The Protein Folding Database
  Deposition
  Search
Adv. Search |
BLAST
  Menu
  PFD
  Links
  Login
Username:
Password:
Lost Password?
Register
Remember me?
  Statistics
Version: 2.2
Last Update: 8-Jun-2007
Entries: 296
Proteins: 70
Families: 53
Species: 30
ϕ values: 230 (5 proteins)
Locations of visitors to this page
  Latest Additions
ACBP (3 WT)
FRB (6 WT)
CI2 (3 WT, 202 mutants)
HPr (1 WT, 4 mutants)
Im7 (1 WT)
En-HD (1 WT)
Im9 (2 WT)
Abp1 SH3 (1 WT)
CheW (1 WT)
U1A (1 WT)
Powered by Mac OS X Server
Fulton et al (2005) Nucleic Acids Res. 33:D279-283  |  Fulton et al (2007) Nucleic Acids Res. 35:D304-307 About PFD | Help | Glossary
Folding Data
Expand All   |   Collapse All
Toggle printer friendly view

Note: A field with its data listed as "ND" denotes there is no data for that field.
[Measurement ID: 9] contact us to make corrections & updates to this data

Expand   Protein Data
Protein Name Chemotaxis protein CheW (CheW)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Beta   |   goto SCOP
SCOP Family CheW-like   |   goto SCOP

Expand   Construct Data
Species Thermotoga maritima (Thermotoga maritima)

goto 3D view
Sequence MKTLADALKEFEVLSFEIDEQALAFDVDNIEMVIEKSDITPVPKSRHFVE
GVINLRGRIIPVVNLAKILGISFDEQKMKSIIVARTKDVEVGFLVDRVLG
VLRITENQLDLTNVSDKFGKKSKGLVKTDGRLIIYLDIDKIIEEITVKEG
V

Blast PFD  |  Blast NCBI NR
Length 152
Molecular Weight 16936.8Da
Fusion None
PDB ID 1K0S   |   goto PDB  
PDB Resolution NMR
Chain Chain 1 (NMR)
Residues 9 - 151
SCOP ID 69272   |   goto SCOP
UniProt ID CHEW_THEMA   |   goto UniProt
Relative Contact Order 12.43

Expand   Publication Data
Publication Maxwell KL et al (2005) Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins., Protein Science 14, 602-616  goto pubmed
Data type in publication Equilibrium & Kinetic   |   view other data in this publication

Expand   Graphical Analysis Data
Chevron Plot chevron plot for measurement 9
unfolding & refolding data
ln(kuH2O)
(s-1)		 ln(kfH2O)
(s-1)		 m‡-N
(kJ mol-1 M-1)		 m‡-D
(kJ mol-1 M-1)
-12.05 ± 0.29 7.44 ± 0.31 5.01 ± 0.16 -8.92 ± 0.29
Notes on Chevron Plot Calculating
Contact Order Plot Data Acyl Coenzyme A Binding Protein Hypothetical protein YjbJ from Escherichia coli E colicin binding Immunity Protein 7 (ImmE7*) E colicin binding Immunity Protein 9 (ImmE9) Lambda C1 repressor, DNA-binding domain E colicin binding Immunity Protein 9 (ImmE9) Acyl Coenzyme A Binding Protein Acyl Coenzyme A Binding Protein Internalin B, C-terminal domain Apo-azurin Chemotaxis protein CheW Fyn proto-oncogene tyrosine kinase, SH3 domain Alpha-Spectrin SH3 Domain c-src tyrosine kinase SH3 Domain Actin binding protein 1 SH3 domain Activation Domain Of Human Procarboxypeptidase A2 Chymotrypsin Inhibitor 2 Ribosomal protein L9 C-domain FK-506 binding protein Ribosomal protein L23 Acylphosphatase Ribosomal protein L9 N-domain Immunoglobulin-binding protein G Immunoglobulin light chain-binding domain of protein L c-Raf1 RBD Ribosomal protein S6 c-src tyrosine kinase SH2 domain Spliceosomal U1A protein Ubiquitin FK-506 binding protein Chymotrypsin Inhibitor 2 Chymotrypsin Inhibitor 2
generated contact order graph

Moving your mouse over a data point will display that protein's name.
Clicking on a data point will display folding data on that protein.
To view more data on a SCOP Class click on it's name in the legend.
Note: Mutant measurements do not have their data plotted on this graph, instead the data from wildtype is marked in red.

view notes on contact order

Expand   Equilibrium Data & Methods
Equilibrium Data
[Denaturant] Minimum
(M)		 [Denaturant] 50%
(M)		 mD-N (m)
(kJ mol-1 M-1)		 ∆GD-N (m)
(kJ mol-1)
ND ND -14.6 ± 0.2 32.5 ± 1.4
Probe Far-UV Circular Dichroism  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Aviv 202SF Stopped Flow Circular Dichroism Spectrometer
Temperature 298K
pH 7
Buffer 0.05M Phosphate
Protein Concentration ND

Expand   Kinetic Data & Methods
Kinetic Unfolding Data
[Denaturant] Minimum
(M)		 [Denaturant] Maximum
(M)		 ku
(s-1)		 lnku
(s-1)		 mu
(M-1)		 m‡-N
(kJ mol-1 M-1)
3.7 5.2 0.0000060 ± ND (0M) -12.05 ± 0.29 (0M) ND 5.01 ± 0.16
Kinetic Folding Data
[Denaturant] Minimum
(M)		 [Denaturant] Maximum
(M)		 kfH2O
(s-1)		 ln(kfH2O)
(s-1)		 mf
(M-1)		 m‡-D
(kJ mol-1 M-1)
2.3 3.1 1702.75 ± 82.47 7.44 ± 0.31 ND -8.92 ± 0.29
Probe Far-UV Circular Dichroism  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Aviv 62A Circular Dichroism Spectrometer
Temperature 298K
pH 7
Buffer 0.05M Phosphate
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes Fold: barrel, closed or partly opened n=5, S=10 or S=8; greek-key. Family: duplication: tandem repeat of two swapped domains, one with a canonical OB-fold topology and one with a circular permutation
Construct Notes
Equilibrium Notes CheW. The protein, from T. maritima, was cloned into a modified pET15b vector and expressed with an amino-terminal 6-his tag followed by a TEV protease site and purified according to standard protocols (Qiagen). The tag was removed by overnight digestion with TEV protease at room temperature followed by a second passage over a Ni-NTA column. Equilibrium parameters were determined on an AVIV 62 CD spectrometer using a Microlab titrator.
Kinetic Notes CheW. The protein, from T. maritima, was cloned into a modified pET15b vector and expressed with an amino-terminal 6-his tag followed by a TEV protease site and purified according to standard protocols (Qiagen). The tag was removed by overnight digestion with TEV protease at room temperature followed by a second passage over a Ni-NTA column. Unfolding and refolding rates were determined under standard consensus conditions using an AVIV 202SF Stopped-flow CD spectrometer.
Comments view comments on this measurement

contact us to make corrections & updates to this data