FMO DATABASE

FMODB ID: LN6M9

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

Total energy (hartree)

FMO2-HF: Electronic energy	-595032.062316
FMO2-HF: Nuclear repulsion	560441.698792
FMO2-HF: Total energy	-34590.363525
FMO2-MP2: Total energy	-34693.68507

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.
-8.316	-3.168	2.786	-1.849	-6.085	-0.004

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 : -0.008 / q_NPA : -0.014

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	0.012	0.026	3.018	-1.301	1.134	0.020	-0.971	-1.484	0.002
4	A	8	LEU	0	0.019	0.003	4.716	0.277	0.325	-0.001	-0.006	-0.041	0.000
5	A	9	GLU	-1	-0.864	-0.942	7.979	-0.054	-0.054	0.000	0.000	0.000	0.000
6	A	10	ASP	-1	-0.864	-0.944	11.200	-0.233	-0.233	0.000	0.000	0.000	0.000
7	A	11	LYS	1	0.895	0.980	7.066	0.231	0.231	0.000	0.000	0.000	0.000
8	A	12	ILE	0	0.026	0.012	7.223	0.008	0.008	0.000	0.000	0.000	0.000
9	A	13	LEU	0	-0.063	-0.027	2.512	-1.598	-0.471	1.089	-0.370	-1.846	-0.003
10	A	14	VAL	0	0.026	0.011	5.647	0.073	0.073	0.000	0.000	0.000	0.000
11	A	15	GLN	0	0.011	0.003	7.756	-0.460	-0.460	0.000	0.000	0.000	0.000
12	A	16	ALA	0	0.002	-0.014	9.320	0.176	0.176	0.000	0.000	0.000	0.000
13	A	17	ASN	0	-0.043	-0.054	11.543	0.073	0.073	0.000	0.000	0.000	0.000
14	A	18	GLU	-1	-0.851	-0.915	13.517	-0.463	-0.463	0.000	0.000	0.000	0.000
15	A	19	ALA	0	-0.050	-0.020	15.831	0.028	0.028	0.000	0.000	0.000	0.000
16	A	20	GLU	-1	-0.903	-0.947	19.703	-0.281	-0.281	0.000	0.000	0.000	0.000
17	A	21	THR	0	-0.082	-0.057	22.815	0.021	0.021	0.000	0.000	0.000	0.000
18	A	22	THR	0	-0.063	-0.031	25.428	0.008	0.008	0.000	0.000	0.000	0.000
19	A	23	THR	0	0.058	0.042	20.298	-0.016	-0.016	0.000	0.000	0.000	0.000
20	A	24	ALA	0	-0.007	-0.010	20.459	0.025	0.025	0.000	0.000	0.000	0.000
21	A	25	SER	0	-0.019	0.019	22.150	0.021	0.021	0.000	0.000	0.000	0.000
22	A	26	GLY	0	-0.045	-0.021	23.793	0.020	0.020	0.000	0.000	0.000	0.000
23	A	27	LEU	0	-0.048	-0.015	23.862	0.020	0.020	0.000	0.000	0.000	0.000
24	A	28	VAL	0	0.017	-0.007	25.464	-0.012	-0.012	0.000	0.000	0.000	0.000
25	A	29	ILE	0	0.032	0.006	21.370	0.013	0.013	0.000	0.000	0.000	0.000
26	A	30	PRO	0	0.020	0.023	24.999	-0.006	-0.006	0.000	0.000	0.000	0.000
27	A	31	ASP	-1	-0.803	-0.915	22.414	-0.271	-0.271	0.000	0.000	0.000	0.000
28	A	32	THR	0	0.013	-0.012	24.008	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	33	ALA	0	-0.027	0.014	25.062	0.013	0.013	0.000	0.000	0.000	0.000
30	A	34	LYS	1	0.834	0.909	21.850	0.238	0.238	0.000	0.000	0.000	0.000
31	A	35	GLU	-1	-0.825	-0.904	21.646	-0.247	-0.247	0.000	0.000	0.000	0.000
32	A	36	LYS	1	0.817	0.901	18.476	0.241	0.241	0.000	0.000	0.000	0.000
33	A	37	PRO	0	-0.093	-0.010	18.305	-0.037	-0.037	0.000	0.000	0.000	0.000
34	A	38	GLN	0	0.065	0.070	13.693	-0.011	-0.011	0.000	0.000	0.000	0.000
35	A	39	GLU	-1	-0.847	-0.961	17.550	-0.355	-0.355	0.000	0.000	0.000	0.000
36	A	40	GLY	0	0.022	0.008	13.902	-0.037	-0.037	0.000	0.000	0.000	0.000
37	A	41	THR	0	-0.021	0.009	12.230	0.097	0.097	0.000	0.000	0.000	0.000
38	A	42	VAL	0	0.002	-0.004	9.951	-0.229	-0.229	0.000	0.000	0.000	0.000
39	A	43	VAL	0	0.004	0.014	5.789	0.085	0.085	0.000	0.000	0.000	0.000
40	A	44	ALA	0	-0.003	0.002	4.591	-0.212	-0.135	-0.001	-0.012	-0.063	0.000
41	A	45	VAL	0	0.050	0.023	6.741	0.004	0.004	0.000	0.000	0.000	0.000
42	A	46	GLY	0	0.008	0.022	8.421	0.104	0.104	0.000	0.000	0.000	0.000
43	A	47	PRO	0	-0.084	-0.061	9.026	0.045	0.045	0.000	0.000	0.000	0.000
44	A	48	GLY	0	0.070	0.047	12.416	-0.015	-0.015	0.000	0.000	0.000	0.000
45	A	49	ARG	1	0.849	0.928	14.144	0.114	0.114	0.000	0.000	0.000	0.000
46	A	50	TRP	0	-0.013	-0.010	16.558	0.004	0.004	0.000	0.000	0.000	0.000
47	A	51	ASP	-1	-0.804	-0.886	19.200	-0.022	-0.022	0.000	0.000	0.000	0.000
48	A	52	GLU	-1	-0.911	-0.964	22.606	-0.011	-0.011	0.000	0.000	0.000	0.000
49	A	53	ASP	-1	-0.934	-0.966	24.546	0.026	0.026	0.000	0.000	0.000	0.000
50	A	54	GLY	0	-0.060	-0.027	22.552	0.011	0.011	0.000	0.000	0.000	0.000
51	A	55	GLU	-1	-0.942	-0.946	23.247	0.043	0.043	0.000	0.000	0.000	0.000
52	A	56	LYS	1	0.805	0.867	21.937	0.009	0.009	0.000	0.000	0.000	0.000
53	A	57	ARG	1	0.823	0.895	14.844	-0.139	-0.139	0.000	0.000	0.000	0.000
54	A	58	ILE	0	-0.008	-0.001	18.679	0.001	0.001	0.000	0.000	0.000	0.000
55	A	59	PRO	0	-0.028	-0.021	16.515	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	60	LEU	0	-0.029	-0.007	11.579	-0.012	-0.012	0.000	0.000	0.000	0.000
57	A	61	ASP	-1	-0.946	-0.965	15.701	-0.178	-0.178	0.000	0.000	0.000	0.000
58	A	62	VAL	0	0.002	0.008	12.718	-0.015	-0.015	0.000	0.000	0.000	0.000
59	A	63	ALA	0	-0.069	-0.047	13.194	0.020	0.020	0.000	0.000	0.000	0.000
60	A	64	GLU	-1	-0.915	-0.977	9.080	-0.571	-0.571	0.000	0.000	0.000	0.000
61	A	65	GLY	0	-0.064	-0.026	12.146	0.102	0.102	0.000	0.000	0.000	0.000
62	A	66	ASP	-1	-0.828	-0.905	14.169	-0.337	-0.337	0.000	0.000	0.000	0.000
63	A	67	THR	0	-0.044	-0.013	14.675	-0.100	-0.100	0.000	0.000	0.000	0.000
64	A	68	VAL	0	0.012	-0.016	13.489	0.055	0.055	0.000	0.000	0.000	0.000
65	A	69	ILE	0	0.005	0.005	16.636	-0.031	-0.031	0.000	0.000	0.000	0.000
66	A	70	TYR	0	-0.025	-0.023	13.090	-0.018	-0.018	0.000	0.000	0.000	0.000
67	A	71	SER	0	0.031	0.028	16.935	0.026	0.026	0.000	0.000	0.000	0.000
68	A	72	LYS	1	0.831	0.896	13.523	0.561	0.561	0.000	0.000	0.000	0.000
69	A	73	TYR	0	-0.025	-0.032	14.734	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	74	GLY	0	-0.042	-0.008	14.762	-0.014	-0.014	0.000	0.000	0.000	0.000
71	A	75	GLY	0	0.017	0.018	11.111	-0.022	-0.022	0.000	0.000	0.000	0.000
72	A	76	THR	0	-0.059	-0.033	7.684	0.121	0.121	0.000	0.000	0.000	0.000
73	A	77	GLU	-1	-0.855	-0.925	7.370	-1.038	-1.038	0.000	0.000	0.000	0.000
74	A	78	ILE	0	-0.013	-0.008	2.283	-0.470	-0.192	1.371	-0.280	-1.369	-0.003
75	A	79	LYS	1	0.812	0.896	5.868	0.498	0.498	0.000	0.000	0.000	0.000
76	A	80	TYR	0	-0.055	-0.034	3.639	-0.413	0.033	0.006	-0.065	-0.388	0.000
77	A	81	ASN	0	-0.046	-0.040	5.765	0.004	0.004	0.000	0.000	0.000	0.000
78	A	82	GLY	0	-0.003	-0.006	8.981	0.035	0.035	0.000	0.000	0.000	0.000
79	A	83	GLU	-1	-0.819	-0.870	7.733	-0.812	-0.812	0.000	0.000	0.000	0.000
80	A	84	GLU	-1	-0.863	-0.922	7.956	-0.856	-0.856	0.000	0.000	0.000	0.000
81	A	85	TYR	0	-0.058	-0.043	4.386	-0.471	-0.239	-0.001	-0.014	-0.217	0.000
82	A	86	LEU	0	0.034	0.011	6.448	0.227	0.227	0.000	0.000	0.000	0.000
83	A	87	ILE	0	-0.039	-0.004	2.652	-0.690	-0.185	0.303	-0.131	-0.677	0.000
84	A	88	LEU	0	-0.003	0.003	6.349	0.225	0.225	0.000	0.000	0.000	0.000
85	A	89	SER	0	-0.059	-0.056	9.517	-0.015	-0.015	0.000	0.000	0.000	0.000
86	A	90	ALA	0	0.098	0.044	11.843	-0.008	-0.008	0.000	0.000	0.000	0.000
87	A	91	ARG	1	0.801	0.883	13.558	0.216	0.216	0.000	0.000	0.000	0.000
88	A	92	ASP	-1	-0.856	-0.903	13.983	-0.388	-0.388	0.000	0.000	0.000	0.000
89	A	93	VAL	0	-0.007	-0.012	13.251	-0.012	-0.012	0.000	0.000	0.000	0.000
90	A	94	LEU	0	-0.042	-0.027	16.030	0.050	0.050	0.000	0.000	0.000	0.000
91	A	95	ALA	0	-0.012	-0.002	19.188	0.036	0.036	0.000	0.000	0.000	0.000
92	A	96	VAL	0	0.039	0.027	17.563	-0.043	-0.043	0.000	0.000	0.000	0.000
93	A	97	VAL	0	-0.059	-0.023	19.923	0.028	0.028	0.000	0.000	0.000	0.000

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