FMO DATABASE

FMODB ID: GNRG1

Calculation Name: 2EHG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EHG

Chain ID: A

ChEMBL ID:

UniProt ID: F9VN79

Base Structure: X-ray

Registration Date: 2023-03-13

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	148
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1474022.405244
FMO2-HF: Nuclear repulsion	1414882.800303
FMO2-HF: Total energy	-59139.604941
FMO2-MP2: Total energy	-59310.811583

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:1:MET)

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

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.
-4.111	-0.833	3.942	-2.256	-4.965	0.008

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.030 / q_NPA : 0.022

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	3	ILE	0	0.018	0.004	3.544	-0.677	2.425	0.006	-1.383	-1.725	0.007
4	A	4	GLY	0	-0.005	-0.006	5.710	-0.324	-0.324	0.000	0.000	0.000	0.000
5	A	5	TYR	0	-0.011	-0.004	9.340	0.348	0.348	0.000	0.000	0.000	0.000
6	A	6	PHE	0	-0.011	-0.017	12.500	-0.090	-0.090	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.797	-0.867	15.689	0.085	0.085	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.020	-0.002	19.287	-0.022	-0.022	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.006	0.029	22.702	0.011	0.011	0.000	0.000	0.000	0.000
10	A	10	CYS	0	-0.056	-0.042	26.284	-0.007	-0.007	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.901	-0.901	29.779	0.014	0.014	0.000	0.000	0.000	0.000
12	A	12	PRO	0	0.015	-0.007	32.718	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.925	0.962	35.294	-0.013	-0.013	0.000	0.000	0.000	0.000
14	A	14	ASN	0	0.061	0.056	31.159	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.014	-0.004	33.679	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.012	-0.021	34.705	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.010	0.013	34.358	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.039	-0.030	31.097	-0.002	-0.002	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.016	0.012	28.124	0.003	0.003	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.013	-0.008	26.247	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	21	PHE	0	-0.003	-0.001	20.615	0.013	0.013	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.049	0.014	20.096	-0.019	-0.019	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.053	-0.025	14.854	0.036	0.036	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.011	0.004	12.710	-0.026	-0.026	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.003	0.001	9.099	0.049	0.049	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.043	-0.037	7.897	0.133	0.133	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.018	-0.011	7.491	-0.628	-0.628	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.883	-0.939	6.840	-2.190	-2.190	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.022	-0.019	8.497	0.286	0.286	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.955	0.979	11.592	0.718	0.718	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.821	0.911	11.971	0.166	0.166	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.044	-0.019	12.610	0.096	0.096	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.756	-0.867	14.947	-0.230	-0.230	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.050	0.017	17.667	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.002	-0.004	19.586	0.016	0.016	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.021	0.007	22.000	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.010	0.006	24.828	0.010	0.010	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.004	-0.013	25.562	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.843	-0.937	27.126	0.011	0.011	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.950	0.986	30.796	0.004	0.004	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.031	-0.010	33.807	0.005	0.005	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.026	-0.023	35.195	0.000	0.000	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.023	0.022	35.095	0.002	0.002	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.028	-0.001	35.748	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.021	-0.022	33.036	0.007	0.007	0.000	0.000	0.000	0.000
46	A	46	SER	0	0.000	0.018	31.287	0.003	0.003	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.035	-0.012	29.278	0.005	0.005	0.000	0.000	0.000	0.000
48	A	48	ASN	0	0.042	0.006	24.992	-0.013	-0.013	0.000	0.000	0.000	0.000
49	A	49	ASN	0	0.045	0.020	24.650	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.026	-0.004	24.126	0.005	0.005	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.018	0.021	24.520	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.789	-0.880	20.757	0.104	0.104	0.000	0.000	0.000	0.000
53	A	53	TYR	0	-0.029	-0.041	19.702	0.010	0.010	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.030	-0.022	19.924	-0.006	-0.006	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.040	0.023	19.209	-0.019	-0.019	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.045	-0.009	13.965	-0.024	-0.024	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.003	-0.012	15.436	-0.015	-0.015	0.000	0.000	0.000	0.000
58	A	58	CYS	0	-0.076	-0.031	17.187	-0.016	-0.016	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.006	0.032	11.143	-0.046	-0.046	0.000	0.000	0.000	0.000
60	A	60	MET	0	0.011	-0.001	11.834	-0.046	-0.046	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.839	-0.903	13.478	-0.092	-0.092	0.000	0.000	0.000	0.000
62	A	62	THR	0	-0.046	-0.037	14.023	-0.018	-0.018	0.000	0.000	0.000	0.000
63	A	63	MET	0	-0.010	-0.009	7.756	0.002	0.002	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.020	0.015	11.216	-0.040	-0.040	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.833	0.901	13.166	0.131	0.131	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.042	-0.017	11.605	0.003	0.003	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.009	0.026	11.478	-0.043	-0.043	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.055	-0.023	5.645	-0.030	-0.030	0.000	0.000	0.000	0.000
69	A	69	SER	0	0.003	-0.013	6.077	0.223	0.223	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.029	-0.002	4.756	-0.230	-0.066	-0.001	-0.006	-0.156	0.000
71	A	71	PRO	0	-0.020	0.010	3.607	-0.443	0.273	0.016	-0.199	-0.534	-0.001
72	A	72	ILE	0	0.006	-0.010	2.898	0.216	-0.483	3.922	-0.660	-2.564	0.002
73	A	73	ILE	0	-0.022	-0.022	5.394	-0.715	-0.720	-0.001	-0.008	0.014	0.000
74	A	74	LYS	1	0.873	0.939	7.940	-0.813	-0.813	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.051	0.018	11.231	-0.145	-0.145	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.796	-0.893	15.005	0.198	0.198	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.025	-0.023	17.909	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.035	-0.001	18.049	0.036	0.036	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.030	-0.001	19.878	0.005	0.005	0.000	0.000	0.000	0.000
80	A	80	VAL	0	0.036	0.005	17.998	0.002	0.002	0.000	0.000	0.000	0.000
81	A	81	ILE	0	0.002	0.008	14.250	0.005	0.005	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.849	0.909	17.270	-0.250	-0.250	0.000	0.000	0.000	0.000
83	A	83	GLN	0	-0.050	-0.001	19.360	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.046	-0.016	15.773	-0.020	-0.020	0.000	0.000	0.000	0.000
85	A	85	ASN	0	-0.065	-0.040	13.203	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.015	0.007	16.883	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.815	-0.881	18.144	0.261	0.261	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.062	-0.032	21.603	-0.015	-0.015	0.000	0.000	0.000	0.000
89	A	89	LYN	0	0.106	0.062	23.939	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.031	0.020	24.043	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.911	0.926	27.247	-0.088	-0.088	0.000	0.000	0.000	0.000
92	A	92	ALA	0	0.003	0.005	29.478	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.975	0.980	30.137	-0.050	-0.050	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.914	0.968	29.713	-0.020	-0.020	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.017	-0.001	25.080	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	96	ILE	0	-0.016	0.003	25.858	0.003	0.003	0.000	0.000	0.000	0.000
97	A	97	PRO	0	0.065	0.036	26.019	0.004	0.004	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.022	-0.007	23.255	-0.002	-0.002	0.000	0.000	0.000	0.000
99	A	99	TYR	0	0.032	-0.001	20.797	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.907	-0.958	21.140	0.070	0.070	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.879	0.938	20.973	0.017	0.017	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.020	-0.003	17.618	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.017	0.004	16.678	0.019	0.019	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.826	-0.901	17.266	0.086	0.086	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.023	-0.008	15.141	-0.004	-0.004	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.943	0.964	11.935	-0.409	-0.409	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.843	0.919	12.440	-0.079	-0.079	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.855	0.921	13.958	-0.031	-0.031	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.005	0.007	9.586	-0.015	-0.015	0.000	0.000	0.000	0.000
110	A	110	ASN	0	-0.040	-0.015	8.487	0.017	0.017	0.000	0.000	0.000	0.000
111	A	111	ALA	0	0.004	0.019	7.606	0.093	0.093	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.008	0.003	6.843	-0.181	-0.181	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.020	-0.013	8.500	0.165	0.165	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.006	-0.008	6.786	-0.014	-0.014	0.000	0.000	0.000	0.000
115	A	115	TRP	0	-0.026	-0.025	11.193	-0.040	-0.040	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.032	-0.009	11.844	0.073	0.073	0.000	0.000	0.000	0.000
117	A	117	PRO	0	0.038	0.026	14.754	-0.052	-0.052	0.000	0.000	0.000	0.000
118	A	118	ARG	1	0.991	0.983	17.685	-0.067	-0.067	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.982	-0.997	19.429	0.130	0.130	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.836	-0.938	12.352	0.496	0.496	0.000	0.000	0.000	0.000
121	A	121	ASN	0	-0.029	-0.041	14.944	-0.003	-0.003	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.956	0.974	16.805	-0.075	-0.075	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.749	-0.828	15.536	-0.256	-0.256	0.000	0.000	0.000	0.000
124	A	124	ALA	0	0.026	0.013	16.046	-0.023	-0.023	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.755	-0.829	17.981	0.007	0.007	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.788	0.863	18.919	0.158	0.158	0.000	0.000	0.000	0.000
127	A	127	LEU	0	-0.063	-0.028	18.147	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	128	SER	0	0.001	-0.037	22.033	-0.008	-0.008	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.851	0.899	23.768	0.008	0.008	0.000	0.000	0.000	0.000
130	A	130	VAL	0	-0.025	0.008	24.988	0.000	0.000	0.000	0.000	0.000	0.000
131	A	131	ALA	0	0.020	0.010	25.667	0.001	0.001	0.000	0.000	0.000	0.000
132	A	132	TYR	0	-0.038	-0.018	27.454	0.003	0.003	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.803	-0.905	29.847	-0.028	-0.028	0.000	0.000	0.000	0.000
134	A	134	LEU	0	-0.057	-0.026	28.387	0.001	0.001	0.000	0.000	0.000	0.000
135	A	135	VAL	0	-0.009	-0.002	30.604	0.002	0.002	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.830	0.916	33.204	0.025	0.025	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.878	0.947	35.293	0.044	0.044	0.000	0.000	0.000	0.000
138	A	138	GLY	0	0.000	0.003	36.385	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.876	0.932	33.444	0.063	0.063	0.000	0.000	0.000	0.000
140	A	140	LEU	0	0.009	0.012	27.436	-0.006	-0.006	0.000	0.000	0.000	0.000
141	A	141	ARG	1	0.934	0.959	32.035	0.052	0.052	0.000	0.000	0.000	0.000
142	A	142	ASP	-1	-0.893	-0.932	30.811	-0.046	-0.046	0.000	0.000	0.000	0.000
143	A	143	ILE	0	-0.044	-0.014	27.672	-0.003	-0.003	0.000	0.000	0.000	0.000
144	A	144	GLY	0	0.028	0.008	25.547	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	146	ILE	0	0.010	0.012	22.444	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	147	ILE	0	-0.011	-0.007	17.817	-0.008	-0.008	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.024	-0.002	20.473	0.014	0.014	0.000	0.000	0.000	0.000
148	A	149	THR	0	-0.003	-0.003	20.205	-0.026	-0.026	0.000	0.000	0.000	0.000

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