BMRB Entry 15458

Name: NMR Structure of the F0 domain (residues 1-85) of the Talin FERM domain
Published: 2010-02-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15458

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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:

NMR Structure of the F0 domain (residues 1-85) of the Talin FERM domain

Deposition date:

2007-09-05

Original release date:

2010-02-18

Authors:

Goult, Benjamin; Elliott, Paul; Roberts, Gordon; Critchley, David; Barsukov, Igor

Citation:

Citation: Goult, Benjamin. "The NMR structure of the F0F1 double domain from the Talin Ferm domain" .

Assembly members:

Assembly members:
F0_domain_of_Talin, polymer, 91 residues, 10339.090 Da.

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: PET-151

Entity Sequences (FASTA):

Entity Sequences (FASTA):
F0_domain_of_Talin: GIDPFTMVALSLKISIGNVV KTMQFEPSTMVYDACRMIRE RIPEALAGPPNDFGLFLSDD DPKKGIWLEAGKALDYYMLR NGDTMEYRKKQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	365
15N chemical shifts	84
1H chemical shifts	599

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 91 residues - 10339.090 Da.

Residues -5 to 0 represent a non-native affinity tag

1

GLY

ILE

ASP

PRO

PHE

THR

MET

VAL

ALA

LEU

2

SER

LEU

LYS

ILE

SER

ILE

GLY

ASN

VAL

3

LYS

THR

MET

GLN

PHE

GLU

PRO

SER

THR

MET

4

VAL

TYR

ASP

ALA

CYS

ARG

MET

ILE

ARG

GLU

5

ARG

ILE

PRO

GLU

ALA

LEU

ALA

GLY

PRO

6

ASN

ASP

PHE

GLY

LEU

PHE

LEU

SER

ASP

7

ASP

PRO

LYS

GLY

ILE

TRP

LEU

GLU

ALA

8

GLY

LYS

ALA

LEU

ASP

TYR

MET

LEU

ARG

9

ASN

GLY

ASP

THR

MET

GLU

TYR

ARG

LYS

10

GLN

Samples:

double-labelled: F0 domain of Talin, [U-100% 13C; U-100% 15N], 1 mM; NaCl 50 mM

single-labelled: F0 domain of Talin, [U-100% 15N], 1 mM; NaCl 50 mM

unlabelled: F0 domain of Talin 1 mM; NaCl 50 mM

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

Software:

TOPSPIN v2.0, Bruker Biospin - collection, processing

CcpNMR v11, CCPN - chemical shift assignment, data analysis, peak picking

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

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement

NMR spectrometers:

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

BMRB	15615
PDB	2KC1 2KMA 3IVF
DBJ	BAC65702 BAE27781
EMBL	CAA39588
GB	AAI50811 EDL02466 EDL02467 EDL98751 EDL98752
PRF	1617167A
REF	NP_001034114 NP_035732 XP_002918927 XP_003341683 XP_003407647
SP	P26039
AlphaFold	P26039