DNA-binding protein H-NS

UniProt P0ACF8 · gene hns · Escherichia coli (strain K12) · 137 residues

19evidence items
0mapped to a state
0states
5techniques
5sources
0conflicts

Coverage grid

Mapped evidence per state and technique. Shaded rows rest on a single technique. Badge = best data level in the cell: raw (traces, images, FIDs: can be re-analysed), proc (maps, curves, tables, trajectories) or rep (values in the paper only).

StateBasisnmr_structurenmr_shiftsforce_spectroscopyaf_predictionmdTotal
No states defined yet.

Unmapped evidence: 19 of 19 items. Mappings come from curator assignments and curated rules; see About for how rules work.

Sources

SourceEvidenceMapped
AlphaFold DB10
BMRB30
MDDB10
RCSB PDB50
SMASH-BIO90

Structure

No state models are exported for this protein yet. Observed states export the representative PDB entry; inferred states need fitted models, not yet built.

States and transitions

No states defined.

StateBasisParentDescription

No transitions recorded in this version (no rate or free-energy evidence has been curated yet).

Evidence

One row per deposit or experiment. Filter by technique, environment or text. Unmapped evidence is listed too.

EvidenceTechniqueObservableConditionsMapped to state
EV-PDB-1NI8-1
RCSB PDB
nmr_structurestructurein vitro · 34.85 °C · pH 6.8
H-NS dimerization motif · DNA-binding protein H-NS (chains A,B)
unmapped
EV-PDB-2MW2-2
RCSB PDB
nmr_structurestructurein vitro · 21.85 °C · pH 7
Hha-H-NS46 charge zipper complex · DNA-binding protein H-NS (chains B,C)
unmapped
EV-PDB-1LR1-1
RCSB PDB
nmr_structurestructurein vitro · 24.85 °C · pH 7
Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS · dna-binding protein h-ns (chains A,B)
unmapped
EV-PDB-1HNS-1
RCSB PDB
nmr_structurestructurein vitro
H-NS (DNA-BINDING DOMAIN) · H-NS (chains A)
unmapped
EV-PDB-1HNR-1
RCSB PDB
nmr_structurestructurein vitro
H-NS (DNA-BINDING DOMAIN) · H-NS (chains A)
unmapped
EV-BMRB-25296
BMRB
nmr_shiftschemical_shiftin vitro · 21.85 °C · pH 7
Hha-H-NS46 charge zipper complex · BMRB data: 15N chemical shifts, 1H chemical shifts
unmapped
EV-BMRB-4802
BMRB
nmr_shiftschemical_shiftin vitro · 24.85 °C · pH 7
1H, 13C, and 15N sequential assignment of the triple labelled N-terminal domain of the Histone like Nucleoid Structuring protein (H-NS) from Salmonella typhimurium (first 64 residues of the protein) · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts
unmapped
EV-BMRB-5390
BMRB
nmr_shiftschemical_shiftin vitro · 24.85 °C · pH 7
1H,13C and 15N Chemical Shifts Assignments for the Oligomerization Domain of H-NS · BMRB data: 1H chemical shifts, 13C chemical shifts, 15N chemical shifts
unmapped
EV-AFDB-AF-P0ACF8-F1
AlphaFold DB
af_predictionplddt: 85.81 pLDDTin silico
AlphaFold DB prediction AF-P0ACF8-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-137
unmapped
EV-MDDB-A00JF
MDDB
mdtrajectory: 10 nsin silico · 26.85 °C
MoDEL 1HNR · start 1HNR; Amber Parm99
unmapped
EV-SMASH-SMFS-002282
SMASH-BIO
force_spectroscopystudy_recordin vitro
Cooperative effects on the compaction of DNA fragments by the nucleoid protein H-NS and the crowding agent PEG probed by Magnetic Tweezers. · H-NS; magnetic tweezers; experiment class: nucleic_acid_protein_interaction, unfolding_protein
unmapped
EV-SMASH-SMFS-003410
SMASH-BIO
force_spectroscopystudy_recordin vitro
Applications of Magnetic Tweezers to Studies of NAPs. · H-NS; magnetic tweezers; experiment class: force_generation_motor, nucleic_acid_protein_interaction, translation_transcription_replication
unmapped
EV-SMASH-SMFS-003655
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 7
Probing the mechanical stability of bridged DNA-H-NS protein complexes by single-molecule AFM pulling. · H-NS; afm smfs; experiment class: chromatin_mechanics, nucleic_acid_protein_interaction, unfolding_protein
unmapped
EV-SMASH-SMFS-004441
SMASH-BIO
force_spectroscopystudy_recordin vitro · pH 8
A biomechanical mechanism for initiating DNA packaging. · H-NS; optical tweezers; experiment class: chromatin_mechanics, force_generation_motor, nucleic_acid_protein_interaction
unmapped
EV-SMASH-SMFS-004592
SMASH-BIO
force_spectroscopystudy_recordin vitro
Locus of enterocyte effacement-encoded regulator (Ler) of pathogenic Escherichia coli competes off histone-like nucleoid-structuring protein (H-NS) through noncooperative DNA binding. · H-NS; magnetic tweezers; experiment class: chromatin_mechanics, nucleic_acid_protein_interaction, rheology_cell, translation_transcription_replication, unfolding_protein
unmapped
EV-SMASH-SMFS-004773
SMASH-BIO
force_spectroscopystudy_recordin vitro
A model of H-NS mediated compaction of bacterial DNA. · H-NS; optical tweezers; experiment class: chromatin_mechanics, nucleic_acid_protein_interaction, unfolding_protein
unmapped
EV-SMASH-SMFS-005633
SMASH-BIO
force_spectroscopystudy_recordin vitro
Salmonella enterica response regulator SsrB relieves H-NS silencing by displacing H-NS bound in polymerization mode and directly activates transcription. · H-NS; magnetic tweezers; experiment class: force_generation_polymerization, nucleic_acid_protein_interaction, translation_transcription_replication
unmapped
EV-SMASH-SMFS-006159
SMASH-BIO
force_spectroscopystudy_recordin vitro
Protein-mediated molecular bridging: a key mechanism in biopolymer organization. · H-NS; optical tweezers; experiment class: chromatin_mechanics, nucleic_acid_protein_interaction, unfolding_protein
unmapped
EV-SMASH-SMFS-006750
SMASH-BIO
force_spectroscopystudy_recordin vitro
Bacterial chromatin organization by H-NS protein unravelled using dual DNA manipulation. · H-NS; optical tweezers; experiment class: chromatin_mechanics, force_generation_motor, nucleic_acid_protein_interaction, unfolding_protein
unmapped

Conflicts

No conflicts found among comparable evidence.

19 evidence items could not be compared: they lack a comparable observable type, a value, or an uncertainty. Absence of a conflict here is not agreement.

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