FMO DATABASE

FMODB ID: Q17RY

Calculation Name: 3HFI-A-Xray320

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3HFI

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	139
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1313574.729298
FMO2-HF: Nuclear repulsion	1258460.26865
FMO2-HF: Total energy	-55114.460648
FMO2-MP2: Total energy	-55278.473976

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:24:ACE )

Summations of interaction energy for fragment #1(A:24:ACE )

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.
-1.838	0.214	1.588	-2.151	-1.488	-0.014

Interaction energy analysis for fragmet #1(A:24:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.010 / q_NPA : -0.013

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	26	THR	0	-0.088	-0.041	3.859	1.379	2.255	-0.005	-0.441	-0.429	-0.001
4	A	27	GLU	-1	-0.831	-0.898	7.145	-0.807	-0.807	0.000	0.000	0.000	0.000
5	A	28	VAL	0	-0.066	-0.049	10.401	0.134	0.134	0.000	0.000	0.000	0.000
6	A	29	ILE	0	-0.010	0.009	13.915	-0.004	-0.004	0.000	0.000	0.000	0.000
7	A	30	THR	0	0.001	-0.017	16.081	0.025	0.025	0.000	0.000	0.000	0.000
8	A	31	SER	0	-0.042	-0.019	18.612	-0.004	-0.004	0.000	0.000	0.000	0.000
9	A	32	ARG	1	0.917	0.960	21.042	0.097	0.097	0.000	0.000	0.000	0.000
10	A	33	ILE	0	0.029	0.036	24.438	-0.002	-0.002	0.000	0.000	0.000	0.000
11	A	34	GLU	-1	-0.848	-0.926	26.202	-0.063	-0.063	0.000	0.000	0.000	0.000
12	A	35	PRO	0	0.078	0.038	28.923	0.002	0.002	0.000	0.000	0.000	0.000
13	A	36	ALA	0	0.002	0.013	29.420	0.001	0.001	0.000	0.000	0.000	0.000
14	A	37	ASN	0	0.029	0.022	29.061	0.006	0.006	0.000	0.000	0.000	0.000
15	A	38	ARG	1	1.016	0.976	31.760	0.018	0.018	0.000	0.000	0.000	0.000
16	A	39	TYR	0	-0.072	-0.040	26.813	0.002	0.002	0.000	0.000	0.000	0.000
17	A	40	VAL	0	0.062	0.010	26.248	0.002	0.002	0.000	0.000	0.000	0.000
18	A	41	ALA	0	-0.019	0.002	28.680	0.000	0.000	0.000	0.000	0.000	0.000
19	A	42	GLU	-1	-0.941	-0.970	31.358	0.001	0.001	0.000	0.000	0.000	0.000
20	A	43	LYS	1	0.865	0.940	26.902	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	44	LEU	0	-0.002	-0.014	24.621	0.003	0.003	0.000	0.000	0.000	0.000
22	A	45	ARG	1	0.876	0.958	28.532	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	46	ILE	0	0.011	0.021	29.367	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	47	THR	0	-0.014	-0.012	33.099	0.002	0.002	0.000	0.000	0.000	0.000
25	A	48	PRO	0	-0.014	-0.031	34.310	-0.003	-0.003	0.000	0.000	0.000	0.000
26	A	49	GLY	0	-0.023	-0.011	33.903	0.001	0.001	0.000	0.000	0.000	0.000
27	A	50	GLN	0	-0.013	-0.003	31.890	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	51	ASP	-1	-0.863	-0.921	30.209	-0.059	-0.059	0.000	0.000	0.000	0.000
29	A	52	ILE	0	-0.069	-0.032	24.764	0.001	0.001	0.000	0.000	0.000	0.000
30	A	53	LEU	0	0.020	0.010	20.894	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	54	TYR	0	-0.090	-0.115	20.603	0.001	0.001	0.000	0.000	0.000	0.000
32	A	55	LEU	0	-0.009	-0.025	16.064	-0.015	-0.015	0.000	0.000	0.000	0.000
33	A	56	GLU	-1	-0.907	-0.943	16.390	-0.114	-0.114	0.000	0.000	0.000	0.000
34	A	57	ARG	1	0.896	0.930	10.552	0.268	0.268	0.000	0.000	0.000	0.000
35	A	58	LEU	0	0.016	0.026	9.851	0.104	0.104	0.000	0.000	0.000	0.000
36	A	59	ARG	1	0.895	0.938	5.189	-0.074	-0.074	0.000	0.000	0.000	0.000
37	A	60	SER	0	0.035	0.004	5.237	0.091	0.136	0.000	-0.014	-0.031	0.000
38	A	61	ILE	0	-0.064	-0.049	2.625	-0.990	-0.024	0.973	-1.268	-0.671	-0.010
39	A	62	GLY	0	0.000	-0.010	2.226	-0.576	-0.387	0.619	-0.392	-0.416	-0.003
40	A	63	ASP	-1	-0.912	-0.942	4.005	-0.695	-0.719	0.001	-0.036	0.059	0.000
41	A	64	GLU	-1	-0.930	-0.947	5.862	0.379	0.379	0.000	0.000	0.000	0.000
42	A	65	LYS	1	0.941	0.965	6.455	0.301	0.301	0.000	0.000	0.000	0.000
43	A	66	ALA	0	-0.002	0.005	6.998	0.077	0.077	0.000	0.000	0.000	0.000
44	A	67	MET	0	-0.060	-0.049	7.940	-0.043	-0.043	0.000	0.000	0.000	0.000
45	A	68	LEU	0	0.039	0.041	10.674	-0.080	-0.080	0.000	0.000	0.000	0.000
46	A	69	ILE	0	-0.059	-0.036	10.102	0.050	0.050	0.000	0.000	0.000	0.000
47	A	70	GLU	-1	-0.738	-0.796	14.232	-0.095	-0.095	0.000	0.000	0.000	0.000
48	A	71	ASN	0	-0.025	-0.020	15.127	-0.014	-0.014	0.000	0.000	0.000	0.000
49	A	72	ARG	1	0.894	0.955	18.398	0.045	0.045	0.000	0.000	0.000	0.000
50	A	73	ILE	0	0.020	0.009	18.636	0.011	0.011	0.000	0.000	0.000	0.000
51	A	74	ASN	0	0.043	0.013	22.906	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	75	ILE	0	0.036	0.000	24.707	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	76	GLU	-1	-0.899	-0.933	26.725	-0.055	-0.055	0.000	0.000	0.000	0.000
54	A	77	LEU	0	-0.088	-0.039	26.776	0.003	0.003	0.000	0.000	0.000	0.000
55	A	78	CYS	0	-0.091	-0.051	23.911	0.000	0.000	0.000	0.000	0.000	0.000
56	A	79	PRO	0	0.042	0.014	25.842	-0.008	-0.008	0.000	0.000	0.000	0.000
57	A	80	GLY	0	0.080	0.040	26.136	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	81	ILE	0	-0.033	-0.016	19.607	-0.013	-0.013	0.000	0.000	0.000	0.000
59	A	82	VAL	0	-0.003	-0.012	21.853	-0.016	-0.016	0.000	0.000	0.000	0.000
60	A	83	GLU	-1	-0.971	-0.977	23.688	-0.116	-0.116	0.000	0.000	0.000	0.000
61	A	84	ILE	0	-0.087	-0.024	17.668	-0.011	-0.011	0.000	0.000	0.000	0.000
62	A	85	ASP	-1	-0.792	-0.894	16.491	-0.378	-0.378	0.000	0.000	0.000	0.000
63	A	86	PHE	0	-0.049	-0.056	13.933	-0.022	-0.022	0.000	0.000	0.000	0.000
64	A	87	ASN	0	0.026	0.022	12.008	-0.174	-0.174	0.000	0.000	0.000	0.000
65	A	88	GLN	0	-0.027	-0.004	11.936	-0.155	-0.155	0.000	0.000	0.000	0.000
66	A	89	HIS	0	-0.028	0.006	13.932	0.030	0.030	0.000	0.000	0.000	0.000
67	A	90	ASN	0	0.035	0.011	9.876	-0.144	-0.144	0.000	0.000	0.000	0.000
68	A	91	LEU	0	-0.001	0.021	12.458	0.058	0.058	0.000	0.000	0.000	0.000
69	A	92	PHE	0	0.032	-0.002	13.427	0.021	0.021	0.000	0.000	0.000	0.000
70	A	93	PRO	0	0.030	0.009	13.409	0.014	0.014	0.000	0.000	0.000	0.000
71	A	94	THR	0	0.036	0.006	16.045	0.012	0.012	0.000	0.000	0.000	0.000
72	A	95	ILE	0	0.031	0.017	18.267	0.016	0.016	0.000	0.000	0.000	0.000
73	A	96	GLU	-1	-0.867	-0.896	19.497	-0.017	-0.017	0.000	0.000	0.000	0.000
74	A	97	SER	0	-0.046	-0.033	20.067	0.007	0.007	0.000	0.000	0.000	0.000
75	A	98	LEU	0	-0.035	-0.010	22.220	0.008	0.008	0.000	0.000	0.000	0.000
76	A	99	SER	0	-0.053	-0.050	23.580	0.011	0.011	0.000	0.000	0.000	0.000
77	A	100	LYS	1	0.902	0.953	25.253	0.064	0.064	0.000	0.000	0.000	0.000
78	A	101	ARG	1	0.887	0.968	25.201	0.038	0.038	0.000	0.000	0.000	0.000
79	A	102	LYS	1	0.946	0.973	22.931	0.008	0.008	0.000	0.000	0.000	0.000
80	A	103	ILE	0	0.009	-0.007	18.601	0.001	0.001	0.000	0.000	0.000	0.000
81	A	104	ARG	1	0.874	0.947	21.989	0.003	0.003	0.000	0.000	0.000	0.000
82	A	105	TYR	0	-0.028	-0.010	23.572	0.006	0.006	0.000	0.000	0.000	0.000
83	A	106	SER	0	0.055	0.032	18.838	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	107	GLU	-1	-0.973	-0.967	21.904	0.035	0.035	0.000	0.000	0.000	0.000
85	A	108	SER	0	-0.035	-0.032	19.649	0.001	0.001	0.000	0.000	0.000	0.000
86	A	109	ARG	1	0.930	0.981	21.853	-0.028	-0.028	0.000	0.000	0.000	0.000
87	A	110	TYR	0	0.010	-0.004	18.050	0.005	0.005	0.000	0.000	0.000	0.000
88	A	111	ALA	0	-0.007	-0.007	22.435	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	112	ALA	0	0.019	0.023	22.710	0.006	0.006	0.000	0.000	0.000	0.000
90	A	113	ARG	1	0.913	0.955	22.903	-0.028	-0.028	0.000	0.000	0.000	0.000
91	A	114	LEU	0	0.027	0.031	23.625	0.010	0.010	0.000	0.000	0.000	0.000
92	A	115	ILE	0	-0.047	0.001	18.120	-0.008	-0.008	0.000	0.000	0.000	0.000
93	A	116	GLY	0	0.045	0.023	21.990	-0.009	-0.009	0.000	0.000	0.000	0.000
94	A	117	ASN	0	0.032	-0.002	22.596	0.001	0.001	0.000	0.000	0.000	0.000
95	A	118	GLU	-1	-0.918	-0.952	21.310	-0.080	-0.080	0.000	0.000	0.000	0.000
96	A	119	ARG	1	0.886	0.936	18.882	0.021	0.021	0.000	0.000	0.000	0.000
97	A	120	GLY	0	0.006	0.002	17.856	0.000	0.000	0.000	0.000	0.000	0.000
98	A	121	HIS	0	0.009	-0.004	18.221	0.003	0.003	0.000	0.000	0.000	0.000
99	A	122	PHE	0	-0.011	0.002	14.946	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	123	LEU	0	-0.039	-0.029	12.464	-0.013	-0.013	0.000	0.000	0.000	0.000
101	A	124	ASP	-1	-0.950	-0.965	14.570	0.005	0.005	0.000	0.000	0.000	0.000
102	A	125	ILE	0	-0.096	-0.055	16.152	0.011	0.011	0.000	0.000	0.000	0.000
103	A	126	SER	0	0.014	0.027	18.719	-0.009	-0.009	0.000	0.000	0.000	0.000
104	A	127	GLU	-1	-0.802	-0.921	22.429	0.001	0.001	0.000	0.000	0.000	0.000
105	A	128	ASP	-1	-0.920	-0.980	23.953	0.021	0.021	0.000	0.000	0.000	0.000
106	A	129	ALA	0	-0.084	-0.023	21.589	0.007	0.007	0.000	0.000	0.000	0.000
107	A	130	PRO	0	-0.027	-0.035	23.085	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	131	VAL	0	-0.030	-0.010	18.229	0.013	0.013	0.000	0.000	0.000	0.000
109	A	132	LEU	0	-0.059	-0.025	17.253	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	133	HIS	0	-0.016	-0.008	18.135	0.005	0.005	0.000	0.000	0.000	0.000
111	A	134	LEU	0	-0.005	-0.005	16.131	0.009	0.009	0.000	0.000	0.000	0.000
112	A	135	GLU	-1	-0.830	-0.891	19.458	0.001	0.001	0.000	0.000	0.000	0.000
113	A	136	GLN	0	-0.014	-0.029	16.311	0.000	0.000	0.000	0.000	0.000	0.000
114	A	137	LEU	0	-0.066	-0.008	20.476	-0.014	-0.014	0.000	0.000	0.000	0.000
115	A	138	VAL	0	0.042	0.021	18.261	0.012	0.012	0.000	0.000	0.000	0.000
116	A	139	PHE	0	0.014	0.000	21.709	-0.010	-0.010	0.000	0.000	0.000	0.000
117	A	140	PHE	0	0.048	0.006	22.793	0.004	0.004	0.000	0.000	0.000	0.000
118	A	141	SER	0	-0.056	-0.042	25.798	0.005	0.005	0.000	0.000	0.000	0.000
119	A	142	ARG	1	0.982	0.989	28.731	-0.023	-0.023	0.000	0.000	0.000	0.000
120	A	143	GLU	-1	-0.920	-0.977	30.411	0.004	0.004	0.000	0.000	0.000	0.000
121	A	144	LEU	0	-0.032	0.003	28.781	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	145	PRO	0	0.000	0.006	26.193	0.000	0.000	0.000	0.000	0.000	0.000
123	A	146	VAL	0	-0.020	-0.011	21.919	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	147	GLU	-1	-0.819	-0.931	18.635	-0.056	-0.056	0.000	0.000	0.000	0.000
125	A	148	PHE	0	-0.007	-0.005	21.933	0.014	0.014	0.000	0.000	0.000	0.000
126	A	149	GLY	0	0.068	0.042	18.198	-0.014	-0.014	0.000	0.000	0.000	0.000
127	A	150	ASN	0	-0.071	-0.037	18.683	0.025	0.025	0.000	0.000	0.000	0.000
128	A	151	VAL	0	-0.011	-0.011	13.482	-0.015	-0.015	0.000	0.000	0.000	0.000
129	A	152	TRP	0	-0.012	-0.015	15.352	0.026	0.026	0.000	0.000	0.000	0.000
130	A	153	LEU	0	-0.005	0.015	13.445	0.003	0.003	0.000	0.000	0.000	0.000
131	A	154	LYS	1	0.934	0.966	11.938	-0.148	-0.148	0.000	0.000	0.000	0.000
132	A	155	GLY	0	0.060	0.023	14.027	0.003	0.003	0.000	0.000	0.000	0.000
133	A	156	ASN	0	-0.079	-0.060	14.463	-0.034	-0.034	0.000	0.000	0.000	0.000
134	A	157	LYS	1	0.958	0.977	14.919	-0.152	-0.152	0.000	0.000	0.000	0.000
135	A	158	TYR	0	0.071	0.022	11.271	0.041	0.041	0.000	0.000	0.000	0.000
136	A	159	TYR	0	0.021	0.026	12.473	0.023	0.023	0.000	0.000	0.000	0.000
137	A	160	LEU	0	-0.066	-0.023	15.700	-0.024	-0.024	0.000	0.000	0.000	0.000
138	A	161	GLY	0	0.051	0.023	17.299	0.024	0.024	0.000	0.000	0.000	0.000
139	A	162	NME	0	-0.005	0.007	17.529	0.008	0.008	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:24:ACE )