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 18255

Title: Solution structure of a MbtH-like protein from Burkholderia pseudomallei, the etiological agent responsible for melioidosis. Seattle Structural Genomics Center for Infectious Disease (SSGCID) target BupsA.13472.b.

Deposition date: 2012-02-10 Original release date: 2012-03-19

Authors: Buchko, Garry

Citation: Buchko, Garry; Hewitt, Stephan; Napuli, Alberto; Van Voorhis, Wesley; Myler, Peter. "Solution structure of a MbtH-like protein from Burkholderia pseudomallei, the etiological agent responsible for melioidosis"  Not known ., .-..

Assembly members:
entity, polymer, 95 residues, 10805.033 Da.

Natural source:   Common Name: Burkholderia pseudomallei   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):
entity: MAHHHHHHMGTLEAQTQGPG SMDDELYFVVRNNEGQYSVW MDGRSLPAGWETVGEPATKQ QCLQRIEQLWTDMVPASVRE HLNQHSGPGIDYAVR

Data sets:
Data typeCount
13C chemical shifts339
15N chemical shifts84
1H chemical shifts517

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MbtH-like protein1

Entities:

Entity 1, MbtH-like protein 95 residues - 10805.033 Da.

The first 21 residues, MAHHHHHHMGTLEAQTQGPGS-,are non-native residue used to facilitate protein purification.

1   METALAHISHISHISHISHISHISMETGLY
2   THRLEUGLUALAGLNTHRGLNGLYPROGLY
3   SERMETASPASPGLULEUTYRPHEVALVAL
4   ARGASNASNGLUGLYGLNTYRSERVALTRP
5   METASPGLYARGSERLEUPROALAGLYTRP
6   GLUTHRVALGLYGLUPROALATHRLYSGLN
7   GLNCYSLEUGLNARGILEGLUGLNLEUTRP
8   THRASPMETVALPROALASERVALARGGLU
9   HISLEUASNGLNHISSERGLYPROGLYILE
10   ASPTYRALAVALARG

Samples:

sample_1: MbtH, [U-99% 13C; U-99% 15N], 1.0 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.1 mM; H2O 93%; D2O 7%

sample_2: MbtH, [U-99% 15N], 1.0 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.1 mM; D2O 100%

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
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
deuterium exchangesample_2isotropicsample_conditions_1

Software:

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

FELIX v2007, Accelrys Software Inc. - processing

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

SPARKY v3.115, Goddard - data analysis, peak picking

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Varian VNMRS 750 MHz
  • Varian INOVA 600 MHz

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