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 15461

Title: NMR resonance assignment of the Ccc2ab protein   PubMed: 17961510

Deposition date: 2007-09-06 Original release date: 2008-06-25

Authors: Banci, Lucia; Bertini, Ivano; Chasapis, Christos; Rosato, Antonio; Tenroi, Leonardo

Citation: Banci, Lucia; Bertini, Ivano; Chasapis, Christos; Rosato, Antonio; Tenori, Leonardo. "Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1"  Biochem. Biophys. Res. Commun. 364, 645-649 (2007).

Assembly members:
Ccc2, polymer, 150 residues, Formula weight is not available

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Ccc2: MREVILAVHGMTCSACTNTI NTQLRALKGVTKCDISLVTN ECQVTYDNEVTADSIKEIIE DCGFDCEILRDSEITAISTK EGLLSVQGMTCGSCVSTVTK QVEGIEGVESVVVSLVTEEC HVIYEPSKTTLETAREMIED CGFDSNIIMD

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts127
1H chemical shifts127

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ccc21

Entities:

Entity 1, ccc2 150 residues - Formula weight is not available

1   METARGGLUVALILELEUALAVALHISGLY
2   METTHRCYSSERALACYSTHRASNTHRILE
3   ASNTHRGLNLEUARGALALEULYSGLYVAL
4   THRLYSCYSASPILESERLEUVALTHRASN
5   GLUCYSGLNVALTHRTYRASPASNGLUVAL
6   THRALAASPSERILELYSGLUILEILEGLU
7   ASPCYSGLYPHEASPCYSGLUILELEUARG
8   ASPSERGLUILETHRALAILESERTHRLYS
9   GLUGLYLEULEUSERVALGLNGLYMETTHR
10   CYSGLYSERCYSVALSERTHRVALTHRLYS
11   GLNVALGLUGLYILEGLUGLYVALGLUSER
12   VALVALVALSERLEUVALTHRGLUGLUCYS
13   HISVALILETYRGLUPROSERLYSTHRTHR
14   LEUGLUTHRALAARGGLUMETILEGLUASP
15   CYSGLYPHEASPSERASNILEILEMETASP

Samples:

sample_1: Ccc2, [U-100% 13C; U-100% 15N], 0.2 – 0.5 mM

sample_conditions_1: pH: 7.00; pressure: 1 atm; temperature: 298 K; viscosity: 100 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 7406

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