BMRB Entry 34544

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34544
MolProbity Validation Chart

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Title:
Solution structure of the C-terminal domain of the vaccinia virus DNA polymerase processivity factor component A20 fused to a short peptide from the viral DNA polymerase E9.
Deposition date:
2020-07-30
Original release date:
2021-05-12
Authors:
Bersch, B.; Tarbouriech, N.; Burmeister, W.; Iseni, F.
Citation:

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).
PubMed: 33901538

Assembly members:

Assembly members:
entity_1, polymer, 151 residues, 16882.934 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GNGKYFSKVGSAGLKQLTNK LDINECATVDELVDEINKSG TVKRKIKNQSAFDLSRECLG YPEADFITLVNNMRFKIENC KVVNFNIENTNCLNNPSIET IYRNFNQFVSIFNVVTDVKK RLFENASGNGSGGGSNRLEE EINNQLALQKS

Data typeCount
13C chemical shifts583
15N chemical shifts169
1H chemical shifts1008
T1 relaxation values116
T2 relaxation values116
heteronuclear NOE values118

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 151 residues - 16882.934 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   SERGLYGLYGLYSERASNARGLEUGLUGLU
15   GLUILEASNASNGLNLEUALALEUGLNLYS
16   SER

Samples:

sample_1: A20-i3, [U-15N], 1 mM; potassium phosphate 50 mM; NaCl 300 mM; TCEP 1.2 mM

sample_2: A20-i3, [U-15N; U-13C], 0.8 mM; potassium phosphate 50 mM; NaCl 300 mM; TCEP 1.2 mM

sample_3: A20-i3, [U-15N; U-13C], 1 mM; potassium phosphate 50 mM; NaCl 300 mM; TCEP 1.2 mM

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

Experiments:

NameSampleSample stateSample conditions
15N-Trosysample_1isotropicsample_conditions_1
13C-HSQCsample_2isotropicsample_conditions_1
2D-Tocsysample_3isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D NOESYsample_3isotropicsample_conditions_1
3D-13C-13C methyl noesysample_2isotropicsample_conditions_1
3D-13C edited NOESYsample_2isotropicsample_conditions_1
3D-15N-edited NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_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

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMR spectrometers:

  • Bruker AVANCE 950 MHz
  • Bruker AVANCE 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks