BMRB Entry 15625

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15625

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

Title:
NMR Structure of the VBS3 domain (residues 1815-1973) of Talin
Deposition date:
2008-01-10
Original release date:
2008-09-19
Authors:
Goult, Benjamin; Gingras, Alexandre; Critchley, David; Barsukov, Igor
Citation:

Citation: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Barsukov, Igor; Critchley, David; Roberts, Gordon. "The domain structure of talin: Residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site."  FEBS Lett 584, 2237-2241 (2010).
PubMed: 20399778

Assembly members:

Assembly members:
VBS3, polymer, 165 residues, 17263.3 Da.

Natural source:

Natural source:   Common Name: not available   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):
VBS3: GIDPFTNEAASAAGVVGGMV DSITQAINQLDEGPMGDPEG SFVDYQTTMVRTAKAIAVTV QEMVTKSNTSPEELGPLANQ LTSDYGRLASQAKPAAVAAE NEEIGAHIKHRVQELGHGCS ALVTKAGALQCSPSDVYTKK ELIECARRVSEKVSHVLAAL QAGNR

Data sets:
Data typeCount
13C chemical shifts521
15N chemical shifts171
1H chemical shifts1107

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VBS31

Entities:

Entity 1, VBS3 165 residues - 17263.3 Da.

Residues 1809 to 1814 (GIDPFT) represent a non-native expression tag

1   GLYILEASPPROPHETHRASNGLUALAALA
2   SERALAALAGLYVALVALGLYGLYMETVAL
3   ASPSERILETHRGLNALAILEASNGLNLEU
4   ASPGLUGLYPROMETGLYASPPROGLUGLY
5   SERPHEVALASPTYRGLNTHRTHRMETVAL
6   ARGTHRALALYSALAILEALAVALTHRVAL
7   GLNGLUMETVALTHRLYSSERASNTHRSER
8   PROGLUGLULEUGLYPROLEUALAASNGLN
9   LEUTHRSERASPTYRGLYARGLEUALASER
10   GLNALALYSPROALAALAVALALAALAGLU
11   ASNGLUGLUILEGLYALAHISILELYSHIS
12   ARGVALGLNGLULEUGLYHISGLYCYSSER
13   ALALEUVALTHRLYSALAGLYALALEUGLN
14   CYSSERPROSERASPVALTYRTHRLYSLYS
15   GLULEUILEGLUCYSALAARGARGVALSER
16   GLULYSVALSERHISVALLEUALAALALEU
17   GLNALAGLYASNARG

Samples:

unlabelled: VBS3 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: VBS3, [U-100% 15N], 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; DTT 2 ± 0.05 mM; H2O 90%; D2O 10%

double: VBS3, [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:

PDB
DBJ BAC65702 BAE27781 BAE41923 BAE42391
EMBL CAA39588
GB AAH18557 AAI00263 AAI21788 AAI50811 EDL02465
PRF 1617167A
REF NP_001034114 NP_001192357 NP_035732 XP_001504543 XP_002918927
SP P26039
TPG DAA26829
AlphaFold P26039

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