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- PDB-1g6p: SOLUTION NMR STRUCTURE OF THE COLD SHOCK PROTEIN FROM THE HYPERTH... -

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Basic information

Entry
Database: PDB / ID: 1g6p
TitleSOLUTION NMR STRUCTURE OF THE COLD SHOCK PROTEIN FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA
ComponentsCOLD SHOCK PROTEIN TMCSP
KeywordsSTRUCTURAL GENOMICS / greek-key / beta barrel / OB-fold
Function / homology
Function and homology information


regulation of gene expression / nucleic acid binding / DNA binding / cytoplasm
Similarity search - Function
Cold shock, CspA / : / Cold-shock (CSD) domain / Cold-shock (CSD) domain signature. / Cold-shock protein, DNA-binding / 'Cold-shock' DNA-binding domain / Cold-shock (CSD) domain profile. / Cold shock domain / Cold shock protein domain / Nucleic acid-binding proteins ...Cold shock, CspA / : / Cold-shock (CSD) domain / Cold-shock (CSD) domain signature. / Cold-shock protein, DNA-binding / 'Cold-shock' DNA-binding domain / Cold-shock (CSD) domain profile. / Cold shock domain / Cold shock protein domain / Nucleic acid-binding proteins / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Nucleic acid-binding, OB-fold / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Cold shock-like protein
Similarity search - Component
Biological speciesThermotoga maritima (bacteria)
MethodSOLUTION NMR / dynamic simulated annealing protocol
AuthorsKremer, W. / Schuler, B. / Harrieder, S. / Geyer, M. / Gronwald, W. / Welker, C. / Jaenicke, R. / Kalbitzer, H.R.
CitationJournal: Eur.J.Biochem. / Year: 2001
Title: Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Authors: Kremer, W. / Schuler, B. / Harrieder, S. / Geyer, M. / Gronwald, W. / Welker, C. / Jaenicke, R. / Kalbitzer, H.R.
History
DepositionNov 7, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 7, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
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: COLD SHOCK PROTEIN TMCSP


Theoretical massNumber of molelcules
Total (without water)7,4861
Polymers7,4861
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)7 / 50structures with the lowest energy
Representative

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Components

#1: Protein COLD SHOCK PROTEIN TMCSP


Mass: 7485.569 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermotoga maritima (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: O54310

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1213D 15N-separated NOESY
1313D 13C-separated NOESY

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Sample preparation

DetailsContents: 1.5mM Cold shock protein U-15N,13C; 50mM phosphate buffer pH6.5; 20mM NaCl, 92% H2O, 8% D2O
Solvent system: 92% H2O, 8% D2O
Sample conditionspH: 6.5 / Pressure: ambient / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMXBrukerDMX5001
Bruker DMXBrukerDMX8002

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6Bruker Analytikcollection
AURELIA2.7.10Bruker Analytikdata analysis
X-PLOR3.851Brungerstructure solution
X-PLOR3.851Brungerrefinement
RefinementMethod: dynamic simulated annealing protocol / Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 7

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