BMRB Entry 25243
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25243
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Title: AN ARSENATE REDUCTASE IN OXIDIZED STATE PubMed: 26224634
Deposition date: 2014-09-23 Original release date: 2015-08-03
Authors: Jin, Changwen; Hu, Cuiyun
Citation: Jin, Changwen; Hu, Cuiyun. "A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction" J. Biol. Chem. 290, 22262-22273 (2015).
Assembly members:
entity, polymer, 131 residues, 14409.351 Da.
Natural source: Common Name: Synechocystis Taxonomy ID: 1142 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MKKVMFVSKRNSSRSQMAEG
FAKTLGAGKIAVTSSGLESS
RVHPTAIAMMEEVGIDISGQ
TSDPIENFNADDYDVVISLC
GCGVNLPPEWVTQEIFEDWQ
LEDPDGQSLEVFRTVRGQVK
ERVENLIAKIS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 542 |
| 15N chemical shifts | 138 |
| 1H chemical shifts | 875 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Arsenate Reductase | 1 |
Entities:
Entity 1, Arsenate Reductase 131 residues - 14409.351 Da.
| 1 | MET | LYS | LYS | VAL | MET | PHE | VAL | SER | LYS | ARG | ||||
| 2 | ASN | SER | SER | ARG | SER | GLN | MET | ALA | GLU | GLY | ||||
| 3 | PHE | ALA | LYS | THR | LEU | GLY | ALA | GLY | LYS | ILE | ||||
| 4 | ALA | VAL | THR | SER | SER | GLY | LEU | GLU | SER | SER | ||||
| 5 | ARG | VAL | HIS | PRO | THR | ALA | ILE | ALA | MET | MET | ||||
| 6 | GLU | GLU | VAL | GLY | ILE | ASP | ILE | SER | GLY | GLN | ||||
| 7 | THR | SER | ASP | PRO | ILE | GLU | ASN | PHE | ASN | ALA | ||||
| 8 | ASP | ASP | TYR | ASP | VAL | VAL | ILE | SER | LEU | CYS | ||||
| 9 | GLY | CYS | GLY | VAL | ASN | LEU | PRO | PRO | GLU | TRP | ||||
| 10 | VAL | THR | GLN | GLU | ILE | PHE | GLU | ASP | TRP | GLN | ||||
| 11 | LEU | GLU | ASP | PRO | ASP | GLY | GLN | SER | LEU | GLU | ||||
| 12 | VAL | PHE | ARG | THR | VAL | ARG | GLY | GLN | VAL | LYS | ||||
| 13 | GLU | ARG | VAL | GLU | ASN | LEU | ILE | ALA | LYS | ILE | ||||
| 14 | SER |
Samples:
sample_1: protein, [U-15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 50 mM
sample_2: protein, [U-13C; U-15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 50 mM
sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts