BMRB Entry 27021

Title:
1H, 15N, 13C resonance assignment of the aortic medial amyloid protein medin in non-denaturing conditions.
Deposition date:
2017-02-02
Original release date:
2020-12-21
Authors:
Davies, Hannah; Phelan, Marie; Madine, Jilllian
Citation:

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).
PubMed: 28327552

Assembly members:

Assembly members:
Medin, polymer, 50 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pOPINS

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts95
15N chemical shifts48
1H chemical shifts95

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Medin1

Entities:

Entity 1, Medin 50 residues - Formula weight is not available

1   ARGLEUASPLYSGLNGLYASNPHEASNALA
2   TRPVALALAGLYSERTYRGLYASNASPGLN
3   TRPLEUGLNVALASPLEUGLYSERSERLYS
4   GLUVALTHRGLYILEILETHRGLNGLYALA
5   ARGASNPHEGLYSERVALGLNPHEVALALA

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 13C(direct)-13C CACOsample_1isotropicsample_conditions_1
2D 13C(direct)-15N CONsample_1isotropicsample_conditions_1
2D 1H-1H HAHNsample_1isotropicsample_conditions_1
2D 1H-13C HNCOsample_1isotropicsample_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

Related Database Links:

UNP Q08431
AlphaFold Q9BTL9

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks