FMO DATABASE

FMODB ID: QYK2Y

Calculation Name: 1HFO-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1HFO

Chain ID: A

ChEMBL ID:

UniProt ID: P81529

Base Structure: X-ray

Registration Date: 2023-06-22

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	113
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-825114.605937
FMO2-HF: Nuclear repulsion	782763.361718
FMO2-HF: Total energy	-42351.244218
FMO2-MP2: Total energy	-42476.247888

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:1:PRO)

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

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.
-18.29	-7.994	16.266	-8.931	-17.628	-0.062

Interaction energy analysis for fragmet #1(A:1:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.025 / q_NPA : -0.026

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	3	PHE	0	0.001	0.002	3.767	0.356	2.056	-0.026	-0.737	-0.937	0.002
4	A	4	THR	0	-0.021	0.004	6.156	-0.079	-0.079	0.000	0.000	0.000	0.000
5	A	5	LEU	0	0.006	-0.003	9.715	0.156	0.156	0.000	0.000	0.000	0.000
6	A	6	ASN	0	0.016	0.017	12.897	-0.033	-0.033	0.000	0.000	0.000	0.000
7	A	7	THR	0	-0.001	-0.010	16.559	0.029	0.029	0.000	0.000	0.000	0.000
8	A	8	ASN	0	0.045	0.019	19.204	-0.014	-0.014	0.000	0.000	0.000	0.000
9	A	9	ILE	0	-0.002	0.009	19.145	0.012	0.012	0.000	0.000	0.000	0.000
10	A	10	LYS	1	1.021	1.001	22.579	0.145	0.145	0.000	0.000	0.000	0.000
11	A	11	ALA	0	0.045	0.023	20.982	-0.012	-0.012	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.086	-0.050	21.627	-0.013	-0.013	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.912	-0.952	23.056	-0.169	-0.169	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.073	-0.019	16.583	-0.010	-0.010	0.000	0.000	0.000	0.000
15	A	15	PRO	0	-0.006	0.006	17.665	0.000	0.000	0.000	0.000	0.000	0.000
16	A	16	SER	0	0.038	0.000	18.029	-0.041	-0.041	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.900	-0.940	16.609	-0.364	-0.364	0.000	0.000	0.000	0.000
18	A	18	PHE	0	0.061	0.039	12.127	-0.038	-0.038	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.058	0.039	11.153	-0.061	-0.061	0.000	0.000	0.000	0.000
20	A	20	SER	0	0.025	0.027	10.347	-0.152	-0.152	0.000	0.000	0.000	0.000
21	A	21	SER	0	-0.012	-0.027	11.083	-0.055	-0.055	0.000	0.000	0.000	0.000
22	A	22	THR	0	0.032	-0.004	7.732	0.069	0.069	0.000	0.000	0.000	0.000
23	A	23	SER	0	-0.017	-0.027	6.395	-0.190	-0.190	0.000	0.000	0.000	0.000
24	A	24	ALA	0	-0.034	-0.013	6.646	-0.084	-0.084	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.015	0.000	8.339	0.079	0.079	0.000	0.000	0.000	0.000
26	A	26	VAL	0	0.046	0.015	2.586	-0.312	0.058	1.028	-0.343	-1.055	-0.001
27	A	27	GLY	0	0.028	0.018	3.661	0.013	0.301	0.003	-0.059	-0.231	0.000
28	A	28	ASN	0	-0.004	-0.009	4.675	0.284	0.354	-0.001	-0.002	-0.066	0.000
29	A	29	ILE	0	-0.049	-0.025	6.484	0.127	0.127	0.000	0.000	0.000	0.000
30	A	30	LEU	0	-0.054	-0.033	2.491	-0.456	-0.382	2.329	-0.500	-1.903	-0.001
31	A	31	SER	0	-0.054	-0.016	5.304	0.142	0.183	-0.001	-0.002	-0.038	0.000
32	A	32	LYS	1	0.856	0.934	2.456	-4.263	-3.175	1.828	-0.621	-2.295	0.003
33	A	33	PRO	0	0.035	0.013	4.648	-0.419	-0.313	-0.001	-0.013	-0.091	0.000
34	A	34	GLY	0	0.071	0.019	4.334	-0.639	-0.506	-0.001	-0.012	-0.119	0.000
35	A	35	SER	0	-0.021	-0.009	5.886	-0.423	-0.423	0.000	0.000	0.000	0.000
36	A	36	TYR	0	-0.021	-0.008	3.032	-0.579	0.347	0.181	-0.285	-0.823	-0.001
37	A	37	VAL	0	-0.054	-0.010	2.072	-10.093	-8.568	6.738	-3.344	-4.919	-0.032
38	A	38	ALA	0	-0.003	0.010	3.300	1.863	2.408	0.036	0.039	-0.620	0.000
39	A	39	VAL	0	-0.009	-0.020	5.045	-0.213	-0.250	-0.001	-0.013	0.051	0.000
40	A	40	HIS	0	-0.037	-0.028	7.532	0.250	0.250	0.000	0.000	0.000	0.000
41	A	41	ILE	0	-0.012	-0.009	10.716	0.029	0.029	0.000	0.000	0.000	0.000
42	A	42	ASN	0	-0.008	0.013	13.695	0.020	0.020	0.000	0.000	0.000	0.000
43	A	43	THR	0	0.016	-0.014	16.859	0.013	0.013	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.884	-0.945	19.793	-0.191	-0.191	0.000	0.000	0.000	0.000
45	A	45	GLN	0	-0.064	-0.022	19.923	0.027	0.027	0.000	0.000	0.000	0.000
46	A	46	GLN	0	-0.010	-0.003	23.133	0.016	0.016	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.014	0.005	20.343	0.003	0.003	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.032	-0.010	24.364	0.004	0.004	0.000	0.000	0.000	0.000
49	A	49	PHE	0	0.030	0.008	20.235	0.004	0.004	0.000	0.000	0.000	0.000
50	A	50	GLY	0	0.013	-0.004	25.167	0.001	0.001	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.009	0.009	27.804	0.002	0.002	0.000	0.000	0.000	0.000
52	A	52	SER	0	0.010	0.009	28.712	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	53	THR	0	0.031	0.000	27.690	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.004	0.017	27.814	-0.009	-0.009	0.000	0.000	0.000	0.000
55	A	55	PRO	0	0.065	0.031	23.614	0.001	0.001	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.005	-0.004	21.437	0.014	0.014	0.000	0.000	0.000	0.000
57	A	57	ALA	0	0.028	0.001	16.565	-0.020	-0.020	0.000	0.000	0.000	0.000
58	A	58	PHE	0	0.006	0.011	15.646	0.027	0.027	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.045	0.014	12.031	-0.047	-0.047	0.000	0.000	0.000	0.000
60	A	60	THR	0	-0.072	-0.020	8.035	0.106	0.106	0.000	0.000	0.000	0.000
61	A	61	LEU	0	0.018	0.018	3.325	-0.505	-0.243	0.019	-0.057	-0.224	0.000
62	A	62	MET	0	-0.007	0.006	4.069	0.019	0.304	0.000	-0.078	-0.207	0.000
63	A	63	SER	0	0.027	-0.014	2.425	-2.665	0.046	4.112	-2.948	-3.875	-0.032
64	A	64	ILE	0	0.031	0.058	3.458	-1.441	-1.290	0.024	0.050	-0.225	0.000
65	A	65	GLY	0	0.066	0.037	5.760	-0.102	-0.102	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.026	-0.023	5.442	0.272	0.272	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.013	0.005	5.025	-0.215	-0.215	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.867	-0.949	8.712	0.462	0.462	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.042	0.009	12.441	-0.048	-0.048	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.060	-0.019	15.461	-0.034	-0.034	0.000	0.000	0.000	0.000
71	A	71	ARG	1	0.960	0.986	8.632	-0.482	-0.482	0.000	0.000	0.000	0.000
72	A	72	ASN	0	0.042	0.014	10.652	0.008	0.008	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.949	0.985	12.489	-0.138	-0.138	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.844	-0.933	13.675	0.044	0.044	0.000	0.000	0.000	0.000
75	A	75	HIS	0	-0.014	-0.016	8.621	-0.120	-0.120	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.019	-0.011	11.027	-0.076	-0.076	0.000	0.000	0.000	0.000
77	A	77	ALA	0	-0.004	0.006	13.179	-0.038	-0.038	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.927	0.962	12.032	-0.035	-0.035	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.026	0.013	7.688	-0.037	-0.037	0.000	0.000	0.000	0.000
80	A	80	PHE	0	-0.028	-0.010	11.988	-0.044	-0.044	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.985	-0.988	15.366	-0.146	-0.146	0.000	0.000	0.000	0.000
82	A	82	HIS	0	0.009	0.004	11.888	0.039	0.039	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.008	-0.014	12.081	-0.020	-0.020	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.089	-0.045	15.506	0.012	0.012	0.000	0.000	0.000	0.000
85	A	85	THR	0	-0.008	-0.005	18.156	0.009	0.009	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.871	0.940	15.334	0.300	0.300	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.011	-0.007	15.406	-0.007	-0.007	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.036	0.035	19.442	0.015	0.015	0.000	0.000	0.000	0.000
89	A	89	ILE	0	-0.063	-0.021	18.283	0.020	0.020	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.013	0.010	20.885	0.002	0.002	0.000	0.000	0.000	0.000
91	A	91	LYS	1	1.016	0.995	19.220	0.084	0.084	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.039	-0.008	20.101	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.768	0.877	21.669	0.093	0.093	0.000	0.000	0.000	0.000
94	A	94	MET	0	0.010	0.007	16.453	-0.028	-0.028	0.000	0.000	0.000	0.000
95	A	95	TYR	0	-0.011	0.003	16.380	0.027	0.027	0.000	0.000	0.000	0.000
96	A	96	ILE	0	0.017	0.002	9.867	-0.045	-0.045	0.000	0.000	0.000	0.000
97	A	97	HIS	0	-0.026	-0.002	11.856	0.041	0.041	0.000	0.000	0.000	0.000
98	A	98	PHE	0	0.016	-0.004	7.971	-0.033	-0.033	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.017	0.000	7.795	-0.011	-0.011	0.000	0.000	0.000	0.000
100	A	100	ASN	0	-0.015	-0.010	6.972	0.447	0.447	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.002	-0.006	4.431	-0.223	-0.165	-0.001	-0.006	-0.051	0.000
102	A	102	ASN	0	0.053	0.027	8.343	0.149	0.149	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.001	-0.017	9.711	0.094	0.094	0.000	0.000	0.000	0.000
104	A	104	ASP	-1	-0.888	-0.954	10.728	0.588	0.588	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.937	-0.958	11.112	0.540	0.540	0.000	0.000	0.000	0.000
106	A	106	VAL	0	-0.074	-0.043	6.591	0.081	0.081	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.021	0.016	9.691	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	108	TRP	0	-0.008	-0.032	7.557	0.065	0.065	0.000	0.000	0.000	0.000
109	A	109	ASN	0	-0.027	-0.015	9.775	-0.043	-0.043	0.000	0.000	0.000	0.000
110	A	110	GLY	0	-0.004	0.002	12.429	0.001	0.001	0.000	0.000	0.000	0.000
111	A	111	THR	0	-0.007	0.010	13.018	-0.023	-0.023	0.000	0.000	0.000	0.000
112	A	112	THR	0	0.024	0.014	12.019	-0.009	-0.009	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.063	-0.014	6.773	0.070	0.070	0.000	0.000	0.000	0.000

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