PDB:1QJN HEADER OXIDASE 28-JUN-99 1QJN TITLE ARYL-ALCOHOL OXIDASE (AAO) FROM PLEUROTUS ERYNGII TITLE 2 (MATURE PROTEIN) COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARYL-ALCOHOL OXIDASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: VERATRYL ALCOHOL OXIDASE; COMPND 5 EC: 1.1.3.7 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLEUROTUS ERYNGII; SOURCE 3 ORGANISM_COMMON: THISTLE MUSHROOM; SOURCE 4 STRAIN: IJFM A169; SOURCE 5 ATCC: 90787; SOURCE 6 ORGAN: HETEROKARYOTIC MYCELIUM; SOURCE 7 GENE: AAO KEYWDS OXIDASE, OXIDOREDUCTASE, FLAVOPROTEIN, HYDROGEN PEROXIDE KEYWDS 2 GENERATION, AROMATIC ALCOHOL OXIDATION, LIGNIN DEGRADATION, KEYWDS 3 EC 1.1.3.7 EXPDTA THEORETICAL MODEL AUTHOR A.T.MARTINEZ,E.VARELA,M.J.MARTINEZ REVDAT 3 12-FEB-04 1QJN 1 JRNL REVDAT 2 27-NOV-01 1QJN 1 JRNL REVDAT 1 29-JUN-00 1QJN 0 JRNL AUTH E.VARELA,M.J.MARTINEZ,A.T.MARTINEZ JRNL TITL ARYL-ALCOHOL OXIDASE PROTEIN SEQUENCE: A COMPARISON JRNL TITL 2 WITH GLUCOSE OXIDASE AND OTHER FAD OXIDOREDUCTASES JRNL REF BIOCHIM.BIOPHYS.ACTA V.1481 202 2001 JRNL REFN ASTM BBACAQ NE ISSN 0006-3002 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.VARELA REMARK 1 TITL DETECCION DE GENES QUE CODIFICAN REMARK 1 TITL 2 LIGNINA PEROXIDASA Y ARIL-ALCOHOL OXIDASA (AAO) EN REMARK 1 TITL 3 HONGOS LIGNINOLITICOS. CARACTERIZACION BIOQUIMICA Y REMARK 1 TITL 4 MOLECULAR DE LA AAO DE PLEUROTUS SPP REMARK 1 REF PH D THESIS 1998 REMARK 1 PUBL MADRID : FASTER (THESIS) REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH E.VARELA,A.T.MARTINEZ,M.J.MARTINEZ REMARK 1 TITL MOLECULAR CLONING OF ARYL-ALCOHOL OXIDASE FROM THE REMARK 1 TITL 2 FUNGUS PLEUROTUS ERYNGII, AN ENZYME INVOLVED IN REMARK 1 TITL 3 LIGNIN DERADATION REMARK 1 REF BIOCHEM.J. V. 341 113 1999 REMARK 1 REFN ASTM BIJOAK UK ISSN 0306-3275 REMARK 1 REFERENCE 3 REMARK 1 AUTH F.GUILLEN,A.T.MARTINEZ,M.J.MARTINEZ REMARK 1 TITL SUBSTRATE SPECIFICITY AND PROPERTIES OF THE REMARK 1 TITL 2 ARYL-ALCOHOL OXIDASE FROM THE LIGNINOLYTIC FUNGUS REMARK 1 TITL 3 PLEUROTUS ERYNGII REMARK 1 REF EUR.J.BIOCHEM. V. 209 603 1992 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CHARMM REMARK 3 AUTHORS : BROOKS ET AL. REMARK 3 REF : J. COMP. CHEM. V. 4 187 1983 REMARK 3 REMARKS : ENERGY MINIMIZATION AND DYNAMICS