Table I. αIIbβ3 γC peptide complex x-ray diffraction and refinement data.
| Peptide sequence | HHLGGAKQAGDV | LGGAKQAGDV | HHLGGAKQRGDV | LGGAKQRGDV |
|---|---|---|---|---|
| Space group | P3221 | P3221 | P3221 | P3221 |
| Unit cell (a, b, c) (Å) | 148.3, 148.3, 176.6 | 148.4, 148.4, 177.2 | 148.5, 148.5, 176.4 | 148.3, 148.3,176.8 |
| α, β, γ (degree) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 |
| Wavelength (Å) | 1.07223 | 1.07223 | 1.07223 | 1.07223 |
| Resolution (Å) | 50–2.5 | 50–2.8 | 50–2.6 | 50–2.4 |
| Number of reflections (total/unique) | 557,015/77,023 | 362,650/55,536 | 416,764/68,878 | 609,049/87,704 |
| Completeness (%) | 99.8/100b | 99.4/99.6b | 98.5/87.4 | 99.7/99.0b |
| I/σ (I) | 17.6/3.5b | 16.2/2.8b | 19.1/2.2b | 17.3/2.3b |
| Rmerge (%) | 8.6/55.2bb | 10.5/62.3b | 8.5/43.3 | 9.0/56.9b |
| Number of atoms (protein/water/other) |
10,538/1,043/205 | 10,446/557/205 | 10,515/1,332/205 | 10,537/1,142/205 |
| Rmsd bond lengths (Å) | 0.006 | 0.006 | 0.007 | 0.007 |
| Rmsd bond angles (degree) | 1.0 | 1.0 | 1.0 | 1.0 |
| Rwork (%) | 14.8 | 15.6 | 14.1 | 14.8 |
| Rfree (%) | 19.0 | 20.4 | 19.0 | 19.3 |
| Ramachandran statistics (% favored/allowed/outlier)a |
96.9/3.0/0.1 | 96.5/3.4/0.1 | 97.1/2.6/0.2 | 97.1/2.7/0.2 |
| PDB code | 2VDO | 2VDP | 2VDQ | 2VDR |
Rmerge = ΣH Σi |Ii(h) − <I(h)>|/ΣHΣi Ii(h), where Ii(h) and <I(h)> are the ith and mean measurement of the intensity of reflection, h. Rwork = ΣH||Fobs (h)| − |Fcalc (h)||/ΣH|Fobs (h)|, where Fobs (h) and Fcalc (h) are the observed and calculated structure factors, respectively. No I/σ cutoff was applied. Rfree is the R value obtained for a test set of reflections consisting of a randomly selected 5% subset of the data set excluded from refinement.
a
Determined with RAMPAGE (Lovell et al., 2003).
b
These numbers correspond to the last resolution shell.