FMO DATABASE

FMODB ID: ZYL3N

Calculation Name: 2O49-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2O49

Chain ID: A

ChEMBL ID:

UniProt ID: Q01826

Base Structure: X-ray

Registration Date: 2023-03-13

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	84
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-608841.68286
FMO2-HF: Nuclear repulsion	574549.120545
FMO2-HF: Total energy	-34292.562315
FMO2-MP2: Total energy	-34394.351513

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:370:GLU)

Summations of interaction energy for fragment #1(A:370:GLU)

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.
-93.989	-87.115	1.662	-3.82	-4.716	0.033

Interaction energy analysis for fragmet #1(A:370:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.930 / q_NPA : -0.972

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	372	SER	0	0.010	0.011	3.813	-3.043	-1.485	-0.022	-0.744	-0.793	0.001
4	A	373	SER	0	-0.017	-0.032	6.019	0.065	0.065	0.000	0.000	0.000	0.000
5	A	374	GLU	-1	-0.931	-0.957	8.490	17.134	17.134	0.000	0.000	0.000	0.000
6	A	375	ILE	0	-0.011	0.009	8.834	-1.196	-1.196	0.000	0.000	0.000	0.000
7	A	376	TYR	0	-0.013	-0.052	10.858	-0.928	-0.928	0.000	0.000	0.000	0.000
8	A	377	GLN	0	-0.030	-0.013	14.047	-0.991	-0.991	0.000	0.000	0.000	0.000
9	A	378	TRP	0	0.055	0.016	8.732	0.351	0.351	0.000	0.000	0.000	0.000
10	A	379	VAL	0	-0.013	-0.004	13.303	-0.675	-0.675	0.000	0.000	0.000	0.000
11	A	380	ARG	1	0.888	0.939	15.853	-15.520	-15.520	0.000	0.000	0.000	0.000
12	A	381	ASP	-1	-0.854	-0.920	18.473	13.862	13.862	0.000	0.000	0.000	0.000
13	A	382	GLU	-1	-0.700	-0.785	17.059	14.912	14.912	0.000	0.000	0.000	0.000
14	A	383	LEU	0	-0.061	-0.049	19.125	-0.669	-0.669	0.000	0.000	0.000	0.000
15	A	384	LYS	1	0.948	0.978	21.372	-11.739	-11.739	0.000	0.000	0.000	0.000
16	A	385	ARG	1	0.715	0.834	20.246	-14.183	-14.183	0.000	0.000	0.000	0.000
17	A	386	ALA	0	-0.001	-0.003	22.141	-0.442	-0.442	0.000	0.000	0.000	0.000
18	A	387	GLY	0	0.002	0.021	23.945	-0.409	-0.409	0.000	0.000	0.000	0.000
19	A	388	ILE	0	-0.080	-0.030	20.801	-0.376	-0.376	0.000	0.000	0.000	0.000
20	A	389	SER	0	0.016	0.006	24.266	0.257	0.257	0.000	0.000	0.000	0.000
21	A	390	GLN	0	0.096	0.018	21.445	0.363	0.363	0.000	0.000	0.000	0.000
22	A	391	ALA	0	-0.013	-0.008	21.091	0.626	0.626	0.000	0.000	0.000	0.000
23	A	392	VAL	0	0.047	0.037	21.848	0.427	0.427	0.000	0.000	0.000	0.000
24	A	393	PHE	0	0.067	0.024	14.045	0.543	0.543	0.000	0.000	0.000	0.000
25	A	394	ALA	0	0.001	-0.013	17.304	1.023	1.023	0.000	0.000	0.000	0.000
26	A	395	ARG	1	0.863	0.956	17.446	-13.941	-13.941	0.000	0.000	0.000	0.000
27	A	396	VAL	0	0.008	-0.014	17.606	0.668	0.668	0.000	0.000	0.000	0.000
28	A	397	ALA	0	-0.003	0.029	13.630	0.836	0.836	0.000	0.000	0.000	0.000
29	A	398	PHE	0	-0.007	-0.024	12.261	1.617	1.617	0.000	0.000	0.000	0.000
30	A	399	ASN	0	0.010	0.022	13.898	-0.703	-0.703	0.000	0.000	0.000	0.000
31	A	400	ARG	1	0.847	0.934	14.138	-21.528	-21.528	0.000	0.000	0.000	0.000
32	A	401	THR	0	0.020	-0.004	18.689	-0.375	-0.375	0.000	0.000	0.000	0.000
33	A	402	GLN	0	0.054	0.004	20.739	0.273	0.273	0.000	0.000	0.000	0.000
34	A	403	GLY	0	0.029	0.021	21.976	0.262	0.262	0.000	0.000	0.000	0.000
35	A	404	LEU	0	0.009	0.008	16.644	0.086	0.086	0.000	0.000	0.000	0.000
36	A	405	LEU	0	0.039	0.023	16.222	0.566	0.566	0.000	0.000	0.000	0.000
37	A	406	SER	0	-0.015	0.000	18.508	0.009	0.009	0.000	0.000	0.000	0.000
38	A	407	GLU	-1	-0.822	-0.901	20.089	13.383	13.383	0.000	0.000	0.000	0.000
39	A	408	ILE	0	-0.065	-0.024	13.778	0.218	0.218	0.000	0.000	0.000	0.000
40	A	409	LEU	0	-0.012	-0.017	16.266	0.353	0.353	0.000	0.000	0.000	0.000
41	A	410	ARG	1	0.780	0.881	18.005	-13.421	-13.421	0.000	0.000	0.000	0.000
42	A	411	LYS	1	0.898	0.938	17.381	-16.032	-16.032	0.000	0.000	0.000	0.000
43	A	412	GLU	-1	-0.911	-0.931	15.329	15.628	15.628	0.000	0.000	0.000	0.000
44	A	413	GLU	-1	-0.928	-0.961	13.018	18.358	18.358	0.000	0.000	0.000	0.000
45	A	414	ASP	-1	-0.764	-0.875	9.727	25.412	25.412	0.000	0.000	0.000	0.000
46	A	415	PRO	0	0.002	-0.013	6.489	0.824	0.824	0.000	0.000	0.000	0.000
47	A	416	LYS	1	0.863	0.935	5.910	-25.006	-25.006	0.000	0.000	0.000	0.000
48	A	417	THR	0	-0.052	-0.019	8.170	-0.720	-0.720	0.000	0.000	0.000	0.000
49	A	418	ALA	0	0.000	0.021	8.472	-1.451	-1.451	0.000	0.000	0.000	0.000
50	A	419	SER	0	0.040	0.016	9.699	2.073	2.073	0.000	0.000	0.000	0.000
51	A	420	GLN	0	0.073	0.013	8.731	5.324	5.324	0.000	0.000	0.000	0.000
52	A	421	SER	0	-0.027	-0.015	9.334	2.511	2.511	0.000	0.000	0.000	0.000
53	A	422	LEU	0	0.012	0.016	10.049	0.440	0.440	0.000	0.000	0.000	0.000
54	A	423	LEU	0	0.062	0.029	4.523	1.088	1.188	-0.001	-0.007	-0.091	0.000
55	A	424	VAL	0	-0.026	0.000	6.496	3.060	3.060	0.000	0.000	0.000	0.000
56	A	425	ASN	0	-0.007	-0.012	8.232	-0.237	-0.237	0.000	0.000	0.000	0.000
57	A	426	LEU	0	0.023	0.006	7.098	-0.624	-0.624	0.000	0.000	0.000	0.000
58	A	427	ARG	1	0.966	0.982	2.337	-90.132	-85.267	1.685	-2.871	-3.679	0.031
59	A	428	ALA	0	-0.043	0.000	5.744	-1.199	-1.199	0.000	0.000	0.000	0.000
60	A	429	MET	0	-0.012	-0.006	8.846	-2.403	-2.403	0.000	0.000	0.000	0.000
61	A	430	GLN	0	0.043	0.012	4.110	-4.426	-4.075	0.000	-0.198	-0.153	0.001
62	A	431	ASN	0	-0.004	-0.012	6.018	-0.367	-0.367	0.000	0.000	0.000	0.000
63	A	432	PHE	0	0.003	0.002	8.421	-2.027	-2.027	0.000	0.000	0.000	0.000
64	A	433	LEU	0	0.004	-0.017	11.242	-1.657	-1.657	0.000	0.000	0.000	0.000
65	A	434	GLN	0	-0.061	-0.017	7.461	0.669	0.669	0.000	0.000	0.000	0.000
66	A	435	LEU	0	-0.028	0.009	12.055	-0.835	-0.835	0.000	0.000	0.000	0.000
67	A	436	PRO	0	0.036	0.009	15.005	-0.518	-0.518	0.000	0.000	0.000	0.000
68	A	437	GLU	-1	-0.893	-0.949	18.435	13.079	13.079	0.000	0.000	0.000	0.000
69	A	438	ALA	0	0.021	0.007	20.281	-0.191	-0.191	0.000	0.000	0.000	0.000
70	A	439	GLU	-1	-0.968	-0.988	19.191	15.332	15.332	0.000	0.000	0.000	0.000
71	A	440	ARG	1	0.827	0.908	15.610	-16.772	-16.772	0.000	0.000	0.000	0.000
72	A	441	ASP	-1	-0.755	-0.868	19.469	12.717	12.717	0.000	0.000	0.000	0.000
73	A	442	ARG	1	0.916	0.964	22.674	-13.198	-13.198	0.000	0.000	0.000	0.000
74	A	443	ILE	0	0.003	0.002	18.476	-0.239	-0.239	0.000	0.000	0.000	0.000
75	A	444	TYR	0	-0.076	-0.086	18.198	0.128	0.128	0.000	0.000	0.000	0.000
76	A	445	GLN	0	-0.017	-0.009	23.266	-0.595	-0.595	0.000	0.000	0.000	0.000
77	A	446	ASP	-1	-0.837	-0.909	25.577	11.217	11.217	0.000	0.000	0.000	0.000
78	A	447	GLU	-1	-0.958	-0.992	22.805	12.735	12.735	0.000	0.000	0.000	0.000
79	A	448	ARG	1	0.909	0.954	25.541	-11.095	-11.095	0.000	0.000	0.000	0.000
80	A	449	GLU	-1	-0.925	-0.961	27.857	9.625	9.625	0.000	0.000	0.000	0.000
81	A	450	ARG	1	0.882	0.936	24.959	-12.419	-12.419	0.000	0.000	0.000	0.000
82	A	451	SER	0	-0.057	-0.031	27.277	-0.089	-0.089	0.000	0.000	0.000	0.000
83	A	452	LEU	0	-0.062	0.000	29.255	-0.200	-0.200	0.000	0.000	0.000	0.000
84	A	453	ARG	1	0.918	0.971	32.406	-9.472	-9.472	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:370:GLU)