BMRB Entry 34469

Name: Solution Structure of Docking Domain Complex of Pax NRPS: PaxC NDD - PaxB CDD
Published: 2020-08-06

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PDB ID: 6trp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34469
MolProbity Validation Chart

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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:

Solution Structure of Docking Domain Complex of Pax NRPS: PaxC NDD - PaxB CDD

Deposition date:

2019-12-19

Original release date:

2020-08-06

Authors:

Watzel, J.; Hacker, C.; Duchardt-Ferner, E.; Bode, H.; Woehnert, J.

Citation:

Citation: Watzel, Jonas; Hacker, Carolin; Duchardt-Ferner, Elke; Bode, Helge; Woehnert, Jens. "A New Docking Domain Type in the Peptide-Antimicrobial-Xenorhabdus Peptide Producing Nonribosomal Peptide Synthetase from Xenorhabdus bovienii" ACS Chem. Biol. 15, 982-989 (2020).
PubMed: 32167274

Assembly members:

Assembly members:
entity_1, polymer, 93 residues, 9841.622 Da.

Natural source:

Natural source: Common Name: Xenorhabdus bovienii SS-2004 Taxonomy ID: 406818 Superkingdom: Bacteria Kingdom: not available Genus/species: Xenorhabdus bovienii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MNINEQTLDKLRQAVLQKKI KERIQNSLSTEKYGSGSGSG SGSGSGSGSGSGSGSGSGYQ IETFFAQDIESVQKELENLS EEELLAMLNGDQQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	292
15N chemical shifts	78
1H chemical shifts	502

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 93 residues - 9841.622 Da.

1

MET

ASN

ILE

ASN

GLU

GLN

THR

LEU

ASP

LYS

2

LEU

ARG

GLN

ALA

VAL

LEU

GLN

LYS

ILE

3

LYS

GLU

ARG

ILE

GLN

ASN

SER

LEU

SER

THR

4

GLU

LYS

TYR

GLY

SER

GLY

SER

GLY

SER

GLY

5

SER

GLY

SER

GLY

SER

GLY

SER

GLY

SER

GLY

6

SER

GLY

SER

GLY

SER

GLY

SER

GLY

TYR

GLN

7

ILE

GLU

THR

PHE

ALA

GLN

ASP

ILE

GLU

8

SER

VAL

GLN

LYS

GLU

LEU

GLU

ASN

LEU

SER

9

GLU

LEU

ALA

MET

LEU

ASN

GLY

10

ASP

GLN

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC, 3D b-tr-HNCACB, 3D b-tr-HNCO, 3D HC(C)H-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC, 3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC, 3D HBHA(CO)NH, 3D HN(CA)CO, 3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC, 3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic, 3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic, 3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 34469

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: