FMO DATABASE

FMODB ID: 9RLL2

Calculation Name: 2EWC-A-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol

Ligand 3-letter code: GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EWC

Chain ID: A

ChEMBL ID:

UniProt ID: Q99XS4

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	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1017618.983203
FMO2-HF: Nuclear repulsion	968862.673473
FMO2-HF: Total energy	-48756.30973
FMO2-MP2: Total energy	-48896.443116

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:3:THR)

Summations of interaction energy for fragment #1(A:3: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.
-27.1	-24.547	0.238	-0.825	-1.964	-0.003

Interaction energy analysis for fragmet #1(A:3:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.830 / q_NPA : 0.903

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	5	ARG	1	0.919	0.983	2.601	45.389	47.836	0.239	-0.813	-1.872	-0.003
4	A	6	ARG	1	0.969	0.982	4.929	35.055	35.161	-0.001	-0.012	-0.092	0.000
5	A	7	TYR	0	0.018	-0.012	7.226	0.016	0.016	0.000	0.000	0.000	0.000
6	A	8	ASP	-1	-0.734	-0.845	11.499	-15.442	-15.442	0.000	0.000	0.000	0.000
7	A	9	VAL	0	0.001	0.011	11.317	0.265	0.265	0.000	0.000	0.000	0.000
8	A	10	ASN	0	-0.004	-0.006	14.413	1.142	1.142	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.863	-0.942	14.645	-17.859	-17.859	0.000	0.000	0.000	0.000
10	A	12	ASP	-1	-0.931	-0.951	18.180	-12.332	-12.332	0.000	0.000	0.000	0.000
11	A	13	ARG	1	0.809	0.894	20.653	12.599	12.599	0.000	0.000	0.000	0.000
12	A	14	GLY	0	0.020	0.035	17.762	0.013	0.013	0.000	0.000	0.000	0.000
13	A	15	HIS	0	-0.020	-0.014	15.994	-1.136	-1.136	0.000	0.000	0.000	0.000
14	A	16	THR	0	-0.048	-0.047	10.852	-1.364	-1.364	0.000	0.000	0.000	0.000
15	A	17	GLY	0	0.019	0.016	14.277	-0.184	-0.184	0.000	0.000	0.000	0.000
16	A	18	LEU	0	0.016	0.007	11.546	0.463	0.463	0.000	0.000	0.000	0.000
17	A	19	VAL	0	-0.021	-0.011	8.629	-1.839	-1.839	0.000	0.000	0.000	0.000
18	A	20	GLU	-1	-0.816	-0.886	6.187	-34.504	-34.504	0.000	0.000	0.000	0.000
19	A	21	ALA	0	-0.036	-0.041	6.214	-7.738	-7.738	0.000	0.000	0.000	0.000
20	A	22	GLY	0	-0.010	-0.001	5.875	3.689	3.689	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.760	-0.864	7.376	-25.705	-25.705	0.000	0.000	0.000	0.000
22	A	24	PHE	0	-0.013	0.000	10.308	2.541	2.541	0.000	0.000	0.000	0.000
23	A	25	TYR	0	-0.009	-0.010	9.299	-2.921	-2.921	0.000	0.000	0.000	0.000
24	A	26	TYR	0	-0.005	-0.002	11.527	2.261	2.261	0.000	0.000	0.000	0.000
25	A	27	LEU	0	0.027	0.009	13.917	-0.891	-0.891	0.000	0.000	0.000	0.000
26	A	28	ASN	0	-0.034	-0.017	16.641	0.132	0.132	0.000	0.000	0.000	0.000
27	A	29	TYR	0	0.037	0.022	18.522	0.222	0.222	0.000	0.000	0.000	0.000
28	A	30	CYS	0	-0.080	0.001	20.924	-0.465	-0.465	0.000	0.000	0.000	0.000
29	A	31	VAL	0	-0.036	-0.036	23.176	0.542	0.542	0.000	0.000	0.000	0.000
30	A	32	GLY	0	0.069	0.032	26.108	-0.260	-0.260	0.000	0.000	0.000	0.000
31	A	33	ASN	0	-0.050	-0.029	28.755	0.154	0.154	0.000	0.000	0.000	0.000
32	A	34	VAL	0	0.007	0.005	30.548	0.238	0.238	0.000	0.000	0.000	0.000
33	A	35	GLY	0	-0.007	0.009	33.321	0.150	0.150	0.000	0.000	0.000	0.000
34	A	36	GLN	0	-0.009	-0.011	35.352	0.152	0.152	0.000	0.000	0.000	0.000
35	A	37	ASP	-1	-0.820	-0.887	37.802	-8.080	-8.080	0.000	0.000	0.000	0.000
36	A	38	ILE	0	0.045	0.010	35.080	-0.246	-0.246	0.000	0.000	0.000	0.000
37	A	39	GLU	-1	-0.804	-0.893	35.313	-8.294	-8.294	0.000	0.000	0.000	0.000
38	A	40	SER	0	-0.008	-0.021	34.767	-0.252	-0.252	0.000	0.000	0.000	0.000
39	A	41	GLN	0	-0.010	-0.017	32.391	-0.512	-0.512	0.000	0.000	0.000	0.000
40	A	42	ILE	0	-0.018	-0.004	30.737	-0.370	-0.370	0.000	0.000	0.000	0.000
41	A	43	ASN	0	-0.010	-0.025	29.807	-0.536	-0.536	0.000	0.000	0.000	0.000
42	A	44	GLY	0	0.049	0.028	28.894	-0.321	-0.321	0.000	0.000	0.000	0.000
43	A	45	ALA	0	-0.038	-0.018	26.372	-0.427	-0.427	0.000	0.000	0.000	0.000
44	A	46	PHE	0	0.010	-0.015	24.876	-0.559	-0.559	0.000	0.000	0.000	0.000
45	A	47	ASP	-1	-0.789	-0.877	24.629	-11.030	-11.030	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.842	-0.914	21.445	-14.005	-14.005	0.000	0.000	0.000	0.000
47	A	49	MET	0	0.001	-0.002	20.510	-0.654	-0.654	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.843	-0.922	19.803	-12.753	-12.753	0.000	0.000	0.000	0.000
49	A	51	ARG	1	0.746	0.843	18.917	13.988	13.988	0.000	0.000	0.000	0.000
50	A	52	ARG	1	0.780	0.858	16.471	14.667	14.667	0.000	0.000	0.000	0.000
51	A	53	LEU	0	-0.005	-0.001	15.578	-1.219	-1.219	0.000	0.000	0.000	0.000
52	A	54	ALA	0	0.041	0.026	15.977	-0.746	-0.746	0.000	0.000	0.000	0.000
53	A	55	LEU	0	-0.088	-0.039	13.603	-0.254	-0.254	0.000	0.000	0.000	0.000
54	A	56	VAL	0	-0.064	-0.031	10.306	-1.400	-1.400	0.000	0.000	0.000	0.000
55	A	57	GLY	0	-0.027	-0.004	12.868	-0.250	-0.250	0.000	0.000	0.000	0.000
56	A	58	LEU	0	-0.062	-0.022	13.728	0.498	0.498	0.000	0.000	0.000	0.000
57	A	59	THR	0	0.013	-0.010	17.393	0.206	0.206	0.000	0.000	0.000	0.000
58	A	60	LEU	0	0.046	0.005	20.314	-0.624	-0.624	0.000	0.000	0.000	0.000
59	A	61	ASP	-1	-0.900	-0.937	22.473	-12.435	-12.435	0.000	0.000	0.000	0.000
60	A	62	ALA	0	-0.017	0.004	17.381	-0.131	-0.131	0.000	0.000	0.000	0.000
61	A	63	VAL	0	-0.018	-0.013	18.800	-0.894	-0.894	0.000	0.000	0.000	0.000
62	A	64	VAL	0	-0.014	-0.007	18.731	0.658	0.658	0.000	0.000	0.000	0.000
63	A	65	GLN	0	-0.092	-0.071	20.919	0.199	0.199	0.000	0.000	0.000	0.000
64	A	66	MET	0	0.019	0.019	21.594	-0.505	-0.505	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.772	-0.841	23.896	-12.415	-12.415	0.000	0.000	0.000	0.000
66	A	68	CYS	0	-0.084	-0.047	25.891	-0.121	-0.121	0.000	0.000	0.000	0.000
67	A	69	LEU	0	0.019	0.013	26.917	0.360	0.360	0.000	0.000	0.000	0.000
68	A	70	PHE	0	0.030	-0.005	30.175	0.036	0.036	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.831	0.902	33.712	8.738	8.738	0.000	0.000	0.000	0.000
70	A	72	ASP	-1	-0.866	-0.941	36.383	-7.646	-7.646	0.000	0.000	0.000	0.000
71	A	73	VAL	0	0.015	0.003	35.384	-0.109	-0.109	0.000	0.000	0.000	0.000
72	A	74	TRP	0	-0.022	-0.010	37.614	-0.032	-0.032	0.000	0.000	0.000	0.000
73	A	75	ASN	0	-0.037	-0.027	37.377	0.199	0.199	0.000	0.000	0.000	0.000
74	A	76	ILE	0	0.008	0.015	34.807	-0.147	-0.147	0.000	0.000	0.000	0.000
75	A	77	PRO	0	0.017	-0.002	36.378	-0.151	-0.151	0.000	0.000	0.000	0.000
76	A	78	VAL	0	0.005	0.014	36.919	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	79	MET	0	0.026	0.038	31.241	-0.247	-0.247	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.884	-0.938	33.395	-8.934	-8.934	0.000	0.000	0.000	0.000
79	A	81	LYS	1	0.803	0.902	35.196	7.815	7.815	0.000	0.000	0.000	0.000
80	A	82	MET	0	0.028	0.038	32.770	-0.106	-0.106	0.000	0.000	0.000	0.000
81	A	83	ILE	0	-0.016	-0.004	29.522	-0.213	-0.213	0.000	0.000	0.000	0.000
82	A	84	LYS	1	0.890	0.938	31.552	8.323	8.323	0.000	0.000	0.000	0.000
83	A	85	GLU	-1	-0.944	-0.969	34.147	-8.527	-8.527	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.762	0.856	27.318	10.626	10.626	0.000	0.000	0.000	0.000
85	A	87	PHE	0	0.014	-0.009	24.574	-0.252	-0.252	0.000	0.000	0.000	0.000
86	A	88	ASN	0	-0.012	0.008	28.846	0.113	0.113	0.000	0.000	0.000	0.000
87	A	89	GLY	0	-0.005	-0.003	30.881	-0.012	-0.012	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.875	0.938	25.967	11.335	11.335	0.000	0.000	0.000	0.000
89	A	91	TYR	0	0.021	0.006	26.914	-0.159	-0.159	0.000	0.000	0.000	0.000
90	A	92	PRO	0	0.016	0.030	23.825	-0.021	-0.021	0.000	0.000	0.000	0.000
91	A	93	ALA	0	-0.026	-0.008	25.149	0.559	0.559	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.883	0.913	25.664	9.497	9.497	0.000	0.000	0.000	0.000
93	A	95	LYS	1	0.813	0.903	24.726	12.978	12.978	0.000	0.000	0.000	0.000
94	A	96	SER	0	-0.039	-0.038	29.353	-0.097	-0.097	0.000	0.000	0.000	0.000
95	A	97	ILE	0	0.016	0.012	28.640	0.218	0.218	0.000	0.000	0.000	0.000
96	A	98	GLN	0	0.026	0.021	32.586	-0.012	-0.012	0.000	0.000	0.000	0.000
97	A	99	THR	0	-0.045	-0.045	30.625	-0.072	-0.072	0.000	0.000	0.000	0.000
98	A	100	GLU	-1	-0.871	-0.922	33.941	-8.293	-8.293	0.000	0.000	0.000	0.000
99	A	101	PHE	0	0.000	0.001	29.363	-0.349	-0.349	0.000	0.000	0.000	0.000
100	A	102	ALA	0	-0.015	0.000	29.818	0.287	0.287	0.000	0.000	0.000	0.000
101	A	103	HIS	0	-0.029	-0.035	31.890	-0.184	-0.184	0.000	0.000	0.000	0.000
102	A	104	HIS	0	-0.016	0.018	33.910	-0.038	-0.038	0.000	0.000	0.000	0.000
103	A	105	GLY	0	0.080	0.040	36.866	-0.204	-0.204	0.000	0.000	0.000	0.000
104	A	106	GLY	0	0.012	0.000	39.191	0.093	0.093	0.000	0.000	0.000	0.000
105	A	107	PRO	0	0.014	-0.005	41.252	-0.142	-0.142	0.000	0.000	0.000	0.000
106	A	108	GLN	0	0.004	0.004	38.902	0.041	0.041	0.000	0.000	0.000	0.000
107	A	109	GLY	0	-0.003	0.022	37.509	-0.197	-0.197	0.000	0.000	0.000	0.000
108	A	110	LEU	0	-0.006	0.013	30.127	-0.043	-0.043	0.000	0.000	0.000	0.000
109	A	111	LEU	0	-0.043	-0.029	34.274	0.166	0.166	0.000	0.000	0.000	0.000
110	A	112	PHE	0	0.026	-0.002	28.890	0.048	0.048	0.000	0.000	0.000	0.000
111	A	113	GLN	0	-0.003	0.004	26.512	-0.304	-0.304	0.000	0.000	0.000	0.000
112	A	114	VAL	0	0.012	0.013	24.264	0.255	0.255	0.000	0.000	0.000	0.000
113	A	115	ASP	-1	-0.834	-0.911	20.796	-14.603	-14.603	0.000	0.000	0.000	0.000
114	A	116	GLY	0	0.038	0.001	19.892	0.523	0.523	0.000	0.000	0.000	0.000
115	A	117	VAL	0	-0.071	-0.020	15.659	-1.147	-1.147	0.000	0.000	0.000	0.000
116	A	118	ALA	0	0.031	0.015	15.891	1.098	1.098	0.000	0.000	0.000	0.000
117	A	119	TYR	0	-0.066	-0.042	14.500	-1.232	-1.232	0.000	0.000	0.000	0.000
118	A	120	SER	0	0.025	0.002	13.187	1.378	1.378	0.000	0.000	0.000	0.000
119	A	121	LYS	1	0.782	0.896	12.867	20.735	20.735	0.000	0.000	0.000	0.000
120	A	122	HIS	0	-0.048	-0.028	8.195	7.390	7.390	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:THR)