BMRB Entry 16959

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16959

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Chemical shift assignments of the Talin F1F2 double domain (residues 86-303 (delta D139-D168))
Deposition date:
2010-05-27
Original release date:
2014-03-10
Authors:
Goult, Ben; Barsukov, Igor; Roberts, Gordon; Critchley, David
Citation:

Citation: Elliott, Paul; Goult, Benjamin; Kopp, Petra; Bate, Neil; Grossmann, J.; Roberts, Gordon; Critchley, David; Barsukov, Igor. "The Structure of the talin head reveals a novel extended conformation of the FERM domain."  Structure 18, 1288-1299 (2010).
PubMed: 20947018

Assembly members:

Assembly members:
F1F2, polymer, 194 residues, 22616.8 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):
F1F2: GIDPFTRPLKIRMLDGTVKT IMVDDSKTVTDMLMTICARI GITNHDEYSLVRELMEEKKD ELNWLDHGRTLREQGVEEHE TLLLRRKFFYSDQNVDSRDP VQLNLLYVQARDDILNGSHP VSFDKACEFAGFQCQIQFGP HNEQKHKAGFLDLKDFLPKE YVKQKGERKIFQAHKNCGQM SEIEAKVRYVKLAR

Data sets:
Data typeCount
13C chemical shifts558
15N chemical shifts185
1H chemical shifts185

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1F1F21

Entities:

Entity 1, F1F2 194 residues - 22616.8 Da.

Residues 1-6 (80-85) represent a non-native affinity tag

1   GLYILEASPPROPHETHRARGPROLEULYS
2   ILEARGMETLEUASPGLYTHRVALLYSTHR
3   ILEMETVALASPASPSERLYSTHRVALTHR
4   ASPMETLEUMETTHRILECYSALAARGILE
5   GLYILETHRASNHISASPGLUTYRSERLEU
6   VALARGGLULEUMETGLUGLULYSLYSASP
7   GLULEUASNTRPLEUASPHISGLYARGTHR
8   LEUARGGLUGLNGLYVALGLUGLUHISGLU
9   THRLEULEULEUARGARGLYSPHEPHETYR
10   SERASPGLNASNVALASPSERARGASPPRO
11   VALGLNLEUASNLEULEUTYRVALGLNALA
12   ARGASPASPILELEUASNGLYSERHISPRO
13   VALSERPHEASPLYSALACYSGLUPHEALA
14   GLYPHEGLNCYSGLNILEGLNPHEGLYPRO
15   HISASNGLUGLNLYSHISLYSALAGLYPHE
16   LEUASPLEULYSASPPHELEUPROLYSGLU
17   TYRVALLYSGLNLYSGLYGLUARGLYSILE
18   PHEGLNALAHISLYSASNCYSGLYGLNMET
19   SERGLUILEGLUALALYSVALARGTYRVAL
20   LYSLEUALAARG

Samples:

sample_1: F1F2, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 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 HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2, Bruker Biospin - collection, processing

Analysis v2.1.3, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

Related Database Links:

SWS P26039
BMRB 15792 16930 16932
PDB

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