BMRB Entry 16932

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16932

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Title:
Chemical shift assignments of the Talin F2F3 domain (residues 196-405)
Deposition date:
2010-05-14
Original release date:
2010-10-14
Authors:
Goult, Ben
Citation:

Citation: Kalli, Antreas; Wegener, Kate; Goult, Benjamin; Anthis, Nicholas; Campbell, Iain; Sansom, Mark. "The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study."  Structure 18, 1280-1288 (2010).
PubMed: 20947017

Assembly members:

Assembly members:
F2F3, polymer, 216 residues, Formula weight is not available

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):
F2F3: GIDPFTKFFYSDQNVDSRDP VQLNLLYVQARDDILNGSHP VSFDKACEFAGFQCQIQFGP HNEQKHKAGFLDLKDFLPKE YVKQKGERKIFQAHKNCGQM SEIEAKVRYVKLARSLKTYG VSFFLVKEKMKGKNKLVPRL LGITKECVMRVDEKTKEVIQ EWSLTNIKRWAASPKSFTLD FGDYQDGYYSVQTTEGEQIA QLIAGYIDIILKKKKS

Data sets:
Data typeCount
13C chemical shifts207
15N chemical shifts198
1H chemical shifts198

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1F2F31

Entities:

Entity 1, F2F3 216 residues - Formula weight is not available

Residues 1-6 (190-195) represent a non-native affinity tag

1   GLYILEASPPROPHETHRLYSPHEPHETYR
2   SERASPGLNASNVALASPSERARGASPPRO
3   VALGLNLEUASNLEULEUTYRVALGLNALA
4   ARGASPASPILELEUASNGLYSERHISPRO
5   VALSERPHEASPLYSALACYSGLUPHEALA
6   GLYPHEGLNCYSGLNILEGLNPHEGLYPRO
7   HISASNGLUGLNLYSHISLYSALAGLYPHE
8   LEUASPLEULYSASPPHELEUPROLYSGLU
9   TYRVALLYSGLNLYSGLYGLUARGLYSILE
10   PHEGLNALAHISLYSASNCYSGLYGLNMET
11   SERGLUILEGLUALALYSVALARGTYRVAL
12   LYSLEUALAARGSERLEULYSTHRTYRGLY
13   VALSERPHEPHELEUVALLYSGLULYSMET
14   LYSGLYLYSASNLYSLEUVALPROARGLEU
15   LEUGLYILETHRLYSGLUCYSVALMETARG
16   VALASPGLULYSTHRLYSGLUVALILEGLN
17   GLUTRPSERLEUTHRASNILELYSARGTRP
18   ALAALASERPROLYSSERPHETHRLEUASP
19   PHEGLYASPTYRGLNASPGLYTYRTYRSER
20   VALGLNTHRTHRGLUGLYGLUGLNILEALA
21   GLNLEUILEALAGLYTYRILEASPILEILE
22   LEULYSLYSLYSLYSSER

Samples:

sample_1: F2F3 0.5 ± 0.05 mM; DTT 2 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2, Bruker Biospin - collection, processing

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

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

BMRB 15792 16930 16959
PDB
DBJ BAA82979 BAC30516 BAC65702 BAE27781 BAG09941
EMBL CAA39588
GB AAD13152 AAF23322 AAF27330 AAH42923 AAI22767
PRF 1617167A
REF NP_001034114 NP_001192357 NP_006280 NP_035732 NP_989854
SP P26039 P54939 Q9Y490
TPG DAA26829
AlphaFold P26039 P54939 Q9Y490

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