FMO DATABASE

FMODB ID: 87V2Y

Calculation Name: 5O2M-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5O2M

Chain ID: A

ChEMBL ID:

UniProt ID: P56945

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	81
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-490902.82462
FMO2-HF: Nuclear repulsion	458852.200448
FMO2-HF: Total energy	-32050.624172
FMO2-MP2: Total energy	-32142.547408

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.
-60.022	-53.569	3.961	-4.774	-5.641	-0.05

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 : 0.825 / q_NPA : 0.905

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	MET	0	0.016	0.011	3.527	-10.958	-9.918	-0.004	-0.602	-0.435	-0.002
4	A	4	LYS	1	0.928	0.975	2.250	59.466	60.119	0.484	-0.358	-0.780	-0.002
73	A	73	PRO	0	0.035	0.020	4.083	-1.794	-1.743	-0.001	-0.015	-0.035	0.000
74	A	74	ALA	0	-0.018	-0.024	2.743	-29.114	-26.330	0.991	-2.034	-1.740	-0.021
75	A	75	GLY	0	-0.067	-0.041	2.480	-22.184	-19.963	2.263	-2.324	-2.161	-0.022
76	A	76	GLU	-1	-0.953	-0.941	2.914	-25.174	-25.470	0.228	0.559	-0.490	-0.003
5	A	5	TYR	0	0.059	0.031	6.432	3.136	3.136	0.000	0.000	0.000	0.000
6	A	6	LEU	0	-0.007	-0.002	9.146	-2.083	-2.083	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.074	-0.039	10.392	-1.119	-1.119	0.000	0.000	0.000	0.000
8	A	8	VAL	0	0.015	0.031	12.393	0.672	0.672	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.011	0.004	15.547	0.233	0.233	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.009	-0.003	18.907	0.137	0.137	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.873	0.945	22.316	11.209	11.209	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.030	0.023	25.777	0.087	0.087	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.053	-0.031	28.666	0.265	0.265	0.000	0.000	0.000	0.000
14	A	14	TYR	0	-0.041	-0.032	31.585	0.347	0.347	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.929	-0.972	32.212	-9.101	-9.101	0.000	0.000	0.000	0.000
16	A	16	ASN	0	-0.021	-0.004	31.447	0.080	0.080	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.030	-0.007	34.816	0.045	0.045	0.000	0.000	0.000	0.000
18	A	18	ALA	0	-0.013	-0.001	31.813	-0.053	-0.053	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.942	-0.972	33.795	-8.207	-8.207	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.019	-0.020	31.633	0.282	0.282	0.000	0.000	0.000	0.000
21	A	21	PRO	0	-0.075	-0.043	30.483	-0.198	-0.198	0.000	0.000	0.000	0.000
22	A	22	ASP	-1	-0.813	-0.900	27.387	-11.276	-11.276	0.000	0.000	0.000	0.000
23	A	23	GLU	-1	-0.906	-0.945	26.944	-10.515	-10.515	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.040	-0.014	23.573	0.087	0.087	0.000	0.000	0.000	0.000
25	A	25	SER	0	-0.021	0.000	28.083	0.291	0.291	0.000	0.000	0.000	0.000
26	A	26	PHE	0	0.006	-0.005	28.242	-0.279	-0.279	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.980	0.973	30.293	9.351	9.351	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.973	0.996	31.108	8.185	8.185	0.000	0.000	0.000	0.000
29	A	29	GLY	0	-0.042	-0.028	31.060	0.239	0.239	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.819	-0.900	27.564	-11.825	-11.825	0.000	0.000	0.000	0.000
31	A	31	ILE	0	-0.072	-0.052	22.198	-0.083	-0.083	0.000	0.000	0.000	0.000
32	A	32	MET	0	0.023	0.041	22.348	-0.080	-0.080	0.000	0.000	0.000	0.000
33	A	33	THR	0	-0.001	-0.010	15.568	-0.539	-0.539	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.017	-0.017	17.345	0.534	0.534	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.048	-0.014	14.252	-1.476	-1.476	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.836	-0.917	14.128	-19.938	-19.938	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.890	0.931	16.577	16.485	16.485	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.808	-0.921	19.736	-14.603	-14.603	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.061	-0.031	20.464	0.567	0.567	0.000	0.000	0.000	0.000
40	A	40	GLN	0	-0.014	-0.013	22.178	0.307	0.307	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.027	0.019	24.778	0.481	0.481	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.068	-0.023	26.300	0.461	0.461	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.889	-0.952	26.173	-12.289	-12.289	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.009	0.009	25.539	0.399	0.399	0.000	0.000	0.000	0.000
45	A	45	TRP	0	-0.028	-0.024	25.886	0.142	0.142	0.000	0.000	0.000	0.000
46	A	46	TRP	0	-0.040	-0.023	20.845	-0.631	-0.631	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.042	0.034	17.797	0.523	0.523	0.000	0.000	0.000	0.000
48	A	48	CYS	0	-0.046	-0.015	19.156	-1.094	-1.094	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.021	-0.031	18.806	-0.046	-0.046	0.000	0.000	0.000	0.000
50	A	50	LEU	0	0.026	-0.004	20.791	-0.275	-0.275	0.000	0.000	0.000	0.000
51	A	51	HIS	0	-0.016	-0.008	23.683	0.345	0.345	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.006	0.001	23.431	0.381	0.381	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.929	0.983	23.599	11.089	11.089	0.000	0.000	0.000	0.000
54	A	54	GLN	0	0.011	0.008	18.479	0.132	0.132	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.050	0.023	21.886	0.457	0.457	0.000	0.000	0.000	0.000
56	A	56	ILE	0	-0.014	-0.001	23.692	-0.510	-0.510	0.000	0.000	0.000	0.000
57	A	57	VAL	0	0.017	-0.007	24.833	0.437	0.437	0.000	0.000	0.000	0.000
58	A	58	PRO	0	0.004	0.023	25.896	-0.338	-0.338	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.077	0.013	25.208	0.137	0.137	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.030	-0.015	25.987	0.005	0.005	0.000	0.000	0.000	0.000
61	A	61	ARG	1	0.904	0.957	28.815	9.905	9.905	0.000	0.000	0.000	0.000
62	A	62	LEU	0	0.012	0.003	24.152	0.077	0.077	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.948	0.980	25.395	11.885	11.885	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.014	0.010	19.322	-0.130	-0.130	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.039	-0.029	20.595	0.614	0.614	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.021	0.007	15.377	-0.675	-0.675	0.000	0.000	0.000	0.000
67	A	67	GLY	0	-0.008	-0.003	17.970	0.283	0.283	0.000	0.000	0.000	0.000
68	A	68	MET	0	0.007	0.005	14.835	0.373	0.373	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.010	0.020	12.678	-1.071	-1.071	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.885	-0.942	11.733	-27.302	-27.302	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.882	0.930	7.478	33.271	33.271	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.982	0.989	7.776	24.789	24.789	0.000	0.000	0.000	0.000
77	A	77	PHE	0	-0.009	-0.031	6.477	3.002	3.002	0.000	0.000	0.000	0.000
78	A	78	ILE	0	0.018	0.022	7.448	-0.993	-0.993	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.021	-0.018	8.653	-2.690	-2.690	0.000	0.000	0.000	0.000
80	A	80	THR	0	-0.066	-0.051	9.271	0.582	0.582	0.000	0.000	0.000	0.000
81	A	81	ASP	-2	-1.889	-1.913	10.447	-43.154	-43.154	0.000	0.000	0.000	0.000

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