FMO DATABASE

FMODB ID: 98MG2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1131042.654571
FMO2-HF: Nuclear repulsion	1074619.575265
FMO2-HF: Total energy	-56423.079306
FMO2-MP2: Total energy	-56580.409942

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.
-1.981	-0.742	-0.002	-0.608	-0.63	0.003

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 : 0.016 / q_NPA : -0.002

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	0.057	0.029	3.797	-0.476	0.763	-0.002	-0.608	-0.630	0.003
4	A	19	THR	0	-0.051	-0.032	6.380	0.182	0.182	0.000	0.000	0.000	0.000
5	A	20	PHE	0	-0.034	-0.011	7.944	0.436	0.436	0.000	0.000	0.000	0.000
6	A	21	PRO	0	0.058	0.020	9.689	-0.223	-0.223	0.000	0.000	0.000	0.000
7	A	22	MET	0	0.014	0.007	13.061	0.059	0.059	0.000	0.000	0.000	0.000
8	A	23	GLN	0	0.033	0.032	16.040	-0.067	-0.067	0.000	0.000	0.000	0.000
9	A	24	CYS	0	0.029	0.035	19.605	-0.009	-0.009	0.000	0.000	0.000	0.000
10	A	25	SER	0	-0.002	-0.002	21.864	-0.008	-0.008	0.000	0.000	0.000	0.000
11	A	26	ALA	0	-0.041	-0.025	19.932	-0.015	-0.015	0.000	0.000	0.000	0.000
12	A	27	LEU	0	-0.001	0.019	18.434	0.010	0.010	0.000	0.000	0.000	0.000
13	A	28	ARG	1	0.882	0.925	21.683	-0.230	-0.230	0.000	0.000	0.000	0.000
14	A	29	LYS	1	1.007	0.995	22.729	-0.084	-0.084	0.000	0.000	0.000	0.000
15	A	30	ASN	0	-0.021	-0.036	23.220	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	31	GLY	0	-0.012	0.013	19.475	0.005	0.005	0.000	0.000	0.000	0.000
17	A	32	PHE	0	0.002	-0.005	14.927	-0.037	-0.037	0.000	0.000	0.000	0.000
18	A	33	VAL	0	0.005	-0.005	16.369	0.043	0.043	0.000	0.000	0.000	0.000
19	A	34	MET	0	-0.012	0.030	11.816	-0.056	-0.056	0.000	0.000	0.000	0.000
20	A	35	LEU	0	-0.021	-0.014	16.587	0.008	0.008	0.000	0.000	0.000	0.000
21	A	36	LYS	1	0.871	0.917	20.050	-0.053	-0.053	0.000	0.000	0.000	0.000
22	A	37	GLY	0	0.028	0.022	16.291	-0.019	-0.019	0.000	0.000	0.000	0.000
23	A	38	ARG	1	0.815	0.906	16.336	0.060	0.060	0.000	0.000	0.000	0.000
24	A	39	PRO	0	0.071	0.020	13.810	0.047	0.047	0.000	0.000	0.000	0.000
25	A	40	CYS	0	-0.049	-0.014	15.887	-0.025	-0.025	0.000	0.000	0.000	0.000
26	A	41	LYS	1	0.951	0.996	18.166	-0.061	-0.061	0.000	0.000	0.000	0.000
27	A	42	ILE	0	-0.018	-0.013	20.614	-0.020	-0.020	0.000	0.000	0.000	0.000
28	A	43	VAL	0	-0.031	-0.014	22.982	0.000	0.000	0.000	0.000	0.000	0.000
29	A	44	GLU	-1	-0.990	-0.998	26.569	0.056	0.056	0.000	0.000	0.000	0.000
30	A	45	MET	0	-0.003	-0.004	24.608	0.010	0.010	0.000	0.000	0.000	0.000
31	A	46	SER	0	-0.013	0.013	28.501	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	47	THR	0	0.012	0.014	30.490	0.004	0.004	0.000	0.000	0.000	0.000
33	A	48	SER	0	0.058	0.015	32.637	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	49	LYS	1	0.972	0.992	33.762	-0.044	-0.044	0.000	0.000	0.000	0.000
35	A	50	THR	0	-0.035	-0.026	33.683	0.005	0.005	0.000	0.000	0.000	0.000
36	A	51	GLY	0	0.032	0.016	36.003	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	52	LYS	1	0.927	0.971	37.921	-0.056	-0.056	0.000	0.000	0.000	0.000
38	A	53	HIS	0	0.000	-0.017	37.370	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	54	GLY	0	0.019	0.038	34.334	0.002	0.002	0.000	0.000	0.000	0.000
40	A	55	HIS	0	0.048	0.004	31.060	0.003	0.003	0.000	0.000	0.000	0.000
41	A	56	ALA	0	-0.011	-0.009	29.015	0.001	0.001	0.000	0.000	0.000	0.000
42	A	57	LYS	1	0.913	0.970	29.086	-0.064	-0.064	0.000	0.000	0.000	0.000
43	A	58	VAL	0	0.009	0.001	26.435	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	59	HIS	0	-0.040	-0.002	27.361	0.006	0.006	0.000	0.000	0.000	0.000
45	A	60	LEU	0	0.021	0.001	22.218	0.006	0.006	0.000	0.000	0.000	0.000
46	A	61	VAL	0	0.056	0.027	26.098	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	62	GLY	0	0.039	-0.006	22.853	0.015	0.015	0.000	0.000	0.000	0.000
48	A	63	ILE	0	-0.047	-0.012	23.436	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	64	ASP	-1	-0.775	-0.877	20.223	-0.020	-0.020	0.000	0.000	0.000	0.000
50	A	65	ILE	0	-0.064	-0.040	15.015	0.004	0.004	0.000	0.000	0.000	0.000
51	A	66	PHE	0	0.013	0.015	14.365	0.001	0.001	0.000	0.000	0.000	0.000
52	A	67	ASN	0	-0.060	-0.039	20.209	0.007	0.007	0.000	0.000	0.000	0.000
53	A	68	GLY	0	0.118	0.050	23.112	0.002	0.002	0.000	0.000	0.000	0.000
54	A	69	LYS	1	0.889	0.949	24.498	0.036	0.036	0.000	0.000	0.000	0.000
55	A	70	LYS	1	0.949	0.983	24.757	-0.027	-0.027	0.000	0.000	0.000	0.000
56	A	71	TYR	0	0.009	0.004	22.852	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	72	GLU	-1	-0.916	-0.986	25.140	0.052	0.052	0.000	0.000	0.000	0.000
58	A	73	ASP	-1	-0.855	-0.893	23.164	0.074	0.074	0.000	0.000	0.000	0.000
59	A	74	ILE	0	-0.066	-0.049	25.654	0.004	0.004	0.000	0.000	0.000	0.000
60	A	75	CYS	0	0.047	0.026	22.744	0.005	0.005	0.000	0.000	0.000	0.000
61	A	76	PRO	0	-0.045	-0.010	24.045	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	77	SER	0	0.063	-0.009	24.374	0.013	0.013	0.000	0.000	0.000	0.000
63	A	78	THR	0	-0.035	-0.013	24.377	0.012	0.012	0.000	0.000	0.000	0.000
64	A	79	HIS	0	0.051	0.035	18.531	0.020	0.020	0.000	0.000	0.000	0.000
65	A	80	ASN	0	-0.041	-0.038	16.135	-0.014	-0.014	0.000	0.000	0.000	0.000
66	A	81	MET	0	-0.001	0.004	17.330	-0.046	-0.046	0.000	0.000	0.000	0.000
67	A	82	ASP	-1	-0.863	-0.925	12.872	0.386	0.386	0.000	0.000	0.000	0.000
68	A	83	VAL	0	-0.022	-0.026	12.632	-0.104	-0.104	0.000	0.000	0.000	0.000
69	A	84	PRO	0	0.010	0.008	10.342	0.165	0.165	0.000	0.000	0.000	0.000
70	A	85	HIS	0	-0.015	-0.005	6.302	-0.316	-0.316	0.000	0.000	0.000	0.000
71	A	86	VAL	0	-0.028	-0.011	9.091	-0.187	-0.187	0.000	0.000	0.000	0.000
72	A	87	LYS	1	0.924	0.955	6.847	-0.487	-0.487	0.000	0.000	0.000	0.000
73	A	88	ARG	1	0.946	0.969	12.010	-0.071	-0.071	0.000	0.000	0.000	0.000
74	A	89	GLU	-1	-0.865	-0.908	14.318	-0.131	-0.131	0.000	0.000	0.000	0.000
75	A	90	ASP	-1	-0.834	-0.853	16.165	-0.015	-0.015	0.000	0.000	0.000	0.000
76	A	91	TYR	0	0.029	0.013	15.146	-0.018	-0.018	0.000	0.000	0.000	0.000
77	A	92	GLN	0	0.028	0.017	21.326	0.011	0.011	0.000	0.000	0.000	0.000
78	A	93	LEU	0	-0.045	-0.030	24.788	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	94	THR	0	-0.080	-0.044	26.533	0.005	0.005	0.000	0.000	0.000	0.000
80	A	95	ASP	-1	-0.860	-0.932	28.025	-0.068	-0.068	0.000	0.000	0.000	0.000
81	A	96	ILE	0	-0.058	-0.034	28.204	-0.004	-0.004	0.000	0.000	0.000	0.000
82	A	97	SER	0	0.061	0.044	28.368	0.005	0.005	0.000	0.000	0.000	0.000
83	A	98	ASP	-1	-0.853	-0.931	30.614	-0.063	-0.063	0.000	0.000	0.000	0.000
84	A	99	ASP	-1	-0.986	-0.992	28.358	-0.098	-0.098	0.000	0.000	0.000	0.000
85	A	100	GLY	0	-0.079	-0.047	29.042	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	101	TYR	0	-0.079	-0.052	22.606	0.001	0.001	0.000	0.000	0.000	0.000
87	A	102	LEU	0	-0.018	-0.019	23.454	0.009	0.009	0.000	0.000	0.000	0.000
88	A	103	THR	0	0.026	0.032	23.762	-0.012	-0.012	0.000	0.000	0.000	0.000
89	A	104	LEU	0	-0.058	-0.041	20.393	0.013	0.013	0.000	0.000	0.000	0.000
90	A	105	MET	0	0.016	0.007	21.562	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	106	ALA	0	0.005	0.000	17.899	0.011	0.011	0.000	0.000	0.000	0.000
92	A	107	ASP	-1	-0.860	-0.926	19.269	-0.040	-0.040	0.000	0.000	0.000	0.000
93	A	108	ASN	0	-0.118	-0.062	16.542	0.011	0.011	0.000	0.000	0.000	0.000
94	A	109	GLY	0	0.001	-0.008	20.404	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	110	ASP	-1	-0.945	-0.959	17.250	-0.197	-0.197	0.000	0.000	0.000	0.000
96	A	111	LEU	0	0.000	-0.011	20.086	0.007	0.007	0.000	0.000	0.000	0.000
97	A	112	ARG	1	0.676	0.809	14.128	0.240	0.240	0.000	0.000	0.000	0.000
98	A	113	GLU	-1	-0.846	-0.941	19.627	-0.111	-0.111	0.000	0.000	0.000	0.000
99	A	114	ASP	-1	-0.854	-0.909	16.561	-0.250	-0.250	0.000	0.000	0.000	0.000
100	A	115	LEU	0	-0.046	-0.018	16.983	0.003	0.003	0.000	0.000	0.000	0.000
101	A	116	LYS	1	0.921	0.971	20.731	0.120	0.120	0.000	0.000	0.000	0.000
102	A	117	ILE	0	-0.004	0.007	24.084	0.003	0.003	0.000	0.000	0.000	0.000
103	A	118	PRO	0	-0.070	-0.008	24.325	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	119	ASP	-1	-0.855	-0.931	25.856	-0.062	-0.062	0.000	0.000	0.000	0.000
105	A	120	GLY	0	-0.039	-0.031	27.910	0.005	0.005	0.000	0.000	0.000	0.000
106	A	121	ASP	-1	-0.869	-0.944	30.727	-0.016	-0.016	0.000	0.000	0.000	0.000
107	A	122	LEU	0	-0.058	-0.012	25.158	0.000	0.000	0.000	0.000	0.000	0.000
108	A	123	GLY	0	0.058	0.031	28.997	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	124	THR	0	-0.015	-0.022	29.686	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	125	GLN	0	-0.066	-0.038	31.826	0.002	0.002	0.000	0.000	0.000	0.000
111	A	126	LEU	0	-0.027	-0.006	26.874	0.000	0.000	0.000	0.000	0.000	0.000
112	A	127	ARG	1	0.952	0.975	30.930	0.049	0.049	0.000	0.000	0.000	0.000
113	A	128	SER	0	0.004	0.008	33.197	0.001	0.001	0.000	0.000	0.000	0.000
114	A	129	ASP	-1	-0.893	-0.962	33.062	-0.019	-0.019	0.000	0.000	0.000	0.000
115	A	130	PHE	0	0.037	-0.008	31.936	0.001	0.001	0.000	0.000	0.000	0.000
116	A	131	ASP	-1	-0.871	-0.911	34.071	-0.042	-0.042	0.000	0.000	0.000	0.000
117	A	132	SER	0	-0.183	-0.097	37.261	0.003	0.003	0.000	0.000	0.000	0.000
118	A	133	GLY	0	0.017	0.003	37.574	-0.002	-0.002	0.000	0.000	0.000	0.000
119	A	134	LYS	1	0.787	0.918	34.328	0.020	0.020	0.000	0.000	0.000	0.000
120	A	135	GLU	-1	-0.842	-0.906	31.460	-0.043	-0.043	0.000	0.000	0.000	0.000
121	A	136	LEU	0	-0.033	-0.028	28.701	0.006	0.006	0.000	0.000	0.000	0.000
122	A	137	LEU	0	0.017	0.008	23.698	-0.005	-0.005	0.000	0.000	0.000	0.000
123	A	138	CYS	0	-0.035	-0.008	22.926	0.008	0.008	0.000	0.000	0.000	0.000
124	A	139	THR	0	-0.046	-0.068	19.122	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	140	VAL	0	-0.013	-0.007	15.649	0.002	0.002	0.000	0.000	0.000	0.000
126	A	141	LEU	0	-0.064	-0.047	15.386	0.022	0.022	0.000	0.000	0.000	0.000
127	A	142	LYS	1	0.873	0.937	11.069	0.186	0.186	0.000	0.000	0.000	0.000
128	A	143	SER	0	-0.028	-0.039	9.967	0.074	0.074	0.000	0.000	0.000	0.000
129	A	144	CYS	0	-0.032	-0.021	9.220	0.009	0.009	0.000	0.000	0.000	0.000
130	A	145	GLY	0	-0.006	0.009	9.481	-0.023	-0.023	0.000	0.000	0.000	0.000
131	A	146	GLU	-1	-0.839	-0.900	10.368	-0.122	-0.122	0.000	0.000	0.000	0.000
132	A	147	GLU	-1	-0.791	-0.915	12.748	-0.328	-0.328	0.000	0.000	0.000	0.000
133	A	148	CYS	0	0.001	0.010	15.325	0.010	0.010	0.000	0.000	0.000	0.000
134	A	149	VAL	0	0.035	0.038	18.758	0.012	0.012	0.000	0.000	0.000	0.000
135	A	150	ILE	0	-0.033	-0.025	19.350	0.009	0.009	0.000	0.000	0.000	0.000
136	A	151	ALA	0	-0.028	-0.026	22.247	0.012	0.012	0.000	0.000	0.000	0.000
137	A	152	VAL	0	0.054	0.031	24.163	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	153	LYS	1	0.889	0.960	26.625	0.004	0.004	0.000	0.000	0.000	0.000
139	A	154	ALA	0	0.027	0.013	28.473	-0.004	-0.004	0.000	0.000	0.000	0.000
140	A	155	ASN	0	-0.015	-0.019	28.344	0.009	0.009	0.000	0.000	0.000	0.000
141	A	156	THR	0	0.002	0.009	31.205	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)