HEADER PRELIMINARY 16-DEC-91 P1APV COMPND ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.7) COMPLEX COMPND 2 WITH A TETRAHEDRAL TRANSITION STATE MIMIC INHIBITOR: COMPND 3 ISOVALERYL (IVA)-VAL-VAL-DIFLUOROSTATONE SOURCE FUNGUS (PENICILLIUM $JANTHINELLUM) AUTHOR A.R.SIELECKI,M.N.G.JAMES REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI,K.HAYAKAWA,M.H.GELB REMARK 1 TITL CRYSTALLOGRAPHIC ANALYSIS OF TRANSITION STATE REMARK 1 TITL 2 MIMICS BOUND TO PENICILLOPEPSIN: DIFLUOROSTATINE- REMARK 1 TITL 3 AND DIFLUOROSTATONE-*CONTAINING PEPTIDES REMARK 1 REF BIOCHEMISTRY V. 31 3872 1992 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI REMARK 1 TITL ASPARTIC PROTEINASES AND THEIR CATALYTIC PATHWAY REMARK 1 EDIT F.A.JURNAK,A.MCPHERSON REMARK 1 REF BIOLOGICAL MACROMOLECULES v. 3 414 1987 REMARK 1 REF 2 AND ASSEMBLIES REMARK 1 PUBL JOHN WILEY and SONS,NEW YORK REMARK 1 REFN US ISBN 0-471-85142-6 879 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI REMARK 1 TITL STEREOCHEMICAL ANALYSIS OF PEPTIDE BOND HYDROLYSIS REMARK 1 TITL 2 CATALYZED BY THE ASPARTIC PROTEINASE REMARK 1 TITL 3 PENICILLOPEPSIN REMARK 1 REF BIOCHEMISTRY V. 24 3701 1985 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 4 REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI,T.HOFMANN REMARK 1 TITL X-RAY DIFFRACTION STUDIES ON PENICILLOPEPSIN AND IT REMARK 1 TITL 2 COMPLEXES: THE HYDROLYTIC MECHANISM REMARK 1 EDIT V.KOSTKA REMARK 1 REF ASPARTIC PROTEINASES AND 163 1985 REMARK 1 REF 2 THEIR INHIBITORS REMARK 1 PUBL WALTER DE GRUYTER & CO.,BERLIN REMARK 1 REFN ISBN 785 REMARK 1 REFERENCE 5 REMARK 1 AUTH T.HOFMANN,R.S.HODGES,M.N.G.JAMES REMARK 1 TITL EFFECT OF $p*H ON THE ACTIVITIES OF PENICILLOPEPSIN REMARK 1 TITL 2 AND RHIZOPUS PEPSIN AND A PROPOSAL FOR THE REMARK 1 TITL 3 PRODUCTIVE SUBSTRATE BINDING MODE IN REMARK 1 TITL 4 PENICILLOPEPSIN REMARK 1 REF BIOCHEMISTRY V. 23 635 1984 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 6 REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI,J.MOULT REMARK 1 TITL CRYSTALLOGRAPHIC ANALYSIS OF A PEPSTATIN ANALOGUE REMARK 1 TITL 2 BINDING TO THE ASPARTYL PROTEINASE PENICILLOPEPSIN REMARK 1 TITL 3 AT 1.8 ANGSTROMS RESOLUTION REMARK 1 REF PEPTIDES: STRUCTURE AND 521 1983 REMARK 1 REF 2 FUNCTION, PROCEEDINGS OF THE REMARK 1 REF 3 OF THE EIGHTH AMERICAN REMARK 1 REF 4 PEPTIDE SYMPOSIUM REMARK 1 REFN ASTM ISBN 0-935940-02-2 817 REMARK 1 REFERENCE 7 REMARK 1 AUTH M.N.G.JAMES,A.R.SIELECKI REMARK 1 TITL STRUCTURE AND REFINEMENT OF PENICILLOPEPSIN AT 1.8 REMARK 1 TITL 2 ANGSTROMS RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 163 299 1983 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 8 REMARK 1 AUTH M.N.G.JAMES,A.SIELECKI,F.SALITURO,D.H.RICH, REMARK 1 AUTH 2 T.HOFMANN REMARK 1 TITL CONFORMATIONAL FLEXIBILITY IN THE ACTIVE SITES OF REMARK 1 TITL 2 ASPARTYL PROTEINASES REVEALED BY A PEPSTATIN REMARK 1 TITL 3 FRAGMENT BINDING TO PENICILLOPEPSIN REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 79 6137 1982 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 REMARK 2 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM PROLSQ REMARK 3 AUTHORS KONNERT,HENDRICKSON REMARK 3 R VALUE 0.131 REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.038 ANGSTROMS 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 UNTIL THIS ENTRY HAS BEEN FULLY PROCESSED, PLEASE CONSULT REMARK 5 PROTEIN DATA BANK ENTRY 3APP FOR FURTHER INFORMATION. SEQRES 1 323 ALA ALA SER GLY VAL ALA THR ASN THR PRO THR ALA ASN SEQRES 2 323 ASP GLU GLU TYR ILE THR PRO VAL THR ILE GLY GLY THR SEQRES 3 323 THR LEU ASN LEU ASN PHE ASP THR GLY SER ALA ASP LEU SEQRES 4 323 TRP VAL PHE SER THR GLU LEU PRO ALA SER GLN GLN SER SEQRES 5 323 GLY HIS SER VAL TYR ASN PRO SER ALA THR GLY LYS GLU SEQRES 6 323 LEU SER GLY TYR THR TRP SER ILE SER TYR GLY ASP GLY SEQRES 7 323 SER SER ALA SER GLY ASN VAL PHE THR ASP SER VAL THR SEQRES 8 323 VAL GLY GLY VAL THR ALA HIS GLY GLN ALA VAL GLN ALA SEQRES 9 323 ALA GLN GLN ILE SER ALA GLN PHE GLN GLN ASP THR ASN SEQRES 10 323 ASN ASP GLY LEU LEU GLY LEU ALA PHE SER SER ILE ASN SEQRES 11 323 THR VAL GLN PRO GLN SER GLN THR THR PHE PHE ASP THR SEQRES 12 323 VAL LYS SER SER LEU ALA GLN PRO LEU PHE ALA VAL ALA SEQRES 13 323 LEU LYS HIS GLN GLN PRO GLY VAL TYR ASP PHE GLY PHE SEQRES 14 323 ILE ASP SER SER LYS TYR THR GLY SER LEU THR TYR THR SEQRES 15 323 GLY VAL ASP ASN SER GLN GLY PHE TRP SER PHE ASN VAL SEQRES 16 323 ASP SER TYR THR ALA GLY SER GLN SER GLY ASP GLY PHE SEQRES 17 323 SER GLY ILE ALA ASP THR GLY THR THR LEU LEU LEU LEU SEQRES 18 323 ASP ASP SER VAL VAL SER GLN TYR TYR SER GLN VAL SER SEQRES 19 323 GLY ALA GLN GLN ASP SER ASN ALA GLY GLY TYR VAL PHE SEQRES 20 323 ASP CYS SER THR ASN LEU PRO ASP PHE SER VAL SER ILE SEQRES 21 323 SER GLY TYR THR ALA THR VAL PRO GLY SER LEU ILE ASN SEQRES 22 323 TYR GLY PRO SER GLY ASP GLY SER THR CYS LEU GLY GLY SEQRES 23 323 ILE GLN SER ASN SER GLY ILE GLY PHE SER ILE PHE GLY SEQRES 24 323 ASP ILE PHE LEU LYS SER GLN TYR VAL VAL PHE ASP SER SEQRES 25 323 ASP GLY PRO GLN LEU GLY PHE ALA PRO GLN ALA FTNOTE 1 FTNOTE 1 RESIDUES PRO 134 AND PRO 315 ARE CIS PROLINES. CRYST1 97.520 46.570 66.230 90.00 116.03 90.00 C 2 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 0.010254 0.000000 0.005008 0.00000 SCALE2 0.000000 0.021473 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016803 0.00000