BMRB Entry 19596

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19596

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
C-terminal disordered region of the pancreatic duodenal homeobox protein 1
Deposition date:
2013-11-01
Original release date:
2014-02-11
Authors:
Sahu, Debashish; Bastidas, Monique; Showalter, Scott
Citation:

Citation: Sahu, Debashish; Bastidas, Monique; Showalter, Scott. "Generating NMR chemical shift assignments of intrinsically disordered proteins using carbon-detected NMR methods."  Anal. Biochem. 449C, 17-25 (2013).
PubMed: 24333248

Assembly members:

Assembly members:
pdx1c, polymer, 83 residues, 8088.9849 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET49-b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
pdx1c: GPGEEDKKRGGGTAVGGGGV AEPEQDCAVTSGEELLALPP PPPPGGAVPPAAPVAAREGR LPPGLSASPQPSSVAPRRPQ EPR

Data sets:
Data typeCount
13C chemical shifts261
15N chemical shifts74
1H chemical shifts342

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1c-terminal of pancreatic duodenal homeobox protein 11

Entities:

Entity 1, c-terminal of pancreatic duodenal homeobox protein 1 83 residues - 8088.9849 Da.

1   GLYPROGLYGLUGLUASPLYSLYSARGGLY
2   GLYGLYTHRALAVALGLYGLYGLYGLYVAL
3   ALAGLUPROGLUGLNASPCYSALAVALTHR
4   SERGLYGLUGLULEULEUALALEUPROPRO
5   PROPROPROPROGLYGLYALAVALPROPRO
6   ALAALAPROVALALAALAARGGLUGLYARG
7   LEUPROPROGLYLEUSERALASERPROGLN
8   PROSERSERVALALAPROARGARGPROGLN
9   GLUPROARG

Samples:

sample_1: pdx1c, [U-99% 13C; U-99% 15N], 0.8 ± 0.2 mM; cacodylate buffer pH 6.5 50 mM; potassium chloride 50 mM; DTT 1 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D (HN-flip)N(CA)CONsample_1isotropicsample_conditions_1
3D (HN-flip)N(CA)NCOsample_1isotropicsample_conditions_1
2D (HN-flip)CONsample_1isotropicsample_conditions_1
2D (HACA)CONsample_1isotropicsample_conditions_1
2D CACON THRsample_1isotropicsample_conditions_1
2D CANCO THRsample_1isotropicsample_conditions_1
2D CACON TAVIsample_1isotropicsample_conditions_1
2D CANCO TAVIsample_1isotropicsample_conditions_1
2D CACON SERsample_1isotropicsample_conditions_1
2D CANCO SERsample_1isotropicsample_conditions_1
2D CACON LEU/ALAsample_1isotropicsample_conditions_1
2D CANCO LEU/ALAsample_1isotropicsample_conditions_1
2D CACON ALAsample_1isotropicsample_conditions_1
2D CANCO ALAsample_1isotropicsample_conditions_1
2D CACON GLYsample_1isotropicsample_conditions_1
2D CANCO GLYsample_1isotropicsample_conditions_1
2D CACON GLUsample_1isotropicsample_conditions_1
2D CANCO GLUsample_1isotropicsample_conditions_1
2D CANCO ASPsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

DBJ BAG74161
EMBL CAA68169
GB AAA74012 AAA88820 AAB47101 AAB88463 AAC05157
REF NP_000200 NP_001074947 XP_001096758 XP_002748960 XP_002824168
SP A1YF08 A1YG85 A2T756 P52945
AlphaFold A1YF08 A1YG85 A2T756 P52945