FMO DATABASE

FMODB ID: 1JGJZ

Calculation Name: 2B8I-A-Xray308

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2B8I

Chain ID: A

ChEMBL ID:

UniProt ID: Q56GA4

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

Apendix: None

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. 1.20200116
Remarks	Structural optimization was performed under the unconstrained condition of hydrogen and heavy atoms fixed using MOE with Auto-FMO protocol as OptH.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	77
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-485138.981131
FMO2-HF: Nuclear repulsion	455478.022761
FMO2-HF: Total energy	-29660.95837
FMO2-MP2: Total energy	-29749.013884

3D Structure Molmil

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:1:ILE )

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

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.
-10.696	-11.755	18.964	-5.471	-12.435	-0.019

Interaction energy analysis for fragmet #1(A:1:ILE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.046 / q_NPA : 0.015

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	3	PRO	0	0.057	0.014	3.057	-3.305	-0.306	0.182	-1.500	-1.681	0.004
4	A	4	TYR	0	-0.006	-0.010	5.094	-0.219	-0.076	0.000	-0.006	-0.138	0.000
5	A	5	MET	0	0.058	0.041	2.542	0.043	-2.966	8.025	-1.263	-3.753	-0.008
6	A	6	LYS	1	1.009	1.016	4.338	0.828	1.063	0.000	-0.020	-0.215	0.000
7	A	7	ALA	0	-0.029	-0.016	5.035	0.081	0.120	0.000	-0.003	-0.036	0.000
8	A	8	LEU	0	0.001	0.016	7.646	0.020	0.020	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.048	0.030	4.110	-0.123	-0.015	0.000	-0.012	-0.096	0.000
10	A	10	TYR	0	-0.001	-0.008	8.074	0.044	0.044	0.000	0.000	0.000	0.000
11	A	11	GLU	-1	-0.918	-0.963	10.237	-0.052	-0.052	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.018	-0.001	11.192	0.054	0.054	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.054	-0.031	10.585	0.014	0.014	0.000	0.000	0.000	0.000
14	A	14	VAL	0	0.014	0.016	13.730	0.021	0.021	0.000	0.000	0.000	0.000
15	A	15	ASN	0	-0.048	-0.027	15.945	0.040	0.040	0.000	0.000	0.000	0.000
16	A	16	LEU	0	-0.051	-0.031	14.521	0.016	0.016	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.003	0.004	17.851	0.005	0.005	0.000	0.000	0.000	0.000
18	A	18	ASN	0	-0.086	-0.044	19.685	0.015	0.015	0.000	0.000	0.000	0.000
19	A	19	GLN	0	-0.060	-0.015	21.007	0.031	0.031	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.880	-0.947	22.956	-0.041	-0.041	0.000	0.000	0.000	0.000
21	A	21	PRO	0	0.017	-0.021	23.845	0.007	0.007	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.935	-0.937	24.468	0.004	0.004	0.000	0.000	0.000	0.000
23	A	23	GLN	0	-0.011	-0.008	22.750	0.012	0.012	0.000	0.000	0.000	0.000
24	A	24	HIS	0	0.006	0.006	20.095	0.009	0.009	0.000	0.000	0.000	0.000
25	A	25	ALA	0	-0.026	-0.018	19.076	0.001	0.001	0.000	0.000	0.000	0.000
26	A	26	THR	0	0.020	-0.002	19.434	0.016	0.016	0.000	0.000	0.000	0.000
27	A	27	ILE	0	-0.016	0.004	15.926	0.035	0.035	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.905	0.952	14.825	0.091	0.091	0.000	0.000	0.000	0.000
29	A	29	GLN	0	-0.056	-0.033	14.499	-0.020	-0.020	0.000	0.000	0.000	0.000
30	A	30	ASN	0	0.022	0.011	15.474	0.109	0.109	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.023	0.020	8.661	0.075	0.075	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.063	-0.054	10.688	0.099	0.099	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.891	-0.936	11.909	0.541	0.541	0.000	0.000	0.000	0.000
34	A	34	GLN	0	-0.061	-0.028	10.607	0.078	0.078	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.093	-0.048	5.839	0.281	0.281	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.934	-0.946	7.839	1.447	1.447	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.038	-0.016	5.857	0.117	0.117	0.000	0.000	0.000	0.000
38	A	38	PRO	0	0.020	0.011	8.695	-0.122	-0.122	0.000	0.000	0.000	0.000
39	A	39	PHE	0	0.072	0.017	11.154	-0.127	-0.127	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.876	-0.938	11.463	-0.269	-0.269	0.000	0.000	0.000	0.000
41	A	41	LYS	1	0.937	0.963	5.931	1.003	1.003	0.000	0.000	0.000	0.000
42	A	42	GLN	0	-0.007	0.005	8.733	-0.099	-0.099	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.009	0.004	10.670	-0.054	-0.054	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.018	0.013	8.795	-0.017	-0.017	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.040	0.017	7.081	-0.065	-0.065	0.000	0.000	0.000	0.000
46	A	46	TYR	0	-0.024	-0.019	9.253	0.039	0.039	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.020	-0.021	13.011	0.007	0.007	0.000	0.000	0.000	0.000
48	A	48	GLY	0	-0.008	0.009	11.798	0.019	0.019	0.000	0.000	0.000	0.000
49	A	49	ALA	0	0.009	-0.006	10.205	-0.019	-0.019	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.005	0.000	10.908	0.073	0.073	0.000	0.000	0.000	0.000
51	A	51	GLY	0	0.013	0.016	13.806	0.048	0.048	0.000	0.000	0.000	0.000
52	A	52	PRO	0	-0.014	-0.014	14.869	0.038	0.038	0.000	0.000	0.000	0.000
53	A	53	ALA	0	0.016	0.014	14.949	0.024	0.024	0.000	0.000	0.000	0.000
54	A	54	SER	0	-0.003	-0.009	16.952	0.043	0.043	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.131	-0.061	19.427	0.017	0.017	0.000	0.000	0.000	0.000
56	A	56	GLY	0	0.095	0.052	20.756	0.008	0.008	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.827	0.916	19.595	0.226	0.226	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.015	-0.005	14.053	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.902	-0.952	18.172	-0.166	-0.166	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.018	-0.010	18.965	0.002	0.002	0.000	0.000	0.000	0.000
61	A	61	HIS	0	0.042	0.020	16.254	-0.049	-0.049	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.881	-0.939	16.147	-0.499	-0.499	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.008	0.002	16.005	-0.056	-0.056	0.000	0.000	0.000	0.000
64	A	64	ILE	0	-0.014	-0.011	12.881	-0.053	-0.053	0.000	0.000	0.000	0.000
65	A	65	SER	0	0.011	-0.001	11.892	-0.079	-0.079	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.028	-0.008	11.129	-0.071	-0.071	0.000	0.000	0.000	0.000
67	A	67	ALA	0	0.018	0.018	11.441	-0.123	-0.123	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.029	-0.021	6.608	-0.150	-0.150	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.915	-0.962	6.561	-1.632	-1.632	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.033	-0.018	7.215	-0.338	-0.338	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.010	-0.012	5.676	-0.144	-0.144	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.045	-0.029	2.083	1.342	-2.048	6.561	-0.798	-2.373	0.001
73	A	73	GLN	0	0.026	0.018	3.305	-2.633	-1.707	0.065	-0.414	-0.577	-0.004
74	A	74	LEU	0	-0.067	-0.030	5.786	0.069	0.069	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.096	-0.048	2.440	-0.420	0.249	0.989	-0.366	-1.292	-0.003
76	A	76	GLU	-1	-1.012	-0.991	1.941	-6.146	-6.120	3.117	-1.056	-2.087	-0.008
77	A	77	ILE	-1	-0.939	-0.968	3.619	-0.671	-0.476	0.025	-0.033	-0.187	-0.001

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