BMRB Entry 27671
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27671
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Amide chemical shifts of human HuR RRM3 PubMed: 30418581
Deposition date: 2018-10-31 Original release date: 2018-11-14
Authors: Pabis, Marta; Popowicz, Grzegorz; Schlundt, Andreas; Sattler, Michael
Citation: Pabis, Marta; Popowicz, Grzegorz; Stehle, Ralf; Fernandez-Ramos, David; Asami, Sam; Warner, Lisa; Garcia-Maurino, Sofia; Schlundt, Andreas; Martinez-Chantar, Maria; Diaz-Moreno, Irene; Sattler, Michael. "HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs." Nucleic Acids Res. 47, 1011-1029 (2019).
Assembly members:
HuR_RRM3, polymer, 87 residues, 9691.17 Da.
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 GST-1a
Entity Sequences (FASTA):
HuR_RRM3: GAMGWCIFIYNLGQDADEGI
LWQMFGPFGAVTNVKVIRDF
NTNKCKGFGFVTMTNYEEAA
MAIASLNGYRLGDKILQVSF
KTNKSHK
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 69 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HuR RRM3 | 1 |
Entities:
Entity 1, HuR RRM3 87 residues - 9691.17 Da.
GAM is from cloning
| 1 | GLY | ALA | MET | GLY | TRP | CYS | ILE | PHE | ILE | TYR | ||||
| 2 | ASN | LEU | GLY | GLN | ASP | ALA | ASP | GLU | GLY | ILE | ||||
| 3 | LEU | TRP | GLN | MET | PHE | GLY | PRO | PHE | GLY | ALA | ||||
| 4 | VAL | THR | ASN | VAL | LYS | VAL | ILE | ARG | ASP | PHE | ||||
| 5 | ASN | THR | ASN | LYS | CYS | LYS | GLY | PHE | GLY | PHE | ||||
| 6 | VAL | THR | MET | THR | ASN | TYR | GLU | GLU | ALA | ALA | ||||
| 7 | MET | ALA | ILE | ALA | SER | LEU | ASN | GLY | TYR | ARG | ||||
| 8 | LEU | GLY | ASP | LYS | ILE | LEU | GLN | VAL | SER | PHE | ||||
| 9 | LYS | THR | ASN | LYS | SER | HIS | LYS |
Samples:
sample_1: HuR RRM3, [U-13C; U-15N], 120 uM; sodium phosphate 20 mM; sodium chloride 200 mM; DTT 5 mM; EDTA 1 mM
sample_2: HuR RRM3, [U-15N; U-2H], 120 uM; sodium phosphate 20 mM; sodium chloride 200 mM; DTT 5 mM; EDTA 1 mM
sample_conditions_1: 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 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
CCPNMR_Analysis v2.4, CCPN - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts