BMRB Entry 53386
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53386
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: von Ehr, Julian; Schlundt, Andreas. "1H, 13C, 15N backbone chemical shift assignments and relaxation analysis of the single and tandem RRMs of the human serine-arginine rich splicing factor 6 (SRSF6)" J. Magn. Reson. ., .-..
Assembly members:
entity_1, polymer, 103 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: JvE-AH_09
Entity Sequences (FASTA):
entity_1: SGGGGYSSRRTSGRDKYGPP
VRTEYRLIVENLSSRCSAQD
LKDFMRQAGEVTYADAHKER
TNEGVIEFRSYSDMKRALDK
LDGTEINGRNIRLIEDKPRT
SHR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 276 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | extRRM2 W123A | 1 |
Entities:
Entity 1, extRRM2 W123A 103 residues - Formula weight is not available
SRSF6 residues 86-188 (based on Uniprot entry Q13247-1) with W123A mutation
| 1 | SER | GLY | GLY | GLY | GLY | TYR | SER | SER | ARG | ARG | ||||
| 2 | THR | SER | GLY | ARG | ASP | LYS | TYR | GLY | PRO | PRO | ||||
| 3 | VAL | ARG | THR | GLU | TYR | ARG | LEU | ILE | VAL | GLU | ||||
| 4 | ASN | LEU | SER | SER | ARG | CYS | SER | ALA | GLN | ASP | ||||
| 5 | LEU | LYS | ASP | PHE | MET | ARG | GLN | ALA | GLY | GLU | ||||
| 6 | VAL | THR | TYR | ALA | ASP | ALA | HIS | LYS | GLU | ARG | ||||
| 7 | THR | ASN | GLU | GLY | VAL | ILE | GLU | PHE | ARG | SER | ||||
| 8 | TYR | SER | ASP | MET | LYS | ARG | ALA | LEU | ASP | LYS | ||||
| 9 | LEU | ASP | GLY | THR | GLU | ILE | ASN | GLY | ARG | ASN | ||||
| 10 | ILE | ARG | LEU | ILE | GLU | ASP | LYS | PRO | ARG | THR | ||||
| 11 | SER | HIS | ARG |
Samples:
sample_1: extRRM2 W123A, [U-99% 13C; U-99% 15N], 400 uM; sodium phosphate 25 mM; sodium chloride 150 mM; l-arginine 50 mM; l-glutatmate 50 mM; DTT 2 mM
sample_conditions_1: 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 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.6 - 4.4 - collection, processing
ANALYSIS v2.5.2 - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker AVANCE NEO 600 MHz
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks