BMRB Entry 19849
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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/BMR19849
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Title: Solution structure of reduced BolA2 from Arabidopsis thaliana PubMed: 25012657
Deposition date: 2014-03-13 Original release date: 2014-07-21
Authors: RORET, THOMAS; TSAN, PASCALE; COUTURIER, JEREMY; ROUHIER, NICOLAS; DIDIERJEAN, CLAUDE
Citation: Roret, Thomas; Tsan, Pascale; Couturier, Jeremy; Zhang, Bo; Johnson, Michael; Rouhier, Nicolas; Didierjean, Claude. "Structural and Spectroscopic Insights into BolA-Glutaredoxin Complexes." J. Biol. Chem. 289, 24588-24598 (2014).
Assembly members:
BolA2, polymer, 93 residues, 10389.931 Da.
Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BolA2: MVTKEQVEASLTSKLKPIHL
EVIDISGGCGSSFEVEVVSE
QFEGKRLLERHRMVNAALEE
EMKEIHALSIKKAQTPQQWK
PPSQDSATLTKDA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 445 |
| 13C chemical shifts | 244 |
| 15N chemical shifts | 95 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | reduced BolA2 from Arabidopsis thaliana | 1 |
Entities:
Entity 1, reduced BolA2 from Arabidopsis thaliana 93 residues - 10389.931 Da.
| 1 | MET | VAL | THR | LYS | GLU | GLN | VAL | GLU | ALA | SER | ||||
| 2 | LEU | THR | SER | LYS | LEU | LYS | PRO | ILE | HIS | LEU | ||||
| 3 | GLU | VAL | ILE | ASP | ILE | SER | GLY | GLY | CYS | GLY | ||||
| 4 | SER | SER | PHE | GLU | VAL | GLU | VAL | VAL | SER | GLU | ||||
| 5 | GLN | PHE | GLU | GLY | LYS | ARG | LEU | LEU | GLU | ARG | ||||
| 6 | HIS | ARG | MET | VAL | ASN | ALA | ALA | LEU | GLU | GLU | ||||
| 7 | GLU | MET | LYS | GLU | ILE | HIS | ALA | LEU | SER | ILE | ||||
| 8 | LYS | LYS | ALA | GLN | THR | PRO | GLN | GLN | TRP | LYS | ||||
| 9 | PRO | PRO | SER | GLN | ASP | SER | ALA | THR | LEU | THR | ||||
| 10 | LYS | ASP | ALA |
Samples:
sample_1: BolA2, [U-100% 13C; U-100% 15N], 0.9 mM; phosphate buffer 50 mM; azide 0.02%; H2O 90%; D2O 10%
sample_2: BolA2, [U-100% 15N], 0.9 mM; phosphate buffer 50 mM; azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
ARIA v2.3, Linge, O, . - chemical shift assignment, refinement, structure solution
CcpNmr, CCPN - data analysis, peak picking
NMRView, Johnson, One Moon Scientific - peak picking
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB09404 BAF00125 |
| GB | AAM65194 AAO24583 AED91453 EFH49685 |
| REF | NP_568217 XP_002873426 |
| SP | Q9FIC3 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts