BMRB Entry 16575
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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/BMR16575
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Title: HUMAN NEDD4 3RD WW DOMAIN COMPLEX WITH EBOLA ZAIRE VIRUS MATRIX PROTEIN VP40 DERIVED PEPTIDE ILPTAPPEYMEA
Deposition date: 2009-10-23 Original release date: 2015-06-19
Authors: Iglesias-Bexiga, Manuel; Luque, Irene; Macias, Maria; Blanco, Francisco; Cobos, Eva; Bonet, Roman
Citation: Iglesias-Bexiga, Manuel. "HUMAN NEDD4 3RD WW DOMAIN COMPLEX WITH EBOLA ZAIRE VIRUS MATRIX PROTEIN VP40 DERIVED PEPTIDE" Not known ., .-..
Assembly members:
NEDD4-WW3, polymer, 49 residues, 4213.847 Da.
ILPTAPPEYMEA, polymer, 12 residues, 1008.108 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
Entity Sequences (FASTA):
NEDD4-WW3: GAMGPSEIEQGFLPKGWEVR
HAPNGRPFFIDHNTKTTTWE
DPRLKIPAH
ILPTAPPEYMEA: ILPTAPPEYMEA
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 45 |
| 1H chemical shifts | 398 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NEDD4-WW3 | 1 |
| 2 | ILPTAPPEYMEA | 2 |
Entities:
Entity 1, NEDD4-WW3 49 residues - 4213.847 Da.
Residues 1-4 represent a non-native cloning tag resulting from TEV cleavage
| 1 | GLY | ALA | MET | GLY | PRO | SER | GLU | ILE | GLU | GLN | ||||
| 2 | GLY | PHE | LEU | PRO | LYS | GLY | TRP | GLU | VAL | ARG | ||||
| 3 | HIS | ALA | PRO | ASN | GLY | ARG | PRO | PHE | PHE | ILE | ||||
| 4 | ASP | HIS | ASN | THR | LYS | THR | THR | THR | TRP | GLU | ||||
| 5 | ASP | PRO | ARG | LEU | LYS | ILE | PRO | ALA | HIS |
Entity 2, ILPTAPPEYMEA 12 residues - 1008.108 Da.
| 1 | ILE | LEU | PRO | THR | ALA | PRO | PRO | GLU | TYR | MET | ||||
| 2 | GLU | ALA |
Samples:
15nSAMPLE: PROTEIN, [U-100% 15N], 1 mM; PEPTIDE 10 mM; sodium phosphate 20 mM; sodium azide 0.02 v/v; H2O 90%; D2O 10%
15N13Csample: PROTEIN, [U-100% 13C; U-100% 15N], 0.5 mM; PEPTIDE 5 mM; sodium phosphate 20 mM; sodium azide 0.02 v/v; H2O 90%; D2O 10%
sample_conditions_1: pH: 7.00; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 15nSAMPLE | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | 15nSAMPLE | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | 15nSAMPLE | isotropic | sample_conditions_1 |
Software:
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
TOPSPIN, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts