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: 2] contact us to make corrections & updates to this data

Expand   Protein Data
Protein Name Internalin B, C-terminal domain (GW1)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Beta   |   goto SCOP
SCOP Family GW domain   |   goto SCOP

Expand   Construct Data
Species Listeria monocytogenes (Listeria monocytogenes)

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Sequence METTEKTVNLTRYVKYIRGNAGIYKLPREDNSLKQGTLASHRCKALTVDR
EARNGGKLWYRLKNIGWTKAENLSLDRLEHHHHHH

Blast PFD  |  Blast NCBI NR
Length 86
Molecular Weight 9959.32Da
Fusion C-terminal hexahistidine
PDB ID 1M9S   |   goto PDB  
PDB Resolution 2.65Å
Chain Any chain
Residues 391 - 466
SCOP ID 78875   |   goto SCOP
UniProt ID INLB_LISMO   |   goto UniProt
Relative Contact Order 16.16

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 2
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)
-1.66 ± 0.18 3.98 ± 0.17 4.63 ± 0.18 -10.12 ± 0.84
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 -13.9 ± 0.3 15.5 ± 0.3
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Aviv ATF 105 Spectrofluorometer
Temperature 298K
pH 7
Buffer 0.05M Phosphate
Additive 1: 0.1M NaCl
Additive 2: 0.0010M DTT
Protein Concentration 0.0010M

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)
1.3 3.4 0.1901 ± 0.0031 (0M) -1.66 ± 0.18 (0M) ND 4.63 ± 0.18
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)
0.2 1.2 53.52 ± 0.78 3.98 ± 0.17 ND -10.12 ± 0.84
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
Buffer 0.05M Phosphate
Additive 1: 0.1M NaCl
Additive 2: 0.0010M DTT
Protein Concentration 0.0030M
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes duplication: tandem repeat of three SH3-like GW domains
Construct Notes
Equilibrium Notes The protein was expressed in E. coli BL21* and purified under denaturing conditions (6M GdnHCl) using nickel affinity chromatography (Maxwell & Davidson, 1998). The purified proteins were subsequently folded through dialysis in 50mM phosphate buffer/100mM NaCl and used as such without cleaving the tag. Equilibrium melts were monitored using 1 uM protein on an Aviv Spectrofluorometer ATF 105 monitoring fluorescence emission at 340 nm with excitation at 295 nm.
Kinetic Notes GW1 was expressed in E. coli BL21* and purified under denaturing conditions (6M GuHCl) using nickel affinity chromatography (Maxwell & Davidson, 1998). The purified proteins were subsequently folded through dialysis in 50mM phosphate buffer/100mM NaCl and used as such without cleaving the tag. Folding and unfolding rates were obtained on a Bio-Logic SFM-4 stopped-flow fluorimeter, with excitation at 295 nm and detection of total fluorescence above 309 nm. Traces were fit to appropriate single exponentials. At each concentration of GuHCl, at least 5 separate shots of uM protein were averaged.
Comments view comments on this measurement

contact us to make corrections & updates to this data