BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15150

Title: Solution Structure and Binding Property of the Domain-swapped Dimer of ZO2PDZ2   PubMed: 17897942

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

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).

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

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts343
15N chemical shifts86
1H chemical shifts595

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11
2subunit 21

Entities:

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

1   METILEGLYVALLEULEUMETLYSSERARG
2   ALAASNGLUGLUTYRGLYLEUARGLEUGLY
3   SERGLNILEPHEVALLYSGLUMETTHRARG
4   THRGLYLEUALATHRLYSASPGLYASNLEU
5   HISGLUGLYASPILEILELEULYSILEASN
6   GLYTHRVALTHRGLUASNMETSERLEUTHR
7   ASPALAARGLYSLEUILEGLULYSSERARG
8   GLYLYSLEUGLNLEUVALVALLEUARGASP
9   SERLEUGLU

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:

NameSampleSample stateSample conditions
2D NOESYsample_1isotropicsample_conditions_1
2D TOCSYsample_1isotropicsample_conditions_1
3D_15N-separated_NOESYsample_2isotropicsample_conditions_1
3D_13C-separated_NOESYsample_4isotropicsample_conditions_1
3D_13C F1-filtered,F3-edited NOESYsample_5isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HCACOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_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

Related Database Links:

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