FMO DATABASE

FMODB ID: LVV79

Calculation Name: 2OSH-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2OSH

Chain ID: A

ChEMBL ID:

UniProt ID: A4FS04

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	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-952636.53952
FMO2-HF: Nuclear repulsion	902768.950546
FMO2-HF: Total energy	-49867.588974
FMO2-MP2: Total energy	-49999.694068

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:ASN)

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

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.
-174.582	-163.02	43.322	-23.998	-30.888	-0.152

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.756 / q_NPA : 0.891

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	TYR	0	0.035	0.026	2.376	3.452	5.875	3.163	-2.157	-3.428	0.020
4	A	4	GLN	0	-0.017	-0.012	1.914	-34.727	-35.387	14.840	-6.047	-8.134	-0.005
5	A	5	PHE	0	0.050	0.036	3.779	5.332	6.082	0.021	-0.353	-0.418	0.002
6	A	6	LYS	1	0.914	0.955	5.391	30.523	30.634	-0.001	-0.007	-0.103	0.000
50	A	51	TYR	0	-0.058	-0.082	4.404	-2.035	-1.939	-0.001	-0.009	-0.086	0.000
61	A	62	PRO	0	-0.016	0.003	4.536	-9.560	-9.306	-0.001	-0.039	-0.214	0.000
62	A	63	TYR	0	0.019	0.006	2.398	-22.346	-19.558	1.464	-2.126	-2.126	-0.026
63	A	64	PHE	0	0.016	-0.001	2.549	-13.786	-10.831	1.650	-2.221	-2.384	-0.027
64	A	65	LYS	1	0.907	0.965	2.653	34.877	37.109	1.707	-1.549	-2.390	-0.018
65	A	66	THR	0	0.001	-0.001	1.840	-49.626	-51.709	15.744	-6.405	-7.256	-0.068
66	A	67	TYR	0	-0.055	-0.047	2.238	11.008	11.768	4.663	-2.007	-3.417	-0.019
67	A	68	SER	0	0.001	0.000	5.178	0.428	0.426	-0.001	0.000	0.004	0.000
86	A	89	VAL	0	0.023	0.006	3.303	-1.281	-0.976	0.019	-0.096	-0.229	-0.001
88	A	93	ASP	-1	-0.722	-0.807	2.927	-72.992	-71.359	0.055	-0.982	-0.707	-0.010
7	A	7	ASN	0	-0.060	-0.053	5.974	5.130	5.130	0.000	0.000	0.000	0.000
8	A	8	MET	0	-0.064	-0.013	5.664	3.131	3.131	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.041	0.027	9.115	2.605	2.605	0.000	0.000	0.000	0.000
10	A	10	GLN	0	0.003	0.004	10.643	0.484	0.484	0.000	0.000	0.000	0.000
11	A	11	CYS	0	-0.052	0.004	11.363	1.437	1.437	0.000	0.000	0.000	0.000
12	A	12	THR	0	-0.043	-0.046	12.880	1.019	1.019	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.008	0.009	15.031	1.244	1.244	0.000	0.000	0.000	0.000
14	A	14	PRO	0	-0.012	0.000	16.938	0.135	0.135	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.054	-0.023	17.839	0.336	0.336	0.000	0.000	0.000	0.000
16	A	16	ARG	1	0.849	0.918	18.371	14.509	14.509	0.000	0.000	0.000	0.000
17	A	17	SER	0	-0.018	-0.033	16.764	-0.514	-0.514	0.000	0.000	0.000	0.000
18	A	18	TRP	0	0.017	-0.014	10.680	-0.577	-0.577	0.000	0.000	0.000	0.000
19	A	19	CYS	0	-0.030	-0.022	13.758	-0.863	-0.863	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.740	-0.802	15.256	-14.932	-14.932	0.000	0.000	0.000	0.000
21	A	21	PHE	0	0.053	0.008	13.711	0.469	0.469	0.000	0.000	0.000	0.000
22	A	22	ALA	0	-0.088	-0.047	12.908	-1.290	-1.290	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.885	-0.942	14.163	-15.688	-15.688	0.000	0.000	0.000	0.000
24	A	24	TYR	0	-0.058	-0.057	17.261	0.944	0.944	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.010	0.004	18.239	-0.619	-0.619	0.000	0.000	0.000	0.000
26	A	26	CYS	0	-0.068	-0.023	20.064	0.272	0.272	0.000	0.000	0.000	0.000
27	A	27	TYR	0	-0.054	-0.027	15.473	-0.561	-0.561	0.000	0.000	0.000	0.000
28	A	28	CYS	0	-0.098	-0.014	13.476	-3.234	-3.234	0.000	0.000	0.000	0.000
29	A	29	GLY	0	0.099	0.054	12.461	0.858	0.858	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.864	0.925	12.035	22.228	22.228	0.000	0.000	0.000	0.000
31	A	31	GLY	0	-0.037	-0.023	11.733	-2.058	-2.058	0.000	0.000	0.000	0.000
32	A	32	GLY	0	0.044	0.014	13.498	-0.033	-0.033	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.081	-0.053	16.854	-0.033	-0.033	0.000	0.000	0.000	0.000
34	A	34	GLY	0	0.084	0.058	20.581	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	35	THR	0	-0.054	-0.022	22.786	-0.401	-0.401	0.000	0.000	0.000	0.000
36	A	36	PRO	0	-0.040	-0.007	20.595	0.086	0.086	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.010	-0.019	22.571	0.529	0.529	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.804	-0.873	22.002	-13.199	-13.199	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.805	-0.907	22.148	-12.951	-12.951	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.003	0.013	16.389	-0.804	-0.804	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.700	-0.857	17.343	-16.684	-16.684	0.000	0.000	0.000	0.000
42	A	42	ARG	1	0.852	0.917	18.089	12.195	12.195	0.000	0.000	0.000	0.000
43	A	43	CYS	0	-0.084	-0.019	14.428	1.092	1.092	0.000	0.000	0.000	0.000
44	A	45	GLN	0	0.051	0.026	13.868	-0.886	-0.886	0.000	0.000	0.000	0.000
45	A	46	VAL	0	-0.041	-0.022	14.138	-0.471	-0.471	0.000	0.000	0.000	0.000
46	A	47	HIS	1	0.781	0.878	6.459	34.407	34.407	0.000	0.000	0.000	0.000
47	A	48	ASP	-1	-0.825	-0.907	10.474	-27.592	-27.592	0.000	0.000	0.000	0.000
48	A	49	ASN	0	0.014	-0.005	11.972	-0.488	-0.488	0.000	0.000	0.000	0.000
49	A	50	CYS	0	-0.045	0.002	6.987	2.108	2.108	0.000	0.000	0.000	0.000
51	A	52	ASN	0	0.003	-0.009	9.542	-1.018	-1.018	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.851	-0.895	12.792	-17.247	-17.247	0.000	0.000	0.000	0.000
53	A	54	ALA	0	-0.019	-0.020	9.187	0.338	0.338	0.000	0.000	0.000	0.000
54	A	55	GLU	-1	-0.864	-0.959	9.384	-29.963	-29.963	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.799	0.902	11.595	19.071	19.071	0.000	0.000	0.000	0.000
56	A	57	ILE	0	-0.063	-0.024	11.193	1.285	1.285	0.000	0.000	0.000	0.000
57	A	58	SER	0	0.001	-0.014	12.864	-1.363	-1.363	0.000	0.000	0.000	0.000
58	A	59	GLY	0	0.001	-0.001	12.202	-0.410	-0.410	0.000	0.000	0.000	0.000
59	A	60	CYS	0	-0.085	-0.004	8.166	-6.692	-6.692	0.000	0.000	0.000	0.000
60	A	61	TRP	0	0.107	0.060	7.284	0.186	0.186	0.000	0.000	0.000	0.000
68	A	69	TYR	0	0.046	0.003	5.898	-1.083	-1.083	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.876	-0.923	8.876	-18.577	-18.577	0.000	0.000	0.000	0.000
70	A	72	SER	0	-0.011	-0.024	12.856	0.759	0.759	0.000	0.000	0.000	0.000
71	A	73	GLN	0	-0.015	-0.016	16.637	0.164	0.164	0.000	0.000	0.000	0.000
72	A	74	GLY	0	0.043	0.032	17.886	0.505	0.505	0.000	0.000	0.000	0.000
73	A	75	THR	0	-0.037	-0.002	16.446	0.016	0.016	0.000	0.000	0.000	0.000
74	A	76	LEU	0	0.001	-0.011	9.455	-0.890	-0.890	0.000	0.000	0.000	0.000
75	A	77	THR	0	-0.005	-0.006	12.280	0.432	0.432	0.000	0.000	0.000	0.000
76	A	78	CYS	0	-0.044	-0.018	5.049	-4.988	-4.988	0.000	0.000	0.000	0.000
77	A	79	LYS	1	0.865	0.942	10.560	26.570	26.570	0.000	0.000	0.000	0.000
78	A	80	GLY	0	0.057	0.030	12.252	-0.846	-0.846	0.000	0.000	0.000	0.000
79	A	81	GLY	0	-0.006	-0.014	13.499	-0.732	-0.732	0.000	0.000	0.000	0.000
80	A	82	ASN	0	-0.048	-0.025	8.311	-4.380	-4.380	0.000	0.000	0.000	0.000
81	A	83	ASN	0	0.046	0.021	10.021	-0.216	-0.216	0.000	0.000	0.000	0.000
82	A	84	ALA	0	0.063	0.016	10.554	-2.026	-2.026	0.000	0.000	0.000	0.000
83	A	86	ALA	0	0.001	-0.014	6.050	-4.074	-4.074	0.000	0.000	0.000	0.000
84	A	87	ALA	0	-0.017	-0.009	6.580	-3.957	-3.957	0.000	0.000	0.000	0.000
85	A	88	ALA	0	0.039	0.030	9.176	-0.392	-0.392	0.000	0.000	0.000	0.000
87	A	91	ASP	-1	-0.820	-0.917	5.933	-22.743	-22.743	0.000	0.000	0.000	0.000
89	A	94	ARG	1	0.912	0.930	6.562	26.448	26.448	0.000	0.000	0.000	0.000
90	A	95	LEU	0	-0.041	-0.017	9.324	2.580	2.580	0.000	0.000	0.000	0.000
91	A	96	ALA	0	0.012	0.017	9.617	1.756	1.756	0.000	0.000	0.000	0.000
92	A	97	ALA	0	0.021	0.012	9.654	1.643	1.643	0.000	0.000	0.000	0.000
93	A	98	ILE	0	-0.013	0.001	11.569	1.777	1.777	0.000	0.000	0.000	0.000
94	A	100	PHE	0	0.009	-0.034	11.923	0.620	0.620	0.000	0.000	0.000	0.000
95	A	101	ALA	0	-0.009	0.005	15.894	0.698	0.698	0.000	0.000	0.000	0.000
96	A	102	GLY	0	-0.044	-0.009	18.002	0.834	0.834	0.000	0.000	0.000	0.000
97	A	103	ALA	0	-0.017	-0.003	19.211	0.733	0.733	0.000	0.000	0.000	0.000
98	A	104	PRO	0	-0.026	-0.006	21.019	-0.077	-0.077	0.000	0.000	0.000	0.000
99	A	105	TYR	0	-0.044	-0.044	18.866	-0.024	-0.024	0.000	0.000	0.000	0.000
100	A	106	THR	0	-0.004	-0.009	22.894	0.769	0.769	0.000	0.000	0.000	0.000
101	A	107	ASP	-1	-0.836	-0.939	24.701	-12.251	-12.251	0.000	0.000	0.000	0.000
102	A	108	ALA	0	-0.057	-0.025	25.755	-0.091	-0.091	0.000	0.000	0.000	0.000
103	A	109	ASN	0	-0.046	-0.042	23.343	0.507	0.507	0.000	0.000	0.000	0.000
104	A	110	TYR	0	-0.018	-0.002	18.494	-0.350	-0.350	0.000	0.000	0.000	0.000
105	A	111	ASN	0	-0.060	-0.015	21.144	0.610	0.610	0.000	0.000	0.000	0.000
106	A	112	ILE	0	-0.030	-0.003	22.491	0.833	0.833	0.000	0.000	0.000	0.000
107	A	113	ASP	-1	-0.856	-0.945	23.463	-11.501	-11.501	0.000	0.000	0.000	0.000
108	A	114	LEU	0	0.050	0.011	19.223	0.276	0.276	0.000	0.000	0.000	0.000
109	A	115	LYS	1	0.909	0.955	23.608	11.586	11.586	0.000	0.000	0.000	0.000
110	A	116	ALA	0	-0.016	0.000	26.404	0.280	0.280	0.000	0.000	0.000	0.000
111	A	117	ARG	1	0.891	0.944	26.225	11.578	11.578	0.000	0.000	0.000	0.000
112	A	119	GLN	-1	-0.903	-0.930	23.663	-12.140	-12.140	0.000	0.000	0.000	0.000

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