HEADER OXIDOREDUCTASE(OXYGEN ACCEPTOR) 08-JAN-92 1AOZ COMPND ASCORBATE OXIDASE (E.C.1.10.3.3) SOURCE ZUCCHINI (CUCURBITA PEPO MEDULLOSA) AUTHOR A.MESSERSCHMIDT,R.LADENSTEIN,R.HUBER REVDAT 1 31-OCT-93 1AOZ 0 JRNL AUTH A.MESSERSCHMIDT,R.LADENSTEIN,R.HUBER,M.BOLOGNESI, JRNL AUTH 2 L.AVIGLIANO,R.PETRUZZELLI,A.ROSSI,A.FINAZZI-*AGRO JRNL TITL REFINED CRYSTAL STRUCTURE OF ASCORBATE OXIDASE AT JRNL TITL 2 1.9 ANGSTROMS RESOLUTION JRNL REF J.MOL.BIOL. V. 224 179 1992 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.MESSERSCHMIDT,A.ROSSI,R.LADENSTEIN,R.HUBER, REMARK 1 AUTH 2 M.BOLOGNESI,G.GATTI,A.MARCHESINI,R.PETRUZZELLI, REMARK 1 AUTH 3 A.FINAZZI-*AGRO REMARK 1 TITL X-RAY CRYSTAL STRUCTURE OF THE BLUE OXIDASE REMARK 1 TITL 2 ASCORBATE OXIDASE FROM ZUCCHINI. ANALYSIS OF THE REMARK 1 TITL 3 POLYPEPTIDE FOLD AND A MODEL OF THE COPPER SITES REMARK 1 TITL 4 AND LIGANDS REMARK 1 REF J.MOL.BIOL. V. 206 513 1989 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 2 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS REMARK 3 RMSD BOND ANGLES 2.99 DEGREES REMARK 4 REMARK 4 THE NUMBERING SCHEME USED IN THE X-RAY MODEL CORRESPONDS TO REMARK 4 THE AMINO ACID SEQUENCE NUMBERS OF THE ZUCCHINI ASCORBATE REMARK 4 OXIDASE SEQUENCE. SEQRES 1 A 552 SER GLN ILE ARG HIS TYR LYS TRP GLU VAL GLU TYR MET SEQRES 2 A 552 PHE TRP ALA PRO ASN CYS ASN GLU ASN ILE VAL MET GLY SEQRES 3 A 552 ILE ASN GLY GLN PHE PRO GLY PRO THR ILE ARG ALA ASN SEQRES 4 A 552 ALA GLY ASP SER VAL VAL VAL GLU LEU THR ASN LYS LEU SEQRES 5 A 552 HIS THR GLU GLY VAL VAL ILE HIS TRP HIS GLY ILE LEU SEQRES 6 A 552 GLN ARG GLY THR PRO TRP ALA ASP GLY THR ALA SER ILE SEQRES 7 A 552 SER GLN CYS ALA ILE ASN PRO GLY GLU THR PHE PHE TYR SEQRES 8 A 552 ASN PHE THR VAL ASP ASN PRO GLY THR PHE PHE TYR HIS SEQRES 9 A 552 GLY HIS LEU GLY MET GLN ARG SER ALA GLY LEU TYR GLY SEQRES 10 A 552 SER LEU ILE VAL ASP PRO PRO GLN GLY LYS LYS GLU PRO SEQRES 11 A 552 PHE HIS TYR ASP GLY GLU ILE ASN LEU LEU LEU SER ASP SEQRES 12 A 552 TRP TRP HIS GLN SER ILE HIS LYS GLN GLU VAL GLY LEU SEQRES 13 A 552 SER SER LYS PRO ILE ARG TRP ILE GLY GLU PRO GLN THR SEQRES 14 A 552 ILE LEU LEU ASN GLY ARG GLY GLN PHE ASP CYS SER ILE SEQRES 15 A 552 ALA ALA LYS TYR ASP SER ASN LEU GLU PRO CYS LYS LEU SEQRES 16 A 552 LYS GLY SER GLU SER CYS ALA PRO TYR ILE PHE HIS VAL SEQRES 17 A 552 SER PRO LYS LYS THR TYR ARG ILE ARG ILE ALA SER THR SEQRES 18 A 552 THR ALA LEU ALA ALA LEU ASN PHE ALA ILE GLY ASN HIS SEQRES 19 A 552 GLN LEU LEU VAL VAL GLU ALA ASP GLY ASN TYR VAL GLN SEQRES 20 A 552 PRO PHE TYR THR SER ASP ILE ASP ILE TYR SER GLY GLU SEQRES 21 A 552 SER TYR SER VAL LEU ILE THR THR ASP GLN ASN PRO SER SEQRES 22 A 552 GLU ASN TYR TRP VAL SER VAL GLY THR ARG ALA ARG HIS SEQRES 23 A 552 PRO ASN THR PRO PRO GLY LEU THR LEU LEU ASN TYR LEU SEQRES 24 A 552 PRO ASN SER VAL SER LYS LEU PRO THR SER PRO PRO PRO SEQRES 25 A 552 GLN THR PRO ALA TRP ASP ASP PHE ASP ARG SER LYS ASN SEQRES 26 A 552 PHE THR TYR ARG ILE THR ALA ALA MET GLY SER PRO LYS SEQRES 27 A 552 PRO PRO VAL LYS PHE ASN ARG ARG ILE PHE LEU LEU ASN SEQRES 28 A 552 THR GLN ASN VAL ILE ASN GLY TYR VAL LYS TRP ALA ILE SEQRES 29 A 552 ASN ASP VAL SER LEU ALA LEU PRO PRO THR PRO TYR LEU SEQRES 30 A 552 GLY ALA MET LYS TYR ASN LEU LEU HIS ALA PHE ASP GLN SEQRES 31 A 552 ASN PRO PRO PRO GLU VAL PHE PRO GLU ASP TYR ASP ILE SEQRES 32 A 552 ASP THR PRO PRO THR ASN GLU LYS THR ARG ILE GLY ASN SEQRES 33 A 552 GLY VAL TYR GLN PHE LYS ILE GLY GLU VAL VAL ASP VAL SEQRES 34 A 552 ILE LEU GLN ASN ALA ASN MET MET LYS GLU ASN LEU SER SEQRES 35 A 552 GLU THR HIS PRO TRP HIS LEU HIS GLY HIS ASP PHE TRP SEQRES 36 A 552 VAL LEU GLY TYR GLY ASP GLY LYS PHE SER ALA GLU GLU SEQRES 37 A 552 GLU SER SER LEU ASN LEU LYS ASN PRO PRO LEU ARG ASN SEQRES 38 A 552 THR VAL VAL ILE PHE PRO TYR GLY TRP THR ALA ILE ARG SEQRES 39 A 552 PHE VAL ALA ASP ASN PRO GLY VAL TRP ALA PHE HIS CYS SEQRES 40 A 552 HIS ILE GLU PRO HIS LEU HIS MET GLY MET GLY VAL VAL SEQRES 41 A 552 PHE ALA GLU GLY VAL GLU LYS VAL GLY ARG ILE PRO THR SEQRES 42 A 552 LYS ALA LEU ALA CYS GLY GLY THR ALA LYS SER LEU ILE SEQRES 43 A 552 ASN ASN PRO LYS ASN PRO SEQRES 1 B 552 SER GLN ILE ARG HIS TYR LYS TRP GLU VAL GLU TYR MET SEQRES 2 B 552 PHE TRP ALA PRO ASN CYS ASN GLU ASN ILE VAL MET GLY SEQRES 3 B 552 ILE ASN GLY GLN PHE PRO GLY PRO THR ILE ARG ALA ASN SEQRES 4 B 552 ALA GLY ASP SER VAL VAL VAL GLU LEU THR ASN LYS LEU SEQRES 5 B 552 HIS THR GLU GLY VAL VAL ILE HIS TRP HIS GLY ILE LEU SEQRES 6 B 552 GLN ARG GLY THR PRO TRP ALA ASP GLY THR ALA SER ILE SEQRES 7 B 552 SER GLN CYS ALA ILE ASN PRO GLY GLU THR PHE PHE TYR SEQRES 8 B 552 ASN PHE THR VAL ASP ASN PRO GLY THR PHE PHE TYR HIS SEQRES 9 B 552 GLY HIS LEU GLY MET GLN ARG SER ALA GLY LEU TYR GLY SEQRES 10 B 552 SER LEU ILE VAL ASP PRO PRO GLN GLY LYS LYS GLU PRO SEQRES 11 B 552 PHE HIS TYR ASP GLY GLU ILE ASN LEU LEU LEU SER ASP SEQRES 12 B 552 TRP TRP HIS GLN SER ILE HIS LYS GLN GLU VAL GLY LEU SEQRES 13 B 552 SER SER LYS PRO ILE ARG TRP ILE GLY GLU PRO GLN THR SEQRES 14 B 552 ILE LEU LEU ASN GLY ARG GLY GLN PHE ASP CYS SER ILE SEQRES 15 B 552 ALA ALA LYS TYR ASP SER ASN LEU GLU PRO CYS LYS LEU SEQRES 16 B 552 LYS GLY SER GLU SER CYS ALA PRO TYR ILE PHE HIS VAL SEQRES 17 B 552 SER PRO LYS LYS THR TYR ARG ILE ARG ILE ALA SER THR SEQRES 18 B 552 THR ALA LEU ALA ALA LEU ASN PHE ALA ILE GLY ASN HIS SEQRES 19 B 552 GLN LEU LEU VAL VAL GLU ALA ASP GLY ASN TYR VAL GLN SEQRES 20 B 552 PRO PHE TYR THR SER ASP ILE ASP ILE TYR SER GLY GLU SEQRES 21 B 552 SER TYR SER VAL LEU ILE THR THR ASP GLN ASN PRO SER SEQRES 22 B 552 GLU ASN TYR TRP VAL SER VAL GLY THR ARG ALA ARG HIS SEQRES 23 B 552 PRO ASN THR PRO PRO GLY LEU THR LEU LEU ASN TYR LEU SEQRES 24 B 552 PRO ASN SER VAL SER LYS LEU PRO THR SER PRO PRO PRO SEQRES 25 B 552 GLN THR PRO ALA TRP ASP ASP PHE ASP ARG SER LYS ASN SEQRES 26 B 552 PHE THR TYR ARG ILE THR ALA ALA MET GLY SER PRO LYS SEQRES 27 B 552 PRO PRO VAL LYS PHE ASN ARG ARG ILE PHE LEU LEU ASN SEQRES 28 B 552 THR GLN ASN VAL ILE ASN GLY TYR VAL LYS TRP ALA ILE SEQRES 29 B 552 ASN ASP VAL SER LEU ALA LEU PRO PRO THR PRO TYR LEU SEQRES 30 B 552 GLY ALA MET LYS TYR ASN LEU LEU HIS ALA PHE ASP GLN SEQRES 31 B 552 ASN PRO PRO PRO GLU VAL PHE PRO GLU ASP TYR ASP ILE SEQRES 32 B 552 ASP THR PRO PRO THR ASN GLU LYS THR ARG ILE GLY ASN SEQRES 33 B 552 GLY VAL TYR GLN PHE LYS ILE GLY GLU VAL VAL ASP VAL SEQRES 34 B 552 ILE LEU GLN ASN ALA ASN MET MET LYS GLU ASN LEU SER SEQRES 35 B 552 GLU THR HIS PRO TRP HIS LEU HIS GLY HIS ASP PHE TRP SEQRES 36 B 552 VAL LEU GLY TYR GLY ASP GLY LYS PHE SER ALA GLU GLU SEQRES 37 B 552 GLU SER SER LEU ASN LEU LYS ASN PRO PRO LEU ARG ASN SEQRES 38 B 552 THR VAL VAL ILE PHE PRO TYR GLY TRP THR ALA ILE ARG SEQRES 39 B 552 PHE VAL ALA ASP ASN PRO GLY VAL TRP ALA PHE HIS CYS SEQRES 40 B 552 HIS ILE GLU PRO HIS LEU HIS MET GLY MET GLY VAL VAL SEQRES 41 B 552 PHE ALA GLU GLY VAL GLU LYS VAL GLY ARG ILE PRO THR SEQRES 42 B 552 LYS ALA LEU ALA CYS GLY GLY THR ALA LYS SER LEU ILE SEQRES 43 B 552 ASN ASN PRO LYS ASN PRO FTNOTE 1 FTNOTE 1 CIS PROLINE - PRO A 32 FTNOTE 2 FTNOTE 2 CIS PROLINE - PRO A 160 FTNOTE 3 FTNOTE 3 CIS PROLINE - PRO A 300 FTNOTE 4 FTNOTE 4 ASN A 551 - PRO A 552 OMEGA ANGLE = 88.478 FTNOTE 4 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION FTNOTE 5 FTNOTE 5 CIS PROLINE - PRO B 32 FTNOTE 6 FTNOTE 6 CIS PROLINE - PRO B 160 FTNOTE 7 FTNOTE 7 CIS PROLINE - PRO B 300 FTNOTE 8 FTNOTE 8 ASN B 551 - PRO B 552 OMEGA ANGLE = 76.915 FTNOTE 8 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION HET NAG A 601 14 N-ACETYL-D-GLUCOSAMINE HET CU A 701 1 COPPER ++ ION HET C2O A 702 3 CU-O-CU LINKAGE HET C1O A 703 2 CU-O LINKAGE HET NAG B 601 14 N-ACETYL-D-GLUCOSAMINE HET CU B 701 1 COPPER ++ ION HET C2O B 702 3 CU-O-CU LINKAGE HET C1O B 703 2 CU-O LINKAGE HET CU 812 1 COPPER ++ ION FORMUL 3 NAG 2(C8 H15 N1 O6) FORMUL 4 CU 3(CU1 ++) FORMUL 5 C2O 2(O1 CU2) FORMUL 6 C1O 2(O1 CU1) FORMUL 7 HOH *970(H2 O1) SSBOND 1 CYS A 19 CYS A 201 SSBOND 2 CYS A 81 CYS A 538 SSBOND 3 CYS A 180 CYS A 193 SSBOND 4 CYS B 19 CYS B 201 SSBOND 5 CYS B 81 CYS B 538 SSBOND 6 CYS B 180 CYS B 193 CRYST1 106.700 105.100 113.500 90.00 90.00 90.00 P 21 21 2 8 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 0.009372 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009515 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008811 0.00000