Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50151
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Citation: Kumari, Pooja; Bhavesh, Neel Sarovar. "Human DND1-RRM2 forms a non-canonical domain swapped dimer" Protein Sci. 30, 1184-1195 (2021).
PubMed: 33860980
Assembly members:
DND1-RRM2, polymer, 100 residues, 10553.19 Da.
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: pet28a
Entity Sequences (FASTA):
DND1-RRM2: MGSSHHHHHHSSGLVPRGSH
MELSVDGLPPNLTRSALLLA
LQPLGPGLQEARLLPSPGPA
PGQIALLKFSSHRAAAMAKK
ALVEGQSHLCGEQVAVEWLK
Data type | Count |
13C chemical shifts | 190 |
15N chemical shifts | 67 |
1H chemical shifts | 67 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | DND1-RRM2 | 1 |
Entity 1, DND1-RRM2 100 residues - 10553.19 Da.
Residue 1-21 belongs to hexa-histidine tag
1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | |
2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | |
3 | MET | GLU | LEU | SER | VAL | ASP | GLY | LEU | PRO | PRO | |
4 | ASN | LEU | THR | ARG | SER | ALA | LEU | LEU | LEU | ALA | |
5 | LEU | GLN | PRO | LEU | GLY | PRO | GLY | LEU | GLN | GLU | |
6 | ALA | ARG | LEU | LEU | PRO | SER | PRO | GLY | PRO | ALA | |
7 | PRO | GLY | GLN | ILE | ALA | LEU | LEU | LYS | PHE | SER | |
8 | SER | HIS | ARG | ALA | ALA | ALA | MET | ALA | LYS | LYS | |
9 | ALA | LEU | VAL | GLU | GLY | GLN | SER | HIS | LEU | CYS | |
10 | GLY | GLU | GLN | VAL | ALA | VAL | GLU | TRP | LEU | LYS |
sample_1_RRM2: DND1-RRM2, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 25 mM; sodium chloride 100 mM
sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1_RRM2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1_RRM2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1_RRM2 | isotropic | sample_conditions_1 |
3D HNCO | sample_1_RRM2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1_RRM2 | isotropic | sample_conditions_1 |
3D HNCA | sample_1_RRM2 | isotropic | sample_conditions_1 |
TOPSPIN v3.6.0, Bruker Biospin - chemical shift assignment, data analysis, peak picking
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