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- PDB-1g1p: NMR Solution Structures of delta-Conotoxin EVIA from Conus ermine... -
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Basic information
Entry | Database: PDB / ID: 1g1p | ||||||
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Title | NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus that Selectively Acts on Vertebrate Neuronal Na+ Channels | ||||||
![]() | CONOTOXIN EVIA | ||||||
![]() | TOXIN / three disulfide linkages / cis/trans isomerism of Leu12-Pro13 peptide bond / hydroxyproline | ||||||
Function / homology | Conotoxin, delta-type, conserved site / Delta-conotoxin family signature. / sodium channel inhibitor activity / toxin activity / extracellular region / Delta-conotoxin EVIA![]() | ||||||
Method | SOLUTION NMR / hybrid distance geometry dynamical simulated annealing with the allhdg force field, simulated annealing with the CHARMM22 force field | ||||||
![]() | Volpon, L. / Lamthanh, H. / Barbier, J. / Gilles, N. / Molgo, J. / Menez, A. / Lancelin, J.M. | ||||||
![]() | ![]() Title: NMR Solution Structures of delta-Conotoxin EVIA from Conus ermineus That Selectively Acts on Vertebrate Neuronal Na+ Channels. Authors: Volpon, L. / Lamthanh, H. / Barbier, J. / Gilles, N. / Lancelin, J.M. #1: ![]() Title: Conotoxin EVIA, a Novel Peptide from Conus ermineus Venom that Preferentially Acts on Neuronal Voltage-dependent Sodium Channels Authors: Barbier, J. / Lamthanh, H. / Le Gall, F. / Favreau, P. / Benoit, E. / Chen, H. / Gilles, N. / Ilan, N. / Heinemann, S.F. / Gordon, D. / Menez, A. / Molgo, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 159 KB | Display | ![]() |
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PDB format | ![]() | 137.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 355.5 KB | Display | ![]() |
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Full document | ![]() | 441 KB | Display | |
Data in XML | ![]() | 11.1 KB | Display | |
Data in CIF | ![]() | 18.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 3294.909 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The solid phase synthesis of conotoxin EVIA was carried out using the F-moc chemistry. The sequence of the peptide is naturally found in Conus ermineus (Atlantic fish-hunting cone). References: UniProt: P60513 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques |
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Sample preparation
Details | Contents: 2mM conotoxin EVIA; 90% H2O, 10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 0.01 / pH: 3 / Pressure: ambient / Temperature: 283 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: hybrid distance geometry dynamical simulated annealing with the allhdg force field, simulated annealing with the CHARMM22 force field Software ordinal: 1 Details: the structures are based on a total of 256 restraints, 210 are NOE-derived distance constraints, 24 dihedral angle restraints and 22 distance restraints from hydrogen bonds. | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 18 |