FMO DATABASE

FMODB ID: Y7512

Calculation Name: 1O22-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1O22

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WZX8

Base Structure: X-ray

Registration Date: 2025-10-11

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1345564.692306
FMO2-HF: Nuclear repulsion	1285237.632273
FMO2-HF: Total energy	-60327.060032
FMO2-MP2: Total energy	-60505.399023

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:6:ILE)

Summations of interaction energy for fragment #1(A:6: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.
-214.938	-207.712	22.473	-12.736	-16.963	-0.149

Interaction energy analysis for fragmet #1(A:6:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.736 / q_NPA : 0.861

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].
3	A	8	GLU	-1	-0.802	-0.893	2.766	-32.033	-29.488	0.558	-1.211	-1.892	-0.010
4	A	9	ILE	0	-0.012	-0.022	5.033	1.959	1.996	-0.001	-0.004	-0.032	0.000
43	A	48	PHE	0	0.000	0.001	2.443	-2.621	-2.000	0.725	-0.279	-1.067	-0.001
44	A	49	LEU	0	0.012	0.006	3.236	2.475	3.602	0.093	-0.382	-0.839	-0.002
45	A	50	LYS	1	0.844	0.915	2.463	19.384	21.279	2.085	-1.598	-2.382	-0.024
46	A	51	ILE	0	0.028	0.005	3.794	5.994	6.130	0.006	-0.010	-0.133	0.000
105	A	110	TRP	0	-0.028	-0.012	2.231	-4.184	-3.842	2.327	-0.613	-2.057	-0.005
106	A	111	TYR	0	0.078	0.032	4.668	2.781	2.821	-0.001	-0.002	-0.037	0.000
107	A	112	LYS	1	0.823	0.894	4.845	22.004	22.129	-0.001	-0.005	-0.118	0.000
148	A	153	GLU	-1	-0.891	-0.953	4.645	-44.633	-44.468	-0.001	-0.027	-0.136	0.000
149	A	154	ILE	-1	-0.862	-0.914	1.711	-115.666	-115.473	16.683	-8.605	-8.270	-0.107
5	A	10	LEU	0	0.013	0.020	8.165	0.991	0.991	0.000	0.000	0.000	0.000
6	A	11	TYR	0	-0.023	-0.032	11.458	0.331	0.331	0.000	0.000	0.000	0.000
7	A	12	TYR	0	0.012	-0.005	14.433	0.636	0.636	0.000	0.000	0.000	0.000
8	A	13	LYS	1	0.868	0.952	18.166	11.859	11.859	0.000	0.000	0.000	0.000
9	A	14	LYS	1	0.856	0.904	21.510	13.021	13.021	0.000	0.000	0.000	0.000
10	A	15	GLY	0	-0.016	-0.004	23.881	0.346	0.346	0.000	0.000	0.000	0.000
11	A	16	LYS	1	0.869	0.961	23.328	12.226	12.226	0.000	0.000	0.000	0.000
12	A	17	GLU	-1	-0.886	-0.941	23.892	-12.216	-12.216	0.000	0.000	0.000	0.000
13	A	18	PHE	0	0.001	-0.017	21.096	0.120	0.120	0.000	0.000	0.000	0.000
14	A	19	GLY	0	0.103	0.066	23.464	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	20	ILE	0	-0.050	-0.036	25.114	0.167	0.167	0.000	0.000	0.000	0.000
16	A	21	LEU	0	-0.020	-0.008	21.069	0.279	0.279	0.000	0.000	0.000	0.000
17	A	22	GLU	-1	-0.838	-0.936	20.358	-14.150	-14.150	0.000	0.000	0.000	0.000
18	A	23	LYS	1	0.893	0.959	22.874	10.058	10.058	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.977	0.981	26.255	9.943	9.943	0.000	0.000	0.000	0.000
20	A	25	MET	0	-0.006	0.017	18.388	0.267	0.267	0.000	0.000	0.000	0.000
21	A	26	LYS	1	0.901	0.957	22.312	13.123	13.123	0.000	0.000	0.000	0.000
22	A	27	GLU	-1	-0.922	-0.979	24.625	-9.887	-9.887	0.000	0.000	0.000	0.000
23	A	28	ILE	0	0.080	0.033	25.964	0.184	0.184	0.000	0.000	0.000	0.000
24	A	29	PHE	0	-0.035	0.011	21.726	0.078	0.078	0.000	0.000	0.000	0.000
25	A	30	ASN	0	-0.058	-0.048	25.016	-0.227	-0.227	0.000	0.000	0.000	0.000
26	A	31	GLU	-1	-0.985	-0.972	27.836	-9.130	-9.130	0.000	0.000	0.000	0.000
27	A	32	THR	0	-0.039	-0.046	27.224	0.109	0.109	0.000	0.000	0.000	0.000
28	A	33	GLY	0	-0.007	0.010	25.506	0.038	0.038	0.000	0.000	0.000	0.000
29	A	34	VAL	0	-0.043	-0.024	22.803	-0.602	-0.602	0.000	0.000	0.000	0.000
30	A	35	SER	0	-0.029	-0.012	17.807	0.235	0.235	0.000	0.000	0.000	0.000
31	A	36	LEU	0	-0.018	-0.015	19.994	-0.039	-0.039	0.000	0.000	0.000	0.000
32	A	37	GLU	-1	-0.837	-0.917	13.884	-19.731	-19.731	0.000	0.000	0.000	0.000
33	A	38	PRO	0	-0.023	-0.022	16.052	0.708	0.708	0.000	0.000	0.000	0.000
34	A	39	VAL	0	-0.003	0.007	16.034	-0.831	-0.831	0.000	0.000	0.000	0.000
35	A	40	ASN	0	-0.038	-0.025	11.231	0.309	0.309	0.000	0.000	0.000	0.000
36	A	41	SER	0	-0.001	0.006	15.759	0.869	0.869	0.000	0.000	0.000	0.000
37	A	42	GLU	-1	-0.805	-0.889	17.938	-12.300	-12.300	0.000	0.000	0.000	0.000
38	A	43	LEU	0	-0.023	-0.009	20.319	0.164	0.164	0.000	0.000	0.000	0.000
39	A	44	ILE	0	0.009	-0.001	16.459	-0.001	-0.001	0.000	0.000	0.000	0.000
40	A	45	GLY	0	0.030	0.015	14.307	0.601	0.601	0.000	0.000	0.000	0.000
41	A	46	ARG	1	0.841	0.931	8.170	25.523	25.523	0.000	0.000	0.000	0.000
42	A	47	ILE	0	-0.019	0.005	7.754	0.956	0.956	0.000	0.000	0.000	0.000
47	A	52	SER	0	-0.027	-0.004	6.550	-3.112	-3.112	0.000	0.000	0.000	0.000
48	A	53	VAL	0	-0.037	-0.013	9.300	1.370	1.370	0.000	0.000	0.000	0.000
49	A	54	LEU	0	0.002	0.018	12.653	-0.731	-0.731	0.000	0.000	0.000	0.000
50	A	55	GLU	-1	-0.893	-0.961	15.657	-16.183	-16.183	0.000	0.000	0.000	0.000
51	A	56	GLU	-1	-0.982	-1.012	18.406	-12.203	-12.203	0.000	0.000	0.000	0.000
52	A	57	GLY	0	-0.024	-0.011	21.854	0.271	0.271	0.000	0.000	0.000	0.000
53	A	58	GLU	-1	-0.830	-0.883	17.839	-16.420	-16.420	0.000	0.000	0.000	0.000
54	A	59	GLU	-1	-0.956	-0.977	21.231	-12.034	-12.034	0.000	0.000	0.000	0.000
55	A	60	VAL	0	-0.035	-0.025	17.660	-0.767	-0.767	0.000	0.000	0.000	0.000
56	A	61	PRO	0	0.035	0.031	14.320	0.686	0.686	0.000	0.000	0.000	0.000
57	A	62	SER	0	0.001	-0.018	17.448	-0.075	-0.075	0.000	0.000	0.000	0.000
58	A	63	PHE	0	0.004	-0.003	18.127	0.279	0.279	0.000	0.000	0.000	0.000
59	A	64	ALA	0	-0.017	0.005	13.781	-0.539	-0.539	0.000	0.000	0.000	0.000
60	A	65	ILE	0	0.010	-0.001	15.754	0.643	0.643	0.000	0.000	0.000	0.000
61	A	66	LYS	1	0.834	0.922	13.065	16.346	16.346	0.000	0.000	0.000	0.000
62	A	67	ALA	0	0.034	-0.002	16.946	0.800	0.800	0.000	0.000	0.000	0.000
63	A	68	LEU	0	-0.019	0.011	18.999	-0.467	-0.467	0.000	0.000	0.000	0.000
64	A	69	THR	0	0.032	0.003	21.278	0.730	0.730	0.000	0.000	0.000	0.000
65	A	70	PRO	0	0.001	0.001	23.533	-0.158	-0.158	0.000	0.000	0.000	0.000
66	A	71	LYS	1	0.788	0.881	25.175	11.928	11.928	0.000	0.000	0.000	0.000
67	A	72	GLU	-1	-0.921	-0.957	24.732	-10.579	-10.579	0.000	0.000	0.000	0.000
68	A	73	ASN	0	-0.058	-0.043	24.254	-0.304	-0.304	0.000	0.000	0.000	0.000
69	A	74	ALA	0	0.069	0.028	20.228	0.255	0.255	0.000	0.000	0.000	0.000
70	A	75	VAL	0	-0.021	-0.002	21.572	-0.441	-0.441	0.000	0.000	0.000	0.000
71	A	76	ASP	-1	-0.845	-0.905	23.731	-12.027	-12.027	0.000	0.000	0.000	0.000
72	A	77	LEU	0	-0.049	-0.023	19.434	0.083	0.083	0.000	0.000	0.000	0.000
73	A	78	PRO	0	0.009	0.025	18.892	-0.517	-0.517	0.000	0.000	0.000	0.000
74	A	79	LEU	0	-0.028	-0.027	11.487	-0.457	-0.457	0.000	0.000	0.000	0.000
75	A	80	GLY	0	-0.049	-0.031	13.662	-0.632	-0.632	0.000	0.000	0.000	0.000
76	A	81	ASP	-1	-0.849	-0.908	14.270	-15.028	-15.028	0.000	0.000	0.000	0.000
77	A	82	TRP	0	-0.094	-0.061	18.016	0.180	0.180	0.000	0.000	0.000	0.000
78	A	83	THR	0	-0.015	-0.022	20.443	0.582	0.582	0.000	0.000	0.000	0.000
79	A	84	ASP	-1	-0.827	-0.892	22.851	-10.884	-10.884	0.000	0.000	0.000	0.000
80	A	85	LEU	0	-0.024	-0.004	19.749	0.228	0.228	0.000	0.000	0.000	0.000
81	A	86	LYS	1	0.810	0.876	24.400	10.988	10.988	0.000	0.000	0.000	0.000
82	A	87	ASN	0	-0.052	-0.028	27.174	0.087	0.087	0.000	0.000	0.000	0.000
83	A	88	VAL	0	0.020	0.020	22.783	-0.056	-0.056	0.000	0.000	0.000	0.000
84	A	89	PHE	0	-0.006	0.005	23.401	0.358	0.358	0.000	0.000	0.000	0.000
85	A	90	VAL	0	-0.011	-0.013	21.363	-0.524	-0.524	0.000	0.000	0.000	0.000
86	A	91	GLU	-1	-0.948	-0.972	18.613	-13.473	-13.473	0.000	0.000	0.000	0.000
87	A	92	GLU	-1	-0.843	-0.914	16.702	-15.390	-15.390	0.000	0.000	0.000	0.000
88	A	93	ILE	0	-0.039	-0.028	18.796	-0.198	-0.198	0.000	0.000	0.000	0.000
89	A	94	ASP	-1	-0.890	-0.929	14.931	-16.012	-16.012	0.000	0.000	0.000	0.000
90	A	95	TYR	0	-0.030	-0.030	17.168	0.014	0.014	0.000	0.000	0.000	0.000
91	A	96	LEU	0	-0.063	-0.026	13.438	-0.647	-0.647	0.000	0.000	0.000	0.000
92	A	97	ASP	-1	-0.812	-0.869	15.228	-14.576	-14.576	0.000	0.000	0.000	0.000
93	A	98	SER	0	-0.031	-0.043	16.561	-0.471	-0.471	0.000	0.000	0.000	0.000
94	A	99	TYR	0	-0.080	-0.054	16.519	0.310	0.310	0.000	0.000	0.000	0.000
95	A	100	GLY	0	0.018	0.009	18.054	-0.437	-0.437	0.000	0.000	0.000	0.000
96	A	101	ASP	-1	-0.862	-0.914	19.066	-13.811	-13.811	0.000	0.000	0.000	0.000
97	A	102	MET	0	-0.071	-0.014	12.990	-0.957	-0.957	0.000	0.000	0.000	0.000
98	A	103	LYS	1	0.872	0.940	14.860	15.565	15.565	0.000	0.000	0.000	0.000
99	A	104	ILE	0	-0.021	-0.026	10.354	-1.849	-1.849	0.000	0.000	0.000	0.000
100	A	105	LEU	0	0.042	0.035	10.162	1.035	1.035	0.000	0.000	0.000	0.000
101	A	106	SER	0	0.010	0.000	9.274	-2.262	-2.262	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.782	-0.884	7.173	-24.494	-24.494	0.000	0.000	0.000	0.000
103	A	108	LYS	1	0.884	0.940	7.623	22.428	22.428	0.000	0.000	0.000	0.000
104	A	109	ASN	0	-0.006	-0.007	8.912	0.660	0.660	0.000	0.000	0.000	0.000
108	A	113	ILE	0	0.043	0.025	7.140	2.451	2.451	0.000	0.000	0.000	0.000
109	A	114	TYR	0	0.002	-0.016	9.363	-2.969	-2.969	0.000	0.000	0.000	0.000
110	A	115	VAL	0	0.025	0.018	12.223	1.157	1.157	0.000	0.000	0.000	0.000
111	A	116	PRO	0	0.099	0.060	14.893	-0.617	-0.617	0.000	0.000	0.000	0.000
112	A	117	TYR	0	0.071	0.018	17.071	-0.085	-0.085	0.000	0.000	0.000	0.000
113	A	118	SER	0	-0.020	-0.019	17.977	0.068	0.068	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.056	-0.060	19.017	0.461	0.461	0.000	0.000	0.000	0.000
115	A	120	VAL	0	-0.029	-0.024	14.457	-0.146	-0.146	0.000	0.000	0.000	0.000
116	A	121	LYS	1	0.907	0.976	16.912	13.004	13.004	0.000	0.000	0.000	0.000
117	A	122	LYS	1	0.889	0.943	19.124	12.626	12.626	0.000	0.000	0.000	0.000
118	A	123	LYS	1	0.958	1.012	16.057	16.378	16.378	0.000	0.000	0.000	0.000
119	A	124	ASN	0	-0.005	-0.010	14.454	-1.813	-1.813	0.000	0.000	0.000	0.000
120	A	125	ARG	1	0.918	0.943	7.504	33.818	33.818	0.000	0.000	0.000	0.000
121	A	126	ASN	0	0.016	0.002	11.315	-2.235	-2.235	0.000	0.000	0.000	0.000
122	A	127	GLU	-1	-0.844	-0.910	13.728	-16.276	-16.276	0.000	0.000	0.000	0.000
123	A	128	LEU	0	-0.002	-0.001	10.835	0.487	0.487	0.000	0.000	0.000	0.000
124	A	129	VAL	0	0.010	0.006	8.853	-0.264	-0.264	0.000	0.000	0.000	0.000
125	A	130	GLU	-1	-0.886	-0.956	11.394	-16.474	-16.474	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-0.905	-0.941	14.832	-14.578	-14.578	0.000	0.000	0.000	0.000
127	A	132	PHE	0	0.015	0.001	8.813	0.088	0.088	0.000	0.000	0.000	0.000
128	A	133	MET	0	-0.021	-0.002	11.801	-0.351	-0.351	0.000	0.000	0.000	0.000
129	A	134	LYS	1	0.823	0.919	13.908	16.349	16.349	0.000	0.000	0.000	0.000
130	A	135	TYR	0	-0.016	-0.025	12.212	-0.013	-0.013	0.000	0.000	0.000	0.000
131	A	136	PHE	0	-0.007	-0.001	11.782	0.376	0.376	0.000	0.000	0.000	0.000
132	A	137	PHE	0	0.010	0.001	14.153	0.446	0.446	0.000	0.000	0.000	0.000
133	A	138	GLU	-1	-0.832	-0.899	17.389	-13.001	-13.001	0.000	0.000	0.000	0.000
134	A	139	SER	0	-0.082	-0.054	15.398	0.435	0.435	0.000	0.000	0.000	0.000
135	A	140	LYS	1	0.868	0.938	13.572	16.926	16.926	0.000	0.000	0.000	0.000
136	A	141	GLY	0	-0.012	0.007	18.983	0.513	0.513	0.000	0.000	0.000	0.000
137	A	142	TRP	0	-0.045	-0.022	16.292	0.108	0.108	0.000	0.000	0.000	0.000
138	A	143	ASN	0	0.029	0.002	21.331	-0.488	-0.488	0.000	0.000	0.000	0.000
139	A	144	PRO	0	0.079	0.026	19.721	-0.136	-0.136	0.000	0.000	0.000	0.000
140	A	145	GLY	0	-0.002	0.012	21.087	-0.281	-0.281	0.000	0.000	0.000	0.000
141	A	146	GLU	-1	-0.906	-0.957	23.327	-10.988	-10.988	0.000	0.000	0.000	0.000
142	A	147	TYR	0	-0.058	-0.037	18.132	0.126	0.126	0.000	0.000	0.000	0.000
143	A	148	THR	0	-0.037	-0.018	18.478	0.195	0.195	0.000	0.000	0.000	0.000
144	A	149	PHE	0	0.017	0.000	12.496	-0.393	-0.393	0.000	0.000	0.000	0.000
145	A	150	SER	0	-0.009	0.003	13.037	0.478	0.478	0.000	0.000	0.000	0.000
146	A	151	VAL	0	-0.004	-0.014	7.756	-0.802	-0.802	0.000	0.000	0.000	0.000
147	A	152	GLN	0	-0.044	-0.022	7.766	3.887	3.887	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ILE)