CALCULATION REMARK 3 REMARK 3 PROGRAM : GROMOS96 REMARK 3 AUTHORS : VAN GUNSTEREN ET AL. REMARK 3 REF : BIOMOLECULAR SIMULATION REMARK 3 VDF HOCHSCHULVERLAG AG AND DER ETH, ZURICH, SWITZERLAND, REMARK 3 PP 1-1042 1996 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ENERGY MINIMIZATION USING 43B1 REMARK 3 PARAMETER SET WITHOUT REACTION FIELD REMARK 4 REMARK 4 1QJN COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 29-JUN-1999. REMARK 100 THE EBI ID CODE IS EBI-2891. REMARK 220 REMARK 220 EXPERIMENTAL DETAILS REMARK 220 EXPERIMENT TYPE: THEORETICAL MODELLING REMARK 220 MODELLING PROGRAM: PROMOD REMARK 220 PROGRAM AUTHORS: M.C. PEITSCH REMARK 220 REF : BIOCHEM. SOC. TRANS. V. 24 274 1996 REMARK 220 MODELLING EXPERIMENT: THIS HOMOLOGY MODEL IS BASED UPON THE REMARK 220 CRYSTAL COORDINATES OF 1GAL (ASPERGILLUS NIGER GLUCOSE OXIDASE) REMARK 220 FOLLOWED BY CHARMM AND GROMOS96 REFINING. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1GAL RELATED DB: PDB REMARK 900 GLUCOSE OXIDASE (E.C.1.1.3.4) (ASPERGILLUS NIGER) REMARK 900 DBREF 1QJN A 1 562 SWALL O94219 O94219 31 592 SEQRES 1 A 562 ASP TYR VAL VAL VAL GLY ALA GLY ASN ALA GLY ASN VAL SEQRES 2 A 562 VAL ALA ALA ARG LEU THR GLU ASP PRO ASP VAL SER VAL SEQRES 3 A 562 LEU VAL LEU GLU ALA GLY VAL SER ASP GLU ASN VAL LEU SEQRES 4 A 562 GLY ALA GLU ALA PRO LEU LEU ALA PRO GLY LEU VAL PRO SEQRES 5 A 562 ASN SER ILE PHE ASP TRP ASN TYR THR THR THR ALA GLN SEQRES 6 A 562 ALA GLY TYR ASN GLY ARG SER ILE ALA TYR PRO ARG GLY SEQRES 7 A 562 ARG MET LEU GLY GLY SER SER SER VAL HIS TYR MET VAL SEQRES 8 A 562 MET MET ARG GLY SER THR GLU ASP PHE ASP ARG TYR ALA SEQRES 9 A 562 ALA VAL THR GLY ASP GLU GLY TRP ASN TRP ASP ASN ILE SEQRES 10 A 562 GLN GLN PHE VAL ARG LYS ASN GLU MET VAL VAL PRO PRO SEQRES 11 A 562 ALA ASP ASN HIS ASN THR SER GLY GLU PHE ILE PRO ALA SEQRES 12 A 562 VAL HIS GLY THR ASN GLY SER VAL SER ILE SER LEU PRO SEQRES 13 A 562 GLY PHE PRO THR PRO LEU ASP ASP ARG VAL LEU ALA THR SEQRES 14 A 562 THR GLN GLU GLN SER GLU GLU PHE PHE PHE ASN PRO ASP SEQRES 15 A 562 MET GLY THR GLY HIS PRO LEU GLY ILE SER TRP SER ILE SEQRES 16 A 562 ALA SER VAL GLY ASN GLY GLN ARG SER SER SER SER THR SEQRES 17 A 562 ALA TYR LEU ARG PRO ALA GLN SER ARG PRO ASN LEU SER SEQRES 18 A 