BMRB Entry 15617
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15617
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Wang, Xu; Weldeghorghis, Thomas; Zhang, Gufeng; Imepriali, Barbara; Prestegard, James. "Solution Structure of Alg13: The Sugar Donor Subunit of a Yeast N-Acetylglucosamine Transferase" Structure 16, 965-975 (2008).
PubMed: 18547528
Assembly members:
Alg13, polymer, 224 residues, 25066.6 Da.
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 668 |
| 15N chemical shifts | 189 |
| 1H chemical shifts | 754 |
| residual dipolar couplings | 115 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alg13 | 1 |
Entities:
Entity 1, alg13 224 residues - 25066.6 Da.
The first 23 residues of the protein are part of a His-Thrombin cleavage site tag. Alg13 starts at G24
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | LEU | GLU | GLY | ILE | ILE | GLU | GLU | LYS | ALA | ||||
| 4 | LEU | PHE | VAL | THR | CYS | GLY | ALA | THR | VAL | PRO | ||||
| 5 | PHE | PRO | LYS | LEU | VAL | SER | CYS | VAL | LEU | SER | ||||
| 6 | ASP | GLU | PHE | CYS | GLN | GLU | LEU | ILE | GLN | TYR | ||||
| 7 | GLY | PHE | VAL | ARG | LEU | ILE | ILE | GLN | PHE | GLY | ||||
| 8 | ARG | ASN | TYR | SER | SER | GLU | PHE | GLU | HIS | LEU | ||||
| 9 | VAL | GLN | GLU | ARG | GLY | GLY | GLN | ARG | GLU | SER | ||||
| 10 | GLN | LYS | ILE | PRO | ILE | ASP | GLN | PHE | GLY | CYS | ||||
| 11 | GLY | ASP | THR | ALA | ARG | GLN | TYR | VAL | LEU | MET | ||||
| 12 | ASN | GLY | LYS | LEU | LYS | VAL | ILE | GLY | PHE | ASP | ||||
| 13 | PHE | SER | THR | LYS | MET | GLN | SER | ILE | ILE | ARG | ||||
| 14 | ASP | TYR | SER | ASP | LEU | VAL | ILE | SER | HIS | ALA | ||||
| 15 | GLY | THR | GLY | SER | ILE | LEU | ASP | SER | LEU | ARG | ||||
| 16 | LEU | ASN | LYS | PRO | LEU | ILE | VAL | CYS | VAL | ASN | ||||
| 17 | ASP | SER | LEU | MET | ASP | ASN | HIS | GLN | GLN | GLN | ||||
| 18 | ILE | ALA | ASP | LYS | PHE | VAL | GLU | LEU | GLY | TYR | ||||
| 19 | VAL | TRP | SER | CYS | ALA | PRO | THR | GLU | THR | GLY | ||||
| 20 | LEU | ILE | ALA | GLY | LEU | ARG | ALA | SER | GLN | THR | ||||
| 21 | GLU | LYS | LEU | LYS | PRO | PHE | PRO | VAL | SER | HIS | ||||
| 22 | ASN | PRO | SER | PHE | GLU | ARG | LEU | LEU | VAL | GLU | ||||
| 23 | THR | ILE | TYR | SER |
Samples:
triple_label: Alg13, [U-13C; U-15N; U-2H], 0.35 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%
methyl_label: Alg13, [U-15N; U-2H; 13C,1H Leu, Val, Ile.D1 methyl], 0.35 mM; sodium phosphate 20 mM; sodium chloride 100 mM
methyl_phe_label: Alg13, [U-15N; U-2H; 13C,1H Leu, Val, Ile.D1 methyl; 1H-Phe], 0.35 mM; sodium phosphate 20 mM; sodium chloride 100 mM
gel_aligned: Alg13, [U-13C; U-15N; U-2H], 0.35 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%; acrylamide 3.5 w/v; (3-acrylamidopropyl)-trimethylammonium chloride 3.5 w/v
sample_conditions_1: ionic strength: 0.1 M; pH: 6.7; pressure: 1 atm; temperature: 297 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | triple_label | isotropic | sample_conditions_1 |
| 3D HNCACB | triple_label | isotropic | sample_conditions_1 |
| 3D HNCA | triple_label | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | triple_label | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | triple_label | isotropic | sample_conditions_1 |
| 3D HNCACO | triple_label | isotropic | sample_conditions_1 |
| 3D HNCO | triple_label | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | methyl_label | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | methyl_label | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | methyl_phe_label | isotropic | sample_conditions_1 |
| 2D S3-TROSY | gel_aligned | anisotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Varian Unity 600 MHz
- Varian Unity 900 MHz
Related Database Links:
| PDB | |
| DBJ | GAA23342 |
| EMBL | CAA96749 CAY79713 |
| GB | AHY79326 AJP38744 AJR76064 AJR76565 AJR77063 |
| REF | NP_011468 |
| SP | P53178 |
| TPG | DAA08054 |
| AlphaFold | P53178 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks