FMO DATABASE

FMODB ID: 1JQZZ

Calculation Name: 2RH3-A-Xray316

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2RH3

Chain ID: A

ChEMBL ID:

UniProt ID: P07166

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-981135.378877
FMO2-HF: Nuclear repulsion	934364.336602
FMO2-HF: Total energy	-46771.042275
FMO2-MP2: Total energy	-46907.938542

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:82:ILE )

Summations of interaction energy for fragment #1(A:82: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.
29.641	35.281	11.554	-6.991	-10.203	-0.068

Interaction energy analysis for fragmet #1(A:82:ILE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.854 / q_NPA : 0.923

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	84	VAL	0	-0.021	0.007	2.850	-0.176	2.674	0.180	-1.172	-1.858	-0.005
4	A	85	PHE	0	0.017	-0.006	4.970	2.896	2.987	0.000	-0.009	-0.082	0.000
5	A	86	LEU	0	-0.037	-0.021	8.126	0.472	0.472	0.000	0.000	0.000	0.000
6	A	87	SER	0	-0.013	-0.011	11.002	0.923	0.923	0.000	0.000	0.000	0.000
7	A	88	ALA	0	0.033	0.020	14.636	-0.105	-0.105	0.000	0.000	0.000	0.000
8	A	89	ARG	1	0.937	0.972	17.846	12.853	12.853	0.000	0.000	0.000	0.000
9	A	90	PRO	0	0.027	0.033	21.606	-0.255	-0.255	0.000	0.000	0.000	0.000
10	A	91	PRO	0	0.009	0.015	23.652	0.154	0.154	0.000	0.000	0.000	0.000
11	A	92	ALA	0	-0.046	-0.024	25.943	0.217	0.217	0.000	0.000	0.000	0.000
12	A	93	PRO	0	0.038	0.011	29.664	-0.144	-0.144	0.000	0.000	0.000	0.000
13	A	94	GLU	-1	-0.938	-0.969	32.158	-8.727	-8.727	0.000	0.000	0.000	0.000
14	A	95	VAL	0	-0.156	-0.055	26.504	-0.104	-0.104	0.000	0.000	0.000	0.000
15	A	96	SER	0	-0.066	-0.061	26.319	-0.258	-0.258	0.000	0.000	0.000	0.000
16	A	97	LYS	1	1.058	1.027	28.408	9.345	9.345	0.000	0.000	0.000	0.000
17	A	98	ILE	0	-0.013	-0.002	25.452	0.004	0.004	0.000	0.000	0.000	0.000
18	A	99	TYR	0	0.000	-0.025	24.693	-0.339	-0.339	0.000	0.000	0.000	0.000
19	A	100	ASP	-1	-0.790	-0.904	27.171	-10.108	-10.108	0.000	0.000	0.000	0.000
20	A	101	ASN	0	0.002	0.003	30.778	0.493	0.493	0.000	0.000	0.000	0.000
21	A	102	LEU	0	-0.063	-0.031	24.990	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	103	ILE	0	-0.039	-0.019	27.898	0.023	0.023	0.000	0.000	0.000	0.000
23	A	104	LEU	0	-0.004	0.019	30.138	0.272	0.272	0.000	0.000	0.000	0.000
24	A	105	GLN	0	-0.042	-0.026	30.520	-0.114	-0.114	0.000	0.000	0.000	0.000
25	A	106	TYR	0	-0.038	-0.024	27.001	-0.329	-0.329	0.000	0.000	0.000	0.000
26	A	107	SER	0	0.040	0.016	25.866	-0.029	-0.029	0.000	0.000	0.000	0.000
27	A	108	PRO	0	0.111	0.045	26.107	-0.419	-0.419	0.000	0.000	0.000	0.000
28	A	109	SER	0	-0.016	-0.005	21.746	-0.719	-0.719	0.000	0.000	0.000	0.000
29	A	110	LYS	1	0.964	0.994	21.391	12.065	12.065	0.000	0.000	0.000	0.000
30	A	111	SER	0	0.040	0.007	22.234	-0.480	-0.480	0.000	0.000	0.000	0.000
31	A	112	LEU	0	0.033	0.011	19.512	-0.345	-0.345	0.000	0.000	0.000	0.000
32	A	113	GLN	0	-0.033	-0.014	17.150	-0.462	-0.462	0.000	0.000	0.000	0.000
33	A	114	MET	0	-0.097	-0.038	17.857	-0.924	-0.924	0.000	0.000	0.000	0.000
34	A	115	ILE	0	0.040	0.032	19.592	-0.542	-0.542	0.000	0.000	0.000	0.000
35	A	116	LEU	0	0.015	0.010	13.722	-0.683	-0.683	0.000	0.000	0.000	0.000
36	A	117	ARG	1	0.945	0.980	14.576	17.377	17.377	0.000	0.000	0.000	0.000
37	A	118	ARG	1	0.925	0.973	14.883	14.511	14.511	0.000	0.000	0.000	0.000
38	A	119	ALA	0	0.033	0.018	16.685	-0.412	-0.412	0.000	0.000	0.000	0.000
39	A	120	LEU	0	-0.032	-0.034	10.588	-0.891	-0.891	0.000	0.000	0.000	0.000
40	A	121	GLY	0	-0.020	0.005	12.105	-1.694	-1.694	0.000	0.000	0.000	0.000
41	A	122	ASP	-1	-0.884	-0.951	13.653	-16.965	-16.965	0.000	0.000	0.000	0.000
42	A	123	PHE	0	0.003	-0.027	12.155	0.077	0.077	0.000	0.000	0.000	0.000
43	A	124	GLU	-1	-0.827	-0.924	8.029	-35.288	-35.288	0.000	0.000	0.000	0.000
44	A	125	ASN	0	0.004	-0.007	11.438	-1.293	-1.293	0.000	0.000	0.000	0.000
45	A	126	MET	0	-0.016	0.010	14.362	0.880	0.880	0.000	0.000	0.000	0.000
46	A	127	LEU	0	-0.079	-0.039	9.291	0.113	0.113	0.000	0.000	0.000	0.000
47	A	128	ALA	0	-0.034	-0.020	12.524	0.228	0.228	0.000	0.000	0.000	0.000
48	A	129	ASP	-1	-0.771	-0.853	13.378	-16.592	-16.592	0.000	0.000	0.000	0.000
49	A	130	GLY	0	-0.074	-0.041	15.876	1.061	1.061	0.000	0.000	0.000	0.000
50	A	131	SER	0	-0.013	-0.040	17.242	0.645	0.645	0.000	0.000	0.000	0.000
51	A	132	PHE	0	-0.043	-0.022	13.142	0.518	0.518	0.000	0.000	0.000	0.000
52	A	133	ARG	1	0.882	0.959	15.165	17.956	17.956	0.000	0.000	0.000	0.000
53	A	134	ALA	0	-0.009	0.005	18.421	0.614	0.614	0.000	0.000	0.000	0.000
54	A	135	ALA	0	-0.013	0.006	18.974	0.585	0.585	0.000	0.000	0.000	0.000
55	A	136	PRO	0	0.003	-0.014	20.578	-0.097	-0.097	0.000	0.000	0.000	0.000
56	A	137	LYS	1	0.908	0.964	17.295	15.250	15.250	0.000	0.000	0.000	0.000
57	A	138	SER	0	-0.020	-0.020	19.042	-0.417	-0.417	0.000	0.000	0.000	0.000
58	A	139	TYR	0	-0.041	-0.037	19.897	0.000	0.000	0.000	0.000	0.000	0.000
59	A	140	PRO	0	0.030	0.017	24.609	-0.109	-0.109	0.000	0.000	0.000	0.000
60	A	141	ILE	0	-0.001	0.000	24.170	-0.330	-0.330	0.000	0.000	0.000	0.000
61	A	142	PRO	0	0.042	0.016	27.368	0.375	0.375	0.000	0.000	0.000	0.000
62	A	143	HIS	0	-0.030	-0.008	29.460	-0.034	-0.034	0.000	0.000	0.000	0.000
63	A	144	THR	0	0.040	0.032	32.910	0.406	0.406	0.000	0.000	0.000	0.000
64	A	145	ALA	0	0.043	0.015	34.472	-0.181	-0.181	0.000	0.000	0.000	0.000
65	A	146	PHE	0	-0.045	-0.027	36.474	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	147	GLU	-1	-0.921	-0.964	30.566	-10.320	-10.320	0.000	0.000	0.000	0.000
67	A	148	LYS	1	0.965	0.985	30.615	9.762	9.762	0.000	0.000	0.000	0.000
68	A	149	SER	0	0.002	-0.001	25.423	-0.371	-0.371	0.000	0.000	0.000	0.000
69	A	150	ILE	0	0.015	0.005	23.131	-0.087	-0.087	0.000	0.000	0.000	0.000
70	A	151	ILE	0	-0.043	-0.022	17.622	-0.150	-0.150	0.000	0.000	0.000	0.000
71	A	152	VAL	0	-0.011	0.002	17.932	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	153	GLN	0	0.015	-0.006	14.595	-1.688	-1.688	0.000	0.000	0.000	0.000
73	A	154	THR	0	-0.001	-0.004	11.876	0.251	0.251	0.000	0.000	0.000	0.000
74	A	155	SER	0	-0.031	-0.012	8.386	-0.299	-0.299	0.000	0.000	0.000	0.000
75	A	156	ARG	1	0.883	0.939	7.543	33.912	33.912	0.000	0.000	0.000	0.000
76	A	157	MET	0	-0.023	0.000	3.730	-10.808	-10.344	0.010	-0.196	-0.279	-0.001
77	A	158	PHE	0	0.068	0.032	3.037	9.413	10.666	0.021	-0.464	-0.811	-0.001
78	A	159	PRO	0	0.042	0.014	1.953	-43.455	-44.058	7.857	-3.968	-3.286	-0.051
79	A	160	VAL	0	0.026	-0.006	2.307	-3.939	-3.393	3.139	-0.962	-2.722	-0.009
80	A	161	SER	0	0.034	0.030	4.010	5.475	5.634	0.002	-0.038	-0.123	0.000
81	A	162	LEU	0	0.066	0.035	6.902	2.362	2.362	0.000	0.000	0.000	0.000
82	A	163	ILE	0	-0.030	-0.017	2.512	1.771	2.546	0.345	-0.174	-0.946	-0.001
83	A	164	GLU	-1	-0.934	-0.950	5.632	-24.522	-24.522	0.000	0.000	0.000	0.000
84	A	165	ALA	0	0.010	0.006	7.394	3.024	3.024	0.000	0.000	0.000	0.000
85	A	166	ALA	0	-0.002	-0.013	7.649	2.186	2.186	0.000	0.000	0.000	0.000
86	A	167	ARG	1	0.945	0.959	4.171	33.745	33.850	0.000	-0.008	-0.096	0.000
87	A	168	ASN	0	0.050	0.035	8.841	1.737	1.737	0.000	0.000	0.000	0.000
88	A	169	HIS	0	-0.045	-0.018	11.980	1.809	1.809	0.000	0.000	0.000	0.000
89	A	170	PHE	0	-0.042	-0.048	11.054	1.252	1.252	0.000	0.000	0.000	0.000
90	A	171	ASP	-1	-0.849	-0.934	10.449	-19.919	-19.919	0.000	0.000	0.000	0.000
91	A	172	PRO	0	0.013	0.024	12.516	-0.257	-0.257	0.000	0.000	0.000	0.000
92	A	173	LEU	0	-0.022	-0.015	15.002	0.437	0.437	0.000	0.000	0.000	0.000
93	A	174	GLY	0	-0.018	0.004	11.882	0.244	0.244	0.000	0.000	0.000	0.000
94	A	175	LEU	0	-0.030	-0.016	12.882	0.039	0.039	0.000	0.000	0.000	0.000
95	A	176	GLU	-1	-0.963	-0.973	11.757	-16.267	-16.267	0.000	0.000	0.000	0.000
96	A	177	THR	0	0.008	-0.001	11.236	-1.401	-1.401	0.000	0.000	0.000	0.000
97	A	178	ALA	0	0.028	-0.009	7.027	-0.730	-0.730	0.000	0.000	0.000	0.000
98	A	179	ARG	1	0.992	1.004	8.571	16.336	16.336	0.000	0.000	0.000	0.000
99	A	180	ALA	0	-0.036	-0.012	11.227	0.265	0.265	0.000	0.000	0.000	0.000
100	A	181	PHE	0	0.048	0.017	5.446	0.041	0.041	0.000	0.000	0.000	0.000
101	A	182	GLY	0	0.058	0.023	9.273	-0.331	-0.331	0.000	0.000	0.000	0.000
102	A	183	HIS	0	-0.028	-0.016	9.954	0.139	0.139	0.000	0.000	0.000	0.000
103	A	184	LYS	1	0.929	0.976	12.511	17.370	17.370	0.000	0.000	0.000	0.000
104	A	185	LEU	0	-0.003	0.014	7.843	0.543	0.543	0.000	0.000	0.000	0.000
105	A	186	ALA	0	0.004	-0.010	11.770	0.481	0.481	0.000	0.000	0.000	0.000
106	A	187	THR	0	-0.040	-0.022	13.642	1.254	1.254	0.000	0.000	0.000	0.000
107	A	188	ALA	0	0.029	0.015	14.880	0.883	0.883	0.000	0.000	0.000	0.000
108	A	189	ALA	0	-0.013	0.004	13.796	0.623	0.623	0.000	0.000	0.000	0.000
109	A	190	LEU	0	-0.004	-0.016	15.918	0.744	0.744	0.000	0.000	0.000	0.000
110	A	191	ALA	0	-0.008	0.011	18.843	0.842	0.842	0.000	0.000	0.000	0.000
111	A	192	CYS	0	-0.061	-0.017	18.764	0.924	0.924	0.000	0.000	0.000	0.000
112	A	193	PHE	0	0.001	0.000	19.821	0.448	0.448	0.000	0.000	0.000	0.000
113	A	194	PHE	0	0.044	-0.002	21.591	0.495	0.495	0.000	0.000	0.000	0.000
114	A	195	ALA	0	-0.010	0.002	24.027	0.583	0.583	0.000	0.000	0.000	0.000
115	A	196	ARG	1	0.956	0.980	20.778	14.564	14.564	0.000	0.000	0.000	0.000
116	A	197	GLU	-1	-0.709	-0.844	25.848	-11.413	-11.413	0.000	0.000	0.000	0.000
117	A	198	LYS	1	0.934	0.978	27.807	10.168	10.168	0.000	0.000	0.000	0.000
118	A	199	ALA	0	-0.052	-0.031	28.921	0.364	0.364	0.000	0.000	0.000	0.000
119	A	200	THR	0	-0.069	-0.041	28.610	0.197	0.197	0.000	0.000	0.000	0.000
120	A	201	ASN	0	-0.052	-0.019	31.347	0.086	0.086	0.000	0.000	0.000	0.000
121	A	202	SER	-1	-0.955	-0.964	30.299	-9.888	-9.888	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:82:ILE )