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 16913

Title: The solution structure of the squash aspartic acid proteinase inhibitor (SQAPI)   PubMed: 20538608

Deposition date: 2010-05-05 Original release date: 2010-07-26

Authors: Headey, Stephen; MacAskill, Ursula; Wright, Michelle; Claridge, Jolyon; Edwards, Patrick; Farley, Peter; Christeller, John; Laing, William; 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, 10421.041 Da.

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

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

Data sets:
Data typeCount
13C chemical shifts421
1H chemical shifts674

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SQAPI1

Entities:

Entity 1, SQAPI 95 residues - 10421.041 Da.

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-98% 13C; U-98% 15N], 0.6 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 3; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HCCCONH TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D 1H-13C NOESYHSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYHSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - processing

XEASY v1.4, Bartels et al. - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 15483
PDB
GB AAC39473 AAT67162 ABB96300 ABB96305 ABB96307