HEADER TRANSCRIPTION REGULATION 02-APR-91 1ROP 1ROP 2 COMPND ROP: COL*E1 REPRESSOR OF PRIMER 1ROP 3 SOURCE (ESCHERICHIA $COLI) K14 1ROP 4 AUTHOR M.KOKKINIDIS,D.W.BANNER,D.TSERNOGLOU 1ROP 5 REVDAT 1 15-JUL-92 1ROP 0 1ROP 6 JRNL AUTH D.W.BANNER,M.KOKKINIDIS,D.TSERNOGLOU 1ROP 7 JRNL TITL STRUCTURE OF THE COL*E1 ROP PROTEIN AT 1.7 1ROP 8 JRNL TITL 2 ANGSTROMS RESOLUTION 1ROP 9 JRNL REF J.MOL.BIOL. V. 196 657 1987 1ROP 10 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1ROP 11 REMARK 1 1ROP 12 REMARK 1 REFERENCE 1 1ROP 13 REMARK 1 AUTH D.W.BANNER,G.CESARENI,D.TSERNOGLOU 1ROP 14 REMARK 1 TITL CRYSTALLIZATION OF THE COL*E1 ROP PROTEIN 1ROP 15 REMARK 1 REF J.MOL.BIOL. V. 170 1059 1983 1ROP 16 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1ROP 17 REMARK 2 1ROP 18 REMARK 2 RESOLUTION. 1.7 ANGSTROMS. 1ROP 19 REMARK 3 1ROP 20 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST-SQUARES PROCEDURE OF J. 1ROP 21 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 1ROP 22 REMARK 3 VALUE IS 0.182 FOR 6725 REFLECTIONS IN THE RESOLUTION 1ROP 23 REMARK 3 RANGE 5.0 TO 1.7 ANGSTROMS. 1ROP 24 REMARK 3 1ROP 25 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1ROP 26 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1ROP 27 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1ROP 28 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1ROP 29 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1ROP 30 REMARK 3 BOND DISTANCE 0.029(0.015) 1ROP 31 REMARK 3 ANGLE DISTANCE 0.034(0.020) 1ROP 32 REMARK 3 PLANAR 1-4 DISTANCE 0.053(0.030) 1ROP 33 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.017(0.020) 1ROP 34 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.243(0.150) 1ROP 35 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1ROP 36 REMARK 3 SINGLE TORSION CONTACT 0.18(0.500) 1ROP 37 REMARK 3 MULTIPLE TORSION CONTACT 0.24(0.500) 1ROP 38 REMARK 3 POSSIBLE HYDROGEN BOND 0.22(0.500) 1ROP 39 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1ROP 40 REMARK 3 PLANAR (OMEGA) 4.2(3.0) 1ROP 41 REMARK 3 STAGGERED 16.7(15.0) 1ROP 42 REMARK 3 ORTHONORMAL 44.7(20.0) 1ROP 43 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1ROP 44 REMARK 3 MAIN-CHAIN BOND 1.76(1.000) 1ROP 45 REMARK 3 MAIN-CHAIN ANGLE 2.36(1.500) 1ROP 46 REMARK 3 SIDE-CHAIN BOND 3.07(1.000) 1ROP 47 REMARK 3 SIDE-CHAIN ANGLE 4.7(1.500) 1ROP 48 REMARK 4 1ROP 49 REMARK 4 THE COMPLETE ROP MOLECULE IS AN EXACT CRYSTALLOGRAPHIC 1ROP 50 REMARK 4 DIMER WHICH FORMS A HIGHLY REGULAR 4-ALPHA-HELIX BUNDLE. 1ROP 51 REMARK 4 THE SECOND MONOMER MAY BE OBTAINED FROM THE COORDINATES IN 1ROP 52 REMARK 4 THIS ENTRY BY APPLICATION OF THE CRYSTALLOGRAPHIC 1ROP 53 REMARK 4 TWO-FOLD AXIS IN SPACE GROUP C2. 1ROP 54 REMARK 5 1ROP 55 REMARK 5 THE SEVEN C-TERMINAL RESIDUES ARE DISORDERED AND WERE 1ROP 56 REMARK 5 INVISIBLE ON ELECTRON DENSITY MAPS. THREE SIDE CHAINS PER 1ROP 57 REMARK 5 MONOMER ARE INCOMPLETE DUE TO DISORDER EFFECTS: LYS 3, 1ROP 58 REMARK 5 LYS 6 AND MET 11. 1ROP 59 REMARK 6 1ROP 60 REMARK 6 THERE IS A VERY TIGHT BEND (RESIDUES ASP 30 AND ALA 31) IN 1ROP 61 REMARK 6 EACH MONOMER. IT IS NOT LISTED ON A *TURN* RECORD BECAUSE 1ROP 62 REMARK 6 EACH RESIDUE IS INTEGRATED IN THE HYDROGEN BONDING NETWORK 1ROP 63 REMARK 6 OF HELICES H1 AND H2. 1ROP 64 SEQRES 1 A 63 MET THR LYS GLN GLU LYS THR ALA LEU ASN MET ALA ARG 1ROP 65 SEQRES 2 A 63 PHE ILE ARG SER GLN THR LEU THR LEU LEU GLU LYS LEU 1ROP 66 SEQRES 3 A 63 ASN GLU LEU ASP ALA ASP GLU GLN ALA ASP ILE CYS GLU 1ROP 67 SEQRES 4 A 63 SER LEU HIS ASP HIS ALA ASP GLU LEU TYR ARG SER CYS 1ROP 68 SEQRES 5 A 63 LEU ALA ARG PHE GLY ASP ASP GLY GLU ASN LEU 1ROP 69 FORMUL 2 HOH *48(H2 O1) 1ROP 70 HELIX 1 H1 THR A 2 ASP A 30 1 27,28,29,30 MIXED ALPHA-3/10 1ROP 71 HELIX 2 H2 ALA A 31 PHE A 56 1 1ROP 72 CRYST1 60.380 40.390 27.730 90.00 105.77 90.00 C 2 4 1ROP 73 ORIGX1 1.000000 0.000000 0.000000 0.00000 1ROP 74 ORIGX2 0.000000 1.000000 0.000000 0.00000 1ROP 75 ORIGX3 0.000000 0.000000 1.000000 0.00000 1ROP 76 SCALE1 0.016562 0.000000 0.004677 0.00000 1ROP 77 SCALE2 0.000000 0.024759 0.000000 0.00000 1ROP 78 SCALE3 0.000000 0.000000 0.037472 0.00000 1ROP 79