BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27027

Title: N-terminally acetylated beta-Synuclein   PubMed: 28820253

Authors: Miotto, Marco; Pavese, Mayra; Quintanar, Liliana; Zweckstetter, Markus; Griesinger, Christian; Fernandez, Claudio

Citation: Miotto, Marco; Pavese, Mayra; Quintanar, Liliana; Zweckstetter, Markus; Griesinger, Christian; Fernandez, Claudio. "Bioinorganic Chemistry of Parkinson's Disease: Affinity and Structural Features of Cu(I) Binding to the Full-Length beta-Synuclein Protein"  Inorg. Chem. 56, 10387-10395 (2017).

Assembly members:
AcBS, polymer, 135 residues, 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: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
AcBS: XMDVFMKGLSMAKEGVVAAA EKTKQGVTEAAEKTKEGVLY VGSKTREGVVQGVASVAEKT KEQASHLGGAVFSGAGNIAA ATGLVKREEFPTDLKPEEVA QEAAEEPLIEPLMEPEGESY EDPPQEEYQEYEPEA

Data sets:
Data typeCount
13C chemical shifts385
15N chemical shifts126
1H chemical shifts255

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1AcBS1

Entities:

Entity 1, AcBS 135 residues - Formula weight is not available

1   ACEMETASPVALPHEMETLYSGLYLEUSER
2   METALALYSGLUGLYVALVALALAALAALA
3   GLULYSTHRLYSGLNGLYVALTHRGLUALA
4   ALAGLULYSTHRLYSGLUGLYVALLEUTYR
5   VALGLYSERLYSTHRARGGLUGLYVALVAL
6   GLNGLYVALALASERVALALAGLULYSTHR
7   LYSGLUGLNALASERHISLEUGLYGLYALA
8   VALPHESERGLYALAGLYASNILEALAALA
9   ALATHRGLYLEUVALLYSARGGLUGLUPHE
10   PROTHRASPLEULYSPROGLUGLUVALALA
11   GLNGLUALAALAGLUGLUPROLEUILEGLU
12   PROLEUMETGLUPROGLUGLYGLUSERTYR
13   GLUASPPROPROGLNGLUGLUTYRGLNGLU
14   TYRGLUPROGLUALA

Samples:

sample_1: AcBS, [U-100% 13C; U-100% 15N], 0.2 mM; MES 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin, Keller and Wuthrich - chemical shift assignment, collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links: