FMO DATABASE

FMODB ID: 895JY

Calculation Name: 2O3A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2O3A

Chain ID: A

ChEMBL ID:

UniProt ID: O29507

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	167
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1696724.965789
FMO2-HF: Nuclear repulsion	1631973.618678
FMO2-HF: Total energy	-64751.347111
FMO2-MP2: Total energy	-64944.911194

3D Structure Molmil

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:1:LEU)

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

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.
-19.076	-7.487	10.64	-7.414	-14.816	-0.047

Interaction energy analysis for fragmet #1(A:1:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.003 / 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	3	VAL	0	0.000	-0.009	2.831	-2.680	0.286	0.432	-1.241	-2.157	-0.002
4	A	4	TYR	0	-0.071	-0.050	5.248	0.352	0.412	-0.001	-0.004	-0.055	0.000
5	A	5	VAL	0	0.023	0.004	8.706	0.023	0.023	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.006	-0.008	11.318	-0.011	-0.011	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.803	0.900	14.354	0.056	0.056	0.000	0.000	0.000	0.000
8	A	8	LEU	0	-0.020	-0.016	17.446	-0.011	-0.011	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.015	-0.016	20.117	0.012	0.012	0.000	0.000	0.000	0.000
10	A	10	HIS	0	-0.031	0.009	22.990	0.010	0.010	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.907	0.921	24.674	0.043	0.043	0.000	0.000	0.000	0.000
12	A	12	PRO	0	-0.022	0.011	28.465	0.006	0.006	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.761	-0.886	30.685	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.790	0.857	30.926	0.000	0.000	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.741	-0.859	25.467	-0.021	-0.021	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.803	0.894	25.485	0.017	0.017	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.916	0.974	25.392	-0.038	-0.038	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.048	0.029	22.113	0.008	0.008	0.000	0.000	0.000	0.000
19	A	19	SER	0	0.045	-0.011	20.979	0.005	0.005	0.000	0.000	0.000	0.000
20	A	20	THR	0	0.011	-0.006	20.362	-0.003	-0.003	0.000	0.000	0.000	0.000
21	A	21	HIS	0	-0.007	-0.007	20.271	0.008	0.008	0.000	0.000	0.000	0.000
22	A	22	VAL	0	0.035	0.035	15.962	0.019	0.019	0.000	0.000	0.000	0.000
23	A	23	ALA	0	0.015	0.009	15.833	0.009	0.009	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.003	-0.006	15.795	0.011	0.011	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.031	-0.015	13.741	0.033	0.033	0.000	0.000	0.000	0.000
26	A	26	ALA	0	-0.004	-0.016	11.646	0.041	0.041	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.835	0.914	11.149	-0.118	-0.118	0.000	0.000	0.000	0.000
28	A	28	ALA	0	-0.017	-0.010	12.911	0.048	0.048	0.000	0.000	0.000	0.000
29	A	29	PHE	0	0.018	-0.006	10.313	0.031	0.031	0.000	0.000	0.000	0.000
30	A	30	GLY	0	0.033	0.012	7.967	0.145	0.145	0.000	0.000	0.000	0.000
31	A	31	ALA	0	-0.071	-0.032	7.261	0.001	0.001	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.930	0.968	6.333	-0.079	-0.079	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.032	0.007	9.990	0.041	0.041	0.000	0.000	0.000	0.000
34	A	34	ILE	0	-0.102	-0.039	11.934	-0.036	-0.036	0.000	0.000	0.000	0.000
35	A	35	TYR	0	0.024	-0.002	12.008	0.048	0.048	0.000	0.000	0.000	0.000
36	A	36	PHE	0	0.002	-0.008	16.337	0.016	0.016	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.811	-0.903	19.468	-0.111	-0.111	0.000	0.000	0.000	0.000
38	A	38	THR	0	-0.054	-0.034	21.887	0.002	0.002	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.820	-0.876	24.002	-0.051	-0.051	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.808	-0.908	26.156	-0.023	-0.023	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.914	0.930	26.380	0.043	0.043	0.000	0.000	0.000	0.000
42	A	42	SER	0	0.060	0.051	27.331	0.002	0.002	0.000	0.000	0.000	0.000
43	A	43	VAL	0	-0.026	0.010	22.342	0.008	0.008	0.000	0.000	0.000	0.000
44	A	44	PHE	0	0.012	-0.007	22.184	0.004	0.004	0.000	0.000	0.000	0.000
45	A	45	GLU	-1	-0.926	-0.970	23.647	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.023	-0.024	24.892	0.009	0.009	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.018	-0.012	18.806	0.011	0.011	0.000	0.000	0.000	0.000
48	A	48	ARG	1	0.897	0.941	21.282	0.049	0.049	0.000	0.000	0.000	0.000
49	A	49	ASP	-1	-0.817	-0.877	22.868	0.061	0.061	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.027	-0.018	20.397	0.011	0.011	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.019	-0.010	18.015	0.017	0.017	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.821	-0.894	20.635	0.079	0.079	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.806	0.885	23.899	-0.055	-0.055	0.000	0.000	0.000	0.000
54	A	54	TRP	0	-0.056	-0.038	21.051	0.010	0.010	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.040	0.027	20.003	0.028	0.028	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.005	0.009	16.317	0.002	0.002	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.905	-0.953	13.968	0.076	0.076	0.000	0.000	0.000	0.000
58	A	58	PHE	0	-0.050	-0.008	12.141	-0.050	-0.050	0.000	0.000	0.000	0.000
59	A	59	PHE	0	0.017	0.011	12.976	0.009	0.009	0.000	0.000	0.000	0.000
60	A	60	ILE	0	0.006	0.003	15.954	-0.009	-0.009	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.897	0.963	17.328	0.202	0.202	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.036	0.029	19.413	-0.011	-0.011	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.019	-0.016	17.647	-0.008	-0.008	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.026	0.014	21.098	0.006	0.006	0.000	0.000	0.000	0.000
65	A	65	TRP	0	0.093	0.030	18.641	-0.025	-0.025	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.875	0.932	18.321	0.119	0.119	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.771	0.867	20.374	0.232	0.232	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.053	0.025	13.394	-0.015	-0.015	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.015	-0.019	13.636	-0.048	-0.048	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.916	0.957	15.899	0.220	0.220	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.836	-0.886	16.553	-0.271	-0.271	0.000	0.000	0.000	0.000
72	A	72	PHE	0	-0.010	0.018	7.185	-0.017	-0.017	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.880	-0.922	11.340	-0.789	-0.789	0.000	0.000	0.000	0.000
74	A	74	GLY	0	0.033	-0.011	7.407	-0.234	-0.234	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.026	0.002	5.938	0.231	0.231	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.809	0.902	7.426	0.554	0.554	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.001	-0.011	7.027	0.051	0.051	0.000	0.000	0.000	0.000
