FMO DATABASE

FMODB ID: 2M42R

Calculation Name: 2E7P-D-Xray547

Preferred Name:

Target Type:

Ligand Name: glutathione | fe2/s2 (inorganic) cluster

Ligand 3-letter code: GSH | FES

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2E7P

Chain ID: D

ChEMBL ID:

UniProt ID: Q5PSJ1

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	101
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-709924.755147
FMO2-HF: Nuclear repulsion	671932.607859
FMO2-HF: Total energy	-37992.147288
FMO2-MP2: Total energy	-38103.014328

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:7:ASP)

Summations of interaction energy for fragment #1(A:7:ASP)

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.
16.712	21.087	0.753	-1.92	-3.207	-0.004

Interaction energy analysis for fragmet #1(A:7:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.002 / q_NPA : -0.008

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	9	ALA	0	0.072	0.028	3.701	0.644	2.382	-0.001	-0.686	-1.051	0.001
4	A	10	LEU	0	0.004	0.004	2.576	1.010	3.062	0.754	-0.981	-1.825	-0.005
5	A	11	LYS	1	0.965	0.979	3.955	7.263	7.784	0.001	-0.242	-0.280	0.000
58	A	64	ALA	0	-0.023	-0.015	4.189	0.041	0.105	-0.001	-0.011	-0.051	0.000
6	A	12	LYS	1	0.894	0.934	5.842	5.695	5.695	0.000	0.000	0.000	0.000
7	A	13	ALA	0	0.036	0.017	7.013	1.236	1.236	0.000	0.000	0.000	0.000
8	A	14	LYS	1	0.912	0.953	6.749	3.684	3.684	0.000	0.000	0.000	0.000
9	A	15	GLU	-1	-0.946	-0.963	9.820	-2.281	-2.281	0.000	0.000	0.000	0.000
10	A	16	LEU	0	0.007	-0.007	11.496	0.482	0.482	0.000	0.000	0.000	0.000
11	A	17	ALA	0	0.003	0.011	12.592	0.361	0.361	0.000	0.000	0.000	0.000
12	A	18	SER	0	-0.006	-0.005	13.829	0.360	0.360	0.000	0.000	0.000	0.000
13	A	19	SER	0	-0.099	-0.044	16.118	0.181	0.181	0.000	0.000	0.000	0.000
14	A	20	ALA	0	0.011	-0.005	17.778	0.081	0.081	0.000	0.000	0.000	0.000
15	A	21	PRO	0	0.059	0.049	20.636	-0.067	-0.067	0.000	0.000	0.000	0.000
16	A	22	VAL	0	0.045	0.019	21.831	0.014	0.014	0.000	0.000	0.000	0.000
17	A	23	VAL	0	-0.045	-0.007	15.907	-0.035	-0.035	0.000	0.000	0.000	0.000
18	A	24	VAL	0	-0.009	-0.004	18.799	0.024	0.024	0.000	0.000	0.000	0.000
19	A	25	PHE	0	-0.010	-0.003	12.030	-0.127	-0.127	0.000	0.000	0.000	0.000
20	A	26	SER	0	-0.050	-0.084	16.072	0.225	0.225	0.000	0.000	0.000	0.000
21	A	27	LYS	1	0.903	0.940	15.651	1.497	1.497	0.000	0.000	0.000	0.000
22	A	28	THR	0	0.001	-0.011	19.965	0.139	0.139	0.000	0.000	0.000	0.000
23	A	29	TYR	0	0.015	0.007	20.316	0.058	0.058	0.000	0.000	0.000	0.000
24	A	30	CYS	0	-0.065	0.003	21.603	0.099	0.099	0.000	0.000	0.000	0.000
25	A	31	GLY	0	0.065	0.026	24.189	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	32	TYR	0	0.044	-0.006	23.839	0.018	0.018	0.000	0.000	0.000	0.000
27	A	33	CYS	0	-0.030	-0.004	21.239	-0.052	-0.052	0.000	0.000	0.000	0.000
28	A	34	ASN	0	0.004	0.004	23.696	-0.031	-0.031	0.000	0.000	0.000	0.000
29	A	35	ARG	1	0.974	0.997	27.204	0.562	0.562	0.000	0.000	0.000	0.000
30	A	36	VAL	0	-0.003	0.004	23.188	0.028	0.028	0.000	0.000	0.000	0.000
31	A	37	LYS	1	0.860	0.923	23.046	1.029	1.029	0.000	0.000	0.000	0.000
32	A	38	GLN	0	-0.003	-0.004	26.894	0.033	0.033	0.000	0.000	0.000	0.000
33	A	39	LEU	0	0.013	0.021	29.020	0.019	0.019	0.000	0.000	0.000	0.000
34	A	40	LEU	0	0.015	-0.007	24.412	0.021	0.021	0.000	0.000	0.000	0.000
35	A	41	THR	0	-0.014	-0.005	29.030	0.020	0.020	0.000	0.000	0.000	0.000
36	A	42	GLN	0	-0.031	-0.014	31.584	0.014	0.014	0.000	0.000	0.000	0.000
37	A	43	VAL	0	-0.053	-0.023	31.016	0.028	0.028	0.000	0.000	0.000	0.000
38	A	44	GLY	0	0.004	0.012	33.480	0.007	0.007	0.000	0.000	0.000	0.000
39	A	45	ALA	0	-0.009	0.002	28.153	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	46	SER	0	-0.010	-0.006	27.687	-0.040	-0.040	0.000	0.000	0.000	0.000
41	A	47	TYR	0	-0.029	-0.025	23.053	-0.043	-0.043	0.000	0.000	0.000	0.000
42	A	48	LYS	1	0.910	0.960	17.140	1.798	1.798	0.000	0.000	0.000	0.000
43	A	49	VAL	0	0.003	0.001	19.834	-0.077	-0.077	0.000	0.000	0.000	0.000
44	A	50	VAL	0	-0.020	-0.018	13.725	-0.083	-0.083	0.000	0.000	0.000	0.000
45	A	51	GLU	-1	-0.682	-0.802	16.629	-1.324	-1.324	0.000	0.000	0.000	0.000
46	A	52	LEU	0	-0.042	-0.039	12.239	-0.122	-0.122	0.000	0.000	0.000	0.000
47	A	53	ASP	-1	-0.847	-0.910	15.326	-1.410	-1.410	0.000	0.000	0.000	0.000
48	A	54	GLU	-1	-0.892	-0.936	18.084	-1.086	-1.086	0.000	0.000	0.000	0.000
49	A	55	LEU	0	-0.036	-0.015	13.100	-0.104	-0.104	0.000	0.000	0.000	0.000
50	A	56	SER	0	0.023	0.015	14.276	-0.079	-0.079	0.000	0.000	0.000	0.000
51	A	57	ASP	-1	-0.813	-0.900	8.944	-4.516	-4.516	0.000	0.000	0.000	0.000
52	A	58	GLY	0	0.052	0.026	9.604	-0.915	-0.915	0.000	0.000	0.000	0.000
53	A	59	SER	0	-0.024	-0.017	11.283	-0.045	-0.045	0.000	0.000	0.000	0.000
54	A	60	GLN	0	0.052	0.025	6.173	-0.018	-0.018	0.000	0.000	0.000	0.000
55	A	61	LEU	0	-0.016	-0.013	6.169	-2.213	-2.213	0.000	0.000	0.000	0.000
56	A	62	GLN	0	0.002	0.002	8.069	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	63	SER	0	-0.015	-0.006	7.036	0.274	0.274	0.000	0.000	0.000	0.000
59	A	65	LEU	0	0.002	-0.003	5.692	1.166	1.166	0.000	0.000	0.000	0.000
60	A	66	ALA	0	-0.002	0.027	9.329	0.665	0.665	0.000	0.000	0.000	0.000
61	A	67	HIS	0	-0.013	-0.011	5.879	1.079	1.079	0.000	0.000	0.000	0.000
62	A	68	TRP	0	-0.039	-0.017	7.877	0.504	0.504	0.000	0.000	0.000	0.000
63	A	69	THR	0	-0.010	-0.026	9.584	0.464	0.464	0.000	0.000	0.000	0.000
64	A	70	GLY	0	0.038	0.041	12.389	0.247	0.247	0.000	0.000	0.000	0.000
65	A	71	ARG	1	0.886	0.956	14.055	1.137	1.137	0.000	0.000	0.000	0.000
66	A	72	GLY	0	0.045	0.016	13.123	-0.313	-0.313	0.000	0.000	0.000	0.000
67	A	73	THR	0	-0.062	-0.026	14.149	-0.050	-0.050	0.000	0.000	0.000	0.000
68	A	74	VAL	0	0.027	0.027	16.036	-0.106	-0.106	0.000	0.000	0.000	0.000
69	A	75	PRO	0	0.020	-0.022	18.249	0.129	0.129	0.000	0.000	0.000	0.000
70	A	76	ASN	0	-0.078	-0.057	13.715	0.202	0.202	0.000	0.000	0.000	0.000
71	A	77	VAL	0	0.007	0.010	16.866	-0.137	-0.137	0.000	0.000	0.000	0.000
72	A	78	PHE	0	-0.001	-0.017	12.652	-0.023	-0.023	0.000	0.000	0.000	0.000
73	A	79	ILE	0	0.031	0.010	18.601	0.017	0.017	0.000	0.000	0.000	0.000
74	A	80	GLY	0	0.072	0.043	21.384	0.038	0.038	0.000	0.000	0.000	0.000
75	A	81	GLY	0	-0.015	0.000	16.916	0.035	0.035	0.000	0.000	0.000	0.000
76	A	82	LYS	1	0.900	0.963	16.404	0.582	0.582	0.000	0.000	0.000	0.000
77	A	83	GLN	0	-0.007	-0.009	13.277	0.099	0.099	0.000	0.000	0.000	0.000
78	A	84	ILE	0	-0.038	-0.011	17.728	0.152	0.152	0.000	0.000	0.000	0.000
79	A	85	GLY	0	0.022	0.003	19.408	0.103	0.103	0.000	0.000	0.000	0.000
80	A	86	GLY	0	0.013	0.008	19.463	-0.134	-0.134	0.000	0.000	0.000	0.000
81	A	87	CYS	0	-0.030	-0.023	21.339	0.080	0.080	0.000	0.000	0.000	0.000
82	A	88	ASP	-1	-0.869	-0.935	24.499	-0.523	-0.523	0.000	0.000	0.000	0.000
83	A	89	THR	0	-0.022	-0.009	23.503	0.014	0.014	0.000	0.000	0.000	0.000
84	A	90	VAL	0	0.021	0.014	23.680	0.025	0.025	0.000	0.000	0.000	0.000
85	A	91	VAL	0	0.005	-0.003	26.402	0.038	0.038	0.000	0.000	0.000	0.000
86	A	92	GLU	-1	-0.880	-0.924	28.677	-0.384	-0.384	0.000	0.000	0.000	0.000
87	A	93	LYS	1	0.907	0.943	25.305	0.504	0.504	0.000	0.000	0.000	0.000
88	A	94	HIS	0	0.017	0.001	29.983	0.011	0.011	0.000	0.000	0.000	0.000
89	A	95	GLN	0	-0.034	-0.012	31.975	0.023	0.023	0.000	0.000	0.000	0.000
90	A	96	ARG	1	0.733	0.841	29.321	0.385	0.385	0.000	0.000	0.000	0.000
91	A	97	ASN	0	-0.017	-0.015	34.682	0.008	0.008	0.000	0.000	0.000	0.000
92	A	98	GLU	-1	-0.765	-0.860	29.900	-0.375	-0.375	0.000	0.000	0.000	0.000
93	A	99	LEU	0	-0.057	-0.020	26.271	-0.026	-0.026	0.000	0.000	0.000	0.000
94	A	100	LEU	0	0.047	0.016	29.356	-0.028	-0.028	0.000	0.000	0.000	0.000
95	A	101	PRO	0	0.023	0.008	31.701	-0.011	-0.011	0.000	0.000	0.000	0.000
96	A	102	LEU	0	-0.008	-0.008	25.582	-0.016	-0.016	0.000	0.000	0.000	0.000
97	A	103	LEU	0	-0.049	-0.032	26.341	-0.041	-0.041	0.000	0.000	0.000	0.000
98	A	104	GLN	0	-0.023	-0.013	28.460	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	105	ASP	-1	-0.989	-0.975	27.240	-0.472	-0.472	0.000	0.000	0.000	0.000
100	A	106	ALA	0	-0.044	-0.026	24.312	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	107	ALA	-1	-0.958	-0.961	25.857	-0.608	-0.608	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:ASP)