BMRB Entry 12020

Title:
1H and 15N Chemical Shifts Assignment for wild-type SPINK1
Deposition date:
2018-06-01
Original release date:
2019-02-07
Authors:
Sebak, Fanni; Bodor, Andrea
Citation:

Citation: Boros, Eszter; Sebak, Fanni; Heja, David; Szakacs, David; Zboray, Katalin; Schlosser, Gitta; Micsonai, Andras; Kardos, Jozsef; Bodor, Andrea; Pal, Gabor. "Directed Evolution of Canonical Loops and Their Swapping between Unrelated Serine Proteinase Inhibitors Disprove the Interscaffolding Additivity Model"  J. Mol. Biol. 431, 557-575 (2019).
PubMed: 30543823

Assembly members:

Assembly members:
wild-type_SPINK1, polymer, 59 residues, Formula weight is not available

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: M13KO7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
wild-type_SPINK1: GSGDSLGREAKCYNELNGCT KIYDPVCGTDGNTYPNECVL CFENRKRQTSILIQKSGPC

Data sets:
Data typeCount
15N chemical shifts45
1H chemical shifts292

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SPINK11

Entities:

Entity 1, SPINK1 59 residues - Formula weight is not available

Residues -2-0 represent a cloning artifact.

1   GLYSERGLYASPSERLEUGLYARGGLUALA
2   LYSCYSTYRASNGLULEUASNGLYCYSTHR
3   LYSILETYRASPPROVALCYSGLYTHRASP
4   GLYASNTHRTYRPROASNGLUCYSVALLEU
5   CYSPHEGLUASNARGLYSARGGLNTHRSER
6   ILELEUILEGLNLYSSERGLYPROCYS

Samples:

sample_1: wild-type SPINK1 1 mM; sodium phosphate 50 mM; DSS 5 uL; H2O 450 uL; D2O, [U-2H], 50 uL

sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avence 700 MHz

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