FMO DATABASE

FMODB ID: 748LK

Calculation Name: 2GPI-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: 2GPI

Chain ID: A

ChEMBL ID:

UniProt ID: A3QJE4

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	91
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-666607.802709
FMO2-HF: Nuclear repulsion	629574.155231
FMO2-HF: Total energy	-37033.647478
FMO2-MP2: Total energy	-37141.312365

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:0:GLY)

Summations of interaction energy for fragment #1(A:0:GLY)

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.
-152.166	-151.06	-0.006	-0.621	-0.477	-0.002

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.876 / q_NPA : 0.924

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	2	ASN	0	0.043	0.019	3.460	-9.520	-8.420	-0.005	-0.621	-0.473	-0.002
75	A	74	GLU	-1	-0.914	-0.936	5.170	-55.077	-55.071	-0.001	0.000	-0.004	0.000
4	A	3	GLN	0	0.069	0.035	5.119	8.308	8.308	0.000	0.000	0.000	0.000
5	A	4	SER	0	-0.048	-0.021	7.453	4.810	4.810	0.000	0.000	0.000	0.000
6	A	5	ILE	0	-0.011	0.004	8.617	2.713	2.713	0.000	0.000	0.000	0.000
7	A	6	ILE	0	-0.034	-0.011	11.470	-0.802	-0.802	0.000	0.000	0.000	0.000
8	A	7	PHE	0	0.052	0.017	12.253	0.565	0.565	0.000	0.000	0.000	0.000
9	A	8	THR	0	-0.033	-0.016	16.572	0.373	0.373	0.000	0.000	0.000	0.000
10	A	9	GLU	-1	-0.787	-0.871	19.173	-15.484	-15.484	0.000	0.000	0.000	0.000
11	A	10	GLN	0	-0.012	0.002	22.317	0.895	0.895	0.000	0.000	0.000	0.000
12	A	11	LEU	0	-0.027	0.002	22.499	0.029	0.029	0.000	0.000	0.000	0.000
13	A	12	THR	0	-0.024	-0.017	26.059	0.591	0.591	0.000	0.000	0.000	0.000
14	A	13	TRP	0	0.020	0.005	28.252	-0.324	-0.324	0.000	0.000	0.000	0.000
15	A	14	ASP	-1	-0.824	-0.915	29.249	-10.186	-10.186	0.000	0.000	0.000	0.000
16	A	15	VAL	0	-0.004	-0.028	31.232	0.041	0.041	0.000	0.000	0.000	0.000
17	A	16	GLN	0	-0.056	-0.011	32.936	0.393	0.393	0.000	0.000	0.000	0.000
18	A	17	LEU	0	-0.010	-0.020	27.853	0.082	0.082	0.000	0.000	0.000	0.000
19	A	18	SER	0	-0.070	-0.014	30.853	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	19	ALA	0	0.008	0.005	26.894	-0.148	-0.148	0.000	0.000	0.000	0.000
21	A	20	ILE	0	0.010	0.022	24.536	0.325	0.325	0.000	0.000	0.000	0.000
22	A	21	HIS	1	0.789	0.881	24.288	11.904	11.904	0.000	0.000	0.000	0.000
23	A	22	PHE	0	0.030	0.006	17.670	0.194	0.194	0.000	0.000	0.000	0.000
24	A	23	THR	0	0.022	-0.005	20.505	0.023	0.023	0.000	0.000	0.000	0.000
25	A	24	ALA	0	0.051	0.038	15.035	-0.570	-0.570	0.000	0.000	0.000	0.000
26	A	25	GLN	0	-0.026	-0.027	15.849	1.414	1.414	0.000	0.000	0.000	0.000
27	A	26	GLN	0	0.020	0.018	11.143	0.528	0.528	0.000	0.000	0.000	0.000
28	A	27	GLN	0	-0.049	-0.037	14.070	1.034	1.034	0.000	0.000	0.000	0.000
29	A	28	GLY	0	-0.030	-0.008	16.542	0.889	0.889	0.000	0.000	0.000	0.000
30	A	29	MET	0	-0.015	0.003	18.287	0.853	0.853	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.013	-0.012	18.290	-0.945	-0.945	0.000	0.000	0.000	0.000
32	A	31	ILE	0	0.020	0.010	15.216	0.167	0.167	0.000	0.000	0.000	0.000
33	A	32	ASP	-1	-0.857	-0.896	19.137	-13.399	-13.399	0.000	0.000	0.000	0.000
34	A	33	CYS	0	-0.047	-0.013	17.828	-0.726	-0.726	0.000	0.000	0.000	0.000
35	A	34	TYR	0	0.008	-0.002	20.418	0.668	0.668	0.000	0.000	0.000	0.000
36	A	35	ILE	0	0.033	0.028	21.820	-0.495	-0.495	0.000	0.000	0.000	0.000
37	A	36	GLY	0	0.053	0.029	23.876	0.515	0.515	0.000	0.000	0.000	0.000
38	A	37	GLN	0	0.006	-0.013	27.359	-0.062	-0.062	0.000	0.000	0.000	0.000
39	A	38	LYS	1	0.779	0.860	29.710	9.447	9.447	0.000	0.000	0.000	0.000
40	A	39	VAL	0	-0.010	0.014	23.520	0.142	0.142	0.000	0.000	0.000	0.000
41	A	40	LEU	0	0.028	0.019	24.820	-0.183	-0.183	0.000	0.000	0.000	0.000
42	A	41	GLU	-1	-0.776	-0.871	26.828	-9.415	-9.415	0.000	0.000	0.000	0.000
43	A	42	HIS	0	-0.068	-0.051	27.843	0.184	0.184	0.000	0.000	0.000	0.000
44	A	43	LEU	0	-0.040	0.004	22.044	0.090	0.090	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.015	0.011	26.013	-0.039	-0.039	0.000	0.000	0.000	0.000
46	A	45	ALA	0	-0.045	-0.010	28.616	0.294	0.294	0.000	0.000	0.000	0.000
47	A	46	GLU	-1	-0.875	-0.915	31.470	-9.224	-9.224	0.000	0.000	0.000	0.000
48	A	47	LYS	1	0.899	0.936	32.815	8.680	8.680	0.000	0.000	0.000	0.000
49	A	48	ILE	0	-0.011	0.003	30.219	0.166	0.166	0.000	0.000	0.000	0.000
50	A	49	ASN	0	-0.084	-0.048	34.870	0.233	0.233	0.000	0.000	0.000	0.000
51	A	50	ASN	0	0.035	0.017	36.404	0.049	0.049	0.000	0.000	0.000	0.000
52	A	51	SER	0	0.041	0.018	33.659	-0.209	-0.209	0.000	0.000	0.000	0.000
53	A	52	GLU	-1	-0.916	-0.952	32.547	-9.132	-9.132	0.000	0.000	0.000	0.000
54	A	53	GLN	0	-0.028	-0.040	32.504	-0.117	-0.117	0.000	0.000	0.000	0.000
55	A	54	ALA	0	-0.002	-0.006	30.306	-0.291	-0.291	0.000	0.000	0.000	0.000
56	A	55	LEU	0	0.021	0.011	27.162	-0.430	-0.430	0.000	0.000	0.000	0.000
57	A	56	SER	0	-0.016	-0.006	27.634	-0.522	-0.522	0.000	0.000	0.000	0.000
58	A	57	LEU	0	0.017	0.000	27.870	-0.364	-0.364	0.000	0.000	0.000	0.000
59	A	58	PHE	0	-0.019	-0.013	20.504	-0.423	-0.423	0.000	0.000	0.000	0.000
60	A	59	GLU	-1	-0.878	-0.976	23.290	-14.046	-14.046	0.000	0.000	0.000	0.000
61	A	60	GLN	0	-0.097	-0.030	23.411	-0.188	-0.188	0.000	0.000	0.000	0.000
62	A	61	PHE	0	0.033	0.018	21.777	0.029	0.029	0.000	0.000	0.000	0.000
63	A	62	ARG	1	0.848	0.949	18.800	15.012	15.012	0.000	0.000	0.000	0.000
64	A	63	PHE	0	-0.033	-0.035	15.394	-0.718	-0.718	0.000	0.000	0.000	0.000
65	A	64	ASP	-1	-0.802	-0.891	15.269	-18.675	-18.675	0.000	0.000	0.000	0.000
66	A	65	ILE	0	-0.032	-0.020	16.061	-0.752	-0.752	0.000	0.000	0.000	0.000
67	A	66	GLU	0	-0.071	-0.066	15.073	-0.547	-0.547	0.000	0.000	0.000	0.000
68	A	67	GLU	-1	-0.876	-0.915	10.715	-27.777	-27.777	0.000	0.000	0.000	0.000
69	A	68	GLN	0	0.009	0.003	11.550	-2.962	-2.962	0.000	0.000	0.000	0.000
70	A	69	ALA	0	0.024	0.000	13.704	-0.259	-0.259	0.000	0.000	0.000	0.000
71	A	70	GLU	0	-0.094	-0.084	6.315	0.365	0.365	0.000	0.000	0.000	0.000
72	A	71	LYS	1	0.846	0.915	9.175	24.859	24.859	0.000	0.000	0.000	0.000
73	A	72	LEU	0	-0.001	-0.002	10.213	-0.152	-0.152	0.000	0.000	0.000	0.000
74	A	73	ILE	0	-0.023	-0.008	11.423	0.704	0.704	0.000	0.000	0.000	0.000
76	A	75	GLN	0	-0.093	-0.041	9.395	1.025	1.025	0.000	0.000	0.000	0.000
77	A	76	GLU	-1	-0.966	-0.976	12.069	-18.972	-18.972	0.000	0.000	0.000	0.000
78	A	77	ALA	0	-0.014	0.006	14.692	1.557	1.557	0.000	0.000	0.000	0.000
79	A	78	PHE	0	-0.045	-0.027	15.322	0.231	0.231	0.000	0.000	0.000	0.000
80	A	79	ASP	-1	-0.760	-0.872	19.263	-12.588	-12.588	0.000	0.000	0.000	0.000
81	A	80	VAL	0	-0.035	-0.038	22.994	-0.045	-0.045	0.000	0.000	0.000	0.000
82	A	81	GLN	0	-0.093	-0.053	25.196	0.387	0.387	0.000	0.000	0.000	0.000
83	A	82	GLY	0	0.002	0.014	21.911	0.097	0.097	0.000	0.000	0.000	0.000
84	A	83	HIS	1	0.836	0.924	21.081	12.222	12.222	0.000	0.000	0.000	0.000
85	A	84	ILE	0	0.047	0.025	15.888	-0.138	-0.138	0.000	0.000	0.000	0.000
86	A	85	GLN	0	-0.024	-0.029	19.269	0.528	0.528	0.000	0.000	0.000	0.000
87	A	86	VAL	0	0.006	-0.002	17.864	-0.532	-0.532	0.000	0.000	0.000	0.000
88	A	87	GLU	-1	-0.952	-0.984	20.272	-12.732	-12.732	0.000	0.000	0.000	0.000
89	A	88	ARG	1	0.739	0.833	20.438	14.502	14.502	0.000	0.000	0.000	0.000
90	A	89	VAL	0	-0.015	-0.014	18.243	-0.906	-0.906	0.000	0.000	0.000	0.000
91	A	90	ASP	-2	-1.719	-1.818	18.790	-30.202	-30.202	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)