HEADER PRELIMINARY 12-MAR-93 P1GLT COMPND GLUTATHIONE SYNTHASE SOURCE ESCHERICHIA COLI B AUTHOR H.YAMAGUCHI,H.KATO,Y.KATSUBE REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.YAMAGUCHI,H.KATO,Y.HATA,T.NISHIOKA,A.KIMURA,J.ODA, REMARK 1 AUTH 2 Y.KATSUBE REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE GLUTATHIONE REMARK 1 TITL 2 SYNTHETASE FROM ESHERICHIA COLI B AT 2.0A REMARK 1 TITL 3 RESOLUTION. REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN ASTM 353 REMARK 1 REFERENCE 2 REMARK 1 AUTH H.YAMAGUCHI,H.KATO,Y.HATA,T.NISHIOKA,J.ODA, REMARK 1 AUTH 2 Y.KATSUBE REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF REMARK 1 TITL 2 GLUTATHIONE SYNTHETASE FROM ESHERICHIA COLI B. REMARK 1 REF J.MOL.BIOL. V. 209 503 1989 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 3 REMARK 1 AUTH H.KATO,M.KOBAYASHI,K.MURATA,T.NISHIOKA,J.ODA REMARK 1 TITL OVEREXPRESSION OF GLUTATHIONE SYNTHETASE IN REMARK 1 TITL 2 ESHERICHIA COLI. REMARK 1 REF AGRIC.BIOL.CHEM. V. 53 3071 1989 REMARK 1 REFN ASTM ABCHA6 JA ISSN 0002-1369 137 REMARK 1 REFERENCE 4 REMARK 1 AUTH H.KATO,T.TANAKA,T.NISHIOKA,A.KIMURA,J.ODA REMARK 1 TITL ROLE OF CYSTEINE RESIDUES IN GLUTATHIONE SYNTHETASE REMARK 1 TITL 2 FROM ESCHERICIA COLI B:CHEMICAL MODIFICATION AND REMARK 1 TITL 3 OLIGONUCLEOTIDE SITE-DIRECTED MUTAGENESIS. REMARK 1 REF J.BIOL.CHEM. V. 263 11646 1988 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REFERENCE 5 REMARK 1 AUTH H.GUSHIMA,S.YASUDA,E.SOEDA,M.YOKOTA,M.KONDO, REMARK 1 AUTH 2 A.KIMURA REMARK 1 TITL COMPLETE NUCLEOTIDE SEQUENCE OF THE E. COLI REMARK 1 TITL 2 GLUTATHIONE SYNTHETASE GSH-II. REMARK 1 REF NUCLEIC ACIDS RES. V. 12 9299 1984 REMARK 1 REFN ASTM NARHAD UK ISSN 0305-1048 389 REMARK 2 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM PROLSQ REMARK 3 AUTHORS HENDRICKSON AND KONNERT REMARK 3 R VALUE 0.186 REMARK 3 RMSD BOND DISTANCES 0.020 ANGSTROMS REMARK 3 RMSD BOND ANGLE 0.04 DEGREES REMARK 4 REMARK 4 ********************************************************** REMARK 4 * * REMARK 4 * NOTE: * REMARK 4 * THIS IS A "PRE-RELEASE" ENTRY. THE OBJECTIVE OF * REMARK 4 * THE PRE-RELEASE IS TO MAKE PENDING ENTRIES * REMARK 4 * AVAILABLE TO THE SCIENTIFIC COMMUNITY AS SOON AS * REMARK 4 * POSSIBLE. INFORMATION THAT UNIQUELY IDENTIFIES * REMARK 4 * THE COORDINATE SET HAS BEEN PROVIDED. ALL OTHER * REMARK 4 * DETAILS WILL BE PROVIDED WHEN THE STANDARD * REMARK 4 * RELEASE ENTRY BECOMES AVAILABLE. * REMARK 4 * * REMARK 4 * THIS ENTRY MAY NOT FULLY CONFORM TO THE * REMARK 4 * SPECIFICATIONS GIVEN IN THE PROTEIN DATA BANK * REMARK 4 * ATOMIC COORDINATE AND BIBLIOGRAPHIC ENTRY FORMAT * REMARK 4 * DESCRIPTION. * REMARK 4 * * REMARK 4 * RESIDUE AND ATOM NAMES FOR HETEROGENS MAY NOT * REMARK 4 * BE IN THE PROTEIN DATA BANK