HEADER OXIDOREDUCTASE(FLAVOPROTEIN) 27-AUG-92 1GAL COMPND GLUCOSE OXIDASE (E.C.1.1.3.4) SOURCE (ASPERGILLUS NIGER) AUTHOR H.J.HECHT,K.KALISZ,J.HENDLE,R.D.SCHMID,D.SCHOMBURG REVDAT 1 31-OCT-93 1GAL 0 JRNL AUTH H.J.HECHT,H.M.KALISZ,J.HENDLE,R.D.SCHMID, JRNL AUTH 2 D.SCHOMBURG JRNL TITL CRYSTAL STRUCTURE OF GLUCOSE OXIDASE FROM JRNL TITL 2 ASPERGILLUS NIGER: REFINED AT 2.3 ANGSTROMS JRNL TITL 3 RESOLUTION JRNL REF J.MOL.BIOL. V. 229 153 1993 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.M.KALISZ,H.-J.HECHT,D.SCHOMBURG,R.D.SCHMID REMARK 1 TITL EFFECTS OF CARBOHYDRATE DEPLETION ON THE REMARK 1 TITL 2 STRUCTURE, STABILITY AND ACTIVITY OF GLUCOSE REMARK 1 TITL 3 OXIDASE FROM ASPERGILLUS NIGER REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1080 138 1991 REMARK 1 REFN ASTM BBACAQ NE ISSN 0006-3002 113 REMARK 2 REMARK 2 RESOLUTION. 2.3 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM 1 X-PLOR REMARK 3 AUTHORS 1 BRUNGER REMARK 3 PROGRAM 2 PROLSQ REMARK 3 AUTHORS KONNERT,HENDRICKSON REMARK 3 R VALUE 0.181 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.048 ANGSTROMS REMARK 3 REMARK 3 NUMBER OF REFLECTIONS 20862 REMARK 3 RESOLUTION RANGE 10.0 - 2.3 ANGSTROMS REMARK 3 PERCENT COMPLETION 83.4 REMARK 3 REMARK 3 NUMBER OF PROTEIN ATOMS 4452 REMARK 3 NUMBER OF SOLVENT ATOMS 152 REMARK 4 REMARK 4 RESIDUES 258 - 260 SHOW VERY POOR ELECTRON DENSITY. REMARK 5 REMARK 5 N-TERMINAL RESIDUES SER AND ASN ARE ABSENT. SEQRES 1 583 SER ASN GLY ILE GLU ALA SER LEU LEU THR ASP PRO LYS SEQRES 2 583 ASP VAL SER GLY ARG THR VAL ASP TYR ILE ILE ALA GLY SEQRES 3 583 GLY GLY LEU THR GLY LEU THR THR ALA ALA ARG LEU THR SEQRES 4 583 GLU ASN PRO ASN ILE SER VAL LEU VAL ILE GLU SER GLY SEQRES 5 583 SER TYR GLU SER ASP ARG GLY PRO ILE ILE GLU ASP LEU SEQRES 6 583 ASN ALA TYR GLY ASP ILE PHE GLY SER SER VAL ASP HIS SEQRES 7 583 ALA TYR GLU THR VAL GLU LEU ALA THR ASN ASN GLN THR SEQRES 8 583 ALA LEU ILE ARG SER GLY ASN GLY LEU GLY GLY SER THR SEQRES 9 583 LEU VAL ASN GLY GLY THR TRP THR ARG PRO HIS LYS ALA SEQRES 10 583 GLN VAL ASP SER TRP GLU THR VAL PHE GLY ASN GLU GLY SEQRES 11 583 TRP ASN TRP ASP ASN VAL ALA ALA TYR SER LEU GLN ALA SEQRES 12 583 GLU ARG ALA ARG ALA PRO ASN ALA LYS GLN ILE ALA ALA SEQRES 13 583 GLY HIS TYR PHE ASN ALA SER CYS HIS GLY VAL ASN GLY SEQRES 14 583 THR VAL HIS ALA GLY PRO ARG ASP THR GLY ASP ASP TYR SEQRES 15 583 SER PRO ILE VAL LYS ALA LEU MET SER ALA VAL GLU ASP SEQRES 16 583 ARG GLY VAL PRO THR LYS LYS ASP PHE GLY CYS GLY ASP SEQRES 17 583 PRO HIS GLY VAL SER MET PHE PRO ASN THR LEU HIS GLU SEQRES 18 583 ASP GLN VAL ARG SER ASP ALA ALA ARG GLU TRP LEU LEU SEQRES 19 583 PRO ASN TYR GLN ARG PRO ASN LEU GLN VAL LEU THR GLY SEQRES 20 583 GLN TYR VAL GLY LYS VAL LEU LEU SER GLN ASN GLY THR SEQRES 21 583 THR PRO ARG ALA VAL GLY VAL GLU PHE GLY THR HIS LYS SEQRES 22 583 GLY ASN THR HIS ASN VAL TYR ALA LYS HIS GLU VAL LEU SEQRES 23 583 LEU ALA ALA GLY SER ALA VAL SER PRO THR ILE LEU GLU SEQRES 24 583 TYR SER GLY ILE GLY MET LYS SER ILE LEU GLU PRO LEU SEQRES 25 583 GLY ILE ASP THR VAL VAL ASP LEU PRO VAL GLY LEU ASN SEQRES 26 583 LEU GLN ASP GLN THR THR ALA THR VAL ARG SER ARG ILE SEQRES 27 583 THR SER ALA GLY ALA GLY GLN GLY GLN ALA ALA TRP PHE SEQRES 28 583 ALA THR PHE ASN GLU THR PHE GLY ASP TYR SER GLU LYS SEQRES 29 583 ALA HIS GLU LEU LEU ASN THR LYS LEU GLU GLN TRP ALA SEQRES 30 583 GLU GLU ALA VAL ALA ARG GLY GLY PHE HIS ASN THR THR SEQRES 31 583 ALA LEU LEU ILE GLN TYR GLU ASN TYR ARG ASP TRP ILE SEQRES 32 583 VAL ASN HIS ASN VAL ALA TYR SER GLU LEU PHE LEU ASP SEQRES 33 583 THR ALA GLY VAL ALA SER PHE ASP VAL TRP ASP LEU LEU SEQRES 34 583 PRO PHE THR ARG GLY TYR VAL HIS ILE LEU ASP LYS ASP SEQRES 35 583 PRO TYR LEU HIS HIS PHE ALA TYR ASP PRO GLN TYR PHE SEQRES 36 583 LEU ASN GLU LEU ASP LEU LEU GLY GLN ALA ALA ALA THR SEQRES 37 583 GLN LEU ALA ARG ASN ILE SER ASN SER GLY ALA MET GLN SEQRES 38 583 THR TYR PHE ALA GLY GLU THR ILE PRO GLY ASP ASN LEU SEQRES 39 583 ALA TYR ASP ALA ASP LEU SER ALA TRP THR GLU TYR ILE SEQRES 40 583 PRO TYR HIS PHE ARG PRO ASN TYR HIS GLY VAL GLY THR SEQRES 41 583 CYS SER MET MET PRO LYS GLU MET GLY GLY VAL VAL ASP SEQRES 42 583 ASN ALA ALA ARG VAL TYR GLY VAL GLN GLY LEU ARG VAL SEQRES 43 583 ILE ASP GLY SER ILE PRO PRO THR GLN MET SER SER HIS SEQRES 44 583 VAL MET THR VAL PHE TYR ALA MET ALA LEU LYS ILE SER SEQRES 45 583 ASP ALA ILE LEU GLU ASP TYR ALA SER MET GLN FTNOTE 1 FTNOTE 1 RESIDUE 490 IS A CIS PROLINE. HET FAD 600 53 FLAVIN-ADENINE DINUCLEOTIDE HET NAG 601 14 N-ACETYL-D-GLUCOSAMINE HET NAG 602 14 N-ACETYL-D-GLUCOSAMINE HET NAG 604 14 N-ACETYL-D-GLUCOSAMINE HET NAG 605 14 N-ACETYL-D-GLUCOSAMINE HET NAG 608 14 N-ACETYL-D-GLUCOSAMINE HET NAG 609 14 N-ACETYL-D-GLUCOSAMINE HET MAN 613 11 ALPHA-D-MANNOSE HET MAN 615 11 ALPHA-D-MANNOSE HET MAN 616 11 ALPHA-D-MANNOSE FORMUL 2 FAD C27 H33 N9 O15 P2 FORMUL 3 NAG 6(C8 H15 N1 O6) FORMUL 4 MAN 3(C6 H12 O6) FORMUL 5 HOH *152(H2 O1) HELIX 1 H1 LEU 29 LEU 38 1 HELIX 2 H2 LYS 116 THR 124 1 HELIX 3 H3 TRP 133 ALA 143 1 HELIX 4 H4 ALA 151 ALA 156 1 HELIX 5 H5 ILE 185 GLU 194 1 HELIX 6 H6 ALA 228 TRP 232 1 HELIX 7 H7 SER 294 SER 301 1 HELIX 8 H8 PHE 354 PHE 358 1 HELIX 9 H9 SER 362 ALA 382 1 HELIX 10 H10 THR 389 VAL 404 1 HELIX 11 H11 GLU 458 SER 475 1 HELIX 12 H12 LEU 500 TYR 506 1 HELIX 13 H13 MET 561 SER 581 1 SHEET 1 A 5 LEU 242 LEU 245 0 SHEET 2 A 5 VAL 46 ILE 49 1 SHEET 3 A 5 THR 19 ALA 25 1 SHEET 4 A 5 HIS 283 LEU 287 1 SHEET 5 A 5 LEU 544 VAL 546 1 SHEET 1 B 3 TYR 249 SER 256 0 SHEET 2 B 3 ARG 263 HIS 272 -1 SHEET 3 B 3 ASN 275 ALA 281 -1 SHEET 1 C 6 GLY 211 SER 213 0 SHEET 2 C 6 GLN 347 THR 353 -1 SHEET 3 C 6 ALA 409 ASP 416 -1 SHEET 4 C 6 VAL 420 ASP 427 -1 SHEET 5 C 6 THR 330 ILE 338 -1 SHEET 6 C 6 PHE 484 ILE 489 -1 SHEET 1 D 3 LEU 324 LEU 326 0 SHEET 2 D 3 GLY 434 ILE 438 -1 SHEET 3 D 3 PHE 448 ASP 451 -1 SSBOND 1 CYS 164 CYS 206 CRYST1 66.500 66.500 214.500 90.00 90.00 120.00 P 31 2 1 6 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 0.015038 0.008682 0.000000 0.00000 SCALE2 0.000000 0.017364 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004662 0.00000