BMRB Entry 15154

Name: HtrA1 bound to an optimized peptide: NMR assignment of PDZ domain and ligand resonances
Published: 2008-02-11

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PDB ID: 2joa
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15154
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: HtrA1 bound to an optimized peptide: NMR assignment of PDZ domain and ligand resonances PubMed: 17962403

Deposition date: 2007-03-01 Original release date: 2008-02-11

Authors: Runyon, Steven; Zhang, Yingnan; Appleton, Brent; Sazinksy, Stephen; Wu, Ping; Pan, Borlan; Wiesmann, Christian; Skelton, Nicholas; Sidhu, Sachdev

Citation: Runyon, Steven; Zhang, Yingnan; Appleton, Brent; Sazinksy, Stephen; Wu, Ping; Pan, Borlan; Wiesmann, Christian; Skelton, Nicholas; Sidhu, Sachdev. "Structural and functional analysis of the PDZ domains of human HtrA1 and HtrA3" Protein Sci. 16, 2454-2471 (2007).

Assembly members:
HtrA1-PDZ, polymer, 105 residues, 11587.366 Da.
synthetic_peptide_H1-C1, polymer, 7 residues, 962.093 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):
HtrA1-PDZ: GSHMKKYIGIRMMSLTSSKA KELKDRHRDFPDVISGAYII EVIPDTPAEAGGLKENDVII SINGQSVVSANDVSDVIKRE STLNMVVRRGNEDIMITVIP EEIDP
synthetic_peptide_H1-C1: DSRIWWV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	782
13C chemical shifts	432
15N chemical shifts	105

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Entity Assembly ID	Entity Name	Entity ID
1	HtrA1-PDZ	1
2	peptide	2

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY 13C,15N-filtered in F1	sample_5	isotropic	sample_conditions_1
2D 1H-1H TOCSY,13C,15N-filtered in F1	sample_5	isotropic	sample_conditions_1
3D 1H-13C NOESY, 13C-filtered in F1	sample_6	isotropic	sample_conditions_1

SWS	Q92743
PDB	2JOA 2YTW 3NUM 3NZI
DBJ	BAA13322 BAF82778 BAG52446 BAG52557 BAJ20722
EMBL	CAA69226 CAI05909
GB	AAC95151 AAC97211 AAD41525 AAH11352 AAI56553
REF	NP_001245105 NP_001269011 NP_002766 XP_002807519 XP_002821267
SP	F1N152 Q92743
TPG	DAA14692

Biological Magnetic Resonance Data Bank

BMRB Entry 15154

Title: HtrA1 bound to an optimized peptide: NMR assignment of PDZ domain and ligand resonances PubMed: 17962403

Additional metadata:

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