BMRB Entry 50898

Name: hDVL2 DEP domain (401-510) S418E mutant
Published: 2021-06-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50898

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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:

hDVL2 DEP domain (401-510) S418E mutant

Deposition date:

2021-04-15

Original release date:

2021-06-25

Authors:

Beitia, Gonzalo; Rutherford, Trevor; Freund, Stefan; Pelham, Hugh; Bienz, Mariann; Gammons, Melissa

Citation:

Citation: Beitia, Gonzalo; Rutherford, Trevor; Freund, Stefan; Pelham, Hugh; Bienz, Mariann; Gammons, Melissa. "Regulation of Dishevelled DEP domain swapping by conserved phosphorylation sites." Proc. Natl. Acad. Sci. U. S. A. 118, e2103258118-e2103258118 (2021).
PubMed: 34155117

Assembly members:

Assembly members:
entity_1, polymer, 110 residues, 12147 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 Vector: pETM-11, EMBL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SITSGSSLPDGCEGRGLEVH TDMASVTKAMAAPESGLEVR DRMWLKITIPNAFLGSDVVD WLYHHVEGFPERREARKYAS GLLKAGLIRHTVNKITFSEQ CYYVFGDLSG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
13C chemical shifts	309
15N chemical shifts	102
1H chemical shifts	213
T2 relaxation values	97
heteronuclear NOE values	101

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DVL2 DEP S418E mutant	1

Entities:

Entity 1, DVL2 DEP S418E mutant 110 residues - 12147 Da.

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_2	isotropic	sample_conditions_2
T2/R2 relaxation	sample_3	isotropic	sample_conditions_3

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

BMRB Entry 50898

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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