FMO DATABASE

FMODB ID: 2J3KR

Calculation Name: 1EW3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1EW3

Chain ID: A

ChEMBL ID:

UniProt ID: Q95182

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	158
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1744633.983832
FMO2-HF: Nuclear repulsion	1679309.328274
FMO2-HF: Total energy	-65324.655558
FMO2-MP2: Total energy	-65516.956985

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:23:VAL)

Summations of interaction energy for fragment #1(A:23: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.
-14.306	-7.213	2.205	-4.106	-5.191	-0.042

Interaction energy analysis for fragmet #1(A:23:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.037 / q_NPA : -0.026

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	25	ILE	0	0.044	0.038	3.728	-0.029	2.022	-0.010	-0.872	-1.169	-0.001
4	A	26	ARG	1	0.914	0.953	6.089	0.950	0.950	0.000	0.000	0.000	0.000
5	A	27	ASN	0	0.015	0.000	9.487	0.159	0.159	0.000	0.000	0.000	0.000
6	A	28	PHE	0	0.080	0.042	12.582	-0.050	-0.050	0.000	0.000	0.000	0.000
7	A	29	ASP	-1	-0.855	-0.909	14.175	-0.128	-0.128	0.000	0.000	0.000	0.000
8	A	30	ILE	0	0.046	0.010	17.023	0.007	0.007	0.000	0.000	0.000	0.000
9	A	31	SER	0	-0.104	-0.049	19.841	0.011	0.011	0.000	0.000	0.000	0.000
10	A	32	LYS	1	0.890	0.925	14.270	0.249	0.249	0.000	0.000	0.000	0.000
11	A	33	ILE	0	-0.027	0.001	17.370	0.003	0.003	0.000	0.000	0.000	0.000
12	A	34	SER	0	-0.045	-0.013	19.316	0.013	0.013	0.000	0.000	0.000	0.000
13	A	35	GLY	0	0.042	0.025	21.963	-0.010	-0.010	0.000	0.000	0.000	0.000
14	A	36	GLU	-1	-0.872	-0.949	22.819	0.003	0.003	0.000	0.000	0.000	0.000
15	A	37	TRP	0	-0.071	-0.034	14.219	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	38	TYR	0	0.035	0.026	18.437	0.002	0.002	0.000	0.000	0.000	0.000
17	A	39	SER	0	0.048	0.035	17.641	0.016	0.016	0.000	0.000	0.000	0.000
18	A	40	ILE	0	-0.024	0.003	13.988	-0.017	-0.017	0.000	0.000	0.000	0.000
19	A	41	PHE	0	-0.003	-0.012	11.868	-0.012	-0.012	0.000	0.000	0.000	0.000
20	A	42	LEU	0	0.029	0.024	16.392	0.002	0.002	0.000	0.000	0.000	0.000
21	A	43	ALA	0	-0.009	-0.008	15.431	0.010	0.010	0.000	0.000	0.000	0.000
22	A	44	SER	0	0.025	0.002	17.511	-0.004	-0.004	0.000	0.000	0.000	0.000
23	A	45	ASP	-1	-0.797	-0.864	19.714	0.177	0.177	0.000	0.000	0.000	0.000
24	A	46	VAL	0	0.006	0.004	21.372	-0.016	-0.016	0.000	0.000	0.000	0.000
25	A	47	LYS	1	0.873	0.924	22.677	-0.146	-0.146	0.000	0.000	0.000	0.000
26	A	48	GLU	-1	-0.831	-0.895	24.725	0.080	0.080	0.000	0.000	0.000	0.000
27	A	49	LYS	1	0.869	0.933	24.733	-0.093	-0.093	0.000	0.000	0.000	0.000
28	A	50	ILE	0	-0.016	0.004	20.609	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	51	GLU	-1	-0.903	-0.953	24.502	0.104	0.104	0.000	0.000	0.000	0.000
30	A	52	GLU	-1	-0.943	-0.982	27.239	0.065	0.065	0.000	0.000	0.000	0.000
31	A	53	ASN	0	0.030	0.006	30.109	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	54	GLY	0	-0.010	0.031	28.352	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	55	SER	0	-0.077	-0.088	28.404	0.002	0.002	0.000	0.000	0.000	0.000
34	A	56	MET	0	0.018	0.012	23.268	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	57	ARG	1	0.856	0.940	23.645	-0.084	-0.084	0.000	0.000	0.000	0.000
36	A	58	VAL	0	-0.019	0.013	23.442	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	59	PHE	0	0.002	-0.027	22.612	0.015	0.015	0.000	0.000	0.000	0.000
38	A	60	VAL	0	0.006	0.015	19.533	-0.010	-0.010	0.000	0.000	0.000	0.000
39	A	61	ASP	-1	-0.872	-0.934	22.851	0.018	0.018	0.000	0.000	0.000	0.000
40	A	62	VAL	0	0.021	0.008	23.628	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	63	ILE	0	0.020	0.027	19.749	0.006	0.006	0.000	0.000	0.000	0.000
42	A	64	ARG	1	0.886	0.927	23.877	-0.009	-0.009	0.000	0.000	0.000	0.000
43	A	65	ALA	0	0.032	0.030	24.837	0.005	0.005	0.000	0.000	0.000	0.000
44	A	66	LEU	0	-0.079	-0.048	26.268	-0.001	-0.001	0.000	0.000	0.000	0.000
45	A	67	ASP	-1	-0.868	-0.940	29.237	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	68	ASN	0	-0.023	-0.003	31.323	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	69	SER	0	-0.112	-0.059	26.610	0.003	0.003	0.000	0.000	0.000	0.000
48	A	70	SER	0	0.083	0.050	26.132	0.001	0.001	0.000	0.000	0.000	0.000
49	A	71	LEU	0	-0.066	-0.025	21.417	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	72	TYR	0	-0.092	-0.110	25.722	0.006	0.006	0.000	0.000	0.000	0.000
51	A	73	ALA	0	0.046	0.012	24.054	-0.003	-0.003	0.000	0.000	0.000	0.000
52	A	74	GLU	-1	-0.849	-0.845	26.052	0.015	0.015	0.000	0.000	0.000	0.000
53	A	75	TYR	0	0.027	-0.015	21.432	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	76	GLN	0	0.004	-0.002	26.694	0.000	0.000	0.000	0.000	0.000	0.000
55	A	77	THR	0	-0.031	-0.037	27.320	0.008	0.008	0.000	0.000	0.000	0.000
56	A	78	LYS	1	0.919	0.963	29.460	-0.054	-0.054	0.000	0.000	0.000	0.000
57	A	79	VAL	0	0.000	0.017	31.993	0.004	0.004	0.000	0.000	0.000	0.000
58	A	80	ASN	0	-0.059	-0.049	34.749	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	81	GLY	0	-0.020	-0.014	34.931	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	82	GLU	-1	-0.935	-0.952	35.845	0.027	0.027	0.000	0.000	0.000	0.000
61	A	83	CYS	0	-0.068	-0.030	26.346	0.002	0.002	0.000	0.000	0.000	0.000
62	A	84	THR	0	-0.004	-0.012	32.665	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	85	GLU	-1	-0.904	-0.965	31.333	0.025	0.025	0.000	0.000	0.000	0.000
64	A	86	PHE	0	-0.086	-0.027	29.052	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	87	PRO	0	0.035	0.029	29.869	0.003	0.003	0.000	0.000	0.000	0.000
66	A	88	MET	0	-0.017	-0.004	25.652	0.004	0.004	0.000	0.000	0.000	0.000
67	A	89	VAL	0	-0.046	-0.034	27.985	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	90	PHE	0	-0.017	-0.015	22.579	0.005	0.005	0.000	0.000	0.000	0.000
69	A	91	ASP	-1	-0.857	-0.924	25.944	0.014	0.014	0.000	0.000	0.000	0.000
70	A	92	LYS	1	0.922	0.957	22.558	0.031	0.031	0.000	0.000	0.000	0.000
71	A	93	THR	0	-0.050	-0.024	22.886	0.002	0.002	0.000	0.000	0.000	0.000
72	A	94	GLU	-1	-1.008	-1.010	25.189	-0.007	-0.007	0.000	0.000	0.000	0.000
73	A	95	GLU	-1	-0.866	-0.921	18.786	-0.016	-0.016	0.000	0.000	0.000	0.000
74	A	96	ASP	-1	-0.867	-0.962	19.172	-0.044	-0.044	0.000	0.000	0.000	0.000
