FMO DATABASE

FMODB ID: 2RN6R

Calculation Name: 3L2A-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3L2A

Chain ID: A

ChEMBL ID:

UniProt ID: Q8JPY0

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1063125.922132
FMO2-HF: Nuclear repulsion	1013826.413464
FMO2-HF: Total energy	-49299.508669
FMO2-MP2: Total energy	-49442.076427

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:204:GLY)

Summations of interaction energy for fragment #1(A:204:GLY)

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.
-22.929	-21.556	0.003	-0.559	-0.817	-0.002

Interaction energy analysis for fragmet #1(A:204:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.891 / q_NPA : 0.932

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	206	PRO	0	0.040	0.015	3.858	1.122	1.892	-0.001	-0.238	-0.531	0.000
46	A	249	HIS	0	-0.031	-0.010	4.168	4.720	4.743	-0.001	-0.009	-0.013	0.000
50	A	253	GLN	0	-0.059	-0.040	3.677	-7.248	-6.668	0.005	-0.312	-0.273	-0.002
4	A	207	TYR	0	0.044	0.044	6.323	5.418	5.418	0.000	0.000	0.000	0.000
5	A	208	ILE	0	-0.081	-0.037	7.024	-1.958	-1.958	0.000	0.000	0.000	0.000
6	A	209	SER	0	0.003	-0.006	9.592	2.932	2.932	0.000	0.000	0.000	0.000
7	A	210	ALA	0	0.054	-0.003	12.516	-0.634	-0.634	0.000	0.000	0.000	0.000
8	A	211	LYS	1	0.833	0.915	15.060	17.954	17.954	0.000	0.000	0.000	0.000
9	A	212	ASP	-1	-0.767	-0.881	9.754	-25.697	-25.697	0.000	0.000	0.000	0.000
10	A	213	LEU	0	0.010	0.006	9.611	-0.897	-0.897	0.000	0.000	0.000	0.000
11	A	214	LYS	1	0.952	0.971	11.486	15.461	15.461	0.000	0.000	0.000	0.000
12	A	215	GLU	-1	-0.914	-0.939	12.891	-18.665	-18.665	0.000	0.000	0.000	0.000
13	A	216	ILE	0	0.041	0.019	6.723	0.028	0.028	0.000	0.000	0.000	0.000
14	A	217	MET	0	-0.041	-0.018	11.035	0.991	0.991	0.000	0.000	0.000	0.000
15	A	218	TYR	0	-0.083	-0.056	13.486	1.781	1.781	0.000	0.000	0.000	0.000
16	A	219	ASP	-1	-0.898	-0.937	12.105	-21.050	-21.050	0.000	0.000	0.000	0.000
17	A	220	HIS	0	-0.020	-0.002	12.324	1.311	1.311	0.000	0.000	0.000	0.000
18	A	221	LEU	0	-0.046	-0.022	16.065	0.796	0.796	0.000	0.000	0.000	0.000
19	A	222	PRO	0	-0.002	0.010	19.041	0.341	0.341	0.000	0.000	0.000	0.000
20	A	223	GLY	0	0.010	-0.002	22.444	0.323	0.323	0.000	0.000	0.000	0.000
21	A	224	PHE	0	0.007	-0.007	23.724	-0.397	-0.397	0.000	0.000	0.000	0.000
22	A	225	GLY	0	0.022	0.004	25.097	0.427	0.427	0.000	0.000	0.000	0.000
23	A	226	THR	0	0.040	-0.003	23.622	0.418	0.418	0.000	0.000	0.000	0.000
24	A	227	ALA	0	0.030	-0.007	25.168	-0.208	-0.208	0.000	0.000	0.000	0.000
25	A	228	PHE	0	0.062	0.031	20.602	-0.132	-0.132	0.000	0.000	0.000	0.000
26	A	229	HIS	0	0.040	0.052	20.478	-0.072	-0.072	0.000	0.000	0.000	0.000
27	A	230	GLN	0	-0.012	-0.009	21.458	-0.542	-0.542	0.000	0.000	0.000	0.000
28	A	231	LEU	0	0.025	0.007	20.188	-0.077	-0.077	0.000	0.000	0.000	0.000
29	A	232	VAL	0	0.046	0.034	16.055	-0.355	-0.355	0.000	0.000	0.000	0.000
30	A	233	GLN	0	-0.059	-0.023	18.137	-0.587	-0.587	0.000	0.000	0.000	0.000
31	A	234	VAL	0	-0.018	-0.007	20.614	-0.071	-0.071	0.000	0.000	0.000	0.000
32	A	235	ILE	0	0.027	0.014	15.839	0.026	0.026	0.000	0.000	0.000	0.000
33	A	236	CYS	0	-0.006	-0.001	15.551	-0.803	-0.803	0.000	0.000	0.000	0.000
34	A	237	LYS	1	0.823	0.899	17.116	12.290	12.290	0.000	0.000	0.000	0.000
35	A	238	ILE	0	0.017	0.012	20.498	0.091	0.091	0.000	0.000	0.000	0.000
36	A	239	GLY	0	0.086	0.031	16.468	0.045	0.045	0.000	0.000	0.000	0.000
37	A	240	LYS	1	0.909	0.952	17.263	14.420	14.420	0.000	0.000	0.000	0.000
38	A	241	ASP	-1	-0.893	-0.936	18.206	-13.338	-13.338	0.000	0.000	0.000	0.000
39	A	242	ASN	0	-0.036	-0.026	20.378	0.889	0.889	0.000	0.000	0.000	0.000
40	A	243	ASN	0	-0.054	-0.022	17.370	-0.383	-0.383	0.000	0.000	0.000	0.000
41	A	244	LEU	0	0.049	0.022	15.561	-0.752	-0.752	0.000	0.000	0.000	0.000
42	A	245	LEU	0	-0.037	-0.014	12.264	-0.588	-0.588	0.000	0.000	0.000	0.000
43	A	246	ASP	-1	-0.775	-0.904	8.985	-31.685	-31.685	0.000	0.000	0.000	0.000
44	A	247	THR	0	0.004	0.007	9.536	-2.236	-2.236	0.000	0.000	0.000	0.000
45	A	248	ILE	0	-0.005	0.007	11.964	-0.074	-0.074	0.000	0.000	0.000	0.000
47	A	250	ALA	0	0.002	0.006	7.558	-1.674	-1.674	0.000	0.000	0.000	0.000
48	A	251	GLU	-1	-0.805	-0.912	8.546	-20.346	-20.346	0.000	0.000	0.000	0.000
49	A	252	PHE	0	-0.045	-0.005	9.386	1.477	1.477	0.000	0.000	0.000	0.000
51	A	254	ALA	0	0.012	0.012	8.202	0.575	0.575	0.000	0.000	0.000	0.000
52	A	255	SER	0	0.003	-0.012	10.998	1.530	1.530	0.000	0.000	0.000	0.000
53	A	256	LEU	0	-0.058	-0.034	9.954	0.989	0.989	0.000	0.000	0.000	0.000
54	A	257	ALA	0	-0.066	-0.022	10.137	0.363	0.363	0.000	0.000	0.000	0.000
55	A	258	ASP	-1	-0.908	-0.951	12.147	-18.682	-18.682	0.000	0.000	0.000	0.000
56	A	259	GLY	0	-0.033	-0.006	15.043	1.227	1.227	0.000	0.000	0.000	0.000
57	A	260	ASP	-1	-0.870	-0.936	16.050	-15.552	-15.552	0.000	0.000	0.000	0.000
58	A	261	SER	0	0.003	-0.007	16.077	-0.835	-0.835	0.000	0.000	0.000	0.000
59	A	262	PRO	0	0.059	0.017	14.947	-0.053	-0.053	0.000	0.000	0.000	0.000
60	A	263	GLN	0	-0.004	-0.012	16.300	-0.368	-0.368	0.000	0.000	0.000	0.000
61	A	264	CYS	0	-0.061	-0.015	19.048	0.512	0.512	0.000	0.000	0.000	0.000
62	A	265	ALA	0	0.102	0.040	14.059	0.227	0.227	0.000	0.000	0.000	0.000
63	A	266	LEU	0	-0.029	-0.019	15.703	-0.014	-0.014	0.000	0.000	0.000	0.000
64	A	267	ILE	0	0.000	-0.003	17.607	0.431	0.431	0.000	0.000	0.000	0.000
65	A	268	GLN	0	0.018	0.026	17.350	1.104	1.104	0.000	0.000	0.000	0.000
66	A	269	ILE	0	0.032	0.013	13.293	0.270	0.270	0.000	0.000	0.000	0.000
67	A	270	THR	0	-0.110	-0.071	17.124	0.569	0.569	0.000	0.000	0.000	0.000
68	A	271	LYS	1	0.887	0.930	20.639	13.718	13.718	0.000	0.000	0.000	0.000
69	A	272	ARG	1	0.856	0.957	15.247	18.793	18.793	0.000	0.000	0.000	0.000
70	A	273	VAL	0	0.003	0.000	15.747	-0.057	-0.057	0.000	0.000	0.000	0.000
71	A	274	PRO	0	0.066	0.021	18.944	0.350	0.350	0.000	0.000	0.000	0.000
72	A	275	ILE	0	0.053	0.041	19.663	0.506	0.506	0.000	0.000	0.000	0.000
73	A	276	PHE	0	-0.042	-0.025	17.848	0.516	0.516	0.000	0.000	0.000	0.000
74	A	277	GLN	0	-0.079	-0.043	23.373	0.275	0.275	0.000	0.000	0.000	0.000
75	A	278	ASP	-1	-0.891	-0.947	25.078	-11.662	-11.662	0.000	0.000	0.000	0.000
76	A	279	VAL	0	-0.037	-0.009	24.861	0.480	0.480	0.000	0.000	0.000	0.000
77	A	280	PRO	0	-0.059	-0.033	27.333	0.024	0.024	0.000	0.000	0.000	0.000
78	A	281	PRO	0	0.019	0.003	27.382	-0.262	-0.262	0.000	0.000	0.000	0.000
79	A	282	PRO	0	-0.009	0.011	25.801	0.398	0.398	0.000	0.000	0.000	0.000
80	A	283	ILE	0	-0.010	-0.012	28.973	0.104	0.104	0.000	0.000	0.000	0.000
81	A	284	ILE	0	-0.013	-0.004	27.956	-0.161	-0.161	0.000	0.000	0.000	0.000
82	A	285	HIS	0	0.026	0.008	32.336	0.052	0.052	0.000	0.000	0.000	0.000
83	A	286	ILE	0	-0.042	-0.021	34.518	-0.137	-0.137	0.000	0.000	0.000	0.000
84	A	287	ARG	1	0.924	0.948	37.195	8.004	8.004	0.000	0.000	0.000	0.000
85	A	288	SER	0	-0.046	-0.051	39.364	0.258	0.258	0.000	0.000	0.000	0.000
86	A	289	ARG	1	0.980	0.975	37.843	7.905	7.905	0.000	0.000	0.000	0.000
87	A	290	GLY	0	-0.024	-0.008	37.653	-0.178	-0.178	0.000	0.000	0.000	0.000
88	A	291	ASP	-1	-0.776	-0.848	35.563	-8.311	-8.311	0.000	0.000	0.000	0.000
89	A	292	ILE	0	-0.016	0.011	32.257	-0.308	-0.308	0.000	0.000	0.000	0.000
90	A	293	PRO	0	0.049	0.026	28.945	0.222	0.222	0.000	0.000	0.000	0.000
91	A	294	ARG	1	0.983	0.978	31.691	8.446	8.446	0.000	0.000	0.000	0.000
92	A	295	ALA	0	0.026	0.014	28.682	0.226	0.226	0.000	0.000	0.000	0.000
93	A	296	CYS	0	-0.002	0.004	28.470	-0.281	-0.281	0.000	0.000	0.000	0.000
94	A	297	GLN	0	-0.080	-0.039	30.679	0.386	0.386	0.000	0.000	0.000	0.000
95	A	298	LYS	1	0.925	0.946	33.637	8.444	8.444	0.000	0.000	0.000	0.000
96	A	299	SER	0	0.044	0.046	30.191	0.046	0.046	0.000	0.000	0.000	0.000
97	A	300	LEU	0	-0.030	0.003	32.182	-0.112	-0.112	0.000	0.000	0.000	0.000
98	A	301	ARG	1	0.947	0.969	34.773	8.308	8.308	0.000	0.000	0.000	0.000
99	A	302	PRO	0	0.016	-0.006	36.749	-0.118	-0.118	0.000	0.000	0.000	0.000
100	A	303	ALA	0	0.013	0.016	36.236	-0.107	-0.107	0.000	0.000	0.000	0.000
101	A	304	PRO	0	-0.012	0.008	35.462	0.235	0.235	0.000	0.000	0.000	0.000
102	A	305	PRO	0	0.046	0.011	37.499	-0.131	-0.131	0.000	0.000	0.000	0.000
103	A	306	SER	0	-0.028	-0.023	35.516	-0.016	-0.016	0.000	0.000	0.000	0.000
104	A	307	PRO	0	-0.046	0.010	31.934	-0.101	-0.101	0.000	0.000	0.000	0.000
105	A	308	LYS	1	0.902	0.945	28.971	10.424	10.424	0.000	0.000	0.000	0.000
106	A	309	ILE	0	0.054	0.015	23.309	0.090	0.090	0.000	0.000	0.000	0.000
107	A	310	ASP	-1	-0.784	-0.881	24.397	-11.386	-11.386	0.000	0.000	0.000	0.000
108	A	311	ARG	1	0.860	0.940	25.417	9.694	9.694	0.000	0.000	0.000	0.000
109	A	312	GLY	0	0.046	0.023	25.951	0.358	0.358	0.000	0.000	0.000	0.000
110	A	313	TRP	0	-0.060	-0.035	27.024	0.282	0.282	0.000	0.000	0.000	0.000
111	A	314	VAL	0	0.028	0.022	24.338	-0.221	-0.221	0.000	0.000	0.000	0.000
112	A	315	CYS	0	0.017	-0.004	26.299	-0.289	-0.289	0.000	0.000	0.000	0.000
113	A	316	LEU	0	-0.031	-0.014	28.855	0.323	0.323	0.000	0.000	0.000	0.000
114	A	317	PHE	0	0.065	0.021	29.954	-0.019	-0.019	0.000	0.000	0.000	0.000
115	A	318	LYS	1	0.922	0.975	34.383	8.001	8.001	0.000	0.000	0.000	0.000
116	A	319	MET	0	-0.014	-0.006	37.583	-0.060	-0.060	0.000	0.000	0.000	0.000
117	A	320	GLN	0	0.031	0.004	40.520	0.046	0.046	0.000	0.000	0.000	0.000
118	A	321	ASP	-1	-0.857	-0.926	43.692	-7.022	-7.022	0.000	0.000	0.000	0.000
119	A	322	GLY	0	-0.006	0.002	43.435	0.104	0.104	0.000	0.000	0.000	0.000
120	A	323	LYS	1	0.909	0.969	42.361	6.707	6.707	0.000	0.000	0.000	0.000
121	A	324	THR	0	-0.011	-0.032	36.316	-0.165	-0.165	0.000	0.000	0.000	0.000
122	A	325	LEU	0	-0.040	-0.005	36.289	0.104	0.104	0.000	0.000	0.000	0.000
123	A	326	GLY	0	0.021	0.011	33.143	-0.223	-0.223	0.000	0.000	0.000	0.000
124	A	327	LEU	0	-0.051	-0.032	27.498	0.173	0.173	0.000	0.000	0.000	0.000
125	A	328	LYS	1	0.806	0.897	29.702	10.003	10.003	0.000	0.000	0.000	0.000
126	A	329	ILE	-1	-0.842	-0.906	23.692	-10.692	-10.692	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:204:GLY)