HEADER TRANSFERASE(METHYLTRANSFERASE) 05-AUG-93 1HMY COMPND HHAI DNA (CYTOSINE-C5-)-METHYLTRANSFERASE (E.C.2.1.1.37) COMPND 2 COMPLEX WITH S-ADENOSYL-L-METHIONINE SOURCE (HAEMOPHILUS HAEMOLYTICUS) RECOMBINANT FORM EXPRESSED SOURCE 2 IN (ESCHERICHIA COLI) AUTHOR X.CHENG REVDAT 1 31-OCT-93 1HMY 0 JRNL AUTH X.CHENG,S.KUMAR,J.POSFAI,J.W.PFLUGRATH,R.J.ROBERTS JRNL TITL CRYSTAL STRUCTURE OF THE HHAL DNA JRNL TITL 2 METHYLTRANSFERASE COMPLEXED WITH JRNL TITL 3 S-ADENOSYL-L-METHIONINE JRNL REF CELL(CAMBRIDGE,MASS.) V. 74 299 1993 JRNL REFN ASTM CELLB5 US ISSN 0092-8674 998 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.KUMAR,X.CHENG,J.W.PFLUGRATH,R.J.ROBERTS REMARK 1 TITL PURIFICATION, CRYSTALLIZATION, AND PRELIMINARY REMARK 1 TITL 2 X-RAY DIFFRACTION ANALYSIS OF AN M.HHAI-ADOMET REMARK 1 TITL 3 COMPLEX REMARK 1 REF BIOCHEMISTRY V. 31 8648 1992 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 2 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.200 REMARK 3 RMSD BOND DISTANCES 0.012 ANGSTROMS REMARK 3 RMSD BOND ANGLES 1.82 DEGREES REMARK 4 REMARK 4 RAMACHANDRAN PLOT QUALITY ASSESSMENT (BY PROGRAM PROCHECK, REMARK 4 SEE REF. LASKOWSKI, J. APPL. CRYST. 26, 283-291, 1993). REMARK 5 REMARK 5 83 PERCENT OF RESIDUES OCCUR IN MOST FAVORED REGIONS. 17 REMARK 5 PERCENT OF RESIDUES OCCUR IN ADDITIONAL ALLOWED REGIONS. SEQRES 1 327 MET ILE GLU ILE LYS ASP LYS GLN LEU THR GLY LEU ARG SEQRES 2 327 PHE ILE ASP LEU PHE ALA GLY LEU GLY GLY PHE ARG LEU SEQRES 3 327 ALA LEU GLU SER CYS GLY ALA GLU CYS VAL TYR SER ASN SEQRES 4 327 GLU TRP ASP LYS TYR ALA GLN GLU VAL TYR GLU MET ASN SEQRES 5 327 PHE GLY GLU LYS PRO GLU GLY ASP ILE THR GLN VAL ASN SEQRES 6 327 GLU LYS THR ILE PRO ASP HIS ASP ILE LEU CYS ALA GLY SEQRES 7 327 PHE PRO CYS GLN ALA PHE SER ILE SER GLY LYS GLN LYS SEQRES 8 327 GLY PHE GLU ASP SER ARG GLY THR LEU PHE PHE ASP ILE SEQRES 9 327 ALA ARG ILE VAL ARG GLU LYS LYS PRO LYS VAL VAL PHE SEQRES 10 327 MET GLU ASN VAL LYS ASN PHE ALA SER HIS ASP ASN GLY SEQRES 11 327 ASN THR LEU GLU VAL VAL LYS ASN THR MET ASN GLU LEU SEQRES 12 327 ASP TYR SER PHE HIS ALA LYS VAL LEU ASN ALA LEU ASP SEQRES 13 327 TYR GLY ILE PRO GLN LYS ARG GLU ARG ILE TYR MET ILE SEQRES 14 327 CYS PHE ARG ASN ASP LEU ASN ILE GLN ASN PHE GLN PHE SEQRES 15 327 PRO LYS PRO PHE GLU LEU ASN THR PHE VAL LYS ASP LEU SEQRES 16 327 LEU LEU PRO ASP SER GLU VAL GLU HIS LEU VAL ILE ASP SEQRES 17 327 ARG LYS ASP LEU VAL MET THR ASN GLN GLU ILE GLU GLN SEQRES 18 327 THR THR PRO LYS THR VAL ARG LEU GLY ILE VAL GLY LYS SEQRES 19 327 GLY GLY GLN GLY GLU ARG ILE TYR SER THR ARG GLY ILE SEQRES 20 327 ALA ILE THR LEU SER ALA TYR GLY GLY GLY ILE PHE ALA SEQRES 21 327 LYS THR GLY GLY TYR LEU VAL ASN GLY LYS THR ARG LYS SEQRES 22 327 LEU HIS PRO ARG GLU CYS ALA ARG VAL MET GLY TYR PRO SEQRES 23 327 ASP SER TYR LYS VAL HIS PRO SER THR SER GLN ALA TYR SEQRES 24 327 LYS GLN PHE GLY ASN SER VAL VAL ILE ASN VAL LEU GLN SEQRES 25 327 TYR ILE ALA TYR ASN ILE GLY SER SER LEU ASN PHE LYS SEQRES 26 327 PRO TYR FTNOTE 1 FTNOTE 1 CIS PROLINE - PRO 113 FTNOTE 2 FTNOTE 2 RESIDUES 85 - 91 ARE FLEXIBLE WITH HIGH TEMPERATURE FTNOTE 2 FACTORS. HET SAM 328 27 S-ADENOSYLMETHIONINE FORMUL 2 SAM C15 H22 N6 O5 S1 HELIX 1 A GLY 23 CYS 31 1 HELIX 2 B LYS 43 ASN 52 1 HELIX 3 C PHE 101 GLU 110 1 HELIX 4 D ASN 131 LEU 143 1 HELIX 5 E PRO 276 MET 283 1 HELIX 6 F THR 295 ASN 304 1 HELIX 7 G ILE 308 ASN 323 1 HELIX 8 B1 ILE 61 GLN 63 1 3 RESIDUES HELIX 9 B2 GLU 66 THR 68 1 3 RESIDUES HELIX 10 B3 PHE 93 ASP 95 1 3 RESIDUES HELIX 11 C1 PHE 124 SER 126 1 3 RESIDUES HELIX 12 D1 LEU 155 TYR 157 1 3 RESIDUES HELIX 13 D2 VAL 192 LEU 195 1 4 RESIDUES HELIX 14 D3 ASP 199 VAL 202 1 4 RESIDUES SHEET 1 1 6 LEU 12 LEU 17 0 SHEET 2 1 6 ALA 33 GLU 40 1 SHEET 3 1 6 ALA 83 SER 87 1 SHEET 4 1 6 VAL 115 ASN 120 1 SHEET 5 1 6 ARG 163 PHE 171 -1 SHEET 6 1 6 TYR 145 ALA 154 -1 SHEET 1 2 5 VAL 206 LYS 210 0 SHEET 2 2 5 LYS 270 LYS 273 -1 SHEET 3 2 5 GLY 264 VAL 267 -1 SHEET 4 2 5 ARG 240 THR 244 -1 SHEET 5 2 5 LYS 225 VAL 232 -1 CRYST1 55.300 72.700 91.000 90.00 102.50 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 0.018083 0.000000 0.004009 0.00000 SCALE2 0.000000 0.013755 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011256 0.00000