FMO DATABASE

FMODB ID: 3Q58L

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1331539.482986
FMO2-HF: Nuclear repulsion	1273958.361205
FMO2-HF: Total energy	-57581.121781
FMO2-MP2: Total energy	-57749.605818

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.
-4.33	-1.619	2.923	-2.622	-3.011	-0.009

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 : 0.021 / q_NPA : -0.007

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	0.051	0.010	3.885	-1.439	0.057	-0.009	-0.659	-0.828	0.001
4	A	130	SER	0	-0.052	-0.024	5.762	-0.269	-0.269	0.000	0.000	0.000	0.000
5	A	131	MET	0	0.028	0.025	7.687	-0.167	-0.167	0.000	0.000	0.000	0.000
6	A	132	ILE	0	0.026	0.024	9.094	-0.193	-0.193	0.000	0.000	0.000	0.000
7	A	133	GLY	0	0.004	0.010	11.706	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	134	LYS	1	0.749	0.875	12.616	-1.087	-1.087	0.000	0.000	0.000	0.000
9	A	135	ILE	0	0.007	0.020	15.806	0.016	0.016	0.000	0.000	0.000	0.000
10	A	136	ALA	0	0.022	0.004	14.502	0.121	0.121	0.000	0.000	0.000	0.000
11	A	137	GLU	-1	-0.755	-0.843	16.466	0.548	0.548	0.000	0.000	0.000	0.000
12	A	138	THR	0	-0.022	-0.031	15.086	0.126	0.126	0.000	0.000	0.000	0.000
13	A	139	ASP	-1	-0.823	-0.917	17.610	0.793	0.793	0.000	0.000	0.000	0.000
14	A	140	VAL	0	-0.019	-0.006	18.251	-0.105	-0.105	0.000	0.000	0.000	0.000
15	A	141	SER	0	-0.012	-0.013	20.841	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	142	GLY	0	-0.011	-0.013	24.207	-0.042	-0.042	0.000	0.000	0.000	0.000
17	A	143	ALA	0	-0.006	0.011	24.945	0.032	0.032	0.000	0.000	0.000	0.000
18	A	144	ASN	0	-0.003	0.002	26.809	-0.027	-0.027	0.000	0.000	0.000	0.000
19	A	145	PHE	0	0.015	0.031	28.740	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	146	ASP	-1	-0.804	-0.905	31.784	0.170	0.170	0.000	0.000	0.000	0.000
21	A	147	GLY	0	0.025	0.008	33.178	-0.007	-0.007	0.000	0.000	0.000	0.000
22	A	148	ASN	0	-0.082	-0.051	36.296	-0.012	-0.012	0.000	0.000	0.000	0.000
23	A	149	ASN	0	-0.052	-0.038	33.933	-0.013	-0.013	0.000	0.000	0.000	0.000
24	A	150	LYS	1	0.822	0.898	33.395	-0.141	-0.141	0.000	0.000	0.000	0.000
25	A	151	LEU	0	0.012	0.001	28.320	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	152	SER	0	-0.017	-0.030	28.031	0.001	0.001	0.000	0.000	0.000	0.000
27	A	153	PHE	0	-0.035	-0.020	26.119	0.020	0.020	0.000	0.000	0.000	0.000
28	A	154	SER	0	0.042	0.021	22.903	-0.021	-0.021	0.000	0.000	0.000	0.000
29	A	155	LEU	0	-0.039	-0.008	24.716	0.031	0.031	0.000	0.000	0.000	0.000
30	A	156	PHE	0	0.028	0.028	21.586	-0.015	-0.015	0.000	0.000	0.000	0.000
31	A	157	PHE	0	0.010	0.018	24.536	0.002	0.002	0.000	0.000	0.000	0.000
32	A	158	ASP	-1	-0.730	-0.840	24.280	0.468	0.468	0.000	0.000	0.000	0.000
33	A	159	GLU	-1	-0.869	-0.930	26.522	0.243	0.243	0.000	0.000	0.000	0.000
34	A	160	LYS	1	0.845	0.909	30.155	-0.183	-0.183	0.000	0.000	0.000	0.000
35	A	161	ILE	0	0.034	0.034	31.421	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	162	ASP	-1	-0.788	-0.861	34.338	0.158	0.158	0.000	0.000	0.000	0.000
37	A	163	ALA	0	-0.018	-0.021	38.025	0.004	0.004	0.000	0.000	0.000	0.000
38	A	164	SER	0	-0.084	-0.045	40.910	-0.007	-0.007	0.000	0.000	0.000	0.000
39	A	165	LYS	1	0.835	0.919	37.093	-0.199	-0.199	0.000	0.000	0.000	0.000
40	A	166	GLY	0	0.010	0.006	40.288	0.012	0.012	0.000	0.000	0.000	0.000
41	A	167	VAL	0	-0.030	-0.028	41.783	-0.008	-0.008	0.000	0.000	0.000	0.000
42	A	168	PRO	0	0.003	0.020	36.563	0.007	0.007	0.000	0.000	0.000	0.000
43	A	169	ALA	0	0.001	-0.012	36.608	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	170	ILE	0	0.009	0.009	31.901	0.017	0.017	0.000	0.000	0.000	0.000
45	A	171	GLN	0	-0.044	-0.037	33.579	-0.003	-0.003	0.000	0.000	0.000	0.000
46	A	172	ILE	0	0.025	0.018	33.038	0.022	0.022	0.000	0.000	0.000	0.000
47	A	173	LEU	0	0.005	-0.002	33.380	-0.018	-0.018	0.000	0.000	0.000	0.000
48	A	174	ASN	0	0.013	-0.019	33.325	0.024	0.024	0.000	0.000	0.000	0.000
49	A	175	GLU	-1	-0.818	-0.911	31.848	0.276	0.276	0.000	0.000	0.000	0.000
50	A	176	ASN	0	-0.047	-0.021	33.689	0.021	0.021	0.000	0.000	0.000	0.000
51	A	177	ASN	0	-0.052	-0.020	33.233	0.019	0.019	0.000	0.000	0.000	0.000
52	A	178	GLU	-1	-0.809	-0.876	35.724	0.187	0.187	0.000	0.000	0.000	0.000
53	A	179	LEU	0	-0.025	-0.012	37.889	0.008	0.008	0.000	0.000	0.000	0.000
54	A	180	VAL	0	-0.044	-0.020	37.607	-0.012	-0.012	0.000	0.000	0.000	0.000
55	A	181	LYS	1	0.818	0.906	37.169	-0.170	-0.170	0.000	0.000	0.000	0.000
56	A	182	THR	0	0.002	-0.018	37.542	0.018	0.018	0.000	0.000	0.000	0.000
57	A	183	ILE	0	-0.016	0.000	34.899	-0.013	-0.013	0.000	0.000	0.000	0.000
58	A	184	PRO	0	-0.014	-0.003	37.008	0.011	0.011	0.000	0.000	0.000	0.000
59	A	185	LEU	0	0.019	-0.004	33.131	0.000	0.000	0.000	0.000	0.000	0.000
60	A	186	LYS	1	0.823	0.894	36.985	-0.139	-0.139	0.000	0.000	0.000	0.000
61	A	187	ASP	-1	-0.837	-0.907	39.319	0.138	0.138	0.000	0.000	0.000	0.000
62	A	188	TYR	0	0.045	0.026	33.207	-0.005	-0.005	0.000	0.000	0.000	0.000
63	A	189	ASN	0	-0.002	0.007	34.973	0.013	0.013	0.000	0.000	0.000	0.000
64	A	190	GLY	0	-0.012	-0.006	35.819	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	191	GLN	0	0.002	0.003	30.841	-0.007	-0.007	0.000	0.000	0.000	0.000
66	A	192	LYS	1	0.890	0.944	26.143	-0.325	-0.325	0.000	0.000	0.000	0.000
67	A	193	GLY	0	0.010	0.020	24.500	-0.014	-0.014	0.000	0.000	0.000	0.000
68	A	194	TYR	0	-0.016	-0.030	18.058	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	195	ILE	0	-0.054	-0.011	24.391	-0.035	-0.035	0.000	0.000	0.000	0.000
70	A	196	ASN	0	-0.023	-0.033	25.081	0.045	0.045	0.000	0.000	0.000	0.000
71	A	197	PHE	0	0.000	-0.008	28.203	-0.022	-0.022	0.000	0.000	0.000	0.000
72	A	198	GLU	-1	-0.768	-0.860	30.281	0.174	0.174	0.000	0.000	0.000	0.000
73	A	199	TRP	0	-0.018	-0.002	32.767	0.002	0.002	0.000	0.000	0.000	0.000
74	A	200	ASP	-1	-0.796	-0.876	34.931	0.158	0.158	0.000	0.000	0.000	0.000
75	A	201	GLY	0	0.029	0.010	36.661	-0.008	-0.008	0.000	0.000	0.000	0.000
76	A	202	THR	0	-0.102	-0.075	37.433	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	203	ASN	0	0.072	0.012	39.729	0.007	0.007	0.000	0.000	0.000	0.000
78	A	204	GLU	-1	-0.787	-0.887	41.767	0.168	0.168	0.000	0.000	0.000	0.000
79	A	205	LYS	1	0.764	0.878	43.931	-0.131	-0.131	0.000	0.000	0.000	0.000
80	A	206	GLY	0	0.009	0.017	44.615	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	207	GLU	-1	-0.826	-0.885	45.255	0.122	0.122	0.000	0.000	0.000	0.000
82	A	208	LYS	1	0.855	0.926	39.049	-0.133	-0.133	0.000	0.000	0.000	0.000
83	A	209	VAL	0	-0.007	0.013	37.357	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	210	PRO	0	0.008	0.007	39.037	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	211	LYS	1	0.903	0.958	31.058	-0.213	-0.213	0.000	0.000	0.000	0.000
86	A	212	GLY	0	0.024	0.008	32.702	-0.004	-0.004	0.000	0.000	0.000	0.000
87	A	213	ASN	0	-0.074	-0.046	26.759	0.005	0.005	0.000	0.000	0.000	0.000
88	A	214	TYR	0	-0.022	-0.027	30.056	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	215	LYS	1	0.852	0.917	28.301	-0.303	-0.303	0.000	0.000	0.000	0.000
90	A	216	ILE	0	-0.023	-0.006	28.526	-0.026	-0.026	0.000	0.000	0.000	0.000
91	A	217	LYS	1	0.829	0.910	28.324	-0.273	-0.273	0.000	0.000	0.000	0.000
92	A	218	ALA	0	0.019	0.001	30.479	-0.021	-0.021	0.000	0.000	0.000	0.000
93	A	219	GLU	-1	-0.850	-0.897	31.680	0.282	0.282	0.000	0.000	0.000	0.000
94	A	220	TYR	0	-0.010	-0.020	28.549	-0.023	-0.023	0.000	0.000	0.000	0.000
95	A	221	ASN	0	-0.027	-0.056	34.793	0.001	0.001	0.000	0.000	0.000	0.000
96	A	222	LEU	0	0.001	0.012	36.797	0.008	0.008	0.000	0.000	0.000	0.000
97	A	223	ASP	-1	-0.754	-0.843	37.840	0.199	0.199	0.000	0.000	0.000	0.000
98	A	224	SER	0	-0.011	-0.007	39.709	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	225	HIS	0	-0.059	-0.027	41.406	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	226	SER	0	-0.021	-0.049	38.624	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	227	LYS	1	0.820	0.902	40.904	-0.165	-0.165	0.000	0.000	0.000	0.000
102	A	228	GLN	0	0.001	0.004	36.924	0.009	0.009	0.000	0.000	0.000	0.000
103	A	229	TYR	0	0.012	0.014	35.649	-0.008	-0.008	0.000	0.000	0.000	0.000
104	A	230	LEU	0	0.011	0.027	31.327	0.017	0.017	0.000	0.000	0.000	0.000
105	A	231	GLN	0	0.036	0.003	30.121	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	232	THR	0	-0.043	-0.032	26.088	0.040	0.040	0.000	0.000	0.000	0.000
107	A	233	ARG	1	0.772	0.868	20.620	-0.708	-0.708	0.000	0.000	0.000	0.000
108	A	234	ILE	0	0.042	0.025	23.321	0.020	0.020	0.000	0.000	0.000	0.000
109	A	235	GLY	0	0.028	0.017	19.921	0.011	0.011	0.000	0.000	0.000	0.000
110	A	236	ARG	1	0.728	0.817	19.460	-0.469	-0.469	0.000	0.000	0.000	0.000
111	A	237	GLY	0	0.045	0.007	19.437	-0.077	-0.077	0.000	0.000	0.000	0.000
112	A	238	GLU	-1	-0.923	-0.957	17.173	0.608	0.608	0.000	0.000	0.000	0.000
113	A	239	VAL	0	-0.001	0.019	10.888	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	240	GLU	-1	-0.827	-0.917	13.987	0.429	0.429	0.000	0.000	0.000	0.000
115	A	241	SER	0	-0.021	-0.031	11.452	-0.164	-0.164	0.000	0.000	0.000	0.000
116	A	242	VAL	0	-0.010	0.009	4.992	0.106	0.106	0.000	0.000	0.000	0.000
117	A	243	ILE	0	-0.034	-0.010	8.145	-0.484	-0.484	0.000	0.000	0.000	0.000
118	A	244	PHE	0	0.018	-0.003	2.265	-1.540	-0.527	2.931	-1.914	-2.029	-0.010
119	A	245	ASP	-1	-0.814	-0.886	7.290	-0.287	-0.287	0.000	0.000	0.000	0.000
120	A	246	LYS	1	0.797	0.882	10.570	0.119	0.119	0.000	0.000	0.000	0.000
121	A	247	GLY	0	0.054	0.019	7.694	-0.069	-0.069	0.000	0.000	0.000	0.000
122	A	248	LYS	1	0.844	0.917	6.096	-1.242	-1.242	0.000	0.000	0.000	0.000
123	A	249	PRO	0	-0.022	0.001	4.050	-0.509	-0.307	0.001	-0.049	-0.154	0.000
124	A	250	MET	0	-0.035	-0.004	6.249	-0.056	-0.056	0.000	0.000	0.000	0.000
125	A	251	LEU	0	0.020	-0.001	8.859	0.114	0.114	0.000	0.000	0.000	0.000
126	A	252	ARG	1	0.920	0.971	11.151	-0.534	-0.534	0.000	0.000	0.000	0.000
127	A	253	MET	0	-0.053	-0.026	14.005	0.127	0.127	0.000	0.000	0.000	0.000
128	A	254	GLY	0	0.069	0.040	16.970	-0.040	-0.040	0.000	0.000	0.000	0.000
129	A	255	GLU	-1	-0.912	-0.955	18.789	0.283	0.283	0.000	0.000	0.000	0.000
130	A	256	MET	0	-0.073	-0.008	18.500	0.005	0.005	0.000	0.000	0.000	0.000
131	A	257	ILE	0	0.010	-0.007	13.191	0.042	0.042	0.000	0.000	0.000	0.000
132	A	258	LEU	0	0.000	0.008	13.877	-0.070	-0.070	0.000	0.000	0.000	0.000
133	A	259	PRO	0	0.035	0.004	10.638	0.230	0.230	0.000	0.000	0.000	0.000
134	A	260	ILE	0	-0.010	0.004	5.748	0.056	0.056	0.000	0.000	0.000	0.000
135	A	261	ASP	-1	-0.836	-0.925	9.157	1.662	1.662	0.000	0.000	0.000	0.000
136	A	262	SER	0	-0.019	-0.005	11.518	-0.237	-0.237	0.000	0.000	0.000	0.000
137	A	263	ALA	0	-0.022	-0.009	11.894	-0.183	-0.183	0.000	0.000	0.000	0.000
138	A	264	ILE	0	-0.029	-0.019	13.881	0.070	0.070	0.000	0.000	0.000	0.000
139	A	265	GLU	-1	-0.841	-0.901	16.348	0.691	0.691	0.000	0.000	0.000	0.000
140	A	266	PHE	0	0.016	-0.009	10.990	0.103	0.103	0.000	0.000	0.000	0.000
141	A	267	TYR	0	-0.045	-0.025	16.047	-0.071	-0.071	0.000	0.000	0.000	0.000
142	A	268	LYS	1	0.948	0.970	18.200	-0.532	-0.532	0.000	0.000	0.000	0.000
143	A	269	PRO	0	0.092	0.032	18.954	-0.014	-0.014	0.000	0.000	0.000	0.000
144	A	270	ASP	-1	-0.917	-0.954	22.056	0.340	0.340	0.000	0.000	0.000	0.000
145	A	271	GLN	0	-0.058	-0.019	23.247	-0.010	-0.010	0.000	0.000	0.000	0.000
146	A	272	LYS	1	0.799	0.887	22.394	-0.643	-0.643	0.000	0.000	0.000	0.000

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