BMRB Entry 50734
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50734
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Title: NMR backbone resonance assignment of the selenoprotein SelW1 (oxidized) from Chlamydomonas reinhardtii. PubMed: 34216797
Deposition date: 2021-01-25 Original release date: 2021-07-11
Authors: Seeger, Karsten; Schmidt, Christian
Citation: Schmidt, Christian; Daberger, Jan; Sobek, Michael; Seeger, Karsten. "Structural and biophysical characterization of the selenoprotein SelW1 from Chlamydomonas reinhardtii." Biochim. Biophys. Acta Proteins Proteom. 1869, 140685-140685 (2021).
Assembly members:
entity_1, polymer, 88 residues, Formula weight is not available
Natural source: Common Name: green algae Taxonomy ID: 3055 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Chlamydomonas reinhardtii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b
Entity Sequences (FASTA):
entity_1: MAPVQVHVLYCGGCGYGSRY
RSLENAIRMKFPNADIKFSF
EATPQATGFFEVEVNGELVH
SKKNGGGHVDNQEKVERIFA
KIGEALAK
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 370 |
| 15N chemical shifts | 122 |
| 1H chemical shifts | 543 |
| T1 relaxation values | 109 |
| T2 relaxation values | 109 |
| heteronuclear NOE values | 94 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SelW1, conformer 1 | 1 |
| 2 | SelW1, conformer 2 | 1 |
| 3 | SelW1, conformer 3 | 1 |
Entities:
Entity 1, SelW1, conformer 1 88 residues - Formula weight is not available
The U14C mutant Selenoprotein W1 (provided amino acid sequence) is investigated. In the wildtype selenoprotein W1 from Chlamydomonas position 14 is selenocystein.
| 1 | MET | ALA | PRO | VAL | GLN | VAL | HIS | VAL | LEU | TYR | ||||
| 2 | CYS | GLY | GLY | CYS | GLY | TYR | GLY | SER | ARG | TYR | ||||
| 3 | ARG | SER | LEU | GLU | ASN | ALA | ILE | ARG | MET | LYS | ||||
| 4 | PHE | PRO | ASN | ALA | ASP | ILE | LYS | PHE | SER | PHE | ||||
| 5 | GLU | ALA | THR | PRO | GLN | ALA | THR | GLY | PHE | PHE | ||||
| 6 | GLU | VAL | GLU | VAL | ASN | GLY | GLU | LEU | VAL | HIS | ||||
| 7 | SER | LYS | LYS | ASN | GLY | GLY | GLY | HIS | VAL | ASP | ||||
| 8 | ASN | GLN | GLU | LYS | VAL | GLU | ARG | ILE | PHE | ALA | ||||
| 9 | LYS | ILE | GLY | GLU | ALA | LEU | ALA | LYS |
Samples:
sample_1: Selenoprotein W1, [U-15N], 0.89 mM; sodium chloride 25 mM; sodium phosphate 25 mM; TSP 0.1 mM
sample_2: Selenoprotein W1, [U-13C; U-15N], 1.0 mM; sodium chloride 25 mM; sodium phosphate 25 mM; TSP 0.1 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 15N-(1H) NOE | sample_1 | isotropic | sample_conditions_1 |
| T1/R1 relaxation | sample_1 | isotropic | sample_conditions_1 |
| T2/R2 relaxation | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment, data analysis
TOPSPIN v3.2 and higher - collection, processing
NMR spectrometers:
- Bruker AVANCE III 500 MHz
Related Database Links:
| NCBI | XP_001693901 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts