BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15987

Title: NMR structure of plasmid copy control protein ORF56 from sulfolobus islandicus   PubMed: 19788170

Deposition date: 2008-10-15 Original release date: 2009-10-16

Authors: Weininger, Ulrich; Balbach, Jochen

Citation: Weininger, Ulrich; Zeeb, Markus; Neumann, Piotr; Low, Christian; Stubbs, Milton; Lipps, Georg; Balbach, Jochen. "Structure-based stability analysis of an extremely stable dimeric DNA binding protein from Sulfolobus islandicus."  Biochemistry 48, 10030-10037 (2009).

Assembly members:
ORF56, polymer, 55 residues, 149.207 Da.

Natural source:   Common Name: Sulfolobus islandicus   Taxonomy ID: 43080   Superkingdom: Archaea   Kingdom: not available   Genus/species: Sulfolobus islandicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
ORF56: GRPYKLLNGIKLGVYIPQEW HDRLMEIAKEKNLTLSDVCR LAIKEYLDNHDKQKK

Data sets:
Data typeCount
1H chemical shifts427

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1METHIONINE, chain 11
2METHIONINE, chain 21

Entities:

Entity 1, METHIONINE, chain 1 55 residues - 149.207 Da.

1   GLYARGPROTYRLYSLEULEUASNGLYILE
2   LYSLEUGLYVALTYRILEPROGLNGLUTRP
3   HISASPARGLEUMETGLUILEALALYSGLU
4   LYSASNLEUTHRLEUSERASPVALCYSARG
5   LEUALAILELYSGLUTYRLEUASPASNHIS
6   ASPLYSGLNLYSLYS

Samples:

sample_1: entity_2, [U-13C; U-15N], 1 mM; entity_2 2 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker DRX 400 MHz