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.

[ViewLarge]
This Feature Is Available To Subscribers Only

or Create an Account

Close Modal
Close Modal