BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 6285

Title: 15N, 13C, 1H NMR assignment of a 14kDa construct of the focal adhesion protein Talin   PubMed: 15642262

Deposition date: 2004-08-09 Original release date: 2007-03-22

Authors: Fillingham, Ian; Critchley, David; Roberts, Gordon; Barsukov, Igor

Citation: Fillingham, Ian; Gingras, A.; Papagrigoriou, E.; Patel, B.; Emsley, J.; Critchley, D.; Roberts, Gordon; Barsukov, Ian. "A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head"  Structure 13, 65-74 (2005).

Assembly members:
talin 755-889, polymer, 139 residues, Formula weight is not available

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Animalia   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
talin 755-889: GSHMQAATEDGQLLRGVGAA ATAVTQALNELLQHVKAHAT GAGPAGRYDQATDTILTVTE NIFSSMGDAGEMVRQARILA QATSDLVNAIKADAEGESDL ENSRKLLSAAKILADATAKM VEAAKGAAAHPDSEEQQQR

Data sets:
Data typeCount
15N chemical shifts141
1H chemical shifts864
13C chemical shifts520

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1talin 755-8891

Entities:

Entity 1, talin 755-889 139 residues - Formula weight is not available

1   GLYSERHISMETGLNALAALATHRGLUASP
2   GLYGLNLEULEUARGGLYVALGLYALAALA
3   ALATHRALAVALTHRGLNALALEUASNGLU
4   LEULEUGLNHISVALLYSALAHISALATHR
5   GLYALAGLYPROALAGLYARGTYRASPGLN
6   ALATHRASPTHRILELEUTHRVALTHRGLU
7   ASNILEPHESERSERMETGLYASPALAGLY
8   GLUMETVALARGGLNALAARGILELEUALA
9   GLNALATHRSERASPLEUVALASNALAILE
10   LYSALAASPALAGLUGLYGLUSERASPLEU
11   GLUASNSERARGLYSLEULEUSERALAALA
12   LYSILELEUALAASPALATHRALALYSMET
13   VALGLUALAALALYSGLYALAALAALAHIS
14   PROASPSERGLUGLUGLNGLNGLNARG

Samples:

sample_1: talin 755-889, [U-95% 13C; U-98% 15N], 1 mM; phosphate buffer 20 mM; sodium chloride 50 mM

sample_conditions: pH: 6.5; temperature: 303 K; ionic strength: 0.05 M

Experiments:

NameSampleSample stateSample conditions
not availablesample_1not availablesample_conditions

Software:

No software information available

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 17332
PDB
DBJ BAA82979 BAC65702 BAE27781 BAG09941
EMBL CAA39588
GB AAD13152 AAF23322 AAF27330 AAH42923 AAI50811
PRF 1617167A
REF NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001084941
SP P26039 Q9Y490

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts