FMO DATABASE

FMODB ID: MR72Z

Calculation Name: 2FO3-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FO3

Chain ID: A

ChEMBL ID:

UniProt ID: A5K893

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	109
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-892921.023651
FMO2-HF: Nuclear repulsion	849474.20056
FMO2-HF: Total energy	-43446.823091
FMO2-MP2: Total energy	-43575.0292

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:9:TYR)

Summations of interaction energy for fragment #1(A:9:TYR)

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.
-76.418	-76.731	23.584	-12.129	-11.141	0.132

Interaction energy analysis for fragmet #1(A:9:TYR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.059 / q_NPA : 0.023

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	11	ILE	0	0.063	0.035	3.601	2.417	4.454	-0.003	-0.788	-1.246	-0.001
4	A	12	GLN	0	0.053	0.029	3.774	2.090	2.850	0.005	-0.247	-0.518	0.000
5	A	13	LYS	1	0.821	0.903	1.757	-75.311	-78.421	23.582	-11.094	-9.377	0.133
6	A	14	GLU	-1	-0.753	-0.847	7.202	-0.324	-0.324	0.000	0.000	0.000	0.000
7	A	15	LEU	0	-0.001	0.006	8.179	0.798	0.798	0.000	0.000	0.000	0.000
8	A	16	HIS	0	-0.005	0.003	9.326	1.220	1.220	0.000	0.000	0.000	0.000
9	A	17	ASN	0	-0.009	-0.018	11.077	-0.395	-0.395	0.000	0.000	0.000	0.000
10	A	18	PHE	0	0.054	0.005	12.835	0.001	0.001	0.000	0.000	0.000	0.000
11	A	19	LEU	0	-0.030	-0.018	12.975	0.048	0.048	0.000	0.000	0.000	0.000
12	A	20	ASN	0	-0.054	-0.023	14.495	0.154	0.154	0.000	0.000	0.000	0.000
13	A	21	ASN	0	-0.039	-0.013	16.425	0.229	0.229	0.000	0.000	0.000	0.000
14	A	22	PRO	0	0.025	0.048	18.209	-0.149	-0.149	0.000	0.000	0.000	0.000
15	A	23	PRO	0	0.000	-0.004	18.315	0.152	0.152	0.000	0.000	0.000	0.000
16	A	24	ILE	0	0.061	0.026	21.533	-0.055	-0.055	0.000	0.000	0.000	0.000
17	A	25	ASN	0	-0.031	-0.025	25.125	-0.045	-0.045	0.000	0.000	0.000	0.000
18	A	26	CYS	0	-0.037	0.003	20.497	-0.191	-0.191	0.000	0.000	0.000	0.000
19	A	27	THR	0	-0.045	-0.021	20.615	0.100	0.100	0.000	0.000	0.000	0.000
20	A	28	LEU	0	-0.027	-0.020	12.907	-0.083	-0.083	0.000	0.000	0.000	0.000
21	A	29	ASP	-1	-0.879	-0.924	16.940	-2.446	-2.446	0.000	0.000	0.000	0.000
22	A	30	VAL	0	-0.023	-0.027	11.607	-0.413	-0.413	0.000	0.000	0.000	0.000
23	A	31	HIS	0	0.019	0.011	13.473	0.149	0.149	0.000	0.000	0.000	0.000
24	A	32	PRO	0	0.009	0.010	13.274	-0.652	-0.652	0.000	0.000	0.000	0.000
25	A	33	ASN	0	-0.014	-0.011	14.549	-0.097	-0.097	0.000	0.000	0.000	0.000
26	A	34	ASN	0	-0.017	-0.018	11.156	-1.319	-1.319	0.000	0.000	0.000	0.000
27	A	35	ILE	0	0.076	0.033	5.067	0.122	0.122	0.000	0.000	0.000	0.000
28	A	36	ARG	1	0.795	0.916	6.269	11.754	11.754	0.000	0.000	0.000	0.000
29	A	37	ILE	0	-0.019	-0.013	9.050	1.195	1.195	0.000	0.000	0.000	0.000
30	A	38	TRP	0	0.015	0.006	8.586	0.437	0.437	0.000	0.000	0.000	0.000
31	A	39	ILE	0	-0.033	-0.031	13.751	0.255	0.255	0.000	0.000	0.000	0.000
32	A	40	VAL	0	0.046	0.034	16.510	0.114	0.114	0.000	0.000	0.000	0.000
33	A	41	LYS	1	0.891	0.954	18.841	1.046	1.046	0.000	0.000	0.000	0.000
34	A	42	TYR	0	0.078	0.031	22.506	0.040	0.040	0.000	0.000	0.000	0.000
35	A	43	VAL	0	-0.043	-0.020	24.660	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	44	GLY	0	0.061	0.027	28.348	0.058	0.058	0.000	0.000	0.000	0.000
37	A	45	LEU	0	0.006	0.004	28.681	0.040	0.040	0.000	0.000	0.000	0.000
38	A	46	GLU	-1	-0.903	-0.947	31.852	-0.189	-0.189	0.000	0.000	0.000	0.000
39	A	47	ASN	0	-0.051	-0.036	35.116	0.011	0.011	0.000	0.000	0.000	0.000
40	A	48	THR	0	0.019	0.014	32.232	-0.013	-0.013	0.000	0.000	0.000	0.000
41	A	49	ILE	0	-0.009	-0.023	35.259	0.001	0.001	0.000	0.000	0.000	0.000
42	A	50	TYR	0	-0.036	-0.025	31.852	-0.035	-0.035	0.000	0.000	0.000	0.000
43	A	51	ALA	0	-0.010	0.013	33.388	-0.038	-0.038	0.000	0.000	0.000	0.000
44	A	52	ASN	0	-0.061	-0.046	33.300	0.001	0.001	0.000	0.000	0.000	0.000
45	A	53	GLU	-1	-0.843	-0.878	32.564	-0.702	-0.702	0.000	0.000	0.000	0.000
46	A	54	VAL	0	-0.063	-0.042	27.554	-0.027	-0.027	0.000	0.000	0.000	0.000
47	A	55	TYR	0	-0.023	-0.030	26.520	-0.073	-0.073	0.000	0.000	0.000	0.000
48	A	56	LYS	1	0.916	0.949	22.497	1.606	1.606	0.000	0.000	0.000	0.000
49	A	57	LEU	0	0.019	0.022	19.341	0.019	0.019	0.000	0.000	0.000	0.000
50	A	58	LYS	1	0.895	0.962	17.178	3.079	3.079	0.000	0.000	0.000	0.000
51	A	59	ILE	0	0.021	0.010	12.589	0.151	0.151	0.000	0.000	0.000	0.000
52	A	60	ILE	0	-0.009	-0.005	12.751	-0.461	-0.461	0.000	0.000	0.000	0.000
53	A	61	PHE	0	0.016	0.004	7.959	-0.147	-0.147	0.000	0.000	0.000	0.000
54	A	62	PRO	0	0.024	0.020	9.573	-1.227	-1.227	0.000	0.000	0.000	0.000
55	A	63	ASP	-1	-0.866	-0.949	8.674	-12.038	-12.038	0.000	0.000	0.000	0.000
56	A	64	ASP	-1	-0.802	-0.893	7.832	-6.615	-6.615	0.000	0.000	0.000	0.000
57	A	65	TYR	0	-0.058	0.007	6.049	0.565	0.565	0.000	0.000	0.000	0.000
58	A	66	PRO	0	-0.047	-0.041	6.029	-3.198	-3.198	0.000	0.000	0.000	0.000
59	A	67	LEU	0	0.038	0.010	8.926	1.357	1.357	0.000	0.000	0.000	0.000
60	A	68	LYS	1	0.862	0.931	11.382	3.776	3.776	0.000	0.000	0.000	0.000
61	A	69	PRO	0	0.054	0.034	11.829	-0.760	-0.760	0.000	0.000	0.000	0.000
62	A	70	PRO	0	-0.042	-0.023	11.828	-0.565	-0.565	0.000	0.000	0.000	0.000
63	A	71	ILE	0	0.014	0.001	13.246	0.611	0.611	0.000	0.000	0.000	0.000
64	A	72	VAL	0	-0.024	-0.021	15.987	-0.294	-0.294	0.000	0.000	0.000	0.000
65	A	73	TYR	0	0.051	0.033	18.244	0.092	0.092	0.000	0.000	0.000	0.000
66	A	74	PHE	0	0.027	0.001	21.177	-0.135	-0.135	0.000	0.000	0.000	0.000
67	A	75	LEU	0	-0.051	-0.028	21.475	-0.045	-0.045	0.000	0.000	0.000	0.000
68	A	76	GLN	0	-0.057	-0.027	24.895	0.208	0.208	0.000	0.000	0.000	0.000
69	A	77	LYS	1	0.909	0.955	28.664	1.000	1.000	0.000	0.000	0.000	0.000
70	A	78	PRO	0	0.055	0.023	27.802	-0.008	-0.008	0.000	0.000	0.000	0.000
71	A	79	PRO	0	0.030	0.030	27.803	0.067	0.067	0.000	0.000	0.000	0.000
72	A	80	LYS	1	0.934	0.952	30.752	0.732	0.732	0.000	0.000	0.000	0.000
73	A	81	HIS	0	0.086	0.065	30.991	0.013	0.013	0.000	0.000	0.000	0.000
74	A	82	THR	0	-0.013	-0.009	32.743	-0.045	-0.045	0.000	0.000	0.000	0.000
75	A	83	HIS	0	0.013	0.013	28.711	-0.055	-0.055	0.000	0.000	0.000	0.000
76	A	84	VAL	0	-0.009	-0.005	27.114	-0.115	-0.115	0.000	0.000	0.000	0.000
77	A	85	TYR	0	0.021	0.023	28.355	0.098	0.098	0.000	0.000	0.000	0.000
78	A	86	SER	0	0.001	-0.010	29.805	-0.057	-0.057	0.000	0.000	0.000	0.000
79	A	87	ASN	0	-0.046	-0.054	26.847	0.075	0.075	0.000	0.000	0.000	0.000
80	A	88	GLY	0	-0.001	0.004	25.944	-0.116	-0.116	0.000	0.000	0.000	0.000
81	A	89	ASP	-1	-0.846	-0.899	24.028	-1.884	-1.884	0.000	0.000	0.000	0.000
82	A	90	ILE	0	-0.013	-0.015	21.813	0.139	0.139	0.000	0.000	0.000	0.000
83	A	91	CYS	0	-0.051	-0.014	24.299	-0.067	-0.067	0.000	0.000	0.000	0.000
84	A	92	LEU	0	0.053	0.014	21.808	0.115	0.115	0.000	0.000	0.000	0.000
85	A	93	SER	0	0.060	0.028	23.001	-0.159	-0.159	0.000	0.000	0.000	0.000
86	A	94	LEU	0	0.008	0.010	19.996	-0.061	-0.061	0.000	0.000	0.000	0.000
87	A	95	LEU	0	-0.054	-0.033	17.579	-0.188	-0.188	0.000	0.000	0.000	0.000
88	A	96	GLY	0	-0.024	-0.019	19.202	-0.265	-0.265	0.000	0.000	0.000	0.000
89	A	97	ASP	-1	-0.938	-0.963	20.568	-0.967	-0.967	0.000	0.000	0.000	0.000
90	A	98	ASP	-1	-0.901	-0.947	22.537	-0.363	-0.363	0.000	0.000	0.000	0.000
91	A	99	TYR	0	-0.105	-0.062	11.835	0.008	0.008	0.000	0.000	0.000	0.000
92	A	100	ASN	0	0.042	0.018	15.298	0.259	0.259	0.000	0.000	0.000	0.000
93	A	101	PRO	0	0.050	0.024	11.110	-0.111	-0.111	0.000	0.000	0.000	0.000
94	A	102	SER	0	-0.038	-0.028	11.169	0.099	0.099	0.000	0.000	0.000	0.000
95	A	103	LEU	0	-0.038	0.000	12.702	0.437	0.437	0.000	0.000	0.000	0.000
96	A	104	SER	0	-0.016	-0.003	12.639	-0.617	-0.617	0.000	0.000	0.000	0.000
97	A	105	ILE	0	-0.004	-0.023	10.945	-0.150	-0.150	0.000	0.000	0.000	0.000
98	A	106	SER	0	-0.016	-0.017	13.959	-0.020	-0.020	0.000	0.000	0.000	0.000
99	A	107	GLY	0	0.054	0.027	16.681	0.030	0.030	0.000	0.000	0.000	0.000
100	A	108	LEU	0	-0.006	0.010	15.444	-0.023	-0.023	0.000	0.000	0.000	0.000
101	A	109	VAL	0	0.006	-0.007	17.158	0.006	0.006	0.000	0.000	0.000	0.000
102	A	110	LEU	0	0.019	0.007	19.673	0.068	0.068	0.000	0.000	0.000	0.000
103	A	111	SER	0	-0.025	-0.022	21.479	0.119	0.119	0.000	0.000	0.000	0.000
104	A	112	ILE	0	-0.020	-0.011	20.054	0.007	0.007	0.000	0.000	0.000	0.000
105	A	113	ILE	0	-0.033	-0.018	23.218	0.024	0.024	0.000	0.000	0.000	0.000
106	A	114	SER	0	-0.031	-0.006	25.790	0.054	0.054	0.000	0.000	0.000	0.000
107	A	115	MET	0	-0.046	-0.010	26.770	0.006	0.006	0.000	0.000	0.000	0.000
108	A	116	LEU	0	-0.099	-0.054	26.827	-0.016	-0.016	0.000	0.000	0.000	0.000
109	A	117	SER	-1	-0.924	-0.954	29.717	-0.310	-0.310	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:TYR)