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- PDB-1gcs: STRUCTURE OF THE BOVINE GAMMA-B CRYSTALLIN AT 150K -

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Basic information

Entry
Database: PDB / ID: 1gcs
TitleSTRUCTURE OF THE BOVINE GAMMA-B CRYSTALLIN AT 150K
ComponentsGAMMA-B CRYSTALLINCRYGB
KeywordsEYE LENS PROTEIN
Function / homology
Function and homology information


structural constituent of eye lens / lens development in camera-type eye / visual perception
Similarity search - Function
Crystallins / Beta/Gamma crystallin / Gamma-B Crystallin; domain 1 / 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: 2 Å
AuthorsNajmudin, S. / Lindley, P. / Slingsby, C. / Bateman, O. / Myles, D. / Kumaraswamy, S. / Glover, I.
Citation
Journal: J.CHEM.SOC.,FARADAY TRANS. / Year: 1993
Title: Structure of the Bovine Gamma-B Crystallin at 150K
Authors: Lindley, P.F. / Najmudin, S. / Bateman, O. / Slingsby, C. / Myles, D. / Kumaraswamy, S. / Glover, I.
#1: Journal: Acta Crystallogr.,Sect.D / Year: 1993
Title: Lindley Structure of Bovine Gamma-B (Gamma-II) Crystallin at 1.47 Angstroms Resolution
Authors: Najmudin, S. / Nalini, V. / Driessen, H.P.C. / Slingsby, C. / Blundell, T.L. / Moss, D.S. / Lindley, P.F.
#2: Journal: Pept.Protein Rev. / Year: 1984
Title: X-Ray Studies of the Lens Specific Proteins, the Crystallins
Authors: Summers, L. / Wistow, G. / Narebor, M. / Moss, D. / Lindley, P. / Slingsby, C. / Blundell, T. / Bartunik, H. / Bartels, K.
#3: Journal: J.Mol.Biol. / Year: 1983
Title: X-Ray Analysis of the Eye Lens Protein Gamma-II Crystallin at 1.9 Angstroms Resolution
Authors: Wistow, G. / Turnell, B. / Summers, L. / Slingsby, C. / Moss, D. / Miller, L. / Lindley, P. / Blundell, T.
#4: Journal: Nature / Year: 1981
Title: The Molecular Structure and Stability of the Eye Lens: X-Ray Analysis of Gamma Crystallin II
Authors: Blundell, T. / Lindley, P. / Miller, L. / Moss, D. / Slingsby, C. / Tickle, I. / Turnell, B. / Wistow, G.
History
DepositionJan 27, 1994Processing site: BNL
Revision 1.0Apr 30, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 3, 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
Remark 700SHEET IN *SHEET* RECORDS BELOW, THERE IS A POSSIBLE BETA-BRIDGE BETWEEN RESIDUES 119 - 121 AND 162 - 164.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GAMMA-B CRYSTALLIN


Theoretical massNumber of molelcules
Total (without water)20,9931
Polymers20,9931
Non-polymers00
Water4,594255
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)56.410, 56.410, 97.110
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Atom site foot note1: THE SIDE CHAINS OF CYS 18 AND CYS 22 ARE IN THE FULLY REDUCED STATE.

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Components

#1: Protein GAMMA-B CRYSTALLIN / CRYGB


Mass: 20992.559 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P02526
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 255 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 1.84 Å3/Da / Density % sol: 33.13 %
Crystal grow
*PLUS
Temperature: 0 K / pH: 7 / Method: unknown / Details: Carlisle, C.H.,(1977) J. Mol. Biol., 110, 417.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
170 mg/mlprotein11
20.05 Mphosphate12
31 mMdithiothreitol12

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Highest resolution: 1.95 Å / Num. all: 11407 / Num. obs: 10735 / Num. measured all: 36656 / Rmerge(I) obs: 0.052

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Processing

SoftwareName: RESTRAIN / Classification: refinement
RefinementResolution: 2→8 Å / σ(F): 0 /
RfactorNum. reflection% reflection
obs0.17 10365 96 %
Refinement stepCycle: LAST / Resolution: 2→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1474 0 0 255 1729
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d0.02
X-RAY DIFFRACTIONp_angle_d0.035
Refinement
*PLUS
Rfactor obs: 0.17
Solvent computation
*PLUS
Displacement parameters
*PLUS

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