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 34545

Title: Solution structure of the C-terminal domain of the vaccinia virus DNA polymerase processivity factor component A20.   PubMed: 33901538

Deposition date: 2020-07-31 Original release date: 2021-05-12

Authors: Bersch, B.; Iseni, F.; Burmeister, W.; Tarbouriech, N.

Citation: Bersch, B.; Tarbouriech, N.; Burmeister, W.; Iseni, F.. "Solution structure of the C-terminal domain of A20, the missing brick for the characterization of the interface between vaccinia virus DNA polymerase and its processivity factor"  J. Mol. Biol. 433, 167009-167009 (2021).

Assembly members:
entity_1, polymer, 148 residues, 16668.709 Da.

Natural source:   Common Name: VACV   Taxonomy ID: 10249   Superkingdom: Viruses   Kingdom: not available   Genus/species: Orthopoxvirus VACV

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: GNGKYFSKVGSAGLKQLTNK LDINECATVDELVDEINKSG TVKRKIKNQSAFDLSRECLG YPEADFITLVNNMRFKIENC KVVNFNIENTNCLNNPSIET IYRNFNQFVSIFNVVTDVKK RLFENASGNGSGGGLNDIFE AQKIEWHE

Data typeCount
13C chemical shifts551
15N chemical shifts162
1H chemical shifts961
T1 relaxation values133
T2 relaxation values133
heteronuclear NOE values133

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 148 residues - 16668.709 Da.

1   GLYASNGLYLYSTYRPHESERLYSVALGLY
2   SERALAGLYLEULYSGLNLEUTHRASNLYS
3   LEUASPILEASNGLUCYSALATHRVALASP
4   GLULEUVALASPGLUILEASNLYSSERGLY
5   THRVALLYSARGLYSILELYSASNGLNSER
6   ALAPHEASPLEUSERARGGLUCYSLEUGLY
7   TYRPROGLUALAASPPHEILETHRLEUVAL
8   ASNASNMETARGPHELYSILEGLUASNCYS
9   LYSVALVALASNPHEASNILEGLUASNTHR
10   ASNCYSLEUASNASNPROSERILEGLUTHR
11   ILETYRARGASNPHEASNGLNPHEVALSER
12   ILEPHEASNVALVALTHRASPVALLYSLYS
13   ARGLEUPHEGLUASNALASERGLYASNGLY
14   SERGLYGLYGLYLEUASNASPILEPHEGLU
15   ALAGLNLYSILEGLUTRPHISGLU

Samples:

sample_1: A20-BAP, [U-15N], 1 mM; sodium citrate 50 mM; sodium chloride 300 mM; TCEP 2 mM

sample_2: A20-BAP, [U-15N], 1 mM; sodium chloride 300 mM; TCEP 1.2 mM; potassium phosphate 50 mM

sample_3: A20-BAP, [U-15N; U-13C], 1 mM; sodium chloride 300 mM; TCEP 1.2 mM; potassium phosphate 50 mM

sample_4: A20-BAP, [U-15N; U-13C], 1 mM; sodium citrate 50 mM; sodium chloride 300 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 0.3 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 15N-TROSYsample_1isotropicsample_conditions_1
2D 13C-HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
2D-NOESYsample_2isotropicsample_conditions_1
13C-NOESYsample_3isotropicsample_conditions_1
15N-NOESYsample_1isotropicsample_conditions_1
13C-13C-methyl-NOESYsample_3isotropicsample_conditions_1
15N hetNOEsample_1isotropicsample_conditions_1
15N-R2sample_1isotropicsample_conditions_1
15N-R1sample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection, processing

CcpNmr Analysis, CCPN - chemical shift assignment

UNIO, Torsten Herrmann - peak picking

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

  • Bruker AVANCE 950 MHz
  • Bruker AVANCE 850 MHz
  • Bruker AVANCE 600 MHz

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