BMRB Entry 50400

Name: 1H, 13C, 15N chemical shifts for PmScsC linker peptide in 50% TFE
Published: 2021-06-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50400

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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:

1H, 13C, 15N chemical shifts for PmScsC linker peptide in 50% TFE

Deposition date:

2020-07-21

Original release date:

2021-06-30

Authors:

Green, Chloe; Redfield, Christina; Smith, Lorna

Citation:

Citation: Smith, Lorna; Green, Chloe; Redfield, Christina. "The 'Shape-Shifter' Peptide from the Disulphide Isomerase PmScsC Shows Context-Dependent Conformational Preferences." Biomolecules 11, 642-642 (2021).
PubMed: 33926076

Assembly members:

Assembly members:
entity_1, polymer, 15 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Proteus mirabilis Taxonomy ID: 584 Superkingdom: Bacteria Kingdom: not available Genus/species: Proteus mirabilis

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XKKADEQQAQFRQAX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	38
15N chemical shifts	13
1H chemical shifts	79

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	peptide	1

Entities:

Entity 1, peptide 15 residues - Formula weight is not available

1

ACE

LYS

ALA

ASP

GLU

GLN

ALA

GLN

2

PHE

ARG

GLN

ALA

NH2

Samples:

sample_1: peptide 2.5 ± 0.1 mM; TFE, [U-2H], 50 ± 2 %; sodium phosphate 0.01 M

sample_conditions_1: ionic strength: 0.01 M; pH: 7; pressure: 1 atm; temperature: 288 K

Experiments:

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

Software:

TOPSPIN v3.1.7 - collection

NMRPipe - processing

CcpNMR v2.4 - chemical shift assignment, data analysis

NMR spectrometers:

Bruker AVANCE II 500 MHz
Bruker AVANCE III 950 MHz MHz

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