1. PcaA Mycolic acid cyclopropyl synthase (Smith&Sacchettini) original structure solved at 2.0A via MAD R-value = 0.22, R-free = 0.27 287 residues,  fold Example of density quality (~1  contour with C  trace)

2. Electron density map (2.8A)

3. Results of tracing

5. Strip off branches of trace (linearize)

6. Linearized trace shows backbone connectivity

7. Pick C  ’s using neural net; link together

8. Results of CAPRA

9. Comparison to backbone of true structure (white) Percent built = 89% (missing: 15-residue N-terminus, 17-residue disordered loop) 4 single-atom insertions; 5 single-atom deletions RMSD = 0.81A

10. CAPRA model consists of 3 chains Chain lengths: 14, 96, 145 residues

11. Results of LOOKUP (modeling side-chains)

12. Comparison of TEXTAL model to true structure Percent amino acid identity = 87.5% (mistakes: small frame-shifts around gaps in alignment) all-atom RMSD = 0.92A

13. Closeup of  -strand (TEXTAL model in green)

14. Closeup of  -helix (TEXTAL model in green)

15. If5A Translation initiation factor 5A (Peat&Terwilliger) 136 residues,  -fold original structure solved at 1.75A by MAD R-value = 0.21, R-free = 0.24 Example of density quality (~1  contour with C  trace)

16. Electron density map (2.8A) with C  chains generated by CAPRA (CAPRA chains shown in color; true backbone shown in white)

17. Results of CAPRA Percent built = 94% chain lengths: 16, 20, 44, 57 C  RMSD = 0.76A

18. LOOKUP: fitting side-chains into density

20. Results of LOOKUP, comparison to true structure Percent identity = 84% all-atom RMSD = 0.92A (TEXTAL model in green; true structure in red/white/blue)

21. Focus on backbone atoms Notice accuracy of carbonyl oxygens and chain directionality

22. Closeup of a strand within a  -sheet

23. Closeup of another  -strand and turn