Stichodactyla Helianthus Neurotoxin I: NMR-Derived Protein Solution Structures

Eight refined three-dimensional structures of a sea anemone neurotoxin, determined using 216 nuclear Overhauser enhancement distance restraints and 15 dihedral angles from 500 MHz NMR data. The structures describe a core of twisted, four-stranded, antiparallel beta-sheet joined by three loops, with one loop poorly defined. This dataset was created by Rasmus H. Fogh of UNSW Sydney.

Use Cases

• Refining protein structure prediction models based on NMR-derived distance and dihedral angle restraints.
• Comparing solution-state protein conformations to related sodium channel-binding toxins.
• Analyzing conformational flexibility in protein loops based on the poorly defined region encompassing residues 7-16.

Strengths

• Structure determination uses 216 specific distance restraints derived from 470 measured nuclear Overhauser enhancement values.
• Refinement via restrained molecular dynamics improved the structures with respect to distance violations and total potential energies.
• The eight best structures form a closely related family with a backbone RMSD of 1.3 +/- 0.2Å when excluding the poorly defined loop.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

Rasmus H. Fogh, UNSW Sydney

Collection Method

Distance geometry and restrained molecular dynamics simulations based on 500 MHz NMR data.