FMO DATABASE

FMODB ID: 8GL1Y

Calculation Name: 2BKF-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2BKF

Chain ID: A

ChEMBL ID:

UniProt ID: Q14596

Base Structure: X-ray

Registration Date: 2025-10-03

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	86
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-604256.775959
FMO2-HF: Nuclear repulsion	569209.026636
FMO2-HF: Total energy	-35047.749323
FMO2-MP2: Total energy	-35148.042619

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:0:ALA)

Summations of interaction energy for fragment #1(A:0:ALA)

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.
-214.495	-220.641	1.076	6.052	-0.982	-0.008

Interaction energy analysis for fragmet #1(A:0:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.815 / q_NPA : 0.903

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	2	GLU	-1	-0.901	-0.924	2.587	-17.823	-24.836	1.073	6.490	-0.550	-0.005
25	A	24	GLU	-1	-0.798	-0.906	3.823	-63.614	-62.747	0.003	-0.438	-0.432	-0.003
4	A	3	PRO	0	-0.046	-0.012	6.141	1.248	1.248	0.000	0.000	0.000	0.000
5	A	4	GLN	0	0.011	-0.002	8.881	1.389	1.389	0.000	0.000	0.000	0.000
6	A	5	VAL	0	0.021	0.024	12.179	0.520	0.520	0.000	0.000	0.000	0.000
7	A	6	THR	0	-0.052	-0.036	14.012	0.644	0.644	0.000	0.000	0.000	0.000
8	A	7	LEU	0	0.016	0.007	16.380	0.097	0.097	0.000	0.000	0.000	0.000
9	A	8	ASN	0	0.006	0.001	19.665	0.617	0.617	0.000	0.000	0.000	0.000
10	A	9	VAL	0	0.010	0.010	22.622	0.146	0.146	0.000	0.000	0.000	0.000
11	A	10	THR	0	0.030	0.014	25.151	0.406	0.406	0.000	0.000	0.000	0.000
12	A	11	PHE	0	0.014	0.009	28.869	-0.004	-0.004	0.000	0.000	0.000	0.000
13	A	12	LYS	1	0.828	0.910	31.614	8.869	8.869	0.000	0.000	0.000	0.000
14	A	13	ASN	0	-0.046	-0.024	34.556	-0.115	-0.115	0.000	0.000	0.000	0.000
15	A	14	GLU	-1	-0.893	-0.928	31.850	-9.627	-9.627	0.000	0.000	0.000	0.000
16	A	15	ILE	0	-0.015	-0.015	27.069	-0.150	-0.150	0.000	0.000	0.000	0.000
17	A	16	GLN	0	-0.058	-0.028	26.566	-0.106	-0.106	0.000	0.000	0.000	0.000
18	A	17	SER	0	-0.029	-0.023	22.816	-0.112	-0.112	0.000	0.000	0.000	0.000
19	A	18	PHE	0	-0.004	-0.005	20.461	-0.010	-0.010	0.000	0.000	0.000	0.000
20	A	19	LEU	0	-0.059	-0.023	17.647	-0.579	-0.579	0.000	0.000	0.000	0.000
21	A	20	VAL	0	0.045	0.024	13.162	0.329	0.329	0.000	0.000	0.000	0.000
22	A	21	SER	0	-0.035	-0.046	12.846	-0.963	-0.963	0.000	0.000	0.000	0.000
23	A	22	ASP	-1	-0.862	-0.940	7.926	-34.281	-34.281	0.000	0.000	0.000	0.000
24	A	23	PRO	0	-0.003	0.015	8.897	1.030	1.030	0.000	0.000	0.000	0.000
26	A	25	ASN	0	-0.150	-0.052	7.993	2.036	2.036	0.000	0.000	0.000	0.000
27	A	26	THR	0	-0.019	-0.004	10.226	2.662	2.662	0.000	0.000	0.000	0.000
28	A	27	THR	0	-0.026	-0.044	13.383	-0.246	-0.246	0.000	0.000	0.000	0.000
29	A	28	TRP	0	0.084	0.015	16.144	0.038	0.038	0.000	0.000	0.000	0.000
30	A	29	ALA	0	-0.018	-0.006	18.588	0.683	0.683	0.000	0.000	0.000	0.000
31	A	30	ASP	-1	-0.829	-0.890	17.253	-16.111	-16.111	0.000	0.000	0.000	0.000
32	A	31	ILE	0	-0.002	0.003	16.452	0.572	0.572	0.000	0.000	0.000	0.000
33	A	32	GLU	-1	-0.875	-0.943	20.225	-11.406	-11.406	0.000	0.000	0.000	0.000
34	A	33	ALA	0	-0.037	-0.015	23.218	0.612	0.612	0.000	0.000	0.000	0.000
35	A	34	MET	0	-0.018	0.003	19.329	0.415	0.415	0.000	0.000	0.000	0.000
36	A	35	VAL	0	0.020	0.020	23.301	0.491	0.491	0.000	0.000	0.000	0.000
37	A	36	LYS	1	0.850	0.936	25.786	11.692	11.692	0.000	0.000	0.000	0.000
38	A	37	VAL	0	-0.032	-0.021	27.451	0.448	0.448	0.000	0.000	0.000	0.000
39	A	38	SER	0	-0.071	-0.045	26.403	0.262	0.262	0.000	0.000	0.000	0.000
40	A	39	PHE	0	-0.041	-0.029	26.996	0.186	0.186	0.000	0.000	0.000	0.000
41	A	40	ASP	-1	-0.984	-0.969	31.606	-8.439	-8.439	0.000	0.000	0.000	0.000
42	A	41	LEU	0	-0.006	0.000	30.591	0.195	0.195	0.000	0.000	0.000	0.000
43	A	42	ASN	0	-0.033	-0.030	31.672	-0.368	-0.368	0.000	0.000	0.000	0.000
44	A	43	THR	0	-0.051	-0.026	31.122	-0.244	-0.244	0.000	0.000	0.000	0.000
45	A	44	ILE	0	0.023	0.011	26.626	0.184	0.184	0.000	0.000	0.000	0.000
46	A	45	GLN	0	-0.027	-0.004	28.303	-0.154	-0.154	0.000	0.000	0.000	0.000
47	A	46	ILE	0	0.000	-0.006	23.589	0.215	0.215	0.000	0.000	0.000	0.000
48	A	47	LYS	1	0.904	0.953	25.327	10.353	10.353	0.000	0.000	0.000	0.000
49	A	48	TYR	0	0.015	-0.006	19.891	-0.387	-0.387	0.000	0.000	0.000	0.000
50	A	49	LEU	0	0.014	0.041	23.712	0.191	0.191	0.000	0.000	0.000	0.000
51	A	50	ASP	-1	-0.801	-0.921	21.699	-13.628	-13.628	0.000	0.000	0.000	0.000
52	A	51	GLU	-1	-0.839	-0.927	17.890	-17.469	-17.469	0.000	0.000	0.000	0.000
53	A	52	GLU	-1	-0.980	-0.989	22.197	-13.025	-13.025	0.000	0.000	0.000	0.000
54	A	53	ASN	0	-0.152	-0.062	25.120	0.617	0.617	0.000	0.000	0.000	0.000
55	A	54	GLU	-1	-0.902	-0.942	26.502	-9.768	-9.768	0.000	0.000	0.000	0.000
56	A	55	GLU	-1	-0.931	-0.988	26.310	-12.167	-12.167	0.000	0.000	0.000	0.000
57	A	56	VAL	0	-0.016	-0.009	23.100	0.454	0.454	0.000	0.000	0.000	0.000
58	A	57	SER	0	-0.027	-0.016	24.765	-0.063	-0.063	0.000	0.000	0.000	0.000
59	A	58	ILE	0	-0.042	-0.011	19.040	-0.459	-0.459	0.000	0.000	0.000	0.000
60	A	59	ASN	0	-0.047	-0.030	22.712	0.729	0.729	0.000	0.000	0.000	0.000
61	A	60	SER	0	-0.080	-0.055	21.123	-0.068	-0.068	0.000	0.000	0.000	0.000
62	A	61	GLN	0	0.019	-0.006	13.450	1.217	1.217	0.000	0.000	0.000	0.000
63	A	62	GLY	0	0.002	0.005	16.027	-0.977	-0.977	0.000	0.000	0.000	0.000
64	A	63	GLU	-1	-0.786	-0.890	16.598	-14.335	-14.335	0.000	0.000	0.000	0.000
65	A	64	TYR	0	-0.020	-0.011	14.072	0.185	0.185	0.000	0.000	0.000	0.000
66	A	65	GLU	-1	-0.841	-0.919	11.644	-24.746	-24.746	0.000	0.000	0.000	0.000
67	A	66	GLU	-1	-0.892	-0.933	12.697	-23.158	-23.158	0.000	0.000	0.000	0.000
68	A	67	ALA	0	0.022	0.027	15.122	-0.247	-0.247	0.000	0.000	0.000	0.000
69	A	68	LEU	0	-0.009	-0.003	10.816	0.233	0.233	0.000	0.000	0.000	0.000
70	A	69	LYS	1	0.815	0.878	9.965	23.963	23.963	0.000	0.000	0.000	0.000
71	A	70	MET	0	-0.070	-0.013	11.796	-0.053	-0.053	0.000	0.000	0.000	0.000
72	A	71	ALA	0	0.045	0.022	13.251	0.441	0.441	0.000	0.000	0.000	0.000
73	A	72	VAL	0	-0.033	-0.016	8.851	0.151	0.151	0.000	0.000	0.000	0.000
74	A	73	LYS	1	0.721	0.853	12.071	20.147	20.147	0.000	0.000	0.000	0.000
75	A	74	GLN	0	-0.023	0.000	14.504	1.320	1.320	0.000	0.000	0.000	0.000
76	A	75	GLY	0	-0.025	-0.006	15.800	0.847	0.847	0.000	0.000	0.000	0.000
77	A	76	ASN	0	-0.044	-0.029	11.986	-0.799	-0.799	0.000	0.000	0.000	0.000
78	A	77	GLN	0	0.006	0.012	14.374	1.205	1.205	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.022	0.013	16.192	-0.162	-0.162	0.000	0.000	0.000	0.000
80	A	79	GLN	0	0.012	0.015	19.345	0.571	0.571	0.000	0.000	0.000	0.000
81	A	80	MET	0	0.008	-0.003	19.199	-0.077	-0.077	0.000	0.000	0.000	0.000
82	A	81	GLN	0	0.026	0.022	24.425	0.257	0.257	0.000	0.000	0.000	0.000
83	A	82	VAL	0	-0.012	-0.010	26.782	-0.151	-0.151	0.000	0.000	0.000	0.000
84	A	83	HIS	0	-0.062	-0.032	29.013	0.693	0.693	0.000	0.000	0.000	0.000
85	A	84	GLU	-1	-0.863	-0.941	31.519	-8.737	-8.737	0.000	0.000	0.000	0.000
86	A	85	GLY	-1	-0.951	-0.975	33.064	-9.227	-9.227	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:ALA)