BMRB Entry 51057
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51057
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Soni, Komal; Jagtap, Pravin Kumar Ankush; Martinez-Lumbreras, Santiago; Bonnal, Sophie; Geerlof, Arie; Stehle, Ralf; Simon, Bernd; Valcarcel, Juan; Sattler, Michael. "Structural basis for specific RNA recognition by the alternative splicing factor RBM5" Nat. Commun. 14, 4233-4233 (2023).
PubMed: 37454201
Assembly members:
entity_1, polymer, 95 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: pETM11
Entity Sequences (FASTA):
entity_1: GAMGERESKTIMLRGLPTTI
TESDIREMMESFEGPQPADV
RLMKRKTGVSRGFAFVEFYH
LQDATSWMEANQKKLVIQGK
HIAMHYSNPRPKFED
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 181 |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 86 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RRM1 | 1 |
Entities:
Entity 1, RRM1 95 residues - Formula weight is not available
| 1 | GLY | ALA | MET | GLY | GLU | ARG | GLU | SER | LYS | THR | ||||
| 2 | ILE | MET | LEU | ARG | GLY | LEU | PRO | THR | THR | ILE | ||||
| 3 | THR | GLU | SER | ASP | ILE | ARG | GLU | MET | MET | GLU | ||||
| 4 | SER | PHE | GLU | GLY | PRO | GLN | PRO | ALA | ASP | VAL | ||||
| 5 | ARG | LEU | MET | LYS | ARG | LYS | THR | GLY | VAL | SER | ||||
| 6 | ARG | GLY | PHE | ALA | PHE | VAL | GLU | PHE | TYR | HIS | ||||
| 7 | LEU | GLN | ASP | ALA | THR | SER | TRP | MET | GLU | ALA | ||||
| 8 | ASN | GLN | LYS | LYS | LEU | VAL | ILE | GLN | GLY | LYS | ||||
| 9 | HIS | ILE | ALA | MET | HIS | TYR | SER | ASN | PRO | ARG | ||||
| 10 | PRO | LYS | PHE | GLU | ASP |
Samples:
sample_1: RBM5 RRM1, [U-100% 13C; U-100% 15N], 300 uM; D2O 10%; MES 20 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment
NMRPipe - processing
TOPSPIN - collection
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks