BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 50594

Title: NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii   PubMed: 33675014

Deposition date: 2020-11-25 Original release date: 2021-06-02

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

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts300
15N chemical shifts99
1H chemical shifts376

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PaxA T1-Cdd1

Entities:

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

1   ASPHISSERSERVALILETHRGLNGLUTYR
2   ALAALAPROGLNGLYGLUILEGLUGLUGLN
3   LEUALAASPILETRPGLNTHRILELEULYS
4   ILEASPARGILEGLYARGTYRASPASNPHE
5   PHEGLULEUGLYGLYHISSERLEULEUVAL
6   LEUGLNLEUGLNSERARGILEASNGLUILE
7   PHEASPVALASPILESERILEGLNGLNLEU
8   PHEALAHISPROSERILECYSGLNLEUGLU
9   GLUCYSILEILEASNALAGLNLEULEUGLN
10   PHEASPALAASPSERLEUGLNASPILETYR
11   LYSSERMETGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_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

Related Database Links:

NCBI PHM77429.1

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