FMO DATABASE

FMODB ID: Q5Q5Y

Calculation Name: 1VR7-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: 1VR7

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WZC3

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	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1019682.354751
FMO2-HF: Nuclear repulsion	971887.500837
FMO2-HF: Total energy	-47794.853914
FMO2-MP2: Total energy	-47935.697571

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:2:LYS)

Summations of interaction energy for fragment #1(A:2:LYS)

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.
-474.794	-471.618	22.076	-14.002	-11.249	-0.153

Interaction energy analysis for fragmet #1(A:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.729 / q_NPA : 1.845

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	4	LEU	0	0.007	0.014	3.644	-3.925	-2.023	-0.014	-1.009	-0.879	-0.001
110	A	111	GLU	-1	-0.779	-0.872	1.676	-173.281	-176.905	18.102	-8.670	-5.807	-0.104
113	A	114	ARG	1	0.819	0.890	3.402	84.237	84.824	0.009	-0.110	-0.485	0.000
114	A	115	TYR	0	0.040	0.005	2.656	-9.697	-5.626	3.980	-4.195	-3.857	-0.048
115	A	116	ASP	-1	-0.840	-0.921	4.557	-87.844	-87.604	-0.001	-0.018	-0.221	0.000
4	A	5	GLY	0	0.057	0.019	6.371	4.549	4.549	0.000	0.000	0.000	0.000
5	A	6	ARG	1	0.788	0.894	6.353	53.582	53.582	0.000	0.000	0.000	0.000
6	A	7	HIS	0	-0.042	-0.036	8.473	3.655	3.655	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.010	0.010	11.543	-1.141	-1.141	0.000	0.000	0.000	0.000
8	A	9	VAL	0	0.015	0.012	13.880	2.185	2.185	0.000	0.000	0.000	0.000
9	A	10	ALA	0	-0.017	-0.022	16.136	-0.449	-0.449	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.801	-0.850	18.661	-24.965	-24.965	0.000	0.000	0.000	0.000
11	A	12	PHE	0	-0.005	-0.021	21.006	-0.058	-0.058	0.000	0.000	0.000	0.000
12	A	13	TYR	0	-0.038	-0.045	23.400	0.899	0.899	0.000	0.000	0.000	0.000
13	A	14	GLU	-1	-0.908	-0.975	27.497	-19.734	-19.734	0.000	0.000	0.000	0.000
14	A	15	CYS	0	-0.029	-0.008	28.666	-0.100	-0.100	0.000	0.000	0.000	0.000
15	A	16	ASP	-1	-0.822	-0.906	31.084	-17.171	-17.171	0.000	0.000	0.000	0.000
16	A	17	ARG	1	0.897	0.936	33.771	17.068	17.068	0.000	0.000	0.000	0.000
17	A	18	GLU	-1	-0.876	-0.935	35.719	-15.905	-15.905	0.000	0.000	0.000	0.000
18	A	19	VAL	0	-0.048	-0.030	31.734	-0.068	-0.068	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.045	-0.021	29.559	-0.275	-0.275	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.726	-0.832	32.964	-17.087	-17.087	0.000	0.000	0.000	0.000
21	A	22	ASN	0	0.022	0.022	35.491	0.299	0.299	0.000	0.000	0.000	0.000
22	A	23	VAL	0	0.041	0.006	33.148	-0.489	-0.489	0.000	0.000	0.000	0.000
23	A	24	GLN	0	-0.024	0.002	32.940	-0.479	-0.479	0.000	0.000	0.000	0.000
24	A	25	LEU	0	0.007	0.006	32.278	-0.341	-0.341	0.000	0.000	0.000	0.000
25	A	26	ILE	0	0.022	0.006	28.540	-0.774	-0.774	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.810	-0.895	28.356	-20.940	-20.940	0.000	0.000	0.000	0.000
27	A	28	GLN	0	-0.048	-0.026	28.298	-0.471	-0.471	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.831	-0.918	27.525	-21.840	-21.840	0.000	0.000	0.000	0.000
29	A	30	MET	0	-0.028	-0.007	22.146	-1.160	-1.160	0.000	0.000	0.000	0.000
30	A	31	LYS	1	0.844	0.933	23.344	19.801	19.801	0.000	0.000	0.000	0.000
31	A	32	GLN	0	-0.029	-0.017	24.000	-0.105	-0.105	0.000	0.000	0.000	0.000
32	A	33	ALA	0	-0.013	-0.008	21.285	-0.830	-0.830	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.007	0.001	19.491	-1.578	-1.578	0.000	0.000	0.000	0.000
34	A	35	TYR	0	-0.025	-0.008	19.389	-1.062	-1.062	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.875	-0.928	20.461	-26.253	-26.253	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.132	-0.068	15.468	-1.315	-1.315	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.062	0.027	15.385	-2.206	-2.206	0.000	0.000	0.000	0.000
38	A	39	ALA	0	-0.027	-0.006	16.402	-0.402	-0.402	0.000	0.000	0.000	0.000
39	A	40	THR	0	-0.028	-0.013	17.424	2.100	2.100	0.000	0.000	0.000	0.000
40	A	41	ILE	0	-0.023	-0.018	19.394	-0.725	-0.725	0.000	0.000	0.000	0.000
41	A	42	VAL	0	-0.028	0.000	20.315	0.737	0.737	0.000	0.000	0.000	0.000
42	A	43	THR	0	-0.032	-0.030	23.054	1.385	1.385	0.000	0.000	0.000	0.000
43	A	44	SER	0	-0.007	-0.022	24.771	-1.241	-1.241	0.000	0.000	0.000	0.000
44	A	45	THR	0	-0.035	-0.006	27.313	0.948	0.948	0.000	0.000	0.000	0.000
45	A	46	PHE	0	0.016	0.016	26.129	-0.702	-0.702	0.000	0.000	0.000	0.000
46	A	47	HIS	0	-0.014	0.000	31.062	1.116	1.116	0.000	0.000	0.000	0.000
47	A	48	ARG	1	0.824	0.876	33.472	15.932	15.932	0.000	0.000	0.000	0.000
48	A	49	PHE	0	-0.043	-0.016	32.182	0.428	0.428	0.000	0.000	0.000	0.000
49	A	50	LEU	0	0.091	0.027	37.943	-0.117	-0.117	0.000	0.000	0.000	0.000
50	A	51	PRO	0	-0.072	0.001	40.315	0.280	0.280	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.044	-0.041	37.038	0.367	0.367	0.000	0.000	0.000	0.000
52	A	53	GLY	0	-0.001	0.013	34.499	-0.107	-0.107	0.000	0.000	0.000	0.000
53	A	54	VAL	0	-0.011	-0.007	30.764	0.278	0.278	0.000	0.000	0.000	0.000
54	A	55	SER	0	-0.042	-0.017	29.063	-0.913	-0.913	0.000	0.000	0.000	0.000
55	A	56	GLY	0	0.014	0.002	27.624	0.758	0.758	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.029	-0.019	22.970	-1.040	-1.040	0.000	0.000	0.000	0.000
57	A	58	VAL	0	0.018	0.012	21.902	1.130	1.130	0.000	0.000	0.000	0.000
58	A	59	VAL	0	-0.005	0.000	20.642	-1.362	-1.362	0.000	0.000	0.000	0.000
59	A	60	ILE	0	0.007	-0.006	15.238	1.205	1.205	0.000	0.000	0.000	0.000
60	A	61	SER	0	0.003	-0.018	15.291	0.015	0.015	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.917	-0.950	11.672	-42.754	-42.754	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.061	-0.046	13.733	-1.571	-1.571	0.000	0.000	0.000	0.000
63	A	64	HIS	0	-0.033	-0.020	15.862	2.389	2.389	0.000	0.000	0.000	0.000
64	A	65	LEU	0	0.069	0.050	16.556	-1.815	-1.815	0.000	0.000	0.000	0.000
65	A	66	THR	0	-0.069	-0.049	19.494	2.146	2.146	0.000	0.000	0.000	0.000
66	A	67	ILE	0	0.060	0.026	22.174	-0.606	-0.606	0.000	0.000	0.000	0.000
67	A	68	HIS	1	0.857	0.918	24.029	25.285	25.285	0.000	0.000	0.000	0.000
68	A	69	THR	0	0.013	-0.006	27.410	-0.376	-0.376	0.000	0.000	0.000	0.000
69	A	70	TRP	0	0.031	0.017	27.133	0.121	0.121	0.000	0.000	0.000	0.000
70	A	71	PRO	0	0.022	0.010	32.446	-0.043	-0.043	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.821	-0.917	35.091	-17.481	-17.481	0.000	0.000	0.000	0.000
72	A	73	TYR	0	-0.018	-0.010	32.098	0.255	0.255	0.000	0.000	0.000	0.000
73	A	74	GLY	0	-0.048	-0.016	32.723	-0.070	-0.070	0.000	0.000	0.000	0.000
74	A	75	TYR	0	-0.090	-0.077	23.923	0.028	0.028	0.000	0.000	0.000	0.000
75	A	76	ALA	0	0.013	-0.005	26.388	0.558	0.558	0.000	0.000	0.000	0.000
76	A	77	ALA	0	0.023	0.043	23.113	-0.688	-0.688	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.012	-0.025	20.258	0.759	0.759	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.873	-0.902	17.978	-34.243	-34.243	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.021	-0.021	15.941	1.263	1.263	0.000	0.000	0.000	0.000
80	A	81	PHE	0	-0.007	-0.010	10.799	-3.176	-3.176	0.000	0.000	0.000	0.000
81	A	82	THR	0	0.002	0.019	10.871	2.103	2.103	0.000	0.000	0.000	0.000
82	A	83	CYS	0	0.019	0.013	8.871	-5.060	-5.060	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.043	0.027	7.773	4.156	4.156	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.990	-1.000	5.828	-73.338	-73.338	0.000	0.000	0.000	0.000
85	A	86	ASP	-1	-0.949	-0.965	7.818	-42.163	-42.163	0.000	0.000	0.000	0.000
86	A	87	VAL	0	-0.019	-0.001	10.604	3.614	3.614	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.788	-0.903	10.808	-48.964	-48.964	0.000	0.000	0.000	0.000
88	A	89	PRO	0	-0.024	-0.007	11.077	3.832	3.832	0.000	0.000	0.000	0.000
89	A	90	TRP	0	-0.029	-0.044	11.090	5.031	5.031	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.914	0.970	15.467	34.764	34.764	0.000	0.000	0.000	0.000
91	A	92	ALA	0	0.053	0.031	17.226	1.997	1.997	0.000	0.000	0.000	0.000
92	A	93	PHE	0	-0.002	-0.008	17.785	1.866	1.866	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.887	-0.946	19.430	-27.077	-27.077	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.078	-0.040	21.344	1.126	1.126	0.000	0.000	0.000	0.000
95	A	96	LEU	0	0.080	0.033	21.543	1.335	1.335	0.000	0.000	0.000	0.000
96	A	97	LYS	1	0.901	0.951	23.050	24.674	24.674	0.000	0.000	0.000	0.000
97	A	98	LYS	1	0.798	0.889	24.180	25.872	25.872	0.000	0.000	0.000	0.000
98	A	99	ALA	0	0.048	0.035	27.439	0.833	0.833	0.000	0.000	0.000	0.000
99	A	100	LEU	0	0.011	-0.010	26.661	0.934	0.934	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.799	0.902	29.474	19.416	19.416	0.000	0.000	0.000	0.000
101	A	102	ALA	0	0.031	0.032	26.064	0.436	0.436	0.000	0.000	0.000	0.000
102	A	103	LYS	1	0.840	0.931	27.511	18.485	18.485	0.000	0.000	0.000	0.000
103	A	104	ARG	1	0.923	0.977	25.211	22.241	22.241	0.000	0.000	0.000	0.000
104	A	105	VAL	0	0.015	0.003	20.768	0.219	0.219	0.000	0.000	0.000	0.000
105	A	106	HIS	0	-0.011	0.004	17.091	0.687	0.687	0.000	0.000	0.000	0.000
106	A	107	VAL	0	-0.002	-0.003	14.202	0.360	0.360	0.000	0.000	0.000	0.000
107	A	108	VAL	0	-0.015	0.004	11.489	-0.622	-0.622	0.000	0.000	0.000	0.000
108	A	109	GLU	-1	-0.783	-0.856	7.977	-62.813	-62.813	0.000	0.000	0.000	0.000
109	A	110	HIS	0	-0.018	-0.014	8.307	-5.453	-5.453	0.000	0.000	0.000	0.000
111	A	112	ARG	1	0.862	0.929	6.076	51.257	51.257	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.073	0.035	7.657	-1.556	-1.556	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.918	-0.963	6.758	-54.321	-54.321	0.000	0.000	0.000	0.000
117	A	118	ILE	0	-0.087	-0.039	7.300	6.015	6.015	0.000	0.000	0.000	0.000
118	A	119	GLY	0	-0.024	0.004	9.407	4.433	4.433	0.000	0.000	0.000	0.000
119	A	120	ILE	0	-0.080	-0.043	5.801	3.940	3.940	0.000	0.000	0.000	0.000
120	A	121	PRO	-1	-0.934	-0.962	5.792	-77.836	-77.836	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LYS)