FMO DATABASE

FMODB ID: 5J69Z

Calculation Name: 3EOI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EOI

Chain ID: A

ChEMBL ID:

UniProt ID: Q68JC9

Base Structure: X-ray

Registration Date: 2023-09-23

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

DOI:

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	123
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-989878.209901
FMO2-HF: Nuclear repulsion	942060.303571
FMO2-HF: Total energy	-47817.906331
FMO2-MP2: Total energy	-47958.572052

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:2:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-4.616	-0.9	2.47	-1.877	-4.307	0.009

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.000 / q_NPA : -0.009

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	ARG	1	0.974	0.971	2.167	-4.616	-1.045	2.471	-1.868	-4.173	0.009
4	A	5	THR	0	-0.032	-0.001	5.057	0.099	0.244	-0.001	-0.009	-0.134	0.000
5	A	6	VAL	0	0.043	0.026	8.591	0.025	0.025	0.000	0.000	0.000	0.000
6	A	7	HIS	0	-0.002	-0.001	9.214	-0.017	-0.017	0.000	0.000	0.000	0.000
7	A	8	HIS	0	0.013	0.001	13.604	-0.019	-0.019	0.000	0.000	0.000	0.000
8	A	9	GLN	0	-0.008	-0.006	14.259	-0.009	-0.009	0.000	0.000	0.000	0.000
9	A	10	GLN	0	0.009	-0.007	18.749	0.000	0.000	0.000	0.000	0.000	0.000
10	A	11	THR	0	0.074	0.035	22.176	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.036	0.032	20.270	-0.002	-0.002	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.829	-0.909	20.054	0.032	0.032	0.000	0.000	0.000	0.000
13	A	14	ILE	0	-0.050	-0.033	22.688	0.000	0.000	0.000	0.000	0.000	0.000
14	A	15	THR	0	-0.006	-0.007	25.532	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	16	GLN	0	0.008	0.000	23.457	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	17	GLN	0	-0.074	-0.049	26.016	0.003	0.003	0.000	0.000	0.000	0.000
17	A	18	ALA	0	0.014	0.000	27.646	0.000	0.000	0.000	0.000	0.000	0.000
18	A	19	ALA	0	0.086	0.052	28.901	0.000	0.000	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.813	-0.888	26.870	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	21	PHE	0	-0.024	-0.016	30.410	0.000	0.000	0.000	0.000	0.000	0.000
21	A	22	ILE	0	0.006	0.005	33.115	0.000	0.000	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.847	0.924	29.060	0.002	0.002	0.000	0.000	0.000	0.000
23	A	24	TYR	0	-0.018	-0.053	30.688	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	25	MET	0	-0.022	0.003	35.813	0.001	0.001	0.000	0.000	0.000	0.000
25	A	26	ASN	0	0.026	0.006	38.398	0.001	0.001	0.000	0.000	0.000	0.000
26	A	27	ALA	0	0.036	0.031	38.202	0.000	0.000	0.000	0.000	0.000	0.000
27	A	28	ILE	0	-0.027	-0.030	37.925	0.000	0.000	0.000	0.000	0.000	0.000
28	A	29	ASN	0	-0.058	-0.033	41.549	0.001	0.001	0.000	0.000	0.000	0.000
29	A	30	ASP	-1	-0.850	-0.926	43.420	0.001	0.001	0.000	0.000	0.000	0.000
30	A	31	TYR	0	-0.002	0.001	43.781	0.000	0.000	0.000	0.000	0.000	0.000
31	A	32	LEU	0	-0.043	-0.056	45.119	0.000	0.000	0.000	0.000	0.000	0.000
32	A	33	TYR	0	-0.044	-0.009	47.655	0.000	0.000	0.000	0.000	0.000	0.000
33	A	34	GLN	0	-0.012	-0.006	46.316	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	HIS	1	0.801	0.914	48.833	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.061	0.035	50.707	0.001	0.001	0.000	0.000	0.000	0.000
36	A	37	GLU	-1	-0.801	-0.902	52.431	0.004	0.004	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.797	0.889	44.647	-0.006	-0.006	0.000	0.000	0.000	0.000
38	A	39	ARG	1	0.852	0.907	48.200	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	40	ALA	0	0.009	0.002	50.172	0.001	0.001	0.000	0.000	0.000	0.000
40	A	41	ALA	0	-0.013	0.002	49.454	0.000	0.000	0.000	0.000	0.000	0.000
41	A	42	GLY	0	-0.008	0.018	47.354	0.000	0.000	0.000	0.000	0.000	0.000
42	A	43	GLY	0	0.028	0.026	43.520	-0.001	-0.001	0.000	0.000	0.000	0.000
43	A	44	GLN	0	0.007	-0.025	38.459	0.000	0.000	0.000	0.000	0.000	0.000
44	A	45	LEU	0	-0.025	-0.004	40.872	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	46	THR	0	-0.001	-0.027	39.234	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	SER	0	0.022	-0.012	34.522	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	ALA	0	-0.015	-0.007	37.054	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	49	GLN	0	-0.016	0.004	39.764	0.000	0.000	0.000	0.000	0.000	0.000
49	A	50	LEU	0	-0.008	-0.005	37.070	0.000	0.000	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.029	0.033	37.787	0.000	0.000	0.000	0.000	0.000	0.000
51	A	52	LEU	0	-0.034	-0.002	32.948	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	53	PRO	0	0.016	0.021	29.607	0.001	0.001	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.040	0.022	29.699	0.001	0.001	0.000	0.000	0.000	0.000
54	A	55	THR	0	0.022	0.017	28.057	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.929	0.958	24.131	-0.025	-0.025	0.000	0.000	0.000	0.000
56	A	57	ASN	0	-0.075	-0.054	25.711	0.003	0.003	0.000	0.000	0.000	0.000
57	A	58	VAL	0	0.049	0.054	27.907	0.001	0.001	0.000	0.000	0.000	0.000
58	A	59	SER	0	-0.042	-0.005	31.675	0.000	0.000	0.000	0.000	0.000	0.000
59	A	60	HIS	0	0.054	0.021	34.479	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	LEU	0	0.003	0.015	38.179	0.001	0.001	0.000	0.000	0.000	0.000
61	A	62	ILE	0	-0.015	0.014	41.417	0.000	0.000	0.000	0.000	0.000	0.000
62	A	63	SER	0	-0.008	-0.012	45.028	0.000	0.000	0.000	0.000	0.000	0.000
63	A	64	GLN	0	0.029	0.003	47.423	0.000	0.000	0.000	0.000	0.000	0.000
64	A	65	GLN	0	-0.013	-0.006	50.408	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	66	ARG	1	0.946	0.988	47.776	-0.011	-0.011	0.000	0.000	0.000	0.000
66	A	67	VAL	0	0.022	0.007	42.350	0.000	0.000	0.000	0.000	0.000	0.000
67	A	68	PHE	0	-0.015	-0.004	41.465	0.000	0.000	0.000	0.000	0.000	0.000
68	A	69	VAL	0	0.024	0.003	36.507	0.000	0.000	0.000	0.000	0.000	0.000
69	A	70	TRP	0	0.025	0.002	34.414	0.000	0.000	0.000	0.000	0.000	0.000
70	A	71	ALA	0	0.049	0.022	30.732	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.936	0.970	25.625	-0.046	-0.046	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.910	-0.954	30.130	0.026	0.026	0.000	0.000	0.000	0.000
73	A	74	LYS	1	0.872	0.925	23.219	-0.034	-0.034	0.000	0.000	0.000	0.000
74	A	75	PRO	0	0.056	0.027	27.397	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.027	0.006	29.166	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	77	LEU	0	-0.009	0.004	29.458	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	78	MET	0	0.016	0.009	31.492	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.037	0.016	34.647	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	80	ALA	0	0.051	0.034	30.962	-0.002	-0.002	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.026	-0.011	32.955	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	82	LEU	0	-0.018	0.004	35.123	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.892	-0.936	32.686	0.002	0.002	0.000	0.000	0.000	0.000
83	A	84	GLN	0	-0.069	-0.041	29.956	-0.002	-0.002	0.000	0.000	0.000	0.000
84	A	85	SER	0	-0.045	-0.034	35.671	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	86	GLY	0	-0.001	0.024	39.120	0.000	0.000	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.942	-0.983	40.429	0.006	0.006	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.081	-0.055	42.166	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	ALA	0	-0.030	-0.008	40.077	0.000	0.000	0.000	0.000	0.000	0.000
89	A	90	LEU	0	0.005	-0.003	42.089	0.001	0.001	0.000	0.000	0.000	0.000
90	A	91	LEU	0	-0.047	-0.026	37.841	0.000	0.000	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.002	-0.004	40.976	0.000	0.000	0.000	0.000	0.000	0.000
92	A	93	ARG	1	0.916	0.945	38.032	-0.023	-0.023	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.021	0.002	38.881	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	95	GLU	-1	-0.847	-0.908	38.533	0.030	0.030	0.000	0.000	0.000	0.000
95	A	96	ASN	0	-0.010	-0.005	39.630	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	97	GLY	0	0.018	-0.002	41.286	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	98	ARG	1	0.793	0.890	43.147	-0.024	-0.024	0.000	0.000	0.000	0.000
98	A	99	LEU	0	0.050	0.036	43.409	0.001	0.001	0.000	0.000	0.000	0.000
99	A	100	LEU	0	-0.022	-0.009	42.216	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.742	-0.883	43.876	0.015	0.015	0.000	0.000	0.000	0.000
101	A	102	THR	0	0.004	-0.007	41.608	0.001	0.001	0.000	0.000	0.000	0.000
102	A	103	HIS	0	-0.033	-0.009	42.906	0.001	0.001	0.000	0.000	0.000	0.000
103	A	104	GLY	0	-0.038	-0.019	44.028	0.001	0.001	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.911	0.961	44.847	-0.015	-0.015	0.000	0.000	0.000	0.000
105	A	106	ARG	1	0.957	0.973	47.801	-0.019	-0.019	0.000	0.000	0.000	0.000
106	A	107	ILE	0	0.047	0.032	46.960	-0.001	-0.001	0.000	0.000	0.000	0.000
107	A	108	SER	0	-0.065	-0.040	49.563	0.001	0.001	0.000	0.000	0.000	0.000
108	A	109	ILE	0	-0.005	0.000	48.474	-0.001	-0.001	0.000	0.000	0.000	0.000
109	A	110	THR	0	-0.017	-0.018	49.395	0.001	0.001	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.014	0.017	42.870	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.019	-0.009	43.429	0.000	0.000	0.000	0.000	0.000	0.000
112	A	113	ALA	0	0.032	0.008	43.331	0.001	0.001	0.000	0.000	0.000	0.000
113	A	114	VAL	0	-0.023	-0.014	39.577	0.001	0.001	0.000	0.000	0.000	0.000
114	A	115	ILE	0	-0.045	-0.007	38.486	0.000	0.000	0.000	0.000	0.000	0.000
115	A	116	PRO	0	-0.012	0.004	34.293	0.001	0.001	0.000	0.000	0.000	0.000
116	A	117	ASP	-1	-0.747	-0.876	36.824	0.028	0.028	0.000	0.000	0.000	0.000
117	A	118	GLN	0	-0.057	-0.035	32.775	0.003	0.003	0.000	0.000	0.000	0.000
118	A	119	VAL	0	-0.047	-0.013	33.349	0.001	0.001	0.000	0.000	0.000	0.000
119	A	120	ILE	0	0.033	0.019	33.783	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.047	-0.041	36.204	-0.001	-0.001	0.000	0.000	0.000	0.000
121	A	122	TRP	0	0.067	0.035	38.959	0.000	0.000	0.000	0.000	0.000	0.000
122	A	123	MET	0	-0.004	-0.015	41.225	0.000	0.000	0.000	0.000	0.000	0.000
123	A	124	ASN	0	0.017	0.046	44.399	0.000	0.000	0.000	0.000	0.000	0.000

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