FMO DATABASE

FMODB ID: LNL79

Calculation Name: 3HX1-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3HX1

Chain ID: A

ChEMBL ID:

UniProt ID: P74513

Base Structure: X-ray

Registration Date: 2023-09-20

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	109
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-884243.248041
FMO2-HF: Nuclear repulsion	840934.475589
FMO2-HF: Total energy	-43308.772452
FMO2-MP2: Total energy	-43436.521807

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:9:LEU)

Summations of interaction energy for fragment #1(A:9:LEU)

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.
-7.198	-3.801	1.678	-1.999	-3.078	-0.002

Interaction energy analysis for fragmet #1(A:9:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.023 / q_NPA : -0.020

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	11	GLU	-1	-0.849	-0.920	3.802	-3.344	-1.818	-0.014	-0.604	-0.909	0.003
4	A	12	HIS	0	0.050	0.035	6.267	0.526	0.526	0.000	0.000	0.000	0.000
5	A	13	ILE	0	-0.010	0.011	9.817	-0.036	-0.036	0.000	0.000	0.000	0.000
6	A	14	LEU	0	0.024	0.001	12.450	0.072	0.072	0.000	0.000	0.000	0.000
7	A	15	ILE	0	-0.031	-0.017	15.382	-0.009	-0.009	0.000	0.000	0.000	0.000
8	A	16	ILE	0	0.003	0.001	18.565	0.017	0.017	0.000	0.000	0.000	0.000
9	A	17	LEU	0	-0.008	0.003	21.880	0.001	0.001	0.000	0.000	0.000	0.000
10	A	18	ASP	-1	-0.713	-0.859	25.231	-0.064	-0.064	0.000	0.000	0.000	0.000
11	A	19	ASP	-1	-0.805	-0.912	28.338	-0.034	-0.034	0.000	0.000	0.000	0.000
12	A	20	ALA	0	-0.138	-0.068	27.393	0.002	0.002	0.000	0.000	0.000	0.000
13	A	21	GLY	0	-0.001	0.012	27.303	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	22	ARG	1	0.938	0.955	21.541	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	23	ARG	1	0.833	0.899	20.774	0.098	0.098	0.000	0.000	0.000	0.000
16	A	24	GLU	-1	-0.817	-0.878	14.607	-0.084	-0.084	0.000	0.000	0.000	0.000
17	A	25	VAL	0	-0.001	0.002	15.820	-0.012	-0.012	0.000	0.000	0.000	0.000
18	A	26	LEU	0	0.017	0.023	8.356	0.015	0.015	0.000	0.000	0.000	0.000
19	A	27	LEU	0	-0.058	-0.039	11.712	0.027	0.027	0.000	0.000	0.000	0.000
20	A	28	THR	0	0.012	-0.006	10.539	-0.132	-0.132	0.000	0.000	0.000	0.000
21	A	29	GLU	-1	-0.862	-0.933	11.709	-0.395	-0.395	0.000	0.000	0.000	0.000
22	A	30	THR	0	-0.004	0.003	14.516	-0.021	-0.021	0.000	0.000	0.000	0.000
23	A	31	PHE	0	0.040	0.024	16.460	0.026	0.026	0.000	0.000	0.000	0.000
24	A	32	TYR	0	0.030	0.035	14.769	-0.037	-0.037	0.000	0.000	0.000	0.000
25	A	33	THR	0	0.035	0.005	20.467	0.019	0.019	0.000	0.000	0.000	0.000
26	A	34	ILE	0	0.012	-0.006	20.718	-0.007	-0.007	0.000	0.000	0.000	0.000
27	A	35	GLY	0	0.058	0.018	24.722	0.011	0.011	0.000	0.000	0.000	0.000
28	A	36	ARG	1	0.877	0.973	27.602	0.036	0.036	0.000	0.000	0.000	0.000
29	A	37	SER	0	-0.086	-0.037	30.297	0.000	0.000	0.000	0.000	0.000	0.000
30	A	38	PRO	0	-0.030	-0.044	29.014	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	39	ARG	1	0.961	0.987	28.421	0.068	0.068	0.000	0.000	0.000	0.000
32	A	40	ALA	0	0.016	0.025	25.848	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	41	ASP	-1	-0.811	-0.853	21.052	-0.159	-0.159	0.000	0.000	0.000	0.000
34	A	42	ILE	0	-0.013	-0.003	18.118	-0.008	-0.008	0.000	0.000	0.000	0.000
35	A	43	ARG	1	0.877	0.929	22.264	0.101	0.101	0.000	0.000	0.000	0.000
36	A	44	ILE	0	0.017	0.011	22.921	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	45	LYS	1	0.829	0.915	26.655	0.054	0.054	0.000	0.000	0.000	0.000
38	A	46	SER	0	0.081	0.021	29.782	0.006	0.006	0.000	0.000	0.000	0.000
39	A	47	GLN	0	-0.047	-0.019	32.599	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	48	PHE	0	-0.013	-0.017	33.787	0.001	0.001	0.000	0.000	0.000	0.000
41	A	49	VAL	0	0.017	0.029	28.868	0.001	0.001	0.000	0.000	0.000	0.000
42	A	50	SER	0	0.055	0.032	32.149	0.000	0.000	0.000	0.000	0.000	0.000
43	A	51	ARG	1	0.893	0.928	31.301	0.045	0.045	0.000	0.000	0.000	0.000
44	A	52	ILE	0	0.031	0.006	27.878	-0.005	-0.005	0.000	0.000	0.000	0.000
45	A	53	HIS	0	0.008	-0.013	28.019	0.000	0.000	0.000	0.000	0.000	0.000
46	A	54	ALA	0	0.023	0.035	25.415	0.007	0.007	0.000	0.000	0.000	0.000
47	A	55	VAL	0	0.025	0.019	23.562	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	56	LEU	0	-0.029	-0.008	17.489	0.011	0.011	0.000	0.000	0.000	0.000
49	A	57	VAL	0	0.022	0.007	19.182	-0.018	-0.018	0.000	0.000	0.000	0.000
50	A	58	ARG	1	0.829	0.910	11.044	0.453	0.453	0.000	0.000	0.000	0.000
51	A	59	LYS	1	0.820	0.904	16.083	0.045	0.045	0.000	0.000	0.000	0.000
52	A	60	SER	0	0.013	0.005	15.681	-0.027	-0.027	0.000	0.000	0.000	0.000
53	A	61	SER	0	-0.001	-0.010	12.873	-0.034	-0.034	0.000	0.000	0.000	0.000
54	A	62	ASP	-1	-0.839	-0.925	13.930	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	63	ASP	-1	-0.855	-0.924	13.764	0.152	0.152	0.000	0.000	0.000	0.000
56	A	64	VAL	0	-0.031	-0.006	8.115	0.089	0.089	0.000	0.000	0.000	0.000
57	A	65	GLN	0	-0.046	-0.017	6.926	-0.219	-0.219	0.000	0.000	0.000	0.000
58	A	66	ALA	0	-0.023	0.004	10.110	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	67	ALA	0	0.015	0.001	11.635	-0.086	-0.086	0.000	0.000	0.000	0.000
60	A	68	TYR	0	-0.037	-0.046	11.766	-0.031	-0.031	0.000	0.000	0.000	0.000
61	A	69	ARG	1	0.811	0.911	16.269	0.058	0.058	0.000	0.000	0.000	0.000
62	A	70	ILE	0	-0.030	-0.013	20.012	-0.018	-0.018	0.000	0.000	0.000	0.000
63	A	71	ILE	0	-0.010	-0.007	22.384	0.014	0.014	0.000	0.000	0.000	0.000
64	A	72	ASP	-1	-0.900	-0.968	25.902	-0.036	-0.036	0.000	0.000	0.000	0.000
65	A	73	GLY	0	0.056	0.016	28.816	0.001	0.001	0.000	0.000	0.000	0.000
66	A	74	ASP	-1	-0.957	-0.990	28.853	-0.062	-0.062	0.000	0.000	0.000	0.000
67	A	75	GLU	-1	-0.913	-0.982	27.297	-0.099	-0.099	0.000	0.000	0.000	0.000
68	A	76	ASP	-1	-0.989	-0.977	29.723	-0.057	-0.057	0.000	0.000	0.000	0.000
69	A	77	GLY	0	-0.041	-0.008	31.938	0.004	0.004	0.000	0.000	0.000	0.000
70	A	78	GLN	0	-0.070	-0.024	32.905	0.009	0.009	0.000	0.000	0.000	0.000
71	A	79	SER	0	0.033	0.024	33.068	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	80	SER	0	-0.039	-0.023	32.770	0.000	0.000	0.000	0.000	0.000	0.000
73	A	81	VAL	0	-0.005	-0.009	34.974	0.003	0.003	0.000	0.000	0.000	0.000
74	A	82	ASN	0	-0.021	-0.007	34.097	0.006	0.006	0.000	0.000	0.000	0.000
75	A	83	GLY	0	0.094	0.065	31.895	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	84	LEU	0	0.022	0.012	25.600	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	85	MET	0	-0.009	0.014	28.961	0.005	0.005	0.000	0.000	0.000	0.000
78	A	86	ILE	0	0.060	0.033	23.644	0.000	0.000	0.000	0.000	0.000	0.000
79	A	87	ASN	0	0.012	-0.002	24.956	0.002	0.002	0.000	0.000	0.000	0.000
80	A	88	GLY	0	-0.012	-0.009	28.738	0.001	0.001	0.000	0.000	0.000	0.000
81	A	89	LYS	1	0.941	0.971	30.824	-0.044	-0.044	0.000	0.000	0.000	0.000
82	A	90	LYS	1	0.835	0.891	30.415	0.000	0.000	0.000	0.000	0.000	0.000
83	A	91	VAL	0	-0.014	0.008	26.583	0.003	0.003	0.000	0.000	0.000	0.000
84	A	92	GLN	0	-0.013	-0.002	29.898	-0.006	-0.006	0.000	0.000	0.000	0.000
85	A	93	GLU	-1	-0.782	-0.904	25.302	-0.034	-0.034	0.000	0.000	0.000	0.000
86	A	94	HIS	0	-0.062	-0.047	21.134	0.004	0.004	0.000	0.000	0.000	0.000
87	A	95	ILE	0	-0.026	-0.010	17.744	-0.018	-0.018	0.000	0.000	0.000	0.000
88	A	96	ILE	0	0.005	0.004	16.968	0.024	0.024	0.000	0.000	0.000	0.000
89	A	97	GLN	0	-0.014	-0.003	15.945	0.029	0.029	0.000	0.000	0.000	0.000
90	A	98	THR	0	-0.008	-0.018	12.430	-0.022	-0.022	0.000	0.000	0.000	0.000
91	A	99	GLY	0	-0.040	-0.024	14.816	0.038	0.038	0.000	0.000	0.000	0.000
92	A	100	ASP	-1	-0.812	-0.876	17.818	0.060	0.060	0.000	0.000	0.000	0.000
93	A	101	GLU	-1	-0.897	-0.947	19.965	0.013	0.013	0.000	0.000	0.000	0.000
94	A	102	ILE	0	-0.027	-0.013	20.809	0.002	0.002	0.000	0.000	0.000	0.000
95	A	103	VAL	0	0.009	0.010	24.481	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	104	MET	0	-0.011	-0.008	26.358	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	105	GLY	0	0.020	-0.001	29.210	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	106	PRO	0	-0.065	-0.041	31.802	0.003	0.003	0.000	0.000	0.000	0.000
99	A	107	GLN	0	0.002	0.002	31.810	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	108	VAL	0	-0.028	0.001	27.716	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	109	SER	0	-0.075	-0.051	25.312	0.001	0.001	0.000	0.000	0.000	0.000
102	A	110	VAL	0	0.012	0.010	20.605	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	111	ARG	1	0.885	0.928	17.065	-0.076	-0.076	0.000	0.000	0.000	0.000
104	A	112	TYR	0	-0.033	-0.025	11.201	0.010	0.010	0.000	0.000	0.000	0.000
105	A	113	GLU	-1	-0.784	-0.872	12.457	0.168	0.168	0.000	0.000	0.000	0.000
106	A	114	TYR	0	-0.012	-0.003	6.152	-0.136	-0.136	0.000	0.000	0.000	0.000
107	A	115	ARG	1	0.812	0.863	8.116	0.387	0.387	0.000	0.000	0.000	0.000
108	A	116	ARG	1	0.904	0.966	3.751	-4.773	-4.248	0.018	-0.256	-0.287	0.002
109	A	117	ARG	1	0.886	0.949	2.127	0.291	1.637	1.674	-1.139	-1.882	-0.007

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:LEU)