FMO DATABASE

FMODB ID: Q1MMY

Calculation Name: 2BA2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2BA2

Chain ID: A

ChEMBL ID:

UniProt ID: P75103

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	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	81
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-364324.870896
FMO2-HF: Nuclear repulsion	331919.742738
FMO2-HF: Total energy	-32405.128157
FMO2-MP2: Total energy	-32500.913995

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:5:GLY)

Summations of interaction energy for fragment #1(A:5:GLY)

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.
-7.994	-4.654	5.217	-3.962	-4.595	-0.012

Interaction energy analysis for fragmet #1(A:5:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.032 / q_NPA : -0.003

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	7	ARG	1	0.950	0.979	3.058	-8.234	-5.667	1.558	-1.470	-2.656	0.003
4	A	8	TYR	0	-0.033	-0.015	2.369	-0.182	0.627	3.660	-2.486	-1.983	-0.015
5	A	9	VAL	0	0.034	0.031	4.847	-0.229	-0.265	-0.001	-0.006	0.044	0.000
6	A	10	THR	0	0.001	-0.015	7.340	0.090	0.090	0.000	0.000	0.000	0.000
7	A	11	HIS	0	0.082	0.017	9.200	0.116	0.116	0.000	0.000	0.000	0.000
8	A	12	LYS	1	0.931	0.975	12.480	0.389	0.389	0.000	0.000	0.000	0.000
9	A	13	GLN	0	0.048	0.035	9.435	-0.064	-0.064	0.000	0.000	0.000	0.000
10	A	14	LEU	0	0.064	0.034	13.082	0.067	0.067	0.000	0.000	0.000	0.000
11	A	15	ASP	-1	-0.843	-0.924	14.542	-0.251	-0.251	0.000	0.000	0.000	0.000
12	A	16	GLU	-1	-0.930	-0.965	16.727	-0.263	-0.263	0.000	0.000	0.000	0.000
13	A	17	LYS	1	0.783	0.869	14.436	0.353	0.353	0.000	0.000	0.000	0.000
14	A	18	LEU	0	0.039	0.014	18.051	0.029	0.029	0.000	0.000	0.000	0.000
15	A	19	LYS	1	0.919	0.982	20.326	0.190	0.190	0.000	0.000	0.000	0.000
16	A	20	ASN	0	-0.084	-0.035	20.446	0.021	0.021	0.000	0.000	0.000	0.000
17	A	21	PHE	0	-0.010	0.006	20.371	0.014	0.014	0.000	0.000	0.000	0.000
18	A	22	VAL	0	0.019	0.015	24.670	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	23	THR	0	-0.041	-0.045	26.261	0.004	0.004	0.000	0.000	0.000	0.000
20	A	24	LYS	1	0.963	0.951	27.567	0.045	0.045	0.000	0.000	0.000	0.000
21	A	25	THR	0	0.038	0.011	30.617	0.006	0.006	0.000	0.000	0.000	0.000
22	A	26	GLU	-1	-0.725	-0.813	29.369	-0.071	-0.071	0.000	0.000	0.000	0.000
23	A	27	PHE	0	0.003	-0.006	32.050	0.005	0.005	0.000	0.000	0.000	0.000
24	A	28	LYS	1	0.781	0.884	33.609	0.038	0.038	0.000	0.000	0.000	0.000
25	A	29	GLU	-1	-0.871	-0.917	36.216	-0.046	-0.046	0.000	0.000	0.000	0.000
26	A	30	PHE	0	0.025	0.006	36.658	0.003	0.003	0.000	0.000	0.000	0.000
27	A	31	GLN	0	-0.008	-0.011	36.593	0.001	0.001	0.000	0.000	0.000	0.000
28	A	32	THR	0	-0.005	0.006	39.748	0.002	0.002	0.000	0.000	0.000	0.000
29	A	33	VAL	0	0.081	0.046	41.860	0.002	0.002	0.000	0.000	0.000	0.000
30	A	34	VAL	0	-0.015	0.013	41.245	0.002	0.002	0.000	0.000	0.000	0.000
31	A	35	MET	0	-0.037	-0.030	43.193	0.002	0.002	0.000	0.000	0.000	0.000
32	A	36	GLU	-1	-0.922	-0.965	45.731	-0.024	-0.024	0.000	0.000	0.000	0.000
33	A	37	SER	0	-0.026	-0.034	46.596	0.001	0.001	0.000	0.000	0.000	0.000
34	A	38	PHE	0	-0.052	-0.032	45.135	0.001	0.001	0.000	0.000	0.000	0.000
35	A	39	ALA	0	-0.016	0.008	49.858	0.001	0.001	0.000	0.000	0.000	0.000
36	A	40	VAL	0	0.009	0.005	51.785	0.001	0.001	0.000	0.000	0.000	0.000
37	A	41	GLN	0	0.011	0.002	51.749	0.001	0.001	0.000	0.000	0.000	0.000
38	A	42	ASN	0	-0.020	-0.008	52.664	0.001	0.001	0.000	0.000	0.000	0.000
39	A	43	GLN	0	0.026	0.023	55.871	0.001	0.001	0.000	0.000	0.000	0.000
40	A	44	ASN	0	-0.038	-0.028	55.862	0.001	0.001	0.000	0.000	0.000	0.000
41	A	45	ILE	0	-0.026	-0.025	55.320	0.001	0.001	0.000	0.000	0.000	0.000
42	A	46	ASP	-1	-0.926	-0.959	59.472	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	47	ALA	0	0.032	0.025	61.675	0.000	0.000	0.000	0.000	0.000	0.000
44	A	48	GLN	0	-0.021	-0.016	61.451	0.001	0.001	0.000	0.000	0.000	0.000
45	A	49	GLY	0	-0.002	0.006	63.693	0.001	0.001	0.000	0.000	0.000	0.000
46	A	50	GLU	-1	-0.948	-0.975	65.238	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	51	GLN	0	0.036	0.012	66.780	0.000	0.000	0.000	0.000	0.000	0.000
48	A	52	ILE	0	-0.034	-0.019	65.726	0.000	0.000	0.000	0.000	0.000	0.000
49	A	53	LYS	1	0.845	0.925	69.565	0.005	0.005	0.000	0.000	0.000	0.000
50	A	54	GLU	-1	-0.881	-0.955	71.437	-0.007	-0.007	0.000	0.000	0.000	0.000
51	A	55	LEU	0	0.007	0.006	71.069	0.000	0.000	0.000	0.000	0.000	0.000
52	A	56	GLN	0	-0.015	0.001	70.442	0.000	0.000	0.000	0.000	0.000	0.000
53	A	57	VAL	0	-0.062	-0.031	75.210	0.000	0.000	0.000	0.000	0.000	0.000
54	A	58	GLU	-1	-0.812	-0.899	77.555	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	59	GLN	0	-0.018	0.004	76.214	0.000	0.000	0.000	0.000	0.000	0.000
56	A	60	LYS	1	0.941	0.971	79.391	0.003	0.003	0.000	0.000	0.000	0.000
57	A	61	ALA	0	-0.032	-0.014	81.131	0.000	0.000	0.000	0.000	0.000	0.000
58	A	62	GLN	0	0.001	-0.020	81.632	0.000	0.000	0.000	0.000	0.000	0.000
59	A	63	GLY	0	0.022	0.019	83.532	0.000	0.000	0.000	0.000	0.000	0.000
60	A	64	LYS	1	0.950	0.965	84.924	0.003	0.003	0.000	0.000	0.000	0.000
61	A	65	THR	0	-0.021	-0.010	87.326	0.000	0.000	0.000	0.000	0.000	0.000
62	A	66	LEU	0	0.012	0.003	85.695	0.000	0.000	0.000	0.000	0.000	0.000
63	A	67	GLN	0	-0.005	-0.003	87.493	0.000	0.000	0.000	0.000	0.000	0.000
64	A	68	LEU	0	0.001	0.007	90.892	0.000	0.000	0.000	0.000	0.000	0.000
65	A	69	ILE	0	0.003	0.007	91.361	0.000	0.000	0.000	0.000	0.000	0.000
66	A	70	LEU	0	-0.016	-0.015	91.059	0.000	0.000	0.000	0.000	0.000	0.000
67	A	71	GLU	-1	-0.943	-0.965	94.718	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	72	ALA	0	-0.048	-0.026	97.008	0.000	0.000	0.000	0.000	0.000	0.000
69	A	73	LEU	0	-0.001	-0.017	95.807	0.000	0.000	0.000	0.000	0.000	0.000
70	A	74	GLN	0	0.046	0.046	99.282	0.000	0.000	0.000	0.000	0.000	0.000
71	A	75	GLY	0	0.023	0.009	100.979	0.000	0.000	0.000	0.000	0.000	0.000
72	A	76	ILE	0	-0.052	-0.035	101.196	0.000	0.000	0.000	0.000	0.000	0.000
73	A	77	ASN	0	0.030	0.001	101.504	0.000	0.000	0.000	0.000	0.000	0.000
74	A	78	LYS	1	0.940	0.987	103.191	0.001	0.001	0.000	0.000	0.000	0.000
75	A	79	ARG	1	0.882	0.938	106.429	0.002	0.002	0.000	0.000	0.000	0.000
76	A	80	LEU	0	-0.001	0.000	105.967	0.000	0.000	0.000	0.000	0.000	0.000
77	A	81	ASP	-1	-0.848	-0.922	107.656	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	82	ASN	0	-0.100	-0.056	110.618	0.000	0.000	0.000	0.000	0.000	0.000
79	A	83	LEU	0	-0.056	-0.027	111.720	0.000	0.000	0.000	0.000	0.000	0.000
80	A	84	GLU	-1	-0.991	-0.977	110.977	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	85	SER	0	-0.078	-0.028	114.322	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:GLY)