FMO DATABASE

FMODB ID: YVZR2

Calculation Name: 2QYZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QYZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q892G2

Base Structure: X-ray

Registration Date: 2023-09-21

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	127
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1112044.785937
FMO2-HF: Nuclear repulsion	1058903.741618
FMO2-HF: Total energy	-53141.044318
FMO2-MP2: Total energy	-53292.926768

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:4:ASN)

Summations of interaction energy for fragment #1(A:4:ASN)

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.
-1.662	0.427	0.002	-1.059	-1.032	0.003

Interaction energy analysis for fragmet #1(A:4:ASN)

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 : 0.008

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	6	GLU	-1	-0.784	-0.871	3.603	-4.225	-2.236	0.003	-1.054	-0.938	0.003
4	A	7	VAL	0	-0.042	-0.026	4.674	0.588	0.688	-0.001	-0.005	-0.094	0.000
5	A	8	LYS	1	0.809	0.884	7.384	0.429	0.429	0.000	0.000	0.000	0.000
6	A	9	PHE	0	0.021	-0.008	10.943	0.076	0.076	0.000	0.000	0.000	0.000
7	A	10	ARG	1	0.782	0.867	14.600	-0.090	-0.090	0.000	0.000	0.000	0.000
8	A	11	ALA	0	0.003	-0.012	18.191	0.043	0.043	0.000	0.000	0.000	0.000
9	A	12	TRP	0	0.057	0.019	21.257	-0.027	-0.027	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.766	-0.868	24.913	0.086	0.086	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.817	0.908	27.383	-0.151	-0.151	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.904	-0.943	30.211	0.086	0.086	0.000	0.000	0.000	0.000
13	A	16	LEU	0	-0.092	-0.065	30.308	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	17	ASN	0	-0.119	-0.045	30.985	-0.009	-0.009	0.000	0.000	0.000	0.000
15	A	18	MET	0	0.024	0.028	27.214	-0.011	-0.011	0.000	0.000	0.000	0.000
16	A	19	MET	0	-0.048	0.012	22.686	0.021	0.021	0.000	0.000	0.000	0.000
17	A	20	VAL	0	-0.055	-0.013	21.311	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	21	TYR	0	-0.029	-0.030	18.466	0.016	0.016	0.000	0.000	0.000	0.000
19	A	22	THR	0	-0.098	-0.069	17.168	-0.019	-0.019	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.867	0.913	19.381	0.050	0.050	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.706	-0.819	22.189	-0.055	-0.055	0.000	0.000	0.000	0.000
22	A	25	GLN	0	0.002	-0.006	24.828	0.015	0.015	0.000	0.000	0.000	0.000
23	A	26	THR	0	-0.048	-0.031	25.095	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	27	GLY	0	0.026	0.009	26.580	0.007	0.007	0.000	0.000	0.000	0.000
25	A	28	HIS	0	-0.082	-0.048	25.778	-0.013	-0.013	0.000	0.000	0.000	0.000
26	A	29	ILE	0	0.002	0.002	21.053	0.007	0.007	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.920	-0.946	23.800	0.136	0.136	0.000	0.000	0.000	0.000
28	A	31	TYR	0	0.046	0.014	22.284	0.004	0.004	0.000	0.000	0.000	0.000
29	A	32	ASN	0	-0.058	-0.022	23.472	0.006	0.006	0.000	0.000	0.000	0.000
30	A	33	THR	0	-0.027	-0.038	20.518	0.010	0.010	0.000	0.000	0.000	0.000
31	A	34	ASN	0	-0.011	0.008	16.970	0.051	0.051	0.000	0.000	0.000	0.000
32	A	35	PRO	0	0.058	0.009	13.880	-0.006	-0.006	0.000	0.000	0.000	0.000
33	A	36	ALA	0	0.015	0.015	13.134	-0.006	-0.006	0.000	0.000	0.000	0.000
34	A	37	ASP	-1	-0.852	-0.911	14.440	0.402	0.402	0.000	0.000	0.000	0.000
35	A	38	THR	0	0.016	0.003	17.596	-0.041	-0.041	0.000	0.000	0.000	0.000
36	A	39	ILE	0	-0.028	-0.011	11.911	-0.027	-0.027	0.000	0.000	0.000	0.000
37	A	40	ASN	0	-0.019	-0.011	15.714	0.002	0.002	0.000	0.000	0.000	0.000
38	A	41	ILE	0	0.008	0.015	17.604	-0.029	-0.029	0.000	0.000	0.000	0.000
39	A	42	ILE	0	0.004	0.001	18.656	-0.022	-0.022	0.000	0.000	0.000	0.000
40	A	43	LEU	0	-0.058	-0.034	14.302	-0.016	-0.016	0.000	0.000	0.000	0.000
41	A	44	ASN	0	-0.075	-0.049	19.030	-0.014	-0.014	0.000	0.000	0.000	0.000
42	A	45	GLN	0	-0.047	-0.012	22.241	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	46	ASP	-1	-0.875	-0.946	24.919	0.168	0.168	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.902	-0.945	26.529	0.159	0.159	0.000	0.000	0.000	0.000
45	A	48	TYR	0	-0.040	-0.011	25.370	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	49	GLY	0	0.069	0.036	27.802	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	50	TYR	0	-0.103	-0.072	21.924	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	51	VAL	0	0.006	0.011	23.375	0.015	0.015	0.000	0.000	0.000	0.000
49	A	52	PHE	0	0.019	0.003	17.993	-0.017	-0.017	0.000	0.000	0.000	0.000
50	A	53	MET	0	-0.015	0.023	18.361	-0.002	-0.002	0.000	0.000	0.000	0.000
51	A	54	GLN	0	0.020	0.012	10.682	0.110	0.110	0.000	0.000	0.000	0.000
52	A	55	TYR	0	-0.060	-0.046	9.660	0.002	0.002	0.000	0.000	0.000	0.000
53	A	56	THR	0	-0.058	-0.061	12.082	0.090	0.090	0.000	0.000	0.000	0.000
54	A	57	GLY	0	-0.019	0.000	10.355	0.153	0.153	0.000	0.000	0.000	0.000
55	A	58	LEU	0	-0.074	-0.030	10.956	-0.137	-0.137	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.906	0.970	11.756	0.715	0.715	0.000	0.000	0.000	0.000
57	A	60	ASP	-1	-0.764	-0.893	16.673	-0.177	-0.177	0.000	0.000	0.000	0.000
58	A	61	LYS	1	0.836	0.913	20.153	0.143	0.143	0.000	0.000	0.000	0.000
59	A	62	ASN	0	-0.090	-0.051	22.427	-0.011	-0.011	0.000	0.000	0.000	0.000
60	A	63	GLU	-1	-0.898	-0.943	16.190	-0.579	-0.579	0.000	0.000	0.000	0.000
61	A	64	LYS	1	0.840	0.914	18.144	0.078	0.078	0.000	0.000	0.000	0.000
62	A	65	GLU	-1	-0.816	-0.894	13.453	-0.413	-0.413	0.000	0.000	0.000	0.000
63	A	66	ILE	0	-0.020	0.004	16.535	0.040	0.040	0.000	0.000	0.000	0.000
64	A	67	TYR	0	-0.007	-0.011	14.942	0.043	0.043	0.000	0.000	0.000	0.000
65	A	68	GLU	-1	-0.825	-0.924	17.298	0.306	0.306	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.083	0.041	19.153	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	70	ASP	-1	-0.773	-0.861	20.778	-0.046	-0.046	0.000	0.000	0.000	0.000
68	A	71	ILE	0	0.000	0.003	23.240	0.017	0.017	0.000	0.000	0.000	0.000
69	A	72	ILE	0	-0.021	-0.009	22.926	-0.022	-0.022	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.892	0.952	26.237	0.100	0.100	0.000	0.000	0.000	0.000
71	A	74	LYS	1	0.907	0.952	25.738	0.028	0.028	0.000	0.000	0.000	0.000
72	A	75	SER	0	-0.039	-0.032	27.903	0.005	0.005	0.000	0.000	0.000	0.000
73	A	76	ASN	0	-0.059	-0.051	29.743	-0.016	-0.016	0.000	0.000	0.000	0.000
74	A	77	ARG	1	0.949	0.975	32.015	0.076	0.076	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.014	0.004	32.908	0.004	0.004	0.000	0.000	0.000	0.000
76	A	79	SER	0	0.048	0.013	34.276	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	80	ASN	0	-0.041	-0.008	32.111	0.005	0.005	0.000	0.000	0.000	0.000
78	A	81	LEU	0	0.009	0.005	30.363	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	82	TYR	0	-0.025	-0.030	26.441	0.004	0.004	0.000	0.000	0.000	0.000
80	A	83	GLU	-1	-0.789	-0.892	25.201	0.095	0.095	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.055	-0.024	19.302	0.011	0.011	0.000	0.000	0.000	0.000
82	A	85	ILE	0	0.037	0.017	21.642	0.004	0.004	0.000	0.000	0.000	0.000
83	A	86	TYR	0	0.045	0.024	15.656	0.038	0.038	0.000	0.000	0.000	0.000
84	A	87	GLN	0	0.011	0.002	19.672	-0.057	-0.057	0.000	0.000	0.000	0.000
85	A	88	ASP	-1	-0.788	-0.908	19.576	0.465	0.465	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.045	-0.021	20.541	0.022	0.022	0.000	0.000	0.000	0.000
87	A	90	ILE	0	-0.078	-0.035	20.118	-0.031	-0.031	0.000	0.000	0.000	0.000
88	A	91	ALA	0	0.000	0.012	15.876	0.020	0.020	0.000	0.000	0.000	0.000
89	A	92	CYS	0	-0.045	-0.015	15.342	0.093	0.093	0.000	0.000	0.000	0.000
90	A	93	PHE	0	0.051	0.029	12.688	-0.056	-0.056	0.000	0.000	0.000	0.000
91	A	94	ARG	1	0.811	0.886	17.567	-0.206	-0.206	0.000	0.000	0.000	0.000
92	A	95	CYS	0	0.004	0.012	20.616	-0.011	-0.011	0.000	0.000	0.000	0.000
93	A	96	LYS	1	0.899	0.961	23.733	-0.079	-0.079	0.000	0.000	0.000	0.000
94	A	97	VAL	0	-0.028	-0.011	27.037	-0.013	-0.013	0.000	0.000	0.000	0.000
95	A	98	ILE	0	0.001	0.023	28.914	0.011	0.011	0.000	0.000	0.000	0.000
96	A	99	LYS	1	0.999	1.004	32.182	0.003	0.003	0.000	0.000	0.000	0.000
97	A	100	GLY	0	0.035	-0.012	33.783	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	101	ASP	-1	-0.889	-0.911	36.317	0.018	0.018	0.000	0.000	0.000	0.000
99	A	102	ILE	0	0.060	0.012	33.489	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	103	LYS	1	0.803	0.911	33.052	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	104	SER	0	-0.050	-0.031	29.301	-0.010	-0.010	0.000	0.000	0.000	0.000
102	A	105	PHE	0	0.044	0.009	22.506	-0.003	-0.003	0.000	0.000	0.000	0.000
103	A	106	PRO	0	-0.021	-0.014	23.646	0.014	0.014	0.000	0.000	0.000	0.000
104	A	107	CYS	0	0.060	0.033	19.156	0.004	0.004	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.044	0.040	17.579	-0.049	-0.049	0.000	0.000	0.000	0.000
106	A	109	ASN	0	0.014	-0.004	15.652	0.000	0.000	0.000	0.000	0.000	0.000
107	A	110	ILE	0	0.125	0.059	12.630	-0.011	-0.011	0.000	0.000	0.000	0.000
108	A	111	GLY	0	0.006	0.012	15.818	-0.033	-0.033	0.000	0.000	0.000	0.000
109	A	112	THR	0	-0.106	-0.067	18.920	-0.002	-0.002	0.000	0.000	0.000	0.000
110	A	113	VAL	0	0.075	0.025	17.205	0.009	0.009	0.000	0.000	0.000	0.000
111	A	114	ARG	1	0.950	0.991	19.685	0.188	0.188	0.000	0.000	0.000	0.000
112	A	115	ASN	0	-0.042	-0.023	21.066	-0.017	-0.017	0.000	0.000	0.000	0.000
113	A	116	CYS	0	-0.069	-0.018	22.705	0.032	0.032	0.000	0.000	0.000	0.000
114	A	117	GLU	-1	-0.752	-0.860	23.678	-0.133	-0.133	0.000	0.000	0.000	0.000
115	A	118	VAL	0	-0.017	-0.019	21.762	0.021	0.021	0.000	0.000	0.000	0.000
116	A	119	ILE	0	-0.085	-0.039	25.140	-0.012	-0.012	0.000	0.000	0.000	0.000
117	A	120	GLY	0	0.090	0.041	27.142	-0.002	-0.002	0.000	0.000	0.000	0.000
118	A	121	ASN	0	-0.082	-0.058	24.419	0.014	0.014	0.000	0.000	0.000	0.000
119	A	122	ILE	0	-0.020	-0.020	25.419	-0.005	-0.005	0.000	0.000	0.000	0.000
120	A	123	TYR	0	0.007	0.010	24.536	0.007	0.007	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.809	-0.906	25.396	-0.019	-0.019	0.000	0.000	0.000	0.000
122	A	125	ASN	0	-0.072	-0.035	29.375	-0.011	-0.011	0.000	0.000	0.000	0.000
123	A	126	PRO	0	0.056	0.022	31.484	0.004	0.004	0.000	0.000	0.000	0.000
124	A	127	GLU	-1	-0.866	-0.935	33.908	-0.003	-0.003	0.000	0.000	0.000	0.000
125	A	128	LEU	0	-0.101	-0.042	30.405	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	129	LEU	0	-0.049	-0.014	30.598	0.005	0.005	0.000	0.000	0.000	0.000
127	A	130	GLU	-1	-0.985	-0.985	34.176	0.028	0.028	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASN)