FMO DATABASE

FMODB ID: MR79Z

Calculation Name: 2F0X-A-Xray547

Preferred Name: Acyl-coenzyme A thioesterase 13

Target Type: SINGLE PROTEIN

Ligand Name: sulfate ion

Ligand 3-letter code: SO4

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F0X

Chain ID: A

ChEMBL ID: CHEMBL4295957

UniProt ID: Q9NPJ3

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1141603.209118
FMO2-HF: Nuclear repulsion	1089540.030729
FMO2-HF: Total energy	-52063.17839
FMO2-MP2: Total energy	-52211.187387

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:SER)

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

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.
5.446	9.547	8.965	-6.531	-6.536	-0.045

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.882 / q_NPA : 0.913

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	5	THR	0	0.088	0.030	3.863	2.195	3.201	-0.009	-0.377	-0.621	0.000
4	A	6	GLN	0	-0.065	-0.025	1.889	-15.993	-14.316	8.960	-5.502	-5.135	-0.041
5	A	7	SER	0	0.047	0.020	3.269	-1.225	0.052	0.015	-0.640	-0.652	-0.004
6	A	8	LEU	0	0.042	0.022	5.153	6.304	6.445	-0.001	-0.012	-0.128	0.000
7	A	9	ARG	1	0.965	0.990	6.597	36.228	36.228	0.000	0.000	0.000	0.000
8	A	10	GLU	-1	-0.907	-0.950	5.254	-43.003	-43.003	0.000	0.000	0.000	0.000
9	A	11	VAL	0	0.009	0.000	9.119	3.022	3.022	0.000	0.000	0.000	0.000
10	A	12	ILE	0	0.004	-0.005	11.299	2.102	2.102	0.000	0.000	0.000	0.000
11	A	13	LYS	1	0.766	0.862	12.215	20.075	20.075	0.000	0.000	0.000	0.000
12	A	14	ALA	0	-0.009	0.001	13.494	1.371	1.371	0.000	0.000	0.000	0.000
13	A	15	MET	0	-0.005	-0.001	15.199	1.303	1.303	0.000	0.000	0.000	0.000
14	A	16	THR	-1	-0.713	-0.832	17.664	-16.488	-16.488	0.000	0.000	0.000	0.000
15	A	17	LYS	1	0.879	0.940	16.524	18.281	18.281	0.000	0.000	0.000	0.000
16	A	18	ALA	0	0.009	0.031	18.810	0.445	0.445	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.885	0.921	20.655	13.800	13.800	0.000	0.000	0.000	0.000
18	A	20	ASN	0	0.019	0.000	19.283	0.836	0.836	0.000	0.000	0.000	0.000
19	A	21	PHE	0	0.036	-0.002	23.684	0.131	0.131	0.000	0.000	0.000	0.000
20	A	22	GLU	-1	-0.774	-0.878	17.417	-17.737	-17.737	0.000	0.000	0.000	0.000
21	A	23	ARG	1	0.882	0.959	20.595	11.723	11.723	0.000	0.000	0.000	0.000
22	A	24	VAL	0	-0.027	-0.005	22.312	0.004	0.004	0.000	0.000	0.000	0.000
23	A	25	LEU	0	-0.011	-0.006	18.979	0.164	0.164	0.000	0.000	0.000	0.000
24	A	26	GLY	0	-0.014	-0.008	19.120	-0.705	-0.705	0.000	0.000	0.000	0.000
25	A	27	LYS	1	0.819	0.893	19.811	12.090	12.090	0.000	0.000	0.000	0.000
26	A	28	ILE	0	-0.046	-0.016	16.335	0.197	0.197	0.000	0.000	0.000	0.000
27	A	29	THR	0	-0.030	-0.011	15.317	-0.714	-0.714	0.000	0.000	0.000	0.000
28	A	30	LEU	0	-0.012	-0.015	8.594	-0.107	-0.107	0.000	0.000	0.000	0.000
29	A	31	VAL	0	-0.015	-0.001	12.917	-0.087	-0.087	0.000	0.000	0.000	0.000
30	A	32	SER	0	-0.051	-0.040	10.931	-0.463	-0.463	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.022	0.004	7.879	0.448	0.448	0.000	0.000	0.000	0.000
32	A	34	ALA	0	-0.007	-0.002	9.123	-1.620	-1.620	0.000	0.000	0.000	0.000
33	A	35	PRO	0	0.025	-0.002	9.485	0.057	0.057	0.000	0.000	0.000	0.000
34	A	36	GLY	0	0.025	0.033	11.305	1.915	1.915	0.000	0.000	0.000	0.000
35	A	37	LYS	1	0.925	0.958	12.812	18.781	18.781	0.000	0.000	0.000	0.000
36	A	38	VAL	0	0.010	-0.002	11.372	-2.127	-2.127	0.000	0.000	0.000	0.000
37	A	39	ILE	0	-0.041	-0.007	13.774	1.734	1.734	0.000	0.000	0.000	0.000
38	A	40	CYS	0	0.009	0.005	14.352	-1.926	-1.926	0.000	0.000	0.000	0.000
39	A	41	GLU	-1	-0.793	-0.868	16.424	-14.076	-14.076	0.000	0.000	0.000	0.000
40	A	42	MET	0	-0.015	0.000	19.059	-0.712	-0.712	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.883	0.939	21.885	11.633	11.633	0.000	0.000	0.000	0.000
42	A	44	VAL	0	-0.021	-0.008	25.291	-0.105	-0.105	0.000	0.000	0.000	0.000
43	A	45	GLU	-1	-0.832	-0.918	27.003	-11.003	-11.003	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.900	-0.954	29.750	-8.978	-8.978	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.847	-0.906	26.711	-11.896	-11.896	0.000	0.000	0.000	0.000
46	A	48	HIS	0	-0.009	-0.006	25.553	-0.064	-0.064	0.000	0.000	0.000	0.000
47	A	49	THR	0	-0.067	-0.039	29.400	0.090	0.090	0.000	0.000	0.000	0.000
48	A	50	ASN	0	-0.021	-0.030	32.977	0.178	0.178	0.000	0.000	0.000	0.000
49	A	51	ALA	0	0.019	-0.006	35.893	0.043	0.043	0.000	0.000	0.000	0.000
50	A	52	ILE	0	-0.033	-0.003	38.703	0.203	0.203	0.000	0.000	0.000	0.000
51	A	53	GLY	0	0.036	0.030	36.675	0.033	0.033	0.000	0.000	0.000	0.000
52	A	54	THR	0	-0.024	-0.018	34.388	-0.156	-0.156	0.000	0.000	0.000	0.000
53	A	55	LEU	0	0.000	0.002	27.475	0.009	0.009	0.000	0.000	0.000	0.000
54	A	56	HIS	0	0.033	0.024	30.823	0.049	0.049	0.000	0.000	0.000	0.000
55	A	57	GLY	0	0.037	0.019	30.240	-0.385	-0.385	0.000	0.000	0.000	0.000
56	A	58	GLY	0	0.048	0.013	29.969	-0.269	-0.269	0.000	0.000	0.000	0.000
57	A	59	LEU	0	0.020	0.029	24.702	-0.397	-0.397	0.000	0.000	0.000	0.000
58	A	60	THR	0	-0.017	-0.011	25.509	-0.566	-0.566	0.000	0.000	0.000	0.000
59	A	61	ALA	0	0.029	0.002	25.481	-0.469	-0.469	0.000	0.000	0.000	0.000
60	A	62	THR	0	-0.015	-0.018	22.280	-0.397	-0.397	0.000	0.000	0.000	0.000
61	A	63	LEU	0	-0.005	-0.003	21.008	-0.860	-0.860	0.000	0.000	0.000	0.000
62	A	64	VAL	0	0.007	0.000	20.566	-0.863	-0.863	0.000	0.000	0.000	0.000
63	A	65	ASP	-1	-0.818	-0.904	20.548	-15.599	-15.599	0.000	0.000	0.000	0.000
64	A	66	ASN	0	0.017	-0.008	16.464	-0.117	-0.117	0.000	0.000	0.000	0.000
65	A	67	ILE	0	0.026	0.006	15.920	-1.605	-1.605	0.000	0.000	0.000	0.000
66	A	68	SER	0	0.047	0.036	15.966	-0.675	-0.675	0.000	0.000	0.000	0.000
67	A	69	THR	0	-0.090	-0.039	14.410	-0.578	-0.578	0.000	0.000	0.000	0.000
68	A	70	MET	0	-0.022	-0.012	11.876	-1.680	-1.680	0.000	0.000	0.000	0.000
69	A	71	ALA	0	0.023	0.010	11.269	-2.425	-2.425	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.003	0.001	12.812	-0.491	-0.491	0.000	0.000	0.000	0.000
71	A	73	LEU	0	-0.022	0.007	8.612	-0.756	-0.756	0.000	0.000	0.000	0.000
72	A	74	CYS	0	-0.080	-0.034	8.092	-5.235	-5.235	0.000	0.000	0.000	0.000
73	A	75	THR	0	-0.022	-0.027	9.198	2.051	2.051	0.000	0.000	0.000	0.000
74	A	76	GLU	-1	-0.917	-0.964	9.289	-24.889	-24.889	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.796	0.885	10.720	17.486	17.486	0.000	0.000	0.000	0.000
76	A	78	GLY	0	0.018	0.019	9.132	0.029	0.029	0.000	0.000	0.000	0.000
77	A	79	ALA	0	-0.027	-0.010	9.905	0.028	0.028	0.000	0.000	0.000	0.000
78	A	80	PRO	0	0.023	0.006	12.585	0.679	0.679	0.000	0.000	0.000	0.000
79	A	81	GLY	0	0.061	0.019	14.602	0.851	0.851	0.000	0.000	0.000	0.000
80	A	82	VAL	0	-0.051	-0.020	18.211	-0.228	-0.228	0.000	0.000	0.000	0.000
81	A	83	SER	0	0.005	-0.024	21.562	-0.093	-0.093	0.000	0.000	0.000	0.000
82	A	84	VAL	0	-0.085	-0.025	23.551	0.316	0.316	0.000	0.000	0.000	0.000
83	A	85	ASP	-1	-0.876	-0.932	26.482	-10.191	-10.191	0.000	0.000	0.000	0.000
84	A	86	MET	0	-0.016	-0.019	23.643	-0.451	-0.451	0.000	0.000	0.000	0.000
85	A	87	ASN	0	-0.033	0.000	27.823	0.291	0.291	0.000	0.000	0.000	0.000
86	A	88	ILE	0	0.037	0.004	27.965	-0.460	-0.460	0.000	0.000	0.000	0.000
87	A	89	THR	0	-0.009	0.014	30.395	0.516	0.516	0.000	0.000	0.000	0.000
88	A	90	TYR	0	-0.009	-0.021	30.801	-0.237	-0.237	0.000	0.000	0.000	0.000
89	A	91	MET	0	-0.016	-0.010	31.107	0.346	0.346	0.000	0.000	0.000	0.000
90	A	92	SER	0	-0.031	-0.015	33.335	0.268	0.268	0.000	0.000	0.000	0.000
91	A	93	PRO	0	0.038	0.028	33.340	-0.318	-0.318	0.000	0.000	0.000	0.000
92	A	94	ALA	0	0.014	0.028	30.026	0.034	0.034	0.000	0.000	0.000	0.000
93	A	95	LYS	1	0.835	0.864	32.010	9.576	9.576	0.000	0.000	0.000	0.000
94	A	96	LEU	0	0.052	0.030	32.001	-0.313	-0.313	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.000	0.002	30.777	0.246	0.246	0.000	0.000	0.000	0.000
96	A	98	GLU	-1	-0.796	-0.847	29.015	-10.264	-10.264	0.000	0.000	0.000	0.000
97	A	99	ASP	-1	-0.842	-0.908	24.821	-12.042	-12.042	0.000	0.000	0.000	0.000
98	A	100	ILE	0	-0.030	-0.023	23.640	0.320	0.320	0.000	0.000	0.000	0.000
99	A	101	VAL	0	0.021	0.008	19.919	-0.649	-0.649	0.000	0.000	0.000	0.000
100	A	102	ILE	0	-0.013	-0.006	19.387	0.587	0.587	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.006	-0.005	18.594	-1.290	-1.290	0.000	0.000	0.000	0.000
102	A	104	ALA	0	0.006	0.017	16.820	0.868	0.868	0.000	0.000	0.000	0.000
103	A	105	HIS	0	-0.016	-0.023	16.967	-1.430	-1.430	0.000	0.000	0.000	0.000
104	A	106	VAL	0	0.010	0.000	15.266	0.853	0.853	0.000	0.000	0.000	0.000
105	A	107	LEU	0	-0.041	-0.005	18.344	0.223	0.223	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.951	0.972	20.996	13.399	13.399	0.000	0.000	0.000	0.000
107	A	109	GLN	0	0.021	0.014	14.962	-0.619	-0.619	0.000	0.000	0.000	0.000
108	A	110	GLY	0	-0.021	-0.015	20.109	0.356	0.356	0.000	0.000	0.000	0.000
109	A	111	LYS	1	0.963	0.976	20.266	11.869	11.869	0.000	0.000	0.000	0.000
110	A	112	THR	0	0.029	0.016	21.252	-0.491	-0.491	0.000	0.000	0.000	0.000
111	A	113	LEU	0	0.033	0.039	22.294	0.174	0.174	0.000	0.000	0.000	0.000
112	A	114	ALA	0	-0.006	-0.006	18.987	-0.358	-0.358	0.000	0.000	0.000	0.000
113	A	115	PHE	0	0.021	0.007	20.979	0.540	0.540	0.000	0.000	0.000	0.000
114	A	116	THR	0	-0.015	-0.023	18.146	-0.298	-0.298	0.000	0.000	0.000	0.000
115	A	117	SER	0	0.021	0.006	21.195	1.019	1.019	0.000	0.000	0.000	0.000
116	A	118	VAL	0	-0.050	-0.025	20.120	-0.913	-0.913	0.000	0.000	0.000	0.000
117	A	119	ASP	-1	-0.825	-0.894	22.500	-11.973	-11.973	0.000	0.000	0.000	0.000
118	A	120	LEU	0	-0.005	-0.003	23.303	-0.571	-0.571	0.000	0.000	0.000	0.000
119	A	121	THR	0	0.025	-0.001	24.212	0.479	0.479	0.000	0.000	0.000	0.000
120	A	122	ASN	0	0.005	-0.005	25.672	-0.339	-0.339	0.000	0.000	0.000	0.000
121	A	123	LYS	1	0.841	0.889	21.201	13.970	13.970	0.000	0.000	0.000	0.000
122	A	124	ALA	0	-0.028	-0.004	25.951	-0.051	-0.051	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.031	-0.032	29.172	0.198	0.198	0.000	0.000	0.000	0.000
124	A	126	GLY	0	0.026	0.027	27.464	0.156	0.156	0.000	0.000	0.000	0.000
125	A	127	LYS	1	0.849	0.918	28.531	9.334	9.334	0.000	0.000	0.000	0.000
126	A	128	LEU	0	0.030	0.010	27.764	-0.225	-0.225	0.000	0.000	0.000	0.000
127	A	129	ILE	0	-0.048	-0.008	27.591	0.454	0.454	0.000	0.000	0.000	0.000
128	A	130	ALA	0	0.025	-0.009	28.817	0.424	0.424	0.000	0.000	0.000	0.000
129	A	131	GLN	0	-0.027	-0.015	27.065	-0.055	-0.055	0.000	0.000	0.000	0.000
130	A	132	GLY	0	0.024	0.019	26.169	0.484	0.484	0.000	0.000	0.000	0.000
131	A	133	ARG	1	0.897	0.969	24.937	10.952	10.952	0.000	0.000	0.000	0.000
132	A	134	HIS	0	-0.026	-0.016	21.074	0.681	0.681	0.000	0.000	0.000	0.000
133	A	135	THR	0	-0.013	-0.011	23.317	-0.405	-0.405	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.853	0.931	18.045	16.702	16.702	0.000	0.000	0.000	0.000
135	A	137	HIS	0	-0.010	-0.012	22.145	0.515	0.515	0.000	0.000	0.000	0.000
136	A	138	LEU	-1	-0.879	-0.928	16.934	-15.567	-15.567	0.000	0.000	0.000	0.000

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