FMO DATABASE

FMODB ID: 858VY

Calculation Name: 4JOX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JOX

Chain ID: A

ChEMBL ID:

UniProt ID: Q939T0

Base Structure: X-ray

Registration Date: 2023-06-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

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	118
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-933484.55406
FMO2-HF: Nuclear repulsion	887974.624283
FMO2-HF: Total energy	-45509.929777
FMO2-MP2: Total energy	-45644.446811

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:3:ALA)

Summations of interaction energy for fragment #1(A:3:ALA)

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.
-2.202	1.291	0.143	-1.577	-2.058	-0.002

Interaction energy analysis for fragmet #1(A:3:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.040 / q_NPA : -0.026

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	5	GLU	-1	-0.852	-0.932	3.480	-3.995	-2.221	0.038	-0.802	-1.010	0.003
4	A	6	VAL	0	-0.010	0.010	5.997	0.310	0.310	0.000	0.000	0.000	0.000
5	A	7	HIS	0	-0.029	-0.014	8.482	0.120	0.120	0.000	0.000	0.000	0.000
6	A	8	ILE	0	0.004	-0.004	12.366	0.054	0.054	0.000	0.000	0.000	0.000
7	A	9	ASP	-1	-0.825	-0.891	15.729	-0.205	-0.205	0.000	0.000	0.000	0.000
8	A	10	VAL	0	0.002	0.004	19.145	0.019	0.019	0.000	0.000	0.000	0.000
9	A	11	ASN	0	0.000	-0.018	22.030	-0.001	-0.001	0.000	0.000	0.000	0.000
10	A	12	ASN	0	-0.015	0.014	25.461	0.013	0.013	0.000	0.000	0.000	0.000
11	A	13	LYS	1	0.848	0.915	28.335	0.053	0.053	0.000	0.000	0.000	0.000
12	A	14	THR	0	0.003	-0.020	30.485	0.005	0.005	0.000	0.000	0.000	0.000
13	A	15	GLY	0	0.016	0.025	33.172	0.004	0.004	0.000	0.000	0.000	0.000
14	A	16	HIS	0	-0.028	-0.017	34.039	0.001	0.001	0.000	0.000	0.000	0.000
15	A	17	THR	0	-0.036	-0.018	30.486	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	18	LEU	0	-0.007	0.009	25.860	0.004	0.004	0.000	0.000	0.000	0.000
17	A	19	GLN	0	-0.027	-0.033	27.670	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.005	0.005	21.239	0.003	0.003	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.826	-0.931	24.846	0.006	0.006	0.000	0.000	0.000	0.000
20	A	22	ASP	-1	-0.900	-0.968	23.792	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	23	LYS	1	0.744	0.894	23.171	-0.020	-0.020	0.000	0.000	0.000	0.000
22	A	24	THR	0	-0.026	0.009	18.764	0.009	0.009	0.000	0.000	0.000	0.000
23	A	25	LYS	1	0.938	0.968	17.457	-0.119	-0.119	0.000	0.000	0.000	0.000
24	A	26	LEU	0	-0.046	-0.015	11.140	-0.008	-0.008	0.000	0.000	0.000	0.000
25	A	27	ASP	-1	-0.902	-0.964	14.340	0.174	0.174	0.000	0.000	0.000	0.000
26	A	28	GLY	0	0.006	0.004	10.856	0.057	0.057	0.000	0.000	0.000	0.000
27	A	29	GLY	0	-0.004	0.004	7.643	-0.008	-0.008	0.000	0.000	0.000	0.000
28	A	30	ARG	1	0.872	0.937	6.461	0.293	0.293	0.000	0.000	0.000	0.000
29	A	31	TRP	0	0.072	0.017	9.208	-0.106	-0.106	0.000	0.000	0.000	0.000
30	A	32	ARG	1	0.775	0.866	5.659	1.065	1.065	0.000	0.000	0.000	0.000
31	A	33	THR	0	-0.038	-0.018	11.322	0.027	0.027	0.000	0.000	0.000	0.000
32	A	34	SER	0	0.010	0.002	14.335	-0.012	-0.012	0.000	0.000	0.000	0.000
33	A	35	PRO	0	0.020	0.010	16.021	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	36	THR	0	-0.005	-0.017	18.940	0.006	0.006	0.000	0.000	0.000	0.000
35	A	37	ASN	0	0.029	0.027	22.535	0.005	0.005	0.000	0.000	0.000	0.000
36	A	38	VAL	0	-0.001	0.010	23.558	-0.010	-0.010	0.000	0.000	0.000	0.000
37	A	39	ALA	0	0.024	0.013	26.550	0.008	0.008	0.000	0.000	0.000	0.000
38	A	40	ASN	0	0.079	0.020	29.437	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	41	ASP	-1	-0.912	-0.943	31.175	-0.051	-0.051	0.000	0.000	0.000	0.000
40	A	42	GLN	0	-0.010	0.000	26.148	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	43	ILE	0	0.015	0.002	22.110	0.004	0.004	0.000	0.000	0.000	0.000
42	A	44	LYS	1	0.858	0.946	21.124	0.099	0.099	0.000	0.000	0.000	0.000
43	A	45	THR	0	0.019	0.004	15.314	0.008	0.008	0.000	0.000	0.000	0.000
44	A	46	PHE	0	-0.051	-0.012	15.745	0.006	0.006	0.000	0.000	0.000	0.000
45	A	47	VAL	0	0.016	-0.003	9.220	-0.022	-0.022	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.028	0.028	9.417	0.043	0.043	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.866	-0.923	5.069	-0.963	-0.963	0.000	0.000	0.000	0.000
48	A	50	SER	0	0.003	0.023	3.417	0.597	1.048	0.023	-0.145	-0.329	0.000
49	A	51	ASN	0	-0.019	-0.040	3.154	-1.681	-0.484	0.084	-0.601	-0.680	-0.005
50	A	52	GLY	0	0.053	0.027	5.203	-0.448	-0.448	0.000	0.000	0.000	0.000
51	A	53	PHE	0	-0.039	-0.021	4.910	0.858	0.945	-0.001	-0.002	-0.083	0.000
52	A	54	MET	0	-0.034	-0.016	6.800	-0.213	-0.213	0.000	0.000	0.000	0.000
53	A	55	THR	0	0.008	0.018	6.805	-0.366	-0.366	0.000	0.000	0.000	0.000
54	A	56	GLY	0	0.004	-0.019	6.369	1.097	1.097	0.000	0.000	0.000	0.000
55	A	57	THR	0	-0.069	-0.030	6.383	-0.099	-0.099	0.000	0.000	0.000	0.000
56	A	58	GLU	-1	-0.882	-0.920	8.246	0.284	0.284	0.000	0.000	0.000	0.000
57	A	59	GLY	0	0.035	0.025	12.002	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	60	THR	0	-0.008	0.004	14.897	-0.011	-0.011	0.000	0.000	0.000	0.000
59	A	61	ILE	0	-0.035	-0.020	16.678	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	62	TYR	0	0.001	-0.003	19.798	0.006	0.006	0.000	0.000	0.000	0.000
61	A	63	TYR	0	-0.024	-0.032	22.046	-0.010	-0.010	0.000	0.000	0.000	0.000
62	A	64	SER	0	0.039	0.034	26.158	0.005	0.005	0.000	0.000	0.000	0.000
63	A	65	ILE	0	-0.012	-0.015	29.904	-0.006	-0.006	0.000	0.000	0.000	0.000
64	A	66	ASN	0	0.025	-0.001	32.516	0.004	0.004	0.000	0.000	0.000	0.000
65	A	67	GLY	0	0.002	0.018	34.654	0.001	0.001	0.000	0.000	0.000	0.000
66	A	68	GLU	-1	-0.916	-0.960	35.909	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	69	ALA	0	-0.061	-0.044	33.188	0.003	0.003	0.000	0.000	0.000	0.000
68	A	70	GLU	-1	-0.868	-0.931	27.879	0.016	0.016	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.027	-0.018	25.056	0.001	0.001	0.000	0.000	0.000	0.000
70	A	72	SER	0	0.013	-0.002	23.528	0.002	0.002	0.000	0.000	0.000	0.000
71	A	73	LEU	0	-0.042	-0.016	20.065	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	74	TYR	0	-0.044	-0.018	16.582	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	75	PHE	0	-0.022	-0.016	11.537	-0.033	-0.033	0.000	0.000	0.000	0.000
74	A	76	ASP	-1	-0.808	-0.915	12.396	0.437	0.437	0.000	0.000	0.000	0.000
75	A	77	ASN	0	-0.016	-0.006	8.255	0.123	0.123	0.000	0.000	0.000	0.000
76	A	78	PRO	0	0.026	0.006	8.573	0.287	0.287	0.000	0.000	0.000	0.000
77	A	79	PHE	0	-0.022	-0.008	6.809	0.089	0.089	0.000	0.000	0.000	0.000
78	A	80	ALA	0	-0.010	-0.013	8.431	0.009	0.009	0.000	0.000	0.000	0.000
79	A	81	GLY	0	0.009	-0.001	11.179	-0.036	-0.036	0.000	0.000	0.000	0.000
80	A	82	SER	0	-0.069	-0.027	13.363	-0.039	-0.039	0.000	0.000	0.000	0.000
81	A	83	ASN	0	0.001	-0.008	11.372	0.113	0.113	0.000	0.000	0.000	0.000
82	A	84	LYS	1	0.887	0.942	14.124	-0.237	-0.237	0.000	0.000	0.000	0.000
83	A	85	TYR	0	-0.006	-0.042	13.718	-0.015	-0.015	0.000	0.000	0.000	0.000
84	A	86	ASP	-1	-0.885	-0.935	18.353	0.036	0.036	0.000	0.000	0.000	0.000
85	A	87	GLY	0	-0.003	0.001	21.243	-0.007	-0.007	0.000	0.000	0.000	0.000
86	A	88	HIS	0	-0.015	-0.008	23.792	0.001	0.001	0.000	0.000	0.000	0.000
87	A	89	SER	0	0.050	0.017	26.930	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	90	ASN	0	0.019	0.017	29.982	0.000	0.000	0.000	0.000	0.000	0.000
89	A	91	LYS	1	0.956	0.985	32.337	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	92	SER	0	-0.011	-0.011	34.449	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	93	GLN	0	-0.025	-0.018	36.541	0.001	0.001	0.000	0.000	0.000	0.000
92	A	94	TYR	0	-0.050	-0.026	31.861	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	95	GLU	-1	-0.904	-0.959	31.211	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	96	ILE	0	-0.036	-0.004	24.367	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	97	ILE	0	-0.025	0.005	25.899	0.005	0.005	0.000	0.000	0.000	0.000
96	A	98	THR	0	0.045	0.006	20.646	-0.012	-0.012	0.000	0.000	0.000	0.000
97	A	99	GLN	0	-0.018	0.003	21.546	0.018	0.018	0.000	0.000	0.000	0.000
98	A	100	GLY	0	0.047	0.011	17.293	-0.020	-0.020	0.000	0.000	0.000	0.000
99	A	101	GLY	0	-0.049	0.002	15.291	0.022	0.022	0.000	0.000	0.000	0.000
100	A	102	SER	0	0.029	0.033	14.389	0.014	0.014	0.000	0.000	0.000	0.000
101	A	103	GLY	0	-0.013	-0.021	11.575	-0.060	-0.060	0.000	0.000	0.000	0.000
102	A	104	ASN	0	0.018	0.007	4.433	0.183	0.167	-0.001	-0.027	0.044	0.000
103	A	105	GLN	0	-0.011	0.009	5.527	-0.049	-0.049	0.000	0.000	0.000	0.000
104	A	106	SER	0	-0.049	-0.026	7.727	0.183	0.183	0.000	0.000	0.000	0.000
105	A	107	HIS	0	0.056	0.022	11.028	-0.079	-0.079	0.000	0.000	0.000	0.000
106	A	108	VAL	0	0.015	0.017	13.995	0.049	0.049	0.000	0.000	0.000	0.000
107	A	109	THR	0	-0.036	-0.019	16.789	-0.017	-0.017	0.000	0.000	0.000	0.000
108	A	110	TYR	0	0.014	-0.012	17.532	0.007	0.007	0.000	0.000	0.000	0.000
109	A	111	THR	0	-0.034	-0.020	22.398	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	112	ILE	0	-0.022	-0.008	24.371	0.009	0.009	0.000	0.000	0.000	0.000
111	A	113	GLN	0	0.000	-0.010	28.066	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	114	THR	0	0.050	0.028	31.627	0.005	0.005	0.000	0.000	0.000	0.000
113	A	115	THR	0	-0.060	-0.004	35.190	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	116	SER	0	0.028	0.014	36.264	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	117	SER	0	-0.047	-0.025	38.767	0.003	0.003	0.000	0.000	0.000	0.000
116	A	118	ARG	1	0.960	0.970	35.961	0.001	0.001	0.000	0.000	0.000	0.000
117	A	119	TYR	0	-0.017	-0.002	42.125	0.001	0.001	0.000	0.000	0.000	0.000
118	A	120	GLY	0	0.040	0.025	45.403	0.001	0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ALA)