78	A	78	HIS	0	0.004	-0.001	10.090	0.043	0.043	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.049	-0.020	11.105	0.021	0.021	0.000	0.000	0.000	0.000
80	A	80	THR	0	0.008	-0.001	14.146	0.005	0.005	0.000	0.000	0.000	0.000
81	A	81	MET	0	-0.003	0.010	17.816	0.008	0.008	0.000	0.000	0.000	0.000
82	A	82	TYR	0	-0.053	-0.042	20.531	0.007	0.007	0.000	0.000	0.000	0.000
83	A	83	GLY	0	0.019	0.026	16.882	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.006	0.005	15.292	0.020	0.020	0.000	0.000	0.000	0.000
85	A	85	PRO	0	-0.005	0.003	14.904	0.004	0.004	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.054	0.030	7.943	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	87	PRO	0	-0.031	-0.035	11.000	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.006	0.000	12.521	-0.015	-0.015	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.849	0.909	10.416	0.249	0.249	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.031	-0.002	6.023	-0.082	-0.082	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.827	-0.896	6.295	-0.087	-0.087	0.000	0.000	0.000	0.000
92	A	92	GLU	-1	-0.814	-0.897	6.903	-0.526	-0.526	0.000	0.000	0.000	0.000
93	A	93	ILE	0	-0.016	-0.016	3.799	-0.520	-0.269	0.003	-0.045	-0.209	0.000
94	A	94	LYS	1	0.836	0.922	2.172	-3.317	-1.989	2.273	-1.380	-2.220	0.001
95	A	95	ARG	1	0.812	0.896	3.190	-0.248	-0.297	-0.001	0.577	-0.527	-0.002
96	A	96	ALA	0	-0.004	0.015	3.326	0.045	0.466	0.018	-0.105	-0.336	0.000
97	A	97	ASP	-1	-0.869	-0.933	2.531	-7.771	-4.801	1.722	-1.937	-2.755	-0.022
98	A	98	LYS	1	0.798	0.894	2.580	-2.845	-0.765	1.719	-2.007	-1.792	-0.019
99	A	99	VAL	0	0.010	0.009	2.472	0.387	0.348	1.907	-0.377	-1.491	0.000
100	A	100	LEU	0	-0.026	-0.009	4.973	0.103	0.095	-0.001	-0.004	0.012	0.000
101	A	101	VAL	0	-0.007	0.001	7.692	0.052	0.052	0.000	0.000	0.000	0.000
102	A	102	VAL	0	-0.008	-0.015	9.364	0.027	0.027	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.015	-0.009	13.172	0.027	0.027	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.063	0.054	15.867	0.001	0.001	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.019	-0.022	18.387	0.009	0.009	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.848	-0.934	19.586	-0.048	-0.048	0.000	0.000	0.000	0.000
107	A	107	LYN	0	-0.023	0.012	22.278	0.002	0.002	0.000	0.000	0.000	0.000
108	A	108	VAL	0	0.025	0.010	21.868	-0.009	-0.009	0.000	0.000	0.000	0.000
109	A	109	PRO	0	0.010	0.006	21.965	0.001	0.001	0.000	0.000	0.000	0.000
110	A	110	PRO	0	0.059	0.028	22.297	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.812	-0.900	22.050	-0.139	-0.139	0.000	0.000	0.000	0.000
112	A	112	VAL	0	-0.020	-0.017	16.940	-0.022	-0.022	0.000	0.000	0.000	0.000
113	A	113	TYR	0	-0.036	-0.026	17.222	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.916	-0.950	18.147	-0.174	-0.174	0.000	0.000	0.000	0.000
115	A	115	LEU	0	-0.071	-0.034	17.417	-0.014	-0.014	0.000	0.000	0.000	0.000
116	A	116	CYS	0	-0.079	-0.021	13.121	-0.048	-0.048	0.000	0.000	0.000	0.000
117	A	117	ASP	-1	-0.758	-0.858	11.133	-0.561	-0.561	0.000	0.000	0.000	0.000
118	A	118	LEU	0	-0.034	-0.014	8.999	0.037	0.037	0.000	0.000	0.000	0.000
119	A	119	ASN	0	0.019	0.001	12.640	0.017	0.017	0.000	0.000	0.000	0.000
120	A	120	ILE	0	-0.018	-0.007	10.597	0.013	0.013	0.000	0.000	0.000	0.000
121	A	121	SER	0	-0.006	0.000	13.954	0.012	0.012	0.000	0.000	0.000	0.000
122	A	122	ILE	0	-0.031	-0.027	11.919	0.018	0.018	0.000	0.000	0.000	0.000
123	A	123	GLY	0	0.024	0.020	15.896	0.007	0.007	0.000	0.000	0.000	0.000
124	A	124	THR	0	0.014	0.011	19.294	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	125	GLN	0	-0.026	-0.026	21.966	0.000	0.000	0.000	0.000	0.000	0.000
126	A	126	PRO	0	0.041	0.024	22.441	0.002	0.002	0.000	0.000	0.000	0.000
127	A	127	HIS	0	-0.007	-0.017	17.740	0.008	0.008	0.000	0.000	0.000	0.000
128	A	128	SER	0	-0.038	-0.018	20.708	-0.002	-0.002	0.000	0.000	0.000	0.000
129	A	129	GLU	-1	-0.739	-0.876	17.322	0.006	0.006	0.000	0.000	0.000	0.000
130	A	130	VAL	0	-0.041	-0.014	16.238	0.007	0.007	0.000	0.000	0.000	0.000
131	A	131	ALA	0	0.011	0.009	16.158	0.022	0.022	0.000	0.000	0.000	0.000
132	A	132	ALA	0	0.007	-0.002	15.056	0.025	0.025	0.000	0.000	0.000	0.000
133	A	133	LEU	0	0.029	0.004	10.595	0.018	0.018	0.000	0.000	0.000	0.000
134	A	134	ALA	0	0.010	0.013	11.183	0.045	0.045	0.000	0.000	0.000	0.000
135	A	135	VAL	0	0.004	-0.003	11.615	0.061	0.061	0.000	0.000	0.000	0.000
136	A	136	PHE	0	0.011	0.001	6.124	0.081	0.081	0.000	0.000	0.000	0.000
137	A	137	LEU	0	0.000	-0.007	6.920	0.106	0.106	0.000	0.000	0.000	0.000
138	A	138	ASP	-1	-0.903	-0.947	7.291	0.623	0.623	0.000	0.000	0.000	0.000
139	A	139	ARG	1	0.952	0.981	8.152	-0.136	-0.136	0.000	0.000	0.000	0.000
140	A	140	VAL	0	-0.027	-0.021	2.343	-0.306	-0.247	1.342	-0.249	-1.151	0.001
141	A	141	LEU	0	-0.020	-0.007	2.611	-0.829	0.662	1.228	-0.639	-2.080	-0.004
142	A	142	GLY	0	-0.012	0.006	4.502	0.113	0.172	-0.001	-0.003	-0.055	0.000
143	A	143	LYS	1	0.943	0.956	5.366	-2.229	-2.229	0.000	0.000	0.000	0.000
144	A	144	VAL	0	-0.001	0.007	9.712	-0.062	-0.062	0.000	0.000	0.000	0.000
145	A	145	PHE	0	-0.058	-0.031	12.747	-0.067	-0.067	0.000	0.000	0.000	0.000
146	A	146	ASP	-1	-0.898	-0.934	12.129	0.651	0.651	0.000	0.000	0.000	0.000
147	A	147	ILE	0	-0.102	-0.037	10.093	0.000	0.000	0.000	0.000	0.000	0.000
148	A	148	SER	0	-0.042	-0.017	14.147	-0.076	-0.076	0.000	0.000	0.000	0.000
149	A	149	PHE	0	0.033	0.016	13.744	0.038	0.038	0.000	0.000	0.000	0.000
150	A	150	ASP	-1	-0.863	-0.935	18.156	0.263	0.263	0.000	0.000	0.000	0.000
151	A	151	ASP	-1	-0.844	-0.922	19.318	0.172	0.172	0.000	0.000	0.000	0.000
152	A	152	ALA	0	-0.066	-0.017	20.929	-0.021	-0.021	0.000	0.000	0.000	0.000
153	A	153	LYS	1	0.870	0.926	22.744	-0.084	-0.084	0.000	0.000	0.000	0.000
154	A	154	ILE	0	-0.040	0.004	25.243	-0.009	-0.009	0.000	0.000	0.000	0.000
155	A	155	LYS	1	0.862	0.924	22.035	-0.193	-0.193	0.000	0.000	0.000	0.000
156	A	156	VAL	0	-0.004	-0.003	23.795	-0.013	-0.013	0.000	0.000	0.000	0.000
157	A	157	ILE	0	0.015	0.009	24.518	0.015	0.015	0.000	0.000	0.000	0.000
158	A	158	PRO	0	0.039	0.015	23.499	-0.016	-0.016	0.000	0.000	0.000	0.000
159	A	159	SER	0	-0.049	-0.038	26.396	-0.010	-0.010	0.000	0.000	0.000	0.000
160	A	160	GLU	-1	-0.822	-0.899	29.086	0.109	0.109	0.000	0.000	0.000	0.000
161	A	161	ARG	1	0.860	0.920	31.091	-0.099	-0.099	0.000	0.000	0.000	0.000
162	A	162	GLY	0	0.039	0.030	32.004	-0.008	-0.008	0.000	0.000	0.000	0.000
163	A	163	LYS	1	0.924	0.958	30.709	-0.083	-0.083	0.000	0.000	0.000	0.000
164	A	164	ARG	1	0.931	0.973	30.047	-0.133	-0.133	0.000	0.000	0.000	0.000
165	A	165	VAL	0	-0.008	-0.005	27.686	0.010	0.010	0.000	0.000	0.000	0.000
166	A	166	VAL	0	0.014	0.017	27.551	-0.008	-0.008	0.000	0.000	0.000	0.000
167	A	167	SER	0	-0.018	-0.025	28.434	0.000	0.000	0.000	0.000	0.000	0.000

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