FMO DATABASE

FMODB ID: N2LNQ

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	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	147
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-486206.003375
FMO2-HF: Nuclear repulsion	456558.820262
FMO2-HF: Total energy	-29647.183113
FMO2-MP2: Total energy	-29734.713801

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.
-10.264	-8.14	1.188	-1.403	-1.909	0.005

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 : 0.122 / q_NPA : 0.008

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	0.888	1.062	4.360	-5.282	-4.917	0.001	-0.172	-0.194	0.000
5	A	3	PRO	0	0.030	-0.090	3.856	-2.270	-0.714	-0.005	-0.887	-0.664	0.005
6	A	4	TYR	0	0.126	0.020	6.379	-0.313	-0.313	0.000	0.000	0.000	0.000
7	A	4	TYR	0	-0.068	0.102	7.249	0.068	0.068	0.000	0.000	0.000	0.000
8	A	5	MET	0	0.096	-0.096	4.474	0.193	0.261	-0.001	-0.010	-0.057	0.000
9	A	5	MET	0	-0.073	0.118	2.377	-1.209	-1.394	1.198	-0.237	-0.776	0.000
10	A	6	LYS	0	0.119	-0.067	5.872	-0.135	-0.135	0.000	0.000	0.000	0.000
11	A	6	LYS	1	0.750	0.980	7.327	1.317	1.317	0.000	0.000	0.000	0.000
12	A	7	ALA	0	0.094	-0.088	8.058	0.081	0.081	0.000	0.000	0.000	0.000
13	A	7	ALA	0	-0.092	0.089	10.737	0.033	0.033	0.000	0.000	0.000	0.000
14	A	8	LEU	0	0.089	-0.087	9.503	0.000	0.000	0.000	0.000	0.000	0.000
15	A	8	LEU	0	-0.082	0.104	8.892	0.035	0.035	0.000	0.000	0.000	0.000
16	A	9	ILE	0	0.115	-0.067	9.495	0.206	0.206	0.000	0.000	0.000	0.000
17	A	9	ILE	0	-0.083	0.088	6.999	-0.055	-0.055	0.000	0.000	0.000	0.000
18	A	10	TYR	0	0.144	-0.066	10.992	0.089	0.089	0.000	0.000	0.000	0.000
19	A	10	TYR	0	-0.147	0.042	12.759	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	11	GLU	0	0.118	-0.106	13.582	0.023	0.023	0.000	0.000	0.000	0.000
21	A	11	GLU	-1	-0.979	-0.834	14.584	-0.189	-0.189	0.000	0.000	0.000	0.000
22	A	12	THR	0	-0.014	-0.093	14.102	0.069	0.069	0.000	0.000	0.000	0.000
23	A	12	THR	0	-0.039	0.057	13.214	0.033	0.033	0.000	0.000	0.000	0.000
24	A	13	LEU	0	0.010	-0.100	15.273	0.058	0.058	0.000	0.000	0.000	0.000
25	A	13	LEU	0	-0.041	0.088	13.879	-0.012	-0.012	0.000	0.000	0.000	0.000
26	A	14	VAL	0	0.082	-0.087	16.964	0.022	0.022	0.000	0.000	0.000	0.000
27	A	14	VAL	0	-0.068	0.112	18.007	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	15	ASN	0	0.128	-0.045	18.729	0.020	0.020	0.000	0.000	0.000	0.000
29	A	15	ASN	0	-0.173	0.021	18.535	0.037	0.037	0.000	0.000	0.000	0.000
30	A	16	LEU	0	0.085	-0.088	19.364	0.039	0.039	0.000	0.000	0.000	0.000
31	A	16	LEU	0	-0.140	0.061	17.563	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	17	ALA	0	0.123	-0.084	21.067	0.018	0.018	0.000	0.000	0.000	0.000
33	A	17	ALA	0	-0.116	0.083	21.827	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	18	ASN	0	-0.012	-0.083	23.055	0.007	0.007	0.000	0.000	0.000	0.000
35	A	18	ASN	0	-0.158	0.014	22.922	0.013	0.013	0.000	0.000	0.000	0.000
36	A	19	GLN	0	0.055	-0.083	24.151	0.018	0.018	0.000	0.000	0.000	0.000
37	A	19	GLN	0	-0.068	0.082	22.624	0.014	0.014	0.000	0.000	0.000	0.000
38	A	20	ASP	0	0.100	-0.087	25.440	-0.019	-0.019	0.000	0.000	0.000	0.000
39	A	20	ASP	-1	-0.938	-0.831	28.765	-0.074	-0.074	0.000	0.000	0.000	0.000
40	A	21	PRO	0	-0.009	-0.140	26.384	0.002	0.002	0.000	0.000	0.000	0.000
41	A	22	GLU	0	0.121	0.020	26.509	-0.007	-0.007	0.000	0.000	0.000	0.000
42	A	22	GLU	-1	-1.047	-0.855	29.258	-0.041	-0.041	0.000	0.000	0.000	0.000
43	A	23	GLN	0	0.028	-0.112	25.181	0.006	0.006	0.000	0.000	0.000	0.000
44	A	23	GLN	0	-0.068	0.090	24.269	0.008	0.008	0.000	0.000	0.000	0.000
45	A	24	HIS	0	0.115	-0.141	22.166	0.014	0.014	0.000	0.000	0.000	0.000
46	A	24	HIS	0	-0.084	0.099	22.585	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	25	ALA	0	0.048	-0.088	21.037	-0.023	-0.023	0.000	0.000	0.000	0.000
48	A	25	ALA	0	-0.069	0.106	23.830	0.002	0.002	0.000	0.000	0.000	0.000
49	A	26	THR	0	-0.003	-0.087	20.736	0.000	0.000	0.000	0.000	0.000	0.000
50	A	26	THR	0	-0.035	0.057	21.360	0.000	0.000	0.000	0.000	0.000	0.000
51	A	27	ILE	0	0.091	-0.063	18.799	0.043	0.043	0.000	0.000	0.000	0.000
52	A	27	ILE	0	-0.069	0.094	18.023	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	28	ARG	0	0.057	-0.094	16.571	0.004	0.004	0.000	0.000	0.000	0.000
54	A	28	ARG	1	0.833	1.026	17.708	0.179	0.179	0.000	0.000	0.000	0.000
55	A	29	GLN	0	0.112	-0.077	15.596	-0.021	-0.021	0.000	0.000	0.000	0.000
56	A	29	GLN	0	-0.129	0.067	17.321	-0.049	-0.049	0.000	0.000	0.000	0.000
57	A	30	ASN	0	0.135	-0.054	15.691	0.053	0.053	0.000	0.000	0.000	0.000
58	A	30	ASN	0	-0.154	0.040	15.046	0.042	0.042	0.000	0.000	0.000	0.000
59	A	31	LEU	0	0.117	-0.094	12.420	0.132	0.132	0.000	0.000	0.000	0.000
60	A	31	LEU	0	-0.108	0.098	9.973	-0.034	-0.034	0.000	0.000	0.000	0.000
61	A	32	TYR	0	0.034	-0.103	10.966	0.066	0.066	0.000	0.000	0.000	0.000
62	A	32	TYR	0	-0.147	0.036	11.729	-0.023	-0.023	0.000	0.000	0.000	0.000
63	A	33	GLU	0	0.070	-0.099	11.859	0.135	0.135	0.000	0.000	0.000	0.000
64	A	33	GLU	-1	-0.938	-0.835	15.307	0.259	0.259	0.000	0.000	0.000	0.000
65	A	34	GLN	0	0.039	-0.073	11.473	0.140	0.140	0.000	0.000	0.000	0.000
66	A	34	GLN	0	-0.074	0.077	10.957	-0.073	-0.073	0.000	0.000	0.000	0.000
67	A	35	LEU	0	-0.012	-0.128	7.693	0.353	0.353	0.000	0.000	0.000	0.000
68	A	35	LEU	0	-0.126	0.058	5.810	-0.069	-0.069	0.000	0.000	0.000	0.000
69	A	36	ASP	0	0.086	-0.087	7.560	0.339	0.339	0.000	0.000	0.000	0.000
70	A	36	ASP	-1	-1.003	-0.842	9.720	0.969	0.969	0.000	0.000	0.000	0.000
71	A	37	LEU	0	0.060	-0.122	8.278	0.197	0.197	0.000	0.000	0.000	0.000
72	A	37	LEU	0	-0.109	0.090	5.537	-0.104	-0.104	0.000	0.000	0.000	0.000
73	A	38	PRO	0	0.030	-0.084	8.298	-0.038	-0.038	0.000	0.000	0.000	0.000
74	A	39	PHE	0	0.190	0.040	11.402	-0.175	-0.175	0.000	0.000	0.000	0.000
75	A	39	PHE	0	-0.093	0.083	15.820	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	40	ASP	0	0.020	-0.105	13.586	-0.029	-0.029	0.000	0.000	0.000	0.000
77	A	40	ASP	-1	-0.894	-0.847	11.557	-0.565	-0.565	0.000	0.000	0.000	0.000
78	A	41	LYS	0	0.103	-0.093	9.209	-0.053	-0.053	0.000	0.000	0.000	0.000
79	A	41	LYS	1	0.708	0.995	6.843	2.244	2.244	0.000	0.000	0.000	0.000
80	A	42	GLN	0	0.088	-0.138	10.482	-0.210	-0.210	0.000	0.000	0.000	0.000
81	A	42	GLN	0	-0.061	0.116	12.182	0.001	0.001	0.000	0.000	0.000	0.000
82	A	43	LEU	0	0.091	-0.071	12.494	-0.026	-0.026	0.000	0.000	0.000	0.000
83	A	43	LEU	0	-0.100	0.106	15.394	0.012	0.012	0.000	0.000	0.000	0.000
84	A	44	ALA	0	0.090	-0.102	11.825	0.104	0.104	0.000	0.000	0.000	0.000
85	A	44	ALA	0	-0.059	0.108	10.938	-0.050	-0.050	0.000	0.000	0.000	0.000
86	A	45	LEU	0	0.094	-0.094	10.903	-0.049	-0.049	0.000	0.000	0.000	0.000
87	A	45	LEU	0	-0.095	0.108	9.203	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	46	TYR	0	0.090	-0.102	11.768	0.034	0.034	0.000	0.000	0.000	0.000
89	A	46	TYR	0	-0.093	0.078	16.117	0.024	0.024	0.000	0.000	0.000	0.000
90	A	47	ALA	0	0.066	-0.109	15.550	0.026	0.026	0.000	0.000	0.000	0.000
91	A	47	ALA	0	-0.076	0.106	16.549	0.007	0.007	0.000	0.000	0.000	0.000
92	A	48	GLY	0	-0.023	-0.110	14.320	0.043	0.043	0.000	0.000	0.000	0.000
93	A	49	ALA	0	0.116	-0.006	13.820	0.000	0.000	0.000	0.000	0.000	0.000
94	A	49	ALA	0	-0.088	0.102	13.200	-0.029	-0.029	0.000	0.000	0.000	0.000
95	A	50	LEU	0	0.035	-0.111	15.006	0.059	0.059	0.000	0.000	0.000	0.000
96	A	50	LEU	0	-0.052	0.113	13.714	0.013	0.013	0.000	0.000	0.000	0.000
97	A	51	GLY	0	0.036	-0.067	16.620	0.072	0.072	0.000	0.000	0.000	0.000
98	A	52	PRO	0	0.012	0.005	17.898	0.055	0.055	0.000	0.000	0.000	0.000
99	A	53	ALA	0	0.080	-0.004	18.912	0.034	0.034	0.000	0.000	0.000	0.000
100	A	53	ALA	0	-0.054	0.117	18.238	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	54	SER	0	0.016	-0.087	20.224	0.027	0.027	0.000	0.000	0.000	0.000
102	A	54	SER	0	-0.044	0.048	20.199	0.017	0.017	0.000	0.000	0.000	0.000
103	A	55	SER	0	-0.034	-0.053	22.421	0.034	0.034	0.000	0.000	0.000	0.000
104	A	55	SER	0	-0.111	0.020	22.992	-0.002	-0.002	0.000	0.000	0.000	0.000
105	A	56	GLY	0	0.094	-0.057	24.519	0.008	0.008	0.000	0.000	0.000	0.000
106	A	57	LYS	0	0.020	-0.003	23.548	0.019	0.019	0.000	0.000	0.000	0.000
107	A	57	LYS	1	0.775	1.004	22.767	0.264	0.264	0.000	0.000	0.000	0.000
108	A	58	LEU	0	0.105	-0.071	20.428	-0.019	-0.019	0.000	0.000	0.000	0.000
109	A	58	LEU	0	-0.152	0.054	17.269	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	59	GLU	0	0.085	-0.112	21.813	0.000	0.000	0.000	0.000	0.000	0.000
111	A	59	GLU	-1	-0.935	-0.803	24.446	-0.224	-0.224	0.000	0.000	0.000	0.000
112	A	60	ASN	0	0.144	-0.074	23.218	0.021	0.021	0.000	0.000	0.000	0.000
113	A	60	ASN	0	-0.161	0.044	23.843	-0.017	-0.017	0.000	0.000	0.000	0.000
114	A	61	HIS	0	0.139	-0.063	20.524	-0.039	-0.039	0.000	0.000	0.000	0.000
115	A	61	HIS	0	-0.059	0.096	18.866	0.001	0.001	0.000	0.000	0.000	0.000
116	A	62	GLU	0	0.126	-0.077	19.311	-0.061	-0.061	0.000	0.000	0.000	0.000
117	A	62	GLU	-1	-0.990	-0.838	20.315	-0.497	-0.497	0.000	0.000	0.000	0.000
118	A	63	ALA	0	0.114	-0.086	18.995	-0.074	-0.074	0.000	0.000	0.000	0.000
119	A	63	ALA	0	-0.062	0.108	21.127	0.011	0.011	0.000	0.000	0.000	0.000
120	A	64	ILE	0	0.099	-0.100	17.474	-0.069	-0.069	0.000	0.000	0.000	0.000
121	A	64	ILE	0	-0.109	0.109	16.357	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	65	SER	0	0.089	-0.089	14.896	-0.112	-0.112	0.000	0.000	0.000	0.000
123	A	65	SER	0	-0.044	0.077	14.845	0.024	0.024	0.000	0.000	0.000	0.000
124	A	66	ASN	0	-0.005	-0.124	14.207	-0.178	-0.178	0.000	0.000	0.000	0.000
125	A	66	ASN	0	-0.111	0.062	17.559	0.057	0.057	0.000	0.000	0.000	0.000
126	A	67	ALA	0	0.081	-0.066	14.676	-0.134	-0.134	0.000	0.000	0.000	0.000
127	A	67	ALA	0	-0.039	0.125	15.448	0.022	0.022	0.000	0.000	0.000	0.000
128	A	68	VAL	0	0.084	-0.091	11.418	-0.145	-0.145	0.000	0.000	0.000	0.000
129	A	68	VAL	0	-0.106	0.090	10.210	-0.012	-0.012	0.000	0.000	0.000	0.000
130	A	69	ASP	0	0.057	-0.095	9.868	-0.453	-0.453	0.000	0.000	0.000	0.000
131	A	69	ASP	-1	-0.888	-0.804	11.294	-1.376	-1.376	0.000	0.000	0.000	0.000
132	A	70	SER	0	0.060	-0.093	10.166	-0.374	-0.374	0.000	0.000	0.000	0.000
133	A	70	SER	0	-0.057	0.049	13.579	0.071	0.071	0.000	0.000	0.000	0.000
134	A	71	VAL	0	0.056	-0.090	9.978	-0.109	-0.109	0.000	0.000	0.000	0.000
135	A	71	VAL	0	-0.107	0.120	8.528	0.014	0.014	0.000	0.000	0.000	0.000
136	A	72	VAL	0	0.123	-0.099	5.953	-0.374	-0.374	0.000	0.000	0.000	0.000
137	A	72	VAL	0	-0.126	0.080	5.001	-0.153	-0.133	-0.001	-0.003	-0.016	0.000
138	A	73	GLN	0	0.115	-0.101	5.857	-1.434	-1.434	0.000	0.000	0.000	0.000
139	A	73	GLN	0	-0.106	0.095	9.929	0.221	0.221	0.000	0.000	0.000	0.000
140	A	74	LEU	0	0.009	-0.107	8.491	0.026	0.026	0.000	0.000	0.000	0.000
141	A	74	LEU	0	-0.051	0.101	9.860	0.088	0.088	0.000	0.000	0.000	0.000
142	A	75	LEU	0	0.051	-0.101	5.265	0.839	0.864	-0.002	-0.001	-0.022	0.000
143	A	75	LEU	0	-0.091	0.102	4.517	-0.284	-0.243	-0.001	-0.009	-0.031	0.000
144	A	76	GLU	0	0.082	-0.086	4.408	-0.913	-0.809	-0.001	-0.023	-0.080	0.000
145	A	76	GLU	-1	-0.949	-0.816	4.247	-3.194	-3.107	0.001	-0.051	-0.037	0.000
146	A	77	ILE	0	-0.128	-0.169	5.031	1.349	1.392	-0.001	-0.010	-0.032	0.000
147	A	77	ILE	0	0.015	0.004	7.618	0.095	0.095	0.000	0.000	0.000	0.000

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