BMRB Entry 18441

Name: Solution structure of harmonin N terminal domain in complex with a exon68 encoded peptide of cadherin23
Published: 2012-08-13

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PDB ID: 2lsr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18441
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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 of harmonin N terminal domain in complex with a exon68 encoded peptide of cadherin23

Deposition date:

2012-05-04

Original release date:

2012-08-13

Authors:

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

Citation:

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).
PubMed: 22879593

Assembly members:

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

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: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
harmonin: MDRKVAREFRHKVDFLIEND AEKDYLYDVLRMYHQTMDVA VLVGDLKLVINEPSRLPLFD AIRPLIPLKHQVEYDQLTPR
cadherin23: GSLLKEVLEDYLRLKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	322
15N chemical shifts	91
1H chemical shifts	719

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	harmonin	1
2	cadherin23	2

Entities:

Entity 1, harmonin 80 residues - 9567.188 Da.

1	MET	ASP	ARG	LYS	VAL	ALA	ARG	GLU	PHE	ARG
2	HIS	LYS	VAL	ASP	PHE	LEU	ILE	GLU	ASN	ASP
3	ALA	GLU	LYS	ASP	TYR	LEU	TYR	ASP	VAL	LEU
4	ARG	MET	TYR	HIS	GLN	THR	MET	ASP	VAL	ALA
5	VAL	LEU	VAL	GLY	ASP	LEU	LYS	LEU	VAL	ILE
6	ASN	GLU	PRO	SER	ARG	LEU	PRO	LEU	PHE	ASP
7	ALA	ILE	ARG	PRO	LEU	ILE	PRO	LEU	LYS	HIS
8	GLN	VAL	GLU	TYR	ASP	GLN	LEU	THR	PRO	ARG

Entity 2, cadherin23 16 residues - 1908.306 Da.

1

GLY

SER

LEU

LYS

GLU

VAL

LEU

GLU

ASP

2

TYR

LEU

ARG

LEU

LYS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

PDB	2KBQ 2KBR 2LSR 3K1R 2LSR
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
AlphaFold	Q3MHQ0 Q9ES64 Q9Y6N9

BMRB Entry 18441

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	MET	ASP	ARG	LYS	VAL	ALA	ARG	GLU	PHE	ARG
2	HIS	LYS	VAL	ASP	PHE	LEU	ILE	GLU	ASN	ASP
3	ALA	GLU	LYS	ASP	TYR	LEU	TYR	ASP	VAL	LEU
4	ARG	MET	TYR	HIS	GLN	THR	MET	ASP	VAL	ALA
5	VAL	LEU	VAL	GLY	ASP	LEU	LYS	LEU	VAL	ILE
6	ASN	GLU	PRO	SER	ARG	LEU	PRO	LEU	PHE	ASP
7	ALA	ILE	ARG	PRO	LEU	ILE	PRO	LEU	LYS	HIS
8	GLN	VAL	GLU	TYR	ASP	GLN	LEU	THR	PRO	ARG

1	MET	ASP	ARG	LYS	VAL	ALA	ARG	GLU	PHE	ARG
2	HIS	LYS	VAL	ASP	PHE	LEU	ILE	GLU	ASN	ASP
3	ALA	GLU	LYS	ASP	TYR	LEU	TYR	ASP	VAL	LEU
4	ARG	MET	TYR	HIS	GLN	THR	MET	ASP	VAL	ALA
5	VAL	LEU	VAL	GLY	ASP	LEU	LYS	LEU	VAL	ILE
6	ASN	GLU	PRO	SER	ARG	LEU	PRO	LEU	PHE	ASP
7	ALA	ILE	ARG	PRO	LEU	ILE	PRO	LEU	LYS	HIS
8	GLN	VAL	GLU	TYR	ASP	GLN	LEU	THR	PRO	ARG

1	MET	ASP	ARG	LYS	VAL	ALA	ARG	GLU	PHE	ARG
2	HIS	LYS	VAL	ASP	PHE	LEU	ILE	GLU	ASN	ASP
3	ALA	GLU	LYS	ASP	TYR	LEU	TYR	ASP	VAL	LEU
4	ARG	MET	TYR	HIS	GLN	THR	MET	ASP	VAL	ALA
5	VAL	LEU	VAL	GLY	ASP	LEU	LYS	LEU	VAL	ILE
6	ASN	GLU	PRO	SER	ARG	LEU	PRO	LEU	PHE	ASP
7	ALA	ILE	ARG	PRO	LEU	ILE	PRO	LEU	LYS	HIS
8	GLN	VAL	GLU	TYR	ASP	GLN	LEU	THR	PRO	ARG