FMO DATABASE

FMODB ID: 5J21Z

Calculation Name: 3EQZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EQZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q483U6

Base Structure: X-ray

Registration Date: 2023-09-21

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	124
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1055133.953511
FMO2-HF: Nuclear repulsion	1006488.239997
FMO2-HF: Total energy	-48645.713514
FMO2-MP2: Total energy	-48785.776913

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:2:LEU)

Summations of interaction energy for fragment #1(A:2:LEU)

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.
-18.768	-6.828	12.267	-8.439	-15.769	-0.05

Interaction energy analysis for fragmet #1(A:2:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.057 / q_NPA : -0.034

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

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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	4	ARG	1	0.853	0.927	3.855	-4.041	0.246	-0.038	-2.315	-1.934	-0.004
4	A	5	VAL	0	-0.019	-0.001	4.890	-0.369	-0.222	-0.001	-0.008	-0.137	0.000
5	A	6	PHE	0	0.032	0.020	7.027	0.163	0.163	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.024	-0.011	10.008	-0.083	-0.083	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.007	-0.007	12.636	0.060	0.060	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.762	-0.896	15.005	-0.236	-0.236	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.851	-0.930	18.281	-0.119	-0.119	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.814	-0.868	21.388	-0.157	-0.157	0.000	0.000	0.000	0.000
11	A	12	THR	0	-0.038	-0.031	21.330	-0.013	-0.013	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.037	-0.028	21.669	-0.011	-0.011	0.000	0.000	0.000	0.000
13	A	14	THR	0	0.001	-0.023	17.473	-0.021	-0.021	0.000	0.000	0.000	0.000
14	A	15	CYS	0	-0.016	0.033	17.093	-0.034	-0.034	0.000	0.000	0.000	0.000
15	A	16	ASN	0	-0.019	-0.011	16.989	-0.026	-0.026	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.012	0.021	17.955	-0.017	-0.017	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.015	-0.004	13.097	-0.035	-0.035	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.897	0.933	13.648	0.197	0.197	0.000	0.000	0.000	0.000
19	A	20	THR	0	-0.070	-0.029	14.350	-0.018	-0.018	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.014	-0.008	12.625	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	22	VAL	0	0.006	-0.003	8.557	-0.071	-0.071	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.878	-0.913	10.458	-0.363	-0.363	0.000	0.000	0.000	0.000
23	A	24	PRO	0	-0.045	-0.024	12.433	0.003	0.003	0.000	0.000	0.000	0.000
24	A	25	ILE	0	-0.059	-0.024	7.499	0.020	0.020	0.000	0.000	0.000	0.000
25	A	26	PHE	0	0.002	-0.011	3.099	-0.669	0.018	0.059	-0.170	-0.576	0.000
26	A	27	GLY	0	0.028	0.016	8.177	0.126	0.126	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.032	-0.016	8.632	0.062	0.062	0.000	0.000	0.000	0.000
28	A	29	VAL	0	0.015	0.007	8.739	-0.093	-0.093	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.919	-0.962	10.694	0.096	0.096	0.000	0.000	0.000	0.000
30	A	31	ALA	0	0.001	-0.007	12.743	-0.045	-0.045	0.000	0.000	0.000	0.000
31	A	32	PHE	0	-0.023	-0.019	14.352	0.042	0.042	0.000	0.000	0.000	0.000
32	A	33	GLN	0	0.027	-0.015	17.498	0.001	0.001	0.000	0.000	0.000	0.000
33	A	34	HIS	0	0.006	0.004	20.287	0.008	0.008	0.000	0.000	0.000	0.000
34	A	35	PRO	0	0.053	0.019	18.116	0.012	0.012	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.833	0.875	18.546	0.059	0.059	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.009	0.008	19.957	0.015	0.015	0.000	0.000	0.000	0.000
37	A	38	PHE	0	0.028	0.023	10.716	0.019	0.019	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.022	-0.009	15.411	0.020	0.020	0.000	0.000	0.000	0.000
39	A	40	THR	0	-0.098	-0.045	17.290	0.025	0.025	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.039	-0.003	13.425	0.031	0.031	0.000	0.000	0.000	0.000
41	A	42	SER	0	-0.023	-0.003	13.696	-0.018	-0.018	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.025	-0.007	8.554	0.048	0.048	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.004	-0.026	6.423	0.529	0.529	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.973	0.978	4.923	-0.787	-0.787	0.000	0.000	0.000	0.000
45	A	46	GLN	0	-0.042	-0.017	2.180	-2.154	-0.810	3.566	-2.088	-2.823	-0.009
46	A	47	ASP	-1	-0.731	-0.828	2.579	-1.255	-0.650	1.730	-0.482	-1.853	-0.021
47	A	48	ILE	0	0.014	0.009	2.258	-2.063	-1.398	4.194	-1.151	-3.709	-0.004
48	A	49	ILE	0	-0.007	-0.008	4.225	0.195	0.278	0.000	-0.029	-0.054	0.000
49	A	50	ILE	0	-0.012	-0.009	7.846	-0.058	-0.058	0.000	0.000	0.000	0.000
50	A	51	LEU	0	0.000	0.002	10.482	0.067	0.067	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.758	-0.880	13.437	-0.225	-0.225	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.045	-0.034	17.013	0.022	0.022	0.000	0.000	0.000	0.000
53	A	54	MET	0	-0.050	-0.018	17.889	0.026	0.026	0.000	0.000	0.000	0.000
54	A	55	MET	0	-0.062	0.009	21.899	0.015	0.015	0.000	0.000	0.000	0.000
55	A	56	PRO	0	0.001	-0.022	24.763	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.866	-0.952	25.879	-0.076	-0.076	0.000	0.000	0.000	0.000
57	A	58	MET	0	-0.070	-0.036	23.303	0.007	0.007	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.714	-0.832	21.317	-0.062	-0.062	0.000	0.000	0.000	0.000
59	A	60	GLY	0	0.011	0.010	18.204	0.002	0.002	0.000	0.000	0.000	0.000
60	A	61	ILE	0	-0.017	-0.017	18.044	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.802	-0.859	19.782	-0.015	-0.015	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.010	-0.001	14.469	0.013	0.013	0.000	0.000	0.000	0.000
63	A	64	ILE	0	0.003	-0.002	14.811	0.010	0.010	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.760	0.837	16.245	0.018	0.018	0.000	0.000	0.000	0.000
65	A	66	HIS	0	0.061	0.031	15.919	0.005	0.005	0.000	0.000	0.000	0.000
66	A	67	LEU	0	0.000	-0.008	11.232	0.031	0.031	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.042	0.029	14.319	0.028	0.028	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.903	-0.932	16.093	0.059	0.059	0.000	0.000	0.000	0.000
69	A	70	HIS	0	-0.094	-0.056	15.782	0.028	0.028	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.799	0.898	14.326	-0.036	-0.036	0.000	0.000	0.000	0.000
71	A	72	SER	0	0.024	0.019	9.957	0.084	0.084	0.000	0.000	0.000	0.000
72	A	73	PRO	0	-0.023	-0.014	7.594	-0.037	-0.037	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.021	0.008	5.244	0.031	0.031	0.000	0.000	0.000	0.000
74	A	75	SER	0	0.008	-0.004	2.380	-1.741	-0.513	0.776	-0.712	-1.292	-0.004
75	A	76	LEU	0	-0.043	-0.010	4.862	-0.076	-0.039	-0.001	-0.007	-0.029	0.000
76	A	77	ILE	0	-0.006	0.001	5.992	-0.031	-0.031	0.000	0.000	0.000	0.000
77	A	78	LEU	0	0.009	0.017	9.486	0.055	0.055	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.008	0.003	13.140	-0.021	-0.021	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.057	0.013	15.660	0.033	0.033	0.000	0.000	0.000	0.000
80	A	81	GLY	0	-0.001	0.008	19.464	-0.010	-0.010	0.000	0.000	0.000	0.000
