BMRB Entry 27331

Title:
1H, 13C and 15N resonance assignment of SpyCatcher part of complex
Deposition date:
2017-12-05
Original release date:
2021-07-22
Authors:
Liu, Jing; Wang, Shenlin
Citation:

Citation: Zhang, Nan; Liu, Jing; Liu, Yajie; Wu, Wen-Hao; Fang, Jing; Da, Xiao-Di; Wang, Shenlin; Zhang, Wen-Bin. "NMR Spectroscopic Studies Reveal the Critical Role of the Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes"  Biochemistry 59, 2226-2236 (2020).
PubMed: 32469203

Assembly members:

Assembly members:
SpyCatcher, polymer, 114 residues, Formula weight is not available
SpyTag, polymer, 16 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Streptococcus pyogenes   Taxonomy ID: 1314   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pyogenes

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28a

Data sets:
Data typeCount
13C chemical shifts312
15N chemical shifts109
1H chemical shifts109

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SpyCatcher1
2SpyTag2

Entities:

Entity 1, SpyCatcher 114 residues - Formula weight is not available

1   ALAMETVALASPTHRLEUSERGLYLEUSER
2   SERGLUGLNGLYGLNSERGLYASPMETTHR
3   ILEGLUGLUASPSERALATHRHISILELYS
4   PHESERLYSARGASPGLUASPGLYLYSGLU
5   LEUALAGLYALATHRMETGLULEUARGASP
6   SERSERGLYLYSTHRILESERTHRTRPILE
7   SERASPGLYGLNVALLYSASPPHETYRLEU
8   TYRPROGLYLYSTYRTHRPHEVALGLUTHR
9   ALAALAPROASPGLYTYRGLUVALALATHR
10   ALAILETHRPHETHRVALASNGLUGLNGLY
11   GLNVALTHRVALASNGLYLYSALATHRLYS
12   GLYASPALAHIS

Entity 2, SpyTag 16 residues - Formula weight is not available

1   ALAHISILEVALMETVALASPALATYRLYS
2   PROTHRLYSLEUASPCYS

Samples:

sample_1: SpyCatcher, [U-100% 13C; U-100% 15N], 0.3 mM; SpyTag 0.3 mM

sample_conditions_1: ionic strength: 16 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1

Software:

TOPSIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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