FMO DATABASE

FMODB ID: LG929

Calculation Name: 5FEA-B-Xray547

Preferred Name:

Target Type:

Ligand Name: bromosporine | bromide ion

Ligand 3-letter code: BMF | BR

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5FEA

Chain ID: B

ChEMBL ID:

UniProt ID: E9BU61

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	121
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-872132.61908
FMO2-HF: Nuclear repulsion	822359.577604
FMO2-HF: Total energy	-49773.041476
FMO2-MP2: Total energy	-49916.894001

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:33:LYS)

Summations of interaction energy for fragment #1(A:33:LYS)

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.
-341.386	-334.082	32.559	-20.349	-19.512	-0.212

Interaction energy analysis for fragmet #1(A:33:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.730 / q_NPA : 1.852

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	35	ALA	0	0.020	0.010	2.813	-8.713	-6.170	0.344	-1.231	-1.655	-0.009
22	A	54	TYR	0	-0.002	-0.008	2.738	-14.701	-13.037	0.454	-0.709	-1.408	-0.009
25	A	57	TYR	0	-0.024	0.009	2.080	-17.420	-17.707	10.254	-4.477	-5.490	-0.034
26	A	58	ASN	0	-0.084	-0.032	1.748	-59.450	-62.546	13.119	-5.677	-4.345	-0.067
27	A	59	GLU	-1	-0.823	-0.897	3.346	-62.765	-62.287	0.000	-0.197	-0.281	-0.002
35	A	67	ARG	1	0.834	0.937	4.287	75.443	75.629	-0.001	-0.010	-0.175	0.000
36	A	68	GLU	-1	-0.812	-0.922	2.215	-170.792	-164.976	8.389	-8.048	-6.158	-0.091
4	A	36	HIS	0	0.053	0.029	5.462	9.900	9.900	0.000	0.000	0.000	0.000
5	A	37	ARG	1	0.899	0.960	7.225	55.816	55.816	0.000	0.000	0.000	0.000
6	A	38	GLN	0	0.060	0.016	11.045	0.181	0.181	0.000	0.000	0.000	0.000
7	A	39	SER	0	-0.013	-0.005	12.985	1.431	1.431	0.000	0.000	0.000	0.000
8	A	40	LEU	0	0.004	-0.012	13.940	-1.871	-1.871	0.000	0.000	0.000	0.000
9	A	41	GLU	-1	-0.943	-0.953	16.650	-25.352	-25.352	0.000	0.000	0.000	0.000
10	A	42	THR	0	-0.027	-0.016	17.835	-0.232	-0.232	0.000	0.000	0.000	0.000
11	A	43	ILE	0	0.070	0.026	20.513	0.471	0.471	0.000	0.000	0.000	0.000
12	A	44	PRO	0	0.037	0.008	20.549	-1.305	-1.305	0.000	0.000	0.000	0.000
13	A	45	GLU	-1	-0.912	-0.951	19.733	-26.739	-26.739	0.000	0.000	0.000	0.000
14	A	46	VAL	0	0.008	0.003	17.240	-1.380	-1.380	0.000	0.000	0.000	0.000
15	A	47	ALA	0	-0.012	0.001	15.941	-2.602	-2.602	0.000	0.000	0.000	0.000
16	A	48	GLU	-1	-0.877	-0.952	14.855	-37.058	-37.058	0.000	0.000	0.000	0.000
17	A	49	LEU	0	0.024	0.024	14.953	-2.169	-2.169	0.000	0.000	0.000	0.000
18	A	50	TYR	0	-0.035	-0.027	8.702	-2.904	-2.904	0.000	0.000	0.000	0.000
19	A	51	HIS	1	0.836	0.915	10.618	37.247	37.247	0.000	0.000	0.000	0.000
20	A	52	CYS	0	-0.031	-0.013	10.425	-2.964	-2.964	0.000	0.000	0.000	0.000
21	A	53	ILE	0	0.012	0.004	9.113	-2.674	-2.674	0.000	0.000	0.000	0.000
23	A	55	LYS	1	0.853	0.893	5.881	42.258	42.258	0.000	0.000	0.000	0.000
24	A	56	LEU	0	0.010	0.020	7.120	-3.194	-3.194	0.000	0.000	0.000	0.000
28	A	60	GLU	-1	-0.873	-0.918	6.369	-39.091	-39.091	0.000	0.000	0.000	0.000
29	A	61	GLU	-1	-0.873	-0.939	8.538	-57.359	-57.359	0.000	0.000	0.000	0.000
30	A	62	SER	0	-0.044	-0.026	9.917	-0.230	-0.230	0.000	0.000	0.000	0.000
31	A	63	SER	0	-0.033	-0.031	7.480	-0.082	-0.082	0.000	0.000	0.000	0.000
32	A	64	VAL	0	-0.010	-0.002	8.109	-2.801	-2.801	0.000	0.000	0.000	0.000
33	A	65	TRP	0	-0.028	-0.020	9.228	-3.156	-3.156	0.000	0.000	0.000	0.000
34	A	66	PHE	0	-0.033	-0.019	10.415	2.605	2.605	0.000	0.000	0.000	0.000
37	A	69	PRO	0	0.011	0.002	6.002	7.460	7.460	0.000	0.000	0.000	0.000
38	A	70	VAL	0	0.072	0.026	8.847	-0.754	-0.754	0.000	0.000	0.000	0.000
39	A	71	ASN	0	-0.013	-0.011	11.033	-0.351	-0.351	0.000	0.000	0.000	0.000
40	A	72	ALA	0	-0.007	-0.004	7.033	1.407	1.407	0.000	0.000	0.000	0.000
41	A	73	LEU	0	0.004	-0.002	8.441	-0.496	-0.496	0.000	0.000	0.000	0.000
42	A	74	ALA	0	-0.001	-0.002	10.547	1.936	1.936	0.000	0.000	0.000	0.000
43	A	75	GLN	0	-0.023	-0.001	7.560	3.656	3.656	0.000	0.000	0.000	0.000
44	A	76	GLU	-1	-0.837	-0.933	10.912	-44.443	-44.443	0.000	0.000	0.000	0.000
45	A	77	ILE	0	-0.052	-0.017	13.512	2.241	2.241	0.000	0.000	0.000	0.000
46	A	78	PHE	0	-0.039	-0.019	15.364	2.158	2.158	0.000	0.000	0.000	0.000
47	A	79	THR	0	0.066	0.027	13.274	2.043	2.043	0.000	0.000	0.000	0.000
48	A	80	TYR	0	-0.015	-0.008	16.540	1.970	1.970	0.000	0.000	0.000	0.000
49	A	81	TYR	0	-0.025	-0.023	18.921	1.264	1.264	0.000	0.000	0.000	0.000
50	A	82	ASP	-1	-0.888	-0.909	19.117	-28.240	-28.240	0.000	0.000	0.000	0.000
51	A	83	VAL	0	-0.055	-0.027	18.235	1.199	1.199	0.000	0.000	0.000	0.000
52	A	84	VAL	0	-0.052	-0.026	21.462	1.386	1.386	0.000	0.000	0.000	0.000
53	A	85	LYS	1	0.873	0.925	23.992	25.344	25.344	0.000	0.000	0.000	0.000
54	A	86	SER	0	-0.013	-0.005	27.426	0.926	0.926	0.000	0.000	0.000	0.000
55	A	87	PRO	0	0.014	0.032	25.198	-0.013	-0.013	0.000	0.000	0.000	0.000
56	A	88	MET	0	0.030	0.025	27.063	0.702	0.702	0.000	0.000	0.000	0.000
57	A	89	SER	0	-0.015	-0.023	27.220	-0.729	-0.729	0.000	0.000	0.000	0.000
58	A	90	LEU	0	0.068	0.017	28.939	0.633	0.633	0.000	0.000	0.000	0.000
59	A	91	ARG	1	0.871	0.929	30.051	19.340	19.340	0.000	0.000	0.000	0.000
60	A	92	HIS	0	0.017	0.014	31.113	0.776	0.776	0.000	0.000	0.000	0.000
61	A	93	ILE	0	0.050	0.026	32.917	0.493	0.493	0.000	0.000	0.000	0.000
62	A	94	LEU	0	-0.016	-0.011	34.063	0.541	0.541	0.000	0.000	0.000	0.000
63	A	95	ASP	-1	-0.841	-0.916	34.670	-17.253	-17.253	0.000	0.000	0.000	0.000
64	A	96	ASN	0	-0.010	-0.011	36.217	0.491	0.491	0.000	0.000	0.000	0.000
65	A	97	ILE	0	-0.036	-0.020	38.946	0.431	0.431	0.000	0.000	0.000	0.000
66	A	98	VAL	0	-0.067	-0.030	40.402	0.406	0.406	0.000	0.000	0.000	0.000
67	A	99	LYS	1	0.894	0.963	37.326	16.551	16.551	0.000	0.000	0.000	0.000
68	A	100	GLY	0	-0.014	0.009	43.363	0.324	0.324	0.000	0.000	0.000	0.000
69	A	101	ASP	-1	-0.873	-0.928	41.869	-14.848	-14.848	0.000	0.000	0.000	0.000
70	A	102	THR	0	-0.068	-0.039	38.787	-0.039	-0.039	0.000	0.000	0.000	0.000
71	A	103	TYR	0	-0.113	-0.093	36.642	0.011	0.011	0.000	0.000	0.000	0.000
72	A	104	SER	0	-0.002	-0.004	43.451	0.325	0.325	0.000	0.000	0.000	0.000
73	A	105	THR	0	0.006	-0.010	45.283	0.147	0.147	0.000	0.000	0.000	0.000
74	A	106	ALA	0	0.034	0.002	43.273	-0.313	-0.313	0.000	0.000	0.000	0.000
75	A	107	LEU	0	-0.008	-0.003	41.800	-0.383	-0.383	0.000	0.000	0.000	0.000
76	A	108	GLN	0	0.126	0.080	40.450	-0.131	-0.131	0.000	0.000	0.000	0.000
77	A	109	VAL	0	0.016	0.019	38.425	-0.439	-0.439	0.000	0.000	0.000	0.000
78	A	110	MET	0	-0.028	-0.018	36.161	-0.530	-0.530	0.000	0.000	0.000	0.000
79	A	111	GLU	-1	-0.907	-0.954	35.952	-16.482	-16.482	0.000	0.000	0.000	0.000
80	A	112	ASP	-1	-0.751	-0.864	34.039	-18.488	-18.488	0.000	0.000	0.000	0.000
81	A	113	VAL	0	-0.039	-0.034	32.500	-0.761	-0.761	0.000	0.000	0.000	0.000
82	A	114	GLU	-1	-0.795	-0.891	31.379	-20.008	-20.008	0.000	0.000	0.000	0.000
83	A	115	LEU	0	-0.069	-0.021	29.903	-0.633	-0.633	0.000	0.000	0.000	0.000
84	A	116	ILE	0	-0.001	0.012	26.881	-0.884	-0.884	0.000	0.000	0.000	0.000
85	A	117	TRP	0	-0.001	-0.012	26.342	-1.382	-1.382	0.000	0.000	0.000	0.000
86	A	118	LYS	1	0.893	0.957	25.852	18.509	18.509	0.000	0.000	0.000	0.000
87	A	119	ASN	0	0.019	0.006	24.813	-0.776	-0.776	0.000	0.000	0.000	0.000
88	A	120	CYS	0	-0.071	-0.010	22.138	-1.732	-1.732	0.000	0.000	0.000	0.000
89	A	121	ILE	0	0.007	-0.011	21.016	-1.501	-1.501	0.000	0.000	0.000	0.000
90	A	122	THR	0	-0.059	-0.033	21.180	-0.683	-0.683	0.000	0.000	0.000	0.000
91	A	123	PHE	0	-0.031	-0.006	15.145	-0.191	-0.191	0.000	0.000	0.000	0.000
92	A	124	ASN	0	-0.030	-0.022	16.500	-3.433	-3.433	0.000	0.000	0.000	0.000
93	A	125	GLY	0	0.052	0.039	16.424	-1.446	-1.446	0.000	0.000	0.000	0.000
94	A	126	ALA	0	-0.014	-0.021	18.668	-0.137	-0.137	0.000	0.000	0.000	0.000
95	A	127	ASN	0	-0.006	-0.007	17.199	1.592	1.592	0.000	0.000	0.000	0.000
96	A	128	SER	0	0.024	0.025	16.040	-0.857	-0.857	0.000	0.000	0.000	0.000
97	A	129	LEU	0	0.060	0.022	16.119	1.754	1.754	0.000	0.000	0.000	0.000
98	A	130	LEU	0	0.049	0.010	16.835	1.741	1.741	0.000	0.000	0.000	0.000
99	A	131	ALA	0	0.019	0.020	19.624	1.641	1.641	0.000	0.000	0.000	0.000
100	A	132	THR	0	-0.026	-0.012	20.533	1.673	1.673	0.000	0.000	0.000	0.000
101	A	133	GLU	-1	-0.844	-0.912	21.210	-25.070	-25.070	0.000	0.000	0.000	0.000
102	A	134	ALA	0	0.029	0.020	23.680	1.172	1.172	0.000	0.000	0.000	0.000
103	A	135	GLY	0	0.002	0.009	25.424	1.098	1.098	0.000	0.000	0.000	0.000
104	A	136	LYS	1	0.837	0.905	23.723	26.201	26.201	0.000	0.000	0.000	0.000
105	A	137	CYS	0	-0.036	-0.018	26.918	0.845	0.845	0.000	0.000	0.000	0.000
106	A	138	ARG	1	0.839	0.900	29.036	20.908	20.908	0.000	0.000	0.000	0.000
107	A	139	SER	0	0.008	-0.018	30.895	0.850	0.850	0.000	0.000	0.000	0.000
108	A	140	ALA	0	-0.079	-0.040	31.924	0.574	0.574	0.000	0.000	0.000	0.000
109	A	141	LEU	0	0.024	0.017	33.724	0.563	0.563	0.000	0.000	0.000	0.000
110	A	142	ASP	-1	-0.886	-0.941	35.773	-15.405	-15.405	0.000	0.000	0.000	0.000
111	A	143	ARG	1	0.981	0.992	32.574	18.624	18.624	0.000	0.000	0.000	0.000
112	A	144	ILE	0	-0.013	-0.004	35.788	0.390	0.390	0.000	0.000	0.000	0.000
113	A	145	ARG	1	0.943	0.967	39.118	16.116	16.116	0.000	0.000	0.000	0.000
114	A	146	ARG	1	0.852	0.932	41.333	15.017	15.017	0.000	0.000	0.000	0.000
115	A	147	ALA	0	0.035	0.010	42.103	0.346	0.346	0.000	0.000	0.000	0.000
116	A	148	TYR	0	-0.014	-0.005	43.497	0.264	0.264	0.000	0.000	0.000	0.000
117	A	149	GLN	0	-0.016	-0.016	45.345	0.032	0.032	0.000	0.000	0.000	0.000
118	A	150	ASP	-1	-0.982	-0.994	46.916	-12.863	-12.863	0.000	0.000	0.000	0.000
119	A	151	ASP	-1	-0.913	-0.953	47.574	-12.871	-12.871	0.000	0.000	0.000	0.000
120	A	152	GLN	0	-0.093	-0.048	49.435	0.364	0.364	0.000	0.000	0.000	0.000
121	A	153	ARG	0	-0.070	-0.001	51.017	0.396	0.396	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:33:LYS)