FMO DATABASE

FMODB ID: 82V7Y

Calculation Name: 4ETR-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4ETR

Chain ID: A

ChEMBL ID:

UniProt ID: Q9I1U6

Base Structure: X-ray

Registration Date: 2023-06-19

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	120
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-981615.403789
FMO2-HF: Nuclear repulsion	933552.154026
FMO2-HF: Total energy	-48063.249763
FMO2-MP2: Total energy	-48202.538948

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:5:ASN)

Summations of interaction energy for fragment #1(A:5:ASN)

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.
-8.11	-0.958	0.608	-3.175	-4.586	-0.013

Interaction energy analysis for fragmet #1(A:5:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.024 / q_NPA : -0.002

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

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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	7	ASP	-1	-0.839	-0.930	2.641	-2.509	0.167	0.271	-1.114	-1.833	0.002
4	A	8	ASP	-1	-0.887	-0.940	2.672	-7.176	-3.500	0.336	-1.814	-2.199	-0.016
5	A	9	THR	0	-0.069	-0.043	3.630	0.751	1.414	0.002	-0.242	-0.424	0.001
6	A	10	LEU	0	-0.044	-0.037	6.104	-0.129	-0.129	0.000	0.000	0.000	0.000
7	A	11	ASP	-1	-0.923	-0.944	6.978	-0.221	-0.221	0.000	0.000	0.000	0.000
8	A	12	VAL	0	-0.077	-0.043	7.912	0.015	0.015	0.000	0.000	0.000	0.000
9	A	13	LEU	0	-0.017	-0.012	10.032	-0.078	-0.078	0.000	0.000	0.000	0.000
10	A	14	ASN	0	0.030	0.008	11.316	-0.036	-0.036	0.000	0.000	0.000	0.000
11	A	15	ASP	-1	-0.898	-0.937	13.168	0.207	0.207	0.000	0.000	0.000	0.000
12	A	16	LEU	0	0.018	-0.004	13.937	-0.026	-0.026	0.000	0.000	0.000	0.000
13	A	17	LEU	0	-0.018	0.024	16.418	-0.032	-0.032	0.000	0.000	0.000	0.000
14	A	18	GLN	0	-0.034	-0.026	17.864	-0.026	-0.026	0.000	0.000	0.000	0.000
15	A	19	THR	0	-0.010	-0.001	19.005	-0.021	-0.021	0.000	0.000	0.000	0.000
16	A	20	SER	0	-0.034	-0.028	20.054	-0.013	-0.013	0.000	0.000	0.000	0.000
17	A	21	LYS	1	0.946	0.968	21.022	-0.160	-0.160	0.000	0.000	0.000	0.000
18	A	22	ASP	-1	-0.925	-0.951	23.836	0.098	0.098	0.000	0.000	0.000	0.000
19	A	23	GLY	0	0.000	-0.001	25.438	-0.010	-0.010	0.000	0.000	0.000	0.000
20	A	24	GLU	-1	-0.941	-0.967	26.807	0.106	0.106	0.000	0.000	0.000	0.000
21	A	25	ALA	0	-0.017	-0.007	28.620	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	26	GLY	0	0.020	0.003	29.728	-0.006	-0.006	0.000	0.000	0.000	0.000
23	A	27	PHE	0	-0.014	-0.027	27.386	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	28	HIS	0	-0.059	-0.041	32.453	-0.004	-0.004	0.000	0.000	0.000	0.000
25	A	29	ALA	0	0.032	0.020	34.487	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	30	CYS	0	-0.035	-0.014	32.481	0.001	0.001	0.000	0.000	0.000	0.000
27	A	31	ALA	0	-0.006	0.000	36.644	-0.003	-0.003	0.000	0.000	0.000	0.000
28	A	32	GLU	-1	-0.942	-0.965	37.967	0.057	0.057	0.000	0.000	0.000	0.000
29	A	33	ASP	-1	-0.953	-0.972	40.092	0.050	0.050	0.000	0.000	0.000	0.000
30	A	34	LEU	0	-0.039	-0.007	38.558	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	35	ARG	1	0.905	0.937	42.866	-0.043	-0.043	0.000	0.000	0.000	0.000
32	A	36	ASP	-1	-0.836	-0.918	44.032	0.051	0.051	0.000	0.000	0.000	0.000
