FMO DATABASE

FMODB ID: 14YKZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1473160.679298
FMO2-HF: Nuclear repulsion	1414021.918264
FMO2-HF: Total energy	-59138.761034
FMO2-MP2: Total energy	-59309.977619

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.
-1.116	-0.887	7.617	-2.302	-5.544	0.002

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 : 0.013 / q_NPA : -0.004

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	0.009	0.002	3.322	-0.126	2.231	0.053	-0.871	-1.539	0.002
4	A	4	GLY	0	-0.009	-0.008	5.646	-0.245	-0.245	0.000	0.000	0.000	0.000
5	A	5	TYR	0	-0.017	-0.003	9.319	0.268	0.268	0.000	0.000	0.000	0.000
6	A	6	PHE	0	-0.017	-0.024	12.453	-0.055	-0.055	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.790	-0.886	15.653	0.110	0.110	0.000	0.000	0.000	0.000
8	A	8	GLY	0	-0.003	-0.011	19.254	-0.005	-0.005	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.050	0.059	22.668	0.000	0.000	0.000	0.000	0.000	0.000
10	A	10	CYS	0	-0.075	-0.055	26.242	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.907	-0.909	29.572	0.037	0.037	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.020	-0.024	32.636	0.000	0.000	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.938	0.971	35.224	-0.033	-0.033	0.000	0.000	0.000	0.000
14	A	14	ASN	0	0.059	0.050	30.513	0.003	0.003	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.014	-0.004	33.664	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.014	-0.018	34.676	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.011	0.014	34.328	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.047	-0.032	30.830	0.001	0.001	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.023	0.010	27.958	0.001	0.001	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.024	-0.013	26.228	0.001	0.001	0.000	0.000	0.000	0.000
21	A	21	PHE	0	0.006	0.006	20.617	0.006	0.006	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.045	0.010	20.050	-0.013	-0.013	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.047	-0.021	14.850	0.024	0.024	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.023	0.009	12.416	-0.021	-0.021	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.000	0.000	9.146	0.039	0.039	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.020	-0.015	7.757	0.106	0.106	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.013	-0.012	7.386	-0.463	-0.463	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.892	-0.944	6.877	-0.120	-0.120	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.016	-0.012	8.442	-0.053	-0.053	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.944	0.972	11.473	0.136	0.136	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.871	0.954	11.819	0.030	0.030	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.045	-0.019	12.197	0.054	0.054	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.849	-0.940	14.854	-0.054	-0.054	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.044	0.013	17.575	0.006	0.006	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.001	-0.004	19.529	0.001	0.001	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.019	0.009	21.947	0.001	0.001	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.016	0.005	24.776	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.002	-0.016	25.397	0.003	0.003	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.875	-0.959	27.080	0.060	0.060	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.934	0.985	30.751	-0.039	-0.039	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.026	-0.012	33.676	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.026	-0.025	35.151	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.015	0.020	35.145	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.041	0.011	35.711	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	ASN	0	-0.015	-0.023	32.985	0.003	0.003	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.013	0.014	31.256	0.006	0.006	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.061	-0.003	29.233	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	ASN	0	0.038	0.006	24.806	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	ASN	0	0.047	0.024	24.616	0.010	0.010	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.037	-0.007	24.097	0.009	0.009	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.022	0.016	24.483	0.005	0.005	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.798	-0.892	20.717	0.121	0.121	0.000	0.000	0.000	0.000
53	A	53	TYR	0	-0.031	-0.051	19.669	0.020	0.020	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.032	-0.021	19.887	0.008	0.008	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.046	0.026	19.165	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.048	-0.008	13.903	0.004	0.004	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.004	-0.015	15.392	0.014	0.014	0.000	0.000	0.000	0.000
58	A	58	CYS	0	-0.041	-0.012	17.137	0.001	0.001	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.003	0.027	11.094	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	60	MET	0	0.005	-0.009	11.838	0.011	0.011	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.938	-0.973	13.427	0.133	0.133	0.000	0.000	0.000	0.000
62	A	62	THR	0	-0.042	-0.035	13.959	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	63	MET	0	-0.016	-0.013	7.804	0.029	0.029	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.015	0.015	11.205	0.036	0.036	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.885	0.937	13.154	-0.107	-0.107	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.043	-0.018	11.563	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.007	0.026	11.475	0.020	0.020	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.044	-0.016	5.579	0.114	0.114	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.002	-0.018	6.070	-0.106	-0.106	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.022	0.005	4.747	-0.036	0.129	-0.001	-0.006	-0.157	0.000
71	A	71	PRO	0	-0.032	0.004	3.559	-0.506	0.256	0.018	-0.215	-0.566	-0.001
72	A	72	ILE	0	0.012	-0.003	2.731	1.519	-1.549	7.548	-1.187	-3.293	0.001
73	A	73	ILE	0	-0.011	-0.020	5.381	-0.695	-0.682	-0.001	-0.023	0.011	0.000
74	A	74	LYS	1	0.946	0.975	6.882	-1.048	-1.048	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.054	0.023	10.906	-0.093	-0.093	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.822	-0.913	14.685	0.159	0.159	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.016	-0.012	17.627	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.043	-0.004	17.517	0.035	0.035	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.055	-0.008	19.631	0.001	0.001	0.000	0.000	0.000	0.000
80	A	80	VAL	0	0.049	0.010	17.886	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	ILE	0	0.002	0.016	14.215	0.008	0.008	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.980	0.994	17.043	-0.108	-0.108	0.000	0.000	0.000	0.000
83	A	83	GLN	0	-0.044	0.013	19.138	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.041	-0.014	15.774	-0.014	-0.014	0.000	0.000	0.000	0.000
85	A	85	ASN	0	-0.065	-0.034	13.170	0.018	0.018	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.021	0.002	16.822	-0.016	-0.016	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.928	-0.958	17.455	0.121	0.121	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.080	-0.042	21.492	-0.011	-0.011	0.000	0.000	0.000	0.000
89	A	89	LYN	0	0.077	0.027	23.831	0.004	0.004	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.029	0.020	24.073	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.933	0.955	27.236	-0.065	-0.065	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.001	0.004	29.411	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.992	0.989	30.115	-0.054	-0.054	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.920	0.974	29.492	-0.060	-0.060	0.000	0.000	0.000	0.000
95	A	95	ILE	0	0.024	0.002	25.080	0.002	0.002	0.000	0.000	0.000	0.000
96	A	96	ILE	0	0.006	0.007	25.831	0.007	0.007	0.000	0.000	0.000	0.000
97	A	97	PRO	0	0.033	0.024	25.993	0.006	0.006	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.019	-0.008	23.169	0.006	0.006	0.000	0.000	0.000	0.000
99	A	99	TYR	0	0.035	0.004	20.808	0.008	0.008	0.000	0.000	0.000	0.000
100	A	100	GLU	-1	-0.916	-0.963	21.116	0.106	0.106	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.955	0.988	20.557	-0.101	-0.101	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.015	-0.003	17.528	0.012	0.012	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.003	-0.003	16.649	0.030	0.030	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.914	-0.963	17.244	0.162	0.162	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.043	-0.017	15.045	0.013	0.013	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.969	0.986	12.355	-0.305	-0.305	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.906	0.954	12.420	-0.114	-0.114	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.934	0.970	13.939	-0.166	-0.166	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.009	0.001	9.552	0.020	0.020	0.000	0.000	0.000	0.000
110	A	110	ASN	0	-0.039	-0.013	8.347	0.036	0.036	0.000	0.000	0.000	0.000
111	A	111	ALA	0	-0.009	0.006	7.589	0.075	0.075	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.020	-0.009	6.838	-0.268	-0.268	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.026	-0.018	8.475	0.215	0.215	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.008	-0.006	6.540	-0.049	-0.049	0.000	0.000	0.000	0.000
115	A	115	TRP	0	-0.028	-0.028	10.931	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.030	-0.013	11.672	0.034	0.034	0.000	0.000	0.000	0.000
117	A	117	PRO	0	0.029	0.031	14.543	-0.024	-0.024	0.000	0.000	0.000	0.000
118	A	118	ARG	1	1.054	1.014	17.452	-0.052	-0.052	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.981	-0.996	19.129	0.061	0.061	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.924	-0.981	13.833	0.180	0.180	0.000	0.000	0.000	0.000
121	A	121	ASN	0	-0.017	-0.022	14.854	0.029	0.029	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.959	0.970	16.716	-0.031	-0.031	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.810	-0.899	15.311	-0.071	-0.071	0.000	0.000	0.000	0.000
124	A	124	ALA	0	0.013	0.007	16.051	-0.009	-0.009	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.838	-0.907	17.924	0.042	0.042	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.874	0.940	19.527	0.016	0.016	0.000	0.000	0.000	0.000
127	A	127	LEU	0	-0.048	-0.021	18.001	-0.003	-0.003	0.000	0.000	0.000	0.000
128	A	128	SER	0	0.010	-0.015	21.975	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.911	0.959	23.708	-0.032	-0.032	0.000	0.000	0.000	0.000
130	A	130	VAL	0	-0.020	0.010	24.430	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	131	ALA	0	0.022	0.008	25.623	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	132	TYR	0	-0.020	-0.008	27.395	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.868	-0.957	29.784	0.018	0.018	0.000	0.000	0.000	0.000
134	A	134	LEU	0	-0.060	-0.029	28.304	-0.002	-0.002	0.000	0.000	0.000	0.000
135	A	135	VAL	0	-0.006	0.002	30.603	0.000	0.000	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.893	0.963	33.154	-0.021	-0.021	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.894	0.950	35.219	-0.016	-0.016	0.000	0.000	0.000	0.000
138	A	138	GLY	0	-0.007	0.004	36.342	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.868	0.929	33.456	-0.015	-0.015	0.000	0.000	0.000	0.000
140	A	140	LEU	0	0.027	0.018	27.388	0.000	0.000	0.000	0.000	0.000	0.000
141	A	141	ARG	1	0.928	0.956	31.980	-0.030	-0.030	0.000	0.000	0.000	0.000
142	A	142	ASP	-1	-0.898	-0.930	30.729	0.042	0.042	0.000	0.000	0.000	0.000
143	A	143	ILE	0	-0.053	-0.015	27.600	0.000	0.000	0.000	0.000	0.000	0.000
144	A	144	GLY	0	0.021	0.004	25.492	0.001	0.001	0.000	0.000	0.000	0.000
145	A	146	ILE	0	0.005	0.010	22.395	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	147	ILE	0	-0.015	-0.008	17.455	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.028	-0.006	20.450	0.002	0.002	0.000	0.000	0.000	0.000
148	A	149	THR	0	-0.007	-0.005	20.197	-0.006	-0.006	0.000	0.000	0.000	0.000

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