FMO DATABASE

FMODB ID: G84V1

Calculation Name: 1HQZ-1-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1HQZ

Chain ID: 1

ChEMBL ID:

UniProt ID: P15891

Base Structure: X-ray

Registration Date: 2025-10-03

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	139
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1264913.135506
FMO2-HF: Nuclear repulsion	1211270.436266
FMO2-HF: Total energy	-53642.69924
FMO2-MP2: Total energy	-53801.396608

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:LEU)

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

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.
-64.236	-57.773	3.998	-3.152	-7.309	-0.029

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.816 / q_NPA : 0.905

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	PRO	0	-0.002	-0.005	2.490	0.847	3.512	0.718	-0.986	-2.396	-0.005
4	A	6	ILE	0	-0.014	0.017	3.685	2.774	2.904	0.018	0.022	-0.171	0.000
93	A	95	THR	0	0.035	0.028	4.895	-6.051	-5.965	-0.001	-0.005	-0.079	0.000
96	A	98	SER	0	-0.028	-0.033	2.406	-16.732	-13.834	2.071	-1.884	-3.085	-0.021
97	A	99	PHE	0	0.045	0.042	3.285	-0.211	0.045	0.007	0.145	-0.407	-0.002
99	A	101	ALA	0	-0.021	-0.012	2.560	1.168	1.324	1.184	-0.374	-0.968	-0.001
100	A	102	ASN	0	0.011	-0.013	4.047	0.153	0.425	0.001	-0.070	-0.203	0.000
5	A	7	ASP	-1	-0.776	-0.837	6.935	-20.562	-20.562	0.000	0.000	0.000	0.000
6	A	8	TYR	0	0.079	0.023	9.717	0.420	0.420	0.000	0.000	0.000	0.000
7	A	9	THR	0	-0.067	-0.043	12.610	1.250	1.250	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.063	-0.053	14.546	1.413	1.413	0.000	0.000	0.000	0.000
9	A	11	HIS	1	0.797	0.884	16.368	16.463	16.463	0.000	0.000	0.000	0.000
10	A	12	SER	0	0.015	0.013	17.924	0.564	0.564	0.000	0.000	0.000	0.000
11	A	13	ARG	1	0.913	0.957	18.991	13.196	13.196	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.816	-0.908	21.208	-13.205	-13.205	0.000	0.000	0.000	0.000
13	A	15	ILE	0	-0.001	0.003	16.026	0.220	0.220	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.891	-0.959	19.510	-14.066	-14.066	0.000	0.000	0.000	0.000
15	A	17	ALA	0	-0.050	-0.021	21.809	0.456	0.456	0.000	0.000	0.000	0.000
16	A	18	GLU	-1	-0.786	-0.879	23.104	-10.479	-10.479	0.000	0.000	0.000	0.000
17	A	19	TYR	0	-0.008	-0.016	20.836	0.255	0.255	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.054	-0.033	22.981	0.402	0.402	0.000	0.000	0.000	0.000
19	A	21	LYS	1	0.778	0.885	26.003	10.551	10.551	0.000	0.000	0.000	0.000
20	A	22	ILE	0	0.021	0.025	24.017	0.264	0.264	0.000	0.000	0.000	0.000
21	A	23	VAL	0	-0.009	-0.019	23.423	0.314	0.314	0.000	0.000	0.000	0.000
22	A	24	ARG	1	0.868	0.931	26.605	10.274	10.274	0.000	0.000	0.000	0.000
23	A	25	GLY	0	0.038	0.033	29.755	0.286	0.286	0.000	0.000	0.000	0.000
24	A	26	SER	0	-0.100	-0.054	31.351	0.193	0.193	0.000	0.000	0.000	0.000
25	A	27	ASP	-1	-0.835	-0.924	31.578	-8.930	-8.930	0.000	0.000	0.000	0.000
26	A	28	PRO	0	-0.029	-0.002	32.483	-0.194	-0.194	0.000	0.000	0.000	0.000
27	A	29	ASP	-1	-0.906	-0.960	33.720	-8.348	-8.348	0.000	0.000	0.000	0.000
28	A	30	THR	0	-0.111	-0.066	27.498	-0.283	-0.283	0.000	0.000	0.000	0.000
29	A	31	THR	0	-0.005	-0.013	29.171	-0.212	-0.212	0.000	0.000	0.000	0.000
30	A	32	TRP	0	-0.020	-0.010	24.234	-0.469	-0.469	0.000	0.000	0.000	0.000
31	A	33	LEU	0	0.006	-0.009	19.951	0.173	0.173	0.000	0.000	0.000	0.000
32	A	34	ILE	0	0.016	0.026	18.624	-0.424	-0.424	0.000	0.000	0.000	0.000
33	A	35	ILE	0	-0.054	-0.019	14.051	0.093	0.093	0.000	0.000	0.000	0.000
34	A	36	SER	0	0.019	-0.028	15.314	-1.110	-1.110	0.000	0.000	0.000	0.000
35	A	37	PRO	0	-0.043	-0.002	11.966	0.065	0.065	0.000	0.000	0.000	0.000
36	A	38	ASN	0	0.051	0.017	14.036	-0.067	-0.067	0.000	0.000	0.000	0.000
37	A	39	ALA	0	-0.021	-0.027	15.585	-0.961	-0.961	0.000	0.000	0.000	0.000
38	A	40	LYS	1	0.868	0.936	15.584	15.392	15.392	0.000	0.000	0.000	0.000
39	A	41	LYS	1	0.815	0.891	9.139	28.200	28.200	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.821	-0.878	11.165	-18.665	-18.665	0.000	0.000	0.000	0.000
41	A	43	TYR	0	-0.073	-0.066	9.596	-0.278	-0.278	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.891	-0.960	13.975	-14.571	-14.571	0.000	0.000	0.000	0.000
43	A	45	PRO	0	-0.002	-0.020	17.731	-0.307	-0.307	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.820	-0.858	19.725	-14.554	-14.554	0.000	0.000	0.000	0.000
45	A	47	SER	0	0.007	-0.003	21.555	0.612	0.612	0.000	0.000	0.000	0.000
46	A	48	THR	0	-0.015	-0.018	23.436	-0.418	-0.418	0.000	0.000	0.000	0.000
47	A	49	GLY	0	0.029	0.027	26.139	0.244	0.244	0.000	0.000	0.000	0.000
48	A	50	SER	0	0.041	0.040	29.232	-0.170	-0.170	0.000	0.000	0.000	0.000
49	A	51	SER	0	-0.041	-0.018	31.842	0.059	0.059	0.000	0.000	0.000	0.000
50	A	52	PHE	0	0.057	0.012	25.352	-0.311	-0.311	0.000	0.000	0.000	0.000
51	A	53	HIS	1	0.852	0.907	28.308	9.035	9.035	0.000	0.000	0.000	0.000
52	A	54	ASP	-1	-0.858	-0.935	29.437	-9.436	-9.436	0.000	0.000	0.000	0.000
53	A	55	PHE	0	-0.024	-0.003	21.097	-0.389	-0.389	0.000	0.000	0.000	0.000
54	A	56	LEU	0	-0.005	-0.009	24.040	-0.508	-0.508	0.000	0.000	0.000	0.000
55	A	57	GLN	0	-0.022	-0.005	25.103	0.147	0.147	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.056	-0.018	24.698	0.048	0.048	0.000	0.000	0.000	0.000
57	A	59	PHE	0	0.007	0.011	18.301	-0.510	-0.510	0.000	0.000	0.000	0.000
58	A	60	ASP	-1	-0.771	-0.851	19.028	-14.327	-14.327	0.000	0.000	0.000	0.000
59	A	61	GLU	-1	-0.887	-0.941	18.463	-13.877	-13.877	0.000	0.000	0.000	0.000
60	A	62	THR	0	-0.084	-0.073	17.704	-0.724	-0.724	0.000	0.000	0.000	0.000
61	A	63	LYS	1	0.768	0.859	14.576	14.010	14.010	0.000	0.000	0.000	0.000
62	A	64	VAL	0	-0.023	-0.005	9.242	0.051	0.051	0.000	0.000	0.000	0.000
63	A	65	GLN	0	-0.012	-0.009	12.570	-0.152	-0.152	0.000	0.000	0.000	0.000
64	A	66	TYR	0	-0.011	-0.012	8.708	-1.003	-1.003	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.047	0.034	15.154	0.502	0.502	0.000	0.000	0.000	0.000
66	A	68	LEU	0	-0.053	-0.026	18.369	-0.415	-0.415	0.000	0.000	0.000	0.000
67	A	69	ALA	0	0.043	0.018	20.861	0.351	0.351	0.000	0.000	0.000	0.000
68	A	70	ARG	1	0.865	0.957	24.512	9.303	9.303	0.000	0.000	0.000	0.000
69	A	71	VAL	0	-0.004	-0.008	27.005	0.194	0.194	0.000	0.000	0.000	0.000
70	A	72	SER	0	0.033	0.021	29.762	0.028	0.028	0.000	0.000	0.000	0.000
71	A	73	PRO	0	-0.018	0.001	31.621	0.039	0.039	0.000	0.000	0.000	0.000
72	A	74	PRO	0	0.010	-0.019	33.421	0.233	0.233	0.000	0.000	0.000	0.000
73	A	75	GLY	0	-0.008	-0.003	36.983	0.002	0.002	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.097	-0.045	36.219	0.092	0.092	0.000	0.000	0.000	0.000
75	A	77	ASP	-1	-0.856	-0.918	37.206	-7.465	-7.465	0.000	0.000	0.000	0.000
76	A	78	VAL	0	-0.081	-0.032	32.781	-0.103	-0.103	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.876	-0.952	31.581	-9.165	-9.165	0.000	0.000	0.000	0.000
78	A	80	LYS	1	0.752	0.878	27.449	9.512	9.512	0.000	0.000	0.000	0.000
79	A	81	ILE	0	0.001	-0.001	22.288	0.006	0.006	0.000	0.000	0.000	0.000
80	A	82	ILE	0	-0.009	-0.002	21.503	-0.145	-0.145	0.000	0.000	0.000	0.000
81	A	83	ILE	0	-0.037	-0.016	15.561	-0.200	-0.200	0.000	0.000	0.000	0.000
82	A	84	ILE	0	0.020	0.004	17.367	-0.011	-0.011	0.000	0.000	0.000	0.000
83	A	85	GLY	0	-0.011	-0.009	13.065	-0.445	-0.445	0.000	0.000	0.000	0.000
84	A	86	TRP	0	-0.011	-0.006	13.877	-0.029	-0.029	0.000	0.000	0.000	0.000
85	A	87	CYS	0	-0.058	-0.050	10.089	-2.084	-2.084	0.000	0.000	0.000	0.000
86	A	88	PRO	0	0.079	0.073	13.067	-0.068	-0.068	0.000	0.000	0.000	0.000
87	A	89	ASP	-1	-0.827	-0.902	14.816	-17.340	-17.340	0.000	0.000	0.000	0.000
88	A	90	SER	0	-0.043	-0.025	15.414	-0.740	-0.740	0.000	0.000	0.000	0.000
89	A	91	ALA	0	0.025	0.046	12.601	-0.243	-0.243	0.000	0.000	0.000	0.000
90	A	92	PRO	0	-0.002	0.000	11.207	-0.927	-0.927	0.000	0.000	0.000	0.000
91	A	93	LEU	0	0.023	0.008	8.836	-2.235	-2.235	0.000	0.000	0.000	0.000
92	A	94	LYS	1	0.931	0.964	5.504	33.717	33.717	0.000	0.000	0.000	0.000
94	A	96	ARG	1	0.956	0.972	6.630	19.830	19.830	0.000	0.000	0.000	0.000
95	A	97	ALA	0	-0.060	-0.031	5.136	-0.033	-0.033	0.000	0.000	0.000	0.000
98	A	100	ALA	0	0.025	0.016	5.835	1.358	1.358	0.000	0.000	0.000	0.000
101	A	103	PHE	0	0.052	0.033	6.229	2.456	2.456	0.000	0.000	0.000	0.000
102	A	104	ALA	0	0.014	0.013	7.551	1.846	1.846	0.000	0.000	0.000	0.000
103	A	105	ALA	0	-0.042	-0.020	7.139	1.583	1.583	0.000	0.000	0.000	0.000
104	A	106	VAL	0	0.010	0.002	9.199	1.666	1.666	0.000	0.000	0.000	0.000
105	A	107	ALA	0	0.031	0.020	12.061	1.305	1.305	0.000	0.000	0.000	0.000
106	A	108	ASN	0	-0.016	-0.011	10.842	2.082	2.082	0.000	0.000	0.000	0.000
107	A	109	ASN	0	-0.085	-0.051	10.325	1.823	1.823	0.000	0.000	0.000	0.000
108	A	110	LEU	0	-0.014	0.010	13.773	0.606	0.606	0.000	0.000	0.000	0.000
109	A	111	PHE	0	0.007	0.003	15.723	0.868	0.868	0.000	0.000	0.000	0.000
110	A	112	LYS	1	0.866	0.929	17.051	15.447	15.447	0.000	0.000	0.000	0.000
111	A	113	GLY	0	0.023	0.020	19.245	0.468	0.468	0.000	0.000	0.000	0.000
112	A	114	TYR	0	-0.006	-0.009	16.226	0.090	0.090	0.000	0.000	0.000	0.000
113	A	115	HIS	0	0.057	0.053	21.836	-0.249	-0.249	0.000	0.000	0.000	0.000
114	A	116	VAL	0	-0.004	-0.004	21.605	0.073	0.073	0.000	0.000	0.000	0.000
115	A	117	GLN	0	-0.023	-0.012	13.195	0.173	0.173	0.000	0.000	0.000	0.000
116	A	118	VAL	0	-0.010	-0.001	17.695	0.247	0.247	0.000	0.000	0.000	0.000
117	A	119	THR	0	-0.050	-0.030	13.162	-1.293	-1.293	0.000	0.000	0.000	0.000
118	A	120	ALA	0	0.006	0.010	15.397	0.695	0.695	0.000	0.000	0.000	0.000
119	A	121	ARG	1	0.671	0.809	15.635	13.886	13.886	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.790	-0.913	17.461	-13.207	-13.207	0.000	0.000	0.000	0.000
121	A	123	GLU	-1	-0.847	-0.953	21.191	-12.132	-12.132	0.000	0.000	0.000	0.000
122	A	124	ASP	-1	-0.938	-0.943	24.251	-10.323	-10.323	0.000	0.000	0.000	0.000
123	A	125	ASP	-1	-0.907	-0.951	19.603	-13.886	-13.886	0.000	0.000	0.000	0.000
124	A	126	LEU	0	-0.093	-0.057	20.383	-0.236	-0.236	0.000	0.000	0.000	0.000
125	A	127	ASP	-1	-0.777	-0.887	24.128	-9.233	-9.233	0.000	0.000	0.000	0.000
126	A	128	GLU	-1	-0.823	-0.909	27.444	-9.447	-9.447	0.000	0.000	0.000	0.000
127	A	129	ASN	0	-0.065	-0.037	29.469	0.238	0.238	0.000	0.000	0.000	0.000
128	A	130	GLU	-1	-0.807	-0.902	25.468	-10.865	-10.865	0.000	0.000	0.000	0.000
129	A	131	LEU	0	-0.007	0.001	22.904	-0.142	-0.142	0.000	0.000	0.000	0.000
130	A	132	LEU	0	0.009	0.006	26.654	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	133	MET	0	-0.037	-0.008	29.247	0.277	0.277	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.817	0.892	22.489	11.885	11.885	0.000	0.000	0.000	0.000
133	A	135	ILE	0	0.034	0.017	25.971	-0.075	-0.075	0.000	0.000	0.000	0.000
134	A	136	SER	0	-0.024	-0.012	27.961	0.137	0.137	0.000	0.000	0.000	0.000
135	A	137	ASN	0	-0.050	-0.044	29.183	0.303	0.303	0.000	0.000	0.000	0.000
136	A	138	ALA	0	-0.022	0.017	26.152	-0.078	-0.078	0.000	0.000	0.000	0.000
137	A	139	ALA	0	-0.004	0.001	26.090	0.371	0.371	0.000	0.000	0.000	0.000
138	A	140	GLY	0	-0.026	-0.024	27.196	0.126	0.126	0.000	0.000	0.000	0.000
139	A	141	ALA	-1	-0.911	-0.947	22.434	-12.325	-12.325	0.000	0.000	0.000	0.000

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