BMRB Entry 52233
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52233
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Fatalska, Agnieszka; Hodgson, George; Freund, Stefan; Maslen, Sarah; Morgan, Tomos; Thorkelsson, Sigurdur; van Slegtenhorst, Marjon; Lorenz, Sonja; Andreeva, Antonina; Kaat, Laura Donker; Bertolotti, Anne. "Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B" Mol. Cell 84, 506-521 (2024).
PubMed: 38159565
Assembly members:
entity_1, polymer, 199 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-47b
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 454 |
| 15N chemical shifts | 174 |
| 1H chemical shifts | 174 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PPP1R15B | 1 |
Entities:
Entity 1, PPP1R15B 199 residues - Formula weight is not available
| 1 | ILE | SER | ALA | ARG | PRO | ALA | CYS | SER | ASN | LYS | ||||
| 2 | LEU | ILE | ASP | TYR | ILE | LEU | GLY | GLY | ALA | SER | ||||
| 3 | SER | ASP | LEU | GLU | THR | SER | SER | ASP | PRO | GLU | ||||
| 4 | GLY | GLU | ASP | TRP | ASP | GLU | GLU | ALA | GLU | ASP | ||||
| 5 | ASP | GLY | PHE | ASP | SER | ASP | SER | SER | LEU | SER | ||||
| 6 | ASP | SER | ASP | LEU | GLU | GLN | ASP | PRO | GLU | GLY | ||||
| 7 | LEU | HIS | LEU | TRP | ASN | SER | PHE | CYS | SER | VAL | ||||
| 8 | ASP | PRO | TYR | ASN | PRO | GLN | ASN | PHE | THR | ALA | ||||
| 9 | THR | ILE | GLN | THR | ALA | ALA | ARG | ILE | VAL | PRO | ||||
| 10 | GLU | GLU | PRO | SER | ASP | SER | GLU | LYS | ASP | LEU | ||||
| 11 | SER | GLY | LYS | SER | ASP | LEU | GLU | ASN | SER | SER | ||||
| 12 | GLN | SER | GLY | SER | LEU | PRO | GLU | THR | PRO | GLU | ||||
| 13 | HIS | SER | SER | GLY | GLU | GLU | ASP | ASP | TRP | GLU | ||||
| 14 | SER | SER | ALA | ASP | GLU | ALA | GLU | SER | LEU | LYS | ||||
| 15 | LEU | TRP | ASN | SER | PHE | CYS | ASN | SER | ASP | ASP | ||||
| 16 | PRO | TYR | ASN | PRO | LEU | ASN | PHE | LYS | ALA | PRO | ||||
| 17 | PHE | GLN | THR | SER | GLY | GLU | ASN | GLU | LYS | GLY | ||||
| 18 | CYS | ARG | ASP | SER | LYS | THR | PRO | SER | GLU | SER | ||||
| 19 | ILE | VAL | ALA | ILE | SER | GLU | CYS | HIS | THR | LEU | ||||
| 20 | LEU | SER | CYS | LYS | VAL | GLN | LEU | LEU | GLY |
Samples:
sample_1: PPP1R15B, [U-98% 13C; U-98% 15N], 150 uM; DTT 10 mM; sodium chloride 150 mM; HEPES 50 mM; D2O 5%
sample_2: PPP1R15B, [U-100% 15N], 150 uM; DTT 10 mM; sodium chloride 150 mM; HEPES 50 mM; D2O 5%
sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 281.5K K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.6.0 - collection, processing
NMRFAM-SPARKY v1.3 - data analysis
qMDD v2.7 - processing
MARS v2.1 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 800 MHz
- Bruker AVANCE II+ 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks