FMO DATABASE

FMODB ID: 98YM2

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

Total energy (hartree)

FMO2-HF: Electronic energy	-883895.440331
FMO2-HF: Nuclear repulsion	840586.0856
FMO2-HF: Total energy	-43309.354731
FMO2-MP2: Total energy	-43437.087397

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.
-5.627	-2.22	0.352	-1.562	-2.196	0.003

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 : 0.012 / q_NPA : -0.005

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	-0.848	-0.911	3.864	-3.169	-1.564	-0.014	-0.758	-0.832	0.003
4	A	12	HIS	0	0.059	0.037	6.520	0.422	0.422	0.000	0.000	0.000	0.000
5	A	13	ILE	0	-0.016	0.004	10.138	-0.024	-0.024	0.000	0.000	0.000	0.000
6	A	14	LEU	0	0.028	0.011	12.684	0.066	0.066	0.000	0.000	0.000	0.000
7	A	15	ILE	0	-0.031	-0.013	15.730	-0.018	-0.018	0.000	0.000	0.000	0.000
8	A	16	ILE	0	-0.006	-0.007	18.777	0.012	0.012	0.000	0.000	0.000	0.000
9	A	17	LEU	0	-0.006	-0.007	22.247	0.000	0.000	0.000	0.000	0.000	0.000
10	A	18	ASP	-1	-0.678	-0.837	25.728	-0.047	-0.047	0.000	0.000	0.000	0.000
11	A	19	ASP	-1	-0.810	-0.888	28.678	-0.023	-0.023	0.000	0.000	0.000	0.000
12	A	20	ALA	0	-0.092	-0.037	27.670	-0.001	-0.001	0.000	0.000	0.000	0.000
13	A	21	GLY	0	-0.002	0.016	27.733	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	22	ARG	1	0.935	0.962	22.431	-0.007	-0.007	0.000	0.000	0.000	0.000
15	A	23	ARG	1	0.805	0.882	21.212	0.073	0.073	0.000	0.000	0.000	0.000
16	A	24	GLU	-1	-0.802	-0.877	15.504	-0.059	-0.059	0.000	0.000	0.000	0.000
17	A	25	VAL	0	0.003	-0.001	15.949	-0.012	-0.012	0.000	0.000	0.000	0.000
18	A	26	LEU	0	0.008	0.017	8.532	0.017	0.017	0.000	0.000	0.000	0.000
19	A	27	LEU	0	-0.033	-0.012	12.598	0.000	0.000	0.000	0.000	0.000	0.000
20	A	28	THR	0	-0.001	-0.011	10.597	-0.098	-0.098	0.000	0.000	0.000	0.000
21	A	29	GLU	-1	-0.839	-0.929	11.944	-0.310	-0.310	0.000	0.000	0.000	0.000
22	A	30	THR	0	-0.023	0.004	14.971	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	31	PHE	0	0.015	0.010	16.421	0.029	0.029	0.000	0.000	0.000	0.000
24	A	32	TYR	0	0.033	0.038	15.175	-0.034	-0.034	0.000	0.000	0.000	0.000
25	A	33	THR	0	0.025	-0.006	20.799	0.018	0.018	0.000	0.000	0.000	0.000
26	A	34	ILE	0	0.025	0.009	21.453	-0.008	-0.008	0.000	0.000	0.000	0.000
27	A	35	GLY	0	0.045	0.013	25.057	0.009	0.009	0.000	0.000	0.000	0.000
28	A	36	ARG	1	0.881	0.947	28.123	0.023	0.023	0.000	0.000	0.000	0.000
29	A	37	SER	0	-0.044	-0.011	30.802	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	38	PRO	0	-0.045	-0.047	29.594	-0.004	-0.004	0.000	0.000	0.000	0.000
31	A	39	ARG	1	0.844	0.903	29.101	0.057	0.057	0.000	0.000	0.000	0.000
32	A	40	ALA	0	-0.003	0.025	26.121	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	41	ASP	-1	-0.813	-0.873	21.306	-0.126	-0.126	0.000	0.000	0.000	0.000
