BMRB Entry 11599
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11599
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Title: NMR structure of eIF1
Deposition date: 2015-10-16 Original release date: 2016-10-20
Authors: NAGATA, Takashi; OBAYASHI, Eiji; ASANO, Katsura
Citation: NAGATA, Takashi; OBAYASHI, Eiji. "NMR structure of eIF1" Not known ., .-..
Assembly members:
eIF1, polymer, 108 residues, 12330.247 Da.
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
Entity Sequences (FASTA):
eIF1: MSIENLKSFDPFADTGDDET
ATSNYIHIRIQQRNGRKTLT
TVQGVPEEYDLKRILKVLKK
DFACNGNIVKDPEMGEIIQL
QGDQRAKVCEFMISQLGLQK
KNIKIHGF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 473 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 738 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | eIF1 | 1 |
Entities:
Entity 1, eIF1 108 residues - 12330.247 Da.
| 1 | MET | SER | ILE | GLU | ASN | LEU | LYS | SER | PHE | ASP | ||||
| 2 | PRO | PHE | ALA | ASP | THR | GLY | ASP | ASP | GLU | THR | ||||
| 3 | ALA | THR | SER | ASN | TYR | ILE | HIS | ILE | ARG | ILE | ||||
| 4 | GLN | GLN | ARG | ASN | GLY | ARG | LYS | THR | LEU | THR | ||||
| 5 | THR | VAL | GLN | GLY | VAL | PRO | GLU | GLU | TYR | ASP | ||||
| 6 | LEU | LYS | ARG | ILE | LEU | LYS | VAL | LEU | LYS | LYS | ||||
| 7 | ASP | PHE | ALA | CYS | ASN | GLY | ASN | ILE | VAL | LYS | ||||
| 8 | ASP | PRO | GLU | MET | GLY | GLU | ILE | ILE | GLN | LEU | ||||
| 9 | GLN | GLY | ASP | GLN | ARG | ALA | LYS | VAL | CYS | GLU | ||||
| 10 | PHE | MET | ILE | SER | GLN | LEU | GLY | LEU | GLN | LYS | ||||
| 11 | LYS | ASN | ILE | LYS | ILE | HIS | GLY | PHE |
Samples:
sample_1: eIF1, [U-100% 13C; U-100% 15N], 0.4 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; D2O, [U-2H], 5%; H2O 95%
sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | 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 |
Software:
AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution
Kujira v0.984, Naohira Kobayashi - chemical shift assignment, data analysis, peak picking
NMRView, Johnson - collection, data analysis, peak picking
NMRDraw, Delaglio - processing
NMRPipe, Delaglio - processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts