BMRB Entry 15153

Name: Mouse Itch 3rd WW domain complex with the Epstein-Barr virus latent membrane protein 2A derived peptide EEPPPPYED
Published: 2007-10-24

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PDB ID: 2jo9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15153
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

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:

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).
PubMed: 17437719

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: petM30

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_13C
- assigned_chemical_shifts_N
spectral_peak_list
- 13C_peaks
- 15N_peaks

Data type	Count
13C chemical shifts	118
15N chemical shifts	42
1H chemical shifts	390

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

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

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

BMRB	15159
PDB	1YIU 2JO9 2JOC 4ROF 5DWS
AlphaFold	Q8AZK9