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 18416

Title: 1H,15N and 13C backbone and side chain chemical shifts of the ubiquitin homology domain of mouse BAG-1   PubMed: 22903788

Deposition date: 2012-04-24 Original release date: 2012-09-14

Authors: Huang, Hsiao Wen; Yu, Chin

Citation: Huang, Hsiao-Wen; Yu, Chin. "Backbone and side-chain resonance assignments (1H, 15N and 13C) of the ubiquitin homology domain of mouse BAG-1."  Biomol. NMR Assignments 7, 235-239 (2013).

Assembly members:
ubiquitin_homology_domain_of_mouse_BAG-1, polymer, 97 residues, Formula weight is not available

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
ubiquitin_homology_domain_of_mouse_BAG-1: MAKTEEMVQTEEMETPRLSV IVTHSNERYDLLVTPQQGNS EPVVQDLAQLVEEATGVPLP FQKLIFKGKSLKEMETPLSA LGMQNGCRVMLIGEKSN

Data sets:
Data typeCount
13C chemical shifts383
15N chemical shifts96
1H chemical shifts634

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ubiquitin homology of mouse BAG-11

Entities:

Entity 1, ubiquitin homology of mouse BAG-1 97 residues - Formula weight is not available

1   METALALYSTHRGLUGLUMETVALGLNTHR
2   GLUGLUMETGLUTHRPROARGLEUSERVAL
3   ILEVALTHRHISSERASNGLUARGTYRASP
4   LEULEUVALTHRPROGLNGLNGLYASNSER
5   GLUPROVALVALGLNASPLEUALAGLNLEU
6   VALGLUGLUALATHRGLYVALPROLEUPRO
7   PHEGLNLYSLEUILEPHELYSGLYLYSSER
8   LEULYSGLUMETGLUTHRPROLEUSERALA
9   LEUGLYMETGLNASNGLYCYSARGVALMET
10   LEUILEGLYGLULYSSERASN

Samples:

sample_1: ubiquitin homology domain of mouse BAG-1, [U-100% 13C; U-100% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

VNMR, Varian - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian VNMR 700 MHz

Related Database Links:

PDB
DBJ BAB26106
GB AAC34259 AAH03722 AAH69918 AAH93509 EDL05422
REF NP_001165210 NP_033866
SP Q60739

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