FMO DATABASE

FMODB ID: M2MVZ

Calculation Name: 2OOK-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: 2OOK

Chain ID: A

ChEMBL ID:

UniProt ID: Q087X8

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	125
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1099027.537743
FMO2-HF: Nuclear repulsion	1049442.857007
FMO2-HF: Total energy	-49584.680736
FMO2-MP2: Total energy	-49732.104059

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:ASP)

Summations of interaction energy for fragment #1(A:2: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.
-7.612	-4.53	0.003	-1.423	-1.663	-0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.051 / q_NPA : -0.051

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	LYS	1	0.794	0.917	3.019	8.477	11.500	0.004	-1.412	-1.615	-0.002
4	A	5	LYS	1	0.971	0.983	4.870	-0.084	-0.025	-0.001	-0.011	-0.048	0.000
5	A	6	HIS	0	0.071	0.035	5.467	1.083	1.083	0.000	0.000	0.000	0.000
6	A	7	GLY	0	0.037	0.022	9.977	0.526	0.526	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.014	-0.013	13.637	0.046	0.046	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.067	-0.016	16.961	0.188	0.188	0.000	0.000	0.000	0.000
9	A	10	ILE	0	0.024	0.005	19.264	-0.045	-0.045	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.002	0.004	23.107	0.085	0.085	0.000	0.000	0.000	0.000
11	A	12	ILE	0	-0.026	-0.007	26.050	-0.029	-0.029	0.000	0.000	0.000	0.000
12	A	13	ASN	0	0.019	0.027	26.218	0.054	0.054	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.914	0.949	30.077	0.056	0.056	0.000	0.000	0.000	0.000
14	A	15	ILE	0	0.058	0.033	30.209	0.030	0.030	0.000	0.000	0.000	0.000
15	A	16	GLU	-1	-0.870	-0.932	34.581	-0.122	-0.122	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.067	-0.045	38.207	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	18	VAL	0	0.011	0.027	36.750	0.006	0.006	0.000	0.000	0.000	0.000
18	A	19	PHE	0	-0.012	-0.020	34.048	0.008	0.008	0.000	0.000	0.000	0.000
19	A	20	PHE	0	-0.001	-0.005	28.606	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	21	VAL	0	0.028	0.015	27.512	0.024	0.024	0.000	0.000	0.000	0.000
21	A	22	THR	0	-0.026	-0.007	24.679	-0.031	-0.031	0.000	0.000	0.000	0.000
22	A	23	LEU	0	0.008	-0.003	21.854	0.018	0.018	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.805	0.907	15.933	1.502	1.502	0.000	0.000	0.000	0.000
24	A	25	ALA	0	-0.014	-0.011	16.964	-0.033	-0.033	0.000	0.000	0.000	0.000
25	A	26	ILE	0	0.007	-0.009	11.766	0.035	0.035	0.000	0.000	0.000	0.000
26	A	27	GLY	0	-0.025	-0.025	10.288	-0.292	-0.292	0.000	0.000	0.000	0.000
27	A	28	THR	0	-0.032	-0.035	10.025	0.706	0.706	0.000	0.000	0.000	0.000
28	A	29	LEU	0	-0.056	-0.013	11.344	-0.380	-0.380	0.000	0.000	0.000	0.000
29	A	30	THR	0	0.047	-0.012	11.839	0.466	0.466	0.000	0.000	0.000	0.000
30	A	31	HIS	0	0.013	-0.006	14.699	0.265	0.265	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.957	-0.972	13.976	-2.155	-2.155	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.799	-0.885	12.639	-3.780	-3.780	0.000	0.000	0.000	0.000
33	A	34	TYR	0	0.004	0.002	15.524	0.270	0.270	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.027	-0.010	19.161	0.226	0.226	0.000	0.000	0.000	0.000
35	A	36	VAL	0	-0.029	-0.006	16.160	0.200	0.200	0.000	0.000	0.000	0.000
36	A	37	ILE	0	-0.026	-0.002	14.515	0.176	0.176	0.000	0.000	0.000	0.000
37	A	38	THR	0	-0.015	-0.016	19.157	0.188	0.188	0.000	0.000	0.000	0.000
38	A	39	PRO	0	0.049	0.026	22.248	0.110	0.110	0.000	0.000	0.000	0.000
39	A	40	MET	0	-0.045	-0.011	20.037	0.124	0.124	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.009	-0.002	20.533	0.087	0.087	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.910	-0.956	24.313	-0.776	-0.776	0.000	0.000	0.000	0.000
42	A	43	GLY	0	-0.002	-0.002	27.087	0.070	0.070	0.000	0.000	0.000	0.000
43	A	44	ALA	0	-0.017	0.002	26.210	0.071	0.071	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.012	0.004	28.160	0.058	0.058	0.000	0.000	0.000	0.000
45	A	46	SER	0	-0.059	-0.036	29.937	0.057	0.057	0.000	0.000	0.000	0.000
46	A	47	GLN	0	-0.044	-0.041	32.096	0.070	0.070	0.000	0.000	0.000	0.000
47	A	48	VAL	0	-0.026	-0.004	31.000	0.041	0.041	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.808	-0.898	34.141	-0.267	-0.267	0.000	0.000	0.000	0.000
49	A	50	GLN	0	0.002	0.013	36.306	0.033	0.033	0.000	0.000	0.000	0.000
50	A	51	PRO	0	0.005	0.002	39.052	-0.016	-0.016	0.000	0.000	0.000	0.000
51	A	52	LYS	1	0.878	0.930	39.317	0.310	0.310	0.000	0.000	0.000	0.000
52	A	53	VAL	0	0.002	0.012	33.551	0.019	0.019	0.000	0.000	0.000	0.000
53	A	54	SER	0	0.074	0.041	33.652	-0.018	-0.018	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.016	-0.004	26.258	0.021	0.021	0.000	0.000	0.000	0.000
55	A	56	PHE	0	0.020	0.010	23.724	-0.014	-0.014	0.000	0.000	0.000	0.000
56	A	57	LEU	0	0.014	-0.008	21.711	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	58	ASP	-1	-0.774	-0.847	19.438	-1.337	-1.337	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.040	-0.001	18.665	-0.118	-0.118	0.000	0.000	0.000	0.000
59	A	60	THR	0	-0.031	-0.029	18.157	-0.252	-0.252	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.879	-0.925	12.831	-2.189	-2.189	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.049	-0.006	13.054	-0.665	-0.665	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.797	-0.889	10.575	-6.164	-6.164	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.000	-0.017	14.205	0.440	0.440	0.000	0.000	0.000	0.000
64	A	65	TRP	0	-0.060	-0.036	15.251	-0.264	-0.264	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.861	-0.920	15.308	-3.234	-3.234	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.011	-0.018	17.887	0.262	0.262	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.736	0.829	21.412	1.378	1.378	0.000	0.000	0.000	0.000
68	A	69	ALA	0	0.022	0.027	19.845	0.127	0.127	0.000	0.000	0.000	0.000
69	A	70	ALA	0	0.020	0.004	21.891	0.070	0.070	0.000	0.000	0.000	0.000
70	A	71	TRP	0	0.041	0.004	16.939	0.216	0.216	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.825	-0.885	22.143	-1.503	-1.503	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.844	-0.890	25.070	-1.056	-1.056	0.000	0.000	0.000	0.000
73	A	74	LEU	0	0.004	0.021	22.696	0.097	0.097	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.830	0.904	26.369	0.959	0.959	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.010	0.004	24.312	0.016	0.016	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.037	0.006	28.944	0.022	0.022	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.006	0.001	32.397	0.011	0.011	0.000	0.000	0.000	0.000
78	A	79	LYS	1	0.872	0.939	34.387	0.252	0.252	0.000	0.000	0.000	0.000
79	A	80	HIS	0	-0.114	-0.068	36.284	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	LYS	1	0.837	0.913	36.085	0.453	0.453	0.000	0.000	0.000	0.000
81	A	82	SER	0	-0.011	0.005	37.999	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.886	-0.936	36.684	-0.484	-0.484	0.000	0.000	0.000	0.000
83	A	84	PHE	0	-0.044	-0.030	30.585	0.029	0.029	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.910	-0.958	35.667	-0.352	-0.352	0.000	0.000	0.000	0.000
85	A	86	ARG	1	0.771	0.872	34.655	0.366	0.366	0.000	0.000	0.000	0.000
86	A	87	VAL	0	0.006	-0.003	28.899	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	88	ALA	0	-0.001	0.007	29.461	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	89	ILE	0	-0.028	-0.015	24.712	-0.037	-0.037	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.004	0.010	22.873	0.018	0.018	0.000	0.000	0.000	0.000
90	A	91	GLY	0	0.010	-0.006	21.494	-0.138	-0.138	0.000	0.000	0.000	0.000
91	A	92	ASN	0	-0.054	-0.043	17.722	0.220	0.220	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.892	0.937	21.910	1.153	1.153	0.000	0.000	0.000	0.000
93	A	94	ASP	-1	-0.911	-0.930	21.450	-1.251	-1.251	0.000	0.000	0.000	0.000
94	A	95	TRP	0	0.009	-0.005	22.554	-0.039	-0.039	0.000	0.000	0.000	0.000
95	A	96	GLN	0	0.028	0.018	16.808	0.058	0.058	0.000	0.000	0.000	0.000
96	A	97	GLU	-1	-0.896	-0.953	18.502	-2.538	-2.538	0.000	0.000	0.000	0.000
97	A	98	TRP	0	0.041	0.010	17.818	0.335	0.335	0.000	0.000	0.000	0.000
98	A	99	ALA	0	0.003	0.018	21.955	0.134	0.134	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.017	-0.028	24.786	0.096	0.096	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.822	0.909	23.722	1.571	1.571	0.000	0.000	0.000	0.000
101	A	102	ILE	0	0.036	0.029	20.832	0.087	0.087	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.037	0.018	24.742	0.063	0.063	0.000	0.000	0.000	0.000
103	A	104	SER	0	-0.058	-0.040	27.829	0.081	0.081	0.000	0.000	0.000	0.000
104	A	105	TRP	0	-0.020	-0.016	20.133	0.028	0.028	0.000	0.000	0.000	0.000
105	A	106	PHE	0	0.008	0.007	25.444	0.051	0.051	0.000	0.000	0.000	0.000
106	A	107	ILE	0	-0.007	0.004	30.908	0.001	0.001	0.000	0.000	0.000	0.000
107	A	108	ALA	0	-0.015	-0.020	33.778	0.016	0.016	0.000	0.000	0.000	0.000
108	A	109	GLY	0	0.013	0.029	35.859	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.939	-0.976	36.153	-0.490	-0.490	0.000	0.000	0.000	0.000
110	A	111	ILE	0	-0.014	-0.010	30.558	-0.016	-0.016	0.000	0.000	0.000	0.000
111	A	112	LYS	1	0.905	0.969	31.935	0.550	0.550	0.000	0.000	0.000	0.000
112	A	113	TYR	0	-0.009	-0.004	26.986	0.000	0.000	0.000	0.000	0.000	0.000
113	A	114	PHE	0	-0.035	-0.013	27.501	0.074	0.074	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.905	-0.955	25.058	-0.892	-0.892	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.872	-0.936	24.988	-0.513	-0.513	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.897	-0.971	23.989	-0.558	-0.558	0.000	0.000	0.000	0.000
117	A	118	ASP	-1	-0.958	-0.971	27.107	-0.268	-0.268	0.000	0.000	0.000	0.000
118	A	119	ASP	-1	-0.911	-0.966	30.679	-0.439	-0.439	0.000	0.000	0.000	0.000
119	A	120	ALA	0	-0.027	-0.009	28.442	0.008	0.008	0.000	0.000	0.000	0.000
120	A	121	LEU	0	-0.006	-0.014	27.741	0.023	0.023	0.000	0.000	0.000	0.000
121	A	122	LYS	1	0.936	0.973	31.404	0.320	0.320	0.000	0.000	0.000	0.000
122	A	123	TRP	0	0.010	-0.012	32.598	0.009	0.009	0.000	0.000	0.000	0.000
123	A	124	LEU	0	-0.029	-0.012	30.235	0.003	0.003	0.000	0.000	0.000	0.000
124	A	125	ARG	1	0.757	0.886	34.534	0.232	0.232	0.000	0.000	0.000	0.000
125	A	126	TYR	-1	-0.890	-0.919	36.947	-0.279	-0.279	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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