BMRB Entry 34800

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34800
MolProbity Validation Chart

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Title:
Solution NMR Structure of Alpha-Synuclein 1-25 Peptide in 50% TFE.
Deposition date:
2023-03-24
Original release date:
2023-08-04
Authors:
Allen, S.; Williams, C.; Meade, R.; Tang, T.; 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, 27 residues, 2653.168 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: XMDVFMKGLSKAKEGVVAAA EKTKQGX

Data sets:
Data typeCount
13C chemical shifts77
15N chemical shifts22
1H chemical shifts176

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 27 residues - 2653.168 Da.

1   ACEMETASPVALPHEMETLYSGLYLEUSER
2   LYSALALYSGLUGLYVALVALALAALAALA
3   GLULYSTHRLYSGLNGLYNH2

Samples:

sample_1: aSyn_1-25 1 ± 0.2 mM; potassium phosphate 20 ± 0.2 mM; D2O, [U-100% 2H], 10 ± 0.2 %; 2,2,2-Trifluoroethanol, [U-2H], 50 ± 0.2 %

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1

Software:

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

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

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

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

AnalysisAssign v2.5.2, CCPN - chemical shift assignment

TopSpin v4.1.3, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz

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