FMO DATABASE

FMODB ID: N9G5Q

Calculation Name: 3SHU-A-Xray372

Preferred Name: Tight junction protein ZO-1

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 3SHU

Chain ID: A

ChEMBL ID: CHEMBL4296026

UniProt ID: Q07157

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	94
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-646739.824503
FMO2-HF: Nuclear repulsion	611480.445264
FMO2-HF: Total energy	-35259.379239
FMO2-MP2: Total energy	-35364.290809

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:3:GLY)

Summations of interaction energy for fragment #1(A:3: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.
0.602	3.028	0.003	-1.285	-1.144	0.002

Interaction energy analysis for fragmet #1(A:3:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.040 / q_NPA : 0.014

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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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	5	GLY	0	0.015	0.036	3.393	-0.813	1.527	0.004	-1.279	-1.065	0.002
4	A	6	SER	0	-0.026	-0.013	5.344	0.691	0.777	-0.001	-0.006	-0.079	0.000
5	A	7	MET	0	-0.016	-0.004	8.563	0.130	0.130	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.840	0.924	11.604	0.663	0.663	0.000	0.000	0.000	0.000
7	A	9	LEU	0	-0.016	-0.022	15.296	-0.036	-0.036	0.000	0.000	0.000	0.000
8	A	10	VAL	0	0.014	0.011	17.898	0.038	0.038	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.946	0.969	21.410	0.237	0.237	0.000	0.000	0.000	0.000
10	A	12	PHE	0	0.080	0.048	24.523	0.013	0.013	0.000	0.000	0.000	0.000
11	A	13	ARG	1	0.943	0.971	27.840	0.140	0.140	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.793	0.914	31.149	0.191	0.191	0.000	0.000	0.000	0.000
13	A	15	GLY	0	0.034	0.032	32.246	0.012	0.012	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.855	-0.931	35.424	-0.128	-0.128	0.000	0.000	0.000	0.000
15	A	17	SER	0	-0.063	-0.053	33.853	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.009	-0.001	27.421	0.002	0.002	0.000	0.000	0.000	0.000
17	A	19	GLY	0	0.023	0.016	29.690	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.008	-0.011	24.356	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	21	ARG	1	0.967	0.999	27.843	0.244	0.244	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.017	0.005	24.344	-0.020	-0.020	0.000	0.000	0.000	0.000
21	A	23	ALA	0	-0.040	-0.025	23.081	0.032	0.032	0.000	0.000	0.000	0.000
22	A	24	GLY	0	0.039	0.025	21.411	-0.036	-0.036	0.000	0.000	0.000	0.000
23	A	25	GLY	0	-0.009	-0.020	21.060	0.045	0.045	0.000	0.000	0.000	0.000
24	A	26	ASN	0	0.033	0.012	20.624	-0.061	-0.061	0.000	0.000	0.000	0.000
25	A	27	ASP	-1	-0.907	-0.932	19.468	-0.443	-0.443	0.000	0.000	0.000	0.000
26	A	28	VAL	0	-0.036	-0.016	15.899	-0.062	-0.062	0.000	0.000	0.000	0.000
27	A	29	GLY	0	0.010	0.009	15.754	-0.114	-0.114	0.000	0.000	0.000	0.000
28	A	30	ILE	0	0.026	0.027	17.589	0.065	0.065	0.000	0.000	0.000	0.000
29	A	31	PHE	0	-0.032	-0.041	15.121	-0.072	-0.072	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.029	0.021	20.254	0.054	0.054	0.000	0.000	0.000	0.000
31	A	33	ALA	0	-0.001	-0.008	22.146	-0.008	-0.008	0.000	0.000	0.000	0.000
32	A	34	GLY	0	-0.036	-0.020	24.689	0.016	0.016	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.004	-0.003	24.324	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	36	LEU	0	0.008	0.013	27.478	0.008	0.008	0.000	0.000	0.000	0.000
35	A	37	GLU	-1	-0.918	-0.948	30.599	-0.157	-0.157	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.906	-0.942	31.850	-0.137	-0.137	0.000	0.000	0.000	0.000
37	A	39	SER	0	-0.105	-0.065	29.689	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	40	PRO	0	0.006	-0.027	30.052	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	41	ALA	0	0.037	0.026	25.780	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	42	ALA	0	0.024	0.003	25.192	-0.021	-0.021	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.880	0.947	26.056	0.155	0.155	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.896	-0.946	24.083	-0.218	-0.218	0.000	0.000	0.000	0.000
43	A	45	GLY	0	-0.017	0.012	22.102	-0.019	-0.019	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.064	-0.030	19.685	-0.054	-0.054	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.902	-0.978	19.762	-0.337	-0.337	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.826	-0.888	20.688	-0.330	-0.330	0.000	0.000	0.000	0.000
47	A	49	GLY	0	-0.096	-0.068	19.087	-0.008	-0.008	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.792	-0.880	16.512	-0.669	-0.669	0.000	0.000	0.000	0.000
49	A	51	GLN	0	0.008	0.000	13.410	-0.047	-0.047	0.000	0.000	0.000	0.000
50	A	52	ILE	0	-0.016	-0.024	16.020	-0.043	-0.043	0.000	0.000	0.000	0.000
51	A	53	LEU	0	-0.019	-0.013	11.479	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	54	ARG	1	0.954	0.972	15.957	0.584	0.584	0.000	0.000	0.000	0.000
53	A	55	VAL	0	0.023	0.034	18.643	0.004	0.004	0.000	0.000	0.000	0.000
54	A	56	ASN	0	0.047	0.030	22.166	0.003	0.003	0.000	0.000	0.000	0.000
55	A	57	ASN	0	-0.061	-0.037	21.000	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	58	VAL	0	0.031	0.035	22.080	0.014	0.014	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.905	-0.957	17.197	-0.663	-0.663	0.000	0.000	0.000	0.000
58	A	60	PHE	0	0.013	-0.012	18.378	0.053	0.053	0.000	0.000	0.000	0.000
59	A	61	THR	0	-0.098	-0.070	14.060	-0.036	-0.036	0.000	0.000	0.000	0.000
60	A	62	ASN	0	-0.021	0.000	17.195	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	63	ILE	0	0.036	0.043	19.955	0.044	0.044	0.000	0.000	0.000	0.000
62	A	64	ILE	0	0.024	0.008	22.492	-0.024	-0.024	0.000	0.000	0.000	0.000
63	A	65	ARG	1	0.972	0.968	25.109	0.276	0.276	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.905	-0.969	25.998	-0.243	-0.243	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.919	-0.963	27.328	-0.241	-0.241	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.005	0.007	24.502	0.002	0.002	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.053	-0.029	26.482	0.007	0.007	0.000	0.000	0.000	0.000
68	A	70	LEU	0	0.033	0.007	29.496	0.008	0.008	0.000	0.000	0.000	0.000
69	A	71	PHE	0	0.058	0.042	26.282	0.003	0.003	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.013	-0.020	25.195	0.006	0.006	0.000	0.000	0.000	0.000
71	A	73	LEU	0	-0.089	-0.049	29.149	0.013	0.013	0.000	0.000	0.000	0.000
72	A	74	ASP	-1	-0.888	-0.951	32.224	-0.168	-0.168	0.000	0.000	0.000	0.000
73	A	75	LEU	0	-0.113	-0.037	27.341	0.006	0.006	0.000	0.000	0.000	0.000
74	A	76	PRO	0	0.047	0.023	31.795	0.007	0.007	0.000	0.000	0.000	0.000
75	A	77	LYS	1	0.927	0.962	33.831	0.135	0.135	0.000	0.000	0.000	0.000
76	A	78	GLY	0	0.029	0.022	35.368	0.008	0.008	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.945	-0.966	32.516	-0.148	-0.148	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.994	-1.006	28.549	-0.191	-0.191	0.000	0.000	0.000	0.000
79	A	81	VAL	0	-0.026	-0.006	25.227	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	82	THR	0	-0.030	-0.034	21.054	0.004	0.004	0.000	0.000	0.000	0.000
81	A	83	ILE	0	0.000	-0.003	19.503	-0.020	-0.020	0.000	0.000	0.000	0.000
82	A	84	LEU	0	-0.019	0.013	13.659	-0.002	-0.002	0.000	0.000	0.000	0.000
83	A	85	ALA	0	0.021	0.005	15.858	-0.013	-0.013	0.000	0.000	0.000	0.000
84	A	86	GLN	0	0.026	-0.007	8.229	-0.462	-0.462	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.915	0.981	13.106	0.530	0.530	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.933	0.984	9.634	1.484	1.484	0.000	0.000	0.000	0.000
87	A	89	LYS	1	1.004	0.988	13.346	0.487	0.487	0.000	0.000	0.000	0.000
88	A	90	ASP	-1	-0.932	-0.958	12.809	-0.729	-0.729	0.000	0.000	0.000	0.000
89	A	91	VAL	0	0.054	0.029	12.954	0.064	0.064	0.000	0.000	0.000	0.000
90	A	92	TYR	0	-0.031	-0.043	15.809	0.064	0.064	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.916	0.936	17.347	0.415	0.415	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.867	0.936	17.108	0.427	0.427	0.000	0.000	0.000	0.000
93	A	95	ILE	0	-0.017	0.019	19.022	0.025	0.025	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.027	0.000	22.357	0.039	0.039	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:GLY)