FMO DATABASE

FMODB ID: Q16LY

Calculation Name: 2OEB-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2OEB

Chain ID: A

ChEMBL ID:

UniProt ID: O28417

Base Structure: X-ray

Registration Date: 2023-06-20

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

DOI:

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	152
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1491382.777284
FMO2-HF: Nuclear repulsion	1432510.204507
FMO2-HF: Total energy	-58872.572777
FMO2-MP2: Total energy	-59047.577062

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:ASP)

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

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.
2.779	-1.443	22.669	-10.338	-8.11	-0.043

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.961 / q_NPA : -0.996

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	4	ARG	1	0.957	0.977	2.653	-44.968	-41.498	0.420	-1.702	-2.189	0.014
4	A	5	GLU	-1	-0.842	-0.914	1.745	37.624	28.967	22.247	-8.248	-5.342	-0.058
5	A	6	ILE	0	0.036	0.021	3.712	-7.306	-6.341	0.002	-0.388	-0.579	0.001
6	A	7	GLU	-1	-0.841	-0.920	5.673	22.953	22.953	0.000	0.000	0.000	0.000
7	A	8	GLN	0	-0.066	-0.022	7.075	-2.929	-2.929	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.797	-0.901	7.691	23.725	23.725	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.760	0.842	8.096	-37.480	-37.480	0.000	0.000	0.000	0.000
10	A	11	ALA	0	-0.037	-0.011	11.631	-2.392	-2.392	0.000	0.000	0.000	0.000
11	A	12	SER	0	0.008	0.008	12.794	-2.159	-2.159	0.000	0.000	0.000	0.000
12	A	13	PHE	0	0.017	0.008	13.945	-1.594	-1.594	0.000	0.000	0.000	0.000
13	A	14	ALA	0	0.009	-0.007	15.658	-1.294	-1.294	0.000	0.000	0.000	0.000
14	A	15	PHE	0	-0.009	0.000	17.326	-1.178	-1.178	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.937	0.986	16.818	-18.448	-18.448	0.000	0.000	0.000	0.000
16	A	17	VAL	0	-0.013	-0.011	19.744	-0.799	-0.799	0.000	0.000	0.000	0.000
17	A	18	VAL	0	-0.006	-0.007	21.618	-0.716	-0.716	0.000	0.000	0.000	0.000
18	A	19	SER	0	-0.010	-0.030	22.655	-0.808	-0.808	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.882	-0.916	24.507	11.106	11.106	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.021	0.005	26.199	-0.552	-0.552	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.841	0.898	27.642	-10.929	-10.929	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.963	-0.976	28.911	9.712	9.712	0.000	0.000	0.000	0.000
23	A	24	LYS	1	0.823	0.894	29.106	-11.102	-11.102	0.000	0.000	0.000	0.000
24	A	25	TYR	0	-0.087	-0.080	31.464	-0.505	-0.505	0.000	0.000	0.000	0.000
25	A	26	SER	0	0.039	0.051	33.769	-0.191	-0.191	0.000	0.000	0.000	0.000
26	A	27	GLN	0	-0.035	-0.025	34.589	-0.243	-0.243	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.026	-0.026	36.338	-0.274	-0.274	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.936	0.942	35.325	-8.217	-8.217	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.935	0.982	35.371	-7.695	-7.695	0.000	0.000	0.000	0.000
30	A	31	VAL	0	0.013	0.017	32.041	0.135	0.135	0.000	0.000	0.000	0.000
31	A	32	GLN	0	-0.003	-0.004	30.856	0.481	0.481	0.000	0.000	0.000	0.000
32	A	33	GLY	0	0.066	0.040	30.571	0.352	0.352	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.819	0.903	31.885	-8.837	-8.837	0.000	0.000	0.000	0.000
34	A	35	TYR	0	-0.001	-0.018	23.434	0.284	0.284	0.000	0.000	0.000	0.000
35	A	36	SER	0	0.046	0.025	27.139	0.646	0.646	0.000	0.000	0.000	0.000
36	A	37	SER	0	-0.024	-0.013	27.317	0.259	0.259	0.000	0.000	0.000	0.000
37	A	38	TYR	0	-0.088	-0.056	28.054	0.067	0.067	0.000	0.000	0.000	0.000
38	A	39	ALA	0	0.065	0.036	23.173	0.315	0.315	0.000	0.000	0.000	0.000
39	A	40	GLH	0	-0.123	-0.077	23.363	0.575	0.575	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.879	0.929	25.177	-10.190	-10.190	0.000	0.000	0.000	0.000
41	A	42	ALA	0	0.036	0.031	23.074	-0.070	-0.070	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.017	0.006	20.419	0.066	0.066	0.000	0.000	0.000	0.000
43	A	44	THR	0	0.019	0.009	22.066	0.254	0.254	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.010	0.016	25.192	-0.216	-0.216	0.000	0.000	0.000	0.000
45	A	46	ILE	0	0.009	0.012	19.679	-0.080	-0.080	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.041	-0.017	19.898	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	48	ASN	0	-0.074	-0.043	23.164	-0.419	-0.419	0.000	0.000	0.000	0.000
48	A	49	ASN	0	-0.058	-0.029	25.851	-0.479	-0.479	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.057	0.046	22.888	-0.125	-0.125	0.000	0.000	0.000	0.000
50	A	51	LEU	0	0.033	0.012	17.794	-0.468	-0.468	0.000	0.000	0.000	0.000
51	A	52	GLY	0	0.053	0.026	21.864	-0.259	-0.259	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.048	0.017	24.255	-0.370	-0.370	0.000	0.000	0.000	0.000
53	A	54	THR	0	0.004	-0.007	23.847	-0.447	-0.447	0.000	0.000	0.000	0.000
54	A	55	LEU	0	-0.026	-0.010	21.303	-0.360	-0.360	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.032	0.011	25.574	-0.385	-0.385	0.000	0.000	0.000	0.000
56	A	57	PHE	0	-0.008	0.002	28.595	-0.485	-0.485	0.000	0.000	0.000	0.000
57	A	58	PHE	0	0.009	0.001	23.733	-0.360	-0.360	0.000	0.000	0.000	0.000
58	A	59	LEU	0	0.059	0.036	28.652	-0.390	-0.390	0.000	0.000	0.000	0.000
59	A	60	SER	0	-0.108	-0.061	31.315	-0.495	-0.495	0.000	0.000	0.000	0.000
60	A	61	LYS	1	0.839	0.913	32.799	-9.610	-9.610	0.000	0.000	0.000	0.000
61	A	62	LEU	0	-0.096	-0.022	31.105	-0.216	-0.216	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.887	-0.929	35.485	7.737	7.737	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.780	0.891	35.442	-8.848	-8.848	0.000	0.000	0.000	0.000
64	A	65	PRO	0	-0.011	-0.017	39.719	-0.189	-0.189	0.000	0.000	0.000	0.000
65	A	66	ILE	0	-0.019	-0.029	33.358	0.043	0.043	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.910	-0.945	35.192	8.685	8.685	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.789	-0.889	30.962	10.567	10.567	0.000	0.000	0.000	0.000
68	A	69	VAL	0	-0.038	-0.019	29.795	0.089	0.089	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.803	-0.869	26.038	13.167	13.167	0.000	0.000	0.000	0.000
70	A	71	TYR	0	-0.057	-0.072	20.746	-0.294	-0.294	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.827	0.900	23.082	-13.330	-13.330	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.026	-0.036	26.078	-0.169	-0.169	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.035	0.012	28.165	-0.383	-0.383	0.000	0.000	0.000	0.000
74	A	75	ASN	0	0.082	0.040	29.378	0.488	0.488	0.000	0.000	0.000	0.000
75	A	76	PRO	0	-0.015	-0.008	28.329	-0.316	-0.316	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.775	-0.865	31.467	9.861	9.861	0.000	0.000	0.000	0.000
77	A	78	SER	0	-0.084	-0.038	34.166	-0.311	-0.311	0.000	0.000	0.000	0.000
78	A	79	PHE	0	0.020	0.017	32.752	-0.176	-0.176	0.000	0.000	0.000	0.000
79	A	80	GLY	0	0.075	0.031	37.275	-0.046	-0.046	0.000	0.000	0.000	0.000
80	A	81	ASN	0	-0.042	-0.030	38.211	0.002	0.002	0.000	0.000	0.000	0.000
81	A	82	ALA	0	0.037	0.008	36.397	0.187	0.187	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.770	-0.867	34.580	9.324	9.324	0.000	0.000	0.000	0.000
83	A	84	ASN	0	0.050	0.006	33.431	0.280	0.280	0.000	0.000	0.000	0.000
84	A	85	ILE	0	0.031	0.040	32.486	0.292	0.292	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.002	0.001	30.351	0.398	0.398	0.000	0.000	0.000	0.000
86	A	87	TYR	0	-0.017	-0.024	28.822	0.322	0.322	0.000	0.000	0.000	0.000
87	A	88	ALA	0	0.021	0.034	28.316	0.431	0.431	0.000	0.000	0.000	0.000
88	A	89	PHE	0	0.015	-0.004	26.743	0.396	0.396	0.000	0.000	0.000	0.000
89	A	90	LEU	0	-0.029	0.001	23.082	0.599	0.599	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.020	-0.028	23.403	0.838	0.838	0.000	0.000	0.000	0.000
91	A	92	LYS	1	0.845	0.913	23.465	-11.531	-11.531	0.000	0.000	0.000	0.000
92	A	93	HIS	0	0.020	0.026	21.054	0.795	0.795	0.000	0.000	0.000	0.000
93	A	94	LEU	0	0.007	0.010	17.635	0.926	0.926	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.038	0.005	18.359	1.141	1.141	0.000	0.000	0.000	0.000
95	A	96	THR	0	-0.015	-0.023	18.423	0.336	0.336	0.000	0.000	0.000	0.000
96	A	97	TRP	0	-0.047	-0.037	10.267	-0.065	-0.065	0.000	0.000	0.000	0.000
97	A	98	LEU	0	0.017	-0.004	14.171	1.431	1.431	0.000	0.000	0.000	0.000
98	A	99	ALA	0	0.012	0.014	14.852	1.066	1.066	0.000	0.000	0.000	0.000
99	A	100	GLU	-1	-0.892	-0.929	15.547	15.734	15.734	0.000	0.000	0.000	0.000
100	A	101	GLY	0	-0.005	0.018	12.155	0.778	0.778	0.000	0.000	0.000	0.000
101	A	102	ASN	0	-0.076	-0.070	12.201	-3.517	-3.517	0.000	0.000	0.000	0.000
102	A	103	GLY	0	0.012	0.015	13.833	-1.118	-1.118	0.000	0.000	0.000	0.000
103	A	104	LYS	1	0.918	0.943	13.339	-16.351	-16.351	0.000	0.000	0.000	0.000
104	A	105	ASP	-1	-0.918	-0.957	13.862	18.651	18.651	0.000	0.000	0.000	0.000
105	A	106	SER	0	-0.079	-0.023	10.878	1.045	1.045	0.000	0.000	0.000	0.000
106	A	107	ALA	0	0.006	-0.002	5.543	0.370	0.370	0.000	0.000	0.000	0.000
107	A	108	PHE	0	-0.004	0.005	6.265	5.234	5.234	0.000	0.000	0.000	0.000
108	A	109	SER	0	0.011	0.008	8.260	-2.618	-2.618	0.000	0.000	0.000	0.000
109	A	110	GLY	0	0.012	0.018	10.608	-2.405	-2.405	0.000	0.000	0.000	0.000
110	A	111	LEU	0	-0.050	-0.037	9.371	1.849	1.849	0.000	0.000	0.000	0.000
111	A	112	THR	0	-0.048	-0.041	12.706	-0.533	-0.533	0.000	0.000	0.000	0.000
112	A	113	ASN	0	-0.033	-0.022	15.170	-0.815	-0.815	0.000	0.000	0.000	0.000
113	A	114	GLY	0	0.024	0.018	16.669	-0.958	-0.958	0.000	0.000	0.000	0.000
114	A	115	GLH	0	-0.093	-0.063	19.290	-0.693	-0.693	0.000	0.000	0.000	0.000
115	A	116	ASP	-1	-0.766	-0.898	20.450	13.818	13.818	0.000	0.000	0.000	0.000
116	A	117	PRO	0	0.022	-0.003	19.021	-0.089	-0.089	0.000	0.000	0.000	0.000
117	A	118	LEU	0	0.000	0.020	20.986	0.101	0.101	0.000	0.000	0.000	0.000
118	A	119	LYS	1	0.875	0.923	24.072	-12.469	-12.469	0.000	0.000	0.000	0.000
119	A	120	TYR	0	0.000	-0.003	15.488	-0.391	-0.391	0.000	0.000	0.000	0.000
120	A	121	ILE	0	-0.017	-0.030	19.811	0.153	0.153	0.000	0.000	0.000	0.000
121	A	122	MET	0	-0.062	-0.027	21.782	-0.287	-0.287	0.000	0.000	0.000	0.000
122	A	123	GLU	-1	-0.802	-0.836	23.317	12.878	12.878	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.799	0.923	18.742	-15.571	-15.571	0.000	0.000	0.000	0.000
124	A	125	THR	0	0.012	-0.017	18.519	-0.503	-0.503	0.000	0.000	0.000	0.000
125	A	126	ALA	0	0.041	0.008	19.526	0.581	0.581	0.000	0.000	0.000	0.000
126	A	127	ILE	0	0.031	0.016	15.085	0.350	0.350	0.000	0.000	0.000	0.000
127	A	128	ASP	-1	-0.783	-0.868	14.946	20.453	20.453	0.000	0.000	0.000	0.000
128	A	129	VAL	0	-0.029	-0.011	15.499	0.944	0.944	0.000	0.000	0.000	0.000
129	A	130	ALA	0	0.002	0.003	16.368	0.314	0.314	0.000	0.000	0.000	0.000
130	A	131	ILE	0	0.048	0.025	10.255	0.466	0.466	0.000	0.000	0.000	0.000
131	A	132	SER	0	-0.019	-0.018	12.246	1.444	1.444	0.000	0.000	0.000	0.000
132	A	133	THR	0	-0.074	-0.047	14.301	-0.653	-0.653	0.000	0.000	0.000	0.000
133	A	134	GLU	-1	-0.936	-0.961	9.700	29.349	29.349	0.000	0.000	0.000	0.000
134	A	135	GLU	-1	-0.730	-0.816	8.911	33.766	33.766	0.000	0.000	0.000	0.000
135	A	136	ALA	0	-0.008	-0.017	11.956	-0.657	-0.657	0.000	0.000	0.000	0.000
136	A	137	LEU	0	-0.006	-0.010	15.296	-1.003	-1.003	0.000	0.000	0.000	0.000
137	A	138	SER	0	-0.029	-0.004	11.311	-0.236	-0.236	0.000	0.000	0.000	0.000
138	A	139	ILE	0	-0.012	-0.004	13.287	-0.876	-0.876	0.000	0.000	0.000	0.000
139	A	140	LEU	0	0.014	0.003	14.855	-1.356	-1.356	0.000	0.000	0.000	0.000
140	A	141	ASN	0	-0.042	-0.016	15.613	-2.081	-2.081	0.000	0.000	0.000	0.000
141	A	142	TRP	0	-0.009	-0.035	11.701	-2.656	-2.656	0.000	0.000	0.000	0.000
142	A	143	ILE	0	0.036	0.021	16.785	-0.941	-0.941	0.000	0.000	0.000	0.000
143	A	144	LYS	1	0.963	0.989	19.905	-14.940	-14.940	0.000	0.000	0.000	0.000
144	A	145	LYS	1	0.807	0.926	14.644	-20.799	-20.799	0.000	0.000	0.000	0.000
145	A	146	PHE	0	0.049	0.013	16.272	-0.634	-0.634	0.000	0.000	0.000	0.000
146	A	147	ALA	0	0.023	0.010	21.601	-0.594	-0.594	0.000	0.000	0.000	0.000
147	A	148	LYS	1	0.933	0.965	22.809	-13.951	-13.951	0.000	0.000	0.000	0.000
148	A	149	ALA	0	-0.056	-0.018	23.040	-0.399	-0.399	0.000	0.000	0.000	0.000
149	A	150	MET	0	-0.045	-0.006	23.511	-0.213	-0.213	0.000	0.000	0.000	0.000
150	A	151	LEU	0	-0.024	-0.001	26.730	-0.421	-0.421	0.000	0.000	0.000	0.000
151	A	152	GLU	-1	-0.841	-0.903	29.222	8.823	8.823	0.000	0.000	0.000	0.000
152	A	153	GLU	-1	-0.864	-0.933	30.674	10.160	10.160	0.000	0.000	0.000	0.000

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