FMO DATABASE

FMODB ID: RL498

Calculation Name: 2WC5-A-Xray547

Preferred Name:

Target Type:

Ligand Name: hexadeca-10,12-dien-1-ol

Ligand 3-letter code: BOM

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2WC5

Chain ID: A

ChEMBL ID:

UniProt ID: P34170

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	138
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1372887.534914
FMO2-HF: Nuclear repulsion	1313574.218431
FMO2-HF: Total energy	-59313.316483
FMO2-MP2: Total energy	-59477.454694

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:THR)

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

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.
-208.912	-198.307	5.889	-6.138	-10.356	-0.03

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.854 / q_NPA : 0.914

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	-0.893	-0.934	2.815	-36.393	-33.481	0.240	-1.316	-1.836	-0.002
4	A	4	VAL	0	-0.044	-0.006	2.601	1.364	3.803	1.337	-1.215	-2.561	0.007
5	A	5	MET	0	0.053	0.032	4.221	8.090	8.481	-0.001	-0.089	-0.301	0.000
84	A	85	VAL	0	-0.072	-0.038	2.448	-1.534	-0.808	0.951	-0.419	-1.258	-0.003
85	A	86	LEU	0	-0.074	-0.032	1.977	-19.761	-17.771	2.110	-1.678	-2.422	-0.020
86	A	87	ALA	0	0.042	0.026	3.618	5.653	5.788	0.014	-0.017	-0.132	0.000
124	A	127	ILE	0	-0.101	-0.075	2.360	-20.291	-18.267	1.238	-1.391	-1.870	-0.012
125	A	128	ALA	0	0.067	0.035	4.088	-0.338	-0.350	0.000	-0.013	0.024	0.000
6	A	6	SER	0	-0.003	0.002	6.068	7.397	7.397	0.000	0.000	0.000	0.000
7	A	7	HIS	0	-0.041	-0.033	7.015	6.466	6.466	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.014	0.003	7.439	2.593	2.593	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.004	-0.012	9.779	3.015	3.015	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.018	0.011	11.935	2.122	2.122	0.000	0.000	0.000	0.000
11	A	11	HIS	0	-0.048	-0.001	13.153	1.205	1.205	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.035	0.015	13.861	1.186	1.186	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.034	0.001	15.653	1.203	1.203	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.870	0.943	17.215	18.001	18.001	0.000	0.000	0.000	0.000
15	A	15	THR	0	-0.023	-0.007	19.425	0.757	0.757	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.001	-0.001	21.224	0.337	0.337	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.798	-0.879	22.808	-11.669	-11.669	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.940	-0.986	24.466	-12.204	-12.204	0.000	0.000	0.000	0.000
19	A	19	CYS	0	-0.036	0.012	22.117	0.157	0.157	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.741	0.871	25.491	12.080	12.080	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.930	-0.974	27.916	-9.576	-9.576	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.971	-0.996	28.235	-10.930	-10.930	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.075	-0.054	26.475	-0.018	-0.018	0.000	0.000	0.000	0.000
24	A	24	GLY	0	-0.003	0.003	28.446	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.013	-0.002	23.799	0.085	0.085	0.000	0.000	0.000	0.000
26	A	26	SER	0	0.003	0.001	28.337	-0.050	-0.050	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.027	-0.001	27.860	-0.396	-0.396	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.923	-0.963	27.854	-10.184	-10.184	0.000	0.000	0.000	0.000
29	A	29	ILE	0	-0.105	-0.038	25.190	-0.098	-0.098	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.001	-0.013	19.943	-0.616	-0.616	0.000	0.000	0.000	0.000
31	A	31	ASP	-1	-0.794	-0.853	23.808	-13.202	-13.202	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.881	-0.959	21.049	-14.362	-14.362	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.034	0.006	14.457	-0.581	-0.581	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.824	0.911	15.738	14.448	14.448	0.000	0.000	0.000	0.000
35	A	35	HIS	0	-0.034	-0.049	15.957	-1.369	-1.369	0.000	0.000	0.000	0.000
36	A	36	PHE	0	-0.002	0.023	12.997	0.232	0.232	0.000	0.000	0.000	0.000
37	A	37	TRP	0	-0.011	-0.038	9.618	-0.916	-0.916	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.035	0.025	14.348	-0.741	-0.741	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.877	-0.904	16.429	-18.148	-18.148	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.922	-0.963	17.369	-14.520	-14.520	0.000	0.000	0.000	0.000
41	A	41	PHE	0	-0.015	0.004	18.824	0.543	0.543	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.891	-0.943	19.529	-14.194	-14.194	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.040	-0.018	17.202	0.297	0.297	0.000	0.000	0.000	0.000
44	A	44	VAL	0	-0.009	-0.021	20.665	0.097	0.097	0.000	0.000	0.000	0.000
45	A	45	HIS	0	0.016	0.017	24.099	0.038	0.038	0.000	0.000	0.000	0.000
46	A	46	ARG	1	0.870	0.902	24.664	10.073	10.073	0.000	0.000	0.000	0.000
47	A	47	GLU	-1	-0.837	-0.925	26.180	-11.098	-11.098	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.032	0.016	19.836	-0.254	-0.254	0.000	0.000	0.000	0.000
49	A	49	GLY	0	0.007	0.010	21.807	-0.619	-0.619	0.000	0.000	0.000	0.000
50	A	50	CYS	0	-0.081	-0.041	22.702	-0.614	-0.614	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.029	0.020	22.709	-0.046	-0.046	0.000	0.000	0.000	0.000
52	A	52	ILE	0	0.023	0.007	17.343	-0.351	-0.351	0.000	0.000	0.000	0.000
53	A	53	ILE	0	0.012	0.020	19.669	-0.499	-0.499	0.000	0.000	0.000	0.000
54	A	55	MET	0	-0.012	-0.011	18.378	0.124	0.124	0.000	0.000	0.000	0.000
55	A	56	SER	0	-0.035	-0.031	17.940	-0.897	-0.897	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.029	-0.018	19.031	-0.417	-0.417	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.857	0.950	21.145	12.681	12.681	0.000	0.000	0.000	0.000
58	A	59	PHE	0	-0.017	-0.014	17.312	0.119	0.119	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.023	-0.004	18.918	-0.248	-0.248	0.000	0.000	0.000	0.000
60	A	61	LEU	0	0.007	-0.002	14.490	-0.263	-0.263	0.000	0.000	0.000	0.000
61	A	62	MET	0	-0.036	0.001	17.858	-0.649	-0.649	0.000	0.000	0.000	0.000
62	A	63	ASP	-1	-0.884	-0.952	20.682	-13.400	-13.400	0.000	0.000	0.000	0.000
63	A	64	ASP	-1	-0.921	-0.966	23.203	-11.161	-11.161	0.000	0.000	0.000	0.000
64	A	65	ASP	-1	-0.963	-0.962	25.720	-10.676	-10.676	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.051	-0.025	22.990	-0.142	-0.142	0.000	0.000	0.000	0.000
66	A	67	ARG	1	0.827	0.912	20.591	12.150	12.150	0.000	0.000	0.000	0.000
67	A	68	MET	0	-0.001	0.001	13.587	-0.668	-0.668	0.000	0.000	0.000	0.000
68	A	69	HIS	0	0.057	0.041	17.841	-0.647	-0.647	0.000	0.000	0.000	0.000
69	A	70	HIS	1	0.810	0.877	15.536	16.504	16.504	0.000	0.000	0.000	0.000
70	A	71	VAL	0	0.016	0.016	14.876	-1.247	-1.247	0.000	0.000	0.000	0.000
71	A	72	ASN	0	0.018	-0.001	15.804	-0.868	-0.868	0.000	0.000	0.000	0.000
72	A	73	MET	0	0.024	0.020	11.333	-1.326	-1.326	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.819	-0.891	11.226	-26.649	-26.649	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.952	-0.983	11.694	-18.511	-18.511	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.010	-0.015	12.390	-1.032	-1.032	0.000	0.000	0.000	0.000
76	A	77	ILE	0	-0.020	-0.008	6.546	-1.586	-1.586	0.000	0.000	0.000	0.000
77	A	78	LYS	1	0.755	0.841	8.625	21.535	21.535	0.000	0.000	0.000	0.000
78	A	79	SER	0	-0.064	-0.021	10.437	1.077	1.077	0.000	0.000	0.000	0.000
79	A	80	PHE	0	0.015	0.019	8.194	0.893	0.893	0.000	0.000	0.000	0.000
80	A	81	PRO	0	0.034	0.002	8.030	-0.961	-0.961	0.000	0.000	0.000	0.000
81	A	82	ASN	0	-0.031	-0.022	5.113	-1.387	-1.387	0.000	0.000	0.000	0.000
82	A	83	GLY	0	0.097	0.050	5.500	-5.939	-5.939	0.000	0.000	0.000	0.000
83	A	84	GLN	0	0.021	-0.002	6.048	-3.270	-3.270	0.000	0.000	0.000	0.000
87	A	88	GLU	-1	-0.901	-0.948	7.331	-23.288	-23.288	0.000	0.000	0.000	0.000
88	A	89	LYS	1	0.826	0.910	5.054	40.717	40.717	0.000	0.000	0.000	0.000
89	A	90	MET	0	0.034	0.023	5.739	1.101	1.101	0.000	0.000	0.000	0.000
90	A	91	VAL	0	0.054	0.026	7.488	3.302	3.302	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.930	0.958	10.520	25.132	25.132	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.051	-0.019	8.236	1.783	1.783	0.000	0.000	0.000	0.000
93	A	94	ILE	0	0.079	0.028	10.474	1.712	1.712	0.000	0.000	0.000	0.000
94	A	95	HIS	0	-0.047	-0.038	12.932	2.083	2.083	0.000	0.000	0.000	0.000
95	A	96	ASN	0	-0.099	-0.051	14.585	2.120	2.120	0.000	0.000	0.000	0.000
96	A	97	CYS	0	0.037	0.020	15.165	0.079	0.079	0.000	0.000	0.000	0.000
97	A	98	GLU	-1	-0.768	-0.876	17.074	-15.889	-15.889	0.000	0.000	0.000	0.000
98	A	99	LYS	1	0.917	0.963	18.149	17.139	17.139	0.000	0.000	0.000	0.000
99	A	100	GLN	0	-0.054	-0.022	18.700	0.134	0.134	0.000	0.000	0.000	0.000
100	A	101	PHE	0	-0.011	-0.008	19.747	0.612	0.612	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.846	-0.904	23.561	-11.950	-11.950	0.000	0.000	0.000	0.000
102	A	103	THR	0	-0.066	-0.035	25.104	0.269	0.269	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.848	-0.896	25.834	-10.496	-10.496	0.000	0.000	0.000	0.000
104	A	105	THR	0	0.020	-0.003	27.190	-0.291	-0.291	0.000	0.000	0.000	0.000
105	A	106	ASP	-1	-0.756	-0.809	28.987	-10.632	-10.632	0.000	0.000	0.000	0.000
106	A	107	ASP	-1	-0.750	-0.866	25.639	-11.808	-11.808	0.000	0.000	0.000	0.000
107	A	109	THR	0	-0.010	-0.041	24.222	-0.494	-0.494	0.000	0.000	0.000	0.000
108	A	110	ARG	1	0.748	0.841	22.288	12.253	12.253	0.000	0.000	0.000	0.000
109	A	111	VAL	0	0.008	0.004	19.138	-0.712	-0.712	0.000	0.000	0.000	0.000
110	A	112	VAL	0	0.003	0.002	19.367	-0.973	-0.973	0.000	0.000	0.000	0.000
111	A	113	LYS	1	0.831	0.915	19.974	11.183	11.183	0.000	0.000	0.000	0.000
112	A	114	VAL	0	-0.022	-0.015	16.354	-0.637	-0.637	0.000	0.000	0.000	0.000
113	A	115	ALA	0	0.011	0.010	15.496	-1.367	-1.367	0.000	0.000	0.000	0.000
114	A	116	ALA	0	0.025	0.014	15.417	-1.270	-1.270	0.000	0.000	0.000	0.000
115	A	118	PHE	0	0.024	-0.002	8.631	-1.636	-1.636	0.000	0.000	0.000	0.000
116	A	119	LYS	1	0.808	0.905	11.366	15.838	15.838	0.000	0.000	0.000	0.000
117	A	120	GLU	-1	-0.960	-0.974	12.172	-18.482	-18.482	0.000	0.000	0.000	0.000
118	A	121	ASP	-1	-0.865	-0.950	11.872	-22.574	-22.574	0.000	0.000	0.000	0.000
119	A	122	SER	0	-0.077	-0.069	7.989	-3.845	-3.845	0.000	0.000	0.000	0.000
120	A	123	ARG	1	0.823	0.886	7.442	16.545	16.545	0.000	0.000	0.000	0.000
121	A	124	LYS	1	0.906	0.979	9.634	20.357	20.357	0.000	0.000	0.000	0.000
122	A	125	GLU	-1	-0.923	-0.970	7.803	-28.557	-28.557	0.000	0.000	0.000	0.000
123	A	126	GLY	0	-0.021	0.003	5.201	-4.419	-4.419	0.000	0.000	0.000	0.000
126	A	129	PRO	0	-0.101	-0.037	7.173	-1.859	-1.859	0.000	0.000	0.000	0.000
127	A	130	GLU	-1	-0.854	-0.947	8.368	-20.660	-20.660	0.000	0.000	0.000	0.000
128	A	131	VAL	0	0.030	0.013	11.379	-0.977	-0.977	0.000	0.000	0.000	0.000
129	A	132	ALA	0	0.064	0.030	13.948	-0.221	-0.221	0.000	0.000	0.000	0.000
130	A	133	MET	0	-0.088	-0.019	7.938	-1.531	-1.531	0.000	0.000	0.000	0.000
131	A	134	VAL	0	0.000	-0.004	10.996	-0.715	-0.715	0.000	0.000	0.000	0.000
132	A	135	GLU	-1	-0.826	-0.905	12.531	-16.244	-16.244	0.000	0.000	0.000	0.000
133	A	136	ALA	0	0.015	0.009	12.366	0.643	0.643	0.000	0.000	0.000	0.000
134	A	137	VAL	0	-0.106	-0.057	10.218	0.014	0.014	0.000	0.000	0.000	0.000
135	A	138	ILE	0	0.006	0.002	13.397	0.735	0.735	0.000	0.000	0.000	0.000
136	A	139	GLU	-1	-0.961	-0.988	16.923	-14.753	-14.753	0.000	0.000	0.000	0.000
137	A	140	LYS	1	0.839	0.922	11.843	22.142	22.142	0.000	0.000	0.000	0.000
138	A	141	TYR	-1	-0.975	-0.962	17.240	-13.522	-13.522	0.000	0.000	0.000	0.000

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