BMRB Entry 27204
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27204
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NMR-STAR v3 text file.
XML gzip file.
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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).
PubMed: 29440511
Assembly members:
Par3_PDZ2_domain, polymer, 96 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_PDZ2_domain: GAMGKRLNIQLKKGTEGLGF
SITSRDVTIGGSAPIYVKNI
LPRGAAIQDGRLKAGDRLIE
VNGVDLVGKSQEEVVSLLRS
TKMEGTVSLLVFRQED
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 89 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hs. Par3 PDZ2 domain | 1 |
Entities:
Entity 1, Hs. Par3 PDZ2 domain 96 residues - Formula weight is not available
| 1 | GLY | ALA | MET | GLY | LYS | ARG | LEU | ASN | ILE | GLN | ||||
| 2 | LEU | LYS | LYS | GLY | THR | GLU | GLY | LEU | GLY | PHE | ||||
| 3 | SER | ILE | THR | SER | ARG | ASP | VAL | THR | ILE | GLY | ||||
| 4 | GLY | SER | ALA | PRO | ILE | TYR | VAL | LYS | ASN | ILE | ||||
| 5 | LEU | PRO | ARG | GLY | ALA | ALA | ILE | GLN | ASP | GLY | ||||
| 6 | ARG | LEU | LYS | ALA | GLY | ASP | ARG | LEU | ILE | GLU | ||||
| 7 | VAL | ASN | GLY | VAL | ASP | LEU | VAL | GLY | LYS | SER | ||||
| 8 | GLN | GLU | GLU | VAL | VAL | SER | LEU | LEU | ARG | SER | ||||
| 9 | THR | LYS | MET | GLU | GLY | THR | VAL | SER | LEU | LEU | ||||
| 10 | VAL | PHE | ARG | GLN | GLU | ASP |
Samples:
sample_1: Par3 PDZ2 domain, [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: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
XEASY, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks