BMRB Entry 19439

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus NS1/2 CW3 WT
Deposition date:
2013-08-20
Original release date:
2014-11-21
Authors:
Borin, Brendan; Krezel, Andrzej
Citation:

Citation: Borin, Brendan; Tang, Wei; Nice, Timothy; McCune, Broc; Virgin, Herbert; Krezel, Andrzej. "Murine norovirus protein NS1/2 aspartate to glutamate mutation sufficient for persistence reorients sidechain of surface exposed tryptophan within a novel structured domain"  Proteins 82, 1200-1209 (2014).
PubMed: 24273131

Assembly members:

Assembly members:
entity, polymer, 69 residues, 7989.188 Da.

Natural source:

Natural source:   Common Name: norovirus   Taxonomy ID: 142786   Superkingdom: virus   Kingdom: not available   Genus/species: norovirus not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-BNK

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts108
15N chemical shifts51
1H chemical shifts371

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1murine norovirus NS1/2 CW3 WT1

Entities:

Entity 1, murine norovirus NS1/2 CW3 WT 69 residues - 7989.188 Da.

MRGSHHHHHHGS is a non-native affinity tag. The remainder of the protein consists of residues 58-114 of the WT protein.

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERGLYALALEUALAALALEUHISALA
3   GLUGLYPROLEUALAGLYLEUPROVALTHR
4   ARGSERASPALAARGVALLEUILEPHEASN
5   GLUTRPGLUGLUARGLYSLYSSERASPPRO
6   TRPLEUARGLEUASPMETSERASPLYSALA
7   ILEPHEARGARGTYRPROHISLEUARG

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 300 mM; entity 0.5 mM; DSS 0 mM

sample_2: sodium phosphate 50 mM; sodium chloride 300 mM; entity, [U-100% 13C; U-100% 15N], 0.5 mM; DSS 0 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
CBCANHsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

SPARKY, Goddard - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

ProcheckNMR, Laskowski and MacArthur - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
GB AAO63098 ABB90153 ABJ98943 ABS29272 ABU55540
REF YP_720001 YP_724455

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