FMO DATABASE

FMODB ID: QK3KY

Calculation Name: 2F41-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2F41

Chain ID: A

ChEMBL ID:

UniProt ID: O34835

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

Total energy (hartree)

FMO2-HF: Electronic energy	-856862.216617
FMO2-HF: Nuclear repulsion	814068.72547
FMO2-HF: Total energy	-42793.491147
FMO2-MP2: Total energy	-42920.823751

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:73:GLU)

Summations of interaction energy for fragment #1(A:73: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.
-92.769	-91.237	15.943	-10.775	-6.702	-0.121

Interaction energy analysis for fragmet #1(A:73:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.207 / q_NPA : -0.118

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	75	ILE	0	-0.049	-0.015	3.186	7.941	10.017	0.070	-0.949	-1.198	-0.003
48	A	120	ALA	0	0.004	0.003	4.344	1.055	1.078	-0.001	-0.008	-0.014	0.000
53	A	125	GLU	-1	-0.840	-0.931	1.726	-85.332	-85.899	15.874	-9.818	-5.490	-0.118
4	A	76	GLY	0	-0.008	-0.020	5.944	-1.042	-1.042	0.000	0.000	0.000	0.000
5	A	77	GLU	-1	-0.903	-0.936	5.362	10.834	10.834	0.000	0.000	0.000	0.000
6	A	78	ILE	0	0.010	-0.011	5.745	-2.057	-2.057	0.000	0.000	0.000	0.000
7	A	79	ILE	0	-0.114	-0.069	7.960	1.112	1.112	0.000	0.000	0.000	0.000
8	A	80	ASP	-1	-0.868	-0.931	11.641	-0.592	-0.592	0.000	0.000	0.000	0.000
9	A	81	LEU	0	-0.021	-0.016	8.004	-0.484	-0.484	0.000	0.000	0.000	0.000
10	A	82	GLU	-1	-0.917	-0.927	11.972	-1.079	-1.079	0.000	0.000	0.000	0.000
11	A	83	LEU	0	-0.004	-0.014	9.893	-0.158	-0.158	0.000	0.000	0.000	0.000
12	A	84	ASP	-1	-0.922	-0.965	13.434	-3.538	-3.538	0.000	0.000	0.000	0.000
13	A	85	ASP	-1	-0.871	-0.926	15.371	-1.590	-1.590	0.000	0.000	0.000	0.000
14	A	86	GLN	0	-0.138	-0.093	15.168	-0.092	-0.092	0.000	0.000	0.000	0.000
15	A	87	ALA	0	0.116	0.063	10.577	-0.299	-0.299	0.000	0.000	0.000	0.000
16	A	88	ILE	0	-0.068	-0.027	12.215	0.174	0.174	0.000	0.000	0.000	0.000
17	A	89	SER	0	0.079	0.039	8.488	0.345	0.345	0.000	0.000	0.000	0.000
18	A	90	ILE	0	-0.088	-0.040	9.761	-0.068	-0.068	0.000	0.000	0.000	0.000
19	A	91	LEU	0	0.037	0.026	9.449	0.951	0.951	0.000	0.000	0.000	0.000
20	A	92	GLU	-1	-0.968	-0.976	11.545	2.469	2.469	0.000	0.000	0.000	0.000
21	A	93	ILE	0	-0.021	-0.001	13.544	0.243	0.243	0.000	0.000	0.000	0.000
22	A	94	LYS	1	0.926	0.944	14.667	-3.267	-3.267	0.000	0.000	0.000	0.000
23	A	95	GLN	0	-0.025	-0.022	16.792	-0.356	-0.356	0.000	0.000	0.000	0.000
24	A	96	GLU	-1	-0.846	-0.920	14.496	2.516	2.516	0.000	0.000	0.000	0.000
25	A	97	HIS	0	0.018	0.020	11.412	-0.543	-0.543	0.000	0.000	0.000	0.000
26	A	98	VAL	0	-0.002	0.015	16.152	-0.367	-0.367	0.000	0.000	0.000	0.000
27	A	99	PHE	0	-0.070	-0.049	19.966	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	100	SER	-1	-0.708	-0.836	23.276	0.313	0.313	0.000	0.000	0.000	0.000
29	A	101	ARG	1	0.930	0.958	26.233	-0.128	-0.128	0.000	0.000	0.000	0.000
30	A	102	ASN	0	-0.147	-0.070	27.951	0.001	0.001	0.000	0.000	0.000	0.000
31	A	103	GLN	0	0.012	-0.003	23.394	0.063	0.063	0.000	0.000	0.000	0.000
32	A	104	ILE	0	-0.029	-0.003	22.660	0.035	0.035	0.000	0.000	0.000	0.000
33	A	105	ALA	0	0.056	0.023	17.812	0.073	0.073	0.000	0.000	0.000	0.000
34	A	106	ARG	1	0.844	0.920	17.807	-0.505	-0.505	0.000	0.000	0.000	0.000
35	A	107	GLY	0	0.059	0.025	17.233	-0.038	-0.038	0.000	0.000	0.000	0.000
36	A	108	HIS	0	0.018	-0.001	14.256	-0.245	-0.245	0.000	0.000	0.000	0.000
37	A	109	HIS	0	0.003	-0.002	12.267	-0.398	-0.398	0.000	0.000	0.000	0.000
38	A	110	LEU	0	0.049	0.027	12.163	-0.270	-0.270	0.000	0.000	0.000	0.000
39	A	111	PHE	0	0.017	0.014	13.693	-0.397	-0.397	0.000	0.000	0.000	0.000
40	A	112	ALA	0	0.003	0.005	9.884	-0.678	-0.678	0.000	0.000	0.000	0.000
41	A	113	GLN	0	-0.020	0.005	8.911	-1.621	-1.621	0.000	0.000	0.000	0.000
42	A	114	ALA	0	-0.017	-0.007	9.779	-1.162	-1.162	0.000	0.000	0.000	0.000
43	A	115	ASN	0	0.045	0.029	9.220	0.403	0.403	0.000	0.000	0.000	0.000
44	A	116	SER	0	-0.024	-0.030	5.289	-0.592	-0.592	0.000	0.000	0.000	0.000
45	A	117	LEU	0	-0.016	-0.008	6.346	-2.615	-2.615	0.000	0.000	0.000	0.000
46	A	118	ALA	0	-0.005	-0.012	8.728	0.450	0.450	0.000	0.000	0.000	0.000
47	A	119	VAL	0	-0.009	0.004	5.500	0.449	0.449	0.000	0.000	0.000	0.000
49	A	121	VAL	0	-0.064	-0.034	6.190	2.521	2.521	0.000	0.000	0.000	0.000
50	A	122	ILE	0	-0.014	-0.017	9.955	1.410	1.410	0.000	0.000	0.000	0.000
51	A	123	ASP	-1	-0.810	-0.879	11.096	-5.201	-5.201	0.000	0.000	0.000	0.000
52	A	124	ASP	-1	-0.862	-0.932	8.458	-10.197	-10.197	0.000	0.000	0.000	0.000
54	A	126	LEU	0	-0.115	-0.045	5.737	-0.693	-0.693	0.000	0.000	0.000	0.000
55	A	127	ALA	0	-0.017	0.012	8.897	1.373	1.373	0.000	0.000	0.000	0.000
56	A	128	LEU	0	-0.058	-0.040	9.734	-0.985	-0.985	0.000	0.000	0.000	0.000
57	A	129	THR	0	-0.035	-0.036	11.816	0.383	0.383	0.000	0.000	0.000	0.000
58	A	130	ALA	0	-0.021	0.002	13.573	0.360	0.360	0.000	0.000	0.000	0.000
59	A	131	SER	0	-0.100	-0.056	17.351	0.499	0.499	0.000	0.000	0.000	0.000
60	A	132	ALA	0	0.033	0.006	16.586	-0.312	-0.312	0.000	0.000	0.000	0.000
61	A	133	ASP	-1	-0.903	-0.919	18.709	-1.451	-1.451	0.000	0.000	0.000	0.000
62	A	134	ILE	0	0.004	-0.001	17.997	-0.061	-0.061	0.000	0.000	0.000	0.000
63	A	135	ARG	1	0.884	0.954	21.303	1.329	1.329	0.000	0.000	0.000	0.000
64	A	136	PHE	0	0.006	-0.002	18.285	-0.048	-0.048	0.000	0.000	0.000	0.000
65	A	137	THR	0	-0.090	-0.049	22.967	0.018	0.018	0.000	0.000	0.000	0.000
66	A	138	ARG	1	0.785	0.875	23.811	0.053	0.053	0.000	0.000	0.000	0.000
67	A	139	GLN	0	-0.034	-0.012	23.008	-0.026	-0.026	0.000	0.000	0.000	0.000
68	A	140	VAL	0	0.032	0.025	18.166	0.050	0.050	0.000	0.000	0.000	0.000
69	A	141	LYS	0	-0.018	-0.018	21.610	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	142	GLN	0	0.019	-0.004	19.743	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	143	GLY	0	-0.052	-0.018	19.288	-0.067	-0.067	0.000	0.000	0.000	0.000
72	A	144	GLU	-1	-0.813	-0.899	19.815	0.255	0.255	0.000	0.000	0.000	0.000
73	A	145	ARG	1	0.941	0.957	14.880	-1.512	-1.512	0.000	0.000	0.000	0.000
74	A	146	VAL	0	0.006	0.006	14.741	-0.158	-0.158	0.000	0.000	0.000	0.000
75	A	147	VAL	0	0.002	-0.005	13.927	0.142	0.142	0.000	0.000	0.000	0.000
76	A	148	ALA	0	0.002	0.016	12.218	-0.124	-0.124	0.000	0.000	0.000	0.000
77	A	149	LYS	1	0.954	0.969	13.915	0.754	0.754	0.000	0.000	0.000	0.000
78	A	150	ALA	0	0.016	0.010	12.874	0.009	0.009	0.000	0.000	0.000	0.000
79	A	151	LYS	1	0.777	0.881	14.838	2.208	2.208	0.000	0.000	0.000	0.000
80	A	152	VAL	0	0.036	0.032	15.633	-0.105	-0.105	0.000	0.000	0.000	0.000
81	A	153	THR	0	-0.089	-0.056	17.921	0.383	0.383	0.000	0.000	0.000	0.000
82	A	154	ALA	0	-0.018	-0.012	20.447	0.251	0.251	0.000	0.000	0.000	0.000
83	A	155	VAL	0	0.070	0.040	18.587	-0.233	-0.233	0.000	0.000	0.000	0.000
84	A	156	GLU	-1	-0.849	-0.887	20.869	-1.867	-1.867	0.000	0.000	0.000	0.000
85	A	157	LYS	1	0.973	0.967	21.477	1.698	1.698	0.000	0.000	0.000	0.000
86	A	158	GLU	-1	-1.008	-1.001	23.083	-1.574	-1.574	0.000	0.000	0.000	0.000
87	A	159	LYS	1	0.938	0.965	22.051	2.395	2.395	0.000	0.000	0.000	0.000
88	A	160	GLY	0	-0.003	0.008	19.950	-0.063	-0.063	0.000	0.000	0.000	0.000
89	A	161	ARG	1	0.724	0.843	18.194	2.100	2.100	0.000	0.000	0.000	0.000
90	A	162	THR	0	-0.001	-0.026	15.605	0.589	0.589	0.000	0.000	0.000	0.000
91	A	163	VAL	0	-0.043	-0.011	17.149	-0.172	-0.172	0.000	0.000	0.000	0.000
92	A	164	VAL	0	0.041	0.021	13.558	0.164	0.164	0.000	0.000	0.000	0.000
93	A	165	GLU	-1	-0.835	-0.910	16.815	-1.848	-1.848	0.000	0.000	0.000	0.000
94	A	166	VAL	0	0.003	-0.003	13.427	-0.086	-0.086	0.000	0.000	0.000	0.000
95	A	167	ASN	0	-0.040	-0.018	16.695	0.346	0.346	0.000	0.000	0.000	0.000
96	A	168	SER	0	0.018	-0.006	15.863	-0.102	-0.102	0.000	0.000	0.000	0.000
97	A	169	TYR	0	-0.031	-0.019	17.650	0.029	0.029	0.000	0.000	0.000	0.000
98	A	170	VAL	0	0.015	0.015	18.538	0.126	0.126	0.000	0.000	0.000	0.000
99	A	171	GLY	0	-0.011	-0.002	21.021	-0.010	-0.010	0.000	0.000	0.000	0.000
100	A	172	GLU	-1	-0.906	-0.966	22.380	-0.187	-0.187	0.000	0.000	0.000	0.000
101	A	173	GLU	-1	-0.906	-0.936	24.392	-0.191	-0.191	0.000	0.000	0.000	0.000
102	A	174	ILE	0	-0.004	-0.002	21.809	0.005	0.005	0.000	0.000	0.000	0.000
103	A	175	VAL	0	0.009	0.005	19.048	0.019	0.019	0.000	0.000	0.000	0.000
104	A	176	PHE	0	0.001	-0.012	16.689	0.031	0.031	0.000	0.000	0.000	0.000
105	A	177	SER	0	-0.068	-0.035	19.804	0.108	0.108	0.000	0.000	0.000	0.000
106	A	178	GLY	0	0.014	0.010	18.998	0.063	0.063	0.000	0.000	0.000	0.000
107	A	179	ARG	1	0.868	0.953	18.209	1.899	1.899	0.000	0.000	0.000	0.000
108	A	180	PHE	0	-0.015	-0.021	13.955	-0.024	-0.024	0.000	0.000	0.000	0.000
109	A	181	ASP	-1	-0.860	-0.925	16.732	-2.477	-2.477	0.000	0.000	0.000	0.000
110	A	182	MET	0	0.000	0.002	10.717	0.171	0.171	0.000	0.000	0.000	0.000
111	A	183	TYR	-1	-0.841	-0.923	13.858	-4.640	-4.640	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:73:GLU)