BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17332

Title: Solution Structure of the talin Vbs2b domain

Deposition date: 2010-12-02 Original release date: 2012-07-25

Authors: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Roberts, Gordon; Barsukov, Igor; Critchley, David

Citation: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Roberts, Gordon; Barsukov, Igor; Critchley, David. "High resolution NMR structure of gpW (W protein of bacteriophage lambda) at acidic pH"  Not known ., .-..

Assembly members:
Vbs2b, polymer, 131 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Vbs2b: GIDPFTAHATGAGPAGRYDQ ATDTILTVTENIFSSMGDAG EMVRQARILAQATSDLVNAI KADAEGESDLENSRKLLSAA KILADATAKMVEAAKGAAAH PDSEEQQQRLREAAEGLRMA TNAAAQNAIKK

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts148
1H chemical shifts877

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1vbs2b1

Entities:

Entity 1, vbs2b 131 residues - Formula weight is not available

Residues 1-6 (781-786) represent a non-native affinity tag

1   GLYILEASPPROPHETHRALAHISALATHR
2   GLYALAGLYPROALAGLYARGTYRASPGLN
3   ALATHRASPTHRILELEUTHRVALTHRGLU
4   ASNILEPHESERSERMETGLYASPALAGLY
5   GLUMETVALARGGLNALAARGILELEUALA
6   GLNALATHRSERASPLEUVALASNALAILE
7   LYSALAASPALAGLUGLYGLUSERASPLEU
8   GLUASNSERARGLYSLEULEUSERALAALA
9   LYSILELEUALAASPALATHRALALYSMET
10   VALGLUALAALALYSGLYALAALAALAHIS
11   PROASPSERGLUGLUGLNGLNGLNARGLEU
12   ARGGLUALAALAGLUGLYLEUARGMETALA
13   THRASNALAALAALAGLNASNALAILELYS
14   LYS

Samples:

15N: Vbs2b, [U-100% 15N], 1 ± 0.05 mM; D2O, [U-100% 2H], 10 ± 0.01 %; sodium chloride 50 ± 0.01 mM; DTT 2 ± 0.01 mM; TRIS 20 ± 0.01 mM; H2O 90 ± 0.01 %

double: Vbs2b, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; D2O, [U-100% 2H], 10 ± 0.01 %; sodium chloride 50 ± 0.01 mM; DTT 2 ± 0.01 mM; TRIS 20 ± 0.01 mM; H2O 90 ± 0.01 %

D20: Vbs2b, [U-100% 15N], 1 ± 0.05 mM; D2O, [U-100% 2H], 100 ± 0.01 %; sodium chloride 50 ± 0.01 mM; DTT 2 ± 0.01 mM; TRIS 20 ± 0.01 mM

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
2D 1H-1H NOESYD20isotropicsample_conditions_1
3D CBCA(CO)NHdoubleisotropicsample_conditions_1
3D HCCH-TOCSYdoubleisotropicsample_conditions_1
3D HNCAdoubleisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-13C NOESYdoubleisotropicsample_conditions_1
3D HNCOdoubleisotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O, . - geometry optimization, refinement, structure solution

CCPNAnalysis v1.15, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAA82979 BAC65702 BAE27781 BAG09941
EMBL CAA39588
GB AAD13152 AAF23322 AAF27330 AAH42923 AAI00263
PRF 1617167A
REF NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001084941
SP P26039 Q9Y490
TPG DAA26829

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