BMRB Entry 15808

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15808

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Title:
Assignment of the 1H, 13C and 15N resonance of the Calponin Homology-2 domain of alpha-actinin-4
Deposition date:
2008-06-17
Original release date:
2008-10-03
Authors:
Chen, Huang-Hui; Murchland, Iain; Booker, Grant
Citation:

Citation: Chen, Huang-Hui; Murchland, Iain; Booker, Grant. "Assignment of the 1H, 13C and 15N resonances of the calponin homology-2 domain of alpha-actinin-4"  Biomol. NMR Assignments 2, 195-197 (2008).
PubMed: 19636903

Assembly members:

Assembly members:
alpha-Actinin4, polymer, 113 residues, Formula weight is not available

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: pGEX-4T2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alpha-Actinin4: GSETSAKEGLLLWCQRKTAP YKNVNVQNFHISWKDGLAFN ALIHRHRPELIEYDKLRKDD PVTNLNNAFEVAEKYLDIPK MLDAEDIVNTARPDEKAIMT YVSSFYHAFSGAQ

Data sets:
Data typeCount
13C chemical shifts443
15N chemical shifts114
1H chemical shifts749

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CH2 domain1

Entities:

Entity 1, CH2 domain 113 residues - Formula weight is not available

1   GLYSERGLUTHRSERALALYSGLUGLYLEU
2   LEULEUTRPCYSGLNARGLYSTHRALAPRO
3   TYRLYSASNVALASNVALGLNASNPHEHIS
4   ILESERTRPLYSASPGLYLEUALAPHEASN
5   ALALEUILEHISARGHISARGPROGLULEU
6   ILEGLUTYRASPLYSLEUARGLYSASPASP
7   PROVALTHRASNLEUASNASNALAPHEGLU
8   VALALAGLULYSTYRLEUASPILEPROLYS
9   METLEUASPALAGLUASPILEVALASNTHR
10   ALAARGPROASPGLULYSALAILEMETTHR
11   TYRVALSERSERPHETYRHISALAPHESER
12   GLYALAGLN

Samples:

15N_sample: alpha-Actinin4, [U-100% 15N], 3 mM; sodium phosphate 10 mM

15N_13C_sample: alpha-Actinin4, [U-100% 13C; U-100% 15N], 3 mM; sodium phosphate 10 mM

D2O_sample: alpha-Actinin4, [U-100% 15N], 3 mM; sodium phosphate 10 mM

unlabelled: alpha-Actinin4 3 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_sampleisotropicsample_conditions_1
2D 1H-1H TOCSYunlabelledisotropicsample_conditions_1
2D 1H-1H NOESYunlabelledisotropicsample_conditions_1
2D 1H-1H NOESYD2O_sampleisotropicsample_conditions_1
3D HNCA15N_13C_sampleisotropicsample_conditions_1
3D HN(CO)CA15N_13C_sampleisotropicsample_conditions_1
3D HNCO15N_13C_sampleisotropicsample_conditions_1
3D CBCA(CO)NH15N_13C_sampleisotropicsample_conditions_1
3D HCCH-TOCSY15N_13C_sampleisotropicsample_conditions_1
3D 1H-15N NOESY15N_sampleisotropicsample_conditions_1
3D 1H-15N TOCSY15N_sampleisotropicsample_conditions_1

Software:

ARIA v2.1, Linge, O'Donoghue and Nilges - structure solution

NMRPipe v2.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ANALYSIS v1.0.15, CCPN - chemical shift assignment, data analysis, peak picking

VNMR v4.1c, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA05644 BAA24447 BAE26366 BAE29264 BAG61782
EMBL CAC10069 CAH90431
GB AAC17470 AAC53102 AAF20064 AAH05033 AAH13616
REF NP_001006810 NP_001087030 NP_001089864 NP_001091521 NP_001127286
SP A5D7D1 O43707 P57780 Q5RCS6 Q90734
TPG DAA19939
AlphaFold P57780 A5D7D1 O43707 Q5RCS6 Q90734

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