***    ***
Job options:
ID = 2410102203191111079
JOBID =
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
SEQRES 1 A 452 THR THR MET ALA SER PRO GLN LEU MET PRO LEU VAL VAL
SEQRES 2 A 452 VAL LEU SER THR ILE CYS LEU VAL THR VAL GLY LEU ASN
SEQRES 3 A 452 LEU LEU VAL LEU TYR ALA VAL ARG SER GLU ARG LYS LEU
SEQRES 4 A 452 HIS THR VAL GLY ASN LEU TYR ILE VAL SER LEU SER VAL
SEQRES 5 A 452 ALA ASP LEU ILE VAL GLY ALA VAL VAL MET PRO MET ASN
SEQRES 6 A 452 ILE LEU TYR LEU LEU MET SER LYS TRP SER LEU GLY ARG
SEQRES 7 A 452 PRO LEU CYS LEU PHE TRP LEU SER MET ASP TYR VAL ALA
SEQRES 8 A 452 SER THR ALA SER ILE PHE SER VAL PHE ILE LEU CYS ILE
SEQRES 9 A 452 ASP ARG TYR ARG SER VAL GLN GLN PRO LEU ARG TYR LEU
SEQRES 10 A 452 LYS TYR ARG THR LYS THR ARG ALA SER ALA THR ILE LEU
SEQRES 11 A 452 GLY ALA TRP PHE LEU SER PHE LEU TRP VAL ILE PRO ILE
SEQRES 12 A 452 LEU GLY TRP ASN HIS PHE MET GLN GLN THR SER VAL ARG
SEQRES 13 A 452 ARG GLU ASP LYS CYS GLU THR ASP PHE TYR ASP VAL THR
SEQRES 14 A 452 TRP PHE LYS VAL MET THR ALA ILE ILE ASN PHE TYR LEU
SEQRES 15 A 452 PRO THR LEU LEU MET LEU TRP PHE TYR ALA LYS ILE TYR
SEQRES 16 A 452 LYS ALA VAL ARG GLN HIS CYS ASN ILE PHE GLU MET LEU
SEQRES 17 A 452 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP
SEQRES 18 A 452 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU
SEQRES 19 A 452 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU
SEQRES 20 A 452 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR
SEQRES 21 A 452 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP
SEQRES 22 A 452 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS
SEQRES 23 A 452 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA
SEQRES 24 A 452 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL
SEQRES 25 A 452 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS
SEQRES 26 A 452 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG
SEQRES 27 A 452 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE
SEQRES 28 A 452 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR LEU HIS
SEQRES 29 A 452 MET ASN ARG GLU ARG LYS ALA ALA LYS GLN LEU GLY PHE
SEQRES 30 A 452 ILE MET ALA ALA PHE ILE LEU CYS TRP ILE PRO TYR PHE
SEQRES 31 A 452 ILE PHE PHE MET VAL ILE ALA PHE CYS LYS ASN CYS CYS
SEQRES 32 A 452 ASN GLU HIS LEU HIS MET PHE THR ILE TRP LEU GLY TYR
SEQRES 33 A 452 ILE ASN SER THR LEU ASN PRO LEU ILE TYR PRO LEU CYS
SEQRES 34 A 452 ASN GLU ASN PHE LYS LYS THR PHE LYS ARG ILE LEU HIS
SEQRES 35 A 452 ILE ARG SER GLY GLU ASN LEU TYR PHE GLN
HELIX 1 1 MET A 28 VAL A 31 1 4
HELIX 2 2 VAL A 32 GLU A 55 1 24
HELIX 3 3 THR A 60 GLY A 62 1 3
HELIX 4 4 ASN A 63 ALA A 78 1 16
HELIX 5 5 VAL A 79 MET A 90 1 12
HELIX 6 6 LEU A 95 GLN A 131 1 37
HELIX 7 7 THR A 140 PHE A 156 1 17
HELIX 8 8 TRP A 158 GLY A 164 1 7
HELIX 9 9 VAL A 187 ASN A 198 1 12
HELIX 10 10 PHE A 199 VAL A 217 1 19
HELIX 11 11 ASN A 1002 GLY A 1012 1 11
HELIX 12 12 SER A 1038 GLY A 1051 1 14
HELIX 13 13 THR A 1059 ARG A 1080 1 22
HELIX 14 14 LEU A 1084 LEU A 1091 1 8
HELIX 15 15 ASP A 1092 MET A 1106 1 15
HELIX 16 16 GLY A 1107 ALA A 1112 1 6
HELIX 17 17 PHE A 1114 GLN A 1123 1 10
HELIX 18 18 ARG A 1125 ALA A 1134 1 10
HELIX 19 19 SER A 1136 GLN A 1141 1 6
HELIX 20 20 THR A 1142 GLY A 1156 1 15
HELIX 21 21 TRP A 1158 LEU A 405 1 5
HELIX 22 22 MET A 407 LYS A 442 1 36
HELIX 23 23 LEU A 449 CYS A 471 1 23
HELIX 24 24 ASN A 472 HIS A 484 1 13
SHEET 1 1 1 LEU A1013 LYS A1019 0
SHEET 2 2 1 TYR A1025 ILE A1029 0
SHEET 3 3 1 HIS A1031 LEU A1032 0
SSBOND 1 CYS A 100 CYS A 180 1555 1555 2.03
SSBOND 2 CYS A 441 CYS A 444 1555 1555 2.03
CRYST1 88.144 88.144 331.654 90.00 90.00 90.00 I 4 2 2 16
ATOM 1 N ASP A 107 8.478 36.028 20.891 1.00111.70 N
ANISOU 1 N ASP A 107 16461 16479 9502 321 -638 1689 N
ATOM 2 CA ASP A 107 9.705 35.243 21.005 1.00110.09 C
ANISOU 2 CA ASP A 107 16390 15990 9451 224 -597 1545 C
ATOM 3 C ASP A 107 10.806 36.150 21.569 1.00111.07 C
ANISOU 3 C ASP A 107 16531 15861 9810 366 -459 1546 C
ATOM 4 O ASP A 107 11.526 35.744 22.481 1.00109.62 O
ANISOU 4 O ASP A 107 16359 15494 9798 315 -454 1457 O
ATOM 5 CB ASP A 107 10.099 34.647 19.639 1.00113.11 C
ANISOU 5 CB ASP A 107 16911 16362 9704 170 -572 1487 C
ATOM 6 CG ASP A 107 11.470 33.999 19.590 1.00122.19 C
ANISOU 6 CG ASP A 107 18199 17244 10984 151 -499 1349 C
ATOM 7 OD1 ASP A 107 12.431 34.680 19.173 1.00122.29 O
ANISOU 7 OD1 ASP A 107 18237 17143 11083 277 -353 1367 O
ATOM 8 OD2 ASP A 107 11.577 32.801 19.941 1.00127.27 O
ANISOU 8 OD2 ASP A 107 18930 17804 11623 12 -592 1230 O
ATOM 9 N TYR A 108 10.907 37.385 21.046 1.00106.44 N
ANISOU 9 N TYR A 108 15954 15271 9217 530 -357 1656 N
ATOM 10 CA TYR A 108 11.896 38.369 21.476 1.00104.79 C
ANISOU 10 CA TYR A 108 15786 14829 9200 630 -236 1679 C
ATOM 11 C TYR A 108 11.567 39.040 22.815 1.00106.69 C
ANISOU 11 C TYR A 108 15961 15020 9554 710 -267 1708 C
ATOM 12 O TYR A 108 12.484 39.290 23.596 1.00105.11 O
ANISOU 12 O TYR A 108 15786 14605 9546 699 -214 1659 O
ATOM 13 CB TYR A 108 12.179 39.396 20.368 1.00106.73 C
ANISOU 13 CB TYR A 108 16111 15059 9381 744 -124 1792 C
ATOM 14 CG TYR A 108 13.174 38.903 19.337 1.00108.22 C
ANISOU 14 CG TYR A 108 16374 15195 9550 676 -38 1740 C
ATOM 15 CD1 TYR A 108 14.543 38.927 19.591 1.00109.70 C
ANISOU 15 CD1 TYR A 108 16590 15187 9904 637 62 1684 C
ATOM 16 CD2 TYR A 108 12.747 38.402 18.111 1.00109.72 C
ANISOU 16 CD2 TYR A 108 16594 15561 9534 657 -57 1745 C
ATOM 17 CE1 TYR A 108 15.465 38.484 18.642 1.00111.04 C
ANISOU 17 CE1 TYR A 108 16805 15357 10029 606 149 1642 C
ATOM 18 CE2 TYR A 108 13.658 37.944 17.158 1.00110.99 C
ANISOU 18 CE2 TYR A 108 16826 15691 9653 625 25 1690 C
ATOM 19 CZ TYR A 108 15.018 37.987 17.428 1.00116.95 C
ANISOU 19 CZ TYR A 108 17597 16270 10570 612 133 1640 C
ATOM 20 OH TYR A 108 15.927 37.538 16.498 1.00116.63 O
ANISOU 20 OH TYR A 108 17605 16246 10464 610 222 1591 O
ATOM 21 N SER A 111 11.787 36.092 25.858 1.00 91.55 N
ANISOU 21 N SER A 111 13898 12999 7886 331 -512 1406 N
ATOM 22 CA SER A 111 13.178 35.702 26.099 1.00 89.65 C
ANISOU 22 CA SER A 111 13729 12515 7818 295 -442 1302 C
ATOM 23 C SER A 111 13.970 36.818 26.793 1.00 91.64 C
ANISOU 23 C SER A 111 13963 12605 8252 396 -346 1324 C
ATOM 24 O SER A 111 14.814 36.523 27.636 1.00 91.05 O
ANISOU 24 O SER A 111 13876 12387 8330 357 -334 1247 O
ATOM 25 CB SER A 111 13.857 35.260 24.810 1.00 92.91 C
ANISOU 25 CB SER A 111 14251 12886 8164 278 -376 1261 C
ATOM 26 OG SER A 111 13.478 33.938 24.469 1.00 99.48 O
ANISOU 26 OG SER A 111 15154 13774 8871 152 -479 1186 O
ATOM 27 N THR A 112 13.665 38.089 26.475 1.00 86.74 N
ANISOU 27 N THR A 112 13355 12003 7599 521 -291 1429 N
ATOM 28 CA THR A 112 14.284 39.251 27.115 1.00 85.40 C
ANISOU 28 CA THR A 112 13215 11661 7572 599 -220 1459 C
ATOM 29 C THR A 112 13.738 39.348 28.544 1.00 87.53 C
ANISOU 29 C THR A 112 13409 11948 7901 633 -302 1437 C
ATOM 30 O THR A 112 14.503 39.604 29.475 1.00 86.57 O
ANISOU 30 O THR A 112 13290 11666 7938 613 -281 1386 O
ATOM 31 CB THR A 112 14.017 40.512 26.287 1.00 90.92 C
ANISOU 31 CB THR A 112 14003 12355 8186 726 -155 1584 C
ATOM 32 OG1 THR A 112 14.575 40.317 24.992 1.00 90.76 O
ANISOU 32 OG1 THR A 112 14037 12342 8107 678 -78 1603 O
ATOM 33 CG2 THR A 112 14.608 41.770 26.904 1.00 88.01 C
ANISOU 33 CG2 THR A 112 13724 11772 7941 785 -98 1621 C
ATOM 34 N ILE A 115 15.630 36.815 30.807 1.00 76.24 N
ANISOU 34 N ILE A 115 11867 10299 6801 346 -383 1152 N
ATOM 35 CA ILE A 115 16.920 37.317 31.304 1.00 75.54 C
ANISOU 35 CA ILE A 115 11781 10042 6881 345 -302 1115 C
ATOM 36 C ILE A 115 16.693 38.472 32.281 1.00 79.03 C
ANISOU 36 C ILE A 115 12210 10427 7390 412 -309 1149 C
ATOM 37 O ILE A 115 17.425 38.590 33.261 1.00 78.20 O
ANISOU 37 O ILE A 115 12074 10221 7417 380 -306 1097 O
ATOM 38 CB ILE A 115 17.979 37.641 30.198 1.00 79.26 C
ANISOU 38 CB ILE A 115 12307 10446 7361 338 -179 1132 C
ATOM 39 CG1 ILE A 115 19.405 37.759 30.798 1.00 79.28 C
ANISOU 39 CG1 ILE A 115 12266 10338 7519 289 -115 1082 C
ATOM 40 CG2 ILE A 115 17.610 38.877 29.351 1.00 80.96 C
ANISOU 40 CG2 ILE A 115 12595 10663 7503 403 -119 1244 C
ATOM 41 CD1 ILE A 115 20.538 37.371 29.876 1.00 87.76 C
ANISOU 41 CD1 ILE A 115 13336 11428 8579 269 -16 1065 C
ATOM 42 N TRP A 158 10.855 45.550 22.097 1.00117.56 N
ANISOU 42 N TRP A 158 17876 15995 10795 1588 -24 2290 N
ATOM 43 CA TRP A 158 11.157 44.678 20.960 1.00117.28 C
ANISOU 43 CA TRP A 158 17772 16091 10697 1430 8 2273 C
ATOM 44 C TRP A 158 10.111 44.745 19.856 1.00122.78 C
ANISOU 44 C TRP A 158 18440 17068 11143 1561 -19 2383 C
ATOM 45 O TRP A 158 10.450 44.514 18.697 1.00122.85 O
ANISOU 45 O TRP A 158 18475 17126 11075 1486 34 2413 O
ATOM 46 CB TRP A 158 11.365 43.233 21.423 1.00114.19 C
ANISOU 46 CB TRP A 158 17217 15788 10382 1232 -45 2117 C
ATOM 47 CG TRP A 158 12.765 42.992 21.874 1.00113.94 C
ANISOU 47 CG TRP A 158 17217 15509 10564 1067 21 2021 C
ATOM 48 CD1 TRP A 158 13.253 43.134 23.138 1.00115.90 C
ANISOU 48 CD1 TRP A 158 17462 15583 10993 1032 10 1952 C
ATOM 49 CD2 TRP A 158 13.892 42.713 21.037 1.00113.90 C
ANISOU 49 CD2 TRP A 158 17251 15430 10596 938 118 2003 C
ATOM 50 NE1 TRP A 158 14.610 42.912 23.149 1.00114.91 N
ANISOU 50 NE1 TRP A 158 17354 15292 11014 877 88 1892 N
ATOM 51 CE2 TRP A 158 15.029 42.650 21.870 1.00117.00 C
ANISOU 51 CE2 TRP A 158 17639 15626 11191 825 158 1924 C
ATOM 52 CE3 TRP A 158 14.050 42.492 19.660 1.00116.03 C
ANISOU 52 CE3 TRP A 158 17547 15810 10731 916 174 2047 C
ATOM 53 CZ2 TRP A 158 16.306 42.361 21.374 1.00116.36 C
ANISOU 53 CZ2 TRP A 158 17556 15484 11171 700 255 1893 C
ATOM 54 CZ3 TRP A 158 15.317 42.223 19.169 1.00117.50 C
ANISOU 54 CZ3 TRP A 158 17747 15919 10980 800 275 2011 C
ATOM 55 CH2 TRP A 158 16.422 42.139 20.023 1.00117.28 C
ANISOU 55 CH2 TRP A 158 17692 15725 11145 697 315 1937 C
ATOM 56 N LYS A 179 12.950 31.070 10.033 1.00149.39 N
ANISOU 56 N LYS A 179 22588 21151 13021 291 -324 968 N
ATOM 57 CA LYS A 179 11.704 31.363 10.761 1.00148.13 C
ANISOU 57 CA LYS A 179 22295 21099 12888 143 -457 1072 C
ATOM 58 C LYS A 179 10.736 32.298 9.980 1.00151.79 C
ANISOU 58 C LYS A 179 22624 21857 13190 166 -458 1250 C
ATOM 59 O LYS A 179 10.696 32.234 8.748 1.00152.95 O
ANISOU 59 O LYS A 179 22847 22141 13125 199 -438 1245 O
ATOM 60 CB LYS A 179 11.988 31.845 12.210 1.00148.40 C
ANISOU 60 CB LYS A 179 22190 20982 13215 166 -421 1121 C
ATOM 61 CG LYS A 179 12.784 33.145 12.345 1.00159.15 C
ANISOU 61 CG LYS A 179 23415 22297 14757 346 -232 1247 C
ATOM 62 CD LYS A 179 12.681 33.694 13.765 1.00166.39 C
