HEADER DNA-BINDING REGULATORY PROTEIN 30-AUG-92 1TRO 1TRO 2 COMPND TRP REPRESSOR COMPLEX WITH OPERATOR 1TRO 3 SOURCE TRP REPRESSOR: (ESCHERICHIA COLI, STRAIN W3110); 1TRO 4 SOURCE 2 OPERATOR: SYNTHETIC 1TRO 5 AUTHOR Z.OTWINOWSKI,R.G.ZHANG,P.B.SIGLER 1TRO 6 REVDAT 1 31-JAN-94 1TRO 0 1TRO 7 REMARK 1 1TRO 8 REMARK 1 REFERENCE 1 1TRO 9 REMARK 1 AUTH Z.OTWINOWSKI,R.W.SCHEVITZ,R.-G.ZHANG,C.L.LAWSON, 1TRO 10 REMARK 1 AUTH 2 A.J.JOACHIMIAK,R.MARMORSTEIN,B.F.LUISI,P.B.SIGLER 1TRO 11 REMARK 1 TITL CRYSTAL STRUCTURE OF TRP REPRESSOR OPERATOR 1TRO 12 REMARK 1 TITL 2 COMPLEX AT ATOMIC RESOLUTION 1TRO 13 REMARK 1 REF NATURE V. 335 321 1988 1TRO 14 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1TRO 15 REMARK 1 REFERENCE 2 1TRO 16 REMARK 1 AUTH A.JOACHIMIAK,R.MARMORSTEIN,R.SCHEVITZ,W.MANDECKI, 1TRO 17 REMARK 1 AUTH 2 J.L.FOX,P.B.SIGLER 1TRO 18 REMARK 1 TITL CRYSTAL OF THE TRP REPRESSOR-OPERATOR COMPLEX 1TRO 19 REMARK 1 TITL 2 SUITABLE FOR X-RAY DIFFRACTION ANALYSIS 1TRO 20 REMARK 1 REF J.BIOL.CHEM. V. 262 4917 1987 1TRO 21 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1TRO 22 REMARK 2 1TRO 23 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. 1TRO 24 REMARK 3 1TRO 25 REMARK 3 REFINEMENT. 1TRO 26 REMARK 3 PROGRAM PROLSQ 1TRO 27 REMARK 3 AUTHORS KONNERT,HENDRICKSON 1TRO 28 REMARK 3 R VALUE 0.167 1TRO 29 REMARK 3 RMSD BOND DISTANCES 0.015 ANGSTROMS 1TRO 30 REMARK 3 RMSD BOND ANGLES 1.3 DEGREES 1TRO 31 REMARK 3 1TRO 32 REMARK 3 NUMBER OF PROTEIN ATOMS 4801 1TRO 33 REMARK 3 NUMBER OF SOLVENT ATOMS 572 1TRO 34 REMARK 4 1TRO 35 REMARK 4 FOR THIS ENTRY, ONE SET OF DIFFRACTION DATA FROM A SINGLE 1TRO 36 REMARK 4 CRYSTAL WAS USED, UNLIKE THE STRUCTURE REPORTED IN 1TRO 37 REMARK 4 REFERENCE 1 WHERE AN AVERAGE OF SEVERAL CRYSTAL DATA SETS 1TRO 38 REMARK 4 WERE USED. THE DATA WERE COLLECTED AT THE PHOTON FACTORY 1TRO 39 REMARK 4 ON A IMAGE PLATE DETECTOR. 1TRO 40 REMARK 5 1TRO 41 REMARK 5 THE NON-CRYSTALLOGRAPHIC SYMMETRY OF THE STRUCTURE IS NOT 1TRO 42 REMARK 5 EXACT AND THE DEPARTURES FROM THE NON-CRYSTALLOGRAPHIC 1TRO 43 REMARK 5 FOUR-FOLD SYMMETRY DO NOT SEEM TO BE FUNCTIONALLY 1TRO 44 REMARK 5 SIGNIFICANT. 1TRO 45 REMARK 6 1TRO 46 REMARK 6 THE CRYSTALLOGRAPHIC TEMPERATURE FACTORS OF THE FIRST TWO 1TRO 47 REMARK 6 PROTEIN AND DNA CHAINS ARE LOWER THAN THE SUBSEQUENT TWO; 1TRO 48 REMARK 6 CONSEQUENTLY THE STRUCTURE OF THE FIRST TWO CHAINS IS 1TRO 49 REMARK 6 MORE ACCURATELY DEFINED. 1TRO 50 REMARK 8 1TRO 51 REMARK 8 THE N- AND C-TERMINAL PORTIONS OF THE PROTEIN ARE 1TRO 52 REMARK 8 DISORDERED AND ARE NOT INCLUDED IN THIS ENTRY. THE AMOUNT 1TRO 53 REMARK 8 OF DISORDER OF IS VARIABLE BETWEEN CHAINS. THUS THE ATOMIC 1TRO 54 REMARK 8 COORDINATES OF THE FOUR CHAINS START AND END AT DIFFERENT 1TRO 55 REMARK 8 AMINO ACID RESIDUES. 1TRO 56 REMARK 9 1TRO 57 REMARK 9 TRP REPRESSOR IS A STABLE DIMERIC PROTEIN. ANY ANALYSIS OF 1TRO 58 REMARK 9 OF THIS STRUCTURE REQUIRES THAT A FULL DIMER BE LOOKED AT 1TRO 59 REMARK 9 ONE TIME. THE COORDINATES CONTAIN TWO DIMERS. THE COMPLEX 1TRO 60 REMARK 9 IS MADE BY FOLLOWING CHAIN NUMBERS. 1TRO 61 REMARK 9 COMPLEX 1: A,B,C,D,I,J; COMPLEX 2: E,F,G,H,K,L. 1TRO 62 REMARK 10 1TRO 63 REMARK 10 THE REGULATORY COFACTOR TRYPTOPHAN, ONE PER MONOMER IS 1TRO 64 REMARK 11 1TRO 65 REMARK 11 SEQUENCE ADVISORY NOTICE: 1TRO 66 REMARK 11 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1TRO 67 REMARK 11 1TRO 68 REMARK 11 SWISS-PROT ENTRY NAME: TRPR_ECOLI 1TRO 69 REMARK 11 1TRO 70 REMARK 11 SWISS-PROT RESIDUE PDB SEQRES 1TRO 71 REMARK 11 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1TRO 72 REMARK 11 GLN 14 GLU A 14 1TRO 73 REMARK 11 GLN 14 GLU C 14 1TRO 74 REMARK 11 GLN 14 GLU E 14 1TRO 75 SEQRES 1 A 108 MET ALA GLN GLN SER PRO TYR SER ALA ALA MET ALA GLU 1TRO 76 SEQRES 2 A 108 GLU ARG HIS GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU 1TRO 77 SEQRES 3 A 108 LYS ASN ALA TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU 1TRO 78 SEQRES 4 A 108 ASN LEU MET LEU THR PRO ASP GLU ARG GLU ALA LEU GLY 1TRO 79 SEQRES 5 A 108 THR ARG VAL ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU 1TRO 80 SEQRES 6 A 108 MET SER GLN ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY 1TRO 81 SEQRES 7 A 108 ILE ALA THR ILE THR ARG GLY SER ASN SER LEU LYS ALA 1TRO 82 SEQRES 8 A 108 ALA PRO VAL GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU 1TRO 83 SEQRES 9 A 108 LEU LYS SER ASP 1TRO 84 SEQRES 1 B 1 TRP 1TRO 85 SEQRES 1 C 108 MET ALA GLN GLN SER PRO TYR SER ALA ALA MET ALA GLU 1TRO 86 SEQRES 2 C 108 GLU ARG HIS GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU 1TRO 87 SEQRES 3 C 108 LYS ASN ALA TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU 1TRO 88 SEQRES 4 C 108 ASN LEU MET LEU THR PRO ASP GLU ARG GLU ALA LEU GLY 1TRO 89 SEQRES 5 C 108 THR ARG VAL ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU 1TRO 90 SEQRES 6 C 108 MET SER GLN ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY 1TRO 91 SEQRES 7 C 108 ILE ALA THR ILE THR ARG GLY SER ASN SER LEU LYS ALA 1TRO 92 SEQRES 8 C 108 ALA PRO VAL GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU 1TRO 93 SEQRES 9 C 108 LEU LYS SER ASP 1TRO 94 SEQRES 1 D 1 TRP 1TRO 95 SEQRES 1 E 108 MET ALA GLN GLN SER PRO TYR SER ALA ALA MET ALA GLU 1TRO 96 SEQRES 2 E 108 GLU ARG HIS GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU 1TRO 97 SEQRES 3 E 108 LYS ASN ALA TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU 1TRO 98 SEQRES 4 E 108 ASN LEU MET LEU THR PRO ASP GLU ARG GLU ALA LEU GLY 1TRO 99 SEQRES 5 E 108 THR ARG VAL ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU 1TRO 100 SEQRES 6 E 108 MET SER GLN ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY 1TRO 101 SEQRES 7 E 108 ILE ALA THR ILE THR ARG GLY SER ASN SER LEU LYS ALA 1TRO 102 SEQRES 8 E 108 ALA PRO VAL GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU 1TRO 103 SEQRES 9 E 108 LEU LYS SER ASP 1TRO 104 SEQRES 1 F 1 TRP 1TRO 105 SEQRES 1 G 108 MET ALA GLN GLN SER PRO TYR SER ALA ALA MET ALA GLU 1TRO 106 SEQRES 2 G 108 GLU ARG HIS GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU 1TRO 107 SEQRES 3 G 108 LYS ASN ALA TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU 1TRO 108 SEQRES 4 G 108 ASN LEU MET LEU THR PRO ASP GLU ARG GLU ALA LEU GLY 1TRO 109 SEQRES 5 G 108 THR ARG VAL ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU 1TRO 110 SEQRES 6 G 108 MET SER GLN ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY 1TRO 111 SEQRES 7 G 108 ILE ALA THR ILE THR ARG GLY SER ASN SER LEU LYS ALA 1TRO 112 SEQRES 8 G 108 ALA PRO VAL GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU 1TRO 113 SEQRES 9 G 108 LEU LYS SER ASP 1TRO 114 SEQRES 1 H 1 TRP 1TRO 115 SEQRES 1 I 19 T G T A C T A G T T A A C 1TRO 116 SEQRES 2 I 19 T A G T A C 1TRO 117 SEQRES 1 J 19 T G T A C T A G T T A A C 1TRO 118 SEQRES 2 J 19 T A G T A C 1TRO 119 SEQRES 1 K 19 T G T A C T A G T T A A C 1TRO 120 SEQRES 2 K 19 T A G T A C 1TRO 121 SEQRES 1 L 19 T G T A C T A G T T A A C 1TRO 122 SEQRES 2 L 19 T A G T A C 1TRO 123 FORMUL 13 HOH *572(H2 O1) 1TRO 124 HELIX 1 1A TYR A 7 GLN A 31 1 1TRO 125 HELIX 2 1B HIS A 35 MET A 42 1 1TRO 126 HELIX 3 1C ASP A 46 ARG A 63 1 1TRO 127 HELIX 4 1D GLN A 68 GLU A 74 1 1TRO 128 HELIX 5 1E ILE A 79 ALA A 91 1 1TRO 129 HELIX 6 1F VAL A 94 LEU A 105 1 1TRO 130 HELIX 7 2A ALA C 10 GLN C 31 1 1TRO 131 HELIX 8 2B HIS C 35 MET C 42 1 1TRO 132 HELIX 9 2C ASP C 46 ARG C 63 1 1TRO 133 HELIX 10 2D GLN C 68 GLU C 74 1 1TRO 134 HELIX 11 2E ILE C 79 ALA C 91 1 1TRO 135 HELIX 12 2F VAL C 94 LEU C 105 1 1TRO 136 HELIX 13 3A ARG E 15 GLN E 31 1 1TRO 137 HELIX 14 3B HIS E 35 MET E 42 1 1TRO 138 HELIX 15 3C ASP E 46 ARG E 63 1 1TRO 139 HELIX 16 3D GLN E 68 GLU E 74 1 1TRO 140 HELIX 17 3E ILE E 79 ALA E 91 1 1TRO 141 HELIX 18 3F VAL E 94 LEU E 105 1 1TRO 142 HELIX 19 4A TYR G 7 GLN G 31 1 1TRO 143 HELIX 20 4B HIS G 35 MET G 42 1 1TRO 144 HELIX 21 4C ASP G 46 ARG G 63 1 1TRO 145 HELIX 22 4D GLN G 68 GLU G 74 1 1TRO 146 HELIX 23 4E ILE G 79 ALA G 91 1 1TRO 147 HELIX 24 4F VAL G 94 LEU G 105 1 1TRO 148 CRYST1 43.650 72.430 107.390 90.00 94.96 90.00 P 21 8 1TRO 149 ORIGX1 1.000000 0.000000 0.000000 0.00000 1TRO 150 ORIGX2 0.000000 1.000000 0.000000 0.00000 1TRO 151 ORIGX3 0.000000 0.000000 1.000000 0.00000 1TRO 152 SCALE1 0.022909 0.000000 0.001988 0.00000 1TRO 153 SCALE2 0.000000 0.013806 0.000000 0.00000 1TRO 154 SCALE3 0.000000 0.000000 0.009347 0.00000 1TRO 155