FMO DATABASE

FMODB ID: 15Y1Z

Calculation Name: 2OP5-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: 2OP5

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-09-02

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	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-923879.609624
FMO2-HF: Nuclear repulsion	877749.353022
FMO2-HF: Total energy	-46130.256602
FMO2-MP2: Total energy	-46265.79605

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:4:THR)

Summations of interaction energy for fragment #1(A:4:THR)

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.
-84.337	-81.739	0.59	-1.034	-2.155	-0.005

Interaction energy analysis for fragmet #1(A:4:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.793 / q_NPA : 0.885

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	6	GLU	-1	-0.938	-0.956	3.804	-31.672	-30.180	-0.019	-0.481	-0.992	-0.001
110	A	113	ILE	0	0.022	0.014	2.521	-1.483	-0.377	0.609	-0.553	-1.163	-0.004
4	A	7	THR	0	-0.039	-0.040	5.553	2.624	2.624	0.000	0.000	0.000	0.000
5	A	8	ALA	0	0.040	0.031	8.995	2.035	2.035	0.000	0.000	0.000	0.000
6	A	9	PHE	0	-0.066	-0.049	11.533	2.821	2.821	0.000	0.000	0.000	0.000
7	A	10	LEU	0	0.056	0.037	12.871	-0.903	-0.903	0.000	0.000	0.000	0.000
8	A	11	ASN	0	-0.037	-0.042	15.553	1.512	1.512	0.000	0.000	0.000	0.000
9	A	12	SER	0	0.023	0.031	18.132	-0.307	-0.307	0.000	0.000	0.000	0.000
10	A	13	LEU	0	-0.009	-0.010	19.535	0.767	0.767	0.000	0.000	0.000	0.000
11	A	14	PHE	0	-0.004	-0.019	22.809	-0.172	-0.172	0.000	0.000	0.000	0.000
12	A	15	MET	0	-0.038	-0.007	25.182	0.304	0.304	0.000	0.000	0.000	0.000
13	A	16	ASP	-1	-0.761	-0.837	28.714	-10.019	-10.019	0.000	0.000	0.000	0.000
14	A	17	PHE	0	0.010	-0.002	29.407	0.188	0.188	0.000	0.000	0.000	0.000
15	A	18	THR	0	-0.032	-0.022	34.370	0.164	0.164	0.000	0.000	0.000	0.000
16	A	19	SER	0	-0.026	-0.019	37.329	0.148	0.148	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.771	-0.867	33.325	-9.392	-9.392	0.000	0.000	0.000	0.000
18	A	21	ASN	0	0.060	0.014	34.952	-0.284	-0.284	0.000	0.000	0.000	0.000
19	A	22	GLU	-1	-0.800	-0.886	35.270	-8.527	-8.527	0.000	0.000	0.000	0.000
20	A	23	LEU	0	0.029	0.016	29.718	-0.215	-0.215	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.948	-0.990	30.997	-9.245	-9.245	0.000	0.000	0.000	0.000
22	A	25	LEU	0	-0.041	-0.015	31.949	-0.151	-0.151	0.000	0.000	0.000	0.000
23	A	26	PHE	0	0.005	0.008	26.746	-0.179	-0.179	0.000	0.000	0.000	0.000
24	A	27	LEU	0	-0.014	-0.018	25.994	-0.306	-0.306	0.000	0.000	0.000	0.000
25	A	28	LYS	1	0.894	0.943	27.532	9.353	9.353	0.000	0.000	0.000	0.000
26	A	29	SER	0	0.020	0.009	29.649	0.282	0.282	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.046	-0.018	23.699	-0.176	-0.176	0.000	0.000	0.000	0.000
28	A	31	ASP	-1	-0.895	-0.941	24.302	-11.527	-11.527	0.000	0.000	0.000	0.000
29	A	32	GLU	-1	-0.882	-0.918	25.366	-9.681	-9.681	0.000	0.000	0.000	0.000
30	A	33	VAL	0	-0.087	-0.035	24.061	0.154	0.154	0.000	0.000	0.000	0.000
31	A	34	TRP	0	-0.003	-0.022	19.894	-0.392	-0.392	0.000	0.000	0.000	0.000
32	A	35	SER	0	0.063	0.043	21.231	-0.387	-0.387	0.000	0.000	0.000	0.000
33	A	36	GLU	-1	-0.851	-0.948	17.547	-16.844	-16.844	0.000	0.000	0.000	0.000
34	A	37	ASP	-1	-0.873	-0.900	18.299	-14.312	-14.312	0.000	0.000	0.000	0.000
35	A	38	LEU	0	0.024	0.023	19.790	-0.528	-0.528	0.000	0.000	0.000	0.000
36	A	39	TYR	0	-0.022	-0.043	15.182	-0.580	-0.580	0.000	0.000	0.000	0.000
37	A	40	SER	0	-0.035	0.006	15.030	-1.720	-1.720	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.729	0.793	15.545	12.728	12.728	0.000	0.000	0.000	0.000
39	A	42	LEU	0	-0.002	0.001	16.398	-0.180	-0.180	0.000	0.000	0.000	0.000
40	A	43	SER	0	-0.017	-0.019	11.153	-0.808	-0.808	0.000	0.000	0.000	0.000
41	A	44	ALA	0	-0.018	-0.006	12.122	-1.330	-1.330	0.000	0.000	0.000	0.000
42	A	45	ALA	0	-0.032	-0.010	13.951	0.230	0.230	0.000	0.000	0.000	0.000
43	A	46	GLY	0	0.054	0.018	12.167	0.759	0.759	0.000	0.000	0.000	0.000
44	A	47	LEU	0	-0.094	-0.053	12.049	-0.803	-0.803	0.000	0.000	0.000	0.000
45	A	48	ILE	0	0.014	0.021	6.376	-0.066	-0.066	0.000	0.000	0.000	0.000
46	A	49	ARG	1	0.923	0.957	6.614	29.156	29.156	0.000	0.000	0.000	0.000
47	A	50	HIS	0	0.030	0.024	10.969	1.054	1.054	0.000	0.000	0.000	0.000
48	A	51	VAL	0	-0.008	0.004	13.530	-0.187	-0.187	0.000	0.000	0.000	0.000
49	A	52	ILE	0	0.026	0.008	16.161	0.704	0.704	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.019	-0.008	19.942	0.104	0.104	0.000	0.000	0.000	0.000
51	A	54	LYS	1	0.909	0.954	21.985	10.093	10.093	0.000	0.000	0.000	0.000
52	A	55	VAL	0	-0.016	-0.009	24.091	-0.028	-0.028	0.000	0.000	0.000	0.000
53	A	56	TRP	0	0.032	0.015	22.072	0.383	0.383	0.000	0.000	0.000	0.000
54	A	57	ASN	0	-0.019	-0.022	28.417	0.339	0.339	0.000	0.000	0.000	0.000
55	A	58	LYS	1	0.893	0.949	31.013	8.695	8.695	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.874	-0.939	34.244	-8.359	-8.359	0.000	0.000	0.000	0.000
57	A	60	GLN	0	-0.051	-0.021	31.608	0.046	0.046	0.000	0.000	0.000	0.000
58	A	61	HIS	1	0.871	0.940	32.790	8.561	8.561	0.000	0.000	0.000	0.000
59	A	62	ARG	1	0.870	0.898	26.856	10.337	10.337	0.000	0.000	0.000	0.000
60	A	63	ILE	0	0.004	0.013	24.737	-0.176	-0.176	0.000	0.000	0.000	0.000
61	A	64	SER	0	-0.043	-0.028	21.950	-0.016	-0.016	0.000	0.000	0.000	0.000
62	A	65	MET	0	0.002	0.004	19.824	-0.110	-0.110	0.000	0.000	0.000	0.000
63	A	66	VAL	0	-0.014	0.008	14.566	0.429	0.429	0.000	0.000	0.000	0.000
64	A	67	PHE	0	-0.008	-0.002	15.242	-0.345	-0.345	0.000	0.000	0.000	0.000
65	A	68	GLU	-1	-0.862	-0.930	9.486	-25.612	-25.612	0.000	0.000	0.000	0.000
66	A	69	TYR	0	0.014	-0.015	11.926	-0.058	-0.058	0.000	0.000	0.000	0.000
67	A	70	ASP	-1	-0.736	-0.854	9.905	-25.045	-25.045	0.000	0.000	0.000	0.000
68	A	71	SER	0	-0.024	-0.029	11.066	1.461	1.461	0.000	0.000	0.000	0.000
69	A	72	LYS	1	0.879	0.924	14.520	14.407	14.407	0.000	0.000	0.000	0.000
70	A	73	GLU	-1	-0.855	-0.936	17.774	-13.947	-13.947	0.000	0.000	0.000	0.000
71	A	74	GLY	0	0.020	0.028	15.213	0.557	0.557	0.000	0.000	0.000	0.000
72	A	75	TYR	0	-0.018	-0.007	16.244	0.909	0.909	0.000	0.000	0.000	0.000
73	A	76	GLN	0	-0.038	-0.017	18.136	0.959	0.959	0.000	0.000	0.000	0.000
74	A	77	LYS	1	0.922	0.963	15.928	19.431	19.431	0.000	0.000	0.000	0.000
75	A	78	CYS	0	-0.016	0.008	16.850	0.156	0.156	0.000	0.000	0.000	0.000
76	A	79	GLN	0	-0.046	-0.031	19.561	0.266	0.266	0.000	0.000	0.000	0.000
77	A	80	GLU	-1	-0.874	-0.915	22.905	-11.085	-11.085	0.000	0.000	0.000	0.000
78	A	81	ILE	0	-0.008	-0.009	19.590	0.466	0.466	0.000	0.000	0.000	0.000
79	A	82	ILE	0	-0.016	-0.013	20.657	0.453	0.453	0.000	0.000	0.000	0.000
80	A	83	ASP	-1	-0.922	-0.952	24.432	-10.038	-10.038	0.000	0.000	0.000	0.000
81	A	84	LYS	1	0.751	0.842	26.848	11.344	11.344	0.000	0.000	0.000	0.000
82	A	85	GLU	-1	-0.826	-0.845	24.827	-12.412	-12.412	0.000	0.000	0.000	0.000
83	A	86	PHE	0	-0.041	-0.021	24.665	0.466	0.466	0.000	0.000	0.000	0.000
84	A	87	GLY	0	0.068	0.034	29.826	0.156	0.156	0.000	0.000	0.000	0.000
85	A	88	ILE	0	-0.035	-0.033	33.610	-0.067	-0.067	0.000	0.000	0.000	0.000
86	A	89	THR	0	0.036	0.006	34.426	0.109	0.109	0.000	0.000	0.000	0.000
87	A	90	LEU	0	0.060	0.046	28.675	0.107	0.107	0.000	0.000	0.000	0.000
88	A	91	LYS	1	0.938	0.971	32.917	9.133	9.133	0.000	0.000	0.000	0.000
89	A	92	GLU	-1	-0.841	-0.929	35.150	-7.543	-7.543	0.000	0.000	0.000	0.000
90	A	93	LYS	1	0.822	0.893	32.817	9.517	9.517	0.000	0.000	0.000	0.000
91	A	94	LEU	0	0.025	-0.006	30.252	0.068	0.068	0.000	0.000	0.000	0.000
92	A	95	LYS	1	0.826	0.914	34.418	7.709	7.709	0.000	0.000	0.000	0.000
93	A	96	LYS	1	0.898	0.960	36.498	8.610	8.610	0.000	0.000	0.000	0.000
94	A	97	PHE	0	-0.057	-0.008	33.709	0.060	0.060	0.000	0.000	0.000	0.000
95	A	98	VAL	0	-0.031	-0.015	36.761	0.058	0.058	0.000	0.000	0.000	0.000
96	A	99	PHE	0	0.024	0.009	29.775	-0.091	-0.091	0.000	0.000	0.000	0.000
97	A	100	LYS	1	0.933	0.964	31.822	8.958	8.958	0.000	0.000	0.000	0.000
98	A	101	ILE	0	0.020	0.012	26.376	-0.131	-0.131	0.000	0.000	0.000	0.000
99	A	102	HIS	0	-0.029	-0.009	27.768	0.375	0.375	0.000	0.000	0.000	0.000
100	A	103	ASN	0	-0.007	-0.015	24.353	-0.782	-0.782	0.000	0.000	0.000	0.000
101	A	104	ASN	0	-0.036	-0.017	21.828	0.720	0.720	0.000	0.000	0.000	0.000
102	A	105	ARG	1	0.942	0.979	20.222	12.108	12.108	0.000	0.000	0.000	0.000
103	A	106	GLY	0	-0.001	-0.003	18.900	0.766	0.766	0.000	0.000	0.000	0.000
104	A	107	VAL	0	-0.008	0.002	15.588	-0.680	-0.680	0.000	0.000	0.000	0.000
105	A	108	VAL	0	-0.015	0.005	11.049	1.166	1.166	0.000	0.000	0.000	0.000
106	A	109	VAL	0	-0.027	-0.017	13.711	-0.276	-0.276	0.000	0.000	0.000	0.000
107	A	110	SER	0	-0.027	-0.024	12.127	-0.366	-0.366	0.000	0.000	0.000	0.000
108	A	111	GLU	-1	-0.828	-0.909	6.030	-35.157	-35.157	0.000	0.000	0.000	0.000
109	A	112	PHE	0	-0.058	-0.029	8.375	-0.348	-0.348	0.000	0.000	0.000	0.000
111	A	114	ARG	1	0.878	0.938	6.063	23.096	23.096	0.000	0.000	0.000	0.000
112	A	115	SER	-1	-0.899	-0.940	6.047	-36.850	-36.850	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:THR)