FMO DATABASE

FMODB ID: Z2M3N

Calculation Name: 2QZ5-A-Xray316

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QZ5

Chain ID: A

ChEMBL ID:

UniProt ID: Q8C4Q6

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	154
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1549673.632181
FMO2-HF: Nuclear repulsion	1488684.289262
FMO2-HF: Total energy	-60989.342919
FMO2-MP2: Total energy	-61168.837627

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:18:ACE )

Summations of interaction energy for fragment #1(A:18: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.
-0.223	1.13	0.076	-0.723	-0.705	-0.001

Interaction energy analysis for fragmet #1(A:18:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / 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

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	20	THR	0	-0.032	-0.016	3.901	0.760	1.458	-0.004	-0.330	-0.364	0.000
4	A	21	LEU	0	-0.040	-0.014	7.023	0.266	0.266	0.000	0.000	0.000	0.000
5	A	22	LEU	0	0.018	0.006	9.640	0.045	0.045	0.000	0.000	0.000	0.000
6	A	23	PRO	0	-0.005	-0.006	13.038	-0.013	-0.013	0.000	0.000	0.000	0.000
7	A	24	ARG	1	0.887	0.952	15.987	0.245	0.245	0.000	0.000	0.000	0.000
8	A	25	LEU	0	-0.012	0.020	19.064	0.016	0.016	0.000	0.000	0.000	0.000
9	A	26	PRO	0	0.008	0.004	21.503	0.001	0.001	0.000	0.000	0.000	0.000
10	A	27	SER	0	-0.034	-0.022	24.807	0.006	0.006	0.000	0.000	0.000	0.000
11	A	28	GLU	-1	-0.830	-0.945	27.268	-0.077	-0.077	0.000	0.000	0.000	0.000
12	A	29	PRO	0	-0.035	-0.023	30.471	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	30	GLY	0	-0.001	0.002	33.951	0.003	0.003	0.000	0.000	0.000	0.000
14	A	31	MET	0	-0.058	-0.004	29.425	0.003	0.003	0.000	0.000	0.000	0.000
15	A	32	THR	0	-0.005	-0.027	27.145	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	33	LEU	0	-0.062	-0.032	22.996	-0.006	-0.006	0.000	0.000	0.000	0.000
17	A	34	LEU	0	0.025	0.013	21.250	0.005	0.005	0.000	0.000	0.000	0.000
18	A	35	THR	0	-0.013	-0.004	18.147	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	36	ILE	0	-0.027	-0.029	17.428	0.027	0.027	0.000	0.000	0.000	0.000
20	A	37	ARG	1	0.986	1.014	16.563	0.253	0.253	0.000	0.000	0.000	0.000
21	A	38	ILE	0	-0.009	-0.016	12.434	0.045	0.045	0.000	0.000	0.000	0.000
22	A	39	GLU	-1	-0.929	-0.968	15.352	-0.220	-0.220	0.000	0.000	0.000	0.000
23	A	40	LYS	1	0.976	0.981	16.030	0.106	0.106	0.000	0.000	0.000	0.000
24	A	41	ILE	0	0.004	0.010	14.548	0.011	0.011	0.000	0.000	0.000	0.000
25	A	42	GLY	0	0.023	0.005	17.626	0.008	0.008	0.000	0.000	0.000	0.000
26	A	43	LEU	0	-0.050	-0.040	15.813	0.012	0.012	0.000	0.000	0.000	0.000
27	A	44	LYS	1	0.940	0.974	20.325	0.000	0.000	0.000	0.000	0.000	0.000
28	A	45	ASP	-1	-0.779	-0.880	19.851	0.024	0.024	0.000	0.000	0.000	0.000
29	A	46	ALA	0	-0.005	0.015	17.263	0.014	0.014	0.000	0.000	0.000	0.000
30	A	47	GLY	0	0.022	0.012	16.124	0.005	0.005	0.000	0.000	0.000	0.000
31	A	48	GLN	0	-0.070	-0.049	16.941	0.013	0.013	0.000	0.000	0.000	0.000
32	A	49	CYS	0	-0.092	-0.024	13.196	0.027	0.027	0.000	0.000	0.000	0.000
33	A	50	ILE	0	-0.009	-0.016	10.697	-0.030	-0.030	0.000	0.000	0.000	0.000
34	A	51	ASP	-1	-0.898	-0.947	6.558	0.737	0.737	0.000	0.000	0.000	0.000
35	A	52	PRO	0	-0.043	-0.023	7.441	0.094	0.094	0.000	0.000	0.000	0.000
36	A	53	TYR	0	0.004	-0.001	5.534	-0.098	-0.098	0.000	0.000	0.000	0.000
37	A	54	ILE	0	-0.001	-0.008	7.551	0.205	0.205	0.000	0.000	0.000	0.000
38	A	55	THR	0	-0.026	-0.010	8.568	-0.117	-0.117	0.000	0.000	0.000	0.000
39	A	56	VAL	0	0.006	-0.006	10.308	0.057	0.057	0.000	0.000	0.000	0.000
40	A	57	SER	0	0.001	0.003	13.219	0.006	0.006	0.000	0.000	0.000	0.000
41	A	58	VAL	0	0.038	0.014	15.904	0.001	0.001	0.000	0.000	0.000	0.000
42	A	59	LYS	1	0.822	0.945	17.415	0.066	0.066	0.000	0.000	0.000	0.000
43	A	60	ASP	-1	-0.755	-0.868	22.079	-0.043	-0.043	0.000	0.000	0.000	0.000
44	A	61	LEU	0	0.027	0.017	25.610	0.002	0.002	0.000	0.000	0.000	0.000
45	A	62	ASN	0	-0.074	-0.075	27.714	0.007	0.007	0.000	0.000	0.000	0.000
46	A	63	GLY	0	0.005	-0.007	23.620	0.007	0.007	0.000	0.000	0.000	0.000
47	A	64	ILE	0	-0.027	-0.015	22.381	0.005	0.005	0.000	0.000	0.000	0.000
48	A	65	ASP	-1	-0.870	-0.938	17.682	-0.078	-0.078	0.000	0.000	0.000	0.000
49	A	66	LEU	0	-0.017	-0.008	20.595	0.006	0.006	0.000	0.000	0.000	0.000
50	A	67	THR	0	-0.036	-0.036	17.412	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	68	PRO	0	-0.017	0.008	15.005	0.011	0.011	0.000	0.000	0.000	0.000
52	A	69	VAL	0	0.009	0.002	11.044	-0.023	-0.023	0.000	0.000	0.000	0.000
53	A	70	GLN	0	0.001	0.013	10.134	-0.077	-0.077	0.000	0.000	0.000	0.000
54	A	71	ASP	-1	-0.807	-0.901	5.328	-0.110	-0.110	0.000	0.000	0.000	0.000
55	A	72	THR	0	0.004	0.005	6.388	-0.350	-0.350	0.000	0.000	0.000	0.000
56	A	73	PRO	0	0.131	0.007	4.453	-1.738	-1.540	0.006	-0.245	0.041	-0.001
57	A	74	VAL	0	-0.149	-0.069	3.076	1.033	1.510	0.074	-0.146	-0.405	0.000
58	A	75	ALA	0	-0.029	-0.015	5.196	-0.080	-0.100	0.000	-0.002	0.023	0.000
59	A	76	SER	0	0.017	0.025	8.929	0.083	0.083	0.000	0.000	0.000	0.000
60	A	77	ARG	1	0.952	0.972	10.933	0.192	0.192	0.000	0.000	0.000	0.000
61	A	78	LYS	1	0.904	0.979	12.326	-0.061	-0.061	0.000	0.000	0.000	0.000
62	A	79	GLU	-1	-0.908	-0.967	15.213	-0.083	-0.083	0.000	0.000	0.000	0.000
63	A	80	ASP	-1	-0.869	-0.935	18.896	-0.021	-0.021	0.000	0.000	0.000	0.000
64	A	81	THR	0	-0.017	-0.021	20.947	0.009	0.009	0.000	0.000	0.000	0.000
65	A	82	TYR	0	-0.014	-0.022	18.825	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	83	VAL	0	-0.031	0.002	12.169	0.012	0.012	0.000	0.000	0.000	0.000
67	A	84	HIS	0	-0.010	-0.024	14.579	-0.029	-0.029	0.000	0.000	0.000	0.000
68	A	85	PHE	0	-0.019	-0.026	8.696	0.002	0.002	0.000	0.000	0.000	0.000
69	A	86	ASN	0	-0.029	-0.014	12.506	-0.027	-0.027	0.000	0.000	0.000	0.000
70	A	87	VAL	0	0.000	0.009	9.912	-0.034	-0.034	0.000	0.000	0.000	0.000
71	A	88	ASP	-1	-0.861	-0.939	13.097	-0.288	-0.288	0.000	0.000	0.000	0.000
72	A	89	ILE	0	-0.033	-0.012	12.444	-0.080	-0.080	0.000	0.000	0.000	0.000
73	A	90	GLU	-1	-0.783	-0.888	14.698	-0.229	-0.229	0.000	0.000	0.000	0.000
74	A	91	LEU	0	0.045	0.020	16.547	-0.013	-0.013	0.000	0.000	0.000	0.000
75	A	92	GLN	0	-0.025	-0.020	15.912	0.037	0.037	0.000	0.000	0.000	0.000
76	A	93	LYS	1	0.899	0.925	19.125	0.114	0.114	0.000	0.000	0.000	0.000
77	A	94	HIS	0	0.015	0.021	22.876	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	95	VAL	0	0.105	0.048	25.341	0.006	0.006	0.000	0.000	0.000	0.000
79	A	96	GLU	-1	-0.791	-0.871	26.884	-0.090	-0.090	0.000	0.000	0.000	0.000
80	A	97	LYS	1	0.822	0.909	27.585	0.088	0.088	0.000	0.000	0.000	0.000
81	A	98	LEU	0	-0.074	-0.015	23.191	0.002	0.002	0.000	0.000	0.000	0.000
82	A	99	THR	0	-0.008	-0.013	27.215	0.005	0.005	0.000	0.000	0.000	0.000
83	A	100	LYS	1	1.029	0.986	28.762	0.042	0.042	0.000	0.000	0.000	0.000
84	A	101	GLY	0	0.017	-0.002	29.578	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	102	ALA	0	-0.016	-0.008	24.468	0.002	0.002	0.000	0.000	0.000	0.000
86	A	103	ALA	0	0.021	0.015	23.349	0.002	0.002	0.000	0.000	0.000	0.000
87	A	104	ILE	0	-0.024	-0.011	18.157	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	105	PHE	0	-0.030	-0.018	17.353	0.010	0.010	0.000	0.000	0.000	0.000
89	A	106	PHE	0	0.049	0.022	14.551	-0.036	-0.036	0.000	0.000	0.000	0.000
90	A	107	GLU	-1	-0.850	-0.907	12.792	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	108	PHE	0	0.049	0.020	11.718	-0.024	-0.024	0.000	0.000	0.000	0.000
92	A	109	LYS	1	0.934	0.962	8.718	0.025	0.025	0.000	0.000	0.000	0.000
93	A	110	HIS	0	0.020	0.006	9.405	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	111	TYR	0	0.057	0.031	9.244	0.017	0.017	0.000	0.000	0.000	0.000
95	A	112	LYS	1	0.870	0.925	11.027	-0.227	-0.227	0.000	0.000	0.000	0.000
96	A	113	PRO	0	0.049	0.011	14.759	0.016	0.016	0.000	0.000	0.000	0.000
97	A	114	LYS	1	0.973	0.984	16.043	-0.111	-0.111	0.000	0.000	0.000	0.000
98	A	115	LYS	1	0.910	0.950	17.627	-0.133	-0.133	0.000	0.000	0.000	0.000
99	A	116	ARG	1	1.005	1.017	14.912	-0.341	-0.341	0.000	0.000	0.000	0.000
100	A	117	PHE	0	0.061	0.024	12.587	0.005	0.005	0.000	0.000	0.000	0.000
101	A	118	THR	0	0.043	0.046	8.227	0.039	0.039	0.000	0.000	0.000	0.000
102	A	119	SER	0	-0.115	-0.048	10.986	-0.063	-0.063	0.000	0.000	0.000	0.000
103	A	120	THR	0	0.079	0.035	12.494	0.014	0.014	0.000	0.000	0.000	0.000
104	A	121	LYS	1	0.742	0.850	14.209	-0.019	-0.019	0.000	0.000	0.000	0.000
105	A	122	CYS	0	-0.054	-0.019	16.006	0.000	0.000	0.000	0.000	0.000	0.000
106	A	123	PHE	0	0.044	0.029	16.147	-0.009	-0.009	0.000	0.000	0.000	0.000
107	A	124	ALA	0	0.058	0.037	17.999	0.012	0.012	0.000	0.000	0.000	0.000
108	A	125	PHE	0	-0.041	-0.025	18.919	-0.012	-0.012	0.000	0.000	0.000	0.000
109	A	126	MET	0	0.044	0.041	20.457	0.004	0.004	0.000	0.000	0.000	0.000
110	A	127	GLU	-1	-0.841	-0.937	23.620	-0.063	-0.063	0.000	0.000	0.000	0.000
111	A	128	MET	0	-0.017	0.014	24.501	-0.005	-0.005	0.000	0.000	0.000	0.000
112	A	129	ASP	-1	-0.929	-0.953	27.693	-0.071	-0.071	0.000	0.000	0.000	0.000
113	A	130	GLU	-1	-0.878	-0.967	26.562	-0.084	-0.084	0.000	0.000	0.000	0.000
114	A	131	ILE	0	-0.049	-0.032	24.330	-0.010	-0.010	0.000	0.000	0.000	0.000
115	A	132	LYS	1	0.925	0.972	26.915	0.092	0.092	0.000	0.000	0.000	0.000
116	A	133	PRO	0	-0.029	-0.004	26.991	-0.009	-0.009	0.000	0.000	0.000	0.000
117	A	134	GLY	0	0.026	0.018	26.658	0.010	0.010	0.000	0.000	0.000	0.000
118	A	135	PRO	0	-0.027	-0.028	24.734	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	136	ILE	0	0.014	0.011	22.959	0.010	0.010	0.000	0.000	0.000	0.000
120	A	137	VAL	0	-0.053	-0.019	23.263	-0.012	-0.012	0.000	0.000	0.000	0.000
121	A	138	ILE	0	0.036	0.028	20.724	0.008	0.008	0.000	0.000	0.000	0.000
122	A	139	GLU	-1	-0.830	-0.903	22.499	-0.068	-0.068	0.000	0.000	0.000	0.000
123	A	140	LEU	0	-0.014	-0.019	18.825	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	141	TYR	0	-0.004	-0.039	21.346	0.017	0.017	0.000	0.000	0.000	0.000
125	A	142	LYS	1	0.858	0.929	20.780	-0.004	-0.004	0.000	0.000	0.000	0.000
126	A	143	LYS	1	0.930	1.018	18.295	-0.081	-0.081	0.000	0.000	0.000	0.000
127	A	144	PRO	0	-0.073	-0.063	19.676	0.004	0.004	0.000	0.000	0.000	0.000
128	A	145	THR	0	0.020	-0.048	16.718	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	146	ASP	-1	-0.794	-0.871	19.902	-0.008	-0.008	0.000	0.000	0.000	0.000
130	A	147	PHE	0	0.029	-0.006	16.466	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	148	LYS	1	0.841	0.968	22.365	0.009	0.009	0.000	0.000	0.000	0.000
132	A	149	ARG	1	0.757	0.883	24.459	0.057	0.057	0.000	0.000	0.000	0.000
133	A	150	LYS	1	0.938	0.970	25.982	0.021	0.021	0.000	0.000	0.000	0.000
134	A	151	LYS	1	0.925	0.962	28.041	-0.003	-0.003	0.000	0.000	0.000	0.000
135	A	152	LEU	0	0.030	0.024	25.257	0.001	0.001	0.000	0.000	0.000	0.000
136	A	153	GLN	0	-0.011	-0.003	26.119	0.002	0.002	0.000	0.000	0.000	0.000
137	A	154	LEU	0	0.046	0.034	25.568	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	155	LEU	0	-0.028	-0.028	20.379	0.009	0.009	0.000	0.000	0.000	0.000
139	A	156	THR	0	-0.066	-0.059	24.485	0.010	0.010	0.000	0.000	0.000	0.000
140	A	157	LYS	1	1.008	1.007	26.706	0.011	0.011	0.000	0.000	0.000	0.000
141	A	158	LYS	1	0.920	0.971	26.963	0.014	0.014	0.000	0.000	0.000	0.000
142	A	159	PRO	0	0.069	0.041	27.096	-0.002	-0.002	0.000	0.000	0.000	0.000
143	A	160	LEU	0	-0.085	-0.027	22.637	-0.003	-0.003	0.000	0.000	0.000	0.000
144	A	161	TYR	0	0.033	0.019	22.432	0.007	0.007	0.000	0.000	0.000	0.000
145	A	162	LEU	0	0.015	0.019	15.914	-0.006	-0.006	0.000	0.000	0.000	0.000
146	A	163	HIS	0	-0.033	-0.028	19.029	0.017	0.017	0.000	0.000	0.000	0.000
147	A	164	LEU	0	0.020	0.024	17.001	-0.034	-0.034	0.000	0.000	0.000	0.000
148	A	165	HIS	0	0.079	0.041	20.280	0.032	0.032	0.000	0.000	0.000	0.000
149	A	166	GLN	0	-0.022	0.003	20.961	-0.026	-0.026	0.000	0.000	0.000	0.000
150	A	167	SER	0	-0.016	-0.026	22.469	0.016	0.016	0.000	0.000	0.000	0.000
151	A	168	LEU	0	0.013	0.018	23.841	-0.009	-0.009	0.000	0.000	0.000	0.000
152	A	169	HIS	0	-0.053	-0.039	22.319	0.020	0.020	0.000	0.000	0.000	0.000
153	A	170	LYS	1	0.930	0.976	27.414	0.103	0.103	0.000	0.000	0.000	0.000
154	A	171	NME	0	0.084	0.045	30.825	-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:18:ACE )