***  test 1  ***
Job options:
ID = 22012619325799739
JOBID = test 1
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 test 1
CRYST1 32.364 53.389 74.944 90.00 90.00 90.00 P 21 21 21 1
ATOM 1 N ACYS A 1 11.779 15.793 0.053 0.50 20.48 N
ANISOU 1 N ACYS A 1 3180 2574 2026 -173 -11 517 N
ATOM 2 N BCYS A 1 11.756 15.735 0.087 0.50 19.68 N
ANISOU 2 N BCYS A 1 3160 2439 1878 -206 -13 544 N
ATOM 3 CA ACYS A 1 10.809 15.332 1.089 0.50 20.58 C
ANISOU 3 CA ACYS A 1 3141 2610 2069 -103 18 483 C
ATOM 4 CA BCYS A 1 10.835 15.087 1.084 0.50 18.98 C
ANISOU 4 CA BCYS A 1 3141 2290 1778 -185 -35 491 C
ATOM 5 C ACYS A 1 9.616 14.557 0.470 0.50 18.36 C
ANISOU 5 C ACYS A 1 2930 2296 1750 -122 -28 697 C
ATOM 6 C BCYS A 1 9.607 14.451 0.450 0.50 17.13 C
ANISOU 6 C BCYS A 1 2901 2072 1533 -171 -3 788 C
ATOM 7 O ACYS A 1 8.889 13.873 1.201 0.50 19.39 O
ANISOU 7 O ACYS A 1 3009 2378 1979 -122 40 611 O
ATOM 8 O BCYS A 1 8.849 13.725 1.133 0.50 17.03 O
ANISOU 8 O BCYS A 1 3105 1839 1524 -133 169 1085 O
ATOM 9 CB ACYS A 1 10.327 16.539 1.937 0.50 21.46 C
ANISOU 9 CB ACYS A 1 3132 2734 2285 -107 68 392 C
ATOM 10 CB BCYS A 1 10.384 16.019 2.194 0.50 18.90 C
ANISOU 10 CB BCYS A 1 3134 2359 1687 -38 53 522 C
ATOM 11 SG ACYS A 1 10.477 16.496 3.830 0.50 26.49 S
ANISOU 11 SG ACYS A 1 3936 3564 2564 102 667 534 S
ATOM 12 SG BCYS A 1 11.719 16.784 3.088 0.50 24.58 S
ANISOU 12 SG BCYS A 1 3916 3366 2056 -263 19 -523 S
ATOM 13 N ASP A 2 9.467 14.575 -0.860 1.00 18.05 N
ANISOU 13 N ASP A 2 2859 2441 1555 -266 -131 820 N
ATOM 14 CA ASP A 2 8.416 13.853 -1.473 1.00 18.44 C
ANISOU 14 CA ASP A 2 3028 2499 1477 -351 -122 915 C
ATOM 15 C ASP A 2 8.594 12.336 -1.275 1.00 17.83 C
ANISOU 15 C ASP A 2 3102 2533 1140 -304 -27 830 C
ATOM 16 O ASP A 2 7.587 11.660 -1.364 1.00 19.15 O
ANISOU 16 O ASP A 2 3004 2855 1416 -441 31 662 O
ATOM 17 CB ASP A 2 8.220 14.232 -2.900 1.00 19.63 C
ANISOU 17 CB ASP A 2 3211 2608 1639 -445 -124 823 C
ATOM 18 CG ASP A 2 7.662 15.655 -3.078 1.00 21.34 C
ANISOU 18 CG ASP A 2 3322 2859 1926 -68 -516 1160 C
ATOM 19 OD1 ASP A 2 6.970 16.176 -2.168 1.00 27.85 O
ANISOU 19 OD1 ASP A 2 4028 3860 2692 381 -249 1139 O
ATOM 20 OD2 ASP A 2 7.923 16.278 -4.088 1.00 25.97 O1-
ANISOU 20 OD2 ASP A 2 3676 3570 2621 -429 -603 1071 O1-
ATOM 21 N ALA A 3 9.822 11.816 -1.047 1.00 16.97 N
ANISOU 21 N ALA A 3 3010 2458 980 -430 331 706 N
ATOM 22 CA ALA A 3 10.015 10.383 -0.794 1.00 17.47 C
ANISOU 22 CA ALA A 3 3122 2407 1109 -153 241 622 C
ATOM 23 C ALA A 3 9.287 9.911 0.449 1.00 13.97 C
ANISOU 23 C ALA A 3 3017 1785 503 -130 285 326 C
ATOM 24 O ALA A 3 9.019 8.724 0.591 1.00 15.18 O
ANISOU 24 O ALA A 3 3283 1748 736 6 510 31 O
ATOM 25 CB ALA A 3 11.465 10.076 -0.649 1.00 19.89 C
ANISOU 25 CB ALA A 3 3172 2583 1802 -203 246 819 C
ATOM 26 N PHE A 4 8.996 10.840 1.361 1.00 12.69 N
ANISOU 26 N PHE A 4 2769 1545 506 -161 133 318 N
ATOM 27 CA PHE A 4 8.264 10.487 2.581 1.00 11.93 C
ANISOU 27 CA PHE A 4 2680 1331 521 -16 138 162 C
ATOM 28 C PHE A 4 6.758 10.530 2.431 1.00 10.76 C
ANISOU 28 C PHE A 4 2567 1133 386 -49 91 42 C
ATOM 29 O PHE A 4 6.040 9.971 3.248 1.00 12.08 O
ANISOU 29 O PHE A 4 2748 1373 468 -214 135 247 O
ATOM 30 CB PHE A 4 8.645 11.433 3.727 1.00 12.73 C
ANISOU 30 CB PHE A 4 2603 1427 807 -52 27 -11 C
ATOM 31 CG PHE A 4 10.069 11.305 4.160 1.00 12.26 C
ANISOU 31 CG PHE A 4 2570 1396 691 11 -32 -65 C
ATOM 32 CD1 PHE A 4 10.447 10.284 5.009 1.00 13.61 C
ANISOU 32 CD1 PHE A 4 2782 1800 588 -93 -47 181 C
ATOM 33 CD2 PHE A 4 11.022 12.214 3.759 1.00 15.76 C
ANISOU 33 CD2 PHE A 4 2885 2139 963 -111 -328 402 C
ATOM 34 CE1 PHE A 4 11.738 10.164 5.416 1.00 15.22 C
ANISOU 34 CE1 PHE A 4 2826 2221 734 126 -112 108 C
ATOM 35 CE2 PHE A 4 12.335 12.061 4.125 1.00 16.62 C
ANISOU 35 CE2 PHE A 4 2725 2638 951 -366 139 249 C
ATOM 36 CZ PHE A 4 12.690 11.033 4.990 1.00 14.48 C
ANISOU 36 CZ PHE A 4 2489 2221 792 101 -116 -197 C
ATOM 37 N VAL A 5 6.278 11.249 1.424 1.00 11.20 N
ANISOU 37 N VAL A 5 2698 1250 306 -29 76 224 N
ATOM 38 CA VAL A 5 4.862 11.496 1.328 1.00 11.54 C
ANISOU 38 CA VAL A 5 2629 1227 528 -128 173 -31 C
ATOM 39 C VAL A 5 4.135 10.193 1.034 1.00 11.80 C
ANISOU 39 C VAL A 5 2735 1289 456 -257 110 -225 C
ATOM 40 O VAL A 5 4.523 9.396 0.166 1.00 15.61 O
ANISOU 40 O VAL A 5 3312 1658 961 -499 528 -510 O
ATOM 41 CB VAL A 5 4.607 12.579 0.295 1.00 12.55 C
ANISOU 41 CB VAL A 5 2774 1210 782 12 76 198 C
ATOM 42 CG1 VAL A 5 3.152 12.606 -0.252 1.00 16.21 C
ANISOU 42 CG1 VAL A 5 3416 1783 958 -100 -371 141 C
ATOM 43 CG2 VAL A 5 5.141 13.916 0.796 1.00 14.35 C
ANISOU 43 CG2 VAL A 5 3054 1278 1118 -221 -173 269 C
ATOM 44 N GLY A 6 2.988 10.031 1.653 1.00 11.59 N
ANISOU 44 N GLY A 6 2673 1303 427 -278 80 -133 N
ATOM 45 CA GLY A 6 2.165 8.885 1.426 1.00 12.62 C
ANISOU 45 CA GLY A 6 2700 1572 522 -234 77 -130 C
ATOM 46 C GLY A 6 1.499 8.402 2.667 1.00 10.77 C
ANISOU 46 C GLY A 6 2341 1318 434 -214 -132 -89 C
ATOM 47 O GLY A 6 1.442 9.081 3.668 1.00 12.82 O
ANISOU 47 O GLY A 6 2926 1391 551 -342 147 -194 O
ATOM 48 N THR A 7 0.980 7.201 2.550 1.00 11.21 N
ANISOU 48 N THR A 7 2530 1333 394 -174 -215 -58 N
ATOM 49 CA THR A 7 0.238 6.535 3.616 1.00 11.96 C
ANISOU 49 CA THR A 7 2563 1212 767 -39 -128 -78 C
ATOM 50 C THR A 7 1.011 5.279 3.974 1.00 11.23 C
ANISOU 50 C THR A 7 2419 1259 588 -98 -186 -1 C
ATOM 51 O THR A 7 1.261 4.449 3.110 1.00 13.32 O
ANISOU 51 O THR A 7 3028 1392 639 82 -363 -90 O
ATOM 52 CB THR A 7 -1.162 6.185 3.147 1.00 13.79 C
ANISOU 52 CB THR A 7 2542 1288 1407 -42 -93 150 C
ATOM 53 CG2 THR A 7 -2.042 5.761 4.247 1.00 17.93 C
ANISOU 53 CG2 THR A 7 2876 2123 1814 -172 -5 -40 C
ATOM 54 OG1 THR A 7 -1.729 7.307 2.452 1.00 18.84 O
ANISOU 54 OG1 THR A 7 2954 1840 2364 -90 -489 130 O
ATOM 55 N TRP A 8 1.350 5.157 5.249 1.00 10.74 N
ANISOU 55 N TRP A 8 2446 1295 336 42 21 82 N
ATOM 56 CA TRP A 8 2.259 4.155 5.759 1.00 10.97 C
ANISOU 56 CA TRP A 8 2552 1224 390 -71 76 96 C
ATOM 57 C TRP A 8 1.597 3.390 6.876 1.00 10.82 C
ANISOU 57 C TRP A 8 2622 1135 353 -133 176 -5 C
ATOM 58 O TRP A 8 0.761 3.944 7.601 1.00 14.92 O
ANISOU 58 O TRP A 8 3378 1369 922 -12 704 172 O
ATOM 59 CB TRP A 8 3.510 4.836 6.296 1.00 10.42 C
ANISOU 59 CB TRP A 8 2473 1177 309 38 97 220 C
ATOM 60 CG TRP A 8 4.243 5.666 5.273 1.00 10.22 C
ANISOU 60 CG TRP A 8 2453 1170 260 -7 -127 -1 C
ATOM 61 CD1 TRP A 8 4.142 7.004 5.047 1.00 10.43 C
ANISOU 61 CD1 TRP A 8 2412 1245 305 -77 24 62 C
ATOM 62 CD2 TRP A 8 5.236 5.176 4.372 1.00 10.16 C
ANISOU 62 CD2 TRP A 8 2380 1057 422 -30 -63 137 C
ATOM 63 CE2 TRP A 8 5.682 6.267 3.609 1.00 10.34 C
ANISOU 63 CE2 TRP A 8 2339 1321 267 -163 90 -113 C
ATOM 64 CE3 TRP A 8 5.778 3.912 4.120 1.00 10.69 C
ANISOU 64 CE3 TRP A 8 2470 1184 404 -192 -82 -38 C
ATOM 65 NE1 TRP A 8 5.005 7.378 4.030 1.00 11.16 N
ANISOU 65 NE1 TRP A 8 2604 1226 408 -198 137 53 N
ATOM 66 CZ2 TRP A 8 6.660 6.125 2.627 1.00 11.66 C
ANISOU 66 CZ2 TRP A 8 2558 1500 371 -296 22 -41 C
ATOM 67 CZ3 TRP A 8 6.763 3.778 3.173 1.00 11.56 C
ANISOU 67 CZ3 TRP A 8 2332 1273 786 -31 -69 -172 C
ATOM 68 CH2 TRP A 8 7.163 4.866 2.406 1.00 12.21 C
ANISOU 68 CH2 TRP A 8 2385 1588 666 -152 239 -385 C
ATOM 69 N LYS A 9 1.920 2.130 7.023 1.00 10.50 N
ANISOU 69 N LYS A 9 2493 1123 371 -150 -56 164 N
ATOM 70 CA LYS A 9 1.380 1.290 8.104 1.00 11.25 C
ANISOU 70 CA LYS A 9 2458 1381 433 -156 -51 195 C
ATOM 71 C LYS A 9 2.505 0.612 8.842 1.00 10.45 C
ANISOU 71 C LYS A 9 2299 1179 491 -179 29 194 C
ATOM 72 O LYS A 9 3.447 0.130 8.245 1.00 11.06 O
ANISOU 72 O LYS A 9 2425 1362 413 -97 -24 70 O
ATOM 73 CB LYS A 9 0.463 0.256 7.499 1.00 13.67 C
ANISOU 73 CB LYS A 9 2544 1663 988 -285 -51 565 C
ATOM 74 CG LYS A 9 1.056 -0.687 6.523 1.00 20.11 C
ANISOU 74 CG LYS A 9 3382 2446 1813 -317 -239 208 C
ATOM 75 CD LYS A 9 0.019 -1.643 5.988 1.00 25.34 C
ANISOU 75 CD LYS A 9 3891 3111 2623 -606 -309 -204 C
ATOM 76 CE LYS A 9 0.667 -2.635 5.032 1.00 27.06 C
ANISOU 76 CE LYS A 9 4027 3352 2901 -822 -280 -769 C
ATOM 77 NZ LYS A 9 0.484 -2.414 3.549 1.00 32.18 N1+
ANISOU 77 NZ LYS A 9 4567 4142 3516 -480 -449 -21 N1+
ATOM 78 N LEU A 10 2.422 0.612 10.175 1.00 11.73 N
ANISOU 78 N LEU A 10 2369 1560 527 -129 -42 266 N
ATOM 79 CA LEU A 10 3.468 -0.006 11.001 1.00 11.33 C
ANISOU 79 CA LEU A 10 2237 1530 536 -313 -90 192 C
ATOM 80 C LEU A 10 3.436 -1.501 10.785 1.00 12.05 C
ANISOU 80 C LEU A 10 2408 1571 599 -315 -127 317 C
ATOM 81 O LEU A 10 2.376 -2.096 10.992 1.00 14.46 O
ANISOU 81 O LEU A 10 2585 1794 1115 -471 -144 470 O
ATOM 82 CB LEU A 10 3.254 0.313 12.477 1.00 12.37 C
ANISOU 82 CB LEU A 10 2426 1850 421 -315 58 240 C
ATOM 83 CG LEU A 10 4.334 -0.246 13.396 1.00 12.95 C
ANISOU 83 CG LEU A 10 2568 1768 584 -306 -225 260 C
ATOM 84 CD1 LEU A 10 5.653 0.444 13.213 1.00 13.42 C
ANISOU 84 CD1 LEU A 10 2362 1950 787 -17 -20 137 C
ATOM 85 CD2 LEU A 10 3.881 -0.178 14.887 1.00 15.73 C
ANISOU 85 CD2 LEU A 10 2826 2632 517 11 33 283 C
ATOM 86 N VAL A 11 4.593 -2.078 10.473 1.00 11.83 N
ANISOU 86 N VAL A 11 2608 1172 716 -222 -365 132 N
ATOM 87 CA VAL A 11 4.713 -3.531 10.340 1.00 14.22 C
ANISOU 87 CA VAL A 11 3007 1390 1005 -106 -483 105 C
ATOM 88 C VAL A 11 5.633 -4.243 11.315 1.00 14.97 C
ANISOU 88 C VAL A 11 3076 1328 1284 -155 -586 459 C
ATOM 89 O VAL A 11 5.518 -5.445 11.488 1.00 19.17 O
ANISOU 89 O VAL A 11 3797 1425 2059 -291 -1008 609 O
ATOM 90 CB VAL A 11 5.074 -3.935 8.931 1.00 15.39 C
ANISOU 90 CB VAL A 11 3209 1258 1379 57 -429 -102 C
ATOM 91 CG1 VAL A 11 3.989 -3.467 7.993 1.00 17.72 C
ANISOU 91 CG1 VAL A 11 3577 1809 1345 164 -592 -69 C
ATOM 92 CG2 VAL A 11 6.488 -3.468 8.493 1.00 16.81 C
ANISOU 92 CG2 VAL A 11 3363 1906 1118 173 -55 -232 C
ATOM 93 N SER A 12 6.565 -3.539 11.949 1.00 13.74 N
ANISOU 93 N SER A 12 2994 1348 876 -176 -459 187 N
ATOM 94 CA SER A 12 7.390 -4.157 12.974 1.00 14.10 C
ANISOU 94 CA SER A 12 3045 1320 992 -11 -462 228 C
ATOM 95 C SER A 12 7.890 -3.096 13.912 1.00 12.27 C
ANISOU 95 C SER A 12 2601 1289 772 -41 -302 276 C
ATOM 96 O SER A 12 8.071 -1.931 13.540 1.00 12.69 O
ANISOU 96 O SER A 12 2812 1368 640 -183 -210 445 O
ATOM 97 CB SER A 12 8.522 -4.928 12.349 1.00 17.16 C
ANISOU 97 CB SER A 12 3292 2042 1183 134 -438 189 C
ATOM 98 OG SER A 12 9.489 -4.078 11.805 1.00 17.97 O
ANISOU 98 OG SER A 12 3608 2082 1138 276 -278 188 O
ATOM 99 N SER A 13 8.180 -3.542 15.111 1.00 13.20 N
ANISOU 99 N SER A 13 2876 1263 873 -298 -436 512 N
ATOM 100 CA SER A 13 8.727 -2.701 16.134 1.00 13.68 C
ANISOU 100 CA SER A 13 2825 1457 915 -297 -483 439 C
ATOM 101 C SER A 13 9.685 -3.511 16.994 1.00 13.84 C
ANISOU 101 C SER A 13 2779 1567 909 -306 -233 639 C
ATOM 102 O SER A 13 9.368 -4.656 17.344 1.00 16.68 O
ANISOU 102 O SER A 13 3267 1603 1466 -494 -634 764 O
ATOM 103 CB SER A 13 7.531 -2.169 16.971 1.00 15.44 C
ANISOU 103 CB SER A 13 3141 1774 951 -329 -495 270 C
ATOM 104 OG SER A 13 7.893 -1.283 17.992 1.00 17.10 O
ANISOU 104 OG SER A 13 3655 2023 818 -269 -688 244 O
ATOM 105 N GLU A 14 10.824 -2.927 17.320 1.00 11.91 N
ANISOU 105 N GLU A 14 2688 1230 606 -144 -290 275 N
ATOM 106 CA AGLU A 14 11.878 -3.514 18.147 0.50 12.88 C
ANISOU 106 CA AGLU A 14 2784 1127 983 9 -235 105 C
ATOM 107 CA BGLU A 14 11.738 -3.542 18.228 0.50 11.40 C
ANISOU 107 CA BGLU A 14 2626 959 745 23 -201 -15 C
ATOM 108 C GLU A 14 12.147 -2.556 19.305 1.00 10.73 C
ANISOU 108 C GLU A 14 2416 1075 584 61 -78 82 C
ATOM 109 O GLU A 14 12.417 -1.379 19.033 1.00 11.44 O
ANISOU 109 O GLU A 14 2780 1064 502 -78 -255 83 O
ATOM 110 CB AGLU A 14 13.236 -3.628 17.367 0.50 14.59 C
ANISOU 110 CB AGLU A 14 2901 1268 1375 6 -281 87 C
ATOM 111 CB BGLU A 14 12.975 -4.025 17.450 0.50 11.91 C
ANISOU 111 CB BGLU A 14 2540 1130 852 74 -214 -211 C
ATOM 112 CG AGLU A 14 13.383 -4.318 16.010 0.50 18.96 C
ANISOU 112 CG AGLU A 14 3393 1734 2076 125 -147 -99 C
ATOM 113 CG BGLU A 14 12.805 -5.143 16.500 0.50 13.49 C
ANISOU 113 CG BGLU A 14 2730 1255 1139 29 53 -491 C
ATOM 114 CD AGLU A 14 14.705 -3.846 15.331 0.50 23.07 C
ANISOU 114 CD AGLU A 14 3796 2400 2570 325 143 -1 C
ATOM 115 CD BGLU A 14 12.765 -6.504 17.158 0.50 14.19 C
ANISOU 115 CD BGLU A 14 2728 1584 1076 231 56 -490 C
ATOM 116 OE1AGLU A 14 15.703 -3.486 16.048 0.50 21.79 O
ANISOU 116 OE1AGLU A 14 3798 1602 2876 691 250 -137 O
ATOM 117 OE1BGLU A 14 13.014 -6.578 18.372 0.50 16.35 O
ANISOU 117 OE1BGLU A 14 3057 1532 1621 150 -736 -562 O
ATOM 118 OE2AGLU A 14 14.734 -3.769 14.075 0.50 23.71 O1-
ANISOU 118 OE2AGLU A 14 4386 1911 2712 337 498 -48 O1-
ATOM 119 OE2BGLU A 14 12.455 -7.485 16.469 0.50 17.79 O1-
ANISOU 119 OE2BGLU A 14 3266 1786 1707 254 95 -870 O1-
ATOM 120 N ASN A 15 12.167 -3.058 20.527 1.00 10.64 N
ANISOU 120 N ASN A 15 2361 1146 533 -57 -145 225 N
ATOM 121 CA AASN A 15 12.670 -2.335 21.699 0.50 9.72 C
ANISOU 121 CA AASN A 15 2309 1062 323 75 -176 160 C
ATOM 122 CA BASN A 15 12.615 -2.319 21.708 0.50 11.06 C
ANISOU 122 CA BASN A 15 2445 1237 518 68 -160 102 C
ATOM 123 C ASN A 15 11.825 -1.109 22.058 1.00 10.22 C
ANISOU 123 C ASN A 15 2327 1141 415 15 -41 116 C
ATOM 124 O ASN A 15 12.305 -0.240 22.784 1.00 11.03 O
ANISOU 124 O ASN A 15 2435 1219 536 5 -115 64 O
ATOM 125 CB AASN A 15 14.172 -1.996 21.542 0.50 10.16 C
ANISOU 125 CB AASN A 15 2362 1094 402 78 -203 202 C
ATOM 126 CB BASN A 15 14.063 -1.929 21.588 0.50 12.10 C
ANISOU 126 CB BASN A 15 2579 1391 627 54 -134 67 C
ATOM 127 CG AASN A 15 14.948 -2.010 22.862 0.50 8.63 C
ANISOU 127 CG AASN A 15 2119 807 354 204 -149 189 C
ATOM 128 CG BASN A 15 14.901 -3.086 21.382 0.50 16.49 C
ANISOU 128 CG BASN A 15 2796 2095 1372 188 -142 -11 C
ATOM 129 ND2AASN A 15 15.777 -0.996 23.073 0.50 9.36 N
ANISOU 129 ND2AASN A 15 2162 1006 387 133 26 153 N
ATOM 130 ND2BASN A 15 15.502 -3.202 20.230 0.50 22.26 N
ANISOU 130 ND2BASN A 15 3501 2965 1991 671 316 214 N
ATOM 131 OD1AASN A 15 14.809 -2.935 23.662 0.50 10.02 O
ANISOU 131 OD1AASN A 15 2321 862 624 -5 -153 346 O
ATOM 132 OD1BASN A 15 14.954 -3.934 22.243 0.50 18.79 O
ANISOU 132 OD1BASN A 15 3839 1557 1740 432 120 -23 O
ATOM 133 N PHE A 16 10.586 -1.038 21.600 1.00 11.10 N
ANISOU 133 N PHE A 16 2358 1190 669 -46 -4 -13 N
ATOM 134 CA PHE A 16 9.770 0.140 21.861 1.00 11.60 C
ANISOU 134 CA PHE A 16 2364 1546 496 0 -81 31 C
ATOM 135 C PHE A 16 9.404 0.277 23.320 1.00 11.48 C
ANISOU 135 C PHE A 16 2379 1360 621 -66 -120 117 C
ATOM 136 O PHE A 16 9.331 1.403 23.828 1.00 11.02 O
ANISOU 136 O PHE A 16 2445 1215 524 -181 -13 50 O
ATOM 137 CB PHE A 16 8.539 0.145 20.934 1.00 12.43 C
ANISOU 137 CB PHE A 16 2355 1689 675 120 -126 -6 C
ATOM 138 CG PHE A 16 7.790 1.457 20.912 1.00 13.17 C
ANISOU 138 CG PHE A 16 2549 2132 320 226 -37 -2 C
ATOM 139 CD1 PHE A 16 8.434 2.638 20.570 1.00 13.46 C
ANISOU 139 CD1 PHE A 16 2587 1789 736 384 -115 -106 C
ATOM 140 CD2 PHE A 16 6.439 1.482 21.144 1.00 14.47 C
ANISOU 140 CD2 PHE A 16 2739 2157 600 344 -27 -249 C
ATOM 141 CE1 PHE A 16 7.721 3.845 20.477 1.00 14.75 C
ANISOU 141 CE1 PHE A 16 2968 1805 830 253 -159 2 C
ATOM 142 CE2 PHE A 16 5.724 2.660 21.038 1.00 15.15 C
ANISOU 142 CE2 PHE A 16 2712 2396 648 473 44 -122 C
ATOM 143 CZ PHE A 16 6.374 3.813 20.730 1.00 14.50 C
ANISOU 143 CZ PHE A 16 2980 1997 529 595 -276 -115 C
ATOM 144 N ASP A 17 9.128 -0.812 24.023 1.00 11.92 N
ANISOU 144 N ASP A 17 2590 1164 772 -96 137 -7 N
ATOM 145 CA ASP A 17 8.817 -0.719 25.447 1.00 12.07 C
ANISOU 145 CA ASP A 17 2644 1314 625 -113 206 172 C
ATOM 146 C ASP A 17 10.004 -0.114 26.192 1.00 12.00 C
ANISOU 146 C ASP A 17 2535 1264 759 -83 30 449 C
ATOM 147 O ASP A 17 9.822 0.782 27.021 1.00 12.36 O
ANISOU 147 O ASP A 17 2867 1281 547 -86 77 123 O
ATOM 148 CB ASP A 17 8.424 -2.080 25.988 1.00 14.58 C
ANISOU 148 CB ASP A 17 2892 1550 1097 -119 229 249 C
ATOM 149 CG ASP A 17 7.882 -1.990 27.377 1.00 16.68 C
ANISOU 149 CG ASP A 17 3061 1929 1347 -352 279 632 C
ATOM 150 OD1 ASP A 17 8.504 -2.522 28.287 1.00 22.59 O
ANISOU 150 OD1 ASP A 17 3571 3517 1495 -145 62 704 O
ATOM 151 OD2 ASP A 17 6.845 -1.378 27.579 1.00 18.00 O1-
ANISOU 151 OD2 ASP A 17 3413 2346 1077 -59 447 434 O1-
ATOM 152 N ASP A 18 11.213 -0.572 25.910 1.00 11.99 N
ANISOU 152 N ASP A 18 2584 1233 739 25 128 304 N
ATOM 153 CA AASP A 18 12.373 -0.051 26.577 0.50 13.22 C
ANISOU 153 CA AASP A 18 2577 1563 881 12 27 438 C
ATOM 154 CA BASP A 18 12.403 -0.043 26.577 0.50 13.30 C
ANISOU 154 CA BASP A 18 2600 1582 869 47 -5 442 C
ATOM 155 C ASP A 18 12.607 1.430 26.252 1.00 11.80 C
ANISOU 155 C ASP A 18 2381 1396 703 7 44 239 C
ATOM 156 O ASP A 18 12.964 2.232 27.122 1.00 12.68 O
ANISOU 156 O ASP A 18 2644 1597 576 54 -121 148 O
ATOM 157 CB AASP A 18 13.583 -0.905 26.251 0.50 14.84 C
ANISOU 157 CB AASP A 18 2650 1793 1193 39 108 394 C
ATOM 158 CB BASP A 18 13.686 -0.806 26.234 0.50 15.11 C
ANISOU 158 CB BASP A 18 2706 1731 1303 80 45 415 C
ATOM 159 CG AASP A 18 13.614 -2.193 27.041 0.50 19.56 C
ANISOU 159 CG AASP A 18 2995 1999 2436 -24 322 473 C
ATOM 160 CG BASP A 18 14.000 -1.942 27.214 0.50 19.86 C
ANISOU 160 CG BASP A 18 3091 2338 2114 293 25 529 C
ATOM 161 OD1AASP A 18 12.834 -2.312 27.995 0.50 21.04 O
ANISOU 161 OD1AASP A 18 4086 2208 1698 327 366 809 O
ATOM 162 OD1BASP A 18 14.921 -1.843 28.057 0.50 23.66 O
ANISOU 162 OD1BASP A 18 4031 2551 2407 534 -413 783 O
ATOM 163 OD2AASP A 18 14.456 -3.055 26.750 0.50 22.13 O1-
ANISOU 163 OD2AASP A 18 3424 2308 2676 146 335 235 O1-
ATOM 164 OD2BASP A 18 13.350 -2.988 27.090 0.50 19.88 O1-
ANISOU 164 OD2BASP A 18 3619 1721 2212 325 819 955 O1-
ATOM 165 N TYR A 19 12.400 1.822 25.004 1.00 10.73 N
ANISOU 165 N TYR A 19 2432 1235 410 -27 -69 216 N
ATOM 166 CA TYR A 19 12.433 3.241 24.646 1.00 10.44 C
ANISOU 166 CA TYR A 19 2257 1343 363 -64 -2 183 C
ATOM 167 C TYR A 19 11.427 4.049 25.450 1.00 10.49 C
ANISOU 167 C TYR A 19 2418 1166 400 -45 13 221 C
ATOM 168 O TYR A 19 11.774 5.104 26.031 1.00 11.09 O
ANISOU 168 O TYR A 19 2590 1328 295 -242 -85 82 O
ATOM 169 CB TYR A 19 12.208 3.410 23.123 1.00 10.35 C
ANISOU 169 CB TYR A 19 2294 1301 337 1 7 -55 C
ATOM 170 CG TYR A 19 11.996 4.856 22.720 1.00 10.11 C
ANISOU 170 CG TYR A 19 2283 1289 270 -87 76 -49 C
ATOM 171 CD1 TYR A 19 13.066 5.736 22.628 1.00 10.39 C
ANISOU 171 CD1 TYR A 19 2357 1322 265 -99 53 28 C
ATOM 172 CD2 TYR A 19 10.714 5.358 22.495 1.00 11.06 C
ANISOU 172 CD2 TYR A 19 2466 1480 256 -49 26 57 C
ATOM 173 CE1 TYR A 19 12.862 7.084 22.328 1.00 10.14 C
ANISOU 173 CE1 TYR A 19 2348 1148 356 -238 105 73 C
ATOM 174 CE2 TYR A 19 10.516 6.703 22.184 1.00 10.66 C
ANISOU 174 CE2 TYR A 19 2284 1398 368 91 -84 1 C
ATOM 175 CZ TYR A 19 11.586 7.549 22.096 1.00 10.54 C
ANISOU 175 CZ TYR A 19 2497 1240 268 -167 -36 -118 C
ATOM 176 OH TYR A 19 11.375 8.872 21.791 1.00 11.49 O
ANISOU 176 OH TYR A 19 2620 1204 541 50 -83 130 O
ATOM 177 N MET A 20 10.191 3.591 25.496 1.00 10.25 N
ANISOU 177 N MET A 20 2388 1190 316 -81 79 63 N
ATOM 178 CA MET A 20 9.182 4.310 26.225 1.00 10.47 C
ANISOU 178 CA MET A 20 2349 1371 258 -32 16 71 C
ATOM 179 C MET A 20 9.529 4.402 27.725 1.00 11.27 C
ANISOU 179 C MET A 20 2460 1354 467 -152 57 135 C
ATOM 180 O MET A 20 9.298 5.426 28.365 1.00 11.68 O
ANISOU 180 O MET A 20 2718 1397 321 -227 -1 -16 O
ATOM 181 CB MET A 20 7.788 3.693 26.047 1.00 10.79 C
ANISOU 181 CB MET A 20 2347 1495 257 -49 65 51 C
ATOM 182 CG MET A 20 7.193 3.944 24.686 1.00 11.80 C
ANISOU 182 CG MET A 20 2596 1570 318 13 40 162 C
ATOM 183 SD MET A 20 5.446 3.473 24.599 1.00 13.76 S
ANISOU 183 SD MET A 20 2553 2243 431 -64 -5 -9 S
ATOM 184 CE MET A 20 5.619 1.696 24.635 1.00 14.37 C
ANISOU 184 CE MET A 20 2616 2101 740 -303 -63 -226 C
ATOM 185 N LYS A 21 10.090 3.329 28.295 1.00 11.50 N
ANISOU 185 N LYS A 21 2621 1494 253 -168 22 -8 N
ATOM 186 CA LYS A 21 10.530 3.385 29.700 1.00 13.03 C
ANISOU 186 CA LYS A 21 2759 1886 305 -234 28 193 C
ATOM 187 C LYS A 21 11.567 4.475 29.865 1.00 13.48 C
ANISOU 187 C LYS A 21 2800 2030 292 -273 -167 128 C
ATOM 188 O LYS A 21 11.504 5.224 30.850 1.00 15.65 O
ANISOU 188 O LYS A 21 3242 2359 342 -445 -109 -89 O
ATOM 189 CB LYS A 21 11.151 2.052 30.142 1.00 14.47 C
ANISOU 189 CB LYS A 21 2880 2303 312 -99 -7 347 C
ATOM 190 CG LYS A 21 10.187 0.935 30.378 1.00 16.40 C
ANISOU 190 CG LYS A 21 3117 2357 757 67 -40 463 C
ATOM 191 CD LYS A 21 10.865 -0.265 30.980 1.00 19.47 C
ANISOU 191 CD LYS A 21 3474 2248 1676 38 -11 1018 C
ATOM 192 CE LYS A 21 9.901 -1.301 31.234 1.00 23.54 C
ANISOU 192 CE LYS A 21 3887 2688 2366 12 -256 960 C
ATOM 193 NZ LYS A 21 10.600 -2.408 31.872 1.00 27.40 N1+
ANISOU 193 NZ LYS A 21 4672 2379 3359 163 -258 1317 N1+
ATOM 194 N GLU A 22 12.523 4.583 28.957 1.00 14.08 N
ANISOU 194 N GLU A 22 2851 2140 359 -358 -165 56 N
ATOM 195 CA GLU A 22 13.580 5.561 29.050 1.00 15.23 C
ANISOU 195 CA GLU A 22 2993 2419 373 -420 -194 30 C
ATOM 196 C GLU A 22 13.002 6.960 28.993 1.00 14.67 C
ANISOU 196 C GLU A 22 3138 2121 312 -495 -110 -151 C
ATOM 197 O GLU A 22 13.446 7.881 29.686 1.00 17.43 O
ANISOU 197 O GLU A 22 3636 2497 488 -729 -291 -208 O
ATOM 198 CB GLU A 22 14.670 5.292 28.000 1.00 16.01 C
ANISOU 198 CB GLU A 22 2978 2412 693 -451 -123 75 C
ATOM 199 CG GLU A 22 16.055 5.731 28.251 1.00 19.25 C
ANISOU 199 CG GLU A 22 3191 2911 1212 -213 -380 -64 C
ATOM 200 CD GLU A 22 16.786 4.901 29.346 1.00 22.45 C
ANISOU 200 CD GLU A 22 3538 3089 1903 -362 -553 265 C
ATOM 201 OE1 GLU A 22 16.247 3.898 29.849 1.00 24.82 O
ANISOU 201 OE1 GLU A 22 3749 3390 2289 -449 -728 421 O
ATOM 202 OE2 GLU A 22 17.949 5.241 29.693 1.00 25.26 O1-
ANISOU 202 OE2 GLU A 22 4225 3136 2235 -20 -1017 -97 O1-
ATOM 203 N VAL A 23 11.977 7.149 28.147 1.00 13.91 N
ANISOU 203 N VAL A 23 3042 1885 355 -396 -42 -69 N
ATOM 204 CA VAL A 23 11.311 8.426 28.005 1.00 13.94 C
ANISOU 204 CA VAL A 23 3149 1872 274 -457 9 -162 C
ATOM 205 C VAL A 23 10.568 8.785 29.304 1.00 14.53 C
ANISOU 205 C VAL A 23 3335 1729 457 -478 151 -179 C
ATOM 206 O VAL A 23 10.423 9.942 29.589 1.00 17.08 O
ANISOU 206 O VAL A 23 4088 1712 691 -506 534 -282 O
ATOM 207 CB VAL A 23 10.383 8.353 26.762 1.00 14.93 C
ANISOU 207 CB VAL A 23 3299 1834 540 -339 86 -96 C
ATOM 208 CG1 VAL A 23 9.428 9.509 26.742 1.00 15.61 C
ANISOU 208 CG1 VAL A 23 3444 1484 1000 -121 -205 36 C
ATOM 209 CG2 VAL A 23 11.211 8.333 25.497 1.00 15.37 C
ANISOU 209 CG2 VAL A 23 3471 2011 356 -46 259 40 C
ATOM 210 N GLY A 24 10.078 7.809 30.026 1.00 13.42 N
ANISOU 210 N GLY A 24 3242 1578 279 -471 176 -66 N
ATOM 211 CA GLY A 24 9.322 8.018 31.271 1.00 14.36 C
ANISOU 211 CA GLY A 24 3123 1803 529 -391 189 -54 C
ATOM 212 C GLY A 24 7.840 7.674 31.143 1.00 13.58 C
ANISOU 212 C GLY A 24 2998 1643 517 -251 292 -46 C
ATOM 213 O GLY A 24 7.038 8.065 32.006 1.00 15.89 O
ANISOU 213 O GLY A 24 3172 2069 793 -375 313 -179 O
ATOM 214 N VAL A 25 7.448 6.907 30.126 1.00 12.33 N
ANISOU 214 N VAL A 25 2887 1240 556 -199 54 10 N
ATOM 215 CA VAL A 25 6.051 6.550 29.965 1.00 12.01 C
ANISOU 215 CA VAL A 25 2771 1321 470 -54 1 88 C
ATOM 216 C VAL A 25 5.663 5.510 31.018 1.00 11.97 C
ANISOU 216 C VAL A 25 2616 1521 411 -172 -65 -98 C
ATOM 217 O VAL A 25 6.417 4.557 31.260 1.00 13.04 O
ANISOU 217 O VAL A 25 2982 1637 335 -247 -125 216 O
ATOM 218 CB VAL A 25 5.832 5.972 28.552 1.00 11.89 C
ANISOU 218 CB VAL A 25 2723 1242 552 20 -34 12 C
ATOM 219 CG1 VAL A 25 4.376 5.704 28.365 1.00 13.64 C
ANISOU 219 CG1 VAL A 25 2832 1826 524 -155 -116 116 C
ATOM 220 CG2 VAL A 25 6.399 6.929 27.439 1.00 13.83 C
ANISOU 220 CG2 VAL A 25 3209 1573 472 -126 -76 429 C
ATOM 221 N GLY A 26 4.496 5.708 31.631 1.00 13.16 N
ANISOU 221 N GLY A 26 2771 1807 420 -174 40 67 N
ATOM 222 CA GLY A 26 4.044 4.797 32.660 1.00 13.49 C
ANISOU 222 CA GLY A 26 2627 2076 419 -300 1 -25 C
ATOM 223 C GLY A 26 3.516 3.477 32.141 1.00 12.70 C
ANISOU 223 C GLY A 26 2569 1912 344 -222 20 54 C
ATOM 224 O GLY A 26 3.271 3.306 30.962 1.00 13.37 O
ANISOU 224 O GLY A 26 2810 2012 256 -360 -51 -57 O
ATOM 225 N PHE A 27 3.312 2.539 33.052 1.00 12.98 N
ANISOU 225 N PHE A 27 2817 1842 270 -227 -127 27 N
ATOM 226 CA PHE A 27 3.019 1.164 32.678 1.00 12.73 C
ANISOU 226 CA PHE A 27 2579 1802 455 -245 -51 151 C
ATOM 227 C PHE A 27 1.808 1.033 31.769 1.00 12.01 C
ANISOU 227 C PHE A 27 2471 1573 518 -324 4 213 C
ATOM 228 O PHE A 27 1.891 0.417 30.706 1.00 12.82 O
ANISOU 228 O PHE A 27 2802 1756 314 -345 -97 70 O
ATOM 229 CB PHE A 27 2.776 0.349 33.985 1.00 13.49 C
ANISOU 229 CB PHE A 27 2697 1929 498 -243 -30 220 C
ATOM 230 CG PHE A 27 2.389 -1.077 33.702 1.00 14.03 C
ANISOU 230 CG PHE A 27 2922 1970 437 -309 -367 433 C
ATOM 231 CD1 PHE A 27 3.341 -2.087 33.593 1.00 16.44 C
ANISOU 231 CD1 PHE A 27 3412 2274 557 -459 -83 326 C
ATOM 232 CD2 PHE A 27 1.083 -1.400 33.586 1.00 16.06 C
ANISOU 232 CD2 PHE A 27 3110 2001 990 -225 -435 709 C
ATOM 233 CE1 PHE A 27 2.945 -3.403 33.331 1.00 18.94 C
ANISOU 233 CE1 PHE A 27 3672 2220 1301 -254 87 352 C
ATOM 234 CE2 PHE A 27 0.688 -2.718 33.314 1.00 17.27 C
ANISOU 234 CE2 PHE A 27 3445 2248 869 -608 -458 764 C
ATOM 235 CZ PHE A 27 1.610 -3.691 33.184 1.00 18.12 C
ANISOU 235 CZ PHE A 27 3786 2236 860 -448 -408 213 C
ATOM 236 N ALA A 28 0.652 1.549 32.171 1.00 12.82 N
ANISOU 236 N ALA A 28 2626 1785 459 -260 59 79 N
ATOM 237 CA ALA A 28 -0.589 1.308 31.402 1.00 13.32 C
ANISOU 237 CA ALA A 28 2548 1857 655 -219 -15 338 C
ATOM 238 C ALA A 28 -0.489 1.943 30.036 1.00 12.79 C
ANISOU 238 C ALA A 28 2548 1680 632 -248 -60 190 C
ATOM 239 O ALA A 28 -0.913 1.350 29.040 1.00 14.25 O
ANISOU 239 O ALA A 28 2749 1917 747 -382 -194 28 O
ATOM 240 CB ALA A 28 -1.792 1.838 32.162 1.00 15.40 C
ANISOU 240 CB ALA A 28 2641 2030 1178 -138 300 297 C
ATOM 241 N THR A 29 0.093 3.143 29.944 1.00 12.77 N
ANISOU 241 N THR A 29 2687 1707 456 -287 -82 83 N
ATOM 242 CA THR A 29 0.284 3.793 28.662 1.00 12.17 C
ANISOU 242 CA THR A 29 2455 1667 502 -141 -117 250 C
ATOM 243 C THR A 29 1.222 2.964 27.812 1.00 12.22 C
ANISOU 243 C THR A 29 2444 1641 555 -193 -13 48 C
ATOM 244 O THR A 29 0.959 2.789 26.597 1.00 12.78 O
ANISOU 244 O THR A 29 2705 1814 335 -224 -216 31 O
ATOM 245 CB THR A 29 0.743 5.234 28.835 1.00 13.70 C
ANISOU 245 CB THR A 29 2716 1578 909 -176 -57 314 C
ATOM 246 CG2 THR A 29 0.916 5.905 27.494 1.00 15.00 C
ANISOU 246 CG2 THR A 29 2760 1613 1326 -128 -141 568 C
ATOM 247 OG1 THR A 29 -0.249 5.958 29.574 1.00 16.63 O
ANISOU 247 OG1 THR A 29 3001 2012 1303 107 0 226 O
ATOM 248 N ARG A 30 2.326 2.457 28.347 1.00 11.99 N
ANISOU 248 N ARG A 30 2545 1746 264 -227 -112 101 N
ATOM 249 CA ARG A 30 3.228 1.629 27.543 1.00 11.70 C
ANISOU 249 CA ARG A 30 2407 1762 275 -162 90 159 C
ATOM 250 C ARG A 30 2.554 0.428 27.006 1.00 11.96 C
ANISOU 250 C ARG A 30 2337 1906 300 -189 -57 278 C
ATOM 251 O ARG A 30 2.775 0.057 25.849 1.00 12.84 O
ANISOU 251 O ARG A 30 2500 2105 272 -180 0 188 O
ATOM 252 CB ARG A 30 4.495 1.133 28.314 1.00 12.50 C
ANISOU 252 CB ARG A 30 2638 1810 299 -254 -41 260 C
ATOM 253 CG ARG A 30 5.449 2.228 28.696 1.00 12.52 C
ANISOU 253 CG ARG A 30 2727 1630 396 -79 7 171 C
ATOM 254 CD ARG A 30 6.827 1.679 28.975 1.00 11.86 C
ANISOU 254 CD ARG A 30 2564 1680 259 -144 2 91 C
ATOM 255 NE ARG A 30 6.764 0.510 29.877 1.00 12.22 N
ANISOU 255 NE ARG A 30 2717 1577 348 -97 37 28 N
ATOM 256 CZ ARG A 30 6.631 0.549 31.184 1.00 12.31 C
ANISOU 256 CZ ARG A 30 2629 1491 555 -109 13 214 C
ATOM 257 NH1 ARG A 30 6.508 1.701 31.846 1.00 12.80 N1+
ANISOU 257 NH1 ARG A 30 3017 1507 336 -170 -86 224 N1+
ATOM 258 NH2 ARG A 30 6.588 -0.596 31.866 1.00 13.87 N
ANISOU 258 NH2 ARG A 30 3270 1697 300 32 147 95 N
ATOM 259 N LYS A 31 1.754 -0.250 27.810 1.00 12.58 N
ANISOU 259 N LYS A 31 2537 1942 300 -264 9 94 N
ATOM 260 CA LYS A 31 1.110 -1.472 27.353 1.00 12.96 C
ANISOU 260 CA LYS A 31 2578 1774 570 -193 0 -49 C
ATOM 261 C LYS A 31 0.150 -1.187 26.198 1.00 12.97 C
ANISOU 261 C LYS A 31 2406 2031 489 -175 -62 -100 C
ATOM 262 O LYS A 31 0.150 -1.905 25.177 1.00 14.42 O
ANISOU 262 O LYS A 31 2657 2164 658 -122 -31 -333 O
ATOM 263 CB LYS A 31 0.358 -2.184 28.486 1.00 14.24 C
ANISOU 263 CB LYS A 31 2898 1814 698 -273 -103 -13 C
ATOM 264 CG LYS A 31 1.294 -2.725 29.572 1.00 17.39 C
ANISOU 264 CG LYS A 31 3240 2388 980 -371 -110 414 C
ATOM 265 CD LYS A 31 2.302 -3.755 29.049 1.00 22.75 C
ANISOU 265 CD LYS A 31 3871 3068 1703 279 -306 625 C
ATOM 266 CE LYS A 31 3.511 -4.034 29.929 1.00 26.27 C
ANISOU 266 CE LYS A 31 3930 3910 2141 387 -167 -69 C
ATOM 267 NZ LYS A 31 4.716 -4.348 29.079 1.00 28.30 N1+
ANISOU 267 NZ LYS A 31 4070 4126 2557 615 -115 -32 N1+
ATOM 268 N VAL A 32 -0.676 -0.175 26.325 1.00 12.62 N
ANISOU 268 N VAL A 32 2400 2011 381 -128 -67 -176 N
ATOM 269 CA AVAL A 32 -1.652 0.161 25.269 0.50 13.49 C
ANISOU 269 CA AVAL A 32 2415 2108 601 -137 -80 -256 C
ATOM 270 CA BVAL A 32 -1.641 0.092 25.241 0.50 13.53 C
ANISOU 270 CA BVAL A 32 2410 2150 578 -152 -97 -256 C
ATOM 271 C VAL A 32 -0.964 0.765 24.058 1.00 12.95 C
ANISOU 271 C VAL A 32 2273 2140 507 -178 -111 -152 C
ATOM 272 O VAL A 32 -1.309 0.476 22.909 1.00 13.63 O
ANISOU 272 O VAL A 32 2350 2409 417 -246 -50 -292 O
ATOM 273 CB AVAL A 32 -2.735 1.158 25.852 0.50 13.38 C
ANISOU 273 CB AVAL A 32 2437 2093 554 -87 -30 -426 C
ATOM 274 CB BVAL A 32 -2.899 0.882 25.781 0.50 13.95 C
ANISOU 274 CB BVAL A 32 2421 2290 588 -96 -24 -253 C
ATOM 275 CG1AVAL A 32 -3.683 1.596 24.756 0.50 13.72 C
ANISOU 275 CG1AVAL A 32 2288 2109 814 27 -134 -137 C
ATOM 276 CG1BVAL A 32 -3.686 0.015 26.784 0.50 14.03 C
ANISOU 276 CG1BVAL A 32 2310 2326 692 -326 -109 -200 C
ATOM 277 CG2AVAL A 32 -3.519 0.518 27.035 0.50 15.00 C
ANISOU 277 CG2AVAL A 32 2680 2209 808 -331 104 -273 C
ATOM 278 CG2BVAL A 32 -2.484 2.236 26.353 0.50 15.57 C
ANISOU 278 CG2BVAL A 32 2705 2139 1069 26 75 -274 C
ATOM 279 N ALA A 33 0.025 1.621 24.274 1.00 12.99 N
ANISOU 279 N ALA A 33 2418 2150 367 -106 -202 -79 N
ATOM 280 CA ALA A 33 0.724 2.241 23.145 1.00 13.95 C
ANISOU 280 CA ALA A 33 2526 2335 437 -130 -127 253 C
ATOM 281 C ALA A 33 1.503 1.183 22.395 1.00 13.95 C
ANISOU 281 C ALA A 33 2435 2476 386 -99 -114 284 C
ATOM 282 O ALA A 33 1.617 1.265 21.168 1.00 14.87 O
ANISOU 282 O ALA A 33 2682 2631 334 -200 18 435 O
ATOM 283 CB ALA A 33 1.627 3.373 23.627 1.00 14.55 C
ANISOU 283 CB ALA A 33 2483 2415 628 -221 -61 269 C
ATOM 284 N GLY A 34 2.070 0.192 23.064 1.00 14.21 N
ANISOU 284 N GLY A 34 2506 2529 362 98 -9 247 N
ATOM 285 CA GLY A 34 2.851 -0.833 22.415 1.00 14.96 C
ANISOU 285 CA GLY A 34 2406 2641 636 212 -11 247 C
ATOM 286 C GLY A 34 2.044 -1.746 21.505 1.00 14.74 C
ANISOU 286 C GLY A 34 2516 2570 514 200 55 250 C
ATOM 287 O GLY A 34 2.600 -2.272 20.560 1.00 16.58 O
ANISOU 287 O GLY A 34 2547 2980 773 235 284 51 O
ATOM 288 N MET A 35 0.745 -1.910 21.760 1.00 13.97 N
ANISOU 288 N MET A 35 2539 2179 587 119 324 446 N
ATOM 289 CA MET A 35 -0.124 -2.725 20.910 1.00 14.13 C
ANISOU 289 CA MET A 35 2542 2007 819 40 299 509 C
ATOM 290 C MET A 35 -0.450 -2.053 19.558 1.00 13.25 C
ANISOU 290 C MET A 35 2519 1789 725 -10 268 551 C
ATOM 291 O MET A 35 -0.730 -2.729 18.547 1.00 15.27 O
ANISOU 291 O MET A 35 2717 1878 1206 -166 55 434 O
ATOM 292 CB MET A 35 -1.434 -3.043 21.584 1.00 14.86 C
ANISOU 292 CB MET A 35 2650 1709 1287 81 448 575 C
ATOM 293 CG MET A 35 -1.304 -3.950 22.773 1.00 14.18 C
ANISOU 293 CG MET A 35 3183 1578 627 -211 563 129 C
ATOM 294 SD MET A 35 -0.669 -5.547 22.430 1.00 14.44 S
ANISOU 294 SD MET A 35 3065 1555 865 49 224 230 S
ATOM 295 CE MET A 35 -1.749 -6.264 21.252 1.00 20.72 C
ANISOU 295 CE MET A 35 4571 2249 1050 -61 -436 524 C
ATOM 296 N ALA A 36 -0.390 -0.727 19.511 1.00 13.36 N
ANISOU 296 N ALA A 36 2392 1789 894 -80 92 524 N
ATOM 297 CA ALA A 36 -0.896 -0.027 18.347 1.00 13.21 C
ANISOU 297 CA ALA A 36 2339 1900 780 -21 154 417 C
ATOM 298 C ALA A 36 -0.095 -0.295 17.102 1.00 12.35 C
ANISOU 298 C ALA A 36 2362 1634 695 -233 51 277 C
ATOM 299 O ALA A 36 1.112 -0.426 17.140 1.00 13.23 O
ANISOU 299 O ALA A 36 2352 2035 639 -134 22 288 O
ATOM 300 CB ALA A 36 -0.911 1.473 18.649 1.00 14.87 C
ANISOU 300 CB ALA A 36 2834 1934 882 147 259 329 C
ATOM 301 N LYS A 37 -0.809 -0.356 16.005 1.00 13.09 N
ANISOU 301 N LYS A 37 2407 1757 807 -290 -31 305 N
ATOM 302 CA LYS A 37 -0.252 -0.521 14.676 1.00 13.23 C
ANISOU 302 CA LYS A 37 2585 1640 801 -274 46 115 C
ATOM 303 C LYS A 37 -0.730 0.663 13.852 1.00 12.35 C
ANISOU 303 C LYS A 37 2523 1714 455 -321 124 53 C
ATOM 304 O LYS A 37 -1.652 0.557 13.042 1.00 14.00 O
ANISOU 304 O LYS A 37 2549 2092 675 -454 -121 262 O
ATOM 305 CB LYS A 37 -0.644 -1.856 14.049 1.00 15.55 C
ANISOU 305 CB LYS A 37 2869 1931 1105 -285 80 104 C
ATOM 306 CG LYS A 37 -0.037 -3.066 14.748 1.00 19.68 C
ANISOU 306 CG LYS A 37 3155 1978 2345 -363 -76 188 C
ATOM 307 CD LYS A 37 1.428 -3.201 14.383 1.00 21.59 C
ANISOU 307 CD LYS A 37 3429 2854 1918 16 -100 411 C
ATOM 308 CE LYS A 37 2.008 -4.530 14.735 1.00 24.71 C
ANISOU 308 CE LYS A 37 3933 3160 2293 63 -26 345 C
ATOM 309 NZ LYS A 37 1.812 -4.835 16.144 1.00 26.50 N1+
ANISOU 309 NZ LYS A 37 4678 2954 2436 383 149 748 N1+
ATOM 310 N PRO A 38 -0.154 1.835 14.037 1.00 12.03 N
ANISOU 310 N PRO A 38 2459 1568 541 -189 69 59 N
ATOM 311 CA PRO A 38 -0.699 3.027 13.435 1.00 12.50 C
ANISOU 311 CA PRO A 38 2630 1613 506 -118 217 145 C
ATOM 312 C PRO A 38 -0.517 3.103 11.943 1.00 12.59 C
ANISOU 312 C PRO A 38 2540 1470 770 -160 353 32 C
ATOM 313 O PRO A 38 0.383 2.496 11.358 1.00 13.09 O
ANISOU 313 O PRO A 38 2797 1630 544 -175 373 143 O
ATOM 314 CB PRO A 38 0.119 4.159 14.048 1.00 15.08 C
ANISOU 314 CB PRO A 38 2974 1842 912 -64 177 -13 C
ATOM 315 CG PRO A 38 1.263 3.493 14.682 1.00 18.40 C
ANISOU 315 CG PRO A 38 2877 2189 1925 -552 -182 152 C
ATOM 316 CD PRO A 38 0.917 2.149 14.985 1.00 12.61 C
ANISOU 316 CD PRO A 38 2472 1660 658 -289 19 -131 C
ATOM 317 N ASN A 39 -1.376 3.915 11.356 1.00 12.33 N
ANISOU 317 N ASN A 39 2772 1498 413 -82 362 98 N
ATOM 318 CA ASN A 39 -1.157 4.434 10.016 1.00 13.93 C
ANISOU 318 CA ASN A 39 3136 1490 666 -91 407 99 C
ATOM 319 C ASN A 39 -0.620 5.819 10.120 1.00 14.61 C
ANISOU 319 C ASN A 39 3433 1405 711 -143 571 -86 C
ATOM 320 O ASN A 39 -1.069 6.623 10.906 1.00 19.55 O
ANISOU 320 O ASN A 39 4155 1620 1650 -483 1386 -328 O
ATOM 321 CB ASN A 39 -2.453 4.428 9.266 1.00 16.71 C
ANISOU 321 CB ASN A 39 3520 1876 953 51 -20 242 C
ATOM 322 CG ASN A 39 -2.657 3.157 8.506 1.00 19.85 C
ANISOU 322 CG ASN A 39 3635 2239 1665 -34 -119 234 C
ATOM 323 ND2 ASN A 39 -3.140 3.278 7.273 1.00 27.04 N
ANISOU 323 ND2 ASN A 39 4488 3835 1949 260 -295 -204 N
ATOM 324 OD1 ASN A 39 -2.347 2.071 9.023 1.00 26.09 O
ANISOU 324 OD1 ASN A 39 5225 2721 1963 -145 -802 258 O
ATOM 325 N MET A 40 0.388 6.105 9.325 1.00 13.65 N
ANISOU 325 N MET A 40 3323 1274 586 -157 511 109 N
ATOM 326 CA MET A 40 0.983 7.404 9.324 1.00 13.42 C
ANISOU 326 CA MET A 40 3103 1348 648 -98 380 -8 C
ATOM 327 C MET A 40 0.822 7.991 7.932 1.00 12.45 C
ANISOU 327 C MET A 40 2912 1311 504 -91 432 137 C
ATOM 328 O MET A 40 1.153 7.364 6.944 1.00 13.84 O
ANISOU 328 O MET A 40 3407 1293 556 156 482 147 O
ATOM 329 CB MET A 40 2.453 7.261 9.702 1.00 14.63 C
ANISOU 329 CB MET A 40 3339 1469 750 -45 268 -2 C
ATOM 330 CG MET A 40 3.242 8.567 9.584 1.00 15.43 C
ANISOU 330 CG MET A 40 3414 1299 1147 47 1 201 C
ATOM 331 SD MET A 40 4.897 8.428 10.218 1.00 17.10 S
ANISOU 331 SD MET A 40 3724 1585 1187 -90 -232 -63 S
ATOM 332 CE MET A 40 5.583 7.094 9.262 1.00 19.34 C
ANISOU 332 CE MET A 40 3726 2671 949 -190 196 38 C
ATOM 333 N ILE A 41 0.292 9.200 7.871 1.00 12.38 N
ANISOU 333 N ILE A 41 2773 1308 621 -84 272 -40 N
ATOM 334 CA ILE A 41 0.072 9.899 6.623 1.00 11.80 C
ANISOU 334 CA ILE A 41 2701 1313 467 -172 132 -3 C
ATOM 335 C ILE A 41 0.952 11.115 6.620 1.00 10.73 C
ANISOU 335 C ILE A 41 2639 1031 406 -132 99 -4 C
ATOM 336 O ILE A 41 0.860 11.987 7.511 1.00 12.18 O
ANISOU 336 O ILE A 41 2929 1194 503 -257 229 -47 O
ATOM 337 CB ILE A 41 -1.410 10.356 6.479 1.00 14.32 C
ANISOU 337 CB ILE A 41 2725 1579 1134 -181 128 -165 C
ATOM 338 CG1 ILE A 41 -2.367 9.147 6.596 1.00 18.60 C
ANISOU 338 CG1 ILE A 41 2990 2063 2012 -360 205 -408 C
ATOM 339 CG2 ILE A 41 -1.634 11.092 5.129 1.00 18.36 C
ANISOU 339 CG2 ILE A 41 3168 2285 1524 -191 -278 -50 C
ATOM 340 CD1 ILE A 41 -3.838 9.601 6.651 1.00 23.91 C
ANISOU 340 CD1 ILE A 41 3215 2862 3005 -460 -124 -404 C
ATOM 341 N ILE A 42 1.821 11.205 5.622 1.00 10.51 N
ANISOU 341 N ILE A 42 2642 1090 260 -126 97 -17 N
ATOM 342 CA ILE A 42 2.776 12.317 5.496 1.00 10.38 C
ANISOU 342 CA ILE A 42 2565 1125 254 -12 45 -5 C
ATOM 343 C ILE A 42 2.428 13.057 4.235 1.00 10.50 C
ANISOU 343 C ILE A 42 2457 1275 258 -74 -104 5 C
ATOM 344 O ILE A 42 2.271 12.467 3.168 1.00 11.34 O
ANISOU 344 O ILE A 42 2858 1166 284 -87 -178 13 O
ATOM 345 CB ILE A 42 4.225 11.813 5.485 1.00 10.74 C
ANISOU 345 CB ILE A 42 2603 1220 255 -62 76 -12 C
ATOM 346 CG1 ILE A 42 4.521 11.039 6.778 1.00 11.28 C
ANISOU 346 CG1 ILE A 42 2727 1295 264 -30 -75 94 C
ATOM 347 CG2 ILE A 42 5.199 12.955 5.295 1.00 11.26 C
ANISOU 347 CG2 ILE A 42 2565 1285 426 -93 -4 52 C
ATOM 348 CD1 ILE A 42 5.930 10.440 6.831 1.00 13.68 C
ANISOU 348 CD1 ILE A 42 3063 1536 597 318 -223 79 C
ATOM 349 N SER A 43 2.274 14.378 4.359 1.00 10.64 N
ANISOU 349 N SER A 43 2668 1099 274 -7 -221 23 N
ATOM 350 CA SER A 43 1.968 15.201 3.209 1.00 11.09 C
ANISOU 350 CA SER A 43 2612 1203 397 -3 -184 44 C
ATOM 351 C SER A 43 2.746 16.492 3.287 1.00 10.81 C
ANISOU 351 C SER A 43 2791 1055 259 -12 -115 -23 C
ATOM 352 O SER A 43 3.227 16.891 4.359 1.00 11.20 O
ANISOU 352 O SER A 43 2795 1202 258 16 -103 -28 O
ATOM 353 CB SER A 43 0.479 15.473 3.171 1.00 13.33 C
ANISOU 353 CB SER A 43 2884 1292 886 -13 -293 296 C
ATOM 354 OG SER A 43 0.015 16.126 4.312 1.00 16.35 O
ANISOU 354 OG SER A 43 3014 1920 1277 202 -151 232 O
ATOM 355 N VAL A 44 2.869 17.136 2.135 1.00 10.99 N
ANISOU 355 N VAL A 44 2814 1086 272 -67 -148 98 N
ATOM 356 CA VAL A 44 3.574 18.395 2.035 1.00 11.44 C
ANISOU 356 CA VAL A 44 2914 1127 304 -60 -235 167 C
ATOM 357 C VAL A 44 2.737 19.372 1.244 1.00 11.86 C
ANISOU 357 C VAL A 44 3004 1232 270 -20 -138 98 C
ATOM 358 O VAL A 44 2.152 19.010 0.210 1.00 15.69 O
ANISOU 358 O VAL A 44 4159 1402 399 17 -743 69 O
ATOM 359 CB VAL A 44 4.963 18.251 1.369 1.00 13.36 C
ANISOU 359 CB VAL A 44 2998 1386 691 -54 -264 54 C
ATOM 360 CG1 VAL A 44 5.663 19.584 1.298 1.00 19.69 C
ANISOU 360 CG1 VAL A 44 3283 1716 2481 -356 11 366 C
ATOM 361 CG2 VAL A 44 5.799 17.240 2.082 1.00 16.18 C
ANISOU 361 CG2 VAL A 44 3003 1956 1187 -67 -357 -9 C
ATOM 362 N ASN A 45 2.686 20.600 1.695 1.00 11.46 N
ANISOU 362 N ASN A 45 2843 1240 269 -45 -201 21 N
ATOM 363 CA ASN A 45 1.982 21.684 1.014 1.00 11.12 C
ANISOU 363 CA ASN A 45 2714 1226 285 -88 -271 28 C
ATOM 364 C ASN A 45 2.850 22.908 1.170 1.00 11.76 C
ANISOU 364 C ASN A 45 2781 1319 368 -6 -136 225 C
ATOM 365 O ASN A 45 2.956 23.496 2.241 1.00 11.55 O
ANISOU 365 O ASN A 45 2727 1332 329 -43 -210 76 O
ATOM 366 CB ASN A 45 0.589 21.821 1.589 1.00 12.16 C
ANISOU 366 CB ASN A 45 2707 1347 563 -68 -245 89 C
ATOM 367 CG ASN A 45 -0.276 22.849 0.913 1.00 12.72 C
ANISOU 367 CG ASN A 45 2661 1710 461 -85 -313 52 C
ATOM 368 ND2 ASN A 45 0.329 23.893 0.416 1.00 12.39 N
ANISOU 368 ND2 ASN A 45 2626 1496 584 -258 -428 301 N
ATOM 369 OD1 ASN A 45 -1.533 22.657 0.829 1.00 14.61 O
ANISOU 369 OD1 ASN A 45 2757 1877 914 -269 -142 -111 O
ATOM 370 N GLY A 46 3.513 23.267 0.091 1.00 12.82 N
ANISOU 370 N GLY A 46 3113 1481 275 -257 -129 149 N
ATOM 371 CA GLY A 46 4.466 24.358 0.166 1.00 13.60 C
ANISOU 371 CA GLY A 46 2903 1673 590 -246 -53 274 C
ATOM 372 C GLY A 46 5.601 24.018 1.117 1.00 13.46 C
ANISOU 372 C GLY A 46 2755 1752 605 -259 76 293 C
ATOM 373 O GLY A 46 6.216 22.956 1.008 1.00 15.61 O
ANISOU 373 O GLY A 46 2943 1973 1015 -72 64 47 O
ATOM 374 N ASP A 47 5.841 24.878 2.094 1.00 13.22 N
ANISOU 374 N ASP A 47 2791 1610 621 -258 -51 270 N
ATOM 375 CA ASP A 47 6.874 24.640 3.104 1.00 13.92 C
ANISOU 375 CA ASP A 47 2668 1795 827 -190 -52 342 C
ATOM 376 C ASP A 47 6.381 23.802 4.278 1.00 11.72 C
ANISOU 376 C ASP A 47 2491 1431 528 -50 -45 191 C
ATOM 377 O ASP A 47 7.183 23.495 5.165 1.00 12.76 O
ANISOU 377 O ASP A 47 2432 1791 622 -56 -75 198 O
ATOM 378 CB ASP A 47 7.405 25.991 3.620 1.00 15.29 C
ANISOU 378 CB ASP A 47 2842 1985 982 -375 -222 376 C
ATOM 379 CG ASP A 47 8.104 26.788 2.587 1.00 21.56 C
ANISOU 379 CG ASP A 47 3353 2667 2170 -504 -186 415 C
ATOM 380 OD1 ASP A 47 8.684 26.187 1.675 1.00 27.03 O
ANISOU 380 OD1 ASP A 47 3831 4239 2197 -1028 814 730 O
ATOM 381 OD2 ASP A 47 8.102 28.027 2.730 1.00 28.42 O1-
ANISOU 381 OD2 ASP A 47 4802 2998 2995 -840 -554 792 O1-
ATOM 382 N VAL A 48 5.098 23.537 4.319 1.00 10.38 N
ANISOU 382 N VAL A 48 2376 1257 311 -42 -88 235 N
ATOM 383 CA VAL A 48 4.520 22.886 5.503 1.00 9.87 C
ANISOU 383 CA VAL A 48 2284 1194 271 -36 -46 127 C
ATOM 384 C VAL A 48 4.420 21.394 5.305 1.00 9.73 C
ANISOU 384 C VAL A 48 2243 1185 267 -70 -162 36 C
ATOM 385 O VAL A 48 3.766 20.911 4.375 1.00 11.03 O
ANISOU 385 O VAL A 48 2568 1302 317 -46 -267 83 O
ATOM 386 CB VAL A 48 3.129 23.433 5.798 1.00 11.16 C
ANISOU 386 CB VAL A 48 2382 1443 412 0 -110 138 C
ATOM 387 CG1 VAL A 48 2.589 22.794 7.103 1.00 12.50 C
ANISOU 387 CG1 VAL A 48 2625 1560 562 -54 167 270 C
ATOM 388 CG2 VAL A 48 3.194 24.988 6.008 1.00 13.64 C
ANISOU 388 CG2 VAL A 48 2904 1263 1015 204 94 139 C
ATOM 389 N ILE A 49 5.034 20.639 6.223 1.00 9.40 N
ANISOU 389 N ILE A 49 2269 1036 265 -151 -113 75 N
ATOM 390 CA ILE A 49 4.950 19.192 6.253 1.00 9.38 C
ANISOU 390 CA ILE A 49 2154 1153 255 -145 -47 -29 C
ATOM 391 C ILE A 49 3.947 18.818 7.331 1.00 9.30 C
ANISOU 391 C ILE A 49 2182 1096 254 -70 -42 26 C
ATOM 392 O ILE A 49 3.997 19.404 8.450 1.00 9.68 O
ANISOU 392 O ILE A 49 2247 1170 261 -141 -42 -78 O
ATOM 393 CB ILE A 49 6.320 18.585 6.523 1.00 10.41 C
ANISOU 393 CB ILE A 49 2357 1337 261 -72 86 -69 C
ATOM 394 CG1 ILE A 49 7.337 19.004 5.475 1.00 11.25 C
ANISOU 394 CG1 ILE A 49 2347 1554 372 -67 196 -51 C
ATOM 395 CG2 ILE A 49 6.271 17.053 6.629 1.00 11.59 C
ANISOU 395 CG2 ILE A 49 2550 1193 658 92 -160 -65 C
ATOM 396 CD1 ILE A 49 8.788 18.773 5.893 1.00 16.87 C
ANISOU 396 CD1 ILE A 49 2642 2717 1050 -46 123 248 C
ATOM 397 N THR A 50 3.095 17.861 7.049 1.00 9.55 N
ANISOU 397 N THR A 50 2178 1193 255 -133 8 -47 N
ATOM 398 CA THR A 50 2.175 17.332 8.062 1.00 9.79 C
ANISOU 398 CA THR A 50 2233 1224 263 -189 121 35 C
ATOM 399 C THR A 50 2.417 15.845 8.197 1.00 9.46 C
ANISOU 399 C THR A 50 2080 1258 253 -142 7 -25 C
ATOM 400 O THR A 50 2.531 15.087 7.218 1.00 10.55 O
ANISOU 400 O THR A 50 2613 1140 254 -162 -24 23 O
ATOM 401 CB THR A 50 0.690 17.591 7.659 1.00 10.58 C
ANISOU 401 CB THR A 50 2348 1262 408 -298 5 -94 C
ATOM 402 CG2 THR A 50 -0.298 17.046 8.633 1.00 12.81 C
ANISOU 402 CG2 THR A 50 2510 1566 788 -368 194 26 C
ATOM 403 OG1 THR A 50 0.499 18.994 7.533 1.00 11.69 O
ANISOU 403 OG1 THR A 50 2351 1480 609 -48 -29 31 O
ATOM 404 N ILE A 51 2.528 15.395 9.465 1.00 9.56 N
ANISOU 404 N ILE A 51 2270 1105 256 -113 4 48 N
ATOM 405 CA ILE A 51 2.617 13.991 9.810 1.00 9.90 C
ANISOU 405 CA ILE A 51 2354 1139 269 -191 29 -36 C
ATOM 406 C ILE A 51 1.428 13.665 10.724 1.00 10.10 C
ANISOU 406 C ILE A 51 2349 1222 265 -166 90 81 C
ATOM 407 O ILE A 51 1.346 14.194 11.843 1.00 11.30 O
ANISOU 407 O ILE A 51 2684 1349 259 -40 55 -24 O
ATOM 408 CB ILE A 51 3.942 13.622 10.507 1.00 9.83 C
ANISOU 408 CB ILE A 51 2334 1139 260 -156 57 -75 C
ATOM 409 CG1 ILE A 51 5.130 13.995 9.615 1.00 11.15 C
ANISOU 409 CG1 ILE A 51 2376 1324 535 -124 141 -214 C
ATOM 410 CG2 ILE A 51 3.955 12.168 10.906 1.00 12.16 C
ANISOU 410 CG2 ILE A 51 2765 1126 727 22 98 106 C
ATOM 411 CD1 ILE A 51 6.467 13.736 10.226 1.00 13.59 C
ANISOU 411 CD1 ILE A 51 2493 1801 870 59 -59 -91 C
ATOM 412 N LYS A 52 0.508 12.854 10.244 1.00 10.57 N
ANISOU 412 N LYS A 52 2427 1286 304 -223 130 -16 N
ATOM 413 CA LYS A 52 -0.641 12.390 10.989 1.00 12.22 C
ANISOU 413 CA LYS A 52 2617 1332 693 -195 309 -64 C
ATOM 414 C LYS A 52 -0.438 10.941 11.350 1.00 12.71 C
ANISOU 414 C LYS A 52 2725 1397 706 -288 373 -251 C
ATOM 415 O LYS A 52 -0.054 10.145 10.506 1.00 15.39 O
ANISOU 415 O LYS A 52 3700 1270 878 -272 737 -33 O
ATOM 416 CB LYS A 52 -1.894 12.529 10.138 1.00 15.27 C
ANISOU 416 CB LYS A 52 2543 2072 1187 -149 341 -326 C
ATOM 417 CG LYS A 52 -3.232 12.322 10.743 1.00 20.28 C
ANISOU 417 CG LYS A 52 3220 2642 1842 -369 104 299 C
ATOM 418 CD LYS A 52 -4.297 12.670 9.705 1.00 26.04 C
ANISOU 418 CD LYS A 52 3465 3717 2709 -150 -241 113 C
ATOM 419 CE LYS A 52 -4.211 14.142 9.323 1.00 32.14 C
ANISOU 419 CE LYS A 52 4015 4129 4068 -310 -430 -67 C
ATOM 420 NZ LYS A 52 -3.347 14.503 8.155 1.00 35.98 N1+
ANISOU 420 NZ LYS A 52 4349 4783 4537 -245 -270 -324 N1+
ATOM 421 N SER A 53 -0.767 10.597 12.579 1.00 12.19 N
ANISOU 421 N SER A 53 2761 1288 582 -258 315 -108 N
ATOM 422 CA SER A 53 -0.774 9.201 13.040 1.00 12.51 C
ANISOU 422 CA SER A 53 2709 1400 642 -226 316 49 C
ATOM 423 C SER A 53 -2.209 8.853 13.453 1.00 12.23 C
ANISOU 423 C SER A 53 2680 1519 446 -328 330 -48 C
ATOM 424 O SER A 53 -2.772 9.518 14.298 1.00 14.50 O
ANISOU 424 O SER A 53 3030 1630 847 -440 522 -178 O
ATOM 425 CB SER A 53 0.154 9.024 14.213 1.00 14.18 C
ANISOU 425 CB SER A 53 2745 1635 1006 -203 301 15 C
ATOM 426 OG SER A 53 0.188 7.670 14.671 1.00 16.98 O
ANISOU 426 OG SER A 53 3485 1793 1173 -227 109 332 O
ATOM 427 N GLU A 54 -2.748 7.843 12.783 1.00 13.04 N
ANISOU 427 N GLU A 54 2720 1694 540 -363 248 -24 N
ATOM 428 CA GLU A 54 -4.066 7.326 13.074 1.00 14.03 C
ANISOU 428 CA GLU A 54 2742 1764 825 -353 171 18 C
ATOM 429 C GLU A 54 -3.865 6.014 13.803 1.00 13.56 C
ANISOU 429 C GLU A 54 2630 1776 744 -294 327 86 C
ATOM 430 O GLU A 54 -3.309 5.070 13.221 1.00 13.62 O
ANISOU 430 O GLU A 54 2828 1756 591 -165 261 112 O
ATOM 431 CB GLU A 54 -4.848 7.099 11.804 1.00 16.04 C
ANISOU 431 CB GLU A 54 2949 1918 1225 -373 47 130 C
ATOM 432 CG GLU A 54 -5.049 8.356 10.985 1.00 21.64 C
ANISOU 432 CG GLU A 54 3500 2526 2194 -377 75 374 C
ATOM 433 CD GLU A 54 -5.991 8.170 9.872 1.00 27.44 C
ANISOU 433 CD GLU A 54 4028 3383 3012 -169 -407 423 C
ATOM 434 OE1 GLU A 54 -5.846 7.171 9.169 1.00 29.86 O
ANISOU 434 OE1 GLU A 54 4922 4364 2057 -449 -1033 4 O
ATOM 435 OE2 GLU A 54 -6.856 9.046 9.676 1.00 35.75 O1-
ANISOU 435 OE2 GLU A 54 4641 4534 4407 232 -391 267 O1-
ATOM 436 N ASER A 55 -4.334 5.863 15.042 0.50 15.07 N
ANISOU 436 N ASER A 55 2719 2066 940 -154 327 139 N
ATOM 437 N BSER A 55 -4.268 6.043 15.053 0.50 13.51 N
ANISOU 437 N BSER A 55 2705 1784 643 -86 249 154 N
ATOM 438 CA ASER A 55 -4.315 4.516 15.684 0.50 15.37 C
ANISOU 438 CA ASER A 55 2640 2207 992 -73 398 318 C
ATOM 439 CA BSER A 55 -3.808 5.080 15.985 0.50 13.06 C
ANISOU 439 CA BSER A 55 2678 1505 777 52 203 217 C
ATOM 440 C ASER A 55 -5.434 4.308 16.667 0.50 14.74 C
ANISOU 440 C ASER A 55 2744 1888 968 -109 506 276 C
ATOM 441 C BSER A 55 -4.924 4.690 16.910 0.50 12.89 C
ANISOU 441 C BSER A 55 2929 1427 538 26 287 246 C
ATOM 442 O ASER A 55 -6.253 5.169 16.922 0.50 14.71 O
ANISOU 442 O ASER A 55 2719 1705 1163 -138 370 357 O
ATOM 443 O BSER A 55 -5.666 5.514 17.410 0.50 13.92 O
ANISOU 443 O BSER A 55 3096 1364 827 269 399 290 O
ATOM 444 CB ASER A 55 -2.974 4.219 16.393 0.50 17.49 C
ANISOU 444 CB ASER A 55 2785 2375 1483 9 365 218 C
ATOM 445 CB BSER A 55 -2.660 5.643 16.784 0.50 13.33 C
ANISOU 445 CB BSER A 55 2730 1500 832 19 167 253 C
ATOM 446 OG ASER A 55 -2.986 4.608 17.740 0.50 16.04 O
ANISOU 446 OG ASER A 55 2370 2293 1429 -40 589 685 O
ATOM 447 OG BSER A 55 -2.207 4.707 17.735 0.50 14.76 O
ANISOU 447 OG BSER A 55 2486 2259 861 230 313 622 O
ATOM 448 N ATHR A 56 -5.453 3.096 17.183 0.50 14.80 N
ANISOU 448 N ATHR A 56 2977 1803 844 1 532 254 N
ATOM 449 N BTHR A 56 -5.050 3.415 17.133 0.50 14.08 N
ANISOU 449 N BTHR A 56 3092 1479 778 90 202 229 N
ATOM 450 CA ATHR A 56 -6.202 2.726 18.346 0.50 14.70 C
ANISOU 450 CA ATHR A 56 3226 1737 620 -94 589 223 C
ATOM 451 CA BTHR A 56 -6.101 2.881 17.971 0.50 15.49 C
ANISOU 451 CA BTHR A 56 3336 1588 960 -5 155 365 C
ATOM 452 C ATHR A 56 -5.652 3.238 19.684 0.50 15.06 C
ANISOU 452 C ATHR A 56 3203 1726 792 -32 521 173 C
ATOM 453 C BTHR A 56 -5.947 3.391 19.424 0.50 15.82 C
ANISOU 453 C BTHR A 56 3383 1587 1038 -102 240 301 C
ATOM 454 O ATHR A 56 -6.333 3.072 20.661 0.50 15.13 O
ANISOU 454 O ATHR A 56 3463 1813 472 -146 570 339 O
ATOM 455 O BTHR A 56 -6.946 3.574 20.180 0.50 17.81 O
ANISOU 455 O BTHR A 56 3604 1942 1221 -294 228 502 O
ATOM 456 CB ATHR A 56 -6.102 1.199 18.438 0.50 14.88 C
ANISOU 456 CB ATHR A 56 3178 1713 763 -72 572 287 C
ATOM 457 CB BTHR A 56 -5.917 1.360 17.771 0.50 15.14 C
ANISOU 457 CB BTHR A 56 3273 1607 872 56 131 327 C
ATOM 458 CG2ATHR A 56 -7.066 0.542 17.407 0.50 17.49 C
ANISOU 458 CG2ATHR A 56 3878 1723 1041 -244 523 417 C
ATOM 459 CG2BTHR A 56 -5.919 0.598 18.984 0.50 14.88 C
ANISOU 459 CG2BTHR A 56 3277 1488 887 173 190 680 C
ATOM 460 OG1ATHR A 56 -4.716 0.799 18.185 0.50 11.67 O
ANISOU 460 OG1ATHR A 56 2807 1326 297 228 220 8 O
ATOM 461 OG1BTHR A 56 -6.837 0.855 16.773 0.50 17.78 O
ANISOU 461 OG1BTHR A 56 3769 2250 737 44 -216 165 O
ATOM 462 N APHE A 57 -4.402 3.717 19.736 0.50 16.00 N
ANISOU 462 N APHE A 57 3437 1797 845 -47 460 173 N
ATOM 463 N BPHE A 57 -4.680 3.605 19.781 0.50 15.88 N
ANISOU 463 N BPHE A 57 3455 1604 974 -99 233 267 N
ATOM 464 CA APHE A 57 -3.819 4.236 21.000 0.50 16.58 C
ANISOU 464 CA APHE A 57 3378 1943 979 -51 411 130 C
ATOM 465 CA BPHE A 57 -4.274 4.262 21.026 0.50 15.66 C
ANISOU 465 CA BPHE A 57 3384 1719 844 -132 292 247 C
ATOM 466 C APHE A 57 -4.154 5.721 21.163 0.50 16.50 C
ANISOU 466 C APHE A 57 3389 1874 1003 -26 534 195 C
ATOM 467 C BPHE A 57 -4.595 5.750 20.979 0.50 15.27 C
ANISOU 467 C BPHE A 57 3275 1757 770 -55 333 275 C
ATOM 468 O APHE A 57 -4.810 6.133 22.129 0.50 16.78 O
ANISOU 468 O APHE A 57 3581 1976 817 -58 583 108 O
ATOM 469 O BPHE A 57 -5.631 6.154 21.484 0.50 16.74 O
ANISOU 469 O BPHE A 57 3233 1875 1249 -45 363 498 O
ATOM 470 CB APHE A 57 -2.278 4.025 21.086 0.50 17.06 C
ANISOU 470 CB APHE A 57 3483 1997 1001 -4 362 175 C
ATOM 471 CB BPHE A 57 -2.764 4.055 21.300 0.50 15.93 C
ANISOU 471 CB BPHE A 57 3479 1747 825 10 322 299 C
ATOM 472 CG APHE A 57 -1.599 4.801 22.199 0.50 18.62 C
ANISOU 472 CG APHE A 57 3407 2151 1514 58 255 176 C
ATOM 473 CG BPHE A 57 -2.217 4.883 22.451 0.50 17.75 C
ANISOU 473 CG BPHE A 57 3702 2160 881 48 103 426 C
ATOM 474 CD1APHE A 57 -2.050 4.732 23.497 0.50 18.03 C
ANISOU 474 CD1APHE A 57 3130 2152 1568 5 209 160 C
ATOM 475 CD1BPHE A 57 -2.856 4.919 23.662 0.50 18.26 C
ANISOU 475 CD1BPHE A 57 3848 2218 872 44 24 223 C
ATOM 476 CD2APHE A 57 -0.505 5.609 21.920 0.50 19.66 C
ANISOU 476 CD2APHE A 57 3547 2203 1718 -32 306 347 C
ATOM 477 CD2BPHE A 57 -1.051 5.637 22.292 0.50 19.16 C
ANISOU 477 CD2BPHE A 57 3499 2453 1324 67 -111 278 C
ATOM 478 CE1APHE A 57 -1.419 5.449 24.486 0.50 19.24 C
ANISOU 478 CE1APHE A 57 3162 2526 1620 -64 138 147 C
ATOM 479 CE1BPHE A 57 -2.353 5.707 24.713 0.50 20.84 C
ANISOU 479 CE1BPHE A 57 3745 2675 1497 56 -470 181 C
ATOM 480 CE2APHE A 57 0.133 6.325 22.910 0.50 19.25 C
ANISOU 480 CE2APHE A 57 3520 2272 1520 -27 378 783 C
ATOM 481 CE2BPHE A 57 -0.556 6.411 23.330 0.50 20.63 C
ANISOU 481 CE2BPHE A 57 3716 2584 1538 307 -320 493 C
ATOM 482 CZ APHE A 57 -0.332 6.257 24.189 0.50 19.24 C
ANISOU 482 CZ APHE A 57 3340 2465 1503 72 241 357 C
ATOM 483 CZ BPHE A 57 -1.209 6.441 24.529 0.50 20.42 C
ANISOU 483 CZ BPHE A 57 3841 2379 1539 187 -357 555 C
ATOM 484 N ALYS A 58 -3.709 6.541 20.224 0.50 16.85 N
ANISOU 484 N ALYS A 58 3292 1781 1327 -31 580 250 N
ATOM 485 N BLYS A 58 -3.698 6.572 20.418 0.50 15.79 N
ANISOU 485 N BLYS A 58 3131 1708 1159 -56 349 264 N
ATOM 486 CA ALYS A 58 -3.938 7.993 20.304 0.50 16.58 C
ANISOU 486 CA ALYS A 58 3047 1836 1416 -63 503 229 C
ATOM 487 CA BLYS A 58 -3.912 8.053 20.355 0.50 16.04 C
ANISOU 487 CA BLYS A 58 2960 1877 1255 -106 320 111 C
ATOM 488 C ALYS A 58 -3.593 8.565 18.939 0.50 16.64 C
ANISOU 488 C ALYS A 58 2954 1907 1458 -93 615 202 C
ATOM 489 C BLYS A 58 -3.557 8.673 19.013 0.50 15.63 C
ANISOU 489 C BLYS A 58 2837 1912 1189 -205 414 43 C
ATOM 490 O ALYS A 58 -2.519 8.291 18.420 0.50 19.47 O
ANISOU 490 O ALYS A 58 3279 2200 1916 164 621 405 O
ATOM 491 O BLYS A 58 -2.384 8.680 18.673 0.50 14.74 O
ANISOU 491 O BLYS A 58 2917 1861 823 -376 94 -172 O
ATOM 492 CB ALYS A 58 -3.113 8.620 21.467 0.50 16.71 C
ANISOU 492 CB ALYS A 58 2996 1828 1525 -154 389 238 C
ATOM 493 CB BLYS A 58 -3.066 8.786 21.411 0.50 17.19 C
ANISOU 493 CB BLYS A 58 2948 1991 1592 -146 223 85 C
ATOM 494 CG ALYS A 58 -3.220 10.144 21.607 0.50 15.35 C
ANISOU 494 CG ALYS A 58 2902 1717 1213 -238 268 191 C
ATOM 495 CG BLYS A 58 -3.164 8.273 22.779 0.50 20.95 C
ANISOU 495 CG BLYS A 58 3311 2724 1925 -79 160 72 C
ATOM 496 CD ALYS A 58 -4.602 10.495 22.071 0.50 17.30 C
ANISOU 496 CD ALYS A 58 3003 2039 1529 -143 90 -215 C
ATOM 497 CD BLYS A 58 -4.383 8.792 23.448 0.50 23.29 C
ANISOU 497 CD BLYS A 58 3380 3199 2269 -79 178 -53 C
ATOM 498 CE ALYS A 58 -4.901 11.990 21.946 0.50 19.71 C
ANISOU 498 CE ALYS A 58 3137 2365 1984 -74 61 -9 C
ATOM 499 CE BLYS A 58 -4.622 8.013 24.713 0.50 23.47 C
ANISOU 499 CE BLYS A 58 3273 3664 1979 24 272 -54 C
ATOM 500 NZ ALYS A 58 -5.358 12.327 20.539 0.50 22.60 N1+
ANISOU 500 NZ ALYS A 58 3782 2813 1991 88 194 79 N1+
ATOM 501 NZ BLYS A 58 -4.757 8.948 25.862 0.50 25.11 N1+
ANISOU 501 NZ BLYS A 58 3812 4064 1663 -24 305 8 N1+
ATOM 502 N ASN A 59 -4.549 9.292 18.350 1.00 15.05 N
ANISOU 502 N ASN A 59 2689 1755 1271 -204 688 179 N
ATOM 503 CA ASN A 59 -4.318 9.981 17.084 1.00 14.87 C
ANISOU 503 CA ASN A 59 2749 1609 1293 -188 695 -17 C
ATOM 504 C ASN A 59 -3.531 11.225 17.364 1.00 15.15 C
ANISOU 504 C ASN A 59 3054 1519 1181 -220 647 -62 C
ATOM 505 O ASN A 59 -3.755 11.918 18.363 1.00 17.57 O
ANISOU 505 O ASN A 59 3400 1750 1526 -311 964 -276 O
ATOM 506 CB ASN A 59 -5.638 10.367 16.456 1.00 15.99 C
ANISOU 506 CB ASN A 59 2998 1731 1344 -40 504 232 C
ATOM 507 CG ASN A 59 -6.538 9.185 16.121 1.00 18.22 C
ANISOU 507 CG ASN A 59 2607 2433 1882 -19 199 85 C
ATOM 508 ND2 ASN A 59 -7.834 9.283 16.486 1.00 24.00 N
ANISOU 508 ND2 ASN A 59 3035 3122 2962 41 561 11 N
ATOM 509 OD1 ASN A 59 -6.105 8.214 15.557 1.00 16.55 O
ANISOU 509 OD1 ASN A 59 2744 1935 1609 -4 403 237 O
ATOM 510 N THR A 60 -2.604 11.526 16.462 1.00 13.31 N
ANISOU 510 N THR A 60 2839 1429 788 -246 578 50 N
ATOM 511 CA THR A 60 -1.828 12.732 16.582 1.00 13.23 C
ANISOU 511 CA THR A 60 2852 1494 679 -184 507 -5 C
ATOM 512 C THR A 60 -1.709 13.365 15.210 1.00 11.87 C
ANISOU 512 C THR A 60 2572 1318 619 -145 402 34 C
ATOM 513 O THR A 60 -1.765 12.679 14.184 1.00 12.53 O
ANISOU 513 O THR A 60 2774 1333 651 -188 343 -29 O
ATOM 514 CB THR A 60 -0.385 12.458 17.148 1.00 13.70 C
ANISOU 514 CB THR A 60 2911 1586 707 -194 344 -3 C
ATOM 515 CG2 THR A 60 -0.378 11.897 18.598 1.00 16.21 C
ANISOU 515 CG2 THR A 60 3386 1872 898 -217 350 149 C
ATOM 516 OG1 THR A 60 0.369 11.624 16.281 1.00 14.42 O
ANISOU 516 OG1 THR A 60 2838 1750 888 -56 242 130 O
ATOM 517 N GLU A 61 -1.412 14.654 15.189 1.00 12.20 N
ANISOU 517 N GLU A 61 2752 1195 687 -217 353 -26 N
ATOM 518 CA GLU A 61 -1.105 15.359 13.933 1.00 12.38 C
ANISOU 518 CA GLU A 61 2558 1381 764 -158 285 -13 C
ATOM 519 C GLU A 61 -0.200 16.509 14.237 1.00 12.23 C
ANISOU 519 C GLU A 61 2663 1310 672 -114 275 -76 C
ATOM 520 O GLU A 61 -0.477 17.285 15.187 1.00 14.29 O
ANISOU 520 O GLU A 61 2978 1504 945 -143 573 -259 O
ATOM 521 CB GLU A 61 -2.395 15.811 13.274 1.00 15.10 C
ANISOU 521 CB GLU A 61 2769 1719 1249 -193 222 128 C
ATOM 522 CG GLU A 61 -2.246 16.495 11.993 1.00 18.90 C
ANISOU 522 CG GLU A 61 2861 2565 1754 -156 10 752 C
ATOM 523 CD GLU A 61 -3.544 17.039 11.453 1.00 25.91 C
ANISOU 523 CD GLU A 61 2978 3753 3112 -146 19 1062 C
ATOM 524 OE1 GLU A 61 -3.485 18.099 10.840 1.00 29.53 O
ANISOU 524 OE1 GLU A 61 3026 4271 3920 -407 -397 1361 O
ATOM 525 OE2 GLU A 61 -4.604 16.426 11.649 1.00 31.17 O1-
ANISOU 525 OE2 GLU A 61 3257 4654 3932 -416 -304 931 O1-
ATOM 526 N ILE A 62 0.928 16.600 13.536 1.00 10.31 N
ANISOU 526 N ILE A 62 2454 1181 281 -230 166 -36 N
ATOM 527 CA ILE A 62 1.799 17.727 13.612 1.00 10.26 C
ANISOU 527 CA ILE A 62 2451 1165 282 -151 74 -27 C
ATOM 528 C ILE A 62 1.997 18.325 12.226 1.00 9.90 C
ANISOU 528 C ILE A 62 2270 1230 260 -264 97 38 C
ATOM 529 O ILE A 62 2.100 17.589 11.240 1.00 11.35 O
ANISOU 529 O ILE A 62 2833 1215 264 -294 90 -96 O
ATOM 530 CB ILE A 62 3.154 17.362 14.245 1.00 10.78 C
ANISOU 530 CB ILE A 62 2557 1283 254 -278 -39 -24 C
ATOM 531 CG1 ILE A 62 3.910 16.276 13.506 1.00 11.87 C
ANISOU 531 CG1 ILE A 62 2459 1515 536 -218 -57 12 C
ATOM 532 CG2 ILE A 62 2.949 16.932 15.734 1.00 13.36 C
ANISOU 532 CG2 ILE A 62 2884 1899 290 6 91 238 C
ATOM 533 CD1 ILE A 62 5.323 16.051 13.976 1.00 13.97 C
ANISOU 533 CD1 ILE A 62 2434 1856 1018 -51 -282 -81 C
ATOM 534 N SER A 63 2.040 19.644 12.176 1.00 9.83 N
ANISOU 534 N SER A 63 2343 1128 262 -56 131 22 N
ATOM 535 CA SER A 63 2.407 20.388 10.962 1.00 9.10 C
ANISOU 535 CA SER A 63 2098 1105 253 -74 27 -4 C
ATOM 536 C SER A 63 3.513 21.336 11.294 1.00 9.52 C
ANISOU 536 C SER A 63 2117 1010 488 -31 39 -28 C
ATOM 537 O SER A 63 3.498 21.955 12.388 1.00 10.67 O
ANISOU 537 O SER A 63 2362 1167 524 -122 167 -233 O
ATOM 538 CB SER A 63 1.238 21.164 10.404 1.00 10.21 C
ANISOU 538 CB SER A 63 2234 1349 296 24 61 -74 C
ATOM 539 OG SER A 63 0.205 20.311 9.912 1.00 12.87 O
ANISOU 539 OG SER A 63 2493 1698 696 -46 -189 -47 O
ATOM 540 N PHE A 64 4.508 21.453 10.429 1.00 9.04 N
ANISOU 540 N PHE A 64 2110 1067 256 -165 13 -54 N
ATOM 541 CA PHE A 64 5.706 22.172 10.763 1.00 9.35 C
ANISOU 541 CA PHE A 64 2175 1123 255 -99 -13 -46 C
ATOM 542 C PHE A 64 6.435 22.606 9.496 1.00 8.77 C
ANISOU 542 C PHE A 64 2186 891 255 -111 -40 29 C
ATOM 543 O PHE A 64 6.206 22.058 8.402 1.00 9.65 O
ANISOU 543 O PHE A 64 2239 1161 263 -124 -107 -58 O
ATOM 544 CB PHE A 64 6.618 21.331 11.673 1.00 9.96 C
ANISOU 544 CB PHE A 64 2252 1178 354 -205 -35 118 C
ATOM 545 CG PHE A 64 6.968 20.016 11.051 1.00 9.44 C
ANISOU 545 CG PHE A 64 2185 1132 267 -23 -152 -10 C
ATOM 546 CD1 PHE A 64 6.181 18.887 11.191 1.00 9.75 C
ANISOU 546 CD1 PHE A 64 2156 1230 317 -65 -108 19 C
ATOM 547 CD2 PHE A 64 8.100 19.879 10.295 1.00 9.85 C
ANISOU 547 CD2 PHE A 64 2237 1108 397 21 -78 134 C
ATOM 548 CE1 PHE A 64 6.459 17.712 10.590 1.00 11.29 C
ANISOU 548 CE1 PHE A 64 2460 1373 457 -80 -315 -15 C
ATOM 549 CE2 PHE A 64 8.388 18.670 9.691 1.00 11.32 C
ANISOU 549 CE2 PHE A 64 2351 1663 287 125 16 220 C
ATOM 550 CZ PHE A 64 7.586 17.584 9.838 1.00 11.37 C
ANISOU 550 CZ PHE A 64 2603 1374 340 9 -231 4 C
ATOM 551 N ILE A 65 7.341 23.528 9.695 1.00 9.17 N
ANISOU 551 N ILE A 65 2159 1069 253 -124 3 4 N
ATOM 552 CA ILE A 65 8.299 23.992 8.711 1.00 9.29 C
ANISOU 552 CA ILE A 65 2183 1071 274 -40 20 -34 C
ATOM 553 C ILE A 65 9.702 23.561 9.171 1.00 9.02 C
ANISOU 553 C ILE A 65 2119 1025 281 5 -26 103 C
ATOM 554 O ILE A 65 10.010 23.665 10.369 1.00 9.48 O
ANISOU 554 O ILE A 65 2242 1048 311 -58 -63 -2 O
ATOM 555 CB ILE A 65 8.222 25.532 8.501 1.00 9.88 C
ANISOU 555 CB ILE A 65 2193 1023 536 -9 -6 -9 C
ATOM 556 CG1 ILE A 65 6.829 25.836 7.940 1.00 11.43 C
ANISOU 556 CG1 ILE A 65 2385 1268 690 -25 -102 216 C
ATOM 557 CG2 ILE A 65 9.347 26.020 7.639 1.00 11.05 C
ANISOU 557 CG2 ILE A 65 2510 1214 474 33 100 172 C
ATOM 558 CD1 ILE A 65 6.511 27.361 7.880 1.00 15.94 C
ANISOU 558 CD1 ILE A 65 2877 1413 1764 211 -107 56 C
ATOM 559 N LEU A 66 10.508 22.982 8.284 1.00 9.22 N
ANISOU 559 N LEU A 66 2184 1046 270 44 153 61 N
ATOM 560 CA LEU A 66 11.801 22.513 8.672 1.00 9.55 C
ANISOU 560 CA LEU A 66 2207 1057 364 18 136 131 C
ATOM 561 C LEU A 66 12.569 23.643 9.339 1.00 9.26 C
ANISOU 561 C LEU A 66 2156 1016 344 10 12 95 C
ATOM 562 O LEU A 66 12.643 24.766 8.831 1.00 10.37 O
ANISOU 562 O LEU A 66 2276 1071 594 -60 -28 164 O
ATOM 563 CB LEU A 66 12.574 21.950 7.467 1.00 10.34 C
ANISOU 563 CB LEU A 66 2199 1327 402 45 153 99 C
ATOM 564 CG LEU A 66 11.945 20.694 6.818 1.00 10.78 C
ANISOU 564 CG LEU A 66 2497 1201 398 16 -34 -222 C
ATOM 565 CD1 LEU A 66 12.640 20.425 5.481 1.00 15.08 C
ANISOU 565 CD1 LEU A 66 3338 1590 802 204 310 -277 C
ATOM 566 CD2 LEU A 66 12.054 19.533 7.745 1.00 12.90 C
ANISOU 566 CD2 LEU A 66 2865 1094 939 -125 -109 64 C
ATOM 567 N GLY A 67 13.235 23.300 10.426 1.00 9.74 N
ANISOU 567 N GLY A 67 2196 1103 402 -82 -76 87 N
ATOM 568 CA GLY A 67 14.079 24.209 11.158 1.00 10.16 C
ANISOU 568 CA GLY A 67 2156 1240 461 -17 -92 45 C
ATOM 569 C GLY A 67 13.396 25.151 12.123 1.00 9.61 C
ANISOU 569 C GLY A 67 2112 1088 448 -49 -123 25 C
ATOM 570 O GLY A 67 14.083 25.884 12.830 1.00 10.65 O
ANISOU 570 O GLY A 67 2161 1358 524 -122 -158 -101 O
ATOM 571 N GLN A 68 12.076 25.106 12.197 1.00 9.30 N
ANISOU 571 N GLN A 68 2148 961 424 -122 -122 -113 N
ATOM 572 CA GLN A 68 11.268 26.063 12.961 1.00 9.93 C
ANISOU 572 CA GLN A 68 2200 1004 568 -116 -156 -124 C
ATOM 573 C GLN A 68 10.540 25.370 14.128 1.00 9.96 C
ANISOU 573 C GLN A 68 2233 948 602 25 -83 -99 C
ATOM 574 O GLN A 68 9.657 24.515 13.910 1.00 9.80 O
ANISOU 574 O GLN A 68 2189 1027 507 -65 -25 -164 O
ATOM 575 CB GLN A 68 10.273 26.752 12.035 1.00 10.29 C
ANISOU 575 CB GLN A 68 2383 889 636 -74 -158 -59 C
ATOM 576 CG GLN A 68 11.017 27.465 10.925 1.00 13.30 C
ANISOU 576 CG GLN A 68 2811 1369 872 -190 -495 154 C
ATOM 577 CD GLN A 68 10.270 28.457 10.131 1.00 15.44 C
ANISOU 577 CD GLN A 68 3368 1306 1190 -75 -639 217 C
ATOM 578 NE2 GLN A 68 10.966 29.016 9.150 1.00 16.72 N
ANISOU 578 NE2 GLN A 68 4059 1303 991 -312 -563 406 N
ATOM 579 OE1 GLN A 68 9.091 28.743 10.407 1.00 18.75 O
ANISOU 579 OE1 GLN A 68 3440 1372 2311 137 -1054 371 O
ATOM 580 N GLU A 69 10.934 25.715 15.335 1.00 9.35 N
ANISOU 580 N GLU A 69 2215 980 357 -90 -101 -131 N
ATOM 581 CA GLU A 69 10.432 25.059 16.536 1.00 10.30 C
ANISOU 581 CA GLU A 69 2361 1050 502 6 6 179 C
ATOM 582 C GLU A 69 8.936 25.208 16.677 1.00 9.61 C
ANISOU 582 C GLU A 69 2370 987 295 14 68 -78 C
ATOM 583 O GLU A 69 8.388 26.273 16.321 1.00 10.57 O
ANISOU 583 O GLU A 69 2309 910 796 65 -66 -25 O
ATOM 584 CB GLU A 69 11.140 25.640 17.776 1.00 12.46 C
ANISOU 584 CB GLU A 69 2446 1786 502 -15 -61 173 C
ATOM 585 CG GLU A 69 10.837 25.032 19.080 1.00 15.74 C
ANISOU 585 CG GLU A 69 3382 1786 812 -299 -157 179 C
ATOM 586 CD GLU A 69 11.775 25.499 20.099 1.00 24.08 C
ANISOU 586 CD GLU A 69 4365 3400 1384 -169 -669 -68 C
ATOM 587 OE1 GLU A 69 11.717 26.713 20.399 1.00 31.87 O
ANISOU 587 OE1 GLU A 69 5206 4493 2409 -1043 -1098 -1144 O
ATOM 588 OE2 GLU A 69 12.566 24.630 20.597 1.00 26.40 O1-
ANISOU 588 OE2 GLU A 69 4681 3721 1625 48 -1029 -309 O1-
ATOM 589 N PHE A 70 8.296 24.185 17.219 1.00 9.52 N
ANISOU 589 N PHE A 70 2299 933 384 -29 102 -16 N
ATOM 590 CA PHE A 70 6.880 24.191 17.455 1.00 9.76 C
ANISOU 590 CA PHE A 70 2297 993 418 50 136 -50 C
ATOM 591 C PHE A 70 6.559 23.415 18.724 1.00 9.88 C
ANISOU 591 C PHE A 70 2341 918 491 147 248 -53 C
ATOM 592 O PHE A 70 7.344 22.627 19.215 1.00 10.78 O
ANISOU 592 O PHE A 70 2370 1263 460 365 133 46 O
ATOM 593 CB PHE A 70 6.123 23.598 16.254 1.00 9.57 C
ANISOU 593 CB PHE A 70 2173 1060 403 117 59 -37 C
ATOM 594 CG PHE A 70 6.475 22.174 15.908 1.00 9.86 C
ANISOU 594 CG PHE A 70 2317 1172 255 -38 0 46 C
ATOM 595 CD1 PHE A 70 7.584 21.875 15.133 1.00 9.16 C
ANISOU 595 CD1 PHE A 70 2127 1093 258 29 54 -57 C
ATOM 596 CD2 PHE A 70 5.687 21.133 16.318 1.00 11.31 C
ANISOU 596 CD2 PHE A 70 2371 1412 514 -29 277 -187 C
ATOM 597 CE1 PHE A 70 7.870 20.594 14.765 1.00 9.82 C
ANISOU 597 CE1 PHE A 70 2321 1140 269 36 -14 -52 C
ATOM 598 CE2 PHE A 70 5.998 19.838 15.966 1.00 11.83 C
ANISOU 598 CE2 PHE A 70 2626 1410 457 -207 195 -110 C
ATOM 599 CZ PHE A 70 7.079 19.553 15.210 1.00 10.49 C
ANISOU 599 CZ PHE A 70 2431 1268 287 137 -22 -184 C
ATOM 600 N ASP A 71 5.346 23.631 19.217 1.00 10.87 N
ANISOU 600 N ASP A 71 2315 1093 720 339 269 186 N
ATOM 601 CA ASP A 71 4.788 22.904 20.382 1.00 11.52 C
ANISOU 601 CA ASP A 71 2562 1369 444 204 430 74 C
ATOM 602 C ASP A 71 4.111 21.657 19.906 1.00 12.04 C
ANISOU 602 C ASP A 71 2577 1534 461 43 289 97 C
ATOM 603 O ASP A 71 3.398 21.623 18.860 1.00 14.01 O
ANISOU 603 O ASP A 71 2741 1625 954 167 139 337 O
ATOM 604 CB ASP A 71 3.702 23.741 21.037 1.00 12.78 C
ANISOU 604 CB ASP A 71 2598 1667 590 313 278 47 C
ATOM 605 CG ASP A 71 4.222 24.948 21.649 1.00 14.19 C
ANISOU 605 CG ASP A 71 2834 2108 450 226 -234 -306 C
ATOM 606 OD1 ASP A 71 5.202 24.813 22.442 1.00 14.99 O
ANISOU 606 OD1 ASP A 71 3161 1795 738 308 -223 -297 O
ATOM 607 OD2 ASP A 71 3.634 26.040 21.445 1.00 14.87 O1-
ANISOU 607 OD2 ASP A 71 2880 1854 916 259 -152 -15 O1-
ATOM 608 N GLU A 72 4.363 20.554 20.633 1.00 12.19 N
ANISOU 608 N GLU A 72 2577 1409 645 129 354 298 N
ATOM 609 CA GLU A 72 3.807 19.239 20.276 1.00 12.71 C
ANISOU 609 CA GLU A 72 2417 1504 906 107 250 322 C
ATOM 610 C GLU A 72 3.315 18.572 21.545 1.00 12.97 C
ANISOU 610 C GLU A 72 2573 1383 971 161 158 367 C
ATOM 611 O GLU A 72 3.995 18.597 22.566 1.00 14.84 O
ANISOU 611 O GLU A 72 2865 2017 754 -58 346 387 O
ATOM 612 CB GLU A 72 4.900 18.373 19.581 1.00 12.12 C
ANISOU 612 CB GLU A 72 2479 1425 698 94 321 254 C
ATOM 613 CG GLU A 72 4.498 16.939 19.298 1.00 12.61 C
ANISOU 613 CG GLU A 72 2695 1578 517 100 59 345 C
ATOM 614 CD GLU A 72 5.544 16.120 18.600 1.00 12.45 C
ANISOU 614 CD GLU A 72 2747 1548 436 85 239 91 C
ATOM 615 OE1 GLU A 72 6.688 16.541 18.514 1.00 12.73 O
ANISOU 615 OE1 GLU A 72 2549 1513 774 -30 144 -26 O
ATOM 616 OE2 GLU A 72 5.210 14.990 18.154 1.00 14.37 O1-
ANISOU 616 OE2 GLU A 72 2844 1593 1021 1 108 -18 O1-
ATOM 617 N VAL A 73 2.130 18.000 21.505 1.00 14.77 N
ANISOU 617 N VAL A 73 2617 1739 1256 57 289 583 N
ATOM 618 CA VAL A 73 1.686 17.151 22.613 1.00 15.39 C
ANISOU 618 CA VAL A 73 2474 1839 1532 67 384 539 C
ATOM 619 C VAL A 73 1.766 15.719 22.043 1.00 14.89 C
ANISOU 619 C VAL A 73 2514 1915 1228 64 241 534 C
ATOM 620 O VAL A 73 1.071 15.362 21.106 1.00 15.98 O
ANISOU 620 O VAL A 73 2751 1820 1497 -59 -70 534 O
ATOM 621 CB VAL A 73 0.277 17.522 23.083 1.00 16.57 C
ANISOU 621 CB VAL A 73 2703 2044 1548 64 610 432 C
ATOM 622 CG1 VAL A 73 -0.170 16.563 24.194 1.00 18.94 C
ANISOU 622 CG1 VAL A 73 2882 2429 1885 118 803 575 C
ATOM 623 CG2 VAL A 73 0.221 18.957 23.605 1.00 18.86 C
ANISOU 623 CG2 VAL A 73 2871 1944 2350 359 650 243 C
ATOM 624 N THR A 74 2.649 14.912 22.582 1.00 13.43 N
ANISOU 624 N THR A 74 2498 1994 608 230 216 398 N
ATOM 625 CA THR A 74 2.939 13.606 22.039 1.00 13.31 C
ANISOU 625 CA THR A 74 2541 1890 624 96 284 318 C
ATOM 626 C THR A 74 1.811 12.611 22.353 1.00 13.92 C
ANISOU 626 C THR A 74 2562 1961 765 132 189 373 C
ATOM 627 O THR A 74 0.969 12.889 23.172 1.00 14.74 O
ANISOU 627 O THR A 74 2828 1817 954 103 437 441 O
ATOM 628 CB THR A 74 4.263 13.045 22.561 1.00 12.09 C
ANISOU 628 CB THR A 74 2401 1867 325 111 303 222 C
ATOM 629 CG2 THR A 74 5.378 14.012 22.348 1.00 13.24 C
ANISOU 629 CG2 THR A 74 2760 1648 620 52 278 233 C
ATOM 630 OG1 THR A 74 4.122 12.814 23.969 1.00 13.17 O
ANISOU 630 OG1 THR A 74 2627 1909 465 239 222 337 O
ATOM 631 N ALA A 75 1.848 11.450 21.707 1.00 14.54 N
ANISOU 631 N ALA A 75 2682 2025 818 -46 311 333 N
ATOM 632 CA ALA A 75 0.801 10.416 21.869 1.00 14.45 C
ANISOU 632 CA ALA A 75 2667 1955 867 -74 126 279 C
ATOM 633 C ALA A 75 0.683 10.021 23.367 1.00 15.56 C
ANISOU 633 C ALA A 75 2695 2060 1157 -180 235 273 C
ATOM 634 O ALA A 75 -0.417 9.758 23.835 1.00 17.13 O
ANISOU 634 O ALA A 75 3020 2321 1165 -229 369 376 O
ATOM 635 CB ALA A 75 1.066 9.203 21.029 1.00 15.31 C
ANISOU 635 CB ALA A 75 2761 1958 1099 -160 78 169 C
ATOM 636 N ASP A 76 1.812 9.961 24.064 1.00 14.96 N
ANISOU 636 N ASP A 76 2867 1865 950 -94 257 436 N
ATOM 637 CA ASP A 76 1.854 9.635 25.520 1.00 15.20 C
ANISOU 637 CA ASP A 76 2905 2004 867 -220 221 426 C
ATOM 638 C ASP A 76 1.630 10.854 26.427 1.00 16.03 C
ANISOU 638 C ASP A 76 3145 2057 888 -190 425 448 C
ATOM 639 O ASP A 76 1.766 10.757 27.627 1.00 18.58 O
ANISOU 639 O ASP A 76 3650 2642 767 -19 360 492 O
ATOM 640 CB ASP A 76 3.180 8.927 25.824 1.00 15.92 C
ANISOU 640 CB ASP A 76 3059 1958 1029 -175 244 343 C
ATOM 641 CG ASP A 76 4.395 9.772 25.538 1.00 14.71 C
ANISOU 641 CG ASP A 76 2960 1830 798 -6 -219 268 C
ATOM 642 OD1 ASP A 76 4.582 10.204 24.365 1.00 14.41 O
ANISOU 642 OD1 ASP A 76 3149 1843 482 -92 -89 421 O
ATOM 643 OD2 ASP A 76 5.152 10.002 26.490 1.00 14.80 O1-
ANISOU 643 OD2 ASP A 76 3410 1618 595 -42 -2 336 O1-
ATOM 644 N ASP A 77 1.288 11.997 25.843 1.00 15.94 N
ANISOU 644 N ASP A 77 3142 2066 847 -122 626 338 N
ATOM 645 CA ASP A 77 0.864 13.190 26.577 1.00 17.86 C
ANISOU 645 CA ASP A 77 3232 2357 1198 -96 767 226 C
ATOM 646 C ASP A 77 2.000 14.008 27.174 1.00 17.68 C
ANISOU 646 C ASP A 77 3318 2283 1117 -36 644 159 C
ATOM 647 O ASP A 77 1.780 14.758 28.123 1.00 20.25 O
ANISOU 647 O ASP A 77 3525 2606 1563 -19 852 -322 O
ATOM 648 CB ASP A 77 -0.271 12.944 27.589 1.00 19.18 C
ANISOU 648 CB ASP A 77 3389 2486 1411 -175 937 273 C
ATOM 649 CG ASP A 77 -1.167 14.156 27.791 1.00 23.75 C
ANISOU 649 CG ASP A 77 3774 3211 2037 -54 1089 228 C
ATOM 650 OD1 ASP A 77 -1.694 14.273 28.912 1.00 30.29 O
ANISOU 650 OD1 ASP A 77 4566 4191 2752 252 1686 -157 O
ATOM 651 OD2 ASP A 77 -1.393 14.961 26.859 1.00 29.24 O1-
ANISOU 651 OD2 ASP A 77 4453 3955 2698 -35 1229 585 O1-
ATOM 652 N ARG A 78 3.192 13.946 26.604 1.00 15.25 N
ANISOU 652 N ARG A 78 3199 1853 743 53 590 329 N
ATOM 653 CA ARG A 78 4.213 14.896 26.948 1.00 14.82 C
ANISOU 653 CA ARG A 78 3165 1873 592 72 460 217 C
ATOM 654 C ARG A 78 3.967 16.176 26.178 1.00 14.42 C
ANISOU 654 C ARG A 78 3212 1782 485 152 472 215 C
ATOM 655 O ARG A 78 3.609 16.142 25.014 1.00 15.50 O
ANISOU 655 O ARG A 78 3487 1624 777 186 314 169 O
ATOM 656 CB ARG A 78 5.615 14.410 26.654 1.00 13.78 C
ANISOU 656 CB ARG A 78 3176 1521 538 55 319 266 C
ATOM 657 CG ARG A 78 6.119 13.312 27.534 1.00 13.52 C
ANISOU 657 CG ARG A 78 3091 1396 649 51 307 127 C
ATOM 658 CD ARG A 78 7.422 12.710 27.025 1.00 13.57 C
ANISOU 658 CD ARG A 78 3195 1554 407 4 10 168 C
ATOM 659 NE ARG A 78 7.150 11.854 25.887 1.00 12.99 N
ANISOU 659 NE ARG A 78 3058 1398 477 119 -121 158 N
ATOM 660 CZ ARG A 78 7.715 11.914 24.678 1.00 12.77 C
ANISOU 660 CZ ARG A 78 2650 1485 714 231 -66 45 C
ATOM 661 NH1 ARG A 78 8.775 12.686 24.439 1.00 13.13 N1+
ANISOU 661 NH1 ARG A 78 2869 1629 488 -73 -86 127 N1+
ATOM 662 NH2 ARG A 78 7.286 11.086 23.732 1.00 12.38 N
ANISOU 662 NH2 ARG A 78 2734 1314 654 -33 -121 21 N
ATOM 663 N LYS A 79 4.207 17.309 26.811 1.00 14.87 N
ANISOU 663 N LYS A 79 3327 1817 505 214 593 166 N
ATOM 664 CA LYS A 79 4.179 18.623 26.180 1.00 15.03 C
ANISOU 664 CA LYS A 79 3104 1772 833 355 521 138 C
ATOM 665 C LYS A 79 5.618 18.991 25.888 1.00 13.93 C
ANISOU 665 C LYS A 79 3028 1503 761 320 329 125 C
ATOM 666 O LYS A 79 6.417 19.269 26.792 1.00 16.10 O
ANISOU 666 O LYS A 79 3473 2222 421 309 523 -43 O
ATOM 667 CB LYS A 79 3.473 19.640 27.055 1.00 16.85 C
ANISOU 667 CB LYS A 79 3434 1944 1022 371 521 207 C
ATOM 668 CG LYS A 79 2.121 19.214 27.572 1.00 22.73 C
ANISOU 668 CG LYS A 79 3543 2705 2388 593 711 -29 C
ATOM 669 CD LYS A 79 1.041 18.792 26.626 1.00 28.57 C
ANISOU 669 CD LYS A 79 4101 3442 3311 393 573 -66 C
ATOM 670 CE LYS A 79 -0.304 18.536 27.357 1.00 31.76 C
ANISOU 670 CE LYS A 79 4325 3850 3892 289 550 49 C
ATOM 671 NZ LYS A 79 -0.289 17.377 28.302 1.00 33.42 N1+
ANISOU 671 NZ LYS A 79 4837 4131 3729 309 511 157 N1+
ATOM 672 N VAL A 80 5.991 18.955 24.608 1.00 12.54 N
ANISOU 672 N VAL A 80 2873 1538 353 243 242 46 N
ATOM 673 CA VAL A 80 7.372 19.084 24.226 1.00 11.96 C
ANISOU 673 CA VAL A 80 2807 1395 339 216 102 69 C
ATOM 674 C VAL A 80 7.545 20.244 23.221 1.00 11.33 C
ANISOU 674 C VAL A 80 2755 1254 294 301 181 -137 C
ATOM 675 O VAL A 80 6.575 20.684 22.593 1.00 12.65 O
ANISOU 675 O VAL A 80 2866 1377 561 313 311 132 O
ATOM 676 CB VAL A 80 7.909 17.746 23.579 1.00 12.12 C
ANISOU 676 CB VAL A 80 2855 1184 564 184 168 30 C
ATOM 677 CG1 VAL A 80 7.606 16.543 24.482 1.00 13.28 C
ANISOU 677 CG1 VAL A 80 3409 1184 450 237 110 236 C
ATOM 678 CG2 VAL A 80 7.304 17.490 22.194 1.00 12.63 C
ANISOU 678 CG2 VAL A 80 3213 1327 259 68 128 -14 C
ATOM 679 N LYS A 81 8.782 20.681 23.119 1.00 11.33 N
ANISOU 679 N LYS A 81 2840 1139 326 175 83 -24 N
ATOM 680 CA LYS A 81 9.180 21.655 22.095 1.00 11.42 C
ANISOU 680 CA LYS A 81 2920 969 450 269 48 5 C
ATOM 681 C LYS A 81 9.975 20.875 21.077 1.00 10.67 C
ANISOU 681 C LYS A 81 2651 1004 398 111 94 -128 C
ATOM 682 O LYS A 81 10.993 20.274 21.420 1.00 11.39 O
ANISOU 682 O LYS A 81 2719 1295 310 247 -143 -125 O
ATOM 683 CB LYS A 81 10.049 22.733 22.728 1.00 13.42 C
ANISOU 683 CB LYS A 81 3275 1149 674 46 221 14 C
ATOM 684 CG LYS A 81 9.405 23.579 23.735 1.00 19.38 C
ANISOU 684 CG LYS A 81 3782 1992 1588 162 -25 -552 C
ATOM 685 CD LYS A 81 8.374 24.486 23.195 1.00 22.36 C
ANISOU 685 CD LYS A 81 4020 2569 1907 180 0 -355 C
ATOM 686 CE LYS A 81 7.785 25.347 24.308 1.00 25.14 C
ANISOU 686 CE LYS A 81 4151 2897 2505 187 -452 -602 C
ATOM 687 NZ LYS A 81 6.954 26.479 23.827 1.00 26.85 N1+
ANISOU 687 NZ LYS A 81 4905 2900 2394 135 -1090 -524 N1+
ATOM 688 N SER A 82 9.515 20.934 19.831 1.00 10.31 N
ANISOU 688 N SER A 82 2580 1082 255 179 68 14 N
ATOM 689 CA SER A 82 10.050 20.090 18.771 1.00 9.26 C
ANISOU 689 CA SER A 82 2357 890 269 64 62 -22 C
ATOM 690 C SER A 82 10.652 20.923 17.654 1.00 9.38 C
ANISOU 690 C SER A 82 2339 955 267 67 -44 91 C
ATOM 691 O SER A 82 10.143 21.974 17.296 1.00 9.80 O
ANISOU 691 O SER A 82 2376 982 366 168 115 98 O
ATOM 692 CB SER A 82 8.938 19.256 18.206 1.00 10.23 C
ANISOU 692 CB SER A 82 2420 1193 271 20 127 62 C
ATOM 693 OG SER A 82 8.568 18.274 19.144 1.00 11.88 O
ANISOU 693 OG SER A 82 2710 1088 715 45 251 287 O
ATOM 694 N THR A 83 11.759 20.406 17.086 1.00 8.94 N
ANISOU 694 N THR A 83 2163 972 259 145 -10 64 N
ATOM 695 CA THR A 83 12.327 20.979 15.898 1.00 9.30 C
ANISOU 695 CA THR A 83 2328 940 264 10 89 69 C
ATOM 696 C THR A 83 12.663 19.835 14.970 1.00 9.54 C
ANISOU 696 C THR A 83 2377 990 257 83 -28 51 C
ATOM 697 O THR A 83 13.293 18.863 15.371 1.00 10.36 O
ANISOU 697 O THR A 83 2646 1032 257 258 -26 -55 O
ATOM 698 CB THR A 83 13.608 21.776 16.209 1.00 10.75 C
ANISOU 698 CB THR A 83 2254 1041 789 162 143 32 C
ATOM 699 CG2 THR A 83 14.057 22.519 14.964 1.00 13.66 C
ANISOU 699 CG2 THR A 83 2745 1225 1218 -125 199 132 C
ATOM 700 OG1 THR A 83 13.353 22.700 17.260 1.00 12.44 O
ANISOU 700 OG1 THR A 83 2706 1222 795 -101 -165 -229 O
ATOM 701 N ILE A 84 12.212 19.951 13.697 1.00 9.62 N
ANISOU 701 N ILE A 84 2383 1014 258 115 -60 49 N
ATOM 702 CA ILE A 84 12.430 18.928 12.698 1.00 9.16 C
ANISOU 702 CA ILE A 84 2270 951 257 101 92 -3 C
ATOM 703 C ILE A 84 13.234 19.533 11.591 1.00 9.49 C
ANISOU 703 C ILE A 84 2456 885 261 1 70 60 C
ATOM 704 O ILE A 84 12.904 20.594 11.051 1.00 10.10 O
ANISOU 704 O ILE A 84 2594 969 273 87 110 106 O
ATOM 705 CB ILE A 84 11.116 18.310 12.197 1.00 9.51 C
ANISOU 705 CB ILE A 84 2334 980 298 182 28 180 C
ATOM 706 CG1 ILE A 84 10.353 17.720 13.403 1.00 9.59 C
ANISOU 706 CG1 ILE A 84 2217 1139 285 75 -16 168 C
ATOM 707 CG2 ILE A 84 11.420 17.229 11.154 1.00 10.98 C
ANISOU 707 CG2 ILE A 84 2608 1087 474 20 215 -209 C
ATOM 708 CD1 ILE A 84 9.035 17.163 13.072 1.00 10.64 C
ANISOU 708 CD1 ILE A 84 2389 1274 380 100 90 109 C
ATOM 709 N THR A 85 14.329 18.854 11.215 1.00 9.77 N
ANISOU 709 N THR A 85 2377 1055 278 115 225 43 N
ATOM 710 CA THR A 85 15.189 19.262 10.127 1.00 10.49 C
ANISOU 710 CA THR A 85 2444 1081 457 76 179 -56 C
ATOM 711 C THR A 85 15.436 18.086 9.228 1.00 10.82 C
ANISOU 711 C THR A 85 2659 1103 346 -74 313 126 C
ATOM 712 O THR A 85 15.122 16.948 9.536 1.00 11.57 O
ANISOU 712 O THR A 85 2961 1124 312 80 382 76 O
ATOM 713 CB THR A 85 16.516 19.806 10.668 1.00 11.90 C
ANISOU 713 CB THR A 85 2349 1282 890 67 190 68 C
ATOM 714 CG2 THR A 85 16.310 21.130 11.430 1.00 13.66 C
ANISOU 714 CG2 THR A 85 2763 1377 1048 -13 34 -533 C
ATOM 715 OG1 THR A 85 17.107 18.788 11.482 1.00 14.64 O
ANISOU 715 OG1 THR A 85 2938 1672 949 247 -108 -146 O
ATOM 716 N LEU A 86 15.995 18.354 8.051 1.00 12.86 N
ANISOU 716 N LEU A 86 3125 1246 513 -154 504 -70 N
ATOM 717 CA LEU A 86 16.601 17.316 7.169 1.00 15.17 C
ANISOU 717 CA LEU A 86 3254 1450 1057 -287 491 -136 C
ATOM 718 C LEU A 86 18.143 17.221 7.410 1.00 17.41 C
ANISOU 718 C LEU A 86 3134 1749 1730 -343 742 -138 C
ATOM 719 O LEU A 86 18.871 18.272 7.516 1.00 20.25 O
ANISOU 719 O LEU A 86 3281 2086 2325 -447 440 -343 O
ATOM 720 CB LEU A 86 16.293 17.555 5.747 1.00 16.96 C
ANISOU 720 CB LEU A 86 3751 1829 862 -284 625 65 C
ATOM 721 CG LEU A 86 14.918 17.177 5.324 1.00 18.07 C
ANISOU 721 CG LEU A 86 3407 2113 1346 44 451 552 C
ATOM 722 CD1 LEU A 86 14.660 17.746 3.919 1.00 19.24 C
ANISOU 722 CD1 LEU A 86 4077 2199 1032 610 821 508 C
ATOM 723 CD2 LEU A 86 14.770 15.554 5.177 1.00 16.85 C
ANISOU 723 CD2 LEU A 86 3522 1860 1017 -150 101 118 C
ATOM 724 N ASP A 87 18.658 16.021 7.521 1.00 16.96 N
ANISOU 724 N ASP A 87 3047 1974 1420 -378 612 -589 N
ATOM 725 CA ASP A 87 20.109 15.792 7.622 1.00 18.78 C
ANISOU 725 CA ASP A 87 2972 2385 1778 -416 424 -433 C
ATOM 726 C ASP A 87 20.312 14.835 6.510 1.00 15.93 C
ANISOU 726 C ASP A 87 2729 2161 1161 -293 409 -390 C
ATOM 727 O ASP A 87 20.025 13.679 6.690 1.00 16.93 O
ANISOU 727 O ASP A 87 2936 2199 1297 -459 338 -176 O
ATOM 728 CB ASP A 87 20.498 15.183 9.009 1.00 21.62 C
ANISOU 728 CB ASP A 87 3135 2985 2093 -424 324 -312 C
ATOM 729 CG ASP A 87 21.985 14.785 9.120 1.00 26.45 C
ANISOU 729 CG ASP A 87 3615 3759 2675 -205 134 16 C
ATOM 730 OD1 ASP A 87 22.798 15.121 8.236 1.00 31.83 O
ANISOU 730 OD1 ASP A 87 3504 5031 3557 -408 130 116 O
ATOM 731 OD2 ASP A 87 22.354 14.104 10.110 1.00 34.08 O1-
ANISOU 731 OD2 ASP A 87 4305 4996 3648 32 -219 154 O1-
ATOM 732 N AGLY A 88 20.885 15.261 5.390 0.50 15.92 N
ANISOU 732 N AGLY A 88 2675 1893 1481 -285 419 -251 N
ATOM 733 N BGLY A 88 20.750 15.332 5.351 0.50 15.56 N
ANISOU 733 N BGLY A 88 2706 1866 1340 -356 490 -270 N
ATOM 734 CA AGLY A 88 21.243 14.306 4.386 0.50 15.05 C
ANISOU 734 CA AGLY A 88 2533 1956 1229 -141 320 -233 C
ATOM 735 CA BGLY A 88 20.770 14.540 4.168 0.50 14.37 C
ANISOU 735 CA BGLY A 88 2548 1891 1020 -225 597 -269 C
ATOM 736 C AGLY A 88 20.099 13.371 4.053 0.50 13.93 C
ANISOU 736 C AGLY A 88 2456 1899 937 -42 272 -197 C
ATOM 737 C BGLY A 88 19.362 14.193 3.813 0.50 13.72 C
ANISOU 737 C BGLY A 88 2544 1947 721 -159 535 -337 C
ATOM 738 O AGLY A 88 20.281 12.171 4.045 0.50 14.78 O
ANISOU 738 O AGLY A 88 2679 1847 1089 112 208 -312 O
ATOM 739 O BGLY A 88 18.515 15.057 3.727 0.50 14.73 O
ANISOU 739 O BGLY A 88 2874 1910 811 -129 472 -160 O
ATOM 740 N AGLY A 89 18.909 13.911 3.830 0.50 13.36 N
ANISOU 740 N AGLY A 89 2517 1899 659 133 361 -100 N
ATOM 741 N BGLY A 89 19.111 12.897 3.673 0.50 12.92 N
ANISOU 741 N BGLY A 89 2418 1948 543 -286 603 -274 N
ATOM 742 CA AGLY A 89 17.786 13.110 3.450 0.50 12.64 C
ANISOU 742 CA AGLY A 89 2616 1823 364 75 329 -159 C
ATOM 743 CA BGLY A 89 17.805 12.342 3.417 0.50 13.66 C
ANISOU 743 CA BGLY A 89 2604 1968 615 -237 315 -493 C
ATOM 744 C AGLY A 89 17.002 12.388 4.580 0.50 13.03 C
ANISOU 744 C AGLY A 89 2618 1883 448 -76 197 -110 C
ATOM 745 C BGLY A 89 17.115 11.873 4.672 0.50 13.01 C
ANISOU 745 C BGLY A 89 2505 1780 657 -196 291 -522 C
ATOM 746 O AGLY A 89 15.918 11.877 4.306 0.50 12.76 O
ANISOU 746 O AGLY A 89 2723 1811 311 -177 -19 -57 O
ATOM 747 O BGLY A 89 16.194 11.059 4.605 0.50 14.06 O
ANISOU 747 O BGLY A 89 2626 1756 959 -106 93 -850 O
ATOM 748 N VAL A 90 17.485 12.388 5.845 1.00 12.85 N
ANISOU 748 N VAL A 90 2588 1887 407 -305 314 -274 N
ATOM 749 CA VAL A 90 16.844 11.877 7.041 1.00 11.91 C
ANISOU 749 CA VAL A 90 2527 1494 503 -199 360 -257 C
ATOM 750 C VAL A 90 16.122 13.008 7.730 1.00 10.20 C
ANISOU 750 C VAL A 90 2335 1260 278 -129 2 -158 C
ATOM 751 O VAL A 90 16.681 14.078 7.957 1.00 11.49 O
ANISOU 751 O VAL A 90 2687 1293 386 -241 211 -57 O
ATOM 752 CB VAL A 90 17.905 11.318 7.985 1.00 13.19 C
ANISOU 752 CB VAL A 90 2715 1481 814 -51 457 -119 C
ATOM 753 CG1 VAL A 90 17.294 10.815 9.299 1.00 12.81 C
ANISOU 753 CG1 VAL A 90 2504 1597 765 185 200 126 C
ATOM 754 CG2 VAL A 90 18.730 10.204 7.371 1.00 16.28 C
ANISOU 754 CG2 VAL A 90 2897 1632 1655 129 612 -274 C
ATOM 755 N LEU A 91 14.845 12.790 8.036 1.00 10.13 N
ANISOU 755 N LEU A 91 2329 1252 265 -226 72 -106 N
ATOM 756 CA LEU A 91 14.115 13.753 8.850 1.00 10.08 C
ANISOU 756 CA LEU A 91 2431 1105 292 -10 94 173 C
ATOM 757 C LEU A 91 14.498 13.524 10.301 1.00 9.40 C
ANISOU 757 C LEU A 91 2351 928 293 138 230 114 C
ATOM 758 O LEU A 91 14.336 12.412 10.813 1.00 10.22 O
ANISOU 758 O LEU A 91 2645 969 267 122 183 4 O
ATOM 759 CB LEU A 91 12.601 13.570 8.708 1.00 12.48 C
ANISOU 759 CB LEU A 91 2736 1381 624 -147 74 284 C
ATOM 760 CG LEU A 91 11.964 14.174 7.449 1.00 13.17 C
ANISOU 760 CG LEU A 91 2834 1722 446 29 41 -64 C
ATOM 761 CD1 LEU A 91 10.578 13.621 7.325 1.00 16.74 C
ANISOU 761 CD1 LEU A 91 2881 2401 1077 -1 -158 -26 C
ATOM 762 CD2 LEU A 91 11.948 15.694 7.605 1.00 13.25 C
ANISOU 762 CD2 LEU A 91 3004 1071 957 227 18 255 C
ATOM 763 N VAL A 92 15.014 14.556 10.946 1.00 9.66 N
ANISOU 763 N VAL A 92 2405 1005 258 149 75 48 N
ATOM 764 CA VAL A 92 15.483 14.459 12.351 1.00 9.76 C
ANISOU 764 CA VAL A 92 2419 1032 254 261 -20 23 C
ATOM 765 C VAL A 92 14.595 15.313 13.206 1.00 9.83 C
ANISOU 765 C VAL A 92 2528 921 285 220 11 34 C
ATOM 766 O VAL A 92 14.541 16.539 13.011 1.00 10.95 O
ANISOU 766 O VAL A 92 2792 1015 351 171 220 48 O
ATOM 767 CB VAL A 92 16.955 14.929 12.419 1.00 11.03 C
ANISOU 767 CB VAL A 92 2488 1343 360 227 4 -120 C
ATOM 768 CG1 VAL A 92 17.476 14.826 13.868 1.00 13.01 C
ANISOU 768 CG1 VAL A 92 2786 1735 420 180 -60 -44 C
ATOM 769 CG2 VAL A 92 17.876 14.098 11.497 1.00 13.47 C
ANISOU 769 CG2 VAL A 92 2646 1753 719 68 68 -237 C
ATOM 770 N HIS A 93 13.929 14.671 14.149 1.00 9.82 N
ANISOU 770 N HIS A 93 2567 868 294 255 185 116 N
ATOM 771 CA HIS A 93 12.891 15.311 14.989 1.00 9.58 C
ANISOU 771 CA HIS A 93 2393 947 298 360 124 175 C
ATOM 772 C HIS A 93 13.346 15.258 16.416 1.00 9.68 C
ANISOU 772 C HIS A 93 2493 919 266 338 -23 85 C
ATOM 773 O HIS A 93 13.465 14.185 17.007 1.00 10.49 O
ANISOU 773 O HIS A 93 2784 939 259 211 -89 40 O
ATOM 774 CB HIS A 93 11.628 14.553 14.802 1.00 10.07 C
ANISOU 774 CB HIS A 93 2390 1161 272 484 98 132 C
ATOM 775 CG HIS A 93 10.444 14.969 15.564 1.00 10.27 C
ANISOU 775 CG HIS A 93 2296 1214 390 385 4 251 C
ATOM 776 CD2 HIS A 93 10.221 15.937 16.510 1.00 11.87 C
ANISOU 776 CD2 HIS A 93 2663 1340 505 516 120 367 C
ATOM 777 ND1 HIS A 93 9.252 14.318 15.363 1.00 13.49 N
ANISOU 777 ND1 HIS A 93 2471 1830 823 479 254 561 N
ATOM 778 CE1 HIS A 93 8.350 14.848 16.162 1.00 13.77 C
ANISOU 778 CE1 HIS A 93 2271 2135 825 417 484 849 C
ATOM 779 NE2 HIS A 93 8.898 15.854 16.843 1.00 14.78 N
ANISOU 779 NE2 HIS A 93 2844 1929 840 492 414 716 N
ATOM 780 N VAL A 94 13.710 16.410 16.988 1.00 9.83 N
ANISOU 780 N VAL A 94 2547 904 284 229 -22 116 N
ATOM 781 CA VAL A 94 14.165 16.495 18.374 1.00 9.97 C
ANISOU 781 CA VAL A 94 2385 1126 274 227 -30 113 C
ATOM 782 C VAL A 94 13.052 17.057 19.201 1.00 9.51 C
ANISOU 782 C VAL A 94 2427 904 281 118 -63 127 C
ATOM 783 O VAL A 94 12.511 18.106 18.892 1.00 11.10 O
ANISOU 783 O VAL A 94 2791 1115 309 419 185 214 O
ATOM 784 CB VAL A 94 15.460 17.335 18.492 1.00 11.50 C
ANISOU 784 CB VAL A 94 2489 1393 488 248 -3 37 C
ATOM 785 CG1 VAL A 94 15.948 17.367 19.905 1.00 15.55 C
ANISOU 785 CG1 VAL A 94 2912 2191 802 -123 -406 -1 C
ATOM 786 CG2 VAL A 94 16.522 16.855 17.524 1.00 16.17 C
ANISOU 786 CG2 VAL A 94 3008 2187 948 469 203 131 C
ATOM 787 N GLN A 95 12.762 16.372 20.309 1.00 9.78 N
ANISOU 787 N GLN A 95 2535 913 265 153 -35 84 N
ATOM 788 CA GLN A 95 11.742 16.791 21.294 1.00 10.47 C
ANISOU 788 CA GLN A 95 2598 1123 256 148 -29 43 C
ATOM 789 C GLN A 95 12.420 17.121 22.609 1.00 10.42 C
ANISOU 789 C GLN A 95 2735 950 273 148 -199 44 C
ATOM 790 O GLN A 95 13.173 16.295 23.145 1.00 11.59 O
ANISOU 790 O GLN A 95 2943 1193 268 214 -114 -50 O
ATOM 791 CB GLN A 95 10.775 15.656 21.546 1.00 10.58 C
ANISOU 791 CB GLN A 95 2574 1185 260 170 -1 82 C
ATOM 792 CG GLN A 95 9.942 15.272 20.340 1.00 10.51 C
ANISOU 792 CG GLN A 95 2694 1042 256 94 -28 -49 C
ATOM 793 CD GLN A 95 8.994 14.100 20.537 1.00 10.33 C
ANISOU 793 CD GLN A 95 2399 1097 428 145 159 15 C
ATOM 794 NE2 GLN A 95 9.313 13.218 21.425 1.00 10.30 N
ANISOU 794 NE2 GLN A 95 2550 1076 284 -6 -80 152 N
ATOM 795 OE1 GLN A 95 7.956 13.979 19.793 1.00 13.11 O
ANISOU 795 OE1 GLN A 95 2524 1729 726 62 -15 143 O
ATOM 796 N LYS A 96 12.129 18.263 23.160 1.00 10.91 N
ANISOU 796 N LYS A 96 2844 1033 268 111 -195 -10 N
ATOM 797 CA LYS A 96 12.683 18.747 24.440 1.00 12.23 C
ANISOU 797 CA LYS A 96 2951 1323 374 168 -148 -120 C
ATOM 798 C LYS A 96 11.547 18.967 25.438 1.00 12.13 C
ANISOU 798 C LYS A 96 3038 1286 285 161 -86 -87 C
ATOM 799 O LYS A 96 10.559 19.630 25.130 1.00 13.18 O
ANISOU 799 O LYS A 96 3392 1359 254 280 -23 -41 O
ATOM 800 CB LYS A 96 13.368 20.080 24.241 1.00 13.53 C
ANISOU 800 CB LYS A 96 2815 1738 588 -16 -188 -113 C
ATOM 801 CG LYS A 96 14.486 20.154 23.275 1.00 15.82 C
ANISOU 801 CG LYS A 96 3255 1819 936 43 -147 -125 C
ATOM 802 CD LYS A 96 15.654 19.275 23.580 1.00 17.26 C
ANISOU 802 CD LYS A 96 3263 1928 1365 -27 -195 -68 C
ATOM 803 CE LYS A 96 16.811 19.555 22.670 1.00 17.81 C
ANISOU 803 CE LYS A 96 2944 1969 1851 -331 -232 -263 C
ATOM 804 NZ LYS A 96 17.987 18.698 22.917 1.00 18.81 N1+
ANISOU 804 NZ LYS A 96 3027 2029 2089 -242 -7 -21 N1+
ATOM 805 N TRP A 97 11.729 18.452 26.651 1.00 13.11 N
ANISOU 805 N TRP A 97 3323 1391 265 290 -45 -70 N
ATOM 806 CA TRP A 97 10.763 18.681 27.722 1.00 14.56 C
ANISOU 806 CA TRP A 97 3467 1741 322 297 -36 -181 C
ATOM 807 C TRP A 97 11.409 18.362 29.051 1.00 15.62 C
ANISOU 807 C TRP A 97 3777 1875 280 284 -150 -195 C
ATOM 808 O TRP A 97 12.221 17.438 29.136 1.00 16.75 O
ANISOU 808 O TRP A 97 4067 2023 274 451 -250 -124 O
ATOM 809 CB TRP A 97 9.472 17.836 27.554 1.00 14.80 C
ANISOU 809 CB TRP A 97 3454 1772 397 280 142 -67 C
ATOM 810 CG TRP A 97 9.661 16.387 27.939 1.00 14.34 C
ANISOU 810 CG TRP A 97 3378 1524 547 150 372 -118 C
ATOM 811 CD1 TRP A 97 9.152 15.778 29.026 1.00 16.04 C
ANISOU 811 CD1 TRP A 97 3706 1828 558 263 612 20 C
ATOM 812 CD2 TRP A 97 10.432 15.377 27.246 1.00 13.52 C
ANISOU 812 CD2 TRP A 97 3209 1527 401 97 98 -64 C
ATOM 813 CE2 TRP A 97 10.332 14.205 28.009 1.00 13.80 C
ANISOU 813 CE2 TRP A 97 3338 1376 527 -86 175 44 C
ATOM 814 CE3 TRP A 97 11.191 15.347 26.076 1.00 13.55 C
ANISOU 814 CE3 TRP A 97 3414 1350 384 -60 144 -126 C
ATOM 815 NE1 TRP A 97 9.541 14.479 29.091 1.00 15.14 N
ANISOU 815 NE1 TRP A 97 3657 1724 372 200 366 24 N
ATOM 816 CZ2 TRP A 97 10.982 13.044 27.666 1.00 13.99 C
ANISOU 816 CZ2 TRP A 97 3213 1415 688 -153 -18 164 C
ATOM 817 CZ3 TRP A 97 11.804 14.185 25.736 1.00 13.42 C
ANISOU 817 CZ3 TRP A 97 3114 1533 450 -176 96 -117 C
ATOM 818 CH2 TRP A 97 11.715 13.048 26.536 1.00 14.06 C
ANISOU 818 CH2 TRP A 97 3203 1408 729 -109 148 -344 C
ATOM 819 N ASP A 98 11.101 19.161 30.055 1.00 17.52 N
ANISOU 819 N ASP A 98 4167 2126 362 288 -75 -327 N
ATOM 820 CA ASP A 98 11.525 18.836 31.427 1.00 19.29 C
ANISOU 820 CA ASP A 98 4374 2505 450 191 -204 -263 C
ATOM 821 C ASP A 98 13.024 18.581 31.533 1.00 19.43 C
ANISOU 821 C ASP A 98 4417 2498 467 140 -322 -486 C
ATOM 822 O ASP A 98 13.461 17.702 32.307 1.00 22.28 O
ANISOU 822 O ASP A 98 4929 2959 578 368 -374 -271 O
ATOM 823 CB ASP A 98 10.788 17.591 31.928 1.00 21.97 C
ANISOU 823 CB ASP A 98 4716 3010 619 42 -217 59 C
ATOM 824 N GLY A 99 13.812 19.314 30.764 1.00 19.49 N
ANISOU 824 N GLY A 99 4234 2248 920 168 -432 -522 N
ATOM 825 CA GLY A 99 15.246 19.144 30.743 1.00 19.44 C
ANISOU 825 CA GLY A 99 4031 2186 1166 -15 -630 -637 C
ATOM 826 C GLY A 99 15.768 17.870 30.068 1.00 19.18 C
ANISOU 826 C GLY A 99 3883 2237 1166 41 -668 -544 C
ATOM 827 O GLY A 99 16.986 17.598 30.095 1.00 22.62 O
ANISOU 827 O GLY A 99 3981 2827 1786 6 -943 -741 O
ATOM 828 N LYS A 100 14.893 17.116 29.398 1.00 16.96 N
ANISOU 828 N LYS A 100 3785 2007 651 0 -651 -373 N
ATOM 829 CA LYS A 100 15.170 15.873 28.689 1.00 15.51 C
ANISOU 829 CA LYS A 100 3437 1911 543 84 -509 -252 C
ATOM 830 C LYS A 100 15.098 16.122 27.192 1.00 13.62 C
ANISOU 830 C LYS A 100 3243 1512 419 126 -629 -43 C
ATOM 831 O LYS A 100 14.536 17.105 26.740 1.00 14.11 O
ANISOU 831 O LYS A 100 3489 1441 431 142 -490 -84 O
ATOM 832 CB LYS A 100 14.121 14.852 29.089 1.00 14.92 C
ANISOU 832 CB LYS A 100 3577 1781 309 202 -248 -76 C
ATOM 833 CG LYS A 100 14.097 14.520 30.641 1.00 19.78 C
ANISOU 833 CG LYS A 100 4042 2690 785 22 -313 70 C
ATOM 834 CD LYS A 100 12.877 13.656 31.001 1.00 22.24 C
ANISOU 834 CD LYS A 100 4151 3198 1100 135 127 399 C
ATOM 835 CE LYS A 100 12.645 13.366 32.464 1.00 26.13 C
ANISOU 835 CE LYS A 100 4601 3567 1760 3 257 464 C
ATOM 836 NZ LYS A 100 11.306 12.728 32.573 1.00 32.12 N1+
ANISOU 836 NZ LYS A 100 4821 4786 2597 10 116 716 N1+
ATOM 837 N SER A 101 15.602 15.152 26.436 1.00 12.96 N
ANISOU 837 N SER A 101 3234 1198 492 44 -507 -92 N
ATOM 838 CA SER A 101 15.579 15.254 24.970 1.00 12.11 C
ANISOU 838 CA SER A 101 2864 1340 394 -3 -350 -5 C
ATOM 839 C SER A 101 15.509 13.858 24.412 1.00 11.63 C
ANISOU 839 C SER A 101 2864 1231 323 46 -309 176 C
ATOM 840 O SER A 101 16.111 12.936 24.933 1.00 12.94 O
ANISOU 840 O SER A 101 3044 1355 515 119 -486 36 O
ATOM 841 CB SER A 101 16.858 15.897 24.513 1.00 13.83 C
ANISOU 841 CB SER A 101 3086 1484 684 -176 -287 28 C
ATOM 842 OG SER A 101 16.884 16.098 23.152 1.00 15.40 O
ANISOU 842 OG SER A 101 3448 1433 968 -278 -174 26 O
ATOM 843 N THR A 102 14.758 13.686 23.323 1.00 10.26 N
ANISOU 843 N THR A 102 2503 1096 296 24 -291 52 N
ATOM 844 CA THR A 102 14.732 12.453 22.544 1.00 9.56 C
ANISOU 844 CA THR A 102 2320 1038 271 95 -170 50 C
ATOM 845 C THR A 102 14.722 12.839 21.085 1.00 9.54 C
ANISOU 845 C THR A 102 2233 1059 331 168 -142 20 C
ATOM 846 O THR A 102 14.230 13.899 20.713 1.00 10.45 O
ANISOU 846 O THR A 102 2642 1063 263 206 -70 73 O
ATOM 847 CB THR A 102 13.528 11.601 22.914 1.00 10.29 C
ANISOU 847 CB THR A 102 2501 1133 272 -31 -157 -85 C
ATOM 848 CG2 THR A 102 12.213 12.195 22.604 1.00 11.61 C
ANISOU 848 CG2 THR A 102 2771 1192 446 105 -122 24 C
ATOM 849 OG1 THR A 102 13.615 10.341 22.288 1.00 11.55 O
ANISOU 849 OG1 THR A 102 2650 1066 672 -51 -53 21 O
ATOM 850 N THR A 103 15.314 11.983 20.244 1.00 10.04 N
ANISOU 850 N THR A 103 2516 942 354 259 -120 85 N
ATOM 851 CA THR A 103 15.401 12.212 18.803 1.00 10.19 C
ANISOU 851 CA THR A 103 2541 1069 259 163 25 68 C
ATOM 852 C THR A 103 14.776 11.055 18.055 1.00 10.18 C
ANISOU 852 C THR A 103 2667 942 259 247 -49 51 C
ATOM 853 O THR A 103 15.020 9.889 18.333 1.00 11.52 O
ANISOU 853 O THR A 103 3104 910 361 262 -251 38 O
ATOM 854 CB THR A 103 16.868 12.400 18.394 1.00 11.80 C
ANISOU 854 CB THR A 103 2666 1179 637 150 5 -81 C
ATOM 855 CG2 THR A 103 16.983 12.631 16.900 1.00 13.89 C
ANISOU 855 CG2 THR A 103 3030 1749 496 45 303 70 C
ATOM 856 OG1 THR A 103 17.395 13.536 19.051 1.00 15.15 O
ANISOU 856 OG1 THR A 103 2914 1899 941 -222 60 48 O
ATOM 857 N ILE A 104 13.894 11.429 17.122 1.00 9.95 N
ANISOU 857 N ILE A 104 2656 840 284 180 -114 113 N
ATOM 858 CA ILE A 104 13.209 10.487 16.255 1.00 10.13 C
ANISOU 858 CA ILE A 104 2661 920 266 94 83 87 C
ATOM 859 C ILE A 104 13.715 10.741 14.839 1.00 9.55 C
ANISOU 859 C ILE A 104 2550 807 271 270 80 97 C
ATOM 860 O ILE A 104 13.578 11.839 14.339 1.00 10.37 O
ANISOU 860 O ILE A 104 2722 963 255 374 46 38 O
ATOM 861 CB ILE A 104 11.701 10.675 16.292 1.00 10.65 C
ANISOU 861 CB ILE A 104 2711 1054 280 115 42 148 C
ATOM 862 CG1 ILE A 104 11.170 10.513 17.721 1.00 12.49 C
ANISOU 862 CG1 ILE A 104 2740 1527 478 77 345 169 C
ATOM 863 CG2 ILE A 104 11.001 9.668 15.341 1.00 13.18 C
ANISOU 863 CG2 ILE A 104 2901 1625 479 52 -35 -6 C
ATOM 864 CD1 ILE A 104 9.922 11.280 17.918 1.00 18.56 C
ANISOU 864 CD1 ILE A 104 3063 2828 1161 314 670 314 C
ATOM 865 N LYS A 105 14.333 9.759 14.223 1.00 9.15 N
ANISOU 865 N LYS A 105 2409 805 261 154 63 63 N
ATOM 866 CA LYS A 105 14.793 9.846 12.851 1.00 9.58 C
ANISOU 866 CA LYS A 105 2415 970 253 89 27 -13 C
ATOM 867 C LYS A 105 13.902 9.041 11.949 1.00 9.50 C
ANISOU 867 C LYS A 105 2419 930 259 -25 -17 54 C
ATOM 868 O LYS A 105 13.518 7.928 12.286 1.00 11.20 O
ANISOU 868 O LYS A 105 3044 936 274 -126 -161 53 O
ATOM 869 CB LYS A 105 16.242 9.382 12.725 1.00 10.88 C
ANISOU 869 CB LYS A 105 2509 1369 254 59 -32 19 C
ATOM 870 CG LYS A 105 17.256 10.368 13.422 1.00 14.79 C
ANISOU 870 CG LYS A 105 2591 1945 1083 182 -168 -139 C
ATOM 871 CD LYS A 105 18.697 10.013 13.246 1.00 20.24 C
ANISOU 871 CD LYS A 105 2680 3003 2005 -86 -144 18 C
ATOM 872 CE LYS A 105 19.624 11.020 13.881 1.00 23.24 C
ANISOU 872 CE LYS A 105 3009 3060 2761 -164 -270 312 C
ATOM 873 NZ LYS A 105 21.053 10.597 13.664 1.00 28.01 N1+
ANISOU 873 NZ LYS A 105 3406 3683 3550 -195 -53 201 N1+
ATOM 874 N ARG A 106 13.590 9.594 10.786 1.00 9.67 N
ANISOU 874 N ARG A 106 2438 962 272 -14 23 116 N
ATOM 875 CA ARG A 106 12.744 8.911 9.783 1.00 10.19 C
ANISOU 875 CA ARG A 106 2426 1177 266 -212 119 68 C
ATOM 876 C ARG A 106 13.537 8.894 8.458 1.00 10.01 C
ANISOU 876 C ARG A 106 2436 1021 345 -172 42 33 C
ATOM 877 O ARG A 106 13.987 9.930 8.011 1.00 10.19 O
ANISOU 877 O ARG A 106 2564 1051 255 -146 69 -4 O
ATOM 878 CB ARG A 106 11.405 9.622 9.663 1.00 11.07 C
ANISOU 878 CB ARG A 106 2525 1417 262 -246 51 88 C
ATOM 879 CG ARG A 106 10.625 9.606 10.962 1.00 12.10 C
ANISOU 879 CG ARG A 106 2550 1684 363 -69 138 148 C
ATOM 880 CD ARG A 106 9.345 10.379 10.922 1.00 15.46 C
ANISOU 880 CD ARG A 106 2698 2704 470 -222 142 82 C
ATOM 881 NE ARG A 106 8.519 10.310 12.123 1.00 15.77 N
ANISOU 881 NE ARG A 106 2728 2724 537 -187 180 176 N
ATOM 882 CZ ARG A 106 8.440 11.241 13.061 1.00 15.21 C
ANISOU 882 CZ ARG A 106 2414 2708 655 89 202 252 C
ATOM 883 NH1 ARG A 106 9.258 12.257 13.098 1.00 14.73 N1+
ANISOU 883 NH1 ARG A 106 2681 2127 787 276 215 267 N1+
ATOM 884 NH2 ARG A 106 7.574 11.093 14.032 1.00 17.19 N
ANISOU 884 NH2 ARG A 106 2660 3233 635 -150 441 -15 N
ATOM 885 N LYS A 107 13.664 7.714 7.894 1.00 10.02 N
ANISOU 885 N LYS A 107 2510 998 298 -201 134 19 N
ATOM 886 CA LYS A 107 14.490 7.555 6.670 1.00 11.22 C
ANISOU 886 CA LYS A 107 2513 1292 457 -217 174 -122 C
ATOM 887 C LYS A 107 13.873 6.520 5.783 1.00 10.78 C
ANISOU 887 C LYS A 107 2516 1308 269 -299 135 70 C
ATOM 888 O LYS A 107 13.360 5.506 6.213 1.00 13.52 O
ANISOU 888 O LYS A 107 3326 1549 259 -573 131 -42 O
ATOM 889 CB LYS A 107 15.925 7.157 7.018 1.00 14.04 C
ANISOU 889 CB LYS A 107 2685 1884 763 -107 167 -412 C
ATOM 890 CG LYS A 107 16.926 7.188 5.891 1.00 17.03 C
ANISOU 890 CG LYS A 107 2983 2249 1238 -163 50 -534 C
ATOM 891 CD LYS A 107 18.336 6.788 6.317 1.00 20.32 C
ANISOU 891 CD LYS A 107 3135 2810 1774 76 129 -756 C
ATOM 892 CE LYS A 107 19.383 7.281 5.294 1.00 23.25 C
ANISOU 892 CE LYS A 107 3561 3243 2028 -146 313 -1019 C
ATOM 893 NZ LYS A 107 18.827 7.316 3.942 1.00 31.66 N1+
ANISOU 893 NZ LYS A 107 4459 4633 2938 -166 -27 -285 N1+
ATOM 894 N ARG A 108 13.927 6.760 4.481 1.00 10.87 N
ANISOU 894 N ARG A 108 2462 1394 274 -222 190 -25 N
ATOM 895 CA ARG A 108 13.528 5.764 3.492 1.00 11.79 C
ANISOU 895 CA ARG A 108 2481 1675 322 -180 160 33 C
ATOM 896 C ARG A 108 14.614 4.709 3.329 1.00 12.80 C
ANISOU 896 C ARG A 108 2481 1868 512 -223 179 -211 C
ATOM 897 O ARG A 108 15.775 5.041 3.091 1.00 14.69 O
ANISOU 897 O ARG A 108 2759 1798 1021 -139 279 -639 O
ATOM 898 CB ARG A 108 13.243 6.412 2.160 1.00 13.65 C
ANISOU 898 CB ARG A 108 2745 2054 385 -218 191 147 C
ATOM 899 CG ARG A 108 11.922 7.092 2.131 1.00 15.19 C
ANISOU 899 CG ARG A 108 3083 2072 615 5 -52 571 C
ATOM 900 CD ARG A 108 10.726 6.146 2.215 1.00 17.77 C
ANISOU 900 CD ARG A 108 2739 2895 1118 -81 -172 996 C
ATOM 901 NE ARG A 108 10.849 5.056 1.209 1.00 20.48 N
ANISOU 901 NE ARG A 108 2966 2882 1932 -81 -360 807 N
ATOM 902 CZ ARG A 108 10.547 5.192 -0.079 1.00 17.57 C
ANISOU 902 CZ ARG A 108 2872 1611 2192 -92 -456 126 C
ATOM 903 NH1 ARG A 108 10.015 6.289 -0.615 1.00 18.23 N1+
ANISOU 903 NH1 ARG A 108 3305 2548 1070 -88 -659 369 N1+
ATOM 904 NH2 ARG A 108 10.757 4.177 -0.887 1.00 21.70 N
ANISOU 904 NH2 ARG A 108 3199 2711 2334 202 -399 -369 N
ATOM 905 N GLU A 109 14.210 3.444 3.354 1.00 11.97 N
ANISOU 905 N GLU A 109 2465 1685 396 -72 170 -292 N
ATOM 906 CA GLU A 109 15.117 2.317 3.099 1.00 12.87 C
ANISOU 906 CA GLU A 109 2596 1835 456 -60 61 -237 C
ATOM 907 C GLU A 109 14.358 1.338 2.232 1.00 12.42 C
ANISOU 907 C GLU A 109 2538 1580 598 18 160 -183 C
ATOM 908 O GLU A 109 13.355 0.774 2.684 1.00 12.35 O
ANISOU 908 O GLU A 109 2674 1729 288 -209 198 -182 O
ATOM 909 CB GLU A 109 15.503 1.627 4.418 1.00 14.27 C
ANISOU 909 CB GLU A 109 2728 2009 685 89 -70 -47 C
ATOM 910 CG GLU A 109 16.238 2.535 5.396 1.00 18.33 C
ANISOU 910 CG GLU A 109 3081 2663 1219 106 -376 -171 C
ATOM 911 CD GLU A 109 17.654 2.778 5.022 1.00 22.49 C
ANISOU 911 CD GLU A 109 3567 3407 1569 -69 44 -439 C
ATOM 912 OE1 GLU A 109 18.355 3.467 5.780 1.00 26.66 O
ANISOU 912 OE1 GLU A 109 3759 3946 2422 -383 149 -759 O
ATOM 913 OE2 GLU A 109 18.095 2.284 3.983 1.00 28.36 O1-
ANISOU 913 OE2 GLU A 109 4269 4024 2481 162 549 -734 O1-
ATOM 914 N ASP A 110 14.789 1.170 0.989 1.00 11.55 N
ANISOU 914 N ASP A 110 2568 1523 296 -10 249 -111 N
ATOM 915 CA ASP A 110 14.044 0.357 0.047 1.00 11.42 C
ANISOU 915 CA ASP A 110 2659 1404 276 -110 230 -41 C
ATOM 916 C ASP A 110 12.632 0.877 -0.021 1.00 10.90 C
ANISOU 916 C ASP A 110 2404 1469 267 -111 146 -82 C
ATOM 917 O ASP A 110 12.471 2.109 -0.129 1.00 11.77 O
ANISOU 917 O ASP A 110 2666 1540 264 -16 156 -31 O
ATOM 918 CB ASP A 110 14.178 -1.131 0.354 1.00 11.93 C
ANISOU 918 CB ASP A 110 2720 1454 358 62 248 -113 C
ATOM 919 CG ASP A 110 15.592 -1.611 0.303 1.00 15.41 C
ANISOU 919 CG ASP A 110 2997 1978 877 46 258 163 C
ATOM 920 OD1 ASP A 110 16.326 -1.157 -0.565 1.00 18.50 O
ANISOU 920 OD1 ASP A 110 3141 2338 1548 386 532 177 O
ATOM 921 OD2 ASP A 110 15.967 -2.490 1.110 1.00 23.23 O1-
ANISOU 921 OD2 ASP A 110 3586 2983 2255 625 50 1115 O1-
ATOM 922 N ASP A 111 11.595 0.079 0.032 1.00 11.98 N
ANISOU 922 N ASP A 111 2690 1571 290 -20 115 -204 N
ATOM 923 CA ASP A 111 10.235 0.559 -0.024 1.00 12.40 C
ANISOU 923 CA ASP A 111 2679 1731 298 -101 57 -149 C
ATOM 924 C ASP A 111 9.658 0.901 1.356 1.00 12.58 C
ANISOU 924 C ASP A 111 2594 1660 526 -44 73 -299 C
ATOM 925 O ASP A 111 8.456 1.137 1.464 1.00 15.60 O
ANISOU 925 O ASP A 111 2750 2487 686 66 32 -688 O
ATOM 926 CB ASP A 111 9.345 -0.446 -0.760 1.00 12.60 C
ANISOU 926 CB ASP A 111 2627 1887 272 -64 -19 -174 C
ATOM 927 CG ASP A 111 9.665 -0.523 -2.240 1.00 13.54 C
ANISOU 927 CG ASP A 111 2953 1753 438 -63 37 -187 C
ATOM 928 OD1 ASP A 111 9.894 0.535 -2.843 1.00 15.32 O
ANISOU 928 OD1 ASP A 111 3512 1809 498 -220 9 -69 O
ATOM 929 OD2 ASP A 111 9.669 -1.615 -2.781 1.00 16.36 O1-
ANISOU 929 OD2 ASP A 111 3936 1791 487 -187 268 -304 O1-
ATOM 930 N LYS A 112 10.485 0.874 2.390 1.00 11.44 N
ANISOU 930 N LYS A 112 2577 1495 275 -43 198 -85 N
ATOM 931 CA LYS A 112 10.046 1.104 3.739 1.00 11.22 C
ANISOU 931 CA LYS A 112 2613 1355 295 -52 306 -55 C
ATOM 932 C LYS A 112 10.371 2.489 4.192 1.00 10.62 C
ANISOU 932 C LYS A 112 2399 1349 286 -72 254 49 C
ATOM 933 O LYS A 112 11.232 3.161 3.661 1.00 11.21 O
ANISOU 933 O LYS A 112 2523 1432 302 -182 173 -39 O
ATOM 934 CB LYS A 112 10.714 0.080 4.654 1.00 12.86 C
ANISOU 934 CB LYS A 112 2999 1546 342 100 443 -122 C
ATOM 935 CG LYS A 112 10.359 -1.334 4.263 1.00 17.60 C
ANISOU 935 CG LYS A 112 3575 1908 1202 221 640 -166 C
ATOM 936 CD LYS A 112 11.010 -2.390 5.006 1.00 23.96 C
ANISOU 936 CD LYS A 112 4323 2956 1824 553 519 -310 C
ATOM 937 CE LYS A 112 10.685 -3.763 4.368 1.00 28.47 C
ANISOU 937 CE LYS A 112 4782 3188 2845 284 212 -342 C
ATOM 938 NZ LYS A 112 11.634 -4.794 4.775 1.00 31.43 N1+
ANISOU 938 NZ LYS A 112 5314 4009 2615 382 -224 -86 N1+
ATOM 939 N LEU A 113 9.712 2.878 5.264 1.00 10.00 N
ANISOU 939 N LEU A 113 2377 1159 264 -107 154 2 N
ATOM 940 CA LEU A 113 10.030 4.088 6.007 1.00 9.84 C
ANISOU 940 CA LEU A 113 2300 1183 255 -132 61 23 C
ATOM 941 C LEU A 113 10.395 3.619 7.434 1.00 10.08 C
ANISOU 941 C LEU A 113 2391 1119 317 -191 271 29 C
ATOM 942 O LEU A 113 9.586 3.006 8.107 1.00 11.11 O
ANISOU 942 O LEU A 113 2476 1480 263 -269 125 42 O
ATOM 943 CB LEU A 113 8.840 5.046 5.983 1.00 11.19 C
ANISOU 943 CB LEU A 113 2530 1364 357 -241 69 -103 C
ATOM 944 CG LEU A 113 9.049 6.444 6.662 1.00 14.06 C
ANISOU 944 CG LEU A 113 2786 1843 713 -90 -89 -415 C
ATOM 945 CD1 LEU A 113 7.884 7.345 6.237 1.00 16.70 C
ANISOU 945 CD1 LEU A 113 3025 2001 1317 329 -184 -101 C
ATOM 946 CD2 LEU A 113 9.253 6.482 8.054 1.00 17.47 C
ANISOU 946 CD2 LEU A 113 3172 2423 1042 108 95 108 C
ATOM 947 N VAL A 114 11.669 3.797 7.774 1.00 9.88 N
ANISOU 947 N VAL A 114 2257 1234 261 -169 65 70 N
ATOM 948 CA VAL A 114 12.188 3.326 9.083 1.00 10.41 C
ANISOU 948 CA VAL A 114 2414 1229 309 -177 -29 207 C
ATOM 949 C VAL A 114 12.225 4.513 10.021 1.00 11.18 C
ANISOU 949 C VAL A 114 2542 1396 310 -308 86 205 C
ATOM 950 O VAL A 114 12.707 5.602 9.685 1.00 11.79 O
ANISOU 950 O VAL A 114 2723 1449 306 -372 140 14 O
ATOM 951 CB VAL A 114 13.574 2.730 8.892 1.00 12.47 C
ANISOU 951 CB VAL A 114 2607 1487 645 -122 -7 268 C
ATOM 952 CG1 VAL A 114 14.142 2.208 10.181 1.00 13.88 C
ANISOU 952 CG1 VAL A 114 2856 1799 615 138 -79 350 C
ATOM 953 CG2 VAL A 114 13.547 1.568 7.854 1.00 14.86 C
ANISOU 953 CG2 VAL A 114 2968 1661 1017 256 258 -202 C
ATOM 954 N VAL A 115 11.711 4.270 11.227 1.00 11.20 N
ANISOU 954 N VAL A 115 2772 1194 288 -287 -52 182 N
ATOM 955 CA VAL A 115 11.635 5.259 12.301 1.00 10.92 C
ANISOU 955 CA VAL A 115 2696 1117 335 -270 -209 24 C
ATOM 956 C VAL A 115 12.514 4.775 13.440 1.00 10.70 C
ANISOU 956 C VAL A 115 2677 1102 283 -235 -170 138 C
ATOM 957 O VAL A 115 12.264 3.721 14.020 1.00 13.93 O
ANISOU 957 O VAL A 115 3270 1458 563 -576 -462 358 O
ATOM 958 CB VAL A 115 10.194 5.472 12.730 1.00 11.60 C
ANISOU 958 CB VAL A 115 2764 1349 293 -292 -169 30 C
ATOM 959 CG1 VAL A 115 10.068 6.582 13.782 1.00 13.97 C
ANISOU 959 CG1 VAL A 115 3063 1901 342 -112 -287 -122 C
ATOM 960 CG2 VAL A 115 9.310 5.790 11.537 1.00 13.12 C
ANISOU 960 CG2 VAL A 115 2779 1565 641 -445 -209 193 C
ATOM 961 N GLU A 116 13.548 5.534 13.759 1.00 10.15 N
ANISOU 961 N GLU A 116 2608 978 270 -199 -83 106 N
ATOM 962 CA AGLU A 116 14.484 5.206 14.857 0.50 10.37 C
ANISOU 962 CA AGLU A 116 2650 908 380 24 -98 117 C
ATOM 963 CA BGLU A 116 14.458 5.210 14.866 0.50 10.92 C
ANISOU 963 CA BGLU A 116 2672 956 521 -34 -112 87 C
ATOM 964 C GLU A 116 14.266 6.222 15.961 1.00 9.95 C
ANISOU 964 C GLU A 116 2554 941 285 44 -219 18 C
ATOM 965 O GLU A 116 14.465 7.409 15.739 1.00 11.58 O
ANISOU 965 O GLU A 116 3145 982 271 97 -71 34 O
ATOM 966 CB AGLU A 116 15.938 5.242 14.337 0.50 12.43 C
ANISOU 966 CB AGLU A 116 2820 1074 826 128 -58 17 C
ATOM 967 CB BGLU A 116 15.902 5.297 14.411 0.50 13.33 C
ANISOU 967 CB BGLU A 116 2839 1227 995 22 -99 19 C
ATOM 968 CG AGLU A 116 17.017 4.875 15.363 0.50 13.22 C
ANISOU 968 CG AGLU A 116 2807 1571 645 442 169 418 C
ATOM 969 CG BGLU A 116 16.502 4.098 13.766 0.50 16.39 C
ANISOU 969 CG BGLU A 116 2924 1612 1689 -12 102 150 C
ATOM 970 CD AGLU A 116 18.407 5.538 15.141 0.50 18.16 C
ANISOU 970 CD AGLU A 116 3208 2229 1460 156 26 132 C
ATOM 971 CD BGLU A 116 18.013 4.073 14.066 0.50 20.78 C
ANISOU 971 CD BGLU A 116 3073 2657 2163 137 -62 -73 C
ATOM 972 OE1AGLU A 116 18.536 6.798 15.082 0.50 19.19 O
ANISOU 972 OE1AGLU A 116 3237 2377 1675 179 291 483 O
ATOM 973 OE1BGLU A 116 18.579 5.084 14.547 0.50 22.55 O
ANISOU 973 OE1BGLU A 116 2967 3444 2154 393 -580 -322 O
ATOM 974 OE2AGLU A 116 19.399 4.788 15.041 0.50 19.99 O1-
ANISOU 974 OE2AGLU A 116 3224 3091 1280 219 310 422 O1-
ATOM 975 OE2BGLU A 116 18.637 3.045 13.805 0.50 22.11 O1-
ANISOU 975 OE2BGLU A 116 3369 2867 2162 540 -131 345 O1-
ATOM 976 N CYS A 117 13.872 5.744 17.136 1.00 10.08 N
ANISOU 976 N CYS A 117 2572 945 313 98 -130 152 N
ATOM 977 CA CYS A 117 13.590 6.569 18.288 1.00 10.43 C
ANISOU 977 CA CYS A 117 2585 947 429 220 -148 -42 C
ATOM 978 C CYS A 117 14.719 6.344 19.289 1.00 10.43 C
ANISOU 978 C CYS A 117 2610 1015 336 220 -160 38 C
ATOM 979 O CYS A 117 14.939 5.214 19.697 1.00 11.37 O
ANISOU 979 O CYS A 117 2867 1009 442 131 -389 66 O
ATOM 980 CB CYS A 117 12.231 6.141 18.917 1.00 12.20 C
ANISOU 980 CB CYS A 117 2701 1616 317 404 -291 -46 C
ATOM 981 SG CYS A 117 10.844 6.160 17.765 1.00 16.58 S
ANISOU 981 SG CYS A 117 2916 2711 673 272 -204 328 S
ATOM 982 N VAL A 118 15.369 7.402 19.714 1.00 10.58 N
ANISOU 982 N VAL A 118 2549 1036 434 200 -151 42 N
ATOM 983 CA VAL A 118 16.542 7.307 20.563 1.00 11.24 C
ANISOU 983 CA VAL A 118 2533 1014 723 171 -89 -70 C
ATOM 984 C VAL A 118 16.374 8.159 21.810 1.00 11.61 C
ANISOU 984 C VAL A 118 2530 1047 833 225 -214 28 C
ATOM 985 O VAL A 118 16.043 9.346 21.731 1.00 11.70 O
ANISOU 985 O VAL A 118 2879 1052 513 231 -155 -13 O
ATOM 986 CB VAL A 118 17.839 7.702 19.796 1.00 13.96 C
ANISOU 986 CB VAL A 118 2644 1354 1304 15 0 -80 C
ATOM 987 CG1 VAL A 118 19.018 7.678 20.700 1.00 18.35 C
ANISOU 987 CG1 VAL A 118 2722 2030 2219 -55 6 -280 C
ATOM 988 CG2 VAL A 118 18.056 6.805 18.593 1.00 16.06 C
ANISOU 988 CG2 VAL A 118 2921 1741 1438 -47 506 -258 C
ATOM 989 N MET A 119 16.604 7.552 22.971 1.00 12.29 N
ANISOU 989 N MET A 119 2737 1113 819 280 -361 88 N
ATOM 990 CA MET A 119 16.628 8.307 24.252 1.00 13.64 C
ANISOU 990 CA MET A 119 2958 1282 940 216 -500 46 C
ATOM 991 C MET A 119 17.831 7.706 24.966 1.00 14.41 C
ANISOU 991 C MET A 119 2835 1558 1079 184 -441 -103 C
ATOM 992 O MET A 119 17.846 6.546 25.355 1.00 13.94 O
ANISOU 992 O MET A 119 2950 1400 944 279 -560 -51 O
ATOM 993 CB MET A 119 15.299 8.034 25.010 1.00 14.83 C
ANISOU 993 CB MET A 119 3090 1848 695 459 -468 -181 C
ATOM 994 CG MET A 119 15.181 8.461 26.442 1.00 17.07 C
ANISOU 994 CG MET A 119 3742 1802 941 18 -380 38 C
ATOM 995 SD MET A 119 14.822 10.194 26.368 1.00 23.10 S
ANISOU 995 SD MET A 119 5376 1873 1528 865 -1441 -468 S
ATOM 996 CE MET A 119 14.873 10.868 27.989 1.00 18.84 C
ANISOU 996 CE MET A 119 4256 1561 1340 -55 -342 -102 C
ATOM 997 N ALYS A 120 18.860 8.502 25.253 0.50 17.56 N
ANISOU 997 N ALYS A 120 3014 1852 1805 110 -372 11 N
ATOM 998 N BLYS A 120 18.833 8.561 25.058 0.50 15.24 N
ANISOU 998 N BLYS A 120 2793 1578 1420 140 -398 -7 N
ATOM 999 CA ALYS A 120 20.056 8.077 26.030 0.50 19.93 C
ANISOU 999 CA ALYS A 120 2998 2353 2221 54 -254 -5 C
ATOM 1000 CA BLYS A 120 20.072 8.244 25.612 0.50 15.06 C
ANISOU 1000 CA BLYS A 120 2619 1693 1408 54 -336 151 C
ATOM 1001 C ALYS A 120 20.472 6.617 26.031 0.50 19.32 C
ANISOU 1001 C ALYS A 120 2917 2311 2111 25 -221 -33 C
ATOM 1002 C BLYS A 120 20.636 7.019 24.885 0.50 12.36 C
ANISOU 1002 C BLYS A 120 2378 1323 992 36 -362 188 C
ATOM 1003 O ALYS A 120 20.377 5.919 27.042 0.50 21.04 O
ANISOU 1003 O ALYS A 120 3176 2582 2236 -105 -246 -181 O
ATOM 1004 O BLYS A 120 20.775 6.992 23.650 0.50 13.32 O
ANISOU 1004 O BLYS A 120 2488 1339 1232 107 -98 490 O
ATOM 1005 CB ALYS A 120 19.939 8.467 27.484 0.50 20.55 C
ANISOU 1005 CB ALYS A 120 3049 2409 2350 136 -273 -44 C
ATOM 1006 CB BLYS A 120 19.872 8.015 27.130 0.50 13.94 C
ANISOU 1006 CB BLYS A 120 2646 1381 1269 45 -520 2 C
ATOM 1007 CG ALYS A 120 18.722 8.034 28.195 0.50 20.92 C
ANISOU 1007 CG ALYS A 120 3073 2522 2351 131 -415 63 C
ATOM 1008 CG BLYS A 120 19.397 9.311 27.931 0.50 16.02 C
ANISOU 1008 CG BLYS A 120 2633 2077 1376 262 -679 -234 C
ATOM 1009 CD ALYS A 120 18.245 9.251 28.926 0.50 23.16 C
ANISOU 1009 CD ALYS A 120 3308 2783 2708 201 -323 -63 C
ATOM 1010 CD BLYS A 120 19.145 8.908 29.380 0.50 19.90 C
ANISOU 1010 CD BLYS A 120 3125 2627 1807 73 -571 -354 C
ATOM 1011 CE ALYS A 120 19.447 9.927 29.526 0.50 25.15 C
ANISOU 1011 CE ALYS A 120 3477 3126 2951 -10 -225 108 C
ATOM 1012 CE BLYS A 120 18.698 10.057 30.253 0.50 22.72 C
ANISOU 1012 CE BLYS A 120 3304 3156 2172 12 -129 -378 C
ATOM 1013 NZ ALYS A 120 20.101 9.020 30.501 0.50 26.28 N1+
ANISOU 1013 NZ ALYS A 120 3899 3398 2686 -34 -268 258 N1+
ATOM 1014 NZ BLYS A 120 19.715 10.422 31.270 0.50 24.58 N1+
ANISOU 1014 NZ BLYS A 120 3601 3076 2661 -73 -421 -193 N1+
ATOM 1015 N AGLY A 121 21.022 6.189 24.912 0.50 18.52 N
ANISOU 1015 N AGLY A 121 2763 2329 1943 48 -164 -2 N
ATOM 1016 N BGLY A 121 20.935 5.940 25.615 0.50 13.01 N
ANISOU 1016 N BGLY A 121 2299 1582 1061 104 -239 333 N
ATOM 1017 CA AGLY A 121 21.542 4.864 24.769 0.50 17.31 C
ANISOU 1017 CA AGLY A 121 2620 2085 1868 36 -122 114 C
ATOM 1018 CA BGLY A 121 21.525 4.784 25.004 0.50 14.87 C
ANISOU 1018 CA BGLY A 121 2401 1765 1483 60 -173 242 C
ATOM 1019 C GLY A 121 20.507 3.822 24.406 1.00 13.86 C
ANISOU 1019 C GLY A 121 2363 1801 1101 85 -206 188 C
ATOM 1020 O GLY A 121 20.877 2.763 23.972 1.00 14.92 O
ANISOU 1020 O GLY A 121 2485 1831 1352 287 57 351 O
ATOM 1021 N VAL A 122 19.215 4.133 24.519 1.00 12.64 N
ANISOU 1021 N VAL A 122 2479 1478 846 99 -205 262 N
ATOM 1022 CA VAL A 122 18.141 3.196 24.132 1.00 11.27 C
ANISOU 1022 CA VAL A 122 2367 1253 663 262 -153 216 C
ATOM 1023 C VAL A 122 17.535 3.591 22.808 1.00 11.35 C
ANISOU 1023 C VAL A 122 2343 1167 800 157 -209 161 C
ATOM 1024 O VAL A 122 17.065 4.728 22.658 1.00 12.27 O
ANISOU 1024 O VAL A 122 2793 1184 684 322 -405 85 O
ATOM 1025 CB VAL A 122 17.055 3.116 25.223 1.00 12.33 C
ANISOU 1025 CB VAL A 122 2416 1473 796 234 -122 164 C
ATOM 1026 CG1 VAL A 122 16.000 2.173 24.790 1.00 14.92 C
ANISOU 1026 CG1 VAL A 122 2501 1906 1260 82 82 262 C
ATOM 1027 CG2 VAL A 122 17.661 2.699 26.559 1.00 14.98 C
ANISOU 1027 CG2 VAL A 122 2864 1989 836 391 -19 471 C
ATOM 1028 N THR A 123 17.552 2.669 21.850 1.00 11.41 N
ANISOU 1028 N THR A 123 2413 1134 786 172 -264 128 N
ATOM 1029 CA THR A 123 16.997 2.850 20.536 1.00 11.34 C
ANISOU 1029 CA THR A 123 2431 1270 606 200 -243 116 C
ATOM 1030 C THR A 123 15.821 1.906 20.315 1.00 10.97 C
ANISOU 1030 C THR A 123 2441 930 794 134 -351 5 C
ATOM 1031 O THR A 123 15.891 0.738 20.678 1.00 14.84 O
ANISOU 1031 O THR A 123 2887 1161 1587 39 -555 383 O
ATOM 1032 CB THR A 123 18.046 2.603 19.494 1.00 13.52 C
ANISOU 1032 CB THR A 123 2663 1628 844 139 -62 63 C
ATOM 1033 CG2 THR A 123 17.482 2.772 18.064 1.00 15.20 C
ANISOU 1033 CG2 THR A 123 2980 2083 709 196 123 142 C
ATOM 1034 OG1 THR A 123 19.104 3.528 19.695 1.00 17.28 O
ANISOU 1034 OG1 THR A 123 3197 2035 1333 -135 493 -58 O
ATOM 1035 N SER A 124 14.796 2.392 19.690 1.00 11.18 N
ANISOU 1035 N SER A 124 2547 1163 536 25 -371 220 N
ATOM 1036 CA SER A 124 13.762 1.572 19.133 1.00 11.24 C
ANISOU 1036 CA SER A 124 2525 1115 627 -22 -330 334 C
ATOM 1037 C SER A 124 13.669 1.784 17.651 1.00 10.51 C
ANISOU 1037 C SER A 124 2395 1092 506 79 -154 161 C
ATOM 1038 O SER A 124 13.704 2.910 17.172 1.00 12.38 O
ANISOU 1038 O SER A 124 3198 1046 460 -70 -172 188 O
ATOM 1039 CB SER A 124 12.394 1.871 19.770 1.00 11.30 C
ANISOU 1039 CB SER A 124 2575 1222 493 -78 -212 313 C
ATOM 1040 OG SER A 124 11.311 1.208 19.171 1.00 12.17 O
ANISOU 1040 OG SER A 124 2614 1447 561 -16 -85 114 O
ATOM 1041 N THR A 125 13.514 0.719 16.893 1.00 10.09 N
ANISOU 1041 N THR A 125 2436 953 443 -67 -222 249 N
ATOM 1042 CA THR A 125 13.347 0.749 15.450 1.00 9.95 C
ANISOU 1042 CA THR A 125 2232 1237 308 79 -34 230 C
ATOM 1043 C THR A 125 11.961 0.282 15.085 1.00 10.22 C
ANISOU 1043 C THR A 125 2379 1212 291 -110 -141 134 C
ATOM 1044 O THR A 125 11.562 -0.839 15.438 1.00 12.01 O
ANISOU 1044 O THR A 125 2743 1198 621 -277 -224 210 O
ATOM 1045 CB THR A 125 14.425 -0.093 14.777 1.00 12.87 C
ANISOU 1045 CB THR A 125 2513 1616 759 223 -25 18 C
ATOM 1046 CG2 THR A 125 14.275 -0.064 13.230 1.00 15.67 C
ANISOU 1046 CG2 THR A 125 3010 2168 776 281 182 163 C
ATOM 1047 OG1 THR A 125 15.733 0.388 15.139 1.00 15.31 O
ANISOU 1047 OG1 THR A 125 2508 1965 1344 270 265 -49 O
ATOM 1048 N ARG A 126 11.251 1.134 14.352 1.00 10.26 N
ANISOU 1048 N ARG A 126 2249 1292 356 -188 -24 192 N
ATOM 1049 CA ARG A 126 9.885 0.878 13.931 1.00 10.42 C
ANISOU 1049 CA ARG A 126 2333 1304 321 -326 -3 261 C
ATOM 1050 C ARG A 126 9.836 0.987 12.408 1.00 10.61 C
ANISOU 1050 C ARG A 126 2346 1396 288 -335 -34 199 C
ATOM 1051 O ARG A 126 10.283 1.969 11.843 1.00 13.91 O
ANISOU 1051 O ARG A 126 3278 1676 330 -784 -147 275 O
ATOM 1052 CB ARG A 126 8.943 1.868 14.601 1.00 12.07 C
ANISOU 1052 CB ARG A 126 2311 1862 410 -216 -94 232 C
ATOM 1053 CG ARG A 126 8.895 1.533 16.090 1.00 14.77 C
ANISOU 1053 CG ARG A 126 2755 2318 539 44 -75 6 C
ATOM 1054 CD ARG A 126 8.177 2.447 16.934 1.00 16.54 C
ANISOU 1054 CD ARG A 126 2918 2586 778 75 -147 380 C
ATOM 1055 NE ARG A 126 6.766 2.736 16.699 1.00 16.96 N
ANISOU 1055 NE ARG A 126 2851 2920 671 -72 62 -42 N
ATOM 1056 CZ ARG A 126 5.719 2.121 17.266 1.00 15.41 C
ANISOU 1056 CZ ARG A 126 2713 2500 640 -399 -77 -33 C
ATOM 1057 NH1 ARG A 126 5.819 0.955 17.900 1.00 16.40 N1+
ANISOU 1057 NH1 ARG A 126 3112 2645 470 -186 -222 46 N1+
ATOM 1058 NH2 ARG A 126 4.547 2.646 17.143 1.00 16.99 N
ANISOU 1058 NH2 ARG A 126 2899 2580 973 -502 65 136 N
ATOM 1059 N VAL A 127 9.312 -0.027 11.752 1.00 9.75 N
ANISOU 1059 N VAL A 127 2312 1122 268 -198 37 106 N
ATOM 1060 CA VAL A 127 9.348 -0.107 10.283 1.00 10.20 C
ANISOU 1060 CA VAL A 127 2190 1409 277 -48 168 98 C
ATOM 1061 C VAL A 127 7.941 -0.001 9.785 1.00 9.62 C
ANISOU 1061 C VAL A 127 2177 1181 296 3 174 -12 C
ATOM 1062 O VAL A 127 7.038 -0.720 10.210 1.00 10.80 O
ANISOU 1062 O VAL A 127 2358 1467 278 -148 43 106 O
ATOM 1063 CB VAL A 127 9.971 -1.414 9.841 1.00 11.77 C
ANISOU 1063 CB VAL A 127 2459 1513 500 131 -92 104 C
ATOM 1064 CG1 VAL A 127 9.937 -1.494 8.284 1.00 14.40 C
ANISOU 1064 CG1 VAL A 127 2989 1992 487 267 14 -167 C
ATOM 1065 CG2 VAL A 127 11.368 -1.545 10.373 1.00 15.59 C
ANISOU 1065 CG2 VAL A 127 2743 2174 1004 301 -53 32 C
ATOM 1066 N TYR A 128 7.754 0.946 8.863 1.00 10.02 N
ANISOU 1066 N TYR A 128 2303 1183 321 -85 19 68 N
ATOM 1067 CA TYR A 128 6.483 1.159 8.180 1.00 9.65 C
ANISOU 1067 CA TYR A 128 2143 1253 268 -104 80 102 C
ATOM 1068 C TYR A 128 6.609 0.760 6.696 1.00 10.56 C
ANISOU 1068 C TYR A 128 2261 1256 494 -59 -45 -18 C
ATOM 1069 O TYR A 128 7.657 0.957 6.078 1.00 11.48 O
ANISOU 1069 O TYR A 128 2462 1563 334 -165 91 -164 O
ATOM 1070 CB TYR A 128 6.074 2.622 8.233 1.00 9.59 C
ANISOU 1070 CB TYR A 128 2158 1199 286 -112 9 175 C
ATOM 1071 CG TYR A 128 5.661 3.134 9.616 1.00 9.71 C
ANISOU 1071 CG TYR A 128 2354 1071 263 -126 -34 89 C
ATOM 1072 CD1 TYR A 128 6.600 3.405 10.595 1.00 11.15 C
ANISOU 1072 CD1 TYR A 128 2393 1293 551 -72 -133 26 C
ATOM 1073 CD2 TYR A 128 4.329 3.352 9.919 1.00 10.31 C
ANISOU 1073 CD2 TYR A 128 2272 1069 574 -43 22 191 C
ATOM 1074 CE1 TYR A 128 6.190 3.911 11.861 1.00 11.83 C
ANISOU 1074 CE1 TYR A 128 2604 1552 337 -127 -141 -150 C
ATOM 1075 CE2 TYR A 128 3.917 3.849 11.134 1.00 11.43 C
ANISOU 1075 CE2 TYR A 128 2375 1391 575 -80 248 3 C
ATOM 1076 CZ TYR A 128 4.838 4.126 12.092 1.00 11.26 C
ANISOU 1076 CZ TYR A 128 2496 1329 453 -169 78 63 C
ATOM 1077 OH TYR A 128 4.402 4.599 13.311 1.00 14.08 O
ANISOU 1077 OH TYR A 128 2821 2107 422 63 186 -180 O
ATOM 1078 N GLU A 129 5.534 0.219 6.171 1.00 11.31 N
ANISOU 1078 N GLU A 129 2391 1456 447 -273 -28 -147 N
ATOM 1079 CA AGLU A 129 5.380 -0.132 4.759 0.50 11.39 C
ANISOU 1079 CA AGLU A 129 2382 1423 522 -79 -60 -399 C
ATOM 1080 CA BGLU A 129 5.485 0.000 4.718 0.50 11.97 C
ANISOU 1080 CA BGLU A 129 2481 1525 539 -72 -106 -373 C
ATOM 1081 C GLU A 129 4.289 0.727 4.166 1.00 10.98 C
ANISOU 1081 C GLU A 129 2353 1453 365 -158 -63 -246 C
ATOM 1082 O GLU A 129 3.444 1.205 4.857 1.00 11.46 O
ANISOU 1082 O GLU A 129 2522 1298 533 -38 -108 -76 O
ATOM 1083 CB AGLU A 129 5.016 -1.616 4.649 0.50 12.45 C
ANISOU 1083 CB AGLU A 129 2445 1543 742 -105 -68 -362 C
ATOM 1084 CB BGLU A 129 5.483 -1.483 4.358 0.50 13.55 C
ANISOU 1084 CB BGLU A 129 2731 1639 778 23 -208 -247 C
ATOM 1085 CG AGLU A 129 6.234 -2.518 4.929 0.50 16.98 C
ANISOU 1085 CG AGLU A 129 3152 2085 1213 151 -371 -418 C
ATOM 1086 CG BGLU A 129 4.223 -2.207 4.799 0.50 17.95 C
ANISOU 1086 CG BGLU A 129 3138 2260 1421 -229 -288 -394 C
ATOM 1087 CD AGLU A 129 5.995 -3.950 4.588 0.50 21.61 C
ANISOU 1087 CD AGLU A 129 3957 2285 1968 53 -396 -444 C
ATOM 1088 CD BGLU A 129 4.238 -3.738 4.509 0.50 22.48 C
ANISOU 1088 CD BGLU A 129 3890 2520 2132 -204 -427 -458 C
ATOM 1089 OE1AGLU A 129 5.208 -4.198 3.644 0.50 24.00 O
ANISOU 1089 OE1AGLU A 129 4700 2393 2025 -8 -629 -481 O
ATOM 1090 OE1BGLU A 129 3.164 -4.296 4.248 0.50 24.75 O
ANISOU 1090 OE1BGLU A 129 4267 2436 2701 -416 -332 -252 O
ATOM 1091 OE2AGLU A 129 6.574 -4.808 5.285 0.50 25.35 O1-
ANISOU 1091 OE2AGLU A 129 4717 2766 2149 244 -558 -575 O1-
ATOM 1092 OE2BGLU A 129 5.311 -4.378 4.557 0.50 23.84 O1-
ANISOU 1092 OE2BGLU A 129 4338 2440 2279 -105 -571 -698 O1-
ATOM 1093 N ARG A 130 4.247 0.845 2.841 1.00 12.39 N
ANISOU 1093 N ARG A 130 2664 1652 389 -92 -141 -352 N
ATOM 1094 CA ARG A 130 3.153 1.551 2.203 1.00 12.69 C
ANISOU 1094 CA ARG A 130 2665 1660 494 -64 -143 -153 C
ATOM 1095 C ARG A 130 1.843 0.883 2.486 1.00 13.49 C
ANISOU 1095 C ARG A 130 2664 1720 739 -145 -343 -210 C
ATOM 1096 O ARG A 130 1.722 -0.356 2.378 1.00 15.91 O
ANISOU 1096 O ARG A 130 3167 1460 1418 -55 -649 -226 O
ATOM 1097 CB ARG A 130 3.357 1.634 0.711 1.00 14.77 C
ANISOU 1097 CB ARG A 130 2784 2411 418 -130 -225 -146 C
ATOM 1098 CG ARG A 130 4.555 2.356 0.336 1.00 16.70 C
ANISOU 1098 CG ARG A 130 3200 2524 621 -209 -20 352 C
ATOM 1099 CD ARG A 130 4.264 3.781 0.216 1.00 19.29 C
ANISOU 1099 CD ARG A 130 3263 2415 1650 -185 -320 -214 C
ATOM 1100 NE ARG A 130 5.418 4.476 -0.342 1.00 20.01 N
ANISOU 1100 NE ARG A 130 3363 2054 2183 -84 -337 312 N
ATOM 1101 CZ ARG A 130 5.490 5.782 -0.530 1.00 16.19 C
ANISOU 1101 CZ ARG A 130 3076 1983 1092 -71 -273 133 C
ATOM 1102 NH1 ARG A 130 4.450 6.504 -0.351 1.00 16.77 N1+
ANISOU 1102 NH1 ARG A 130 3245 2213 913 -69 -165 70 N1+
ATOM 1103 NH2 ARG A 130 6.626 6.322 -0.899 1.00 19.62 N
ANISOU 1103 NH2 ARG A 130 3530 2656 1265 -115 244 500 N
ATOM 1104 N ALA A 131 0.815 1.660 2.769 1.00 15.10 N
ANISOU 1104 N ALA A 131 2719 1744 1274 -197 -385 -224 N
ATOM 1105 CA ALA A 131 -0.490 1.075 3.058 1.00 18.72 C
ANISOU 1105 CA ALA A 131 2899 2130 2083 -258 -336 -128 C
ATOM 1106 C ALA A 131 -1.124 0.543 1.782 1.00 21.44 C
ANISOU 1106 C ALA A 131 3196 2358 2590 -340 -350 -139 C
ATOM 1107 O ALA A 131 -0.721 0.956 0.699 1.00 22.42 O
ANISOU 1107 O ALA A 131 3348 2640 2530 -369 -808 -41 O
ATOM 1108 CB ALA A 131 -1.377 2.088 3.806 1.00 21.27 C
ANISOU 1108 CB ALA A 131 3064 2482 2533 -292 -95 -144 C
TER
HETATM 1109 CAAAFBZ A 133 7.319 8.707 17.358 0.50 19.36 C
ANISOU 1109 CAAAFBZ A 133 3012 2713 1631 150 -18 1043 C
HETATM 1110 CAABFBZ A 133 7.670 8.115 17.789 0.50 17.24 C
ANISOU 1110 CAABFBZ A 133 3225 1893 1431 253 -353 -716 C
HETATM 1111 CADAFBZ A 133 6.004 7.792 22.273 0.50 20.69 C
ANISOU 1111 CADAFBZ A 133 2930 2673 2255 130 189 -210 C
HETATM 1112 CADBFBZ A 133 5.407 7.397 22.237 0.50 17.14 C
ANISOU 1112 CADBFBZ A 133 3194 2117 1199 421 -295 -579 C
HETATM 1113 CAEAFBZ A 133 5.131 8.523 21.468 0.50 21.30 C
ANISOU 1113 CAEAFBZ A 133 3075 2862 2155 117 219 -2 C
HETATM 1114 CAEBFBZ A 133 4.440 7.066 21.291 0.50 17.59 C
ANISOU 1114 CAEBFBZ A 133 3120 2252 1310 451 -230 -420 C
HETATM 1115 CAFAFBZ A 133 6.979 7.028 21.642 0.50 20.05 C
ANISOU 1115 CAFAFBZ A 133 2984 2874 1760 290 -144 -268 C
HETATM 1116 CAFBFBZ A 133 6.672 7.775 21.776 0.50 17.72 C
ANISOU 1116 CAFBFBZ A 133 3163 2376 1192 196 -531 -857 C
HETATM 1117 CAGAFBZ A 133 5.206 8.521 20.079 0.50 20.59 C
ANISOU 1117 CAGAFBZ A 133 3099 2590 2134 167 58 -167 C
HETATM 1118 CAGBFBZ A 133 4.700 7.125 19.931 0.50 17.27 C
ANISOU 1118 CAGBFBZ A 133 2999 2270 1289 374 -324 -275 C
HETATM 1119 CAHAFBZ A 133 7.051 7.021 20.243 0.50 20.23 C
ANISOU 1119 CAHAFBZ A 133 3111 2835 1738 151 -156 -511 C
HETATM 1120 CAHBFBZ A 133 6.941 7.835 20.406 0.50 18.60 C
ANISOU 1120 CAHBFBZ A 133 3253 2568 1244 361 -582 -615 C
HETATM 1121 CAIAFBZ A 133 6.523 6.357 17.312 0.50 19.46 C
ANISOU 1121 CAIAFBZ A 133 3373 2155 1863 184 168 228 C
HETATM 1122 CAIBFBZ A 133 6.179 6.138 17.358 0.50 16.08 C
ANISOU 1122 CAIBFBZ A 133 3130 2063 916 351 -325 -576 C
HETATM 1123 CAJAFBZ A 133 5.988 6.129 15.874 0.50 18.80 C
ANISOU 1123 CAJAFBZ A 133 3635 1802 1703 51 173 480 C
HETATM 1124 CAJBFBZ A 133 6.014 6.112 15.824 0.50 15.91 C
ANISOU 1124 CAJBFBZ A 133 3290 1898 855 277 -295 -517 C
HETATM 1125 CAKAFBZ A 133 6.184 7.770 19.438 0.50 20.10 C
ANISOU 1125 CAKAFBZ A 133 3134 2494 2006 179 -6 -143 C
HETATM 1126 CAKBFBZ A 133 5.960 7.510 19.488 0.50 16.42 C
ANISOU 1126 CAKBFBZ A 133 2972 2233 1032 427 -415 -613 C
HETATM 1127 CALAFBZ A 133 6.241 7.766 17.885 0.50 20.53 C
ANISOU 1127 CALAFBZ A 133 3282 2401 2117 73 249 88 C
HETATM 1128 CALBFBZ A 133 6.267 7.554 18.001 0.50 16.96 C
ANISOU 1128 CALBFBZ A 133 3272 2246 927 322 -177 -853 C
HETATM 1129 OABAFBZ A 133 5.635 7.109 15.177 0.50 18.90 O
ANISOU 1129 OABAFBZ A 133 3578 1772 1828 60 219 283 O
HETATM 1130 OABBFBZ A 133 5.676 7.157 15.235 0.50 17.64 O
ANISOU 1130 OABBFBZ A 133 3420 2075 1207 274 -84 -257 O
HETATM 1131 OACAFBZ A 133 5.926 4.939 15.490 0.50 19.29 O
ANISOU 1131 OACAFBZ A 133 3884 1939 1503 297 93 -5 O
HETATM 1132 OACBFBZ A 133 6.126 5.002 15.267 0.50 16.26 O
ANISOU 1132 OACBFBZ A 133 3781 1949 448 709 -541 -494 O
HETATM 1133 O HOH A 134 10.455 22.054 12.801 1.00 9.68 O
ANISOU 1133 O HOH A 134 2346 1032 298 45 18 73 O
HETATM 1134 O HOH A 135 18.691 0.008 22.066 1.00 11.73 O
ANISOU 1134 O HOH A 135 2394 1239 823 208 -75 84 O
HETATM 1135 O HOH A 136 2.745 -7.735 16.893 1.00 39.72 O
ANISOU 1135 O HOH A 136 6034 4803 4253 1312 -836 -1828 O
HETATM 1136 O HOH A 137 6.281 23.748 -4.014 1.00 42.77 O
ANISOU 1136 O HOH A 137 4664 6272 5315 424 -230 801 O
HETATM 1137 O HOH A 138 7.220 24.848 12.379 1.00 11.52 O
ANISOU 1137 O HOH A 138 2225 1593 556 -37 48 -320 O
HETATM 1138 O HOH A 139 20.117 16.981 24.217 1.00 45.36 O
ANISOU 1138 O HOH A 139 5173 4090 7971 -240 -1532 969 O
HETATM 1139 O HOH A 140 -3.785 -0.601 22.289 1.00 12.93 O
ANISOU 1139 O HOH A 140 2556 1621 733 -248 -88 246 O
HETATM 1140 O HOH A 141 1.107 20.239 5.139 1.00 14.89 O
ANISOU 1140 O HOH A 141 2782 2004 870 -116 -207 314 O
HETATM 1141 O HOH A 142 -3.731 -1.145 19.583 1.00 13.97 O
ANISOU 1141 O HOH A 142 2408 1806 1092 -441 74 246 O
HETATM 1142 O HOH A 143 -8.225 5.546 21.604 1.00 45.80 O
ANISOU 1142 O HOH A 143 3725 7987 5688 -1237 405 1498 O
HETATM 1143 O HOH A 144 8.595 21.595 26.655 1.00 68.64 O
ANISOU 1143 O HOH A 144 16849 5599 3630 2524 -2319 -1690 O
HETATM 1144 O HOH A 145 6.313 19.934 29.712 1.00105.05 O
ANISOU 1144 O HOH A 145 18034 17780 4099 5741 1291 523 O
HETATM 1145 O HOH A 146 11.877 12.407 12.160 1.00 11.51 O
ANISOU 1145 O HOH A 146 2748 1231 393 123 233 60 O
HETATM 1146 O HOH A 147 1.800 3.883 19.630 1.00 34.68 O
ANISOU 1146 O HOH A 147 5302 4951 2923 257 258 1324 O
HETATM 1147 O HOH A 148 -6.866 5.144 23.866 1.00 88.16 O
ANISOU 1147 O HOH A 148 18241 8832 6422 -5580 3262 -3958 O
HETATM 1148 O HOH A 149 -3.562 3.185 28.808 1.00 30.99 O
ANISOU 1148 O HOH A 149 4917 3846 3008 28 -1140 135 O
HETATM 1149 O HOH A 150 9.781 23.013 5.438 1.00 13.95 O
ANISOU 1149 O HOH A 150 2600 2210 490 315 -50 42 O
HETATM 1150 O HOH A 151 0.049 -2.559 9.802 1.00 32.86 O
ANISOU 1150 O HOH A 151 3717 4612 4156 -1244 -745 1379 O
HETATM 1151 O HOH A 152 -4.667 -2.372 24.206 1.00 11.83 O
ANISOU 1151 O HOH A 152 2446 1503 545 -64 -81 240 O
HETATM 1152 O HOH A 153 1.710 5.759 0.130 1.00 16.90 O
ANISOU 1152 O HOH A 153 3593 2000 827 -349 -194 -246 O
HETATM 1153 O HOH A 154 -4.982 3.751 30.948 1.00 36.04 O
ANISOU 1153 O HOH A 154 6273 3634 3786 261 997 466 O
HETATM 1154 O HOH A 155 4.704 -3.545 16.263 1.00 53.00 O
ANISOU 1154 O HOH A 155 5425 4837 9873 1097 -2017 1278 O
HETATM 1155 O HOH A 156 3.114 8.276 30.910 1.00 25.74 O
ANISOU 1155 O HOH A 156 4468 2662 2650 436 512 553 O
HETATM 1156 O HOH A 157 3.521 11.395 19.314 1.00 16.02 O
ANISOU 1156 O HOH A 157 2856 2219 1010 -187 270 197 O
HETATM 1157 O HOH A 158 8.872 10.506 21.424 1.00 14.52 O
ANISOU 1157 O HOH A 158 3166 1609 741 -185 258 124 O
HETATM 1158 O HOH A 159 8.845 -3.027 20.091 1.00 17.71 O
ANISOU 1158 O HOH A 159 3454 2242 1030 88 -20 -322 O
HETATM 1159 O HOH A 160 -0.597 14.332 6.411 1.00 15.73 O
ANISOU 1159 O HOH A 160 3253 1653 1070 1 -225 27 O
HETATM 1160 O HOH A 161 21.846 9.918 5.449 1.00 33.20 O
ANISOU 1160 O HOH A 161 3712 5216 3683 299 1009 -633 O
HETATM 1161 O HOH A 162 12.453 10.484 31.531 1.00140.81 O
ANISOU 1161 O HOH A 162 30132 15157 8212 -11415 -858 -1690 O
HETATM 1162 O HOH A 163 1.703 15.760 -0.147 1.00 18.93 O
ANISOU 1162 O HOH A 163 4462 2096 636 -169 -683 -221 O
HETATM 1163 O HOH A 164 5.886 -7.408 13.349 1.00 38.42 O
ANISOU 1163 O HOH A 164 5616 2630 6351 -947 -2048 1162 O
HETATM 1164 O HOH A 165 18.177 0.833 1.685 1.00 37.98 O
ANISOU 1164 O HOH A 165 3872 8216 2342 -62 673 -448 O
HETATM 1165 O HOH A 166 4.406 -4.502 26.339 1.00 44.34 O
ANISOU 1165 O HOH A 166 7158 7231 2457 1185 1131 281 O
HETATM 1166 O HOH A 167 16.210 18.837 14.202 1.00 17.80 O
ANISOU 1166 O HOH A 167 3592 2059 1111 -140 -233 -62 O
HETATM 1167 O HOH A 168 13.106 21.646 19.888 1.00 17.62 O
ANISOU 1167 O HOH A 168 3297 2814 583 -253 -89 27 O
HETATM 1168 O HOH A 169 6.396 11.418 19.573 1.00 15.88 O
ANISOU 1168 O HOH A 169 2864 1791 1377 -144 148 56 O
HETATM 1169 O HOH A 170 13.100 12.122 -3.273 1.00 63.91 O
ANISOU 1169 O HOH A 170 11696 7126 5460 -1740 -757 145 O
HETATM 1170 O HOH A 171 16.389 21.123 7.295 1.00 18.19 O
ANISOU 1170 O HOH A 171 3855 1614 1442 -412 78 207 O
HETATM 1171 O HOH A 172 15.233 9.057 3.243 1.00 18.25 O
ANISOU 1171 O HOH A 172 3906 1883 1145 -558 488 118 O
HETATM 1172 O HOH A 173 4.141 27.136 2.505 1.00 17.62 O
ANISOU 1172 O HOH A 173 3271 2043 1381 51 -209 17 O
HETATM 1173 O HOH A 174 14.490 0.676 31.721 1.00 29.44 O
ANISOU 1173 O HOH A 174 4880 4072 2233 -133 -265 932 O
HETATM 1174 O HOH A 175 20.161 20.241 14.212 1.00 25.36 O
ANISOU 1174 O HOH A 175 4523 2671 2441 53 116 -326 O
HETATM 1175 O HOH A 176 1.429 2.512 -2.579 1.00 39.05 O
ANISOU 1175 O HOH A 176 6417 6156 2263 787 -471 -1260 O
HETATM 1176 O HOH A 177 -5.951 3.201 27.293 1.00 29.56 O
ANISOU 1176 O HOH A 177 3773 3339 4117 -360 -237 -523 O
HETATM 1177 O HOH A 178 11.465 -3.105 13.710 1.00 19.03 O
ANISOU 1177 O HOH A 178 4403 1803 1023 -232 -49 84 O
HETATM 1178 O HOH A 179 14.045 -2.182 31.402 1.00 35.61 O
ANISOU 1178 O HOH A 179 5368 4648 3513 1101 1456 554 O
HETATM 1179 O HOH A 180 2.902 13.842 18.210 1.00 19.96 O
ANISOU 1179 O HOH A 180 3123 2095 2365 -285 50 275 O
HETATM 1180 O HOH A 181 18.960 17.860 14.834 1.00 30.91 O
ANISOU 1180 O HOH A 181 4741 3266 3736 -324 -871 201 O
HETATM 1181 O HOH A 182 2.622 6.759 13.707 1.00 20.31 O
ANISOU 1181 O HOH A 182 3374 1935 2408 -330 882 -275 O
HETATM 1182 O HOH A 183 19.778 20.030 4.928 1.00 46.93 O
ANISOU 1182 O HOH A 183 7244 3389 7196 -726 -1552 -203 O
HETATM 1183 O HOH A 184 2.882 0.886 18.682 1.00 20.72 O
ANISOU 1183 O HOH A 184 3034 3932 906 -1233 208 -122 O
HETATM 1184 O HOH A 185 1.898 12.695 14.263 1.00 21.31 O
ANISOU 1184 O HOH A 185 3925 2828 1343 -98 248 1191 O
HETATM 1185 O HOH A 186 1.674 26.185 2.278 1.00 18.15 O
