FMO DATABASE

FMODB ID: 192NZ

Calculation Name: 1G9O-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1G9O

Chain ID: A

ChEMBL ID:

UniProt ID: O14745

Base Structure: X-ray

Registration Date: 2025-10-05

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	91
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-612733.625713
FMO2-HF: Nuclear repulsion	577520.630586
FMO2-HF: Total energy	-35212.995127
FMO2-MP2: Total energy	-35315.464835

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:9:ARG)

Summations of interaction energy for fragment #1(A:9:ARG)

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.
-447.856	-447.509	55.993	-27.48	-28.858	-0.316

Interaction energy analysis for fragmet #1(A:9:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.598 / q_NPA : 1.775

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	11	LEU	0	0.039	0.008	2.085	-18.379	-14.750	3.502	-3.423	-3.708	-0.045
4	A	12	PRO	0	-0.008	-0.008	4.706	-5.349	-5.144	-0.001	-0.007	-0.197	0.000
83	A	91	VAL	0	-0.011	-0.013	2.526	-2.652	-3.379	4.461	-0.942	-2.793	0.003
84	A	92	ASP	-1	-0.774	-0.844	2.490	-85.788	-84.348	1.343	-0.807	-1.975	-0.004
85	A	93	PRO	0	0.012	0.027	1.777	-54.533	-61.195	20.015	-7.607	-5.746	-0.100
86	A	94	GLU	-1	-0.796	-0.927	1.981	-219.687	-217.336	26.674	-14.688	-14.336	-0.170
87	A	95	THR	0	-0.032	-0.020	4.839	6.453	6.564	-0.001	-0.006	-0.103	0.000
5	A	13	ARG	1	0.819	0.887	6.411	67.353	67.353	0.000	0.000	0.000	0.000
6	A	14	LEU	0	-0.026	-0.016	8.286	1.556	1.556	0.000	0.000	0.000	0.000
7	A	15	CYS	0	0.004	0.025	10.188	0.456	0.456	0.000	0.000	0.000	0.000
8	A	16	CYS	0	-0.049	-0.037	13.113	1.569	1.569	0.000	0.000	0.000	0.000
9	A	17	LEU	0	0.002	0.011	14.949	0.391	0.391	0.000	0.000	0.000	0.000
10	A	18	GLU	-1	-0.889	-0.944	18.885	-22.106	-22.106	0.000	0.000	0.000	0.000
11	A	19	LYS	1	0.882	0.938	22.366	21.530	21.530	0.000	0.000	0.000	0.000
12	A	20	GLY	0	0.073	0.039	23.858	0.676	0.676	0.000	0.000	0.000	0.000
13	A	21	PRO	0	-0.005	-0.006	25.586	0.158	0.158	0.000	0.000	0.000	0.000
14	A	22	ASN	0	-0.003	-0.003	26.469	0.842	0.842	0.000	0.000	0.000	0.000
15	A	23	GLY	0	-0.037	-0.020	24.495	-0.456	-0.456	0.000	0.000	0.000	0.000
16	A	24	TYR	0	-0.004	-0.039	19.041	-0.202	-0.202	0.000	0.000	0.000	0.000
17	A	25	GLY	0	0.048	0.029	19.352	-0.916	-0.916	0.000	0.000	0.000	0.000
18	A	26	PHE	0	-0.003	-0.008	14.765	-1.090	-1.090	0.000	0.000	0.000	0.000
19	A	27	HIS	0	-0.061	-0.031	16.400	1.123	1.123	0.000	0.000	0.000	0.000
20	A	28	LEU	0	-0.005	-0.005	13.355	-2.039	-2.039	0.000	0.000	0.000	0.000
21	A	29	HIS	0	-0.025	-0.020	12.069	3.466	3.466	0.000	0.000	0.000	0.000
22	A	30	GLY	0	0.042	0.025	13.456	-2.107	-2.107	0.000	0.000	0.000	0.000
23	A	31	GLU	-1	-0.859	-0.933	8.845	-54.480	-54.480	0.000	0.000	0.000	0.000
24	A	32	LYS	1	0.937	0.955	12.805	32.393	32.393	0.000	0.000	0.000	0.000
25	A	33	GLY	0	0.012	0.011	13.229	-1.654	-1.654	0.000	0.000	0.000	0.000
26	A	34	LYS	1	0.873	0.950	7.721	54.406	54.406	0.000	0.000	0.000	0.000
27	A	35	LEU	0	-0.015	-0.003	12.482	1.876	1.876	0.000	0.000	0.000	0.000
28	A	36	GLY	0	0.064	0.043	12.091	1.573	1.573	0.000	0.000	0.000	0.000
29	A	37	GLN	0	-0.012	-0.018	12.489	1.693	1.693	0.000	0.000	0.000	0.000
30	A	38	TYR	0	0.055	0.017	6.481	-4.399	-4.399	0.000	0.000	0.000	0.000
31	A	39	ILE	0	-0.003	-0.002	9.811	4.762	4.762	0.000	0.000	0.000	0.000
32	A	40	ARG	1	0.917	0.976	11.521	27.587	27.587	0.000	0.000	0.000	0.000
33	A	41	LEU	0	0.019	-0.001	14.116	0.419	0.419	0.000	0.000	0.000	0.000
34	A	42	VAL	0	0.007	0.007	12.884	0.361	0.361	0.000	0.000	0.000	0.000
35	A	43	GLU	-1	-0.863	-0.919	15.831	-25.234	-25.234	0.000	0.000	0.000	0.000
36	A	44	PRO	0	0.030	0.011	19.342	-0.384	-0.384	0.000	0.000	0.000	0.000
37	A	45	GLY	0	-0.034	-0.017	20.672	1.193	1.193	0.000	0.000	0.000	0.000
38	A	46	SER	0	-0.048	-0.019	18.608	0.307	0.307	0.000	0.000	0.000	0.000
39	A	47	PRO	0	0.013	-0.008	19.556	-0.833	-0.833	0.000	0.000	0.000	0.000
40	A	48	ALA	0	0.009	0.010	15.198	-1.002	-1.002	0.000	0.000	0.000	0.000
41	A	49	GLU	-1	-0.772	-0.869	14.881	-31.027	-31.027	0.000	0.000	0.000	0.000
42	A	50	LYS	1	0.787	0.885	16.074	26.158	26.158	0.000	0.000	0.000	0.000
43	A	51	ALA	0	-0.021	0.003	15.188	0.075	0.075	0.000	0.000	0.000	0.000
44	A	52	GLY	0	0.002	0.009	12.701	-2.117	-2.117	0.000	0.000	0.000	0.000
45	A	53	LEU	0	-0.034	-0.016	10.269	-3.943	-3.943	0.000	0.000	0.000	0.000
46	A	54	LEU	0	-0.015	-0.012	6.895	3.116	3.116	0.000	0.000	0.000	0.000
47	A	55	ALA	0	-0.018	-0.014	9.734	-0.044	-0.044	0.000	0.000	0.000	0.000
48	A	56	GLY	0	0.029	0.001	7.812	-2.440	-2.440	0.000	0.000	0.000	0.000
49	A	57	ASP	-1	-0.801	-0.901	5.795	-71.659	-71.659	0.000	0.000	0.000	0.000
50	A	58	ARG	1	0.817	0.889	5.148	74.099	74.099	0.000	0.000	0.000	0.000
51	A	59	LEU	0	-0.017	-0.018	6.818	-1.704	-1.704	0.000	0.000	0.000	0.000
52	A	60	VAL	0	-0.041	-0.014	8.217	-0.061	-0.061	0.000	0.000	0.000	0.000
53	A	61	GLU	-1	-0.901	-0.971	10.787	-34.837	-34.837	0.000	0.000	0.000	0.000
54	A	62	VAL	0	-0.010	-0.010	13.860	-0.887	-0.887	0.000	0.000	0.000	0.000
55	A	63	ASN	0	-0.019	-0.030	16.625	0.876	0.876	0.000	0.000	0.000	0.000
56	A	64	GLY	0	-0.001	0.009	17.237	1.562	1.562	0.000	0.000	0.000	0.000
57	A	65	GLU	-1	-0.888	-0.919	18.296	-26.642	-26.642	0.000	0.000	0.000	0.000
58	A	66	ASN	0	-0.024	-0.034	12.963	-0.562	-0.562	0.000	0.000	0.000	0.000
59	A	67	VAL	0	-0.011	-0.010	13.158	1.807	1.807	0.000	0.000	0.000	0.000
60	A	68	GLU	-1	-0.819	-0.870	9.464	-50.889	-50.889	0.000	0.000	0.000	0.000
61	A	69	LYS	1	0.905	0.940	12.986	31.054	31.054	0.000	0.000	0.000	0.000
62	A	70	GLU	-1	-0.806	-0.854	16.147	-26.361	-26.361	0.000	0.000	0.000	0.000
63	A	71	THR	0	-0.020	-0.032	17.126	-0.801	-0.801	0.000	0.000	0.000	0.000
64	A	72	HIS	0	-0.015	-0.018	17.547	1.200	1.200	0.000	0.000	0.000	0.000
65	A	73	GLN	0	0.050	0.016	19.122	-0.486	-0.486	0.000	0.000	0.000	0.000
66	A	74	GLN	0	0.049	0.064	20.717	-0.174	-0.174	0.000	0.000	0.000	0.000
67	A	75	VAL	0	0.078	0.036	15.152	0.323	0.323	0.000	0.000	0.000	0.000
68	A	76	VAL	0	0.007	-0.002	18.567	0.152	0.152	0.000	0.000	0.000	0.000
69	A	77	SER	0	-0.043	-0.030	20.423	1.055	1.055	0.000	0.000	0.000	0.000
70	A	78	ARG	1	0.771	0.857	19.258	28.352	28.352	0.000	0.000	0.000	0.000
71	A	79	ILE	0	0.008	0.008	16.347	0.233	0.233	0.000	0.000	0.000	0.000
72	A	80	ARG	1	0.896	0.954	20.670	23.631	23.631	0.000	0.000	0.000	0.000
73	A	81	ALA	0	0.006	-0.004	24.248	0.817	0.817	0.000	0.000	0.000	0.000
74	A	82	ALA	0	-0.002	0.016	22.215	0.643	0.643	0.000	0.000	0.000	0.000
75	A	83	LEU	0	-0.043	-0.019	24.171	-0.239	-0.239	0.000	0.000	0.000	0.000
76	A	84	ASN	0	-0.018	-0.005	26.262	0.494	0.494	0.000	0.000	0.000	0.000
77	A	85	ALA	0	0.057	0.024	22.197	-0.105	-0.105	0.000	0.000	0.000	0.000
78	A	86	VAL	0	-0.049	-0.016	17.708	0.417	0.417	0.000	0.000	0.000	0.000
79	A	87	ARG	1	0.911	0.963	16.776	28.584	28.584	0.000	0.000	0.000	0.000
80	A	88	LEU	0	0.012	0.000	12.594	0.919	0.919	0.000	0.000	0.000	0.000
81	A	89	LEU	0	0.021	0.032	9.998	-1.772	-1.772	0.000	0.000	0.000	0.000
82	A	90	VAL	0	0.027	0.002	6.912	1.158	1.158	0.000	0.000	0.000	0.000
88	A	96	ASP	-1	-0.908	-0.940	6.482	-75.148	-75.148	0.000	0.000	0.000	0.000
89	A	97	GLU	-1	-1.045	-1.016	8.257	-37.065	-37.065	0.000	0.000	0.000	0.000
90	A	98	GLN	0	-0.045	-0.028	11.627	-1.926	-1.926	0.000	0.000	0.000	0.000
91	A	99	LEU	-1	-0.951	-0.968	13.647	-32.545	-32.545	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:ARG)