BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 18236

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18236

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Title: Backbone and sidechain 13C, 15N, and 1H assignments of cruzain in complex with K777   PubMed: 23181936

Deposition date: 2012-02-01 Original release date: 2014-04-22

Authors: Lee, Gregory; Balouch, Eamon; Craik, Charles

Citation: Lee, Gregory; Balouch, Eaman; Goetz, David; Lazic, Ana; McKerrow, James; Craik, Charles. "Mapping inhibitor binding modes on an active cysteine protease via nuclear magnetic resonance spectroscopy."  Biochemistry 51, 10087-10098 (2012).

Assembly members:
cruzain, polymer, 215 residues, 22703.2 Da.
D1R, non-polymer, 576.749 Da.

Natural source:   Common Name: Trypanosoma cruzi   Taxonomy ID: 5693   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma cruzi

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
cruzain: APAAVDWRARGAVTAVKDQG QCGSCWAFSAIGNVECQWFL AGHPLTNLSEQMLVSCDKTD SGCSGGLMNNAFEWIVQENN GAVYTEDSYPYASGEGISPP CTTSGHTVGATITGHVELPQ DEAQIAAWLAVNGPVAVAVD ASSWMTYTGGVMTSCVSEQL DHGVLLVGYNDSAAVPYWII KNSWTTQWGEEGYIRIAKGS NQCLVKEEASSAVVG

Data sets:
Data typeCount
13C chemical shifts632
15N chemical shifts182
1H chemical shifts205

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cruzain1
2D1R2

Entities:

Entity 1, cruzain 215 residues - 22703.2 Da.

residue sequence numbers match that of x-ray crystal structure of cruzain-K777 complex (2OZ2).

1   ALAPROALAALAVALASPTRPARGALAARG
2   GLYALAVALTHRALAVALLYSASPGLNGLY
3   GLNCYSGLYSERCYSTRPALAPHESERALA
4   ILEGLYASNVALGLUCYSGLNTRPPHELEU
5   ALAGLYHISPROLEUTHRASNLEUSERGLU
6   GLNMETLEUVALSERCYSASPLYSTHRASP
7   SERGLYCYSSERGLYGLYLEUMETASNASN
8   ALAPHEGLUTRPILEVALGLNGLUASNASN
9   GLYALAVALTYRTHRGLUASPSERTYRPRO
10   TYRALASERGLYGLUGLYILESERPROPRO
11   CYSTHRTHRSERGLYHISTHRVALGLYALA
12   THRILETHRGLYHISVALGLULEUPROGLN
13   ASPGLUALAGLNILEALAALATRPLEUALA
14   VALASNGLYPROVALALAVALALAVALASP
15   ALASERSERTRPMETTHRTYRTHRGLYGLY
16   VALMETTHRSERCYSVALSERGLUGLNLEU
17   ASPHISGLYVALLEULEUVALGLYTYRASN
18   ASPSERALAALAVALPROTYRTRPILEILE
19   LYSASNSERTRPTHRTHRGLNTRPGLYGLU
20   GLUGLYTYRILEARGILEALALYSGLYSER
21   ASNGLNCYSLEUVALLYSGLUGLUALASER
22   SERALAVALVALGLY

Entity 2, D1R - C32 H40 N4 O4 S - 576.749 Da.

1   D1R

Samples:

sample_1: cruzain, [U-13C; U-15N; U-2H], 500 uM; D1R 500 uM; H2O 90%; D2O 10%

sample_2: cruzain, [U-15N], 500 uM; D1R 500 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.02 M; pH: 5.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

SPARKY v3.0, Goddard - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

GB 2OZ2_A AAA30181 AAB41118 AAB41119 AAC00067 AAF75546
PDB
DBJ BAA96735 BAA96736 BAA96737
REF XP_804236 XP_805951 XP_818578 XP_818579 XP_820174
SP P25779

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