BMRB Entry 26858

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26858

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Title:
Backbone chemical shift assignments for the U1 protein from the Bas-Congo virus. Seattle Structural Genomic Center for Infectious Disease target RhbaA.18619.a.D16.
Deposition date:
2016-07-24
Original release date:
2016-08-23
Authors:
Buchko, Garry
Citation:

Citation: Buchko, Garry; Clifton, Matthew; Wallace, Ellen; Atkins, Kateri; Myler, Peter. "Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus"  Biomol NMR Assign 11, 51-56 (2017).
PubMed: 27981424

Assembly members:

Assembly members:
BASV_U1, polymer, 177 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bas-Congo viruses   Taxonomy ID: 1231712   Superkingdom: Viruses   Kingdom: not available   Genus/species: not available Bas-Congo viruses

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pEMB32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BASV_U1: ATMAFHPMLCRLELSVSAAP PASPIDATLLRSLITSVLNS SWVDLGGNTANEKVLCAIGL IEAFCRERVIPPTSNSFNTS VTYHIMVEDLDPDDLGNIQL INKPLLSLEGDLKVLGSYQL TFQTIPGHSEPRSMTDNGIY HSDSPFFQIALGHALLGTGK IYDHITRALRVAPITIA

Data sets:
Data typeCount
13C chemical shifts395
15N chemical shifts124
1H chemical shifts303

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BASV-U11

Entities:

Entity 1, BASV-U1 177 residues - Formula weight is not available

1   ALATHRMETALAPHEHISPROMETLEUCYS
2   ARGLEUGLULEUSERVALSERALAALAPRO
3   PROALASERPROILEASPALATHRLEULEU
4   ARGSERLEUILETHRSERVALLEUASNSER
5   SERTRPVALASPLEUGLYGLYASNTHRALA
6   ASNGLULYSVALLEUCYSALAILEGLYLEU
7   ILEGLUALAPHECYSARGGLUARGVALILE
8   PROPROTHRSERASNSERPHEASNTHRSER
9   VALTHRTYRHISILEMETVALGLUASPLEU
10   ASPPROASPASPLEUGLYASNILEGLNLEU
11   ILEASNLYSPROLEULEUSERLEUGLUGLY
12   ASPLEULYSVALLEUGLYSERTYRGLNLEU
13   THRPHEGLNTHRILEPROGLYHISSERGLU
14   PROARGSERMETTHRASPASNGLYILETYR
15   HISSERASPSERPROPHEPHEGLNILEALA
16   LEUGLYHISALALEULEUGLYTHRGLYLYS
17   ILETYRASPHISILETHRARGALALEUARG
18   VALALAPROILETHRILEALA

Samples:

sample_1: BASV_U1, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; urea 500 ± 10 mM; H2O 93%; D2O 7%

sample_2: BASV_U1, [U-100% 13C; U-100% 15N; U-80% 2H], 1 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.2 mM; urea 500 ± 10 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.62 M; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - data analysis

Felix v2007, Accelrys Software Inc. - processing

NMR spectrometers:

  • Varian VXRS 750 MHz
  • Varian INOVA 600 MHz

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