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Open data
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Basic information
Entry | Database: PDB / ID: 1cx7 | ||||||
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Title | T4 LYSOZYME METHIONINE CORE MUTANT | ||||||
![]() | LYSOZYME | ||||||
![]() | HYDROLASE / HYDROLASE (O-GLYCOSYL) / T4 LYSOZYME / METHIONINE CORE MUTANT / PROTEIN ENGINEERING / PROTEIN 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 | ![]() | ||||||
![]() | Gassner, N.C. / Baase, W.A. / Lindstrom, J. / Lu, J. / Matthews, B.W. | ||||||
![]() | ![]() Title: Use of differentially substituted selenomethionine proteins in X-ray structure determination. Authors: Gassner, N.C. / Matthews, B.W. #1: ![]() Title: A Test of the "Jigsaw-Puzzle" Model for Protein Folding by Multiple Methionine substitutions within the core of T4 lysozyme Authors: Gassner, N.C. / Baase, W.A. / Matthews, B.W. #2: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 A Resolution Authors: Weaver, L.H. / Matthews, B.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 47.5 KB | Display | ![]() |
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PDB format | ![]() | 33.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 409.2 KB | Display | ![]() |
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Full document | ![]() | 415.5 KB | Display | |
Data in XML | ![]() | 6.8 KB | Display | |
Data in CIF | ![]() | 9.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1d2wC ![]() 1d2yC ![]() 1d3fC ![]() 1d3jC ![]() 1d3mC ![]() 1d3nC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 18720.611 Da / Num. of mol.: 1 Mutation: C54T, L84M, L91M, C97A, L99M, L118M, L121M, L133M, F153M Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-HED / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.01 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: Na2PO4, NaCl, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / Details: Eriksson, A.E., (1993) J.Mol.Biol., 229, 747. / PH range low: 7.1 / PH range high: 6.3 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Detector: AREA DETECTOR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.63→30 Å / Num. all: 23194 / Num. obs: 23194 / % possible obs: 85.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.1 % / Biso Wilson estimate: 25.5 Å2 / Rmerge(I) obs: 0.044 / Net I/σ(I): 2.4 |
Reflection shell | Resolution: 1.63→1.7 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.31 / Num. unique all: 3092 / % possible all: 58.1 |
Reflection | *PLUS Highest resolution: 1.9 Å |
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Processing
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Refinement | Resolution: 1.94→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: TNT PROTGEO
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Refinement step | Cycle: LAST / Resolution: 1.94→30 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5E / Classification: refinement | ||||||||||||
Refinement | *PLUS σ(F): 0 / Rfactor all: 0.152 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS Type: t_angle_deg / Dev ideal: 3 |