FMO DATABASE

FMODB ID: G6GJ1

Calculation Name: 5MZ7-A-Xray372

Preferred Name: Disks large homolog 4

Target Type: SINGLE PROTEIN

Ligand Name: azidohomoalanine

ligand 3-letter code: AZH

PDB ID: 5MZ7

Chain ID: A

ChEMBL ID: CHEMBL3797015

UniProt ID: P31016

Base Structure: X-ray

Registration Date: 2023-09-19

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	OptH
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	100
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-694944.552416
FMO2-HF: Nuclear repulsion	657952.755243
FMO2-HF: Total energy	-36991.797172
FMO2-MP2: Total energy	-37102.498441

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:303:GLY)

Summations of interaction energy for fragment #1(A:303:GLY)

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.
-10.926	-6.195	1.863	-3.278	-3.317	-0.022

Interaction energy analysis for fragmet #1(A:303:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.012 / q_NPA : 0.007

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	305	GLU	-1	-0.973	-0.989	2.280	-10.250	-6.624	1.840	-2.668	-2.799	-0.018
4	A	306	ASP	-1	-0.952	-0.972	3.432	-5.007	-3.902	0.023	-0.610	-0.518	-0.004
5	A	307	ILE	0	-0.024	0.012	5.080	1.584	1.584	0.000	0.000	0.000	0.000
6	A	308	PRO	0	-0.005	-0.001	7.335	0.235	0.235	0.000	0.000	0.000	0.000
7	A	309	ARG	1	0.887	0.932	7.344	2.748	2.748	0.000	0.000	0.000	0.000
8	A	310	GLU	-1	-0.924	-0.955	12.928	-0.761	-0.761	0.000	0.000	0.000	0.000
9	A	311	PRO	0	-0.056	-0.042	15.932	-0.024	-0.024	0.000	0.000	0.000	0.000
10	A	312	ARG	1	0.806	0.880	14.067	0.757	0.757	0.000	0.000	0.000	0.000
11	A	313	ARG	1	0.929	0.961	18.505	0.277	0.277	0.000	0.000	0.000	0.000
12	A	314	ILE	0	0.036	0.029	17.175	0.003	0.003	0.000	0.000	0.000	0.000
13	A	315	VAL	0	-0.043	-0.020	20.841	0.020	0.020	0.000	0.000	0.000	0.000
14	A	316	ILE	0	0.032	0.030	20.989	0.007	0.007	0.000	0.000	0.000	0.000
15	A	317	HIS	0	0.033	0.005	24.059	0.008	0.008	0.000	0.000	0.000	0.000
16	A	318	ARG	1	0.825	0.902	26.547	0.117	0.117	0.000	0.000	0.000	0.000
17	A	319	GLY	0	0.013	0.005	28.546	0.008	0.008	0.000	0.000	0.000	0.000
18	A	320	SER	0	-0.026	-0.028	30.601	0.000	0.000	0.000	0.000	0.000	0.000
19	A	321	THR	0	0.012	0.008	26.887	0.007	0.007	0.000	0.000	0.000	0.000
20	A	322	GLY	0	-0.014	0.010	27.854	0.002	0.002	0.000	0.000	0.000	0.000
21	A	323	LEU	0	0.030	-0.007	23.975	0.004	0.004	0.000	0.000	0.000	0.000
22	A	324	GLY	0	0.028	0.018	22.264	-0.010	-0.010	0.000	0.000	0.000	0.000
23	A	325	PHE	0	-0.014	-0.008	19.538	-0.004	-0.004	0.000	0.000	0.000	0.000
24	A	326	ASN	0	-0.033	-0.003	20.831	0.014	0.014	0.000	0.000	0.000	0.000
25	A	327	ILE	0	-0.009	-0.008	20.769	-0.027	-0.027	0.000	0.000	0.000	0.000
26	A	328	ILE	0	-0.003	0.004	20.376	0.028	0.028	0.000	0.000	0.000	0.000
27	A	329	GLY	0	0.036	0.009	22.821	-0.030	-0.030	0.000	0.000	0.000	0.000
28	A	330	GLY	0	0.009	0.010	25.107	0.014	0.014	0.000	0.000	0.000	0.000
29	A	331	GLU	-1	-0.937	-0.979	28.257	-0.117	-0.117	0.000	0.000	0.000	0.000
30	A	332	ASP	-1	-0.922	-0.969	29.544	-0.162	-0.162	0.000	0.000	0.000	0.000
31	A	333	GLY	0	-0.035	-0.018	28.782	0.004	0.004	0.000	0.000	0.000	0.000
32	A	334	GLU	-1	-0.913	-0.938	25.688	-0.192	-0.192	0.000	0.000	0.000	0.000
33	A	335	GLY	0	-0.008	0.005	23.203	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	336	ILE	0	-0.028	-0.016	22.926	0.021	0.021	0.000	0.000	0.000	0.000
35	A	337	PHE	0	0.006	-0.002	17.414	-0.048	-0.048	0.000	0.000	0.000	0.000
36	A	338	ILE	0	-0.032	-0.005	16.521	0.057	0.057	0.000	0.000	0.000	0.000
37	A	339	SER	0	0.056	0.019	16.711	-0.035	-0.035	0.000	0.000	0.000	0.000
38	A	340	PHE	0	-0.056	-0.039	17.489	0.030	0.030	0.000	0.000	0.000	0.000
39	A	341	AZH	0	0.033	0.015	15.651	-0.048	-0.048	0.000	0.000	0.000	0.000
40	A	342	LEU	0	-0.048	-0.021	17.637	0.033	0.033	0.000	0.000	0.000	0.000
41	A	343	ALA	0	0.011	0.007	18.192	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	344	GLY	0	-0.001	-0.010	18.880	0.006	0.006	0.000	0.000	0.000	0.000
43	A	345	GLY	0	-0.033	-0.014	20.582	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	346	PRO	0	-0.018	-0.014	20.525	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	347	ALA	0	0.015	0.006	18.347	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	348	ASP	-1	-0.817	-0.885	15.362	-0.083	-0.083	0.000	0.000	0.000	0.000
47	A	349	LEU	0	-0.058	-0.029	16.063	-0.009	-0.009	0.000	0.000	0.000	0.000
48	A	350	SER	0	-0.062	-0.031	17.178	-0.017	-0.017	0.000	0.000	0.000	0.000
49	A	351	GLY	0	0.013	0.014	13.522	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	352	GLU	-1	-0.977	-0.990	12.550	-0.456	-0.456	0.000	0.000	0.000	0.000
51	A	353	LEU	0	-0.042	-0.023	14.519	-0.051	-0.051	0.000	0.000	0.000	0.000
52	A	354	ARG	1	0.929	0.978	9.063	1.168	1.168	0.000	0.000	0.000	0.000
53	A	355	LYS	1	0.957	0.968	12.220	0.138	0.138	0.000	0.000	0.000	0.000
54	A	356	GLY	0	0.079	0.037	11.956	-0.128	-0.128	0.000	0.000	0.000	0.000
55	A	357	ASP	-1	-0.773	-0.868	13.510	-0.875	-0.875	0.000	0.000	0.000	0.000
56	A	358	GLN	0	0.004	0.002	15.232	0.054	0.054	0.000	0.000	0.000	0.000
57	A	359	ILE	0	-0.029	-0.027	18.553	-0.019	-0.019	0.000	0.000	0.000	0.000
58	A	360	LEU	0	-0.029	-0.016	20.645	0.028	0.028	0.000	0.000	0.000	0.000
59	A	361	SER	0	-0.024	-0.017	23.387	0.030	0.030	0.000	0.000	0.000	0.000
60	A	362	VAL	0	0.042	0.013	24.854	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	363	ASN	0	-0.014	-0.017	27.275	0.004	0.004	0.000	0.000	0.000	0.000
62	A	364	GLY	0	-0.018	-0.004	28.616	0.011	0.011	0.000	0.000	0.000	0.000
63	A	365	VAL	0	-0.018	0.000	30.197	0.000	0.000	0.000	0.000	0.000	0.000
64	A	366	ASP	-1	-0.854	-0.924	28.151	-0.255	-0.255	0.000	0.000	0.000	0.000
65	A	367	LEU	0	0.001	-0.016	26.054	0.017	0.017	0.000	0.000	0.000	0.000
66	A	368	ARG	1	0.880	0.927	24.755	0.291	0.291	0.000	0.000	0.000	0.000
67	A	369	ASN	0	-0.037	-0.026	26.501	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	370	ALA	0	-0.002	0.019	28.444	0.014	0.014	0.000	0.000	0.000	0.000
69	A	371	SER	0	0.110	0.063	28.606	-0.011	-0.011	0.000	0.000	0.000	0.000
70	A	372	HIS	0	-0.002	-0.019	26.798	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	373	GLU	-1	-0.947	-0.976	28.669	-0.098	-0.098	0.000	0.000	0.000	0.000
72	A	374	GLN	0	0.047	0.019	31.830	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	375	ALA	0	0.027	0.017	26.903	0.000	0.000	0.000	0.000	0.000	0.000
74	A	376	ALA	0	-0.014	-0.006	28.620	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	377	ILE	0	-0.019	-0.010	29.542	0.008	0.008	0.000	0.000	0.000	0.000
76	A	378	ALA	0	-0.005	0.004	29.845	0.005	0.005	0.000	0.000	0.000	0.000
77	A	379	LEU	0	0.021	0.005	24.861	0.003	0.003	0.000	0.000	0.000	0.000
78	A	380	LYS	1	0.901	0.959	28.930	0.088	0.088	0.000	0.000	0.000	0.000
79	A	381	ASN	0	-0.017	-0.014	31.698	0.012	0.012	0.000	0.000	0.000	0.000
80	A	382	ALA	0	-0.014	0.013	29.808	0.003	0.003	0.000	0.000	0.000	0.000
81	A	383	GLY	0	0.022	0.015	31.844	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	384	GLN	0	-0.008	-0.017	31.302	-0.007	-0.007	0.000	0.000	0.000	0.000
83	A	385	THR	0	-0.005	0.004	28.547	0.003	0.003	0.000	0.000	0.000	0.000
84	A	386	VAL	0	-0.020	0.001	25.857	0.001	0.001	0.000	0.000	0.000	0.000
85	A	387	THR	0	-0.013	-0.012	25.178	-0.010	-0.010	0.000	0.000	0.000	0.000
86	A	388	ILE	0	0.029	0.013	20.714	0.011	0.011	0.000	0.000	0.000	0.000
87	A	389	ILE	0	-0.048	-0.007	21.443	-0.015	-0.015	0.000	0.000	0.000	0.000
88	A	390	ALA	0	0.032	0.020	17.221	0.020	0.020	0.000	0.000	0.000	0.000
89	A	391	GLN	0	-0.030	-0.035	16.142	0.034	0.034	0.000	0.000	0.000	0.000
90	A	392	TYR	0	-0.053	-0.066	7.745	0.298	0.298	0.000	0.000	0.000	0.000
91	A	393	LYS	1	0.873	0.947	13.274	0.595	0.595	0.000	0.000	0.000	0.000
92	A	394	PRO	0	0.064	0.044	9.880	0.152	0.152	0.000	0.000	0.000	0.000
93	A	395	GLU	-1	-0.874	-0.945	12.025	-0.932	-0.932	0.000	0.000	0.000	0.000
94	A	396	GLU	-1	-0.922	-0.957	14.735	-0.510	-0.510	0.000	0.000	0.000	0.000
95	A	397	TYR	0	-0.058	-0.032	13.691	0.072	0.072	0.000	0.000	0.000	0.000
96	A	398	SER	0	-0.042	-0.043	14.223	0.085	0.085	0.000	0.000	0.000	0.000
97	A	399	ARG	1	0.917	0.958	15.988	0.413	0.413	0.000	0.000	0.000	0.000
98	A	400	PHE	0	-0.041	-0.015	19.027	0.035	0.035	0.000	0.000	0.000	0.000
99	A	401	GLU	-1	-0.939	-0.947	14.027	-0.214	-0.214	0.000	0.000	0.000	0.000
100	A	402	ALA	0	-0.014	-0.007	17.133	0.010	0.010	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:303:GLY)