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 19436

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus NS1/2 D94E mutant   PubMed: 24273131

Deposition date: 2013-08-18 Original release date: 2013-12-16

Authors: Borin, Brendan; Krezel, Andrzej

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 ., .-. (2013).

Assembly members:
entity, polymer, 98 residues, 11122.521 Da.

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

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

Entity Sequences (FASTA):
entity: MRGSHHHHHHGSVSFGAPSP LSSESEDEINYMTPPEQEAQ PGALAALHAEGPLAGLPVTR SDARVLIFNEWEERKKSEPW LRLDMSDKAIFRRYPHLR

Data sets:
Data typeCount
1H chemical shifts529
15N chemical shifts75
13C chemical shifts307

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1murine norovirus NS1/2 D94E mutant1

Entities:

Entity 1, murine norovirus NS1/2 D94E mutant 98 residues - 11122.521 Da.

MRGSHHHHHHGS is a purification tag. The remainder of the sequence corresponds to residues 28-114.

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERVALSERPHEGLYALAPROSERPRO
3   LEUSERSERGLUSERGLUASPGLUILEASN
4   TYRMETTHRPROPROGLUGLNGLUALAGLN
5   PROGLYALALEUALAALALEUHISALAGLU
6   GLYPROLEUALAGLYLEUPROVALTHRARG
7   SERASPALAARGVALLEUILEPHEASNGLU
8   TRPGLUGLUARGLYSLYSSERGLUPROTRP
9   LEUARGLEUASPMETSERASPLYSALAILE
10   PHEARGARGTYRPROHISLEUARG

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 300 mM; entity, [U-100% 15N], 1 mM; DSS 0 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 50 mM; sodium chloride 300 mM; entity, [U-100% 13C; U-100% 15N], 1 mM; DSS 0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.35 M; pH: 7.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
CBCANHsample_2isotropicsample_conditions_1
CBCACONHsample_2isotropicsample_conditions_1
HCCCONHsample_2isotropicsample_conditions_1
CCCONHsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_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 ABS29272 ACS70958 AET79289

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