BMRB Entry 27198
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27198
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Dm. Par3 PDZ3 domain PubMed: 29440511
Deposition date: 2017-08-02 Original release date: 2018-02-15
Authors: Susanne, Bruekner; Fabian, Renschler; Silke, Wiesner
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, 108 residues, Formula weight is not available
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 Vector: pETM-30
Entity Sequences (FASTA):
Par3_PDZ3_domain: NSWHSREELTLHIPVHDTEK
AGLGVSVKGKTCSDGDLGIF
VKNVIHGGAASRDGRLRMND
QLLSVNGVSLRGQNNAEAME
TLRRAMVNTPGKHPGTITLL
VGRKILRS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 268 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 89 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Par3 PDZ3 domain | 1 |
Entities:
Entity 1, Par3 PDZ3 domain 108 residues - Formula weight is not available
Residues 667-685 of the natural sequence were deleted from the domain
| 1 | ASN | SER | TRP | HIS | SER | ARG | GLU | GLU | LEU | THR | ||||
| 2 | LEU | HIS | ILE | PRO | VAL | HIS | ASP | THR | GLU | LYS | ||||
| 3 | ALA | GLY | LEU | GLY | VAL | SER | VAL | LYS | GLY | LYS | ||||
| 4 | THR | CYS | SER | ASP | GLY | ASP | LEU | GLY | ILE | PHE | ||||
| 5 | VAL | LYS | ASN | VAL | ILE | HIS | GLY | GLY | ALA | ALA | ||||
| 6 | SER | ARG | ASP | GLY | ARG | LEU | ARG | MET | ASN | ASP | ||||
| 7 | GLN | LEU | LEU | SER | VAL | ASN | GLY | VAL | SER | LEU | ||||
| 8 | ARG | GLY | GLN | ASN | ASN | ALA | GLU | ALA | MET | GLU | ||||
| 9 | THR | LEU | ARG | ARG | ALA | MET | VAL | ASN | THR | PRO | ||||
| 10 | GLY | LYS | HIS | PRO | GLY | THR | ILE | THR | LEU | LEU | ||||
| 11 | VAL | GLY | ARG | LYS | ILE | LEU | ARG | 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: 293 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 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
XEASY, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts