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 51827

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for FASP peptide of hPER2   PubMed: 37207626

Deposition date: 2023-02-08 Original release date: 2023-02-13

Authors: Philpott, Jonathan; Hunt, Sabrina; Partch, Carrie

Citation: Philpott, Jonathan; Freeberg, Alfred; Park, Jiyoung; Lee, Kwangiun; Ricci, Clarisse; Hunt, Sabrina; Narasimamurthy, Rajesh; Segal, David; Robles, Rafael; Cai, Yao; Tripathi, Sarvind; McCammon, J. Andrew; Virshup, David; Chiu, Joanna; Lee, Choogon; Partch, Carrie. "PERIOD phosphorylation leads to feedback inhibition of CK1 activity to control circadian period"  Mol. Cell 83, 1677-1692 (2023).

Assembly members:
entity_1, polymer, 55 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):
entity_1: GAMDPEFWRKKKTGVGTHLT SLALPGKAESVASLTSQCSY SSTIVHVGDKKPQPE

Data sets:
Data typeCount
13C chemical shifts150
15N chemical shifts48
1H chemical shifts48

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hPER2 FASP1

Entities:

Entity 1, hPER2 FASP 55 residues - Formula weight is not available

Residues 1-12 represent non-native sequence. Residues 13-55 correspond to hPER2 residues 645-687.

1   GLYALAMETASPPROGLUPHETRPARGLYS
2   LYSLYSTHRGLYVALGLYTHRHISLEUTHR
3   SERLEUALALEUPROGLYLYSALAGLUSER
4   VALALASERLEUTHRSERGLNCYSSERTYR
5   SERSERTHRILEVALHISVALGLYASPLYS
6   LYSPROGLNPROGLU

Samples:

sample_1: hPER2 FASP, [U-13C; U-15N], 0.5 mM; MES 25 mM; sodium chloride 50 mM; TCEP 2 mM; EDTA 1 mM; Pierce protease inhibitor tablet 1 tablet/50mL; ATP 2.5 mM; D2O, [U-2H], 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRDraw - processing

CcpNMR_Analysis - chemical shift assignment, data analysis, peak picking

hmsIST - data reconstruction

NMR spectrometers:

  • Varian INOVA 600 MHz

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