FMO DATABASE

FMODB ID: 4Q4GN

Calculation Name: 2FHQ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FHQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q8A7U5

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	135
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1169893.845817
FMO2-HF: Nuclear repulsion	1116734.028646
FMO2-HF: Total energy	-53159.817171
FMO2-MP2: Total energy	-53313.626729

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:3:THR)

Summations of interaction energy for fragment #1(A:3:THR)

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.
-75.181	-73.11	0.031	-0.976	-1.126	-0.004

Interaction energy analysis for fragmet #1(A:3:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.858 / q_NPA : 0.915

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	5	THR	0	-0.003	-0.024	3.319	-0.069	2.002	0.031	-0.976	-1.126	-0.004
4	A	6	MET	0	0.039	0.008	5.844	1.105	1.105	0.000	0.000	0.000	0.000
5	A	7	LYS	1	0.927	0.980	8.673	22.858	22.858	0.000	0.000	0.000	0.000
6	A	8	GLU	-1	-0.785	-0.877	6.576	-44.577	-44.577	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.871	0.940	6.237	36.060	36.060	0.000	0.000	0.000	0.000
8	A	10	ALA	0	0.054	0.018	9.247	1.911	1.911	0.000	0.000	0.000	0.000
9	A	11	VAL	0	-0.022	0.005	12.245	1.598	1.598	0.000	0.000	0.000	0.000
10	A	12	GLU	-1	-0.826	-0.910	8.588	-32.555	-32.555	0.000	0.000	0.000	0.000
11	A	13	LEU	0	-0.027	-0.009	12.657	1.236	1.236	0.000	0.000	0.000	0.000
12	A	14	LEU	0	0.013	0.012	15.239	1.138	1.138	0.000	0.000	0.000	0.000
13	A	15	GLN	0	-0.047	-0.038	14.541	0.136	0.136	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.804	0.905	15.296	17.372	17.372	0.000	0.000	0.000	0.000
15	A	17	CYS	0	-0.041	-0.012	18.959	0.622	0.622	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.773	-0.874	21.408	-13.160	-13.160	0.000	0.000	0.000	0.000
17	A	19	VAL	0	-0.061	-0.016	24.756	0.490	0.490	0.000	0.000	0.000	0.000
18	A	20	VAL	0	0.001	0.008	22.818	-0.624	-0.624	0.000	0.000	0.000	0.000
19	A	21	THR	0	-0.053	-0.031	25.248	0.704	0.704	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.011	0.000	26.520	-0.352	-0.352	0.000	0.000	0.000	0.000
21	A	23	ALA	0	-0.033	-0.027	28.691	0.413	0.413	0.000	0.000	0.000	0.000
22	A	24	SER	0	0.012	-0.008	30.503	-0.252	-0.252	0.000	0.000	0.000	0.000
23	A	25	VAL	0	-0.026	-0.020	33.056	-0.029	-0.029	0.000	0.000	0.000	0.000
24	A	26	ASN	0	0.071	0.039	35.560	0.056	0.056	0.000	0.000	0.000	0.000
25	A	27	LYS	1	0.979	0.982	39.266	6.796	6.796	0.000	0.000	0.000	0.000
26	A	28	GLU	-1	-0.978	-0.991	41.928	-6.827	-6.827	0.000	0.000	0.000	0.000
27	A	29	GLY	0	-0.015	0.001	38.808	0.033	0.033	0.000	0.000	0.000	0.000
28	A	30	TYR	0	-0.025	-0.008	37.585	-0.257	-0.257	0.000	0.000	0.000	0.000
29	A	31	PRO	0	-0.003	0.002	32.791	-0.046	-0.046	0.000	0.000	0.000	0.000
30	A	32	ARG	1	0.921	0.956	34.304	8.301	8.301	0.000	0.000	0.000	0.000
31	A	33	PRO	0	-0.005	-0.002	30.501	-0.145	-0.145	0.000	0.000	0.000	0.000
32	A	34	VAL	0	0.007	0.000	31.416	0.336	0.336	0.000	0.000	0.000	0.000
33	A	35	PRO	0	-0.010	0.005	29.660	-0.319	-0.319	0.000	0.000	0.000	0.000
34	A	36	MET	0	0.005	-0.004	29.161	0.431	0.431	0.000	0.000	0.000	0.000
35	A	37	SER	0	0.024	0.006	28.311	-0.411	-0.411	0.000	0.000	0.000	0.000
36	A	38	LYS	1	0.768	0.877	21.262	14.322	14.322	0.000	0.000	0.000	0.000
37	A	39	ILE	0	0.000	0.001	26.379	-0.155	-0.155	0.000	0.000	0.000	0.000
38	A	40	ALA	0	0.031	0.018	25.027	-0.053	-0.053	0.000	0.000	0.000	0.000
39	A	41	ALA	0	-0.003	-0.010	20.855	0.061	0.061	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.845	-0.894	20.654	-13.504	-13.504	0.000	0.000	0.000	0.000
41	A	43	GLY	0	-0.024	-0.028	16.569	-0.496	-0.496	0.000	0.000	0.000	0.000
42	A	44	ILE	0	-0.023	-0.029	14.821	-0.082	-0.082	0.000	0.000	0.000	0.000
43	A	45	SER	0	-0.039	-0.017	17.966	0.019	0.019	0.000	0.000	0.000	0.000
44	A	46	THR	0	0.003	0.004	20.271	0.572	0.572	0.000	0.000	0.000	0.000
45	A	47	ILE	0	-0.052	-0.022	20.537	-0.582	-0.582	0.000	0.000	0.000	0.000
46	A	48	TRP	0	0.031	0.001	24.416	0.704	0.704	0.000	0.000	0.000	0.000
47	A	49	MET	0	-0.018	0.000	27.336	-0.218	-0.218	0.000	0.000	0.000	0.000
48	A	50	SER	0	0.017	0.020	30.389	0.095	0.095	0.000	0.000	0.000	0.000
49	A	51	THR	0	-0.034	-0.035	34.216	-0.035	-0.035	0.000	0.000	0.000	0.000
50	A	52	GLY	0	0.070	0.044	37.149	0.103	0.103	0.000	0.000	0.000	0.000
51	A	53	ALA	0	-0.013	-0.027	40.696	-0.077	-0.077	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.914	-0.959	42.629	-6.908	-6.908	0.000	0.000	0.000	0.000
53	A	55	SER	0	-0.035	0.000	39.127	-0.048	-0.048	0.000	0.000	0.000	0.000
54	A	56	LEU	0	0.034	-0.013	39.951	-0.065	-0.065	0.000	0.000	0.000	0.000
55	A	57	LYS	1	0.831	0.923	32.618	9.242	9.242	0.000	0.000	0.000	0.000
56	A	58	THR	0	0.016	0.018	37.046	-0.239	-0.239	0.000	0.000	0.000	0.000
57	A	59	ILE	0	0.000	0.002	39.006	0.001	0.001	0.000	0.000	0.000	0.000
58	A	60	ASP	-1	-0.826	-0.885	37.279	-8.228	-8.228	0.000	0.000	0.000	0.000
59	A	61	PHE	0	0.006	-0.013	31.520	-0.019	-0.019	0.000	0.000	0.000	0.000
60	A	62	LEU	0	-0.020	-0.002	36.826	-0.047	-0.047	0.000	0.000	0.000	0.000
61	A	63	SER	0	-0.107	-0.038	39.843	0.187	0.187	0.000	0.000	0.000	0.000
62	A	64	ASN	0	-0.010	-0.021	35.652	-0.133	-0.133	0.000	0.000	0.000	0.000
63	A	65	PRO	0	0.075	0.040	33.391	-0.129	-0.129	0.000	0.000	0.000	0.000
64	A	66	LYS	1	0.919	0.975	30.989	9.266	9.266	0.000	0.000	0.000	0.000
65	A	67	ALA	0	0.016	0.009	28.572	0.227	0.227	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.026	-0.009	26.012	-0.377	-0.377	0.000	0.000	0.000	0.000
67	A	69	LEU	0	0.003	0.006	22.408	0.360	0.360	0.000	0.000	0.000	0.000
68	A	70	CYS	0	-0.039	-0.015	21.746	-0.498	-0.498	0.000	0.000	0.000	0.000
69	A	71	PHE	0	0.054	0.018	16.388	0.431	0.431	0.000	0.000	0.000	0.000
70	A	72	GLN	0	0.019	-0.006	19.027	-0.692	-0.692	0.000	0.000	0.000	0.000
71	A	73	GLU	-1	-0.781	-0.889	17.975	-15.265	-15.265	0.000	0.000	0.000	0.000
72	A	74	LYS	1	0.894	0.941	16.808	16.268	16.268	0.000	0.000	0.000	0.000
73	A	75	GLY	0	0.019	0.013	18.030	-0.389	-0.389	0.000	0.000	0.000	0.000
74	A	76	ASP	-1	-0.821	-0.883	13.282	-21.958	-21.958	0.000	0.000	0.000	0.000
75	A	77	SER	0	-0.041	-0.045	15.828	0.759	0.759	0.000	0.000	0.000	0.000
76	A	78	VAL	0	-0.001	-0.005	14.834	-1.184	-1.184	0.000	0.000	0.000	0.000
77	A	79	ALA	0	-0.009	-0.003	17.490	0.866	0.866	0.000	0.000	0.000	0.000
78	A	80	LEU	0	-0.002	0.001	17.814	-0.504	-0.504	0.000	0.000	0.000	0.000
79	A	81	MET	0	-0.024	-0.022	21.252	0.687	0.687	0.000	0.000	0.000	0.000
80	A	82	GLY	0	0.004	0.002	23.540	-0.621	-0.621	0.000	0.000	0.000	0.000
81	A	83	GLU	-1	-0.860	-0.915	26.136	-10.466	-10.466	0.000	0.000	0.000	0.000
82	A	84	VAL	0	-0.037	-0.017	28.567	-0.379	-0.379	0.000	0.000	0.000	0.000
83	A	85	GLU	-1	-0.845	-0.898	30.331	-10.218	-10.218	0.000	0.000	0.000	0.000
84	A	86	VAL	0	0.012	-0.001	33.088	-0.125	-0.125	0.000	0.000	0.000	0.000
85	A	87	VAL	0	-0.043	-0.021	33.028	0.139	0.139	0.000	0.000	0.000	0.000
86	A	88	THR	0	0.018	-0.013	36.398	-0.036	-0.036	0.000	0.000	0.000	0.000
87	A	89	ASP	-1	-0.842	-0.921	36.438	-8.536	-8.536	0.000	0.000	0.000	0.000
88	A	90	GLU	-1	-0.881	-0.942	38.206	-7.487	-7.487	0.000	0.000	0.000	0.000
89	A	91	LYS	1	0.856	0.944	33.593	9.368	9.368	0.000	0.000	0.000	0.000
90	A	92	LEU	0	0.027	0.007	31.572	-0.147	-0.147	0.000	0.000	0.000	0.000
91	A	93	LYS	1	0.814	0.920	34.533	7.657	7.657	0.000	0.000	0.000	0.000
92	A	94	GLN	0	0.001	-0.003	36.986	-0.063	-0.063	0.000	0.000	0.000	0.000
93	A	95	GLU	-1	-0.918	-0.971	32.309	-9.780	-9.780	0.000	0.000	0.000	0.000
94	A	96	LEU	0	-0.021	-0.009	29.259	-0.319	-0.319	0.000	0.000	0.000	0.000
95	A	97	TRP	0	0.012	0.023	32.682	-0.016	-0.016	0.000	0.000	0.000	0.000
96	A	98	GLN	0	-0.025	-0.019	30.778	-0.321	-0.321	0.000	0.000	0.000	0.000
97	A	99	ASP	-1	-0.887	-0.936	34.807	-8.459	-8.459	0.000	0.000	0.000	0.000
98	A	100	TRP	0	-0.010	-0.015	31.946	0.274	0.274	0.000	0.000	0.000	0.000
99	A	101	PHE	0	0.018	-0.008	33.471	0.056	0.056	0.000	0.000	0.000	0.000
100	A	102	ILE	0	-0.021	-0.004	38.564	0.186	0.186	0.000	0.000	0.000	0.000
101	A	103	GLU	-1	-0.976	-0.983	40.720	-7.210	-7.210	0.000	0.000	0.000	0.000
102	A	104	HIS	0	-0.075	-0.028	38.623	0.123	0.123	0.000	0.000	0.000	0.000
103	A	105	PHE	0	-0.037	-0.020	37.730	0.077	0.077	0.000	0.000	0.000	0.000
104	A	106	PRO	0	0.057	0.020	43.285	-0.023	-0.023	0.000	0.000	0.000	0.000
105	A	107	GLY	0	-0.043	-0.019	46.364	0.102	0.102	0.000	0.000	0.000	0.000
106	A	108	GLY	0	-0.004	0.001	43.091	0.013	0.013	0.000	0.000	0.000	0.000
107	A	109	PRO	0	0.000	-0.018	39.560	-0.014	-0.014	0.000	0.000	0.000	0.000
108	A	110	THR	0	0.000	-0.016	41.258	-0.100	-0.100	0.000	0.000	0.000	0.000
109	A	111	ASP	-1	-0.821	-0.882	43.659	-6.968	-6.968	0.000	0.000	0.000	0.000
110	A	112	PRO	0	-0.008	-0.018	44.040	-0.178	-0.178	0.000	0.000	0.000	0.000
111	A	113	GLY	0	0.001	0.008	44.620	-0.041	-0.041	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.067	-0.027	36.138	-0.208	-0.208	0.000	0.000	0.000	0.000
113	A	115	VAL	0	-0.014	-0.005	37.281	0.046	0.046	0.000	0.000	0.000	0.000
114	A	116	LEU	0	0.009	0.011	32.803	-0.188	-0.188	0.000	0.000	0.000	0.000
115	A	117	LEU	0	-0.040	-0.022	31.953	0.169	0.169	0.000	0.000	0.000	0.000
116	A	118	LYS	1	0.878	0.936	28.047	10.747	10.747	0.000	0.000	0.000	0.000
117	A	119	PHE	0	-0.010	-0.007	22.893	0.137	0.137	0.000	0.000	0.000	0.000
118	A	120	THR	0	0.034	0.005	25.003	-0.578	-0.578	0.000	0.000	0.000	0.000
119	A	121	ALA	0	-0.013	-0.007	20.856	0.237	0.237	0.000	0.000	0.000	0.000
120	A	122	ASN	0	-0.014	-0.019	22.149	-0.535	-0.535	0.000	0.000	0.000	0.000
121	A	123	HIS	0	-0.048	-0.040	19.902	-0.646	-0.646	0.000	0.000	0.000	0.000
122	A	124	ALA	0	0.000	0.006	16.217	0.311	0.311	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.011	0.006	17.070	-0.318	-0.318	0.000	0.000	0.000	0.000
124	A	126	TYR	0	0.011	-0.014	12.811	-0.210	-0.210	0.000	0.000	0.000	0.000
125	A	127	TRP	0	-0.019	-0.001	14.888	0.459	0.459	0.000	0.000	0.000	0.000
126	A	128	ILE	0	0.028	0.005	9.891	-0.042	-0.042	0.000	0.000	0.000	0.000
127	A	129	GLU	-1	-0.937	-0.967	7.609	-34.859	-34.859	0.000	0.000	0.000	0.000
128	A	130	GLY	0	-0.013	0.001	11.583	0.203	0.203	0.000	0.000	0.000	0.000
129	A	131	THR	0	-0.036	-0.012	11.226	1.157	1.157	0.000	0.000	0.000	0.000
130	A	132	PHE	0	-0.007	-0.012	13.369	-0.518	-0.518	0.000	0.000	0.000	0.000
131	A	133	ILE	0	-0.050	-0.022	10.303	-0.431	-0.431	0.000	0.000	0.000	0.000
132	A	134	HIS	0	0.047	0.024	14.461	0.072	0.072	0.000	0.000	0.000	0.000
133	A	135	LYS	1	0.849	0.933	11.503	21.844	21.844	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.902	0.950	16.790	15.210	15.210	0.000	0.000	0.000	0.000
135	A	137	LEU	-1	-0.870	-0.922	16.072	-17.986	-17.986	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:THR)