BMRB Entry 52385

Name: C-terminal EF-hand (EF34) Domain of a-actinin-1
Published: 2024-09-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52385

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

C-terminal EF-hand (EF34) Domain of a-actinin-1

Deposition date:

2024-04-02

Original release date:

2024-09-03

Authors:

Bej, Aritra; Ames, James

Citation:

Citation: Bej, Aritra; Hell, Johannes; Ames, James. "Chemical shift assignments of the alpha-actinin C-terminal EF-hand domain bound to a cytosolic C0 domain of GluN1 (residues 841-865) from the NMDA receptor" Biomol. NMR Assign. 18, 239-244 (2024).
PubMed: 39207574

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, Formula weight is not available

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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MDTADQVMASFKILAGDKNY ITMDELRRELPPDQAEYCIA RMAPYTGPDSVPGALDYMSF STALYGESDL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	255
15N chemical shifts	64
1H chemical shifts	430

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ACTN1 EF34	1

Entities:

Entity 1, ACTN1 EF34 90 residues - Formula weight is not available

Residues 1-21 represent non-native affinity tag and cleavage site

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	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 52385

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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