BMRB Entry 26576

Name: 1H, 15N, resonance assignment of the aortic medial amyloid protein medin in non-denaturing conditions.
Published: 2015-09-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26576

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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, resonance assignment of the aortic medial amyloid protein medin in non-denaturing conditions.

Deposition date:

2015-05-11

Original release date:

2015-09-22

Authors:

Davies, Hannah; Phelan, Marie; Madine, Jilllian

Citation:

Citation: Davies, Hannah; Phelan, Marie; Madine, Jilllian. "1H, 15N and 13C assignment of the amyloidogenic protein medin using fast-pulsing NMR techniques" Biomol. NMR Assign. 10, 75-77 (2016).
PubMed: 26377205

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
15N chemical shifts	44
1H chemical shifts	44

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], 20 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: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

Analysis, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 800 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