81	A	82	TYR	0	-0.039	-0.002	22.622	0.013	0.013	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.784	-0.912	23.570	-0.125	-0.125	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.006	0.004	21.995	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.027	0.024	22.107	-0.011	-0.011	0.000	0.000	0.000	0.000
85	A	86	VAL	0	-0.023	-0.011	22.743	0.000	0.000	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.051	-0.022	16.322	0.001	0.001	0.000	0.000	0.000	0.000
87	A	88	HIS	0	-0.027	-0.021	18.221	0.004	0.004	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.003	-0.012	19.535	0.005	0.005	0.000	0.000	0.000	0.000
89	A	90	ALA	0	-0.010	0.001	18.383	0.007	0.007	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.849	-0.923	14.238	-0.317	-0.317	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.005	-0.005	16.027	0.003	0.003	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.049	-0.035	18.399	0.014	0.014	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.026	0.010	14.172	0.019	0.019	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.008	0.002	11.861	0.016	0.016	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.045	-0.003	14.806	0.025	0.025	0.000	0.000	0.000	0.000
96	A	97	CYS	0	-0.138	-0.073	16.860	0.025	0.025	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.014	-0.009	14.467	0.025	0.025	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.033	-0.005	11.184	0.018	0.018	0.000	0.000	0.000	0.000
99	A	100	ASN	0	0.003	-0.009	4.823	0.070	0.070	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.004	0.006	7.513	-0.141	-0.141	0.000	0.000	0.000	0.000
101	A	102	ILE	0	-0.038	-0.018	3.781	-0.225	-0.013	0.004	-0.030	-0.186	0.000
102	A	103	ASN	0	0.001	-0.012	7.800	0.067	0.067	0.000	0.000	0.000	0.000
103	A	104	THR	0	-0.020	-0.006	10.435	0.027	0.027	0.000	0.000	0.000	0.000
104	A	105	PHE	0	-0.007	-0.005	10.207	-0.011	-0.011	0.000	0.000	0.000	0.000
105	A	106	THR	0	0.044	0.022	15.368	0.016	0.016	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.742	0.859	18.385	0.210	0.210	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.013	-0.017	20.609	0.014	0.014	0.000	0.000	0.000	0.000
108	A	109	ILE	0	0.014	0.008	15.509	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	110	ASN	0	0.028	0.022	17.456	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	111	THR	0	0.031	0.001	16.151	-0.037	-0.037	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.854	-0.901	15.597	-0.351	-0.351	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.023	0.009	13.785	-0.046	-0.046	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.021	0.015	10.015	-0.072	-0.072	0.000	0.000	0.000	0.000
114	A	115	THR	0	-0.022	-0.027	10.709	-0.122	-0.122	0.000	0.000	0.000	0.000
115	A	116	CYS	0	-0.068	-0.038	11.228	-0.090	-0.090	0.000	0.000	0.000	0.000
116	A	117	PHE	0	0.026	0.023	6.792	-0.099	-0.099	0.000	0.000	0.000	0.000
117	A	118	LEU	0	0.051	0.023	6.263	-0.230	-0.230	0.000	0.000	0.000	0.000
118	A	119	THR	0	-0.030	-0.037	6.473	-0.346	-0.346	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.104	-0.044	7.338	-0.106	-0.106	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.019	0.022	2.303	-0.966	-0.427	1.778	-0.405	-1.912	0.002
121	A	122	SER	0	-0.064	-0.027	3.062	-3.929	-2.051	0.201	-1.033	-1.046	-0.010
122	A	123	ASN	0	-0.004	-0.015	4.443	-0.445	-0.217	-0.001	-0.009	-0.218	0.000
123	A	124	ARG	1	0.821	0.925	6.499	1.223	1.223	0.000	0.000	0.000	0.000
124	A	125	GLN	0	0.018	0.014	10.057	-0.050	-0.050	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LEU)