BMRB Entry 30375
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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/BMR30375
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Title: Structure of two-domain translational regulator Yih1 reveals a possible mechanism of action
Deposition date: 2017-11-27 Original release date: 2018-11-19
Authors: Harjes, E.; Jameson, G.; Edwards, P.; Goroncy, A.; Loo, T.; Norris, G.
Citation: Harjes, E.; Jameson, G.; Tu, J.; Burr, N.; Loo, T.; Goroncy, A.; Edwards, P.; Harjjes, S.; Sattlegger, E.; Norris, G.. "Structure of two-domain translational regulator Yih1 reveals a possible mechanism of action." . ., .-..
Assembly members:
entity_1, polymer, 258 residues, 29047.422 Da.
Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MDDDHEQLVEELEAVEAIYP
DLLSKKQEDGSIIVVKVPQH
EYMTLQISFPTHYPSEEAPN
VIEVGVCTSLAKRDLYDTKY
LQHLFQEVMDSVFHRGSVCL
FDFLTELDGVLYVEPEEETE
PVQQSDIPTDPFEGWTASDP
ITDRGSTFMAFAAHVTSEEQ
AFAMLDLLKTDSKMRKANHV
MSAWRIKQDGSAATYQDSDD
DGETAAGSRMLHLITIMDVW
NVIVVVARWFGGAHIGPDRF
KHINSTAREAVVRAGFDS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 921 |
| 15N chemical shifts | 244 |
| 1H chemical shifts | 1517 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 258 residues - 29047.422 Da.
| 1 | MET | ASP | ASP | ASP | HIS | GLU | GLN | LEU | VAL | GLU | ||||
| 2 | GLU | LEU | GLU | ALA | VAL | GLU | ALA | ILE | TYR | PRO | ||||
| 3 | ASP | LEU | LEU | SER | LYS | LYS | GLN | GLU | ASP | GLY | ||||
| 4 | SER | ILE | ILE | VAL | VAL | LYS | VAL | PRO | GLN | HIS | ||||
| 5 | GLU | TYR | MET | THR | LEU | GLN | ILE | SER | PHE | PRO | ||||
| 6 | THR | HIS | TYR | PRO | SER | GLU | GLU | ALA | PRO | ASN | ||||
| 7 | VAL | ILE | GLU | VAL | GLY | VAL | CYS | THR | SER | LEU | ||||
| 8 | ALA | LYS | ARG | ASP | LEU | TYR | ASP | THR | LYS | TYR | ||||
| 9 | LEU | GLN | HIS | LEU | PHE | GLN | GLU | VAL | MET | ASP | ||||
| 10 | SER | VAL | PHE | HIS | ARG | GLY | SER | VAL | CYS | LEU | ||||
| 11 | PHE | ASP | PHE | LEU | THR | GLU | LEU | ASP | GLY | VAL | ||||
| 12 | LEU | TYR | VAL | GLU | PRO | GLU | GLU | GLU | THR | GLU | ||||
| 13 | PRO | VAL | GLN | GLN | SER | ASP | ILE | PRO | THR | ASP | ||||
| 14 | PRO | PHE | GLU | GLY | TRP | THR | ALA | SER | ASP | PRO | ||||
| 15 | ILE | THR | ASP | ARG | GLY | SER | THR | PHE | MET | ALA | ||||
| 16 | PHE | ALA | ALA | HIS | VAL | THR | SER | GLU | GLU | GLN | ||||
| 17 | ALA | PHE | ALA | MET | LEU | ASP | LEU | LEU | LYS | THR | ||||
| 18 | ASP | SER | LYS | MET | ARG | LYS | ALA | ASN | HIS | VAL | ||||
| 19 | MET | SER | ALA | TRP | ARG | ILE | LYS | GLN | ASP | GLY | ||||
| 20 | SER | ALA | ALA | THR | TYR | GLN | ASP | SER | ASP | ASP | ||||
| 21 | ASP | GLY | GLU | THR | ALA | ALA | GLY | SER | ARG | MET | ||||
| 22 | LEU | HIS | LEU | ILE | THR | ILE | MET | ASP | VAL | TRP | ||||
| 23 | ASN | VAL | ILE | VAL | VAL | VAL | ALA | ARG | TRP | PHE | ||||
| 24 | GLY | GLY | ALA | HIS | ILE | GLY | PRO | ASP | ARG | PHE | ||||
| 25 | LYS | HIS | ILE | ASN | SER | THR | ALA | ARG | GLU | ALA | ||||
| 26 | VAL | VAL | ARG | ALA | GLY | PHE | ASP | SER |
Samples:
sample_1: Yih1 (Yeast Impact Homologue), [U-13C; U-15N], 1 mM
sample_conditions_1: ionic strength: 30 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts