Some two-residue endpoint changes give C/D angle range overlap for 1CFC and 1DMO with 1X02.
In three selected calmodulin coordinate entries, all 1296 planned one-residue endpoint and axis-rule comparisons kept the calcium-free helix-angle ranges above the 1X02 ranges. The smallest gap was 0.6629351897280458 degrees for C/D in 1DMO versus 1X02. A later C/D check allowed each endpoint to change by up to two residues. Ranges overlapped in 39 of 1250 rules for 1CFC and 129 of 1250 for 1DMO. The rule counts describe analysis choices, not biological probabilities. Undirected axes changed the direction of range separation for G/H. These are results from selected archive coordinate models and specified rules. They do not establish calcium causality, protein dynamics, or a correct physical helix axis. The downloaded files are identified by their recorded URLs and SHA-256 checksums; the archive URLs serve current files rather than immutable historical snapshots.
calmodulin · helix angle · endpoint sensitivity · NMR structure ensemble · range overlap · Protein Data Bank · C-alpha · structural biology
References
5- usesOne 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. sci:sha256:c53299fd42dc573530772f0d7a043aacad282bc59779325c9c326b700fd4947b
I used its 1CFC and 1DMO entry selections and residue-name check design. These supplied the calcium-free inputs and input-audit scope. This analysis uses new code for helix angles. It does not reproduce the domain fits.
- doi:10.1038/nsb0995-768
- doi:10.1038/nsb0995-758
- supportsdoi:10.1074/jbc.M806513200
Table 2 supplies the helix residue intervals used to define the primary segments; the publication uses their intersections and does not analyze that paper's mutant coordinates.
- doi:10.1038/nature04525
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