FMO DATABASE

FMODB ID: 98412

Calculation Name: 3EWI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EWI

Chain ID: A

ChEMBL ID:

UniProt ID: Q99KK2

Base Structure: X-ray

Registration Date: 2023-09-21

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	157
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1508279.852109
FMO2-HF: Nuclear repulsion	1446707.716244
FMO2-HF: Total energy	-61572.135865
FMO2-MP2: Total energy	-61746.609037

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:7:LYS)

Summations of interaction energy for fragment #1(A:7:LYS)

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.
-86.353	-82.686	23.194	-13.371	-13.489	-0.125

Interaction energy analysis for fragmet #1(A:7:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.836 / q_NPA : 0.904

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	9	ILE	0	0.009	0.007	3.176	-10.702	-7.351	0.062	-1.731	-1.682	-0.003
4	A	10	LYS	1	0.915	0.945	4.383	57.075	57.260	-0.001	-0.008	-0.175	0.000
5	A	11	LEU	0	0.009	0.011	7.070	3.745	3.745	0.000	0.000	0.000	0.000
6	A	12	LEU	0	-0.020	0.009	9.794	-0.784	-0.784	0.000	0.000	0.000	0.000
7	A	13	VAL	0	-0.006	0.004	12.454	1.185	1.185	0.000	0.000	0.000	0.000
8	A	14	CYS	0	-0.032	-0.019	15.220	-0.206	-0.206	0.000	0.000	0.000	0.000
9	A	15	ASN	0	0.036	-0.002	18.236	0.290	0.290	0.000	0.000	0.000	0.000
10	A	16	ILE	0	-0.028	-0.022	21.184	0.108	0.108	0.000	0.000	0.000	0.000
11	A	17	ASP	-1	-0.863	-0.935	24.413	-10.593	-10.593	0.000	0.000	0.000	0.000
12	A	18	GLY	0	0.015	0.002	26.077	-0.097	-0.097	0.000	0.000	0.000	0.000
13	A	19	CYS	0	-0.064	-0.011	19.971	-0.304	-0.304	0.000	0.000	0.000	0.000
14	A	20	LEU	0	0.024	0.011	22.878	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	21	THR	0	0.001	0.002	24.153	0.331	0.331	0.000	0.000	0.000	0.000
16	A	22	ASN	0	0.008	-0.024	26.956	-0.210	-0.210	0.000	0.000	0.000	0.000
17	A	23	GLY	0	0.006	-0.005	29.276	0.178	0.178	0.000	0.000	0.000	0.000
18	A	24	HIS	0	-0.079	-0.023	30.524	0.484	0.484	0.000	0.000	0.000	0.000
19	A	25	ILE	0	0.023	0.016	34.096	-0.137	-0.137	0.000	0.000	0.000	0.000
20	A	26	TYR	0	-0.025	0.005	34.657	0.137	0.137	0.000	0.000	0.000	0.000
21	A	27	VAL	0	0.028	-0.021	39.390	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	28	SER	0	-0.058	-0.085	42.697	0.089	0.089	0.000	0.000	0.000	0.000
23	A	29	GLY	0	0.090	0.036	46.222	0.148	0.148	0.000	0.000	0.000	0.000
24	A	30	ASH	0	-0.077	-0.031	46.478	0.009	0.009	0.000	0.000	0.000	0.000
25	A	31	GLN	0	0.006	0.069	41.211	0.061	0.061	0.000	0.000	0.000	0.000
26	A	32	LYS	1	0.983	1.008	40.129	7.918	7.918	0.000	0.000	0.000	0.000
27	A	33	GLU	-1	-0.958	-0.985	37.943	-8.262	-8.262	0.000	0.000	0.000	0.000
28	A	34	ILE	0	-0.034	-0.007	37.148	-0.159	-0.159	0.000	0.000	0.000	0.000
29	A	35	ILE	0	0.031	0.027	30.638	-0.014	-0.014	0.000	0.000	0.000	0.000
30	A	36	SER	0	-0.005	0.002	32.520	0.052	0.052	0.000	0.000	0.000	0.000
31	A	37	TYR	0	0.044	0.008	27.516	-0.276	-0.276	0.000	0.000	0.000	0.000
32	A	38	ASP	-1	-0.835	-0.910	26.280	-10.666	-10.666	0.000	0.000	0.000	0.000
33	A	39	VAL	0	0.039	0.006	26.502	-0.479	-0.479	0.000	0.000	0.000	0.000
34	A	40	LYS	1	0.959	0.975	24.183	10.864	10.864	0.000	0.000	0.000	0.000
35	A	41	ASP	-1	-0.754	-0.877	22.084	-13.682	-13.682	0.000	0.000	0.000	0.000
36	A	42	ALA	0	0.009	0.012	21.908	-0.710	-0.710	0.000	0.000	0.000	0.000
37	A	43	ILE	0	-0.026	-0.024	22.711	-0.475	-0.475	0.000	0.000	0.000	0.000
38	A	44	GLY	0	0.026	0.014	19.738	-0.522	-0.522	0.000	0.000	0.000	0.000
39	A	45	ILE	0	0.022	0.006	18.114	-1.027	-1.027	0.000	0.000	0.000	0.000
40	A	46	SER	0	-0.031	-0.016	18.175	-1.002	-1.002	0.000	0.000	0.000	0.000
41	A	47	LEU	0	-0.045	-0.037	18.205	-0.360	-0.360	0.000	0.000	0.000	0.000
42	A	48	LEU	0	0.038	0.027	12.737	-0.769	-0.769	0.000	0.000	0.000	0.000
43	A	49	LYS	1	0.968	0.998	13.924	16.107	16.107	0.000	0.000	0.000	0.000
44	A	50	LYS	1	0.896	0.961	15.376	15.322	15.322	0.000	0.000	0.000	0.000
45	A	51	SER	0	-0.077	-0.031	12.995	-0.519	-0.519	0.000	0.000	0.000	0.000
46	A	52	GLY	0	0.017	0.011	11.419	-1.790	-1.790	0.000	0.000	0.000	0.000
47	A	53	ILE	0	-0.079	-0.029	9.223	-2.593	-2.593	0.000	0.000	0.000	0.000
48	A	54	GLU	-1	-0.831	-0.904	10.960	-18.077	-18.077	0.000	0.000	0.000	0.000
49	A	55	VAL	0	-0.017	-0.019	12.737	-0.798	-0.798	0.000	0.000	0.000	0.000
50	A	56	ARG	1	0.679	0.794	15.279	21.308	21.308	0.000	0.000	0.000	0.000
51	A	57	LEU	0	-0.013	-0.005	17.474	-0.045	-0.045	0.000	0.000	0.000	0.000
52	A	58	ILE	0	0.029	0.014	19.260	0.145	0.145	0.000	0.000	0.000	0.000
53	A	59	SER	0	0.035	0.004	21.811	0.275	0.275	0.000	0.000	0.000	0.000
54	A	60	GLU	-1	-0.869	-0.919	24.789	-10.839	-10.839	0.000	0.000	0.000	0.000
55	A	61	ARG	1	0.798	0.891	26.625	11.086	11.086	0.000	0.000	0.000	0.000
56	A	62	ALA	0	0.031	0.020	29.073	-0.277	-0.277	0.000	0.000	0.000	0.000
57	A	63	CYS	0	0.063	0.018	28.685	0.020	0.020	0.000	0.000	0.000	0.000
58	A	64	SER	0	-0.026	0.007	30.805	-0.129	-0.129	0.000	0.000	0.000	0.000
59	A	65	LYS	1	1.068	1.017	29.395	10.447	10.447	0.000	0.000	0.000	0.000
60	A	66	GLN	0	-0.014	-0.015	30.684	-0.035	-0.035	0.000	0.000	0.000	0.000
61	A	67	THR	0	0.031	0.019	31.464	0.002	0.002	0.000	0.000	0.000	0.000
62	A	68	LEU	0	0.059	0.043	25.141	0.022	0.022	0.000	0.000	0.000	0.000
63	A	69	SER	0	-0.072	-0.050	28.615	-0.177	-0.177	0.000	0.000	0.000	0.000
64	A	70	ALA	0	-0.037	-0.027	29.817	-0.022	-0.022	0.000	0.000	0.000	0.000
65	A	71	LEU	0	-0.004	-0.010	26.599	0.126	0.126	0.000	0.000	0.000	0.000
66	A	72	LYS	1	0.846	0.935	27.767	9.958	9.958	0.000	0.000	0.000	0.000
67	A	73	LEU	0	0.032	0.013	22.702	-0.187	-0.187	0.000	0.000	0.000	0.000
68	A	74	ASP	-1	-0.945	-0.957	22.124	-14.846	-14.846	0.000	0.000	0.000	0.000
69	A	75	CYS	0	-0.008	0.003	19.856	-0.993	-0.993	0.000	0.000	0.000	0.000
70	A	76	LYS	1	0.943	0.998	18.425	15.496	15.496	0.000	0.000	0.000	0.000
71	A	77	THR	0	-0.016	-0.032	20.110	-0.350	-0.350	0.000	0.000	0.000	0.000
72	A	78	GLU	-1	-0.921	-0.961	21.419	-13.600	-13.600	0.000	0.000	0.000	0.000
73	A	79	VAL	0	-0.036	-0.026	23.777	-0.131	-0.131	0.000	0.000	0.000	0.000
74	A	80	SER	0	-0.063	-0.034	26.706	0.113	0.113	0.000	0.000	0.000	0.000
75	A	81	VAL	0	-0.013	-0.006	22.310	0.119	0.119	0.000	0.000	0.000	0.000
76	A	82	SER	0	0.019	0.003	25.475	0.093	0.093	0.000	0.000	0.000	0.000
77	A	83	ASP	-1	-0.862	-0.933	22.001	-13.531	-13.531	0.000	0.000	0.000	0.000
78	A	84	LYS	1	0.878	0.927	19.454	12.909	12.909	0.000	0.000	0.000	0.000
79	A	85	LEU	0	0.038	0.011	14.856	-1.020	-1.020	0.000	0.000	0.000	0.000
80	A	86	ALA	0	0.020	0.019	17.100	-1.100	-1.100	0.000	0.000	0.000	0.000
81	A	87	THR	0	0.002	0.010	18.649	-0.320	-0.320	0.000	0.000	0.000	0.000
82	A	88	VAL	0	-0.001	-0.011	13.165	-0.856	-0.856	0.000	0.000	0.000	0.000
83	A	89	ASP	-1	-0.857	-0.938	13.681	-22.569	-22.569	0.000	0.000	0.000	0.000
84	A	90	GLU	-1	-0.946	-0.972	14.261	-18.304	-18.304	0.000	0.000	0.000	0.000
85	A	91	TRP	0	0.021	-0.005	14.220	-0.647	-0.647	0.000	0.000	0.000	0.000
86	A	92	ARG	1	0.802	0.902	8.976	25.478	25.478	0.000	0.000	0.000	0.000
87	A	93	LYS	1	0.882	0.942	10.323	16.030	16.030	0.000	0.000	0.000	0.000
88	A	94	GLU	-1	-0.821	-0.853	12.440	-20.652	-20.652	0.000	0.000	0.000	0.000
89	A	95	MET	0	-0.042	-0.019	9.246	0.392	0.392	0.000	0.000	0.000	0.000
90	A	96	GLY	0	-0.017	0.004	8.940	-2.809	-2.809	0.000	0.000	0.000	0.000
91	A	97	LEU	0	-0.023	0.000	5.493	-5.376	-5.376	0.000	0.000	0.000	0.000
92	A	98	CYS	0	-0.049	-0.006	3.614	8.980	9.314	0.004	-0.042	-0.295	0.000
93	A	99	TRP	0	0.099	0.021	5.757	-0.967	-0.967	0.000	0.000	0.000	0.000
94	A	100	LYS	1	0.964	0.943	2.376	30.433	31.811	1.221	-0.708	-1.891	0.006
95	A	101	GLU	-1	-0.819	-0.884	1.762	-127.846	-129.876	21.903	-10.763	-9.111	-0.127
96	A	102	VAL	0	0.013	0.020	4.269	2.862	2.987	0.001	-0.033	-0.093	0.000
97	A	103	ALA	0	0.016	0.001	7.700	0.751	0.751	0.000	0.000	0.000	0.000
98	A	104	TYR	0	-0.034	-0.050	9.731	0.830	0.830	0.000	0.000	0.000	0.000
99	A	105	LEU	0	-0.014	0.007	13.247	0.356	0.356	0.000	0.000	0.000	0.000
100	A	106	GLY	0	0.010	-0.020	16.254	0.330	0.330	0.000	0.000	0.000	0.000
101	A	107	ASN	0	0.026	0.016	19.190	-0.382	-0.382	0.000	0.000	0.000	0.000
102	A	108	GLU	-1	-0.761	-0.879	22.337	-11.035	-11.035	0.000	0.000	0.000	0.000
103	A	109	VAL	0	0.078	0.018	22.843	-0.395	-0.395	0.000	0.000	0.000	0.000
104	A	110	SER	0	0.037	0.031	22.961	-0.556	-0.556	0.000	0.000	0.000	0.000
105	A	111	ASP	-1	-0.758	-0.857	18.986	-14.456	-14.456	0.000	0.000	0.000	0.000
106	A	112	GLU	-1	-0.852	-0.950	18.161	-13.002	-13.002	0.000	0.000	0.000	0.000
107	A	113	GLU	-1	-0.941	-0.973	17.809	-14.050	-14.050	0.000	0.000	0.000	0.000
108	A	114	CYS	0	-0.039	-0.017	14.859	-0.942	-0.942	0.000	0.000	0.000	0.000
109	A	115	LEU	0	-0.047	-0.012	13.393	-1.477	-1.477	0.000	0.000	0.000	0.000
110	A	116	LYS	1	0.948	0.968	13.391	13.224	13.224	0.000	0.000	0.000	0.000
111	A	117	ARG	1	0.867	0.960	11.362	20.009	20.009	0.000	0.000	0.000	0.000
112	A	118	VAL	0	-0.070	-0.033	9.029	-1.684	-1.684	0.000	0.000	0.000	0.000
113	A	119	GLY	0	-0.016	0.001	5.302	0.566	0.566	0.000	0.000	0.000	0.000
114	A	120	LEU	0	-0.048	-0.012	6.276	1.167	1.167	0.000	0.000	0.000	0.000
115	A	121	SER	0	0.038	0.027	8.178	0.421	0.421	0.000	0.000	0.000	0.000
116	A	122	ALA	0	0.010	-0.004	11.948	0.282	0.282	0.000	0.000	0.000	0.000
117	A	123	VAL	0	0.025	0.016	14.913	0.162	0.162	0.000	0.000	0.000	0.000
118	A	124	PRO	0	-0.002	-0.010	18.709	-0.044	-0.044	0.000	0.000	0.000	0.000
119	A	125	ALA	0	-0.024	-0.012	21.454	0.179	0.179	0.000	0.000	0.000	0.000
120	A	126	ASP	-1	-0.867	-0.932	23.899	-10.722	-10.722	0.000	0.000	0.000	0.000
121	A	127	ALA	0	-0.013	0.012	22.654	0.178	0.178	0.000	0.000	0.000	0.000
122	A	128	CYS	0	-0.051	-0.004	24.567	0.370	0.370	0.000	0.000	0.000	0.000
123	A	129	SER	0	0.013	-0.022	24.506	-0.390	-0.390	0.000	0.000	0.000	0.000
124	A	130	GLY	0	-0.006	0.001	24.416	-0.154	-0.154	0.000	0.000	0.000	0.000
125	A	131	ALA	0	0.083	0.027	20.854	-0.363	-0.363	0.000	0.000	0.000	0.000
