BMRB Entry 16713

Name: 1H, 13C and 15N backbone and side-chain chemical shift assignments for reduced desulthioredoxin
Published: 2010-04-26

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16713

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C and 15N backbone and side-chain chemical shift assignments for reduced desulthioredoxin

Deposition date:

2010-02-08

Original release date:

2010-04-26

Authors:

Garcin, Edwige; Bornet, Olivier; Sebban-Kreuzer, Corinne; Guerlesquin, Francoise

Citation:

Citation: Garcin, Edwige; Bornet, Olivier; Pieulle, Laetitia; Guerlesquin, Francoise; Sebban-Kreuzer, Corinne. "1H, 13C and 15N backbone and side-chain chemical shift assignments for oxidized and reduced desulfothioredoxin." Biomol. NMR Assignments 4, 135-137 (2010).
PubMed: 20390383

Assembly members:

Assembly members:
Desulfothioredoxin, polymer, 110 residues, 12362.3 Da.

Natural source:

Natural source: Common Name: Desulfovibrio vulgaris Taxonomy ID: 881 Superkingdom: Bacteria Kingdom: not available Genus/species: Desulfovibrio vulgaris

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Desulfothioredoxin: MSAIRDITTEAGMAHFEGLS DAIVFFHKNLCPHCKNMEKV LDKFGARAPQVAISSVDSEA RPELMKELGFERVPTLVFIR DGKVAKVFSGIMNPRELQAL YASIHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	489
15N chemical shifts	114
1H chemical shifts	768

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	desulfothioredoxin	1

Entities:

Entity 1, desulfothioredoxin 110 residues - 12362.3 Da.

1	MET	SER	ALA	ILE	ARG	ASP	ILE	THR	THR	GLU
2	ALA	GLY	MET	ALA	HIS	PHE	GLU	GLY	LEU	SER
3	ASP	ALA	ILE	VAL	PHE	PHE	HIS	LYS	ASN	LEU
4	CYS	PRO	HIS	CYS	LYS	ASN	MET	GLU	LYS	VAL
5	LEU	ASP	LYS	PHE	GLY	ALA	ARG	ALA	PRO	GLN
6	VAL	ALA	ILE	SER	SER	VAL	ASP	SER	GLU	ALA
7	ARG	PRO	GLU	LEU	MET	LYS	GLU	LEU	GLY	PHE
8	GLU	ARG	VAL	PRO	THR	LEU	VAL	PHE	ILE	ARG
9	ASP	GLY	LYS	VAL	ALA	LYS	VAL	PHE	SER	GLY
10	ILE	MET	ASN	PRO	ARG	GLU	LEU	GLN	ALA	LEU
11	TYR	ALA	SER	ILE	HIS	HIS	HIS	HIS	HIS	HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

BMRB	16712
PDB	2L6C 2L6D
GB	AAS94861 ABM29571 ADP85513
REF	WP_010937685 YP_009602

BMRB Entry 16713

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	MET	SER	ALA	ILE	ARG	ASP	ILE	THR	THR	GLU
2	ALA	GLY	MET	ALA	HIS	PHE	GLU	GLY	LEU	SER
3	ASP	ALA	ILE	VAL	PHE	PHE	HIS	LYS	ASN	LEU
4	CYS	PRO	HIS	CYS	LYS	ASN	MET	GLU	LYS	VAL
5	LEU	ASP	LYS	PHE	GLY	ALA	ARG	ALA	PRO	GLN
6	VAL	ALA	ILE	SER	SER	VAL	ASP	SER	GLU	ALA
7	ARG	PRO	GLU	LEU	MET	LYS	GLU	LEU	GLY	PHE
8	GLU	ARG	VAL	PRO	THR	LEU	VAL	PHE	ILE	ARG
9	ASP	GLY	LYS	VAL	ALA	LYS	VAL	PHE	SER	GLY
10	ILE	MET	ASN	PRO	ARG	GLU	LEU	GLN	ALA	LEU
11	TYR	ALA	SER	ILE	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	SER	ALA	ILE	ARG	ASP	ILE	THR	THR	GLU
2	ALA	GLY	MET	ALA	HIS	PHE	GLU	GLY	LEU	SER
3	ASP	ALA	ILE	VAL	PHE	PHE	HIS	LYS	ASN	LEU
4	CYS	PRO	HIS	CYS	LYS	ASN	MET	GLU	LYS	VAL
5	LEU	ASP	LYS	PHE	GLY	ALA	ARG	ALA	PRO	GLN
6	VAL	ALA	ILE	SER	SER	VAL	ASP	SER	GLU	ALA
7	ARG	PRO	GLU	LEU	MET	LYS	GLU	LEU	GLY	PHE
8	GLU	ARG	VAL	PRO	THR	LEU	VAL	PHE	ILE	ARG
9	ASP	GLY	LYS	VAL	ALA	LYS	VAL	PHE	SER	GLY
10	ILE	MET	ASN	PRO	ARG	GLU	LEU	GLN	ALA	LEU
11	TYR	ALA	SER	ILE	HIS	HIS	HIS	HIS	HIS	HIS

1	MET	SER	ALA	ILE	ARG	ASP	ILE	THR	THR	GLU
2	ALA	GLY	MET	ALA	HIS	PHE	GLU	GLY	LEU	SER
3	ASP	ALA	ILE	VAL	PHE	PHE	HIS	LYS	ASN	LEU
4	CYS	PRO	HIS	CYS	LYS	ASN	MET	GLU	LYS	VAL
5	LEU	ASP	LYS	PHE	GLY	ALA	ARG	ALA	PRO	GLN
6	VAL	ALA	ILE	SER	SER	VAL	ASP	SER	GLU	ALA
7	ARG	PRO	GLU	LEU	MET	LYS	GLU	LEU	GLY	PHE
8	GLU	ARG	VAL	PRO	THR	LEU	VAL	PHE	ILE	ARG
9	ASP	GLY	LYS	VAL	ALA	LYS	VAL	PHE	SER	GLY
10	ILE	MET	ASN	PRO	ARG	GLU	LEU	GLN	ALA	LEU
11	TYR	ALA	SER	ILE	HIS	HIS	HIS	HIS	HIS	HIS