FMO DATABASE

FMODB ID: N81ZQ

Calculation Name: 2YV8-A-Xray547

Preferred Name: Galectin-8

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2YV8

Chain ID: A

ChEMBL ID: CHEMBL5475

UniProt ID: O00214

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	151
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1460393.513678
FMO2-HF: Nuclear repulsion	1401847.177206
FMO2-HF: Total energy	-58546.336472
FMO2-MP2: Total energy	-58718.563242

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:14:ASN)

Summations of interaction energy for fragment #1(A:14:ASN)

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.
-41.486	-39.571	0.058	-0.908	-1.065	-0.003

Interaction energy analysis for fragmet #1(A:14:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.850 / 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	16	GLN	0	0.048	0.022	3.367	0.477	2.165	0.047	-0.848	-0.887	-0.003
5	A	18	ILE	0	-0.040	-0.008	3.282	1.814	2.041	0.011	-0.060	-0.178	0.000
4	A	17	ASN	0	-0.025	-0.021	6.204	2.211	2.211	0.000	0.000	0.000	0.000
6	A	19	ILE	0	0.001	0.012	7.963	1.783	1.783	0.000	0.000	0.000	0.000
7	A	20	TYR	0	0.016	-0.014	6.344	-0.688	-0.688	0.000	0.000	0.000	0.000
8	A	21	ASN	0	-0.050	-0.024	12.340	1.144	1.144	0.000	0.000	0.000	0.000
9	A	22	PRO	0	-0.020	0.008	14.563	0.776	0.776	0.000	0.000	0.000	0.000
10	A	23	VAL	0	0.021	0.002	17.473	0.358	0.358	0.000	0.000	0.000	0.000
11	A	24	ILE	0	-0.026	0.005	19.244	-0.198	-0.198	0.000	0.000	0.000	0.000
12	A	25	PRO	0	-0.073	-0.049	22.887	0.504	0.504	0.000	0.000	0.000	0.000
13	A	26	TYR	0	0.056	0.027	16.307	-0.036	-0.036	0.000	0.000	0.000	0.000
14	A	27	VAL	0	-0.013	-0.027	21.354	0.196	0.196	0.000	0.000	0.000	0.000
15	A	28	GLY	0	-0.014	0.005	18.730	0.154	0.154	0.000	0.000	0.000	0.000
16	A	29	THR	0	0.001	0.003	18.955	0.076	0.076	0.000	0.000	0.000	0.000
17	A	30	ILE	0	-0.055	-0.032	14.945	-1.057	-1.057	0.000	0.000	0.000	0.000
18	A	31	PRO	0	-0.055	-0.028	12.822	0.644	0.644	0.000	0.000	0.000	0.000
19	A	32	ASP	-1	-0.864	-0.921	12.781	-23.940	-23.940	0.000	0.000	0.000	0.000
20	A	33	GLN	0	0.032	0.006	15.882	0.367	0.367	0.000	0.000	0.000	0.000
21	A	34	LEU	0	-0.020	0.001	15.972	-1.149	-1.149	0.000	0.000	0.000	0.000
22	A	35	ASP	-1	-0.885	-0.939	16.532	-15.998	-15.998	0.000	0.000	0.000	0.000
23	A	36	PRO	0	-0.102	-0.065	16.438	-0.783	-0.783	0.000	0.000	0.000	0.000
24	A	37	GLY	0	0.038	0.011	14.393	-0.168	-0.168	0.000	0.000	0.000	0.000
25	A	38	THR	0	-0.036	-0.024	12.224	-2.145	-2.145	0.000	0.000	0.000	0.000
26	A	39	LEU	0	-0.047	-0.022	8.239	1.585	1.585	0.000	0.000	0.000	0.000
27	A	40	ILE	0	0.006	0.000	11.030	-1.367	-1.367	0.000	0.000	0.000	0.000
28	A	41	VAL	0	-0.004	-0.006	8.128	1.167	1.167	0.000	0.000	0.000	0.000
29	A	42	ILE	0	-0.004	-0.005	10.769	-0.400	-0.400	0.000	0.000	0.000	0.000
30	A	43	CYS	0	0.005	0.016	10.808	0.703	0.703	0.000	0.000	0.000	0.000
31	A	44	GLY	0	0.028	0.004	13.361	0.201	0.201	0.000	0.000	0.000	0.000
32	A	45	HIS	0	-0.044	-0.029	16.763	-0.543	-0.543	0.000	0.000	0.000	0.000
33	A	46	VAL	0	-0.025	0.008	20.297	0.223	0.223	0.000	0.000	0.000	0.000
34	A	47	PRO	0	0.015	0.015	23.765	0.197	0.197	0.000	0.000	0.000	0.000
35	A	48	SER	0	0.015	-0.052	26.277	0.051	0.051	0.000	0.000	0.000	0.000
36	A	49	ASP	-1	-0.844	-0.905	29.564	-9.912	-9.912	0.000	0.000	0.000	0.000
37	A	50	ALA	0	0.003	0.013	27.287	0.147	0.147	0.000	0.000	0.000	0.000
38	A	51	ASP	-1	-0.805	-0.893	29.306	-8.843	-8.843	0.000	0.000	0.000	0.000
39	A	52	ARG	1	0.850	0.912	28.738	10.324	10.324	0.000	0.000	0.000	0.000
40	A	53	PHE	0	0.005	0.023	20.726	0.132	0.132	0.000	0.000	0.000	0.000
41	A	54	GLN	0	-0.035	-0.019	24.329	0.615	0.615	0.000	0.000	0.000	0.000
42	A	55	VAL	0	0.031	0.022	18.346	-0.225	-0.225	0.000	0.000	0.000	0.000
43	A	56	ASP	-1	-0.773	-0.869	21.561	-11.605	-11.605	0.000	0.000	0.000	0.000
44	A	57	LEU	0	0.006	0.006	18.374	-0.372	-0.372	0.000	0.000	0.000	0.000
45	A	58	GLN	0	-0.006	-0.020	22.092	0.668	0.668	0.000	0.000	0.000	0.000
46	A	59	ASN	0	-0.007	0.011	23.715	-0.682	-0.682	0.000	0.000	0.000	0.000
47	A	60	GLY	0	0.078	0.042	25.224	0.582	0.582	0.000	0.000	0.000	0.000
48	A	61	SER	0	-0.009	-0.026	24.798	0.053	0.053	0.000	0.000	0.000	0.000
49	A	62	SER	0	-0.025	-0.015	26.530	0.257	0.257	0.000	0.000	0.000	0.000
50	A	63	VAL	0	0.017	0.001	29.971	-0.056	-0.056	0.000	0.000	0.000	0.000
51	A	64	LYS	1	0.924	0.968	32.082	8.298	8.298	0.000	0.000	0.000	0.000
52	A	65	PRO	0	0.041	0.023	35.554	0.092	0.092	0.000	0.000	0.000	0.000
53	A	66	ARG	1	0.859	0.938	28.423	10.190	10.190	0.000	0.000	0.000	0.000
54	A	67	ALA	0	0.011	0.010	28.314	0.168	0.168	0.000	0.000	0.000	0.000
55	A	68	ASP	-1	-0.838	-0.914	29.772	-10.000	-10.000	0.000	0.000	0.000	0.000
56	A	69	VAL	0	-0.053	-0.023	25.698	-0.468	-0.468	0.000	0.000	0.000	0.000
57	A	70	ALA	0	0.054	0.022	24.477	0.351	0.351	0.000	0.000	0.000	0.000
58	A	71	PHE	0	-0.025	-0.021	20.325	0.245	0.245	0.000	0.000	0.000	0.000
59	A	72	HIS	0	-0.092	-0.042	23.759	-0.056	-0.056	0.000	0.000	0.000	0.000
60	A	73	PHE	0	0.059	0.024	20.651	0.377	0.377	0.000	0.000	0.000	0.000
61	A	74	ASN	0	0.018	-0.014	23.666	0.158	0.158	0.000	0.000	0.000	0.000
62	A	75	PRO	0	0.017	0.028	22.941	0.522	0.522	0.000	0.000	0.000	0.000
63	A	76	ARG	1	0.780	0.865	26.204	9.967	9.967	0.000	0.000	0.000	0.000
64	A	77	PHE	0	0.038	0.009	24.809	0.030	0.030	0.000	0.000	0.000	0.000
65	A	78	LYS	1	0.834	0.915	30.885	8.889	8.889	0.000	0.000	0.000	0.000
66	A	79	ARG	1	0.931	0.953	34.746	8.026	8.026	0.000	0.000	0.000	0.000
67	A	80	ALA	0	0.043	0.025	34.338	-0.057	-0.057	0.000	0.000	0.000	0.000
68	A	81	GLY	0	0.000	0.019	30.819	-0.254	-0.254	0.000	0.000	0.000	0.000
69	A	82	CYS	0	-0.081	-0.040	29.812	0.207	0.207	0.000	0.000	0.000	0.000
70	A	83	ILE	0	0.020	0.010	23.471	-0.268	-0.268	0.000	0.000	0.000	0.000
71	A	84	VAL	0	-0.039	-0.008	27.433	0.297	0.297	0.000	0.000	0.000	0.000
72	A	85	CYS	0	-0.004	0.015	25.530	-0.529	-0.529	0.000	0.000	0.000	0.000
73	A	86	ASN	0	0.014	-0.003	27.773	0.457	0.457	0.000	0.000	0.000	0.000
74	A	87	THR	0	-0.006	0.006	27.951	-0.409	-0.409	0.000	0.000	0.000	0.000
75	A	88	LEU	0	-0.076	-0.022	29.921	0.402	0.402	0.000	0.000	0.000	0.000
76	A	89	ILE	0	0.046	0.007	31.326	-0.249	-0.249	0.000	0.000	0.000	0.000
77	A	90	ASN	0	-0.022	-0.015	34.057	0.318	0.318	0.000	0.000	0.000	0.000
78	A	91	GLU	-1	-0.849	-0.916	35.061	-8.333	-8.333	0.000	0.000	0.000	0.000
79	A	92	LYS	1	0.925	0.970	36.213	8.252	8.252	0.000	0.000	0.000	0.000
80	A	93	TRP	0	0.000	0.003	29.469	-0.289	-0.289	0.000	0.000	0.000	0.000
81	A	94	GLY	0	0.017	0.020	33.879	0.283	0.283	0.000	0.000	0.000	0.000
82	A	95	ARG	1	0.947	0.972	35.280	8.395	8.395	0.000	0.000	0.000	0.000
83	A	96	GLU	-1	-0.826	-0.901	32.653	-9.519	-9.519	0.000	0.000	0.000	0.000
84	A	97	GLU	-1	-0.854	-0.909	29.703	-10.222	-10.222	0.000	0.000	0.000	0.000
85	A	98	ILE	0	-0.026	-0.015	30.157	-0.316	-0.316	0.000	0.000	0.000	0.000
86	A	99	THR	0	0.012	0.010	26.238	0.038	0.038	0.000	0.000	0.000	0.000
87	A	100	TYR	0	0.025	-0.014	29.320	-0.071	-0.071	0.000	0.000	0.000	0.000
88	A	101	ASP	-1	-0.860	-0.902	26.676	-11.224	-11.224	0.000	0.000	0.000	0.000
89	A	102	THR	0	0.026	0.009	25.797	-0.604	-0.604	0.000	0.000	0.000	0.000
90	A	103	PRO	0	0.001	0.006	21.668	0.260	0.260	0.000	0.000	0.000	0.000
91	A	104	PHE	0	-0.010	-0.002	19.404	-0.158	-0.158	0.000	0.000	0.000	0.000
92	A	105	LYS	1	0.959	0.967	23.884	11.820	11.820	0.000	0.000	0.000	0.000
93	A	106	ARG	1	0.904	0.922	25.262	9.243	9.243	0.000	0.000	0.000	0.000
94	A	107	GLU	-1	-0.818	-0.871	26.000	-10.133	-10.133	0.000	0.000	0.000	0.000
95	A	108	LYS	1	0.867	0.950	22.456	12.305	12.305	0.000	0.000	0.000	0.000
96	A	109	SER	0	0.040	0.025	17.526	0.261	0.261	0.000	0.000	0.000	0.000
97	A	110	PHE	0	-0.057	-0.042	16.395	0.668	0.668	0.000	0.000	0.000	0.000
98	A	111	GLU	-1	-0.879	-0.935	10.559	-24.381	-24.381	0.000	0.000	0.000	0.000
99	A	112	ILE	0	-0.042	-0.021	14.065	1.219	1.219	0.000	0.000	0.000	0.000
100	A	113	VAL	0	0.043	0.018	10.898	-1.642	-1.642	0.000	0.000	0.000	0.000
101	A	114	ILE	0	-0.003	-0.003	13.265	1.702	1.702	0.000	0.000	0.000	0.000
102	A	115	MET	0	0.028	0.021	13.939	-1.645	-1.645	0.000	0.000	0.000	0.000
103	A	116	VAL	0	-0.015	-0.006	15.463	1.814	1.814	0.000	0.000	0.000	0.000
104	A	117	LEU	0	0.021	0.015	17.199	-0.356	-0.356	0.000	0.000	0.000	0.000
105	A	118	LYS	1	0.993	0.994	19.803	13.193	13.193	0.000	0.000	0.000	0.000
106	A	119	ASP	-1	-0.818	-0.898	22.688	-12.410	-12.410	0.000	0.000	0.000	0.000
107	A	120	LYS	1	0.834	0.903	22.645	13.429	13.429	0.000	0.000	0.000	0.000
108	A	121	PHE	0	0.050	0.020	19.331	-0.590	-0.590	0.000	0.000	0.000	0.000
109	A	122	GLN	0	-0.033	-0.035	17.117	0.179	0.179	0.000	0.000	0.000	0.000
110	A	123	VAL	0	0.005	0.006	17.588	-0.823	-0.823	0.000	0.000	0.000	0.000
111	A	124	ALA	0	0.023	0.014	15.391	0.942	0.942	0.000	0.000	0.000	0.000
112	A	125	VAL	0	0.006	-0.009	16.312	-0.628	-0.628	0.000	0.000	0.000	0.000
113	A	126	ASN	0	0.002	-0.004	15.445	0.050	0.050	0.000	0.000	0.000	0.000
114	A	127	GLY	0	0.056	0.041	14.824	0.569	0.569	0.000	0.000	0.000	0.000
115	A	128	LYS	1	0.821	0.920	15.698	12.514	12.514	0.000	0.000	0.000	0.000
116	A	129	HIS	0	0.030	0.018	19.213	-0.853	-0.853	0.000	0.000	0.000	0.000
117	A	130	THR	0	-0.050	-0.028	20.250	0.648	0.648	0.000	0.000	0.000	0.000
118	A	131	LEU	0	-0.004	-0.008	21.727	0.647	0.647	0.000	0.000	0.000	0.000
119	A	132	LEU	0	-0.016	-0.011	22.012	-0.726	-0.726	0.000	0.000	0.000	0.000
120	A	133	TYR	0	0.009	-0.013	23.892	0.500	0.500	0.000	0.000	0.000	0.000
121	A	134	GLY	0	0.048	0.031	24.785	-0.447	-0.447	0.000	0.000	0.000	0.000
122	A	135	HIS	1	0.798	0.892	21.752	13.721	13.721	0.000	0.000	0.000	0.000
123	A	136	ARG	1	0.813	0.888	26.953	10.498	10.498	0.000	0.000	0.000	0.000
124	A	137	ILE	0	-0.009	-0.001	27.657	0.369	0.369	0.000	0.000	0.000	0.000
125	A	138	GLY	0	-0.023	-0.003	26.808	-0.311	-0.311	0.000	0.000	0.000	0.000
126	A	139	PRO	0	0.002	-0.010	21.238	0.088	0.088	0.000	0.000	0.000	0.000
127	A	140	GLU	-1	-0.776	-0.886	22.301	-12.591	-12.591	0.000	0.000	0.000	0.000
128	A	141	LYS	1	0.826	0.903	23.653	11.248	11.248	0.000	0.000	0.000	0.000
129	A	142	ILE	0	-0.053	-0.019	20.661	0.333	0.333	0.000	0.000	0.000	0.000
130	A	143	ASP	-1	-0.761	-0.849	20.814	-13.930	-13.930	0.000	0.000	0.000	0.000
131	A	144	THR	0	-0.047	-0.032	20.387	-0.483	-0.483	0.000	0.000	0.000	0.000
132	A	145	LEU	0	-0.021	-0.007	15.428	0.070	0.070	0.000	0.000	0.000	0.000
133	A	146	GLY	0	0.024	0.016	19.444	0.124	0.124	0.000	0.000	0.000	0.000
134	A	147	ILE	0	-0.019	-0.019	16.746	-0.304	-0.304	0.000	0.000	0.000	0.000
135	A	148	TYR	0	-0.012	-0.017	21.440	0.385	0.385	0.000	0.000	0.000	0.000
136	A	149	GLY	0	-0.017	-0.011	24.893	-0.072	-0.072	0.000	0.000	0.000	0.000
137	A	150	LYS	1	0.832	0.898	26.000	9.676	9.676	0.000	0.000	0.000	0.000
138	A	151	VAL	0	-0.002	-0.018	20.438	0.027	0.027	0.000	0.000	0.000	0.000
139	A	152	ASN	0	0.028	0.031	20.478	0.279	0.279	0.000	0.000	0.000	0.000
140	A	153	ILE	0	0.002	-0.004	14.907	-0.319	-0.319	0.000	0.000	0.000	0.000
141	A	154	HIS	0	0.037	0.016	13.641	0.080	0.080	0.000	0.000	0.000	0.000
142	A	155	SER	0	-0.010	-0.019	9.099	-0.103	-0.103	0.000	0.000	0.000	0.000
143	A	156	ILE	0	0.004	0.018	11.111	1.032	1.032	0.000	0.000	0.000	0.000
144	A	157	GLY	0	0.027	0.016	7.495	-1.513	-1.513	0.000	0.000	0.000	0.000
145	A	158	PHE	0	0.028	0.012	7.812	2.715	2.715	0.000	0.000	0.000	0.000
146	A	159	SER	0	-0.011	-0.014	6.045	-10.206	-10.206	0.000	0.000	0.000	0.000
147	A	160	GLY	0	0.083	0.055	7.969	4.257	4.257	0.000	0.000	0.000	0.000
148	A	161	PRO	0	-0.009	0.009	9.287	-2.678	-2.678	0.000	0.000	0.000	0.000
149	A	162	SER	0	-0.048	-0.030	11.187	1.162	1.162	0.000	0.000	0.000	0.000
150	A	163	SER	0	-0.053	-0.040	5.374	-1.513	-1.513	0.000	0.000	0.000	0.000
151	A	164	GLY	-1	-0.933	-0.948	6.479	-41.034	-41.034	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:14:ASN)