FMO DATABASE

FMODB ID: LQ279

Calculation Name: 2F2E-A-Xray547

Preferred Name:

Target Type:

Ligand Name: alpha-d-glucopyranose

Ligand 3-letter code: GLC

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F2E

Chain ID: A

ChEMBL ID:

UniProt ID: Q9I3B4

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	142
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1134195.264385
FMO2-HF: Nuclear repulsion	1079554.467231
FMO2-HF: Total energy	-54640.797154
FMO2-MP2: Total energy	-54801.474856

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:5:THR)

Summations of interaction energy for fragment #1(A:5: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.
-37.146	-31.742	22.247	-14.478	-13.171	-0.1

Interaction energy analysis for fragmet #1(A:5:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.776 / q_NPA : 0.859

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	7	HIS	0	0.041	0.020	3.411	11.242	13.992	-0.017	-1.293	-1.439	-0.004
4	A	8	LYS	1	0.934	0.979	2.192	47.974	48.435	1.759	-0.622	-1.598	0.000
5	A	9	GLN	0	0.014	-0.011	4.304	4.347	4.518	0.001	-0.035	-0.137	0.000
15	A	19	ASP	-1	-0.804	-0.893	2.163	-96.865	-96.887	13.506	-8.435	-5.049	-0.054
16	A	20	VAL	0	-0.089	-0.040	3.547	-4.641	-3.901	0.005	-0.224	-0.521	-0.002
56	A	60	ASN	0	0.001	0.006	3.547	-1.395	-1.195	0.000	-0.042	-0.157	0.000
60	A	64	HIS	0	-0.023	-0.009	2.039	-25.284	-24.180	6.993	-3.827	-4.270	-0.040
6	A	10	ALA	0	0.014	0.026	7.671	3.475	3.475	0.000	0.000	0.000	0.000
7	A	11	SER	0	0.025	0.009	9.830	-0.200	-0.200	0.000	0.000	0.000	0.000
8	A	12	CYS	0	0.002	0.021	12.161	1.192	1.192	0.000	0.000	0.000	0.000
9	A	13	PRO	0	0.054	0.012	11.232	-2.299	-2.299	0.000	0.000	0.000	0.000
10	A	14	VAL	0	0.050	0.014	11.516	-1.030	-1.030	0.000	0.000	0.000	0.000
11	A	15	ALA	0	0.013	0.008	8.794	-1.064	-1.064	0.000	0.000	0.000	0.000
12	A	16	ARG	1	0.870	0.928	6.092	24.483	24.483	0.000	0.000	0.000	0.000
13	A	17	PRO	0	0.036	0.011	5.557	-5.496	-5.496	0.000	0.000	0.000	0.000
14	A	18	LEU	0	0.034	0.021	7.061	-1.266	-1.266	0.000	0.000	0.000	0.000
17	A	21	ILE	0	0.009	-0.009	6.025	3.363	3.363	0.000	0.000	0.000	0.000
18	A	22	GLY	0	0.019	0.032	7.610	3.279	3.279	0.000	0.000	0.000	0.000
19	A	23	ASP	-1	-0.843	-0.902	8.294	-32.055	-32.055	0.000	0.000	0.000	0.000
20	A	24	GLY	0	0.022	0.010	10.192	1.319	1.319	0.000	0.000	0.000	0.000
21	A	25	TRP	0	0.008	-0.008	12.294	1.426	1.426	0.000	0.000	0.000	0.000
22	A	26	SER	0	-0.036	-0.056	9.028	1.637	1.637	0.000	0.000	0.000	0.000
23	A	27	MET	0	0.049	0.016	11.909	0.512	0.512	0.000	0.000	0.000	0.000
24	A	28	LEU	0	-0.021	0.001	14.585	1.350	1.350	0.000	0.000	0.000	0.000
25	A	29	ILE	0	0.003	0.001	12.939	0.835	0.835	0.000	0.000	0.000	0.000
26	A	30	VAL	0	0.009	0.001	13.328	0.800	0.800	0.000	0.000	0.000	0.000
27	A	31	ARG	1	0.868	0.920	16.218	14.960	14.960	0.000	0.000	0.000	0.000
28	A	32	ASP	-1	-0.730	-0.826	19.442	-13.777	-13.777	0.000	0.000	0.000	0.000
29	A	33	ALA	0	0.004	0.009	18.220	0.637	0.637	0.000	0.000	0.000	0.000
30	A	34	PHE	0	-0.105	-0.056	17.952	0.591	0.591	0.000	0.000	0.000	0.000
31	A	35	GLU	-1	-0.938	-0.966	22.132	-11.965	-11.965	0.000	0.000	0.000	0.000
32	A	36	GLY	0	-0.014	0.003	23.557	0.536	0.536	0.000	0.000	0.000	0.000
33	A	37	LEU	0	-0.054	-0.017	22.037	0.264	0.264	0.000	0.000	0.000	0.000
34	A	38	THR	0	0.020	0.002	20.991	-0.466	-0.466	0.000	0.000	0.000	0.000
35	A	39	ARG	1	0.957	0.983	20.958	10.474	10.474	0.000	0.000	0.000	0.000
36	A	40	PHE	0	0.014	-0.003	17.622	0.043	0.043	0.000	0.000	0.000	0.000
37	A	41	GLY	0	-0.003	-0.018	21.102	-0.219	-0.219	0.000	0.000	0.000	0.000
38	A	42	GLU	-1	-0.843	-0.907	23.603	-11.561	-11.561	0.000	0.000	0.000	0.000
39	A	43	PHE	0	0.059	0.021	18.973	-0.033	-0.033	0.000	0.000	0.000	0.000
40	A	44	GLN	0	-0.097	-0.062	21.103	0.370	0.370	0.000	0.000	0.000	0.000
41	A	45	LYS	1	0.935	0.962	22.134	10.739	10.739	0.000	0.000	0.000	0.000
42	A	46	SER	0	-0.066	-0.031	22.378	0.424	0.424	0.000	0.000	0.000	0.000
43	A	47	LEU	0	-0.028	-0.017	17.379	-0.176	-0.176	0.000	0.000	0.000	0.000
44	A	48	GLY	0	0.029	0.022	21.199	-0.121	-0.121	0.000	0.000	0.000	0.000
45	A	49	LEU	0	-0.039	0.000	14.594	-0.080	-0.080	0.000	0.000	0.000	0.000
46	A	50	ALA	0	0.044	0.020	18.295	0.410	0.410	0.000	0.000	0.000	0.000
47	A	51	LYS	1	1.005	0.999	17.900	12.339	12.339	0.000	0.000	0.000	0.000
48	A	52	ASN	0	0.027	-0.009	17.422	-0.173	-0.173	0.000	0.000	0.000	0.000
49	A	53	ILE	0	0.025	0.020	12.889	-1.066	-1.066	0.000	0.000	0.000	0.000
50	A	54	LEU	0	0.058	0.037	13.334	-1.659	-1.659	0.000	0.000	0.000	0.000
51	A	55	ALA	0	-0.020	-0.005	14.321	-0.715	-0.715	0.000	0.000	0.000	0.000
52	A	56	ALA	0	-0.047	-0.030	10.847	-0.553	-0.553	0.000	0.000	0.000	0.000
53	A	57	ARG	1	0.926	0.975	8.193	27.452	27.452	0.000	0.000	0.000	0.000
54	A	58	LEU	0	0.025	0.018	10.117	-1.274	-1.274	0.000	0.000	0.000	0.000
55	A	59	ARG	1	0.952	0.973	10.833	20.570	20.570	0.000	0.000	0.000	0.000
57	A	61	LEU	0	0.043	0.015	6.635	-2.387	-2.387	0.000	0.000	0.000	0.000
58	A	62	VAL	0	-0.041	-0.007	9.056	0.876	0.876	0.000	0.000	0.000	0.000
59	A	63	GLU	-1	-0.931	-0.952	5.877	-29.748	-29.748	0.000	0.000	0.000	0.000
61	A	65	GLY	0	0.033	0.022	6.496	1.085	1.085	0.000	0.000	0.000	0.000
62	A	66	VAL	0	-0.034	0.001	9.322	1.680	1.680	0.000	0.000	0.000	0.000
63	A	67	MET	0	-0.023	-0.019	11.557	1.648	1.648	0.000	0.000	0.000	0.000
64	A	68	VAL	0	0.035	0.018	13.013	-0.938	-0.938	0.000	0.000	0.000	0.000
65	A	69	ALA	0	-0.014	-0.010	15.493	0.404	0.404	0.000	0.000	0.000	0.000
66	A	70	VAL	0	-0.015	-0.007	17.193	-0.029	-0.029	0.000	0.000	0.000	0.000
67	A	71	PRO	0	0.028	0.014	20.796	-0.021	-0.021	0.000	0.000	0.000	0.000
68	A	72	ALA	0	0.000	-0.005	24.159	0.043	0.043	0.000	0.000	0.000	0.000
69	A	73	GLU	-1	-0.948	-0.968	26.684	-10.249	-10.249	0.000	0.000	0.000	0.000
70	A	74	SER	0	-0.020	-0.014	29.264	0.348	0.348	0.000	0.000	0.000	0.000
71	A	75	GLY	0	-0.001	0.005	30.662	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	76	SER	0	-0.021	-0.007	29.165	-0.045	-0.045	0.000	0.000	0.000	0.000
73	A	77	HIS	0	-0.104	-0.070	24.887	0.046	0.046	0.000	0.000	0.000	0.000
74	A	78	GLN	0	0.018	0.015	19.340	0.497	0.497	0.000	0.000	0.000	0.000
75	A	79	GLU	-1	-0.879	-0.936	21.611	-11.605	-11.605	0.000	0.000	0.000	0.000
76	A	80	TYR	0	-0.053	-0.037	14.773	-0.277	-0.277	0.000	0.000	0.000	0.000
77	A	81	ARG	1	0.994	0.993	17.843	12.980	12.980	0.000	0.000	0.000	0.000
78	A	82	LEU	0	-0.017	-0.005	15.373	-0.855	-0.855	0.000	0.000	0.000	0.000
79	A	83	THR	0	0.003	-0.002	13.772	1.002	1.002	0.000	0.000	0.000	0.000
80	A	84	ASP	-1	-0.844	-0.931	16.813	-14.413	-14.413	0.000	0.000	0.000	0.000
81	A	85	LYS	1	0.846	0.920	7.856	28.616	28.616	0.000	0.000	0.000	0.000
82	A	86	GLY	0	0.048	0.009	14.358	-0.729	-0.729	0.000	0.000	0.000	0.000
83	A	87	ARG	1	0.918	0.958	15.119	13.651	13.651	0.000	0.000	0.000	0.000
84	A	88	ALA	0	0.018	0.004	16.127	0.536	0.536	0.000	0.000	0.000	0.000
85	A	89	LEU	0	-0.011	-0.005	12.257	-0.246	-0.246	0.000	0.000	0.000	0.000
86	A	90	PHE	0	-0.001	0.015	16.508	0.127	0.127	0.000	0.000	0.000	0.000
87	A	91	PRO	0	0.048	0.007	19.382	0.237	0.237	0.000	0.000	0.000	0.000
88	A	92	LEU	0	0.014	0.012	14.016	0.117	0.117	0.000	0.000	0.000	0.000
89	A	93	LEU	0	-0.009	-0.007	18.296	0.014	0.014	0.000	0.000	0.000	0.000
90	A	94	VAL	0	0.002	0.000	19.533	0.414	0.414	0.000	0.000	0.000	0.000
91	A	95	ALA	0	0.015	0.014	20.136	0.436	0.436	0.000	0.000	0.000	0.000
92	A	96	ILE	0	-0.031	-0.018	15.749	0.177	0.177	0.000	0.000	0.000	0.000
93	A	97	ARG	1	0.858	0.938	20.414	12.994	12.994	0.000	0.000	0.000	0.000
94	A	98	GLN	0	0.031	0.007	23.547	0.215	0.215	0.000	0.000	0.000	0.000
95	A	99	TRP	0	0.035	0.025	19.664	0.050	0.050	0.000	0.000	0.000	0.000
96	A	100	GLY	0	0.036	0.005	23.814	0.178	0.178	0.000	0.000	0.000	0.000
97	A	101	GLU	-1	-0.971	-1.021	24.612	-10.612	-10.612	0.000	0.000	0.000	0.000
98	A	102	ASP	-1	-0.807	-0.847	27.776	-10.524	-10.524	0.000	0.000	0.000	0.000
99	A	103	TYR	0	-0.061	-0.033	25.947	0.414	0.414	0.000	0.000	0.000	0.000
100	A	104	PHE	0	-0.084	-0.036	21.897	-0.198	-0.198	0.000	0.000	0.000	0.000
101	A	105	PHE	0	-0.021	0.002	26.859	-0.146	-0.146	0.000	0.000	0.000	0.000
102	A	106	ALA	0	0.020	0.016	30.291	0.149	0.149	0.000	0.000	0.000	0.000
103	A	107	PRO	0	-0.036	-0.043	33.673	0.021	0.021	0.000	0.000	0.000	0.000
104	A	108	ASP	-1	-0.942	-0.964	36.682	-8.437	-8.437	0.000	0.000	0.000	0.000
105	A	109	GLU	-1	-0.872	-0.918	31.237	-10.240	-10.240	0.000	0.000	0.000	0.000
106	A	110	SER	0	-0.059	-0.025	34.245	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	111	HIS	1	0.862	0.931	29.500	10.225	10.225	0.000	0.000	0.000	0.000
108	A	112	VAL	0	-0.005	-0.008	27.816	0.235	0.235	0.000	0.000	0.000	0.000
109	A	113	ARG	1	0.991	1.004	30.034	8.832	8.832	0.000	0.000	0.000	0.000
110	A	114	LEU	0	0.002	0.011	25.977	-0.024	-0.024	0.000	0.000	0.000	0.000
111	A	115	VAL	0	-0.015	0.001	29.499	0.158	0.158	0.000	0.000	0.000	0.000
112	A	116	GLU	-1	-0.872	-0.918	31.699	-9.207	-9.207	0.000	0.000	0.000	0.000
113	A	117	ARG	1	0.901	0.923	29.031	10.178	10.178	0.000	0.000	0.000	0.000
114	A	118	ASP	-1	-0.929	-0.948	34.728	-7.807	-7.807	0.000	0.000	0.000	0.000
115	A	119	SER	0	0.014	-0.022	37.651	0.132	0.132	0.000	0.000	0.000	0.000
116	A	120	GLY	0	-0.016	0.014	36.179	0.133	0.133	0.000	0.000	0.000	0.000
117	A	121	GLN	0	-0.043	-0.025	37.123	0.071	0.071	0.000	0.000	0.000	0.000
118	A	122	PRO	0	-0.011	-0.025	33.290	-0.211	-0.211	0.000	0.000	0.000	0.000
119	A	123	VAL	0	0.004	0.008	28.749	0.134	0.134	0.000	0.000	0.000	0.000
120	A	124	PRO	0	0.002	-0.002	31.418	-0.163	-0.163	0.000	0.000	0.000	0.000
121	A	125	ARG	1	0.786	0.858	29.105	10.190	10.190	0.000	0.000	0.000	0.000
122	A	126	LEU	0	-0.029	-0.012	23.696	0.142	0.142	0.000	0.000	0.000	0.000
123	A	127	GLN	0	-0.021	-0.019	27.771	-0.115	-0.115	0.000	0.000	0.000	0.000
124	A	128	VAL	0	0.023	0.020	24.898	-0.183	-0.183	0.000	0.000	0.000	0.000
125	A	129	ARG	1	0.891	0.928	27.536	10.067	10.067	0.000	0.000	0.000	0.000
126	A	130	ALA	0	0.046	0.044	28.928	-0.365	-0.365	0.000	0.000	0.000	0.000
127	A	131	GLY	0	-0.008	-0.017	31.416	0.009	0.009	0.000	0.000	0.000	0.000
128	A	132	ASP	-1	-0.829	-0.887	32.367	-8.659	-8.659	0.000	0.000	0.000	0.000
129	A	133	GLY	0	-0.022	-0.003	33.159	0.183	0.183	0.000	0.000	0.000	0.000
130	A	134	SER	0	-0.069	-0.049	34.196	-0.085	-0.085	0.000	0.000	0.000	0.000
131	A	135	PRO	0	-0.040	-0.046	32.449	-0.292	-0.292	0.000	0.000	0.000	0.000
132	A	136	LEU	0	-0.011	0.009	28.326	0.225	0.225	0.000	0.000	0.000	0.000
133	A	137	ALA	0	0.019	0.025	29.385	-0.360	-0.360	0.000	0.000	0.000	0.000
134	A	138	ALA	0	-0.009	-0.010	25.682	-0.174	-0.174	0.000	0.000	0.000	0.000
135	A	139	GLU	-1	-0.889	-0.949	27.332	-10.638	-10.638	0.000	0.000	0.000	0.000
136	A	140	ASP	-1	-0.904	-0.934	29.970	-9.293	-9.293	0.000	0.000	0.000	0.000
137	A	141	THR	0	-0.128	-0.078	26.031	-0.247	-0.247	0.000	0.000	0.000	0.000
138	A	142	ARG	1	0.968	0.971	25.825	10.753	10.753	0.000	0.000	0.000	0.000
139	A	143	VAL	0	-0.027	-0.011	19.958	-0.250	-0.250	0.000	0.000	0.000	0.000
140	A	144	SER	0	-0.055	-0.060	22.919	0.532	0.532	0.000	0.000	0.000	0.000
141	A	145	ARG	1	0.850	0.904	20.703	13.140	13.140	0.000	0.000	0.000	0.000
142	A	146	ASP	-2	-1.785	-1.834	23.778	-23.272	-23.272	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:THR)