BMRB Entry 36154

Name: An anthrahydroquino-Gama-pyrone synthase Txn09
Published: 2025-10-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36154

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

An anthrahydroquino-Gama-pyrone synthase Txn09

Deposition date:

2018-01-11

Original release date:

2025-10-11

Authors:

Song, Y.; Cao, C.

Citation:

Citation: Hou, Xian-Feng; Song, Yu-Jiao; Zhang, Mei; Lan, Wenxian; Meng, Song; Wang, Chunxi; Pan, Hai-Xue; Cao, Chunyang; Tang, Gong-Li. "Enzymology of Anthraquinone-g-Pyrone Ring Formation in Complex Aromatic Polyketide Biosynthesis." Angew. Chem Int Ed Engl. 57, 13475-13479 (2018).
PubMed: 30151879

Assembly members:

Assembly members:
TxnO9, polymer, 154 residues, 17451.539 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 42235 Superkingdom: Bacteria Kingdom: Bacillati Genus/species: Streptomyces bottropensis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TxnO9: MPEEIPDVRKSVVVAASVEH CFEVFTSRPADWWPPSHVLV KKERAGLAFEPFVGGRYYEW DIDGTEIVWGRILEWDPPHR LAMTWRIDGHWQSVPDDDRA SEIEVDFVPNGSGGTRVELA HVKLHRHGDGAWNIHKALDG PSPGETLARFANVI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	632
15N chemical shifts	140
1H chemical shifts	994

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 154 residues - 17451.539 Da.

1

MET

PRO

GLU

ILE

PRO

ASP

VAL

ARG

LYS

2

SER

VAL

ALA

SER

VAL

GLU

HIS

3

CYS

PHE

GLU

VAL

PHE

THR

SER

ARG

PRO

ALA

4

ASP

TRP

PRO

SER

HIS

VAL

LEU

VAL

5

LYS

GLU

ARG

ALA

GLY

LEU

ALA

PHE

GLU

6

PRO

PHE

VAL

GLY

ARG

TYR

GLU

TRP

7

ASP

ILE

ASP

GLY

THR

GLU

ILE

VAL

TRP

GLY

8

ARG

ILE

LEU

GLU

TRP

ASP

PRO

HIS

ARG

9

LEU

ALA

MET

THR

TRP

ARG

ILE

ASP

GLY

HIS

10

TRP

GLN

SER

VAL

PRO

ASP

ARG

ALA

11

SER

GLU

ILE

GLU

VAL

ASP

PHE

VAL

PRO

ASN

12

GLY

SER

GLY

THR

ARG

VAL

GLU

LEU

ALA

13

HIS

VAL

LYS

LEU

HIS

ARG

HIS

GLY

ASP

GLY

14

ALA

TRP

ASN

ILE

HIS

LYS

ALA

LEU

ASP

GLY

15

PRO

SER

PRO

GLY

GLU

THR

LEU

ALA

ARG

PHE

16

ALA

ASN

VAL

ILE

Samples:

sample_1: Txn09, [U-99% 13C; U-99% 15N], 0.7 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 60 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	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 HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	not available
2D 1H-13C HSQC aliphatic	sample_1	isotropic	not available
2D 1H-15N HSQC	sample_1	isotropic	not available
3D HCCH-TOCSY	sample_1	isotropic	not available
3D 1H-15N NOESY	sample_1	isotropic	not available
3D 1H-13C NOESY	sample_1	isotropic	not available
3D 1H-13C NOESY aliphatic	sample_1	isotropic	not available

Software:

CNS, Brunger A. T. et.al. - refinement

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking

NMR spectrometers:

Agilent DD2 700 MHz
Agilent DD2 600 MHz

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