Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50450
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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, 94 residues, 9680 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: KRGELGIMGTELNSELAKAM
KVDAQRGAFVSQVLPNSSAA
KAGIKAGDVITSLNGKPISS
FAALRAQVGTMPVGSKLTLG
LLRDGKQVNVNLEL
Data type | Count |
13C chemical shifts | 217 |
15N chemical shifts | 76 |
1H chemical shifts | 76 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PDZ1 | 1 |
Entity 1, PDZ1 94 residues - 9680 Da.
1 | LYS | ARG | GLY | GLU | LEU | GLY | ILE | MET | GLY | THR | ||||
2 | GLU | LEU | ASN | SER | GLU | LEU | ALA | LYS | ALA | MET | ||||
3 | LYS | VAL | ASP | ALA | GLN | ARG | GLY | ALA | PHE | VAL | ||||
4 | SER | GLN | VAL | LEU | PRO | ASN | SER | SER | ALA | ALA | ||||
5 | LYS | ALA | GLY | ILE | LYS | ALA | GLY | ASP | VAL | ILE | ||||
6 | THR | SER | LEU | ASN | GLY | LYS | PRO | ILE | SER | SER | ||||
7 | PHE | ALA | ALA | LEU | ARG | ALA | GLN | VAL | GLY | THR | ||||
8 | MET | PRO | VAL | GLY | SER | LYS | LEU | THR | LEU | GLY | ||||
9 | LEU | LEU | ARG | ASP | GLY | LYS | GLN | VAL | ASN | VAL | ||||
10 | ASN | LEU | GLU | LEU |
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