BMRB Entry 15016
Click here to enlarge.
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/BMR15016
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of the Su(dx) WW4 - Notch peptide complex PubMed: 17656366
Deposition date: 2006-11-05 Original release date: 2007-10-09
Authors: Avis, Johanna; Blankley, Richard; Jennings, Martin; Golovanov, Alexander
Citation: Jennings, Martin; Blankley, Richard; Baron, Martin; Golovanov, Alexander; Avis, Johanna. "Specificity and Autoregulation of Notch Binding by Tandem WW Domains in Suppressor of Deltex." J. Biol. Chem. 282, 29032-29042 (2007).
Assembly members:
Su(dx), polymer, 53 residues, 5921.61 Da.
Notch, polymer, 21 residues, 2159.40 Da.
Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Su(dx): GPLGSPEFHMVSLINEGPLP
PGWEIRYTAAGERFFVDHNT
RRTTFEDPRPGAP
Notch: GPLGSPNTGAKQPPSYEDCI
K
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 305 |
| 15N chemical shifts | 63 |
| 1H chemical shifts | 414 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | WW4 | 1 |
| 2 | L/PPxY motif | 2 |
Entities:
Entity 1, WW4 53 residues - 5921.61 Da.
Residues 1-10 Represent plasmid derived sequence
| 1 | GLY | PRO | LEU | GLY | SER | PRO | GLU | PHE | HIS | MET | ||||
| 2 | VAL | SER | LEU | ILE | ASN | GLU | GLY | PRO | LEU | PRO | ||||
| 3 | PRO | GLY | TRP | GLU | ILE | ARG | TYR | THR | ALA | ALA | ||||
| 4 | GLY | GLU | ARG | PHE | PHE | VAL | ASP | HIS | ASN | THR | ||||
| 5 | ARG | ARG | THR | THR | PHE | GLU | ASP | PRO | ARG | PRO | ||||
| 6 | GLY | ALA | PRO |
Entity 2, L/PPxY motif 21 residues - 2159.40 Da.
Residues 1-6 are plasmid derived
| 1 | GLY | PRO | LEU | GLY | SER | PRO | ASN | THR | GLY | ALA | ||||
| 2 | LYS | GLN | PRO | PRO | SER | TYR | GLU | ASP | CYS | ILE | ||||
| 3 | LYS |
Samples:
Labelled_WW4: Su(dx), [U-13C; U-15N], 0.4 – 0.6 mM; Notch1.5 – 2.5 mM; sodium chloride 45 mM; DTT 9 mM; EDTA 0.9 mM; Arginine 45 mM; Glutamate 45 mM; D2O 10%
Labelled_Notch: Notch, [U-13C; U-15N], 0.4 – 0.6 mM; Su(dx)1.5 – 2.5 mM; sodium chloride 45 mM; DTT 9 mM; EDTA 0.9 mM; Arginine 45 mM; Glutamate 45 mM; D2O 10%
Standard_conditions: pH: 6.75; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Labelled_WW4 | isotropic | Standard_conditions |
| 2D 1H-15N HSQC | Labelled_Notch | isotropic | Standard_conditions |
| 3D HNCO | Labelled_WW4 | isotropic | Standard_conditions |
| 3D HNCO | Labelled_Notch | isotropic | Standard_conditions |
| 3D HNCA | Labelled_WW4 | isotropic | Standard_conditions |
| 3D HNCA | Labelled_Notch | isotropic | Standard_conditions |
| 3D HNCACB | Labelled_WW4 | isotropic | Standard_conditions |
| 3D HNCACB | Labelled_Notch | isotropic | Standard_conditions |
| 3D HN(CO)CA | Labelled_WW4 | isotropic | Standard_conditions |
| 3D HN(CO)CA | Labelled_Notch | isotropic | Standard_conditions |
| 3D HCCH-TOCSY | Labelled_WW4 | isotropic | Standard_conditions |
| 3D HCCH-TOCSY | Labelled_Notch | isotropic | Standard_conditions |
| 3D 1H-15N NOESY | Labelled_WW4 | isotropic | Standard_conditions |
| 3D 1H-15N NOESY | Labelled_Notch | isotropic | Standard_conditions |
| 3D 1H-15N TOCSY | Labelled_WW4 | isotropic | Standard_conditions |
| 3D 1H-15N TOCSY | Labelled_Notch | isotropic | Standard_conditions |
| 3D 1H-13C NOESY | Labelled_WW4 | isotropic | Standard_conditions |
| 3D 1H-13C NOESY | Labelled_Notch | isotropic | Standard_conditions |
| 2D 1H-13C HSQC | Labelled_WW4 | isotropic | Standard_conditions |
| 2D 1H-13C HSQC | Labelled_Notch | isotropic | Standard_conditions |
Software:
NMRPipe, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - data analysis
CARA, R Keller and K Wuthrich - chemical shift assignment
CYANA v2.1, P Guntert, C Mumenthaler and K Wuthrich - refinement, structure solution
NMRView, B Johnson, One Moon Scientific - peak picking
AMBER, DA Case, TA Darden, TE Cheatham, III, CL Simmerling, J Wang, RE Duke, - refinement
NMR spectrometers:
- Bruker AMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts