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 17143

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the first dsRBD of protein HYL1   PubMed: 20735118

Deposition date: 2010-08-23 Original release date: 2010-09-24

Authors: Rasia, Rodolfo; Mateos, Julieta; Bologna, Nicolas; Burdisso, Paula; Imbert, Lionel; Palatnik, Javier; Boisbouvier, Jerome

Citation: Rasia, Rodolfo; Mateos, Julieta; Bologna, Nicolas; Burdisso, Paula; Imbert, Lionel; Palatnik, Javier; Boisbouvier, Jerome. "Structure and RNA Interactions of the Plant MicroRNA Processing-Associated Protein HYL1."  Biochemistry 49, 8237-8239 (2010).

Assembly members:
HYL1_dsRBD_1, polymer, 103 residues, 8031.225 Da.

Natural source:   Common Name: thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-TEV

Entity Sequences (FASTA):
HYL1_dsRBD_1: GHMMTSTDVSSGVSNCYVFK SRLQEYAQKYKLPTPVYEIV KEGPSHKSLFQSTVILDGVR YNSLPGFFNRKAAEQSAAEV ALRELAKSSELSQCVSQPVH ETG

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts80
1H chemical shifts156
residual dipolar couplings292

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HYL1_dsRBD_1-11

Entities:

Entity 1, HYL1_dsRBD_1-1 103 residues - 8031.225 Da.

1   GLYHISMETMETTHRSERTHRASPVALSER
2   SERGLYVALSERASNCYSTYRVALPHELYS
3   SERARGLEUGLNGLUTYRALAGLNLYSTYR
4   LYSLEUPROTHRPROVALTYRGLUILEVAL
5   LYSGLUGLYPROSERHISLYSSERLEUPHE
6   GLNSERTHRVALILELEUASPGLYVALARG
7   TYRASNSERLEUPROGLYPHEPHEASNARG
8   LYSALAALAGLUGLNSERALAALAGLUVAL
9   ALALEUARGGLULEUALALYSSERSERGLU
10   LEUSERGLNCYSVALSERGLNPROVALHIS
11   GLUTHRGLY

Samples:

Isotropic_sample: HYL1 dsRBD 1, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 100 mM; sodium chloride 50 mM; DTT 10 mM; sodium azide 0.05%; H2O 90%; D2O 10%

Aligned_sample: HYL1 dsRBD 1, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 100 mM; sodium chloride 50 mM; DTT 10 mM; sodium azide 0.05%; C12E5 5%; Hexanol 0.2%; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCIsotropic_sampleisotropicsample_conditions_1
3D HNCOIsotropic_sampleisotropicsample_conditions_1
3D HNCAIsotropic_sampleisotropicsample_conditions_1
3D HNCACBIsotropic_sampleisotropicsample_conditions_1
3D HN(CO)CAIsotropic_sampleisotropicsample_conditions_1
3D HN(COCA)CBIsotropic_sampleisotropicsample_conditions_1
3D HN(CA)COIsotropic_sampleisotropicsample_conditions_1
3D HBHA(CO)NHIsotropic_sampleisotropicsample_conditions_1
3D HNCO JNHIsotropic_sampleisotropicsample_conditions_1
3D HNCOCA JCAHAIsotropic_sampleisotropicsample_conditions_1
3D HNCO JCACOIsotropic_sampleisotropicsample_conditions_1
3D HNCO JCHIsotropic_sampleisotropicsample_conditions_1
3D HNCO JNHAligned_sampleanisotropicsample_conditions_1
3D HNCOCA JCAHAAligned_sampleanisotropicsample_conditions_1
3D HNCO JCACOAligned_sampleanisotropicsample_conditions_1
3D HNCO JCHAligned_sampleanisotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian DirectDrive 600 MHz

Related Database Links:

PDB
GB AAB60726 AAG49890 AAK96822 AAM10087 AEE28481
REF NP_563850
SP O04492
AlphaFold O04492

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