FMO DATABASE

FMODB ID: KG923

Calculation Name: 2OVI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2OVI

Chain ID: A

ChEMBL ID:

UniProt ID: Q8X5N5

Base Structure: X-ray

Registration Date: 2023-09-21

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	158
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1522088.961193
FMO2-HF: Nuclear repulsion	1459975.936193
FMO2-HF: Total energy	-62113.025
FMO2-MP2: Total energy	-62293.627146

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:4:VAL)

Summations of interaction energy for fragment #1(A:4: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.
-7.779	-1.065	2.208	-2.97	-5.953	-0.012

Interaction energy analysis for fragmet #1(A:4:VAL)

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 : -0.001

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	6	LEU	0	0.091	0.049	2.759	-4.051	-1.214	0.419	-1.482	-1.774	-0.005
4	A	7	GLN	0	0.021	0.010	5.226	-0.368	-0.219	-0.001	-0.005	-0.143	0.000
5	A	8	GLU	-1	-0.887	-0.923	2.562	-0.305	0.253	0.526	-0.240	-0.844	0.001
6	A	9	PHE	0	-0.009	-0.002	2.380	-1.904	-0.095	1.060	-0.853	-2.016	-0.006
7	A	10	LEU	0	-0.011	-0.010	3.326	0.589	0.439	0.090	0.285	-0.225	0.000
8	A	11	LYS	1	0.819	0.880	6.512	0.341	0.341	0.000	0.000	0.000	0.000
9	A	12	THR	0	-0.027	-0.002	5.068	0.156	0.156	0.000	0.000	0.000	0.000
10	A	13	GLU	-1	-1.021	-1.013	7.477	-0.370	-0.370	0.000	0.000	0.000	0.000
11	A	14	PRO	0	-0.022	0.000	7.493	0.060	0.060	0.000	0.000	0.000	0.000
12	A	15	ASP	-1	-0.890	-0.930	9.243	-0.415	-0.415	0.000	0.000	0.000	0.000
13	A	16	GLY	0	0.045	0.017	12.145	-0.055	-0.055	0.000	0.000	0.000	0.000
14	A	17	THR	0	-0.037	-0.034	13.975	0.025	0.025	0.000	0.000	0.000	0.000
15	A	18	LEU	0	0.035	0.006	12.555	-0.078	-0.078	0.000	0.000	0.000	0.000
16	A	19	GLU	-1	-0.774	-0.871	13.441	-0.413	-0.413	0.000	0.000	0.000	0.000
17	A	20	VAL	0	0.011	0.014	12.701	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	21	VAL	0	0.008	0.002	7.964	-0.090	-0.090	0.000	0.000	0.000	0.000
19	A	22	ALA	0	-0.019	-0.020	10.277	-0.094	-0.094	0.000	0.000	0.000	0.000
20	A	23	GLU	-1	-0.873	-0.923	12.383	-0.527	-0.527	0.000	0.000	0.000	0.000
21	A	24	GLN	0	-0.064	-0.029	8.683	-0.088	-0.088	0.000	0.000	0.000	0.000
22	A	25	TYR	0	-0.085	-0.058	2.797	-1.008	0.503	0.114	-0.675	-0.951	-0.002
23	A	26	ASN	0	-0.087	-0.036	9.290	0.191	0.191	0.000	0.000	0.000	0.000
24	A	27	THR	0	-0.006	-0.011	11.069	0.126	0.126	0.000	0.000	0.000	0.000
25	A	28	THR	0	0.011	0.012	13.863	-0.016	-0.016	0.000	0.000	0.000	0.000
26	A	29	LEU	0	0.019	-0.003	14.461	-0.042	-0.042	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.011	0.001	15.452	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	31	GLU	-1	-0.764	-0.861	13.004	-0.139	-0.139	0.000	0.000	0.000	0.000
29	A	32	VAL	0	0.014	0.035	10.343	-0.031	-0.031	0.000	0.000	0.000	0.000
30	A	33	VAL	0	-0.023	-0.019	11.887	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	34	ARG	1	0.775	0.874	14.290	0.134	0.134	0.000	0.000	0.000	0.000
32	A	35	ASN	0	-0.063	-0.057	9.249	0.091	0.091	0.000	0.000	0.000	0.000
33	A	36	LEU	0	0.009	0.023	10.240	-0.066	-0.066	0.000	0.000	0.000	0.000
34	A	37	PRO	0	0.000	0.000	10.776	0.068	0.068	0.000	0.000	0.000	0.000
35	A	38	SER	0	-0.009	-0.028	13.459	0.004	0.004	0.000	0.000	0.000	0.000
36	A	39	SER	0	-0.014	0.026	15.434	0.031	0.031	0.000	0.000	0.000	0.000
37	A	40	THR	0	-0.002	0.005	17.724	0.034	0.034	0.000	0.000	0.000	0.000
38	A	41	VAL	0	-0.007	0.003	18.862	-0.010	-0.010	0.000	0.000	0.000	0.000
39	A	42	VAL	0	0.028	0.021	21.421	0.018	0.018	0.000	0.000	0.000	0.000
40	A	43	PRO	0	0.028	-0.001	24.943	-0.010	-0.010	0.000	0.000	0.000	0.000
41	A	44	GLY	0	0.028	0.014	27.053	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	45	ASP	-1	-0.910	-0.952	29.254	-0.039	-0.039	0.000	0.000	0.000	0.000
43	A	46	LYS	1	0.875	0.935	29.153	0.046	0.046	0.000	0.000	0.000	0.000
44	A	47	PHE	0	0.006	-0.005	30.812	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	48	ASP	-1	-0.790	-0.877	31.985	-0.058	-0.058	0.000	0.000	0.000	0.000
46	A	49	THR	0	0.001	0.008	32.795	0.000	0.000	0.000	0.000	0.000	0.000
47	A	50	VAL	0	-0.010	0.003	28.524	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	51	TRP	0	0.012	-0.020	31.621	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	52	ASP	-1	-0.897	-0.957	33.761	-0.059	-0.059	0.000	0.000	0.000	0.000
50	A	53	THR	0	-0.065	-0.036	33.104	0.002	0.002	0.000	0.000	0.000	0.000
51	A	54	VAL	0	-0.013	-0.019	30.232	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	55	CYS	0	-0.136	-0.051	33.614	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	56	GLU	-1	-0.935	-0.958	36.957	-0.057	-0.057	0.000	0.000	0.000	0.000
54	A	57	TRP	0	-0.054	-0.019	28.916	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	58	GLY	0	0.055	0.050	35.903	-0.002	-0.002	0.000	0.000	0.000	0.000
56	A	59	ASN	0	-0.052	-0.043	35.830	0.001	0.001	0.000	0.000	0.000	0.000
57	A	60	VAL	0	0.013	0.029	30.995	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	61	THR	0	0.046	0.026	29.087	0.009	0.009	0.000	0.000	0.000	0.000
59	A	62	THR	0	0.006	0.012	29.167	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	63	LEU	0	-0.015	-0.010	25.028	0.000	0.000	0.000	0.000	0.000	0.000
61	A	64	VAL	0	0.000	0.002	27.918	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	65	HIS	0	0.002	-0.005	22.503	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	66	THR	0	-0.041	-0.027	26.357	0.005	0.005	0.000	0.000	0.000	0.000
64	A	67	ALA	0	-0.036	-0.015	25.810	-0.013	-0.013	0.000	0.000	0.000	0.000
65	A	68	ASP	-1	-0.896	-0.949	26.880	-0.148	-0.148	0.000	0.000	0.000	0.000
66	A	69	VAL	0	-0.021	-0.015	29.137	0.005	0.005	0.000	0.000	0.000	0.000
67	A	70	ILE	0	0.009	0.009	25.146	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	71	LEU	0	-0.042	-0.011	28.439	0.005	0.005	0.000	0.000	0.000	0.000
69	A	72	GLU	-1	-0.893	-0.971	28.473	-0.172	-0.172	0.000	0.000	0.000	0.000
70	A	73	PHE	0	-0.002	-0.009	31.501	0.008	0.008	0.000	0.000	0.000	0.000
71	A	74	SER	0	-0.002	-0.003	32.784	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	75	GLY	0	-0.023	-0.018	34.784	0.006	0.006	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.869	-0.915	35.889	-0.073	-0.073	0.000	0.000	0.000	0.000
74	A	77	LEU	0	0.032	0.020	32.905	0.000	0.000	0.000	0.000	0.000	0.000
75	A	78	PRO	0	0.000	-0.001	36.308	0.005	0.005	0.000	0.000	0.000	0.000
76	A	79	SER	0	0.095	0.054	38.102	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	80	GLY	0	0.018	-0.005	39.540	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	81	PHE	0	-0.071	-0.037	40.462	0.003	0.003	0.000	0.000	0.000	0.000
79	A	82	HIS	0	0.020	0.000	36.496	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	83	ARG	1	0.890	0.933	41.593	0.040	0.040	0.000	0.000	0.000	0.000
81	A	84	HIS	0	0.000	-0.003	43.453	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	85	GLY	0	0.080	0.045	40.946	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	86	TYR	0	-0.056	-0.020	38.010	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	87	PHE	0	0.038	0.031	36.551	0.004	0.004	0.000	0.000	0.000	0.000
85	A	88	ASN	0	-0.056	-0.040	38.467	-0.005	-0.005	0.000	0.000	0.000	0.000
86	A	89	LEU	0	0.014	0.013	36.435	0.002	0.002	0.000	0.000	0.000	0.000
87	A	90	ARG	1	0.888	0.935	40.666	0.055	0.055	0.000	0.000	0.000	0.000
88	A	91	GLY	0	-0.025	-0.024	42.900	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	92	LYS	1	0.867	0.933	40.298	0.073	0.073	0.000	0.000	0.000	0.000
90	A	93	HIS	0	-0.015	-0.011	41.148	-0.007	-0.007	0.000	0.000	0.000	0.000
91	A	94	GLY	0	0.000	0.010	41.468	0.003	0.003	0.000	0.000	0.000	0.000
92	A	95	MET	0	0.001	0.022	33.750	0.000	0.000	0.000	0.000	0.000	0.000
93	A	96	SER	0	-0.013	-0.014	39.717	0.004	0.004	0.000	0.000	0.000	0.000
94	A	97	GLY	0	0.036	0.022	39.044	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	98	HIS	0	-0.050	-0.038	38.279	0.003	0.003	0.000	0.000	0.000	0.000
96	A	99	ILE	0	0.048	0.033	32.539	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	100	LYS	1	0.870	0.939	33.852	0.066	0.066	0.000	0.000	0.000	0.000
98	A	101	ALA	0	0.043	0.017	32.825	-0.003	-0.003	0.000	0.000	0.000	0.000
99	A	102	GLU	-1	-0.875	-0.926	32.654	-0.050	-0.050	0.000	0.000	0.000	0.000
100	A	103	ASN	0	-0.037	-0.025	30.752	0.007	0.007	0.000	0.000	0.000	0.000
101	A	104	CYS	0	-0.045	-0.009	27.290	-0.008	-0.008	0.000	0.000	0.000	0.000
102	A	105	THR	0	0.016	-0.011	24.958	0.008	0.008	0.000	0.000	0.000	0.000
103	A	106	HIS	0	-0.003	-0.003	22.819	0.000	0.000	0.000	0.000	0.000	0.000
104	A	107	ILE	0	0.021	0.028	24.578	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	108	ALA	0	-0.017	-0.005	19.815	0.005	0.005	0.000	0.000	0.000	0.000
106	A	109	LEU	0	-0.011	0.016	21.747	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	110	ILE	0	-0.021	-0.026	16.913	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	111	GLU	-1	-0.805	-0.902	18.297	-0.151	-0.151	0.000	0.000	0.000	0.000
109	A	112	ARG	1	0.845	0.919	12.575	0.525	0.525	0.000	0.000	0.000	0.000
110	A	113	LYS	1	0.873	0.931	15.938	0.274	0.274	0.000	0.000	0.000	0.000
111	A	114	PHE	0	-0.027	-0.019	15.700	-0.052	-0.052	0.000	0.000	0.000	0.000
112	A	115	MET	0	0.019	0.006	17.132	0.037	0.037	0.000	0.000	0.000	0.000
113	A	116	GLY	0	0.012	0.006	18.101	0.029	0.029	0.000	0.000	0.000	0.000
114	A	117	MET	0	-0.013	0.003	19.811	0.030	0.030	0.000	0.000	0.000	0.000
115	A	118	ASP	-1	-0.815	-0.887	20.474	-0.244	-0.244	0.000	0.000	0.000	0.000
116	A	119	THR	0	-0.004	-0.003	19.351	0.027	0.027	0.000	0.000	0.000	0.000
117	A	120	ALA	0	0.090	0.050	21.026	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	121	SER	0	-0.054	-0.025	21.081	0.000	0.000	0.000	0.000	0.000	0.000
119	A	122	ILE	0	0.028	0.010	22.770	-0.001	-0.001	0.000	0.000	0.000	0.000
120	A	123	LEU	0	-0.054	-0.023	19.309	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	124	PHE	0	0.073	0.033	23.338	0.010	0.010	0.000	0.000	0.000	0.000
122	A	125	PHE	0	0.014	-0.015	19.023	-0.010	-0.010	0.000	0.000	0.000	0.000
123	A	126	ASN	0	0.084	0.042	24.232	0.013	0.013	0.000	0.000	0.000	0.000
124	A	127	LYS	1	0.868	0.904	24.171	0.070	0.070	0.000	0.000	0.000	0.000
125	A	128	GLU	-1	-0.863	-0.910	23.214	-0.091	-0.091	0.000	0.000	0.000	0.000
126	A	129	GLY	0	0.024	0.015	20.046	-0.015	-0.015	0.000	0.000	0.000	0.000
127	A	130	SER	0	-0.013	-0.008	19.493	-0.033	-0.033	0.000	0.000	0.000	0.000
128	A	131	ALA	0	-0.026	-0.032	21.500	0.018	0.018	0.000	0.000	0.000	0.000
129	A	132	MET	0	-0.084	-0.024	23.237	0.003	0.003	0.000	0.000	0.000	0.000
130	A	133	LEU	0	-0.004	-0.004	26.345	0.004	0.004	0.000	0.000	0.000	0.000
131	A	134	LYS	1	0.869	0.925	20.448	0.266	0.266	0.000	0.000	0.000	0.000
132	A	135	ILE	0	0.032	0.023	25.831	0.008	0.008	0.000	0.000	0.000	0.000
133	A	136	PHE	0	-0.030	-0.020	21.684	-0.012	-0.012	0.000	0.000	0.000	0.000
134	A	137	LEU	0	0.011	0.006	26.215	0.011	0.011	0.000	0.000	0.000	0.000
135	A	138	GLY	0	0.021	0.020	28.312	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	139	ARG	1	0.778	0.870	23.684	0.189	0.189	0.000	0.000	0.000	0.000
137	A	140	ASP	-1	-0.716	-0.854	30.926	-0.097	-0.097	0.000	0.000	0.000	0.000
138	A	141	ASP	-1	-0.903	-0.950	33.730	-0.098	-0.098	0.000	0.000	0.000	0.000
139	A	142	HIS	0	-0.113	-0.062	33.597	0.004	0.004	0.000	0.000	0.000	0.000
140	A	143	ARG	1	0.813	0.892	28.995	0.121	0.121	0.000	0.000	0.000	0.000
141	A	144	GLN	0	-0.015	0.000	28.115	-0.016	-0.016	0.000	0.000	0.000	0.000
142	A	145	LEU	0	-0.003	-0.010	24.497	0.005	0.005	0.000	0.000	0.000	0.000
143	A	146	LEU	0	0.050	0.050	29.047	0.006	0.006	0.000	0.000	0.000	0.000
144	A	147	SER	0	0.045	0.009	31.278	-0.004	-0.004	0.000	0.000	0.000	0.000
145	A	148	GLU	-1	-0.899	-0.951	32.068	-0.083	-0.083	0.000	0.000	0.000	0.000
146	A	149	GLN	0	0.014	-0.021	30.896	-0.006	-0.006	0.000	0.000	0.000	0.000
147	A	150	VAL	0	0.000	0.002	26.455	-0.001	-0.001	0.000	0.000	0.000	0.000
148	A	151	SER	0	0.011	0.017	28.387	0.002	0.002	0.000	0.000	0.000	0.000
149	A	152	ALA	0	0.042	0.032	30.669	0.005	0.005	0.000	0.000	0.000	0.000
150	A	153	PHE	0	-0.013	-0.014	22.597	0.003	0.003	0.000	0.000	0.000	0.000
151	A	154	HIS	0	-0.053	-0.052	24.010	0.013	0.013	0.000	0.000	0.000	0.000
152	A	155	THR	0	-0.053	-0.028	27.470	0.008	0.008	0.000	0.000	0.000	0.000
153	A	156	LEU	0	-0.032	-0.016	28.791	0.006	0.006	0.000	0.000	0.000	0.000
154	A	157	ALA	0	0.006	-0.006	24.326	0.004	0.004	0.000	0.000	0.000	0.000
155	A	158	ALA	0	-0.039	-0.026	26.303	0.005	0.005	0.000	0.000	0.000	0.000
156	A	159	SER	0	-0.072	-0.040	27.874	0.007	0.007	0.000	0.000	0.000	0.000
157	A	160	LEU	0	-0.073	-0.024	26.908	0.005	0.005	0.000	0.000	0.000	0.000
158	A	161	LYS	1	0.864	0.929	20.106	0.105	0.105	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:VAL)