FMO DATABASE

FMODB ID: JL9J9

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

Total energy (hartree)

FMO2-HF: Electronic energy	-647906.48034
FMO2-HF: Nuclear repulsion	612646.488543
FMO2-HF: Total energy	-35259.991797
FMO2-MP2: Total energy	-35364.929583

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.
0.739	3.13	0.003	-1.267	-1.126	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 : 0.018

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	-0.003	0.020	3.397	-0.777	1.523	0.004	-1.261	-1.043	0.002
4	A	6	SER	0	-0.003	-0.003	5.342	0.686	0.777	-0.001	-0.006	-0.083	0.000
5	A	7	MET	0	-0.039	-0.011	8.415	0.144	0.144	0.000	0.000	0.000	0.000
6	A	8	LYS	1	0.763	0.860	11.602	0.643	0.643	0.000	0.000	0.000	0.000
7	A	9	LEU	0	-0.005	-0.017	15.294	-0.041	-0.041	0.000	0.000	0.000	0.000
8	A	10	VAL	0	0.012	0.009	17.897	0.039	0.039	0.000	0.000	0.000	0.000
9	A	11	LYS	1	0.867	0.933	21.409	0.216	0.216	0.000	0.000	0.000	0.000
10	A	12	PHE	0	0.071	0.036	24.522	0.014	0.014	0.000	0.000	0.000	0.000
11	A	13	ARG	1	0.853	0.939	27.838	0.142	0.142	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.736	0.865	31.078	0.192	0.192	0.000	0.000	0.000	0.000
13	A	15	GLY	0	0.040	0.034	32.246	0.012	0.012	0.000	0.000	0.000	0.000
14	A	16	ASP	-1	-0.839	-0.933	35.424	-0.127	-0.127	0.000	0.000	0.000	0.000
15	A	17	SER	0	-0.049	-0.044	34.046	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	18	VAL	0	0.010	-0.002	27.470	0.002	0.002	0.000	0.000	0.000	0.000
17	A	19	GLY	0	0.027	0.018	29.684	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	20	LEU	0	-0.016	-0.011	24.444	-0.009	-0.009	0.000	0.000	0.000	0.000
19	A	21	ARG	1	0.952	0.999	27.650	0.248	0.248	0.000	0.000	0.000	0.000
20	A	22	LEU	0	0.030	0.012	24.785	-0.021	-0.021	0.000	0.000	0.000	0.000
21	A	23	ALA	0	-0.040	-0.031	23.112	0.030	0.030	0.000	0.000	0.000	0.000
22	A	24	GLY	0	0.038	0.024	21.426	-0.036	-0.036	0.000	0.000	0.000	0.000
23	A	25	GLY	0	0.014	-0.011	21.076	0.045	0.045	0.000	0.000	0.000	0.000
24	A	26	ASN	0	-0.009	-0.015	20.638	-0.012	-0.012	0.000	0.000	0.000	0.000
25	A	27	ASP	-1	-0.900	-0.933	19.511	-0.445	-0.445	0.000	0.000	0.000	0.000
26	A	28	VAL	0	-0.027	-0.015	16.032	-0.061	-0.061	0.000	0.000	0.000	0.000
27	A	29	GLY	0	0.007	0.008	15.768	-0.113	-0.113	0.000	0.000	0.000	0.000
28	A	30	ILE	0	0.024	0.025	17.604	0.063	0.063	0.000	0.000	0.000	0.000
29	A	31	PHE	0	-0.033	-0.040	15.214	-0.070	-0.070	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.022	0.018	20.245	0.055	0.055	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.013	0.001	22.138	-0.007	-0.007	0.000	0.000	0.000	0.000
32	A	34	GLY	0	-0.033	-0.036	24.681	0.017	0.017	0.000	0.000	0.000	0.000
33	A	35	VAL	0	-0.008	-0.002	24.291	-0.011	-0.011	0.000	0.000	0.000	0.000
34	A	36	LEU	0	0.012	0.021	27.472	0.007	0.007	0.000	0.000	0.000	0.000
35	A	37	GLU	-1	-0.914	-0.947	30.594	-0.155	-0.155	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.920	-0.953	31.845	-0.140	-0.140	0.000	0.000	0.000	0.000
37	A	39	SER	0	-0.082	-0.051	29.626	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	40	PRO	0	0.018	-0.026	30.039	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	41	ALA	0	0.035	0.026	25.818	-0.009	-0.009	0.000	0.000	0.000	0.000
40	A	42	ALA	0	0.017	0.001	25.188	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	43	LYS	1	0.869	0.942	26.053	0.160	0.160	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.893	-0.947	24.242	-0.210	-0.210	0.000	0.000	0.000	0.000
43	A	45	GLY	0	-0.005	0.020	22.100	-0.019	-0.019	0.000	0.000	0.000	0.000
44	A	46	LEU	0	-0.046	-0.009	19.677	-0.054	-0.054	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.790	-0.895	19.141	-0.366	-0.366	0.000	0.000	0.000	0.000
46	A	48	GLU	-1	-0.807	-0.884	20.682	-0.326	-0.326	0.000	0.000	0.000	0.000
47	A	49	GLY	0	-0.052	-0.032	19.082	-0.006	-0.006	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.786	-0.875	16.508	-0.657	-0.657	0.000	0.000	0.000	0.000
49	A	51	GLN	0	-0.006	-0.004	13.462	-0.050	-0.050	0.000	0.000	0.000	0.000
50	A	52	ILE	0	-0.007	-0.019	16.013	-0.043	-0.043	0.000	0.000	0.000	0.000
51	A	53	LEU	0	-0.008	-0.006	11.652	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	54	ARG	1	0.849	0.904	15.957	0.603	0.603	0.000	0.000	0.000	0.000
53	A	55	VAL	0	0.027	0.030	18.643	0.005	0.005	0.000	0.000	0.000	0.000
54	A	56	ASN	0	0.048	0.030	22.166	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	57	ASN	0	-0.051	-0.030	20.994	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	58	VAL	0	0.039	0.039	22.080	0.013	0.013	0.000	0.000	0.000	0.000
57	A	59	ASP	-1	-0.827	-0.887	17.145	-0.668	-0.668	0.000	0.000	0.000	0.000
58	A	60	PHE	0	0.032	-0.014	18.396	0.052	0.052	0.000	0.000	0.000	0.000
59	A	61	THR	0	-0.092	-0.074	14.129	-0.039	-0.039	0.000	0.000	0.000	0.000
60	A	62	ASN	0	-0.030	-0.005	17.208	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	63	ILE	0	0.021	0.044	19.965	0.040	0.040	0.000	0.000	0.000	0.000
62	A	64	ILE	0	0.045	0.024	22.505	-0.024	-0.024	0.000	0.000	0.000	0.000
63	A	65	ARG	1	0.884	0.926	25.098	0.271	0.271	0.000	0.000	0.000	0.000
64	A	66	GLU	-1	-0.871	-0.947	26.013	-0.247	-0.247	0.000	0.000	0.000	0.000
65	A	67	GLU	-1	-0.870	-0.941	27.083	-0.253	-0.253	0.000	0.000	0.000	0.000
66	A	68	ALA	0	-0.004	0.001	24.514	0.003	0.003	0.000	0.000	0.000	0.000
67	A	69	VAL	0	-0.046	-0.022	26.490	0.007	0.007	0.000	0.000	0.000	0.000
68	A	70	LEU	0	0.028	0.007	29.513	0.008	0.008	0.000	0.000	0.000	0.000
69	A	71	PHE	0	0.058	0.039	26.749	0.005	0.005	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.006	-0.015	25.245	0.006	0.006	0.000	0.000	0.000	0.000
71	A	73	LEU	0	-0.070	-0.037	29.149	0.013	0.013	0.000	0.000	0.000	0.000
72	A	74	ASP	-1	-0.871	-0.940	32.249	-0.167	-0.167	0.000	0.000	0.000	0.000
73	A	75	LEU	0	-0.107	-0.030	27.241	0.006	0.006	0.000	0.000	0.000	0.000
74	A	76	PRO	0	0.071	0.045	31.795	0.006	0.006	0.000	0.000	0.000	0.000
75	A	77	LYS	1	0.907	0.964	33.831	0.134	0.134	0.000	0.000	0.000	0.000
76	A	78	GLY	0	0.015	0.011	35.349	0.008	0.008	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.935	-0.968	32.586	-0.147	-0.147	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.878	-0.939	28.536	-0.185	-0.185	0.000	0.000	0.000	0.000
79	A	81	VAL	0	-0.013	-0.009	25.159	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	82	THR	0	-0.036	-0.041	21.086	0.006	0.006	0.000	0.000	0.000	0.000
81	A	83	ILE	0	0.009	0.002	19.629	-0.021	-0.021	0.000	0.000	0.000	0.000
82	A	84	LEU	0	-0.011	0.019	13.626	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	85	ALA	0	0.021	0.003	15.825	-0.012	-0.012	0.000	0.000	0.000	0.000
84	A	86	GLN	0	0.034	0.001	8.362	-0.270	-0.270	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.834	0.923	13.100	0.514	0.514	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.922	0.979	9.597	1.363	1.363	0.000	0.000	0.000	0.000
87	A	89	LYS	1	0.950	0.948	13.338	0.473	0.473	0.000	0.000	0.000	0.000
88	A	90	ASP	-1	-0.875	-0.942	12.949	-0.691	-0.691	0.000	0.000	0.000	0.000
89	A	91	VAL	0	0.017	0.030	12.884	0.052	0.052	0.000	0.000	0.000	0.000
90	A	92	TYR	0	-0.019	-0.032	15.799	0.061	0.061	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.918	0.940	17.488	0.395	0.395	0.000	0.000	0.000	0.000
92	A	94	ARG	1	0.861	0.924	15.513	0.461	0.461	0.000	0.000	0.000	0.000
93	A	95	ILE	0	-0.036	0.008	18.611	0.027	0.027	0.000	0.000	0.000	0.000
94	A	96	VAL	0	-0.048	-0.005	22.372	0.052	0.052	0.000	0.000	0.000	0.000

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