CASP: Opportunity to obtain the structure of a protein of interest in your research

Interested in obtaining the NMR structure of a protein/domain relevant to your research and help advancing the methods of structural prediction from sequence?   You may send the protein sequence and a brief justification of your selection to with subject: “CASP NMR structure determination” or contact Krzysztof Fidelis ( directly. 

If your protein is selected as CASP target, you will receive the structural information and the expression vectors at the end of CASP13 (ca. Oct., 2018).

We are seeking proteins for which knowledge of structure will significantly advance research programs, and invite your nominations.  As part of the CASP13 experiment (Critical Assessment of Structure Prediction –, April-July, 2018), Dr. Gaetano Montelione and colleagues ( will purify a few proteins and determine their structures using NMR. Concurrently, these structures will be predicted as part of the CASP13 modeling methods assessment.  Restrictions on proteins to be considered, imposed by the need to test structure modeling methods, and the limited resources available for experimental structure determination are:

  • No significant sequence homology to any known structures in the PDB
  • 60-180 amino acid residues, preferably monomeric domain, or 15-20 kD dimer
  • Predicted to be ordered (i.e. not an intrinsically disordered protein)
  • Soluble, non-disulfide bonded, globular protein which is predicted to fold inside of the cell
  • No integral membrane proteins will be pursued in this cycle
  • Shallow sequence alignment, avoiding high-accuracy evolutionary covariance contact prediction

 Please feel free to share with your colleagues.

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