BMRB Entry 16342

Title:
Backbone 1H, 13C, 15N and 13C-beta Chemical Shift Assignments for alpha-synuclein at pH 3   PubMed: 19554627
Deposition date:
2009-06-09
Original release date:
2009-07-06
Authors:
Cho, Min-Kyu; Kim, Hai-Young; Zweckstetter, Markus
Citation:

Citation: Cho, Min-Kyu; Nodet, Gabrielle; Kim, Hai-Young; Jensen, Malene; Bernado, Pau; Fernandez, Claudio; Becker, Stefan; Blackledge, Martin; Zweckstetter, Markus. "Structural characterization of alpha-synuclein in an aggregation prone state"  Protein Sci. 18, 1840-1846 (2009).

Assembly members:

Assembly members:
human_a-synuclein, polymer, 140 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:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: T7

Experimental source:

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: T7

Data sets:
Data typeCount
13C chemical shifts210
15N chemical shifts130
1H chemical shifts130
heteronuclear NOE values128
residual dipolar couplings117

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1human a-synuclein1

Entities:

Entity 1, human a-synuclein 140 residues - Formula weight is not available

1   METASPVALPHEMETLYSGLYLEUSERLYS
2   ALALYSGLUGLYVALVALALAALAALAGLU
3   LYSTHRLYSGLNGLYVALALAGLUALAALA
4   GLYLYSTHRLYSGLUGLYVALLEUTYRVAL
5   GLYSERLYSTHRLYSGLUGLYVALVALHIS
6   GLYVALALATHRVALALAGLULYSTHRLYS
7   GLUGLNVALTHRASNVALGLYGLYALAVAL
8   VALTHRGLYVALTHRALAVALALAGLNLYS
9   THRVALGLUGLYALAGLYSERILEALAALA
10   ALATHRGLYPHEVALLYSLYSASPGLNLEU
11   GLYLYSASNGLUGLUGLYALAPROGLNGLU
12   GLYILELEUGLUASPMETPROVALASPPRO
13   ASPASNGLUALATYRGLUMETPROSERGLU
14   GLUGLYTYRGLNASPTYRGLUPROGLUALA

Samples:

sample_1: a-synuclein, [U-13C; U-15N], 300 uM; sodium chloride 100 mM; sodium acetate 20 mM; H2O 90%; D2O 10%

pH3: ionic strength: 0.28 M; pH: 3.0; pressure: 1 atm; temperature: 288 K

pH3_anisotropic: ionic strength: 0.28 M; pH: 3.0; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicpH3
3D CBCA(CO)NHsample_1isotropicpH3
3D HNCACBsample_1isotropicpH3
2D Heteronuclear NOEsample_1isotropicpH3
2D IPAP 1H-15N HSQCsample_1anisotropicpH3_anisotropic
2D 1H-15N R1rhosample_1isotropicpH3
2D 1H-15N R2sample_1isotropicpH3

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16300 16302 16543 16546 16547 16548 16904 16939 17214 17498 17648 17649 17654 17665 17910 18207 18208 18243 18857 18860 19257 19337 19338 19344 19345 19350 19351 25227 25228
PDB
DBJ BAB29375 BAF82858 BAG73790
EMBL CAG33339 CAG46454
GB AAA16117 AAC02114 AAG30302 AAH13293 AAI08276
REF NP_000336 NP_001009158 NP_001032222 NP_001129014 NP_001139526
SP P37840 P61139 P61140 P61142 P61143
AlphaFold P61139

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