Structural Basis for the Selective Inhibition of Cdc2-Like Kinases by CX-4945
Table 1
Data collection and refinement statistics for CLKs in complex with CX-4945.
CLK1/CX-4945
CLK2/CX-4945
CLK3/CX-4945
Data collection
Space group
P21
P43212
I222
Cell dimensions
a, b, c (Å)
56.5, 115.7, 90.6
75.6, 75.6, 161.8
61.8, 115.0, 158.3
α, β, γ (°)
90, 100.4, 90
90, 90, 90
90, 90, 90
Resolution range (Å)
50–2.7 (2.8–2.7)
50–2.8 (2.9–2.8)
50–2.6 (2.69–2.6)
(%)
15.9 (199.1)
18.9 (136.7)
15.4 (67.2)
I / σI
23.8 (2.4)
16.5 (2.0)
12.8 (2.3)
Unique reflection
31866
12177
17657
Completeness (%)
99.8 (99.7)
99.6 (99.5)
99.7 (100.0)
Redundancy
7.0 (7.1)
18.5 (18.6)
6.9 (5.8)
0.988 (0.703)
0.962 (0.837)
0.987 (0.418)
Wilson B-factor
56.2
51.3
34.6
Refinement
Resolution
31.9–2.7
40.5–2.8
24.4–2.6
No. of reflections
32028
12156
17642
(%)
20.0/27.4
19.6/26.1
22.3/28.4
No. of atoms
7711
2907
2780
protein
7614
2848
2689
ligand
75
25
25
water
22
34
66
B-factors
protein
63.9
53.5
50.1
ligand
82.7
54.9
52.4
water
60.5
47.2
43.5
R.m.s. deviations
bond lengths (Å)
0.009
0.008
0.010
bond angles (°)
1.29
1.03
1.38
PDB code
6KHD
6KHE
6KHF
The numbers in parentheses are statistics from the highest resolution shell. , where is the observed intensity of individual reflections and is averaged over symmetry equivalents. [22]. , where and are the observed and calculated structure factor amplitudes, respectively. was calculated using 10% of the data.
