FMO DATABASE

FMODB ID: 7Y35K

Calculation Name: 4Z8E-A-Xray540

Preferred Name: Transcriptional enhancer factor TEF-1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4Z8E

Chain ID: A

ChEMBL ID: CHEMBL3334416

UniProt ID: P28347

Base Structure: X-ray

Registration Date: 2025-07-11

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-264839.056007
FMO2-HF: Nuclear repulsion	241246.281397
FMO2-HF: Total energy	-23592.77461
FMO2-MP2: Total energy	-23662.138927

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:16:ASN)

Summations of interaction energy for fragment #1(A:16:ASN)

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.
-3.22	-0.595	-0.014	-1.311	-1.299	-0.003

Interaction energy analysis for fragmet #1(A:16:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.159 / q_NPA : 0.092

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].
4	A	17	ASP	-1	-0.949	-0.830	4.138	-2.680	-1.886	0.001	-0.313	-0.481	-0.001
5	A	18	ALA	0	0.101	-0.088	3.918	-0.614	1.189	-0.014	-0.995	-0.794	-0.002
6	A	18	ALA	0	-0.085	0.097	5.633	0.142	0.142	0.000	0.000	0.000	0.000
7	A	19	GLU	0	0.117	-0.097	6.270	0.162	0.162	0.000	0.000	0.000	0.000
8	A	19	GLU	-1	-1.024	-0.862	9.099	-0.426	-0.426	0.000	0.000	0.000	0.000
9	A	20	GLY	0	-0.038	-0.128	7.900	0.157	0.157	0.000	0.000	0.000	0.000
10	A	21	VAL	0	0.046	0.009	6.810	0.213	0.213	0.000	0.000	0.000	0.000
11	A	21	VAL	0	-0.132	0.050	4.767	-0.169	-0.141	-0.001	-0.003	-0.024	0.000
12	A	22	TRP	0	-0.012	-0.085	7.938	0.170	0.170	0.000	0.000	0.000	0.000
13	A	22	TRP	0	-0.106	0.069	8.433	0.054	0.054	0.000	0.000	0.000	0.000
14	A	23	SER	0	0.163	-0.044	10.924	0.078	0.078	0.000	0.000	0.000	0.000
15	A	23	SER	0	-0.038	0.048	12.573	-0.019	-0.019	0.000	0.000	0.000	0.000
16	A	24	PRO	0	-0.009	-0.121	13.368	0.039	0.039	0.000	0.000	0.000	0.000
17	A	25	ASP	0	0.051	0.025	16.992	0.033	0.033	0.000	0.000	0.000	0.000
18	A	25	ASP	-1	-0.861	-0.802	16.346	-0.456	-0.456	0.000	0.000	0.000	0.000
19	A	26	ILE	0	0.068	-0.119	14.439	0.069	0.069	0.000	0.000	0.000	0.000
20	A	26	ILE	0	-0.081	0.120	12.476	0.003	0.003	0.000	0.000	0.000	0.000
21	A	27	GLU	0	0.136	-0.095	15.499	0.019	0.019	0.000	0.000	0.000	0.000
22	A	27	GLU	-1	-0.935	-0.806	14.839	-0.394	-0.394	0.000	0.000	0.000	0.000
23	A	28	GLN	0	0.074	-0.111	16.222	0.029	0.029	0.000	0.000	0.000	0.000
24	A	28	GLN	0	-0.132	0.060	20.669	0.000	0.000	0.000	0.000	0.000	0.000
25	A	29	SER	0	0.003	-0.114	19.245	0.032	0.032	0.000	0.000	0.000	0.000
26	A	29	SER	0	-0.062	0.073	18.557	0.006	0.006	0.000	0.000	0.000	0.000
27	A	30	PHE	0	0.045	-0.094	16.721	0.036	0.036	0.000	0.000	0.000	0.000
28	A	30	PHE	0	-0.088	0.092	16.004	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	31	GLN	0	0.058	-0.111	18.134	0.017	0.017	0.000	0.000	0.000	0.000
30	A	31	GLN	0	-0.123	0.070	17.862	0.031	0.031	0.000	0.000	0.000	0.000
31	A	32	GLU	0	0.111	-0.102	20.744	0.024	0.024	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.952	-0.809	23.018	-0.201	-0.201	0.000	0.000	0.000	0.000
33	A	33	ALA	0	0.097	-0.111	21.384	0.029	0.029	0.000	0.000	0.000	0.000
34	A	33	ALA	0	-0.091	0.107	20.441	-0.004	-0.004	0.000	0.000	0.000	0.000
35	A	34	LEU	0	0.031	-0.117	21.340	0.018	0.018	0.000	0.000	0.000	0.000
36	A	34	LEU	0	-0.091	0.111	19.453	0.002	0.002	0.000	0.000	0.000	0.000
37	A	35	SER	0	-0.035	-0.104	22.261	0.016	0.016	0.000	0.000	0.000	0.000
38	A	35	SER	0	-0.072	0.043	25.583	0.006	0.006	0.000	0.000	0.000	0.000
39	A	36	ILE	0	0.022	-0.100	25.478	0.016	0.016	0.000	0.000	0.000	0.000
40	A	36	ILE	0	-0.111	0.088	25.717	0.001	0.001	0.000	0.000	0.000	0.000
41	A	37	TYR	0	0.017	-0.147	24.904	0.018	0.018	0.000	0.000	0.000	0.000
42	A	37	TYR	0	-0.110	0.105	23.374	0.007	0.007	0.000	0.000	0.000	0.000
43	A	38	PRO	0	-0.001	-0.094	24.664	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	39	GLY	0	0.078	0.029	24.633	-0.004	-0.004	0.000	0.000	0.000	0.000
45	A	40	LYS	0	0.089	0.016	25.345	0.005	0.005	0.000	0.000	0.000	0.000
46	A	40	LYS	1	0.798	1.026	29.122	0.065	0.065	0.000	0.000	0.000	0.000
47	A	41	MET	0	0.165	-0.070	29.005	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	41	MET	0	-0.112	0.114	31.596	0.003	0.003	0.000	0.000	0.000	0.000
49	A	42	TYR	0	0.018	-0.153	32.057	0.007	0.007	0.000	0.000	0.000	0.000
50	A	42	TYR	0	-0.007	0.158	30.047	0.006	0.006	0.000	0.000	0.000	0.000
51	A	43	GLY	0	0.084	-0.075	34.533	0.000	0.000	0.000	0.000	0.000	0.000
52	A	44	ARG	0	0.117	-0.008	36.669	0.003	0.003	0.000	0.000	0.000	0.000
53	A	44	ARG	1	0.913	1.095	34.751	0.046	0.046	0.000	0.000	0.000	0.000
54	A	45	ASN	0	0.066	-0.086	37.822	0.002	0.002	0.000	0.000	0.000	0.000
55	A	45	ASN	0	-0.097	0.075	38.932	-0.001	-0.001	0.000	0.000	0.000	0.000
56	A	46	GLU	0	0.095	-0.123	40.764	0.004	0.004	0.000	0.000	0.000	0.000
57	A	46	GLU	-1	-0.890	-0.799	40.991	-0.048	-0.048	0.000	0.000	0.000	0.000
58	A	47	LEU	0	0.055	-0.107	40.789	0.003	0.003	0.000	0.000	0.000	0.000
59	A	47	LEU	0	-0.037	0.129	38.275	0.000	0.000	0.000	0.000	0.000	0.000
60	A	48	ILE	0	0.098	-0.089	41.719	0.001	0.001	0.000	0.000	0.000	0.000
61	A	48	ILE	0	-0.098	0.097	39.134	0.000	0.000	0.000	0.000	0.000	0.000
62	A	49	ALA	0	0.114	-0.094	43.106	0.002	0.002	0.000	0.000	0.000	0.000
63	A	49	ALA	0	-0.080	0.100	45.806	0.000	0.000	0.000	0.000	0.000	0.000
64	A	50	ARG	0	0.081	-0.085	45.604	0.002	0.002	0.000	0.000	0.000	0.000
65	A	50	ARG	1	0.876	1.074	45.020	0.041	0.041	0.000	0.000	0.000	0.000
66	A	51	TYR	0	0.104	-0.089	45.344	0.001	0.001	0.000	0.000	0.000	0.000
67	A	51	TYR	0	-0.055	0.110	44.552	0.000	0.000	0.000	0.000	0.000	0.000
68	A	52	ILE	0	0.097	-0.090	46.643	0.001	0.001	0.000	0.000	0.000	0.000
69	A	52	ILE	0	-0.097	0.085	46.244	0.000	0.000	0.000	0.000	0.000	0.000
70	A	53	LYS	0	0.084	-0.068	48.958	0.002	0.002	0.000	0.000	0.000	0.000
71	A	53	LYS	1	0.769	1.014	50.564	0.024	0.024	0.000	0.000	0.000	0.000
72	A	54	LEU	0	0.067	-0.106	50.206	0.002	0.002	0.000	0.000	0.000	0.000
73	A	54	LEU	0	-0.086	0.084	48.226	0.000	0.000	0.000	0.000	0.000	0.000
74	A	55	ARG	0	0.046	-0.107	50.618	0.001	0.001	0.000	0.000	0.000	0.000
75	A	55	ARG	1	0.845	1.060	46.912	0.031	0.031	0.000	0.000	0.000	0.000
76	A	56	THR	0	0.020	-0.083	51.811	0.001	0.001	0.000	0.000	0.000	0.000
77	A	56	THR	0	-0.096	0.033	51.855	0.000	0.000	0.000	0.000	0.000	0.000
78	A	57	GLY	0	0.105	-0.024	54.104	0.001	0.001	0.000	0.000	0.000	0.000
79	A	58	LYS	0	0.035	-0.003	54.572	0.000	0.000	0.000	0.000	0.000	0.000
80	A	58	LYS	1	0.898	1.078	54.266	0.018	0.018	0.000	0.000	0.000	0.000
81	A	59	THR	0	0.006	-0.091	52.720	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	59	THR	0	0.017	0.089	52.797	0.000	0.000	0.000	0.000	0.000	0.000
83	A	60	ARG	0	0.084	-0.084	50.128	0.002	0.002	0.000	0.000	0.000	0.000
84	A	60	ARG	1	0.888	1.090	49.414	0.019	0.019	0.000	0.000	0.000	0.000
85	A	61	THR	0	0.119	-0.019	48.844	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	61	THR	0	-0.080	0.047	48.470	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	62	ARG	0	0.133	-0.072	44.599	0.001	0.001	0.000	0.000	0.000	0.000
88	A	62	ARG	1	0.849	1.036	42.533	0.041	0.041	0.000	0.000	0.000	0.000
89	A	63	LYS	0	0.032	-0.136	43.817	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	63	LYS	1	0.935	1.107	43.540	0.029	0.029	0.000	0.000	0.000	0.000
91	A	64	GLN	0	0.135	-0.068	45.212	0.001	0.001	0.000	0.000	0.000	0.000
92	A	64	GLN	0	0.006	0.108	48.511	-0.001	-0.001	0.000	0.000	0.000	0.000
93	A	65	VAL	0	0.103	-0.067	44.190	0.002	0.002	0.000	0.000	0.000	0.000
94	A	65	VAL	0	-0.130	0.106	42.019	0.000	0.000	0.000	0.000	0.000	0.000
95	A	66	SER	0	0.061	-0.077	40.855	0.000	0.000	0.000	0.000	0.000	0.000
96	A	66	SER	0	-0.062	0.035	40.320	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	67	SER	0	0.051	-0.080	41.234	0.000	0.000	0.000	0.000	0.000	0.000
98	A	67	SER	0	-0.023	0.080	45.278	0.000	0.000	0.000	0.000	0.000	0.000
99	A	68	HIS	0	0.058	-0.084	43.639	0.002	0.002	0.000	0.000	0.000	0.000
100	A	68	HIS	0	-0.086	0.091	44.274	0.000	0.000	0.000	0.000	0.000	0.000
101	A	69	ILE	0	0.118	-0.061	39.651	0.002	0.002	0.000	0.000	0.000	0.000
102	A	69	ILE	0	-0.123	0.051	37.564	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	70	GLN	0	0.056	-0.104	38.972	0.000	0.000	0.000	0.000	0.000	0.000
104	A	70	GLN	0	-0.080	0.082	38.435	0.002	0.002	0.000	0.000	0.000	0.000
105	A	71	VAL	0	0.065	-0.070	40.032	0.002	0.002	0.000	0.000	0.000	0.000
106	A	71	VAL	0	-0.068	0.086	44.456	0.000	0.000	0.000	0.000	0.000	0.000
107	A	72	LEU	0	0.048	-0.112	41.861	0.003	0.003	0.000	0.000	0.000	0.000
108	A	72	LEU	0	-0.112	0.084	41.222	0.000	0.000	0.000	0.000	0.000	0.000
109	A	73	ALA	0	0.138	-0.057	37.322	0.001	0.001	0.000	0.000	0.000	0.000
110	A	73	ALA	0	-0.101	0.080	36.327	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	74	ARG	0	-0.070	-0.089	37.490	0.002	0.002	0.000	0.000	0.000	0.000
112	A	74	ARG	1	0.926	0.954	38.225	0.014	0.014	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:16:ASN)