BMRB Entry 27489
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27489
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H, 15N, 13C Assignment of rS1-D5 PubMed: 30124944
Deposition date: 2018-05-23 Original release date: 2018-08-13
Authors: Qureshi, Nusrat; Bains, Jasleen; Sreeramulu, Sridhar; Schwalbe, Harald; Fuertig, Boris
Citation: Qureshi, Nusrat; Bains, Jasleen; Sreeramulu, Sridhar; Schwalbe, Harald; Fuertig, Boris. "Conformational switch in the ribosomal protein S1 guides unfolding of structured RNAs for translation initiation" Nucleic Acids Res. 46, 10917-10929 (2018).
Assembly members:
rS1-D5, polymer, 94 residues, Formula weight is not available
Natural source: Common Name: Vibrio vulnificus Taxonomy ID: 672 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio vulnificus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pKMTX
Entity Sequences (FASTA):
rS1-D5: GAMAEAQAKGDKVTGKIKSI
TDFGIFIGLDGGIDGLVHLS
DISWNVAGEETVREFKKGDE
ISAVVLAVDAERERISLGIK
QMENDPFNAYVADN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 220 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 91 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rS1-D5 | 1 |
Entities:
Entity 1, rS1-D5 94 residues - Formula weight is not available
| 1 | GLY | ALA | MET | ALA | GLU | ALA | GLN | ALA | LYS | GLY | ||||
| 2 | ASP | LYS | VAL | THR | GLY | LYS | ILE | LYS | SER | ILE | ||||
| 3 | THR | ASP | PHE | GLY | ILE | PHE | ILE | GLY | LEU | ASP | ||||
| 4 | GLY | GLY | ILE | ASP | GLY | LEU | VAL | HIS | LEU | SER | ||||
| 5 | ASP | ILE | SER | TRP | ASN | VAL | ALA | GLY | GLU | GLU | ||||
| 6 | THR | VAL | ARG | GLU | PHE | LYS | LYS | GLY | ASP | GLU | ||||
| 7 | ILE | SER | ALA | VAL | VAL | LEU | ALA | VAL | ASP | ALA | ||||
| 8 | GLU | ARG | GLU | ARG | ILE | SER | LEU | GLY | ILE | LYS | ||||
| 9 | GLN | MET | GLU | ASN | ASP | PRO | PHE | ASN | ALA | TYR | ||||
| 10 | VAL | ALA | ASP | ASN |
Samples:
sample_1: rS1-D5, [U-98% 13C; U-98% 15N], 0.35 mM; potassium phosphate 25 mM; KCl 150 mM; DTT 5 mM
sample_2: rS1-D5, [U-98% 15N], 0.1 mM; potassium phosphate 25 mM; KCl 150 mM; DTT 5 mM
sample_conditions_1: ionic strength: 206 mM; pH: 7.2; pressure: 1 atm; temperature: 285 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.5, Bruker Biospin - collection, processing
SPARKY v3.114, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 600 MHz
- Bruker Avance 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts