BMRB Entry 27926
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR27926
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Citation: Brooks, Rhiannon; Dixon, Ann. "Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum" Biochim. Biophys. Acta Biomembr. 1862, 183160-183160 (2020).
PubMed: 31874147
Assembly members:
RTNLB13, polymer, 16 residues, Formula weight is not available
Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
RTNLB13: EYGDQIQKHLGSLKDK
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 1H chemical shifts | 88 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | R13-APH16 | 1 |
Entities:
Entity 1, R13-APH16 16 residues - Formula weight is not available
| 1 | GLU | TYR | GLY | ASP | GLN | ILE | GLN | LYS | HIS | LEU | ||||
| 2 | GLY | SER | LEU | LYS | ASP | LYS |
Samples:
sample_1: RTNLB13 APH peptide 1 mM; DPC-d38 50 mM; sodium phosphate 25 mM
sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CCPNmr_Analysis v2.4, CCPN - chemical shift assignment
TOPSPIN v3.2, Bruker BioSpin - collection, processing
NMR spectrometers:
- Bruker Avance 700 MHz