FMO DATABASE

FMODB ID: J2VQ9

Calculation Name: 2B8I-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2B8I

Chain ID: A

ChEMBL ID:

UniProt ID: Q56GA4

Base Structure: X-ray

Registration Date: 2025-07-08

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

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
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	147
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-485260.592226
FMO2-HF: Nuclear repulsion	455614.979102
FMO2-HF: Total energy	-29645.613125
FMO2-MP2: Total energy	-29733.258532

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:1:ILE)

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

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.
-12.165	-9.421	0.018	-1.237	-1.527	0.007

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.114 / q_NPA : -0.029

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].
4	A	2	ARG	1	0.879	1.060	3.973	-5.217	-4.784	0.004	-0.211	-0.226	0.001
5	A	3	PRO	0	0.043	-0.088	3.804	-2.737	-0.984	-0.013	-1.074	-0.667	0.007
6	A	4	TYR	0	0.116	-0.006	6.722	-0.234	-0.234	0.000	0.000	0.000	0.000
7	A	4	TYR	0	-0.052	0.114	7.571	0.072	0.072	0.000	0.000	0.000	0.000
8	A	5	MET	0	0.099	-0.101	4.821	0.319	0.372	-0.002	-0.004	-0.048	0.000
9	A	5	MET	0	-0.057	0.132	3.307	-1.144	-1.031	0.033	0.178	-0.324	-0.001
10	A	6	LYS	0	0.144	-0.073	6.201	-0.023	-0.023	0.000	0.000	0.000	0.000
11	A	6	LYS	1	0.872	1.079	7.061	1.740	1.740	0.000	0.000	0.000	0.000
12	A	7	ALA	0	0.074	-0.100	7.945	0.136	0.136	0.000	0.000	0.000	0.000
13	A	7	ALA	0	-0.090	0.100	11.024	0.034	0.034	0.000	0.000	0.000	0.000
14	A	8	LEU	0	0.106	-0.093	9.861	0.053	0.053	0.000	0.000	0.000	0.000
15	A	8	LEU	0	-0.105	0.110	9.038	0.021	0.021	0.000	0.000	0.000	0.000
16	A	9	ILE	0	0.115	-0.076	9.823	0.232	0.232	0.000	0.000	0.000	0.000
17	A	9	ILE	0	-0.068	0.095	7.222	-0.053	-0.053	0.000	0.000	0.000	0.000
18	A	10	TYR	0	0.133	-0.072	11.132	0.102	0.102	0.000	0.000	0.000	0.000
19	A	10	TYR	0	-0.121	0.067	12.634	0.007	0.007	0.000	0.000	0.000	0.000
20	A	11	GLU	0	0.089	-0.128	13.534	0.040	0.040	0.000	0.000	0.000	0.000
21	A	11	GLU	-1	-1.009	-0.836	14.733	-0.275	-0.275	0.000	0.000	0.000	0.000
22	A	12	THR	0	0.032	-0.071	14.436	0.069	0.069	0.000	0.000	0.000	0.000
23	A	12	THR	0	-0.052	0.045	13.633	0.037	0.037	0.000	0.000	0.000	0.000
24	A	13	LEU	0	-0.002	-0.110	15.318	0.077	0.077	0.000	0.000	0.000	0.000
25	A	13	LEU	0	-0.045	0.101	13.979	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	14	VAL	0	0.077	-0.098	17.005	0.034	0.034	0.000	0.000	0.000	0.000
27	A	14	VAL	0	-0.052	0.111	17.958	0.000	0.000	0.000	0.000	0.000	0.000
28	A	15	ASN	0	0.057	-0.100	19.048	0.028	0.028	0.000	0.000	0.000	0.000
29	A	15	ASN	0	-0.094	0.078	18.570	0.008	0.008	0.000	0.000	0.000	0.000
30	A	16	LEU	0	0.045	-0.090	19.640	0.046	0.046	0.000	0.000	0.000	0.000
