FMO DATABASE

FMODB ID: 662KZ

Calculation Name: 2RH3-A-Xray372

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: 2023-06-20

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	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-984608.393021
FMO2-HF: Nuclear repulsion	937836.444326
FMO2-HF: Total energy	-46771.948695
FMO2-MP2: Total energy	-46908.834095

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.
-11.083	-3.894	8.846	-5.538	-10.497	-0.017

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 : 0 / q_Mulliken : 0.063 / q_NPA : 0.034

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	84	VAL	0	-0.031	-0.006	2.873	-2.917	0.860	0.147	-1.820	-2.103	0.004
4	A	85	PHE	0	0.017	-0.005	5.317	0.064	0.124	-0.001	-0.003	-0.055	0.000
5	A	86	LEU	0	-0.034	-0.015	8.833	0.028	0.028	0.000	0.000	0.000	0.000
6	A	87	SER	0	-0.005	-0.009	11.441	0.067	0.067	0.000	0.000	0.000	0.000
7	A	88	ALA	0	0.042	0.020	15.188	-0.004	-0.004	0.000	0.000	0.000	0.000
8	A	89	ARG	1	0.886	0.937	18.054	0.216	0.216	0.000	0.000	0.000	0.000
9	A	90	PRO	0	0.019	0.018	21.899	-0.017	-0.017	0.000	0.000	0.000	0.000
10	A	91	PRO	0	-0.004	0.010	23.649	0.006	0.006	0.000	0.000	0.000	0.000
11	A	92	ALA	0	-0.038	-0.019	25.888	0.007	0.007	0.000	0.000	0.000	0.000
12	A	93	PRO	0	0.041	0.008	29.542	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	94	GLU	-1	-0.952	-0.974	32.062	-0.124	-0.124	0.000	0.000	0.000	0.000
14	A	95	VAL	0	-0.139	-0.052	26.566	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	96	SER	0	-0.068	-0.070	26.309	-0.014	-0.014	0.000	0.000	0.000	0.000
16	A	97	LYS	1	0.984	0.986	28.351	0.144	0.144	0.000	0.000	0.000	0.000
17	A	98	ILE	0	-0.046	-0.016	25.341	0.002	0.002	0.000	0.000	0.000	0.000
18	A	99	TYR	0	0.021	-0.012	24.936	-0.013	-0.013	0.000	0.000	0.000	0.000
19	A	100	ASP	-1	-0.790	-0.906	27.062	-0.162	-0.162	0.000	0.000	0.000	0.000
20	A	101	ASN	0	-0.005	-0.008	30.632	0.016	0.016	0.000	0.000	0.000	0.000
21	A	102	LEU	0	-0.064	-0.030	24.890	0.001	0.001	0.000	0.000	0.000	0.000
22	A	103	ILE	0	-0.003	-0.006	28.078	0.003	0.003	0.000	0.000	0.000	0.000
23	A	104	LEU	0	-0.029	0.008	30.296	0.009	0.009	0.000	0.000	0.000	0.000
24	A	105	GLN	0	-0.021	-0.001	30.524	0.003	0.003	0.000	0.000	0.000	0.000
25	A	106	TYR	0	0.013	-0.009	27.094	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	107	SER	0	0.073	0.035	25.869	-0.003	-0.003	0.000	0.000	0.000	0.000
27	A	108	PRO	0	0.086	0.035	26.019	-0.016	-0.016	0.000	0.000	0.000	0.000
28	A	109	SER	0	-0.018	-0.010	21.272	-0.020	-0.020	0.000	0.000	0.000	0.000
29	A	110	LYS	1	0.864	0.954	21.435	0.187	0.187	0.000	0.000	0.000	0.000
30	A	111	SER	0	0.022	-0.004	22.231	-0.021	-0.021	0.000	0.000	0.000	0.000
31	A	112	LEU	0	0.031	0.016	19.484	-0.013	-0.013	0.000	0.000	0.000	0.000
32	A	113	GLN	0	0.000	-0.009	17.217	-0.009	-0.009	0.000	0.000	0.000	0.000
33	A	114	MET	0	-0.102	-0.044	17.851	-0.043	-0.043	0.000	0.000	0.000	0.000
34	A	115	ILE	0	0.041	0.036	19.474	-0.029	-0.029	0.000	0.000	0.000	0.000
35	A	116	LEU	0	0.012	0.005	13.777	-0.030	-0.030	0.000	0.000	0.000	0.000
36	A	117	ARG	1	0.938	0.976	14.449	0.437	0.437	0.000	0.000	0.000	0.000
37	A	118	ARG	1	0.816	0.882	14.810	0.305	0.305	0.000	0.000	0.000	0.000
38	A	119	ALA	0	0.022	0.010	16.409	-0.026	-0.026	0.000	0.000	0.000	0.000
39	A	120	LEU	0	0.011	-0.008	10.397	-0.017	-0.017	0.000	0.000	0.000	0.000
40	A	121	GLY	0	-0.006	0.015	12.181	-0.099	-0.099	0.000	0.000	0.000	0.000
41	A	122	ASP	-1	-0.811	-0.869	13.665	-0.357	-0.357	0.000	0.000	0.000	0.000
42	A	123	PHE	0	0.015	-0.013	12.013	0.041	0.041	0.000	0.000	0.000	0.000
43	A	124	GLU	-1	-0.792	-0.887	7.601	-1.742	-1.742	0.000	0.000	0.000	0.000
44	A	125	ASN	0	-0.040	-0.028	11.541	0.104	0.104	0.000	0.000	0.000	0.000
45	A	126	MET	0	0.023	0.020	14.617	0.045	0.045	0.000	0.000	0.000	0.000
46	A	127	LEU	0	-0.072	-0.027	8.959	0.019	0.019	0.000	0.000	0.000	0.000
47	A	128	ALA	0	-0.034	-0.015	12.548	0.056	0.056	0.000	0.000	0.000	0.000
48	A	129	ASP	-1	-0.773	-0.852	13.628	-0.200	-0.200	0.000	0.000	0.000	0.000
49	A	130	GLY	0	-0.025	-0.010	15.264	0.037	0.037	0.000	0.000	0.000	0.000
50	A	131	SER	0	-0.027	-0.054	16.282	0.002	0.002	0.000	0.000	0.000	0.000
51	A	132	PHE	0	-0.059	-0.034	12.542	0.005	0.005	0.000	0.000	0.000	0.000
52	A	133	ARG	1	0.929	0.972	14.289	0.201	0.201	0.000	0.000	0.000	0.000
53	A	134	ALA	0	0.022	0.016	17.967	0.013	0.013	0.000	0.000	0.000	0.000
54	A	135	ALA	0	-0.013	0.014	18.530	0.010	0.010	0.000	0.000	0.000	0.000
55	A	136	PRO	0	0.006	-0.009	20.403	0.002	0.002	0.000	0.000	0.000	0.000
56	A	137	LYS	1	0.845	0.915	16.942	0.244	0.244	0.000	0.000	0.000	0.000
57	A	138	SER	0	-0.028	-0.016	19.215	-0.016	-0.016	0.000	0.000	0.000	0.000
58	A	139	TYR	0	-0.051	-0.035	19.806	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	140	PRO	0	0.035	0.019	24.766	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	141	ILE	0	0.003	0.006	24.374	-0.013	-0.013	0.000	0.000	0.000	0.000
61	A	142	PRO	0	0.016	0.001	27.470	0.011	0.011	0.000	0.000	0.000	0.000
62	A	143	HIS	0	-0.027	-0.006	29.627	0.003	0.003	0.000	0.000	0.000	0.000
63	A	144	THR	0	0.032	0.014	33.226	0.010	0.010	0.000	0.000	0.000	0.000
64	A	145	ALA	0	0.034	0.017	34.940	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	146	PHE	0	-0.023	-0.006	36.689	0.000	0.000	0.000	0.000	0.000	0.000
66	A	147	GLU	-1	-0.916	-0.964	31.261	-0.153	-0.153	0.000	0.000	0.000	0.000
67	A	148	LYS	1	0.970	0.983	31.578	0.124	0.124	0.000	0.000	0.000	0.000
68	A	149	SER	0	0.043	0.024	26.646	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	150	ILE	0	0.021	0.013	23.577	0.001	0.001	0.000	0.000	0.000	0.000
70	A	151	ILE	0	-0.038	-0.027	18.553	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	152	VAL	0	0.021	0.029	18.214	0.004	0.004	0.000	0.000	0.000	0.000
72	A	153	GLN	0	0.001	-0.009	15.816	-0.052	-0.052	0.000	0.000	0.000	0.000
73	A	154	THR	0	-0.024	-0.016	12.171	0.067	0.067	0.000	0.000	0.000	0.000
74	A	155	SER	0	-0.029	-0.012	8.565	0.020	0.020	0.000	0.000	0.000	0.000
75	A	156	ARG	1	0.821	0.880	7.739	1.892	1.892	0.000	0.000	0.000	0.000
76	A	157	MET	0	0.017	0.025	4.076	-1.279	-0.790	0.020	-0.190	-0.319	0.000
77	A	158	PHE	0	0.060	0.016	3.059	1.231	2.293	0.020	-0.351	-0.732	0.001
78	A	159	PRO	0	0.042	0.026	2.057	-6.819	-7.355	4.818	-2.089	-2.193	-0.024
79	A	160	VAL	0	0.047	0.015	2.266	-2.540	-1.042	2.742	-0.968	-3.273	0.001
80	A	161	SER	0	0.042	0.035	3.424	-0.478	-0.442	0.011	0.177	-0.224	0.000
81	A	162	LEU	0	0.036	0.017	6.507	-0.032	-0.032	0.000	0.000	0.000	0.000
82	A	163	ILE	0	-0.025	-0.013	2.333	-0.916	-0.213	1.090	-0.292	-1.501	0.001
83	A	164	GLU	-1	-0.915	-0.955	4.819	0.338	0.438	-0.001	-0.002	-0.097	0.000
84	A	165	ALA	0	0.009	0.012	6.487	0.032	0.032	0.000	0.000	0.000	0.000
85	A	166	ALA	0	0.008	0.000	7.305	0.044	0.044	0.000	0.000	0.000	0.000
86	A	167	ARG	1	0.820	0.879	5.700	0.351	0.351	0.000	0.000	0.000	0.000
87	A	168	ASN	0	-0.031	-0.022	8.887	0.065	0.065	0.000	0.000	0.000	0.000
88	A	169	HIS	0	-0.060	-0.023	11.725	0.016	0.016	0.000	0.000	0.000	0.000
89	A	170	PHE	0	-0.001	-0.018	10.446	0.017	0.017	0.000	0.000	0.000	0.000
90	A	171	ASP	-1	-0.768	-0.878	10.470	-0.154	-0.154	0.000	0.000	0.000	0.000
91	A	172	PRO	0	0.012	0.019	12.538	0.026	0.026	0.000	0.000	0.000	0.000
92	A	173	LEU	0	-0.016	-0.011	14.513	0.023	0.023	0.000	0.000	0.000	0.000
93	A	174	GLY	0	0.001	0.022	11.860	0.025	0.025	0.000	0.000	0.000	0.000
94	A	175	LEU	0	-0.024	-0.019	12.922	0.020	0.020	0.000	0.000	0.000	0.000
95	A	176	GLU	-1	-0.883	-0.927	11.633	-0.232	-0.232	0.000	0.000	0.000	0.000
96	A	177	THR	0	0.039	0.017	11.208	-0.019	-0.019	0.000	0.000	0.000	0.000
97	A	178	ALA	0	0.026	0.002	7.441	-0.045	-0.045	0.000	0.000	0.000	0.000
98	A	179	ARG	1	0.963	0.989	8.885	0.196	0.196	0.000	0.000	0.000	0.000
99	A	180	ALA	0	-0.021	0.002	11.587	-0.036	-0.036	0.000	0.000	0.000	0.000
100	A	181	PHE	0	0.057	0.020	5.369	0.008	0.008	0.000	0.000	0.000	0.000
101	A	182	GLY	0	0.065	0.031	9.473	-0.059	-0.059	0.000	0.000	0.000	0.000
102	A	183	HIS	0	-0.028	-0.014	10.078	-0.024	-0.024	0.000	0.000	0.000	0.000
103	A	184	LYS	1	0.801	0.908	12.778	0.275	0.275	0.000	0.000	0.000	0.000
104	A	185	LEU	0	0.023	0.029	7.852	0.026	0.026	0.000	0.000	0.000	0.000
105	A	186	ALA	0	-0.006	-0.012	11.880	0.005	0.005	0.000	0.000	0.000	0.000
106	A	187	THR	0	-0.048	-0.036	13.680	0.055	0.055	0.000	0.000	0.000	0.000
107	A	188	ALA	0	0.041	0.012	14.973	0.037	0.037	0.000	0.000	0.000	0.000
108	A	189	ALA	0	-0.003	0.012	13.820	0.029	0.029	0.000	0.000	0.000	0.000
109	A	190	LEU	0	-0.012	-0.010	15.944	0.037	0.037	0.000	0.000	0.000	0.000
110	A	191	ALA	0	-0.012	0.010	18.875	0.034	0.034	0.000	0.000	0.000	0.000
111	A	192	CYS	0	-0.034	-0.010	18.539	0.040	0.040	0.000	0.000	0.000	0.000
112	A	193	PHE	0	-0.003	-0.002	19.706	0.021	0.021	0.000	0.000	0.000	0.000
113	A	194	PHE	0	0.052	0.003	21.472	0.020	0.020	0.000	0.000	0.000	0.000
114	A	195	ALA	0	0.000	0.011	24.006	0.022	0.022	0.000	0.000	0.000	0.000
115	A	196	ARG	1	0.926	0.953	20.166	0.312	0.312	0.000	0.000	0.000	0.000
116	A	197	GLU	-1	-0.707	-0.797	25.579	-0.192	-0.192	0.000	0.000	0.000	0.000
117	A	198	LYS	1	0.948	0.974	27.447	0.156	0.156	0.000	0.000	0.000	0.000
118	A	199	ALA	0	-0.046	-0.025	28.474	0.012	0.012	0.000	0.000	0.000	0.000
119	A	200	THR	0	-0.036	-0.032	28.705	0.006	0.006	0.000	0.000	0.000	0.000
120	A	201	ASN	0	-0.036	-0.010	31.337	0.005	0.005	0.000	0.000	0.000	0.000
121	A	202	SER	0	-0.025	-0.023	30.216	0.007	0.007	0.000	0.000	0.000	0.000

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