FMO DATABASE

FMODB ID: 52V6Z

Calculation Name: 3EP0-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EP0

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H4Q4

Base Structure: X-ray

Registration Date: 2023-09-19

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	OptH
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	119
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1007242.65977
FMO2-HF: Nuclear repulsion	959725.352242
FMO2-HF: Total energy	-47517.307528
FMO2-MP2: Total energy	-47655.186117

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:17:VAL)

Summations of interaction energy for fragment #1(A:17:VAL)

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.
-8.454	-6.383	16.144	-6.043	-12.171	-0.036

Interaction energy analysis for fragmet #1(A:17:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.020 / q_NPA : -0.015

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	19	LYS	1	0.946	0.974	2.173	-1.220	-2.111	9.586	-2.903	-5.792	-0.005
4	A	20	LEU	0	0.005	0.010	4.409	0.281	0.396	0.000	-0.027	-0.087	0.000
5	A	21	SER	0	0.043	0.012	7.853	-0.049	-0.049	0.000	0.000	0.000	0.000
6	A	22	SER	0	0.031	0.021	10.406	0.042	0.042	0.000	0.000	0.000	0.000
7	A	23	LEU	0	-0.035	-0.001	13.122	0.052	0.052	0.000	0.000	0.000	0.000
8	A	24	VAL	0	0.007	-0.004	15.004	0.034	0.034	0.000	0.000	0.000	0.000
9	A	25	LEU	0	-0.016	-0.004	14.751	-0.034	-0.034	0.000	0.000	0.000	0.000
10	A	26	PRO	0	0.010	0.013	11.585	0.034	0.034	0.000	0.000	0.000	0.000
11	A	27	ALA	0	0.030	0.009	13.747	0.022	0.022	0.000	0.000	0.000	0.000
12	A	28	GLU	-1	-0.922	-0.969	10.117	-0.140	-0.140	0.000	0.000	0.000	0.000
13	A	29	VAL	0	-0.017	-0.004	12.404	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	30	ILE	0	-0.025	-0.008	15.106	0.025	0.025	0.000	0.000	0.000	0.000
15	A	31	ILE	0	0.000	0.002	18.514	-0.021	-0.021	0.000	0.000	0.000	0.000
16	A	32	ALA	0	-0.029	-0.010	21.015	0.021	0.021	0.000	0.000	0.000	0.000
17	A	33	GLN	0	-0.039	-0.033	23.714	-0.013	-0.013	0.000	0.000	0.000	0.000
18	A	34	SER	0	-0.012	-0.008	22.700	0.004	0.004	0.000	0.000	0.000	0.000
19	A	35	SER	0	-0.094	-0.058	22.616	0.014	0.014	0.000	0.000	0.000	0.000
20	A	36	ILE	0	-0.006	-0.012	22.089	0.011	0.011	0.000	0.000	0.000	0.000
21	A	37	PRO	0	-0.078	-0.051	25.862	0.001	0.001	0.000	0.000	0.000	0.000
22	A	38	GLY	0	0.004	0.020	28.599	0.006	0.006	0.000	0.000	0.000	0.000
23	A	39	GLU	-1	-0.932	-0.970	24.820	-0.155	-0.155	0.000	0.000	0.000	0.000
24	A	40	GLY	0	0.028	0.026	26.892	0.002	0.002	0.000	0.000	0.000	0.000
25	A	41	LEU	0	-0.033	-0.023	23.765	0.003	0.003	0.000	0.000	0.000	0.000
26	A	42	GLY	0	0.091	0.047	20.798	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	43	ILE	0	-0.037	-0.013	14.561	0.012	0.012	0.000	0.000	0.000	0.000
28	A	44	PHE	0	0.018	0.018	17.300	-0.011	-0.011	0.000	0.000	0.000	0.000
29	A	45	SER	0	-0.024	-0.046	13.823	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	46	LYS	1	0.948	0.984	14.914	0.059	0.059	0.000	0.000	0.000	0.000
31	A	47	THR	0	-0.026	-0.024	12.355	0.033	0.033	0.000	0.000	0.000	0.000
32	A	48	TRP	0	0.031	0.019	11.691	-0.028	-0.028	0.000	0.000	0.000	0.000
33	A	49	ILE	0	0.001	0.005	7.513	0.049	0.049	0.000	0.000	0.000	0.000
34	A	50	LYS	1	0.870	0.932	5.110	-0.210	-0.210	0.000	0.000	0.000	0.000
35	A	51	ALA	0	0.082	0.046	6.165	-0.389	-0.389	0.000	0.000	0.000	0.000
36	A	52	GLY	0	0.009	0.001	3.705	0.205	0.544	0.003	-0.093	-0.249	0.000
37	A	53	THR	0	-0.061	-0.035	2.246	-3.565	-3.800	5.101	-1.911	-2.955	-0.018
38	A	54	GLU	-1	-0.867	-0.911	2.381	-5.772	-3.736	1.219	-0.874	-2.380	-0.014
39	A	55	MET	0	-0.020	-0.014	4.373	0.352	0.376	0.000	-0.006	-0.018	0.000
40	A	56	GLY	0	0.028	0.030	7.798	0.045	0.045	0.000	0.000	0.000	0.000
41	A	57	PRO	0	-0.027	-0.020	9.906	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	58	PHE	0	0.054	0.008	11.956	0.052	0.052	0.000	0.000	0.000	0.000
43	A	59	THR	0	-0.056	-0.026	14.493	0.024	0.024	0.000	0.000	0.000	0.000
44	A	60	GLY	0	0.046	0.004	17.773	0.006	0.006	0.000	0.000	0.000	0.000
45	A	61	ARG	1	0.786	0.888	21.322	0.169	0.169	0.000	0.000	0.000	0.000
46	A	62	VAL	0	0.000	0.006	22.309	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	63	ILE	0	-0.070	-0.027	24.455	0.019	0.019	0.000	0.000	0.000	0.000
48	A	64	ALA	0	0.013	-0.003	26.189	-0.010	-0.010	0.000	0.000	0.000	0.000
49	A	65	PRO	0	0.005	0.013	26.866	0.007	0.007	0.000	0.000	0.000	0.000
50	A	76	LEU	0	0.029	0.036	18.711	0.008	0.008	0.000	0.000	0.000	0.000
51	A	77	MET	0	-0.087	-0.039	21.464	-0.004	-0.004	0.000	0.000	0.000	0.000
52	A	78	TRP	0	0.029	0.022	16.860	-0.010	-0.010	0.000	0.000	0.000	0.000
53	A	79	GLU	-1	-0.829	-0.904	19.397	-0.252	-0.252	0.000	0.000	0.000	0.000
54	A	80	VAL	0	-0.041	-0.014	17.499	-0.037	-0.037	0.000	0.000	0.000	0.000
55	A	81	PHE	0	0.007	-0.006	17.675	0.037	0.037	0.000	0.000	0.000	0.000
56	A	82	ASN	0	-0.030	-0.020	19.602	-0.017	-0.017	0.000	0.000	0.000	0.000
57	A	83	GLU	-1	-0.943	-0.980	20.020	-0.196	-0.196	0.000	0.000	0.000	0.000
58	A	84	ASP	-1	-0.854	-0.915	21.091	-0.173	-0.173	0.000	0.000	0.000	0.000
59	A	85	GLY	0	0.000	0.006	21.480	0.008	0.008	0.000	0.000	0.000	0.000
60	A	86	THR	0	-0.045	-0.021	22.541	0.000	0.000	0.000	0.000	0.000	0.000
61	A	87	VAL	0	0.005	-0.002	23.047	-0.015	-0.015	0.000	0.000	0.000	0.000
62	A	88	ARG	1	0.841	0.926	21.649	0.222	0.222	0.000	0.000	0.000	0.000
63	A	89	TYR	0	-0.040	-0.047	19.673	0.021	0.021	0.000	0.000	0.000	0.000
64	A	90	PHE	0	0.058	0.040	22.068	-0.015	-0.015	0.000	0.000	0.000	0.000
65	A	91	ILE	0	-0.050	-0.007	17.437	0.014	0.014	0.000	0.000	0.000	0.000
66	A	92	ASP	-1	-0.702	-0.837	20.784	-0.198	-0.198	0.000	0.000	0.000	0.000
67	A	93	ALA	0	0.010	0.028	20.335	0.009	0.009	0.000	0.000	0.000	0.000
68	A	94	SER	0	0.038	-0.050	22.381	0.022	0.022	0.000	0.000	0.000	0.000
69	A	95	GLN	0	-0.083	-0.052	25.354	0.001	0.001	0.000	0.000	0.000	0.000
70	A	96	GLU	-1	-0.830	-0.897	24.340	-0.143	-0.143	0.000	0.000	0.000	0.000
71	A	97	ASP	-1	-0.789	-0.909	22.406	-0.227	-0.227	0.000	0.000	0.000	0.000
72	A	98	HIS	0	-0.100	-0.056	22.057	-0.015	-0.015	0.000	0.000	0.000	0.000
73	A	99	ARG	1	0.768	0.884	19.444	0.195	0.195	0.000	0.000	0.000	0.000
74	A	100	SER	0	0.006	-0.020	15.856	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	101	TRP	0	0.030	0.012	10.936	0.020	0.020	0.000	0.000	0.000	0.000
76	A	102	MET	0	-0.012	0.001	11.366	0.002	0.002	0.000	0.000	0.000	0.000
77	A	103	THR	0	-0.050	-0.021	15.690	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	104	TYR	0	-0.045	-0.025	18.485	0.027	0.027	0.000	0.000	0.000	0.000
79	A	105	ILE	0	-0.086	-0.031	12.920	0.014	0.014	0.000	0.000	0.000	0.000
80	A	106	LYS	1	0.927	0.986	17.350	0.192	0.192	0.000	0.000	0.000	0.000
81	A	107	CYS	0	0.017	-0.008	18.208	-0.037	-0.037	0.000	0.000	0.000	0.000
82	A	108	ALA	0	-0.002	0.028	18.085	0.026	0.026	0.000	0.000	0.000	0.000
83	A	109	ARG	1	0.813	0.876	20.032	0.142	0.142	0.000	0.000	0.000	0.000
84	A	110	ASN	0	-0.053	-0.041	22.013	0.011	0.011	0.000	0.000	0.000	0.000
85	A	111	GLU	-1	-0.879	-0.945	18.233	-0.241	-0.241	0.000	0.000	0.000	0.000
86	A	112	GLN	0	-0.059	-0.032	18.914	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	113	GLU	-1	-0.759	-0.858	19.787	-0.162	-0.162	0.000	0.000	0.000	0.000
88	A	114	GLN	0	-0.057	-0.035	14.243	0.029	0.029	0.000	0.000	0.000	0.000
89	A	115	ASN	0	0.032	0.014	12.877	-0.032	-0.032	0.000	0.000	0.000	0.000
90	A	116	LEU	0	-0.061	-0.032	9.172	-0.117	-0.117	0.000	0.000	0.000	0.000
91	A	117	GLU	-1	-0.872	-0.939	9.478	-0.704	-0.704	0.000	0.000	0.000	0.000
92	A	118	VAL	0	-0.023	-0.013	10.123	-0.159	-0.159	0.000	0.000	0.000	0.000
93	A	119	VAL	0	-0.020	-0.001	6.895	-0.008	-0.008	0.000	0.000	0.000	0.000
94	A	120	GLN	0	0.014	-0.011	10.355	0.012	0.012	0.000	0.000	0.000	0.000
95	A	121	ILE	0	-0.011	0.000	6.483	0.011	0.011	0.000	0.000	0.000	0.000
96	A	122	GLY	0	0.000	-0.002	11.091	0.059	0.059	0.000	0.000	0.000	0.000
97	A	123	THR	0	-0.032	-0.013	14.355	0.004	0.004	0.000	0.000	0.000	0.000
98	A	124	SER	0	-0.021	-0.006	12.710	0.032	0.032	0.000	0.000	0.000	0.000
99	A	125	ILE	0	0.028	0.028	12.465	-0.053	-0.053	0.000	0.000	0.000	0.000
100	A	126	PHE	0	-0.005	-0.011	7.340	0.033	0.033	0.000	0.000	0.000	0.000
101	A	127	TYR	0	0.044	0.034	9.000	0.081	0.081	0.000	0.000	0.000	0.000
102	A	128	LYS	1	0.834	0.893	2.535	3.635	4.318	0.235	-0.229	-0.690	0.001
103	A	129	ALA	0	-0.007	0.006	6.067	0.276	0.276	0.000	0.000	0.000	0.000
104	A	130	ILE	0	0.027	0.035	7.275	-0.172	-0.172	0.000	0.000	0.000	0.000
105	A	131	GLU	-1	-0.876	-0.946	9.790	-0.270	-0.270	0.000	0.000	0.000	0.000
106	A	132	MET	0	-0.122	-0.077	9.316	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	133	ILE	0	0.040	0.024	10.480	0.003	0.003	0.000	0.000	0.000	0.000
108	A	134	PRO	0	0.014	0.004	12.498	0.042	0.042	0.000	0.000	0.000	0.000
109	A	135	PRO	0	-0.012	0.020	15.542	-0.038	-0.038	0.000	0.000	0.000	0.000
110	A	136	ASP	-1	-0.920	-0.959	17.001	-0.027	-0.027	0.000	0.000	0.000	0.000
111	A	137	GLN	0	-0.062	-0.032	16.239	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	138	GLU	-1	-0.752	-0.858	16.645	-0.197	-0.197	0.000	0.000	0.000	0.000
113	A	139	LEU	0	-0.053	-0.032	11.405	-0.019	-0.019	0.000	0.000	0.000	0.000
114	A	140	LEU	0	-0.015	-0.002	15.114	0.012	0.012	0.000	0.000	0.000	0.000
115	A	141	VAL	0	-0.007	-0.002	13.205	-0.033	-0.033	0.000	0.000	0.000	0.000
116	A	142	TRP	0	0.031	0.001	14.819	0.060	0.060	0.000	0.000	0.000	0.000
117	A	143	TYR	0	-0.033	-0.036	14.744	-0.070	-0.070	0.000	0.000	0.000	0.000
118	A	144	GLY	0	0.089	0.057	13.850	0.006	0.006	0.000	0.000	0.000	0.000
119	A	145	ASN	0	-0.069	-0.029	12.936	0.042	0.042	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:17:VAL)