BMRB Entry 15814

Title:
1H, 13C and 15N resonance assignments of the domain 5 of ABP-120 from Dictyostelium in native and 8M urea-denatured states.
Deposition date:
2008-06-22
Original release date:
2009-01-06
Authors:
Hsu, Shang-Te Danny; Cabrita, Lisa; Christodoulou, John; Dobson, Christopher
Citation:

Citation: Hsu, Shang-Te Danny; Cabrita, Lisa; Christodoulou, John; Dobson, Christopher. "1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states"  Biomol. NMR Assignments 3, 29-31 (2009).
PubMed: 19636940

Assembly members:

Assembly members:
Domain_5_of_Dictyostelium_ABP-120, polymer, 108 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: N/A

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts688
15N chemical shifts192
1H chemical shifts819

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Domain 5 of ABP-1201

Entities:

Entity 1, Domain 5 of ABP-120 108 residues - Formula weight is not available

1   METTHRVALLYSPROALAPROSERALAGLU
2   HISSERTYRALAGLUGLYGLUGLYLEUVAL
3   LYSVALPHEASPASNALAPROALAGLUPHE
4   THRILEPHEALAVALASPTHRLYSGLYVAL
5   ALAARGTHRASPGLYGLYASPPROPHEGLU
6   VALALAILEASNGLYPROASPGLYLEUVAL
7   VALASPALALYSVALTHRASPASNASNASP
8   GLYTHRTYRGLYVALVALTYRASPALAPRO
9   VALGLUGLYASNTYRASNVALASNVALTHR
10   LEUARGGLYASNPROILELYSASNMETPRO
11   ILEASPVALLYSCYSILEGLUGLY

Samples:

sample_1: Domain 5 of Dictyostelium ABP-120, [U-98% 13C; U-98% 15N], 0.4 mM; D2O 5%; H2O 95%; DTT 2 mM; HEPES 10 mM; urea 8 M

sample_2: Domain 5 of Dictyostelium ABP-120, [U-98% 13C; U-98% 15N], 0.4 mM; beta-mercaptoethanol 2 mM; potassium phosphate 20 mM; D2O 5%; H2O 95%

298K: ionic strength: 0.14 M; pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropic298K
3D HNCOsample_1isotropic298K
3D HNCACBsample_1isotropic298K
3D CBCA(CO)NHsample_1isotropic298K
3D HN(CA)COsample_1isotropic298K
3D 1H-15N TOCSYsample_1isotropic298K
(H)N(COCA)NHsample_1isotropic298K
2D 1H-15N HSQCsample_2isotropic298K
3D HNCOsample_2isotropic298K
3D HNCACBsample_2isotropic298K
3D CBCA(CO)NHsample_2isotropic298K
3D HN(CA)COsample_2isotropic298K
3D 1H-15N TOCSYsample_2isotropic298K
(H)N(COCA)NHsample_2isotropic298K
2D 1H-13C HSQCsample_2isotropic298K
3D HCCH-TOCSYsample_2isotropic298K
3D HBHA(CO)NHsample_2isotropic298K
3D HCCH-COSYsample_2isotropic298K

Software:

SPARKY v3.1, Goddard - data analysis

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

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
EMBL P13466

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