BMRB Entry 52004

Name: Identifying structural and dynamics changes during the Biliverdin Reductase B catalytic cycle
Published: 2023-09-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52004

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAVKKIAIFGATGQTGLTTL AQAVQAGYEVTVLVRDSSRL PSEGPRPAHVVVGDVLQAAD VDKTVAGQDAVIVLLGTRND LSPTTVMSEGARNIVAAMKA HGVDKVVACTSAFLLWDPTK VPPRLQAVTDDHIRMHKVLR ESGLKYVAVMPPHIGDQPLT GAYTVTLDGRGPSRVISKHD LGHFMLRCLTTDEYDGHSTY PSHQYQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	271
15N chemical shifts	182
1H chemical shifts	183

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BLVRB	1
2	NADPH	2

Entities:

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

1

MET

ALA

VAL

LYS

ILE

ALA

ILE

PHE

GLY

2

ALA

THR

GLY

GLN

THR

GLY

LEU

THR

LEU

3

ALA

GLN

ALA

VAL

GLN

ALA

GLY

TYR

GLU

VAL

4

THR

VAL

LEU

VAL

ARG

ASP

SER

ARG

LEU

5

PRO

SER

GLU

GLY

PRO

ARG

PRO

ALA

HIS

VAL

6

VAL

GLY

ASP

VAL

LEU

GLN

ALA

ASP

7

VAL

ASP

LYS

THR

VAL

ALA

GLY

GLN

ASP

ALA

8

VAL

ILE

VAL

LEU

GLY

THR

ARG

ASN

ASP

9

LEU

SER

PRO

THR

VAL

MET

SER

GLU

GLY

10

ALA

ARG

ASN

ILE

VAL

ALA

MET

LYS

ALA

11

HIS

GLY

VAL

ASP

LYS

VAL

ALA

CYS

THR

12

SER

ALA

PHE

LEU

TRP

ASP

PRO

THR

LYS

13

VAL

PRO

ARG

LEU

GLN

ALA

VAL

THR

ASP

14

ASP

HIS

ILE

ARG

MET

HIS

LYS

VAL

LEU

ARG

15

GLU

SER

GLY

LEU

LYS

TYR

VAL

ALA

VAL

MET

16

PRO

HIS

ILE

GLY

ASP

GLN

PRO

LEU

THR

17

GLY

ALA

TYR

THR

VAL

THR

LEU

ASP

GLY

ARG

18

GLY

PRO

SER

ARG

VAL

ILE

SER

LYS

HIS

ASP

19

LEU

GLY

HIS

PHE

MET

LEU

ARG

CYS

LEU

THR

20

THR

ASP

GLU

TYR

ASP

GLY

HIS

SER

THR

TYR

21

PRO

SER

HIS

GLN

TYR

GLN

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_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