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

Expand   Protein Data
Protein Name Lambda C1 repressor, DNA-binding domain (Lambda Repressor)
Oligomeric State Monomer
Folding Mechanism Framework
Intermediates 0
Phi Pattern Barnase
SCOP Class Alpha   |   goto SCOP
SCOP Family Phage Repressor   |   goto SCOP

Expand   Construct Data
Species lambda phage (Enterobacteria phage lambda)

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Sequence PLTQEQLEDARRLKAIWEKKKNELGLSQESVADKMGMGQSGVGALFNGIN
ALNAYNAALLAKILKVSVEEFSPSIAREIYE

Blast PFD  |  Blast NCBI NR
Length 82
Molecular Weight 8875.17Da
Fusion None
PDB ID 1LMB   |   goto PDB  
PDB Resolution 1.8Å
Chain Any chain
Residues 6 - 85
SCOP ID 47421   |   goto SCOP
UniProt ID RPC1_LAMBD   |   goto UniProt
Relative Contact Order 11.46

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 17
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)
3.21 ± 0.19 10.38 ± 0.28 2.86 ± 0.16 -7.34 ± 0.52
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 -10.1 ± 0.4 21.2 ± 1.9
Probe Far-UV Circular Dichroism  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Jasco J-715 Spectrophotometer
Temperature 298K
pH 8
Buffer 0.02M 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)
1.9 3.48 24.78 ± 0.45 (0M) 3.21 ± 0.19 (0M) ND 2.86 ± 0.16
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)
1.15 1.9 32208.96 ± 1270.86 10.38 ± 0.28 ND -7.34 ± 0.52
Probe Trp Fluorescence  what is this?
Pertubation Denaturant  what is this?
Technique GdnHCl
Instrument Bio-Logic SFM-3 Stopped-flow Fluorometer  what is this?
Temperature 298K
pH 8
Buffer 0.02M Phosphate
Protein Concentration ND
Unfolding Fit Linear
Refolding Fit Linear

Expand   Notes & Comments on this measurement
Measurement Notes
Protein Notes The dimerization helix is truncated at residue 85, and the N-terminal arm (residues 1 to 5) is deleted. The structure of lambda6-85, determined by NMR methods, is identical to that found for these residues in the crystal structure of the N-terminal domain. However, this protein is not expected to be active because both the dimerization helix and N-terminal arm are necessary for tight specific DNA binding.
Construct Notes Problems calculating CO using PDB file 1LMB.
Equilibrium Notes Lambda repressor and protein G. Maxwell et al 2005. These proteins were expressed, purified and characterized as previously described (Krantz et al., 2002) save under the conditions described. The pH employed for lambda-repressor was raised slightly to improve its fluorescence properties. (TRS) Krantz et al 2002. Equilibrium. CD was used to monitored changes in stability at wavelengths from 222-228 nm (5 nm) using a Jasco 715 at concentrations of 2-10 muM.
Kinetic Notes Lambda Repressor and Protein G. Maxwell et al 2005. These proteins were expressed, purified and characterized as previously described (Krantz et al., 2002) save under the conditions described. The pH employed for lambda-repressor was raised slightly to improve its fluorescence properties. (TRS) Krantz et al 2002. Kinetics. Experiments used a Biologic stopped-flow at concentrations of 0.1-10 microM.
Comments view comments on this measurement

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