STANDARD FORMAT. * REMARK 4 * CHANGES TO THESE NAMES MAY THEREFORE OCCUR WHEN * REMARK 4 * THE STANDARD RELEASE ENTRY BECOMES AVAILABLE. * REMARK 4 * * REMARK 4 * THE FOLLOWING CHECKS HAVE BEEN MADE: * REMARK 4 * * REMARK 4 * 1. AMINO ACID SEQUENCE COMPARED TO THE * REMARK 4 * NON-REDUNDANT SEQUENCE DATABASE USING THE * REMARK 4 * GENINFO - GENETIC COMPUTING ENVIRONMENT * REMARK 4 * (NATIONAL CENTER FOR BIOTECHNOLOGY * REMARK 4 * INFORMATION, NATIONAL LIBRARY OF MEDICINE) * REMARK 4 * 2. STEREOCHEMISTRY * REMARK 4 * BOND DISTANCES AND ANGLES * REMARK 4 * DISTORTIONS OF PLANAR GROUPS * REMARK 4 * RAMACHANDRAN PLOT * REMARK 4 * 3. CRYSTAL PACKING * REMARK 4 * * REMARK 4 * A VISUAL CHECK OF THE ENTRY HAS BEEN MADE USING * REMARK 4 * MIDASPLUS (COMPUTER GRAPHICS LABORATORY, * REMARK 4 * UNIVERSITY OF CALIFORNIA, SAN FRANCISCO). * REMARK 4 * * REMARK 4 ********************************************************** SEQRES 1 316 MET ILE LYS LEU GLY ILE VAL MET ASP PRO ILE ALA ASN SEQRES 2 316 ILE ASN ILE LYS LYS ASP SER SER PHE ALA MET LEU LEU SEQRES 3 316 GLU ALA GLN ARG ARG GLY TYR GLU LEU HIS TYR MET GLU SEQRES 4 316 MET GLY ASP LEU TYR LEU ILE ASN GLY GLU ALA ARG ALA SEQRES 5 316 HIS THR ARG THR LEU ASN VAL LYS GLN ASN TYR GLU GLU SEQRES 6 316 TRP PHE SER PHE VAL GLY GLU GLN ASP LEU PRO LEU ALA SEQRES 7 316 ASP LEU ASP VAL ILE LEU MET ARG LYS ASP PRO PRO PHE SEQRES 8 316 ASP THR GLU PHE ILE TYR ALA THR TYR ILE LEU GLU ARG SEQRES 9 316 ALA GLU GLU LYS GLY THR LEU ILE VAL ASN LYS PRO GLN SEQRES 10 316 SER LEU ARG ASP CYS ASN GLU LYS LEU PHE THR ALA TRP SEQRES 11 316 PHE SER ASP LEU THR PRO GLU THR LEU VAL THR ARG ASN SEQRES 12 316 LYS ALA GLN LEU LYS ALA PHE TRP GLU LYS HIS SER ASP SEQRES 13 316 ILE ILE LEU LYS PRO LEU ASP GLY MET GLY GLY ALA SER SEQRES 14 316 ILE PHE ARG VAL LYS GLU GLY ASP PRO ASN LEU GLY VAL SEQRES 15 316 ILE ALA GLU THR LEU THR GLU HIS GLY THR ARG TYR CYS SEQRES 16 316 MET ALA GLN ASN TYR LEU PRO ALA ILE LYS ASP GLY ASP SEQRES 17 316 LYS ARG VAL LEU VAL VAL ASP GLY GLU PRO VAL PRO TYR SEQRES 18 316 CYS LEU ALA ARG ILE PRO GLN GLY GLY GLU THR ARG GLY SEQRES 19 316 ASN LEU ALA ALA GLY GLY ARG GLY GLU PRO ARG PRO LEU SEQRES 20 316 THR GLU SER ASP TRP LYS ILE ALA ARG GLN ILE GLY PRO SEQRES 21 316 THR LEU LYS GLU LYS GLY LEU ILE PHE VAL GLY LEU ASP SEQRES 22 316 ILE ILE GLY ASP ARG LEU THR GLU ILE ASN VAL THR SER SEQRES 23 316 PRO THR CYS ILE ARG GLU ILE GLU ALA GLU PHE PRO VAL SEQRES 24 316 SER ILE THR GLY MET LEU MET ASP ALA ILE GLU ALA ARG SEQRES 25 316 LEU GLN GLN GLN CRYST1 88.000 88.000 164.200 90.00 90.00 120.00 P 62 2 2 12 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 0.011364 0.006561 0.000000 0.00000 SCALE2 0.000000 0.013122 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006090 0.00000