HEADER    TRANSCRIPTION REGULATION                06-MAR-92   1D66      1D66   2
COMPND    GAL4 (RESIDUES 1 - 65) COMPLEX WITH 19MER DNA                 1D66   3
SOURCE    (SACCHAROMYCES $CEREVISIAE) OVEREXPRESSED IN (ESCHERICHIA     1D66   4
SOURCE   2 $COLI)                                                       1D66   5
AUTHOR    R.MARMORSTEIN,S.HARRISON                                      1D66   6
REVDAT   1   15-APR-93 1D66    0                                        1D66   7
JRNL        AUTH   R.MARMORSTEIN,M.CAREY,M.PTASHNE,S.C.HARRISON         1D66   8
JRNL        TITL   /DNA$ RECOGNITION BY /GAL4$: STRUCTURE OF A          1D66   9
JRNL        TITL 2 PROTEIN(SLASH)/DNA$ COMPLEX                          1D66  10
JRNL        REF    NATURE                        V. 356   408 1992      1D66  11
JRNL        REFN   ASTM NATUAS  UK ISSN 0028-0836                  006  1D66  12
REMARK   1                                                              1D66  13
REMARK   2                                                              1D66  14
REMARK   2 RESOLUTION. 2.7  ANGSTROMS.                                  1D66  15
REMARK   3                                                              1D66  16
REMARK   3 REFINEMENT.                                                  1D66  17
REMARK   3   PROGRAM                    CORELS;TNT;XPLOR                1D66  18
REMARK   3   AUTHORS                    J.SUSSMAN;D.TRONRUD;A.BRUNGER   1D66  19
REMARK   3   R VALUE                    0.230                           1D66  20
REMARK   3   RMSD BOND DISTANCES        0.015  ANGSTROMS                1D66  21
REMARK   3   RMSD BOND ANGLES           2.9    DEGREES                  1D66  22
REMARK   4                                                              1D66  23
REMARK   4 THERE ARE TWO DNA CHAINS WHICH HAVE BEEN ASSIGNED CHAIN      1D66  24
REMARK   4 INDICATORS *D* AND *E*.  THERE ARE TWO PROTEIN CHAINS        1D66  25
REMARK   4 WHICH HAVE BEEN ASSIGNED CHAIN INDICATORS *A* AND *B*.       1D66  26
REMARK   4 EACH PROTEIN - DNA COMPLEX CONTAINS FOUR BOUND CD IONS.      1D66  27
REMARK   5                                                              1D66  28
REMARK   5 THE PROTEIN CONTAINS THE N-TERMINAL 65 RESIDUES OF GAL4      1D66  29
REMARK   5 PLUS A C-TERMINAL PHE DERIVED FROM THE CLONING CONSTRUCT.    1D66  30
REMARK   6                                                              1D66  31
REMARK   6 RESIDUES LEU A 19 - LYS A 27 AND LEU B 19 - LYS B 27 FORM    1D66  32
REMARK   6 TIGHT TURNS WHICH CONNECT HELICES.  RESIDUES TRP A 39 -      1D66  33
REMARK   6 LEU A 49 AND TRP B 39 - LEU B 49 FORM EXTENDED CHAINS        1D66  34
REMARK   6 WHICH CONNECT HELICES.                                       1D66  35
REMARK   7                                                              1D66  36
REMARK   7 RESIDUES LYS A 18, ASN A 35, LYS B 18, AND ASN B 35 HAVE     1D66  37
REMARK   7 POSITIVE PHI ANGLES.                                         1D66  38
REMARK   8                                                              1D66  39
REMARK   8 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL   1D66  40
REMARK   8 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO  1D66  41
REMARK   8 CHAIN *A*.                                                   1D66  42
REMARK   9                                                              1D66  43
REMARK   9 THE HYDROGEN BONDS BETWEEN BASE PAIRS IN THIS ENTRY FOLLOW   1D66  44
