FMO DATABASE

FMODB ID: 85MRY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-695485.830469
FMO2-HF: Nuclear repulsion	658493.817054
FMO2-HF: Total energy	-36992.013416
FMO2-MP2: Total energy	-37102.700427

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.
-15.505	-11.486	5	-4.505	-4.514	-0.039

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 : 0.005 / 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	-0.949	-0.974	2.045	-11.349	-9.473	4.534	-3.284	-3.126	-0.024
4	A	306	ASP	-1	-0.950	-0.974	2.589	-8.695	-6.552	0.466	-1.221	-1.388	-0.015
5	A	307	ILE	0	-0.028	0.006	4.993	1.645	1.645	0.000	0.000	0.000	0.000
6	A	308	PRO	0	-0.002	0.001	7.340	0.245	0.245	0.000	0.000	0.000	0.000
7	A	309	ARG	1	0.880	0.924	7.199	2.917	2.917	0.000	0.000	0.000	0.000
8	A	310	GLU	-1	-0.904	-0.941	12.903	-0.834	-0.834	0.000	0.000	0.000	0.000
9	A	311	PRO	0	-0.054	-0.043	15.932	-0.021	-0.021	0.000	0.000	0.000	0.000
10	A	312	ARG	1	0.808	0.881	13.943	0.783	0.783	0.000	0.000	0.000	0.000
11	A	313	ARG	1	0.929	0.962	18.511	0.286	0.286	0.000	0.000	0.000	0.000
12	A	314	ILE	0	0.041	0.035	17.208	0.002	0.002	0.000	0.000	0.000	0.000
13	A	315	VAL	0	-0.055	-0.027	20.845	0.022	0.022	0.000	0.000	0.000	0.000
14	A	316	ILE	0	0.036	0.031	20.998	0.007	0.007	0.000	0.000	0.000	0.000
15	A	317	HIS	0	0.032	0.010	24.063	0.008	0.008	0.000	0.000	0.000	0.000
16	A	318	ARG	1	0.802	0.885	26.550	0.120	0.120	0.000	0.000	0.000	0.000
17	A	319	GLY	0	0.014	0.007	28.549	0.008	0.008	0.000	0.000	0.000	0.000
18	A	320	SER	0	-0.027	-0.029	30.604	-0.003	-0.003	0.000	0.000	0.000	0.000
19	A	321	THR	0	0.018	0.014	26.943	0.008	0.008	0.000	0.000	0.000	0.000
20	A	322	GLY	0	-0.015	0.008	27.857	0.002	0.002	0.000	0.000	0.000	0.000
21	A	323	LEU	0	0.025	-0.008	24.010	0.003	0.003	0.000	0.000	0.000	0.000
22	A	324	GLY	0	0.029	0.017	22.267	-0.011	-0.011	0.000	0.000	0.000	0.000
23	A	325	PHE	0	-0.016	-0.009	19.506	-0.003	-0.003	0.000	0.000	0.000	0.000
24	A	326	ASN	0	-0.033	-0.003	20.841	0.013	0.013	0.000	0.000	0.000	0.000
25	A	327	ILE	0	-0.006	-0.006	20.770	-0.027	-0.027	0.000	0.000	0.000	0.000
26	A	328	ILE	0	-0.002	0.002	20.329	0.028	0.028	0.000	0.000	0.000	0.000
27	A	329	GLY	0	0.037	0.011	22.820	-0.031	-0.031	0.000	0.000	0.000	0.000
28	A	330	GLY	0	0.018	0.013	25.106	0.015	0.015	0.000	0.000	0.000	0.000
29	A	331	GLU	-1	-0.937	-0.974	28.255	-0.118	-0.118	0.000	0.000	0.000	0.000
30	A	332	ASP	-1	-0.865	-0.934	29.542	-0.162	-0.162	0.000	0.000	0.000	0.000
31	A	333	GLY	0	-0.033	-0.017	28.777	0.004	0.004	0.000	0.000	0.000	0.000
32	A	334	GLU	-1	-0.904	-0.941	25.680	-0.191	-0.191	0.000	0.000	0.000	0.000
33	A	335	GLY	0	-0.004	0.007	23.200	-0.027	-0.027	0.000	0.000	0.000	0.000
34	A	336	ILE	0	-0.035	-0.018	22.925	0.022	0.022	0.000	0.000	0.000	0.000
35	A	337	PHE	0	0.003	-0.005	17.370	-0.049	-0.049	0.000	0.000	0.000	0.000
36	A	338	ILE	0	-0.038	-0.006	16.487	0.059	0.059	0.000	0.000	0.000	0.000
37	A	339	SER	0	0.053	0.014	16.711	-0.033	-0.033	0.000	0.000	0.000	0.000
38	A	340	PHE	0	-0.052	-0.033	17.507	0.033	0.033	0.000	0.000	0.000	0.000
39	A	341	AZH	0	0.026	0.011	15.574	-0.050	-0.050	0.000	0.000	0.000	0.000
40	A	342	LEU	0	-0.039	-0.015	17.638	0.035	0.035	0.000	0.000	0.000	0.000
41	A	343	ALA	0	0.026	0.011	18.194	-0.011	-0.011	0.000	0.000	0.000	0.000
42	A	344	GLY	0	-0.005	-0.008	18.882	0.005	0.005	0.000	0.000	0.000	0.000
43	A	345	GLY	0	-0.032	-0.013	20.586	-0.005	-0.005	0.000	0.000	0.000	0.000
44	A	346	PRO	0	-0.013	-0.014	20.527	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	347	ALA	0	0.006	0.002	18.441	-0.014	-0.014	0.000	0.000	0.000	0.000
46	A	348	ASP	-1	-0.824	-0.886	15.398	-0.077	-0.077	0.000	0.000	0.000	0.000
47	A	349	LEU	0	-0.042	-0.024	16.065	-0.010	-0.010	0.000	0.000	0.000	0.000
48	A	350	SER	0	-0.064	-0.036	17.245	-0.020	-0.020	0.000	0.000	0.000	0.000
49	A	351	GLY	0	0.008	0.009	13.524	-0.014	-0.014	0.000	0.000	0.000	0.000
50	A	352	GLU	-1	-0.979	-0.991	12.553	-0.497	-0.497	0.000	0.000	0.000	0.000
51	A	353	LEU	0	-0.055	-0.031	14.525	-0.053	-0.053	0.000	0.000	0.000	0.000
52	A	354	ARG	1	0.930	0.972	8.971	1.129	1.129	0.000	0.000	0.000	0.000
53	A	355	LYS	1	0.852	0.894	12.342	0.168	0.168	0.000	0.000	0.000	0.000
54	A	356	GLY	0	0.068	0.030	11.956	-0.128	-0.128	0.000	0.000	0.000	0.000
55	A	357	ASP	-1	-0.766	-0.857	13.533	-0.894	-0.894	0.000	0.000	0.000	0.000
56	A	358	GLN	0	0.002	0.002	15.232	0.060	0.060	0.000	0.000	0.000	0.000
57	A	359	ILE	0	-0.025	-0.024	18.553	-0.021	-0.021	0.000	0.000	0.000	0.000
58	A	360	LEU	0	-0.016	-0.009	20.604	0.029	0.029	0.000	0.000	0.000	0.000
59	A	361	SER	0	-0.026	-0.018	23.387	0.031	0.031	0.000	0.000	0.000	0.000
60	A	362	VAL	0	0.039	0.012	24.859	-0.015	-0.015	0.000	0.000	0.000	0.000
61	A	363	ASN	0	-0.006	-0.010	27.279	0.003	0.003	0.000	0.000	0.000	0.000
62	A	364	GLY	0	-0.010	0.001	28.620	0.012	0.012	0.000	0.000	0.000	0.000
63	A	365	VAL	0	-0.026	-0.001	30.202	0.000	0.000	0.000	0.000	0.000	0.000
64	A	366	ASP	-1	-0.831	-0.913	28.060	-0.261	-0.261	0.000	0.000	0.000	0.000
65	A	367	LEU	0	-0.006	-0.019	26.116	0.018	0.018	0.000	0.000	0.000	0.000
66	A	368	ARG	1	0.875	0.922	24.727	0.298	0.298	0.000	0.000	0.000	0.000
67	A	369	ASN	0	-0.043	-0.028	26.501	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	370	ALA	0	0.001	0.020	28.427	0.015	0.015	0.000	0.000	0.000	0.000
69	A	371	SER	0	0.085	0.053	28.604	-0.010	-0.010	0.000	0.000	0.000	0.000
70	A	372	HIS	0	0.003	-0.014	26.486	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	373	GLU	-1	-0.949	-0.978	28.668	-0.097	-0.097	0.000	0.000	0.000	0.000
72	A	374	GLN	0	-0.006	-0.015	31.704	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	375	ALA	0	0.027	0.015	26.910	0.000	0.000	0.000	0.000	0.000	0.000
74	A	376	ALA	0	-0.013	-0.004	28.624	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	377	ILE	0	-0.015	-0.008	29.545	0.008	0.008	0.000	0.000	0.000	0.000
76	A	378	ALA	0	-0.001	0.005	29.880	0.005	0.005	0.000	0.000	0.000	0.000
77	A	379	LEU	0	0.030	0.010	24.773	0.002	0.002	0.000	0.000	0.000	0.000
78	A	380	LYS	1	0.903	0.964	28.934	0.087	0.087	0.000	0.000	0.000	0.000
79	A	381	ASN	0	-0.022	-0.022	31.701	0.012	0.012	0.000	0.000	0.000	0.000
80	A	382	ALA	0	-0.006	0.018	29.798	0.002	0.002	0.000	0.000	0.000	0.000
81	A	383	GLY	0	0.014	0.012	31.847	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	384	GLN	0	0.000	-0.011	31.305	-0.008	-0.008	0.000	0.000	0.000	0.000
83	A	385	THR	0	-0.006	0.001	28.575	0.003	0.003	0.000	0.000	0.000	0.000
84	A	386	VAL	0	-0.021	-0.005	25.941	0.001	0.001	0.000	0.000	0.000	0.000
85	A	387	THR	0	-0.015	-0.013	25.205	-0.011	-0.011	0.000	0.000	0.000	0.000
86	A	388	ILE	0	0.021	0.007	20.794	0.011	0.011	0.000	0.000	0.000	0.000
87	A	389	ILE	0	-0.046	-0.009	21.458	-0.016	-0.016	0.000	0.000	0.000	0.000
88	A	390	ALA	0	0.022	0.014	17.270	0.022	0.022	0.000	0.000	0.000	0.000
89	A	391	GLN	0	-0.023	-0.034	16.082	0.042	0.042	0.000	0.000	0.000	0.000
90	A	392	TYR	0	-0.058	-0.042	7.710	0.341	0.341	0.000	0.000	0.000	0.000
91	A	393	LYS	1	0.803	0.894	13.274	0.564	0.564	0.000	0.000	0.000	0.000
92	A	394	PRO	0	0.063	0.043	9.761	0.162	0.162	0.000	0.000	0.000	0.000
93	A	395	GLU	-1	-0.881	-0.948	11.883	-0.959	-0.959	0.000	0.000	0.000	0.000
94	A	396	GLU	-1	-0.849	-0.912	14.730	-0.504	-0.504	0.000	0.000	0.000	0.000
95	A	397	TYR	0	-0.021	-0.032	13.679	0.068	0.068	0.000	0.000	0.000	0.000
96	A	398	SER	0	-0.050	-0.044	14.164	0.084	0.084	0.000	0.000	0.000	0.000
97	A	399	ARG	1	0.903	0.957	15.984	0.427	0.427	0.000	0.000	0.000	0.000
98	A	400	PHE	0	-0.037	-0.009	19.036	0.033	0.033	0.000	0.000	0.000	0.000
99	A	401	GLU	-1	-0.856	-0.858	14.039	-0.165	-0.165	0.000	0.000	0.000	0.000
100	A	402	ALA	0	-0.008	-0.005	17.078	0.009	0.009	0.000	0.000	0.000	0.000

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