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 17627

Title: 1H, 13C, and 15N chemical shift assignments for apo actinin-2 C-terminal EF-hand (Act2-EF34)

Deposition date: 2011-05-05 Original release date: 2011-06-03

Authors: Au, Yunghan; Beck, Moriah; Campbell, Sharon; Pastore, Annalisa

Citation: Au, Yunghan; Pastore, Annalisa. "The Interaction of alpha-Actinin-2 with ZASP and Titin"  Not known ., .-. (2004).

Assembly members:
Act2-EF34, polymer, 75 residues, 8071.05 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):
Act2-EF34: GAMADTDTAEQVIASFRILA SDKPYILAEELRRELPPDQA QYCIKRMPAYSGPGSVPGAL DYAAFSSALYGESDL

Data sets:
Data typeCount
13C chemical shifts135
15N chemical shifts67
1H chemical shifts276

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ef-Hands 3,4 From Alpha-Actinin1

Entities:

Entity 1, Ef-Hands 3,4 From Alpha-Actinin 75 residues - 8071.05 Da.

N-terminal residue of natural sequence replaced by M N-terminal GA left after cleavage from fusion protein

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

Samples:

sample_1: Act2-EF34, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; D2O, [U-2H], 10%; sodium phosphate 20 mM; sodium azide 0.02 mM; H2O 90%

sample_2: Act2-EF34, [U-100% 15N], 0.5 – 1 mM; D2O, [U-2H], 10%; sodium phosphate 20 mM; sodium azide 0.02 mM; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 6.6; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking, processing

XEASY, Bartels et al. - data analysis

NMR spectrometers:

  • Varian Unity 500 MHz
  • Varian Unity 600 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 17626 4453 4454
PDB
DBJ BAB22865 BAD92758 BAG37672 BAH11921 BAH12587
EMBL CAB61269
GB AAA51583 AAF76325 AAH47901 AAH51770 AAH89579
REF NP_001029807 NP_001094 NP_001163796 NP_001230595 NP_001265272
SP P35609 Q3ZC55 Q9JI91

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