FMO DATABASE

FMODB ID: R5R18

Calculation Name: 3HFI-A-Xray372

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: 2023-06-20

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	137
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1306461.308163
FMO2-HF: Nuclear repulsion	1251517.745279
FMO2-HF: Total energy	-54943.562884
FMO2-MP2: Total energy	-55107.042874

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:25:THR)

Summations of interaction energy for fragment #1(A:25: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.
-17.701	-13.959	10.301	-6.81	-7.232	-0.042

Interaction energy analysis for fragmet #1(A:25:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.058 / q_NPA : 0.030

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	27	GLU	-1	-0.839	-0.903	3.283	-8.036	-4.252	0.134	-1.677	-2.240	0.004
4	A	28	VAL	0	-0.069	-0.049	4.306	0.082	0.128	0.000	-0.012	-0.033	0.000
5	A	29	ILE	0	-0.002	0.010	8.134	-0.013	-0.013	0.000	0.000	0.000	0.000
6	A	30	THR	0	0.001	-0.017	10.078	0.240	0.240	0.000	0.000	0.000	0.000
7	A	31	SER	0	-0.045	-0.020	13.289	-0.009	-0.009	0.000	0.000	0.000	0.000
8	A	32	ARG	1	0.916	0.961	15.688	0.516	0.516	0.000	0.000	0.000	0.000
9	A	33	ILE	0	0.030	0.036	19.429	-0.005	-0.005	0.000	0.000	0.000	0.000
10	A	34	GLU	-1	-0.850	-0.927	22.204	-0.400	-0.400	0.000	0.000	0.000	0.000
11	A	35	PRO	0	0.079	0.038	24.519	0.009	0.009	0.000	0.000	0.000	0.000
12	A	36	ALA	0	0.004	0.013	26.228	-0.021	-0.021	0.000	0.000	0.000	0.000
13	A	37	ASN	0	0.029	0.023	26.216	0.029	0.029	0.000	0.000	0.000	0.000
14	A	38	ARG	1	1.012	0.975	28.876	0.189	0.189	0.000	0.000	0.000	0.000
15	A	39	TYR	0	-0.072	-0.041	25.526	0.022	0.022	0.000	0.000	0.000	0.000
16	A	40	VAL	0	0.064	0.011	24.041	0.004	0.004	0.000	0.000	0.000	0.000
17	A	41	ALA	0	-0.021	0.001	26.638	0.009	0.009	0.000	0.000	0.000	0.000
18	A	42	GLU	-1	-0.937	-0.969	29.301	-0.156	-0.156	0.000	0.000	0.000	0.000
19	A	43	LYS	1	0.868	0.941	25.694	0.234	0.234	0.000	0.000	0.000	0.000
20	A	44	LEU	0	-0.007	-0.015	23.171	0.014	0.014	0.000	0.000	0.000	0.000
21	A	45	ARG	1	0.879	0.958	27.170	0.118	0.118	0.000	0.000	0.000	0.000
22	A	46	ILE	0	0.008	0.021	27.118	0.012	0.012	0.000	0.000	0.000	0.000
23	A	47	THR	0	-0.016	-0.012	31.241	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	48	PRO	0	-0.009	-0.029	31.572	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	49	GLY	0	-0.025	-0.012	30.759	0.012	0.012	0.000	0.000	0.000	0.000
26	A	50	GLN	0	-0.015	-0.003	28.865	0.000	0.000	0.000	0.000	0.000	0.000
27	A	51	ASP	-1	-0.863	-0.922	26.205	-0.194	-0.194	0.000	0.000	0.000	0.000
28	A	52	ILE	0	-0.072	-0.033	21.511	0.011	0.011	0.000	0.000	0.000	0.000
29	A	53	LEU	0	0.024	0.011	16.987	-0.008	-0.008	0.000	0.000	0.000	0.000
30	A	54	TYR	0	-0.091	-0.116	15.966	-0.016	-0.016	0.000	0.000	0.000	0.000
31	A	55	LEU	0	-0.010	-0.025	12.417	0.008	0.008	0.000	0.000	0.000	0.000
32	A	56	GLU	-1	-0.905	-0.942	11.745	-1.051	-1.051	0.000	0.000	0.000	0.000
33	A	57	ARG	1	0.894	0.929	7.710	0.935	0.935	0.000	0.000	0.000	0.000
34	A	58	LEU	0	0.019	0.027	6.091	0.352	0.352	0.000	0.000	0.000	0.000
35	A	59	ARG	1	0.894	0.938	3.994	0.931	1.284	0.000	-0.100	-0.252	0.000
36	A	60	SER	0	0.025	-0.003	2.597	-2.533	-0.099	0.875	-1.359	-1.951	-0.011
37	A	61	ILE	0	-0.055	-0.036	1.859	-5.970	-9.126	9.294	-3.629	-2.509	-0.035
38	A	62	GLY	0	0.001	-0.006	3.897	0.076	0.217	-0.001	-0.025	-0.116	0.000
39	A	63	ASP	-1	-0.924	-0.951	4.549	-3.583	-3.443	-0.001	-0.008	-0.131	0.000
40	A	64	GLU	-1	-0.928	-0.945	5.476	-0.906	-0.906	0.000	0.000	0.000	0.000
41	A	65	LYS	1	0.940	0.964	6.185	1.739	1.739	0.000	0.000	0.000	0.000
42	A	66	ALA	0	0.002	0.007	6.614	0.708	0.708	0.000	0.000	0.000	0.000
43	A	67	MET	0	-0.063	-0.051	7.730	0.733	0.733	0.000	0.000	0.000	0.000
44	A	68	LEU	0	0.043	0.043	8.940	-0.541	-0.541	0.000	0.000	0.000	0.000
45	A	69	ILE	0	-0.063	-0.038	8.864	0.310	0.310	0.000	0.000	0.000	0.000
46	A	70	GLU	-1	-0.737	-0.796	11.983	-0.796	-0.796	0.000	0.000	0.000	0.000
47	A	71	ASN	0	-0.025	-0.020	12.896	-0.022	-0.022	0.000	0.000	0.000	0.000
48	A	72	ARG	1	0.894	0.955	15.993	0.463	0.463	0.000	0.000	0.000	0.000
49	A	73	ILE	0	0.024	0.010	16.088	0.029	0.029	0.000	0.000	0.000	0.000
50	A	74	ASN	0	0.038	0.012	20.596	0.000	0.000	0.000	0.000	0.000	0.000
51	A	75	ILE	0	0.040	0.001	21.651	0.019	0.019	0.000	0.000	0.000	0.000
52	A	76	GLU	-1	-0.901	-0.935	24.015	-0.071	-0.071	0.000	0.000	0.000	0.000
53	A	77	LEU	0	-0.084	-0.038	24.924	0.022	0.022	0.000	0.000	0.000	0.000
54	A	78	CYS	0	-0.098	-0.053	21.578	0.016	0.016	0.000	0.000	0.000	0.000
55	A	79	PRO	0	0.042	0.014	23.136	-0.015	-0.015	0.000	0.000	0.000	0.000
56	A	80	GLY	0	0.081	0.041	22.802	0.024	0.024	0.000	0.000	0.000	0.000
57	A	81	ILE	0	-0.031	-0.015	17.021	0.005	0.005	0.000	0.000	0.000	0.000
58	A	82	VAL	0	-0.003	-0.013	18.111	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	83	GLU	-1	-0.972	-0.977	19.074	-0.032	-0.032	0.000	0.000	0.000	0.000
60	A	84	ILE	0	-0.086	-0.024	13.727	0.041	0.041	0.000	0.000	0.000	0.000
61	A	85	ASP	-1	-0.791	-0.893	10.916	-0.215	-0.215	0.000	0.000	0.000	0.000
62	A	86	PHE	0	-0.045	-0.055	10.311	0.141	0.141	0.000	0.000	0.000	0.000
63	A	87	ASN	0	0.020	0.019	6.535	-0.518	-0.518	0.000	0.000	0.000	0.000
64	A	88	GLN	0	-0.027	-0.005	6.806	0.559	0.559	0.000	0.000	0.000	0.000
65	A	89	HIS	0	-0.025	0.008	9.472	0.232	0.232	0.000	0.000	0.000	0.000
66	A	90	ASN	0	0.032	0.011	7.813	-0.041	-0.041	0.000	0.000	0.000	0.000
67	A	91	LEU	0	-0.004	0.020	10.125	-0.035	-0.035	0.000	0.000	0.000	0.000
68	A	92	PHE	0	0.035	-0.001	12.263	0.043	0.043	0.000	0.000	0.000	0.000
69	A	93	PRO	0	0.029	0.009	12.367	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	94	THR	0	0.038	0.006	13.608	0.012	0.012	0.000	0.000	0.000	0.000
71	A	95	ILE	0	0.030	0.018	16.229	-0.019	-0.019	0.000	0.000	0.000	0.000
72	A	96	GLU	-1	-0.866	-0.897	18.172	0.199	0.199	0.000	0.000	0.000	0.000
73	A	97	SER	0	-0.050	-0.035	18.371	0.007	0.007	0.000	0.000	0.000	0.000
74	A	98	LEU	0	-0.032	-0.008	19.550	-0.007	-0.007	0.000	0.000	0.000	0.000
75	A	99	SER	0	-0.049	-0.048	22.043	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	100	LYS	1	0.896	0.951	23.633	-0.106	-0.106	0.000	0.000	0.000	0.000
77	A	101	ARG	1	0.888	0.968	23.979	-0.029	-0.029	0.000	0.000	0.000	0.000
78	A	102	LYS	1	0.947	0.974	22.227	-0.154	-0.154	0.000	0.000	0.000	0.000
79	A	103	ILE	0	0.009	-0.007	17.737	-0.029	-0.029	0.000	0.000	0.000	0.000
80	A	104	ARG	1	0.876	0.947	21.464	-0.057	-0.057	0.000	0.000	0.000	0.000
81	A	105	TYR	0	-0.026	-0.009	23.040	0.009	0.009	0.000	0.000	0.000	0.000
82	A	106	SER	0	0.051	0.030	18.468	-0.017	-0.017	0.000	0.000	0.000	0.000
83	A	107	GLU	-1	-0.971	-0.965	21.459	-0.112	-0.112	0.000	0.000	0.000	0.000
84	A	108	SER	0	-0.034	-0.032	19.332	-0.035	-0.035	0.000	0.000	0.000	0.000
85	A	109	ARG	1	0.929	0.981	21.461	0.269	0.269	0.000	0.000	0.000	0.000
86	A	110	TYR	0	0.008	-0.005	18.094	-0.040	-0.040	0.000	0.000	0.000	0.000
87	A	111	ALA	0	-0.005	-0.005	22.040	0.039	0.039	0.000	0.000	0.000	0.000
88	A	112	ALA	0	0.019	0.022	22.126	-0.041	-0.041	0.000	0.000	0.000	0.000
89	A	113	ARG	1	0.916	0.956	21.742	0.469	0.469	0.000	0.000	0.000	0.000
90	A	114	LEU	0	0.024	0.030	22.665	-0.017	-0.017	0.000	0.000	0.000	0.000
91	A	115	ILE	0	-0.042	0.002	16.207	0.011	0.011	0.000	0.000	0.000	0.000
92	A	116	GLY	0	0.041	0.022	20.401	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	117	ASN	0	0.034	0.000	20.122	-0.078	-0.078	0.000	0.000	0.000	0.000
94	A	118	GLU	-1	-0.921	-0.954	17.112	-0.760	-0.760	0.000	0.000	0.000	0.000
95	A	119	ARG	1	0.888	0.938	15.522	0.641	0.641	0.000	0.000	0.000	0.000
96	A	120	GLY	0	0.004	0.002	15.105	-0.133	-0.133	0.000	0.000	0.000	0.000
97	A	121	HIS	0	0.008	-0.005	15.888	-0.121	-0.121	0.000	0.000	0.000	0.000
98	A	122	PHE	0	-0.008	0.002	11.239	-0.146	-0.146	0.000	0.000	0.000	0.000
99	A	123	LEU	0	-0.040	-0.029	10.520	-0.340	-0.340	0.000	0.000	0.000	0.000
100	A	124	ASP	-1	-0.950	-0.964	12.580	-1.491	-1.491	0.000	0.000	0.000	0.000
101	A	125	ILE	0	-0.095	-0.056	14.996	0.146	0.146	0.000	0.000	0.000	0.000
102	A	126	SER	0	0.011	0.028	17.303	0.014	0.014	0.000	0.000	0.000	0.000
103	A	127	GLU	-1	-0.797	-0.920	20.876	-0.476	-0.476	0.000	0.000	0.000	0.000
104	A	128	ASP	-1	-0.926	-0.983	22.043	-0.384	-0.384	0.000	0.000	0.000	0.000
105	A	129	ALA	0	-0.083	-0.023	20.467	0.033	0.033	0.000	0.000	0.000	0.000
106	A	130	PRO	0	-0.029	-0.035	22.055	-0.020	-0.020	0.000	0.000	0.000	0.000
107	A	131	VAL	0	-0.028	-0.010	17.305	-0.043	-0.043	0.000	0.000	0.000	0.000
108	A	132	LEU	0	-0.057	-0.024	17.138	0.087	0.087	0.000	0.000	0.000	0.000
109	A	133	HIS	0	-0.017	-0.009	17.368	-0.044	-0.044	0.000	0.000	0.000	0.000
110	A	134	LEU	0	-0.008	-0.005	15.594	0.076	0.076	0.000	0.000	0.000	0.000
111	A	135	GLU	-1	-0.831	-0.892	18.593	-0.363	-0.363	0.000	0.000	0.000	0.000
112	A	136	GLN	0	-0.005	-0.025	15.875	0.015	0.015	0.000	0.000	0.000	0.000
113	A	137	LEU	0	-0.075	-0.011	19.665	-0.023	-0.023	0.000	0.000	0.000	0.000
114	A	138	VAL	0	0.045	0.022	17.309	0.031	0.031	0.000	0.000	0.000	0.000
115	A	139	PHE	0	0.010	-0.002	20.802	0.000	0.000	0.000	0.000	0.000	0.000
116	A	140	PHE	0	0.049	0.007	21.716	0.019	0.019	0.000	0.000	0.000	0.000
117	A	141	SER	0	-0.056	-0.042	24.931	0.018	0.018	0.000	0.000	0.000	0.000
118	A	142	ARG	1	0.982	0.989	27.930	0.004	0.004	0.000	0.000	0.000	0.000
119	A	143	GLU	-1	-0.918	-0.977	29.761	-0.031	-0.031	0.000	0.000	0.000	0.000
120	A	144	LEU	0	-0.031	0.004	27.603	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	145	PRO	0	-0.001	0.005	25.126	0.011	0.011	0.000	0.000	0.000	0.000
122	A	146	VAL	0	-0.021	-0.011	20.658	0.009	0.009	0.000	0.000	0.000	0.000
123	A	147	GLU	-1	-0.817	-0.930	17.178	-0.414	-0.414	0.000	0.000	0.000	0.000
124	A	148	PHE	0	-0.004	-0.004	20.449	0.017	0.017	0.000	0.000	0.000	0.000
125	A	149	GLY	0	0.059	0.040	16.916	-0.034	-0.034	0.000	0.000	0.000	0.000
126	A	150	ASN	0	-0.066	-0.036	17.103	0.066	0.066	0.000	0.000	0.000	0.000
127	A	151	VAL	0	-0.012	-0.012	12.558	-0.101	-0.101	0.000	0.000	0.000	0.000
128	A	152	TRP	0	-0.013	-0.014	14.111	0.183	0.183	0.000	0.000	0.000	0.000
129	A	153	LEU	0	-0.001	0.016	12.807	-0.188	-0.188	0.000	0.000	0.000	0.000
130	A	154	LYS	1	0.928	0.963	11.555	1.598	1.598	0.000	0.000	0.000	0.000
131	A	155	GLY	0	0.063	0.023	13.979	0.063	0.063	0.000	0.000	0.000	0.000
132	A	156	ASN	0	-0.076	-0.057	14.589	0.145	0.145	0.000	0.000	0.000	0.000
133	A	157	LYS	1	0.958	0.977	15.424	0.232	0.232	0.000	0.000	0.000	0.000
134	A	158	TYR	0	0.071	0.022	11.202	-0.018	-0.018	0.000	0.000	0.000	0.000
135	A	159	TYR	0	0.018	0.026	11.965	0.057	0.057	0.000	0.000	0.000	0.000
136	A	160	LEU	0	-0.067	-0.023	16.080	0.042	0.042	0.000	0.000	0.000	0.000
137	A	161	GLY	0	0.050	0.031	18.254	0.009	0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:25:THR)