FMO DATABASE

FMODB ID: 85Z9Y

Calculation Name: 2ZP2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2ZP2

Chain ID: A

ChEMBL ID:

UniProt ID: P60495

Base Structure: X-ray

Registration Date: 2023-09-20

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	OptHSide
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	122
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-966757.239409
FMO2-HF: Nuclear repulsion	921557.701364
FMO2-HF: Total energy	-45199.538045
FMO2-MP2: Total energy	-45332.819821

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:100:ARG)

Summations of interaction energy for fragment #1(A:100:ARG)

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.
-111.751	-107.026	27.883	-14.092	-18.516	-0.162

Interaction energy analysis for fragmet #1(A:100:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.789 / q_NPA : 0.879

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	102	VAL	0	-0.040	-0.020	2.866	-6.226	-4.094	0.152	-0.766	-1.518	0.000
4	A	103	GLU	-1	-0.874	-0.949	5.238	-23.442	-23.350	-0.001	-0.004	-0.086	0.000
5	A	104	ILE	0	-0.047	-0.012	8.279	0.185	0.185	0.000	0.000	0.000	0.000
6	A	105	PRO	0	0.039	0.029	11.019	1.919	1.919	0.000	0.000	0.000	0.000
7	A	106	VAL	0	-0.049	-0.045	14.531	-0.245	-0.245	0.000	0.000	0.000	0.000
8	A	107	CYS	0	-0.049	0.001	17.135	0.976	0.976	0.000	0.000	0.000	0.000
9	A	108	TYR	0	0.035	-0.031	17.709	-0.374	-0.374	0.000	0.000	0.000	0.000
10	A	109	GLY	0	-0.019	-0.003	22.594	0.571	0.571	0.000	0.000	0.000	0.000
11	A	110	GLY	0	0.008	-0.004	25.487	-0.181	-0.181	0.000	0.000	0.000	0.000
12	A	111	GLU	-1	-0.838	-0.926	24.235	-12.991	-12.991	0.000	0.000	0.000	0.000
13	A	112	PHE	0	0.003	0.007	21.618	-0.227	-0.227	0.000	0.000	0.000	0.000
14	A	113	GLY	0	-0.047	-0.014	22.777	-0.517	-0.517	0.000	0.000	0.000	0.000
15	A	114	PRO	0	-0.024	-0.026	24.213	0.454	0.454	0.000	0.000	0.000	0.000
16	A	115	ASP	-1	-0.763	-0.847	25.767	-11.384	-11.384	0.000	0.000	0.000	0.000
17	A	116	LEU	0	0.026	0.010	24.556	-0.024	-0.024	0.000	0.000	0.000	0.000
18	A	117	GLU	-1	-0.862	-0.935	26.850	-9.420	-9.420	0.000	0.000	0.000	0.000
19	A	118	GLU	-1	-0.840	-0.898	29.147	-9.763	-9.763	0.000	0.000	0.000	0.000
20	A	119	VAL	0	-0.003	-0.001	24.615	0.160	0.160	0.000	0.000	0.000	0.000
21	A	120	ALA	0	0.005	0.008	27.852	0.051	0.051	0.000	0.000	0.000	0.000
22	A	121	LYS	1	0.871	0.940	29.758	9.663	9.663	0.000	0.000	0.000	0.000
23	A	122	ILE	0	-0.041	-0.035	29.944	0.211	0.211	0.000	0.000	0.000	0.000
24	A	123	ASN	0	-0.121	-0.059	27.994	0.340	0.340	0.000	0.000	0.000	0.000
25	A	124	GLN	0	-0.017	-0.018	31.079	-0.039	-0.039	0.000	0.000	0.000	0.000
26	A	125	LEU	0	-0.023	0.000	27.648	0.042	0.042	0.000	0.000	0.000	0.000
27	A	126	SER	0	0.019	-0.025	31.045	0.007	0.007	0.000	0.000	0.000	0.000
28	A	127	PRO	0	0.006	-0.023	28.297	-0.377	-0.377	0.000	0.000	0.000	0.000
29	A	128	GLU	-1	-0.801	-0.870	26.767	-12.204	-12.204	0.000	0.000	0.000	0.000
30	A	129	GLU	-1	-0.799	-0.857	26.567	-10.318	-10.318	0.000	0.000	0.000	0.000
31	A	130	VAL	0	-0.031	-0.022	24.143	-0.469	-0.469	0.000	0.000	0.000	0.000
32	A	131	ILE	0	-0.045	-0.009	21.526	-0.717	-0.717	0.000	0.000	0.000	0.000
33	A	132	ASP	-1	-0.896	-0.945	21.015	-13.382	-13.382	0.000	0.000	0.000	0.000
34	A	133	ILE	0	0.003	0.006	21.241	-0.249	-0.249	0.000	0.000	0.000	0.000
35	A	134	HIS	0	-0.020	0.001	16.319	-0.460	-0.460	0.000	0.000	0.000	0.000
36	A	135	THR	0	-0.017	-0.029	16.744	-1.171	-1.171	0.000	0.000	0.000	0.000
37	A	136	ASN	0	-0.063	-0.014	16.394	-0.538	-0.538	0.000	0.000	0.000	0.000
38	A	137	GLY	0	-0.003	0.018	15.285	0.038	0.038	0.000	0.000	0.000	0.000
39	A	138	GLU	-1	-0.901	-0.951	9.704	-20.853	-20.853	0.000	0.000	0.000	0.000
40	A	139	TYR	0	-0.089	-0.052	10.288	1.239	1.239	0.000	0.000	0.000	0.000
41	A	140	VAL	0	0.052	0.037	7.573	-3.230	-3.230	0.000	0.000	0.000	0.000
42	A	141	VAL	0	-0.009	0.001	6.027	2.531	2.531	0.000	0.000	0.000	0.000
43	A	142	TYR	0	-0.055	-0.031	8.733	-0.540	-0.540	0.000	0.000	0.000	0.000
44	A	143	MET	0	-0.017	-0.011	6.909	-0.409	-0.409	0.000	0.000	0.000	0.000
45	A	144	LEU	0	-0.009	-0.035	12.623	0.934	0.934	0.000	0.000	0.000	0.000
46	A	145	GLY	0	0.020	0.008	16.169	0.120	0.120	0.000	0.000	0.000	0.000
47	A	146	PHE	0	0.038	0.053	18.079	-0.176	-0.176	0.000	0.000	0.000	0.000
48	A	147	ALA	0	0.011	0.015	17.786	-0.082	-0.082	0.000	0.000	0.000	0.000
49	A	148	PRO	0	-0.084	-0.028	14.175	-0.564	-0.564	0.000	0.000	0.000	0.000
50	A	149	GLY	0	0.056	0.010	11.058	0.000	0.000	0.000	0.000	0.000	0.000
51	A	150	PHE	0	-0.035	-0.020	10.728	-1.553	-1.553	0.000	0.000	0.000	0.000
52	A	151	PRO	0	-0.029	-0.011	7.956	0.125	0.125	0.000	0.000	0.000	0.000
53	A	152	PHE	0	0.018	0.004	9.918	1.190	1.190	0.000	0.000	0.000	0.000
54	A	153	LEU	0	0.022	0.023	9.410	-2.241	-2.241	0.000	0.000	0.000	0.000
55	A	154	GLY	0	-0.019	-0.009	12.322	2.016	2.016	0.000	0.000	0.000	0.000
56	A	155	GLY	0	0.049	0.005	12.532	-1.119	-1.119	0.000	0.000	0.000	0.000
57	A	156	MET	0	-0.062	0.008	14.747	0.411	0.411	0.000	0.000	0.000	0.000
58	A	157	SER	0	0.081	0.039	17.605	0.803	0.803	0.000	0.000	0.000	0.000
59	A	158	LYS	1	1.001	0.971	20.593	11.175	11.175	0.000	0.000	0.000	0.000
60	A	159	ARG	1	0.844	0.930	23.787	10.644	10.644	0.000	0.000	0.000	0.000
61	A	160	ILE	0	0.049	0.026	22.582	0.302	0.302	0.000	0.000	0.000	0.000
62	A	161	ALA	0	0.006	0.002	24.124	-0.366	-0.366	0.000	0.000	0.000	0.000
63	A	162	ALA	0	0.045	0.024	25.001	0.462	0.462	0.000	0.000	0.000	0.000
64	A	163	PRO	0	0.003	0.032	25.510	-0.442	-0.442	0.000	0.000	0.000	0.000
65	A	164	ARG	1	0.970	0.971	24.070	11.980	11.980	0.000	0.000	0.000	0.000
66	A	165	LYS	1	0.770	0.875	26.549	11.343	11.343	0.000	0.000	0.000	0.000
67	A	166	SER	0	-0.010	-0.010	28.830	-0.193	-0.193	0.000	0.000	0.000	0.000
68	A	167	SER	0	0.030	0.026	31.498	0.151	0.151	0.000	0.000	0.000	0.000
69	A	168	PRO	0	-0.047	-0.034	26.762	-0.259	-0.259	0.000	0.000	0.000	0.000
70	A	169	ARG	1	0.858	0.918	25.056	12.446	12.446	0.000	0.000	0.000	0.000
71	A	170	PRO	0	0.032	0.003	26.547	-0.308	-0.308	0.000	0.000	0.000	0.000
72	A	171	SER	0	-0.044	-0.041	23.297	-0.107	-0.107	0.000	0.000	0.000	0.000
73	A	172	ILE	0	-0.057	-0.004	19.627	0.400	0.400	0.000	0.000	0.000	0.000
74	A	173	PRO	0	0.036	0.024	20.516	-0.365	-0.365	0.000	0.000	0.000	0.000
75	A	174	ALA	0	0.014	0.004	15.645	-0.476	-0.476	0.000	0.000	0.000	0.000
76	A	175	GLY	0	0.014	0.008	14.042	0.444	0.444	0.000	0.000	0.000	0.000
77	A	176	SER	0	-0.018	-0.023	15.105	0.269	0.269	0.000	0.000	0.000	0.000
78	A	177	VAL	0	0.010	0.006	14.610	-1.451	-1.451	0.000	0.000	0.000	0.000
79	A	178	GLY	0	0.021	0.007	16.813	1.228	1.228	0.000	0.000	0.000	0.000
80	A	179	ILE	0	0.012	0.011	17.959	-0.980	-0.980	0.000	0.000	0.000	0.000
81	A	180	ALA	0	-0.045	-0.021	20.371	0.816	0.816	0.000	0.000	0.000	0.000
82	A	181	GLY	0	-0.013	-0.015	21.720	-0.325	-0.325	0.000	0.000	0.000	0.000
83	A	182	LEU	0	0.007	0.005	20.777	0.364	0.364	0.000	0.000	0.000	0.000
84	A	183	GLN	0	0.014	0.021	17.767	-0.720	-0.720	0.000	0.000	0.000	0.000
85	A	184	THR	0	0.054	0.028	14.875	0.410	0.410	0.000	0.000	0.000	0.000
86	A	185	GLY	0	0.007	-0.009	13.049	-0.691	-0.691	0.000	0.000	0.000	0.000
87	A	186	VAL	0	0.001	0.009	10.843	1.393	1.393	0.000	0.000	0.000	0.000
88	A	187	TYR	0	0.036	0.014	12.646	-0.536	-0.536	0.000	0.000	0.000	0.000
89	A	188	PRO	0	-0.009	0.014	10.287	0.306	0.306	0.000	0.000	0.000	0.000
90	A	189	ILE	0	0.046	0.015	12.414	0.685	0.685	0.000	0.000	0.000	0.000
91	A	190	SER	0	-0.006	-0.014	15.740	0.345	0.345	0.000	0.000	0.000	0.000
92	A	191	THR	0	0.011	0.021	17.905	0.422	0.422	0.000	0.000	0.000	0.000
93	A	192	PRO	0	0.039	0.048	20.440	0.131	0.131	0.000	0.000	0.000	0.000
94	A	193	GLY	0	0.017	-0.012	22.363	-0.456	-0.456	0.000	0.000	0.000	0.000
95	A	194	GLY	0	-0.006	-0.007	23.763	0.066	0.066	0.000	0.000	0.000	0.000
96	A	195	TRP	0	-0.012	0.003	16.513	0.344	0.344	0.000	0.000	0.000	0.000
97	A	196	GLN	0	0.024	0.012	22.718	0.263	0.263	0.000	0.000	0.000	0.000
98	A	197	LEU	0	-0.007	-0.014	20.447	-0.648	-0.648	0.000	0.000	0.000	0.000
99	A	198	ILE	0	0.023	0.008	19.678	0.713	0.713	0.000	0.000	0.000	0.000
100	A	199	GLY	0	0.082	0.028	19.805	0.381	0.381	0.000	0.000	0.000	0.000
101	A	200	LYS	1	0.789	0.891	17.488	14.354	14.354	0.000	0.000	0.000	0.000
102	A	201	THR	0	-0.013	0.006	12.795	-0.462	-0.462	0.000	0.000	0.000	0.000
103	A	202	PRO	0	-0.026	0.019	13.675	0.617	0.617	0.000	0.000	0.000	0.000
104	A	203	LEU	0	0.110	-0.004	10.291	-0.687	-0.687	0.000	0.000	0.000	0.000
105	A	204	ALA	0	-0.083	-0.006	7.880	-1.763	-1.763	0.000	0.000	0.000	0.000
106	A	214	THR	0	0.025	0.015	5.643	3.424	3.424	0.000	0.000	0.000	0.000
107	A	215	LEU	0	-0.043	-0.022	2.159	-7.975	-7.685	2.223	-0.843	-1.670	-0.001
108	A	216	LEU	0	0.050	0.031	1.828	-42.979	-44.869	12.578	-5.724	-4.964	-0.081
109	A	217	ARG	1	0.876	0.917	2.577	68.188	70.418	1.274	-0.954	-2.550	0.000
110	A	218	ALA	0	0.033	-0.008	4.448	-1.852	-1.773	-0.001	-0.008	-0.070	0.000
111	A	219	GLY	0	-0.016	-0.010	6.286	-2.238	-2.238	0.000	0.000	0.000	0.000
112	A	220	ASP	-1	-0.801	-0.872	2.054	-116.727	-115.443	11.658	-5.702	-7.241	-0.080
113	A	221	ILE	0	0.016	0.002	3.897	7.614	8.122	0.000	-0.091	-0.417	0.000
114	A	222	VAL	0	-0.016	-0.015	5.483	-3.566	-3.566	0.000	0.000	0.000	0.000
115	A	223	LYS	1	0.868	0.930	8.432	22.943	22.943	0.000	0.000	0.000	0.000
116	A	224	PHE	0	-0.021	-0.012	10.951	-1.293	-1.293	0.000	0.000	0.000	0.000
117	A	225	VAL	0	0.053	0.023	13.401	1.173	1.173	0.000	0.000	0.000	0.000
118	A	226	ARG	1	0.820	0.883	15.488	12.617	12.617	0.000	0.000	0.000	0.000
119	A	227	ILE	0	0.014	0.006	17.342	-0.241	-0.241	0.000	0.000	0.000	0.000
120	A	228	SER	0	-0.019	-0.006	20.244	0.447	0.447	0.000	0.000	0.000	0.000
121	A	229	GLU	-1	-0.756	-0.867	22.441	-11.796	-11.796	0.000	0.000	0.000	0.000
122	A	230	LYS	1	0.786	0.881	22.220	10.790	10.790	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:100:ARG)