FMO DATABASE

FMODB ID: K9G63

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	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. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-920704.574702
FMO2-HF: Nuclear repulsion	874993.02488
FMO2-HF: Total energy	-45711.549823
FMO2-MP2: Total energy	-45841.616987

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.
-31.27	-14.815	10.085	-8.551	-17.987	-0.046

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 : -0.068 / q_NPA : -0.050

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	-0.015	-0.012	2.799	-0.505	1.413	0.072	-0.825	-1.165	0.001
4	A	25	GLU	-1	-0.915	-0.972	2.231	-13.812	-10.385	5.181	-3.409	-5.199	-0.044
5	A	26	PHE	0	-0.008	-0.001	4.377	0.443	0.552	0.000	-0.032	-0.077	0.000
6	A	27	ARG	1	0.900	0.951	7.379	0.987	0.987	0.000	0.000	0.000	0.000
7	A	28	ALA	0	0.035	0.005	9.740	-0.060	-0.060	0.000	0.000	0.000	0.000
8	A	29	GLY	0	0.040	0.042	11.329	0.144	0.144	0.000	0.000	0.000	0.000
9	A	30	LYS	1	0.884	0.941	13.767	-0.365	-0.365	0.000	0.000	0.000	0.000
10	A	31	MET	0	-0.037	-0.022	15.434	-0.019	-0.019	0.000	0.000	0.000	0.000
11	A	32	SER	0	-0.010	0.008	18.832	0.017	0.017	0.000	0.000	0.000	0.000
12	A	33	LEU	0	0.029	0.010	21.242	-0.015	-0.015	0.000	0.000	0.000	0.000
13	A	34	LYS	1	0.978	0.998	24.736	-0.051	-0.051	0.000	0.000	0.000	0.000
14	A	35	GLY	0	0.019	-0.004	26.838	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	36	THR	0	0.021	0.007	29.325	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	37	THR	0	-0.014	-0.007	27.931	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	38	VAL	0	-0.007	0.013	23.100	0.012	0.012	0.000	0.000	0.000	0.000
18	A	39	THR	0	-0.032	-0.024	23.819	-0.012	-0.012	0.000	0.000	0.000	0.000
19	A	40	PRO	0	0.009	-0.013	20.502	0.016	0.016	0.000	0.000	0.000	0.000
20	A	41	ASP	-1	-0.833	-0.884	17.038	0.235	0.235	0.000	0.000	0.000	0.000
21	A	42	LYS	1	0.960	0.954	17.861	-0.084	-0.084	0.000	0.000	0.000	0.000
22	A	43	ARG	1	0.726	0.829	14.434	-0.390	-0.390	0.000	0.000	0.000	0.000
23	A	44	LYS	1	0.938	0.970	12.328	-0.148	-0.148	0.000	0.000	0.000	0.000
24	A	45	GLY	0	0.059	0.019	9.808	0.129	0.129	0.000	0.000	0.000	0.000
25	A	46	LEU	0	-0.087	-0.039	2.839	-0.558	0.055	0.252	-0.176	-0.688	0.001
26	A	47	VAL	0	0.023	0.027	6.887	0.585	0.585	0.000	0.000	0.000	0.000
27	A	48	TYR	0	0.002	-0.010	2.475	-5.874	-0.765	3.539	-1.667	-6.981	0.006
28	A	49	ILE	0	0.006	0.014	3.112	0.201	0.803	0.017	-0.141	-0.479	0.000
29	A	50	GLN	0	0.032	0.011	2.704	-6.075	-2.380	0.995	-1.951	-2.739	-0.012
30	A	51	GLN	0	-0.039	-0.014	3.690	-0.582	-0.455	0.011	-0.017	-0.120	0.000
31	A	52	THR	0	-0.051	-0.041	6.487	0.549	0.549	0.000	0.000	0.000	0.000
32	A	53	ASP	-1	-0.907	-0.961	8.782	0.491	0.491	0.000	0.000	0.000	0.000
33	A	54	ASP	-1	-0.812	-0.881	11.820	0.273	0.273	0.000	0.000	0.000	0.000
34	A	55	SER	0	-0.069	-0.042	11.509	-0.074	-0.074	0.000	0.000	0.000	0.000
35	A	56	LEU	0	-0.016	0.008	11.779	-0.082	-0.082	0.000	0.000	0.000	0.000
36	A	57	ILE	0	0.027	0.016	7.897	0.133	0.133	0.000	0.000	0.000	0.000
37	A	58	HIS	1	0.820	0.886	7.101	-0.408	-0.408	0.000	0.000	0.000	0.000
38	A	59	PHE	0	0.012	0.001	7.114	0.022	0.022	0.000	0.000	0.000	0.000
39	A	60	CYS	0	-0.020	-0.015	5.757	-0.033	-0.033	0.000	0.000	0.000	0.000
40	A	61	TRP	0	-0.039	-0.023	8.151	-0.007	-0.007	0.000	0.000	0.000	0.000
41	A	62	LYS	1	0.911	0.967	3.435	-7.174	-6.319	0.018	-0.333	-0.539	0.002
42	A	63	ASP	-1	-0.791	-0.905	7.510	0.313	0.313	0.000	0.000	0.000	0.000
43	A	64	ARG	1	0.898	0.932	7.526	-0.101	-0.101	0.000	0.000	0.000	0.000
44	A	65	THR	0	-0.061	-0.020	9.458	0.005	0.005	0.000	0.000	0.000	0.000
45	A	66	SER	0	-0.001	-0.003	12.127	0.040	0.040	0.000	0.000	0.000	0.000
46	A	67	GLY	0	-0.001	0.005	7.925	-0.011	-0.011	0.000	0.000	0.000	0.000
47	A	68	THR	0	0.024	0.008	7.197	0.257	0.257	0.000	0.000	0.000	0.000
48	A	69	VAL	0	-0.013	-0.012	5.112	0.239	0.239	0.000	0.000	0.000	0.000
49	A	70	GLU	-1	-0.831	-0.887	7.985	0.234	0.234	0.000	0.000	0.000	0.000
50	A	71	ASP	-1	-0.878	-0.917	10.349	0.224	0.224	0.000	0.000	0.000	0.000
51	A	72	ASP	-1	-0.799	-0.892	9.371	0.440	0.440	0.000	0.000	0.000	0.000
52	A	73	LEU	0	-0.066	-0.034	10.616	-0.069	-0.069	0.000	0.000	0.000	0.000
53	A	74	ILE	0	0.037	0.024	11.723	-0.010	-0.010	0.000	0.000	0.000	0.000
54	A	75	ILE	0	-0.086	-0.045	12.320	-0.022	-0.022	0.000	0.000	0.000	0.000
55	A	76	PHE	0	0.007	0.002	13.198	0.005	0.005	0.000	0.000	0.000	0.000
56	A	77	PRO	0	0.042	0.014	15.464	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	78	ASP	-1	-0.930	-0.959	16.932	-0.128	-0.128	0.000	0.000	0.000	0.000
58	A	79	ASP	-1	-0.860	-0.914	17.191	-0.024	-0.024	0.000	0.000	0.000	0.000
59	A	80	CYS	0	-0.106	-0.062	15.498	0.025	0.025	0.000	0.000	0.000	0.000
60	A	81	GLU	-1	-0.952	-0.973	17.224	-0.238	-0.238	0.000	0.000	0.000	0.000
61	A	82	PHE	0	-0.050	-0.021	13.031	0.043	0.043	0.000	0.000	0.000	0.000
62	A	83	LYS	1	0.992	0.988	15.940	0.154	0.154	0.000	0.000	0.000	0.000
63	A	84	ARG	1	0.994	1.011	18.669	0.244	0.244	0.000	0.000	0.000	0.000
64	A	85	VAL	0	-0.026	-0.031	20.207	0.022	0.022	0.000	0.000	0.000	0.000
65	A	86	PRO	0	-0.012	-0.005	23.026	0.002	0.002	0.000	0.000	0.000	0.000
66	A	87	GLN	0	-0.003	-0.014	25.901	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	88	CYS	0	-0.021	0.013	24.438	0.016	0.016	0.000	0.000	0.000	0.000
68	A	89	PRO	0	0.068	0.018	26.119	-0.015	-0.015	0.000	0.000	0.000	0.000
69	A	90	SER	0	-0.022	0.001	22.392	-0.013	-0.013	0.000	0.000	0.000	0.000
70	A	91	GLY	0	0.007	0.004	23.340	-0.015	-0.015	0.000	0.000	0.000	0.000
71	A	92	ARG	1	0.771	0.849	16.601	0.292	0.292	0.000	0.000	0.000	0.000
72	A	93	VAL	0	-0.010	-0.001	18.104	-0.013	-0.013	0.000	0.000	0.000	0.000
73	A	94	TYR	0	-0.015	-0.018	15.877	-0.015	-0.015	0.000	0.000	0.000	0.000
74	A	95	VAL	0	-0.078	-0.046	17.843	0.045	0.045	0.000	0.000	0.000	0.000
75	A	96	LEU	0	0.054	0.043	13.212	-0.038	-0.038	0.000	0.000	0.000	0.000
76	A	97	LYS	1	0.875	0.921	16.534	0.130	0.130	0.000	0.000	0.000	0.000
77	A	98	PHE	0	0.079	0.029	16.064	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	99	LYS	1	0.901	0.940	20.217	0.172	0.172	0.000	0.000	0.000	0.000
79	A	100	ALA	0	0.042	0.031	23.090	0.004	0.004	0.000	0.000	0.000	0.000
80	A	101	GLY	0	0.043	0.016	24.332	0.008	0.008	0.000	0.000	0.000	0.000
81	A	102	SER	0	-0.101	-0.052	24.693	0.000	0.000	0.000	0.000	0.000	0.000
82	A	103	LYS	1	1.009	1.025	18.398	-0.068	-0.068	0.000	0.000	0.000	0.000
83	A	104	ARG	1	0.916	0.955	20.298	0.037	0.037	0.000	0.000	0.000	0.000
84	A	105	LEU	0	0.024	0.027	15.486	0.024	0.024	0.000	0.000	0.000	0.000
85	A	106	PHE	0	0.008	-0.001	17.506	-0.039	-0.039	0.000	0.000	0.000	0.000
86	A	107	PHE	0	0.034	0.012	12.907	0.031	0.031	0.000	0.000	0.000	0.000
87	A	108	TRP	0	-0.049	-0.018	15.652	-0.047	-0.047	0.000	0.000	0.000	0.000
88	A	109	MET	0	-0.005	0.016	12.825	0.019	0.019	0.000	0.000	0.000	0.000
89	A	110	GLN	0	-0.045	-0.042	12.744	0.067	0.067	0.000	0.000	0.000	0.000
90	A	111	GLU	-1	-0.852	-0.921	10.011	-0.955	-0.955	0.000	0.000	0.000	0.000
91	A	112	PRO	0	-0.024	-0.001	14.523	0.034	0.034	0.000	0.000	0.000	0.000
92	A	113	LYS	1	0.946	0.968	17.757	0.330	0.330	0.000	0.000	0.000	0.000
93	A	114	THR	0	0.036	0.003	17.435	-0.034	-0.034	0.000	0.000	0.000	0.000
94	A	115	ASP	-1	-0.896	-0.940	18.502	-0.393	-0.393	0.000	0.000	0.000	0.000
95	A	116	GLN	0	0.009	-0.004	12.787	-0.124	-0.124	0.000	0.000	0.000	0.000
96	A	117	ASP	-1	-0.755	-0.848	14.481	-0.510	-0.510	0.000	0.000	0.000	0.000
97	A	118	GLU	-1	-0.868	-0.947	14.957	-0.422	-0.422	0.000	0.000	0.000	0.000
98	A	119	GLU	-1	-0.816	-0.910	12.899	-0.876	-0.876	0.000	0.000	0.000	0.000
99	A	120	HIS	0	0.012	0.008	10.055	-0.210	-0.210	0.000	0.000	0.000	0.000
100	A	121	CYS	0	-0.068	-0.028	11.003	-0.025	-0.025	0.000	0.000	0.000	0.000
101	A	122	ARG	1	0.922	0.950	13.353	0.604	0.604	0.000	0.000	0.000	0.000
102	A	123	LYS	1	0.973	1.001	8.861	1.714	1.714	0.000	0.000	0.000	0.000
103	A	124	VAL	0	-0.008	0.002	8.704	-0.058	-0.058	0.000	0.000	0.000	0.000
104	A	125	ASN	0	-0.007	-0.018	10.199	0.138	0.138	0.000	0.000	0.000	0.000
105	A	126	GLU	-1	-0.920	-0.956	11.999	-0.728	-0.728	0.000	0.000	0.000	0.000
106	A	127	CYS	0	-0.057	-0.021	7.897	-0.154	-0.154	0.000	0.000	0.000	0.000
107	A	128	LEU	0	-0.068	-0.033	9.951	0.153	0.153	0.000	0.000	0.000	0.000
108	A	129	ASN	0	-0.010	-0.005	12.047	0.133	0.133	0.000	0.000	0.000	0.000
109	A	130	ASN	0	-0.016	0.020	11.557	0.044	0.044	0.000	0.000	0.000	0.000

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