FMO DATABASE

FMODB ID: QVGRY

Calculation Name: 2X5Y-A-Xray372

Preferred Name: Zinc finger CCCH-type antiviral protein 1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2X5Y

Chain ID: A

ChEMBL ID: CHEMBL4295879

UniProt ID: Q7Z2W4

Base Structure: X-ray

Registration Date: 2023-09-23

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	171
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1945666.747402
FMO2-HF: Nuclear repulsion	1875286.945105
FMO2-HF: Total energy	-70379.802297
FMO2-MP2: Total energy	-70585.835266

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:726:LYS)

Summations of interaction energy for fragment #1(A:726:LYS)

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.
-132.1	-127.986	29.756	-16.337	-17.534	-0.161

Interaction energy analysis for fragmet #1(A:726:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.865 / q_NPA : 0.922

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	728	TYR	0	-0.072	-0.064	2.340	-5.347	0.226	8.496	-5.481	-8.587	-0.024
4	A	729	LYS	1	0.826	0.910	2.797	15.594	17.949	0.392	-1.312	-1.435	-0.015
5	A	730	LEU	0	0.024	0.008	4.104	3.074	3.211	-0.001	-0.007	-0.129	0.000
6	A	731	SER	0	-0.047	-0.037	6.567	1.093	1.093	0.000	0.000	0.000	0.000
7	A	732	GLU	-1	-0.823	-0.884	10.055	-22.685	-22.685	0.000	0.000	0.000	0.000
8	A	733	ILE	0	-0.029	-0.009	12.633	0.841	0.841	0.000	0.000	0.000	0.000
9	A	734	HIS	0	0.046	0.018	16.083	0.238	0.238	0.000	0.000	0.000	0.000
10	A	735	HIS	0	0.080	0.019	18.962	-0.233	-0.233	0.000	0.000	0.000	0.000
11	A	736	LEU	0	-0.010	0.002	21.468	0.565	0.565	0.000	0.000	0.000	0.000
12	A	737	HIS	0	0.019	0.023	19.731	0.532	0.532	0.000	0.000	0.000	0.000
13	A	738	PRO	0	0.069	0.013	22.405	-0.166	-0.166	0.000	0.000	0.000	0.000
14	A	739	GLU	-1	-0.863	-0.894	17.647	-17.382	-17.382	0.000	0.000	0.000	0.000
15	A	740	TYR	0	0.029	0.020	18.094	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	741	VAL	0	0.003	0.008	20.182	0.094	0.094	0.000	0.000	0.000	0.000
17	A	742	ARG	1	0.994	1.010	21.149	14.050	14.050	0.000	0.000	0.000	0.000
18	A	743	VAL	0	-0.023	0.000	17.651	0.193	0.193	0.000	0.000	0.000	0.000
19	A	744	SER	0	0.038	0.006	21.059	0.019	0.019	0.000	0.000	0.000	0.000
20	A	745	GLU	-1	-0.957	-0.979	22.673	-11.167	-11.167	0.000	0.000	0.000	0.000
21	A	746	HIS	0	-0.032	-0.027	22.115	0.613	0.613	0.000	0.000	0.000	0.000
22	A	747	PHE	0	0.014	0.003	20.288	0.199	0.199	0.000	0.000	0.000	0.000
23	A	748	LYS	1	0.946	0.981	23.429	12.267	12.267	0.000	0.000	0.000	0.000
24	A	749	ALA	0	0.026	0.034	26.584	0.609	0.609	0.000	0.000	0.000	0.000
25	A	750	SER	0	-0.045	-0.032	26.478	0.371	0.371	0.000	0.000	0.000	0.000
26	A	751	MET	0	-0.048	-0.004	22.399	0.488	0.488	0.000	0.000	0.000	0.000
27	A	752	LYS	1	0.828	0.903	26.575	10.167	10.167	0.000	0.000	0.000	0.000
28	A	753	ASN	0	0.012	0.017	29.157	0.046	0.046	0.000	0.000	0.000	0.000
29	A	754	PHE	0	0.041	0.018	23.736	-0.123	-0.123	0.000	0.000	0.000	0.000
30	A	755	LYS	1	0.789	0.892	22.849	12.813	12.813	0.000	0.000	0.000	0.000
31	A	756	ILE	0	-0.003	-0.007	17.984	-0.463	-0.463	0.000	0.000	0.000	0.000
32	A	757	GLU	-1	-0.794	-0.868	17.098	-14.637	-14.637	0.000	0.000	0.000	0.000
33	A	758	LYS	1	0.810	0.881	12.461	20.106	20.106	0.000	0.000	0.000	0.000
34	A	759	ILE	0	0.033	0.032	14.312	0.086	0.086	0.000	0.000	0.000	0.000
35	A	760	LYS	1	0.852	0.915	8.209	30.128	30.128	0.000	0.000	0.000	0.000
36	A	761	LYS	1	0.897	0.932	11.516	19.245	19.245	0.000	0.000	0.000	0.000
37	A	762	ILE	0	-0.014	-0.007	7.582	-3.316	-3.316	0.000	0.000	0.000	0.000
38	A	763	GLU	-1	-0.838	-0.890	7.855	-23.639	-23.639	0.000	0.000	0.000	0.000
39	A	764	ASN	0	0.032	-0.007	7.092	-2.178	-2.178	0.000	0.000	0.000	0.000
40	A	765	SER	0	0.076	0.040	8.407	1.285	1.285	0.000	0.000	0.000	0.000
41	A	766	GLU	-1	-0.822	-0.899	7.903	-24.952	-24.952	0.000	0.000	0.000	0.000
42	A	767	LEU	0	-0.035	-0.022	9.968	1.968	1.968	0.000	0.000	0.000	0.000
43	A	768	LEU	0	0.014	0.012	12.432	1.477	1.477	0.000	0.000	0.000	0.000
44	A	769	ASP	-1	-0.878	-0.933	14.378	-16.923	-16.923	0.000	0.000	0.000	0.000
45	A	770	LYS	1	0.790	0.878	14.191	18.223	18.223	0.000	0.000	0.000	0.000
46	A	771	PHE	0	-0.011	0.006	16.583	1.079	1.079	0.000	0.000	0.000	0.000
47	A	772	THR	0	-0.007	-0.020	18.096	1.074	1.074	0.000	0.000	0.000	0.000
48	A	773	TRP	0	-0.001	0.002	20.054	0.960	0.960	0.000	0.000	0.000	0.000
49	A	774	LYS	1	0.890	0.933	21.204	13.125	13.125	0.000	0.000	0.000	0.000
50	A	775	LYS	1	0.858	0.911	21.809	14.128	14.128	0.000	0.000	0.000	0.000
51	A	776	SER	0	-0.019	-0.002	24.217	0.716	0.716	0.000	0.000	0.000	0.000
52	A	777	GLN	0	-0.006	-0.012	25.840	0.855	0.855	0.000	0.000	0.000	0.000
53	A	778	MET	0	-0.064	-0.006	25.797	0.186	0.186	0.000	0.000	0.000	0.000
54	A	779	LYS	1	0.785	0.896	28.461	10.460	10.460	0.000	0.000	0.000	0.000
55	A	780	GLU	-1	-0.743	-0.843	26.263	-11.174	-11.174	0.000	0.000	0.000	0.000
56	A	781	GLU	-1	-0.807	-0.884	24.020	-13.259	-13.259	0.000	0.000	0.000	0.000
57	A	782	GLY	0	-0.022	-0.013	22.252	0.113	0.113	0.000	0.000	0.000	0.000
58	A	783	LYS	1	0.789	0.876	23.237	11.849	11.849	0.000	0.000	0.000	0.000
59	A	784	LEU	0	0.007	-0.002	18.983	-0.541	-0.541	0.000	0.000	0.000	0.000
60	A	785	LEU	0	0.004	0.022	20.740	0.633	0.633	0.000	0.000	0.000	0.000
61	A	786	PHE	0	-0.015	-0.025	19.388	-1.189	-1.189	0.000	0.000	0.000	0.000
62	A	787	TYR	0	-0.033	-0.050	15.994	0.014	0.014	0.000	0.000	0.000	0.000
63	A	788	ALA	0	0.046	0.021	16.507	-1.286	-1.286	0.000	0.000	0.000	0.000
64	A	789	THR	0	0.010	-0.002	13.515	0.408	0.408	0.000	0.000	0.000	0.000
65	A	790	SER	0	0.039	0.031	14.699	-0.701	-0.701	0.000	0.000	0.000	0.000
66	A	791	ARG	1	0.826	0.854	9.750	21.252	21.252	0.000	0.000	0.000	0.000
67	A	792	ALA	0	-0.017	-0.007	9.396	-3.372	-3.372	0.000	0.000	0.000	0.000
68	A	793	TYR	0	-0.005	0.000	9.516	-2.560	-2.560	0.000	0.000	0.000	0.000
69	A	794	VAL	0	0.007	0.008	5.369	-1.156	-1.156	0.000	0.000	0.000	0.000
70	A	795	GLU	-1	-0.703	-0.808	1.722	-141.575	-145.699	20.871	-9.517	-7.231	-0.122
71	A	796	SER	0	-0.023	0.018	5.081	1.441	1.508	-0.001	0.000	-0.066	0.000
72	A	797	ILE	0	-0.003	0.010	7.884	0.931	0.931	0.000	0.000	0.000	0.000
73	A	798	CYS	0	-0.032	-0.016	5.159	3.134	3.134	0.000	0.000	0.000	0.000
74	A	799	SER	0	-0.031	-0.028	4.330	2.029	2.135	-0.001	-0.020	-0.086	0.000
75	A	800	ASN	0	0.010	-0.015	6.162	3.491	3.491	0.000	0.000	0.000	0.000
76	A	801	ASN	0	0.021	0.003	9.656	2.624	2.624	0.000	0.000	0.000	0.000
77	A	802	PHE	0	0.040	0.013	11.951	-0.690	-0.690	0.000	0.000	0.000	0.000
78	A	803	ASP	-1	-0.780	-0.890	14.322	-16.847	-16.847	0.000	0.000	0.000	0.000
79	A	804	SER	0	0.029	0.025	16.641	-0.200	-0.200	0.000	0.000	0.000	0.000
80	A	805	PHE	0	-0.039	-0.023	19.265	1.007	1.007	0.000	0.000	0.000	0.000
81	A	806	LEU	0	-0.022	-0.007	13.189	0.075	0.075	0.000	0.000	0.000	0.000
82	A	807	HIS	0	-0.004	-0.017	12.056	-0.213	-0.213	0.000	0.000	0.000	0.000
83	A	808	GLU	-1	-0.793	-0.855	16.622	-14.688	-14.688	0.000	0.000	0.000	0.000
84	A	809	THR	0	-0.046	-0.034	20.094	0.276	0.276	0.000	0.000	0.000	0.000
85	A	810	HIS	0	-0.007	0.017	22.626	0.663	0.663	0.000	0.000	0.000	0.000
86	A	811	GLU	-1	-0.821	-0.895	25.224	-9.801	-9.801	0.000	0.000	0.000	0.000
87	A	812	ASN	0	-0.029	-0.018	28.622	-0.260	-0.260	0.000	0.000	0.000	0.000
88	A	813	LYS	1	0.863	0.913	29.616	10.075	10.075	0.000	0.000	0.000	0.000
89	A	814	TYR	0	-0.004	-0.015	29.345	0.413	0.413	0.000	0.000	0.000	0.000
90	A	815	GLY	0	0.094	0.063	29.777	0.102	0.102	0.000	0.000	0.000	0.000
91	A	816	LYS	1	0.860	0.932	23.400	12.608	12.608	0.000	0.000	0.000	0.000
92	A	817	GLY	0	0.005	0.008	23.870	-0.338	-0.338	0.000	0.000	0.000	0.000
93	A	818	ILE	0	-0.058	-0.041	17.692	-0.163	-0.163	0.000	0.000	0.000	0.000
94	A	819	TYR	0	-0.023	-0.038	21.598	0.510	0.510	0.000	0.000	0.000	0.000
95	A	820	PHE	0	0.008	0.010	17.215	-0.419	-0.419	0.000	0.000	0.000	0.000
96	A	821	ALA	0	-0.003	-0.004	22.330	0.744	0.744	0.000	0.000	0.000	0.000
97	A	822	LYS	1	0.885	0.938	23.876	9.940	9.940	0.000	0.000	0.000	0.000
98	A	823	ASP	-1	-0.856	-0.912	26.100	-10.963	-10.963	0.000	0.000	0.000	0.000
99	A	824	ALA	0	0.047	0.024	22.513	-0.113	-0.113	0.000	0.000	0.000	0.000
100	A	825	ILE	0	0.009	-0.011	23.698	-0.194	-0.194	0.000	0.000	0.000	0.000
101	A	826	TYR	0	-0.058	-0.049	25.983	0.347	0.347	0.000	0.000	0.000	0.000
102	A	827	SER	0	0.067	0.030	21.290	-0.288	-0.288	0.000	0.000	0.000	0.000
103	A	828	HIS	0	0.076	0.049	22.320	-0.674	-0.674	0.000	0.000	0.000	0.000
104	A	829	LYS	1	0.888	0.951	23.285	10.523	10.523	0.000	0.000	0.000	0.000
105	A	830	ASN	0	-0.041	-0.021	25.162	0.660	0.660	0.000	0.000	0.000	0.000
106	A	831	CYS	0	-0.052	-0.001	19.599	-0.492	-0.492	0.000	0.000	0.000	0.000
107	A	832	PRO	0	0.009	0.013	21.123	0.259	0.259	0.000	0.000	0.000	0.000
108	A	833	TYR	0	0.004	-0.009	18.351	-0.220	-0.220	0.000	0.000	0.000	0.000
109	A	834	ASP	-1	-0.791	-0.878	20.819	-13.952	-13.952	0.000	0.000	0.000	0.000
110	A	835	ALA	0	0.084	0.027	19.795	-0.865	-0.865	0.000	0.000	0.000	0.000
111	A	836	LYS	1	0.857	0.916	19.304	13.653	13.653	0.000	0.000	0.000	0.000
112	A	837	ASN	0	-0.022	-0.013	15.834	-1.447	-1.447	0.000	0.000	0.000	0.000
113	A	838	VAL	0	-0.037	0.003	15.074	-1.492	-1.492	0.000	0.000	0.000	0.000
114	A	839	VAL	0	-0.028	-0.003	11.467	-0.550	-0.550	0.000	0.000	0.000	0.000
115	A	840	MET	0	-0.018	0.000	14.701	0.682	0.682	0.000	0.000	0.000	0.000
116	A	841	PHE	0	0.010	-0.005	9.092	-1.014	-1.014	0.000	0.000	0.000	0.000
117	A	842	VAL	0	-0.010	-0.008	14.655	1.610	1.610	0.000	0.000	0.000	0.000
118	A	843	ALA	0	0.001	0.002	15.298	-1.553	-1.553	0.000	0.000	0.000	0.000
119	A	844	GLN	0	-0.028	-0.006	16.903	1.856	1.856	0.000	0.000	0.000	0.000
120	A	845	VAL	0	0.001	-0.006	18.777	-0.572	-0.572	0.000	0.000	0.000	0.000
121	A	846	LEU	0	-0.011	0.004	21.484	0.620	0.620	0.000	0.000	0.000	0.000
122	A	847	VAL	0	0.006	-0.001	24.105	-0.035	-0.035	0.000	0.000	0.000	0.000
123	A	848	GLY	0	0.019	0.017	26.641	0.245	0.245	0.000	0.000	0.000	0.000
124	A	849	LYS	1	0.841	0.920	29.414	9.024	9.024	0.000	0.000	0.000	0.000
125	A	850	PHE	0	0.008	0.006	30.725	-0.141	-0.141	0.000	0.000	0.000	0.000
126	A	851	ILE	0	-0.008	-0.017	32.644	0.347	0.347	0.000	0.000	0.000	0.000
127	A	852	GLU	-1	-0.741	-0.849	33.558	-8.820	-8.820	0.000	0.000	0.000	0.000
128	A	853	GLY	0	0.004	0.001	32.539	0.019	0.019	0.000	0.000	0.000	0.000
129	A	854	ASN	0	-0.003	0.008	33.182	0.222	0.222	0.000	0.000	0.000	0.000
130	A	855	ILE	0	0.038	0.028	32.825	-0.222	-0.222	0.000	0.000	0.000	0.000
131	A	856	THR	0	-0.040	-0.030	32.681	-0.228	-0.228	0.000	0.000	0.000	0.000
132	A	857	TYR	0	-0.012	0.000	31.325	0.053	0.053	0.000	0.000	0.000	0.000
133	A	858	THR	0	0.048	0.010	28.853	-0.279	-0.279	0.000	0.000	0.000	0.000
134	A	859	SER	0	-0.060	-0.032	27.939	-0.401	-0.401	0.000	0.000	0.000	0.000
135	A	860	PRO	0	0.013	0.016	28.169	0.229	0.229	0.000	0.000	0.000	0.000
136	A	861	PRO	0	0.017	0.020	31.296	0.080	0.080	0.000	0.000	0.000	0.000
137	A	862	PRO	0	0.043	0.004	34.078	-0.174	-0.174	0.000	0.000	0.000	0.000
138	A	863	GLN	0	-0.028	-0.020	35.171	0.093	0.093	0.000	0.000	0.000	0.000
139	A	864	PHE	0	0.004	0.021	32.728	0.151	0.151	0.000	0.000	0.000	0.000
140	A	865	ASP	-1	-0.821	-0.903	27.881	-10.697	-10.697	0.000	0.000	0.000	0.000
141	A	866	SER	0	-0.073	-0.053	26.848	-0.509	-0.509	0.000	0.000	0.000	0.000
142	A	867	CYS	0	-0.040	-0.011	28.463	0.484	0.484	0.000	0.000	0.000	0.000
143	A	868	VAL	0	0.005	0.007	29.050	-0.431	-0.431	0.000	0.000	0.000	0.000
144	A	869	ASP	-1	-0.764	-0.885	31.265	-9.924	-9.924	0.000	0.000	0.000	0.000
145	A	870	THR	0	-0.031	-0.026	33.165	0.385	0.385	0.000	0.000	0.000	0.000
146	A	871	ARG	1	0.863	0.897	35.139	8.152	8.152	0.000	0.000	0.000	0.000
147	A	872	SER	0	-0.044	-0.013	36.557	0.089	0.089	0.000	0.000	0.000	0.000
148	A	873	ASN	0	-0.047	-0.024	34.896	0.135	0.135	0.000	0.000	0.000	0.000
149	A	874	PRO	0	-0.017	0.032	31.280	-0.132	-0.132	0.000	0.000	0.000	0.000
150	A	875	SER	0	-0.028	-0.048	29.919	-0.215	-0.215	0.000	0.000	0.000	0.000
151	A	876	VAL	0	-0.034	-0.009	26.582	-0.496	-0.496	0.000	0.000	0.000	0.000
152	A	877	PHE	0	-0.014	-0.012	25.249	0.378	0.378	0.000	0.000	0.000	0.000
153	A	878	VAL	0	-0.022	0.002	24.624	-0.622	-0.622	0.000	0.000	0.000	0.000
154	A	879	ILE	0	-0.013	-0.006	21.588	0.443	0.443	0.000	0.000	0.000	0.000
155	A	880	PHE	0	0.054	0.010	22.905	-0.393	-0.393	0.000	0.000	0.000	0.000
156	A	881	GLN	0	0.018	0.019	21.426	-0.092	-0.092	0.000	0.000	0.000	0.000
157	A	882	LYS	1	0.856	0.917	14.153	19.188	19.188	0.000	0.000	0.000	0.000
158	A	883	ASP	-1	-0.799	-0.888	17.520	-16.742	-16.742	0.000	0.000	0.000	0.000
159	A	884	GLN	0	-0.039	-0.030	18.781	0.381	0.381	0.000	0.000	0.000	0.000
160	A	885	VAL	0	-0.001	0.003	15.947	0.377	0.377	0.000	0.000	0.000	0.000
161	A	886	TYR	0	-0.004	0.005	11.381	-1.026	-1.026	0.000	0.000	0.000	0.000
162	A	887	PRO	0	0.001	-0.004	10.920	0.802	0.802	0.000	0.000	0.000	0.000
163	A	888	GLN	0	-0.012	0.008	11.936	-0.251	-0.251	0.000	0.000	0.000	0.000
164	A	889	TYR	0	-0.049	-0.072	12.723	-0.533	-0.533	0.000	0.000	0.000	0.000
165	A	890	VAL	0	0.013	0.016	8.913	0.008	0.008	0.000	0.000	0.000	0.000
166	A	891	ILE	0	-0.007	-0.002	12.252	0.125	0.125	0.000	0.000	0.000	0.000
167	A	892	GLU	-1	-0.800	-0.871	11.666	-24.350	-24.350	0.000	0.000	0.000	0.000
168	A	893	TYR	0	-0.066	-0.073	15.229	0.609	0.609	0.000	0.000	0.000	0.000
169	A	894	THR	0	-0.016	-0.025	19.008	0.050	0.050	0.000	0.000	0.000	0.000
170	A	895	GLU	-1	-0.915	-0.960	22.065	-11.408	-11.408	0.000	0.000	0.000	0.000
171	A	896	ASP	-1	-0.905	-0.942	25.795	-11.523	-11.523	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:726:LYS)