FMO DATABASE

FMODB ID: J3Z79

Calculation Name: 4ZZK-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4ZZK

Chain ID: A

ChEMBL ID:

UniProt ID: B5Z7R3

Base Structure: X-ray

Registration Date: 2023-06-20

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	146
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1329043.591248
FMO2-HF: Nuclear repulsion	1271462.842505
FMO2-HF: Total energy	-57580.748743
FMO2-MP2: Total energy	-57749.137669

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:127:ASN)

Summations of interaction energy for fragment #1(A:127:ASN)

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.
-3.598	-0.907	1.858	-1.97	-2.578	-0.003

Interaction energy analysis for fragmet #1(A:127:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.008 / q_NPA : -0.021

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	129	VAL	0	0.075	0.024	3.853	-0.889	0.433	-0.010	-0.594	-0.717	0.001
4	A	130	SER	0	-0.031	-0.011	6.014	-0.218	-0.218	0.000	0.000	0.000	0.000
5	A	131	MET	0	0.020	0.019	7.894	-0.119	-0.119	0.000	0.000	0.000	0.000
6	A	132	ILE	0	0.017	0.019	8.941	-0.145	-0.145	0.000	0.000	0.000	0.000
7	A	133	GLY	0	-0.004	0.001	11.622	-0.024	-0.024	0.000	0.000	0.000	0.000
8	A	134	LYS	1	0.765	0.888	12.796	-0.917	-0.917	0.000	0.000	0.000	0.000
9	A	135	ILE	0	0.011	0.019	15.848	-0.016	-0.016	0.000	0.000	0.000	0.000
10	A	136	ALA	0	0.019	-0.002	14.592	0.087	0.087	0.000	0.000	0.000	0.000
11	A	137	GLU	-1	-0.753	-0.843	16.643	0.436	0.436	0.000	0.000	0.000	0.000
12	A	138	THR	0	-0.037	-0.045	15.693	0.087	0.087	0.000	0.000	0.000	0.000
13	A	139	ASP	-1	-0.887	-0.948	17.874	0.639	0.639	0.000	0.000	0.000	0.000
14	A	140	VAL	0	0.011	0.013	18.550	-0.072	-0.072	0.000	0.000	0.000	0.000
15	A	141	SER	0	-0.011	-0.017	21.184	-0.015	-0.015	0.000	0.000	0.000	0.000
16	A	142	GLY	0	-0.038	-0.020	24.599	-0.032	-0.032	0.000	0.000	0.000	0.000
17	A	143	ALA	0	0.017	0.017	25.064	0.020	0.020	0.000	0.000	0.000	0.000
18	A	144	ASN	0	0.027	0.009	26.959	-0.017	-0.017	0.000	0.000	0.000	0.000
19	A	145	PHE	0	0.016	0.030	28.786	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	146	ASP	-1	-0.822	-0.913	31.979	0.104	0.104	0.000	0.000	0.000	0.000
21	A	147	GLY	0	0.041	0.012	33.427	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	148	ASN	0	-0.091	-0.053	36.416	-0.007	-0.007	0.000	0.000	0.000	0.000
23	A	149	ASN	0	-0.052	-0.046	34.025	-0.010	-0.010	0.000	0.000	0.000	0.000
24	A	150	LYS	1	0.817	0.899	34.374	-0.082	-0.082	0.000	0.000	0.000	0.000
25	A	151	LEU	0	0.005	0.005	28.388	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	152	SER	0	0.011	0.002	27.836	-0.005	-0.005	0.000	0.000	0.000	0.000
27	A	153	PHE	0	-0.018	-0.019	26.069	0.016	0.016	0.000	0.000	0.000	0.000
28	A	154	SER	0	0.058	0.033	23.045	-0.014	-0.014	0.000	0.000	0.000	0.000
29	A	155	LEU	0	-0.045	-0.017	24.903	0.025	0.025	0.000	0.000	0.000	0.000
30	A	156	PHE	0	0.029	0.023	21.763	-0.014	-0.014	0.000	0.000	0.000	0.000
31	A	157	PHE	0	0.016	0.020	24.755	0.009	0.009	0.000	0.000	0.000	0.000
32	A	158	ASP	-1	-0.733	-0.836	24.652	0.367	0.367	0.000	0.000	0.000	0.000
33	A	159	GLU	-1	-0.896	-0.952	26.699	0.212	0.212	0.000	0.000	0.000	0.000
34	A	160	LYS	1	0.880	0.937	30.183	-0.143	-0.143	0.000	0.000	0.000	0.000
35	A	161	ILE	0	0.009	0.019	31.864	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	162	ASP	-1	-0.814	-0.875	34.588	0.125	0.125	0.000	0.000	0.000	0.000
37	A	163	ALA	0	-0.003	-0.023	38.203	0.003	0.003	0.000	0.000	0.000	0.000
38	A	164	SER	0	-0.098	-0.050	40.722	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	165	LYS	1	0.858	0.924	37.799	-0.158	-0.158	0.000	0.000	0.000	0.000
40	A	166	GLY	0	0.013	0.004	40.415	0.008	0.008	0.000	0.000	0.000	0.000
41	A	167	VAL	0	-0.026	-0.025	41.842	-0.006	-0.006	0.000	0.000	0.000	0.000
42	A	168	PRO	0	0.000	0.017	36.677	0.006	0.006	0.000	0.000	0.000	0.000
43	A	169	ALA	0	0.000	-0.023	36.704	-0.011	-0.011	0.000	0.000	0.000	0.000
44	A	170	ILE	0	0.006	0.008	32.101	0.013	0.013	0.000	0.000	0.000	0.000
45	A	171	GLN	0	-0.066	-0.056	33.983	-0.001	-0.001	0.000	0.000	0.000	0.000
46	A	172	ILE	0	0.029	0.015	33.445	0.016	0.016	0.000	0.000	0.000	0.000
47	A	173	LEU	0	-0.007	-0.008	33.637	-0.011	-0.011	0.000	0.000	0.000	0.000
48	A	174	ASN	0	0.014	-0.012	33.637	0.018	0.018	0.000	0.000	0.000	0.000
49	A	175	GLU	-1	-0.845	-0.941	32.307	0.199	0.199	0.000	0.000	0.000	0.000
50	A	176	ASN	0	-0.046	-0.015	34.125	0.014	0.014	0.000	0.000	0.000	0.000
51	A	177	ASN	0	-0.046	-0.016	33.801	0.007	0.007	0.000	0.000	0.000	0.000
52	A	178	GLU	-1	-0.827	-0.887	36.339	0.137	0.137	0.000	0.000	0.000	0.000
53	A	179	LEU	0	-0.040	-0.024	38.278	0.005	0.005	0.000	0.000	0.000	0.000
54	A	180	VAL	0	-0.015	-0.009	37.833	-0.010	-0.010	0.000	0.000	0.000	0.000
55	A	181	LYS	1	0.826	0.909	37.732	-0.122	-0.122	0.000	0.000	0.000	0.000
56	A	182	THR	0	-0.002	0.001	37.989	0.014	0.014	0.000	0.000	0.000	0.000
57	A	183	ILE	0	-0.021	-0.007	34.856	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	184	PRO	0	-0.004	0.008	37.327	0.009	0.009	0.000	0.000	0.000	0.000
59	A	185	LEU	0	0.020	-0.005	33.415	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	186	LYS	1	0.849	0.909	37.281	-0.102	-0.102	0.000	0.000	0.000	0.000
61	A	187	ASP	-1	-0.866	-0.924	39.676	0.101	0.101	0.000	0.000	0.000	0.000
62	A	188	TYR	0	0.017	0.021	33.621	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	189	ASN	0	0.038	0.016	35.275	0.013	0.013	0.000	0.000	0.000	0.000
64	A	190	GLY	0	-0.042	-0.028	36.057	-0.006	-0.006	0.000	0.000	0.000	0.000
65	A	191	GLN	0	-0.011	-0.005	31.364	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	192	LYS	1	0.913	0.939	26.378	-0.251	-0.251	0.000	0.000	0.000	0.000
67	A	193	GLY	0	0.008	0.023	24.966	-0.010	-0.010	0.000	0.000	0.000	0.000
68	A	194	TYR	0	0.001	-0.018	18.239	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	195	ILE	0	-0.048	-0.006	24.775	-0.026	-0.026	0.000	0.000	0.000	0.000
70	A	196	ASN	0	-0.044	-0.041	25.383	0.035	0.035	0.000	0.000	0.000	0.000
71	A	197	PHE	0	-0.001	-0.009	28.545	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	198	GLU	-1	-0.805	-0.891	30.470	0.106	0.106	0.000	0.000	0.000	0.000
73	A	199	TRP	0	-0.016	-0.007	33.034	0.003	0.003	0.000	0.000	0.000	0.000
74	A	200	ASP	-1	-0.809	-0.886	34.943	0.108	0.108	0.000	0.000	0.000	0.000
75	A	201	GLY	0	0.054	0.015	36.825	-0.005	-0.005	0.000	0.000	0.000	0.000
76	A	202	THR	0	-0.126	-0.077	37.627	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	203	ASN	0	0.076	0.023	40.082	0.005	0.005	0.000	0.000	0.000	0.000
78	A	204	GLU	-1	-0.793	-0.913	42.179	0.121	0.121	0.000	0.000	0.000	0.000
79	A	205	LYS	1	0.771	0.872	44.542	-0.094	-0.094	0.000	0.000	0.000	0.000
80	A	206	GLY	0	0.025	0.029	44.860	-0.005	-0.005	0.000	0.000	0.000	0.000
81	A	207	GLU	-1	-0.843	-0.895	45.421	0.084	0.084	0.000	0.000	0.000	0.000
82	A	208	LYS	1	0.847	0.928	39.178	-0.086	-0.086	0.000	0.000	0.000	0.000
83	A	209	VAL	0	-0.007	0.012	37.513	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	210	PRO	0	0.003	0.009	38.912	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	211	LYS	1	0.925	0.977	31.247	-0.139	-0.139	0.000	0.000	0.000	0.000
86	A	212	GLY	0	-0.008	-0.008	32.831	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	213	ASN	0	-0.057	-0.032	27.039	0.003	0.003	0.000	0.000	0.000	0.000
88	A	214	TYR	0	-0.013	-0.034	30.268	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	215	LYS	1	0.856	0.932	28.786	-0.230	-0.230	0.000	0.000	0.000	0.000
90	A	216	ILE	0	0.009	0.014	28.832	-0.020	-0.020	0.000	0.000	0.000	0.000
91	A	217	LYS	1	0.902	0.961	28.650	-0.217	-0.217	0.000	0.000	0.000	0.000
92	A	218	ALA	0	0.001	-0.006	30.688	-0.019	-0.019	0.000	0.000	0.000	0.000
93	A	219	GLU	-1	-0.853	-0.898	32.233	0.213	0.213	0.000	0.000	0.000	0.000
94	A	220	TYR	0	0.005	-0.016	28.871	-0.019	-0.019	0.000	0.000	0.000	0.000
95	A	221	ASN	0	0.002	-0.004	34.430	0.000	0.000	0.000	0.000	0.000	0.000
96	A	222	LEU	0	-0.025	0.001	36.976	0.007	0.007	0.000	0.000	0.000	0.000
97	A	223	ASP	-1	-0.763	-0.860	37.799	0.170	0.170	0.000	0.000	0.000	0.000
98	A	224	SER	0	-0.005	-0.007	39.691	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	225	HIS	0	-0.086	-0.035	41.754	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	226	SER	0	-0.027	-0.059	39.208	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	227	LYS	1	0.854	0.926	41.564	-0.140	-0.140	0.000	0.000	0.000	0.000
102	A	228	GLN	0	0.011	0.014	37.153	0.002	0.002	0.000	0.000	0.000	0.000
103	A	229	TYR	0	0.039	0.031	35.978	-0.007	-0.007	0.000	0.000	0.000	0.000
104	A	230	LEU	0	0.002	0.024	31.557	0.015	0.015	0.000	0.000	0.000	0.000
105	A	231	GLN	0	0.015	-0.017	30.375	-0.012	-0.012	0.000	0.000	0.000	0.000
106	A	232	THR	0	-0.038	-0.024	26.137	0.031	0.031	0.000	0.000	0.000	0.000
107	A	233	ARG	1	0.772	0.873	21.067	-0.545	-0.545	0.000	0.000	0.000	0.000
108	A	234	ILE	0	0.037	0.020	23.760	0.019	0.019	0.000	0.000	0.000	0.000
109	A	235	GLY	0	0.024	0.020	20.504	0.010	0.010	0.000	0.000	0.000	0.000
110	A	236	ARG	1	0.727	0.823	19.622	-0.367	-0.367	0.000	0.000	0.000	0.000
111	A	237	GLY	0	0.040	0.008	19.203	-0.065	-0.065	0.000	0.000	0.000	0.000
112	A	238	GLU	-1	-0.942	-0.958	17.247	0.463	0.463	0.000	0.000	0.000	0.000
113	A	239	VAL	0	-0.007	0.017	11.023	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	240	GLU	-1	-0.820	-0.922	14.275	0.293	0.293	0.000	0.000	0.000	0.000
115	A	241	SER	0	-0.048	-0.034	11.611	-0.143	-0.143	0.000	0.000	0.000	0.000
116	A	242	VAL	0	-0.016	-0.007	5.248	0.153	0.153	0.000	0.000	0.000	0.000
117	A	243	ILE	0	-0.030	-0.010	8.421	-0.353	-0.353	0.000	0.000	0.000	0.000
118	A	244	PHE	0	0.014	-0.003	2.332	-1.468	-0.332	1.866	-1.298	-1.704	-0.004
119	A	245	ASP	-1	-0.846	-0.912	7.608	-0.350	-0.350	0.000	0.000	0.000	0.000
120	A	246	LYS	1	0.808	0.898	10.034	0.275	0.275	0.000	0.000	0.000	0.000
121	A	247	GLY	0	0.073	0.024	7.535	0.033	0.033	0.000	0.000	0.000	0.000
122	A	248	LYS	1	0.928	0.966	5.786	-0.894	-0.894	0.000	0.000	0.000	0.000
123	A	249	PRO	0	-0.007	0.006	4.128	-0.687	-0.454	0.002	-0.078	-0.157	0.000
124	A	250	MET	0	-0.011	0.007	6.435	-0.020	-0.020	0.000	0.000	0.000	0.000
125	A	251	LEU	0	0.005	0.001	9.266	0.014	0.014	0.000	0.000	0.000	0.000
126	A	252	ARG	1	0.937	0.973	11.300	-0.318	-0.318	0.000	0.000	0.000	0.000
127	A	253	MET	0	-0.054	-0.026	14.123	0.088	0.088	0.000	0.000	0.000	0.000
128	A	254	GLY	0	0.075	0.041	16.890	-0.025	-0.025	0.000	0.000	0.000	0.000
129	A	255	GLU	-1	-0.918	-0.955	18.953	0.172	0.172	0.000	0.000	0.000	0.000
130	A	256	MET	0	-0.076	-0.016	18.790	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	257	ILE	0	-0.004	-0.010	13.502	0.037	0.037	0.000	0.000	0.000	0.000
132	A	258	LEU	0	0.012	0.015	14.250	-0.051	-0.051	0.000	0.000	0.000	0.000
133	A	259	PRO	0	0.044	0.010	11.176	0.151	0.151	0.000	0.000	0.000	0.000
134	A	260	ILE	0	-0.011	0.002	6.267	0.063	0.063	0.000	0.000	0.000	0.000
135	A	261	ASP	-1	-0.954	-0.983	9.581	1.225	1.225	0.000	0.000	0.000	0.000
136	A	262	SER	0	0.012	0.010	11.809	-0.150	-0.150	0.000	0.000	0.000	0.000
137	A	263	ALA	0	-0.020	-0.005	12.248	-0.147	-0.147	0.000	0.000	0.000	0.000
138	A	264	ILE	0	-0.014	-0.017	14.048	0.092	0.092	0.000	0.000	0.000	0.000
139	A	265	GLU	-1	-0.850	-0.905	16.478	0.599	0.599	0.000	0.000	0.000	0.000
140	A	266	PHE	0	0.014	-0.003	11.265	0.035	0.035	0.000	0.000	0.000	0.000
141	A	267	TYR	0	-0.028	-0.020	16.263	-0.033	-0.033	0.000	0.000	0.000	0.000
142	A	268	LYS	1	0.944	0.967	18.384	-0.510	-0.510	0.000	0.000	0.000	0.000
143	A	269	PRO	0	0.085	0.030	19.067	-0.012	-0.012	0.000	0.000	0.000	0.000
144	A	270	ASP	-1	-0.921	-0.949	22.214	0.295	0.295	0.000	0.000	0.000	0.000
145	A	271	GLN	0	-0.067	-0.024	23.244	0.003	0.003	0.000	0.000	0.000	0.000
146	A	272	LYS	1	0.806	0.889	22.797	-0.532	-0.532	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:127:ASN)