HEADER PRELIMINARY 15-JUL-92 P1LTS COMPND HEAT-LABILE ENTEROTOXIN (LT); CHOLERA-LIKE TOXIN, AB5 TOXIN SOURCE PORCINE ESCHERICHIA COLI (PLASMID EWD299) AUTHOR T.K.SIXMA,W.G.J.HOL REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.K.SIXMA,B.A.M.$VAN *ZANTEN,Z.DAUTER,W.G.J.HOL REMARK 1 TITL THE REFINED STRUCTURE OF E. COLI HEAT LABILE REMARK 1 TITL 2 ENTEROTOXIN, A CLOSE RELATIVE OF CHOLERA TOXIN REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN ASTM 353 REMARK 1 REFERENCE 2 REMARK 1 AUTH T.K.SIXMA,S.E.PRONK,K.H.KALK,B.A.M.$VAN *ZANTEN, REMARK 1 AUTH 2 A.M.BERGHUIS,W.G.J.HOL REMARK 1 TITL LACTOSE BINDING TO HEAT-LABILE ENTEROTOXIN REMARK 1 TITL 2 REVEALED BY X-RAY CRYSTALLOGRAPHY REMARK 1 REF NATURE V. 355 561 1992 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 1 REFERENCE 3 REMARK 1 AUTH T.K.SIXMA,S.E.PRONK,K.H.KALK,E.S.WARTNA, REMARK 1 AUTH 2 B.A.M.$VAN *ZANTEN,B.WITHOLT,W.G.J.HOL REMARK 1 TITL CRYSTAL STRUCTURE OF A CHOLERA TOXIN-RELATED REMARK 1 TITL 2 HEAT-LABILE ENTEROTOXIN FROM E. COLI REMARK 1 REF NATURE V. 351 371 1991 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 1 REFERENCE 4 REMARK 1 AUTH T.K.SIXMA,S.E.PRONK,A.C.TERWISSCHA VAN *SCHELTINGA, REMARK 1 AUTH 2 A.AGUIRRE,K.H.KALK,G.VRIEND,W.G.J.HOL REMARK 1 TITL NATIVE NON-ISOMORPHISM IN THE STRUCTURE REMARK 1 TITL 2 DETERMINATION OF HEAT LABILE ENTEROTOXIN (/LT$) REMARK 1 TITL 3 FROM E. COLI REMARK 1 EDIT W.WOLF,P.R.EVANS,A.G.W.LESLIE REMARK 1 REF PROCEEDINGS CCP4 STUDY 133 1991 REMARK 1 REF 2 WEEKEND: ISOMORPHOUS REMARK 1 REF 3 REPLACEMENT AND ANOMALOUS REMARK 1 REF 4 SCATTERING REMARK 1 PUBL DARESBURY LABORATORY, ENGLAND REMARK 1 REFN 784 REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.182 REMARK 3 RMSD BOND DISTANCES 0.015 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 COORDINATES WERE OMITTED, BECAUSE OF POOR DENSITY, FOR REMARK 5 REGIONS: N-TERMINUS OF A SUBUNIT A:1-3; TRANSITION FROM A1 REMARK 5 TO A2 A:189 - C:195; C-TERMINUS OF A2 FRAGMENT OF A SUBUNIT REMARK 5 C:237-240. REMARK 6 WEAK DENSITY IN LOOPS OF B SUBUNITS: D:53-59, E:53-59, REMARK 6 F:53-59, G:53-59, H:53-59 REMARK 6 WEAK DENSITY IN SEVERAL LOOPS OF A1: A:33-38, A:79-80, REMARK 6 A:110, A:137-138. REMARK 7 REMARK 7 THE QUANTITY Z PRESENTED IN COLUMNS 79 - 80 OF THE CRYST1 REMARK 7 RECORD IS DEFINED AS BEING THE NUMBER OF TIMES THE SAME REMARK 7 POLYMERIC CHAIN IS CONTAINED IN