BMRB Entry 27463

Title:
Backbone chemical shift assignments for Holo form of Biliverdin reductase B
Deposition date:
2018-04-23
Original release date:
2018-09-18
Authors:
Paukovich, Natasia; Eisenmesser, Elan
Citation:

Citation: Paukovich, Natasia; Xue, Mengjun; Elder, James; Redzic, Jasmina; Blue, Ashley; Pike, Hamish; Miller, Brian; Pitts, Todd; Pollock, David; Hansen, Kirk; D'Alessandro, Angelo; Eisenmesser, Elan Zohar. "Biliverdin Reductase B Dynamics Are Coupled to Coenzyme Binding."  J. Mol. Biol. 430, 3234-3250 (2018).
PubMed: 29932944

Assembly members:

Assembly members:
BLVRB, polymer, 206 residues, Formula weight is not available
entity_NAP, non-polymer, 743.405 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Data sets:
Data typeCount
13C chemical shifts373
15N chemical shifts180
1H chemical shifts181

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1BLVRB1
2NADP2

Entities:

Entity 1, BLVRB 206 residues - Formula weight is not available

1   METALAVALLYSLYSILEALAILEPHEGLY
2   ALATHRGLYGLNTHRGLYLEUTHRTHRLEU
3   ALAGLNALAVALGLNALAGLYTYRGLUVAL
4   THRVALLEUVALARGASPSERSERARGLEU
5   PROSERGLUGLYPROARGPROALAHISVAL
6   VALVALGLYASPVALLEUGLNALAALAASP
7   VALASPLYSTHRVALALAGLYGLNASPALA
8   VALILEVALLEULEUGLYTHRARGASNASP
9   LEUSERPROTHRTHRVALMETSERGLUGLY
10   ALAARGASNILEVALALAALAMETLYSALA
11   HISGLYVALASPLYSVALVALALACYSTHR
12   SERALAPHELEULEUTRPASPPROTHRLYS
13   VALPROPROARGLEUGLNALAVALTHRASP
14   ASPHISILEARGMETHISLYSVALLEUARG
15   GLUSERGLYLEULYSTYRVALALAVALMET
16   PROPROHISILEGLYASPGLNPROLEUTHR
17   GLYALATYRTHRVALTHRLEUASPGLYARG
18   GLYPROSERARGVALILESERLYSHISASP
19   LEUGLYHISPHEMETLEUARGCYSLEUTHR
20   THRASPGLUTYRASPGLYHISSERTHRTYR
21   PROSERHISGLNTYRGLN

Entity 2, NADP - C21 H28 N7 O17 P3 - 743.405 Da.

1   NAP

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