BMRB Entry 36048

Name: Solution NMR Structure of DNA Mismatch Repair Protein MutT (Family Nudix Hydrolase) from Methicillin Resistant Staphylococcus aureus 252
Published: 2017-04-24

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PDB ID: 5x1x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36048
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 NMR Structure of DNA Mismatch Repair Protein MutT (Family Nudix Hydrolase) from Methicillin Resistant Staphylococcus aureus 252

Deposition date:

2017-01-27

Original release date:

2017-04-24

Authors:

Wahab, A.; Durreshahwar, S.; Schwalbe, H.; Richter, C.; Choudhary, M.

Citation:

Citation: Wahab, A.. "Solution NMR Structure of DNA Mismatch Repair Protein MutT (Family Nudix Hydrolase) from Methicillin Resistant Staphylococcus aureus 252" .

Assembly members:

Assembly members:
entity_1, polymer, 130 residues, 14914.342 Da.

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 548470 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pSpeedET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKKVINVVGAIIFSDNKILC AQRSEKMSLPLMWEFPGGKV EKNETEKDALIREIREEMKC DLIVGDKVITTEHEYDFGIV RLTTYKCTLNKELPTLTEHK SIEWLSINELDKLNWAPADI PAVNKIMTEG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	586
15N chemical shifts	134
1H chemical shifts	982

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 130 residues - 14914.342 Da.

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	anisotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 36048

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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