FMO DATABASE

FMODB ID: ML9RZ

Calculation Name: 2B4A-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: 2B4A

Chain ID: A

ChEMBL ID:

UniProt ID: Q9K8I2

Base Structure: X-ray

Registration Date: 2025-10-05

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	118
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-992543.470565
FMO2-HF: Nuclear repulsion	946747.315129
FMO2-HF: Total energy	-45796.155436
FMO2-MP2: Total energy	-45932.68215

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:GLN)

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

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.
-176.977	-168.975	5.651	-6.076	-7.575	-0.074

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.789 / q_NPA : 0.895

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	PHE	0	0.065	0.033	2.406	-17.415	-14.209	2.989	-2.740	-3.455	-0.030
4	A	5	ARG	1	0.785	0.870	3.433	35.956	36.201	0.000	-0.035	-0.209	0.000
5	A	6	VAL	0	0.022	0.004	5.326	1.455	1.508	-0.001	0.001	-0.052	0.000
49	A	50	ASP	-1	-0.800	-0.891	2.298	-72.424	-68.714	2.619	-3.114	-3.215	-0.045
50	A	51	LEU	0	-0.017	-0.007	5.253	3.503	3.536	-0.001	-0.001	-0.031	0.000
117	A	118	PRO	0	-0.002	0.002	3.448	0.289	1.044	0.045	-0.187	-0.613	0.001
6	A	7	THR	0	-0.025	-0.023	8.631	1.479	1.479	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.026	-0.002	11.711	0.214	0.214	0.000	0.000	0.000	0.000
8	A	9	VAL	0	-0.023	-0.010	15.145	0.321	0.321	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.809	-0.903	18.404	-12.306	-12.306	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.815	-0.901	21.406	-11.421	-11.421	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.899	-0.938	24.688	-9.964	-9.964	0.000	0.000	0.000	0.000
12	A	13	PRO	0	0.009	-0.003	24.584	-0.520	-0.520	0.000	0.000	0.000	0.000
13	A	14	SER	0	-0.002	0.006	24.449	-0.526	-0.526	0.000	0.000	0.000	0.000
14	A	15	HIS	0	0.040	0.021	23.597	-0.506	-0.506	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.041	0.016	20.373	-0.635	-0.635	0.000	0.000	0.000	0.000
16	A	17	THR	0	-0.019	-0.033	19.622	-0.744	-0.744	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.014	0.008	20.739	-0.607	-0.607	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.028	-0.001	16.273	-0.611	-0.611	0.000	0.000	0.000	0.000
19	A	20	GLN	0	0.027	0.013	15.933	-0.359	-0.359	0.000	0.000	0.000	0.000
20	A	21	TYR	0	-0.036	-0.015	16.284	-1.074	-1.074	0.000	0.000	0.000	0.000
21	A	22	HIS	0	0.041	0.005	17.613	-1.140	-1.140	0.000	0.000	0.000	0.000
22	A	23	LEU	0	0.033	0.027	11.393	-0.854	-0.854	0.000	0.000	0.000	0.000
23	A	24	ASN	0	0.010	0.006	12.777	-2.860	-2.860	0.000	0.000	0.000	0.000
24	A	25	GLN	0	-0.099	-0.045	14.508	-1.114	-1.114	0.000	0.000	0.000	0.000
25	A	26	LEU	0	-0.028	-0.006	12.827	0.667	0.667	0.000	0.000	0.000	0.000
26	A	27	GLY	0	-0.009	0.000	10.246	-2.008	-2.008	0.000	0.000	0.000	0.000
27	A	28	ALA	0	-0.013	0.002	8.075	-4.444	-4.444	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.884	-0.910	7.439	-28.102	-28.102	0.000	0.000	0.000	0.000
29	A	30	VAL	0	0.015	-0.001	8.614	-0.522	-0.522	0.000	0.000	0.000	0.000
30	A	31	THR	0	-0.012	0.003	11.326	1.468	1.468	0.000	0.000	0.000	0.000
31	A	32	VAL	0	-0.005	-0.010	13.097	0.021	0.021	0.000	0.000	0.000	0.000
32	A	33	HIS	0	0.016	0.009	14.909	1.087	1.087	0.000	0.000	0.000	0.000
33	A	34	PRO	0	-0.015	-0.015	18.829	0.161	0.161	0.000	0.000	0.000	0.000
34	A	35	SER	0	0.027	0.006	21.811	0.599	0.599	0.000	0.000	0.000	0.000
35	A	36	GLY	0	0.053	0.013	21.730	-0.630	-0.630	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.055	-0.058	22.418	-0.183	-0.183	0.000	0.000	0.000	0.000
37	A	38	ALA	0	-0.047	-0.019	20.955	-0.107	-0.107	0.000	0.000	0.000	0.000
38	A	39	PHE	0	0.069	0.032	15.532	-0.514	-0.514	0.000	0.000	0.000	0.000
39	A	40	PHE	0	0.020	0.013	18.682	-0.366	-0.366	0.000	0.000	0.000	0.000
40	A	41	GLN	0	-0.084	-0.049	21.073	-0.105	-0.105	0.000	0.000	0.000	0.000
41	A	42	HIS	0	-0.054	-0.035	16.121	-0.146	-0.146	0.000	0.000	0.000	0.000
42	A	43	ARG	1	0.919	0.981	15.718	11.602	11.602	0.000	0.000	0.000	0.000
43	A	44	SER	0	0.056	0.030	14.759	-0.882	-0.882	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.009	-0.010	12.048	-1.521	-1.521	0.000	0.000	0.000	0.000
45	A	46	LEU	0	0.034	0.027	10.372	-2.235	-2.235	0.000	0.000	0.000	0.000
46	A	47	SER	0	0.009	0.007	9.207	-1.254	-1.254	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.115	-0.071	6.695	-1.250	-1.250	0.000	0.000	0.000	0.000
48	A	49	CYS	0	-0.067	0.000	5.616	-4.393	-4.393	0.000	0.000	0.000	0.000
51	A	52	LEU	0	0.009	-0.002	8.925	-0.175	-0.175	0.000	0.000	0.000	0.000
52	A	53	ILE	0	0.002	0.002	12.162	1.014	1.014	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.013	-0.005	15.001	0.134	0.134	0.000	0.000	0.000	0.000
54	A	55	SER	0	-0.006	-0.013	18.376	0.362	0.362	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.844	-0.908	22.038	-11.203	-11.203	0.000	0.000	0.000	0.000
56	A	57	GLN	0	-0.064	-0.040	24.192	0.348	0.348	0.000	0.000	0.000	0.000
57	A	58	LEU	0	-0.002	0.016	21.570	0.138	0.138	0.000	0.000	0.000	0.000
58	A	59	VAL	0	-0.042	-0.029	26.129	0.304	0.304	0.000	0.000	0.000	0.000
59	A	60	ASP	-1	-0.799	-0.870	26.048	-10.902	-10.902	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.045	-0.015	22.244	0.003	0.003	0.000	0.000	0.000	0.000
61	A	62	SER	0	0.043	0.033	25.446	-0.270	-0.270	0.000	0.000	0.000	0.000
62	A	63	ILE	0	0.072	0.034	20.541	-0.242	-0.242	0.000	0.000	0.000	0.000
63	A	64	PHE	0	0.032	0.006	22.602	-0.380	-0.380	0.000	0.000	0.000	0.000
64	A	65	SER	0	0.027	0.004	23.610	-0.114	-0.114	0.000	0.000	0.000	0.000
65	A	66	LEU	0	-0.042	-0.008	17.899	-0.273	-0.273	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.059	0.012	18.124	-0.648	-0.648	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.889	-0.917	19.745	-11.503	-11.503	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.015	-0.009	18.562	-0.217	-0.217	0.000	0.000	0.000	0.000
69	A	70	VAL	0	-0.036	-0.028	14.319	-0.620	-0.620	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.887	0.931	16.046	11.699	11.699	0.000	0.000	0.000	0.000
71	A	72	GLU	-1	-0.968	-0.973	18.400	-12.161	-12.161	0.000	0.000	0.000	0.000
72	A	73	GLN	0	-0.094	-0.042	13.855	-0.339	-0.339	0.000	0.000	0.000	0.000
73	A	74	THR	0	-0.016	-0.017	14.707	-0.391	-0.391	0.000	0.000	0.000	0.000
74	A	75	LYS	1	0.792	0.895	6.080	27.239	27.239	0.000	0.000	0.000	0.000
75	A	76	GLN	0	0.026	0.004	10.823	-0.715	-0.715	0.000	0.000	0.000	0.000
76	A	77	PRO	0	-0.039	-0.001	8.293	-1.451	-1.451	0.000	0.000	0.000	0.000
77	A	78	SER	0	0.059	0.028	8.782	2.259	2.259	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.018	-0.012	10.752	-0.667	-0.667	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.005	-0.002	13.909	0.336	0.336	0.000	0.000	0.000	0.000
80	A	81	ILE	0	0.013	0.006	15.977	0.043	0.043	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.028	-0.018	18.664	0.285	0.285	0.000	0.000	0.000	0.000
82	A	83	THR	0	0.053	-0.002	21.686	0.537	0.537	0.000	0.000	0.000	0.000
83	A	84	THR	0	-0.048	-0.043	25.015	0.056	0.056	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.034	0.029	28.718	0.375	0.375	0.000	0.000	0.000	0.000
85	A	86	ARG	1	0.828	0.906	29.783	9.272	9.272	0.000	0.000	0.000	0.000
86	A	87	HIS	0	-0.002	0.007	29.337	-0.087	-0.087	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.883	-0.945	26.925	-9.558	-9.558	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.097	-0.048	24.980	-0.284	-0.284	0.000	0.000	0.000	0.000
89	A	90	ILE	0	0.000	0.009	23.312	0.324	0.324	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.909	-0.958	23.845	-10.746	-10.746	0.000	0.000	0.000	0.000
91	A	92	SER	0	-0.055	-0.051	19.849	-0.088	-0.088	0.000	0.000	0.000	0.000
92	A	93	SER	0	-0.008	0.003	22.470	0.089	0.089	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.905	-0.931	17.081	-13.894	-13.894	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.015	-0.013	16.654	0.026	0.026	0.000	0.000	0.000	0.000
95	A	96	ASN	0	-0.018	-0.009	12.973	0.344	0.344	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.001	0.009	14.669	-0.730	-0.730	0.000	0.000	0.000	0.000
97	A	98	SER	0	0.015	0.002	15.018	0.841	0.841	0.000	0.000	0.000	0.000
98	A	99	TYR	0	0.010	0.004	17.570	0.099	0.099	0.000	0.000	0.000	0.000
99	A	100	LEU	0	-0.022	-0.010	19.676	-0.224	-0.224	0.000	0.000	0.000	0.000
100	A	101	GLN	0	-0.021	-0.001	21.828	0.350	0.350	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.841	0.933	23.918	11.853	11.853	0.000	0.000	0.000	0.000
102	A	103	PRO	0	-0.049	-0.045	26.653	0.325	0.325	0.000	0.000	0.000	0.000
103	A	104	PHE	0	0.085	0.047	21.960	0.047	0.047	0.000	0.000	0.000	0.000
104	A	105	ALA	0	-0.028	-0.015	25.920	0.085	0.085	0.000	0.000	0.000	0.000
105	A	106	ILE	0	-0.005	-0.021	21.960	-0.522	-0.522	0.000	0.000	0.000	0.000
106	A	107	SER	0	-0.003	-0.007	21.420	-0.695	-0.695	0.000	0.000	0.000	0.000
107	A	108	GLU	-1	-0.827	-0.908	21.065	-12.728	-12.728	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.004	0.010	17.833	-0.686	-0.686	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.859	0.912	16.959	16.652	16.652	0.000	0.000	0.000	0.000
110	A	111	ALA	0	0.021	0.017	16.126	-1.217	-1.217	0.000	0.000	0.000	0.000
111	A	112	ALA	0	0.015	0.013	16.141	-0.830	-0.830	0.000	0.000	0.000	0.000
112	A	113	ILE	0	-0.032	-0.014	11.743	-0.988	-0.988	0.000	0.000	0.000	0.000
113	A	114	ASP	-1	-0.879	-0.938	11.582	-26.346	-26.346	0.000	0.000	0.000	0.000
114	A	115	TYR	0	-0.026	-0.027	11.855	-1.091	-1.091	0.000	0.000	0.000	0.000
115	A	116	HIS	0	0.000	0.005	9.687	1.527	1.527	0.000	0.000	0.000	0.000
116	A	117	LYS	1	0.767	0.892	7.365	27.201	27.201	0.000	0.000	0.000	0.000
118	A	119	SER	-1	-0.984	-0.979	6.052	-33.239	-33.239	0.000	0.000	0.000	0.000

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