HEADER DISULFIDE OXIDOREDUCTASE 24-MAY-93 1DSB 1DSB 2 COMPND DSBA (DISULFIDE BOND FORMATION PROTEIN) 1DSB 3 SOURCE (ESCHERICHIA COLI) 1DSB 4 AUTHOR J.L.MARTIN,J.C.A.BARDWELL,J.KURIYAN 1DSB 5 REVDAT 1 31-JAN-94 1DSB 0 1DSB 6 JRNL AUTH J.L.MARTIN,J.C.A.BARDWELL,J.KURIYAN 1DSB 7 JRNL TITL CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR 1DSB 8 JRNL TITL 2 DISULPHIDE BOND FORMATION IN VIVO 1DSB 9 JRNL REF NATURE V. 365 464 1993 1DSB 10 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 006 1DSB 11 REMARK 1 1DSB 12 REMARK 1 REFERENCE 1 1DSB 13 REMARK 1 AUTH J.L.MARTIN,G.WAKSMAN,J.C.A.BARDWELL,J.BECKWITH, 1DSB 14 REMARK 1 AUTH 2 J.KURIYAN 1DSB 15 REMARK 1 TITL CRYSTALLIZATION OF DSBA, AN ESCHERICHIA COLI 1DSB 16 REMARK 1 TITL 2 PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN 1DSB 17 REMARK 1 TITL 3 VIVO 1DSB 18 REMARK 1 REF J.MOL.BIOL. V. 230 1097 1993 1DSB 19 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1DSB 20 REMARK 2 1DSB 21 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1DSB 22 REMARK 3 1DSB 23 REMARK 3 REFINEMENT. 1DSB 24 REMARK 3 PROGRAM X-PLOR 1DSB 25 REMARK 3 AUTHORS BRUNGER 1DSB 26 REMARK 3 R VALUE 0.169 1DSB 27 REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1DSB 28 REMARK 3 RMSD BOND ANGLES 1.61 DEGREES 1DSB 29 REMARK 4 1DSB 30 REMARK 4 THERE ARE TWO MOLECULES IN THE ASYMMETRIC UNIT. EACH 1DSB 31 REMARK 4 CONTAINS 189 RESIDUES, BUT THE LAST RESIDUE (189) IS NOT 1DSB 32 REMARK 4 OBSERVED. THE ACTIVE SITE DISULFIDE RESIDUES ARE CYS 30 1DSB 33 REMARK 4 AND CYS 33. PRO 151 FORMS PART OF THE ACTIVE SITE. 1DSB 34 REMARK 5 1DSB 35 REMARK 5 HELIX A1' IS SEPARATED FROM A1 BY A THREE RESIDUE LOOP. 1DSB 36 REMARK 5 HELIX B1' IS SEPARATED FROM B1 BY A THREE RESIDUE LOOP. 1DSB 37 REMARK 5 HELIX A3 IS KINKED BY PRO A 91 AND HELIX B3 BY PRO B 91. 1DSB 38 SEQRES 1 A 189 ALA GLN TYR GLU ASP GLY LYS GLN TYR THR THR LEU GLU 1DSB 39 SEQRES 2 A 189 LYS PRO VAL ALA GLY ALA PRO GLN VAL LEU GLU PHE PHE 1DSB 40 SEQRES 3 A 189 SER PHE PHE CYS PRO HIS CYS TYR GLN PHE GLU GLU VAL 1DSB 41 SEQRES 4 A 189 LEU HIS ILE SER ASP ASN VAL LYS LYS LYS LEU PRO GLU 1DSB 42 SEQRES 5 A 189 GLY VAL LYS MET THR LYS TYR HIS VAL ASN PHE MET GLY 1DSB 43 SEQRES 6 A 189 GLY ASP LEU GLY LYS ASP LEU THR GLN ALA TRP ALA VAL 1DSB 44 SEQRES 7 A 189 ALA MET ALA LEU GLY VAL GLU ASP LYS VAL THR VAL PRO 1DSB 45 SEQRES 8 A 189 LEU PHE GLU GLY VAL GLN LYS THR GLN THR ILE ARG SER 1DSB 46 SEQRES 9 A 189 ALA SER ASP ILE ARG ASP VAL PHE ILE ASN ALA GLY ILE 1DSB 47 SEQRES 10 A 189 LYS GLY GLU GLU TYR ASP ALA ALA TRP ASN SER PHE VAL 1DSB 48 SEQRES 11 A 189 VAL LYS SER LEU VAL ALA GLN GLN GLU LYS ALA ALA ALA 1DSB 49 SEQRES 12 A 189 ASP VAL GLN LEU ARG GLY VAL PRO ALA MET PHE VAL ASN 1DSB 50 SEQRES 13 A 189 GLY LYS TYR GLN LEU ASN PRO GLN GLY MET ASP THR SER 1DSB 51 SEQRES 14 A 189 ASN MET ASP VAL PHE VAL GLN GLN TYR ALA ASP THR VAL 1DSB 52 SEQRES 15 A 189 LYS TYR LEU SER GLU LYS LYS 1DSB 53 SEQRES 1 B 189 ALA GLN TYR GLU ASP GLY LYS GLN TYR THR THR LEU GLU 1DSB 54 SEQRES 2 B 189 LYS PRO VAL ALA GLY ALA PRO GLN VAL LEU GLU PHE PHE 1DSB 55 SEQRES 3 B 189 SER PHE PHE CYS PRO HIS CYS TYR GLN PHE GLU GLU VAL 1DSB 56 SEQRES 4 B 189 LEU HIS ILE SER ASP ASN VAL LYS LYS LYS LEU PRO GLU 1DSB 57 SEQRES 5 B 189 GLY VAL LYS MET THR LYS TYR HIS VAL ASN PHE MET GLY 1DSB 58 SEQRES 6 B 189 GLY ASP LEU GLY LYS ASP LEU THR GLN ALA TRP ALA VAL 1DSB 59 SEQRES 7 B 189 ALA MET ALA LEU GLY VAL GLU ASP LYS VAL THR VAL PRO 1DSB 60 SEQRES 8 B 189 LEU PHE GLU GLY VAL GLN LYS THR GLN THR ILE ARG SER 1DSB 61 SEQRES 9 B 189 ALA SER ASP ILE ARG ASP VAL PHE ILE ASN ALA GLY ILE 1DSB 62 SEQRES 10 B 189 LYS GLY GLU GLU TYR ASP ALA ALA TRP ASN SER PHE VAL 1DSB 63 SEQRES 11 B 189 VAL LYS SER LEU VAL ALA GLN GLN GLU LYS ALA ALA ALA 1DSB 64 SEQRES 12 B 189 ASP VAL GLN LEU ARG GLY VAL PRO ALA MET PHE VAL ASN 1DSB 65 SEQRES 13 B 189 GLY LYS TYR GLN LEU ASN PRO GLN GLY MET ASP THR SER 1DSB 66 SEQRES 14 B 189 ASN MET ASP VAL PHE VAL GLN GLN TYR ALA ASP THR VAL 1DSB 67 SEQRES 15 B 189 LYS TYR LEU SER GLU LYS LYS 1DSB 68 FTNOTE 1 1DSB 69 FTNOTE 1 CIS PROLINE - PRO A 151 1DSB 70 FTNOTE 2 1DSB 71 FTNOTE 2 CIS PROLINE - PRO B 151 1DSB 72 FORMUL 3 HOH *195(H2 O1) 1DSB 73 HELIX 1 A1 CYS A 30 GLU A 37 1 1DSB 74 HELIX 2 A1' HIS A 41 LEU A 50 1 SEE REMARK 4 1DSB 75 HELIX 3 A2 GLY A 66 LEU A 82 1 1DSB 76 HELIX 4 A3 VAL A 84 GLN A 100 1 1DSB 77 HELIX 5 A4 SER A 104 ALA A 115 1 1DSB 78 HELIX 6 A5 LYS A 118 SER A 128 1 1DSB 79 HELIX 7 A6 PHE A 129 GLN A 146 1 1DSB 80 HELIX 8 A7 ASN A 170 LYS A 188 1 1DSB 81 HELIX 9 B1 CYS B 30 GLU B 37 1 1DSB 82 HELIX 10 B1' HIS B 41 LEU B 50 1 SEE REMARK 4 1DSB 83 HELIX 11 B2 GLY B 66 LEU B 82 1 1DSB 84 HELIX 12 B3 VAL B 84 GLN B 100 1 1DSB 85 HELIX 13 B4 SER B 104 ALA B 115 1 1DSB 86 HELIX 14 B5 LYS B 118 SER B 128 1 1DSB 87 HELIX 15 B6 PHE B 129 GLN B 146 1 1DSB 88 HELIX 16 B7 ASN B 170 LYS B 188 1 1DSB 89 SHEET 1 S1A 5 GLN A 8 LEU A 12 0 1DSB 90 SHEET 2 S1A 5 LYS A 158 ASN A 162 -1 1DSB 91 SHEET 3 S1A 5 ALA A 152 ASN A 156 -1 1DSB 92 SHEET 4 S1A 5 GLN A 21 PHE A 28 -1 1DSB 93 SHEET 5 S1A 5 LYS A 55 VAL A 61 1 1DSB 94 SHEET 1 S1B 5 GLN B 8 LEU B 12 0 1DSB 95 SHEET 2 S1B 5 LYS B 158 ASN B 162 -1 1DSB 96 SHEET 3 S1B 5 ALA B 152 ASN B 156 -1 1DSB 97 SHEET 4 S1B 5 GLN B 21 PHE B 28 -1 1DSB 98 SHEET 5 S1B 5 LYS B 55 VAL B 61 1 1DSB 99 SSBOND 1 CYS A 30 CYS A 33 1DSB 100 SSBOND 2 CYS B 30 CYS B 33 1DSB 101 SITE 1 CAA 5 CYS A 30 PRO A 31 HIS A 32 CYS A 33 1DSB 102 SITE 2 CAA 5 PRO A 151 1DSB 103 SITE 1 CAB 5 CYS B 30 PRO B 31 HIS B 32 CYS B 33 1DSB 104 SITE 2 CAB 5 PRO B 151 1DSB 105 CRYST1 117.500 65.000 76.500 90.00 126.30 90.00 C 2 8 1DSB 106 ORIGX1 1.000000 0.000000 0.000000 0.00000 1DSB 107 ORIGX2 0.000000 1.000000 0.000000 0.00000 1DSB 108 ORIGX3 0.000000 0.000000 1.000000 0.00000 1DSB 109 SCALE1 0.008511 0.000000 0.006252 0.00000 1DSB 110 SCALE2 0.000000 0.015385 0.000000 0.00000 1DSB 111 SCALE3 0.000000 0.000000 0.016220 0.00000 1DSB 112