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  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)
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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
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Note: A field with its data listed as "ND" denotes there is no data for that field.
[Measurement ID: 24] contact us to make corrections & updates to this data

Expand   Protein Data
Protein Name Ribosomal protein S6 (S6)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Alpha+Beta   |   goto SCOP
SCOP Family Ribosomal protein S6   |   goto SCOP

Expand   Construct Data
Species Thermus thermophilus (Thermus thermophilus)

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Sequence MRRYEVNIVLNPNLDQSQLALGKEIIQRALENYGARVEKVEELGLRRLAY
PIAKDPQGYFLWYQVEMPEDRVNDLARELRIRDNVRRVMVVKSQEPFLAN
A

Blast PFD  |  Blast NCBI NR
Length 101
Molecular Weight 11882.7Da
Fusion None
PDB ID 1RIS   |   goto PDB  
PDB Resolution 2Å
Chain Any chain
Residues 1 - 97
SCOP ID 54988   |   goto SCOP
UniProt ID RS6_THETH   |   goto UniProt
Relative Contact Order 18.02

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 24
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)
-8.28 ± 0.49 6.07 ± 0.21 3.13 ± 0.22 -7.04 ± 0.28
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

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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 -10 ± 0.1 34.7 ± 0.4
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Jobin-Yvon Horiba Fluoromax 3
Temperature 298K
pH 7.5
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)
3.89 6.92 0.000254 ± 0.000031 (0M) -8.28 ± 0.49 (0M) ND 3.13 ± 0.22
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)
0.46 3.58 432.68 ± 9.58 6.07 ± 0.21 ND -7.04 ± 0.28
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Bio-Logic SFM4/QFM4 Stopped-flow Fluorometer  what is this?
Temperature 298K
pH 7.5
Buffer 0.05M Phosphate
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes
Construct Notes
Equilibrium Notes S6. Maxwell et al 2005. A 100 microM stock of T. thermophilus S6, obtained as previously described (Miller et al., 2002), was diluted into buffered GuHCl solutions under the conditions listed using a Biologic SFM-4, and fluorescence emission at 350 nm using 280 nm excitation was recorded using a Jobin-Yvon Horiba Fluoromax 3. Data below 2.02 M GuHCl were fit to a double exponential, and the major refolding phase was used to fit the chevron. Similar results have been observed for S6 previously (Otzen et al., 1999). All other points fit well to a single exponential equation. (EJM, SM)
Kinetic Notes S6. Maxwell et al 2005. A 100 microM stock of T. thermophilus S6, obtained as previously described (Miller et al., 2002), was diluted into buffered GuHCl solutions under the conditions listed using a Biologic SFM-4, and fluorescence emission at 350 nm using 280 nm excitation was recorded using a Jobin-Yvon Horiba Fluoromax 3. Data below 2.02 M GuHCl were fit to a double exponential, and the major refolding phase was used to fit the chevron. Similar results have been observed for S6 previously (Otzen et al., 1999). All other points fit well to a single exponential equation. (EJM, SM)
Comments view comments on this measurement

contact us to make corrections & updates to this data