BMRB Entry 53766
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53766
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Krall, Jeffrey; Beck, Lily; Nichols, Parker; Vicens, Quentin; Henen, Morkos; Vogeli, Beat. "ZBP1's Inability to Convert Unmodified RNAs to the Z-form Underlies a Balanced Mechanism of RNA Recognition with ADAR1." bioRxiv ., .-. (2026).
PubMed: 42079158
Assembly members:
entity_1, polymer, 63 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: pET28(+)
Entity Sequences (FASTA):
entity_1: QFSQQREEDIYRFLKDNGPQ
RALVIAQALGMRTAKDVNRD
LYRMKSRHLLDMDEQSKAWT
IYR
- heteronucl_T1_relaxation
- heteronucl_T1rho_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| T1 relaxation values | 61 |
| T1rho relaxation values | 61 |
| T2 relaxation values | 61 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Za2-ZBP1 | 1 |
Entities:
Entity 1, Za2-ZBP1 63 residues - Formula weight is not available
The sequence starts at residue 104, which is the actual start of the Za2 domain of the human ZBP1 protein.
| 1 | GLN | PHE | SER | GLN | GLN | ARG | GLU | GLU | ASP | ILE | ||||
| 2 | TYR | ARG | PHE | LEU | LYS | ASP | ASN | GLY | PRO | GLN | ||||
| 3 | ARG | ALA | LEU | VAL | ILE | ALA | GLN | ALA | LEU | GLY | ||||
| 4 | MET | ARG | THR | ALA | LYS | ASP | VAL | ASN | ARG | ASP | ||||
| 5 | LEU | TYR | ARG | MET | LYS | SER | ARG | HIS | LEU | LEU | ||||
| 6 | ASP | MET | ASP | GLU | GLN | SER | LYS | ALA | TRP | THR | ||||
| 7 | ILE | TYR | ARG |
Samples:
sample_1: Za2-ZBP1, [U-100% 15N], 500 uM; potassium phosphate 20 mM; NaCl 100 mM; DTT 1 mM; EDTA 0.5 mM
sample_conditions_1: ionic strength: 120 mM; pH: 6.4; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| T1/R1 relaxation | sample_1 | isotropic | sample_conditions_1 |
| T1rho/R1rho relaxation | sample_1 | isotropic | sample_conditions_1 |
| T2/R2 relaxation | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR - chemical shift assignment
TOPSPIN - collection
MATLAB - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz