FMO DATABASE

FMODB ID: 52JKZ

Calculation Name: 2R2Y-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2R2Y

Chain ID: A

ChEMBL ID:

UniProt ID: Q9JKV1

Base Structure: X-ray

Registration Date: 2023-06-22

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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-922384.189888
FMO2-HF: Nuclear repulsion	876671.7299
FMO2-HF: Total energy	-45712.459988
FMO2-MP2: Total energy	-45842.491554

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:22:TYR)

Summations of interaction energy for fragment #1(A:22:TYR)

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.
-53.498	-33.261	17.104	-12.563	-24.78	-0.019

Interaction energy analysis for fragmet #1(A:22:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.051 / q_NPA : -0.032

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	24	VAL	0	-0.002	-0.006	3.006	-0.259	1.476	0.024	-0.744	-1.015	0.001
4	A	25	GLU	-1	-0.916	-0.969	2.437	-13.075	-8.054	2.272	-2.969	-4.325	-0.039
5	A	26	PHE	0	0.009	0.005	4.545	0.488	0.563	-0.001	-0.018	-0.055	0.000
6	A	27	ARG	1	0.862	0.911	7.763	0.965	0.965	0.000	0.000	0.000	0.000
7	A	28	ALA	0	0.042	0.007	9.960	-0.045	-0.045	0.000	0.000	0.000	0.000
8	A	29	GLY	0	0.029	0.048	11.034	0.131	0.131	0.000	0.000	0.000	0.000
9	A	30	LYS	1	0.834	0.903	12.526	-0.281	-0.281	0.000	0.000	0.000	0.000
10	A	31	MET	0	-0.051	-0.027	14.945	0.005	0.005	0.000	0.000	0.000	0.000
11	A	32	SER	0	0.003	0.016	18.142	0.001	0.001	0.000	0.000	0.000	0.000
12	A	33	LEU	0	0.044	0.014	20.399	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	34	LYS	1	0.993	1.007	23.762	-0.027	-0.027	0.000	0.000	0.000	0.000
14	A	35	GLY	0	0.021	0.008	25.824	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	36	THR	0	-0.004	-0.017	28.325	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	37	THR	0	-0.037	-0.004	27.582	-0.007	-0.007	0.000	0.000	0.000	0.000
17	A	38	VAL	0	0.010	0.011	22.553	0.010	0.010	0.000	0.000	0.000	0.000
18	A	39	THR	0	-0.034	-0.028	23.274	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	40	PRO	0	-0.019	-0.028	19.835	0.011	0.011	0.000	0.000	0.000	0.000
20	A	41	ASP	-1	-0.804	-0.876	16.085	0.242	0.242	0.000	0.000	0.000	0.000
21	A	42	LYS	1	0.949	0.955	17.582	-0.086	-0.086	0.000	0.000	0.000	0.000
22	A	43	ARG	1	0.751	0.845	13.760	-0.403	-0.403	0.000	0.000	0.000	0.000
23	A	44	LYS	1	0.945	0.978	12.454	-0.229	-0.229	0.000	0.000	0.000	0.000
24	A	45	GLY	0	0.056	0.018	9.621	0.164	0.164	0.000	0.000	0.000	0.000
25	A	46	LEU	0	-0.062	-0.039	2.991	-0.461	0.111	0.134	-0.134	-0.573	0.000
26	A	47	VAL	0	0.015	0.026	6.637	0.466	0.466	0.000	0.000	0.000	0.000
27	A	48	TYR	0	-0.013	-0.022	2.658	-7.964	-2.578	7.821	-2.790	-10.417	-0.002
28	A	49	ILE	0	0.013	0.018	3.322	0.136	0.621	0.005	-0.090	-0.400	0.000
29	A	50	GLN	0	0.016	-0.003	2.641	-9.635	-4.996	2.207	-2.760	-4.086	-0.025
30	A	51	GLN	0	-0.031	-0.008	3.677	-0.524	-0.393	0.013	-0.025	-0.119	0.000
31	A	52	THR	0	-0.072	-0.075	6.420	0.540	0.540	0.000	0.000	0.000	0.000
32	A	53	ASP	-1	-0.860	-0.936	8.769	0.307	0.307	0.000	0.000	0.000	0.000
33	A	54	ASP	-1	-0.829	-0.878	11.860	-0.017	-0.017	0.000	0.000	0.000	0.000
34	A	55	SER	0	-0.038	-0.022	11.851	-0.044	-0.044	0.000	0.000	0.000	0.000
35	A	56	LEU	0	-0.035	0.002	11.970	-0.057	-0.057	0.000	0.000	0.000	0.000
36	A	57	ILE	0	0.015	0.003	7.875	0.051	0.051	0.000	0.000	0.000	0.000
37	A	58	HIS	1	0.817	0.893	6.887	0.395	0.395	0.000	0.000	0.000	0.000
38	A	59	PHE	0	0.021	0.003	6.927	-0.129	-0.129	0.000	0.000	0.000	0.000
39	A	60	CYS	0	-0.039	-0.024	5.506	-0.165	-0.165	0.000	0.000	0.000	0.000
40	A	61	TRP	0	-0.062	-0.045	7.471	0.119	0.119	0.000	0.000	0.000	0.000
41	A	62	LYS	1	0.905	0.957	1.989	-24.153	-22.197	4.628	-2.991	-3.593	0.046
42	A	63	ASP	-1	-0.733	-0.830	7.004	0.457	0.457	0.000	0.000	0.000	0.000
43	A	64	ARG	1	0.877	0.930	7.218	-0.028	-0.028	0.000	0.000	0.000	0.000
44	A	65	THR	0	-0.097	-0.061	9.138	-0.046	-0.046	0.000	0.000	0.000	0.000
45	A	66	SER	0	-0.034	-0.027	11.401	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	67	GLY	0	-0.013	0.010	7.525	0.002	0.002	0.000	0.000	0.000	0.000
47	A	68	THR	0	0.000	-0.017	6.558	0.677	0.677	0.000	0.000	0.000	0.000
48	A	69	VAL	0	-0.003	-0.008	3.547	0.172	0.409	0.001	-0.042	-0.197	0.000
49	A	70	GLU	-1	-0.825	-0.874	6.624	0.137	0.137	0.000	0.000	0.000	0.000
50	A	71	ASP	-1	-0.848	-0.908	8.873	0.073	0.073	0.000	0.000	0.000	0.000
51	A	72	ASP	-1	-0.788	-0.884	7.942	-0.688	-0.688	0.000	0.000	0.000	0.000
52	A	73	LEU	0	-0.058	-0.030	9.410	0.111	0.111	0.000	0.000	0.000	0.000
53	A	74	ILE	0	0.041	0.034	11.463	-0.070	-0.070	0.000	0.000	0.000	0.000
54	A	75	ILE	0	-0.083	-0.049	12.102	0.020	0.020	0.000	0.000	0.000	0.000
55	A	76	PHE	0	0.001	0.001	13.121	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	77	PRO	0	0.037	0.008	15.178	-0.018	-0.018	0.000	0.000	0.000	0.000
57	A	78	ASP	-1	-0.834	-0.907	17.041	-0.194	-0.194	0.000	0.000	0.000	0.000
58	A	79	ASP	-1	-0.836	-0.893	17.058	-0.181	-0.181	0.000	0.000	0.000	0.000
59	A	80	CYS	0	-0.114	-0.056	16.063	0.022	0.022	0.000	0.000	0.000	0.000
60	A	81	GLU	-1	-0.853	-0.911	17.547	-0.275	-0.275	0.000	0.000	0.000	0.000
61	A	82	PHE	0	-0.026	-0.005	13.332	0.023	0.023	0.000	0.000	0.000	0.000
62	A	83	LYS	1	0.905	0.940	16.200	0.231	0.231	0.000	0.000	0.000	0.000
63	A	84	ARG	1	0.924	0.970	18.786	0.255	0.255	0.000	0.000	0.000	0.000
64	A	85	VAL	0	-0.011	-0.020	20.291	0.021	0.021	0.000	0.000	0.000	0.000
65	A	86	PRO	0	-0.019	-0.003	23.108	0.006	0.006	0.000	0.000	0.000	0.000
66	A	87	GLN	0	0.038	0.000	25.787	-0.008	-0.008	0.000	0.000	0.000	0.000
67	A	88	CYS	0	-0.018	0.015	24.358	0.016	0.016	0.000	0.000	0.000	0.000
68	A	89	PRO	0	0.056	0.014	26.078	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	90	SER	0	-0.011	0.006	23.222	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	91	GLY	0	0.021	0.021	23.336	-0.015	-0.015	0.000	0.000	0.000	0.000
71	A	92	ARG	1	0.750	0.812	16.777	0.300	0.300	0.000	0.000	0.000	0.000
72	A	93	VAL	0	-0.006	0.008	18.221	-0.014	-0.014	0.000	0.000	0.000	0.000
73	A	94	TYR	0	-0.037	-0.047	16.153	-0.014	-0.014	0.000	0.000	0.000	0.000
74	A	95	VAL	0	-0.066	-0.036	18.076	0.042	0.042	0.000	0.000	0.000	0.000
75	A	96	LEU	0	0.064	0.047	13.432	-0.027	-0.027	0.000	0.000	0.000	0.000
76	A	97	LYS	1	0.788	0.879	16.787	0.200	0.200	0.000	0.000	0.000	0.000
77	A	98	PHE	0	0.144	0.039	16.648	-0.018	-0.018	0.000	0.000	0.000	0.000
78	A	99	LYS	1	0.824	0.912	20.179	0.274	0.274	0.000	0.000	0.000	0.000
79	A	100	ALA	0	0.076	0.039	23.343	0.015	0.015	0.000	0.000	0.000	0.000
80	A	101	GLY	0	0.024	0.002	24.181	-0.004	-0.004	0.000	0.000	0.000	0.000
81	A	102	SER	0	-0.057	-0.028	24.668	0.003	0.003	0.000	0.000	0.000	0.000
82	A	103	LYS	1	0.946	1.001	17.000	0.138	0.138	0.000	0.000	0.000	0.000
83	A	104	ARG	1	0.894	0.947	20.457	0.101	0.101	0.000	0.000	0.000	0.000
84	A	105	LEU	0	0.022	0.025	14.526	0.025	0.025	0.000	0.000	0.000	0.000
85	A	106	PHE	0	0.021	0.002	17.408	-0.036	-0.036	0.000	0.000	0.000	0.000
86	A	107	PHE	0	0.024	0.006	12.332	0.021	0.021	0.000	0.000	0.000	0.000
87	A	108	TRP	0	-0.041	-0.020	15.566	-0.026	-0.026	0.000	0.000	0.000	0.000
88	A	109	MET	0	-0.028	0.007	12.891	0.015	0.015	0.000	0.000	0.000	0.000
89	A	110	GLN	0	-0.061	-0.049	12.888	0.082	0.082	0.000	0.000	0.000	0.000
90	A	111	GLU	-1	-0.757	-0.848	10.640	-0.708	-0.708	0.000	0.000	0.000	0.000
91	A	112	PRO	0	-0.042	-0.020	14.561	0.033	0.033	0.000	0.000	0.000	0.000
92	A	113	LYS	1	0.841	0.898	17.442	0.322	0.322	0.000	0.000	0.000	0.000
93	A	114	THR	0	0.041	0.012	17.536	-0.033	-0.033	0.000	0.000	0.000	0.000
94	A	115	ASP	-1	-0.865	-0.910	18.495	-0.361	-0.361	0.000	0.000	0.000	0.000
95	A	116	GLN	0	0.049	0.020	12.949	-0.115	-0.115	0.000	0.000	0.000	0.000
96	A	117	ASP	-1	-0.751	-0.830	14.518	-0.482	-0.482	0.000	0.000	0.000	0.000
97	A	118	GLU	-1	-0.770	-0.899	15.105	-0.459	-0.459	0.000	0.000	0.000	0.000
98	A	119	GLU	-1	-0.827	-0.874	13.111	-0.759	-0.759	0.000	0.000	0.000	0.000
99	A	120	HIS	0	0.038	0.010	10.628	-0.186	-0.186	0.000	0.000	0.000	0.000
100	A	121	CYS	0	-0.081	-0.024	11.427	-0.029	-0.029	0.000	0.000	0.000	0.000
101	A	122	ARG	1	0.884	0.929	13.966	0.579	0.579	0.000	0.000	0.000	0.000
102	A	123	LYS	1	0.881	0.922	9.099	1.076	1.076	0.000	0.000	0.000	0.000
103	A	124	VAL	0	-0.006	0.000	9.311	-0.102	-0.102	0.000	0.000	0.000	0.000
104	A	125	ASN	0	-0.038	-0.039	10.603	0.102	0.102	0.000	0.000	0.000	0.000
105	A	126	GLU	-1	-0.828	-0.902	12.095	-0.797	-0.797	0.000	0.000	0.000	0.000
106	A	127	CYS	0	-0.011	-0.003	7.981	-0.053	-0.053	0.000	0.000	0.000	0.000
107	A	128	LEU	0	-0.046	-0.017	9.918	0.112	0.112	0.000	0.000	0.000	0.000
108	A	129	ASN	0	-0.059	-0.041	11.948	0.129	0.129	0.000	0.000	0.000	0.000
109	A	130	ASN	0	-0.027	0.002	11.296	0.035	0.035	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:TYR)