REMARK   9 THE CONVENTIONAL WATSON-CRICK HYDROGEN BONDING PATTERN.      1D66  45
REMARK   9 THEY HAVE NOT BEEN PRESENTED ON *CONECT* RECORDS IN THIS     1D66  46
REMARK   9 ENTRY.                                                       1D66  47
SEQRES   1 D   19    C   C   G   G   A   G   G   A   C   A   G   T   C  1D66  48
SEQRES   2 D   19    C   T   C   C   G   G                              1D66  49
SEQRES   1 E   19    C   C   G   G   A   G   G   A   C   T   G   T   C  1D66  50
SEQRES   2 E   19    C   T   C   C   G   G                              1D66  51
SEQRES   1 A   66  MET LYS LEU LEU SER SER ILE GLU GLN ALA CYS ASP ILE  1D66  52
SEQRES   2 A   66  CYS ARG LEU LYS LYS LEU LYS CYS SER LYS GLU LYS PRO  1D66  53
SEQRES   3 A   66  LYS CYS ALA LYS CYS LEU LYS ASN ASN TRP GLU CYS ARG  1D66  54
SEQRES   4 A   66  TYR SER PRO LYS THR LYS ARG SER PRO LEU THR ARG ALA  1D66  55
SEQRES   5 A   66  HIS LEU THR GLU VAL GLU SER ARG LEU GLU ARG LEU GLU  1D66  56
SEQRES   6 A   66  PHE                                                  1D66  57
SEQRES   1 B   66  MET LYS LEU LEU SER SER ILE GLU GLN ALA CYS ASP ILE  1D66  58
SEQRES   2 B   66  CYS ARG LEU LYS LYS LEU LYS CYS SER LYS GLU LYS PRO  1D66  59
SEQRES   3 B   66  LYS CYS ALA LYS CYS LEU LYS ASN ASN TRP GLU CYS ARG  1D66  60
SEQRES   4 B   66  TYR SER PRO LYS THR LYS ARG SER PRO LEU THR ARG ALA  1D66  61
SEQRES   5 B   66  HIS LEU THR GLU VAL GLU SER ARG LEU GLU ARG LEU GLU  1D66  62
SEQRES   6 B   66  PHE                                                  1D66  63
FTNOTE   1                                                              1D66  64
FTNOTE   1 RESIDUES PRO A 26 AND PRO B 26 ARE CIS-PROLINES.             1D66  65
HET     CD     39       1     CADMIUM                                   1D66  66
HET     CD     40       1     CADMIUM                                   1D66  67
HET     CD     41       1     CADMIUM                                   1D66  68
HET     CD     42       1     CADMIUM                                   1D66  69
FORMUL   5   CD    4(CD1)                                               1D66  70
FORMUL   6  HOH   *51(H2 O1)                                            1D66  71
HELIX    1 H1A CYS A   11  LYS A   18  1 RESIDUE 18 HAS POSITIVE PHI    1D66  72
HELIX    2 H2A CYS A   28  ASN A   35  1 RESIDUE 35 HAS POSITIVE PHI    1D66  73
HELIX    3 H3A THR A   50  LEU A   64  1                                1D66  74
HELIX    4 H1B CYS B   11  LYS B   18  1 RESIDUE 18 HAS POSITIVE PHI    1D66  75
HELIX    5 H2B CYS B   28  ASN B   35  1 RESIDUE 35 HAS POSITIVE PHI    1D66  76
HELIX    6 H3B THR B   50  LEU B   64  1                                1D66  77
CRYST1   80.850   80.850   73.700  90.00  90.00  90.00 P 43 21 2     8  1D66  78
ORIGX1      1.000000  0.000000  0.000000        0.00000                 1D66  79
ORIGX2      0.000000  1.000000  0.000000        0.00000                 1D66  80
ORIGX3      0.000000  0.000000  1.000000        0.00000                 1D66  81
SCALE1      0.012369  0.000000  0.000000        0.00000                 1D66  82
SCALE2      0.000000  0.012369  0.000000        0.00000                 1D66  83
SCALE3      0.000000  0.000000  0.013569        0.00000                 1D66  84
MTRIX1   1  0.969990  0.014680 -0.242700        7.19246    1            1D66  85
MTRIX2   1  0.014290 -0.999900 -0.003900       83.38941    1            1D66  86
MTRIX3   1 -0.242710 -0.000190 -0.970100       62.87497    1            1D66  87