BMRB Entry 5180

Title:
Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106)
Deposition date:
2001-10-16
Original release date:
2001-11-12
Authors:
Hidalgo, P.; Ansari, A.; Schmidt, P.; Hare, B.; Simkovic, N.; Farrell, S.; Shin, E.; Ptashne, M.; Wagner, G.
Citation:

Citation: Hidalgo, Patricia; Ansari, A.; Schmidt, P.; Hare, B.; Simkovic, N.; Farrell, S.; Shin, E.; Ptashne, M.; Wagner, G.. "Recruitment of the transcriptional machinery through GAL11P:structure and interactions of the GAL4 dimerization domain"  Genes Dev. 15, 1007-1020 (2001).
PubMed: 11316794

Assembly members:

Assembly members:
GAL4 dimerization domain, polymer, 57 residues, 6812 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GAL4 dimerization domain: TRAHLTEVESRLERLEQLFL LIFPREDLDMILKMDSLRDI EALLTGLFVQDNVNKDA

Data sets:
Data typeCount
13C chemical shifts34
15N chemical shifts39
1H chemical shifts150

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Gal4 subunit A, monomer1
2Gal4 subunit B, monomer1

Entities:

Entity 1, Gal4 subunit A, monomer 57 residues - 6812 Da.

1   THRARGALAHISLEUTHRGLUVALGLUSER
2   ARGLEUGLUARGLEUGLUGLNLEUPHELEU
3   LEUILEPHEPROARGGLUASPLEUASPMET
4   ILELEULYSMETASPSERLEUARGASPILE
5   GLUALALEULEUTHRGLYLEUPHEVALGLN
6   ASPASNVALASNLYSASPALA

Samples:

gal4_sample1: GAL4 dimerization domain1 – 2.0 mM

gal4_sample2: GAL4 dimerization domain, [U-15N; U-2H], 1.0 – 2.0 mM

gal4_sample3: GAL4 dimerization domain, [U-15N], 1.0 – 2.0 mM

gal4_sample4: GAL4 dimerization domain, [U-15N; U-13C], 1.0 – 2.0 mM

sample_cond_1: ionic strength: 0.1 M; pH: 7.4; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-13C HSQCnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available
3D 13C-1H-1H NOESYnot availablenot availablenot available
3D HNCAnot availablenot availablenot available
3D HN(CO)CAnot availablenot availablenot available
3D HNHAnot availablenot availablenot available
3D HNHBnot availablenot availablenot available

Software:

FELIX - Data processing

XEASY - Assignments

Molmol - Visual inspection of structures

InsightII - Visual inspection of structures

Procheck - Assesment quality of structures

NMR spectrometers:

  • Varian UnityPlus 400 MHz
  • Varian Unity 500 MHz
  • Varian INOVA 500 MHz
  • Varian UnityPlus 750 MHz
  • Bruker AMX 500 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks