FMO DATABASE

FMODB ID: N858Q

Calculation Name: 6X0B-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: 6X0B

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-04

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-972908.606146
FMO2-HF: Nuclear repulsion	926516.552815
FMO2-HF: Total energy	-46392.053331
FMO2-MP2: Total energy	-46525.269717

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:22:GLY)

Summations of interaction energy for fragment #1(A:22: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.
18.076	19.057	-0.014	-0.396	-0.571	-0.001

Interaction energy analysis for fragmet #1(A:22:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.844 / q_NPA : 0.910

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	24	SER	0	0.015	-0.004	3.841	1.682	2.663	-0.014	-0.396	-0.571	-0.001
4	A	25	SER	0	0.000	-0.014	7.166	0.033	0.033	0.000	0.000	0.000	0.000
5	A	26	GLU	-1	-0.822	-0.871	10.479	-23.901	-23.901	0.000	0.000	0.000	0.000
6	A	27	PRO	0	-0.015	-0.018	11.266	-1.801	-1.801	0.000	0.000	0.000	0.000
7	A	28	SER	0	-0.002	-0.018	10.277	0.943	0.943	0.000	0.000	0.000	0.000
8	A	29	ARG	1	0.916	0.953	12.426	16.451	16.451	0.000	0.000	0.000	0.000
9	A	30	VAL	0	0.004	0.015	10.641	0.900	0.900	0.000	0.000	0.000	0.000
10	A	31	ILE	0	-0.026	-0.004	10.116	-2.519	-2.519	0.000	0.000	0.000	0.000
11	A	32	ALA	0	-0.008	-0.005	8.472	1.053	1.053	0.000	0.000	0.000	0.000
12	A	33	PHE	0	-0.035	-0.023	10.558	-0.930	-0.930	0.000	0.000	0.000	0.000
13	A	34	HIS	1	0.852	0.892	7.918	30.307	30.307	0.000	0.000	0.000	0.000
14	A	35	SER	0	0.048	0.014	12.856	0.749	0.749	0.000	0.000	0.000	0.000
15	A	36	SER	0	0.057	0.008	16.550	-0.330	-0.330	0.000	0.000	0.000	0.000
16	A	37	ASN	0	0.008	0.006	19.712	0.850	0.850	0.000	0.000	0.000	0.000
17	A	38	ARG	1	0.882	0.952	14.959	17.974	17.974	0.000	0.000	0.000	0.000
18	A	39	TRP	0	0.066	0.034	17.799	-0.282	-0.282	0.000	0.000	0.000	0.000
19	A	40	GLN	0	0.020	0.013	18.773	0.667	0.667	0.000	0.000	0.000	0.000
20	A	41	LEU	0	-0.008	-0.008	21.010	0.553	0.553	0.000	0.000	0.000	0.000
21	A	42	HIS	0	-0.035	-0.022	18.391	0.119	0.119	0.000	0.000	0.000	0.000
22	A	43	PHE	0	0.035	0.021	20.938	0.538	0.538	0.000	0.000	0.000	0.000
23	A	44	ASN	0	0.045	0.018	23.404	0.790	0.790	0.000	0.000	0.000	0.000
24	A	45	SER	0	-0.010	0.001	23.456	0.543	0.543	0.000	0.000	0.000	0.000
25	A	46	SER	0	-0.064	-0.052	23.434	0.351	0.351	0.000	0.000	0.000	0.000
26	A	47	LYS	1	0.893	0.951	25.459	11.029	11.029	0.000	0.000	0.000	0.000
27	A	48	GLN	0	-0.039	-0.020	28.955	0.503	0.503	0.000	0.000	0.000	0.000
28	A	49	LEU	0	-0.016	0.003	25.054	0.158	0.158	0.000	0.000	0.000	0.000
29	A	50	ASN	0	0.021	0.002	28.863	-0.268	-0.268	0.000	0.000	0.000	0.000
30	A	51	LYS	1	0.911	0.960	20.833	13.981	13.981	0.000	0.000	0.000	0.000
31	A	52	LEU	0	-0.009	0.004	24.380	0.059	0.059	0.000	0.000	0.000	0.000
32	A	53	ILE	0	-0.005	-0.012	19.999	-0.483	-0.483	0.000	0.000	0.000	0.000
33	A	54	VAL	0	0.001	0.004	18.812	0.536	0.536	0.000	0.000	0.000	0.000
34	A	55	VAL	0	-0.021	-0.015	18.048	-0.816	-0.816	0.000	0.000	0.000	0.000
35	A	56	ASP	-1	-0.884	-0.952	13.860	-19.352	-19.352	0.000	0.000	0.000	0.000
36	A	57	PHE	0	0.011	0.005	15.576	-1.097	-1.097	0.000	0.000	0.000	0.000
37	A	58	ALA	0	0.048	-0.006	13.229	0.596	0.596	0.000	0.000	0.000	0.000
38	A	59	ALA	0	0.055	0.016	14.402	0.404	0.404	0.000	0.000	0.000	0.000
39	A	60	THR	0	-0.056	-0.028	9.746	-0.208	-0.208	0.000	0.000	0.000	0.000
40	A	61	TRP	0	-0.019	-0.021	11.816	-0.873	-0.873	0.000	0.000	0.000	0.000
41	A	62	CYS	0	-0.015	0.018	14.525	1.234	1.234	0.000	0.000	0.000	0.000
42	A	63	GLY	0	0.065	0.026	14.965	-0.774	-0.774	0.000	0.000	0.000	0.000
43	A	64	PRO	0	0.013	-0.019	16.046	-0.483	-0.483	0.000	0.000	0.000	0.000
44	A	65	CYS	0	-0.007	0.026	13.636	0.312	0.312	0.000	0.000	0.000	0.000
45	A	66	LYS	1	0.827	0.912	8.022	30.087	30.087	0.000	0.000	0.000	0.000
46	A	67	MET	0	-0.025	-0.012	12.869	-0.177	-0.177	0.000	0.000	0.000	0.000
47	A	68	MET	0	-0.004	0.014	15.408	0.681	0.681	0.000	0.000	0.000	0.000
48	A	69	GLU	-1	-0.805	-0.872	8.643	-31.014	-31.014	0.000	0.000	0.000	0.000
49	A	70	PRO	0	0.052	0.028	11.915	0.000	0.000	0.000	0.000	0.000	0.000
50	A	71	VAL	0	-0.009	-0.002	13.165	0.903	0.903	0.000	0.000	0.000	0.000
51	A	72	ILE	0	-0.002	-0.003	13.956	0.885	0.885	0.000	0.000	0.000	0.000
52	A	73	ASN	0	-0.040	-0.004	9.009	0.599	0.599	0.000	0.000	0.000	0.000
53	A	74	ALA	0	0.068	0.029	13.354	0.770	0.770	0.000	0.000	0.000	0.000
54	A	75	MET	0	-0.084	-0.035	16.704	0.948	0.948	0.000	0.000	0.000	0.000
55	A	76	SER	0	-0.018	-0.005	14.577	0.280	0.280	0.000	0.000	0.000	0.000
56	A	77	ALA	0	-0.013	-0.011	15.844	0.237	0.237	0.000	0.000	0.000	0.000
57	A	78	LYS	1	0.859	0.933	17.531	13.579	13.579	0.000	0.000	0.000	0.000
58	A	79	TYR	0	-0.075	-0.066	20.871	0.815	0.815	0.000	0.000	0.000	0.000
59	A	80	THR	0	-0.009	-0.013	19.398	-0.169	-0.169	0.000	0.000	0.000	0.000
60	A	81	ASP	-1	-0.790	-0.869	21.171	-12.326	-12.326	0.000	0.000	0.000	0.000
61	A	82	VAL	0	-0.061	-0.028	21.097	0.331	0.331	0.000	0.000	0.000	0.000
62	A	83	ASP	-1	-0.912	-0.954	17.930	-16.664	-16.664	0.000	0.000	0.000	0.000
63	A	84	PHE	0	0.019	0.012	15.347	0.383	0.383	0.000	0.000	0.000	0.000
64	A	85	VAL	0	0.019	0.017	14.619	-1.237	-1.237	0.000	0.000	0.000	0.000
65	A	86	LYS	1	0.869	0.929	8.286	29.145	29.145	0.000	0.000	0.000	0.000
66	A	87	ILE	0	-0.009	-0.011	13.283	-0.863	-0.863	0.000	0.000	0.000	0.000
67	A	88	ASP	-1	-0.812	-0.901	12.179	-21.689	-21.689	0.000	0.000	0.000	0.000
68	A	89	VAL	0	0.019	-0.026	14.219	0.721	0.721	0.000	0.000	0.000	0.000
69	A	90	ASP	-1	-0.849	-0.904	16.347	-16.150	-16.150	0.000	0.000	0.000	0.000
70	A	91	GLU	-1	-0.879	-0.919	11.717	-25.314	-25.314	0.000	0.000	0.000	0.000
71	A	92	LEU	0	-0.065	-0.034	15.213	0.570	0.570	0.000	0.000	0.000	0.000
72	A	93	SER	0	0.038	0.018	18.254	0.821	0.821	0.000	0.000	0.000	0.000
73	A	94	ASP	-1	-0.843	-0.892	21.080	-13.716	-13.716	0.000	0.000	0.000	0.000
74	A	95	VAL	0	0.008	-0.004	20.180	0.452	0.452	0.000	0.000	0.000	0.000
75	A	96	ALA	0	-0.003	-0.005	20.267	0.326	0.326	0.000	0.000	0.000	0.000
76	A	97	GLN	0	-0.037	-0.011	22.136	0.845	0.845	0.000	0.000	0.000	0.000
77	A	98	GLU	-1	-0.940	-0.960	25.217	-11.660	-11.660	0.000	0.000	0.000	0.000
78	A	99	PHE	0	-0.011	-0.011	23.766	0.399	0.399	0.000	0.000	0.000	0.000
79	A	100	GLY	0	0.018	0.017	26.097	0.128	0.128	0.000	0.000	0.000	0.000
80	A	101	VAL	0	-0.050	-0.034	21.068	0.152	0.152	0.000	0.000	0.000	0.000
81	A	102	GLN	0	-0.018	-0.009	24.464	0.139	0.139	0.000	0.000	0.000	0.000
82	A	103	ALA	0	-0.008	-0.001	23.263	0.058	0.058	0.000	0.000	0.000	0.000
83	A	104	MET	0	0.010	0.038	17.880	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	105	PRO	0	0.016	-0.017	16.884	0.149	0.149	0.000	0.000	0.000	0.000
85	A	106	THR	0	-0.026	-0.026	18.744	1.145	1.145	0.000	0.000	0.000	0.000
86	A	107	PHE	0	-0.020	-0.011	16.632	-0.521	-0.521	0.000	0.000	0.000	0.000
87	A	108	LEU	0	0.015	0.021	21.111	0.735	0.735	0.000	0.000	0.000	0.000
88	A	109	LEU	0	-0.022	-0.009	22.395	-0.478	-0.478	0.000	0.000	0.000	0.000
89	A	110	LEU	0	0.026	0.005	22.935	0.518	0.518	0.000	0.000	0.000	0.000
90	A	111	LYS	1	0.885	0.945	25.718	9.988	9.988	0.000	0.000	0.000	0.000
91	A	112	GLN	0	0.004	0.018	28.247	0.392	0.392	0.000	0.000	0.000	0.000
92	A	113	GLY	0	0.003	0.010	27.974	0.268	0.268	0.000	0.000	0.000	0.000
93	A	114	LYS	1	0.918	0.959	28.992	9.151	9.151	0.000	0.000	0.000	0.000
94	A	115	GLU	-1	-0.771	-0.856	28.048	-11.268	-11.268	0.000	0.000	0.000	0.000
95	A	116	VAL	0	-0.050	-0.027	28.397	0.402	0.402	0.000	0.000	0.000	0.000
96	A	117	GLU	-1	-0.806	-0.880	27.717	-9.507	-9.507	0.000	0.000	0.000	0.000
97	A	118	ARG	1	0.808	0.879	25.318	11.085	11.085	0.000	0.000	0.000	0.000
98	A	119	VAL	0	-0.049	-0.004	23.605	0.440	0.440	0.000	0.000	0.000	0.000
99	A	120	VAL	0	0.039	0.022	23.641	-0.416	-0.416	0.000	0.000	0.000	0.000
100	A	121	GLY	0	0.046	0.021	22.532	0.539	0.539	0.000	0.000	0.000	0.000
101	A	122	ALA	0	0.001	-0.014	19.770	-0.211	-0.211	0.000	0.000	0.000	0.000
102	A	123	LYS	1	0.855	0.935	21.048	11.478	11.478	0.000	0.000	0.000	0.000
103	A	124	LYS	1	0.921	0.957	21.610	12.740	12.740	0.000	0.000	0.000	0.000
104	A	125	ASP	-1	-0.808	-0.911	22.757	-11.574	-11.574	0.000	0.000	0.000	0.000
105	A	126	GLU	-1	-0.837	-0.916	26.362	-10.641	-10.641	0.000	0.000	0.000	0.000
106	A	127	LEU	0	0.025	0.017	20.030	0.257	0.257	0.000	0.000	0.000	0.000
107	A	128	GLU	-1	-0.771	-0.863	24.090	-12.549	-12.549	0.000	0.000	0.000	0.000
108	A	129	LYS	1	0.959	0.978	25.202	9.484	9.484	0.000	0.000	0.000	0.000
109	A	130	LYS	1	0.770	0.872	26.832	10.965	10.965	0.000	0.000	0.000	0.000
110	A	131	ILE	0	0.030	0.009	21.656	0.139	0.139	0.000	0.000	0.000	0.000
111	A	132	LEU	0	-0.022	-0.016	26.140	0.240	0.240	0.000	0.000	0.000	0.000
112	A	133	LYS	1	0.822	0.904	28.953	9.497	9.497	0.000	0.000	0.000	0.000
113	A	134	HIS	1	0.844	0.901	28.715	10.216	10.216	0.000	0.000	0.000	0.000
114	A	135	ARG	1	0.869	0.915	25.830	11.261	11.261	0.000	0.000	0.000	0.000
115	A	136	GLU	-1	-0.945	-0.965	28.321	-9.462	-9.462	0.000	0.000	0.000	0.000
116	A	137	ALA	-1	-0.952	-0.976	31.674	-8.854	-8.854	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:GLY)