HEADER PEROXIDASE 13-JAN-98 1A20 TITLE MOLECULAR MODEL FOR A PLEUROTUS ERYNGII PEROXIDASE OXIDIZING TITLE 2 MNII AS WELL AS DIFFERENT PHENOLIC AND NON-PHENOLIC TITLE 3 AROMATIC COMPOUNDS AND DYES, THEORETICAL MODEL COMPND MOL_ID: 1; COMPND 2 MOLECULE: PEROXIDASE; COMPND 3 CHAIN: NULL SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLEUROTUS ERYNGII; SOURCE 3 ORGANISM_COMMON: THISTLE MUSHROOM; SOURCE 4 STRAIN: IJFM A169; SOURCE 5 VARIANT: MNPL1 (ALLELIC); SOURCE 6 COLLECTION: ATCC 90787; SOURCE 7 ORGAN: HETEROKARYOTIC MYCELIUM; SOURCE 8 GENE: MNPL KEYWDS POLYVALENT PEROXIDASE, MANGANESE PEROXIDASE, LIGNIN KEYWDS 2 PEROXIDASE, HOMOLOGY MODELING, MNII-BINDING SITE, KEYWDS 3 AROMATIC-SUBSTRATE BINDING, ELECTRON TRANSFER, ALLELIC KEYWDS 4 VARIANT, LIGNIN DEGRADATION, MNII OXIDATION, MN-INDEPENDENT KEYWDS 5 OXIDATION OF PHENOLIC AND NON-PHENOLIC AROMATICS AND DYES, KEYWDS 6 CLASS II (FUNGAL) PEROXIDASES EXPDTA THEORETICAL MODEL AUTHOR A.T.MARTINEZ,A.ROMERO,F.J.RUIZ-DUENAS,M.J.MARTINEZ REVDAT 1 16-FEB-99 1A20 0 JRNL AUTH F.J.RUIZ-DUENAS,M.J.MARTINEZ,A.T.MARTINEZ JRNL TITL MOLECULAR CHARACTERIZATION OF A NOVEL PEROXIDASE JRNL TITL 2 ISOLATED FROM THE LIGNINOLYTIC FUNGUS PLEUROTUS JRNL TITL 3 ERYNGII JRNL REF MOL.MICROBIOL. V. 31 223 1999 JRNL REFN ASTM MOMIEE UK ISSN 0950-382X 2007 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.HEINFLING,F.J.RUIZ-DUENAS,M.J.MARTINEZ, REMARK 1 AUTH 2 M.BERGBAUER,U.SZEWZYK,A.T.MARTINEZ REMARK 1 TITL A STUDY ON REDUCING SUBSTRATES OF REMARK 1 TITL 2 MANGANESE-OXIDIZING PEROXIDASES FROM PLEUROTUS REMARK 1 TITL 3 ERYNGII AND BJERKANDERA ADUSTA REMARK 1 REF FEBS LETT. V. 428 141 1998 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.J.MARTINEZ,F.J.RUIZ-DUENAS,F.GUILLEN,A.T.MARTINEZ REMARK 1 TITL PURIFICATION AND CATALYTIC PROPERTIES OF TWO REMARK 1 TITL 2 MANGANESE PEROXIDASE ISOENZYMES FROM PLEUROTUS REMARK 1 TITL 3 ERYNGII REMARK 1 REF EUR.J.BIOCHEM. V. 237 424 1996 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 0262 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: MOLECULAR DYNAMICS REMARK 4 REMARK 4 1A20 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 220 REMARK 220 EXPERIMENTAL DETAILS REMARK 220 EXPERIMENT TYPE : THEORETICAL MODELLING REMARK 220 REMARK 220 REMARK: REMARK 220 MODELLING PROGRAM: PROMOD REMARK 220 PROGRAM AUTHORS: M.C.PEITSCH REMARK 220 MODELLING EXPERIMENT: - THIS MODEL IS BASED UPON THE REMARK 220 COORDINATES OF 1QPA (X-RAY DIFFRACTION), 1ARP REMARK 220 (X-RAY DIFFRACTION), 1LGA (X-RAY DIFFRACTION), 1MNP REMARK 220 (X-RAY DIFFRACTION) REMARK 220 (FOLLOWED BY CHARMM REFINING, AND MOLECULAR DYNAMICS REMARK 220 REFINING OF PROTEIN PLUS HEM AND MN WITH X-PLOR 3.1) REMARK 225 REMARK 225 THEORETICAL MODEL REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE. REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE REMARK 225 RECORDS ARE MEANINGLESS. REMARK 400 REMARK 400 COMPOUND REMARK 400 THE ENZYME OXIDIZES MN(II) (EC 1.11.1.13), BUT EXHIBITED REMARK 400 ALSO MN-INDEPENDENT PEROXIDASE ACTIVITY ON DYES AND REMARK 400 PHENOLIC (EC 1.11.1.7) AS WELL AS NON-PHENOLIC REMARK 400 (EC 1.11.1.14) AROMATIC SUBSTRATES. REMARK 450 REMARK 450 SOURCE REMARK 450 STRAIN CBS 613.91, TAXONOMIC POSITION: BASIDIOMYCOTA, REMARK 450 HYMENOMYCETES, APHYLLOPHORALES, POLYPORACEAE REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 15 DEGREES (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION REMARK 500 CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 0 GLU 40 OE1 - CD - OE2 ANGL. DEV. = 16.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 4*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 500 NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,A4,A1,2X, REMARK 500 A3,1X,A1,I4,A1,1X,A4,A1,4X,F5.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 0 SER 41 H SER 41 N 0.216 REMARK 500 0 SER 41 HG SER 41 OG 0.265 REMARK 500 0 SER 53 HG SER 53 OG 0.150 REMARK 500 0 ALA 67 H ALA 67 N 0.158 REMARK 500 0 ASN 96 2HD2 ASN 96 ND2 0.158 REMARK 500 0 VAL 118 H VAL 118 N 0.154 REMARK 500 0 ALA 132 H ALA 132 N 0.175 REMARK 500 0 SER 133 HG SER 133 OG 0.151 REMARK 500 0 VAL 162 H VAL 162 N 0.175 REMARK 500 0 THR 201 HG1 THR 201 OG1 0.157 REMARK 500 0 THR 211 HG1 THR 211 OG1 0.153 REMARK 500 0 ILE 276 H ILE 276 N 0.171 REMARK 500 0 ALA 292 H ALA 292 N 0.162 REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: BASED ON DSSP BY KABSCH AND SANDER REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: MN REMARK 800 SITE_DESCRIPTION: MN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: CA1 REMARK 800 SITE_DESCRIPTION: DISTAL CA-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: CA2 REMARK 800 SITE_DESCRIPTION: PROXIMAL CA-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: HME REMARK 800 SITE_DESCRIPTION: CHARACTERISTIC HEME POCKET RESIDUES REMARK 800 (DISTAL AND PROXIMAL SIDES) REMARK 850 REMARK 850 CORRECTION BEFORE RELEASE REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE REMARK 850 DATE REVISED: 15-JAN-1998 TRACKING NUMBER: T14064 REMARK 999 REMARK 999 GENBANK ENTRY: REMARK 999 AF007223 REMARK 999 DIFFERENCES BETWEEN GENBANK AND PDB: REMARK 999 30 AA SIGNAL-PEPTIDE INCLUDED IN AF007223 REMARK 999 GLY360 AND SER361 OF AF007223 ARE NOT INCLUDED IN PDB DBREF 1A20 1 329 PDB 1A20 1A20 1 329 SEQRES 1 329 ALA THR CYS ALA ASP GLY ARG THR THR ALA ASN ALA ALA SEQRES 2 329 CYS CYS VAL LEU PHE PRO ILE LEU ASP ASP ILE GLN GLU SEQRES 3 329 ASN LEU PHE ASP GLY ALA GLN CYS GLY GLU GLU VAL HIS SEQRES 4 329 GLU SER LEU ARG LEU THR PHE HIS ASP ALA ILE GLY PHE SEQRES 5 329 SER PRO THR LEU GLY GLY GLY GLY ALA ASP GLY SER ILE SEQRES 6 329 ILE ALA PHE ASP THR ILE GLU THR ASN PHE PRO ALA ASN SEQRES 7 329 ALA GLY ILE ASP GLU ILE VAL SER ALA GLN LYS PRO PHE SEQRES 8 329 VAL ALA LYS HIS ASN ILE SER ALA GLY ASP PHE ILE GLN SEQRES 9 329 PHE ALA GLY ALA VAL GLY VAL SER ASN CYS PRO GLY GLY SEQRES 10 329 VAL ARG ILE PRO PHE PHE LEU GLY ARG PRO ASP ALA VAL SEQRES 11 329 ALA ALA SER PRO ASP HIS LEU VAL PRO GLU PRO PHE ASP SEQRES 12 329 SER VAL ASP SER ILE LEU ALA ARG MET SER ASP ALA GLY SEQRES 13 329 PHE SER PRO VAL GLU VAL VAL TRP LEU LEU ALA SER HIS SEQRES 14 329 SER ILE ALA ALA ALA ASP LYS VAL ASP PRO SER ILE PRO SEQRES 15 329 GLY THR PRO PHE ASP SER THR PRO GLY VAL PHE ASP SER SEQRES 16 329 GLN PHE PHE ILE GLU THR GLN LEU LYS GLY ARG LEU PHE SEQRES 17 329 PRO GLY THR ALA ASP ASN LYS GLY GLU ALA GLN SER PRO SEQRES 18 329 LEU GLN GLY GLU ILE ARG LEU GLN SER ASP HIS LEU LEU SEQRES 19 329 ALA ARG ASP PRO GLN THR ALA CYS GLU TRP GLN SER MET SEQRES 20 329 VAL ASN ASN GLN PRO LYS ILE GLN ASN ARG PHE ALA ALA SEQRES 21 329 THR MET SER LYS MET ALA LEU LEU GLY GLN ASP LYS THR SEQRES 22 329 LYS LEU ILE ASP CYS SER ASP VAL ILE PRO THR PRO PRO SEQRES 23 329 ALA LEU VAL GLY ALA ALA HIS LEU PRO ALA GLY PHE SER SEQRES 24 329 LEU SER ASP VAL GLU GLN ALA CYS ALA ALA THR PRO PHE SEQRES 25 329 PRO ALA LEU THR ALA ASP PRO GLY PRO VAL THR SER VAL SEQRES 26 329 PRO PRO VAL PRO HET HEM 396 44 PROTOPORPHYRIN IX CONTAINS FE(III) HET MN 400 1 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM MN MANGANESE (II) ION HETSYN HEM HEME FORMUL 2 HEM C34 H32 N4 O4 FE1 1+ FORMUL 3 MN MN1 2+ HELIX 1 A ALA 12 ASN 27 5 16 HELIX 2 B GLU 36 GLY 51 1 16 HELIX 3 B' SER 64 ALA 67 1 4 HELIX 4 B'' ASP 69 GLU 72 1 4 HELIX 5 C ILE 81 HIS 95 1 15 HELIX 6 D ALA 99 ASN 113 1 15 HELIX 7 E VAL 145 ALA 155 1 11 HELIX 8 F PRO 159 ILE 171 1 13 HELIX 9 G SER 195 GLU 200 5 6 HELIX 10 H GLN 229 ARG 236 1 8 HELIX 11 I ALA 241 MET 247 1 7 HELIX 12 J GLN 251 ALA 266 1 16 SSBOND 1 CYS 3 CYS 15 SSBOND 2 CYS 14 CYS 278 SSBOND 3 CYS 34 CYS 114 SSBOND 4 CYS 242 CYS 307 SITE 1 MN 5 GLU 36 GLU 40 ALA 174 ASP 175 SITE 2 MN 5 HEM 396 SITE 1 CA1 4 ASP 48 GLY 60 ASP 62 SER 64 SITE 1 CA2 5 SER 170 ASP 187 THR 189 VAL 192 SITE 2 CA2 5 ASP 194 SITE 1 HME 6 ARG 43 PHE 46 HIS 47 HIS 169 SITE 2 HME 6 PHE 186 ASP 231 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 ALA 1 24.033 19.016 69.336 1.00 28.33 N 199801131MJRNL AUTH F.J.RUIZ-DUENAS,M.J.MARTINEZ,A.T.MARTINEZ JRNL TITL MOLECULAR CHARACTERIZATION OF A NOVEL PEROXIDASE JRNL TITL 2 ISOLATED FROM THE LIGNINOLYTIC FUNGUS PLEUROTUS JRNL TITL 3 ERYNGII JRNL REF MOL.MICROBIOL. V. 31 223 1999 JRNL REFN ASTM MOMIEE UK ISSN 0950-382X 2007 REMARK 1 AUTH A.HEINFLING,F.J.RUIZ-DUENAS,M.J.MARTINEZ, REMARK 1 AUTH 2 M.BERGBAUER,U.SZEWZYK,A.T.MARTINEZ REMARK 1 TITL A STUDY ON REDUCING SUBSTRATES OF REMARK 1 TITL 2 MANGANESE-OXIDIZING PEROXIDASES FROM PLEUROTUS REMARK 1 TITL 3 ERYNGII AND BJERKANDERA ADUSTA REMARK 1 REF FEBS LETT. V. 428 141 1998 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165 REMARK 1 AUTH M.J.MARTINEZ,F.J.RUIZ-DUENAS,F.GUILLEN,A.T.MARTINEZ REMARK 1 TITL PURIFICATION AND CATALYTIC PROPERTIES OF TWO REMARK 1 TITL 2 MANGANESE PEROXIDASE ISOENZYMES FROM PLEUROTUS REMARK 1 TITL 3 ERYNGII REMARK 1 REF EUR.J.BIOCHEM. V. 237 424 1996 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 0262 999.0000001.0001.0001.00090.0090.0090.00P 1HET HEM 396 44 PROTOPORPHYRIN IX CONTAINS FE(III) HET MN 400 1 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM MN MANGANESE (II) ION HETSYN HEM HEME HELIX 1 A ALA 12 ASN 27 5 16 HELIX 2 B GLU 36 GLY 51 1 16 HELIX 3 B' SER 64 ALA 67 1 4 HELIX 4 B'' ASP 69 GLU 72 1 4 HELIX 5 C ILE 81 HIS 95 1 15 HELIX 6 D ALA 99 ASN 113 1 15 HELIX 7 E VAL 145 ALA 155 1 11 HELIX 8 F PRO 159 ILE 171 1 13 HELIX 9 G SER 195 GLU 200 5 6 HELIX 10 H GLN 229 ARG 236 1 8 HELIX 11 I ALA 241 MET 247 1 7 HELIX 12 J GLN 251 ALA 266 1 16 ID MN DESCR RESID GLU 36 RESID GLU 40 RESID ALA 174 RESID ASP 175 RESID HEM 396 ID CA1 DESCR distal ca-binding site. RESID ASP 48 RESID GLY 60 RESID ASP 62 RESID SER 64 ID CA2 DESCR proximal ca-binding site. RESID SER 170 RESID ASP 187 RESID THR 189 RESID VAL 192 RESID ASP 194 ID HME DESCR characteristic heme pocket residues RESID ARG 43 RESID PHE 46 RESID HIS 47 RESID HIS 169 RESID PHE 186 RESID ASP 231 HEADER PEROXIDASE 13-JAN-98 1A20 TITLE MOLECULAR MODEL FOR A PLEUROTUS ERYNGII PEROXIDASE OXIDIZING TITLE 2 MNII AS WELL AS DIFFERENT PHENOLIC AND NON-PHENOLIC TITLE 3 AROMATIC COMPOUNDS AND DYES, THEORETICAL MODEL COMPND MOL_ID: 1; COMPND 2 MOLECULE: PEROXIDASE; COMPND 3 CHAIN: NULL SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLEUROTUS ERYNGII; SOURCE 3 ORGANISM_COMMON: THISTLE MUSHROOM; SOURCE 4 STRAIN: IJFM A169; SOURCE 5 VARIANT: MNPL1 (ALLELIC); SOURCE 6 COLLECTION: ATCC 90787; SOURCE 7 ORGAN: HETEROKARYOTIC MYCELIUM; SOURCE 8 GENE: MNPL KEYWDS POLYVALENT PEROXIDASE, MANGANESE PEROXIDASE, LIGNIN KEYWDS 2 PEROXIDASE, HOMOLOGY MODELING, MNII-BINDING SITE, KEYWDS 3 AROMATIC-SUBSTRATE BINDING, ELECTRON TRANSFER, ALLELIC KEYWDS 4 VARIANT, LIGNIN DEGRADATION, MNII OXIDATION, MN-INDEPENDENT KEYWDS 5 OXIDATION OF PHENOLIC AND NON-PHENOLIC AROMATICS AND DYES, KEYWDS 6 CLASS II (FUNGAL) PEROXIDASES EXPDTA THEORETICAL MODEL AUTHOR A.T.MARTINEZ,A.ROMERO,F.J.RUIZ-DUENAS,M.J.MARTINEZ REVDAT 1 16-FEB-99 1A20 0 JRNL AUTH F.J.RUIZ-DUENAS,M.J.MARTINEZ,A.T.MARTINEZ JRNL TITL MOLECULAR CHARACTERIZATION OF A NOVEL PEROXIDASE JRNL TITL 2 ISOLATED FROM THE LIGNINOLYTIC FUNGUS PLEUROTUS JRNL TITL 3 ERYNGII JRNL REF MOL.MICROBIOL. V. 31 223 1999 JRNL REFN ASTM MOMIEE UK ISSN 0950-382X 2007 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.HEINFLING,F.J.RUIZ-DUENAS,M.J.MARTINEZ, REMARK 1 AUTH 2 M.BERGBAUER,U.SZEWZYK,A.T.MARTINEZ REMARK 1 TITL A STUDY ON REDUCING SUBSTRATES OF REMARK 1 TITL 2 MANGANESE-OXIDIZING PEROXIDASES FROM PLEUROTUS REMARK 1 TITL 3 ERYNGII AND BJERKANDERA ADUSTA REMARK 1 REF FEBS LETT. V. 428 141 1998 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 0165 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.J.MARTINEZ,F.J.RUIZ-DUENAS,F.GUILLEN,A.T.MARTINEZ REMARK 1 TITL PURIFICATION AND CATALYTIC PROPERTIES OF TWO REMARK 1 TITL 2 MANGANESE PEROXIDASE ISOENZYMES FROM PLEUROTUS REMARK 1 TITL 3 ERYNGII REMARK 1 REF EUR.J.BIOCHEM. V. 237 424 1996 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 0262 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: MOLECULAR DYNAMICS REMARK 4 REMARK 4 1A20 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 220 REMARK 220 EXPERIMENTAL DETAILS REMARK 220 EXPERIMENT TYPE : THEORETICAL MODELLING REMARK 220 REMARK 220 REMARK: REMARK 220 MODELLING PROGRAM: PROMOD REMARK 220 PROGRAM AUTHORS: M.C.PEITSCH REMARK 220 MODELLING EXPERIMENT: - THIS MODEL IS BASED UPON THE REMARK 220 COORDINATES OF 1QPA (X-RAY DIFFRACTION), 1ARP REMARK 220 (X-RAY DIFFRACTION), 1LGA (X-RAY DIFFRACTION), 1MNP REMARK 220 (X-RAY DIFFRACTION) REMARK 220 (FOLLOWED BY CHARMM REFINING, AND MOLECULAR DYNAMICS REMARK 220 REFINING OF PROTEIN PLUS HEM AND MN WITH X-PLOR 3.1) REMARK 225 REMARK 225 THEORETICAL MODEL REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE. REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE REMARK 225 RECORDS ARE MEANINGLESS. REMARK 400 REMARK 400 COMPOUND REMARK 400 THE ENZYME OXIDIZES MN(II) (EC 1.11.1.13), BUT EXHIBITED REMARK 400 ALSO MN-INDEPENDENT PEROXIDASE ACTIVITY ON DYES AND REMARK 400 PHENOLIC (EC 1.11.1.7) AS WELL AS NON-PHENOLIC REMARK 400 (EC 1.11.1.14) AROMATIC SUBSTRATES. REMARK 450 REMARK 450 SOURCE REMARK 450 STRAIN CBS 613.91, TAXONOMIC POSITION: BASIDIOMYCOTA, REMARK 450 HYMENOMYCETES, APHYLLOPHORALES, POLYPORACEAE REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 15 DEGREES (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION REMARK 500 CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 0 GLU 40 OE1 - CD - OE2 ANGL. DEV. = 16.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 4*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 500 NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,A4,A1,2X, REMARK 500 A3,1X,A1,I4,A1,1X,A4,A1,4X,F5.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 0 SER 41 H SER 41 N 0.216 REMARK 500 0 SER 41 HG SER 41 OG 0.265 REMARK 500 0 SER 53 HG SER 53 OG 0.150 REMARK 500 0 ALA 67 H ALA 67 N 0.158 REMARK 500 0 ASN 96 2HD2 ASN 96 ND2 0.158 REMARK 500 0 VAL 118 H VAL 118 N 0.154 REMARK 500 0 ALA 132 H ALA 132 N 0.175 REMARK 500 0 SER 133 HG SER 133 OG 0.151 REMARK 500 0 VAL 162 H VAL 162 N 0.175 REMARK 500 0 THR 201 HG1 THR 201 OG1 0.157 REMARK 500 0 THR 211 HG1 THR 211 OG1 0.153 REMARK 500 0 ILE 276 H ILE 276 N 0.171 REMARK 500 0 ALA 292 H ALA 292 N 0.162 REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: BASED ON DSSP BY KABSCH AND SANDER REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: MN REMARK 800 SITE_DESCRIPTION: MN-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: CA1 REMARK 800 SITE_DESCRIPTION: DISTAL CA-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: CA2 REMARK 800 SITE_DESCRIPTION: PROXIMAL CA-BINDING SITE. REMARK 800 REMARK 800 SITE_IDENTIFIER: HME REMARK 800 SITE_DESCRIPTION: CHARACTERISTIC HEME POCKET RESIDUES REMARK 800 (DISTAL AND PROXIMAL SIDES) REMARK 850 REMARK 850 CORRECTION BEFORE RELEASE REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE REMARK 850 DATE REVISED: 15-JAN-1998 TRACKING NUMBER: T14064 REMARK 999 REMARK 999 GENBANK ENTRY: REMARK 999 AF007223 REMARK 999 DIFFERENCES BETWEEN GENBANK AND PDB: REMARK 999 30 AA SIGNAL-PEPTIDE INCLUDED IN AF007223 REMARK 999 GLY360 AND SER361 OF AF007223 ARE NOT INCLUDED IN PDB DBREF 1A20 1 329 PDB 1A20 1A20 1 329 SEQRES 1 329 ALA THR CYS ALA ASP GLY ARG THR THR ALA ASN ALA ALA SEQRES 2 329 CYS CYS VAL LEU PHE PRO ILE LEU ASP ASP ILE GLN GLU SEQRES 3 329 ASN LEU PHE ASP GLY ALA GLN CYS GLY GLU GLU VAL HIS SEQRES 4 329 GLU SER LEU ARG LEU THR PHE HIS ASP ALA ILE GLY PHE SEQRES 5 329 SER PRO THR LEU GLY GLY GLY GLY ALA ASP GLY SER ILE SEQRES 6 329 ILE ALA PHE ASP THR ILE GLU THR ASN PHE PRO ALA ASN SEQRES 7 329 ALA GLY ILE ASP GLU ILE VAL SER ALA GLN LYS PRO PHE SEQRES 8 329 VAL ALA LYS HIS ASN ILE SER ALA GLY ASP PHE ILE GLN SEQRES 9 329 PHE ALA GLY ALA VAL GLY VAL SER ASN CYS PRO GLY GLY SEQRES 10 329 VAL ARG ILE PRO PHE PHE LEU GLY ARG PRO ASP ALA VAL SEQRES 11 329 ALA ALA SER PRO ASP HIS LEU VAL PRO GLU PRO PHE ASP SEQRES 12 329 SER VAL ASP SER ILE LEU ALA ARG MET SER ASP ALA GLY SEQRES 13 329 PHE SER PRO VAL GLU VAL VAL TRP LEU LEU ALA SER HIS SEQRES 14 329 SER ILE ALA ALA ALA ASP LYS VAL ASP PRO SER ILE PRO SEQRES 15 329 GLY THR PRO PHE ASP SER THR PRO GLY VAL PHE ASP SER SEQRES 16 329 GLN PHE PHE ILE GLU THR GLN LEU LYS GLY ARG LEU PHE SEQRES 17 329 PRO GLY THR ALA ASP ASN LYS GLY GLU ALA GLN SER PRO SEQRES 18 329 LEU GLN GLY GLU ILE ARG LEU GLN SER ASP HIS LEU LEU SEQRES 19 329 ALA ARG ASP PRO GLN THR ALA CYS GLU TRP GLN SER MET SEQRES 20 329 VAL ASN ASN GLN PRO LYS ILE GLN ASN ARG PHE ALA ALA SEQRES 21 329 THR MET SER LYS MET ALA LEU LEU GLY GLN ASP LYS THR SEQRES 22 329 LYS LEU ILE ASP CYS SER ASP VAL ILE PRO THR PRO PRO SEQRES 23 329 ALA LEU VAL GLY ALA ALA HIS LEU PRO ALA GLY PHE SER SEQRES 24 329 LEU SER ASP VAL GLU GLN ALA CYS ALA ALA THR PRO PHE SEQRES 25 329 PRO ALA LEU THR ALA ASP PRO GLY PRO VAL THR SER VAL SEQRES 26 329 PRO PRO VAL PRO HET HEM 396 44 PROTOPORPHYRIN IX CONTAINS FE(III) HET MN 400 1 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM MN MANGANESE (II) ION HETSYN HEM HEME FORMUL 2 HEM C34 H32 N4 O4 FE1 1+ FORMUL 3 MN MN1 2+ HELIX 1 A ALA 12 ASN 27 5 16 HELIX 2 B GLU 36 GLY 51 1 16 HELIX 3 B' SER 64 ALA 67 1 4 HELIX 4 B'' ASP 69 GLU 72 1 4 HELIX 5 C ILE 81 HIS 95 1 15 HELIX 6 D ALA 99 ASN 113 1 15 HELIX 7 E VAL 145 ALA 155 1 11 HELIX 8 F PRO 159 ILE 171 1 13 HELIX 9 G SER 195 GLU 200 5 6 HELIX 10 H GLN 229 ARG 236 1 8 HELIX 11 I ALA 241 MET 247 1 7 HELIX 12 J GLN 251 ALA 266 1 16 SSBOND 1 CYS 3 CYS 15 SSBOND 2 CYS 14 CYS 278 SSBOND 3 CYS 34 CYS 114 SSBOND 4 CYS 242 CYS 307 SITE 1 MN 5 GLU 36 GLU 40 ALA 174 ASP 175 SITE 2 MN 5 HEM 396 SITE 1 CA1 4 ASP 48 GLY 60 ASP 62 SER 64 SITE 1 CA2 5 SER 170 ASP 187 THR 189 VAL 192 SITE 2 CA2 5 ASP 194 SITE 1 HME 6 ARG 43 PHE 46 HIS 47 HIS 169 SITE 2 HME 6 PHE 186 ASP 231 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 ALA 1 24.033 19.016 69.336 1.00 28.33 N