BMRB Entry 27863

Title:
NMR 1H chemical shifts assignment heptapeptide EVNPPAP
Deposition date:
2019-04-01
Original release date:
2019-05-30
Authors:
Pichlo, Christian; Jutten, Linda; Wojtalla, Fabian; Schacherl, Magdalena; Diaz, Dolores; Baumann, Ulrich
Citation:

Citation: Pichlo, Christian; Jutten, Linda; Wojtalla, Fabian; Schacherl, Magdalena; Diaz, Dolores; Baumann, Ulrich. "Molecular determinants of the mechanism and substrate specificity of Clostridium difficile proline-proline endopeptidase-1"  J. Biol. Chem. 294, 11525-11535 (2019).
PubMed: 31182482

Assembly members:

Assembly members:
PP_peptide, polymer, 7 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PP_peptide: EVNPPVP

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1EVNPPVP heptapeptide1

Entities:

Entity 1, EVNPPVP heptapeptide 7 residues - Formula weight is not available

1   GLUVALASNPROPROVALPRO