BMRB Entry 31032

Name: NMR Solution Structure of C-terminally amidated, Full-length Human Galanin
Published: 2022-08-17

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PDB ID: 8dj4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31032
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Solution Structure of C-terminally amidated, Full-length Human Galanin

Deposition date:

2022-06-30

Original release date:

2022-08-17

Authors:

Wilkinson, R.; Kraichely, K.; Buchanan, L.; Parnham, S.; Giuliano, M.

Citation:

Citation: Wilkinson, R.; Kraichely, K.; Hendy, C.; Buchanan, L.; Parnham, S.; Giuliano, M.. "The neuropeptide galanin adopts an irregular secondary structure" Biochem. Biophys. Res. Commun. 626, 121-128 (2022).
PubMed: 35994823

Assembly members:

Assembly members:
entity_1, polymer, 31 residues, 3159.454 Da.

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GWTLNSAGYLLGPHAVGNHR SFSDKNGLTSX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
1H chemical shifts	194

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 31 residues - 3159.454 Da.

1

GLY

TRP

THR

LEU

ASN

SER

ALA

GLY

TYR

LEU

2

LEU

GLY

PRO

HIS

ALA

VAL

GLY

ASN

HIS

ARG

3

SER

PHE

SER

ASP

LYS

ASN

GLY

LEU

THR

SER

4

NH2

Samples:

sample_1: hGal(1-30)NH2 0.5 mM; sodium acetate, [U-2H], 4.14 mM; acetic acid, [U-2H], 5.86 mM

sample_conditions_1: pH: 4.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H 1D NMR Spectrum	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H ROESY	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al., Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

MestreLab (Mnova / MestReNova / MestReC), MestreLab - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz