BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15095

Title: Solution Structure of a Dodecapeptide from Alpha-Synuclein Bound with Synphilin-1   PubMed: 19762560

Authors: Zhou, Chen-Jie; Hu, Hong-Yu; Lin, Dong-Hai

Citation: Xie, Yuan-Yuan; Zhou, Chen-Jie; Zhou, Zi-Ren; Hong, Jing; Che, Mei-Xia; Fu, Qing-Shan; Song, Ai-Xin; Lin, Dong-Hai; Hu, Hong-Yu. "Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication."  FASEB J. 24, 196-205 (2010).

Assembly members:
Alpha-Syn12, polymer, 12 residues, 1357.708 Da.
Synphilin, non-polymer, Formula weight is not available

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
Alpha-Syn12: MDVFMKGLSKAK

Data sets:
Data typeCount
1H chemical shifts73

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Alpha-Syn121
2Synphilin-12

Entities:

Entity 1, Alpha-Syn12 12 residues - 1357.708 Da.

1   METASPVALPHEMETLYSGLYLEUSERLYS
2   ALALYS

Entity 2, Synphilin-1 - . - Formula weight is not available

1   Synphilin

Samples:

sample_1: entity 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; Synphilin-1 0.1 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

NMRDraw v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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

ARIA v2.0, Linge, O, . - data analysis, refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links: