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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: 27] 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 c-src tyrosine kinase SH3 Domain (SrcSH3)
Oligomeric State Monomer
Folding Mechanism Nucleation-condensation
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Beta   |   goto SCOP
SCOP Family SH3 domain   |   goto SCOP

Expand   Construct Data
Species Chicken (Gallus gallus)

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Sequence GATTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGY
IPSNYVAPSDSL

Blast PFD  |  Blast NCBI NR
Length 64
Molecular Weight 6898.53Da
Fusion None
PDB ID 1RLQ   |   goto PDB  
PDB Resolution NMR
Chain Any chain
Residues 9 - 64
SCOP ID 50066   |   goto SCOP
UniProt ID SRC_CHICK   |   goto UniProt
Relative Contact Order 17.66

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 27
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)
-1.27 ± 0.13 4.36 ± 0.07 1.7 ± 0.07 -4.19 ± 0.16
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 -6.7 ± 0.8 15.9 ± 2.5
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
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)
2.92 5.47 0.2808 ± 0.0024 (0M) -1.27 ± 0.13 (0M) ND 1.7 ± 0.07
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 2.59 78.26 ± 0.19 4.36 ± 0.07 ND -4.19 ± 0.16
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
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes 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 (1998), Nat. Struct. Biol. 5, 662)).
Construct Notes
Equilibrium Notes SrcSH3. Maxwell et al 2005. SrcSH2 and SrcSH3. Both proteins were expressed with amino-terminal 6-his tags 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. The SH2 domain was characterized under the conditions described (Table 1), which included 1 mM tris carboxyethyl phosphine (TCEP) (Pierce), to prevent the intermolecular disulfide bond formation. The SH3 domain was characterized under standard consensus conditions (Table 1). Kinetics of both proteins were determined using a Biologic SFM 4 stopped-flow coupled to a Fluoromax 3 fluorimeter, with excitation at 290 nm and emission recorded between 310 and 330 nm. A slow, denaturant-independent refolding phase (kf = ~0.05 s-1) accounting for about 15% of the total amplitude of the SH2 domain folding was assumed to represent proline isomerization and ignored (data not shown). A slow phase (~0.02 s-1) observed in the folding of the srcSH3 domain and previously assigned (Grantcharov & Baker, 1997) to proline isomerization was also ignored. (DW, SM)
Kinetic Notes SrcSH3. Maxwell et al 2005. SrcSH2 and SrcSH3. Both proteins were expressed with amino-terminal 6-his tags 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. The SH2 domain was characterized under the conditions described (Table 1), which included 1 mM tris carboxyethyl phosphine (TCEP) (Pierce), to prevent the intermolecular disulfide bond formation. The SH3 domain was characterized under standard consensus conditions (Table 1). Kinetics of both proteins were determined using a Biologic SFM 4 stopped-flow coupled to a Fluoromax 3 fluorimeter, with excitation at 290 nm and emission recorded between 310 and 330 nm. A slow, denaturant-independent refolding phase (kf = ~0.05 s-1) accounting for about 15% of the total amplitude of the SH2 domain folding was assumed to represent proline isomerization and ignored (data not shown). A slow phase (~0.02 s-1) observed in the folding of the srcSH3 domain and previously assigned (Grantcharov & Baker, 1997) to proline isomerization was also ignored. (DW, SM)
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