FMO DATABASE

FMODB ID: V5V71

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	OptAll
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	-1348158.776308
FMO2-HF: Nuclear repulsion	1287831.102662
FMO2-HF: Total energy	-60327.673646
FMO2-MP2: Total energy	-60506.14612

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.
-12.036	-1.883	7.766	-5.193	-12.724	-0.034

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 : -0.015 / q_NPA : -0.003

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	-0.799	-0.883	2.843	-4.213	-0.826	0.358	-1.760	-1.984	-0.007
4	A	9	ILE	0	-0.015	-0.023	5.218	0.194	0.244	-0.001	-0.004	-0.044	0.000
5	A	10	LEU	0	0.000	0.023	8.108	0.103	0.103	0.000	0.000	0.000	0.000
6	A	11	TYR	0	-0.026	-0.034	11.553	0.027	0.027	0.000	0.000	0.000	0.000
7	A	12	TYR	0	0.023	-0.001	14.413	0.033	0.033	0.000	0.000	0.000	0.000
8	A	13	LYS	1	0.837	0.935	18.175	0.160	0.160	0.000	0.000	0.000	0.000
9	A	14	LYS	1	0.847	0.901	21.431	0.215	0.215	0.000	0.000	0.000	0.000
10	A	15	GLY	0	-0.020	-0.004	23.905	0.015	0.015	0.000	0.000	0.000	0.000
11	A	16	LYS	1	0.831	0.928	23.286	0.223	0.223	0.000	0.000	0.000	0.000
12	A	17	GLU	-1	-0.823	-0.912	24.378	-0.253	-0.253	0.000	0.000	0.000	0.000
13	A	18	PHE	0	-0.026	-0.022	21.035	0.008	0.008	0.000	0.000	0.000	0.000
14	A	19	GLY	0	0.125	0.080	23.966	0.002	0.002	0.000	0.000	0.000	0.000
15	A	20	ILE	0	-0.055	-0.038	25.303	0.006	0.006	0.000	0.000	0.000	0.000
16	A	21	LEU	0	-0.026	-0.012	21.860	0.013	0.013	0.000	0.000	0.000	0.000
17	A	22	GLU	-1	-0.843	-0.935	20.294	-0.333	-0.333	0.000	0.000	0.000	0.000
18	A	23	LYS	1	0.869	0.952	22.786	0.163	0.163	0.000	0.000	0.000	0.000
19	A	24	LYS	1	0.978	0.981	26.089	0.150	0.150	0.000	0.000	0.000	0.000
20	A	25	MET	0	-0.009	0.015	18.319	0.016	0.016	0.000	0.000	0.000	0.000
21	A	26	LYS	1	0.809	0.918	22.675	0.236	0.236	0.000	0.000	0.000	0.000
22	A	27	GLU	-1	-0.875	-0.962	24.453	-0.147	-0.147	0.000	0.000	0.000	0.000
23	A	28	ILE	0	0.080	0.034	25.840	0.008	0.008	0.000	0.000	0.000	0.000
24	A	29	PHE	0	0.018	0.024	21.109	0.008	0.008	0.000	0.000	0.000	0.000
25	A	30	ASN	0	-0.046	-0.042	25.222	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	31	GLU	-1	-0.977	-0.969	28.210	-0.107	-0.107	0.000	0.000	0.000	0.000
27	A	32	THR	0	-0.031	-0.036	27.325	0.008	0.008	0.000	0.000	0.000	0.000
28	A	33	GLY	0	-0.012	0.006	25.669	0.007	0.007	0.000	0.000	0.000	0.000
29	A	34	VAL	0	-0.043	-0.025	22.957	-0.011	-0.011	0.000	0.000	0.000	0.000
30	A	35	SER	0	-0.020	-0.005	18.255	-0.012	-0.012	0.000	0.000	0.000	0.000
31	A	36	LEU	0	-0.030	-0.021	19.854	0.014	0.014	0.000	0.000	0.000	0.000
32	A	37	GLU	-1	-0.818	-0.907	13.670	-0.542	-0.542	0.000	0.000	0.000	0.000
33	A	38	PRO	0	-0.036	-0.016	16.338	0.043	0.043	0.000	0.000	0.000	0.000
34	A	39	VAL	0	0.006	0.012	15.993	-0.023	-0.023	0.000	0.000	0.000	0.000
35	A	40	ASN	0	-0.038	-0.026	11.278	-0.024	-0.024	0.000	0.000	0.000	0.000
36	A	41	SER	0	0.006	0.012	15.791	0.043	0.043	0.000	0.000	0.000	0.000
37	A	42	GLU	-1	-0.806	-0.891	18.090	-0.158	-0.158	0.000	0.000	0.000	0.000
38	A	43	LEU	0	-0.006	0.001	20.474	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	44	ILE	0	-0.001	-0.005	16.675	-0.012	-0.012	0.000	0.000	0.000	0.000
40	A	45	GLY	0	0.026	0.014	14.357	0.050	0.050	0.000	0.000	0.000	0.000
41	A	46	ARG	1	0.820	0.900	8.397	0.847	0.847	0.000	0.000	0.000	0.000
42	A	47	ILE	0	-0.030	-0.001	7.670	0.150	0.150	0.000	0.000	0.000	0.000
43	A	48	PHE	0	0.000	0.003	2.635	-1.166	-0.377	0.618	-0.266	-1.141	-0.001
44	A	49	LEU	0	0.023	0.010	2.789	-0.739	0.574	0.191	-0.441	-1.063	-0.002
45	A	50	LYS	1	0.853	0.921	2.538	-5.395	-3.024	2.936	-1.849	-3.458	-0.015
46	A	51	ILE	0	0.035	0.010	3.095	-0.130	-0.493	0.094	0.551	-0.283	0.000
47	A	52	SER	0	-0.039	-0.014	6.067	0.827	0.827	0.000	0.000	0.000	0.000
48	A	53	VAL	0	-0.018	-0.006	8.834	-0.201	-0.201	0.000	0.000	0.000	0.000
49	A	54	LEU	0	-0.004	0.019	12.360	0.087	0.087	0.000	0.000	0.000	0.000
50	A	55	GLU	-1	-0.833	-0.937	15.468	0.345	0.345	0.000	0.000	0.000	0.000
51	A	56	GLU	-1	-0.871	-0.930	18.318	0.161	0.161	0.000	0.000	0.000	0.000
52	A	57	GLY	0	-0.037	-0.024	21.743	-0.021	-0.021	0.000	0.000	0.000	0.000
53	A	58	GLU	-1	-0.848	-0.887	17.233	0.540	0.540	0.000	0.000	0.000	0.000
54	A	59	GLU	-1	-0.945	-0.970	20.628	0.230	0.230	0.000	0.000	0.000	0.000
55	A	60	VAL	0	-0.020	-0.016	17.183	0.047	0.047	0.000	0.000	0.000	0.000
56	A	61	PRO	0	0.024	0.027	14.041	-0.035	-0.035	0.000	0.000	0.000	0.000
57	A	62	SER	0	0.019	-0.019	17.006	-0.026	-0.026	0.000	0.000	0.000	0.000
58	A	63	PHE	0	-0.009	-0.007	17.787	-0.036	-0.036	0.000	0.000	0.000	0.000
59	A	64	ALA	0	-0.014	0.007	13.614	0.050	0.050	0.000	0.000	0.000	0.000
60	A	65	ILE	0	0.020	-0.003	15.623	-0.054	-0.054	0.000	0.000	0.000	0.000
61	A	66	LYS	1	0.759	0.881	13.306	-0.306	-0.306	0.000	0.000	0.000	0.000
62	A	67	ALA	0	0.040	0.000	16.358	-0.048	-0.048	0.000	0.000	0.000	0.000
63	A	68	LEU	0	-0.009	0.017	18.323	0.032	0.032	0.000	0.000	0.000	0.000
64	A	69	THR	0	0.025	-0.009	20.837	-0.023	-0.023	0.000	0.000	0.000	0.000
65	A	70	PRO	0	0.000	0.005	23.521	0.002	0.002	0.000	0.000	0.000	0.000
66	A	71	LYS	1	0.790	0.881	24.646	-0.280	-0.280	0.000	0.000	0.000	0.000
67	A	72	GLU	-1	-0.916	-0.953	24.339	0.178	0.178	0.000	0.000	0.000	0.000
68	A	73	ASN	0	-0.068	-0.044	23.785	0.010	0.010	0.000	0.000	0.000	0.000
69	A	74	ALA	0	0.068	0.026	19.867	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	75	VAL	0	-0.023	-0.004	21.240	0.029	0.029	0.000	0.000	0.000	0.000
71	A	76	ASP	-1	-0.830	-0.898	23.476	0.291	0.291	0.000	0.000	0.000	0.000
72	A	77	LEU	0	-0.046	-0.022	19.229	-0.001	-0.001	0.000	0.000	0.000	0.000
73	A	78	PRO	0	0.007	0.021	18.659	0.030	0.030	0.000	0.000	0.000	0.000
74	A	79	LEU	0	-0.019	-0.022	11.251	0.036	0.036	0.000	0.000	0.000	0.000
75	A	80	GLY	0	-0.046	-0.026	13.833	0.089	0.089	0.000	0.000	0.000	0.000
76	A	81	ASP	-1	-0.863	-0.918	14.408	0.428	0.428	0.000	0.000	0.000	0.000
77	A	82	TRP	0	-0.091	-0.061	18.106	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	83	THR	0	-0.006	-0.018	20.080	-0.037	-0.037	0.000	0.000	0.000	0.000
79	A	84	ASP	-1	-0.837	-0.898	22.667	0.235	0.235	0.000	0.000	0.000	0.000
80	A	85	LEU	0	0.009	0.000	19.316	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	86	LYS	1	0.809	0.885	24.018	-0.237	-0.237	0.000	0.000	0.000	0.000
82	A	87	ASN	0	-0.076	-0.044	26.556	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	88	VAL	0	0.025	0.033	22.125	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	89	PHE	0	-0.020	-0.005	22.808	-0.016	-0.016	0.000	0.000	0.000	0.000
85	A	90	VAL	0	-0.007	-0.014	21.064	0.023	0.023	0.000	0.000	0.000	0.000
86	A	91	GLU	-1	-0.953	-0.971	18.750	0.242	0.242	0.000	0.000	0.000	0.000
87	A	92	GLU	-1	-0.860	-0.927	16.569	0.262	0.262	0.000	0.000	0.000	0.000
88	A	93	ILE	0	-0.034	-0.023	18.405	0.029	0.029	0.000	0.000	0.000	0.000
89	A	94	ASP	-1	-0.836	-0.892	14.434	0.343	0.343	0.000	0.000	0.000	0.000
90	A	95	TYR	0	-0.006	-0.013	16.789	0.027	0.027	0.000	0.000	0.000	0.000
91	A	96	LEU	0	-0.061	-0.022	12.919	0.017	0.017	0.000	0.000	0.000	0.000
92	A	97	ASP	-1	-0.784	-0.869	14.701	0.103	0.103	0.000	0.000	0.000	0.000
93	A	98	SER	0	-0.030	-0.030	16.155	0.044	0.044	0.000	0.000	0.000	0.000
94	A	99	TYR	0	-0.087	-0.062	16.166	-0.027	-0.027	0.000	0.000	0.000	0.000
95	A	100	GLY	0	0.018	0.011	17.685	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	101	ASP	-1	-0.848	-0.910	18.766	0.153	0.153	0.000	0.000	0.000	0.000
97	A	102	MET	0	-0.076	-0.021	12.653	0.046	0.046	0.000	0.000	0.000	0.000
98	A	103	LYS	1	0.828	0.922	14.412	-0.321	-0.321	0.000	0.000	0.000	0.000
99	A	104	ILE	0	-0.025	-0.031	10.250	0.082	0.082	0.000	0.000	0.000	0.000
100	A	105	LEU	0	0.050	0.034	9.699	-0.019	-0.019	0.000	0.000	0.000	0.000
101	A	106	SER	0	-0.024	-0.018	8.629	0.006	0.006	0.000	0.000	0.000	0.000
102	A	107	GLU	-1	-0.769	-0.872	7.246	0.812	0.812	0.000	0.000	0.000	0.000
103	A	108	LYS	1	0.892	0.937	7.494	-0.253	-0.253	0.000	0.000	0.000	0.000
104	A	109	ASN	0	-0.017	-0.010	8.928	0.096	0.096	0.000	0.000	0.000	0.000
105	A	110	TRP	0	0.001	0.005	2.605	-1.381	-0.428	0.888	-0.409	-1.432	-0.002
106	A	111	TYR	0	0.067	0.030	4.440	0.063	0.123	-0.001	-0.003	-0.056	0.000
107	A	112	LYS	1	0.792	0.885	4.408	-1.153	-0.957	-0.001	-0.017	-0.178	0.000
108	A	113	ILE	0	0.028	0.017	6.659	-0.173	-0.173	0.000	0.000	0.000	0.000
109	A	114	TYR	0	0.020	-0.003	8.869	0.393	0.393	0.000	0.000	0.000	0.000
110	A	115	VAL	0	0.025	0.024	11.734	-0.118	-0.118	0.000	0.000	0.000	0.000
111	A	116	PRO	0	0.091	0.054	14.546	0.064	0.064	0.000	0.000	0.000	0.000
112	A	117	TYR	0	0.074	0.015	16.752	-0.055	-0.055	0.000	0.000	0.000	0.000
