FMO DATABASE

FMODB ID: RQJV8

Calculation Name: 2FTB-A-Xray547

Preferred Name:

Target Type:

Ligand Name: oleic acid

Ligand 3-letter code: OLA

Ligand of Interest (LOI):

PDB ID: 2FTB

Chain ID: A

ChEMBL ID:

UniProt ID: P81400

Base Structure: X-ray

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	125
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1027581.629777
FMO2-HF: Nuclear repulsion	979530.492231
FMO2-HF: Total energy	-48051.137545
FMO2-MP2: Total energy	-48191.840309

3D Structure

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:PRO)

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

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.
-42.349	-37.988	9.959	-7.447	-6.872	-0.083

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.807 / 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

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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	ASN	0	-0.007	0.021	3.461	9.832	14.072	-0.019	-1.932	-2.288	-0.008
4	A	4	GLY	0	0.042	0.031	5.372	-0.608	-0.525	-0.001	-0.009	-0.072	0.000
42	A	42	GLN	0	0.042	0.021	1.803	-36.640	-37.131	9.974	-5.352	-4.131	-0.075
102	A	102	VAL	0	-0.015	-0.001	3.537	1.357	1.663	0.006	-0.067	-0.246	0.000
124	A	124	ARG	1	0.795	0.887	4.119	47.329	47.552	-0.001	-0.087	-0.135	0.000
5	A	5	THR	0	-0.004	-0.011	8.951	0.398	0.398	0.000	0.000	0.000	0.000
6	A	6	TRP	0	-0.016	-0.015	5.830	-0.096	-0.096	0.000	0.000	0.000	0.000
7	A	7	GLN	0	-0.012	-0.006	12.431	1.337	1.337	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.018	-0.004	15.475	-0.430	-0.430	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.115	-0.103	14.873	1.388	1.388	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.035	-0.034	18.084	1.089	1.089	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.009	-0.014	18.461	-1.347	-1.347	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.764	-0.811	20.040	-14.184	-14.184	0.000	0.000	0.000	0.000
13	A	13	ASN	0	-0.020	-0.042	22.323	0.124	0.124	0.000	0.000	0.000	0.000
14	A	14	TYR	0	0.012	0.012	22.827	0.003	0.003	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.861	-0.938	24.522	-10.007	-10.007	0.000	0.000	0.000	0.000
16	A	16	ALA	0	-0.016	0.000	27.490	0.248	0.248	0.000	0.000	0.000	0.000
17	A	17	PHE	0	0.001	-0.007	21.358	0.027	0.027	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.004	-0.006	24.990	0.082	0.082	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.891	0.923	27.132	9.608	9.608	0.000	0.000	0.000	0.000
20	A	20	ALA	0	-0.034	-0.013	27.253	0.262	0.262	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.066	-0.032	24.474	-0.013	-0.013	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.007	0.012	27.764	0.098	0.098	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.050	-0.024	27.890	0.175	0.175	0.000	0.000	0.000	0.000
24	A	24	PRO	0	0.015	0.007	31.672	0.129	0.129	0.000	0.000	0.000	0.000
25	A	25	GLU	-1	-0.765	-0.889	33.966	-9.188	-9.188	0.000	0.000	0.000	0.000
26	A	26	ASP	-1	-0.918	-0.943	34.633	-8.318	-8.318	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.054	-0.031	30.631	-0.163	-0.163	0.000	0.000	0.000	0.000
28	A	28	ILE	0	-0.006	0.001	29.764	-0.409	-0.409	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.014	-0.020	30.222	-0.333	-0.333	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.007	0.011	30.480	-0.046	-0.046	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.008	-0.019	26.779	-0.291	-0.291	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.837	0.912	25.982	9.534	9.534	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.858	-0.909	25.840	-10.841	-10.841	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.070	-0.026	23.589	-0.255	-0.255	0.000	0.000	0.000	0.000
35	A	35	ASN	0	0.029	0.012	20.373	-0.373	-0.373	0.000	0.000	0.000	0.000
36	A	36	PRO	0	-0.046	-0.029	17.727	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	37	ILE	0	0.023	0.027	15.989	-0.510	-0.510	0.000	0.000	0.000	0.000
38	A	38	ILE	0	-0.038	-0.029	12.130	0.511	0.511	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.818	-0.896	11.695	-27.294	-27.294	0.000	0.000	0.000	0.000
40	A	40	ILE	0	-0.023	-0.011	6.587	0.491	0.491	0.000	0.000	0.000	0.000
41	A	41	GLN	0	-0.010	-0.006	7.988	-1.659	-1.659	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.050	-0.017	5.762	-2.784	-2.784	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.056	0.008	6.319	-1.073	-1.073	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.872	-0.933	6.195	-35.630	-35.630	0.000	0.000	0.000	0.000
46	A	46	ASN	0	-0.063	-0.018	8.662	2.806	2.806	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.037	0.001	4.869	-5.342	-5.342	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.009	0.014	9.242	3.178	3.178	0.000	0.000	0.000	0.000
49	A	49	VAL	0	0.010	0.003	9.791	-2.573	-2.573	0.000	0.000	0.000	0.000
50	A	50	THR	0	-0.010	0.001	12.131	2.495	2.495	0.000	0.000	0.000	0.000
51	A	51	SER	0	-0.002	0.016	15.199	-0.658	-0.658	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.904	0.933	17.210	17.053	17.053	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.047	0.023	20.088	-0.124	-0.124	0.000	0.000	0.000	0.000
54	A	54	PRO	0	0.041	0.010	23.331	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	55	ASN	0	-0.006	0.003	26.609	0.210	0.210	0.000	0.000	0.000	0.000
56	A	56	GLN	0	-0.007	0.000	23.834	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	57	SER	0	0.036	0.020	20.563	-0.705	-0.705	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.028	-0.002	19.526	0.520	0.520	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.009	-0.017	15.889	-0.577	-0.577	0.000	0.000	0.000	0.000
60	A	60	ASN	0	0.001	0.008	15.482	1.603	1.603	0.000	0.000	0.000	0.000
61	A	61	SER	0	0.002	-0.020	13.476	-1.070	-1.070	0.000	0.000	0.000	0.000
62	A	62	PHE	0	0.018	0.017	9.685	1.451	1.451	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.023	-0.025	11.918	-1.138	-1.138	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.009	0.000	7.165	1.180	1.180	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.014	-0.010	11.697	0.724	0.724	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.909	0.958	14.915	19.721	19.721	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.935	-0.964	16.743	-14.037	-14.037	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.008	-0.004	16.976	-0.031	-0.031	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.905	-0.952	18.992	-11.911	-11.911	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.013	-0.004	16.473	-0.489	-0.489	0.000	0.000	0.000	0.000
71	A	71	THR	0	-0.006	-0.012	20.003	1.133	1.133	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.015	-0.019	20.333	-0.745	-0.745	0.000	0.000	0.000	0.000
73	A	73	MET	0	0.020	-0.001	20.514	0.063	0.063	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.068	0.035	23.091	0.272	0.272	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.048	-0.016	25.229	0.418	0.418	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.938	0.979	26.446	10.959	10.959	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.942	0.985	23.928	12.015	12.015	0.000	0.000	0.000	0.000
78	A	78	ILE	0	0.001	-0.004	21.273	0.571	0.571	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.905	0.958	22.367	11.642	11.642	0.000	0.000	0.000	0.000
80	A	80	CYS	0	-0.018	-0.006	18.475	-0.108	-0.108	0.000	0.000	0.000	0.000
81	A	81	THR	0	0.053	0.032	16.184	-0.337	-0.337	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.023	0.005	10.900	0.152	0.152	0.000	0.000	0.000	0.000
83	A	83	VAL	0	0.004	-0.012	12.123	-0.051	-0.051	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.022	0.012	5.623	-1.522	-1.522	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.887	-0.943	9.494	-16.884	-16.884	0.000	0.000	0.000	0.000
86	A	86	GLY	0	0.011	-0.007	10.654	-0.377	-0.377	0.000	0.000	0.000	0.000
87	A	87	GLY	0	-0.010	0.004	6.243	-0.587	-0.587	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.860	0.930	5.683	16.402	16.402	0.000	0.000	0.000	0.000
89	A	89	LEU	0	0.004	0.011	6.460	0.760	0.760	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.007	-0.017	8.885	1.767	1.767	0.000	0.000	0.000	0.000
91	A	91	SER	0	0.018	0.015	12.681	0.368	0.368	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.942	0.954	15.709	16.823	16.823	0.000	0.000	0.000	0.000
93	A	93	THR	0	-0.029	0.000	19.325	0.206	0.206	0.000	0.000	0.000	0.000
94	A	94	ASP	-1	-0.843	-0.932	22.821	-11.330	-11.330	0.000	0.000	0.000	0.000
95	A	95	GLN	0	-0.044	-0.006	24.691	0.247	0.247	0.000	0.000	0.000	0.000
96	A	96	PHE	0	0.002	-0.003	17.696	0.146	0.146	0.000	0.000	0.000	0.000
97	A	97	SER	0	-0.020	-0.008	18.472	-0.264	-0.264	0.000	0.000	0.000	0.000
98	A	98	HIS	0	-0.051	-0.027	13.006	0.737	0.737	0.000	0.000	0.000	0.000
99	A	99	ILE	0	-0.021	-0.002	11.770	-0.690	-0.690	0.000	0.000	0.000	0.000
100	A	100	GLN	0	0.018	-0.010	7.620	1.337	1.337	0.000	0.000	0.000	0.000
101	A	101	GLU	-1	-0.876	-0.946	6.629	-28.815	-28.815	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.863	0.934	5.639	24.408	24.408	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.040	0.024	6.314	2.928	2.928	0.000	0.000	0.000	0.000
105	A	105	ASN	0	0.054	0.023	6.797	-6.926	-6.926	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.744	-0.815	9.467	-18.694	-18.694	0.000	0.000	0.000	0.000
107	A	107	MET	0	-0.008	0.014	7.772	-4.978	-4.978	0.000	0.000	0.000	0.000
108	A	108	VAL	0	-0.027	-0.009	9.303	2.431	2.431	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.764	-0.854	10.582	-24.043	-24.043	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.053	-0.033	12.853	1.411	1.411	0.000	0.000	0.000	0.000
111	A	111	LEU	0	0.012	0.016	15.663	-0.622	-0.622	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.005	0.004	18.335	0.778	0.778	0.000	0.000	0.000	0.000
113	A	113	VAL	0	0.059	0.021	21.613	-0.239	-0.239	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.033	0.021	24.767	0.226	0.226	0.000	0.000	0.000	0.000
115	A	115	GLY	0	-0.029	-0.009	26.734	0.345	0.345	0.000	0.000	0.000	0.000
116	A	116	ALA	0	0.003	0.015	26.369	0.024	0.024	0.000	0.000	0.000	0.000
117	A	117	THR	0	-0.008	-0.030	20.374	-0.205	-0.205	0.000	0.000	0.000	0.000
118	A	118	LEU	0	-0.008	0.016	19.020	0.389	0.389	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.010	-0.008	16.466	-0.741	-0.741	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.848	0.904	14.115	19.790	19.790	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.820	0.879	13.988	15.068	15.068	0.000	0.000	0.000	0.000
122	A	122	SER	0	0.060	0.015	11.717	1.531	1.531	0.000	0.000	0.000	0.000
123	A	123	LYS	1	0.836	0.916	12.166	17.767	17.767	0.000	0.000	0.000	0.000
125	A	125	VAL	-1	-0.945	-0.961	10.925	-21.112	-21.112	0.000	0.000	0.000	0.000

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