BMRB Entry 27021

Name: 1H, 15N, 13C resonance assignment of the aortic medial amyloid protein medin in non-denaturing conditions.
Published: 2020-12-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27021

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
Medin: RLDKQGNFNAWVAGSYGNDQ WLQVDLGSSKEVTGIITQGA RNFGSVQFVA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	95
15N chemical shifts	48
1H chemical shifts	95

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

UNP	Q08431
AlphaFold	Q9BTL9

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

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