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 26770

Title: CP12 reduced state   PubMed: 27268235

Deposition date: 2016-03-24 Original release date: 2016-09-02

Authors: Launay, Helene; Barre, Patrick; Puppo, Carine; Receveur-Brechot, Veronique; Gontero-Meunier, Brigitte

Citation: Launay, Helene; Barre, Patrick; Puppo, Carine; Manneville, Stephanie; Gontero-Meunier, Brigitte; Receveur-Brechot, Veronique. "Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state"  Biochem. Biophys. Res. Commun. 477, 20-26 (2016).

Assembly members:
CP12_reduced, polymer, 99 residues, Formula weight is not available

Natural source:   Common Name: green algae   Taxonomy ID: 3055   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Chlamydomonas reinhardtii

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

Entity Sequences (FASTA):
CP12_reduced: HHHHHHHHHSSGHIEGRHMS GQPAVDLNKKVQDAVKEAED ACAKGTSADCAVAWDTVEEL SAAVSHKKDAVKADVTLTDP LEAFCKDAPDADECRVYED

Data sets:
Data typeCount
13C chemical shifts263
15N chemical shifts85
1H chemical shifts467

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CP12 reduced1

Entities:

Entity 1, CP12 reduced 99 residues - Formula weight is not available

1   HISHISHISHISHISHISHISHISHISSER
2   SERGLYHISILEGLUGLYARGHISMETSER
3   GLYGLNPROALAVALASPLEUASNLYSLYS
4   VALGLNASPALAVALLYSGLUALAGLUASP
5   ALACYSALALYSGLYTHRSERALAASPCYS
6   ALAVALALATRPASPTHRVALGLUGLULEU
7   SERALAALAVALSERHISLYSLYSASPALA
8   VALLYSALAASPVALTHRLEUTHRASPPRO
9   LEUGLUALAPHECYSLYSASPALAPROASP
10   ALAASPGLUCYSARGVALTYRGLUASP

Samples:

sample_1: CP12 reduced, [U-100% 13C; U-100% 15N], 770 uM; DTT 20 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 2%

sample_conditions_1: pH: 6.5; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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