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 6716

Title: Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation   PubMed: 15837199

Deposition date: 2005-06-30 Original release date: 2006-04-25

Authors: Syson, K.; Thirlway, J.; Hounslow, A.; Soultanas, P.; Waltho, J.

Citation: Syson, K.; Thirlway, J.; Hounslow, A.; Soultanas, P.; Waltho, J.. "Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation"  Structure (Cambridge, MA, U. S.) 13, 609-616 (2005).

Assembly members:
DNA primase, polymer, 146 residues, Formula weight is not available

Natural source:   Common Name: Geobacillus stearothermophilus   Taxonomy ID: 1422   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Geobacillus stearothermophilus

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
DNA primase: MAKKLLPAFQNAERLLLAHM MRSRDVALVVQERIGGRFNI EEHRALAAYIYAFYEEGHEA DPGALISRIPGELQPLASEL SLLLIADDVSEQELEDYIRH VLNRPKWLMLKVKEQEKTEA ERRKDFLTAARIAKEMIEMK KMLSSS

Data sets:
Data typeCount
13C chemical shifts581
15N chemical shifts134
1H chemical shifts898

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DNA primase1

Entities:

Entity 1, DNA primase 146 residues - Formula weight is not available

1   METALALYSLYSLEULEUPROALAPHEGLN
2   ASNALAGLUARGLEULEULEUALAHISMET
3   METARGSERARGASPVALALALEUVALVAL
4   GLNGLUARGILEGLYGLYARGPHEASNILE
5   GLUGLUHISARGALALEUALAALATYRILE
6   TYRALAPHETYRGLUGLUGLYHISGLUALA
7   ASPPROGLYALALEUILESERARGILEPRO
8   GLYGLULEUGLNPROLEUALASERGLULEU
9   SERLEULEULEUILEALAASPASPVALSER
10   GLUGLNGLULEUGLUASPTYRILEARGHIS
11   VALLEUASNARGPROLYSTRPLEUMETLEU
12   LYSVALLYSGLUGLNGLULYSTHRGLUALA
13   GLUARGARGLYSASPPHELEUTHRALAALA
14   ARGILEALALYSGLUMETILEGLUMETLYS
15   LYSMETLEUSERSERSER

Samples:

sample_1: DNA primase, [U-15N], 1 mM; potassium phosphate 20 mM; sodium chloride 200 mM; H2O 90%; D2O 10%

sample_2: DNA primase, [U-13C; U-15N], 1 mM; potassium phosphate 20 mM; sodium chloride 200 mM; H2O 90%; D2O 10%

sample_3: DNA primase, [U-15N], 0.5 mM; potassium phosphate 20 mM; sodium chloride 200 mM; H2O 50%; D2O 50%

sample_cond_1: ionic strength: 220 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
simultaneously acquired 15N- and 13C-edited 3D NOESYnot availablenot availablenot available

Software:

xwinnmr v3.5 - collection

FELIX v2000 - data analysis, processing

CNS v1.1 - refinement, structure solution

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
GB AAD20315 KFL17518 KFX31918
REF WP_033007926 WP_033014674
SP Q9X4D0

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