FMO DATABASE

FMODB ID: R8R68

Calculation Name: 4JOI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JOI

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H668

Base Structure: X-ray

Registration Date: 2023-09-24

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	141
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1336260.012213
FMO2-HF: Nuclear repulsion	1278535.10658
FMO2-HF: Total energy	-57724.905632
FMO2-MP2: Total energy	-57894.644395

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:24:LEU)

Summations of interaction energy for fragment #1(A:24: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.
0.545	2.29	-0.02	-0.875	-0.849	0.003

Interaction energy analysis for fragmet #1(A:24:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.041 / q_NPA : -0.002

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	26	PHE	0	-0.074	-0.046	3.783	-1.595	-0.002	-0.019	-0.867	-0.707	0.003
4	A	27	ALA	0	0.017	0.007	5.845	0.202	0.202	0.000	0.000	0.000	0.000
5	A	28	LYS	1	0.776	0.874	7.298	-0.606	-0.606	0.000	0.000	0.000	0.000
6	A	29	LEU	0	0.040	0.022	9.497	0.092	0.092	0.000	0.000	0.000	0.000
7	A	30	TYR	0	0.036	0.014	12.819	-0.057	-0.057	0.000	0.000	0.000	0.000
8	A	31	ILE	0	-0.021	-0.018	15.664	0.012	0.012	0.000	0.000	0.000	0.000
9	A	32	ARG	1	0.883	0.941	17.269	-0.135	-0.135	0.000	0.000	0.000	0.000
10	A	33	ASP	-1	-0.740	-0.842	14.775	0.294	0.294	0.000	0.000	0.000	0.000
11	A	34	ILE	0	-0.054	-0.030	12.227	-0.007	-0.007	0.000	0.000	0.000	0.000
12	A	35	LEU	0	-0.046	-0.018	14.587	-0.027	-0.027	0.000	0.000	0.000	0.000
13	A	36	ASP	-1	-0.901	-0.938	17.620	0.154	0.154	0.000	0.000	0.000	0.000
14	A	37	MET	0	-0.009	0.031	10.779	0.028	0.028	0.000	0.000	0.000	0.000
15	A	38	LYS	1	0.951	0.974	15.602	-0.157	-0.157	0.000	0.000	0.000	0.000
16	A	39	GLU	-1	-0.816	-0.909	13.930	0.009	0.009	0.000	0.000	0.000	0.000
17	A	40	SER	0	-0.037	-0.016	12.721	0.006	0.006	0.000	0.000	0.000	0.000
18	A	41	ARG	1	0.974	0.968	14.614	-0.037	-0.037	0.000	0.000	0.000	0.000
19	A	42	GLN	0	-0.015	-0.009	15.254	-0.022	-0.022	0.000	0.000	0.000	0.000
20	A	43	VAL	0	-0.012	-0.004	10.128	-0.022	-0.022	0.000	0.000	0.000	0.000
21	A	44	PRO	0	0.042	0.022	12.506	0.007	0.007	0.000	0.000	0.000	0.000
22	A	45	GLY	0	-0.039	-0.017	12.050	-0.044	-0.044	0.000	0.000	0.000	0.000
23	A	46	VAL	0	-0.075	-0.026	7.662	-0.050	-0.050	0.000	0.000	0.000	0.000
24	A	47	PHE	0	-0.003	-0.008	9.298	0.012	0.012	0.000	0.000	0.000	0.000
25	A	48	LEU	0	-0.019	-0.004	9.719	0.093	0.093	0.000	0.000	0.000	0.000
26	A	49	TYR	0	-0.022	-0.032	11.175	-0.057	-0.057	0.000	0.000	0.000	0.000
27	A	50	ASN	0	-0.023	-0.012	12.242	0.043	0.043	0.000	0.000	0.000	0.000
28	A	51	GLY	0	0.001	0.001	13.230	0.025	0.025	0.000	0.000	0.000	0.000
29	A	52	HIS	0	-0.033	-0.025	8.506	0.277	0.277	0.000	0.000	0.000	0.000
30	A	53	PRO	0	-0.049	-0.011	5.725	-0.110	-0.110	0.000	0.000	0.000	0.000
31	A	54	ILE	0	0.006	-0.005	5.584	0.418	0.418	0.000	0.000	0.000	0.000
32	A	55	LYS	1	0.931	0.960	4.938	0.387	0.387	0.000	0.000	0.000	0.000
33	A	56	GLN	0	-0.032	-0.022	4.567	0.215	0.367	-0.001	-0.008	-0.142	0.000
34	A	57	VAL	0	0.079	0.052	5.921	0.356	0.356	0.000	0.000	0.000	0.000
35	A	58	ASP	-1	-0.780	-0.864	8.697	-0.108	-0.108	0.000	0.000	0.000	0.000
36	A	59	VAL	0	0.053	0.038	11.322	0.076	0.076	0.000	0.000	0.000	0.000
37	A	60	LEU	0	-0.026	-0.029	14.809	-0.034	-0.034	0.000	0.000	0.000	0.000
38	A	61	GLY	0	0.042	0.022	18.227	0.018	0.018	0.000	0.000	0.000	0.000
39	A	62	THR	0	0.020	0.018	21.542	-0.013	-0.013	0.000	0.000	0.000	0.000
40	A	63	VAL	0	-0.033	-0.013	23.942	0.001	0.001	0.000	0.000	0.000	0.000
41	A	64	ILE	0	0.042	0.009	25.690	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	65	GLY	0	0.002	0.001	26.992	0.000	0.000	0.000	0.000	0.000	0.000
43	A	66	VAL	0	0.008	0.006	26.757	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	67	ARG	1	0.911	0.962	27.356	0.016	0.016	0.000	0.000	0.000	0.000
45	A	68	GLU	-1	-0.755	-0.859	27.420	-0.047	-0.047	0.000	0.000	0.000	0.000
46	A	69	ARG	1	0.903	0.952	27.673	0.037	0.037	0.000	0.000	0.000	0.000
47	A	70	ASP	-1	-0.854	-0.921	29.236	-0.051	-0.051	0.000	0.000	0.000	0.000
48	A	71	ALA	0	0.019	0.007	25.410	-0.002	-0.002	0.000	0.000	0.000	0.000
49	A	72	PHE	0	-0.019	-0.009	22.927	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	73	TYR	0	0.015	0.009	23.820	0.010	0.010	0.000	0.000	0.000	0.000
51	A	74	SER	0	-0.025	-0.013	22.905	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	75	TYR	0	0.035	-0.003	21.875	0.006	0.006	0.000	0.000	0.000	0.000
53	A	76	GLY	0	0.051	0.033	21.967	0.001	0.001	0.000	0.000	0.000	0.000
54	A	77	VAL	0	-0.029	-0.024	19.395	0.000	0.000	0.000	0.000	0.000	0.000
55	A	78	ASP	-1	-0.830	-0.919	21.633	0.074	0.074	0.000	0.000	0.000	0.000
56	A	79	ASP	-1	-0.736	-0.844	18.605	0.146	0.146	0.000	0.000	0.000	0.000
57	A	80	SER	0	-0.083	-0.033	21.618	0.015	0.015	0.000	0.000	0.000	0.000
58	A	81	THR	0	-0.053	-0.047	20.094	0.008	0.008	0.000	0.000	0.000	0.000
59	A	82	GLY	0	0.000	-0.019	21.440	0.000	0.000	0.000	0.000	0.000	0.000
60	A	83	VAL	0	0.020	0.004	21.961	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	84	ILE	0	0.003	0.007	16.416	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	85	ASN	0	0.004	0.016	20.504	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	86	CYS	0	-0.007	0.009	17.766	-0.002	-0.002	0.000	0.000	0.000	0.000
64	A	87	ILE	0	-0.006	-0.003	18.370	0.002	0.002	0.000	0.000	0.000	0.000
65	A	88	CYS	0	-0.048	-0.021	18.316	-0.022	-0.022	0.000	0.000	0.000	0.000
66	A	89	TRP	0	0.024	0.013	17.481	0.020	0.020	0.000	0.000	0.000	0.000
67	A	90	LYS	1	0.808	0.894	21.575	0.054	0.054	0.000	0.000	0.000	0.000
68	A	91	LYS	1	0.950	0.976	22.736	0.082	0.082	0.000	0.000	0.000	0.000
69	A	92	LEU	0	0.033	0.026	24.323	0.006	0.006	0.000	0.000	0.000	0.000
70	A	112	GLN	0	0.091	0.030	34.450	0.000	0.000	0.000	0.000	0.000	0.000
71	A	113	LEU	0	0.067	0.026	32.274	0.002	0.002	0.000	0.000	0.000	0.000
72	A	114	LYS	1	0.872	0.897	33.792	0.054	0.054	0.000	0.000	0.000	0.000
73	A	115	LYS	1	0.896	0.940	36.280	0.037	0.037	0.000	0.000	0.000	0.000
74	A	116	LEU	0	-0.009	0.009	36.239	0.002	0.002	0.000	0.000	0.000	0.000
75	A	117	GLN	0	-0.008	0.001	29.310	0.002	0.002	0.000	0.000	0.000	0.000
76	A	118	GLU	-1	-0.798	-0.856	32.806	-0.051	-0.051	0.000	0.000	0.000	0.000
77	A	119	THR	0	0.006	-0.011	33.948	0.001	0.001	0.000	0.000	0.000	0.000
78	A	120	ILE	0	0.008	0.008	33.452	0.003	0.003	0.000	0.000	0.000	0.000
79	A	121	GLU	-1	-0.893	-0.946	28.432	-0.062	-0.062	0.000	0.000	0.000	0.000
80	A	122	GLN	0	-0.045	-0.014	31.981	0.005	0.005	0.000	0.000	0.000	0.000
81	A	123	LYS	1	0.861	0.920	34.156	0.024	0.024	0.000	0.000	0.000	0.000
82	A	124	THR	0	0.018	0.005	31.376	0.002	0.002	0.000	0.000	0.000	0.000
83	A	125	LYS	1	0.830	0.908	29.387	0.038	0.038	0.000	0.000	0.000	0.000
84	A	126	ILE	0	-0.025	-0.006	23.616	0.003	0.003	0.000	0.000	0.000	0.000
85	A	127	GLU	-1	-0.968	-0.981	27.945	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	128	ILE	0	-0.037	-0.037	28.893	0.002	0.002	0.000	0.000	0.000	0.000
87	A	129	GLY	0	0.013	0.011	29.034	0.000	0.000	0.000	0.000	0.000	0.000
88	A	130	ASP	-1	-0.764	-0.849	26.509	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	131	THR	0	0.003	0.014	22.633	0.002	0.002	0.000	0.000	0.000	0.000
90	A	132	ILE	0	-0.024	-0.007	20.207	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	133	ARG	1	0.816	0.887	13.043	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	134	VAL	0	0.018	-0.004	14.509	-0.032	-0.032	0.000	0.000	0.000	0.000
93	A	135	ARG	1	0.862	0.941	9.374	0.262	0.262	0.000	0.000	0.000	0.000
94	A	136	GLY	0	0.071	0.028	10.587	-0.042	-0.042	0.000	0.000	0.000	0.000
95	A	137	SER	0	-0.057	-0.011	9.162	-0.057	-0.057	0.000	0.000	0.000	0.000
96	A	138	ILE	0	0.052	0.046	9.935	0.030	0.030	0.000	0.000	0.000	0.000
97	A	139	ARG	1	0.881	0.936	11.992	0.181	0.181	0.000	0.000	0.000	0.000
98	A	140	THR	0	0.047	0.026	14.988	0.024	0.024	0.000	0.000	0.000	0.000
99	A	141	TYR	0	-0.010	-0.012	18.147	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	142	ARG	1	0.901	0.944	21.309	0.038	0.038	0.000	0.000	0.000	0.000
101	A	143	GLU	-1	-0.945	-0.969	23.374	0.005	0.005	0.000	0.000	0.000	0.000
102	A	144	GLU	-1	-0.889	-0.919	22.380	0.025	0.025	0.000	0.000	0.000	0.000
103	A	145	ARG	1	0.794	0.878	15.161	-0.103	-0.103	0.000	0.000	0.000	0.000
104	A	146	GLU	-1	-0.864	-0.935	17.198	-0.044	-0.044	0.000	0.000	0.000	0.000
105	A	147	ILE	0	0.012	0.006	12.811	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	148	HIS	0	-0.077	-0.046	13.853	-0.023	-0.023	0.000	0.000	0.000	0.000
107	A	149	ALA	0	-0.005	-0.003	13.325	-0.043	-0.043	0.000	0.000	0.000	0.000
108	A	150	THR	0	-0.035	-0.037	10.655	-0.031	-0.031	0.000	0.000	0.000	0.000
109	A	151	THR	0	-0.056	-0.045	13.404	-0.013	-0.013	0.000	0.000	0.000	0.000
110	A	152	TYR	0	-0.014	-0.015	15.327	0.017	0.017	0.000	0.000	0.000	0.000
111	A	153	TYR	0	-0.025	-0.005	16.840	-0.006	-0.006	0.000	0.000	0.000	0.000
112	A	154	LYS	1	0.899	0.947	21.002	0.025	0.025	0.000	0.000	0.000	0.000
113	A	155	VAL	0	-0.080	-0.056	20.801	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	156	ASP	-1	-0.884	-0.937	23.755	0.008	0.008	0.000	0.000	0.000	0.000
115	A	157	ASP	-1	-0.764	-0.895	25.259	0.057	0.057	0.000	0.000	0.000	0.000
116	A	158	PRO	0	0.023	0.021	27.354	0.005	0.005	0.000	0.000	0.000	0.000
117	A	159	VAL	0	-0.020	-0.013	30.173	0.001	0.001	0.000	0.000	0.000	0.000
118	A	160	TRP	0	0.014	0.003	26.969	0.003	0.003	0.000	0.000	0.000	0.000
119	A	161	ASN	0	-0.008	0.008	25.883	0.012	0.012	0.000	0.000	0.000	0.000
120	A	162	ILE	0	0.005	-0.010	20.860	0.013	0.013	0.000	0.000	0.000	0.000
121	A	163	GLN	0	-0.036	-0.039	21.750	0.018	0.018	0.000	0.000	0.000	0.000
122	A	164	ILE	0	0.016	0.016	22.804	0.017	0.017	0.000	0.000	0.000	0.000
123	A	165	ALA	0	0.002	0.003	21.625	0.016	0.016	0.000	0.000	0.000	0.000
124	A	166	ARG	1	0.840	0.903	13.930	-0.165	-0.165	0.000	0.000	0.000	0.000
125	A	167	MET	0	0.002	-0.011	19.104	0.028	0.028	0.000	0.000	0.000	0.000
126	A	168	LEU	0	-0.026	-0.005	21.665	0.013	0.013	0.000	0.000	0.000	0.000
127	A	169	GLU	-1	-0.826	-0.895	15.313	0.320	0.320	0.000	0.000	0.000	0.000
128	A	170	LEU	0	0.001	-0.005	14.530	0.048	0.048	0.000	0.000	0.000	0.000
129	A	171	PRO	0	0.034	0.020	16.670	0.048	0.048	0.000	0.000	0.000	0.000
130	A	172	THR	0	-0.017	-0.006	17.437	0.010	0.010	0.000	0.000	0.000	0.000
131	A	173	ILE	0	-0.035	-0.013	11.532	0.028	0.028	0.000	0.000	0.000	0.000
132	A	174	TYR	0	-0.043	-0.048	13.812	0.130	0.130	0.000	0.000	0.000	0.000
133	A	175	ARG	1	0.979	1.002	15.467	-0.229	-0.229	0.000	0.000	0.000	0.000
134	A	176	LYS	1	0.908	0.953	14.959	-0.408	-0.408	0.000	0.000	0.000	0.000
135	A	177	VAL	0	-0.016	-0.009	9.253	0.025	0.025	0.000	0.000	0.000	0.000
136	A	178	TYR	0	-0.027	-0.023	8.294	0.084	0.084	0.000	0.000	0.000	0.000
137	A	179	ASP	-1	-0.790	-0.894	12.664	0.341	0.341	0.000	0.000	0.000	0.000
138	A	180	GLN	0	-0.099	-0.036	14.578	-0.092	-0.092	0.000	0.000	0.000	0.000
139	A	181	PRO	0	0.017	0.012	14.310	0.066	0.066	0.000	0.000	0.000	0.000
140	A	182	PHE	0	0.010	0.009	7.000	0.037	0.037	0.000	0.000	0.000	0.000
141	A	183	HIS	0	-0.046	-0.019	7.255	-0.078	-0.078	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:LEU)