FMO DATABASE

FMODB ID: KG5R3

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1359202.635076
FMO2-HF: Nuclear repulsion	1303863.37872
FMO2-HF: Total energy	-55339.256356
FMO2-MP2: Total energy	-55502.971542

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.
-3.416	0.496	2.33	-2.135	-4.108	-0.004

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 : 0.056 / q_NPA : 0.016

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	0.040	0.021	3.389	-1.954	-0.513	-0.001	-0.606	-0.834	0.001
4	A	3	ARG	1	0.969	0.999	2.505	0.924	1.676	0.882	-0.438	-1.197	0.000
5	A	4	LEU	0	0.068	0.028	5.066	-0.356	-0.258	-0.001	-0.003	-0.093	0.000
6	A	5	GLY	0	0.014	0.016	6.504	-0.051	-0.051	0.000	0.000	0.000	0.000
7	A	6	THR	0	-0.074	-0.043	2.661	-2.246	-1.303	1.396	-0.824	-1.515	-0.006
8	A	7	LYS	1	0.885	0.961	4.552	0.816	0.855	-0.001	-0.008	-0.030	0.000
9	A	8	ALA	0	0.038	0.028	4.236	-1.127	-1.050	-0.001	-0.023	-0.053	0.000
10	A	9	LEU	0	-0.008	0.005	3.399	-0.284	0.278	0.056	-0.233	-0.386	0.001
11	A	10	ASN	0	0.034	0.022	6.263	-0.167	-0.167	0.000	0.000	0.000	0.000
12	A	11	PHE	0	0.030	0.011	9.807	0.163	0.163	0.000	0.000	0.000	0.000
13	A	12	THR	0	0.015	-0.005	12.676	-0.068	-0.068	0.000	0.000	0.000	0.000
14	A	13	TYR	0	-0.002	0.011	16.450	0.019	0.019	0.000	0.000	0.000	0.000
15	A	14	THR	0	-0.015	-0.011	18.962	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	15	LEU	0	0.044	0.031	22.759	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	16	ASP	-1	-0.779	-0.880	25.332	0.034	0.034	0.000	0.000	0.000	0.000
18	A	17	SER	0	0.000	0.000	28.598	0.005	0.005	0.000	0.000	0.000	0.000
19	A	18	GLY	0	0.006	0.009	27.710	0.000	0.000	0.000	0.000	0.000	0.000
20	A	19	VAL	0	-0.027	-0.011	25.201	0.006	0.006	0.000	0.000	0.000	0.000
21	A	20	LYS	1	0.821	0.900	21.145	-0.108	-0.108	0.000	0.000	0.000	0.000
22	A	21	GLY	0	0.020	0.016	20.157	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.022	-0.026	14.653	0.017	0.017	0.000	0.000	0.000	0.000
24	A	23	LEU	0	0.020	0.016	9.997	-0.035	-0.035	0.000	0.000	0.000	0.000
25	A	24	TYR	0	-0.050	-0.072	6.910	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	25	GLN	0	0.026	0.039	13.698	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	26	PHE	0	-0.012	0.006	16.510	0.010	0.010	0.000	0.000	0.000	0.000
28	A	27	PRO	0	0.000	0.007	17.835	-0.035	-0.035	0.000	0.000	0.000	0.000
29	A	28	ALA	0	0.011	-0.006	19.238	0.016	0.016	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.844	-0.898	18.726	-0.204	-0.204	0.000	0.000	0.000	0.000
31	A	30	TYR	0	0.018	0.004	17.238	-0.033	-0.033	0.000	0.000	0.000	0.000
32	A	31	THR	0	-0.024	-0.029	14.809	0.038	0.038	0.000	0.000	0.000	0.000
33	A	32	LEU	0	0.037	0.020	15.378	-0.042	-0.042	0.000	0.000	0.000	0.000
34	A	33	LEU	0	-0.018	0.000	11.542	0.029	0.029	0.000	0.000	0.000	0.000
35	A	34	PHE	0	0.025	0.005	15.624	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	35	ILE	0	0.021	0.019	12.289	0.022	0.022	0.000	0.000	0.000	0.000
37	A	36	ASN	0	-0.033	-0.037	16.982	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	37	ASN	0	0.087	0.006	20.497	0.006	0.006	0.000	0.000	0.000	0.000
39	A	38	PRO	0	0.020	-0.001	23.341	-0.005	-0.005	0.000	0.000	0.000	0.000
40	A	39	GLY	0	-0.019	0.008	26.728	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	40	CYS	0	-0.055	-0.026	25.648	0.000	0.000	0.000	0.000	0.000	0.000
42	A	41	HIS	0	0.082	0.024	28.350	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	42	ALA	0	0.042	0.028	25.415	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	43	CYS	0	-0.012	0.002	24.829	-0.008	-0.008	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.010	0.021	25.814	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	45	GLU	-1	-0.891	-0.949	28.504	-0.021	-0.021	0.000	0.000	0.000	0.000
47	A	46	MET	0	-0.037	-0.004	20.788	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	47	ILE	0	-0.038	-0.016	25.823	-0.010	-0.010	0.000	0.000	0.000	0.000
49	A	48	GLU	-1	-0.770	-0.882	27.266	-0.026	-0.026	0.000	0.000	0.000	0.000
50	A	49	GLY	0	0.025	0.012	27.534	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	50	LEU	0	-0.067	-0.050	22.091	-0.010	-0.010	0.000	0.000	0.000	0.000
52	A	51	LYS	1	0.736	0.854	26.276	0.015	0.015	0.000	0.000	0.000	0.000
53	A	52	ALA	0	0.003	0.017	29.819	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	53	SER	0	-0.043	-0.045	26.658	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	54	PRO	0	0.032	0.011	28.716	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	55	VAL	0	-0.008	0.006	25.264	-0.001	-0.001	0.000	0.000	0.000	0.000
57	A	56	ILE	0	0.021	0.000	22.629	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	57	ASN	0	-0.040	-0.031	25.489	0.000	0.000	0.000	0.000	0.000	0.000
59	A	58	GLY	0	0.025	0.025	28.868	0.002	0.002	0.000	0.000	0.000	0.000
60	A	59	PHE	0	0.009	-0.013	22.526	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	60	THR	0	-0.010	0.006	25.044	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	61	ALA	0	-0.004	0.003	26.981	0.005	0.005	0.000	0.000	0.000	0.000
63	A	62	ALA	0	0.004	0.000	27.958	0.004	0.004	0.000	0.000	0.000	0.000
64	A	63	LYS	1	0.793	0.886	27.036	0.070	0.070	0.000	0.000	0.000	0.000
65	A	64	LYS	1	0.844	0.928	23.266	0.153	0.153	0.000	0.000	0.000	0.000
66	A	65	LEU	0	-0.016	-0.005	20.415	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	66	LYS	1	0.900	0.959	20.868	0.094	0.094	0.000	0.000	0.000	0.000
68	A	67	VAL	0	0.029	0.022	19.939	-0.020	-0.020	0.000	0.000	0.000	0.000
69	A	68	LEU	0	-0.054	-0.022	15.514	0.009	0.009	0.000	0.000	0.000	0.000
70	A	69	SER	0	-0.003	0.015	17.965	0.004	0.004	0.000	0.000	0.000	0.000
71	A	70	ILE	0	-0.037	-0.020	15.172	0.007	0.007	0.000	0.000	0.000	0.000
72	A	71	TYR	0	0.067	0.036	18.553	0.006	0.006	0.000	0.000	0.000	0.000
73	A	72	PRO	0	-0.023	-0.025	16.546	0.011	0.011	0.000	0.000	0.000	0.000
74	A	73	ASP	-1	-0.811	-0.886	18.483	0.186	0.186	0.000	0.000	0.000	0.000
75	A	74	GLU	-1	-0.784	-0.890	21.695	0.180	0.180	0.000	0.000	0.000	0.000
76	A	75	GLU	-1	-0.919	-0.939	24.775	0.081	0.081	0.000	0.000	0.000	0.000
77	A	76	LEU	0	-0.039	-0.030	25.968	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	77	ASP	-1	-0.861	-0.931	27.621	0.051	0.051	0.000	0.000	0.000	0.000
79	A	78	GLU	-1	-0.792	-0.872	29.047	0.035	0.035	0.000	0.000	0.000	0.000
80	A	79	TRP	0	-0.032	-0.023	24.089	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	80	LYS	1	0.839	0.884	27.839	-0.051	-0.051	0.000	0.000	0.000	0.000
82	A	81	LYS	1	0.821	0.902	30.446	-0.044	-0.044	0.000	0.000	0.000	0.000
83	A	82	HIS	1	0.810	0.889	29.096	-0.033	-0.033	0.000	0.000	0.000	0.000
84	A	83	ARG	1	0.827	0.913	28.452	-0.020	-0.020	0.000	0.000	0.000	0.000
85	A	84	ASN	0	-0.037	-0.026	29.485	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	85	ASP	-1	-0.786	-0.849	29.482	0.008	0.008	0.000	0.000	0.000	0.000
87	A	86	PHE	0	-0.031	-0.021	23.713	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	87	ALA	0	0.047	0.036	28.062	0.002	0.002	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.932	0.965	28.111	0.027	0.027	0.000	0.000	0.000	0.000
90	A	89	GLU	-1	-0.872	-0.949	28.513	-0.037	-0.037	0.000	0.000	0.000	0.000
91	A	90	TRP	0	-0.070	-0.033	23.927	-0.009	-0.009	0.000	0.000	0.000	0.000
92	A	91	THR	0	-0.016	-0.005	21.585	0.003	0.003	0.000	0.000	0.000	0.000
93	A	92	ASN	0	0.038	0.003	21.854	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	93	GLY	0	0.000	-0.015	22.005	0.001	0.001	0.000	0.000	0.000	0.000
95	A	94	TYR	0	0.039	0.021	21.010	0.004	0.004	0.000	0.000	0.000	0.000
96	A	95	ASP	-1	-0.753	-0.879	16.146	0.275	0.275	0.000	0.000	0.000	0.000
97	A	96	LYS	1	0.852	0.928	19.217	-0.101	-0.101	0.000	0.000	0.000	0.000
98	A	97	GLU	-1	-0.806	-0.895	19.208	0.137	0.137	0.000	0.000	0.000	0.000
99	A	98	LEU	0	0.020	0.023	18.588	0.031	0.031	0.000	0.000	0.000	0.000
100	A	99	VAL	0	-0.036	-0.027	13.318	0.057	0.057	0.000	0.000	0.000	0.000
101	A	100	ILE	0	-0.028	-0.038	11.886	0.127	0.127	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.808	0.885	12.889	-0.107	-0.107	0.000	0.000	0.000	0.000
103	A	102	ASN	0	0.001	-0.001	14.987	0.059	0.059	0.000	0.000	0.000	0.000
104	A	103	LYS	1	0.902	0.951	11.291	-0.540	-0.540	0.000	0.000	0.000	0.000
105	A	104	ASN	0	-0.026	-0.007	10.355	0.215	0.215	0.000	0.000	0.000	0.000
106	A	105	LEU	0	-0.058	-0.007	8.013	0.278	0.278	0.000	0.000	0.000	0.000
107	A	106	TYR	0	-0.030	-0.053	7.339	0.086	0.086	0.000	0.000	0.000	0.000
108	A	107	ASP	-1	-0.844	-0.889	9.617	0.233	0.233	0.000	0.000	0.000	0.000
109	A	108	LEU	0	0.032	0.001	11.707	-0.066	-0.066	0.000	0.000	0.000	0.000
110	A	109	ARG	1	0.819	0.871	13.392	-0.196	-0.196	0.000	0.000	0.000	0.000
111	A	110	ALA	0	0.010	0.014	17.057	-0.010	-0.010	0.000	0.000	0.000	0.000
112	A	111	ILE	0	-0.039	0.031	16.126	-0.018	-0.018	0.000	0.000	0.000	0.000
113	A	112	PRO	0	-0.044	-0.030	19.601	0.004	0.004	0.000	0.000	0.000	0.000
114	A	113	THR	0	0.019	-0.018	14.192	0.000	0.000	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.017	-0.011	16.459	0.003	0.003	0.000	0.000	0.000	0.000
116	A	115	TYR	0	-0.014	-0.008	8.599	-0.072	-0.072	0.000	0.000	0.000	0.000
117	A	116	LEU	0	0.008	0.014	12.975	0.040	0.040	0.000	0.000	0.000	0.000
118	A	117	LEU	0	-0.016	-0.011	9.528	-0.097	-0.097	0.000	0.000	0.000	0.000
119	A	118	ASP	-1	-0.670	-0.815	12.321	-0.446	-0.446	0.000	0.000	0.000	0.000
120	A	119	LYS	1	0.994	1.012	14.196	0.258	0.258	0.000	0.000	0.000	0.000
121	A	120	ASN	0	-0.111	-0.064	12.500	0.059	0.059	0.000	0.000	0.000	0.000
122	A	121	LYS	1	0.810	0.906	10.593	0.215	0.215	0.000	0.000	0.000	0.000
123	A	122	THR	0	-0.026	-0.029	7.921	-0.224	-0.224	0.000	0.000	0.000	0.000
124	A	123	VAL	0	-0.055	-0.033	6.295	0.225	0.225	0.000	0.000	0.000	0.000
125	A	124	LEU	0	-0.005	0.003	8.622	-0.046	-0.046	0.000	0.000	0.000	0.000
126	A	125	LEU	0	-0.005	-0.002	11.830	0.038	0.038	0.000	0.000	0.000	0.000
127	A	126	LYS	1	0.859	0.912	7.366	0.447	0.447	0.000	0.000	0.000	0.000
128	A	127	ASP	-1	-0.896	-0.935	11.084	-0.045	-0.045	0.000	0.000	0.000	0.000
129	A	128	ALA	0	0.005	0.029	13.962	0.018	0.018	0.000	0.000	0.000	0.000
130	A	129	THR	0	0.056	0.010	16.516	0.017	0.017	0.000	0.000	0.000	0.000
131	A	130	LEU	0	0.048	0.022	20.164	-0.017	-0.017	0.000	0.000	0.000	0.000
132	A	131	GLN	0	0.048	0.023	22.154	-0.013	-0.013	0.000	0.000	0.000	0.000
133	A	132	LYS	1	0.830	0.923	18.084	0.199	0.199	0.000	0.000	0.000	0.000
134	A	133	VAL	0	0.004	-0.011	17.516	-0.021	-0.021	0.000	0.000	0.000	0.000
135	A	134	GLU	-1	-0.835	-0.894	19.759	-0.096	-0.096	0.000	0.000	0.000	0.000
136	A	135	GLN	0	0.007	0.002	22.230	-0.013	-0.013	0.000	0.000	0.000	0.000
137	A	136	TYR	0	-0.009	-0.014	16.029	-0.016	-0.016	0.000	0.000	0.000	0.000
138	A	137	LEU	0	-0.049	-0.023	19.893	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	138	ALA	0	-0.032	-0.009	22.339	0.009	0.009	0.000	0.000	0.000	0.000
140	A	139	GLU	-1	-0.908	-0.938	20.664	-0.197	-0.197	0.000	0.000	0.000	0.000

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