FMO DATABASE

FMODB ID: KG393

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1000800.140461
FMO2-HF: Nuclear repulsion	952452.050955
FMO2-HF: Total energy	-48348.089506
FMO2-MP2: Total energy	-48489.547206

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.
-11.052	-7.431	0.34	-1.614	-2.349	0.009

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 : 0.043 / q_NPA : 0.011

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	0.026	-0.007	3.646	-2.267	-0.335	0.027	-0.877	-1.083	0.005
4	A	11	GLY	0	-0.007	0.001	2.778	-3.698	-2.507	0.306	-0.626	-0.871	0.003
5	A	12	PHE	0	0.079	0.041	3.493	-1.312	-0.814	0.007	-0.111	-0.395	0.001
6	A	13	TYR	0	-0.014	-0.013	5.404	-0.583	-0.583	0.000	0.000	0.000	0.000
7	A	14	LYS	1	0.932	0.965	7.035	-2.391	-2.391	0.000	0.000	0.000	0.000
8	A	15	GLN	0	0.020	0.014	6.444	0.225	0.225	0.000	0.000	0.000	0.000
9	A	16	TYR	0	0.022	0.021	9.290	-0.238	-0.238	0.000	0.000	0.000	0.000
10	A	17	LYS	1	0.870	0.918	11.410	-0.730	-0.730	0.000	0.000	0.000	0.000
11	A	18	ALA	0	0.003	-0.002	12.387	-0.111	-0.111	0.000	0.000	0.000	0.000
12	A	19	LEU	0	0.050	0.015	13.257	-0.095	-0.095	0.000	0.000	0.000	0.000
13	A	20	SER	0	-0.050	-0.022	15.098	-0.099	-0.099	0.000	0.000	0.000	0.000
14	A	21	GLU	-1	-0.843	-0.916	16.911	0.398	0.398	0.000	0.000	0.000	0.000
15	A	22	TYR	0	-0.082	-0.048	18.035	-0.046	-0.046	0.000	0.000	0.000	0.000
16	A	23	ILE	0	0.027	-0.003	18.458	-0.041	-0.041	0.000	0.000	0.000	0.000
17	A	24	ASP	-1	-0.939	-0.955	21.166	0.244	0.244	0.000	0.000	0.000	0.000
18	A	25	LYS	1	0.878	0.921	22.274	-0.304	-0.304	0.000	0.000	0.000	0.000
19	A	26	LYS	1	0.854	0.959	23.879	-0.222	-0.222	0.000	0.000	0.000	0.000
20	A	27	TYR	0	-0.076	-0.100	23.718	-0.029	-0.029	0.000	0.000	0.000	0.000
21	A	28	LYS	1	0.902	0.968	26.342	-0.187	-0.187	0.000	0.000	0.000	0.000
22	A	29	LEU	0	-0.034	-0.021	24.881	-0.019	-0.019	0.000	0.000	0.000	0.000
23	A	30	SER	0	0.011	-0.004	22.307	0.023	0.023	0.000	0.000	0.000	0.000
24	A	31	LEU	0	0.100	0.024	16.241	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	32	ASN	0	0.011	0.005	20.496	-0.023	-0.023	0.000	0.000	0.000	0.000
26	A	33	ASP	-1	-0.788	-0.878	22.946	0.146	0.146	0.000	0.000	0.000	0.000
27	A	34	LEU	0	0.037	0.016	20.967	-0.016	-0.016	0.000	0.000	0.000	0.000
28	A	35	ALA	0	0.041	0.033	21.123	-0.016	-0.016	0.000	0.000	0.000	0.000
29	A	36	VAL	0	-0.027	-0.016	22.738	-0.021	-0.021	0.000	0.000	0.000	0.000
30	A	37	LEU	0	-0.006	-0.004	26.214	-0.012	-0.012	0.000	0.000	0.000	0.000
31	A	38	ASP	-1	-0.852	-0.935	23.511	0.034	0.034	0.000	0.000	0.000	0.000
32	A	39	LEU	0	0.010	0.013	25.587	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	40	THR	0	-0.117	-0.063	27.436	-0.010	-0.010	0.000	0.000	0.000	0.000
34	A	41	MET	0	0.027	0.011	28.047	-0.007	-0.007	0.000	0.000	0.000	0.000
35	A	42	LYS	1	0.893	0.960	23.148	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	43	HIS	0	-0.020	-0.015	29.117	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	44	CYS	0	-0.070	-0.031	32.671	0.000	0.000	0.000	0.000	0.000	0.000
38	A	45	LYS	1	0.936	0.959	33.516	-0.014	-0.014	0.000	0.000	0.000	0.000
39	A	46	ASP	-1	-0.898	-0.932	35.159	0.021	0.021	0.000	0.000	0.000	0.000
40	A	47	GLU	-1	-0.865	-0.911	38.247	0.009	0.009	0.000	0.000	0.000	0.000
41	A	48	LYS	1	0.818	0.904	38.607	-0.012	-0.012	0.000	0.000	0.000	0.000
42	A	49	VAL	0	0.060	0.032	36.119	-0.003	-0.003	0.000	0.000	0.000	0.000
43	A	50	LEU	0	-0.061	-0.026	39.087	0.005	0.005	0.000	0.000	0.000	0.000
44	A	51	MET	0	0.032	0.023	35.382	0.000	0.000	0.000	0.000	0.000	0.000
45	A	52	GLN	0	0.019	-0.004	36.755	0.005	0.005	0.000	0.000	0.000	0.000
46	A	53	SER	0	0.009	0.017	37.191	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	54	PHE	0	0.066	0.031	29.708	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	55	LEU	0	-0.018	-0.026	32.636	0.001	0.001	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.903	0.964	32.097	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	57	THR	0	0.077	0.032	29.905	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	58	ALA	0	0.019	0.006	28.419	-0.002	-0.002	0.000	0.000	0.000	0.000
52	A	59	MET	0	-0.126	-0.069	27.256	0.004	0.004	0.000	0.000	0.000	0.000
53	A	60	ASP	-1	-0.954	-0.960	27.259	-0.020	-0.020	0.000	0.000	0.000	0.000
54	A	61	GLU	-1	-0.911	-0.960	25.163	-0.018	-0.018	0.000	0.000	0.000	0.000
55	A	62	LEU	0	-0.061	-0.036	22.240	0.001	0.001	0.000	0.000	0.000	0.000
56	A	63	ASP	-1	-0.909	-0.933	22.028	0.045	0.045	0.000	0.000	0.000	0.000
57	A	64	LEU	0	-0.032	-0.006	23.134	0.022	0.022	0.000	0.000	0.000	0.000
58	A	65	SER	0	0.013	-0.007	25.764	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	66	ARG	1	1.001	0.971	29.085	-0.042	-0.042	0.000	0.000	0.000	0.000
60	A	67	THR	0	-0.045	-0.032	31.809	0.000	0.000	0.000	0.000	0.000	0.000
61	A	68	LYS	1	0.983	0.981	23.726	-0.161	-0.161	0.000	0.000	0.000	0.000
62	A	69	LEU	0	0.074	0.060	27.581	0.007	0.007	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.009	-0.009	30.088	0.000	0.000	0.000	0.000	0.000	0.000
64	A	71	VAL	0	-0.057	-0.013	30.128	0.001	0.001	0.000	0.000	0.000	0.000
65	A	72	SER	0	0.019	-0.004	27.251	0.003	0.003	0.000	0.000	0.000	0.000
66	A	73	ILE	0	-0.010	0.006	29.788	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	74	ARG	1	0.887	0.945	32.671	-0.077	-0.077	0.000	0.000	0.000	0.000
68	A	75	ARG	1	0.910	0.945	27.732	-0.161	-0.161	0.000	0.000	0.000	0.000
69	A	76	LEU	0	0.022	0.016	28.366	0.002	0.002	0.000	0.000	0.000	0.000
70	A	77	ILE	0	-0.048	-0.022	32.281	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	78	GLU	-1	-1.015	-1.008	35.057	0.103	0.103	0.000	0.000	0.000	0.000
72	A	79	LYS	1	0.895	0.965	30.171	-0.143	-0.143	0.000	0.000	0.000	0.000
73	A	80	GLU	-1	-0.942	-0.971	34.155	0.075	0.075	0.000	0.000	0.000	0.000
74	A	81	ARG	1	0.941	0.965	29.571	-0.127	-0.127	0.000	0.000	0.000	0.000
75	A	82	LEU	0	0.032	0.021	32.661	-0.003	-0.003	0.000	0.000	0.000	0.000
76	A	83	SER	0	0.013	0.010	34.830	0.002	0.002	0.000	0.000	0.000	0.000
77	A	84	LYS	1	0.904	0.942	38.358	-0.054	-0.054	0.000	0.000	0.000	0.000
