FMO DATABASE

FMODB ID: RQ348

Calculation Name: 2JAC-A-Xray547

Preferred Name:

Target Type:

Ligand Name: glutathione

Ligand 3-letter code: GSH

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2JAC

Chain ID: A

ChEMBL ID:

UniProt ID: P25373

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	108
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-851300.614932
FMO2-HF: Nuclear repulsion	808713.027859
FMO2-HF: Total energy	-42587.587072
FMO2-MP2: Total energy	-42712.27603

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.
-119.466	-112.44	2.525	-3.824	-5.725	-0.037

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 : 0.814 / q_NPA : 0.908

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	SER	0	0.016	0.023	2.820	-4.480	-2.209	0.663	-1.292	-1.641	-0.008
4	A	4	GLN	0	0.052	0.002	2.671	-4.127	-3.360	1.126	-0.526	-1.367	-0.008
7	A	7	ILE	0	-0.031	-0.017	3.560	1.964	2.257	0.004	-0.041	-0.256	0.000
68	A	68	GLU	-1	-0.949	-0.996	2.902	-58.208	-54.513	0.732	-1.965	-2.461	-0.021
5	A	5	GLU	-1	-0.833	-0.904	5.429	-19.564	-19.564	0.000	0.000	0.000	0.000
6	A	6	THR	0	0.011	0.005	6.979	2.694	2.694	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.833	0.916	6.846	21.448	21.448	0.000	0.000	0.000	0.000
9	A	9	HIS	0	0.053	0.027	9.912	1.354	1.354	0.000	0.000	0.000	0.000
10	A	10	VAL	0	0.002	-0.006	10.054	1.221	1.221	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.937	0.971	8.472	24.959	24.959	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.881	-0.940	12.789	-17.071	-17.071	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.005	-0.007	15.205	0.964	0.964	0.000	0.000	0.000	0.000
14	A	14	ILE	0	-0.070	-0.026	13.562	0.765	0.765	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.030	-0.013	17.086	0.697	0.697	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.978	-0.990	18.878	-13.791	-13.791	0.000	0.000	0.000	0.000
17	A	17	ASN	0	-0.091	-0.055	20.193	0.948	0.948	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.749	-0.854	22.323	-10.319	-10.319	0.000	0.000	0.000	0.000
19	A	19	ILE	0	0.016	0.013	23.481	-0.025	-0.025	0.000	0.000	0.000	0.000
20	A	20	PHE	0	-0.004	0.008	15.297	-0.248	-0.248	0.000	0.000	0.000	0.000
21	A	21	VAL	0	0.002	-0.007	20.338	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	22	ALA	0	0.013	0.029	16.049	-0.129	-0.129	0.000	0.000	0.000	0.000
23	A	23	SER	0	0.006	-0.039	18.064	0.673	0.673	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.886	0.939	15.009	18.375	18.375	0.000	0.000	0.000	0.000
25	A	25	THR	0	0.008	0.017	21.180	0.491	0.491	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.004	0.004	19.648	0.294	0.294	0.000	0.000	0.000	0.000
27	A	27	CYS	0	-0.076	-0.001	21.593	0.383	0.383	0.000	0.000	0.000	0.000
28	A	28	PRO	0	0.075	0.031	24.347	0.130	0.130	0.000	0.000	0.000	0.000
29	A	29	TYR	0	0.043	0.011	23.396	0.217	0.217	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.029	-0.005	22.637	-0.222	-0.222	0.000	0.000	0.000	0.000
31	A	31	HIS	0	-0.042	-0.030	24.892	0.453	0.453	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.000	0.008	28.566	0.302	0.302	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.062	0.046	25.565	0.323	0.323	0.000	0.000	0.000	0.000
34	A	34	LEU	0	0.006	0.002	25.167	0.249	0.249	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.021	-0.019	28.647	0.274	0.274	0.000	0.000	0.000	0.000
36	A	36	THR	0	-0.038	-0.051	29.999	0.466	0.466	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.057	0.028	25.977	0.240	0.240	0.000	0.000	0.000	0.000
38	A	38	PHE	0	-0.006	-0.012	28.012	0.219	0.219	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.964	-0.966	32.856	-8.522	-8.522	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.811	0.908	33.151	9.502	9.502	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.023	0.023	31.342	0.171	0.171	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.894	0.962	35.054	7.682	7.682	0.000	0.000	0.000	0.000
43	A	43	VAL	0	0.074	0.052	29.577	0.094	0.094	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.016	0.002	32.944	-0.074	-0.074	0.000	0.000	0.000	0.000
45	A	45	ARG	1	0.925	0.950	31.009	9.225	9.225	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.027	-0.016	29.407	-0.314	-0.314	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.826	0.918	28.400	9.460	9.460	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.003	-0.002	24.901	-0.283	-0.283	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.003	0.020	19.528	0.085	0.085	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.032	-0.022	21.743	-0.473	-0.473	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.004	0.005	16.509	-0.018	-0.018	0.000	0.000	0.000	0.000
52	A	52	GLN	0	0.065	0.035	19.421	-0.703	-0.703	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.012	-0.006	14.048	-0.080	-0.080	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.074	-0.038	16.652	-0.963	-0.963	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.837	-0.914	18.795	-13.668	-13.668	0.000	0.000	0.000	0.000
56	A	56	MET	0	-0.024	-0.011	16.868	0.398	0.398	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.829	0.909	14.041	21.299	21.299	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.749	-0.867	11.577	-24.719	-24.719	0.000	0.000	0.000	0.000
59	A	59	GLY	0	-0.003	0.000	12.274	-1.431	-1.431	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.012	-0.009	10.272	-0.119	-0.119	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.870	-0.941	7.243	-41.297	-41.297	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.010	0.001	8.184	-1.739	-1.739	0.000	0.000	0.000	0.000
63	A	63	GLN	0	-0.011	-0.008	10.543	0.678	0.678	0.000	0.000	0.000	0.000
64	A	64	ALA	0	-0.035	-0.015	5.451	0.200	0.200	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.016	-0.003	6.167	-1.401	-1.401	0.000	0.000	0.000	0.000
66	A	66	LEU	0	0.006	0.003	7.156	1.214	1.214	0.000	0.000	0.000	0.000
67	A	67	TYR	0	-0.020	0.001	6.376	2.423	2.423	0.000	0.000	0.000	0.000
69	A	69	ILE	0	-0.095	-0.036	6.592	1.626	1.626	0.000	0.000	0.000	0.000
70	A	70	ASN	0	0.010	-0.012	9.378	0.914	0.914	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.017	0.024	10.661	1.302	1.302	0.000	0.000	0.000	0.000
72	A	72	GLN	0	-0.031	-0.023	11.683	0.202	0.202	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.934	0.957	9.471	24.420	24.420	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.018	0.000	13.330	-0.539	-0.539	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.012	0.017	16.347	-0.501	-0.501	0.000	0.000	0.000	0.000
76	A	76	PRO	0	0.000	-0.018	18.674	0.513	0.513	0.000	0.000	0.000	0.000
77	A	77	ASN	0	-0.044	-0.014	14.105	0.505	0.505	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.001	0.005	17.930	-0.221	-0.221	0.000	0.000	0.000	0.000
79	A	79	TYR	0	0.037	0.022	14.203	-0.788	-0.788	0.000	0.000	0.000	0.000
80	A	80	ILE	0	0.035	0.018	20.219	0.238	0.238	0.000	0.000	0.000	0.000
81	A	81	ASN	0	0.040	0.010	23.037	-0.173	-0.173	0.000	0.000	0.000	0.000
82	A	82	GLY	0	0.001	0.011	18.979	0.083	0.083	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.919	0.974	18.555	10.828	10.828	0.000	0.000	0.000	0.000
84	A	84	HIS	0	-0.042	-0.024	16.971	0.144	0.144	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.045	-0.031	19.040	0.499	0.499	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.058	0.044	19.176	0.229	0.229	0.000	0.000	0.000	0.000
87	A	87	GLY	0	-0.006	-0.017	20.214	-0.355	-0.355	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.030	-0.043	21.785	0.629	0.629	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.902	-0.953	23.675	-12.377	-12.377	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.780	-0.875	22.051	-12.882	-12.882	0.000	0.000	0.000	0.000
91	A	91	LEU	0	-0.038	-0.023	25.323	0.314	0.314	0.000	0.000	0.000	0.000
92	A	92	GLN	0	-0.071	-0.034	27.030	0.733	0.733	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.851	-0.917	27.854	-9.785	-9.785	0.000	0.000	0.000	0.000
94	A	94	LEU	0	0.016	0.007	25.803	0.260	0.260	0.000	0.000	0.000	0.000
95	A	95	ARG	1	0.810	0.892	30.170	9.485	9.485	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-1.027	-1.004	32.923	-8.899	-8.899	0.000	0.000	0.000	0.000
97	A	97	THR	0	-0.059	-0.064	31.676	0.312	0.312	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.038	-0.014	34.367	0.233	0.233	0.000	0.000	0.000	0.000
99	A	99	GLU	-1	-0.869	-0.898	30.624	-9.699	-9.699	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.058	-0.040	28.316	-0.275	-0.275	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.929	-0.969	31.098	-8.658	-8.658	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.892	-0.941	30.956	-9.260	-9.260	0.000	0.000	0.000	0.000
103	A	103	LEU	0	-0.076	-0.045	26.285	-0.250	-0.250	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.035	-0.028	28.997	-0.284	-0.284	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.879	-0.943	31.301	-8.148	-8.148	0.000	0.000	0.000	0.000
106	A	106	PRO	0	-0.096	-0.046	29.781	0.118	0.118	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.108	-0.049	27.166	-0.179	-0.179	0.000	0.000	0.000	0.000
108	A	108	LEU	-1	-0.969	-0.975	31.469	-8.320	-8.320	0.000	0.000	0.000	0.000

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