FMO DATABASE

FMODB ID: 39V7L

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	OptAll
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	-1524928.960648
FMO2-HF: Nuclear repulsion	1461993.044951
FMO2-HF: Total energy	-62935.915696
FMO2-MP2: Total energy	-63122.407951

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.
-1.328	1.644	-0.011	-1.64	-1.322	0.004

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 : 0.053 / q_NPA : 0.030

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	0.018	0.016	3.594	-2.483	0.148	-0.013	-1.520	-1.098	0.004
4	A	78	SER	0	0.012	0.012	5.423	-0.627	-0.627	0.000	0.000	0.000	0.000
5	A	79	GLU	-1	-0.819	-0.908	6.804	-0.491	-0.491	0.000	0.000	0.000	0.000
6	A	80	ASN	0	0.003	-0.005	9.217	0.193	0.193	0.000	0.000	0.000	0.000
7	A	81	ASP	-1	-0.804	-0.874	9.334	-0.298	-0.298	0.000	0.000	0.000	0.000
8	A	82	PRO	0	0.000	-0.014	11.365	-0.021	-0.021	0.000	0.000	0.000	0.000
9	A	83	ASN	0	-0.069	-0.037	12.604	0.067	0.067	0.000	0.000	0.000	0.000
10	A	84	LEU	0	-0.050	-0.006	9.200	-0.002	-0.002	0.000	0.000	0.000	0.000
11	A	85	PHE	0	0.044	0.005	12.116	0.062	0.062	0.000	0.000	0.000	0.000
12	A	86	VAL	0	-0.045	-0.029	13.708	-0.083	-0.083	0.000	0.000	0.000	0.000
13	A	87	ALA	0	0.028	0.030	16.085	0.038	0.038	0.000	0.000	0.000	0.000
14	A	88	LEU	0	-0.029	-0.008	18.598	-0.012	-0.012	0.000	0.000	0.000	0.000
15	A	89	TYR	0	-0.045	-0.035	22.109	0.002	0.002	0.000	0.000	0.000	0.000
16	A	90	ASP	-1	-0.823	-0.901	21.214	-0.090	-0.090	0.000	0.000	0.000	0.000
17	A	91	PHE	0	-0.022	-0.017	21.331	0.005	0.005	0.000	0.000	0.000	0.000
18	A	92	VAL	0	-0.011	-0.008	21.427	0.005	0.005	0.000	0.000	0.000	0.000
19	A	93	ALA	0	-0.005	-0.001	21.813	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	94	SER	0	0.002	-0.001	23.804	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	95	GLY	0	-0.023	-0.018	25.411	0.001	0.001	0.000	0.000	0.000	0.000
22	A	96	ASP	-1	-0.789	-0.892	21.905	0.136	0.136	0.000	0.000	0.000	0.000
23	A	97	ASN	0	-0.076	-0.029	22.497	-0.020	-0.020	0.000	0.000	0.000	0.000
24	A	98	THR	0	-0.058	-0.021	22.571	-0.013	-0.013	0.000	0.000	0.000	0.000
25	A	99	LEU	0	-0.007	0.001	15.082	0.015	0.015	0.000	0.000	0.000	0.000
26	A	100	SER	0	-0.001	-0.008	18.893	-0.024	-0.024	0.000	0.000	0.000	0.000
27	A	101	ILE	0	-0.040	-0.008	15.777	0.003	0.003	0.000	0.000	0.000	0.000
28	A	102	THR	0	0.022	0.006	16.111	0.012	0.012	0.000	0.000	0.000	0.000
29	A	103	LYS	1	0.893	0.931	17.485	0.101	0.101	0.000	0.000	0.000	0.000
30	A	104	GLY	0	-0.017	-0.005	17.211	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	105	GLU	-1	-0.803	-0.875	12.525	-0.158	-0.158	0.000	0.000	0.000	0.000
32	A	106	LYS	1	0.826	0.903	10.058	0.508	0.508	0.000	0.000	0.000	0.000
33	A	107	LEU	0	0.016	0.005	11.220	0.024	0.024	0.000	0.000	0.000	0.000
34	A	108	ARG	1	0.840	0.903	9.112	0.106	0.106	0.000	0.000	0.000	0.000
35	A	109	VAL	0	-0.007	0.005	12.181	0.079	0.079	0.000	0.000	0.000	0.000
36	A	110	LEU	0	-0.044	-0.024	12.999	-0.007	-0.007	0.000	0.000	0.000	0.000
37	A	111	GLY	0	0.023	0.011	16.814	0.011	0.011	0.000	0.000	0.000	0.000
38	A	112	TYR	0	-0.008	-0.008	20.506	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	113	ASN	0	0.044	0.014	23.768	0.005	0.005	0.000	0.000	0.000	0.000
40	A	114	HIS	0	-0.020	-0.021	26.925	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	115	ASN	0	-0.053	-0.033	30.113	0.000	0.000	0.000	0.000	0.000	0.000
42	A	116	GLY	0	0.031	0.021	26.663	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	117	GLU	-1	-0.883	-0.903	26.522	-0.029	-0.029	0.000	0.000	0.000	0.000
44	A	118	TRP	0	-0.022	-0.005	24.503	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	119	CYS	0	-0.016	-0.010	19.913	-0.005	-0.005	0.000	0.000	0.000	0.000
46	A	120	GLU	-1	-0.867	-0.900	17.740	0.104	0.104	0.000	0.000	0.000	0.000
47	A	121	ALA	0	0.000	-0.014	15.911	-0.027	-0.027	0.000	0.000	0.000	0.000
48	A	122	GLN	0	0.023	-0.001	10.509	0.021	0.021	0.000	0.000	0.000	0.000
49	A	123	THR	0	-0.006	-0.024	10.450	-0.103	-0.103	0.000	0.000	0.000	0.000
50	A	124	LYS	1	0.880	0.928	3.663	1.170	1.511	0.002	-0.120	-0.224	0.000
51	A	125	ASN	0	-0.018	-0.001	8.723	0.204	0.204	0.000	0.000	0.000	0.000
52	A	126	GLY	0	0.015	0.018	12.190	0.021	0.021	0.000	0.000	0.000	0.000
53	A	127	GLN	0	-0.054	-0.049	13.353	0.015	0.015	0.000	0.000	0.000	0.000
54	A	128	GLY	0	0.032	0.024	15.558	0.010	0.010	0.000	0.000	0.000	0.000
55	A	129	TRP	0	-0.037	-0.018	18.822	-0.030	-0.030	0.000	0.000	0.000	0.000
56	A	130	VAL	0	0.006	0.002	18.709	0.003	0.003	0.000	0.000	0.000	0.000
57	A	131	PRO	0	0.015	0.024	21.899	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	132	SER	0	0.001	-0.039	22.828	-0.014	-0.014	0.000	0.000	0.000	0.000
59	A	133	ASN	0	0.007	-0.004	23.576	-0.015	-0.015	0.000	0.000	0.000	0.000
60	A	134	TYR	0	-0.004	-0.004	22.728	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	135	ILE	0	-0.057	-0.021	18.463	-0.018	-0.018	0.000	0.000	0.000	0.000
62	A	136	THR	0	0.032	0.015	19.306	0.024	0.024	0.000	0.000	0.000	0.000
63	A	137	PRO	0	-0.015	0.006	17.173	-0.036	-0.036	0.000	0.000	0.000	0.000
64	A	138	VAL	0	-0.037	-0.027	13.245	0.004	0.004	0.000	0.000	0.000	0.000
65	A	139	ASN	0	-0.058	-0.027	12.596	0.054	0.054	0.000	0.000	0.000	0.000
66	A	140	SER	0	0.009	-0.036	16.395	0.019	0.019	0.000	0.000	0.000	0.000
67	A	141	LEU	0	-0.001	-0.011	18.682	-0.003	-0.003	0.000	0.000	0.000	0.000
68	A	142	GLU	-1	-0.853	-0.889	21.040	-0.118	-0.118	0.000	0.000	0.000	0.000
69	A	143	LYS	1	0.825	0.925	16.169	0.302	0.302	0.000	0.000	0.000	0.000
70	A	144	HIS	0	-0.037	-0.005	19.285	0.010	0.010	0.000	0.000	0.000	0.000
71	A	145	SER	0	0.041	0.012	24.443	0.006	0.006	0.000	0.000	0.000	0.000
72	A	146	TRP	0	0.044	0.020	22.578	0.007	0.007	0.000	0.000	0.000	0.000
73	A	147	TYR	0	-0.101	-0.096	23.862	0.009	0.009	0.000	0.000	0.000	0.000
74	A	148	HIS	0	0.012	-0.015	26.888	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	149	GLY	0	0.057	0.047	26.630	0.001	0.001	0.000	0.000	0.000	0.000
76	A	150	PRO	0	-0.008	0.000	27.600	0.008	0.008	0.000	0.000	0.000	0.000
77	A	151	VAL	0	0.003	0.006	30.206	0.001	0.001	0.000	0.000	0.000	0.000
78	A	152	SER	0	0.039	0.037	33.456	0.004	0.004	0.000	0.000	0.000	0.000
79	A	153	ARG	1	0.819	0.889	36.431	0.017	0.017	0.000	0.000	0.000	0.000
80	A	154	ASN	0	0.063	0.015	38.084	-0.001	-0.001	0.000	0.000	0.000	0.000
81	A	155	ALA	0	0.038	0.030	37.370	0.000	0.000	0.000	0.000	0.000	0.000
82	A	156	ALA	0	0.048	0.021	35.432	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	157	GLU	-1	-0.836	-0.918	37.217	-0.022	-0.022	0.000	0.000	0.000	0.000
84	A	158	TYR	0	-0.017	0.001	40.372	0.000	0.000	0.000	0.000	0.000	0.000
85	A	159	LEU	0	0.001	0.007	35.060	0.000	0.000	0.000	0.000	0.000	0.000
86	A	160	LEU	0	-0.028	0.011	35.809	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	161	SER	0	-0.009	-0.010	39.736	0.003	0.003	0.000	0.000	0.000	0.000
88	A	162	SER	0	-0.055	-0.023	42.239	0.001	0.001	0.000	0.000	0.000	0.000
89	A	163	GLY	0	0.049	0.025	40.721	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	164	ILE	0	0.008	0.002	38.898	0.003	0.003	0.000	0.000	0.000	0.000
91	A	165	ASN	0	-0.004	-0.020	40.432	-0.002	-0.002	0.000	0.000	0.000	0.000
92	A	166	GLY	0	0.081	0.048	37.262	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	167	SER	0	-0.061	-0.044	35.549	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	168	PHE	0	-0.026	-0.019	28.600	0.003	0.003	0.000	0.000	0.000	0.000
95	A	169	LEU	0	0.000	0.020	31.345	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	170	VAL	0	-0.033	-0.016	25.980	0.006	0.006	0.000	0.000	0.000	0.000
97	A	171	ARG	1	0.859	0.916	28.670	0.029	0.029	0.000	0.000	0.000	0.000
98	A	172	GLU	-1	-0.791	-0.868	23.924	-0.086	-0.086	0.000	0.000	0.000	0.000
99	A	173	SER	0	-0.006	-0.011	28.581	0.002	0.002	0.000	0.000	0.000	0.000
100	A	174	GLU	-1	-0.822	-0.938	29.986	-0.041	-0.041	0.000	0.000	0.000	0.000
101	A	175	SER	0	-0.034	0.005	31.729	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	176	SER	0	0.018	-0.009	27.436	0.001	0.001	0.000	0.000	0.000	0.000
103	A	177	PRO	0	0.070	0.040	23.760	0.004	0.004	0.000	0.000	0.000	0.000
104	A	178	GLY	0	0.023	0.022	23.548	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	179	GLN	0	-0.011	-0.001	24.498	0.004	0.004	0.000	0.000	0.000	0.000
106	A	180	ARG	1	0.909	0.950	20.636	0.078	0.078	0.000	0.000	0.000	0.000
107	A	181	SER	0	-0.066	-0.042	27.580	0.010	0.010	0.000	0.000	0.000	0.000
108	A	182	ILE	0	0.023	0.028	29.279	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	183	SER	0	-0.016	-0.016	31.531	0.004	0.004	0.000	0.000	0.000	0.000
110	A	184	LEU	0	0.018	0.000	34.442	-0.003	-0.003	0.000	0.000	0.000	0.000
111	A	185	ARG	1	0.841	0.921	36.696	0.031	0.031	0.000	0.000	0.000	0.000
112	A	186	TYR	0	-0.055	-0.060	39.852	0.000	0.000	0.000	0.000	0.000	0.000
113	A	187	GLU	-1	-0.764	-0.856	42.355	-0.017	-0.017	0.000	0.000	0.000	0.000
114	A	188	GLY	0	-0.021	-0.002	45.605	0.001	0.001	0.000	0.000	0.000	0.000
115	A	189	ARG	1	0.870	0.940	44.204	0.015	0.015	0.000	0.000	0.000	0.000
116	A	190	VAL	0	0.023	0.010	39.232	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	191	TYR	0	-0.029	-0.001	39.118	0.004	0.004	0.000	0.000	0.000	0.000
118	A	192	HIS	0	-0.023	-0.005	36.156	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	193	TYR	0	0.029	0.022	33.146	0.003	0.003	0.000	0.000	0.000	0.000
120	A	194	ARG	1	0.844	0.916	30.876	0.013	0.013	0.000	0.000	0.000	0.000
121	A	195	ILE	0	0.015	0.012	25.128	0.001	0.001	0.000	0.000	0.000	0.000
122	A	196	ASN	0	-0.022	-0.004	27.311	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	197	THR	0	-0.002	-0.009	21.882	-0.008	-0.008	0.000	0.000	0.000	0.000
124	A	198	ALA	0	-0.031	-0.007	23.760	0.003	0.003	0.000	0.000	0.000	0.000
125	A	199	SER	0	0.028	0.001	23.092	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	200	ASP	-1	-0.875	-0.942	19.944	0.084	0.084	0.000	0.000	0.000	0.000
127	A	201	GLY	0	0.012	0.009	18.602	0.010	0.010	0.000	0.000	0.000	0.000
128	A	202	LYS	1	0.847	0.930	18.413	-0.090	-0.090	0.000	0.000	0.000	0.000
129	A	203	LEU	0	0.009	0.012	19.954	-0.001	-0.001	0.000	0.000	0.000	0.000
130	A	204	TYR	0	0.002	-0.011	23.138	0.004	0.004	0.000	0.000	0.000	0.000
131	A	205	VAL	0	-0.004	-0.007	26.674	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	206	SER	0	-0.005	-0.022	30.334	0.002	0.002	0.000	0.000	0.000	0.000
133	A	207	SER	0	-0.059	-0.046	30.053	0.001	0.001	0.000	0.000	0.000	0.000
134	A	208	GLU	-1	-0.815	-0.887	29.253	0.026	0.026	0.000	0.000	0.000	0.000
135	A	209	SER	0	-0.065	-0.046	27.866	0.004	0.004	0.000	0.000	0.000	0.000
136	A	210	ARG	1	0.833	0.905	24.175	-0.039	-0.039	0.000	0.000	0.000	0.000
137	A	211	PHE	0	0.018	0.007	21.463	0.002	0.002	0.000	0.000	0.000	0.000
138	A	212	ASN	0	-0.020	-0.017	15.477	0.029	0.029	0.000	0.000	0.000	0.000
139	A	213	THR	0	-0.022	-0.010	16.227	-0.016	-0.016	0.000	0.000	0.000	0.000
140	A	214	LEU	0	0.052	0.017	18.248	0.011	0.011	0.000	0.000	0.000	0.000
141	A	215	ALA	0	0.001	0.005	19.269	0.006	0.006	0.000	0.000	0.000	0.000
142	A	216	GLU	-1	-0.765	-0.887	18.714	-0.012	-0.012	0.000	0.000	0.000	0.000
143	A	217	LEU	0	-0.032	0.017	22.073	0.006	0.006	0.000	0.000	0.000	0.000
144	A	218	VAL	0	0.022	-0.005	24.186	0.006	0.006	0.000	0.000	0.000	0.000
145	A	219	HIS	0	-0.009	0.014	22.270	0.007	0.007	0.000	0.000	0.000	0.000
146	A	220	HIS	0	0.004	-0.002	25.996	0.003	0.003	0.000	0.000	0.000	0.000
147	A	221	HIS	1	0.812	0.902	27.813	0.018	0.018	0.000	0.000	0.000	0.000
148	A	222	SER	0	-0.014	-0.009	29.324	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	223	THR	0	-0.077	-0.032	29.450	0.001	0.001	0.000	0.000	0.000	0.000
150	A	224	VAL	0	-0.011	-0.020	31.719	0.003	0.003	0.000	0.000	0.000	0.000
151	A	225	ALA	0	0.022	0.017	32.992	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	226	ASP	-1	-0.787	-0.844	31.428	-0.002	-0.002	0.000	0.000	0.000	0.000
153	A	227	GLY	0	0.062	0.032	33.588	-0.001	-0.001	0.000	0.000	0.000	0.000
154	A	228	LEU	0	-0.068	-0.028	32.182	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	229	ILE	0	-0.034	-0.020	36.420	0.001	0.001	0.000	0.000	0.000	0.000
156	A	230	THR	0	-0.018	-0.013	37.628	0.001	0.001	0.000	0.000	0.000	0.000
157	A	231	THR	0	-0.013	0.005	34.347	0.001	0.001	0.000	0.000	0.000	0.000
158	A	232	LEU	0	-0.029	-0.019	29.512	0.000	0.000	0.000	0.000	0.000	0.000
159	A	233	HIS	0	0.015	-0.002	33.390	0.002	0.002	0.000	0.000	0.000	0.000
160	A	234	TYR	0	0.002	-0.004	25.034	-0.005	-0.005	0.000	0.000	0.000	0.000
161	A	235	PRO	0	-0.022	-0.014	29.321	0.002	0.002	0.000	0.000	0.000	0.000
162	A	236	ALA	0	0.013	0.017	30.396	-0.002	-0.002	0.000	0.000	0.000	0.000
163	A	237	PRO	0	-0.011	-0.001	28.901	-0.004	-0.004	0.000	0.000	0.000	0.000

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