FMO DATABASE

FMODB ID: ZLRRN

Calculation Name: 2LJ4-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2LJ4

Chain ID: A

ChEMBL ID:

UniProt ID: Q57YG1

Base Structure: SolutionNMR

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-890728.167051
FMO2-HF: Nuclear repulsion	846512.180143
FMO2-HF: Total energy	-44215.986907
FMO2-MP2: Total energy	-44344.130362

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:4:MET)

Summations of interaction energy for fragment #1(A:4:MET)

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.
-25.219	-23.959	-0.008	-0.511	-0.741	-0.001

Interaction energy analysis for fragmet #1(A:4:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.859 / q_NPA : 0.914

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	6	GLU	-1	-0.816	-0.874	3.852	-35.542	-34.282	-0.008	-0.511	-0.741	-0.001
4	A	7	LYS	1	0.861	0.940	5.953	29.502	29.502	0.000	0.000	0.000	0.000
5	A	8	LEU	0	0.008	0.017	8.351	-2.921	-2.921	0.000	0.000	0.000	0.000
6	A	9	ARG	1	0.834	0.912	11.016	18.616	18.616	0.000	0.000	0.000	0.000
7	A	10	ALA	0	0.037	0.009	14.684	-0.296	-0.296	0.000	0.000	0.000	0.000
8	A	11	ALA	0	0.025	0.021	17.235	0.544	0.544	0.000	0.000	0.000	0.000
9	A	12	HIS	0	-0.063	-0.083	21.030	-0.539	-0.539	0.000	0.000	0.000	0.000
10	A	13	LEU	0	-0.001	0.006	23.064	0.468	0.468	0.000	0.000	0.000	0.000
11	A	14	LEU	0	-0.075	-0.030	26.493	-0.212	-0.212	0.000	0.000	0.000	0.000
12	A	15	VAL	0	0.058	0.019	28.244	0.326	0.326	0.000	0.000	0.000	0.000
13	A	16	LYS	1	0.856	0.933	30.671	9.924	9.924	0.000	0.000	0.000	0.000
14	A	17	PHE	0	0.002	-0.005	32.871	0.072	0.072	0.000	0.000	0.000	0.000
15	A	18	SER	0	0.031	0.012	37.149	-0.103	-0.103	0.000	0.000	0.000	0.000
16	A	19	GLY	0	0.019	0.006	38.829	-0.056	-0.056	0.000	0.000	0.000	0.000
17	A	20	SER	0	-0.020	-0.006	33.427	-0.206	-0.206	0.000	0.000	0.000	0.000
18	A	21	ARG	1	0.890	0.937	28.957	10.066	10.066	0.000	0.000	0.000	0.000
19	A	22	ASN	0	-0.066	-0.056	32.445	0.298	0.298	0.000	0.000	0.000	0.000
20	A	23	PRO	0	0.012	0.024	35.728	-0.156	-0.156	0.000	0.000	0.000	0.000
21	A	24	VAL	0	0.042	0.016	37.052	0.190	0.190	0.000	0.000	0.000	0.000
22	A	25	SER	0	0.028	0.025	35.294	-0.232	-0.232	0.000	0.000	0.000	0.000
23	A	26	ARG	1	0.920	0.948	33.299	9.263	9.263	0.000	0.000	0.000	0.000
24	A	27	ARG	1	0.813	0.888	35.725	8.520	8.520	0.000	0.000	0.000	0.000
25	A	28	THR	0	-0.046	-0.040	37.419	0.215	0.215	0.000	0.000	0.000	0.000
26	A	29	GLY	0	-0.033	0.005	39.328	0.214	0.214	0.000	0.000	0.000	0.000
27	A	30	ASP	-1	-0.913	-0.941	40.662	-7.231	-7.231	0.000	0.000	0.000	0.000
28	A	31	SER	0	0.005	-0.030	41.509	-0.146	-0.146	0.000	0.000	0.000	0.000
29	A	32	THR	0	-0.104	-0.057	37.096	0.102	0.102	0.000	0.000	0.000	0.000
30	A	33	ALA	0	-0.004	-0.025	40.366	-0.124	-0.124	0.000	0.000	0.000	0.000
31	A	34	ASP	-1	-0.882	-0.929	42.674	-6.971	-6.971	0.000	0.000	0.000	0.000
32	A	35	VAL	0	-0.042	0.004	38.379	0.029	0.029	0.000	0.000	0.000	0.000
33	A	36	THR	0	0.039	0.010	40.080	-0.179	-0.179	0.000	0.000	0.000	0.000
34	A	37	TYR	0	0.002	-0.017	34.653	-0.254	-0.254	0.000	0.000	0.000	0.000
35	A	38	GLU	-1	-0.870	-0.930	35.719	-8.133	-8.133	0.000	0.000	0.000	0.000
36	A	39	ASP	-1	-0.860	-0.918	37.730	-7.832	-7.832	0.000	0.000	0.000	0.000
37	A	40	ALA	0	0.026	0.015	34.027	-0.110	-0.110	0.000	0.000	0.000	0.000
38	A	41	ILE	0	-0.001	-0.001	32.263	-0.311	-0.311	0.000	0.000	0.000	0.000
39	A	42	LYS	1	0.926	0.970	33.989	7.531	7.531	0.000	0.000	0.000	0.000
40	A	43	GLU	-1	-0.811	-0.873	34.931	-8.743	-8.743	0.000	0.000	0.000	0.000
41	A	44	LEU	0	0.000	-0.006	27.987	-0.088	-0.088	0.000	0.000	0.000	0.000
42	A	45	GLN	0	0.036	0.005	30.377	-0.616	-0.616	0.000	0.000	0.000	0.000
43	A	46	LYS	1	0.901	0.969	32.334	8.341	8.341	0.000	0.000	0.000	0.000
44	A	47	TRP	0	0.010	-0.016	31.077	0.028	0.028	0.000	0.000	0.000	0.000
45	A	48	SER	0	0.030	0.006	26.980	-0.271	-0.271	0.000	0.000	0.000	0.000
46	A	49	GLN	0	-0.071	-0.037	28.648	-0.102	-0.102	0.000	0.000	0.000	0.000
47	A	50	ARG	1	0.844	0.920	31.031	8.689	8.689	0.000	0.000	0.000	0.000
48	A	51	ILE	0	-0.034	-0.005	25.999	-0.014	-0.014	0.000	0.000	0.000	0.000
49	A	52	ALA	0	-0.012	-0.002	27.038	-0.316	-0.316	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.084	-0.059	27.970	-0.061	-0.061	0.000	0.000	0.000	0.000
51	A	54	GLY	0	0.024	0.016	30.865	0.131	0.131	0.000	0.000	0.000	0.000
52	A	55	GLU	-1	-0.870	-0.903	31.688	-8.773	-8.773	0.000	0.000	0.000	0.000
53	A	56	VAL	0	-0.024	-0.020	32.063	0.266	0.266	0.000	0.000	0.000	0.000
54	A	57	SER	0	0.025	0.001	28.139	-0.139	-0.139	0.000	0.000	0.000	0.000
55	A	58	PHE	0	0.003	-0.013	23.745	0.136	0.136	0.000	0.000	0.000	0.000
56	A	59	GLU	-1	-0.787	-0.871	25.755	-12.243	-12.243	0.000	0.000	0.000	0.000
57	A	60	GLU	-1	-0.911	-0.944	28.337	-9.348	-9.348	0.000	0.000	0.000	0.000
58	A	61	ALA	0	-0.020	0.004	29.835	0.350	0.350	0.000	0.000	0.000	0.000
59	A	62	ALA	0	0.023	0.003	27.598	0.233	0.233	0.000	0.000	0.000	0.000
60	A	63	SER	0	0.005	-0.002	29.622	0.048	0.048	0.000	0.000	0.000	0.000
61	A	64	GLN	0	-0.092	-0.045	31.842	0.576	0.576	0.000	0.000	0.000	0.000
62	A	65	ARG	1	0.860	0.925	32.197	9.091	9.091	0.000	0.000	0.000	0.000
63	A	66	SER	0	-0.082	-0.039	28.372	-0.107	-0.107	0.000	0.000	0.000	0.000
64	A	67	ASP	-1	-0.790	-0.897	30.448	-9.507	-9.507	0.000	0.000	0.000	0.000
65	A	68	CYS	-1	-0.789	-0.831	25.720	-12.488	-12.488	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.021	0.006	27.361	0.232	0.232	0.000	0.000	0.000	0.000
67	A	70	SER	0	0.004	0.000	24.442	0.222	0.222	0.000	0.000	0.000	0.000
68	A	71	TYR	0	0.008	0.010	26.360	0.045	0.045	0.000	0.000	0.000	0.000
69	A	72	ALA	0	-0.026	-0.008	30.033	0.171	0.171	0.000	0.000	0.000	0.000
70	A	73	SER	0	-0.048	-0.018	25.314	-0.012	-0.012	0.000	0.000	0.000	0.000
71	A	74	GLY	0	0.052	0.047	26.552	-0.186	-0.186	0.000	0.000	0.000	0.000
72	A	75	GLY	0	-0.019	-0.039	25.841	-0.203	-0.203	0.000	0.000	0.000	0.000
73	A	76	ASP	-1	-0.938	-0.964	20.982	-14.940	-14.940	0.000	0.000	0.000	0.000
74	A	77	LEU	0	0.045	0.023	19.030	0.530	0.530	0.000	0.000	0.000	0.000
75	A	78	GLY	0	0.015	0.006	18.342	-0.296	-0.296	0.000	0.000	0.000	0.000
76	A	79	PHE	0	-0.043	-0.038	12.179	-0.292	-0.292	0.000	0.000	0.000	0.000
77	A	80	PHE	0	0.017	0.016	13.319	0.469	0.469	0.000	0.000	0.000	0.000
78	A	81	SER	0	-0.044	-0.066	10.127	-1.623	-1.623	0.000	0.000	0.000	0.000
79	A	82	SER	0	-0.029	-0.027	7.724	2.033	2.033	0.000	0.000	0.000	0.000
80	A	83	GLY	0	0.017	0.004	9.763	-0.901	-0.901	0.000	0.000	0.000	0.000
81	A	84	GLU	-1	-0.923	-0.953	12.649	-19.463	-19.463	0.000	0.000	0.000	0.000
82	A	85	MET	0	-0.005	0.011	15.057	1.492	1.492	0.000	0.000	0.000	0.000
83	A	86	MET	0	0.035	0.012	17.375	-0.003	-0.003	0.000	0.000	0.000	0.000
84	A	87	LYS	1	0.979	0.992	17.488	15.577	15.577	0.000	0.000	0.000	0.000
85	A	88	PRO	0	0.007	-0.009	18.019	-0.726	-0.726	0.000	0.000	0.000	0.000
86	A	89	PHE	0	0.033	0.015	17.421	0.115	0.115	0.000	0.000	0.000	0.000
87	A	90	GLU	-1	-0.877	-0.959	11.647	-25.643	-25.643	0.000	0.000	0.000	0.000
88	A	91	ASP	-1	-0.932	-0.954	14.442	-18.838	-18.838	0.000	0.000	0.000	0.000
89	A	92	ALA	0	0.034	0.012	16.049	-0.430	-0.430	0.000	0.000	0.000	0.000
90	A	93	VAL	0	-0.008	-0.005	13.680	-0.030	-0.030	0.000	0.000	0.000	0.000
91	A	94	ARG	1	0.817	0.906	10.659	20.850	20.850	0.000	0.000	0.000	0.000
92	A	95	ALA	0	-0.059	-0.016	11.816	-1.260	-1.260	0.000	0.000	0.000	0.000
93	A	96	LEU	0	-0.047	-0.001	13.845	1.098	1.098	0.000	0.000	0.000	0.000
94	A	97	LYS	1	0.946	0.957	10.109	25.247	25.247	0.000	0.000	0.000	0.000
95	A	98	ILE	0	-0.021	-0.024	12.105	0.957	0.957	0.000	0.000	0.000	0.000
96	A	99	GLY	0	-0.015	0.000	15.480	0.502	0.502	0.000	0.000	0.000	0.000
97	A	100	ASP	-1	-0.861	-0.906	16.674	-17.054	-17.054	0.000	0.000	0.000	0.000
98	A	101	ILE	0	-0.001	-0.032	19.112	-0.360	-0.360	0.000	0.000	0.000	0.000
99	A	102	SER	0	-0.023	-0.002	20.046	0.057	0.057	0.000	0.000	0.000	0.000
100	A	103	PRO	0	0.018	0.009	21.434	0.607	0.607	0.000	0.000	0.000	0.000
101	A	104	ILE	0	-0.009	-0.008	24.166	-0.310	-0.310	0.000	0.000	0.000	0.000
102	A	105	VAL	0	0.006	0.017	21.894	0.034	0.034	0.000	0.000	0.000	0.000
103	A	106	GLN	0	-0.005	-0.005	25.068	0.437	0.437	0.000	0.000	0.000	0.000
104	A	107	THR	0	-0.043	-0.039	23.808	-0.664	-0.664	0.000	0.000	0.000	0.000
105	A	108	ASP	-1	-0.825	-0.914	26.456	-10.973	-10.973	0.000	0.000	0.000	0.000
106	A	109	SER	0	-0.029	-0.002	28.586	0.430	0.430	0.000	0.000	0.000	0.000
107	A	110	GLY	0	0.042	0.023	29.897	0.226	0.226	0.000	0.000	0.000	0.000
108	A	111	LEU	0	-0.034	0.005	28.365	-0.412	-0.412	0.000	0.000	0.000	0.000
109	A	112	HIS	1	0.891	0.922	23.626	12.856	12.856	0.000	0.000	0.000	0.000
110	A	113	ILE	0	0.008	0.025	23.867	0.116	0.116	0.000	0.000	0.000	0.000
111	A	114	ILE	0	0.016	-0.016	18.232	0.150	0.150	0.000	0.000	0.000	0.000
112	A	115	LYS	1	0.904	0.979	19.474	13.869	13.869	0.000	0.000	0.000	0.000
113	A	116	ARG	1	0.823	0.910	8.482	28.978	28.978	0.000	0.000	0.000	0.000
114	A	117	LEU	0	-0.044	-0.032	15.925	0.822	0.822	0.000	0.000	0.000	0.000
115	A	118	ALA	-1	-0.784	-0.870	11.273	-28.121	-28.121	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:MET)