FMO DATABASE

FMODB ID: 2GQQR

Calculation Name: 1L3A-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1L3A

Chain ID: A

ChEMBL ID:

UniProt ID: Q9LL85

Base Structure: X-ray

Registration Date: 2025-10-11

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1536063.291788
FMO2-HF: Nuclear repulsion	1471873.988964
FMO2-HF: Total energy	-64189.302824
FMO2-MP2: Total energy	-64378.416831

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:89:THR)

Summations of interaction energy for fragment #1(A:89:THR)

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.
37.296	39.279	0.095	-0.956	-1.122	-0.005

Interaction energy analysis for fragmet #1(A:89:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.876 / q_NPA : 0.928

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	91	LYS	1	0.915	0.965	3.120	26.701	28.575	0.096	-0.949	-1.021	-0.005
4	A	92	VAL	0	0.040	0.021	4.588	3.795	3.904	-0.001	-0.007	-0.101	0.000
5	A	93	PHE	0	-0.010	-0.013	7.130	0.024	0.024	0.000	0.000	0.000	0.000
6	A	94	VAL	0	0.023	0.012	10.036	0.459	0.459	0.000	0.000	0.000	0.000
7	A	95	GLY	0	0.080	0.017	12.670	0.154	0.154	0.000	0.000	0.000	0.000
8	A	96	TYR	0	-0.022	0.015	16.201	0.527	0.527	0.000	0.000	0.000	0.000
9	A	97	SER	0	0.013	0.006	18.864	0.277	0.277	0.000	0.000	0.000	0.000
10	A	98	ILE	0	-0.012	0.016	22.084	0.230	0.230	0.000	0.000	0.000	0.000
11	A	99	TYR	0	0.040	0.012	22.776	-0.019	-0.019	0.000	0.000	0.000	0.000
12	A	100	LYS	1	0.808	0.884	28.378	10.301	10.301	0.000	0.000	0.000	0.000
13	A	101	GLY	0	-0.029	-0.011	32.128	-0.008	-0.008	0.000	0.000	0.000	0.000
14	A	102	LYS	1	0.951	0.977	35.032	8.296	8.296	0.000	0.000	0.000	0.000
15	A	103	ALA	0	0.032	0.020	30.847	0.033	0.033	0.000	0.000	0.000	0.000
16	A	104	ALA	0	-0.015	0.004	26.430	0.026	0.026	0.000	0.000	0.000	0.000
17	A	105	LEU	0	-0.012	-0.009	24.287	0.106	0.106	0.000	0.000	0.000	0.000
18	A	106	THR	0	-0.004	-0.001	19.129	0.029	0.029	0.000	0.000	0.000	0.000
19	A	107	VAL	0	-0.011	-0.010	18.655	0.214	0.214	0.000	0.000	0.000	0.000
20	A	108	GLU	-1	-0.886	-0.947	14.716	-18.632	-18.632	0.000	0.000	0.000	0.000
21	A	109	PRO	0	-0.022	0.002	11.385	0.812	0.812	0.000	0.000	0.000	0.000
22	A	110	ARG	1	0.867	0.897	12.384	16.067	16.067	0.000	0.000	0.000	0.000
23	A	111	SER	0	-0.009	-0.031	10.119	-0.261	-0.261	0.000	0.000	0.000	0.000
24	A	112	PRO	0	0.008	0.016	11.549	1.081	1.081	0.000	0.000	0.000	0.000
25	A	113	GLU	-1	-0.887	-0.891	13.164	-17.150	-17.150	0.000	0.000	0.000	0.000
26	A	114	PHE	0	0.056	0.012	11.836	0.420	0.420	0.000	0.000	0.000	0.000
27	A	115	SER	0	0.001	0.006	16.182	0.315	0.315	0.000	0.000	0.000	0.000
28	A	116	PRO	0	0.025	0.014	17.602	-0.346	-0.346	0.000	0.000	0.000	0.000
29	A	117	LEU	0	-0.037	-0.032	18.638	0.734	0.734	0.000	0.000	0.000	0.000
30	A	118	ASP	-1	-0.849	-0.923	21.431	-12.399	-12.399	0.000	0.000	0.000	0.000
31	A	119	SER	0	-0.030	-0.014	22.008	-0.292	-0.292	0.000	0.000	0.000	0.000
32	A	120	GLY	0	-0.013	-0.001	18.450	-0.137	-0.137	0.000	0.000	0.000	0.000
33	A	121	ALA	0	-0.003	0.015	17.683	-0.820	-0.820	0.000	0.000	0.000	0.000
34	A	122	PHE	0	-0.004	-0.020	14.478	-0.464	-0.464	0.000	0.000	0.000	0.000
35	A	123	LYS	1	0.923	0.968	17.869	14.336	14.336	0.000	0.000	0.000	0.000
36	A	124	LEU	0	-0.024	0.007	15.873	-0.419	-0.419	0.000	0.000	0.000	0.000
37	A	125	SER	0	-0.077	-0.080	18.158	0.639	0.639	0.000	0.000	0.000	0.000
38	A	126	ARG	1	0.833	0.910	18.256	15.221	15.221	0.000	0.000	0.000	0.000
39	A	127	GLU	-1	-0.844	-0.919	17.355	-14.350	-14.350	0.000	0.000	0.000	0.000
40	A	128	GLY	0	-0.025	-0.017	15.003	-0.284	-0.284	0.000	0.000	0.000	0.000
41	A	129	MET	0	0.011	0.024	15.853	1.058	1.058	0.000	0.000	0.000	0.000
42	A	130	VAL	0	0.022	0.025	16.490	-0.988	-0.988	0.000	0.000	0.000	0.000
43	A	131	MET	0	-0.074	-0.022	17.119	1.041	1.041	0.000	0.000	0.000	0.000
44	A	132	LEU	0	0.027	0.020	19.397	-0.237	-0.237	0.000	0.000	0.000	0.000
45	A	133	GLN	0	-0.013	-0.016	18.862	0.728	0.728	0.000	0.000	0.000	0.000
46	A	134	PHE	0	0.063	0.028	23.645	-0.082	-0.082	0.000	0.000	0.000	0.000
47	A	135	ALA	0	0.025	0.011	26.848	0.120	0.120	0.000	0.000	0.000	0.000
48	A	136	PRO	0	0.066	0.026	28.662	0.065	0.065	0.000	0.000	0.000	0.000
49	A	137	ALA	0	-0.030	-0.016	31.854	-0.218	-0.218	0.000	0.000	0.000	0.000
50	A	138	ALA	0	0.001	0.002	33.505	0.224	0.224	0.000	0.000	0.000	0.000
51	A	139	GLY	0	0.025	0.017	35.173	0.237	0.237	0.000	0.000	0.000	0.000
52	A	140	VAL	0	-0.019	-0.030	34.221	-0.240	-0.240	0.000	0.000	0.000	0.000
53	A	141	ARG	1	0.944	0.975	32.797	8.518	8.518	0.000	0.000	0.000	0.000
54	A	142	GLN	0	0.035	0.041	29.656	-0.403	-0.403	0.000	0.000	0.000	0.000
55	A	143	TYR	0	-0.017	-0.039	28.008	0.152	0.152	0.000	0.000	0.000	0.000
56	A	144	ASP	-1	-0.785	-0.883	28.886	-10.136	-10.136	0.000	0.000	0.000	0.000
57	A	145	TRP	0	-0.022	-0.032	23.831	-0.078	-0.078	0.000	0.000	0.000	0.000
58	A	146	SER	0	-0.031	-0.001	26.552	-0.388	-0.388	0.000	0.000	0.000	0.000
59	A	147	ARG	1	0.854	0.911	29.033	9.232	9.232	0.000	0.000	0.000	0.000
60	A	148	LYS	1	0.888	0.962	22.026	13.718	13.718	0.000	0.000	0.000	0.000
61	A	149	GLN	0	0.033	0.016	28.263	-0.226	-0.226	0.000	0.000	0.000	0.000
62	A	150	VAL	0	-0.004	-0.002	23.000	-0.205	-0.205	0.000	0.000	0.000	0.000
63	A	151	PHE	0	0.021	-0.002	24.148	0.377	0.377	0.000	0.000	0.000	0.000
64	A	152	SER	0	-0.003	-0.013	21.286	-0.358	-0.358	0.000	0.000	0.000	0.000
65	A	153	LEU	0	-0.013	0.002	21.676	0.595	0.595	0.000	0.000	0.000	0.000
66	A	154	SER	0	0.006	-0.027	21.012	-0.679	-0.679	0.000	0.000	0.000	0.000
67	A	155	VAL	0	0.092	0.037	19.738	0.168	0.168	0.000	0.000	0.000	0.000
68	A	156	THR	0	0.033	0.013	22.184	0.269	0.269	0.000	0.000	0.000	0.000
69	A	157	GLU	-1	-0.797	-0.864	25.139	-10.943	-10.943	0.000	0.000	0.000	0.000
70	A	158	ILE	0	-0.008	-0.013	19.246	0.148	0.148	0.000	0.000	0.000	0.000
71	A	159	GLY	0	0.038	0.010	23.523	0.115	0.115	0.000	0.000	0.000	0.000
72	A	160	SER	0	-0.017	0.008	25.744	0.419	0.419	0.000	0.000	0.000	0.000
73	A	161	ILE	0	-0.033	-0.016	25.226	0.213	0.213	0.000	0.000	0.000	0.000
74	A	162	ILE	0	-0.080	-0.044	23.029	0.128	0.128	0.000	0.000	0.000	0.000
75	A	163	SER	0	-0.050	-0.031	26.373	0.200	0.200	0.000	0.000	0.000	0.000
76	A	164	LEU	0	-0.026	0.010	29.838	0.326	0.326	0.000	0.000	0.000	0.000
77	A	165	GLY	0	0.080	0.044	31.843	-0.118	-0.118	0.000	0.000	0.000	0.000
78	A	166	THR	0	-0.079	-0.068	34.550	-0.021	-0.021	0.000	0.000	0.000	0.000
79	A	167	LYS	1	0.939	0.956	36.432	7.573	7.573	0.000	0.000	0.000	0.000
80	A	168	ASP	-1	-0.867	-0.894	35.207	-8.094	-8.094	0.000	0.000	0.000	0.000
81	A	169	SER	0	0.020	-0.014	35.393	-0.073	-0.073	0.000	0.000	0.000	0.000
82	A	170	CYS	0	-0.038	-0.004	31.369	-0.049	-0.049	0.000	0.000	0.000	0.000
83	A	171	GLU	-1	-0.869	-0.936	33.501	-8.184	-8.184	0.000	0.000	0.000	0.000
84	A	172	PHE	0	-0.012	-0.004	29.019	-0.036	-0.036	0.000	0.000	0.000	0.000
85	A	173	PHE	0	0.030	0.011	31.707	-0.090	-0.090	0.000	0.000	0.000	0.000
86	A	174	HIS	1	0.776	0.870	26.388	10.732	10.732	0.000	0.000	0.000	0.000
87	A	175	ASP	-1	-0.772	-0.902	31.342	-8.598	-8.598	0.000	0.000	0.000	0.000
88	A	176	PRO	0	-0.029	-0.017	30.437	-0.125	-0.125	0.000	0.000	0.000	0.000
89	A	177	ASN	0	-0.124	-0.044	32.058	-0.259	-0.259	0.000	0.000	0.000	0.000
90	A	178	LYS	1	0.987	0.999	31.991	9.512	9.512	0.000	0.000	0.000	0.000
91	A	179	GLY	0	0.081	0.044	35.669	0.061	0.061	0.000	0.000	0.000	0.000
92	A	180	ARG	1	0.851	0.916	35.503	8.544	8.544	0.000	0.000	0.000	0.000
93	A	181	SER	0	-0.006	0.002	36.257	0.048	0.048	0.000	0.000	0.000	0.000
94	A	182	ASP	-1	-0.822	-0.915	39.083	-7.752	-7.752	0.000	0.000	0.000	0.000
95	A	183	GLU	-1	-0.913	-0.963	39.792	-7.383	-7.383	0.000	0.000	0.000	0.000
96	A	184	GLY	0	0.007	0.018	38.441	-0.131	-0.131	0.000	0.000	0.000	0.000
97	A	185	ARG	1	0.897	0.937	38.511	7.468	7.468	0.000	0.000	0.000	0.000
98	A	186	VAL	0	-0.034	-0.013	33.471	0.038	0.038	0.000	0.000	0.000	0.000
99	A	187	ARG	1	0.934	0.963	34.213	7.824	7.824	0.000	0.000	0.000	0.000
100	A	188	LYS	1	0.859	0.930	27.472	10.911	10.911	0.000	0.000	0.000	0.000
101	A	189	VAL	0	0.009	-0.001	32.462	-0.028	-0.028	0.000	0.000	0.000	0.000
102	A	190	LEU	0	-0.025	0.013	27.229	-0.041	-0.041	0.000	0.000	0.000	0.000
103	A	191	LYS	1	0.840	0.924	31.310	8.044	8.044	0.000	0.000	0.000	0.000
104	A	192	VAL	0	-0.012	-0.013	29.387	-0.146	-0.146	0.000	0.000	0.000	0.000
105	A	193	GLU	-1	-0.813	-0.916	32.841	-7.855	-7.855	0.000	0.000	0.000	0.000
106	A	194	PRO	0	0.004	0.010	35.554	-0.157	-0.157	0.000	0.000	0.000	0.000
107	A	195	LEU	0	-0.057	-0.026	34.844	0.124	0.124	0.000	0.000	0.000	0.000
108	A	196	PRO	0	-0.001	-0.013	38.418	0.085	0.085	0.000	0.000	0.000	0.000
109	A	197	ASP	-1	-0.839	-0.890	39.900	-7.678	-7.678	0.000	0.000	0.000	0.000
110	A	198	GLY	0	-0.032	-0.011	39.447	0.035	0.035	0.000	0.000	0.000	0.000
111	A	199	SER	0	-0.074	-0.061	36.791	-0.210	-0.210	0.000	0.000	0.000	0.000
112	A	200	GLY	0	-0.021	-0.028	33.701	-0.319	-0.319	0.000	0.000	0.000	0.000
113	A	201	HIS	0	0.016	0.031	31.863	0.155	0.155	0.000	0.000	0.000	0.000
114	A	202	PHE	0	-0.040	-0.015	33.052	-0.171	-0.171	0.000	0.000	0.000	0.000
115	A	203	PHE	0	0.021	0.006	26.524	-0.090	-0.090	0.000	0.000	0.000	0.000
116	A	204	ASN	0	0.003	-0.015	31.298	0.148	0.148	0.000	0.000	0.000	0.000
117	A	205	LEU	0	-0.026	0.001	28.101	-0.048	-0.048	0.000	0.000	0.000	0.000
118	A	206	SER	0	0.018	0.002	31.952	0.108	0.108	0.000	0.000	0.000	0.000
119	A	207	VAL	0	-0.065	-0.047	31.093	-0.262	-0.262	0.000	0.000	0.000	0.000
120	A	208	GLN	0	0.034	0.026	34.304	0.146	0.146	0.000	0.000	0.000	0.000
121	A	209	ASN	0	-0.021	-0.022	35.360	-0.032	-0.032	0.000	0.000	0.000	0.000
122	A	210	LYS	1	0.935	0.963	38.000	7.673	7.673	0.000	0.000	0.000	0.000
123	A	211	LEU	0	-0.011	0.005	36.677	0.139	0.139	0.000	0.000	0.000	0.000
124	A	212	ILE	0	-0.003	-0.004	36.882	0.059	0.059	0.000	0.000	0.000	0.000
125	A	213	ASN	0	-0.047	-0.021	40.081	0.139	0.139	0.000	0.000	0.000	0.000
126	A	214	LEU	0	-0.014	0.013	34.407	0.022	0.022	0.000	0.000	0.000	0.000
127	A	215	ASP	-1	-0.900	-0.967	38.847	-7.692	-7.692	0.000	0.000	0.000	0.000
128	A	216	GLU	-1	-0.850	-0.918	35.124	-8.596	-8.596	0.000	0.000	0.000	0.000
129	A	217	ASN	0	-0.039	-0.023	35.568	-0.123	-0.123	0.000	0.000	0.000	0.000
130	A	218	ILE	0	0.010	0.024	31.067	0.085	0.085	0.000	0.000	0.000	0.000
131	A	219	TYR	0	0.021	0.011	32.899	-0.171	-0.171	0.000	0.000	0.000	0.000
132	A	220	ILE	0	-0.032	-0.025	28.361	0.014	0.014	0.000	0.000	0.000	0.000
133	A	221	PRO	0	-0.001	0.016	32.192	-0.031	-0.031	0.000	0.000	0.000	0.000
134	A	222	VAL	0	-0.033	-0.024	27.727	-0.264	-0.264	0.000	0.000	0.000	0.000
135	A	223	THR	0	0.040	-0.012	30.515	0.149	0.149	0.000	0.000	0.000	0.000
136	A	224	LYS	1	1.015	0.982	30.118	8.475	8.475	0.000	0.000	0.000	0.000
137	A	225	ALA	0	-0.016	0.003	28.979	-0.197	-0.197	0.000	0.000	0.000	0.000
138	A	226	GLU	-1	-0.748	-0.831	26.026	-10.751	-10.751	0.000	0.000	0.000	0.000
139	A	227	PHE	0	0.030	0.011	25.284	-0.537	-0.537	0.000	0.000	0.000	0.000
140	A	228	ALA	0	0.016	0.014	25.865	-0.292	-0.292	0.000	0.000	0.000	0.000
141	A	229	VAL	0	-0.023	-0.006	20.980	-0.440	-0.440	0.000	0.000	0.000	0.000
142	A	230	LEU	0	-0.004	-0.005	21.280	-0.686	-0.686	0.000	0.000	0.000	0.000
143	A	231	VAL	0	0.035	0.017	21.456	-0.535	-0.535	0.000	0.000	0.000	0.000
144	A	232	SER	0	-0.014	0.009	20.909	-0.394	-0.394	0.000	0.000	0.000	0.000
145	A	233	ALA	0	0.013	-0.002	17.167	-0.581	-0.581	0.000	0.000	0.000	0.000
146	A	234	PHE	0	-0.015	-0.023	17.166	-0.828	-0.828	0.000	0.000	0.000	0.000
147	A	235	ASN	0	0.004	-0.014	19.028	-0.193	-0.193	0.000	0.000	0.000	0.000
148	A	236	PHE	0	-0.017	0.005	11.279	-0.305	-0.305	0.000	0.000	0.000	0.000
149	A	237	VAL	0	0.004	-0.013	12.718	-0.878	-0.878	0.000	0.000	0.000	0.000
150	A	238	MET	0	0.011	0.021	15.024	-0.723	-0.723	0.000	0.000	0.000	0.000
151	A	239	PRO	0	0.030	0.017	15.518	-0.060	-0.060	0.000	0.000	0.000	0.000
152	A	240	TYR	0	-0.022	-0.015	10.020	-1.234	-1.234	0.000	0.000	0.000	0.000
153	A	241	LEU	0	-0.097	-0.038	13.195	-0.692	-0.692	0.000	0.000	0.000	0.000
154	A	242	LEU	0	0.064	0.030	15.314	0.196	0.196	0.000	0.000	0.000	0.000
155	A	243	GLY	0	0.009	0.003	13.646	0.292	0.292	0.000	0.000	0.000	0.000
156	A	244	TRP	0	0.014	0.014	14.680	-0.406	-0.406	0.000	0.000	0.000	0.000
157	A	245	HIS	0	0.017	0.019	9.049	1.695	1.695	0.000	0.000	0.000	0.000
158	A	246	THR	0	-0.070	-0.054	11.048	-0.313	-0.313	0.000	0.000	0.000	0.000
159	A	247	ALA	0	0.045	0.036	13.246	0.211	0.211	0.000	0.000	0.000	0.000
160	A	248	VAL	0	0.026	0.020	14.978	0.252	0.252	0.000	0.000	0.000	0.000
161	A	249	ASN	0	-0.052	-0.025	10.287	0.751	0.751	0.000	0.000	0.000	0.000
162	A	250	SER	0	-0.060	-0.043	14.283	-0.029	-0.029	0.000	0.000	0.000	0.000
163	A	251	PHE	0	-0.032	-0.013	17.198	0.759	0.759	0.000	0.000	0.000	0.000
164	A	252	LYS	1	0.881	0.943	14.420	18.834	18.834	0.000	0.000	0.000	0.000
165	A	253	PRO	0	-0.021	-0.014	20.304	0.233	0.233	0.000	0.000	0.000	0.000
166	A	254	GLU	-2	-1.865	-1.915	20.962	-27.423	-27.423	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:89:THR)