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

Expand   Protein Data
Protein Name Activation Domain Of Human Procarboxypeptidase A2 (ADAh2)
Oligomeric State Monomer
Folding Mechanism Not characterised
Intermediates 0
Phi Pattern No phi value analysis
SCOP Class Alpha+Beta   |   goto SCOP
SCOP Family Pancreatic carboxypeptidase, activation domain   |   goto SCOP

Expand   Construct Data
Species Human (Homo sapiens)

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Sequence MRSLETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETA
HVRVPFVNVQAVKVFLESQGIAYSIMIEDV

Blast PFD  |  Blast NCBI NR
Length 81
Molecular Weight 9064.34Da
Fusion None
PDB ID 1O6X   |   goto PDB  
PDB Resolution NMR
Chain Any chain
Residues 1 - 81
SCOP ID 54902   |   goto SCOP
UniProt ID CBPA2_HUMAN   |   goto UniProt
Relative Contact Order 14.32

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 4
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)
-0.42 ± 0.18 6.8 ± 0.12 1.12 ± 0.05 -3.12 ± 0.13
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 -3.9 ± 0.1 17.1 ± 0.4
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Aminco Bowman Series 2 Luminescence Spectrometer
Temperature 298K
pH 7
Buffer 0.05M Phosphate
Protein Concentration 0.0022M

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)
5.25 9.2 0.66 ± 0.01 (0M) -0.42 ± 0.18 (0M) ND 1.12 ± 0.05
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)
0.92 4.6 897.85 ± 6.47 6.8 ± 0.12 ND -3.12 ± 0.13
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique Urea
Instrument Bio-Logic SFM-3 Stopped-flow Fluorometer  what is this?
Temperature 298K
pH 7.5
Buffer 0.05M Phosphate
Protein Concentration 0.0022M
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2.
Construct Notes
Equilibrium Notes (From Villegas et al 1998): The experiments were performed at 25degC in 50 mM sodium phosphate (pH 7.0) and the suitable concentration of urea. Fluorescence emission spectra of Trp40 of ADA2h was used to monitor any changes in the environment of this residue upon the unfolding of the protein. Fluorescence was measured in an Aminco Bowman Series 2 luminescence spectrometer. Excitation was at 290 nm with a 2 nm slit. Fluorescence was detected through an 8 nm slit at 315 nm.
Kinetic Notes (From Villegas et al 1998): The experiments were performed at 25 degC in 50 mM sodium phosphate (pH 7.0) and the suitable concentration of urea. Kinetics were followed in a Bio-Logic stopped-flow machine (SFM-3) by fluorescence. The average dead time of the experiments was 50 ms due to artifacts arising from mixing water and high urea concentrations. A cell of 150 microl and an aging loop of 10 microl were used. The unfolding process was promoted by dilution of the native ADA2h in a 50 mM sodium phosphate buffer (pH 7.0) with the appropriate ratio of the same buffer containing different concentrations of urea. For the refolding reaction, the unfolded domain in the 50 mM sodium phosphate buffer (pH 7.0), containing 9.5 M urea, was mixed with an excess of the same buffer without urea to give several final urea concentrations. Fluorescence was measured through a 320 nm cutoff filter (excitation at 290 nm). The cell chamber and the syringes were kept at 298 K. The logarithm of the rate constants for the unfolding (ln kf) and the refolding reactions (ln ku) versus urea concentration can be fitted to a linear equation, outside the transition region. The rate constants in the transition region between the linear equations concerning both the unfolding and the refolding reactions were indistinguishable.
Comments view comments on this measurement

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