FMO DATABASE

FMODB ID: 9LQL2

Calculation Name: 1ECM-A-Xray547

Preferred Name: P-protein

Target Type: SINGLE PROTEIN

Ligand Name: 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid

Ligand 3-letter code: TSA

Ligand of Interest (LOI):

PDB ID: 1ECM

Chain ID: A

ChEMBL ID: CHEMBL3341586

UniProt ID: P0A9J8

Base Structure: X-ray

Registration Date: 2025-09-02

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	91
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-591446.074549
FMO2-HF: Nuclear repulsion	555699.001884
FMO2-HF: Total energy	-35747.072665
FMO2-MP2: Total energy	-35854.707058

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:5:ASN)

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

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.
28.619	32.907	7.062	-3.593	-7.757	0.026

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.909 / q_NPA : 0.936

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	7	LEU	0	0.054	0.024	2.202	0.900	1.847	3.912	-1.698	-3.161	0.014
4	A	8	LEU	0	0.001	-0.007	2.360	-5.708	-2.918	3.149	-1.744	-4.196	0.012
5	A	9	ALA	0	0.064	0.035	3.846	5.073	5.495	0.002	-0.145	-0.279	0.000
6	A	10	LEU	0	-0.036	-0.017	5.300	5.784	5.913	-0.001	-0.006	-0.121	0.000
7	A	11	ARG	1	0.989	0.989	6.306	29.726	29.726	0.000	0.000	0.000	0.000
8	A	12	GLU	-1	-0.907	-0.931	6.613	-38.847	-38.847	0.000	0.000	0.000	0.000
9	A	13	LYS	1	0.923	0.959	9.526	30.255	30.255	0.000	0.000	0.000	0.000
10	A	14	ILE	0	-0.007	0.002	10.757	1.475	1.475	0.000	0.000	0.000	0.000
11	A	15	SER	0	0.017	0.000	11.810	1.492	1.492	0.000	0.000	0.000	0.000
12	A	16	ALA	0	0.047	0.024	13.799	1.253	1.253	0.000	0.000	0.000	0.000
13	A	17	LEU	0	-0.076	-0.036	15.639	1.115	1.115	0.000	0.000	0.000	0.000
14	A	18	ASP	-1	-0.847	-0.942	16.874	-15.557	-15.557	0.000	0.000	0.000	0.000
15	A	19	GLU	-1	-0.939	-0.973	17.483	-15.777	-15.777	0.000	0.000	0.000	0.000
16	A	20	LYS	1	0.878	0.940	18.405	16.392	16.392	0.000	0.000	0.000	0.000
17	A	21	LEU	0	-0.016	0.001	20.974	0.745	0.745	0.000	0.000	0.000	0.000
18	A	22	LEU	0	0.004	-0.001	22.094	0.648	0.648	0.000	0.000	0.000	0.000
19	A	23	ALA	0	0.004	0.011	24.820	0.535	0.535	0.000	0.000	0.000	0.000
20	A	24	LEU	0	0.015	0.005	25.512	0.459	0.459	0.000	0.000	0.000	0.000
21	A	25	LEU	0	-0.043	-0.021	26.291	0.486	0.486	0.000	0.000	0.000	0.000
22	A	26	ALA	0	-0.020	-0.001	29.380	0.400	0.400	0.000	0.000	0.000	0.000
23	A	27	GLU	-1	-0.850	-0.922	30.892	-9.555	-9.555	0.000	0.000	0.000	0.000
24	A	28	ARG	1	0.904	0.947	32.307	9.284	9.284	0.000	0.000	0.000	0.000
25	A	29	ARG	1	0.823	0.867	32.960	9.478	9.478	0.000	0.000	0.000	0.000
26	A	30	GLU	-1	-0.918	-0.952	34.017	-8.789	-8.789	0.000	0.000	0.000	0.000
27	A	31	LEU	0	-0.003	-0.010	35.691	0.329	0.329	0.000	0.000	0.000	0.000
28	A	32	ALA	0	-0.038	-0.014	38.225	0.250	0.250	0.000	0.000	0.000	0.000
29	A	33	VAL	0	0.012	0.004	39.863	0.275	0.275	0.000	0.000	0.000	0.000
30	A	34	GLU	-1	-0.816	-0.884	41.117	-7.092	-7.092	0.000	0.000	0.000	0.000
31	A	35	VAL	0	-0.024	-0.022	42.405	0.237	0.237	0.000	0.000	0.000	0.000
32	A	36	GLY	0	0.042	0.020	43.985	0.182	0.182	0.000	0.000	0.000	0.000
33	A	37	LYS	1	0.834	0.896	43.977	7.378	7.378	0.000	0.000	0.000	0.000
34	A	38	ALA	0	0.002	0.005	47.350	0.181	0.181	0.000	0.000	0.000	0.000
35	A	39	LYS	1	0.780	0.886	44.864	7.110	7.110	0.000	0.000	0.000	0.000
36	A	40	LEU	0	0.051	0.035	49.868	0.144	0.144	0.000	0.000	0.000	0.000
37	A	41	LEU	0	-0.036	-0.020	51.725	0.158	0.158	0.000	0.000	0.000	0.000
38	A	42	SER	0	-0.085	-0.055	52.556	0.154	0.154	0.000	0.000	0.000	0.000
39	A	43	HIS	1	0.879	0.947	54.476	5.745	5.745	0.000	0.000	0.000	0.000
40	A	44	ARG	1	0.965	0.994	50.882	6.205	6.205	0.000	0.000	0.000	0.000
41	A	45	PRO	0	0.041	0.023	50.399	-0.046	-0.046	0.000	0.000	0.000	0.000
42	A	46	VAL	0	0.016	0.009	44.597	-0.070	-0.070	0.000	0.000	0.000	0.000
43	A	47	ARG	1	0.826	0.888	42.166	7.058	7.058	0.000	0.000	0.000	0.000
44	A	48	ASP	-1	-0.865	-0.936	45.021	-6.522	-6.522	0.000	0.000	0.000	0.000
45	A	49	ILE	0	0.028	0.000	44.646	-0.142	-0.142	0.000	0.000	0.000	0.000
46	A	50	ASP	-1	-0.845	-0.903	44.782	-6.500	-6.500	0.000	0.000	0.000	0.000
47	A	51	ARG	1	0.975	0.997	40.306	7.405	7.405	0.000	0.000	0.000	0.000
48	A	52	GLU	-1	-0.832	-0.916	40.641	-7.548	-7.548	0.000	0.000	0.000	0.000
49	A	53	ARG	1	0.886	0.944	40.252	6.413	6.413	0.000	0.000	0.000	0.000
50	A	54	ASP	-1	-0.839	-0.915	41.008	-7.117	-7.117	0.000	0.000	0.000	0.000
51	A	55	LEU	0	-0.139	-0.064	36.033	-0.204	-0.204	0.000	0.000	0.000	0.000
52	A	56	LEU	0	0.028	0.002	35.205	-0.280	-0.280	0.000	0.000	0.000	0.000
53	A	57	GLU	-1	-0.892	-0.939	36.380	-7.505	-7.505	0.000	0.000	0.000	0.000
54	A	58	ARG	1	0.952	0.989	35.589	8.367	8.367	0.000	0.000	0.000	0.000
55	A	59	LEU	0	-0.015	-0.012	32.136	-0.190	-0.190	0.000	0.000	0.000	0.000
56	A	60	ILE	0	0.023	0.017	32.587	-0.339	-0.339	0.000	0.000	0.000	0.000
57	A	61	THR	0	-0.043	-0.032	33.475	-0.136	-0.136	0.000	0.000	0.000	0.000
58	A	62	LEU	0	-0.030	-0.021	32.309	-0.056	-0.056	0.000	0.000	0.000	0.000
59	A	63	GLY	0	0.021	0.012	29.345	-0.280	-0.280	0.000	0.000	0.000	0.000
60	A	64	LYS	1	0.923	0.965	28.877	8.413	8.413	0.000	0.000	0.000	0.000
61	A	65	ALA	0	-0.048	-0.020	30.421	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	66	HIS	0	-0.050	-0.023	25.389	-0.538	-0.538	0.000	0.000	0.000	0.000
63	A	67	HIS	0	-0.026	-0.009	25.002	-0.355	-0.355	0.000	0.000	0.000	0.000
64	A	68	LEU	0	-0.012	0.007	23.341	-0.177	-0.177	0.000	0.000	0.000	0.000
65	A	69	ASP	-1	-0.808	-0.914	26.794	-10.123	-10.123	0.000	0.000	0.000	0.000
66	A	70	ALA	0	0.052	0.003	29.244	-0.040	-0.040	0.000	0.000	0.000	0.000
67	A	71	HIS	0	0.030	0.031	29.874	0.230	0.230	0.000	0.000	0.000	0.000
68	A	72	TYR	0	-0.028	-0.014	22.550	0.088	0.088	0.000	0.000	0.000	0.000
69	A	73	ILE	0	0.005	0.009	28.311	0.026	0.026	0.000	0.000	0.000	0.000
70	A	74	THR	0	-0.017	-0.026	30.184	0.163	0.163	0.000	0.000	0.000	0.000
71	A	75	ARG	1	0.916	0.958	27.299	10.139	10.139	0.000	0.000	0.000	0.000
72	A	76	LEU	0	0.010	0.019	25.751	0.078	0.078	0.000	0.000	0.000	0.000
73	A	77	PHE	0	0.015	-0.016	29.093	0.061	0.061	0.000	0.000	0.000	0.000
74	A	78	GLN	0	0.002	0.002	32.478	0.122	0.122	0.000	0.000	0.000	0.000
75	A	79	LEU	0	0.048	0.039	29.459	0.158	0.158	0.000	0.000	0.000	0.000
76	A	80	ILE	0	0.007	-0.001	28.682	0.134	0.134	0.000	0.000	0.000	0.000
77	A	81	ILE	0	-0.068	-0.033	33.070	0.156	0.156	0.000	0.000	0.000	0.000
78	A	82	GLU	-1	-0.926	-0.961	35.917	-8.133	-8.133	0.000	0.000	0.000	0.000
79	A	83	ASP	-1	-0.761	-0.843	34.023	-8.881	-8.881	0.000	0.000	0.000	0.000
80	A	84	SER	0	-0.015	0.009	36.083	0.186	0.186	0.000	0.000	0.000	0.000
81	A	85	VAL	0	0.001	0.000	38.069	0.211	0.211	0.000	0.000	0.000	0.000
82	A	86	LEU	0	0.019	0.009	37.570	0.215	0.215	0.000	0.000	0.000	0.000
83	A	87	THR	0	-0.025	-0.016	37.615	0.106	0.106	0.000	0.000	0.000	0.000
84	A	88	GLN	0	-0.005	-0.023	40.242	0.316	0.316	0.000	0.000	0.000	0.000
85	A	89	GLN	0	-0.008	-0.019	43.484	0.175	0.175	0.000	0.000	0.000	0.000
86	A	90	ALA	0	0.014	0.018	42.514	0.157	0.157	0.000	0.000	0.000	0.000
87	A	91	LEU	0	-0.011	0.003	44.019	0.121	0.121	0.000	0.000	0.000	0.000
88	A	92	LEU	0	-0.054	-0.030	45.688	0.152	0.152	0.000	0.000	0.000	0.000
89	A	93	GLN	0	-0.017	-0.011	47.530	0.111	0.111	0.000	0.000	0.000	0.000
90	A	94	GLN	0	-0.063	-0.014	46.817	0.033	0.033	0.000	0.000	0.000	0.000
91	A	95	HIS	0	-0.053	-0.020	48.138	0.496	0.496	0.000	0.000	0.000	0.000

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