Table 1.

X-ray crystal structure coordinates taken from PDB database. Their accession codes from the PDB database, type of the receptor’s mutation, resolution in Å, and number of active torsion added to the ligands are presented.

Protein–Ligand Complexes	Type of Mutation	PDB Code	Resolution (Å)	No. of Active Torsions
EGFR/AMPPNP	Wild type	3vjo	2.64	8
EGFR/Dacomitinib	Wild type	4i23	2.8	3
EGFR/AZD9291	Wild type	4zau	2.8	9
EGFR/AEE788 inhibitor	Wild type	2j6m	3.1	7
EGFR/Gefitinib	T790M/G719S	3ug2	2.5	8
EGFR/AMP-PNP	T790M/G719S	3vjn	2.34	8
EGFR/AMP-PNP	G719S	2itn	2.47	8
EGFR/Iressa	G719S	2ito	3.25	8
EGFR/AEE788	G719S	2itp	2.74	7
EGFR/AFN941	G719S	2itq	2.68	6
EGFR/AMP-PNP	L858R	2eb3	2.84	8
EGFR/AFN941	L858R	2itu	2.8	6
EGFR/Iressa	L858R	2itz	2.8	8
EGFR/AEE788	T790M	2jiu	3.05	7
EGFR/Pyrazolopyrimidine	T790M	5j9y	2.8	3
EGFR/Pyrazolopyrimidine inhibitor a1	T790M	5j9z	2.5	3
EGFR/Inhibitor compound 4	T790M/L858R	3w2s	1.9	11
EGFR/Inhibitor compound 6	T790M/L858R	4rj4	2.78	5
EGFR/Inhibitor compound 5	T790M/L858R	4rj5	3.1	4
EGFR/Inhibitor compound 4	T790M/L858R	4rj6	2.7	4
EGFR/Inhibitor compound 1	T790M/L858R	4rj7	2.55	6
EGFR/Inhibitor compound 8	T790M/L858R	4rj8	2.5	4
EGFR/Inhibitor compound 17	T790M/L858R	5c8m	2.9	4
EGFR/Inhibitor compound 1	T790M/L858R	5c8k	3	4
EGFR/Inhibitor compound 24	T790M/L858R	5cal	2.7	6
EGFR/Inhibitor compound 27	T790M/L858R	5can	2.8	4
EGFR/Inhibitor compound 29	T790M/L858R	5cao	2.6	6
EGFR/Inhibitor compound 30	T790M/L858R	5cap	2.4	7
EGFR/Inhibitor compound 33	T790M/L858R	5caq	2.5	4
EGFR/Inhibitor compound 41a	T790M/L858R	5cas	2.1	6
EGFR/Inhibitor compound 41b	T790M/L858R	5cau	2.25	6
EGFR/pyridone compound 2	T790M/L858R	5em5	2.65	7
EGFR/pyridone compound 13	T790M/L858R	5em7	2.81	12
EGFR/pyridone compound 13	T790M/L858R	5em8	2.8	6
EGFR/pyridone compound 13	T790M/L858R	5hic	2.6	6