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 15153

Title: Mouse Itch 3rd WW domain complex with the Epstein-Barr virus latent membrane protein 2A derived peptide EEPPPPYED   PubMed: 17437719

Deposition date: 2007-03-01 Original release date: 2007-10-24

Authors: Macias, Maria; Shaw, Alison; Martin-Malpartida, Pau; Morales, Begonya; Ruiz, Lidia; Ramirez-Espain, Ximena; Yraola, Francesc; Royo, Miriam

Citation: Morales, Begonya; Ramirez-Espain, Ximena; Shaw, Alison; Martin-Malpartida, Pau; Yraola, Francesc; Sanchez-Till, Ester; Farrera, Consol; Celada, Antonio; Royo, Miriam; Macias, Maria. "NMR structural studies of the ItchWW3 domain reveal that phosphorylation at T30 inhibits the interaction with PPxY-containing ligands."  Structure 15, 473-483 (2007).

Assembly members:
WW3, polymer, 37 residues, 3720.131 Da.
Ligand, polymer, 9 residues, 1076.122 Da.

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

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
WW3: GAMGPLPPGWEKRTDSNGRV YFVNHNTRITQWEDPRS
Ligand: EEPPPPYED

Data sets:
Data typeCount
13C chemical shifts118
15N chemical shifts42
1H chemical shifts390

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1WW31
2Ligand2

Entities:

Entity 1, WW3 37 residues - 3720.131 Da.

1   GLYALAMETGLYPROLEUPROPROGLYTRP
2   GLULYSARGTHRASPSERASNGLYARGVAL
3   TYRPHEVALASNHISASNTHRARGILETHR
4   GLNTRPGLUASPPROARGSER

Entity 2, Ligand 9 residues - 1076.122 Da.

1   GLUGLUPROPROPROPROTYRGLUASP

Samples:

1H: WW3 1.0 mM; Ligand 3.0 mM; Sodium Phosphate' 'natural abundance; natural abundance; .

15N: WW3, [U-100% 15N], 1.0 mM; Ligand 3.0 mM; Sodium Phosphate' 'natural abundance; natural abundance; .

15N-13C: WW3, [U-100% 13C; U-100% 15N], 1.0 mM; Ligand 3.0 mM; Sodium Phosphate' 'natural abundance; natural abundance; .

Standard: ionic strength: 0.4 M; pH: 6.7; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NH15N-13CisotropicStandard
3D CBCANH15N-13CisotropicStandard
2D 1H-15N HSQC15NisotropicStandard
3D 1H-15N NOESY15NisotropicStandard
3D 1H-15N TOCSY15NisotropicStandard
3D 1H-13C NOESY15N-13CisotropicStandard
3D 1H-13C TOCSY15N-13CisotropicStandard
2D 1H-1H NOESY1HisotropicStandard
2D 1H-1H TOCSY1HisotropicStandard

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ARIA, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 15159
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