BMRB Entry 17529
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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/BMR17529
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Title: Third WW domain of human Nedd4L in complex with doubly phosphorylated human smad3 derived peptide. PubMed: 21685363
Deposition date: 2011-03-16 Original release date: 2011-06-23
Authors: Macias, Maria; Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan
Citation: Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan; Macias, Maria. "A Smad action turnover switch operated by WW domain readers of a phosphoserine code." Genes Dev. 25, 1275-1288 (2011).
Assembly members:
NEDD4LWW3, polymer, 44 residues, 4822.491 Da.
SMAD3, polymer, 10 residues, 1112.977 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):
NEDD4LWW3: GAMEQSFLPPGWEMRIAPNG
RPFFYDHNTKTTTWEDPRLK
FPVH
SMAD3: AGXPNLXPNP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 61 |
| 15N chemical shifts | 22 |
| 1H chemical shifts | 276 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NEDD4LWW3 | 1 |
| 2 | SMAD3 | 2 |
Entities:
Entity 1, NEDD4LWW3 44 residues - 4822.491 Da.
| 1 | GLY | ALA | MET | GLU | GLN | SER | PHE | LEU | PRO | PRO | ||||
| 2 | GLY | TRP | GLU | MET | ARG | ILE | ALA | PRO | ASN | GLY | ||||
| 3 | ARG | PRO | PHE | PHE | TYR | ASP | HIS | ASN | THR | LYS | ||||
| 4 | THR | THR | THR | TRP | GLU | ASP | PRO | ARG | LEU | LYS | ||||
| 5 | PHE | PRO | VAL | HIS |
Entity 2, SMAD3 10 residues - 1112.977 Da.
| 1 | ALA | GLY | SEP | PRO | ASN | LEU | SEP | PRO | ASN | PRO |
Samples:
H: NEDD4LWW3 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%
15N: NEDD4LWW3, [U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%
15N13C: NEDD4LWW3, [U-100% 13C; U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.420 M; pH: 7; pressure: 1 atm; temperature: 285 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | H | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | H | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 15N13C | isotropic | sample_conditions_1 |
| 3D HNCACB | 15N13C | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | 15N | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
XEASY, Bartels et al. - chemical shift assignment
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts