BMRB Entry 50636

Name: NMR data of gallium binding peptide C3.15 (with gallium)
Published: 2021-05-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50636

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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 data of gallium binding peptide C3.15 (with gallium)

Deposition date:

2020-12-09

Original release date:

2021-05-27

Authors:

Lanikova, Alice; Zidek, Lukas

Citation:

Citation: Taylor, Corey; Shonberger, Nora; Lanikova, Alice; Patzschke, Michael; Drobot, Bjorn; Zidek, Lukas; Lederer, Franziska. "Investigation of the structure and dynamics of Gallium binding to high-affinity peptides elucidated by multi-scale simulation, quantum chemistry, NMR and ITC" Phys. Chem. Chem. Phys. 23, 8618-8632 (2021).
PubMed: 33876023

Assembly members:

Assembly members:
entity_1, polymer, 13 residues, Formula weight is not available
entity_GA, non-polymer, 69.723 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NYLPHQSSSPSRC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	23
1H chemical shifts	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C3.15 peptide	1
2	gallium ion	2

Entities:

Entity 1, C3.15 peptide 13 residues - Formula weight is not available

1

ASN

TYR

LEU

PRO

HIS

GLN

SER

PRO

2

SER

ARG

CYS

Entity 2, gallium ion - Ga - 69.723 Da.

1

GA

Samples:

sample_1: sodium azide 0.02%; sodium chloride 150 mM; TFA 0.5 mM; peptide 0.5 mM; D2O 10%

sample_conditions_1: pH: 3; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 850 MHz
Bruker AVANCE III 950 MHz