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
Back to Last Page
Go to Homework 3-2
Mail me!