FMO DATABASE

FMODB ID: R8218

Calculation Name: 3EUR-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EUR

Chain ID: A

ChEMBL ID:

UniProt ID: Q5LF10

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	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	140
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1355248.129727
FMO2-HF: Nuclear repulsion	1299910.054171
FMO2-HF: Total energy	-55338.075556
FMO2-MP2: Total energy	-55501.728209

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:0:ALA)

Summations of interaction energy for fragment #1(A:0:ALA)

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.
-3.453	-0.262	3.816	-2.568	-4.438	-0.006

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.060 / q_NPA : 0.022

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	2	ASN	0	0.076	0.032	3.468	-2.228	-0.703	-0.006	-0.661	-0.858	0.002
4	A	3	ARG	1	0.925	0.984	2.568	0.669	1.584	0.808	-0.475	-1.248	0.001
5	A	4	LEU	0	0.060	0.021	4.840	-0.447	-0.335	-0.001	-0.006	-0.106	0.000
6	A	5	GLY	0	0.024	0.015	6.176	-0.097	-0.097	0.000	0.000	0.000	0.000
7	A	6	THR	0	-0.087	-0.043	2.223	-2.379	-2.135	3.009	-1.297	-1.956	-0.009
8	A	7	LYS	1	0.935	0.978	4.418	0.897	0.970	-0.001	-0.017	-0.054	0.000
9	A	8	ALA	0	0.037	0.026	4.376	-0.465	-0.434	-0.001	-0.013	-0.016	0.000
10	A	9	LEU	0	0.020	0.018	3.854	-0.025	0.266	0.008	-0.099	-0.200	0.000
11	A	10	ASN	0	0.032	0.021	6.886	-0.248	-0.248	0.000	0.000	0.000	0.000
12	A	11	PHE	0	-0.001	-0.008	10.343	0.142	0.142	0.000	0.000	0.000	0.000
13	A	12	THR	0	0.032	0.008	13.469	-0.067	-0.067	0.000	0.000	0.000	0.000
14	A	13	TYR	0	0.013	0.020	17.207	0.011	0.011	0.000	0.000	0.000	0.000
15	A	14	THR	0	-0.030	-0.012	19.572	-0.010	-0.010	0.000	0.000	0.000	0.000
16	A	15	LEU	0	0.032	0.017	23.327	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	16	ASP	-1	-0.841	-0.927	25.800	0.046	0.046	0.000	0.000	0.000	0.000
18	A	17	SER	0	0.015	0.009	29.154	0.003	0.003	0.000	0.000	0.000	0.000
19	A	18	GLY	0	0.010	0.010	28.282	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	19	VAL	0	-0.026	-0.012	25.252	0.006	0.006	0.000	0.000	0.000	0.000
21	A	20	LYS	1	0.904	0.946	22.250	-0.103	-0.103	0.000	0.000	0.000	0.000
22	A	21	GLY	0	0.022	0.025	20.591	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.008	-0.001	15.252	0.016	0.016	0.000	0.000	0.000	0.000
24	A	23	LEU	0	0.041	0.019	10.489	-0.038	-0.038	0.000	0.000	0.000	0.000
25	A	24	TYR	0	-0.086	-0.087	7.245	-0.032	-0.032	0.000	0.000	0.000	0.000
26	A	25	GLN	0	-0.021	-0.007	13.959	-0.024	-0.024	0.000	0.000	0.000	0.000
27	A	26	PHE	0	0.004	0.024	16.831	0.001	0.001	0.000	0.000	0.000	0.000
28	A	27	PRO	0	-0.015	0.005	17.761	-0.032	-0.032	0.000	0.000	0.000	0.000
29	A	28	ALA	0	0.022	-0.014	18.918	0.014	0.014	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.876	-0.913	18.597	-0.193	-0.193	0.000	0.000	0.000	0.000
31	A	30	TYR	0	0.032	0.014	17.343	-0.029	-0.029	0.000	0.000	0.000	0.000
32	A	31	THR	0	-0.019	-0.021	15.223	0.042	0.042	0.000	0.000	0.000	0.000
33	A	32	LEU	0	0.011	0.005	15.951	-0.038	-0.038	0.000	0.000	0.000	0.000
34	A	33	LEU	0	-0.028	-0.008	12.254	0.026	0.026	0.000	0.000	0.000	0.000
35	A	34	PHE	0	0.030	-0.005	16.056	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	35	ILE	0	0.003	0.001	13.130	0.019	0.019	0.000	0.000	0.000	0.000
37	A	36	ASN	0	0.018	-0.014	17.800	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	37	ASN	0	0.063	0.000	21.383	0.005	0.005	0.000	0.000	0.000	0.000
39	A	38	PRO	0	0.003	-0.029	23.911	-0.006	-0.006	0.000	0.000	0.000	0.000
40	A	39	GLY	0	0.020	0.041	26.998	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	40	CYS	0	-0.060	-0.036	25.610	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	41	HIS	0	0.063	0.024	28.946	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	42	ALA	0	0.035	0.029	25.688	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	43	CYS	0	0.003	0.003	25.145	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.009	0.019	26.174	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	45	GLU	-1	-0.874	-0.944	29.060	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	46	MET	0	-0.044	-0.005	20.963	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	47	ILE	0	-0.045	-0.030	26.173	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	48	GLU	-1	-0.881	-0.944	27.547	-0.019	-0.019	0.000	0.000	0.000	0.000
50	A	49	GLY	0	0.011	0.001	27.986	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	50	LEU	0	-0.069	-0.050	22.591	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	51	LYS	1	0.860	0.934	26.733	0.005	0.005	0.000	0.000	0.000	0.000
53	A	52	ALA	0	0.028	0.037	30.111	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	53	SER	0	-0.045	-0.031	27.316	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	54	PRO	0	0.039	0.009	29.356	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	55	VAL	0	0.017	0.013	25.099	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	56	ILE	0	0.018	0.000	22.862	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	57	ASN	0	-0.048	-0.037	25.971	0.001	0.001	0.000	0.000	0.000	0.000
59	A	58	GLY	0	0.023	0.028	29.261	0.002	0.002	0.000	0.000	0.000	0.000
60	A	59	PHE	0	-0.003	-0.020	23.068	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	60	THR	0	-0.039	-0.022	25.136	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	61	ALA	0	-0.015	0.003	27.065	0.003	0.003	0.000	0.000	0.000	0.000
63	A	62	ALA	0	-0.027	-0.013	28.224	0.004	0.004	0.000	0.000	0.000	0.000
64	A	63	LYS	1	0.884	0.942	27.226	0.052	0.052	0.000	0.000	0.000	0.000
65	A	64	LYS	1	0.880	0.953	23.541	0.139	0.139	0.000	0.000	0.000	0.000
66	A	65	LEU	0	-0.010	-0.002	20.512	-0.016	-0.016	0.000	0.000	0.000	0.000
67	A	66	LYS	1	0.928	0.962	21.008	0.078	0.078	0.000	0.000	0.000	0.000
68	A	67	VAL	0	0.038	0.025	20.147	-0.016	-0.016	0.000	0.000	0.000	0.000
69	A	68	LEU	0	-0.046	-0.010	16.048	0.011	0.011	0.000	0.000	0.000	0.000
70	A	69	SER	0	-0.006	0.004	18.474	0.004	0.004	0.000	0.000	0.000	0.000
71	A	70	ILE	0	-0.027	-0.022	15.622	0.005	0.005	0.000	0.000	0.000	0.000
72	A	71	TYR	0	0.032	0.021	19.117	0.004	0.004	0.000	0.000	0.000	0.000
73	A	72	PRO	0	-0.021	-0.025	17.136	0.010	0.010	0.000	0.000	0.000	0.000
74	A	73	ASP	-1	-0.804	-0.876	19.102	0.199	0.199	0.000	0.000	0.000	0.000
75	A	74	GLU	-1	-0.783	-0.889	22.225	0.180	0.180	0.000	0.000	0.000	0.000
76	A	75	GLU	-1	-0.907	-0.941	25.454	0.090	0.090	0.000	0.000	0.000	0.000
77	A	76	LEU	0	-0.062	-0.036	26.470	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	77	ASP	-1	-0.842	-0.928	28.410	0.060	0.060	0.000	0.000	0.000	0.000
79	A	78	GLU	-1	-0.904	-0.951	29.906	0.057	0.057	0.000	0.000	0.000	0.000
80	A	79	TRP	0	0.003	-0.011	24.627	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	80	LYS	1	0.808	0.879	28.516	-0.066	-0.066	0.000	0.000	0.000	0.000
82	A	81	LYS	1	0.924	0.976	31.106	-0.045	-0.045	0.000	0.000	0.000	0.000
83	A	82	HIS	1	0.863	0.929	29.611	-0.044	-0.044	0.000	0.000	0.000	0.000
84	A	83	ARG	1	0.944	0.990	29.028	-0.033	-0.033	0.000	0.000	0.000	0.000
85	A	84	ASN	0	-0.065	-0.048	30.044	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	85	ASP	-1	-0.826	-0.890	30.104	0.016	0.016	0.000	0.000	0.000	0.000
87	A	86	PHE	0	-0.101	-0.044	24.397	-0.006	-0.006	0.000	0.000	0.000	0.000
88	A	87	ALA	0	0.034	0.019	28.416	0.000	0.000	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.946	0.972	28.661	0.015	0.015	0.000	0.000	0.000	0.000
90	A	89	GLU	-1	-0.904	-0.967	28.822	-0.023	-0.023	0.000	0.000	0.000	0.000
91	A	90	TRP	0	-0.068	-0.020	24.312	-0.004	-0.004	0.000	0.000	0.000	0.000
92	A	91	THR	0	-0.050	-0.019	21.964	0.004	0.004	0.000	0.000	0.000	0.000
93	A	92	ASN	0	0.044	0.010	22.299	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	93	GLY	0	0.009	-0.005	21.923	0.001	0.001	0.000	0.000	0.000	0.000
95	A	94	TYR	0	0.015	0.011	21.521	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	95	ASP	-1	-0.737	-0.878	16.874	0.299	0.299	0.000	0.000	0.000	0.000
97	A	96	LYS	1	0.901	0.962	19.855	-0.112	-0.112	0.000	0.000	0.000	0.000
98	A	97	GLU	-1	-0.916	-0.984	19.513	0.189	0.189	0.000	0.000	0.000	0.000
99	A	98	LEU	0	0.025	0.040	19.223	0.022	0.022	0.000	0.000	0.000	0.000
100	A	99	VAL	0	-0.025	-0.024	13.777	0.057	0.057	0.000	0.000	0.000	0.000
101	A	100	ILE	0	-0.032	-0.026	12.560	0.117	0.117	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.833	0.894	13.444	-0.121	-0.121	0.000	0.000	0.000	0.000
103	A	102	ASN	0	-0.005	-0.001	15.495	0.045	0.045	0.000	0.000	0.000	0.000
