BMRB Entry 27016

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the DHDD Region of GbnD4 KS14 from the Gladiolin Polyketide Synthase
Published: 2017-12-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27016

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the DHDD Region of GbnD4 KS14 from the Gladiolin Polyketide Synthase

Deposition date:

2017-01-27

Original release date:

2017-12-12

Authors:

Jenner, Matthew; Kosol, Simone; Lewandowski, Jozef; Challis, Gregory

Citation:

Citation: Jenner, Matthew; Kosol, Simone; Griffiths, Daniel; Prasongpolchai, Panward; Manzi, Lucio; Barrow, Andrew; Moses, John; Oldham, Neil; Lewandowski, Jozef; Challis, Gregory. "Mechanism of intersubunit ketosynthase-dehydratase interaction in polyketide synthases" Nat. Chem. Biol. 14, 270-275 (2018).
PubMed: 29309054

Assembly members:

Assembly members:
DHDD, polymer, 91 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Burkholderia gladioli Taxonomy ID: 28095 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia gladioli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DHDD: MKHHHHHHHHGGLVPRGSHG SDEGVPDALRADTVPRAGPV RYARRRYWIGEARSDALAPA APLEREPLPAEAMGAYFAIR RTDADDTVAAH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	230
15N chemical shifts	69
1H chemical shifts	69

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Protein DHDD	1

Entities:

Entity 1, Protein DHDD 91 residues - Formula weight is not available

1

MET

LYS

HIS

2

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

GLY

3

SER

ASP

GLU

GLY

VAL

PRO

ASP

ALA

LEU

ARG

4

ALA

ASP

THR

VAL

PRO

ARG

ALA

GLY

PRO

VAL

5

ARG

TYR

ALA

ARG

TYR

TRP

ILE

GLY

6

GLU

ALA

ARG

SER

ASP

ALA

LEU

ALA

PRO

ALA

7

ALA

PRO

LEU

GLU

ARG

GLU

PRO

LEU

PRO

ALA

8

GLU

ALA

MET

GLY

ALA

TYR

PHE

ALA

ILE

ARG

9

ARG

THR

ASP

ALA

ASP

THR

VAL

ALA

10

HIS

Samples:

sample_1: Protein DHDD, [U-99% 13C; U-99% 15N], 0.3 mM; potassium phosphate 50 mM; sodium chloride 200 mM; DSS 50 uM

sample_conditions_1: ionic strength: 0.28 M; pH: 6.8; pressure: 1 atm; temperature: 280 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 HNCO	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(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - processing

CcpNMR v2.4.1, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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