+
Open data
-
Basic information
Entry | Database: PDB / ID: 1d2w | ||||||
---|---|---|---|---|---|---|---|
Title | N-TERMINAL DOMAIN CORE METHIONINE MUTATION | ||||||
![]() | 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. / Matthews, B.W. | ||||||
![]() | ![]() Title: Use of differentially substituted selenomethionine proteins in X-ray structure determination. Authors: Gassner, N.C. / Matthews, B.W. #1: ![]() Title: Methionine and Alanine Substitutions Show that the Formation of Wild-type-like Structure in the Carboxy-terminal Domain of T4 Lysozyme is a Rate-Limiting Step in Folding Authors: Gassner, N.C. / Baase, W.A. / Lindstrom, J.D. / Lu, J. / Dahlquist, F.W. / Matthews, B.W. #2: ![]() 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. #3: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 A Resolution Authors: Weaver, L.H. / Matthews, B.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 48.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 34.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 429.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 432.5 KB | Display | |
Data in XML | ![]() | 10.3 KB | Display | |
Data in CIF | ![]() | 14.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1cx7C ![]() 1d2yC ![]() 1d3fC ![]() 1d3jC ![]() 1d3mC ![]() 1d3nC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 18646.400 Da / Num. of mol.: 1 / Mutation: I27M, C54T, C97A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
---|---|---|---|---|---|
#2: Chemical | #3: Chemical | ChemComp-HED / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.05 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.9 Details: NA2PO4, NACL, pH 6.9, 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
|
-Data collection
Diffraction | Mean temperature: 298 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: SDMS / 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: 1.81→30 Å / Num. all: 17155 / Num. obs: 17155 / % possible obs: 87 % / Redundancy: 2.7 % / Biso Wilson estimate: 22.6 Å2 / Rmerge(I) obs: 0.088 / Net I/σ(I): 1.5 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 1.5 % / Rmerge(I) obs: 0.281 / % possible all: 50 |
Reflection | *PLUS Highest resolution: 1.81 Å |
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.89→30 Å / Stereochemistry target values: TNT PROTGEO
| ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.89→30 Å
| ||||||||||||
Refine LS restraints |
| ||||||||||||
Software | *PLUS Name: TNT / Version: 5E / Classification: refinement | ||||||||||||
Refinement | *PLUS Rfactor all: 0.157 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
|