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- PDB-1cqu: SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9 -

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Entry
Database: PDB / ID: 1cqu
TitleSOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF RIBOSOMAL PROTEIN L9
Components50S RIBOSOMAL PROTEIN L9
KeywordsRIBOSOME / PROTEIN L9
Function / homology
Function and homology information


rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex
Similarity search - Function
Ribosomal protein L9, N-terminal domain / Ribosomal Protein L9; domain 1 / Ribosomal protein L9 signature. / Ribosomal protein L9, bacteria/chloroplast / Ribosomal protein L9, C-terminal / Ribosomal protein L9, C-terminal domain / Ribosomal protein L9, C-terminal domain superfamily / Ribosomal protein L9, N-terminal domain superfamily / Ribosomal protein L9 / Ribosomal protein L9, N-terminal ...Ribosomal protein L9, N-terminal domain / Ribosomal Protein L9; domain 1 / Ribosomal protein L9 signature. / Ribosomal protein L9, bacteria/chloroplast / Ribosomal protein L9, C-terminal / Ribosomal protein L9, C-terminal domain / Ribosomal protein L9, C-terminal domain superfamily / Ribosomal protein L9, N-terminal domain superfamily / Ribosomal protein L9 / Ribosomal protein L9, N-terminal / Ribosomal protein L9, N-terminal domain / Ribosomal protein L9/RNase H1, N-terminal / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Large ribosomal subunit protein bL9
Similarity search - Component
Biological speciesGeobacillus stearothermophilus (bacteria)
MethodSOLUTION NMR / DISTANCE GEOMETRY SIMULATED ANNEALING
AuthorsHua, Y. / Kuhlman, B. / Hoffman, D. / Raleigh, D.P.
Citation
Journal: J.Mol.Biol. / Year: 1999
Title: Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant ...Title: Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9.
Authors: Luisi, D.L. / Kuhlman, B. / Sideras, K. / Evans, P.A. / Raleigh, D.P.
#1: Journal: Eur.J.Biochem. / Year: 1994
Title: Crystal Structure of Prokaryotic Ribosomal Protein L9: A Bi-Lobed RNA-Binding Protein
Authors: Hoffman, D.W. / Cameron, C. / Davies, C. / Gerchman, S.E. / Kycia, J.H. / Porter, S. / Ramakrishnan, V. / White, S.W.
History
DepositionAug 11, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 27, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: 50S RIBOSOMAL PROTEIN L9


Theoretical massNumber of molelcules
Total (without water)6,2311
Polymers6,2311
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)18 / 50structures with the least restraint violations
Representative

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Components

#1: Protein 50S RIBOSOMAL PROTEIN L9


Mass: 6231.309 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN / Source method: isolated from a natural source / Source: (natural) Geobacillus stearothermophilus (bacteria) / References: UniProt: P02417

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D NOESY

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Sample preparation

Sample conditionspH: 5 / Pressure: AMBIENT / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.81BRUNGERstructure calculation
X-PLOR3.81BRUNGERrefinement
RefinementMethod: DISTANCE GEOMETRY SIMULATED ANNEALING / Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 50 / Conformers submitted total number: 18

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