THE CELL. IN THIS REMARK 7 STRUCTURE THERE ARE FOUR COPIES OF THE MOLECULE IN THE REMARK 7 CELL. THUS ONE WOULD EXPECT Z TO HAVE THE VALUE 4 IN THIS REMARK 7 ENTRY. HOWEVER, THERE ARE FIVE IDENTICAL CHAINS (CHAINS REMARK 7 D, E, F, G, AND H) IN THE UNIT CELL PLUS CHAINS A AND C REMARK 7 THAT ARE DIFFERENT. PROTEIN DATA BANK SPECIFICATIONS REMARK 7 SPECIFY THAT IN THE CASE OF DIFFERENT NUMBERS OF DIFFERENT REMARK 7 CHAINS PER CELL, Z WILL DENOTE THE NUMBER OF THE MOST REMARK 7 POPULOUS SPECIES PER CELL. THUS Z IS GIVEN AS 20 ON THE REMARK 7 CRYST1 RECORD BELOW. SEQRES 1 D 103 ALA PRO GLN THR ILE THR GLU LEU CYS SER GLU TYR ARG SEQRES 2 D 103 ASN THR GLN ILE TYR THR ILE ASN ASP LYS ILE LEU SER SEQRES 3 D 103 TYR THR GLU SER MET ALA GLY LYS ARG GLU MET VAL ILE SEQRES 4 D 103 ILE THR PHE LYS SER GLY GLU THR PHE GLN VAL GLU VAL SEQRES 5 D 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE SEQRES 6 D 103 GLU ARG MET LYS ASP THR LEU ARG ILE THR TYR LEU THR SEQRES 7 D 103 GLU THR LYS ILE ASP LYS LEU CYS VAL TRP ASN ASN LYS SEQRES 8 D 103 THR PRO ASN SER ILE ALA ALA ILE SER MET LYS ASN SEQRES 1 E 103 ALA PRO GLN THR ILE THR GLU LEU CYS SER GLU TYR ARG SEQRES 2 E 103 ASN THR GLN ILE TYR THR ILE ASN ASP LYS ILE LEU SER SEQRES 3 E 103 TYR THR GLU SER MET ALA GLY LYS ARG GLU MET VAL ILE SEQRES 4 E 103 ILE THR PHE LYS SER GLY GLU THR PHE GLN VAL GLU VAL SEQRES 5 E 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE SEQRES 6 E 103 GLU ARG MET LYS ASP THR LEU ARG ILE THR TYR LEU THR SEQRES 7 E 103 GLU THR LYS ILE ASP LYS LEU CYS VAL TRP ASN ASN LYS SEQRES 8 E 103 THR PRO ASN SER ILE ALA ALA ILE SER MET LYS ASN SEQRES 1 F 103 ALA PRO GLN THR ILE THR GLU LEU CYS SER GLU TYR ARG SEQRES 2 F 103 ASN THR GLN ILE TYR THR ILE ASN ASP LYS ILE LEU SER SEQRES 3 F 103 TYR THR GLU SER MET ALA GLY LYS ARG GLU MET VAL ILE SEQRES 4 F 103 ILE THR PHE LYS SER GLY GLU THR PHE GLN VAL GLU VAL SEQRES 5 F 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE SEQRES 6 F 103 GLU ARG MET LYS ASP THR LEU ARG ILE THR TYR LEU THR SEQRES 7 F 103 GLU THR LYS ILE ASP LYS LEU CYS VAL TRP ASN ASN LYS SEQRES 8 F 103 THR PRO ASN SER ILE ALA ALA ILE SER MET LYS ASN SEQRES 1 G 103 ALA PRO GLN THR ILE THR GLU LEU CYS SER GLU TYR ARG SEQRES 2 G 103 ASN THR GLN ILE TYR THR ILE ASN ASP LYS ILE LEU SER SEQRES 3 G 103 TYR THR GLU SER MET ALA GLY LYS ARG GLU MET VAL ILE SEQRES 4 G 103 ILE THR PHE LYS SER GLY GLU THR PHE GLN VAL GLU VAL SEQRES 5 G 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE SEQRES 6 G 103 GLU ARG MET LYS ASP THR LEU ARG ILE THR TYR LEU THR SEQRES 7 G 103 GLU THR LYS ILE ASP LYS LEU CYS VAL TRP ASN ASN LYS SEQRES 8 G 103 THR PRO ASN SER ILE ALA ALA ILE SER MET LYS ASN SEQRES 1 H 103 ALA PRO GLN THR ILE THR GLU LEU CYS SER GLU TYR ARG SEQRES 2 H 103 ASN THR GLN ILE TYR THR ILE ASN ASP LYS ILE LEU SER SEQRES 3 H 103 TYR THR GLU SER MET ALA GLY LYS ARG GLU MET VAL ILE SEQRES 4 H 103 ILE THR PHE LYS SER GLY GLU THR PHE GLN VAL GLU VAL SEQRES 5 H 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE SEQRES 6 H 103 GLU ARG MET LYS ASP THR LEU ARG ILE THR TYR LEU THR SEQRES 7 H 103 GLU THR LYS ILE ASP LYS LEU CYS VAL TRP ASN ASN LYS SEQRES 8 H 103 THR PRO ASN SER ILE ALA ALA ILE SER MET LYS ASN SEQRES 1 A 185 ARG LEU TYR ARG ALA ASP SER ARG PRO PRO ASP GLU ILE SEQRES 2 A 185 LYS ARG SER GLY GLY LEU MET PRO ARG GLY HIS ASN GLU SEQRES 3 A 185 TYR PHE ASP ARG GLY THR GLN MET ASN ILE ASN LEU TYR SEQRES 4 A 185 ASP HIS ALA ARG GLY THR GLN THR GLY PHE VAL ARG TYR SEQRES 5 A 185 ASP ASP GLY TYR VAL SER THR SER LEU SER LEU ARG SER SEQRES 6 A 185 ALA HIS LEU ALA GLY GLN SER ILE LEU SER GLY TYR SER SEQRES 7 A 185 THR TYR TYR ILE TYR VAL ILE ALA THR ALA PRO ASN MET SEQRES 8 A 185 PHE ASN VAL ASN ASP VAL LEU GLY VAL TYR SER PRO HIS SEQRES 9 A 185 PRO TYR GLU GLN GLU VAL SER ALA LEU GLY GLY ILE PRO SEQRES 10 A 185 TYR SER GLN ILE TYR GLY TRP TYR ARG VAL ASN PHE GLY SEQRES 11 A 185 VAL ILE ASP GLU ARG LEU HIS ARG ASN ARG GLU TYR ARG SEQRES 12 A 185 ASP ARG TYR TYR ARG ASN LEU ASN ILE ALA PRO ALA GLU SEQRES 13 A 185 ASP GLY TYR ARG LEU ALA GLY PHE PRO PRO ASP HIS GLN SEQRES 14 A 185 ALA TRP ARG GLU GLU PRO TRP ILE HIS HIS ALA PRO GLN SEQRES 15 A 185 GLY CYS GLY SEQRES 1 C 41 GLY ASP THR CYS ASN GLU GLU THR GLN ASN LEU SER THR SEQRES 2 C 41 ILE TYR LEU ARG GLU TYR GLN SER LYS VAL LYS ARG GLN SEQRES 3 C 41 ILE PHE SER ASP TYR GLN SER GLU VAL ASP ILE TYR ASN SEQRES 4 C 41 ARG ILE FTNOTE 1 FTNOTE 1 RESIDUE 93 IN ALL FIVE B SUBUNITS AND 178 OF A SUBUNIT FTNOTE 1 ARE CIS PROLINES. CRYST1 119.200 98.200 64.800 90.00 90.00 90.00 P 21 21 21 20 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 0.008389 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010183 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015432 0.00000