562 VAL LEU ILE ASN ALA GLN VAL THR LYS LEU VAL ASN SER SEQRES 19 A 562 GLY THR THR ASN GLY LEU PRO ALA PHE ARG CYS VAL GLU SEQRES 20 A 562 TYR ALA GLU GLN GLU GLY ALA PRO THR THR THR VAL CYS SEQRES 21 A 562 ALA LYS LYS GLU VAL VAL LEU SER ALA GLY SER VAL GLY SEQRES 22 A 562 THR PRO ILE LEU LEU GLN LEU SER GLY ILE GLY ASP GLU SEQRES 23 A 562 ASN ASP LEU SER SER VAL GLY ILE ASP THR ILE VAL ASN SEQRES 24 A 562 ASN PRO SER VAL GLY ARG ASN LEU SER ASP HIS LEU LEU SEQRES 25 A 562 LEU PRO ALA ALA PHE PHE VAL ASN SER ASN GLN THR PHE SEQRES 26 A 562 ASP ASN ILE PHE ARG ASP SER SER GLU PHE ASN VAL ASP SEQRES 27 A 562 LEU ASP GLN TRP THR ASN THR ARG THR GLY PRO LEU THR SEQRES 28 A 562 ALA LEU ILE ALA ASN HIS LEU ALA TRP LEU ARG LEU PRO SEQRES 29 A 562 SER ASN SER SER ILE PHE GLN THR PHE PRO ASP PRO ALA SEQRES 30 A 562 ALA GLY PRO ASN SER ALA HIS TRP GLU THR ILE PHE SER SEQRES 31 A 562 ASN GLN TRP PHE HIS PRO ALA ILE PRO ARG PRO ASP THR SEQRES 32 A 562 GLY SER PHE MET SER VAL THR ASN ALA LEU ILE SER PRO SEQRES 33 A 562 VAL ALA ARG GLY ASP ILE LYS LEU ALA THR SER ASN PRO SEQRES 34 A 562 PHE ASP LYS PRO LEU ILE ASN PRO GLN TYR LEU SER THR SEQRES 35 A 562 GLU PHE ASP ILE PHE THR MET ILE GLN ALA VAL LYS SER SEQRES 36 A 562 ASN LEU ARG PHE LEU SER GLY GLN ALA TRP ALA ASP PHE SEQRES 37 A 562 VAL ILE ARG PRO PHE ASP PRO ARG LEU ARG ASP PRO THR SEQRES 38 A 562 ASP ASP ALA ALA ILE GLU SER TYR ILE ARG ASP ASN ALA SEQRES 39 A 562 ASN THR ILE PHE HIS PRO VAL GLY THR ALA SER MET SER SEQRES 40 A 562 PRO ARG GLY ALA SER TRP GLY VAL VAL ASP PRO ASP LEU SEQRES 41 A 562 LYS VAL LYS GLY VAL ASP GLY LEU ARG ILE VAL ASP GLY SEQRES 42 A 562 SER ILE LEU PRO PHE ALA PRO ASN ALA HIS THR GLN GLY SEQRES 43 A 562 PRO ILE TYR LEU VAL GLY LYS GLN GLY ALA ASP LEU ILE SEQRES 44 A 562 LYS ALA ASP HELIX 1 1 GLY A 8 THR A 19 1 12 HELIX 2 2 GLY A 83 SER A 86 5 4 HELIX 3 3 SER A 96 VAL A 106 1 11 HELIX 4 4 ASN A 113 LYS A 123 1 11 HELIX 5 5 ALA A 131 GLY A 138 1 8 HELIX 6 6 ASP A 164 PHE A 177 1 14 HELIX 7 7 SER A 205 TYR A 210 1 6 HELIX 8 8 LEU A 211 GLN A 215 5 5 HELIX 9 9 VAL A 272 SER A 281 1 10 HELIX 10 10 ASP A 285 VAL A 292 1 8 HELIX 11 11 SER A 321 THR A 324 5 4 HELIX 12 12 GLU A 334 ASP A 340 1 7 HELIX 13 13 TRP A 342 ALA A 355 1 14 HELIX 14 14 LEU A 358 SER A 368 1 11 HELIX 15 15 PRO A 374 SER A 390 1 17 HELIX 16 16 THR A 442 SER A 461 1 20 HELIX 17 17 GLY A 462 ASP A 467 5 6 HELIX 18 18 ASP A 482 ARG A 491 1 10 HELIX 19 19 THR A 544 ILE A 559 1 16 SHEET 1 A 5 LEU A 528 ILE A 530 0 SHEET 2 A 5 GLU A 264 LEU A 267 1 N VAL A 265 O ARG A 529 SHEET 3 A 5 TYR A 2 VAL A 5 1 N VAL A 3 O GLU A 264 SHEET 4 A 5 VAL A 26 LEU A 29 1 N LEU A 27 O TYR A 2 SHEET 5 A 5 LEU A 220 LEU A 223 1 N SER A 221 O VAL A 26 SHEET 1 B 2 GLU A 125 VAL A 127 0 SHEET 2 B 2 VAL A 151 ILE A 153 1 N VAL A 151 O MET A 126 SHEET 1 C 2 GLY A 190 TRP A 193 0 SHEET 2 C 2 PHE A 329 SER A 332 -1 N SER A 332 O GLY A 190 SHEET 1 D 3 LEU A 312 PHE A 317 0 SHEET 2 D 3 MET A 407 LEU A 413 -1 N ASN A 411 O LEU A 313 SHEET 3 D 3 ALA A 397 ASP A 402 -1 N ASP A 402 O SER A 408 CISPEP 1 GLN A 392 TRP A 393 0 -14.04 CISPEP 2 GLY A 502 THR A 503 0 -6.96 SSBOND 1 CYS A 245 CYS A 260 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 ATOM 1 N ASP A 1 -27.464 -4.968 -4.065 1.00 42.50 N 199906281MJRNL AUTH E.VARELA,M.J.MARTINEZ,A.T.MARTINEZ JRNL TITL ARYL-ALCOHOL OXIDASE PROTEIN SEQUENCE: A COMPARISON JRNL TITL 2 WITH GLUCOSE OXIDASE AND OTHER FAD OXIDOREDUCTASES JRNL REF BIOCHIM.BIOPHYS.ACTA V.1481 202 2001 JRNL REFN ASTM BBACAQ NE ISSN 0006-3002 REMARK 1 AUTH E.VARELA REMARK 1 TITL DETECCION DE GENES QUE CODIFICAN REMARK 1 TITL 2 LIGNINA PEROXIDASA Y ARIL-ALCOHOL OXIDASA (AAO) EN REMARK 1 TITL 3 HONGOS LIGNINOLITICOS. CARACTERIZACION BIOQUIMICA Y REMARK 1 TITL 4 MOLECULAR DE LA AAO DE PLEUROTUS SPP REMARK 1 REF PH D THESIS 1998 REMARK 1 PUBL MADRID : FASTER (THESIS) REMARK 1 REFN REMARK 1 AUTH E.VARELA,A.T.MARTINEZ,M.J.MARTINEZ REMARK 1 TITL MOLECULAR CLONING OF ARYL-ALCOHOL OXIDASE FROM THE REMARK 1 TITL 2 FUNGUS PLEUROTUS ERYNGII, AN ENZYME INVOLVED IN REMARK 1 TITL 3 LIGNIN DERADATION REMARK 1 REF BIOCHEM.J. V. 341 113 1999 REMARK 1 REFN ASTM BIJOAK UK ISSN 0306-3275 REMARK 1 AUTH F.GUILLEN,A.T.MARTINEZ,M.J.MARTINEZ REMARK 1 TITL SUBSTRATE SPECIFICITY AND PROPERTIES OF THE REMARK 1 TITL 2 ARYL-ALCOHOL OXIDASE FROM THE LIGNINOLYTIC FUNGUS REMARK 1 TITL 3 PLEUROTUS ERYNGII REMARK 1 REF EUR.J.BIOCHEM. V. 209 603 1992 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 99.0000001.0001.0001.00090.0090.0090.00P 