+
Open data
-
Basic information
Entry | Database: PDB / ID: 1p5c | ||||||
---|---|---|---|---|---|---|---|
Title | Circular permutation of Helix A in T4 lysozyme | ||||||
![]() | Lysozyme | ||||||
![]() | HYDROLASE / Circular permutation / protein design / context dependent folding | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / host cell cytoplasm / defense response to bacterium Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sagermann, M. / Gay, L. / Baase, W.A. / Matthews, B.W. | ||||||
![]() | ![]() Title: Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Authors: Sagermann, M. / Baase, W.A. / Mooers, B.H. / Gay, L. / Matthews, B.W. #1: ![]() Title: Crystal structures of a T4-lysozyme duplication-extension mutant demonstrates that the highly conserved beta-sheet region has low intrinsic folding propensity Authors: Sagermann, M. / Matthews, B.W. #2: ![]() Title: Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution Authors: Weaver, L.H. / Matthews, B.W. #3: ![]() Title: Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding Authors: Sagermann, M. / Baase, W.A. / Matthews, B.W. | ||||||
History |
| ||||||
Remark 999 | SEQUENCE Residue Leu 164 was deleted and sequence SGGAMNIFEMLRIDE was appended to the C-terminus |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 144.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 114.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 453.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 469.6 KB | Display | |
Data in XML | ![]() | 29.2 KB | Display | |
Data in CIF | ![]() | 40.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1p56C ![]() 2lzmS C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
4 | ![]()
| ||||||||
Unit cell |
| ||||||||
Details | Protein is a monomer in solution. The asymmetric unit contains 4 molecules. The refinement was performed in the absence of NCS operators. |
-
Components
#1: Protein | Mass: 18861.607 Da / Num. of mol.: 4 / Mutation: C54T, C97A, G12M Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.77 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.1 Details: 30% PEG 3400, 50mM Phosphate buffer, 5% isopropanol, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 170 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 7, 2002 / Details: mirror |
Radiation | Monochromator: single SI crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→25 Å / Num. all: 57195 / Num. obs: 22893 / % possible obs: 97.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Biso Wilson estimate: 35.11 Å2 / Rsym value: 0.076 / Net I/σ(I): 6.7 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 2.4 % / Num. unique all: 3389 / Rsym value: 0.088 / % possible all: 99.3 |
-
Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2LZM Resolution: 2.5→25 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: Amino terminal Methionine residue not visible in density.
| |||||||||||||||||||||||||
Displacement parameters |
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→25 Å
| |||||||||||||||||||||||||
Refine LS restraints |
|