FMO DATABASE

FMODB ID: Y9K72

Calculation Name: 2FLJ-A-Other547

Preferred Name:

Target Type:

Ligand Name: oleic acid

Ligand 3-letter code: OLA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FLJ

Chain ID: A

ChEMBL ID:

UniProt ID: P41509

Base Structure: SolutionNMR

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	133
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1184394.518421
FMO2-HF: Nuclear repulsion	1132770.086203
FMO2-HF: Total energy	-51624.432218
FMO2-MP2: Total energy	-51777.410527

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:VAL)

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

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.
-189.843	-183.791	36.444	-19.95	-22.547	-0.213

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.771 / q_NPA : 0.861

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	GLU	-1	-0.825	-0.887	1.718	-112.972	-114.536	16.884	-8.543	-6.777	-0.101
4	A	4	PHE	0	-0.027	-0.021	2.031	6.497	7.338	2.945	-1.636	-2.150	-0.002
5	A	5	ALA	0	0.000	0.007	5.233	4.111	4.262	-0.001	-0.012	-0.138	0.000
43	A	43	LEU	0	-0.010	0.008	2.898	-0.096	0.573	0.221	-0.150	-0.741	-0.001
51	A	51	PHE	0	0.001	-0.001	2.703	-5.149	-4.132	0.689	-0.401	-1.305	-0.004
68	A	68	LEU	0	-0.011	-0.011	3.962	0.216	0.372	0.000	-0.018	-0.138	0.000
88	A	88	GLN	0	-0.032	-0.036	2.634	-12.508	-10.110	2.205	-1.635	-2.968	-0.018
91	A	91	PRO	0	-0.017	-0.005	3.157	-6.574	-5.752	0.015	-0.325	-0.513	-0.002
92	A	92	ASN	0	0.024	0.000	1.746	-45.034	-45.833	12.545	-6.581	-5.165	-0.081
93	A	93	LYS	1	0.927	0.983	3.661	33.875	34.258	0.014	-0.049	-0.348	-0.001
94	A	94	LEU	0	-0.027	-0.008	2.406	-5.753	-4.604	0.862	-0.340	-1.672	-0.001
95	A	95	VAL	0	0.016	0.005	4.765	3.154	3.178	-0.001	-0.007	-0.015	0.000
110	A	110	PHE	0	-0.045	-0.021	3.420	1.928	2.733	0.066	-0.253	-0.617	-0.002
6	A	6	GLY	0	-0.023	-0.009	6.587	1.412	1.412	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.044	-0.007	7.880	2.196	2.196	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.864	0.924	9.535	18.321	18.321	0.000	0.000	0.000	0.000
9	A	9	TYR	0	0.050	-0.002	7.036	-0.267	-0.267	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.945	0.983	12.373	13.955	13.955	0.000	0.000	0.000	0.000
11	A	11	LEU	0	-0.080	-0.028	15.918	-0.222	-0.222	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.874	-0.929	17.179	-13.934	-13.934	0.000	0.000	0.000	0.000
13	A	13	SER	0	0.009	0.000	18.379	0.734	0.734	0.000	0.000	0.000	0.000
14	A	14	GLN	0	0.038	0.009	18.382	-1.215	-1.215	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.054	-0.026	20.141	0.791	0.791	0.000	0.000	0.000	0.000
16	A	16	ASN	0	0.026	-0.007	21.197	-0.067	-0.067	0.000	0.000	0.000	0.000
17	A	17	PHE	0	0.057	0.022	19.391	-0.141	-0.141	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.793	-0.873	22.471	-9.718	-9.718	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.876	-0.948	25.761	-10.504	-10.504	0.000	0.000	0.000	0.000
20	A	20	TYR	0	0.014	0.000	19.455	0.082	0.082	0.000	0.000	0.000	0.000
21	A	21	MET	0	-0.018	0.024	23.417	0.273	0.273	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.952	0.967	24.627	9.226	9.226	0.000	0.000	0.000	0.000
23	A	23	ALA	0	-0.023	0.001	25.489	0.294	0.294	0.000	0.000	0.000	0.000
24	A	24	ILE	0	-0.065	-0.032	21.786	0.138	0.138	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.004	0.007	25.882	0.075	0.075	0.000	0.000	0.000	0.000
26	A	26	VAL	0	-0.022	-0.004	25.269	0.259	0.259	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.055	0.029	28.662	0.139	0.139	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.028	-0.037	31.172	-0.186	-0.186	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.036	-0.010	33.140	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.796	-0.915	28.950	-9.233	-9.233	0.000	0.000	0.000	0.000
31	A	31	ARG	1	0.827	0.876	27.624	9.116	9.116	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.932	0.963	27.695	8.354	8.354	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.001	0.003	28.822	-0.139	-0.139	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.008	-0.007	24.688	-0.260	-0.260	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.058	-0.031	23.735	-0.530	-0.530	0.000	0.000	0.000	0.000
36	A	36	ALA	0	-0.034	0.000	25.825	-0.077	-0.077	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.039	-0.006	22.325	-0.063	-0.063	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.010	-0.016	20.610	-0.132	-0.132	0.000	0.000	0.000	0.000
39	A	39	PRO	0	-0.025	-0.011	16.767	-0.071	-0.071	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.033	0.019	14.409	-0.403	-0.403	0.000	0.000	0.000	0.000
41	A	41	ILE	0	-0.030	-0.016	9.860	0.403	0.403	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.837	-0.910	9.636	-20.747	-20.747	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.916	-0.961	7.212	-20.959	-20.959	0.000	0.000	0.000	0.000
45	A	45	VAL	0	-0.017	-0.015	5.489	-2.042	-2.042	0.000	0.000	0.000	0.000
46	A	46	LEU	0	-0.005	-0.006	7.892	2.368	2.368	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.834	-0.904	11.108	-18.850	-18.850	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.010	0.006	11.825	0.113	0.113	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.938	-0.975	8.456	-26.746	-26.746	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.783	0.882	8.332	16.434	16.434	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.879	0.932	7.514	20.715	20.715	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.010	0.009	6.645	-2.388	-2.388	0.000	0.000	0.000	0.000
54	A	54	THR	0	0.000	0.006	10.026	2.374	2.374	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.011	-0.005	12.320	-0.963	-0.963	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.900	0.949	14.479	18.799	18.799	0.000	0.000	0.000	0.000
57	A	57	THR	0	-0.002	-0.032	18.032	0.126	0.126	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.012	0.000	21.453	0.105	0.105	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.002	0.010	24.817	0.314	0.314	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.958	0.982	21.580	12.124	12.124	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.026	0.037	19.467	-0.516	-0.516	0.000	0.000	0.000	0.000
62	A	62	THR	0	-0.003	-0.005	17.212	0.660	0.660	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.863	-0.933	14.689	-17.331	-17.331	0.000	0.000	0.000	0.000
64	A	64	PHE	0	0.025	0.025	10.376	0.786	0.786	0.000	0.000	0.000	0.000
65	A	65	THR	0	0.002	-0.011	11.673	-1.532	-1.532	0.000	0.000	0.000	0.000
66	A	66	PHE	0	-0.002	0.005	5.981	0.843	0.843	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.936	0.948	9.239	17.743	17.743	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.008	-0.010	8.158	0.993	0.993	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.919	-0.930	11.338	-16.419	-16.419	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.835	-0.908	13.191	-14.288	-14.288	0.000	0.000	0.000	0.000
72	A	72	PHE	0	-0.029	-0.017	11.793	0.244	0.244	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.828	-0.910	16.271	-12.585	-12.585	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.818	-0.876	15.012	-18.112	-18.112	0.000	0.000	0.000	0.000
75	A	75	ASP	-1	-0.917	-0.956	18.150	-11.620	-11.620	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.037	-0.046	19.149	-0.562	-0.562	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.019	-0.027	17.943	0.318	0.318	0.000	0.000	0.000	0.000
78	A	78	ASP	-1	-0.801	-0.848	21.585	-11.473	-11.473	0.000	0.000	0.000	0.000
79	A	79	GLY	0	-0.025	0.003	23.878	0.439	0.439	0.000	0.000	0.000	0.000
80	A	80	ARG	1	0.796	0.858	22.256	12.141	12.141	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.860	0.929	22.721	11.546	11.546	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.023	-0.012	18.820	0.422	0.422	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.866	0.932	19.272	12.359	12.359	0.000	0.000	0.000	0.000
84	A	84	SER	0	0.021	-0.031	14.525	0.417	0.417	0.000	0.000	0.000	0.000
85	A	85	ILE	0	0.011	0.010	12.059	-0.019	-0.019	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.000	0.012	6.643	-0.447	-0.447	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.010	0.001	7.470	-0.080	-0.080	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.911	-0.943	5.432	-25.126	-25.126	0.000	0.000	0.000	0.000
90	A	90	GLY	0	0.049	0.027	6.371	-2.101	-2.101	0.000	0.000	0.000	0.000
96	A	96	HIS	0	-0.039	-0.019	8.567	-1.530	-1.530	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.908	-0.950	10.819	-14.834	-14.834	0.000	0.000	0.000	0.000
98	A	98	GLN	0	-0.030	-0.020	14.564	0.387	0.387	0.000	0.000	0.000	0.000
99	A	99	LYS	1	0.888	0.931	17.190	14.976	14.976	0.000	0.000	0.000	0.000
100	A	100	GLY	0	0.006	-0.003	20.594	0.080	0.080	0.000	0.000	0.000	0.000
101	A	101	ASP	-1	-0.819	-0.893	24.162	-10.930	-10.930	0.000	0.000	0.000	0.000
102	A	102	HIS	1	0.830	0.903	23.316	11.119	11.119	0.000	0.000	0.000	0.000
103	A	103	PRO	0	0.002	0.016	21.127	-0.519	-0.519	0.000	0.000	0.000	0.000
104	A	104	THR	0	-0.017	-0.011	16.796	0.316	0.316	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.007	0.008	13.746	-0.559	-0.559	0.000	0.000	0.000	0.000
106	A	106	ILE	0	-0.013	-0.012	10.928	0.382	0.382	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.003	-0.001	8.641	-1.284	-1.284	0.000	0.000	0.000	0.000
108	A	108	ARG	1	0.874	0.921	6.097	25.710	25.710	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.814	-0.915	5.658	-30.686	-30.686	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.001	-0.009	5.676	-1.824	-1.824	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.909	0.941	7.047	35.920	35.920	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.836	-0.911	9.838	-22.012	-22.012	0.000	0.000	0.000	0.000
114	A	114	GLN	0	-0.015	-0.010	10.692	2.756	2.756	0.000	0.000	0.000	0.000
115	A	115	CYS	0	-0.045	-0.001	6.854	-2.412	-2.412	0.000	0.000	0.000	0.000
116	A	116	VAL	0	0.011	0.007	9.129	2.465	2.465	0.000	0.000	0.000	0.000
117	A	117	ILE	0	-0.010	-0.007	9.904	-1.554	-1.554	0.000	0.000	0.000	0.000
118	A	118	THR	0	-0.002	-0.002	11.785	1.849	1.849	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.005	-0.002	13.234	-0.847	-0.847	0.000	0.000	0.000	0.000
120	A	120	LYS	1	0.849	0.931	15.969	13.495	13.495	0.000	0.000	0.000	0.000
121	A	121	LEU	0	0.022	0.023	18.584	-0.220	-0.220	0.000	0.000	0.000	0.000
122	A	122	GLY	0	0.031	0.013	21.475	0.533	0.533	0.000	0.000	0.000	0.000
123	A	123	ASP	-1	-0.853	-0.944	22.991	-11.502	-11.502	0.000	0.000	0.000	0.000
124	A	124	LEU	0	-0.073	-0.010	22.804	-0.129	-0.129	0.000	0.000	0.000	0.000
125	A	125	VAL	0	0.029	0.008	18.516	-0.509	-0.509	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.000	0.010	18.945	0.603	0.603	0.000	0.000	0.000	0.000
127	A	127	THR	0	0.006	0.008	16.331	-0.628	-0.628	0.000	0.000	0.000	0.000
128	A	128	ARG	1	0.881	0.939	15.172	16.355	16.355	0.000	0.000	0.000	0.000
129	A	129	ILE	0	0.025	0.026	13.959	-1.433	-1.433	0.000	0.000	0.000	0.000
130	A	130	TYR	0	0.016	-0.002	12.108	1.333	1.333	0.000	0.000	0.000	0.000
131	A	131	LYS	1	0.879	0.926	12.884	13.991	13.991	0.000	0.000	0.000	0.000
132	A	132	ALA	0	-0.018	-0.010	12.010	0.203	0.203	0.000	0.000	0.000	0.000
133	A	133	GLN	-1	-0.958	-0.966	13.609	-16.673	-16.673	0.000	0.000	0.000	0.000

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