FMO DATABASE

FMODB ID: ZV58N

Calculation Name: 2RE2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2RE2

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HJC9

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	118
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-917747.370636
FMO2-HF: Nuclear repulsion	873484.983277
FMO2-HF: Total energy	-44262.387359
FMO2-MP2: Total energy	-44391.155761

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:-3:TYR)

Summations of interaction energy for fragment #1(A:-3:TYR)

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.
-26.047	-21.213	10.943	-7.429	-8.347	-0.063

Interaction energy analysis for fragmet #1(A:-3:TYR)

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 : -0.036

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	-1	GLN	0	-0.043	0.001	1.867	-6.812	-7.568	9.604	-4.587	-4.261	-0.030
4	A	0	GLY	0	-0.012	-0.019	4.963	-0.435	-0.401	-0.001	-0.005	-0.027	0.000
5	A	1	MET	0	-0.028	0.008	3.861	-0.522	0.400	0.093	-0.283	-0.732	0.002
6	A	2	LYS	1	0.894	0.933	8.057	0.801	0.801	0.000	0.000	0.000	0.000
7	A	3	PHE	0	-0.008	-0.006	5.091	-0.217	-0.217	0.000	0.000	0.000	0.000
8	A	4	ALA	0	0.010	0.005	10.304	0.269	0.269	0.000	0.000	0.000	0.000
9	A	5	VAL	0	-0.001	-0.010	12.795	-0.146	-0.146	0.000	0.000	0.000	0.000
10	A	6	ALA	0	-0.007	0.011	14.753	0.088	0.088	0.000	0.000	0.000	0.000
11	A	7	VAL	0	-0.020	-0.013	17.860	-0.001	-0.001	0.000	0.000	0.000	0.000
12	A	8	SER	0	0.055	0.011	20.277	0.015	0.015	0.000	0.000	0.000	0.000
13	A	9	GLY	0	-0.009	0.012	23.699	0.001	0.001	0.000	0.000	0.000	0.000
14	A	10	ASP	-1	-0.978	-1.000	21.150	-0.263	-0.263	0.000	0.000	0.000	0.000
15	A	11	ARG	1	0.923	0.968	20.451	0.220	0.220	0.000	0.000	0.000	0.000
16	A	12	VAL	0	-0.001	0.002	15.089	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	13	ASN	0	0.012	0.010	18.192	0.073	0.073	0.000	0.000	0.000	0.000
18	A	14	GLY	0	0.118	0.067	18.366	-0.071	-0.071	0.000	0.000	0.000	0.000
19	A	15	PRO	0	-0.017	-0.009	17.514	0.029	0.029	0.000	0.000	0.000	0.000
20	A	16	GLY	0	-0.032	-0.042	19.463	0.021	0.021	0.000	0.000	0.000	0.000
21	A	17	GLU	-1	-0.796	-0.868	23.021	-0.253	-0.253	0.000	0.000	0.000	0.000
22	A	18	SER	0	-0.031	-0.003	20.848	0.016	0.016	0.000	0.000	0.000	0.000
23	A	19	GLU	-1	-0.828	-0.921	23.141	-0.244	-0.244	0.000	0.000	0.000	0.000
24	A	20	GLU	-1	-0.825	-0.888	22.150	-0.287	-0.287	0.000	0.000	0.000	0.000
25	A	21	VAL	0	-0.026	-0.010	17.326	-0.043	-0.043	0.000	0.000	0.000	0.000
26	A	22	GLN	0	-0.008	-0.009	17.503	0.033	0.033	0.000	0.000	0.000	0.000
27	A	23	ILE	0	0.007	0.000	14.303	-0.113	-0.113	0.000	0.000	0.000	0.000
28	A	24	TYR	0	0.014	-0.010	12.793	0.121	0.121	0.000	0.000	0.000	0.000
29	A	25	GLU	-1	-0.836	-0.897	11.744	-0.580	-0.580	0.000	0.000	0.000	0.000
30	A	26	THR	0	0.015	-0.003	7.390	0.196	0.196	0.000	0.000	0.000	0.000
31	A	27	ASP	-1	-0.826	-0.906	7.895	0.082	0.082	0.000	0.000	0.000	0.000
32	A	28	GLY	0	-0.017	-0.017	5.998	0.419	0.419	0.000	0.000	0.000	0.000
33	A	29	GLY	0	-0.002	0.008	6.729	0.192	0.192	0.000	0.000	0.000	0.000
34	A	30	ASN	0	-0.083	-0.044	10.253	-0.177	-0.177	0.000	0.000	0.000	0.000
35	A	31	VAL	0	0.001	0.008	10.942	-0.061	-0.061	0.000	0.000	0.000	0.000
36	A	32	ARG	1	0.829	0.911	12.228	0.246	0.246	0.000	0.000	0.000	0.000
37	A	33	LEU	0	0.017	0.016	15.625	-0.076	-0.076	0.000	0.000	0.000	0.000
38	A	34	ILE	0	-0.045	-0.029	15.831	0.044	0.044	0.000	0.000	0.000	0.000
39	A	35	GLU	-1	-0.831	-0.898	18.830	-0.380	-0.380	0.000	0.000	0.000	0.000
40	A	36	LYS	1	0.825	0.892	19.393	0.232	0.232	0.000	0.000	0.000	0.000
41	A	37	TYR	0	-0.037	-0.014	19.632	0.023	0.023	0.000	0.000	0.000	0.000
42	A	38	SER	0	0.014	0.017	23.269	-0.021	-0.021	0.000	0.000	0.000	0.000
43	A	39	ASN	0	0.015	-0.014	22.213	-0.024	-0.024	0.000	0.000	0.000	0.000
44	A	40	PRO	0	0.019	-0.002	22.612	0.025	0.025	0.000	0.000	0.000	0.000
45	A	41	ALA	0	-0.037	-0.003	22.970	0.025	0.025	0.000	0.000	0.000	0.000
46	A	42	LEU	0	-0.009	0.002	24.977	0.022	0.022	0.000	0.000	0.000	0.000
47	A	43	ASN	0	-0.032	-0.015	28.055	0.032	0.032	0.000	0.000	0.000	0.000
48	A	44	ALA	0	-0.051	-0.006	27.202	0.014	0.014	0.000	0.000	0.000	0.000
49	A	45	THR	0	0.031	0.015	29.161	0.002	0.002	0.000	0.000	0.000	0.000
50	A	46	ALA	0	0.010	-0.007	29.232	0.003	0.003	0.000	0.000	0.000	0.000
51	A	47	ALA	0	-0.012	-0.010	24.592	-0.011	-0.011	0.000	0.000	0.000	0.000
52	A	48	ARG	1	0.838	0.889	23.978	0.232	0.232	0.000	0.000	0.000	0.000
53	A	49	GLY	0	0.062	0.026	20.825	-0.020	-0.020	0.000	0.000	0.000	0.000
54	A	50	VAL	0	0.022	-0.002	19.488	-0.047	-0.047	0.000	0.000	0.000	0.000
55	A	51	PHE	0	0.009	0.000	20.000	-0.026	-0.026	0.000	0.000	0.000	0.000
56	A	52	MET	0	-0.029	0.030	15.894	-0.021	-0.021	0.000	0.000	0.000	0.000
57	A	53	LEU	0	0.004	0.003	14.318	-0.035	-0.035	0.000	0.000	0.000	0.000
58	A	54	LYS	1	0.802	0.879	16.510	0.334	0.334	0.000	0.000	0.000	0.000
59	A	55	SER	0	0.034	0.030	18.973	0.001	0.001	0.000	0.000	0.000	0.000
60	A	56	ALA	0	0.035	0.001	14.407	0.007	0.007	0.000	0.000	0.000	0.000
61	A	57	LEU	0	-0.022	-0.011	14.037	-0.027	-0.027	0.000	0.000	0.000	0.000
62	A	58	ASP	-1	-0.858	-0.911	15.839	-0.376	-0.376	0.000	0.000	0.000	0.000
63	A	59	HIS	1	0.752	0.857	17.870	0.477	0.477	0.000	0.000	0.000	0.000
64	A	60	GLY	0	-0.005	0.012	15.282	0.001	0.001	0.000	0.000	0.000	0.000
65	A	61	ALA	0	-0.046	-0.013	11.859	-0.053	-0.053	0.000	0.000	0.000	0.000
66	A	62	ASN	0	-0.002	-0.021	7.797	0.132	0.132	0.000	0.000	0.000	0.000
67	A	63	ALA	0	0.016	0.023	5.795	-0.556	-0.556	0.000	0.000	0.000	0.000
68	A	64	LEU	0	-0.014	-0.011	7.884	0.574	0.574	0.000	0.000	0.000	0.000
69	A	65	VAL	0	-0.015	-0.003	9.484	-0.321	-0.321	0.000	0.000	0.000	0.000
70	A	66	LEU	0	0.000	-0.014	11.687	0.175	0.175	0.000	0.000	0.000	0.000
71	A	67	SER	0	-0.010	-0.018	14.620	-0.054	-0.054	0.000	0.000	0.000	0.000
72	A	68	GLU	-1	-0.923	-0.949	17.094	-0.365	-0.365	0.000	0.000	0.000	0.000
73	A	69	ILE	0	0.004	-0.010	13.945	-0.056	-0.056	0.000	0.000	0.000	0.000
74	A	70	GLY	0	0.077	0.056	17.240	0.037	0.037	0.000	0.000	0.000	0.000
75	A	71	SER	0	0.013	-0.027	18.239	-0.059	-0.059	0.000	0.000	0.000	0.000
76	A	72	PRO	0	-0.029	-0.017	19.002	-0.023	-0.023	0.000	0.000	0.000	0.000
77	A	73	GLY	0	0.021	0.001	17.973	-0.011	-0.011	0.000	0.000	0.000	0.000
78	A	74	PHE	0	0.056	0.016	11.088	-0.023	-0.023	0.000	0.000	0.000	0.000
79	A	75	ASN	0	-0.005	-0.012	14.477	-0.045	-0.045	0.000	0.000	0.000	0.000
80	A	76	PHE	0	-0.042	-0.002	16.414	0.021	0.021	0.000	0.000	0.000	0.000
81	A	77	ILE	0	0.014	-0.015	11.585	0.039	0.039	0.000	0.000	0.000	0.000
82	A	78	LYS	1	0.919	0.980	10.788	0.317	0.317	0.000	0.000	0.000	0.000
83	A	79	ASN	0	-0.041	-0.018	9.686	-0.100	-0.100	0.000	0.000	0.000	0.000
84	A	80	LYS	1	0.863	0.934	11.011	0.622	0.622	0.000	0.000	0.000	0.000
85	A	81	MET	0	0.001	0.006	7.445	0.047	0.047	0.000	0.000	0.000	0.000
86	A	82	ASP	-1	-0.802	-0.861	2.320	-19.442	-16.630	0.921	-1.828	-1.905	-0.027
87	A	83	VAL	0	-0.024	-0.026	6.024	0.429	0.429	0.000	0.000	0.000	0.000
88	A	84	TYR	0	-0.036	-0.036	2.703	-0.667	0.954	0.327	-0.708	-1.240	-0.008
89	A	85	ILE	0	-0.034	-0.014	9.208	0.209	0.209	0.000	0.000	0.000	0.000
90	A	86	VAL	0	-0.004	-0.012	11.749	0.032	0.032	0.000	0.000	0.000	0.000
91	A	87	PRO	0	0.033	0.000	14.417	0.031	0.031	0.000	0.000	0.000	0.000
92	A	88	GLU	-1	-0.807	-0.879	17.545	-0.385	-0.385	0.000	0.000	0.000	0.000
93	A	89	MET	0	-0.106	-0.040	16.541	0.042	0.042	0.000	0.000	0.000	0.000
94	A	90	PRO	0	0.042	0.001	18.827	-0.046	-0.046	0.000	0.000	0.000	0.000
95	A	91	VAL	0	0.060	0.041	15.312	-0.033	-0.033	0.000	0.000	0.000	0.000
96	A	92	ALA	0	0.008	-0.001	14.879	-0.064	-0.064	0.000	0.000	0.000	0.000
97	A	93	ASP	-1	-0.880	-0.946	14.481	-0.141	-0.141	0.000	0.000	0.000	0.000
98	A	94	ALA	0	-0.008	-0.013	13.261	0.009	0.009	0.000	0.000	0.000	0.000
99	A	95	LEU	0	-0.010	-0.007	10.128	-0.122	-0.122	0.000	0.000	0.000	0.000
100	A	96	LYS	1	0.865	0.920	9.515	-0.225	-0.225	0.000	0.000	0.000	0.000
101	A	97	LEU	0	-0.005	-0.010	10.169	0.134	0.134	0.000	0.000	0.000	0.000
102	A	98	ILE	0	-0.016	-0.008	5.972	0.103	0.103	0.000	0.000	0.000	0.000
103	A	99	LEU	0	0.002	0.006	5.359	-0.201	-0.201	0.000	0.000	0.000	0.000
104	A	100	GLU	-1	-0.879	-0.907	5.873	1.245	1.245	0.000	0.000	0.000	0.000
105	A	101	GLY	0	-0.020	-0.010	6.318	0.317	0.317	0.000	0.000	0.000	0.000
106	A	102	LYS	1	0.803	0.896	7.181	-0.593	-0.593	0.000	0.000	0.000	0.000
107	A	103	VAL	0	0.021	0.015	8.641	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	104	SER	0	-0.008	0.006	7.241	-0.361	-0.361	0.000	0.000	0.000	0.000
109	A	105	PRO	0	0.004	-0.001	3.968	0.066	0.267	-0.001	-0.018	-0.182	0.000
110	A	106	ALA	0	-0.019	-0.003	6.796	0.576	0.576	0.000	0.000	0.000	0.000
111	A	107	THR	0	-0.017	-0.028	9.537	-0.108	-0.108	0.000	0.000	0.000	0.000
112	A	108	ALA	0	-0.018	-0.014	11.677	0.108	0.108	0.000	0.000	0.000	0.000
113	A	109	PRO	0	-0.053	-0.006	14.501	-0.084	-0.084	0.000	0.000	0.000	0.000
114	A	110	THR	0	0.030	0.009	16.086	0.028	0.028	0.000	0.000	0.000	0.000
115	A	111	HIS	0	-0.078	-0.041	18.392	0.073	0.073	0.000	0.000	0.000	0.000
116	A	112	ASP	-1	-0.833	-0.928	20.983	-0.308	-0.308	0.000	0.000	0.000	0.000
117	A	113	HIS	0	0.001	0.015	23.114	0.033	0.033	0.000	0.000	0.000	0.000
118	A	114	GLY	0	-0.040	-0.010	25.195	0.017	0.017	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-3:TYR)