FMO DATABASE

FMODB ID: 7K2LK

Calculation Name: 1VYF-A-Xray547

Preferred Name:

Target Type:

Ligand Name: oleic acid

Ligand 3-letter code: OLA

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1VYF

Chain ID: A

ChEMBL ID:

UniProt ID: P29498

Base Structure: X-ray

Registration Date: 2025-10-05

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	135
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1200817.235868
FMO2-HF: Nuclear repulsion	1147114.059873
FMO2-HF: Total energy	-53703.175995
FMO2-MP2: Total energy	-53856.162047

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:GLY)

Summations of interaction energy for fragment #1(A:-1: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.
-18.152	-16.825	0.011	-0.469	-0.869	-0.001

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.867 / q_NPA : 0.922

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	1	MET	0	-0.013	-0.002	3.823	-0.641	0.056	-0.003	-0.281	-0.413	0.000
4	A	2	SER	0	-0.009	-0.005	3.028	8.309	8.783	0.016	-0.179	-0.310	-0.001
5	A	3	SER	0	0.001	0.009	5.141	5.200	5.312	-0.001	-0.006	-0.106	0.000
7	A	5	LEU	0	-0.041	0.012	4.733	1.917	1.961	-0.001	-0.003	-0.040	0.000
6	A	4	PHE	0	0.068	0.013	8.591	3.693	3.693	0.000	0.000	0.000	0.000
8	A	6	GLY	0	0.035	0.033	9.278	0.869	0.869	0.000	0.000	0.000	0.000
9	A	7	LYS	1	0.921	0.953	12.401	17.507	17.507	0.000	0.000	0.000	0.000
10	A	8	TRP	0	0.002	-0.004	12.634	0.588	0.588	0.000	0.000	0.000	0.000
11	A	9	LYS	1	0.930	0.965	18.170	12.637	12.637	0.000	0.000	0.000	0.000
12	A	10	LEU	0	-0.071	-0.007	21.990	-0.074	-0.074	0.000	0.000	0.000	0.000
13	A	11	SER	0	-0.086	-0.056	24.396	0.269	0.269	0.000	0.000	0.000	0.000
14	A	12	GLU	-1	-0.824	-0.896	26.205	-11.184	-11.184	0.000	0.000	0.000	0.000
15	A	13	SER	0	-0.011	-0.026	27.098	-0.535	-0.535	0.000	0.000	0.000	0.000
16	A	14	HIS	0	0.016	0.017	29.571	0.257	0.257	0.000	0.000	0.000	0.000
17	A	15	ASN	0	0.004	-0.026	31.184	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	16	PHE	0	0.030	0.008	28.362	0.028	0.028	0.000	0.000	0.000	0.000
19	A	17	ASP	-1	-0.730	-0.871	32.161	-8.466	-8.466	0.000	0.000	0.000	0.000
20	A	18	ALA	0	0.038	0.025	35.522	0.151	0.151	0.000	0.000	0.000	0.000
21	A	19	VAL	0	-0.009	-0.004	30.014	0.102	0.102	0.000	0.000	0.000	0.000
22	A	20	MET	0	-0.021	0.027	32.252	0.185	0.185	0.000	0.000	0.000	0.000
23	A	21	SER	0	-0.042	-0.016	34.006	0.238	0.238	0.000	0.000	0.000	0.000
24	A	22	LYS	1	0.859	0.936	35.661	8.850	8.850	0.000	0.000	0.000	0.000
25	A	23	LEU	0	-0.043	-0.016	30.700	0.080	0.080	0.000	0.000	0.000	0.000
26	A	24	GLY	0	-0.046	-0.008	35.333	0.070	0.070	0.000	0.000	0.000	0.000
27	A	25	VAL	0	-0.032	-0.011	33.323	0.108	0.108	0.000	0.000	0.000	0.000
28	A	26	SER	0	0.019	0.007	36.740	0.122	0.122	0.000	0.000	0.000	0.000
29	A	27	TRP	0	0.073	0.023	38.540	-0.225	-0.225	0.000	0.000	0.000	0.000
30	A	28	ALA	0	0.042	0.017	39.850	-0.088	-0.088	0.000	0.000	0.000	0.000
31	A	29	THR	0	0.010	-0.003	33.880	-0.154	-0.154	0.000	0.000	0.000	0.000
32	A	30	ARG	1	0.843	0.898	34.736	7.963	7.963	0.000	0.000	0.000	0.000
33	A	31	GLN	0	-0.012	-0.007	35.635	-0.199	-0.199	0.000	0.000	0.000	0.000
34	A	32	ILE	0	0.021	0.030	32.591	-0.147	-0.147	0.000	0.000	0.000	0.000
35	A	33	GLY	0	-0.010	-0.004	31.278	-0.271	-0.271	0.000	0.000	0.000	0.000
36	A	34	ASN	0	-0.053	-0.047	31.308	-0.552	-0.552	0.000	0.000	0.000	0.000
37	A	35	THR	0	-0.045	-0.031	33.641	0.030	0.030	0.000	0.000	0.000	0.000
38	A	36	VAL	0	-0.046	-0.015	28.946	-0.141	-0.141	0.000	0.000	0.000	0.000
39	A	37	THR	0	0.005	-0.011	27.392	-0.105	-0.105	0.000	0.000	0.000	0.000
40	A	38	PRO	0	-0.060	-0.027	23.666	-0.127	-0.127	0.000	0.000	0.000	0.000
41	A	39	THR	0	0.009	0.005	20.174	-0.227	-0.227	0.000	0.000	0.000	0.000
42	A	40	VAL	0	-0.032	-0.019	16.579	0.379	0.379	0.000	0.000	0.000	0.000
43	A	41	THR	0	0.002	-0.007	14.497	-0.478	-0.478	0.000	0.000	0.000	0.000
44	A	42	PHE	0	0.004	-0.004	10.849	0.799	0.799	0.000	0.000	0.000	0.000
45	A	43	THR	0	-0.042	-0.049	9.250	-0.668	-0.668	0.000	0.000	0.000	0.000
46	A	44	MET	0	-0.007	-0.011	5.007	2.011	2.011	0.000	0.000	0.000	0.000
47	A	45	ASP	-1	-0.873	-0.902	6.621	-29.697	-29.697	0.000	0.000	0.000	0.000
48	A	46	GLY	0	-0.006	-0.001	7.512	2.660	2.660	0.000	0.000	0.000	0.000
49	A	47	ASP	-1	-0.938	-0.978	8.191	-26.196	-26.196	0.000	0.000	0.000	0.000
50	A	48	LYS	1	0.867	0.939	10.415	19.776	19.776	0.000	0.000	0.000	0.000
51	A	49	MET	0	0.027	0.027	8.975	-1.651	-1.651	0.000	0.000	0.000	0.000
52	A	50	THR	0	0.004	0.008	10.916	2.828	2.828	0.000	0.000	0.000	0.000
53	A	51	MET	0	-0.037	-0.009	12.954	-1.276	-1.276	0.000	0.000	0.000	0.000
54	A	52	LEU	0	0.024	0.022	15.623	1.124	1.124	0.000	0.000	0.000	0.000
55	A	53	THR	0	-0.032	-0.029	18.176	-0.343	-0.343	0.000	0.000	0.000	0.000
56	A	54	GLU	-1	-0.897	-0.958	20.897	-14.047	-14.047	0.000	0.000	0.000	0.000
57	A	55	SER	0	-0.038	-0.053	23.791	0.144	0.144	0.000	0.000	0.000	0.000
58	A	56	THR	0	0.029	0.006	27.354	0.013	0.013	0.000	0.000	0.000	0.000
59	A	57	PHE	0	-0.012	0.010	30.262	0.307	0.307	0.000	0.000	0.000	0.000
60	A	58	LYS	1	0.869	0.923	27.745	10.329	10.329	0.000	0.000	0.000	0.000
61	A	59	ASN	0	0.046	0.050	24.702	-0.380	-0.380	0.000	0.000	0.000	0.000
62	A	60	LEU	0	-0.023	-0.015	23.559	0.419	0.419	0.000	0.000	0.000	0.000
63	A	61	SER	0	0.019	0.000	18.726	-0.782	-0.782	0.000	0.000	0.000	0.000
64	A	62	CYS	0	-0.014	0.013	18.569	0.428	0.428	0.000	0.000	0.000	0.000
65	A	63	THR	0	0.046	0.011	14.446	-0.512	-0.512	0.000	0.000	0.000	0.000
66	A	64	PHE	0	-0.018	-0.011	13.195	0.846	0.846	0.000	0.000	0.000	0.000
67	A	65	LYS	1	0.882	0.932	13.469	16.863	16.863	0.000	0.000	0.000	0.000
68	A	66	PHE	0	-0.019	-0.028	9.423	0.465	0.465	0.000	0.000	0.000	0.000
69	A	67	GLY	0	0.060	0.039	14.773	0.068	0.068	0.000	0.000	0.000	0.000
70	A	68	GLU	-1	-0.908	-0.943	17.794	-15.985	-15.985	0.000	0.000	0.000	0.000
71	A	69	GLU	-1	-0.857	-0.930	19.485	-11.844	-11.844	0.000	0.000	0.000	0.000
72	A	70	PHE	0	-0.064	-0.034	19.171	-0.112	-0.112	0.000	0.000	0.000	0.000
73	A	71	ASP	-1	-0.889	-0.935	23.129	-11.011	-11.011	0.000	0.000	0.000	0.000
74	A	72	GLU	-1	-0.820	-0.891	23.033	-14.046	-14.046	0.000	0.000	0.000	0.000
75	A	73	LYS	1	0.916	0.968	25.405	10.283	10.283	0.000	0.000	0.000	0.000
76	A	74	THR	0	0.001	-0.024	26.432	-0.307	-0.307	0.000	0.000	0.000	0.000
77	A	75	SER	0	0.021	0.003	26.817	0.309	0.309	0.000	0.000	0.000	0.000
78	A	76	ASP	-1	-0.817	-0.886	28.409	-9.963	-9.963	0.000	0.000	0.000	0.000
79	A	77	GLY	0	-0.026	-0.009	30.753	0.356	0.356	0.000	0.000	0.000	0.000
80	A	78	ARG	1	0.809	0.887	29.887	10.390	10.390	0.000	0.000	0.000	0.000
81	A	79	ASN	0	-0.005	-0.009	30.072	-0.514	-0.514	0.000	0.000	0.000	0.000
82	A	80	VAL	0	-0.052	-0.029	26.354	0.324	0.324	0.000	0.000	0.000	0.000
83	A	81	LYS	1	0.888	0.950	26.999	10.783	10.783	0.000	0.000	0.000	0.000
84	A	82	SER	0	0.000	-0.041	22.181	0.255	0.255	0.000	0.000	0.000	0.000
85	A	83	VAL	0	0.051	0.038	19.940	-0.161	-0.161	0.000	0.000	0.000	0.000
86	A	84	VAL	0	-0.025	-0.009	15.284	0.168	0.168	0.000	0.000	0.000	0.000
87	A	85	GLU	-1	-0.854	-0.934	16.453	-17.692	-17.692	0.000	0.000	0.000	0.000
88	A	86	LYS	1	0.858	0.925	9.250	30.153	30.153	0.000	0.000	0.000	0.000
89	A	87	ASN	0	-0.010	-0.001	13.801	0.612	0.612	0.000	0.000	0.000	0.000
90	A	88	SER	0	0.023	0.004	12.546	0.114	0.114	0.000	0.000	0.000	0.000
91	A	89	GLU	-1	-0.789	-0.895	6.413	-45.022	-45.022	0.000	0.000	0.000	0.000
92	A	90	SER	0	-0.005	0.003	8.814	-2.701	-2.701	0.000	0.000	0.000	0.000
93	A	91	LYS	1	0.845	0.919	11.608	18.918	18.918	0.000	0.000	0.000	0.000
94	A	92	LEU	0	0.023	0.021	12.302	-0.812	-0.812	0.000	0.000	0.000	0.000
95	A	93	THR	0	0.003	-0.019	15.208	1.273	1.273	0.000	0.000	0.000	0.000
96	A	94	GLN	0	0.009	0.028	18.779	-0.727	-0.727	0.000	0.000	0.000	0.000
97	A	95	THR	0	-0.008	-0.001	20.138	0.729	0.729	0.000	0.000	0.000	0.000
98	A	96	GLN	0	-0.043	-0.028	23.532	0.136	0.136	0.000	0.000	0.000	0.000
99	A	97	VAL	0	-0.009	-0.008	25.932	0.348	0.348	0.000	0.000	0.000	0.000
100	A	98	ASP	-1	-0.736	-0.855	29.375	-9.508	-9.508	0.000	0.000	0.000	0.000
101	A	99	PRO	0	-0.021	-0.035	32.408	0.075	0.075	0.000	0.000	0.000	0.000
102	A	100	LYS	1	0.896	0.963	35.693	8.337	8.337	0.000	0.000	0.000	0.000
103	A	101	ASN	0	-0.011	-0.004	33.209	0.132	0.132	0.000	0.000	0.000	0.000
104	A	102	THR	0	0.020	0.019	28.340	-0.246	-0.246	0.000	0.000	0.000	0.000
105	A	103	THR	0	-0.030	-0.019	26.778	0.283	0.283	0.000	0.000	0.000	0.000
106	A	104	VAL	0	0.001	0.004	23.837	-0.365	-0.365	0.000	0.000	0.000	0.000
107	A	105	ILE	0	-0.017	-0.011	21.134	0.307	0.307	0.000	0.000	0.000	0.000
108	A	106	VAL	0	0.010	0.014	19.553	-0.757	-0.757	0.000	0.000	0.000	0.000
109	A	107	ARG	1	0.881	0.924	16.502	17.139	17.139	0.000	0.000	0.000	0.000
110	A	108	GLU	-1	-0.795	-0.894	16.016	-17.746	-17.746	0.000	0.000	0.000	0.000
111	A	109	VAL	0	-0.040	-0.017	12.413	1.025	1.025	0.000	0.000	0.000	0.000
112	A	110	ASP	-1	-0.912	-0.956	14.538	-18.540	-18.540	0.000	0.000	0.000	0.000
113	A	111	GLY	0	0.029	0.020	15.108	0.820	0.820	0.000	0.000	0.000	0.000
114	A	112	ASP	-1	-0.852	-0.905	14.450	-20.786	-20.786	0.000	0.000	0.000	0.000
115	A	113	THR	0	-0.033	-0.025	16.874	1.079	1.079	0.000	0.000	0.000	0.000
116	A	114	MET	0	-0.001	0.016	16.087	-1.126	-1.126	0.000	0.000	0.000	0.000
117	A	115	LYS	1	0.917	0.961	17.707	15.894	15.894	0.000	0.000	0.000	0.000
118	A	116	THR	0	-0.022	-0.015	20.082	-0.720	-0.720	0.000	0.000	0.000	0.000
119	A	117	THR	0	-0.039	-0.023	21.718	0.830	0.830	0.000	0.000	0.000	0.000
120	A	118	VAL	0	-0.004	-0.004	24.000	-0.330	-0.330	0.000	0.000	0.000	0.000
121	A	119	THR	0	-0.018	-0.011	26.411	0.425	0.425	0.000	0.000	0.000	0.000
122	A	120	VAL	0	0.042	0.010	28.985	-0.180	-0.180	0.000	0.000	0.000	0.000
123	A	121	GLY	0	0.010	0.003	31.863	0.382	0.382	0.000	0.000	0.000	0.000
124	A	122	ASP	-1	-0.839	-0.912	32.959	-8.827	-8.827	0.000	0.000	0.000	0.000
125	A	123	VAL	0	-0.038	-0.004	33.931	-0.059	-0.059	0.000	0.000	0.000	0.000
126	A	124	THR	0	0.036	0.011	28.945	-0.414	-0.414	0.000	0.000	0.000	0.000
127	A	125	ALA	0	-0.032	-0.003	29.460	0.357	0.357	0.000	0.000	0.000	0.000
128	A	126	ILE	0	0.004	0.007	25.245	-0.477	-0.477	0.000	0.000	0.000	0.000
129	A	127	ARG	1	0.893	0.951	24.885	12.161	12.161	0.000	0.000	0.000	0.000
130	A	128	ASN	0	0.025	0.008	22.617	-1.137	-1.137	0.000	0.000	0.000	0.000
131	A	129	TYR	0	0.013	-0.004	19.577	0.778	0.778	0.000	0.000	0.000	0.000
132	A	130	LYS	1	0.983	0.999	19.700	12.476	12.476	0.000	0.000	0.000	0.000
133	A	131	ARG	1	0.858	0.918	11.254	24.184	24.184	0.000	0.000	0.000	0.000
134	A	132	LEU	0	-0.103	-0.060	17.157	1.202	1.202	0.000	0.000	0.000	0.000
135	A	133	SER	-1	-0.930	-0.949	16.859	-18.537	-18.537	0.000	0.000	0.000	0.000

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