BMRB Entry 30432

Name: CSP2-d10
Published: 2018-08-22

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PDB ID: 6cot
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30432
MolProbity Validation Chart

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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:

CSP2-d10

Deposition date:

2018-03-12

Original release date:

2018-08-22

Authors:

Yang, Y.

Citation:

Citation: Yang, Y.; Cornilescu, G.; Tal-Gan, Y.. "Structural Characterization of Competence-Stimulating Peptide Analogues Reveals Key Features for ComD1 and ComD2 Receptor Binding in Streptococcus pneumoniae" Biochemistry 57, 5359-5369 (2018).
PubMed: 30125091

Assembly members:

Assembly members:
Competence-stimulating peptide type 2, polymer, 17 residues, 2183.726 Da.

Natural source:

Natural source: Common Name: Streptococcus pneumoniae Taxonomy ID: 1313 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pneumoniae

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Competence-stimulating peptide type 2: EMRISRIILDFLFLRKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	31
15N chemical shifts	14
1H chemical shifts	116

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 17 residues - 2183.726 Da.

1

GLU

MET

ARG

ILE

SER

ARG

ILE

LEU

ASP

2

PHE

LEU

PHE

LEU

ARG

LYS

Samples:

sample_1: DPC, D, 250 mM; competence stimulating peptide type 2 mutant-CSP2d10 1.9 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 900 MHz

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