BMRB Entry 11372
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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/BMR11372
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Title: Assigned chemical shifts of the second RNA recognition motif (RRM) of TIA-1, K138A mutant PubMed: 18500819
Deposition date: 2010-09-08 Original release date: 2010-11-30
Authors: Takahashi, M.; Kuwasako, K.; Abe, C.; Tsuda, K.; Inoue, M.; Terada, T.; Shirouzu, M.; Kobayashi, N.; Kigawa, T.; Taguchi, S.; Guntert, P.; Hayashizaki, Y.; Tanaka, A.; Muto, Y.; Yokoyama, S.
Citation: Kuwasako, Kanako; Takahashi, Mari; Tochio, Naoya; Abe, Chikage; Tsuda, Kengo; Inoue, Makoto; Terada, Takaho; Shirouzu, Mikako; Kobayashi, Naohiro; Kigawa, Takanori; Taguchi, Seiichi; Tanaka, Akiko; Hayashizaki, Yoshihide; Guntert, Peter; Muto, Yutaka; Yokoyama, Shigeyuki. "Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode." Biochemistry 47, 6437-6450 (2008).
Assembly members:
RRM domain K138A mutant, polymer, 103 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: cell free synthesis Host organism: Escherichia coli
Entity Sequences (FASTA):
RRM domain K138A mutant: GQKKDTSNHFHVFVGDLSPE
ITTEDIKAAFAPFGRISDAR
VVKDMATGKSAGYGFVSFFN
KWDAENAIQQMGGQWLGGRQ
IRTNWATRKPPAPKSTYESN
TKQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 293 |
| 15N chemical shifts | 95 |
| 1H chemical shifts | 95 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RRM domain K138A mutant | 1 |
Entities:
Entity 1, RRM domain K138A mutant 103 residues - Formula weight is not available
| 1 | GLY | GLN | LYS | LYS | ASP | THR | SER | ASN | HIS | PHE | ||||
| 2 | HIS | VAL | PHE | VAL | GLY | ASP | LEU | SER | PRO | GLU | ||||
| 3 | ILE | THR | THR | GLU | ASP | ILE | LYS | ALA | ALA | PHE | ||||
| 4 | ALA | PRO | PHE | GLY | ARG | ILE | SER | ASP | ALA | ARG | ||||
| 5 | VAL | VAL | LYS | ASP | MET | ALA | THR | GLY | LYS | SER | ||||
| 6 | ALA | GLY | TYR | GLY | PHE | VAL | SER | PHE | PHE | ASN | ||||
| 7 | LYS | TRP | ASP | ALA | GLU | ASN | ALA | ILE | GLN | GLN | ||||
| 8 | MET | GLY | GLY | GLN | TRP | LEU | GLY | GLY | ARG | GLN | ||||
| 9 | ILE | ARG | THR | ASN | TRP | ALA | THR | ARG | LYS | PRO | ||||
| 10 | PRO | ALA | PRO | LYS | SER | THR | TYR | GLU | SER | ASN | ||||
| 11 | THR | LYS | GLN |
Samples:
sample_1: RRM domain K138A mutant, [U-99% 13C; U-99% 15N], 1 mM; TRIS, [U-99% 2H], 20 mM; sodium chloride 100 mM; DTT, [U-98% 2H], 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | condition_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | condition_1 |
Software:
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement, structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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