FMO DATABASE

FMODB ID: 34Q8L

Calculation Name: 5E7X-A-Xray549

Preferred Name:

Target Type:

Ligand Name: palmitic acid | acetate ion | glycerol

Ligand 3-letter code: PLM | ACT | GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5E7X

Chain ID: A

ChEMBL ID:

UniProt ID: A8HBN5

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	155
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1338372.996452
FMO2-HF: Nuclear repulsion	1282105.134352
FMO2-HF: Total energy	-56267.8621
FMO2-MP2: Total energy	-56435.850903

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:27:THR)

Summations of interaction energy for fragment #1(A:27:THR)

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.
-33.753	-29.091	13.13	-8.013	-9.778	-0.088

Interaction energy analysis for fragmet #1(A:27:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.813 / q_NPA : 0.901

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	29	ASP	-1	-0.733	-0.850	2.701	-46.681	-42.994	0.513	-1.692	-2.507	-0.005
4	A	30	GLN	0	0.082	0.009	1.886	-35.909	-35.488	12.605	-6.218	-6.808	-0.082
5	A	31	ARG	1	0.884	0.939	3.647	55.048	55.602	0.012	-0.103	-0.463	-0.001
6	A	32	ASP	-1	-0.844	-0.915	5.976	-30.371	-30.371	0.000	0.000	0.000	0.000
7	A	33	VAL	0	0.003	0.009	6.460	3.212	3.212	0.000	0.000	0.000	0.000
8	A	34	ASN	0	-0.032	-0.031	7.196	4.686	4.686	0.000	0.000	0.000	0.000
9	A	35	VAL	0	0.018	0.026	9.664	1.876	1.876	0.000	0.000	0.000	0.000
10	A	36	PHE	0	0.087	0.035	11.936	1.625	1.625	0.000	0.000	0.000	0.000
11	A	37	LYS	1	0.903	0.957	9.126	29.383	29.383	0.000	0.000	0.000	0.000
12	A	38	LYS	1	0.829	0.913	12.084	24.400	24.400	0.000	0.000	0.000	0.000
13	A	39	VAL	0	0.039	0.048	15.429	1.212	1.212	0.000	0.000	0.000	0.000
14	A	40	LEU	0	-0.008	-0.014	15.752	0.926	0.926	0.000	0.000	0.000	0.000
15	A	41	GLU	-1	-0.857	-0.908	15.774	-19.100	-19.100	0.000	0.000	0.000	0.000
16	A	42	ASN	0	-0.016	-0.013	18.897	0.879	0.879	0.000	0.000	0.000	0.000
17	A	43	ILE	0	0.012	0.007	21.317	0.756	0.756	0.000	0.000	0.000	0.000
18	A	44	GLY	0	0.020	0.009	21.928	0.629	0.629	0.000	0.000	0.000	0.000
19	A	45	ASN	0	-0.012	-0.001	20.947	0.782	0.782	0.000	0.000	0.000	0.000
20	A	46	ALA	0	0.011	0.013	24.628	0.519	0.519	0.000	0.000	0.000	0.000
21	A	47	VAL	0	0.011	-0.008	26.704	0.500	0.500	0.000	0.000	0.000	0.000
22	A	48	THR	0	-0.035	-0.028	26.070	0.429	0.429	0.000	0.000	0.000	0.000
23	A	49	GLN	0	-0.060	-0.031	28.690	0.068	0.068	0.000	0.000	0.000	0.000
24	A	50	PHE	0	0.040	0.013	30.981	0.380	0.380	0.000	0.000	0.000	0.000
25	A	51	ASN	0	0.028	0.016	31.481	0.500	0.500	0.000	0.000	0.000	0.000
26	A	52	ASN	0	-0.008	-0.007	30.551	0.312	0.312	0.000	0.000	0.000	0.000
27	A	53	ASP	-1	-0.756	-0.836	34.359	-8.806	-8.806	0.000	0.000	0.000	0.000
28	A	54	ILE	0	-0.037	-0.007	35.089	0.343	0.343	0.000	0.000	0.000	0.000
29	A	55	LEU	0	-0.042	-0.015	35.036	0.292	0.292	0.000	0.000	0.000	0.000
30	A	56	ALA	0	-0.008	-0.003	38.682	0.240	0.240	0.000	0.000	0.000	0.000
31	A	57	TYR	0	-0.035	-0.022	40.582	0.232	0.232	0.000	0.000	0.000	0.000
32	A	58	THR	0	-0.002	-0.011	42.809	0.062	0.062	0.000	0.000	0.000	0.000
33	A	59	GLY	0	0.024	0.005	46.382	0.152	0.152	0.000	0.000	0.000	0.000
34	A	60	GLY	0	-0.018	0.009	47.752	-0.058	-0.058	0.000	0.000	0.000	0.000
35	A	61	ASP	-1	-0.831	-0.897	44.972	-7.203	-7.203	0.000	0.000	0.000	0.000
36	A	62	ALA	0	0.064	0.031	42.958	-0.123	-0.123	0.000	0.000	0.000	0.000
37	A	63	ASN	0	-0.051	-0.045	41.869	-0.220	-0.220	0.000	0.000	0.000	0.000
38	A	64	HIS	0	-0.020	-0.011	35.798	-0.045	-0.045	0.000	0.000	0.000	0.000
39	A	65	LEU	0	0.018	0.025	37.607	-0.247	-0.247	0.000	0.000	0.000	0.000
40	A	66	ILE	0	-0.013	-0.019	37.265	-0.206	-0.206	0.000	0.000	0.000	0.000
41	A	67	HIS	0	0.015	0.018	34.287	-0.100	-0.100	0.000	0.000	0.000	0.000
42	A	68	ASP	0	-0.067	-0.077	33.350	-0.353	-0.353	0.000	0.000	0.000	0.000
43	A	69	GLY	0	0.008	0.016	32.393	-0.346	-0.346	0.000	0.000	0.000	0.000
44	A	70	ASP	-1	-0.844	-0.928	32.649	-9.033	-9.033	0.000	0.000	0.000	0.000
45	A	71	ALA	0	-0.020	-0.010	30.098	-0.287	-0.287	0.000	0.000	0.000	0.000
46	A	72	ILE	0	-0.011	0.006	27.659	-0.545	-0.545	0.000	0.000	0.000	0.000
47	A	73	ILE	0	-0.017	0.013	27.813	-0.403	-0.403	0.000	0.000	0.000	0.000
48	A	74	LYS	1	0.905	0.971	28.248	10.684	10.684	0.000	0.000	0.000	0.000
49	A	75	ALA	0	0.014	0.002	24.110	-0.381	-0.381	0.000	0.000	0.000	0.000
50	A	76	THR	0	-0.041	-0.035	23.695	-0.693	-0.693	0.000	0.000	0.000	0.000
51	A	77	GLU	-1	-0.930	-0.978	24.808	-10.621	-10.621	0.000	0.000	0.000	0.000
52	A	78	ASN	0	-0.059	-0.021	22.906	0.235	0.235	0.000	0.000	0.000	0.000
53	A	79	GLY	0	0.094	0.026	20.454	-0.484	-0.484	0.000	0.000	0.000	0.000
54	A	80	LEU	0	-0.031	-0.018	20.680	-0.529	-0.529	0.000	0.000	0.000	0.000
55	A	81	GLN	0	-0.062	-0.021	22.617	0.269	0.269	0.000	0.000	0.000	0.000
56	A	82	GLU	-1	-0.948	-0.984	17.816	-17.005	-17.005	0.000	0.000	0.000	0.000
57	A	83	LEU	0	-0.014	-0.027	15.580	-1.015	-1.015	0.000	0.000	0.000	0.000
58	A	84	GLY	0	0.036	0.030	18.382	-0.090	-0.090	0.000	0.000	0.000	0.000
59	A	85	PRO	0	-0.019	-0.017	18.968	0.149	0.149	0.000	0.000	0.000	0.000
60	A	86	GLN	0	-0.035	0.006	13.607	-1.477	-1.477	0.000	0.000	0.000	0.000
61	A	87	PRO	0	0.019	0.016	12.924	1.150	1.150	0.000	0.000	0.000	0.000
62	A	88	PRO	0	-0.005	-0.017	14.890	-0.332	-0.332	0.000	0.000	0.000	0.000
63	A	89	LEU	0	-0.009	0.008	10.339	-1.072	-1.072	0.000	0.000	0.000	0.000
64	A	90	SER	0	-0.032	-0.044	8.326	1.977	1.977	0.000	0.000	0.000	0.000
65	A	91	LEU	0	0.012	-0.013	11.365	0.323	0.323	0.000	0.000	0.000	0.000
66	A	92	THR	0	-0.011	-0.008	7.141	1.825	1.825	0.000	0.000	0.000	0.000
67	A	93	GLU	-1	-0.812	-0.896	6.923	-30.150	-30.150	0.000	0.000	0.000	0.000
68	A	94	ALA	0	0.018	0.007	9.007	0.729	0.729	0.000	0.000	0.000	0.000
69	A	95	LEU	0	-0.001	-0.007	12.330	1.015	1.015	0.000	0.000	0.000	0.000
70	A	96	ALA	0	-0.056	-0.017	9.425	0.762	0.762	0.000	0.000	0.000	0.000
71	A	97	LEU	0	-0.005	-0.010	11.319	-0.348	-0.348	0.000	0.000	0.000	0.000
72	A	98	VAL	0	-0.002	0.009	13.906	1.087	1.087	0.000	0.000	0.000	0.000
73	A	99	GLY	0	0.036	0.024	16.310	0.806	0.806	0.000	0.000	0.000	0.000
74	A	100	PRO	0	-0.019	-0.025	14.033	0.715	0.715	0.000	0.000	0.000	0.000
75	A	101	VAL	0	0.045	0.035	17.374	0.683	0.683	0.000	0.000	0.000	0.000
76	A	102	GLN	0	0.003	0.000	19.771	0.409	0.409	0.000	0.000	0.000	0.000
77	A	103	GLY	0	-0.028	-0.008	20.848	0.683	0.683	0.000	0.000	0.000	0.000
78	A	104	VAL	0	0.030	0.013	20.741	0.621	0.621	0.000	0.000	0.000	0.000
79	A	105	ASN	0	-0.018	-0.028	23.217	0.345	0.345	0.000	0.000	0.000	0.000
80	A	106	LYS	1	0.926	0.959	25.426	11.581	11.581	0.000	0.000	0.000	0.000
81	A	107	LEU	0	-0.019	0.001	25.584	0.445	0.445	0.000	0.000	0.000	0.000
82	A	108	ILE	0	0.037	0.030	26.031	0.458	0.458	0.000	0.000	0.000	0.000
83	A	109	MET	0	-0.032	-0.023	29.236	0.278	0.278	0.000	0.000	0.000	0.000
84	A	110	LYS	1	0.958	0.983	31.166	9.928	9.928	0.000	0.000	0.000	0.000
85	A	111	THR	0	0.009	0.000	30.622	0.234	0.234	0.000	0.000	0.000	0.000
86	A	112	VAL	0	-0.017	-0.007	33.224	0.275	0.275	0.000	0.000	0.000	0.000
87	A	113	ASP	-1	-0.881	-0.931	35.449	-8.356	-8.356	0.000	0.000	0.000	0.000
88	A	114	HIS	0	-0.010	-0.029	34.129	0.282	0.282	0.000	0.000	0.000	0.000
89	A	115	LEU	0	-0.007	0.003	36.884	0.205	0.205	0.000	0.000	0.000	0.000
90	A	116	ILE	0	-0.046	-0.031	39.089	0.252	0.252	0.000	0.000	0.000	0.000
91	A	117	GLU	-1	-0.934	-0.967	40.606	-7.716	-7.716	0.000	0.000	0.000	0.000
92	A	118	LYS	1	0.771	0.881	41.373	7.915	7.915	0.000	0.000	0.000	0.000
93	A	119	LYS	1	0.912	0.951	43.774	6.871	6.871	0.000	0.000	0.000	0.000
94	A	120	GLY	0	-0.010	-0.002	45.391	0.110	0.110	0.000	0.000	0.000	0.000
95	A	121	PRO	0	0.012	0.010	46.094	0.108	0.108	0.000	0.000	0.000	0.000
96	A	122	LEU	0	0.016	0.015	41.810	0.049	0.049	0.000	0.000	0.000	0.000
97	A	123	VAL	0	-0.046	-0.030	46.365	0.036	0.036	0.000	0.000	0.000	0.000
98	A	124	GLY	0	-0.020	-0.003	48.999	0.107	0.107	0.000	0.000	0.000	0.000
99	A	125	GLY	0	-0.021	-0.010	49.559	0.117	0.117	0.000	0.000	0.000	0.000
100	A	126	GLY	0	-0.012	-0.002	50.208	-0.005	-0.005	0.000	0.000	0.000	0.000
101	A	127	TYR	0	0.022	0.005	44.651	-0.024	-0.024	0.000	0.000	0.000	0.000
102	A	128	GLY	0	-0.004	0.006	45.017	-0.151	-0.151	0.000	0.000	0.000	0.000
103	A	129	PRO	0	0.043	0.006	44.593	-0.159	-0.159	0.000	0.000	0.000	0.000
104	A	130	GLN	0	0.031	0.021	42.111	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	131	VAL	0	0.014	0.007	39.847	-0.238	-0.238	0.000	0.000	0.000	0.000
106	A	132	LYS	1	0.886	0.941	39.653	6.866	6.866	0.000	0.000	0.000	0.000
107	A	133	ALA	0	0.004	0.000	39.935	-0.176	-0.176	0.000	0.000	0.000	0.000
108	A	134	SER	0	-0.003	-0.018	36.391	-0.264	-0.264	0.000	0.000	0.000	0.000
109	A	135	LEU	0	0.012	0.002	35.215	-0.285	-0.285	0.000	0.000	0.000	0.000
110	A	136	GLN	0	-0.001	-0.008	35.324	-0.120	-0.120	0.000	0.000	0.000	0.000
111	A	137	LYS	1	0.956	0.986	34.221	8.828	8.828	0.000	0.000	0.000	0.000
112	A	138	GLN	0	-0.036	-0.022	31.647	-0.431	-0.431	0.000	0.000	0.000	0.000
113	A	139	ALA	0	0.009	0.005	30.827	-0.365	-0.365	0.000	0.000	0.000	0.000
114	A	140	HIS	0	0.002	0.001	31.409	-0.359	-0.359	0.000	0.000	0.000	0.000
115	A	141	ALA	0	0.011	0.020	28.774	-0.215	-0.215	0.000	0.000	0.000	0.000
116	A	142	ALA	0	0.016	0.001	26.877	-0.437	-0.437	0.000	0.000	0.000	0.000
117	A	143	VAL	0	0.006	0.006	26.624	-0.398	-0.398	0.000	0.000	0.000	0.000
118	A	144	THR	0	0.012	0.006	27.114	-0.215	-0.215	0.000	0.000	0.000	0.000
119	A	145	LEU	0	-0.007	-0.011	20.968	-0.383	-0.383	0.000	0.000	0.000	0.000
120	A	146	SER	0	-0.070	-0.037	22.568	-0.516	-0.516	0.000	0.000	0.000	0.000
121	A	147	GLU	-1	-0.861	-0.927	23.214	-11.426	-11.426	0.000	0.000	0.000	0.000
122	A	148	LEU	0	-0.057	-0.004	20.700	-0.355	-0.355	0.000	0.000	0.000	0.000
123	A	149	VAL	0	0.001	-0.005	17.387	-0.705	-0.705	0.000	0.000	0.000	0.000
124	A	150	SER	0	0.001	-0.018	18.787	-0.698	-0.698	0.000	0.000	0.000	0.000
125	A	151	SER	0	-0.092	-0.057	20.852	-0.186	-0.186	0.000	0.000	0.000	0.000
126	A	152	LYS	1	0.802	0.905	15.837	15.383	15.383	0.000	0.000	0.000	0.000
127	A	153	VAL	0	-0.027	0.000	15.834	-1.195	-1.195	0.000	0.000	0.000	0.000
128	A	154	PRO	0	0.025	0.022	15.098	0.879	0.879	0.000	0.000	0.000	0.000
129	A	155	SER	0	0.051	0.008	18.120	0.021	0.021	0.000	0.000	0.000	0.000
130	A	156	PRO	0	-0.013	-0.014	18.542	0.439	0.439	0.000	0.000	0.000	0.000
131	A	157	LEU	0	0.028	0.006	16.091	0.214	0.214	0.000	0.000	0.000	0.000
132	A	158	ALA	0	0.029	0.047	20.116	0.186	0.186	0.000	0.000	0.000	0.000
133	A	159	PRO	0	-0.017	-0.020	23.241	0.347	0.347	0.000	0.000	0.000	0.000
134	A	160	ILE	0	-0.009	-0.009	20.559	0.390	0.390	0.000	0.000	0.000	0.000
135	A	161	SER	0	0.012	-0.007	20.600	0.259	0.259	0.000	0.000	0.000	0.000
136	A	162	LYS	1	0.995	1.024	22.417	10.791	10.791	0.000	0.000	0.000	0.000
137	A	163	GLN	0	-0.022	-0.005	25.443	0.425	0.425	0.000	0.000	0.000	0.000
138	A	164	LEU	0	-0.035	-0.025	21.101	0.196	0.196	0.000	0.000	0.000	0.000
139	A	165	SER	0	0.060	0.018	24.700	-0.090	-0.090	0.000	0.000	0.000	0.000
140	A	166	ASP	-1	-0.890	-0.946	26.573	-9.826	-9.826	0.000	0.000	0.000	0.000
141	A	167	GLN	0	-0.019	-0.004	26.704	-0.040	-0.040	0.000	0.000	0.000	0.000
142	A	168	VAL	0	0.006	0.012	25.830	0.275	0.275	0.000	0.000	0.000	0.000
143	A	169	ALA	0	0.019	0.012	29.124	0.284	0.284	0.000	0.000	0.000	0.000
144	A	170	GLN	0	-0.017	-0.022	31.927	0.245	0.245	0.000	0.000	0.000	0.000
145	A	171	ALA	0	-0.026	-0.005	31.440	0.270	0.270	0.000	0.000	0.000	0.000
146	A	172	LEU	0	0.035	0.011	30.239	0.240	0.240	0.000	0.000	0.000	0.000
147	A	173	GLN	0	-0.005	0.002	34.258	0.366	0.366	0.000	0.000	0.000	0.000
148	A	174	LYS	1	0.910	0.954	36.888	8.440	8.440	0.000	0.000	0.000	0.000
149	A	175	GLY	0	0.035	0.009	37.401	0.191	0.191	0.000	0.000	0.000	0.000
150	A	176	ILE	0	-0.025	-0.016	36.664	0.227	0.227	0.000	0.000	0.000	0.000
151	A	177	GLU	-1	-0.937	-0.952	40.342	-7.312	-7.312	0.000	0.000	0.000	0.000
152	A	178	ALA	0	0.003	0.011	41.770	0.203	0.203	0.000	0.000	0.000	0.000
153	A	179	PHE	0	-0.042	-0.025	41.257	0.203	0.203	0.000	0.000	0.000	0.000
154	A	180	SER	0	-0.061	-0.037	44.221	0.052	0.052	0.000	0.000	0.000	0.000
155	A	181	ILE	-1	-0.949	-0.956	46.545	-6.247	-6.247	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:27:THR)