104	A	103	LYS	1	0.896	0.944	11.735	-0.592	-0.592	0.000	0.000	0.000	0.000
105	A	104	ASN	0	-0.040	-0.005	10.910	0.168	0.168	0.000	0.000	0.000	0.000
106	A	105	LEU	0	-0.050	-0.016	8.604	0.270	0.270	0.000	0.000	0.000	0.000
107	A	106	TYR	0	-0.049	-0.056	8.078	0.140	0.140	0.000	0.000	0.000	0.000
108	A	107	ASP	-1	-0.849	-0.890	10.484	0.205	0.205	0.000	0.000	0.000	0.000
109	A	108	LEU	0	0.045	0.005	12.368	-0.063	-0.063	0.000	0.000	0.000	0.000
110	A	109	ARG	1	0.809	0.876	13.731	-0.211	-0.211	0.000	0.000	0.000	0.000
111	A	110	ALA	0	0.011	0.014	17.211	-0.012	-0.012	0.000	0.000	0.000	0.000
112	A	111	ILE	0	-0.022	0.050	16.621	-0.020	-0.020	0.000	0.000	0.000	0.000
113	A	112	PRO	0	-0.055	-0.055	19.787	0.001	0.001	0.000	0.000	0.000	0.000
114	A	113	THR	0	0.018	0.018	14.772	0.000	0.000	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.005	0.003	16.658	0.009	0.009	0.000	0.000	0.000	0.000
116	A	115	TYR	0	-0.005	-0.011	8.956	-0.046	-0.046	0.000	0.000	0.000	0.000
117	A	116	LEU	0	0.014	0.023	13.348	0.036	0.036	0.000	0.000	0.000	0.000
118	A	117	LEU	0	-0.019	-0.014	10.147	-0.092	-0.092	0.000	0.000	0.000	0.000
119	A	118	ASP	-1	-0.734	-0.879	12.473	-0.455	-0.455	0.000	0.000	0.000	0.000
120	A	119	LYS	1	1.009	1.006	14.428	0.251	0.251	0.000	0.000	0.000	0.000
121	A	120	ASN	0	-0.109	-0.051	12.539	0.090	0.090	0.000	0.000	0.000	0.000
122	A	121	LYS	1	0.814	0.902	10.354	0.166	0.166	0.000	0.000	0.000	0.000
123	A	122	THR	0	-0.005	0.007	7.901	-0.206	-0.206	0.000	0.000	0.000	0.000
124	A	123	VAL	0	-0.058	-0.020	6.733	0.233	0.233	0.000	0.000	0.000	0.000
125	A	124	LEU	0	0.011	0.008	8.838	-0.062	-0.062	0.000	0.000	0.000	0.000
126	A	125	LEU	0	-0.010	-0.008	11.931	0.034	0.034	0.000	0.000	0.000	0.000
127	A	126	LYS	1	0.879	0.936	7.043	0.435	0.435	0.000	0.000	0.000	0.000
128	A	127	ASP	-1	-0.950	-0.984	11.124	-0.048	-0.048	0.000	0.000	0.000	0.000
129	A	128	ALA	0	0.000	0.026	14.094	0.004	0.004	0.000	0.000	0.000	0.000
130	A	129	THR	0	0.081	0.025	16.639	0.019	0.019	0.000	0.000	0.000	0.000
131	A	130	LEU	0	0.050	0.015	20.191	-0.017	-0.017	0.000	0.000	0.000	0.000
132	A	131	GLN	0	0.036	0.016	22.418	-0.014	-0.014	0.000	0.000	0.000	0.000
133	A	132	LYS	1	0.933	0.982	17.239	0.198	0.198	0.000	0.000	0.000	0.000
134	A	133	VAL	0	0.001	-0.009	17.774	-0.019	-0.019	0.000	0.000	0.000	0.000
135	A	134	GLU	-1	-0.842	-0.908	19.996	-0.087	-0.087	0.000	0.000	0.000	0.000
136	A	135	GLN	0	-0.020	-0.013	22.237	0.002	0.002	0.000	0.000	0.000	0.000
137	A	136	TYR	0	-0.009	-0.012	15.929	-0.021	-0.021	0.000	0.000	0.000	0.000
138	A	137	LEU	0	-0.028	-0.020	19.949	-0.005	-0.005	0.000	0.000	0.000	0.000
139	A	138	ALA	0	-0.054	-0.016	22.277	0.006	0.006	0.000	0.000	0.000	0.000
140	A	139	GLU	-1	-1.011	-0.989	20.846	-0.195	-0.195	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)