FMO DATABASE

FMODB ID: Q836Y

Calculation Name: 2EJX-A-Xray310

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EJX

Chain ID: A

ChEMBL ID:

UniProt ID: Q973T5

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	135
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1270185.189886
FMO2-HF: Nuclear repulsion	1216817.112303
FMO2-HF: Total energy	-53368.077583
FMO2-MP2: Total energy	-53526.98468

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:2:ACE )

Summations of interaction energy for fragment #1(A:2:ACE )

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.
-2.396	-1.532	-0.006	-0.38	-0.477	0

Interaction energy analysis for fragmet #1(A:2:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.023 / 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].
3	A	4	VAL	0	-0.066	-0.022	3.858	1.346	2.091	-0.006	-0.353	-0.386
4	A	5	GLU	-1	-0.879	-0.949	7.178	-0.864	-0.864	0.000	0.000	0.000
5	A	6	LYS	1	0.845	0.925	10.085	0.305	0.305	0.000	0.000	0.000
6	A	7	GLU	-1	-0.855	-0.874	13.725	-0.202	-0.202	0.000	0.000	0.000
7	A	8	ILE	0	-0.003	-0.015	16.621	0.021	0.021	0.000	0.000	0.000
8	A	9	LYS	1	0.885	0.934	19.850	0.130	0.130	0.000	0.000	0.000
9	A	10	THR	0	-0.023	-0.036	23.282	0.003	0.003	0.000	0.000	0.000
10	A	11	ASN	0	0.000	-0.013	26.201	0.001	0.001	0.000	0.000	0.000
11	A	12	GLN	0	-0.042	-0.007	28.472	0.008	0.008	0.000	0.000	0.000
12	A	13	ASP	-1	-0.852	-0.922	29.298	-0.110	-0.110	0.000	0.000	0.000
13	A	14	ILE	0	0.040	0.006	23.462	-0.008	-0.008	0.000	0.000	0.000
14	A	15	ASP	-1	-0.852	-0.925	26.118	-0.145	-0.145	0.000	0.000	0.000
15	A	16	VAL	0	-0.040	-0.022	27.692	-0.007	-0.007	0.000	0.000	0.000
16	A	17	VAL	0	-0.002	-0.009	23.435	-0.008	-0.008	0.000	0.000	0.000
17	A	18	MET	0	-0.027	-0.007	20.158	-0.020	-0.020	0.000	0.000	0.000
18	A	19	THR	0	-0.010	-0.009	23.591	-0.012	-0.012	0.000	0.000	0.000
19	A	20	ILE	0	-0.028	0.013	24.996	-0.001	-0.001	0.000	0.000	0.000
20	A	21	PHE	0	0.024	0.008	19.075	-0.010	-0.010	0.000	0.000	0.000
21	A	22	SER	0	-0.102	-0.038	20.986	-0.020	-0.020	0.000	0.000	0.000
22	A	23	ASP	-1	-0.741	-0.868	22.851	-0.140	-0.140	0.000	0.000	0.000
23	A	24	PRO	0	0.017	0.015	21.448	-0.011	-0.011	0.000	0.000	0.000
24	A	25	ALA	0	0.008	-0.027	22.294	-0.004	-0.004	0.000	0.000	0.000
25	A	26	PHE	0	-0.046	-0.013	22.039	0.012	0.012	0.000	0.000	0.000
26	A	27	THR	0	0.000	-0.059	17.669	0.002	0.002	0.000	0.000	0.000
27	A	28	ILE	0	-0.010	0.003	17.221	-0.024	-0.024	0.000	0.000	0.000
28	A	29	PRO	0	-0.010	-0.017	18.671	-0.006	-0.006	0.000	0.000	0.000
29	A	30	GLN	0	0.031	0.035	20.241	0.003	0.003	0.000	0.000	0.000
30	A	31	ILE	0	0.008	0.009	13.832	-0.007	-0.007	0.000	0.000	0.000
31	A	32	PHE	0	-0.011	0.000	13.406	-0.021	-0.021	0.000	0.000	0.000
32	A	33	PRO	0	-0.006	-0.006	13.745	0.036	0.036	0.000	0.000	0.000
33	A	34	GLY	0	0.026	0.041	16.611	0.010	0.010	0.000	0.000	0.000
34	A	35	ILE	0	-0.033	-0.005	18.500	0.011	0.011	0.000	0.000	0.000
35	A	36	ALA	0	0.011	-0.003	21.517	0.008	0.008	0.000	0.000	0.000
36	A	37	SER	0	-0.073	-0.031	24.390	0.012	0.012	0.000	0.000	0.000
37	A	38	ILE	0	0.033	0.004	22.564	-0.013	-0.013	0.000	0.000	0.000
38	A	39	LYS	1	0.896	0.971	25.580	0.103	0.103	0.000	0.000	0.000
39	A	40	CYS	0	-0.019	-0.018	25.744	-0.012	-0.012	0.000	0.000	0.000
40	A	41	ILE	0	-0.006	-0.012	28.026	0.005	0.005	0.000	0.000	0.000
41	A	42	GLU	-1	-0.839	-0.913	28.969	-0.107	-0.107	0.000	0.000	0.000
42	A	43	PRO	0	0.012	0.006	28.281	-0.008	-0.008	0.000	0.000	0.000
43	A	44	GLU	-1	-0.901	-0.945	24.726	-0.171	-0.171	0.000	0.000	0.000
44	A	45	ILE	0	-0.049	-0.014	23.794	-0.017	-0.017	0.000	0.000	0.000
45	A	46	PHE	0	0.017	0.003	17.817	0.006	0.006	0.000	0.000	0.000
46	A	47	GLU	-1	-0.924	-0.977	22.684	-0.113	-0.113	0.000	0.000	0.000
47	A	48	ALA	0	-0.014	-0.015	20.529	0.005	0.005	0.000	0.000	0.000
48	A	49	GLU	-1	-0.917	-0.948	21.566	-0.083	-0.083	0.000	0.000	0.000
49	A	50	GLY	0	0.063	0.035	20.040	-0.003	-0.003	0.000	0.000	0.000
50	A	51	LYS	1	0.889	0.957	19.988	0.043	0.043	0.000	0.000	0.000
51	A	52	PHE	0	0.025	0.020	13.671	-0.008	-0.008	0.000	0.000	0.000
52	A	53	LEU	0	0.025	0.013	16.430	0.014	0.014	0.000	0.000	0.000
53	A	54	ALA	0	-0.014	-0.012	20.020	-0.007	-0.007	0.000	0.000	0.000
54	A	55	PHE	0	-0.047	-0.033	17.161	0.004	0.004	0.000	0.000	0.000
55	A	56	SER	0	0.037	0.015	19.129	-0.012	-0.012	0.000	0.000	0.000
56	A	57	TYR	0	-0.046	-0.049	17.198	-0.001	-0.001	0.000	0.000	0.000
57	A	58	LYS	1	0.975	0.988	19.394	0.088	0.088	0.000	0.000	0.000
58	A	59	VAL	0	-0.028	-0.018	15.935	-0.005	-0.005	0.000	0.000	0.000
59	A	60	LYS	1	0.876	0.941	18.831	0.152	0.152	0.000	0.000	0.000
60	A	61	GLY	0	0.024	0.006	18.699	-0.026	-0.026	0.000	0.000	0.000
61	A	62	ARG	1	0.885	0.959	19.127	0.175	0.175	0.000	0.000	0.000
62	A	63	VAL	0	-0.013	-0.003	19.200	-0.037	-0.037	0.000	0.000	0.000
63	A	64	TYR	0	-0.002	-0.004	18.920	0.034	0.034	0.000	0.000	0.000
64	A	65	LYS	1	0.903	0.945	20.545	0.138	0.138	0.000	0.000	0.000
65	A	66	GLY	0	0.004	0.002	22.202	0.010	0.010	0.000	0.000	0.000
66	A	67	VAL	0	0.002	-0.009	23.110	0.005	0.005	0.000	0.000	0.000
67	A	68	ASP	-1	-0.878	-0.929	22.351	-0.176	-0.176	0.000	0.000	0.000
68	A	69	GLU	-1	-0.832	-0.905	16.276	-0.416	-0.416	0.000	0.000	0.000
69	A	70	VAL	0	-0.015	0.008	18.524	0.028	0.028	0.000	0.000	0.000
70	A	71	ARG	1	0.842	0.898	14.798	0.321	0.321	0.000	0.000	0.000
71	A	72	ILE	0	0.006	-0.002	15.499	0.051	0.051	0.000	0.000	0.000
72	A	73	ILE	0	-0.010	0.000	14.568	-0.079	-0.079	0.000	0.000	0.000
73	A	74	TYR	0	-0.031	-0.044	10.081	0.015	0.015	0.000	0.000	0.000
74	A	75	ASP	-1	-0.856	-0.923	14.376	-0.206	-0.206	0.000	0.000	0.000
75	A	76	SER	0	0.037	-0.006	14.515	0.019	0.019	0.000	0.000	0.000
76	A	77	ASP	-1	-0.835	-0.913	16.477	-0.085	-0.085	0.000	0.000	0.000
77	A	78	ARG	1	0.822	0.907	14.059	0.072	0.072	0.000	0.000	0.000
78	A	79	GLY	0	0.011	0.022	11.501	0.013	0.013	0.000	0.000	0.000
79	A	80	ASN	0	0.041	0.026	11.405	0.003	0.003	0.000	0.000	0.000
80	A	81	GLY	0	0.027	0.013	9.677	-0.096	-0.096	0.000	0.000	0.000
81	A	82	ILE	0	-0.028	0.001	9.552	0.167	0.167	0.000	0.000	0.000
82	A	83	LEU	0	-0.013	-0.005	10.064	-0.236	-0.236	0.000	0.000	0.000
83	A	84	TYR	0	-0.023	-0.020	9.445	0.218	0.218	0.000	0.000	0.000
84	A	85	ILE	0	0.015	0.003	13.671	-0.028	-0.028	0.000	0.000	0.000
85	A	86	ARG	1	0.926	0.968	11.521	0.606	0.606	0.000	0.000	0.000
86	A	87	LYS	1	0.969	0.995	17.754	0.144	0.144	0.000	0.000	0.000
87	A	88	LYS	1	0.723	0.833	16.339	0.240	0.240	0.000	0.000	0.000
88	A	89	ASP	-1	-0.797	-0.882	20.861	-0.122	-0.122	0.000	0.000	0.000
89	A	90	ASN	0	-0.035	-0.035	24.577	-0.010	-0.010	0.000	0.000	0.000
90	A	91	ASN	0	-0.040	-0.004	25.897	0.007	0.007	0.000	0.000	0.000
91	A	92	THR	0	0.002	-0.006	19.975	0.003	0.003	0.000	0.000	0.000
92	A	93	LEU	0	0.019	0.015	18.275	-0.005	-0.005	0.000	0.000	0.000
93	A	94	GLN	0	-0.002	-0.009	11.964	0.083	0.083	0.000	0.000	0.000
94	A	95	ILE	0	0.023	0.019	12.738	-0.012	-0.012	0.000	0.000	0.000
95	A	96	ILE	0	-0.008	-0.006	7.900	-0.048	-0.048	0.000	0.000	0.000
96	A	97	LEU	0	-0.001	0.002	8.450	0.104	0.104	0.000	0.000	0.000
97	A	98	GLU	-1	-0.913	-0.976	5.194	-2.628	-2.509	0.000	-0.027	-0.091
98	A	99	HIS	0	-0.035	0.012	5.306	0.638	0.638	0.000	0.000	0.000
99	A	100	ASP	-1	-0.841	-0.925	5.419	-0.308	-0.308	0.000	0.000	0.000
100	A	101	ASN	0	0.011	0.018	7.452	0.337	0.337	0.000	0.000	0.000
101	A	102	LYS	1	1.007	0.982	5.623	-1.254	-1.254	0.000	0.000	0.000
102	A	103	LEU	0	0.004	0.009	6.940	0.011	0.011	0.000	0.000	0.000
103	A	104	THR	0	-0.006	-0.039	9.994	0.007	0.007	0.000	0.000	0.000
104	A	105	ALA	0	0.021	0.012	5.273	-0.056	-0.056	0.000	0.000	0.000
105	A	106	PHE	0	-0.083	-0.038	7.284	-0.021	-0.021	0.000	0.000	0.000
106	A	107	LEU	0	-0.013	-0.003	8.673	-0.049	-0.049	0.000	0.000	0.000
107	A	108	GLY	0	0.048	0.022	10.705	-0.017	-0.017	0.000	0.000	0.000
108	A	109	LYS	1	0.948	0.978	6.667	-0.121	-0.121	0.000	0.000	0.000
109	A	110	PRO	0	0.014	0.004	9.905	-0.046	-0.046	0.000	0.000	0.000
110	A	111	TYR	0	0.006	0.007	13.304	-0.007	-0.007	0.000	0.000	0.000
111	A	112	VAL	0	0.024	0.014	10.484	-0.013	-0.013	0.000	0.000	0.000
112	A	113	SER	0	-0.047	-0.030	11.582	0.002	0.002	0.000	0.000	0.000
113	A	114	SER	0	0.033	0.030	13.192	0.012	0.012	0.000	0.000	0.000
114	A	115	ASN	0	-0.018	-0.020	15.850	0.037	0.037	0.000	0.000	0.000
115	A	116	LEU	0	-0.025	-0.022	11.840	-0.002	-0.002	0.000	0.000	0.000
116	A	117	ASP	-1	-0.858	-0.919	16.126	-0.147	-0.147	0.000	0.000	0.000
117	A	118	ARG	1	0.892	0.960	18.275	0.162	0.162	0.000	0.000	0.000
118	A	119	LEU	0	-0.035	-0.030	18.258	0.008	0.008	0.000	0.000	0.000
119	A	120	ALA	0	-0.032	-0.037	18.871	0.008	0.008	0.000	0.000	0.000
120	A	121	GLU	-1	-0.978	-0.980	20.888	-0.084	-0.084	0.000	0.000	0.000
121	A	122	ASN	0	-0.048	-0.012	23.854	0.018	0.018	0.000	0.000	0.000
122	A	123	ILE	0	0.000	0.024	22.372	0.001	0.001	0.000	0.000	0.000
123	A	124	ASP	-1	-0.696	-0.845	25.064	-0.112	-0.112	0.000	0.000	0.000
124	A	125	GLU	-1	-0.950	-0.984	28.536	-0.083	-0.083	0.000	0.000	0.000
125	A	126	ILE	0	-0.012	-0.007	24.217	0.002	0.002	0.000	0.000	0.000
126	A	127	ILE	0	0.009	-0.001	24.860	0.003	0.003	0.000	0.000	0.000
127	A	128	ARG	1	0.962	0.989	28.658	0.077	0.077	0.000	0.000	0.000
128	A	129	LEU	0	-0.024	-0.019	31.342	0.006	0.006	0.000	0.000	0.000
129	A	130	GLU	-1	-0.839	-0.917	27.469	-0.115	-0.115	0.000	0.000	0.000
130	A	131	ARG	1	0.825	0.892	30.972	0.096	0.096	0.000	0.000	0.000
131	A	132	ILE	0	-0.039	-0.003	33.230	0.005	0.005	0.000	0.000	0.000
132	A	133	LYS	1	0.866	0.943	30.046	0.108	0.108	0.000	0.000	0.000
133	A	134	ARG	1	0.734	0.838	27.571	0.129	0.129	0.000	0.000	0.000
134	A	135	LYS	1	0.897	0.959	34.492	0.067	0.067	0.000	0.000	0.000
135	A	136	ILE	-1	-0.813	-0.874	30.717	-0.089	-0.089	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ACE )