78	A	85	VAL	0	-0.009	-0.008	40.686	0.000	0.000	0.000	0.000	0.000	0.000
79	A	86	ARG	1	0.842	0.902	44.206	-0.039	-0.039	0.000	0.000	0.000	0.000
80	A	87	SER	0	-0.010	0.103	46.649	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	88	SER	0	0.011	-0.074	48.878	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	89	LYS	1	0.914	0.932	51.954	-0.013	-0.013	0.000	0.000	0.000	0.000
83	A	90	ASP	-1	-0.763	-0.864	50.056	0.015	0.015	0.000	0.000	0.000	0.000
84	A	91	GLU	-1	-0.749	-0.880	49.548	0.034	0.034	0.000	0.000	0.000	0.000
85	A	92	ARG	1	0.902	0.956	47.202	-0.022	-0.022	0.000	0.000	0.000	0.000
86	A	93	LYS	1	0.839	0.916	45.245	-0.013	-0.013	0.000	0.000	0.000	0.000
87	A	94	ILE	0	-0.013	0.002	41.381	0.001	0.001	0.000	0.000	0.000	0.000
88	A	95	TYR	0	0.008	-0.011	41.019	-0.002	-0.002	0.000	0.000	0.000	0.000
89	A	96	ILE	0	-0.021	-0.025	34.324	0.004	0.004	0.000	0.000	0.000	0.000
90	A	97	TYR	0	0.012	-0.012	37.108	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	98	LEU	0	0.029	0.039	31.667	0.005	0.005	0.000	0.000	0.000	0.000
92	A	99	ASN	0	0.046	0.042	36.177	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	100	ASN	0	0.073	0.011	36.972	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	101	ASP	-1	-0.903	-0.960	37.094	0.063	0.063	0.000	0.000	0.000	0.000
95	A	102	ASP	-1	-0.819	-0.908	34.443	0.066	0.066	0.000	0.000	0.000	0.000
96	A	103	ILE	0	-0.019	-0.009	32.816	0.005	0.005	0.000	0.000	0.000	0.000
97	A	104	SER	0	0.009	0.013	32.058	0.000	0.000	0.000	0.000	0.000	0.000
98	A	105	LYS	1	0.883	0.937	31.656	-0.076	-0.076	0.000	0.000	0.000	0.000
99	A	106	PHE	0	-0.037	-0.008	25.698	0.013	0.013	0.000	0.000	0.000	0.000
100	A	107	ASN	0	0.011	-0.016	27.479	0.007	0.007	0.000	0.000	0.000	0.000
101	A	108	ALA	0	0.025	0.028	27.338	0.004	0.004	0.000	0.000	0.000	0.000
102	A	109	LEU	0	-0.059	-0.032	23.797	0.013	0.013	0.000	0.000	0.000	0.000
103	A	110	PHE	0	0.001	-0.017	21.518	0.026	0.026	0.000	0.000	0.000	0.000
104	A	111	GLU	-1	-0.893	-0.905	21.984	0.088	0.088	0.000	0.000	0.000	0.000
105	A	112	ASP	-1	-0.748	-0.805	22.374	0.222	0.222	0.000	0.000	0.000	0.000
106	A	113	VAL	0	-0.056	-0.053	18.938	0.032	0.032	0.000	0.000	0.000	0.000
107	A	114	GLU	-1	-0.918	-0.970	17.846	0.138	0.138	0.000	0.000	0.000	0.000
108	A	115	GLN	0	0.003	0.010	17.284	0.017	0.017	0.000	0.000	0.000	0.000
109	A	116	PHE	0	-0.062	-0.039	15.902	0.040	0.040	0.000	0.000	0.000	0.000
110	A	117	LEU	0	-0.001	-0.008	12.012	0.080	0.080	0.000	0.000	0.000	0.000
111	A	118	ASN	0	0.057	0.035	12.812	0.045	0.045	0.000	0.000	0.000	0.000
112	A	119	ILE	0	-0.053	-0.018	13.420	0.023	0.023	0.000	0.000	0.000	0.000
113	A	120	LEU	0	-0.054	-0.041	10.690	0.078	0.078	0.000	0.000	0.000	0.000
114	A	121	GLU	-1	-0.920	-0.957	8.706	0.700	0.700	0.000	0.000	0.000	0.000
115	A	122	HIS	0	-0.123	-0.033	9.133	-0.166	-0.166	0.000	0.000	0.000	0.000
116	A	123	HIS	1	0.908	0.959	9.486	-0.422	-0.422	0.000	0.000	0.000	0.000

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