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