BMRB Entry 27462

Title:
Backbone chemical shift assignments for Apo 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

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 shifts558
15N chemical shifts184
1H chemical shifts603

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BLVRB1

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

Samples:

apo_1: BLVRB, [U-100% 13C; U-100% 15N; U-80% 2H], 500 uM; Bis-Tris 50 mM; NaCl 50 mM; DTT 1 mM

apo_2: BLVRB, [U-100% 15N], 500 uM; Bis-Tris 50 mM; NaCl 50 mM; DTT 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HN(CO)CAapo_1isotropicsample_conditions_1
3D HNCAapo_1isotropicsample_conditions_1
3D HNCACBapo_1isotropicsample_conditions_1
3D HN(COCA)CBapo_1isotropicsample_conditions_1
3D 1H-15N NOESYapo_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz

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