+
Open data
-
Basic information
Entry | Database: PDB / ID: 137l | ||||||
---|---|---|---|---|---|---|---|
Title | STRUCTURAL BASIS OF AMINO ACID ALPHA HELIX PROPENSITY | ||||||
![]() | T4 LYSOZYME | ||||||
![]() | HYDROLASE(O-GLYCOSYL) | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Blaber, M. / Matthews, B.W. | ||||||
![]() | ![]() Title: Structural basis of amino acid alpha helix propensity. Authors: Blaber, M. / Zhang, X.J. / Matthews, B.W. #1: ![]() Title: Control of Enzyme Activity by an Engineered Disulfide Bond Authors: Matsumura, M. / Matthews, B.W. #2: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution Authors: Weaver, L.H. / Matthews, B.W. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 79.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 61 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 107lC ![]() 108lC ![]() 109lC ![]() 110lC ![]() 111lC ![]() 112lC ![]() 113lC ![]() 114lC ![]() 115lC ![]() 216lC ![]() 217lC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 18688.459 Da / Num. of mol.: 2 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: 2.35 Å3/Da / Density % sol: 47.72 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow![]() | *PLUS Method: unknown / pH: 6.7 Details: S. Dao-pin, (1990) Proteins Struct. Funct. Gen., 7, 198. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
-
Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.85→6 Å / σ(F): 2 Details: MUTANT SPACE GROUP, P2(1), IS NON-ISOMORPHOUS TO WILD TYPE P3(2)21. THERE ARE TWO MOLECULES IN THE ASYMMETRIC UNIT, AND THE POSITION OF EACH OF THESE WAS SOLVED BY A SIX-DIMENSIONAL SEARCH ...Details: MUTANT SPACE GROUP, P2(1), IS NON-ISOMORPHOUS TO WILD TYPE P3(2)21. THERE ARE TWO MOLECULES IN THE ASYMMETRIC UNIT, AND THE POSITION OF EACH OF THESE WAS SOLVED BY A SIX-DIMENSIONAL SEARCH USING THE WILD TYPE COORDINATES. RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE. THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE. IN THIS ENTRY CHAIN A DOES NOT INCLUDE RESIDUES 163 AND 164 AND CHAIN B DOES INCLUDE THEM.
| ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.85→6 Å
| ||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||
Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.15 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_d / Dev ideal: 1.9 |