BMRB Entry 34193

Name: Solution Structure of Rhabdopeptide NRPS Docking Domain Kj12A-NDD
Published: 2018-10-24

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PDB ID: 6ews
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34193
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of Rhabdopeptide NRPS Docking Domain Kj12A-NDD PubMed: 30341296

Deposition date: 2017-11-06 Original release date: 2018-10-24

Authors: Hacker, C.; Cai, X.; Kegler, C.; Zhao, L.; Weickhmann, A.; Bode, H.; Woehnert, J.

Citation: Hacker, C.; Cai, X.; Kegler, C.; Zhao, L.; Weickhmann, A.; Bode, H.; Woehnert, J.. "Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS" Nat. Commun. 9, 4366-4366 (2018).

Assembly members:
entity_1, polymer, 63 residues, 7496.248 Da.

Natural source: Common Name: Xenorhabdus stockiae Taxonomy ID: 351614 Superkingdom: Bacteria Kingdom: not available Genus/species: Xenorhabdus stockiae

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

Entity Sequences (FASTA):
entity_1: MKNAAQIVDEALNQGITLFV ADNRLQYETSRDNIPEELLN EWKYYRQDLIDFLQQLDAKE ETQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	282
15N chemical shifts	72
1H chemical shifts	455

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 63 residues - 7496.248 Da.

1

MET

LYS

ASN

ALA

GLN

ILE

VAL

ASP

GLU

2

ALA

LEU

ASN

GLN

GLY

ILE

THR

LEU

PHE

VAL

3

ALA

ASP

ASN

ARG

LEU

GLN

TYR

GLU

THR

SER

4

ARG

ASP

ASN

ILE

PRO

GLU

LEU

ASN

5

GLU

TRP

LYS

TYR

ARG

GLN

ASP

LEU

ILE

6

ASP

PHE

LEU

GLN

LEU

ASP

ALA

LYS

GLU

7

GLU

THR

GLN

Samples:

sample_1: Kj12A NDD, [U-13C; U-15N], 1 mM; sodium phosphate buffer 50 mM; sodium chloride 100 mM

sample_2: Kj12A NDD, [U-15N], 500 uM; sodium phosphate buffer 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 Pa; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.97, Guentert - structure calculation

TOPSPIN v3.97, Bruker Biospin - processing

CARA, Keller and Wuthrich - chemical shift assignment

Analysis, CCPN - data analysis

CANDID, Herrmann, Guntert and Wuthrich - peak picking

OpalP - refinement

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz
Bruker Avance 599 MHz
Bruker Avance 950 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts