FMO DATABASE

FMODB ID: Q1Q8Y

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1306068.976178
FMO2-HF: Nuclear repulsion	1251124.077271
FMO2-HF: Total energy	-54944.898907
FMO2-MP2: Total energy	-55108.264174

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.
-20.605	-18.928	11.576	-6.413	-6.841	-0.05

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 : 0.002 / q_NPA : -0.011

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	-0.870	-0.919	3.225	-6.158	-3.611	0.063	-0.946	-1.665	0.000
4	A	28	VAL	0	-0.048	-0.040	4.457	0.213	0.252	-0.001	-0.009	-0.030	0.000
5	A	29	ILE	0	-0.002	0.017	8.287	-0.091	-0.091	0.000	0.000	0.000	0.000
6	A	30	THR	0	-0.012	-0.025	10.215	0.177	0.177	0.000	0.000	0.000	0.000
7	A	31	SER	0	-0.044	-0.017	13.449	0.046	0.046	0.000	0.000	0.000	0.000
8	A	32	ARG	1	0.855	0.921	15.845	0.306	0.306	0.000	0.000	0.000	0.000
9	A	33	ILE	0	0.027	0.032	19.588	0.019	0.019	0.000	0.000	0.000	0.000
10	A	34	GLU	-1	-0.762	-0.855	22.235	-0.232	-0.232	0.000	0.000	0.000	0.000
11	A	35	PRO	0	0.071	0.036	24.685	0.016	0.016	0.000	0.000	0.000	0.000
12	A	36	ALA	0	-0.003	0.013	26.397	-0.015	-0.015	0.000	0.000	0.000	0.000
13	A	37	ASN	0	0.031	0.015	25.942	0.018	0.018	0.000	0.000	0.000	0.000
14	A	38	ARG	1	1.019	0.981	29.044	0.085	0.085	0.000	0.000	0.000	0.000
15	A	39	TYR	0	-0.079	-0.050	25.916	0.017	0.017	0.000	0.000	0.000	0.000
16	A	40	VAL	0	0.063	0.013	24.301	0.011	0.011	0.000	0.000	0.000	0.000
17	A	41	ALA	0	-0.022	-0.002	26.804	0.017	0.017	0.000	0.000	0.000	0.000
18	A	42	GLU	-1	-0.852	-0.912	29.468	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	43	LYS	1	0.795	0.890	26.059	0.028	0.028	0.000	0.000	0.000	0.000
20	A	44	LEU	0	-0.007	-0.014	23.264	0.020	0.020	0.000	0.000	0.000	0.000
21	A	45	ARG	1	0.830	0.933	27.385	-0.070	-0.070	0.000	0.000	0.000	0.000
22	A	46	ILE	0	0.002	0.021	27.264	0.007	0.007	0.000	0.000	0.000	0.000
23	A	47	THR	0	0.000	0.002	31.408	-0.005	-0.005	0.000	0.000	0.000	0.000
24	A	48	PRO	0	-0.021	-0.037	31.710	-0.006	-0.006	0.000	0.000	0.000	0.000
25	A	49	GLY	0	-0.028	-0.013	30.925	0.003	0.003	0.000	0.000	0.000	0.000
26	A	50	GLN	0	-0.054	-0.034	29.024	-0.004	-0.004	0.000	0.000	0.000	0.000
27	A	51	ASP	-1	-0.861	-0.923	26.361	-0.070	-0.070	0.000	0.000	0.000	0.000
28	A	52	ILE	0	-0.078	-0.040	21.768	0.022	0.022	0.000	0.000	0.000	0.000
29	A	53	LEU	0	0.019	0.010	17.194	-0.021	-0.021	0.000	0.000	0.000	0.000
30	A	54	TYR	0	-0.066	-0.060	16.407	0.010	0.010	0.000	0.000	0.000	0.000
31	A	55	LEU	0	-0.007	-0.018	12.565	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	56	GLU	-1	-0.876	-0.939	11.713	-0.742	-0.742	0.000	0.000	0.000	0.000
