FMO DATABASE

FMODB ID: 7621K

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	OptAll
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	-1513054.702394
FMO2-HF: Nuclear repulsion	1451481.338571
FMO2-HF: Total energy	-61573.363822
FMO2-MP2: Total energy	-61747.827437

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.
-137.552	-139.94	39.687	-18.755	-18.542	-0.126

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 : 0.826 / q_NPA : 0.903

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	0.016	0.011	2.011	-35.991	-32.052	5.351	-4.706	-4.583	-0.058
4	A	10	LYS	1	0.842	0.905	3.592	53.601	53.958	0.003	-0.050	-0.310	0.000
5	A	11	LEU	0	0.014	0.022	6.052	5.347	5.347	0.000	0.000	0.000	0.000
6	A	12	LEU	0	-0.027	-0.005	9.206	-1.066	-1.066	0.000	0.000	0.000	0.000
7	A	13	VAL	0	-0.004	0.004	11.932	1.315	1.315	0.000	0.000	0.000	0.000
8	A	14	CYS	0	-0.032	-0.014	15.198	0.071	0.071	0.000	0.000	0.000	0.000
9	A	15	ASN	0	0.024	-0.017	18.409	0.323	0.323	0.000	0.000	0.000	0.000
10	A	16	ILE	0	-0.012	-0.020	21.616	0.143	0.143	0.000	0.000	0.000	0.000
11	A	17	ASP	-1	-0.808	-0.875	24.690	-11.043	-11.043	0.000	0.000	0.000	0.000
12	A	18	GLY	0	0.026	0.013	26.728	0.033	0.033	0.000	0.000	0.000	0.000
13	A	19	CYS	0	-0.055	-0.030	19.893	-0.354	-0.354	0.000	0.000	0.000	0.000
14	A	20	LEU	0	-0.004	0.006	22.176	-0.053	-0.053	0.000	0.000	0.000	0.000
15	A	21	THR	0	-0.041	-0.030	23.974	0.438	0.438	0.000	0.000	0.000	0.000
16	A	22	ASN	0	0.019	-0.001	27.043	-0.270	-0.270	0.000	0.000	0.000	0.000
17	A	23	GLY	0	0.033	0.008	29.344	0.270	0.270	0.000	0.000	0.000	0.000
18	A	24	HIS	0	-0.107	-0.036	30.559	0.513	0.513	0.000	0.000	0.000	0.000
19	A	25	ILE	0	0.015	0.007	33.927	-0.166	-0.166	0.000	0.000	0.000	0.000
20	A	26	TYR	0	-0.040	-0.019	34.831	0.117	0.117	0.000	0.000	0.000	0.000
21	A	27	VAL	0	-0.003	-0.021	39.496	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	28	SER	0	-0.035	-0.024	42.930	0.117	0.117	0.000	0.000	0.000	0.000
23	A	29	GLY	0	0.061	0.026	46.486	0.162	0.162	0.000	0.000	0.000	0.000
24	A	30	ASH	0	-0.056	-0.019	46.091	-0.021	-0.021	0.000	0.000	0.000	0.000
25	A	31	GLN	0	-0.010	-0.006	41.340	0.055	0.055	0.000	0.000	0.000	0.000
26	A	32	LYS	1	0.963	0.984	39.002	8.215	8.215	0.000	0.000	0.000	0.000
27	A	33	GLU	-1	-0.910	-0.958	37.797	-8.515	-8.515	0.000	0.000	0.000	0.000
28	A	34	ILE	0	-0.039	-0.007	36.710	-0.164	-0.164	0.000	0.000	0.000	0.000
29	A	35	ILE	0	0.031	0.026	30.096	0.014	0.014	0.000	0.000	0.000	0.000
30	A	36	SER	0	-0.009	-0.001	32.329	0.062	0.062	0.000	0.000	0.000	0.000
31	A	37	TYR	0	0.051	0.022	26.786	-0.289	-0.289	0.000	0.000	0.000	0.000
32	A	38	ASP	-1	-0.778	-0.867	26.446	-11.103	-11.103	0.000	0.000	0.000	0.000
33	A	39	VAL	0	0.036	0.015	26.169	-0.492	-0.492	0.000	0.000	0.000	0.000
34	A	40	LYS	1	0.828	0.891	24.400	11.070	11.070	0.000	0.000	0.000	0.000
35	A	41	ASP	-1	-0.745	-0.876	21.969	-14.505	-14.505	0.000	0.000	0.000	0.000
36	A	42	ALA	0	0.009	0.004	21.215	-0.775	-0.775	0.000	0.000	0.000	0.000
37	A	43	ILE	0	-0.022	-0.016	21.734	-0.527	-0.527	0.000	0.000	0.000	0.000
38	A	44	GLY	0	0.025	0.005	18.895	-0.621	-0.621	0.000	0.000	0.000	0.000
39	A	45	ILE	0	0.022	0.010	17.174	-1.173	-1.173	0.000	0.000	0.000	0.000
40	A	46	SER	0	-0.024	-0.006	17.004	-1.146	-1.146	0.000	0.000	0.000	0.000
41	A	47	LEU	0	-0.052	-0.031	17.148	-0.382	-0.382	0.000	0.000	0.000	0.000
42	A	48	LEU	0	0.040	0.025	11.706	-0.933	-0.933	0.000	0.000	0.000	0.000
43	A	49	LYS	1	0.888	0.940	12.896	16.426	16.426	0.000	0.000	0.000	0.000
44	A	50	LYS	1	0.905	0.956	14.102	16.035	16.035	0.000	0.000	0.000	0.000
45	A	51	SER	0	-0.072	-0.044	11.779	-0.506	-0.506	0.000	0.000	0.000	0.000
46	A	52	GLY	0	0.015	0.018	9.937	-1.995	-1.995	0.000	0.000	0.000	0.000
47	A	53	ILE	0	-0.080	-0.044	7.720	-5.440	-5.440	0.000	0.000	0.000	0.000
48	A	54	GLU	-1	-0.778	-0.873	9.873	-18.843	-18.843	0.000	0.000	0.000	0.000
49	A	55	VAL	0	-0.047	-0.034	11.871	-0.869	-0.869	0.000	0.000	0.000	0.000
50	A	56	ARG	1	0.712	0.821	14.666	22.217	22.217	0.000	0.000	0.000	0.000
51	A	57	LEU	0	-0.018	-0.009	16.921	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	58	ILE	0	0.031	0.010	19.354	0.242	0.242	0.000	0.000	0.000	0.000
53	A	59	SER	0	0.015	-0.005	21.906	0.246	0.246	0.000	0.000	0.000	0.000
54	A	60	GLU	-1	-0.791	-0.859	25.129	-11.157	-11.157	0.000	0.000	0.000	0.000
55	A	61	ARG	1	0.726	0.815	26.854	11.521	11.521	0.000	0.000	0.000	0.000
56	A	62	ALA	0	0.037	0.022	29.116	-0.332	-0.332	0.000	0.000	0.000	0.000
57	A	63	CYS	0	0.052	0.028	28.598	0.102	0.102	0.000	0.000	0.000	0.000
58	A	64	SER	0	0.012	0.008	30.715	-0.078	-0.078	0.000	0.000	0.000	0.000
59	A	65	LYS	1	1.053	1.014	28.044	10.940	10.940	0.000	0.000	0.000	0.000
60	A	66	GLN	0	0.009	0.016	30.249	0.002	0.002	0.000	0.000	0.000	0.000
61	A	67	THR	0	0.050	0.026	31.454	-0.032	-0.032	0.000	0.000	0.000	0.000
62	A	68	LEU	0	0.052	0.032	24.608	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	69	SER	0	-0.067	-0.042	27.957	-0.199	-0.199	0.000	0.000	0.000	0.000
64	A	70	ALA	0	0.002	-0.004	29.422	0.019	0.019	0.000	0.000	0.000	0.000
65	A	71	LEU	0	0.024	0.012	26.523	0.107	0.107	0.000	0.000	0.000	0.000
66	A	72	LYS	1	0.780	0.885	26.620	10.400	10.400	0.000	0.000	0.000	0.000
67	A	73	LEU	0	0.035	0.017	21.825	-0.215	-0.215	0.000	0.000	0.000	0.000
68	A	74	ASP	-1	-0.866	-0.899	20.496	-16.396	-16.396	0.000	0.000	0.000	0.000
69	A	75	CYS	0	0.009	0.021	18.792	-1.080	-1.080	0.000	0.000	0.000	0.000
70	A	76	LYS	1	0.846	0.922	17.571	16.024	16.024	0.000	0.000	0.000	0.000
71	A	77	THR	0	-0.002	-0.024	19.108	-0.458	-0.458	0.000	0.000	0.000	0.000
72	A	78	GLU	-1	-0.819	-0.877	20.906	-14.557	-14.557	0.000	0.000	0.000	0.000
73	A	79	VAL	0	-0.056	-0.040	23.435	-0.082	-0.082	0.000	0.000	0.000	0.000
74	A	80	SER	0	-0.062	-0.037	26.656	0.123	0.123	0.000	0.000	0.000	0.000
75	A	81	VAL	0	-0.003	0.008	22.476	0.152	0.152	0.000	0.000	0.000	0.000
76	A	82	SER	0	0.012	-0.007	25.628	0.030	0.030	0.000	0.000	0.000	0.000
77	A	83	ASP	-1	-0.834	-0.908	21.758	-13.930	-13.930	0.000	0.000	0.000	0.000
78	A	84	LYS	1	0.848	0.915	19.913	12.986	12.986	0.000	0.000	0.000	0.000
79	A	85	LEU	0	0.019	0.010	15.720	-1.081	-1.081	0.000	0.000	0.000	0.000
80	A	86	ALA	0	0.005	-0.002	17.187	-1.170	-1.170	0.000	0.000	0.000	0.000
81	A	87	THR	0	-0.015	-0.016	18.379	-0.452	-0.452	0.000	0.000	0.000	0.000
82	A	88	VAL	0	-0.013	-0.007	13.284	-0.872	-0.872	0.000	0.000	0.000	0.000
83	A	89	ASP	-1	-0.777	-0.876	13.721	-22.816	-22.816	0.000	0.000	0.000	0.000
84	A	90	GLU	-1	-0.846	-0.911	14.368	-18.142	-18.142	0.000	0.000	0.000	0.000
85	A	91	TRP	0	0.002	-0.016	13.953	-0.982	-0.982	0.000	0.000	0.000	0.000
86	A	92	ARG	1	0.794	0.883	9.118	24.975	24.975	0.000	0.000	0.000	0.000
87	A	93	LYS	1	0.718	0.842	10.366	16.136	16.136	0.000	0.000	0.000	0.000
88	A	94	GLU	-1	-0.845	-0.886	12.762	-20.629	-20.629	0.000	0.000	0.000	0.000
89	A	95	MET	0	-0.046	-0.018	8.406	0.498	0.498	0.000	0.000	0.000	0.000
90	A	96	GLY	0	0.001	0.012	8.789	-2.644	-2.644	0.000	0.000	0.000	0.000
91	A	97	LEU	0	-0.018	0.007	4.909	-3.255	-3.255	0.000	0.000	0.000	0.000
92	A	98	CYS	0	-0.027	-0.012	3.879	9.168	9.370	0.000	-0.020	-0.182	0.000
93	A	99	TRP	0	0.071	0.005	5.927	-2.989	-2.989	0.000	0.000	0.000	0.000
94	A	100	LYS	1	0.927	0.920	2.048	11.321	9.371	10.972	-4.159	-4.863	0.039
95	A	101	GLU	-1	-0.824	-0.880	1.686	-126.392	-131.712	23.358	-9.736	-8.302	-0.107
96	A	102	VAL	0	0.035	0.024	4.155	2.449	2.578	0.001	-0.026	-0.104	0.000
97	A	103	ALA	0	0.002	0.003	7.751	0.274	0.274	0.000	0.000	0.000	0.000
98	A	104	TYR	0	-0.018	-0.058	10.148	1.008	1.008	0.000	0.000	0.000	0.000
99	A	105	LEU	0	0.010	0.016	13.717	0.280	0.280	0.000	0.000	0.000	0.000
100	A	106	GLY	0	0.032	0.010	16.538	0.382	0.382	0.000	0.000	0.000	0.000
101	A	107	ASN	0	0.017	-0.019	19.473	-0.302	-0.302	0.000	0.000	0.000	0.000
102	A	108	GLU	-1	-0.749	-0.829	22.752	-11.496	-11.496	0.000	0.000	0.000	0.000
103	A	109	VAL	0	0.066	0.005	22.968	-0.459	-0.459	0.000	0.000	0.000	0.000
104	A	110	SER	0	0.016	0.002	23.340	-0.501	-0.501	0.000	0.000	0.000	0.000
105	A	111	ASP	-1	-0.732	-0.835	19.332	-14.854	-14.854	0.000	0.000	0.000	0.000
106	A	112	GLU	-1	-0.843	-0.911	18.432	-13.476	-13.476	0.000	0.000	0.000	0.000
107	A	113	GLU	-1	-0.830	-0.916	17.798	-14.157	-14.157	0.000	0.000	0.000	0.000
108	A	114	CYS	0	-0.039	-0.002	15.131	-0.792	-0.792	0.000	0.000	0.000	0.000
109	A	115	LEU	0	-0.044	-0.016	13.691	-1.493	-1.493	0.000	0.000	0.000	0.000
110	A	116	LYS	1	0.811	0.891	13.408	12.967	12.967	0.000	0.000	0.000	0.000
111	A	117	ARG	1	0.871	0.954	11.887	20.497	20.497	0.000	0.000	0.000	0.000
112	A	118	VAL	0	-0.063	-0.030	9.286	-1.569	-1.569	0.000	0.000	0.000	0.000
113	A	119	GLY	0	-0.034	-0.003	5.557	1.107	1.107	0.000	0.000	0.000	0.000
114	A	120	LEU	0	-0.034	-0.008	6.123	0.695	0.695	0.000	0.000	0.000	0.000
115	A	121	SER	0	0.004	-0.002	8.145	0.103	0.103	0.000	0.000	0.000	0.000
116	A	122	ALA	0	0.013	0.004	11.969	0.508	0.508	0.000	0.000	0.000	0.000
117	A	123	VAL	0	0.018	0.004	15.033	0.118	0.118	0.000	0.000	0.000	0.000
118	A	124	PRO	0	-0.003	-0.010	18.835	-0.016	-0.016	0.000	0.000	0.000	0.000
119	A	125	ALA	0	-0.010	0.003	21.748	0.179	0.179	0.000	0.000	0.000	0.000
120	A	126	ASP	-1	-0.814	-0.890	24.277	-11.040	-11.040	0.000	0.000	0.000	0.000
121	A	127	ALA	0	-0.018	0.010	22.676	0.181	0.181	0.000	0.000	0.000	0.000
122	A	128	CYS	0	-0.058	-0.008	24.630	0.361	0.361	0.000	0.000	0.000	0.000
123	A	129	SER	0	0.038	-0.004	24.445	-0.408	-0.408	0.000	0.000	0.000	0.000
124	A	130	GLY	0	-0.003	0.021	24.444	-0.011	-0.011	0.000	0.000	0.000	0.000
125	A	131	ALA	0	0.082	0.014	20.734	-0.323	-0.323	0.000	0.000	0.000	0.000
126	A	132	GLN	0	-0.039	-0.029	19.590	-0.458	-0.458	0.000	0.000	0.000	0.000
127	A	133	LYS	1	0.857	0.920	20.147	10.797	10.797	0.000	0.000	0.000	0.000
128	A	134	ALA	0	-0.043	-0.006	17.931	-0.122	-0.122	0.000	0.000	0.000	0.000
129	A	135	VAL	0	-0.035	-0.007	14.399	-0.970	-0.970	0.000	0.000	0.000	0.000
130	A	136	GLY	0	0.001	0.011	12.171	0.587	0.587	0.000	0.000	0.000	0.000
131	A	137	TYR	0	-0.110	-0.087	13.250	-0.041	-0.041	0.000	0.000	0.000	0.000
132	A	138	ILE	0	0.024	0.009	15.268	0.005	0.005	0.000	0.000	0.000	0.000
133	A	139	CYS	0	-0.065	-0.014	18.176	-0.043	-0.043	0.000	0.000	0.000	0.000
134	A	140	LYS	1	0.972	0.973	20.019	11.787	11.787	0.000	0.000	0.000	0.000
135	A	141	CYS	0	-0.126	-0.061	22.565	0.669	0.669	0.000	0.000	0.000	0.000
136	A	142	SER	0	0.019	-0.011	23.399	-0.278	-0.278	0.000	0.000	0.000	0.000
137	A	143	GLY	0	-0.005	-0.005	24.208	-0.424	-0.424	0.000	0.000	0.000	0.000
138	A	144	GLY	0	-0.016	0.002	24.776	0.556	0.556	0.000	0.000	0.000	0.000
139	A	145	ARG	1	0.812	0.885	25.698	10.924	10.924	0.000	0.000	0.000	0.000
140	A	146	GLY	0	-0.014	-0.015	23.822	0.300	0.300	0.000	0.000	0.000	0.000
141	A	147	ALA	0	0.018	0.031	20.782	-0.546	-0.546	0.000	0.000	0.000	0.000
142	A	148	ILE	0	0.064	0.017	17.890	-0.789	-0.789	0.000	0.000	0.000	0.000
143	A	149	ARG	1	0.753	0.866	17.802	14.285	14.285	0.000	0.000	0.000	0.000
144	A	150	GLU	-1	-0.716	-0.831	18.277	-14.686	-14.686	0.000	0.000	0.000	0.000
145	A	151	PHE	0	0.027	0.001	11.450	-0.733	-0.733	0.000	0.000	0.000	0.000
146	A	152	ALA	0	-0.002	0.001	13.554	-1.541	-1.541	0.000	0.000	0.000	0.000
147	A	153	GLU	-1	-0.793	-0.886	14.262	-18.128	-18.128	0.000	0.000	0.000	0.000
148	A	154	HIS	0	-0.009	0.004	11.781	-0.640	-0.640	0.000	0.000	0.000	0.000
149	A	155	ILE	0	0.016	-0.001	9.440	-1.618	-1.618	0.000	0.000	0.000	0.000
150	A	156	PHE	0	-0.055	-0.032	10.191	-2.268	-2.268	0.000	0.000	0.000	0.000
151	A	157	LEU	0	0.021	0.007	12.109	-0.473	-0.473	0.000	0.000	0.000	0.000
152	A	158	LEU	0	-0.065	-0.042	6.693	0.215	0.215	0.000	0.000	0.000	0.000
153	A	159	ILE	0	-0.015	0.005	7.452	-1.607	-1.607	0.000	0.000	0.000	0.000
154	A	160	GLU	-1	-0.906	-0.950	8.506	-21.273	-21.273	0.000	0.000	0.000	0.000
155	A	161	LYS	1	0.874	0.957	8.421	23.080	23.080	0.000	0.000	0.000	0.000
156	A	162	VAL	0	-0.088	-0.032	3.915	-0.103	0.152	0.002	-0.058	-0.198	0.000
157	A	163	ASN	0	-0.074	-0.038	6.823	1.424	1.424	0.000	0.000	0.000	0.000

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