FMO DATABASE

FMODB ID: 5J9JZ

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	OptHSide
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	-700021.981032
FMO2-HF: Nuclear repulsion	661631.804787
FMO2-HF: Total energy	-38390.176245
FMO2-MP2: Total energy	-38502.216767

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.
-2.997	-1.051	-0.011	-0.943	-0.993	0.004

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 : -0.018 / q_NPA : -0.011

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	-0.036	-0.007	3.835	-1.313	0.633	-0.011	-0.943	-0.993	0.004
4	A	7	SER	0	-0.005	-0.003	6.606	0.579	0.579	0.000	0.000	0.000	0.000
5	A	8	SER	0	-0.046	-0.047	8.685	-0.040	-0.040	0.000	0.000	0.000	0.000
6	A	9	GLY	0	0.011	0.006	12.088	0.036	0.036	0.000	0.000	0.000	0.000
7	A	10	GLU	-1	-0.878	-0.916	6.773	-1.722	-1.722	0.000	0.000	0.000	0.000
8	A	11	VAL	0	-0.001	-0.008	9.150	0.037	0.037	0.000	0.000	0.000	0.000
9	A	12	ALA	0	0.034	0.024	7.451	-0.269	-0.269	0.000	0.000	0.000	0.000
10	A	13	SER	0	-0.022	-0.007	8.844	0.250	0.250	0.000	0.000	0.000	0.000
11	A	14	VAL	0	0.002	-0.021	10.699	-0.077	-0.077	0.000	0.000	0.000	0.000
12	A	15	LEU	0	0.004	0.009	13.288	0.080	0.080	0.000	0.000	0.000	0.000
13	A	16	PRO	0	-0.015	-0.005	14.885	-0.023	-0.023	0.000	0.000	0.000	0.000
14	A	17	LEU	0	0.017	0.009	11.948	-0.008	-0.008	0.000	0.000	0.000	0.000
15	A	18	GLY	0	-0.005	-0.005	15.985	0.032	0.032	0.000	0.000	0.000	0.000
16	A	19	LYS	1	0.919	0.943	19.367	0.113	0.113	0.000	0.000	0.000	0.000
17	A	20	GLN	0	0.022	0.016	14.739	0.047	0.047	0.000	0.000	0.000	0.000
18	A	21	LEU	0	-0.021	0.014	15.334	0.006	0.006	0.000	0.000	0.000	0.000
19	A	22	THR	0	0.006	-0.019	15.709	-0.005	-0.005	0.000	0.000	0.000	0.000
20	A	23	GLN	0	-0.028	-0.002	15.085	0.014	0.014	0.000	0.000	0.000	0.000
21	A	24	THR	0	-0.045	-0.022	10.135	0.010	0.010	0.000	0.000	0.000	0.000
22	A	25	PRO	0	-0.002	0.009	8.798	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	26	SER	0	0.023	0.001	10.036	-0.100	-0.100	0.000	0.000	0.000	0.000
24	A	27	ALA	0	-0.011	-0.001	5.716	0.106	0.106	0.000	0.000	0.000	0.000
25	A	28	ALA	0	-0.002	0.005	6.768	0.025	0.025	0.000	0.000	0.000	0.000
26	A	29	LEU	0	-0.026	-0.012	5.478	-0.555	-0.555	0.000	0.000	0.000	0.000
27	A	30	PHE	0	0.045	0.009	6.429	-0.729	-0.729	0.000	0.000	0.000	0.000
28	A	31	LYS	1	0.909	0.979	8.132	0.630	0.630	0.000	0.000	0.000	0.000
29	A	32	GLU	-1	-0.889	-0.935	10.146	-0.384	-0.384	0.000	0.000	0.000	0.000
30	A	33	HIS	0	-0.017	-0.026	12.877	0.043	0.043	0.000	0.000	0.000	0.000
31	A	34	ARG	1	0.957	0.966	16.405	0.258	0.258	0.000	0.000	0.000	0.000
32	A	35	LEU	0	-0.019	-0.003	15.216	0.022	0.022	0.000	0.000	0.000	0.000
33	A	36	GLU	-1	-0.879	-0.945	11.404	-0.458	-0.458	0.000	0.000	0.000	0.000
34	A	37	VAL	0	-0.004	0.012	11.415	0.089	0.089	0.000	0.000	0.000	0.000
35	A	38	MET	0	0.018	0.007	10.072	-0.203	-0.203	0.000	0.000	0.000	0.000
36	A	39	ARG	1	0.941	0.987	9.232	0.817	0.817	0.000	0.000	0.000	0.000
37	A	40	MET	0	-0.009	-0.008	11.298	0.012	0.012	0.000	0.000	0.000	0.000
38	A	41	VAL	0	0.002	-0.013	12.446	-0.020	-0.020	0.000	0.000	0.000	0.000
39	A	42	LEU	0	-0.063	-0.028	15.165	0.041	0.041	0.000	0.000	0.000	0.000
40	A	43	PRO	0	0.036	0.018	18.582	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	44	ALA	0	0.033	-0.014	20.977	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	45	GLY	0	0.002	0.007	24.530	0.012	0.012	0.000	0.000	0.000	0.000
43	A	46	LYS	1	0.840	0.936	20.327	0.063	0.063	0.000	0.000	0.000	0.000
44	A	47	GLN	0	0.023	-0.002	23.721	-0.006	-0.006	0.000	0.000	0.000	0.000
45	A	48	VAL	0	-0.068	-0.026	20.418	0.011	0.011	0.000	0.000	0.000	0.000
46	A	49	GLY	0	0.056	0.025	23.655	-0.003	-0.003	0.000	0.000	0.000	0.000
47	A	50	SER	0	0.018	0.013	25.682	-0.012	-0.012	0.000	0.000	0.000	0.000
48	A	51	HIS	0	-0.025	-0.012	22.228	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	52	SER	0	0.050	0.020	25.336	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	53	VAL	0	0.000	0.006	20.027	0.008	0.008	0.000	0.000	0.000	0.000
51	A	54	ALA	0	0.024	0.001	23.311	0.002	0.002	0.000	0.000	0.000	0.000
52	A	55	GLY	0	0.026	0.030	22.864	0.008	0.008	0.000	0.000	0.000	0.000
53	A	56	PRO	0	-0.005	-0.003	23.725	0.002	0.002	0.000	0.000	0.000	0.000
54	A	57	SER	0	-0.014	-0.018	20.485	-0.021	-0.021	0.000	0.000	0.000	0.000
55	A	58	THR	0	0.013	0.006	19.509	0.019	0.019	0.000	0.000	0.000	0.000
56	A	59	ILE	0	-0.006	-0.001	19.323	-0.035	-0.035	0.000	0.000	0.000	0.000
57	A	60	GLN	0	0.001	0.008	18.662	0.024	0.024	0.000	0.000	0.000	0.000
58	A	61	CYS	0	-0.028	0.009	18.891	-0.025	-0.025	0.000	0.000	0.000	0.000
59	A	62	LEU	0	0.020	0.020	14.633	0.000	0.000	0.000	0.000	0.000	0.000
60	A	63	GLU	-1	-0.744	-0.851	17.077	-0.284	-0.284	0.000	0.000	0.000	0.000
61	A	64	GLY	0	0.001	0.010	21.096	0.000	0.000	0.000	0.000	0.000	0.000
62	A	65	GLU	-1	-0.831	-0.911	23.628	-0.120	-0.120	0.000	0.000	0.000	0.000
63	A	66	VAL	0	-0.005	-0.002	22.481	0.007	0.007	0.000	0.000	0.000	0.000
64	A	67	GLU	-1	-0.825	-0.888	25.137	-0.092	-0.092	0.000	0.000	0.000	0.000
65	A	68	ILE	0	-0.029	-0.023	23.060	-0.002	-0.002	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.050	0.043	27.108	0.003	0.003	0.000	0.000	0.000	0.000
67	A	70	VAL	0	-0.044	-0.047	28.529	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	71	ASP	-1	-0.870	-0.938	31.012	-0.082	-0.082	0.000	0.000	0.000	0.000
69	A	72	GLY	0	-0.018	-0.008	34.200	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	73	ALA	0	-0.095	-0.052	33.934	0.001	0.001	0.000	0.000	0.000	0.000
71	A	74	GLN	0	0.080	0.050	31.427	-0.008	-0.008	0.000	0.000	0.000	0.000
72	A	75	ARG	1	0.891	0.954	28.936	0.116	0.116	0.000	0.000	0.000	0.000
73	A	76	ARG	1	0.806	0.878	29.012	0.094	0.094	0.000	0.000	0.000	0.000
74	A	77	LEU	0	-0.048	-0.020	23.884	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	78	HIS	1	0.882	0.921	26.414	0.141	0.141	0.000	0.000	0.000	0.000
76	A	79	GLN	0	-0.022	-0.034	21.400	0.005	0.005	0.000	0.000	0.000	0.000
77	A	80	GLY	0	-0.019	-0.008	22.791	0.012	0.012	0.000	0.000	0.000	0.000
78	A	81	ASP	-1	-0.839	-0.889	24.150	-0.173	-0.173	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.015	-0.024	21.554	-0.024	-0.024	0.000	0.000	0.000	0.000
80	A	83	LEU	0	-0.011	0.002	23.732	0.019	0.019	0.000	0.000	0.000	0.000
81	A	84	TYR	0	0.002	-0.011	23.948	-0.021	-0.021	0.000	0.000	0.000	0.000
82	A	85	LEU	0	-0.011	-0.001	23.232	0.019	0.019	0.000	0.000	0.000	0.000
83	A	86	GLY	0	0.054	0.023	25.755	-0.011	-0.011	0.000	0.000	0.000	0.000
84	A	87	ALA	0	-0.019	-0.023	26.242	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	88	GLY	0	0.003	0.001	26.394	0.011	0.011	0.000	0.000	0.000	0.000
86	A	89	ALA	0	-0.018	0.003	27.770	0.011	0.011	0.000	0.000	0.000	0.000
87	A	90	ALA	0	0.028	0.034	27.292	-0.010	-0.010	0.000	0.000	0.000	0.000
88	A	91	HIS	1	0.798	0.877	22.531	0.146	0.146	0.000	0.000	0.000	0.000
89	A	92	ASP	-1	-0.914	-0.948	25.992	-0.088	-0.088	0.000	0.000	0.000	0.000
90	A	93	VAL	0	-0.005	-0.013	21.482	-0.012	-0.012	0.000	0.000	0.000	0.000
91	A	94	ASN	0	0.042	0.030	24.709	0.021	0.021	0.000	0.000	0.000	0.000
92	A	95	ALA	0	0.022	0.019	22.376	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	96	ILE	0	-0.012	0.003	24.381	0.015	0.015	0.000	0.000	0.000	0.000
94	A	97	THR	0	-0.018	-0.016	24.011	0.010	0.010	0.000	0.000	0.000	0.000
95	A	98	ASN	0	-0.005	-0.005	20.844	0.002	0.002	0.000	0.000	0.000	0.000
96	A	99	THR	0	-0.031	-0.025	20.133	-0.009	-0.009	0.000	0.000	0.000	0.000
97	A	100	SER	0	-0.009	-0.033	14.801	-0.016	-0.016	0.000	0.000	0.000	0.000
98	A	101	LEU	0	0.017	0.004	15.868	0.012	0.012	0.000	0.000	0.000	0.000
99	A	102	LEU	0	-0.001	0.013	12.975	-0.053	-0.053	0.000	0.000	0.000	0.000
100	A	103	VAL	0	-0.008	-0.014	14.462	0.062	0.062	0.000	0.000	0.000	0.000
101	A	104	THR	0	0.007	0.013	14.616	-0.098	-0.098	0.000	0.000	0.000	0.000
102	A	105	VAL	0	-0.011	-0.022	16.298	0.067	0.067	0.000	0.000	0.000	0.000
103	A	106	VAL	0	0.034	0.019	17.312	-0.032	-0.032	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.063	-0.027	15.068	0.032	0.032	0.000	0.000	0.000	0.000
105	A	108	VAL	0	0.004	0.000	19.606	0.007	0.007	0.000	0.000	0.000	0.000

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