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 11542

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for yeast Tim50 PBD domain   PubMed: 24462684

Deposition date: 2013-11-12 Original release date: 2014-03-25

Authors: Rahman, Bytul; Anzai, Takahiro; Kawano, Shin; Endo, Toshiya

Citation: Rahman, Bytul; Kawano, Shin; Esaki, Kaori; Anzai, Takahiro; Endo, Toshiya. "NMR analyses on the interactions of the yeast Tim50 C-terminal region with the presequence and Tim50 core domain."  FEBS Lett. 588, 678-684 (2014).

Assembly members:
Tim50_PBD, polymer, 72 residues, 8400 Da.

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   Vector: pET15b

Entity Sequences (FASTA):
Tim50_PBD: MGSSHHHHHHSSGLVPRGSH MEEGQKNYLMFMKMIEEEKE KIRIQQEQMGGQTFTLKDYV EGNLPSPEEQMK

Data sets:
Data typeCount
13C chemical shifts160
15N chemical shifts55
1H chemical shifts55

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tim50 PBD1

Entities:

Entity 1, Tim50 PBD 72 residues - 8400 Da.

Residues 379-399 represent a non-native affinity His-tag.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLUGLUGLYGLNLYSASNTYRLEUMET
4   PHEMETLYSMETILEGLUGLUGLULYSGLU
5   LYSILEARGILEGLNGLNGLUGLNMETGLY
6   GLYGLNTHRPHETHRLEULYSASPTYRVAL
7   GLUGLYASNLEUPROSERPROGLUGLUGLN
8   METLYS

Samples:

sample_1: Tim50 sPBD, [U-100% 13C; U-100% 15N], 100 uM; potassium phosphate 20 mM; potassium chloride 50 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 70 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCANNHsample_1isotropicsample_conditions_1

Software:

SPARKY v3.114, Goddard - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

DBJ GAA26910
EMBL CAY86898
GB AAB68302 AHY78114 AJP42082 AJV91172 AJV91610
REF NP_015262
SP Q02776
TPG DAA11368
AlphaFold Q02776

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