BMRB Entry 18485

Name: Solution structure of a monomeric truncated mutant of Trypanosoma brucei 1-C-Grx1
Published: 2013-04-02

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PDB ID: 2ltk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18485
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of a monomeric truncated mutant of Trypanosoma brucei 1-C-Grx1 PubMed: 23259530

Deposition date: 2012-05-29 Original release date: 2013-04-02

Authors: Bellanda, Massimo; Pavan, Carlo; Gesiot, Lorenzo; Comini, Marcelo; Manta, Bruno; Mammi, Stefano; Sturlese, Mattia

Citation: Manta, Bruno; Pavan, Carlo; Sturlese, Mattia; Medeiros, Andrea; Crispo, Martina; Berndt, Carsten; Krauth-Siegel, R.; Bellanda, Massimo; Comini, Marcelo. "Iron-sulfur cluster binding by mitochondrial monothiol glutaredoxin-1 of Trypanosoma brucei: molecular basis of iron-sulfur cluster coordination and relevance for parasite infectivity" Antioxid. Redox Signal. 19, 665-682 (2013).

Assembly members:
1-C-Grx1, polymer, 110 residues, 12325.543 Da.

Natural source: Common Name: kinetoplastids Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

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

Entity Sequences (FASTA):
1-C-Grx1: GAMVKKDIDDTIKSEDVVTF IKGLPEAPMCAYSKRMIDVL EALGLEYTSFDVLAHPVVRS YVKEVSEWPTIPQLFIKAEF VGGLDIVTKMLESGDLKKML RDKGITCRDL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	496
15N chemical shifts	103
1H chemical shifts	816

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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1	GLY	ALA	MET	VAL	LYS	LYS	ASP	ILE	ASP	ASP
2	THR	ILE	LYS	SER	GLU	ASP	VAL	VAL	THR	PHE
3	ILE	LYS	GLY	LEU	PRO	GLU	ALA	PRO	MET	CYS
4	ALA	TYR	SER	LYS	ARG	MET	ILE	ASP	VAL	LEU
5	GLU	ALA	LEU	GLY	LEU	GLU	TYR	THR	SER	PHE
6	ASP	VAL	LEU	ALA	HIS	PRO	VAL	VAL	ARG	SER
7	TYR	VAL	LYS	GLU	VAL	SER	GLU	TRP	PRO	THR
8	ILE	PRO	GLN	LEU	PHE	ILE	LYS	ALA	GLU	PHE
9	VAL	GLY	GLY	LEU	ASP	ILE	VAL	THR	LYS	MET
10	LEU	GLU	SER	GLY	ASP	LEU	LYS	LYS	MET	LEU
11	ARG	ASP	LYS	GLY	ILE	THR	CYS	ARG	ASP	LEU

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CBCACO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D H(CCCO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D (H)C(CCO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(C)CH-TOCSY	sample_1	isotropic	sample_conditions_1
2D (H)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1
2D (H)CB(CGCC)H-TOCSY (Tyr-optimized)	sample_1	isotropic	sample_conditions_1
2D (H)CB(CGCC)H-TOCSY (Phe-optimized)	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY (arom)	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY( aliph)	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY (arom)	sample_1	isotropic	sample_conditions_1

BMRB	19736
PDB	2LTK
EMBL	CAF02300 CBH14109
GB	EAN76448
REF	XP_011776380 XP_803662

Biological Magnetic Resonance Data Bank

BMRB Entry 18485

Title: Solution structure of a monomeric truncated mutant of Trypanosoma brucei 1-C-Grx1 PubMed: 23259530

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

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

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

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