FMO DATABASE

FMODB ID: 4GVZN

Calculation Name: 1HFO-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1HFO

Chain ID: A

ChEMBL ID:

UniProt ID: P81529

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	113
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230712

Total energy (hartree)

FMO2-HF: Electronic energy	-824609.817591
FMO2-HF: Nuclear repulsion	782258.27517
FMO2-HF: Total energy	-42351.542421
FMO2-MP2: Total energy	-42476.486062

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:1:PRO)

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

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.
-81.687	-73.014	23.955	-12.929	-19.702	-0.127

Interaction energy analysis for fragmet #1(A:1:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.781 / q_NPA : 0.871

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	3	PHE	0	0.021	0.009	3.822	3.401	4.844	-0.013	-0.574	-0.856	-0.001
26	A	26	VAL	0	0.015	-0.008	2.513	-1.542	-1.015	1.003	-0.398	-1.132	-0.002
27	A	27	GLY	0	0.018	0.009	3.676	-6.153	-5.482	0.010	-0.287	-0.394	-0.002
28	A	28	ASN	0	0.002	-0.001	4.608	0.666	0.745	-0.001	-0.002	-0.075	0.000
30	A	30	LEU	0	-0.035	-0.019	2.418	0.287	0.363	2.652	-0.599	-2.129	-0.005
31	A	31	SER	0	-0.040	-0.012	4.819	-0.546	-0.479	-0.001	-0.003	-0.063	0.000
32	A	32	LYS	1	0.829	0.922	2.392	51.262	52.081	2.158	-0.619	-2.359	-0.002
33	A	33	PRO	0	0.050	0.021	4.510	0.876	0.978	-0.001	-0.010	-0.091	0.000
34	A	34	GLY	0	0.047	0.013	4.666	-6.942	-6.851	-0.001	-0.004	-0.086	0.000
36	A	36	TYR	0	-0.012	0.004	3.284	1.430	2.446	0.055	-0.401	-0.670	-0.002
37	A	37	VAL	0	-0.076	-0.030	1.823	-44.930	-45.782	12.974	-6.134	-5.989	-0.068
38	A	38	ALA	0	0.022	0.028	3.217	11.965	12.286	0.048	0.139	-0.508	-0.001
61	A	61	LEU	0	-0.004	0.017	3.792	-1.980	-1.781	0.004	-0.037	-0.167	0.000
62	A	62	MET	0	0.021	0.016	3.952	4.002	4.313	0.000	-0.100	-0.211	0.000
63	A	63	SER	0	-0.038	-0.054	2.256	-30.421	-26.952	5.044	-3.868	-4.645	-0.043
64	A	64	ILE	0	0.068	0.079	3.463	7.117	7.316	0.026	-0.018	-0.207	-0.001
67	A	67	ILE	0	-0.042	-0.020	4.127	0.662	0.758	-0.001	-0.011	-0.085	0.000
101	A	101	LEU	0	-0.021	-0.008	4.663	1.498	1.537	-0.001	-0.003	-0.035	0.000
4	A	4	THR	0	0.005	0.013	5.923	2.344	2.344	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.003	0.001	9.591	0.779	0.779	0.000	0.000	0.000	0.000
6	A	6	ASN	0	0.028	0.026	12.842	0.668	0.668	0.000	0.000	0.000	0.000
7	A	7	THR	0	-0.031	-0.045	16.628	0.356	0.356	0.000	0.000	0.000	0.000
8	A	8	ASN	0	0.039	0.016	19.390	-0.201	-0.201	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.001	0.015	19.222	0.577	0.577	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.955	0.970	22.335	11.030	11.030	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.001	-0.008	21.050	-0.341	-0.341	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.084	-0.051	21.663	-0.227	-0.227	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.884	-0.934	23.130	-11.627	-11.627	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.046	-0.012	16.679	-0.483	-0.483	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.003	0.020	17.909	0.225	0.225	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.041	0.001	17.974	-0.945	-0.945	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.831	-0.900	16.867	-16.985	-16.985	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.062	0.055	12.302	-1.377	-1.377	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.050	0.040	11.528	-1.669	-1.669	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.035	0.029	10.502	-2.651	-2.651	0.000	0.000	0.000	0.000
21	A	21	SER	0	0.002	-0.031	11.139	-1.692	-1.692	0.000	0.000	0.000	0.000
22	A	22	THR	0	0.008	-0.008	7.647	-0.579	-0.579	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.006	-0.025	6.495	-4.094	-4.094	0.000	0.000	0.000	0.000
24	A	24	ALA	0	-0.003	0.003	6.564	-3.774	-3.774	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.024	-0.001	8.147	-0.860	-0.860	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.040	-0.021	6.282	1.470	1.470	0.000	0.000	0.000	0.000
35	A	35	SER	0	0.007	0.006	5.965	-1.920	-1.920	0.000	0.000	0.000	0.000
39	A	39	VAL	0	-0.021	-0.022	5.286	-3.407	-3.407	0.000	0.000	0.000	0.000
40	A	40	HIS	0	-0.034	-0.020	7.880	3.411	3.411	0.000	0.000	0.000	0.000
41	A	41	ILE	0	-0.025	-0.022	10.893	-0.385	-0.385	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.031	-0.004	13.877	1.086	1.086	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.016	-0.008	17.105	-0.082	-0.082	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.814	-0.901	20.135	-12.433	-12.433	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.034	-0.011	19.960	0.331	0.331	0.000	0.000	0.000	0.000
46	A	46	GLN	0	-0.017	-0.017	23.284	0.578	0.578	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.012	0.011	20.226	-0.200	-0.200	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.009	-0.001	24.355	0.333	0.333	0.000	0.000	0.000	0.000
49	A	49	PHE	0	0.019	0.010	20.001	-0.095	-0.095	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.024	0.006	25.126	0.328	0.328	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.004	0.001	27.759	0.306	0.306	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.013	0.012	28.906	0.202	0.202	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.026	0.001	27.659	-0.447	-0.447	0.000	0.000	0.000	0.000
54	A	54	ASN	0	0.012	0.024	27.756	-0.018	-0.018	0.000	0.000	0.000	0.000
55	A	55	PRO	0	0.048	0.033	23.744	-0.296	-0.296	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.017	0.008	21.599	0.144	0.144	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.035	0.017	16.463	-0.249	-0.249	0.000	0.000	0.000	0.000
58	A	58	PHE	0	-0.002	0.000	15.913	0.260	0.260	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.076	0.028	12.220	-0.158	-0.158	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.094	-0.045	7.923	1.452	1.452	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.075	0.045	5.716	-1.347	-1.347	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.013	-0.005	5.206	-5.823	-5.823	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.815	-0.896	8.159	-19.425	-19.425	0.000	0.000	0.000	0.000
69	A	69	PRO	0	-0.007	-0.015	11.954	0.098	0.098	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.058	-0.037	15.070	0.373	0.373	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.921	0.951	8.154	27.129	27.129	0.000	0.000	0.000	0.000
72	A	72	ASN	0	0.028	0.002	10.210	-1.511	-1.511	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.985	0.997	12.231	14.448	14.448	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.786	-0.879	13.851	-18.646	-18.646	0.000	0.000	0.000	0.000
75	A	75	HIS	0	-0.005	0.012	8.986	-0.669	-0.669	0.000	0.000	0.000	0.000
76	A	76	SER	0	0.001	0.005	10.894	-0.306	-0.306	0.000	0.000	0.000	0.000
77	A	77	ALA	0	0.000	0.006	13.080	0.321	0.321	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.874	0.916	12.114	20.150	20.150	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.001	-0.001	7.804	0.014	0.014	0.000	0.000	0.000	0.000
80	A	80	PHE	0	-0.007	-0.012	12.042	0.473	0.473	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.894	-0.936	15.572	-14.463	-14.463	0.000	0.000	0.000	0.000
82	A	82	HIS	0	0.006	0.000	11.823	1.290	1.290	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.004	-0.010	12.015	0.428	0.428	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.055	-0.035	15.370	0.917	0.917	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.029	-0.019	17.999	0.873	0.873	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.780	0.879	15.297	17.031	17.031	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.009	0.004	15.095	0.184	0.184	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.037	0.033	19.272	0.514	0.514	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.044	-0.012	18.084	0.558	0.558	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.012	0.009	20.771	-0.346	-0.346	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.871	0.933	19.277	14.199	14.199	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.013	-0.009	20.335	-0.549	-0.549	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.775	0.871	21.821	12.014	12.014	0.000	0.000	0.000	0.000
94	A	94	MET	0	0.009	0.012	16.537	-0.610	-0.610	0.000	0.000	0.000	0.000
95	A	95	TYR	0	-0.009	-0.002	16.359	0.333	0.333	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.017	-0.007	9.724	-0.673	-0.673	0.000	0.000	0.000	0.000
97	A	97	HIS	0	0.029	0.021	11.697	0.532	0.532	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.002	-0.015	7.903	-2.356	-2.356	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.006	0.001	7.668	1.864	1.864	0.000	0.000	0.000	0.000
100	A	100	ASN	0	0.012	-0.004	6.833	-7.014	-7.014	0.000	0.000	0.000	0.000
102	A	102	ASN	0	0.008	-0.012	8.400	-0.671	-0.671	0.000	0.000	0.000	0.000
103	A	103	GLY	0	-0.005	-0.013	9.210	-1.932	-1.932	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.851	-0.934	10.275	-20.757	-20.757	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.899	-0.936	10.813	-21.306	-21.306	0.000	0.000	0.000	0.000
106	A	106	VAL	0	-0.103	-0.058	5.964	-1.807	-1.807	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.038	0.028	9.431	0.358	0.358	0.000	0.000	0.000	0.000
108	A	108	TRP	0	-0.016	-0.035	7.412	-2.489	-2.489	0.000	0.000	0.000	0.000
109	A	109	ASN	0	-0.049	-0.024	10.012	2.272	2.272	0.000	0.000	0.000	0.000
110	A	110	GLY	0	0.006	0.005	12.606	1.246	1.246	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.048	-0.014	12.350	2.018	2.018	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.009	0.006	11.580	-0.971	-0.971	0.000	0.000	0.000	0.000
113	A	113	PHE	-1	-0.927	-0.957	6.358	-26.990	-26.990	0.000	0.000	0.000	0.000

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