113	A	118	SER	0	-0.017	-0.017	17.643	-0.030	-0.030	0.000	0.000	0.000	0.000
114	A	119	SER	0	-0.065	-0.056	18.637	-0.023	-0.023	0.000	0.000	0.000	0.000
115	A	120	VAL	0	-0.034	-0.027	14.167	-0.029	-0.029	0.000	0.000	0.000	0.000
116	A	121	LYS	1	0.774	0.890	16.798	-0.191	-0.191	0.000	0.000	0.000	0.000
117	A	122	LYS	1	0.879	0.940	19.139	-0.042	-0.042	0.000	0.000	0.000	0.000
118	A	123	LYS	1	0.929	1.006	15.772	-0.039	-0.039	0.000	0.000	0.000	0.000
119	A	124	ASN	0	-0.025	-0.032	14.450	-0.043	-0.043	0.000	0.000	0.000	0.000
120	A	125	ARG	1	0.865	0.890	7.249	1.351	1.351	0.000	0.000	0.000	0.000
121	A	126	ASN	0	0.012	-0.004	11.214	-0.106	-0.106	0.000	0.000	0.000	0.000
122	A	127	GLU	-1	-0.812	-0.881	13.462	-0.083	-0.083	0.000	0.000	0.000	0.000
123	A	128	LEU	0	0.010	0.004	10.416	0.013	0.013	0.000	0.000	0.000	0.000
124	A	129	VAL	0	0.000	0.000	8.693	0.014	0.014	0.000	0.000	0.000	0.000
125	A	130	GLU	-1	-0.823	-0.909	11.302	-0.203	-0.203	0.000	0.000	0.000	0.000
126	A	131	GLU	-1	-0.927	-0.965	14.527	-0.012	-0.012	0.000	0.000	0.000	0.000
127	A	132	PHE	0	0.020	0.005	8.846	0.028	0.028	0.000	0.000	0.000	0.000
128	A	133	MET	0	-0.022	-0.006	11.499	-0.025	-0.025	0.000	0.000	0.000	0.000
129	A	134	LYS	1	0.768	0.887	13.741	0.125	0.125	0.000	0.000	0.000	0.000
130	A	135	TYR	0	-0.001	-0.015	11.963	0.007	0.007	0.000	0.000	0.000	0.000
131	A	136	PHE	0	-0.013	-0.004	11.370	-0.001	-0.001	0.000	0.000	0.000	0.000
132	A	137	PHE	0	0.013	-0.005	14.045	0.002	0.002	0.000	0.000	0.000	0.000
133	A	138	GLU	-1	-0.800	-0.880	17.295	-0.047	-0.047	0.000	0.000	0.000	0.000
134	A	139	SER	0	-0.054	-0.026	15.359	0.014	0.014	0.000	0.000	0.000	0.000
135	A	140	LYS	1	0.802	0.895	13.036	0.098	0.098	0.000	0.000	0.000	0.000
136	A	141	GLY	0	-0.019	0.001	18.914	0.000	0.000	0.000	0.000	0.000	0.000
137	A	142	TRP	0	-0.052	-0.024	16.498	-0.012	-0.012	0.000	0.000	0.000	0.000
138	A	143	ASN	0	0.024	-0.006	21.208	0.000	0.000	0.000	0.000	0.000	0.000
139	A	144	PRO	0	0.070	0.024	19.406	-0.018	-0.018	0.000	0.000	0.000	0.000
140	A	145	GLY	0	0.005	0.014	20.740	-0.022	-0.022	0.000	0.000	0.000	0.000
141	A	146	GLU	-1	-0.877	-0.930	23.288	-0.136	-0.136	0.000	0.000	0.000	0.000
142	A	147	TYR	0	-0.050	-0.031	18.122	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	148	THR	0	-0.044	-0.026	18.340	0.011	0.011	0.000	0.000	0.000	0.000
144	A	149	PHE	0	0.023	0.001	12.487	0.000	0.000	0.000	0.000	0.000	0.000
145	A	150	SER	0	-0.029	-0.016	12.338	0.087	0.087	0.000	0.000	0.000	0.000
146	A	151	VAL	0	0.003	-0.010	7.819	-0.034	-0.034	0.000	0.000	0.000	0.000
147	A	152	GLN	0	0.004	-0.005	7.805	0.376	0.376	0.000	0.000	0.000	0.000
148	A	153	GLU	-1	-0.787	-0.864	5.045	-2.630	-2.630	0.000	0.000	0.000	0.000
149	A	154	ILE	0	-0.046	-0.006	2.211	-1.497	-0.100	2.684	-0.995	-3.085	-0.007

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