BMRB Entry 15150

Name: Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2
Published: 2007-10-24

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15150

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2

Deposition date:

2007-02-26

Original release date:

2007-10-24

Authors:

Wu, J.; Yang, Y.; Zhang, J.; Ji, P.; Wu, J.; Shi, Y.

Citation:

Citation: Wu, J.; Yang, Y.; Zhang, J.; Ji, P.; Du, W.; Jiang, P.; Xie, D.; Huang, H.; Wu, M.; Zhang, G.; Wu, J.; Shi, Y.. "Domain-swapped dimerization of the second PDZ domain of ZO2 may provide a structural basis for the polymerization of claudins" J. Biol. Chem. 282, 35988-35999 (2007).
PubMed: 17897942

Assembly members:

Assembly members:
ZO2PDZ2, polymer, 83 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b (+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ZO2PDZ2: MIGVLLMKSRANEEYGLRLG SQIFVKEMTRTGLATKDGNL HEGDIILKINGTVTENMSLT DARKLIEKSRGKLQLVVLRD SLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	343
15N chemical shifts	86
1H chemical shifts	595

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit 1	1
2	subunit 2	1

Entities:

Entity 1, subunit 1 83 residues - Formula weight is not available

1

MET

ILE

GLY

VAL

LEU

MET

LYS

SER

ARG

2

ALA

ASN

GLU

TYR

GLY

LEU

ARG

LEU

GLY

3

SER

GLN

ILE

PHE

VAL

LYS

GLU

MET

THR

ARG

4

THR

GLY

LEU

ALA

THR

LYS

ASP

GLY

ASN

LEU

5

HIS

GLU

GLY

ASP

ILE

LEU

LYS

ILE

ASN

6

GLY

THR

VAL

THR

GLU

ASN

MET

SER

LEU

THR

7

ASP

ALA

ARG

LYS

LEU

ILE

GLU

LYS

SER

ARG

8

GLY

LYS

LEU

GLN

LEU

VAL

LEU

ARG

ASP

9

SER

LEU

GLU

Samples:

sample_1: ZO2PDZ2 0.8 ± 0.1 mM; phosphate buffer 20 mM; NaCl 50 mM; EDTA 1 mM

sample_2: ZO2PDZ2, [U-100% 15N], 0.8 ± 0.1 mM; phosphate buffer 20 mM; NaCl 50 mM; EDTA 1 mM

sample_3: ZO2PDZ2, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM; phosphate buffer 20 mM; NaCl 50 mM; EDTA 1 mM

sample_4: ZO2PDZ2, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM; phosphate buffer 20 mM; NaCl 50 mM; EDTA 1 mM

sample_5: ZO2PDZ2, [U-100% 13C; U-100% 15N], 0.4 ± 0.05 mM; ZO2PDZ2 0.4 ± 0.05 mM; phosphate buffer 20 mM; NaCl 50 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_1	isotropic	sample_conditions_1
2D TOCSY	sample_1	isotropic	sample_conditions_1
3D_15N-separated_NOESY	sample_2	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample_4	isotropic	sample_conditions_1
3D_13C F1-filtered,F3-edited NOESY	sample_5	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D C(CO)NH	sample_3	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HCACO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_4	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_1

Software:

CNS v1.1, A.T. Brunger - refinement, structure solution

NMRPipe v2.2, F. Delaglio and A. Bax - processing

Molmol v2k.2, Koradi - data analysis

TALOS, Cornilescu - data analysis

SPARKY v3, T.D.Goddard and D.G.Kneller - data analysis

NMR spectrometers:

Bruker DMX 600 MHz

PDB	2OSG 3E17
DBJ	BAG11079 BAH11949 BAH11954 BAH13722 BAH14190
EMBL	CAL37567 CAL37590 CAL37681 CAL37845
GB	AAA61300 AAC02527 AAD20387 AAD56218 AAD56219
REF	NP_001095952 NP_001163885 NP_001163886 NP_001163887 NP_001164101
SP	Q9UDY2
AlphaFold	Q9UDY2