31	A	16	LEU	0	-0.120	0.071	17.541	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	17	ALA	0	0.132	-0.082	21.101	0.028	0.028	0.000	0.000	0.000	0.000
33	A	17	ALA	0	-0.132	0.074	21.547	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	18	ASN	0	0.031	-0.074	22.984	0.011	0.011	0.000	0.000	0.000	0.000
35	A	18	ASN	0	-0.172	0.020	23.024	0.018	0.018	0.000	0.000	0.000	0.000
36	A	19	GLN	0	0.044	-0.092	24.454	0.018	0.018	0.000	0.000	0.000	0.000
37	A	19	GLN	0	-0.064	0.076	23.551	0.020	0.020	0.000	0.000	0.000	0.000
38	A	20	ASP	0	0.093	-0.111	25.920	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	20	ASP	-1	-0.945	-0.839	29.251	-0.088	-0.088	0.000	0.000	0.000	0.000
40	A	21	PRO	0	-0.006	-0.131	26.706	0.003	0.003	0.000	0.000	0.000	0.000
41	A	22	GLU	0	0.128	-0.004	27.038	-0.004	-0.004	0.000	0.000	0.000	0.000
42	A	22	GLU	-1	-1.022	-0.829	29.685	-0.051	-0.051	0.000	0.000	0.000	0.000
43	A	23	GLN	0	0.013	-0.115	25.591	0.012	0.012	0.000	0.000	0.000	0.000
44	A	23	GLN	0	-0.068	0.109	24.736	0.005	0.005	0.000	0.000	0.000	0.000
45	A	24	HIS	0	0.125	-0.122	22.592	0.010	0.010	0.000	0.000	0.000	0.000
46	A	24	HIS	0	-0.087	0.123	22.915	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	25	ALA	0	0.073	-0.116	21.277	-0.020	-0.020	0.000	0.000	0.000	0.000
48	A	25	ALA	0	-0.065	0.112	23.749	0.003	0.003	0.000	0.000	0.000	0.000
49	A	26	THR	0	-0.030	-0.090	20.964	0.006	0.006	0.000	0.000	0.000	0.000
50	A	26	THR	0	-0.019	0.069	21.966	0.003	0.003	0.000	0.000	0.000	0.000
51	A	27	ILE	0	0.085	-0.081	19.507	0.045	0.045	0.000	0.000	0.000	0.000
52	A	27	ILE	0	-0.051	0.092	18.261	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	28	ARG	0	0.034	-0.094	16.855	0.000	0.000	0.000	0.000	0.000	0.000
54	A	28	ARG	1	0.844	1.041	17.691	0.180	0.180	0.000	0.000	0.000	0.000
55	A	29	GLN	0	0.107	-0.091	15.887	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	29	GLN	0	-0.126	0.074	17.375	-0.052	-0.052	0.000	0.000	0.000	0.000
57	A	30	ASN	0	0.141	-0.048	16.258	0.063	0.063	0.000	0.000	0.000	0.000
58	A	30	ASN	0	-0.119	0.055	16.723	0.060	0.060	0.000	0.000	0.000	0.000
59	A	31	LEU	0	0.125	-0.089	13.029	0.120	0.120	0.000	0.000	0.000	0.000
60	A	31	LEU	0	-0.113	0.103	10.296	-0.033	-0.033	0.000	0.000	0.000	0.000
61	A	32	TYR	0	0.049	-0.110	11.555	0.075	0.075	0.000	0.000	0.000	0.000
62	A	32	TYR	0	-0.159	0.055	12.317	-0.033	-0.033	0.000	0.000	0.000	0.000
63	A	33	GLU	0	0.065	-0.107	12.226	0.126	0.126	0.000	0.000	0.000	0.000
64	A	33	GLU	-1	-0.970	-0.828	15.506	0.339	0.339	0.000	0.000	0.000	0.000
65	A	34	GLN	0	0.045	-0.080	11.654	0.146	0.146	0.000	0.000	0.000	0.000
66	A	34	GLN	0	-0.074	0.063	11.172	-0.085	-0.085	0.000	0.000	0.000	0.000
67	A	35	LEU	0	0.023	-0.134	7.830	0.342	0.342	0.000	0.000	0.000	0.000
68	A	35	LEU	0	-0.150	0.043	6.500	-0.083	-0.083	0.000	0.000	0.000	0.000
69	A	36	ASP	0	0.066	-0.098	7.839	0.420	0.420	0.000	0.000	0.000	0.000
70	A	36	ASP	-1	-0.990	-0.834	9.888	1.126	1.126	0.000	0.000	0.000	0.000
71	A	37	LEU	0	0.015	-0.144	8.823	0.357	0.357	0.000	0.000	0.000	0.000
72	A	37	LEU	0	-0.095	0.129	6.193	-0.122	-0.122	0.000	0.000	0.000	0.000
73	A	38	PRO	0	0.035	-0.072	8.809	-0.107	-0.107	0.000	0.000	0.000	0.000
74	A	39	PHE	0	0.217	0.039	11.978	-0.135	-0.135	0.000	0.000	0.000	0.000
75	A	39	PHE	0	-0.092	0.087	16.243	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	40	ASP	0	0.030	-0.109	13.880	-0.069	-0.069	0.000	0.000	0.000	0.000
77	A	40	ASP	-1	-0.902	-0.828	11.990	-0.186	-0.186	0.000	0.000	0.000	0.000
78	A	41	LYS	0	0.066	-0.112	9.434	-0.131	-0.131	0.000	0.000	0.000	0.000
79	A	41	LYS	1	0.853	1.061	6.251	1.126	1.126	0.000	0.000	0.000	0.000
80	A	42	GLN	0	0.071	-0.126	10.709	-0.234	-0.234	0.000	0.000	0.000	0.000
81	A	42	GLN	0	-0.058	0.110	12.256	0.050	0.050	0.000	0.000	0.000	0.000
82	A	43	LEU	0	0.112	-0.081	12.575	-0.066	-0.066	0.000	0.000	0.000	0.000
83	A	43	LEU	0	-0.097	0.111	15.419	0.011	0.011	0.000	0.000	0.000	0.000
84	A	44	ALA	0	0.072	-0.094	11.951	0.076	0.076	0.000	0.000	0.000	0.000
85	A	44	ALA	0	-0.035	0.111	11.051	-0.041	-0.041	0.000	0.000	0.000	0.000
86	A	45	LEU	0	0.094	-0.109	11.163	-0.101	-0.101	0.000	0.000	0.000	0.000
87	A	45	LEU	0	-0.090	0.116	9.677	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	46	TYR	0	0.095	-0.109	11.851	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	46	TYR	0	-0.108	0.076	16.176	0.023	0.023	0.000	0.000	0.000	0.000
90	A	47	ALA	0	0.059	-0.126	15.578	0.021	0.021	0.000	0.000	0.000	0.000
91	A	47	ALA	0	-0.075	0.126	16.462	0.007	0.007	0.000	0.000	0.000	0.000
92	A	48	GLY	0	-0.040	-0.100	14.533	0.039	0.039	0.000	0.000	0.000	0.000
93	A	49	ALA	0	0.098	-0.014	13.791	0.008	0.008	0.000	0.000	0.000	0.000
94	A	49	ALA	0	-0.053	0.114	13.208	-0.033	-0.033	0.000	0.000	0.000	0.000
95	A	50	LEU	0	0.027	-0.120	15.026	0.046	0.046	0.000	0.000	0.000	0.000
96	A	50	LEU	0	-0.069	0.111	13.625	0.016	0.016	0.000	0.000	0.000	0.000
97	A	51	GLY	0	0.018	-0.087	16.642	0.064	0.064	0.000	0.000	0.000	0.000
98	A	52	PRO	0	0.006	-0.012	17.779	0.052	0.052	0.000	0.000	0.000	0.000
99	A	53	ALA	0	0.100	-0.013	18.920	0.037	0.037	0.000	0.000	0.000	0.000
100	A	53	ALA	0	-0.038	0.128	18.227	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	54	SER	0	0.009	-0.057	20.179	0.024	0.024	0.000	0.000	0.000	0.000
102	A	54	SER	0	-0.059	0.040	20.275	0.019	0.019	0.000	0.000	0.000	0.000
103	A	55	SER	0	-0.057	-0.080	22.445	0.032	0.032	0.000	0.000	0.000	0.000
104	A	55	SER	0	-0.090	0.026	23.405	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	56	GLY	0	0.080	-0.056	23.953	0.017	0.017	0.000	0.000	0.000	0.000
106	A	57	LYS	0	0.018	-0.014	23.502	0.015	0.015	0.000	0.000	0.000	0.000
107	A	57	LYS	1	0.828	1.038	22.766	0.292	0.292	0.000	0.000	0.000	0.000
108	A	58	LEU	0	0.078	-0.078	20.495	-0.016	-0.016	0.000	0.000	0.000	0.000
109	A	58	LEU	0	-0.152	0.038	17.387	-0.004	-0.004	0.000	0.000	0.000	0.000
110	A	59	GLU	0	0.101	-0.131	21.610	0.003	0.003	0.000	0.000	0.000	0.000
111	A	59	GLU	-1	-0.925	-0.758	23.860	-0.257	-0.257	0.000	0.000	0.000	0.000
112	A	60	ASN	0	0.101	-0.077	22.433	0.027	0.027	0.000	0.000	0.000	0.000
113	A	60	ASN	0	-0.127	0.056	23.359	-0.019	-0.019	0.000	0.000	0.000	0.000
114	A	61	HIS	0	0.169	-0.050	20.787	-0.044	-0.044	0.000	0.000	0.000	0.000
115	A	61	HIS	0	-0.095	0.074	19.330	-0.018	-0.018	0.000	0.000	0.000	0.000
116	A	62	GLU	0	0.154	-0.093	19.505	-0.069	-0.069	0.000	0.000	0.000	0.000
117	A	62	GLU	-1	-1.037	-0.854	20.953	-0.531	-0.531	0.000	0.000	0.000	0.000
118	A	63	ALA	0	0.089	-0.090	19.265	-0.073	-0.073	0.000	0.000	0.000	0.000
119	A	63	ALA	0	-0.074	0.106	21.264	0.012	0.012	0.000	0.000	0.000	0.000
120	A	64	ILE	0	0.046	-0.130	17.555	-0.060	-0.060	0.000	0.000	0.000	0.000
121	A	64	ILE	0	-0.103	0.107	16.330	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	65	SER	0	0.074	-0.093	15.216	-0.126	-0.126	0.000	0.000	0.000	0.000
123	A	65	SER	0	-0.013	0.093	15.614	0.026	0.026	0.000	0.000	0.000	0.000
124	A	66	ASN	0	0.017	-0.109	14.323	-0.183	-0.183	0.000	0.000	0.000	0.000
125	A	66	ASN	0	-0.070	0.097	17.103	0.089	0.089	0.000	0.000	0.000	0.000
126	A	67	ALA	0	0.075	-0.086	14.455	-0.140	-0.140	0.000	0.000	0.000	0.000
127	A	67	ALA	0	-0.046	0.124	15.186	0.023	0.023	0.000	0.000	0.000	0.000
128	A	68	VAL	0	0.059	-0.114	11.318	-0.141	-0.141	0.000	0.000	0.000	0.000
129	A	68	VAL	0	-0.083	0.096	10.068	-0.016	-0.016	0.000	0.000	0.000	0.000
130	A	69	ASP	0	0.072	-0.129	9.779	-0.492	-0.492	0.000	0.000	0.000	0.000
131	A	69	ASP	-1	-1.010	-0.845	11.830	-1.436	-1.436	0.000	0.000	0.000	0.000
132	A	70	SER	0	0.051	-0.082	9.993	-0.409	-0.409	0.000	0.000	0.000	0.000
133	A	70	SER	0	-0.077	0.059	13.305	0.084	0.084	0.000	0.000	0.000	0.000
134	A	71	VAL	0	0.056	-0.099	9.923	-0.120	-0.120	0.000	0.000	0.000	0.000
135	A	71	VAL	0	-0.084	0.109	8.458	0.030	0.030	0.000	0.000	0.000	0.000
136	A	72	VAL	0	0.097	-0.116	5.911	-0.186	-0.186	0.000	0.000	0.000	0.000
137	A	72	VAL	0	-0.096	0.095	4.714	-0.286	-0.246	-0.001	-0.017	-0.022	0.000
138	A	73	GLN	0	0.169	-0.084	5.581	-1.545	-1.561	-0.002	0.001	0.017	0.000
139	A	73	GLN	0	-0.120	0.098	9.552	0.153	0.153	0.000	0.000	0.000	0.000
140	A	74	LEU	0	-0.028	-0.135	7.976	-0.102	-0.102	0.000	0.000	0.000	0.000
141	A	74	LEU	0	-0.078	0.095	9.589	0.103	0.103	0.000	0.000	0.000	0.000
142	A	75	LEU	0	-0.012	-0.129	5.232	0.897	0.924	-0.002	-0.001	-0.024	0.000
143	A	75	LEU	0	-0.082	0.105	4.551	-0.175	-0.136	-0.001	-0.009	-0.029	0.000
144	A	76	GLU	0	0.029	-0.140	4.558	-0.415	-0.307	-0.002	-0.014	-0.093	0.000
145	A	76	GLU	-1	-1.022	-0.841	3.942	-5.072	-4.921	0.005	-0.083	-0.073	0.000
146	A	77	ILE	0	-0.090	-0.114	5.195	1.059	1.102	-0.001	-0.003	-0.038	0.000
147	A	77	ILE	0	0.033	0.007	7.173	0.132	0.132	0.000	0.000	0.000	0.000

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