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 19237

Title: Solution structure of AhPDF1 from Arabidopsis halleri

Deposition date: 2013-05-13 Original release date: 2014-05-12

Authors: Meindre, Fanny; Paquet, Francoise; Landon, Celine

Citation: Meindre, Fanny; Paquet, Francoise; Landon, Celine; Meindre, Fanny; Paquet, Francoise; Landon, Celine. "Folding and structural studies of the protein AhPDF1"  Not known ., .-..

Assembly members:
AhPDF1, polymer, 51 residues, 5699.622 Da.

Natural source:   Common Name: Eudicots   Taxonomy ID: 81970   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Arabidopsis halleri

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
AhPDF1: XRLCEKPSGTWSGVCGNNGA CRNQCIRLEKARHGSCNYVF PAHKCICYFPC

Data sets:
Data typeCount
13C chemical shifts128
15N chemical shifts30
1H chemical shifts344

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AhPDF1 from Arabidopsis halleri1

Entities:

Entity 1, AhPDF1 from Arabidopsis halleri 51 residues - 5699.622 Da.

1   PCAARGLEUCYSGLULYSPROSERGLYTHR
2   TRPSERGLYVALCYSGLYASNASNGLYALA
3   CYSARGASNGLNCYSILEARGLEUGLULYS
4   ALAARGHISGLYSERCYSASNTYRVALPHE
5   PROALAHISLYSCYSILECYSTYRPHEPRO
6   CYS

Samples:

sample_1: AhPDF1 1.3 mM; H2O 90%; D2O 10%

sample_2: AhPDF1 1.3 mM; D2O 100%

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 273 K

sample_conditions_2: pH: 4.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_2isotropicsample_conditions_2

Software:

CcpNMR v2.2.2, CCPN - chemical shift assignment, peak picking

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

ARIA v2.3, Linge, O, . - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CCN97877
GB AAY27736

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