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HEADER ENTEROTOXIN 13-JUN-95 1EHS TITLE THE STRUCTURE OF ESCHERICHIA COLI HEAT-STABLE ENTEROTOXIN B TITLE 2 BY NUCLEAR MAGNETIC RESONANCE AND CIRCULAR DICHROISM COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAT-STABLE ENTEROTOXIN B; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: STB; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 STRAIN: K12/711; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PPD21K KEYWDS HEAT-STABLE, ENTEROTOXIN, DISULFIDE EXPDTA NMR AUTHOR M.SUKUMAR,J.RIZO,M.WALL,L.A.DREYFUS,Y.M.KUPERSZTOCH, AUTHOR 2 L.M.GIERASCH REVDAT 1 15-SEP-95 1EHS 0 JRNL AUTH M.SUKUMAR,J.RIZO,M.WALL,L.A.DREYFUS, JRNL AUTH 2 Y.M.KUPERSZTOCH,L.M.GIERASCH JRNL TITL THE STRUCTURE OF ESCHERICHIA COLI HEAT-STABLE JRNL TITL 2 ENTEROTOXIN B BY NUCLEAR MAGNETIC RESONANCE AND JRNL TITL 3 CIRCULAR DICHROISM. JRNL REF PROTEIN SCI. V. 4 1718 1995 JRNL REFN ASTM PRCIEI US ISSN 0961-8368 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DGII REMARK 3 AUTHORS : BIOSYM TECHNOLOGIES REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1EHS COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-16) REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : NULL REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 9 -53.75 138.76 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASP A 8 LEU A 9 -140.91 REMARK 500 CYS A 10 GLU A 11 149.97 REMARK 500 ASP A 30 GLY A 31 115.37 DBREF 1EHS A 1 48 UNP P22542 HSTI_ECOLI 24 71 SEQRES 1 A 48 SER THR GLN SER ASN LYS LYS ASP LEU CYS GLU HIS TYR SEQRES 2 A 48 ARG GLN ILE ALA LYS GLU SER CYS LYS LYS GLY PHE LEU SEQRES 3 A 48 GLY VAL ARG ASP GLY THR ALA GLY ALA CYS PHE GLY ALA SEQRES 4 A 48 GLN ILE MET VAL ALA ALA LYS GLY CYS HELIX 1 1 HIS A 12 LYS A 22 1 11 HELIX 2 2 GLN A 40 ALA A 45 1 6 SSBOND 1 CYS A 10 CYS A 48 SSBOND 2 CYS A 21 CYS A 36 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000