BMRB Entry 18630

Name: Backbone Chemical Shifts for N-terminal domain of sulfhydryl oxidase ALR
Published: 2012-11-28

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18630

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	225
15N chemical shifts	81
1H chemical shifts	72

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-80 ALR	1

Entities:

Entity 1, N-80 ALR 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, [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:

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

BMRB	18631
DBJ	BAI46852
GB	AAD56538 AAG38105 EAW85580
REF	NP_005253 XP_003269203 XP_003807737 XP_004057029
SP	P55789
AlphaFold	P55789

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

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