FMO DATABASE

FMODB ID: G8GN1

Calculation Name: 1TP5-A-Xray547

Preferred Name: Disks large homolog 4

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1TP5

Chain ID: A

ChEMBL ID: CHEMBL3797015

UniProt ID: P31016

Base Structure: X-ray

Registration Date: 2025-10-03

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	115
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-852694.282805
FMO2-HF: Nuclear repulsion	810113.798914
FMO2-HF: Total energy	-42580.483891
FMO2-MP2: Total energy	-42707.738806

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:301:PHE)

Summations of interaction energy for fragment #1(A:301:PHE)

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.
-199.734	-194.56	16.138	-11.578	-9.736	-0.136

Interaction energy analysis for fragmet #1(A:301:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.760 / q_NPA : 0.862

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	303	GLY	0	-0.068	-0.031	3.238	8.325	9.872	0.003	-0.589	-0.962	-0.001
4	A	304	GLU	-1	-0.851	-0.916	1.722	-116.542	-115.445	13.959	-9.034	-6.022	-0.112
5	A	305	GLU	-1	-0.894	-0.943	2.508	-56.927	-54.397	2.176	-1.955	-2.752	-0.023
6	A	306	ASP	-1	-0.882	-0.937	6.060	-25.746	-25.746	0.000	0.000	0.000	0.000
7	A	307	ILE	0	-0.059	-0.019	9.858	0.264	0.264	0.000	0.000	0.000	0.000
8	A	308	PRO	0	-0.018	-0.016	11.590	1.642	1.642	0.000	0.000	0.000	0.000
9	A	309	ARG	1	0.836	0.879	14.416	19.048	19.048	0.000	0.000	0.000	0.000
10	A	310	GLU	-1	-0.948	-0.951	17.775	-13.721	-13.721	0.000	0.000	0.000	0.000
11	A	311	PRO	0	-0.049	-0.042	19.893	-0.389	-0.389	0.000	0.000	0.000	0.000
12	A	312	ARG	1	0.822	0.882	17.890	16.503	16.503	0.000	0.000	0.000	0.000
13	A	313	ARG	1	0.929	0.949	21.662	11.990	11.990	0.000	0.000	0.000	0.000
14	A	314	ILE	0	0.032	0.039	21.646	-0.175	-0.175	0.000	0.000	0.000	0.000
15	A	315	VAL	0	-0.050	-0.037	24.011	0.667	0.667	0.000	0.000	0.000	0.000
16	A	316	ILE	0	0.045	0.033	24.794	-0.070	-0.070	0.000	0.000	0.000	0.000
17	A	317	HIS	0	0.030	0.025	27.225	0.742	0.742	0.000	0.000	0.000	0.000
18	A	318	ARG	1	0.834	0.917	29.301	9.172	9.172	0.000	0.000	0.000	0.000
19	A	319	GLY	0	-0.001	0.021	31.347	0.179	0.179	0.000	0.000	0.000	0.000
20	A	320	SER	0	-0.001	-0.018	35.021	0.091	0.091	0.000	0.000	0.000	0.000
21	A	321	THR	0	-0.019	-0.015	32.449	0.016	0.016	0.000	0.000	0.000	0.000
22	A	322	GLY	0	0.024	0.007	32.528	-0.022	-0.022	0.000	0.000	0.000	0.000
23	A	323	LEU	0	0.041	0.005	28.318	-0.188	-0.188	0.000	0.000	0.000	0.000
24	A	324	GLY	0	0.012	0.013	26.847	-0.383	-0.383	0.000	0.000	0.000	0.000
25	A	325	PHE	0	-0.011	-0.001	24.908	-0.513	-0.513	0.000	0.000	0.000	0.000
26	A	326	ASN	0	-0.012	0.002	26.189	0.609	0.609	0.000	0.000	0.000	0.000
27	A	327	ILE	0	-0.006	-0.009	26.713	-0.488	-0.488	0.000	0.000	0.000	0.000
28	A	328	VAL	0	-0.007	-0.008	26.947	0.274	0.274	0.000	0.000	0.000	0.000
29	A	329	GLY	0	0.066	0.049	29.735	-0.220	-0.220	0.000	0.000	0.000	0.000
30	A	330	GLY	0	0.011	-0.017	31.685	0.140	0.140	0.000	0.000	0.000	0.000
31	A	331	GLU	-1	-0.971	-0.988	34.765	-8.425	-8.425	0.000	0.000	0.000	0.000
32	A	332	ASP	-1	-0.952	-0.992	36.199	-8.161	-8.161	0.000	0.000	0.000	0.000
33	A	333	GLY	0	-0.017	-0.002	36.430	0.001	0.001	0.000	0.000	0.000	0.000
34	A	334	GLU	-1	-0.876	-0.929	32.088	-10.068	-10.068	0.000	0.000	0.000	0.000
35	A	335	GLY	0	0.006	0.013	30.318	-0.427	-0.427	0.000	0.000	0.000	0.000
36	A	336	ILE	0	-0.033	-0.015	29.778	0.093	0.093	0.000	0.000	0.000	0.000
37	A	337	PHE	0	0.007	-0.011	24.646	-0.474	-0.474	0.000	0.000	0.000	0.000
38	A	338	ILE	0	-0.017	0.000	22.611	0.407	0.407	0.000	0.000	0.000	0.000
39	A	339	SER	0	0.031	0.010	23.222	-0.580	-0.580	0.000	0.000	0.000	0.000
40	A	340	PHE	0	-0.023	-0.014	22.606	-0.506	-0.506	0.000	0.000	0.000	0.000
41	A	341	ILE	0	0.016	0.004	19.734	0.449	0.449	0.000	0.000	0.000	0.000
42	A	342	LEU	0	-0.046	-0.012	22.254	-0.222	-0.222	0.000	0.000	0.000	0.000
43	A	343	ALA	0	0.034	0.015	21.123	-0.060	-0.060	0.000	0.000	0.000	0.000
44	A	344	GLY	0	-0.013	-0.016	22.143	0.622	0.622	0.000	0.000	0.000	0.000
45	A	345	GLY	0	-0.025	-0.009	24.046	0.555	0.555	0.000	0.000	0.000	0.000
46	A	346	PRO	0	-0.020	-0.029	24.024	-0.503	-0.503	0.000	0.000	0.000	0.000
47	A	347	ALA	0	0.016	0.014	23.171	-0.235	-0.235	0.000	0.000	0.000	0.000
48	A	348	ASP	-1	-0.837	-0.896	18.999	-16.388	-16.388	0.000	0.000	0.000	0.000
49	A	349	LEU	0	-0.047	-0.029	19.322	-0.602	-0.602	0.000	0.000	0.000	0.000
50	A	350	SER	0	-0.063	-0.029	20.760	-0.093	-0.093	0.000	0.000	0.000	0.000
51	A	351	GLY	0	0.017	0.013	16.540	-0.395	-0.395	0.000	0.000	0.000	0.000
52	A	352	GLU	-1	-0.920	-0.968	15.942	-15.546	-15.546	0.000	0.000	0.000	0.000
53	A	353	LEU	0	-0.041	-0.019	18.351	0.228	0.228	0.000	0.000	0.000	0.000
54	A	354	ARG	1	0.936	0.968	12.143	22.162	22.162	0.000	0.000	0.000	0.000
55	A	355	LYS	1	0.851	0.915	18.489	16.642	16.642	0.000	0.000	0.000	0.000
56	A	356	GLY	0	0.065	0.015	18.463	-1.017	-1.017	0.000	0.000	0.000	0.000
57	A	357	ASP	-1	-0.785	-0.859	19.720	-16.751	-16.751	0.000	0.000	0.000	0.000
58	A	358	GLN	0	-0.011	-0.005	21.912	0.857	0.857	0.000	0.000	0.000	0.000
59	A	359	ILE	0	-0.011	-0.017	25.145	-0.226	-0.226	0.000	0.000	0.000	0.000
60	A	360	LEU	0	-0.006	-0.003	25.731	0.435	0.435	0.000	0.000	0.000	0.000
61	A	361	SER	0	-0.003	-0.013	28.877	0.483	0.483	0.000	0.000	0.000	0.000
62	A	362	VAL	0	0.018	0.014	29.826	-0.395	-0.395	0.000	0.000	0.000	0.000
63	A	363	ASN	0	-0.033	-0.025	32.195	0.063	0.063	0.000	0.000	0.000	0.000
64	A	364	GLY	0	-0.003	0.007	33.337	0.276	0.276	0.000	0.000	0.000	0.000
65	A	365	VAL	0	-0.021	-0.005	34.989	0.173	0.173	0.000	0.000	0.000	0.000
66	A	366	ASP	-1	-0.810	-0.888	33.736	-9.718	-9.718	0.000	0.000	0.000	0.000
67	A	367	LEU	0	-0.017	-0.026	31.898	0.253	0.253	0.000	0.000	0.000	0.000
68	A	368	ARG	1	0.848	0.904	30.235	9.654	9.654	0.000	0.000	0.000	0.000
69	A	369	ASN	0	-0.019	-0.010	32.460	-0.029	-0.029	0.000	0.000	0.000	0.000
70	A	370	ALA	0	-0.021	0.008	35.285	0.290	0.290	0.000	0.000	0.000	0.000
71	A	371	SER	0	0.059	0.029	36.140	-0.166	-0.166	0.000	0.000	0.000	0.000
72	A	372	HIS	0	-0.017	-0.012	32.624	0.073	0.073	0.000	0.000	0.000	0.000
73	A	373	GLU	-1	-0.930	-0.969	36.165	-7.780	-7.780	0.000	0.000	0.000	0.000
74	A	374	GLN	0	0.012	0.002	38.666	-0.033	-0.033	0.000	0.000	0.000	0.000
75	A	375	ALA	0	0.041	0.028	33.683	-0.037	-0.037	0.000	0.000	0.000	0.000
76	A	376	ALA	0	0.019	0.010	34.560	-0.164	-0.164	0.000	0.000	0.000	0.000
77	A	377	ILE	0	-0.051	-0.021	35.560	-0.012	-0.012	0.000	0.000	0.000	0.000
78	A	378	ALA	0	0.024	0.020	35.925	0.051	0.051	0.000	0.000	0.000	0.000
79	A	379	LEU	0	0.002	-0.009	30.400	-0.040	-0.040	0.000	0.000	0.000	0.000
80	A	380	LYS	1	0.899	0.950	33.880	8.680	8.680	0.000	0.000	0.000	0.000
81	A	381	ASN	0	-0.049	-0.043	36.205	0.174	0.174	0.000	0.000	0.000	0.000
82	A	382	ALA	0	-0.009	0.021	34.506	0.156	0.156	0.000	0.000	0.000	0.000
83	A	383	GLY	0	0.041	0.029	36.544	0.052	0.052	0.000	0.000	0.000	0.000
84	A	384	GLN	0	-0.010	-0.013	35.272	-0.275	-0.275	0.000	0.000	0.000	0.000
85	A	385	THR	0	-0.014	-0.013	30.916	-0.133	-0.133	0.000	0.000	0.000	0.000
86	A	386	VAL	0	-0.042	-0.015	30.129	0.257	0.257	0.000	0.000	0.000	0.000
87	A	387	THR	0	0.009	0.003	28.679	-0.462	-0.462	0.000	0.000	0.000	0.000
88	A	388	ILE	0	-0.003	-0.003	25.812	0.384	0.384	0.000	0.000	0.000	0.000
89	A	389	ILE	0	-0.041	-0.006	25.880	-0.345	-0.345	0.000	0.000	0.000	0.000
90	A	390	ALA	0	0.031	0.012	22.801	0.286	0.286	0.000	0.000	0.000	0.000
91	A	391	GLN	0	-0.024	-0.020	21.352	0.155	0.155	0.000	0.000	0.000	0.000
92	A	392	TYR	0	-0.035	-0.033	15.209	0.424	0.424	0.000	0.000	0.000	0.000
93	A	393	LYS	1	0.781	0.877	19.659	13.094	13.094	0.000	0.000	0.000	0.000
94	A	394	PRO	0	0.041	0.033	17.218	0.653	0.653	0.000	0.000	0.000	0.000
95	A	395	GLU	-1	-0.721	-0.840	19.192	-16.314	-16.314	0.000	0.000	0.000	0.000
96	A	396	GLU	-1	-0.875	-0.920	22.271	-12.539	-12.539	0.000	0.000	0.000	0.000
97	A	397	TYR	0	-0.002	-0.028	21.612	0.503	0.503	0.000	0.000	0.000	0.000
98	A	398	SER	0	-0.013	-0.018	21.372	0.395	0.395	0.000	0.000	0.000	0.000
99	A	399	ARG	1	0.890	0.952	23.259	11.604	11.604	0.000	0.000	0.000	0.000
100	A	400	PHE	0	-0.040	-0.011	26.380	0.387	0.387	0.000	0.000	0.000	0.000
101	A	401	GLU	-1	-0.825	-0.855	22.362	-14.362	-14.362	0.000	0.000	0.000	0.000
102	A	402	ALA	0	0.025	0.000	25.021	-0.221	-0.221	0.000	0.000	0.000	0.000
103	A	403	ASN	0	-0.046	-0.033	23.493	0.036	0.036	0.000	0.000	0.000	0.000
104	A	404	SER	0	-0.044	0.001	20.749	-0.841	-0.841	0.000	0.000	0.000	0.000
105	A	405	ARG	1	0.818	0.857	15.690	18.386	18.386	0.000	0.000	0.000	0.000
106	A	406	VAL	0	-0.010	-0.003	15.967	-0.769	-0.769	0.000	0.000	0.000	0.000
107	A	407	ASP	-1	-0.810	-0.872	11.326	-26.994	-26.994	0.000	0.000	0.000	0.000
108	A	408	SER	0	0.004	-0.023	11.161	0.636	0.636	0.000	0.000	0.000	0.000
109	A	409	SER	0	-0.053	-0.017	8.969	-1.025	-1.025	0.000	0.000	0.000	0.000
110	A	410	GLY	0	0.013	-0.011	10.876	-0.088	-0.088	0.000	0.000	0.000	0.000
111	A	411	ARG	1	0.817	0.909	7.627	39.289	39.289	0.000	0.000	0.000	0.000
112	A	412	ILE	0	-0.023	0.000	12.953	0.898	0.898	0.000	0.000	0.000	0.000
113	A	413	VAL	0	-0.031	-0.004	13.377	-0.806	-0.806	0.000	0.000	0.000	0.000
114	A	414	THR	0	-0.040	-0.051	16.030	1.044	1.044	0.000	0.000	0.000	0.000
115	A	415	ASP	-2	-1.673	-1.761	18.788	-31.045	-31.045	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:301:PHE)