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Open data
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Basic information
Entry | Database: PDB / ID: 2igu | ||||||
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Title | Deamidated analogue of ImI Conotoxin | ||||||
![]() | Alpha-conotoxin ImI | ||||||
![]() | TOXIN / Conotoxin / disulfide linkage / ribbon conformation | ||||||
Function / homology | Conotoxin, alpha-type, conserved site / Alpha-conotoxin family signature. / host cell postsynaptic membrane / acetylcholine receptor inhibitor activity / ion channel regulator activity / toxin activity / extracellular region / Alpha-conotoxin ImI![]() | ||||||
Method | SOLUTION NMR / Energy Minization, Molecular Dynamics, Simulated Annealing | ||||||
Model type details | minimized average | ||||||
![]() | Kini, R.M. / Kang, T.S. | ||||||
![]() | ![]() Title: Protein folding determinants: structural features determining alternative disulfide pairing in alpha- and chi/lambda-conotoxins Authors: Kang, T.S. / Talley, T.T. / Jois, S.D. / Taylor, P. / Kini, R.M. #1: Journal: Angew.Chem.Int.Ed.Engl. / Year: 2005 Title: Effect of C-terminal amidation on folding and disulfide-pairing of alpha-conotoxin ImI Authors: Kang, T.S. / Vivekanandan, S. / Jois, S.D. / Kini, R.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 44.5 KB | Display | ![]() |
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PDB format | ![]() | 33.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 359.9 KB | Display | ![]() |
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Full document | ![]() | 423.1 KB | Display | |
Data in XML | ![]() | 5 KB | Display | |
Data in CIF | ![]() | 7.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ifiC ![]() 2ifjC ![]() 2ifzC ![]() 2ih6C ![]() 2ih7C ![]() 2ihaC C: citing same article ( |
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Similar 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: 1358.594 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: Chemically synthesized using Fmoc solid phase peptide synthesis. References: UniProt: P50983*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 2mM peptide sample, pH 3.0; 10% D2O, 90% H2O / Solvent system: 10% D2O, 90% H2O |
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Sample conditions | Ionic strength: 2mM / pH: 3.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
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: Energy Minization, Molecular Dynamics, Simulated Annealing Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: minimized average structure | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 14 |