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 27081

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27081
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Title: 1H, 13C, and 15N backbone and side chain resonance assignments for a structured domain in atg32   PubMed: 28766175

Deposition date: 2017-04-22 Original release date: 2017-11-16

Authors: Xia, Xue; Pellegrini, Maria; Ragusa, Michael

Citation: Xia, Xue; Pellegrini, Maria; Ragusa, Michael. "Backbone and side chain resonance assignments for a structured domain within Atg32"  Biomol. NMR Assignments 11, 211-214 (2017).

Assembly members:
atg32, polymer, 145 residues, Formula weight is not available

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
atg32: SNATNSFVMPKLSLTQKNPV FRLLILGRTGSSFYQSIPKE YQSLFELPKYHDSATFPQYT GIVIIFQELREMVSLLNRIV QYSQGKPVIPIcQPGQVIQV KNVLKSFLRNKLVKLLFPPV VVTNKRDLKKMFQRLQDLSL EYGED

Data sets:
Data typeCount
13C chemical shifts603
15N chemical shifts140
1H chemical shifts1040

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1atg321

Entities:

Entity 1, atg32 145 residues - Formula weight is not available

1   SERASNALATHRASNSERPHEVALMETPRO
2   LYSLEUSERLEUTHRGLNLYSASNPROVAL
3   PHEARGLEULEUILELEUGLYARGTHRGLY
4   SERSERPHETYRGLNSERILEPROLYSGLU
5   TYRGLNSERLEUPHEGLULEUPROLYSTYR
6   HISASPSERALATHRPHEPROGLNTYRTHR
7   GLYILEVALILEILEPHEGLNGLULEUARG
8   GLUMETVALSERLEULEUASNARGILEVAL
9   GLNTYRSERGLNGLYLYSPROVALILEPRO
10   ILECYSGLNPROGLYGLNVALILEGLNVAL
11   LYSASNVALLEULYSSERPHELEUARGASN
12   LYSLEUVALLYSLEULEUPHEPROPROVAL
13   VALVALTHRASNLYSARGASPLEULYSLYS
14   METPHEGLNARGLEUGLNASPLEUSERLEU
15   GLUTYRGLYGLUASP

Samples:

sample_1: atg32, [U-99% 13C; U-99% 15N], 750 uM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.2 mM

sample_2: atg32 370 uM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.2 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Ascend 850 MHz

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