33	A	37	PRO	0	-0.002	-0.001	43.458	0.003	0.003	0.000	0.000	0.000	0.000
34	A	38	GLN	0	0.007	-0.015	42.448	0.001	0.001	0.000	0.000	0.000	0.000
35	A	39	LEU	0	0.033	0.012	38.808	0.004	0.004	0.000	0.000	0.000	0.000
36	A	40	LYS	1	0.866	0.958	38.594	-0.051	-0.051	0.000	0.000	0.000	0.000
37	A	41	ALA	0	-0.025	-0.013	38.260	0.003	0.003	0.000	0.000	0.000	0.000
38	A	42	ALA	0	0.017	0.018	35.731	0.003	0.003	0.000	0.000	0.000	0.000
39	A	43	MET	0	-0.004	0.008	34.026	0.008	0.008	0.000	0.000	0.000	0.000
40	A	44	LEU	0	0.002	0.009	33.677	0.004	0.004	0.000	0.000	0.000	0.000
41	A	45	GLU	-1	-1.013	-1.025	33.231	0.087	0.087	0.000	0.000	0.000	0.000
42	A	46	GLN	0	-0.006	-0.016	28.435	0.015	0.015	0.000	0.000	0.000	0.000
43	A	47	SER	0	-0.052	-0.025	28.933	0.008	0.008	0.000	0.000	0.000	0.000
44	A	48	ARG	1	0.946	0.955	29.219	-0.081	-0.081	0.000	0.000	0.000	0.000
45	A	49	ASP	-1	-0.854	-0.924	26.917	0.129	0.129	0.000	0.000	0.000	0.000
46	A	50	CYS	0	-0.089	-0.024	24.640	0.017	0.017	0.000	0.000	0.000	0.000
47	A	51	ALA	0	0.069	0.045	24.183	0.014	0.014	0.000	0.000	0.000	0.000
48	A	52	ALA	0	0.003	-0.002	24.959	0.006	0.006	0.000	0.000	0.000	0.000
49	A	53	ALA	0	-0.029	-0.007	21.033	0.013	0.013	0.000	0.000	0.000	0.000
50	A	54	ALA	0	0.055	-0.003	20.139	0.029	0.029	0.000	0.000	0.000	0.000
51	A	55	ASP	-1	-0.929	-0.945	20.565	0.149	0.149	0.000	0.000	0.000	0.000
52	A	56	GLU	-1	-0.943	-0.977	18.351	0.258	0.258	0.000	0.000	0.000	0.000
53	A	57	LEU	0	-0.042	-0.021	15.062	0.034	0.034	0.000	0.000	0.000	0.000
54	A	58	GLU	-1	-0.869	-0.936	16.059	0.183	0.183	0.000	0.000	0.000	0.000
55	A	59	ARG	1	0.908	0.955	17.733	-0.187	-0.187	0.000	0.000	0.000	0.000
56	A	60	ILE	0	0.070	0.034	12.121	-0.006	-0.006	0.000	0.000	0.000	0.000
57	A	61	VAL	0	0.037	0.039	12.897	0.045	0.045	0.000	0.000	0.000	0.000
58	A	62	LEU	0	-0.086	-0.041	13.723	-0.016	-0.016	0.000	0.000	0.000	0.000
59	A	63	GLU	-1	-1.029	-1.011	13.783	0.196	0.196	0.000	0.000	0.000	0.000
60	A	64	LEU	0	-0.040	-0.027	8.130	-0.005	-0.005	0.000	0.000	0.000	0.000
61	A	65	GLY	0	-0.022	-0.005	10.180	0.028	0.028	0.000	0.000	0.000	0.000
62	A	66	GLY	0	-0.005	0.008	12.507	-0.016	-0.016	0.000	0.000	0.000	0.000
63	A	67	LYS	1	0.885	0.918	13.083	-0.175	-0.175	0.000	0.000	0.000	0.000
64	A	68	PRO	0	0.015	0.030	15.333	-0.017	-0.017	0.000	0.000	0.000	0.000
65	A	94	GLU	-1	-0.873	-0.967	43.259	0.047	0.047	0.000	0.000	0.000	0.000
66	A	95	GLU	-1	-0.857	-0.928	42.178	0.054	0.054	0.000	0.000	0.000	0.000
67	A	96	ALA	0	-0.056	-0.051	40.762	0.003	0.003	0.000	0.000	0.000	0.000
68	A	97	VAL	0	0.026	0.020	38.559	0.001	0.001	0.000	0.000	0.000	0.000
69	A	98	LEU	0	0.039	0.022	37.464	0.004	0.004	0.000	0.000	0.000	0.000
70	A	99	ASN	0	-0.004	-0.004	36.326	0.006	0.006	0.000	0.000	0.000	0.000
71	A	100	GLU	-1	-0.871	-0.918	32.151	0.072	0.072	0.000	0.000	0.000	0.000
72	A	102	GLU	-1	-0.692	-0.803	31.702	0.087	0.087	0.000	0.000	0.000	0.000
73	A	103	ARG	1	0.877	0.934	27.649	-0.072	-0.072	0.000	0.000	0.000	0.000
74	A	104	GLY	0	0.005	-0.001	28.148	0.007	0.007	0.000	0.000	0.000	0.000
75	A	105	GLU	-1	-0.794	-0.885	26.901	0.114	0.114	0.000	0.000	0.000	0.000
76	A	106	ASP	-1	-0.919	-0.953	26.263	0.125	0.125	0.000	0.000	0.000	0.000
77	A	107	VAL	0	-0.102	-0.056	23.056	0.013	0.013	0.000	0.000	0.000	0.000
78	A	108	ALA	0	0.021	0.018	22.485	0.017	0.017	0.000	0.000	0.000	0.000
79	A	109	LYS	1	0.987	0.985	21.376	-0.121	-0.121	0.000	0.000	0.000	0.000
80	A	110	HIS	0	-0.071	-0.041	21.056	0.012	0.012	0.000	0.000	0.000	0.000
81	A	111	ARG	1	0.940	0.973	17.956	-0.135	-0.135	0.000	0.000	0.000	0.000
82	A	112	TYR	0	0.032	-0.007	16.587	0.039	0.039	0.000	0.000	0.000	0.000
83	A	113	GLN	0	-0.008	-0.003	16.386	0.042	0.042	0.000	0.000	0.000	0.000
84	A	114	ALA	0	0.006	0.005	15.096	0.039	0.039	0.000	0.000	0.000	0.000
85	A	115	ALA	0	-0.028	-0.021	12.485	0.081	0.081	0.000	0.000	0.000	0.000
86	A	116	LEU	0	-0.058	-0.030	11.698	0.193	0.193	0.000	0.000	0.000	0.000
87	A	117	GLU	-1	-0.920	-0.940	13.129	0.433	0.433	0.000	0.000	0.000	0.000
88	A	118	LYS	1	0.834	0.935	8.011	-0.512	-0.512	0.000	0.000	0.000	0.000
89	A	119	SER	0	-0.030	-0.013	6.864	-0.262	-0.262	0.000	0.000	0.000	0.000
90	A	120	LEU	0	0.004	-0.009	5.362	1.667	1.667	0.000	0.000	0.000	0.000
91	A	121	PRO	0	-0.005	0.001	4.810	-0.989	-0.852	-0.001	-0.005	-0.130	0.000
92	A	122	ALA	0	0.028	0.021	7.201	0.008	0.008	0.000	0.000	0.000	0.000
93	A	123	GLU	-1	-0.914	-0.977	10.080	0.274	0.274	0.000	0.000	0.000	0.000
94	A	124	ILE	0	0.012	0.001	8.725	-0.048	-0.048	0.000	0.000	0.000	0.000
95	A	125	HIS	0	0.038	0.029	10.869	-0.119	-0.119	0.000	0.000	0.000	0.000
96	A	126	GLN	0	-0.006	-0.009	12.322	-0.116	-0.116	0.000	0.000	0.000	0.000
97	A	127	VAL	0	-0.036	-0.005	14.789	-0.060	-0.060	0.000	0.000	0.000	0.000
98	A	128	ILE	0	0.046	0.026	11.768	-0.053	-0.053	0.000	0.000	0.000	0.000
99	A	129	GLU	-1	-0.843	-0.925	15.845	0.288	0.288	0.000	0.000	0.000	0.000
100	A	130	ARG	1	0.845	0.893	17.820	-0.288	-0.288	0.000	0.000	0.000	0.000
101	A	131	GLN	0	-0.034	-0.001	18.392	-0.015	-0.015	0.000	0.000	0.000	0.000
102	A	132	TYR	0	0.022	0.016	19.023	-0.036	-0.036	0.000	0.000	0.000	0.000
103	A	133	GLN	0	-0.049	-0.031	20.962	-0.047	-0.047	0.000	0.000	0.000	0.000
104	A	134	GLY	0	-0.074	-0.024	23.707	-0.021	-0.021	0.000	0.000	0.000	0.000
105	A	135	VAL	0	0.040	0.013	22.085	-0.016	-0.016	0.000	0.000	0.000	0.000
106	A	136	LEU	0	0.011	0.003	24.279	-0.016	-0.016	0.000	0.000	0.000	0.000
107	A	137	ARG	1	0.909	0.984	26.883	-0.138	-0.138	0.000	0.000	0.000	0.000
108	A	138	HIS	0	-0.078	-0.058	27.773	-0.017	-0.017	0.000	0.000	0.000	0.000
109	A	139	HIS	0	0.048	0.029	29.176	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	140	ASP	-1	-0.906	-0.961	30.679	0.107	0.107	0.000	0.000	0.000	0.000
111	A	141	ARG	1	0.842	0.920	32.647	-0.095	-0.095	0.000	0.000	0.000	0.000
112	A	142	VAL	0	0.066	0.025	34.072	-0.008	-0.008	0.000	0.000	0.000	0.000
113	A	143	ARG	1	0.812	0.886	34.323	-0.082	-0.082	0.000	0.000	0.000	0.000
114	A	144	ALA	0	0.010	-0.001	36.275	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	145	LEU	0	-0.095	-0.045	38.208	-0.005	-0.005	0.000	0.000	0.000	0.000
116	A	146	ARG	1	0.842	0.918	36.833	-0.070	-0.070	0.000	0.000	0.000	0.000
117	A	147	ASP	-1	-0.878	-0.930	39.700	0.062	0.062	0.000	0.000	0.000	0.000
118	A	148	ALA	0	-0.084	-0.039	42.333	-0.003	-0.003	0.000	0.000	0.000	0.000
119	A	149	ARG	1	0.778	0.890	43.780	-0.056	-0.056	0.000	0.000	0.000	0.000
120	A	150	ALA	0	-0.061	-0.017	44.658	-0.003	-0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ASN)