FMO DATABASE

FMODB ID: R51L8

Calculation Name: 4QXZ-A-Xray322

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4QXZ

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H3

Base Structure: X-ray

Registration Date: 2021-09-07

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	148
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1416551.367864
FMO2-HF: Nuclear repulsion	1356350.984964
FMO2-HF: Total energy	-60200.3829
FMO2-MP2: Total energy	-60375.621039

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:-2:ACE )

Summations of interaction energy for fragment #1(A:-2: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.
1.775	2.578	-0.007	-0.369	-0.427	-0.001

Interaction energy analysis for fragmet #1(A:-2:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.029 / q_NPA : 0.004

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	0	HIS	0	0.026	0.011	3.807	0.804	1.607	-0.007	-0.369	-0.427	-0.001
4	A	1	MET	0	-0.046	0.006	6.822	0.373	0.373	0.000	0.000	0.000	0.000
5	A	2	LYS	1	0.981	0.987	8.803	0.313	0.313	0.000	0.000	0.000	0.000
6	A	3	THR	0	0.021	0.016	11.840	0.086	0.086	0.000	0.000	0.000	0.000
7	A	4	PHE	0	0.007	0.002	7.837	-0.125	-0.125	0.000	0.000	0.000	0.000
8	A	5	LYS	1	1.002	1.008	13.454	0.298	0.298	0.000	0.000	0.000	0.000
9	A	6	ALA	0	-0.030	-0.008	15.364	-0.033	-0.033	0.000	0.000	0.000	0.000
10	A	7	VAL	0	-0.031	-0.032	16.535	0.021	0.021	0.000	0.000	0.000	0.000
11	A	8	ARG	1	0.836	0.906	18.467	0.129	0.129	0.000	0.000	0.000	0.000
12	A	9	PHE	0	0.060	0.030	18.997	-0.011	-0.011	0.000	0.000	0.000	0.000
13	A	10	GLN	0	-0.036	-0.029	21.175	0.014	0.014	0.000	0.000	0.000	0.000
14	A	11	ILE	0	0.029	0.017	22.272	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	12	VAL	0	-0.033	-0.007	22.603	0.002	0.002	0.000	0.000	0.000	0.000
16	A	13	ASN	0	0.044	0.018	25.482	0.004	0.004	0.000	0.000	0.000	0.000
17	A	14	GLU	-1	-0.865	-0.944	27.742	0.005	0.005	0.000	0.000	0.000	0.000
18	A	15	HIS	0	-0.020	0.010	29.610	0.004	0.004	0.000	0.000	0.000	0.000
19	A	16	GLY	0	0.062	0.022	26.706	0.001	0.001	0.000	0.000	0.000	0.000
20	A	17	ARG	1	0.871	0.929	27.614	0.010	0.010	0.000	0.000	0.000	0.000
21	A	18	ILE	0	0.056	0.030	23.678	0.001	0.001	0.000	0.000	0.000	0.000
22	A	19	ILE	0	-0.009	-0.002	26.908	0.001	0.001	0.000	0.000	0.000	0.000
23	A	20	GLU	-1	-0.784	-0.874	23.692	-0.094	-0.094	0.000	0.000	0.000	0.000
24	A	21	TYR	0	-0.051	-0.036	25.427	0.006	0.006	0.000	0.000	0.000	0.000
25	A	22	GLU	-1	-0.914	-0.957	25.390	-0.106	-0.106	0.000	0.000	0.000	0.000
26	A	23	LEU	0	-0.084	-0.040	21.065	0.002	0.002	0.000	0.000	0.000	0.000
27	A	24	GLU	-1	-0.945	-0.968	25.422	-0.091	-0.091	0.000	0.000	0.000	0.000
28	A	25	ASP	-1	-0.960	-0.992	23.881	-0.169	-0.169	0.000	0.000	0.000	0.000
29	A	26	GLY	0	0.043	0.004	20.795	0.010	0.010	0.000	0.000	0.000	0.000
30	A	27	VAL	0	-0.034	0.015	17.633	-0.035	-0.035	0.000	0.000	0.000	0.000
31	A	28	ILE	0	0.013	-0.003	13.725	0.024	0.024	0.000	0.000	0.000	0.000
32	A	29	ILE	0	-0.030	-0.021	14.696	-0.058	-0.058	0.000	0.000	0.000	0.000
33	A	30	ASN	0	-0.025	-0.020	9.905	0.075	0.075	0.000	0.000	0.000	0.000
34	A	31	LYS	1	0.914	0.949	13.616	0.106	0.106	0.000	0.000	0.000	0.000
35	A	32	GLU	-1	-0.859	-0.937	13.586	-0.146	-0.146	0.000	0.000	0.000	0.000
36	A	33	GLU	-1	-0.987	-0.976	15.739	-0.069	-0.069	0.000	0.000	0.000	0.000
37	A	34	SER	0	-0.051	-0.019	18.686	0.016	0.016	0.000	0.000	0.000	0.000
38	A	35	GLY	0	0.015	0.029	18.416	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	36	THR	0	-0.051	-0.069	19.036	0.006	0.006	0.000	0.000	0.000	0.000
40	A	37	GLY	0	0.052	0.055	16.558	0.001	0.001	0.000	0.000	0.000	0.000
41	A	38	TRP	0	-0.023	-0.030	9.226	-0.057	-0.057	0.000	0.000	0.000	0.000
42	A	39	LEU	0	-0.029	-0.004	16.601	0.022	0.022	0.000	0.000	0.000	0.000
43	A	40	LEU	0	-0.023	0.005	18.163	-0.031	-0.031	0.000	0.000	0.000	0.000
44	A	41	GLU	-1	-0.923	-0.959	19.806	-0.098	-0.098	0.000	0.000	0.000	0.000
45	A	42	ILE	0	-0.004	0.002	21.882	-0.017	-0.017	0.000	0.000	0.000	0.000
46	A	43	VAL	0	0.001	0.004	24.104	0.012	0.012	0.000	0.000	0.000	0.000
47	A	44	ILE	0	0.029	0.021	26.812	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	45	SER	0	0.059	0.019	29.355	0.005	0.005	0.000	0.000	0.000	0.000
49	A	46	ASN	0	0.070	0.010	32.992	0.000	0.000	0.000	0.000	0.000	0.000
50	A	47	GLU	-1	-0.959	-0.970	35.099	-0.043	-0.043	0.000	0.000	0.000	0.000
51	A	48	HIS	1	0.896	0.947	32.030	0.057	0.057	0.000	0.000	0.000	0.000
52	A	49	TYR	0	0.054	0.000	33.617	0.000	0.000	0.000	0.000	0.000	0.000
53	A	50	GLU	-1	-0.886	-0.953	35.462	-0.034	-0.034	0.000	0.000	0.000	0.000
54	A	51	THR	0	-0.027	0.001	31.977	0.001	0.001	0.000	0.000	0.000	0.000
55	A	52	PHE	0	0.009	-0.012	27.144	0.001	0.001	0.000	0.000	0.000	0.000
56	A	53	LYS	1	0.874	0.956	32.178	0.033	0.033	0.000	0.000	0.000	0.000
57	A	54	GLU	-1	-0.890	-0.948	35.081	-0.021	-0.021	0.000	0.000	0.000	0.000
58	A	55	TYR	0	-0.043	-0.040	29.823	0.003	0.003	0.000	0.000	0.000	0.000
59	A	56	GLN	0	-0.050	-0.029	31.538	0.001	0.001	0.000	0.000	0.000	0.000
60	A	57	ASP	-1	-0.890	-0.942	32.471	-0.027	-0.027	0.000	0.000	0.000	0.000
61	A	58	ASN	0	-0.047	-0.019	34.491	0.003	0.003	0.000	0.000	0.000	0.000
62	A	59	GLU	-1	-0.977	-0.980	31.166	-0.017	-0.017	0.000	0.000	0.000	0.000
63	A	60	GLN	0	-0.074	-0.017	29.472	0.002	0.002	0.000	0.000	0.000	0.000
64	A	61	LEU	0	0.007	0.004	25.826	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	62	LEU	0	-0.065	-0.037	24.760	0.001	0.001	0.000	0.000	0.000	0.000
66	A	63	ASP	-1	-0.729	-0.821	21.190	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	64	ILE	0	-0.018	-0.013	18.862	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	65	ARG	1	0.763	0.881	17.565	0.029	0.029	0.000	0.000	0.000	0.000
69	A	66	VAL	0	0.030	0.015	15.239	-0.006	-0.006	0.000	0.000	0.000	0.000
70	A	67	VAL	0	-0.002	0.018	14.411	-0.022	-0.022	0.000	0.000	0.000	0.000
71	A	68	ILE	0	0.043	0.015	10.273	-0.012	-0.012	0.000	0.000	0.000	0.000
72	A	69	THR	0	-0.044	-0.012	12.029	-0.050	-0.050	0.000	0.000	0.000	0.000
73	A	70	ARG	1	0.903	0.916	13.138	0.424	0.424	0.000	0.000	0.000	0.000
74	A	71	PRO	0	0.039	0.025	15.179	-0.005	-0.005	0.000	0.000	0.000	0.000
75	A	72	ALA	0	-0.001	-0.010	16.120	0.019	0.019	0.000	0.000	0.000	0.000
76	A	73	ASN	0	-0.040	-0.014	10.844	0.061	0.061	0.000	0.000	0.000	0.000
77	A	74	ASP	-1	-0.860	-0.926	11.592	-0.019	-0.019	0.000	0.000	0.000	0.000
78	A	75	PRO	0	-0.083	-0.043	12.176	-0.045	-0.045	0.000	0.000	0.000	0.000
79	A	76	ALA	0	0.002	0.014	11.063	0.024	0.024	0.000	0.000	0.000	0.000
80	A	77	LEU	0	-0.033	-0.027	12.800	0.001	0.001	0.000	0.000	0.000	0.000
81	A	78	PHE	0	0.007	-0.011	12.879	0.003	0.003	0.000	0.000	0.000	0.000
82	A	79	GLU	-1	-0.901	-0.941	17.351	0.011	0.011	0.000	0.000	0.000	0.000
83	A	80	SER	0	-0.052	-0.041	20.560	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	81	THR	0	0.107	0.067	22.577	0.003	0.003	0.000	0.000	0.000	0.000
85	A	82	VAL	0	0.001	-0.006	25.316	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	83	LYS	1	0.978	0.999	25.215	0.062	0.062	0.000	0.000	0.000	0.000
87	A	84	SER	0	-0.084	-0.054	28.116	0.003	0.003	0.000	0.000	0.000	0.000
88	A	85	ILE	0	0.057	0.032	29.224	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	86	LYS	1	0.919	0.965	31.656	0.072	0.072	0.000	0.000	0.000	0.000
90	A	87	ASN	0	0.019	0.008	33.187	-0.005	-0.005	0.000	0.000	0.000	0.000
91	A	88	PHE	0	-0.017	-0.011	31.634	0.001	0.001	0.000	0.000	0.000	0.000
92	A	89	LYS	1	0.928	0.963	36.862	0.051	0.051	0.000	0.000	0.000	0.000
93	A	90	THR	0	0.035	0.012	36.496	0.002	0.002	0.000	0.000	0.000	0.000
94	A	91	THR	0	-0.005	0.010	32.047	0.001	0.001	0.000	0.000	0.000	0.000
95	A	92	MET	0	-0.030	0.007	30.943	0.005	0.005	0.000	0.000	0.000	0.000
96	A	93	SER	0	-0.027	0.003	27.895	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	94	ILE	0	0.016	0.003	26.707	0.008	0.008	0.000	0.000	0.000	0.000
98	A	95	VAL	0	0.008	0.012	23.733	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	96	PHE	0	-0.001	-0.020	21.824	0.011	0.011	0.000	0.000	0.000	0.000
100	A	97	GLU	-1	-0.926	-0.969	21.843	-0.052	-0.052	0.000	0.000	0.000	0.000
101	A	98	CYS	0	-0.049	-0.027	17.668	0.010	0.010	0.000	0.000	0.000	0.000
102	A	99	HIS	0	0.078	0.044	17.115	-0.006	-0.006	0.000	0.000	0.000	0.000
103	A	100	ILE	0	-0.064	-0.020	10.262	0.001	0.001	0.000	0.000	0.000	0.000
104	A	101	TYR	0	-0.064	-0.087	14.376	0.029	0.029	0.000	0.000	0.000	0.000
105	A	102	THR	0	0.007	-0.003	11.771	-0.017	-0.017	0.000	0.000	0.000	0.000
106	A	103	LEU	0	-0.030	-0.005	13.838	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	104	ARG	1	0.804	0.881	16.135	-0.039	-0.039	0.000	0.000	0.000	0.000
108	A	105	GLN	0	0.049	0.002	16.119	-0.010	-0.010	0.000	0.000	0.000	0.000
109	A	106	GLN	0	0.011	0.002	19.668	-0.007	-0.007	0.000	0.000	0.000	0.000
110	A	107	TYR	0	-0.005	-0.005	20.715	-0.011	-0.011	0.000	0.000	0.000	0.000
111	A	108	ALA	0	0.018	-0.004	22.702	-0.011	-0.011	0.000	0.000	0.000	0.000
112	A	109	GLU	-1	-0.845	-0.938	24.890	0.081	0.081	0.000	0.000	0.000	0.000
113	A	110	SER	0	0.031	0.015	25.660	-0.005	-0.005	0.000	0.000	0.000	0.000
114	A	111	LEU	0	-0.047	-0.013	25.755	-0.006	-0.006	0.000	0.000	0.000	0.000
115	A	112	LEU	0	-0.052	-0.041	27.885	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	113	GLU	-1	-0.947	-0.974	30.538	0.045	0.045	0.000	0.000	0.000	0.000
117	A	114	GLN	0	0.075	0.047	29.819	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	115	LEU	0	-0.047	-0.036	30.725	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	116	ILE	0	-0.016	-0.014	33.912	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	117	ASP	-1	-0.896	-0.925	35.692	0.029	0.029	0.000	0.000	0.000	0.000
121	A	118	ASP	-1	-0.957	-0.969	34.964	0.016	0.016	0.000	0.000	0.000	0.000
122	A	119	GLY	0	-0.047	-0.030	38.011	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	120	LEU	0	-0.068	-0.029	35.290	-0.002	-0.002	0.000	0.000	0.000	0.000
124	A	121	SER	0	0.018	-0.007	38.899	0.002	0.002	0.000	0.000	0.000	0.000
125	A	122	GLY	0	0.021	0.002	40.025	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	123	GLU	-1	-0.805	-0.900	38.201	0.011	0.011	0.000	0.000	0.000	0.000
127	A	124	GLU	-1	-0.893	-0.943	37.465	0.005	0.005	0.000	0.000	0.000	0.000
128	A	125	LEU	0	-0.008	0.018	33.961	0.000	0.000	0.000	0.000	0.000	0.000
129	A	126	LYS	1	0.869	0.898	33.524	-0.013	-0.013	0.000	0.000	0.000	0.000
130	A	127	LYS	1	0.920	0.978	32.521	0.002	0.002	0.000	0.000	0.000	0.000
131	A	128	SER	0	-0.037	-0.045	31.971	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	129	PHE	0	0.058	0.041	27.300	-0.001	-0.001	0.000	0.000	0.000	0.000
133	A	130	ASN	0	0.030	0.005	27.847	0.005	0.005	0.000	0.000	0.000	0.000
134	A	131	ARG	1	0.755	0.886	26.933	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	132	MET	0	-0.014	-0.005	26.128	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	133	MET	0	0.011	0.017	22.738	0.003	0.003	0.000	0.000	0.000	0.000
137	A	134	GLN	0	-0.058	-0.020	21.639	-0.003	-0.003	0.000	0.000	0.000	0.000
138	A	135	SER	0	-0.049	-0.027	21.048	-0.001	-0.001	0.000	0.000	0.000	0.000
139	A	136	LYS	1	0.930	0.969	16.500	-0.028	-0.028	0.000	0.000	0.000	0.000
140	A	137	PRO	0	0.013	0.035	21.742	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	138	LYS	1	0.969	0.999	20.042	-0.026	-0.026	0.000	0.000	0.000	0.000
142	A	139	LEU	0	-0.028	0.000	24.208	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	140	LYS	1	0.919	0.938	26.683	-0.018	-0.018	0.000	0.000	0.000	0.000
144	A	141	ASP	-1	-0.807	-0.861	27.106	0.050	0.050	0.000	0.000	0.000	0.000
145	A	142	GLU	-1	-0.904	-0.961	22.677	0.058	0.058	0.000	0.000	0.000	0.000
146	A	143	LYS	1	0.863	0.942	27.159	-0.014	-0.014	0.000	0.000	0.000	0.000
147	A	144	LEU	0	0.011	0.002	29.763	0.002	0.002	0.000	0.000	0.000	0.000
148	A	145	NME	0	-0.002	0.009	32.925	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-2:ACE )