BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30565

Title: Solution structure of the Arabidopsis thaliana RALF8 peptide   PubMed: 31004454

Deposition date: 2019-01-30 Original release date: 2019-05-02

Authors: Lee, W.; Markley, J.; Frederick, R.; Miyoshi, H.; Tonelli, M.; Cornilescu, G.; Cornilescu, C.; Sussman, M.

Citation: Frederick, R.; Miyoshi, H.; Tonelli, M.; Lee, W.; Cornilescu, G.; Cornilescu, C.; Sussman, M.; Markley, J.. "NMR Assignments and solution structure of the Arabidopsis thaliana RALF8 peptide"  Protein Sci. 28, 1115-1126 (2019).

Assembly members:
entity_1, polymer, 56 residues, 6248.083 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: EASVRYITYPAIDRGDHAVH CDKAHPNTCKKKQANPYRRG CGVLEGCHRETGPKPT

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts50
1H chemical shifts307

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 56 residues - 6248.083 Da.

1   GLUALASERVALARGTYRILETHRTYRPRO
2   ALAILEASPARGGLYASPHISALAVALHIS
3   CYSASPLYSALAHISPROASNTHRCYSLYS
4   LYSLYSGLNALAASNPROTYRARGARGGLY
5   CYSGLYVALLEUGLUGLYCYSHISARGGLU
6   THRGLYPROLYSPROTHR

Samples:

sample_1: Rapid ALkalinization Factor-8 (RALF8), [U-13C; U-15N], 1.0 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

VNMR, Varian - collection

AUDANA, W. Lee, C.M. Petit, G. Cornilescu, J.L. Stark, J.L. Markley - structure calculation

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

SMILE, J. Ying, F. Delaglio, D.A. Torchia, and A. Bax - processing

NMRFAM-SPARKY, W. Lee, M. Tonelli, J.L. Markley - chemical shift assignment, peak picking

I-PINE, W. Lee, A. Bahrami, H. Dashti, H.R. Eghbalnia, M. Tonelli, W.M. Westler, J.L. Markley - chemical shift assignment

TALOS-N, Y. Shen, A. Bax - structure calculation

PECAN, Eghbalnia, Wang, Bahrami, Assadi, and Markley - structure calculation

PONDEROSA-C/S, W. Lee, J.L. Stark, J.L. Markley - refinement, structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Varian VNMRS 600 MHz
  • Varian VNMRS 800 MHz

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