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Open data
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Basic information
Entry | Database: PDB / ID: 2moa | |||||||||
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Title | Solution NMR structure of peptide ImI1 (peak 2) | |||||||||
![]() | Alpha-conotoxin ImI | |||||||||
![]() | TOXIN / dithiol amino acid / conotoxin / bicyclic peptide / macrocycle / phage display | |||||||||
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 mutant / Alpha-conotoxin ImI![]() | |||||||||
Biological species | ![]() | |||||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | |||||||||
Model details | closest to the average, model1 | |||||||||
![]() | Heinis, C. / Chen, S. | |||||||||
![]() | ![]() Title: Dithiol amino acids can structurally shape and enhance the ligand-binding properties of polypeptides. Authors: Chen, S. / Gopalakrishnan, R. / Schaer, T. / Marger, F. / Hovius, R. / Bertrand, D. / Pojer, F. / Heinis, C. #1: ![]() Title: Solution structure of alpha-conotoxin ImI by 1H nuclear magnetic resonance. Authors: Gehrmann, J. / Daly, N.L. / Alewood, P.F. / Craik, D.J. #2: ![]() Title: NMR spatial structure of alpha-conotoxin ImI reveals a common scaffold in snail and snake toxins recognizing neuronal nicotinic acetylcholine receptors. Authors: Maslennikov, I.V. / Shenkarev, Z.O. / Zhmak, M.N. / Ivanov, V.T. / Methfessel, C. / Tsetlin, V.I. / Arseniev, A.S. #3: ![]() Title: NMR solution structure of alpha-conotoxin ImI and comparison to other conotoxins specific for neuronal nicotinic acetylcholine receptors. Authors: Rogers, J.P. / Luginbuhl, P. / Shen, G.S. / McCabe, R.T. / Stevens, R.C. / Wemmer, D.E. #4: ![]() Title: Minimal conformation of the alpha-conotoxin ImI for the alpha7 neuronal nicotinic acetylcholine receptor recognition: correlated CD, NMR and binding studies. Authors: Lamthanh, H. / Jegou-Matheron, C. / Servent, D. / Menez, A. / Lancelin, J.M. #5: ![]() Title: Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP. Authors: Ulens, C. / Hogg, R.C. / Celie, P.H. / Bertrand, D. / Tsetlin, V. / Smit, A.B. / Sixma, T.K. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 68.2 KB | Display | ![]() |
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PDB format | ![]() | 46.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.8 KB | Display | ![]() |
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Full document | ![]() | 576.7 KB | Display | |
Data in XML | ![]() | 12.8 KB | Display | |
Data in CIF | ![]() | 17.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4os1C ![]() 4os2C ![]() 4os4C ![]() 4os5C ![]() 4os6C ![]() 4os7C C: citing same article ( |
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Similar structure data | |
Other databases |
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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 | |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Bicyclic peptide ImI1 (peak 2) was generated by substituing two adjacent cysteines in ImI with a dithiol amino acid 1a. | ||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1 mM ImI1, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: ImI1-1 |
Sample conditions | Ionic strength: 0.1 / pH: 5.8 / Pressure: ambient / Temperature: 278 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 163 / NOE intraresidue total count: 107 / NOE long range total count: 3 / NOE medium range total count: 11 / NOE sequential total count: 42 | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0 Å / Maximum upper distance constraint violation: 0.143 Å | ||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.071 Å / Distance rms dev error: 0.023 Å |