BMRB Entry 6075
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6075
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Title: Backbone and side chain assignment of arsenate reductase from Bacillus Subtilis PubMed: 15213468
Deposition date: 2004-01-13 Original release date: 2004-07-06
Authors: Peng, Kuan; Su, Xiao-dong; Xia, Bin; Jin, Changwen
Citation: Peng, Kuan; Su, Xiao-dong; Xia, Bin; Jin, Changwen. "Letter to the Editor: 1H, 13C and 15N resonance assignments of a Bacillus Subtilis arsenate reductase " J. Biomol. NMR 29, 459-460 (2004).
Assembly members:
Arsenate reductase, polymer, 139 residues, Formula weight is not available
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Eubacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Arsenate reductase: MENKIIYFLCTGNSCRSQMA
EGWAKQYLGDEWKVYSAGIE
AHGLNPNAVKAMKEVGIDIS
NQTSDIIDSDILNNADLVVT
LCGDAADKCPMTPPHVKREH
WGFDDPARAQGTEEEKWAFF
QRVRDEIGNRLKEFAETGK
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 859 |
| 13C chemical shifts | 526 |
| 15N chemical shifts | 147 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ArsC monomer | 1 |
Entities:
Entity 1, ArsC monomer 139 residues - Formula weight is not available
| 1 | MET | GLU | ASN | LYS | ILE | ILE | TYR | PHE | LEU | CYS | ||||
| 2 | THR | GLY | ASN | SER | CYS | ARG | SER | GLN | MET | ALA | ||||
| 3 | GLU | GLY | TRP | ALA | LYS | GLN | TYR | LEU | GLY | ASP | ||||
| 4 | GLU | TRP | LYS | VAL | TYR | SER | ALA | GLY | ILE | GLU | ||||
| 5 | ALA | HIS | GLY | LEU | ASN | PRO | ASN | ALA | VAL | LYS | ||||
| 6 | ALA | MET | LYS | GLU | VAL | GLY | ILE | ASP | ILE | SER | ||||
| 7 | ASN | GLN | THR | SER | ASP | ILE | ILE | ASP | SER | ASP | ||||
| 8 | ILE | LEU | ASN | ASN | ALA | ASP | LEU | VAL | VAL | THR | ||||
| 9 | LEU | CYS | GLY | ASP | ALA | ALA | ASP | LYS | CYS | PRO | ||||
| 10 | MET | THR | PRO | PRO | HIS | VAL | LYS | ARG | GLU | HIS | ||||
| 11 | TRP | GLY | PHE | ASP | ASP | PRO | ALA | ARG | ALA | GLN | ||||
| 12 | GLY | THR | GLU | GLU | GLU | LYS | TRP | ALA | PHE | PHE | ||||
| 13 | GLN | ARG | VAL | ARG | ASP | GLU | ILE | GLY | ASN | ARG | ||||
| 14 | LEU | LYS | GLU | PHE | ALA | GLU | THR | GLY | LYS |
Samples:
sample_1: Arsenate reductase, [U-13C; U-15N], 1 – 3 mM; Tris-HCl buffer 20 mM; KCl 40 mM; Na2SO4 20 mM; DTT 20 mM; Urea 20 mM; H2O 95%; D2O 5%
condition_1: pH: 6.85 na; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 15N HSQC | not available | not available | not available |
| HNCACB | not available | not available | not available |
| CBCA(CO)NH | not available | not available | not available |
| HBHA(CO)NH | not available | not available | not available |
| 1H-15N TOCSYHSQC | not available | not available | not available |
| 1H-15N NOESYHSQC | not available | not available | not available |
| HCCHCOSY | not available | not available | not available |
Software:
No software information available
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 500 MHz
Related Database Links:
| BMRB | 15028 6563 |
| PDB | |
| DBJ | BAA06970 BAA12434 BAM58640 |
| EMBL | CAB14519 CEI57801 CEJ78223 |
| GB | ADV93326 AFH58698 AFH58699 AFH58701 AFH58702 |
| REF | NP_390455 WP_004398596 WP_015385204 WP_015483976 WP_029318100 |
| SP | P45947 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts