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

Expand   Protein Data
Protein Name c-src tyrosine kinase SH2 domain (SrcSH2)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates
Phi Pattern No phi value analysis
SCOP Class Alpha+Beta   |   goto SCOP
SCOP Family SH2 domain   |   goto SCOP

Expand   Construct Data
Species Rous sarcoma virus (Rous sarcoma virus)

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Sequence GAQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDF
DNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRL
TNVCPTSKPQ

Blast PFD  |  Blast NCBI NR
Length 112
Molecular Weight 12503.1Da
Fusion None
PDB ID 1SPR   |   goto PDB  
PDB Resolution 2.5Å
Chain A
Residues 2 - 104
SCOP ID 69782   |   goto SCOP
UniProt ID SRC_RSVSA   |   goto UniProt
Relative Contact Order 10.63

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 26
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)
-3.48 ± 0.29 8.74 ± 0.21 0.89 ± 0.09 -4.25 ± 0.12
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 -5.6 ± 0.1 31 ± 0.4
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Bio-Logic SFM4/QFM4 Stopped-flow Fluorometer  what is this?
Temperature 298K
pH 7
Buffer 0.02M Imidazole
Protein Concentration NDM

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)
6.88 9.28 0.0308 ± 0.0013 (0M) -3.48 ± 0.29 (0M) ND 0.89 ± 0.09
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)
3.49 6.48 6247.9 ± 138.27 8.74 ± 0.21 ND -4.25 ± 0.12
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Bio-Logic SFM4/QFM4 Stopped-flow Fluorometer  what is this?
Temperature 298K
pH 7
Buffer 0.02M Imidazole
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes
Construct Notes
Equilibrium Notes 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 SrcSH2. 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)
Comments view comments on this measurement

contact us to make corrections & updates to this data