FMO DATABASE

FMODB ID: Y12L2

Calculation Name: 1EUW-A-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol | ethyl mercury ion

Ligand 3-letter code: GOL | EMC

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EUW

Chain ID: A

ChEMBL ID:

UniProt ID: P06968

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	136
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1066185.654918
FMO2-HF: Nuclear repulsion	1014156.644612
FMO2-HF: Total energy	-52029.010307
FMO2-MP2: Total energy	-52177.938826

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:MET)

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

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.
-31.27	-28.333	0.518	-1.036	-2.42	-0.005

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

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 : 0.919

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	LYS	1	0.929	0.956	3.435	34.203	37.136	0.519	-1.029	-2.424	-0.005
4	A	4	LYS	1	0.925	0.968	5.589	24.966	24.970	-0.001	-0.007	0.004	0.000
5	A	5	ILE	0	0.019	0.007	8.619	-0.273	-0.273	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.890	-0.917	11.581	-17.676	-17.676	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.025	-0.031	15.370	-0.066	-0.066	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.943	0.977	17.746	13.204	13.204	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.006	0.001	21.563	-0.114	-0.114	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.072	-0.038	24.061	0.343	0.343	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.813	-0.913	26.865	-10.115	-10.115	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.004	-0.006	27.549	-0.394	-0.394	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.869	0.930	27.740	10.139	10.139	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.003	0.001	22.460	-0.268	-0.268	0.000	0.000	0.000	0.000
15	A	15	GLY	0	-0.021	-0.022	22.848	-0.034	-0.034	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.870	0.939	23.757	10.165	10.165	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.909	-0.939	27.225	-9.930	-9.930	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.007	0.003	22.870	-0.044	-0.044	0.000	0.000	0.000	0.000
19	A	19	PRO	0	-0.020	-0.014	20.269	-0.118	-0.118	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.056	0.031	17.501	0.046	0.046	0.000	0.000	0.000	0.000
21	A	21	PRO	0	-0.014	-0.006	15.089	-0.204	-0.204	0.000	0.000	0.000	0.000
22	A	22	THR	0	-0.013	-0.007	13.084	-0.705	-0.705	0.000	0.000	0.000	0.000
23	A	23	TYR	0	0.000	0.002	7.758	0.100	0.100	0.000	0.000	0.000	0.000
24	A	24	ALA	0	0.005	0.009	11.080	0.642	0.642	0.000	0.000	0.000	0.000
25	A	25	THR	0	0.013	0.008	10.905	0.064	0.064	0.000	0.000	0.000	0.000
26	A	26	SER	0	0.020	0.000	6.639	-0.924	-0.924	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.010	0.010	5.809	-7.366	-7.366	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.077	-0.038	7.782	2.837	2.837	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.033	0.010	6.957	-3.490	-3.490	0.000	0.000	0.000	0.000
30	A	30	GLY	0	-0.001	0.002	8.037	-0.304	-0.304	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.042	-0.002	10.591	0.146	0.146	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.750	-0.870	12.839	-16.054	-16.054	0.000	0.000	0.000	0.000
33	A	33	LEU	0	-0.041	-0.030	16.482	-0.046	-0.046	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.872	0.911	18.917	14.562	14.562	0.000	0.000	0.000	0.000
35	A	35	ALA	0	0.047	0.032	22.433	-0.081	-0.081	0.000	0.000	0.000	0.000
36	A	36	CYS	0	-0.100	-0.030	25.941	0.300	0.300	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.004	-0.003	27.516	0.126	0.126	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.004	-0.003	31.207	-0.244	-0.244	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.877	-0.931	34.581	-8.235	-8.235	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.016	-0.017	33.771	-0.256	-0.256	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.028	-0.010	32.732	0.228	0.228	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.905	-0.942	33.838	-8.299	-8.299	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.064	-0.033	31.116	-0.070	-0.070	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.092	0.042	35.396	-0.065	-0.065	0.000	0.000	0.000	0.000
45	A	45	PRO	0	-0.035	-0.026	36.636	-0.227	-0.227	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.008	0.009	35.851	0.215	0.215	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.846	-0.901	35.645	-8.495	-8.495	0.000	0.000	0.000	0.000
48	A	48	THR	0	-0.040	-0.050	30.599	-0.444	-0.444	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.007	0.006	30.714	0.257	0.257	0.000	0.000	0.000	0.000
50	A	50	LEU	0	-0.019	-0.009	27.265	-0.412	-0.412	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.011	0.010	26.650	0.226	0.226	0.000	0.000	0.000	0.000
52	A	52	PRO	0	0.023	0.006	26.292	-0.513	-0.513	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.033	-0.006	21.280	-0.195	-0.195	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.013	-0.003	23.782	-0.123	-0.123	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.009	-0.011	18.723	-0.205	-0.205	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.012	0.015	20.984	0.263	0.263	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.020	-0.017	14.187	-0.447	-0.447	0.000	0.000	0.000	0.000
58	A	58	HIS	0	0.041	0.018	15.943	0.570	0.570	0.000	0.000	0.000	0.000
59	A	59	ILE	0	-0.013	0.005	10.274	-1.163	-1.163	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.004	0.017	10.951	-1.295	-1.295	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.847	-0.924	6.627	-25.468	-25.468	0.000	0.000	0.000	0.000
62	A	62	PRO	0	0.002	-0.007	10.155	-0.471	-0.471	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.001	0.007	7.243	0.948	0.948	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.101	-0.048	5.513	-2.916	-2.916	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.035	0.027	8.761	2.026	2.026	0.000	0.000	0.000	0.000
66	A	66	ALA	0	-0.002	-0.006	10.479	-2.506	-2.506	0.000	0.000	0.000	0.000
67	A	67	MET	0	-0.006	0.000	12.490	1.333	1.333	0.000	0.000	0.000	0.000
68	A	68	MET	0	-0.004	0.009	14.339	-0.641	-0.641	0.000	0.000	0.000	0.000
69	A	69	LEU	0	0.029	-0.001	14.733	0.644	0.644	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.080	0.036	18.377	0.064	0.064	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.825	0.935	19.108	14.037	14.037	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.010	0.002	19.587	0.951	0.951	0.000	0.000	0.000	0.000
73	A	73	GLY	0	0.006	-0.008	21.339	0.558	0.558	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.005	0.010	23.759	0.467	0.467	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.094	0.050	24.366	0.451	0.451	0.000	0.000	0.000	0.000
76	A	76	HIS	0	-0.061	-0.039	25.477	0.392	0.392	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.920	0.947	27.209	11.428	11.428	0.000	0.000	0.000	0.000
78	A	78	HIS	0	0.026	0.018	27.971	0.442	0.442	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.023	0.034	29.612	0.236	0.236	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.010	0.010	26.807	0.026	0.026	0.000	0.000	0.000	0.000
81	A	81	VAL	0	-0.039	-0.029	25.041	-0.648	-0.648	0.000	0.000	0.000	0.000
82	A	82	LEU	0	-0.007	0.003	20.337	0.113	0.113	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.046	0.007	24.921	0.167	0.167	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.022	-0.012	22.681	0.245	0.245	0.000	0.000	0.000	0.000
85	A	85	LEU	0	-0.009	0.007	24.107	-0.299	-0.299	0.000	0.000	0.000	0.000
86	A	86	VAL	0	-0.014	-0.030	17.893	-0.642	-0.642	0.000	0.000	0.000	0.000
87	A	87	GLY	0	-0.015	0.000	19.466	0.515	0.515	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.033	-0.008	15.523	-0.991	-0.991	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.023	-0.006	15.599	0.846	0.846	0.000	0.000	0.000	0.000
90	A	90	ASP	0	0.002	-0.070	15.111	-1.189	-1.189	0.000	0.000	0.000	0.000
91	A	91	SER	0	0.059	0.020	12.703	0.174	0.174	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.877	-0.888	14.108	-14.389	-14.389	0.000	0.000	0.000	0.000
93	A	93	TYR	0	-0.035	-0.023	17.364	0.956	0.956	0.000	0.000	0.000	0.000
94	A	94	GLN	0	-0.001	-0.008	18.161	-0.381	-0.381	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.019	-0.001	20.593	0.491	0.491	0.000	0.000	0.000	0.000
96	A	96	GLN	0	0.028	-0.002	22.037	-0.677	-0.677	0.000	0.000	0.000	0.000
97	A	97	LEU	0	0.005	0.014	17.251	0.073	0.073	0.000	0.000	0.000	0.000
98	A	98	MET	0	-0.022	0.017	21.593	0.180	0.180	0.000	0.000	0.000	0.000
99	A	99	ILE	0	0.024	-0.002	21.812	-0.405	-0.405	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.001	0.014	24.178	0.616	0.616	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.014	-0.005	25.748	-0.434	-0.434	0.000	0.000	0.000	0.000
102	A	102	TRP	0	0.012	0.001	27.768	0.211	0.211	0.000	0.000	0.000	0.000
103	A	103	ASN	0	-0.034	-0.020	29.615	-0.483	-0.483	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.844	0.931	28.806	10.713	10.713	0.000	0.000	0.000	0.000
105	A	105	GLY	0	-0.002	-0.006	32.513	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	106	GLN	0	-0.028	-0.025	34.357	0.056	0.056	0.000	0.000	0.000	0.000
107	A	107	ASP	-1	-0.909	-0.945	36.018	-8.226	-8.226	0.000	0.000	0.000	0.000
108	A	108	SER	0	-0.014	-0.015	36.047	-0.200	-0.200	0.000	0.000	0.000	0.000
109	A	109	PHE	0	-0.051	-0.011	28.989	-0.089	-0.089	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.014	-0.013	33.761	0.174	0.174	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.014	0.003	28.433	-0.228	-0.228	0.000	0.000	0.000	0.000
112	A	112	GLN	0	0.017	-0.007	30.087	0.423	0.423	0.000	0.000	0.000	0.000
113	A	113	PRO	0	0.045	0.015	29.140	-0.462	-0.462	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.022	0.006	25.960	-0.030	-0.030	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.886	-0.930	24.898	-11.745	-11.745	0.000	0.000	0.000	0.000
116	A	116	ARG	1	0.810	0.894	19.099	14.780	14.780	0.000	0.000	0.000	0.000
117	A	117	ILE	0	0.075	0.032	22.565	0.094	0.094	0.000	0.000	0.000	0.000
118	A	118	ALA	0	0.007	0.010	20.143	0.160	0.160	0.000	0.000	0.000	0.000
119	A	119	GLN	0	-0.051	-0.035	14.994	-1.201	-1.201	0.000	0.000	0.000	0.000
120	A	120	MET	0	-0.029	-0.005	12.966	1.180	1.180	0.000	0.000	0.000	0.000
121	A	121	ILE	0	0.033	0.027	9.751	-1.526	-1.526	0.000	0.000	0.000	0.000
122	A	122	PHE	0	0.010	-0.004	7.035	1.896	1.896	0.000	0.000	0.000	0.000
123	A	123	VAL	0	-0.011	-0.013	7.066	-3.420	-3.420	0.000	0.000	0.000	0.000
124	A	124	PRO	0	0.003	-0.007	4.807	1.108	1.108	0.000	0.000	0.000	0.000
125	A	125	VAL	0	-0.048	-0.015	7.422	1.372	1.372	0.000	0.000	0.000	0.000
126	A	126	VAL	0	0.022	0.002	10.443	-0.536	-0.536	0.000	0.000	0.000	0.000
127	A	127	GLN	0	-0.019	-0.004	12.945	0.681	0.681	0.000	0.000	0.000	0.000
128	A	128	ALA	0	-0.007	-0.004	16.397	-0.119	-0.119	0.000	0.000	0.000	0.000
129	A	129	GLU	-1	-0.932	-0.955	19.155	-11.803	-11.803	0.000	0.000	0.000	0.000
130	A	130	PHE	0	-0.051	-0.041	21.266	-0.024	-0.024	0.000	0.000	0.000	0.000
131	A	131	ASN	0	0.004	0.011	24.457	0.350	0.350	0.000	0.000	0.000	0.000
132	A	132	LEU	0	-0.044	-0.023	26.558	-0.061	-0.061	0.000	0.000	0.000	0.000
133	A	133	VAL	0	-0.014	-0.010	29.681	0.009	0.009	0.000	0.000	0.000	0.000
134	A	134	GLU	-1	-0.962	-0.983	32.082	-8.277	-8.277	0.000	0.000	0.000	0.000
135	A	135	ASP	-1	-0.964	-0.975	34.320	-7.740	-7.740	0.000	0.000	0.000	0.000
136	A	136	PHE	-1	-0.996	-0.991	28.611	-9.328	-9.328	0.000	0.000	0.000	0.000

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