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 34287

Title: NMR structure of the free helix bundle domain from the functional pRN1 primase   PubMed: 30595448

Deposition date: 2018-06-15 Original release date: 2018-12-19

Authors: Boudet, J.; Lipps, G.; Allain, F.

Citation: Boudet, J.; Devillier, J.; Wiegand, T.; Salmon, L.; Meier, B.; Lipps, G.; Allain, F.. "A Small Helical Bundle Prepares Primer Synthesis by Binding Two Nucleotides that Enhance Sequence-Specific Recognition of the DNA Template"  Cell 176, 154-166 (2019).

Assembly members:
entity_1, polymer, 115 residues, 13528.738 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 BL21(DE3)

Entity Sequences (FASTA):
entity_1: TVVEFEELRKELVKRDSGKP VEKIKEEICTKSPPKLIKEI ICENKTYADVNIDRSRGDWH VILYLMKHGVTDPDKILELL PRDSKAKENEKWNTQKYFVI TLSKAWSVVKKYLEA

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts102
1H chemical shifts693

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 115 residues - 13528.738 Da.

1   THRVALVALGLUPHEGLUGLULEUARGLYS
2   GLULEUVALLYSARGASPSERGLYLYSPRO
3   VALGLULYSILELYSGLUGLUILECYSTHR
4   LYSSERPROPROLYSLEUILELYSGLUILE
5   ILECYSGLUASNLYSTHRTYRALAASPVAL
6   ASNILEASPARGSERARGGLYASPTRPHIS
7   VALILELEUTYRLEUMETLYSHISGLYVAL
8   THRASPPROASPLYSILELEUGLULEULEU
9   PROARGASPSERLYSALALYSGLUASNGLU
10   LYSTRPASNTHRGLNLYSTYRPHEVALILE
11   THRLEUSERLYSALATRPSERVALVALLYS
12   LYSTYRLEUGLUALA

Samples:

sample_1: 13C, 15N helix bundle domain, [U-99% 13C; U-99% 15N], 1.2 mM; 15N helix bundle domain, [U-99% 15N], 0.9 mM; NaCl 50 mM

sample_2: 13C helix bundle domain, [U-100% 13C], 0.7 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N-NOESY-HSQCsample_1isotropicsample_conditions_1
13Cali-NOESY-HSQCsample_1isotropicsample_conditions_1
13Caro-NOESY-HSQCsample_1isotropicsample_conditions_1
13Cali-HSQCsample_2isotropicsample_conditions_1
13Caro-HSQCsample_2isotropicsample_conditions_1
15N-HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment

CANDID, Herrmann, Guntert and Wuthrich - peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 900 MHz
  • Bruker AVANCE III 700 MHz
  • Bruker AVANCE III 600 MHz

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