BMRB Entry 18132

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18132
MolProbity Validation Chart

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Title:
THERMOSTABLE PROTEIN FROM HYPERTHERMOPHILIC VIRUS SSV-RH
Deposition date:
2011-12-09
Original release date:
2012-03-23
Authors:
Schlenker, C.; Goel, Anupam; Tripet, B.; Menon, S.; Lawrence, C.; Copie, V.
Citation:

Citation: Schlenker, Casey; Goel, Anupam; Tripet, Brian; Menon, Smita; Willi, Taylor; Dlakic, Mensur; Young, Mark; Lawrence, C. Martin; Copie, Valerie. "Structural studies of E73 from a hyperthermophilic archaeal virus identify the "RH3" domain, an elaborated ribbon-helix-helix motif involved in DNA recognition."  Biochemistry 51, 2899-2910 (2012).
PubMed: 22409376

Assembly members:

Assembly members:
ORF_E73, polymer, 73 residues, 8627.1995 Da.

Natural source:

Natural source:   Common Name: Sulfolobus virus Ragged Hills   Taxonomy ID: 256994   Superkingdom: Viruses   Kingdom: not available   Genus/species: Fusellovirus Sulfolobus virus Ragged Hills

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ORF_E73: MVESKKIAKKKTTLAFDEDV YHTLKLVSVYLNRDMTEIIE EAVVMWLIQNKEKLPNELKP KIDEISKRFFPAK

Data sets:
Data typeCount
13C chemical shifts171
15N chemical shifts69
1H chemical shifts335

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ORF E73, chain 11
2ORF E73, chain 21

Entities:

Entity 1, ORF E73, chain 1 73 residues - 8627.1995 Da.

1   METVALGLUSERLYSLYSILEALALYSLYS
2   LYSTHRTHRLEUALAPHEASPGLUASPVAL
3   TYRHISTHRLEULYSLEUVALSERVALTYR
4   LEUASNARGASPMETTHRGLUILEILEGLU
5   GLUALAVALVALMETTRPLEUILEGLNASN
6   LYSGLULYSLEUPROASNGLULEULYSPRO
7   LYSILEASPGLUILESERLYSARGPHEPHE
8   PROALALYS

Samples:

sample_1: PMSF, [U-13C; U-15N], 1 mM; SODIUM AZIDE 0.01%; POTASSIUM PHOSPHATE 50 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 0.050 mM; pH: 5.000; pressure: 1.000 atm; temperature: 312.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1solutionsample_conditions_1
3D CBCA(CO)NHsample_1solutionsample_conditions_1
3D C(CO)NHsample_1solutionsample_conditions_1
3D H(CCO)NHsample_1solutionsample_conditions_1
3D HNCAsample_1solutionsample_conditions_1
2D 1H-13C HSQCsample_1solutionsample_conditions_1
3D HBHA(CO)NHsample_1solutionsample_conditions_1
3D HCCH-TOCSYsample_1solutionsample_conditions_1
2D 1H-15N HSQCsample_1solutionsample_conditions_1

Software:

ARIA vany, Linge, O'Donoghue and Nilges - chemical shift assignment

AutoDep v4.3, PDBe - collection

CNS vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

UNP Q6TRU9_9VIRU
BMRB 16177 17069
PDB
GB AAR27912
REF NP_963940
AlphaFold Q6TRU9

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