BMRB Entry 19464

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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/BMR19464
MolProbity Validation Chart

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Title:
NMR structure of the HicA toxin from Burkholderia pseudomallei
Deposition date:
2013-08-28
Original release date:
2014-02-12
Authors:
Higman, Victoria; Butt, Aaron; Hemsley, Claudia; Harmer, Nicholas; Crump, Matthew; Titball, Richard; Williams, C.
Citation:

Citation: Butt, Aaron; Higman, Victoria; Williams, Christopher; Crump, Matthew; Hemsley, Claudia; Harmer, Nicholas; Titball, Richard. "The HicA toxin from Burkholderia pseudomallei has a role in persister cell formation."  Biochem. J. ., .-. (2014).
PubMed: 24502667

Assembly members:

Assembly members:
HicA, polymer, 66 residues, 7321.6006 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET26-b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HicA: DRTGSELMNSSKLIRMLEED GWRLVRVTGSAHHFKHPKKP GLVTVPHPKKDLPIGTVKSI QKSAGL

Data sets:
Data typeCount
13C chemical shifts176
15N chemical shifts50
1H chemical shifts345

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1HicA1

Entities:

Entity 1, HicA 66 residues - 7321.6006 Da.

1   ASPARGTHRGLYSERGLULEUMETASNSER
2   SERLYSLEUILEARGMETLEUGLUGLUASP
3   GLYTRPARGLEUVALARGVALTHRGLYSER
4   ALAHISHISPHELYSHISPROLYSLYSPRO
5   GLYLEUVALTHRVALPROHISPROLYSLYS
6   ASPLEUPROILEGLYTHRVALLYSSERILE
7   GLNLYSSERALAGLYLEU

Samples:

HicA1H15N: HicA, [U-98% 13C; U-98% 15N], 1.0 mM

HicA1H15N13C: HicA, [U-98% 13C; U-98% 15N], 1.0 mM

HicA1H: HicA, [U-98% 13C; U-98% 15N], 1.0 mM; NaCl 150.0 mM; sodium phosphate 20.0 mM

sample_new_3: HicA, [U-98% 13C; U-98% 15N], 1.0 mM; NaCl 150.0 mM; sodium phosphate 20.0 mM

25C: pH: 7.400; pressure: 1.000 atm; temperature: 298.000 K

20C: pH: 7.400; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYHicA1H15Nisotropic25C
3D 1H-15N TOCSYHicA1H15Nisotropic25C
HNHA (H{[N]+[HA]})HicA1H15Nisotropic25C
3D HNCAHicA1H15N13Cisotropic25C
2D 1H-15N HSQC/HMQCHicA1H15Nisotropic25C
2D 1H-13C HSQC/HMQCHicA1H15N13Cisotropic25C
3D 1H-13C NOESYHicA1H15N13Cisotropic25C
3D HNCOHicA1H15N13Cisotropic25C
3D HCCH-TOCSYHicA1H15N13Cisotropic25C
2D 1H-1H NOESYHicA1Hisotropic20C
3D 1H-13C NOESYHicA1H15N13Cisotropic25C
HNHAsample_new_3solution20C

Software:

ARIA v2.3, RIEPING W., HABECK M., BARDIAUX B., BERNARD A.,MALLIAVIN T.E., NILGES M. - NOE Assignment, Structure Calculation, Water Refinement

AutoDep v4.3 -

CING v-, Doreleijers, Sousa da Silva, Krieger, Nabuurs, Spronk, Stevens, Vranken, Vriend, Vuister - Structure and Restraint Validation

ANALYSIS v2.2, CCPN - Peak Picking, Refinement, Resonance Assignment

DANGLE v1.1, Cheung, Maguire, Stevens, Broadhurst - Dihedral Angle Prediction from Chemical Shifts

NMRPipe v-, Frank Delaglio - Spectral Processing

PSVS v1.4, Bhattacharya, Tejero, Montelione - Structure Validation

PyRPF v0.4, CCPN - Restraint Validation

NMR spectrometers:

  • Varian VNMRS 600 MHz

Related Database Links:

UNP Q63NA6_BURPS
PDB
EMBL CAH37841
GB ABC36086
REF WP_009893919 YP_110413
AlphaFold Q63NA6

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