+Open data
-Basic information
Entry | Database: PDB / ID: 1ne5 | ||||||
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Title | Solution Structure of HERG Specific Scorpion Toxin CnErg1 | ||||||
Components | ergtoxin | ||||||
Keywords | TOXIN / alpha-helix / triple-stranded beta-sheet | ||||||
Function / homology | Function and homology information potassium channel inhibitor activity / toxin activity / extracellular region Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics, distance geometry, torsion angle dynamics | ||||||
Authors | Torres, A.M. / Paramjit, B. / Alewood, P. / Kuchel, P.W. / Vandenberg, J.I. | ||||||
Citation | Journal: FEBS Lett. / Year: 2003 Title: Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin Authors: Torres, A.M. / Bansal, P. / Alewood, P.F. / Bursill, J.A. / Kuchel, P.W. / Vandenberg, J.I. #1: Journal: FASEB J. / Year: 1999 Title: A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated from Centruroides noxius scorpion venom. Authors: Gurrola, G.B. / Rosati, B. / Rocchetti, M. / Pimienta, G. / Zaza, A. / Arcangeli, A. / Olivotto, M. / Possani, L.D. / Wanke, E. #2: Journal: FEBS Lett. / Year: 2000 Title: Disulfide bridges of ergtoxin, a member of a new sub-family of peptide blockers of the ether-a-go-go-related K+ channel Authors: Scaloni, A. / Bottiglieri, C. / Ferrara, L. / Corona, M. / Gurrola, G.B. / Batista, C. / Wanke, E. / Possani, L.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ne5.cif.gz | 238.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ne5.ent.gz | 207.5 KB | Display | PDB format |
PDBx/mmJSON format | 1ne5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ne5_validation.pdf.gz | 338.2 KB | Display | wwPDB validaton report |
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Full document | 1ne5_full_validation.pdf.gz | 462.5 KB | Display | |
Data in XML | 1ne5_validation.xml.gz | 13.3 KB | Display | |
Data in CIF | 1ne5_validation.cif.gz | 21.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ne/1ne5 ftp://data.pdbj.org/pub/pdb/validation_reports/ne/1ne5 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4746.415 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: This sequence occurs naturally in Centruroides noxius References: UniProt: Q86QT3 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
NMR details | Text: This structure were determined using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 1.7mM CnErg1 / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: no salt added / pH: 3.2 / Pressure: ambient / Temperature: 298 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 AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics, distance geometry, torsion angle dynamics Software ordinal: 1 Details: The structures are based on a total of 578 restraints, 535 are NOE-derived distance restraints, 11 dihedral angle restraints, 32 distance restraints from hydrogen bonds. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 4000 / Conformers submitted total number: 20 |