BMRB Entry 25885
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25885
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Title: RBM24 RRM domain PubMed: 27002326
Deposition date: 2015-11-09 Original release date: 2016-06-15
Authors: Upadhyay, Santosh Kumar; Mackereth, Cameron
Citation: Upadhyay, Santosh Kumar; Mackereth, Cameron. "1H, 15N and 13C backbone and side chain resonance assignments of the RRM domain from human RBM24" Biomol. NMR Assign. 10, 237-240 (2016).
Assembly members:
RBM24, polymer, 105 residues, Formula weight is not available
Natural source: Common Name: humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RBM24: GAMAHTTQKDTTYTKIFVGG
LPYHTTDASLRKYFEVFGEI
EEAVVITDRQTGKSRGYGFV
TMADRAAAERACKDPNPIID
GRKANVNLAYLGAKPRIMQP
GFAFG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 450 |
15N chemical shifts | 104 |
1H chemical shifts | 708 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RBM24 | 1 |
Entities:
Entity 1, RBM24 105 residues - Formula weight is not available
The N-terminal Gly-Ala-Met-Ala remains following removal of the His6-tag by TEV potease
1 | GLY | ALA | MET | ALA | HIS | THR | THR | GLN | LYS | ASP | ||||
2 | THR | THR | TYR | THR | LYS | ILE | PHE | VAL | GLY | GLY | ||||
3 | LEU | PRO | TYR | HIS | THR | THR | ASP | ALA | SER | LEU | ||||
4 | ARG | LYS | TYR | PHE | GLU | VAL | PHE | GLY | GLU | ILE | ||||
5 | GLU | GLU | ALA | VAL | VAL | ILE | THR | ASP | ARG | GLN | ||||
6 | THR | GLY | LYS | SER | ARG | GLY | TYR | GLY | PHE | VAL | ||||
7 | THR | MET | ALA | ASP | ARG | ALA | ALA | ALA | GLU | ARG | ||||
8 | ALA | CYS | LYS | ASP | PRO | ASN | PRO | ILE | ILE | ASP | ||||
9 | GLY | ARG | LYS | ALA | ASN | VAL | ASN | LEU | ALA | TYR | ||||
10 | LEU | GLY | ALA | LYS | PRO | ARG | ILE | MET | GLN | PRO | ||||
11 | GLY | PHE | ALA | PHE | GLY |
Samples:
sample_1: RBM24, [U-99% 13C; U-99% 15N], 0.25 mM; sodium phosphate 20 mM; sodium chloride 300 mM; H2O 90%; D2O 10%
sample_2: RBM24, [U-10% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O 100%
sample_conditions_1: ionic strength: 320 mM; pH: 6.5; 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-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCC(CO)-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCC(CO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC CT | sample_2 | isotropic | sample_conditions_1 |
D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - Visualisation, collection
NMRPipe v2014, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.115, Goddard - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
- 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