FMO DATABASE

FMODB ID: JYM79

Calculation Name: 2U2F-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2U2F

Chain ID: A

ChEMBL ID:

UniProt ID: P26368

Base Structure: SolutionNMR

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	85
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-507596.591103
FMO2-HF: Nuclear repulsion	475956.653452
FMO2-HF: Total energy	-31639.937651
FMO2-MP2: Total energy	-31732.763728

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:ALA)

Summations of interaction energy for fragment #1(A:1: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.
-42.142	-41.975	13.833	-6.645	-7.357	-0.026

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.872 / q_NPA : 0.926

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

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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	LYS	1	0.950	0.999	3.821	24.922	26.561	-0.026	-0.907	-0.707	0.001
50	A	50	TYR	0	-0.028	-0.027	4.178	5.099	5.222	-0.001	-0.007	-0.115	0.000
51	A	51	VAL	0	-0.042	-0.020	4.315	-6.624	-6.554	-0.001	-0.021	-0.047	0.000
52	A	52	ASP	-1	-0.804	-0.892	4.793	-46.107	-45.996	-0.001	-0.026	-0.084	0.000
53	A	53	ILE	0	-0.111	-0.079	1.713	-30.682	-33.089	13.576	-6.213	-4.957	-0.014
54	A	54	ASN	0	0.039	0.025	2.661	3.868	2.419	0.053	1.635	-0.239	-0.001
56	A	56	THR	0	-0.007	-0.007	2.803	-9.359	-7.321	0.234	-1.100	-1.173	-0.012
57	A	57	ASP	-1	-0.819	-0.904	4.862	-36.094	-36.052	-0.001	-0.006	-0.035	0.000
4	A	4	LEU	0	0.016	0.016	5.705	1.269	1.269	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.017	-0.012	7.984	2.240	2.240	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.036	0.013	11.454	-0.299	-0.299	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.013	-0.014	14.558	1.179	1.179	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.000	-0.022	17.680	0.611	0.611	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.036	0.000	17.552	0.240	0.240	0.000	0.000	0.000	0.000
10	A	10	PRO	0	-0.007	0.011	20.846	0.453	0.453	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.012	-0.028	24.563	-0.127	-0.127	0.000	0.000	0.000	0.000
12	A	12	TYR	0	0.004	0.007	25.789	-0.153	-0.153	0.000	0.000	0.000	0.000
13	A	13	LEU	0	0.015	0.019	21.118	-0.024	-0.024	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.002	-0.019	22.944	-0.455	-0.455	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.836	-0.920	18.152	-17.833	-17.833	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.827	-0.927	18.658	-16.094	-16.094	0.000	0.000	0.000	0.000
17	A	17	GLN	0	0.015	0.012	19.547	-0.368	-0.368	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.022	-0.016	16.125	-0.242	-0.242	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.880	0.945	14.045	16.809	16.809	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.915	-0.965	15.030	-16.168	-16.168	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.032	-0.021	16.724	-0.485	-0.485	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.012	-0.006	11.645	-0.789	-0.789	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.043	-0.008	11.707	-2.412	-2.412	0.000	0.000	0.000	0.000
24	A	24	SER	0	-0.001	0.008	13.469	0.026	0.026	0.000	0.000	0.000	0.000
25	A	25	PHE	0	0.006	0.013	10.692	0.328	0.328	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.012	0.009	10.747	-1.121	-1.121	0.000	0.000	0.000	0.000
27	A	27	PRO	0	-0.002	0.008	10.343	0.238	0.238	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.008	-0.011	8.126	-3.954	-3.954	0.000	0.000	0.000	0.000
29	A	29	LYS	1	0.931	0.966	6.922	37.789	37.789	0.000	0.000	0.000	0.000
30	A	30	ALA	0	0.003	-0.003	8.459	2.643	2.643	0.000	0.000	0.000	0.000
31	A	31	PHE	0	-0.007	-0.015	9.639	-2.028	-2.028	0.000	0.000	0.000	0.000
32	A	32	ASN	0	0.027	0.014	12.249	1.770	1.770	0.000	0.000	0.000	0.000
33	A	33	LEU	0	0.031	0.023	14.937	-0.431	-0.431	0.000	0.000	0.000	0.000
34	A	34	VAL	0	-0.033	-0.022	17.188	0.341	0.341	0.000	0.000	0.000	0.000
35	A	35	LYS	1	0.924	0.952	19.965	13.597	13.597	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.762	-0.866	23.633	-10.880	-10.880	0.000	0.000	0.000	0.000
37	A	37	SER	0	-0.072	-0.044	25.766	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.021	0.011	28.489	0.163	0.163	0.000	0.000	0.000	0.000
39	A	39	THR	0	-0.024	-0.025	30.880	0.415	0.415	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.006	0.002	31.551	0.338	0.338	0.000	0.000	0.000	0.000
41	A	41	LEU	0	-0.041	-0.015	28.631	-0.033	-0.033	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.014	-0.019	26.618	-0.137	-0.137	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.905	0.952	22.201	13.335	13.335	0.000	0.000	0.000	0.000
44	A	44	GLY	0	0.065	0.040	22.344	-0.071	-0.071	0.000	0.000	0.000	0.000
45	A	45	TYR	0	-0.019	-0.007	16.857	0.050	0.050	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.019	0.013	15.139	0.632	0.632	0.000	0.000	0.000	0.000
47	A	47	PHE	0	-0.040	-0.025	11.106	-0.318	-0.318	0.000	0.000	0.000	0.000
48	A	48	CYS	0	-0.029	0.016	9.417	0.978	0.978	0.000	0.000	0.000	0.000
49	A	49	GLU	-1	-0.854	-0.937	5.155	-42.338	-42.338	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.027	0.016	6.084	1.440	1.440	0.000	0.000	0.000	0.000
58	A	58	GLN	0	-0.025	-0.005	7.330	2.731	2.731	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.042	0.021	8.407	2.695	2.695	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.045	-0.029	7.748	2.531	2.531	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.016	-0.021	10.699	2.375	2.375	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.009	0.018	12.962	1.628	1.628	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.038	-0.016	12.187	0.905	0.905	0.000	0.000	0.000	0.000
64	A	64	ASN	0	-0.054	-0.025	13.344	1.698	1.698	0.000	0.000	0.000	0.000
65	A	65	GLY	0	-0.026	-0.004	15.267	0.644	0.644	0.000	0.000	0.000	0.000
66	A	66	MET	0	0.018	0.020	18.613	0.608	0.608	0.000	0.000	0.000	0.000
67	A	67	GLN	0	-0.018	-0.034	20.518	-0.027	-0.027	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.012	0.006	23.738	0.016	0.016	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.034	-0.029	25.637	0.355	0.355	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.903	-0.935	28.505	-10.014	-10.014	0.000	0.000	0.000	0.000
71	A	71	LYS	1	0.953	0.974	24.303	12.034	12.034	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.968	0.979	20.310	13.988	13.988	0.000	0.000	0.000	0.000
73	A	73	LEU	0	0.009	0.015	17.705	-0.230	-0.230	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.035	-0.003	16.931	-0.506	-0.506	0.000	0.000	0.000	0.000
75	A	75	VAL	0	0.012	0.012	11.688	-0.835	-0.835	0.000	0.000	0.000	0.000
76	A	76	GLN	0	0.018	0.004	10.745	0.934	0.934	0.000	0.000	0.000	0.000
77	A	77	ARG	1	0.867	0.912	5.443	37.126	37.126	0.000	0.000	0.000	0.000
78	A	78	ALA	0	-0.031	-0.014	8.399	3.345	3.345	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.059	-0.059	6.537	0.456	0.456	0.000	0.000	0.000	0.000
80	A	80	VAL	0	0.094	0.055	8.978	-0.010	-0.010	0.000	0.000	0.000	0.000
81	A	81	GLY	0	-0.020	-0.004	11.530	-0.633	-0.633	0.000	0.000	0.000	0.000
82	A	82	ALA	0	-0.028	-0.017	11.414	0.884	0.884	0.000	0.000	0.000	0.000
83	A	83	LYS	1	0.906	0.941	13.541	18.299	18.299	0.000	0.000	0.000	0.000
84	A	84	ASN	0	-0.052	-0.021	13.568	0.958	0.958	0.000	0.000	0.000	0.000
85	A	85	ALA	-1	-0.878	-0.923	14.144	-19.240	-19.240	0.000	0.000	0.000	0.000

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