FMO DATABASE

FMODB ID: 676KZ

Calculation Name: 3A0R-B-Xray547

Preferred Name:

Target Type:

Ligand Name: mercury (ii) ion

Ligand 3-letter code: HG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3A0R

Chain ID: B

ChEMBL ID:

UniProt ID: Q9X180

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-991456.290861
FMO2-HF: Nuclear repulsion	944821.140471
FMO2-HF: Total energy	-46635.15039
FMO2-MP2: Total energy	-46771.623271

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.
-182.444	-176.479	0.875	-2.407	-4.434	-0.018

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 : 0.928

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	3	ARG	1	0.909	0.967	3.485	33.060	35.422	0.036	-0.879	-1.519	-0.004
4	A	4	ILE	0	-0.006	0.000	4.842	1.928	1.958	-0.001	-0.006	-0.023	0.000
26	A	26	TYR	0	-0.090	-0.049	3.519	-13.887	-11.583	0.442	-1.078	-1.668	-0.010
27	A	27	GLU	-1	-0.920	-0.961	3.520	-38.432	-37.180	0.396	-0.441	-1.207	-0.004
28	A	28	ILE	0	-0.006	-0.010	4.998	-0.086	-0.069	0.002	-0.003	-0.017	0.000
5	A	5	LEU	0	-0.017	0.003	8.451	0.646	0.646	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.001	-0.009	11.757	0.487	0.487	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.037	-0.025	14.365	0.366	0.366	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.802	-0.902	18.076	-13.138	-13.138	0.000	0.000	0.000	0.000
9	A	9	ASP	-1	-0.849	-0.925	20.941	-11.665	-11.665	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.930	-0.971	24.054	-10.866	-10.866	0.000	0.000	0.000	0.000
11	A	11	PRO	0	-0.049	-0.028	21.838	-0.570	-0.570	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.036	0.000	20.849	-0.703	-0.703	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.005	0.009	20.992	-0.377	-0.377	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.874	0.947	17.230	13.606	13.606	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.967	-0.975	16.058	-15.252	-15.252	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.004	0.005	16.030	-0.678	-0.678	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.035	0.006	14.987	-0.712	-0.712	0.000	0.000	0.000	0.000
18	A	18	LYS	1	0.869	0.947	11.233	18.382	18.382	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.956	-0.998	10.829	-19.588	-19.588	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.823	-0.891	12.238	-18.559	-18.559	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.028	-0.024	9.280	-1.466	-1.466	0.000	0.000	0.000	0.000
22	A	22	GLN	0	-0.036	-0.034	7.063	-3.413	-3.413	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.934	-0.943	7.292	-21.487	-21.487	0.000	0.000	0.000	0.000
24	A	24	GLU	-1	-0.881	-0.954	8.516	-28.777	-28.777	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.041	-0.005	4.826	-2.038	-2.038	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.796	-0.881	8.773	-21.995	-21.995	0.000	0.000	0.000	0.000
30	A	30	THR	0	-0.029	-0.014	10.820	0.528	0.528	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.034	-0.020	14.430	0.176	0.176	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.911	-0.961	17.345	-12.526	-12.526	0.000	0.000	0.000	0.000
33	A	33	ASN	0	0.067	0.040	20.933	0.381	0.381	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.070	0.014	21.886	-0.496	-0.496	0.000	0.000	0.000	0.000
35	A	35	GLU	-1	-0.962	-0.977	22.675	-10.789	-10.789	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.972	-0.999	19.912	-13.409	-13.409	0.000	0.000	0.000	0.000
37	A	37	ALA	0	0.008	0.003	18.159	-0.718	-0.718	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.013	-0.004	17.946	-0.717	-0.717	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.921	0.957	19.296	11.320	11.320	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.851	0.932	13.178	18.650	18.650	0.000	0.000	0.000	0.000
41	A	41	PHE	0	0.000	0.009	13.352	-1.137	-1.137	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.016	-0.020	15.580	-0.335	-0.335	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.039	-0.016	17.032	0.198	0.198	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.022	0.006	13.001	-0.216	-0.216	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.063	-0.026	9.791	1.106	1.106	0.000	0.000	0.000	0.000
46	A	46	TYR	0	-0.002	-0.018	8.578	-2.069	-2.069	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.936	-0.965	7.662	-34.081	-34.081	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.005	-0.014	9.931	0.784	0.784	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.034	-0.004	11.450	-0.449	-0.449	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.018	0.016	13.401	0.383	0.383	0.000	0.000	0.000	0.000
51	A	51	LEU	0	-0.006	-0.001	16.182	0.123	0.123	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.618	-0.777	19.693	-11.785	-11.785	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.073	-0.076	22.998	-0.056	-0.056	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.939	-0.961	26.384	-9.311	-9.311	0.000	0.000	0.000	0.000
55	A	55	MET	0	0.018	0.027	23.056	-0.236	-0.236	0.000	0.000	0.000	0.000
56	A	56	PRO	0	0.004	-0.007	27.267	0.235	0.235	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.020	-0.002	27.662	-0.383	-0.383	0.000	0.000	0.000	0.000
58	A	58	ILE	0	-0.010	-0.012	26.098	0.272	0.272	0.000	0.000	0.000	0.000
59	A	59	SER	0	0.075	0.045	27.458	-0.362	-0.362	0.000	0.000	0.000	0.000
60	A	60	GLY	0	0.008	-0.015	24.536	-0.180	-0.180	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.030	-0.018	24.482	-0.460	-0.460	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.938	-0.963	26.645	-9.993	-9.993	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.005	0.004	21.329	-0.262	-0.262	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.023	0.010	21.831	-0.500	-0.500	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.007	0.004	22.906	-0.268	-0.268	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.957	-0.981	23.980	-11.155	-11.155	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.027	-0.015	18.052	-0.229	-0.229	0.000	0.000	0.000	0.000
68	A	68	ARG	1	0.799	0.893	20.011	14.282	14.282	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.928	0.955	22.734	10.334	10.334	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.902	0.971	21.404	12.115	12.115	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.931	0.969	16.450	17.567	17.567	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.930	0.957	20.420	13.402	13.402	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.887	-0.939	18.599	-14.822	-14.822	0.000	0.000	0.000	0.000
74	A	74	ALA	0	-0.002	0.011	16.606	-1.239	-1.239	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.870	0.946	12.775	23.754	23.754	0.000	0.000	0.000	0.000
76	A	76	ILE	0	0.006	-0.005	15.139	-0.751	-0.751	0.000	0.000	0.000	0.000
77	A	77	ILE	0	0.027	0.018	15.336	0.532	0.532	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.048	-0.023	18.334	0.113	0.113	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.000	-0.002	18.245	-0.079	-0.079	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.020	-0.022	21.549	0.179	0.179	0.000	0.000	0.000	0.000
81	A	81	ALA	0	0.035	0.007	24.657	-0.015	-0.015	0.000	0.000	0.000	0.000
82	A	82	TYR	0	-0.072	-0.027	26.783	0.268	0.268	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.006	0.005	25.973	0.114	0.114	0.000	0.000	0.000	0.000
84	A	84	HIS	0	0.010	-0.002	28.149	0.230	0.230	0.000	0.000	0.000	0.000
85	A	85	TYR	0	0.010	0.008	28.556	-0.403	-0.403	0.000	0.000	0.000	0.000
86	A	86	ARG	1	0.938	0.973	25.810	11.776	11.776	0.000	0.000	0.000	0.000
87	A	87	SER	0	-0.015	-0.016	29.133	0.154	0.154	0.000	0.000	0.000	0.000
88	A	88	ASP	-1	-0.825	-0.898	30.723	-9.353	-9.353	0.000	0.000	0.000	0.000
89	A	89	MET	0	-0.022	0.002	30.833	-0.392	-0.392	0.000	0.000	0.000	0.000
90	A	90	SER	0	0.046	0.011	28.698	-0.183	-0.183	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.074	-0.061	26.422	-0.450	-0.450	0.000	0.000	0.000	0.000
92	A	92	TRP	0	-0.046	-0.022	26.240	-0.413	-0.413	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.007	0.018	26.221	-0.072	-0.072	0.000	0.000	0.000	0.000
94	A	94	ALA	0	-0.024	-0.004	22.155	-0.547	-0.547	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.924	-0.960	18.684	-16.055	-16.055	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.847	-0.914	18.824	-14.221	-14.221	0.000	0.000	0.000	0.000
97	A	97	TYR	0	-0.036	-0.035	21.023	-0.028	-0.028	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.024	-0.007	18.458	-0.117	-0.117	0.000	0.000	0.000	0.000
99	A	99	VAL	0	-0.015	-0.017	21.932	0.345	0.345	0.000	0.000	0.000	0.000
100	A	100	LYS	1	0.828	0.908	22.141	12.497	12.497	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.033	-0.017	23.579	0.653	0.653	0.000	0.000	0.000	0.000
102	A	102	PHE	0	-0.010	-0.013	22.938	-0.334	-0.334	0.000	0.000	0.000	0.000
103	A	103	ASN	0	-0.030	-0.002	22.004	-0.783	-0.783	0.000	0.000	0.000	0.000
104	A	104	PHE	0	0.098	0.034	16.960	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.903	-0.956	17.317	-16.930	-16.930	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.868	-0.927	18.115	-14.029	-14.029	0.000	0.000	0.000	0.000
107	A	107	LEU	0	0.005	-0.006	14.730	-0.587	-0.587	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.860	0.933	13.149	18.522	18.522	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.929	-0.956	13.341	-17.148	-17.148	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.845	0.912	15.084	14.368	14.368	0.000	0.000	0.000	0.000
111	A	111	VAL	0	0.010	0.001	9.842	-0.503	-0.503	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.866	0.938	7.785	31.098	31.098	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.842	0.927	11.406	15.382	15.382	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.008	0.002	13.685	0.061	0.061	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.037	-0.012	7.314	-1.945	-1.945	0.000	0.000	0.000	0.000
116	A	116	SER	-1	-0.972	-0.979	9.012	-25.607	-25.607	0.000	0.000	0.000	0.000

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