BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30226

Title: NMR SOLUTION STRUCTURE OF THE ALPHA-CONOTOXIN GID MUTANT V13Y   PubMed: 28874590

Deposition date: 2017-01-06 Original release date: 2017-01-06

Authors: Hussein, A.; A., Leffler; ., A.; ., A.; ., .; 7, .; A., 8; Lyskov, S.; A., Nicke; ., J.; ., .; ., .; 15, .; ,

Citation: Leffler, Abba; A., Kuryatov; A., H.; ., R.; ., .; 30226, .; 8, 30226; Sergey, 9; Tsien, Richard; S., Poget; ., A.; ., .; ., .; 30226, .; , 30226. "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).

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

Natural source:   Common Name: not available   Taxonomy ID: 6491   Superkingdom: Metazoa   Kingdom: Conus   Genus/species: geographus not available

Experimental source:   Production method: chemical synthesis

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

Data sets:
Data typeCount
13C chemical shifts34
110

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 19 residues - 2213.479 Da.

1   ILE.3022656SER.302261112
2   TYR.302261718CYS

Samples:

sample_1: design 8, none, 1.5 ± 0.3 mM; natural abundance; .

sample_2: design 8, none, 1.5 ± 0.3 mM; natural abundance

sample_conditions_1: ionic strength: 0 mM; 3: . 30226; .: atm temperature; K: 30226

sample_conditions_2: ionic strength: 0 mM; 3: . 30226; .: atm temperature; K: 30226

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
nosotropicnot availablenot available
not availablenot availablenot availablenot available
not availablenot available2not available
not availablenot available$sample_conditions_2not available

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