BMRB Entry 17685
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17685
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of the C-terminal Pdr1 activating domain of Zuo1 PubMed: 23036859
Deposition date: 2011-06-02 Original release date: 2012-10-01
Authors: Volkman, B.; Waltner, J.; Peterson, F.
Citation: Ducett, Jeanette; Peterson, Francis; Hoover, Lindsey; Prunuske, Amy; Volkman, Brian; Craig, Elizabeth. "Unfolding of the C-terminal domain of the J-protein Zuo1 releases autoinhibition and activates Pdr1-dependent transcription." J. Mol. Biol. 425, 19-31 (2013).
Assembly members:
Zuo1, polymer, 108 residues, 11836.323 Da.
Natural source: Common Name: yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Zuo1: MRGSHHHHHHHHGSENLYFQ
GSKAAKKKNKRAIRNSAKEA
DYFGDADKATTIDEQVGLIV
DSLNDEELVSTADKIKANAA
GAKEVLKESAKTIVDSGKLP
SSLLSYFV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 373 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 616 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Zuo1 | 1 |
Entities:
Entity 1, Zuo1 108 residues - 11836.323 Da.
The N-terminal residues 'MRGSHHHHHHHHGSENLYFQGS' are a cloning artifact.
| 1 | MET | ARG | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | HIS | HIS | GLY | SER | GLU | ASN | LEU | TYR | PHE | GLN | ||||
| 3 | GLY | SER | LYS | ALA | ALA | LYS | LYS | LYS | ASN | LYS | ||||
| 4 | ARG | ALA | ILE | ARG | ASN | SER | ALA | LYS | GLU | ALA | ||||
| 5 | ASP | TYR | PHE | GLY | ASP | ALA | ASP | LYS | ALA | THR | ||||
| 6 | THR | ILE | ASP | GLU | GLN | VAL | GLY | LEU | ILE | VAL | ||||
| 7 | ASP | SER | LEU | ASN | ASP | GLU | GLU | LEU | VAL | SER | ||||
| 8 | THR | ALA | ASP | LYS | ILE | LYS | ALA | ASN | ALA | ALA | ||||
| 9 | GLY | ALA | LYS | GLU | VAL | LEU | LYS | GLU | SER | ALA | ||||
| 10 | LYS | THR | ILE | VAL | ASP | SER | GLY | LYS | LEU | PRO | ||||
| 11 | SER | SER | LEU | LEU | SER | TYR | PHE | VAL |
Samples:
sample: Zuo1, [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_13C-separated_NOESY (AROMATIC) | sample | isotropic | sample_conditions_1 |
| 3D_13C-separated_NOESY | sample | isotropic | sample_conditions_1 |
| 3D_15N-separated_NOESY | sample | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement
TOPSPIN v2.1, Bruker - collection
NMRPipe v2007, Delagio,F. et al. - processing
XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis
GARANT v2.1, C. Bartels - data analysis
CYANA v2.1, Guntert, P. - structural calculation
NMR spectrometers:
- Bruker Avance II 600 MHz
Related Database Links:
| PDB | |
| DBJ | GAA23651 |
| EMBL | CAY80044 |
| GB | AHY79619 AJP39050 AJR76370 AJR76866 AJR77364 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts