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 18631

Title: N-terminal of Sulfydryl Oxidase of ALR reduced   PubMed: 23207295

Deposition date: 2012-08-01 Original release date: 2012-11-28

Authors: Banci, Lucia; Ciofi-Baffoni, Simone; Felli, Isabella; Gallo, Angelo; Pavelkova, Anna

Citation: Banci, Lucia; Bertini, Ivano; Cefaro, Chiara; Ciofi-Baffoni, Simone; Gajda, Karolina; Felli, Isabella; Gallo, Angelo; Pavelkova, Anna; Kallergi, Emmanouela; Andreadaki, Maria; Katrakili, Nitsa; Pozidis, Charalambos; Tokatlidis, Kostas. "An intrinsically disordered domain has a dual function coupled to compartment-dependent redox control."  J. Mol. Biol. 425, 594-608 (2013).

Assembly members:
N-terminal_of_sulfhydryl_oxidase_ALR_reduced, polymer, 80 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):
N-terminal_of_sulfhydryl_oxidase_ALR_reduced: MAAPGERGRFHGGNLFFLPG GARSEMMDDLATDARGRGAG RRDAAASASTPAQAPTSDSP VAEDASRRRPCRACVDFKTW

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts77
1H chemical shifts79

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

BMRB 18630
DBJ BAI46852
GB AAD56538 AAG38105 EAW85580
REF NP_005253 XP_003269203 XP_003807737 XP_004057029
SP P55789

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