BMRB Entry 15616

Name: NMR Structure of the F1 domain (residues 86-202) of the Talin FERM domain
Published: 2010-02-18

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15616

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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 F1 domain (residues 86-202) of the Talin FERM domain

Deposition date:

2008-01-04

Original release date:

2010-02-18

Authors:

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

Citation:

Citation: Goult, Benjamin; Elliott, Paul; Roberts, Gordon; Critchley, David; Barsukov, Igor. "The NMR Structure of the F0F1 double domain (Residues 1-202) from the talin FERM domain" .

Assembly members:

Assembly members:
F1, polymer, 128 residues, 15001.2 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):
F1: SSGLVPRGSHMRPLKIRMLD GTVKTIMVDDSKTVTDMLMT ICARIGITNHDEYSLVRELM EEKKDEGTGTLRKDKTLLRD EKKMEKLKQKLHTDDELNWL DHGRTLREQGVEEHETLLLR RKFFYSDQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	517
15N chemical shifts	132
1H chemical shifts	804

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	F1	1

Entities:

Entity 1, F1 128 residues - 15001.2 Da.

Residues 75 to 85 (SSGLVPRGSHM) represent a non-native expression tag

1

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

2

MET

ARG

PRO

LEU

LYS

ILE

ARG

MET

LEU

ASP

3

GLY

THR

VAL

LYS

THR

ILE

MET

VAL

ASP

4

SER

LYS

THR

VAL

THR

ASP

MET

LEU

MET

THR

5

ILE

CYS

ALA

ARG

ILE

GLY

ILE

THR

ASN

HIS

6

ASP

GLU

TYR

SER

LEU

VAL

ARG

GLU

LEU

MET

7

GLU

LYS

ASP

GLU

GLY

THR

GLY

THR

8

LEU

ARG

LYS

ASP

LYS

THR

LEU

ARG

ASP

9

GLU

LYS

MET

GLU

LYS

LEU

LYS

GLN

LYS

10

LEU

HIS

THR

ASP

GLU

LEU

ASN

TRP

LEU

11

ASP

HIS

GLY

ARG

THR

LEU

ARG

GLU

GLN

GLY

12

VAL

GLU

HIS

GLU

THR

LEU

ARG

13

ARG

LYS

PHE

TYR

SER

ASP

GLN

Samples:

unlabelled: F1 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; DTT 2 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; H2O 90%; D2O 10%

15n: F1, [U-100% 15N], 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; DTT 2 ± 0.05 mM; H2O 90%; D2O 10%

double: F1, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; DTT 2 ± 0.05 mM; H2O 90%; D2O 10%

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

Software:

TOPSPIN v2.0, Bruker Biospin - collection, processing

Analysis v1.015, 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	2KC2
DBJ	BAA82979 BAC30516 BAC65702 BAE27781 BAG09941
EMBL	CAA39588
GB	AAD13152 AAF23322 AAF27330 AAH42923 AAI50811
PRF	1617167A
REF	NP_001034114 NP_006280 NP_035732 XP_001084941 XP_001504543
SP	P26039 Q9Y490
AlphaFold	P26039 Q9Y490