Fig. 6
![Fig. 6](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2Fs12900-018-0089-0/MediaObjects/12900_2018_89_Fig6_HTML.png)
Flexible fitting of an atomic model comprised of F-actin, tropomyosin and Ig-domains of MyBP-C (blue ribbons) into an EM map (yellow surface) filtered to 11Å resolution. Helices and β-strands were kept rigid. In addition, distance constraints were imposed between adjacent endpoints of β-strands in the C0 and C1 domains. a The initial atomic model, docked into the electron density map using rigid body fitting, is shown in blue. b The resulting atomic model (final conformation of the trajectory) yielded by DDforge. c Evolution of the overlap values along the trajectory. The indicated value of t1=53 is the warning time, where overfitting is likely to begin. (Coincidentally, its value was equal to that for lactoferrin. See Fig. 4.) The stopping time for this case was t2=106