BMRB Entry 11424

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11424
MolProbity Validation Chart

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Title:
Interplay between phosphatidyl-inositol-phosphates and claudins upon binding to the 1st PDZ domain of zonula ocludens 1
Deposition date:
2011-01-05
Original release date:
2011-07-01
Authors:
Hiroaki, Hidekazu; Satomura, kaori; Goda, Natsuko; Umetsu, Yoshitaka; Taniguchi, Ryo; Ikegami, Takahisa; Furuse, Mikio
Citation:

Citation: Umetsu, Yoshitaka; Goda, Natsuko; Taniguchi, Ryo; Satomura, Kaori; Ikegami, Takahisa; Furuse, Mikio; Hiroaki, Hidekazu. "(1)H, (13)C, and (15)N resonance assignment of the first PDZ domain of mouse ZO-1."  Biomol. NMR Assignments ., .-. (2011).
PubMed: 21431884

Assembly members:

Assembly members:
the first PDZ domain of mouse ZO-1, polymer, 100 residues, 10817.255 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PRESAT-vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
the first PDZ domain of mouse ZO-1: GPLGSDHIWEQHTVTLHRAP GFGFGIAISGGRDNPHFQSG ETSIVISDVLKGGPAEGQLQ ENDRVAMVNGVSMDNVEHAF AVQQLRKSGKNAKITIRRKK

Data sets:
Data typeCount
13C chemical shifts368
15N chemical shifts86
1H chemical shifts594

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1the first PDZ domain of mouse ZO-11

Entities:

Entity 1, the first PDZ domain of mouse ZO-1 100 residues - 10817.255 Da.

1   GLYPROLEUGLYSERASPHISILETRPGLU
2   GLNHISTHRVALTHRLEUHISARGALAPRO
3   GLYPHEGLYPHEGLYILEALAILESERGLY
4   GLYARGASPASNPROHISPHEGLNSERGLY
5   GLUTHRSERILEVALILESERASPVALLEU
6   LYSGLYGLYPROALAGLUGLYGLNLEUGLN
7   GLUASNASPARGVALALAMETVALASNGLY
8   VALSERMETASPASNVALGLUHISALAPHE
9   ALAVALGLNGLNLEUARGLYSSERGLYLYS
10   ASNALALYSILETHRILEARGARGLYSLYS

Samples:

sample_1: ZO-1(PDZ1), [U-13C; U-15N], 0.7 mM; MES 20 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 5.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - predicts angles from chemical shift homology

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA03274 BAF95000 BAG10532 BAG65513
EMBL CAE45936
GB AAA02891 AAD11529 AAH88825 AAI11713 AAI38029
REF NP_001003140 NP_001099736 NP_001157046 NP_001287954 NP_001287955
SP O97758 P39447 Q07157
AlphaFold O97758 P39447 Q07157

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks