BMRB Entry 28082

Name: Solution structure of anti-CRISPR protein AcrIF7 from Pseudomonas aeruginosa Phage
Published: 2021-07-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28082

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
AcrIF7: GHMTTFTSIVTTNPDFGGFE FYVEAGQQFDDSAYEEAYGV SVPSAVVEEMNAKAAQLKDG EWLNVSHEA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	268
15N chemical shifts	72
1H chemical shifts	430

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AcrIF7 monomer	1

Entities:

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

1

GLY

HIS

MET

THR

PHE

THR

SER

ILE

VAL

2

THR

ASN

PRO

ASP

PHE

GLY

PHE

GLU

3

PHE

TYR

VAL

GLU

ALA

GLY

GLN

PHE

ASP

4

ASP

SER

ALA

TYR

GLU

ALA

TYR

GLY

VAL

5

SER

VAL

PRO

SER

ALA

VAL

GLU

MET

6

ASN

ALA

LYS

ALA

GLN

LEU

LYS

ASP

GLY

7

GLU

TRP

LEU

ASN

VAL

SER

HIS

GLU

ALA

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_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