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- PDB-1llh: ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1llh | |||||||||
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Title | ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS | |||||||||
![]() | Lysozyme![]() | |||||||||
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Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Sagermann, M. / Martensson, L.-G. / Baase, W.A. / Matthews, B.W. | |||||||||
![]() | ![]() Title: A test of proposed rules for helix capping: Implications for protein design Authors: Sagermann, M. / Martensson, L.-G. / Baase, W.A. / Matthews, B.W. #1: Journal: Science / Year: 1994 Title: Rules for alpha-helix termination by glycine. Authors: Aurora, R. / Srinivasan, R. / Rose, G.D. #2: ![]() Title: The alpha-L Conformations at the Ends of Helices Authors: Schellman, C. #3: ![]() 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 | ![]() | 46.8 KB | Display | ![]() |
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PDB format | ![]() | 32.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1jquC ![]() 2lzmS C: citing same article ( S: Starting model for refinement |
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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: 18640.418 Da / Num. of mol.: 1 / Mutation: C54T, C97A, T157I Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ![]() #3: Chemical | ChemComp-BME / | ![]() #4: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.12 % |
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Crystal grow![]() | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: 1.8M Phosphate, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Ambient pressure: 101 kPa / Mean temperature: 298 K |
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Diffraction source | Source: rotating-anode X-ray tube / Type: RIGAKU RU200 / Wavelength: 1.5418 Å / Target: Cu |
Detector | Type: AREA DETECTOR / Detector: AREA DETECTOR / Date: Feb 15, 1995 / Details: Xuong-Hamlin |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray / Wavelength: 1.5418 Å |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.8→26.44 Å / Num. all: 17775 / Num. obs: 17775 / % possible obs: 81 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.37 % / Biso Wilson estimate: 16.36 Å2 / Rsym value: 0.04 / Net I/σ(I): 10.76 |
Reflection shell | Resolution: 1.8→1.94 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.215 / Mean I/σ(I) obs: 1.9 / Num. unique all: 3101 / % possible all: 81 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: PDB entry 2LZM Resolution: 1.8→27 Å / Isotropic thermal model: ANISOTROPIC / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: Residues 163 and 164 are missing in the electron density.
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.8→27 Å
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Refine LS restraints |
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