ANISOU 62 CD LYS A 179 24197 23112 15912 338 -241 1309 C
ATOM 63 CE LYS A 179 13.029 35.158 13.856 1.00174.81 C
ANISOU 63 CE LYS A 179 25149 24167 17105 475 -100 1470 C
ATOM 64 NZ LYS A 179 14.477 35.401 13.643 1.00183.66 N
ANISOU 64 NZ LYS A 179 26296 25150 18336 560 63 1447 N
ATOM 65 N LYS A 191 22.160 43.024 14.780 1.00109.47 N
ANISOU 65 N LYS A 191 16639 15134 9822 335 1020 2300 N
ATOM 66 CA LYS A 191 22.083 41.670 15.331 1.00107.59 C
ANISOU 66 CA LYS A 191 16315 14937 9626 408 953 2087 C
ATOM 67 C LYS A 191 23.112 41.452 16.448 1.00111.00 C
ANISOU 67 C LYS A 191 16633 15307 10236 322 969 2010 C
ATOM 68 O LYS A 191 22.816 40.736 17.404 1.00109.24 O
ANISOU 68 O LYS A 191 16385 15004 10116 359 876 1868 O
ATOM 69 CB LYS A 191 22.290 40.622 14.232 1.00110.77 C
ANISOU 69 CB LYS A 191 16684 15560 9842 503 1000 2002 C
ATOM 70 CG LYS A 191 21.009 39.990 13.713 1.00123.48 C
ANISOU 70 CG LYS A 191 18387 17218 11314 606 896 1933 C
ATOM 71 CD LYS A 191 21.308 38.618 13.104 1.00135.11 C
ANISOU 71 CD LYS A 191 19854 18834 12648 693 900 1767 C
ATOM 72 CE LYS A 191 20.135 37.971 12.402 1.00145.97 C
ANISOU 72 CE LYS A 191 21335 20283 13844 754 798 1704 C
ATOM 73 NZ LYS A 191 19.083 37.493 13.341 1.00153.27 N
ANISOU 73 NZ LYS A 191 22295 21095 14847 725 634 1617 N
ATOM 74 N THR A 194 22.191 43.905 19.712 1.00108.61 N
ANISOU 74 N THR A 194 16533 14357 10377 148 768 2113 N
ATOM 75 CA THR A 194 21.102 43.368 20.540 1.00106.61 C
ANISOU 75 CA THR A 194 16286 14051 10170 268 642 1998 C
ATOM 76 C THR A 194 21.563 42.094 21.250 1.00109.10 C
ANISOU 76 C THR A 194 16453 14431 10570 261 611 1823 C
ATOM 77 O THR A 194 20.990 41.726 22.276 1.00107.41 O
ANISOU 77 O THR A 194 16223 14148 10440 298 511 1732 O
ATOM 78 CB THR A 194 19.824 43.127 19.734 1.00112.91 C
ANISOU 78 CB THR A 194 17143 14953 10806 415 592 2018 C
ATOM 79 OG1 THR A 194 20.102 42.266 18.631 1.00112.10 O
ANISOU 79 OG1 THR A 194 16981 15041 10570 431 647 1983 O
ATOM 80 CG2 THR A 194 19.162 44.417 19.278 1.00112.38 C
ANISOU 80 CG2 THR A 194 17240 14800 10657 476 595 2188 C
ATOM 81 N ALA A 195 22.598 41.424 20.699 1.00105.70 N
ANISOU 81 N ALA A 195 15918 14144 10101 230 699 1784 N
ATOM 82 CA ALA A 195 23.197 40.224 21.276 1.00104.28 C
ANISOU 82 CA ALA A 195 15619 14024 9978 253 683 1628 C
ATOM 83 C ALA A 195 23.882 40.590 22.592 1.00106.88 C
ANISOU 83 C ALA A 195 15876 14245 10490 151 667 1608 C
ATOM 84 O ALA A 195 23.747 39.858 23.567 1.00105.22 O
ANISOU 84 O ALA A 195 15622 13990 10368 185 588 1487 O
ATOM 85 CB ALA A 195 24.206 39.623 20.311 1.00106.32 C
ANISOU 85 CB ALA A 195 15794 14482 10123 283 795 1611 C
ATOM 86 N ASN A 198 21.009 42.777 25.172 1.00 96.83 N
ANISOU 86 N ASN A 198 14904 12471 9416 218 383 1674 N
ATOM 87 CA ASN A 198 20.013 41.868 25.751 1.00 94.61 C
ANISOU 87 CA ASN A 198 14572 12248 9125 320 277 1572 C
ATOM 88 C ASN A 198 20.549 40.548 26.354 1.00 96.45 C
ANISOU 88 C ASN A 198 14674 12544 9431 286 249 1431 C
ATOM 89 O ASN A 198 19.799 39.862 27.052 1.00 95.00 O
ANISOU 89 O ASN A 198 14458 12380 9256 329 150 1356 O
ATOM 90 CB ASN A 198 18.845 41.637 24.787 1.00 94.18 C
ANISOU 90 CB ASN A 198 14563 12320 8901 431 246 1615 C
ATOM 91 CG ASN A 198 18.078 42.896 24.479 1.00113.01 C
ANISOU 91 CG ASN A 198 17083 14645 11211 522 244 1747 C
ATOM 92 OD1 ASN A 198 17.055 43.194 25.099 1.00106.63 O
ANISOU 92 OD1 ASN A 198 16301 13833 10379 633 161 1754 O
ATOM 93 ND2 ASN A 198 18.566 43.679 23.528 1.00105.12 N
ANISOU 93 ND2 ASN A 198 16178 13607 10158 490 335 1862 N
ATOM 94 N PHE A 199 21.830 40.199 26.116 1.00 92.61 N
