FMO DATABASE

FMODB ID: JV1K9

Calculation Name: 5CSD-D-Xray547

Preferred Name:

Target Type:

Ligand Name: arachidonic acid | glycerol

Ligand 3-letter code: ACD | GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5CSD

Chain ID: D

ChEMBL ID:

UniProt ID: A0A093

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	159
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1399821.305649
FMO2-HF: Nuclear repulsion	1341516.68072
FMO2-HF: Total energy	-58304.624929
FMO2-MP2: Total energy	-58478.345213

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:2:THR)

Summations of interaction energy for fragment #1(A:2: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.
-61.504	-58.941	0.187	-1.294	-1.456	-0.01

Interaction energy analysis for fragmet #1(A:2:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.866 / q_NPA : 0.919

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	4	VAL	0	0.065	0.033	2.967	-1.563	0.931	0.188	-1.293	-1.389	-0.010
4	A	5	LYS	1	0.959	0.983	5.290	27.471	27.540	-0.001	-0.001	-0.067	0.000
5	A	6	ARG	1	0.785	0.859	6.613	17.782	17.782	0.000	0.000	0.000	0.000
6	A	7	ASP	-1	-0.834	-0.901	5.974	-41.256	-41.256	0.000	0.000	0.000	0.000
7	A	8	ILE	0	0.059	0.029	8.046	1.808	1.808	0.000	0.000	0.000	0.000
8	A	9	SER	0	-0.029	-0.037	8.457	2.079	2.079	0.000	0.000	0.000	0.000
9	A	10	ALA	0	0.033	0.031	11.189	1.495	1.495	0.000	0.000	0.000	0.000
10	A	11	PHE	0	0.054	0.014	13.183	1.376	1.376	0.000	0.000	0.000	0.000
11	A	12	GLN	0	-0.021	-0.016	12.599	-0.569	-0.569	0.000	0.000	0.000	0.000
12	A	13	LYS	1	0.806	0.891	14.006	18.405	18.405	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.052	0.041	15.978	1.030	1.030	0.000	0.000	0.000	0.000
14	A	15	ILE	0	0.005	0.001	18.842	0.840	0.840	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.030	-0.014	17.349	0.359	0.359	0.000	0.000	0.000	0.000
16	A	17	ASP	-1	-0.803	-0.885	18.974	-15.442	-15.442	0.000	0.000	0.000	0.000
17	A	18	ILE	0	0.013	0.003	21.634	0.692	0.692	0.000	0.000	0.000	0.000
18	A	19	SER	0	-0.019	-0.019	23.508	0.545	0.545	0.000	0.000	0.000	0.000
19	A	20	LEU	0	-0.028	-0.024	21.733	0.535	0.535	0.000	0.000	0.000	0.000
20	A	21	ALA	0	-0.004	0.007	25.564	0.517	0.517	0.000	0.000	0.000	0.000
21	A	22	VAL	0	0.014	0.007	27.748	0.493	0.493	0.000	0.000	0.000	0.000
22	A	23	ASN	0	0.005	0.005	26.968	0.680	0.680	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.802	0.897	29.694	9.762	9.762	0.000	0.000	0.000	0.000
24	A	25	PHE	0	0.004	-0.006	31.411	0.354	0.354	0.000	0.000	0.000	0.000
25	A	26	ASN	0	0.032	0.009	33.377	0.420	0.420	0.000	0.000	0.000	0.000
26	A	27	VAL	0	0.001	0.002	33.353	0.292	0.292	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.819	-0.885	35.825	-8.549	-8.549	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.003	0.009	36.678	0.292	0.292	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.856	-0.916	37.995	-8.010	-8.010	0.000	0.000	0.000	0.000
30	A	31	ARG	1	0.899	0.943	38.460	8.090	8.090	0.000	0.000	0.000	0.000
31	A	32	TYR	0	-0.052	-0.025	41.872	0.159	0.159	0.000	0.000	0.000	0.000
32	A	33	VAL	0	0.009	0.000	43.737	0.043	0.043	0.000	0.000	0.000	0.000
33	A	34	GLY	0	0.037	0.022	47.264	0.171	0.171	0.000	0.000	0.000	0.000
34	A	35	GLY	0	-0.019	0.003	47.998	-0.072	-0.072	0.000	0.000	0.000	0.000
35	A	36	ASP	-1	-0.814	-0.881	44.654	-7.122	-7.122	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.073	0.027	42.895	-0.086	-0.086	0.000	0.000	0.000	0.000
37	A	38	SER	0	-0.052	-0.057	41.307	-0.191	-0.191	0.000	0.000	0.000	0.000
38	A	39	HIS	0	-0.015	-0.002	38.009	-0.206	-0.206	0.000	0.000	0.000	0.000
39	A	40	LEU	0	0.030	0.028	36.745	-0.284	-0.284	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.008	0.007	36.627	-0.227	-0.227	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.027	-0.003	34.961	-0.234	-0.234	0.000	0.000	0.000	0.000
42	A	43	ASP	0	-0.053	-0.065	32.408	-0.418	-0.418	0.000	0.000	0.000	0.000
43	A	44	GLY	0	0.073	0.042	31.774	-0.340	-0.340	0.000	0.000	0.000	0.000
44	A	45	ASN	0	-0.020	-0.023	32.372	-0.165	-0.165	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.023	-0.006	27.216	-0.323	-0.323	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.018	0.016	27.671	-0.485	-0.485	0.000	0.000	0.000	0.000
47	A	48	ILE	0	0.001	0.015	28.103	-0.388	-0.388	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.757	0.861	24.352	12.214	12.214	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.057	0.021	23.707	-0.391	-0.391	0.000	0.000	0.000	0.000
50	A	51	THR	0	-0.013	-0.021	23.451	-0.570	-0.570	0.000	0.000	0.000	0.000
51	A	52	LEU	0	-0.003	-0.004	24.967	-0.248	-0.248	0.000	0.000	0.000	0.000
52	A	53	ASP	-1	-0.813	-0.888	20.889	-13.670	-13.670	0.000	0.000	0.000	0.000
53	A	54	GLY	0	0.009	0.013	20.358	-0.855	-0.855	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.019	-0.010	20.822	-0.407	-0.407	0.000	0.000	0.000	0.000
55	A	56	GLN	0	-0.019	-0.018	21.375	-0.485	-0.485	0.000	0.000	0.000	0.000
56	A	57	SER	0	-0.071	-0.059	16.276	-0.692	-0.692	0.000	0.000	0.000	0.000
57	A	58	LEU	0	0.037	0.023	15.899	-1.303	-1.303	0.000	0.000	0.000	0.000
58	A	59	GLN	0	0.008	0.014	17.641	0.370	0.370	0.000	0.000	0.000	0.000
59	A	60	ASN	0	-0.031	-0.034	14.059	0.471	0.471	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.823	-0.891	12.035	-24.991	-24.991	0.000	0.000	0.000	0.000
61	A	62	PRO	0	-0.014	-0.002	11.882	1.332	1.332	0.000	0.000	0.000	0.000
62	A	63	PRO	0	0.058	0.036	15.171	-0.188	-0.188	0.000	0.000	0.000	0.000
63	A	64	LEU	0	-0.022	0.016	15.324	-1.288	-1.288	0.000	0.000	0.000	0.000
64	A	65	SER	0	-0.001	-0.029	15.164	1.262	1.262	0.000	0.000	0.000	0.000
65	A	66	SER	0	0.055	0.012	17.569	-0.156	-0.156	0.000	0.000	0.000	0.000
66	A	67	MET	0	-0.019	-0.012	17.129	0.331	0.331	0.000	0.000	0.000	0.000
67	A	68	GLU	-1	-0.812	-0.881	13.679	-21.658	-21.658	0.000	0.000	0.000	0.000
68	A	69	ALA	0	0.035	0.017	16.795	0.124	0.124	0.000	0.000	0.000	0.000
69	A	70	LEU	0	0.008	0.000	20.091	0.386	0.386	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.062	-0.029	17.496	0.338	0.338	0.000	0.000	0.000	0.000
71	A	72	LEU	0	-0.010	-0.009	16.652	-0.143	-0.143	0.000	0.000	0.000	0.000
72	A	73	VAL	0	0.001	0.011	20.410	0.474	0.474	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.033	0.026	23.858	0.441	0.441	0.000	0.000	0.000	0.000
74	A	75	PRO	0	0.013	-0.003	20.109	0.348	0.348	0.000	0.000	0.000	0.000
75	A	76	VAL	0	0.020	0.014	22.638	0.238	0.238	0.000	0.000	0.000	0.000
76	A	77	GLN	0	-0.014	0.002	24.992	0.255	0.255	0.000	0.000	0.000	0.000
77	A	78	ASP	-1	-0.902	-0.960	25.959	-11.142	-11.142	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.031	-0.011	24.039	0.289	0.289	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.010	0.003	27.205	0.439	0.439	0.000	0.000	0.000	0.000
80	A	81	ASN	0	-0.026	-0.020	30.366	0.551	0.551	0.000	0.000	0.000	0.000
81	A	82	GLN	0	0.026	0.034	26.403	0.108	0.108	0.000	0.000	0.000	0.000
82	A	83	ILE	0	0.006	0.002	28.628	0.272	0.272	0.000	0.000	0.000	0.000
83	A	84	LEU	0	-0.024	-0.013	32.445	0.341	0.341	0.000	0.000	0.000	0.000
84	A	85	LEU	0	-0.017	0.007	34.860	0.271	0.271	0.000	0.000	0.000	0.000
85	A	86	ALA	0	0.006	0.007	33.949	0.235	0.235	0.000	0.000	0.000	0.000
86	A	87	ILE	0	-0.025	-0.017	35.807	0.238	0.238	0.000	0.000	0.000	0.000
87	A	88	GLN	0	-0.068	-0.042	38.225	0.175	0.175	0.000	0.000	0.000	0.000
88	A	89	ASN	0	0.015	-0.014	37.941	0.387	0.387	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.043	-0.022	38.709	0.157	0.157	0.000	0.000	0.000	0.000
90	A	91	ILE	0	-0.040	-0.022	41.414	0.200	0.200	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.863	-0.919	44.098	-6.948	-6.948	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.751	0.866	43.294	7.417	7.417	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.907	0.943	46.006	6.462	6.462	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.875	-0.929	47.738	-5.923	-5.923	0.000	0.000	0.000	0.000
95	A	96	PRO	0	-0.005	0.003	47.794	0.058	0.058	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.004	0.007	43.411	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.028	-0.021	47.673	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.065	-0.038	50.578	0.109	0.109	0.000	0.000	0.000	0.000
99	A	100	ALA	0	-0.044	-0.005	48.866	0.083	0.083	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.010	0.008	50.366	-0.029	-0.029	0.000	0.000	0.000	0.000
101	A	102	PHE	0	-0.047	-0.048	43.594	-0.117	-0.117	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.052	0.038	45.610	-0.161	-0.161	0.000	0.000	0.000	0.000
103	A	104	GLY	0	0.078	0.033	45.769	-0.129	-0.129	0.000	0.000	0.000	0.000
104	A	105	LYS	1	0.887	0.941	43.047	6.821	6.821	0.000	0.000	0.000	0.000
105	A	106	VAL	0	0.014	0.006	41.146	-0.242	-0.242	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.775	-0.861	41.039	-7.095	-7.095	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.002	-0.011	41.454	-0.154	-0.154	0.000	0.000	0.000	0.000
108	A	109	ASN	0	-0.013	0.003	35.799	-0.303	-0.303	0.000	0.000	0.000	0.000
109	A	110	LEU	0	0.039	0.018	36.666	-0.283	-0.283	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.888	0.923	37.238	7.118	7.118	0.000	0.000	0.000	0.000
111	A	112	GLN	0	-0.010	0.000	34.808	-0.260	-0.260	0.000	0.000	0.000	0.000
112	A	113	GLN	0	-0.038	-0.029	32.762	-0.378	-0.378	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.928	-0.962	32.780	-8.426	-8.426	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.874	-0.925	33.873	-9.325	-9.325	0.000	0.000	0.000	0.000
115	A	116	ALA	0	-0.040	-0.028	29.335	-0.280	-0.280	0.000	0.000	0.000	0.000
116	A	117	ALA	0	0.033	0.007	29.128	-0.420	-0.420	0.000	0.000	0.000	0.000
117	A	118	GLN	0	-0.016	0.012	29.793	-0.256	-0.256	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.935	0.963	28.273	9.615	9.615	0.000	0.000	0.000	0.000
119	A	120	LEU	0	-0.028	-0.007	22.717	-0.435	-0.435	0.000	0.000	0.000	0.000
120	A	121	SER	0	-0.011	-0.022	25.376	-0.435	-0.435	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.931	-0.964	27.201	-10.244	-10.244	0.000	0.000	0.000	0.000
122	A	123	LEU	0	-0.021	0.021	20.825	-0.227	-0.227	0.000	0.000	0.000	0.000
123	A	124	VAL	0	0.024	0.017	21.984	-0.528	-0.528	0.000	0.000	0.000	0.000
124	A	125	SER	0	-0.073	-0.050	23.387	-0.181	-0.181	0.000	0.000	0.000	0.000
125	A	126	THR	0	-0.062	-0.048	22.757	-0.118	-0.118	0.000	0.000	0.000	0.000
126	A	127	LYS	1	0.776	0.882	18.014	15.452	15.452	0.000	0.000	0.000	0.000
127	A	128	VAL	0	-0.033	-0.006	19.955	-0.742	-0.742	0.000	0.000	0.000	0.000
128	A	129	PRO	0	-0.007	0.015	20.659	0.458	0.458	0.000	0.000	0.000	0.000
129	A	130	HIS	0	0.059	0.010	23.379	0.124	0.124	0.000	0.000	0.000	0.000
130	A	131	GLU	-1	-0.916	-0.969	24.898	-12.147	-12.147	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.041	-0.024	23.655	0.093	0.093	0.000	0.000	0.000	0.000
132	A	133	ALA	0	-0.001	0.012	26.369	0.062	0.062	0.000	0.000	0.000	0.000
133	A	134	ASP	-1	-0.815	-0.898	27.839	-9.387	-9.387	0.000	0.000	0.000	0.000
134	A	135	ILE	0	-0.013	-0.002	27.812	0.161	0.161	0.000	0.000	0.000	0.000
135	A	136	SER	0	0.006	0.000	25.416	0.096	0.096	0.000	0.000	0.000	0.000
136	A	137	ARG	1	0.869	0.938	27.698	9.704	9.704	0.000	0.000	0.000	0.000
137	A	138	GLN	0	0.032	0.011	30.930	0.076	0.076	0.000	0.000	0.000	0.000
138	A	139	LEU	0	-0.022	-0.010	27.790	0.205	0.205	0.000	0.000	0.000	0.000
139	A	140	SER	0	-0.020	-0.016	28.944	-0.041	-0.041	0.000	0.000	0.000	0.000
140	A	141	ASP	-1	-0.903	-0.960	30.980	-8.969	-8.969	0.000	0.000	0.000	0.000
141	A	142	GLY	0	-0.020	-0.009	34.269	0.269	0.269	0.000	0.000	0.000	0.000
142	A	143	ILE	0	0.011	0.007	29.342	0.193	0.193	0.000	0.000	0.000	0.000
143	A	144	ALA	0	-0.003	0.003	33.581	0.190	0.190	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.019	-0.016	35.624	0.243	0.243	0.000	0.000	0.000	0.000
145	A	146	GLY	0	-0.002	-0.003	37.029	0.246	0.246	0.000	0.000	0.000	0.000
146	A	147	ILE	0	0.007	-0.006	32.934	0.202	0.202	0.000	0.000	0.000	0.000
147	A	148	LYS	1	0.888	0.939	37.574	7.419	7.419	0.000	0.000	0.000	0.000
148	A	149	LYS	1	0.936	0.976	40.716	7.604	7.604	0.000	0.000	0.000	0.000
149	A	150	GLY	0	0.062	0.024	40.889	0.179	0.179	0.000	0.000	0.000	0.000
150	A	151	ILE	0	-0.040	-0.019	39.185	0.180	0.180	0.000	0.000	0.000	0.000
151	A	152	ASP	-1	-0.863	-0.933	43.053	-6.920	-6.920	0.000	0.000	0.000	0.000
152	A	153	ALA	0	-0.033	0.000	45.095	0.186	0.186	0.000	0.000	0.000	0.000
153	A	154	PHE	0	0.005	0.003	43.554	0.169	0.169	0.000	0.000	0.000	0.000
154	A	155	ALA	0	0.009	0.031	46.712	0.070	0.070	0.000	0.000	0.000	0.000
155	A	156	GLY	0	-0.015	-0.005	48.165	0.141	0.141	0.000	0.000	0.000	0.000
156	A	157	THR	0	-0.101	-0.072	48.470	0.099	0.099	0.000	0.000	0.000	0.000
157	A	158	GLY	0	-0.037	-0.022	50.267	-0.052	-0.052	0.000	0.000	0.000	0.000
158	A	159	PRO	0	-0.040	-0.015	50.770	0.087	0.087	0.000	0.000	0.000	0.000
159	A	160	ALA	-1	-0.934	-0.955	53.852	-5.751	-5.751	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:THR)