FMO DATABASE

FMODB ID: L6ZV9

Calculation Name: 3FSD-A-Xray549

Preferred Name:

Target Type:

Ligand Name: 1,2-ethanediol

Ligand 3-letter code: EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3FSD

Chain ID: A

ChEMBL ID:

UniProt ID: Q2RRQ9

Base Structure: X-ray

Registration Date: 2025-10-12

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	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-983404.290327
FMO2-HF: Nuclear repulsion	937010.165994
FMO2-HF: Total energy	-46394.124332
FMO2-MP2: Total energy	-46530.523585

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:13:ASP)

Summations of interaction energy for fragment #1(A:13: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.
-7.963	-4.332	0.053	-1.441	-2.242	0.001

Interaction energy analysis for fragmet #1(A:13:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.084 / q_NPA : -0.059

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	15	ILE	0	0.009	0.015	3.704	-13.114	-11.429	0.004	-0.861	-0.827	0.001
6	A	18	TYR	0	-0.021	-0.017	3.265	2.006	2.323	0.007	-0.080	-0.244	0.000
74	A	86	ARG	1	0.777	0.887	4.677	-6.925	-6.840	-0.001	-0.007	-0.077	0.000
103	A	115	ARG	1	0.903	0.931	3.577	-6.769	-6.398	0.001	-0.148	-0.224	0.001
109	A	121	GLY	0	-0.034	-0.015	4.488	-3.798	-3.780	-0.001	-0.003	-0.014	0.000
110	A	122	TRP	0	-0.058	-0.030	2.970	3.774	4.929	0.043	-0.342	-0.856	-0.001
4	A	16	ALA	0	0.027	0.014	6.037	-0.136	-0.136	0.000	0.000	0.000	0.000
5	A	17	PHE	0	0.002	-0.005	5.078	0.587	0.587	0.000	0.000	0.000	0.000
7	A	19	GLU	-1	-0.749	-0.848	8.181	-0.980	-0.980	0.000	0.000	0.000	0.000
8	A	20	GLU	-1	-0.820	-0.891	10.655	-1.727	-1.727	0.000	0.000	0.000	0.000
9	A	21	ARG	1	0.912	0.963	8.220	7.887	7.887	0.000	0.000	0.000	0.000
10	A	22	LEU	0	0.005	0.004	12.281	0.442	0.442	0.000	0.000	0.000	0.000
11	A	23	ARG	1	0.827	0.896	14.172	1.945	1.945	0.000	0.000	0.000	0.000
12	A	24	ALA	0	0.035	0.014	15.459	0.280	0.280	0.000	0.000	0.000	0.000
13	A	25	ALA	0	-0.004	0.018	16.235	0.249	0.249	0.000	0.000	0.000	0.000
14	A	26	MET	0	-0.037	-0.021	17.949	0.195	0.195	0.000	0.000	0.000	0.000
15	A	27	LEU	0	-0.024	0.001	19.911	0.173	0.173	0.000	0.000	0.000	0.000
16	A	28	THR	0	-0.047	-0.062	19.947	0.141	0.141	0.000	0.000	0.000	0.000
17	A	29	GLY	0	0.020	0.017	22.013	0.135	0.135	0.000	0.000	0.000	0.000
18	A	30	ASP	-1	-0.850	-0.914	18.269	-2.404	-2.404	0.000	0.000	0.000	0.000
19	A	31	LEU	0	0.045	0.013	19.608	-0.212	-0.212	0.000	0.000	0.000	0.000
20	A	32	LYS	1	0.887	0.942	19.142	1.753	1.753	0.000	0.000	0.000	0.000
21	A	33	GLY	0	0.051	0.036	15.842	-0.269	-0.269	0.000	0.000	0.000	0.000
22	A	34	LEU	0	-0.026	-0.019	15.381	-0.377	-0.377	0.000	0.000	0.000	0.000
23	A	35	GLU	-1	-0.821	-0.911	16.926	-1.756	-1.756	0.000	0.000	0.000	0.000
24	A	36	THR	0	-0.091	-0.041	12.707	-0.078	-0.078	0.000	0.000	0.000	0.000
25	A	37	LEU	0	-0.017	-0.013	10.422	-0.523	-0.523	0.000	0.000	0.000	0.000
26	A	38	LEU	0	0.006	0.019	12.580	-0.180	-0.180	0.000	0.000	0.000	0.000
27	A	39	ALA	0	-0.018	-0.003	14.582	-0.050	-0.050	0.000	0.000	0.000	0.000
28	A	40	ASP	-1	-0.831	-0.935	16.155	-1.701	-1.701	0.000	0.000	0.000	0.000
29	A	41	ASP	-1	-0.832	-0.876	18.199	-1.279	-1.279	0.000	0.000	0.000	0.000
30	A	42	LEU	0	-0.065	-0.015	17.159	0.097	0.097	0.000	0.000	0.000	0.000
31	A	43	ALA	0	0.015	0.011	19.699	0.087	0.087	0.000	0.000	0.000	0.000
32	A	44	PHE	0	-0.034	-0.037	18.647	-0.040	-0.040	0.000	0.000	0.000	0.000
33	A	45	VAL	0	-0.017	0.005	22.332	0.040	0.040	0.000	0.000	0.000	0.000
34	A	46	ASP	-1	-0.743	-0.881	24.555	-0.574	-0.574	0.000	0.000	0.000	0.000
35	A	47	HIS	1	0.856	0.885	26.728	0.569	0.569	0.000	0.000	0.000	0.000
36	A	48	THR	0	-0.104	-0.064	28.892	0.048	0.048	0.000	0.000	0.000	0.000
37	A	49	GLY	0	-0.025	-0.011	29.744	0.045	0.045	0.000	0.000	0.000	0.000
38	A	50	CYS	-1	-0.746	-0.782	30.397	-0.500	-0.500	0.000	0.000	0.000	0.000
39	A	51	VAL	0	-0.016	-0.021	25.820	-0.037	-0.037	0.000	0.000	0.000	0.000
40	A	52	LYS	1	0.738	0.811	24.752	0.602	0.602	0.000	0.000	0.000	0.000
41	A	53	THR	0	0.069	0.036	24.097	-0.049	-0.049	0.000	0.000	0.000	0.000
42	A	54	LYS	1	0.787	0.889	17.670	2.149	2.149	0.000	0.000	0.000	0.000
43	A	55	GLN	0	0.035	0.007	22.053	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	56	THR	0	0.015	-0.004	25.123	0.021	0.021	0.000	0.000	0.000	0.000
45	A	57	HIS	0	-0.009	0.003	20.253	0.112	0.112	0.000	0.000	0.000	0.000
46	A	58	LEU	0	-0.030	-0.023	19.735	-0.055	-0.055	0.000	0.000	0.000	0.000
47	A	59	GLU	-1	-0.841	-0.903	23.986	-0.932	-0.932	0.000	0.000	0.000	0.000
48	A	60	PRO	0	0.019	0.010	26.498	0.014	0.014	0.000	0.000	0.000	0.000
49	A	61	TYR	0	0.006	-0.001	22.450	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	62	ARG	1	0.764	0.865	24.677	1.194	1.194	0.000	0.000	0.000	0.000
51	A	63	ALA	0	0.006	0.005	27.940	0.024	0.024	0.000	0.000	0.000	0.000
52	A	64	GLY	0	-0.031	-0.010	29.838	0.048	0.048	0.000	0.000	0.000	0.000
53	A	65	LEU	0	-0.030	-0.001	31.037	0.028	0.028	0.000	0.000	0.000	0.000
54	A	66	LEU	0	-0.035	-0.010	25.437	0.044	0.044	0.000	0.000	0.000	0.000
55	A	67	LYS	1	0.843	0.924	25.458	1.037	1.037	0.000	0.000	0.000	0.000
56	A	68	LEU	0	0.008	0.013	22.722	0.070	0.070	0.000	0.000	0.000	0.000
57	A	69	SER	0	-0.035	-0.031	26.658	-0.042	-0.042	0.000	0.000	0.000	0.000
58	A	70	ARG	1	0.854	0.907	25.584	0.493	0.493	0.000	0.000	0.000	0.000
59	A	71	LEU	0	0.028	0.011	19.335	0.004	0.004	0.000	0.000	0.000	0.000
60	A	72	ASP	-1	-0.817	-0.873	21.070	-0.784	-0.784	0.000	0.000	0.000	0.000
61	A	73	LEU	0	-0.017	-0.016	16.020	0.028	0.028	0.000	0.000	0.000	0.000
62	A	74	SER	0	-0.005	-0.006	19.526	0.081	0.081	0.000	0.000	0.000	0.000
63	A	75	ASP	-1	-0.888	-0.961	19.747	0.148	0.148	0.000	0.000	0.000	0.000
64	A	76	ALA	0	-0.010	-0.001	14.704	0.006	0.006	0.000	0.000	0.000	0.000
65	A	77	VAL	0	-0.025	-0.004	15.233	0.378	0.378	0.000	0.000	0.000	0.000
66	A	78	VAL	0	0.031	0.021	9.153	-0.262	-0.262	0.000	0.000	0.000	0.000
67	A	79	ARG	1	0.893	0.931	12.504	-1.514	-1.514	0.000	0.000	0.000	0.000
68	A	80	ALA	0	0.014	0.010	9.505	-0.193	-0.193	0.000	0.000	0.000	0.000
69	A	81	ALA	0	-0.008	-0.001	11.275	-0.263	-0.263	0.000	0.000	0.000	0.000
70	A	82	GLY	0	0.050	0.025	12.347	-0.367	-0.367	0.000	0.000	0.000	0.000
71	A	83	GLU	-1	-0.907	-0.960	7.271	6.381	6.381	0.000	0.000	0.000	0.000
72	A	84	ASP	-1	-0.803	-0.890	7.344	2.767	2.767	0.000	0.000	0.000	0.000
73	A	85	GLY	0	0.039	0.031	9.255	-1.312	-1.312	0.000	0.000	0.000	0.000
75	A	87	VAL	0	0.019	0.010	10.187	-0.729	-0.729	0.000	0.000	0.000	0.000
76	A	88	VAL	0	0.000	-0.003	11.298	0.474	0.474	0.000	0.000	0.000	0.000
77	A	89	VAL	0	0.007	0.011	14.269	-0.214	-0.214	0.000	0.000	0.000	0.000
78	A	90	VAL	0	-0.001	-0.003	16.762	0.149	0.149	0.000	0.000	0.000	0.000
79	A	91	ARG	1	0.942	0.992	18.882	0.041	0.041	0.000	0.000	0.000	0.000
80	A	92	ALA	0	0.012	-0.005	21.102	-0.077	-0.077	0.000	0.000	0.000	0.000
81	A	93	VAL	0	-0.008	0.001	22.714	0.076	0.076	0.000	0.000	0.000	0.000
82	A	94	THR	0	-0.046	-0.040	23.959	-0.098	-0.098	0.000	0.000	0.000	0.000
83	A	95	ALA	0	0.033	0.003	26.451	0.084	0.084	0.000	0.000	0.000	0.000
84	A	96	GLY	0	0.032	0.024	28.011	-0.097	-0.097	0.000	0.000	0.000	0.000
85	A	97	VAL	0	-0.026	0.003	30.240	0.061	0.061	0.000	0.000	0.000	0.000
86	A	98	TYR	0	-0.039	-0.041	29.965	-0.095	-0.095	0.000	0.000	0.000	0.000
87	A	99	ASP	-1	-0.822	-0.901	32.448	-0.551	-0.551	0.000	0.000	0.000	0.000
88	A	100	GLY	0	-0.030	-0.011	35.139	0.032	0.032	0.000	0.000	0.000	0.000
89	A	101	GLU	-1	-0.942	-0.962	36.430	-0.365	-0.365	0.000	0.000	0.000	0.000
90	A	102	ALA	0	-0.040	-0.025	34.920	-0.041	-0.041	0.000	0.000	0.000	0.000
91	A	103	PHE	0	-0.015	-0.002	28.023	0.035	0.035	0.000	0.000	0.000	0.000
92	A	104	THR	0	-0.003	-0.022	31.060	-0.029	-0.029	0.000	0.000	0.000	0.000
93	A	105	GLU	-1	-0.816	-0.879	28.552	-0.454	-0.454	0.000	0.000	0.000	0.000
94	A	106	THR	0	-0.021	-0.002	27.323	-0.048	-0.048	0.000	0.000	0.000	0.000
95	A	107	LEU	0	0.027	0.015	24.461	0.035	0.035	0.000	0.000	0.000	0.000
96	A	108	ARG	1	0.923	0.968	21.985	-0.028	-0.028	0.000	0.000	0.000	0.000
97	A	109	PHE	0	0.024	0.006	18.863	-0.070	-0.070	0.000	0.000	0.000	0.000
98	A	110	THR	0	-0.021	-0.017	18.301	0.196	0.196	0.000	0.000	0.000	0.000
99	A	111	ARG	1	0.831	0.900	14.094	1.565	1.565	0.000	0.000	0.000	0.000
100	A	112	ILE	0	0.022	0.008	13.899	0.260	0.260	0.000	0.000	0.000	0.000
101	A	113	TRP	0	-0.023	-0.018	9.294	-0.829	-0.829	0.000	0.000	0.000	0.000
102	A	114	ARG	1	0.839	0.885	10.874	2.360	2.360	0.000	0.000	0.000	0.000
104	A	116	THR	0	-0.063	-0.034	7.750	0.885	0.885	0.000	0.000	0.000	0.000
105	A	117	GLN	0	0.047	0.014	8.463	-1.717	-1.717	0.000	0.000	0.000	0.000
106	A	118	GLY	0	0.035	0.017	11.087	0.126	0.126	0.000	0.000	0.000	0.000
107	A	119	PRO	0	-0.025	-0.027	10.651	-0.351	-0.351	0.000	0.000	0.000	0.000
108	A	120	ALA	0	-0.001	0.010	6.209	-0.162	-0.162	0.000	0.000	0.000	0.000
111	A	123	LYS	1	0.879	0.934	6.956	4.064	4.064	0.000	0.000	0.000	0.000
112	A	124	LEU	0	-0.035	0.003	10.691	0.488	0.488	0.000	0.000	0.000	0.000
113	A	125	VAL	0	0.006	-0.006	13.285	0.082	0.082	0.000	0.000	0.000	0.000
114	A	126	ALA	0	0.034	0.008	15.910	0.214	0.214	0.000	0.000	0.000	0.000
115	A	127	GLY	0	-0.009	-0.017	16.836	-0.166	-0.166	0.000	0.000	0.000	0.000
116	A	128	HIS	0	0.029	0.027	19.202	0.056	0.056	0.000	0.000	0.000	0.000
117	A	129	CYS	0	-0.055	-0.003	21.504	-0.045	-0.045	0.000	0.000	0.000	0.000
118	A	130	SER	0	0.066	0.033	23.975	0.052	0.052	0.000	0.000	0.000	0.000
119	A	131	VAL	0	0.029	0.018	26.757	-0.016	-0.016	0.000	0.000	0.000	0.000
120	A	132	ILE	0	-0.114	-0.059	25.423	0.053	0.053	0.000	0.000	0.000	0.000
121	A	133	LEU	-1	-0.919	-0.945	29.725	-0.029	-0.029	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:13:ASP)