BMRB Entry 25349

Title:
Nedd4 WW3
Deposition date:
2014-11-17
Original release date:
2016-01-25
Authors:
Lecher, Justin; Dingley, Andrew J.; Panwalkar, Vineet
Citation:

Citation: Panwalkar, Vineet; Neudecker, Philipp; Schmitz, Michael; Lecher, Justin; Schulte, Marianne; Medini, Karima; Stoldt, Matthias; Brimble, Margaret; Willbold, Dieter; Dingley, Andrew. "The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria"  Biochemistry 55, 659-674 (2016).
PubMed: 26685112

Assembly members:

Assembly members:
E3_ubiquitin-protein_ligase_Nedd4, polymer, 43 residues, 4966.6205 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: pGEX2TK

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E3_ubiquitin-protein_ligase_Nedd4: GSMEQGFLPKGWEVRHAPNG RPFFIDHNTKTTTWEDPRLK IPA

Data sets:
Data typeCount
13C chemical shifts184
15N chemical shifts44
1H chemical shifts297

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E3 ubiquitin-protein ligase Nedd41

Entities:

Entity 1, E3 ubiquitin-protein ligase Nedd4 43 residues - 4966.6205 Da.

1   GLYSERMETGLUGLNGLYPHELEUPROLYS
2   GLYTRPGLUVALARGHISALAPROASNGLY
3   ARGPROPHEPHEILEASPHISASNTHRLYS
4   THRTHRTHRTRPGLUASPPROARGLEULYS
5   ILEPROALA

Samples:

sample_1: E3 ubiquitin-protein ligase Nedd4, [U-13C; U-15N], 1.5 mM; Na2HPO4 20.0 mM; NaCl 50.0 mM; DSS 0.1 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.050 M; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-13C HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CcpNmr_Analysis v2.4.1, CCPN - Chemical shift assignment

NMR spectrometers:

  • Bruker Avance 599 MHz
  • Varian VNMRS 900 MHz

Related Database Links:

UniProt P46934
AlphaFold D6RF89

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