BMRB Entry 50509
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50509
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Title: Backbone and sidechain assignments of RRM1 domain of human RBM6
Deposition date: 2020-10-12 Original release date: 2020-10-16
Authors: Aggarwal, Priyanka; Bhavesh, Neel
Citation: Aggarwal, Priyanka; Bhavesh, Neel. "1H, 13C, 15N chemical shift assignments for RRM1 domain of human RBM6" The BMRB entry is the only known published source for the data..
Assembly members:
entity_1, polymer, 87 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: GAMGHMSRLIRLSGVPEDAT
KEEILNAFRTPDGMPVKNLQ
LKEYNTGYDYGYVCVEFSLL
EDAIGCMEANQGTLMIQDKE
VTLEYVS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 311 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 448 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RRM1 domain of human RBM6 | 1 |
Entities:
Entity 1, RRM1 domain of human RBM6 87 residues - Formula weight is not available
| 1 | GLY | ALA | MET | GLY | HIS | MET | SER | ARG | LEU | ILE | ||||
| 2 | ARG | LEU | SER | GLY | VAL | PRO | GLU | ASP | ALA | THR | ||||
| 3 | LYS | GLU | GLU | ILE | LEU | ASN | ALA | PHE | ARG | THR | ||||
| 4 | PRO | ASP | GLY | MET | PRO | VAL | LYS | ASN | LEU | GLN | ||||
| 5 | LEU | LYS | GLU | TYR | ASN | THR | GLY | TYR | ASP | TYR | ||||
| 6 | GLY | TYR | VAL | CYS | VAL | GLU | PHE | SER | LEU | LEU | ||||
| 7 | GLU | ASP | ALA | ILE | GLY | CYS | MET | GLU | ALA | ASN | ||||
| 8 | GLN | GLY | THR | LEU | MET | ILE | GLN | ASP | LYS | GLU | ||||
| 9 | VAL | THR | LEU | GLU | TYR | VAL | SER |
Samples:
sample_1: RBM6 RRM1 domain, [U-99% 13C; U-99% 15N], 1 ± 0.01 mM; Sodium Phosphate 50 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC aliphatic | 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.5pl6 - collection
CARA - data analysis
TOPSPIN v4.0.9 - data processing
NMR spectrometers:
- Bruker AVANCE III 500.15 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts