BMRB Entry 25394
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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/BMR25394
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Title: complex structure of Dvl PDZ domain with ligand
Deposition date: 2015-12-28 Original release date: 2015-12-28
Authors: Zhang, Xinxin; Zheng, Jie
Citation: Zhang, Xinxin; Zheng, Jie. "Protein-ligand interaction decoded by NMR chemical shift analysis" Not known ., .-..
Assembly members:
entity_1, polymer, 90 residues, 9632.958 Da.
entity_2, polymer, 3 residues, 303.360 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: NIITVTLNMERHHFLGISIV
GQSNDRGDGGIYIGSIMKGG
AVAADGRIEPGDMLLQVNDV
NFENMSNDDAVRVLREIVSQ
TGPISLTVAK
entity_2: XWV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 24 |
| 1H chemical shifts | 65 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 90 residues - 9632.958 Da.
| 1 | ASN | ILE | ILE | THR | VAL | THR | LEU | ASN | MET | GLU | |
| 2 | ARG | HIS | HIS | PHE | LEU | GLY | ILE | SER | ILE | VAL | |
| 3 | GLY | GLN | SER | ASN | ASP | ARG | GLY | ASP | GLY | GLY | |
| 4 | ILE | TYR | ILE | GLY | SER | ILE | MET | LYS | GLY | GLY | |
| 5 | ALA | VAL | ALA | ALA | ASP | GLY | ARG | ILE | GLU | PRO | |
| 6 | GLY | ASP | MET | LEU | LEU | GLN | VAL | ASN | ASP | VAL | |
| 7 | ASN | PHE | GLU | ASN | MET | SER | ASN | ASP | ASP | ALA | |
| 8 | VAL | ARG | VAL | LEU | ARG | GLU | ILE | VAL | SER | GLN | |
| 9 | THR | GLY | PRO | ILE | SER | LEU | THR | VAL | ALA | LYS |
Entity 2, entity_2 3 residues - 303.360 Da.
| 1 | PHQ | TRP | VAL |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 1 mM; entity_2 10 mM; potassium phosphate 100 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz