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

Expand   Compare Data
compare with other measurements for proteins in this SCOP Family (4)

Expand   Protein Data
Protein Name Fyn proto-oncogene tyrosine kinase, SH3 domain (FynSH3)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Beta   |   goto SCOP
SCOP Family SH3 domain   |   goto SCOP

Expand   Construct Data
Species Human (Homo sapiens)

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Sequence MGSSHHHHHHSSGLVPRCSHMNKDEAGGNWKQFKGKVKEQWGKLTDDDMT
IIEGKRDQLVGKIQERYGYQKDQAEKEVVDWETRNEYRW

Blast PFD  |  Blast NCBI NR
Length 89
Molecular Weight 10516.6Da
Fusion N-terminal hexahistidine
PDB ID 1AVZ   |   goto PDB  
PDB Resolution 3Å
Chain C
Residues 85 - 141
SCOP ID 50049   |   goto SCOP
UniProt ID FYN_HUMAN   |   goto UniProt
Relative Contact Order 12.58

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 14
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)
-4.34 ± 0.37 4.88 ± 0.17 1.68 ± 0.17 -4.92 ± 0.21
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 -6.1 ± 0.4 20.3 ± 1.4
Probe Far-UV Circular Dichroism  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Aviv titrating Circular Di 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)
4.6 6.8 0.01304 ± 0.00090 (0M) -4.34 ± 0.37 (0M) ND 1.68 ± 0.17
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)
0.7 3.6 131.63 ± 1.91 4.88 ± 0.17 ND -4.92 ± 0.21
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
Buffer 0.05M Phosphate
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes The SH3 domain is a small ( ∼60 residue) protein module found in a large number of multidomain proteins, primarily those involved in cellular signaling (1). This module has been well characterized by both NMR and X-ray techniques and is a small B-barrel composed of two perpendicular B-sheets, lacking disulfide bonds and cis-proline residues. SH3-like barrel, partly opened; n*=4, S*=8; meander. The last strand is interrupted by a turn of 3-10 helix. SH3 domains have emerged in the last decade as intergal parts of many signal transduction and cytoskeletal proteins and have been shown to mediate a myriad of protein-protein interactions. Beside their biological importance as protein adapters, their ability to fold independently, modest size, and lack of disulfide bonds and bound cofactors make the SH3 domains an attractive model system for understanding the principles of protein folding at their simplest level. The abundance of both crystal and solution structures for many members of the SH3 family further facilitates detailed investigations of their folding. Except for some variability in the loop regions, all structures display the distinctive SH3 fold: two 3-stranded beta-sheets packed orthogonally against each other to form a single hydrophobic core. It has been suggested that the phi-pattern model is more like CI2 than barnase (Gruebele et al, Nat. Struct. Biol. 5, 662 (1998)
Construct Notes
Equilibrium Notes Protein L and FynSH3. Maxwell et al., 2005: Protein L and FynSH3 were expressed and purified as previously described (Scalley et al., 1997; Maxwell & Davidson, 1998) and employed without cleavage of the his-tag. Kinetics were monitored via tryptophan fluorescence (excitation 280 nm, emission >320 nm) on an APP stopped-flow fluorimeter. Equilibrium unfolding was monitored via CD at 220 nm on an Aviv titrating CD spectrometer with a 2 minute equilibration time. Buffer conditions were as described. Both proteins have previously been established to fold via an apparently two-state process (Scalley et al., 1997; Plaxco et al., 1998a). (MAR, KWP).
Kinetic Notes Protein L and FynSH3. Maxwell et al., 2005: Protein L and FynSH3 were expressed and purified as previously described (Scalley et al., 1997; Maxwell & Davidson, 1998) and employed without cleavage of the his-tag. Kinetics were monitored via tryptophan fluorescence (excitation 280 nm, emission >320 nm) on an APP stopped-flow fluorimeter. Equilibrium unfolding was monitored via CD at 220 nm on an Aviv titrating CD spectrometer with a 2 minute equilibration time. Buffer conditions were as described. Both proteins have previously been established to fold via an apparently two-state process (Scalley et al., 1997; Plaxco et al., 1998a). (MAR, KWP).
Comments view comments on this measurement

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