FMO DATABASE

FMODB ID: 8NQ9Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-485178.074608
FMO2-HF: Nuclear repulsion	455530.984289
FMO2-HF: Total energy	-29647.090319
FMO2-MP2: Total energy	-29734.652483

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.
-11.672	-8.76	0.252	-1.489	-1.678	0.008

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 : 0.112 / q_NPA : -0.002

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	0.878	1.056	4.013	-4.968	-4.534	0.003	-0.221	-0.216	0.001
5	A	3	PRO	0	0.056	-0.089	3.804	-2.963	-1.100	-0.013	-1.123	-0.727	0.007
6	A	4	TYR	0	0.124	0.015	6.722	-0.280	-0.280	0.000	0.000	0.000	0.000
7	A	4	TYR	0	-0.063	0.104	7.583	0.073	0.073	0.000	0.000	0.000	0.000
8	A	5	MET	0	0.091	-0.094	4.859	0.327	0.381	-0.002	-0.004	-0.049	0.000
9	A	5	MET	0	-0.074	0.113	2.734	-1.303	-1.112	0.269	-0.008	-0.452	0.000
10	A	6	LYS	0	0.137	-0.057	6.254	-0.052	-0.052	0.000	0.000	0.000	0.000
11	A	6	LYS	1	0.776	1.007	7.038	1.562	1.562	0.000	0.000	0.000	0.000
12	A	7	ALA	0	0.085	-0.098	7.938	0.116	0.116	0.000	0.000	0.000	0.000
13	A	7	ALA	0	-0.088	0.092	11.073	0.037	0.037	0.000	0.000	0.000	0.000
14	A	8	LEU	0	0.094	-0.082	9.907	0.052	0.052	0.000	0.000	0.000	0.000
15	A	8	LEU	0	-0.090	0.104	9.389	0.024	0.024	0.000	0.000	0.000	0.000
16	A	9	ILE	0	0.120	-0.072	9.750	0.233	0.233	0.000	0.000	0.000	0.000
17	A	9	ILE	0	-0.078	0.088	7.105	-0.059	-0.059	0.000	0.000	0.000	0.000
18	A	10	TYR	0	0.141	-0.071	11.049	0.103	0.103	0.000	0.000	0.000	0.000
19	A	10	TYR	0	-0.128	0.057	12.653	0.002	0.002	0.000	0.000	0.000	0.000
20	A	11	GLU	0	0.076	-0.120	13.494	0.040	0.040	0.000	0.000	0.000	0.000
21	A	11	GLU	-1	-0.969	-0.819	14.883	-0.287	-0.287	0.000	0.000	0.000	0.000
22	A	12	THR	0	0.009	-0.095	14.377	0.077	0.077	0.000	0.000	0.000	0.000
23	A	12	THR	0	-0.046	0.055	13.704	0.029	0.029	0.000	0.000	0.000	0.000
24	A	13	LEU	0	0.005	-0.101	15.238	0.073	0.073	0.000	0.000	0.000	0.000
25	A	13	LEU	0	-0.048	0.087	13.835	-0.011	-0.011	0.000	0.000	0.000	0.000
26	A	14	VAL	0	0.098	-0.083	16.926	0.036	0.036	0.000	0.000	0.000	0.000
27	A	14	VAL	0	-0.068	0.113	18.018	0.001	0.001	0.000	0.000	0.000	0.000
28	A	15	ASN	0	0.059	-0.106	18.960	0.032	0.032	0.000	0.000	0.000	0.000
29	A	15	ASN	0	-0.123	0.054	19.131	0.023	0.023	0.000	0.000	0.000	0.000
30	A	16	LEU	0	0.065	-0.086	19.545	0.048	0.048	0.000	0.000	0.000	0.000
31	A	16	LEU	0	-0.113	0.070	17.506	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	17	ALA	0	0.110	-0.079	21.027	0.028	0.028	0.000	0.000	0.000	0.000
33	A	17	ALA	0	-0.106	0.083	21.594	-0.009	-0.009	0.000	0.000	0.000	0.000
34	A	18	ASN	0	0.002	-0.069	22.905	0.013	0.013	0.000	0.000	0.000	0.000
35	A	18	ASN	0	-0.168	0.013	22.877	0.015	0.015	0.000	0.000	0.000	0.000
36	A	19	GLN	0	0.057	-0.086	24.352	0.020	0.020	0.000	0.000	0.000	0.000
37	A	19	GLN	0	-0.045	0.082	23.476	0.018	0.018	0.000	0.000	0.000	0.000
38	A	20	ASP	0	0.079	-0.097	25.861	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	20	ASP	-1	-0.934	-0.822	29.264	-0.108	-0.108	0.000	0.000	0.000	0.000
40	A	21	PRO	0	0.001	-0.138	26.577	0.001	0.001	0.000	0.000	0.000	0.000
41	A	22	GLU	0	0.127	0.014	26.987	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	22	GLU	-1	-1.041	-0.845	29.875	-0.075	-0.075	0.000	0.000	0.000	0.000
43	A	23	GLN	0	0.005	-0.110	25.713	0.009	0.009	0.000	0.000	0.000	0.000
44	A	23	GLN	0	-0.078	0.083	24.859	0.009	0.009	0.000	0.000	0.000	0.000
45	A	24	HIS	0	0.130	-0.132	22.602	0.005	0.005	0.000	0.000	0.000	0.000
46	A	24	HIS	0	-0.092	0.123	22.785	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	25	ALA	0	0.066	-0.105	21.347	-0.027	-0.027	0.000	0.000	0.000	0.000
48	A	25	ALA	0	-0.068	0.106	23.869	0.003	0.003	0.000	0.000	0.000	0.000
49	A	26	THR	0	-0.007	-0.095	21.028	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	26	THR	0	-0.018	0.065	22.055	0.001	0.001	0.000	0.000	0.000	0.000
51	A	27	ILE	0	0.088	-0.064	19.553	0.037	0.037	0.000	0.000	0.000	0.000
52	A	27	ILE	0	-0.062	0.097	18.473	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	28	ARG	0	0.053	-0.096	16.927	-0.008	-0.008	0.000	0.000	0.000	0.000
54	A	28	ARG	1	0.825	1.018	17.719	0.240	0.240	0.000	0.000	0.000	0.000
55	A	29	GLN	0	0.106	-0.085	15.952	-0.027	-0.027	0.000	0.000	0.000	0.000
56	A	29	GLN	0	-0.122	0.070	17.494	-0.049	-0.049	0.000	0.000	0.000	0.000
57	A	30	ASN	0	0.127	-0.049	16.305	0.050	0.050	0.000	0.000	0.000	0.000
58	A	30	ASN	0	-0.131	0.052	16.068	0.045	0.045	0.000	0.000	0.000	0.000
59	A	31	LEU	0	0.122	-0.092	13.086	0.113	0.113	0.000	0.000	0.000	0.000
60	A	31	LEU	0	-0.106	0.097	10.419	-0.033	-0.033	0.000	0.000	0.000	0.000
61	A	32	TYR	0	0.047	-0.105	11.605	0.038	0.038	0.000	0.000	0.000	0.000
62	A	32	TYR	0	-0.156	0.040	12.125	-0.028	-0.028	0.000	0.000	0.000	0.000
63	A	33	GLU	0	0.038	-0.118	12.262	0.089	0.089	0.000	0.000	0.000	0.000
64	A	33	GLU	-1	-0.940	-0.832	15.533	0.200	0.200	0.000	0.000	0.000	0.000
65	A	34	GLN	0	0.057	-0.059	11.674	0.143	0.143	0.000	0.000	0.000	0.000
66	A	34	GLN	0	-0.090	0.060	11.114	-0.085	-0.085	0.000	0.000	0.000	0.000
67	A	35	LEU	0	-0.003	-0.119	7.862	0.350	0.350	0.000	0.000	0.000	0.000
68	A	35	LEU	0	-0.138	0.054	6.448	-0.109	-0.109	0.000	0.000	0.000	0.000
69	A	36	ASP	0	0.087	-0.094	7.853	0.329	0.329	0.000	0.000	0.000	0.000
70	A	36	ASP	-1	-1.001	-0.830	10.086	0.840	0.840	0.000	0.000	0.000	0.000
71	A	37	LEU	0	0.039	-0.131	8.844	0.309	0.309	0.000	0.000	0.000	0.000
72	A	37	LEU	0	-0.093	0.084	5.779	-0.124	-0.124	0.000	0.000	0.000	0.000
73	A	38	PRO	0	0.020	-0.075	8.773	-0.040	-0.040	0.000	0.000	0.000	0.000
74	A	39	PHE	0	0.211	0.045	11.896	-0.155	-0.155	0.000	0.000	0.000	0.000
75	A	39	PHE	0	-0.095	0.084	16.200	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	40	ASP	0	0.026	-0.109	13.842	-0.063	-0.063	0.000	0.000	0.000	0.000
77	A	40	ASP	-1	-0.904	-0.849	11.872	-0.407	-0.407	0.000	0.000	0.000	0.000
78	A	41	LYS	0	0.114	-0.093	9.297	-0.083	-0.083	0.000	0.000	0.000	0.000
79	A	41	LYS	1	0.758	1.021	6.699	1.946	1.946	0.000	0.000	0.000	0.000
80	A	42	GLN	0	0.046	-0.134	10.569	-0.247	-0.247	0.000	0.000	0.000	0.000
81	A	42	GLN	0	-0.051	0.113	12.284	0.037	0.037	0.000	0.000	0.000	0.000
82	A	43	LEU	0	0.089	-0.073	12.412	-0.054	-0.054	0.000	0.000	0.000	0.000
83	A	43	LEU	0	-0.091	0.112	15.308	0.014	0.014	0.000	0.000	0.000	0.000
84	A	44	ALA	0	0.093	-0.095	11.880	0.097	0.097	0.000	0.000	0.000	0.000
85	A	44	ALA	0	-0.049	0.110	10.968	-0.042	-0.042	0.000	0.000	0.000	0.000
86	A	45	LEU	0	0.098	-0.093	10.899	-0.061	-0.061	0.000	0.000	0.000	0.000
87	A	45	LEU	0	-0.091	0.107	9.175	-0.020	-0.020	0.000	0.000	0.000	0.000
88	A	46	TYR	0	0.085	-0.119	11.730	0.013	0.013	0.000	0.000	0.000	0.000
89	A	46	TYR	0	-0.072	0.079	16.056	0.025	0.025	0.000	0.000	0.000	0.000
90	A	47	ALA	0	0.026	-0.102	15.450	0.034	0.034	0.000	0.000	0.000	0.000
91	A	47	ALA	0	-0.076	0.110	16.310	0.008	0.008	0.000	0.000	0.000	0.000
92	A	48	GLY	0	-0.027	-0.106	14.471	0.050	0.050	0.000	0.000	0.000	0.000
93	A	49	ALA	0	0.099	-0.007	13.701	0.024	0.024	0.000	0.000	0.000	0.000
94	A	49	ALA	0	-0.075	0.112	13.053	-0.037	-0.037	0.000	0.000	0.000	0.000
95	A	50	LEU	0	0.034	-0.119	14.919	0.055	0.055	0.000	0.000	0.000	0.000
96	A	50	LEU	0	-0.054	0.112	13.416	0.016	0.016	0.000	0.000	0.000	0.000
97	A	51	GLY	0	0.030	-0.077	16.529	0.072	0.072	0.000	0.000	0.000	0.000
98	A	52	PRO	0	0.006	-0.016	17.728	0.058	0.058	0.000	0.000	0.000	0.000
99	A	53	ALA	0	0.095	-0.009	18.835	0.045	0.045	0.000	0.000	0.000	0.000
100	A	53	ALA	0	-0.033	0.129	18.122	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	54	SER	0	0.002	-0.071	20.097	0.029	0.029	0.000	0.000	0.000	0.000
102	A	54	SER	0	-0.052	0.040	20.161	0.016	0.016	0.000	0.000	0.000	0.000
103	A	55	SER	0	-0.065	-0.067	22.339	0.034	0.034	0.000	0.000	0.000	0.000
104	A	55	SER	0	-0.095	0.021	23.179	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	56	GLY	0	0.081	-0.058	23.848	0.019	0.019	0.000	0.000	0.000	0.000
106	A	57	LYS	0	0.031	-0.005	23.433	0.018	0.018	0.000	0.000	0.000	0.000
107	A	57	LYS	1	0.826	1.037	22.773	0.303	0.303	0.000	0.000	0.000	0.000
108	A	58	LEU	0	0.094	-0.062	20.406	-0.010	-0.010	0.000	0.000	0.000	0.000
109	A	58	LEU	0	-0.169	0.034	17.400	-0.008	-0.008	0.000	0.000	0.000	0.000
110	A	59	GLU	0	0.073	-0.136	21.548	0.005	0.005	0.000	0.000	0.000	0.000
111	A	59	GLU	-1	-0.904	-0.790	24.055	-0.264	-0.264	0.000	0.000	0.000	0.000
112	A	60	ASN	0	0.111	-0.054	22.393	0.028	0.028	0.000	0.000	0.000	0.000
113	A	60	ASN	0	-0.139	0.045	23.487	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	61	HIS	0	0.153	-0.047	20.779	-0.047	-0.047	0.000	0.000	0.000	0.000
115	A	61	HIS	0	-0.068	0.081	19.137	-0.009	-0.009	0.000	0.000	0.000	0.000
116	A	62	GLU	0	0.135	-0.093	19.523	-0.067	-0.067	0.000	0.000	0.000	0.000
117	A	62	GLU	-1	-0.984	-0.834	20.454	-0.530	-0.530	0.000	0.000	0.000	0.000
118	A	63	ALA	0	0.101	-0.087	19.292	-0.069	-0.069	0.000	0.000	0.000	0.000
119	A	63	ALA	0	-0.067	0.104	21.276	0.012	0.012	0.000	0.000	0.000	0.000
120	A	64	ILE	0	0.047	-0.124	17.532	-0.064	-0.064	0.000	0.000	0.000	0.000
121	A	64	ILE	0	-0.101	0.103	16.345	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	65	SER	0	0.088	-0.092	15.238	-0.129	-0.129	0.000	0.000	0.000	0.000
123	A	65	SER	0	-0.025	0.090	15.462	0.026	0.026	0.000	0.000	0.000	0.000
124	A	66	ASN	0	0.000	-0.119	14.359	-0.175	-0.175	0.000	0.000	0.000	0.000
125	A	66	ASN	0	-0.107	0.074	17.466	0.058	0.058	0.000	0.000	0.000	0.000
126	A	67	ALA	0	0.081	-0.062	14.478	-0.139	-0.139	0.000	0.000	0.000	0.000
127	A	67	ALA	0	-0.042	0.119	15.220	0.022	0.022	0.000	0.000	0.000	0.000
128	A	68	VAL	0	0.070	-0.101	11.290	-0.160	-0.160	0.000	0.000	0.000	0.000
129	A	68	VAL	0	-0.104	0.092	10.103	-0.011	-0.011	0.000	0.000	0.000	0.000
130	A	69	ASP	0	0.067	-0.111	9.786	-0.486	-0.486	0.000	0.000	0.000	0.000
131	A	69	ASP	-1	-0.935	-0.806	11.533	-1.421	-1.421	0.000	0.000	0.000	0.000
132	A	70	SER	0	0.060	-0.098	10.049	-0.382	-0.382	0.000	0.000	0.000	0.000
133	A	70	SER	0	-0.068	0.048	13.318	0.083	0.083	0.000	0.000	0.000	0.000
134	A	71	VAL	0	0.079	-0.088	9.894	-0.118	-0.118	0.000	0.000	0.000	0.000
135	A	71	VAL	0	-0.094	0.116	8.483	0.018	0.018	0.000	0.000	0.000	0.000
136	A	72	VAL	0	0.095	-0.102	5.897	-0.308	-0.308	0.000	0.000	0.000	0.000
137	A	72	VAL	0	-0.097	0.090	4.679	-0.204	-0.172	-0.001	-0.010	-0.021	0.000
138	A	73	GLN	0	0.158	-0.087	5.615	-1.481	-1.485	-0.002	0.001	0.005	0.000
139	A	73	GLN	0	-0.120	0.091	9.619	0.193	0.193	0.000	0.000	0.000	0.000
140	A	74	LEU	0	-0.004	-0.111	8.023	-0.096	-0.096	0.000	0.000	0.000	0.000
141	A	74	LEU	0	-0.075	0.090	9.651	0.095	0.095	0.000	0.000	0.000	0.000
142	A	75	LEU	0	0.021	-0.129	5.165	0.922	0.947	-0.002	-0.001	-0.023	0.000
143	A	75	LEU	0	-0.081	0.108	4.465	-0.266	-0.223	0.000	-0.012	-0.031	0.000
144	A	76	GLU	0	0.065	-0.107	4.702	-0.649	-0.545	-0.001	-0.013	-0.090	0.000
145	A	76	GLU	-1	-1.009	-0.860	4.104	-4.195	-4.055	0.002	-0.095	-0.048	0.000
146	A	77	ILE	0	-0.108	-0.118	5.240	1.261	1.291	-0.001	-0.003	-0.026	0.000
147	A	77	ILE	0	0.041	0.014	7.264	0.081	0.081	0.000	0.000	0.000	0.000

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