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 34193

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 typeCount
13C chemical shifts282
15N chemical shifts72
1H chemical shifts455

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 63 residues - 7496.248 Da.

1   METLYSASNALAALAGLNILEVALASPGLU
2   ALALEUASNGLNGLYILETHRLEUPHEVAL
3   ALAASPASNARGLEUGLNTYRGLUTHRSER
4   ARGASPASNILEPROGLUGLULEULEUASN
5   GLUTRPLYSTYRTYRARGGLNASPLEUILE
6   ASPPHELEUGLNGLNLEUASPALALYSGLU
7   GLUTHRGLN

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_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