BMRB Entry 4592
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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/BMR4592
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Title: Solution structure of the syndecan-4 whole cytoplasmic domain in the presence of phosphatidylinositol 4,5-bisphosphate
Deposition date: 2000-05-05 Original release date: 2001-03-06
Authors: Shin, J.; Oh, E.; Lee, D.; Couchman, J.; Lee, W.
Citation: Lee, D.; Oh, E.; Woods, A.; Couchman, J.; Lee, W.. "Solution Structure of a Syndecan-4 Cytoplasmic Domain and Its Interaction with Phosphatidylinositol 4,5-Bisphosphate " J. Biol. Chem. 273, 13022-13029 (1998).
Assembly members:
Syndecan 4, polymer, 28 residues, Formula weight is not available
PT5, non-polymer, 1047.088 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: not reported
Entity Sequences (FASTA):
Syndecan 4: RMKKKDEGSYDLGKKPIYKK
APTNEFYA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 170 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Syndecan 4 monomer 1 | 1 |
| 2 | Syndecan 4 monomer 2 | 1 |
| 3 | PIP2 | 2 |
Entities:
Entity 1, Syndecan 4 monomer 1 28 residues - Formula weight is not available
| 1 | ARG | MET | LYS | LYS | LYS | ASP | GLU | GLY | SER | TYR | ||||
| 2 | ASP | LEU | GLY | LYS | LYS | PRO | ILE | TYR | LYS | LYS | ||||
| 3 | ALA | PRO | THR | ASN | GLU | PHE | TYR | ALA |
Entity 2, PIP2 - C47 H85 O19 P3 - 1047.088 Da.
| 1 | PT5 |
Samples:
sample_1: Syndecan 42 – 4 mM; PIP20.5 – 1 mM; phosphate buffer 50 mM; H2O 90%; D2O 10%
sample_2: Syndecan 42 – 4 mM; PIP20.5 – 1 mM; phosphate buffer 50 mM; D2O 100%
sample_cond_1: pH: 7.4; temperature: 298 K; ionic strength: 50 mM; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | not available | not available | sample_cond_1 |
| DQF COSY | not available | not available | sample_cond_1 |
Software:
XWINNMR v2.5 - data collection, data processing
Sparky v3.6 - data analysis
X-PLOR v3.851 - refinement
NMR spectrometers:
- Bruker DRX 500 MHz