BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27863

Title: NMR 1H chemical shifts assignment heptapeptide EVNPPAP   PubMed: 31182482

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: 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).

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

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

Experimental source:   Production method: chemical synthesis

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

Samples:

sample_1: PP peptide 2 mM; PBS buffer 50 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 - collection, processing

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

NMR spectrometers:

  • Bruker Avance 600 MHz