BMRB Entry 26301

Name: Crystal structure of higher plant heme oxygenase-1 and the mechanism of interaction with ferredoxin
Published: 2020-12-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26301

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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:

Crystal structure of higher plant heme oxygenase-1 and the mechanism of interaction with ferredoxin

Deposition date:

2020-10-05

Original release date:

2020-12-22

Authors:

Makiyama, Yuki; Konuma, Tsuyoshi; Ikegami, Takahisa

Citation:

Citation: Tohda, Rei; Tanaka, Hideaki; Mutoh, Risa; Zhang, Xuhong; Lee, Young-Ho; Konuma, Tsuyoshi; Ikegami, Takahisa; Migita, Taiko; Kurisu, Genji. "Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin" J. Biol. Chem. ., .-..

Assembly members:

Assembly members:
ferredoxin maize, polymer, 97 residues, Formula weight is not available
FE2/S2 (INORGANIC) CLUSTER, non-polymer, 175.820 Da.

Natural source:

Natural source: Common Name: Zea mays Taxonomy ID: 4577 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Zea mays

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pKK233-2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ferredoxin maize: AVYKVKLVGPEGEEHEFDAP DDAYILDAAETAGVELPYSC RAGACSTCAGKIESGSVDQS DGSFLDDGQQEEGYVLTCVS YPKSDCVIHTHKEGDLY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	210
15N chemical shifts	74
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Fd	1
2	FES	2

Entities:

Entity 1, Fd 97 residues - Formula weight is not available

1

ALA

VAL

TYR

LYS

VAL

LYS

LEU

VAL

GLY

PRO

2

GLU

GLY

GLU

HIS

GLU

PHE

ASP

ALA

PRO

3

ASP

ALA

TYR

ILE

LEU

ASP

ALA

GLU

4

THR

ALA

GLY

VAL

GLU

LEU

PRO

TYR

SER

CYS

5

ARG

ALA

GLY

ALA

CYS

SER

THR

CYS

ALA

GLY

6

LYS

ILE

GLU

SER

GLY

SER

VAL

ASP

GLN

SER

7

ASP

GLY

SER

PHE

LEU

ASP

GLY

GLN

8

GLU

GLY

TYR

VAL

LEU

THR

CYS

VAL

SER

9

TYR

PRO

LYS

SER

ASP

CYS

VAL

ILE

HIS

THR

10

HIS

LYS

GLU

GLY

ASP

LEU

TYR

Entity 2, FES - Fe2 S2 - 175.820 Da.

1

FES

Samples:

sample_1: FdIII, [U-13C; U-15N], 0.5 mM; FES 0.5 mM; potassium phosphate 50 mM; potassium chloride 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 60 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRFAM-SPARKY - peak picking

NMR spectrometers:

Bruker AVANCE III 500 MHz

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