996 1194 2301 -643 B C
ATOM 5216 CG GLU B 236 15.964 -12.449 449.340 1.00 97.73 B C
ANISOU 5216 CG GLU B 236 13413 8454 15266 1346 2347 -727 B C
ATOM 5217 CD GLU B 236 17.023 -13.049 450.242 1.00 96.64 B C
ANISOU 5217 CD GLU B 236 13070 8290 15360 1619 2256 -739 B C
ATOM 5218 OE1 GLU B 236 17.160 -12.569 451.384 1.00 94.30 B O
ANISOU 5218 OE1 GLU B 236 12568 8107 15156 1675 2056 -643 B O
ATOM 5219 OE2 GLU B 236 17.709 -14.009 449.799 1.00 82.46 B O1-
ANISOU 5219 OE2 GLU B 236 11331 6356 13644 1782 2377 -847 B O1-
ATOM 5220 N ALA B 237 13.262 -8.741 449.080 1.00 51.47 B N
ANISOU 5220 N ALA B 237 7575 2996 8984 703 2167 -495 B N
ATOM 5221 CA ALA B 237 12.631 -7.426 449.157 1.00 47.62 B C
ANISOU 5221 CA ALA B 237 7034 2643 8417 556 2090 -426 B C
ATOM 5222 C ALA B 237 13.407 -6.474 450.058 1.00 63.64 B C
ANISOU 5222 C ALA B 237 8734 4788 10658 632 2068 -390 B C
ATOM 5223 O ALA B 237 13.952 -6.870 451.097 1.00 47.16 B O
ANISOU 5223 O ALA B 237 6467 2721 8729 783 1953 -361 B O
ATOM 5224 CB ALA B 237 11.196 -7.561 449.674 1.00 45.48 B C
ANISOU 5224 CB ALA B 237 6890 2423 7967 453 1800 -325 B C
ATOM 5225 N VAL B 238 13.451 -5.194 449.654 1.00 45.94 B N
ANISOU 5225 N VAL B 238 6430 2613 8410 519 2166 -390 B N
ATOM 5226 CA VAL B 238 14.215 -4.202 450.397 1.00 45.44 B C
ANISOU 5226 CA VAL B 238 6060 2644 8559 563 2165 -370 B C
ATOM 5227 C VAL B 238 13.317 -3.595 451.459 1.00 42.72 B C
ANISOU 5227 C VAL B 238 5662 2427 8140 523 1867 -252 B C
ATOM 5228 O VAL B 238 12.142 -3.325 451.209 1.00 48.38 B O
ANISOU 5228 O VAL B 238 6562 3178 8642 402 1748 -203 B O
ATOM 5229 CB VAL B 238 14.785 -3.131 449.450 1.00 53.09 B C
ANISOU 5229 CB VAL B 238 7003 3594 9574 454 2441 -438 B C
ATOM 5230 CG1 VAL B 238 15.636 -2.114 450.218 1.00 46.06 B C
ANISOU 5230 CG1 VAL B 238 5779 2783 8939 484 2445 -430 B C
ATOM 5231 CG2 VAL B 238 15.602 -3.795 448.347 1.00 49.24 B C
ANISOU 5231 CG2 VAL B 238 6601 2977 9130 479 2773 -569 B C
ATOM 5232 N ASN B 239 13.872 -3.367 452.645 1.00 50.80 B N
ANISOU 5232 N ASN B 239 6435 3527 9342 624 1744 -214 B N
ATOM 5233 CA ASN B 239 13.117 -2.766 453.741 1.00 49.93 B C
ANISOU 5233 CA ASN B 239 6269 3536 9165 592 1488 -114 B C
ATOM 5234 C ASN B 239 12.881 -1.272 453.500 1.00 59.93 B C
ANISOU 5234 C ASN B 239 7489 4874 10407 468 1510 -102 B C
ATOM 5235 O ASN B 239 13.824 -0.509 453.251 1.00 61.36 B O
ANISOU 5235 O ASN B 239 7508 5042 10764 457 1668 -152 B O
ATOM 5236 CB ASN B 239 13.871 -2.965 455.052 1.00 40.61 B C
ANISOU 5236 CB ASN B 239 4861 2402 8167 734 1353 -85 B C
ATOM 5237 CG ASN B 239 13.033 -2.641 456.241 1.00 50.65 B C
ANISOU 5237 CG ASN B 239 6133 3776 9337 711 1103 11 B C
ATOM 5238 ND2 ASN B 239 13.288 -3.325 457.345 1.00 39.18 B N
ANISOU 5238 ND2 ASN B 239 4629 2327 7931 829 950 54 B N
ATOM 5239 OD1 ASN B 239 12.178 -1.752 456.189 1.00 62.62 B O
ANISOU 5239 OD1 ASN B 239 7699 5363 10730 594 1050 45 B O
ATOM 5240 N LEU B 240 11.628 -0.835 453.608 1.00 36.92 B N
ANISOU 5240 N LEU B 240 4711 2029 7290 374 1349 -38 B N
ATOM 5241 CA LEU B 240 11.308 0.557 453.321 1.00 40.91 B C
ANISOU 5241 CA LEU B 240 5216 2588 7739 268 1344 -24 B C
ATOM 5242 C LEU B 240 10.918 1.357 454.546 1.00 34.88 B C
ANISOU 5242 C LEU B 240 4319 1943 6990 279 1140 40 B C
ATOM 5243 O LEU B 240 10.547 2.525 454.402 1.00 49.59 B O
ANISOU 5243 O LEU B 240 6200 3849 8792 203 1103 56 B O
ATOM 5244 CB LEU B 240 10.169 0.660 452.308 1.00 35.39 B C
ANISOU 5244 CB LEU B 240 4784 1870 6792 150 1316 -12 B C
ATOM 5245 CG LEU B 240 10.130 -0.256 451.104 1.00 36.82 B C
ANISOU 5245 CG LEU B 240 5180 1936 6875 114 1460 -67 B C
ATOM 5246 CD1 LEU B 240 8.861 -0.008 450.326 1.00 44.82 B C
ANISOU 5246 CD1 LEU B 240 6431 2948 7650 -10 1347 -38 B C
ATOM 5247 CD2 LEU B 240 11.333 0.070 450.269 1.00 38.65 B C
ANISOU 5247 CD2 LEU B 240 5381 2083 7221 101 1752 -148 B C
ATOM 5248 N SER B 241 11.046 0.797 455.744 1.00 34.09 B N
ANISOU 5248 N SER B 241 4105 1885 6964 373 1011 74 B N
ATOM 5249 CA SER B 241 10.334 1.382 456.880 1.00 48.08 B C
ANISOU 5249 CA SER B 241 5826 3762 8678 367 815 134 B C
ATOM 5250 C SER B 241 10.873 2.742 457.352 1.00 48.84 B C
ANISOU 5250 C SER B 241 5753 3908 8895 350 794 127 B C
ATOM 5251 O SER B 241 10.199 3.388 458.162 1.00 58.06 B O
ANISOU 5251 O SER B 241 6909 5156 9995 335 650 164 B O
ATOM 5252 CB SER B 241 10.286 0.376 458.036 1.00 40.01 B C
ANISOU 5252 CB SER B 241 4780 2754 7670 457 689 177 B C
ATOM 5253 OG SER B 241 11.550 -0.162 458.300 1.00 44.23 B O
ANISOU 5253 OG SER B 241 5178 3237 8390 564 734 149 B O
ATOM 5254 N SER B 242 12.044 3.198 456.884 1.00 33.57 B N
ANISOU 5254 N SER B 242 3690 1916 7149 346 944 72 B N
ATOM 5255 CA SER B 242 12.602 4.465 457.352 1.00 42.20 B C
ANISOU 5255 CA SER B 242 4622 3028 8382 314 921 58 B C
ATOM 5256 C SER B 242 11.964 5.710 456.721 1.00 49.46 B C
ANISOU 5256 C SER B 242 5674 3956 9162 200 936 63 B C
ATOM 5257 O SER B 242 12.081 6.807 457.289 1.00 48.93 B O
ANISOU 5257 O SER B 242 5529 3914 9150 170 860 65 B O
ATOM 5258 CB SER B 242 14.118 4.507 457.120 1.00 40.97 B C
ANISOU 5258 CB SER B 242 4251 2790 8525 339 1088 -14 B C
ATOM 5259 OG SER B 242 14.813 3.978 458.236 1.00 47.14 B O
ANISOU 5259 OG SER B 242 4835 3603 9473 454 960 -11 B O
ATOM 5260 N GLY B 243 11.327 5.591 455.564 1.00 35.41 B N
ANISOU 5260 N GLY B 243 4109 2144 7201 137 1013 65 B N
ATOM 5261 CA GLY B 243 10.725 6.727 454.912 1.00 39.11 B C
ANISOU 5261 CA GLY B 243 4734 2609 7516 41 996 79 B C
ATOM 5262 C GLY B 243 9.285 6.930 455.321 1.00 37.63 B C
ANISOU 5262 C GLY B 243 4659 2501 7138 53 790 132 B C
ATOM 5263 O GLY B 243 8.822 6.426 456.344 1.00 48.56 B O
ANISOU 5263 O GLY B 243 5968 3958 8527 119 668 156 B O
ATOM 5264 N VAL B 244 8.564 7.681 454.497 1.00 32.49 B N
ANISOU 5264 N VAL B 244 4195 1823 6327 -16 758 149 B N
ATOM 5265 CA VAL B 244 7.139 7.888 454.692 1.00 40.14 B C
ANISOU 5265 CA VAL B 244 5263 2839 7149 -3 584 189 B C
ATOM 5266 C VAL B 244 6.306 7.242 453.593 1.00 34.56 B C
ANISOU 5266 C VAL B 244 4761 2078 6294 -50 574 204 B C
ATOM 5267 O VAL B 244 5.098 7.048 453.792 1.00 37.83 B O
ANISOU 5267 O VAL B 244 5219 2521 6634 -35 444 232 B O
ATOM 5268 CB VAL B 244 6.792 9.388 454.791 1.00 29.50 B C
ANISOU 5268 CB VAL B 244 3964 1484 5759 -21 497 203 B C
ATOM 5269 CG1 VAL B 244 7.453 10.018 455.987 1.00 31.74 B C
ANISOU 5269 CG1 VAL B 244 4061 1816 6184 17 475 184 B C
ATOM 5270 CG2 VAL B 244 7.206 10.071 453.528 1.00 30.69 B C
ANISOU 5270 CG2 VAL B 244 4291 1528 5842 -117 585 202 B C
ATOM 5271 N LEU B 245 6.906 6.870 452.465 1.00 34.68 B N
ANISOU 5271 N LEU B 245 4891 2006 6280 -112 717 180 B N
ATOM 5272 CA LEU B 245 6.121 6.441 451.318 1.00 42.85 B C
ANISOU 5272 CA LEU B 245 6154 2967 7161 -178 687 193 B C
ATOM 5273 C LEU B 245 5.652 5.001 451.410 1.00 42.68 B C
ANISOU 5273 C LEU B 245 6143 2950 7122 -159 669 185 B C
ATOM 5274 O LEU B 245 4.736 4.643 450.660 1.00 55.19 B O
ANISOU 5274 O LEU B 245 7899 4478 8591 -220 590 201 B O
ATOM 5275 CB LEU B 245 6.900 6.641 450.003 1.00 33.26 B C
ANISOU 5275 CB LEU B 245 5094 1647 5897 -269 867 166 B C
ATOM 5276 CG LEU B 245 7.155 8.095 449.544 1.00 33.93 B C
ANISOU 5276 CG LEU B 245 5267 1684 5939 -337 875 188 B C
ATOM 5277 CD1 LEU B 245 7.791 8.211 448.153 1.00 38.42 B C
ANISOU 5277 CD1 LEU B 245 6036 2145 6415 -451 1078 166 B C
ATOM 5278 CD2 LEU B 245 5.915 8.958 449.598 1.00 33.36 B C
ANISOU 5278 CD2 LEU B 245 5297 1604 5773 -331 629 251 B C
ATOM 5279 N ARG B 246 6.206 4.203 452.331 1.00 41.72 B N
ANISOU 5279 N ARG B 246 5854 2879 7119 -82 718 168 B N
ATOM 5280 CA ARG B 246 5.863 2.783 452.429 1.00 42.60 B C
ANISOU 5280 CA ARG B 246 6002 2971 7211 -68 708 163 B C
ATOM 5281 C ARG B 246 4.349 2.552 452.401 1.00 46.52 B C
ANISOU 5281 C ARG B 246 6603 3474 7599 -121 544 201 B C
ATOM 5282 O ARG B 246 3.580 3.257 453.070 1.00 45.90 B O
ANISOU 5282 O ARG B 246 6450 3463 7528 -106 428 236 B O
ATOM 5283 CB ARG B 246 6.457 2.194 453.710 1.00 40.28 B C
ANISOU 5283 CB ARG B 246 5515 2735 7055 31 715 165 B C
ATOM 5284 CG ARG B 246 5.993 0.804 454.020 1.00 31.05 B C
ANISOU 5284 CG ARG B 246 4401 1540 5857 45 676 176 B C
ATOM 5285 CD ARG B 246 6.620 0.260 455.287 1.00 30.97 B C
ANISOU 5285 CD ARG B 246 4234 1565 5970 146 662 191 B C
ATOM 5286 NE ARG B 246 6.444 1.123 456.448 1.00 39.91 B N
ANISOU 5286 NE ARG B 246 5212 2800 7150 177 562 227 B N
ATOM 5287 CZ ARG B 246 5.411 1.052 457.288 1.00 45.84 B C
ANISOU 5287 CZ ARG B 246 5956 3606 7854 164 447 271 B C
ATOM 5288 NH1 ARG B 246 4.451 0.157 457.094 1.00 29.30 B N1+
ANISOU 5288 NH1 ARG B 246 3987 1471 5675 106 414 291 B N1+
ATOM 5289 NH2 ARG B 246 5.339 1.871 458.332 1.00 43.69 B N
ANISOU 5289 NH2 ARG B 246 5553 3417 7633 197 374 292 B N
ATOM 5290 N ALA B 247 3.936 1.540 451.629 1.00 34.13 B N
ANISOU 5290 N ALA B 247 5194 1821 5952 -186 549 188 B N
ATOM 5291 CA ALA B 247 2.528 1.249 451.405 1.00 31.64 B C
ANISOU 5291 CA ALA B 247 4985 1478 5559 -269 406 219 B C
ATOM 5292 C ALA B 247 1.860 0.741 452.680 1.00 30.83 B C
ANISOU 5292 C ALA B 247 4751 1448 5515 -241 338 250 B C
ATOM 5293 O ALA B 247 2.513 0.289 453.617 1.00 53.10 B O
ANISOU 5293 O ALA B 247 7451 4315 8409 -163 389 250 B O
ATOM 5294 CB ALA B 247 2.366 0.218 450.299 1.00 33.02 B C
ANISOU 5294 CB ALA B 247 5352 1537 5656 -358 433 189 B C
ATOM 5295 N VAL B 248 0.538 0.872 452.722 1.00 31.74 B N
ANISOU 5295 N VAL B 248 4878 1565 5619 -310 227 280 B N
ATOM 5296 CA VAL B 248 -0.272 0.514 453.882 1.00 30.31 B C
ANISOU 5296 CA VAL B 248 4546 1450 5523 -312 173 314 B C
ATOM 5297 C VAL B 248 -0.940 -0.833 453.649 1.00 40.36 B C
ANISOU 5297 C VAL B 248 5936 2645 6755 -434 159 315 B C
ATOM 5298 O VAL B 248 -1.516 -1.071 452.579 1.00 46.08 B O
ANISOU 5298 O VAL B 248 6821 3279 7408 -549 116 299 B O
ATOM 5299 CB VAL B 248 -1.341 1.584 454.155 1.00 30.00 B C
ANISOU 5299 CB VAL B 248 4368 1461 5569 -309 52 343 B C
ATOM 5300 CG1 VAL B 248 -2.115 1.252 455.422 1.00 29.75 B C
ANISOU 5300 CG1 VAL B 248 4150 1494 5659 -317 6 376 B C
ATOM 5301 CG2 VAL B 248 -0.726 2.967 454.213 1.00 29.35 B C
ANISOU 5301 CG2 VAL B 248 4228 1425 5498 -204 57 337 B C
ATOM 5302 N SER B 249 -0.924 -1.687 454.672 1.00 35.41 B N
ANISOU 5302 N SER B 249 5245 2040 6168 -426 183 337 B N
ATOM 5303 CA SER B 249 -1.658 -2.938 454.639 1.00 32.25 B C
ANISOU 5303 CA SER B 249 4952 1569 5735 -563 165 346 B C
ATOM 5304 C SER B 249 -3.112 -2.675 454.309 1.00 37.71 B C
ANISOU 5304 C SER B 249 5587 2265 6475 -712 57 357 B C
ATOM 5305 O SER B 249 -3.769 -1.928 455.045 1.00 39.90 B O
ANISOU 5305 O SER B 249 5647 2634 6880 -696 -16 391 B O
ATOM 5306 CB SER B 249 -1.582 -3.629 455.996 1.00 39.30 B C
ANISOU 5306 CB SER B 249 5766 2490 6677 -538 191 389 B C
ATOM 5307 OG SER B 249 -2.590 -4.623 456.137 1.00 42.33 B O
ANISOU 5307 OG SER B 249 6216 2822 7045 -710 164 412 B O
ATOM 5308 N PRO B 250 -3.664 -3.274 453.252 1.00 39.08 B N
ANISOU 5308 N PRO B 250 5934 2342 6573 -863 18 327 B N
ATOM 5309 CA PRO B 250 -5.084 -3.049 452.946 1.00 35.05 B C
ANISOU 5309 CA PRO B 250 5325 1858 6133 -1022 -166 339 B C
ATOM 5310 C PRO B 250 -6.003 -3.389 454.095 1.00 35.31 B C
ANISOU 5310 C PRO B 250 5147 2021 6247 -1103 -203 371 B C
ATOM 5311 O PRO B 250 -7.106 -2.847 454.155 1.00 35.88 B O
ANISOU 5311 O PRO B 250 5028 2266 6338 -1150 -337 363 B O
ATOM 5312 CB PRO B 250 -5.328 -3.948 451.734 1.00 36.66 B C
ANISOU 5312 CB PRO B 250 5783 1950 6197 -1179 -183 287 B C
ATOM 5313 CG PRO B 250 -4.012 -4.052 451.091 1.00 36.37 B C
ANISOU 5313 CG PRO B 250 5903 1811 6105 -1047 12 244 B C
ATOM 5314 CD PRO B 250 -3.013 -4.096 452.224 1.00 36.27 B C
ANISOU 5314 CD PRO B 250 5863 1850 6069 -901 66 284 B C
ATOM 5315 N LEU B 251 -5.590 -4.264 455.013 1.00 35.18 B N
ANISOU 5315 N LEU B 251 5162 1954 6249 -1108 -81 401 B N
ATOM 5316 CA LEU B 251 -6.357 -4.460 456.238 1.00 41.70 B C
ANISOU 5316 CA LEU B 251 5798 2907 7139 -1180 -81 441 B C
ATOM 5317 C LEU B 251 -6.588 -3.140 456.953 1.00 42.49 B C
ANISOU 5317 C LEU B 251 5633 3202 7309 -1037 -116 446 B C
ATOM 5318 O LEU B 251 -7.707 -2.829 457.366 1.00 46.63 B O
ANISOU 5318 O LEU B 251 5945 3909 7863 -1104 -177 434 B O
ATOM 5319 CB LEU B 251 -5.637 -5.432 457.167 1.00 44.91 B C
ANISOU 5319 CB LEU B 251 6325 3225 7514 -1155 51 484 B C
ATOM 5320 CG LEU B 251 -5.480 -6.878 456.692 1.00 50.97 B C
ANISOU 5320 CG LEU B 251 7376 3852 8138 -1270 101 464 B C
ATOM 5321 CD1 LEU B 251 -5.137 -7.709 457.886 1.00 49.46 B C
ANISOU 5321 CD1 LEU B 251 7253 3626 7914 -1260 170 526 B C
ATOM 5322 CD2 LEU B 251 -6.722 -7.415 455.977 1.00 38.52 B C
ANISOU 5322 CD2 LEU B 251 5816 2265 6553 -1531 28 430 B C
ATOM 5323 N HIS B 252 -5.529 -2.359 457.127 1.00 46.54 B N
ANISOU 5323 N HIS B 252 6149 3675 7859 -841 -69 453 B N
ATOM 5324 CA HIS B 252 -5.639 -1.094 457.842 1.00 44.67 B C
ANISOU 5324 CA HIS B 252 5698 3590 7682 -700 -96 450 B C
ATOM 5325 C HIS B 252 -6.302 -0.003 456.997 1.00 47.40 B C
ANISOU 5325 C HIS B 252 5954 4024 8031 -661 -232 410 B C
ATOM 5326 O HIS B 252 -6.989 0.871 457.546 1.00 32.48 B O
ANISOU 5326 O HIS B 252 3854 2294 6195 -594 -287 393 B O
ATOM 5327 CB HIS B 252 -4.265 -0.628 458.307 1.00 33.89 B C
ANISOU 5327 CB HIS B 252 4372 2147 6359 -526 -15 467 B C
ATOM 5328 CG HIS B 252 -4.320 0.646 459.074 1.00 36.06 B C
ANISOU 5328 CG HIS B 252 4463 2553 6684 -393 -41 456 B C
ATOM 5329 CD2 HIS B 252 -3.787 1.864 458.827 1.00 29.27 B C
ANISOU 5329 CD2 HIS B 252 3574 1690 5858 -258 -69 434 B C
ATOM 5330 ND1 HIS B 252 -5.053 0.768 460.234 1.00 30.41 B N
ANISOU 5330 ND1 HIS B 252 3587 1989 5981 -405 -31 459 B N
ATOM 5331 CE1 HIS B 252 -4.943 2.004 460.683 1.00 31.36 B C
ANISOU 5331 CE1 HIS B 252 3588 2187 6141 -266 -54 432 B C
ATOM 5332 NE2 HIS B 252 -4.188 2.689 459.844 1.00 31.56 B N
ANISOU 5332 NE2 HIS B 252 3692 2115 6182 -179 -86 419 B N
ATOM 5333 N MET B 253 -6.057 0.014 455.675 1.00 44.40 B N
ANISOU 5333 N MET B 253 5750 3531 7589 -686 -288 394 B N
ATOM 5334 CA MET B 253 -6.842 0.883 454.800 1.00 33.41 B C
ANISOU 5334 CA MET B 253 4312 2208 6175 -674 -457 370 B C
ATOM 5335 C MET B 253 -8.333 0.619 454.999 1.00 46.76 B C
ANISOU 5335 C MET B 253 5803 4069 7896 -792 -574 349 B C
ATOM 5336 O MET B 253 -9.126 1.553 455.139 1.00 55.80 B O
ANISOU 5336 O MET B 253 6741 5357 9102 -710 -690 329 B O
ATOM 5337 CB MET B 253 -6.447 0.692 453.334 1.00 33.95 B C
ANISOU 5337 CB MET B 253 4651 2119 6129 -732 -496 359 B C
ATOM 5338 CG MET B 253 -5.016 1.066 452.979 1.00 71.25 B C
ANISOU 5338 CG MET B 253 9551 6689 10830 -628 -365 366 B C
ATOM 5339 SD MET B 253 -4.601 2.804 453.184 1.00 54.99 B S
ANISOU 5339 SD MET B 253 7398 4671 8825 -436 -396 378 B S
ATOM 5340 CE MET B 253 -3.757 3.232 451.670 1.00 47.58 B C
ANISOU 5340 CE MET B 253 6766 3554 7759 -449 -367 375 B C
ATOM 5341 N GLN B 254 -8.721 -0.658 455.066 1.00 36.81 B N
ANISOU 5341 N GLN B 254 4588 2790 6606 -984 -538 349 B N
ATOM 5342 CA GLN B 254 -10.112 -1.023 455.304 1.00 37.65 B C
ANISOU 5342 CA GLN B 254 4485 3066 6755 -1137 -625 324 B C
ATOM 5343 C GLN B 254 -10.557 -0.613 456.698 1.00 47.50 B C
ANISOU 5343 C GLN B 254 5455 4493 8102 -1073 -541 323 B C
ATOM 5344 O GLN B 254 -11.694 -0.169 456.892 1.00 54.05 B O
ANISOU 5344 O GLN B 254 6015 5514 9008 -1086 -627 283 B O
ATOM 5345 CB GLN B 254 -10.288 -2.531 455.127 1.00 46.09 B C
ANISOU 5345 CB GLN B 254 5709 4042 7762 -1380 -577 328 B C
ATOM 5346 CG GLN B 254 -11.721 -2.955 455.063 1.00 41.04 B C
ANISOU 5346 CG GLN B 254 4876 3560 7156 -1587 -690 292 B C
ATOM 5347 CD GLN B 254 -12.512 -2.089 454.115 1.00 50.15 B C
ANISOU 5347 CD GLN B 254 5904 4822 8328 -1544 -929 250 B C
ATOM 5348 NE2 GLN B 254 -13.524 -1.419 454.646 1.00 57.93 B N
ANISOU 5348 NE2 GLN B 254 6538 6037 9437 -1499 -1000 220 B N
ATOM 5349 OE1 GLN B 254 -12.183 -1.970 452.935 1.00 42.29 B O
ANISOU 5349 OE1 GLN B 254 5132 3701 7235 -1533 -1046 245 B O
ATOM 5350 N TYR B 255 -9.683 -0.797 457.685 1.00 52.13 B N
ANISOU 5350 N TYR B 255 6102 5020 8685 -1007 -372 361 B N
ATOM 5351 CA TYR B 255 -9.981 -0.384 459.052 1.00 55.92 B C
ANISOU 5351 CA TYR B 255 6371 5652 9224 -945 -276 358 B C
ATOM 5352 C TYR B 255 -10.320 1.093 459.110 1.00 61.47 B C
ANISOU 5352 C TYR B 255 6874 6482 10001 -749 -359 312 B C
ATOM 5353 O TYR B 255 -11.290 1.488 459.765 1.00 37.10 B O
ANISOU 5353 O TYR B 255 3527 3584 6984 -740 -351 267 B O
ATOM 5354 CB TYR B 255 -8.789 -0.716 459.947 1.00 49.97 B C
ANISOU 5354 CB TYR B 255 5771 4782 8433 -878 -127 411 B C
ATOM 5355 CG TYR B 255 -8.849 -0.200 461.365 1.00 34.54 B C
ANISOU 5355 CG TYR B 255 3669 2954 6501 -794 -30 411 B C
ATOM 5356 CD1 TYR B 255 -8.472 1.103 461.648 1.00 33.54 B C
ANISOU 5356 CD1 TYR B 255 3457 2871 6416 -585 -52 380 B C
ATOM 5357 CD2 TYR B 255 -9.232 -1.011 462.416 1.00 35.54 B C
ANISOU 5357 CD2 TYR B 255 3779 3136 6588 -932 90 440 B C
ATOM 5358 CE1 TYR B 255 -8.490 1.604 462.931 1.00 33.52 B C
ANISOU 5358 CE1 TYR B 255 3351 2972 6415 -508 36 367 B C
ATOM 5359 CE2 TYR B 255 -9.246 -0.527 463.715 1.00 35.56 B C
ANISOU 5359 CE2 TYR B 255 3686 3247 6579 -860 188 435 B C
ATOM 5360 CZ TYR B 255 -8.876 0.790 463.963 1.00 56.43 B C
ANISOU 5360 CZ TYR B 255 6241 5938 9262 -643 158 392 B C
ATOM 5361 OH TYR B 255 -8.893 1.307 465.246 1.00 57.09 B O
ANISOU 5361 OH TYR B 255 6253 6123 9318 -573 253 374 B O
ATOM 5362 N LEU B 256 -9.506 1.925 458.446 1.00 48.94 B N
ANISOU 5362 N LEU B 256 5412 4781 8402 -589 -424 318 B N
ATOM 5363 CA LEU B 256 -9.772 3.356 458.395 1.00 47.00 B C
ANISOU 5363 CA LEU B 256 5030 4609 8219 -398 -519 280 B C
ATOM 5364 C LEU B 256 -11.057 3.657 457.630 1.00 37.41 B C
ANISOU 5364 C LEU B 256 3651 3510 7052 -421 -707 239 B C
ATOM 5365 O LEU B 256 -11.839 4.514 458.049 1.00 39.25 B O
ANISOU 5365 O LEU B 256 3644 3889 7379 -301 -758 189 B O
ATOM 5366 CB LEU B 256 -8.581 4.084 457.779 1.00 44.06 B C
ANISOU 5366 CB LEU B 256 4867 4065 7809 -266 -538 305 B C
ATOM 5367 CG LEU B 256 -7.301 4.065 458.615 1.00 47.06 B C
ANISOU 5367 CG LEU B 256 5343 4358 8179 -202 -382 331 B C
ATOM 5368 CD1 LEU B 256 -6.129 4.696 457.860 1.00 47.18 B C
ANISOU 5368 CD1 LEU B 256 5548 4208 8168 -113 -388 348 B C
ATOM 5369 CD2 LEU B 256 -7.541 4.793 459.915 1.00 51.43 B C
ANISOU 5369 CD2 LEU B 256 5714 5039 8789 -91 -328 298 B C
ATOM 5370 N ARG B 257 -11.314 2.937 456.537 1.00 37.49 B N
ANISOU 5370 N ARG B 257 3781 3459 7003 -572 -816 251 B N
ATOM 5371 CA ARG B 257 -12.593 3.081 455.850 1.00 39.70 B C
ANISOU 5371 CA ARG B 257 3888 3865 7332 -619 -1024 212 B C
ATOM 5372 C ARG B 257 -13.756 2.854 456.807 1.00 41.34 B C
ANISOU 5372 C ARG B 257 3744 4304 7657 -687 -974 159 B C
ATOM 5373 O ARG B 257 -14.656 3.695 456.911 1.00 50.68 B O
ANISOU 5373 O ARG B 257 4656 5643 8957 -564 -1083 104 B O
ATOM 5374 CB ARG B 257 -12.669 2.114 454.671 1.00 40.56 B C
ANISOU 5374 CB ARG B 257 4204 3872 7336 -821 -1130 228 B C
ATOM 5375 CG ARG B 257 -11.884 2.584 453.471 1.00 39.91 B C
ANISOU 5375 CG ARG B 257 4427 3601 7138 -745 -1230 259 B C
ATOM 5376 CD ARG B 257 -12.094 1.709 452.248 1.00 41.23 B C
ANISOU 5376 CD ARG B 257 4808 3676 7182 -943 -1354 258 B C
ATOM 5377 NE ARG B 257 -10.942 1.760 451.348 1.00 49.65 B N
ANISOU 5377 NE ARG B 257 6244 4521 8101 -918 -1310 289 B N
ATOM 5378 CZ ARG B 257 -10.016 0.816 451.280 1.00 41.86 B C
ANISOU 5378 CZ ARG B 257 5491 3379 7035 -1014 -1126 297 B C
ATOM 5379 NH1 ARG B 257 -10.129 -0.248 452.049 1.00 54.31 B N1+
ANISOU 5379 NH1 ARG B 257 6998 4983 8655 -1142 -998 291 B N1+
ATOM 5380 NH2 ARG B 257 -8.998 0.931 450.444 1.00 38.66 B N
ANISOU 5380 NH2 ARG B 257 5391 2789 6510 -984 -1067 311 B N
ATOM 5381 N ASN B 258 -13.737 1.725 457.535 1.00 42.50 B N
ANISOU 5381 N ASN B 258 3899 4471 7779 -880 -797 173 B N
ATOM 5382 CA ASN B 258 -14.786 1.388 458.497 1.00 43.09 B C
ANISOU 5382 CA ASN B 258 3668 4761 7945 -993 -698 126 B C
ATOM 5383 C ASN B 258 -14.895 2.420 459.608 1.00 42.88 B C
ANISOU 5383 C ASN B 258 3432 4862 7999 -787 -587 83 B C
ATOM 5384 O ASN B 258 -15.916 2.465 460.308 1.00 61.54 B O
ANISOU 5384 O ASN B 258 5487 7436 10460 -829 -517 18 B O
ATOM 5385 CB ASN B 258 -14.535 0.022 459.144 1.00 44.71 B C
ANISOU 5385 CB ASN B 258 4005 4911 8071 -1233 -505 170 B C
ATOM 5386 CG ASN B 258 -14.473 -1.105 458.148 1.00 43.54 B C
ANISOU 5386 CG ASN B 258 4079 4624 7841 -1455 -589 198 B C
ATOM 5387 ND2 ASN B 258 -14.291 -2.314 458.652 1.00 43.77 B N
ANISOU 5387 ND2 ASN B 258 4249 4578 7805 -1663 -438 238 B N
ATOM 5388 OD1 ASN B 258 -14.631 -0.907 456.951 1.00 44.02 B O
ANISOU 5388 OD1 ASN B 258 4200 4638 7888 -1447 -791 183 B O
ATOM 5389 N PHE B 259 -13.845 3.204 459.825 1.00 40.79 B N
ANISOU 5389 N PHE B 259 3333 4473 7693 -582 -550 109 B N
ATOM 5390 CA PHE B 259 -13.814 4.211 460.867 1.00 40.54 B C
ANISOU 5390 CA PHE B 259 3163 4527 7715 -386 -448 62 B C
ATOM 5391 C PHE B 259 -14.344 5.564 460.377 1.00 52.77 B C
ANISOU 5391 C PHE B 259 4550 6128 9371 -150 -624 2 B C
ATOM 5392 O PHE B 259 -14.514 6.491 461.185 1.00 44.92 B O
ANISOU 5392 O PHE B 259 3414 5214 8441 30 -555 -61 B O
ATOM 5393 CB PHE B 259 -12.377 4.306 461.384 1.00 38.10 B C
ANISOU 5393 CB PHE B 259 3122 4048 7306 -310 -333 119 B C
ATOM 5394 CG PHE B 259 -12.260 4.715 462.822 1.00 49.79 B C
ANISOU 5394 CG PHE B 259 4522 5612 8782 -229 -157 86 B C
ATOM 5395 CD1 PHE B 259 -13.385 4.931 463.592 1.00 39.99 B C
ANISOU 5395 CD1 PHE B 259 2997 4585 7614 -232 -71 4 B C
ATOM 5396 CD2 PHE B 259 -11.000 4.831 463.423 1.00 52.21 B C
ANISOU 5396 CD2 PHE B 259 5043 5788 9007 -162 -73 130 B C
ATOM 5397 CE1 PHE B 259 -13.269 5.306 464.922 1.00 40.11 B C
ANISOU 5397 CE1 PHE B 259 2975 4671 7596 -166 107 -36 B C
ATOM 5398 CE2 PHE B 259 -10.869 5.199 464.757 1.00 44.38 B C
ANISOU 5398 CE2 PHE B 259 4012 4866 7984 -99 70 97 B C
ATOM 5399 CZ PHE B 259 -12.010 5.445 465.510 1.00 46.69 B C
ANISOU 5399 CZ PHE B 259 4055 5363 8324 -102 167 13 B C
ATOM 5400 N GLY B 260 -14.657 5.681 459.082 1.00 42.19 B N
ANISOU 5400 N GLY B 260 3244 4740 8045 -147 -856 15 B N
ATOM 5401 CA GLY B 260 -15.069 6.944 458.514 1.00 43.19 B C
ANISOU 5401 CA GLY B 260 3280 4873 8256 87 -1058 -22 B C
ATOM 5402 C GLY B 260 -13.932 7.885 458.221 1.00 41.28 B C
ANISOU 5402 C GLY B 260 3317 4423 7943 265 -1088 23 B C
ATOM 5403 O GLY B 260 -14.165 9.077 458.006 1.00 42.05 B O
ANISOU 5403 O GLY B 260 3370 4501 8107 487 -1219 -6 B O
ATOM 5404 N VAL B 261 -12.709 7.376 458.199 1.00 39.06 B N
ANISOU 5404 N VAL B 261 3320 3982 7539 173 -971 90 B N
ATOM 5405 CA VAL B 261 -11.503 8.167 458.042 1.00 37.29 B C
ANISOU 5405 CA VAL B 261 3346 3570 7254 301 -953 128 B C
ATOM 5406 C VAL B 261 -10.985 8.047 456.619 1.00 46.51 B C
ANISOU 5406 C VAL B 261 4787 4564 8320 242 -1086 192 B C
ATOM 5407 O VAL B 261 -10.892 6.946 456.071 1.00 49.29 B O
ANISOU 5407 O VAL B 261 5247 4883 8598 55 -1077 224 B O
ATOM 5408 CB VAL B 261 -10.444 7.733 459.054 1.00 35.40 B C
ANISOU 5408 CB VAL B 261 3204 3283 6963 251 -727 148 B C
ATOM 5409 CG1 VAL B 261 -9.252 8.608 458.913 1.00 33.95 B C
ANISOU 5409 CG1 VAL B 261 3230 2928 6743 371 -716 173 B C
ATOM 5410 CG2 VAL B 261 -11.023 7.818 460.445 1.00 36.05 B C
ANISOU 5410 CG2 VAL B 261 3052 3538 7109 288 -594 84 B C
ATOM 5411 N SER B 262 -10.661 9.183 456.011 1.00 44.57 B N
ANISOU 5411 N SER B 262 4681 4197 8059 395 -1203 209 B N
ATOM 5412 CA SER B 262 -10.158 9.205 454.650 1.00 37.05 B C
ANISOU 5412 CA SER B 262 4021 3072 6984 341 -1315 270 B C
ATOM 5413 C SER B 262 -8.658 9.438 454.576 1.00 48.77 B C
ANISOU 5413 C SER B 262 5769 4373 8389 336 -1164 310 B C
ATOM 5414 O SER B 262 -8.030 9.053 453.582 1.00 35.95 B O
ANISOU 5414 O SER B 262 4399 2614 6647 229 -1160 354 B O
ATOM 5415 CB SER B 262 -10.888 10.290 453.852 1.00 38.97 B C
ANISOU 5415 CB SER B 262 4276 3286 7243 494 -1576 274 B C
ATOM 5416 OG SER B 262 -12.192 9.858 453.498 1.00 46.00 B O
ANISOU 5416 OG SER B 262 4964 4328 8188 453 -1761 247 B O
ATOM 5417 N ALA B 263 -8.068 10.035 455.609 1.00 48.40 B N
ANISOU 5417 N ALA B 263 5663 4324 8404 438 -1034 287 B N
ATOM 5418 CA ALA B 263 -6.628 10.205 455.662 1.00 32.55 B C
ANISOU 5418 CA ALA B 263 3849 2168 6349 418 -887 315 B C
ATOM 5419 C ALA B 263 -6.207 10.268 457.121 1.00 31.48 B C
ANISOU 5419 C ALA B 263 3568 2105 6288 469 -736 277 B C
ATOM 5420 O ALA B 263 -6.916 10.826 457.949 1.00 32.08 B O
ANISOU 5420 O ALA B 263 3461 2290 6437 581 -762 225 B O
ATOM 5421 CB ALA B 263 -6.214 11.459 454.894 1.00 33.03 B C
ANISOU 5421 CB ALA B 263 4113 2069 6369 508 -976 341 B C
ATOM 5422 N SER B 264 -5.019 9.761 457.429 1.00 35.35 B N
ANISOU 5422 N SER B 264 4148 2527 6757 397 -585 296 B N
ATOM 5423 CA SER B 264 -4.562 9.776 458.811 1.00 39.72 B C
ANISOU 5423 CA SER B 264 4590 3141 7360 437 -470 267 B C
ATOM 5424 C SER B 264 -3.073 10.075 458.908 1.00 43.77 B C
ANISOU 5424 C SER B 264 5231 3569 7832 423 -372 274 B C
ATOM 5425 O SER B 264 -2.319 9.945 457.947 1.00 54.53 B O
ANISOU 5425 O SER B 264 6753 4882 9085 349 -332 296 B O
ATOM 5426 CB SER B 264 -4.862 8.446 459.511 1.00 29.18 B C
ANISOU 5426 CB SER B 264 3153 1916 6018 335 -386 274 B C
ATOM 5427 OG SER B 264 -4.276 7.370 458.821 1.00 46.18 B O
ANISOU 5427 OG SER B 264 5440 3981 8125 213 -336 319 B O
ATOM 5428 N THR B 265 -2.671 10.529 460.083 1.00 27.99 B N
ANISOU 5428 N THR B 265 3158 1633 5843 478 -321 237 B N
ATOM 5429 CA THR B 265 -1.269 10.618 460.443 1.00 46.95 B C
ANISOU 5429 CA THR B 265 5624 4051 8164 436 -232 230 B C
ATOM 5430 C THR B 265 -1.151 10.279 461.916 1.00 48.47 B C
ANISOU 5430 C THR B 265 5707 4302 8410 463 -194 213 B C
ATOM 5431 O THR B 265 -2.011 10.663 462.709 1.00 41.84 B O
ANISOU 5431 O THR B 265 4767 3491 7639 545 -223 179 B O
ATOM 5432 CB THR B 265 -0.673 12.004 460.161 1.00 41.63 B C
ANISOU 5432 CB THR B 265 5047 3344 7427 468 -251 202 B C
ATOM 5433 CG2 THR B 265 0.827 11.991 460.389 1.00 41.35 B C
ANISOU 5433 CG2 THR B 265 5045 3309 7357 408 -168 196 B C
ATOM 5434 OG1 THR B 265 -0.924 12.363 458.800 1.00 49.85 B O
ANISOU 5434 OG1 THR B 265 6222 4306 8411 451 -296 228 B O
ATOM 5435 N SER B 266 -0.102 9.551 462.290 1.00 49.51 B N
ANISOU 5435 N SER B 266 5856 4444 8513 409 -131 233 B N
ATOM 5436 CA SER B 266 0.116 9.331 463.703 1.00 26.54 B C
ANISOU 5436 CA SER B 266 2880 1563 5641 440 -120 226 B C
ATOM 5437 C SER B 266 1.581 9.508 464.038 1.00 26.34 B C
ANISOU 5437 C SER B 266 2881 1537 5590 424 -110 217 B C
ATOM 5438 O SER B 266 2.466 9.247 463.221 1.00 26.16 B O
ANISOU 5438 O SER B 266 2899 1498 5544 376 -74 229 B O
ATOM 5439 CB SER B 266 -0.405 7.966 464.149 1.00 26.67 B C
ANISOU 5439 CB SER B 266 2863 1567 5703 405 -86 280 B C
ATOM 5440 OG SER B 266 -0.072 6.987 463.217 1.00 38.17 B O
ANISOU 5440 OG SER B 266 4389 2997 7117 327 -53 319 B O
ATOM 5441 N ILE B 267 1.808 10.006 465.247 1.00 26.64 B N
ANISOU 5441 N ILE B 267 2886 1582 5654 473 -143 186 B N
ATOM 5442 CA ILE B 267 3.126 10.226 465.812 1.00 35.49 B C
ANISOU 5442 CA ILE B 267 4000 2687 6796 468 -170 172 B C
ATOM 5443 C ILE B 267 3.198 9.401 467.086 1.00 38.09 B C
ANISOU 5443 C ILE B 267 4310 3012 7150 497 -200 204 B C
ATOM 5444 O ILE B 267 2.256 9.420 467.892 1.00 32.49 B O
ANISOU 5444 O ILE B 267 3596 2302 6445 542 -203 198 B O
ATOM 5445 CB ILE B 267 3.361 11.726 466.102 1.00 27.70 B C
ANISOU 5445 CB ILE B 267 3031 1675 5821 496 -214 103 B C
ATOM 5446 CG1 ILE B 267 3.169 12.543 464.833 1.00 27.11 B C
ANISOU 5446 CG1 ILE B 267 3015 1576 5708 472 -192 91 B C
ATOM 5447 CG2 ILE B 267 4.751 11.981 466.671 1.00 27.67 B C
ANISOU 5447 CG2 ILE B 267 2996 1632 5884 475 -261 83 B C
ATOM 5448 CD1 ILE B 267 2.659 13.933 465.090 1.00 38.92 B C
ANISOU 5448 CD1 ILE B 267 4559 3039 7189 530 -236 30 B C
ATOM 5449 N GLY B 268 4.316 8.698 467.278 1.00 27.41 B N
ANISOU 5449 N GLY B 268 2945 1643 5825 484 -223 237 B N
ATOM 5450 CA GLY B 268 4.480 7.919 468.487 1.00 28.06 B C
ANISOU 5450 CA GLY B 268 3045 1698 5920 520 -285 285 B C
ATOM 5451 C GLY B 268 4.927 8.778 469.654 1.00 39.62 B C
ANISOU 5451 C GLY B 268 4507 3157 7388 559 -387 237 B C
ATOM 5452 O GLY B 268 5.767 9.668 469.514 1.00 44.81 B O
ANISOU 5452 O GLY B 268 5120 3777 8130 561 -436 183 B O
ATOM 5453 N ILE B 269 4.375 8.481 470.828 1.00 29.50 B N
ANISOU 5453 N ILE B 269 3297 1953 5960 559 -410 250 B N
ATOM 5454 CA ILE B 269 4.737 9.166 472.066 1.00 30.53 B C
ANISOU 5454 CA ILE B 269 3474 2122 6004 573 -509 197 B C
ATOM 5455 C ILE B 269 5.633 8.228 472.861 1.00 31.53 B C
ANISOU 5455 C ILE B 269 3644 2234 6103 582 -630 271 B C
ATOM 5456 O ILE B 269 5.203 7.156 473.298 1.00 45.34 B O
ANISOU 5456 O ILE B 269 5481 4000 7748 568 -610 352 B O
ATOM 5457 CB ILE B 269 3.507 9.583 472.877 1.00 31.04 B C
ANISOU 5457 CB ILE B 269 3612 2280 5900 568 -440 146 B C
ATOM 5458 CG1 ILE B 269 2.559 10.412 472.035 1.00 30.33 B C
ANISOU 5458 CG1 ILE B 269 3463 2200 5861 591 -340 79 B C
ATOM 5459 CG2 ILE B 269 3.913 10.389 474.072 1.00 39.63 B C
ANISOU 5459 CG2 ILE B 269 4779 3392 6886 578 -534 73 B C
ATOM 5460 CD1 ILE B 269 1.246 10.654 472.738 1.00 31.09 B C
ANISOU 5460 CD1 ILE B 269 3585 2403 5823 602 -244 24 B C
ATOM 5461 N PHE B 270 6.888 8.616 473.023 1.00 32.16 B N
ANISOU 5461 N PHE B 270 3661 2275 6283 602 -763 246 B N
ATOM 5462 CA PHE B 270 7.909 7.769 473.613 1.00 38.44 B C
ANISOU 5462 CA PHE B 270 4457 3045 7104 638 -915 313 B C
ATOM 5463 C PHE B 270 8.323 8.262 474.989 1.00 34.95 B C
ANISOU 5463 C PHE B 270 4099 2647 6534 633 -1089 279 B C
ATOM 5464 O PHE B 270 8.594 9.448 475.174 1.00 35.21 B O
ANISOU 5464 O PHE B 270 4103 2693 6582 605 -1135 179 B O
ATOM 5465 CB PHE B 270 9.131 7.686 472.706 1.00 33.36 B C
ANISOU 5465 CB PHE B 270 3639 2333 6704 668 -947 308 B C
ATOM 5466 CG PHE B 270 8.944 6.782 471.546 1.00 36.58 B C
ANISOU 5466 CG PHE B 270 4010 2680 7208 686 -809 363 B C
ATOM 5467 CD1 PHE B 270 9.140 5.415 471.688 1.00 33.07 B C
ANISOU 5467 CD1 PHE B 270 3614 2188 6765 742 -842 458 B C
ATOM 5468 CD2 PHE B 270 8.587 7.284 470.309 1.00 31.15 B C
ANISOU 5468 CD2 PHE B 270 3275 1996 6565 634 -648 315 B C
ATOM 5469 CE1 PHE B 270 8.975 4.564 470.612 1.00 32.41 B C
ANISOU 5469 CE1 PHE B 270 3535 2111 6670 718 -688 477 B C
ATOM 5470 CE2 PHE B 270 8.420 6.425 469.226 1.00 36.13 B C
ANISOU 5470 CE2 PHE B 270 3914 2647 7168 606 -509 343 B C
ATOM 5471 CZ PHE B 270 8.627 5.067 469.379 1.00 31.13 B C
ANISOU 5471 CZ PHE B 270 3326 1988 6513 648 -526 416 B C
ATOM 5472 N ASN B 271 8.338 7.356 475.954 1.00 36.62 B N
ANISOU 5472 N ASN B 271 4446 2867 6600 651 -1189 364 B N
ATOM 5473 CA ASN B 271 8.993 7.588 477.230 1.00 42.72 B C
ANISOU 5473 CA ASN B 271 5312 3664 7255 655 -1407 354 B C
ATOM 5474 C ASN B 271 10.318 6.838 477.149 1.00 52.03 B C
ANISOU 5474 C ASN B 271 6379 4784 8605 733 -1600 422 B C
ATOM 5475 O ASN B 271 10.356 5.616 477.308 1.00 53.25 B O
ANISOU 5475 O ASN B 271 6615 4891 8729 788 -1642 538 B O
ATOM 5476 CB ASN B 271 8.116 7.112 478.383 1.00 54.05 B C
ANISOU 5476 CB ASN B 271 7003 5143 8390 619 -1392 407 B C
ATOM 5477 CG ASN B 271 8.697 7.453 479.735 1.00 60.34 B C
ANISOU 5477 CG ASN B 271 7946 5965 9014 608 -1618 387 B C
ATOM 5478 ND2 ASN B 271 7.881 7.314 480.780 1.00 51.81 B N
ANISOU 5478 ND2 ASN B 271 7116 4932 7638 553 -1573 403 B N
ATOM 5479 OD1 ASN B 271 9.871 7.835 479.846 1.00 64.77 B O
ANISOU 5479 OD1 ASN B 271 8399 6508 9703 637 -1831 354 B O
ATOM 5480 N GLU B 272 11.398 7.568 476.869 1.00 58.40 B N
ANISOU 5480 N GLU B 272 6992 5588 9607 739 -1711 344 B N
ATOM 5481 CA GLU B 272 12.706 6.984 476.550 1.00 41.39 B C
ANISOU 5481 CA GLU B 272 4643 3392 7691 823 -1860 379 B C
ATOM 5482 C GLU B 272 12.516 6.072 475.346 1.00 47.90 B C
ANISOU 5482 C GLU B 272 5389 4149 8662 878 -1670 437 B C
ATOM 5483 O GLU B 272 12.140 6.574 474.270 1.00 64.16 B O
ANISOU 5483 O GLU B 272 7365 6201 10811 826 -1462 380 B O
ATOM 5484 CB GLU B 272 13.266 6.342 477.808 1.00 45.40 B C
ANISOU 5484 CB GLU B 272 5267 3900 8084 887 -2145 455 B C
ATOM 5485 CG GLU B 272 13.353 7.318 478.955 1.00 68.76 B C
ANISOU 5485 CG GLU B 272 8341 6924 10862 809 -2317 381 B C
ATOM 5486 CD GLU B 272 14.191 8.546 478.615 1.00 87.31 B C
ANISOU 5486 CD GLU B 272 10465 9304 13407 744 -2375 245 B C
ATOM 5487 OE1 GLU B 272 15.330 8.369 478.116 1.00 90.12 B O
ANISOU 5487 OE1 GLU B 272 10557 9648 14038 793 -2475 236 B O
ATOM 5488 OE2 GLU B 272 13.686 9.681 478.806 1.00 85.48 B O1-
ANISOU 5488 OE2 GLU B 272 10317 9099 13061 642 -2302 142 B O1-
ATOM 5489 N ASP B 273 12.730 4.768 475.461 1.00 53.71 B N
ANISOU 5489 N ASP B 273 6177 4820 9412 978 -1734 546 B N
ATOM 5490 CA ASP B 273 12.587 3.860 474.330 1.00 53.61 B C
ANISOU 5490 CA ASP B 273 6114 4723 9530 1029 -1558 590 B C
ATOM 5491 C ASP B 273 11.222 3.186 474.265 1.00 46.25 B C
ANISOU 5491 C ASP B 273 5412 3765 8396 977 -1394 664 B C
ATOM 5492 O ASP B 273 10.981 2.393 473.348 1.00 37.60 B O
ANISOU 5492 O ASP B 273 4322 2640 7324 974 -1224 683 B O
ATOM 5493 CB ASP B 273 13.696 2.799 474.382 1.00 70.00 B C
ANISOU 5493 CB ASP B 273 8120 6788 11688 1137 -1664 628 B C
ATOM 5494 CG ASP B 273 15.093 3.407 474.340 1.00 83.41 B C
ANISOU 5494 CG ASP B 273 9543 8540 13608 1168 -1798 540 B C
ATOM 5495 OD1 ASP B 273 15.288 4.445 473.655 1.00 69.89 B O1-
ANISOU 5495 OD1 ASP B 273 7658 6862 12034 1088 -1694 439 B O1-
ATOM 5496 OD2 ASP B 273 15.988 2.848 475.013 1.00 95.67 B O1-
ANISOU 5496 OD2 ASP B 273 11058 10094 15198 1268 -2014 574 B O1-
ATOM 5497 N GLU B 274 10.336 3.474 475.217 1.00 44.03 B N
ANISOU 5497 N GLU B 274 5323 3547 7858 898 -1406 679 B N
ATOM 5498 CA GLU B 274 9.017 2.856 475.289 1.00 42.83 B C
ANISOU 5498 CA GLU B 274 5369 3391 7512 824 -1248 743 B C
ATOM 5499 C GLU B 274 7.954 3.661 474.547 1.00 50.81 B C
ANISOU 5499 C GLU B 274 6327 4472 8507 729 -1026 659 B C
ATOM 5500 O GLU B 274 7.854 4.883 474.709 1.00 43.15 B O
ANISOU 5500 O GLU B 274 5299 3578 7520 696 -1022 561 B O
ATOM 5501 CB GLU B 274 8.614 2.680 476.750 1.00 42.38 B C
ANISOU 5501 CB GLU B 274 5554 3372 7178 783 -1356 802 B C
ATOM 5502 CG GLU B 274 9.521 1.736 477.495 1.00 63.09 B C
ANISOU 5502 CG GLU B 274 8283 5905 9783 882 -1596 913 B C
ATOM 5503 CD GLU B 274 8.978 1.377 478.856 1.00 89.03 B C
ANISOU 5503 CD GLU B 274 11876 9204 12747 819 -1673 997 B C
ATOM 5504 OE1 GLU B 274 7.749 1.514 479.056 1.00 88.29 B O
ANISOU 5504 OE1 GLU B 274 11910 9176 12462 692 -1474 985 B O
ATOM 5505 OE2 GLU B 274 9.778 0.937 479.713 1.00100.50 B O1-
ANISOU 5505 OE2 GLU B 274 13443 10603 14140 897 -1930 1074 B O1-
ATOM 5506 N LEU B 275 7.147 2.967 473.753 1.00 34.70 B N
ANISOU 5506 N LEU B 275 4319 2396 6470 689 -859 697 B N
ATOM 5507 CA LEU B 275 5.999 3.597 473.117 1.00 37.18 B C
ANISOU 5507 CA LEU B 275 4596 2779 6751 606 -677 632 B C
ATOM 5508 C LEU B 275 4.895 3.707 474.168 1.00 43.35 B C
ANISOU 5508 C LEU B 275 5521 3656 7295 526 -627 637 B C
ATOM 5509 O LEU B 275 4.310 2.700 474.596 1.00 34.60 B O
ANISOU 5509 O LEU B 275 4561 2532 6054 468 -584 725 B O
ATOM 5510 CB LEU B 275 5.560 2.810 471.884 1.00 32.26 B C
ANISOU 5510 CB LEU B 275 3953 2088 6215 580 -540 663 B C
ATOM 5511 CG LEU B 275 4.460 3.398 471.003 1.00 30.89 B C
ANISOU 5511 CG LEU B 275 3719 1975 6044 508 -386 600 B C
ATOM 5512 CD1 LEU B 275 4.910 4.733 470.397 1.00 34.24 B C
ANISOU 5512 CD1 LEU B 275 4004 2417 6587 542 -392 502 B C
ATOM 5513 CD2 LEU B 275 4.054 2.443 469.894 1.00 30.40 B C
ANISOU 5513 CD2 LEU B 275 3679 1837 6035 466 -285 640 B C
ATOM 5514 N TRP B 276 4.652 4.939 474.615 1.00 33.73 B N
ANISOU 5514 N TRP B 276 4269 2527 6019 518 -625 539 B N
ATOM 5515 CA TRP B 276 3.695 5.189 475.679 1.00 34.65 B C
ANISOU 5515 CA TRP B 276 4512 2743 5911 455 -561 516 B C
ATOM 5516 C TRP B 276 2.291 5.286 475.119 1.00 48.02 B C
ANISOU 5516 C TRP B 276 6146 4509 7588 392 -357 477 B C
ATOM 5517 O TRP B 276 1.326 4.849 475.762 1.00 34.83 B O
ANISOU 5517 O TRP B 276 4572 2910 5752 309 -246 500 B O
ATOM 5518 CB TRP B 276 4.086 6.475 476.400 1.00 35.20 B C
ANISOU 5518 CB TRP B 276 4582 2860 5932 486 -648 409 B C
ATOM 5519 CG TRP B 276 3.220 6.872 477.545 1.00 36.45 B C
ANISOU 5519 CG TRP B 276 4881 3117 5852 435 -574 358 B C
ATOM 5520 CD1 TRP B 276 3.393 6.544 478.847 1.00 43.16 B C
ANISOU 5520 CD1 TRP B 276 5936 3984 6480 402 -655 397 B C
ATOM 5521 CD2 TRP B 276 2.062 7.721 477.497 1.00 36.23 B C
ANISOU 5521 CD2 TRP B 276 4804 3181 5781 421 -399 246 B C
ATOM 5522 CE2 TRP B 276 1.583 7.846 478.809 1.00 38.05 B C
ANISOU 5522 CE2 TRP B 276 5207 3487 5762 374 -352 213 B C
ATOM 5523 CE3 TRP B 276 1.387 8.383 476.468 1.00 44.41 B C
ANISOU 5523 CE3 TRP B 276 5673 4237 6964 452 -284 171 B C
ATOM 5524 NE1 TRP B 276 2.406 7.111 479.617 1.00 39.29 B N
ANISOU 5524 NE1 TRP B 276 5536 3595 5796 352 -512 312 B N
ATOM 5525 CZ2 TRP B 276 0.465 8.608 479.123 1.00 44.32 B C
ANISOU 5525 CZ2 TRP B 276 5986 4384 6471 368 -172 93 B C
ATOM 5526 CZ3 TRP B 276 0.272 9.135 476.782 1.00 35.52 B C
ANISOU 5526 CZ3 TRP B 276 4527 3207 5761 458 -138 63 B C
ATOM 5527 CH2 TRP B 276 -0.179 9.238 478.095 1.00 37.35 B C
ANISOU 5527 CH2 TRP B 276 4907 3520 5765 421 -72 18 B C
ATOM 5528 N GLY B 277 2.198 5.834 473.914 1.00 48.83 B N
ANISOU 5528 N GLY B 277 6093 4596 7864 423 -311 423 B N
ATOM 5529 CA GLY B 277 0.948 6.046 473.223 1.00 31.81 B C
ANISOU 5529 CA GLY B 277 3850 2507 5730 385 -164 379 B C
ATOM 5530 C GLY B 277 1.262 6.627 471.864 1.00 30.42 B C
ANISOU 5530 C GLY B 277 3548 2268 5741 435 -178 341 B C
ATOM 5531 O GLY B 277 2.409 6.607 471.400 1.00 38.59 B O
ANISOU 5531 O GLY B 277 4565 3209 6889 474 -263 360 B O
ATOM 5532 N ILE B 278 0.233 7.152 471.218 1.00 34.19 B N
ANISOU 5532 N ILE B 278 3939 2801 6251 432 -94 284 B N
ATOM 5533 CA ILE B 278 0.389 7.788 469.921 1.00 41.66 B C
ANISOU 5533 CA ILE B 278 4806 3683 7340 471 -109 252 B C
ATOM 5534 C ILE B 278 -0.538 8.990 469.873 1.00 29.20 B C
ANISOU 5534 C ILE B 278 3162 2171 5762 525 -77 154 B C
ATOM 5535 O ILE B 278 -1.519 9.085 470.614 1.00 48.98 B O
ANISOU 5535 O ILE B 278 5644 4787 8180 523 -7 111 B O
ATOM 5536 CB ILE B 278 0.121 6.834 468.723 1.00 44.04 B C
ANISOU 5536 CB ILE B 278 5093 3936 7704 414 -70 316 B C
ATOM 5537 CG1 ILE B 278 -1.348 6.489 468.592 1.00 36.08 B C
ANISOU 5537 CG1 ILE B 278 4034 3030 6647 353 10 309 B C
ATOM 5538 CG2 ILE B 278 0.935 5.530 468.827 1.00 46.44 B C
ANISOU 5538 CG2 ILE B 278 5479 4160 8008 378 -89 408 B C
ATOM 5539 CD1 ILE B 278 -1.576 5.408 467.591 1.00 52.70 B C
ANISOU 5539 CD1 ILE B 278 6157 5081 8785 269 32 372 B C
ATOM 5540 N VAL B 279 -0.194 9.926 469.007 1.00 32.15 B N
ANISOU 5540 N VAL B 279 3513 2466 6236 578 -122 115 B N
ATOM 5541 CA VAL B 279 -1.096 10.997 468.613 1.00 34.86 B C
ANISOU 5541 CA VAL B 279 3804 2831 6609 650 -113 38 B C
ATOM 5542 C VAL B 279 -1.752 10.555 467.310 1.00 28.49 B C
ANISOU 5542 C VAL B 279 2949 2014 5862 622 -105 81 B C
ATOM 5543 O VAL B 279 -1.091 10.455 466.280 1.00 27.76 B O
ANISOU 5543 O VAL B 279 2902 1815 5830 597 -137 124 B O
ATOM 5544 CB VAL B 279 -0.344 12.331 468.465 1.00 28.88 B C
ANISOU 5544 CB VAL B 279 3099 1969 5907 713 -181 -23 B C
ATOM 5545 CG1 VAL B 279 -1.258 13.457 467.987 1.00 29.43 B C
ANISOU 5545 CG1 VAL B 279 3145 2024 6013 810 -191 -94 B C
ATOM 5546 CG2 VAL B 279 0.321 12.699 469.786 1.00 29.53 B C
ANISOU 5546 CG2 VAL B 279 3238 2065 5918 720 -210 -71 B C
ATOM 5547 N ALA B 280 -3.048 10.283 467.329 1.00 29.18 B N
ANISOU 5547 N ALA B 280 2944 2214 5930 617 -60 63 B N
ATOM 5548 CA ALA B 280 -3.759 9.845 466.130 1.00 29.11 B C
ANISOU 5548 CA ALA B 280 2884 2206 5968 578 -81 98 B C
ATOM 5549 C ALA B 280 -4.485 11.017 465.496 1.00 29.72 B C
ANISOU 5549 C ALA B 280 2905 2277 6108 692 -149 36 B C
ATOM 5550 O ALA B 280 -5.185 11.751 466.183 1.00 30.75 B O
ANISOU 5550 O ALA B 280 2953 2487 6243 787 -129 -47 B O
ATOM 5551 CB ALA B 280 -4.769 8.756 466.464 1.00 29.86 B C
ANISOU 5551 CB ALA B 280 2891 2432 6021 480 -8 118 B C
ATOM 5552 N CYS B 281 -4.330 11.183 464.188 1.00 37.42 B N
ANISOU 5552 N CYS B 281 3942 3150 7125 689 -228 73 B N
ATOM 5553 CA CYS B 281 -4.967 12.272 463.458 1.00 30.13 B C
ANISOU 5553 CA CYS B 281 3007 2188 6253 803 -328 35 B C
ATOM 5554 C CYS B 281 -5.781 11.721 462.300 1.00 33.41 B C
ANISOU 5554 C CYS B 281 3387 2626 6681 754 -403 76 B C
ATOM 5555 O CYS B 281 -5.221 11.122 461.384 1.00 40.46 B O
ANISOU 5555 O CYS B 281 4399 3430 7545 655 -417 143 B O
ATOM 5556 CB CYS B 281 -3.932 13.284 462.955 1.00 31.62 B C
ANISOU 5556 CB CYS B 281 3373 2239 6402 824 -370 41 B C
ATOM 5557 SG CYS B 281 -2.811 13.865 464.204 1.00 29.30 B S
ANISOU 5557 SG CYS B 281 3142 1943 6049 823 -306 -6 B S
ATOM 5558 N HIS B 282 -7.091 11.959 462.329 1.00 37.70 B N
ANISOU 5558 N HIS B 282 3763 3289 7272 827 -454 26 B N
ATOM 5559 CA HIS B 282 -8.030 11.584 461.278 1.00 35.94 B C
ANISOU 5559 CA HIS B 282 3474 3107 7074 795 -569 50 B C
ATOM 5560 C HIS B 282 -8.563 12.807 460.564 1.00 34.23 B C
ANISOU 5560 C HIS B 282 3266 2826 6912 963 -735 24 B C
ATOM 5561 O HIS B 282 -8.833 13.838 461.188 1.00 43.72 B O
ANISOU 5561 O HIS B 282 4407 4036 8169 1130 -739 -49 B O
ATOM 5562 CB HIS B 282 -9.235 10.841 461.841 1.00 35.77 B C
ANISOU 5562 CB HIS B 282 3208 3294 7090 739 -519 9 B C
ATOM 5563 CG HIS B 282 -8.879 9.583 462.542 1.00 43.53 B C
ANISOU 5563 CG HIS B 282 4201 4331 8007 566 -368 44 B C
ATOM 5564 CD2 HIS B 282 -7.771 8.813 462.464 1.00 31.89 B C
ANISOU 5564 CD2 HIS B 282 2909 2747 6462 454 -310 116 B C
ATOM 5565 ND1 HIS B 282 -9.738 8.950 463.411 1.00 48.73 B N
ANISOU 5565 ND1 HIS B 282 4675 5166 8673 490 -259 7 B N
ATOM 5566 CE1 HIS B 282 -9.158 7.857 463.866 1.00 54.76 B C
ANISOU 5566 CE1 HIS B 282 5540 5910 9356 336 -151 66 B C
ATOM 5567 NE2 HIS B 282 -7.965 7.750 463.304 1.00 55.71 B N
ANISOU 5567 NE2 HIS B 282 5873 5857 9437 326 -188 130 B N
ATOM 5568 N HIS B 283 -8.775 12.649 459.258 1.00 34.65 B N
ANISOU 5568 N HIS B 283 3412 2813 6943 922 -879 81 B N
ATOM 5569 CA HIS B 283 -9.391 13.664 458.418 1.00 41.93 B C
ANISOU 5569 CA HIS B 283 4365 3665 7901 1074 -1082 78 B C
ATOM 5570 C HIS B 283 -10.489 13.024 457.579 1.00 40.15 B C
ANISOU 5570 C HIS B 283 4021 3541 7693 1020 -1237 94 B C
ATOM 5571 O HIS B 283 -10.340 11.888 457.124 1.00 51.10 B O
ANISOU 5571 O HIS B 283 5457 4947 9012 828 -1208 140 B O
ATOM 5572 CB HIS B 283 -8.328 14.337 457.532 1.00 35.59 B C
ANISOU 5572 CB HIS B 283 3884 2624 7013 1071 -1132 146 B C
ATOM 5573 CG HIS B 283 -8.742 15.686 457.027 1.00 69.53 B C
ANISOU 5573 CG HIS B 283 8279 6844 11295 1237 -1290 138 B C
ATOM 5574 CD2 HIS B 283 -8.703 16.222 455.784 1.00 49.00 B C
ANISOU 5574 CD2 HIS B 283 5911 4111 8596 1241 -1443 203 B C
ATOM 5575 ND1 HIS B 283 -9.290 16.653 457.845 1.00 53.49 B N
ANISOU 5575 ND1 HIS B 283 6132 4897 9294 1398 -1274 53 B N
ATOM 5576 CE1 HIS B 283 -9.572 17.722 457.125 1.00 40.02 B C
ANISOU 5576 CE1 HIS B 283 4575 3104 7527 1504 -1415 71 B C
ATOM 5577 NE2 HIS B 283 -9.224 17.487 455.873 1.00 39.96 B N
ANISOU 5577 NE2 HIS B 283 4781 2967 7437 1410 -1524 165 B N
ATOM 5578 N THR B 284 -11.584 13.754 457.352 1.00 48.18 B N
ANISOU 5578 N THR B 284 4885 4614 8806 1192 -1416 51 B N
ATOM 5579 CA THR B 284 -12.738 13.174 456.655 1.00 55.49 B C
ANISOU 5579 CA THR B 284 5639 5669 9775 1145 -1591 50 B C
ATOM 5580 C THR B 284 -12.659 13.314 455.152 1.00 51.15 B C
ANISOU 5580 C THR B 284 5341 4967 9126 1118 -1825 135 B C
ATOM 5581 O THR B 284 -13.646 13.023 454.476 1.00 46.51 B O
ANISOU 5581 O THR B 284 4631 4469 8570 1104 -2030 134 B O
ATOM 5582 CB THR B 284 -14.066 13.787 457.113 1.00 44.39 B C
ANISOU 5582 CB THR B 284 3890 4429 8547 1347 -1690 -48 B C
ATOM 5583 CG2 THR B 284 -14.372 13.406 458.546 1.00 44.23 B C
ANISOU 5583 CG2 THR B 284 3596 4604 8607 1324 -1441 -141 B C
ATOM 5584 OG1 THR B 284 -14.007 15.211 456.988 1.00 61.15 B O
ANISOU 5584 OG1 THR B 284 6118 6406 10710 1605 -1811 -61 B O
ATOM 5585 N LYS B 285 -11.570 13.860 454.634 1.00 44.58 B N
ANISOU 5585 N LYS B 285 4850 3911 8176 1120 -1811 202 B N
ATOM 5586 CA LYS B 285 -11.263 13.869 453.213 1.00 41.87 B C
ANISOU 5586 CA LYS B 285 4821 3403 7685 1043 -1972 293 B C
ATOM 5587 C LYS B 285 -9.757 13.722 453.080 1.00 39.65 B C
ANISOU 5587 C LYS B 285 4838 2953 7275 910 -1766 344 B C
ATOM 5588 O LYS B 285 -9.039 13.832 454.076 1.00 38.04 B O
ANISOU 5588 O LYS B 285 4583 2752 7117 920 -1559 311 B O
ATOM 5589 CB LYS B 285 -11.800 15.147 452.562 1.00 44.15 B C
ANISOU 5589 CB LYS B 285 5209 3577 7990 1260 -2242 317 B C
ATOM 5590 CG LYS B 285 -11.512 16.380 453.393 1.00 66.56 B C
ANISOU 5590 CG LYS B 285 8042 6349 10898 1455 -2158 272 B C
ATOM 5591 CD LYS B 285 -12.447 17.553 453.086 1.00 58.36 B C
ANISOU 5591 CD LYS B 285 6982 5332 9858 1657 -2349 245 B C
ATOM 5592 CE LYS B 285 -12.153 18.723 454.031 1.00 69.14 B C
ANISOU 5592 CE LYS B 285 8361 6694 11214 1779 -2169 179 B C
ATOM 5593 NZ LYS B 285 -12.235 18.375 455.484 1.00 62.29 B N1+
ANISOU 5593 NZ LYS B 285 7205 5998 10464 1794 -1946 76 B N1+
ATOM 5594 N PRO B 286 -9.253 13.390 451.892 1.00 39.72 B N
ANISOU 5594 N PRO B 286 5145 2825 7121 771 -1808 416 B N
ATOM 5595 CA PRO B 286 -7.798 13.261 451.747 1.00 61.70 B C
ANISOU 5595 CA PRO B 286 8179 5459 9804 648 -1588 451 B C
ATOM 5596 C PRO B 286 -7.081 14.546 452.132 1.00 50.65 B C
ANISOU 5596 C PRO B 286 6889 3922 8434 769 -1531 455 B C
ATOM 5597 O PRO B 286 -7.617 15.651 452.010 1.00 59.39 B O
ANISOU 5597 O PRO B 286 8018 5015 9533 919 -1674 452 B O
ATOM 5598 CB PRO B 286 -7.605 12.916 450.263 1.00 38.91 B C
ANISOU 5598 CB PRO B 286 5614 2443 6728 510 -1675 517 B C
ATOM 5599 CG PRO B 286 -8.958 12.998 449.633 1.00 41.24 B C
ANISOU 5599 CG PRO B 286 5847 2806 7016 574 -1985 527 B C
ATOM 5600 CD PRO B 286 -9.956 12.828 450.731 1.00 49.56 B C
ANISOU 5600 CD PRO B 286 6480 4082 8269 679 -2017 451 B C
ATOM 5601 N ARG B 287 -5.850 14.383 452.606 1.00 50.09 B N
ANISOU 5601 N ARG B 287 6860 3861 8311 665 -1261 437 B N
ATOM 5602 CA ARG B 287 -5.090 15.498 453.159 1.00 36.93 B C
ANISOU 5602 CA ARG B 287 5240 2197 6596 713 -1126 409 B C
ATOM 5603 C ARG B 287 -3.618 15.124 453.191 1.00 40.48 B C
ANISOU 5603 C ARG B 287 5790 2632 6957 558 -869 409 B C
ATOM 5604 O ARG B 287 -3.235 14.159 453.859 1.00 46.04 B O
ANISOU 5604 O ARG B 287 6353 3423 7717 497 -745 381 B O
ATOM 5605 CB ARG B 287 -5.583 15.841 454.557 1.00 39.87 B C
ANISOU 5605 CB ARG B 287 5346 2696 7108 851 -1116 332 B C
ATOM 5606 CG ARG B 287 -4.767 16.926 455.241 1.00 34.87 B C
ANISOU 5606 CG ARG B 287 4775 2052 6423 880 -986 296 B C
ATOM 5607 CD ARG B 287 -5.569 17.678 456.287 1.00 51.62 B C
ANISOU 5607 CD ARG B 287 6722 4255 8638 1055 -1039 222 B C
ATOM 5608 NE ARG B 287 -4.857 18.883 456.689 1.00 64.19 B N
ANISOU 5608 NE ARG B 287 8445 5782 10164 1080 -960 199 B N
ATOM 5609 CZ ARG B 287 -4.866 20.030 456.011 1.00 61.72 B C
ANISOU 5609 CZ ARG B 287 8331 5339 9779 1131 -1031 231 B C
ATOM 5610 NH1 ARG B 287 -5.572 20.155 454.888 1.00 57.20 B N1+
ANISOU 5610 NH1 ARG B 287 7858 4698 9177 1176 -1202 289 B N1+
ATOM 5611 NH2 ARG B 287 -4.162 21.053 456.468 1.00 61.50 B N
ANISOU 5611 NH2 ARG B 287 8414 5240 9712 1132 -945 208 B N
ATOM 5612 N ALA B 288 -2.796 15.869 452.469 1.00 34.62 B N
ANISOU 5612 N ALA B 288 5285 1782 6088 498 -787 441 B N
ATOM 5613 CA ALA B 288 -1.357 15.695 452.538 1.00 40.09 B C
ANISOU 5613 CA ALA B 288 6047 2462 6723 372 -544 427 B C
ATOM 5614 C ALA B 288 -0.756 16.800 453.391 1.00 38.26 B C
ANISOU 5614 C ALA B 288 5791 2233 6513 418 -482 389 B C
ATOM 5615 O ALA B 288 -1.266 17.926 453.426 1.00 39.74 B O
ANISOU 5615 O ALA B 288 6031 2366 6703 517 -586 396 B O
ATOM 5616 CB ALA B 288 -0.719 15.705 451.147 1.00 40.89 B C
ANISOU 5616 CB ALA B 288 6417 2426 6694 242 -449 479 B C
ATOM 5617 N ILE B 289 0.354 16.474 454.056 1.00 39.16 B N
ANISOU 5617 N ILE B 289 5836 2403 6642 343 -332 348 B N
ATOM 5618 CA ILE B 289 1.095 17.425 454.877 1.00 42.66 B C
ANISOU 5618 CA ILE B 289 6262 2839 7107 350 -285 307 B C
ATOM 5619 C ILE B 289 2.553 17.340 454.463 1.00 40.36 B C
ANISOU 5619 C ILE B 289 6075 2490 6768 195 -138 304 B C
ATOM 5620 O ILE B 289 3.096 16.231 454.329 1.00 40.80 B O
ANISOU 5620 O ILE B 289 6055 2607 6839 122 -63 298 B O
ATOM 5621 CB ILE B 289 0.935 17.175 456.393 1.00 46.97 B C
ANISOU 5621 CB ILE B 289 6554 3528 7764 425 -310 247 B C
ATOM 5622 CG1 ILE B 289 1.221 15.707 456.756 1.00 37.79 B C
ANISOU 5622 CG1 ILE B 289 5226 2482 6651 371 -244 240 B C
ATOM 5623 CG2 ILE B 289 -0.450 17.680 456.899 1.00 31.85 B C
ANISOU 5623 CG2 ILE B 289 4555 1646 5902 586 -452 228 B C
ATOM 5624 CD1 ILE B 289 1.312 15.461 458.226 1.00 29.18 B C
ANISOU 5624 CD1 ILE B 289 3930 1504 5653 416 -240 193 B C
ATOM 5625 N GLY B 290 3.161 18.515 454.196 1.00 37.30 B N
ANISOU 5625 N GLY B 290 5865 1974 6333 142 -102 308 B N
ATOM 5626 CA GLY B 290 4.535 18.589 453.728 1.00 34.12 B C
ANISOU 5626 CA GLY B 290 5559 1502 5904 -29 -2 304 B C
ATOM 5627 C GLY B 290 5.545 18.192 454.792 1.00 33.23 B C
ANISOU 5627 C GLY B 290 5176 1506 5944 -64 62 247 B C
ATOM 5628 O GLY B 290 5.230 18.031 455.969 1.00 32.25 B O
ANISOU 5628 O GLY B 290 4854 1490 5909 35 16 211 B O
ATOM 5629 N ARG B 291 6.810 18.093 454.367 1.00 31.47 B N
ANISOU 5629 N ARG B 291 4689 1943 5325 192 -674 -1263 B N
ATOM 5630 CA ARG B 291 7.875 17.678 455.282 1.00 31.23 B C
ANISOU 5630 CA ARG B 291 4590 2021 5256 252 -519 -1306 B C
ATOM 5631 C ARG B 291 8.034 18.621 456.466 1.00 29.95 B C
ANISOU 5631 C ARG B 291 4404 1882 5094 415 -491 -1232 B C
ATOM 5632 O ARG B 291 8.310 18.168 457.587 1.00 29.18 B O
ANISOU 5632 O ARG B 291 4220 1869 4999 514 -431 -1209 B O
ATOM 5633 CB ARG B 291 9.207 17.624 454.532 1.00 30.80 B C
ANISOU 5633 CB ARG B 291 4610 2008 5086 74 -412 -1426 B C
ATOM 5634 CG ARG B 291 9.277 16.631 453.386 1.00 31.47 B C
ANISOU 5634 CG ARG B 291 4710 2116 5131 -124 -398 -1517 B C
ATOM 5635 CD ARG B 291 10.725 16.271 453.069 1.00 39.85 B C
ANISOU 5635 CD ARG B 291 5796 3260 6086 -229 -287 -1612 B C
ATOM 5636 NE ARG B 291 10.806 15.621 451.772 1.00 48.06 B N
ANISOU 5636 NE ARG B 291 6875 4331 7053 -448 -288 -1693 B N
ATOM 5637 CZ ARG B 291 10.439 14.367 451.543 1.00 45.24 B C
ANISOU 5637 CZ ARG B 291 6429 4007 6753 -480 -281 -1723 B C
ATOM 5638 NH1 ARG B 291 9.948 13.638 452.540 1.00 35.62 B N1+
ANISOU 5638 NH1 ARG B 291 5093 2776 5666 -307 -282 -1673 B N1+
ATOM 5639 NH2 ARG B 291 10.530 13.860 450.312 1.00 33.80 B N
ANISOU 5639 NH2 ARG B 291 5007 2607 5227 -690 -282 -1795 B N
ATOM 5640 N ARG B 292 7.807 19.920 456.258 1.00 30.51 B N
ANISOU 5640 N ARG B 292 4554 1874 5164 434 -543 -1189 B N
ATOM 5641 CA ARG B 292 8.017 20.891 457.330 1.00 30.14 B C
ANISOU 5641 CA ARG B 292 4485 1857 5110 560 -492 -1138 B C
ATOM 5642 C ARG B 292 6.924 20.789 458.378 1.00 29.83 B C
ANISOU 5642 C ARG B 292 4337 1858 5139 723 -534 -1034 B C
ATOM 5643 O ARG B 292 7.192 20.934 459.577 1.00 53.38 B O
ANISOU 5643 O ARG B 292 7259 4926 8097 804 -457 -1017 B O
ATOM 5644 CB ARG B 292 8.103 22.308 456.771 1.00 38.57 B C
ANISOU 5644 CB ARG B 292 5672 2813 6169 526 -527 -1122 B C
ATOM 5645 CG ARG B 292 9.413 22.567 456.067 1.00 32.69 B C
ANISOU 5645 CG ARG B 292 5035 2064 5322 354 -431 -1237 B C
ATOM 5646 CD ARG B 292 9.455 23.926 455.412 1.00 32.46 B C
ANISOU 5646 CD ARG B 292 5147 1901 5287 290 -477 -1217 B C
ATOM 5647 NE ARG B 292 10.820 24.226 454.984 1.00 43.70 B N
ANISOU 5647 NE ARG B 292 6661 3351 6591 123 -342 -1338 B N
ATOM 5648 CZ ARG B 292 11.359 23.757 453.866 1.00 33.20 B C
ANISOU 5648 CZ ARG B 292 5413 2035 5168 -98 -314 -1433 B C
ATOM 5649 NH1 ARG B 292 10.623 23.012 453.060 1.00 49.33 B N1+
ANISOU 5649 NH1 ARG B 292 7454 4058 7230 -181 -422 -1422 B N1+
ATOM 5650 NH2 ARG B 292 12.614 24.044 453.546 1.00 33.46 B N
ANISOU 5650 NH2 ARG B 292 5547 2109 5058 -247 -191 -1530 B N
ATOM 5651 N ILE B 293 5.683 20.546 457.952 1.00 30.36 B N
ANISOU 5651 N ILE B 293 4384 1869 5283 757 -658 -967 B N
ATOM 5652 CA ILE B 293 4.627 20.356 458.938 1.00 36.28 B C
ANISOU 5652 CA ILE B 293 5022 2679 6084 890 -678 -883 B C
ATOM 5653 C ILE B 293 4.854 19.062 459.710 1.00 30.13 B C
ANISOU 5653 C ILE B 293 4163 2000 5284 892 -605 -912 B C
ATOM 5654 O ILE B 293 4.714 19.041 460.936 1.00 39.16 B O
ANISOU 5654 O ILE B 293 5242 3224 6411 972 -550 -878 B O
ATOM 5655 CB ILE B 293 3.238 20.397 458.254 1.00 31.14 B C
ANISOU 5655 CB ILE B 293 4358 1947 5525 926 -838 -799 B C
ATOM 5656 CG1 ILE B 293 2.802 21.840 458.004 1.00 32.18 B C
ANISOU 5656 CG1 ILE B 293 4539 1996 5694 985 -918 -716 B C
ATOM 5657 CG2 ILE B 293 2.168 19.736 459.083 1.00 30.97 B C
ANISOU 5657 CG2 ILE B 293 4210 2006 5551 1020 -844 -746 B C
ATOM 5658 CD1 ILE B 293 2.422 22.580 459.257 1.00 32.13 B C
ANISOU 5658 CD1 ILE B 293 4444 2067 5698 1109 -840 -676 B C
ATOM 5659 N ARG B 294 5.315 18.004 459.033 1.00 29.18 B N
ANISOU 5659 N ARG B 294 4058 1870 5161 792 -597 -981 B N
ATOM 5660 CA ARG B 294 5.697 16.765 459.711 1.00 28.59 B C
ANISOU 5660 CA ARG B 294 3920 1867 5077 790 -532 -1003 B C
ATOM 5661 C ARG B 294 6.758 17.018 460.777 1.00 33.85 B C
ANISOU 5661 C ARG B 294 4577 2610 5674 825 -440 -1013 B C
ATOM 5662 O ARG B 294 6.608 16.590 461.935 1.00 37.05 B O
ANISOU 5662 O ARG B 294 4926 3074 6078 895 -418 -971 B O
ATOM 5663 CB ARG B 294 6.219 15.748 458.703 1.00 31.06 B C
ANISOU 5663 CB ARG B 294 4253 2151 5398 661 -520 -1093 B C
ATOM 5664 CG ARG B 294 5.239 15.286 457.648 1.00 34.04 B C
ANISOU 5664 CG ARG B 294 4638 2452 5845 593 -610 -1105 B C
ATOM 5665 CD ARG B 294 6.046 14.568 456.607 1.00 29.72 B C
ANISOU 5665 CD ARG B 294 4127 1897 5270 423 -559 -1224 B C
ATOM 5666 NE ARG B 294 5.341 14.478 455.345 1.00 42.46 B N
ANISOU 5666 NE ARG B 294 5785 3439 6909 289 -646 -1262 B N
ATOM 5667 CZ ARG B 294 5.949 14.124 454.219 1.00 50.38 B C
ANISOU 5667 CZ ARG B 294 6839 4454 7849 87 -601 -1374 B C
ATOM 5668 NH1 ARG B 294 7.245 13.839 454.243 1.00 53.61 B N1+
ANISOU 5668 NH1 ARG B 294 7254 4930 8187 37 -475 -1448 B N1+
ATOM 5669 NH2 ARG B 294 5.288 14.073 453.073 1.00 44.77 B N
ANISOU 5669 NH2 ARG B 294 6172 3706 7131 -81 -690 -1406 B N
ATOM 5670 N ARG B 295 7.832 17.733 460.419 1.00 28.00 B N
ANISOU 5670 N ARG B 295 3898 1864 4875 770 -391 -1072 B N
ATOM 5671 CA ARG B 295 8.878 17.961 461.406 1.00 27.56 B C
ANISOU 5671 CA ARG B 295 3829 1879 4763 798 -317 -1088 B C
ATOM 5672 C ARG B 295 8.323 18.767 462.568 1.00 36.21 B C
ANISOU 5672 C ARG B 295 4894 3009 5854 901 -310 -1021 B C
ATOM 5673 O ARG B 295 8.631 18.486 463.734 1.00 27.18 B O
ANISOU 5673 O ARG B 295 3705 1930 4692 950 -280 -1008 B O
ATOM 5674 CB ARG B 295 10.085 18.693 460.798 1.00 34.13 B C
ANISOU 5674 CB ARG B 295 4736 2700 5533 716 -263 -1167 B C
ATOM 5675 CG ARG B 295 10.754 18.121 459.547 1.00 33.21 B C
ANISOU 5675 CG ARG B 295 4664 2555 5398 584 -249 -1258 B C
ATOM 5676 CD ARG B 295 11.444 16.809 459.832 1.00 35.10 B C
ANISOU 5676 CD ARG B 295 4834 2848 5655 573 -228 -1295 B C
ATOM 5677 NE ARG B 295 12.393 16.411 458.801 1.00 48.17 B N
ANISOU 5677 NE ARG B 295 6520 4501 7279 447 -191 -1397 B N
ATOM 5678 CZ ARG B 295 12.021 15.845 457.653 1.00 60.98 B C
ANISOU 5678 CZ ARG B 295 8169 6085 8915 341 -205 -1443 B C
ATOM 5679 NH1 ARG B 295 10.728 15.646 457.396 1.00 56.81 B N1+
ANISOU 5679 NH1 ARG B 295 7638 5506 8442 355 -266 -1395 B N1+
ATOM 5680 NH2 ARG B 295 12.935 15.491 456.760 1.00 63.78 B N
ANISOU 5680 NH2 ARG B 295 8549 6457 9228 216 -163 -1541 B N
ATOM 5681 N LEU B 296 7.509 19.784 462.273 1.00 39.28 B N
ANISOU 5681 N LEU B 296 5307 3350 6267 934 -343 -983 B N
ATOM 5682 CA LEU B 296 6.934 20.582 463.344 1.00 28.01 B C
ANISOU 5682 CA LEU B 296 3841 1955 4845 1026 -325 -933 B C
ATOM 5683 C LEU B 296 6.070 19.741 464.280 1.00 27.90 B C
ANISOU 5683 C LEU B 296 3746 1996 4858 1089 -341 -884 B C
ATOM 5684 O LEU B 296 6.115 19.907 465.515 1.00 27.82 B O
ANISOU 5684 O LEU B 296 3697 2045 4827 1142 -299 -878 B O
ATOM 5685 CB LEU B 296 6.151 21.732 462.738 1.00 28.76 B C
ANISOU 5685 CB LEU B 296 3969 1971 4988 1055 -372 -898 B C
ATOM 5686 CG LEU B 296 5.290 22.557 463.688 1.00 29.47 B C
ANISOU 5686 CG LEU B 296 4004 2083 5110 1153 -360 -851 B C
ATOM 5687 CD1 LEU B 296 6.124 23.091 464.806 1.00 28.91 B C
ANISOU 5687 CD1 LEU B 296 3930 2071 4983 1167 -263 -891 B C
ATOM 5688 CD2 LEU B 296 4.685 23.683 462.888 1.00 30.20 B C
ANISOU 5688 CD2 LEU B 296 4136 2072 5266 1177 -420 -814 B C
ATOM 5689 N LEU B 297 5.312 18.804 463.715 1.00 28.01 B N
ANISOU 5689 N LEU B 297 3738 1985 4920 1078 -403 -860 B N
ATOM 5690 CA LEU B 297 4.526 17.860 464.510 1.00 28.02 B C
ANISOU 5690 CA LEU B 297 3671 2025 4950 1124 -416 -821 B C
ATOM 5691 C LEU B 297 5.425 17.018 465.416 1.00 28.86 B C
ANISOU 5691 C LEU B 297 3768 2178 5021 1118 -372 -841 B C
ATOM 5692 O LEU B 297 5.245 16.994 466.643 1.00 34.59 B O
ANISOU 5692 O LEU B 297 4456 2950 5737 1177 -351 -822 B O
ATOM 5693 CB LEU B 297 3.709 16.976 463.581 1.00 32.06 B C
ANISOU 5693 CB LEU B 297 4168 2487 5526 1094 -487 -806 B C
ATOM 5694 CG LEU B 297 2.596 17.772 462.905 1.00 34.33 B C
ANISOU 5694 CG LEU B 297 4443 2729 5870 1127 -562 -768 B C
ATOM 5695 CD1 LEU B 297 1.829 16.895 461.965 1.00 29.31 B C
ANISOU 5695 CD1 LEU B 297 3789 2040 5306 1092 -647 -762 B C
ATOM 5696 CD2 LEU B 297 1.692 18.440 463.915 1.00 40.24 B C
ANISOU 5696 CD2 LEU B 297 5126 3526 6636 1222 -549 -726 B C
ATOM 5697 N VAL B 298 6.408 16.316 464.836 1.00 27.39 B N
ANISOU 5697 N VAL B 298 3610 1973 4824 1051 -366 -885 B N
ATOM 5698 CA VAL B 298 7.208 15.410 465.661 1.00 28.25 B C
ANISOU 5698 CA VAL B 298 3699 2109 4926 1059 -348 -896 B C
ATOM 5699 C VAL B 298 7.957 16.176 466.745 1.00 35.83 B C
ANISOU 5699 C VAL B 298 4655 3124 5836 1100 -309 -912 B C
ATOM 5700 O VAL B 298 8.000 15.740 467.905 1.00 37.38 B O
ANISOU 5700 O VAL B 298 4817 3349 6037 1153 -315 -894 B O
ATOM 5701 CB VAL B 298 8.181 14.585 464.803 1.00 27.27 B C
ANISOU 5701 CB VAL B 298 3591 1954 4816 982 -347 -955 B C
ATOM 5702 CG1 VAL B 298 9.143 13.831 465.710 1.00 27.40 B C
ANISOU 5702 CG1 VAL B 298 3581 1991 4840 1007 -343 -968 B C
ATOM 5703 CG2 VAL B 298 7.434 13.627 463.901 1.00 27.52 B C
ANISOU 5703 CG2 VAL B 298 3616 1928 4913 938 -383 -952 B C
ATOM 5704 N ARG B 299 8.468 17.371 466.422 1.00 27.05 B N
ANISOU 5704 N ARG B 299 3577 2020 4682 1078 -273 -948 B N
ATOM 5705 CA ARG B 299 9.172 18.172 467.430 1.00 32.98 B C
ANISOU 5705 CA ARG B 299 4321 2821 5390 1109 -232 -976 B C
ATOM 5706 C ARG B 299 8.217 18.581 468.543 1.00 33.43 B C
ANISOU 5706 C ARG B 299 4335 2909 5456 1186 -228 -941 B C
ATOM 5707 O ARG B 299 8.586 18.604 469.723 1.00 27.53 B O
ANISOU 5707 O ARG B 299 3556 2208 4696 1228 -217 -962 B O
ATOM 5708 CB ARG B 299 9.760 19.436 466.793 1.00 34.68 B C
ANISOU 5708 CB ARG B 299 4588 3021 5566 1067 -189 -1019 B C
ATOM 5709 CG ARG B 299 10.820 19.215 465.751 1.00 34.54 B C
ANISOU 5709 CG ARG B 299 4606 2979 5539 986 -189 -1086 B C
ATOM 5710 CD ARG B 299 12.115 18.697 466.290 1.00 39.53 B C
ANISOU 5710 CD ARG B 299 5193 3654 6174 979 -198 -1157 B C
ATOM 5711 NE ARG B 299 12.066 17.249 466.365 1.00 35.92 B N
ANISOU 5711 NE ARG B 299 4700 3191 5758 986 -235 -1134 B N
ATOM 5712 CZ ARG B 299 12.241 16.443 465.339 1.00 36.56 B C
ANISOU 5712 CZ ARG B 299 4790 3235 5867 926 -247 -1158 B C
ATOM 5713 NH1 ARG B 299 12.472 16.960 464.133 1.00 36.76 B N1+
ANISOU 5713 NH1 ARG B 299 4866 3231 5870 849 -222 -1205 B N1+
ATOM 5714 NH2 ARG B 299 12.166 15.126 465.527 1.00 36.96 B N
ANISOU 5714 NH2 ARG B 299 4806 3270 5968 939 -277 -1136 B N
ATOM 5715 N THR B 300 6.975 18.910 468.183 1.00 31.86 B N
ANISOU 5715 N THR B 300 4129 2685 5290 1208 -243 -900 B N
ATOM 5716 CA THR B 300 6.026 19.324 469.201 1.00 28.02 B C
ANISOU 5716 CA THR B 300 3589 2232 4824 1280 -233 -885 B C
ATOM 5717 C THR B 300 5.683 18.167 470.135 1.00 34.15 B C
ANISOU 5717 C THR B 300 4320 3035 5623 1320 -261 -866 B C
ATOM 5718 O THR B 300 5.698 18.334 471.361 1.00 35.33 B O
ANISOU 5718 O THR B 300 4428 3229 5765 1371 -246 -895 B O
ATOM 5719 CB THR B 300 4.775 19.850 468.526 1.00 32.46 B C
ANISOU 5719 CB THR B 300 4139 2758 5435 1300 -257 -849 B C
ATOM 5720 CG2 THR B 300 3.833 20.408 469.591 1.00 29.05 B C
ANISOU 5720 CG2 THR B 300 3638 2365 5035 1374 -236 -857 B C
ATOM 5721 OG1 THR B 300 5.139 20.945 467.690 1.00 28.42 B O
ANISOU 5721 OG1 THR B 300 3681 2202 4915 1272 -243 -863 B O
ATOM 5722 N VAL B 301 5.382 16.983 469.573 1.00 28.16 B N
ANISOU 5722 N VAL B 301 3565 2237 4896 1298 -306 -827 B N
ATOM 5723 CA VAL B 301 5.110 15.795 470.396 1.00 28.54 B C
ANISOU 5723 CA VAL B 301 3583 2284 4977 1335 -340 -801 B C
ATOM 5724 C VAL B 301 6.324 15.436 471.261 1.00 28.64 B C
ANISOU 5724 C VAL B 301 3599 2314 4967 1351 -346 -828 B C
ATOM 5725 O VAL B 301 6.183 15.030 472.421 1.00 29.23 B O
ANISOU 5725 O VAL B 301 3643 2406 5059 1414 -374 -824 B O
ATOM 5726 CB VAL B 301 4.689 14.604 469.515 1.00 28.52 B C
ANISOU 5726 CB VAL B 301 3593 2220 5023 1295 -381 -760 B C
ATOM 5727 CG1 VAL B 301 4.670 13.355 470.325 1.00 29.03 B C
ANISOU 5727 CG1 VAL B 301 3645 2257 5130 1327 -418 -727 B C
ATOM 5728 CG2 VAL B 301 3.309 14.824 468.883 1.00 34.33 B C
ANISOU 5728 CG2 VAL B 301 4300 2942 5800 1299 -399 -736 B C
ATOM 5729 N GLU B 302 7.535 15.612 470.730 1.00 28.22 B N
ANISOU 5729 N GLU B 302 3580 2260 4883 1302 -332 -865 B N
ATOM 5730 CA GLU B 302 8.724 15.287 471.518 1.00 28.48 B C
ANISOU 5730 CA GLU B 302 3602 2311 4908 1324 -353 -900 B C
ATOM 5731 C GLU B 302 8.903 16.269 472.673 1.00 35.52 B C
ANISOU 5731 C GLU B 302 4463 3270 5763 1376 -332 -951 B C
ATOM 5732 O GLU B 302 9.226 15.860 473.798 1.00 30.87 B O
ANISOU 5732 O GLU B 302 3842 2703 5184 1440 -378 -968 B O
ATOM 5733 CB GLU B 302 9.964 15.313 470.629 1.00 28.09 B C
ANISOU 5733 CB GLU B 302 3579 2251 4843 1257 -339 -948 B C
ATOM 5734 CG GLU B 302 10.137 14.050 469.818 1.00 39.82 B C
ANISOU 5734 CG GLU B 302 5073 3674 6380 1218 -372 -931 B C
ATOM 5735 CD GLU B 302 11.180 14.160 468.706 1.00 43.38 B C
ANISOU 5735 CD GLU B 302 5543 4118 6822 1140 -348 -998 B C
ATOM 5736 OE1 GLU B 302 11.655 15.273 468.398 1.00 39.15 B O
ANISOU 5736 OE1 GLU B 302 5027 3616 6232 1109 -305 -1044 B O
ATOM 5737 OE2 GLU B 302 11.429 13.129 468.045 1.00 57.66 B O1-
ANISOU 5737 OE2 GLU B 302 7347 5878 8684 1105 -369 -1008 B O1-
ATOM 5738 N PHE B 303 8.685 17.575 472.420 1.00 49.98 B N
ANISOU 5738 N PHE B 303 6303 5128 7559 1355 -269 -982 B N
ATOM 5739 CA PHE B 303 8.766 18.556 473.498 1.00 28.89 B C
ANISOU 5739 CA PHE B 303 3596 2519 4860 1397 -235 -1046 B C
ATOM 5740 C PHE B 303 7.654 18.350 474.497 1.00 37.94 B C
ANISOU 5740 C PHE B 303 4687 3694 6036 1470 -250 -1045 B C
ATOM 5741 O PHE B 303 7.886 18.433 475.709 1.00 37.22 B O
ANISOU 5741 O PHE B 303 4549 3661 5931 1527 -262 -1112 B O
ATOM 5742 CB PHE B 303 8.711 19.974 472.918 1.00 42.98 B C
ANISOU 5742 CB PHE B 303 5409 4300 6619 1358 -163 -1069 B C
ATOM 5743 CG PHE B 303 8.889 21.072 473.947 1.00 33.92 B C
ANISOU 5743 CG PHE B 303 4229 3211 5449 1386 -112 -1150 B C
ATOM 5744 CD1 PHE B 303 7.806 21.513 474.701 1.00 29.76 B C
ANISOU 5744 CD1 PHE B 303 3647 2714 4947 1437 -87 -1174 B C
ATOM 5745 CD2 PHE B 303 10.135 21.622 474.194 1.00 29.09 B C
ANISOU 5745 CD2 PHE B 303 3628 2631 4794 1359 -87 -1219 B C
ATOM 5746 CE1 PHE B 303 7.970 22.483 475.671 1.00 30.39 B C
ANISOU 5746 CE1 PHE B 303 3685 2853 5007 1456 -32 -1269 B C
ATOM 5747 CE2 PHE B 303 10.300 22.599 475.157 1.00 29.66 B C
ANISOU 5747 CE2 PHE B 303 3665 2761 4844 1379 -37 -1305 B C
ATOM 5748 CZ PHE B 303 9.227 23.021 475.901 1.00 30.32 B C
ANISOU 5748 CZ PHE B 303 3695 2874 4951 1425 -7 -1333 B C
ATOM 5749 N ALA B 304 6.473 17.962 474.015 1.00 42.49 B N
ANISOU 5749 N ALA B 304 5259 4234 6653 1473 -259 -984 B N
ATOM 5750 CA ALA B 304 5.352 17.762 474.922 1.00 33.60 B C
ANISOU 5750 CA ALA B 304 4066 3138 5563 1540 -269 -999 B C
ATOM 5751 C ALA B 304 5.595 16.525 475.777 1.00 38.30 B C
ANISOU 5751 C ALA B 304 4649 3729 6177 1597 -348 -984 B C
ATOM 5752 O ALA B 304 5.282 16.505 476.969 1.00 35.71 B O
ANISOU 5752 O ALA B 304 4260 3457 5850 1672 -365 -1046 B O
ATOM 5753 CB ALA B 304 4.043 17.645 474.144 1.00 30.34 B C
ANISOU 5753 CB ALA B 304 3640 2689 5200 1530 -268 -945 B C
ATOM 5754 N ALA B 305 6.185 15.491 475.196 1.00 30.67 B N
ANISOU 5754 N ALA B 305 3734 2693 5227 1567 -403 -912 B N
ATOM 5755 CA ALA B 305 6.425 14.291 475.974 1.00 33.20 B C
ANISOU 5755 CA ALA B 305 4055 2979 5582 1629 -499 -871 B C
ATOM 5756 C ALA B 305 7.421 14.527 477.108 1.00 35.75 B C
ANISOU 5756 C ALA B 305 4355 3362 5866 1699 -547 -939 B C
ATOM 5757 O ALA B 305 7.117 14.237 478.273 1.00 45.89 B O
ANISOU 5757 O ALA B 305 5605 4682 7150 1799 -617 -955 B O
ATOM 5758 CB ALA B 305 6.892 13.152 475.068 1.00 31.20 B C
ANISOU 5758 CB ALA B 305 3856 2631 5369 1575 -538 -787 B C
ATOM 5759 N GLU B 306 8.589 15.105 476.816 1.00 31.62 B N
ANISOU 5759 N GLU B 306 3845 2867 5304 1657 -517 -993 B N
ATOM 5760 CA GLU B 306 9.501 15.418 477.914 1.00 34.15 B C
ANISOU 5760 CA GLU B 306 4129 3262 5583 1729 -564 -1080 B C
ATOM 5761 C GLU B 306 8.812 16.206 479.012 1.00 35.89 B C
ANISOU 5761 C GLU B 306 4285 3592 5759 1798 -530 -1184 B C
ATOM 5762 O GLU B 306 8.926 15.866 480.193 1.00 34.23 B O
ANISOU 5762 O GLU B 306 4039 3463 5503 1885 -609 -1208 B O
ATOM 5763 CB GLU B 306 10.696 16.232 477.409 1.00 44.12 B C
ANISOU 5763 CB GLU B 306 5401 4555 6809 1659 -507 -1153 B C
ATOM 5764 CG GLU B 306 11.511 15.564 476.313 1.00 58.05 B C
ANISOU 5764 CG GLU B 306 7205 6243 8609 1591 -523 -1102 B C
ATOM 5765 CD GLU B 306 12.095 14.238 476.721 1.00 68.36 B C
ANISOU 5765 CD GLU B 306 8505 7494 9974 1654 -650 -1050 B C
ATOM 5766 OE1 GLU B 306 12.991 14.232 477.571 1.00 71.36 B O
ANISOU 5766 OE1 GLU B 306 8850 7919 10346 1725 -728 -1106 B O
ATOM 5767 OE2 GLU B 306 11.669 13.199 476.161 1.00 74.02 B O1-
ANISOU 5767 OE2 GLU B 306 9253 8121 10752 1634 -676 -953 B O1-
ATOM 5768 N ARG B 307 7.946 17.138 478.624 1.00 43.42 B N
ANISOU 5768 N ARG B 307 5221 4567 6709 1741 -414 -1217 B N
ATOM 5769 CA ARG B 307 7.173 17.909 479.587 1.00 33.35 B C
ANISOU 5769 CA ARG B 307 3863 3404 5406 1785 -350 -1339 B C
ATOM 5770 C ARG B 307 6.269 17.002 480.407 1.00 44.95 B C
ANISOU 5770 C ARG B 307 5303 4944 6833 1793 -392 -1270 B C
ATOM 5771 O ARG B 307 6.199 17.123 481.632 1.00 59.29 B O
ANISOU 5771 O ARG B 307 7080 6949 8500 1724 -361 -1280 B O
ATOM 5772 CB ARG B 307 6.390 18.974 478.844 1.00 44.96 B C
ANISOU 5772 CB ARG B 307 5329 4853 6899 1704 -233 -1338 B C
ATOM 5773 CG ARG B 307 5.693 19.992 479.694 1.00 42.17 B C
ANISOU 5773 CG ARG B 307 4881 4608 6532 1715 -135 -1476 B C
ATOM 5774 CD ARG B 307 6.611 20.878 480.451 1.00 38.06 B C
ANISOU 5774 CD ARG B 307 4333 4185 5941 1702 -84 -1605 B C
ATOM 5775 NE ARG B 307 5.835 21.621 481.439 1.00 39.24 B N
ANISOU 5775 NE ARG B 307 4370 4465 6073 1702 19 -1759 B N
ATOM 5776 CZ ARG B 307 6.360 22.248 482.477 1.00 40.11 B C
ANISOU 5776 CZ ARG B 307 4415 4722 6102 1689 82 -1919 B C
ATOM 5777 NH1 ARG B 307 7.672 22.225 482.674 1.00 41.00 B N1+
ANISOU 5777 NH1 ARG B 307 4565 4865 6148 1694 35 -1943 B N1+
ATOM 5778 NH2 ARG B 307 5.568 22.886 483.326 1.00 50.61 B N
ANISOU 5778 NH2 ARG B 307 5631 6185 7413 1656 199 -2067 B N
ATOM 5779 N LEU B 308 5.547 16.099 479.745 1.00 46.67 B N
ANISOU 5779 N LEU B 308 5558 5058 7115 1776 -433 -1141 B N
ATOM 5780 CA LEU B 308 4.630 15.210 480.451 1.00 45.61 B C
ANISOU 5780 CA LEU B 308 5427 5021 6884 1676 -439 -1003 B C
ATOM 5781 C LEU B 308 5.362 14.324 481.449 1.00 46.74 B C
ANISOU 5781 C LEU B 308 5620 5246 6892 1626 -532 -876 B C
ATOM 5782 O LEU B 308 4.920 14.194 482.598 1.00 40.95 B O
ANISOU 5782 O LEU B 308 4870 4694 5997 1521 -505 -830 B O
ATOM 5783 CB LEU B 308 3.878 14.336 479.446 1.00 34.80 B C
ANISOU 5783 CB LEU B 308 4096 3506 5621 1666 -471 -894 B C
ATOM 5784 CG LEU B 308 2.768 13.451 480.013 1.00 40.62 B C
ANISOU 5784 CG LEU B 308 4835 4325 6274 1550 -457 -766 B C
ATOM 5785 CD1 LEU B 308 1.814 14.270 480.806 1.00 59.49 B C
ANISOU 5785 CD1 LEU B 308 7128 6898 8578 1486 -339 -867 B C
ATOM 5786 CD2 LEU B 308 2.018 12.797 478.877 1.00 35.33 B C
ANISOU 5786 CD2 LEU B 308 4185 3512 5726 1545 -470 -703 B C
ATOM 5787 N TRP B 309 6.520 13.768 481.056 1.00 36.10 B N
ANISOU 5787 N TRP B 309 4329 3777 5610 1696 -644 -828 B N
ATOM 5788 CA TRP B 309 7.308 12.946 481.976 1.00 43.85 B C
ANISOU 5788 CA TRP B 309 5352 4820 6488 1671 -763 -697 B C
ATOM 5789 C TRP B 309 7.835 13.779 483.135 1.00 55.19 B C
ANISOU 5789 C TRP B 309 6737 6474 7760 1641 -735 -789 B C
ATOM 5790 O TRP B 309 7.898 13.301 484.272 1.00 60.79 B O
ANISOU 5790 O TRP B 309 7465 7334 8300 1555 -792 -672 B O
ATOM 5791 CB TRP B 309 8.470 12.265 481.243 1.00 39.37 B C
ANISOU 5791 CB TRP B 309 4827 4064 6066 1770 -886 -664 B C
ATOM 5792 CG TRP B 309 8.125 11.643 479.902 1.00 35.92 B C
ANISOU 5792 CG TRP B 309 4427 3409 5813 1800 -891 -637 B C
ATOM 5793 CD1 TRP B 309 8.958 11.517 478.841 1.00 34.99 B C
ANISOU 5793 CD1 TRP B 309 4317 3119 5859 1881 -929 -713 B C
ATOM 5794 CD2 TRP B 309 6.880 11.034 479.504 1.00 43.04 B C
ANISOU 5794 CD2 TRP B 309 5355 4256 6742 1730 -853 -540 B C
ATOM 5795 CE2 TRP B 309 7.038 10.598 478.178 1.00 41.01 B C
ANISOU 5795 CE2 TRP B 309 5120 3798 6663 1775 -871 -564 B C
ATOM 5796 CE3 TRP B 309 5.644 10.830 480.135 1.00 50.92 B C
ANISOU 5796 CE3 TRP B 309 6352 5369 7627 1621 -796 -453 B C
ATOM 5797 NE1 TRP B 309 8.310 10.920 477.794 1.00 34.37 B N
ANISOU 5797 NE1 TRP B 309 4272 2944 5843 1794 -872 -645 B N
ATOM 5798 CZ2 TRP B 309 6.010 9.963 477.469 1.00 46.43 B C
ANISOU 5798 CZ2 TRP B 309 5828 4398 7415 1718 -840 -496 B C
ATOM 5799 CZ3 TRP B 309 4.621 10.202 479.424 1.00 36.51 B C
ANISOU 5799 CZ3 TRP B 309 4545 3451 5874 1571 -765 -390 B C
ATOM 5800 CH2 TRP B 309 4.813 9.778 478.109 1.00 35.48 B C
ANISOU 5800 CH2 TRP B 309 4438 3124 5920 1622 -790 -409 B C
ATOM 5801 N LEU B 310 8.231 15.023 482.868 1.00 51.60 B N
ANISOU 5801 N LEU B 310 6222 6041 7345 1700 -649 -996 B N
ATOM 5802 CA LEU B 310 8.618 15.896 483.964 1.00 43.32 B C
ANISOU 5802 CA LEU B 310 5110 5209 6139 1655 -595 -1113 B C
ATOM 5803 C LEU B 310 7.457 16.118 484.911 1.00 39.45 B C
ANISOU 5803 C LEU B 310 4577 4914 5497 1520 -492 -1111 B C
ATOM 5804 O LEU B 310 7.647 16.143 486.131 1.00 40.98 B O
ANISOU 5804 O LEU B 310 4751 5325 5494 1421 -497 -1097 B O
ATOM 5805 CB LEU B 310 9.128 17.230 483.428 1.00 49.30 B C
ANISOU 5805 CB LEU B 310 5814 5931 6989 1732 -498 -1347 B C
ATOM 5806 CG LEU B 310 9.495 18.219 484.529 1.00 45.18 B C
ANISOU 5806 CG LEU B 310 5215 5633 6317 1677 -417 -1503 B C
ATOM 5807 CD1 LEU B 310 10.521 17.561 485.425 1.00 53.71 B C
ANISOU 5807 CD1 LEU B 310 6312 6843 7252 1650 -553 -1408 B C
ATOM 5808 CD2 LEU B 310 10.048 19.504 483.944 1.00 43.59 B C
ANISOU 5808 CD2 LEU B 310 4975 5365 6224 1750 -321 -1731 B C
ATOM 5809 N ILE B 311 6.237 16.211 484.379 1.00 45.02 B N
ANISOU 5809 N ILE B 311 5264 5556 6285 1503 -404 -1123 B N
ATOM 5810 CA ILE B 311 5.087 16.476 485.239 1.00 46.30 B C
ANISOU 5810 CA ILE B 311 5362 5906 6323 1370 -289 -1161 B C
ATOM 5811 C ILE B 311 4.813 15.258 486.102 1.00 51.42 B C
ANISOU 5811 C ILE B 311 6077 6663 6796 1234 -367 -947 B C
ATOM 5812 O ILE B 311 4.532 15.376 487.301 1.00 55.35 B O
ANISOU 5812 O ILE B 311 6544 7397 7090 1088 -316 -960 B O
ATOM 5813 CB ILE B 311 3.848 16.890 484.422 1.00 48.11 B C
ANISOU 5813 CB ILE B 311 5537 6039 6705 1396 -186 -1237 B C
ATOM 5814 CG1 ILE B 311 4.016 18.312 483.876 1.00 45.94 B C
ANISOU 5814 CG1 ILE B 311 5187 5700 6570 1500 -92 -1457 B C
ATOM 5815 CG2 ILE B 311 2.584 16.780 485.259 1.00 51.04 B C
ANISOU 5815 CG2 ILE B 311 5845 6589 6957 1245 -87 -1243 B C
ATOM 5816 CD1 ILE B 311 2.992 18.700 482.832 1.00 47.43 B C
ANISOU 5816 CD1 ILE B 311 5333 5742 6945 1564 -39 -1504 B C
ATOM 5817 N HIS B 312 4.907 14.070 485.510 1.00 45.85 B N
ANISOU 5817 N HIS B 312 5469 5787 6166 1267 -490 -751 B N
ATOM 5818 CA HIS B 312 4.760 12.845 486.281 1.00 45.51 B C
ANISOU 5818 CA HIS B 312 5512 5807 5973 1144 -586 -521 B C
ATOM 5819 C HIS B 312 5.827 12.754 487.364 1.00 48.04 B C
ANISOU 5819 C HIS B 312 5857 6281 6116 1105 -688 -458 B C
ATOM 5820 O HIS B 312 5.528 12.451 488.524 1.00 50.58 B O
ANISOU 5820 O HIS B 312 6199 6808 6211 939 -693 -365 B O
ATOM 5821 CB HIS B 312 4.771 11.655 485.333 1.00 46.00 B C
ANISOU 5821 CB HIS B 312 5666 5620 6193 1206 -694 -348 B C
ATOM 5822 CG HIS B 312 3.564 11.619 484.450 1.00 47.53 B C
ANISOU 5822 CG HIS B 312 5835 5715 6510 1198 -597 -387 B C
ATOM 5823 CD2 HIS B 312 2.386 12.289 484.535 1.00 45.85 B C
ANISOU 5823 CD2 HIS B 312 5535 5613 6273 1131 -449 -512 B C
ATOM 5824 ND1 HIS B 312 3.448 10.777 483.365 1.00 54.63 B N
ANISOU 5824 ND1 HIS B 312 6790 6388 7578 1256 -655 -294 B N
ATOM 5825 CE1 HIS B 312 2.266 10.957 482.796 1.00 57.14 B C
ANISOU 5825 CE1 HIS B 312 7061 6691 7960 1224 -552 -355 B C
ATOM 5826 NE2 HIS B 312 1.599 11.861 483.493 1.00 54.10 B N
ANISOU 5826 NE2 HIS B 312 6585 6502 7467 1156 -432 -485 B N
ATOM 5827 N SER B 313 7.073 13.036 487.010 1.00 53.53 B N
ANISOU 5827 N SER B 313 6545 6895 6900 1243 -771 -515 B N
ATOM 5828 CA SER B 313 8.160 12.925 487.975 1.00 51.09 B C
ANISOU 5828 CA SER B 313 6246 6729 6436 1222 -891 -456 B C
ATOM 5829 C SER B 313 7.976 13.874 489.155 1.00 56.68 B C
ANISOU 5829 C SER B 313 6877 7747 6913 1085 -777 -594 B C
ATOM 5830 O SER B 313 8.253 13.505 490.300 1.00 71.31 B O
ANISOU 5830 O SER B 313 8757 9798 8538 960 -857 -475 B O
ATOM 5831 CB SER B 313 9.488 13.197 487.288 1.00 49.03 B C
ANISOU 5831 CB SER B 313 5964 6332 6334 1398 -973 -547 B C
ATOM 5832 OG SER B 313 10.537 12.626 488.024 1.00 53.35 B O
ANISOU 5832 OG SER B 313 6538 6950 6784 1403 -1150 -417 B O
ATOM 5833 N ARG B 314 7.466 15.084 488.908 1.00 58.15 B N
ANISOU 5833 N ARG B 314 6964 7978 7152 1093 -590 -843 B N
ATOM 5834 CA ARG B 314 7.232 16.017 490.007 1.00 53.67 B C
ANISOU 5834 CA ARG B 314 6307 7698 6388 954 -456 -1010 B C
ATOM 5835 C ARG B 314 6.082 15.560 490.887 1.00 55.20 B C
ANISOU 5835 C ARG B 314 6512 8075 6389 742 -393 -922 B C
ATOM 5836 O ARG B 314 6.032 15.893 492.077 1.00 59.63 B O
ANISOU 5836 O ARG B 314 7029 8917 6709 570 -336 -979 B O
ATOM 5837 CB ARG B 314 6.968 17.401 489.416 1.00 53.99 B C
ANISOU 5837 CB ARG B 314 6238 7690 6587 1035 -276 -1299 B C
ATOM 5838 CG ARG B 314 8.263 18.133 489.127 1.00 58.83 B C
ANISOU 5838 CG ARG B 314 6822 8259 7271 1159 -303 -1439 B C
ATOM 5839 CD ARG B 314 8.132 19.380 488.264 1.00 66.13 B C
ANISOU 5839 CD ARG B 314 7676 9051 8401 1268 -157 -1682 B C
ATOM 5840 NE ARG B 314 9.425 20.073 488.243 1.00 79.05 B N
ANISOU 5840 NE ARG B 314 9286 10698 10050 1340 -171 -1823 B N
ATOM 5841 CZ ARG B 314 9.776 21.033 487.392 1.00 66.14 B C
ANISOU 5841 CZ ARG B 314 7625 8912 8594 1451 -93 -2003 B C
ATOM 5842 NH1 ARG B 314 8.933 21.435 486.450 1.00 64.18 B N1+
ANISOU 5842 NH1 ARG B 314 7373 8478 8533 1515 -11 -2050 B N1+
ATOM 5843 NH2 ARG B 314 10.978 21.588 487.488 1.00 64.79 B N
ANISOU 5843 NH2 ARG B 314 7431 8779 8407 1489 -103 -2132 B N
ATOM 5844 N ASN B 315 5.159 14.790 490.329 1.00 54.14 B N
ANISOU 5844 N ASN B 315 6432 7797 6343 732 -396 -793 B N
ATOM 5845 CA ASN B 315 4.082 14.242 491.134 1.00 57.97 B C
ANISOU 5845 CA ASN B 315 6938 8448 6641 515 -339 -700 B C
ATOM 5846 C ASN B 315 4.614 13.213 492.129 1.00 62.52 B C
ANISOU 5846 C ASN B 315 7631 9149 6976 380 -505 -437 B C
ATOM 5847 O ASN B 315 4.170 13.159 493.286 1.00 64.91 B O
ANISOU 5847 O ASN B 315 7933 9718 7011 151 -453 -415 B O
ATOM 5848 CB ASN B 315 3.068 13.589 490.209 1.00 59.20 B C
ANISOU 5848 CB ASN B 315 7128 8401 6963 546 -318 -618 B C
ATOM 5849 CG ASN B 315 2.212 14.589 489.490 1.00 61.40 B C
ANISOU 5849 CG ASN B 315 7280 8625 7425 618 -145 -862 B C
ATOM 5850 ND2 ASN B 315 1.542 14.133 488.434 1.00 59.67 B N
ANISOU 5850 ND2 ASN B 315 7080 8198 7391 694 -150 -807 B N
ATOM 5851 OD1 ASN B 315 2.189 15.771 489.836 1.00 71.58 B O
ANISOU 5851 OD1 ASN B 315 8450 10045 8703 612 -15 -1100 B O
ATOM 5852 N VAL B 316 5.587 12.401 491.695 1.00 62.21 B N
ANISOU 5852 N VAL B 316 7689 8918 7029 514 -710 -240 B N
ATOM 5853 CA VAL B 316 6.263 11.470 492.595 1.00 63.91 B C
ANISOU 5853 CA VAL B 316 8012 9222 7049 423 -906 23 B C
ATOM 5854 C VAL B 316 6.977 12.201 493.721 1.00 73.82 B C
ANISOU 5854 C VAL B 316 9206 10777 8064 329 -910 -71 B C
ATOM 5855 O VAL B 316 6.875 11.808 494.890 1.00 93.50 B O
ANISOU 5855 O VAL B 316 11751 13505 10269 118 -961 70 B O
ATOM 5856 CB VAL B 316 7.229 10.566 491.810 1.00 59.60 B C
ANISOU 5856 CB VAL B 316 7549 8385 6710 621 -1121 207 B C
ATOM 5857 CG1 VAL B 316 7.979 9.644 492.758 1.00 60.50 B C
ANISOU 5857 CG1 VAL B 316 7765 8576 6648 548 -1349 487 B C
ATOM 5858 CG2 VAL B 316 6.478 9.782 490.747 1.00 57.68 B C
ANISOU 5858 CG2 VAL B 316 7367 7864 6684 681 -1108 297 B C
ATOM 5859 N GLU B 317 7.687 13.284 493.407 1.00 67.42 B N
ANISOU 5859 N GLU B 317 8287 9977 7353 463 -850 -315 B N
ATOM 5860 CA GLU B 317 8.341 14.033 494.474 1.00 72.04 B C
ANISOU 5860 CA GLU B 317 8801 10864 7708 361 -834 -435 B C
ATOM 5861 C GLU B 317 7.321 14.574 495.473 1.00 75.72 B C
ANISOU 5861 C GLU B 317 9206 11634 7930 101 -638 -565 B C
ATOM 5862 O GLU B 317 7.499 14.443 496.689 1.00 81.10 B O
ANISOU 5862 O GLU B 317 9904 12605 8305 -104 -681 -491 B O
ATOM 5863 CB GLU B 317 9.189 15.165 493.896 1.00 81.47 B C
ANISOU 5863 CB GLU B 317 9885 12002 9069 539 -770 -704 B C
ATOM 5864 CG GLU B 317 10.383 14.712 493.057 1.00 91.85 B C
ANISOU 5864 CG GLU B 317 11239 13070 10590 768 -960 -615 B C
ATOM 5865 CD GLU B 317 11.146 15.884 492.436 1.00 98.81 B C
ANISOU 5865 CD GLU B 317 12017 13897 11630 918 -869 -901 B C
ATOM 5866 OE1 GLU B 317 10.624 16.523 491.498 1.00 96.08 B O
ANISOU 5866 OE1 GLU B 317 11634 13386 11485 1005 -718 -1069 B O
ATOM 5867 OE2 GLU B 317 12.282 16.159 492.890 1.00100.31 B O1-
ANISOU 5867 OE2 GLU B 317 12165 14209 11738 943 -956 -952 B O1-
ATOM 5868 N ARG B 318 6.236 15.176 494.979 1.00 72.74 B N
ANISOU 5868 N ARG B 318 8751 11204 7685 98 -425 -763 B N
ATOM 5869 CA ARG B 318 5.227 15.711 495.889 1.00 75.26 B C
ANISOU 5869 CA ARG B 318 8986 11805 7804 -147 -222 -927 B C
ATOM 5870 C ARG B 318 4.656 14.613 496.787 1.00 83.99 B C
ANISOU 5870 C ARG B 318 10206 13072 8635 -400 -291 -671 B C
ATOM 5871 O ARG B 318 4.443 14.820 497.996 1.00 85.17 B O
ANISOU 5871 O ARG B 318 10328 13554 8480 -659 -218 -720 B O
ATOM 5872 CB ARG B 318 4.121 16.397 495.086 1.00 72.29 B C
ANISOU 5872 CB ARG B 318 8505 11297 7666 -78 -14 -1156 B C
ATOM 5873 CG ARG B 318 3.447 17.562 495.803 1.00 84.23 B C
ANISOU 5873 CG ARG B 318 9851 13062 9089 -235 236 -1482 B C
ATOM 5874 CD ARG B 318 2.751 18.519 494.823 1.00 97.16 B C
ANISOU 5874 CD ARG B 318 11362 14510 11046 -72 405 -1740 B C
ATOM 5875 NE ARG B 318 3.674 19.154 493.874 1.00103.92 B N
ANISOU 5875 NE ARG B 318 12207 15137 12142 187 354 -1818 B N
ATOM 5876 CZ ARG B 318 3.653 18.962 492.554 1.00 95.96 B C
ANISOU 5876 CZ ARG B 318 11244 13810 11406 404 286 -1746 B C
ATOM 5877 NH1 ARG B 318 2.745 18.154 492.016 1.00 99.03 B N1+
ANISOU 5877 NH1 ARG B 318 11685 14070 11874 405 259 -1599 B N1+
ATOM 5878 NH2 ARG B 318 4.533 19.582 491.768 1.00 76.27 B N
ANISOU 5878 NH2 ARG B 318 8744 11137 9097 603 251 -1830 B N
ATOM 5879 N TYR B 319 4.431 13.426 496.216 1.00 77.01 B N
ANISOU 5879 N TYR B 319 9457 11956 7847 -342 -429 -396 B N
ATOM 5880 CA TYR B 319 3.899 12.310 496.992 1.00 72.38 B C
ANISOU 5880 CA TYR B 319 9003 11481 7016 -580 -504 -125 B C
ATOM 5881 C TYR B 319 4.883 11.836 498.051 1.00 74.61 B C
ANISOU 5881 C TYR B 319 9379 11953 7017 -697 -705 96 B C
ATOM 5882 O TYR B 319 4.481 11.490 499.167 1.00 74.32 B O
ANISOU 5882 O TYR B 319 9399 12184 6655 -988 -697 204 B O
ATOM 5883 CB TYR B 319 3.533 11.154 496.076 1.00 66.44 B C
ANISOU 5883 CB TYR B 319 8374 10407 6461 -475 -610 113 B C
ATOM 5884 CG TYR B 319 3.010 9.952 496.816 1.00 66.26 B C
ANISOU 5884 CG TYR B 319 8508 10462 6207 -719 -692 410 B C
ATOM 5885 CD1 TYR B 319 1.710 9.928 497.303 1.00 67.36 B C
ANISOU 5885 CD1 TYR B 319 8630 10777 6189 -975 -507 338 B C
ATOM 5886 CD2 TYR B 319 3.809 8.834 497.012 1.00 65.28 B C
ANISOU 5886 CD2 TYR B 319 8548 10222 6035 -695 -956 759 B C
ATOM 5887 CE1 TYR B 319 1.225 8.828 497.971 1.00 69.29 B C
ANISOU 5887 CE1 TYR B 319 9029 11089 6209 -1220 -573 611 B C
ATOM 5888 CE2 TYR B 319 3.331 7.732 497.677 1.00 67.59 B C
ANISOU 5888 CE2 TYR B 319 9000 10562 6120 -923 -1038 1048 B C
ATOM 5889 CZ TYR B 319 2.042 7.736 498.155 1.00 69.27 B C
ANISOU 5889 CZ TYR B 319 9206 10957 6155 -1195 -841 976 B C
ATOM 5890 OH TYR B 319 1.560 6.639 498.817 1.00 74.58 B O
ANISOU 5890 OH TYR B 319 10051 11678 6610 -1445 -914 1265 B O
ATOM 5891 N MET B 320 6.172 11.794 497.719 1.00 75.04 B N
ANISOU 5891 N MET B 320 9448 11879 7185 -484 -893 168 B N
ATOM 5892 CA MET B 320 7.169 11.399 498.710 1.00 77.56 B C
ANISOU 5892 CA MET B 320 9834 12383 7251 -573 -1106 372 B C
ATOM 5893 C MET B 320 7.276 12.419 499.841 1.00 79.01 B C
ANISOU 5893 C MET B 320 9906 12977 7136 -783 -977 151 B C
ATOM 5894 O MET B 320 7.520 12.041 500.995 1.00 82.22 B O
ANISOU 5894 O MET B 320 10380 13653 7206 -1010 -1088 324 B O
ATOM 5895 CB MET B 320 8.517 11.184 498.029 1.00 79.03 B C
ANISOU 5895 CB MET B 320 10028 12334 7663 -281 -1325 454 B C
ATOM 5896 CG MET B 320 8.596 9.887 497.242 1.00 83.63 B C
ANISOU 5896 CG MET B 320 10748 12559 8468 -131 -1514 748 B C
ATOM 5897 SD MET B 320 10.248 9.549 496.609 1.00100.90 B S
ANISOU 5897 SD MET B 320 12930 14505 10904 182 -1784 839 B S
ATOM 5898 CE MET B 320 10.478 10.891 495.440 1.00100.65 B C
ANISOU 5898 CE MET B 320 12730 14355 11159 407 -1576 422 B C
ATOM 5899 N VAL B 321 7.120 13.713 499.532 1.00 83.55 B N
ANISOU 5899 N VAL B 321 10313 13603 7828 -719 -748 -228 B N
ATOM 5900 CA VAL B 321 7.030 14.723 500.592 1.00 87.70 B C
ANISOU 5900 CA VAL B 321 10716 14517 8089 -946 -575 -484 B C
ATOM 5901 C VAL B 321 5.841 14.436 501.502 1.00 81.42 B C
ANISOU 5901 C VAL B 321 9950 13976 7011 -1289 -442 -458 B C
ATOM 5902 O VAL B 321 5.940 14.561 502.729 1.00 87.05 B O
ANISOU 5902 O VAL B 321 10657 15055 7363 -1568 -430 -461 B O
ATOM 5903 CB VAL B 321 6.964 16.143 500.003 1.00 82.18 B C
ANISOU 5903 CB VAL B 321 9833 13771 7618 -804 -339 -899 B C
ATOM 5904 CG1 VAL B 321 6.587 17.152 501.091 1.00 82.02 B C
ANISOU 5904 CG1 VAL B 321 9675 14139 7349 -1070 -111 -1197 B C
ATOM 5905 CG2 VAL B 321 8.297 16.508 499.398 1.00 76.89 B C
ANISOU 5905 CG2 VAL B 321 9136 12948 7133 -539 -466 -941 B C
ATOM 5906 N THR B 322 4.694 14.071 500.922 1.00 75.74 B N
ANISOU 5906 N THR B 322 9254 13085 6437 -1293 -333 -449 B N
ATOM 5907 CA THR B 322 3.552 13.708 501.763 1.00 77.55 B C
ANISOU 5907 CA THR B 322 9516 13551 6399 -1633 -207 -421 B C
ATOM 5908 C THR B 322 3.897 12.509 502.644 1.00 79.60 B C
ANISOU 5908 C THR B 322 9974 13938 6334 -1840 -442 -18 B C
ATOM 5909 O THR B 322 3.503 12.455 503.816 1.00 82.93 B O
ANISOU 5909 O THR B 322 10416 14710 6385 -2190 -378 -6 B O
ATOM 5910 CB THR B 322 2.298 13.429 500.938 1.00 81.73 B C
ANISOU 5910 CB THR B 322 10037 13863 7153 -1591 -70 -465 B C
ATOM 5911 CG2 THR B 322 1.774 14.711 500.316 1.00 76.74 B C
ANISOU 5911 CG2 THR B 322 9194 13179 6784 -1457 182 -879 B C
ATOM 5912 OG1 THR B 322 2.583 12.460 499.923 1.00 97.89 B O
ANISOU 5912 OG1 THR B 322 12219 15534 9441 -1353 -269 -187 B O
ATOM 5913 N VAL B 323 4.556 11.498 502.074 1.00 78.58 B N
ANISOU 5913 N VAL B 323 9994 13516 6346 -1642 -711 318 B N
ATOM 5914 CA VAL B 323 4.951 10.335 502.865 1.00 78.33 B C
ANISOU 5914 CA VAL B 323 10158 13560 6043 -1809 -967 731 B C
ATOM 5915 C VAL B 323 5.857 10.749 504.029 1.00 82.46 B C
ANISOU 5915 C VAL B 323 10656 14445 6231 -1967 -1065 737 B C
ATOM 5916 O VAL B 323 5.697 10.252 505.148 1.00 91.26 B O
ANISOU 5916 O VAL B 323 11877 15835 6962 -2287 -1135 936 B O
ATOM 5917 CB VAL B 323 5.609 9.279 501.959 1.00 75.87 B C
ANISOU 5917 CB VAL B 323 9981 12835 6012 -1522 -1238 1047 B C
ATOM 5918 CG1 VAL B 323 6.405 8.296 502.769 1.00 78.94 B C
ANISOU 5918 CG1 VAL B 323 10538 13287 6169 -1618 -1551 1451 B C
ATOM 5919 CG2 VAL B 323 4.559 8.569 501.169 1.00 74.62 B C
ANISOU 5919 CG2 VAL B 323 9897 12406 6050 -1498 -1161 1125 B C
ATOM 5920 N GLN B 324 6.797 11.683 503.813 1.00 85.10 B N
ANISOU 5920 N GLN B 324 10848 14804 6681 -1771 -1063 513 B N
ATOM 5921 CA GLN B 324 7.661 12.064 504.935 1.00 91.70 B C
ANISOU 5921 CA GLN B 324 11651 16005 7185 -1934 -1158 513 B C
ATOM 5922 C GLN B 324 6.895 12.882 505.963 1.00 93.30 B C
ANISOU 5922 C GLN B 324 11750 16638 7061 -2298 -884 234 B C
ATOM 5923 O GLN B 324 7.174 12.789 507.166 1.00109.43 B O
ANISOU 5923 O GLN B 324 13832 19048 8699 -2588 -960 335 B O
ATOM 5924 CB GLN B 324 8.875 12.892 504.500 1.00102.28 B C
ANISOU 5924 CB GLN B 324 12857 17291 8716 -1658 -1209 316 B C
ATOM 5925 CG GLN B 324 9.981 12.233 503.691 1.00114.16 B C
ANISOU 5925 CG GLN B 324 14426 18456 10495 -1318 -1500 546 B C
ATOM 5926 CD GLN B 324 10.881 13.287 503.036 1.00116.90 B C
ANISOU 5926 CD GLN B 324 14606 18725 11085 -1054 -1440 234 B C
ATOM 5927 NE2 GLN B 324 12.099 12.897 502.663 1.00116.02 B N
ANISOU 5927 NE2 GLN B 324 14512 18448 11122 -815 -1699 382 B N
ATOM 5928 OE1 GLN B 324 10.485 14.447 502.903 1.00116.64 B O
ANISOU 5928 OE1 GLN B 324 14428 18786 11106 -1076 -1162 -142 B O
ATOM 5929 N ALA B 325 5.892 13.644 505.525 1.00 82.44 B N
ANISOU 5929 N ALA B 325 10242 15230 5852 -2303 -571 -112 B N
ATOM 5930 CA ALA B 325 5.078 14.367 506.493 1.00 85.34 B C
ANISOU 5930 CA ALA B 325 10496 15994 5935 -2659 -295 -398 B C
ATOM 5931 C ALA B 325 4.267 13.392 507.330 1.00 94.36 B C
ANISOU 5931 C ALA B 325 11796 17324 6733 -3025 -321 -141 B C
ATOM 5932 O ALA B 325 4.061 13.609 508.532 1.00 95.14 B O
ANISOU 5932 O ALA B 325 11875 17845 6427 -3401 -233 -211 B O
ATOM 5933 CB ALA B 325 4.158 15.362 505.785 1.00 81.07 B C
ANISOU 5933 CB ALA B 325 9768 15340 5696 -2557 30 -820 B C
ATOM 5934 N ALA B 326 3.813 12.304 506.707 1.00 90.06 B N
ANISOU 5934 N ALA B 326 11411 16474 6335 -2936 -439 154 B N
ATOM 5935 CA ALA B 326 3.132 11.248 507.444 1.00 88.21 B C
ANISOU 5935 CA ALA B 326 11360 16373 5784 -3274 -496 451 B C
ATOM 5936 C ALA B 326 4.062 10.558 508.434 1.00 99.01 B C
ANISOU 5936 C ALA B 326 12893 17941 6784 -3444 -798 828 B C
ATOM 5937 O ALA B 326 3.651 10.258 509.557 1.00112.53 B O
ANISOU 5937 O ALA B 326 14690 19997 8069 -3854 -775 932 B O
ATOM 5938 CB ALA B 326 2.547 10.225 506.477 1.00 86.68 B C
ANISOU 5938 CB ALA B 326 11300 15770 5863 -3112 -568 686 B C
ATOM 5939 N ARG B 327 5.281 10.195 508.012 1.00 96.65 B N
ANISOU 5939 N ARG B 327 12655 17417 6649 -3141 -1099 1064 B N
ATOM 5940 CA ARG B 327 6.174 9.513 508.947 1.00 99.86 B C
ANISOU 5940 CA ARG B 327 13212 18004 6726 -3285 -1416 1441 B C
ATOM 5941 C ARG B 327 6.572 10.424 510.111 1.00105.46 B C
ANISOU 5941 C ARG B 327 13803 19221 7046 -3558 -1337 1230 B C
ATOM 5942 O ARG B 327 6.777 9.947 511.242 1.00108.92 B O
ANISOU 5942 O ARG B 327 14365 19970 7049 -3878 -1494 1488 B O
ATOM 5943 CB ARG B 327 7.398 8.995 508.191 1.00 95.16 B C
ANISOU 5943 CB ARG B 327 12669 17050 6437 -2878 -1743 1688 B C
ATOM 5944 CG ARG B 327 7.003 8.022 507.082 1.00 92.66 B C
ANISOU 5944 CG ARG B 327 12474 16244 6489 -2641 -1820 1900 B C
ATOM 5945 CD ARG B 327 8.144 7.233 506.472 1.00 96.13 B C
ANISOU 5945 CD ARG B 327 12998 16331 7196 -2299 -2170 2208 B C
ATOM 5946 NE ARG B 327 8.988 6.543 507.435 1.00106.21 B N
ANISOU 5946 NE ARG B 327 14408 17762 8186 -2421 -2507 2591 B N
ATOM 5947 CZ ARG B 327 10.268 6.252 507.232 1.00106.92 B C
ANISOU 5947 CZ ARG B 327 14493 17699 8431 -2151 -2813 2764 B C
ATOM 5948 NH1 ARG B 327 10.853 6.597 506.093 1.00104.20 B N1+
ANISOU 5948 NH1 ARG B 327 14023 17051 8518 -1759 -2805 2573 B N1+
ATOM 5949 NH2 ARG B 327 10.949 5.577 508.144 1.00109.51 B N
ANISOU 5949 NH2 ARG B 327 14946 18169 8492 -2275 -3134 3137 B N
ATOM 5950 N GLU B 328 6.625 11.742 509.876 1.00108.93 B N
ANISOU 5950 N GLU B 328 14006 19760 7621 -3463 -1083 758 B N
ATOM 5951 CA GLU B 328 6.900 12.661 510.980 1.00116.45 B C
ANISOU 5951 CA GLU B 328 14829 21206 8211 -3749 -961 505 B C
ATOM 5952 C GLU B 328 5.690 12.809 511.882 1.00115.83 B C
ANISOU 5952 C GLU B 328 14740 21486 7784 -4217 -690 350 B C
ATOM 5953 O GLU B 328 5.823 12.908 513.106 1.00117.96 B O
ANISOU 5953 O GLU B 328 15019 22181 7620 -4583 -695 369 B O
ATOM 5954 CB GLU B 328 7.305 14.045 510.474 1.00120.57 B C
ANISOU 5954 CB GLU B 328 15102 21714 8996 -3521 -754 32 B C
ATOM 5955 CG GLU B 328 7.671 14.999 511.623 1.00132.06 B C
ANISOU 5955 CG GLU B 328 16413 23679 10083 -3818 -628 -244 B C
ATOM 5956 CD GLU B 328 8.288 16.307 511.151 1.00137.55 B C
ANISOU 5956 CD GLU B 328 16882 24343 11038 -3578 -469 -669 B C
ATOM 5957 OE1 GLU B 328 8.196 16.611 509.937 1.00129.21 B O
ANISOU 5957 OE1 GLU B 328 15765 22888 10442 -3220 -392 -808 B O
ATOM 5958 OE2 GLU B 328 8.864 17.027 512.000 1.00145.35 B O1-
ANISOU 5958 OE2 GLU B 328 17757 25710 11758 -3764 -421 -863 B O1-
ATOM 5959 N GLN B 329 4.500 12.815 511.284 1.00116.53 B N
ANISOU 5959 N GLN B 329 14797 21392 8088 -4206 -450 187 B N
ATOM 5960 CA GLN B 329 3.268 12.846 512.054 1.00118.01 B C
ANISOU 5960 CA GLN B 329 14973 21887 7980 -4645 -189 39 B C
ATOM 5961 C GLN B 329 3.178 11.628 512.966 1.00109.76 B C
ANISOU 5961 C GLN B 329 14187 21017 6500 -4995 -407 504 B C
ATOM 5962 O GLN B 329 2.878 11.749 514.162 1.00118.48 B O
ANISOU 5962 O GLN B 329 15249 22399 7371 -5356 -301 441 B O
ATOM 5963 CB GLN B 329 2.110 12.887 511.050 1.00126.40 B C
ANISOU 5963 CB GLN B 329 15969 22636 9422 -4490 39 -152 B C
ATOM 5964 CG GLN B 329 0.715 12.930 511.582 1.00134.64 B C
ANISOU 5964 CG GLN B 329 16968 23917 10272 -4876 336 -356 B C
ATOM 5965 CD GLN B 329 0.346 14.278 512.163 1.00137.63 B C
ANISOU 5965 CD GLN B 329 17080 24653 10560 -5076 681 -901 B C
ATOM 5966 NE2 GLN B 329 0.358 15.303 511.310 1.00129.25 B N
ANISOU 5966 NE2 GLN B 329 15804 23384 9922 -4745 846 -1269 B N
ATOM 5967 OE1 GLN B 329 0.030 14.400 513.353 1.00135.33 B O
ANISOU 5967 OE1 GLN B 329 16739 24669 10011 -5458 784 -979 B O
ATOM 5968 N LEU B 330 3.447 10.443 512.410 1.00103.42 B N
ANISOU 5968 N LEU B 330 13601 19852 5844 -4796 -702 961 B N
ATOM 5969 CA LEU B 330 3.492 9.224 513.206 1.00107.28 B C
ANISOU 5969 CA LEU B 330 14342 20388 6030 -5054 -950 1447 B C
ATOM 5970 C LEU B 330 4.478 9.370 514.359 1.00116.39 B C
ANISOU 5970 C LEU B 330 15474 21776 6972 -5179 -1117 1550 B C
ATOM 5971 O LEU B 330 4.174 9.010 515.500 1.00125.71 B O
ANISOU 5971 O LEU B 330 16716 23160 7887 -5541 -1109 1667 B O
ATOM 5972 CB LEU B 330 3.848 8.018 512.326 1.00105.97 B C
ANISOU 5972 CB LEU B 330 14395 19771 6098 -4758 -1270 1908 B C
ATOM 5973 CG LEU B 330 3.532 6.589 512.810 1.00109.35 B C
ANISOU 5973 CG LEU B 330 15103 20082 6364 -4971 -1474 2404 B C
ATOM 5974 CD1 LEU B 330 3.653 5.592 511.683 1.00107.19 B C
ANISOU 5974 CD1 LEU B 330 14988 19307 6431 -4641 -1689 2730 B C
ATOM 5975 CD2 LEU B 330 4.407 6.126 513.964 1.00120.57 B C
ANISOU 5975 CD2 LEU B 330 16613 21616 7581 -5100 -1742 2707 B C
ATOM 5976 N SER B 331 5.679 9.891 514.073 1.00109.12 B N
ANISOU 5976 N SER B 331 14460 20835 6163 -4889 -1274 1503 B N
ATOM 5977 CA SER B 331 6.672 10.047 515.135 1.00114.16 B C
ANISOU 5977 CA SER B 331 15066 21700 6608 -4991 -1436 1594 B C
ATOM 5978 C SER B 331 6.237 11.029 516.233 1.00124.72 B C
ANISOU 5978 C SER B 331 16211 23455 7721 -5362 -1123 1206 B C
ATOM 5979 O SER B 331 6.538 10.810 517.414 1.00124.90 B O
ANISOU 5979 O SER B 331 16269 23708 7479 -5636 -1217 1357 B O
ATOM 5980 CB SER B 331 8.006 10.469 514.514 1.00114.41 B C
ANISOU 5980 CB SER B 331 15012 21619 6838 -4593 -1639 1570 B C
ATOM 5981 OG SER B 331 8.967 10.781 515.506 1.00122.49 B O
ANISOU 5981 OG SER B 331 15967 22888 7683 -4685 -1757 1589 B O
ATOM 5982 N THR B 332 5.556 12.126 515.871 1.00123.62 B N
ANISOU 5982 N THR B 332 15857 23408 7705 -5372 -756 701 B N
ATOM 5983 CA THR B 332 5.063 13.073 516.881 1.00121.20 B C
ANISOU 5983 CA THR B 332 15342 23461 7247 -5721 -443 306 B C
ATOM 5984 C THR B 332 3.949 12.482 517.737 1.00121.81 B C
ANISOU 5984 C THR B 332 15501 23687 7095 -6158 -329 390 B C
ATOM 5985 O THR B 332 3.878 12.758 518.940 1.00133.80 B O
ANISOU 5985 O THR B 332 16939 25523 8374 -6516 -245 299 B O
ATOM 5986 CB THR B 332 4.617 14.394 516.250 1.00118.95 B C
ANISOU 5986 CB THR B 332 14792 23182 7222 -5589 -86 -262 B C
ATOM 5987 CG2 THR B 332 4.484 15.493 517.320 1.00114.11 B C
ANISOU 5987 CG2 THR B 332 13930 22918 6508 -5889 182 -667 B C
ATOM 5988 OG1 THR B 332 5.584 14.810 515.275 1.00123.56 B O
ANISOU 5988 OG1 THR B 332 15334 23574 8041 -5163 -206 -313 B O
ATOM 5989 N THR B 333 3.057 11.690 517.141 1.00117.31 B N
ANISOU 5989 N THR B 333 15079 22899 6595 -6151 -314 545 B N
ATOM 5990 CA THR B 333 1.978 11.095 517.929 1.00123.90 B C
ANISOU 5990 CA THR B 333 15994 23865 7218 -6574 -205 616 B C
ATOM 5991 C THR B 333 2.496 10.065 518.923 1.00135.97 B C
ANISOU 5991 C THR B 333 17742 25468 8453 -6796 -512 1098 B C
ATOM 5992 O THR B 333 2.046 10.033 520.075 1.00147.57 B O
ANISOU 5992 O THR B 333 19191 27221 9660 -7222 -418 1057 B O
ATOM 5993 CB THR B 333 0.934 10.452 517.018 1.00125.03 B C
ANISOU 5993 CB THR B 333 16249 23743 7515 -6505 -123 676 B C
ATOM 5994 CG2 THR B 333 -0.189 9.832 517.841 1.00122.46 B C
ANISOU 5994 CG2 THR B 333 16002 23555 6974 -6955 -6 730 B C
ATOM 5995 OG1 THR B 333 0.388 11.443 516.142 1.00130.72 B O
ANISOU 5995 OG1 THR B 333 16750 24407 8511 -6314 175 207 B O
ATOM 5996 N ALA B 334 3.424 9.206 518.503 1.00124.83 B N
ANISOU 5996 N ALA B 334 16535 23797 7099 -6517 -883 1551 B N
ATOM 5997 CA ALA B 334 3.932 8.175 519.404 1.00134.35 B C
ANISOU 5997 CA ALA B 334 17953 25026 8068 -6692 -1195 2027 B C
ATOM 5998 C ALA B 334 4.598 8.759 520.653 1.00137.68 B C
ANISOU 5998 C ALA B 334 18255 25828 8229 -6934 -1212 1939 B C
ATOM 5999 O ALA B 334 4.497 8.171 521.738 1.00137.78 B O
ANISOU 5999 O ALA B 334 18380 26012 7958 -7284 -1309 2169 B O
ATOM 6000 CB ALA B 334 4.913 7.284 518.646 1.00127.88 B C
ANISOU 6000 CB ALA B 334 17325 23826 7437 -6283 -1590 2476 B C
ATOM 6001 N ASP B 335 5.264 9.912 520.527 1.00142.71 B N
ANISOU 6001 N ASP B 335 18664 26603 8955 -6770 -1112 1602 B N
ATOM 6002 CA ASP B 335 5.923 10.536 521.676 1.00148.95 B C
ANISOU 6002 CA ASP B 335 19320 27760 9513 -6995 -1110 1490 B C
ATOM 6003 C ASP B 335 4.915 11.127 522.661 1.00153.65 B C
ANISOU 6003 C ASP B 335 19759 28717 9902 -7487 -769 1143 B C
ATOM 6004 O ASP B 335 5.150 11.119 523.877 1.00152.27 B O
ANISOU 6004 O ASP B 335 19571 28850 9434 -7830 -814 1208 B O
ATOM 6005 CB ASP B 335 6.909 11.607 521.192 1.00149.03 B C
ANISOU 6005 CB ASP B 335 19127 27789 9709 -6668 -1085 1210 B C
ATOM 6006 CG ASP B 335 8.145 11.016 520.503 1.00149.97 B C
ANISOU 6006 CG ASP B 335 19381 27619 9983 -6233 -1476 1571 B C
ATOM 6007 OD1 ASP B 335 8.499 9.855 520.801 1.00154.01 B O
ANISOU 6007 OD1 ASP B 335 20119 28003 10394 -6240 -1803 2058 B O
ATOM 6008 OD2 ASP B 335 8.739 11.700 519.636 1.00143.21 B O1-
ANISOU 6008 OD2 ASP B 335 18398 26642 9374 -5878 -1457 1359 B O1-
ATOM 6009 N ASP B 336 3.791 11.657 522.159 1.00155.45 B N
ANISOU 6009 N ASP B 336 19856 28917 10292 -7529 -431 760 B N
ATOM 6010 CA ASP B 336 2.785 12.243 523.046 1.00156.29 B C
ANISOU 6010 CA ASP B 336 19786 29344 10253 -7983 -103 389 B C
ATOM 6011 C ASP B 336 1.986 11.166 523.771 1.00154.42 B C
ANISOU 6011 C ASP B 336 19748 29169 9754 -8380 -163 674 B C
ATOM 6012 O ASP B 336 1.622 11.338 524.940 1.00156.92 B O
ANISOU 6012 O ASP B 336 19990 29821 9810 -8833 -52 558 B O
ATOM 6013 CB ASP B 336 1.838 13.161 522.262 1.00154.93 B C
ANISOU 6013 CB ASP B 336 19391 29096 10380 -7877 265 -127 B C
ATOM 6014 CG ASP B 336 2.349 14.597 522.157 1.00152.52 B C
ANISOU 6014 CG ASP B 336 18788 28906 10255 -7724 455 -585 B C
ATOM 6015 OD1 ASP B 336 2.336 15.317 523.183 1.00144.74 B O
ANISOU 6015 OD1 ASP B 336 17614 28253 9129 -8042 610 -852 B O
ATOM 6016 OD2 ASP B 336 2.744 15.009 521.041 1.00153.49 B O1-
ANISOU 6016 OD2 ASP B 336 18867 28782 10672 -7294 455 -688 B O1-
ATOM 6017 N LYS B 337 1.695 10.057 523.098 1.00150.64 B N
ANISOU 6017 N LYS B 337 19520 28370 9346 -8232 -332 1035 B N
ATOM 6018 CA LYS B 337 0.903 8.989 523.694 1.00151.09 B C
ANISOU 6018 CA LYS B 337 19781 28442 9182 -8592 -386 1308 B C
ATOM 6019 C LYS B 337 1.706 7.699 523.809 1.00151.27 B C
ANISOU 6019 C LYS B 337 20116 28262 9098 -8490 -816 1937 B C
ATOM 6020 O LYS B 337 1.138 6.606 523.809 1.00151.33 B O
ANISOU 6020 O LYS B 337 20351 28101 9045 -8614 -917 2246 B O
ATOM 6021 CB LYS B 337 -0.359 8.744 522.871 1.00149.28 B C
ANISOU 6021 CB LYS B 337 19572 28009 9141 -8567 -175 1159 B C
ATOM 6022 CG LYS B 337 -1.076 10.017 522.465 1.00148.39 B C
ANISOU 6022 CG LYS B 337 19144 27996 9242 -8535 218 542 B C
ATOM 6023 CD LYS B 337 -2.197 9.720 521.483 1.00146.86 B C
ANISOU 6023 CD LYS B 337 18978 27553 9271 -8428 385 435 B C
ATOM 6024 CE LYS B 337 -2.978 10.978 521.137 1.00140.28 B C
ANISOU 6024 CE LYS B 337 17818 26810 8673 -8403 772 -189 B C
ATOM 6025 NZ LYS B 337 -4.244 10.670 520.412 1.00134.72 B N1+
ANISOU 6025 NZ LYS B 337 17119 25928 8141 -8396 959 -326 B N1+
ATOM 6026 N SER B 340 -0.240 1.328 520.476 1.00144.01 B N
ANISOU 6026 N SER B 340 20524 25367 8827 -7892 -1610 3839 B N
ATOM 6027 CA SER B 340 0.107 1.544 519.070 1.00141.79 B C
ANISOU 6027 CA SER B 340 20191 24768 8916 -7396 -1634 3788 B C
ATOM 6028 C SER B 340 -1.148 1.619 518.195 1.00139.07 B C
ANISOU 6028 C SER B 340 19801 24310 8729 -7407 -1331 3527 B C
ATOM 6029 O SER B 340 -1.189 2.330 517.175 1.00130.56 B O
ANISOU 6029 O SER B 340 18569 23146 7889 -7115 -1186 3255 B O
ATOM 6030 CB SER B 340 1.033 0.431 518.571 1.00139.63 B C
ANISOU 6030 CB SER B 340 20142 24062 8850 -7051 -2038 4305 B C
ATOM 6031 OG SER B 340 0.340 -0.796 518.445 1.00140.28 B O
ANISOU 6031 OG SER B 340 20458 23873 8967 -7165 -2097 4600 B O
ATOM 6032 N HIS B 341 -2.180 0.872 518.594 1.00144.69 B N
ANISOU 6032 N HIS B 341 20646 25023 9305 -7750 -1236 3607 B N
ATOM 6033 CA HIS B 341 -3.480 1.043 517.957 1.00142.04 B C
ANISOU 6033 CA HIS B 341 20232 24663 9075 -7835 -906 3294 B C
ATOM 6034 C HIS B 341 -4.008 2.458 518.168 1.00140.57 B C
ANISOU 6034 C HIS B 341 19727 24851 8832 -7973 -544 2703 B C
ATOM 6035 O HIS B 341 -4.724 2.989 517.306 1.00130.89 B O
ANISOU 6035 O HIS B 341 18350 23575 7807 -7849 -285 2366 B O
ATOM 6036 CB HIS B 341 -4.469 0.003 518.489 1.00140.76 B C
ANISOU 6036 CB HIS B 341 20261 24473 8748 -8218 -871 3465 B C
ATOM 6037 CG HIS B 341 -3.931 -1.399 518.507 1.00144.17 B C
ANISOU 6037 CG HIS B 341 21004 24559 9214 -8131 -1231 4044 B C
ATOM 6038 CD2 HIS B 341 -3.340 -2.114 519.493 1.00149.46 B C
ANISOU 6038 CD2 HIS B 341 21855 25258 9676 -8302 -1505 4419 B C
ATOM 6039 ND1 HIS B 341 -3.990 -2.237 517.413 1.00145.52 B N
ANISOU 6039 ND1 HIS B 341 21327 24281 9684 -7837 -1338 4285 B N
ATOM 6040 CE1 HIS B 341 -3.454 -3.404 517.723 1.00147.92 B C
ANISOU 6040 CE1 HIS B 341 21883 24336 9983 -7817 -1658 4770 B C
ATOM 6041 NE2 HIS B 341 -3.052 -3.357 518.980 1.00149.33 B N
ANISOU 6041 NE2 HIS B 341 22088 24799 9853 -8093 -1769 4867 B N
ATOM 6042 N GLU B 342 -3.652 3.085 519.301 1.00142.80 B N
ANISOU 6042 N GLU B 342 19894 25500 8865 -8223 -523 2565 B N
ATOM 6043 CA GLU B 342 -3.931 4.505 519.489 1.00140.04 B C
ANISOU 6043 CA GLU B 342 19219 25473 8516 -8297 -209 2002 B C
ATOM 6044 C GLU B 342 -3.344 5.317 518.346 1.00150.42 B C
ANISOU 6044 C GLU B 342 20382 26634 10136 -7816 -181 1815 B C
ATOM 6045 O GLU B 342 -3.972 6.256 517.841 1.00150.46 B O
ANISOU 6045 O GLU B 342 20151 26712 10305 -7751 124 1349 B O
ATOM 6046 CB GLU B 342 -3.289 4.988 520.792 1.00140.04 B C
ANISOU 6046 CB GLU B 342 19140 25836 8234 -8560 -269 1967 B C
ATOM 6047 CG GLU B 342 -3.971 4.633 522.089 1.00148.22 B C
ANISOU 6047 CG GLU B 342 20224 27159 8933 -9115 -200 1970 B C
ATOM 6048 CD GLU B 342 -3.105 5.018 523.276 1.00151.55 B C
ANISOU 6048 CD GLU B 342 20593 27900 9088 -9318 -322 2017 B C
ATOM 6049 OE1 GLU B 342 -1.921 5.357 523.057 1.00147.61 B O
ANISOU 6049 OE1 GLU B 342 20066 27351 8670 -9002 -507 2127 B O
ATOM 6050 OE2 GLU B 342 -3.603 4.979 524.420 1.00161.48 B O1-
ANISOU 6050 OE2 GLU B 342 21836 29464 10055 -9800 -235 1940 B O1-
ATOM 6051 N ILE B 343 -2.121 4.968 517.943 1.00152.55 B N
ANISOU 6051 N ILE B 343 20779 26686 10497 -7473 -507 2168 B N
ATOM 6052 CA ILE B 343 -1.426 5.654 516.859 1.00135.03 B C
ANISOU 6052 CA ILE B 343 18442 24309 8556 -7011 -529 2035 B C
ATOM 6053 C ILE B 343 -2.164 5.445 515.541 1.00132.56 B C
ANISOU 6053 C ILE B 343 18146 23701 8518 -6786 -404 1965 B C
ATOM 6054 O ILE B 343 -2.313 6.369 514.729 1.00129.35 B O
ANISOU 6054 O ILE B 343 17542 23288 8317 -6561 -204 1599 B O
ATOM 6055 CB ILE B 343 0.027 5.152 516.793 1.00131.13 B C
ANISOU 6055 CB ILE B 343 18095 23630 8098 -6724 -941 2464 B C
ATOM 6056 CG1 ILE B 343 0.800 5.660 518.011 1.00132.11 B C
ANISOU 6056 CG1 ILE B 343 18134 24093 7971 -6912 -1016 2429 B C
ATOM 6057 CG2 ILE B 343 0.715 5.642 515.515 1.00129.19 B C
ANISOU 6057 CG2 ILE B 343 17767 23153 8166 -6229 -1004 2380 B C
ATOM 6058 CD1 ILE B 343 2.098 4.951 518.214 1.00131.70 B C
ANISOU 6058 CD1 ILE B 343 18248 23885 7906 -6719 -1436 2894 B C
ATOM 6059 N VAL B 344 -2.619 4.210 515.307 1.00135.31 B N
ANISOU 6059 N VAL B 344 18735 23794 8885 -6842 -523 2320 B N
ATOM 6060 CA VAL B 344 -3.388 3.863 514.108 1.00125.94 B C
ANISOU 6060 CA VAL B 344 17586 22324 7943 -6673 -408 2292 B C
ATOM 6061 C VAL B 344 -4.688 4.668 513.983 1.00121.55 B C
ANISOU 6061 C VAL B 344 16798 21970 7416 -6853 21 1762 B C
ATOM 6062 O VAL B 344 -5.004 5.192 512.909 1.00113.38 B O
ANISOU 6062 O VAL B 344 15632 20821 6628 -6601 187 1512 B O
ATOM 6063 CB VAL B 344 -3.670 2.344 514.120 1.00127.20 B C
ANISOU 6063 CB VAL B 344 18045 22198 8086 -6774 -605 2766 B C
ATOM 6064 CG1 VAL B 344 -4.605 1.949 513.007 1.00117.92 B C
ANISOU 6064 CG1 VAL B 344 16903 20764 7137 -6675 -450 2718 B C
ATOM 6065 CG2 VAL B 344 -2.373 1.547 514.047 1.00127.45 B C
ANISOU 6065 CG2 VAL B 344 18278 21951 8196 -6511 -1035 3269 B C
ATOM 6066 N ILE B 345 -5.427 4.825 515.087 1.00131.94 B N
ANISOU 6066 N ILE B 345 18040 23592 8498 -7283 203 1564 B N
ATOM 6067 CA ILE B 345 -6.699 5.567 515.113 1.00128.40 B C
ANISOU 6067 CA ILE B 345 17347 23340 8097 -7480 600 1040 B C
ATOM 6068 C ILE B 345 -6.595 7.069 514.817 1.00122.55 B C
ANISOU 6068 C ILE B 345 16278 22756 7529 -7295 831 522 B C
ATOM 6069 O ILE B 345 -7.504 7.645 514.205 1.00117.96 B O
ANISOU 6069 O ILE B 345 15497 22162 7159 -7233 1116 126 B O
ATOM 6070 CB ILE B 345 -7.394 5.313 516.463 1.00134.29 B C
ANISOU 6070 CB ILE B 345 18106 24375 8542 -8002 690 983 B C
ATOM 6071 CG1 ILE B 345 -8.107 3.960 516.434 1.00139.21 B C
ANISOU 6071 CG1 ILE B 345 18987 24812 9095 -8191 617 1309 B C
ATOM 6072 CG2 ILE B 345 -8.400 6.402 516.772 1.00132.47 B C
ANISOU 6072 CG2 ILE B 345 17552 24423 8356 -8203 1070 371 B C
ATOM 6073 CD1 ILE B 345 -8.523 3.457 517.808 1.00142.83 B C
ANISOU 6073 CD1 ILE B 345 19541 25516 9212 -8699 604 1393 B C
ATOM 6074 N GLU B 346 -5.499 7.721 515.187 1.00125.05 B N
ANISOU 6074 N GLU B 346 16525 23196 7792 -7180 712 507 B N
ATOM 6075 CA GLU B 346 -5.409 9.174 515.031 1.00121.31 B C
ANISOU 6075 CA GLU B 346 15733 22873 7485 -7038 941 -4 B C
ATOM 6076 C GLU B 346 -5.223 9.616 513.590 1.00119.98 B C
ANISOU 6076 C GLU B 346 15489 22447 7652 -6576 984 -131 B C
ATOM 6077 O GLU B 346 -5.682 10.702 513.214 1.00108.83 B O
ANISOU 6077 O GLU B 346 13801 21083 6465 -6466 1257 -615 B O
ATOM 6078 CB GLU B 346 -4.253 9.727 515.860 1.00122.42 B C
ANISOU 6078 CB GLU B 346 15825 23221 7469 -7060 802 19 B C
ATOM 6079 CG GLU B 346 -4.614 10.013 517.297 1.00140.97 B C
ANISOU 6079 CG GLU B 346 18072 25932 9557 -7525 921 -155 B C
ATOM 6080 CD GLU B 346 -5.578 11.176 517.436 1.00143.48 B C
ANISOU 6080 CD GLU B 346 18058 26429 10030 -7651 1303 -773 B C
ATOM 6081 OE1 GLU B 346 -5.722 11.951 516.461 1.00140.11 B O
ANISOU 6081 OE1 GLU B 346 17454 25855 9929 -7326 1459 -1081 B O
ATOM 6082 OE2 GLU B 346 -6.186 11.310 518.524 1.00143.03 B O1-
ANISOU 6082 OE2 GLU B 346 17913 26648 9785 -8073 1435 -952 B O1-
ATOM 6083 N HIS B 347 -4.527 8.825 512.788 1.00117.51 B N
ANISOU 6083 N HIS B 347 15403 21850 7397 -6298 707 288 B N
ATOM 6084 CA HIS B 347 -4.040 9.268 511.499 1.00108.09 B C
ANISOU 6084 CA HIS B 347 14115 20326 6629 -5786 660 200 B C
ATOM 6085 C HIS B 347 -4.632 8.517 510.320 1.00105.27 B C
ANISOU 6085 C HIS B 347 13830 19517 6651 -5526 627 340 B C
ATOM 6086 O HIS B 347 -4.271 8.820 509.180 1.00106.94 B O
ANISOU 6086 O HIS B 347 13951 19370 7310 -5067 570 273 B O
ATOM 6087 CB HIS B 347 -2.521 9.131 511.487 1.00110.76 B C
ANISOU 6087 CB HIS B 347 14563 20554 6966 -5534 313 511 B C
ATOM 6088 CG HIS B 347 -1.873 9.949 512.550 1.00118.21 B C
ANISOU 6088 CG HIS B 347 15411 21935 7569 -5752 343 346 B C
ATOM 6089 CD2 HIS B 347 -1.240 9.576 513.686 1.00121.71 B C
ANISOU 6089 CD2 HIS B 347 15956 22547 7740 -5973 147 603 B C
ATOM 6090 ND1 HIS B 347 -1.875 11.325 512.544 1.00119.42 B N
ANISOU 6090 ND1 HIS B 347 15276 22252 7847 -5681 595 -164 B N
ATOM 6091 CE1 HIS B 347 -1.273 11.766 513.634 1.00119.05 B C
ANISOU 6091 CE1 HIS B 347 15157 22463 7615 -5862 558 -214 B C
ATOM 6092 NE2 HIS B 347 -0.860 10.725 514.333 1.00124.35 B N
ANISOU 6092 NE2 HIS B 347 16061 23153 8032 -6038 284 248 B N
ATOM 6093 N ALA B 348 -5.557 7.581 510.547 1.00106.67 B N
ANISOU 6093 N ALA B 348 14160 19711 6660 -5822 677 509 B N
ATOM 6094 CA ALA B 348 -5.959 6.672 509.479 1.00107.32 B C
ANISOU 6094 CA ALA B 348 14357 19354 7065 -5590 590 724 B C
ATOM 6095 C ALA B 348 -6.746 7.368 508.374 1.00100.41 B C
ANISOU 6095 C ALA B 348 13228 18278 6643 -5308 826 317 B C
ATOM 6096 O ALA B 348 -6.693 6.922 507.223 1.00 95.91 B O
ANISOU 6096 O ALA B 348 12699 17293 6448 -4959 715 449 B O
ATOM 6097 CB ALA B 348 -6.789 5.530 510.066 1.00110.89 B C
ANISOU 6097 CB ALA B 348 15035 19899 7200 -6016 607 986 B C
ATOM 6098 N ALA B 349 -7.468 8.448 508.673 1.00104.22 B N
ANISOU 6098 N ALA B 349 13445 19039 7116 -5446 1143 -176 B N
ATOM 6099 CA ALA B 349 -8.107 9.183 507.585 1.00105.06 B C
ANISOU 6099 CA ALA B 349 13300 18933 7685 -5132 1329 -547 B C
ATOM 6100 C ALA B 349 -7.059 9.775 506.652 1.00112.46 B C
ANISOU 6100 C ALA B 349 14168 19568 8996 -4625 1169 -553 B C
ATOM 6101 O ALA B 349 -7.228 9.770 505.426 1.00120.25 B O
ANISOU 6101 O ALA B 349 15097 20195 10396 -4270 1145 -582 B O
ATOM 6102 CB ALA B 349 -9.012 10.286 508.132 1.00109.43 B C
ANISOU 6102 CB ALA B 349 13563 19834 8180 -5364 1688 -1088 B C
ATOM 6103 N ASP B 350 -5.969 10.295 507.221 1.00113.18 B N
ANISOU 6103 N ASP B 350 14257 19814 8932 -4604 1062 -533 B N
ATOM 6104 CA ASP B 350 -4.827 10.725 506.421 1.00102.03 B C
ANISOU 6104 CA ASP B 350 12817 18126 7825 -4156 880 -487 B C
ATOM 6105 C ASP B 350 -4.184 9.558 505.674 1.00 94.16 B C
ANISOU 6105 C ASP B 350 12060 16741 6978 -3909 564 -20 B C
ATOM 6106 O ASP B 350 -3.810 9.698 504.503 1.00 92.31 B O
ANISOU 6106 O ASP B 350 11782 16152 7142 -3503 482 -26 B O
ATOM 6107 CB ASP B 350 -3.819 11.416 507.335 1.00117.70 B C
ANISOU 6107 CB ASP B 350 14762 20404 9552 -4249 831 -550 B C
ATOM 6108 CG ASP B 350 -4.318 12.769 507.834 1.00127.06 B C
ANISOU 6108 CG ASP B 350 15666 21903 10707 -4396 1155 -1080 B C
ATOM 6109 OD1 ASP B 350 -5.200 12.775 508.730 1.00128.31 B O
ANISOU 6109 OD1 ASP B 350 15780 22400 10571 -4812 1362 -1239 B O
ATOM 6110 OD2 ASP B 350 -3.826 13.815 507.347 1.00123.97 B O1-
ANISOU 6110 OD2 ASP B 350 15099 21418 10587 -4111 1207 -1343 B O1-
ATOM 6111 N TRP B 351 -3.988 8.415 506.351 1.00 94.31 B N
ANISOU 6111 N TRP B 351 12332 16819 6682 -4153 378 390 B N
ATOM 6112 CA TRP B 351 -3.369 7.263 505.692 1.00 93.15 B C
ANISOU 6112 CA TRP B 351 12409 16290 6693 -3927 76 833 B C
ATOM 6113 C TRP B 351 -4.198 6.723 504.536 1.00102.05 B C
ANISOU 6113 C TRP B 351 13542 17067 8163 -3754 137 837 B C
ATOM 6114 O TRP B 351 -3.632 6.210 503.564 1.00108.39 B O
ANISOU 6114 O TRP B 351 14425 17489 9270 -3422 -55 1037 B O
ATOM 6115 CB TRP B 351 -3.044 6.118 506.657 1.00 92.98 B C
ANISOU 6115 CB TRP B 351 12666 16378 6283 -4228 -145 1289 B C
ATOM 6116 CG TRP B 351 -2.058 6.450 507.740 1.00 95.31 B C
ANISOU 6116 CG TRP B 351 12992 16985 6234 -4374 -283 1379 B C
ATOM 6117 CD1 TRP B 351 -1.280 7.571 507.834 1.00 94.08 B C
ANISOU 6117 CD1 TRP B 351 12656 16970 6121 -4217 -260 1123 B C
ATOM 6118 CD2 TRP B 351 -1.594 5.563 508.756 1.00 99.14 B C
ANISOU 6118 CD2 TRP B 351 13721 17625 6323 -4656 -519 1801 B C
ATOM 6119 CE2 TRP B 351 -0.611 6.248 509.492 1.00101.65 B C
ANISOU 6119 CE2 TRP B 351 13974 18221 6427 -4684 -612 1753 B C
ATOM 6120 CE3 TRP B 351 -1.953 4.274 509.149 1.00102.01 B C
ANISOU 6120 CE3 TRP B 351 14354 17930 6478 -4909 -653 2211 B C
ATOM 6121 NE1 TRP B 351 -0.445 7.480 508.916 1.00 97.04 B N
ANISOU 6121 NE1 TRP B 351 13127 17627 6119 -4419 -439 1323 B N
ATOM 6122 CZ2 TRP B 351 0.018 5.684 510.597 1.00108.19 B C
ANISOU 6122 CZ2 TRP B 351 14991 19283 6836 -4952 -849 2110 B C
ATOM 6123 CZ3 TRP B 351 -1.330 3.716 510.240 1.00105.89 B C
ANISOU 6123 CZ3 TRP B 351 15043 18629 6560 -5173 -889 2577 B C
ATOM 6124 CH2 TRP B 351 -0.354 4.418 510.953 1.00114.65 B C
ANISOU 6124 CH2 TRP B 351 16078 20028 7457 -5191 -993 2529 B C
ATOM 6125 N CYS B 352 -5.527 6.809 504.612 1.00103.41 B N
ANISOU 6125 N CYS B 352 13625 17369 8295 -3980 401 609 B N
ATOM 6126 CA CYS B 352 -6.337 6.312 503.505 1.00 95.23 B C
ANISOU 6126 CA CYS B 352 12581 16022 7579 -3823 459 599 B C
ATOM 6127 C CYS B 352 -6.058 7.117 502.249 1.00 95.14 B C
ANISOU 6127 C CYS B 352 12384 15742 8024 -3371 475 369 B C
ATOM 6128 O CYS B 352 -6.025 6.565 501.142 1.00100.29 B O
ANISOU 6128 O CYS B 352 13090 16032 8983 -3108 373 502 B O
ATOM 6129 CB CYS B 352 -7.815 6.322 503.874 1.00 97.74 B C
ANISOU 6129 CB CYS B 352 12810 16563 7761 -4161 746 364 B C
ATOM 6130 SG CYS B 352 -8.233 4.904 504.918 1.00101.70 B S
ANISOU 6130 SG CYS B 352 13615 17214 7811 -4653 681 756 B S
ATOM 6131 N LYS B 353 -5.830 8.420 502.404 1.00 89.75 B N
ANISOU 6131 N LYS B 353 11487 15230 7385 -3288 602 26 B N
ATOM 6132 CA LYS B 353 -5.409 9.224 501.268 1.00 86.60 B C
ANISOU 6132 CA LYS B 353 10936 14576 7393 -2866 592 -161 B C
ATOM 6133 C LYS B 353 -4.002 8.823 500.849 1.00 86.64 B C
ANISOU 6133 C LYS B 353 11085 14332 7500 -2591 297 137 B C
ATOM 6134 O LYS B 353 -3.740 8.593 499.661 1.00 83.85 B O
ANISOU 6134 O LYS B 353 10747 13628 7485 -2272 196 207 B O
ATOM 6135 CB LYS B 353 -5.472 10.717 501.595 1.00 85.84 B C
ANISOU 6135 CB LYS B 353 10584 14712 7318 -2859 799 -594 B C
ATOM 6136 CG LYS B 353 -6.855 11.239 501.924 1.00 91.25 B C
ANISOU 6136 CG LYS B 353 11078 15624 7970 -3090 1104 -950 B C
ATOM 6137 CD LYS B 353 -6.813 12.727 502.241 1.00 96.74 B C
ANISOU 6137 CD LYS B 353 11518 16515 8722 -3061 1297 -1379 B C
ATOM 6138 CE LYS B 353 -8.157 13.220 502.730 1.00100.11 B C
ANISOU 6138 CE LYS B 353 11740 17200 9096 -3326 1602 -1749 B C
ATOM 6139 NZ LYS B 353 -9.216 13.085 501.668 1.00 93.04 B N1+
ANISOU 6139 NZ LYS B 353 10746 16069 8536 -3165 1683 -1852 B N1+
ATOM 6140 N LEU B 354 -3.075 8.764 501.814 1.00 86.40 B N
ANISOU 6140 N LEU B 354 11150 14495 7183 -2716 157 298 B N
ATOM 6141 CA LEU B 354 -1.704 8.354 501.516 1.00 81.23 B C
ANISOU 6141 CA LEU B 354 10620 13629 6616 -2469 -135 578 B C
ATOM 6142 C LEU B 354 -1.632 7.069 500.696 1.00 80.77 B C
ANISOU 6142 C LEU B 354 10745 13192 6754 -2320 -327 920 B C
ATOM 6143 O LEU B 354 -0.789 6.952 499.798 1.00 84.77 B O
ANISOU 6143 O LEU B 354 11267 13398 7545 -1988 -489 1004 B O
ATOM 6144 CB LEU B 354 -0.909 8.181 502.806 1.00 81.33 B C
ANISOU 6144 CB LEU B 354 10740 13927 6234 -2697 -282 773 B C
ATOM 6145 CG LEU B 354 0.579 8.265 502.489 1.00 80.65 B C
ANISOU 6145 CG LEU B 354 10679 13680 6283 -2395 -533 906 B C
ATOM 6146 CD1 LEU B 354 0.895 9.606 501.843 1.00 76.33 B C
ANISOU 6146 CD1 LEU B 354 9906 13100 5995 -2132 -395 520 B C
ATOM 6147 CD2 LEU B 354 1.413 8.036 503.724 1.00 86.88 B C
ANISOU 6147 CD2 LEU B 354 11574 14745 6693 -2602 -715 1126 B C
ATOM 6148 N PHE B 355 -2.509 6.102 500.963 1.00 78.31 B N
ANISOU 6148 N PHE B 355 10568 12883 6304 -2568 -298 1100 B N
ATOM 6149 CA PHE B 355 -2.391 4.807 500.307 1.00 80.33 B C
ANISOU 6149 CA PHE B 355 11014 12785 6723 -2459 -486 1442 B C
ATOM 6150 C PHE B 355 -3.487 4.566 499.295 1.00 81.12 B C
ANISOU 6150 C PHE B 355 11059 12681 7081 -2395 -328 1317 B C
ATOM 6151 O PHE B 355 -3.479 3.516 498.641 1.00 80.46 B O
ANISOU 6151 O PHE B 355 11116 12289 7166 -2303 -453 1561 B O
ATOM 6152 CB PHE B 355 -2.470 3.652 501.307 1.00 89.19 B C
ANISOU 6152 CB PHE B 355 12380 14000 7510 -2785 -618 1821 B C
ATOM 6153 CG PHE B 355 -1.410 3.651 502.351 1.00 98.00 B C
ANISOU 6153 CG PHE B 355 13586 15310 8340 -2880 -821 2025 B C
ATOM 6154 CD1 PHE B 355 -0.076 3.751 502.011 1.00100.92 B C
ANISOU 6154 CD1 PHE B 355 13953 15511 8881 -2569 -1053 2129 B C
ATOM 6155 CD2 PHE B 355 -1.747 3.454 503.681 1.00 98.32 B C
ANISOU 6155 CD2 PHE B 355 13727 15703 7928 -3299 -793 2136 B C
ATOM 6156 CE1 PHE B 355 0.899 3.721 502.990 1.00 96.70 B C
ANISOU 6156 CE1 PHE B 355 13494 15169 8078 -2659 -1257 2324 B C
ATOM 6157 CE2 PHE B 355 -0.777 3.413 504.654 1.00 97.64 B C
ANISOU 6157 CE2 PHE B 355 13730 15811 7557 -3401 -1000 2347 B C
ATOM 6158 CZ PHE B 355 0.548 3.545 504.308 1.00 92.39 B C
ANISOU 6158 CZ PHE B 355 13048 14981 7076 -3072 -1238 2444 B C
ATOM 6159 N ARG B 356 -4.384 5.529 499.105 1.00 90.61 B N
ANISOU 6159 N ARG B 356 12050 14033 8344 -2422 -67 936 B N
ATOM 6160 CA ARG B 356 -5.495 5.406 498.167 1.00 88.36 B C
ANISOU 6160 CA ARG B 356 11681 13594 8297 -2368 88 786 B C
ATOM 6161 C ARG B 356 -6.173 4.049 498.357 1.00 90.80 B C
ANISOU 6161 C ARG B 356 12185 13832 8481 -2611 62 1059 B C
ATOM 6162 O ARG B 356 -6.278 3.237 497.435 1.00 90.15 B O
ANISOU 6162 O ARG B 356 12186 13435 8631 -2469 -16 1208 B O
ATOM 6163 CB ARG B 356 -4.999 5.598 496.735 1.00 82.55 B C
ANISOU 6163 CB ARG B 356 10882 12506 7977 -1956 4 740 B C
ATOM 6164 CG ARG B 356 -4.428 6.984 496.468 1.00 87.83 B C
ANISOU 6164 CG ARG B 356 11358 13229 8786 -1726 53 452 B C
ATOM 6165 CD ARG B 356 -4.119 7.179 494.999 1.00104.49 B C
ANISOU 6165 CD ARG B 356 13406 15004 11292 -1361 -2 390 B C
ATOM 6166 NE ARG B 356 -4.668 8.419 494.457 1.00114.05 B N
ANISOU 6166 NE ARG B 356 14387 16259 12686 -1235 182 24 B N
ATOM 6167 CZ ARG B 356 -5.776 8.495 493.724 1.00113.42 B C
ANISOU 6167 CZ ARG B 356 14203 16110 12783 -1212 317 -130 B C
ATOM 6168 NH1 ARG B 356 -6.453 7.393 493.419 1.00107.79 B N1+
ANISOU 6168 NH1 ARG B 356 13592 15285 12079 -1314 303 37 B N1+
ATOM 6169 NH2 ARG B 356 -6.185 9.675 493.268 1.00114.66 B N
ANISOU 6169 NH2 ARG B 356 14150 16297 13119 -1080 457 -448 B N
ATOM 6170 N CYS B 357 -6.582 3.790 499.602 1.00 93.36 B N
ANISOU 6170 N CYS B 357 12595 14459 8420 -2999 125 1130 B N
ATOM 6171 CA CYS B 357 -7.257 2.558 499.993 1.00 95.03 B C
ANISOU 6171 CA CYS B 357 13006 14654 8447 -3300 119 1387 B C
ATOM 6172 C CYS B 357 -8.512 2.890 500.788 1.00 93.85 B C
ANISOU 6172 C CYS B 357 12760 14869 8030 -3686 397 1140 B C
ATOM 6173 O CYS B 357 -8.678 4.000 501.297 1.00 96.38 B O
ANISOU 6173 O CYS B 357 12889 15485 8247 -3758 559 822 B O
ATOM 6174 CB CYS B 357 -6.343 1.640 500.813 1.00 99.49 B C
ANISOU 6174 CB CYS B 357 13840 15197 8764 -3430 -142 1827 B C
ATOM 6175 SG CYS B 357 -5.746 2.375 502.341 1.00112.79 B S
ANISOU 6175 SG CYS B 357 15515 17332 10008 -3682 -160 1803 B S
ATOM 6176 N ASP B 358 -9.432 1.935 500.821 1.00 93.56 B N
ANISOU 6176 N ASP B 358 12840 14795 7912 -3929 468 1257 B N
ATOM 6177 CA ASP B 358 -10.713 2.130 501.486 1.00101.28 B C
ANISOU 6177 CA ASP B 358 13724 16101 8657 -4311 745 1011 B C
ATOM 6178 C ASP B 358 -10.714 1.789 502.981 1.00105.59 B C
ANISOU 6178 C ASP B 358 14434 16982 8702 -4771 750 1176 B C
ATOM 6179 O ASP B 358 -11.352 2.495 503.772 1.00105.84 B O
ANISOU 6179 O ASP B 358 14319 17393 8502 -5052 977 877 B O
ATOM 6180 CB ASP B 358 -11.763 1.359 500.712 1.00101.18 B C
ANISOU 6180 CB ASP B 358 13728 15900 8818 -4347 845 1005 B C
ATOM 6181 CG ASP B 358 -11.683 1.673 499.238 1.00 98.18 B C
ANISOU 6181 CG ASP B 358 13199 15200 8905 -3905 815 871 B C
ATOM 6182 OD1 ASP B 358 -12.188 2.737 498.821 1.00100.28 B O
ANISOU 6182 OD1 ASP B 358 13193 15564 9346 -3771 984 485 B O
ATOM 6183 OD2 ASP B 358 -11.080 0.863 498.500 1.00 97.97 B O1-
ANISOU 6183 OD2 ASP B 358 13328 14821 9075 -3692 615 1154 B O1-
ATOM 6184 N GLY B 359 -10.039 0.722 503.392 1.00106.74 B N
ANISOU 6184 N GLY B 359 14877 17001 8678 -4868 508 1637 B N
ATOM 6185 CA GLY B 359 -10.107 0.271 504.768 1.00109.83 B C
ANISOU 6185 CA GLY B 359 15457 17696 8579 -5333 495 1841 B C
ATOM 6186 C GLY B 359 -8.743 -0.038 505.351 1.00113.49 B C
ANISOU 6186 C GLY B 359 16119 18122 8879 -5280 178 2228 B C
ATOM 6187 O GLY B 359 -7.814 -0.440 504.647 1.00114.01 B O
ANISOU 6187 O GLY B 359 16269 17829 9219 -4922 -74 2470 B O
ATOM 6188 N ILE B 360 -8.640 0.148 506.667 1.00116.62 B N
ANISOU 6188 N ILE B 360 16582 18909 8818 -5655 192 2276 B N
ATOM 6189 CA ILE B 360 -7.369 -0.010 507.380 1.00123.66 B C
ANISOU 6189 CA ILE B 360 17635 19850 9499 -5646 -105 2614 B C
ATOM 6190 C ILE B 360 -7.447 -1.093 508.458 1.00109.28 B C
ANISOU 6190 C ILE B 360 16132 18153 7238 -6093 -235 3043 B C
ATOM 6191 O ILE B 360 -8.303 -1.048 509.326 1.00112.19 B O
ANISOU 6191 O ILE B 360 16518 18876 7233 -6557 -28 2930 B O
ATOM 6192 CB ILE B 360 -6.912 1.342 507.986 1.00116.81 B C
ANISOU 6192 CB ILE B 360 16548 19356 8479 -5651 -15 2291 B C
ATOM 6193 CG1 ILE B 360 -6.481 2.304 506.868 1.00108.52 B C
ANISOU 6193 CG1 ILE B 360 15240 18098 7894 -5143 16 1981 B C
ATOM 6194 CG2 ILE B 360 -5.782 1.146 508.990 1.00112.27 B C
ANISOU 6194 CG2 ILE B 360 16145 18946 7567 -5772 -292 2630 B C
ATOM 6195 CD1 ILE B 360 -5.820 3.564 507.347 1.00104.55 B C
ANISOU 6195 CD1 ILE B 360 14544 17881 7300 -5084 58 1710 B C
ATOM 6196 N THR B 369 -8.980 -3.907 515.651 1.00137.80 B N
ANISOU 6196 N THR B 369 20472 22939 8946 -8455 -423 3765 B N
ATOM 6197 CA THR B 369 -8.596 -2.590 515.141 1.00133.61 B C
ANISOU 6197 CA THR B 369 19669 22556 8539 -8193 -298 3421 B C
ATOM 6198 C THR B 369 -8.927 -2.409 513.659 1.00138.25 B C
ANISOU 6198 C THR B 369 20168 22883 9477 -7852 -164 3275 B C
ATOM 6199 O THR B 369 -8.244 -2.961 512.792 1.00130.88 B O
ANISOU 6199 O THR B 369 19366 21570 8793 -7500 -385 3587 B O
ATOM 6200 CB THR B 369 -7.099 -2.335 515.321 1.00137.58 B C
ANISOU 6200 CB THR B 369 20195 23026 9053 -7921 -603 3660 B C
ATOM 6201 CG2 THR B 369 -6.756 -0.918 514.880 1.00129.26 B C
ANISOU 6201 CG2 THR B 369 18854 22161 8097 -7690 -449 3264 B C
ATOM 6202 OG1 THR B 369 -6.748 -2.510 516.698 1.00146.04 B O
ANISOU 6202 OG1 THR B 369 21346 24345 9799 -8237 -738 3811 B O
ATOM 6203 N THR B 370 -9.964 -1.621 513.370 1.00131.48 B N
ANISOU 6203 N THR B 370 19074 22229 8655 -7952 195 2789 B N
ATOM 6204 CA THR B 370 -10.453 -1.458 512.007 1.00127.93 B C
ANISOU 6204 CA THR B 370 18524 21563 8519 -7683 358 2620 B C
ATOM 6205 C THR B 370 -10.924 -0.024 511.797 1.00129.18 B C
ANISOU 6205 C THR B 370 18331 22016 8735 -7644 680 2045 B C
ATOM 6206 O THR B 370 -11.328 0.657 512.746 1.00122.04 B O
ANISOU 6206 O THR B 370 17262 21474 7633 -7928 849 1723 B O
ATOM 6207 CB THR B 370 -11.600 -2.431 511.692 1.00127.29 B C
ANISOU 6207 CB THR B 370 18559 21310 8494 -7869 480 2665 B C
ATOM 6208 CG2 THR B 370 -11.071 -3.852 511.487 1.00124.66 B C
ANISOU 6208 CG2 THR B 370 18560 20566 8241 -7775 164 3228 B C
ATOM 6209 OG1 THR B 370 -12.555 -2.416 512.761 1.00127.33 B O
ANISOU 6209 OG1 THR B 370 18516 21635 8228 -8331 668 2436 B O
ATOM 6210 N TYR B 371 -10.877 0.419 510.535 1.00124.33 B N
ANISOU 6210 N TYR B 371 17597 21227 8416 -7290 761 1912 B N
ATOM 6211 CA TYR B 371 -11.277 1.767 510.145 1.00114.13 B C
ANISOU 6211 CA TYR B 371 15964 20147 7254 -7177 1055 1373 B C
ATOM 6212 C TYR B 371 -11.555 1.736 508.654 1.00119.23 B C
ANISOU 6212 C TYR B 371 16498 20388 8417 -6738 1081 1272 B C
ATOM 6213 O TYR B 371 -10.749 1.193 507.893 1.00126.09 B O
ANISOU 6213 O TYR B 371 17499 20859 9551 -6374 812 1588 B O
ATOM 6214 CB TYR B 371 -10.201 2.801 510.463 1.00113.77 B C
ANISOU 6214 CB TYR B 371 15794 20276 7159 -7005 971 1266 B C
ATOM 6215 CG TYR B 371 -10.518 4.208 510.000 1.00113.79 B C
ANISOU 6215 CG TYR B 371 15418 20381 7436 -6785 1230 694 B C
ATOM 6216 CD1 TYR B 371 -11.168 5.095 510.847 1.00115.66 B C
ANISOU 6216 CD1 TYR B 371 15427 21020 7500 -7086 1507 251 B C
ATOM 6217 CD2 TYR B 371 -10.152 4.659 508.736 1.00107.22 B C
ANISOU 6217 CD2 TYR B 371 14436 19184 7120 -6239 1167 582 B C
ATOM 6218 CE1 TYR B 371 -11.446 6.389 510.458 1.00113.50 B C
ANISOU 6218 CE1 TYR B 371 14819 20858 7449 -6911 1754 -261 B C
ATOM 6219 CE2 TYR B 371 -10.436 5.957 508.333 1.00106.61 B C
ANISOU 6219 CE2 TYR B 371 14023 19179 7305 -6036 1387 78 B C
ATOM 6220 CZ TYR B 371 -11.081 6.818 509.203 1.00110.74 B C
ANISOU 6220 CZ TYR B 371 14342 20137 7599 -6370 1679 -339 B C
ATOM 6221 OH TYR B 371 -11.381 8.111 508.828 1.00110.68 B O
ANISOU 6221 OH TYR B 371 13995 20183 7874 -6170 1897 -842 B O
ATOM 6222 N GLY B 372 -12.658 2.363 508.230 1.00125.28 B N
ANISOU 6222 N GLY B 372 16994 21240 9368 -6743 1391 806 B N
ATOM 6223 CA GLY B 372 -12.984 2.343 506.813 1.00118.66 B C
ANISOU 6223 CA GLY B 372 16031 20017 9037 -6326 1404 697 B C
ATOM 6224 C GLY B 372 -13.558 0.984 506.441 1.00113.18 B C
ANISOU 6224 C GLY B 372 15565 19079 8359 -6449 1356 996 B C
ATOM 6225 O GLY B 372 -13.992 0.216 507.307 1.00115.31 B O
ANISOU 6225 O GLY B 372 16037 19528 8250 -6904 1393 1184 B O
ATOM 6226 N GLU B 373 -13.591 0.684 505.147 1.00109.90 B N
ANISOU 6226 N GLU B 373 15119 18262 8377 -6065 1283 1032 B N
ATOM 6227 CA GLU B 373 -14.253 -0.544 504.728 1.00115.19 B C
ANISOU 6227 CA GLU B 373 15969 18706 9093 -6187 1280 1250 B C
ATOM 6228 C GLU B 373 -13.356 -1.741 505.036 1.00114.72 B C
ANISOU 6228 C GLU B 373 16282 18421 8885 -6237 971 1828 B C
ATOM 6229 O GLU B 373 -12.264 -1.868 504.475 1.00116.19 B O
ANISOU 6229 O GLU B 373 16539 18304 9306 -5859 710 2057 B O
ATOM 6230 CB GLU B 373 -14.530 -0.483 503.223 1.00116.62 B C
ANISOU 6230 CB GLU B 373 15995 18536 9782 -5764 1294 1103 B C
ATOM 6231 CG GLU B 373 -15.263 0.769 502.724 1.00116.82 B C
ANISOU 6231 CG GLU B 373 15638 18708 10042 -5606 1540 561 B C
ATOM 6232 CD GLU B 373 -16.731 0.821 503.121 1.00125.51 B C
ANISOU 6232 CD GLU B 373 16595 20100 10992 -5986 1856 237 B C
ATOM 6233 OE1 GLU B 373 -17.249 -0.175 503.683 1.00130.21 B O
ANISOU 6233 OE1 GLU B 373 17398 20766 11310 -6379 1900 431 B O
ATOM 6234 OE2 GLU B 373 -17.374 1.863 502.864 1.00123.13 B O1-
ANISOU 6234 OE2 GLU B 373 15970 19952 10863 -5894 2062 -218 B O1-
ATOM 6235 N THR B 374 -13.809 -2.631 505.910 1.00119.47 B N
ANISOU 6235 N THR B 374 17122 19159 9114 -6703 996 2063 B N
ATOM 6236 CA THR B 374 -13.036 -3.824 506.214 1.00122.06 B C
ANISOU 6236 CA THR B 374 17814 19250 9315 -6765 695 2631 B C
ATOM 6237 C THR B 374 -13.969 -5.009 506.393 1.00122.64 B C
ANISOU 6237 C THR B 374 18108 19261 9231 -7146 784 2819 B C
ATOM 6238 O THR B 374 -15.147 -4.839 506.724 1.00120.04 B O
ANISOU 6238 O THR B 374 17663 19200 8748 -7471 1074 2510 B O
ATOM 6239 CB THR B 374 -12.181 -3.686 507.486 1.00120.57 B C
ANISOU 6239 CB THR B 374 17776 19333 8704 -6989 527 2870 B C
ATOM 6240 CG2 THR B 374 -11.460 -2.351 507.556 1.00114.23 B C
ANISOU 6240 CG2 THR B 374 16722 18719 7963 -6732 521 2590 B C
ATOM 6241 OG1 THR B 374 -13.014 -3.839 508.639 1.00121.35 B O
ANISOU 6241 OG1 THR B 374 17895 19748 8464 -7458 678 2751 B O
ATOM 6242 N PRO B 375 -13.458 -6.224 506.211 1.00122.27 B N
ANISOU 6242 N PRO B 375 18364 18848 9244 -7101 531 3303 B N
ATOM 6243 CA PRO B 375 -14.203 -7.433 506.585 1.00123.20 B C
ANISOU 6243 CA PRO B 375 18679 18843 9287 -7385 542 3463 B C
ATOM 6244 C PRO B 375 -14.443 -7.489 508.089 1.00124.37 B C
ANISOU 6244 C PRO B 375 18891 19324 9041 -7778 545 3450 B C
ATOM 6245 O PRO B 375 -13.889 -6.709 508.865 1.00124.66 B O
ANISOU 6245 O PRO B 375 18848 19645 8874 -7816 493 3378 B O
ATOM 6246 CB PRO B 375 -13.279 -8.567 506.127 1.00121.52 B C
ANISOU 6246 CB PRO B 375 18737 18133 9304 -7134 207 3965 B C
ATOM 6247 CG PRO B 375 -12.488 -7.970 505.006 1.00114.54 B C
ANISOU 6247 CG PRO B 375 17724 17043 8751 -6677 118 3936 B C
ATOM 6248 CD PRO B 375 -12.267 -6.537 505.398 1.00111.19 B C
ANISOU 6248 CD PRO B 375 17031 17004 8212 -6609 216 3577 B C
ATOM 6249 N ASP B 376 -15.315 -8.401 508.509 1.00126.08 B N
ANISOU 6249 N ASP B 376 19244 19518 9143 -8093 619 3496 B N
ATOM 6250 CA ASP B 376 -15.598 -8.456 509.933 1.00135.30 B C
ANISOU 6250 CA ASP B 376 20473 21010 9927 -8499 629 3471 B C
ATOM 6251 C ASP B 376 -14.415 -9.161 510.598 1.00142.02 B C
ANISOU 6251 C ASP B 376 21591 21686 10683 -8446 253 3976 B C
ATOM 6252 O ASP B 376 -13.545 -9.717 509.919 1.00140.03 B O
ANISOU 6252 O ASP B 376 21473 21040 10691 -8108 9 4316 B O
ATOM 6253 CB ASP B 376 -16.917 -9.206 510.186 1.00144.49 B C
ANISOU 6253 CB ASP B 376 21702 22214 10985 -8866 826 3351 B C
ATOM 6254 CG ASP B 376 -17.307 -9.296 511.679 1.00154.62 B C
ANISOU 6254 CG ASP B 376 23053 23842 11854 -9335 850 3308 B C
ATOM 6255 OD1 ASP B 376 -16.518 -8.892 512.565 1.00158.07 B O
ANISOU 6255 OD1 ASP B 376 23512 24467 12080 -9389 692 3416 B O
ATOM 6256 OD2 ASP B 376 -18.413 -9.810 511.968 1.00157.75 B O1-
ANISOU 6256 OD2 ASP B 376 23487 24319 12132 -9665 1023 3167 B O1-
ATOM 6257 N GLN B 377 -14.353 -9.103 511.935 1.00150.90 B N
ANISOU 6257 N GLN B 377 22773 23109 11452 -8773 200 4009 B N
ATOM 6258 CA GLN B 377 -13.185 -9.633 512.637 1.00148.74 B C
ANISOU 6258 CA GLN B 377 22715 22720 11080 -8719 -159 4460 B C
ATOM 6259 C GLN B 377 -12.892 -11.072 512.212 1.00152.69 B C
ANISOU 6259 C GLN B 377 23498 22727 11788 -8582 -389 4915 B C
ATOM 6260 O GLN B 377 -11.733 -11.437 511.986 1.00152.05 B O
ANISOU 6260 O GLN B 377 23529 22357 11887 -8263 -695 5266 B O
ATOM 6261 CB GLN B 377 -13.375 -9.528 514.157 1.00145.09 B C
ANISOU 6261 CB GLN B 377 22293 22647 10186 -9168 -157 4430 B C
ATOM 6262 CG GLN B 377 -12.338 -10.302 514.975 1.00149.08 B C
ANISOU 6262 CG GLN B 377 23052 23026 10567 -9182 -527 4927 B C
ATOM 6263 CD GLN B 377 -12.203 -9.806 516.409 1.00156.08 B C
ANISOU 6263 CD GLN B 377 23908 24352 11042 -9546 -546 4861 B C
ATOM 6264 NE2 GLN B 377 -11.164 -10.267 517.101 1.00156.25 B N
ANISOU 6264 NE2 GLN B 377 24102 24303 10962 -9516 -876 5266 B N
ATOM 6265 OE1 GLN B 377 -13.021 -9.020 516.887 1.00153.62 B O
ANISOU 6265 OE1 GLN B 377 23410 24436 10523 -9849 -269 4441 B O
ATOM 6266 N THR B 378 -13.935 -11.906 512.109 1.00155.23 B N
ANISOU 6266 N THR B 378 23928 22946 12105 -8815 -242 4896 B N
ATOM 6267 CA THR B 378 -13.747 -13.313 511.756 1.00152.96 B C
ANISOU 6267 CA THR B 378 23907 22194 12017 -8715 -433 5302 B C
ATOM 6268 C THR B 378 -13.159 -13.495 510.355 1.00149.20 B C
ANISOU 6268 C THR B 378 23405 21279 12004 -8223 -531 5412 B C
ATOM 6269 O THR B 378 -12.181 -14.231 510.173 1.00154.56 B O
ANISOU 6269 O THR B 378 24246 21591 12888 -7958 -832 5799 B O
ATOM 6270 CB THR B 378 -15.081 -14.053 511.864 1.00150.44 B C
ANISOU 6270 CB THR B 378 23675 21887 11598 -9074 -208 5190 B C
ATOM 6271 CG2 THR B 378 -15.820 -13.644 513.143 1.00151.37 B C
ANISOU 6271 CG2 THR B 378 23753 22494 11267 -9575 -48 4959 B C
ATOM 6272 OG1 THR B 378 -15.892 -13.739 510.722 1.00147.48 B O
ANISOU 6272 OG1 THR B 378 23120 21454 11463 -8957 63 4857 B O
ATOM 6273 N THR B 379 -13.729 -12.821 509.348 1.00135.90 B N
ANISOU 6273 N THR B 379 21507 19626 10505 -8093 -283 5064 B N
ATOM 6274 CA THR B 379 -13.169 -12.925 508.002 1.00137.16 B C
ANISOU 6274 CA THR B 379 21631 19386 11099 -7644 -371 5147 B C
ATOM 6275 C THR B 379 -11.748 -12.383 507.957 1.00139.77 B C
ANISOU 6275 C THR B 379 21924 19653 11528 -7292 -644 5315 B C
ATOM 6276 O THR B 379 -10.877 -12.949 507.283 1.00144.50 B O
ANISOU 6276 O THR B 379 22611 19835 12456 -6937 -883 5587 B O
ATOM 6277 CB THR B 379 -14.060 -12.190 506.992 1.00133.62 B C
ANISOU 6277 CB THR B 379 20941 19033 10797 -7598 -47 4723 B C
ATOM 6278 CG2 THR B 379 -13.490 -12.310 505.586 1.00123.06 B C
ANISOU 6278 CG2 THR B 379 19571 17280 9905 -7157 -140 4810 B C
ATOM 6279 OG1 THR B 379 -15.377 -12.752 507.015 1.00138.22 B O
ANISOU 6279 OG1 THR B 379 21548 19664 11307 -7913 199 4558 B O
ATOM 6280 N ILE B 380 -11.500 -11.286 508.679 1.00138.84 B N
ANISOU 6280 N ILE B 380 21661 19951 11140 -7386 -608 5132 B N
ATOM 6281 CA ILE B 380 -10.165 -10.695 508.733 1.00138.63 B C
ANISOU 6281 CA ILE B 380 21583 19918 11170 -7079 -857 5260 B C
ATOM 6282 C ILE B 380 -9.183 -11.688 509.335 1.00145.75 B C
ANISOU 6282 C ILE B 380 22718 20569 12090 -7001 -1223 5726 B C
ATOM 6283 O ILE B 380 -8.021 -11.780 508.914 1.00153.34 B O
ANISOU 6283 O ILE B 380 23694 21264 13303 -6620 -1490 5938 B O
ATOM 6284 CB ILE B 380 -10.188 -9.362 509.513 1.00134.29 B C
ANISOU 6284 CB ILE B 380 20831 19894 10297 -7250 -718 4945 B C
ATOM 6285 CG1 ILE B 380 -10.724 -8.221 508.645 1.00128.39 B C
ANISOU 6285 CG1 ILE B 380 19813 19314 9657 -7142 -425 4505 B C
ATOM 6286 CG2 ILE B 380 -8.807 -8.996 510.020 1.00135.87 B C
ANISOU 6286 CG2 ILE B 380 21039 20139 10449 -7050 -1014 5145 B C
ATOM 6287 CD1 ILE B 380 -10.762 -6.882 509.366 1.00123.03 B C
ANISOU 6287 CD1 ILE B 380 18907 19136 8701 -7288 -266 4152 B C
ATOM 6288 N ASN B 381 -9.647 -12.474 510.305 1.00142.78 B N
ANISOU 6288 N ASN B 381 22521 20264 11465 -7357 -1241 5884 B N
ATOM 6289 CA ASN B 381 -8.788 -13.482 510.910 1.00145.06 B C
ANISOU 6289 CA ASN B 381 23035 20312 11767 -7305 -1581 6334 B C
ATOM 6290 C ASN B 381 -8.569 -14.659 509.968 1.00146.79 B C
ANISOU 6290 C ASN B 381 23397 19968 12407 -7021 -1716 6593 B C
ATOM 6291 O ASN B 381 -7.484 -15.244 509.959 1.00149.46 B O
ANISOU 6291 O ASN B 381 23834 20006 12947 -6746 -2028 6916 B O
ATOM 6292 CB ASN B 381 -9.369 -13.939 512.250 1.00151.52 B C
ANISOU 6292 CB ASN B 381 24006 21390 12174 -7795 -1555 6423 B C
ATOM 6293 CG ASN B 381 -9.362 -12.833 513.311 1.00155.83 B C
ANISOU 6293 CG ASN B 381 24413 22480 12316 -8063 -1475 6201 B C
ATOM 6294 ND2 ASN B 381 -10.330 -12.875 514.222 1.00157.70 B N
ANISOU 6294 ND2 ASN B 381 24687 23037 12196 -8546 -1291 6064 B N
ATOM 6295 OD1 ASN B 381 -8.490 -11.969 513.317 1.00159.01 B O
ANISOU 6295 OD1 ASN B 381 24673 23009 12734 -7844 -1575 6145 B O
ATOM 6296 N LYS B 382 -9.578 -15.036 509.176 1.00142.80 B N
ANISOU 6296 N LYS B 382 22892 19311 12053 -7082 -1481 6441 B N
ATOM 6297 CA LYS B 382 -9.335 -16.025 508.118 1.00139.57 B C
ANISOU 6297 CA LYS B 382 22574 18363 12094 -6773 -1583 6626 B C
ATOM 6298 C LYS B 382 -8.290 -15.533 507.116 1.00133.43 B C
ANISOU 6298 C LYS B 382 21654 17354 11689 -6274 -1730 6612 B C
ATOM 6299 O LYS B 382 -7.451 -16.315 506.647 1.00133.77 B O
ANISOU 6299 O LYS B 382 21778 16970 12080 -5953 -1968 6865 B O
ATOM 6300 CB LYS B 382 -10.615 -16.431 507.400 1.00136.82 B C
ANISOU 6300 CB LYS B 382 22225 17920 11843 -6929 -1286 6428 B C
ATOM 6301 CG LYS B 382 -11.631 -17.095 508.281 1.00143.21 B C
ANISOU 6301 CG LYS B 382 23190 18886 12338 -7397 -1154 6456 B C
ATOM 6302 CD LYS B 382 -12.805 -17.502 507.448 1.00141.48 B C
ANISOU 6302 CD LYS B 382 22948 18543 12264 -7499 -872 6248 B C
ATOM 6303 CE LYS B 382 -12.352 -18.721 506.649 1.00140.40 B C
ANISOU 6303 CE LYS B 382 22957 17836 12552 -7213 -1038 6532 B C
ATOM 6304 NZ LYS B 382 -13.277 -19.137 505.578 1.00138.31 B N1+
ANISOU 6304 NZ LYS B 382 22649 17369 12533 -7210 -797 6343 B N1+
ATOM 6305 N LEU B 383 -8.318 -14.236 506.796 1.00129.41 B N
ANISOU 6305 N LEU B 383 20925 17127 11117 -6207 -1588 6304 B N
ATOM 6306 CA LEU B 383 -7.334 -13.637 505.897 1.00138.55 B C
ANISOU 6306 CA LEU B 383 21940 18114 12590 -5758 -1721 6265 B C
ATOM 6307 C LEU B 383 -5.952 -13.791 506.517 1.00141.74 B C
ANISOU 6307 C LEU B 383 22399 18442 13012 -5550 -2078 6551 B C
ATOM 6308 O LEU B 383 -5.010 -14.320 505.893 1.00141.56 B O
ANISOU 6308 O LEU B 383 22397 18018 13372 -5168 -2309 6732 B O
ATOM 6309 CB LEU B 383 -7.693 -12.165 505.661 1.00137.66 B C
ANISOU 6309 CB LEU B 383 21592 18389 12323 -5795 -1487 5880 B C
ATOM 6310 CG LEU B 383 -8.884 -11.898 504.730 1.00132.28 B C
ANISOU 6310 CG LEU B 383 20799 17726 11735 -5883 -1150 5566 B C
ATOM 6311 CD1 LEU B 383 -9.156 -10.403 504.617 1.00126.47 B C
ANISOU 6311 CD1 LEU B 383 19820 17400 10835 -5916 -930 5189 B C
ATOM 6312 CD2 LEU B 383 -8.650 -12.504 503.360 1.00127.66 B C
ANISOU 6312 CD2 LEU B 383 20226 16640 11637 -5540 -1215 5640 B C
ATOM 6313 N VAL B 384 -5.826 -13.313 507.755 1.00142.40 B N
ANISOU 6313 N VAL B 384 22490 18924 12690 -5804 -2114 6567 B N
ATOM 6314 CA VAL B 384 -4.581 -13.411 508.505 1.00145.08 B C
ANISOU 6314 CA VAL B 384 22877 19262 12985 -5665 -2441 6827 B C
ATOM 6315 C VAL B 384 -4.075 -14.840 508.443 1.00148.82 B C
ANISOU 6315 C VAL B 384 23545 19270 13730 -5511 -2692 7200 B C
ATOM 6316 O VAL B 384 -2.925 -15.096 508.065 1.00141.56 B O
ANISOU 6316 O VAL B 384 22603 18060 13123 -5124 -2952 7359 B O
ATOM 6317 CB VAL B 384 -4.783 -12.927 509.954 1.00147.04 B C
ANISOU 6317 CB VAL B 384 23143 20006 12720 -6068 -2409 6804 B C
ATOM 6318 CG1 VAL B 384 -3.615 -13.373 510.835 1.00148.79 B C
ANISOU 6318 CG1 VAL B 384 23469 20178 12886 -5987 -2764 7147 B C
ATOM 6319 CG2 VAL B 384 -4.879 -11.371 509.966 1.00143.57 B C
ANISOU 6319 CG2 VAL B 384 22462 20005 12085 -6102 -2215 6423 B C
ATOM 6320 N GLU B 385 -4.936 -15.784 508.820 1.00156.33 B N
ANISOU 6320 N GLU B 385 24680 20151 14567 -5815 -2607 7323 B N
ATOM 6321 CA GLU B 385 -4.598 -17.202 508.829 1.00156.63 B C
ANISOU 6321 CA GLU B 385 24918 19758 14836 -5719 -2813 7673 B C
ATOM 6322 C GLU B 385 -4.066 -17.695 507.488 1.00155.99 B C
ANISOU 6322 C GLU B 385 24784 19173 15312 -5261 -2892 7691 B C
ATOM 6323 O GLU B 385 -3.054 -18.408 507.448 1.00158.93 B O
ANISOU 6323 O GLU B 385 25213 19221 15953 -4981 -3168 7944 B O
ATOM 6324 CB GLU B 385 -5.846 -18.030 509.153 1.00154.46 B C
ANISOU 6324 CB GLU B 385 24820 19479 14388 -6117 -2625 7713 B C
ATOM 6325 CG GLU B 385 -6.505 -17.902 510.504 1.00160.76 B C
ANISOU 6325 CG GLU B 385 25718 20703 14661 -6622 -2544 7728 B C
ATOM 6326 CD GLU B 385 -7.782 -18.745 510.552 1.00164.19 B C
ANISOU 6326 CD GLU B 385 26306 21075 15003 -6967 -2330 7719 B C
ATOM 6327 OE1 GLU B 385 -7.885 -19.726 509.781 1.00162.60 B O
ANISOU 6327 OE1 GLU B 385 26197 20437 15146 -6801 -2344 7840 B O
ATOM 6328 OE2 GLU B 385 -8.699 -18.403 511.329 1.00165.66 B O1-
ANISOU 6328 OE2 GLU B 385 26504 21654 14784 -7403 -2131 7561 B O1-
ATOM 6329 N TRP B 386 -4.727 -17.354 506.371 1.00153.21 B N
ANISOU 6329 N TRP B 386 24315 18743 15154 -5182 -2650 7415 B N
ATOM 6330 CA TRP B 386 -4.179 -17.881 505.125 1.00151.93 B C
ANISOU 6330 CA TRP B 386 24103 18096 15528 -4759 -2732 7430 B C
ATOM 6331 C TRP B 386 -2.793 -17.307 504.876 1.00151.17 B C
ANISOU 6331 C TRP B 386 23858 17940 15640 -4350 -2971 7436 B C
ATOM 6332 O TRP B 386 -1.920 -18.001 504.330 1.00151.71 B O
ANISOU 6332 O TRP B 386 23924 17605 16114 -4001 -3165 7567 B O
ATOM 6333 CB TRP B 386 -5.068 -17.559 503.926 1.00146.12 B C
ANISOU 6333 CB TRP B 386 23253 17292 14972 -4734 -2443 7126 B C
ATOM 6334 CG TRP B 386 -4.502 -18.160 502.654 1.00148.46 B C
ANISOU 6334 CG TRP B 386 23496 17087 15825 -4319 -2523 7129 B C
ATOM 6335 CD1 TRP B 386 -4.804 -19.403 502.171 1.00152.15 B C
ANISOU 6335 CD1 TRP B 386 24080 17161 16570 -4292 -2498 7240 B C
ATOM 6336 CD2 TRP B 386 -3.480 -17.634 501.777 1.00149.01 B C
ANISOU 6336 CD2 TRP B 386 23385 16990 16243 -3879 -2649 7020 B C
ATOM 6337 CE2 TRP B 386 -3.267 -18.601 500.764 1.00148.62 B C
ANISOU 6337 CE2 TRP B 386 23342 16456 16671 -3619 -2674 7044 B C
ATOM 6338 CE3 TRP B 386 -2.744 -16.443 501.732 1.00145.21 B C
ANISOU 6338 CE3 TRP B 386 22732 16726 15716 -3690 -2727 6884 B C
ATOM 6339 NE1 TRP B 386 -4.095 -19.659 501.026 1.00153.70 B N
ANISOU 6339 NE1 TRP B 386 24168 16972 17259 -3880 -2577 7179 B N
ATOM 6340 CZ2 TRP B 386 -2.360 -18.409 499.717 1.00139.76 B C
ANISOU 6340 CZ2 TRP B 386 22053 15072 15976 -3188 -2769 6920 B C
ATOM 6341 CZ3 TRP B 386 -1.835 -16.260 500.689 1.00141.49 B C
ANISOU 6341 CZ3 TRP B 386 22106 15981 15674 -3253 -2834 6780 B C
ATOM 6342 CH2 TRP B 386 -1.656 -17.239 499.698 1.00138.96 B C
ANISOU 6342 CH2 TRP B 386 21788 15188 15821 -3011 -2851 6791 B C
ATOM 6343 N LEU B 387 -2.552 -16.055 505.296 1.00150.57 B N
ANISOU 6343 N LEU B 387 23649 18266 15294 -4391 -2957 7282 B N
ATOM 6344 CA LEU B 387 -1.203 -15.524 505.105 1.00149.25 B C
ANISOU 6344 CA LEU B 387 23341 18051 15316 -4010 -3189 7286 B C
ATOM 6345 C LEU B 387 -0.211 -16.270 506.000 1.00151.40 B C
ANISOU 6345 C LEU B 387 23727 18220 15580 -3943 -3508 7620 B C
ATOM 6346 O LEU B 387 0.918 -16.556 505.580 1.00155.09 B O
ANISOU 6346 O LEU B 387 24128 18401 16397 -3559 -3731 7701 B O
ATOM 6347 CB LEU B 387 -1.167 -14.011 505.326 1.00141.93 B C
ANISOU 6347 CB LEU B 387 22242 17577 14108 -4067 -3090 7034 B C
ATOM 6348 CG LEU B 387 0.079 -13.257 504.822 1.00138.57 B C
ANISOU 6348 CG LEU B 387 21628 17106 13914 -3652 -3262 6941 B C
ATOM 6349 CD1 LEU B 387 -0.216 -11.778 504.804 1.00137.64 B C
ANISOU 6349 CD1 LEU B 387 21345 17410 13541 -3743 -3079 6640 B C
ATOM 6350 CD2 LEU B 387 1.329 -13.492 505.682 1.00145.16 B C
ANISOU 6350 CD2 LEU B 387 22487 17952 14716 -3523 -3582 7177 B C
ATOM 6351 N GLU B 388 -0.610 -16.586 507.244 1.00144.62 B N
ANISOU 6351 N GLU B 388 23030 17596 14321 -4320 -3531 7806 B N
ATOM 6352 CA GLU B 388 0.284 -17.330 508.128 1.00156.90 B C
ANISOU 6352 CA GLU B 388 24708 19054 15853 -4281 -3842 8147 B C
ATOM 6353 C GLU B 388 0.653 -18.655 507.486 1.00164.58 B C
ANISOU 6353 C GLU B 388 25774 19478 17283 -4019 -3978 8347 B C
ATOM 6354 O GLU B 388 1.769 -19.159 507.665 1.00170.87 B O
ANISOU 6354 O GLU B 388 26578 20064 18282 -3762 -4261 8554 B O
ATOM 6355 CB GLU B 388 -0.335 -17.552 509.511 1.00163.52 B C
ANISOU 6355 CB GLU B 388 25725 20210 16195 -4763 -3827 8317 B C
ATOM 6356 CG GLU B 388 -0.904 -16.329 510.203 1.00161.34 B C
ANISOU 6356 CG GLU B 388 25362 20499 15442 -5097 -3636 8084 B C
ATOM 6357 CD GLU B 388 -1.203 -16.600 511.676 1.00167.40 B C
ANISOU 6357 CD GLU B 388 26294 21568 15742 -5536 -3691 8280 B C
ATOM 6358 OE1 GLU B 388 -2.241 -17.232 511.971 1.00164.84 B O
ANISOU 6358 OE1 GLU B 388 26128 21247 15255 -5875 -3541 8330 B O
ATOM 6359 OE2 GLU B 388 -0.393 -16.192 512.542 1.00174.45 B O1-
ANISOU 6359 OE2 GLU B 388 27157 22696 16429 -5550 -3883 8380 B O1-
ATOM 6360 N GLU B 389 -0.297 -19.255 506.765 1.00162.96 B N
ANISOU 6360 N GLU B 389 25636 19044 17238 -4095 -3769 8278 B N
ATOM 6361 CA GLU B 389 -0.005 -20.491 506.050 1.00162.60 B C
ANISOU 6361 CA GLU B 389 25659 18471 17651 -3846 -3858 8420 B C
ATOM 6362 C GLU B 389 0.991 -20.209 504.936 1.00156.98 B C
ANISOU 6362 C GLU B 389 24737 17503 17404 -3354 -3944 8257 B C
ATOM 6363 O GLU B 389 1.856 -21.042 504.642 1.00162.28 B O
ANISOU 6363 O GLU B 389 25415 17803 18442 -3061 -4140 8401 B O
ATOM 6364 CB GLU B 389 -1.276 -21.132 505.482 1.00157.67 B C
ANISOU 6364 CB GLU B 389 25136 17682 17090 -4048 -3589 8346 B C
ATOM 6365 CG GLU B 389 -2.049 -22.015 506.454 1.00157.65 B C
ANISOU 6365 CG GLU B 389 25386 17722 16791 -4455 -3566 8594 B C
ATOM 6366 CD GLU B 389 -3.308 -22.584 505.826 1.00159.76 B C
ANISOU 6366 CD GLU B 389 25730 17840 17132 -4647 -3280 8481 B C
ATOM 6367 OE1 GLU B 389 -3.265 -22.944 504.628 1.00160.51 B O
ANISOU 6367 OE1 GLU B 389 25745 17581 17659 -4376 -3207 8358 B O
ATOM 6368 OE2 GLU B 389 -4.338 -22.669 506.524 1.00163.39 B O1-
ANISOU 6368 OE2 GLU B 389 26320 18545 17217 -5076 -3122 8496 B O1-
ATOM 6369 N ASN B 390 0.888 -19.038 504.312 1.00145.26 B N
ANISOU 6369 N ASN B 390 23063 16216 15914 -3264 -3797 7947 B N
ATOM 6370 CA ASN B 390 1.595 -18.788 503.072 1.00141.39 B C
ANISOU 6370 CA ASN B 390 22375 15468 15878 -2835 -3815 7741 B C
ATOM 6371 C ASN B 390 2.454 -17.530 503.193 1.00136.29 B C
ANISOU 6371 C ASN B 390 21540 15102 15143 -2659 -3913 7595 B C
ATOM 6372 O ASN B 390 3.268 -17.420 504.117 1.00135.22 B O
ANISOU 6372 O ASN B 390 21418 15119 14842 -2646 -4137 7762 B O
ATOM 6373 CB ASN B 390 0.581 -18.633 501.945 1.00136.65 B C
ANISOU 6373 CB ASN B 390 21718 14772 15428 -2868 -3519 7479 B C
ATOM 6374 CG ASN B 390 0.034 -19.967 501.482 1.00137.23 B C
ANISOU 6374 CG ASN B 390 21928 14457 15755 -2905 -3443 7581 B C
ATOM 6375 ND2 ASN B 390 0.607 -20.511 500.415 1.00137.17 B N
ANISOU 6375 ND2 ASN B 390 21829 14048 16242 -2556 -3479 7501 B N
ATOM 6376 OD1 ASN B 390 -0.888 -20.511 502.093 1.00137.40 B O
ANISOU 6376 OD1 ASN B 390 22132 14548 15525 -3255 -3344 7717 B O
ATOM 6377 N LEU B 395 7.651 -11.135 504.833 1.00132.89 B N
ANISOU 6377 N LEU B 395 20150 16295 14048 -1846 -4537 6906 B N
ATOM 6378 CA LEU B 395 7.279 -10.276 503.706 1.00133.52 B C
ANISOU 6378 CA LEU B 395 20083 16366 14282 -1718 -4331 6585 B C
ATOM 6379 C LEU B 395 5.826 -9.840 503.761 1.00135.69 B C
ANISOU 6379 C LEU B 395 20432 16877 14246 -2079 -4046 6486 B C
ATOM 6380 O LEU B 395 5.033 -10.371 504.553 1.00139.87 B O
ANISOU 6380 O LEU B 395 21135 17516 14492 -2424 -3986 6657 B O
ATOM 6381 CB LEU B 395 7.518 -10.975 502.358 1.00129.54 B C
ANISOU 6381 CB LEU B 395 19524 15360 14334 -1379 -4328 6510 B C
ATOM 6382 CG LEU B 395 8.894 -11.044 501.694 1.00124.68 B C
ANISOU 6382 CG LEU B 395 18736 14494 14145 -939 -4502 6414 B C
ATOM 6383 CD1 LEU B 395 9.967 -11.521 502.666 1.00130.72 B C
ANISOU 6383 CD1 LEU B 395 19526 15286 14855 -874 -4784 6645 B C
ATOM 6384 CD2 LEU B 395 8.820 -11.942 500.462 1.00114.47 B C
ANISOU 6384 CD2 LEU B 395 17426 12721 13346 -714 -4439 6346 B C
ATOM 6385 N PHE B 396 5.508 -8.827 502.951 1.00132.26 B N
ANISOU 6385 N PHE B 396 19857 16541 13854 -2005 -3870 6198 B N
ATOM 6386 CA PHE B 396 4.138 -8.403 502.701 1.00128.62 B C
ANISOU 6386 CA PHE B 396 19432 16246 13190 -2284 -3577 6054 B C
ATOM 6387 C PHE B 396 3.590 -9.183 501.506 1.00137.04 B C
ANISOU 6387 C PHE B 396 20539 16875 14656 -2155 -3479 6034 B C
ATOM 6388 O PHE B 396 4.322 -9.865 500.781 1.00141.27 B O
ANISOU 6388 O PHE B 396 21038 17008 15630 -1827 -3616 6071 B O
ATOM 6389 CB PHE B 396 4.032 -6.913 502.361 1.00109.91 B C
ANISOU 6389 CB PHE B 396 16877 14194 10689 -2258 -3420 5729 B C
ATOM 6390 CG PHE B 396 4.933 -6.477 501.240 1.00107.84 B C
ANISOU 6390 CG PHE B 396 16403 13695 10877 -1798 -3465 5486 B C
ATOM 6391 CD1 PHE B 396 4.355 -5.964 500.085 1.00116.25 B C
ANISOU 6391 CD1 PHE B 396 17300 14662 12206 -1647 -3180 5096 B C
ATOM 6392 CD2 PHE B 396 6.308 -6.620 501.285 1.00107.48 B C
ANISOU 6392 CD2 PHE B 396 16318 13512 11009 -1520 -3774 5628 B C
ATOM 6393 CE1 PHE B 396 5.123 -5.563 499.014 1.00112.03 B C
ANISOU 6393 CE1 PHE B 396 16581 13916 12068 -1257 -3201 4864 B C
ATOM 6394 CE2 PHE B 396 7.087 -6.233 500.212 1.00113.19 B C
ANISOU 6394 CE2 PHE B 396 16850 14017 12138 -1127 -3799 5393 B C
ATOM 6395 CZ PHE B 396 6.493 -5.698 499.074 1.00111.57 B C
ANISOU 6395 CZ PHE B 396 16491 13730 12169 -1002 -3502 5004 B C
ATOM 6396 N TRP B 397 2.283 -9.047 501.292 1.00135.48 B N
ANISOU 6396 N TRP B 397 20399 16781 14298 -2427 -3218 5942 B N
ATOM 6397 CA TRP B 397 1.572 -9.567 500.129 1.00127.01 B C
ANISOU 6397 CA TRP B 397 19337 15370 13550 -2354 -3063 5855 B C
ATOM 6398 C TRP B 397 0.573 -8.542 499.609 1.00118.21 B C
ANISOU 6398 C TRP B 397 18018 14510 12387 -2410 -2682 5379 B C
ATOM 6399 O TRP B 397 -0.107 -7.873 500.391 1.00111.84 B O
ANISOU 6399 O TRP B 397 17186 14118 11189 -2704 -2506 5251 B O
ATOM 6400 CB TRP B 397 0.863 -10.909 500.359 1.00129.67 B C
ANISOU 6400 CB TRP B 397 19875 15489 13905 -2563 -3029 6073 B C
ATOM 6401 CG TRP B 397 0.324 -11.508 499.043 1.00128.19 B C
ANISOU 6401 CG TRP B 397 19680 14907 14118 -2433 -2898 5976 B C
ATOM 6402 CD1 TRP B 397 -0.811 -12.267 498.898 1.00123.36 B C
ANISOU 6402 CD1 TRP B 397 19196 14190 13486 -2681 -2717 6014 B C
ATOM 6403 CD2 TRP B 397 0.866 -11.346 497.706 1.00127.44 B C
ANISOU 6403 CD2 TRP B 397 19431 14504 14486 -2049 -2920 5795 B C
ATOM 6404 CE2 TRP B 397 0.016 -12.046 496.824 1.00126.21 B C
ANISOU 6404 CE2 TRP B 397 19319 14071 14563 -2091 -2750 5737 B C
ATOM 6405 CE3 TRP B 397 1.994 -10.695 497.175 1.00121.36 B C
ANISOU 6405 CE3 TRP B 397 18474 13677 13960 -1678 -3048 5641 B C
ATOM 6406 NE1 TRP B 397 -0.993 -12.598 497.573 1.00125.79 B N
ANISOU 6406 NE1 TRP B 397 19439 14146 14208 -2476 -2631 5878 B N
ATOM 6407 CZ2 TRP B 397 0.256 -12.107 495.445 1.00119.57 B C
ANISOU 6407 CZ2 TRP B 397 18325 12922 14183 -1773 -2693 5506 B C
ATOM 6408 CZ3 TRP B 397 2.217 -10.747 495.808 1.00117.82 B C
ANISOU 6408 CZ3 TRP B 397 17879 12921 13966 -1369 -2983 5407 B C
ATOM 6409 CH2 TRP B 397 1.356 -11.450 494.961 1.00116.42 B C
ANISOU 6409 CH2 TRP B 397 17743 12488 14005 -1421 -2810 5345 B C
ATOM 6410 N HIS B 398 0.487 -8.418 498.288 1.00117.05 B N
ANISOU 6410 N HIS B 398 17717 14115 12640 -2133 -2558 5112 B N
ATOM 6411 CA HIS B 398 -0.312 -7.373 497.674 1.00114.30 B C
ANISOU 6411 CA HIS B 398 17150 13974 12304 -2117 -2237 4659 B C
ATOM 6412 C HIS B 398 -0.812 -7.896 496.340 1.00117.22 B C
ANISOU 6412 C HIS B 398 17479 13997 13063 -1967 -2113 4529 B C
ATOM 6413 O HIS B 398 -0.056 -8.521 495.588 1.00117.89 B O
ANISOU 6413 O HIS B 398 17580 13701 13511 -1699 -2278 4631 B O
ATOM 6414 CB HIS B 398 0.535 -6.128 497.404 1.00116.88 B C
ANISOU 6414 CB HIS B 398 17245 14452 12711 -1837 -2249 4377 B C
ATOM 6415 CG HIS B 398 1.549 -6.323 496.312 1.00120.39 B C
ANISOU 6415 CG HIS B 398 17608 14526 13608 -1431 -2401 4346 B C
ATOM 6416 CD2 HIS B 398 1.532 -5.951 495.008 1.00117.26 B C
ANISOU 6416 CD2 HIS B 398 17043 13955 13556 -1173 -2274 4048 B C
ATOM 6417 ND1 HIS B 398 2.738 -6.998 496.500 1.00123.37 B N
ANISOU 6417 ND1 HIS B 398 18077 14669 14127 -1263 -2720 4640 B N
ATOM 6418 CE1 HIS B 398 3.414 -7.022 495.364 1.00118.66 B C
ANISOU 6418 CE1 HIS B 398 17362 13775 13948 -921 -2769 4501 B C
ATOM 6419 NE2 HIS B 398 2.704 -6.392 494.443 1.00119.94 B N
ANISOU 6419 NE2 HIS B 398 17374 13973 14226 -871 -2500 4148 B N
ATOM 6420 N SER B 399 -2.102 -7.682 496.081 1.00120.58 B N
ANISOU 6420 N SER B 399 17848 14561 13404 -2158 -1824 4305 B N
ATOM 6421 CA SER B 399 -2.705 -7.950 494.780 1.00121.02 B C
ANISOU 6421 CA SER B 399 17820 14370 13791 -2033 -1665 4109 B C
ATOM 6422 C SER B 399 -4.149 -7.470 494.771 1.00118.73 B C
ANISOU 6422 C SER B 399 17439 14352 13320 -2279 -1348 3839 B C
ATOM 6423 O SER B 399 -4.818 -7.453 495.813 1.00108.05 B O
ANISOU 6423 O SER B 399 16171 13283 11600 -2620 -1262 3904 B O
ATOM 6424 CB SER B 399 -2.652 -9.420 494.382 1.00119.72 B C
ANISOU 6424 CB SER B 399 17847 13778 13863 -2033 -1785 4397 B C
ATOM 6425 OG SER B 399 -3.432 -9.612 493.209 1.00111.83 B O
ANISOU 6425 OG SER B 399 16757 12615 13117 -1980 -1586 4171 B O
ATOM 6426 N HIS B 400 -4.644 -7.130 493.588 1.00117.18 B N
ANISOU 6426 N HIS B 400 17071 14070 13383 -2120 -1179 3539 B N
ATOM 6427 CA HIS B 400 -6.030 -6.733 493.394 1.00110.28 B C
ANISOU 6427 CA HIS B 400 16083 13409 12408 -2312 -891 3266 B C
ATOM 6428 C HIS B 400 -6.838 -7.926 492.899 1.00111.27 B C
ANISOU 6428 C HIS B 400 16330 13294 12652 -2458 -816 3371 B C
ATOM 6429 O HIS B 400 -6.631 -8.414 491.780 1.00106.91 B O
ANISOU 6429 O HIS B 400 15756 12421 12445 -2250 -847 3348 B O
ATOM 6430 CB HIS B 400 -6.101 -5.558 492.422 1.00103.04 B C
ANISOU 6430 CB HIS B 400 14896 12566 11688 -2053 -764 2877 B C
ATOM 6431 CG HIS B 400 -5.390 -5.805 491.128 1.00108.42 B C
ANISOU 6431 CG HIS B 400 15529 12894 12774 -1716 -865 2848 B C
ATOM 6432 CD2 HIS B 400 -5.851 -6.186 489.913 1.00111.87 B C
ANISOU 6432 CD2 HIS B 400 15905 13112 13487 -1620 -777 2726 B C
ATOM 6433 ND1 HIS B 400 -4.027 -5.644 490.990 1.00103.96 B N
ANISOU 6433 ND1 HIS B 400 14962 12182 12357 -1447 -1075 2931 B N
ATOM 6434 CE1 HIS B 400 -3.678 -5.923 489.747 1.00101.32 B C
ANISOU 6434 CE1 HIS B 400 14570 11549 12376 -1206 -1106 2857 B C
ATOM 6435 NE2 HIS B 400 -4.766 -6.252 489.072 1.00106.76 B N
ANISOU 6435 NE2 HIS B 400 15227 12194 13144 -1309 -928 2736 B N
ATOM 6436 N MET B 401 -7.737 -8.389 493.761 1.00116.44 B N
ANISOU 6436 N MET B 401 17115 14117 13011 -2835 -710 3477 B N
ATOM 6437 CA MET B 401 -8.653 -9.504 493.535 1.00123.73 B C
ANISOU 6437 CA MET B 401 18171 14875 13965 -3062 -607 3577 B C
ATOM 6438 C MET B 401 -7.940 -10.665 492.842 1.00127.94 B C
ANISOU 6438 C MET B 401 18851 14927 14831 -2883 -793 3830 B C
ATOM 6439 O MET B 401 -8.200 -10.989 491.683 1.00128.14 B O
ANISOU 6439 O MET B 401 18800 14724 15163 -2743 -718 3693 B O
ATOM 6440 CB MET B 401 -9.880 -9.054 492.729 1.00122.87 B C
ANISOU 6440 CB MET B 401 17854 14896 13935 -3100 -328 3201 B C
ATOM 6441 CG MET B 401 -10.990 -10.123 492.580 1.00125.04 B C
ANISOU 6441 CG MET B 401 18245 15070 14193 -3387 -179 3256 B C
ATOM 6442 SD MET B 401 -11.651 -10.821 494.134 1.00137.37 B S
ANISOU 6442 SD MET B 401 20064 16837 15293 -3912 -128 3520 B S
ATOM 6443 CE MET B 401 -13.065 -9.753 494.453 1.00127.04 B C
ANISOU 6443 CE MET B 401 18512 16032 13726 -4158 203 3086 B C
ATOM 6444 N LEU B 402 -6.975 -11.258 493.555 1.00128.28 B N
ANISOU 6444 N LEU B 402 19095 14818 14827 -2874 -1049 4195 B N
ATOM 6445 CA LEU B 402 -6.380 -12.488 493.038 1.00123.93 B C
ANISOU 6445 CA LEU B 402 18702 13794 14592 -2746 -1225 4459 B C
ATOM 6446 C LEU B 402 -7.402 -13.604 492.974 1.00122.00 B C
ANISOU 6446 C LEU B 402 18620 13398 14338 -3038 -1093 4570 B C
ATOM 6447 O LEU B 402 -7.354 -14.444 492.064 1.00114.49 B O
ANISOU 6447 O LEU B 402 17701 12076 13723 -2925 -1104 4598 B O
ATOM 6448 CB LEU B 402 -5.161 -12.945 493.834 1.00123.11 B C
ANISOU 6448 CB LEU B 402 18777 13540 14460 -2674 -1546 4845 B C
ATOM 6449 CG LEU B 402 -3.870 -12.514 493.139 1.00116.33 B C
ANISOU 6449 CG LEU B 402 17772 12504 13923 -2242 -1726 4765 B C
ATOM 6450 CD1 LEU B 402 -2.676 -12.812 494.017 1.00122.28 B C
ANISOU 6450 CD1 LEU B 402 18667 13175 14619 -2169 -2049 5119 B C
ATOM 6451 CD2 LEU B 402 -3.746 -13.149 491.756 1.00105.03 B C
ANISOU 6451 CD2 LEU B 402 16282 10666 12957 -2014 -1703 4662 B C
ATOM 6452 N LYS B 403 -8.302 -13.659 493.959 1.00128.66 B N
ANISOU 6452 N LYS B 403 19572 14521 14792 -3430 -967 4634 B N
ATOM 6453 CA LYS B 403 -9.239 -14.765 494.110 1.00129.12 B C
ANISOU 6453 CA LYS B 403 19823 14456 14782 -3763 -853 4782 B C
ATOM 6454 C LYS B 403 -8.498 -16.042 494.459 1.00135.60 B C
ANISOU 6454 C LYS B 403 20933 |