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 5697

Title: 1H and 15N resonance assignments of the PDZ domain of ZASP in complex with the EF hand domains of alpha-actinin-2   PubMed: 15062084

Deposition date: 2003-02-17 Original release date: 2004-04-07

Authors: Au, Yunghan; Atkinson, R.; Faulkner, Georgine; Frenkiel, Thomas; Joseph, Catherine; Kelly, Geoff; Muskett, Frederick; Pallavicini, Alberto; Pastore, Annalisa

Citation: Au, Yunghan; Atkinson, R.; Guerrini, R.; Kelly, Geoff; Joseph, Catherine; Martin, S.; Muskett, Frederick; Pallavicini, Alberto; Faulkner, Georgine; Pastore, Annalisa. "Solution Structure of ZASP PDZ Domain; Implications for Sarcomere Ultrastructure and Enigma Family Redundancy"  Structure (Cambridge, MA, U. S.) 12, 611-622 (2004).

Assembly members:
Z-band alternatively spliced PDZ motif protein, polymer, 85 residues, 9139.40 Da.
Alpha-Actinin-2 EF-hand domains, polymer, 154 residues, 17163.2 Da.

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Z-band alternatively spliced PDZ motif protein: MAYSVTLTGPGPWGFRLQGG KDFNMPLTISRITPGSKAAQ SQLSQGDLVVAIDGVNTDTM THLEAQNKIKSASYNLSLTL QKSKR
Alpha-Actinin-2 EF-hand domains: GAMGRDAKGITQEQMNEFRA SFNHFDRRKNGLMDHEDFRA CLISMGYDLGEAEFARIMTL VDPNGQGTVTFQSFIDFMTR EPADTDTAEQVIASFRILAS DKPYILAEELRRELPPDQAQ YCIKRMPAYSGPGSVPGALD YAAFSSALYGESDL

Data sets:
Data typeCount
1H chemical shifts434
15N chemical shifts82

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ZASP-PDZ Domain1
2Alpha-Actinin-2 EF-hand domain2

Entities:

Entity 1, ZASP-PDZ Domain 85 residues - 9139.40 Da.

1   METALATYRSERVALTHRLEUTHRGLYPRO
2   GLYPROTRPGLYPHEARGLEUGLNGLYGLY
3   LYSASPPHEASNMETPROLEUTHRILESER
4   ARGILETHRPROGLYSERLYSALAALAGLN
5   SERGLNLEUSERGLNGLYASPLEUVALVAL
6   ALAILEASPGLYVALASNTHRASPTHRMET
7   THRHISLEUGLUALAGLNASNLYSILELYS
8   SERALASERTYRASNLEUSERLEUTHRLEU
9   GLNLYSSERLYSARG

Entity 2, Alpha-Actinin-2 EF-hand domain 154 residues - 17163.2 Da.

1   GLYALAMETGLYARGASPALALYSGLYILE
2   THRGLNGLUGLNMETASNGLUPHEARGALA
3   SERPHEASNHISPHEASPARGARGLYSASN
4   GLYLEUMETASPHISGLUASPPHEARGALA
5   CYSLEUILESERMETGLYTYRASPLEUGLY
6   GLUALAGLUPHEALAARGILEMETTHRLEU
7   VALASPPROASNGLYGLNGLYTHRVALTHR
8   PHEGLNSERPHEILEASPPHEMETTHRARG
9   GLUPROALAASPTHRASPTHRALAGLUGLN
10   VALILEALASERPHEARGILELEUALASER
11   ASPLYSPROTYRILELEUALAGLUGLULEU
12   ARGARGGLULEUPROPROASPGLNALAGLN
13   TYRCYSILELYSARGMETPROALATYRSER
14   GLYPROGLYSERVALPROGLYALALEUASP
15   TYRALAALAPHESERSERALALEUTYRGLY
16   GLUSERASPLEU

Samples:

Sample_1: Z-band alternatively spliced PDZ motif protein, [U-15N], 0.14 mM; Alpha-Actinin-2 EF-hand domains 0.28 mM; sodium phosphate 20 mM; sodium azide 0.2 % v/v; deuterium oxide 10 % v/v

Condition_1: pH: 6.6; temperature: 300 K; ionic strength: 0.02 M

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availablenot available
1H-15N TOCSYnot availablenot availablenot available
1H-15N NOESYnot availablenot availablenot available

Software:

nmrPipe - processing

XEASY - analysis

NMR spectrometers:

  • Varian UnityPlus 500 MHz
  • Varian UnityPlus 600 MHz

Related Database Links:

PDB
DBJ BAD92758 BAG37672 BAH11921 BAH12587 BAH12632 BAD92758 BAG37672
EMBL CAB61269 CAI13778 CAB61269 CAH73201
GB AAA51583 AAH47901 AAH51770 AAI02909 AIC48214
REF NP_001029807 NP_001094 NP_001230595 NP_001265272 NP_001265273 NP_001094
SP P35609 Q3ZC55
TPG DAA14356
SWISS-PROT P35609
GenBank EAW70064 EAW70065 AAH47901 AAH51770 AAA51583
AlphaFold P35609 Q3ZC55

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