75	A	97	GLY	0	-0.054	-0.029	16.824	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	98	VAL	0	-0.055	-0.033	17.550	0.029	0.029	0.000	0.000	0.000	0.000
77	A	99	TYR	0	0.005	0.028	19.630	-0.017	-0.017	0.000	0.000	0.000	0.000
78	A	100	SER	0	0.005	-0.002	22.410	0.011	0.011	0.000	0.000	0.000	0.000
79	A	101	LEU	0	0.037	0.011	24.430	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	102	ASN	0	-0.040	-0.016	26.750	0.006	0.006	0.000	0.000	0.000	0.000
81	A	103	TYR	0	-0.005	-0.030	26.871	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	104	ASP	-1	-0.797	-0.844	28.510	0.080	0.080	0.000	0.000	0.000	0.000
83	A	105	GLY	0	0.051	0.042	29.662	0.005	0.005	0.000	0.000	0.000	0.000
84	A	106	TYR	0	-0.013	-0.010	27.390	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	107	ASN	0	-0.008	-0.015	23.627	0.014	0.014	0.000	0.000	0.000	0.000
86	A	108	VAL	0	0.007	0.003	20.794	-0.010	-0.010	0.000	0.000	0.000	0.000
87	A	109	PHE	0	0.004	-0.005	17.997	0.016	0.016	0.000	0.000	0.000	0.000
88	A	110	ARG	1	0.894	0.963	13.063	-0.058	-0.058	0.000	0.000	0.000	0.000
89	A	111	ILE	0	0.015	-0.013	14.625	0.046	0.046	0.000	0.000	0.000	0.000
90	A	112	SER	0	-0.099	-0.061	9.930	-0.063	-0.063	0.000	0.000	0.000	0.000
91	A	113	GLU	-1	-0.942	-0.951	8.784	-0.344	-0.344	0.000	0.000	0.000	0.000
92	A	114	PHE	0	-0.015	-0.043	5.489	0.565	0.565	0.000	0.000	0.000	0.000
93	A	115	GLU	-1	-0.884	-0.957	2.286	-13.227	-9.649	1.690	-2.679	-2.589	-0.040
94	A	116	ASN	0	0.000	0.015	4.958	-0.243	-0.206	-0.001	-0.001	-0.034	0.000
95	A	117	ASP	-1	-0.865	-0.938	8.717	-0.099	-0.099	0.000	0.000	0.000	0.000
96	A	118	GLU	-1	-0.908	-0.957	11.486	-0.133	-0.133	0.000	0.000	0.000	0.000
97	A	119	HIS	0	-0.075	-0.060	8.933	0.090	0.090	0.000	0.000	0.000	0.000
98	A	120	ILE	0	0.004	0.016	10.434	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	121	ILE	0	-0.046	-0.016	8.247	0.078	0.078	0.000	0.000	0.000	0.000
100	A	122	LEU	0	-0.002	0.022	11.174	-0.083	-0.083	0.000	0.000	0.000	0.000
101	A	123	TYR	0	-0.065	-0.016	12.978	0.031	0.031	0.000	0.000	0.000	0.000
102	A	124	LEU	0	0.047	0.011	14.915	-0.037	-0.037	0.000	0.000	0.000	0.000
103	A	125	VAL	0	-0.005	0.003	18.687	0.016	0.016	0.000	0.000	0.000	0.000
104	A	126	ASN	0	-0.023	-0.005	21.341	-0.015	-0.015	0.000	0.000	0.000	0.000
105	A	127	PHE	0	-0.047	-0.046	23.315	0.003	0.003	0.000	0.000	0.000	0.000
106	A	128	ASP	-1	-0.850	-0.903	27.384	0.062	0.062	0.000	0.000	0.000	0.000
107	A	129	LYS	1	0.824	0.877	29.814	-0.050	-0.050	0.000	0.000	0.000	0.000
108	A	130	ASP	-1	-0.917	-0.939	32.012	0.058	0.058	0.000	0.000	0.000	0.000
109	A	131	ARG	1	0.777	0.866	28.560	-0.082	-0.082	0.000	0.000	0.000	0.000
110	A	132	PRO	0	0.029	0.038	25.412	0.003	0.003	0.000	0.000	0.000	0.000
111	A	133	PHE	0	-0.030	-0.018	22.201	0.002	0.002	0.000	0.000	0.000	0.000
112	A	134	GLN	0	0.016	-0.027	17.481	0.010	0.010	0.000	0.000	0.000	0.000
113	A	135	LEU	0	-0.001	-0.007	18.428	0.001	0.001	0.000	0.000	0.000	0.000
114	A	136	PHE	0	-0.044	-0.031	11.021	0.023	0.023	0.000	0.000	0.000	0.000
115	A	137	GLU	-1	-0.832	-0.904	15.042	0.121	0.121	0.000	0.000	0.000	0.000
116	A	138	PHE	0	-0.021	-0.020	8.475	0.055	0.055	0.000	0.000	0.000	0.000
117	A	139	TYR	0	-0.021	-0.027	13.534	-0.053	-0.053	0.000	0.000	0.000	0.000
118	A	140	ALA	0	0.025	0.017	13.290	0.028	0.028	0.000	0.000	0.000	0.000
119	A	141	ARG	1	0.898	0.947	14.740	0.044	0.044	0.000	0.000	0.000	0.000
120	A	142	GLU	-1	-0.907	-0.937	16.208	-0.071	-0.071	0.000	0.000	0.000	0.000
121	A	143	PRO	0	-0.004	-0.015	17.360	0.026	0.026	0.000	0.000	0.000	0.000
122	A	144	ASP	-1	-0.825	-0.914	16.956	0.093	0.093	0.000	0.000	0.000	0.000
123	A	145	VAL	0	0.007	0.014	11.922	-0.013	-0.013	0.000	0.000	0.000	0.000
124	A	146	SER	0	0.029	0.010	10.548	0.036	0.036	0.000	0.000	0.000	0.000
125	A	147	PRO	0	0.041	-0.014	11.522	0.063	0.063	0.000	0.000	0.000	0.000
126	A	148	GLU	-1	-0.905	-0.953	7.581	-0.182	-0.182	0.000	0.000	0.000	0.000
127	A	149	ILE	0	0.008	0.017	6.466	0.106	0.106	0.000	0.000	0.000	0.000
128	A	150	LYS	1	0.856	0.937	7.775	0.163	0.163	0.000	0.000	0.000	0.000
129	A	151	GLU	-1	-0.928	-0.958	8.703	0.352	0.352	0.000	0.000	0.000	0.000
130	A	152	GLU	-1	-0.867	-0.946	2.424	0.348	1.505	0.528	-0.520	-1.164	-0.001
131	A	153	PHE	0	0.040	0.018	5.774	0.293	0.293	0.000	0.000	0.000	0.000
132	A	154	VAL	0	0.029	0.011	8.317	-0.083	-0.083	0.000	0.000	0.000	0.000
133	A	155	LYS	1	0.819	0.908	3.867	-1.547	-1.383	-0.001	-0.022	-0.141	0.000
134	A	156	ILE	0	-0.037	0.001	4.100	-0.359	-0.253	-0.001	-0.012	-0.094	0.000
135	A	157	VAL	0	0.029	0.011	7.830	-0.152	-0.152	0.000	0.000	0.000	0.000
136	A	158	GLN	0	0.027	0.017	11.202	-0.143	-0.143	0.000	0.000	0.000	0.000
137	A	159	LYS	1	0.916	0.963	7.318	-0.740	-0.740	0.000	0.000	0.000	0.000
138	A	160	ARG	1	0.816	0.922	11.489	-0.327	-0.327	0.000	0.000	0.000	0.000
139	A	161	GLY	0	-0.035	-0.015	13.435	-0.046	-0.046	0.000	0.000	0.000	0.000
140	A	162	ILE	0	-0.011	0.006	15.217	-0.034	-0.034	0.000	0.000	0.000	0.000
141	A	163	VAL	0	-0.041	-0.012	16.124	0.030	0.030	0.000	0.000	0.000	0.000
142	A	164	LYS	1	1.000	0.981	14.269	-0.292	-0.292	0.000	0.000	0.000	0.000
143	A	165	GLU	-1	-0.855	-0.939	17.840	0.183	0.183	0.000	0.000	0.000	0.000
144	A	166	ASN	0	-0.085	-0.048	19.576	-0.026	-0.026	0.000	0.000	0.000	0.000
145	A	167	ILE	0	0.028	0.022	13.986	0.011	0.011	0.000	0.000	0.000	0.000
146	A	168	ILE	0	-0.063	-0.029	17.934	-0.024	-0.024	0.000	0.000	0.000	0.000
147	A	169	ASP	-1	-0.823	-0.890	17.468	0.163	0.163	0.000	0.000	0.000	0.000
148	A	170	LEU	0	0.036	-0.014	18.585	-0.023	-0.023	0.000	0.000	0.000	0.000
149	A	171	THR	0	-0.111	-0.061	17.751	-0.023	-0.023	0.000	0.000	0.000	0.000
150	A	172	LYS	1	0.847	0.921	19.450	-0.102	-0.102	0.000	0.000	0.000	0.000
151	A	173	ILE	0	-0.022	-0.006	23.301	-0.005	-0.005	0.000	0.000	0.000	0.000
152	A	174	ASP	-1	-0.878	-0.945	25.481	0.040	0.040	0.000	0.000	0.000	0.000
153	A	175	ARG	1	0.833	0.917	19.818	-0.074	-0.074	0.000	0.000	0.000	0.000
154	A	177	PHE	0	0.025	-0.010	22.970	-0.003	-0.003	0.000	0.000	0.000	0.000
155	A	178	GLN	0	-0.066	-0.036	28.810	-0.004	-0.004	0.000	0.000	0.000	0.000
156	A	179	LEU	0	-0.016	-0.017	31.387	-0.003	-0.003	0.000	0.000	0.000	0.000
157	A	180	ARG	1	0.814	0.950	22.978	-0.025	-0.025	0.000	0.000	0.000	0.000
158	A	181	GLY	0	-0.030	0.001	29.563	-0.006	-0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:23:VAL)