FMO DATABASE

FMODB ID: 52RKZ

Calculation Name: 1O22-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1O22

Chain ID: A

ChEMBL ID:

UniProt ID: Q9WZX8

Base Structure: X-ray

Registration Date: 2023-06-22

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	OptH
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	149
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1346586.020557
FMO2-HF: Nuclear repulsion	1286259.996731
FMO2-HF: Total energy	-60326.023827
FMO2-MP2: Total energy	-60504.267226

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:6:ILE)

Summations of interaction energy for fragment #1(A:6:ILE)

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.
-11.222	-8.624	23.933	-8.95	-17.578	-0.051

Interaction energy analysis for fragmet #1(A:6:ILE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.046 / q_NPA : -0.009

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	8	GLU	-1	-0.857	-0.935	2.862	-3.812	-0.343	0.377	-1.693	-2.153	-0.004
4	A	9	ILE	0	-0.003	-0.017	5.217	0.093	0.144	-0.001	-0.004	-0.045	0.000
5	A	10	LEU	0	-0.001	0.010	8.037	0.146	0.146	0.000	0.000	0.000	0.000
6	A	11	TYR	0	-0.024	-0.022	11.423	0.022	0.022	0.000	0.000	0.000	0.000
7	A	12	TYR	0	0.014	-0.004	14.199	0.031	0.031	0.000	0.000	0.000	0.000
8	A	13	LYS	1	0.947	0.979	17.915	0.142	0.142	0.000	0.000	0.000	0.000
9	A	14	LYS	1	0.844	0.893	21.135	0.177	0.177	0.000	0.000	0.000	0.000
10	A	15	GLY	0	-0.023	-0.006	23.319	0.016	0.016	0.000	0.000	0.000	0.000
11	A	16	LYS	1	0.893	0.969	23.175	0.187	0.187	0.000	0.000	0.000	0.000
12	A	17	GLU	-1	-0.898	-0.941	23.899	-0.236	-0.236	0.000	0.000	0.000	0.000
13	A	18	PHE	0	0.012	-0.019	20.820	0.015	0.015	0.000	0.000	0.000	0.000
14	A	19	GLY	0	0.088	0.057	23.341	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	20	ILE	0	-0.031	-0.031	25.291	0.003	0.003	0.000	0.000	0.000	0.000
16	A	21	LEU	0	-0.016	-0.006	20.455	0.011	0.011	0.000	0.000	0.000	0.000
17	A	22	GLU	-1	-0.850	-0.939	20.210	-0.325	-0.325	0.000	0.000	0.000	0.000
18	A	23	LYS	1	0.885	0.958	22.762	0.168	0.168	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.976	0.978	26.237	0.142	0.142	0.000	0.000	0.000	0.000
20	A	25	MET	0	0.009	0.021	18.131	0.015	0.015	0.000	0.000	0.000	0.000
21	A	26	LYS	1	0.927	0.968	21.838	0.271	0.271	0.000	0.000	0.000	0.000
22	A	27	GLU	-1	-0.941	-0.991	24.565	-0.144	-0.144	0.000	0.000	0.000	0.000
23	A	28	ILE	0	0.052	0.026	25.379	0.008	0.008	0.000	0.000	0.000	0.000
24	A	29	PHE	0	-0.033	0.010	21.972	0.004	0.004	0.000	0.000	0.000	0.000
25	A	30	ASN	0	-0.055	-0.040	24.943	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	31	GLU	-1	-0.973	-0.961	27.807	-0.104	-0.104	0.000	0.000	0.000	0.000
27	A	32	THR	0	-0.049	-0.056	26.924	0.007	0.007	0.000	0.000	0.000	0.000
28	A	33	GLY	0	0.010	0.021	25.518	0.007	0.007	0.000	0.000	0.000	0.000
29	A	34	VAL	0	-0.053	-0.024	22.592	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	35	SER	0	-0.012	-0.015	17.947	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	36	LEU	0	-0.047	-0.020	19.557	0.008	0.008	0.000	0.000	0.000	0.000
32	A	37	GLU	-1	-0.907	-0.962	13.985	-0.483	-0.483	0.000	0.000	0.000	0.000
33	A	38	PRO	0	-0.048	-0.022	15.750	0.041	0.041	0.000	0.000	0.000	0.000
34	A	39	VAL	0	0.014	0.017	15.545	-0.018	-0.018	0.000	0.000	0.000	0.000
35	A	40	ASN	0	-0.027	-0.024	10.715	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	41	SER	0	0.011	0.006	15.204	0.039	0.039	0.000	0.000	0.000	0.000
37	A	42	GLU	-1	-0.858	-0.921	17.541	-0.122	-0.122	0.000	0.000	0.000	0.000
38	A	43	LEU	0	-0.030	-0.016	20.030	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	44	ILE	0	0.019	0.010	16.246	-0.012	-0.012	0.000	0.000	0.000	0.000
40	A	45	GLY	0	0.013	0.008	13.714	0.048	0.048	0.000	0.000	0.000	0.000
41	A	46	ARG	1	0.956	0.995	7.989	0.695	0.695	0.000	0.000	0.000	0.000
42	A	47	ILE	0	-0.033	0.002	7.214	0.148	0.148	0.000	0.000	0.000	0.000
43	A	48	PHE	0	0.004	0.011	1.943	-0.686	-1.317	3.851	-1.059	-2.160	-0.003
44	A	49	LEU	0	0.034	0.024	2.779	-0.437	0.661	0.205	-0.265	-1.037	-0.002
45	A	50	LYS	1	0.941	0.967	2.431	-8.144	-4.117	2.004	-2.641	-3.390	-0.026
46	A	51	ILE	0	0.007	-0.007	3.706	-1.010	-0.840	0.017	-0.018	-0.169	0.000
47	A	52	SER	0	-0.056	-0.024	6.619	0.563	0.563	0.000	0.000	0.000	0.000
48	A	53	VAL	0	-0.016	-0.016	9.299	-0.219	-0.219	0.000	0.000	0.000	0.000
49	A	54	LEU	0	-0.008	0.017	12.575	0.067	0.067	0.000	0.000	0.000	0.000
50	A	55	GLU	-1	-0.883	-0.945	15.681	0.397	0.397	0.000	0.000	0.000	0.000
51	A	56	GLU	-1	-0.971	-1.007	18.388	0.189	0.189	0.000	0.000	0.000	0.000
52	A	57	GLY	0	-0.040	-0.019	21.699	0.000	0.000	0.000	0.000	0.000	0.000
53	A	58	GLU	-1	-0.892	-0.940	18.174	0.530	0.530	0.000	0.000	0.000	0.000
54	A	59	GLU	-1	-0.984	-0.991	20.643	0.265	0.265	0.000	0.000	0.000	0.000
55	A	60	VAL	0	-0.031	-0.026	16.736	0.050	0.050	0.000	0.000	0.000	0.000
56	A	61	PRO	0	0.035	0.026	14.177	-0.041	-0.041	0.000	0.000	0.000	0.000
57	A	62	SER	0	-0.002	-0.026	17.234	-0.017	-0.017	0.000	0.000	0.000	0.000
58	A	63	PHE	0	0.001	-0.005	17.674	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	64	ALA	0	-0.014	0.011	13.634	0.047	0.047	0.000	0.000	0.000	0.000
60	A	65	ILE	0	0.014	0.000	15.558	-0.052	-0.052	0.000	0.000	0.000	0.000
61	A	66	LYS	1	0.835	0.921	13.064	-0.379	-0.379	0.000	0.000	0.000	0.000
62	A	67	ALA	0	0.035	0.008	17.199	-0.048	-0.048	0.000	0.000	0.000	0.000
63	A	68	LEU	0	-0.015	0.001	19.126	0.024	0.024	0.000	0.000	0.000	0.000
64	A	69	THR	0	0.019	-0.010	21.431	-0.028	-0.028	0.000	0.000	0.000	0.000
65	A	70	PRO	0	0.022	0.012	23.754	0.002	0.002	0.000	0.000	0.000	0.000
66	A	71	LYS	1	0.913	0.964	25.466	-0.243	-0.243	0.000	0.000	0.000	0.000
67	A	72	GLU	-1	-0.909	-0.955	25.069	0.164	0.164	0.000	0.000	0.000	0.000
68	A	73	ASN	0	-0.102	-0.053	24.313	0.011	0.011	0.000	0.000	0.000	0.000
69	A	74	ALA	0	0.076	0.021	20.258	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	75	VAL	0	-0.049	-0.016	21.704	0.025	0.025	0.000	0.000	0.000	0.000
71	A	76	ASP	-1	-0.938	-0.974	23.794	0.278	0.278	0.000	0.000	0.000	0.000
72	A	77	LEU	0	-0.027	0.000	19.784	0.003	0.003	0.000	0.000	0.000	0.000
73	A	78	PRO	0	-0.008	0.023	18.939	0.011	0.011	0.000	0.000	0.000	0.000
74	A	79	LEU	0	-0.015	-0.026	11.868	0.050	0.050	0.000	0.000	0.000	0.000
75	A	80	GLY	0	-0.067	-0.043	14.208	0.017	0.017	0.000	0.000	0.000	0.000
76	A	81	ASP	-1	-0.818	-0.907	14.731	0.434	0.434	0.000	0.000	0.000	0.000
77	A	82	TRP	0	-0.074	-0.019	18.458	0.003	0.003	0.000	0.000	0.000	0.000
78	A	83	THR	0	-0.026	-0.028	21.123	-0.033	-0.033	0.000	0.000	0.000	0.000
79	A	84	ASP	-1	-0.899	-0.937	23.535	0.255	0.255	0.000	0.000	0.000	0.000
80	A	85	LEU	0	-0.006	-0.008	20.352	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	86	LYS	1	0.883	0.936	25.044	-0.241	-0.241	0.000	0.000	0.000	0.000
82	A	87	ASN	0	-0.047	-0.024	27.600	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	88	VAL	0	0.012	0.015	23.238	0.002	0.002	0.000	0.000	0.000	0.000
84	A	89	PHE	0	-0.003	-0.004	23.479	-0.016	-0.016	0.000	0.000	0.000	0.000
85	A	90	VAL	0	-0.018	-0.012	21.777	0.024	0.024	0.000	0.000	0.000	0.000
86	A	91	GLU	-1	-0.943	-0.972	18.694	0.262	0.262	0.000	0.000	0.000	0.000
87	A	92	GLU	-1	-0.859	-0.916	16.334	0.307	0.307	0.000	0.000	0.000	0.000
88	A	93	ILE	0	-0.046	-0.029	18.832	0.028	0.028	0.000	0.000	0.000	0.000
89	A	94	ASP	-1	-0.901	-0.938	15.197	0.334	0.334	0.000	0.000	0.000	0.000
90	A	95	TYR	0	-0.039	-0.030	16.983	0.030	0.030	0.000	0.000	0.000	0.000
91	A	96	LEU	0	-0.043	-0.018	12.964	0.015	0.015	0.000	0.000	0.000	0.000
92	A	97	ASP	-1	-0.802	-0.860	15.135	0.157	0.157	0.000	0.000	0.000	0.000
93	A	98	SER	0	-0.039	-0.043	15.954	0.047	0.047	0.000	0.000	0.000	0.000
94	A	99	TYR	0	-0.039	-0.014	16.218	-0.029	-0.029	0.000	0.000	0.000	0.000
95	A	100	GLY	0	0.021	0.008	17.632	0.009	0.009	0.000	0.000	0.000	0.000
96	A	101	ASP	-1	-0.828	-0.870	18.709	0.184	0.184	0.000	0.000	0.000	0.000
97	A	102	MET	0	-0.095	-0.030	12.818	0.057	0.057	0.000	0.000	0.000	0.000
98	A	103	LYS	1	0.895	0.966	14.345	-0.362	-0.362	0.000	0.000	0.000	0.000
99	A	104	ILE	0	0.020	-0.006	10.416	0.109	0.109	0.000	0.000	0.000	0.000
100	A	105	LEU	0	0.021	0.020	9.499	-0.029	-0.029	0.000	0.000	0.000	0.000
101	A	106	SER	0	0.006	0.004	9.039	0.054	0.054	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.849	-0.939	7.419	0.848	0.848	0.000	0.000	0.000	0.000
103	A	108	LYS	1	0.854	0.931	7.785	-0.344	-0.344	0.000	0.000	0.000	0.000
104	A	109	ASN	0	-0.039	-0.034	8.149	0.079	0.079	0.000	0.000	0.000	0.000
105	A	110	TRP	0	-0.001	0.002	2.085	-0.263	-1.631	4.962	-0.864	-2.731	-0.007
106	A	111	TYR	0	0.080	0.030	4.655	0.007	0.061	-0.001	-0.003	-0.050	0.000
107	A	112	LYS	1	0.905	0.958	4.580	-1.312	-1.162	-0.001	-0.012	-0.137	0.000
108	A	113	ILE	0	0.025	0.009	6.532	-0.239	-0.239	0.000	0.000	0.000	0.000
109	A	114	TYR	0	0.007	0.003	9.286	0.356	0.356	0.000	0.000	0.000	0.000
110	A	115	VAL	0	0.011	0.004	11.998	-0.136	-0.136	0.000	0.000	0.000	0.000
111	A	116	PRO	0	0.098	0.055	14.457	0.064	0.064	0.000	0.000	0.000	0.000
112	A	117	TYR	0	0.089	0.032	16.974	-0.055	-0.055	0.000	0.000	0.000	0.000
113	A	118	SER	0	-0.029	-0.033	17.889	-0.032	-0.032	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.065	-0.080	18.449	-0.029	-0.029	0.000	0.000	0.000	0.000
115	A	120	VAL	0	-0.051	-0.030	14.219	-0.044	-0.044	0.000	0.000	0.000	0.000
116	A	121	LYS	1	0.932	0.985	16.481	-0.153	-0.153	0.000	0.000	0.000	0.000
117	A	122	LYS	1	0.882	0.935	18.532	-0.062	-0.062	0.000	0.000	0.000	0.000
118	A	123	LYS	1	0.976	1.021	15.828	-0.112	-0.112	0.000	0.000	0.000	0.000
119	A	124	ASN	0	0.011	0.016	13.805	-0.018	-0.018	0.000	0.000	0.000	0.000
120	A	125	ARG	1	1.026	0.988	6.974	1.334	1.334	0.000	0.000	0.000	0.000
121	A	126	ASN	0	-0.006	0.001	11.106	-0.085	-0.085	0.000	0.000	0.000	0.000
122	A	127	GLU	-1	-0.874	-0.944	13.630	-0.049	-0.049	0.000	0.000	0.000	0.000
123	A	128	LEU	0	0.002	0.003	10.752	0.020	0.020	0.000	0.000	0.000	0.000
124	A	129	VAL	0	0.007	0.003	8.580	0.016	0.016	0.000	0.000	0.000	0.000
125	A	130	GLU	-1	-0.939	-0.974	11.256	-0.214	-0.214	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-0.924	-0.976	14.820	0.041	0.041	0.000	0.000	0.000	0.000
127	A	132	PHE	0	0.013	0.003	9.221	0.027	0.027	0.000	0.000	0.000	0.000
128	A	133	MET	0	-0.013	0.003	11.341	-0.014	-0.014	0.000	0.000	0.000	0.000
129	A	134	LYS	1	0.900	0.965	13.668	0.090	0.090	0.000	0.000	0.000	0.000
130	A	135	TYR	0	-0.024	-0.030	12.822	0.012	0.012	0.000	0.000	0.000	0.000
131	A	136	PHE	0	-0.010	-0.005	11.641	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	137	PHE	0	-0.005	-0.002	14.371	0.001	0.001	0.000	0.000	0.000	0.000
133	A	138	GLU	-1	-0.890	-0.945	17.425	-0.005	-0.005	0.000	0.000	0.000	0.000
134	A	139	SER	0	-0.091	-0.057	15.630	0.011	0.011	0.000	0.000	0.000	0.000
135	A	140	LYS	1	0.883	0.944	13.770	0.053	0.053	0.000	0.000	0.000	0.000
136	A	141	GLY	0	-0.029	0.007	18.709	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	142	TRP	0	-0.032	-0.014	16.148	-0.015	-0.015	0.000	0.000	0.000	0.000
138	A	143	ASN	0	0.071	0.020	21.592	0.003	0.003	0.000	0.000	0.000	0.000
139	A	144	PRO	0	0.086	0.029	19.023	-0.019	-0.019	0.000	0.000	0.000	0.000
140	A	145	GLY	0	-0.003	0.016	20.378	-0.022	-0.022	0.000	0.000	0.000	0.000
141	A	146	GLU	-1	-0.977	-0.987	22.626	-0.116	-0.116	0.000	0.000	0.000	0.000
142	A	147	TYR	0	-0.056	-0.037	17.670	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	148	THR	0	-0.033	-0.015	18.075	0.004	0.004	0.000	0.000	0.000	0.000
144	A	149	PHE	0	0.027	0.000	12.086	-0.009	-0.009	0.000	0.000	0.000	0.000
145	A	150	SER	0	-0.009	0.005	12.117	0.066	0.066	0.000	0.000	0.000	0.000
146	A	151	VAL	0	-0.020	-0.016	7.499	-0.033	-0.033	0.000	0.000	0.000	0.000
147	A	152	GLN	0	0.023	0.015	7.748	0.173	0.173	0.000	0.000	0.000	0.000
148	A	153	GLU	-1	-0.948	-0.972	4.896	-2.541	-2.541	0.000	0.000	0.000	0.000
149	A	154	ILE	0	-0.034	-0.007	1.959	1.420	-3.002	12.520	-2.391	-5.706	-0.009

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Interactive mode: IFIE and PIEDA for fragment #1(A:6:ILE)