FMO DATABASE

FMODB ID: VN4K1

Calculation Name: 1BV1-A-Xray547

Preferred Name: Major pollen allergen Bet v 1-A

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1BV1

Chain ID: A

ChEMBL ID: CHEMBL3879834

UniProt ID: P15494

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	159
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1493200.850537
FMO2-HF: Nuclear repulsion	1433172.580826
FMO2-HF: Total energy	-60028.269712
FMO2-MP2: Total energy	-60207.287734

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:1:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-173.528	-177.559	30.439	-15.308	-11.102	-0.17

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.783 / q_NPA : 0.879

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	3	PHE	0	0.016	0.017	2.782	2.222	3.973	0.043	-0.748	-1.047	-0.004
121	A	121	HIS	0	-0.003	0.002	4.659	-5.573	-5.538	-0.001	-0.030	-0.004	0.000
122	A	122	THR	0	0.031	-0.005	1.955	-13.704	-14.105	6.708	-3.265	-3.042	-0.039
123	A	123	LYS	1	0.983	0.993	1.826	0.912	-1.617	10.789	-5.071	-3.189	-0.058
124	A	124	GLY	0	0.013	0.009	3.668	4.014	4.492	0.012	-0.212	-0.277	-0.001
125	A	125	ASP	-1	-0.880	-0.944	1.725	-91.126	-94.865	12.889	-5.767	-3.383	-0.067
126	A	126	HIS	0	-0.061	-0.024	4.109	11.392	11.478	-0.001	-0.025	-0.061	0.000
127	A	127	GLU	-1	-0.893	-0.928	3.819	-46.160	-45.872	0.000	-0.190	-0.099	-0.001
4	A	4	ASN	0	-0.029	-0.014	6.450	2.176	2.176	0.000	0.000	0.000	0.000
5	A	5	TYR	0	0.012	0.001	8.334	1.810	1.810	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.854	-0.911	12.990	-18.899	-18.899	0.000	0.000	0.000	0.000
7	A	7	THR	0	-0.038	-0.040	16.384	0.017	0.017	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.845	-0.902	20.018	-12.931	-12.931	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.000	0.004	23.544	0.260	0.260	0.000	0.000	0.000	0.000
10	A	10	THR	0	-0.005	-0.008	26.366	0.080	0.080	0.000	0.000	0.000	0.000
11	A	11	SER	0	-0.040	-0.035	30.087	0.018	0.018	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.007	-0.012	32.688	0.088	0.088	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.046	-0.006	34.692	0.303	0.303	0.000	0.000	0.000	0.000
14	A	14	PRO	0	0.057	0.053	34.925	-0.274	-0.274	0.000	0.000	0.000	0.000
15	A	15	ALA	0	0.032	0.006	32.066	-0.013	-0.013	0.000	0.000	0.000	0.000
16	A	16	ALA	0	0.011	0.010	33.180	-0.173	-0.173	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.794	0.890	35.508	8.048	8.048	0.000	0.000	0.000	0.000
18	A	18	LEU	0	0.027	0.011	30.629	-0.069	-0.069	0.000	0.000	0.000	0.000
19	A	19	PHE	0	0.028	0.010	27.182	-0.131	-0.131	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.873	0.925	31.517	8.192	8.192	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.027	0.024	33.939	0.016	0.016	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.026	-0.022	25.412	-0.104	-0.104	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.032	-0.012	25.423	-0.402	-0.402	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.057	-0.032	28.594	-0.077	-0.077	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.766	-0.852	31.153	-9.093	-9.093	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.039	0.032	29.047	0.170	0.170	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.851	-0.941	27.540	-11.669	-11.669	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.042	-0.013	29.969	0.251	0.251	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.009	-0.004	32.811	0.283	0.283	0.000	0.000	0.000	0.000
30	A	30	PHE	0	0.035	0.022	26.503	0.188	0.188	0.000	0.000	0.000	0.000
31	A	31	PRO	0	-0.014	-0.008	30.783	0.092	0.092	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.823	0.922	32.711	9.174	9.174	0.000	0.000	0.000	0.000
33	A	33	VAL	0	-0.035	-0.024	32.566	0.218	0.218	0.000	0.000	0.000	0.000
34	A	34	ALA	0	-0.011	-0.004	30.377	0.034	0.034	0.000	0.000	0.000	0.000
35	A	35	PRO	0	0.061	0.048	30.977	-0.353	-0.353	0.000	0.000	0.000	0.000
36	A	36	GLN	0	-0.016	-0.018	31.230	0.008	0.008	0.000	0.000	0.000	0.000
37	A	37	ALA	0	-0.037	-0.015	26.988	-0.252	-0.252	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.007	-0.022	25.063	-0.540	-0.540	0.000	0.000	0.000	0.000
39	A	39	SER	0	0.000	-0.003	28.614	0.366	0.366	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.021	-0.022	29.523	0.332	0.332	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.001	0.008	26.936	-0.481	-0.481	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.869	-0.913	28.040	-10.554	-10.554	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.022	-0.024	27.631	-0.697	-0.697	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.029	-0.013	24.672	0.277	0.277	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.923	-0.967	25.899	-12.091	-12.091	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.037	0.024	27.463	-0.296	-0.296	0.000	0.000	0.000	0.000
47	A	47	ASN	0	-0.019	-0.024	29.276	0.170	0.170	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.056	0.030	28.639	0.289	0.289	0.000	0.000	0.000	0.000
49	A	49	GLY	0	-0.014	0.004	27.963	-0.210	-0.210	0.000	0.000	0.000	0.000
50	A	50	PRO	0	0.000	-0.002	24.271	-0.243	-0.243	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.009	0.003	23.060	0.432	0.432	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.048	-0.026	24.028	0.097	0.097	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.017	0.004	20.977	-0.769	-0.769	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.862	0.923	23.048	12.282	12.282	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.828	0.909	22.917	10.882	10.882	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.029	0.028	22.516	0.703	0.703	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.024	-0.026	24.294	-0.527	-0.527	0.000	0.000	0.000	0.000
58	A	58	PHE	0	0.003	0.009	21.315	0.126	0.126	0.000	0.000	0.000	0.000
59	A	59	PRO	0	0.022	0.020	26.991	0.215	0.215	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.912	-0.968	28.685	-10.194	-10.194	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.018	0.001	29.813	-0.074	-0.074	0.000	0.000	0.000	0.000
62	A	62	LEU	0	-0.040	-0.010	23.288	-0.262	-0.262	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.020	-0.019	21.293	-0.041	-0.041	0.000	0.000	0.000	0.000
64	A	64	PHE	0	-0.020	0.001	16.604	-0.496	-0.496	0.000	0.000	0.000	0.000
65	A	65	LYS	1	1.014	1.005	22.186	12.378	12.378	0.000	0.000	0.000	0.000
66	A	66	TYR	0	-0.104	-0.089	21.309	0.683	0.683	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.004	0.006	17.739	-0.712	-0.712	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.805	0.889	19.196	15.196	15.196	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.803	-0.911	18.250	-18.022	-18.022	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.867	0.919	15.531	19.297	19.297	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.011	0.016	19.531	-0.713	-0.713	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.813	-0.882	16.992	-18.664	-18.664	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.875	-0.943	20.406	-14.096	-14.096	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.013	-0.013	22.915	-0.093	-0.093	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.796	-0.876	26.172	-10.971	-10.971	0.000	0.000	0.000	0.000
76	A	76	HIS	0	0.022	-0.012	27.949	-0.088	-0.088	0.000	0.000	0.000	0.000
77	A	77	THR	0	-0.062	-0.017	30.850	0.405	0.405	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.097	-0.065	27.580	0.355	0.355	0.000	0.000	0.000	0.000
79	A	79	PHE	0	-0.022	-0.003	27.879	-0.226	-0.226	0.000	0.000	0.000	0.000
80	A	80	LYS	1	0.808	0.894	20.744	14.536	14.536	0.000	0.000	0.000	0.000
81	A	81	TYR	0	0.024	0.012	22.549	0.199	0.199	0.000	0.000	0.000	0.000
82	A	82	ASN	0	-0.008	-0.013	17.702	0.186	0.186	0.000	0.000	0.000	0.000
83	A	83	TYR	0	0.028	0.022	18.344	0.560	0.560	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.019	-0.031	14.368	-2.054	-2.054	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.002	0.016	14.315	0.904	0.904	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.017	-0.039	13.521	-2.214	-2.214	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.774	-0.848	15.028	-15.399	-15.399	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.044	0.032	16.985	0.730	0.730	0.000	0.000	0.000	0.000
89	A	89	GLY	0	0.043	0.006	16.487	-1.145	-1.145	0.000	0.000	0.000	0.000
90	A	90	PRO	0	-0.058	-0.018	12.874	0.084	0.084	0.000	0.000	0.000	0.000
91	A	91	ILE	0	-0.075	-0.017	11.513	-2.427	-2.427	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.032	0.014	11.333	2.150	2.150	0.000	0.000	0.000	0.000
93	A	93	ASP	-1	-0.915	-0.954	10.892	-28.910	-28.910	0.000	0.000	0.000	0.000
94	A	94	THR	0	-0.070	-0.043	7.006	-2.029	-2.029	0.000	0.000	0.000	0.000
95	A	95	LEU	0	-0.053	-0.023	6.043	-10.286	-10.286	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.841	-0.906	6.735	-30.017	-30.017	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.862	0.911	8.105	34.848	34.848	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.013	-0.005	8.889	-4.528	-4.528	0.000	0.000	0.000	0.000
99	A	99	SER	0	-0.044	-0.013	11.179	1.456	1.456	0.000	0.000	0.000	0.000
100	A	100	ASN	0	-0.019	-0.017	13.028	-2.006	-2.006	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.811	-0.883	15.780	-15.506	-15.506	0.000	0.000	0.000	0.000
102	A	102	ILE	0	0.006	0.004	18.407	-0.140	-0.140	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.883	0.922	21.110	14.994	14.994	0.000	0.000	0.000	0.000
104	A	104	ILE	0	-0.013	0.005	24.282	-0.019	-0.019	0.000	0.000	0.000	0.000
105	A	105	VAL	0	-0.006	-0.009	27.013	0.238	0.238	0.000	0.000	0.000	0.000
106	A	106	ALA	0	0.015	0.012	29.760	0.048	0.048	0.000	0.000	0.000	0.000
107	A	107	THR	0	-0.034	-0.043	32.194	-0.186	-0.186	0.000	0.000	0.000	0.000
108	A	108	PRO	0	-0.029	-0.037	34.628	0.191	0.191	0.000	0.000	0.000	0.000
109	A	109	ASP	-1	-0.860	-0.895	37.013	-8.564	-8.564	0.000	0.000	0.000	0.000
110	A	110	GLY	0	-0.027	-0.006	38.362	0.215	0.215	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.009	0.015	35.981	0.013	0.013	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.020	-0.050	31.103	-0.071	-0.071	0.000	0.000	0.000	0.000
113	A	113	ILE	0	-0.027	-0.006	27.668	-0.054	-0.054	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.017	-0.005	25.105	-0.055	-0.055	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.857	0.920	21.881	12.390	12.390	0.000	0.000	0.000	0.000
116	A	116	ILE	0	-0.004	-0.008	17.989	0.029	0.029	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.058	-0.027	13.990	-0.499	-0.499	0.000	0.000	0.000	0.000
118	A	118	ASN	0	0.063	0.025	13.201	0.789	0.789	0.000	0.000	0.000	0.000
119	A	119	LYS	1	0.904	0.951	7.918	31.062	31.062	0.000	0.000	0.000	0.000
120	A	120	TYR	0	0.052	0.016	6.740	1.067	1.067	0.000	0.000	0.000	0.000
128	A	128	VAL	0	-0.031	-0.017	6.288	2.005	2.005	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.971	0.981	8.629	24.234	24.234	0.000	0.000	0.000	0.000
130	A	130	ALA	0	0.074	0.026	12.386	0.173	0.173	0.000	0.000	0.000	0.000
131	A	131	GLU	-1	-0.820	-0.908	14.613	-15.228	-15.228	0.000	0.000	0.000	0.000
132	A	132	GLN	0	-0.003	0.010	12.171	1.374	1.374	0.000	0.000	0.000	0.000
133	A	133	VAL	0	-0.023	-0.005	11.802	0.452	0.452	0.000	0.000	0.000	0.000
134	A	134	LYS	1	0.876	0.934	14.491	15.232	15.232	0.000	0.000	0.000	0.000
135	A	135	ALA	0	0.036	0.018	18.072	0.676	0.676	0.000	0.000	0.000	0.000
136	A	136	SER	0	-0.033	-0.025	15.661	0.429	0.429	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.853	0.941	16.310	18.796	18.796	0.000	0.000	0.000	0.000
138	A	138	GLU	-1	-0.864	-0.942	20.349	-12.884	-12.884	0.000	0.000	0.000	0.000
139	A	139	MET	0	-0.013	0.013	21.228	0.894	0.894	0.000	0.000	0.000	0.000
140	A	140	GLY	0	0.018	0.011	21.867	0.487	0.487	0.000	0.000	0.000	0.000
141	A	141	GLU	-1	-0.885	-0.951	23.153	-11.539	-11.539	0.000	0.000	0.000	0.000
142	A	142	THR	0	-0.075	-0.055	25.992	0.584	0.584	0.000	0.000	0.000	0.000
143	A	143	LEU	0	-0.011	0.004	24.659	0.525	0.525	0.000	0.000	0.000	0.000
144	A	144	LEU	0	0.018	0.016	27.358	0.417	0.417	0.000	0.000	0.000	0.000
145	A	145	ARG	1	0.939	0.952	28.377	11.253	11.253	0.000	0.000	0.000	0.000
146	A	146	ALA	0	0.005	0.032	31.342	0.420	0.420	0.000	0.000	0.000	0.000
147	A	147	VAL	0	0.014	0.001	31.182	0.383	0.383	0.000	0.000	0.000	0.000
148	A	148	GLU	-1	-0.808	-0.875	33.187	-9.283	-9.283	0.000	0.000	0.000	0.000
149	A	149	SER	0	-0.011	-0.027	35.008	0.377	0.377	0.000	0.000	0.000	0.000
150	A	150	TYR	0	-0.025	-0.012	36.706	0.329	0.329	0.000	0.000	0.000	0.000
151	A	151	LEU	0	0.007	0.005	35.278	0.269	0.269	0.000	0.000	0.000	0.000
152	A	152	LEU	0	-0.013	0.000	38.613	0.231	0.231	0.000	0.000	0.000	0.000
153	A	153	ALA	0	-0.039	-0.013	41.185	0.221	0.221	0.000	0.000	0.000	0.000
154	A	154	HIS	1	0.834	0.913	41.333	7.812	7.812	0.000	0.000	0.000	0.000
155	A	155	SER	0	0.021	0.016	42.781	-0.168	-0.168	0.000	0.000	0.000	0.000
156	A	156	ASP	-1	-0.852	-0.931	44.423	-7.237	-7.237	0.000	0.000	0.000	0.000
157	A	157	ALA	0	0.011	0.016	40.425	-0.089	-0.089	0.000	0.000	0.000	0.000
158	A	158	TYR	0	-0.065	-0.085	36.961	-0.093	-0.093	0.000	0.000	0.000	0.000
159	A	159	ASN	-1	-0.957	-0.950	40.192	-7.548	-7.548	0.000	0.000	0.000	0.000

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