BMRB Entry 52004

Title:
Identifying structural and dynamics changes during the Biliverdin Reductase B catalytic cycle
Deposition date:
2023-06-16
Original release date:
2023-09-11
Authors:
Lee, Eunjeong
Citation:

Citation: Lee, Eunjeong; McLeod, Matthew; Redzic, Jasmina; Marcolin, Barbara; Thorne, Robert; Agarwal, Pratul; Eisenmesser, Elan Zohar. "Identifying structural and dynamic changes during the Biliverdin Reductase B catalytic cycle"  Front Mol Biosci 10, 1244587-1244587 (2023).
PubMed: 37645217

Assembly members:

Assembly members:
entity_1, polymer, 206 residues, Formula weight is not available
entity_NDP, non-polymer, 745.421 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: Pet 21

Data sets:
Data typeCount
13C chemical shifts271
15N chemical shifts182
1H chemical shifts183

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BLVRB1
2NADPH2

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, NADPH - C21 H30 N7 O17 P3 - 745.421 Da.

1   NDP

Samples:

sample_1: Biliverdin reductase, [U-100% 13C; U-100% 15N; U-80% 2H], 500 uM; NADP 1 mM; Bis Tris 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz

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