FMO DATABASE

FMODB ID: KR653

Calculation Name: 2EHG-A-Xray310

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	148
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1472908.10773
FMO2-HF: Nuclear repulsion	1413769.847564
FMO2-HF: Total energy	-59138.260166
FMO2-MP2: Total energy	-59309.467166

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.
-0.994	-0.799	7.63	-2.304	-5.52	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 : 0.009 / q_NPA : -0.006

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	0.000	-0.001	3.322	-0.021	2.291	0.058	-0.855	-1.514	0.002
4	A	4	GLY	0	0.002	-0.002	5.646	-0.221	-0.221	0.000	0.000	0.000	0.000
5	A	5	TYR	0	-0.023	-0.005	9.319	0.272	0.272	0.000	0.000	0.000	0.000
6	A	6	PHE	0	-0.015	-0.022	12.453	-0.054	-0.054	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.791	-0.886	15.653	0.105	0.105	0.000	0.000	0.000	0.000
8	A	8	GLY	0	-0.004	-0.011	19.254	-0.006	-0.006	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.049	0.058	22.668	0.000	0.000	0.000	0.000	0.000	0.000
10	A	10	CYS	0	-0.078	-0.056	26.242	-0.001	-0.001	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.910	-0.911	29.572	0.035	0.035	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.018	-0.023	32.636	0.000	0.000	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.935	0.969	35.224	-0.032	-0.032	0.000	0.000	0.000	0.000
14	A	14	ASN	0	0.058	0.050	30.513	0.003	0.003	0.000	0.000	0.000	0.000
15	A	15	PRO	0	0.017	-0.005	33.664	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.009	-0.018	34.676	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	17	GLY	0	-0.009	0.015	34.328	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	18	ILE	0	-0.045	-0.032	30.830	0.001	0.001	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.024	0.010	27.959	0.001	0.001	0.000	0.000	0.000	0.000
20	A	20	THR	0	-0.029	-0.013	26.228	0.001	0.001	0.000	0.000	0.000	0.000
21	A	21	PHE	0	0.015	0.008	20.617	0.006	0.006	0.000	0.000	0.000	0.000
22	A	22	GLY	0	0.040	0.010	20.050	-0.012	-0.012	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.039	-0.020	14.850	0.024	0.024	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.017	0.010	12.416	-0.020	-0.020	0.000	0.000	0.000	0.000
25	A	25	ILE	0	0.000	-0.001	9.146	0.034	0.034	0.000	0.000	0.000	0.000
26	A	26	TYR	0	-0.021	-0.015	7.757	0.102	0.102	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.010	-0.010	7.386	-0.481	-0.481	0.000	0.000	0.000	0.000
28	A	28	ASP	-1	-0.904	-0.949	6.888	-0.112	-0.112	0.000	0.000	0.000	0.000
29	A	29	ASN	0	-0.025	-0.017	8.452	-0.053	-0.053	0.000	0.000	0.000	0.000
30	A	30	ARG	1	0.940	0.971	11.483	0.135	0.135	0.000	0.000	0.000	0.000
31	A	31	LYS	1	0.863	0.949	11.829	0.032	0.032	0.000	0.000	0.000	0.000
32	A	32	ILE	0	-0.020	-0.005	12.198	0.053	0.053	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.849	-0.941	14.854	-0.059	-0.059	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.054	0.019	17.575	0.008	0.008	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.009	-0.009	19.529	0.002	0.002	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.027	0.013	21.947	0.001	0.001	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.027	0.000	24.776	0.000	0.000	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.006	-0.015	25.397	0.003	0.003	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.879	-0.962	27.080	0.058	0.058	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.935	0.985	30.751	-0.038	-0.038	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.025	-0.012	33.676	0.000	0.000	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.025	-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	0.039	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	-0.015	0.013	31.256	0.006	0.006	0.000	0.000	0.000	0.000
47	A	47	THR	0	0.059	-0.006	29.233	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	48	ASN	0	0.041	0.007	24.806	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	49	ASN	0	0.045	0.024	24.616	0.009	0.009	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.035	-0.007	24.097	0.009	0.009	0.000	0.000	0.000	0.000
51	A	51	ALA	0	0.019	0.016	24.483	0.005	0.005	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.791	-0.890	20.717	0.117	0.117	0.000	0.000	0.000	0.000
53	A	53	TYR	0	-0.038	-0.054	19.669	0.019	0.019	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.032	-0.022	19.887	0.008	0.008	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.051	0.029	19.165	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.044	-0.007	13.903	0.004	0.004	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.010	-0.018	15.392	0.013	0.013	0.000	0.000	0.000	0.000
58	A	145	CYS	0	-0.046	-0.014	17.137	0.001	0.001	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.001	0.030	11.094	-0.007	-0.007	0.000	0.000	0.000	0.000
60	A	60	MET	0	-0.003	-0.013	11.838	0.012	0.012	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.936	-0.974	13.427	0.128	0.128	0.000	0.000	0.000	0.000
62	A	62	THR	0	-0.042	-0.033	13.959	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	63	MET	0	-0.007	-0.010	7.802	0.032	0.032	0.000	0.000	0.000	0.000
64	A	64	LEU	0	0.007	0.011	11.205	0.038	0.038	0.000	0.000	0.000	0.000
65	A	65	ARG	1	0.885	0.938	13.154	-0.103	-0.103	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.035	-0.012	11.563	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	67	GLY	0	0.004	0.025	11.475	0.024	0.024	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.042	-0.015	5.579	0.119	0.119	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.004	-0.020	6.070	-0.100	-0.100	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.026	0.003	4.747	-0.040	0.125	0.000	-0.008	-0.157	0.000
71	A	71	PRO	0	-0.031	0.005	3.559	-0.519	0.250	0.019	-0.219	-0.570	-0.001
72	A	72	ILE	0	0.009	-0.005	2.731	1.568	-1.501	7.553	-1.199	-3.284	0.001
73	A	73	ILE	0	-0.006	-0.017	5.381	-0.726	-0.708	0.000	-0.023	0.005	0.000
74	A	74	LYS	1	0.942	0.974	6.882	-1.026	-1.026	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.061	0.025	10.906	-0.098	-0.098	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.826	-0.914	14.685	0.153	0.153	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.015	-0.012	17.627	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	78	GLN	0	0.041	-0.005	17.517	0.035	0.035	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.057	-0.008	19.631	0.001	0.001	0.000	0.000	0.000	0.000
80	A	80	VAL	0	0.054	0.011	17.886	0.000	0.000	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.003	0.015	14.216	0.008	0.008	0.000	0.000	0.000	0.000
82	A	82	LYS	1	0.981	0.994	17.043	-0.108	-0.108	0.000	0.000	0.000	0.000
83	A	83	GLN	0	-0.045	0.012	19.138	-0.007	-0.007	0.000	0.000	0.000	0.000
84	A	84	MET	0	-0.040	-0.013	15.773	-0.014	-0.014	0.000	0.000	0.000	0.000
85	A	85	ASN	0	-0.065	-0.033	13.170	0.017	0.017	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.022	0.002	16.822	-0.017	-0.017	0.000	0.000	0.000	0.000
87	A	87	GLU	-1	-0.929	-0.959	17.455	0.120	0.120	0.000	0.000	0.000	0.000
88	A	88	TYR	0	-0.079	-0.041	21.492	-0.012	-0.012	0.000	0.000	0.000	0.000
89	A	89	LYN	0	0.072	0.025	23.831	0.004	0.004	0.000	0.000	0.000	0.000
90	A	90	VAL	0	0.032	0.022	24.073	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.932	0.953	27.236	-0.064	-0.064	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.003	0.004	29.410	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.992	0.990	30.115	-0.053	-0.053	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.920	0.974	29.492	-0.058	-0.058	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	0.002	0.006	25.831	0.007	0.007	0.000	0.000	0.000	0.000
97	A	97	PRO	0	0.036	0.025	25.993	0.006	0.006	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.018	-0.007	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	-0.921	-0.964	21.116	0.104	0.104	0.000	0.000	0.000	0.000
101	A	101	LYS	1	0.958	0.989	20.557	-0.098	-0.098	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.018	-0.002	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	-0.919	-0.965	17.244	0.159	0.159	0.000	0.000	0.000	0.000
105	A	105	LEU	0	-0.043	-0.017	15.044	0.014	0.014	0.000	0.000	0.000	0.000
106	A	106	LYS	1	0.973	0.988	12.355	-0.301	-0.301	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.904	0.954	12.420	-0.113	-0.113	0.000	0.000	0.000	0.000
108	A	108	LYS	1	0.931	0.969	13.939	-0.163	-0.163	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.011	0.001	9.552	0.022	0.022	0.000	0.000	0.000	0.000
110	A	110	ASN	0	-0.035	-0.013	8.347	0.035	0.035	0.000	0.000	0.000	0.000
111	A	111	ALA	0	-0.009	0.007	7.589	0.077	0.077	0.000	0.000	0.000	0.000
112	A	112	THR	0	-0.023	-0.011	6.838	-0.261	-0.261	0.000	0.000	0.000	0.000
113	A	113	LEU	0	-0.027	-0.017	8.475	0.208	0.208	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.009	-0.007	6.539	-0.050	-0.050	0.000	0.000	0.000	0.000
115	A	115	TRP	0	-0.031	-0.029	10.931	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	116	VAL	0	-0.030	-0.012	11.673	0.033	0.033	0.000	0.000	0.000	0.000
117	A	117	PRO	0	0.027	0.030	14.543	-0.026	-0.026	0.000	0.000	0.000	0.000
118	A	118	ARG	1	1.054	1.014	17.452	-0.051	-0.051	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.980	-0.995	19.129	0.058	0.058	0.000	0.000	0.000	0.000
120	A	120	GLU	-1	-0.928	-0.983	13.833	0.174	0.174	0.000	0.000	0.000	0.000
121	A	121	ASN	0	-0.016	-0.022	14.854	0.027	0.027	0.000	0.000	0.000	0.000
122	A	122	LYS	1	0.958	0.968	16.716	-0.028	-0.028	0.000	0.000	0.000	0.000
123	A	123	GLU	-1	-0.809	-0.898	15.310	-0.077	-0.077	0.000	0.000	0.000	0.000
124	A	124	ALA	0	0.017	0.009	16.051	-0.008	-0.008	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.843	-0.910	17.924	0.039	0.039	0.000	0.000	0.000	0.000
126	A	126	ARG	1	0.873	0.939	19.528	0.021	0.021	0.000	0.000	0.000	0.000
127	A	127	LEU	0	-0.041	-0.017	18.001	-0.002	-0.002	0.000	0.000	0.000	0.000
128	A	128	SER	0	0.010	-0.016	21.975	0.000	0.000	0.000	0.000	0.000	0.000
129	A	129	ARG	1	0.906	0.957	23.708	-0.029	-0.029	0.000	0.000	0.000	0.000
130	A	130	VAL	0	-0.015	0.013	24.426	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	131	ALA	0	0.023	0.009	25.623	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	132	TYR	0	-0.023	-0.010	27.395	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	133	GLU	-1	-0.870	-0.958	29.784	0.016	0.016	0.000	0.000	0.000	0.000
134	A	134	LEU	0	-0.058	-0.028	28.304	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	135	VAL	0	-0.007	0.002	30.603	0.000	0.000	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.890	0.962	33.154	-0.020	-0.020	0.000	0.000	0.000	0.000
137	A	137	ARG	1	0.892	0.949	35.219	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	138	GLY	0	-0.008	0.003	36.342	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.867	0.929	33.456	-0.013	-0.013	0.000	0.000	0.000	0.000
140	A	140	LEU	0	0.030	0.021	27.388	0.000	0.000	0.000	0.000	0.000	0.000
141	A	141	ARG	1	0.925	0.955	31.980	-0.028	-0.028	0.000	0.000	0.000	0.000
142	A	142	ASP	-1	-0.899	-0.932	30.729	0.040	0.040	0.000	0.000	0.000	0.000
143	A	143	ILE	0	-0.056	-0.016	27.599	0.000	0.000	0.000	0.000	0.000	0.000
144	A	144	GLY	0	0.021	0.004	25.492	0.002	0.002	0.000	0.000	0.000	0.000
145	A	146	ILE	0	0.004	0.007	22.395	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	147	ILE	0	-0.029	-0.018	17.456	0.000	0.000	0.000	0.000	0.000	0.000
147	A	148	LEU	0	-0.063	-0.026	20.439	0.003	0.003	0.000	0.000	0.000	0.000
148	A	149	THR	-1	-0.915	-0.956	20.197	-0.024	-0.024	0.000	0.000	0.000	0.000

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