BMRB Entry 27205
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27205
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Hs. Par3 PDZ3 domain PubMed: 29440511
Deposition date: 2017-08-07 Original release date: 2018-02-15
Authors: Wiesner, Silke
Citation: Renschler, Fabian; Bruekner, Susanne; Salomon, Paulin; Mukherjee, Amrita; Kullmann, Lars; Schutz-Stoffregen, Mira; Henzler, Christine; Pawson, Tony; Krahn, Michael; Wiesner, Silke. "Structural basis for the interaction between the cell polarity proteins Par3 and Par6" Sci. Signal. 11, 9899-9899 (2018).
Assembly members:
Par3_PDZ3_domain, polymer, 107 residues, Formula weight is not available
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 Vector: pETM-41
Entity Sequences (FASTA):
Par3_PDZ3_domain: GAMGTREFLTFEVPLNDSGS
AGLGVSVKGNRSKENHADLG
IFVKSIINGGAASKDGRLRV
NDQLIAVNGESLLGKTNQDA
METLRRSMSTEGNKRGMIQL
IVARRIS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 190 |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hs. Par3 PDZ3 domain | 1 |
Entities:
Entity 1, Hs. Par3 PDZ3 domain 107 residues - Formula weight is not available
The N-terminal 4 residues (GAMG) are the result of the NcoI restriction site.
| 1 | GLY | ALA | MET | GLY | THR | ARG | GLU | PHE | LEU | THR | ||||
| 2 | PHE | GLU | VAL | PRO | LEU | ASN | ASP | SER | GLY | SER | ||||
| 3 | ALA | GLY | LEU | GLY | VAL | SER | VAL | LYS | GLY | ASN | ||||
| 4 | ARG | SER | LYS | GLU | ASN | HIS | ALA | ASP | LEU | GLY | ||||
| 5 | ILE | PHE | VAL | LYS | SER | ILE | ILE | ASN | GLY | GLY | ||||
| 6 | ALA | ALA | SER | LYS | ASP | GLY | ARG | LEU | ARG | VAL | ||||
| 7 | ASN | ASP | GLN | LEU | ILE | ALA | VAL | ASN | GLY | GLU | ||||
| 8 | SER | LEU | LEU | GLY | LYS | THR | ASN | GLN | ASP | ALA | ||||
| 9 | MET | GLU | THR | LEU | ARG | ARG | SER | MET | SER | THR | ||||
| 10 | GLU | GLY | ASN | LYS | ARG | GLY | MET | ILE | GLN | LEU | ||||
| 11 | ILE | VAL | ALA | ARG | ARG | ILE | SER |
Samples:
sample_1: Par3 PDZ3 domain, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
XEASY, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts