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 25083

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR structure for potential drug target from Burkholderia thailandensis E264'

Deposition date: 2014-07-09 Original release date: 2014-07-16

Authors: Barnwal, Ravi P; Varani, Gabriele

Citation: Barnwal, Ravi P; Varani, Gabriele. "Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR structure for potential drug target from Burkholderia thailandensis E264'"  To be Published ., .-..

Assembly members:
entity, polymer, 72 residues, 8133.381 Da.

Natural source:   Common Name: Burkholderia thailandensis   Taxonomy ID: 57975   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia thailandensis

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

Entity Sequences (FASTA):
entity: MDRIFMTRTEALEFLLKAHQ TAVDKIGHPSHKQTPADHAA IEALDRLLLDVRARRVDQFQ INASAAQIIVTD

Data sets:
Data typeCount
1H chemical shifts468
13C chemical shifts321
15N chemical shifts76

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 72 residues - 8133.381 Da.

1   METASPARGILEPHEMETTHRARGTHRGLU
2   ALALEUGLUPHELEULEULYSALAHISGLN
3   THRALAVALASPLYSILEGLYHISPROSER
4   HISLYSGLNTHRPROALAASPHISALAALA
5   ILEGLUALALEUASPARGLEULEULEUASP
6   VALARGALAARGARGVALASPGLNPHEGLN
7   ILEASNALASERALAALAGLNILEILEVAL
8   THRASP

Samples:

sample_1: Putative uncharacterized protein (BTH_I2711), [U-95% 13C; U-95% 15N], 7.2 mg/mL

sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

TALOS, Cornilescu, Delaglio and Bax - data analysis

CCPNMR, CCPN - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB ABC38190 AHI63721 AHI71863 AHI77508 AIC85718
REF WP_009910381

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