BMRB Entry 30226

Name: NMR SOLUTION STRUCTURE OF THE ALPHA-CONOTOXIN GID MUTANT V13Y
Published: 2017-08-31

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PDB ID: 5ug5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30226
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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 THE ALPHA-CONOTOXIN GID MUTANT V13Y

Deposition date:

2017-01-06

Original release date:

2017-08-31

Authors:

Hussein, A.; Leffler, A.; Kuryatov, A.; Zebroski, H.; Powell, S.; Filipenko, P.; Gorson, J.; Heizmann, A.; Lyskov, S.; Nicke, A.; Lindstrom, J.; Rudy, B.; Bonneau, R.; Holford, M.; Poget, S.

Citation:

Citation: Leffler, Abba; Kuryatov, Alexander; Zebroski, Henry; Powell, Susan; Filipenko, Petr; Hussein, Adel; Gorson, Juliette; Heizmann, Anna; Lyskov, Sergey; Tsien, Richard; Poget, Sebastien; Nicke, Annette; Lindstrom, Jon; Rudy, Bernardo; Bonneau, Richard; Holford, Mande. "Discovery of peptide ligands through docking and virtual screening at nicotinic acetylcholine receptor homology models." Proc. Natl. Acad. Sci. U.S.A. 114, E8100-E8109 (2017).
PubMed: 28874590

Assembly members:

Assembly members:
Alpha-conotoxin GID, polymer, 19 residues, 2213.479 Da.

Natural source:

Natural source: Common Name: Geography cone Taxonomy ID: 6491 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Conus geographus

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Alpha-conotoxin GID: IRDECCSNPACRYNNPHVC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	34
1H chemical shifts	110

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 19 residues - 2213.479 Da.

1

ILE

ARG

ASP

GLU

CYS

SER

ASN

PRO

ALA

2

CYS

ARG

TYR

ASN

HYP

HIS

VAL

CYS

Samples:

sample_1: design 8, none, 1.5 ± 0.3 mM; H2O 90%; D2O 10%

sample_2: design 8, none, 1.5 ± 0.3 mM; D2O 100%

sample_conditions_1: ionic strength: 0 mM; pH: 3; pressure: 1 atm; temperature: 280 K

sample_conditions_2: ionic strength: 0 mM; pH: 3; pressure: 1 atm; temperature: 280 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 DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

CcpNMR, CCPN - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN, Bruker Biospin - collection

VNMR, Varian - collection

NMR spectrometers:

Varian UNITYPLUS 600 MHz
Bruker Avance 800 MHz