BMRB Entry 25712
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25712
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Title: Solution structure of the dehydroascorbate reductase 3A from Populus trichocarpa PubMed: 26699905
Deposition date: 2015-07-15 Original release date: 2016-03-14
Authors: Roret, Thomas; Tsan, Pascale
Citation: Lallement, Pierre-Alexandre; Roret, Thomas; Tsan, Pascale; M. Gualberto, Jose; Girardet, Jean-Michel; Didierjean, Claude; Rouhier, Nicolas; Hecker, Arnaud. "Biochemical and structural characterization of dehydroascorbate reductases from poplar (Populus trichocarpa), enzymes contributing to the maintenance of the ascorbate pool in plants" Biochem. J. 473, 717-731 (2016).
Assembly members:
Pt-DHAR3A, polymer, 217 residues, 23535.525 Da.
Natural source: Common Name: black cottonwood Taxonomy ID: 3694 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Populus trichocarpa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Pt-DHAR3A: MALEICVKAAVGAPNILGDC
PFCQRVLLSLEEKKIPYKSH
LINLGDKPQWFLEISPEGKV
PVVKIDDKWVADSDVIVGIL
EEKNPEPPLATPPEFASVGS
KIFPSFVKFLKSKDPNDGTE
QALLEELKALDGHLKVHGPF
IAGEKITAVDLSLAPKLYHL
EVALGHFKNWPIPDNLTHVL
NYIKLLFSRESFKKTRAAEE
HVIAGWEPKVNAHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 542 |
| 15N chemical shifts | 207 |
| 1H chemical shifts | 1107 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 217 residues - 23535.525 Da.
| 1 | MET | ALA | LEU | GLU | ILE | CYS | VAL | LYS | ALA | ALA | ||||
| 2 | VAL | GLY | ALA | PRO | ASN | ILE | LEU | GLY | ASP | CYS | ||||
| 3 | PRO | PHE | CYS | GLN | ARG | VAL | LEU | LEU | SER | LEU | ||||
| 4 | GLU | GLU | LYS | LYS | ILE | PRO | TYR | LYS | SER | HIS | ||||
| 5 | LEU | ILE | ASN | LEU | GLY | ASP | LYS | PRO | GLN | TRP | ||||
| 6 | PHE | LEU | GLU | ILE | SER | PRO | GLU | GLY | LYS | VAL | ||||
| 7 | PRO | VAL | VAL | LYS | ILE | ASP | ASP | LYS | TRP | VAL | ||||
| 8 | ALA | ASP | SER | ASP | VAL | ILE | VAL | GLY | ILE | LEU | ||||
| 9 | GLU | GLU | LYS | ASN | PRO | GLU | PRO | PRO | LEU | ALA | ||||
| 10 | THR | PRO | PRO | GLU | PHE | ALA | SER | VAL | GLY | SER | ||||
| 11 | LYS | ILE | PHE | PRO | SER | PHE | VAL | LYS | PHE | LEU | ||||
| 12 | LYS | SER | LYS | ASP | PRO | ASN | ASP | GLY | THR | GLU | ||||
| 13 | GLN | ALA | LEU | LEU | GLU | GLU | LEU | LYS | ALA | LEU | ||||
| 14 | ASP | GLY | HIS | LEU | LYS | VAL | HIS | GLY | PRO | PHE | ||||
| 15 | ILE | ALA | GLY | GLU | LYS | ILE | THR | ALA | VAL | ASP | ||||
| 16 | LEU | SER | LEU | ALA | PRO | LYS | LEU | TYR | HIS | LEU | ||||
| 17 | GLU | VAL | ALA | LEU | GLY | HIS | PHE | LYS | ASN | TRP | ||||
| 18 | PRO | ILE | PRO | ASP | ASN | LEU | THR | HIS | VAL | LEU | ||||
| 19 | ASN | TYR | ILE | LYS | LEU | LEU | PHE | SER | ARG | GLU | ||||
| 20 | SER | PHE | LYS | LYS | THR | ARG | ALA | ALA | GLU | GLU | ||||
| 21 | HIS | VAL | ILE | ALA | GLY | TRP | GLU | PRO | LYS | VAL | ||||
| 22 | ASN | ALA | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Pt-DHAR3A, [U-100% 13C; U-100% 15N], 0.7 – 1.3 mM; sodium phosphate 50 mM; 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 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA vv 2.3, Linge, O'Donoghue and Nilges - refinement, structure solution
CNS vv 1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMRView vv 2.4, Johnson, One Moon Scientific - data analysis
CcpNMR vv 2.4.1, CCPN - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts