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Open data
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Basic information
Entry | Database: PDB / ID: 1hk0 | ||||||
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Title | Human GammaD Crystallin Structure at 1.25 A Resolution | ||||||
![]() | Gamma-crystallin D | ||||||
![]() | EYE LENS PROTEIN / CATARACT | ||||||
Function / homology | ![]() lens fiber cell differentiation / structural constituent of eye lens / lens development in camera-type eye / visual perception / cellular response to reactive oxygen species / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Basak, A.K. / Slingsby, C. | ||||||
![]() | ![]() Title: High-Resolution X-Ray Crystal Structures of Human Gammad Crystallin (1.25A) and the R58H Mutant (1.15A) Associated with Aculeiform Cataract Authors: Basak, A.K. / Bateman, O. / Slingsby, C. / Pande, A. / Asherie, N. / Ogun, O. / Benedek, G. / Pande, J. #1: Journal: Exp.Eye Res. / Year: 1991 Title: Crystal Structure of Calf Eye Lens Gamma-Crystallin Iiib at 2.5 A Resolution: Its Relation to Function Authors: Yu, C. / Nevskaya, N. / Vernoslova, E. / Nikonov, S. / Yu, S. / Brazhnikov, E. / Fomenkova, N. / Lunin, V. / Urzhumtsev, A. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 95.9 KB | Display | ![]() |
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PDB format | ![]() | 72.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.7 KB | Display | ![]() |
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Full document | ![]() | 426.7 KB | Display | |
Data in XML | ![]() | 12 KB | Display | |
Data in CIF | ![]() | 18.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1h4aC ![]() 1elpS 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 20634.969 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.87 Å3/Da / Density % sol: 38 % | ||||||||||||||||||
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Crystal grow | Temperature: 277 K / pH: 7 / Details: 10MM PHOSPHATE, 4 DEGREE CELSIUS, pH 7.00 | ||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: batch method | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Apr 15, 2001 / Details: MIRROR |
Radiation | Monochromator: LAUE DIAMOND C111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→28.17 Å / Num. obs: 39066 / % possible obs: 86.8 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.048 / Net I/σ(I): 7.4 |
Reflection shell | Resolution: 1.25→1.32 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.189 / Mean I/σ(I) obs: 3.7 / % possible all: 45.5 |
Reflection | *PLUS Num. obs: 39021 / Num. measured all: 212732 |
Reflection shell | *PLUS % possible obs: 45.5 % / Redundancy: 1.9 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ELP Resolution: 1.25→28.17 Å / SU B: 0.877 / SU ML: 0.038 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.066 / ESU R Free: 0.062 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Displacement parameters | Biso mean: 13.5 Å2
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Refinement step | Cycle: LAST / Resolution: 1.25→28.17 Å
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Refinement | *PLUS % reflection Rfree: 8 % / Rfactor obs: 0.1671 / Rfactor Rfree: 0.2078 / Rfactor Rwork: 0.1636 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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