1HELIX 1 1 GLY A 8 THR A 19 1 12 HELIX 2 2 GLY A 83 SER A 86 5 4 HELIX 3 3 SER A 96 VAL A 106 1 11 HELIX 4 4 ASN A 113 LYS A 123 1 11 HELIX 5 5 ALA A 131 GLY A 138 1 8 HELIX 6 6 ASP A 164 PHE A 177 1 14 HELIX 7 7 SER A 205 TYR A 210 1 6 HELIX 8 8 LEU A 211 GLN A 215 5 5 HELIX 9 9 VAL A 272 SER A 281 1 10 HELIX 10 10 ASP A 285 VAL A 292 1 8 HELIX 11 11 SER A 321 THR A 324 5 4 HELIX 12 12 GLU A 334 ASP A 340 1 7 HELIX 13 13 TRP A 342 ALA A 355 1 14 HELIX 14 14 LEU A 358 SER A 368 1 11 HELIX 15 15 PRO A 374 SER A 390 1 17 HELIX 16 16 THR A 442 SER A 461 1 20 HELIX 17 17 GLY A 462 ASP A 467 5 6 HELIX 18 18 ASP A 482 ARG A 491 1 10 HELIX 19 19 THR A 544 ILE A 559 1 16 SHEET 1 A 5 LEU A 528 ILE A 530 0 SHEET 2 A 5 GLU A 264 LEU A 267 1 N VAL A 265 O ARG A 529 SHEET 3 A 5 TYR A 2 VAL A 5 1 N VAL A 3 O GLU A 264 SHEET 4 A 5 VAL A 26 LEU A 29 1 N LEU A 27 O TYR A 2 SHEET 5 A 5 LEU A 220 LEU A 223 1 N SER A 221 O VAL A 26 SHEET 1 B 2 GLU A 125 VAL A 127 0 SHEET 2 B 2 VAL A 151 ILE A 153 1 N VAL A 151 O MET A 126 SHEET 1 C 2 GLY A 190 TRP A 193 0 SHEET 2 C 2 PHE A 329 SER A 332 -1 N SER A 332 O GLY A 190 SHEET 1 D 3 LEU A 312 PHE A 317 0 SHEET 2 D 3 MET A 407 LEU A 413 -1 N ASN A 411 O LEU A 313 SHEET 3 D 3 ALA A 397 ASP A 402 -1 N ASP A 402 O SER A 408 HEADER OXIDASE 28-JUN-99 1QJN TITLE ARYL-ALCOHOL OXIDASE (AAO) FROM PLEUROTUS ERYNGII TITLE 2 (MATURE PROTEIN) COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARYL-ALCOHOL OXIDASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: VERATRYL ALCOHOL OXIDASE; COMPND 5 EC: 1.1.3.7 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLEUROTUS ERYNGII; SOURCE 3 ORGANISM_COMMON: THISTLE MUSHROOM; SOURCE 4 STRAIN: IJFM A169; SOURCE 5 ATCC: 90787; SOURCE 6 ORGAN: HETEROKARYOTIC MYCELIUM; SOURCE 7 GENE: AAO KEYWDS OXIDASE, OXIDOREDUCTASE, FLAVOPROTEIN, HYDROGEN PEROXIDE KEYWDS 2 GENERATION, AROMATIC ALCOHOL OXIDATION, LIGNIN DEGRADATION, KEYWDS 3 EC 1.1.3.7 EXPDTA THEORETICAL MODEL AUTHOR A.T.MARTINEZ,E.VARELA,M.J.MARTINEZ REVDAT 3 12-FEB-04 1QJN 1 JRNL REVDAT 2 27-NOV-01 1QJN 1 JRNL REVDAT 1 29-JUN-00 1QJN 0 JRNL AUTH E.VARELA,M.J.MARTINEZ,A.T.MARTINEZ JRNL TITL ARYL-ALCOHOL OXIDASE PROTEIN SEQUENCE: A COMPARISON JRNL TITL 2 WITH GLUCOSE OXIDASE AND OTHER FAD OXIDOREDUCTASES JRNL REF BIOCHIM.BIOPHYS.ACTA V.1481 202 2001 JRNL REFN ASTM BBACAQ NE ISSN 0006-3002 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.VARELA REMARK 1 TITL DETECCION DE GENES QUE CODIFICAN REMARK 1 TITL 2 LIGNINA PEROXIDASA Y ARIL-ALCOHOL OXIDASA (AAO) EN REMARK 1 TITL 3 HONGOS LIGNINOLITICOS. CARACTERIZACION BIOQUIMICA Y REMARK 1 TITL 4 MOLECULAR DE LA AAO DE PLEUROTUS SPP REMARK 1 REF PH D THESIS 1998 REMARK 1 PUBL MADRID : FASTER (THESIS) REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH E.VARELA,A.T.MARTINEZ,M.J.MARTINEZ REMARK 1 TITL MOLECULAR CLONING OF ARYL-ALCOHOL OXIDASE FROM THE REMARK 1 TITL 2 FUNGUS PLEUROTUS ERYNGII, AN ENZYME INVOLVED IN REMARK 1 TITL 3 LIGNIN DERADATION REMARK 1 REF BIOCHEM.J. V. 341 113 1999 REMARK 1 REFN ASTM BIJOAK UK ISSN 0306-3275 REMARK 1 REFERENCE 3 REMARK 1 AUTH F.GUILLEN,A.T.MARTINEZ,M.J.MARTINEZ REMARK 1 TITL SUBSTRATE SPECIFICITY AND PROPERTIES OF THE REMARK 1 TITL 2 ARYL-ALCOHOL OXIDASE FROM THE LIGNINOLYTIC FUNGUS REMARK 1 TITL 3 PLEUROTUS ERYNGII REMARK 1 REF EUR.J.BIOCHEM. V. 209 603 1992 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CHARMM REMARK 3 AUTHORS : BROOKS ET AL. REMARK 3 REF : J. COMP. CHEM. V. 4 187 1983 REMARK 3 REMARKS : ENERGY MINIMIZATION AND DYNAMICS CALCULATION REMARK 3 REMARK 3 PROGRAM : GROMOS96 REMARK 3 AUTHORS : VAN GUNSTEREN ET AL. REMARK 3 REF : BIOMOLECULAR SIMULATION REMARK 3 VDF HOCHSCHULVERLAG AG AND DER ETH, ZURICH, SWITZERLAND, REMARK 3 PP 1-1042 1996 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ENERGY MINIMIZATION USING 43B1 REMARK 3 PARAMETER SET WITHOUT REACTION FIELD REMARK 4 REMARK 4 1QJN COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 29-JUN-1999. REMARK 100 THE EBI ID CODE IS EBI-2891. REMARK 220 REMARK 220 EXPERIMENTAL DETAILS REMARK 220 EXPERIMENT TYPE: THEORETICAL MODELLING REMARK 220 MODELLING PROGRAM: PROMOD REMARK 220 PROGRAM AUTHORS: M.C. PEITSCH REMARK 220 REF : BIOCHEM. SOC. TRANS. V. 24 274 1996 REMARK 220 MODELLING EXPERIMENT: THIS HOMOLOGY MODEL IS BASED UPON THE REMARK 220 CRYSTAL COORDINATES OF 1GAL (ASPERGILLUS NIGER GLUCOSE OXIDASE) REMARK 220 FOLLOWED BY CHARMM AND GROMOS96 REFINING. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1GAL RELATED DB: PDB REMARK 900 GLUCOSE OXIDASE (E.C.1.1.3.4) (ASPERGILLUS NIGER) REMARK 900 DBREF 1QJN A 1 562 SWALL O94219 O94219 31 592 SEQRES 1 A 562 ASP TYR VAL VAL VAL GLY ALA GLY ASN ALA GLY ASN VAL SEQRES 2 A 562 VAL ALA ALA ARG LEU THR GLU ASP PRO ASP VAL SER VAL SEQRES 3 A 562 LEU VAL LEU GLU ALA GLY VAL SER ASP GLU ASN VAL LEU SEQRES 4 A 562 GLY ALA GLU ALA PRO LEU LEU ALA PRO GLY LEU VAL PRO SEQRES 5 A 562 ASN SER ILE PHE ASP TRP ASN TYR THR THR THR ALA GLN SEQRES 6 A 562 ALA GLY TYR ASN GLY ARG SER ILE ALA TYR PRO ARG GLY SEQRES 7 A 562 ARG MET LEU GLY GLY SER SER SER VAL HIS TYR MET VAL SEQRES 8 A 562 MET MET ARG GLY SER THR GLU ASP PHE ASP ARG TYR ALA SEQRES 9 A 562 ALA VAL THR GLY ASP GLU GLY TRP ASN TRP ASP ASN ILE SEQRES 10 A 562 GLN GLN PHE VAL ARG LYS ASN GLU MET VAL VAL PRO PRO SEQRES 11 A 562 ALA ASP ASN HIS ASN THR SER GLY GLU PHE ILE PRO ALA SEQRES 12 A 562 VAL HIS GLY THR ASN GLY SER VAL SER ILE SER LEU PRO SEQRES 13 A 562 GLY PHE PRO THR PRO LEU ASP ASP ARG VAL LEU ALA THR SEQRES 14 A 562 THR GLN GLU GLN SER GLU GLU PHE PHE PHE ASN PRO ASP SEQRES 15 A 562 MET GLY THR GLY HIS PRO LEU GLY ILE SER TRP SER ILE SEQRES 16 A 562 ALA SER VAL GLY ASN GLY GLN ARG SER SER SER SER THR SEQRES 17 A 562 ALA TYR LEU ARG PRO ALA GLN SER ARG PRO ASN LEU SER SEQRES 18 A 562 VAL LEU ILE ASN ALA GLN VAL THR LYS LEU VAL ASN SER SEQRES 19 A 562 GLY THR THR ASN GLY LEU PRO ALA PHE ARG CYS VAL GLU SEQRES 20 A 562 TYR ALA GLU GLN GLU GLY ALA PRO THR THR THR VAL CYS SEQRES 21 A 562 ALA LYS LYS GLU VAL VAL LEU SER ALA GLY SER VAL GLY SEQRES 22 A 562 THR PRO ILE LEU LEU GLN LEU SER GLY ILE GLY ASP GLU SEQRES 23 A 562 ASN ASP LEU SER SER VAL GLY ILE ASP THR ILE VAL ASN SEQRES 24 A 562 ASN PRO SER VAL GLY ARG ASN LEU SER ASP HIS LEU LEU SEQRES 25 A 562 LEU PRO ALA ALA PHE PHE VAL ASN SER ASN GLN THR PHE SEQRES 26 A 562 ASP ASN ILE PHE ARG ASP SER SER GLU PHE ASN VAL ASP SEQRES 27 A 562 LEU ASP GLN TRP THR ASN THR ARG THR GLY PRO LEU THR SEQRES 28 A 562 ALA LEU ILE ALA ASN HIS LEU ALA TRP LEU ARG LEU PRO SEQRES 29 A 562 SER ASN SER SER ILE PHE GLN THR PHE PRO ASP PRO ALA SEQRES 30 A 562 ALA GLY PRO ASN SER ALA HIS TRP GLU THR ILE PHE SER SEQRES 31 A 562 ASN GLN TRP PHE HIS PRO ALA ILE PRO ARG PRO ASP THR SEQRES 32 A 562 GLY SER PHE MET SER VAL THR ASN ALA LEU ILE SER PRO SEQRES 33 A 562 VAL ALA ARG GLY ASP ILE LYS LEU ALA THR SER ASN PRO SEQRES 34 A 562 PHE ASP LYS PRO LEU ILE ASN PRO GLN TYR LEU SER THR SEQRES 35 A 562 GLU PHE ASP ILE PHE THR MET ILE GLN ALA VAL LYS SER SEQRES 36 A 562 ASN LEU ARG PHE LEU SER GLY GLN ALA TRP ALA ASP PHE SEQRES 37 A 562 VAL ILE ARG PRO PHE ASP PRO ARG LEU ARG ASP PRO THR SEQRES 38 A 562 ASP ASP ALA ALA ILE GLU SER TYR ILE ARG ASP ASN ALA SEQRES 39 A 562 ASN THR ILE PHE HIS PRO VAL GLY THR ALA SER MET SER SEQRES 40 A 562 PRO ARG GLY ALA SER TRP GLY VAL VAL ASP PRO ASP LEU SEQRES 41 A 562 LYS VAL LYS GLY VAL ASP GLY LEU ARG ILE VAL ASP GLY SEQRES 42 A 562 SER ILE LEU PRO PHE ALA PRO ASN ALA HIS THR GLN GLY SEQRES 43 A 562 PRO ILE TYR LEU VAL GLY LYS GLN GLY ALA ASP LEU ILE SEQRES 44 A 562 LYS ALA ASP HELIX 1 1 GLY A 8 THR A 19 1 12 HELIX 2 2 GLY A 83 SER A 86 5 4 HELIX 3 3 SER A 96 VAL A 106 1 11 HELIX 4 4 ASN A 113 LYS A 123 1 11 HELIX 5 5 ALA A 131 GLY A 138 1 8 HELIX 6 6 ASP A 164 PHE A 177 1 14 HELIX 7 7 SER A 205 TYR A 210 1 6 HELIX 8 8 LEU A 211 GLN A 215 5 5 HELIX 9 9 VAL A 272 SER A 281 1 10 HELIX 10 10 ASP A 285 VAL A 292 1 8 HELIX 11 11 SER A 321 THR A 324 5 4 HELIX 12 12 GLU A 334 ASP A 340 1 7 HELIX 13 13 TRP A 342 ALA A 355 1 14 HELIX 14 14 LEU A 358 SER A 368 1 11 HELIX 15 15 PRO A 374 SER A 390 1 17 HELIX 16 16 THR A 442 SER A 461 1 20 HELIX 17 17 GLY A 462 ASP A 467 5 6 HELIX 18 18 ASP A 482 ARG A 491 1 10 HELIX 19 19 THR A 544 ILE A 559 1 16 SHEET 1 A 5 LEU A 528 ILE A 530 0 SHEET 2 A 5 GLU A 264 LEU A 267 1 N VAL A 265 O ARG A 529 SHEET 3 A 5 TYR A 2 VAL A 5 1 N VAL A 3 O GLU A 264 SHEET 4 A 5 VAL A 26 LEU A 29 1 N LEU A 27 O TYR A 2 SHEET 5 A 5 LEU A 220 LEU A 223 1 N SER A 221 O VAL A 26 SHEET 1 B 2 GLU A 125 VAL A 127 0 SHEET 2 B 2 VAL A 151 ILE A 153 1 N VAL A 151 O MET A 126 SHEET 1 C 2 GLY A 190 TRP A 193 0 SHEET 2 C 2 PHE A 329 SER A 332 -1 N SER A 332 O GLY A 190 SHEET 1 D 3 LEU A 312 PHE A 317 0 SHEET 2 D 3 MET A 407 LEU A 413 -1 N ASN A 411 O LEU A 313 SHEET 3 D 3 ALA A 397 ASP A 402 -1 N ASP A 402 O SER A 408 CISPEP 1 GLN A 392 TRP A 393 0 -14.04 CISPEP 2 GLY A 502 THR A 503 0 -6.96 SSBOND 1 CYS A 245 CYS A 260 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 ATOM 1 N ASP A 1 -27.464 -4.968 -4.065 1.00 42.50 N