We are happy to announce an opportunity to obtain the three-dimensional structure of proteins you are working on. Dr. Gaetano Montelione and colleagues (http://www-nmr.cabm.rutgers.edu) will determine structures of a few nominated proteins using NMR. Concurrently, these structures will be suggested as prediction targets in the forthcoming CASP13 experiment.

We are seeking proteins for which knowledge of structure will significantly advance research programs, and invite your nominations.

There are some restrictions on proteins that will be considered, imposed by the need to test structure modeling methods, and the limited resources available for experimental structure determination:

• - No significant sequence homology to any of the structures in the PDB;
• - 60-180 amino acid residues, preferably monomeric domain;
• - 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 provide a brief justification /explanation of your selection. Solved structures will be made publicly available.

Please submit your nominations to casp@predictioncenter.org with -CASP NMR structure determination- as subject line.

Feel free to share this with your colleagues.

The CASP Organizing Committee and the Montelione Laboratory