FMO DATABASE

FMODB ID: QKL4Y

Calculation Name: 1BFJ-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1BFJ

Chain ID: A

ChEMBL ID:

UniProt ID: P23727

Base Structure: SolutionNMR

Registration Date: 2025-09-02

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	111
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-878814.742593
FMO2-HF: Nuclear repulsion	834595.6036
FMO2-HF: Total energy	-44219.138993
FMO2-MP2: Total energy	-44348.364212

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:GLU)

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

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.
7.225	9.206	0.097	-0.913	-1.165	-0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.078 / q_NPA : -0.050

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	LEU	0	0.009	0.003	3.360	0.832	2.813	0.097	-0.913	-1.165	-0.002
4	A	4	PRO	0	0.011	-0.005	5.715	0.970	0.970	0.000	0.000	0.000	0.000
5	A	5	HIS	0	0.032	0.011	8.458	0.398	0.398	0.000	0.000	0.000	0.000
6	A	6	HIS	0	-0.067	-0.042	6.966	1.397	1.397	0.000	0.000	0.000	0.000
7	A	7	ASP	-1	-0.866	-0.937	11.472	-2.203	-2.203	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.876	-0.947	13.176	-1.116	-1.116	0.000	0.000	0.000	0.000
9	A	9	LYS	1	0.844	0.931	12.584	2.002	2.002	0.000	0.000	0.000	0.000
10	A	10	THR	0	-0.034	-0.013	11.462	0.136	0.136	0.000	0.000	0.000	0.000
11	A	11	TRP	0	0.042	0.019	13.130	0.358	0.358	0.000	0.000	0.000	0.000
12	A	12	ASN	0	-0.027	0.001	16.746	0.251	0.251	0.000	0.000	0.000	0.000
13	A	13	VAL	0	-0.012	-0.008	19.845	-0.003	-0.003	0.000	0.000	0.000	0.000
14	A	14	GLY	0	0.037	0.029	22.437	0.050	0.050	0.000	0.000	0.000	0.000
15	A	15	SER	0	0.000	-0.004	25.257	0.019	0.019	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.005	0.004	26.820	0.045	0.045	0.000	0.000	0.000	0.000
17	A	17	ASN	0	0.054	0.019	28.752	-0.003	-0.003	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.921	0.936	29.996	0.269	0.269	0.000	0.000	0.000	0.000
19	A	19	ASN	0	0.096	0.042	30.032	-0.010	-0.010	0.000	0.000	0.000	0.000
20	A	20	LYS	1	0.947	0.985	26.127	0.378	0.378	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.027	0.008	26.010	-0.009	-0.009	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.858	-0.917	25.980	-0.144	-0.144	0.000	0.000	0.000	0.000
23	A	23	ASN	0	-0.019	-0.021	27.395	0.032	0.032	0.000	0.000	0.000	0.000
24	A	24	LEU	0	-0.066	-0.014	22.430	0.009	0.009	0.000	0.000	0.000	0.000
25	A	25	LEU	0	0.010	0.022	22.281	-0.008	-0.008	0.000	0.000	0.000	0.000
26	A	26	ARG	1	0.899	0.934	24.184	0.142	0.142	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.006	0.004	24.974	-0.019	-0.019	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.820	0.922	19.206	0.243	0.243	0.000	0.000	0.000	0.000
29	A	29	ARG	1	0.999	0.994	18.040	-0.431	-0.431	0.000	0.000	0.000	0.000
30	A	30	ASP	-1	-0.704	-0.855	19.456	0.052	0.052	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.014	0.014	16.216	0.078	0.078	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.104	-0.045	15.787	-0.131	-0.131	0.000	0.000	0.000	0.000
33	A	33	PHE	0	0.006	-0.013	14.490	0.024	0.024	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.027	-0.018	17.551	-0.078	-0.078	0.000	0.000	0.000	0.000
35	A	35	VAL	0	-0.008	-0.011	18.866	0.036	0.036	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.786	0.888	21.321	0.408	0.408	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.828	-0.916	24.902	-0.547	-0.547	0.000	0.000	0.000	0.000
38	A	38	SER	0	-0.006	0.001	28.198	0.045	0.045	0.000	0.000	0.000	0.000
39	A	39	SER	0	-0.025	-0.034	30.945	0.042	0.042	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.931	0.975	32.569	0.256	0.256	0.000	0.000	0.000	0.000
41	A	41	GLN	0	0.048	0.027	33.582	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.054	0.029	31.610	-0.014	-0.014	0.000	0.000	0.000	0.000
43	A	43	CYS	0	-0.031	-0.004	30.239	-0.025	-0.025	0.000	0.000	0.000	0.000
44	A	44	TYR	0	0.003	0.005	24.937	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	ALA	0	0.001	-0.004	25.588	0.040	0.040	0.000	0.000	0.000	0.000
46	A	46	CYS	0	-0.006	0.021	20.455	-0.072	-0.072	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.017	-0.030	22.527	0.049	0.049	0.000	0.000	0.000	0.000
48	A	48	VAL	0	0.029	0.000	19.626	-0.055	-0.055	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.034	-0.011	21.078	0.022	0.022	0.000	0.000	0.000	0.000
50	A	50	VAL	0	-0.016	-0.009	21.360	0.003	0.003	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.974	-1.001	23.191	0.264	0.264	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.005	0.020	24.660	0.004	0.004	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.924	-0.976	26.988	-0.023	-0.023	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.024	-0.016	25.554	-0.011	-0.011	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.890	0.960	25.731	0.033	0.033	0.000	0.000	0.000	0.000
56	A	56	HIS	0	0.009	0.011	25.697	-0.061	-0.061	0.000	0.000	0.000	0.000
57	A	57	CYS	0	0.009	0.023	24.081	0.031	0.031	0.000	0.000	0.000	0.000
58	A	58	VAL	0	-0.004	-0.005	25.691	-0.047	-0.047	0.000	0.000	0.000	0.000
59	A	59	ILE	0	-0.002	-0.003	22.745	-0.008	-0.008	0.000	0.000	0.000	0.000
60	A	60	ASN	0	-0.022	-0.001	26.325	0.016	0.016	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.966	0.976	27.538	0.559	0.559	0.000	0.000	0.000	0.000
62	A	62	THR	0	-0.005	-0.017	29.498	0.029	0.029	0.000	0.000	0.000	0.000
63	A	63	ALA	0	0.050	0.033	29.677	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.028	0.014	29.606	-0.014	-0.014	0.000	0.000	0.000	0.000
65	A	65	GLY	0	0.006	-0.002	29.842	0.032	0.032	0.000	0.000	0.000	0.000
66	A	66	TYR	0	0.006	0.005	24.024	0.010	0.010	0.000	0.000	0.000	0.000
67	A	67	GLY	0	-0.014	-0.036	25.198	-0.022	-0.022	0.000	0.000	0.000	0.000
68	A	68	PHE	0	-0.004	0.005	23.907	0.038	0.038	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.034	0.018	26.724	-0.032	-0.032	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.913	-0.960	29.484	-0.208	-0.208	0.000	0.000	0.000	0.000
71	A	71	PRO	0	-0.037	-0.011	25.397	0.019	0.019	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.028	-0.018	26.392	-0.024	-0.024	0.000	0.000	0.000	0.000
73	A	73	ASN	0	0.008	0.002	22.428	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.038	-0.015	23.151	-0.056	-0.056	0.000	0.000	0.000	0.000
75	A	75	TYR	0	0.020	0.002	19.362	-0.060	-0.060	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.018	-0.029	18.940	0.040	0.040	0.000	0.000	0.000	0.000
77	A	77	SER	0	-0.034	-0.028	18.398	-0.035	-0.035	0.000	0.000	0.000	0.000
78	A	78	LEU	0	0.044	0.000	19.788	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.931	0.975	13.707	2.608	2.608	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.797	-0.862	15.000	-1.520	-1.520	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.026	0.012	16.554	0.071	0.071	0.000	0.000	0.000	0.000
82	A	82	VAL	0	-0.012	-0.016	13.466	0.105	0.105	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.008	0.004	9.952	0.062	0.062	0.000	0.000	0.000	0.000
84	A	84	HIS	0	0.022	0.010	13.539	0.203	0.203	0.000	0.000	0.000	0.000
85	A	85	TYR	0	-0.022	-0.022	16.496	0.173	0.173	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.066	-0.008	10.087	0.043	0.043	0.000	0.000	0.000	0.000
87	A	87	HIS	0	0.004	-0.005	10.332	0.499	0.499	0.000	0.000	0.000	0.000
88	A	88	THR	0	-0.047	-0.010	15.224	0.149	0.149	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.012	-0.017	18.976	-0.051	-0.051	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.006	-0.035	20.438	-0.032	-0.032	0.000	0.000	0.000	0.000
91	A	91	VAL	0	-0.050	-0.011	22.928	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	92	GLN	0	0.076	0.045	25.422	-0.015	-0.015	0.000	0.000	0.000	0.000
93	A	93	HIS	0	-0.024	-0.014	27.001	0.002	0.002	0.000	0.000	0.000	0.000
94	A	94	ASN	0	0.007	-0.010	30.329	-0.006	-0.006	0.000	0.000	0.000	0.000
95	A	95	ASP	-1	-0.926	-0.945	29.463	0.021	0.021	0.000	0.000	0.000	0.000
96	A	96	SER	0	-0.015	-0.015	29.314	0.038	0.038	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.099	-0.043	25.638	0.006	0.006	0.000	0.000	0.000	0.000
98	A	98	ASN	0	0.013	0.005	22.107	-0.043	-0.043	0.000	0.000	0.000	0.000
99	A	99	VAL	0	0.003	0.032	18.912	0.046	0.046	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.027	0.025	15.540	-0.021	-0.021	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.053	-0.036	15.765	0.038	0.038	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.016	-0.002	11.755	-0.237	-0.237	0.000	0.000	0.000	0.000
103	A	103	TYR	0	-0.017	-0.008	10.832	-0.072	-0.072	0.000	0.000	0.000	0.000
104	A	104	PRO	0	-0.036	-0.011	10.958	0.006	0.006	0.000	0.000	0.000	0.000
105	A	105	VAL	0	-0.012	-0.010	13.891	0.126	0.126	0.000	0.000	0.000	0.000
106	A	106	TYR	0	-0.062	-0.029	16.018	0.155	0.155	0.000	0.000	0.000	0.000
107	A	107	ALA	0	0.055	0.025	11.024	-0.230	-0.230	0.000	0.000	0.000	0.000
108	A	108	GLN	0	0.004	-0.007	10.507	0.032	0.032	0.000	0.000	0.000	0.000
109	A	109	GLN	0	-0.037	-0.025	10.601	0.236	0.236	0.000	0.000	0.000	0.000
110	A	110	ARG	1	0.950	0.979	9.615	1.246	1.246	0.000	0.000	0.000	0.000
111	A	111	ARG	0	0.067	0.053	7.690	-0.566	-0.566	0.000	0.000	0.000	0.000

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