BMRB Entry 53394
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53394
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Lalic, Milena; Thomsen, Elisabeth; Thomasen, F.; Udupa, Aditya; Andersen, Emma; Kuppermann, Sonja; Christensen, Casper; Holm-Olesen, Emma; Saar, Daniel; Prestel, Andreas; Bauer, Lukas; McKenna, Joseph; Olsen, Johan; Mandrup, Susanne; Hartmann-Petersen, Rasmus; Jeffries, Cy; Staller, Max; Lindorff-Larsen, Kresten; Kragelund, Birthe. "Autoinhibition of untimely DNA binding by structural disorder in the full-length peroxisome proliferator-activated receptors (PPARs)
" Nat. Commun. ., .-. (2026).
Assembly members:
entity_1, polymer, 137 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: pET24a
Entity Sequences (FASTA):
entity_1: MGETLGDSPIDPESDSFTDT
LSANISQEMTMVDTEMPFWP
TNFGISSVDLSVMEDHSHSF
DIKPFTTVDFSSISTPHYED
IPFTRTDPVVADYKYDLKLQ
EYQSAIKVEPASPPYYSEKT
QLYNKPHEEPSNSLMAI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 251 |
| 15N chemical shifts | 122 |
| 1H chemical shifts | 122 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PPARg2 AB domain | 1 |
Entities:
Entity 1, PPARg2 AB domain 137 residues - Formula weight is not available
| 1 | MET | GLY | GLU | THR | LEU | GLY | ASP | SER | PRO | ILE | ||||
| 2 | ASP | PRO | GLU | SER | ASP | SER | PHE | THR | ASP | THR | ||||
| 3 | LEU | SER | ALA | ASN | ILE | SER | GLN | GLU | MET | THR | ||||
| 4 | MET | VAL | ASP | THR | GLU | MET | PRO | PHE | TRP | PRO | ||||
| 5 | THR | ASN | PHE | GLY | ILE | SER | SER | VAL | ASP | LEU | ||||
| 6 | SER | VAL | MET | GLU | ASP | HIS | SER | HIS | SER | PHE | ||||
| 7 | ASP | ILE | LYS | PRO | PHE | THR | THR | VAL | ASP | PHE | ||||
| 8 | SER | SER | ILE | SER | THR | PRO | HIS | TYR | GLU | ASP | ||||
| 9 | ILE | PRO | PHE | THR | ARG | THR | ASP | PRO | VAL | VAL | ||||
| 10 | ALA | ASP | TYR | LYS | TYR | ASP | LEU | LYS | LEU | GLN | ||||
| 11 | GLU | TYR | GLN | SER | ALA | ILE | LYS | VAL | GLU | PRO | ||||
| 12 | ALA | SER | PRO | PRO | TYR | TYR | SER | GLU | LYS | THR | ||||
| 13 | GLN | LEU | TYR | ASN | LYS | PRO | HIS | GLU | GLU | PRO | ||||
| 14 | SER | ASN | SER | LEU | MET | ALA | ILE |
Samples:
sample_1: PPARg2 AB domain, [U-100% 13C; U-100% 15N], 800 uM; salt 135 mM
sample_conditions_1: ionic strength: 135 mM; pH: 7.3; pressure: 1 atm; temperature: 278.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE NEO 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks