FMO DATABASE

FMODB ID: VVYZ1

Calculation Name: 1BEB-A-Xray547

Preferred Name: Beta-lactoglobulin

Target Type: SINGLE PROTEIN

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1BEB

Chain ID: A

ChEMBL ID: CHEMBL1075053

UniProt ID: P02754

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	154
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1582637.618694
FMO2-HF: Nuclear repulsion	1519741.032131
FMO2-HF: Total energy	-62896.586563
FMO2-MP2: Total energy	-63076.054066

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:GLN)

Summations of interaction energy for fragment #1(A:5: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.
-97.489	-95.452	-0.023	-0.8	-1.213	-0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.861 / q_NPA : 0.916

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	MET	0	0.041	0.039	3.859	0.695	2.312	-0.020	-0.737	-0.859	-0.002
4	A	8	LYS	1	0.837	0.905	4.389	47.591	47.720	-0.001	-0.007	-0.120	0.000
91	A	95	LEU	0	-0.024	-0.023	4.000	-6.504	-6.298	-0.001	-0.053	-0.152	0.000
138	A	143	LEU	0	-0.010	0.008	4.596	-1.557	-1.472	-0.001	-0.003	-0.082	0.000
5	A	9	GLY	0	0.020	0.007	8.853	1.208	1.208	0.000	0.000	0.000	0.000
6	A	10	LEU	0	-0.015	-0.002	11.322	0.668	0.668	0.000	0.000	0.000	0.000
7	A	11	ASP	-1	-0.840	-0.919	13.072	-14.991	-14.991	0.000	0.000	0.000	0.000
8	A	12	ILE	0	0.021	0.009	14.931	0.044	0.044	0.000	0.000	0.000	0.000
9	A	13	GLN	0	0.055	0.012	17.452	0.046	0.046	0.000	0.000	0.000	0.000
10	A	14	LYS	1	0.835	0.913	18.534	16.003	16.003	0.000	0.000	0.000	0.000
11	A	15	VAL	0	-0.018	-0.011	15.406	-0.013	-0.013	0.000	0.000	0.000	0.000
12	A	16	ALA	0	-0.011	0.016	18.795	0.088	0.088	0.000	0.000	0.000	0.000
13	A	17	GLY	0	0.026	0.032	22.357	0.132	0.132	0.000	0.000	0.000	0.000
14	A	18	THR	0	0.017	-0.003	22.829	-0.420	-0.420	0.000	0.000	0.000	0.000
15	A	19	TRP	0	-0.096	-0.056	17.216	-0.863	-0.863	0.000	0.000	0.000	0.000
16	A	20	TYR	0	0.087	0.056	20.874	0.475	0.475	0.000	0.000	0.000	0.000
17	A	21	SER	0	-0.002	-0.028	18.002	-0.587	-0.587	0.000	0.000	0.000	0.000
18	A	22	LEU	0	0.011	0.026	17.810	0.476	0.476	0.000	0.000	0.000	0.000
19	A	23	ALA	0	-0.007	-0.019	15.770	0.656	0.656	0.000	0.000	0.000	0.000
20	A	24	MET	0	-0.027	0.006	14.573	-0.912	-0.912	0.000	0.000	0.000	0.000
21	A	25	ALA	0	-0.011	-0.012	12.438	0.978	0.978	0.000	0.000	0.000	0.000
22	A	26	ALA	0	0.060	0.028	13.121	-1.278	-1.278	0.000	0.000	0.000	0.000
23	A	27	SER	0	0.010	-0.016	12.102	0.441	0.441	0.000	0.000	0.000	0.000
24	A	28	ASP	-1	-0.799	-0.880	13.906	-14.241	-14.241	0.000	0.000	0.000	0.000
25	A	29	ILE	0	-0.016	-0.022	17.651	-0.149	-0.149	0.000	0.000	0.000	0.000
26	A	30	SER	0	-0.052	-0.053	20.340	0.200	0.200	0.000	0.000	0.000	0.000
27	A	31	LEU	0	-0.002	0.011	16.063	0.415	0.415	0.000	0.000	0.000	0.000
28	A	32	LEU	0	-0.015	-0.023	16.691	-0.215	-0.215	0.000	0.000	0.000	0.000
29	A	33	ASP	-1	-0.912	-0.943	20.417	-11.778	-11.778	0.000	0.000	0.000	0.000
30	A	34	ALA	0	-0.026	-0.018	23.787	0.268	0.268	0.000	0.000	0.000	0.000
31	A	35	GLN	0	-0.009	-0.017	25.125	-0.738	-0.738	0.000	0.000	0.000	0.000
32	A	36	SER	0	-0.012	-0.001	26.226	-0.234	-0.234	0.000	0.000	0.000	0.000
33	A	37	ALA	0	0.008	0.030	22.231	0.074	0.074	0.000	0.000	0.000	0.000
34	A	38	PRO	0	-0.058	-0.025	21.560	-0.097	-0.097	0.000	0.000	0.000	0.000
35	A	39	LEU	0	0.025	-0.003	15.643	-0.399	-0.399	0.000	0.000	0.000	0.000
36	A	40	ARG	1	0.849	0.935	18.642	12.477	12.477	0.000	0.000	0.000	0.000
37	A	41	VAL	0	-0.044	-0.023	18.668	0.699	0.699	0.000	0.000	0.000	0.000
38	A	42	TYR	0	0.041	0.016	19.507	-1.150	-1.150	0.000	0.000	0.000	0.000
39	A	43	VAL	0	-0.050	-0.029	17.491	0.368	0.368	0.000	0.000	0.000	0.000
40	A	44	GLU	-1	-0.772	-0.851	20.806	-11.192	-11.192	0.000	0.000	0.000	0.000
41	A	45	GLU	-1	-0.908	-0.984	22.938	-11.987	-11.987	0.000	0.000	0.000	0.000
42	A	46	LEU	0	-0.008	0.006	16.202	-0.555	-0.555	0.000	0.000	0.000	0.000
43	A	47	LYS	1	0.853	0.925	20.711	12.638	12.638	0.000	0.000	0.000	0.000
44	A	48	PRO	0	-0.009	0.013	20.148	-0.056	-0.056	0.000	0.000	0.000	0.000
45	A	49	THR	0	0.027	0.006	21.643	0.701	0.701	0.000	0.000	0.000	0.000
46	A	50	PRO	0	-0.025	-0.026	23.590	-0.318	-0.318	0.000	0.000	0.000	0.000
47	A	51	GLU	-1	-0.883	-0.943	23.885	-12.371	-12.371	0.000	0.000	0.000	0.000
48	A	52	GLY	0	0.001	0.012	20.262	-0.390	-0.390	0.000	0.000	0.000	0.000
49	A	53	ASP	-1	-0.851	-0.921	18.561	-15.879	-15.879	0.000	0.000	0.000	0.000
50	A	54	LEU	0	-0.021	-0.023	15.604	0.231	0.231	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.788	-0.877	18.944	-12.052	-12.052	0.000	0.000	0.000	0.000
52	A	56	ILE	0	-0.039	-0.018	17.451	-0.228	-0.228	0.000	0.000	0.000	0.000
53	A	57	LEU	0	-0.010	-0.006	20.542	0.451	0.451	0.000	0.000	0.000	0.000
54	A	58	LEU	0	0.013	-0.006	19.433	-0.513	-0.513	0.000	0.000	0.000	0.000
55	A	59	GLN	0	0.032	0.013	23.083	0.382	0.382	0.000	0.000	0.000	0.000
56	A	60	LYS	1	0.858	0.907	23.814	11.566	11.566	0.000	0.000	0.000	0.000
57	A	61	TRP	0	0.073	0.046	25.924	0.414	0.414	0.000	0.000	0.000	0.000
58	A	62	GLU	-1	-0.831	-0.902	27.777	-11.413	-11.413	0.000	0.000	0.000	0.000
59	A	63	ASN	0	-0.029	-0.002	30.737	0.211	0.211	0.000	0.000	0.000	0.000
60	A	64	GLY	0	-0.040	-0.032	33.497	-0.177	-0.177	0.000	0.000	0.000	0.000
61	A	65	GLU	-1	-0.916	-0.949	34.408	-8.621	-8.621	0.000	0.000	0.000	0.000
62	A	160	CYS	-1	-0.887	-0.920	26.437	-11.691	-11.691	0.000	0.000	0.000	0.000
63	A	67	ALA	0	-0.002	0.009	29.453	0.138	0.138	0.000	0.000	0.000	0.000
64	A	68	GLN	0	-0.027	-0.025	27.500	-0.282	-0.282	0.000	0.000	0.000	0.000
65	A	69	LYS	1	0.778	0.862	24.353	11.671	11.671	0.000	0.000	0.000	0.000
66	A	70	LYS	1	0.865	0.930	24.105	11.141	11.141	0.000	0.000	0.000	0.000
67	A	71	ILE	0	-0.001	0.006	18.377	0.188	0.188	0.000	0.000	0.000	0.000
68	A	72	ILE	0	0.008	0.003	21.136	0.004	0.004	0.000	0.000	0.000	0.000
69	A	73	ALA	0	0.012	-0.003	15.641	-0.264	-0.264	0.000	0.000	0.000	0.000
70	A	74	GLU	-1	-0.930	-0.952	17.737	-13.998	-13.998	0.000	0.000	0.000	0.000
71	A	75	LYS	1	0.845	0.915	15.901	12.708	12.708	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.038	-0.034	12.575	0.201	0.201	0.000	0.000	0.000	0.000
73	A	77	LYS	1	0.937	0.950	13.952	17.231	17.231	0.000	0.000	0.000	0.000
74	A	78	ILE	0	-0.050	-0.013	7.920	-0.078	-0.078	0.000	0.000	0.000	0.000
75	A	79	PRO	0	0.044	0.015	11.401	-0.703	-0.703	0.000	0.000	0.000	0.000
76	A	80	ALA	0	0.002	0.014	8.047	0.630	0.630	0.000	0.000	0.000	0.000
77	A	81	VAL	0	-0.041	-0.021	7.297	-3.580	-3.580	0.000	0.000	0.000	0.000
78	A	82	PHE	0	0.012	0.029	9.953	1.847	1.847	0.000	0.000	0.000	0.000
79	A	83	LYS	1	0.852	0.931	12.596	18.577	18.577	0.000	0.000	0.000	0.000
80	A	84	ILE	0	-0.018	-0.002	14.677	0.522	0.522	0.000	0.000	0.000	0.000
81	A	85	ASP	-1	-0.907	-0.956	17.227	-14.002	-14.002	0.000	0.000	0.000	0.000
82	A	86	ALA	0	0.022	0.010	18.969	0.749	0.749	0.000	0.000	0.000	0.000
83	A	87	LEU	0	-0.013	-0.007	18.621	-0.618	-0.618	0.000	0.000	0.000	0.000
84	A	88	ASN	0	0.002	0.003	19.458	0.204	0.204	0.000	0.000	0.000	0.000
85	A	89	GLU	-1	-0.765	-0.852	13.990	-21.345	-21.345	0.000	0.000	0.000	0.000
86	A	90	ASN	0	0.015	-0.022	13.713	-0.609	-0.609	0.000	0.000	0.000	0.000
87	A	91	LYS	1	0.782	0.896	8.070	30.518	30.518	0.000	0.000	0.000	0.000
88	A	92	VAL	0	0.057	0.039	10.805	0.019	0.019	0.000	0.000	0.000	0.000
89	A	93	LEU	0	-0.071	-0.027	5.455	-1.293	-1.293	0.000	0.000	0.000	0.000
90	A	94	VAL	0	0.065	0.027	7.633	0.090	0.090	0.000	0.000	0.000	0.000
92	A	96	ASP	-1	-0.830	-0.925	5.834	-30.954	-30.954	0.000	0.000	0.000	0.000
93	A	97	THR	0	0.004	-0.020	8.380	2.085	2.085	0.000	0.000	0.000	0.000
94	A	98	ASP	-1	-0.752	-0.846	12.239	-17.844	-17.844	0.000	0.000	0.000	0.000
95	A	99	TYR	0	-0.022	-0.022	14.435	1.215	1.215	0.000	0.000	0.000	0.000
96	A	100	LYS	1	0.897	0.947	17.583	15.006	15.006	0.000	0.000	0.000	0.000
97	A	101	LYS	1	0.891	0.935	18.393	16.864	16.864	0.000	0.000	0.000	0.000
98	A	102	TYR	0	0.041	0.016	11.028	0.709	0.709	0.000	0.000	0.000	0.000
99	A	103	LEU	0	-0.008	0.008	12.624	-0.673	-0.673	0.000	0.000	0.000	0.000
100	A	104	LEU	0	-0.003	0.018	8.033	0.257	0.257	0.000	0.000	0.000	0.000
101	A	105	PHE	0	-0.018	-0.020	8.822	-2.492	-2.492	0.000	0.000	0.000	0.000
102	A	106	CYS	0	-0.086	-0.043	7.096	-4.436	-4.436	0.000	0.000	0.000	0.000
103	A	107	MET	0	-0.017	-0.003	9.157	0.643	0.643	0.000	0.000	0.000	0.000
104	A	108	GLU	-1	-0.706	-0.883	7.193	-35.880	-35.880	0.000	0.000	0.000	0.000
105	A	109	ASN	0	-0.002	0.008	11.570	0.090	0.090	0.000	0.000	0.000	0.000
106	A	110	SER	0	-0.035	-0.038	11.666	-0.168	-0.168	0.000	0.000	0.000	0.000
107	A	111	ALA	0	-0.059	-0.024	12.640	-0.158	-0.158	0.000	0.000	0.000	0.000
108	A	112	GLU	-1	-0.886	-0.943	14.930	-17.647	-17.647	0.000	0.000	0.000	0.000
109	A	113	PRO	0	0.019	0.001	9.959	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	114	GLU	-1	-0.942	-0.951	12.119	-21.835	-21.835	0.000	0.000	0.000	0.000
111	A	115	GLN	0	-0.051	-0.011	13.877	0.075	0.075	0.000	0.000	0.000	0.000
112	A	116	SER	0	-0.045	-0.045	13.335	1.104	1.104	0.000	0.000	0.000	0.000
113	A	117	LEU	0	-0.047	-0.012	7.489	-0.756	-0.756	0.000	0.000	0.000	0.000
114	A	118	VAL	0	0.053	0.038	11.421	0.604	0.604	0.000	0.000	0.000	0.000
115	A	120	GLN	0	0.036	0.010	10.683	2.595	2.595	0.000	0.000	0.000	0.000
116	A	121	CYS	0	-0.076	-0.031	11.675	-2.080	-2.080	0.000	0.000	0.000	0.000
117	A	122	LEU	0	-0.010	0.005	13.922	1.328	1.328	0.000	0.000	0.000	0.000
118	A	123	VAL	0	0.042	0.006	16.473	-0.848	-0.848	0.000	0.000	0.000	0.000
119	A	124	ARG	1	0.777	0.880	19.317	15.380	15.380	0.000	0.000	0.000	0.000
120	A	125	THR	0	-0.044	-0.038	21.966	0.310	0.310	0.000	0.000	0.000	0.000
121	A	126	PRO	0	0.030	0.027	23.703	-0.549	-0.549	0.000	0.000	0.000	0.000
122	A	127	GLU	-1	-0.891	-0.935	24.355	-11.372	-11.372	0.000	0.000	0.000	0.000
123	A	128	VAL	0	0.003	-0.012	21.601	-0.629	-0.629	0.000	0.000	0.000	0.000
124	A	129	ASP	-1	-0.835	-0.921	19.178	-15.961	-15.961	0.000	0.000	0.000	0.000
125	A	130	ASP	-1	-0.839	-0.944	18.723	-14.986	-14.986	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-0.949	-0.967	17.088	-16.675	-16.675	0.000	0.000	0.000	0.000
127	A	132	ALA	0	-0.041	-0.021	14.607	-1.749	-1.749	0.000	0.000	0.000	0.000
128	A	133	LEU	0	-0.014	-0.005	13.893	-1.870	-1.870	0.000	0.000	0.000	0.000
129	A	134	GLU	-1	-0.846	-0.919	14.174	-19.706	-19.706	0.000	0.000	0.000	0.000
130	A	135	LYS	1	0.845	0.902	10.230	22.947	22.947	0.000	0.000	0.000	0.000
131	A	136	PHE	0	-0.016	0.002	9.560	-3.397	-3.397	0.000	0.000	0.000	0.000
132	A	137	ASP	-1	-0.778	-0.868	10.039	-22.915	-22.915	0.000	0.000	0.000	0.000
133	A	138	LYS	1	0.733	0.860	9.281	20.013	20.013	0.000	0.000	0.000	0.000
134	A	139	ALA	0	-0.036	-0.010	5.775	-2.789	-2.789	0.000	0.000	0.000	0.000
135	A	140	LEU	0	0.020	0.005	5.976	-5.875	-5.875	0.000	0.000	0.000	0.000
136	A	141	LYS	1	0.888	0.952	8.489	24.934	24.934	0.000	0.000	0.000	0.000
137	A	142	ALA	0	-0.054	-0.018	5.559	1.859	1.859	0.000	0.000	0.000	0.000
139	A	144	PRO	0	0.023	0.020	8.532	2.435	2.435	0.000	0.000	0.000	0.000
140	A	145	MET	0	-0.043	-0.022	9.062	1.814	1.814	0.000	0.000	0.000	0.000
141	A	146	HIS	1	0.824	0.891	13.302	19.385	19.385	0.000	0.000	0.000	0.000
142	A	147	ILE	0	0.000	0.024	16.399	1.109	1.109	0.000	0.000	0.000	0.000
143	A	148	ARG	1	0.846	0.890	15.341	17.214	17.214	0.000	0.000	0.000	0.000
144	A	149	LEU	0	-0.025	-0.001	17.391	1.066	1.066	0.000	0.000	0.000	0.000
145	A	150	SER	0	-0.016	-0.024	18.145	-1.161	-1.161	0.000	0.000	0.000	0.000
146	A	151	PHE	0	-0.021	0.003	19.978	0.604	0.604	0.000	0.000	0.000	0.000
147	A	152	ASN	0	0.010	-0.002	23.322	-0.179	-0.179	0.000	0.000	0.000	0.000
148	A	153	PRO	0	0.062	0.011	26.297	-0.065	-0.065	0.000	0.000	0.000	0.000
149	A	154	THR	0	0.022	0.013	27.963	-0.017	-0.017	0.000	0.000	0.000	0.000
150	A	155	GLN	0	-0.009	-0.009	26.297	-0.065	-0.065	0.000	0.000	0.000	0.000
151	A	156	LEU	0	-0.076	-0.010	22.270	-0.282	-0.282	0.000	0.000	0.000	0.000
152	A	157	GLU	-1	-0.987	-0.998	25.931	-10.246	-10.246	0.000	0.000	0.000	0.000
153	A	158	GLU	-1	-0.959	-0.960	28.806	-9.150	-9.150	0.000	0.000	0.000	0.000
154	A	159	GLN	0	-0.099	-0.061	28.383	-0.415	-0.415	0.000	0.000	0.000	0.000

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