BMRB Entry 27490
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27490
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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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).
PubMed: 30124944
Assembly members:
rS1-D345, polymer, 272 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-D345: GAMVERDELLETLQEGSEVK
GIVKNLTDYGAFVDLGGVDG
LLHITDMAWKRVKHPSEIVN
VGDEILVKVLKFDRDRTRVS
LGLKQLGEDPWVAIAKRYPE
GHKLSGRVTNLTDYGCFVEI
EEGVEGLVHVSEMDWTNKNI
HPSKVVNVGDEVEVMVLEID
EERRRISLGLKQCKANPWQS
FAEAQAKGDKVTGKIKSITD
FGIFIGLDGGIDGLVHLSDI
SWNVAGEETVREFKKGDEIS
AVVLAVDAERERISLGIKQM
ENDPFNAYVADN
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 357 |
| 1H chemical shifts | 357 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rS1-D345 | 1 |
Entities:
Entity 1, rS1-D345 272 residues - Formula weight is not available
| 1 | GLY | ALA | MET | VAL | GLU | ARG | ASP | GLU | LEU | LEU | ||||
| 2 | GLU | THR | LEU | GLN | GLU | GLY | SER | GLU | VAL | LYS | ||||
| 3 | GLY | ILE | VAL | LYS | ASN | LEU | THR | ASP | TYR | GLY | ||||
| 4 | ALA | PHE | VAL | ASP | LEU | GLY | GLY | VAL | ASP | GLY | ||||
| 5 | LEU | LEU | HIS | ILE | THR | ASP | MET | ALA | TRP | LYS | ||||
| 6 | ARG | VAL | LYS | HIS | PRO | SER | GLU | ILE | VAL | ASN | ||||
| 7 | VAL | GLY | ASP | GLU | ILE | LEU | VAL | LYS | VAL | LEU | ||||
| 8 | LYS | PHE | ASP | ARG | ASP | ARG | THR | ARG | VAL | SER | ||||
| 9 | LEU | GLY | LEU | LYS | GLN | LEU | GLY | GLU | ASP | PRO | ||||
| 10 | TRP | VAL | ALA | ILE | ALA | LYS | ARG | TYR | PRO | GLU | ||||
| 11 | GLY | HIS | LYS | LEU | SER | GLY | ARG | VAL | THR | ASN | ||||
| 12 | LEU | THR | ASP | TYR | GLY | CYS | PHE | VAL | GLU | ILE | ||||
| 13 | GLU | GLU | GLY | VAL | GLU | GLY | LEU | VAL | HIS | VAL | ||||
| 14 | SER | GLU | MET | ASP | TRP | THR | ASN | LYS | ASN | ILE | ||||
| 15 | HIS | PRO | SER | LYS | VAL | VAL | ASN | VAL | GLY | ASP | ||||
| 16 | GLU | VAL | GLU | VAL | MET | VAL | LEU | GLU | ILE | ASP | ||||
| 17 | GLU | GLU | ARG | ARG | ARG | ILE | SER | LEU | GLY | LEU | ||||
| 18 | LYS | GLN | CYS | LYS | ALA | ASN | PRO | TRP | GLN | SER | ||||
| 19 | PHE | ALA | GLU | ALA | GLN | ALA | LYS | GLY | ASP | LYS | ||||
| 20 | VAL | THR | GLY | LYS | ILE | LYS | SER | ILE | THR | ASP | ||||
| 21 | PHE | GLY | ILE | PHE | ILE | GLY | LEU | ASP | GLY | GLY | ||||
| 22 | ILE | ASP | GLY | LEU | VAL | HIS | LEU | SER | ASP | ILE | ||||
| 23 | SER | TRP | ASN | VAL | ALA | GLY | GLU | GLU | THR | VAL | ||||
| 24 | ARG | GLU | PHE | LYS | LYS | GLY | ASP | GLU | ILE | SER | ||||
| 25 | ALA | VAL | VAL | LEU | ALA | VAL | ASP | ALA | GLU | ARG | ||||
| 26 | GLU | ARG | ILE | SER | LEU | GLY | ILE | LYS | GLN | MET | ||||
| 27 | GLU | ASN | ASP | PRO | PHE | ASN | ALA | TYR | VAL | ALA | ||||
| 28 | ASP | ASN |
Samples:
sample_1: rS1-D345, [U-98% 15N], 0.1 mM; potassium phosphate 25 mM; KCl 150 mM; DTT 5 mM
sample_conditions_1: ionic strength: 208 mM; pH: 7.2; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks