BMRB Entry 27021
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27021
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Title: 1H, 15N, 13C resonance assignment of the aortic medial amyloid protein medin in non-denaturing conditions. PubMed: 28327552
Deposition date: 2017-02-02 Original release date: 2020-12-21
Authors: Davies, Hannah; Phelan, Marie; Madine, Jilllian
Citation: Davies, Hannah; Rigden, Daniel; Phelan, Marie; Madine, Jillian. "Probing Medin Monomer Structure and its Amyloid Nucleation Using 13 C-Direct Detection NMR in Combination with Structural Bioinformatics" Sci. Rep. 7, 45224-45224 (2017).
Assembly members:
Medin, polymer, 50 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: pOPINS
Entity Sequences (FASTA):
Medin: RLDKQGNFNAWVAGSYGNDQ
WLQVDLGSSKEVTGIITQGA
RNFGSVQFVA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 95 |
| 15N chemical shifts | 48 |
| 1H chemical shifts | 95 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Medin | 1 |
Entities:
Entity 1, Medin 50 residues - Formula weight is not available
| 1 | ARG | LEU | ASP | LYS | GLN | GLY | ASN | PHE | ASN | ALA | |
| 2 | TRP | VAL | ALA | GLY | SER | TYR | GLY | ASN | ASP | GLN | |
| 3 | TRP | LEU | GLN | VAL | ASP | LEU | GLY | SER | SER | LYS | |
| 4 | GLU | VAL | THR | GLY | ILE | ILE | THR | GLN | GLY | ALA | |
| 5 | ARG | ASN | PHE | GLY | SER | VAL | GLN | PHE | VAL | ALA |
Samples:
sample_1: Medin, [U-98% 13C; U-98% 15N], 80 uM; sodium chloride 20 mM; sodium phosphate 20 mM; TSP, [U-2H], 2 uM
sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C(direct)-13C CACO | sample_1 | isotropic | sample_conditions_1 |
| 2D 13C(direct)-15N CON | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H HAHN | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
Analysis v2.4.2, CCPN - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- 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