BMRB Entry 34391
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34391
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Title: 3D NMR solution structure of ligand peptide (Ac)EVNPPVP of Pro-Pro endopeptidase-1 PubMed: 31182482
Deposition date: 2019-04-04 Original release date: 2019-10-18
Authors: Diaz, D.
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).
Assembly members:
entity_1, polymer, 9 residues, 774.883 Da.
Natural source: Common Name: Clostridioides difficile Taxonomy ID: 1496 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridioides difficile
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: XEVNPPVPX
- assigned_chemical_shifts
- spectral_peak_list
Data type | Count |
13C chemical shifts | 23 |
1H chemical shifts | 51 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 9 residues - 774.883 Da.
1 | ACE | GLU | VAL | ASN | PRO | PRO | VAL | PRO | NH2 |
Samples:
sample_1: peptide 2 mM
sample_conditions_1: ionic strength: 0.175 M; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_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