FMO DATABASE

FMODB ID: 4JNJN

Calculation Name: 3FJS-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3FJS

Chain ID: A

ChEMBL ID:

UniProt ID: Q46TU1

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

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. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	105
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-699728.589545
FMO2-HF: Nuclear repulsion	661338.778097
FMO2-HF: Total energy	-38389.811449
FMO2-MP2: Total energy	-38501.872603

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:4:PRO)

Summations of interaction energy for fragment #1(A:4:PRO)

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.
-3.112	-1.2	-0.012	-0.92	-0.981	0.003

Interaction energy analysis for fragmet #1(A:4:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.014 / q_NPA : -0.017

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	6	LEU	0	-0.023	0.003	3.835	-1.288	0.624	-0.012	-0.920	-0.981	0.003
4	A	7	SER	0	-0.003	0.007	6.606	0.701	0.701	0.000	0.000	0.000	0.000
5	A	8	SER	0	-0.039	-0.043	8.676	-0.070	-0.070	0.000	0.000	0.000	0.000
6	A	9	GLY	0	0.012	0.006	12.103	0.035	0.035	0.000	0.000	0.000	0.000
7	A	10	GLU	-1	-0.901	-0.936	6.345	-1.927	-1.927	0.000	0.000	0.000	0.000
8	A	11	VAL	0	-0.003	-0.006	9.124	0.041	0.041	0.000	0.000	0.000	0.000
9	A	12	ALA	0	0.034	0.021	7.278	-0.293	-0.293	0.000	0.000	0.000	0.000
10	A	13	SER	0	-0.020	-0.011	8.712	0.273	0.273	0.000	0.000	0.000	0.000
11	A	14	VAL	0	-0.015	-0.025	10.569	-0.091	-0.091	0.000	0.000	0.000	0.000
12	A	15	LEU	0	0.006	0.006	13.103	0.089	0.089	0.000	0.000	0.000	0.000
13	A	16	PRO	0	-0.026	-0.009	14.779	-0.031	-0.031	0.000	0.000	0.000	0.000
14	A	17	LEU	0	0.006	0.004	11.930	-0.014	-0.014	0.000	0.000	0.000	0.000
15	A	18	GLY	0	-0.006	-0.005	15.935	0.031	0.031	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.914	0.940	19.331	0.156	0.156	0.000	0.000	0.000	0.000
17	A	20	GLN	0	0.041	0.025	14.653	0.056	0.056	0.000	0.000	0.000	0.000
18	A	21	LEU	0	-0.018	0.025	15.130	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	22	THR	0	-0.010	-0.025	15.513	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	23	GLN	0	-0.024	-0.001	15.035	0.018	0.018	0.000	0.000	0.000	0.000
21	A	24	THR	0	-0.042	-0.028	9.970	-0.003	-0.003	0.000	0.000	0.000	0.000
22	A	25	PRO	0	-0.001	0.007	8.581	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	26	SER	0	0.023	0.003	9.861	-0.122	-0.122	0.000	0.000	0.000	0.000
24	A	27	ALA	0	-0.007	-0.001	5.743	0.103	0.103	0.000	0.000	0.000	0.000
25	A	28	ALA	0	-0.009	0.005	6.772	0.038	0.038	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.027	-0.014	5.715	-0.639	-0.639	0.000	0.000	0.000	0.000
27	A	30	PHE	0	0.052	0.013	6.434	-0.728	-0.728	0.000	0.000	0.000	0.000
28	A	31	LYS	1	0.910	0.974	8.058	0.527	0.527	0.000	0.000	0.000	0.000
29	A	32	GLU	-1	-0.894	-0.939	10.142	-0.319	-0.319	0.000	0.000	0.000	0.000
30	A	33	HIS	0	-0.017	-0.034	12.898	0.039	0.039	0.000	0.000	0.000	0.000
31	A	34	ARG	1	0.965	0.982	16.445	0.213	0.213	0.000	0.000	0.000	0.000
32	A	35	LEU	0	-0.003	0.009	14.896	0.013	0.013	0.000	0.000	0.000	0.000
33	A	36	GLU	-1	-0.897	-0.955	11.352	-0.365	-0.365	0.000	0.000	0.000	0.000
34	A	37	VAL	0	-0.001	0.015	11.372	0.078	0.078	0.000	0.000	0.000	0.000
35	A	38	MET	0	0.016	0.008	10.196	-0.207	-0.207	0.000	0.000	0.000	0.000
36	A	39	ARG	1	0.968	1.002	9.326	0.917	0.917	0.000	0.000	0.000	0.000
37	A	40	MET	0	-0.012	-0.013	11.460	0.001	0.001	0.000	0.000	0.000	0.000
38	A	41	VAL	0	-0.011	-0.014	12.512	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	42	LEU	0	-0.054	-0.027	15.157	0.046	0.046	0.000	0.000	0.000	0.000
40	A	43	PRO	0	0.023	0.011	18.348	-0.006	-0.006	0.000	0.000	0.000	0.000
41	A	44	ALA	0	0.043	-0.011	20.805	0.001	0.001	0.000	0.000	0.000	0.000
42	A	45	GLY	0	-0.005	0.005	24.412	0.013	0.013	0.000	0.000	0.000	0.000
43	A	46	LYS	1	0.891	0.965	19.792	0.060	0.060	0.000	0.000	0.000	0.000
44	A	47	GLN	0	-0.008	-0.034	23.572	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	48	VAL	0	-0.072	-0.028	20.493	0.009	0.009	0.000	0.000	0.000	0.000
46	A	49	GLY	0	0.047	0.022	23.625	-0.004	-0.004	0.000	0.000	0.000	0.000
47	A	50	SER	0	0.018	0.017	25.718	-0.012	-0.012	0.000	0.000	0.000	0.000
48	A	51	HIS	0	-0.067	-0.041	22.274	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	52	SER	0	0.058	0.020	25.264	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	53	VAL	0	-0.002	0.009	20.074	0.010	0.010	0.000	0.000	0.000	0.000
51	A	54	ALA	0	0.024	0.002	23.293	0.000	0.000	0.000	0.000	0.000	0.000
52	A	55	GLY	0	0.018	0.024	22.825	0.006	0.006	0.000	0.000	0.000	0.000
53	A	56	PRO	0	-0.001	-0.001	23.668	0.000	0.000	0.000	0.000	0.000	0.000
54	A	57	SER	0	-0.013	-0.015	20.458	-0.021	-0.021	0.000	0.000	0.000	0.000
55	A	58	THR	0	0.007	-0.001	20.363	0.010	0.010	0.000	0.000	0.000	0.000
56	A	59	ILE	0	0.024	0.014	19.706	-0.033	-0.033	0.000	0.000	0.000	0.000
57	A	60	GLN	0	-0.001	0.006	18.963	0.031	0.031	0.000	0.000	0.000	0.000
58	A	61	CYS	0	-0.026	0.010	19.349	-0.030	-0.030	0.000	0.000	0.000	0.000
59	A	62	LEU	0	0.012	0.013	15.036	0.002	0.002	0.000	0.000	0.000	0.000
60	A	63	GLU	-1	-0.743	-0.859	17.466	-0.329	-0.329	0.000	0.000	0.000	0.000
61	A	64	GLY	0	-0.002	0.011	21.324	0.001	0.001	0.000	0.000	0.000	0.000
62	A	65	GLU	-1	-0.865	-0.942	23.821	-0.133	-0.133	0.000	0.000	0.000	0.000
63	A	66	VAL	0	-0.002	0.001	22.679	0.007	0.007	0.000	0.000	0.000	0.000
64	A	67	GLU	-1	-0.880	-0.945	25.328	-0.098	-0.098	0.000	0.000	0.000	0.000
65	A	68	ILE	0	-0.029	-0.018	23.730	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.046	0.045	27.360	0.003	0.003	0.000	0.000	0.000	0.000
67	A	70	VAL	0	-0.050	-0.047	28.900	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	71	ASP	-1	-0.880	-0.942	31.306	-0.076	-0.076	0.000	0.000	0.000	0.000
69	A	72	GLY	0	-0.024	-0.013	34.357	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	73	ALA	0	-0.093	-0.053	34.375	0.001	0.001	0.000	0.000	0.000	0.000
71	A	74	GLN	0	0.084	0.051	32.003	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	75	ARG	1	0.887	0.950	29.292	0.120	0.120	0.000	0.000	0.000	0.000
73	A	76	ARG	1	0.884	0.950	29.308	0.104	0.104	0.000	0.000	0.000	0.000
74	A	77	LEU	0	-0.046	-0.019	24.041	0.000	0.000	0.000	0.000	0.000	0.000
75	A	78	HIS	1	0.903	0.936	26.764	0.154	0.154	0.000	0.000	0.000	0.000
76	A	79	GLN	0	-0.018	-0.031	21.391	0.008	0.008	0.000	0.000	0.000	0.000
77	A	80	GLY	0	-0.023	-0.009	22.967	0.013	0.013	0.000	0.000	0.000	0.000
78	A	81	ASP	-1	-0.836	-0.888	24.253	-0.188	-0.188	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.021	-0.025	21.776	-0.025	-0.025	0.000	0.000	0.000	0.000
80	A	83	LEU	0	-0.009	0.005	24.262	0.021	0.021	0.000	0.000	0.000	0.000
81	A	84	TYR	0	-0.013	-0.019	24.429	-0.020	-0.020	0.000	0.000	0.000	0.000
82	A	85	LEU	0	-0.012	-0.003	23.568	0.018	0.018	0.000	0.000	0.000	0.000
83	A	86	GLY	0	0.049	0.023	25.710	-0.010	-0.010	0.000	0.000	0.000	0.000
84	A	87	ALA	0	-0.012	-0.019	26.190	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	88	GLY	0	-0.007	-0.001	26.347	0.010	0.010	0.000	0.000	0.000	0.000
86	A	89	ALA	0	-0.021	0.002	27.710	0.010	0.010	0.000	0.000	0.000	0.000
87	A	90	ALA	0	0.028	0.022	27.219	-0.009	-0.009	0.000	0.000	0.000	0.000
88	A	91	HIS	1	0.832	0.903	22.323	0.144	0.144	0.000	0.000	0.000	0.000
89	A	92	ASP	-1	-0.905	-0.941	26.093	-0.088	-0.088	0.000	0.000	0.000	0.000
90	A	93	VAL	0	-0.003	-0.007	21.563	-0.014	-0.014	0.000	0.000	0.000	0.000
91	A	94	ASN	0	0.066	0.049	24.828	0.021	0.021	0.000	0.000	0.000	0.000
92	A	95	ALA	0	0.013	0.018	22.366	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	96	ILE	0	-0.022	-0.001	24.412	0.016	0.016	0.000	0.000	0.000	0.000
94	A	97	THR	0	-0.012	-0.015	24.009	0.010	0.010	0.000	0.000	0.000	0.000
95	A	98	ASN	0	0.006	-0.001	20.709	0.006	0.006	0.000	0.000	0.000	0.000
96	A	99	THR	0	-0.041	-0.024	20.164	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	100	SER	0	-0.004	-0.032	15.045	-0.017	-0.017	0.000	0.000	0.000	0.000
98	A	101	LEU	0	0.013	0.007	16.160	0.014	0.014	0.000	0.000	0.000	0.000
99	A	102	LEU	0	0.003	0.009	13.186	-0.058	-0.058	0.000	0.000	0.000	0.000
100	A	103	VAL	0	-0.012	-0.014	14.947	0.068	0.068	0.000	0.000	0.000	0.000
101	A	104	THR	0	0.013	0.018	14.875	-0.104	-0.104	0.000	0.000	0.000	0.000
102	A	105	VAL	0	-0.015	-0.023	16.205	0.067	0.067	0.000	0.000	0.000	0.000
103	A	106	VAL	0	0.032	0.015	17.253	-0.026	-0.026	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.065	-0.027	14.930	0.032	0.032	0.000	0.000	0.000	0.000
105	A	108	VAL	0	0.004	-0.001	19.596	0.009	0.009	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:PRO)