BMRB Entry 27862

Title:
NMR 1H chemical shift assignment heptapeptide EVNPAVP
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:
EVNPAVP_heptapeptide, 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):
EVNPAVP_heptapeptide: EVNPAVP

Data sets:
Data typeCount
1H chemical shifts47

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EVNPAVP heptapeptide1

Entities:

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

1   GLUVALASNPROALAVALPRO

Samples:

sample_1: EVNPAVP 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

Software:

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

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz