FMO DATABASE

FMODB ID: LQ2L9

Calculation Name: 2EDG-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EDG

Chain ID: A

ChEMBL ID:

UniProt ID: Q91WK5

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	130
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1058571.538619
FMO2-HF: Nuclear repulsion	1008370.0273
FMO2-HF: Total energy	-50201.511319
FMO2-MP2: Total energy	-50346.645453

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:1:GLY)

Summations of interaction energy for fragment #1(A:1: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.
-175.779	-174.529	-0.016	-0.569	-0.664	-0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.846 / q_NPA : 0.908

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	3	SER	0	0.080	0.046	3.841	-1.513	-0.263	-0.016	-0.569	-0.664	-0.003
4	A	4	GLY	0	0.003	0.007	6.879	1.170	1.170	0.000	0.000	0.000	0.000
5	A	5	SER	0	-0.017	-0.006	10.421	-0.470	-0.470	0.000	0.000	0.000	0.000
6	A	6	SER	0	0.003	0.003	13.311	0.119	0.119	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.029	-0.003	14.739	0.720	0.720	0.000	0.000	0.000	0.000
8	A	8	ARG	1	0.926	0.979	18.473	12.027	12.027	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.849	0.934	13.731	20.450	20.450	0.000	0.000	0.000	0.000
10	A	10	PHE	0	0.013	-0.003	19.881	0.927	0.927	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.055	0.024	20.603	-0.647	-0.647	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.966	-0.982	22.974	-12.703	-12.703	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.937	0.957	24.305	11.391	11.391	0.000	0.000	0.000	0.000
14	A	14	HIS	0	0.005	0.011	26.481	0.437	0.437	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.862	-0.931	26.850	-11.098	-11.098	0.000	0.000	0.000	0.000
16	A	16	TRP	0	-0.071	-0.024	24.340	-0.793	-0.793	0.000	0.000	0.000	0.000
17	A	17	ILE	0	0.025	0.002	22.057	0.353	0.353	0.000	0.000	0.000	0.000
18	A	18	THR	0	-0.051	-0.021	22.646	-0.621	-0.621	0.000	0.000	0.000	0.000
19	A	19	THR	0	-0.007	-0.020	20.500	-0.087	-0.087	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.941	-0.966	23.087	-12.282	-12.282	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.940	-0.970	25.674	-11.263	-11.263	0.000	0.000	0.000	0.000
22	A	22	GLY	0	-0.025	-0.007	24.548	0.240	0.240	0.000	0.000	0.000	0.000
23	A	23	ILE	0	-0.048	-0.029	25.603	0.097	0.097	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.046	0.010	25.692	-0.498	-0.498	0.000	0.000	0.000	0.000
25	A	25	THR	0	-0.048	-0.019	26.468	0.668	0.668	0.000	0.000	0.000	0.000
26	A	26	VAL	0	0.026	0.019	27.535	-0.458	-0.458	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.069	0.020	28.862	0.489	0.489	0.000	0.000	0.000	0.000
28	A	28	ILE	0	0.043	0.034	29.127	-0.366	-0.366	0.000	0.000	0.000	0.000
29	A	29	SER	0	0.032	0.003	27.498	0.176	0.176	0.000	0.000	0.000	0.000
30	A	30	ASN	0	-0.044	-0.044	29.545	-0.041	-0.041	0.000	0.000	0.000	0.000
31	A	31	PHE	0	0.044	0.024	29.817	0.284	0.284	0.000	0.000	0.000	0.000
32	A	32	ALA	0	0.052	0.029	31.465	0.246	0.246	0.000	0.000	0.000	0.000
33	A	33	GLN	0	0.016	0.026	33.142	0.494	0.494	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.918	-0.947	34.488	-8.828	-8.828	0.000	0.000	0.000	0.000
35	A	35	ALA	0	-0.044	-0.015	35.262	0.275	0.275	0.000	0.000	0.000	0.000
36	A	36	LEU	0	-0.026	-0.013	37.131	0.249	0.249	0.000	0.000	0.000	0.000
37	A	37	GLY	0	-0.058	-0.039	39.018	0.277	0.277	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.953	-0.973	41.032	-7.107	-7.107	0.000	0.000	0.000	0.000
39	A	39	VAL	0	0.020	0.004	39.543	0.054	0.054	0.000	0.000	0.000	0.000
40	A	40	VAL	0	-0.010	-0.010	42.893	0.100	0.100	0.000	0.000	0.000	0.000
41	A	41	TYR	0	-0.043	-0.022	44.444	0.145	0.145	0.000	0.000	0.000	0.000
42	A	42	CYS	0	0.003	-0.003	40.463	-0.175	-0.175	0.000	0.000	0.000	0.000
43	A	43	SER	0	-0.030	0.013	41.371	0.196	0.196	0.000	0.000	0.000	0.000
44	A	44	LEU	0	0.028	0.000	37.354	-0.278	-0.278	0.000	0.000	0.000	0.000
45	A	45	PRO	0	0.002	0.010	36.178	0.189	0.189	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.909	-0.954	39.509	-7.207	-7.207	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.009	0.020	38.138	-0.245	-0.245	0.000	0.000	0.000	0.000
48	A	48	GLY	0	-0.003	0.006	37.551	0.197	0.197	0.000	0.000	0.000	0.000
49	A	49	THR	0	-0.058	-0.051	36.099	0.056	0.056	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.774	0.875	33.612	8.518	8.518	0.000	0.000	0.000	0.000
51	A	51	LEU	0	0.075	0.049	31.127	0.152	0.152	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.940	0.973	28.915	9.506	9.506	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.899	0.936	21.015	14.777	14.777	0.000	0.000	0.000	0.000
54	A	54	GLN	0	-0.037	-0.025	25.193	0.090	0.090	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.941	-0.950	27.855	-9.312	-9.312	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.954	-0.972	31.427	-8.604	-8.604	0.000	0.000	0.000	0.000
57	A	57	PHE	0	-0.064	-0.043	31.288	0.182	0.182	0.000	0.000	0.000	0.000
58	A	58	GLY	0	0.040	0.013	35.404	0.232	0.232	0.000	0.000	0.000	0.000
59	A	59	ALA	0	-0.018	-0.005	37.014	-0.159	-0.159	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.013	0.002	36.137	0.131	0.131	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.903	-0.965	39.771	-7.185	-7.185	0.000	0.000	0.000	0.000
62	A	62	SER	0	-0.001	-0.007	41.842	0.085	0.085	0.000	0.000	0.000	0.000
63	A	63	VAL	0	-0.048	-0.026	43.871	0.117	0.117	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.854	0.939	41.352	7.757	7.757	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.001	-0.003	40.909	0.072	0.072	0.000	0.000	0.000	0.000
66	A	66	ALA	0	0.041	0.038	41.206	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	67	SER	0	-0.020	-0.016	34.848	-0.142	-0.142	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.880	-0.907	35.172	-8.818	-8.818	0.000	0.000	0.000	0.000
69	A	69	LEU	0	-0.039	-0.012	32.987	-0.246	-0.246	0.000	0.000	0.000	0.000
70	A	70	TYR	0	-0.045	-0.057	29.458	0.040	0.040	0.000	0.000	0.000	0.000
71	A	71	SER	0	0.000	0.006	28.339	-0.196	-0.196	0.000	0.000	0.000	0.000
72	A	72	PRO	0	0.023	0.022	23.964	-0.321	-0.321	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.021	-0.027	20.402	-0.709	-0.709	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.054	-0.037	24.601	0.589	0.589	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.032	0.020	26.212	-0.464	-0.464	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.901	-0.927	28.908	-8.763	-8.763	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.024	0.004	32.064	-0.237	-0.237	0.000	0.000	0.000	0.000
78	A	78	THR	0	-0.081	-0.048	32.329	0.203	0.203	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.857	-0.937	34.938	-7.969	-7.969	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.014	-0.015	35.895	-0.341	-0.341	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.030	-0.031	37.274	0.351	0.351	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.890	-0.956	39.425	-7.213	-7.213	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.017	0.003	41.743	0.183	0.183	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.032	-0.019	38.053	0.136	0.136	0.000	0.000	0.000	0.000
85	A	85	ALA	0	0.017	0.017	42.766	0.083	0.083	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.996	-0.990	45.891	-6.285	-6.285	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.076	-0.054	45.172	-0.004	-0.004	0.000	0.000	0.000	0.000
88	A	88	PRO	0	0.082	0.045	42.453	-0.169	-0.169	0.000	0.000	0.000	0.000
89	A	89	GLY	0	0.036	0.016	41.369	-0.201	-0.201	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.031	-0.014	40.316	-0.075	-0.075	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.004	0.006	35.805	-0.159	-0.159	0.000	0.000	0.000	0.000
92	A	92	ASN	0	-0.069	-0.051	36.857	-0.066	-0.066	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.861	0.931	38.376	7.404	7.404	0.000	0.000	0.000	0.000
94	A	94	SER	0	-0.026	-0.006	36.342	-0.099	-0.099	0.000	0.000	0.000	0.000
95	A	95	CYS	0	-0.019	0.002	31.068	0.023	0.023	0.000	0.000	0.000	0.000
96	A	96	TYR	0	-0.053	-0.050	27.461	-0.218	-0.218	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.948	-0.966	31.818	-9.571	-9.571	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.850	-0.941	34.397	-8.381	-8.381	0.000	0.000	0.000	0.000
99	A	99	GLY	0	-0.025	-0.001	35.599	0.159	0.159	0.000	0.000	0.000	0.000
100	A	100	TRP	0	-0.058	-0.016	32.833	-0.275	-0.275	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.011	0.007	32.427	0.287	0.287	0.000	0.000	0.000	0.000
102	A	102	ILE	0	0.019	0.001	31.832	0.282	0.282	0.000	0.000	0.000	0.000
103	A	103	LYS	1	0.914	0.972	31.345	9.372	9.372	0.000	0.000	0.000	0.000
104	A	104	MET	0	-0.004	0.019	28.006	0.328	0.328	0.000	0.000	0.000	0.000
105	A	105	THR	0	0.024	0.011	28.021	-0.273	-0.273	0.000	0.000	0.000	0.000
106	A	106	LEU	0	-0.005	-0.004	22.119	-0.172	-0.172	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.042	-0.034	23.791	-0.087	-0.087	0.000	0.000	0.000	0.000
108	A	108	ASP	-1	-0.904	-0.950	20.399	-14.593	-14.593	0.000	0.000	0.000	0.000
109	A	109	PRO	0	-0.014	-0.019	18.294	-0.462	-0.462	0.000	0.000	0.000	0.000
110	A	110	SER	0	-0.011	-0.012	14.374	-1.134	-1.134	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.833	-0.913	14.989	-17.592	-17.592	0.000	0.000	0.000	0.000
112	A	112	LEU	0	-0.018	-0.007	16.890	0.038	0.038	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-1.013	-0.997	10.302	-30.156	-30.156	0.000	0.000	0.000	0.000
114	A	114	GLU	-1	-0.977	-0.987	13.361	-17.816	-17.816	0.000	0.000	0.000	0.000
115	A	115	LEU	0	0.023	0.031	14.932	0.583	0.583	0.000	0.000	0.000	0.000
116	A	116	MET	0	0.004	0.002	15.794	-1.409	-1.409	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.009	-0.018	13.878	0.632	0.632	0.000	0.000	0.000	0.000
118	A	118	GLU	-1	-0.864	-0.938	16.765	-13.746	-13.746	0.000	0.000	0.000	0.000
119	A	119	GLU	-1	-0.889	-0.941	14.415	-17.459	-17.459	0.000	0.000	0.000	0.000
120	A	120	ALA	0	0.006	-0.006	15.027	0.210	0.210	0.000	0.000	0.000	0.000
121	A	121	TYR	0	0.055	0.036	17.047	0.707	0.707	0.000	0.000	0.000	0.000
122	A	122	GLU	-1	-0.846	-0.932	20.414	-13.594	-13.594	0.000	0.000	0.000	0.000
123	A	123	LYS	1	0.712	0.857	16.870	16.947	16.947	0.000	0.000	0.000	0.000
124	A	124	TYR	0	0.011	0.016	20.809	0.457	0.457	0.000	0.000	0.000	0.000
125	A	125	VAL	0	0.012	-0.005	22.465	0.476	0.476	0.000	0.000	0.000	0.000
126	A	126	LYS	1	0.901	0.953	21.981	13.386	13.386	0.000	0.000	0.000	0.000
127	A	127	SER	0	-0.022	-0.017	23.395	0.269	0.269	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.075	-0.023	26.164	0.217	0.217	0.000	0.000	0.000	0.000
129	A	129	GLU	-1	-1.055	-1.026	29.307	-9.383	-9.383	0.000	0.000	0.000	0.000
130	A	130	GLU	-2	-1.941	-1.958	27.341	-22.044	-22.044	0.000	0.000	0.000	0.000

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