FMO DATABASE

FMODB ID: 2GV9R

Calculation Name: 1OSY-A-Xray549

Preferred Name:

Target Type:

Ligand Name: bromide ion | acetyl group

Ligand 3-letter code: BR | ACE

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1OSY

Chain ID: A

ChEMBL ID:

UniProt ID: P80412

Base Structure: X-ray

Registration Date: 2025-10-11

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-867650.950973
FMO2-HF: Nuclear repulsion	824111.22817
FMO2-HF: Total energy	-43539.722803
FMO2-MP2: Total energy	-43670.40772

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:SER)

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

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.
-8.226	-3.804	8.099	-5.454	-7.065	-0.023

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.875 / q_NPA : 0.923

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	THR	0	0.051	0.035	2.834	2.097	4.390	0.273	-1.043	-1.523	0.001
4	A	4	SER	0	0.023	0.018	1.946	-20.632	-19.800	7.790	-4.007	-4.615	-0.023
5	A	5	LEU	0	0.031	0.015	2.989	7.928	9.054	0.038	-0.390	-0.774	-0.001
6	A	6	THR	0	0.016	0.005	5.299	8.355	8.509	-0.001	-0.011	-0.141	0.000
8	A	8	GLN	0	-0.015	-0.010	5.073	-4.279	-4.262	-0.001	-0.003	-0.012	0.000
7	A	7	PHE	0	0.018	-0.002	7.023	3.851	3.851	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.032	0.020	8.885	3.133	3.133	0.000	0.000	0.000	0.000
10	A	10	ALA	0	0.013	0.008	10.994	2.407	2.407	0.000	0.000	0.000	0.000
11	A	11	TYR	0	-0.013	-0.007	12.065	2.211	2.211	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.005	0.006	12.068	1.760	1.760	0.000	0.000	0.000	0.000
13	A	13	VAL	0	0.028	0.004	14.776	1.269	1.269	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.830	0.933	16.244	18.326	18.326	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.916	0.944	17.729	14.940	14.940	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.034	-0.010	14.073	0.573	0.573	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.876	-0.943	17.493	-14.955	-14.955	0.000	0.000	0.000	0.000
18	A	18	PHE	0	-0.007	-0.008	12.436	0.412	0.412	0.000	0.000	0.000	0.000
19	A	19	ASP	-1	-0.822	-0.893	17.657	-16.978	-16.978	0.000	0.000	0.000	0.000
20	A	20	TYR	0	0.052	0.025	15.788	0.670	0.670	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.026	-0.036	17.249	-0.637	-0.637	0.000	0.000	0.000	0.000
22	A	22	PRO	0	-0.027	-0.012	16.914	0.912	0.912	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.035	-0.025	19.907	0.636	0.636	0.000	0.000	0.000	0.000
24	A	24	TRP	0	0.021	-0.001	19.541	0.591	0.591	0.000	0.000	0.000	0.000
25	A	25	GLY	0	0.020	0.028	25.281	0.275	0.275	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.735	0.836	27.473	10.615	10.615	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.067	0.048	31.584	0.144	0.144	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.078	-0.028	34.971	0.120	0.120	0.000	0.000	0.000	0.000
29	A	29	PRO	0	0.031	0.001	38.057	0.117	0.117	0.000	0.000	0.000	0.000
30	A	30	SER	0	0.051	0.018	34.147	-0.145	-0.145	0.000	0.000	0.000	0.000
31	A	31	SER	0	0.012	0.010	32.986	-0.245	-0.245	0.000	0.000	0.000	0.000
32	A	32	TYR	0	-0.053	-0.015	32.302	-0.203	-0.203	0.000	0.000	0.000	0.000
33	A	33	ILE	0	0.003	0.003	26.254	0.021	0.021	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.799	-0.928	29.676	-9.253	-9.253	0.000	0.000	0.000	0.000
35	A	35	ASN	0	-0.049	-0.025	28.497	-0.158	-0.158	0.000	0.000	0.000	0.000
36	A	36	LEU	0	0.007	0.031	20.659	-0.188	-0.188	0.000	0.000	0.000	0.000
37	A	37	THR	0	-0.018	0.008	24.874	0.260	0.260	0.000	0.000	0.000	0.000
38	A	38	PHE	0	0.023	0.014	18.626	-0.540	-0.540	0.000	0.000	0.000	0.000
39	A	39	PRO	0	-0.007	-0.007	20.869	0.587	0.587	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.829	0.917	21.524	14.489	14.489	0.000	0.000	0.000	0.000
41	A	41	VAL	0	0.017	0.023	20.695	-0.970	-0.970	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.008	-0.011	16.523	0.318	0.318	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.012	-0.021	21.030	0.465	0.465	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.818	-0.870	21.660	-14.130	-14.130	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.856	0.917	20.462	15.126	15.126	0.000	0.000	0.000	0.000
46	A	46	LYS	1	0.857	0.929	25.231	10.462	10.462	0.000	0.000	0.000	0.000
47	A	47	TYR	0	-0.060	-0.059	19.555	-0.223	-0.223	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.010	0.008	23.792	0.724	0.724	0.000	0.000	0.000	0.000
49	A	49	TYR	0	0.002	-0.018	20.664	-0.995	-0.995	0.000	0.000	0.000	0.000
50	A	50	ARG	1	0.822	0.904	22.839	13.505	13.505	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.008	0.007	23.297	-0.586	-0.586	0.000	0.000	0.000	0.000
52	A	52	VAL	0	0.021	0.019	23.213	0.434	0.434	0.000	0.000	0.000	0.000
53	A	53	VAL	0	-0.001	-0.005	24.410	-0.345	-0.345	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.028	-0.029	25.862	0.043	0.043	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.030	0.018	24.872	0.205	0.205	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.009	0.005	25.826	0.193	0.193	0.000	0.000	0.000	0.000
57	A	57	ASP	-1	-0.826	-0.910	27.122	-11.857	-11.857	0.000	0.000	0.000	0.000
58	A	58	LEU	0	-0.056	-0.026	28.141	0.467	0.467	0.000	0.000	0.000	0.000
59	A	59	GLY	0	0.019	0.017	28.769	0.338	0.338	0.000	0.000	0.000	0.000
60	A	60	VAL	0	-0.039	-0.039	25.800	-0.454	-0.454	0.000	0.000	0.000	0.000
61	A	61	GLU	-1	-0.908	-0.943	27.785	-9.374	-9.374	0.000	0.000	0.000	0.000
62	A	62	SER	0	0.014	-0.014	27.642	-0.414	-0.414	0.000	0.000	0.000	0.000
63	A	63	ASN	0	-0.025	0.007	29.324	-0.264	-0.264	0.000	0.000	0.000	0.000
64	A	64	PHE	0	0.015	0.005	27.723	0.231	0.231	0.000	0.000	0.000	0.000
65	A	65	ALA	0	0.012	0.006	29.841	-0.220	-0.220	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.010	0.013	27.241	-0.238	-0.238	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.003	-0.005	29.547	0.312	0.312	0.000	0.000	0.000	0.000
68	A	68	PRO	0	0.019	-0.010	30.032	-0.288	-0.288	0.000	0.000	0.000	0.000
69	A	69	SER	0	-0.027	-0.006	27.912	0.087	0.087	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.016	0.009	25.867	-0.465	-0.465	0.000	0.000	0.000	0.000
71	A	71	GLY	0	0.021	0.034	25.292	-0.518	-0.518	0.000	0.000	0.000	0.000
72	A	72	GLN	0	0.004	-0.008	24.992	-0.058	-0.058	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.012	-0.021	25.600	-0.348	-0.348	0.000	0.000	0.000	0.000
74	A	74	ILE	0	-0.007	0.010	23.105	0.416	0.416	0.000	0.000	0.000	0.000
75	A	75	ASN	0	0.007	-0.014	27.303	-0.097	-0.097	0.000	0.000	0.000	0.000
76	A	76	PHE	0	0.011	-0.015	24.325	0.022	0.022	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.005	0.021	30.262	0.108	0.108	0.000	0.000	0.000	0.000
78	A	78	GLN	0	-0.027	0.000	32.665	0.306	0.306	0.000	0.000	0.000	0.000
79	A	79	TYR	0	0.011	-0.003	26.723	0.152	0.152	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.087	-0.056	31.885	0.161	0.161	0.000	0.000	0.000	0.000
81	A	81	LYS	1	0.903	0.937	33.826	8.677	8.677	0.000	0.000	0.000	0.000
82	A	82	GLY	0	0.031	0.021	36.733	0.247	0.247	0.000	0.000	0.000	0.000
83	A	83	TYR	0	-0.020	-0.002	36.665	0.156	0.156	0.000	0.000	0.000	0.000
84	A	84	GLY	0	0.083	0.050	32.826	-0.255	-0.255	0.000	0.000	0.000	0.000
85	A	85	VAL	0	-0.056	-0.037	28.640	0.209	0.209	0.000	0.000	0.000	0.000
86	A	86	ALA	0	-0.010	-0.002	30.660	-0.110	-0.110	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.733	-0.849	28.190	-10.742	-10.742	0.000	0.000	0.000	0.000
88	A	88	THR	0	0.014	0.012	27.543	-0.398	-0.398	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.898	0.967	27.696	9.743	9.743	0.000	0.000	0.000	0.000
90	A	90	THR	0	-0.005	-0.005	21.403	-0.434	-0.434	0.000	0.000	0.000	0.000
91	A	91	ILE	0	-0.040	-0.023	23.036	0.435	0.435	0.000	0.000	0.000	0.000
92	A	92	GLN	0	-0.042	-0.014	18.464	-0.151	-0.151	0.000	0.000	0.000	0.000
93	A	93	VAL	0	0.027	0.007	19.672	0.757	0.757	0.000	0.000	0.000	0.000
94	A	94	PHE	0	0.044	0.017	17.651	-1.147	-1.147	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.003	0.003	16.820	0.916	0.916	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.006	-0.006	18.844	-0.628	-0.628	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.016	-0.002	17.859	0.324	0.324	0.000	0.000	0.000	0.000
98	A	98	PRO	0	-0.003	-0.001	21.784	0.464	0.464	0.000	0.000	0.000	0.000
99	A	99	ASP	-1	-0.861	-0.951	24.871	-11.185	-11.185	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.024	0.034	21.976	0.276	0.276	0.000	0.000	0.000	0.000
101	A	101	GLY	0	-0.015	-0.002	25.136	-0.064	-0.064	0.000	0.000	0.000	0.000
102	A	102	ASN	0	-0.044	-0.035	24.731	0.011	0.011	0.000	0.000	0.000	0.000
103	A	103	SER	0	-0.029	-0.016	23.563	-0.285	-0.285	0.000	0.000	0.000	0.000
104	A	104	GLU	-1	-0.827	-0.881	17.787	-17.075	-17.075	0.000	0.000	0.000	0.000
105	A	105	GLU	-1	-0.838	-0.914	18.497	-13.888	-13.888	0.000	0.000	0.000	0.000
106	A	106	TYR	0	-0.083	-0.060	12.802	-1.531	-1.531	0.000	0.000	0.000	0.000
107	A	107	ILE	0	-0.048	-0.014	13.080	0.832	0.832	0.000	0.000	0.000	0.000
108	A	108	ILE	0	-0.051	-0.023	13.962	-1.449	-1.449	0.000	0.000	0.000	0.000
109	A	109	ALA	0	-0.005	-0.007	15.907	-0.205	-0.205	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.821	-0.903	16.859	-16.539	-16.539	0.000	0.000	0.000	0.000
111	A	111	TRP	0	-0.046	-0.017	18.374	-0.216	-0.216	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.897	0.903	18.562	16.064	16.064	0.000	0.000	0.000	0.000
113	A	113	LYS	1	0.818	0.922	21.744	10.705	10.705	0.000	0.000	0.000	0.000
114	A	114	THR	-1	-0.918	-0.948	21.282	-12.457	-12.457	0.000	0.000	0.000	0.000

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