Table 2.
Refinement statistics
| Data set | Resolution*, Å | Completeness†, % | Rfactor, %‡ | Rfree, %‡ | rms deviations
|
Model atoms
|
Average B Factor
|
|||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Bonds, Å | Angles, ° | Protein§ | Water | Ligand | Protein | Water | Ligand | |||||
| Apo | 2.1 (4.9%) | 97.1 (88.2) | 21.8 (23.3) | 25.5 (26.8) | 0.008 | 1.33 | 2059 (4) | 874 | 25.1 | 34.3 | ||
| BMP | 2.4 (6.1%) | 91.3 (78.4) | 21.3 (23.1) | 25.8 (27.3) | 0.010 | 1.50 | 2059 (4) | 501 | 32 (4) | 29.3 | 35.5 | 27.5 |
*
Rsym is reported in parenthesis.
† Completeness of the outer shell is shown in parenthesis, 2.2–2.1 parentheses, for apo and 2.5–2.4 for BMP complex.
‡ Rfactor = 100 × Σ|Fobs − Fcalc|/Σ|Fobs| for F > 2σ and, in parentheses, F > 0σ, respectively; Fobs and Fcalc are the observed and calculated structure factor amplitudes. Rfree is the same as Rfactor but is calculated from 9% (apo) and 5% (BMP complex) of the reflection data that were excluded during the refinement.
§ For clarity, the atoms given represent the number of atoms in one monomer or in one BMP ligand and should be multiplied by four to obtain the total number of atoms used in refinement.