BMRB Entry 30677

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30677
MolProbity Validation Chart

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Title:
Solution structure of an organic hydroperoxide resistance protein from Burkholderia pseudomallei. Seattle Structural Genomics Center for Infectious Disease target BupsA.00074.a.
Deposition date:
2019-09-29
Original release date:
2019-10-14
Authors:
Buchko, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID
Citation:

Citation: Buchko, G.; Hewitt, S.; Napuli, A.; Van Voorhis, W.; Myler, P.. "Backbone and side chain (1)H, (13)C, and (15)N NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei."  Biomol. NMR Assign. 3, 163-166 (2009).
PubMed: 19888681

Assembly members:

Assembly members:
entity_1, polymer, 139 residues, 14413.182 Da.

Natural source:

Natural source:   Common Name: Burkholderia pseudomallei   Taxonomy ID: 320372   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia pseudomallei

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MNILYKTAATSTGGRDGRAT SHDQKLDVKLSAPRELGGAG AEGTNPEQLFAAGYSACFLS AMKFVAGQNKQTLPADTTVT AEVGIGPNEEGGFALDVELR VALPGLDAAAAKTLVDRAHH VCPYSNATRNNVAVRLVVA

Data sets:
Data typeCount
13C chemical shifts482
15N chemical shifts134
1H chemical shifts780

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 139 residues - 14413.182 Da.

1   METASNILELEUTYRLYSTHRALAALATHR
2   SERTHRGLYGLYARGASPGLYARGALATHR
3   SERHISASPGLNLYSLEUASPVALLYSLEU
4   SERALAPROARGGLULEUGLYGLYALAGLY
5   ALAGLUGLYTHRASNPROGLUGLNLEUPHE
6   ALAALAGLYTYRSERALACYSPHELEUSER
7   ALAMETLYSPHEVALALAGLYGLNASNLYS
8   GLNTHRLEUPROALAASPTHRTHRVALTHR
9   ALAGLUVALGLYILEGLYPROASNGLUGLU
10   GLYGLYPHEALALEUASPVALGLULEUARG
11   VALALALEUPROGLYLEUASPALAALAALA
12   ALALYSTHRLEUVALASPARGALAHISHIS
13   VALCYSPROTYRSERASNALATHRARGASN
14   ASNVALALAVALARGLEUVALVALALA

Samples:

sample_1: TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; B74, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM

sample_2: TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; B74, 99% 13C; U-99% 15N; 50%-2H]], 1 ± 0.2 mM

sample_3: TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; B74, 99% 13C; U-99% 15N], 1 ± 0.2 mM

sample_4: TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; B74, [U-10% 13C; U-99% 15N], 1 ± 0.2 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

Felix v2007, Accelrys Software Inc. - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

Sparky v3.115, Goddard - chemical shift assignment, data analysis, peak picking

TALOS v+, Cornilescu, Delaglio and Bax - data analysis

PSVS v1.5, Bhattacharya and Montelione - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

  • Bruker AVANCE II 750 MHz
  • Varian VXRS 750 MHz
  • Varian VXRS 600 MHz

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