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 15740

Title: Structure ensemble Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments, 1H-15N RDCs and 1H-1H nOe restraints for protein K7 from the Vaccinia virus   PubMed: 18845156

Authors: Kalverda, Arnout; Thompson, Gary; Vogel, Andre; Schr der, Martina; Bowie, Andrew; Khan, Amir; Homans, Steve

Citation: Kalverda, Arnout; Thompson, Gary; Vogel, Andre; Schroeder, Martina; Bowie, Andrew; Khan, Amir; Homans, Steve. "Poxvirus K7 protein adopts a Bcl-2 fold: Biochemical mapping of its interactions with human DEAD box RNA helicase DDX3"  J. Mol. Biol. 385, 843-853 (2009).

Assembly members:
K7, polymer, 145 residues, 17489.023 Da.

Natural source:   Common Name: Vaccinia Virus   Taxonomy ID: 10245   Superkingdom: Viruses   Kingdom: not available   Genus/species: Vaccinia Virus

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

Entity Sequences (FASTA):
K7: GAMEDAVFYFVDDDKICSRD SIIDLIDEYITWRNHVIVFN KDITSCGRLYKELMKFDDVA IRYYGIDKINEIVEAMSEGD HYINFTKVHDQESLFATIGI CAKITEHWGYKKISESRFQS LGNITDLMTDDNINILILFL EKKLN

Data sets:
Data typeCount
13C chemical shifts612
15N chemical shifts145
1H chemical shifts941
residual dipolar couplings70

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1K71

Entities:

Entity 1, K7 145 residues - 17489.023 Da.

The sequence matches the natural polymer from residue 4 onwards which is equivalent to residue 8 in the natural sequence The GAM n-terminal tag is an expression artifact

1   GLYALAMETGLUASPALAVALPHETYRPHE
2   VALASPASPASPLYSILECYSSERARGASP
3   SERILEILEASPLEUILEASPGLUTYRILE
4   THRTRPARGASNHISVALILEVALPHEASN
5   LYSASPILETHRSERCYSGLYARGLEUTYR
6   LYSGLULEUMETLYSPHEASPASPVALALA
7   ILEARGTYRTYRGLYILEASPLYSILEASN
8   GLUILEVALGLUALAMETSERGLUGLYASP
9   HISTYRILEASNPHETHRLYSVALHISASP
10   GLNGLUSERLEUPHEALATHRILEGLYILE
11   CYSALALYSILETHRGLUHISTRPGLYTYR
12   LYSLYSILESERGLUSERARGPHEGLNSER
13   LEUGLYASNILETHRASPLEUMETTHRASP
14   ASPASNILEASNILELEUILELEUPHELEU
15   GLULYSLYSLEUASN

Samples:

K7D8_UCN: K7D8, [U-13C; U-15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 100 mM; DTT 10 mM; DSS 0.1 mM; D2O 10%; H2O 90%

K7D8_UN: K7D8, [U-15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 100 mM; DTT 10 mM; DSS 0.1 mM; D2O 10%; H2O 90%

K7D8_UN_PF1: K7D8, [U-15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 100 mM; DTT 10 mM; DSS 0.1 mM; Pf1 phage 12 mg/ml; D2O 10%; H2O 90%

K7R_CONDITIONS_1: ionic strength: 122.5 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCK7D8_UNisotropicK7R_CONDITIONS_1
2D 1H-13C HSQCK7D8_UCNisotropicK7R_CONDITIONS_1
3D HNCAK7D8_UCNisotropicK7R_CONDITIONS_1
3D HN(CO)CAK7D8_UCNisotropicK7R_CONDITIONS_1
3D CBCA(CO)NHK7D8_UCNisotropicK7R_CONDITIONS_1
3D HNCOK7D8_UCNisotropicK7R_CONDITIONS_1
3D HNHAK7D8_UCNisotropicK7R_CONDITIONS_1
3D 1H-15N NOESYK7D8_UNisotropicK7R_CONDITIONS_1
3D CBCA(CO)NHK7D8_UCNisotropicK7R_CONDITIONS_1
2D 1H-13C constant time aromatic selected HSQCK7D8_UCNisotropicK7R_CONDITIONS_1
3D H(C)CH-TOCSYK7D8_UCNisotropicK7R_CONDITIONS_1
3D (H)CCH-TOCSYK7D8_UCNisotropicK7R_CONDITIONS_1
2D HB(CBCGCD)HDK7D8_UCNisotropicK7R_CONDITIONS_1
2D HB(CBCGCDCE)HEK7D8_UCNisotropicK7R_CONDITIONS_1
3D 1H-13C NOESYK7D8_UCNisotropicK7R_CONDITIONS_1
2D j modulated 1H-15N HSQCK7D8_UNisotropicK7R_CONDITIONS_1
2D 1H-(13C)-1H aromatic optimised 13C filtered (HSQC) NOESYK7D8_UCNisotropicK7R_CONDITIONS_1

Software:

VNMR v6.1c, Varian - nmr data collection

NMRPipe v2.5 Rev 2006.184.15.37, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - determination of RDC Da & Dr parameters, processing

ccpn_analysis v1.0.9-1.0.15, CCPN - chemical shift assignment, peak picking

X-PLOR NIH v2.17, Schwieters, Kuszewski, Tjandra and Clore - structure solution

ARIA v2.17, Linge, O, nilges@pasteur.fr - refinement

NMRView v5.22, Johnson, One Moon Scientific - rdc data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAA00293
EMBL CAA48965 CAA64114 CAB54624 CAM58208 CRL86498
GB AAA48013 AAA60772 AAB96484 AAF33890 AAO89318
PRF 2015436AB
REF NP_042068 YP_232921
SP P68466 P68467 Q76ZX2