BMRB Entry 52587

Title:
Cc ProXp-ala
Deposition date:
2024-08-19
Original release date:
2024-09-19
Authors:
Duran, Antonia; Danhart, Eric; Foster, Mark
Citation:

Citation: Duran, Antonia; Danhart, Eric; Ma, Xiao; Kuzmishin, Alexandra; Musier-Forsyth, Karin; Foster, Mark. "NMR-based solution structure of the Caulobacter crescentus ProXp-ala trans-editing enzyme"  Biomol. NMR Assign. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 171 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Caulobacter vibrioides   Taxonomy ID: 155892   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Caulobacter crescentus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet15b

Data sets:
Data typeCount
13C chemical shifts665
15N chemical shifts163
1H chemical shifts1076

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ProXp-ala1

Entities:

Entity 1, ProXp-ala 171 residues - Formula weight is not available

1   GLYSERHISMETLYSTHRARGALAASPLEU
2   PHEALAPHEPHEASPALAHISGLYVALASP
3   HISLYSTHRLEUASPHISPROPROVALPHE
4   ARGVALGLUGLUGLYLEUGLUILELYSALA
5   ALAMETPROGLYGLYHISTHRLYSASNLEU
6   PHELEULYSASPALALYSGLYGLNLEUTRP
7   LEUILESERALALEUGLYGLUTHRTHRILE
8   ASPLEULYSLYSLEUHISHISVALILEGLY
9   SERGLYARGLEUSERPHEGLYPROGLNGLU
10   METMETLEUGLUTHRLEUGLYVALTHRPRO
11   GLYSERVALTHRALAPHEGLYLEUILEASN
12   ASPTHRGLULYSARGVALARGPHEVALLEU
13   ASPLYSALALEUALAASPSERASPPROVAL
14   ASNPHEHISPROLEULYSASNASPALATHR
15   THRALAVALSERGLNALAGLYLEUARGARG
16   PHELEUALAALALEUGLYVALGLUPROMET
17   ILEVALASPPHEALAALAMETGLUVALVAL
18   GLY

Samples:

sample_1: Cc ProXp-ala, [U-100% 13C; U-100% 15N], 0.6 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1
1D 1Hsample_1isotropicsample_conditions_1

Software:

TOPSPIN - processing

NMRPipe - processing

NMRViewJ - chemical shift assignment, peak picking

CYANA - structure solution

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks