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 15483

Title: SQAPI   PubMed: 20538608

Deposition date: 2007-09-23 Original release date: 2010-08-16

Authors: Macaskill, Ursula; Farley, Peter; Pascal, Steven

Citation: Headey, Stephen; Macaskill, Ursula; Wright, Michele; Claridge, Jolyon; Edwards, Patrick; Farley, Peter; Christeller, John; Laing, William; Pascal, Steven. "Solution Structure of the Squash Aspartic Acid Proteinase Inhibitor (SQAPI) and Mutational Analysis of Pepsin Inhibition."  J. Biol. Chem. 285, 27019-27025 (2010).

Assembly members:
SQAPI, polymer, 95 residues, Formula weight is not available

Natural source:   Common Name: winter squash   Taxonomy ID: 3661   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Cucurbita maxima

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRSET/30.2/18

Entity Sequences (FASTA):
SQAPI: GPGPAIGEVIGISVNDPRVK EIAEFALKQHAEQNLILAGV DAGQIIKGIPHWDNYYNLIL SAKHSPHEFSKFYNVVVLEK ASDNSLKLVAFVPLF

Data sets:
Data typeCount
13C chemical shifts405
15N chemical shifts90
1H chemical shifts665

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1SQAPI1

Entities:

Entity 1, SQAPI 95 residues - Formula weight is not available

1   GLYPROGLYPROALAILEGLYGLUVALILE
2   GLYILESERVALASNASPPROARGVALLYS
3   GLUILEALAGLUPHEALALEULYSGLNHIS
4   ALAGLUGLNASNLEUILELEUALAGLYVAL
5   ASPALAGLYGLNILEILELYSGLYILEPRO
6   HISTRPASPASNTYRTYRASNLEUILELEU
7   SERALALYSHISSERPROHISGLUPHESER
8   LYSPHETYRASNVALVALVALLEUGLULYS
9   ALASERASPASNSERLEULYSLEUVALALA
10   PHEVALPROLEUPHE

Samples:

sample_1: SQAPI, [U-13C; U-15N], 0.6 mM

sample_2: SQAPI, [U-15N], 0.2 mM

sample_3: SQAPI, [U-13C; U-15N], 0.15 mM

sample_conditions_1: ionic strength: 0.001 M; pH: 3; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16913
PDB
GB AAC39473 AAT67162 ABB96300 ABB96305 ABB96307

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