BMRB Entry 5180
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5180
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Title: Solution nmr structure of the dimerization domain of the yeast transcriptional activator Gal4 (residues 50-106) PubMed: 11316794
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: 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).
Assembly members:
GAL4 dimerization domain, polymer, 57 residues, 6812 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
GAL4 dimerization domain: TRAHLTEVESRLERLEQLFL
LIFPREDLDMILKMDSLRDI
EALLTGLFVQDNVNKDA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 34 |
15N chemical shifts | 39 |
1H chemical shifts | 150 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Gal4 subunit A, monomer | 1 |
2 | Gal4 subunit B, monomer | 1 |
Entities:
Entity 1, Gal4 subunit A, monomer 57 residues - 6812 Da.
1 | THR | ARG | ALA | HIS | LEU | THR | GLU | VAL | GLU | SER | ||||
2 | ARG | LEU | GLU | ARG | LEU | GLU | GLN | LEU | PHE | LEU | ||||
3 | LEU | ILE | PHE | PRO | ARG | GLU | ASP | LEU | ASP | MET | ||||
4 | ILE | LEU | LYS | MET | ASP | SER | LEU | ARG | ASP | ILE | ||||
5 | GLU | ALA | LEU | LEU | THR | GLY | LEU | PHE | VAL | GLN | ||||
6 | ASP | ASN | VAL | ASN | LYS | ASP | ALA |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H NOESY | not available | not available | not available |
2D 1H-13C HSQC | not available | not available | not available |
2D 1H-15N HSQC | not available | not available | not available |
3D 1H-1H-15N NOESY | not available | not available | not available |
3D 13C-1H-1H NOESY | not available | not available | not available |
3D HNCA | not available | not available | not available |
3D HN(CO)CA | not available | not available | not available |
3D HNHA | not available | not available | not available |
3D HNHB | not available | not available | not 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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts