BMRB Entry 34801

Name: Solution NMR Structure of Lactamised Alpha-Synuclein 2-12 Peptide in 50% TFE.
Published: 2024-07-01

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PDB ID: 8ol8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34801
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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:

Solution NMR Structure of Lactamised Alpha-Synuclein 2-12 Peptide in 50% TFE.

Deposition date:

2023-03-30

Original release date:

2024-07-01

Authors:

Allen, S.; Williams, C.; Meade, R.; Crump, M.; Mason, J.

Citation:

Citation: Meade, R.; Allen, S.; Williams, C.; Tang, T.; Crump, M.; Mason, J.. "The N-terminal domain of alpha-Synuclein modulates lipid induced aggregation via competitive inhibition" .

Assembly members:

Assembly members:
entity_1, polymer, 13 residues, 1366.692 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XDVFMKKLSKDKX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	44
15N chemical shifts	13
1H chemical shifts	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 13 residues - 1366.692 Da.

1

ACE

ASP

VAL

PHE

MET

LYS

LEU

SER

LYS

2

ASP

LYS

NH2

Samples:

sample_1: aSyn1-12 1 ± 0.2 mM; potassium phosphate 20 ± 0.2 mM; D2O, [U-99% 2H], 10 ± 0.2 % v/v; 2,2,2-Trifluoroethanol, [U-100% 2H], 50 ± 0.2 % v/v

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-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

ARIA v2.3.2, Linge, O'Donoghue and Nilges - structure calculation

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

DANGLE v1.1, Cheung MS, Maguire ML, Stevens TJ, Broadhurst RW. - data analysis

TopSpin v3.6.1, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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