ANISOU 1185 O HOH A 186 3239 1843 1813 111 -88 -229 O
HETATM 1186 O HOH A 187 7.028 27.670 11.942 1.00 20.26 O
ANISOU 1186 O HOH A 187 2962 2669 2065 773 -511 -485 O
HETATM 1187 O HOH A 188 -0.644 18.705 3.772 1.00 19.74 O
ANISOU 1187 O HOH A 188 3796 1877 1826 73 -1038 105 O
HETATM 1188 O HOH A 189 2.973 5.839 16.790 1.00 73.20 O
ANISOU 1188 O HOH A 189 13250 10320 4240 -2967 -116 -1820 O
HETATM 1189 O HOH A 190 14.722 25.125 17.374 1.00 16.90 O
ANISOU 1189 O HOH A 190 2945 1889 1585 -9 -601 -138 O
HETATM 1190 O HOH A 191 11.381 -2.746 0.864 1.00 18.74 O
ANISOU 1190 O HOH A 191 4166 1762 1193 -260 -44 2 O
HETATM 1191 O HOH A 192 2.225 9.807 17.398 1.00 17.93 O
ANISOU 1191 O HOH A 192 3281 2407 1123 -220 278 -7 O
HETATM 1192 O HOH A 193 11.517 -5.762 21.044 1.00 23.78 O
ANISOU 1192 O HOH A 193 4663 1204 3165 74 297 618 O
HETATM 1193 O HOH A 194 -6.097 0.823 22.091 1.00 18.77 O
ANISOU 1193 O HOH A 194 3086 1637 2405 -265 -867 519 O
HETATM 1194 O HOH A 195 0.232 3.005 34.679 1.00 23.81 O
ANISOU 1194 O HOH A 195 5753 2599 694 555 216 -73 O
HETATM 1195 O HOH A 196 20.255 11.058 20.158 1.00 39.89 O
ANISOU 1195 O HOH A 196 5678 3992 5486 -922 -501 -1088 O
HETATM 1196 O HOH A 197 6.306 -0.507 1.379 1.00 20.23 O
ANISOU 1196 O HOH A 197 3211 2989 1486 -116 412 -605 O
HETATM 1197 O HOH A 198 3.500 3.676 35.727 1.00 25.23 O
ANISOU 1197 O HOH A 198 5940 2600 1047 -1136 -297 165 O
HETATM 1198 O HOH A 199 22.695 6.191 29.193 1.00 43.53 O
ANISOU 1198 O HOH A 199 7814 2936 5788 296 -2537 993 O
HETATM 1199 O AHOH A 200 1.027 15.694 18.510 0.50 17.42 O
ANISOU 1199 O AHOH A 200 3981 2159 479 -410 434 118 O
HETATM 1200 O BHOH A 200 0.482 18.580 19.254 0.50 24.34 O
ANISOU 1200 O BHOH A 200 3661 2540 3047 -1077 -1852 1651 O
HETATM 1201 O HOH A 201 14.779 1.567 29.188 1.00 24.77 O
ANISOU 1201 O HOH A 201 3790 4471 1149 1031 -585 595 O
HETATM 1202 O HOH A 202 2.196 -3.676 24.702 1.00 23.80 O
ANISOU 1202 O HOH A 202 3329 4081 1630 581 -198 -158 O
HETATM 1203 O HOH A 203 8.675 -3.499 22.947 1.00 29.18 O
ANISOU 1203 O HOH A 203 6296 2266 2525 -841 1128 -488 O
HETATM 1204 O HOH A 204 5.171 22.595 24.114 1.00 24.32 O
ANISOU 1204 O HOH A 204 4725 2677 1838 1057 210 -22 O
HETATM 1205 O HOH A 205 15.406 19.770 27.364 1.00 24.31 O
ANISOU 1205 O HOH A 205 5891 2146 1199 -710 -789 -196 O
HETATM 1206 O HOH A 206 0.496 5.041 32.287 1.00 22.73 O
ANISOU 1206 O HOH A 206 4770 2785 1081 -279 234 -82 O
HETATM 1207 O HOH A 207 0.276 3.416 -0.275 1.00 21.46 O
ANISOU 1207 O HOH A 207 3585 2297 2268 -183 -773 -487 O
HETATM 1208 O HOH A 208 -1.902 15.884 17.808 1.00 24.41 O
ANISOU 1208 O HOH A 208 5391 2321 1560 -276 862 -669 O
HETATM 1209 O HOH A 209 17.845 13.911 21.772 1.00 20.67 O
ANISOU 1209 O HOH A 209 3594 3068 1192 -228 -111 -433 O
HETATM 1210 O HOH A 210 11.324 13.592 -5.357 1.00 45.18 O
ANISOU 1210 O HOH A 210 4984 3635 8545 -544 2100 -1355 O
HETATM 1211 O HOH A 211 6.576 8.372 12.992 1.00 21.00 O
ANISOU 1211 O HOH A 211 3325 3779 874 -575 47 159 O
HETATM 1212 O HOH A 212 -2.673 20.049 1.501 1.00 26.72 O
ANISOU 1212 O HOH A 212 4875 3601 1676 -2132 204 -53 O
HETATM 1213 O HOH A 213 15.386 -2.645 3.840 1.00 38.63 O
ANISOU 1213 O HOH A 213 8441 2451 3783 -36 1154 -128 O
HETATM 1214 O HOH A 214 2.851 -2.549 17.656 1.00 25.53 O
ANISOU 1214 O HOH A 214 4868 3150 1680 656 -754 199 O
HETATM 1215 O HOH A 215 7.012 -3.033 30.534 1.00 24.64 O
ANISOU 1215 O HOH A 215 6193 1802 1366 -370 955 -12 O
HETATM 1216 O HOH A 216 5.016 -1.572 25.409 1.00 23.14 O
ANISOU 1216 O HOH A 216 3820 3373 1600 459 -117 -471 O
HETATM 1217 O HOH A 217 13.187 21.173 28.471 1.00 25.65 O
ANISOU 1217 O HOH A 217 5384 2790 1569 228 -407 -275 O
HETATM 1218 O HOH A 218 18.327 11.294 24.301 1.00 31.54 O
ANISOU 1218 O HOH A 218 4228 1744 6009 386 -604 296 O
HETATM 1219 O HOH A 219 9.022 12.051 30.743 1.00 23.96 O
ANISOU 1219 O HOH A 219 5086 2753 1265 -23 643 344 O
HETATM 1220 O HOH A 220 17.543 13.416 28.020 1.00 26.60 O
ANISOU 1220 O HOH A 220 4312 2814 2980 442 -1092 572 O
HETATM 1221 O HOH A 221 4.823 10.044 29.236 1.00 24.29 O
ANISOU 1221 O HOH A 221 5723 2548 955 -271 113 504 O
HETATM 1222 O HOH A 222 18.765 4.770 2.368 1.00 27.39 O
ANISOU 1222 O HOH A 222 6869 3071 464 796 -554 -651 O
HETATM 1223 O HOH A 223 17.382 9.039 16.433 1.00 25.12 O
ANISOU 1223 O HOH A 223 4397 3151 1995 576 20 637 O
HETATM 1224 O HOH A 224 -7.181 9.454 19.644 1.00 33.25 O
ANISOU 1224 O HOH A 224 3400 7454 1777 74 429 -49 O
HETATM 1225 O HOH A 225 -1.888 20.176 11.480 1.00 35.86 O
ANISOU 1225 O HOH A 225 5466 2449 5710 -715 3383 -332 O
HETATM 1226 O HOH A 226 18.598 17.341 2.345 1.00 31.17 O
ANISOU 1226 O HOH A 226 5497 3667 2679 -220 1450 -733 O
HETATM 1227 O HOH A 227 -7.973 6.294 14.894 1.00 38.78 O
ANISOU 1227 O HOH A 227 5038 3190 6504 -1106 -1770 837 O
HETATM 1228 O HOH A 228 0.186 4.987 18.323 1.00 45.69 O
ANISOU 1228 O HOH A 228 6180 5501 5678 -2024 -1767 2338 O
HETATM 1229 O HOH A 229 2.408 -5.352 19.808 1.00 34.98 O
ANISOU 1229 O HOH A 229 5308 4919 3063 497 -193 -1205 O
HETATM 1230 O HOH A 230 -0.562 -5.133 17.441 1.00 33.60 O
ANISOU 1230 O HOH A 230 3772 2570 6422 352 968 1176 O
HETATM 1231 O HOH A 231 -4.800 11.591 13.359 1.00 33.49 O
ANISOU 1231 O HOH A 231 3963 6547 2214 1486 139 1259 O
HETATM 1232 O HOH A 232 7.530 -5.977 15.286 1.00 80.48 O
ANISOU 1232 O HOH A 232 10538 12355 7686 -6170 -7045 -452 O
HETATM 1233 O HOH A 233 19.735 10.033 17.639 1.00 30.90 O
ANISOU 1233 O HOH A 233 4804 3603 3332 846 1114 564 O
HETATM 1234 O HOH A 234 -7.692 6.520 19.026 1.00 31.28 O
ANISOU 1234 O HOH A 234 4084 3847 3953 364 576 -736 O
HETATM 1235 O HOH A 235 20.076 16.550 20.290 1.00 52.78 O
ANISOU 1235 O HOH A 235 5700 5686 8665 661 -123 -3854 O
HETATM 1236 O HOH A 236 23.782 11.638 18.115 1.00 42.02 O
ANISOU 1236 O HOH A 236 3294 6129 6542 -283 416 -1169 O
HETATM 1237 O HOH A 237 8.726 -6.070 20.158 1.00 34.62 O
ANISOU 1237 O HOH A 237 4693 4189 4272 786 664 -11 O
HETATM 1238 O HOH A 238 5.338 -1.772 19.859 1.00 36.95 O
ANISOU 1238 O HOH A 238 4304 4969 4765 -1778 2222 -2405 O
HETATM 1239 O HOH A 239 21.042 5.142 21.515 1.00 30.13 O
ANISOU 1239 O HOH A 239 6246 3234 1968 1457 -306 280 O
HETATM 1240 O HOH A 240 -6.869 13.782 18.029 1.00 47.09 O
ANISOU 1240 O HOH A 240 6348 4508 7036 -1096 2167 -2747 O
HETATM 1241 O HOH A 241 9.184 21.238 29.603 1.00 26.02 O
ANISOU 1241 O HOH A 241 5215 2969 1702 1136 56 -459 O
HETATM 1242 O HOH A 242 0.039 7.893 17.515 1.00 25.91 O
ANISOU 1242 O HOH A 242 3869 4367 1608 277 422 489 O
HETATM 1243 O HOH A 243 17.722 0.847 13.302 1.00 29.71 O
ANISOU 1243 O HOH A 243 3747 3458 4082 -122 1083 -608 O
HETATM 1244 O HOH A 244 0.880 7.214 -1.985 1.00 25.47 O
ANISOU 1244 O HOH A 244 4313 4119 1245 -197 -529 566 O
HETATM 1245 O HOH A 245 15.123 8.320 -0.936 1.00 24.67 O
ANISOU 1245 O HOH A 245 4940 2424 2008 -697 439 -116 O
HETATM 1246 O HOH A 246 21.160 7.942 15.070 1.00 45.14 O
ANISOU 1246 O HOH A 246 3754 5927 7469 618 999 2266 O
HETATM 1247 O HOH A 247 -2.215 4.503 -0.412 1.00 36.07 O
ANISOU 1247 O HOH A 247 4863 4499 4343 -855 -778 1421 O
HETATM 1248 O HOH A 248 5.842 -2.611 22.983 1.00 38.56 O
ANISOU 1248 O HOH A 248 5494 6846 2309 2244 -674 -905 O
HETATM 1249 O HOH A 249 16.473 -5.617 17.875 1.00 31.29 O
ANISOU 1249 O HOH A 249 4605 1957 5325 626 -1946 -1006 O
HETATM 1250 O HOH A 250 5.087 29.029 4.242 1.00 29.35 O
ANISOU 1250 O HOH A 250 4255 2724 4170 -633 -326 -1303 O
HETATM 1251 O HOH A 251 15.625 9.803 1.009 1.00 94.35 O
ANISOU 1251 O HOH A 251 7168 24866 3812 -5015 1799 5203 O
HETATM 1252 O HOH A 252 15.918 22.196 4.736 1.00 63.02 O
ANISOU 1252 O HOH A 252 13743 6233 3967 -4413 -1817 4561 O
HETATM 1253 O HOH A 253 5.194 19.261 -8.206 1.00 33.15 O
ANISOU 1253 O HOH A 253 3920 5609 3065 -26 116 303 O
HETATM 1254 O HOH A 254 19.681 14.785 18.344 1.00 26.87 O
ANISOU 1254 O HOH A 254 3078 3293 3837 -303 -87 1363 O
HETATM 1255 O HOH A 255 9.004 -3.969 -1.933 1.00 34.94 O
ANISOU 1255 O HOH A 255 7768 3388 2119 -1319 768 -196 O
HETATM 1256 O HOH A 256 11.184 22.268 26.602 1.00 32.10 O
ANISOU 1256 O HOH A 256 7341 3028 1827 -94 398 -315 O
HETATM 1257 O HOH A 257 6.189 19.155 -2.709 1.00 46.40 O
ANISOU 1257 O HOH A 257 8440 5739 3451 2690 2087 1249 O
HETATM 1258 O HOH A 258 8.824 4.952 32.755 1.00 26.93 O
ANISOU 1258 O HOH A 258 4575 2836 2821 -608 -1559 453 O
HETATM 1259 O HOH A 259 -7.859 9.805 22.474 1.00 52.62 O
ANISOU 1259 O HOH A 259 6816 10333 2842 552 -1183 856 O
HETATM 1260 O HOH A 260 20.724 4.395 17.579 1.00 33.71 O
ANISOU 1260 O HOH A 260 4561 4221 4025 669 1688 1968 O
HETATM 1261 O HOH A 261 10.741 -3.859 28.323 1.00 77.55 O
ANISOU 1261 O HOH A 261 7744 9496 12223 3430 1318 4660 O
HETATM 1262 O HOH A 262 6.249 12.303 16.699 1.00 31.04 O
ANISOU 1262 O HOH A 262 2701 7111 1982 -399 338 1449 O
HETATM 1263 O HOH A 263 9.329 14.977 -5.866 1.00 39.76 O
ANISOU 1263 O HOH A 263 5929 5082 4093 3 -158 1783 O
HETATM 1264 O HOH A 264 18.349 11.628 21.882 1.00 41.47 O
ANISOU 1264 O HOH A 264 3838 7289 4629 1650 -1235 -2723 O
HETATM 1265 O HOH A 265 2.530 -6.395 11.756 1.00 34.26 O
ANISOU 1265 O HOH A 265 5386 3945 3686 -525 1086 441 O
HETATM 1266 O HOH A 266 4.583 28.303 0.134 1.00 38.68 O
ANISOU 1266 O HOH A 266 8147 3725 2825 -943 -825 1111 O
HETATM 1267 O AHOH A 267 7.889 2.352 -2.875 0.50 24.99 O
ANISOU 1267 O AHOH A 267 4730 3034 1732 -290 -226 181 O
HETATM 1268 O BHOH A 267 9.611 3.093 -2.738 0.50 22.68 O
ANISOU 1268 O BHOH A 267 5258 1765 1595 292 -453 -494 O
HETATM 1269 O HOH A 268 9.421 28.808 15.294 1.00 23.05 O
ANISOU 1269 O HOH A 268 4149 2018 2589 66 357 83 O
HETATM 1270 O HOH A 269 3.218 21.290 23.989 1.00 35.06 O
ANISOU 1270 O HOH A 269 7662 3086 2571 1575 1794 40 O
HETATM 1271 O HOH A 270 3.972 16.612 -2.007 1.00 29.91 O
ANISOU 1271 O HOH A 270 5980 3533 1850 -959 413 173 O
HETATM 1272 O HOH A 271 17.666 21.238 14.942 1.00 23.86 O
ANISOU 1272 O HOH A 271 5029 2625 1411 -184 -638 -346 O
HETATM 1273 O HOH A 272 -9.448 4.024 20.676 1.00 22.88 O
ANISOU 1273 O HOH A 272 4855 2166 1671 500 1072 337 O
HETATM 1274 O HOH A 273 -3.765 1.768 15.050 1.00 23.02 O
ANISOU 1274 O HOH A 273 4091 2132 2521 420 1189 258 O
HETATM 1275 O HOH A 274 13.002 -7.467 20.088 1.00 43.08 O
ANISOU 1275 O HOH A 274 5732 2404 8230 813 -1166 -713 O
HETATM 1276 O AHOH A 275 4.484 11.673 14.838 0.50 23.95 O
ANISOU 1276 O AHOH A 275 4000 3413 1685 658 -800 -816 O
HETATM 1277 O BHOH A 275 4.123 13.245 15.571 0.50 25.30 O
ANISOU 1277 O BHOH A 275 5706 3019 888 -351 -240 -217 O
HETATM 1278 O HOH A 276 20.843 2.493 21.395 1.00 35.83 O
ANISOU 1278 O HOH A 276 4158 7085 2368 -150 -416 -1456 O
HETATM 1279 O HOH A 277 -3.663 17.977 23.869 1.00108.93 O
ANISOU 1279 O HOH A 277 3508 13818 24062 5342 906 -9142 O
HETATM 1280 O HOH A 278 20.488 4.934 28.349 0.50 16.76 O
ANISOU 1280 O HOH A 278 3462 2050 853 66 -205 335 O
HETATM 1281 O HOH A 279 17.221 21.153 17.700 1.00 30.20 O
ANISOU 1281 O HOH A 279 4475 5314 1685 -204 -348 129 O
HETATM 1282 O AHOH A 280 11.478 24.741 4.310 0.50 27.35 O
ANISOU 1282 O AHOH A 280 3455 5045 1891 -1618 581 1843 O
HETATM 1283 O BHOH A 280 12.706 25.401 6.083 0.50 23.12 O
ANISOU 1283 O BHOH A 280 6067 2161 555 -502 79 420 O
HETATM 1284 O HOH A 281 -1.531 14.222 21.851 1.00 31.26 O
ANISOU 1284 O HOH A 281 4224 5200 2452 -366 170 -404 O
HETATM 1285 O HOH A 282 18.341 -2.172 14.333 1.00 31.30 O
ANISOU 1285 O HOH A 282 4596 4143 3153 -190 25 1316 O
HETATM 1286 O HOH A 283 19.209 20.523 7.253 1.00 36.27 O
ANISOU 1286 O HOH A 283 6135 3405 4239 -1275 1764 -1675 O
HETATM 1287 O HOH A 284 -1.652 9.272 26.208 1.00 43.27 O
ANISOU 1287 O HOH A 284 6805 4642 4991 -80 2437 68 O
HETATM 1288 O HOH A 285 0.394 9.025 29.392 1.00 38.87 O
ANISOU 1288 O HOH A 285 7352 4468 2950 -994 1533 936 O
HETATM 1289 O HOH A 286 13.304 28.441 7.857 1.00 33.83 O
ANISOU 1289 O HOH A 286 5952 5175 1727 -441 -484 -743 O
HETATM 1290 O HOH A 287 11.822 -3.130 24.855 1.00 28.39 O
ANISOU 1290 O HOH A 287 6580 1965 2241 -230 1418 385 O
HETATM 1291 O HOH A 288 3.044 -2.319 1.125 1.00 33.38 O
ANISOU 1291 O HOH A 288 5236 3165 4282 81 102 -1973 O
HETATM 1292 O HOH A 289 12.340 -1.430 34.233 1.00 42.37 O
ANISOU 1292 O HOH A 289 6520 6621 2956 1741 428 2556 O
HETATM 1293 O HOH A 290 21.861 11.619 7.681 1.00 38.58 O
ANISOU 1293 O HOH A 290 4208 4608 5842 -556 -973 1615 O
HETATM 1294 O HOH A 291 6.543 21.653 -1.448 1.00 33.87 O
ANISOU 1294 O HOH A 291 6646 4162 2058 -344 1430 -436 O
HETATM 1295 O HOH A 292 12.823 6.160 32.965 1.00 63.17 O
ANISOU 1295 O HOH A 292 8834 12935 2231 -77 -3449 -2709 O
HETATM 1296 O HOH A 293 -4.078 11.781 25.808 1.00 41.59 O
ANISOU 1296 O HOH A 293 6129 5286 4385 -405 519 271 O
HETATM 1297 O HOH A 294 -2.719 -1.920 3.826 1.00 44.12 O
ANISOU 1297 O HOH A 294 5346 4798 6617 -2008 -477 -108 O
HETATM 1298 O HOH A 295 -2.362 18.880 16.062 1.00 41.50 O
ANISOU 1298 O HOH A 295 4039 5474 6252 766 1082 -1861 O
HETATM 1299 O HOH A 296 15.113 4.118 32.592 1.00 40.75 O
ANISOU 1299 O HOH A 296 7333 4978 3172 -527 -1145 227 O
HETATM 1300 O HOH A 297 17.167 12.467 30.593 1.00 37.09 O
ANISOU 1300 O HOH A 297 6074 5612 2406 970 -945 299 O
HETATM 1301 O HOH A 298 11.709 27.883 5.387 1.00 35.46 O
ANISOU 1301 O HOH A 298 6601 3820 3049 0 835 901 O
HETATM 1302 O HOH A 299 -2.052 12.843 23.427 1.00 39.97 O
ANISOU 1302 O HOH A 299 3648 5358 6180 -208 656 -437 O
HETATM 1303 O HOH A 300 10.106 -0.757 34.531 1.00 42.86 O
ANISOU 1303 O HOH A 300 5975 6819 3489 -27 -76 1404 O
HETATM 1304 O HOH A 301 12.908 2.673 33.505 1.00 43.36 O
ANISOU 1304 O HOH A 301 7265 6683 2524 -1122 -737 713 O
HETATM 1305 O HOH A 302 -4.585 11.790 28.960 1.00 55.41 O
ANISOU 1305 O HOH A 302 7743 7344 5964 1095 -1414 -1083 O
HETATM 1306 O HOH A 303 7.558 25.947 -0.868 1.00 36.34 O
ANISOU 1306 O HOH A 303 5360 6128 2317 -1373 259 67 O
HETATM 1307 O HOH A 304 10.159 -7.236 15.244 1.00 36.75 O
ANISOU 1307 O HOH A 304 5176 2765 6022 -79 -85 572 O
HETATM 1308 O HOH A 305 8.651 -4.143 32.601 1.00 39.83 O
ANISOU 1308 O HOH A 305 6942 4905 3287 -347 1956 -309 O
HETATM 1309 O HOH A 306 19.107 12.635 26.198 1.00 39.26 O
ANISOU 1309 O HOH A 306 6293 5476 3147 74 374 654 O
HETATM 1310 O HOH A 307 19.708 18.963 11.732 1.00 43.45 O
ANISOU 1310 O HOH A 307 4161 5659 6686 1804 463 1256 O
HETATM 1311 O HOH A 308 0.156 17.543 17.998 1.00 38.66 O
ANISOU 1311 O HOH A 308 5633 5739 3315 733 1674 662 O
HETATM 1312 O HOH A 309 13.435 -3.953 2.405 1.00 36.15 O
ANISOU 1312 O HOH A 309 6307 3359 4069 1299 -263 1241 O
HETATM 1313 O HOH A 310 10.800 18.261 34.067 1.00 35.93 O
ANISOU 1313 O HOH A 310 6500 5533 1615 -225 446 616 O
HETATM 1314 O HOH A 311 15.659 -5.277 4.676 1.00 42.89 O
ANISOU 1314 O HOH A 311 8228 4551 3515 1666 242 1169 O
HETATM 1315 O HOH A 312 -5.523 11.006 31.351 1.00 44.60 O
ANISOU 1315 O HOH A 312 6179 6127 4638 510 -967 1050 O
HETATM 1316 O HOH A 313 8.578 17.282 32.212 1.00 44.69 O
ANISOU 1316 O HOH A 313 6017 9342 1621 1419 68 -944 O
HETATM 1317 O HOH A 314 16.412 -1.008 17.606 1.00 29.12 O
ANISOU 1317 O HOH A 314 5970 3196 1895 1060 -1464 -134 O
HETATM 1318 O HOH A 315 -1.543 7.605 -0.427 1.00 29.25 O
ANISOU 1318 O HOH A 315 4938 4794 1380 -1362 157 46 O
HETATM 1319 O HOH A 316 10.113 21.406 2.977 1.00 41.62 O
ANISOU 1319 O HOH A 316 7265 5866 2683 759 1300 -711 O
HETATM 1320 O HOH A 317 23.326 2.144 20.506 1.00 23.04 O
ANISOU 1320 O HOH A 317 3482 2064 3208 110 687 99 O
HETATM 1321 O HOH A 318 10.384 -5.220 9.401 1.00 32.59 O
ANISOU 1321 O HOH A 318 7608 2904 1869 848 602 -230 O
HETATM 1322 O HOH A 319 -3.232 14.286 19.692 1.00 29.49 O
ANISOU 1322 O HOH A 319 4923 2933 3348 -440 1088 -555 O
HETATM 1323 O HOH A 320 10.175 28.742 19.922 1.00 41.24 O
ANISOU 1323 O HOH A 320 5169 6592 3908 -1140 -187 -2991 O
HETATM 1324 O HOH A 321 17.160 7.095 2.158 1.00 32.39 O
ANISOU 1324 O HOH A 321 6372 3297 2637 -1742 1604 -30 O
HETATM 1325 O HOH A 322 7.705 3.207 -0.669 1.00 31.76 O
ANISOU 1325 O HOH A 322 5619 4014 2435 1866 1528 995 O
HETATM 1326 O HOH A 323 -2.728 5.921 28.670 1.00 40.71 O
ANISOU 1326 O HOH A 323 5377 4367 5722 929 -1905 -1700 O
HETATM 1327 O HOH A 324 2.064 22.845 25.930 1.00 53.74 O
ANISOU 1327 O HOH A 324 10158 6457 3801 2778 279 4461 O
HETATM 1328 O HOH A 325 7.140 29.303 13.869 1.00 24.23 O
ANISOU 1328 O HOH A 325 4680 2618 1906 -65 122 -335 O
HETATM 1329 O HOH A 326 6.383 9.135 -1.784 1.00 21.50 O
ANISOU 1329 O HOH A 326 3757 2275 2135 -393 713 -455 O
HETATM 1330 O HOH A 327 4.918 16.969 29.671 1.00 28.32 O
ANISOU 1330 O HOH A 327 6569 2938 1252 -380 636 -89 O
HETATM 1331 O HOH A 328 21.630 17.943 4.649 1.00 43.28 O
ANISOU 1331 O HOH A 328 5778 2639 8027 -638 3777 -136 O
HETATM 1332 O HOH A 329 -2.286 19.497 6.726 1.00 33.31 O
ANISOU 1332 O HOH A 329 3941 4199 4515 154 -1369 1294 O
HETATM 1333 O HOH A 330 7.855 -6.494 17.894 1.00 36.04 O
ANISOU 1333 O HOH A 330 6429 3048 4216 -961 -1948 1500 O
HETATM 1334 O HOH A 331 15.761 26.181 8.680 1.00 31.63 O
ANISOU 1334 O HOH A 331 5455 4974 1586 -1642 -11 -166 O
HETATM 1335 O HOH A 332 2.991 12.169 29.996 1.00 33.64 O
ANISOU 1335 O HOH A 332 6394 4023 2363 665 -76 -46 O
HETATM 1336 O HOH A 333 16.031 23.272 8.578 1.00 35.14 O
ANISOU 1336 O HOH A 333 4336 3477 5538 -250 1483 -892 O
HETATM 1337 O HOH A 334 4.074 9.313 15.359 1.00 30.37 O
ANISOU 1337 O HOH A 334 6289 3022 2227 1409 1970 738 O
HETATM 1338 O HOH A 335 3.077 -4.636 22.477 1.00 33.30 O
ANISOU 1338 O HOH A 335 6209 3859 2583 583 341 686 O
CONECT 1109 1127
CONECT 1110 1128
CONECT 1111 1113 1115
CONECT 1112 1114 1116
CONECT 1113 1111 1117
CONECT 1114 1112 1118
CONECT 1115 1111 1119
CONECT 1116 1112 1120
CONECT 1117 1113 1125
CONECT 1118 1114 1126
CONECT 1119 1115 1125
CONECT 1120 1116 1126
CONECT 1121 1123 1127
CONECT 1122 1124 1128
CONECT 1123 1121 1129 1131
CONECT 1124 1122 1130 1132
CONECT 1125 1117 1119 1127
CONECT 1126 1118 1120 1128
CONECT 1127 1109 1121 1125
CONECT 1128 1110 1122 1126
CONECT 1129 1123
CONECT 1130 1124
CONECT 1131 1123
CONECT 1132 1124
END
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elNémo
is maintained by Yves-Henri Sanejouand.
It was developed
by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.
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