BMRB Entry 50451

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50451

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Title:
DegP-PDZ2
Deposition date:
2020-09-02
Original release date:
2021-10-15
Authors:
Sulskis, Darius; Thoma, Johannes; Burmann, Bjorn
Citation:

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:

Assembly members:
entity_1, polymer, 90 residues, 9510 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QNQVDSSSIFNGIEGAEMSN KGKDQGVVVNNVKTGTPAAQ IGLKKGDVIIGANQQAVKNI AELRKVLDSKPSVLALNIQR GDSTIYLLMQ

Data sets:
Data typeCount
13C chemical shifts120
15N chemical shifts62
1H chemical shifts63

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDZ21

Entities:

Entity 1, PDZ2 90 residues - 9510 Da.

PDZ2 domain (359-448 a.a.) of DegP

1   GLNASNGLNVALASPSERSERSERILEPHE
2   ASNGLYILEGLUGLYALAGLUMETSERASN
3   LYSGLYLYSASPGLNGLYVALVALVALASN
4   ASNVALLYSTHRGLYTHRPROALAALAGLN
5   ILEGLYLEULYSLYSGLYASPVALILEILE
6   GLYALAASNGLNGLNALAVALLYSASNILE
7   ALAGLULEUARGLYSVALLEUASPSERLYS
8   PROSERVALLEUALALEUASNILEGLNARG
9   GLYASPSERTHRILETYRLEULEUMETGLN

Samples:

sample_1: PDZ2 domain of DegP, [U-100% 13C; U-100% 15N], 1.08 mM; 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:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_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

Related Database Links:

UNP P0C0V0
AlphaFold P15724

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks