FMO DATABASE

FMODB ID: 6NGLZ

Calculation Name: 2ZOV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2ZOV

Chain ID: A

ChEMBL ID:

UniProt ID: P55892

Base Structure: X-ray

Registration Date: 2023-06-22

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	166
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1652676.101423
FMO2-HF: Nuclear repulsion	1587733.792418
FMO2-HF: Total energy	-64942.309005
FMO2-MP2: Total energy	-65132.957246

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:108:LYS)

Summations of interaction energy for fragment #1(A:108: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.
59.385	63.5	3.155	-1.433	-5.839	0.014

Interaction energy analysis for fragmet #1(A:108:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 1.019 / q_NPA : 0.991

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	110	ARG	1	0.997	0.984	2.134	43.517	45.132	2.153	-0.286	-3.482	0.004
4	A	111	MET	0	0.041	0.031	2.778	-2.940	-0.656	1.003	-1.119	-2.169	0.010
5	A	112	GLU	-1	-0.838	-0.900	4.473	-26.221	-26.005	-0.001	-0.028	-0.188	0.000
6	A	113	GLN	0	0.050	0.021	6.387	3.116	3.116	0.000	0.000	0.000	0.000
7	A	114	SER	0	-0.021	-0.023	7.225	2.076	2.076	0.000	0.000	0.000	0.000
8	A	115	ARG	1	0.967	0.990	5.776	25.174	25.174	0.000	0.000	0.000	0.000
9	A	116	LEU	0	0.035	0.022	10.441	1.287	1.287	0.000	0.000	0.000	0.000
10	A	117	ASN	0	0.011	-0.006	11.709	1.662	1.662	0.000	0.000	0.000	0.000
11	A	118	LYS	1	0.827	0.909	13.257	14.981	14.981	0.000	0.000	0.000	0.000
12	A	119	LEU	0	0.030	0.024	14.512	0.732	0.732	0.000	0.000	0.000	0.000
13	A	120	ARG	1	0.903	0.940	16.310	14.809	14.809	0.000	0.000	0.000	0.000
14	A	121	GLY	0	0.035	0.020	17.894	0.617	0.617	0.000	0.000	0.000	0.000
15	A	122	ASP	-1	-0.820	-0.901	18.041	-13.004	-13.004	0.000	0.000	0.000	0.000
16	A	123	LEU	0	-0.025	-0.017	19.773	0.565	0.565	0.000	0.000	0.000	0.000
17	A	124	ASP	-1	-0.887	-0.925	22.284	-10.714	-10.714	0.000	0.000	0.000	0.000
18	A	125	GLN	0	0.006	-0.001	22.893	0.687	0.687	0.000	0.000	0.000	0.000
19	A	126	LEU	0	0.010	0.019	24.831	0.413	0.413	0.000	0.000	0.000	0.000
20	A	127	ILE	0	-0.021	-0.023	25.954	0.400	0.400	0.000	0.000	0.000	0.000
21	A	128	GLU	-1	-0.845	-0.910	28.254	-9.499	-9.499	0.000	0.000	0.000	0.000
22	A	129	SER	0	-0.051	-0.024	28.749	0.322	0.322	0.000	0.000	0.000	0.000
23	A	130	ASP	-1	-0.821	-0.912	31.337	-8.110	-8.110	0.000	0.000	0.000	0.000
24	A	131	PRO	0	-0.036	-0.027	33.120	-0.021	-0.021	0.000	0.000	0.000	0.000
25	A	132	LYS	1	0.862	0.925	35.472	7.687	7.687	0.000	0.000	0.000	0.000
26	A	133	LEU	0	0.000	0.007	29.189	-0.019	-0.019	0.000	0.000	0.000	0.000
27	A	134	ARG	1	0.870	0.930	32.726	8.185	8.185	0.000	0.000	0.000	0.000
28	A	135	ALA	0	-0.024	-0.003	34.001	0.006	0.006	0.000	0.000	0.000	0.000
29	A	136	LEU	0	-0.011	-0.010	33.870	0.136	0.136	0.000	0.000	0.000	0.000
30	A	137	ARG	1	0.878	0.929	26.472	10.078	10.078	0.000	0.000	0.000	0.000
31	A	138	PRO	0	-0.008	-0.004	31.437	-0.233	-0.233	0.000	0.000	0.000	0.000
32	A	139	HIS	0	-0.073	-0.037	33.128	0.099	0.099	0.000	0.000	0.000	0.000
33	A	140	LEU	0	0.008	0.015	28.218	-0.149	-0.149	0.000	0.000	0.000	0.000
34	A	141	LYS	1	0.939	0.972	27.070	10.065	10.065	0.000	0.000	0.000	0.000
35	A	142	ILE	0	0.056	0.026	20.923	-0.238	-0.238	0.000	0.000	0.000	0.000
36	A	143	ASP	-1	-0.817	-0.873	20.771	-12.890	-12.890	0.000	0.000	0.000	0.000
37	A	144	LEU	0	-0.013	-0.002	13.808	-0.188	-0.188	0.000	0.000	0.000	0.000
38	A	145	VAL	0	0.000	0.008	16.989	0.410	0.410	0.000	0.000	0.000	0.000
39	A	146	GLN	0	-0.032	-0.033	15.011	-0.883	-0.883	0.000	0.000	0.000	0.000
40	A	147	GLU	-1	-0.857	-0.933	13.923	-18.033	-18.033	0.000	0.000	0.000	0.000
41	A	148	GLY	0	-0.016	-0.008	13.745	-0.489	-0.489	0.000	0.000	0.000	0.000
42	A	149	LEU	0	-0.035	0.000	14.762	0.382	0.382	0.000	0.000	0.000	0.000
43	A	150	ARG	1	0.829	0.882	16.944	13.212	13.212	0.000	0.000	0.000	0.000
44	A	151	ILE	0	0.028	0.010	20.642	0.181	0.181	0.000	0.000	0.000	0.000
45	A	152	GLN	0	-0.041	-0.023	23.484	0.385	0.385	0.000	0.000	0.000	0.000
46	A	153	ILE	0	0.040	0.017	26.978	0.107	0.107	0.000	0.000	0.000	0.000
47	A	154	ILE	0	-0.046	-0.035	30.077	0.042	0.042	0.000	0.000	0.000	0.000
48	A	155	ASP	-1	-0.769	-0.869	33.231	-7.830	-7.830	0.000	0.000	0.000	0.000
49	A	156	SER	0	0.014	0.003	36.217	0.124	0.124	0.000	0.000	0.000	0.000
50	A	157	GLN	0	0.095	0.038	39.430	-0.056	-0.056	0.000	0.000	0.000	0.000
51	A	158	ASN	0	-0.009	0.003	42.277	0.177	0.177	0.000	0.000	0.000	0.000
52	A	159	ARG	1	0.854	0.925	37.225	7.856	7.856	0.000	0.000	0.000	0.000
53	A	160	PRO	0	0.032	0.049	38.726	-0.249	-0.249	0.000	0.000	0.000	0.000
54	A	161	MET	0	-0.020	-0.025	34.216	0.014	0.014	0.000	0.000	0.000	0.000
55	A	162	PHE	0	-0.007	-0.032	33.558	-0.126	-0.126	0.000	0.000	0.000	0.000
56	A	163	LYS	1	0.885	0.952	39.343	6.894	6.894	0.000	0.000	0.000	0.000
57	A	164	THR	0	0.028	-0.017	42.675	-0.142	-0.142	0.000	0.000	0.000	0.000
58	A	165	GLY	0	0.021	0.020	43.912	0.085	0.085	0.000	0.000	0.000	0.000
59	A	166	SER	0	0.046	0.042	42.539	-0.037	-0.037	0.000	0.000	0.000	0.000
60	A	167	ALA	0	0.032	0.011	37.532	-0.151	-0.151	0.000	0.000	0.000	0.000
61	A	168	GLU	-1	-0.904	-0.939	37.899	-7.021	-7.021	0.000	0.000	0.000	0.000
62	A	169	VAL	0	-0.020	-0.013	34.640	0.013	0.013	0.000	0.000	0.000	0.000
63	A	170	GLU	-1	-0.838	-0.919	37.985	-6.795	-6.795	0.000	0.000	0.000	0.000
64	A	171	PRO	0	-0.043	-0.038	37.902	-0.203	-0.203	0.000	0.000	0.000	0.000
65	A	172	TYR	0	0.046	0.005	36.758	-0.106	-0.106	0.000	0.000	0.000	0.000
66	A	173	MET	0	-0.001	0.025	31.309	-0.295	-0.295	0.000	0.000	0.000	0.000
67	A	174	ARG	1	0.836	0.909	33.008	7.436	7.436	0.000	0.000	0.000	0.000
68	A	175	ASP	-1	-0.835	-0.924	33.103	-7.944	-7.944	0.000	0.000	0.000	0.000
69	A	176	ILE	0	0.000	-0.001	29.314	-0.231	-0.231	0.000	0.000	0.000	0.000
70	A	177	LEU	0	-0.020	-0.013	28.252	-0.339	-0.339	0.000	0.000	0.000	0.000
71	A	178	ARG	1	0.838	0.901	28.055	8.070	8.070	0.000	0.000	0.000	0.000
72	A	179	ALA	0	0.018	0.024	28.905	-0.117	-0.117	0.000	0.000	0.000	0.000
73	A	180	ILE	0	-0.003	-0.011	24.183	-0.279	-0.279	0.000	0.000	0.000	0.000
74	A	181	ALA	0	-0.025	0.005	23.595	-0.475	-0.475	0.000	0.000	0.000	0.000
75	A	182	PRO	0	0.032	0.009	23.080	-0.475	-0.475	0.000	0.000	0.000	0.000
76	A	183	VAL	0	0.004	0.005	20.288	-0.409	-0.409	0.000	0.000	0.000	0.000
77	A	184	LEU	0	-0.031	-0.017	19.028	-0.713	-0.713	0.000	0.000	0.000	0.000
78	A	185	ASN	0	0.037	0.001	18.135	-0.980	-0.980	0.000	0.000	0.000	0.000
79	A	186	GLY	0	-0.006	0.034	17.591	-0.166	-0.166	0.000	0.000	0.000	0.000
80	A	187	ILE	0	-0.080	-0.034	12.424	-0.798	-0.798	0.000	0.000	0.000	0.000
81	A	188	PRO	0	0.028	0.006	11.073	0.489	0.489	0.000	0.000	0.000	0.000
82	A	189	ASN	0	-0.117	-0.068	9.970	0.330	0.330	0.000	0.000	0.000	0.000
83	A	190	ARG	1	0.954	0.990	13.573	15.305	15.305	0.000	0.000	0.000	0.000
84	A	191	ILE	0	0.004	-0.015	16.710	-0.448	-0.448	0.000	0.000	0.000	0.000
85	A	192	SER	0	0.018	0.028	19.466	0.367	0.367	0.000	0.000	0.000	0.000
86	A	193	LEU	0	-0.048	-0.031	21.905	-0.081	-0.081	0.000	0.000	0.000	0.000
87	A	194	ALA	0	0.005	0.002	25.153	0.198	0.198	0.000	0.000	0.000	0.000
88	A	195	GLY	0	0.016	0.016	27.702	0.047	0.047	0.000	0.000	0.000	0.000
89	A	196	HIS	0	-0.015	-0.015	30.136	-0.291	-0.291	0.000	0.000	0.000	0.000
90	A	197	THR	0	-0.045	-0.048	32.969	0.167	0.167	0.000	0.000	0.000	0.000
91	A	198	ASP	-1	-0.795	-0.887	35.883	-8.688	-8.688	0.000	0.000	0.000	0.000
92	A	199	ASP	-1	-0.783	-0.895	38.681	-7.217	-7.217	0.000	0.000	0.000	0.000
93	A	200	PHE	0	-0.025	-0.018	42.075	0.012	0.012	0.000	0.000	0.000	0.000
94	A	201	PRO	0	-0.017	-0.014	45.278	-0.064	-0.064	0.000	0.000	0.000	0.000
95	A	202	TYR	0	-0.004	0.016	43.541	0.008	0.008	0.000	0.000	0.000	0.000
96	A	203	ALA	0	0.040	0.026	46.453	0.103	0.103	0.000	0.000	0.000	0.000
97	A	204	ASN	0	-0.052	-0.044	49.330	0.066	0.066	0.000	0.000	0.000	0.000
98	A	205	GLY	0	0.008	0.003	50.121	-0.028	-0.028	0.000	0.000	0.000	0.000
99	A	206	GLU	-1	-0.868	-0.943	47.806	-6.587	-6.587	0.000	0.000	0.000	0.000
100	A	207	LYS	1	0.869	0.949	48.187	6.217	6.217	0.000	0.000	0.000	0.000
101	A	208	GLY	0	0.019	0.004	47.039	-0.058	-0.058	0.000	0.000	0.000	0.000
102	A	209	TYR	0	-0.122	-0.079	40.453	-0.132	-0.132	0.000	0.000	0.000	0.000
103	A	210	SER	0	0.080	0.019	42.325	0.063	0.063	0.000	0.000	0.000	0.000
104	A	211	ASN	0	0.013	-0.021	40.066	-0.058	-0.058	0.000	0.000	0.000	0.000
105	A	212	TRP	0	0.013	0.012	34.248	-0.379	-0.379	0.000	0.000	0.000	0.000
106	A	213	GLU	-1	-0.778	-0.872	37.232	-7.869	-7.869	0.000	0.000	0.000	0.000
107	A	214	LEU	0	-0.002	0.017	38.165	-0.129	-0.129	0.000	0.000	0.000	0.000
108	A	215	SER	0	-0.059	-0.031	34.516	-0.234	-0.234	0.000	0.000	0.000	0.000
109	A	216	ALA	0	0.041	0.005	33.101	-0.275	-0.275	0.000	0.000	0.000	0.000
110	A	217	ASP	-1	-0.831	-0.889	33.550	-8.064	-8.064	0.000	0.000	0.000	0.000
111	A	218	ARG	1	0.830	0.928	34.658	7.766	7.766	0.000	0.000	0.000	0.000
112	A	219	ALA	0	0.028	0.034	29.690	-0.159	-0.159	0.000	0.000	0.000	0.000
113	A	220	ASN	0	0.005	-0.010	30.271	-0.366	-0.366	0.000	0.000	0.000	0.000
114	A	221	ALA	0	-0.031	-0.005	32.006	-0.026	-0.026	0.000	0.000	0.000	0.000
115	A	222	SER	0	0.014	-0.018	29.770	0.036	0.036	0.000	0.000	0.000	0.000
116	A	223	ARG	1	0.897	0.945	27.006	9.500	9.500	0.000	0.000	0.000	0.000
117	A	224	ARG	1	0.940	0.967	28.879	8.143	8.143	0.000	0.000	0.000	0.000
118	A	225	GLU	-1	-0.729	-0.830	31.566	-8.079	-8.079	0.000	0.000	0.000	0.000
119	A	226	LEU	0	-0.009	0.002	24.827	-0.043	-0.043	0.000	0.000	0.000	0.000
120	A	227	VAL	0	-0.013	-0.004	27.003	-0.066	-0.066	0.000	0.000	0.000	0.000
121	A	228	ALA	0	-0.039	-0.009	28.502	0.066	0.066	0.000	0.000	0.000	0.000
122	A	229	GLY	0	-0.047	-0.037	29.373	0.160	0.160	0.000	0.000	0.000	0.000
123	A	230	GLY	0	0.000	0.005	27.203	-0.065	-0.065	0.000	0.000	0.000	0.000
124	A	231	LEU	0	-0.093	-0.034	21.286	-0.344	-0.344	0.000	0.000	0.000	0.000
125	A	232	ASP	-1	-0.838	-0.918	20.957	-11.531	-11.531	0.000	0.000	0.000	0.000
126	A	233	ASN	0	-0.009	-0.025	23.109	-0.207	-0.207	0.000	0.000	0.000	0.000
127	A	234	GLY	0	0.010	0.014	22.362	-0.203	-0.203	0.000	0.000	0.000	0.000
128	A	235	LYS	1	0.831	0.914	16.808	13.722	13.722	0.000	0.000	0.000	0.000
129	A	236	VAL	0	-0.041	-0.010	19.737	-0.490	-0.490	0.000	0.000	0.000	0.000
130	A	237	LEU	0	-0.041	-0.020	18.197	0.145	0.145	0.000	0.000	0.000	0.000
131	A	238	ARG	1	0.898	0.940	21.654	13.453	13.453	0.000	0.000	0.000	0.000
132	A	239	VAL	0	-0.018	-0.007	24.622	-0.128	-0.128	0.000	0.000	0.000	0.000
133	A	240	VAL	0	-0.015	-0.019	25.916	-0.005	-0.005	0.000	0.000	0.000	0.000
134	A	241	GLY	0	0.059	0.039	28.835	0.118	0.118	0.000	0.000	0.000	0.000
135	A	242	MET	0	-0.048	-0.023	29.620	-0.265	-0.265	0.000	0.000	0.000	0.000
136	A	243	ALA	0	0.052	0.027	33.434	0.071	0.071	0.000	0.000	0.000	0.000
137	A	244	ALA	0	-0.017	0.013	37.027	0.041	0.041	0.000	0.000	0.000	0.000
138	A	245	THR	0	-0.006	-0.003	38.819	0.145	0.145	0.000	0.000	0.000	0.000
139	A	255	ASP	-1	-0.947	-0.982	43.695	-6.786	-6.786	0.000	0.000	0.000	0.000
140	A	256	ALA	0	-0.036	-0.025	41.015	-0.171	-0.171	0.000	0.000	0.000	0.000
141	A	257	ILE	0	-0.031	0.002	40.266	-0.136	-0.136	0.000	0.000	0.000	0.000
142	A	258	ASN	0	-0.038	-0.029	33.628	-0.246	-0.246	0.000	0.000	0.000	0.000
143	A	259	ARG	1	0.771	0.850	35.592	7.562	7.562	0.000	0.000	0.000	0.000
144	A	260	ARG	1	0.825	0.912	28.983	9.944	9.944	0.000	0.000	0.000	0.000
145	A	261	ILE	0	0.000	0.024	28.211	-0.058	-0.058	0.000	0.000	0.000	0.000
146	A	262	SER	0	-0.045	-0.026	25.323	-0.173	-0.173	0.000	0.000	0.000	0.000
147	A	263	LEU	0	0.016	0.010	21.045	-0.017	-0.017	0.000	0.000	0.000	0.000
148	A	264	LEU	0	-0.010	-0.006	17.766	-0.174	-0.174	0.000	0.000	0.000	0.000
149	A	265	VAL	0	0.033	0.006	14.793	-0.110	-0.110	0.000	0.000	0.000	0.000
150	A	266	LEU	0	0.010	0.008	14.997	-0.668	-0.668	0.000	0.000	0.000	0.000
151	A	267	ASN	0	-0.032	0.005	9.900	-0.853	-0.853	0.000	0.000	0.000	0.000
152	A	268	LYS	1	0.901	0.909	8.368	21.465	21.465	0.000	0.000	0.000	0.000
153	A	269	GLN	0	-0.008	-0.007	9.787	-2.236	-2.236	0.000	0.000	0.000	0.000
154	A	270	ALA	0	0.049	0.023	11.201	1.079	1.079	0.000	0.000	0.000	0.000
155	A	271	GLU	-1	-0.822	-0.899	13.613	-17.529	-17.529	0.000	0.000	0.000	0.000
156	A	272	GLN	0	-0.014	-0.024	12.042	0.785	0.785	0.000	0.000	0.000	0.000
157	A	273	ALA	0	-0.008	-0.003	14.874	0.747	0.747	0.000	0.000	0.000	0.000
158	A	274	ILE	0	-0.003	0.005	16.960	0.878	0.878	0.000	0.000	0.000	0.000
159	A	275	LEU	0	-0.026	-0.012	16.481	0.787	0.787	0.000	0.000	0.000	0.000
160	A	276	HIS	0	-0.031	-0.021	15.507	0.940	0.940	0.000	0.000	0.000	0.000
161	A	277	GLU	-1	-0.872	-0.919	20.258	-13.051	-13.051	0.000	0.000	0.000	0.000
162	A	278	ASN	0	-0.095	-0.073	22.591	1.038	1.038	0.000	0.000	0.000	0.000
163	A	279	ALA	0	-0.020	0.021	22.906	0.407	0.407	0.000	0.000	0.000	0.000
164	A	280	GLU	-1	-0.923	-0.961	24.856	-10.315	-10.315	0.000	0.000	0.000	0.000
165	A	281	SER	0	-0.045	-0.029	24.581	0.089	0.089	0.000	0.000	0.000	0.000
166	A	282	GLN	0	-0.020	0.004	23.009	-0.406	-0.406	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:108:LYS)