FMO DATABASE

FMODB ID: 9L942

Calculation Name: 1TS9-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1TS9

Chain ID: A

ChEMBL ID:

UniProt ID: O28362

Base Structure: X-ray

Registration Date: 2025-10-03

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	98
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-749677.139942
FMO2-HF: Nuclear repulsion	709938.478815
FMO2-HF: Total energy	-39738.661127
FMO2-MP2: Total energy	-39853.547077

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:5:LEU)

Summations of interaction energy for fragment #1(A:5:LEU)

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.
162.03	166.745	0.43	-1.646	-3.499	-0.001

Interaction energy analysis for fragmet #1(A:5:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.910 / q_NPA : 0.935

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	7	GLY	0	0.024	0.023	3.618	5.263	7.283	0.010	-0.801	-1.230	0.000
4	A	8	VAL	0	-0.009	-0.005	2.805	4.124	5.450	0.056	-0.519	-0.864	-0.003
5	A	9	GLU	-1	-0.797	-0.880	4.857	-32.625	-32.368	-0.001	-0.033	-0.223	0.000
66	A	70	LYS	1	0.864	0.939	2.704	45.145	45.958	0.365	-0.244	-0.933	0.002
93	A	97	ALA	0	-0.047	-0.017	3.808	0.051	0.193	0.001	-0.040	-0.103	0.000
94	A	98	LYS	1	0.866	0.930	4.821	32.348	32.505	-0.001	-0.009	-0.146	0.000
6	A	10	LEU	0	0.023	0.017	6.729	4.591	4.591	0.000	0.000	0.000	0.000
7	A	11	ILE	0	-0.020	0.004	7.591	3.096	3.096	0.000	0.000	0.000	0.000
8	A	12	ALA	0	-0.004	0.001	9.557	2.771	2.771	0.000	0.000	0.000	0.000
9	A	13	ARG	1	0.839	0.922	10.852	23.004	23.004	0.000	0.000	0.000	0.000
10	A	14	ASP	-1	-0.828	-0.907	12.726	-18.343	-18.343	0.000	0.000	0.000	0.000
11	A	15	TRP	0	-0.066	-0.078	12.011	-0.902	-0.902	0.000	0.000	0.000	0.000
12	A	16	ILE	0	0.007	0.010	16.302	0.323	0.323	0.000	0.000	0.000	0.000
13	A	17	GLY	0	0.032	0.026	17.872	-0.693	-0.693	0.000	0.000	0.000	0.000
14	A	18	LEU	0	-0.086	-0.029	12.761	-0.890	-0.890	0.000	0.000	0.000	0.000
15	A	19	MET	0	0.020	0.027	16.083	0.899	0.899	0.000	0.000	0.000	0.000
16	A	20	VAL	0	-0.019	-0.023	15.698	-1.559	-1.559	0.000	0.000	0.000	0.000
17	A	21	GLU	-1	-0.778	-0.876	17.473	-14.179	-14.179	0.000	0.000	0.000	0.000
18	A	22	VAL	0	-0.036	0.005	18.254	-1.057	-1.057	0.000	0.000	0.000	0.000
19	A	23	VAL	0	-0.040	-0.030	16.758	0.386	0.386	0.000	0.000	0.000	0.000
20	A	24	GLU	-1	-0.798	-0.860	18.343	-16.852	-16.852	0.000	0.000	0.000	0.000
21	A	25	SER	0	0.030	-0.020	21.446	-0.370	-0.370	0.000	0.000	0.000	0.000
22	A	26	PRO	0	-0.026	0.008	24.028	0.293	0.293	0.000	0.000	0.000	0.000
23	A	27	ASN	0	-0.003	0.014	26.930	0.760	0.760	0.000	0.000	0.000	0.000
24	A	28	HIS	0	0.071	0.016	27.879	-0.147	-0.147	0.000	0.000	0.000	0.000
25	A	29	SER	0	-0.040	-0.028	28.849	-0.098	-0.098	0.000	0.000	0.000	0.000
26	A	30	GLU	-1	-0.769	-0.846	25.436	-12.189	-12.189	0.000	0.000	0.000	0.000
27	A	31	VAL	0	-0.017	-0.004	23.444	-0.548	-0.548	0.000	0.000	0.000	0.000
28	A	32	GLY	0	0.023	0.010	23.341	0.418	0.418	0.000	0.000	0.000	0.000
29	A	33	ILE	0	-0.042	-0.009	24.115	0.233	0.233	0.000	0.000	0.000	0.000
30	A	34	LYS	1	0.859	0.919	19.404	14.130	14.130	0.000	0.000	0.000	0.000
31	A	35	GLY	0	0.030	-0.002	21.473	0.732	0.732	0.000	0.000	0.000	0.000
32	A	36	GLU	-1	-0.866	-0.937	20.146	-14.705	-14.705	0.000	0.000	0.000	0.000
33	A	37	VAL	0	-0.073	-0.030	18.730	0.703	0.703	0.000	0.000	0.000	0.000
34	A	38	VAL	0	0.048	0.016	21.225	-0.278	-0.278	0.000	0.000	0.000	0.000
35	A	39	ASP	-1	-0.817	-0.901	23.903	-11.904	-11.904	0.000	0.000	0.000	0.000
36	A	40	GLU	-1	-0.773	-0.864	17.631	-18.586	-18.586	0.000	0.000	0.000	0.000
37	A	41	THR	0	0.005	0.004	22.158	0.156	0.156	0.000	0.000	0.000	0.000
38	A	42	GLN	0	0.029	0.013	21.195	-0.372	-0.372	0.000	0.000	0.000	0.000
39	A	43	ASN	0	0.004	-0.009	21.290	-0.612	-0.612	0.000	0.000	0.000	0.000
40	A	44	THR	0	0.017	0.027	23.231	0.188	0.188	0.000	0.000	0.000	0.000
41	A	45	LEU	0	-0.005	0.012	17.991	-0.272	-0.272	0.000	0.000	0.000	0.000
42	A	46	LYS	1	0.878	0.922	22.341	11.785	11.785	0.000	0.000	0.000	0.000
43	A	47	ILE	0	-0.014	-0.004	22.063	-0.409	-0.409	0.000	0.000	0.000	0.000
44	A	48	MET	0	0.044	0.024	24.665	0.747	0.747	0.000	0.000	0.000	0.000
45	A	49	THR	0	-0.053	-0.046	25.069	-0.350	-0.350	0.000	0.000	0.000	0.000
46	A	50	GLU	-1	-0.903	-0.968	26.839	-10.783	-10.783	0.000	0.000	0.000	0.000
47	A	51	LYS	1	0.923	0.966	28.838	10.009	10.009	0.000	0.000	0.000	0.000
48	A	52	GLY	0	0.044	0.036	30.820	0.350	0.350	0.000	0.000	0.000	0.000
49	A	53	LEU	0	-0.003	0.021	29.170	-0.431	-0.431	0.000	0.000	0.000	0.000
50	A	54	LYS	1	0.953	0.977	27.091	10.577	10.577	0.000	0.000	0.000	0.000
51	A	55	VAL	0	0.001	0.008	26.717	-0.319	-0.319	0.000	0.000	0.000	0.000
52	A	56	VAL	0	0.010	0.014	23.007	0.220	0.220	0.000	0.000	0.000	0.000
53	A	57	ALA	0	0.012	0.005	23.779	-0.358	-0.358	0.000	0.000	0.000	0.000
54	A	58	LYS	1	0.772	0.866	18.056	16.554	16.554	0.000	0.000	0.000	0.000
55	A	59	ARG	1	0.924	0.952	20.109	12.043	12.043	0.000	0.000	0.000	0.000
56	A	60	GLY	0	0.022	0.011	20.979	0.641	0.641	0.000	0.000	0.000	0.000
57	A	61	ARG	1	0.772	0.869	20.059	13.039	13.039	0.000	0.000	0.000	0.000
58	A	62	THR	0	-0.089	-0.076	15.070	-1.345	-1.345	0.000	0.000	0.000	0.000
59	A	63	PHE	0	0.026	0.013	15.624	1.055	1.055	0.000	0.000	0.000	0.000
60	A	64	ARG	1	0.853	0.905	13.661	15.178	15.178	0.000	0.000	0.000	0.000
61	A	65	VAL	0	0.029	0.018	11.412	1.135	1.135	0.000	0.000	0.000	0.000
62	A	66	TRP	0	0.001	-0.005	11.566	-1.653	-1.653	0.000	0.000	0.000	0.000
63	A	67	TYR	0	-0.030	-0.061	6.902	1.333	1.333	0.000	0.000	0.000	0.000
64	A	68	LYS	1	0.894	0.952	6.822	26.491	26.491	0.000	0.000	0.000	0.000
65	A	69	GLY	0	0.046	0.025	7.471	-2.058	-2.058	0.000	0.000	0.000	0.000
67	A	71	ILE	0	0.050	0.024	8.608	1.150	1.150	0.000	0.000	0.000	0.000
68	A	72	MET	0	-0.051	-0.016	5.651	-1.256	-1.256	0.000	0.000	0.000	0.000
69	A	73	ARG	1	0.910	0.940	9.324	20.682	20.682	0.000	0.000	0.000	0.000
70	A	74	ILE	0	-0.013	-0.006	8.650	-2.326	-2.326	0.000	0.000	0.000	0.000
71	A	75	LYS	1	0.953	0.982	11.983	20.158	20.158	0.000	0.000	0.000	0.000
72	A	76	GLY	0	0.051	0.014	14.307	-0.870	-0.870	0.000	0.000	0.000	0.000
73	A	77	ASP	-1	-0.837	-0.918	16.880	-15.568	-15.568	0.000	0.000	0.000	0.000
74	A	78	LEU	0	-0.036	-0.023	10.415	-0.139	-0.139	0.000	0.000	0.000	0.000
75	A	79	ILE	0	-0.014	0.000	12.716	-0.660	-0.660	0.000	0.000	0.000	0.000
76	A	80	ASN	0	-0.021	0.003	15.261	0.257	0.257	0.000	0.000	0.000	0.000
77	A	81	PHE	0	-0.033	-0.024	16.235	0.887	0.887	0.000	0.000	0.000	0.000
78	A	82	ARG	1	0.985	0.992	19.156	12.295	12.295	0.000	0.000	0.000	0.000
79	A	83	PRO	0	0.066	0.015	17.462	-0.703	-0.703	0.000	0.000	0.000	0.000
80	A	84	GLU	-1	-0.882	-0.939	16.834	-14.686	-14.686	0.000	0.000	0.000	0.000
81	A	85	ASP	-1	-0.841	-0.910	17.634	-17.445	-17.445	0.000	0.000	0.000	0.000
82	A	86	ARG	1	0.830	0.899	12.961	20.208	20.208	0.000	0.000	0.000	0.000
83	A	87	ILE	0	0.046	0.029	12.612	-2.317	-2.317	0.000	0.000	0.000	0.000
84	A	88	LYS	1	0.972	0.992	12.318	14.585	14.585	0.000	0.000	0.000	0.000
85	A	89	ARG	1	0.859	0.922	12.480	17.100	17.100	0.000	0.000	0.000	0.000
86	A	90	GLY	0	0.042	0.019	8.605	-1.871	-1.871	0.000	0.000	0.000	0.000
87	A	91	LEU	0	0.015	0.003	8.073	-3.914	-3.914	0.000	0.000	0.000	0.000
88	A	92	MET	0	-0.011	-0.006	10.010	-0.265	-0.265	0.000	0.000	0.000	0.000
89	A	93	MET	0	-0.022	-0.027	6.967	0.481	0.481	0.000	0.000	0.000	0.000
90	A	94	LEU	0	-0.036	-0.006	5.039	-5.414	-5.414	0.000	0.000	0.000	0.000
91	A	95	LYS	1	0.874	0.923	6.280	19.809	19.809	0.000	0.000	0.000	0.000
92	A	96	ARG	1	0.979	0.985	8.768	24.467	24.467	0.000	0.000	0.000	0.000
95	A	99	GLY	0	0.036	0.037	7.042	2.372	2.372	0.000	0.000	0.000	0.000
96	A	100	VAL	0	-0.056	-0.017	10.145	1.931	1.931	0.000	0.000	0.000	0.000
97	A	101	TRP	0	0.048	0.006	12.194	-0.699	-0.699	0.000	0.000	0.000	0.000
98	A	102	ILE	-1	-0.865	-0.906	13.438	-22.103	-22.103	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:LEU)