BMRB Entry 17070

Name: SOLUTION STRUCTURE OF THE R6 DOMAIN OF TALIN
Published: 2013-02-04

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PDB ID: 2l10
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17070
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

SOLUTION STRUCTURE OF THE R6 DOMAIN OF TALIN

Deposition date:

2010-07-22

Original release date:

2013-02-04

Authors:

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

Citation:

Citation: Goult, Benjamin; Zacharchenko, Thomas; 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. 288, 8238-8249 (2013).
PubMed: 23389036

Assembly members:

Assembly members:
talin_domain_C, polymer, 158 residues, 16488.461 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet151

Entity Sequences (FASTA):

Entity Sequences (FASTA):
talin_domain_C: GIDPFTQRDVDNALRAVGDA SKRLLSDLLPPSTGTFQEAQ SRLNEAAAGLNQAATELVQA SRGTPQDLARASGRFGQDFS TFLEAGVEMAGQAPSQEDRA QVVSNLKGISMSSSKLLLAA KALSTDPASPNLKSQLAAAA RAVTDSINQLITMCTQQA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	484
15N chemical shifts	166
1H chemical shifts	1040

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	talin_domain_C	1

Entities:

Entity 1, talin_domain_C 158 residues - 16488.461 Da.

Residues 1-6 (1200-1205) represent a non-native affinity tag

1

GLY

ILE

ASP

PRO

PHE

THR

GLN

ARG

ASP

VAL

2

ASP

ASN

ALA

LEU

ARG

ALA

VAL

GLY

ASP

ALA

3

SER

LYS

ARG

LEU

SER

ASP

LEU

PRO

4

PRO

SER

THR

GLY

THR

PHE

GLN

GLU

ALA

GLN

5

SER

ARG

LEU

ASN

GLU

ALA

GLY

LEU

6

ASN

GLN

ALA

THR

GLU

LEU

VAL

GLN

ALA

7

SER

ARG

GLY

THR

PRO

GLN

ASP

LEU

ALA

ARG

8

ALA

SER

GLY

ARG

PHE

GLY

GLN

ASP

PHE

SER

9

THR

PHE

LEU

GLU

ALA

GLY

VAL

GLU

MET

ALA

10

GLY

GLN

ALA

PRO

SER

GLN

GLU

ASP

ARG

ALA

11

GLN

VAL

SER

ASN

LEU

LYS

GLY

ILE

SER

12

MET

SER

LYS

LEU

ALA

13

LYS

ALA

LEU

SER

THR

ASP

PRO

ALA

SER

PRO

14

ASN

LEU

LYS

SER

GLN

LEU

ALA

15

ARG

ALA

VAL

THR

ASP

SER

ILE

ASN

GLN

LEU

16

ILE

THR

MET

CYS

THR

GLN

ALA

Samples:

sample_1: talin_domain_C, [U-100% 15N], 1 ± 0.05 mM; D2O, [U-100% 2H], 5 ± 0.05 %; DTT 2 ± 0.01 mM; sodium chloride 50 ± 0.01 mM; TRIS 20 ± 0.01 mM; H2O 90 ± 0.01 %; D2O 5 ± 0.01 %

sample_2: talin_domain_C, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; D2O, [U-100% 2H], 5 ± 0.05 %; DTT 2 ± 0.01 mM; sodium chloride 50 ± 0.01 mM; TRIS 20 ± 0.01 mM; H2O 90 ± 0.01 %; D2O 5 ± 0.01 %

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
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN v2.1, Bruker Biospin - collection, processing

CcpNMR v1.13, CCPN - chemical shift assignment, data analysis, peak picking, refinement

ARIA v1.2, Linge, O'Donoghue and Nilges - geometry optimization, refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis, geometry optimization

NMR spectrometers:

Bruker DRX 800 MHz
Bruker DRX 600 MHz
Bruker DRX 600 MHz

PDB	2L10
DBJ	BAA82979 BAC65702 BAE27781 BAG09941
EMBL	CAA39588
GB	AAD13152 AAF23322 AAF27330 AAH42923 AAI00263
PRF	1617167A
REF	NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001084941
SP	P26039 Q9Y490
TPG	DAA26829
AlphaFold	P26039 Q9Y490