BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30807

Title: The structure of anti-CRISPR AcrIE2   PubMed: 33338493

Deposition date: 2020-10-25 Original release date: 2021-05-21

Authors: Pawluk, A.; Davidson, A.; Maxwell, K.

Citation: Mejdani, M.; Pawluk, A.; Maxwell, K.; Davidson, A.. "Anti-CRISPR AcrIE2 Binds the Type I-E CRISPR-Cas Complex But Does Not Block DNA Binding"  J. Mol. Biol. 433, 166759-166759 (2021).

Assembly members:
entity_1, polymer, 91 residues, 10319.222 Da.

Natural source:   Common Name: Pseudomonas phage JBD16C   Taxonomy ID: 1777051   Superkingdom: Viruses   Kingdom: not available   Genus/species: Casadabanvirus Pseudomonas phage JBD16C

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21   Vector: pET15b

Entity Sequences (FASTA):
entity_1: MNTYLIDPRKNNDNSGERFT VDAVDITAAAKSAAQQILGE EFEGLVYRETGESNGSGMFQ AYHHLHGTNRTETTVGYPFH VMELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts309
15N chemical shifts84
1H chemical shifts504

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 91 residues - 10319.222 Da.

1   METASNTHRTYRLEUILEASPPROARGLYS
2   ASNASNASPASNSERGLYGLUARGPHETHR
3   VALASPALAVALASPILETHRALAALAALA
4   LYSSERALAALAGLNGLNILELEUGLYGLU
5   GLUPHEGLUGLYLEUVALTYRARGGLUTHR
6   GLYGLUSERASNGLYSERGLYMETPHEGLN
7   ALATYRHISHISLEUHISGLYTHRASNARG
8   THRGLUTHRTHRVALGLYTYRPROPHEHIS
9   VALMETGLULEUGLUHISHISHISHISHIS
10   HIS

Samples:

sample_1: anti-CRISPR, [U-100% 13C; U-100% 15N], 1.0 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 .; temperature: 298 K

Experiments:

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

Software:

CYANA v2.1, Schmidt - refinement

Sparky v2.1, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - peak picking

PINE-SPARKY, Goddard - peak picking

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

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