BMRB Entry 18630

Title:
Backbone Chemical Shifts for N-terminal domain of sulfhydryl oxidase ALR
Deposition date:
2012-08-01
Original release date:
2012-11-28
Authors:
Banci, Lucia; Ciofi-Baffoni, Simone; Isabella, Felli; Gallo, Angelo; Pavelkova, Anna
Citation:

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).
PubMed: 23207295

Assembly members:

Assembly members:
N-terminal_of_sulfhydryl_oxidase_ALR, polymer, 80 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal_of_sulfhydryl_oxidase_ALR: MAAPGERGRFHGGNLFFLPG GARSEMMDDLATDARGRGAG RRDAAASASTPAQAPTSDSP VAEDASRRRPCRACVDFKTW

Data sets:
Data typeCount
13C chemical shifts225
15N chemical shifts81
1H chemical shifts72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-80 ALR1

Entities:

Entity 1, N-80 ALR 80 residues - Formula weight is not available

1   METALAALAPROGLYGLUARGGLYARGPHE
2   HISGLYGLYASNLEUPHEPHELEUPROGLY
3   GLYALAARGSERGLUMETMETASPASPLEU
4   ALATHRASPALAARGGLYARGGLYALAGLY
5   ARGARGASPALAALAALASERALASERTHR
6   PROALAGLNALAPROTHRSERASPSERPRO
7   VALALAGLUASPALASERARGARGARGPRO
8   CYSARGALACYSVALASPPHELYSTHRTRP

Samples:

sample_1: N-terminal of sulfhydryl oxidase ALR, [U-13C; U-15N], 0.5 mM; potassium phosphate 50 mM; D2O 90%; H2O 10%

sample_2: N-terminal of sulfhydryl oxidase ALR, [U-100% 15N], 0.5 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
CBCACONsample_1isotropicsample_conditions_1
CONsample_1isotropicsample_conditions_1
CACOsample_1isotropicsample_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 18631
DBJ BAI46852
GB AAD56538 AAG38105 EAW85580
REF NP_005253 XP_003269203 XP_003807737 XP_004057029
SP P55789
AlphaFold P55789

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks