Table 1.
Overview of constraints used for structure calculation and refinement statistics for the ten lowest-energy structures of BSAP1 obtained with Protein Structure Validation Server (38)
| Summary of experimental constraints and structure validation | |
| Number of distance constraints | |
| Long [(i–j) > 5] | 305 |
| Medium [1 < (i–j) < 5] | 63 |
| Sequential [(i–j) = 1] | 247 |
| Intraresidual [i = j] | 371 |
| Total | 986 |
| Dihedral angle constraints | 75 |
| Average number of restrains per residue | 17.7 |
| Average atomic RMSD to the mean structure (Å) | |
| Backbone | 0.7 |
| Heavy atoms | 1.0 |
| Global quality scores (mean/Z score) | |
| Verify3D | 0.19 |
| Prosall | 0.50 |
| PROCHECK (φ–ψ) | −1.24 |
| PROCHECK (all) | −1.09 |
| MolProbity clash score | 8.61 |
| Ramachandran statistics (% of all residues) | |
| Most favored | 62.2 |
| Additionally allowed | 35.1 |
| Generously allowed | 2.7 |
| Disallowed regions | 0.0 |
All values are given for the D1-S60 region of BSAP1.