Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50451
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Sulskis, Darius; Thoma, Johannes; Burmann, Bjorn. "Structural basis of DegP protease temperature-dependent activation" Sci. Adv. 7, eabj1816-eabj1816 (2021).
PubMed: 34878848
Assembly members:
entity_1, polymer, 90 residues, 9510 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a(+)
Entity Sequences (FASTA):
entity_1: QNQVDSSSIFNGIEGAEMSN
KGKDQGVVVNNVKTGTPAAQ
IGLKKGDVIIGANQQAVKNI
AELRKVLDSKPSVLALNIQR
GDSTIYLLMQ
Data type | Count |
13C chemical shifts | 120 |
15N chemical shifts | 62 |
1H chemical shifts | 63 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PDZ2 | 1 |
Entity 1, PDZ2 90 residues - 9510 Da.
PDZ2 domain (359-448 a.a.) of DegP
1 | GLN | ASN | GLN | VAL | ASP | SER | SER | SER | ILE | PHE | |
2 | ASN | GLY | ILE | GLU | GLY | ALA | GLU | MET | SER | ASN | |
3 | LYS | GLY | LYS | ASP | GLN | GLY | VAL | VAL | VAL | ASN | |
4 | ASN | VAL | LYS | THR | GLY | THR | PRO | ALA | ALA | GLN | |
5 | ILE | GLY | LEU | LYS | LYS | GLY | ASP | VAL | ILE | ILE | |
6 | GLY | ALA | ASN | GLN | GLN | ALA | VAL | LYS | ASN | ILE | |
7 | ALA | GLU | LEU | ARG | LYS | VAL | LEU | ASP | SER | LYS | |
8 | PRO | SER | VAL | LEU | ALA | LEU | ASN | ILE | GLN | ARG | |
9 | GLY | ASP | SER | THR | ILE | TYR | LEU | LEU | MET | GLN |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks