FMO DATABASE

FMODB ID: 8G37Y

Calculation Name: 2COQ-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2COQ

Chain ID: A

ChEMBL ID:

UniProt ID: Q8JJ25

Base Structure: X-ray

Registration Date: 2025-10-03

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	106
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-788528.630795
FMO2-HF: Nuclear repulsion	746649.645404
FMO2-HF: Total energy	-41878.985391
FMO2-MP2: Total energy	-41999.480376

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:ALA)

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

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.
-73.894	-67.352	24.924	-17.965	-13.503	-0.212

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.720 / q_NPA : 0.842

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	VAL	0	0.034	0.015	3.438	-10.718	-8.674	0.000	-1.125	-0.919	-0.002
24	A	24	LEU	0	-0.017	-0.010	2.449	-9.199	-8.610	0.572	-0.425	-0.736	-0.006
25	A	25	ARG	1	0.879	0.937	4.009	37.351	37.941	-0.001	-0.255	-0.335	-0.001
26	A	26	ASP	-1	-0.764	-0.912	1.737	-163.055	-161.127	24.132	-15.768	-10.292	-0.200
27	A	27	THR	0	0.024	0.027	3.252	8.108	8.339	0.079	-0.031	-0.279	-0.002
29	A	29	CYS	0	-0.153	-0.078	4.164	0.536	0.680	-0.002	-0.033	-0.110	0.000
86	A	87	ARG	1	0.846	0.918	3.340	52.825	53.225	0.013	-0.092	-0.321	-0.001
96	A	98	LYS	1	0.893	0.952	2.791	58.633	59.249	0.131	-0.236	-0.511	0.000
4	A	4	ASP	-1	-0.857	-0.913	5.944	-32.818	-32.818	0.000	0.000	0.000	0.000
5	A	5	GLN	0	-0.002	-0.031	9.135	-0.616	-0.616	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.055	-0.006	12.199	1.411	1.411	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.103	0.053	15.555	-0.048	-0.048	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.919	0.954	16.477	17.250	17.250	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.016	-0.015	18.442	0.046	0.046	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.005	-0.002	22.057	-0.128	-0.128	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.014	0.015	24.490	0.067	0.067	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.834	0.911	25.930	11.486	11.486	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.887	-0.940	29.626	-8.975	-8.975	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.030	-0.033	32.204	-0.164	-0.164	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.003	0.006	33.223	0.235	0.235	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.829	-0.888	29.817	-10.802	-10.802	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.018	-0.022	26.629	-0.090	-0.090	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.025	-0.013	21.586	0.058	0.058	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.005	0.010	19.005	0.087	0.087	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.044	-0.008	15.424	-0.071	-0.071	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.037	0.024	14.444	0.099	0.099	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.022	-0.001	9.688	0.383	0.383	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.060	0.041	8.123	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	28	ALA	0	0.011	0.017	5.049	5.982	5.982	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.120	0.068	5.609	-5.301	-5.301	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.041	-0.029	7.669	-3.475	-3.475	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.833	-0.905	8.723	-20.479	-20.479	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.025	-0.018	10.914	3.011	3.011	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.029	-0.009	10.899	-3.857	-3.857	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.025	0.003	12.729	2.349	2.349	0.000	0.000	0.000	0.000
36	A	36	TRP	0	0.005	-0.020	13.991	-1.482	-1.482	0.000	0.000	0.000	0.000
37	A	37	TYR	0	0.004	0.001	14.491	1.211	1.211	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.905	0.955	18.354	11.975	11.975	0.000	0.000	0.000	0.000
39	A	39	THR	0	0.029	0.020	20.979	0.309	0.309	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.927	0.968	23.164	10.559	10.559	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.044	0.005	26.204	-0.112	-0.112	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.000	0.012	27.865	0.366	0.366	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.036	-0.005	27.348	0.262	0.262	0.000	0.000	0.000	0.000
44	A	44	THR	0	0.025	-0.002	25.220	-0.195	-0.195	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.911	0.960	24.783	10.678	10.678	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.893	-0.944	17.778	-17.414	-17.414	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.032	-0.024	22.049	0.670	0.670	0.000	0.000	0.000	0.000
48	A	48	THR	0	0.020	0.005	18.460	-0.161	-0.161	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.069	-0.029	19.927	0.826	0.826	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.003	0.005	20.777	-0.683	-0.683	0.000	0.000	0.000	0.000
51	A	51	ILE	0	0.004	0.001	19.172	0.361	0.361	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.074	0.033	22.839	0.269	0.269	0.000	0.000	0.000	0.000
53	A	53	GLY	0	-0.001	0.002	26.388	0.073	0.073	0.000	0.000	0.000	0.000
54	A	54	ARG	1	0.794	0.876	28.096	10.790	10.790	0.000	0.000	0.000	0.000
55	A	55	TYR	0	-0.016	-0.002	23.135	-0.167	-0.167	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.017	-0.017	22.854	0.479	0.479	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.797	-0.895	15.557	-20.083	-20.083	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.015	-0.002	18.236	0.986	0.986	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.005	-0.008	14.842	-0.998	-0.998	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.825	-0.891	14.205	-18.854	-18.854	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.934	-0.965	12.882	-21.184	-21.184	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.001	0.007	12.619	-1.414	-1.414	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.090	-0.075	12.033	-1.171	-1.171	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.040	-0.014	5.881	0.826	0.826	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.020	-0.019	8.331	-3.914	-3.914	0.000	0.000	0.000	0.000
66	A	66	ALA	0	0.055	0.036	10.853	1.736	1.736	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.020	-0.040	13.230	-1.406	-1.406	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.017	0.020	16.049	0.926	0.926	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.008	-0.021	18.540	0.049	0.049	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.018	-0.013	21.830	0.201	0.201	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.927	0.951	24.592	11.830	11.830	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.818	-0.911	28.218	-9.473	-9.473	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.024	-0.003	26.057	-0.036	-0.036	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.891	0.936	30.167	10.018	10.018	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.075	0.047	30.814	-0.319	-0.319	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.896	-0.950	31.194	-9.800	-9.800	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.824	-0.881	26.842	-11.493	-11.493	0.000	0.000	0.000	0.000
78	A	78	SER	0	0.023	0.021	26.202	-0.656	-0.656	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.017	-0.007	24.789	0.228	0.228	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.046	-0.008	18.784	-0.377	-0.377	0.000	0.000	0.000	0.000
81	A	81	TYR	0	-0.038	-0.044	18.548	0.023	0.023	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.887	0.940	14.118	19.987	19.987	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.838	0.912	10.034	19.728	19.728	0.000	0.000	0.000	0.000
84	A	85	ALA	0	0.037	0.016	6.357	1.673	1.673	0.000	0.000	0.000	0.000
85	A	86	TYR	0	0.002	-0.025	6.917	-4.425	-4.425	0.000	0.000	0.000	0.000
87	A	88	ARG	1	0.915	0.967	7.642	24.942	24.942	0.000	0.000	0.000	0.000
88	A	90	ALA	0	0.045	0.021	8.577	2.655	2.655	0.000	0.000	0.000	0.000
89	A	91	PHE	0	-0.012	0.007	8.107	1.566	1.566	0.000	0.000	0.000	0.000
90	A	92	ASN	0	0.033	-0.002	12.098	1.823	1.823	0.000	0.000	0.000	0.000
91	A	93	THR	0	-0.011	0.007	11.891	-1.841	-1.841	0.000	0.000	0.000	0.000
92	A	94	GLY	0	0.056	0.028	10.884	1.164	1.164	0.000	0.000	0.000	0.000
93	A	95	VAL	0	-0.002	0.000	7.952	-0.292	-0.292	0.000	0.000	0.000	0.000
94	A	96	GLY	0	0.007	0.002	7.186	-6.095	-6.095	0.000	0.000	0.000	0.000
95	A	97	TYR	0	0.014	0.007	7.882	1.697	1.697	0.000	0.000	0.000	0.000
97	A	99	GLU	-1	-0.773	-0.871	6.510	-21.087	-21.087	0.000	0.000	0.000	0.000
98	A	100	GLY	0	0.035	0.034	8.253	-3.155	-3.155	0.000	0.000	0.000	0.000
99	A	101	ALA	0	-0.054	-0.043	10.267	1.773	1.773	0.000	0.000	0.000	0.000
100	A	102	GLY	0	-0.005	0.004	13.050	1.670	1.670	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.028	-0.015	15.655	-0.301	-0.301	0.000	0.000	0.000	0.000
102	A	104	VAL	0	-0.034	-0.019	18.502	0.331	0.331	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.012	0.006	22.007	0.157	0.157	0.000	0.000	0.000	0.000
104	A	106	THR	0	-0.004	-0.015	24.449	0.240	0.240	0.000	0.000	0.000	0.000
105	A	107	VAL	0	-0.047	-0.024	28.258	-0.105	-0.105	0.000	0.000	0.000	0.000
106	A	108	LYS	0	0.074	0.046	30.659	-0.358	-0.358	0.000	0.000	0.000	0.000

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