FMO DATABASE

FMODB ID: Y7672

Calculation Name: 4EC7-A-Xray547

Preferred Name:

Target Type:

Ligand Name: (2s)-1-hydroxy-3-(tetradecanoyloxy)propan-2-yl docosanoate

Ligand 3-letter code: L44

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4EC7

Chain ID: A

ChEMBL ID:

UniProt ID: P61898

Base Structure: X-ray

Registration Date: 2025-10-06

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	105
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-737522.643113
FMO2-HF: Nuclear repulsion	693455.786851
FMO2-HF: Total energy	-44066.856262
FMO2-MP2: Total energy	-44190.055455

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:9:GLY)

Summations of interaction energy for fragment #1(A:9:GLY)

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.
5.538	6.662	-0.021	-0.44	-0.663	-0.002

Interaction energy analysis for fragmet #1(A:9:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.834 / q_NPA : 0.900

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	11	HIS	0	0.027	0.008	3.771	6.781	7.905	-0.021	-0.440	-0.663	-0.002
4	A	12	SER	0	0.019	0.015	7.162	1.173	1.173	0.000	0.000	0.000	0.000
5	A	13	VAL	0	0.032	0.009	10.489	0.115	0.115	0.000	0.000	0.000	0.000
6	A	14	CYS	0	-0.060	-0.034	13.400	1.326	1.326	0.000	0.000	0.000	0.000
7	A	15	ASP	-1	-0.830	-0.891	12.507	-24.119	-24.119	0.000	0.000	0.000	0.000
8	A	16	SER	0	0.012	0.008	14.488	1.060	1.060	0.000	0.000	0.000	0.000
9	A	17	VAL	0	-0.042	-0.037	16.111	-0.529	-0.529	0.000	0.000	0.000	0.000
10	A	18	SER	0	-0.014	-0.009	17.597	0.232	0.232	0.000	0.000	0.000	0.000
11	A	19	ALA	0	-0.031	-0.020	19.252	-0.096	-0.096	0.000	0.000	0.000	0.000
12	A	20	TRP	0	-0.006	0.004	22.391	0.235	0.235	0.000	0.000	0.000	0.000
13	A	21	VAL	0	-0.017	-0.004	25.373	0.239	0.239	0.000	0.000	0.000	0.000
14	A	22	THR	0	0.011	0.007	28.453	0.041	0.041	0.000	0.000	0.000	0.000
15	A	23	LYS	1	0.857	0.899	29.287	10.487	10.487	0.000	0.000	0.000	0.000
16	A	24	THR	0	0.049	0.027	34.126	0.061	0.061	0.000	0.000	0.000	0.000
17	A	25	THR	0	-0.007	0.002	36.770	0.228	0.228	0.000	0.000	0.000	0.000
18	A	26	ALA	0	0.034	0.021	34.610	-0.324	-0.324	0.000	0.000	0.000	0.000
19	A	27	THR	0	0.003	0.012	35.133	0.304	0.304	0.000	0.000	0.000	0.000
20	A	28	ASP	-1	-0.722	-0.861	35.269	-8.382	-8.382	0.000	0.000	0.000	0.000
21	A	29	ILE	0	-0.028	-0.025	33.304	-0.014	-0.014	0.000	0.000	0.000	0.000
22	A	30	LYS	1	0.814	0.907	35.991	7.936	7.936	0.000	0.000	0.000	0.000
23	A	31	GLY	0	0.022	0.020	38.437	0.152	0.152	0.000	0.000	0.000	0.000
24	A	32	ASN	0	-0.037	-0.021	39.441	0.186	0.186	0.000	0.000	0.000	0.000
25	A	33	THR	0	-0.026	-0.009	39.577	-0.185	-0.185	0.000	0.000	0.000	0.000
26	A	34	VAL	0	-0.041	-0.015	38.967	0.237	0.237	0.000	0.000	0.000	0.000
27	A	35	THR	0	0.017	0.013	39.779	-0.174	-0.174	0.000	0.000	0.000	0.000
28	A	36	VAL	0	-0.026	-0.025	35.435	0.004	0.004	0.000	0.000	0.000	0.000
29	A	37	MET	0	-0.016	-0.006	38.841	0.149	0.149	0.000	0.000	0.000	0.000
30	A	38	GLU	-1	-0.847	-0.916	38.146	-8.088	-8.088	0.000	0.000	0.000	0.000
31	A	39	ASN	0	-0.041	-0.040	37.925	-0.364	-0.364	0.000	0.000	0.000	0.000
32	A	40	VAL	0	0.031	0.015	37.535	0.164	0.164	0.000	0.000	0.000	0.000
33	A	41	ASN	0	-0.029	-0.024	40.672	-0.047	-0.047	0.000	0.000	0.000	0.000
34	A	42	LEU	0	0.004	0.000	38.603	0.040	0.040	0.000	0.000	0.000	0.000
35	A	43	ASP	-1	-0.871	-0.933	40.713	-7.797	-7.797	0.000	0.000	0.000	0.000
36	A	44	ASN	0	-0.061	-0.034	43.921	-0.016	-0.016	0.000	0.000	0.000	0.000
37	A	45	LYS	1	0.901	0.971	41.505	7.610	7.610	0.000	0.000	0.000	0.000
38	A	46	VAL	0	0.015	0.013	41.648	-0.054	-0.054	0.000	0.000	0.000	0.000
39	A	47	TYR	0	-0.003	-0.010	36.671	-0.141	-0.141	0.000	0.000	0.000	0.000
40	A	48	LYS	1	0.907	0.951	35.246	8.555	8.555	0.000	0.000	0.000	0.000
41	A	49	GLU	-1	-0.842	-0.908	34.393	-8.936	-8.936	0.000	0.000	0.000	0.000
42	A	50	TYR	0	-0.030	-0.024	29.294	0.006	0.006	0.000	0.000	0.000	0.000
43	A	51	PHE	0	0.002	-0.010	28.368	-0.023	-0.023	0.000	0.000	0.000	0.000
44	A	52	PHE	0	0.008	0.004	18.404	-0.088	-0.088	0.000	0.000	0.000	0.000
45	A	53	GLU	-1	-0.795	-0.881	24.202	-11.404	-11.404	0.000	0.000	0.000	0.000
46	A	54	THR	0	-0.075	-0.038	17.939	-0.823	-0.823	0.000	0.000	0.000	0.000
47	A	55	LYS	1	0.899	0.950	21.028	11.972	11.972	0.000	0.000	0.000	0.000
48	A	56	CYS	0	-0.036	-0.007	17.275	-0.412	-0.412	0.000	0.000	0.000	0.000
49	A	57	LYS	1	0.912	0.957	15.463	18.894	18.894	0.000	0.000	0.000	0.000
50	A	58	ASN	0	-0.005	-0.017	18.337	0.691	0.691	0.000	0.000	0.000	0.000
51	A	59	PRO	0	0.056	0.038	20.172	-0.718	-0.718	0.000	0.000	0.000	0.000
52	A	60	ASN	0	-0.051	-0.035	20.823	0.478	0.478	0.000	0.000	0.000	0.000
53	A	61	PRO	0	-0.013	0.017	15.571	0.179	0.179	0.000	0.000	0.000	0.000
54	A	62	GLU	-1	-0.804	-0.891	14.569	-21.525	-21.525	0.000	0.000	0.000	0.000
55	A	63	PRO	0	-0.008	-0.014	18.168	0.786	0.786	0.000	0.000	0.000	0.000
56	A	64	SER	0	-0.058	-0.029	20.566	0.600	0.600	0.000	0.000	0.000	0.000
57	A	65	GLY	0	0.017	0.012	21.215	0.336	0.336	0.000	0.000	0.000	0.000
58	A	66	CYS	0	-0.033	-0.038	17.057	0.508	0.508	0.000	0.000	0.000	0.000
59	A	67	ARG	1	0.851	0.925	10.526	24.681	24.681	0.000	0.000	0.000	0.000
60	A	68	GLY	0	-0.017	-0.021	13.425	-0.693	-0.693	0.000	0.000	0.000	0.000
61	A	69	ILE	0	-0.026	-0.006	14.242	0.427	0.427	0.000	0.000	0.000	0.000
62	A	70	ASP	-1	-0.764	-0.842	17.907	-14.174	-14.174	0.000	0.000	0.000	0.000
63	A	71	SER	0	0.025	-0.003	20.383	0.757	0.757	0.000	0.000	0.000	0.000
64	A	72	SER	0	-0.093	-0.067	22.851	0.855	0.855	0.000	0.000	0.000	0.000
65	A	73	HIS	0	-0.077	-0.050	24.391	1.124	1.124	0.000	0.000	0.000	0.000
66	A	74	TRP	0	-0.016	-0.022	22.577	0.678	0.678	0.000	0.000	0.000	0.000
67	A	75	ASN	0	-0.023	-0.021	24.406	-0.013	-0.013	0.000	0.000	0.000	0.000
68	A	76	SER	0	-0.007	-0.013	21.180	-0.380	-0.380	0.000	0.000	0.000	0.000
69	A	77	TYR	0	0.028	0.021	22.442	0.212	0.212	0.000	0.000	0.000	0.000
70	A	79	THR	0	0.023	0.007	21.418	0.739	0.739	0.000	0.000	0.000	0.000
71	A	80	GLU	-1	-0.820	-0.903	22.186	-14.069	-14.069	0.000	0.000	0.000	0.000
72	A	81	THR	0	-0.034	-0.010	22.179	0.425	0.425	0.000	0.000	0.000	0.000
73	A	82	ASP	-1	-0.831	-0.918	24.347	-11.342	-11.342	0.000	0.000	0.000	0.000
74	A	83	THR	0	-0.029	-0.015	24.918	-0.015	-0.015	0.000	0.000	0.000	0.000
75	A	84	PHE	0	0.022	-0.011	26.912	0.409	0.409	0.000	0.000	0.000	0.000
76	A	85	ILE	0	0.034	0.028	26.935	0.019	0.019	0.000	0.000	0.000	0.000
77	A	86	LYS	1	0.873	0.954	31.010	8.982	8.982	0.000	0.000	0.000	0.000
78	A	87	ALA	0	0.022	0.013	34.331	-0.132	-0.132	0.000	0.000	0.000	0.000
79	A	88	LEU	0	-0.019	-0.020	36.251	0.232	0.232	0.000	0.000	0.000	0.000
80	A	89	THR	0	-0.055	-0.035	38.612	-0.068	-0.068	0.000	0.000	0.000	0.000
81	A	90	MET	0	0.001	-0.008	41.260	0.224	0.224	0.000	0.000	0.000	0.000
82	A	91	GLU	-1	-0.803	-0.879	44.236	-7.268	-7.268	0.000	0.000	0.000	0.000
83	A	92	GLY	0	0.014	0.011	46.240	0.147	0.147	0.000	0.000	0.000	0.000
84	A	93	ASN	0	-0.010	-0.018	49.146	-0.068	-0.068	0.000	0.000	0.000	0.000
85	A	94	GLN	0	0.009	0.006	49.264	-0.036	-0.036	0.000	0.000	0.000	0.000
86	A	95	ALA	0	0.011	0.006	45.979	-0.163	-0.163	0.000	0.000	0.000	0.000
87	A	96	SER	0	-0.001	-0.005	44.176	0.051	0.051	0.000	0.000	0.000	0.000
88	A	97	TRP	0	0.019	0.020	37.663	-0.213	-0.213	0.000	0.000	0.000	0.000
89	A	98	ARG	1	0.726	0.837	38.815	7.605	7.605	0.000	0.000	0.000	0.000
90	A	99	PHE	0	-0.003	0.007	33.146	-0.111	-0.111	0.000	0.000	0.000	0.000
91	A	100	ILE	0	-0.008	-0.013	33.053	0.211	0.211	0.000	0.000	0.000	0.000
92	A	101	ARG	1	0.870	0.944	30.564	9.590	9.590	0.000	0.000	0.000	0.000
93	A	102	ILE	0	-0.032	-0.009	26.083	0.179	0.179	0.000	0.000	0.000	0.000
94	A	103	GLU	-1	-0.780	-0.861	24.434	-12.083	-12.083	0.000	0.000	0.000	0.000
95	A	104	THR	0	-0.018	-0.022	21.687	-0.031	-0.031	0.000	0.000	0.000	0.000
96	A	105	ALA	0	-0.005	-0.005	18.311	-0.850	-0.850	0.000	0.000	0.000	0.000
97	A	107	VAL	0	-0.011	-0.010	17.468	-1.167	-1.167	0.000	0.000	0.000	0.000
98	A	109	VAL	0	-0.014	0.003	19.669	0.216	0.216	0.000	0.000	0.000	0.000
99	A	110	ILE	0	0.038	0.001	21.462	-0.035	-0.035	0.000	0.000	0.000	0.000
100	A	111	THR	0	-0.029	-0.018	24.370	0.612	0.612	0.000	0.000	0.000	0.000
101	A	112	LYS	1	0.903	0.956	26.738	11.759	11.759	0.000	0.000	0.000	0.000
102	A	113	LYS	1	0.816	0.920	27.073	11.878	11.878	0.000	0.000	0.000	0.000
103	A	114	LYS	1	0.917	0.936	30.053	9.257	9.257	0.000	0.000	0.000	0.000
104	A	115	GLY	0	0.010	0.006	33.015	0.350	0.350	0.000	0.000	0.000	0.000
105	A	116	ASN	-1	-0.782	-0.838	30.320	-10.676	-10.676	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:GLY)