FMO DATABASE

FMODB ID: JL949

Calculation Name: 2EGO-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EGO

Chain ID: A

ChEMBL ID:

UniProt ID: Q8R4T5

Base Structure: X-ray

Registration Date: 2023-09-19

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	88
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-577195.960686
FMO2-HF: Nuclear repulsion	543867.202364
FMO2-HF: Total energy	-33328.758322
FMO2-MP2: Total energy	-33427.491416

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:95:SER)

Summations of interaction energy for fragment #1(A:95:SER)

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.
1.64	3.296	0.063	-0.642	-1.077	0.001

Interaction energy analysis for fragmet #1(A:95:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.016 / q_NPA : -0.008

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	97	GLN	0	0.031	0.009	2.816	0.799	2.455	0.063	-0.642	-1.077	0.001
4	A	98	ARG	1	0.845	0.917	6.181	0.951	0.951	0.000	0.000	0.000	0.000
5	A	99	LYS	1	0.851	0.930	8.787	0.125	0.125	0.000	0.000	0.000	0.000
6	A	100	VAL	0	-0.004	-0.010	11.096	-0.081	-0.081	0.000	0.000	0.000	0.000
7	A	101	LEU	0	-0.001	0.008	14.543	0.058	0.058	0.000	0.000	0.000	0.000
8	A	102	THR	0	0.009	-0.007	17.483	-0.035	-0.035	0.000	0.000	0.000	0.000
9	A	103	LEU	0	-0.009	0.027	20.478	0.017	0.017	0.000	0.000	0.000	0.000
10	A	104	GLU	-1	-0.926	-0.969	23.817	0.068	0.068	0.000	0.000	0.000	0.000
11	A	105	LYS	1	0.767	0.898	27.368	-0.018	-0.018	0.000	0.000	0.000	0.000
12	A	106	GLY	0	0.056	0.030	30.608	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	107	ASP	-1	-0.859	-0.921	34.163	0.024	0.024	0.000	0.000	0.000	0.000
14	A	108	ASN	0	-0.052	-0.027	36.296	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	109	GLN	0	0.006	0.006	31.251	0.004	0.004	0.000	0.000	0.000	0.000
16	A	110	THR	0	0.026	0.009	30.757	-0.002	-0.002	0.000	0.000	0.000	0.000
17	A	111	PHE	0	0.057	0.010	26.021	0.005	0.005	0.000	0.000	0.000	0.000
18	A	112	GLY	0	0.015	0.011	26.532	0.009	0.009	0.000	0.000	0.000	0.000
19	A	113	PHE	0	0.004	-0.018	23.176	0.009	0.009	0.000	0.000	0.000	0.000
20	A	114	GLU	-1	-0.889	-0.932	25.069	0.000	0.000	0.000	0.000	0.000	0.000
21	A	115	ILE	0	-0.023	-0.017	22.907	-0.001	-0.001	0.000	0.000	0.000	0.000
22	A	116	GLN	0	-0.010	0.000	23.546	0.015	0.015	0.000	0.000	0.000	0.000
23	A	117	THR	0	0.004	-0.013	23.120	-0.007	-0.007	0.000	0.000	0.000	0.000
24	A	118	TYR	0	-0.033	-0.026	22.139	0.021	0.021	0.000	0.000	0.000	0.000
25	A	119	GLY	0	0.070	0.035	22.922	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	120	LEU	0	-0.050	-0.026	17.811	0.008	0.008	0.000	0.000	0.000	0.000
27	A	128	DVA	0	0.013	0.003	19.392	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	129	GLU	-1	-0.801	-0.903	20.648	-0.126	-0.126	0.000	0.000	0.000	0.000
29	A	130	MET	0	-0.084	-0.021	22.510	-0.002	-0.002	0.000	0.000	0.000	0.000
30	A	131	VAL	0	0.044	0.036	17.199	-0.019	-0.019	0.000	0.000	0.000	0.000
31	A	132	THR	0	0.034	0.018	20.008	0.034	0.034	0.000	0.000	0.000	0.000
32	A	133	PHE	0	-0.007	0.007	18.304	-0.024	-0.024	0.000	0.000	0.000	0.000
33	A	134	VAL	0	0.030	0.015	18.297	0.016	0.016	0.000	0.000	0.000	0.000
34	A	135	ALA	0	-0.003	0.006	20.539	0.011	0.011	0.000	0.000	0.000	0.000
35	A	136	ARG	1	0.926	0.951	23.372	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	137	VAL	0	0.024	0.016	20.750	-0.009	-0.009	0.000	0.000	0.000	0.000
37	A	138	HIS	0	-0.071	-0.028	24.043	0.008	0.008	0.000	0.000	0.000	0.000
38	A	139	GLU	-1	-0.811	-0.891	26.166	0.122	0.122	0.000	0.000	0.000	0.000
39	A	140	SER	0	-0.033	-0.018	27.067	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	141	SER	0	-0.045	-0.007	25.394	-0.003	-0.003	0.000	0.000	0.000	0.000
41	A	142	PRO	0	-0.003	-0.016	25.356	0.010	0.010	0.000	0.000	0.000	0.000
42	A	143	ALA	0	0.005	0.004	22.434	0.009	0.009	0.000	0.000	0.000	0.000
43	A	144	GLN	0	0.000	-0.015	20.923	0.001	0.001	0.000	0.000	0.000	0.000
44	A	145	LEU	0	-0.037	-0.010	20.774	0.023	0.023	0.000	0.000	0.000	0.000
45	A	146	ALA	0	-0.021	-0.006	20.170	0.020	0.020	0.000	0.000	0.000	0.000
46	A	147	GLY	0	0.010	0.010	16.708	0.015	0.015	0.000	0.000	0.000	0.000
47	A	148	LEU	0	-0.034	-0.020	16.031	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	149	THR	0	-0.021	-0.017	14.472	0.027	0.027	0.000	0.000	0.000	0.000
49	A	150	PRO	0	-0.008	-0.016	16.971	-0.034	-0.034	0.000	0.000	0.000	0.000
50	A	151	GLY	0	0.012	0.009	17.230	0.017	0.017	0.000	0.000	0.000	0.000
51	A	152	ASP	-1	-0.778	-0.856	13.277	-0.060	-0.060	0.000	0.000	0.000	0.000
52	A	153	THR	0	-0.008	0.002	13.944	0.017	0.017	0.000	0.000	0.000	0.000
53	A	154	ILE	0	-0.020	-0.025	14.996	-0.024	-0.024	0.000	0.000	0.000	0.000
54	A	155	ALA	0	-0.029	-0.015	14.454	-0.023	-0.023	0.000	0.000	0.000	0.000
55	A	156	SER	0	-0.066	-0.078	16.606	0.010	0.010	0.000	0.000	0.000	0.000
56	A	157	VAL	0	0.033	0.013	19.411	0.021	0.021	0.000	0.000	0.000	0.000
57	A	158	ASN	0	-0.033	-0.037	22.362	0.003	0.003	0.000	0.000	0.000	0.000
58	A	159	GLY	0	0.011	0.017	20.699	0.005	0.005	0.000	0.000	0.000	0.000
59	A	160	LEU	0	-0.028	-0.002	21.772	-0.021	-0.021	0.000	0.000	0.000	0.000
60	A	161	ASN	0	-0.009	-0.038	19.937	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	162	VAL	0	0.005	-0.008	20.211	0.017	0.017	0.000	0.000	0.000	0.000
62	A	163	GLU	-1	-0.923	-0.936	20.138	-0.278	-0.278	0.000	0.000	0.000	0.000
63	A	164	GLY	0	0.009	0.008	21.564	0.005	0.005	0.000	0.000	0.000	0.000
64	A	165	ILE	0	-0.051	-0.005	24.832	0.016	0.016	0.000	0.000	0.000	0.000
65	A	166	ARG	1	0.848	0.907	25.969	0.117	0.117	0.000	0.000	0.000	0.000
66	A	167	HIS	0	0.016	-0.006	26.932	0.004	0.004	0.000	0.000	0.000	0.000
67	A	168	ARG	1	0.862	0.900	28.537	0.045	0.045	0.000	0.000	0.000	0.000
68	A	169	GLU	-1	-0.868	-0.926	29.886	-0.082	-0.082	0.000	0.000	0.000	0.000
69	A	170	ILE	0	0.023	0.008	23.822	0.003	0.003	0.000	0.000	0.000	0.000
70	A	171	VAL	0	-0.010	-0.005	27.575	0.008	0.008	0.000	0.000	0.000	0.000
71	A	172	ASP	-1	-0.842	-0.904	29.622	-0.033	-0.033	0.000	0.000	0.000	0.000
72	A	173	ILE	0	-0.015	-0.004	26.577	0.006	0.006	0.000	0.000	0.000	0.000
73	A	174	ILE	0	-0.011	-0.010	24.731	0.007	0.007	0.000	0.000	0.000	0.000
74	A	175	LYS	1	0.907	0.954	28.207	0.019	0.019	0.000	0.000	0.000	0.000
75	A	176	ALA	0	-0.030	-0.025	31.562	0.006	0.006	0.000	0.000	0.000	0.000
76	A	177	SER	0	-0.006	-0.008	27.840	-0.001	-0.001	0.000	0.000	0.000	0.000
77	A	178	GLY	0	-0.014	0.006	30.140	0.006	0.006	0.000	0.000	0.000	0.000
78	A	179	ASN	0	-0.030	-0.043	31.415	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	180	VAL	0	0.031	0.014	26.540	0.009	0.009	0.000	0.000	0.000	0.000
80	A	181	LEU	0	0.002	0.036	23.718	-0.011	-0.011	0.000	0.000	0.000	0.000
81	A	182	ARG	1	0.868	0.937	19.046	-0.028	-0.028	0.000	0.000	0.000	0.000
82	A	183	LEU	0	0.014	0.007	18.895	-0.021	-0.021	0.000	0.000	0.000	0.000
83	A	184	GLU	-1	-0.782	-0.854	14.829	-0.164	-0.164	0.000	0.000	0.000	0.000
84	A	185	THR	0	-0.051	-0.041	13.583	-0.012	-0.012	0.000	0.000	0.000	0.000
85	A	186	LEU	0	0.004	0.000	9.566	-0.077	-0.077	0.000	0.000	0.000	0.000
86	A	187	TYR	0	-0.022	-0.012	6.523	0.155	0.155	0.000	0.000	0.000	0.000
87	A	188	GLY	0	0.040	0.029	10.369	-0.078	-0.078	0.000	0.000	0.000	0.000
88	A	189	THR	0	-0.068	-0.022	10.156	0.067	0.067	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:95:SER)