BMRB Entry 36085

Title:
Anti-CRISPR protein AcrIIA4
Deposition date:
2017-05-17
Original release date:
2018-07-17
Authors:
Suh, J.-Y., .; Kim, I.
Citation:

Citation: Kim, I.; Jeong, M.; Ka, D.; Han, M.; Kim, N.; Bae, E.; Suh, J.. "Solution structure and dynamics of anti-CRISPR AcrIIA4, the Cas9 inhibitor."  Sci. Rep. 8, 3883-3883 (2018).
PubMed: 29497118

Assembly members:

Assembly members:
Anti-CRISPR AcrIIA4, polymer, 87 residues, 10182.073 Da.

Natural source:

Natural source:   Common Name: Listeria monocytogenes   Taxonomy ID: 1639   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Listeria monocytogenes

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts97
1H chemical shifts589

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 87 residues - 10182.073 Da.

1   METASNILEASNASPLEUILEARGGLUILE
2   LYSASNLYSASPTYRTHRVALLYSLEUSER
3   GLYTHRASPSERASNSERILETHRGLNLEU
4   ILEILEARGVALASNASNASPGLYASNGLU
5   TYRVALILESERGLUSERGLUASNGLUSER
6   ILEVALGLULYSPHEILESERALAPHELYS
7   ASNGLYTRPASNGLNGLUTYRGLUASPGLU
8   GLUGLUPHETYRASNASPMETGLNTHRILE
9   THRLEULYSSERGLULEUASN

Samples:

sample_1: AcrIIA4, [U-99% 13C; U-99% 15N], 2.0 mM; Tris HCl 20 mM; NaCl 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

PIPP, Garrett - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker Avance 800 MHz

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