33	A	57	ARG	1	0.902	0.942	7.486	-0.157	-0.157	0.000	0.000	0.000	0.000
34	A	58	LEU	0	0.029	0.036	6.325	0.407	0.407	0.000	0.000	0.000	0.000
35	A	59	ARG	1	0.928	0.953	3.969	-2.968	-2.679	-0.001	-0.080	-0.208	0.000
36	A	60	SER	0	0.033	0.004	2.450	-2.666	-0.483	1.507	-1.487	-2.202	-0.013
37	A	61	ILE	0	-0.040	-0.034	1.838	-4.999	-8.644	10.010	-3.858	-2.507	-0.037
38	A	62	GLY	0	-0.009	-0.011	3.986	0.163	0.301	-0.001	-0.027	-0.110	0.000
39	A	63	ASP	-1	-0.932	-0.955	4.604	-4.734	-4.608	-0.001	-0.006	-0.119	0.000
40	A	64	GLU	-1	-0.860	-0.911	5.740	-0.708	-0.708	0.000	0.000	0.000	0.000
41	A	65	LYS	1	0.927	0.968	6.199	1.766	1.766	0.000	0.000	0.000	0.000
42	A	66	ALA	0	0.004	0.007	6.514	0.666	0.666	0.000	0.000	0.000	0.000
43	A	67	MET	0	-0.056	-0.037	7.587	0.609	0.609	0.000	0.000	0.000	0.000
44	A	68	LEU	0	0.036	0.042	8.855	-0.416	-0.416	0.000	0.000	0.000	0.000
45	A	69	ILE	0	-0.062	-0.038	8.971	0.312	0.312	0.000	0.000	0.000	0.000
46	A	70	GLU	-1	-0.719	-0.816	12.145	-0.498	-0.498	0.000	0.000	0.000	0.000
47	A	71	ASN	0	-0.037	-0.044	13.129	0.051	0.051	0.000	0.000	0.000	0.000
48	A	72	ARG	1	0.822	0.911	16.160	0.163	0.163	0.000	0.000	0.000	0.000
49	A	73	ILE	0	0.024	0.006	16.218	0.043	0.043	0.000	0.000	0.000	0.000
50	A	74	ASN	0	0.029	0.009	20.761	-0.030	-0.030	0.000	0.000	0.000	0.000
51	A	75	ILE	0	0.056	0.001	21.790	0.029	0.029	0.000	0.000	0.000	0.000
52	A	76	GLU	-1	-0.854	-0.896	24.173	0.054	0.054	0.000	0.000	0.000	0.000
53	A	77	LEU	0	-0.081	-0.037	24.875	0.015	0.015	0.000	0.000	0.000	0.000
54	A	78	CYS	0	-0.113	-0.049	21.577	0.028	0.028	0.000	0.000	0.000	0.000
55	A	79	PRO	0	0.054	0.010	23.137	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	80	GLY	0	0.074	0.041	22.959	0.029	0.029	0.000	0.000	0.000	0.000
57	A	81	ILE	0	-0.035	-0.019	17.148	0.006	0.006	0.000	0.000	0.000	0.000
58	A	82	VAL	0	-0.012	-0.016	18.286	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	83	GLU	-1	-0.937	-0.960	19.211	0.052	0.052	0.000	0.000	0.000	0.000
60	A	84	ILE	0	-0.085	-0.028	13.909	0.024	0.024	0.000	0.000	0.000	0.000
61	A	85	ASP	-1	-0.767	-0.876	11.147	-0.168	-0.168	0.000	0.000	0.000	0.000
62	A	86	PHE	0	-0.033	-0.045	10.502	0.150	0.150	0.000	0.000	0.000	0.000
63	A	87	ASN	0	-0.026	-0.014	6.811	-0.303	-0.303	0.000	0.000	0.000	0.000
64	A	88	GLN	0	-0.023	-0.008	6.908	0.434	0.434	0.000	0.000	0.000	0.000
65	A	89	HIS	0	-0.028	0.010	9.574	0.247	0.247	0.000	0.000	0.000	0.000
66	A	90	ASN	0	0.016	0.004	7.786	0.260	0.260	0.000	0.000	0.000	0.000
67	A	91	LEU	0	0.008	0.020	10.117	-0.141	-0.141	0.000	0.000	0.000	0.000
68	A	92	PHE	0	0.039	0.004	12.418	-0.035	-0.035	0.000	0.000	0.000	0.000
69	A	93	PRO	0	0.037	0.011	12.431	-0.079	-0.079	0.000	0.000	0.000	0.000
70	A	94	THR	0	0.041	0.011	13.679	-0.079	-0.079	0.000	0.000	0.000	0.000
71	A	95	ILE	0	0.026	0.016	16.222	-0.070	-0.070	0.000	0.000	0.000	0.000
72	A	96	GLU	-1	-0.866	-0.904	18.155	0.514	0.514	0.000	0.000	0.000	0.000
73	A	97	SER	0	-0.049	-0.033	18.359	-0.036	-0.036	0.000	0.000	0.000	0.000
74	A	98	LEU	0	-0.013	0.001	19.605	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	99	SER	0	-0.046	-0.040	22.148	-0.034	-0.034	0.000	0.000	0.000	0.000
76	A	100	LYS	1	0.848	0.932	23.624	-0.264	-0.264	0.000	0.000	0.000	0.000
77	A	101	ARG	1	0.899	0.975	23.972	-0.208	-0.208	0.000	0.000	0.000	0.000
78	A	102	LYS	1	0.942	0.967	22.525	-0.353	-0.353	0.000	0.000	0.000	0.000
79	A	103	ILE	0	0.013	-0.006	18.102	-0.048	-0.048	0.000	0.000	0.000	0.000
80	A	104	ARG	1	0.876	0.947	22.035	-0.250	-0.250	0.000	0.000	0.000	0.000
81	A	105	TYR	0	-0.015	-0.005	23.914	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	106	SER	0	0.017	0.013	19.691	0.002	0.002	0.000	0.000	0.000	0.000
83	A	107	GLU	-1	-0.903	-0.934	22.327	0.103	0.103	0.000	0.000	0.000	0.000
84	A	108	SER	0	-0.019	-0.019	19.761	0.005	0.005	0.000	0.000	0.000	0.000
85	A	109	ARG	1	0.861	0.937	21.896	0.044	0.044	0.000	0.000	0.000	0.000
86	A	110	TYR	0	0.016	0.001	18.405	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	111	ALA	0	-0.002	-0.005	21.909	0.010	0.010	0.000	0.000	0.000	0.000
88	A	112	ALA	0	0.019	0.020	22.008	-0.021	-0.021	0.000	0.000	0.000	0.000
89	A	113	ARG	1	0.894	0.941	21.593	0.238	0.238	0.000	0.000	0.000	0.000
90	A	114	LEU	0	0.030	0.028	22.575	-0.010	-0.010	0.000	0.000	0.000	0.000
91	A	115	ILE	0	-0.047	-0.007	16.439	0.007	0.007	0.000	0.000	0.000	0.000
92	A	116	GLY	0	0.048	0.031	20.511	0.009	0.009	0.000	0.000	0.000	0.000
93	A	117	ASN	0	0.038	0.003	20.211	-0.082	-0.082	0.000	0.000	0.000	0.000
94	A	118	GLU	-1	-0.939	-0.969	17.415	-0.581	-0.581	0.000	0.000	0.000	0.000
95	A	119	ARG	1	0.884	0.919	15.625	0.388	0.388	0.000	0.000	0.000	0.000
96	A	120	GLY	0	0.008	0.009	15.196	-0.108	-0.108	0.000	0.000	0.000	0.000
97	A	121	HIS	0	-0.010	-0.011	15.975	-0.137	-0.137	0.000	0.000	0.000	0.000
98	A	122	PHE	0	-0.032	-0.011	11.272	-0.157	-0.157	0.000	0.000	0.000	0.000
99	A	123	LEU	0	-0.044	-0.033	10.385	-0.304	-0.304	0.000	0.000	0.000	0.000
100	A	124	ASP	-1	-0.926	-0.956	12.212	-1.580	-1.580	0.000	0.000	0.000	0.000
101	A	125	ILE	0	-0.063	-0.040	15.110	0.138	0.138	0.000	0.000	0.000	0.000
102	A	126	SER	0	-0.001	0.024	17.392	0.007	0.007	0.000	0.000	0.000	0.000
103	A	127	GLU	-1	-0.789	-0.916	20.968	-0.387	-0.387	0.000	0.000	0.000	0.000
104	A	128	ASP	-1	-0.933	-0.985	22.154	-0.291	-0.291	0.000	0.000	0.000	0.000
105	A	129	ALA	0	-0.098	-0.027	20.466	0.034	0.034	0.000	0.000	0.000	0.000
106	A	130	PRO	0	-0.027	-0.028	22.058	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	131	VAL	0	-0.013	-0.002	17.082	-0.030	-0.030	0.000	0.000	0.000	0.000
108	A	132	LEU	0	-0.073	-0.037	17.082	0.065	0.065	0.000	0.000	0.000	0.000
109	A	133	HIS	0	-0.014	-0.008	17.254	-0.031	-0.031	0.000	0.000	0.000	0.000
110	A	134	LEU	0	-0.014	-0.009	15.809	0.050	0.050	0.000	0.000	0.000	0.000
111	A	135	GLU	-1	-0.782	-0.847	18.636	-0.099	-0.099	0.000	0.000	0.000	0.000
112	A	136	GLN	0	-0.015	-0.036	16.491	0.066	0.066	0.000	0.000	0.000	0.000
113	A	137	LEU	0	-0.060	-0.002	20.137	-0.018	-0.018	0.000	0.000	0.000	0.000
114	A	138	VAL	0	0.032	0.013	18.013	0.030	0.030	0.000	0.000	0.000	0.000
115	A	139	PHE	0	0.001	-0.004	21.497	-0.025	-0.025	0.000	0.000	0.000	0.000
116	A	140	PHE	0	0.051	0.008	21.845	0.030	0.030	0.000	0.000	0.000	0.000
117	A	141	SER	0	-0.048	-0.049	25.358	0.011	0.011	0.000	0.000	0.000	0.000
118	A	142	ARG	1	0.952	0.980	28.540	-0.157	-0.157	0.000	0.000	0.000	0.000
119	A	143	GLU	-1	-0.877	-0.954	30.534	0.127	0.127	0.000	0.000	0.000	0.000
120	A	144	LEU	0	-0.010	0.011	27.673	-0.012	-0.012	0.000	0.000	0.000	0.000
121	A	145	PRO	0	0.004	0.003	25.567	0.028	0.028	0.000	0.000	0.000	0.000
122	A	146	VAL	0	-0.032	-0.013	20.941	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	147	GLU	-1	-0.823	-0.927	17.394	0.087	0.087	0.000	0.000	0.000	0.000
124	A	148	PHE	0	0.004	-0.001	20.564	0.010	0.010	0.000	0.000	0.000	0.000
125	A	149	GLY	0	0.057	0.039	17.244	-0.036	-0.036	0.000	0.000	0.000	0.000
126	A	150	ASN	0	-0.064	-0.027	17.280	0.010	0.010	0.000	0.000	0.000	0.000
127	A	151	VAL	0	-0.016	-0.013	12.431	-0.051	-0.051	0.000	0.000	0.000	0.000
128	A	152	TRP	0	0.002	-0.016	13.978	0.102	0.102	0.000	0.000	0.000	0.000
129	A	153	LEU	0	-0.009	0.005	12.714	-0.130	-0.130	0.000	0.000	0.000	0.000
130	A	154	LYS	1	0.907	0.946	10.964	1.468	1.468	0.000	0.000	0.000	0.000
131	A	155	GLY	0	0.032	0.021	13.893	0.020	0.020	0.000	0.000	0.000	0.000
132	A	156	ASN	0	-0.063	-0.057	14.505	0.091	0.091	0.000	0.000	0.000	0.000
133	A	157	LYS	1	0.944	0.968	15.329	0.020	0.020	0.000	0.000	0.000	0.000
134	A	158	TYR	0	0.053	0.019	11.182	-0.021	-0.021	0.000	0.000	0.000	0.000
135	A	159	TYR	0	0.021	0.019	12.334	0.134	0.134	0.000	0.000	0.000	0.000
136	A	160	LEU	0	-0.075	-0.020	16.511	0.004	0.004	0.000	0.000	0.000	0.000
137	A	161	GLY	0	0.058	0.031	18.665	0.035	0.035	0.000	0.000	0.000	0.000

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