FMO DATABASE

FMODB ID: JYL19

Calculation Name: 3FT9-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3FT9

Chain ID: A

ChEMBL ID:

UniProt ID: Q69B42

Base Structure: X-ray

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	94
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-695979.84249
FMO2-HF: Nuclear repulsion	659165.972768
FMO2-HF: Total energy	-36813.869722
FMO2-MP2: Total energy	-36922.729836

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:2:VAL)

Summations of interaction energy for fragment #1(A:2:VAL)

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.
42.348	47.743	2.947	-3.46	-4.881	-0.03

Interaction energy analysis for fragmet #1(A:2:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.808 / q_NPA : 0.888

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	4	VAL	0	0.059	0.042	3.722	4.389	6.038	-0.032	-0.590	-1.027	-0.001
23	A	24	THR	0	-0.030	-0.011	4.071	3.953	4.244	0.000	-0.078	-0.213	0.000
24	A	25	ARG	1	0.903	0.936	2.313	18.733	21.417	2.955	-2.624	-3.015	-0.028
25	A	26	PRO	0	0.028	0.004	3.239	4.967	5.396	0.025	-0.131	-0.322	-0.001
76	A	77	ASN	0	-0.067	-0.034	3.909	-3.932	-3.708	0.000	-0.023	-0.201	0.000
78	A	79	PHE	0	-0.027	-0.012	3.954	-3.063	-2.945	-0.001	-0.014	-0.103	0.000
4	A	5	THR	0	-0.037	-0.021	7.103	0.249	0.249	0.000	0.000	0.000	0.000
5	A	6	PHE	0	0.062	0.025	9.933	0.151	0.151	0.000	0.000	0.000	0.000
6	A	7	THR	0	0.014	0.018	13.985	0.233	0.233	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.038	0.033	17.121	0.251	0.251	0.000	0.000	0.000	0.000
8	A	9	GLN	0	0.034	0.018	19.971	0.346	0.346	0.000	0.000	0.000	0.000
9	A	10	LYS	1	0.969	0.962	22.477	11.525	11.525	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.014	0.010	26.116	-0.056	-0.056	0.000	0.000	0.000	0.000
11	A	12	SER	0	-0.018	-0.004	23.394	-0.136	-0.136	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.896	-0.953	25.700	-10.341	-10.341	0.000	0.000	0.000	0.000
13	A	14	PRO	0	0.044	0.009	26.675	-0.345	-0.345	0.000	0.000	0.000	0.000
14	A	15	LYS	1	0.906	0.976	27.530	9.807	9.807	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.840	0.918	24.988	11.533	11.533	0.000	0.000	0.000	0.000
16	A	17	LEU	0	0.056	0.044	19.028	-0.034	-0.034	0.000	0.000	0.000	0.000
17	A	18	VAL	0	-0.003	-0.013	21.281	-0.073	-0.073	0.000	0.000	0.000	0.000
18	A	19	LEU	0	0.022	0.011	15.815	-0.083	-0.083	0.000	0.000	0.000	0.000
19	A	20	ASP	-1	-0.826	-0.902	15.404	-19.792	-19.792	0.000	0.000	0.000	0.000
20	A	21	ILE	0	-0.005	0.006	10.817	-0.781	-0.781	0.000	0.000	0.000	0.000
21	A	22	LYS	1	0.788	0.885	9.833	22.290	22.290	0.000	0.000	0.000	0.000
22	A	23	TYR	0	0.054	0.029	5.400	-5.083	-5.083	0.000	0.000	0.000	0.000
26	A	27	GLY	0	0.038	0.027	6.108	-0.619	-0.619	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.751	-0.835	6.628	-27.702	-27.702	0.000	0.000	0.000	0.000
28	A	29	SER	0	-0.067	-0.056	8.355	0.454	0.454	0.000	0.000	0.000	0.000
29	A	30	LEU	0	-0.039	-0.010	9.115	0.349	0.349	0.000	0.000	0.000	0.000
30	A	31	ALA	0	-0.043	-0.014	10.123	1.548	1.548	0.000	0.000	0.000	0.000
31	A	32	GLU	-1	-0.852	-0.923	12.359	-16.537	-16.537	0.000	0.000	0.000	0.000
32	A	33	VAL	0	-0.020	-0.022	11.630	-2.058	-2.058	0.000	0.000	0.000	0.000
33	A	34	GLU	-1	-0.757	-0.834	13.644	-16.465	-16.465	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.021	-0.008	14.460	-1.337	-1.337	0.000	0.000	0.000	0.000
35	A	36	ARG	1	0.892	0.956	16.763	16.081	16.081	0.000	0.000	0.000	0.000
36	A	37	GLN	0	-0.006	-0.020	18.640	-0.156	-0.156	0.000	0.000	0.000	0.000
37	A	38	HIS	0	-0.048	-0.022	20.792	0.441	0.441	0.000	0.000	0.000	0.000
38	A	39	GLY	0	-0.026	-0.019	22.178	0.505	0.505	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.049	-0.001	23.014	0.229	0.229	0.000	0.000	0.000	0.000
40	A	41	GLU	-1	-0.883	-0.952	21.861	-11.919	-11.919	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.928	-0.961	21.419	-12.070	-12.070	0.000	0.000	0.000	0.000
42	A	43	TRP	0	-0.031	-0.029	14.276	-0.986	-0.986	0.000	0.000	0.000	0.000
43	A	44	GLU	-1	-0.839	-0.910	19.168	-12.513	-12.513	0.000	0.000	0.000	0.000
44	A	45	PRO	0	-0.009	-0.021	18.300	-0.795	-0.795	0.000	0.000	0.000	0.000
45	A	46	LEU	0	-0.044	-0.012	15.682	0.554	0.554	0.000	0.000	0.000	0.000
46	A	47	THR	0	-0.020	-0.012	18.701	-0.048	-0.048	0.000	0.000	0.000	0.000
47	A	48	LYS	1	0.899	0.963	15.772	17.663	17.663	0.000	0.000	0.000	0.000
48	A	49	LYS	1	0.860	0.920	20.018	12.880	12.880	0.000	0.000	0.000	0.000
49	A	50	GLY	0	0.052	0.030	22.129	-0.139	-0.139	0.000	0.000	0.000	0.000
50	A	51	ASN	0	-0.017	-0.027	17.714	0.165	0.165	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.027	0.003	17.081	-1.146	-1.146	0.000	0.000	0.000	0.000
52	A	53	TRP	0	0.014	-0.004	14.046	0.442	0.442	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.817	-0.899	18.585	-12.007	-12.007	0.000	0.000	0.000	0.000
54	A	55	VAL	0	0.067	0.043	19.719	0.087	0.087	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.928	0.957	22.120	10.550	10.550	0.000	0.000	0.000	0.000
56	A	57	SER	0	0.110	0.070	25.708	0.170	0.170	0.000	0.000	0.000	0.000
57	A	58	SER	0	-0.036	-0.025	27.854	0.147	0.147	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.938	0.962	30.103	9.147	9.147	0.000	0.000	0.000	0.000
59	A	60	PRO	0	-0.031	-0.035	29.019	-0.265	-0.265	0.000	0.000	0.000	0.000
60	A	61	LEU	0	-0.003	0.018	22.737	0.049	0.049	0.000	0.000	0.000	0.000
61	A	62	VAL	0	0.017	-0.005	25.146	0.004	0.004	0.000	0.000	0.000	0.000
62	A	63	GLY	0	0.008	0.019	21.480	-0.459	-0.459	0.000	0.000	0.000	0.000
63	A	64	PRO	0	-0.030	-0.039	19.090	0.635	0.635	0.000	0.000	0.000	0.000
64	A	65	PHE	0	-0.050	-0.019	17.561	0.200	0.200	0.000	0.000	0.000	0.000
65	A	66	ASN	0	0.017	0.025	14.477	-1.576	-1.576	0.000	0.000	0.000	0.000
66	A	67	PHE	0	0.000	-0.019	11.474	0.750	0.750	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.858	0.928	10.758	16.126	16.126	0.000	0.000	0.000	0.000
68	A	69	PHE	0	-0.003	-0.014	7.708	-0.035	-0.035	0.000	0.000	0.000	0.000
69	A	70	MET	0	0.004	0.023	9.301	-1.428	-1.428	0.000	0.000	0.000	0.000
70	A	71	SER	0	-0.047	-0.049	7.373	0.749	0.749	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.949	0.957	9.467	21.787	21.787	0.000	0.000	0.000	0.000
72	A	73	GLY	0	-0.007	0.009	10.396	1.484	1.484	0.000	0.000	0.000	0.000
73	A	74	GLY	0	0.001	0.006	11.318	0.180	0.180	0.000	0.000	0.000	0.000
74	A	75	MET	0	-0.051	-0.024	6.628	-0.848	-0.848	0.000	0.000	0.000	0.000
75	A	76	ARG	1	0.832	0.880	8.523	19.326	19.326	0.000	0.000	0.000	0.000
77	A	78	VAL	0	0.031	0.007	7.178	1.929	1.929	0.000	0.000	0.000	0.000
79	A	80	ASP	-1	-0.787	-0.904	9.861	-18.319	-18.319	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.877	-0.962	13.352	-16.455	-16.455	0.000	0.000	0.000	0.000
81	A	82	VAL	0	-0.036	0.006	11.357	0.130	0.130	0.000	0.000	0.000	0.000
82	A	83	ILE	0	-0.036	-0.021	14.206	0.046	0.046	0.000	0.000	0.000	0.000
83	A	84	PRO	0	0.029	0.025	17.486	0.458	0.458	0.000	0.000	0.000	0.000
84	A	85	THR	0	0.070	0.013	21.075	-0.160	-0.160	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.020	0.006	23.986	0.259	0.259	0.000	0.000	0.000	0.000
86	A	87	PHE	0	-0.021	0.003	21.572	-0.361	-0.361	0.000	0.000	0.000	0.000
87	A	88	SER	0	-0.007	-0.015	22.668	0.609	0.609	0.000	0.000	0.000	0.000
88	A	89	ILE	0	-0.024	-0.029	22.677	-0.531	-0.531	0.000	0.000	0.000	0.000
89	A	90	GLY	0	-0.005	-0.002	22.138	0.371	0.371	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.922	0.988	18.793	15.864	15.864	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.037	-0.037	13.587	-0.079	-0.079	0.000	0.000	0.000	0.000
92	A	93	TYR	0	0.011	-0.002	14.825	0.953	0.953	0.000	0.000	0.000	0.000
93	A	94	LYS	1	0.909	0.935	8.047	32.018	32.018	0.000	0.000	0.000	0.000
94	A	95	PRO	-1	-0.863	-0.899	7.826	-30.686	-30.686	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:VAL)