FMO DATABASE

FMODB ID: 3J43L

Calculation Name: 1HX5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1HX5

Chain ID: A

ChEMBL ID:

UniProt ID: P9WPE5

Base Structure: X-ray

Registration Date: 2023-09-23

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	93
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-594773.709924
FMO2-HF: Nuclear repulsion	560184.511014
FMO2-HF: Total energy	-34589.19891
FMO2-MP2: Total energy	-34692.611804

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:5:ILE)

Summations of interaction energy for fragment #1(A:5:ILE)

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.
-6.525	-4.461	6.932	-2.271	-6.722	-0.001

Interaction energy analysis for fragmet #1(A:5:ILE)

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 : -0.004

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

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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	7	PRO	0	0.011	0.023	3.098	-1.337	1.173	0.034	-0.983	-1.560	0.003
4	A	8	LEU	0	0.007	-0.005	4.483	0.309	0.371	-0.001	-0.008	-0.052	0.000
5	A	9	GLU	-1	-0.980	-1.015	7.767	-0.170	-0.170	0.000	0.000	0.000	0.000
6	A	10	ASP	-1	-0.855	-0.958	10.970	-0.319	-0.319	0.000	0.000	0.000	0.000
7	A	11	LYS	1	0.921	1.003	6.930	0.380	0.380	0.000	0.000	0.000	0.000
8	A	12	ILE	0	0.029	0.006	7.059	-0.016	-0.016	0.000	0.000	0.000	0.000
9	A	13	LEU	0	-0.073	-0.032	2.423	-1.764	-0.640	1.589	-0.479	-2.233	-0.004
10	A	14	VAL	0	0.043	0.014	5.583	0.090	0.090	0.000	0.000	0.000	0.000
11	A	15	GLN	0	-0.054	-0.053	7.524	-0.369	-0.369	0.000	0.000	0.000	0.000
12	A	16	ALA	0	-0.016	-0.005	9.149	0.159	0.159	0.000	0.000	0.000	0.000
13	A	17	ASN	0	-0.072	-0.063	11.535	0.073	0.073	0.000	0.000	0.000	0.000
14	A	18	GLU	-1	-0.816	-0.896	13.570	-0.432	-0.432	0.000	0.000	0.000	0.000
15	A	19	ALA	0	-0.050	-0.020	15.744	0.028	0.028	0.000	0.000	0.000	0.000
16	A	20	GLU	-1	-0.909	-0.947	19.625	-0.270	-0.270	0.000	0.000	0.000	0.000
17	A	21	THR	0	-0.092	-0.064	22.815	0.018	0.018	0.000	0.000	0.000	0.000
18	A	22	THR	0	-0.049	-0.023	25.223	0.007	0.007	0.000	0.000	0.000	0.000
19	A	23	THR	0	0.066	0.048	20.724	-0.014	-0.014	0.000	0.000	0.000	0.000
20	A	24	ALA	0	-0.027	-0.019	20.455	0.024	0.024	0.000	0.000	0.000	0.000
21	A	25	SER	0	-0.015	0.014	21.929	0.021	0.021	0.000	0.000	0.000	0.000
22	A	26	GLY	0	-0.064	-0.031	23.615	0.021	0.021	0.000	0.000	0.000	0.000
23	A	27	LEU	0	-0.041	-0.017	23.555	0.020	0.020	0.000	0.000	0.000	0.000
24	A	28	VAL	0	0.025	0.001	25.276	-0.012	-0.012	0.000	0.000	0.000	0.000
25	A	29	ILE	0	0.062	0.015	21.079	0.014	0.014	0.000	0.000	0.000	0.000
26	A	30	PRO	0	0.012	0.022	24.807	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	31	ASP	-1	-0.827	-0.926	22.188	-0.271	-0.271	0.000	0.000	0.000	0.000
28	A	32	THR	0	-0.004	-0.024	24.130	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	33	ALA	0	-0.023	0.015	25.409	0.015	0.015	0.000	0.000	0.000	0.000
30	A	34	LYS	1	0.848	0.920	21.744	0.255	0.255	0.000	0.000	0.000	0.000
31	A	35	GLU	-1	-0.867	-0.951	21.881	-0.238	-0.238	0.000	0.000	0.000	0.000
32	A	36	LYS	1	0.834	0.911	18.543	0.239	0.239	0.000	0.000	0.000	0.000
33	A	37	PRO	0	-0.087	-0.004	18.552	-0.036	-0.036	0.000	0.000	0.000	0.000
34	A	38	GLN	0	0.074	0.047	13.405	0.019	0.019	0.000	0.000	0.000	0.000
35	A	39	GLU	-1	-0.857	-0.957	17.456	-0.383	-0.383	0.000	0.000	0.000	0.000
36	A	40	GLY	0	0.021	0.011	13.685	-0.031	-0.031	0.000	0.000	0.000	0.000
37	A	41	THR	0	-0.004	0.015	11.636	0.097	0.097	0.000	0.000	0.000	0.000
38	A	42	VAL	0	-0.001	-0.004	9.819	-0.244	-0.244	0.000	0.000	0.000	0.000
39	A	43	VAL	0	0.008	0.018	5.590	0.084	0.084	0.000	0.000	0.000	0.000
40	A	44	ALA	0	0.002	-0.005	4.590	-0.275	-0.194	-0.001	-0.010	-0.069	0.000
41	A	45	VAL	0	0.075	0.033	6.601	0.019	0.019	0.000	0.000	0.000	0.000
42	A	46	GLY	0	-0.025	0.014	8.190	0.081	0.081	0.000	0.000	0.000	0.000
43	A	47	PRO	0	-0.096	-0.066	8.779	0.067	0.067	0.000	0.000	0.000	0.000
44	A	48	GLY	0	0.073	0.047	12.152	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	49	ARG	1	0.910	0.962	13.903	0.192	0.192	0.000	0.000	0.000	0.000
46	A	50	TRP	0	-0.028	-0.007	16.331	0.004	0.004	0.000	0.000	0.000	0.000
47	A	51	ASP	-1	-0.880	-0.939	18.967	-0.054	-0.054	0.000	0.000	0.000	0.000
48	A	52	GLU	-1	-0.958	-0.995	22.412	-0.027	-0.027	0.000	0.000	0.000	0.000
49	A	53	ASP	-1	-0.948	-0.969	24.328	0.009	0.009	0.000	0.000	0.000	0.000
50	A	54	GLY	0	-0.061	-0.033	22.324	0.013	0.013	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.966	-0.970	23.013	0.014	0.014	0.000	0.000	0.000	0.000
52	A	56	LYS	1	0.899	0.939	21.704	0.036	0.036	0.000	0.000	0.000	0.000
53	A	57	ARG	1	0.917	0.960	14.329	-0.068	-0.068	0.000	0.000	0.000	0.000
54	A	58	ILE	0	-0.011	-0.002	18.362	0.001	0.001	0.000	0.000	0.000	0.000
55	A	59	PRO	0	-0.039	-0.027	16.265	-0.023	-0.023	0.000	0.000	0.000	0.000
56	A	60	LEU	0	-0.012	0.001	11.168	-0.007	-0.007	0.000	0.000	0.000	0.000
57	A	61	ASP	-1	-0.940	-0.961	15.482	-0.224	-0.224	0.000	0.000	0.000	0.000
58	A	62	VAL	0	-0.009	0.006	12.460	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	63	ALA	0	-0.073	-0.061	13.017	0.013	0.013	0.000	0.000	0.000	0.000
60	A	64	GLU	-1	-0.918	-0.981	9.371	-0.731	-0.731	0.000	0.000	0.000	0.000
61	A	65	GLY	0	-0.071	-0.027	12.044	0.115	0.115	0.000	0.000	0.000	0.000
62	A	66	ASP	-1	-0.830	-0.902	14.075	-0.397	-0.397	0.000	0.000	0.000	0.000
63	A	67	THR	0	-0.047	-0.007	14.609	-0.104	-0.104	0.000	0.000	0.000	0.000
64	A	68	VAL	0	0.008	-0.017	13.619	0.056	0.056	0.000	0.000	0.000	0.000
65	A	69	ILE	0	0.009	0.011	16.604	-0.026	-0.026	0.000	0.000	0.000	0.000
66	A	70	TYR	0	-0.006	-0.018	13.008	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	71	SER	0	-0.006	0.011	16.795	0.037	0.037	0.000	0.000	0.000	0.000
68	A	72	LYS	1	0.869	0.913	14.251	0.469	0.469	0.000	0.000	0.000	0.000
69	A	73	TYR	0	-0.011	-0.005	14.649	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	74	GLY	0	-0.044	-0.008	14.591	-0.018	-0.018	0.000	0.000	0.000	0.000
71	A	75	GLY	0	0.021	0.019	10.972	-0.029	-0.029	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.063	-0.035	7.602	0.139	0.139	0.000	0.000	0.000	0.000
73	A	77	GLU	-1	-0.881	-0.955	7.340	-0.917	-0.917	0.000	0.000	0.000	0.000
74	A	78	ILE	0	-0.055	-0.027	2.113	1.416	-1.341	5.259	-0.652	-1.850	0.000
75	A	79	LYS	1	0.948	0.984	5.881	0.373	0.373	0.000	0.000	0.000	0.000
76	A	80	TYR	0	-0.036	-0.026	3.811	-0.209	0.105	0.001	-0.026	-0.289	0.000
77	A	81	ASN	0	-0.049	-0.036	5.914	-0.029	-0.029	0.000	0.000	0.000	0.000
78	A	82	GLY	0	-0.004	-0.006	9.200	0.017	0.017	0.000	0.000	0.000	0.000
79	A	83	GLU	-1	-0.821	-0.856	7.623	-0.750	-0.750	0.000	0.000	0.000	0.000
80	A	84	GLU	-1	-0.943	-0.979	7.965	-0.801	-0.801	0.000	0.000	0.000	0.000
81	A	85	TYR	0	-0.024	-0.015	4.340	-0.454	-0.193	0.000	-0.027	-0.234	0.000
82	A	86	LEU	0	0.056	0.027	6.322	0.214	0.214	0.000	0.000	0.000	0.000
83	A	87	ILE	0	-0.047	-0.007	3.143	-0.695	-0.226	0.051	-0.086	-0.435	0.000
84	A	88	LEU	0	-0.008	0.001	6.190	0.252	0.252	0.000	0.000	0.000	0.000
85	A	89	SER	0	0.014	-0.004	9.401	-0.042	-0.042	0.000	0.000	0.000	0.000
86	A	90	ALA	0	0.100	0.050	11.714	-0.003	-0.003	0.000	0.000	0.000	0.000
87	A	91	ARG	1	0.807	0.892	13.397	0.259	0.259	0.000	0.000	0.000	0.000
88	A	92	ASP	-1	-0.848	-0.916	13.892	-0.443	-0.443	0.000	0.000	0.000	0.000
89	A	93	VAL	0	-0.036	-0.026	13.208	-0.007	-0.007	0.000	0.000	0.000	0.000
90	A	94	LEU	0	-0.038	-0.032	15.923	0.053	0.053	0.000	0.000	0.000	0.000
91	A	95	ALA	0	-0.016	-0.001	19.088	0.038	0.038	0.000	0.000	0.000	0.000
92	A	96	VAL	0	0.043	0.029	17.479	-0.046	-0.046	0.000	0.000	0.000	0.000
93	A	97	VAL	0	-0.046	-0.019	19.825	0.033	0.033	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ILE)