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 34575

Title: Solution structure of a non-covalent extended docking domain complex of the Pax NRPS: PaxA T1-CDD/PaxB NDD   PubMed: 33675014

Deposition date: 2020-11-26 Original release date: 2021-06-02

Authors: Watzel, J.; Sarawi, S.; Duchardt-Ferner, E.; Bode, H.; Woehnert, J.

Citation: Watzel, J.; Sarawi, S.; Duchardt-Ferner, E.; Bode, H.; Woehnert, J.. "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, 135 residues, 15574.582 Da.

Natural source:   Common Name: Xenorhabdus cabanillasii   Taxonomy ID: 1427517   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Xenorhabdus cabanillasii

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET-11a

Entity Sequences (FASTA):
entity_1: MNNNELTSLPLAERKRLLEL AKAAKLSRQHYDHSSVITQE YAAPQGEIEEQLADIWQTIL KIDRIGRYDNFFELGGHSLL VLQLQSRINEIFDVDISIQQ LFAHPSICQLEECIINAQLL QFDADSLQDIYKSME

Data typeCount
13C chemical shifts591
15N chemical shifts150
1H chemical shifts977

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 135 residues - 15574.582 Da.

1   METASNASNASNGLULEUTHRSERLEUPRO
2   LEUALAGLUARGLYSARGLEULEUGLULEU
3   ALALYSALAALALYSLEUSERARGGLNHIS
4   TYRASPHISSERSERVALILETHRGLNGLU
5   TYRALAALAPROGLNGLYGLUILEGLUGLU
6   GLNLEUALAASPILETRPGLNTHRILELEU
7   LYSILEASPARGILEGLYARGTYRASPASN
8   PHEPHEGLULEUGLYGLYHISSERLEULEU
9   VALLEUGLNLEUGLNSERARGILEASNGLU
10   ILEPHEASPVALASPILESERILEGLNGLN
11   LEUPHEALAHISPROSERILECYSGLNLEU
12   GLUGLUCYSILEILEASNALAGLNLEULEU
13   GLNPHEASPALAASPSERLEUGLNASPILE
14   TYRLYSSERMETGLU

Samples:

sample_1: PaxA T1-CDD, [U-15N], 300 uM; PaxB NDD 360 uM; sodium phosphate 50 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; D2O, [U-2H], 5%; DSS 100 uM

sample_2: PaxA T1-CDD 360 uM; PaxB NDD, [U-15N], 300 uM; sodium phosphate 50 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; D2O, [U-2H], 5%; DSS 100 uM

sample_3: PaxA T1-CDD, [U-13C; U-15N], 300 uM; PaxB NDD 360 uM; sodium phosphate 50 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; D2O, [U-2H], 5%; DSS 100 uM

sample_4: PaxA T1-CDD 360 uM; PaxB NDD, [U-13C; U-15N], 300 uM; sodium phosphate 50 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; D2O, [U-2H], 5%; DSS 100 uM

sample_5: PaxA T1-CDD, [U-13C; U-15N], 300 uM; PaxB NDD 360 uM; sodium phosphate 50 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; D2O, [U-2H], 5%; DSS 100 uM

sample_6: PaxA T1-CDD 360 uM; PaxB NDD, [U-13C; U-15N], 300 uM; sodium phosphate 50 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; D2O, [U-2H], 5%; DSS 100 uM

sample_7: PaxA T1-CDD, [U-10% 13C; U-15N], 300 uM; PaxB NDD 360 uM; sodium phosphate 50 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; D2O, [U-2H], 5%; DSS 100 uM

sample_8: PaxA T1-CDD, [U-15N], 180 uM; PaxB NDD, [U-10% 13C; U-15N], 150 uM; sodium phosphate 50 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; D2O, [U-2H], 5%; DSS 100 uM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_6isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_7isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_8isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C-filtered NOESY aliphaticsample_5isotropicsample_conditions_1
3D 1H-13C-filtered NOESY aliphaticsample_6isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_1
3D HBHA(CO)NHsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_4isotropicsample_conditions_1

Software:

TopSpin v3.6.2, Bruker Biospin - data analysis

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment

CcpNmr Analysis v2.4.2, CCPN - peak picking

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

OPALp, Koradi, Billeter and Guntert - refinement

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz
  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE II 600 MHz
  • Bruker AVANCE NEO 900 MHz
  • Bruker AVANCE III 950 MHz

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