FMO DATABASE

FMODB ID: LZRG9

Calculation Name: 2COQ-A-Xray372

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: 2023-06-26

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

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. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-789879.868848
FMO2-HF: Nuclear repulsion	748000.956065
FMO2-HF: Total energy	-41878.912783
FMO2-MP2: Total energy	-41999.490438

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.
-41.461	-30.878	7.822	-8.976	-9.429	-0.021

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 : 0 / q_Mulliken : -0.022 / q_NPA : -0.019

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	0.001	0.018	3.780	-2.707	-0.773	-0.021	-1.026	-0.887	0.001
4	A	4	ASP	-1	-0.840	-0.895	5.920	-0.780	-0.780	0.000	0.000	0.000	0.000
5	A	5	GLN	0	0.012	-0.023	9.105	0.153	0.153	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.063	-0.013	12.032	-0.016	-0.016	0.000	0.000	0.000	0.000
7	A	7	PRO	0	0.091	0.054	15.440	0.009	0.009	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.914	0.953	16.190	-0.215	-0.215	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.006	-0.012	18.259	0.038	0.038	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.004	0.000	21.954	-0.023	-0.023	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.011	0.004	24.403	0.013	0.013	0.000	0.000	0.000	0.000
12	A	12	LYS	1	0.831	0.909	25.662	-0.040	-0.040	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.900	-0.940	29.564	0.035	0.035	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.039	-0.040	32.379	0.002	0.002	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.020	0.004	33.136	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.810	-0.870	29.569	0.023	0.023	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.006	-0.019	26.433	0.009	0.009	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.021	-0.005	21.405	-0.010	-0.010	0.000	0.000	0.000	0.000
19	A	19	THR	0	0.031	0.008	19.064	0.017	0.017	0.000	0.000	0.000	0.000
20	A	20	ILE	0	-0.052	-0.008	15.274	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	21	ASN	0	0.020	0.016	14.630	0.007	0.007	0.000	0.000	0.000	0.000
22	A	22	CYS	0	-0.011	0.017	9.833	0.016	0.016	0.000	0.000	0.000	0.000
23	A	23	VAL	0	0.051	0.024	8.558	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.007	0.006	2.614	0.027	0.544	0.434	-0.293	-0.658	-0.001
25	A	25	ARG	1	0.866	0.929	4.577	0.883	1.072	-0.001	-0.032	-0.156	0.000
26	A	26	ASP	-1	-0.831	-0.952	2.597	-20.894	-14.805	2.103	-4.059	-4.133	-0.050
27	A	27	THR	0	0.017	0.011	3.729	1.018	1.117	0.009	-0.013	-0.095	0.000
28	A	28	ALA	0	-0.037	-0.003	5.246	0.702	0.702	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.157	-0.079	4.605	0.450	0.546	-0.002	-0.006	-0.088	0.000
30	A	30	ALA	0	0.101	0.061	6.597	-0.368	-0.368	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.006	-0.029	7.768	0.337	0.337	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.861	-0.906	8.587	0.092	0.092	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.035	-0.020	11.147	-0.034	-0.034	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.008	-0.015	11.064	0.202	0.202	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.047	-0.004	12.892	-0.159	-0.159	0.000	0.000	0.000	0.000
36	A	36	TRP	0	0.027	-0.015	14.256	0.126	0.126	0.000	0.000	0.000	0.000
37	A	37	TYR	0	0.004	0.001	14.862	0.003	0.003	0.000	0.000	0.000	0.000
38	A	38	ARG	1	0.893	0.951	18.586	-0.225	-0.225	0.000	0.000	0.000	0.000
39	A	39	THR	0	0.020	0.012	21.506	0.019	0.019	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.859	0.931	23.250	-0.181	-0.181	0.000	0.000	0.000	0.000
41	A	41	LEU	0	0.039	0.006	26.204	0.012	0.012	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.016	0.017	27.795	-0.013	-0.013	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.027	0.001	27.650	0.002	0.002	0.000	0.000	0.000	0.000
44	A	44	THR	0	0.030	0.001	25.135	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.929	0.969	24.726	-0.213	-0.213	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.874	-0.929	17.938	0.626	0.626	0.000	0.000	0.000	0.000
47	A	47	GLN	0	-0.022	-0.013	22.484	-0.026	-0.026	0.000	0.000	0.000	0.000
48	A	48	THR	0	0.034	0.011	18.932	0.014	0.014	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.063	-0.032	20.375	-0.040	-0.040	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.020	0.016	21.240	0.019	0.019	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.030	-0.013	19.513	-0.020	-0.020	0.000	0.000	0.000	0.000
52	A	52	GLY	0	0.079	0.042	22.991	-0.011	-0.011	0.000	0.000	0.000	0.000
53	A	53	GLY	0	0.015	0.014	26.364	0.005	0.005	0.000	0.000	0.000	0.000
54	A	54	ARG	1	0.776	0.857	28.187	-0.119	-0.119	0.000	0.000	0.000	0.000
55	A	55	TYR	0	-0.011	-0.005	23.263	0.001	0.001	0.000	0.000	0.000	0.000
56	A	56	SER	0	0.007	-0.004	22.955	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	57	GLU	-1	-0.775	-0.886	15.394	0.269	0.269	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.040	-0.006	18.431	-0.019	-0.019	0.000	0.000	0.000	0.000
59	A	59	VAL	0	0.017	-0.001	15.041	0.015	0.015	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.833	-0.894	14.631	-0.373	-0.373	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.928	-0.969	13.485	-0.363	-0.363	0.000	0.000	0.000	0.000
62	A	62	GLY	0	-0.001	0.010	13.131	-0.107	-0.107	0.000	0.000	0.000	0.000
63	A	63	SER	0	-0.093	-0.073	12.691	-0.135	-0.135	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.048	-0.015	6.392	0.321	0.321	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.027	-0.024	8.747	0.019	0.019	0.000	0.000	0.000	0.000
66	A	66	ALA	0	0.083	0.051	11.282	0.038	0.038	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.033	-0.049	13.450	0.033	0.033	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.013	0.019	16.264	0.002	0.002	0.000	0.000	0.000	0.000
69	A	69	THR	0	-0.038	-0.033	18.672	-0.019	-0.019	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.034	-0.008	22.078	0.012	0.012	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.940	0.954	24.860	-0.073	-0.073	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.836	-0.919	28.392	0.077	0.077	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.030	0.004	26.214	0.009	0.009	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.905	0.949	30.345	-0.096	-0.096	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.058	0.027	30.849	0.009	0.009	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.870	-0.935	31.391	0.116	0.116	0.000	0.000	0.000	0.000
77	A	77	ASP	-1	-0.798	-0.881	26.809	0.148	0.148	0.000	0.000	0.000	0.000
78	A	78	SER	0	0.013	0.019	26.148	0.013	0.013	0.000	0.000	0.000	0.000
79	A	79	GLY	0	0.029	-0.001	24.735	0.006	0.006	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.067	-0.024	18.831	-0.013	-0.013	0.000	0.000	0.000	0.000
81	A	81	TYR	0	-0.020	-0.032	18.545	0.022	0.022	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.880	0.933	14.164	-0.791	-0.791	0.000	0.000	0.000	0.000
83	A	84	LYS	1	0.793	0.891	10.293	-0.727	-0.727	0.000	0.000	0.000	0.000
84	A	85	ALA	0	0.045	0.025	6.670	-0.297	-0.297	0.000	0.000	0.000	0.000
85	A	86	TYR	0	0.007	0.005	7.624	0.864	0.864	0.000	0.000	0.000	0.000
86	A	87	ARG	1	0.884	0.946	3.109	-3.775	-2.986	0.088	-0.281	-0.596	0.001
87	A	88	ARG	1	0.917	0.971	7.594	-0.018	-0.018	0.000	0.000	0.000	0.000
88	A	90	ALA	0	0.056	0.024	9.186	0.134	0.134	0.000	0.000	0.000	0.000
89	A	91	PHE	0	-0.007	0.000	7.843	0.098	0.098	0.000	0.000	0.000	0.000
90	A	92	ASN	0	0.020	-0.005	12.209	0.040	0.040	0.000	0.000	0.000	0.000
91	A	93	THR	0	0.001	0.011	11.752	0.030	0.030	0.000	0.000	0.000	0.000
92	A	94	GLY	0	0.025	0.021	10.363	-0.053	-0.053	0.000	0.000	0.000	0.000
93	A	95	VAL	0	-0.006	-0.017	8.304	0.074	0.074	0.000	0.000	0.000	0.000
94	A	96	GLY	0	-0.025	-0.014	6.531	0.802	0.802	0.000	0.000	0.000	0.000
95	A	97	TYR	0	0.019	-0.005	7.030	-0.313	-0.313	0.000	0.000	0.000	0.000
96	A	98	LYS	1	0.863	0.960	2.025	-16.345	-15.475	5.212	-3.266	-2.816	0.028
97	A	99	GLU	-1	-0.785	-0.875	6.235	0.216	0.216	0.000	0.000	0.000	0.000
98	A	100	GLY	0	0.036	0.030	8.348	0.097	0.097	0.000	0.000	0.000	0.000
99	A	101	ALA	0	-0.002	-0.019	10.334	0.006	0.006	0.000	0.000	0.000	0.000
100	A	102	GLY	0	-0.022	-0.004	12.780	-0.061	-0.061	0.000	0.000	0.000	0.000
101	A	103	THR	0	-0.026	-0.021	15.605	-0.046	-0.046	0.000	0.000	0.000	0.000
102	A	104	VAL	0	-0.009	-0.009	18.487	0.022	0.022	0.000	0.000	0.000	0.000
103	A	105	LEU	0	-0.023	0.003	22.100	-0.028	-0.028	0.000	0.000	0.000	0.000
104	A	106	THR	0	0.009	-0.004	24.515	0.012	0.012	0.000	0.000	0.000	0.000
105	A	107	VAL	0	-0.023	-0.006	28.272	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	108	LYS	1	0.957	0.980	30.733	-0.047	-0.047	0.000	0.000	0.000	0.000

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