BMRB Entry 36728

Name: Anti-CRISPR protein AcrIE7
Published: 2025-12-12

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PDB ID: 9lo1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36728
MolProbity Validation Chart

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NMR-STAR v3 text file.
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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:

Anti-CRISPR protein AcrIE7

Deposition date:

2025-01-22

Original release date:

2025-12-12

Authors:

Suh, J.; Park, C.

Citation:

Citation: Kang, Jeehee; Park, Changkon; Lee, Gyujin; Koo, Jasung; Oh, Hyejin; Kim, Eun-Hee; Bae, Euiyoung; Suh, Jeong-Yong. "Structural Investigation of the Anti-CRISPR Protein AcrIE7." Proteins 93, 1645-1656 (2025).
PubMed: 40318042

Assembly members:

Assembly members:
Anti-CRISPR AcrIE7, polymer, 106 residues, 11957.555 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Anti-CRISPR AcrIE7: MIGSEKQVNWAKSIIEKEVE AWEAIGVDVREVAAFLRSIS DARVIIDNRNLIHFQSSGIS YSLESSPLNSPIFLRRFSAC SVGFEEIPTALQRIRSVYTA KLLEDE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	446
15N chemical shifts	97
1H chemical shifts	652

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 106 residues - 11957.555 Da.

1

MET

ILE

GLY

SER

GLU

LYS

GLN

VAL

ASN

TRP

2

ALA

LYS

SER

ILE

GLU

LYS

GLU

VAL

GLU

3

ALA

TRP

GLU

ALA

ILE

GLY

VAL

ASP

VAL

ARG

4

GLU

VAL

ALA

PHE

LEU

ARG

SER

ILE

SER

5

ASP

ALA

ARG

VAL

ILE

ASP

ASN

ARG

ASN

6

LEU

ILE

HIS

PHE

GLN

SER

GLY

ILE

SER

7

TYR

SER

LEU

GLU

SER

PRO

LEU

ASN

SER

8

PRO

ILE

PHE

LEU

ARG

PHE

SER

ALA

CYS

9

SER

VAL

GLY

PHE

GLU

ILE

PRO

THR

ALA

10

LEU

GLN

ARG

ILE

ARG

SER

VAL

TYR

THR

ALA

11

LYS

LEU

GLU

ASP

GLU

Samples:

sample_1: AcrIE7, [U-13C; U-15N], 0.5 mM; NaCl 150 mM; sodium phosphate 10 mM; H2O 90%; D2O, [U-2H], 10%

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

Experiments:

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

Software:

Xipp, Garrett - chemical shift assignment

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

NMR spectrometers:

Bruker AVANCE 900 MHz

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