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:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | N-80 ALR reduced | 1 |
Entities:
Entity 1, N-80 ALR reduced 80 residues - Formula weight is not available
1 | MET | ALA | ALA | PRO | GLY | GLU | ARG | GLY | ARG | PHE | |
2 | HIS | GLY | GLY | ASN | LEU | PHE | PHE | LEU | PRO | GLY | |
3 | GLY | ALA | ARG | SER | GLU | MET | MET | ASP | ASP | LEU | |
4 | ALA | THR | ASP | ALA | ARG | GLY | ARG | GLY | ALA | GLY | |
5 | ARG | ARG | ASP | ALA | ALA | ALA | SER | ALA | SER | THR | |
6 | PRO | ALA | GLN | ALA | PRO | THR | SER | ASP | SER | PRO | |
7 | VAL | ALA | GLU | ASP | ALA | SER | ARG | ARG | ARG | PRO | |
8 | CYS | ARG | ALA | CYS | VAL | ASP | PHE | LYS | THR | TRP |
Samples:
sample_1: N-terminal of sulfhydryl oxidase ALR reduced, [U-13C; U-15N], 0.5 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%
sample_2: N-terminal of sulfhydryl oxidase ALR reduced, [U-100% 15N], 0.5 mM; potassium phosphate 50 mM; H20 90%; D20 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
CBCACON | sample_1 | isotropic | sample_conditions_1 |
CON | sample_1 | isotropic | sample_conditions_1 |
CACO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
CARA v2.1, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
BMRB | 18630 |
DBJ | BAI46852 |
GB | AAD56538 AAG38105 EAW85580 |
REF | NP_005253 XP_003269203 XP_003807737 XP_004057029 |
SP | P55789 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts