BMRB Entry 25691

Title:
The solution structure of the kallikrein inhibitor SPINK6
Deposition date:
2015-07-06
Original release date:
2016-03-14
Authors:
Groetzinger, Joachim
Citation:

Citation: Jung, Sascha; Fischer, Jan; Spudy, Bjorn; Kerkow, Tim; Sonnichsen, Frank; Xue, Li; Bonvin, Alexandre; Goettig, Peter; Magdolen, Viktor; Meyer-Hoffert, Ulf; Groetzinger, Joachim. "The solution structure of the kallikrein-related peptidases inhibitor SPINK6"  Biochem. Biophys. Res. Commun. 471, 103-108 (2016).
PubMed: 26828269

Assembly members:

Assembly members:
entity, polymer, 57 residues, 6077.895 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: pet32a

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts55
1H chemical shifts263

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 57 residues - 6077.895 Da.

1   GLNGLYGLYGLNVALASPCYSGLYGLUPHE
2   GLNASPTHRLYSVALTYRCYSTHRARGGLU
3   SERASNPROHISCYSGLYSERASPGLYGLN
4   THRTYRGLYASNLYSCYSALAPHECYSLYS
5   ALAILEVALLYSSERGLYGLYLYSILESER
6   LEULYSHISPROGLYLYSCYS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 mM; Phosphat 10 mM; NaCl 150 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA, G??ntert P. - refinement

NMR spectrometers:

  • Bruker AMX 600 MHz

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