FMO DATABASE

FMODB ID: 72VGK

Calculation Name: 1JQQ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1JQQ

Chain ID: A

ChEMBL ID:

UniProt ID: P80667

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	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	79
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-516343.072374
FMO2-HF: Nuclear repulsion	484475.240571
FMO2-HF: Total energy	-31867.831803
FMO2-MP2: Total energy	-31961.624545

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: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.
-6.025	-2.364	7.631	-3.758	-7.534	-0.026

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 : -0.003 / q_NPA : 0.006

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	GLU	-1	-0.951	-0.985	2.936	-6.831	-2.592	0.365	-2.410	-2.194	-0.003
4	A	4	PHE	0	-0.059	-0.041	5.256	0.339	0.477	-0.001	-0.005	-0.132	0.000
5	A	5	GLY	0	0.029	0.025	2.186	1.491	0.220	3.355	-0.809	-1.274	0.002
6	A	6	SER	0	0.022	-0.007	2.588	-2.721	-2.391	3.889	-0.510	-3.709	-0.025
7	A	7	GLU	-1	-0.916	-0.937	3.652	1.108	1.333	0.023	-0.024	-0.225	0.000
8	A	8	PRO	0	-0.021	-0.021	6.965	-0.274	-0.274	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.018	0.010	8.446	0.074	0.074	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.881	-0.947	11.087	-0.004	-0.004	0.000	0.000	0.000	0.000
11	A	11	PRO	0	0.028	-0.006	14.709	-0.016	-0.016	0.000	0.000	0.000	0.000
12	A	12	SER	0	-0.020	-0.007	16.789	-0.015	-0.015	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.921	0.973	11.842	-0.075	-0.075	0.000	0.000	0.000	0.000
14	A	14	LEU	0	-0.044	-0.012	13.223	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.823	-0.903	16.705	-0.045	-0.045	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.004	-0.008	18.819	-0.034	-0.034	0.000	0.000	0.000	0.000
17	A	17	ALA	0	0.002	-0.004	21.359	0.024	0.024	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.901	0.952	23.675	0.093	0.093	0.000	0.000	0.000	0.000
19	A	19	ALA	0	0.013	0.020	26.737	0.010	0.010	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.009	-0.001	27.751	0.005	0.005	0.000	0.000	0.000	0.000
21	A	21	TYR	0	-0.052	-0.050	30.269	0.007	0.007	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.872	-0.919	30.062	-0.116	-0.116	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.029	-0.028	24.403	0.009	0.009	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.020	-0.015	28.265	-0.013	-0.013	0.000	0.000	0.000	0.000
25	A	25	PRO	0	-0.037	-0.012	24.349	0.008	0.008	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.915	-0.940	26.299	-0.077	-0.077	0.000	0.000	0.000	0.000
27	A	27	ASN	0	-0.004	0.000	21.463	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	28	PRO	0	-0.015	-0.035	22.667	-0.016	-0.016	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.944	-0.951	19.365	-0.230	-0.230	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.053	-0.016	15.340	-0.041	-0.041	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.853	-0.939	18.306	-0.155	-0.155	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.050	0.032	18.849	-0.020	-0.020	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.003	-0.007	21.738	0.020	0.020	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.003	-0.020	24.029	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.937	0.992	27.020	0.146	0.146	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.975	0.991	29.486	0.074	0.074	0.000	0.000	0.000	0.000
37	A	37	GLY	0	-0.029	-0.019	30.328	0.001	0.001	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.905	-0.972	25.758	-0.177	-0.177	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.018	-0.021	24.259	0.007	0.007	0.000	0.000	0.000	0.000
40	A	40	MET	0	0.001	0.011	20.054	-0.015	-0.015	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.001	0.002	16.532	0.022	0.022	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.002	-0.011	15.760	-0.027	-0.027	0.000	0.000	0.000	0.000
43	A	43	LEU	0	-0.047	-0.005	11.308	-0.009	-0.009	0.000	0.000	0.000	0.000
44	A	44	SER	0	-0.030	-0.025	10.864	0.052	0.052	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.881	0.937	12.833	0.028	0.028	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.898	0.961	11.627	-0.113	-0.113	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.713	-0.836	13.829	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	48	PRO	0	0.005	-0.017	12.238	0.015	0.015	0.000	0.000	0.000	0.000
49	A	49	LEU	0	-0.030	-0.023	11.650	0.019	0.019	0.000	0.000	0.000	0.000
50	A	50	GLY	0	-0.019	0.009	11.507	0.073	0.073	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.821	0.890	12.273	-0.035	-0.035	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.881	-0.932	15.570	0.080	0.080	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.043	-0.024	17.480	-0.013	-0.013	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.880	-0.937	19.572	-0.018	-0.018	0.000	0.000	0.000	0.000
55	A	55	TRP	0	0.025	0.012	19.577	-0.018	-0.018	0.000	0.000	0.000	0.000
56	A	56	TRP	0	0.015	-0.001	16.987	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.966	1.007	9.784	0.615	0.615	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.002	-0.016	15.309	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.940	0.973	12.996	0.641	0.641	0.000	0.000	0.000	0.000
60	A	60	THR	0	0.039	0.007	16.743	0.022	0.022	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.898	0.965	20.018	0.153	0.153	0.000	0.000	0.000	0.000
62	A	62	ASN	0	-0.048	-0.026	21.800	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	63	GLY	0	0.029	0.034	18.118	-0.016	-0.016	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.007	-0.002	16.714	-0.028	-0.028	0.000	0.000	0.000	0.000
65	A	65	ILE	0	0.023	-0.013	12.062	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.036	-0.017	15.872	-0.006	-0.006	0.000	0.000	0.000	0.000
67	A	67	TYR	0	-0.069	-0.049	13.410	-0.022	-0.022	0.000	0.000	0.000	0.000
68	A	68	ILE	0	-0.020	-0.003	18.778	0.002	0.002	0.000	0.000	0.000	0.000
69	A	69	PRO	0	0.045	0.028	21.435	0.008	0.008	0.000	0.000	0.000	0.000
70	A	70	TYR	0	0.056	0.007	22.374	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.010	-0.001	23.660	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.022	-0.017	26.297	0.004	0.004	0.000	0.000	0.000	0.000
73	A	73	ILE	0	-0.053	-0.024	21.801	-0.010	-0.010	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.909	-0.952	26.219	-0.068	-0.068	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.017	0.001	21.830	-0.013	-0.013	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.042	-0.019	24.772	0.012	0.012	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.974	0.986	25.481	0.035	0.035	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.956	0.968	23.614	0.034	0.034	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.996	1.013	28.558	0.070	0.070	0.000	0.000	0.000	0.000

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