HEADER SELF-CLEAVAGE STIMULATION 06-MAR-92 2REB COMPND REC A PROTEIN (E.C.3.4.99.37) SOURCE (ESCHERICHIA COLI) AUTHOR R.M.STORY,T.A.STEITZ REVDAT 1 31-OCT-93 2REB 0 JRNL AUTH R.M.STORY,I.T.WEBER,T.A.STEITZ JRNL TITL THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER JRNL TITL 2 AND POLYMER JRNL REF NATURE V. 355 318 1992 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.M.STORY,T.A.STEITZ REMARK 1 TITL STRUCTURE OF THE RECA PROTEIN-ADP COMPLEX REMARK 1 REF NATURE V. 355 374 1992 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 1 REFERENCE 2 REMARK 1 AUTH R.M.STORY,I.T.WEBER,T.A.STEITZ REMARK 1 TITL THE STRUCTURE OF THE E. $COLI REC*A PROTEIN MONOMER REMARK 1 TITL 2 AND POLYMER: ERRATUM REMARK 1 REF NATURE V. 355 567 1992 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 REMARK 2 REMARK 2 RESOLUTION. 2.3 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REVISION 2.1 REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.210 REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS REMARK 3 RMSD BOND ANGLES 2.6 DEGREES REMARK 4 REMARK 4 THE FOLLOWING RESIDUES LIE IN VERY WEAK ELECTRON DENSITY REMARK 4 AND HAVE NOT BEEN INCLUDED IN THE MODEL: 1 - 2; 157 - 164; REMARK 4 195 - 209; 329 - 352. SEQRES 1 352 ALA ILE ASP GLU ASN LYS GLN LYS ALA LEU ALA ALA ALA SEQRES 2 352 LEU GLY GLN ILE GLU LYS GLN PHE GLY LYS GLY SER ILE SEQRES 3 352 MET ARG LEU GLY GLU ASP ARG SER MET ASP VAL GLU THR SEQRES 4 352 ILE SER THR GLY SER LEU SER LEU ASP ILE ALA LEU GLY SEQRES 5 352 ALA GLY GLY LEU PRO MET GLY ARG ILE VAL GLU ILE TYR SEQRES 6 352 GLY PRO GLU SER SER GLY LYS THR THR LEU THR LEU GLN SEQRES 7 352 VAL ILE ALA ALA ALA GLN ARG GLU GLY LYS THR CYS ALA SEQRES 8 352 PHE ILE ASP ALA GLU HIS ALA LEU ASP PRO ILE TYR ALA SEQRES 9 352 ARG LYS LEU GLY VAL ASP ILE ASP ASN LEU LEU CYS SER SEQRES 10 352 GLN PRO ASP THR GLY GLU GLN ALA LEU GLU ILE CYS ASP SEQRES 11 352 ALA LEU ALA ARG SER GLY ALA VAL ASP VAL ILE VAL VAL SEQRES 12 352 ASP SER VAL ALA ALA LEU THR PRO LYS ALA GLU ILE GLU SEQRES 13 352 GLY GLU ILE GLY ASP SER HIS MET GLY LEU ALA ALA ARG SEQRES 14 352 MET MET SER GLN ALA MET ARG LYS LEU ALA GLY ASN LEU SEQRES 15 352 LYS GLN SER ASN THR LEU LEU ILE PHE ILE ASN GLN ILE SEQRES 16 352 ARG MET LYS ILE GLY VAL MET PHE GLY ASN PRO GLU THR SEQRES 17 352 THR THR GLY GLY ASN ALA LEU LYS PHE TYR ALA SER VAL SEQRES 18 352 ARG LEU ASP ILE ARG ARG ILE GLY ALA VAL LYS GLU GLY SEQRES 19 352 GLU ASN VAL VAL GLY SER GLU THR ARG VAL LYS VAL VAL SEQRES 20 352 LYS ASN LYS ILE ALA ALA PRO PHE LYS GLN ALA GLU PHE SEQRES 21 352 GLN ILE LEU TYR GLY GLU GLY ILE ASN PHE TYR GLY GLU SEQRES 22 352 LEU VAL ASP LEU GLY VAL LYS GLU LYS LEU ILE GLU LYS SEQRES 23 352 ALA GLY ALA TRP TYR SER TYR LYS GLY GLU LYS ILE GLY SEQRES 24 352 GLN GLY LYS ALA ASN ALA THR ALA TRP LEU LYS ASP ASN SEQRES 25 352 PRO GLU THR ALA LYS GLU ILE GLU LYS LYS VAL ARG GLU SEQRES 26 352 LEU LEU LEU SER ASN PRO ASN SER THR PRO ASP PHE SER SEQRES 27 352 VAL ASP ASP SER GLU GLY VAL ALA GLU THR ASN GLU ASP SEQRES 28 352 PHE FTNOTE 1 FTNOTE 1 THE PEPTIDE BOND BETWEEN ASP 144 AND SER 145 HAS BEEN BUILT FTNOTE 1 IN THE CIS CONFORMATION. FORMUL 2 HOH *136(H2 O1) CRYST1 102.400 102.400 82.700 90.00 90.00 120.00 P 61 6 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 0.009766 0.005638 0.000000 0.00000 SCALE2 0.000000 0.011276 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012092 0.00000