BMRB Entry 50450
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50450
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Title: 1H, 13C and 15N backbone resonance assignments for isolated PDZ1 domain of the DegP serine protease from E. coli PubMed: 34878848
Deposition date: 2020-09-01 Original release date: 2021-10-15
Authors: Sulskis, Darius; Thoma, Johannes; Burmann, Bjorn
Citation: Sulskis, Darius; Thoma, Johannes; Burmann, Bjorn. "Structural basis of DegP protease temperature-dependent activation" Sci. Adv. 7, eabj1816-eabj1816 (2021).
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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 217 |
| 15N chemical shifts | 76 |
| 1H chemical shifts | 76 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PDZ1 | 1 |
Entities:
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 |
Samples:
sample_1: PDZ1 domain of DegP, [U-100% 13C; U-100% 15N], 665 uM; D2O, [U-100% 2H], 10%; H2O 90%; potassium phosphate 25 mM; EDTA 1 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 25 mM; pH: 7.0; pressure: 1 atm; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.5 - collection, data analysis
CARA v1.9.1.7 - chemical shift assignment, chemical shift calculation, data analysis, peak picking
qMDD v3.2 - processing
NMRPipe v9.6 - processing
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts