BMRB Entry 50594

Name: NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii
Published: 2021-06-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50594

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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:

NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii

Deposition date:

2020-11-25

Original release date:

2021-06-02

Authors:

Watzel, Jonas; Sarawi, Sepas; Duchardt-Ferner, Elke; Bode, Helge; Woehnert, Jens

Citation:

Citation: Watzel, Jonas; Sarawi, Sepas; Duchardt-Ferner, Elke; Bode, Helge; Woehnert, Jens. "NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii." Biomol. NMR Assign. 15, 229-234 (2021).
PubMed: 33675014

Assembly members:

Assembly members:
entity_1, polymer, 104 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Xenorhabdus cabanillasii Taxonomy ID: 351673 Superkingdom: Bacteria Kingdom: not available Genus/species: Xenorhabdus cabanillasii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DHSSVITQEYAAPQGEIEEQ LADIWQTILKIDRIGRYDNF FELGGHSLLVLQLQSRINEI FDVDISIQQLFAHPSICQLE ECIINAQLLQFDADSLQDIY KSME

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	300
15N chemical shifts	99
1H chemical shifts	376

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PaxA T1-Cdd	1

Entities:

Entity 1, PaxA T1-Cdd 104 residues - Formula weight is not available

1

ASP

HIS

SER

VAL

ILE

THR

GLN

GLU

TYR

2

ALA

PRO

GLN

GLY

GLU

ILE

GLU

GLN

3

LEU

ALA

ASP

ILE

TRP

GLN

THR

ILE

LEU

LYS

4

ILE

ASP

ARG

ILE

GLY

ARG

TYR

ASP

ASN

PHE

5

PHE

GLU

LEU

GLY

HIS

SER

LEU

VAL

6

LEU

GLN

LEU

GLN

SER

ARG

ILE

ASN

GLU

ILE

7

PHE

ASP

VAL

ASP

ILE

SER

ILE

GLN

LEU

8

PHE

ALA

HIS

PRO

SER

ILE

CYS

GLN

LEU

GLU

9

GLU

CYS

ILE

ASN

ALA

GLN

LEU

GLN

10

PHE

ASP

ALA

ASP

SER

LEU

GLN

ASP

ILE

TYR

11

LYS

SER

MET

GLU

Samples:

sample_1: PaxA T1-Cdd, [U-13C; U-15N], 300 uM; sodium phosphate 50 mM; sodium chloride 100 mM; D2O, [U-2H], 10%; DSS 100 uM; beta-mercaptoethanol 2 mM

sample_conditions_1: 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 HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.8.4 - chemical shift assignment, peak picking

TOPSPIN v3.6.2 - data analysis

NMR spectrometers:

Bruker Avance II 600 MHz
Bruker AVANCE III HD 800 MHz