BMRB Entry 51632

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Alpha-synuclein linker region mutant &quot;3AE&quot; bound to SDS micelles
Published: 2023-02-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51632

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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: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Alpha-synuclein linker region mutant "3AE" bound to SDS micelles PubMed: 36551244

Deposition date: 2022-09-16 Original release date: 2023-02-08

Authors: Das, Tapojyoti; Ramezani, Meraj; Snead, David; Follmer, Cristian; Chung, Peter; Lee, Ka-Yee; Holowka, David; Baird, Barbara; Eliezer, David

Citation: Das, Tapojyoti; Ramezani, Meraj; Snead, David; Follmer, Cristian; Chung, Peter; Lee, Ka-Yee; Holowka, David; Baird, Barbara; Eliezer, David. "The Role of Membrane Affinity and Binding Modes in Alpha-Synuclein Regulation of Vesicle Release and Trafficking" Biomolecules 12, 1816-1816 (2022).

Assembly members:
entity_1, polymer, 102 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: pT7.7

Entity Sequences (FASTA):
entity_1: MDVFMKGLSKAKEGVVAAAE KTKQGVAEAAGKTKEGVLAA AEKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQK TVEGAGSIAAATGFVKKDQL GK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	289
15N chemical shifts	100
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Alpha-synuclein	1
2	2H-SDS	2

Entities:

Entity 1, Alpha-synuclein 102 residues - Formula weight is not available

1

MET

ASP

VAL

PHE

MET

LYS

GLY

LEU

SER

LYS

2

ALA

LYS

GLU

GLY

VAL

ALA

GLU

3

LYS

THR

LYS

GLN

GLY

VAL

ALA

GLU

ALA

4

GLY

LYS

THR

LYS

GLU

GLY

VAL

LEU

ALA

5

ALA

GLU

LYS

THR

LYS

GLU

GLY

VAL

HIS

6

GLY

VAL

ALA

THR

VAL

ALA

GLU

LYS

THR

LYS

7

GLU

GLN

VAL

THR

ASN

VAL

GLY

ALA

VAL

8

VAL

THR

GLY

VAL

THR

ALA

VAL

ALA

GLN

LYS

9

THR

VAL

GLU

GLY

ALA

GLY

SER

ILE

ALA

10

ALA

THR

GLY

PHE

VAL

LYS

ASP

GLN

LEU

11

GLY

LYS

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

1

SDS

Samples:

sample_1: Alpha-synuclein linker mutant 3AE (1-102), [U-10% 13C; U-100% 15N], 100 uM; SDS, [U-99% 2H], 40 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

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