HEADER PRELIMINARY 18-DEC-92 P1PYA COMPND PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE (L-HISTIDINE COMPND 2 CARBOXYLASE, E.C. 4.1.1.22) SOURCE LACTOBACILLUS_ 30A AUTHOR T.GALLAGHER,D.A.ROZWARSKI,S.R.ERNST,M.L.HACKERT REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.GALLAGHER,D.A.ROZWARSKI,S.R.ERNST,M.L.HACKERT REMARK 1 TITL THE REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT REMARK 1 TITL 2 HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN ASTM 353 REMARK 2 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM XPLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.150 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS REMARK 3 RMSD BOND ANGLE 3.00 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 THE ENZYME IS A HEXAMER OF *AB* SUBUNITS. EACH *AB* REMARK 5 SUBUNIT CONTAINS TWO CHAINS RESULTING FROM AN AUTOCATALYTIC REMARK 5 CLEAVAGE REACTION. THE *B* CHAIN CONTAINS RESIDUES 1 REMARK 5 THROUGH 81, WHILE THE *A* CHAIN IS COMPOSED OF RESIDUES 82 REMARK 5 THROUGH 310. RESIDUE 82 IS AN N-TERMINAL PYRUVOYL GROUP REMARK 5 USED AS A COFACTOR. REMARK 6 REMARK 6 THREE *AB* SUBUNITS (OR TRIMER) ARE RELATED BY A MOLECULAR REMARK 6 THREE-FOLD SYMMETRY AXIS AND CONSTITUTE THE ASYMMETRIC REMARK 6 UNIT. THUS, THESE COORDINATES CONTAIN THREE ACTIVE SITES. REMARK 6 EACH COMPLETE *AB* SUBUNIT CONSISTS OF A *B* CHAIN AND A REMARK 6 PYR COFACTOR LINKED TO THE N TERMINUS OF AN *A* CHAIN. REMARK 7 REMARK 7 TWO TRIMERS RELATED BY A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY REMARK 7 AXIS GENERATE THE HEXAMER. SEQRES 1 A 81 SER GLU LEU ASP ALA LYS LEU ASN LYS LEU GLY VAL ASP SEQRES 2 A 81 ARG ILE ALA ILE SER PRO TYR LYS GLN TRP THR ARG GLY SEQRES 3 A 81 TYR MET GLU PRO GLY ASN ILE GLY ASN GLY TYR VAL THR SEQRES 4 A 81 GLY LEU LYS VAL ASP ALA GLY VAL ARG ASP LYS SER ASP SEQRES 5 A 81 ASP ASP VAL LEU ASP GLY ILE VAL SER TYR ASP ARG ALA SEQRES 6 A 81 GLU THR LYS ASN ALA TYR ILE GLY GLN ILE ASN MET THR SEQRES 7 A 81 THR ALA SER SEQRES 1 B 228 PHE THR GLY VAL GLN GLY ARG VAL ILE GLY TYR ASP ILE SEQRES 2 B 228 LEU ARG SER PRO GLU VAL ASP LYS ALA LYS PRO LEU PHE SEQRES 3 B 228 THR GLU THR GLN TRP ASP GLY SER GLU LEU PRO ILE TYR SEQRES 4 B 228 ASP ALA LYS PRO LEU GLN ASP ALA LEU VAL GLU TYR PHE SEQRES 5 B 228 GLY THR GLU GLN ASP ARG ARG HIS TYR PRO ALA PRO GLY SEQRES 6 B 228 SER PHE ILE VAL CYS ALA ASN LYS GLY VAL THR ALA GLU SEQRES 7 B 228 ARG PRO LYS ASN ASP ALA ASP MET LYS PRO GLY GLN GLY SEQRES 8 B 228 TYR GLY VAL TRP SER ALA ILE ALA ILE SER PHE ALA LYS SEQRES 9 B 228 ASP PRO THR LYS ASP SER SER MET PHE VAL GLU ASP ALA SEQRES 10 B 228 GLY VAL TRP GLU THR PRO ASN GLU ASP GLU LEU LEU GLU SEQRES 11 B 228 TYR LEU GLU GLY ARG ARG LYS ALA MET ALA LYS SER ILE SEQRES 12 B 228 ALA GLU CYS GLY GLN ASP ALA HIS ALA SER PHE GLU SER SEQRES 13 B 228 SER TRP ILE GLY PHE ALA TYR THR MET MET GLU PRO GLY SEQRES 14 B 228 GLN ILE GLY ASN ALA ILE THR VAL ALA PRO TYR VAL SER SEQRES 15 B 228 LEU PRO ILE ASP SER ILE PRO GLY GLY SER ILE LEU THR SEQRES 16 B 228 PRO ASP LYS ASP MET GLU ILE MET GLU ASN LEU THR MET SEQRES 17 B 228 PRO GLU TRP LEU GLU LYS MET GLY TYR LYS SER LEU SER SEQRES 18 B 228 ALA ASN ASN ALA LEU LYS TYR SEQRES 1 C 81 SER GLU LEU ASP ALA LYS LEU ASN LYS LEU GLY VAL ASP SEQRES 2 C 81 ARG ILE ALA ILE SER PRO TYR LYS GLN TRP THR ARG GLY SEQRES 3 C 81 TYR MET GLU PRO GLY ASN ILE GLY ASN GLY TYR VAL THR SEQRES 4 C 81 GLY LEU LYS VAL ASP ALA GLY VAL ARG ASP LYS SER ASP SEQRES 5 C 81 ASP ASP VAL LEU ASP GLY ILE VAL SER TYR ASP ARG ALA SEQRES 6 C 81 GLU THR LYS ASN ALA TYR ILE GLY GLN ILE ASN MET THR SEQRES 7 C 81 THR ALA SER SEQRES 1 D 228 PHE THR GLY VAL GLN GLY ARG VAL ILE GLY TYR ASP ILE SEQRES 2 D 228 LEU ARG SER PRO GLU VAL ASP LYS ALA LYS PRO LEU PHE SEQRES 3 D 228 THR GLU THR GLN TRP ASP GLY SER GLU LEU PRO ILE TYR SEQRES 4 D 228 ASP ALA LYS PRO LEU GLN ASP ALA LEU VAL GLU TYR PHE SEQRES 5 D 228 GLY THR GLU GLN ASP ARG ARG HIS TYR PRO ALA PRO GLY SEQRES 6 D 228 SER PHE ILE VAL CYS ALA ASN LYS GLY VAL THR ALA GLU SEQRES 7 D 228 ARG PRO LYS ASN ASP ALA ASP MET LYS PRO GLY GLN GLY SEQRES 8 D 228 TYR GLY VAL TRP SER ALA ILE ALA ILE SER PHE ALA LYS SEQRES 9 D 228 ASP PRO THR LYS ASP SER SER MET PHE VAL GLU ASP ALA SEQRES 10 D 228 GLY VAL TRP GLU THR PRO ASN GLU ASP GLU LEU LEU GLU SEQRES 11 D 228 TYR LEU GLU GLY ARG ARG LYS ALA MET ALA LYS SER ILE SEQRES 12 D 228 ALA GLU CYS GLY GLN ASP ALA HIS ALA SER PHE GLU SER SEQRES 13 D 228 SER TRP ILE GLY PHE ALA TYR THR MET MET GLU PRO GLY SEQRES 14 D 228 GLN ILE GLY ASN ALA ILE THR VAL ALA PRO TYR VAL SER SEQRES 15 D 228 LEU PRO ILE ASP SER ILE PRO GLY GLY SER ILE LEU THR SEQRES 16 D 228 PRO ASP LYS ASP MET GLU ILE MET GLU ASN LEU THR MET SEQRES 17 D 228 PRO GLU TRP LEU GLU LYS MET GLY TYR LYS SER LEU SER SEQRES 18 D 228 ALA ASN ASN ALA LEU LYS TYR SEQRES 1 E 81 SER GLU LEU ASP ALA LYS LEU ASN LYS LEU GLY VAL ASP SEQRES 2 E 81 ARG ILE ALA ILE SER PRO TYR LYS GLN TRP THR ARG GLY SEQRES 3 E 81 TYR MET GLU PRO GLY ASN ILE GLY ASN GLY TYR VAL THR SEQRES 4 E 81 GLY LEU LYS VAL ASP ALA GLY VAL ARG ASP LYS SER ASP SEQRES 5 E 81 ASP ASP VAL LEU ASP GLY ILE VAL SER TYR ASP ARG ALA SEQRES 6 E 81 GLU THR LYS ASN ALA TYR ILE GLY GLN ILE ASN MET THR SEQRES 7 E 81 THR ALA SER SEQRES 1 F 228 PHE THR GLY VAL GLN GLY ARG VAL ILE GLY TYR ASP ILE SEQRES 2 F 228 LEU ARG SER PRO GLU VAL ASP LYS ALA LYS PRO LEU PHE SEQRES 3 F 228 THR GLU THR GLN TRP ASP GLY SER GLU LEU PRO ILE TYR SEQRES 4 F 228 ASP ALA LYS PRO LEU GLN ASP ALA LEU VAL GLU TYR PHE SEQRES 5 F 228 GLY THR GLU GLN ASP ARG ARG HIS TYR PRO ALA PRO GLY SEQRES 6 F 228 SER PHE ILE VAL CYS ALA ASN LYS GLY VAL THR ALA GLU SEQRES 7 F 228 ARG PRO LYS ASN ASP ALA ASP MET LYS PRO GLY GLN GLY SEQRES 8 F 228 TYR GLY VAL TRP SER ALA ILE ALA ILE SER PHE ALA LYS SEQRES 9 F 228 ASP PRO THR LYS ASP SER SER MET PHE VAL GLU ASP ALA SEQRES 10 F 228 GLY VAL TRP GLU THR PRO ASN GLU ASP GLU LEU LEU GLU SEQRES 11 F 228 TYR LEU GLU GLY ARG ARG LYS ALA MET ALA LYS SER ILE SEQRES 12 F 228 ALA GLU CYS GLY GLN ASP ALA HIS ALA SER PHE GLU SER SEQRES 13 F 228 SER TRP ILE GLY PHE ALA TYR THR MET MET GLU PRO GLY SEQRES 14 F 228 GLN ILE GLY ASN ALA ILE THR VAL ALA PRO TYR VAL SER SEQRES 15 F 228 LEU PRO ILE ASP SER ILE PRO GLY GLY SER ILE LEU THR SEQRES 16 F 228 PRO ASP LYS ASP MET GLU ILE MET GLU ASN LEU THR MET SEQRES 17 F 228 PRO GLU TRP LEU GLU LYS MET GLY TYR LYS SER LEU SER SEQRES 18 F 228 ALA ASN ASN ALA LEU LYS TYR CRYST1 221.700 221.700 107.100 90.00 90.00 90.00 I 41 2 2 48 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 0.004511 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004511 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009337 0.00000