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- PDB-1blb: CLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES L... -

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Basic information

Entry
Database: PDB / ID: 1blb
TitleCLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES LOSS OF SYMMETRY AND ORDERING OF SEQUENCE EXTENSIONS
ComponentsBETA B2-CRYSTALLIN
KeywordsEYE LENS PROTEIN
Function / homology
Function and homology information


structural constituent of eye lens / lens development in camera-type eye / visual perception / identical protein binding
Similarity search - Function
Crystallins / Gamma-B Crystallin; domain 1 / Beta/Gamma crystallin / Crystallins beta and gamma 'Greek key' motif profile. / Beta/gamma crystallins / Beta/gamma crystallin / Gamma-crystallin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / Resolution: 3.3 Å
AuthorsNalini, V. / Bax, B. / Driessen, H. / Moss, D.S. / Lindley, P.F. / Slingsby, C.
Citation
Journal: J.Mol.Biol. / Year: 1994
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: Journal: Acta Crystallogr.,Sect.B / Year: 1991
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: Journal: J.Mol.Biol. / Year: 1982
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
DepositionDec 22, 1993Processing site: BNL
Revision 1.0Dec 20, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 7, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: BETA B2-CRYSTALLIN
B: BETA B2-CRYSTALLIN
C: BETA B2-CRYSTALLIN
D: BETA B2-CRYSTALLIN


Theoretical massNumber of molelcules
Total (without water)92,7904
Polymers92,7904
Non-polymers00
Water0
1
A: BETA B2-CRYSTALLIN
B: BETA B2-CRYSTALLIN

A: BETA B2-CRYSTALLIN
B: BETA B2-CRYSTALLIN


Theoretical massNumber of molelcules
Total (without water)92,7904
Polymers92,7904
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_555-x,y,-z1
2
C: BETA B2-CRYSTALLIN
D: BETA B2-CRYSTALLIN

C: BETA B2-CRYSTALLIN
D: BETA B2-CRYSTALLIN


Theoretical massNumber of molelcules
Total (without water)92,7904
Polymers92,7904
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_556x,-y,-z+11
Unit cell
Length a, b, c (Å)154.710, 165.900, 78.480
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number21
Space group name H-MC222
Atom site foot note1: 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
BETA B2-CRYSTALLIN


Mass: 23197.621 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Tissue: LENS / References: UniProt: P02522
Sequence detailsTHE 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). SUBSEQUENTLY, SOME CORRECTIONS WERE PUBLISHED BASED ON THE NUCLEOTIDE SEQUENCE. THE SEQUENCE PRESENTED IN THIS ENTRY IS FROM D. HOGG, ET AL. (1987). NUCLEOTIDE SEQUENCE FOR THE CDNA OF THE BOVINE BETAB2 CRYSTALLIN AND ASSIGNMENT OF THE ORTHOLOGOUS HUMAN LOCUS TO CHROMOSOME 22, CURRENT EYE RESEARCH, VOLUME 6, PAGES 1335 - 1342.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.71 Å3/Da / Density % sol: 54.64 %
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
IDConc.Common nameCrystal-IDSol-ID
14 %(w/w)protein1drop
20.05 MTris-acetate1drop
30.02 %(w/v)sodium azide1drop
41 mMdithiothreitol1drop
535 %(w/v)MPD1reservoir
60.05 MTris-acetate1reservoir

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

Software
NameClassification
X-PLORmodel building
RESTRAINrefinement
X-PLORrefinement
X-PLORphasing
RefinementHighest resolution: 3.3 Å
Refinement stepCycle: LAST / Highest resolution: 3.3 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5941 0 0 0 5941
Refinement
*PLUS
Highest resolution: 2.6 Å / Rfactor obs: 0.205
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.013
X-RAY DIFFRACTIONo_angle_deg3.1

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