FMO DATABASE

FMODB ID: NZ67Q

Calculation Name: 1F2Q-A-Xray547

Preferred Name: IgE Fc receptor, alpha-subunit

Target Type: SINGLE PROTEIN

Ligand Name: 2-acetamido-2-deoxy-beta-d-glucopyranose | alpha-d-mannopyranose

Ligand 3-letter code: NAG | MAN

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1F2Q

Chain ID: A

ChEMBL ID: CHEMBL2248

UniProt ID: P12319

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	169
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1764216.575652
FMO2-HF: Nuclear repulsion	1694584.592079
FMO2-HF: Total energy	-69631.983574
FMO2-MP2: Total energy	-69835.62978

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:LYS)

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

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.
-324.105	-308.354	6.332	-11.017	-11.065	-0.124

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.742 / q_NPA : 1.878

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	LYS	1	0.979	0.952	3.397	62.627	64.940	0.088	-0.989	-1.412	-0.004
68	A	72	GLN	0	-0.006	0.007	2.369	-1.786	0.291	1.859	-1.674	-2.262	-0.024
69	A	73	VAL	0	0.009	0.011	3.754	-15.074	-14.546	0.010	-0.226	-0.312	-0.001
70	A	74	ASN	0	-0.065	-0.027	2.051	11.142	11.569	1.626	-0.846	-1.207	-0.006
71	A	75	GLU	-1	-0.828	-0.930	2.168	-90.189	-86.403	2.301	-3.504	-2.582	-0.052
72	A	76	SER	0	-0.047	-0.029	2.825	-22.050	-19.029	0.338	-1.753	-1.606	-0.018
73	A	77	GLU	-1	-0.931	-0.959	3.071	-103.856	-100.257	0.110	-2.025	-1.684	-0.019
4	A	7	VAL	0	0.052	0.039	5.696	3.988	3.988	0.000	0.000	0.000	0.000
5	A	8	SER	0	-0.062	-0.030	9.418	-0.013	-0.013	0.000	0.000	0.000	0.000
6	A	9	LEU	0	0.019	0.013	11.964	0.660	0.660	0.000	0.000	0.000	0.000
7	A	10	ASN	0	0.003	0.016	15.734	0.671	0.671	0.000	0.000	0.000	0.000
8	A	11	PRO	0	0.048	0.002	18.996	0.604	0.604	0.000	0.000	0.000	0.000
9	A	12	PRO	0	0.004	-0.010	17.416	-0.776	-0.776	0.000	0.000	0.000	0.000
10	A	13	TRP	0	-0.025	0.003	17.504	-1.421	-1.421	0.000	0.000	0.000	0.000
11	A	14	ASN	0	-0.027	-0.027	16.682	0.776	0.776	0.000	0.000	0.000	0.000
12	A	15	ARG	1	0.878	0.972	18.708	25.804	25.804	0.000	0.000	0.000	0.000
13	A	16	ILE	0	0.014	0.010	22.343	0.539	0.539	0.000	0.000	0.000	0.000
14	A	17	PHE	0	0.012	-0.003	25.071	0.287	0.287	0.000	0.000	0.000	0.000
15	A	18	LYS	1	0.931	0.962	28.084	18.851	18.851	0.000	0.000	0.000	0.000
16	A	19	GLY	0	-0.058	-0.027	29.040	0.799	0.799	0.000	0.000	0.000	0.000
17	A	20	GLU	-1	-0.812	-0.881	26.905	-22.029	-22.029	0.000	0.000	0.000	0.000
18	A	21	ASN	0	-0.013	-0.016	25.195	-0.167	-0.167	0.000	0.000	0.000	0.000
19	A	22	VAL	0	0.001	0.002	19.000	-0.027	-0.027	0.000	0.000	0.000	0.000
20	A	23	THR	0	-0.025	-0.013	17.597	0.366	0.366	0.000	0.000	0.000	0.000
21	A	24	LEU	0	0.005	0.008	14.070	-1.299	-1.299	0.000	0.000	0.000	0.000
22	A	25	THR	0	0.011	-0.014	13.012	1.514	1.514	0.000	0.000	0.000	0.000
23	A	26	CYS	0	-0.052	-0.010	7.682	-3.668	-3.668	0.000	0.000	0.000	0.000
24	A	27	ASN	0	-0.015	-0.020	4.997	7.840	7.840	0.000	0.000	0.000	0.000
25	A	28	GLY	0	0.044	0.030	8.684	1.530	1.530	0.000	0.000	0.000	0.000
26	A	29	ASN	0	-0.088	-0.039	5.596	5.728	5.728	0.000	0.000	0.000	0.000
27	A	30	ASN	0	-0.002	-0.012	9.393	5.978	5.978	0.000	0.000	0.000	0.000
28	A	31	PHE	0	0.016	0.010	10.954	0.641	0.641	0.000	0.000	0.000	0.000
29	A	32	PHE	0	-0.017	-0.015	12.391	2.819	2.819	0.000	0.000	0.000	0.000
30	A	33	GLU	-1	-0.850	-0.922	8.839	-50.951	-50.951	0.000	0.000	0.000	0.000
31	A	34	VAL	0	-0.051	-0.028	13.158	0.675	0.675	0.000	0.000	0.000	0.000
32	A	35	SER	0	-0.036	-0.022	11.341	1.318	1.318	0.000	0.000	0.000	0.000
33	A	36	SER	0	0.019	0.028	13.438	-0.724	-0.724	0.000	0.000	0.000	0.000
34	A	37	THR	0	-0.049	-0.016	9.349	-3.994	-3.994	0.000	0.000	0.000	0.000
35	A	38	LYS	1	0.882	0.937	9.927	48.713	48.713	0.000	0.000	0.000	0.000
36	A	39	TRP	0	0.030	0.006	10.461	-5.149	-5.149	0.000	0.000	0.000	0.000
37	A	40	PHE	0	0.003	-0.007	9.587	2.456	2.456	0.000	0.000	0.000	0.000
38	A	41	HIS	1	0.848	0.913	13.478	29.971	29.971	0.000	0.000	0.000	0.000
39	A	42	ASN	0	0.031	0.002	16.261	0.214	0.214	0.000	0.000	0.000	0.000
40	A	43	GLY	0	0.020	0.015	14.459	1.279	1.279	0.000	0.000	0.000	0.000
41	A	44	SER	0	-0.027	-0.003	15.524	0.178	0.178	0.000	0.000	0.000	0.000
42	A	45	LEU	0	-0.070	-0.031	13.551	-1.350	-1.350	0.000	0.000	0.000	0.000
43	A	46	SER	0	0.002	0.003	15.697	2.536	2.536	0.000	0.000	0.000	0.000
44	A	47	GLU	-1	-0.915	-0.961	17.093	-25.303	-25.303	0.000	0.000	0.000	0.000
45	A	48	GLU	-1	-0.870	-0.919	16.229	-30.508	-30.508	0.000	0.000	0.000	0.000
46	A	49	THR	0	-0.020	-0.021	14.742	-1.806	-1.806	0.000	0.000	0.000	0.000
47	A	50	ASN	0	-0.038	-0.021	14.856	-1.032	-1.032	0.000	0.000	0.000	0.000
48	A	51	SER	0	0.022	0.012	12.410	-0.978	-0.978	0.000	0.000	0.000	0.000
49	A	52	SER	0	-0.012	-0.018	13.079	-2.586	-2.586	0.000	0.000	0.000	0.000
50	A	53	LEU	0	0.013	0.032	15.590	1.446	1.446	0.000	0.000	0.000	0.000
51	A	54	ASN	0	-0.002	0.001	17.264	-0.418	-0.418	0.000	0.000	0.000	0.000
52	A	55	ILE	0	0.025	0.030	18.561	0.830	0.830	0.000	0.000	0.000	0.000
53	A	56	VAL	0	-0.009	-0.023	22.157	0.398	0.398	0.000	0.000	0.000	0.000
54	A	57	ASN	0	-0.077	-0.038	25.917	0.777	0.777	0.000	0.000	0.000	0.000
55	A	58	ALA	0	0.001	0.023	24.741	0.264	0.264	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.960	0.963	25.853	23.119	23.119	0.000	0.000	0.000	0.000
57	A	60	PHE	0	0.026	0.005	25.643	-0.510	-0.510	0.000	0.000	0.000	0.000
58	A	61	GLU	-1	-0.881	-0.949	25.023	-22.395	-22.395	0.000	0.000	0.000	0.000
59	A	62	ASP	-1	-0.838	-0.898	21.997	-26.091	-26.091	0.000	0.000	0.000	0.000
60	A	63	SER	0	0.024	0.022	20.705	-1.537	-1.537	0.000	0.000	0.000	0.000
61	A	64	GLY	0	-0.029	-0.017	19.246	0.338	0.338	0.000	0.000	0.000	0.000
62	A	65	GLU	-1	-0.877	-0.927	13.090	-44.254	-44.254	0.000	0.000	0.000	0.000
63	A	66	TYR	0	-0.021	-0.029	13.148	1.446	1.446	0.000	0.000	0.000	0.000
64	A	67	LYS	1	0.894	0.957	8.159	48.120	48.120	0.000	0.000	0.000	0.000
65	A	69	GLN	0	0.033	0.016	5.610	-4.790	-4.790	0.000	0.000	0.000	0.000
66	A	70	HIS	0	0.019	0.003	5.272	7.020	7.020	0.000	0.000	0.000	0.000
67	A	71	GLN	0	0.025	-0.003	5.895	-5.397	-5.397	0.000	0.000	0.000	0.000
74	A	78	PRO	0	-0.014	-0.003	5.732	2.225	2.225	0.000	0.000	0.000	0.000
75	A	79	VAL	0	-0.014	-0.001	9.529	-0.804	-0.804	0.000	0.000	0.000	0.000
76	A	80	TYR	0	-0.028	-0.035	12.166	1.104	1.104	0.000	0.000	0.000	0.000
77	A	81	LEU	0	-0.006	0.010	15.686	0.315	0.315	0.000	0.000	0.000	0.000
78	A	82	GLU	-1	-0.872	-0.953	18.716	-25.467	-25.467	0.000	0.000	0.000	0.000
79	A	83	VAL	0	-0.022	0.004	22.308	0.363	0.363	0.000	0.000	0.000	0.000
80	A	84	PHE	0	0.043	0.011	24.204	0.808	0.808	0.000	0.000	0.000	0.000
81	A	85	SER	0	-0.058	-0.056	28.785	0.267	0.267	0.000	0.000	0.000	0.000
82	A	86	ASP	-1	-0.830	-0.887	32.593	-17.774	-17.774	0.000	0.000	0.000	0.000
83	A	87	TRP	0	-0.046	-0.038	34.116	-0.066	-0.066	0.000	0.000	0.000	0.000
84	A	88	LEU	0	-0.034	-0.023	32.852	-0.041	-0.041	0.000	0.000	0.000	0.000
85	A	89	LEU	0	-0.008	0.009	25.738	-0.103	-0.103	0.000	0.000	0.000	0.000
86	A	90	LEU	0	0.004	0.023	25.430	-0.026	-0.026	0.000	0.000	0.000	0.000
87	A	91	GLN	0	-0.023	-0.012	23.042	-0.491	-0.491	0.000	0.000	0.000	0.000
88	A	92	ALA	0	0.059	0.017	20.119	0.705	0.705	0.000	0.000	0.000	0.000
89	A	93	SER	0	-0.011	-0.006	17.414	-0.115	-0.115	0.000	0.000	0.000	0.000
90	A	94	ALA	0	-0.035	-0.025	14.161	-2.250	-2.250	0.000	0.000	0.000	0.000
91	A	95	GLU	-1	-0.812	-0.889	15.967	-30.783	-30.783	0.000	0.000	0.000	0.000
92	A	96	VAL	0	-0.015	-0.013	11.872	1.011	1.011	0.000	0.000	0.000	0.000
93	A	97	VAL	0	-0.010	-0.001	13.131	-2.334	-2.334	0.000	0.000	0.000	0.000
94	A	98	MET	0	-0.051	-0.023	8.862	-1.533	-1.533	0.000	0.000	0.000	0.000
95	A	99	GLU	-1	-0.876	-0.961	13.286	-28.247	-28.247	0.000	0.000	0.000	0.000
96	A	100	GLY	0	-0.034	-0.006	15.543	-1.452	-1.452	0.000	0.000	0.000	0.000
97	A	101	GLN	0	-0.061	-0.028	13.182	1.392	1.392	0.000	0.000	0.000	0.000
98	A	102	PRO	0	-0.018	0.002	16.651	0.978	0.978	0.000	0.000	0.000	0.000
99	A	103	LEU	0	-0.019	0.000	17.929	-1.755	-1.755	0.000	0.000	0.000	0.000
100	A	104	PHE	0	-0.006	-0.017	19.194	1.494	1.494	0.000	0.000	0.000	0.000
101	A	105	LEU	0	0.001	-0.004	21.645	-0.935	-0.935	0.000	0.000	0.000	0.000
102	A	106	ARG	1	0.905	0.954	24.404	22.796	22.796	0.000	0.000	0.000	0.000
103	A	107	CYS	0	-0.074	-0.016	26.801	-0.141	-0.141	0.000	0.000	0.000	0.000
104	A	108	HIS	0	-0.051	-0.048	27.669	0.834	0.834	0.000	0.000	0.000	0.000
105	A	109	GLY	0	0.097	0.046	29.931	0.265	0.265	0.000	0.000	0.000	0.000
106	A	110	TRP	0	-0.005	-0.004	32.423	-0.283	-0.283	0.000	0.000	0.000	0.000
107	A	111	ARG	1	0.878	0.932	33.592	17.186	17.186	0.000	0.000	0.000	0.000
108	A	112	ASN	0	-0.020	-0.007	30.496	-0.111	-0.111	0.000	0.000	0.000	0.000
109	A	113	TRP	0	-0.032	-0.013	33.920	0.464	0.464	0.000	0.000	0.000	0.000
110	A	114	ASP	-1	-0.840	-0.906	35.905	-16.377	-16.377	0.000	0.000	0.000	0.000
111	A	115	VAL	0	-0.003	0.001	34.119	0.277	0.277	0.000	0.000	0.000	0.000
112	A	116	TYR	0	-0.060	-0.031	37.122	0.053	0.053	0.000	0.000	0.000	0.000
113	A	117	LYS	1	0.809	0.879	39.138	14.416	14.416	0.000	0.000	0.000	0.000
114	A	118	VAL	0	0.025	0.021	32.774	-0.030	-0.030	0.000	0.000	0.000	0.000
115	A	119	ILE	0	-0.025	0.001	35.388	0.149	0.149	0.000	0.000	0.000	0.000
116	A	120	TYR	0	0.043	0.011	28.672	-0.409	-0.409	0.000	0.000	0.000	0.000
117	A	121	TYR	0	-0.029	-0.015	31.144	0.616	0.616	0.000	0.000	0.000	0.000
118	A	122	LYS	1	0.837	0.912	25.582	21.049	21.049	0.000	0.000	0.000	0.000
119	A	123	ASP	-1	-0.825	-0.905	27.800	-20.991	-20.991	0.000	0.000	0.000	0.000
120	A	124	GLY	0	-0.013	0.001	30.455	0.532	0.532	0.000	0.000	0.000	0.000
121	A	125	GLU	-1	-0.888	-0.935	32.853	-15.971	-15.971	0.000	0.000	0.000	0.000
122	A	126	ALA	0	0.017	0.008	32.898	-0.513	-0.513	0.000	0.000	0.000	0.000
123	A	127	LEU	0	-0.060	-0.037	28.233	0.025	0.025	0.000	0.000	0.000	0.000
124	A	128	LYS	1	0.889	0.929	32.302	17.490	17.490	0.000	0.000	0.000	0.000
125	A	129	TYR	0	-0.083	-0.054	25.846	0.693	0.693	0.000	0.000	0.000	0.000
126	A	130	TRP	0	0.007	0.004	32.005	0.461	0.461	0.000	0.000	0.000	0.000
127	A	131	TYR	0	-0.022	-0.012	31.024	-0.663	-0.663	0.000	0.000	0.000	0.000
128	A	132	GLU	-1	-0.893	-0.926	30.222	-19.064	-19.064	0.000	0.000	0.000	0.000
129	A	133	ASN	0	-0.029	-0.049	33.207	-0.312	-0.312	0.000	0.000	0.000	0.000
130	A	134	HIS	0	-0.042	-0.023	30.854	-0.604	-0.604	0.000	0.000	0.000	0.000
131	A	135	ASN	0	-0.044	-0.013	26.937	-1.295	-1.295	0.000	0.000	0.000	0.000
132	A	136	ILE	0	0.039	0.018	26.424	0.634	0.634	0.000	0.000	0.000	0.000
133	A	137	SER	0	-0.039	-0.019	23.365	-0.987	-0.987	0.000	0.000	0.000	0.000
134	A	138	ILE	0	0.036	0.029	23.072	0.878	0.878	0.000	0.000	0.000	0.000
135	A	139	THR	0	-0.023	-0.027	22.149	-1.170	-1.170	0.000	0.000	0.000	0.000
136	A	140	ASN	0	-0.031	-0.018	20.748	-1.622	-1.622	0.000	0.000	0.000	0.000
137	A	141	ALA	0	0.027	0.034	18.202	0.901	0.901	0.000	0.000	0.000	0.000
138	A	142	THR	0	0.033	0.008	19.445	-0.912	-0.912	0.000	0.000	0.000	0.000
139	A	143	VAL	0	0.016	-0.004	20.322	-0.159	-0.159	0.000	0.000	0.000	0.000
140	A	144	GLU	-1	-0.922	-0.962	21.257	-20.982	-20.982	0.000	0.000	0.000	0.000
141	A	145	ASP	-1	-0.796	-0.867	21.717	-23.381	-23.381	0.000	0.000	0.000	0.000
142	A	146	SER	0	-0.015	-0.008	20.513	-1.189	-1.189	0.000	0.000	0.000	0.000
143	A	147	GLY	0	0.009	0.006	22.096	1.140	1.140	0.000	0.000	0.000	0.000
144	A	148	THR	0	-0.068	-0.042	23.873	-0.768	-0.768	0.000	0.000	0.000	0.000
145	A	149	TYR	0	-0.033	-0.035	23.306	1.251	1.251	0.000	0.000	0.000	0.000
146	A	150	TYR	0	0.034	0.010	27.205	-0.410	-0.410	0.000	0.000	0.000	0.000
147	A	152	THR	0	0.077	0.044	32.273	0.195	0.195	0.000	0.000	0.000	0.000
148	A	153	GLY	0	0.012	-0.003	35.954	-0.141	-0.141	0.000	0.000	0.000	0.000
149	A	154	LYS	1	0.834	0.942	37.678	13.772	13.772	0.000	0.000	0.000	0.000
150	A	155	VAL	0	0.041	0.022	37.270	-0.186	-0.186	0.000	0.000	0.000	0.000
151	A	156	TRP	0	-0.005	-0.012	40.475	0.533	0.533	0.000	0.000	0.000	0.000
152	A	157	GLN	0	0.006	-0.019	43.764	0.201	0.201	0.000	0.000	0.000	0.000
153	A	158	LEU	0	0.002	0.017	43.638	0.291	0.291	0.000	0.000	0.000	0.000
154	A	159	ASP	-1	-0.837	-0.909	41.435	-14.736	-14.736	0.000	0.000	0.000	0.000
155	A	160	TYR	0	-0.018	-0.013	37.420	0.224	0.224	0.000	0.000	0.000	0.000
156	A	161	GLU	-1	-0.915	-0.975	34.819	-17.001	-17.001	0.000	0.000	0.000	0.000
157	A	162	SER	0	-0.029	-0.009	30.391	-0.116	-0.116	0.000	0.000	0.000	0.000
158	A	163	GLU	-1	-0.867	-0.935	29.029	-19.687	-19.687	0.000	0.000	0.000	0.000
159	A	164	PRO	0	-0.037	-0.011	28.248	-0.541	-0.541	0.000	0.000	0.000	0.000
160	A	165	LEU	0	-0.036	-0.021	21.066	-0.590	-0.590	0.000	0.000	0.000	0.000
161	A	166	ASN	0	-0.017	-0.011	22.205	1.034	1.034	0.000	0.000	0.000	0.000
162	A	167	ILE	0	0.001	0.010	18.758	-1.258	-1.258	0.000	0.000	0.000	0.000
163	A	168	THR	0	-0.028	-0.020	16.704	1.412	1.412	0.000	0.000	0.000	0.000
164	A	169	VAL	0	-0.004	0.005	16.361	-1.968	-1.968	0.000	0.000	0.000	0.000
165	A	170	ILE	0	0.002	0.010	10.094	0.921	0.921	0.000	0.000	0.000	0.000
166	A	171	LYS	1	0.941	0.959	13.675	30.032	30.032	0.000	0.000	0.000	0.000
167	A	172	ALA	0	0.036	0.018	11.249	-2.380	-2.380	0.000	0.000	0.000	0.000
168	A	173	PRO	0	-0.103	-0.061	9.772	-3.265	-3.265	0.000	0.000	0.000	0.000
169	A	174	ARG	0	0.069	0.056	6.389	-13.237	-13.237	0.000	0.000	0.000	0.000

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