BMRB Entry 26701
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26701
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: T-STAR KH domain PubMed: 26758068
Deposition date: 2015-11-04 Original release date: 2016-01-06
Authors: Feracci, Mikael; Dominguez, Cyril
Citation: Feracci, Mikael; Foot, Jaelle; Grellscheid, Sushma; Danilenko, Marina; Stehle, Ralf; Gonchar, Oksana; Kang, Hyun-Seo; Dalgliesh, Caroline; Meyer, Helge; Liu, Yilei; Lahat, Albert; Sattler, Michael; Eperon, Ian; Elliott, David; Dominguez, Cyril. "Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68" Nat. Commun. 7, 10355-10355 (2016).
Assembly members:
T_STAR, polymer, 113 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
Entity Sequences (FASTA):
T_STAR: GAINKNMKLGQKVLIPVKQF
PKFNFVGKLLGPRGNSLKRL
QEETLTKMSILGKGSMRDKA
KEEELRKSGEAKYFHLNDDL
HVLIEVFAPPAEAYARMGHA
LEEIKKFLIPDYN
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 101 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | KH domain | 1 |
Entities:
Entity 1, KH domain 113 residues - Formula weight is not available
residues 1 and 2 are non-native amino acids from the tag after Tev cleavage
| 1 | GLY | ALA | ILE | ASN | LYS | ASN | MET | LYS | LEU | GLY | ||||
| 2 | GLN | LYS | VAL | LEU | ILE | PRO | VAL | LYS | GLN | PHE | ||||
| 3 | PRO | LYS | PHE | ASN | PHE | VAL | GLY | LYS | LEU | LEU | ||||
| 4 | GLY | PRO | ARG | GLY | ASN | SER | LEU | LYS | ARG | LEU | ||||
| 5 | GLN | GLU | GLU | THR | LEU | THR | LYS | MET | SER | ILE | ||||
| 6 | LEU | GLY | LYS | GLY | SER | MET | ARG | ASP | LYS | ALA | ||||
| 7 | LYS | GLU | GLU | GLU | LEU | ARG | LYS | SER | GLY | GLU | ||||
| 8 | ALA | LYS | TYR | PHE | HIS | LEU | ASN | ASP | ASP | LEU | ||||
| 9 | HIS | VAL | LEU | ILE | GLU | VAL | PHE | ALA | PRO | PRO | ||||
| 10 | ALA | GLU | ALA | TYR | ALA | ARG | MET | GLY | HIS | ALA | ||||
| 11 | LEU | GLU | GLU | ILE | LYS | LYS | PHE | LEU | ILE | PRO | ||||
| 12 | ASP | TYR | ASN |
Samples:
sample_1: T_STAR, [U-15N], 0.5 ± 0.1 mM; T_STAR, [U-13C; U-15N], 1 ± 0.1 mM; H2O 93%; D2O 7%; sodium phosphate 20 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.110, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts