BMRB Entry 18569

Title:
13C, 15N and 1H backbone and sidechain assignments of the ENA-VASP homology 1 (EVH1) domain of the human vasodilator-stimulated phosphoprotein (VASP)
Deposition date:
2012-07-05
Original release date:
2012-07-18
Authors:
Ball, Linda; Peter, Schmieder; Jarchau, Thomas; Walter, Ulrich; Oschkinat, Hartmut
Citation:

Citation: Ball, Linda; Kuehne, Ronald; Hoffmann, Berit; Haefner, Angelika; Schmieder, Peter; Volkmer, Rudolf; Hof, Martin; Wahl, Martin; Schneider-Mergener, Jens; Walter, Ulrich; Oschkinat, Hartmut; Jarchau, Thomas. "Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity"  EMBO J. 19, 4903-4914 (2000).
PubMed: 10990454

Assembly members:

Assembly members:
EVH1, polymer, 115 residues, 12732.3 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-4T-1 (Pharmacia)

Data sets:
Data typeCount
13C chemical shifts371
15N chemical shifts137
1H chemical shifts789

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EVH11

Entities:

Entity 1, EVH1 115 residues - 12732.3 Da.

1   METSERGLUTHRVALILECYSSERSERARG
2   ALATHRVALMETLEUTYRASPASPGLYASN
3   LYSARGTRPLEUPROALAGLYTHRGLYPRO
4   GLNALAPHESERARGVALGLNILETYRHIS
5   ASNPROTHRALAASNSERPHEARGVALVAL
6   GLYARGLYSMETGLNPROASPGLNGLNVAL
7   VALILEASNCYSALAILEVALARGGLYVAL
8   LYSTYRASNGLNALATHRPROASNPHEHIS
9   GLNTRPARGASPALAARGGLNVALTRPGLY
10   LEUASNPHEGLYSERLYSGLUASPALAALA
11   GLNPHEALAALAGLYMETALASERALALEU
12   GLUALALEUGLUGLY

Samples:

sample_1: EVH1, [U-100% 15N], 2 mM; D2O 10%; potassium phosphate, pH 6.0 20 mM; potassium chloride 50 mM; sodium azide 0.2 mM

sample_2: EVH1, [U-100% 13C; U-100% 15N], 1.3 mM; D2O 10%; potassium phosphate, pH 6.0 20 mM; potassium chloride 50 mM; sodium azide 0.2 mM

sample_3: EVH1, [U-100% 13C; U-100% 15N], 1.3 mM; D2O 100%; potassium phosphate, pH 6.0 20 mM; potassium chloride 50 mM; sodium azide 0.2 mM

sample_4: EVH1, [U-100% 15N], 2 mM; D2O 100%; potassium phosphate, pH 6.0 20 mM; potassium chloride 50 mM; sodium azide 0.2 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

sample_conditions_2: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

sample_conditions_3: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

sample_conditions_4: ionic strength: 0.07 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D CBCANHsample_2isotropicsample_conditions_2
3D C(CO)NHsample_2isotropicsample_conditions_2
3D H(CCO)NHsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_3
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_3isotropicsample_conditions_3
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
2D 1H-15N HSQC exchange seriessample_4isotropicsample_conditions_4
2D 15N T1 and T2 relaxation seriessample_1isotropicsample_conditions_1
2D 15N-1H heteronuclear NOE on and offsample_1isotropicsample_conditions_1

Software:

AZARA v2.1, Boucher - peak picking, processing

xwinnmr v1.3, Bruker Biospin - collection, processing

ANSIG v3.3, Kraulis - data analysis, peak picking

CNS v0.9a, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DMX 750 MHz

Related Database Links:

PDB
UNP P50552
SP P50552
NCBI GI:1718079
AlphaFold Q93035

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