FMO DATABASE

FMODB ID: 3MZLL

Calculation Name: 2KUP-A-Other547

Preferred Name: ALK tyrosine kinase receptor

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2KUP

Chain ID: A

ChEMBL ID: CHEMBL4247

UniProt ID: Q9UM73

Base Structure: SolutionNMR

Registration Date: 2025-10-05

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1166659.01805
FMO2-HF: Nuclear repulsion	1108469.711586
FMO2-HF: Total energy	-58189.306464
FMO2-MP2: Total energy	-58355.530289

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:1:GLY)

Summations of interaction energy for fragment #1(A:1:GLY)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-195.263	-193.957	18.892	-12.094	-8.102	-0.144

Interaction energy analysis for fragmet #1(A:1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.799 / q_NPA : 0.891

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	SER	0	-0.005	0.004	3.857	3.809	4.721	-0.013	-0.406	-0.493	0.000
103	A	103	ASP	-1	-0.818	-0.903	1.911	-145.435	-145.134	18.906	-11.684	-7.522	-0.144
104	A	104	LEU	0	-0.008	-0.007	4.901	0.156	0.249	-0.001	-0.004	-0.087	0.000
4	A	4	GLY	0	0.072	0.036	7.119	1.242	1.242	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.020	-0.018	10.796	0.195	0.195	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.017	-0.021	13.894	0.861	0.861	0.000	0.000	0.000	0.000
7	A	7	GLY	0	-0.003	0.024	17.669	-0.179	-0.179	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.006	-0.005	20.087	0.716	0.716	0.000	0.000	0.000	0.000
9	A	9	ASN	0	0.016	0.002	20.878	-0.498	-0.498	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.894	0.938	17.185	15.964	15.964	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.856	-0.891	23.015	-12.450	-12.450	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.040	-0.036	24.176	0.180	0.180	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.001	-0.003	18.403	-0.559	-0.559	0.000	0.000	0.000	0.000
14	A	14	PRO	0	-0.004	-0.002	18.125	0.629	0.629	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.886	-0.970	19.299	-15.953	-15.953	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.002	-0.019	15.952	-0.596	-0.596	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.019	0.031	13.634	-1.663	-1.663	0.000	0.000	0.000	0.000
18	A	18	PRO	0	0.007	0.001	9.233	-0.226	-0.226	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.011	-0.002	9.379	-2.049	-2.049	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.814	0.903	11.539	20.518	20.518	0.000	0.000	0.000	0.000
21	A	21	PHE	0	0.066	0.034	10.359	0.249	0.249	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.890	0.960	16.462	14.695	14.695	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.007	0.002	19.036	-0.434	-0.434	0.000	0.000	0.000	0.000
24	A	24	THR	0	-0.001	-0.007	21.755	0.412	0.412	0.000	0.000	0.000	0.000
25	A	25	ASN	0	-0.023	0.000	24.923	-0.582	-0.582	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.020	-0.019	25.723	0.388	0.388	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.830	-0.924	28.248	-9.878	-9.878	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.976	-0.977	30.012	-9.894	-9.894	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.954	-0.979	32.281	-8.571	-8.571	0.000	0.000	0.000	0.000
30	A	30	GLY	0	-0.025	0.006	29.504	-0.089	-0.089	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.045	-0.029	30.136	-0.192	-0.192	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.936	-0.986	28.411	-11.345	-11.345	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.033	-0.010	30.008	0.326	0.326	0.000	0.000	0.000	0.000
34	A	34	GLY	0	-0.018	-0.017	29.446	0.324	0.324	0.000	0.000	0.000	0.000
35	A	35	SER	0	-0.032	-0.005	26.256	-0.301	-0.301	0.000	0.000	0.000	0.000
36	A	36	GLY	0	-0.004	-0.006	24.235	0.354	0.354	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.076	-0.039	18.704	-0.269	-0.269	0.000	0.000	0.000	0.000
38	A	38	MET	0	0.041	0.042	15.933	0.332	0.332	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.867	-0.923	14.842	-19.379	-19.379	0.000	0.000	0.000	0.000
40	A	40	LEU	0	0.000	0.000	9.764	0.408	0.408	0.000	0.000	0.000	0.000
41	A	41	THR	0	0.012	0.007	11.136	-1.928	-1.928	0.000	0.000	0.000	0.000
42	A	42	GLN	0	0.067	0.032	6.813	2.856	2.856	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.008	0.034	11.088	0.528	0.528	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.878	-0.951	14.907	-14.959	-14.959	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.008	0.015	13.882	-0.987	-0.987	0.000	0.000	0.000	0.000
46	A	46	VAL	0	-0.015	-0.016	16.505	1.197	1.197	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.010	0.010	18.848	-0.551	-0.551	0.000	0.000	0.000	0.000
48	A	48	HIS	0	-0.043	-0.036	19.153	1.332	1.332	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.025	-0.004	23.290	-0.070	-0.070	0.000	0.000	0.000	0.000
50	A	50	HIS	0	0.033	0.033	26.543	-0.043	-0.043	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.947	0.958	29.982	9.170	9.170	0.000	0.000	0.000	0.000
52	A	52	ARG	1	0.903	0.958	30.656	9.403	9.403	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.874	-0.928	29.416	-10.429	-10.429	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.015	0.009	24.247	-0.110	-0.110	0.000	0.000	0.000	0.000
55	A	55	VAL	0	-0.019	-0.003	24.343	0.257	0.257	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.885	0.944	21.264	13.048	13.048	0.000	0.000	0.000	0.000
57	A	57	TRP	0	0.015	-0.003	19.407	0.424	0.424	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.073	0.040	18.082	-1.101	-1.101	0.000	0.000	0.000	0.000
59	A	59	TYR	0	0.041	-0.016	12.338	0.428	0.428	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.006	0.007	16.369	0.242	0.242	0.000	0.000	0.000	0.000
61	A	61	CYS	0	-0.080	-0.028	19.222	1.075	1.075	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.022	0.031	15.308	0.691	0.691	0.000	0.000	0.000	0.000
63	A	63	ARG	1	0.818	0.893	17.789	12.759	12.759	0.000	0.000	0.000	0.000
64	A	64	ARG	1	0.939	0.965	18.416	13.462	13.462	0.000	0.000	0.000	0.000
65	A	65	TYR	0	0.017	0.003	11.782	0.044	0.044	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.001	0.004	16.386	-0.535	-0.535	0.000	0.000	0.000	0.000
67	A	67	TYR	0	-0.032	-0.024	15.137	0.089	0.089	0.000	0.000	0.000	0.000
68	A	68	ASP	-1	-0.804	-0.875	17.825	-13.470	-13.470	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.037	-0.049	20.053	-0.565	-0.565	0.000	0.000	0.000	0.000
70	A	70	ASN	0	-0.090	-0.039	20.870	0.780	0.780	0.000	0.000	0.000	0.000
71	A	71	LEU	0	0.044	0.037	20.848	0.216	0.216	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.038	0.003	15.259	-0.831	-0.831	0.000	0.000	0.000	0.000
73	A	73	SER	0	0.016	0.006	18.742	0.919	0.919	0.000	0.000	0.000	0.000
74	A	74	PHE	0	0.006	0.006	18.342	-1.092	-1.092	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.847	-0.926	20.340	-11.675	-11.675	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.041	-0.027	21.817	-0.882	-0.882	0.000	0.000	0.000	0.000
77	A	77	GLY	0	0.054	0.030	24.076	0.566	0.566	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.972	0.970	27.096	9.780	9.780	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.793	0.866	24.803	12.420	12.420	0.000	0.000	0.000	0.000
80	A	80	CYS	0	-0.009	0.013	24.575	-0.162	-0.162	0.000	0.000	0.000	0.000
81	A	81	GLN	0	0.006	-0.011	25.956	-0.088	-0.088	0.000	0.000	0.000	0.000
82	A	82	THR	0	0.026	0.015	26.323	0.204	0.204	0.000	0.000	0.000	0.000
83	A	83	GLY	0	-0.007	0.011	28.637	0.342	0.342	0.000	0.000	0.000	0.000
84	A	84	GLN	0	-0.078	-0.060	28.203	-0.175	-0.175	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.026	0.011	27.543	0.403	0.403	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.024	-0.007	24.361	-0.495	-0.495	0.000	0.000	0.000	0.000
87	A	87	PHE	0	-0.008	0.001	23.066	0.496	0.496	0.000	0.000	0.000	0.000
88	A	88	ALA	0	0.039	0.019	22.534	-0.718	-0.718	0.000	0.000	0.000	0.000
89	A	89	PHE	0	0.000	-0.009	20.595	0.427	0.427	0.000	0.000	0.000	0.000
90	A	90	LYS	1	0.964	0.997	21.546	10.735	10.735	0.000	0.000	0.000	0.000
91	A	91	CYS	0	-0.036	-0.022	17.924	-0.551	-0.551	0.000	0.000	0.000	0.000
92	A	92	SER	0	0.016	0.011	19.775	0.070	0.070	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.859	0.916	11.992	22.691	22.691	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.029	0.018	14.358	-1.546	-1.546	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.887	-0.937	12.642	-22.405	-22.405	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.867	-0.940	10.295	-31.510	-31.510	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.025	-0.002	9.513	-3.121	-3.121	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.047	0.019	10.529	-1.729	-1.729	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.027	-0.007	7.333	-1.433	-1.433	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.028	-0.010	5.126	-6.938	-6.938	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.005	-0.004	6.632	-2.118	-2.118	0.000	0.000	0.000	0.000
102	A	102	GLN	0	-0.043	-0.020	7.080	0.056	0.056	0.000	0.000	0.000	0.000
105	A	105	MET	0	-0.048	-0.020	7.624	3.013	3.013	0.000	0.000	0.000	0.000
106	A	106	GLN	0	-0.063	-0.027	5.044	6.279	6.279	0.000	0.000	0.000	0.000
107	A	107	CYS	0	-0.029	-0.003	6.982	2.342	2.342	0.000	0.000	0.000	0.000
108	A	108	ASN	0	-0.058	-0.039	8.771	3.911	3.911	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.040	-0.032	11.360	0.790	0.790	0.000	0.000	0.000	0.000
110	A	110	ILE	0	-0.009	-0.007	12.661	1.312	1.312	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.022	-0.008	16.053	0.060	0.060	0.000	0.000	0.000	0.000
112	A	112	VAL	0	-0.014	0.002	11.593	0.196	0.196	0.000	0.000	0.000	0.000
113	A	113	MET	0	-0.034	-0.014	15.074	-0.770	-0.770	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.942	-0.965	17.765	-12.536	-12.536	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.947	-0.969	20.335	-14.863	-14.863	0.000	0.000	0.000	0.000
116	A	116	PRO	0	-0.023	-0.015	23.139	0.560	0.560	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.017	-0.014	26.746	-0.069	-0.069	0.000	0.000	0.000	0.000
118	A	118	ILE	0	0.050	0.020	25.223	0.162	0.162	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.033	-0.037	28.614	0.189	0.189	0.000	0.000	0.000	0.000
120	A	120	THR	0	0.022	0.021	25.967	0.258	0.258	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.918	0.982	28.948	9.246	9.246	0.000	0.000	0.000	0.000
122	A	122	ASN	0	0.035	0.006	31.546	0.164	0.164	0.000	0.000	0.000	0.000
123	A	123	SER	0	-0.072	-0.042	34.757	0.082	0.082	0.000	0.000	0.000	0.000
124	A	124	HIS	0	0.019	0.021	37.490	0.100	0.100	0.000	0.000	0.000	0.000
125	A	125	PRO	0	0.004	0.005	38.434	-0.184	-0.184	0.000	0.000	0.000	0.000
126	A	126	ALA	0	-0.003	-0.014	36.964	0.206	0.206	0.000	0.000	0.000	0.000
127	A	127	GLU	-1	-0.952	-0.970	36.528	-8.409	-8.409	0.000	0.000	0.000	0.000
128	A	128	LEU	0	-0.021	-0.012	29.845	-0.180	-0.180	0.000	0.000	0.000	0.000
129	A	129	ASP	-1	-0.855	-0.886	27.146	-11.517	-11.517	0.000	0.000	0.000	0.000
130	A	130	LEU	0	0.018	0.012	30.493	0.009	0.009	0.000	0.000	0.000	0.000
131	A	131	PRO	0	0.004	-0.002	27.532	-0.371	-0.371	0.000	0.000	0.000	0.000
132	A	132	ARG	1	0.951	0.968	22.267	13.436	13.436	0.000	0.000	0.000	0.000
133	A	133	ALA	0	0.041	0.022	28.287	0.138	0.138	0.000	0.000	0.000	0.000
134	A	134	PRO	0	-0.030	-0.014	30.688	-0.278	-0.278	0.000	0.000	0.000	0.000
135	A	135	GLN	0	0.037	0.017	32.326	0.046	0.046	0.000	0.000	0.000	0.000
136	A	136	PRO	0	-0.025	-0.007	34.031	0.050	0.050	0.000	0.000	0.000	0.000
137	A	137	PRO	0	0.007	0.004	37.804	-0.067	-0.067	0.000	0.000	0.000	0.000
138	A	138	ASN	0	-0.035	-0.020	39.469	-0.035	-0.035	0.000	0.000	0.000	0.000
139	A	139	ALA	0	0.019	0.009	42.436	0.035	0.035	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.010	-0.007	46.071	-0.083	-0.083	0.000	0.000	0.000	0.000
141	A	141	GLY	0	0.013	0.011	48.469	0.078	0.078	0.000	0.000	0.000	0.000
142	A	142	TYR	0	-0.024	-0.016	52.084	-0.010	-0.010	0.000	0.000	0.000	0.000
143	A	143	THR	0	0.001	0.000	55.412	0.006	0.006	0.000	0.000	0.000	0.000
144	A	144	VAL	0	-0.014	-0.006	58.575	0.009	0.009	0.000	0.000	0.000	0.000
145	A	145	SER	0	-0.046	-0.025	62.178	-0.008	-0.008	0.000	0.000	0.000	0.000
146	A	146	SER	-1	-0.906	-0.945	65.491	-4.669	-4.669	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1:GLY)