FMO DATABASE

FMODB ID: 4NM8N

Calculation Name: 1OZ9-A-Xray315

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1OZ9

Chain ID: A

ChEMBL ID:

UniProt ID: O67367

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	143
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1372658.866277
FMO2-HF: Nuclear repulsion	1316360.452021
FMO2-HF: Total energy	-56298.414256
FMO2-MP2: Total energy	-56466.84212

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:7:ACE )

Summations of interaction energy for fragment #1(A:7: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.
0.073	0.887	-0.004	-0.371	-0.439	-0.001

Interaction energy analysis for fragmet #1(A:7:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.026 / q_NPA : 0.005

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	9	ASN	0	0.039	0.031	3.879	0.727	1.541	-0.004	-0.371	-0.439	-0.001
4	A	10	ARG	1	0.920	0.977	5.287	-0.055	-0.055	0.000	0.000	0.000	0.000
5	A	11	VAL	0	0.049	0.024	7.430	-0.051	-0.051	0.000	0.000	0.000	0.000
6	A	12	LEU	0	-0.049	-0.014	9.946	0.112	0.112	0.000	0.000	0.000	0.000
7	A	13	VAL	0	0.028	0.015	12.616	-0.034	-0.034	0.000	0.000	0.000	0.000
8	A	14	LYS	1	0.927	0.955	15.268	-0.060	-0.060	0.000	0.000	0.000	0.000
9	A	15	LEU	0	-0.006	-0.003	18.655	-0.014	-0.014	0.000	0.000	0.000	0.000
10	A	16	LYS	1	0.962	0.994	21.524	-0.016	-0.016	0.000	0.000	0.000	0.000
11	A	17	LYS	1	0.873	0.944	24.888	-0.015	-0.015	0.000	0.000	0.000	0.000
12	A	18	ARG	1	0.958	0.959	22.509	-0.061	-0.061	0.000	0.000	0.000	0.000
13	A	19	LYS	1	0.941	0.994	24.679	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	20	VAL	0	0.030	0.023	20.554	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	21	ARG	1	0.841	0.897	17.976	-0.029	-0.029	0.000	0.000	0.000	0.000
16	A	22	LYS	1	1.000	0.997	13.635	-0.200	-0.200	0.000	0.000	0.000	0.000
17	A	23	ASP	-1	-0.731	-0.850	13.884	0.049	0.049	0.000	0.000	0.000	0.000
18	A	24	LYS	1	0.826	0.915	14.084	-0.014	-0.014	0.000	0.000	0.000	0.000
19	A	25	ILE	0	0.017	0.014	15.826	-0.026	-0.026	0.000	0.000	0.000	0.000
20	A	26	GLU	-1	-0.916	-0.964	9.067	0.178	0.178	0.000	0.000	0.000	0.000
21	A	27	LYS	1	1.028	1.020	11.395	0.060	0.060	0.000	0.000	0.000	0.000
22	A	28	TRP	0	-0.034	-0.025	12.452	-0.054	-0.054	0.000	0.000	0.000	0.000
23	A	29	ALA	0	0.046	0.025	12.866	-0.031	-0.031	0.000	0.000	0.000	0.000
24	A	30	GLU	-1	-0.918	-0.962	6.970	-0.243	-0.243	0.000	0.000	0.000	0.000
25	A	31	LEU	0	-0.067	-0.045	10.239	-0.102	-0.102	0.000	0.000	0.000	0.000
26	A	32	ALA	0	0.014	0.009	12.678	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	33	LEU	0	0.012	0.003	10.310	-0.010	-0.010	0.000	0.000	0.000	0.000
28	A	34	SER	0	-0.031	-0.013	10.013	-0.046	-0.046	0.000	0.000	0.000	0.000
29	A	35	ALA	0	-0.046	-0.022	11.800	0.029	0.029	0.000	0.000	0.000	0.000
30	A	36	LEU	0	-0.029	-0.028	14.964	0.033	0.033	0.000	0.000	0.000	0.000
31	A	37	GLY	0	-0.022	0.010	13.728	0.021	0.021	0.000	0.000	0.000	0.000
32	A	38	LEU	0	-0.019	0.000	12.255	-0.020	-0.020	0.000	0.000	0.000	0.000
33	A	39	ASN	0	-0.035	-0.036	8.606	-0.408	-0.408	0.000	0.000	0.000	0.000
34	A	40	ASN	0	-0.003	0.004	6.717	0.037	0.037	0.000	0.000	0.000	0.000
35	A	41	VAL	0	0.019	0.019	8.061	0.195	0.195	0.000	0.000	0.000	0.000
36	A	42	GLU	-1	-0.853	-0.905	9.138	0.020	0.020	0.000	0.000	0.000	0.000
37	A	43	LEU	0	-0.004	0.004	11.277	-0.013	-0.013	0.000	0.000	0.000	0.000
38	A	44	SER	0	0.009	0.008	12.867	0.043	0.043	0.000	0.000	0.000	0.000
39	A	45	VAL	0	0.000	-0.002	15.057	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	46	TYR	0	-0.113	-0.077	17.393	0.027	0.027	0.000	0.000	0.000	0.000
41	A	47	ILE	0	0.021	0.018	20.440	-0.010	-0.010	0.000	0.000	0.000	0.000
42	A	48	THR	0	-0.004	-0.041	22.864	0.011	0.011	0.000	0.000	0.000	0.000
43	A	49	ASP	-1	-0.908	-0.964	26.273	0.009	0.009	0.000	0.000	0.000	0.000
44	A	50	ASP	-1	-0.703	-0.836	30.005	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	51	GLN	0	-0.046	-0.026	32.809	0.000	0.000	0.000	0.000	0.000	0.000
46	A	52	GLU	-1	-0.739	-0.828	27.574	0.019	0.019	0.000	0.000	0.000	0.000
47	A	53	ILE	0	-0.031	-0.012	27.402	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	54	ARG	1	0.860	0.931	30.297	0.001	0.001	0.000	0.000	0.000	0.000
49	A	55	GLU	-1	-0.954	-0.965	32.512	0.008	0.008	0.000	0.000	0.000	0.000
50	A	56	LEU	0	0.012	0.004	26.807	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	57	ASN	0	0.007	-0.016	30.950	-0.006	-0.006	0.000	0.000	0.000	0.000
52	A	58	LYS	1	0.920	0.968	32.847	0.001	0.001	0.000	0.000	0.000	0.000
53	A	59	THR	0	-0.045	-0.029	32.368	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	60	TYR	0	-0.010	-0.011	28.599	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	61	ARG	1	0.937	0.981	27.839	0.038	0.038	0.000	0.000	0.000	0.000
56	A	62	LYS	1	0.923	0.978	34.145	0.015	0.015	0.000	0.000	0.000	0.000
57	A	63	LYS	1	0.942	0.968	35.607	0.029	0.029	0.000	0.000	0.000	0.000
58	A	64	ASP	-1	-0.868	-0.919	36.493	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	65	LYS	1	0.947	0.964	36.629	0.020	0.020	0.000	0.000	0.000	0.000
60	A	66	PRO	0	0.039	0.027	33.916	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	67	THR	0	0.002	-0.004	29.982	-0.002	-0.002	0.000	0.000	0.000	0.000
62	A	68	ASP	-1	-0.749	-0.877	28.723	-0.036	-0.036	0.000	0.000	0.000	0.000
63	A	69	VAL	0	-0.047	-0.032	23.706	0.002	0.002	0.000	0.000	0.000	0.000
64	A	70	LEU	0	-0.052	-0.020	25.491	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	71	SER	0	0.013	-0.004	22.462	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	72	PHE	0	-0.053	-0.032	22.373	0.003	0.003	0.000	0.000	0.000	0.000
67	A	73	PRO	0	0.061	0.032	21.202	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	74	MET	0	-0.021	-0.001	18.898	0.013	0.013	0.000	0.000	0.000	0.000
69	A	75	GLY	0	-0.005	-0.016	18.785	0.000	0.000	0.000	0.000	0.000	0.000
70	A	76	GLU	-1	-0.929	-0.943	18.538	-0.016	-0.016	0.000	0.000	0.000	0.000
71	A	77	GLU	-1	-0.879	-0.948	16.019	-0.137	-0.137	0.000	0.000	0.000	0.000
72	A	78	PHE	0	-0.002	-0.004	14.130	0.024	0.024	0.000	0.000	0.000	0.000
73	A	79	GLY	0	0.005	-0.002	13.808	-0.007	-0.007	0.000	0.000	0.000	0.000
74	A	80	GLY	0	0.002	-0.004	13.280	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	81	TYR	0	-0.101	-0.057	7.944	-0.043	-0.043	0.000	0.000	0.000	0.000
76	A	82	LYS	1	0.840	0.901	11.533	0.179	0.179	0.000	0.000	0.000	0.000
77	A	83	ILE	0	0.016	0.010	12.880	-0.036	-0.036	0.000	0.000	0.000	0.000
78	A	84	LEU	0	-0.013	-0.003	13.934	0.004	0.004	0.000	0.000	0.000	0.000
79	A	85	GLY	0	0.034	0.016	16.255	0.014	0.014	0.000	0.000	0.000	0.000
80	A	86	ASP	-1	-0.879	-0.942	17.037	-0.015	-0.015	0.000	0.000	0.000	0.000
81	A	87	VAL	0	0.003	0.001	18.793	-0.007	-0.007	0.000	0.000	0.000	0.000
82	A	88	VAL	0	-0.031	-0.012	20.365	0.012	0.012	0.000	0.000	0.000	0.000
83	A	89	ILE	0	0.025	0.011	21.307	-0.005	-0.005	0.000	0.000	0.000	0.000
84	A	90	SER	0	-0.029	-0.015	24.745	0.009	0.009	0.000	0.000	0.000	0.000
85	A	91	GLN	0	0.053	-0.009	26.599	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	92	ASP	-1	-0.831	-0.911	27.977	0.002	0.002	0.000	0.000	0.000	0.000
87	A	93	THR	0	-0.068	-0.044	30.911	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	94	ALA	0	0.037	0.022	27.545	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	95	GLU	-1	-0.964	-1.001	29.562	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	96	ARG	1	0.783	0.884	31.717	0.009	0.009	0.000	0.000	0.000	0.000
91	A	97	GLN	0	0.035	0.011	30.575	0.002	0.002	0.000	0.000	0.000	0.000
92	A	98	ALA	0	-0.024	0.000	30.311	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	99	ARG	1	0.907	0.946	32.215	0.011	0.011	0.000	0.000	0.000	0.000
94	A	100	GLU	-1	-0.993	-1.004	35.766	-0.021	-0.021	0.000	0.000	0.000	0.000
95	A	101	LEU	0	-0.029	-0.018	32.104	-0.001	-0.001	0.000	0.000	0.000	0.000
96	A	102	GLY	0	-0.012	0.025	35.338	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	103	HIS	0	-0.089	-0.065	29.598	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	104	SER	0	0.007	-0.002	27.283	0.002	0.002	0.000	0.000	0.000	0.000
99	A	105	LEU	0	0.084	0.030	26.395	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	106	GLU	-1	-0.890	-0.947	23.243	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	107	GLU	-1	-0.825	-0.885	23.621	-0.075	-0.075	0.000	0.000	0.000	0.000
102	A	108	GLU	-1	-0.783	-0.876	25.125	-0.050	-0.050	0.000	0.000	0.000	0.000
103	A	109	VAL	0	-0.016	-0.024	21.148	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	110	LYS	1	0.889	0.958	19.710	0.076	0.076	0.000	0.000	0.000	0.000
105	A	111	ARG	1	0.880	0.903	21.138	0.046	0.046	0.000	0.000	0.000	0.000
106	A	112	LEU	0	0.025	0.027	23.737	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	113	ILE	0	-0.033	-0.012	16.943	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	114	VAL	0	-0.031	-0.011	19.036	-0.014	-0.014	0.000	0.000	0.000	0.000
109	A	115	HIS	0	0.002	-0.008	20.486	-0.003	-0.003	0.000	0.000	0.000	0.000
110	A	116	GLY	0	0.018	-0.006	21.799	0.000	0.000	0.000	0.000	0.000	0.000
111	A	117	ILE	0	-0.017	-0.017	15.455	-0.004	-0.004	0.000	0.000	0.000	0.000
112	A	118	VAL	0	-0.006	-0.005	19.278	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	119	HIS	0	-0.012	-0.004	21.858	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	120	LEU	0	-0.065	-0.022	17.947	0.003	0.003	0.000	0.000	0.000	0.000
115	A	121	LEU	0	-0.109	-0.038	17.261	-0.008	-0.008	0.000	0.000	0.000	0.000
116	A	122	GLY	0	-0.029	-0.008	21.160	0.000	0.000	0.000	0.000	0.000	0.000
117	A	123	TYR	0	-0.063	-0.016	22.800	0.007	0.007	0.000	0.000	0.000	0.000
118	A	124	ASP	-1	-0.799	-0.926	26.767	-0.057	-0.057	0.000	0.000	0.000	0.000
119	A	125	HIS	0	-0.066	-0.040	29.216	0.001	0.001	0.000	0.000	0.000	0.000
120	A	126	GLU	-1	-0.959	-0.980	31.756	-0.040	-0.040	0.000	0.000	0.000	0.000
121	A	127	LYS	1	0.803	0.921	34.167	0.058	0.058	0.000	0.000	0.000	0.000
122	A	128	GLY	0	0.047	0.034	35.267	0.003	0.003	0.000	0.000	0.000	0.000
123	A	129	GLY	0	-0.013	-0.030	35.898	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	130	GLU	-1	-0.908	-0.969	33.618	-0.076	-0.076	0.000	0.000	0.000	0.000
125	A	131	GLU	-1	-0.839	-0.916	31.909	-0.068	-0.068	0.000	0.000	0.000	0.000
126	A	132	GLU	-1	-0.922	-0.944	31.003	-0.062	-0.062	0.000	0.000	0.000	0.000
127	A	133	LYS	1	0.935	0.981	31.392	0.069	0.069	0.000	0.000	0.000	0.000
128	A	134	LYS	1	0.931	0.954	28.555	0.100	0.100	0.000	0.000	0.000	0.000
129	A	135	PHE	0	0.011	0.015	25.924	-0.011	-0.011	0.000	0.000	0.000	0.000
130	A	136	ARG	1	0.888	0.924	26.648	0.062	0.062	0.000	0.000	0.000	0.000
131	A	137	GLU	-1	-0.949	-0.969	27.692	-0.100	-0.100	0.000	0.000	0.000	0.000
132	A	138	LEU	0	-0.008	0.008	21.366	-0.010	-0.010	0.000	0.000	0.000	0.000
133	A	139	GLU	-1	-0.741	-0.871	22.915	-0.101	-0.101	0.000	0.000	0.000	0.000
134	A	140	ASN	0	0.008	-0.008	23.667	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	141	TYR	0	-0.029	-0.005	19.378	0.004	0.004	0.000	0.000	0.000	0.000
136	A	142	VAL	0	0.044	0.036	18.064	-0.012	-0.012	0.000	0.000	0.000	0.000
137	A	143	LEU	0	0.024	0.008	20.056	-0.005	-0.005	0.000	0.000	0.000	0.000
138	A	144	SER	0	-0.094	-0.071	22.339	0.002	0.002	0.000	0.000	0.000	0.000
139	A	145	LYS	1	0.887	0.935	17.953	0.215	0.215	0.000	0.000	0.000	0.000
140	A	146	LEU	0	-0.029	-0.003	16.319	-0.009	-0.009	0.000	0.000	0.000	0.000
141	A	147	SER	0	-0.052	-0.008	19.201	0.014	0.014	0.000	0.000	0.000	0.000
142	A	148	LYS	1	0.867	0.939	21.354	0.142	0.142	0.000	0.000	0.000	0.000
143	A	149	NME	0	0.036	0.029	18.388	-0.009	-0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:ACE )