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 25994

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for designed protein E_1r26   PubMed: 27522946

Deposition date: 2016-03-12 Original release date: 2016-10-13

Authors: Zhou, Xiaoqun

Citation: Zhou, Xiaoqun; Xiong, Peng; Wang, Meng; Ma, Rongsheng; Zhang, Jiahai; Chen, Quan; Liu, Haiyan. "Proteins of well-defined structures can be designed without backbone readjustment by a statistical model."  J. Struct. Biol. 196, 350-357 (2016).

Assembly members:
E_1r26, polymer, 122 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
E_1r26: MARPSNVKPSPHVIKSLEEL REATASNRISVIVFTHPDSK RSKEIKEKLKKLAEEFPDVD IYLVDTSTNPEAREWYNITS VPTFVIEKGGEPLGEVKGPD IDKLRETLDELLARLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts311
15N chemical shifts106
1H chemical shifts591

Additional metadata:

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