FMO DATABASE

FMODB ID: LGQL9

Calculation Name: 3R0A-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3R0A

Chain ID: A

ChEMBL ID:

UniProt ID: Q8PXX2

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	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-966850.437243
FMO2-HF: Nuclear repulsion	917866.499261
FMO2-HF: Total energy	-48983.937982
FMO2-MP2: Total energy	-49126.757333

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:SER)

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

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.
17.124	22.02	11.698	-8.771	-7.823	-0.085

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.840 / q_NPA : 0.897

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	0	ALA	0	0.004	0.009	3.090	4.177	8.283	0.037	-2.078	-2.066	-0.007
4	A	1	MET	0	0.003	0.018	4.254	-7.249	-7.038	-0.001	-0.053	-0.157	0.000
14	A	11	VAL	0	0.033	0.016	3.013	-0.661	-0.177	0.039	-0.138	-0.385	-0.001
15	A	12	GLU	-1	-0.821	-0.920	2.017	-99.109	-99.141	11.625	-6.484	-5.110	-0.077
16	A	13	ASP	-1	-0.850	-0.929	4.518	-25.835	-25.765	-0.001	-0.017	-0.051	0.000
18	A	15	ILE	0	0.012	0.005	4.658	2.481	2.538	-0.001	-0.001	-0.054	0.000
5	A	2	ILE	0	-0.034	-0.017	6.984	-1.055	-1.055	0.000	0.000	0.000	0.000
6	A	3	ASP	-1	-0.860	-0.917	9.106	-20.516	-20.516	0.000	0.000	0.000	0.000
7	A	4	PHE	0	-0.016	-0.024	12.761	-0.135	-0.135	0.000	0.000	0.000	0.000
8	A	5	ALA	0	0.001	-0.004	14.782	0.404	0.404	0.000	0.000	0.000	0.000
9	A	6	CYS	0	0.000	0.005	17.864	0.665	0.665	0.000	0.000	0.000	0.000
10	A	7	LYS	1	0.949	0.978	16.245	15.760	15.760	0.000	0.000	0.000	0.000
11	A	8	GLU	-1	-0.833	-0.922	11.617	-26.190	-26.190	0.000	0.000	0.000	0.000
12	A	9	PHE	0	-0.049	-0.023	9.886	0.476	0.476	0.000	0.000	0.000	0.000
13	A	10	LYS	1	0.968	0.973	5.645	27.816	27.816	0.000	0.000	0.000	0.000
17	A	14	VAL	0	0.051	0.037	7.635	3.311	3.311	0.000	0.000	0.000	0.000
19	A	16	LYS	1	0.821	0.918	8.057	33.464	33.464	0.000	0.000	0.000	0.000
20	A	17	CYS	0	-0.006	0.013	10.335	2.851	2.851	0.000	0.000	0.000	0.000
21	A	18	ALA	0	0.035	0.023	12.056	1.602	1.602	0.000	0.000	0.000	0.000
22	A	19	LEU	0	0.026	-0.006	10.875	1.600	1.600	0.000	0.000	0.000	0.000
23	A	20	ASN	0	-0.016	0.015	13.972	0.954	0.954	0.000	0.000	0.000	0.000
24	A	21	LEU	0	-0.038	-0.004	10.543	0.789	0.789	0.000	0.000	0.000	0.000
25	A	22	THR	0	0.045	0.003	12.679	-0.959	-0.959	0.000	0.000	0.000	0.000
26	A	23	LYS	1	0.969	0.966	10.449	22.709	22.709	0.000	0.000	0.000	0.000
27	A	24	ALA	0	0.019	0.020	11.454	-1.403	-1.403	0.000	0.000	0.000	0.000
28	A	25	ASP	-1	-0.692	-0.826	13.346	-19.687	-19.687	0.000	0.000	0.000	0.000
29	A	26	LEU	0	0.006	0.012	5.883	-0.067	-0.067	0.000	0.000	0.000	0.000
30	A	27	ASN	0	0.003	-0.014	8.615	-5.461	-5.461	0.000	0.000	0.000	0.000
31	A	28	VAL	0	0.026	0.037	10.318	0.137	0.137	0.000	0.000	0.000	0.000
32	A	29	MET	0	0.023	0.013	8.569	0.812	0.812	0.000	0.000	0.000	0.000
33	A	30	LYS	1	0.832	0.905	5.013	47.111	47.111	0.000	0.000	0.000	0.000
34	A	31	SER	0	0.012	-0.010	9.229	0.649	0.649	0.000	0.000	0.000	0.000
35	A	32	PHE	0	-0.018	-0.014	12.356	1.218	1.218	0.000	0.000	0.000	0.000
36	A	33	LEU	0	-0.042	-0.030	8.287	0.474	0.474	0.000	0.000	0.000	0.000
37	A	34	ASN	0	-0.028	-0.013	8.755	-1.734	-1.734	0.000	0.000	0.000	0.000
38	A	35	GLU	-1	-0.863	-0.921	11.264	-16.615	-16.615	0.000	0.000	0.000	0.000
39	A	36	PRO	0	-0.012	-0.005	13.609	0.808	0.808	0.000	0.000	0.000	0.000
40	A	37	ASP	-1	-0.850	-0.940	15.859	-14.603	-14.603	0.000	0.000	0.000	0.000
41	A	38	ARG	1	0.846	0.937	16.173	18.143	18.143	0.000	0.000	0.000	0.000
42	A	39	TRP	0	0.002	0.000	19.983	-0.527	-0.527	0.000	0.000	0.000	0.000
43	A	40	ILE	0	-0.037	-0.021	19.291	0.161	0.161	0.000	0.000	0.000	0.000
44	A	41	ASP	-1	-0.779	-0.888	22.619	-12.469	-12.469	0.000	0.000	0.000	0.000
45	A	42	THR	0	0.022	-0.017	22.359	-0.757	-0.757	0.000	0.000	0.000	0.000
46	A	43	ASP	-1	-0.883	-0.935	22.733	-11.948	-11.948	0.000	0.000	0.000	0.000
47	A	44	ALA	0	-0.004	0.004	23.720	-0.328	-0.328	0.000	0.000	0.000	0.000
48	A	45	LEU	0	-0.010	-0.005	16.316	-0.545	-0.545	0.000	0.000	0.000	0.000
49	A	46	SER	0	-0.067	-0.040	18.980	-0.632	-0.632	0.000	0.000	0.000	0.000
50	A	47	LYS	1	0.983	0.983	20.294	11.432	11.432	0.000	0.000	0.000	0.000
51	A	48	SER	0	0.005	0.009	16.828	-0.005	-0.005	0.000	0.000	0.000	0.000
52	A	49	LEU	0	-0.065	-0.043	14.196	-0.826	-0.826	0.000	0.000	0.000	0.000
53	A	50	LYS	1	0.888	0.963	16.733	16.227	16.227	0.000	0.000	0.000	0.000
54	A	51	LEU	0	-0.032	-0.001	15.217	-0.149	-0.149	0.000	0.000	0.000	0.000
55	A	52	ASP	-1	-0.779	-0.885	19.635	-12.716	-12.716	0.000	0.000	0.000	0.000
56	A	53	VAL	0	0.065	0.023	21.981	-0.665	-0.665	0.000	0.000	0.000	0.000
57	A	54	SER	0	0.020	0.016	23.575	-0.282	-0.282	0.000	0.000	0.000	0.000
58	A	55	THR	0	-0.070	-0.057	18.712	-0.312	-0.312	0.000	0.000	0.000	0.000
59	A	56	VAL	0	-0.003	0.002	18.197	-0.585	-0.585	0.000	0.000	0.000	0.000
60	A	57	GLN	0	0.033	0.027	19.943	-0.296	-0.296	0.000	0.000	0.000	0.000
61	A	58	ARG	1	0.920	0.950	21.220	14.202	14.202	0.000	0.000	0.000	0.000
62	A	59	SER	0	-0.058	-0.044	16.347	-0.214	-0.214	0.000	0.000	0.000	0.000
63	A	60	VAL	0	-0.003	-0.006	18.016	-0.567	-0.567	0.000	0.000	0.000	0.000
64	A	61	LYS	1	0.851	0.926	19.682	12.239	12.239	0.000	0.000	0.000	0.000
65	A	62	LYS	1	0.857	0.916	16.754	17.873	17.873	0.000	0.000	0.000	0.000
66	A	63	LEU	0	-0.014	-0.018	13.670	-0.301	-0.301	0.000	0.000	0.000	0.000
67	A	64	HIS	0	-0.036	-0.017	17.661	0.483	0.483	0.000	0.000	0.000	0.000
68	A	65	GLU	-1	-0.820	-0.903	21.028	-12.663	-12.663	0.000	0.000	0.000	0.000
69	A	66	LYS	1	0.827	0.910	16.891	17.767	17.767	0.000	0.000	0.000	0.000
70	A	67	GLU	-1	-0.925	-0.951	18.571	-13.944	-13.944	0.000	0.000	0.000	0.000
71	A	68	ILE	0	-0.026	-0.010	13.648	-0.678	-0.678	0.000	0.000	0.000	0.000
72	A	69	LEU	0	-0.024	-0.021	16.194	-0.442	-0.442	0.000	0.000	0.000	0.000
73	A	70	GLN	0	0.008	0.021	18.969	0.435	0.435	0.000	0.000	0.000	0.000
74	A	71	ARG	1	0.886	0.946	22.411	11.226	11.226	0.000	0.000	0.000	0.000
75	A	72	SER	0	0.025	0.019	25.034	0.437	0.437	0.000	0.000	0.000	0.000
76	A	73	GLN	0	0.014	-0.008	28.169	-0.415	-0.415	0.000	0.000	0.000	0.000
77	A	74	GLN	0	0.000	0.015	29.091	-0.104	-0.104	0.000	0.000	0.000	0.000
78	A	75	ASN	0	0.006	-0.010	31.623	-0.093	-0.093	0.000	0.000	0.000	0.000
79	A	76	LEU	0	-0.004	-0.010	33.175	-0.160	-0.160	0.000	0.000	0.000	0.000
80	A	77	ASP	-1	-0.875	-0.937	36.941	-7.979	-7.979	0.000	0.000	0.000	0.000
81	A	78	GLY	0	-0.049	-0.019	40.194	0.196	0.196	0.000	0.000	0.000	0.000
82	A	79	GLY	0	-0.004	0.005	41.249	0.073	0.073	0.000	0.000	0.000	0.000
83	A	80	GLY	0	0.003	0.014	37.745	-0.029	-0.029	0.000	0.000	0.000	0.000
84	A	81	TYR	0	-0.045	-0.037	31.617	0.046	0.046	0.000	0.000	0.000	0.000
85	A	82	VAL	0	0.031	0.027	29.080	-0.067	-0.067	0.000	0.000	0.000	0.000
86	A	83	TYR	0	-0.031	-0.026	26.807	-0.031	-0.031	0.000	0.000	0.000	0.000
87	A	84	ILE	0	-0.015	-0.001	25.061	-0.368	-0.368	0.000	0.000	0.000	0.000
88	A	85	TYR	0	-0.009	-0.029	20.767	0.188	0.188	0.000	0.000	0.000	0.000
89	A	86	LYS	1	0.881	0.951	19.540	14.778	14.778	0.000	0.000	0.000	0.000
90	A	87	ILE	0	-0.074	-0.012	13.540	-0.102	-0.102	0.000	0.000	0.000	0.000
91	A	88	TYR	0	0.050	0.026	17.005	0.697	0.697	0.000	0.000	0.000	0.000
92	A	89	SER	0	0.022	0.012	16.438	-0.760	-0.760	0.000	0.000	0.000	0.000
93	A	90	LYS	1	1.007	0.979	12.611	20.307	20.307	0.000	0.000	0.000	0.000
94	A	91	ASN	0	0.018	-0.002	13.825	-2.091	-2.091	0.000	0.000	0.000	0.000
95	A	92	GLN	0	0.006	0.021	16.403	-0.021	-0.021	0.000	0.000	0.000	0.000
96	A	93	ILE	0	0.015	0.001	10.983	-0.230	-0.230	0.000	0.000	0.000	0.000
97	A	94	ARG	1	0.926	0.964	10.843	22.676	22.676	0.000	0.000	0.000	0.000
98	A	95	ASN	0	0.016	0.005	13.259	-0.371	-0.371	0.000	0.000	0.000	0.000
99	A	96	ILE	0	0.029	0.024	15.445	0.385	0.385	0.000	0.000	0.000	0.000
100	A	97	ILE	0	-0.009	-0.009	9.338	0.041	0.041	0.000	0.000	0.000	0.000
101	A	98	GLN	0	0.021	0.011	13.453	-0.903	-0.903	0.000	0.000	0.000	0.000
102	A	99	LYS	1	0.958	0.976	15.222	15.137	15.137	0.000	0.000	0.000	0.000
103	A	100	ILE	0	-0.018	0.014	15.535	0.600	0.600	0.000	0.000	0.000	0.000
104	A	101	VAL	0	0.014	0.014	12.708	0.472	0.472	0.000	0.000	0.000	0.000
105	A	102	GLN	0	-0.089	-0.049	16.072	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	103	SER	0	-0.023	-0.024	19.406	0.668	0.668	0.000	0.000	0.000	0.000
107	A	104	TRP	0	-0.027	-0.031	12.911	-0.073	-0.073	0.000	0.000	0.000	0.000
108	A	105	ALA	0	0.016	0.018	19.618	0.476	0.476	0.000	0.000	0.000	0.000
109	A	106	ASP	-1	-0.817	-0.905	21.268	-12.658	-12.658	0.000	0.000	0.000	0.000
110	A	107	ARG	1	0.935	0.972	22.096	13.754	13.754	0.000	0.000	0.000	0.000
111	A	108	LEU	0	-0.022	-0.009	21.469	0.294	0.294	0.000	0.000	0.000	0.000
112	A	109	GLY	0	0.026	0.010	24.571	0.354	0.354	0.000	0.000	0.000	0.000
113	A	110	GLN	0	-0.086	-0.053	27.112	0.798	0.798	0.000	0.000	0.000	0.000
114	A	111	GLU	-1	-0.870	-0.942	26.855	-10.665	-10.665	0.000	0.000	0.000	0.000
115	A	112	LEU	0	-0.052	-0.024	26.760	0.138	0.138	0.000	0.000	0.000	0.000
116	A	113	LYS	1	0.831	0.916	30.073	10.021	10.021	0.000	0.000	0.000	0.000
117	A	114	GLU	-1	-0.912	-0.943	32.440	-9.221	-9.221	0.000	0.000	0.000	0.000
118	A	115	TRP	0	-0.074	-0.018	31.964	-0.069	-0.069	0.000	0.000	0.000	0.000
119	A	116	GLU	-1	-0.991	-1.012	33.926	-8.224	-8.224	0.000	0.000	0.000	0.000
120	A	117	ASN	-1	-1.001	-0.985	36.723	-8.096	-8.096	0.000	0.000	0.000	0.000

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