BMRB Entry 34391

Name: 3D NMR solution structure of ligand peptide (Ac)EVNPPVP of Pro-Pro endopeptidase-1
Published: 2019-10-18

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PDB ID: 6r9z
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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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	23
1H chemical shifts	51

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

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