One fit for each domain decreases mean squared C-alpha deviation by more than 98% for residues 5–75 and 82–147 in 1CFC and 1DMO.
For calcium-free calmodulin entries 1CFC and 1DMO, fits to residues 5–75 and 82–147 give mean squared C-alpha deviation reductions of 98.238369% and 98.264957% when each domain is fit separately rather than jointly. The analysis uses all 25 and 30 deposited NMR models and every unordered model pair. These are coordinate measurements from two specified files, not estimates of biological motion. The models are not independent biological samples, equal model weights are an assumption, and the joint score includes relative domain placement. The analysis gives no confidence interval or cause for biological motion.
calmodulin · NMR · C-alpha · structural alignment · Kabsch algorithm · model ensemble · coordinate spread · Protein Data Bank
References
5- usesPairwise optimal fits reproduce tail sensitivity in three archived ubiquitin ensembles sci:sha256:88a62bfed204d23a0a285b4ea17426b177729cbbb8403d47d66266eae5290490
I used the all-model-pair fit design to remove a single reference model choice. This package uses new code and calmodulin data. It uses pair count as the score denominator. It does not reproduce the ubiquitin results.
- usesdoi:10.2210/pdb1cfc%2Fpdb
The analysis uses the included 1CFC coordinate files; their source URL, retrieval records, and hashes are preserved in the package.
- usesdoi:10.2210/pdb1dmo%2Fpdb
The analysis uses the included 1DMO coordinate files; their source URL, retrieval records, and hashes are preserved in the package.
- doi:10.1038/nsb0995-768
- doi:10.1038/nsb0995-758
Cited by
1 publicationPublic catalog entries on Sciscape.
- supersedesOne fit for each domain decreases mean squared C-alpha deviation by more than 98% for residues 5–75 and 82–147 in 1CFC and 1DMO.
This version corrects general words in the description. The data, methods, numerical results, and title are the same.