The Protein Folding Database
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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: 21] contact us to make corrections & updates to this data

Expand   Compare Data
compare with other measurements for proteins in this SCOP Family (1)

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

Expand   Construct Data
Species Streptococcus sp., group G (Streptococcus sp., group G)

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Sequence MTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATK
TFTVTEHHHHHH

Blast PFD  |  Blast NCBI NR
Length 64
Molecular Weight 7000.65Da
Fusion C-terminal hexahistidine
PDB ID 3GB1   |   goto PDB  
PDB Resolution NMR
Chain Any chain
Residues 1 - 56
SCOP ID 54361   |   goto SCOP
UniProt ID ND
Relative Contact Order 14.22

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 21
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)
-1.72 ± 0.17 6.3 ± 0.08 1.38 ± 0.12 -7.03 ± 0.15
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   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)
2.73 4.3 0.1791 ± 0.0026 (0M) -1.72 ± 0.17 (0M) ND 1.38 ± 0.12
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)
0.66 2.62 544.57 ± 1.74 6.3 ± 0.08 ND -7.03 ± 0.15
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Standard Stopped-Flow Spectrophotometer  what is this?
Temperature 298K
pH 7.5
Buffer 0.05M Hepes
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes
Construct Notes CO calculated using PDB entry file 3GB1 (B1 domain).
Kinetic Notes Lambda Repressor and Protein G. Maxwell et al 2005. These proteins were expressed, purified and characterized as previously described (Krantz et al., 2002) save under the conditions described. The pH employed for lambda-repressor was raised slightly to improve its fluorescence properties. (TRS)
Comments view comments on this measurement

contact us to make corrections & updates to this data