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- PDB-1nmf: MAJOR COLD-SHOCK PROTEIN, NMR, 20 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1nmf
TitleMAJOR COLD-SHOCK PROTEIN, NMR, 20 STRUCTURES
ComponentsMAJOR COLD-SHOCK PROTEIN
KeywordsTRANSCRIPTION REGULATION / COLD SHOCK PROTEIN
Function / homology
Function and homology information


nucleoid / 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 protein CspB
Similarity search - Component
Biological speciesBacillus subtilis (bacteria)
MethodSOLUTION NMR
AuthorsSchnuchel, A. / Holak, T.A.
Citation
Journal: Nature / Year: 1993
Title: Structure in solution of the major cold-shock protein from Bacillus subtilis.
Authors: Schnuchel, A. / Wiltscheck, R. / Czisch, M. / Herrler, M. / Willimsky, G. / Graumann, P. / Marahiel, M.A. / Holak, T.A.
#1: Journal: J.Bacteriol. / Year: 1992
Title: Characterization of Cspb, a Bacillus Subtilis Inducible Cold Shock Gene Affecting Cell Viability at Low Temperatures
Authors: Willimsky, G. / Bang, H. / Fischer, G. / Marahiel, M.A.
History
DepositionFeb 5, 1996Processing site: BNL
Revision 1.0Jul 11, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4May 1, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MAJOR COLD-SHOCK PROTEIN


Theoretical massNumber of molelcules
Total (without water)7,3721
Polymers7,3721
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein MAJOR COLD-SHOCK PROTEIN / CSPB


Mass: 7372.126 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus subtilis (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P32081

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR ensembleConformers submitted total number: 20

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