HEADER DNA-BINDING REGULATORY PROTEIN 28-AUG-92 1CMB COMPND MET APO-REPRESSOR (METJ) SOURCE (ESCHERICHIA COLI) AUTHOR J.B.RAFFERTY,K.PHILLIPS,S.E.V.PHILLIPS REVDAT 1 31-OCT-93 1CMB 0 JRNL AUTH J.B.RAFFERTY,W.S.SOMERS,I.SAINT-GIRONS, JRNL AUTH 2 S.E.V.PHILLIPS JRNL TITL THREE DIMENSIONAL CRYSTAL STRUCTURES OF JRNL TITL 2 ESCHERICHIA COLI MET REPRESSOR WITH AND WITHOUT JRNL TITL 3 COREPRESSOR JRNL REF NATURE V. 341 705 1989 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 1 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 0.196 (ALL DATA) REMARK 3 R VALUE 0.186 (FOR F>3SIGMA(F)) REMARK 3 RMSD BOND DISTANCES 0.012 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.040 ANGSTROMS REMARK 3 RMSD PLANES 0.011 ANGSTROMS REMARK 3 B FACTORS 5.7 ANGSTROMS**2 REMARK 4 REMARK 4 THE ASYMMETRIC UNIT IS COMPRISED OF ONE REPRESSOR DIMER REMARK 4 (CHAINS A AND B) WITH APPROXIMATE TWO-FOLD SYMMETRY. REMARK 5 REMARK 5 ONE OF THE FLEXIBLE HAIRPIN LOOPS 12B - 20B IS SEVERELY REMARK 5 DISORDERED. THE CONFORMATION IN THE COORDINATES IS POOR, REMARK 5 BUT PROBABLY APPROXIMATES TO A MAJOR COMPONENT. THE LOOP REMARK 5 IS UNLIKE THE EQUIVALENT ONE (12A - 20A) IN THE FIRST REMARK 5 SUBUNIT. SEQRES 1 A 104 ALA GLU TRP SER GLY GLU TYR ILE SER PRO TYR ALA GLU SEQRES 2 A 104 HIS GLY LYS LYS SER GLU GLN VAL LYS LYS ILE THR VAL SEQRES 3 A 104 SER ILE PRO LEU LYS VAL LEU LYS ILE LEU THR ASP GLU SEQRES 4 A 104 ARG THR ARG ARG GLN VAL ASN ASN LEU ARG HIS ALA THR SEQRES 5 A 104 ASN SER GLU LEU LEU CYS GLU ALA PHE LEU HIS ALA PHE SEQRES 6 A 104 THR GLY GLN PRO LEU PRO ASP ASP ALA ASP LEU ARG LYS SEQRES 7 A 104 GLU ARG SER ASP GLU ILE PRO GLU ALA ALA LYS GLU ILE SEQRES 8 A 104 MET ARG GLU MET GLY ILE ASN PRO GLU THR TRP GLU TYR SEQRES 1 B 104 ALA GLU TRP SER GLY GLU TYR ILE SER PRO TYR ALA GLU SEQRES 2 B 104 HIS GLY LYS LYS SER GLU GLN VAL LYS LYS ILE THR VAL SEQRES 3 B 104 SER ILE PRO LEU LYS VAL LEU LYS ILE LEU THR ASP GLU SEQRES 4 B 104 ARG THR ARG ARG GLN VAL ASN ASN LEU ARG HIS ALA THR SEQRES 5 B 104 ASN SER GLU LEU LEU CYS GLU ALA PHE LEU HIS ALA PHE SEQRES 6 B 104 THR GLY GLN PRO LEU PRO ASP ASP ALA ASP LEU ARG LYS SEQRES 7 B 104 GLU ARG SER ASP GLU ILE PRO GLU ALA ALA LYS GLU ILE SEQRES 8 B 104 MET ARG GLU MET GLY ILE ASN PRO GLU THR TRP GLU TYR HET PO4 1 5 PHOSPHATE GROUP FORMUL 3 PO4 O4 P1 FORMUL 4 HOH *88(H2 O1) HELIX 1 A LEU A 30 VAL A 45 1 HELIX 2 B ASN A 53 THR A 66 1 HELIX 3 C GLU A 86 GLU A 94 1 HELIX 4 A' LEU B 30 VAL B 45 1 HELIX 5 B' ASN B 53 THR B 66 1 HELIX 6 C' GLU B 86 GLU B 94 1 SHEET 1 S1 2 LYS A 22 ILE A 28 -1 SHEET 2 S1 2 LYS B 22 ILE B 28 -1 O ILE B 28 N LYS A 22 TURN 1 TRN HIS A 14 LYS A 17 TYPE II' CRYST1 35.600 62.600 44.500 90.00 102.40 90.00 P 21 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 0.028090 0.000000 0.006176 0.00000 SCALE2 0.000000 0.015974 0.000000 0.00000 SCALE3 0.000000 0.000000 0.023009 0.00000