[English] 日本語
Yorodumi
- PDB-1elp: GAMMA-D CRYSTALLIN STRUCTURE AT 1.95 A RESOLUTION -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1elp
TitleGAMMA-D CRYSTALLIN STRUCTURE AT 1.95 A RESOLUTION
ComponentsGAMMA-D CRYSTALLIN
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 / 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 / SYNCHROTRON / Resolution: 1.95 Å
AuthorsChirgadze, Yu.N. / Driessen, H.P.C. / Wright, G. / Slingsby, C. / Hay, R.E. / Lindley, P.F.
Citation
Journal: Acta Crystallogr.,Sect.D / Year: 1996
Title: Structure of bovine eye lens gammaD (gammaIIIb)-crystallin at 1.95 A.
Authors: Chirgadze, Y.N. / Driessen, H.P. / Wright, G. / Slingsby, C. / Hay, R.E. / Lindley, P.F.
#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: Chirgadze, Yu. / Nevskaya, N. / Vernoslova, E. / Nikonov, S. / Sergeev, Yu. / Brazhnikov, E. / Fomenkova, N. / Lunin, V. / Urzhumtsev, A.
#2: Journal: Proteins / Year: 1988
Title: Surface Interactions of Gamma-Crystallins in the Crystal Medium in Relation to Their Association in the Eye Lens
Authors: Sergeev, Y.V. / Chirgadze, Y.N. / Mylvaganam, S.E. / Driessen, H. / Slingsby, C. / Blundell, T.L.
#3: Journal: Mol.Biol.(Moscow) / Year: 1987
Title: [the Key Role of the Residue 103 in the Surface Interactions of Gamma-Crystallins]
Authors: Sergeev, Iu.V. / Chirgadze, Iu.N. / Driessen, H. / Slingsby, C. / Blundell, T.L.
#4: Journal: Mol.Biol.(Engl.Transl.) / Year: 1987
Title: Key Role of Residue 103 in Surface Interactions of Gamma-Crystallins
Authors: Sergeev, Yu.V. / Chirgadze, Yu.N. / Driessen, H. / Slingsby, C. / Blundell, T.L.
#5: Journal: Dokl.Akad.Nauk Sssr / Year: 1986
Title: Spatial Structure of Gamma-Crystallin Iiib from Calf Eye Lens at 2.5 Angstroms Resolution
Authors: Chirgadze, Yu.N. / Nevskaya, N.A. / Fomenkova, N.P. / Nikonov, S.V. / Sergeev, Yu.V. / Brazhnikov, E.V. / Garber, M.B. / Lunin, V.Yu. / Urzumtsev, A.P. / Vernoslova, E.A.
#6: Journal: Acta Crystallogr.,Sect.A / Year: 1985
Title: Phase Improvement in Protein Crystallography Using a Mixed Electron Density Model
Authors: Lunin, V.Yu. / Urzhumtsev, A.G. / Vernoslova, E.A. / Chirgadze, Yu.N. / Nevskaya, N.A. / Fomenkova, N.P.
#7: Journal: Acta Crystallogr.,Sect.A / Year: 1984
Title: Improvement of Protein Phases by Coarse Model Modification
Authors: Lunin, V.Yu. / Urzhumtsev, A.G.
#8: Journal: Dokl.Akad.Nauk Sssr / Year: 1981
Title: Structure of Gamma-Crystallin Iiib from the Eye Lens of the Calf at 3 Angstroms Resolution
Authors: Chirgadze, Yu.N. / Sergeev, Yu.V. / Fomenkova, N.P. / Oreshin, V.D. / Nikonov, S.V.
#9: Journal: FEBS Lett. / Year: 1981
Title: Polypeptide Chain Pathway in Gamma-Crystallin Iiib from Calf Lens at 3 A Resolution
Authors: Chirgadze, Yu.N. / Sergeev, Yu.V. / Fomenkova, N.P. / Oreshin, V.D.
#10: Journal: FEBS Lett. / Year: 1980
Title: Structure of Gamma-Crystallin Iiib from Calf Lens at 5 A Resolution
Authors: Chirgadze, Y.N. / Oreshin, V.D. / Sergeev, Y.V. / Nikonov, S.V. / Lunin, V.Y.
#11: Journal: J.Mol.Biol. / Year: 1977
Title: Crystallographic Study of Gamma-Crystallins from Calf Lens
Authors: Chirgadze, Y.N. / Nikonov, S.V. / Garber, M.B. / Reshetnikova, L.S.
#12: Journal: Dokl.Akad.Nauk Sssr / Year: 1976
Title: Growing Single Crystals of Gamma Crystallin from the Calf Crystalline Lens
Authors: Garber, M.B. / Reshetnikova, L.S.
History
DepositionDec 20, 1995Processing site: BNL
Revision 1.0Jun 10, 1996Provider: 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: GAMMA-D CRYSTALLIN
B: GAMMA-D CRYSTALLIN


Theoretical massNumber of molelcules
Total (without water)41,5562
Polymers41,5562
Non-polymers00
Water3,927218
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)57.810, 70.030, 117.250
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein GAMMA-D CRYSTALLIN


Mass: 20778.236 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Organ: EYE / Tissue: EYE LENSLens (anatomy) / References: UniProt: P08209
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 218 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 2.85 Å3/Da / Density % sol: 56.91 %
Crystal
*PLUS
Density % sol: 57 %
Crystal grow
*PLUS
Temperature: 5 ℃ / pH: 7 / Method: unknown
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
11 %protein11
21 mMdithiothreitol11

-
Data collection

DiffractionMean temperature: 277 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX9.5 / Wavelength: 0.92
DetectorType: MARRESEARCH / Detector: IMAGE PLATE
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionNum. obs: 33667 / % possible obs: 95.2 % / Observed criterion σ(I): 3 / Redundancy: 4.3 % / Rmerge(I) obs: 0.081
Reflection
*PLUS
Highest resolution: 1.95 Å / Num. measured all: 144932

-
Processing

Software
NameClassification
RESTRAINrefinement
DENZOdata reduction
RefinementResolution: 1.95→8 Å / σ(F): 0
RfactorNum. reflection% reflection
Rwork0.204 --
obs-33104 95.2 %
Refinement stepCycle: LAST / Resolution: 1.95→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2928 0 0 219 3147
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.014
X-RAY DIFFRACTIONo_bond_d_na
X-RAY DIFFRACTIONo_bond_d_prot
X-RAY DIFFRACTIONo_angle_d
X-RAY DIFFRACTIONo_angle_d_na
X-RAY DIFFRACTIONo_angle_d_prot
X-RAY DIFFRACTIONo_angle_deg2.924
X-RAY DIFFRACTIONo_angle_deg_na
X-RAY DIFFRACTIONo_angle_deg_prot
X-RAY DIFFRACTIONo_dihedral_angle_d
X-RAY DIFFRACTIONo_dihedral_angle_d_na
X-RAY DIFFRACTIONo_dihedral_angle_d_prot
X-RAY DIFFRACTIONo_improper_angle_d
X-RAY DIFFRACTIONo_improper_angle_d_na
X-RAY DIFFRACTIONo_improper_angle_d_prot
X-RAY DIFFRACTIONo_mcbond_it
X-RAY DIFFRACTIONo_mcangle_it
X-RAY DIFFRACTIONo_scbond_it
X-RAY DIFFRACTIONo_scangle_it
Software
*PLUS
Name: RESTRAIN / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.204
Solvent computation
*PLUS
Displacement parameters
*PLUS

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more