FMO DATABASE

FMODB ID: QV68Y

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	OptHSide
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	-1355741.577617
FMO2-HF: Nuclear repulsion	1300402.570884
FMO2-HF: Total energy	-55339.006734
FMO2-MP2: Total energy	-55502.677561

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.
-3.444	-0.097999999999999	3.639	-2.497	-4.486	-0.007

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 : 0.052 / q_NPA : 0.014

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	0.043	0.021	3.406	-1.947	-0.446	-0.005	-0.637	-0.859	0.002
4	A	3	ARG	1	0.958	1.003	2.502	0.634	1.450	1.142	-0.580	-1.379	0.000
5	A	4	LEU	0	0.054	0.018	4.922	-0.435	-0.328	-0.001	-0.005	-0.101	0.000
6	A	5	GLY	0	0.025	0.016	6.243	-0.075	-0.075	0.000	0.000	0.000	0.000
7	A	6	THR	0	-0.086	-0.048	2.299	-2.508	-1.983	2.496	-1.146	-1.875	-0.009
8	A	7	LYS	1	0.890	0.963	4.442	0.868	0.940	-0.001	-0.018	-0.052	0.000
9	A	8	ALA	0	0.037	0.027	4.364	-0.511	-0.479	-0.001	-0.013	-0.017	0.000
10	A	9	LEU	0	0.018	0.015	3.853	-0.043	0.250	0.009	-0.098	-0.203	0.000
11	A	10	ASN	0	0.040	0.028	6.850	-0.233	-0.233	0.000	0.000	0.000	0.000
12	A	11	PHE	0	0.018	-0.001	10.313	0.143	0.143	0.000	0.000	0.000	0.000
13	A	12	THR	0	0.019	0.000	13.433	-0.061	-0.061	0.000	0.000	0.000	0.000
14	A	13	TYR	0	0.004	0.017	17.172	0.017	0.017	0.000	0.000	0.000	0.000
15	A	14	THR	0	-0.021	-0.014	19.533	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	15	LEU	0	0.038	0.024	23.288	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	16	ASP	-1	-0.789	-0.891	25.761	0.042	0.042	0.000	0.000	0.000	0.000
18	A	17	SER	0	0.001	0.001	29.112	0.003	0.003	0.000	0.000	0.000	0.000
19	A	18	GLY	0	-0.003	0.003	28.246	-0.001	-0.001	0.000	0.000	0.000	0.000
20	A	19	VAL	0	-0.024	-0.007	25.302	0.005	0.005	0.000	0.000	0.000	0.000
21	A	20	LYS	1	0.796	0.885	21.701	-0.121	-0.121	0.000	0.000	0.000	0.000
22	A	21	GLY	0	0.018	0.021	20.564	-0.014	-0.014	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.025	-0.031	15.174	0.016	0.016	0.000	0.000	0.000	0.000
24	A	23	LEU	0	0.012	0.011	10.438	-0.038	-0.038	0.000	0.000	0.000	0.000
25	A	24	TYR	0	-0.062	-0.080	7.201	-0.034	-0.034	0.000	0.000	0.000	0.000
26	A	25	GLN	0	0.022	0.032	13.945	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	26	PHE	0	0.000	0.019	16.799	0.004	0.004	0.000	0.000	0.000	0.000
28	A	27	PRO	0	-0.006	0.004	17.746	-0.032	-0.032	0.000	0.000	0.000	0.000
29	A	28	ALA	0	0.022	-0.010	18.830	0.014	0.014	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.850	-0.897	18.590	-0.192	-0.192	0.000	0.000	0.000	0.000
31	A	30	TYR	0	0.041	0.015	17.394	-0.030	-0.030	0.000	0.000	0.000	0.000
32	A	31	THR	0	-0.033	-0.024	15.146	0.041	0.041	0.000	0.000	0.000	0.000
33	A	32	LEU	0	0.015	0.007	15.975	-0.039	-0.039	0.000	0.000	0.000	0.000
34	A	33	LEU	0	-0.033	-0.009	12.230	0.026	0.026	0.000	0.000	0.000	0.000
35	A	34	PHE	0	0.033	0.001	16.019	-0.010	-0.010	0.000	0.000	0.000	0.000
36	A	35	ILE	0	0.006	0.009	13.051	0.020	0.020	0.000	0.000	0.000	0.000
37	A	36	ASN	0	0.003	-0.023	17.752	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	37	ASN	0	0.049	-0.007	21.334	0.004	0.004	0.000	0.000	0.000	0.000
39	A	38	PRO	0	0.017	-0.016	23.859	-0.004	-0.004	0.000	0.000	0.000	0.000
40	A	39	GLY	0	-0.002	0.021	26.947	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	40	CYS	0	-0.043	-0.026	25.477	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	41	HIS	0	0.075	0.026	28.895	-0.005	-0.005	0.000	0.000	0.000	0.000
43	A	42	ALA	0	0.031	0.028	25.701	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	43	CYS	0	0.009	0.002	25.172	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.005	0.019	26.127	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	45	GLU	-1	-0.879	-0.944	29.043	-0.015	-0.015	0.000	0.000	0.000	0.000
47	A	46	MET	0	-0.043	-0.009	21.177	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	47	ILE	0	-0.049	-0.028	26.178	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	48	GLU	-1	-0.790	-0.894	27.505	-0.020	-0.020	0.000	0.000	0.000	0.000
50	A	49	GLY	0	0.013	0.002	28.067	-0.004	-0.004	0.000	0.000	0.000	0.000
51	A	50	LEU	0	-0.068	-0.049	22.620	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	51	LYS	1	0.770	0.879	26.806	0.007	0.007	0.000	0.000	0.000	0.000
53	A	52	ALA	0	0.009	0.027	30.124	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	53	SER	0	-0.044	-0.041	27.353	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	54	PRO	0	0.041	0.016	29.433	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	55	VAL	0	0.003	0.006	25.365	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	56	ILE	0	0.023	0.002	23.093	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	57	ASN	0	-0.041	-0.042	26.040	0.000	0.000	0.000	0.000	0.000	0.000
59	A	58	GLY	0	0.015	0.024	29.325	0.002	0.002	0.000	0.000	0.000	0.000
60	A	59	PHE	0	0.006	-0.018	22.812	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	60	THR	0	-0.026	-0.010	25.186	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	61	ALA	0	-0.029	-0.009	27.117	0.004	0.004	0.000	0.000	0.000	0.000
63	A	62	ALA	0	-0.023	-0.015	28.284	0.004	0.004	0.000	0.000	0.000	0.000
64	A	63	LYS	1	0.866	0.941	27.211	0.058	0.058	0.000	0.000	0.000	0.000
65	A	64	LYS	1	0.858	0.937	23.591	0.142	0.142	0.000	0.000	0.000	0.000
66	A	65	LEU	0	-0.020	-0.014	20.581	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	66	LYS	1	0.926	0.967	20.988	0.080	0.080	0.000	0.000	0.000	0.000
68	A	67	VAL	0	0.034	0.024	20.120	-0.017	-0.017	0.000	0.000	0.000	0.000
69	A	68	LEU	0	-0.054	-0.016	15.982	0.011	0.011	0.000	0.000	0.000	0.000
70	A	69	SER	0	0.003	0.014	18.434	0.002	0.002	0.000	0.000	0.000	0.000
71	A	70	ILE	0	-0.041	-0.030	15.565	0.007	0.007	0.000	0.000	0.000	0.000
72	A	71	TYR	0	0.042	0.030	19.071	0.004	0.004	0.000	0.000	0.000	0.000
73	A	72	PRO	0	-0.024	-0.026	17.082	0.012	0.012	0.000	0.000	0.000	0.000
74	A	73	ASP	-1	-0.793	-0.877	19.051	0.186	0.186	0.000	0.000	0.000	0.000
75	A	74	GLU	-1	-0.777	-0.888	22.173	0.179	0.179	0.000	0.000	0.000	0.000
76	A	75	GLU	-1	-0.933	-0.949	25.402	0.084	0.084	0.000	0.000	0.000	0.000
77	A	76	LEU	0	-0.037	-0.024	26.522	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	77	ASP	-1	-0.847	-0.928	28.360	0.057	0.057	0.000	0.000	0.000	0.000
79	A	78	GLU	-1	-0.782	-0.867	29.915	0.040	0.040	0.000	0.000	0.000	0.000
80	A	79	TRP	0	-0.014	-0.015	24.356	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	80	LYS	1	0.843	0.889	28.466	-0.060	-0.060	0.000	0.000	0.000	0.000
82	A	81	LYS	1	0.820	0.900	31.058	-0.048	-0.048	0.000	0.000	0.000	0.000
83	A	82	HIS	1	0.818	0.903	29.523	-0.039	-0.039	0.000	0.000	0.000	0.000
84	A	83	ARG	1	0.865	0.940	28.983	-0.029	-0.029	0.000	0.000	0.000	0.000
85	A	84	ASN	0	-0.060	-0.042	29.998	-0.006	-0.006	0.000	0.000	0.000	0.000
86	A	85	ASP	-1	-0.805	-0.873	30.012	0.014	0.014	0.000	0.000	0.000	0.000
87	A	86	PHE	0	-0.070	-0.030	24.049	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	87	ALA	0	0.050	0.029	28.410	0.001	0.001	0.000	0.000	0.000	0.000
89	A	88	LYS	1	0.935	0.965	28.624	0.019	0.019	0.000	0.000	0.000	0.000
90	A	89	GLU	-1	-0.900	-0.963	28.774	-0.027	-0.027	0.000	0.000	0.000	0.000
91	A	90	TRP	0	-0.073	-0.027	24.281	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	91	THR	0	-0.042	-0.014	21.931	0.003	0.003	0.000	0.000	0.000	0.000
93	A	92	ASN	0	0.053	0.014	22.261	-0.002	-0.002	0.000	0.000	0.000	0.000
94	A	93	GLY	0	0.015	-0.003	21.882	0.001	0.001	0.000	0.000	0.000	0.000
95	A	94	TYR	0	0.023	0.016	21.480	0.004	0.004	0.000	0.000	0.000	0.000
96	A	95	ASP	-1	-0.745	-0.879	16.881	0.288	0.288	0.000	0.000	0.000	0.000
97	A	96	LYS	1	0.899	0.961	19.809	-0.104	-0.104	0.000	0.000	0.000	0.000
98	A	97	GLU	-1	-0.814	-0.918	19.647	0.159	0.159	0.000	0.000	0.000	0.000
99	A	98	LEU	0	0.025	0.040	19.154	0.023	0.023	0.000	0.000	0.000	0.000
100	A	99	VAL	0	-0.024	-0.028	13.836	0.052	0.052	0.000	0.000	0.000	0.000
101	A	100	ILE	0	-0.029	-0.030	12.501	0.113	0.113	0.000	0.000	0.000	0.000
102	A	101	LYS	1	0.832	0.892	13.444	-0.113	-0.113	0.000	0.000	0.000	0.000
103	A	102	ASN	0	-0.014	-0.001	15.495	0.046	0.046	0.000	0.000	0.000	0.000
104	A	103	LYS	1	0.897	0.942	11.756	-0.555	-0.555	0.000	0.000	0.000	0.000
105	A	104	ASN	0	-0.049	-0.011	10.910	0.179	0.179	0.000	0.000	0.000	0.000
106	A	105	LEU	0	-0.045	-0.009	8.627	0.260	0.260	0.000	0.000	0.000	0.000
107	A	106	TYR	0	-0.045	-0.059	8.025	0.120	0.120	0.000	0.000	0.000	0.000
108	A	107	ASP	-1	-0.857	-0.892	10.431	0.207	0.207	0.000	0.000	0.000	0.000
109	A	108	LEU	0	0.046	0.004	12.368	-0.063	-0.063	0.000	0.000	0.000	0.000
110	A	109	ARG	1	0.813	0.877	13.848	-0.193	-0.193	0.000	0.000	0.000	0.000
111	A	110	ALA	0	0.005	0.006	17.214	-0.011	-0.011	0.000	0.000	0.000	0.000
112	A	111	ILE	0	-0.013	0.041	16.362	-0.019	-0.019	0.000	0.000	0.000	0.000
113	A	112	PRO	0	-0.063	-0.048	19.787	0.001	0.001	0.000	0.000	0.000	0.000
114	A	113	THR	0	0.031	0.014	14.478	0.001	0.001	0.000	0.000	0.000	0.000
115	A	114	LEU	0	-0.023	-0.010	16.734	0.008	0.008	0.000	0.000	0.000	0.000
116	A	115	TYR	0	-0.003	-0.012	9.037	-0.051	-0.051	0.000	0.000	0.000	0.000
117	A	116	LEU	0	0.011	0.025	13.444	0.036	0.036	0.000	0.000	0.000	0.000
118	A	117	LEU	0	-0.011	-0.012	10.118	-0.093	-0.093	0.000	0.000	0.000	0.000
119	A	118	ASP	-1	-0.667	-0.836	12.516	-0.439	-0.439	0.000	0.000	0.000	0.000
120	A	119	LYS	1	0.995	1.015	14.455	0.259	0.259	0.000	0.000	0.000	0.000
121	A	120	ASN	0	-0.141	-0.071	12.456	0.078	0.078	0.000	0.000	0.000	0.000
122	A	121	LYS	1	0.826	0.908	10.466	0.172	0.172	0.000	0.000	0.000	0.000
123	A	122	THR	0	-0.019	-0.015	7.929	-0.187	-0.187	0.000	0.000	0.000	0.000
124	A	123	VAL	0	-0.063	-0.027	6.784	0.231	0.231	0.000	0.000	0.000	0.000
125	A	124	LEU	0	0.012	0.009	8.900	-0.058	-0.058	0.000	0.000	0.000	0.000
126	A	125	LEU	0	-0.011	-0.006	12.000	0.035	0.035	0.000	0.000	0.000	0.000
127	A	126	LYS	1	0.888	0.935	7.527	0.338	0.338	0.000	0.000	0.000	0.000
128	A	127	ASP	-1	-0.933	-0.957	11.212	-0.038	-0.038	0.000	0.000	0.000	0.000
129	A	128	ALA	0	-0.004	0.022	14.181	0.008	0.008	0.000	0.000	0.000	0.000
130	A	129	THR	0	0.073	0.020	16.728	0.018	0.018	0.000	0.000	0.000	0.000
131	A	130	LEU	0	0.051	0.019	20.278	-0.016	-0.016	0.000	0.000	0.000	0.000
132	A	131	GLN	0	0.033	0.017	22.502	-0.012	-0.012	0.000	0.000	0.000	0.000
133	A	132	LYS	1	0.864	0.944	18.110	0.187	0.187	0.000	0.000	0.000	0.000
134	A	133	VAL	0	0.011	-0.006	17.837	-0.019	-0.019	0.000	0.000	0.000	0.000
135	A	134	GLU	-1	-0.838	-0.890	20.078	-0.089	-0.089	0.000	0.000	0.000	0.000
136	A	135	GLN	0	0.014	0.005	22.284	-0.011	-0.011	0.000	0.000	0.000	0.000
137	A	136	TYR	0	-0.030	-0.023	16.036	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	137	LEU	0	-0.029	-0.013	20.005	-0.005	-0.005	0.000	0.000	0.000	0.000
139	A	138	ALA	0	-0.046	-0.013	22.347	0.006	0.006	0.000	0.000	0.000	0.000
140	A	139	GLU	-1	-0.953	-0.967	20.859	-0.190	-0.190	0.000	0.000	0.000	0.000

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