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 27016

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the DHDD Region of GbnD4 KS14 from the Gladiolin Polyketide Synthase

Authors: Jenner, Matthew; Kosol, Simone; Lewandowski, Jozef; Challis, Gregory

Citation: Jenner, Matthew; Kosol, Simone; Griffiths, Daniel; Prasongpolchai, Panward; Manzi, Lucio; Barrow, Andrew; Moses, John; Oldham, Neil; Lewandowski, Jozef; Challis, Gregory; Jenner, Matthew; Kosol, Simone; Griffiths, Daniel; Prasongpolchai, Panward; Manzi, Lucio; Barrow, Andrew; Moses, John; Oldham, Neil; Lewandowski, Jozef; Challis, Gregory. "Ketosynthase Docking Domains Interact Directly with Dehydratase Domains in trans-AT Polyketide Synthase Split Modules"  Nat. Chem. Biol. ., .-..

Assembly members:
DHDD, polymer, 91 residues, Formula weight is not available

Natural source:   Common Name: Burkholderia gladioli   Taxonomy ID: 28095   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia gladioli

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

Entity Sequences (FASTA):
DHDD: MKHHHHHHHHGGLVPRGSHG SDEGVPDALRADTVPRAGPV RYARRRYWIGEARSDALAPA APLEREPLPAEAMGAYFAIR RTDADDTVAAH

Data sets:
Data typeCount
13C chemical shifts230
15N chemical shifts69
1H chemical shifts69

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Protein DHDD1

Entities:

Entity 1, Protein DHDD 91 residues - Formula weight is not available

1   METLYSHISHISHISHISHISHISHISHIS
2   GLYGLYLEUVALPROARGGLYSERHISGLY
3   SERASPGLUGLYVALPROASPALALEUARG
4   ALAASPTHRVALPROARGALAGLYPROVAL
5   ARGTYRALAARGARGARGTYRTRPILEGLY
6   GLUALAARGSERASPALALEUALAPROALA
7   ALAPROLEUGLUARGGLUPROLEUPROALA
8   GLUALAMETGLYALATYRPHEALAILEARG
9   ARGTHRASPALAASPASPTHRVALALAALA
10   HIS

Samples:

sample_1: Protein DHDD, [U-99% 13C; U-99% 15N], 0.3 mM; potassium phosphate 50 mM; sodium chloride 200 mM; DSS 50 uM

sample_conditions_1: ionic strength: 0.28 M; pH: 6.8; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - processing

CcpNMR v2.4.1, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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