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 18441

Title: Solution structure of harmonin N terminal domain in complex with a exon68 encoded peptide of cadherin23   PubMed: 22879593

Deposition date: 2012-05-04 Original release date: 2012-08-13

Authors: Pan, Lifeng; Wu, Lin; Zhang, Chuchu; Zhang, Mingjie

Citation: Wu, Lin; Pan, Lifeng; Zhang, Chuchu; Zhang, Mingjie. "Large protein assemblies formed by multivalent interactions between cadherin23 and harmonin suggest a stable anchorage structure at the tip link of stereocilia."  J. Biol. Chem. 287, 33460-33471 (2012).

Assembly members:
harmonin, polymer, 80 residues, 9567.188 Da.
cadherin23, polymer, 16 residues, 1908.306 Da.

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):
harmonin: MDRKVAREFRHKVDFLIEND AEKDYLYDVLRMYHQTMDVA VLVGDLKLVINEPSRLPLFD AIRPLIPLKHQVEYDQLTPR
cadherin23: GSLLKEVLEDYLRLKK

Data sets:
Data typeCount
13C chemical shifts322
15N chemical shifts91
1H chemical shifts719

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1harmonin1
2cadherin232

Entities:

Entity 1, harmonin 80 residues - 9567.188 Da.

1   METASPARGLYSVALALAARGGLUPHEARG
2   HISLYSVALASPPHELEUILEGLUASNASP
3   ALAGLULYSASPTYRLEUTYRASPVALLEU
4   ARGMETTYRHISGLNTHRMETASPVALALA
5   VALLEUVALGLYASPLEULYSLEUVALILE
6   ASNGLUPROSERARGLEUPROLEUPHEASP
7   ALAILEARGPROLEUILEPROLEULYSHIS
8   GLNVALGLUTYRASPGLNLEUTHRPROARG

Entity 2, cadherin23 16 residues - 1908.306 Da.

1   GLYSERLEULEULYSGLUVALLEUGLUASP
2   TYRLEUARGLEULYSLYS

Samples:

sample_1: harmonin, [U-99% 13C; U-99% 15N], 0.6 mM; cadherin23, [U-99% 13C; U-99% 15N], 0.6 mM; potassium phosphate 100 mM; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

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

PIPP, Garrett - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAA81739 BAA81740 BAF83477 BAG62565
EMBL CAH92093
GB AAC18048 AAC18049 AAG12457 AAG12458 AAH10819
REF NP_001030459 NP_001126221 NP_001157205 NP_001278111 NP_001284693
SP Q3MHQ0 Q9ES64 Q9Y6N9
TPG DAA00086 DAA22239

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts