BMRB Entry 11545

Name: Backbone 1H, 13C, and 15N chemical shift assignment for aqMutL-CTD
Published: 2017-03-13

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11545

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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 1H, 13C, and 15N chemical shift assignment for aqMutL-CTD

Deposition date:

2013-11-26

Original release date:

2017-03-13

Authors:

Mizushima, Ryota; Lee, Young-Ho

Citation:

Citation: Mizushima, Ryota; Kim, Ju Yaen; Suetake, Isao; Tanaka, Hiroaki; Takai, Tomoyo; Kamiya, Narutoshi; Takano, Yu; Mishima, Yuichi; Tajima, Shoji; Goto, Yuji; Fukui, Kenji; Lee, Young-Ho. "NMR characterization of the interaction of the endonuclease domain of MutL with divalent metal ions and ATP" PLoS ONE 9, e98554-e98554 (2014).
PubMed: 24901533

Assembly members:

Assembly members:
aqMutL-CTD_homodimer, polymer, 110 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Aquifex aeolicus Taxonomy ID: 63363 Superkingdom: Bacteria Kingdom: not available Genus/species: Aquifex aeolicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
aqMutL-CTD_homodimer: PLSQPVKTYKPTYEILGQMD ETFILVKDSEYLYFVDQHLL EERINYEKLKDENLACRISV KAGQKLSEEKIRELIKTWRN LENPHVCPHGRPIYYKIPLR EIYEKVGRNY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	283
15N chemical shifts	98
1H chemical shifts	98

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain, chain 1	1
2	C-terminal domain, chain 2	1

Entities:

Entity 1, C-terminal domain, chain 1 110 residues - Formula weight is not available

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

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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 11545

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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