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- PDB-1hnr: H-NS (DNA-BINDING DOMAIN) -

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Basic information

Entry
Database: PDB / ID: 1hnr
TitleH-NS (DNA-BINDING DOMAIN)
ComponentsH-NSHistone-like nucleoid-structuring protein
KeywordsDNA BINDING PROTEIN / HISTONE-LIKE PROTEIN H1 / DNA-BINDING PROTEIN
Function / homology
Function and homology information


H-NS-Cnu complex / H-NS complex / H-NS-Hha complex / negative regulation of single-species biofilm formation on inanimate substrate / bacterial nucleoid packaging / bent DNA binding / DNA-binding transcription repressor activity / minor groove of adenine-thymine-rich DNA binding / protein-DNA complex / structural constituent of chromatin ...H-NS-Cnu complex / H-NS complex / H-NS-Hha complex / negative regulation of single-species biofilm formation on inanimate substrate / bacterial nucleoid packaging / bent DNA binding / DNA-binding transcription repressor activity / minor groove of adenine-thymine-rich DNA binding / protein-DNA complex / structural constituent of chromatin / regulation of translation / transcription regulator complex / protein dimerization activity / transcription cis-regulatory region binding / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / RNA binding / membrane / identical protein binding / cytosol
Similarity search - Function
Histone-like protein H-NS, C-terminal domain / H-NS DNA Binding Protein / Histone-like protein H-NS, N-terminal / Histone-like protein H-NS, C-terminal domain superfamily / Histone-like protein H-NS / Histone-like protein H-NS, C-terminal domain / H-NS histone family / Domain in histone-like proteins of HNS family / Few Secondary Structures / Irregular
Similarity search - Domain/homology
DNA-binding protein H-NS
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR
AuthorsShindo, H. / Iwaki, T. / Ieda, R. / Kurumizaka, H. / Ueguchi, C. / Mizuno, T. / Morikawa, S. / Nakamura, H. / Kuboniwa, H.
CitationJournal: FEBS Lett. / Year: 1995
Title: Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli.
Authors: Shindo, H. / Iwaki, T. / Ieda, R. / Kurumizaka, H. / Ueguchi, C. / Mizuno, T. / Morikawa, S. / Nakamura, H. / Kuboniwa, H.
History
DepositionApr 6, 1995Processing site: BNL
Revision 1.0Jul 10, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations ...Database references / Derived calculations / Other / Structure summary
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_keywords
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_keywords.text

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: H-NS


Theoretical massNumber of molelcules
Total (without water)5,3091
Polymers5,3091
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein/peptide H-NS / Histone-like nucleoid-structuring protein


Mass: 5308.929 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0ACF8

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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

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Processing

SoftwareName: AMBER / Classification: refinement
NMR software
NameDeveloperClassification
EMBOSSNAKAI,KIDERA,NAKAMURArefinement
PRESTOMORIKAMI,NAKAI,KIDERA,SAITO,NAKAMURArefinement
NMR ensembleConformers submitted total number: 1

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