FMO DATABASE

FMODB ID: KR1N3

Calculation Name: 2QYA-A-Xray316

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QYA

Chain ID: A

ChEMBL ID:

UniProt ID: Q8TWR4

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	117
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-859473.966414
FMO2-HF: Nuclear repulsion	815003.163571
FMO2-HF: Total energy	-44470.802842
FMO2-MP2: Total energy	-44599.911115

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:1:ACE )

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

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.
-1.619	-0.813	-0.004	-0.37	-0.432	-0.001

Interaction energy analysis for fragmet #1(A:1:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.038 / q_NPA : -0.030

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	3	ARG	1	0.893	0.963	3.841	0.957	1.763	-0.004	-0.370	-0.432	-0.001
4	A	4	VAL	0	0.038	0.021	6.315	0.056	0.056	0.000	0.000	0.000	0.000
5	A	5	LEU	0	-0.034	-0.016	10.080	0.136	0.136	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.004	0.005	12.727	-0.003	-0.003	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.028	-0.015	15.769	0.045	0.045	0.000	0.000	0.000	0.000
8	A	8	ILE	0	0.005	0.011	18.992	-0.009	-0.009	0.000	0.000	0.000	0.000
9	A	9	HIS	0	0.002	0.010	22.110	0.012	0.012	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.045	0.029	25.544	-0.006	-0.006	0.000	0.000	0.000	0.000
11	A	11	THR	0	-0.055	-0.041	29.008	0.006	0.006	0.000	0.000	0.000	0.000
12	A	12	GLY	0	0.004	0.004	32.192	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	13	ASP	-1	-0.912	-0.956	35.421	-0.036	-0.036	0.000	0.000	0.000	0.000
14	A	14	THR	0	-0.022	-0.002	29.809	-0.003	-0.003	0.000	0.000	0.000	0.000
15	A	15	VAL	0	0.022	0.007	25.980	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	VAL	0	-0.020	-0.004	24.025	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	17	LEU	0	-0.002	-0.006	21.204	0.003	0.003	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.006	-0.008	20.090	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.006	-0.013	15.136	0.001	0.001	0.000	0.000	0.000	0.000
20	A	20	CYS	0	-0.015	-0.014	14.223	0.026	0.026	0.000	0.000	0.000	0.000
21	A	21	ASP	-1	-0.756	-0.862	10.768	-0.725	-0.725	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.848	-0.894	6.581	-0.238	-0.238	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.946	-0.973	8.430	-0.774	-0.774	0.000	0.000	0.000	0.000
24	A	24	LEU	0	0.003	0.002	10.141	0.105	0.105	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.039	-0.019	13.037	0.066	0.066	0.000	0.000	0.000	0.000
26	A	26	GLY	0	-0.032	-0.014	14.912	0.011	0.011	0.000	0.000	0.000	0.000
27	A	27	VAL	0	-0.010	0.016	16.502	0.021	0.021	0.000	0.000	0.000	0.000
28	A	28	GLU	-1	-0.935	-0.987	18.499	-0.084	-0.084	0.000	0.000	0.000	0.000
29	A	29	LEU	0	0.014	0.014	18.768	-0.005	-0.005	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.948	0.975	22.839	0.110	0.110	0.000	0.000	0.000	0.000
31	A	31	TYR	0	0.072	0.021	26.116	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.963	0.973	28.216	0.096	0.096	0.000	0.000	0.000	0.000
33	A	33	GLY	0	-0.004	0.008	31.646	0.005	0.005	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.920	0.973	29.233	0.095	0.095	0.000	0.000	0.000	0.000
35	A	35	THR	0	0.008	-0.015	26.466	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.064	-0.008	22.207	0.010	0.010	0.000	0.000	0.000	0.000
37	A	37	HIS	0	0.020	0.004	22.966	-0.005	-0.005	0.000	0.000	0.000	0.000
38	A	38	ILE	0	0.001	0.014	17.091	0.011	0.011	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.032	-0.019	18.908	0.003	0.003	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.859	-0.943	18.202	-0.049	-0.049	0.000	0.000	0.000	0.000
41	A	41	PRO	0	-0.046	-0.018	19.848	0.002	0.002	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.023	-0.011	22.446	0.003	0.003	0.000	0.000	0.000	0.000
43	A	43	TYR	0	-0.028	-0.012	17.285	-0.011	-0.011	0.000	0.000	0.000	0.000
44	A	44	SER	0	0.062	-0.028	16.225	0.001	0.001	0.000	0.000	0.000	0.000
45	A	45	GLY	0	0.002	0.051	15.148	0.018	0.018	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.918	0.954	13.611	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.028	-0.057	8.137	-0.034	-0.034	0.000	0.000	0.000	0.000
48	A	48	MET	0	-0.156	-0.085	9.503	0.150	0.150	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.859	-0.930	5.278	-0.873	-0.873	0.000	0.000	0.000	0.000
50	A	50	PRO	0	0.085	0.041	7.227	0.167	0.167	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.802	-0.887	10.536	-0.179	-0.179	0.000	0.000	0.000	0.000
52	A	52	ARG	1	0.839	0.908	11.621	0.056	0.056	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.018	-0.016	12.576	0.038	0.038	0.000	0.000	0.000	0.000
54	A	54	ALA	0	0.112	0.055	14.366	0.033	0.033	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.830	0.916	16.236	0.060	0.060	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.913	0.944	16.901	0.050	0.050	0.000	0.000	0.000	0.000
57	A	57	ILE	0	0.020	0.021	17.653	0.012	0.012	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.923	0.960	18.485	0.145	0.145	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.915	-0.961	21.428	-0.032	-0.032	0.000	0.000	0.000	0.000
60	A	60	ALA	0	0.028	0.023	23.078	0.007	0.007	0.000	0.000	0.000	0.000
61	A	61	VAL	0	-0.022	-0.021	24.548	0.004	0.004	0.000	0.000	0.000	0.000
62	A	62	GLN	0	-0.021	-0.011	26.589	0.004	0.004	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.999	-0.990	26.891	-0.031	-0.031	0.000	0.000	0.000	0.000
64	A	64	TYR	0	0.003	-0.015	27.072	0.005	0.005	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.903	-0.934	31.057	-0.048	-0.048	0.000	0.000	0.000	0.000
66	A	66	ASP	-1	-0.806	-0.877	32.612	-0.038	-0.038	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.991	-1.009	34.391	-0.028	-0.028	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.793	0.900	31.842	0.038	0.038	0.000	0.000	0.000	0.000
69	A	69	THR	0	0.015	0.013	31.641	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	70	VAL	0	0.004	0.004	26.275	0.000	0.000	0.000	0.000	0.000	0.000
71	A	71	ALA	0	-0.027	-0.013	27.581	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	72	ILE	0	0.010	-0.002	21.557	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	73	ASN	0	0.000	-0.010	22.065	0.009	0.009	0.000	0.000	0.000	0.000
74	A	74	ALA	0	-0.013	0.003	17.830	-0.007	-0.007	0.000	0.000	0.000	0.000
75	A	75	LEU	0	0.000	0.001	17.516	0.016	0.016	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.052	0.003	14.531	-0.035	-0.035	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.925	-0.954	13.034	-0.523	-0.523	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.011	0.000	7.743	0.021	0.021	0.000	0.000	0.000	0.000
79	A	79	ALA	0	0.004	-0.011	11.926	0.082	0.082	0.000	0.000	0.000	0.000
80	A	80	CYS	0	-0.030	-0.014	14.394	0.072	0.072	0.000	0.000	0.000	0.000
81	A	81	SER	0	-0.021	-0.008	13.357	0.035	0.035	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.005	0.004	13.012	0.036	0.036	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.031	-0.018	15.556	0.047	0.047	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.002	0.006	18.743	0.028	0.028	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.930	-0.963	16.343	-0.214	-0.214	0.000	0.000	0.000	0.000
86	A	86	ALA	0	-0.076	-0.038	18.379	0.028	0.028	0.000	0.000	0.000	0.000
87	A	87	GLY	0	-0.055	-0.023	20.248	0.022	0.022	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.062	-0.032	22.237	0.013	0.013	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.015	0.007	23.056	0.008	0.008	0.000	0.000	0.000	0.000
90	A	90	ARG	1	0.860	0.910	23.493	0.106	0.106	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.902	-0.964	20.633	-0.232	-0.232	0.000	0.000	0.000	0.000
92	A	92	ASP	-1	-0.918	-0.951	23.105	-0.134	-0.134	0.000	0.000	0.000	0.000
93	A	93	GLU	-1	-0.922	-0.956	25.683	-0.114	-0.114	0.000	0.000	0.000	0.000
94	A	94	ILE	0	-0.087	-0.021	20.207	0.000	0.000	0.000	0.000	0.000	0.000
95	A	95	GLY	0	0.013	0.011	23.586	0.009	0.009	0.000	0.000	0.000	0.000
96	A	96	GLU	-1	-0.879	-0.964	22.479	-0.205	-0.205	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.061	-0.043	22.443	0.025	0.025	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.042	-0.028	22.445	-0.009	-0.009	0.000	0.000	0.000	0.000
99	A	99	GLY	0	-0.050	-0.018	22.165	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	100	VAL	0	-0.024	0.003	16.894	-0.028	-0.028	0.000	0.000	0.000	0.000
101	A	101	PRO	0	0.038	0.030	17.069	0.031	0.031	0.000	0.000	0.000	0.000
102	A	102	HIS	0	-0.006	-0.013	19.051	-0.014	-0.014	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.060	0.033	21.069	0.012	0.012	0.000	0.000	0.000	0.000
104	A	104	GLN	0	-0.011	-0.003	22.967	-0.007	-0.007	0.000	0.000	0.000	0.000
105	A	105	MET	0	-0.024	-0.002	24.862	0.003	0.003	0.000	0.000	0.000	0.000
106	A	106	TYR	0	-0.026	-0.016	27.541	0.001	0.001	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.008	0.007	26.737	0.001	0.001	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.031	-0.018	30.971	0.002	0.002	0.000	0.000	0.000	0.000
109	A	109	PRO	0	0.028	0.016	34.258	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	110	ARG	1	0.807	0.890	35.183	0.041	0.041	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.947	-0.976	37.686	-0.036	-0.036	0.000	0.000	0.000	0.000
112	A	112	PRO	0	-0.010	0.000	41.371	0.001	0.001	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.045	-0.013	39.370	0.001	0.001	0.000	0.000	0.000	0.000
114	A	114	LEU	0	-0.040	-0.020	44.336	0.001	0.001	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.877	-0.944	41.901	-0.023	-0.023	0.000	0.000	0.000	0.000
116	A	116	GLY	0	-0.050	-0.020	46.431	0.001	0.001	0.000	0.000	0.000	0.000
117	A	117	NME	0	-0.039	-0.020	48.876	0.001	0.001	0.000	0.000	0.000	0.000

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