BMRB Entry 27365

Name: CSP1_DPC
Published: 2019-02-08

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR27365

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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:

CSP1_DPC

Deposition date:

2018-01-18

Original release date:

2019-02-08

Authors:

Yang, Yifang; Cornilescu, Gabriel; Tal-Gan, Yftah

Citation:

Citation: Yang, Yifang; Cornilescu, Gabriel; Tal-Gan, Yftah. "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:
CSP1, polymer, 17 residues, Formula weight is not available

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 Host organism: streptococcus pneumoniae

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CSP1: EMRLSKFFRDFILQRKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	32
15N chemical shifts	18
1H chemical shifts	129

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CSP1, 1	1
2	CSP1, 2	1

Entities:

Entity 1, CSP1, 1 17 residues - Formula weight is not available

1

GLU

MET

ARG

LEU

SER

LYS

PHE

ARG

ASP

2

PHE

ILE

LEU

GLN

ARG

LYS

Samples:

sample_1: DPC, [U-2H], 250 mM; CSP1 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 TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	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:

SPARKY, Goddard - chemical shift assignment

X-PLOR_NIH vv. 2.42, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

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