BMRB Entry 18631
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18631
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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
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 231 |
15N chemical shifts | 77 |
1H chemical shifts | 79 |
Additional metadata:
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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