BMRB Entry 34391

Title:
3D NMR solution structure of ligand peptide (Ac)EVNPPVP of Pro-Pro endopeptidase-1
Deposition date:
2019-04-04
Original release date:
2019-10-18
Authors:
Diaz, D.
Citation:

Citation: Pichlo, C.; Juetten, L.; Wojtalla, F.; Schacherl, M.; Diaz, D.; Baumann, U.. "Molecular determinants of the mechanism and substrate specificity ofClostridium difficileproline-proline endopeptidase-1."  J. Biol. Chem. 294, 11525-11535 (2019).
PubMed: 31182482

Assembly members:

Assembly members:
entity_1, polymer, 9 residues, 774.883 Da.

Natural source:

Natural source:   Common Name: Clostridioides difficile   Taxonomy ID: 1496   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridioides difficile

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XEVNPPVPX

Data sets:
Data typeCount
13C chemical shifts23
1H chemical shifts51

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 9 residues - 774.883 Da.

1   ACEGLUVALASNPROPROVALPRONH2

Samples:

sample_1: peptide 2 mM

sample_conditions_1: ionic strength: 0.175 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE II 600 MHz