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 19042

Title: Complete 1H, 13C, and 15N Chemical Shift Assignments for Burkholderia pseudomallei Frataxin like protein   PubMed: 23616103

Deposition date: 2013-02-19 Original release date: 2013-08-14

Authors: Gaudesi, Davide; Musco, Giovanna; Quilici, Giacomo

Citation: Gaudesi, Davide; Quilici, Giacomo; Musco, Giovanna. "1H, 13C, and 15N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei."  Biomol. NMR Assignments 8, 181-184 (2014).

Assembly members:
Frataxin_like, polymer, 130 residues, 12240 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):
Frataxin_like: GAMGMSPDTARRFDTEFAPR IARAIADLLNHRAHTDVVGY GGHGHPTQVRIVAPHAEHVR GYAHPLNLALTWNTDEIERL MEADGAARFERYLAALPRKL AAWENARGVDFGSRTQADAL VLLGGLDFEA

Data sets:
Data typeCount
13C chemical shifts365
15N chemical shifts121
1H chemical shifts852

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Frataxin like monomer1

Entities:

Entity 1, Frataxin like monomer 130 residues - 12240 Da.

Residue 1-4 represent a non-native affinity tag residual sequence.

1   GLYALAMETGLYMETSERPROASPTHRALA
2   ARGARGPHEASPTHRGLUPHEALAPROARG
3   ILEALAARGALAILEALAASPLEULEUASN
4   HISARGALAHISTHRASPVALVALGLYTYR
5   GLYGLYHISGLYHISPROTHRGLNVALARG
6   ILEVALALAPROHISALAGLUHISVALARG
7   GLYTYRALAHISPROLEUASNLEUALALEU
8   THRTRPASNTHRASPGLUILEGLUARGLEU
9   METGLUALAASPGLYALAALAARGPHEGLU
10   ARGTYRLEUALAALALEUPROARGLYSLEU
11   ALAALATRPGLUASNALAARGGLYVALASP
12   PHEGLYSERARGTHRGLNALAASPALALEU
13   VALLEULEUGLYGLYLEUASPPHEGLUALA

Samples:

not_labeled: Frataxin like; potassium phosphate, [U-100% 1H], 0.6 mM; potassium phosphate 20 mM; sodium chloride 150 mM; DTT 2 mM

15N_H2O: Frataxin like, [U-99% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 150 mM; DTT 2 mM

15N_13C: Frataxin like, [U-99% 13C; U-99% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 150 mM; DTT 2 mM

15N_D2O: Frataxin like, [U-99% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 150 mM; DTT 2 mM

15N_13C_D2O: Frataxin like, [U-99% 13C; U-99% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 150 mM; DTT 2 mM

not_labeled_D2O: Frataxin like, [U-100% 1H], 0.6 mM; potassium phosphate 20 mM; sodium chloride 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYnot_labeledisotropicsample_conditions_1
2D 1H-1H NOESYnot_labeledisotropicsample_conditions_1
2D 1H-1H TOCSYnot_labeled_D2Oisotropicsample_conditions_1
2D 1H-1H NOESYnot_labeled_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC15N_H2Oisotropicsample_conditions_1
2D 1H-15N HSQC15N_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic15N_13C_D2Oisotropicsample_conditions_1
2D 1H-13C HSQC aromatic15N_13C_D2Oisotropicsample_conditions_1
3D CBCA(CO)NH15N_13Cisotropicsample_conditions_1
3D HNCACB15N_13Cisotropicsample_conditions_1
3D HNCA15N_13Cisotropicsample_conditions_1
3D H(CCO)NH15N_13Cisotropicsample_conditions_1
3D HNCO15N_H2Oisotropicsample_conditions_1
3D HNHA15N_H2Oisotropicsample_conditions_1
3D C(CO)NH15N_13C_D2Oisotropicsample_conditions_1
3D 1H-15N NOESY15N_13Cisotropicsample_conditions_1
3D 1H-13C NOESY15N_13C_D2Oisotropicsample_conditions_1
hbCBcgcdHD15N_13C_D2Oisotropicsample_conditions_1
3D HCCH-TOCSY15N_13C_D2Oisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

Analysis, CCPN - chemical shift assignment, collection, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP Q63W39
PDB
EMBL CAH35046 CDU27687 CFB50711 CFD85665 CFD91967
GB AAU48433 ABA47781 ABM50277 ABN00967 ABN84691
REF WP_004192184 WP_004534344 WP_004550752 WP_004555425 WP_009919325

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