FMO DATABASE

FMODB ID: N9Y1Q

Calculation Name: 2E0Q-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2E0Q

Chain ID: A

ChEMBL ID:

UniProt ID: F9VP91

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	103
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-808086.943169
FMO2-HF: Nuclear repulsion	767520.686906
FMO2-HF: Total energy	-40566.256263
FMO2-MP2: Total energy	-40685.274516

3D Structure Molmil

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:37:VAL)

Summations of interaction energy for fragment #1(A:37:VAL)

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.
-8.335	-3.525	13.024	-4.391	-13.444	-0.036

Interaction energy analysis for fragmet #1(A:37:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.001 / q_NPA : 0.002

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	39	HIS	0	-0.032	-0.014	3.461	-1.836	-0.090	0.026	-0.822	-0.950	0.001
4	A	40	LEU	0	-0.023	0.001	5.160	0.359	0.447	-0.001	-0.004	-0.082	0.000
5	A	41	ASP	-1	-0.778	-0.900	7.578	-0.067	-0.067	0.000	0.000	0.000	0.000
6	A	42	SER	0	-0.021	-0.018	11.339	0.052	0.052	0.000	0.000	0.000	0.000
7	A	43	LYS	1	0.813	0.898	14.223	0.052	0.052	0.000	0.000	0.000	0.000
8	A	44	ASN	0	-0.003	0.002	8.731	0.027	0.027	0.000	0.000	0.000	0.000
9	A	45	PHE	0	0.073	0.058	9.644	0.082	0.082	0.000	0.000	0.000	0.000
10	A	46	ASP	-1	-0.861	-0.940	11.613	0.131	0.131	0.000	0.000	0.000	0.000
11	A	47	SER	0	-0.096	-0.064	12.574	0.049	0.049	0.000	0.000	0.000	0.000
12	A	48	PHE	0	0.017	0.001	5.040	0.046	0.046	0.000	0.000	0.000	0.000
13	A	49	LEU	0	-0.013	0.014	9.871	0.113	0.113	0.000	0.000	0.000	0.000
14	A	50	ALA	0	-0.018	-0.003	11.804	0.009	0.009	0.000	0.000	0.000	0.000
15	A	51	SER	0	-0.102	-0.052	9.275	0.103	0.103	0.000	0.000	0.000	0.000
16	A	52	HIS	1	0.788	0.882	8.049	-1.083	-1.083	0.000	0.000	0.000	0.000
17	A	53	GLU	-1	-0.787	-0.843	12.182	0.147	0.147	0.000	0.000	0.000	0.000
18	A	54	ILE	0	0.032	0.024	11.768	-0.053	-0.053	0.000	0.000	0.000	0.000
19	A	55	ALA	0	-0.022	-0.012	8.614	0.130	0.130	0.000	0.000	0.000	0.000
20	A	56	VAL	0	0.012	0.005	6.407	-0.093	-0.093	0.000	0.000	0.000	0.000
21	A	57	VAL	0	-0.032	-0.014	5.430	0.001	0.001	0.000	0.000	0.000	0.000
22	A	58	ASP	-1	-0.840	-0.926	4.224	-1.163	-1.045	-0.001	-0.013	-0.104	0.000
23	A	59	PHE	0	-0.014	-0.020	6.292	-0.049	-0.049	0.000	0.000	0.000	0.000
24	A	60	TRP	0	0.002	-0.016	6.443	-0.023	-0.023	0.000	0.000	0.000	0.000
25	A	61	ALA	0	0.046	0.019	9.443	0.046	0.046	0.000	0.000	0.000	0.000
26	A	62	GLU	-1	-0.906	-0.955	11.694	-0.579	-0.579	0.000	0.000	0.000	0.000
27	A	63	TRP	0	-0.095	-0.060	12.971	0.019	0.019	0.000	0.000	0.000	0.000
28	A	64	CYS	0	0.012	0.039	9.369	0.034	0.034	0.000	0.000	0.000	0.000
29	A	65	ALA	0	0.027	0.008	13.086	-0.048	-0.048	0.000	0.000	0.000	0.000
30	A	66	PRO	0	-0.008	-0.019	14.074	-0.028	-0.028	0.000	0.000	0.000	0.000
31	A	68	LEU	0	-0.006	0.005	9.097	-0.130	-0.130	0.000	0.000	0.000	0.000
32	A	69	ILE	0	-0.062	-0.029	10.559	-0.035	-0.035	0.000	0.000	0.000	0.000
33	A	70	LEU	0	0.006	0.003	7.735	0.008	0.008	0.000	0.000	0.000	0.000
34	A	71	ALA	0	-0.016	-0.005	5.795	-0.084	-0.084	0.000	0.000	0.000	0.000
35	A	72	PRO	0	0.059	0.031	4.787	-0.503	-0.397	-0.001	-0.002	-0.103	0.000
36	A	73	ILE	0	0.003	0.013	6.520	0.025	0.025	0.000	0.000	0.000	0.000
37	A	74	ILE	0	-0.006	-0.010	2.357	-0.434	-0.017	0.950	-0.269	-1.099	0.000
38	A	75	GLU	-1	-0.887	-0.949	2.292	-3.543	-2.964	3.946	-1.812	-2.714	-0.007
39	A	76	GLU	-1	-0.928	-0.968	3.216	0.660	-0.293	0.032	1.161	-0.240	-0.001
40	A	77	LEU	0	-0.038	-0.021	6.038	0.246	0.246	0.000	0.000	0.000	0.000
41	A	78	ALA	0	-0.020	-0.017	2.288	-0.179	-0.078	1.918	-0.693	-1.326	-0.005
42	A	79	GLU	-1	-1.005	-0.994	4.367	0.430	0.504	-0.001	-0.033	-0.040	0.000
43	A	80	ASP	-1	-0.858	-0.914	6.755	0.065	0.065	0.000	0.000	0.000	0.000
44	A	81	TYR	0	-0.118	-0.070	8.083	0.026	0.026	0.000	0.000	0.000	0.000
45	A	82	PRO	0	0.062	0.033	8.045	0.147	0.147	0.000	0.000	0.000	0.000
46	A	83	GLN	0	-0.062	-0.033	9.065	0.183	0.183	0.000	0.000	0.000	0.000
47	A	84	VAL	0	-0.018	-0.012	7.803	-0.109	-0.109	0.000	0.000	0.000	0.000
48	A	85	GLY	0	-0.037	-0.008	6.489	0.361	0.361	0.000	0.000	0.000	0.000
49	A	86	PHE	0	0.069	0.027	2.479	-1.756	-0.592	0.693	-0.429	-1.428	-0.001
50	A	87	GLY	0	0.023	-0.006	2.545	-1.543	0.139	3.313	-2.448	-2.547	-0.021
51	A	88	LYS	1	0.846	0.927	2.357	2.018	1.685	2.143	0.957	-2.767	-0.002
52	A	89	LEU	0	-0.054	-0.014	3.832	-0.044	-0.023	0.007	0.016	-0.044	0.000
53	A	90	ASN	0	0.014	-0.003	7.582	0.036	0.036	0.000	0.000	0.000	0.000
54	A	91	SER	0	0.064	0.000	9.778	0.060	0.060	0.000	0.000	0.000	0.000
55	A	92	ASP	-1	-0.872	-0.935	13.177	-0.263	-0.263	0.000	0.000	0.000	0.000
56	A	93	GLU	-1	-0.896	-0.922	10.670	-0.443	-0.443	0.000	0.000	0.000	0.000
57	A	94	ASN	0	-0.027	-0.016	11.272	0.083	0.083	0.000	0.000	0.000	0.000
58	A	95	PRO	0	0.058	0.041	14.106	0.005	0.005	0.000	0.000	0.000	0.000
59	A	96	ASP	-1	-0.916	-0.970	16.673	-0.089	-0.089	0.000	0.000	0.000	0.000
60	A	97	ILE	0	-0.063	-0.030	12.282	0.022	0.022	0.000	0.000	0.000	0.000
61	A	98	ALA	0	0.048	0.024	14.023	0.003	0.003	0.000	0.000	0.000	0.000
62	A	99	ALA	0	-0.019	-0.008	15.040	0.013	0.013	0.000	0.000	0.000	0.000
63	A	100	ARG	1	0.860	0.940	16.287	0.036	0.036	0.000	0.000	0.000	0.000
64	A	101	TYR	0	-0.009	-0.011	13.885	0.022	0.022	0.000	0.000	0.000	0.000
65	A	102	GLY	0	0.024	0.024	17.089	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	103	VAL	0	0.019	0.009	13.443	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	104	MET	0	-0.064	-0.031	16.735	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	105	SER	0	-0.043	-0.019	17.303	0.010	0.010	0.000	0.000	0.000	0.000
69	A	106	LEU	0	-0.020	0.013	12.140	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	107	PRO	0	0.034	-0.019	10.344	0.021	0.021	0.000	0.000	0.000	0.000
71	A	108	THR	0	-0.029	-0.016	10.949	0.053	0.053	0.000	0.000	0.000	0.000
72	A	109	VAL	0	-0.025	-0.002	7.961	-0.047	-0.047	0.000	0.000	0.000	0.000
73	A	110	ILE	0	0.019	0.016	9.857	0.045	0.045	0.000	0.000	0.000	0.000
74	A	111	PHE	0	-0.011	-0.011	9.757	0.000	0.000	0.000	0.000	0.000	0.000
75	A	112	PHE	0	0.022	-0.011	10.334	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	113	LYS	1	0.869	0.915	13.145	-0.118	-0.118	0.000	0.000	0.000	0.000
77	A	114	ASH	0	-0.096	-0.077	15.725	-0.029	-0.029	0.000	0.000	0.000	0.000
78	A	115	GLY	0	0.018	0.015	14.916	-0.008	-0.008	0.000	0.000	0.000	0.000
79	A	116	GLU	-1	-0.949	-0.967	15.901	0.029	0.029	0.000	0.000	0.000	0.000
80	A	117	PRO	0	-0.038	-0.016	14.791	0.012	0.012	0.000	0.000	0.000	0.000
81	A	118	VAL	0	-0.039	-0.034	15.475	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	119	ASP	-1	-0.847	-0.913	15.627	-0.062	-0.062	0.000	0.000	0.000	0.000
83	A	120	GLU	-1	-0.964	-0.988	13.881	-0.129	-0.129	0.000	0.000	0.000	0.000
84	A	121	ILE	0	-0.023	0.003	12.369	0.008	0.008	0.000	0.000	0.000	0.000
85	A	122	ILE	0	0.009	0.012	13.761	-0.027	-0.027	0.000	0.000	0.000	0.000
86	A	123	GLY	0	-0.002	-0.005	14.547	0.023	0.023	0.000	0.000	0.000	0.000
87	A	124	ALA	0	-0.039	-0.016	13.055	-0.033	-0.033	0.000	0.000	0.000	0.000
88	A	125	VAL	0	-0.011	-0.004	13.258	0.036	0.036	0.000	0.000	0.000	0.000
89	A	126	PRO	0	-0.017	-0.019	13.276	-0.039	-0.039	0.000	0.000	0.000	0.000
90	A	127	ARG	1	0.867	0.915	10.502	0.190	0.190	0.000	0.000	0.000	0.000
91	A	128	GLU	-1	-0.869	-0.948	12.328	-0.163	-0.163	0.000	0.000	0.000	0.000
92	A	129	GLU	-1	-0.868	-0.919	15.108	-0.120	-0.120	0.000	0.000	0.000	0.000
93	A	130	ILE	0	0.027	0.022	8.642	0.021	0.021	0.000	0.000	0.000	0.000
94	A	131	GLU	-1	-0.774	-0.857	11.762	-0.020	-0.020	0.000	0.000	0.000	0.000
95	A	132	ILE	0	-0.032	-0.014	12.580	0.047	0.047	0.000	0.000	0.000	0.000
96	A	133	ARG	1	0.788	0.878	13.576	0.131	0.131	0.000	0.000	0.000	0.000
97	A	134	ILE	0	0.019	0.017	8.377	0.032	0.032	0.000	0.000	0.000	0.000
98	A	135	LYS	1	0.836	0.900	12.636	-0.040	-0.040	0.000	0.000	0.000	0.000
99	A	136	ASN	0	-0.074	-0.054	15.670	0.019	0.019	0.000	0.000	0.000	0.000
100	A	137	LEU	0	-0.015	-0.004	13.786	0.009	0.009	0.000	0.000	0.000	0.000
101	A	138	LEU	0	-0.050	-0.015	12.500	0.025	0.025	0.000	0.000	0.000	0.000
102	A	139	GLY	0	-0.023	0.008	16.623	0.007	0.007	0.000	0.000	0.000	0.000
103	A	140	GLU	-1	-0.937	-0.963	15.866	0.143	0.143	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:37:VAL)