BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34196

Title: Solution Structure of Docking Domain Complex of RXP NRPS: Kj12C NDD - Kj12B CDD   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: Cai, X.; Hacker, C.; Kegler, C.; Zhai, L.; Woehnert, J.; Bode, H.. "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, 99 residues, 11107.151 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-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
entity_1: GIDAAQIVDEALEQGITLFV VNNRLQYETSRDSIPTELLN KWKQHKQELIDFLNQLDSEE QTKGSGSGSGSGSGSLLKEK RKHFQAEQNSSQEYLRGEI

Data typeCount
13C chemical shifts312
15N chemical shifts90
1H chemical shifts626

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 99 residues - 11107.151 Da.

1   GLYILEASPALAALAGLNILEVALASPGLU
2   ALALEUGLUGLNGLYILETHRLEUPHEVAL
3   VALASNASNARGLEUGLNTYRGLUTHRSER
4   ARGASPSERILEPROTHRGLULEULEUASN
5   LYSTRPLYSGLNHISLYSGLNGLULEUILE
6   ASPPHELEUASNGLNLEUASPSERGLUGLU
7   GLNTHRLYSGLYSERGLYSERGLYSERGLY
8   SERGLYSERGLYSERLEULEULYSGLULYS
9   ARGLYSHISPHEGLNALAGLUGLNASNSER
10   SERGLNGLUTYRLEUARGGLYGLUILE

Samples:

sample_1: KJ12C Ndd 12xGS KJ12B Cdd, [U-99% 15N], 700 uM; sodium phosphate buffer 50 mM; sodium chloride 100 mM

sample_2: KJ12C Ndd 12xGS KJ12B Cdd, [U-99% 13C; U-99% 15N], 850 uM; sodium phosphate buffer 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 Pa; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D b-tr-HN(CO)CAsample_2isotropicsample_conditions_1
3D b-tr-HNCACBsample_2isotropicsample_conditions_1
3D b-tr-HNCOsample_2isotropicsample_conditions_1
2D 1H-15N b-tr-HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1

Software:

OpalP v3.97, Guentert Peter - refinement

CARA v1.8.4.2, Keller, R. (2004) The Computer Aided Resonance Tutorial, CANTINA Verlag, Goldau - chemical shift assignment

TOPSPIN v3.5, Bruker Biospin - collection

Analysis, CCPN - data analysis

UNIO v10, Herrmann, Thorsten, Guentert, Peter and Wuethrich, Kurt - peak picking

CYANA v3.97, Guentert Peter - structure calculation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 599 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

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