BMRB Entry 52643

Title:
hyrax with NADP+
Deposition date:
2024-10-17
Original release date:
2025-01-09
Authors:
Lee, Eunjeong
Citation:

Citation: Lee, Eunjeong; Redzic, Jasmina; Eisenmesser, Elan Zohar. "Evolutionary Adaptations in Biliverdin Reductase B: Insights into Coenzyme Dynamics and Catalytic Efficiency"  Int. J. Mol. Sci. 25, 13233-13233 (2024).
PubMed: 39768998

Assembly members:

Assembly members:
entity_1, polymer, 206 residues, Formula weight is not available
entity_NAP, non-polymer, 743.405 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 shifts380
15N chemical shifts191
1H chemical shifts191

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hyrax BLVRB1
2NADP2

Entities:

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

1   METALAVALLYSLYSILEALAILEPHEGLY
2   ALATHRGLYMETTHRGLYLEUTHRTHRLEU
3   ALAGLNALAVALLYSALAGLYTYRGLUVAL
4   THRVALLEUVALARGASNPROSERLYSLEU
5   PROSERGLUGLYPROGLNPROALAHISVAL
6   ILEVALGLYASPVALLEULYSALAASPASP
7   VALASPLYSTHRVALALAGLYGLNASPALA
8   VALVALVALLEULEUGLYTHRGLYASNASP
9   LEUSERPROTHRTHRVALMETSERGLUGLY
10   ALAARGASNILEVALALAALAMETLYSALA
11   HISGLYVALASPLYSVALVALALACYSTHR
12   SERALAPHELEULEUTRPASPPROALALYS
13   VALPROSERARGLEUGLNASPVALTHRASP
14   ASPHISILEARGMETHISLYSVALLEUGLN
15   GLUSERGLYLEULYSTYRVALALAVALMET
16   PROPROHISILEGLYASPGLNPROLEUTHR
17   LYSALATYRSERVALTHRLEUASPGLYARG
18   GLYPROSERARGVALILESERLYSHISASP
19   LEUGLYHISPHEMETLEUGLNCYSLEUTHR
20   THRASPLYSTYRASPGLYHISSERALATYR
21   PROCYSHISGLUTYRASN

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

1   NAP

Samples:

sample_1: hyrax BLVRB mM; D2O, [U-100% 2H], 10%; sodium chloride 50 mM; Bis Tris 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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