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 15159

Title: Mouse Itch 3rd domain phosphorilated in T30   PubMed: 17437719

Deposition date: 2007-03-06 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-Tillo, 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:
PhosphoI3, polymer, 37 residues, 4360.759 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
PhosphoI3: GAMGPLPPGWEKRTDSNGRV YFVNHNTRIXQWEDPRS

Data sets:
Data typeCount
1H chemical shifts240

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PhosphoI31

Entities:

Entity 1, PhosphoI3 37 residues - 4360.759 Da.

1   GLYALAMETGLYPROLEUPROPROGLYTRP
2   GLULYSARGTHRASPSERASNGLYARGVAL
3   TYRPHEVALASNHISASNTHRARGILETPO
4   GLNTRPGLUASPPROARGSER

Samples:

sample_1: PhosphoI3 1.0 mM; Sodium Phosphate 20 mM; NaCl 100 mM; Sodium Azide 0.02 % v/v

sample_conditions_1: ionic strength: 0.4 M; pH: 6.5; pressure: 1 atm; temperature: 280 K

sample_conditions_2: ionic strength: 0.4 M; pH: 6.5; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_2

Software:

TOPSPIN, Bruker Biospin - collection

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

ARIA, Linge, O, . - structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 15153
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