FMO DATABASE

FMODB ID: J4Z99

Calculation Name: 2GAL-A-Xray547

Preferred Name: Galectin-7

Target Type: SINGLE PROTEIN

Ligand Name: beta-d-galactopyranose

Ligand 3-letter code: GAL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2GAL

Chain ID: A

ChEMBL ID: CHEMBL5008

UniProt ID: P47929

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	133
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1171393.512408
FMO2-HF: Nuclear repulsion	1120659.047218
FMO2-HF: Total energy	-50734.465191
FMO2-MP2: Total energy	-50886.111185

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:3:VAL)

Summations of interaction energy for fragment #1(A:3:VAL)

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.
-27.427	-22.302	0.632	-1.849	-3.911	-0.01

Interaction energy analysis for fragmet #1(A:3:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.865 / q_NPA : 0.922

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

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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	5	HIS	0	0.029	0.026	3.053	4.966	7.495	0.221	-0.901	-1.849	-0.004
4	A	6	LYS	1	0.915	0.934	3.747	31.794	31.925	0.010	-0.017	-0.124	0.000
122	A	124	GLY	0	-0.003	0.000	4.788	-8.349	-8.392	-0.001	-0.025	0.069	0.000
124	A	126	ASP	-1	-0.810	-0.888	4.496	-45.785	-45.750	-0.001	-0.012	-0.023	0.000
125	A	127	VAL	0	-0.027	-0.025	4.092	6.111	6.305	-0.001	-0.036	-0.158	0.000
126	A	128	GLN	0	-0.047	-0.023	3.321	-15.087	-13.973	0.029	-0.551	-0.592	-0.004
127	A	129	LEU	0	-0.036	-0.019	2.874	5.887	6.899	0.376	-0.293	-1.096	-0.002
128	A	130	ASP	-1	-0.862	-0.903	4.417	-25.566	-25.413	-0.001	-0.014	-0.138	0.000
5	A	7	SER	0	-0.021	-0.019	7.406	0.570	0.570	0.000	0.000	0.000	0.000
6	A	8	SER	0	-0.006	-0.007	10.330	0.952	0.952	0.000	0.000	0.000	0.000
7	A	9	LEU	0	-0.017	-0.016	13.720	0.173	0.173	0.000	0.000	0.000	0.000
8	A	10	PRO	0	0.026	0.011	16.933	0.467	0.467	0.000	0.000	0.000	0.000
9	A	11	GLU	-1	-0.916	-0.966	20.086	-12.099	-12.099	0.000	0.000	0.000	0.000
10	A	12	GLY	0	-0.045	-0.004	19.843	0.407	0.407	0.000	0.000	0.000	0.000
11	A	13	ILE	0	-0.036	-0.021	18.153	-0.252	-0.252	0.000	0.000	0.000	0.000
12	A	14	ARG	1	0.955	0.967	21.354	11.340	11.340	0.000	0.000	0.000	0.000
13	A	15	PRO	0	0.010	0.017	23.892	-0.498	-0.498	0.000	0.000	0.000	0.000
14	A	16	GLY	0	-0.022	-0.011	25.474	0.287	0.287	0.000	0.000	0.000	0.000
15	A	17	THR	0	-0.022	-0.010	18.994	-0.178	-0.178	0.000	0.000	0.000	0.000
16	A	18	VAL	0	-0.041	-0.029	17.924	-0.044	-0.044	0.000	0.000	0.000	0.000
17	A	19	LEU	0	0.013	0.013	13.196	-0.599	-0.599	0.000	0.000	0.000	0.000
18	A	20	ARG	1	0.942	0.972	14.105	18.303	18.303	0.000	0.000	0.000	0.000
19	A	21	ILE	0	-0.016	-0.015	8.310	-1.396	-1.396	0.000	0.000	0.000	0.000
20	A	22	ARG	1	0.854	0.910	9.545	20.155	20.155	0.000	0.000	0.000	0.000
21	A	23	GLY	0	0.028	0.008	7.749	-3.696	-3.696	0.000	0.000	0.000	0.000
22	A	24	LEU	0	-0.008	0.018	7.734	3.312	3.312	0.000	0.000	0.000	0.000
23	A	25	VAL	0	0.037	0.021	7.949	-4.465	-4.465	0.000	0.000	0.000	0.000
24	A	26	PRO	0	0.004	0.016	7.417	2.418	2.418	0.000	0.000	0.000	0.000
25	A	27	PRO	0	0.053	0.005	10.344	1.704	1.704	0.000	0.000	0.000	0.000
26	A	28	ASN	0	-0.038	-0.040	12.191	-0.674	-0.674	0.000	0.000	0.000	0.000
27	A	29	ALA	0	0.000	0.035	10.449	-0.228	-0.228	0.000	0.000	0.000	0.000
28	A	30	SER	0	-0.017	-0.025	10.904	2.870	2.870	0.000	0.000	0.000	0.000
29	A	31	ARG	1	0.862	0.887	10.886	22.050	22.050	0.000	0.000	0.000	0.000
30	A	32	PHE	0	-0.008	0.019	7.443	-3.243	-3.243	0.000	0.000	0.000	0.000
31	A	33	HIS	0	-0.009	-0.004	8.419	3.751	3.751	0.000	0.000	0.000	0.000
32	A	34	VAL	0	-0.002	0.003	8.909	-3.928	-3.928	0.000	0.000	0.000	0.000
33	A	35	ASN	0	-0.036	-0.012	11.044	3.350	3.350	0.000	0.000	0.000	0.000
34	A	36	LEU	0	0.018	0.014	12.689	-0.780	-0.780	0.000	0.000	0.000	0.000
35	A	37	LEU	0	0.015	-0.002	12.728	1.045	1.045	0.000	0.000	0.000	0.000
36	A	38	CYS	0	-0.049	-0.037	16.313	0.370	0.370	0.000	0.000	0.000	0.000
37	A	39	GLY	0	0.035	0.023	17.758	0.958	0.958	0.000	0.000	0.000	0.000
38	A	40	GLU	-1	-0.893	-0.932	15.018	-19.575	-19.575	0.000	0.000	0.000	0.000
39	A	41	GLU	-1	-0.910	-0.941	15.193	-15.975	-15.975	0.000	0.000	0.000	0.000
40	A	42	GLN	0	-0.014	-0.014	15.475	0.073	0.073	0.000	0.000	0.000	0.000
41	A	43	GLY	0	0.001	-0.005	17.438	0.881	0.881	0.000	0.000	0.000	0.000
42	A	44	SER	0	-0.012	-0.008	17.449	0.894	0.894	0.000	0.000	0.000	0.000
43	A	45	ASP	-1	-0.771	-0.870	18.934	-13.820	-13.820	0.000	0.000	0.000	0.000
44	A	46	ALA	0	-0.059	-0.030	17.598	-0.718	-0.718	0.000	0.000	0.000	0.000
45	A	47	ALA	0	0.027	0.007	18.959	0.636	0.636	0.000	0.000	0.000	0.000
46	A	48	LEU	0	-0.016	-0.006	16.960	0.576	0.576	0.000	0.000	0.000	0.000
47	A	49	HIS	0	-0.076	-0.029	13.616	-0.446	-0.446	0.000	0.000	0.000	0.000
48	A	50	PHE	0	0.039	0.010	12.885	1.148	1.148	0.000	0.000	0.000	0.000
49	A	51	ASN	0	0.011	-0.013	12.595	-0.697	-0.697	0.000	0.000	0.000	0.000
50	A	52	PRO	0	-0.005	0.011	12.231	1.573	1.573	0.000	0.000	0.000	0.000
51	A	53	ARG	1	0.811	0.900	13.104	15.211	15.211	0.000	0.000	0.000	0.000
52	A	54	LEU	0	0.039	0.011	12.230	1.217	1.217	0.000	0.000	0.000	0.000
53	A	55	ASP	-1	-0.850	-0.900	15.656	-18.358	-18.358	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.032	-0.026	17.530	0.892	0.892	0.000	0.000	0.000	0.000
55	A	57	SER	0	-0.039	-0.007	19.147	0.717	0.717	0.000	0.000	0.000	0.000
56	A	58	GLU	-1	-0.773	-0.851	19.248	-13.589	-13.589	0.000	0.000	0.000	0.000
57	A	59	VAL	0	0.002	-0.006	16.466	-1.292	-1.292	0.000	0.000	0.000	0.000
58	A	60	VAL	0	-0.039	-0.002	17.790	1.017	1.017	0.000	0.000	0.000	0.000
59	A	61	PHE	0	0.031	0.011	17.845	-1.278	-1.278	0.000	0.000	0.000	0.000
60	A	62	ASN	0	-0.006	-0.019	19.516	1.212	1.212	0.000	0.000	0.000	0.000
61	A	63	SER	0	0.053	0.025	20.330	-0.393	-0.393	0.000	0.000	0.000	0.000
62	A	64	LYS	1	0.826	0.927	18.095	17.069	17.069	0.000	0.000	0.000	0.000
63	A	65	GLU	-1	-0.873	-0.947	22.038	-11.797	-11.797	0.000	0.000	0.000	0.000
64	A	66	GLN	0	0.023	0.009	24.830	0.194	0.194	0.000	0.000	0.000	0.000
65	A	67	GLY	0	-0.009	0.008	22.848	0.182	0.182	0.000	0.000	0.000	0.000
66	A	68	SER	0	-0.069	-0.020	23.285	-0.222	-0.222	0.000	0.000	0.000	0.000
67	A	69	TRP	0	0.008	-0.017	16.960	-0.345	-0.345	0.000	0.000	0.000	0.000
68	A	70	GLY	0	0.042	0.033	23.784	0.587	0.587	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.958	0.976	25.081	10.242	10.242	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.778	-0.871	21.245	-14.807	-14.807	0.000	0.000	0.000	0.000
71	A	73	GLU	-1	-0.817	-0.892	23.404	-11.828	-11.828	0.000	0.000	0.000	0.000
72	A	74	ARG	1	0.730	0.804	22.554	12.994	12.994	0.000	0.000	0.000	0.000
73	A	75	GLY	0	0.039	0.044	22.111	0.501	0.501	0.000	0.000	0.000	0.000
74	A	76	PRO	0	-0.026	-0.014	23.361	0.096	0.096	0.000	0.000	0.000	0.000
75	A	77	GLY	0	0.052	0.036	23.323	-0.035	-0.035	0.000	0.000	0.000	0.000
76	A	78	VAL	0	-0.009	0.005	16.861	-0.497	-0.497	0.000	0.000	0.000	0.000
77	A	79	PRO	0	-0.025	0.003	17.645	0.212	0.212	0.000	0.000	0.000	0.000
78	A	80	PHE	0	0.012	-0.007	13.517	-0.840	-0.840	0.000	0.000	0.000	0.000
79	A	81	GLN	0	0.022	0.003	15.653	0.717	0.717	0.000	0.000	0.000	0.000
80	A	82	ARG	1	0.820	0.898	13.819	18.405	18.405	0.000	0.000	0.000	0.000
81	A	83	GLY	0	-0.017	-0.004	13.364	1.274	1.274	0.000	0.000	0.000	0.000
82	A	84	GLN	0	0.010	0.011	14.146	0.913	0.913	0.000	0.000	0.000	0.000
83	A	85	PRO	0	-0.007	-0.006	12.307	-1.892	-1.892	0.000	0.000	0.000	0.000
84	A	86	PHE	0	-0.017	-0.013	8.160	1.328	1.328	0.000	0.000	0.000	0.000
85	A	87	GLU	-1	-0.790	-0.888	12.559	-18.426	-18.426	0.000	0.000	0.000	0.000
86	A	88	VAL	0	-0.014	-0.007	12.898	0.867	0.867	0.000	0.000	0.000	0.000
87	A	89	LEU	0	-0.012	-0.007	14.450	-0.518	-0.518	0.000	0.000	0.000	0.000
88	A	90	ILE	0	-0.014	-0.007	14.182	0.267	0.267	0.000	0.000	0.000	0.000
89	A	91	ILE	0	-0.007	-0.002	17.518	-0.014	-0.014	0.000	0.000	0.000	0.000
90	A	92	ALA	0	0.014	0.016	20.877	0.312	0.312	0.000	0.000	0.000	0.000
91	A	93	SER	0	-0.020	-0.006	22.721	0.451	0.451	0.000	0.000	0.000	0.000
92	A	94	ASP	-1	-0.855	-0.946	26.494	-10.299	-10.299	0.000	0.000	0.000	0.000
93	A	95	ASP	-1	-0.898	-0.956	28.966	-10.606	-10.606	0.000	0.000	0.000	0.000
94	A	96	GLY	0	0.058	0.011	25.598	0.040	0.040	0.000	0.000	0.000	0.000
95	A	97	PHE	0	-0.028	-0.013	20.004	-0.119	-0.119	0.000	0.000	0.000	0.000
96	A	98	LYS	1	0.946	0.984	22.302	11.728	11.728	0.000	0.000	0.000	0.000
97	A	99	ALA	0	0.004	0.006	18.542	-0.582	-0.582	0.000	0.000	0.000	0.000
98	A	100	VAL	0	0.007	-0.005	18.997	0.677	0.677	0.000	0.000	0.000	0.000
99	A	101	VAL	0	-0.006	-0.016	16.145	-1.173	-1.173	0.000	0.000	0.000	0.000
100	A	102	GLY	0	-0.001	0.010	17.983	0.564	0.564	0.000	0.000	0.000	0.000
101	A	103	ASP	-1	-0.899	-0.945	19.687	-12.597	-12.597	0.000	0.000	0.000	0.000
102	A	104	ALA	0	-0.024	-0.001	22.392	0.609	0.609	0.000	0.000	0.000	0.000
103	A	105	GLN	0	-0.048	-0.041	22.245	-0.964	-0.964	0.000	0.000	0.000	0.000
104	A	106	TYR	0	-0.040	-0.033	19.762	0.043	0.043	0.000	0.000	0.000	0.000
105	A	107	HIS	0	0.002	-0.019	21.868	0.245	0.245	0.000	0.000	0.000	0.000
106	A	108	HIS	0	-0.081	-0.039	23.150	-0.631	-0.631	0.000	0.000	0.000	0.000
107	A	109	PHE	0	0.002	0.018	22.114	0.187	0.187	0.000	0.000	0.000	0.000
108	A	110	ARG	1	0.924	0.973	24.068	10.498	10.498	0.000	0.000	0.000	0.000
109	A	111	HIS	0	-0.051	-0.032	23.326	-0.479	-0.479	0.000	0.000	0.000	0.000
110	A	112	ARG	1	0.782	0.875	24.730	13.259	13.259	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.021	0.019	22.535	0.254	0.254	0.000	0.000	0.000	0.000
112	A	114	PRO	0	-0.013	-0.007	25.396	-0.109	-0.109	0.000	0.000	0.000	0.000
113	A	115	LEU	0	0.050	0.014	22.245	-0.319	-0.319	0.000	0.000	0.000	0.000
114	A	116	ALA	0	0.024	0.014	22.585	-0.454	-0.454	0.000	0.000	0.000	0.000
115	A	117	ARG	1	0.862	0.910	23.257	12.504	12.504	0.000	0.000	0.000	0.000
116	A	118	VAL	0	-0.028	-0.001	17.338	-0.405	-0.405	0.000	0.000	0.000	0.000
117	A	119	ARG	1	0.881	0.936	17.897	13.970	13.970	0.000	0.000	0.000	0.000
118	A	120	LEU	0	0.008	0.025	10.843	-0.631	-0.631	0.000	0.000	0.000	0.000
119	A	121	VAL	0	0.012	0.011	10.346	0.261	0.261	0.000	0.000	0.000	0.000
120	A	122	GLU	-1	-0.840	-0.918	7.849	-30.964	-30.964	0.000	0.000	0.000	0.000
121	A	123	VAL	0	0.000	-0.004	5.492	2.293	2.293	0.000	0.000	0.000	0.000
123	A	125	GLY	0	0.025	0.023	5.263	5.201	5.201	0.000	0.000	0.000	0.000
129	A	131	SER	0	-0.056	-0.069	6.891	0.297	0.297	0.000	0.000	0.000	0.000
130	A	132	VAL	0	-0.005	0.015	6.901	0.516	0.516	0.000	0.000	0.000	0.000
131	A	133	ARG	1	0.867	0.926	9.525	22.607	22.607	0.000	0.000	0.000	0.000
132	A	134	ILE	0	0.029	0.012	12.371	-0.374	-0.374	0.000	0.000	0.000	0.000
133	A	135	PHE	-1	-0.843	-0.905	15.744	-14.143	-14.143	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:VAL)