34	A	42	ILE	0	-0.019	-0.006	18.253	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	43	ARG	1	0.876	0.930	22.344	0.087	0.087	0.000	0.000	0.000	0.000
36	A	44	ILE	0	0.017	0.019	23.236	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	45	LYS	1	0.825	0.901	26.951	0.042	0.042	0.000	0.000	0.000	0.000
38	A	46	SER	0	0.038	-0.020	30.163	0.005	0.005	0.000	0.000	0.000	0.000
39	A	47	GLN	0	-0.028	-0.011	32.653	0.000	0.000	0.000	0.000	0.000	0.000
40	A	48	PHE	0	-0.016	-0.013	34.027	0.001	0.001	0.000	0.000	0.000	0.000
41	A	49	VAL	0	0.002	0.025	29.025	0.002	0.002	0.000	0.000	0.000	0.000
42	A	50	SER	0	0.044	0.010	32.403	-0.002	-0.002	0.000	0.000	0.000	0.000
43	A	51	ARG	1	0.896	0.936	31.688	0.032	0.032	0.000	0.000	0.000	0.000
44	A	52	ILE	0	0.042	0.017	27.987	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	53	HIS	0	-0.008	0.006	28.828	0.001	0.001	0.000	0.000	0.000	0.000
46	A	54	ALA	0	0.024	0.022	25.505	0.007	0.007	0.000	0.000	0.000	0.000
47	A	55	VAL	0	0.022	0.025	23.999	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	56	LEU	0	-0.028	-0.018	17.897	0.012	0.012	0.000	0.000	0.000	0.000
49	A	57	VAL	0	0.024	0.004	19.392	-0.013	-0.013	0.000	0.000	0.000	0.000
50	A	58	ARG	1	0.851	0.919	11.197	0.348	0.348	0.000	0.000	0.000	0.000
51	A	59	LYS	1	0.800	0.903	15.798	-0.024	-0.024	0.000	0.000	0.000	0.000
52	A	60	SER	0	0.021	0.018	15.422	-0.034	-0.034	0.000	0.000	0.000	0.000
53	A	61	SER	0	0.002	-0.019	12.755	-0.016	-0.016	0.000	0.000	0.000	0.000
54	A	62	ASP	-1	-0.818	-0.916	13.787	0.074	0.074	0.000	0.000	0.000	0.000
55	A	63	ASP	-1	-0.861	-0.925	13.493	0.230	0.230	0.000	0.000	0.000	0.000
56	A	64	VAL	0	-0.031	-0.007	7.936	0.102	0.102	0.000	0.000	0.000	0.000
57	A	65	GLN	0	-0.043	-0.013	6.936	-0.142	-0.142	0.000	0.000	0.000	0.000
58	A	66	ALA	0	-0.016	-0.005	9.892	-0.019	-0.019	0.000	0.000	0.000	0.000
59	A	67	ALA	0	0.005	0.011	11.921	-0.076	-0.076	0.000	0.000	0.000	0.000
60	A	68	TYR	0	-0.037	-0.050	11.983	-0.032	-0.032	0.000	0.000	0.000	0.000
61	A	69	ARG	1	0.811	0.900	16.186	0.021	0.021	0.000	0.000	0.000	0.000
62	A	70	ILE	0	-0.028	-0.007	19.873	-0.019	-0.019	0.000	0.000	0.000	0.000
63	A	71	ILE	0	0.007	-0.011	22.382	0.012	0.012	0.000	0.000	0.000	0.000
64	A	72	ASP	-1	-0.840	-0.922	26.019	-0.013	-0.013	0.000	0.000	0.000	0.000
65	A	73	GLY	0	0.043	0.007	29.053	0.001	0.001	0.000	0.000	0.000	0.000
66	A	74	ASP	-1	-0.909	-0.948	29.075	-0.040	-0.040	0.000	0.000	0.000	0.000
67	A	75	GLU	-1	-0.817	-0.915	27.959	-0.067	-0.067	0.000	0.000	0.000	0.000
68	A	76	ASP	-1	-0.957	-0.959	30.185	-0.042	-0.042	0.000	0.000	0.000	0.000
69	A	77	GLY	0	-0.031	-0.004	32.040	0.003	0.003	0.000	0.000	0.000	0.000
70	A	78	GLN	0	-0.106	-0.051	33.048	0.007	0.007	0.000	0.000	0.000	0.000
71	A	79	SER	0	0.033	0.016	33.163	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	80	SER	0	-0.004	-0.007	32.952	0.000	0.000	0.000	0.000	0.000	0.000
73	A	81	VAL	0	-0.003	-0.011	35.402	0.003	0.003	0.000	0.000	0.000	0.000
74	A	82	ASN	0	-0.030	-0.011	35.007	0.006	0.006	0.000	0.000	0.000	0.000
75	A	83	GLY	0	0.101	0.058	32.081	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	84	LEU	0	-0.049	-0.030	25.612	0.004	0.004	0.000	0.000	0.000	0.000
77	A	85	MET	0	-0.011	0.006	28.836	0.003	0.003	0.000	0.000	0.000	0.000
78	A	86	ILE	0	0.044	0.024	23.813	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	87	ASN	0	-0.004	-0.004	24.702	0.001	0.001	0.000	0.000	0.000	0.000
80	A	88	GLY	0	-0.002	0.004	28.514	0.000	0.000	0.000	0.000	0.000	0.000
81	A	89	LYS	1	0.927	0.965	30.767	-0.061	-0.061	0.000	0.000	0.000	0.000
82	A	90	LYS	1	0.853	0.908	30.557	-0.012	-0.012	0.000	0.000	0.000	0.000
83	A	91	VAL	0	-0.022	0.003	26.746	0.004	0.004	0.000	0.000	0.000	0.000
84	A	92	GLN	0	-0.035	-0.026	29.614	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	93	GLU	-1	-0.820	-0.896	25.470	0.004	0.004	0.000	0.000	0.000	0.000
86	A	94	HIS	0	-0.039	-0.035	21.174	0.001	0.001	0.000	0.000	0.000	0.000
87	A	95	ILE	0	-0.022	-0.007	17.757	-0.017	-0.017	0.000	0.000	0.000	0.000
88	A	96	ILE	0	-0.005	0.012	17.006	0.022	0.022	0.000	0.000	0.000	0.000
89	A	97	GLN	0	-0.012	-0.016	16.079	0.046	0.046	0.000	0.000	0.000	0.000
90	A	98	THR	0	-0.018	-0.017	12.184	-0.029	-0.029	0.000	0.000	0.000	0.000
91	A	99	GLY	0	-0.004	-0.009	14.664	0.041	0.041	0.000	0.000	0.000	0.000
92	A	100	ASP	-1	-0.791	-0.881	17.739	0.085	0.085	0.000	0.000	0.000	0.000
93	A	101	GLU	-1	-0.921	-0.943	20.221	0.032	0.032	0.000	0.000	0.000	0.000
94	A	102	ILE	0	-0.019	-0.012	20.980	0.002	0.002	0.000	0.000	0.000	0.000
95	A	103	VAL	0	0.005	0.003	24.903	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	104	MET	0	-0.031	-0.022	26.865	-0.002	-0.002	0.000	0.000	0.000	0.000
97	A	105	GLY	0	0.037	0.006	29.741	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	106	PRO	0	-0.026	-0.022	32.272	0.003	0.003	0.000	0.000	0.000	0.000
99	A	107	GLN	0	-0.012	-0.004	32.380	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	108	VAL	0	-0.030	0.008	28.441	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	109	SER	0	-0.065	-0.056	25.706	0.000	0.000	0.000	0.000	0.000	0.000
102	A	110	VAL	0	0.016	0.009	21.184	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	111	ARG	1	0.843	0.914	17.750	-0.088	-0.088	0.000	0.000	0.000	0.000
104	A	112	TYR	0	-0.037	-0.023	11.469	0.006	0.006	0.000	0.000	0.000	0.000
105	A	113	GLU	-1	-0.787	-0.877	12.817	0.176	0.176	0.000	0.000	0.000	0.000
106	A	114	TYR	0	0.013	-0.001	6.304	-0.137	-0.137	0.000	0.000	0.000	0.000
107	A	115	ARG	1	0.817	0.877	8.520	0.362	0.362	0.000	0.000	0.000	0.000
108	A	116	ARG	1	0.944	0.948	3.954	-4.083	-3.751	0.006	-0.134	-0.204	0.001
109	A	117	ARG	1	0.802	0.903	2.551	0.849	2.319	0.360	-0.670	-1.160	-0.001

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