BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30225

Title: NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN GID MUTANT A10V

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

Citation: Hussein, A.; Leffler, A.; Zebroski, H.; Powell, S.; Kuryatov, A.; Filipenko, P.; Gorson, J.; Heizmann, A.; Lyskov, S.; Nicke, A.; Lindstrom, J.; Rudy, B.; Bonneau, R.; Holford, M.; Poget, S.. "Peptide Ligand Discovery from an Ion Channel Homology Model"  . ., .-..

Assembly members:
Alpha-conotoxin GID, polymer, 19 residues, 2177.489 Da.

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

Experimental source:   Production method: chemical synthesis

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

Data sets:
Data typeCount
13C chemical shifts36
1H chemical shifts114

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 - 2177.489 Da.

1   ILEARGASPGLUCYSCYSSERASNPROVAL
2   CYSARGVALASNASNHYPHISVALCYS

Samples:

sample_3: A10V design 5 mutant, none, 1.5 ± 0.3 mM; D2O 100%

sample_4: A10V design 5 mutant, none, 1.5 ± 0.3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 3; pressure: 1 atm; temperature: 380 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D DQF-COSYsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1

Software:

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

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

CcpNMR, CCPN - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

VNMR, Varian - collection

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Varian UNITYPLUS 600 MHz

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