BMRB Entry 25464

Name: Solution structure of an MbtH-like protein from Mycobacterium marinum. Seattle Structural Genomics Center for Infectious Disease target MymaA.01649.c
Published: 2015-03-30

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PDB ID: 2myy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25464
MolProbity Validation Chart

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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: Solution structure of an MbtH-like protein from Mycobacterium marinum. Seattle Structural Genomics Center for Infectious Disease target MymaA.01649.c PubMed: 24878278

Deposition date: 2015-02-02 Original release date: 2015-03-30

Authors: Buchko, Garry

Citation: Zhang, Yanfeng; Zheng, Yi; Qin, Ling; Wang, Shihua; Buchko, Garry; Garavito, R. Michael. "Structural characterization of a beta-hydroxyacid dehydrogenase from Geobacter sulfurreducens and Geobacter metallireducens with succinic semialdehyde reductase activity" Biochimie 104, 61-69 (2014).

Assembly members:
entity, polymer, 80 residues, 9012.041 Da.

Natural source: Common Name: high GC Gram+ bacteria Taxonomy ID: 1348799 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium marinum

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

Entity Sequences (FASTA):
entity: GPGSMKIMSDNPFDDEDGMF FVLINDEEQHSLWPTFADVP AGWRVVFGEASRASCVEYVD QHWTDIRPKSLREKLASGQG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	412
13C chemical shifts	267
15N chemical shifts	65

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 80 residues - 9012.041 Da.

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

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; D2O 7%; H2O 93%

sample_2: entity, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; D2O 100%

sample_conditions_1: temperature: 293 K; pH: 7; pressure: 1 atm; ionic strength: 0.12 M

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
D2O exchange	sample_2	isotropic	sample_conditions_1
HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY v3.115, Goddard - data analysis, peak picking

Felix v2007, Accelrys Software Inc. - processing

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Agilent VNMRS 800 MHz
Agilent VNMRS 600 MHz

PDB	2MYY
EMBL	CDM77311
GB	ACC41692 EPQ77034 EPQ80949
REF	WP_020725647

Biological Magnetic Resonance Data Bank