FMO DATABASE

FMODB ID: K3NR3

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	OptAll
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	-1306731.972859
FMO2-HF: Nuclear repulsion	1251786.329877
FMO2-HF: Total energy	-54945.642982
FMO2-MP2: Total energy	-55109.009252

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.
-21.152	-16.017	6.265	-4.866	-6.533	-0.046

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 : 0.004 / q_NPA : -0.006

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	-0.871	-0.921	3.320	-5.256	-3.069	0.015	-0.844	-1.357	0.000
4	A	28	VAL	0	-0.046	-0.040	4.609	0.159	0.191	-0.001	-0.006	-0.025	0.000
5	A	29	ILE	0	0.001	0.023	8.455	-0.028	-0.028	0.000	0.000	0.000	0.000
6	A	30	THR	0	-0.015	-0.019	10.338	0.170	0.170	0.000	0.000	0.000	0.000
7	A	31	SER	0	-0.032	-0.014	13.379	0.043	0.043	0.000	0.000	0.000	0.000
8	A	32	ARG	1	0.839	0.910	15.798	0.296	0.296	0.000	0.000	0.000	0.000
9	A	33	ILE	0	0.019	0.020	19.550	0.018	0.018	0.000	0.000	0.000	0.000
10	A	34	GLU	-1	-0.767	-0.862	21.811	-0.229	-0.229	0.000	0.000	0.000	0.000
11	A	35	PRO	0	0.053	0.029	24.529	0.015	0.015	0.000	0.000	0.000	0.000
12	A	36	ALA	0	-0.007	0.010	26.361	-0.016	-0.016	0.000	0.000	0.000	0.000
13	A	37	ASN	0	0.037	0.015	25.653	0.020	0.020	0.000	0.000	0.000	0.000
14	A	38	ARG	1	0.987	0.969	29.000	0.084	0.084	0.000	0.000	0.000	0.000
15	A	39	TYR	0	-0.043	-0.034	25.755	0.018	0.018	0.000	0.000	0.000	0.000
16	A	40	VAL	0	0.043	0.011	23.985	0.010	0.010	0.000	0.000	0.000	0.000
17	A	41	ALA	0	-0.005	0.003	26.476	0.018	0.018	0.000	0.000	0.000	0.000
18	A	42	GLU	-1	-0.830	-0.900	29.268	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	43	LYS	1	0.769	0.877	25.607	0.043	0.043	0.000	0.000	0.000	0.000
20	A	44	LEU	0	-0.012	-0.018	22.818	0.021	0.021	0.000	0.000	0.000	0.000
21	A	45	ARG	1	0.793	0.906	26.871	-0.067	-0.067	0.000	0.000	0.000	0.000
22	A	46	ILE	0	-0.020	0.011	27.087	0.008	0.008	0.000	0.000	0.000	0.000
23	A	47	THR	0	0.011	0.006	31.181	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	48	PRO	0	-0.057	-0.053	31.711	-0.007	-0.007	0.000	0.000	0.000	0.000
25	A	49	GLY	0	-0.022	-0.004	30.957	0.001	0.001	0.000	0.000	0.000	0.000
26	A	50	GLN	0	-0.007	-0.022	29.447	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	51	ASP	-1	-0.874	-0.937	26.345	-0.059	-0.059	0.000	0.000	0.000	0.000
28	A	52	ILE	0	-0.063	-0.033	21.588	0.022	0.022	0.000	0.000	0.000	0.000
29	A	53	LEU	0	0.012	0.010	16.976	-0.023	-0.023	0.000	0.000	0.000	0.000
30	A	54	TYR	0	-0.050	-0.041	16.285	0.010	0.010	0.000	0.000	0.000	0.000
31	A	55	LEU	0	-0.020	-0.022	12.211	0.007	0.007	0.000	0.000	0.000	0.000
32	A	56	GLU	-1	-0.874	-0.935	11.550	-0.770	-0.770	0.000	0.000	0.000	0.000
33	A	57	ARG	1	0.890	0.926	7.138	-0.276	-0.276	0.000	0.000	0.000	0.000
34	A	58	LEU	0	0.033	0.037	5.949	0.325	0.325	0.000	0.000	0.000	0.000
35	A	59	ARG	1	0.908	0.938	3.554	-2.076	-1.708	0.001	-0.098	-0.272	0.000
36	A	60	SER	0	-0.004	0.012	2.488	-2.710	-0.771	1.470	-1.272	-2.138	-0.013
37	A	61	ILE	0	-0.028	-0.034	2.047	-6.096	-5.767	4.783	-2.617	-2.495	-0.033
38	A	62	GLY	0	-0.020	-0.014	4.360	0.249	0.343	-0.001	-0.019	-0.074	0.000
39	A	63	ASP	-1	-0.931	-0.963	4.501	-5.657	-5.498	-0.001	-0.009	-0.148	0.000
40	A	64	GLU	-1	-0.832	-0.893	5.357	-1.471	-1.444	-0.001	-0.001	-0.024	0.000
41	A	65	LYS	1	0.957	0.983	6.339	2.110	2.110	0.000	0.000	0.000	0.000
42	A	66	ALA	0	0.007	0.002	6.666	0.636	0.636	0.000	0.000	0.000	0.000
43	A	67	MET	0	-0.059	-0.018	7.175	0.735	0.735	0.000	0.000	0.000	0.000
44	A	68	LEU	0	0.055	0.039	8.536	-0.495	-0.495	0.000	0.000	0.000	0.000
45	A	69	ILE	0	-0.057	-0.033	8.691	0.330	0.330	0.000	0.000	0.000	0.000
46	A	70	GLU	-1	-0.723	-0.832	11.997	-0.464	-0.464	0.000	0.000	0.000	0.000
47	A	71	ASN	0	-0.020	-0.035	12.703	0.077	0.077	0.000	0.000	0.000	0.000
48	A	72	ARG	1	0.809	0.891	15.577	0.165	0.165	0.000	0.000	0.000	0.000
49	A	73	ILE	0	0.013	0.007	15.839	0.045	0.045	0.000	0.000	0.000	0.000
50	A	74	ASN	0	0.034	0.005	20.339	-0.030	-0.030	0.000	0.000	0.000	0.000
51	A	75	ILE	0	0.050	0.002	21.860	0.030	0.030	0.000	0.000	0.000	0.000
52	A	76	GLU	-1	-0.834	-0.879	23.978	0.066	0.066	0.000	0.000	0.000	0.000
53	A	77	LEU	0	-0.100	-0.045	24.848	0.013	0.013	0.000	0.000	0.000	0.000
54	A	78	CYS	0	-0.103	-0.051	21.496	0.030	0.030	0.000	0.000	0.000	0.000
55	A	79	PRO	0	0.053	0.015	22.869	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	80	GLY	0	0.046	0.029	22.816	0.028	0.028	0.000	0.000	0.000	0.000
57	A	81	ILE	0	-0.050	-0.028	17.005	0.018	0.018	0.000	0.000	0.000	0.000
58	A	82	VAL	0	-0.002	-0.012	18.390	-0.010	-0.010	0.000	0.000	0.000	0.000
59	A	83	GLU	-1	-0.901	-0.947	19.469	0.085	0.085	0.000	0.000	0.000	0.000
60	A	84	ILE	0	-0.072	-0.020	14.096	0.031	0.031	0.000	0.000	0.000	0.000
61	A	85	ASP	-1	-0.779	-0.882	11.152	-0.039	-0.039	0.000	0.000	0.000	0.000
62	A	86	PHE	0	-0.021	-0.041	10.551	0.156	0.156	0.000	0.000	0.000	0.000
63	A	87	ASN	0	-0.020	-0.014	6.959	-0.309	-0.309	0.000	0.000	0.000	0.000
64	A	88	GLN	0	-0.032	-0.007	7.072	0.504	0.504	0.000	0.000	0.000	0.000
65	A	89	HIS	0	-0.021	0.006	9.816	0.236	0.236	0.000	0.000	0.000	0.000
66	A	90	ASN	0	0.004	-0.004	8.101	0.184	0.184	0.000	0.000	0.000	0.000
67	A	91	LEU	0	0.042	0.035	10.328	-0.129	-0.129	0.000	0.000	0.000	0.000
68	A	92	PHE	0	0.030	0.010	12.615	-0.051	-0.051	0.000	0.000	0.000	0.000
69	A	93	PRO	0	0.057	0.017	12.764	-0.081	-0.081	0.000	0.000	0.000	0.000
70	A	94	THR	0	0.017	0.015	13.830	-0.083	-0.083	0.000	0.000	0.000	0.000
71	A	95	ILE	0	0.034	0.017	16.395	-0.070	-0.070	0.000	0.000	0.000	0.000
72	A	96	GLU	-1	-0.868	-0.909	18.359	0.535	0.535	0.000	0.000	0.000	0.000
73	A	97	SER	0	-0.036	-0.033	18.396	-0.042	-0.042	0.000	0.000	0.000	0.000
74	A	98	LEU	0	-0.044	-0.007	19.643	-0.034	-0.034	0.000	0.000	0.000	0.000
75	A	99	SER	0	-0.041	-0.040	22.308	-0.035	-0.035	0.000	0.000	0.000	0.000
76	A	100	LYS	1	0.837	0.921	23.754	-0.283	-0.283	0.000	0.000	0.000	0.000
77	A	101	ARG	1	0.882	0.966	24.053	-0.222	-0.222	0.000	0.000	0.000	0.000
78	A	102	LYS	1	0.960	0.970	22.379	-0.384	-0.384	0.000	0.000	0.000	0.000
79	A	103	ILE	0	0.012	0.001	18.098	-0.050	-0.050	0.000	0.000	0.000	0.000
80	A	104	ARG	1	0.858	0.931	22.100	-0.255	-0.255	0.000	0.000	0.000	0.000
81	A	105	TYR	0	-0.005	-0.002	23.850	-0.018	-0.018	0.000	0.000	0.000	0.000
82	A	106	SER	0	0.036	0.013	19.631	0.025	0.025	0.000	0.000	0.000	0.000
83	A	107	GLU	-1	-0.928	-0.941	21.894	0.093	0.093	0.000	0.000	0.000	0.000
84	A	108	SER	0	-0.037	-0.046	19.565	0.016	0.016	0.000	0.000	0.000	0.000
85	A	109	ARG	1	0.853	0.930	21.571	0.069	0.069	0.000	0.000	0.000	0.000
86	A	110	TYR	0	0.018	0.007	17.877	-0.022	-0.022	0.000	0.000	0.000	0.000
87	A	111	ALA	0	-0.006	-0.002	21.490	0.014	0.014	0.000	0.000	0.000	0.000
88	A	112	ALA	0	0.021	0.018	21.701	-0.025	-0.025	0.000	0.000	0.000	0.000
89	A	113	ARG	1	0.870	0.932	21.507	0.275	0.275	0.000	0.000	0.000	0.000
90	A	114	LEU	0	0.033	0.025	22.738	-0.011	-0.011	0.000	0.000	0.000	0.000
91	A	115	ILE	0	-0.038	-0.010	16.239	0.020	0.020	0.000	0.000	0.000	0.000
92	A	116	GLY	0	0.039	0.023	20.038	-0.004	-0.004	0.000	0.000	0.000	0.000
93	A	117	ASN	0	-0.023	-0.043	19.997	-0.090	-0.090	0.000	0.000	0.000	0.000
94	A	118	GLU	-1	-0.902	-0.944	17.255	-0.565	-0.565	0.000	0.000	0.000	0.000
95	A	119	ARG	1	0.856	0.900	15.379	0.436	0.436	0.000	0.000	0.000	0.000
96	A	120	GLY	0	0.009	0.017	15.037	-0.107	-0.107	0.000	0.000	0.000	0.000
97	A	121	HIS	0	-0.012	-0.015	15.512	-0.152	-0.152	0.000	0.000	0.000	0.000
98	A	122	PHE	0	-0.041	-0.018	11.172	-0.156	-0.156	0.000	0.000	0.000	0.000
99	A	123	LEU	0	-0.028	-0.023	10.072	-0.343	-0.343	0.000	0.000	0.000	0.000
100	A	124	ASP	-1	-0.875	-0.938	11.587	-1.757	-1.757	0.000	0.000	0.000	0.000
101	A	125	ILE	0	-0.080	-0.036	14.574	0.148	0.148	0.000	0.000	0.000	0.000
102	A	126	SER	0	0.019	0.011	17.143	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	127	GLU	-1	-0.828	-0.919	20.588	-0.426	-0.426	0.000	0.000	0.000	0.000
104	A	128	ASP	-1	-0.948	-0.984	22.318	-0.322	-0.322	0.000	0.000	0.000	0.000
105	A	129	ALA	0	-0.005	0.021	20.055	0.032	0.032	0.000	0.000	0.000	0.000
106	A	130	PRO	0	-0.039	-0.025	21.600	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	131	VAL	0	0.005	-0.001	17.261	-0.041	-0.041	0.000	0.000	0.000	0.000
108	A	132	LEU	0	-0.067	-0.019	16.781	0.074	0.074	0.000	0.000	0.000	0.000
109	A	133	HIS	0	-0.003	-0.009	17.139	-0.046	-0.046	0.000	0.000	0.000	0.000
110	A	134	LEU	0	-0.006	-0.007	15.344	0.053	0.053	0.000	0.000	0.000	0.000
111	A	135	GLU	-1	-0.767	-0.828	18.064	-0.106	-0.106	0.000	0.000	0.000	0.000
112	A	136	GLN	0	-0.039	-0.040	15.759	0.066	0.066	0.000	0.000	0.000	0.000
113	A	137	LEU	0	-0.045	0.002	19.640	-0.019	-0.019	0.000	0.000	0.000	0.000
114	A	138	VAL	0	0.034	0.019	17.716	0.026	0.026	0.000	0.000	0.000	0.000
115	A	139	PHE	0	0.014	0.002	21.204	-0.020	-0.020	0.000	0.000	0.000	0.000
116	A	140	PHE	0	0.052	0.012	21.906	0.031	0.031	0.000	0.000	0.000	0.000
117	A	141	SER	0	-0.076	-0.073	25.453	0.009	0.009	0.000	0.000	0.000	0.000
118	A	142	ARG	1	0.962	0.991	28.414	-0.148	-0.148	0.000	0.000	0.000	0.000
119	A	143	GLU	-1	-0.820	-0.898	30.216	0.128	0.128	0.000	0.000	0.000	0.000
120	A	144	LEU	0	-0.013	0.004	27.637	-0.015	-0.015	0.000	0.000	0.000	0.000
121	A	145	PRO	0	0.012	0.006	25.253	0.029	0.029	0.000	0.000	0.000	0.000
122	A	146	VAL	0	-0.043	-0.018	20.820	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	147	GLU	-1	-0.795	-0.905	17.121	0.069	0.069	0.000	0.000	0.000	0.000
124	A	148	PHE	0	-0.003	-0.007	20.203	0.008	0.008	0.000	0.000	0.000	0.000
125	A	149	GLY	0	0.067	0.057	16.710	-0.046	-0.046	0.000	0.000	0.000	0.000
126	A	150	ASN	0	-0.050	-0.027	16.738	-0.008	-0.008	0.000	0.000	0.000	0.000
127	A	151	VAL	0	-0.024	-0.002	12.029	-0.064	-0.064	0.000	0.000	0.000	0.000
128	A	152	TRP	0	-0.014	-0.024	13.714	0.103	0.103	0.000	0.000	0.000	0.000
129	A	153	LEU	0	-0.013	-0.015	12.736	-0.147	-0.147	0.000	0.000	0.000	0.000
130	A	154	LYS	1	0.847	0.932	10.653	1.749	1.749	0.000	0.000	0.000	0.000
131	A	155	GLY	0	0.058	0.037	14.292	0.013	0.013	0.000	0.000	0.000	0.000
132	A	156	ASN	0	-0.055	-0.037	14.592	0.123	0.123	0.000	0.000	0.000	0.000
133	A	157	LYS	1	0.928	0.954	14.968	0.043	0.043	0.000	0.000	0.000	0.000
134	A	158	TYR	0	0.081	0.025	10.991	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	159	TYR	0	-0.009	0.006	11.718	0.157	0.157	0.000	0.000	0.000	0.000
136	A	160	LEU	0	-0.046	-0.023	15.931	-0.020	-0.020	0.000	0.000	0.000	0.000
137	A	161	GLY	0	0.022	0.025	18.700	0.006	0.006	0.000	0.000	0.000	0.000

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