FMO DATABASE

FMODB ID: 5J32Z

Calculation Name: 5HS5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HS5

Chain ID: A

ChEMBL ID:

UniProt ID: Q2G0D1

Base Structure: X-ray

Registration Date: 2023-09-20

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	116
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1004671.197344
FMO2-HF: Nuclear repulsion	956321.743298
FMO2-HF: Total energy	-48349.454046
FMO2-MP2: Total energy	-48490.919617

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:8:THR)

Summations of interaction energy for fragment #1(A:8:THR)

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.
-3.238	-0.243	0.048	-1.153	-1.891	0.005

Interaction energy analysis for fragmet #1(A:8:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.082 / q_NPA : 0.027

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

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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	10	LEU	0	0.030	0.002	3.775	-2.428	-0.588	0.005	-0.834	-1.012	0.004
4	A	11	GLY	0	-0.002	0.001	3.100	-0.675	-0.154	0.044	-0.112	-0.453	0.001
5	A	12	PHE	0	0.094	0.045	3.806	0.222	0.764	0.000	-0.203	-0.339	0.000
6	A	13	TYR	0	-0.015	-0.005	5.356	0.716	0.808	-0.001	-0.004	-0.087	0.000
7	A	14	LYS	1	0.924	0.956	7.195	-0.673	-0.673	0.000	0.000	0.000	0.000
8	A	15	GLN	0	-0.012	-0.004	5.853	-0.318	-0.318	0.000	0.000	0.000	0.000
9	A	16	TYR	0	0.020	0.014	9.361	0.111	0.111	0.000	0.000	0.000	0.000
10	A	17	LYS	1	0.858	0.913	11.328	0.085	0.085	0.000	0.000	0.000	0.000
11	A	18	ALA	0	0.014	-0.003	12.920	0.027	0.027	0.000	0.000	0.000	0.000
12	A	19	LEU	0	0.053	0.027	13.346	0.024	0.024	0.000	0.000	0.000	0.000
13	A	20	SER	0	-0.009	-0.010	15.262	0.014	0.014	0.000	0.000	0.000	0.000
14	A	21	GLU	-1	-0.853	-0.904	17.290	0.016	0.016	0.000	0.000	0.000	0.000
15	A	22	TYR	0	-0.024	-0.016	18.335	0.017	0.017	0.000	0.000	0.000	0.000
16	A	23	ILE	0	0.010	0.001	17.985	0.007	0.007	0.000	0.000	0.000	0.000
17	A	24	ASP	-1	-0.868	-0.920	21.330	-0.021	-0.021	0.000	0.000	0.000	0.000
18	A	25	LYS	1	0.749	0.836	22.362	0.009	0.009	0.000	0.000	0.000	0.000
19	A	26	LYS	1	0.799	0.915	23.969	0.014	0.014	0.000	0.000	0.000	0.000
20	A	27	TYR	0	-0.060	-0.067	23.598	0.003	0.003	0.000	0.000	0.000	0.000
21	A	28	LYS	1	0.944	0.982	26.191	0.007	0.007	0.000	0.000	0.000	0.000
22	A	29	LEU	0	-0.027	-0.013	24.502	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	30	SER	0	0.011	-0.020	21.614	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	31	LEU	0	0.078	0.020	15.388	0.005	0.005	0.000	0.000	0.000	0.000
25	A	32	ASN	0	-0.011	-0.011	19.546	-0.018	-0.018	0.000	0.000	0.000	0.000
26	A	33	ASP	-1	-0.743	-0.815	22.246	-0.091	-0.091	0.000	0.000	0.000	0.000
27	A	34	LEU	0	0.053	0.027	19.976	0.006	0.006	0.000	0.000	0.000	0.000
28	A	35	ALA	0	0.031	0.027	20.414	0.003	0.003	0.000	0.000	0.000	0.000
29	A	36	VAL	0	-0.009	-0.013	22.181	0.008	0.008	0.000	0.000	0.000	0.000
30	A	37	LEU	0	0.007	0.007	25.408	0.007	0.007	0.000	0.000	0.000	0.000
31	A	38	ASP	-1	-0.787	-0.877	22.804	-0.152	-0.152	0.000	0.000	0.000	0.000
32	A	39	LEU	0	0.015	0.021	24.653	0.008	0.008	0.000	0.000	0.000	0.000
33	A	40	THR	0	-0.079	-0.068	26.949	0.011	0.011	0.000	0.000	0.000	0.000
34	A	41	MET	0	-0.017	-0.008	27.293	0.010	0.010	0.000	0.000	0.000	0.000
35	A	42	LYS	1	0.786	0.891	22.409	0.164	0.164	0.000	0.000	0.000	0.000
36	A	43	HIS	0	-0.055	-0.041	28.455	0.013	0.013	0.000	0.000	0.000	0.000
37	A	44	CYS	0	-0.095	-0.042	32.208	0.004	0.004	0.000	0.000	0.000	0.000
38	A	45	LYS	1	0.934	0.973	32.902	0.054	0.054	0.000	0.000	0.000	0.000
39	A	46	ASP	-1	-0.856	-0.920	34.664	-0.042	-0.042	0.000	0.000	0.000	0.000
40	A	47	GLU	-1	-0.829	-0.884	37.457	-0.043	-0.043	0.000	0.000	0.000	0.000
41	A	48	LYS	1	0.771	0.863	37.749	0.041	0.041	0.000	0.000	0.000	0.000
42	A	49	VAL	0	0.055	0.028	35.359	0.001	0.001	0.000	0.000	0.000	0.000
43	A	50	LEU	0	-0.026	-0.016	38.275	0.001	0.001	0.000	0.000	0.000	0.000
44	A	51	MET	0	0.011	0.003	34.927	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	52	GLN	0	0.035	0.006	36.106	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	53	SER	0	0.041	0.030	36.344	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	54	PHE	0	0.026	0.027	29.041	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	55	LEU	0	-0.027	-0.018	31.860	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.782	0.867	31.560	0.100	0.100	0.000	0.000	0.000	0.000
50	A	57	THR	0	0.001	-0.010	29.623	-0.005	-0.005	0.000	0.000	0.000	0.000
51	A	58	ALA	0	0.059	0.017	27.547	-0.009	-0.009	0.000	0.000	0.000	0.000
52	A	59	MET	0	-0.111	-0.046	26.710	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	60	ASP	-1	-0.797	-0.879	26.452	-0.130	-0.130	0.000	0.000	0.000	0.000
54	A	61	GLU	-1	-0.837	-0.912	24.858	-0.150	-0.150	0.000	0.000	0.000	0.000
55	A	62	LEU	0	-0.065	-0.033	21.740	-0.017	-0.017	0.000	0.000	0.000	0.000
56	A	63	ASP	-1	-0.904	-0.932	21.639	-0.215	-0.215	0.000	0.000	0.000	0.000
57	A	64	LEU	0	-0.052	-0.010	22.234	0.007	0.007	0.000	0.000	0.000	0.000
58	A	65	SER	0	0.039	-0.002	25.365	0.010	0.010	0.000	0.000	0.000	0.000
59	A	66	ARG	1	0.979	0.959	28.753	0.070	0.070	0.000	0.000	0.000	0.000
60	A	67	THR	0	-0.024	-0.013	31.235	0.003	0.003	0.000	0.000	0.000	0.000
61	A	68	LYS	1	0.989	0.998	23.038	0.154	0.154	0.000	0.000	0.000	0.000
62	A	69	LEU	0	0.046	0.042	26.998	0.005	0.005	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.016	-0.014	29.393	0.005	0.005	0.000	0.000	0.000	0.000
64	A	71	VAL	0	-0.038	-0.010	29.308	0.006	0.006	0.000	0.000	0.000	0.000
65	A	72	SER	0	0.003	-0.026	26.597	0.002	0.002	0.000	0.000	0.000	0.000
66	A	73	ILE	0	0.017	0.007	28.943	0.005	0.005	0.000	0.000	0.000	0.000
67	A	74	ARG	1	0.854	0.942	31.755	0.056	0.056	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.902	0.936	27.455	0.078	0.078	0.000	0.000	0.000	0.000
69	A	76	LEU	0	0.006	0.008	27.297	0.005	0.005	0.000	0.000	0.000	0.000
70	A	77	ILE	0	-0.047	-0.026	31.202	0.005	0.005	0.000	0.000	0.000	0.000
71	A	78	GLU	-1	-0.875	-0.917	33.409	-0.034	-0.034	0.000	0.000	0.000	0.000
72	A	79	LYS	1	0.753	0.860	30.302	0.042	0.042	0.000	0.000	0.000	0.000
73	A	80	GLU	-1	-0.899	-0.935	33.229	-0.026	-0.026	0.000	0.000	0.000	0.000
74	A	81	ARG	1	0.936	0.955	28.641	0.047	0.047	0.000	0.000	0.000	0.000
75	A	82	LEU	0	0.005	0.002	31.763	-0.006	-0.006	0.000	0.000	0.000	0.000
76	A	83	SER	0	-0.012	-0.005	34.019	0.005	0.005	0.000	0.000	0.000	0.000
77	A	84	LYS	1	0.894	0.926	37.432	0.036	0.036	0.000	0.000	0.000	0.000
78	A	85	VAL	0	0.000	0.018	39.788	0.003	0.003	0.000	0.000	0.000	0.000
79	A	86	ARG	1	0.888	0.917	43.034	0.033	0.033	0.000	0.000	0.000	0.000
80	A	87	SER	0	-0.011	0.030	45.771	0.002	0.002	0.000	0.000	0.000	0.000
81	A	88	SER	0	0.018	-0.014	48.154	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	89	LYS	1	0.885	0.938	51.431	0.034	0.034	0.000	0.000	0.000	0.000
83	A	90	ASP	-1	-0.768	-0.871	49.662	-0.034	-0.034	0.000	0.000	0.000	0.000
84	A	91	GLU	-1	-0.760	-0.885	48.973	-0.034	-0.034	0.000	0.000	0.000	0.000
85	A	92	ARG	1	0.903	0.958	46.574	0.036	0.036	0.000	0.000	0.000	0.000
86	A	93	LYS	1	0.834	0.920	44.695	0.038	0.038	0.000	0.000	0.000	0.000
87	A	94	ILE	0	-0.008	-0.013	40.472	0.002	0.002	0.000	0.000	0.000	0.000
88	A	95	TYR	0	-0.004	-0.005	40.084	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	96	ILE	0	-0.005	-0.009	33.553	0.003	0.003	0.000	0.000	0.000	0.000
90	A	97	TYR	0	0.006	-0.004	36.337	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	98	LEU	0	0.013	0.028	30.491	0.002	0.002	0.000	0.000	0.000	0.000
92	A	99	ASN	0	0.009	0.000	35.116	0.003	0.003	0.000	0.000	0.000	0.000
93	A	100	ASN	0	0.061	0.016	36.133	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	101	ASP	-1	-0.840	-0.906	36.168	-0.030	-0.030	0.000	0.000	0.000	0.000
95	A	102	ASP	-1	-0.755	-0.849	33.449	-0.047	-0.047	0.000	0.000	0.000	0.000
96	A	103	ILE	0	-0.021	-0.015	31.859	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	104	SER	0	-0.030	-0.020	31.290	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	105	LYS	1	0.770	0.872	31.235	0.033	0.033	0.000	0.000	0.000	0.000
99	A	106	PHE	0	-0.009	-0.009	24.816	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	107	ASN	0	0.005	-0.012	26.706	-0.009	-0.009	0.000	0.000	0.000	0.000
101	A	108	ALA	0	0.041	0.029	26.472	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	109	LEU	0	-0.046	-0.012	23.365	0.002	0.002	0.000	0.000	0.000	0.000
103	A	110	PHE	0	-0.027	-0.028	21.142	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	111	GLU	-1	-0.899	-0.930	21.338	-0.029	-0.029	0.000	0.000	0.000	0.000
105	A	112	ASP	-1	-0.748	-0.822	21.634	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	113	VAL	0	-0.035	-0.028	18.064	0.004	0.004	0.000	0.000	0.000	0.000
107	A	114	GLU	-1	-0.892	-0.950	16.999	-0.129	-0.129	0.000	0.000	0.000	0.000
108	A	115	GLN	0	-0.012	0.004	16.619	0.017	0.017	0.000	0.000	0.000	0.000
109	A	116	PHE	0	-0.035	-0.027	16.298	0.026	0.026	0.000	0.000	0.000	0.000
110	A	117	LEU	0	0.004	-0.002	10.816	0.015	0.015	0.000	0.000	0.000	0.000
111	A	118	ASN	0	0.016	0.006	12.379	0.006	0.006	0.000	0.000	0.000	0.000
112	A	119	ILE	0	-0.040	-0.022	13.194	0.058	0.058	0.000	0.000	0.000	0.000
113	A	120	LEU	0	-0.060	-0.027	10.835	0.062	0.062	0.000	0.000	0.000	0.000
114	A	121	GLU	-1	-0.897	-0.934	8.343	-0.289	-0.289	0.000	0.000	0.000	0.000
115	A	122	HIS	0	-0.040	-0.014	9.400	0.120	0.120	0.000	0.000	0.000	0.000
116	A	123	HIS	1	0.857	0.936	9.524	-0.264	-0.264	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:THR)