594 of 2,346 C-alpha distances in 1CFD residues 5–75 are less than the minimum distances from 25 1CFC models by more than 0.01 Å.

This analysis compares chain A C-alpha distances in the representative calcium-free calmodulin structure 1CFD with the 25 coordinate models in its related 1CFC ensemble. For residues 5–75, 594 of 2,346 within-domain distances in 1CFD were more than 0.01 Å below the ensemble minimum, and 9 were more than 0.01 Å above the ensemble maximum. The corresponding counts were 50 and 1 of 2,016 for residues 82–147, and 0 and 0 of 4,686 between domains. The largest difference from an ensemble limit was 0.685028 Å for N-domain residues 38 and 63. At 0.10 Å tolerance, the combined counts were 379, 7, and 0 for the N domain, C domain, and between domains. These results apply to the recorded coordinate files and selections. The ranges from 25 archive models are not physical limits or confidence intervals; models are not independent physical samples or time points. The comparison does not test experimental restraint satisfaction or establish a cause for shorter distances. Independent arithmetic, synthetic boundary and rigid-motion checks, and offline reproducibility checks passed in the original work.

calmodulin · protein structure · NMR · coordinate models · C-alpha distance · structure ensemble · PDB · reproducibility