FMO DATABASE

FMODB ID: 928R2

Calculation Name: 4ACV-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4ACV

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

Base Structure: X-ray

Registration Date: 2025-10-12

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	124
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1094035.750444
FMO2-HF: Nuclear repulsion	1042060.305378
FMO2-HF: Total energy	-51975.445066
FMO2-MP2: Total energy	-52121.023773

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:2:LYS)

Summations of interaction energy for fragment #1(A:2:LYS)

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.
-422.809	-415.157	1.411	-4.065	-4.998	-0.041

Interaction energy analysis for fragmet #1(A:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.789 / q_NPA : 1.886

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

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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	4	LEU	0	-0.053	-0.010	2.507	-23.812	-19.182	1.330	-2.860	-3.100	-0.033
4	A	5	SER	0	-0.010	-0.007	5.309	5.571	5.698	-0.001	-0.006	-0.120	0.000
46	A	47	GLU	-1	-0.795	-0.893	5.080	-91.601	-91.560	-0.001	-0.003	-0.037	0.000
53	A	54	TRP	0	-0.055	-0.024	4.585	-13.697	-13.656	-0.001	-0.009	-0.031	0.000
90	A	91	TYR	0	-0.048	-0.047	2.895	-9.218	-7.631	0.072	-0.699	-0.960	-0.004
122	A	123	ARG	1	0.606	0.766	3.461	87.241	88.417	0.013	-0.487	-0.702	-0.004
124	A	125	LEU	-1	-0.988	-0.980	5.004	-67.519	-67.469	-0.001	-0.001	-0.048	0.000
5	A	6	PHE	0	0.158	0.063	6.059	3.955	3.955	0.000	0.000	0.000	0.000
6	A	7	MET	0	0.001	0.011	9.351	2.716	2.716	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.895	0.945	8.283	55.631	55.631	0.000	0.000	0.000	0.000
8	A	9	VAL	0	0.039	0.022	9.811	2.450	2.450	0.000	0.000	0.000	0.000
9	A	10	LEU	0	-0.006	0.001	12.114	2.722	2.722	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.890	-0.961	13.264	-32.701	-32.701	0.000	0.000	0.000	0.000
11	A	12	ALA	0	-0.026	0.004	13.712	1.796	1.796	0.000	0.000	0.000	0.000
12	A	13	VAL	0	0.008	0.008	15.523	2.162	2.162	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.852	0.930	17.818	29.724	29.724	0.000	0.000	0.000	0.000
14	A	15	THR	0	-0.029	-0.028	17.351	1.662	1.662	0.000	0.000	0.000	0.000
15	A	16	MET	0	-0.051	-0.002	19.639	1.896	1.896	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.043	0.009	21.521	1.444	1.444	0.000	0.000	0.000	0.000
17	A	18	GLN	0	-0.005	0.000	22.335	1.108	1.108	0.000	0.000	0.000	0.000
18	A	19	GLU	-1	-1.022	-1.003	23.039	-26.207	-26.207	0.000	0.000	0.000	0.000
19	A	20	LYS	1	0.764	0.881	23.279	27.135	27.135	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.003	-0.007	26.697	0.737	0.737	0.000	0.000	0.000	0.000
21	A	22	GLY	0	-0.021	0.001	28.098	0.786	0.786	0.000	0.000	0.000	0.000
22	A	23	LEU	0	-0.054	-0.027	26.876	0.599	0.599	0.000	0.000	0.000	0.000
23	A	24	ASP	-1	-0.931	-0.967	25.897	-23.828	-23.828	0.000	0.000	0.000	0.000
24	A	25	VAL	0	0.022	0.013	22.406	0.342	0.342	0.000	0.000	0.000	0.000
25	A	26	SER	0	-0.018	0.001	22.308	-1.291	-1.291	0.000	0.000	0.000	0.000
26	A	27	ILE	0	0.017	-0.001	15.251	-0.143	-0.143	0.000	0.000	0.000	0.000
27	A	28	VAL	0	-0.055	-0.024	17.921	-1.365	-1.365	0.000	0.000	0.000	0.000
28	A	29	MET	0	0.055	0.046	20.019	1.088	1.088	0.000	0.000	0.000	0.000
29	A	30	ARG	1	0.843	0.889	22.235	20.217	20.217	0.000	0.000	0.000	0.000
30	A	31	ASN	0	0.002	0.001	25.538	0.614	0.614	0.000	0.000	0.000	0.000
31	A	32	GLN	0	0.062	0.050	28.211	-0.212	-0.212	0.000	0.000	0.000	0.000
32	A	33	VAL	0	0.031	0.028	29.510	-0.237	-0.237	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.942	-0.995	32.161	-16.360	-16.360	0.000	0.000	0.000	0.000
34	A	35	MET	0	-0.041	-0.017	33.882	0.681	0.681	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.002	-0.009	33.226	-0.493	-0.493	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.032	-0.006	28.201	-0.326	-0.326	0.000	0.000	0.000	0.000
37	A	38	THR	0	0.045	0.023	25.462	0.314	0.314	0.000	0.000	0.000	0.000
38	A	39	MET	0	-0.083	-0.033	23.393	-0.559	-0.559	0.000	0.000	0.000	0.000
39	A	40	ILE	0	0.001	0.008	18.104	0.191	0.191	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.851	-0.919	19.317	-27.034	-27.034	0.000	0.000	0.000	0.000
41	A	42	MET	0	-0.060	-0.027	12.960	-0.591	-0.591	0.000	0.000	0.000	0.000
42	A	43	ILE	0	-0.042	-0.007	16.480	0.742	0.742	0.000	0.000	0.000	0.000
43	A	44	ASP	-1	-0.882	-0.930	14.775	-34.541	-34.541	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.013	-0.030	6.980	1.820	1.820	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.899	-0.923	11.542	-45.155	-45.155	0.000	0.000	0.000	0.000
47	A	48	GLU	-1	-0.888	-0.965	9.863	-45.255	-45.255	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.873	-0.912	12.706	-29.942	-29.942	0.000	0.000	0.000	0.000
49	A	50	SER	0	-0.032	-0.035	12.121	0.734	0.734	0.000	0.000	0.000	0.000
50	A	51	GLN	0	-0.036	-0.004	12.176	-0.381	-0.381	0.000	0.000	0.000	0.000
51	A	52	THR	0	0.083	0.044	9.895	-3.330	-3.330	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.028	0.011	5.832	0.090	0.090	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.765	0.825	6.650	44.969	44.969	0.000	0.000	0.000	0.000
55	A	56	GLU	-1	-0.707	-0.825	6.309	-87.374	-87.374	0.000	0.000	0.000	0.000
56	A	57	LYS	1	0.773	0.885	10.144	36.918	36.918	0.000	0.000	0.000	0.000
57	A	58	TYR	0	-0.034	-0.051	7.638	-2.423	-2.423	0.000	0.000	0.000	0.000
58	A	59	ARG	1	0.825	0.899	13.990	35.489	35.489	0.000	0.000	0.000	0.000
59	A	60	PHE	0	0.019	-0.009	16.335	-1.265	-1.265	0.000	0.000	0.000	0.000
60	A	61	ALA	0	0.035	0.033	18.744	1.023	1.023	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.047	-0.023	21.277	-0.872	-0.872	0.000	0.000	0.000	0.000
62	A	63	HIS	0	-0.009	-0.014	23.626	1.880	1.880	0.000	0.000	0.000	0.000
63	A	64	HIS	0	-0.002	-0.014	26.557	-0.932	-0.932	0.000	0.000	0.000	0.000
64	A	65	TYR	0	-0.025	-0.029	28.694	0.382	0.382	0.000	0.000	0.000	0.000
65	A	66	THR	0	0.015	-0.018	32.496	-0.107	-0.107	0.000	0.000	0.000	0.000
66	A	67	ASN	0	-0.016	-0.019	35.934	0.001	0.001	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.944	-0.955	39.457	-14.536	-14.536	0.000	0.000	0.000	0.000
68	A	69	GLN	0	-0.011	-0.016	38.379	-0.571	-0.571	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.775	-0.862	34.519	-17.788	-17.788	0.000	0.000	0.000	0.000
70	A	71	LEU	0	0.006	0.001	35.000	-0.451	-0.451	0.000	0.000	0.000	0.000
71	A	72	ALA	0	0.013	0.008	35.026	-0.395	-0.395	0.000	0.000	0.000	0.000
72	A	73	GLY	0	0.047	0.015	32.890	-0.432	-0.432	0.000	0.000	0.000	0.000
73	A	74	VAL	0	-0.023	-0.013	30.416	-0.779	-0.779	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.900	-0.952	30.076	-18.872	-18.872	0.000	0.000	0.000	0.000
75	A	76	MET	0	-0.034	0.004	30.333	-0.285	-0.285	0.000	0.000	0.000	0.000
76	A	77	ILE	0	0.009	-0.005	25.470	-0.819	-0.819	0.000	0.000	0.000	0.000
77	A	78	ASP	-1	-0.803	-0.881	26.171	-23.785	-23.785	0.000	0.000	0.000	0.000
78	A	79	THR	0	0.004	-0.010	26.671	-0.695	-0.695	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.040	-0.024	25.639	-0.667	-0.667	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.030	0.013	21.360	-1.226	-1.226	0.000	0.000	0.000	0.000
81	A	82	GLN	0	-0.036	-0.030	22.403	-1.306	-1.306	0.000	0.000	0.000	0.000
82	A	83	MET	0	-0.102	-0.042	23.695	-0.148	-0.148	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.011	0.010	20.316	-0.366	-0.366	0.000	0.000	0.000	0.000
84	A	85	PHE	0	0.004	-0.018	14.705	1.044	1.044	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.002	0.007	15.975	-1.221	-1.221	0.000	0.000	0.000	0.000
86	A	87	LEU	0	0.015	0.004	10.913	-1.548	-1.548	0.000	0.000	0.000	0.000
87	A	88	PRO	0	-0.039	-0.033	9.057	1.850	1.850	0.000	0.000	0.000	0.000
88	A	89	GLU	-1	-0.770	-0.867	10.106	-45.794	-45.794	0.000	0.000	0.000	0.000
89	A	90	GLY	0	-0.024	-0.016	7.412	-4.369	-4.369	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.837	0.898	8.574	46.987	46.987	0.000	0.000	0.000	0.000
92	A	93	LEU	0	0.009	0.023	11.950	-1.803	-1.803	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.030	-0.019	13.679	1.915	1.915	0.000	0.000	0.000	0.000
94	A	95	ALA	0	-0.046	-0.032	16.199	2.245	2.245	0.000	0.000	0.000	0.000
95	A	96	VAL	0	0.022	0.016	17.901	-1.982	-1.982	0.000	0.000	0.000	0.000
96	A	97	ARG	1	0.818	0.903	18.377	31.450	31.450	0.000	0.000	0.000	0.000
97	A	98	HIS	0	-0.026	-0.020	22.642	-0.941	-0.941	0.000	0.000	0.000	0.000
98	A	99	CYS	-1	-0.889	-0.936	21.879	-27.667	-27.667	0.000	0.000	0.000	0.000
99	A	100	GLY	0	0.010	-0.009	24.000	0.073	0.073	0.000	0.000	0.000	0.000
100	A	101	LYS	0	-0.076	-0.029	25.512	0.912	0.912	0.000	0.000	0.000	0.000
101	A	102	GLN	0	0.028	0.015	26.140	-0.408	-0.408	0.000	0.000	0.000	0.000
102	A	103	ASN	0	-0.087	-0.049	29.856	0.656	0.656	0.000	0.000	0.000	0.000
103	A	104	LEU	0	0.036	0.019	31.996	-0.246	-0.246	0.000	0.000	0.000	0.000
104	A	105	VAL	0	-0.024	0.001	33.596	0.582	0.582	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.923	0.970	36.231	14.671	14.671	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.831	-0.902	32.456	-18.924	-18.924	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.024	-0.016	36.586	0.508	0.508	0.000	0.000	0.000	0.000
108	A	109	THR	0	-0.058	-0.040	38.695	0.351	0.351	0.000	0.000	0.000	0.000
109	A	110	LEU	0	-0.027	-0.005	34.494	0.262	0.262	0.000	0.000	0.000	0.000
110	A	111	ILE	0	-0.046	-0.023	36.022	0.153	0.153	0.000	0.000	0.000	0.000
111	A	112	HIS	0	-0.002	-0.009	28.499	0.303	0.303	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.009	0.001	31.355	0.304	0.304	0.000	0.000	0.000	0.000
113	A	114	LYS	0	0.007	0.003	25.083	-0.271	-0.271	0.000	0.000	0.000	0.000
114	A	115	THR	0	0.017	0.016	26.402	0.632	0.632	0.000	0.000	0.000	0.000
115	A	116	SER	0	-0.027	-0.017	23.341	-1.170	-1.170	0.000	0.000	0.000	0.000
116	A	117	PHE	0	0.028	0.009	20.737	0.777	0.777	0.000	0.000	0.000	0.000
117	A	118	GLU	-1	-0.756	-0.853	17.744	-33.177	-33.177	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.034	-0.020	14.627	0.852	0.852	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.005	-0.015	14.198	-0.895	-0.895	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.027	-0.015	9.122	1.712	1.712	0.000	0.000	0.000	0.000
121	A	122	CYS	-1	-0.754	-0.795	9.314	-45.733	-45.733	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.928	-0.963	6.078	-49.837	-49.837	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LYS)