HEADER PRELIMINARY 21-JUN-91 P1PII COMPND N-(5'PHOSPORIBOSYL)ANTHRANILATE ISOMERASE (E.C.5.3.1.6): COMPND 2 INDOL-3-GLYCEROL-PHOSPHATE SYNTHASE (E.C.4.1.1.8) SOURCE (ESCHERICHIA COLI) AUTHOR M.WILMANNS,J.P.PRIESTLE,J.N.JANSONIUS REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.WILMANNS,J.P.PRIESTLE,T.NIERMANN,J.N.JANSONIUS REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL REMARK 1 TITL 2 ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE REMARK 1 TITL 3 : INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM REMARK 1 TITL 4 ESCHERICHIA $COLI REFINED AT 2.0 ANGSTROMS REMARK 1 TITL 5 RESOLUTION. REMARK 1 REF J.MOL.BIOL. V. 223 477 1992 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.WILMANNS,C.C.HYDE,D.R.DAVIES,K.KIRSCHNER, REMARK 1 AUTH 2 J.N.JANSONIUS REMARK 1 TITL STRUCTURAL CONSERVATION IN PARALLEL REMARK 1 TITL 2 BETA(SLASH)ALPHA-*BARREL ENZYMES THAT CATALYZE REMARK 1 TITL 3 THREE SEQUENTIAL REACTIONS IN THE PATHWAY OF REMARK 1 TITL 4 TRYPTOPHAN BIOSYNTHESIS REMARK 1 REF BIOCHEMISTRY V. 30 9161 1991 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.P.PRIESTLE,M.G.GRUETTER,J.L.WHITE,M.G.VINCENT, REMARK 1 AUTH 2 M.KANIA,E.WILSON,T.S.JARDETSKY,K.KIRSCHNER, REMARK 1 AUTH 3 J.N.JANSONIUS REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL REMARK 1 TITL 2 ENZYME N-(5'-PHOSPHORIBOSYL)ANTHRANILATE REMARK 1 TITL 3 ISOMERASE-INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE FROM REMARK 1 TITL 4 ESCHERICHIA $COLI REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 84 5690 1987 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 REMARK 2 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM TNT REMARK 3 AUTHORS TRONRUD REMARK 3 R VALUE 0.173 REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS REMARK 3 RMSD BOND ANGLE 3.20 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 ********************************************************** REMARK 5 REMARK 5 THIS BIFUNCTIONAL ENZYME CATALYZES TWO SEQUENTIAL STEPS OF REMARK 5 THE TRYPTOPHAN BIOSYNTHETIC PATHWAY. THE TWO ACTIVE SITES REMARK 5 ARE DISTINCT AND NONOVERLAPPING; RESIDUES 1 - 255 REMARK 5 CORRESPOND TO THE INDOLE-3-PHOSPHATE SYNTHASE DOMAIN. REMARK 5 RESIDUES 256 - 452 CORRESPOND TO THE N-(5'PHOSPORIBOSYL) REMARK 5 ANTHRANILATE ISOMERASE DOMAIN. REMARK 6 REMARK 6 NOTE THAT SOME WATERS ARE DISTANT FROM THE PROTEIN AND MAY REMARK 6 BELONG TO A SYMMETRY-RELATED MOLECULE. SEQRES 1 452 MET GLN THR VAL LEU ALA LYS ILE VAL ALA ASP LYS ALA SEQRES 2 452 ILE TRP VAL GLU ALA ARG LYS GLN GLN GLN PRO LEU ALA SEQRES 3 452 SER PHE GLN ASN GLU VAL GLN PRO SER THR ARG HIS PHE SEQRES 4 452 TYR ASP ALA LEU GLN GLY ALA ARG THR ALA PHE ILE LEU SEQRES 5 452 GLU CYS LYS LYS ALA SER PRO SER LYS GLY VAL ILE ARG SEQRES 6 452 ASP ASP PHE ASP PRO ALA ARG ILE ALA ALA ILE TYR LYS SEQRES 7 452 HIS TYR ALA SER ALA ILE SER VAL LEU THR ASP GLU LYS SEQRES 8 452 TYR PHE GLN GLY SER PHE ASN PHE LEU PRO ILE VAL SER SEQRES 9 452 GLN ILE ALA PRO GLN PRO ILE LEU CYS LYS ASP PHE ILE SEQRES 10 452 ILE ASP PRO TYR GLN ILE TYR LEU ALA ARG TYR TYR GLN SEQRES 11 452 ALA ASP ALA CYS LEU LEU MET LEU SER VAL LEU ASP ASP SEQRES 12 452 ASP GLN TYR ARG GLN LEU ALA ALA VAL ALA HIS SER LEU SEQRES 13 452 GLU MET GLY VAL LEU THR GLU VAL SER ASN GLU GLU GLU SEQRES 14 452 GLN GLU ARG ALA ILE ALA LEU GLY ALA LYS VAL VAL GLY SEQRES 15 452 ILE ASN ASN ARG ASP LEU ARG ASP LEU SER ILE ASP LEU SEQRES 16 452 ASN ARG THR ARG GLU LEU ALA PRO LYS LEU GLY HIS ASN SEQRES 17 452 VAL THR VAL ILE SER GLU SER GLY ILE ASN THR TYR ALA SEQRES 18 452 GLN VAL ARG GLU LEU SER HIS PHE ALA ASN GLY PHE LEU SEQRES 19 452 ILE GLY SER ALA LEU MET ALA HIS ASP ASP LEU HIS ALA SEQRES 20 452 ALA VAL ARG ARG VAL LEU LEU GLY GLU ASN LYS VAL CYS SEQRES 21 452 GLY LEU THR ARG GLY GLN ASP ALA LYS ALA ALA TYR ASP SEQRES 22 452 ALA GLY ALA ILE TYR GLY GLY LEU ILE PHE VAL ALA THR SEQRES 23 452 SER PRO ARG CYS VAL ASN VAL GLU GLN ALA GLN GLU VAL SEQRES 24 452 MET ALA ALA ALA PRO LEU GLN TYR VAL GLY VAL PHE ARG SEQRES 25 452 ASN HIS ASP ILE ALA ASP VAL VAL ASP LYS ALA LYS VAL SEQRES 26 452 LEU SER LEU ALA ALA VAL GLN LEU HIS GLY ASN GLU GLU SEQRES 27 452 GLN LEU TYR ILE ASP THR LEU ARG GLU ALA LEU PRO ALA SEQRES 28 452 HIS VAL ALA ILE TRP LYS ALA LEU SER VAL GLY GLU THR SEQRES 29 452 LEU PRO ALA ARG GLU PHE GLN HIS VAL ASP LYS TYR VAL SEQRES 30 452 LEU ASP ASN GLY GLN GLY GLY SER GLY GLN ARG PHE ASP SEQRES 31 452 TRP SER LEU LEU ASN GLY GLN SER LEU GLY ASN VAL LEU SEQRES 32 452 LEU ALA GLY GLY LEU GLY ALA ASP ASN CYS VAL GLU ALA SEQRES 33 452 ALA GLN THR GLY CYS ALA GLY LEU ASP PHE ASN SER ALA SEQRES 34 452 VAL GLU SER GLN PRO GLY ILE LYS ASP ALA ARG LEU LEU SEQRES 35 452 ALA SER VAL PHE GLN THR LEU ARG ALA TYR CRYST1 104.700 104.700 68.000 90.00 90.00 90.00 P 41 4 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 0.009551 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009551 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014706 0.00000