FMO DATABASE

FMODB ID: 76MGK

Calculation Name: 5HY6-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HY6

Chain ID: A

ChEMBL ID:

UniProt ID: P62925

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1131218.730436
FMO2-HF: Nuclear repulsion	1074794.333089
FMO2-HF: Total energy	-56424.397347
FMO2-MP2: Total energy	-56581.670986

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:16:ALA)

Summations of interaction energy for fragment #1(A:16: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.
-1.8	-0.637	-0.008	-0.563	-0.591	0.002

Interaction energy analysis for fragmet #1(A:16:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.008 / q_NPA : -0.012

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	18	ALA	0	0.056	0.029	3.863	-0.344	0.819	-0.008	-0.563	-0.591	0.002
4	A	19	THR	0	-0.048	-0.047	6.681	0.278	0.278	0.000	0.000	0.000	0.000
5	A	20	PHE	0	-0.024	-0.005	7.559	0.546	0.546	0.000	0.000	0.000	0.000
6	A	21	PRO	0	0.023	0.011	9.642	-0.217	-0.217	0.000	0.000	0.000	0.000
7	A	22	MET	0	0.005	0.017	13.114	0.068	0.068	0.000	0.000	0.000	0.000
8	A	23	GLN	0	0.025	0.017	16.106	-0.053	-0.053	0.000	0.000	0.000	0.000
9	A	24	CYS	0	0.006	0.013	19.706	-0.004	-0.004	0.000	0.000	0.000	0.000
10	A	25	SER	0	-0.018	-0.012	22.097	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	26	ALA	0	-0.022	-0.006	19.852	-0.014	-0.014	0.000	0.000	0.000	0.000
12	A	27	LEU	0	0.034	0.041	18.306	0.010	0.010	0.000	0.000	0.000	0.000
13	A	28	ARG	1	0.854	0.900	21.421	-0.230	-0.230	0.000	0.000	0.000	0.000
14	A	29	LYS	1	0.946	0.950	22.620	-0.083	-0.083	0.000	0.000	0.000	0.000
15	A	30	ASN	0	-0.018	-0.008	23.266	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	31	GLY	0	0.032	0.036	19.493	0.006	0.006	0.000	0.000	0.000	0.000
17	A	32	PHE	0	0.006	-0.012	15.101	-0.036	-0.036	0.000	0.000	0.000	0.000
18	A	33	VAL	0	-0.013	-0.022	16.137	0.044	0.044	0.000	0.000	0.000	0.000
19	A	34	MET	0	0.006	0.024	12.295	-0.038	-0.038	0.000	0.000	0.000	0.000
20	A	35	LEU	0	-0.046	-0.024	16.764	0.015	0.015	0.000	0.000	0.000	0.000
21	A	36	LYS	1	0.818	0.877	20.252	-0.048	-0.048	0.000	0.000	0.000	0.000
22	A	37	GLY	0	0.006	0.017	16.551	-0.019	-0.019	0.000	0.000	0.000	0.000
23	A	38	ARG	1	0.779	0.849	16.394	0.077	0.077	0.000	0.000	0.000	0.000
24	A	39	PRO	0	0.064	0.031	13.698	0.048	0.048	0.000	0.000	0.000	0.000
25	A	40	CYS	0	-0.039	-0.014	15.798	-0.019	-0.019	0.000	0.000	0.000	0.000
26	A	41	LYS	1	0.897	0.946	17.945	-0.057	-0.057	0.000	0.000	0.000	0.000
27	A	42	ILE	0	-0.014	-0.002	20.362	-0.022	-0.022	0.000	0.000	0.000	0.000
28	A	43	VAL	0	-0.023	-0.009	22.973	0.002	0.002	0.000	0.000	0.000	0.000
29	A	44	GLU	-1	-0.844	-0.908	26.670	0.051	0.051	0.000	0.000	0.000	0.000
30	A	45	MET	0	-0.004	0.005	24.491	0.008	0.008	0.000	0.000	0.000	0.000
31	A	46	SER	0	-0.019	0.008	28.480	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	47	THR	0	0.016	0.006	30.292	0.006	0.006	0.000	0.000	0.000	0.000
33	A	48	SER	0	0.036	0.021	32.584	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	49	LYS	1	0.974	0.979	33.875	-0.036	-0.036	0.000	0.000	0.000	0.000
35	A	50	THR	0	0.040	0.019	33.654	0.003	0.003	0.000	0.000	0.000	0.000
36	A	51	GLY	0	0.037	0.023	35.773	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	52	LYS	1	0.924	0.953	37.765	-0.051	-0.051	0.000	0.000	0.000	0.000
38	A	53	HIS	0	0.010	-0.005	37.296	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	54	GLY	0	0.018	0.030	34.267	0.001	0.001	0.000	0.000	0.000	0.000
40	A	55	HIS	0	0.013	0.004	31.181	0.004	0.004	0.000	0.000	0.000	0.000
41	A	56	ALA	0	0.006	0.006	29.155	0.000	0.000	0.000	0.000	0.000	0.000
42	A	57	LYS	1	0.850	0.912	29.083	-0.063	-0.063	0.000	0.000	0.000	0.000
43	A	58	VAL	0	0.015	0.019	26.392	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	59	HIS	0	-0.069	-0.042	27.315	0.007	0.007	0.000	0.000	0.000	0.000
45	A	60	LEU	0	0.011	-0.002	22.327	0.008	0.008	0.000	0.000	0.000	0.000
46	A	61	VAL	0	0.057	0.022	25.983	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	62	GLY	0	0.027	0.003	22.840	0.014	0.014	0.000	0.000	0.000	0.000
48	A	63	ILE	0	-0.024	-0.004	23.069	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	64	ASP	-1	-0.728	-0.857	20.008	-0.039	-0.039	0.000	0.000	0.000	0.000
50	A	65	ILE	0	-0.080	-0.045	14.507	0.005	0.005	0.000	0.000	0.000	0.000
51	A	66	PHE	0	0.016	0.014	13.985	0.003	0.003	0.000	0.000	0.000	0.000
52	A	67	ASN	0	-0.027	-0.017	20.034	0.003	0.003	0.000	0.000	0.000	0.000
53	A	68	GLY	0	0.043	0.023	22.956	0.003	0.003	0.000	0.000	0.000	0.000
54	A	69	LYS	1	0.901	0.956	24.456	0.045	0.045	0.000	0.000	0.000	0.000
55	A	70	LYS	1	0.841	0.907	24.538	-0.034	-0.034	0.000	0.000	0.000	0.000
56	A	71	TYR	0	0.010	0.004	22.490	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	72	GLU	-1	-0.849	-0.921	25.181	0.048	0.048	0.000	0.000	0.000	0.000
58	A	73	ASP	-1	-0.801	-0.894	22.719	0.039	0.039	0.000	0.000	0.000	0.000
59	A	74	ILE	0	-0.044	-0.020	25.308	0.005	0.005	0.000	0.000	0.000	0.000
60	A	75	CYS	0	0.022	0.023	22.654	0.002	0.002	0.000	0.000	0.000	0.000
61	A	76	PRO	0	-0.003	0.003	24.552	0.000	0.000	0.000	0.000	0.000	0.000
62	A	77	SER	0	0.056	-0.008	24.501	0.013	0.013	0.000	0.000	0.000	0.000
63	A	78	THR	0	-0.002	0.001	24.142	0.015	0.015	0.000	0.000	0.000	0.000
64	A	79	HIS	0	0.034	0.034	18.866	0.025	0.025	0.000	0.000	0.000	0.000
65	A	80	ASN	0	-0.039	-0.027	16.229	0.024	0.024	0.000	0.000	0.000	0.000
66	A	81	MET	0	0.022	0.009	17.398	-0.049	-0.049	0.000	0.000	0.000	0.000
67	A	82	ASP	-1	-0.842	-0.898	12.182	0.364	0.364	0.000	0.000	0.000	0.000
68	A	83	VAL	0	-0.014	-0.013	12.738	-0.100	-0.100	0.000	0.000	0.000	0.000
69	A	84	PRO	0	0.017	0.013	10.444	0.151	0.151	0.000	0.000	0.000	0.000
70	A	85	HIS	0	0.050	0.016	6.172	-0.293	-0.293	0.000	0.000	0.000	0.000
71	A	86	VAL	0	-0.045	0.012	8.659	-0.220	-0.220	0.000	0.000	0.000	0.000
72	A	87	LYS	1	0.839	0.908	6.246	-0.684	-0.684	0.000	0.000	0.000	0.000
73	A	88	ARG	1	0.893	0.942	11.721	-0.082	-0.082	0.000	0.000	0.000	0.000
74	A	89	GLU	-1	-0.789	-0.855	13.945	-0.155	-0.155	0.000	0.000	0.000	0.000
75	A	90	ASP	-1	-0.859	-0.896	15.851	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	91	TYR	0	0.012	-0.013	14.872	-0.020	-0.020	0.000	0.000	0.000	0.000
77	A	92	GLN	0	-0.033	-0.029	21.218	0.009	0.009	0.000	0.000	0.000	0.000
78	A	93	LEU	0	-0.040	-0.025	24.400	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	94	THR	0	-0.013	-0.021	26.573	0.004	0.004	0.000	0.000	0.000	0.000
80	A	95	ASP	-1	-0.856	-0.931	27.970	-0.068	-0.068	0.000	0.000	0.000	0.000
81	A	96	ILE	0	-0.099	-0.048	28.091	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	97	SER	0	0.016	0.016	28.262	0.004	0.004	0.000	0.000	0.000	0.000
83	A	98	ASP	-1	-0.900	-0.961	30.706	-0.066	-0.066	0.000	0.000	0.000	0.000
84	A	99	ASP	-1	-0.931	-0.964	28.105	-0.107	-0.107	0.000	0.000	0.000	0.000
85	A	100	GLY	0	0.017	0.019	29.097	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	101	TYR	0	-0.059	-0.034	22.403	-0.006	-0.006	0.000	0.000	0.000	0.000
87	A	102	LEU	0	-0.026	-0.013	23.471	0.011	0.011	0.000	0.000	0.000	0.000
88	A	103	THR	0	-0.016	-0.020	23.500	-0.011	-0.011	0.000	0.000	0.000	0.000
89	A	104	LEU	0	-0.021	-0.019	20.661	0.013	0.013	0.000	0.000	0.000	0.000
90	A	105	MET	0	-0.007	-0.006	21.625	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	106	ALA	0	0.012	0.011	17.714	0.012	0.012	0.000	0.000	0.000	0.000
92	A	107	ASP	-1	-0.898	-0.959	19.514	-0.028	-0.028	0.000	0.000	0.000	0.000
93	A	108	ASN	0	-0.147	-0.093	17.069	0.015	0.015	0.000	0.000	0.000	0.000
94	A	109	GLY	0	-0.004	-0.001	20.379	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	110	ASP	-1	-0.892	-0.919	16.886	-0.196	-0.196	0.000	0.000	0.000	0.000
96	A	111	LEU	0	-0.011	-0.017	19.816	0.011	0.011	0.000	0.000	0.000	0.000
97	A	112	ARG	1	0.662	0.768	13.981	0.247	0.247	0.000	0.000	0.000	0.000
98	A	113	GLU	-1	-0.832	-0.899	19.633	-0.110	-0.110	0.000	0.000	0.000	0.000
99	A	114	ASP	-1	-0.804	-0.865	16.629	-0.251	-0.251	0.000	0.000	0.000	0.000
100	A	115	LEU	0	-0.042	-0.017	16.708	0.006	0.006	0.000	0.000	0.000	0.000
101	A	116	LYS	1	0.832	0.911	20.562	0.124	0.124	0.000	0.000	0.000	0.000
102	A	117	ILE	0	-0.018	0.002	24.030	0.004	0.004	0.000	0.000	0.000	0.000
103	A	118	PRO	0	-0.041	0.001	23.968	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	119	ASP	-1	-0.885	-0.955	25.742	-0.065	-0.065	0.000	0.000	0.000	0.000
105	A	120	GLY	0	-0.010	-0.011	28.075	0.006	0.006	0.000	0.000	0.000	0.000
106	A	121	ASP	-1	-0.890	-0.947	31.215	-0.019	-0.019	0.000	0.000	0.000	0.000
107	A	122	LEU	0	-0.037	0.000	24.820	0.001	0.001	0.000	0.000	0.000	0.000
108	A	123	GLY	0	0.067	0.032	29.114	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	124	THR	0	-0.041	-0.033	29.800	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	125	GLN	0	-0.076	-0.040	31.887	0.002	0.002	0.000	0.000	0.000	0.000
111	A	126	LEU	0	0.007	0.000	26.684	0.001	0.001	0.000	0.000	0.000	0.000
112	A	127	ARG	1	0.828	0.884	30.753	0.050	0.050	0.000	0.000	0.000	0.000
113	A	128	SER	0	0.005	-0.012	33.101	0.001	0.001	0.000	0.000	0.000	0.000
114	A	129	ASP	-1	-0.852	-0.914	32.905	-0.017	-0.017	0.000	0.000	0.000	0.000
115	A	130	PHE	0	0.027	0.009	31.639	0.001	0.001	0.000	0.000	0.000	0.000
116	A	131	ASP	-1	-0.788	-0.845	33.992	-0.044	-0.044	0.000	0.000	0.000	0.000
117	A	132	SER	0	-0.122	-0.059	37.035	0.004	0.004	0.000	0.000	0.000	0.000
118	A	133	GLY	0	-0.001	0.001	36.798	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	134	LYS	1	0.738	0.862	34.413	0.020	0.020	0.000	0.000	0.000	0.000
120	A	135	GLU	-1	-0.768	-0.853	30.178	-0.041	-0.041	0.000	0.000	0.000	0.000
121	A	136	LEU	0	-0.017	-0.018	28.670	0.006	0.006	0.000	0.000	0.000	0.000
122	A	137	LEU	0	0.030	0.024	23.814	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	138	CYS	0	-0.026	-0.013	23.040	0.004	0.004	0.000	0.000	0.000	0.000
124	A	139	THR	0	-0.047	-0.058	18.490	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	140	VAL	0	0.000	0.014	15.403	0.004	0.004	0.000	0.000	0.000	0.000
126	A	141	LEU	0	-0.057	-0.025	15.124	0.024	0.024	0.000	0.000	0.000	0.000
127	A	142	LYS	1	0.865	0.914	10.632	0.197	0.197	0.000	0.000	0.000	0.000
128	A	143	SER	0	-0.001	-0.039	9.769	0.095	0.095	0.000	0.000	0.000	0.000
129	A	144	CYS	0	-0.086	-0.050	9.132	-0.010	-0.010	0.000	0.000	0.000	0.000
130	A	145	GLY	0	0.024	0.030	9.817	-0.039	-0.039	0.000	0.000	0.000	0.000
131	A	146	GLU	-1	-0.815	-0.872	10.622	-0.117	-0.117	0.000	0.000	0.000	0.000
132	A	147	GLU	-1	-0.768	-0.879	12.684	-0.328	-0.328	0.000	0.000	0.000	0.000
133	A	148	CYS	0	-0.010	0.011	15.379	0.011	0.011	0.000	0.000	0.000	0.000
134	A	149	VAL	0	0.057	0.037	18.718	0.010	0.010	0.000	0.000	0.000	0.000
135	A	150	ILE	0	-0.019	-0.023	19.114	0.008	0.008	0.000	0.000	0.000	0.000
136	A	151	ALA	0	-0.056	-0.033	22.114	0.013	0.013	0.000	0.000	0.000	0.000
137	A	152	VAL	0	0.054	0.028	23.988	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	153	LYS	1	0.856	0.931	26.532	0.005	0.005	0.000	0.000	0.000	0.000
139	A	154	ALA	0	0.054	0.036	28.361	-0.004	-0.004	0.000	0.000	0.000	0.000
140	A	155	ASN	0	-0.061	-0.045	29.167	0.012	0.012	0.000	0.000	0.000	0.000
141	A	156	THR	0	-0.009	0.002	31.249	0.000	0.000	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:16:ALA)