BMRB Entry 25349
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25349
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: Nedd4 WW3 PubMed: 26685112
Deposition date: 2014-11-17 Original release date: 2016-01-25
Authors: Lecher, Justin; Dingley, Andrew J.; Panwalkar, Vineet
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).
Assembly members:
E3_ubiquitin-protein_ligase_Nedd4, polymer, 43 residues, 4966.6205 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX2TK
Entity Sequences (FASTA):
E3_ubiquitin-protein_ligase_Nedd4: GSMEQGFLPKGWEVRHAPNG
RPFFIDHNTKTTTWEDPRLK
IPA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 184 |
| 15N chemical shifts | 44 |
| 1H chemical shifts | 297 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E3 ubiquitin-protein ligase Nedd4 | 1 |
Entities:
Entity 1, E3 ubiquitin-protein ligase Nedd4 43 residues - 4966.6205 Da.
| 1 | GLY | SER | MET | GLU | GLN | GLY | PHE | LEU | PRO | LYS | ||||
| 2 | GLY | TRP | GLU | VAL | ARG | HIS | ALA | PRO | ASN | GLY | ||||
| 3 | ARG | PRO | PHE | PHE | ILE | ASP | HIS | ASN | THR | LYS | ||||
| 4 | THR | THR | THR | TRP | GLU | ASP | PRO | ARG | LEU | LYS | ||||
| 5 | ILE | PRO | ALA |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNmr_Analysis v2.4.1, CCPN - Chemical shift assignment
NMR spectrometers:
- Bruker Avance 599 MHz
- Varian VNMRS 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts