FMO DATABASE

FMODB ID: 4J9GN

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1110228.357843
FMO2-HF: Nuclear repulsion	1057089.299215
FMO2-HF: Total energy	-53139.058629
FMO2-MP2: Total energy	-53291.0745

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.
4.308	5.707	-0.001	-0.588	-0.811	0.002

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 : -0.001 / q_NPA : -0.016

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	-0.891	-0.955	3.899	1.150	2.549	-0.001	-0.588	-0.811	0.002
4	A	7	VAL	0	-0.045	-0.021	5.951	0.210	0.210	0.000	0.000	0.000	0.000
5	A	8	LYS	1	0.850	0.926	8.391	-0.279	-0.279	0.000	0.000	0.000	0.000
6	A	9	PHE	0	0.039	0.001	11.818	0.005	0.005	0.000	0.000	0.000	0.000
7	A	10	ARG	1	0.793	0.892	15.549	-0.297	-0.297	0.000	0.000	0.000	0.000
8	A	11	ALA	0	0.016	-0.001	18.713	0.057	0.057	0.000	0.000	0.000	0.000
9	A	12	TRP	0	0.041	0.017	22.055	-0.047	-0.047	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.747	-0.885	25.639	0.223	0.223	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.903	0.934	28.061	-0.280	-0.280	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.961	-0.960	31.139	0.176	0.176	0.000	0.000	0.000	0.000
13	A	16	LEU	0	-0.058	-0.034	30.853	-0.018	-0.018	0.000	0.000	0.000	0.000
14	A	17	ASN	0	-0.097	-0.033	31.390	-0.006	-0.006	0.000	0.000	0.000	0.000
15	A	18	MET	0	0.022	0.014	27.415	-0.016	-0.016	0.000	0.000	0.000	0.000
16	A	19	MET	0	-0.021	0.012	22.773	0.039	0.039	0.000	0.000	0.000	0.000
17	A	20	VAL	0	-0.027	-0.002	21.329	-0.031	-0.031	0.000	0.000	0.000	0.000
18	A	21	TYR	0	-0.030	-0.015	17.864	0.050	0.050	0.000	0.000	0.000	0.000
19	A	22	THR	0	-0.075	-0.057	16.779	0.016	0.016	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.941	0.956	19.080	-0.085	-0.085	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.796	-0.876	22.271	0.097	0.097	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.001	0.010	24.565	0.009	0.009	0.000	0.000	0.000	0.000
23	A	26	THR	0	-0.048	-0.013	24.741	0.007	0.007	0.000	0.000	0.000	0.000
24	A	27	GLY	0	0.039	-0.001	26.068	0.015	0.015	0.000	0.000	0.000	0.000
25	A	28	HIS	0	-0.058	-0.028	25.956	-0.018	-0.018	0.000	0.000	0.000	0.000
26	A	29	ILE	0	0.002	0.015	22.107	0.006	0.006	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.951	-0.980	24.652	0.221	0.221	0.000	0.000	0.000	0.000
28	A	31	TYR	0	0.046	0.022	22.730	0.010	0.010	0.000	0.000	0.000	0.000
29	A	32	ASN	0	-0.018	-0.013	24.446	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	33	THR	0	-0.059	-0.064	20.945	0.005	0.005	0.000	0.000	0.000	0.000
31	A	34	ASN	0	-0.016	0.006	17.735	0.071	0.071	0.000	0.000	0.000	0.000
32	A	35	PRO	0	0.057	-0.005	14.156	0.005	0.005	0.000	0.000	0.000	0.000
33	A	36	ALA	0	0.004	0.010	14.129	0.043	0.043	0.000	0.000	0.000	0.000
34	A	37	ASP	-1	-0.829	-0.892	15.283	0.626	0.626	0.000	0.000	0.000	0.000
35	A	38	THR	0	0.002	-0.004	18.136	-0.056	-0.056	0.000	0.000	0.000	0.000
36	A	39	ILE	0	-0.016	0.004	12.719	-0.019	-0.019	0.000	0.000	0.000	0.000
37	A	40	ASN	0	-0.001	-0.009	16.746	0.039	0.039	0.000	0.000	0.000	0.000
38	A	41	ILE	0	0.001	0.016	18.823	-0.049	-0.049	0.000	0.000	0.000	0.000
39	A	42	ILE	0	-0.003	0.002	19.137	-0.037	-0.037	0.000	0.000	0.000	0.000
40	A	43	LEU	0	-0.076	-0.043	15.577	-0.017	-0.017	0.000	0.000	0.000	0.000
41	A	44	ASN	0	-0.074	-0.052	19.883	-0.036	-0.036	0.000	0.000	0.000	0.000
42	A	45	GLN	0	-0.030	0.026	23.198	-0.025	-0.025	0.000	0.000	0.000	0.000
43	A	46	ASP	-1	-0.918	-0.971	25.989	0.399	0.399	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-1.001	-1.010	27.838	0.276	0.276	0.000	0.000	0.000	0.000
45	A	48	TYR	0	-0.009	0.006	26.811	-0.016	-0.016	0.000	0.000	0.000	0.000
46	A	49	GLY	0	0.016	0.017	28.966	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	50	TYR	0	-0.070	-0.065	22.893	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	51	VAL	0	-0.029	-0.005	24.244	0.023	0.023	0.000	0.000	0.000	0.000
49	A	52	PHE	0	0.038	0.010	19.022	-0.007	-0.007	0.000	0.000	0.000	0.000
50	A	53	MET	0	-0.027	0.019	19.408	-0.017	-0.017	0.000	0.000	0.000	0.000
51	A	54	GLN	0	-0.027	-0.019	11.943	0.336	0.336	0.000	0.000	0.000	0.000
52	A	55	TYR	0	-0.038	-0.007	9.835	-0.112	-0.112	0.000	0.000	0.000	0.000
53	A	56	THR	0	-0.038	-0.043	12.751	0.156	0.156	0.000	0.000	0.000	0.000
54	A	57	GLY	0	-0.029	-0.011	10.720	0.147	0.147	0.000	0.000	0.000	0.000
55	A	58	LEU	0	-0.087	-0.034	11.465	-0.285	-0.285	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.996	0.995	11.725	0.910	0.910	0.000	0.000	0.000	0.000
57	A	60	ASP	-1	-0.784	-0.901	16.663	-0.164	-0.164	0.000	0.000	0.000	0.000
58	A	61	LYS	1	0.876	0.936	19.860	0.122	0.122	0.000	0.000	0.000	0.000
59	A	62	ASN	0	-0.068	-0.028	22.281	-0.047	-0.047	0.000	0.000	0.000	0.000
60	A	63	GLU	-1	-0.895	-0.951	16.867	-0.566	-0.566	0.000	0.000	0.000	0.000
61	A	64	LYS	1	0.918	0.974	17.743	0.020	0.020	0.000	0.000	0.000	0.000
62	A	65	GLU	-1	-0.903	-0.944	12.832	-0.176	-0.176	0.000	0.000	0.000	0.000
63	A	66	ILE	0	-0.021	-0.010	16.243	0.043	0.043	0.000	0.000	0.000	0.000
64	A	67	TYR	0	-0.002	-0.002	15.287	0.114	0.114	0.000	0.000	0.000	0.000
65	A	68	GLU	-1	-0.841	-0.926	18.124	0.556	0.556	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.058	0.012	20.101	-0.014	-0.014	0.000	0.000	0.000	0.000
67	A	70	ASP	-1	-0.790	-0.879	20.771	0.104	0.104	0.000	0.000	0.000	0.000
68	A	71	ILE	0	0.011	0.013	23.621	0.012	0.012	0.000	0.000	0.000	0.000
69	A	72	ILE	0	-0.023	-0.009	23.050	-0.028	-0.028	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.958	0.989	26.430	0.064	0.064	0.000	0.000	0.000	0.000
71	A	74	LYS	1	0.951	0.971	25.647	0.009	0.009	0.000	0.000	0.000	0.000
72	A	75	SER	0	-0.014	-0.007	27.993	0.008	0.008	0.000	0.000	0.000	0.000
73	A	76	ASN	0	-0.052	-0.037	29.839	-0.025	-0.025	0.000	0.000	0.000	0.000
74	A	77	ARG	1	0.959	0.976	32.302	0.061	0.061	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.066	-0.037	33.115	0.010	0.010	0.000	0.000	0.000	0.000
76	A	79	SER	0	0.063	0.012	34.836	-0.004	-0.004	0.000	0.000	0.000	0.000
77	A	80	ASN	0	-0.066	-0.026	32.285	0.013	0.013	0.000	0.000	0.000	0.000
78	A	81	LEU	0	0.028	0.021	30.855	-0.013	-0.013	0.000	0.000	0.000	0.000
79	A	82	TYR	0	-0.028	-0.027	26.980	0.006	0.006	0.000	0.000	0.000	0.000
80	A	83	GLU	-1	-0.806	-0.912	25.928	0.216	0.216	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.057	-0.021	19.582	0.008	0.008	0.000	0.000	0.000	0.000
82	A	85	ILE	0	0.065	0.036	22.903	0.014	0.014	0.000	0.000	0.000	0.000
83	A	86	TYR	0	0.058	0.022	15.858	0.052	0.052	0.000	0.000	0.000	0.000
84	A	87	GLN	0	-0.020	-0.017	20.390	-0.056	-0.056	0.000	0.000	0.000	0.000
85	A	88	ASP	-1	-0.768	-0.907	20.318	0.719	0.719	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.064	-0.029	21.001	0.029	0.029	0.000	0.000	0.000	0.000
87	A	90	ILE	0	-0.069	-0.033	20.839	-0.038	-0.038	0.000	0.000	0.000	0.000
88	A	91	ALA	0	-0.028	-0.001	16.685	0.017	0.017	0.000	0.000	0.000	0.000
89	A	92	CYS	0	-0.034	-0.005	16.404	0.060	0.060	0.000	0.000	0.000	0.000
90	A	93	PHE	0	0.046	0.019	13.768	-0.049	-0.049	0.000	0.000	0.000	0.000
91	A	94	ARG	1	0.874	0.936	18.586	-0.323	-0.323	0.000	0.000	0.000	0.000
92	A	95	CYS	0	-0.017	0.004	21.726	0.002	0.002	0.000	0.000	0.000	0.000
93	A	96	LYS	1	0.905	0.963	24.747	-0.205	-0.205	0.000	0.000	0.000	0.000
94	A	97	VAL	0	-0.041	-0.022	27.939	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	98	ILE	0	0.052	0.033	30.180	0.010	0.010	0.000	0.000	0.000	0.000
96	A	99	LYS	1	0.971	0.999	32.757	-0.042	-0.042	0.000	0.000	0.000	0.000
97	A	100	GLY	0	0.021	0.001	34.425	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	101	ASP	-1	-0.930	-0.970	37.030	0.048	0.048	0.000	0.000	0.000	0.000
99	A	102	ILE	0	0.026	0.020	34.095	-0.004	-0.004	0.000	0.000	0.000	0.000
100	A	103	LYS	1	0.906	0.955	33.698	-0.020	-0.020	0.000	0.000	0.000	0.000
101	A	104	SER	0	-0.089	0.012	29.230	-0.007	-0.007	0.000	0.000	0.000	0.000
102	A	105	PHE	0	0.090	-0.016	22.469	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	106	PRO	0	-0.071	-0.048	24.262	0.018	0.018	0.000	0.000	0.000	0.000
104	A	107	CYS	0	0.072	0.042	19.728	0.019	0.019	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.062	0.063	18.211	-0.064	-0.064	0.000	0.000	0.000	0.000
106	A	109	ASN	0	-0.013	-0.004	16.164	-0.002	-0.002	0.000	0.000	0.000	0.000
107	A	110	ILE	0	0.140	0.054	12.602	-0.007	-0.007	0.000	0.000	0.000	0.000
108	A	111	GLY	0	0.005	0.007	15.932	-0.037	-0.037	0.000	0.000	0.000	0.000
109	A	112	THR	0	-0.138	-0.098	19.219	-0.010	-0.010	0.000	0.000	0.000	0.000
110	A	113	VAL	0	0.079	0.022	17.735	0.022	0.022	0.000	0.000	0.000	0.000
111	A	114	ARG	1	0.974	1.009	20.191	0.206	0.206	0.000	0.000	0.000	0.000
112	A	115	ASN	0	-0.083	-0.049	21.178	-0.020	-0.020	0.000	0.000	0.000	0.000
113	A	116	CYS	0	-0.046	0.000	23.192	0.033	0.033	0.000	0.000	0.000	0.000
114	A	117	GLU	-1	-0.881	-0.942	23.890	-0.128	-0.128	0.000	0.000	0.000	0.000
115	A	118	VAL	0	-0.004	-0.015	21.195	0.024	0.024	0.000	0.000	0.000	0.000
116	A	119	ILE	0	-0.101	-0.065	24.630	-0.021	-0.021	0.000	0.000	0.000	0.000
117	A	120	GLY	0	0.077	0.045	26.765	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	121	ASN	0	-0.066	-0.051	24.814	0.022	0.022	0.000	0.000	0.000	0.000
119	A	122	ILE	0	-0.021	-0.024	26.636	-0.014	-0.014	0.000	0.000	0.000	0.000
120	A	123	TYR	0	0.002	0.004	25.730	0.001	0.001	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.873	-0.926	26.296	0.090	0.090	0.000	0.000	0.000	0.000
122	A	125	ASN	0	-0.044	-0.014	29.340	-0.008	-0.008	0.000	0.000	0.000	0.000
123	A	126	PRO	0	0.069	0.046	32.029	0.002	0.002	0.000	0.000	0.000	0.000
124	A	127	GLU	-1	-0.869	-0.946	34.497	0.060	0.060	0.000	0.000	0.000	0.000
125	A	128	LEU	0	-0.104	-0.052	30.749	-0.008	-0.008	0.000	0.000	0.000	0.000
126	A	129	LEU	0	-0.079	-0.035	31.297	0.005	0.005	0.000	0.000	0.000	0.000
127	A	130	GLU	-1	-0.998	-0.983	34.800	0.076	0.076	0.000	0.000	0.000	0.000

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