FMO DATABASE

FMODB ID: MN93Z

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	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	-1131590.025638
FMO2-HF: Nuclear repulsion	1075166.008611
FMO2-HF: Total energy	-56424.017027
FMO2-MP2: Total energy	-56581.360453

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.
-1.861	-0.64	-0.001	-0.596	-0.623	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 : 0.009 / q_NPA : -0.009

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	0.042	0.020	3.797	-0.332	0.889	-0.001	-0.596	-0.623	0.002
4	A	19	THR	0	-0.054	-0.051	6.383	0.193	0.193	0.000	0.000	0.000	0.000
5	A	20	PHE	0	-0.051	-0.019	7.944	0.401	0.401	0.000	0.000	0.000	0.000
6	A	21	PRO	0	0.050	0.016	9.689	-0.217	-0.217	0.000	0.000	0.000	0.000
7	A	22	MET	0	-0.008	0.005	13.061	0.058	0.058	0.000	0.000	0.000	0.000
8	A	23	GLN	0	0.068	0.045	16.040	-0.063	-0.063	0.000	0.000	0.000	0.000
9	A	24	CYS	0	0.019	0.029	19.605	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	25	SER	0	-0.001	0.000	21.864	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	26	ALA	0	-0.035	-0.019	19.963	-0.015	-0.015	0.000	0.000	0.000	0.000
12	A	27	LEU	0	0.007	0.026	18.413	0.010	0.010	0.000	0.000	0.000	0.000
13	A	28	ARG	1	0.870	0.910	21.662	-0.227	-0.227	0.000	0.000	0.000	0.000
14	A	29	LYS	1	0.943	0.951	22.714	-0.084	-0.084	0.000	0.000	0.000	0.000
15	A	30	ASN	0	-0.024	-0.023	23.198	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	31	GLY	0	0.017	0.025	19.462	0.005	0.005	0.000	0.000	0.000	0.000
17	A	32	PHE	0	0.016	0.001	14.995	-0.035	-0.035	0.000	0.000	0.000	0.000
18	A	33	VAL	0	0.003	-0.009	16.336	0.043	0.043	0.000	0.000	0.000	0.000
19	A	34	MET	0	0.006	0.024	12.280	-0.038	-0.038	0.000	0.000	0.000	0.000
20	A	35	LEU	0	-0.053	-0.025	16.582	0.010	0.010	0.000	0.000	0.000	0.000
21	A	36	LYS	1	0.828	0.883	20.048	-0.054	-0.054	0.000	0.000	0.000	0.000
22	A	37	GLY	0	0.016	0.019	16.290	-0.019	-0.019	0.000	0.000	0.000	0.000
23	A	38	ARG	1	0.779	0.863	16.336	0.062	0.062	0.000	0.000	0.000	0.000
24	A	39	PRO	0	0.056	0.027	13.794	0.047	0.047	0.000	0.000	0.000	0.000
25	A	40	CYS	0	-0.042	-0.017	15.888	-0.023	-0.023	0.000	0.000	0.000	0.000
26	A	41	LYS	1	0.925	0.969	18.161	-0.060	-0.060	0.000	0.000	0.000	0.000
27	A	42	ILE	0	-0.003	-0.001	20.669	-0.021	-0.021	0.000	0.000	0.000	0.000
28	A	43	VAL	0	-0.001	-0.007	22.973	0.001	0.001	0.000	0.000	0.000	0.000
29	A	44	GLU	-1	-0.907	-0.950	26.561	0.051	0.051	0.000	0.000	0.000	0.000
30	A	45	MET	0	0.017	0.011	24.633	0.007	0.007	0.000	0.000	0.000	0.000
31	A	46	SER	0	-0.006	0.014	28.488	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	47	THR	0	0.023	0.017	30.490	0.004	0.004	0.000	0.000	0.000	0.000
33	A	48	SER	0	0.059	0.024	32.637	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	49	LYS	1	0.975	0.989	33.762	-0.039	-0.039	0.000	0.000	0.000	0.000
35	A	50	THR	0	-0.037	-0.028	33.966	0.006	0.006	0.000	0.000	0.000	0.000
36	A	51	GLY	0	0.056	0.030	35.963	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	52	LYS	1	0.917	0.968	37.838	-0.053	-0.053	0.000	0.000	0.000	0.000
38	A	53	HIS	0	0.012	-0.014	37.291	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	54	GLY	0	0.019	0.040	34.260	0.002	0.002	0.000	0.000	0.000	0.000
40	A	55	HIS	0	0.048	0.003	30.982	0.002	0.002	0.000	0.000	0.000	0.000
41	A	56	ALA	0	0.004	-0.002	28.999	0.001	0.001	0.000	0.000	0.000	0.000
42	A	57	LYS	1	0.858	0.936	29.079	-0.065	-0.065	0.000	0.000	0.000	0.000
43	A	58	VAL	0	0.011	0.004	26.432	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	59	HIS	0	-0.074	-0.041	27.361	0.007	0.007	0.000	0.000	0.000	0.000
45	A	60	LEU	0	0.003	-0.003	22.322	0.007	0.007	0.000	0.000	0.000	0.000
46	A	61	VAL	0	0.040	0.020	26.088	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	62	GLY	0	0.039	0.001	22.845	0.016	0.016	0.000	0.000	0.000	0.000
48	A	63	ILE	0	-0.042	-0.010	23.427	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	64	ASP	-1	-0.770	-0.879	20.143	-0.026	-0.026	0.000	0.000	0.000	0.000
50	A	65	ILE	0	-0.059	-0.036	14.895	0.005	0.005	0.000	0.000	0.000	0.000
51	A	66	PHE	0	0.007	0.010	14.236	0.003	0.003	0.000	0.000	0.000	0.000
52	A	67	ASN	0	-0.045	-0.031	20.219	0.005	0.005	0.000	0.000	0.000	0.000
53	A	68	GLY	0	0.105	0.051	23.123	0.003	0.003	0.000	0.000	0.000	0.000
54	A	69	LYS	1	0.889	0.950	24.488	0.037	0.037	0.000	0.000	0.000	0.000
55	A	70	LYS	1	0.879	0.953	24.761	-0.033	-0.033	0.000	0.000	0.000	0.000
56	A	71	TYR	0	0.001	-0.007	22.052	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	72	GLU	-1	-0.857	-0.935	25.186	0.049	0.049	0.000	0.000	0.000	0.000
58	A	73	ASP	-1	-0.808	-0.896	23.152	0.048	0.048	0.000	0.000	0.000	0.000
59	A	74	ILE	0	-0.056	-0.020	25.654	0.005	0.005	0.000	0.000	0.000	0.000
60	A	75	CYS	0	0.027	0.024	22.633	0.003	0.003	0.000	0.000	0.000	0.000
61	A	76	PRO	0	-0.021	-0.006	24.111	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	77	SER	0	0.051	-0.005	24.374	0.013	0.013	0.000	0.000	0.000	0.000
63	A	78	THR	0	-0.036	-0.012	24.377	0.012	0.012	0.000	0.000	0.000	0.000
64	A	79	HIS	0	0.043	0.030	18.555	0.023	0.023	0.000	0.000	0.000	0.000
65	A	80	ASN	0	-0.038	-0.034	16.361	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	81	MET	0	-0.003	-0.004	17.357	-0.047	-0.047	0.000	0.000	0.000	0.000
67	A	82	ASP	-1	-0.824	-0.887	12.231	0.414	0.414	0.000	0.000	0.000	0.000
68	A	83	VAL	0	-0.031	-0.029	12.613	-0.098	-0.098	0.000	0.000	0.000	0.000
69	A	84	PRO	0	0.023	0.021	10.318	0.161	0.161	0.000	0.000	0.000	0.000
70	A	85	HIS	0	0.024	0.012	6.551	-0.291	-0.291	0.000	0.000	0.000	0.000
71	A	86	VAL	0	-0.031	-0.002	9.082	-0.189	-0.189	0.000	0.000	0.000	0.000
72	A	87	LYS	1	0.885	0.940	6.558	-0.617	-0.617	0.000	0.000	0.000	0.000
73	A	88	ARG	1	0.954	0.974	12.011	-0.081	-0.081	0.000	0.000	0.000	0.000
74	A	89	GLU	-1	-0.805	-0.869	14.279	-0.134	-0.134	0.000	0.000	0.000	0.000
75	A	90	ASP	-1	-0.863	-0.902	16.175	-0.007	-0.007	0.000	0.000	0.000	0.000
76	A	91	TYR	0	0.006	-0.018	15.044	-0.022	-0.022	0.000	0.000	0.000	0.000
77	A	92	GLN	0	-0.017	-0.015	21.342	0.009	0.009	0.000	0.000	0.000	0.000
78	A	93	LEU	0	-0.038	-0.023	24.807	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	94	THR	0	-0.006	-0.016	26.749	0.004	0.004	0.000	0.000	0.000	0.000
80	A	95	ASP	-1	-0.871	-0.938	28.059	-0.066	-0.066	0.000	0.000	0.000	0.000
81	A	96	ILE	0	-0.081	-0.043	28.239	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	97	SER	0	0.032	0.030	28.067	0.003	0.003	0.000	0.000	0.000	0.000
83	A	98	ASP	-1	-0.866	-0.939	30.656	-0.061	-0.061	0.000	0.000	0.000	0.000
84	A	99	ASP	-1	-0.967	-0.991	28.020	-0.101	-0.101	0.000	0.000	0.000	0.000
85	A	100	GLY	0	0.004	0.004	29.098	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	101	TYR	0	-0.065	-0.041	22.318	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	102	LEU	0	-0.027	-0.018	23.595	0.010	0.010	0.000	0.000	0.000	0.000
88	A	103	THR	0	-0.012	-0.015	23.800	-0.012	-0.012	0.000	0.000	0.000	0.000
89	A	104	LEU	0	-0.053	-0.034	20.481	0.012	0.012	0.000	0.000	0.000	0.000
90	A	105	MET	0	0.010	0.007	21.579	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	106	ALA	0	0.011	0.004	17.877	0.013	0.013	0.000	0.000	0.000	0.000
92	A	107	ASP	-1	-0.866	-0.932	19.248	-0.027	-0.027	0.000	0.000	0.000	0.000
93	A	108	ASN	0	-0.167	-0.102	17.148	0.012	0.012	0.000	0.000	0.000	0.000
94	A	109	GLY	0	-0.002	-0.006	20.383	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	110	ASP	-1	-0.901	-0.924	17.218	-0.186	-0.186	0.000	0.000	0.000	0.000
96	A	111	LEU	0	-0.003	-0.011	20.080	0.007	0.007	0.000	0.000	0.000	0.000
97	A	112	ARG	1	0.665	0.770	13.965	0.234	0.234	0.000	0.000	0.000	0.000
98	A	113	GLU	-1	-0.829	-0.906	19.650	-0.105	-0.105	0.000	0.000	0.000	0.000
99	A	114	ASP	-1	-0.822	-0.866	16.668	-0.239	-0.239	0.000	0.000	0.000	0.000
100	A	115	LEU	0	-0.045	-0.017	16.860	0.003	0.003	0.000	0.000	0.000	0.000
101	A	116	LYS	1	0.834	0.925	20.783	0.119	0.119	0.000	0.000	0.000	0.000
102	A	117	ILE	0	-0.002	0.009	24.141	0.003	0.003	0.000	0.000	0.000	0.000
103	A	118	PRO	0	-0.060	-0.012	24.202	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	119	ASP	-1	-0.873	-0.934	25.820	-0.061	-0.061	0.000	0.000	0.000	0.000
105	A	120	GLY	0	-0.028	-0.026	27.927	0.005	0.005	0.000	0.000	0.000	0.000
106	A	121	ASP	-1	-0.890	-0.958	30.742	-0.015	-0.015	0.000	0.000	0.000	0.000
107	A	122	LEU	0	-0.042	-0.006	25.113	0.000	0.000	0.000	0.000	0.000	0.000
108	A	123	GLY	0	0.071	0.036	28.994	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	124	THR	0	-0.016	-0.011	29.704	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	125	GLN	0	-0.062	-0.037	31.908	0.002	0.002	0.000	0.000	0.000	0.000
111	A	126	LEU	0	-0.013	-0.004	26.954	0.000	0.000	0.000	0.000	0.000	0.000
112	A	127	ARG	1	0.830	0.883	30.947	0.046	0.046	0.000	0.000	0.000	0.000
113	A	128	SER	0	0.004	-0.004	33.242	0.001	0.001	0.000	0.000	0.000	0.000
114	A	129	ASP	-1	-0.840	-0.921	33.168	-0.015	-0.015	0.000	0.000	0.000	0.000
115	A	130	PHE	0	0.025	-0.004	31.812	0.001	0.001	0.000	0.000	0.000	0.000
116	A	131	ASP	-1	-0.792	-0.841	34.089	-0.041	-0.041	0.000	0.000	0.000	0.000
117	A	132	SER	0	-0.157	-0.079	37.301	0.003	0.003	0.000	0.000	0.000	0.000
118	A	133	GLY	0	0.021	0.006	37.592	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	134	LYS	1	0.733	0.876	34.361	0.016	0.016	0.000	0.000	0.000	0.000
120	A	135	GLU	-1	-0.776	-0.865	30.513	-0.040	-0.040	0.000	0.000	0.000	0.000
121	A	136	LEU	0	-0.027	-0.019	28.737	0.006	0.006	0.000	0.000	0.000	0.000
122	A	137	LEU	0	0.031	0.018	23.989	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	138	CYS	0	-0.028	-0.002	22.974	0.005	0.005	0.000	0.000	0.000	0.000
124	A	139	THR	0	-0.035	-0.043	19.054	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	140	VAL	0	-0.018	-0.007	15.639	0.002	0.002	0.000	0.000	0.000	0.000
126	A	141	LEU	0	-0.058	-0.035	15.224	0.022	0.022	0.000	0.000	0.000	0.000
127	A	142	LYS	1	0.840	0.915	11.022	0.180	0.180	0.000	0.000	0.000	0.000
128	A	143	SER	0	-0.028	-0.043	9.992	0.075	0.075	0.000	0.000	0.000	0.000
129	A	144	CYS	0	-0.063	-0.039	9.221	0.010	0.010	0.000	0.000	0.000	0.000
130	A	145	GLY	0	0.005	0.013	9.547	-0.022	-0.022	0.000	0.000	0.000	0.000
131	A	146	GLU	-1	-0.814	-0.872	10.450	-0.110	-0.110	0.000	0.000	0.000	0.000
132	A	147	GLU	-1	-0.768	-0.889	12.743	-0.300	-0.300	0.000	0.000	0.000	0.000
133	A	148	CYS	0	-0.002	0.016	15.374	0.010	0.010	0.000	0.000	0.000	0.000
134	A	149	VAL	0	0.053	0.042	18.774	0.013	0.013	0.000	0.000	0.000	0.000
135	A	150	ILE	0	-0.020	-0.020	19.419	0.009	0.009	0.000	0.000	0.000	0.000
136	A	151	ALA	0	-0.042	-0.030	22.259	0.012	0.012	0.000	0.000	0.000	0.000
137	A	152	VAL	0	0.046	0.030	24.175	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	153	LYS	1	0.880	0.955	26.597	0.001	0.001	0.000	0.000	0.000	0.000
139	A	154	ALA	0	0.027	0.012	28.482	-0.004	-0.004	0.000	0.000	0.000	0.000
140	A	155	ASN	0	-0.051	-0.046	29.163	0.010	0.010	0.000	0.000	0.000	0.000
141	A	156	THR	0	-0.010	0.006	31.215	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:16:ALA)