ANISOU 94 N PHE A 199 14109 12100 8980 216 333 1404 N
ATOM 95 CA PHE A 199 22.400 38.970 26.671 1.00 91.24 C
ANISOU 95 CA PHE A 199 13832 11977 8857 224 310 1275 C
ATOM 96 C PHE A 199 23.798 39.126 27.266 1.00 95.82 C
ANISOU 96 C PHE A 199 14298 12562 9547 139 372 1260 C
ATOM 97 O PHE A 199 23.934 38.922 28.466 1.00 94.92 O
ANISOU 97 O PHE A 199 14131 12389 9546 118 310 1194 O
ATOM 98 CB PHE A 199 22.299 37.789 25.689 1.00 93.08 C
ANISOU 98 CB PHE A 199 14081 12330 8953 303 318 1212 C
ATOM 99 CG PHE A 199 22.787 36.452 26.203 1.00 93.89 C
ANISOU 99 CG PHE A 199 14140 12453 9082 348 280 1077 C
ATOM 100 CD1 PHE A 199 21.926 35.591 26.875 1.00 95.73 C
ANISOU 100 CD1 PHE A 199 14420 12634 9319 364 152 997 C
ATOM 101 CD2 PHE A 199 24.095 36.033 25.972 1.00 96.70 C
ANISOU 101 CD2 PHE A 199 14413 12895 9432 383 371 1040 C
ATOM 102 CE1 PHE A 199 22.372 34.347 27.330 1.00 96.32 C
ANISOU 102 CE1 PHE A 199 14499 12693 9404 409 109 881 C
ATOM 103 CE2 PHE A 199 24.541 34.791 26.430 1.00 99.27 C
ANISOU 103 CE2 PHE A 199 14728 13228 9762 468 333 917 C
ATOM 104 CZ PHE A 199 23.676 33.955 27.104 1.00 96.24 C
ANISOU 104 CZ PHE A 199 14431 12743 9392 479 200 837 C
ATOM 105 N PHE A 424 20.023 28.933 32.688 1.00 84.51 N
ANISOU 105 N PHE A 424 13307 10790 8012 202 -602 557 N
ATOM 106 CA PHE A 424 19.898 29.984 31.673 1.00 84.74 C
ANISOU 106 CA PHE A 424 13273 10916 8010 222 -502 613 C
ATOM 107 C PHE A 424 21.162 30.228 30.840 1.00 90.30 C
ANISOU 107 C PHE A 424 13958 11632 8718 356 -358 584 C
ATOM 108 O PHE A 424 21.050 30.688 29.708 1.00 90.33 O
ANISOU 108 O PHE A 424 13982 11702 8639 373 -290 618 O
ATOM 109 CB PHE A 424 19.412 31.283 32.322 1.00 85.43 C
ANISOU 109 CB PHE A 424 13194 11075 8190 181 -484 700 C
ATOM 110 CG PHE A 424 18.684 32.222 31.394 1.00 87.16 C
ANISOU 110 CG PHE A 424 13399 11389 8330 174 -443 782 C
ATOM 111 CD1 PHE A 424 17.321 32.082 31.167 1.00 90.33 C
ANISOU 111 CD1 PHE A 424 13828 11888 8605 98 -539 831 C
ATOM 112 CD2 PHE A 424 19.350 33.279 30.786 1.00 89.61 C
ANISOU 112 CD2 PHE A 424 13660 11707 8680 237 -314 824 C
ATOM 113 CE1 PHE A 424 16.642 32.961 30.321 1.00 91.63 C
ANISOU 113 CE1 PHE A 424 13973 12161 8682 122 -503 914 C
ATOM 114 CE2 PHE A 424 18.671 34.158 29.939 1.00 92.82 C
ANISOU 114 CE2 PHE A 424 14077 12187 9005 246 -280 910 C
ATOM 115 CZ PHE A 424 17.319 33.998 29.718 1.00 90.97 C
ANISOU 115 CZ PHE A 424 13869 12052 8644 207 -373 952 C
ATOM 116 N TRP A 428 21.094 28.956 26.771 1.00102.93 N
ANISOU 116 N TRP A 428 15978 13307 9824 514 -273 485 N
ATOM 117 CA TRP A 428 21.181 30.034 25.795 1.00102.88 C
ANISOU 117 CA TRP A 428 15872 13432 9786 534 -152 568 C
ATOM 118 C TRP A 428 22.562 30.351 25.231 1.00109.33 C
ANISOU 118 C TRP A 428 16603 14333 10606 680 11 563 C
ATOM 119 O TRP A 428 22.623 30.731 24.061 1.00110.09 O
ANISOU 119 O TRP A 428 16710 14531 10590 715 93 599 O
ATOM 120 CB TRP A 428 20.501 31.298 26.319 1.00 99.96 C
ANISOU 120 CB TRP A 428 15348 13109 9524 427 -151 689 C
ATOM 121 CG TRP A 428 19.006 31.225 26.336 1.00100.40 C
ANISOU 121 CG TRP A 428 15454 13195 9497 307 -279 730 C
ATOM 122 CD1 TRP A 428 18.205 31.075 27.430 1.00102.28 C
ANISOU 122 CD1 TRP A 428 15657 13415 9790 208 -396 746 C
ATOM 123 CD2 TRP A 428 18.131 31.342 25.210 1.00100.96 C
ANISOU 123 CD2 TRP A 428 15592 13369 9400 272 -300 774 C
ATOM 124 NE1 TRP A 428 16.882 31.095 27.055 1.00101.97 N
ANISOU 124 NE1 TRP A 428 15640 13483 9619 112 -487 803 N
ATOM 125 CE2 TRP A 428 16.806 31.270 25.698 1.00104.41 C
