FMO DATABASE

FMODB ID: 4J91N

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	OptH
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	-1053818.559089
FMO2-HF: Nuclear repulsion	1005173.567045
FMO2-HF: Total energy	-48644.992044
FMO2-MP2: Total energy	-48785.108363

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.
-18.362	-7.192	12.084	-7.843	-15.406	-0.055

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

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	4	ARG	1	0.884	0.952	3.855	-4.344	0.252	-0.041	-2.462	-2.092	-0.005
4	A	5	VAL	0	-0.006	0.003	4.856	-0.462	-0.314	-0.001	-0.008	-0.138	0.000
5	A	6	PHE	0	0.024	0.011	7.009	0.208	0.208	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.018	-0.005	10.054	-0.090	-0.090	0.000	0.000	0.000	0.000
7	A	8	VAL	0	-0.003	-0.014	12.509	0.067	0.067	0.000	0.000	0.000	0.000
8	A	9	ASP	-1	-0.747	-0.894	15.023	-0.258	-0.258	0.000	0.000	0.000	0.000
9	A	10	ASP	-1	-0.830	-0.919	18.340	-0.143	-0.143	0.000	0.000	0.000	0.000
10	A	11	ASP	-1	-0.836	-0.864	21.520	-0.173	-0.173	0.000	0.000	0.000	0.000
11	A	12	THR	0	-0.024	-0.032	21.317	-0.014	-0.014	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.032	-0.029	21.665	-0.012	-0.012	0.000	0.000	0.000	0.000
13	A	14	THR	0	-0.017	-0.036	17.744	-0.020	-0.020	0.000	0.000	0.000	0.000
14	A	15	CYS	0	-0.037	0.008	17.089	-0.037	-0.037	0.000	0.000	0.000	0.000
15	A	16	ASN	0	-0.025	-0.013	16.992	-0.028	-0.028	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.007	0.010	18.051	-0.016	-0.016	0.000	0.000	0.000	0.000
17	A	18	LEU	0	0.015	-0.005	13.362	-0.035	-0.035	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.977	0.982	13.672	0.212	0.212	0.000	0.000	0.000	0.000
19	A	20	THR	0	-0.048	-0.006	14.382	-0.018	-0.018	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.010	-0.009	12.698	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	22	VAL	0	0.004	-0.006	8.639	-0.067	-0.067	0.000	0.000	0.000	0.000
22	A	23	GLU	-1	-0.961	-0.960	10.511	-0.393	-0.393	0.000	0.000	0.000	0.000
23	A	24	PRO	0	-0.058	-0.033	12.491	0.004	0.004	0.000	0.000	0.000	0.000
24	A	25	ILE	0	-0.076	-0.021	7.509	0.018	0.018	0.000	0.000	0.000	0.000
25	A	26	PHE	0	-0.012	-0.019	3.305	-0.671	-0.028	0.032	-0.163	-0.511	0.000
26	A	27	GLY	0	0.041	0.019	8.235	0.120	0.120	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.026	-0.008	8.700	0.031	0.031	0.000	0.000	0.000	0.000
28	A	29	VAL	0	0.034	0.014	8.745	-0.115	-0.115	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.950	-0.970	10.699	0.045	0.045	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.034	-0.018	12.720	-0.054	-0.054	0.000	0.000	0.000	0.000
31	A	32	PHE	0	-0.035	-0.026	13.952	0.048	0.048	0.000	0.000	0.000	0.000
32	A	33	GLN	0	0.042	0.004	17.469	0.004	0.004	0.000	0.000	0.000	0.000
33	A	34	HIS	0	0.009	0.004	20.234	0.010	0.010	0.000	0.000	0.000	0.000
34	A	35	PRO	0	0.055	0.023	18.027	0.011	0.011	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.850	0.896	18.426	0.083	0.083	0.000	0.000	0.000	0.000
36	A	37	ALA	0	0.010	0.013	19.763	0.016	0.016	0.000	0.000	0.000	0.000
37	A	38	PHE	0	0.021	0.019	10.700	0.021	0.021	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.022	-0.012	15.230	0.018	0.018	0.000	0.000	0.000	0.000
39	A	40	THR	0	-0.100	-0.043	17.107	0.027	0.027	0.000	0.000	0.000	0.000
40	A	41	LEU	0	-0.029	0.000	13.399	0.033	0.033	0.000	0.000	0.000	0.000
41	A	42	SER	0	-0.030	-0.013	13.260	-0.009	-0.009	0.000	0.000	0.000	0.000
42	A	43	LEU	0	-0.023	0.001	8.218	0.047	0.047	0.000	0.000	0.000	0.000
43	A	44	ASN	0	0.028	-0.012	6.184	0.454	0.454	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.969	0.969	4.710	-1.117	-0.928	-0.001	-0.034	-0.154	0.000
45	A	46	GLN	0	-0.075	-0.039	1.975	-1.707	-1.805	6.400	-2.928	-3.373	-0.011
46	A	47	ASP	-1	-0.705	-0.824	2.564	-0.434	-0.925	1.954	0.599	-2.061	-0.024
47	A	48	ILE	0	0.020	0.017	2.380	-2.974	-1.127	2.314	-1.038	-3.123	-0.006
48	A	49	ILE	0	-0.008	-0.014	4.261	0.309	0.372	0.000	-0.025	-0.039	0.000
49	A	50	ILE	0	-0.019	-0.010	7.866	-0.049	-0.049	0.000	0.000	0.000	0.000
50	A	51	LEU	0	-0.006	-0.001	10.528	0.071	0.071	0.000	0.000	0.000	0.000
51	A	52	ASP	-1	-0.783	-0.891	13.506	-0.243	-0.243	0.000	0.000	0.000	0.000
52	A	53	LEU	0	-0.043	-0.036	17.027	0.022	0.022	0.000	0.000	0.000	0.000
53	A	54	MET	0	-0.031	-0.011	18.133	0.025	0.025	0.000	0.000	0.000	0.000
54	A	55	MET	0	-0.073	0.000	21.959	0.017	0.017	0.000	0.000	0.000	0.000
55	A	56	PRO	0	-0.010	-0.026	24.814	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	57	ASP	-1	-0.860	-0.941	25.722	-0.092	-0.092	0.000	0.000	0.000	0.000
57	A	58	MET	0	-0.068	-0.039	23.370	0.008	0.008	0.000	0.000	0.000	0.000
58	A	59	ASP	-1	-0.747	-0.862	21.403	-0.087	-0.087	0.000	0.000	0.000	0.000
59	A	60	GLY	0	0.023	0.008	18.193	-0.001	-0.001	0.000	0.000	0.000	0.000
60	A	61	ILE	0	-0.032	-0.017	18.018	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.791	-0.860	19.719	-0.037	-0.037	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.022	-0.003	14.389	0.013	0.013	0.000	0.000	0.000	0.000
63	A	64	ILE	0	0.010	-0.002	14.882	0.006	0.006	0.000	0.000	0.000	0.000
64	A	65	ARG	1	0.770	0.863	16.172	0.040	0.040	0.000	0.000	0.000	0.000
65	A	66	HIS	0	0.038	0.016	15.473	0.008	0.008	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.018	-0.022	11.079	0.030	0.030	0.000	0.000	0.000	0.000
67	A	68	ALA	0	0.024	0.018	14.123	0.028	0.028	0.000	0.000	0.000	0.000
68	A	69	GLU	-1	-0.945	-0.965	15.930	0.048	0.048	0.000	0.000	0.000	0.000
69	A	70	HIS	0	-0.092	-0.051	15.571	0.033	0.033	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.886	0.943	14.118	-0.032	-0.032	0.000	0.000	0.000	0.000
71	A	72	SER	0	0.019	0.017	9.571	0.088	0.088	0.000	0.000	0.000	0.000
72	A	73	PRO	0	-0.028	-0.018	7.235	-0.032	-0.032	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.021	0.005	4.984	0.013	0.013	0.000	0.000	0.000	0.000
74	A	75	SER	0	0.002	0.000	2.430	-1.550	-0.236	0.538	-0.653	-1.199	-0.003
75	A	76	LEU	0	-0.039	-0.014	4.865	-0.073	-0.039	-0.001	-0.007	-0.027	0.000
76	A	77	ILE	0	0.002	0.004	6.309	-0.008	-0.008	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.005	0.017	9.461	0.054	0.054	0.000	0.000	0.000	0.000
78	A	79	ILE	0	0.014	0.005	13.224	-0.014	-0.014	0.000	0.000	0.000	0.000
79	A	80	SER	0	0.051	0.004	15.706	0.033	0.033	0.000	0.000	0.000	0.000
80	A	81	GLY	0	0.004	0.006	19.508	-0.009	-0.009	0.000	0.000	0.000	0.000
81	A	82	TYR	0	-0.039	0.001	22.703	0.014	0.014	0.000	0.000	0.000	0.000
82	A	83	ASP	-1	-0.779	-0.897	23.587	-0.136	-0.136	0.000	0.000	0.000	0.000
83	A	84	SER	0	0.008	-0.001	22.017	-0.004	-0.004	0.000	0.000	0.000	0.000
84	A	85	GLY	0	0.027	0.017	22.082	-0.011	-0.011	0.000	0.000	0.000	0.000
85	A	86	VAL	0	-0.023	-0.007	22.618	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	87	LEU	0	-0.048	-0.021	16.351	0.000	0.000	0.000	0.000	0.000	0.000
87	A	88	HIS	0	0.003	0.002	18.381	0.001	0.001	0.000	0.000	0.000	0.000
88	A	89	SER	0	0.000	-0.018	19.559	0.005	0.005	0.000	0.000	0.000	0.000
89	A	90	ALA	0	-0.014	0.000	18.342	0.007	0.007	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.896	-0.960	13.894	-0.353	-0.353	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.024	-0.006	16.000	0.003	0.003	0.000	0.000	0.000	0.000
92	A	93	LEU	0	-0.042	-0.038	18.435	0.015	0.015	0.000	0.000	0.000	0.000
93	A	94	ALA	0	0.012	0.001	14.097	0.018	0.018	0.000	0.000	0.000	0.000
94	A	95	LEU	0	-0.003	0.003	11.899	0.016	0.016	0.000	0.000	0.000	0.000
95	A	96	SER	0	-0.085	-0.018	14.818	0.031	0.031	0.000	0.000	0.000	0.000
96	A	97	CYS	0	-0.066	-0.037	16.877	0.027	0.027	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.022	-0.013	14.379	0.025	0.025	0.000	0.000	0.000	0.000
98	A	99	LEU	0	-0.030	-0.005	11.084	0.015	0.015	0.000	0.000	0.000	0.000
99	A	100	ASN	0	0.001	-0.008	4.931	0.090	0.090	0.000	0.000	0.000	0.000
100	A	101	VAL	0	0.004	0.007	7.562	-0.174	-0.174	0.000	0.000	0.000	0.000
101	A	102	ILE	0	-0.035	-0.015	3.680	-0.239	-0.003	0.007	-0.038	-0.205	0.000
102	A	103	ASN	0	0.016	-0.002	7.903	0.091	0.091	0.000	0.000	0.000	0.000
103	A	104	THR	0	-0.020	0.002	10.426	0.021	0.021	0.000	0.000	0.000	0.000
104	A	105	PHE	0	-0.002	-0.011	10.363	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	106	THR	0	0.038	0.015	15.470	0.014	0.014	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.766	0.883	18.788	0.231	0.231	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.019	-0.010	20.751	0.015	0.015	0.000	0.000	0.000	0.000
108	A	109	ILE	0	0.016	0.010	15.603	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	110	ASN	0	0.029	0.022	17.543	0.000	0.000	0.000	0.000	0.000	0.000
110	A	111	THR	0	0.057	0.019	16.408	-0.043	-0.043	0.000	0.000	0.000	0.000
111	A	112	GLU	-1	-0.861	-0.914	15.912	-0.361	-0.361	0.000	0.000	0.000	0.000
112	A	113	VAL	0	0.006	0.006	13.884	-0.045	-0.045	0.000	0.000	0.000	0.000
113	A	114	LEU	0	0.018	0.013	10.429	-0.070	-0.070	0.000	0.000	0.000	0.000
114	A	115	THR	0	-0.022	-0.023	11.022	-0.125	-0.125	0.000	0.000	0.000	0.000
115	A	116	CYS	0	-0.065	-0.042	11.515	-0.084	-0.084	0.000	0.000	0.000	0.000
116	A	117	PHE	0	0.031	0.018	6.588	-0.084	-0.084	0.000	0.000	0.000	0.000
117	A	118	LEU	0	0.054	0.026	6.612	-0.221	-0.221	0.000	0.000	0.000	0.000
118	A	119	THR	0	-0.015	-0.019	6.713	-0.336	-0.336	0.000	0.000	0.000	0.000
119	A	120	SER	0	-0.113	-0.054	7.515	-0.107	-0.107	0.000	0.000	0.000	0.000
120	A	121	LEU	0	0.019	0.024	2.572	-1.167	-0.144	0.763	-0.286	-1.500	0.001
121	A	122	SER	0	-0.068	-0.028	3.117	-3.324	-1.858	0.121	-0.796	-0.790	-0.007
122	A	123	ASN	0	0.014	-0.011	5.181	-0.176	0.024	-0.001	-0.004	-0.194	0.000
123	A	124	ARG	1	0.842	0.931	6.495	1.225	1.225	0.000	0.000	0.000	0.000
124	A	125	GLN	0	-0.003	0.004	10.063	-0.045	-0.045	0.000	0.000	0.000	0.000

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