Table 1. Data collection and refinement statistics of the EGFR/CO-1686 complex crystal structures.

	CO-1686/EGFR T790M	CO-1686/EGFR L858R
Data collection
Space group	I23	I23
Cell dimensions
a, b, c (Å)	145.5, 145.5, 145.5	143.5, 143.5, 143.5
α, β, γ (°)	90.0, 90.0, 90.0	90.0, 90.0, 90.0
Resolution (Å)	50-2.35(2.43-2.35)	50-2.70(2.91-2.70)
Rp.i.m.a (%)	3.3(54)	3.5(3.49)
I/σI	27.6(2)	25.98(2.19)
Completeness (%)	100(100)	98.3(99.5)
Redundancy	16.7(16.3)	7.3(7.4)
Refinement
Resolution (Å)	41.99-2.35	38.36-2.7
No. reflections	20894	13462
Rwork/Rfreeb	0.217/0.250	0.208/0.252
No. atoms
Protein	2456	2348
Water	108	19
B-factors
Protein	40.86	75.72
Water	42.12	73.59
R.M.S. deviations
Bond lengths (Å)	0.016	0.011
Bond angles (°)	1.307	1.122
Ramachandran plot
Favored, %	98.67	97.89
Allowed, %	1.33	2.11
Disallowed, %	0	0

*Values in parentheses are for highest-resolution shell. One crystal was used for each data set.

^a$R_{p.i.m.}={\displaystyle {\sum }_h(\frac{1}{n_h-1}}){\displaystyle {\sum }_l|I_{hl}}-\langle I_h\rangle |{\displaystyle {\sum }_h{\displaystyle {\sum }_i\langle I_h\rangle }}$, where I_hl is the lth observation of reflection h and 〈I_h〉 is the average intensity for all observations l of reflection h. R_p.i.m. is a multiplicity-independent R factor to evaluate diffraction data quality [31].

^b The R factor for refinement is defined as:

$$R={\displaystyle \sum \left|\right|F_{obs}}|-|F_{cal}\left|\right|/{\displaystyle \sum \left|F_{obs}\right|}$$

where F_obs and F_cal are observed and calculated structure factor amplitudes, respectively. R_work is calculated using reflections included in the refinement, while R_free is calculated using reflections excluded from the refinement.