BMRB Entry 28121
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28121
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Title: Assignment of first 249 residues of yeast eIF4G1 PubMed: 36213119
Deposition date: 2020-05-15 Original release date: 2022-10-27
Authors: Chaves-Arquero, Belen; Martinez-Lumbreras, Santiago; Perez-Canadillas, Jose Manuel
Citation: Chaves-Arquero, Belen; Martinez-Lumbreras, Santiago; Sibille, Nathalie; Camero, Sergio; Bernado, Pau; Jimenez, Maria Angeles; Zorrilla, Silvia; Perez-Canadillas, Jose Manuel. "eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly" Front. Mol. Biosci. 9, 986121-986121 (2022).
Assembly members:
eIF4G1, polymer, 249 residues, Formula weight is not available
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28
Entity Sequences (FASTA):
eIF4G1: MTDETAHPTQSASKQESAAL
KQTGDDQQESQQQRGYTNYN
NGSNYTQKKPYNSNRPHQQR
GGKFGPNRYNNRGNYNGGGS
FRGGHMGANSSNVPWTGYYN
NYPVYYQPQQMAAAGSAPAN
PIPVEEKSPVPTKIEITTKS
GEHLDLKEQHKAKLQSQERS
TVSPQPESKLKETSDSTSTS
TPTPTPSTNDSKASSEENIS
EAEKTRRNFIEQVKLRKAAL
EKKRKEQLEGSSGNNNIPMK
TTPENVEEK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 721 |
| 15N chemical shifts | 249 |
| 1H chemical shifts | 734 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | eIF4G1 | 1 |
Entities:
Entity 1, eIF4G1 249 residues - Formula weight is not available
| 1 | MET | THR | ASP | GLU | THR | ALA | HIS | PRO | THR | GLN | ||||
| 2 | SER | ALA | SER | LYS | GLN | GLU | SER | ALA | ALA | LEU | ||||
| 3 | LYS | GLN | THR | GLY | ASP | ASP | GLN | GLN | GLU | SER | ||||
| 4 | GLN | GLN | GLN | ARG | GLY | TYR | THR | ASN | TYR | ASN | ||||
| 5 | ASN | GLY | SER | ASN | TYR | THR | GLN | LYS | LYS | PRO | ||||
| 6 | TYR | ASN | SER | ASN | ARG | PRO | HIS | GLN | GLN | ARG | ||||
| 7 | GLY | GLY | LYS | PHE | GLY | PRO | ASN | ARG | TYR | ASN | ||||
| 8 | ASN | ARG | GLY | ASN | TYR | ASN | GLY | GLY | GLY | SER | ||||
| 9 | PHE | ARG | GLY | GLY | HIS | MET | GLY | ALA | ASN | SER | ||||
| 10 | SER | ASN | VAL | PRO | TRP | THR | GLY | TYR | TYR | ASN | ||||
| 11 | ASN | TYR | PRO | VAL | TYR | TYR | GLN | PRO | GLN | GLN | ||||
| 12 | MET | ALA | ALA | ALA | GLY | SER | ALA | PRO | ALA | ASN | ||||
| 13 | PRO | ILE | PRO | VAL | GLU | GLU | LYS | SER | PRO | VAL | ||||
| 14 | PRO | THR | LYS | ILE | GLU | ILE | THR | THR | LYS | SER | ||||
| 15 | GLY | GLU | HIS | LEU | ASP | LEU | LYS | GLU | GLN | HIS | ||||
| 16 | LYS | ALA | LYS | LEU | GLN | SER | GLN | GLU | ARG | SER | ||||
| 17 | THR | VAL | SER | PRO | GLN | PRO | GLU | SER | LYS | LEU | ||||
| 18 | LYS | GLU | THR | SER | ASP | SER | THR | SER | THR | SER | ||||
| 19 | THR | PRO | THR | PRO | THR | PRO | SER | THR | ASN | ASP | ||||
| 20 | SER | LYS | ALA | SER | SER | GLU | GLU | ASN | ILE | SER | ||||
| 21 | GLU | ALA | GLU | LYS | THR | ARG | ARG | ASN | PHE | ILE | ||||
| 22 | GLU | GLN | VAL | LYS | LEU | ARG | LYS | ALA | ALA | LEU | ||||
| 23 | GLU | LYS | LYS | ARG | LYS | GLU | GLN | LEU | GLU | GLY | ||||
| 24 | SER | SER | GLY | ASN | ASN | ASN | ILE | PRO | MET | LYS | ||||
| 25 | THR | THR | PRO | GLU | ASN | VAL | GLU | GLU | LYS |
Samples:
sample_1: eIF4G1, [U-100% 13C; U-100% 15N], 200 uM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 301.2 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CCPNanalysis, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts