BMRB Entry 17076
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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/BMR17076
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Title: An arsenate reductase PubMed: 20960080
Deposition date: 2010-07-24 Original release date: 2010-10-22
Authors: Yu, Caifang; Xia, Bin; Jin, Changwen
Citation: Yu, Caifang; Xia, Bin; Jin, Changwen. "(1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803." Biomol. NMR Assignments 5, 85-87 (2011).
Assembly members:
SynArsC, polymer, 134 residues, Formula weight is not available
Natural source: Common Name: Synechocystis sp. PCC 6803 Taxonomy ID: 1148 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SynArsC: GSHMKKVMFVCKRNSCRSQM
AEGFAKTLGAGKIAVTSCGL
ESSRVHPTAIAMMEEVGIDI
SGQTSDPIENFNADDYDVVI
SLCGCGVNLPPEWVTQEIFE
DWQLEDPDGQSLEVFRTVRG
QVKERVENLIAKIS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 519 |
15N chemical shifts | 133 |
1H chemical shifts | 839 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SynArsC | 1 |
Entities:
Entity 1, SynArsC 134 residues - Formula weight is not available
1 | GLY | SER | HIS | MET | LYS | LYS | VAL | MET | PHE | VAL | ||||
2 | CYS | LYS | ARG | ASN | SER | CYS | ARG | SER | GLN | MET | ||||
3 | ALA | GLU | GLY | PHE | ALA | LYS | THR | LEU | GLY | ALA | ||||
4 | GLY | LYS | ILE | ALA | VAL | THR | SER | CYS | GLY | LEU | ||||
5 | GLU | SER | SER | ARG | VAL | HIS | PRO | THR | ALA | ILE | ||||
6 | ALA | MET | MET | GLU | GLU | VAL | GLY | ILE | ASP | ILE | ||||
7 | SER | GLY | GLN | THR | SER | ASP | PRO | ILE | GLU | ASN | ||||
8 | PHE | ASN | ALA | ASP | ASP | TYR | ASP | VAL | VAL | ILE | ||||
9 | SER | LEU | CYS | GLY | CYS | GLY | VAL | ASN | LEU | PRO | ||||
10 | PRO | GLU | TRP | VAL | THR | GLN | GLU | ILE | PHE | GLU | ||||
11 | ASP | TRP | GLN | LEU | GLU | ASP | PRO | ASP | GLY | GLN | ||||
12 | SER | LEU | GLU | VAL | PHE | ARG | THR | VAL | ARG | GLY | ||||
13 | GLN | VAL | LYS | GLU | ARG | VAL | GLU | ASN | LEU | ILE | ||||
14 | ALA | LYS | ILE | SER |
Samples:
sample_1: SynArsC, [U-15N], 1 mM; DSS 0.01%; sodium azide 0.01%; sodium chloride 50 mM; TRIS 50 mM; DTT 40 mM; D2O 10%; H2O 90%
sample_2: SynArsC, [U-13C; U-15N], 1 mM; DSS 0.01%; sodium azide 0.01%; sodium chloride 50 mM; TRIS 50 mM; DTT 40 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D CCH-COSY | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
Related Database Links:
BMRB | 17074 17077 25243 |
PDB | |
DBJ | BAA18407 BAK50581 BAL29580 BAL32749 BAL35918 |
GB | AGF52095 ALJ68053 |
REF | WP_010873028 |
SP | P74313 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts