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 25278

Title: Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS. Seattle Structural Genomics Center for Infectious Disease target BupsA.00863.i.

Deposition date: 2014-10-09 Original release date: 2014-11-11

Authors: Buchko, Garry

Citation: Buchko, Garry; Edwards, Thomas; Hewitt, Stephen; Phan, Isabelle; Van Voorhis, Wesley; Miller, Samuel; Myler, Peter. "Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS - An "invisible" dimer interface."  Not known ., .-..

Assembly members:
RisS, polymer, 127 residues, Formula weight is not available

Natural source:   Common Name: b-proteobacteria   Taxonomy ID: 28450   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia pseudomallei

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

Entity Sequences (FASTA):
RisS: GPGSMSFRVIEREPRAQRVA LQLVAIVKLTRTALLYSDPD LRRALLQDLESNEGVRVYPR EKTDKFKLQPDESVNRLIEH DIRSRLGDDTVIAQSVNDIP GVWISFKIDDDDYWVALDRD QLDTVTG

Data sets:
Data typeCount
13C chemical shifts247
1H chemical shifts75
15N chemical shifts77

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 127 residues - Formula weight is not available

1   GLYPROGLYSERMETSERPHEARGVALILE
2   GLUARGGLUPROARGALAGLNARGVALALA
3   LEUGLNLEUVALALAILEVALLYSLEUTHR
4   ARGTHRALALEULEUTYRSERASPPROASP
5   LEUARGARGALALEULEUGLNASPLEUGLU
6   SERASNGLUGLYVALARGVALTYRPROARG
7   GLULYSTHRASPLYSPHELYSLEUGLNPRO
8   ASPGLUSERVALASNARGLEUILEGLUHIS
9   ASPILEARGSERARGLEUGLYASPASPTHR
10   VALILEALAGLNSERVALASNASPILEPRO
11   GLYVALTRPILESERPHELYSILEASPASP
12   ASPASPTYRTRPVALALALEUASPARGASP
13   GLNLEUASPTHRVALTHRGLY

Samples:

sample_1: RisS, [U-13C; U-15N; U-2H], 1 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.1 mM; H2O 93 ± 0.1 %; D2O 7 ± 0.1 %

sample_conditions_1: temperature: 203 K; pH: 7; pressure: 1 atm; ionic strength: 0.12 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

Felix v2007, Accelrys Software Inc. - processing

SPARKY v3.115, Goddard - data analysis

NMR spectrometers:

  • Agilent INOVA 750 MHz
  • Agilent INOVA 600 MHz

Related Database Links:

PDB
DBJ BAG43831
EMBL CAH36098 CAR52312 CDN60458 CDU28740 CFB52363
GB AAU47661 ABA50560 ABB08844 ABC38194 ABF81004
REF WP_004196632 WP_004531418 WP_006402221 WP_006408378 WP_006415644

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