ANISOU 125 CE2 TRP A 428 16012 13866 9792 148 -433 820 C
ATOM 126 CE3 TRP A 428 18.335 31.511 23.831 1.00103.22 C
ANISOU 126 CE3 TRP A 428 15935 13730 9553 334 -218 785 C
ATOM 127 CZ2 TRP A 428 15.691 31.346 24.856 1.00104.45 C
ANISOU 127 CZ2 TRP A 428 16048 14017 9622 83 -491 877 C
ATOM 128 CZ3 TRP A 428 17.230 31.587 22.998 1.00105.44 C
ANISOU 128 CZ3 TRP A 428 16266 14126 9670 272 -277 835 C
ATOM 129 CH2 TRP A 428 15.927 31.500 23.510 1.00105.59 C
ANISOU 129 CH2 TRP A 428 16259 14214 9645 146 -415 881 C
ATOM 130 N TYR A 431 23.535 29.030 21.668 1.00115.48 N
ANISOU 130 N TYR A 431 17704 15314 10860 1034 179 412 N
ATOM 131 CA TYR A 431 22.812 29.778 20.632 1.00115.85 C
ANISOU 131 CA TYR A 431 17742 15463 10811 948 207 503 C
ATOM 132 C TYR A 431 23.432 31.158 20.393 1.00120.39 C
ANISOU 132 C TYR A 431 18086 16189 11465 931 364 649 C
ATOM 133 O TYR A 431 23.517 31.586 19.243 1.00121.47 O
ANISOU 133 O TYR A 431 18217 16462 11474 964 453 705 O
ATOM 134 CB TYR A 431 21.313 29.894 20.994 1.00115.77 C
ANISOU 134 CB TYR A 431 17789 15376 10821 753 57 546 C
ATOM 135 CG TYR A 431 20.538 30.946 20.222 1.00117.24 C
ANISOU 135 CG TYR A 431 17908 15685 10952 671 88 677 C
ATOM 136 CD1 TYR A 431 20.116 30.713 18.917 1.00120.59 C
ANISOU 136 CD1 TYR A 431 18453 16201 11165 692 87 665 C
ATOM 137 CD2 TYR A 431 20.190 32.158 20.814 1.00116.59 C
ANISOU 137 CD2 TYR A 431 17664 15621 11013 587 110 811 C
ATOM 138 CE1 TYR A 431 19.401 31.677 18.205 1.00121.48 C
ANISOU 138 CE1 TYR A 431 18504 16439 11214 635 114 795 C
ATOM 139 CE2 TYR A 431 19.464 33.124 20.116 1.00117.53 C
ANISOU 139 CE2 TYR A 431 17749 15841 11067 547 134 937 C
ATOM 140 CZ TYR A 431 19.062 32.874 18.815 1.00125.96 C
ANISOU 140 CZ TYR A 431 18918 17016 11927 572 136 934 C
ATOM 141 OH TYR A 431 18.352 33.821 18.118 1.00126.38 O
ANISOU 141 OH TYR A 431 18937 17181 11903 551 158 1066 O
ATOM 142 N PHE A 432 23.822 31.863 21.473 1.00116.07 N
ANISOU 142 N PHE A 432 17370 15614 11119 861 388 714 N
ATOM 143 CA PHE A 432 24.436 33.187 21.379 1.00116.28 C
ANISOU 143 CA PHE A 432 17210 15745 11224 800 517 856 C
ATOM 144 C PHE A 432 25.865 33.126 20.876 1.00123.29 C
ANISOU 144 C PHE A 432 17980 16817 12047 916 665 857 C
ATOM 145 O PHE A 432 26.332 34.088 20.261 1.00123.62 O
ANISOU 145 O PHE A 432 17911 16997 12062 862 783 983 O
ATOM 146 CB PHE A 432 24.314 33.972 22.690 1.00116.39 C
ANISOU 146 CB PHE A 432 17117 15655 11450 669 476 918 C
ATOM 147 CG PHE A 432 22.992 34.690 22.810 1.00116.67 C
ANISOU 147 CG PHE A 432 17209 15607 11512 562 394 997 C
ATOM 148 CD1 PHE A 432 21.923 34.106 23.478 1.00118.33 C
ANISOU 148 CD1 PHE A 432 17500 15720 11742 529 247 939 C
ATOM 149 CD2 PHE A 432 22.806 35.940 22.230 1.00119.08 C
ANISOU 149 CD2 PHE A 432 17492 15952 11803 503 462 1140 C
ATOM 150 CE1 PHE A 432 20.696 34.766 23.577 1.00118.42 C
ANISOU 150 CE1 PHE A 432 17533 15715 11748 460 177 1019 C
ATOM 151 CE2 PHE A 432 21.574 36.595 22.323 1.00121.08 C
ANISOU 151 CE2 PHE A 432 17802 16147 12055 456 388 1214 C
ATOM 152 CZ PHE A 432 20.531 36.006 23.003 1.00117.97 C
ANISOU 152 CZ PHE A 432 17453 15697 11671 446 249 1152 C
ATOM 153 N PHE A 435 25.523 32.758 17.182 1.00131.61 N
ANISOU 153 N PHE A 435 19258 18199 12548 1126 813 868 N
ATOM 154 CA PHE A 435 25.196 34.066 16.627 1.00131.74 C
ANISOU 154 CA PHE A 435 19202 18285 12570 990 877 1049 C
ATOM 155 C PHE A 435 26.502 34.804 16.370 1.00137.98 C
ANISOU 155 C PHE A 435 19789 19278 13359 981 1046 1165 C
ATOM 156 O PHE A 435 26.593 35.576 15.420 1.00138.49 O
ANISOU 156 O PHE A 435 19818 19480 13323 935 1140 1299 O
ATOM 157 CB PHE A 435 24.329 34.848 17.622 1.00131.56 C
ANISOU 157 CB PHE A 435 19169 18078 12738 819 781 1126 C
ATOM 158 CG PHE A 435 22.970 35.249 17.104 1.00132.73 C
ANISOU 158 CG PHE A 435 19431 18184 12817 757 703 1190 C
ATOM 159 CD1 PHE A 435 22.632 36.590 16.960 1.00135.73 C
ANISOU 159 CD1 PHE A 435 19773 18558 13240 661 741 1364 C
ATOM 160 CD2 PHE A 435 22.023 34.287 16.764 1.00134.96 C
ANISOU 160 CD2 PHE A 435 19869 18437 12974 793 584 1081 C
ATOM 161 CE1 PHE A 435 21.373 36.963 16.480 1.00136.56 C
ANISOU 161 CE1 PHE A 435 19970 18657 13260 643 670 1430 C
ATOM 162 CE2 PHE A 435 20.771 34.661 16.269 1.00137.75 C
ANISOU 162 CE2 PHE A 435 20291 18808 13239 734 511 1151 C
ATOM 163 CZ PHE A 435 20.450 35.996 16.139 1.00135.68 C
ANISOU 163 CZ PHE A 435 19967 18567 13019 679 558 1326 C
ATOM 164 N ILE A 454 17.973 26.891 19.272 1.00136.14 N
ANISOU 164 N ILE A 454 21129 17816 12781 409 -446 319 N
ATOM 165 CA ILE A 454 16.786 27.710 19.542 1.00134.79 C
ANISOU 165 CA ILE A 454 20786 17781 12646 227 -504 462 C
ATOM 166 C ILE A 454 15.829 26.923 20.439 1.00138.10 C
ANISOU 166 C ILE A 454 21295 18122 13056 9 -702 444 C
ATOM 167 O ILE A 454 15.138 27.524 21.262 1.00136.45 O
ANISOU 167 O ILE A 454 20899 17997 12950 -98 -741 552 O
ATOM 168 CB ILE A 454 16.076 28.302 18.287 1.00138.88 C
ANISOU 168 CB ILE A 454 21275 18503 12990 196 -484 540 C
ATOM 169 CG1 ILE A 454 15.560 27.225 17.315 1.00141.71 C
ANISOU 169 CG1 ILE A 454 21904 18854 13084 112 -606 432 C
ATOM 170 CG2 ILE A 454 16.936 29.326 17.572 1.00139.45 C
ANISOU 170 CG2 ILE A 454 21212 18676 13098 377 -284 608 C
ATOM 171 CD1 ILE A 454 14.072 27.249 17.121 1.00150.94 C
ANISOU 171 CD1 ILE A 454 23054 20185 14113 -121 -758 511 C
ATOM 172 N TYR A 458 14.476 27.007 24.507 1.00119.89 N
ANISOU 172 N TYR A 458 18647 15758 11149 -345 -946 605 N
ATOM 173 CA TYR A 458 13.080 26.699 24.823 1.00120.08 C
ANISOU 173 CA TYR A 458 18647 15925 11053 -597 -1115 677 C
ATOM 174 C TYR A 458 13.044 25.589 25.891 1.00122.39 C
ANISOU 174 C TYR A 458 19078 16051 11374 -747 -1253 628 C
ATOM 175 O TYR A 458 12.014 25.398 26.538 1.00121.83 O
ANISOU 175 O TYR A 458 18933 16108 11247 -964 -1385 708 O
ATOM 176 CB TYR A 458 12.284 26.272 23.559 1.00123.83 C
ANISOU 176 CB TYR A 458 19262 16517 11269 -733 -1202 671 C
ATOM 177 CG TYR A 458 12.138 27.309 22.454 1.00126.44 C
ANISOU 177 CG TYR A 458 19466 17041 11533 -609 -1088 739 C
ATOM 178 CD1 TYR A 458 11.970 28.661 22.750 1.00127.29 C
ANISOU 178 CD1 TYR A 458 19304 17305 11754 -488 -983 864 C
ATOM 179 CD2 TYR A 458 12.053 26.923 21.116 1.00129.03 C
ANISOU 179 CD2 TYR A 458 19965 17399 11659 -624 -1102 684 C
ATOM 180 CE1 TYR A 458 11.812 29.613 21.738 1.00128.47 C
ANISOU 180 CE1 TYR A 458 19367 17614 11830 -373 -886 940 C
ATOM 181 CE2 TYR A 458 11.894 27.866 20.096 1.00130.15 C
ANISOU 181 CE2 TYR A 458 19994 17730 11729 -512 -1001 759 C
ATOM 182 CZ TYR A 458 11.765 29.209 20.412 1.00135.54 C
ANISOU 182 CZ TYR A 458 20415 18551 12534 -390 -894 894 C
ATOM 183 OH TYR A 458 11.602 30.139 19.413 1.00135.19 O
ANISOU 183 OH TYR A 458 20288 18672 12408 -277 -800 980 O
TER 184 ILE A 485
HETATM 185 C01A5EH A1200 14.569 31.755 20.378 0.50128.73 C
HETATM 186 N02A5EH A1200 14.525 32.943 19.512 0.50135.70 N
HETATM 187 C03A5EH A1200 14.452 32.511 18.106 0.50 23.95 C
HETATM 188 C04A5EH A1200 15.730 33.765 19.724 0.50108.61 C
HETATM 189 C05A5EH A1200 15.364 35.138 20.280 0.50 60.67 C
HETATM 190 C06A5EH A1200 15.773 35.211 21.734 0.50113.33 C
HETATM 191 C07A5EH A1200 16.751 36.014 22.195 0.50165.91 C
HETATM 192 C08A5EH A1200 17.526 36.943 21.311 0.50153.27 C
HETATM 193 C09A5EH A1200 18.420 36.473 20.347 0.50127.97 C
HETATM 194 C10A5EH A1200 19.149 37.384 19.580 0.50131.79 C
HETATM 195 C11A5EH A1200 18.997 38.757 19.793 0.50 91.15 C
HETATM 196 C12A5EH A1200 18.119 39.218 20.775 0.50 77.62 C
HETATM 197 C13A5EH A1200 17.392 38.303 21.537 0.50 99.53 C
HETATM 198 C14A5EH A1200 16.426 38.762 22.605 0.50 29.88 C
HETATM 199 O15A5EH A1200 16.962 38.468 23.894 0.50129.74 O
HETATM 200 C16A5EH A1200 17.176 37.205 24.405 0.50141.60 C
HETATM 201 C17A5EH A1200 17.517 37.134 25.758 0.50123.84 C
HETATM 202 C18A5EH A1200 17.770 35.908 26.373 0.50140.03 C
HETATM 203 C19A5EH A1200 17.686 34.733 25.630 0.50137.78 C
HETATM 204 C20A5EH A1200 17.350 34.796 24.279 0.50113.47 C
HETATM 205 C21A5EH A1200 17.092 36.021 23.659 0.50159.27 C
HETATM 206 C1 BD7V A1201 14.808 32.837 18.106 0.50 73.17 C
HETATM 207 N1 BD7V A1201 14.677 33.217 19.522 0.50134.26 N
HETATM 208 O1 BD7V A1201 17.822 39.257 22.374 0.50 60.56 O
HETATM 209 C2 BD7V A1201 14.643 32.000 20.349 0.50132.98 C
HETATM 210 C3 BD7V A1201 15.818 34.061 19.915 0.50101.39 C
HETATM 211 C4 BD7V A1201 15.343 35.458 20.304 0.50 63.13 C
HETATM 212 C5 BD7V A1201 15.754 35.727 21.733 0.50 97.28 C
HETATM 213 C6 BD7V A1201 16.832 36.440 22.115 0.50159.20 C
HETATM 214 C7 BD7V A1201 17.090 36.591 23.581 0.50151.60 C
HETATM 215 C8 BD7V A1201 17.401 35.486 24.375 0.50133.41 C
HETATM 216 C9 BD7V A1201 17.654 35.666 25.736 0.50144.02 C
HETATM 217 C10BD7V A1201 17.597 36.946 26.291 0.50124.82 C
HETATM 218 C11BD7V A1201 17.280 38.046 25.491 0.50 95.05 C
HETATM 219 C12BD7V A1201 17.027 37.857 24.132 0.50118.35 C
HETATM 220 C13BD7V A1201 16.702 39.017 23.224 0.50 79.50 C
HETATM 221 C14BD7V A1201 18.247 38.425 21.362 0.50105.70 C
HETATM 222 C15BD7V A1201 17.803 37.105 21.170 0.50154.58 C
HETATM 223 C16BD7V A1201 19.189 38.972 20.486 0.50 61.44 C
HETATM 224 C17BD7V A1201 19.706 38.223 19.432 0.50 50.85 C
HETATM 225 C18BD7V A1201 19.279 36.910 19.253 0.50146.65 C
HETATM 226 C19BD7V A1201 18.351 36.351 20.130 0.50111.98 C
HETATM 227 P PO4 A1202 17.536 33.739 14.081 1.00172.63 P
HETATM 228 O1 PO4 A1202 18.998 33.196 13.827 1.00178.54 O
HETATM 229 O2 PO4 A1202 17.291 35.061 13.244 1.00178.73 O
HETATM 230 O3 PO4 A1202 16.485 32.632 13.656 1.00178.41 O
HETATM 231 O4 PO4 A1202 17.396 34.078 15.613 1.00178.53 O
CONECT 185 186
CONECT 186 185 187 188
CONECT 187 186
CONECT 188 186 189
CONECT 189 188 190
CONECT 190 189 191
CONECT 191 190 192 205
CONECT 192 191 193 197
CONECT 193 192 194
CONECT 194 193 195
CONECT 195 194 196
CONECT 196 195 197
CONECT 197 192 196 198
CONECT 198 197 199
CONECT 199 198 200
CONECT 200 199 201 205
CONECT 201 200 202
CONECT 202 201 203
CONECT 203 202 204
CONECT 204 203 205
CONECT 205 191 200 204
CONECT 206 207
CONECT 207 206 209 210
CONECT 208 220 221
CONECT 209 207
CONECT 210 207 211
CONECT 211 210 212
CONECT 212 211 213
CONECT 213 212 214 222
CONECT 214 213 215 219
CONECT 215 214 216
CONECT 216 215 217
CONECT 217 216 218
CONECT 218 217 219
CONECT 219 214 218 220
CONECT 220 208 219
CONECT 221 208 222 223
CONECT 222 213 221 226
CONECT 223 221 224
CONECT 224 223 225
CONECT 225 224 226
CONECT 226 222 225
CONECT 227 228 229 230 231
CONECT 228 227
CONECT 229 227
CONECT 230 227
CONECT 231 227
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: April 25th, 2023.
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