BMRB Entry 30895

Name: NMR Solution Structure of a CsrA-binding peptide
Published: 2022-02-04

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PDB ID: 7m7x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30895
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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:

NMR Solution Structure of a CsrA-binding peptide

Deposition date:

2021-03-29

Original release date:

2022-02-04

Authors:

Harvey, P.; White, A.; Durek, T.; Craik, D.

Citation:

Citation: Jakob, V.; Zoller, B.; Rinkes, J.; Wu, Y.; Kiefer, A.; Hust, M.; Polten, S.; White, A.; Harvey, P.; Durek, T.; Craik, D.; Siebert, A.; Kazmaier, U.; Empting, M.. "Phage display-based discovery of cyclic peptides against the broad spectrum bacterial anti-virulence target CsrA" Eur. J. Med. Chem. 231, 114148-114148 (2022).
PubMed: 35114538

Assembly members:

Assembly members:
entity_1, polymer, 9 residues, 863.036 Da.

Natural source:

Natural source: Common Name: Yersinia pseudotuberculosis Taxonomy ID: 633 Superkingdom: Bacteria Kingdom: not available Genus/species: Yersinia pseudotuberculosis

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XVCSELCWX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	20
15N chemical shifts	7
1H chemical shifts	47

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 9 residues - 863.036 Da.

1

ACE

VAL

CYS

SER

GLU

LEU

CYS

TRP

NH2

Samples:

sample_1: peptide 2 mM

sample_conditions_1: pH: 3.4; 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 ROESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TopSpin v3.6, Bruker Biospin - processing

CcpNmr Analysis, CCPN - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker AVANCE III HD 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks