BMRB Entry 16507

Title:
NMR structure of mouse Par3-PDZ3 in complex with VE-Cadherin C-terminus
Deposition date:
2009-09-22
Original release date:
2010-01-28
Authors:
Volkman, B.; Tyler, R.; Peterson, F.
Citation:

Citation: Tyler, Robert; Peterson, Francis; Volkman, Brian. "Distal interactions within the par3-VE-cadherin complex."  Biochemistry 49, 951-957 (2010).
PubMed: 20047332

Assembly members:

Assembly members:
MmPar3_PDZ3, polymer, 111 residues, 11905.506 Da.
MmVE-Cadherin, polymer, 16 residues, 1821.067 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: pQE30-SMT

Data sets:
Data typeCount
13C chemical shifts499
15N chemical shifts137
1H chemical shifts841

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MmPar3 PDZ31
2MmVE-Cadherin2

Entities:

Entity 1, MmPar3 PDZ3 111 residues - 11905.506 Da.

The N-terminal GS dipeptide is a cloning artifact.

1   GLYSERASPGLYTHRARGGLUPHELEUTHR
2   PHEGLUVALPROLEUASNASPSERGLYSER
3   ALAGLYLEUGLYVALSERVALLYSGLYASN
4   ARGSERLYSGLUASNHISALAASPLEUGLY
5   ILEPHEVALLYSSERILEILEASNGLYGLY
6   ALAALASERLYSASPGLYARGLEUARGVAL
7   ASNASPGLNLEUILEALAVALASNGLYGLU
8   SERLEULEUGLYLYSALAASNGLNGLUALA
9   METGLUTHRLEUARGARGSERMETSERTHR
10   GLUGLYASNLYSARGGLYMETILEGLNLEU
11   ILEVALALAARGARGILESERARGCYSASN
12   GLU

Entity 2, MmVE-Cadherin 16 residues - 1821.067 Da.

1   METLEUALAGLULEUTYRGLYSERASPPRO
2   GLNGLUGLULEUILEILE

Samples:

sample_1: MmPar3 PDZ3, [U-100% 13C; U-100% 15N], 1 mM; MmVE-Cadherin 2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; sodium azide 0.02%; H2O 90%

sample_2: MmVE-Cadherin, [U-100% 13C; U-100% 15N], 1 mM; MmPar3 PDZ3 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O 10%; sodium chloride 0.02%; H2O 90%

sample_conditions_1: ionic strength: 53 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sample_1isotropicsample_conditions_1
3D_15N-separated_NOESYsample_2isotropicsample_conditions_1
3D_13C-separated_NOESYsample_2isotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sample_2isotropicsample_conditions_1
3D_13C-F1-filtered_13C-F3-separated_NOESYsample_2isotropicsample_conditions_1
3D_13C-F1-filtered_13C-F3-separated_NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2007, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

NMR spectrometers:

  • Bruker Avance II 600 MHz

Related Database Links:

PDB
REF XP_009513481 XP_009571943 NP_001100877 NP_033998 XP_006530693
DBJ BAA22617 BAE39672
EMBL CAA58782
GB AAH54790 EDL11198 EDL87251
PRF 2208309A
SP P55284
AlphaFold P55284

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