FMO DATABASE

FMODB ID: 16R7Z

Calculation Name: 4XO1-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4XO1

Chain ID: A

ChEMBL ID:

UniProt ID: P0AC92

Base Structure: X-ray

Registration Date: 2025-07-10

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-295279.085174
FMO2-HF: Nuclear repulsion	269866.400615
FMO2-HF: Total energy	-25412.684559
FMO2-MP2: Total energy	-25483.07059

3D Structure Molmil

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:MET)

Summations of interaction energy for fragment #1(A:1: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.
-3.853	-0.628	1.212	-2.211	-2.226	-0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.189 / 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].
4	A	2	ASN	0	-0.123	0.026	4.139	-1.236	-0.868	0.002	-0.130	-0.240	0.000
5	A	3	ILE	0	0.166	-0.084	3.867	-2.485	-1.263	-0.008	-0.797	-0.417	0.004
6	A	3	ILE	0	-0.045	0.100	8.148	0.079	0.079	0.000	0.000	0.000	0.000
7	A	4	GLU	0	0.072	-0.104	7.144	-0.237	-0.237	0.000	0.000	0.000	0.000
8	A	4	GLU	-1	-0.930	-0.809	7.957	-0.331	-0.331	0.000	0.000	0.000	0.000
9	A	5	GLU	0	0.104	-0.135	4.920	0.320	0.365	-0.002	-0.004	-0.039	0.000
10	A	5	GLU	-1	-0.887	-0.810	2.586	-0.133	1.352	1.220	-1.256	-1.449	-0.013
11	A	6	LEU	0	0.073	-0.077	5.597	0.086	0.086	0.000	0.000	0.000	0.000
12	A	6	LEU	0	-0.096	0.096	4.112	0.084	0.189	0.000	-0.024	-0.081	0.000
13	A	7	LYS	0	0.087	-0.092	6.513	0.290	0.290	0.000	0.000	0.000	0.000
14	A	7	LYS	1	0.769	1.005	10.148	0.637	0.637	0.000	0.000	0.000	0.000
15	A	8	LYS	0	0.171	-0.046	9.638	0.101	0.101	0.000	0.000	0.000	0.000
16	A	8	LYS	1	0.782	1.025	9.755	0.382	0.382	0.000	0.000	0.000	0.000
17	A	9	GLN	0	0.068	-0.078	8.664	0.360	0.360	0.000	0.000	0.000	0.000
18	A	9	GLN	0	-0.128	0.068	7.240	-0.482	-0.482	0.000	0.000	0.000	0.000
19	A	10	ALA	0	0.161	-0.072	9.978	0.179	0.179	0.000	0.000	0.000	0.000
20	A	10	ALA	0	-0.089	0.093	11.047	-0.002	-0.002	0.000	0.000	0.000	0.000
21	A	11	GLU	0	0.012	-0.131	12.074	0.123	0.123	0.000	0.000	0.000	0.000
22	A	11	GLU	-1	-0.985	-0.862	13.913	-0.671	-0.671	0.000	0.000	0.000	0.000
23	A	12	THR	0	0.035	-0.102	13.559	0.122	0.122	0.000	0.000	0.000	0.000
24	A	12	THR	0	-0.054	0.063	13.397	0.035	0.035	0.000	0.000	0.000	0.000
25	A	13	GLU	0	0.071	-0.100	13.945	0.124	0.124	0.000	0.000	0.000	0.000
26	A	13	GLU	-1	-0.953	-0.820	11.325	-1.418	-1.418	0.000	0.000	0.000	0.000
27	A	14	ILE	0	0.089	-0.080	15.449	0.078	0.078	0.000	0.000	0.000	0.000
28	A	14	ILE	0	-0.112	0.079	16.202	0.015	0.015	0.000	0.000	0.000	0.000
29	A	15	ALA	0	0.060	-0.129	17.919	0.062	0.062	0.000	0.000	0.000	0.000
30	A	15	ALA	0	-0.071	0.117	18.681	0.006	0.006	0.000	0.000	0.000	0.000
31	A	16	ASP	0	0.107	-0.117	18.615	0.069	0.069	0.000	0.000	0.000	0.000
32	A	16	ASP	-1	-0.991	-0.825	18.038	-0.478	-0.478	0.000	0.000	0.000	0.000
33	A	17	PHE	0	0.087	-0.094	19.615	0.054	0.054	0.000	0.000	0.000	0.000
34	A	17	PHE	0	-0.109	0.078	19.803	0.004	0.004	0.000	0.000	0.000	0.000
35	A	18	ILE	0	0.051	-0.112	21.387	0.038	0.038	0.000	0.000	0.000	0.000
36	A	18	ILE	0	-0.082	0.095	22.111	0.006	0.006	0.000	0.000	0.000	0.000
37	A	19	ALA	0	0.089	-0.116	23.204	0.036	0.036	0.000	0.000	0.000	0.000
38	A	19	ALA	0	-0.062	0.131	23.507	0.001	0.001	0.000	0.000	0.000	0.000
39	A	20	GLN	0	0.080	-0.104	24.038	0.037	0.037	0.000	0.000	0.000	0.000
40	A	20	GLN	0	-0.098	0.078	24.051	-0.027	-0.027	0.000	0.000	0.000	0.000
41	A	21	LYS	0	-0.005	-0.128	25.636	0.026	0.026	0.000	0.000	0.000	0.000
42	A	21	LYS	1	0.759	1.002	25.318	0.303	0.303	0.000	0.000	0.000	0.000
43	A	22	ILE	0	0.080	-0.082	27.640	0.019	0.019	0.000	0.000	0.000	0.000
44	A	22	ILE	0	-0.066	0.099	27.521	0.001	0.001	0.000	0.000	0.000	0.000
45	A	23	ALA	0	0.119	-0.092	28.848	0.021	0.021	0.000	0.000	0.000	0.000
46	A	23	ALA	0	-0.068	0.109	28.988	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	24	GLU	0	0.091	-0.111	29.891	0.021	0.021	0.000	0.000	0.000	0.000
48	A	24	GLU	-1	-0.949	-0.795	28.838	-0.266	-0.266	0.000	0.000	0.000	0.000
49	A	25	MET	0	0.074	-0.112	31.587	0.014	0.014	0.000	0.000	0.000	0.000
50	A	25	MET	0	-0.073	0.109	32.345	0.003	0.003	0.000	0.000	0.000	0.000
51	A	26	ASN	0	0.070	-0.074	33.445	0.011	0.011	0.000	0.000	0.000	0.000
52	A	26	ASN	0	-0.045	0.106	33.970	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	27	LYS	0	0.146	-0.057	34.531	0.012	0.012	0.000	0.000	0.000	0.000
54	A	27	LYS	1	0.797	1.023	33.436	0.176	0.176	0.000	0.000	0.000	0.000
55	A	28	ASN	0	0.021	-0.111	35.752	0.010	0.010	0.000	0.000	0.000	0.000
56	A	28	ASN	0	-0.114	0.068	34.096	0.003	0.003	0.000	0.000	0.000	0.000
57	A	29	THR	0	0.008	-0.093	37.538	0.006	0.006	0.000	0.000	0.000	0.000
58	A	29	THR	0	-0.059	0.052	37.461	0.003	0.003	0.000	0.000	0.000	0.000
59	A	30	GLY	0	-0.006	-0.072	39.190	0.009	0.009	0.000	0.000	0.000	0.000
60	A	31	LYS	0	0.071	0.070	39.395	0.008	0.008	0.000	0.000	0.000	0.000
61	A	31	LYS	1	0.780	0.976	39.843	0.118	0.118	0.000	0.000	0.000	0.000
62	A	32	GLU	0	0.111	-0.141	36.790	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	32	GLU	-1	-1.000	-0.816	37.238	-0.123	-0.123	0.000	0.000	0.000	0.000
64	A	33	VAL	0	0.051	-0.140	33.456	0.009	0.009	0.000	0.000	0.000	0.000
65	A	33	VAL	0	-0.091	0.105	31.727	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	34	SER	0	0.045	-0.077	34.464	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	34	SER	0	-0.041	0.078	36.801	0.003	0.003	0.000	0.000	0.000	0.000
68	A	35	GLU	0	0.100	-0.112	32.449	0.000	0.000	0.000	0.000	0.000	0.000
69	A	35	GLU	-1	-0.913	-0.805	32.600	-0.160	-0.160	0.000	0.000	0.000	0.000
70	A	36	MET	0	0.000	-0.121	29.539	0.007	0.007	0.000	0.000	0.000	0.000
71	A	36	MET	0	-0.054	0.113	28.330	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	37	ARG	0	0.076	-0.102	29.889	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	37	ARG	1	0.755	0.988	32.363	0.158	0.158	0.000	0.000	0.000	0.000
74	A	38	PHE	0	0.089	-0.081	26.886	0.001	0.001	0.000	0.000	0.000	0.000
75	A	38	PHE	0	-0.054	0.120	25.030	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	39	THR	0	0.045	-0.095	28.267	0.006	0.006	0.000	0.000	0.000	0.000
77	A	39	THR	0	-0.062	0.060	30.673	0.009	0.009	0.000	0.000	0.000	0.000
78	A	40	ALA	0	0.108	-0.080	26.142	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	40	ALA	0	-0.049	0.128	26.281	0.002	0.002	0.000	0.000	0.000	0.000
80	A	41	ARG	0	0.133	-0.096	25.958	0.029	0.029	0.000	0.000	0.000	0.000
81	A	41	ARG	1	0.625	0.937	26.202	0.306	0.306	0.000	0.000	0.000	0.000
82	A	42	GLU	0	0.098	-0.138	25.756	-0.034	-0.034	0.000	0.000	0.000	0.000
83	A	42	GLU	-1	-0.959	-0.819	24.817	-0.287	-0.287	0.000	0.000	0.000	0.000
84	A	43	LYS	0	0.008	-0.132	26.296	0.025	0.025	0.000	0.000	0.000	0.000
85	A	43	LYS	1	0.843	1.071	26.351	0.257	0.257	0.000	0.000	0.000	0.000
86	A	44	MET	0	0.144	-0.070	27.182	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	44	MET	0	-0.074	0.098	29.883	0.002	0.002	0.000	0.000	0.000	0.000
88	A	45	THR	0	-0.036	-0.114	25.053	0.015	0.015	0.000	0.000	0.000	0.000
89	A	45	THR	0	-0.031	0.080	24.039	0.008	0.008	0.000	0.000	0.000	0.000
90	A	46	GLY	0	0.016	-0.077	22.818	-0.028	-0.028	0.000	0.000	0.000	0.000
91	A	47	LEU	0	0.119	0.001	22.219	0.017	0.017	0.000	0.000	0.000	0.000
92	A	47	LEU	0	-0.116	0.108	20.510	-0.003	-0.003	0.000	0.000	0.000	0.000
93	A	48	GLU	0	0.086	-0.091	21.245	-0.047	-0.047	0.000	0.000	0.000	0.000
94	A	48	GLU	-1	-0.985	-0.861	23.553	-0.315	-0.315	0.000	0.000	0.000	0.000
95	A	49	SER	0	0.008	-0.074	21.492	-0.049	-0.049	0.000	0.000	0.000	0.000
96	A	49	SER	0	-0.031	0.056	22.118	0.011	0.011	0.000	0.000	0.000	0.000
97	A	50	TYR	0	0.068	-0.093	23.008	0.022	0.022	0.000	0.000	0.000	0.000
98	A	50	TYR	0	-0.050	0.117	21.416	0.017	0.017	0.000	0.000	0.000	0.000
99	A	51	ASP	0	0.146	-0.055	25.165	-0.017	-0.017	0.000	0.000	0.000	0.000
100	A	51	ASP	-1	-0.967	-0.821	29.421	-0.261	-0.261	0.000	0.000	0.000	0.000
101	A	52	VAL	0	0.054	-0.128	28.373	0.007	0.007	0.000	0.000	0.000	0.000
102	A	52	VAL	0	-0.026	0.143	26.469	0.000	0.000	0.000	0.000	0.000	0.000
103	A	53	LYS	0	0.030	-0.122	29.409	0.005	0.005	0.000	0.000	0.000	0.000
104	A	53	LYS	1	0.772	1.037	32.100	0.216	0.216	0.000	0.000	0.000	0.000
105	A	54	ILE	0	0.135	-0.096	32.656	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	54	ILE	0	-0.052	0.113	30.765	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	55	LYS	0	-0.004	-0.124	33.460	0.007	0.007	0.000	0.000	0.000	0.000
108	A	55	LYS	1	0.884	1.071	35.321	0.147	0.147	0.000	0.000	0.000	0.000
109	A	56	ILE	0	0.125	-0.053	35.947	-0.005	-0.005	0.000	0.000	0.000	0.000
110	A	56	ILE	0	-0.074	0.097	36.075	0.000	0.000	0.000	0.000	0.000	0.000
111	A	57	MET	0	0.081	-0.121	38.245	0.004	0.004	0.000	0.000	0.000	0.000
112	A	57	MET	0	-0.077	0.122	39.619	0.000	0.000	0.000	0.000	0.000	0.000
113	A	58	LEU	0	0.040	-0.136	41.106	-0.003	-0.003	0.000	0.000	0.000	0.000
114	A	58	LEU	0	-0.065	0.099	43.563	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	59	GLU	0	0.085	-0.124	44.325	0.000	0.000	0.000	0.000	0.000	0.000
116	A	59	GLU	-1	-0.998	-0.816	47.307	-0.080	-0.080	0.000	0.000	0.000	0.000
117	A	60	HIS	0	-0.062	-0.128	47.577	0.001	0.001	0.000	0.000	0.000	0.000
118	A	60	HIS	0	0.006	0.019	50.025	0.001	0.001	0.000	0.000	0.000	0.000

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