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 30161

Title: Solution structure of response regulator protein from Burkholderia multivorans

Deposition date: 2016-08-26 Original release date: 2016-09-09

Authors: Yang, F.; Lim, Y.-B.; Barnwal, R.; Varani, G.

Citation: Yang, F.; Lim, Y.-B.; Barnwal, R.; Varani, G.. "Solution structure of response regulator protein from Burkholderia multivorans"  . ., .-..

Assembly members:
entity_1, polymer, 125 residues, 13024.712 Da.

Natural source:   Common Name: Burkholderia multivorans   Taxonomy ID: 87883   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia multivorans

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

Entity Sequences (FASTA):
entity_1: MIRTILAIDDSATMRALLHA TLAQAGYEVTVAADGEAGFD LAATTAYDLVLTDQNMPRKS GLELIAALRQLSAYADTPIL VLTTEGSDAFKAAARDAGAT GWIEKPIDPGVLVELVATLS EPAAN

Data sets:
Data typeCount
13C chemical shifts468
15N chemical shifts111
1H chemical shifts736

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 125 residues - 13024.712 Da.

1   METILEARGTHRILELEUALAILEASPASP
2   SERALATHRMETARGALALEULEUHISALA
3   THRLEUALAGLNALAGLYTYRGLUVALTHR
4   VALALAALAASPGLYGLUALAGLYPHEASP
5   LEUALAALATHRTHRALATYRASPLEUVAL
6   LEUTHRASPGLNASNMETPROARGLYSSER
7   GLYLEUGLULEUILEALAALALEUARGGLN
8   LEUSERALATYRALAASPTHRPROILELEU
9   VALLEUTHRTHRGLUGLYSERASPALAPHE
10   LYSALAALAALAARGASPALAGLYALATHR
11   GLYTRPILEGLULYSPROILEASPPROGLY
12   VALLEUVALGLULEUVALALATHRLEUSER
13   GLUPROALAALAASN

Samples:

sample_1: HEPES 25 mM; response regulator protein, [U-13C; U-15N], 0.9 mM

sample_2: HEPES 25 mM; response regulator protein, [U-13C; U-15N], 0.9 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

CcpNMR, CCPN - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

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