FMO DATABASE

FMODB ID: R8G28

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

Total energy (hartree)

FMO2-HF: Electronic energy	-917773.684478
FMO2-HF: Nuclear repulsion	873511.126408
FMO2-HF: Total energy	-44262.558069
FMO2-MP2: Total energy	-44391.311178

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.
-37.432	-36.618	20.886	-10.919	-10.78	-0.092

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 : -0.080 / q_NPA : -0.066

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	-0.062	-0.014	1.912	-6.771	-6.759	7.946	-3.937	-4.022	-0.028
4	A	0	GLY	0	0.005	-0.006	4.969	-0.319	-0.257	-0.001	-0.005	-0.056	0.000
5	A	1	MET	0	-0.046	0.001	3.688	-0.534	0.587	0.157	-0.366	-0.913	0.003
6	A	2	LYS	1	0.894	0.929	7.919	0.729	0.729	0.000	0.000	0.000	0.000
7	A	3	PHE	0	-0.009	-0.008	4.954	-0.344	-0.344	0.000	0.000	0.000	0.000
8	A	4	ALA	0	0.004	0.008	10.098	0.288	0.288	0.000	0.000	0.000	0.000
9	A	5	VAL	0	-0.006	-0.009	12.164	-0.179	-0.179	0.000	0.000	0.000	0.000
10	A	6	ALA	0	-0.004	0.012	14.580	0.096	0.096	0.000	0.000	0.000	0.000
11	A	7	VAL	0	-0.025	-0.016	17.727	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	8	SER	0	0.052	0.004	20.136	0.018	0.018	0.000	0.000	0.000	0.000
13	A	9	GLY	0	-0.004	0.011	23.514	0.001	0.001	0.000	0.000	0.000	0.000
14	A	10	ASP	-1	-0.980	-0.997	21.352	-0.267	-0.267	0.000	0.000	0.000	0.000
15	A	11	ARG	1	0.872	0.943	20.353	0.220	0.220	0.000	0.000	0.000	0.000
16	A	12	VAL	0	0.034	0.022	14.817	-0.020	-0.020	0.000	0.000	0.000	0.000
17	A	13	ASN	0	-0.019	-0.007	17.846	0.083	0.083	0.000	0.000	0.000	0.000
18	A	14	GLY	0	0.097	0.055	18.147	-0.080	-0.080	0.000	0.000	0.000	0.000
19	A	15	PRO	0	-0.013	0.001	17.182	0.033	0.033	0.000	0.000	0.000	0.000
20	A	16	GLY	0	-0.032	-0.031	19.186	0.022	0.022	0.000	0.000	0.000	0.000
21	A	17	GLU	-1	-0.809	-0.881	22.753	-0.277	-0.277	0.000	0.000	0.000	0.000
22	A	18	SER	0	-0.023	-0.007	20.729	0.013	0.013	0.000	0.000	0.000	0.000
23	A	19	GLU	-1	-0.820	-0.912	23.027	-0.251	-0.251	0.000	0.000	0.000	0.000
24	A	20	GLU	-1	-0.834	-0.894	21.945	-0.305	-0.305	0.000	0.000	0.000	0.000
25	A	21	VAL	0	-0.018	-0.010	17.204	-0.045	-0.045	0.000	0.000	0.000	0.000
26	A	22	GLN	0	-0.002	-0.010	17.306	0.035	0.035	0.000	0.000	0.000	0.000
27	A	23	ILE	0	0.004	0.001	14.315	-0.119	-0.119	0.000	0.000	0.000	0.000
28	A	24	TYR	0	0.025	-0.009	12.716	0.127	0.127	0.000	0.000	0.000	0.000
29	A	25	GLU	-1	-0.816	-0.891	11.370	-0.551	-0.551	0.000	0.000	0.000	0.000
30	A	26	THR	0	0.012	-0.002	7.105	0.216	0.216	0.000	0.000	0.000	0.000
31	A	27	ASP	-1	-0.807	-0.891	8.098	0.037	0.037	0.000	0.000	0.000	0.000
32	A	28	GLY	0	-0.006	-0.007	6.039	0.272	0.272	0.000	0.000	0.000	0.000
33	A	29	GLY	0	-0.015	0.001	6.611	0.263	0.263	0.000	0.000	0.000	0.000
34	A	30	ASN	0	-0.076	-0.037	10.200	-0.155	-0.155	0.000	0.000	0.000	0.000
35	A	31	VAL	0	0.006	0.004	10.946	-0.054	-0.054	0.000	0.000	0.000	0.000
36	A	32	ARG	1	0.795	0.887	12.344	0.239	0.239	0.000	0.000	0.000	0.000
37	A	33	LEU	0	0.013	0.011	15.301	-0.082	-0.082	0.000	0.000	0.000	0.000
38	A	34	ILE	0	-0.058	-0.038	15.412	0.048	0.048	0.000	0.000	0.000	0.000
39	A	35	GLU	-1	-0.819	-0.893	18.601	-0.389	-0.389	0.000	0.000	0.000	0.000
40	A	36	LYS	1	0.826	0.894	19.224	0.252	0.252	0.000	0.000	0.000	0.000
41	A	37	TYR	0	-0.040	-0.013	19.438	0.029	0.029	0.000	0.000	0.000	0.000
42	A	38	SER	0	0.016	0.017	23.086	-0.022	-0.022	0.000	0.000	0.000	0.000
43	A	39	ASN	0	0.007	-0.013	22.112	-0.027	-0.027	0.000	0.000	0.000	0.000
44	A	40	PRO	0	0.007	-0.007	22.233	0.026	0.026	0.000	0.000	0.000	0.000
45	A	41	ALA	0	-0.036	-0.005	22.509	0.028	0.028	0.000	0.000	0.000	0.000
46	A	42	LEU	0	0.020	0.020	24.586	0.024	0.024	0.000	0.000	0.000	0.000
47	A	43	ASN	0	-0.057	-0.022	27.586	0.036	0.036	0.000	0.000	0.000	0.000
48	A	44	ALA	0	-0.024	0.011	26.847	0.016	0.016	0.000	0.000	0.000	0.000
49	A	45	THR	0	0.012	0.000	28.870	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	46	ALA	0	0.016	0.002	28.963	0.006	0.006	0.000	0.000	0.000	0.000
51	A	47	ALA	0	-0.012	-0.017	24.311	-0.010	-0.010	0.000	0.000	0.000	0.000
52	A	48	ARG	1	0.820	0.879	23.325	0.239	0.239	0.000	0.000	0.000	0.000
53	A	49	GLY	0	0.062	0.021	20.513	-0.020	-0.020	0.000	0.000	0.000	0.000
54	A	50	VAL	0	0.018	-0.006	19.001	-0.058	-0.058	0.000	0.000	0.000	0.000
55	A	51	PHE	0	-0.003	0.001	19.457	-0.028	-0.028	0.000	0.000	0.000	0.000
56	A	52	MET	0	-0.015	0.036	15.424	-0.026	-0.026	0.000	0.000	0.000	0.000
57	A	53	LEU	0	0.022	0.012	13.727	-0.041	-0.041	0.000	0.000	0.000	0.000
58	A	54	LYS	1	0.793	0.872	15.770	0.347	0.347	0.000	0.000	0.000	0.000
59	A	55	SER	0	0.016	0.017	18.356	0.001	0.001	0.000	0.000	0.000	0.000
60	A	56	ALA	0	0.042	0.008	13.766	0.011	0.011	0.000	0.000	0.000	0.000
61	A	57	LEU	0	-0.022	-0.015	13.418	-0.027	-0.027	0.000	0.000	0.000	0.000
62	A	58	ASP	-1	-0.848	-0.900	15.209	-0.395	-0.395	0.000	0.000	0.000	0.000
63	A	59	HIS	1	0.767	0.871	17.351	0.515	0.515	0.000	0.000	0.000	0.000
64	A	60	GLY	0	-0.015	0.006	14.877	-0.003	-0.003	0.000	0.000	0.000	0.000
65	A	61	ALA	0	-0.027	-0.010	11.350	-0.030	-0.030	0.000	0.000	0.000	0.000
66	A	62	ASN	0	-0.032	-0.033	7.686	0.195	0.195	0.000	0.000	0.000	0.000
67	A	63	ALA	0	0.009	0.021	5.187	-0.800	-0.800	0.000	0.000	0.000	0.000
68	A	64	LEU	0	-0.002	-0.005	7.287	0.768	0.768	0.000	0.000	0.000	0.000
69	A	65	VAL	0	-0.001	0.003	9.030	-0.366	-0.366	0.000	0.000	0.000	0.000
70	A	66	LEU	0	-0.007	-0.013	11.447	0.185	0.185	0.000	0.000	0.000	0.000
71	A	67	SER	0	-0.021	-0.031	14.574	-0.047	-0.047	0.000	0.000	0.000	0.000
72	A	68	GLU	-1	-0.906	-0.945	17.248	-0.429	-0.429	0.000	0.000	0.000	0.000
73	A	69	ILE	0	0.026	-0.008	13.253	-0.078	-0.078	0.000	0.000	0.000	0.000
74	A	70	GLY	0	0.056	0.054	16.621	0.026	0.026	0.000	0.000	0.000	0.000
75	A	71	SER	0	-0.026	-0.048	18.262	-0.061	-0.061	0.000	0.000	0.000	0.000
76	A	72	PRO	0	-0.019	-0.020	18.492	-0.024	-0.024	0.000	0.000	0.000	0.000
77	A	73	GLY	0	0.013	0.003	17.599	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	74	PHE	0	0.052	0.011	11.031	-0.024	-0.024	0.000	0.000	0.000	0.000
79	A	75	ASN	0	-0.006	-0.011	13.968	-0.051	-0.051	0.000	0.000	0.000	0.000
80	A	76	PHE	0	-0.031	0.002	16.049	0.031	0.031	0.000	0.000	0.000	0.000
81	A	77	ILE	0	-0.004	-0.015	11.139	0.035	0.035	0.000	0.000	0.000	0.000
82	A	78	LYS	1	0.941	0.980	9.874	0.303	0.303	0.000	0.000	0.000	0.000
83	A	79	ASN	0	-0.059	-0.030	9.408	-0.053	-0.053	0.000	0.000	0.000	0.000
84	A	80	LYS	1	0.861	0.935	10.359	0.692	0.692	0.000	0.000	0.000	0.000
85	A	81	MET	0	0.000	0.013	6.970	0.127	0.127	0.000	0.000	0.000	0.000
86	A	82	ASP	-1	-0.760	-0.826	1.724	-33.155	-35.775	12.090	-5.524	-3.945	-0.062
87	A	83	VAL	0	-0.031	-0.031	5.277	0.770	0.794	-0.001	-0.001	-0.021	0.000
88	A	84	TYR	0	-0.028	-0.033	2.482	0.978	2.918	0.695	-1.048	-1.586	-0.005
89	A	85	ILE	0	-0.027	-0.017	8.986	0.231	0.231	0.000	0.000	0.000	0.000
90	A	86	VAL	0	-0.001	-0.002	11.939	0.061	0.061	0.000	0.000	0.000	0.000
91	A	87	PRO	0	0.029	-0.002	14.635	0.027	0.027	0.000	0.000	0.000	0.000
92	A	88	GLU	-1	-0.786	-0.855	17.720	-0.405	-0.405	0.000	0.000	0.000	0.000
93	A	89	MET	0	-0.089	-0.039	16.515	0.043	0.043	0.000	0.000	0.000	0.000
94	A	90	PRO	0	0.062	0.015	18.729	-0.050	-0.050	0.000	0.000	0.000	0.000
95	A	91	VAL	0	0.035	0.023	14.970	-0.034	-0.034	0.000	0.000	0.000	0.000
96	A	92	ALA	0	0.010	0.006	14.703	-0.066	-0.066	0.000	0.000	0.000	0.000
97	A	93	ASP	-1	-0.875	-0.942	14.396	-0.137	-0.137	0.000	0.000	0.000	0.000
98	A	94	ALA	0	-0.012	-0.012	13.360	0.010	0.010	0.000	0.000	0.000	0.000
99	A	95	LEU	0	0.005	0.003	9.854	-0.126	-0.126	0.000	0.000	0.000	0.000
100	A	96	LYS	1	0.865	0.920	9.543	-0.199	-0.199	0.000	0.000	0.000	0.000
101	A	97	LEU	0	-0.011	-0.013	10.418	0.168	0.168	0.000	0.000	0.000	0.000
102	A	98	ILE	0	-0.009	0.003	5.894	0.130	0.130	0.000	0.000	0.000	0.000
103	A	99	LEU	0	0.009	0.008	5.393	0.023	0.023	0.000	0.000	0.000	0.000
104	A	100	GLU	-1	-0.887	-0.919	6.123	1.310	1.310	0.000	0.000	0.000	0.000
105	A	101	GLY	0	-0.003	0.000	6.643	0.255	0.255	0.000	0.000	0.000	0.000
106	A	102	LYS	1	0.788	0.886	7.479	-0.667	-0.667	0.000	0.000	0.000	0.000
107	A	103	VAL	0	-0.001	0.004	8.860	-0.031	-0.031	0.000	0.000	0.000	0.000
108	A	104	SER	0	0.003	0.013	7.102	-0.180	-0.180	0.000	0.000	0.000	0.000
109	A	105	PRO	0	-0.001	-0.005	3.737	-0.112	0.163	0.000	-0.038	-0.237	0.000
110	A	106	ALA	0	-0.015	-0.003	6.523	0.696	0.696	0.000	0.000	0.000	0.000
111	A	107	THR	0	-0.003	-0.015	9.671	-0.084	-0.084	0.000	0.000	0.000	0.000
112	A	108	ALA	0	-0.024	-0.014	11.368	0.109	0.109	0.000	0.000	0.000	0.000
113	A	109	PRO	0	-0.025	0.002	13.998	-0.099	-0.099	0.000	0.000	0.000	0.000
114	A	110	THR	0	0.025	0.012	15.828	0.034	0.034	0.000	0.000	0.000	0.000
115	A	111	HIS	0	-0.057	-0.038	18.045	0.080	0.080	0.000	0.000	0.000	0.000
116	A	112	ASP	-1	-0.795	-0.906	20.646	-0.326	-0.326	0.000	0.000	0.000	0.000
117	A	113	HIS	0	-0.039	-0.005	22.891	0.036	0.036	0.000	0.000	0.000	0.000
118	A	114	GLY	0	-0.051	-0.010	25.198	0.020	0.020	0.000	0.000	0.000	0.000

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