BMRB Entry 25902

Name: actinin-1 EF hand 3,4 Bound to Cav1.2 IQ Motif
Published: 2016-10-27

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PDB ID: 6c0a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25902
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:

actinin-1 EF hand 3,4 Bound to Cav1.2 IQ Motif

Deposition date:

2015-11-17

Original release date:

2016-10-27

Authors:

Turner, Matthew; Ames, James

Citation:

Citation: Turner, Matthew; Anderson, David; Rajan, Sahana; Hell, Johannes; Ames, James. "Chemical shift assignments of the C-terminal EF-hand domain of alpha-actinin-1" Biomol. NMR Assign. 10, 219-222 (2016).
PubMed: 26861220

Assembly members:

Assembly members:
actinin-1, polymer, 89 residues, Formula weight is not available
IQ-Motif, polymer, 25 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: pET15-b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
actinin-1: MGSSHHHHHSSGLVPRGSHM DTADQVMASFKILAGDKNYI TMDELRRELPPDQAEYCIAR MAPYTGPDSVPGALDYMSFS TALYGESDL
IQ-Motif: TVGKFYATFLIQEYFRKFKK RKEQG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	258
15N chemical shifts	64
1H chemical shifts	433

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EF hand	1
2	Cav1.2IQMotif	2

Entities:

Entity 1, EF hand 89 residues - Formula weight is not available

residues 824-892 of actinin-1 EF hand c-lobe. Contains a non native 6His tag at the c-terminus (MGSSHHHHHSSGLVPRGSHM)

1

MET

GLY

SER

HIS

SER

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

MET

3

ASP

THR

ALA

ASP

GLN

VAL

MET

ALA

SER

PHE

4

LYS

ILE

LEU

ALA

GLY

ASP

LYS

ASN

TYR

ILE

5

THR

MET

ASP

GLU

LEU

ARG

GLU

LEU

PRO

6

PRO

ASP

GLN

ALA

GLU

TYR

CYS

ILE

ALA

ARG

7

MET

ALA

PRO

TYR

THR

GLY

PRO

ASP

SER

VAL

8

PRO

GLY

ALA

LEU

ASP

TYR

MET

SER

PHE

SER

9

THR

ALA

LEU

TYR

GLY

GLU

SER

ASP

LEU

Entity 2, Cav1.2IQMotif 25 residues - Formula weight is not available

1

THR

VAL

GLY

LYS

PHE

TYR

ALA

THR

PHE

LEU

2

ILE

GLN

GLU

TYR

PHE

ARG

LYS

PHE

LYS

3

ARG

LYS

GLU

GLN

GLY

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	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 25902

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: