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- PDB-1egs: NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETI... -

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Basic information

Entry
Database: PDB / ID: 1egs
TitleNMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES
ComponentsGROES
KeywordsCHAPERONIN / PROTEIN FOLDING / HEAT SHOCK
Function / homology
Function and homology information


GroEL-GroES complex / virion assembly / : / protein folding chaperone / unfolded protein binding / protein folding / protein-folding chaperone binding / response to heat / ATP binding / metal ion binding ...GroEL-GroES complex / virion assembly / : / protein folding chaperone / unfolded protein binding / protein folding / protein-folding chaperone binding / response to heat / ATP binding / metal ion binding / identical protein binding / cytosol
Similarity search - Function
Chaperonin GroES, conserved site / Chaperonins cpn10 signature. / Chaperonin 10 Kd subunit / GroES chaperonin family / GroES chaperonin superfamily / Chaperonin 10 Kd subunit / GroES-like superfamily
Similarity search - Domain/homology
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / MOLECULAR DYNAMICS, SIMULATED ANNEALING
AuthorsLandry, S.J.
Citation
Journal: Proc.Natl.Acad.Sci.USA / Year: 1996
Title: Interplay of structure and disorder in cochaperonin mobile loops.
Authors: Landry, S.J. / Taher, A. / Georgopoulos, C. / van der Vies, S.M.
#1: Journal: Nature / Year: 1993
Title: Characterization of a Functionally Important Mobile Domain of Groes
Authors: Landry, S.J. / Zeilstra-Ryalls, J. / Fayet, O. / Georgopoulos, C. / Gierasch, L.M.
History
DepositionJun 30, 1997Processing site: BNL
Revision 1.0Sep 17, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Oct 23, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GROES


Theoretical massNumber of molelcules
Total (without water)8701
Polymers8701
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 20
Representative

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Components

#1: Protein/peptide GROES / 10 KD CHAPERONIN / PROTEIN CPN10


Mass: 870.050 Da / Num. of mol.: 1 / Fragment: MOBILE LOOP
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0A6F9
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY

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Sample preparation

Sample conditionspH: 6.5 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian VXR500 / Manufacturer: Varian / Model: VXR500 / Field strength: 500 MHz

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Processing

NMR software
NameDeveloperClassification
DiscoverBIOSYMrefinement
Discoverstructure solution
RefinementMethod: MOLECULAR DYNAMICS, SIMULATED ANNEALING / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformers calculated total number: 20 / Conformers submitted total number: 20

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