FMO DATABASE

FMODB ID: K92Z3

Calculation Name: 4ATI-A-Xray372

Preferred Name: Microphthalmia-associated transcription factor

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 4ATI

Chain ID: A

ChEMBL ID: CHEMBL1075142

UniProt ID: Q08874

Base Structure: X-ray

Registration Date: 2023-06-22

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

DOI:

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	61
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-320950.026531
FMO2-HF: Nuclear repulsion	295312.17743
FMO2-HF: Total energy	-25637.849101
FMO2-MP2: Total energy	-25713.622843

3D Structure

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:209:HIS)

Summations of interaction energy for fragment #1(A:209:HIS)

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.
2.129	5.854	1.197	-1.514	-3.409	0.004

Interaction energy analysis for fragmet #1(A:209:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.064 / q_NPA : 0.022

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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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	211	LEU	0	-0.017	0.001	3.559	-2.668	-0.845	-0.002	-0.767	-1.054	0.003
4	A	212	ILE	0	0.038	0.004	2.337	-1.716	-0.303	1.198	-0.656	-1.956	0.001
5	A	213	GLU	-1	-0.694	-0.807	3.477	-2.846	-2.357	0.001	-0.091	-0.399	0.000
6	A	214	ARG	1	0.928	0.975	5.481	1.640	1.640	0.000	0.000	0.000	0.000
7	A	215	ARG	1	0.961	0.966	6.377	0.870	0.870	0.000	0.000	0.000	0.000
8	A	216	ARG	1	0.940	0.970	7.634	1.981	1.981	0.000	0.000	0.000	0.000
9	A	217	ARG	1	0.810	0.878	6.671	2.928	2.928	0.000	0.000	0.000	0.000
10	A	218	PHE	0	0.035	0.005	11.108	0.174	0.174	0.000	0.000	0.000	0.000
11	A	219	ASN	0	0.051	0.038	12.948	0.173	0.173	0.000	0.000	0.000	0.000
12	A	220	ILE	0	0.019	0.011	12.137	0.083	0.083	0.000	0.000	0.000	0.000
13	A	221	ASN	0	-0.005	-0.020	13.862	0.114	0.114	0.000	0.000	0.000	0.000
14	A	222	ASP	-1	-0.805	-0.899	16.901	-0.430	-0.430	0.000	0.000	0.000	0.000
15	A	223	ARG	1	0.879	0.929	18.428	0.382	0.382	0.000	0.000	0.000	0.000
16	A	224	ILE	0	-0.033	-0.011	18.429	0.029	0.029	0.000	0.000	0.000	0.000
17	A	225	LYS	1	0.851	0.912	18.636	0.482	0.482	0.000	0.000	0.000	0.000
18	A	226	GLU	-1	-0.842	-0.895	22.600	-0.253	-0.253	0.000	0.000	0.000	0.000
19	A	227	LEU	0	-0.008	-0.006	23.304	0.022	0.022	0.000	0.000	0.000	0.000
20	A	228	GLY	0	-0.026	-0.020	25.710	0.018	0.018	0.000	0.000	0.000	0.000
21	A	229	THR	0	-0.055	-0.021	27.502	0.016	0.016	0.000	0.000	0.000	0.000
22	A	230	LEU	0	-0.010	-0.001	28.760	0.013	0.013	0.000	0.000	0.000	0.000
23	A	231	ILE	0	-0.060	-0.007	29.019	0.011	0.011	0.000	0.000	0.000	0.000
24	A	232	PRO	0	-0.001	0.011	32.204	-0.001	-0.001	0.000	0.000	0.000	0.000
25	A	233	LYS	1	0.959	0.965	33.912	0.141	0.141	0.000	0.000	0.000	0.000
26	A	234	SER	0	-0.087	-0.055	36.071	0.002	0.002	0.000	0.000	0.000	0.000
27	A	235	ASN	0	-0.021	-0.032	37.735	0.003	0.003	0.000	0.000	0.000	0.000
28	A	236	ASP	-1	-0.761	-0.853	37.717	-0.117	-0.117	0.000	0.000	0.000	0.000
29	A	237	PRO	0	-0.026	-0.016	38.874	-0.006	-0.006	0.000	0.000	0.000	0.000
30	A	238	ASP	-1	-0.947	-0.972	37.394	-0.124	-0.124	0.000	0.000	0.000	0.000
31	A	239	MET	0	-0.025	0.013	32.308	-0.014	-0.014	0.000	0.000	0.000	0.000
32	A	240	ARG	1	0.979	0.999	27.438	0.202	0.202	0.000	0.000	0.000	0.000
33	A	241	TRP	0	0.023	0.023	27.969	-0.014	-0.014	0.000	0.000	0.000	0.000
34	A	242	ASN	0	-0.023	-0.019	24.507	-0.018	-0.018	0.000	0.000	0.000	0.000
35	A	243	LYS	1	0.930	0.948	16.029	0.654	0.654	0.000	0.000	0.000	0.000
36	A	244	GLY	0	0.025	0.004	22.377	0.006	0.006	0.000	0.000	0.000	0.000
37	A	245	THR	0	0.014	-0.031	24.036	0.004	0.004	0.000	0.000	0.000	0.000
38	A	246	ILE	0	0.040	0.035	24.691	0.013	0.013	0.000	0.000	0.000	0.000
39	A	247	LEU	0	-0.005	0.001	20.801	0.010	0.010	0.000	0.000	0.000	0.000
40	A	248	LYS	1	0.905	0.939	25.459	0.165	0.165	0.000	0.000	0.000	0.000
41	A	249	ALA	0	0.020	0.021	28.561	0.015	0.015	0.000	0.000	0.000	0.000
42	A	250	SER	0	0.026	0.002	27.111	0.007	0.007	0.000	0.000	0.000	0.000
43	A	251	VAL	0	-0.025	-0.007	27.147	0.012	0.012	0.000	0.000	0.000	0.000
44	A	252	ASP	-1	-0.821	-0.919	29.839	-0.132	-0.132	0.000	0.000	0.000	0.000
45	A	253	TYR	0	0.024	0.023	32.300	0.010	0.010	0.000	0.000	0.000	0.000
46	A	254	ILE	0	0.016	0.007	28.696	0.007	0.007	0.000	0.000	0.000	0.000
47	A	255	ARG	1	0.900	0.945	31.266	0.145	0.145	0.000	0.000	0.000	0.000
48	A	256	LYS	1	0.834	0.908	35.356	0.101	0.101	0.000	0.000	0.000	0.000
49	A	257	LEU	0	0.023	0.018	34.545	0.007	0.007	0.000	0.000	0.000	0.000
50	A	258	GLN	0	0.042	0.016	33.569	0.004	0.004	0.000	0.000	0.000	0.000
51	A	259	ARG	1	0.929	0.966	38.167	0.083	0.083	0.000	0.000	0.000	0.000
52	A	260	GLU	-1	-0.879	-0.924	40.955	-0.091	-0.091	0.000	0.000	0.000	0.000
53	A	261	GLN	0	0.027	0.013	37.809	0.002	0.002	0.000	0.000	0.000	0.000
54	A	262	GLN	0	-0.030	-0.014	41.820	0.002	0.002	0.000	0.000	0.000	0.000
55	A	263	ARG	1	0.920	0.954	43.694	0.067	0.067	0.000	0.000	0.000	0.000
56	A	264	ALA	0	0.016	0.006	44.525	0.003	0.003	0.000	0.000	0.000	0.000
57	A	265	LYS	1	0.792	0.882	43.973	0.067	0.067	0.000	0.000	0.000	0.000
58	A	266	ASP	-1	-0.844	-0.909	46.685	-0.058	-0.058	0.000	0.000	0.000	0.000
59	A	267	LEU	0	-0.047	-0.009	49.934	0.002	0.002	0.000	0.000	0.000	0.000
60	A	268	GLU	-1	-0.904	-0.933	48.706	-0.056	-0.056	0.000	0.000	0.000	0.000
61	A	269	ASN	0	-0.079	-0.045	50.790	0.003	0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:209:HIS)