HEADER PRELIMINARY 14-SEP-92 P1OMP COMPND D-MALTODEXTRIN-BINDING PROTEIN SOURCE (ESCHERICHIA $COLI) AUTHOR A.J.SHARFF,F.A.QUIOCHO REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.J.SHARFF,L.E.RODSETH,J.C.SPURLINO,F.A.QUIOCHO REMARK 1 TITL CRYSTALLOGRAPHIC EVIDENCE OF A LARGE LIGAND-INDUCED REMARK 1 TITL 2 HINGE-TWIST MOTION BETWEEN THE TWO DOMAINS OF THE REMARK 1 TITL 3 MALTODEXTRIN-BINDING PROTEIN INVOLVED IN ACTIVE REMARK 1 TITL 4 TRANSPORT AND CHEMOTAXIS. REMARK 1 REF BIOCHEMISTRY V. 31 10657 1992 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.SPURLINO,F.QUIOCHO,G-Y.LU REMARK 1 TITL THE 2.3 A RESOLUTION STRUCTURE OF THE MALTOSE- OR REMARK 1 TITL 2 MALTODEXTRIN-BINDING PROTEIN,A PRIMARY RECEPTOR OF REMARK 1 TITL 3 BACTERIAL ACTIVE TRANSPORT AND CHEMOTAXIS. REMARK 1 REF J.BIOL.CHEM. V. 266 5202 1991 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 2 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM XPLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.210 REMARK 3 RMSD BOND DISTANCES 0.015 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.031 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 THE DISCREPANCY IN THE SEQUENCE OBTAINED FROM THE SEQUENCE REMARK 5 DATABASE GIVEN BELOW AND THAT OF THE COORDINATES IS DUE TO REMARK 5 POOR ELECTRON DENSITY FOR THE N TERMINAL RESIDUES. THEY REMARK 5 HAVE BEEN DESIGNATED ALA TO ALLOW FITTING. SEQRES 1 366 GLY LYS LEU VAL ILE TRP ILE ASN GLY ASP LYS GLY TYR SEQRES 2 366 ASN GLY LEU ALA GLU VAL GLY LYS LYS PHE GLU LYS ASP SEQRES 3 366 THR GLY ILE LYS VAL THR VAL GLU HIS PRO ASP LYS LEU SEQRES 4 366 GLU GLU LYS PHE PRO GLN VAL ALA ALA THR GLY ASP GLY SEQRES 5 366 PRO ASP ILE ILE PHE TRP ALA HIS ASP ARG PHE GLY GLY SEQRES 6 366 TYR ALA GLN SER GLY LEU LEU ALA GLU ILE THR PRO ASP SEQRES 7 366 LYS ALA PHE GLN ASP LYS LEU TYR PRO PHE THR TRP ASP SEQRES 8 366 ALA VAL ARG TYR ASN GLY LYS LEU ILE ALA TYR PRO ILE SEQRES 9 366 ALA VAL GLU ALA LEU SER LEU ILE TYR ASN LYS ASP LEU SEQRES 10 366 LEU PRO ASN PRO PRO LYS THR TRP GLU GLU ILE PRO ALA SEQRES 11 366 LEU ASP LYS GLU LEU LYS ALA LYS GLY LYS SER ALA LEU SEQRES 12 366 MET PHE ASN LEU GLN GLU PRO TYR PHE THR TRP PRO LEU SEQRES 13 366 ILE ALA ALA ASP GLY GLY TYR ALA PHE LYS TYR GLU ASN SEQRES 14 366 GLY LYS TYR ASP ILE LYS ASP VAL GLY VAL ASP ASN ALA SEQRES 15 366 GLY ALA LYS ALA GLY LEU THR PHE LEU VAL ASP LEU ILE SEQRES 16 366 LYS ASN LYS HIS MET ASN ALA ASP THR ASP TYR SER ILE SEQRES 17 366 ALA GLU ALA ALA PHE ASN LYS GLY GLU THR ALA MET THR SEQRES 18 366 ILE ASN GLY PRO TRP ALA TRP SER ASN ILE ASP THR SER SEQRES 19 366 LYS VAL ASN TYR GLY VAL THR VAL LEU PRO THR PHE LYS SEQRES 20 366 GLY GLN PRO SER LYS PRO PHE VAL GLY VAL LEU SER ALA SEQRES 21 366 GLY ILE ASN ALA ALA SER PRO ASN LYS GLU LEU ALA LYS SEQRES 22 366 GLU PHE LEU GLU ASN TYR LEU LEU THR ASP GLU GLY LEU SEQRES 23 366 GLU ALA VAL ASN LYS ASP LYS PRO LEU GLY ALA VAL ALA SEQRES 24 366 LEU LYS SER TYR GLU GLU GLU LEU ALA LYS ASP PRO ARG SEQRES 25 366 ILE ALA ALA THR MET GLU ASN ALA GLN LYS GLY GLU ILE SEQRES 26 366 MET PRO ASN ILE PRO GLN MET SER ALA PHE TRP TYR ALA SEQRES 27 366 VAL ARG THR ALA VAL ILE ASN ALA ALA SER GLY ARG GLN SEQRES 28 366 THR VAL ASP GLU ALA LEU LYS ASP ALA GLN THR ARG ILE SEQRES 29 366 THR LYS CRYST1 38.350 44.440 58.250 101.00 100.40 104.20 P 1 1 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 0.026076 0.006598 0.006617 0.00000 SCALE2 0.000000 0.023211 0.005905 0.00000 SCALE3 0.000000 0.000000 0.018010 0.00000