BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 25463

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25463

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Title: Backbone Chemical Shift Assignments for the Wild-Type Dimeric Non-Structural Protein 1 Effector Domain from Influenza B Virus   PubMed: 27545620

Deposition date: 2015-02-02 Original release date: 2015-03-02

Authors: Hamilton, Keith; Aramini, James; Ma, Li-Chung; Krug, Robert; Montelione, Gaetano

Citation: Ma, Li-Chung; Guan, Rongjin; Hamilton, Keith; Aramini, James; Mao, Lei; Wang, Shanshan; Krug, Robert; Montelione, Gaetano. "A Second RNA-Binding Site in the NS1 Protein of Influenza B Virus."  Structure 24, 1562-1572 (2016).

Assembly members:
NS1B_ED, polymer, 141 residues, Formula weight is not available

Natural source:   Common Name: Influenza B virus   Taxonomy ID: 11520   Superkingdom: Viruses   Kingdom: not available   Genus/species: Influenzavirus B Influenza B virus

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

Entity Sequences (FASTA):
NS1B_ED: HPIEVVLRDMNNKDARQKIK DEVNTQKEGKFRLTIKRDIR NVLSLRVLVNGTFLKHPNGD KSLSTLHRLNAYDQNGGLVA KLVATDDLTVEDEKDGHRIL NSLFERFDEGHSKPIRAAET AVGVLSQFGQEHRLSPEEGD N

Data sets:
Data typeCount
13C chemical shifts376
15N chemical shifts135
1H chemical shifts136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS1B ED dimer, 11
2NS1B ED dimer, 21

Entities:

Entity 1, NS1B ED dimer, 1 141 residues - Formula weight is not available

1   HISPROILEGLUVALVALLEUARGASPMET
2   ASNASNLYSASPALAARGGLNLYSILELYS
3   ASPGLUVALASNTHRGLNLYSGLUGLYLYS
4   PHEARGLEUTHRILELYSARGASPILEARG
5   ASNVALLEUSERLEUARGVALLEUVALASN
6   GLYTHRPHELEULYSHISPROASNGLYASP
7   LYSSERLEUSERTHRLEUHISARGLEUASN
8   ALATYRASPGLNASNGLYGLYLEUVALALA
9   LYSLEUVALALATHRASPASPLEUTHRVAL
10   GLUASPGLULYSASPGLYHISARGILELEU
11   ASNSERLEUPHEGLUARGPHEASPGLUGLY
12   HISSERLYSPROILEARGALAALAGLUTHR
13   ALAVALGLYVALLEUSERGLNPHEGLYGLN
14   GLUHISARGLEUSERPROGLUGLUGLYASP
15   ASN

Samples:

sample_1: NS1B ED, [U-13C; U-15N; U-2H; 1H-Ile-delta1,Leu-delta,Val-gamma], 25 mM; sodium chloride 450 mM; calcium chloride 5 mM; arginine 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.45 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY-HSQCsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-TROSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - data collection

NMRPipe v2.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data processing

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AVS v2.4.0, Moseley and Montelione - chemical shift validation

SPARKY v3, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP P03502

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