FMO DATABASE

FMODB ID: JL929

Calculation Name: 2ABL-A-Xray372

Preferred Name: Tyrosine-protein kinase ABL

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2ABL

Chain ID: A

ChEMBL ID: CHEMBL1862

UniProt ID: P00519

Base Structure: X-ray

Registration Date: 2023-09-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	163
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1524829.015442
FMO2-HF: Nuclear repulsion	1461893.922114
FMO2-HF: Total energy	-62935.093329
FMO2-MP2: Total energy	-63121.537528

3D Structure

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:75:MET)

Summations of interaction energy for fragment #1(A:75:MET)

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.
-8.008	-2.317	0.277	-3.343	-2.626	0.01

Interaction energy analysis for fragmet #1(A:75:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.031 / q_NPA : 0.025

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	77	PRO	0	-0.003	-0.024	2.710	-8.518	-2.921	0.278	-3.338	-2.537	0.010
4	A	78	SER	0	0.031	0.022	5.208	-0.849	-0.849	0.000	0.000	0.000	0.000
5	A	79	GLU	-1	-0.843	-0.923	6.412	-0.739	-0.739	0.000	0.000	0.000	0.000
6	A	80	ASN	0	-0.027	-0.025	9.005	0.331	0.331	0.000	0.000	0.000	0.000
7	A	81	ASP	-1	-0.786	-0.863	8.969	-0.451	-0.451	0.000	0.000	0.000	0.000
8	A	82	PRO	0	-0.014	-0.022	11.024	0.011	0.011	0.000	0.000	0.000	0.000
9	A	83	ASN	0	-0.062	-0.030	12.371	0.101	0.101	0.000	0.000	0.000	0.000
10	A	84	LEU	0	-0.045	-0.002	9.099	0.028	0.028	0.000	0.000	0.000	0.000
11	A	85	PHE	0	0.055	0.010	12.086	0.058	0.058	0.000	0.000	0.000	0.000
12	A	86	VAL	0	-0.059	-0.040	13.993	-0.066	-0.066	0.000	0.000	0.000	0.000
13	A	87	ALA	0	0.032	0.022	16.263	0.038	0.038	0.000	0.000	0.000	0.000
14	A	88	LEU	0	-0.048	-0.033	18.681	-0.019	-0.019	0.000	0.000	0.000	0.000
15	A	89	TYR	0	-0.033	-0.030	22.085	0.001	0.001	0.000	0.000	0.000	0.000
16	A	90	ASP	-1	-0.822	-0.907	21.594	-0.052	-0.052	0.000	0.000	0.000	0.000
17	A	91	PHE	0	-0.012	0.001	21.688	0.000	0.000	0.000	0.000	0.000	0.000
18	A	92	VAL	0	-0.037	-0.031	22.015	0.014	0.014	0.000	0.000	0.000	0.000
19	A	93	ALA	0	-0.011	-0.011	22.097	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	94	SER	0	0.014	0.014	24.116	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	95	GLY	0	-0.001	-0.014	25.850	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	96	ASP	-1	-0.846	-0.895	21.435	0.253	0.253	0.000	0.000	0.000	0.000
23	A	97	ASN	0	-0.079	-0.053	22.264	-0.027	-0.027	0.000	0.000	0.000	0.000
24	A	98	THR	0	-0.012	0.013	22.454	-0.017	-0.017	0.000	0.000	0.000	0.000
25	A	99	LEU	0	-0.005	0.001	14.829	0.022	0.022	0.000	0.000	0.000	0.000
26	A	100	SER	0	0.015	0.000	19.306	-0.036	-0.036	0.000	0.000	0.000	0.000
27	A	101	ILE	0	-0.046	-0.009	16.259	0.017	0.017	0.000	0.000	0.000	0.000
28	A	102	THR	0	-0.010	-0.001	17.016	0.003	0.003	0.000	0.000	0.000	0.000
29	A	103	LYS	1	0.921	0.945	17.608	0.103	0.103	0.000	0.000	0.000	0.000
30	A	104	GLY	0	-0.019	-0.004	17.220	0.005	0.005	0.000	0.000	0.000	0.000
31	A	105	GLU	-1	-0.844	-0.927	12.685	-0.043	-0.043	0.000	0.000	0.000	0.000
32	A	106	LYS	1	0.831	0.908	10.279	0.595	0.595	0.000	0.000	0.000	0.000
33	A	107	LEU	0	0.033	0.020	11.598	0.085	0.085	0.000	0.000	0.000	0.000
34	A	108	ARG	1	0.861	0.927	8.702	0.121	0.121	0.000	0.000	0.000	0.000
35	A	109	VAL	0	-0.046	-0.029	11.949	0.112	0.112	0.000	0.000	0.000	0.000
36	A	110	LEU	0	0.000	0.002	13.037	-0.029	-0.029	0.000	0.000	0.000	0.000
37	A	111	GLY	0	0.018	0.013	16.608	0.000	0.000	0.000	0.000	0.000	0.000
38	A	112	TYR	0	-0.003	0.005	20.331	-0.001	-0.001	0.000	0.000	0.000	0.000
39	A	113	ASN	0	0.052	0.018	23.338	0.004	0.004	0.000	0.000	0.000	0.000
40	A	114	HIS	0	-0.006	-0.019	26.475	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	115	ASN	0	-0.041	-0.026	29.735	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	116	GLY	0	-0.004	0.006	26.067	-0.008	-0.008	0.000	0.000	0.000	0.000
43	A	117	GLU	-1	-0.886	-0.920	25.945	-0.022	-0.022	0.000	0.000	0.000	0.000
44	A	118	TRP	0	-0.022	-0.003	24.414	0.002	0.002	0.000	0.000	0.000	0.000
45	A	119	CYS	0	-0.026	0.000	19.569	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	120	GLU	-1	-0.861	-0.910	17.755	0.178	0.178	0.000	0.000	0.000	0.000
47	A	121	ALA	0	0.006	-0.009	15.586	-0.028	-0.028	0.000	0.000	0.000	0.000
48	A	122	GLN	0	0.019	-0.002	10.366	0.068	0.068	0.000	0.000	0.000	0.000
49	A	123	THR	0	0.000	-0.013	10.372	-0.102	-0.102	0.000	0.000	0.000	0.000
50	A	124	LYS	1	0.897	0.945	4.598	0.219	0.313	-0.001	-0.005	-0.089	0.000
51	A	125	ASN	0	0.005	0.011	9.190	0.217	0.217	0.000	0.000	0.000	0.000
52	A	126	GLY	0	0.010	0.013	12.239	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	127	GLN	0	-0.037	-0.042	13.328	0.040	0.040	0.000	0.000	0.000	0.000
54	A	128	GLY	0	0.025	0.027	15.583	0.003	0.003	0.000	0.000	0.000	0.000
55	A	129	TRP	0	-0.063	-0.048	18.663	-0.032	-0.032	0.000	0.000	0.000	0.000
56	A	130	VAL	0	0.043	0.031	18.733	0.008	0.008	0.000	0.000	0.000	0.000
57	A	131	PRO	0	-0.010	0.003	21.701	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	132	SER	0	0.009	-0.025	22.546	-0.015	-0.015	0.000	0.000	0.000	0.000
59	A	133	ASN	0	-0.002	-0.009	23.494	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	134	TYR	0	-0.006	-0.003	22.871	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	135	ILE	0	-0.014	0.007	18.308	-0.013	-0.013	0.000	0.000	0.000	0.000
62	A	136	THR	0	0.001	0.003	19.174	0.022	0.022	0.000	0.000	0.000	0.000
63	A	137	PRO	0	0.009	0.007	17.449	-0.038	-0.038	0.000	0.000	0.000	0.000
64	A	138	VAL	0	-0.036	-0.001	13.399	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	139	ASN	0	-0.064	-0.052	12.677	0.046	0.046	0.000	0.000	0.000	0.000
66	A	140	SER	0	0.021	-0.014	16.339	0.018	0.018	0.000	0.000	0.000	0.000
67	A	141	LEU	0	-0.002	-0.016	18.200	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	142	GLU	-1	-0.886	-0.932	20.667	-0.163	-0.163	0.000	0.000	0.000	0.000
69	A	143	LYS	1	0.873	0.983	16.384	0.454	0.454	0.000	0.000	0.000	0.000
70	A	144	HIS	0	-0.015	0.001	19.282	0.011	0.011	0.000	0.000	0.000	0.000
71	A	145	SER	0	0.013	-0.011	24.428	0.011	0.011	0.000	0.000	0.000	0.000
72	A	146	TRP	0	0.058	0.036	22.369	0.011	0.011	0.000	0.000	0.000	0.000
73	A	147	TYR	0	-0.114	-0.128	23.164	0.013	0.013	0.000	0.000	0.000	0.000
74	A	148	HIS	0	0.027	-0.010	26.400	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	149	GLY	0	0.056	0.061	26.555	0.001	0.001	0.000	0.000	0.000	0.000
76	A	150	PRO	0	0.019	0.006	27.538	0.008	0.008	0.000	0.000	0.000	0.000
77	A	151	VAL	0	0.010	0.008	30.248	0.002	0.002	0.000	0.000	0.000	0.000
78	A	152	SER	0	0.053	0.038	33.441	0.003	0.003	0.000	0.000	0.000	0.000
79	A	153	ARG	1	0.876	0.919	36.131	0.028	0.028	0.000	0.000	0.000	0.000
80	A	154	ASN	0	0.049	0.002	37.592	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	155	ALA	0	0.026	0.017	37.302	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	156	ALA	0	0.046	0.018	35.275	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	157	GLU	-1	-0.853	-0.916	37.005	-0.038	-0.038	0.000	0.000	0.000	0.000
84	A	158	TYR	0	-0.032	0.004	40.277	0.000	0.000	0.000	0.000	0.000	0.000
85	A	159	LEU	0	0.004	0.000	34.856	0.000	0.000	0.000	0.000	0.000	0.000
86	A	160	LEU	0	-0.023	0.013	35.583	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	161	SER	0	-0.029	-0.033	39.627	0.004	0.004	0.000	0.000	0.000	0.000
88	A	162	SER	0	-0.058	-0.026	42.109	0.002	0.002	0.000	0.000	0.000	0.000
89	A	163	GLY	0	0.047	0.021	40.451	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	164	ILE	0	-0.009	0.000	38.828	0.004	0.004	0.000	0.000	0.000	0.000
91	A	165	ASN	0	-0.013	-0.030	40.186	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	166	GLY	0	0.093	0.048	36.999	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	167	SER	0	-0.058	-0.031	35.241	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	168	PHE	0	-0.016	-0.026	28.266	0.005	0.005	0.000	0.000	0.000	0.000
95	A	169	LEU	0	-0.002	0.021	30.629	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	170	VAL	0	-0.017	-0.010	25.453	0.008	0.008	0.000	0.000	0.000	0.000
97	A	171	ARG	1	0.841	0.925	28.436	0.049	0.049	0.000	0.000	0.000	0.000
98	A	172	GLU	-1	-0.824	-0.870	23.821	-0.122	-0.122	0.000	0.000	0.000	0.000
99	A	173	SER	0	-0.042	-0.030	28.158	0.003	0.003	0.000	0.000	0.000	0.000
100	A	174	GLU	-1	-0.892	-0.959	29.471	-0.056	-0.056	0.000	0.000	0.000	0.000
101	A	175	SER	0	-0.018	0.003	30.780	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	176	SER	0	0.047	0.020	26.604	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	177	PRO	0	0.082	0.028	23.486	0.002	0.002	0.000	0.000	0.000	0.000
104	A	178	GLY	0	0.001	0.008	23.381	-0.010	-0.010	0.000	0.000	0.000	0.000
105	A	179	GLN	0	-0.037	-0.002	24.327	0.003	0.003	0.000	0.000	0.000	0.000
106	A	180	ARG	1	0.956	0.977	20.259	0.108	0.108	0.000	0.000	0.000	0.000
107	A	181	SER	0	-0.071	-0.035	27.593	0.014	0.014	0.000	0.000	0.000	0.000
108	A	182	ILE	0	0.042	0.032	28.581	-0.009	-0.009	0.000	0.000	0.000	0.000
109	A	183	SER	0	-0.055	-0.039	31.212	0.007	0.007	0.000	0.000	0.000	0.000
110	A	184	LEU	0	0.010	0.003	34.287	-0.006	-0.006	0.000	0.000	0.000	0.000
111	A	185	ARG	1	0.912	0.972	36.390	0.054	0.054	0.000	0.000	0.000	0.000
112	A	186	TYR	0	-0.073	-0.050	39.684	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	187	GLU	-1	-0.775	-0.877	41.877	-0.036	-0.036	0.000	0.000	0.000	0.000
114	A	188	GLY	0	-0.024	-0.004	44.804	0.002	0.002	0.000	0.000	0.000	0.000
115	A	189	ARG	1	0.879	0.946	44.463	0.029	0.029	0.000	0.000	0.000	0.000
116	A	190	VAL	0	0.034	0.019	38.570	-0.002	-0.002	0.000	0.000	0.000	0.000
117	A	191	TYR	0	-0.033	-0.006	38.754	0.006	0.006	0.000	0.000	0.000	0.000
118	A	192	HIS	0	-0.020	-0.019	35.932	-0.006	-0.006	0.000	0.000	0.000	0.000
119	A	193	TYR	0	0.018	0.013	32.855	0.004	0.004	0.000	0.000	0.000	0.000
120	A	194	ARG	1	0.853	0.907	30.683	0.023	0.023	0.000	0.000	0.000	0.000
121	A	195	ILE	0	0.031	0.028	24.919	0.001	0.001	0.000	0.000	0.000	0.000
122	A	196	ASN	0	-0.057	-0.029	27.164	-0.003	-0.003	0.000	0.000	0.000	0.000
123	A	197	THR	0	0.009	0.005	21.231	-0.013	-0.013	0.000	0.000	0.000	0.000
124	A	198	ALA	0	-0.048	-0.024	23.178	0.007	0.007	0.000	0.000	0.000	0.000
125	A	199	SER	0	0.019	-0.012	22.581	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	200	ASP	-1	-0.858	-0.929	19.188	0.085	0.085	0.000	0.000	0.000	0.000
127	A	201	GLY	0	0.023	0.013	18.068	0.011	0.011	0.000	0.000	0.000	0.000
128	A	202	LYS	1	0.841	0.928	18.254	-0.067	-0.067	0.000	0.000	0.000	0.000
129	A	203	LEU	0	0.018	0.020	19.665	0.003	0.003	0.000	0.000	0.000	0.000
130	A	204	TYR	0	0.004	-0.011	22.713	0.003	0.003	0.000	0.000	0.000	0.000
131	A	205	VAL	0	0.018	0.013	26.139	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	206	SER	0	0.003	-0.018	29.685	0.005	0.005	0.000	0.000	0.000	0.000
133	A	207	SER	0	-0.034	-0.026	29.316	0.001	0.001	0.000	0.000	0.000	0.000
134	A	208	GLU	-1	-0.835	-0.901	28.920	0.020	0.020	0.000	0.000	0.000	0.000
135	A	209	SER	0	-0.093	-0.045	27.351	0.003	0.003	0.000	0.000	0.000	0.000
136	A	210	ARG	1	0.855	0.905	23.728	-0.033	-0.033	0.000	0.000	0.000	0.000
137	A	211	PHE	0	0.005	-0.002	21.054	0.001	0.001	0.000	0.000	0.000	0.000
138	A	212	ASN	0	-0.018	-0.013	14.922	0.039	0.039	0.000	0.000	0.000	0.000
139	A	213	THR	0	0.010	0.009	15.954	-0.017	-0.017	0.000	0.000	0.000	0.000
140	A	214	LEU	0	0.058	0.019	17.893	0.020	0.020	0.000	0.000	0.000	0.000
141	A	215	ALA	0	-0.003	-0.008	19.177	0.013	0.013	0.000	0.000	0.000	0.000
142	A	216	GLU	-1	-0.774	-0.884	18.519	-0.083	-0.083	0.000	0.000	0.000	0.000
143	A	217	LEU	0	-0.034	0.011	21.537	0.014	0.014	0.000	0.000	0.000	0.000
144	A	218	VAL	0	-0.014	-0.019	24.060	0.010	0.010	0.000	0.000	0.000	0.000
145	A	219	HIS	0	0.003	0.017	22.322	0.010	0.010	0.000	0.000	0.000	0.000
146	A	220	HIS	0	-0.015	-0.009	25.550	0.004	0.004	0.000	0.000	0.000	0.000
147	A	221	HIS	1	0.802	0.875	27.325	0.053	0.053	0.000	0.000	0.000	0.000
148	A	222	SER	0	-0.027	-0.008	28.966	0.002	0.002	0.000	0.000	0.000	0.000
149	A	223	THR	0	-0.059	-0.030	29.104	0.002	0.002	0.000	0.000	0.000	0.000
150	A	224	VAL	0	-0.014	-0.011	31.269	0.006	0.006	0.000	0.000	0.000	0.000
151	A	225	ALA	0	0.043	0.036	32.411	-0.002	-0.002	0.000	0.000	0.000	0.000
152	A	226	ASP	-1	-0.821	-0.884	31.140	-0.027	-0.027	0.000	0.000	0.000	0.000
153	A	227	GLY	0	0.085	0.049	33.074	0.000	0.000	0.000	0.000	0.000	0.000
154	A	228	LEU	0	-0.090	-0.033	31.721	0.001	0.001	0.000	0.000	0.000	0.000
155	A	229	ILE	0	-0.004	-0.005	35.848	0.002	0.002	0.000	0.000	0.000	0.000
156	A	230	THR	0	-0.011	-0.005	37.541	0.002	0.002	0.000	0.000	0.000	0.000
157	A	231	THR	0	-0.030	-0.002	34.171	0.001	0.001	0.000	0.000	0.000	0.000
158	A	232	LEU	0	-0.001	-0.003	29.204	0.001	0.001	0.000	0.000	0.000	0.000
159	A	233	HIS	0	-0.006	0.002	33.099	0.003	0.003	0.000	0.000	0.000	0.000
160	A	234	TYR	0	0.009	0.001	24.870	-0.007	-0.007	0.000	0.000	0.000	0.000
161	A	235	PRO	0	-0.015	-0.018	29.056	0.004	0.004	0.000	0.000	0.000	0.000
162	A	236	ALA	0	0.009	0.019	30.609	-0.005	-0.005	0.000	0.000	0.000	0.000
163	A	237	PRO	0	-0.007	-0.006	29.067	-0.006	-0.006	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:75:MET)