FMO DATABASE

FMODB ID: 6R31Z

Calculation Name: 2V3S-A-Xray549

Preferred Name: Serine/threonine-protein kinase OSR1

Target Type: SINGLE PROTEIN

Ligand Name: acetate ion

Ligand 3-letter code: ACT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2V3S

Chain ID: A

ChEMBL ID: CHEMBL1163104

UniProt ID: O95747

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	96
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-643599.102789
FMO2-HF: Nuclear repulsion	608164.567339
FMO2-HF: Total energy	-35434.53545
FMO2-MP2: Total energy	-35540.540377

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:432:GLY)

Summations of interaction energy for fragment #1(A:432: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.
-120.395	-124.816	9.881	-0.63	-4.829	-0.066

Interaction energy analysis for fragmet #1(A:432:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.814 / q_NPA : 0.911

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	434	ILE	0	-0.026	-0.010	2.179	-19.935	-24.755	6.693	1.729	-3.602	-0.056
4	A	435	SER	0	0.029	0.021	4.061	5.338	5.465	0.001	-0.054	-0.074	0.000
24	A	455	THR	0	-0.031	-0.033	3.555	-13.539	-12.988	0.013	-0.272	-0.291	-0.001
25	A	456	PRO	0	0.014	0.003	2.214	3.887	3.570	3.176	-2.017	-0.843	-0.009
26	A	457	GLY	0	-0.003	0.005	4.777	-2.499	-2.495	-0.001	-0.010	0.007	0.000
62	A	493	PRO	0	-0.022	-0.005	4.350	1.809	1.843	-0.001	-0.006	-0.026	0.000
5	A	436	LEU	0	0.004	0.005	7.646	0.124	0.124	0.000	0.000	0.000	0.000
6	A	437	VAL	0	0.003	-0.009	10.084	1.651	1.651	0.000	0.000	0.000	0.000
7	A	438	LEU	0	-0.002	0.012	13.899	-0.078	-0.078	0.000	0.000	0.000	0.000
8	A	439	ARG	1	0.819	0.873	16.185	15.451	15.451	0.000	0.000	0.000	0.000
9	A	440	LEU	0	0.042	0.012	19.659	0.171	0.171	0.000	0.000	0.000	0.000
10	A	441	ARG	1	0.808	0.890	22.693	11.036	11.036	0.000	0.000	0.000	0.000
11	A	442	ASN	0	0.038	0.019	26.174	0.220	0.220	0.000	0.000	0.000	0.000
12	A	443	SER	0	0.046	0.003	27.367	0.181	0.181	0.000	0.000	0.000	0.000
13	A	444	LYS	1	0.785	0.884	30.680	9.745	9.745	0.000	0.000	0.000	0.000
14	A	445	LYS	1	0.853	0.907	30.411	9.153	9.153	0.000	0.000	0.000	0.000
15	A	446	GLU	-1	-0.800	-0.860	29.169	-10.056	-10.056	0.000	0.000	0.000	0.000
16	A	447	LEU	0	-0.009	-0.002	24.349	-0.238	-0.238	0.000	0.000	0.000	0.000
17	A	448	ASN	0	-0.027	-0.023	22.602	0.327	0.327	0.000	0.000	0.000	0.000
18	A	449	ASP	-1	-0.764	-0.837	18.529	-15.889	-15.889	0.000	0.000	0.000	0.000
19	A	450	ILE	0	0.028	0.012	16.276	-0.038	-0.038	0.000	0.000	0.000	0.000
20	A	451	ARG	1	0.871	0.933	13.971	16.207	16.207	0.000	0.000	0.000	0.000
21	A	452	PHE	0	-0.006	-0.003	10.476	0.876	0.876	0.000	0.000	0.000	0.000
22	A	453	GLU	-1	-0.924	-0.958	7.064	-34.971	-34.971	0.000	0.000	0.000	0.000
23	A	454	PHE	0	0.018	0.009	5.186	2.719	2.719	0.000	0.000	0.000	0.000
27	A	458	ARG	1	0.820	0.917	7.248	33.692	33.692	0.000	0.000	0.000	0.000
28	A	459	ASP	-1	-0.745	-0.858	7.772	-29.507	-29.507	0.000	0.000	0.000	0.000
29	A	460	THR	0	0.013	-0.013	9.276	-0.511	-0.511	0.000	0.000	0.000	0.000
30	A	461	ALA	0	0.037	0.022	11.610	0.429	0.429	0.000	0.000	0.000	0.000
31	A	462	GLU	-1	-0.839	-0.918	12.666	-14.656	-14.656	0.000	0.000	0.000	0.000
32	A	463	GLY	0	0.012	0.009	15.018	0.693	0.693	0.000	0.000	0.000	0.000
33	A	464	VAL	0	0.062	0.024	10.475	0.585	0.585	0.000	0.000	0.000	0.000
34	A	465	SER	0	-0.018	-0.028	13.868	0.686	0.686	0.000	0.000	0.000	0.000
35	A	466	GLN	0	-0.056	-0.031	16.650	0.870	0.870	0.000	0.000	0.000	0.000
36	A	467	GLU	-1	-0.934	-0.957	14.244	-19.327	-19.327	0.000	0.000	0.000	0.000
37	A	468	LEU	0	-0.004	-0.002	14.963	0.873	0.873	0.000	0.000	0.000	0.000
38	A	469	ILE	0	-0.039	-0.007	18.484	0.727	0.727	0.000	0.000	0.000	0.000
39	A	470	SER	0	-0.089	-0.047	20.511	0.624	0.624	0.000	0.000	0.000	0.000
40	A	471	ALA	0	-0.013	-0.008	20.264	0.496	0.496	0.000	0.000	0.000	0.000
41	A	472	GLY	0	-0.026	-0.010	22.210	0.276	0.276	0.000	0.000	0.000	0.000
42	A	473	LEU	0	-0.067	-0.033	18.906	0.193	0.193	0.000	0.000	0.000	0.000
43	A	474	VAL	0	-0.010	-0.010	19.157	-0.211	-0.211	0.000	0.000	0.000	0.000
44	A	475	ASP	-1	-0.763	-0.851	22.446	-10.520	-10.520	0.000	0.000	0.000	0.000
45	A	476	GLY	0	0.050	0.010	24.299	-0.402	-0.402	0.000	0.000	0.000	0.000
46	A	477	ARG	1	0.798	0.876	25.544	10.080	10.080	0.000	0.000	0.000	0.000
47	A	478	ASP	-1	-0.744	-0.856	22.523	-12.291	-12.291	0.000	0.000	0.000	0.000
48	A	479	LEU	0	-0.006	0.015	19.397	-0.560	-0.560	0.000	0.000	0.000	0.000
49	A	480	VAL	0	0.044	0.017	19.760	-0.752	-0.752	0.000	0.000	0.000	0.000
50	A	481	ILE	0	-0.030	-0.004	20.159	-0.580	-0.580	0.000	0.000	0.000	0.000
51	A	482	VAL	0	0.022	0.013	16.515	-0.636	-0.636	0.000	0.000	0.000	0.000
52	A	483	ALA	0	0.057	0.034	15.611	-1.253	-1.253	0.000	0.000	0.000	0.000
53	A	484	ALA	0	-0.016	-0.010	15.212	-1.244	-1.244	0.000	0.000	0.000	0.000
54	A	485	ASN	0	-0.069	-0.051	15.886	-0.902	-0.902	0.000	0.000	0.000	0.000
55	A	486	LEU	0	-0.005	0.002	10.105	-1.394	-1.394	0.000	0.000	0.000	0.000
56	A	487	GLN	0	-0.045	-0.046	10.845	-2.550	-2.550	0.000	0.000	0.000	0.000
57	A	488	LYS	1	0.943	0.986	11.160	16.180	16.180	0.000	0.000	0.000	0.000
58	A	489	ILE	0	-0.066	-0.028	9.783	-0.922	-0.922	0.000	0.000	0.000	0.000
59	A	490	VAL	0	-0.028	-0.019	6.398	-3.746	-3.746	0.000	0.000	0.000	0.000
60	A	491	GLU	-1	-0.909	-0.930	6.209	-28.777	-28.777	0.000	0.000	0.000	0.000
61	A	492	GLU	-1	-0.868	-0.921	7.881	-29.407	-29.407	0.000	0.000	0.000	0.000
63	A	494	GLN	0	-0.059	-0.055	6.995	2.160	2.160	0.000	0.000	0.000	0.000
64	A	495	SER	0	-0.015	0.005	9.071	3.373	3.373	0.000	0.000	0.000	0.000
65	A	496	ASN	0	-0.049	-0.031	11.264	3.628	3.628	0.000	0.000	0.000	0.000
66	A	497	ARG	1	0.900	0.933	10.343	24.691	24.691	0.000	0.000	0.000	0.000
67	A	498	SER	0	-0.003	-0.009	12.945	-0.111	-0.111	0.000	0.000	0.000	0.000
68	A	499	VAL	0	-0.020	0.001	14.825	0.618	0.618	0.000	0.000	0.000	0.000
69	A	500	THR	0	0.028	0.015	17.225	-0.034	-0.034	0.000	0.000	0.000	0.000
70	A	501	PHE	0	-0.012	-0.008	17.329	0.296	0.296	0.000	0.000	0.000	0.000
71	A	502	LYS	1	0.961	0.981	22.299	10.843	10.843	0.000	0.000	0.000	0.000
72	A	503	LEU	0	-0.014	-0.005	22.321	-0.491	-0.491	0.000	0.000	0.000	0.000
73	A	504	ALA	0	-0.002	-0.010	25.563	0.467	0.467	0.000	0.000	0.000	0.000
74	A	505	SER	0	-0.112	-0.090	26.279	0.543	0.543	0.000	0.000	0.000	0.000
75	A	506	GLY	0	0.005	-0.005	28.924	0.328	0.328	0.000	0.000	0.000	0.000
76	A	507	VAL	0	-0.055	-0.018	30.246	0.101	0.101	0.000	0.000	0.000	0.000
77	A	508	GLU	-1	-0.896	-0.958	32.367	-9.115	-9.115	0.000	0.000	0.000	0.000
78	A	509	GLY	0	0.031	0.037	33.893	0.260	0.260	0.000	0.000	0.000	0.000
79	A	510	SER	0	-0.071	-0.055	34.919	0.024	0.024	0.000	0.000	0.000	0.000
80	A	511	ASP	-1	-0.882	-0.905	34.122	-8.795	-8.795	0.000	0.000	0.000	0.000
81	A	512	ILE	0	-0.016	-0.016	35.185	-0.070	-0.070	0.000	0.000	0.000	0.000
82	A	513	PRO	0	-0.032	-0.015	30.561	-0.124	-0.124	0.000	0.000	0.000	0.000
83	A	514	ASP	-1	-0.843	-0.913	30.625	-9.728	-9.728	0.000	0.000	0.000	0.000
84	A	515	ASP	-1	-0.883	-0.946	26.150	-11.666	-11.666	0.000	0.000	0.000	0.000
85	A	516	GLY	0	0.027	0.017	26.523	-0.398	-0.398	0.000	0.000	0.000	0.000
86	A	517	LYS	1	0.818	0.897	28.068	9.185	9.185	0.000	0.000	0.000	0.000
87	A	518	LEU	0	-0.006	0.008	22.577	-0.075	-0.075	0.000	0.000	0.000	0.000
88	A	519	ILE	0	0.011	0.004	26.552	0.039	0.039	0.000	0.000	0.000	0.000
89	A	520	GLY	0	0.070	0.029	28.671	0.131	0.131	0.000	0.000	0.000	0.000
90	A	521	PHE	0	-0.047	-0.022	24.828	-0.067	-0.067	0.000	0.000	0.000	0.000
91	A	522	ALA	0	0.001	0.011	20.499	0.146	0.146	0.000	0.000	0.000	0.000
92	A	523	GLN	0	-0.024	-0.022	17.737	-0.309	-0.309	0.000	0.000	0.000	0.000
93	A	524	LEU	0	0.007	0.019	12.730	-0.178	-0.178	0.000	0.000	0.000	0.000
94	A	525	SER	0	-0.037	-0.025	13.671	0.461	0.461	0.000	0.000	0.000	0.000
95	A	526	ILE	0	-0.022	-0.005	7.601	-1.448	-1.448	0.000	0.000	0.000	0.000
96	A	527	SER	-1	-0.884	-0.926	10.066	-22.988	-22.988	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:432:GLY)