BMRB Entry 27499
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27499
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Title: SFRS1-RRM1
Deposition date: 2018-05-31 Original release date: 2018-07-31
Authors: Serrano, Pedro; Wuthrich, Kurt
Citation: Wuthrich, Kurt; Serrano, Pedro. "NMR assignments of the the protein SFRS1-RRM1" .
Assembly members:
SFRS1-RRM1, polymer, 111 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: pET28B
Entity Sequences (FASTA):
SFRS1-RRM1: GGSSGSSGMSGGGVIRGPAG
NNDCRIYVGNLPPDIRTKDI
EDVFYKYGAIRDIDLKNRRG
GPPFAFVEFEDPRDAEDAVY
GRDGYDYDGYRLRVEFPRSG
RGTGSGSGPSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 110 |
| 15N chemical shifts | 56 |
| 1H chemical shifts | 59 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | sfrs1-RRM1 | 1 |
Entities:
Entity 1, sfrs1-RRM1 111 residues - Formula weight is not available
| 1 | GLY | GLY | SER | SER | GLY | SER | SER | GLY | MET | SER | ||||
| 2 | GLY | GLY | GLY | VAL | ILE | ARG | GLY | PRO | ALA | GLY | ||||
| 3 | ASN | ASN | ASP | CYS | ARG | ILE | TYR | VAL | GLY | ASN | ||||
| 4 | LEU | PRO | PRO | ASP | ILE | ARG | THR | LYS | ASP | ILE | ||||
| 5 | GLU | ASP | VAL | PHE | TYR | LYS | TYR | GLY | ALA | ILE | ||||
| 6 | ARG | ASP | ILE | ASP | LEU | LYS | ASN | ARG | ARG | GLY | ||||
| 7 | GLY | PRO | PRO | PHE | ALA | PHE | VAL | GLU | PHE | GLU | ||||
| 8 | ASP | PRO | ARG | ASP | ALA | GLU | ASP | ALA | VAL | TYR | ||||
| 9 | GLY | ARG | ASP | GLY | TYR | ASP | TYR | ASP | GLY | TYR | ||||
| 10 | ARG | LEU | ARG | VAL | GLU | PHE | PRO | ARG | SER | GLY | ||||
| 11 | ARG | GLY | THR | GLY | SER | GLY | SER | GLY | PRO | SER | ||||
| 12 | SER |
Samples:
sample_1: SFRS1-RRM1, [U-99% 13C; U-99% 15N], 0.5 mM; D2O, [U-99% 2H], 5%; sodium azide 0.1%; sodium chloride 150 mM; sodium phosphate 25 mM
sample_conditions_1: ionic strength: 0.02 M; 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| APSY CACBCoNH | sample_1 | isotropic | sample_conditions_1 |
| APSY HACANH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Braun and Wuthrich - structure solution
NMR spectrometers:
- 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