BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 6127

Title: Solution structure of the E. coli bacteriophage P1 encoded HOT protein: a homologue of the theta subunit of E. coli DNA polymerase III   PubMed: 15576035

Deposition date: 2004-03-03 Original release date: 2005-02-15

Authors: DeRose, E.; Kirby, T.; Mueller, G.; Chikova, A.; Schaaper, R.; London, R.

Citation: DeRose, E.; Kirby, T.; Mueller, G.; Chikova, A.; Schaaper, R.; London, R.. "Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III"  Structure 12, 2221-2231 (2004).

Assembly members:
p1 encoded protein, polymer, 83 residues, Formula weight is not available

Natural source:   Common Name: E. coli bacteriophage P1   Taxonomy ID: not available   Superkingdom: Bacteriophage   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
p1 encoded protein: MYDWNIAAKSQEERDKVNVD LAASGVAYKERLNIPVIAEQ VAREQPENLRTYFMERLRHY RQLSLQLPKGSDPAYQKDDA VKK

Data sets:
Data typeCount
13C chemical shifts341
1H chemical shifts466
15N chemical shifts87

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HOT protein1

Entities:

Entity 1, HOT protein 83 residues - Formula weight is not available

1   METTYRASPTRPASNILEALAALALYSSER
2   GLNGLUGLUARGASPLYSVALASNVALASP
3   LEUALAALASERGLYVALALATYRLYSGLU
4   ARGLEUASNILEPROVALILEALAGLUGLN
5   VALALAARGGLUGLNPROGLUASNLEUARG
6   THRTYRPHEMETGLUARGLEUARGHISTYR
7   ARGGLNLEUSERLEUGLNLEUPROLYSGLY
8   SERASPPROALATYRGLNLYSASPASPALA
9   VALLYSLYS

Samples:

sample_1: p1 encoded protein, [U-13C; U-15N], 1.3 mM; Tris 5 mM; NaCl 100 mM; NaN3 5 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 7; temperature: 298 K; ionic strength: 100 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1not availablesample_cond_1
3D 15N-separated NOESYsample_1not availablesample_cond_1

Software:

NMRPipe v2.1 Rev 2002.044.17.08 - processing

NMRView v5.0.4 - data analysis

ARIA v1.2 - structure solution

CNS v1.1 - structure solution, refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAQ14071 AAQ14179 EHN41319 EHU11765 EII43590
REF WP_001286531 WP_001667237 WP_024224114 YP_006567

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts