BMRB Entry 17350

Name: SOLUTION STRUCTURE OF THE R2 DOMAIN OF TALIN
Published: 2013-02-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17350

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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 R2 DOMAIN OF TALIN

Deposition date:

2010-12-07

Original release date:

2013-02-04

Authors:

Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Roberts, Gordon; Barsukov, Igor; Critchley, David

Citation:

Citation: Goult, Benjamin; Zacharchenko, Tom; Bate, Neil; Tsang, Ricky; Hey, Fiona; Gingras, Alexandre; Elliott, Paul; Roberts, Gordon; Ballestrem, Christoph; Critchley, David; Barsukov, Igor. "RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover" J. Biol. Chem. ., .-..

Assembly members:

Assembly members:
vbs2a, polymer, 138 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet151TOPO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
vbs2a: GIDPFTIGESDTDPHFQDVL MQLANAVASAAAALVLKAKS VAQRTEDSGLQTQVIAAATQ CALSTSQLVACTKVVAPTIS SPVCQEQLVEAGRLVAKAVE GCVSASQAATEDGQLLRGVG AAATAVTQALNELLQHVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	396
15N chemical shifts	131
1H chemical shifts	131

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	vbs2a	1

Entities:

Entity 1, vbs2a 138 residues - Formula weight is not available

Residues 1-6 (residues 649-654) represent a non-native affinity tag

1

GLY

ILE

ASP

PRO

PHE

THR

ILE

GLY

GLU

SER

2

ASP

THR

ASP

PRO

HIS

PHE

GLN

ASP

VAL

LEU

3

MET

GLN

LEU

ALA

ASN

ALA

VAL

ALA

SER

ALA

4

ALA

LEU

VAL

LEU

LYS

ALA

LYS

SER

5

VAL

ALA

GLN

ARG

THR

GLU

ASP

SER

GLY

LEU

6

GLN

THR

GLN

VAL

ILE

ALA

THR

GLN

7

CYS

ALA

LEU

SER

THR

SER

GLN

LEU

VAL

ALA

8

CYS

THR

LYS

VAL

ALA

PRO

THR

ILE

SER

9

SER

PRO

VAL

CYS

GLN

GLU

GLN

LEU

VAL

GLU

10

ALA

GLY

ARG

LEU

VAL

ALA

LYS

ALA

VAL

GLU

11

GLY

CYS

VAL

SER

ALA

SER

GLN

ALA

THR

12

GLU

ASP

GLY

GLN

LEU

ARG

GLY

VAL

GLY

13

ALA

THR

ALA

VAL

THR

GLN

ALA

LEU

14

ASN

GLU

LEU

GLN

HIS

VAL

LYS

Samples:

sample_1: vbs2a, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; DTT 2 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; D2O 10 ± 0.1 %; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CCPNAnalysis v1.15, CCPN - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - Dihedral angle prediction

NMR spectrometers:

Bruker DRX 600 MHz

PDB	1SJ8
DBJ	BAA82979 BAC65702 BAE27781 BAG09941
EMBL	CAA39588
GB	AAD13152 AAF23322 AAF27330 AAH42923 AAI50811
PRF	1617167A
REF	NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001084941
SP	P26039 Q9Y490
TPG	DAA26829
AlphaFold	P26039 Q9Y490