BMRB Entry 28082

Title:
Solution structure of anti-CRISPR protein AcrIF7 from Pseudomonas aeruginosa Phage
Deposition date:
2020-02-17
Original release date:
2021-07-16
Authors:
Kim, Iktae; Koo, Jasung; An, So Young; Bae, Euiyoung; Suh, Jeong-Yong
Citation:

Citation: Kim, Iktae; Koo, Jasung; An, So Young; Hong, Suji; Ka, Donghyun; Kim, Eun-Hee; Bae, Euiyoung; Suh, Jeong-Yong. "Structural and mechanistic insights into the CRISPR inhibition of AcrIF7."  Nucleic Acids Res. 48, 9959-9968 (2020).
PubMed: 32810226

Assembly members:

Assembly members:
AcrIF7, polymer, 69 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts268
15N chemical shifts72
1H chemical shifts430

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AcrIF7 monomer1

Entities:

Entity 1, AcrIF7 monomer 69 residues - Formula weight is not available

1   GLYHISMETTHRTHRPHETHRSERILEVAL
2   THRTHRASNPROASPPHEGLYGLYPHEGLU
3   PHETYRVALGLUALAGLYGLNGLNPHEASP
4   ASPSERALATYRGLUGLUALATYRGLYVAL
5   SERVALPROSERALAVALVALGLUGLUMET
6   ASNALALYSALAALAGLNLEULYSASPGLY
7   GLUTRPLEUASNVALSERHISGLUALA

Samples:

sample_1: AcrIF7, [U-99% 13C; U-99% 15N], 0.6 mM; HEPES 20 mM; sodium chloride 200 mM; DTT 1 mM; EDTA 1 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

SPARKY vNMRFAM-SPARKY, Goddard - chemical shift assignment, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH v2.52, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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