126	A	132	GLN	0	-0.056	-0.032	19.599	-0.606	-0.606	0.000	0.000	0.000	0.000
127	A	133	LYS	1	0.911	0.951	19.688	10.379	10.379	0.000	0.000	0.000	0.000
128	A	134	ALA	0	-0.044	0.002	17.936	-0.166	-0.166	0.000	0.000	0.000	0.000
129	A	135	VAL	0	-0.029	-0.008	14.679	-0.988	-0.988	0.000	0.000	0.000	0.000
130	A	136	GLY	0	-0.019	0.000	12.634	0.559	0.559	0.000	0.000	0.000	0.000
131	A	137	TYR	0	-0.075	-0.068	13.184	0.121	0.121	0.000	0.000	0.000	0.000
132	A	138	ILE	0	0.013	0.011	15.068	-0.128	-0.128	0.000	0.000	0.000	0.000
133	A	139	CYS	0	-0.094	-0.026	18.095	-0.049	-0.049	0.000	0.000	0.000	0.000
134	A	140	LYS	1	0.974	0.974	19.696	11.315	11.315	0.000	0.000	0.000	0.000
135	A	141	CYS	0	-0.103	-0.046	22.367	0.656	0.656	0.000	0.000	0.000	0.000
136	A	142	SER	0	0.026	0.014	23.037	-0.216	-0.216	0.000	0.000	0.000	0.000
137	A	143	GLY	0	0.039	0.013	24.147	-0.326	-0.326	0.000	0.000	0.000	0.000
138	A	144	GLY	0	-0.051	-0.012	24.743	0.544	0.544	0.000	0.000	0.000	0.000
139	A	145	ARG	1	0.784	0.865	25.708	10.396	10.396	0.000	0.000	0.000	0.000
140	A	146	GLY	0	0.028	0.008	23.759	0.184	0.184	0.000	0.000	0.000	0.000
141	A	147	ALA	0	0.001	0.010	20.460	-0.454	-0.454	0.000	0.000	0.000	0.000
142	A	148	ILE	0	0.056	0.020	18.108	-0.792	-0.792	0.000	0.000	0.000	0.000
143	A	149	ARG	1	0.777	0.883	17.660	13.320	13.320	0.000	0.000	0.000	0.000
144	A	150	GLU	-1	-0.753	-0.850	17.822	-14.060	-14.060	0.000	0.000	0.000	0.000
145	A	151	PHE	0	0.048	0.008	11.163	-0.663	-0.663	0.000	0.000	0.000	0.000
146	A	152	ALA	0	-0.001	-0.006	13.347	-1.259	-1.259	0.000	0.000	0.000	0.000
147	A	153	GLU	-1	-0.834	-0.914	13.712	-16.954	-16.954	0.000	0.000	0.000	0.000
148	A	154	HIS	0	-0.004	0.008	10.586	-0.167	-0.167	0.000	0.000	0.000	0.000
149	A	155	ILE	0	-0.012	-0.019	8.573	-1.417	-1.417	0.000	0.000	0.000	0.000
150	A	156	PHE	0	-0.042	-0.028	9.428	-2.053	-2.053	0.000	0.000	0.000	0.000
151	A	157	LEU	0	0.036	0.009	11.263	-0.522	-0.522	0.000	0.000	0.000	0.000
152	A	158	LEU	0	-0.079	-0.043	6.190	0.037	0.037	0.000	0.000	0.000	0.000
153	A	159	ILE	0	-0.019	0.006	6.857	-1.572	-1.572	0.000	0.000	0.000	0.000
154	A	160	GLU	-1	-0.935	-0.978	7.880	-20.109	-20.109	0.000	0.000	0.000	0.000
155	A	161	LYS	1	0.870	0.969	7.781	23.155	23.155	0.000	0.000	0.000	0.000
156	A	162	VAL	0	-0.090	-0.045	3.586	0.001	0.325	0.004	-0.086	-0.242	-0.001
157	A	163	ASN	0	-0.007	0.016	6.626	-1.237	-1.237	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:LYS)