FMO DATABASE

FMODB ID: VN8J1

Calculation Name: 2O4A-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2O4A

Chain ID: A

ChEMBL ID:

UniProt ID: Q01826

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	84
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-606660.090567
FMO2-HF: Nuclear repulsion	572367.195522
FMO2-HF: Total energy	-34292.895044
FMO2-MP2: Total energy	-34394.57354

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:370:GLU)

Summations of interaction energy for fragment #1(A:370:GLU)

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.
-21.286	-17.25	0.153	-1.981	-2.207	0.006

Interaction energy analysis for fragmet #1(A:370:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.120 / q_NPA : -0.069

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

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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	372	SER	0	0.054	0.039	3.378	6.388	8.480	0.032	-0.988	-1.136	-0.003
47	A	416	LYS	1	0.902	0.952	3.004	-36.836	-34.949	0.122	-0.965	-1.043	0.009
61	A	430	GLN	0	0.047	0.026	4.598	2.745	2.802	-0.001	-0.028	-0.028	0.000
4	A	373	SER	0	-0.012	-0.031	5.969	0.177	0.177	0.000	0.000	0.000	0.000
5	A	374	GLU	-1	-0.865	-0.916	8.096	-1.085	-1.085	0.000	0.000	0.000	0.000
6	A	375	ILE	0	-0.035	-0.014	8.510	-0.276	-0.276	0.000	0.000	0.000	0.000
7	A	376	TYR	0	-0.021	-0.044	10.473	-0.521	-0.521	0.000	0.000	0.000	0.000
8	A	377	GLN	0	-0.044	-0.013	13.584	0.182	0.182	0.000	0.000	0.000	0.000
9	A	378	TRP	0	0.006	-0.022	8.839	-0.751	-0.751	0.000	0.000	0.000	0.000
10	A	379	VAL	0	0.002	0.003	13.642	-0.040	-0.040	0.000	0.000	0.000	0.000
11	A	380	ARG	1	0.789	0.881	16.214	0.508	0.508	0.000	0.000	0.000	0.000
12	A	381	ASP	-1	-0.855	-0.923	18.249	-1.014	-1.014	0.000	0.000	0.000	0.000
13	A	382	GLU	-1	-0.706	-0.775	17.953	-2.144	-2.144	0.000	0.000	0.000	0.000
14	A	383	LEU	0	-0.074	-0.044	19.838	0.109	0.109	0.000	0.000	0.000	0.000
15	A	384	LYS	1	0.925	0.962	21.997	0.828	0.828	0.000	0.000	0.000	0.000
16	A	385	ARG	1	0.670	0.788	21.172	1.842	1.842	0.000	0.000	0.000	0.000
17	A	386	ALA	0	0.038	0.020	23.502	0.070	0.070	0.000	0.000	0.000	0.000
18	A	387	GLY	0	-0.011	0.015	25.218	0.070	0.070	0.000	0.000	0.000	0.000
19	A	388	ILE	0	-0.084	-0.034	21.385	0.060	0.060	0.000	0.000	0.000	0.000
20	A	389	SER	0	0.042	0.014	25.138	0.004	0.004	0.000	0.000	0.000	0.000
21	A	390	GLN	0	0.081	0.019	21.999	-0.086	-0.086	0.000	0.000	0.000	0.000
22	A	391	ALA	0	-0.017	-0.012	22.003	-0.119	-0.119	0.000	0.000	0.000	0.000
23	A	392	VAL	0	0.040	0.038	23.345	-0.085	-0.085	0.000	0.000	0.000	0.000
24	A	393	PHE	0	0.085	0.031	15.314	-0.109	-0.109	0.000	0.000	0.000	0.000
25	A	394	ALA	0	-0.017	-0.014	18.449	-0.260	-0.260	0.000	0.000	0.000	0.000
26	A	395	ARG	1	0.882	0.960	18.878	1.281	1.281	0.000	0.000	0.000	0.000
27	A	396	VAL	0	0.006	-0.010	19.129	-0.131	-0.131	0.000	0.000	0.000	0.000
28	A	397	ALA	0	0.003	0.025	15.069	-0.275	-0.275	0.000	0.000	0.000	0.000
29	A	398	PHE	0	-0.024	-0.036	13.527	-0.483	-0.483	0.000	0.000	0.000	0.000
30	A	399	ASN	0	0.003	0.030	15.218	0.316	0.316	0.000	0.000	0.000	0.000
31	A	400	ARG	1	0.811	0.910	14.844	2.336	2.336	0.000	0.000	0.000	0.000
32	A	401	THR	0	0.041	0.012	19.786	0.009	0.009	0.000	0.000	0.000	0.000
33	A	402	GLN	0	0.050	0.001	21.412	-0.026	-0.026	0.000	0.000	0.000	0.000
34	A	403	GLY	0	0.035	0.025	22.532	0.004	0.004	0.000	0.000	0.000	0.000
35	A	404	LEU	0	0.003	0.004	17.379	0.087	0.087	0.000	0.000	0.000	0.000
36	A	405	LEU	0	0.014	0.013	16.703	0.038	0.038	0.000	0.000	0.000	0.000
37	A	406	SER	0	-0.003	-0.002	18.840	0.053	0.053	0.000	0.000	0.000	0.000
38	A	407	GLU	-1	-0.828	-0.898	20.228	0.126	0.126	0.000	0.000	0.000	0.000
39	A	408	ILE	0	-0.041	-0.017	13.965	0.137	0.137	0.000	0.000	0.000	0.000
40	A	409	LEU	0	0.003	-0.007	16.059	0.178	0.178	0.000	0.000	0.000	0.000
41	A	410	ARG	1	0.803	0.880	17.706	-0.043	-0.043	0.000	0.000	0.000	0.000
42	A	411	LYS	1	0.863	0.944	16.777	-0.075	-0.075	0.000	0.000	0.000	0.000
43	A	412	GLU	-1	-0.830	-0.892	14.168	0.314	0.314	0.000	0.000	0.000	0.000
44	A	413	GLU	-1	-0.910	-0.954	12.420	1.387	1.387	0.000	0.000	0.000	0.000
45	A	414	ASP	-1	-0.752	-0.870	8.357	7.253	7.253	0.000	0.000	0.000	0.000
46	A	415	PRO	0	0.007	-0.012	5.214	0.454	0.454	0.000	0.000	0.000	0.000
48	A	417	THR	0	-0.067	-0.029	6.473	-0.766	-0.766	0.000	0.000	0.000	0.000
49	A	418	ALA	0	0.003	0.032	8.375	-1.039	-1.039	0.000	0.000	0.000	0.000
50	A	419	SER	0	0.053	0.024	9.832	0.144	0.144	0.000	0.000	0.000	0.000
51	A	420	GLN	0	0.056	0.007	9.224	-0.964	-0.964	0.000	0.000	0.000	0.000
52	A	421	SER	0	-0.010	-0.002	10.107	-0.898	-0.898	0.000	0.000	0.000	0.000
53	A	422	LEU	0	0.017	0.025	10.572	-0.703	-0.703	0.000	0.000	0.000	0.000
54	A	423	LEU	0	0.048	0.016	5.164	-1.429	-1.429	0.000	0.000	0.000	0.000
55	A	424	VAL	0	-0.073	-0.041	7.069	-2.577	-2.577	0.000	0.000	0.000	0.000
56	A	425	ASN	0	0.020	0.001	9.317	-0.741	-0.741	0.000	0.000	0.000	0.000
57	A	426	LEU	0	0.036	0.015	7.820	-0.485	-0.485	0.000	0.000	0.000	0.000
58	A	427	ARG	1	0.951	0.976	5.241	7.684	7.684	0.000	0.000	0.000	0.000
59	A	428	ALA	0	-0.052	-0.002	6.889	-0.493	-0.493	0.000	0.000	0.000	0.000
60	A	429	MET	0	0.030	0.020	10.530	0.318	0.318	0.000	0.000	0.000	0.000
62	A	431	ASN	0	-0.025	-0.024	7.165	-0.757	-0.757	0.000	0.000	0.000	0.000
63	A	432	PHE	0	0.030	0.012	9.843	0.703	0.703	0.000	0.000	0.000	0.000
64	A	433	LEU	0	0.000	-0.016	12.229	0.499	0.499	0.000	0.000	0.000	0.000
65	A	434	GLN	0	-0.042	-0.021	7.830	-1.195	-1.195	0.000	0.000	0.000	0.000
66	A	435	LEU	0	-0.010	0.024	12.659	0.222	0.222	0.000	0.000	0.000	0.000
67	A	436	PRO	0	0.030	0.009	15.808	0.205	0.205	0.000	0.000	0.000	0.000
68	A	437	GLU	-1	-0.860	-0.924	19.139	-1.660	-1.660	0.000	0.000	0.000	0.000
69	A	438	ALA	0	0.040	0.009	21.102	0.055	0.055	0.000	0.000	0.000	0.000
70	A	439	GLU	-1	-0.947	-0.969	20.021	-2.548	-2.548	0.000	0.000	0.000	0.000
71	A	440	ARG	1	0.777	0.869	16.655	2.818	2.818	0.000	0.000	0.000	0.000
72	A	441	ASP	-1	-0.750	-0.857	20.687	-1.522	-1.522	0.000	0.000	0.000	0.000
73	A	442	ARG	1	0.857	0.919	24.319	1.773	1.773	0.000	0.000	0.000	0.000
74	A	443	ILE	0	0.004	0.008	20.168	0.088	0.088	0.000	0.000	0.000	0.000
75	A	444	TYR	0	-0.048	-0.073	19.455	0.006	0.006	0.000	0.000	0.000	0.000
76	A	445	GLN	0	-0.009	0.001	24.737	0.088	0.088	0.000	0.000	0.000	0.000
77	A	446	ASP	-1	-0.835	-0.914	26.042	-1.418	-1.418	0.000	0.000	0.000	0.000
78	A	447	GLU	-1	-0.907	-0.959	24.555	-1.372	-1.372	0.000	0.000	0.000	0.000
79	A	448	ARG	1	0.916	0.969	26.940	1.124	1.124	0.000	0.000	0.000	0.000
80	A	449	GLU	-1	-0.887	-0.948	29.812	-0.811	-0.811	0.000	0.000	0.000	0.000
81	A	450	ARG	1	0.779	0.890	24.224	1.529	1.529	0.000	0.000	0.000	0.000
82	A	451	SER	0	-0.070	-0.056	29.231	0.056	0.056	0.000	0.000	0.000	0.000
83	A	452	LEU	0	-0.052	-0.018	31.256	0.058	0.058	0.000	0.000	0.000	0.000
84	A	453	ARG	0	-0.004	0.025	34.400	0.125	0.125	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:370:GLU)