BMRB Entry 34105
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34105
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Title: Dehydroascorbate reductase 3A from Populus trichocarpa complexed with GSH. PubMed: 26699905
Deposition date: 2017-02-27 Original release date: 2017-03-09
Authors: Roret, T.; Tsan, P.
Citation: Lallement, P.; Roret, T.; Tsan, P.; Gualberto, J.; Girardet, J.; Didierjean, C.; Rouhier, N.; Hecker, A.. "Insights into ascorbate regeneration in plants: investigating the redox and structural properties of dehydroascorbate reductases from Populus trichocarpa." Biochem. J. 473, 717-731 (2016).
Assembly members:
entity_1, polymer, 218 residues, 24364.195 Da.
entity_GSH, non-polymer, 307.323 Da.
Natural source: Common Name: Western balsam poplar Taxonomy ID: 3694 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Populus trichocarpa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MALEICVKAAVGAPNILGDC
PFCQRVLLSLEEKKIPYKSH
LINLGDKPQWFLEISPEGKV
PVVKIDDKWVADSDVIVGIL
EEKNPEPPLATPPEFASVGS
KIFPSFVKFLKSKDPNDGTE
QALLEELKALDGHLKVHGPF
IAGEKITAVDLSLAPKLYHL
EVALGHFKNWPIPDNLTHVL
NYIKLLFSRESFKKTRAAEE
HVIAGWEPKVNAHHHHHH
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 376 |
1H chemical shifts | 376 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 218 residues - 24364.195 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 | HIS |
Entity 2, entity_2 - C10 H17 N3 O6 S - 307.323 Da.
1 | GSH |
Samples:
sample_1: Dehydroascorbate reductase, [U-100% 15N], 0.37 mM
sample_2: Dehydroascorbate reductase, [U-100% 15N], 0.37 mM; GLUTATHIONE 74.0 mM
sample_conditions_1: ionic strength: 50 mM; pH: 8.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
YASARA, YASARA - refinement
AutoDock, AutoDock - structure calculation
CcpNMR, CCPN - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts