FMO DATABASE

FMODB ID: 46J9N

Calculation Name: 3H96-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 1,2-ethanediol

Ligand 3-letter code: EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3H96

Chain ID: A

ChEMBL ID:

UniProt ID: A0QXM5

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	137
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1171373.101956
FMO2-HF: Nuclear repulsion	1119379.527083
FMO2-HF: Total energy	-51993.574874
FMO2-MP2: Total energy	-52146.263221

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:6:ASP)

Summations of interaction energy for fragment #1(A:6: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.
12.255	17.916	0.336	-2.312	-3.687	-0.007

Interaction energy analysis for fragmet #1(A:6:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.076 / q_NPA : -0.045

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	8	ASN	0	-0.011	-0.027	3.133	-0.100	2.153	0.047	-0.838	-1.463	-0.002
4	A	9	SER	0	-0.038	-0.016	2.706	1.933	3.900	0.139	-0.948	-1.159	-0.007
5	A	10	GLN	0	0.023	0.007	3.086	-1.985	-0.544	0.150	-0.526	-1.065	0.002
6	A	11	VAL	0	0.077	0.031	6.411	0.766	0.766	0.000	0.000	0.000	0.000
7	A	12	ILE	0	-0.008	0.006	6.264	0.783	0.783	0.000	0.000	0.000	0.000
8	A	13	GLN	0	-0.037	-0.022	7.268	1.473	1.473	0.000	0.000	0.000	0.000
9	A	14	GLU	-1	-0.843	-0.917	10.169	-0.093	-0.093	0.000	0.000	0.000	0.000
10	A	15	PHE	0	0.004	0.016	11.619	0.254	0.254	0.000	0.000	0.000	0.000
11	A	16	ARG	1	0.795	0.847	10.696	4.067	4.067	0.000	0.000	0.000	0.000
12	A	17	ALA	0	-0.021	0.008	14.295	0.230	0.230	0.000	0.000	0.000	0.000
13	A	18	ASN	0	-0.061	-0.032	15.433	0.337	0.337	0.000	0.000	0.000	0.000
14	A	19	GLY	0	0.000	0.001	18.089	0.030	0.030	0.000	0.000	0.000	0.000
15	A	20	GLY	0	0.018	0.002	16.762	0.073	0.073	0.000	0.000	0.000	0.000
16	A	21	ARG	1	0.859	0.929	16.894	0.885	0.885	0.000	0.000	0.000	0.000
17	A	22	VAL	0	-0.020	-0.016	12.269	-0.205	-0.205	0.000	0.000	0.000	0.000
18	A	23	GLY	0	0.083	0.048	15.080	0.092	0.092	0.000	0.000	0.000	0.000
19	A	24	GLY	0	0.000	-0.014	14.852	-0.203	-0.203	0.000	0.000	0.000	0.000
20	A	25	ASN	0	-0.040	-0.041	14.311	0.160	0.160	0.000	0.000	0.000	0.000
21	A	26	PHE	0	-0.044	-0.038	11.001	-0.309	-0.309	0.000	0.000	0.000	0.000
22	A	27	GLU	-1	-0.876	-0.929	16.627	-0.407	-0.407	0.000	0.000	0.000	0.000
23	A	28	GLY	0	-0.008	0.007	19.537	-0.041	-0.041	0.000	0.000	0.000	0.000
24	A	29	ALA	0	-0.064	-0.022	18.738	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	30	PRO	0	-0.011	0.004	19.914	-0.055	-0.055	0.000	0.000	0.000	0.000
26	A	31	MET	0	-0.039	0.007	13.528	-0.134	-0.134	0.000	0.000	0.000	0.000
27	A	32	VAL	0	0.012	-0.002	15.991	0.127	0.127	0.000	0.000	0.000	0.000
28	A	33	LEU	0	-0.051	-0.008	10.481	-0.664	-0.664	0.000	0.000	0.000	0.000
29	A	34	VAL	0	0.047	0.011	13.197	0.363	0.363	0.000	0.000	0.000	0.000
30	A	35	HIS	0	-0.070	-0.046	12.781	-0.894	-0.894	0.000	0.000	0.000	0.000
31	A	36	HIS	0	0.008	-0.003	11.406	0.997	0.997	0.000	0.000	0.000	0.000
32	A	37	VAL	0	0.045	0.009	14.479	-0.382	-0.382	0.000	0.000	0.000	0.000
33	A	38	GLY	0	-0.005	-0.002	15.585	0.174	0.174	0.000	0.000	0.000	0.000
34	A	39	ARG	1	0.987	0.992	16.486	2.009	2.009	0.000	0.000	0.000	0.000
35	A	40	LYS	1	0.860	0.935	18.902	1.773	1.773	0.000	0.000	0.000	0.000
36	A	41	THR	0	-0.011	-0.024	15.151	0.161	0.161	0.000	0.000	0.000	0.000
37	A	42	GLY	0	0.058	0.041	17.918	0.034	0.034	0.000	0.000	0.000	0.000
38	A	43	LYS	1	0.940	0.971	9.445	5.739	5.739	0.000	0.000	0.000	0.000
39	A	44	ALA	0	0.050	0.036	13.611	-0.061	-0.061	0.000	0.000	0.000	0.000
40	A	45	ALA	0	-0.063	-0.038	9.863	-0.787	-0.787	0.000	0.000	0.000	0.000
41	A	46	VAL	0	0.048	0.035	8.802	0.808	0.808	0.000	0.000	0.000	0.000
42	A	47	THR	0	-0.034	-0.010	7.981	-2.045	-2.045	0.000	0.000	0.000	0.000
43	A	48	PRO	0	0.027	0.032	8.041	0.921	0.921	0.000	0.000	0.000	0.000
44	A	49	MET	0	-0.062	-0.032	11.009	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	50	MET	0	0.048	0.020	14.215	0.165	0.165	0.000	0.000	0.000	0.000
46	A	51	TYR	0	-0.069	-0.033	17.699	-0.109	-0.109	0.000	0.000	0.000	0.000
47	A	52	LEU	0	0.022	0.021	20.704	0.104	0.104	0.000	0.000	0.000	0.000
48	A	53	PRO	0	-0.009	-0.017	24.474	-0.060	-0.060	0.000	0.000	0.000	0.000
49	A	54	SER	0	0.005	0.002	26.492	0.052	0.052	0.000	0.000	0.000	0.000
50	A	55	ASP	-1	-0.939	-0.970	29.574	-0.691	-0.691	0.000	0.000	0.000	0.000
51	A	56	ASP	-1	-0.907	-0.946	32.695	-0.626	-0.626	0.000	0.000	0.000	0.000
52	A	57	ASP	-1	-0.895	-0.924	31.894	-0.822	-0.822	0.000	0.000	0.000	0.000
53	A	58	PRO	0	-0.010	-0.015	30.942	-0.067	-0.067	0.000	0.000	0.000	0.000
54	A	59	GLY	0	0.021	0.018	28.039	0.007	0.007	0.000	0.000	0.000	0.000
55	A	60	THR	0	-0.019	-0.017	27.209	-0.120	-0.120	0.000	0.000	0.000	0.000
56	A	61	ILE	0	-0.065	-0.026	20.723	0.033	0.033	0.000	0.000	0.000	0.000
57	A	62	TYR	0	0.059	0.024	24.230	-0.058	-0.058	0.000	0.000	0.000	0.000
58	A	63	VAL	0	0.004	-0.002	18.608	-0.080	-0.080	0.000	0.000	0.000	0.000
59	A	64	PHE	0	0.065	0.026	19.570	0.070	0.070	0.000	0.000	0.000	0.000
60	A	65	ALA	0	-0.004	0.005	18.239	-0.232	-0.232	0.000	0.000	0.000	0.000
61	A	66	SER	0	0.030	0.007	18.393	-0.041	-0.041	0.000	0.000	0.000	0.000
62	A	67	LYS	1	0.896	0.955	14.184	2.352	2.352	0.000	0.000	0.000	0.000
63	A	68	ALA	0	0.032	0.016	15.720	0.122	0.122	0.000	0.000	0.000	0.000
64	A	69	GLY	0	0.075	0.043	17.578	0.211	0.211	0.000	0.000	0.000	0.000
65	A	70	ALA	0	-0.080	-0.026	17.617	0.124	0.124	0.000	0.000	0.000	0.000
66	A	71	ALA	0	0.082	0.037	19.656	-0.056	-0.056	0.000	0.000	0.000	0.000
67	A	72	SER	0	-0.006	-0.001	18.965	0.021	0.021	0.000	0.000	0.000	0.000
68	A	73	ASN	0	0.080	0.036	18.985	-0.093	-0.093	0.000	0.000	0.000	0.000
69	A	74	PRO	0	-0.038	-0.008	14.703	-0.082	-0.082	0.000	0.000	0.000	0.000
70	A	75	ALA	0	0.007	-0.013	13.684	0.136	0.136	0.000	0.000	0.000	0.000
71	A	76	TRP	0	0.081	0.034	12.470	0.196	0.196	0.000	0.000	0.000	0.000
72	A	77	TYR	0	-0.022	-0.031	15.386	0.099	0.099	0.000	0.000	0.000	0.000
73	A	78	TYR	0	0.034	0.019	18.831	0.147	0.147	0.000	0.000	0.000	0.000
74	A	79	ASN	0	-0.074	-0.026	14.833	0.432	0.432	0.000	0.000	0.000	0.000
75	A	80	LEU	0	0.038	0.023	17.489	0.110	0.110	0.000	0.000	0.000	0.000
76	A	81	THR	0	0.006	-0.009	20.365	0.151	0.151	0.000	0.000	0.000	0.000
77	A	82	THR	0	-0.101	-0.067	22.219	0.147	0.147	0.000	0.000	0.000	0.000
78	A	83	ALA	0	-0.008	-0.001	21.334	0.090	0.090	0.000	0.000	0.000	0.000
79	A	84	GLY	0	0.017	0.023	23.385	0.085	0.085	0.000	0.000	0.000	0.000
80	A	85	THR	0	-0.039	-0.017	23.564	0.061	0.061	0.000	0.000	0.000	0.000
81	A	86	ALA	0	-0.028	-0.019	18.768	-0.185	-0.185	0.000	0.000	0.000	0.000
82	A	87	GLN	0	-0.005	0.005	17.632	0.181	0.181	0.000	0.000	0.000	0.000
83	A	88	VAL	0	0.011	0.000	16.804	-0.372	-0.372	0.000	0.000	0.000	0.000
84	A	89	GLU	-1	-0.766	-0.824	13.452	-3.403	-3.403	0.000	0.000	0.000	0.000
85	A	90	VAL	0	0.034	0.004	16.794	-0.184	-0.184	0.000	0.000	0.000	0.000
86	A	91	GLY	0	0.020	0.026	19.342	0.157	0.157	0.000	0.000	0.000	0.000
87	A	92	THR	0	-0.001	-0.019	19.118	-0.086	-0.086	0.000	0.000	0.000	0.000
88	A	93	GLU	-1	-0.854	-0.880	21.233	-1.065	-1.065	0.000	0.000	0.000	0.000
89	A	94	THR	0	-0.010	-0.021	17.980	-0.172	-0.172	0.000	0.000	0.000	0.000
90	A	95	TYR	0	-0.010	-0.005	20.270	0.141	0.141	0.000	0.000	0.000	0.000
91	A	96	ALA	0	0.010	0.012	21.087	-0.217	-0.217	0.000	0.000	0.000	0.000
92	A	97	VAL	0	0.026	0.013	21.977	0.063	0.063	0.000	0.000	0.000	0.000
93	A	98	GLY	0	0.042	0.034	24.065	-0.058	-0.058	0.000	0.000	0.000	0.000
94	A	99	VAL	0	-0.056	-0.040	22.119	-0.030	-0.030	0.000	0.000	0.000	0.000
95	A	100	THR	0	0.004	0.001	25.131	0.102	0.102	0.000	0.000	0.000	0.000
96	A	101	GLU	-1	-0.834	-0.909	26.100	-1.366	-1.366	0.000	0.000	0.000	0.000
97	A	102	VAL	0	-0.009	0.008	27.409	0.078	0.078	0.000	0.000	0.000	0.000
98	A	103	THR	0	-0.032	-0.026	28.969	-0.008	-0.008	0.000	0.000	0.000	0.000
99	A	104	GLY	0	0.037	0.018	31.654	0.029	0.029	0.000	0.000	0.000	0.000
100	A	105	GLU	-1	-0.852	-0.946	33.352	-0.591	-0.591	0.000	0.000	0.000	0.000
101	A	106	ASP	-1	-0.810	-0.877	33.365	-0.686	-0.686	0.000	0.000	0.000	0.000
102	A	107	ARG	1	0.705	0.829	26.662	0.860	0.860	0.000	0.000	0.000	0.000
103	A	108	ASP	-1	-0.805	-0.887	29.827	-0.756	-0.756	0.000	0.000	0.000	0.000
104	A	109	ARG	1	0.771	0.876	31.754	0.692	0.692	0.000	0.000	0.000	0.000
105	A	110	ILE	0	0.023	0.019	27.069	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	111	TYR	0	-0.053	-0.059	23.633	-0.107	-0.107	0.000	0.000	0.000	0.000
107	A	112	SER	0	-0.038	-0.033	27.903	0.020	0.020	0.000	0.000	0.000	0.000
108	A	113	GLU	-1	-0.753	-0.831	29.467	-0.581	-0.581	0.000	0.000	0.000	0.000
109	A	114	GLN	0	0.025	0.007	21.617	0.059	0.059	0.000	0.000	0.000	0.000
110	A	115	ALA	0	-0.044	-0.026	25.692	0.006	0.006	0.000	0.000	0.000	0.000
111	A	116	ARG	1	0.804	0.887	27.091	0.600	0.600	0.000	0.000	0.000	0.000
112	A	117	ARG	1	0.823	0.906	26.200	0.782	0.782	0.000	0.000	0.000	0.000
113	A	118	TYR	0	0.029	0.014	22.181	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	119	PRO	0	0.070	0.026	24.512	-0.063	-0.063	0.000	0.000	0.000	0.000
115	A	120	GLY	0	0.001	0.006	22.461	0.018	0.018	0.000	0.000	0.000	0.000
116	A	121	PHE	0	0.024	-0.006	19.031	-0.080	-0.080	0.000	0.000	0.000	0.000
117	A	122	ALA	0	0.055	0.035	23.643	-0.021	-0.021	0.000	0.000	0.000	0.000
118	A	123	ASP	-1	-0.934	-0.963	23.409	-0.542	-0.542	0.000	0.000	0.000	0.000
119	A	124	TYR	0	-0.034	-0.027	18.598	-0.088	-0.088	0.000	0.000	0.000	0.000
120	A	125	GLU	-1	-0.782	-0.874	23.059	-0.883	-0.883	0.000	0.000	0.000	0.000
121	A	126	LYS	1	0.951	0.971	26.155	0.462	0.462	0.000	0.000	0.000	0.000
122	A	127	LYS	1	0.842	0.926	20.321	0.791	0.791	0.000	0.000	0.000	0.000
123	A	128	THR	0	-0.049	-0.033	22.856	-0.023	-0.023	0.000	0.000	0.000	0.000
124	A	129	ALA	0	0.054	0.039	25.946	-0.008	-0.008	0.000	0.000	0.000	0.000
125	A	130	GLY	0	-0.019	-0.009	29.741	0.035	0.035	0.000	0.000	0.000	0.000
126	A	131	ILE	0	-0.085	-0.027	25.421	0.002	0.002	0.000	0.000	0.000	0.000
127	A	132	ARG	1	0.733	0.833	19.907	1.389	1.389	0.000	0.000	0.000	0.000
128	A	133	THR	0	0.048	0.039	27.088	0.048	0.048	0.000	0.000	0.000	0.000
129	A	134	ILE	0	-0.065	-0.021	21.878	-0.106	-0.106	0.000	0.000	0.000	0.000
130	A	135	PRO	0	0.013	0.014	22.279	0.030	0.030	0.000	0.000	0.000	0.000
131	A	136	VAL	0	0.025	0.010	22.890	-0.102	-0.102	0.000	0.000	0.000	0.000
132	A	137	LEU	0	-0.047	-0.012	20.348	0.040	0.040	0.000	0.000	0.000	0.000
133	A	138	ALA	0	0.033	0.020	23.784	-0.033	-0.033	0.000	0.000	0.000	0.000
134	A	139	LEU	0	-0.055	-0.038	19.725	-0.093	-0.093	0.000	0.000	0.000	0.000
135	A	140	THR	0	0.042	0.009	24.232	0.015	0.015	0.000	0.000	0.000	0.000
136	A	141	ARG	1	0.784	0.857	25.719	1.088	1.088	0.000	0.000	0.000	0.000
137	A	142	THR	-1	-0.939	-0.965	26.429	-1.105	-1.105	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ASP)