BMRB Entry 15087
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15087
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Title: SOLUTION STRUCTURE OF THE PABC DOMAIN FROM TRITICUM AEVESTIUM POLY(A)-BINDING PROTEIN PubMed: 17358048
Deposition date: 2006-12-28 Original release date: 2007-03-05
Authors: Siddiqui, Nadeem
Citation: Siddiqui, Nadeem; Osborne, Michael; Gallie, Daniel; Gehring, Kalle. "Solution structure of the PABC domain from wheat poly (A)-binding protein: an insight into RNA metabolic and translational control in plants." Biochemistry 46, 4221-4231 (2007).
Assembly members:
Poly(A)-binding_protein, polymer, 85 residues, Formula weight is not available
Natural source: Common Name: Wheat Taxonomy ID: 4565 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Triticum aestivum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P1
Entity Sequences (FASTA):
Poly(A)-binding_protein: GPLGSPIGALASALANSPPE
TQRMMLGENLYPLVDQLEHD
QAAKVTGMLLEMDQTEVLHL
LESPDALKAKVAEAMEVLRS
AQQHT
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 393 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PABC | 1 |
Entities:
Entity 1, PABC 85 residues - Formula weight is not available
This is the C-terminal segment from wheat PABP.
| 1 | GLY | PRO | LEU | GLY | SER | PRO | ILE | GLY | ALA | LEU | ||||
| 2 | ALA | SER | ALA | LEU | ALA | ASN | SER | PRO | PRO | GLU | ||||
| 3 | THR | GLN | ARG | MET | MET | LEU | GLY | GLU | ASN | LEU | ||||
| 4 | TYR | PRO | LEU | VAL | ASP | GLN | LEU | GLU | HIS | ASP | ||||
| 5 | GLN | ALA | ALA | LYS | VAL | THR | GLY | MET | LEU | LEU | ||||
| 6 | GLU | MET | ASP | GLN | THR | GLU | VAL | LEU | HIS | LEU | ||||
| 7 | LEU | GLU | SER | PRO | ASP | ALA | LEU | LYS | ALA | LYS | ||||
| 8 | VAL | ALA | GLU | ALA | MET | GLU | VAL | LEU | ARG | SER | ||||
| 9 | ALA | GLN | GLN | HIS | THR |
Samples:
sample_1: PABP; Sodium phosphate, Sodium Chloride, Sodium Azide, [U-15N], 1 – 2 mM; phosphate buffer 50 mM; NaCl 150 mM; NaN3 1 mM; H2O 90%; D2O 10%
sample_2: PABP; Sodium phosphate, Sodium Chloride, Sodium Azide, [U-100% 13C; U-100% 15N], 1 – 2 mM; phosphate buffer 50 mM; NaCl 150 mM; NaN3 1 mM; H2O 90%; D2O 10%
sample_3: PABP; Sodium phosphate, Sodium Chloride, Sodium Azide, none, 1 – 2 mM; phosphate buffer 50 mM; NaCl 150 mM; NaN3 1 mM; H2O 90%; D2O 10%
sample_4: Poly(A)-binding protein, [U-100% 13C; U-100% 15N], 1 – 2 mM; phosphate buffer 50 mM; NaCl 150 mM; NaN3 1 mM; D2O 100%
sample_conditions_1: ionic strength: 200 mM; pH: 6.3; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 2D NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D_15N-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
| HNCACB | sample_2 | isotropic | sample_conditions_1 |
| CBCACONH | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.1, A Brunger, P Adams, M Clore, P Gros, M Nilges and R Read - refinement
NMR spectrometers:
- Varian UNITY 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts