FMO DATABASE

FMODB ID: 67JVZ

Calculation Name: 1DUX-C-Xray547

Preferred Name: ETS domain protein Elk-1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1DUX

Chain ID: C

ChEMBL ID: CHEMBL4453

UniProt ID: P19419

Base Structure: X-ray

Registration Date: 2025-10-05

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	-661233.396233
FMO2-HF: Nuclear repulsion	625928.017778
FMO2-HF: Total energy	-35305.378455
FMO2-MP2: Total energy	-35410.99354

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:5:VAL)

Summations of interaction energy for fragment #1(A:5:VAL)

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.
95.324	105.514	7.167	-6.496	-10.862	-0.059

Interaction energy analysis for fragmet #1(A:5:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.840 / q_NPA : 0.925

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	7	LEU	0	0.041	0.020	2.605	-3.977	-1.385	0.772	-1.447	-1.916	-0.012
4	A	8	TRP	0	0.099	0.036	5.312	-0.723	-0.547	-0.001	-0.008	-0.166	0.000
5	A	9	GLN	0	0.051	0.035	2.330	-18.579	-16.588	4.224	-2.676	-3.539	-0.030
6	A	10	PHE	0	-0.030	-0.013	2.892	0.542	1.777	0.202	-0.393	-1.045	-0.002
7	A	11	LEU	0	0.007	-0.003	3.905	3.800	3.916	0.010	-0.030	-0.097	0.000
9	A	13	GLN	0	0.002	0.026	2.433	-3.468	-1.689	0.857	-1.172	-1.464	-0.012
42	A	46	TRP	0	-0.032	-0.017	2.404	-5.067	-4.289	0.400	-0.241	-0.938	-0.002
45	A	49	ARG	1	0.835	0.919	2.371	41.457	42.735	0.704	-0.503	-1.479	-0.001
46	A	50	LYS	1	0.874	0.943	4.477	39.386	39.631	-0.001	-0.026	-0.218	0.000
8	A	12	LEU	0	0.048	0.020	6.941	1.904	1.904	0.000	0.000	0.000	0.000
10	A	14	LEU	0	0.021	0.008	6.943	2.514	2.514	0.000	0.000	0.000	0.000
11	A	15	LEU	0	-0.045	-0.032	9.400	1.706	1.706	0.000	0.000	0.000	0.000
12	A	16	ARG	1	0.864	0.936	7.112	27.884	27.884	0.000	0.000	0.000	0.000
13	A	17	GLU	-1	-0.849	-0.925	7.906	-27.872	-27.872	0.000	0.000	0.000	0.000
14	A	18	GLN	0	-0.047	-0.014	11.820	1.375	1.375	0.000	0.000	0.000	0.000
15	A	19	GLY	0	0.028	0.018	14.090	0.393	0.393	0.000	0.000	0.000	0.000
16	A	20	ASN	0	-0.031	-0.022	17.229	0.580	0.580	0.000	0.000	0.000	0.000
17	A	21	GLY	0	0.050	0.025	17.192	-0.724	-0.724	0.000	0.000	0.000	0.000
18	A	22	HIS	0	0.006	-0.003	18.865	-0.082	-0.082	0.000	0.000	0.000	0.000
19	A	23	ILE	0	0.054	0.023	12.595	0.064	0.064	0.000	0.000	0.000	0.000
20	A	24	ILE	0	-0.062	-0.030	11.145	-0.487	-0.487	0.000	0.000	0.000	0.000
21	A	25	SER	0	0.032	0.016	15.167	0.402	0.402	0.000	0.000	0.000	0.000
22	A	26	TRP	0	0.015	0.005	13.159	-0.190	-0.190	0.000	0.000	0.000	0.000
23	A	27	THR	0	-0.057	-0.034	17.862	0.308	0.308	0.000	0.000	0.000	0.000
24	A	28	SER	0	0.059	0.024	20.250	0.576	0.576	0.000	0.000	0.000	0.000
25	A	29	ARG	1	0.976	0.991	15.966	15.522	15.522	0.000	0.000	0.000	0.000
26	A	30	ASP	-1	-0.866	-0.915	18.941	-12.963	-12.963	0.000	0.000	0.000	0.000
27	A	31	GLY	0	0.004	0.013	21.225	-0.039	-0.039	0.000	0.000	0.000	0.000
28	A	32	GLY	0	0.066	0.031	16.789	-0.301	-0.301	0.000	0.000	0.000	0.000
29	A	33	GLU	-1	-0.931	-0.953	16.194	-13.896	-13.896	0.000	0.000	0.000	0.000
30	A	34	PHE	0	0.041	0.013	12.282	-0.099	-0.099	0.000	0.000	0.000	0.000
31	A	35	LYS	1	0.943	0.975	16.598	12.830	12.830	0.000	0.000	0.000	0.000
32	A	36	LEU	0	-0.013	-0.010	12.378	-0.526	-0.526	0.000	0.000	0.000	0.000
33	A	37	VAL	0	-0.050	-0.025	16.077	0.733	0.733	0.000	0.000	0.000	0.000
34	A	38	ASP	-1	-0.815	-0.899	17.295	-14.440	-14.440	0.000	0.000	0.000	0.000
35	A	39	ALA	0	-0.024	-0.029	15.733	-1.064	-1.064	0.000	0.000	0.000	0.000
36	A	40	GLU	-1	-0.807	-0.908	14.975	-17.159	-17.159	0.000	0.000	0.000	0.000
37	A	41	GLU	-1	-0.756	-0.821	14.821	-18.628	-18.628	0.000	0.000	0.000	0.000
38	A	42	VAL	0	0.004	-0.003	10.295	-1.587	-1.587	0.000	0.000	0.000	0.000
39	A	43	ALA	0	-0.038	-0.017	10.219	-2.444	-2.444	0.000	0.000	0.000	0.000
40	A	44	ARG	1	0.855	0.879	10.639	16.201	16.201	0.000	0.000	0.000	0.000
41	A	45	LEU	0	0.016	0.005	8.912	-1.354	-1.354	0.000	0.000	0.000	0.000
43	A	47	GLY	0	-0.022	-0.022	6.382	-2.999	-2.999	0.000	0.000	0.000	0.000
44	A	48	LEU	0	0.039	0.025	8.668	-1.191	-1.191	0.000	0.000	0.000	0.000
47	A	51	ASN	0	0.013	0.015	6.749	2.688	2.688	0.000	0.000	0.000	0.000
48	A	52	LYS	1	0.899	0.952	10.118	24.238	24.238	0.000	0.000	0.000	0.000
49	A	53	THR	0	0.070	0.025	11.741	-0.739	-0.739	0.000	0.000	0.000	0.000
50	A	54	ASN	0	0.013	0.014	14.348	-0.616	-0.616	0.000	0.000	0.000	0.000
51	A	55	MET	0	-0.064	-0.008	9.387	0.743	0.743	0.000	0.000	0.000	0.000
52	A	56	ASN	0	0.088	0.031	12.994	-0.171	-0.171	0.000	0.000	0.000	0.000
53	A	57	TYR	0	0.080	0.027	14.205	-1.225	-1.225	0.000	0.000	0.000	0.000
54	A	58	ASP	-1	-0.917	-0.930	15.878	-15.780	-15.780	0.000	0.000	0.000	0.000
55	A	59	LYS	1	0.920	0.946	13.659	18.031	18.031	0.000	0.000	0.000	0.000
56	A	60	LEU	0	-0.001	0.012	9.867	-1.136	-1.136	0.000	0.000	0.000	0.000
57	A	61	SER	0	0.003	-0.019	12.232	-0.443	-0.443	0.000	0.000	0.000	0.000
58	A	62	ARG	1	0.915	0.955	15.219	17.447	17.447	0.000	0.000	0.000	0.000
59	A	63	ALA	0	-0.001	0.006	10.628	0.168	0.168	0.000	0.000	0.000	0.000
60	A	64	LEU	0	-0.002	-0.005	10.649	-0.393	-0.393	0.000	0.000	0.000	0.000
61	A	65	ARG	1	0.910	0.939	13.373	16.389	16.389	0.000	0.000	0.000	0.000
62	A	66	TYR	0	-0.038	-0.011	11.512	1.355	1.355	0.000	0.000	0.000	0.000
63	A	67	TYR	0	0.013	-0.012	7.621	-1.349	-1.349	0.000	0.000	0.000	0.000
64	A	68	TYR	0	0.040	0.032	14.076	0.390	0.390	0.000	0.000	0.000	0.000
65	A	69	ASP	-1	-0.828	-0.910	17.678	-14.714	-14.714	0.000	0.000	0.000	0.000
66	A	70	LYS	1	0.860	0.935	13.928	19.185	19.185	0.000	0.000	0.000	0.000
67	A	71	ASN	0	-0.025	-0.004	15.940	0.144	0.144	0.000	0.000	0.000	0.000
68	A	72	ILE	0	0.013	0.027	10.304	-0.350	-0.350	0.000	0.000	0.000	0.000
69	A	73	ILE	0	-0.016	-0.020	10.173	-0.152	-0.152	0.000	0.000	0.000	0.000
70	A	74	ARG	1	0.879	0.934	14.322	15.525	15.525	0.000	0.000	0.000	0.000
71	A	75	LYS	1	0.774	0.877	17.310	13.405	13.405	0.000	0.000	0.000	0.000
72	A	76	VAL	0	0.049	0.035	19.512	0.382	0.382	0.000	0.000	0.000	0.000
73	A	77	SER	0	0.023	-0.001	21.815	-0.126	-0.126	0.000	0.000	0.000	0.000
74	A	78	GLY	0	0.036	0.025	25.077	0.130	0.130	0.000	0.000	0.000	0.000
75	A	79	GLN	0	0.043	0.030	23.491	0.096	0.096	0.000	0.000	0.000	0.000
76	A	80	LYS	1	0.954	0.965	22.972	11.008	11.008	0.000	0.000	0.000	0.000
77	A	81	PHE	0	0.017	-0.003	18.388	0.178	0.178	0.000	0.000	0.000	0.000
78	A	82	VAL	0	0.007	0.024	17.754	-0.727	-0.727	0.000	0.000	0.000	0.000
79	A	83	TYR	0	-0.038	-0.027	15.083	0.301	0.301	0.000	0.000	0.000	0.000
80	A	84	LYS	1	0.868	0.909	16.571	14.067	14.067	0.000	0.000	0.000	0.000
81	A	85	PHE	0	-0.011	-0.010	9.409	-0.776	-0.776	0.000	0.000	0.000	0.000
82	A	86	VAL	0	-0.032	-0.016	14.662	0.964	0.964	0.000	0.000	0.000	0.000
83	A	87	SER	0	-0.004	0.006	13.838	0.781	0.781	0.000	0.000	0.000	0.000
84	A	88	TYR	0	0.007	-0.004	14.503	-0.859	-0.859	0.000	0.000	0.000	0.000
85	A	89	PRO	0	-0.086	-0.057	12.496	-0.850	-0.850	0.000	0.000	0.000	0.000
86	A	90	GLU	-2	-1.892	-1.914	10.995	-40.203	-40.203	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:5:VAL)