FMO DATABASE

FMODB ID: R8LY8

Calculation Name: 2HR3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2HR3

Chain ID: A

ChEMBL ID:

UniProt ID: Q9HZE1

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:

Apendix: None

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	145
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1176846.115859
FMO2-HF: Nuclear repulsion	1120490.138792
FMO2-HF: Total energy	-56355.977067
FMO2-MP2: Total energy	-56521.544027

3D Structure Molmil

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:2:PRO)

Summations of interaction energy for fragment #1(A:2:PRO)

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.
-0.839	1.277	0.032	-0.975	-1.172	0.001

Interaction energy analysis for fragmet #1(A:2:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / q_NPA : -0.026

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	4	ASN	0	0.058	0.013	3.852	-1.594	-0.383	-0.015	-0.522	-0.674	0.004
4	A	5	GLN	0	-0.040	-0.039	6.657	0.086	0.086	0.000	0.000	0.000	0.000
5	A	6	ASP	-1	-0.781	-0.863	3.408	-0.284	0.621	0.047	-0.453	-0.498	-0.003
6	A	7	LEU	0	-0.013	-0.003	5.441	0.158	0.158	0.000	0.000	0.000	0.000
7	A	8	GLN	0	-0.019	-0.026	6.612	0.228	0.228	0.000	0.000	0.000	0.000
8	A	9	LEU	0	0.023	0.029	8.985	0.060	0.060	0.000	0.000	0.000	0.000
9	A	10	ALA	0	0.043	0.021	7.801	0.051	0.051	0.000	0.000	0.000	0.000
10	A	11	ALA	0	-0.054	-0.027	9.776	0.039	0.039	0.000	0.000	0.000	0.000
11	A	12	HIS	0	0.040	0.013	12.228	0.031	0.031	0.000	0.000	0.000	0.000
12	A	13	LEU	0	0.064	0.049	12.555	0.019	0.019	0.000	0.000	0.000	0.000
13	A	14	ARG	1	1.007	0.995	13.405	0.262	0.262	0.000	0.000	0.000	0.000
14	A	15	SER	0	-0.092	-0.029	15.177	0.022	0.022	0.000	0.000	0.000	0.000
15	A	16	GLN	0	0.078	0.022	17.608	0.017	0.017	0.000	0.000	0.000	0.000
16	A	17	VAL	0	0.074	0.065	17.609	0.012	0.012	0.000	0.000	0.000	0.000
17	A	18	THR	0	-0.069	-0.043	18.604	0.007	0.007	0.000	0.000	0.000	0.000
18	A	19	THR	0	-0.045	-0.055	21.084	0.008	0.008	0.000	0.000	0.000	0.000
19	A	20	LEU	0	0.018	0.023	22.920	0.005	0.005	0.000	0.000	0.000	0.000
20	A	21	THR	0	0.021	-0.009	22.821	0.007	0.007	0.000	0.000	0.000	0.000
21	A	22	ARG	1	0.924	0.962	22.128	0.106	0.106	0.000	0.000	0.000	0.000
22	A	23	ARG	1	0.782	0.888	27.244	0.041	0.041	0.000	0.000	0.000	0.000
23	A	24	LEU	0	0.098	0.038	27.202	0.003	0.003	0.000	0.000	0.000	0.000
24	A	25	ARG	1	0.881	0.959	27.338	0.072	0.072	0.000	0.000	0.000	0.000
25	A	26	ARG	1	0.922	0.941	28.834	0.061	0.061	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.779	-0.862	33.268	-0.031	-0.031	0.000	0.000	0.000	0.000
27	A	28	ALA	0	-0.028	-0.005	34.826	0.003	0.003	0.000	0.000	0.000	0.000
28	A	29	GLN	0	-0.070	-0.038	36.440	0.002	0.002	0.000	0.000	0.000	0.000
29	A	30	ALA	0	0.024	0.022	38.220	0.002	0.002	0.000	0.000	0.000	0.000
30	A	31	ASP	-1	-0.810	-0.891	38.649	-0.037	-0.037	0.000	0.000	0.000	0.000
31	A	32	PRO	0	0.050	-0.009	38.318	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	33	VAL	0	0.022	0.037	38.733	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	34	GLN	0	-0.002	-0.020	40.453	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.028	-0.016	31.192	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	SER	0	-0.035	-0.037	35.614	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	37	GLN	0	-0.017	-0.020	36.368	0.000	0.000	0.000	0.000	0.000	0.000
37	A	38	LEU	0	-0.013	0.010	34.809	0.001	0.001	0.000	0.000	0.000	0.000
38	A	39	VAL	0	-0.012	0.001	31.079	0.000	0.000	0.000	0.000	0.000	0.000
39	A	40	VAL	0	0.015	0.015	33.417	0.000	0.000	0.000	0.000	0.000	0.000
40	A	41	LEU	0	0.035	0.002	35.524	0.001	0.001	0.000	0.000	0.000	0.000
41	A	42	GLY	0	-0.028	-0.026	33.498	0.002	0.002	0.000	0.000	0.000	0.000
42	A	43	ALA	0	0.006	0.001	31.512	0.001	0.001	0.000	0.000	0.000	0.000
43	A	44	ILE	0	-0.007	-0.001	32.495	0.001	0.001	0.000	0.000	0.000	0.000
44	A	45	ASP	-1	-0.791	-0.860	35.005	-0.021	-0.021	0.000	0.000	0.000	0.000
45	A	46	ARG	1	0.834	0.908	28.175	0.052	0.052	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.051	-0.020	29.450	0.001	0.001	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.032	0.021	32.497	0.001	0.001	0.000	0.000	0.000	0.000
48	A	49	GLY	0	-0.037	-0.016	35.390	0.002	0.002	0.000	0.000	0.000	0.000
49	A	50	ASP	-1	-0.878	-0.949	37.822	-0.021	-0.021	0.000	0.000	0.000	0.000
50	A	51	VAL	0	0.026	0.044	34.788	0.000	0.000	0.000	0.000	0.000	0.000
51	A	52	THR	0	-0.010	0.002	36.194	-0.001	-0.001	0.000	0.000	0.000	0.000
52	A	53	PRO	0	0.037	0.003	36.419	-0.002	-0.002	0.000	0.000	0.000	0.000
53	A	54	SER	0	-0.014	-0.018	34.915	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.814	-0.894	32.256	-0.039	-0.039	0.000	0.000	0.000	0.000
55	A	56	LEU	0	0.027	0.019	31.216	-0.003	-0.003	0.000	0.000	0.000	0.000
56	A	57	ALA	0	-0.010	-0.021	31.607	-0.003	-0.003	0.000	0.000	0.000	0.000
57	A	58	ALA	0	-0.035	-0.010	28.653	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.044	0.031	27.094	-0.008	-0.008	0.000	0.000	0.000	0.000
59	A	60	GLU	-1	-0.822	-0.895	26.897	-0.064	-0.064	0.000	0.000	0.000	0.000
60	A	61	ARG	1	0.848	0.913	23.916	0.092	0.092	0.000	0.000	0.000	0.000
61	A	62	MET	0	-0.045	0.006	27.701	-0.001	-0.001	0.000	0.000	0.000	0.000
62	A	63	ARG	1	0.966	0.969	31.252	0.077	0.077	0.000	0.000	0.000	0.000
63	A	64	SER	0	0.057	0.024	33.576	0.004	0.004	0.000	0.000	0.000	0.000
64	A	65	SER	0	0.000	-0.015	36.378	0.002	0.002	0.000	0.000	0.000	0.000
65	A	66	ASN	0	-0.049	-0.026	35.780	0.001	0.001	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.108	0.047	35.065	0.002	0.002	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.006	0.017	37.739	0.003	0.003	0.000	0.000	0.000	0.000
68	A	69	ALA	0	-0.032	-0.039	41.080	0.003	0.003	0.000	0.000	0.000	0.000
69	A	70	LEU	0	0.067	0.038	37.128	0.002	0.002	0.000	0.000	0.000	0.000
70	A	71	LEU	0	-0.021	-0.003	38.997	0.002	0.002	0.000	0.000	0.000	0.000
71	A	72	ARG	1	0.972	0.981	42.042	0.038	0.038	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.961	-0.979	43.323	-0.036	-0.036	0.000	0.000	0.000	0.000
73	A	74	LEU	0	0.029	0.015	39.686	0.002	0.002	0.000	0.000	0.000	0.000
74	A	75	GLU	-1	-0.818	-0.878	44.376	-0.024	-0.024	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.872	0.941	47.202	0.030	0.030	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.016	0.012	47.909	0.001	0.001	0.000	0.000	0.000	0.000
77	A	78	GLY	0	0.049	0.034	48.469	0.001	0.001	0.000	0.000	0.000	0.000
78	A	79	LEU	0	-0.018	0.013	43.049	0.001	0.001	0.000	0.000	0.000	0.000
79	A	80	ILE	0	-0.034	-0.032	41.133	0.000	0.000	0.000	0.000	0.000	0.000
80	A	81	VAL	0	-0.009	-0.014	44.355	0.001	0.001	0.000	0.000	0.000	0.000
81	A	82	ARG	1	0.853	0.925	44.907	0.027	0.027	0.000	0.000	0.000	0.000
82	A	83	HIS	0	0.041	0.029	44.881	0.002	0.002	0.000	0.000	0.000	0.000
83	A	84	ALA	0	-0.002	-0.012	45.963	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.790	-0.894	47.876	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	86	PRO	0	0.006	0.033	50.104	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	87	GLN	0	0.022	-0.004	50.254	0.000	0.000	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.827	-0.904	45.890	-0.028	-0.028	0.000	0.000	0.000	0.000
88	A	89	GLY	0	-0.022	-0.011	45.061	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.750	0.838	44.887	0.018	0.018	0.000	0.000	0.000	0.000
90	A	91	ARG	1	0.875	0.949	39.771	0.031	0.031	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.016	-0.002	42.963	0.001	0.001	0.000	0.000	0.000	0.000
92	A	93	ARG	1	0.820	0.885	37.173	0.024	0.024	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.025	-0.012	39.350	0.001	0.001	0.000	0.000	0.000	0.000
94	A	95	SER	0	0.036	0.010	40.340	0.000	0.000	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.030	0.005	38.577	0.000	0.000	0.000	0.000	0.000	0.000
96	A	97	SER	0	0.044	0.001	42.412	0.002	0.002	0.000	0.000	0.000	0.000
97	A	98	SER	0	0.013	-0.024	44.754	0.000	0.000	0.000	0.000	0.000	0.000
98	A	99	GLU	-1	-0.789	-0.875	46.172	-0.019	-0.019	0.000	0.000	0.000	0.000
99	A	100	GLY	0	0.067	0.038	43.252	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	101	ARG	1	0.876	0.937	41.153	0.016	0.016	0.000	0.000	0.000	0.000
101	A	102	ARG	1	0.800	0.877	41.677	0.019	0.019	0.000	0.000	0.000	0.000
102	A	103	ASN	0	-0.052	-0.023	41.319	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	104	LEU	0	-0.007	0.015	35.132	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	105	TYR	0	-0.038	-0.056	37.403	0.000	0.000	0.000	0.000	0.000	0.000
105	A	106	GLY	0	0.065	0.044	39.114	0.001	0.001	0.000	0.000	0.000	0.000
106	A	107	ASN	0	-0.024	-0.001	36.464	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.809	0.866	33.056	0.025	0.025	0.000	0.000	0.000	0.000
108	A	109	ALA	0	0.070	0.059	35.828	0.000	0.000	0.000	0.000	0.000	0.000
109	A	110	LYS	1	0.963	0.993	38.299	0.023	0.023	0.000	0.000	0.000	0.000
110	A	111	ARG	1	0.835	0.899	32.248	0.033	0.033	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.895	-0.950	32.883	-0.019	-0.019	0.000	0.000	0.000	0.000
112	A	113	GLU	-1	-0.931	-0.958	34.740	-0.013	-0.013	0.000	0.000	0.000	0.000
113	A	114	TRP	0	-0.088	-0.048	30.521	0.000	0.000	0.000	0.000	0.000	0.000
114	A	115	LEU	0	0.015	0.001	28.770	0.000	0.000	0.000	0.000	0.000	0.000
115	A	116	VAL	0	0.067	0.037	32.861	0.001	0.001	0.000	0.000	0.000	0.000
116	A	117	ARG	1	0.948	0.980	35.147	0.019	0.019	0.000	0.000	0.000	0.000
117	A	118	ALA	0	-0.038	-0.021	31.875	0.000	0.000	0.000	0.000	0.000	0.000
118	A	119	MET	0	0.029	0.007	29.539	0.000	0.000	0.000	0.000	0.000	0.000
119	A	120	HIS	0	-0.061	-0.031	32.569	0.005	0.005	0.000	0.000	0.000	0.000
120	A	121	ALA	0	-0.049	-0.017	35.472	0.002	0.002	0.000	0.000	0.000	0.000
121	A	122	CYS	0	-0.102	-0.050	30.779	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	123	LEU	0	0.004	0.018	27.854	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	124	ASP	-1	-0.794	-0.882	31.516	0.020	0.020	0.000	0.000	0.000	0.000
124	A	125	GLU	-1	-0.849	-0.922	31.755	0.015	0.015	0.000	0.000	0.000	0.000
125	A	126	SER	0	-0.090	-0.062	29.860	0.003	0.003	0.000	0.000	0.000	0.000
126	A	127	GLU	-1	-0.842	-0.938	27.337	0.011	0.011	0.000	0.000	0.000	0.000
127	A	128	ARG	1	0.816	0.887	27.179	-0.009	-0.009	0.000	0.000	0.000	0.000
128	A	129	ALA	0	0.010	0.015	28.577	0.000	0.000	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.002	0.000	22.645	0.005	0.005	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.011	-0.007	23.184	0.001	0.001	0.000	0.000	0.000	0.000
131	A	132	ALA	0	-0.033	-0.003	24.568	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	133	ALA	0	-0.027	-0.015	23.188	0.001	0.001	0.000	0.000	0.000	0.000
133	A	134	ALA	0	-0.008	-0.016	19.826	0.005	0.005	0.000	0.000	0.000	0.000
134	A	135	GLY	0	0.020	0.027	20.013	-0.006	-0.006	0.000	0.000	0.000	0.000
135	A	136	PRO	0	0.016	-0.002	21.445	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	137	LEU	0	-0.032	-0.020	16.752	0.003	0.003	0.000	0.000	0.000	0.000
137	A	138	LEU	0	-0.020	-0.007	16.938	-0.011	-0.011	0.000	0.000	0.000	0.000
138	A	139	THR	0	-0.004	0.000	18.161	-0.015	-0.015	0.000	0.000	0.000	0.000
139	A	140	ARG	1	0.976	0.990	16.039	-0.086	-0.086	0.000	0.000	0.000	0.000
140	A	141	LEU	0	-0.008	-0.006	11.825	-0.005	-0.005	0.000	0.000	0.000	0.000
141	A	142	ALA	0	-0.065	-0.040	15.244	-0.019	-0.019	0.000	0.000	0.000	0.000
142	A	143	GLN	0	-0.050	-0.019	17.995	0.000	0.000	0.000	0.000	0.000	0.000
143	A	144	PHE	0	-0.056	-0.013	10.030	0.020	0.020	0.000	0.000	0.000	0.000
144	A	145	GLU	-1	-0.931	-0.961	15.566	-0.090	-0.090	0.000	0.000	0.000	0.000
145	A	146	GLU	-1	-1.005	-0.995	9.582	-0.254	-0.254	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:PRO)