BMRB Entry 30421

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30421
MolProbity Validation Chart

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Title:
Solution structure of the Burkholderia thailandensis transcription antitermination protein NusB (BTH_I1529) - Seattle Structural Genomics Center for Infectious Disease target ButhA.17903.a
Deposition date:
2018-02-28
Original release date:
2018-03-29
Authors:
Buchko, G.; Seattle Structural Genomics Center for Infectious Disease, SSGCID
Citation:

Citation: Buchko, G.; SSGCID, SSGCID. "Solution structure of the Burkholderia thailandensis transcription antitermination protein NusB (BTH_I1529)."  .

Assembly members:

Assembly members:
entity_1, polymer, 149 residues, 16301.551 Da.

Natural source:

Natural source:   Common Name: Burkholderia thailandensis   Taxonomy ID: 271848   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia thailandensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSMKKSARRQSRELATQG LYQWLLSNAAPGEIDAQLRG ALGYDKADKTLLDTILHGVI REHATLAEAISPSLDRPIDQ LSPVERAVLLIATYELTHQI ETPYRVIINEAVELAKTFGG SDGYKYVNGVLDKLAVKLRP AETQARRGA

Data sets:
Data typeCount
13C chemical shifts543
15N chemical shifts147
1H chemical shifts825

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 149 residues - 16301.551 Da.

1   GLYPROGLYSERMETLYSLYSSERALAARG
2   ARGGLNSERARGGLULEUALATHRGLNGLY
3   LEUTYRGLNTRPLEULEUSERASNALAALA
4   PROGLYGLUILEASPALAGLNLEUARGGLY
5   ALALEUGLYTYRASPLYSALAASPLYSTHR
6   LEULEUASPTHRILELEUHISGLYVALILE
7   ARGGLUHISALATHRLEUALAGLUALAILE
8   SERPROSERLEUASPARGPROILEASPGLN
9   LEUSERPROVALGLUARGALAVALLEULEU
10   ILEALATHRTYRGLULEUTHRHISGLNILE
11   GLUTHRPROTYRARGVALILEILEASNGLU
12   ALAVALGLULEUALALYSTHRPHEGLYGLY
13   SERASPGLYTYRLYSTYRVALASNGLYVAL
14   LEUASPLYSLEUALAVALLYSLEUARGPRO
15   ALAGLUTHRGLNALAARGARGGLYALA

Samples:

sample_1: NusB, [U-99% 13C; U-99% 15N], 1 ± 0.3 mM; sodium chloride 100 ± 0.05 mM; TRIS 20 ± 0.05 mM; DTT 1 ± 0.02 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D Deltassample_1isotropicsample_conditions_1
deuterium exchangesample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY v3.13, Goddard - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.5, Bhattacharya and Montelione - peak picking

Felix v2007, Accelrys Software Inc. - processing

NMR spectrometers:

  • Varian VXRS 600 MHz
  • Agilent VXRS 750 MHz
  • Agilent VXRS 800 MHz

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