BMRB Entry 15153
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15153
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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 Host organism: Escherichia coli
Entity Sequences (FASTA):
WW3: GAMGPLPPGWEKRTDSNGRV
YFVNHNTRITQWEDPRS
Ligand: EEPPPPYED
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 118 |
| 15N chemical shifts | 42 |
| 1H chemical shifts | 390 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | WW3 | 1 |
| 2 | Ligand | 2 |
Entities:
Entity 1, WW3 37 residues - 3720.131 Da.
| 1 | GLY | ALA | MET | GLY | PRO | LEU | PRO | PRO | GLY | TRP | ||||
| 2 | GLU | LYS | ARG | THR | ASP | SER | ASN | GLY | ARG | VAL | ||||
| 3 | TYR | PHE | VAL | ASN | HIS | ASN | THR | ARG | ILE | THR | ||||
| 4 | GLN | TRP | GLU | ASP | PRO | ARG | SER |
Entity 2, Ligand 9 residues - 1076.122 Da.
| 1 | GLU | GLU | PRO | PRO | PRO | PRO | TYR | GLU | ASP |
Samples:
1H: WW3 1.0 mM; Ligand 3.0 mM; Sodium Phosphate 20 mM; NaCl 100 mM; Sodium Azide 0.02 v/v %
15N: WW3, [U-100% 15N], 1.0 mM; Ligand 3.0 mM; Sodium Phosphate 20 mM; NaCl 100 mM; Sodium Azide 0.02 v/v %
15N-13C: WW3, [U-100% 13C; U-100% 15N], 1.0 mM; Ligand 3.0 mM; Sodium Phosphate 20 mM; NaCl 100 mM; Sodium Azide 0.02 v/v %
Standard: ionic strength: 0.4 M; pH: 6.7; pressure: 1 atm; temperature: 285 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | 15N-13C | isotropic | Standard |
| 3D CBCANH | 15N-13C | isotropic | Standard |
| 2D 1H-15N HSQC | 15N | isotropic | Standard |
| 3D 1H-15N NOESY | 15N | isotropic | Standard |
| 3D 1H-15N TOCSY | 15N | isotropic | Standard |
| 3D 1H-13C NOESY | 15N-13C | isotropic | Standard |
| 3D 1H-13C TOCSY | 15N-13C | isotropic | Standard |
| 2D 1H-1H NOESY | 1H | isotropic | Standard |
| 2D 1H-1H TOCSY | 1H | isotropic | Standard |
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