FMO DATABASE

FMODB ID: GY161

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	OptAll
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	-296166.982488
FMO2-HF: Nuclear repulsion	270754.224282
FMO2-HF: Total energy	-25412.758206
FMO2-MP2: Total energy	-25483.113281

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.
-3.064	-0.494	2.631	-2.665	-2.539	-0.014

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 : 0.208 / 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	ASN	0	-0.114	0.022	4.128	-1.278	-0.897	0.002	-0.129	-0.255	0.000
5	A	3	ILE	0	0.154	-0.081	3.877	-2.258	-1.008	-0.009	-0.799	-0.443	0.003
6	A	3	ILE	0	-0.046	0.098	8.307	0.075	0.075	0.000	0.000	0.000	0.000
7	A	4	GLU	0	0.073	-0.107	7.113	-0.182	-0.182	0.000	0.000	0.000	0.000
8	A	4	GLU	-1	-0.901	-0.796	7.878	-0.259	-0.259	0.000	0.000	0.000	0.000
9	A	5	GLU	0	0.090	-0.113	4.747	0.447	0.500	-0.002	-0.008	-0.044	0.000
10	A	5	GLU	-1	-0.879	-0.801	2.397	0.392	1.176	2.641	-1.703	-1.722	-0.017
11	A	6	LEU	0	0.078	-0.089	5.651	0.062	0.062	0.000	0.000	0.000	0.000
12	A	6	LEU	0	-0.101	0.088	4.223	0.076	0.178	-0.001	-0.026	-0.075	0.000
13	A	7	LYS	0	0.084	-0.085	6.603	0.262	0.262	0.000	0.000	0.000	0.000
14	A	7	LYS	1	0.736	0.992	10.179	0.572	0.572	0.000	0.000	0.000	0.000
15	A	8	LYS	0	0.169	-0.043	9.705	0.053	0.053	0.000	0.000	0.000	0.000
16	A	8	LYS	1	0.778	1.024	9.601	0.340	0.340	0.000	0.000	0.000	0.000
17	A	9	GLN	0	0.085	-0.073	8.785	0.349	0.349	0.000	0.000	0.000	0.000
18	A	9	GLN	0	-0.145	0.055	7.300	-0.562	-0.562	0.000	0.000	0.000	0.000
19	A	10	ALA	0	0.164	-0.070	10.054	0.196	0.196	0.000	0.000	0.000	0.000
20	A	10	ALA	0	-0.084	0.098	11.169	-0.004	-0.004	0.000	0.000	0.000	0.000
21	A	11	GLU	0	0.019	-0.134	12.202	0.124	0.124	0.000	0.000	0.000	0.000
22	A	11	GLU	-1	-0.985	-0.865	13.697	-0.645	-0.645	0.000	0.000	0.000	0.000
23	A	12	THR	0	0.019	-0.098	13.596	0.123	0.123	0.000	0.000	0.000	0.000
24	A	12	THR	0	-0.051	0.060	13.357	0.038	0.038	0.000	0.000	0.000	0.000
25	A	13	GLU	0	0.072	-0.107	14.026	0.119	0.119	0.000	0.000	0.000	0.000
26	A	13	GLU	-1	-0.951	-0.819	11.691	-1.346	-1.346	0.000	0.000	0.000	0.000
27	A	14	ILE	0	0.082	-0.082	15.614	0.074	0.074	0.000	0.000	0.000	0.000
28	A	14	ILE	0	-0.109	0.078	16.228	0.014	0.014	0.000	0.000	0.000	0.000
29	A	15	ALA	0	0.068	-0.120	17.923	0.059	0.059	0.000	0.000	0.000	0.000
30	A	15	ALA	0	-0.080	0.114	18.607	0.006	0.006	0.000	0.000	0.000	0.000
31	A	16	ASP	0	0.109	-0.118	18.731	0.065	0.065	0.000	0.000	0.000	0.000
32	A	16	ASP	-1	-0.984	-0.825	18.071	-0.461	-0.461	0.000	0.000	0.000	0.000
33	A	17	PHE	0	0.107	-0.086	19.749	0.049	0.049	0.000	0.000	0.000	0.000
34	A	17	PHE	0	-0.092	0.086	20.013	0.004	0.004	0.000	0.000	0.000	0.000
35	A	18	ILE	0	0.050	-0.102	21.563	0.034	0.034	0.000	0.000	0.000	0.000
36	A	18	ILE	0	-0.083	0.093	22.101	0.006	0.006	0.000	0.000	0.000	0.000
37	A	19	ALA	0	0.093	-0.125	23.318	0.035	0.035	0.000	0.000	0.000	0.000
38	A	19	ALA	0	-0.068	0.130	23.487	0.001	0.001	0.000	0.000	0.000	0.000
39	A	20	GLN	0	0.075	-0.099	24.071	0.035	0.035	0.000	0.000	0.000	0.000
40	A	20	GLN	0	-0.109	0.078	23.869	-0.028	-0.028	0.000	0.000	0.000	0.000
41	A	21	LYS	0	-0.003	-0.130	25.725	0.025	0.025	0.000	0.000	0.000	0.000
42	A	21	LYS	1	0.733	0.983	25.241	0.308	0.308	0.000	0.000	0.000	0.000
43	A	22	ILE	0	0.093	-0.074	27.749	0.017	0.017	0.000	0.000	0.000	0.000
44	A	22	ILE	0	-0.081	0.097	27.414	0.002	0.002	0.000	0.000	0.000	0.000
45	A	23	ALA	0	0.133	-0.092	28.940	0.019	0.019	0.000	0.000	0.000	0.000
46	A	23	ALA	0	-0.068	0.112	28.966	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	24	GLU	0	0.080	-0.120	29.806	0.020	0.020	0.000	0.000	0.000	0.000
48	A	24	GLU	-1	-0.945	-0.791	28.560	-0.270	-0.270	0.000	0.000	0.000	0.000
49	A	25	MET	0	0.080	-0.108	31.382	0.012	0.012	0.000	0.000	0.000	0.000
50	A	25	MET	0	-0.068	0.108	32.362	0.003	0.003	0.000	0.000	0.000	0.000
51	A	26	ASN	0	0.070	-0.070	33.454	0.011	0.011	0.000	0.000	0.000	0.000
52	A	26	ASN	0	-0.039	0.107	34.055	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	27	LYS	0	0.146	-0.062	34.511	0.013	0.013	0.000	0.000	0.000	0.000
54	A	27	LYS	1	0.811	1.034	33.100	0.178	0.178	0.000	0.000	0.000	0.000
55	A	28	ASN	0	0.010	-0.109	35.563	0.010	0.010	0.000	0.000	0.000	0.000
56	A	28	ASN	0	-0.111	0.070	33.854	0.002	0.002	0.000	0.000	0.000	0.000
57	A	29	THR	0	-0.026	-0.100	37.255	0.005	0.005	0.000	0.000	0.000	0.000
58	A	29	THR	0	-0.057	0.052	37.377	0.003	0.003	0.000	0.000	0.000	0.000
59	A	30	GLY	0	0.019	-0.077	39.352	0.008	0.008	0.000	0.000	0.000	0.000
60	A	31	LYS	0	0.016	0.034	39.214	0.009	0.009	0.000	0.000	0.000	0.000
61	A	31	LYS	1	0.834	0.995	39.719	0.116	0.116	0.000	0.000	0.000	0.000
62	A	32	GLU	0	0.124	-0.122	36.460	-0.007	-0.007	0.000	0.000	0.000	0.000
63	A	32	GLU	-1	-1.002	-0.822	36.713	-0.121	-0.121	0.000	0.000	0.000	0.000
64	A	33	VAL	0	0.050	-0.134	33.243	0.010	0.010	0.000	0.000	0.000	0.000
65	A	33	VAL	0	-0.092	0.105	31.540	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	34	SER	0	0.025	-0.080	34.103	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	34	SER	0	-0.016	0.082	36.867	0.002	0.002	0.000	0.000	0.000	0.000
68	A	35	GLU	0	0.088	-0.096	32.609	0.002	0.002	0.000	0.000	0.000	0.000
69	A	35	GLU	-1	-0.896	-0.823	32.898	-0.152	-0.152	0.000	0.000	0.000	0.000
70	A	36	MET	0	-0.017	-0.132	29.822	0.004	0.004	0.000	0.000	0.000	0.000
71	A	36	MET	0	-0.036	0.115	28.459	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	37	ARG	0	0.119	-0.071	30.188	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	37	ARG	1	0.772	1.002	32.322	0.149	0.149	0.000	0.000	0.000	0.000
74	A	38	PHE	0	0.029	-0.112	26.939	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	38	PHE	0	-0.033	0.126	25.228	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	39	THR	0	0.043	-0.087	28.291	0.005	0.005	0.000	0.000	0.000	0.000
77	A	39	THR	0	-0.063	0.066	30.438	0.008	0.008	0.000	0.000	0.000	0.000
78	A	40	ALA	0	0.166	-0.071	26.173	-0.017	-0.017	0.000	0.000	0.000	0.000
79	A	40	ALA	0	-0.067	0.129	26.566	0.002	0.002	0.000	0.000	0.000	0.000
80	A	41	ARG	0	0.125	-0.072	26.164	0.028	0.028	0.000	0.000	0.000	0.000
81	A	41	ARG	1	0.648	0.952	26.146	0.289	0.289	0.000	0.000	0.000	0.000
82	A	42	GLU	0	0.129	-0.111	26.357	-0.029	-0.029	0.000	0.000	0.000	0.000
83	A	42	GLU	-1	-0.938	-0.828	25.349	-0.268	-0.268	0.000	0.000	0.000	0.000
84	A	43	LYS	0	0.008	-0.151	27.036	0.015	0.015	0.000	0.000	0.000	0.000
85	A	43	LYS	1	0.790	1.035	26.608	0.258	0.258	0.000	0.000	0.000	0.000
86	A	44	MET	0	0.111	-0.069	27.753	-0.005	-0.005	0.000	0.000	0.000	0.000
87	A	44	MET	0	-0.072	0.095	30.275	0.002	0.002	0.000	0.000	0.000	0.000
88	A	45	THR	0	-0.043	-0.115	25.360	0.016	0.016	0.000	0.000	0.000	0.000
89	A	45	THR	0	-0.020	0.082	24.337	0.006	0.006	0.000	0.000	0.000	0.000
90	A	46	GLY	0	0.028	-0.072	23.279	-0.025	-0.025	0.000	0.000	0.000	0.000
91	A	47	LEU	0	0.058	-0.025	22.600	0.007	0.007	0.000	0.000	0.000	0.000
92	A	47	LEU	0	-0.113	0.110	20.688	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	48	GLU	0	0.127	-0.079	21.585	-0.045	-0.045	0.000	0.000	0.000	0.000
94	A	48	GLU	-1	-0.946	-0.824	23.853	-0.297	-0.297	0.000	0.000	0.000	0.000
95	A	49	SER	0	0.013	-0.076	21.873	-0.045	-0.045	0.000	0.000	0.000	0.000
96	A	49	SER	0	-0.031	0.059	22.618	0.010	0.010	0.000	0.000	0.000	0.000
97	A	50	TYR	0	0.084	-0.092	23.204	0.023	0.023	0.000	0.000	0.000	0.000
98	A	50	TYR	0	-0.085	0.112	21.597	0.014	0.014	0.000	0.000	0.000	0.000
99	A	51	ASP	0	0.155	-0.066	25.028	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	51	ASP	-1	-0.945	-0.805	29.312	-0.238	-0.238	0.000	0.000	0.000	0.000
101	A	52	VAL	0	0.065	-0.129	28.210	0.017	0.017	0.000	0.000	0.000	0.000
102	A	52	VAL	0	-0.032	0.129	26.462	0.000	0.000	0.000	0.000	0.000	0.000
103	A	53	LYS	0	0.033	-0.114	29.127	0.004	0.004	0.000	0.000	0.000	0.000
104	A	53	LYS	1	0.704	0.992	31.948	0.212	0.212	0.000	0.000	0.000	0.000
105	A	54	ILE	0	0.137	-0.084	32.618	0.005	0.005	0.000	0.000	0.000	0.000
106	A	54	ILE	0	-0.057	0.102	30.512	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	55	LYS	0	0.000	-0.127	33.285	0.006	0.006	0.000	0.000	0.000	0.000
108	A	55	LYS	1	0.865	1.075	35.262	0.144	0.144	0.000	0.000	0.000	0.000
109	A	56	ILE	0	0.090	-0.075	35.585	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	56	ILE	0	-0.064	0.094	35.943	0.000	0.000	0.000	0.000	0.000	0.000
111	A	57	MET	0	0.050	-0.105	38.097	0.004	0.004	0.000	0.000	0.000	0.000
112	A	57	MET	0	-0.084	0.111	39.580	0.000	0.000	0.000	0.000	0.000	0.000
113	A	58	LEU	0	0.095	-0.124	41.013	-0.004	-0.004	0.000	0.000	0.000	0.000
114	A	58	LEU	0	-0.082	0.102	43.986	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	59	GLU	0	0.084	-0.118	44.347	0.000	0.000	0.000	0.000	0.000	0.000
116	A	59	GLU	-1	-0.993	-0.830	47.502	-0.076	-0.076	0.000	0.000	0.000	0.000
117	A	60	HIS	0	-0.083	-0.132	47.597	0.000	0.000	0.000	0.000	0.000	0.000
118	A	60	HIS	0	0.015	0.018	50.148	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)