FMO DATABASE

FMODB ID: 3JN7L

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

Total energy (hartree)

FMO2-HF: Electronic energy	-883652.53944
FMO2-HF: Nuclear repulsion	840344.493157
FMO2-HF: Total energy	-43308.046283
FMO2-MP2: Total energy	-43435.890558

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.
-8.078	-4.204	0.571	-1.615	-2.828	0.001

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 : -0.042 / q_NPA : -0.036

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	-0.896	-0.941	3.802	-3.509	-2.012	-0.014	-0.553	-0.930	0.002
4	A	12	HIS	0	0.049	0.073	6.235	0.578	0.578	0.000	0.000	0.000	0.000
5	A	13	ILE	0	-0.017	0.013	9.786	0.003	0.003	0.000	0.000	0.000	0.000
6	A	14	LEU	0	0.023	0.000	12.419	0.081	0.081	0.000	0.000	0.000	0.000
7	A	15	ILE	0	-0.023	-0.014	15.410	0.000	0.000	0.000	0.000	0.000	0.000
8	A	16	ILE	0	-0.013	-0.009	18.510	0.021	0.021	0.000	0.000	0.000	0.000
9	A	17	LEU	0	-0.020	0.000	21.725	0.003	0.003	0.000	0.000	0.000	0.000
10	A	18	ASP	-1	-0.740	-0.890	25.083	-0.101	-0.101	0.000	0.000	0.000	0.000
11	A	19	ASP	-1	-0.873	-0.942	28.131	-0.059	-0.059	0.000	0.000	0.000	0.000
12	A	20	ALA	0	-0.154	-0.074	27.159	0.004	0.004	0.000	0.000	0.000	0.000
13	A	21	GLY	0	0.000	0.012	27.094	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	22	ARG	1	0.955	0.963	21.150	0.048	0.048	0.000	0.000	0.000	0.000
15	A	23	ARG	1	0.869	0.934	20.292	0.158	0.158	0.000	0.000	0.000	0.000
16	A	24	GLU	-1	-0.835	-0.918	14.179	-0.217	-0.217	0.000	0.000	0.000	0.000
17	A	25	VAL	0	-0.024	-0.006	15.674	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	26	LEU	0	0.026	0.022	8.344	0.012	0.012	0.000	0.000	0.000	0.000
19	A	27	LEU	0	-0.064	-0.039	11.677	0.048	0.048	0.000	0.000	0.000	0.000
20	A	28	THR	0	0.015	-0.012	10.514	-0.159	-0.159	0.000	0.000	0.000	0.000
21	A	29	GLU	-1	-0.889	-0.950	11.690	-0.444	-0.444	0.000	0.000	0.000	0.000
22	A	30	THR	0	0.000	0.025	14.496	-0.037	-0.037	0.000	0.000	0.000	0.000
23	A	31	PHE	0	0.038	0.016	16.443	0.023	0.023	0.000	0.000	0.000	0.000
24	A	32	TYR	0	0.023	0.049	14.781	-0.044	-0.044	0.000	0.000	0.000	0.000
25	A	33	THR	0	0.031	0.004	20.444	0.019	0.019	0.000	0.000	0.000	0.000
26	A	34	ILE	0	0.004	-0.011	20.882	-0.009	-0.009	0.000	0.000	0.000	0.000
27	A	35	GLY	0	0.056	0.016	24.696	0.014	0.014	0.000	0.000	0.000	0.000
28	A	36	ARG	1	0.867	0.961	27.576	0.059	0.059	0.000	0.000	0.000	0.000
29	A	37	SER	0	-0.097	-0.048	30.270	0.001	0.001	0.000	0.000	0.000	0.000
30	A	38	PRO	0	-0.027	-0.048	28.990	-0.006	-0.006	0.000	0.000	0.000	0.000
31	A	39	ARG	1	0.969	0.982	28.401	0.088	0.088	0.000	0.000	0.000	0.000
32	A	40	ALA	0	0.007	0.026	25.829	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	41	ASP	-1	-0.793	-0.843	21.064	-0.194	-0.194	0.000	0.000	0.000	0.000
34	A	42	ILE	0	-0.009	0.000	18.133	-0.009	-0.009	0.000	0.000	0.000	0.000
35	A	43	ARG	1	0.904	0.950	22.240	0.128	0.128	0.000	0.000	0.000	0.000
36	A	44	ILE	0	0.021	0.017	23.284	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	45	LYS	1	0.861	0.930	26.627	0.083	0.083	0.000	0.000	0.000	0.000
38	A	46	SER	0	0.116	0.042	29.749	0.006	0.006	0.000	0.000	0.000	0.000
39	A	47	GLN	0	-0.031	-0.022	32.571	0.000	0.000	0.000	0.000	0.000	0.000
40	A	48	PHE	0	-0.037	-0.019	33.755	0.002	0.002	0.000	0.000	0.000	0.000
41	A	49	VAL	0	0.023	0.042	28.914	0.001	0.001	0.000	0.000	0.000	0.000
42	A	50	SER	0	0.040	0.024	32.120	0.003	0.003	0.000	0.000	0.000	0.000
43	A	51	ARG	1	0.877	0.923	31.274	0.061	0.061	0.000	0.000	0.000	0.000
44	A	52	ILE	0	0.038	0.020	27.981	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	53	HIS	0	-0.005	-0.019	27.969	0.003	0.003	0.000	0.000	0.000	0.000
46	A	54	ALA	0	0.026	0.033	25.374	0.007	0.007	0.000	0.000	0.000	0.000
47	A	55	VAL	0	0.019	0.022	23.541	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	56	LEU	0	-0.037	-0.013	17.621	0.008	0.008	0.000	0.000	0.000	0.000
49	A	57	VAL	0	0.035	0.013	19.189	-0.017	-0.017	0.000	0.000	0.000	0.000
50	A	58	ARG	1	0.856	0.927	11.213	0.540	0.540	0.000	0.000	0.000	0.000
51	A	59	LYS	1	0.807	0.904	16.064	0.108	0.108	0.000	0.000	0.000	0.000
52	A	60	SER	0	0.006	0.004	16.166	-0.028	-0.028	0.000	0.000	0.000	0.000
53	A	61	SER	0	-0.037	-0.009	13.368	-0.034	-0.034	0.000	0.000	0.000	0.000
54	A	62	ASP	-1	-0.789	-0.921	14.013	-0.074	-0.074	0.000	0.000	0.000	0.000
55	A	63	ASP	-1	-0.878	-0.941	13.843	0.101	0.101	0.000	0.000	0.000	0.000
56	A	64	VAL	0	-0.033	-0.008	8.279	0.083	0.083	0.000	0.000	0.000	0.000
57	A	65	GLN	0	-0.053	-0.026	6.972	-0.273	-0.273	0.000	0.000	0.000	0.000
58	A	66	ALA	0	-0.023	0.001	10.398	0.006	0.006	0.000	0.000	0.000	0.000
59	A	67	ALA	0	0.019	0.005	11.619	-0.105	-0.105	0.000	0.000	0.000	0.000
60	A	68	TYR	0	-0.059	-0.086	11.857	-0.029	-0.029	0.000	0.000	0.000	0.000
61	A	69	ARG	1	0.843	0.922	16.242	0.102	0.102	0.000	0.000	0.000	0.000
62	A	70	ILE	0	-0.026	-0.013	19.986	-0.018	-0.018	0.000	0.000	0.000	0.000
63	A	71	ILE	0	-0.011	-0.002	22.355	0.016	0.016	0.000	0.000	0.000	0.000
64	A	72	ASP	-1	-0.891	-0.977	25.874	-0.069	-0.069	0.000	0.000	0.000	0.000
65	A	73	GLY	0	0.052	0.022	28.787	0.002	0.002	0.000	0.000	0.000	0.000
66	A	74	ASP	-1	-0.947	-0.990	28.827	-0.087	-0.087	0.000	0.000	0.000	0.000
67	A	75	GLU	-1	-0.912	-0.990	27.202	-0.129	-0.129	0.000	0.000	0.000	0.000
68	A	76	ASP	-1	-0.994	-0.977	29.700	-0.073	-0.073	0.000	0.000	0.000	0.000
69	A	77	GLY	0	-0.042	-0.009	31.914	0.005	0.005	0.000	0.000	0.000	0.000
70	A	78	GLN	0	-0.068	-0.023	32.881	0.011	0.011	0.000	0.000	0.000	0.000
71	A	79	SER	0	0.041	0.029	33.038	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	80	SER	0	-0.026	-0.014	32.101	0.002	0.002	0.000	0.000	0.000	0.000
73	A	81	VAL	0	0.005	-0.005	34.945	0.003	0.003	0.000	0.000	0.000	0.000
74	A	82	ASN	0	-0.072	-0.043	33.677	0.005	0.005	0.000	0.000	0.000	0.000
75	A	83	GLY	0	0.114	0.063	31.863	-0.004	-0.004	0.000	0.000	0.000	0.000
76	A	84	LEU	0	0.031	0.011	25.624	-0.003	-0.003	0.000	0.000	0.000	0.000
77	A	85	MET	0	-0.052	-0.026	28.940	0.007	0.007	0.000	0.000	0.000	0.000
78	A	86	ILE	0	0.062	0.038	23.592	-0.002	-0.002	0.000	0.000	0.000	0.000
79	A	87	ASN	0	0.031	0.005	25.265	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	88	GLY	0	-0.022	-0.011	28.759	0.003	0.003	0.000	0.000	0.000	0.000
81	A	89	LYS	1	0.936	0.965	30.840	-0.014	-0.014	0.000	0.000	0.000	0.000
82	A	90	LYS	1	0.895	0.949	30.426	0.027	0.027	0.000	0.000	0.000	0.000
83	A	91	VAL	0	-0.025	0.006	26.660	0.004	0.004	0.000	0.000	0.000	0.000
84	A	92	GLN	0	0.010	0.009	29.891	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	93	GLU	-1	-0.816	-0.914	25.303	-0.071	-0.071	0.000	0.000	0.000	0.000
86	A	94	HIS	0	-0.048	-0.023	21.376	0.010	0.010	0.000	0.000	0.000	0.000
87	A	95	ILE	0	-0.021	-0.007	17.826	-0.021	-0.021	0.000	0.000	0.000	0.000
88	A	96	ILE	0	-0.003	-0.008	16.946	0.025	0.025	0.000	0.000	0.000	0.000
89	A	97	GLN	0	-0.011	-0.001	15.958	0.011	0.011	0.000	0.000	0.000	0.000
90	A	98	THR	0	-0.013	-0.018	12.719	-0.036	-0.036	0.000	0.000	0.000	0.000
91	A	99	GLY	0	-0.045	-0.035	14.840	0.046	0.046	0.000	0.000	0.000	0.000
92	A	100	ASP	-1	-0.823	-0.895	17.821	0.005	0.005	0.000	0.000	0.000	0.000
93	A	101	GLU	-1	-0.956	-0.997	19.965	-0.035	-0.035	0.000	0.000	0.000	0.000
94	A	102	ILE	0	-0.003	-0.003	21.062	0.007	0.007	0.000	0.000	0.000	0.000
95	A	103	VAL	0	-0.002	0.007	24.481	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	104	MET	0	-0.017	-0.014	26.410	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	105	GLY	0	0.014	-0.001	29.168	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	106	PRO	0	-0.065	-0.032	31.802	0.001	0.001	0.000	0.000	0.000	0.000
99	A	107	GLN	0	0.019	0.003	31.736	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	108	VAL	0	-0.022	0.002	27.534	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	109	SER	0	-0.048	-0.021	25.429	0.002	0.002	0.000	0.000	0.000	0.000
102	A	110	VAL	0	0.029	0.024	20.511	-0.009	-0.009	0.000	0.000	0.000	0.000
103	A	111	ARG	1	0.893	0.939	17.341	0.015	0.015	0.000	0.000	0.000	0.000
104	A	112	TYR	0	-0.023	-0.052	11.141	-0.001	-0.001	0.000	0.000	0.000	0.000
105	A	113	GLU	-1	-0.831	-0.917	12.308	0.049	0.049	0.000	0.000	0.000	0.000
106	A	114	TYR	0	-0.009	0.012	5.894	-0.275	-0.275	0.000	0.000	0.000	0.000
107	A	115	ARG	1	0.844	0.918	7.692	0.558	0.558	0.000	0.000	0.000	0.000
108	A	116	ARG	1	0.942	0.997	3.757	-4.163	-3.808	0.007	-0.171	-0.190	0.001
109	A	117	ARG	1	0.989	1.005	2.379	-0.875	1.147	0.578	-0.891	-1.708	-0.002

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