+Open data
-Basic information
Entry | Database: PDB / ID: 1mxn | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of alpha-conotoxin AuIB | ||||||
Components | alpha-conotoxin AuIB | ||||||
Keywords | TOXIN / alpha helix | ||||||
Function / homology | Function and homology information host cell postsynaptic membrane / acetylcholine receptor inhibitor activity / ion channel regulator activity / toxin activity / extracellular region Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics, energy minimisation in a CHARM forcefield | ||||||
Authors | Dutton, J.L. / Bansal, P.S. / Hogg, R.C. / Adams, D.J. / Alewood, P.F. / Craik, D.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: A New Level of Conotoxin Diversity, a Non-native Disulfide Bond Connectivity in alpha -Conotoxin AuIB Reduces Structural Definition but Increases Biological Activity. Authors: Dutton, J.L. / Bansal, P.S. / Hogg, R.C. / Adams, D.J. / Alewood, P.F. / Craik, D.J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1mxn.cif.gz | 69.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1mxn.ent.gz | 50.8 KB | Display | PDB format |
PDBx/mmJSON format | 1mxn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mx/1mxn ftp://data.pdbj.org/pub/pdb/validation_reports/mx/1mxn | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein/peptide | Mass: 1575.788 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: This peptide was synthesised by BOC chemistry but occurs naturally in Conus aulicus. References: UniProt: P56640 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||
NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 2mM peptide / Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 0 / pH: 3.5 / Pressure: atmospheric atm / Temperature: 290 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing, molecular dynamics, energy minimisation in a CHARM forcefield Software ordinal: 1 Details: 32 medium and 18 long range NOEs were included, 7 dihedral angle restraints were included, 5 H-bond restraints were included | ||||||||||||||||||||
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: 50 / Conformers submitted total number: 20 |