BMRB Entry 50996

Name: SDS-Micelle bound alpha-Synuclein
Published: 2023-04-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50996

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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: SDS-Micelle bound alpha-Synuclein PubMed: 37027427

Deposition date: 2021-06-29 Original release date: 2023-04-05

Authors: Schwarz, Thomas; Ledolter, Karin; Kontaxis, Georg; Konrat, Robert

Citation: Schwarz, Thomas; Beier, Andreas; Ledolter, Karin; Gossenreiter, Thomas; Hofurthner, Theresa; Hartl, Markus; Baker, Terry; Taylor, Richard; Konrat, Robert. "High-Resolution Structural Information of Membrane-bound alpha-Synuclein provides Insight into the MoA of the Anti-Parkinson Drug UCB0599" Proc. Nat. Acad. Sci. 120, e2201910120-e2201910120 (2023).

Assembly members:
entity_1, polymer, 140 residues, Formula weight is not available
entity_SDS, non-polymer, 266.397 Da.

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: pET-3d

Entity Sequences (FASTA):
entity_1: MDVFMKGLSKAKEGVVAAAE KTKQGVAEAAGKTKEGVLYV GSKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQK TVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	399
15N chemical shifts	133
1H chemical shifts	133

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	aSyn	1
2	SDS	2

Entities:

Entity 1, aSyn 140 residues - Formula weight is not available

WT protein expressed without tag, sequence numbering from first expressed residue.

1	MET	ASP	VAL	PHE	MET	LYS	GLY	LEU	SER	LYS
2	ALA	LYS	GLU	GLY	VAL	VAL	ALA	ALA	ALA	GLU
3	LYS	THR	LYS	GLN	GLY	VAL	ALA	GLU	ALA	ALA
4	GLY	LYS	THR	LYS	GLU	GLY	VAL	LEU	TYR	VAL
5	GLY	SER	LYS	THR	LYS	GLU	GLY	VAL	VAL	HIS
6	GLY	VAL	ALA	THR	VAL	ALA	GLU	LYS	THR	LYS
7	GLU	GLN	VAL	THR	ASN	VAL	GLY	GLY	ALA	VAL
8	VAL	THR	GLY	VAL	THR	ALA	VAL	ALA	GLN	LYS
9	THR	VAL	GLU	GLY	ALA	GLY	SER	ILE	ALA	ALA
10	ALA	THR	GLY	PHE	VAL	LYS	LYS	ASP	GLN	LEU
11	GLY	LYS	ASN	GLU	GLU	GLY	ALA	PRO	GLN	GLU
12	GLY	ILE	LEU	GLU	ASP	MET	PRO	VAL	ASP	PRO
13	ASP	ASN	GLU	ALA	TYR	GLU	MET	PRO	SER	GLU
14	GLU	GLY	TYR	GLN	ASP	TYR	GLU	PRO	GLU	ALA

Entity 2, SDS - C12 H26 O4 S - 266.397 Da.

1

SDS

Samples:

sample_1: Bound Synucelin, [U-98% 13C; U-98% 15N], 150 uM; SDS 40 mM; D2O, [U-100% 2H], 10%; sodium phosphate 10 mM; EDTA 100 uM; sodium azide 100 uM

sample_conditions_1: ionic strength: 50.2 mM; pH: 5.5; pressure: 1 atm; temperature: 323 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
HNCACB	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.5 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

UNP	P37840
AlphaFold	Q6IAU6

Biological Magnetic Resonance Data Bank