BMRB Entry 16548

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16548

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Title:
Backbone 1H and 15N Chemical Shifts for Disordered A53T alpha-Synuclein
Deposition date:
2009-10-07
Original release date:
2010-01-28
Authors:
Bodner, Christina; Dobson, Christopher; Bax, Ad
Citation:

Citation: Bodner, Christina; Maltsev, Alexander; Dobson, Christopher; Bax, Ad. "Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy."  Biochemistry 49, 862-871 (2010).
PubMed: 20041693

Assembly members:

Assembly members:
A53T_alpha-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:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28(a)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A53T_alpha-synuclein: MDVFMKGLSKAKEGVVAAAE KTKQGVAEAAGKTKEGVLYV GSKTKEGVVHGVTTVAEKTK EQVTNVGGAVVTGVTAVAQK TVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA

Data sets:
Data typeCount
15N chemical shifts133
1H chemical shifts133

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer A53T alpha-synuclein1

Entities:

Entity 1, monomer A53T alpha-synuclein 140 residues - Formula weight is not available

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

Samples:

sample_1: sodium phosphate 20 mM; H2O 95%; D2O 5%; protein, [U-15N; U-2H], 0.6 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 16300 16302 16342 16543 16546 16547 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 P37840 P61139 P61140 P61142 P61143

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