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 16703

Title: SPI2

Deposition date: 2010-02-03 Original release date: 2012-08-03

Authors: Lenarcic, Martina; Kludkiewicz, Barbara; Nowicka, Ursula; Grzelak, Krystina; Zagorski-Ostoja, Wlodzimierz; Zhukov, Igor

Citation: Lenarcic, Martina; Grzelak, Krystina; Zhukov, Igor; Zagorski-Ostoja, Wlodzimierz; Nowicka, Ursula. "High-resolution structure of atypical serine proteinase inhibitors by means of NMR spectroscopy"  Not known ., .-..

Assembly members:
spi2, polymer, 45 residues, 5033.501 Da.

Natural source:   Common Name: greater wax moth   Taxonomy ID: 7137   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Galleria Mellonella

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris

Entity Sequences (FASTA):
spi2: EAAVCTTEWDPVCGKDGKTY SNLCWLNEAGVGLDHEGECH HHHHH

Data sets:
Data typeCount
13C chemical shifts111
15N chemical shifts38
1H chemical shifts244

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1spi21

Entities:

Entity 1, spi2 45 residues - 5033.501 Da.

additional two residues (EA) on N-termini; His-Tag6 on C-termini

1   GLUALAALAVALCYSTHRTHRGLUTRPASP
2   PROVALCYSGLYLYSASPGLYLYSTHRTYR
3   SERASNLEUCYSTRPLEUASNGLUALAGLY
4   VALGLYLEUASPHISGLUGLYGLUCYSHIS
5   HISHISHISHISHIS

Samples:

sample_1: spi2 1.2 mM; H2O 90%; D2O 10%; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 3.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz
  • Varian UnityPlus 500 MHz

Related Database Links:

BMRB 16704 16705 19085
PDB
GB AAK48526

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts