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REMARK 999 CY41_TRYBB AND CY43_TRYBB FROM T. BRUCEI STRAIN REMARK 999 ANTAT1.3, SEVERAL SEQUENCE DIFFERENCES WERE FOUND FOR THE REMARK 999 CODING SEQUENCES WHICH WERE CONFIRMED BY REPEATED PCR REMARK 999 AMPLIFICATIONS AND SEQUENCING OF BOTH STRANDS. REMARK 999 REMARK 999 THE GRESAG4.1(1FX2) SEQUENCE (SWISSPROT ENTRY) SHOWS REMARK 999 THE SEQUENCE EXCHANGES Y1120I AND THE CODON FOR I1032 REMARK 999 IS MISSING. REMARK 999 REMARK 999 THE GRESAG4.3 (1FX4)SEQUENCE (SWISSPROT ENTRY) SHOWS REMARK 999 THE SEQUENCE EXCHANGES R959C, H994S, M995L, N1098S, C1164W REMARK 999 AND G1165R. REMARK 999 REMARK 999 NONE OF THE EXCHANGES IS OBSERVED AT POSITIONS WHICH MIGHT REMARK 999 BE CRUCIAL FOR CATALITIC ACTIVITY. DBREF 1FX2 A 888 1122 SWS Q99279 CY41_TRYBB 888 1123 SEQADV 1FX2 A Q99279 ILE 1032 DELETION SEQRES 1 A 235 ASN ASN ASN ARG ALA PRO LYS GLU PRO THR ASP PRO VAL SEQRES 2 A 235 THR LEU ILE PHE THR ASP ILE GLU SER SER THR ALA LEU SEQRES 3 A 235 TRP ALA ALA HIS PRO ASP LEU MET PRO ASP ALA VAL ALA SEQRES 4 A 235 ALA HIS HIS ARG MET VAL ARG SER LEU ILE GLY ARG TYR SEQRES 5 A 235 LYS CYS TYR GLU VAL LYS THR VAL GLY ASP SER PHE MET SEQRES 6 A 235 ILE ALA SER LYS SER PRO PHE ALA ALA VAL GLN LEU ALA SEQRES 7 A 235 GLN GLU LEU GLN LEU CYS PHE LEU HIS HIS ASP TRP GLY SEQRES 8 A 235 THR ASN ALA LEU ASP ASP SER TYR ARG GLU PHE GLU GLU SEQRES 9 A 235 GLN ARG ALA GLU GLY GLU CYS GLU TYR THR PRO PRO THR SEQRES 10 A 235 ALA HIS MET ASP PRO GLU VAL TYR SER ARG LEU TRP ASN SEQRES 11 A 235 GLY LEU ARG VAL ARG VAL GLY ILE HIS THR GLY LEU CYS SEQRES 12 A 235 ASP ILE ARG HIS ASP GLU VAL THR LYS GLY TYR ASP TYR SEQRES 13 A 235 TYR GLY ARG THR PRO ASN MET ALA ALA ARG THR GLU SER SEQRES 14 A 235 VAL ALA ASN GLY GLY GLN VAL LEU MET THR HIS ALA ALA SEQRES 15 A 235 TYR MET SER LEU SER ALA GLU ASP ARG LYS GLN ILE ASP SEQRES 16 A 235 VAL THR ALA LEU GLY ASP VAL ALA LEU ARG GLY VAL SER SEQRES 17 A 235 ASP PRO VAL LYS MET TYR GLN LEU ASN THR VAL PRO SER SEQRES 18 A 235 ARG ASN PHE ALA ALA LEU ARG LEU ASP ARG GLU TYR PHE SEQRES 19 A 235 ASP HET SO4 1123 5 HET DTT 1124 8 HETNAM SO4 SULFATE ION HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE HETSYN DTT 1,4-DITHIOTHREITOL FORMUL 2 SO4 O4 S1 2- FORMUL 3 DTT C4 H10 O2 S2 FORMUL 4 HOH *272(H2 O1) HELIX 1 1 ASN A 888 ALA A 892 5 5 HELIX 2 2 SER A 909 HIS A 917 1 9 HELIX 3 3 LEU A 920 TYR A 939 1 20 HELIX 4 4 SER A 957 HIS A 975 1 19 HELIX 5 5 ASN A 980 GLU A 997 1 18 HELIX 6 6 ASP A 1008 TRP A 1016 1 9 HELIX 7 7 GLY A 1045 VAL A 1057 1 13 HELIX 8 8 HIS A 1067 SER A 1072 1 6 HELIX 9 9 SER A 1074 GLN A 1080 1 7 SHEET 1 A 7 TYR A 942 VAL A 947 0 SHEET 2 A 7 SER A 950 SER A 955 -1 N SER A 950 O VAL A 947 SHEET 3 A 7 VAL A 900 ILE A 907 -1 O THR A 901 N SER A 955 SHEET 4 A 7 VAL A1021 GLY A1028 -1 N ARG A1022 O ASP A 906 SHEET 5 A 7 VAL A1063 THR A1066 1 N LEU A1064 O VAL A1023 SHEET 6 A 7 VAL A1098 LEU A1103 -1 O TYR A1101 N MET A1065 SHEET 7 A 7 VAL A1083 VAL A1089 -1 O THR A1084 N GLN A1102 SHEET 1 B 2 ASP A1031 HIS A1034 0 SHEET 2 B 2 TYR A1041 TYR A1044 -1 N ASP A1042 O ARG A1033 CRYST1 49.600 60.070 78.880 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.020161 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016647 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012677 0.00000 ATOM 1 N ASN A 888 21.989 17.769 -4.326 1.00 54.09 N ATOM 2 CA ASN A 888 22.278 18.536 -5.583 1.00 58.93 C ATOM 3 C ASN A 888 23.776 18.800 -5.788 1.00 52.64 C ATOM 4 O ASN A 888 24.263 19.964 -5.666 1.00 45.88 O ATOM 5 CB ASN A 888 21.477 19.860 -5.635 1.00 60.99 C ATOM 6 CG ASN A 888 21.100 20.286 -7.081 1.00 66.12 C ATOM 7 OD1 ASN A 888 20.231 21.153 -7.287 1.00 67.33 O ATOM 8 ND2 ASN A 888 21.748 19.673 -8.074 1.00 66.39 N ATOM 9 N ASN A 889 24.498 17.724 -6.130 1.00 39.31 N ATOM 10 CA ASN A 889 25.937 17.844 -6.414 1.00 29.83 C ATOM 11 C ASN A 889 26.122 18.629 -7.706 1.00 22.83 C ATOM 12 O ASN A 889 27.242 19.052 -8.018 1.00 20.70 O ATOM 13 CB ASN A 889 26.635 16.497 -6.568 1.00 33.44 C ATOM 14 CG ASN A 889 27.058 15.889 -5.249 1.00 31.57 C ATOM 15 OD1 ASN A 889 27.111 16.552 -4.201 1.00 29.22 O ATOM 16 ND2 ASN A 889 27.358 14.593 -5.282 1.00 30.92 N ATOM 17 N ASN A 890 25.048 18.887 -8.433 1.00 21.86 N ATOM 18 CA ASN A 890 25.119 19.661 -9.646 1.00 18.68 C ATOM 19 C ASN A 890 25.726 21.073 -9.426 1.00 21.51 C ATOM 20 O ASN A 890 26.435 21.567 -10.269 1.00 21.08 O ATOM 21 CB ASN A 890 23.709 19.732 -10.270 1.00 33.11 C ATOM 22 CG ASN A 890 23.454 21.007 -11.038 1.00 48.46 C ATOM 23 OD1 ASN A 890 24.145 21.301 -12.032 1.00 56.60 O ATOM 24 ND2 ASN A 890 22.443 21.789 -10.585 1.00 43.76 N ATOM 25 N ARG A 891 25.495 21.643 -8.256 1.00 20.50 N ATOM 26 CA ARG A 891 26.005 22.991 -7.961 1.00 16.78 C ATOM 27 C ARG A 891 27.401 22.987 -7.401 1.00 13.07 C ATOM 28 O ARG A 891 28.045 24.066 -7.300 1.00 13.51 O ATOM 29 CB ARG A 891 25.058 23.702 -7.009 1.00 20.28 C ATOM 30 CG ARG A 891 23.755 24.064 -7.723 1.00 26.96 C ATOM 31 CD ARG A 891 22.626 24.265 -6.739 1.00 31.84 C ATOM 32 NE ARG A 891 21.350 24.358 -7.458 1.00 43.68 N ATOM 33 CZ ARG A 891 20.195 24.712 -6.899 1.00 47.39 C ATOM 34 NH1 ARG A 891 20.151 25.013 -5.615 1.00 43.78 N ATOM 35 NH2 ARG A 891 19.077 24.747 -7.622 1.00 43.32 N ATOM 36 N ALA A 892 27.952 21.824 -7.083 1.00 14.20 N ATOM 37 CA ALA A 892 29.317 21.734 -6.575 1.00 12.76 C ATOM 38 C ALA A 892 30.364 22.063 -7.614 1.00 12.24 C ATOM 39 O ALA A 892 30.297 21.553 -8.740 1.00 15.53 O ATOM 40 CB ALA A 892 29.623 20.324 -6.047 1.00 14.63 C ATOM 41 N PRO A 893 31.276 22.993 -7.304 1.00 10.94 N ATOM 42 CA PRO A 893 32.381 23.317 -8.250 1.00 11.57 C ATOM 43 C PRO A 893 33.169 21.986 -8.405 1.00 12.65 C ATOM 44 O PRO A 893 33.537 21.306 -7.394 1.00 14.14 O ATOM 45 CB PRO A 893 33.229 24.316 -7.462 1.00 11.91 C ATOM 46 CG PRO A 893 32.132 25.069 -6.682 1.00 12.38 C ATOM 47 CD PRO A 893 31.220 23.959 -6.158 1.00 11.45 C ATOM 48 N LYS A 894 33.356 21.533 -9.671 1.00 12.32 N ATOM 49 CA LYS A 894 34.067 20.263 -9.900 1.00 13.18 C ATOM 50 C LYS A 894 35.247 20.323 -10.830 1.00 12.72 C ATOM 51 O LYS A 894 35.994 19.367 -10.936 1.00 18.52 O ATOM 52 CB LYS A 894 33.097 19.237 -10.516 1.00 14.62 C ATOM 53 CG LYS A 894 31.865 19.017 -9.738 1.00 25.46 C ATOM 54 CD LYS A 894 30.875 18.225 -10.660 1.00 19.23 C ATOM 55 CE LYS A 894 29.607 18.197 -9.929 1.00 21.40 C ATOM 56 NZ LYS A 894 29.012 19.565 -10.089 1.00 22.91 N ATOM 57 N GLU A 895 35.389 21.432 -11.554 1.00 11.90 N ATOM 58 CA GLU A 895 36.485 21.515 -12.559 1.00 11.27 C ATOM 59 C GLU A 895 37.716 22.062 -11.868 1.00 11.52 C ATOM 60 O GLU A 895 37.719 23.214 -11.423 1.00 12.39 O ATOM 61 CB GLU A 895 35.999 22.403 -13.690 1.00 11.98 C ATOM 62 CG GLU A 895 37.145 22.795 -14.689 1.00 9.73 C ATOM 63 CD GLU A 895 37.995 21.591 -15.156 1.00 12.93 C ATOM 64 OE1 GLU A 895 37.428 20.536 -15.482 1.00 13.10 O ATOM 65 OE2 GLU A 895 39.222 21.749 -15.132 1.00 11.83 O ATOM 66 N PRO A 896 38.830 21.301 -11.780 1.00 9.48 N ATOM 67 CA PRO A 896 40.034 21.763 -11.085 1.00 11.03 C ATOM 68 C PRO A 896 40.664 23.043 -11.581 1.00 9.85 C ATOM 69 O PRO A 896 41.345 23.730 -10.817 1.00 11.79 O ATOM 70 CB PRO A 896 41.004 20.553 -11.146 1.00 14.53 C ATOM 71 CG PRO A 896 40.477 19.743 -12.198 1.00 20.33 C ATOM 72 CD PRO A 896 38.973 19.896 -12.310 1.00 12.31 C ATOM 73 N THR A 897 40.470 23.320 -12.888 1.00 10.16 N ATOM 74 CA THR A 897 41.111 24.519 -13.427 1.00 8.43 C ATOM 75 C THR A 897 40.292 25.766 -13.299 1.00 11.65 C ATOM 76 O THR A 897 40.721 26.826 -13.756 1.00 10.33 O ATOM 77 CB THR A 897 41.509 24.301 -14.906 1.00 9.11 C ATOM 78 OG1 THR A 897 40.327 24.116 -15.676 1.00 10.27 O ATOM 79 CG2 THR A 897 42.401 23.057 -15.042 1.00 10.94 C ATOM 80 N ASP A 898 39.083 25.631 -12.696 1.00 10.69 N ATOM 81 CA ASP A 898 38.235 26.806 -12.477 1.00 9.57 C ATOM 82 C ASP A 898 38.339 27.170 -10.985 1.00 10.49 C ATOM 83 O ASP A 898 38.208 26.326 -10.105 1.00 11.15 O ATOM 84 CB ASP A 898 36.791 26.582 -12.801 1.00 11.04 C ATOM 85 CG ASP A 898 36.542 26.340 -14.261 1.00 13.10 C ATOM 86 OD1 ASP A 898 37.318 26.922 -15.067 1.00 17.83 O ATOM 87 OD2 ASP A 898 35.482 25.738 -14.570 1.00 17.17 O ATOM 88 N PRO A 899 38.679 28.435 -10.686 1.00 10.96 N ATOM 89 CA PRO A 899 38.784 28.832 -9.261 1.00 9.91 C ATOM 90 C PRO A 899 37.406 28.621 -8.570 1.00 9.08 C ATOM 91 O PRO A 899 36.332 28.757 -9.211 1.00 11.13 O ATOM 92 CB PRO A 899 39.066 30.321 -9.327 1.00 12.16 C ATOM 93 CG PRO A 899 39.898 30.453 -10.722 1.00 15.54 C ⌨️ 快捷键说明
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