FMO DATABASE

FMODB ID: N6MKQ

Calculation Name: 2AG4-A-Xray549

Preferred Name:

Target Type:

Ligand Name: (7r)-4,7-dihydroxy-n,n,n-trimethyl-10-oxo-3,5,9-trioxa-4-phosphaheptacosan-1-aminium 4-oxide | oleic acid | isopropyl alcohol

Ligand 3-letter code: LP3 | OLA | IPA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2AG4

Chain ID: A

ChEMBL ID:

UniProt ID: P17900

Base Structure: X-ray

Registration Date: 2025-10-11

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	160
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1469687.021137
FMO2-HF: Nuclear repulsion	1405957.224108
FMO2-HF: Total energy	-63729.79703
FMO2-MP2: Total energy	-63910.637185

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:HIS)

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

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.
-169.883	-162.597	15.561	-10.325	-12.521	-0.142

Interaction energy analysis for fragmet #1(A:1:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.755 / q_NPA : 0.877

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	-0.005	-0.002	3.842	-0.288	1.363	-0.007	-0.705	-0.939	-0.001
60	A	60	GLU	-1	-0.804	-0.895	1.844	-131.406	-126.460	11.816	-8.917	-7.845	-0.127
62	A	62	ALA	0	-0.006	-0.014	3.818	1.439	1.737	0.002	-0.101	-0.198	0.000
63	A	63	GLY	0	-0.019	-0.009	2.209	-9.295	-7.208	3.268	-2.806	-2.548	-0.011
64	A	64	LEU	0	-0.025	0.005	2.910	10.634	7.863	0.380	2.750	-0.360	-0.001
135	A	138	ASN	0	-0.038	-0.022	2.552	15.511	16.586	0.102	-0.546	-0.631	-0.002
4	A	4	SER	0	0.016	0.012	6.099	0.636	0.636	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.028	-0.017	9.915	-0.198	-0.198	0.000	0.000	0.000	0.000
6	A	6	SER	0	-0.045	-0.023	11.258	1.328	1.328	0.000	0.000	0.000	0.000
7	A	7	TRP	0	-0.047	-0.028	13.511	-0.264	-0.264	0.000	0.000	0.000	0.000
8	A	8	ASP	-1	-0.834	-0.905	16.208	-15.508	-15.508	0.000	0.000	0.000	0.000
9	A	9	ASN	0	-0.020	-0.026	18.383	0.144	0.144	0.000	0.000	0.000	0.000
10	A	10	CYS	0	-0.117	-0.039	20.415	-0.516	-0.516	0.000	0.000	0.000	0.000
11	A	11	ASP	-1	-0.794	-0.896	21.418	-12.328	-12.328	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.912	-0.956	24.327	-11.414	-11.414	0.000	0.000	0.000	0.000
13	A	13	GLY	0	-0.023	-0.004	26.049	0.377	0.377	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.781	0.875	27.043	11.576	11.576	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.831	-0.914	26.305	-11.232	-11.232	0.000	0.000	0.000	0.000
16	A	16	PRO	0	-0.026	-0.008	29.364	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	17	ALA	0	-0.023	-0.011	29.632	0.209	0.209	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.005	0.003	26.178	-0.427	-0.427	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.004	-0.006	22.457	0.409	0.409	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.863	0.927	24.764	10.717	10.717	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.018	-0.015	23.287	-0.115	-0.115	0.000	0.000	0.000	0.000
22	A	22	LEU	0	0.048	0.019	19.053	0.314	0.314	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.037	0.000	19.750	-0.346	-0.346	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.024	0.007	16.382	0.586	0.586	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.851	-0.887	17.578	-15.142	-15.142	0.000	0.000	0.000	0.000
26	A	26	PRO	0	0.017	0.000	16.470	0.842	0.842	0.000	0.000	0.000	0.000
27	A	27	ASP	-1	-0.801	-0.900	11.664	-27.358	-27.358	0.000	0.000	0.000	0.000
28	A	28	PRO	0	-0.043	-0.033	9.841	-0.119	-0.119	0.000	0.000	0.000	0.000
29	A	29	ILE	0	0.015	0.009	11.862	1.788	1.788	0.000	0.000	0.000	0.000
30	A	30	VAL	0	-0.026	-0.019	13.938	-1.281	-1.281	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.012	0.013	16.313	0.857	0.857	0.000	0.000	0.000	0.000
32	A	32	PRO	0	0.076	0.027	17.620	-0.746	-0.746	0.000	0.000	0.000	0.000
33	A	33	GLY	0	-0.010	-0.002	20.443	-0.301	-0.301	0.000	0.000	0.000	0.000
34	A	34	ASN	0	-0.045	-0.026	21.748	0.216	0.216	0.000	0.000	0.000	0.000
35	A	35	VAL	0	0.003	0.000	18.992	-0.744	-0.744	0.000	0.000	0.000	0.000
36	A	36	THR	0	-0.003	0.002	21.707	0.986	0.986	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.008	-0.006	21.764	-0.764	-0.764	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.061	-0.032	23.463	0.791	0.791	0.000	0.000	0.000	0.000
39	A	39	VAL	0	0.040	0.008	23.779	-0.624	-0.624	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.016	0.009	25.733	0.575	0.575	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.052	0.028	26.716	-0.475	-0.475	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.033	-0.005	28.624	0.387	0.387	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.015	-0.007	30.692	-0.335	-0.335	0.000	0.000	0.000	0.000
44	A	44	SER	0	0.006	0.003	33.189	0.248	0.248	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.004	-0.006	34.884	0.301	0.301	0.000	0.000	0.000	0.000
46	A	46	PRO	0	0.008	0.024	36.201	-0.218	-0.218	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.017	-0.007	31.846	-0.035	-0.035	0.000	0.000	0.000	0.000
48	A	48	SER	0	0.008	-0.018	35.778	0.144	0.144	0.000	0.000	0.000	0.000
49	A	49	SER	0	0.025	0.023	37.217	-0.259	-0.259	0.000	0.000	0.000	0.000
50	A	50	PRO	0	-0.011	0.003	36.725	0.206	0.206	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.002	-0.021	32.568	-0.073	-0.073	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.837	0.929	29.463	10.299	10.299	0.000	0.000	0.000	0.000
53	A	53	VAL	0	0.001	-0.003	25.055	-0.081	-0.081	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.831	-0.893	24.694	-11.618	-11.618	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.002	0.001	20.411	-0.434	-0.434	0.000	0.000	0.000	0.000
56	A	56	VAL	0	-0.051	-0.038	15.865	0.180	0.180	0.000	0.000	0.000	0.000
57	A	57	LEU	0	0.026	0.032	14.135	-0.707	-0.707	0.000	0.000	0.000	0.000
58	A	58	GLU	-1	-0.836	-0.902	10.726	-24.491	-24.491	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.884	0.966	8.397	30.545	30.545	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.008	-0.017	5.934	-0.235	-0.235	0.000	0.000	0.000	0.000
65	A	65	TRP	0	-0.001	0.000	4.936	-2.627	-2.627	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.008	-0.004	8.249	3.032	3.032	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.966	0.987	11.190	16.115	16.115	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.000	0.007	13.325	0.584	0.584	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.012	0.001	16.420	0.671	0.671	0.000	0.000	0.000	0.000
70	A	70	CYS	0	-0.109	-0.019	20.202	0.430	0.430	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.004	-0.010	22.278	0.562	0.562	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.878	-0.936	23.545	-12.454	-12.454	0.000	0.000	0.000	0.000
73	A	73	TYR	0	-0.039	-0.030	25.415	0.129	0.129	0.000	0.000	0.000	0.000
74	A	74	ILE	0	0.041	0.023	19.043	-0.417	-0.417	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.020	0.001	18.414	-0.087	-0.087	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.090	-0.056	18.032	-0.094	-0.094	0.000	0.000	0.000	0.000
77	A	78	THR	0	0.000	-0.019	23.869	-0.262	-0.262	0.000	0.000	0.000	0.000
78	A	79	PHE	0	-0.040	-0.019	24.341	0.314	0.314	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.872	-0.952	29.377	-9.718	-9.718	0.000	0.000	0.000	0.000
80	A	81	HIS	0	0.028	0.013	32.929	0.302	0.302	0.000	0.000	0.000	0.000
81	A	82	PHE	0	0.016	0.009	31.206	0.137	0.137	0.000	0.000	0.000	0.000
82	A	83	CYS	0	-0.043	0.016	33.611	-0.110	-0.110	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.783	-0.896	36.937	-8.069	-8.069	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.021	-0.015	33.983	0.138	0.138	0.000	0.000	0.000	0.000
85	A	86	LEU	0	-0.033	-0.011	33.812	0.040	0.040	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.928	-0.973	37.319	-7.788	-7.788	0.000	0.000	0.000	0.000
87	A	88	MET	0	-0.091	-0.037	39.065	0.218	0.218	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.048	-0.022	35.147	0.096	0.096	0.000	0.000	0.000	0.000
89	A	90	ILE	0	-0.033	-0.008	36.518	0.016	0.016	0.000	0.000	0.000	0.000
90	A	91	PRO	0	0.057	0.038	40.809	0.038	0.038	0.000	0.000	0.000	0.000
91	A	92	THR	0	0.016	-0.007	44.352	-0.104	-0.104	0.000	0.000	0.000	0.000
92	A	93	GLY	0	-0.034	-0.011	45.505	0.164	0.164	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.937	-0.961	43.914	-6.919	-6.919	0.000	0.000	0.000	0.000
94	A	95	PRO	0	-0.077	-0.042	41.991	-0.153	-0.153	0.000	0.000	0.000	0.000
95	A	96	CYS	0	-0.001	-0.004	35.648	-0.292	-0.292	0.000	0.000	0.000	0.000
96	A	97	PRO	0	0.041	0.017	34.155	0.139	0.139	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.804	-0.878	34.467	-8.739	-8.739	0.000	0.000	0.000	0.000
98	A	99	PRO	0	0.000	-0.004	29.864	-0.195	-0.195	0.000	0.000	0.000	0.000
99	A	100	LEU	0	-0.011	-0.020	31.358	0.114	0.114	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.917	0.970	34.615	7.971	7.971	0.000	0.000	0.000	0.000
101	A	102	THR	0	-0.031	-0.039	35.725	0.233	0.233	0.000	0.000	0.000	0.000
102	A	103	TYR	0	-0.042	-0.027	32.535	0.210	0.210	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.012	0.005	36.977	0.031	0.031	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.053	-0.020	32.512	0.060	0.060	0.000	0.000	0.000	0.000
105	A	106	PRO	0	-0.008	-0.007	36.169	0.074	0.074	0.000	0.000	0.000	0.000
106	A	108	HIS	1	0.898	0.943	36.690	8.042	8.042	0.000	0.000	0.000	0.000
107	A	110	PRO	0	-0.023	-0.008	38.836	0.192	0.192	0.000	0.000	0.000	0.000
108	A	111	PHE	0	0.015	0.000	34.717	0.119	0.119	0.000	0.000	0.000	0.000
109	A	112	LYS	1	0.950	0.975	37.095	7.334	7.334	0.000	0.000	0.000	0.000
110	A	113	GLU	-1	-0.870	-0.909	37.111	-8.003	-8.003	0.000	0.000	0.000	0.000
111	A	114	GLY	0	0.012	-0.001	36.473	0.222	0.222	0.000	0.000	0.000	0.000
112	A	115	THR	0	-0.053	-0.039	32.000	-0.353	-0.353	0.000	0.000	0.000	0.000
113	A	116	TYR	0	-0.032	-0.020	31.814	0.282	0.282	0.000	0.000	0.000	0.000
114	A	117	SER	0	-0.026	-0.039	30.492	-0.286	-0.286	0.000	0.000	0.000	0.000
115	A	118	LEU	0	0.014	0.025	27.654	0.360	0.360	0.000	0.000	0.000	0.000
116	A	119	PRO	0	0.012	0.002	28.488	-0.467	-0.467	0.000	0.000	0.000	0.000
117	A	120	LYS	1	0.832	0.900	23.567	13.286	13.286	0.000	0.000	0.000	0.000
118	A	121	SER	0	-0.005	-0.006	27.083	0.588	0.588	0.000	0.000	0.000	0.000
119	A	122	GLU	-1	-0.911	-0.943	25.629	-12.464	-12.464	0.000	0.000	0.000	0.000
120	A	123	PHE	0	-0.017	-0.015	24.430	0.515	0.515	0.000	0.000	0.000	0.000
121	A	124	VAL	0	0.013	0.009	24.507	-0.444	-0.444	0.000	0.000	0.000	0.000
122	A	125	VAL	0	-0.018	-0.010	19.846	0.091	0.091	0.000	0.000	0.000	0.000
123	A	126	PRO	0	-0.029	-0.032	23.091	-0.142	-0.142	0.000	0.000	0.000	0.000
124	A	127	ASP	-1	-0.907	-0.950	23.330	-13.916	-13.916	0.000	0.000	0.000	0.000
125	A	128	LEU	0	-0.046	-0.014	22.804	0.631	0.631	0.000	0.000	0.000	0.000
126	A	129	GLU	-1	-0.928	-0.973	22.820	-12.566	-12.566	0.000	0.000	0.000	0.000
127	A	130	LEU	0	0.003	0.008	17.500	-0.144	-0.144	0.000	0.000	0.000	0.000
128	A	131	PRO	0	0.017	0.001	18.286	0.054	0.054	0.000	0.000	0.000	0.000
129	A	132	SER	0	0.021	0.006	17.681	-0.983	-0.983	0.000	0.000	0.000	0.000
130	A	133	TRP	0	0.041	0.013	13.540	-1.309	-1.309	0.000	0.000	0.000	0.000
131	A	134	LEU	0	-0.028	0.007	12.814	-2.521	-2.521	0.000	0.000	0.000	0.000
132	A	135	THR	0	0.022	0.006	11.772	-0.137	-0.137	0.000	0.000	0.000	0.000
133	A	136	THR	0	0.038	0.007	8.024	-0.528	-0.528	0.000	0.000	0.000	0.000
134	A	137	GLY	0	-0.034	-0.007	5.991	-1.709	-1.709	0.000	0.000	0.000	0.000
136	A	139	TYR	0	-0.003	-0.029	6.227	0.271	0.271	0.000	0.000	0.000	0.000
137	A	140	ARG	1	0.830	0.887	8.848	28.466	28.466	0.000	0.000	0.000	0.000
138	A	141	ILE	0	0.005	-0.002	11.464	0.676	0.676	0.000	0.000	0.000	0.000
139	A	142	GLU	-1	-0.889	-0.923	15.257	-16.054	-16.054	0.000	0.000	0.000	0.000
140	A	143	SER	0	0.003	-0.005	17.898	0.466	0.466	0.000	0.000	0.000	0.000
141	A	144	VAL	0	0.023	-0.001	21.419	0.154	0.154	0.000	0.000	0.000	0.000
142	A	145	LEU	0	0.017	0.025	24.629	0.259	0.259	0.000	0.000	0.000	0.000
143	A	146	SER	0	0.008	-0.015	27.934	0.204	0.204	0.000	0.000	0.000	0.000
144	A	147	SER	0	0.043	0.018	31.146	0.150	0.150	0.000	0.000	0.000	0.000
145	A	148	SER	0	-0.026	-0.015	34.878	0.151	0.151	0.000	0.000	0.000	0.000
146	A	149	GLY	0	-0.009	0.000	33.683	0.176	0.176	0.000	0.000	0.000	0.000
147	A	150	LYS	1	0.910	0.961	33.416	7.900	7.900	0.000	0.000	0.000	0.000
148	A	151	ARG	1	0.913	0.950	23.887	12.111	12.111	0.000	0.000	0.000	0.000
149	A	152	LEU	0	-0.020	-0.011	30.055	0.304	0.304	0.000	0.000	0.000	0.000
150	A	153	GLY	0	0.064	0.029	27.417	0.122	0.122	0.000	0.000	0.000	0.000
151	A	155	ILE	0	0.011	0.015	20.035	0.039	0.039	0.000	0.000	0.000	0.000
152	A	156	LYS	1	0.881	0.922	14.798	17.881	17.881	0.000	0.000	0.000	0.000
153	A	157	ILE	0	0.011	0.003	14.412	0.403	0.403	0.000	0.000	0.000	0.000
154	A	158	ALA	0	-0.029	-0.010	9.215	-0.946	-0.946	0.000	0.000	0.000	0.000
155	A	159	ALA	0	0.048	0.018	10.506	1.387	1.387	0.000	0.000	0.000	0.000
156	A	160	SER	0	-0.007	0.000	6.780	-1.876	-1.876	0.000	0.000	0.000	0.000
157	A	161	LEU	0	0.006	0.015	9.141	3.193	3.193	0.000	0.000	0.000	0.000
158	A	162	LYS	1	0.818	0.897	9.792	18.229	18.229	0.000	0.000	0.000	0.000
159	A	163	GLY	0	0.047	0.028	12.185	1.500	1.500	0.000	0.000	0.000	0.000
160	A	164	ILE	-1	-0.930	-0.963	14.768	-17.435	-17.435	0.000	0.000	0.000	0.000

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