BMRB Entry 15615

Title:
NMR Structure of the F0F1 double domain (residues 1-202) 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:
F0F1, polymer, 208 residues, 24194.9 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

Data sets:
Data typeCount
13C chemical shifts791
15N chemical shifts192
1H chemical shifts1320

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1F0F11

Entities:

Entity 1, F0F1 208 residues - 24194.9 Da.

Residues -5 to 0 (GIDPFT) represent a non-native expression tag

1   GLYILEASPPROPHETHRMETVALALALEU
2   SERLEULYSILESERILEGLYASNVALVAL
3   LYSTHRMETGLNPHEGLUPROSERTHRMET
4   VALTYRASPALACYSARGMETILEARGGLU
5   ARGILEPROGLUALALEUALAGLYPROPRO
6   ASNASPPHEGLYLEUPHELEUSERASPASP
7   ASPPROLYSLYSGLYILETRPLEUGLUALA
8   GLYLYSALALEUASPTYRTYRMETLEUARG
9   ASNGLYASPTHRMETGLUTYRARGLYSLYS
10   GLNARGPROLEULYSILEARGMETLEUASP
11   GLYTHRVALLYSTHRILEMETVALASPASP
12   SERLYSTHRVALTHRASPMETLEUMETTHR
13   ILECYSALAARGILEGLYILETHRASNHIS
14   ASPGLUTYRSERLEUVALARGGLULEUMET
15   GLUGLULYSLYSASPGLUGLYTHRGLYTHR
16   LEUARGLYSASPLYSTHRLEULEUARGASP
17   GLULYSLYSMETGLULYSLEULYSGLNLYS
18   LEUHISTHRASPASPGLULEUASNTRPLEU
19   ASPHISGLYARGTHRLEUARGGLUGLNGLY
20   VALGLUGLUHISGLUTHRLEULEULEUARG
21   ARGLYSPHEPHETYRSERASPGLN

Samples:

unlabelled: F0F1 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: F0F1, [U-100% 15N], 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; DTT 2 ± 0.05 mM; H2O 90%; D2O 10%

double: F0F1, [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:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15nisotropicsample_conditions_1
2D 1H-13C HSQCdoubleisotropicsample_conditions_1
3D CBCA(CO)NHdoubleisotropicsample_conditions_1
3D HNCOdoubleisotropicsample_conditions_1
3D HNCAdoubleisotropicsample_conditions_1
3D HNCACBdoubleisotropicsample_conditions_1
3D HCCH-TOCSYdoubleisotropicsample_conditions_1
3D 1H-13C NOESYdoubleisotropicsample_conditions_1
3D 1H-15N NOESY15nisotropicsample_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

Related Database Links:

BMRB 15616
PDB
DBJ BAA82979 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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks