BMRB Entry 30725

Name: Solution structure of the N-terminal helix-hairpin-helix domain of human MUS81
Published: 2021-02-20

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PDB ID: 6vwb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30725
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 the N-terminal helix-hairpin-helix domain of human MUS81

Deposition date:

2020-02-19

Original release date:

2021-02-20

Authors:

Payliss, B.; Houliston, S.; Lemak, A.; Arrowsmith, C.; Wyatt, H.

Citation:

Citation: Payliss, Brandon; Tse, Ying Wah; Reichheld, Sean; Lemak, Alexander; Yun, Hwa Young; Houliston, Scott; Patel, Ayushi; Arrowsmith, Cheryl; Sharpe, Simon; Wyatt, Haley. "Phosphorylation of the DNA repair scaffold SLX4 drives folding of the SAP domain and activation of the MUS81-EME1 endonuclease" Cell Rep. 41, 111537-111537 (2022).
PubMed: 36288699

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, 10618.409 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AAAPVRLGRKRPLPACPNPL FVRWLTEWRDEATRSRRRTR FVFQKALRSLRRYPLPLRSG KEAKILQHFGDGLCRMLDER LQRHRTSGGD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	385
15N chemical shifts	82
1H chemical shifts	629

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 90 residues - 10618.409 Da.

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

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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 30725

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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