BMRB Entry 15229
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15229
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Title: ATOMIC STRUCTURE OF TRANSLATION INITIATION FACTOR aIF2 beta-SUBUNIT FROM ARCHAEBACTERIA SULFOLOBUS SOLFATARICUS: HIGH RESOLUTION NMR IN SOLUTION PubMed: 18004773
Deposition date: 2007-04-30 Original release date: 2008-02-20
Authors: Vasile, F.; Pechkova, E.; Stolboushkina, E.; Garber, M.; Nicolini, C.
Citation: Vasile, F.; Pechkova, E.; Nicolini, C.. "Solution structure of the beta-subunit of the translation initiation factor aIF2 from archaebacteria Sulfolobus solfataricus." Proteins 70, 1112-1115 (2008).
Assembly members:
Translation_initiation_factor_2_beta_subunit, polymer, 146 residues, 16799 Da.
Natural source: Common Name: Sulfolobus solfataricus Taxonomy ID: 2287 Superkingdom: Archaea Kingdom: not available Genus/species: Sulfolobus solfataricus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Translation_initiation_factor_2_beta_subunit: HHHHHHMGSSEKEYVEMLDR
LYSKLPEKGRKEGTQSLPNM
IILNIGNTTIIRNFAEYCDR
IRREDKICMKYLLKELAAPG
NVDDKGELVIQGKFSSQVIN
TLMERFLKAYVECSTCKSLD
TILKKEKKSWYIVCLACGAQ
TPVKPL
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 848 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit beta | 1 |
Entities:
Entity 1, subunit beta 146 residues - 16799 Da.
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | MET | GLY | SER | SER | ||||
| 2 | GLU | LYS | GLU | TYR | VAL | GLU | MET | LEU | ASP | ARG | ||||
| 3 | LEU | TYR | SER | LYS | LEU | PRO | GLU | LYS | GLY | ARG | ||||
| 4 | LYS | GLU | GLY | THR | GLN | SER | LEU | PRO | ASN | MET | ||||
| 5 | ILE | ILE | LEU | ASN | ILE | GLY | ASN | THR | THR | ILE | ||||
| 6 | ILE | ARG | ASN | PHE | ALA | GLU | TYR | CYS | ASP | ARG | ||||
| 7 | ILE | ARG | ARG | GLU | ASP | LYS | ILE | CYS | MET | LYS | ||||
| 8 | TYR | LEU | LEU | LYS | GLU | LEU | ALA | ALA | PRO | GLY | ||||
| 9 | ASN | VAL | ASP | ASP | LYS | GLY | GLU | LEU | VAL | ILE | ||||
| 10 | GLN | GLY | LYS | PHE | SER | SER | GLN | VAL | ILE | ASN | ||||
| 11 | THR | LEU | MET | GLU | ARG | PHE | LEU | LYS | ALA | TYR | ||||
| 12 | VAL | GLU | CYS | SER | THR | CYS | LYS | SER | LEU | ASP | ||||
| 13 | THR | ILE | LEU | LYS | LYS | GLU | LYS | LYS | SER | TRP | ||||
| 14 | TYR | ILE | VAL | CYS | LEU | ALA | CYS | GLY | ALA | GLN | ||||
| 15 | THR | PRO | VAL | LYS | PRO | LEU |
Samples:
sample: Translation initiation factor 2 beta subunit 0.6 mM; sodium phosphate 50 mM; NaCl 10 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0.2 M; pH: 8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D TOCSY | sample | isotropic | sample_conditions_1 |
| 2D NOESY | sample | isotropic | sample_conditions_1 |
Software:
xwinnmr v2.6, Bruker - collection
XEASY v1.3.13, P. Guntert and K. Wuthrich et al - data analysis
DYANA v1.5, P. Guntert and K. Wuthrich et al - structure solution
GROMACS v3.3.1, David van der Spoel et al. - refinement
NMR spectrometers:
- Bruker AMX 500 MHz