FMO DATABASE

FMODB ID: 39VYL

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	OptAll
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	-648143.22368
FMO2-HF: Nuclear repulsion	612882.864117
FMO2-HF: Total energy	-35260.359563
FMO2-MP2: Total energy	-35365.287849

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.
1.48	3.374	0.003	-0.98	-0.916	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 : 0.055 / q_NPA : 0.024

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	0.005	0.017	3.529	-0.221	1.575	0.004	-0.973	-0.827	0.002
4	A	6	SER	0	-0.028	-0.017	5.382	0.768	0.866	-0.001	-0.007	-0.089	0.000
5	A	7	MET	0	-0.056	-0.019	8.009	0.294	0.294	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.761	0.861	11.179	0.688	0.688	0.000	0.000	0.000	0.000
7	A	9	LEU	0	-0.002	-0.015	14.895	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	10	VAL	0	-0.004	0.013	17.484	0.038	0.038	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.846	0.897	21.177	0.227	0.227	0.000	0.000	0.000	0.000
10	A	12	PHE	0	0.060	0.042	24.355	0.015	0.015	0.000	0.000	0.000	0.000
11	A	13	ARG	1	0.844	0.908	27.742	0.147	0.147	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.736	0.869	31.050	0.192	0.192	0.000	0.000	0.000	0.000
13	A	15	GLY	0	0.058	0.035	32.187	0.012	0.012	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.835	-0.938	35.411	-0.132	-0.132	0.000	0.000	0.000	0.000
15	A	17	SER	0	-0.046	-0.033	33.583	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.032	0.009	27.005	0.002	0.002	0.000	0.000	0.000	0.000
17	A	19	GLY	0	0.025	0.019	29.363	-0.008	-0.008	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.014	-0.005	24.531	-0.008	-0.008	0.000	0.000	0.000	0.000
19	A	21	ARG	1	0.941	0.980	27.502	0.261	0.261	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.038	0.019	24.503	-0.024	-0.024	0.000	0.000	0.000	0.000
21	A	23	ALA	0	-0.033	-0.016	23.279	0.033	0.033	0.000	0.000	0.000	0.000
22	A	24	GLY	0	0.038	0.026	20.836	-0.033	-0.033	0.000	0.000	0.000	0.000
23	A	25	GLY	0	0.034	0.007	20.641	0.048	0.048	0.000	0.000	0.000	0.000
24	A	26	ASN	0	-0.014	-0.020	20.117	-0.026	-0.026	0.000	0.000	0.000	0.000
25	A	27	ASP	-1	-0.901	-0.937	19.709	-0.415	-0.415	0.000	0.000	0.000	0.000
26	A	28	VAL	0	-0.058	-0.026	15.986	-0.045	-0.045	0.000	0.000	0.000	0.000
27	A	29	GLY	0	0.016	0.012	15.538	-0.124	-0.124	0.000	0.000	0.000	0.000
28	A	30	ILE	0	0.028	0.024	17.374	0.055	0.055	0.000	0.000	0.000	0.000
29	A	31	PHE	0	-0.019	-0.027	14.798	-0.076	-0.076	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.005	0.009	19.949	0.059	0.059	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.033	0.001	22.055	-0.008	-0.008	0.000	0.000	0.000	0.000
32	A	34	GLY	0	-0.033	-0.034	24.488	0.024	0.024	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.039	-0.005	24.354	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	36	LEU	0	0.022	0.025	27.433	0.008	0.008	0.000	0.000	0.000	0.000
35	A	37	GLU	-1	-0.895	-0.939	30.376	-0.167	-0.167	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.883	-0.942	31.589	-0.152	-0.152	0.000	0.000	0.000	0.000
37	A	39	SER	0	-0.080	-0.046	29.364	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	40	PRO	0	0.042	-0.006	29.819	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	41	ALA	0	0.008	0.016	25.545	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	42	ALA	0	0.009	0.001	25.143	-0.022	-0.022	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.808	0.913	26.485	0.182	0.182	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.897	-0.950	23.952	-0.222	-0.222	0.000	0.000	0.000	0.000
43	A	45	GLY	0	0.004	0.019	22.223	-0.027	-0.027	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.023	-0.004	19.569	-0.056	-0.056	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.781	-0.882	18.727	-0.412	-0.412	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.791	-0.873	20.632	-0.346	-0.346	0.000	0.000	0.000	0.000
47	A	49	GLY	0	-0.020	-0.022	18.894	-0.002	-0.002	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.786	-0.877	16.091	-0.700	-0.700	0.000	0.000	0.000	0.000
49	A	51	GLN	0	-0.005	0.005	13.115	-0.029	-0.029	0.000	0.000	0.000	0.000
50	A	52	ILE	0	-0.009	-0.020	15.502	-0.068	-0.068	0.000	0.000	0.000	0.000
51	A	53	LEU	0	-0.012	-0.015	11.418	-0.038	-0.038	0.000	0.000	0.000	0.000
52	A	54	ARG	1	0.809	0.882	15.618	0.566	0.566	0.000	0.000	0.000	0.000
53	A	55	VAL	0	0.021	0.025	18.324	-0.002	-0.002	0.000	0.000	0.000	0.000
54	A	56	ASN	0	0.025	0.002	21.939	0.001	0.001	0.000	0.000	0.000	0.000
55	A	57	ASN	0	-0.031	-0.020	20.474	-0.006	-0.006	0.000	0.000	0.000	0.000
56	A	58	VAL	0	0.032	0.034	21.008	-0.009	-0.009	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.805	-0.874	17.057	-0.631	-0.631	0.000	0.000	0.000	0.000
58	A	60	PHE	0	0.030	-0.007	18.180	0.046	0.046	0.000	0.000	0.000	0.000
59	A	61	THR	0	-0.084	-0.063	13.780	-0.035	-0.035	0.000	0.000	0.000	0.000
60	A	62	ASN	0	-0.044	-0.013	16.900	0.006	0.006	0.000	0.000	0.000	0.000
61	A	63	ILE	0	0.029	0.040	19.560	0.035	0.035	0.000	0.000	0.000	0.000
62	A	64	ILE	0	0.018	0.010	22.573	-0.022	-0.022	0.000	0.000	0.000	0.000
63	A	65	ARG	1	0.850	0.895	24.976	0.261	0.261	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.851	-0.929	25.777	-0.248	-0.248	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.840	-0.921	26.734	-0.249	-0.249	0.000	0.000	0.000	0.000
66	A	68	ALA	0	0.006	0.007	24.105	0.003	0.003	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.046	-0.034	26.022	0.003	0.003	0.000	0.000	0.000	0.000
68	A	70	LEU	0	0.008	0.006	29.016	0.009	0.009	0.000	0.000	0.000	0.000
69	A	71	PHE	0	0.070	0.032	26.289	0.005	0.005	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.017	-0.015	24.852	0.004	0.004	0.000	0.000	0.000	0.000
71	A	73	LEU	0	-0.057	-0.027	28.817	0.012	0.012	0.000	0.000	0.000	0.000
72	A	74	ASP	-1	-0.878	-0.943	32.061	-0.167	-0.167	0.000	0.000	0.000	0.000
73	A	75	LEU	0	-0.082	-0.023	26.988	0.006	0.006	0.000	0.000	0.000	0.000
74	A	76	PRO	0	0.061	0.039	31.622	0.004	0.004	0.000	0.000	0.000	0.000
75	A	77	LYS	1	0.854	0.932	33.777	0.136	0.136	0.000	0.000	0.000	0.000
76	A	78	GLY	0	0.026	0.023	35.330	0.008	0.008	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.937	-0.965	32.533	-0.145	-0.145	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.832	-0.895	28.246	-0.191	-0.191	0.000	0.000	0.000	0.000
79	A	81	VAL	0	-0.001	-0.002	25.084	-0.005	-0.005	0.000	0.000	0.000	0.000
80	A	82	THR	0	-0.010	-0.014	20.920	0.005	0.005	0.000	0.000	0.000	0.000
81	A	83	ILE	0	-0.008	-0.001	19.419	-0.011	-0.011	0.000	0.000	0.000	0.000
82	A	84	LEU	0	0.010	0.023	13.195	-0.005	-0.005	0.000	0.000	0.000	0.000
83	A	85	ALA	0	0.026	0.007	15.284	0.006	0.006	0.000	0.000	0.000	0.000
84	A	86	GLN	0	0.040	0.007	7.618	-0.101	-0.101	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.842	0.925	12.667	0.563	0.563	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.902	0.959	9.802	1.202	1.202	0.000	0.000	0.000	0.000
87	A	89	LYS	1	0.881	0.911	13.499	0.465	0.465	0.000	0.000	0.000	0.000
88	A	90	ASP	-1	-0.855	-0.927	12.836	-0.786	-0.786	0.000	0.000	0.000	0.000
89	A	91	VAL	0	0.003	0.023	13.138	0.070	0.070	0.000	0.000	0.000	0.000
90	A	92	TYR	0	-0.003	-0.012	15.981	0.059	0.059	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.934	0.951	17.536	0.421	0.421	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.840	0.922	15.083	0.494	0.494	0.000	0.000	0.000	0.000
93	A	95	ILE	0	-0.010	0.007	18.262	0.031	0.031	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.066	-0.017	22.011	0.048	0.048	0.000	0.000	0.000	0.000

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