FMO DATABASE

FMODB ID: M8R5Z

Calculation Name: 3V4H-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3V4H

Chain ID: A

ChEMBL ID:

UniProt ID: Q8CLE0

Base Structure: X-ray

Registration Date: 2025-10-04

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	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	140
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1268374.018756
FMO2-HF: Nuclear repulsion	1211999.125432
FMO2-HF: Total energy	-56374.893323
FMO2-MP2: Total energy	-56537.826949

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:4:ASP)

Summations of interaction energy for fragment #1(A:4:ASP)

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.
-123.694	-119.859	31.582	-17.741	-17.674	0.072

Interaction energy analysis for fragmet #1(A:4:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.025 / q_NPA : -0.008

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	6	PHE	0	-0.018	0.003	2.447	0.997	3.458	2.446	-1.738	-3.168	-0.011
15	A	18	ASP	-1	-0.725	-0.830	5.120	15.356	15.445	-0.001	-0.001	-0.086	0.000
72	A	87	ARG	1	0.761	0.836	1.923	-32.437	-30.770	7.993	-4.378	-5.282	0.049
73	A	88	LYS	1	0.831	0.910	1.792	-93.784	-94.318	21.145	-11.609	-9.002	0.034
74	A	89	ALA	0	0.010	0.008	4.351	-3.128	-2.976	-0.001	-0.015	-0.136	0.000
4	A	7	ILE	0	0.019	0.007	5.995	-0.365	-0.365	0.000	0.000	0.000	0.000
5	A	8	LYS	1	0.890	0.958	9.809	0.639	0.639	0.000	0.000	0.000	0.000
6	A	9	ILE	0	0.052	0.010	12.431	-0.217	-0.217	0.000	0.000	0.000	0.000
7	A	10	ASP	-1	-0.802	-0.895	15.897	-0.289	-0.289	0.000	0.000	0.000	0.000
8	A	11	GLY	0	-0.060	-0.035	19.159	-0.028	-0.028	0.000	0.000	0.000	0.000
9	A	12	ILE	0	-0.055	-0.028	16.622	0.064	0.064	0.000	0.000	0.000	0.000
10	A	13	GLU	-1	-0.833	-0.889	15.138	0.575	0.575	0.000	0.000	0.000	0.000
11	A	14	GLY	0	0.023	0.011	12.465	-0.132	-0.132	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.817	-0.920	11.805	0.875	0.875	0.000	0.000	0.000	0.000
13	A	16	SER	0	-0.051	-0.027	6.354	0.799	0.799	0.000	0.000	0.000	0.000
14	A	17	LEU	0	0.057	0.013	8.995	-0.030	-0.030	0.000	0.000	0.000	0.000
16	A	19	ALA	0	-0.065	-0.035	7.333	-1.943	-1.943	0.000	0.000	0.000	0.000
17	A	20	ASN	0	0.013	0.002	7.710	-1.028	-1.028	0.000	0.000	0.000	0.000
18	A	21	HIS	1	0.745	0.844	6.089	-2.518	-2.518	0.000	0.000	0.000	0.000
19	A	22	LYS	1	0.883	0.945	8.435	-4.927	-4.927	0.000	0.000	0.000	0.000
20	A	23	ASN	0	-0.041	-0.022	11.083	-0.236	-0.236	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.791	-0.858	8.641	-0.769	-0.769	0.000	0.000	0.000	0.000
22	A	25	ILE	0	0.017	-0.001	9.836	0.457	0.457	0.000	0.000	0.000	0.000
23	A	26	GLN	0	0.008	0.015	5.626	0.859	0.859	0.000	0.000	0.000	0.000
24	A	27	VAL	0	-0.033	-0.015	6.055	0.724	0.724	0.000	0.000	0.000	0.000
25	A	28	LEU	0	-0.025	-0.008	5.610	-2.099	-2.099	0.000	0.000	0.000	0.000
26	A	29	ALA	0	0.011	-0.002	7.909	-0.809	-0.809	0.000	0.000	0.000	0.000
27	A	30	TRP	0	0.010	-0.009	8.326	0.788	0.788	0.000	0.000	0.000	0.000
28	A	31	ASN	0	-0.047	-0.018	11.949	0.150	0.150	0.000	0.000	0.000	0.000
29	A	32	TRP	0	0.023	0.001	14.923	0.044	0.044	0.000	0.000	0.000	0.000
30	A	33	ASP	-1	-0.870	-0.890	17.466	-1.960	-1.960	0.000	0.000	0.000	0.000
31	A	34	VAL	0	0.002	-0.006	20.358	0.139	0.139	0.000	0.000	0.000	0.000
32	A	35	ALA	0	0.015	0.018	23.453	-0.019	-0.019	0.000	0.000	0.000	0.000
33	A	36	GLN	0	-0.065	-0.053	26.771	0.078	0.078	0.000	0.000	0.000	0.000
34	A	37	HIS	-1	-0.901	-0.932	30.285	-0.820	-0.820	0.000	0.000	0.000	0.000
35	A	50	LYS	2	1.632	1.791	30.463	1.636	1.636	0.000	0.000	0.000	0.000
36	A	51	ALA	0	0.109	0.061	27.380	0.027	0.027	0.000	0.000	0.000	0.000
37	A	52	SER	0	0.002	0.009	28.392	0.046	0.046	0.000	0.000	0.000	0.000
38	A	53	VAL	0	-0.031	-0.024	22.798	-0.077	-0.077	0.000	0.000	0.000	0.000
39	A	54	SER	0	-0.011	-0.027	21.286	0.057	0.057	0.000	0.000	0.000	0.000
40	A	55	ASP	-1	-0.771	-0.870	21.285	-1.298	-1.298	0.000	0.000	0.000	0.000
41	A	56	PHE	0	-0.039	-0.018	11.978	-0.168	-0.168	0.000	0.000	0.000	0.000
42	A	57	CYS	0	-0.015	0.004	16.487	0.292	0.292	0.000	0.000	0.000	0.000
43	A	58	PHE	0	-0.004	-0.026	11.377	-0.571	-0.571	0.000	0.000	0.000	0.000
44	A	59	ALA	0	0.043	0.033	11.789	0.514	0.514	0.000	0.000	0.000	0.000
45	A	60	HIS	1	0.729	0.840	10.435	0.439	0.439	0.000	0.000	0.000	0.000
46	A	61	TYR	0	0.048	0.016	10.039	0.104	0.104	0.000	0.000	0.000	0.000
47	A	62	ILE	0	-0.009	0.001	13.536	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	63	ASP	-1	-0.812	-0.902	12.718	-0.324	-0.324	0.000	0.000	0.000	0.000
49	A	64	LYS	1	0.838	0.899	15.776	-0.759	-0.759	0.000	0.000	0.000	0.000
50	A	65	ALA	0	0.003	0.014	15.109	-0.010	-0.010	0.000	0.000	0.000	0.000
51	A	66	SER	0	0.007	-0.026	16.948	-0.038	-0.038	0.000	0.000	0.000	0.000
52	A	67	PRO	0	0.004	0.011	18.789	-0.050	-0.050	0.000	0.000	0.000	0.000
53	A	68	ASN	0	0.002	0.009	20.105	0.007	0.007	0.000	0.000	0.000	0.000
54	A	69	LEU	0	0.010	-0.004	15.774	-0.041	-0.041	0.000	0.000	0.000	0.000
55	A	70	LEU	0	0.054	0.029	20.453	-0.035	-0.035	0.000	0.000	0.000	0.000
56	A	71	SER	0	-0.032	-0.032	23.522	0.021	0.021	0.000	0.000	0.000	0.000
57	A	72	TYR	0	-0.007	-0.031	22.803	0.061	0.061	0.000	0.000	0.000	0.000
58	A	73	CYS	0	-0.058	-0.003	23.649	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	74	LEU	0	0.005	-0.004	25.493	0.019	0.019	0.000	0.000	0.000	0.000
60	A	75	LEU	0	-0.056	-0.021	28.295	0.035	0.035	0.000	0.000	0.000	0.000
61	A	76	GLY	0	0.023	0.030	28.368	0.018	0.018	0.000	0.000	0.000	0.000
62	A	77	LYS	1	0.821	0.923	25.821	0.331	0.331	0.000	0.000	0.000	0.000
63	A	78	HIS	1	0.822	0.884	25.371	0.555	0.555	0.000	0.000	0.000	0.000
64	A	79	ILE	0	0.004	0.008	19.386	0.078	0.078	0.000	0.000	0.000	0.000
65	A	80	LYS	1	0.918	0.969	22.849	0.268	0.268	0.000	0.000	0.000	0.000
66	A	81	ASN	0	-0.021	-0.026	18.954	-0.092	-0.092	0.000	0.000	0.000	0.000
67	A	82	VAL	0	0.012	0.016	14.630	0.061	0.061	0.000	0.000	0.000	0.000
68	A	83	GLN	0	-0.012	-0.004	11.186	0.091	0.091	0.000	0.000	0.000	0.000
69	A	84	PHE	0	0.031	0.022	8.120	0.075	0.075	0.000	0.000	0.000	0.000
70	A	85	VAL	0	-0.013	-0.021	5.747	0.825	0.825	0.000	0.000	0.000	0.000
71	A	86	LEU	0	-0.011	0.014	4.913	-3.143	-3.143	0.000	0.000	0.000	0.000
75	A	90	GLY	0	0.016	0.008	6.571	0.771	0.771	0.000	0.000	0.000	0.000
76	A	91	GLY	0	0.029	0.026	8.676	0.879	0.879	0.000	0.000	0.000	0.000
77	A	92	ASP	-1	-0.864	-0.962	10.173	1.547	1.547	0.000	0.000	0.000	0.000
78	A	93	PRO	0	-0.078	-0.034	5.522	-0.137	-0.137	0.000	0.000	0.000	0.000
79	A	94	LEU	0	0.054	0.042	6.896	0.452	0.452	0.000	0.000	0.000	0.000
80	A	95	GLU	-1	-0.836	-0.929	5.790	-0.294	-0.294	0.000	0.000	0.000	0.000
81	A	96	TYR	0	0.008	0.010	5.057	1.549	1.549	0.000	0.000	0.000	0.000
82	A	97	LEU	0	0.026	0.017	8.400	0.615	0.615	0.000	0.000	0.000	0.000
83	A	98	THR	0	-0.046	-0.012	9.107	-0.751	-0.751	0.000	0.000	0.000	0.000
84	A	99	ILE	0	0.021	0.005	11.391	0.284	0.284	0.000	0.000	0.000	0.000
85	A	100	LYS	1	0.888	0.952	13.743	1.551	1.551	0.000	0.000	0.000	0.000
86	A	101	PHE	0	0.030	0.003	14.443	0.021	0.021	0.000	0.000	0.000	0.000
87	A	102	THR	0	-0.012	-0.018	19.092	0.110	0.110	0.000	0.000	0.000	0.000
88	A	103	ASP	-1	-0.879	-0.916	22.441	-0.679	-0.679	0.000	0.000	0.000	0.000
89	A	104	VAL	0	0.016	0.013	19.416	-0.043	-0.043	0.000	0.000	0.000	0.000
90	A	105	ILE	0	0.001	-0.011	22.664	0.129	0.129	0.000	0.000	0.000	0.000
91	A	106	ILE	0	-0.008	-0.003	19.851	-0.095	-0.095	0.000	0.000	0.000	0.000
92	A	107	THR	0	-0.027	-0.039	22.704	0.088	0.088	0.000	0.000	0.000	0.000
93	A	108	ARG	1	0.900	0.950	22.258	1.184	1.184	0.000	0.000	0.000	0.000
94	A	109	VAL	0	0.001	-0.006	19.997	-0.112	-0.112	0.000	0.000	0.000	0.000
95	A	110	ASP	-1	-0.868	-0.914	20.503	-0.983	-0.983	0.000	0.000	0.000	0.000
96	A	111	MET	0	-0.058	-0.047	19.690	-0.068	-0.068	0.000	0.000	0.000	0.000
97	A	112	ALA	0	-0.001	0.006	19.897	0.059	0.059	0.000	0.000	0.000	0.000
98	A	113	GLY	0	-0.005	-0.018	19.884	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	114	SER	0	-0.044	-0.023	21.073	0.026	0.026	0.000	0.000	0.000	0.000
100	A	115	LEU	0	-0.031	-0.032	22.169	0.051	0.051	0.000	0.000	0.000	0.000
101	A	116	GLU	-1	-0.909	-0.954	22.890	-0.275	-0.275	0.000	0.000	0.000	0.000
102	A	117	ASP	-1	-0.823	-0.890	17.100	-0.952	-0.952	0.000	0.000	0.000	0.000
103	A	118	GLU	-1	-0.846	-0.886	16.936	-0.819	-0.819	0.000	0.000	0.000	0.000
104	A	119	THR	0	-0.028	-0.018	14.285	0.082	0.082	0.000	0.000	0.000	0.000
105	A	120	ARG	1	0.762	0.878	13.190	-0.343	-0.343	0.000	0.000	0.000	0.000
106	A	121	PRO	0	0.058	0.021	16.596	-0.119	-0.119	0.000	0.000	0.000	0.000
107	A	122	ARG	1	0.786	0.871	14.103	1.209	1.209	0.000	0.000	0.000	0.000
108	A	123	GLU	-1	-0.747	-0.853	15.284	-0.731	-0.731	0.000	0.000	0.000	0.000
109	A	124	GLU	-1	-0.839	-0.897	15.073	-2.187	-2.187	0.000	0.000	0.000	0.000
110	A	125	ILE	0	-0.036	-0.016	15.538	0.262	0.262	0.000	0.000	0.000	0.000
111	A	126	ARG	1	0.841	0.897	17.005	1.364	1.364	0.000	0.000	0.000	0.000
112	A	127	PHE	0	-0.034	-0.024	15.398	0.165	0.165	0.000	0.000	0.000	0.000
113	A	128	SER	0	0.057	0.042	20.824	-0.088	-0.088	0.000	0.000	0.000	0.000
114	A	129	PHE	0	-0.039	-0.038	20.246	-0.013	-0.013	0.000	0.000	0.000	0.000
115	A	130	THR	0	0.006	0.017	23.421	0.015	0.015	0.000	0.000	0.000	0.000
116	A	131	LYS	1	0.923	0.970	24.131	0.736	0.736	0.000	0.000	0.000	0.000
117	A	132	MET	0	-0.025	0.009	18.507	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	133	THR	0	-0.015	-0.029	18.639	0.217	0.217	0.000	0.000	0.000	0.000
119	A	134	GLN	0	-0.030	0.001	14.628	0.020	0.020	0.000	0.000	0.000	0.000
120	A	135	ASP	-1	-0.834	-0.896	14.605	-1.318	-1.318	0.000	0.000	0.000	0.000
121	A	136	TYR	0	0.009	0.003	11.764	-0.344	-0.344	0.000	0.000	0.000	0.000
122	A	137	VAL	0	-0.036	-0.023	12.194	0.521	0.521	0.000	0.000	0.000	0.000
123	A	138	MET	0	-0.011	-0.003	13.105	-0.255	-0.255	0.000	0.000	0.000	0.000
124	A	139	GLN	0	0.036	-0.001	14.690	0.088	0.088	0.000	0.000	0.000	0.000
125	A	140	ASN	0	-0.056	-0.024	16.463	-0.120	-0.120	0.000	0.000	0.000	0.000
126	A	141	ALA	0	0.023	0.004	18.425	0.001	0.001	0.000	0.000	0.000	0.000
127	A	142	GLU	-1	-0.899	-0.942	14.230	0.257	0.257	0.000	0.000	0.000	0.000
128	A	143	GLY	0	0.077	0.067	15.492	-0.020	-0.020	0.000	0.000	0.000	0.000
129	A	144	HIS	0	-0.093	-0.058	16.830	-0.067	-0.067	0.000	0.000	0.000	0.000
130	A	145	LYS	1	0.875	0.924	15.414	0.516	0.516	0.000	0.000	0.000	0.000
131	A	146	SER	0	0.008	0.015	17.285	-0.074	-0.074	0.000	0.000	0.000	0.000
132	A	147	GLY	0	0.028	0.007	18.223	0.036	0.036	0.000	0.000	0.000	0.000
133	A	148	VAL	0	-0.042	-0.033	16.286	-0.033	-0.033	0.000	0.000	0.000	0.000
134	A	149	ILE	0	-0.017	0.013	17.404	0.163	0.163	0.000	0.000	0.000	0.000
135	A	150	SER	0	0.001	-0.030	17.727	-0.205	-0.205	0.000	0.000	0.000	0.000
136	A	151	ALA	0	-0.020	-0.001	19.700	0.122	0.122	0.000	0.000	0.000	0.000
137	A	152	ASN	0	-0.022	-0.009	20.531	-0.118	-0.118	0.000	0.000	0.000	0.000
138	A	153	TYR	0	0.011	-0.003	23.027	0.069	0.069	0.000	0.000	0.000	0.000
139	A	154	ASP	-1	-0.874	-0.953	24.788	-0.801	-0.801	0.000	0.000	0.000	0.000
140	A	155	VAL	-1	-0.861	-0.895	27.169	-0.740	-0.740	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASP)