Table 1
Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
Stevan R. Hubbard
- The EMBO Journal (1997) 16, 5572 - 5581
- doi:10.1093/emboj/16.18.5572
| Data collection | |||||
| Resolution (Å) | Observations (N) | Completeness (%) | Redundancy (%) | Rsym (%)a | Signal <I/ (I)> |
| 20.0–1.9 | 93535 | 98.6 (90.6)b | 4.1 | 6.5 (15.3)b | 12.9 |
| Refinementc | |||||
| Resolution (Å) | Reflections (N) | R-value (%)d | Root-mean-square deviations | ||
| Bonds (Å) | Angles (°) | B-factors (Å2)e | |||
| 6.0–1.9 | 25082 | 19.4 (22.6)f | 0.008 | 1.5 | 1.4 |
aRsym = 100  hkli | Ii(hkl)–<I(hkl)> |/hkliIi(hkl). | |||||
| bValue in parentheses is for the highest resolution shell. | |||||
| cAtomic model includes 303 IRK3P residues, six peptide residues, one AMP-PNP molecule, two Mg2+ ions, 202 water molecules (2653 atoms). | |||||
| dR-value = 100hkl| |Fo(hkl)|–|Fc(hkl)| |/hkl|Fo(hkl)|, where Fo and Fc are the observed and calculated structure factors, respectively (Fo >2). | |||||
| eFor bonded protein atoms. | |||||
| fValue in parentheses is the free R-value determined from 5% of the data. | |||||
