BMRB Entry 25856
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25856
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Title: Solution structure of translation initiation factor from Staphylococcus aureus Mu50 PubMed: 27784646
Deposition date: 2015-10-21 Original release date: 2016-10-20
Authors: Kim, Do-Hee; Lee, Ki-Young; Lee, Bong-Jin
Citation: Kim, Do-Hee; Kang, Su-Jin; Lee, Ki-Young; Jang, Sun-Bok; Kang, Sung-Min; Lee, Bong-Jin. "Structure and dynamics study of translation initiation factor 1 from Staphylococcus aureus suggests its RNA binding mode." Biochim. Biophys. Acta 1865, 65-75 (2017).
Assembly members:
Translation_factor, polymer, 72 residues, 8291.713 Da.
Natural source: Common Name: firmicutes Taxonomy ID: 1388021 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Translation_factor: MAKQDVIELEGTVLDTLPNA
MFKVELENGHEILAHVSGKI
RMNYIRILPGDKVTVEMSPY
DLTRGRITYRYK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 269 |
| 15N chemical shifts | 65 |
| 1H chemical shifts | 378 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Translation_factor | 1 |
Entities:
Entity 1, Translation_factor 72 residues - 8291.713 Da.
| 1 | MET | ALA | LYS | GLN | ASP | VAL | ILE | GLU | LEU | GLU | ||||
| 2 | GLY | THR | VAL | LEU | ASP | THR | LEU | PRO | ASN | ALA | ||||
| 3 | MET | PHE | LYS | VAL | GLU | LEU | GLU | ASN | GLY | HIS | ||||
| 4 | GLU | ILE | LEU | ALA | HIS | VAL | SER | GLY | LYS | ILE | ||||
| 5 | ARG | MET | ASN | TYR | ILE | ARG | ILE | LEU | PRO | GLY | ||||
| 6 | ASP | LYS | VAL | THR | VAL | GLU | MET | SER | PRO | TYR | ||||
| 7 | ASP | LEU | THR | ARG | GLY | ARG | ILE | THR | TYR | ARG | ||||
| 8 | TYR | LYS |
Samples:
sample_1: PMSF 0.1 mM; EDTA 1 mM; sodium chloride 50 mM; MES 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts