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- PDB-1blb: CLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES L... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1blb | ||||||
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Title | CLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES LOSS OF SYMMETRY AND ORDERING OF SEQUENCE EXTENSIONS | ||||||
![]() | BETA B2-CRYSTALLIN | ||||||
![]() | EYE LENS PROTEIN | ||||||
Function / homology | ![]() structural constituent of eye lens / lens development in camera-type eye / visual perception Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Nalini, V. / Bax, B. / Driessen, H. / Moss, D.S. / Lindley, P.F. / Slingsby, C. | ||||||
![]() | ![]() Title: Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions. Authors: Nalini, V. / Bax, B. / Driessen, H. / Moss, D.S. / Lindley, P.F. / Slingsby, C. #1: ![]() Title: Structure of Oligomeric Betab2-Crystallin: An Application of the T2 Translation Function to an Asymmetric Unit Containing Two Dimers Authors: Driessen, H.P.C. / Bax, B. / Slingsby, C. / Lindley, P.F. / Mahadevan, D. / Moss, D.S. / Tickle, I. #2: ![]() Title: Preliminary X-Ray Crystallographic Study of the Principle Subunit of the Lens Structural Protein, Bovine Beta-Crystallin Authors: Slingsby, C. / Miller, L.R. / Berbers, G.A.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 138 KB | Display | ![]() |
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PDB format | ![]() | 106.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 401.8 KB | Display | ![]() |
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Full document | ![]() | 520.2 KB | Display | |
Data in XML | ![]() | 31.7 KB | Display | |
Data in CIF | ![]() | 45 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 41 / 2: CIS PROLINE - PRO B 41 / 3: CIS PROLINE - PRO C 41 / 4: CIS PROLINE - PRO D 41 |
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Components
#1: Protein | Mass: 23197.621 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Sequence details | THE SEQUENCE PRESENTED IN THIS ENTRY DIFFERS FROM THAT OF SWISS-PROT ENTRY CRB2_BOVINE WHICH WAS ...THE SEQUENCE PRESENTED IN THIS ENTRY DIFFERS FROM THAT OF SWISS-PROT ENTRY CRB2_BOVINE WHICH WAS BASED ON THE AUTHOR'S PREVIOUS WORK (H.P.C. DRIESSEN ET AL. (1981). EUR. J. BIOCHEM. VOLUME 121, PAGES 83 - 91). SUBSEQUENT | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.64 % | |||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 54 % | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 5 ℃ / Method: vapor diffusion, hanging drop / PH range low: 7.2 / PH range high: 6.8 | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
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Refinement | Highest resolution: 3.3 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 3.3 Å
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Refinement | *PLUS Highest resolution: 2.6 Å / Rfactor obs: 0.205 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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