BMRB Entry 17626

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Act2-EF34 in complex with palladin peptide
Deposition date:
2011-05-05
Original release date:
2011-10-12
Authors:
Beck, Moriah; Campbell, Sharon
Citation:

Citation: Beck, Moriah; Otey, Carol; Campbell, Sharon. "Structural characterization of the interactions between palladin and -actinin."  J. Mol. Biol. 413, 712-725 (2011).
PubMed: 21925511

Assembly members:

Assembly members:
Act2-EF34, polymer, 75 residues, 8071.05 Da.
palladin, polymer, 17 residues, 1777 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: pET9d

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts103
15N chemical shifts54
1H chemical shifts54

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein1
2ligand2

Entities:

Entity 1, protein 75 residues - 8071.05 Da.

1   GLYALAMETALAASPTHRASPTHRALAGLU
2   GLNVALILEALASERPHEARGILELEUALA
3   SERASPLYSPROTYRILELEUALAGLUGLU
4   LEUARGARGGLULEUPROPROASPGLNALA
5   GLNTYRCYSILELYSARGMETPROALATYR
6   SERGLYPROGLYSERVALPROGLYALALEU
7   ASPTYRALAALAPHESERSERALALEUTYR
8   GLYGLUSERASPLEU

Entity 2, ligand 17 residues - 1777 Da.

Residues 235-252 of 90kDa (isoform #4) of palladin

1   HISGLYGLNTHRPROALAALAPHELEUSER
2   ALALEULEUPROSERGLNPRO

Samples:

sample_1: Act2-EF34, [U-100% 15N], 0.2 – 0.5 mM; palladin0.5 – 2 mM; D2O 10%; sodium azide 0.05 mM; TCEP2 – 5 mM; MOPS 20 mM; sodium chloride 10 mM; H2O 90%

sample_2: Act2-EF34, [U-100% 13C; U-100% 15N], 0.2 – 0.5 mM; palladin0.5 – 2 mM; D2O 10%; sodium azide 0.05 mM; TCEP2 – 5 mM; MOPS 20 mM; sodium chloride 10 mM; H2O 90%

sample_conditions_1: ionic strength: 0.01 M; pH: 6.6; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRViewJ v8.1, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 700 MHz
  • Varian INOVA 700 MHz

Related Database Links:

BMRB 17627 4453 4454
PDB
DBJ BAB22865 BAD92758 BAG37672 BAH11921 BAH12587 BAA76836 BAG09933
EMBL CAB61269
GB AAA51583 AAF76325 AAH47901 AAH51770 AAH89579 AAG00079 EDL87206
REF NP_001029807 NP_001094 NP_001163796 NP_001230595 NP_001265272 XP_004852973 XP_004852974 XP_005003446 XP_005369855 XP_005369857
SP P35609 Q3ZC55 Q9JI91
AlphaFold Q9JI91 P35609 Q3ZC55

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