BMRB Entry 30807

Name: The structure of anti-CRISPR AcrIE2
Published: 2021-05-21

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PDB ID: 7kix
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30807
MolProbity Validation Chart

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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:

The structure of anti-CRISPR AcrIE2

Deposition date:

2020-10-25

Original release date:

2021-05-21

Authors:

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

Citation:

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).
PubMed: 33338493

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	309
15N chemical shifts	84
1H chemical shifts	504

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 91 residues - 10319.222 Da.

1

MET

ASN

THR

TYR

LEU

ILE

ASP

PRO

ARG

LYS

2

ASN

ASP

ASN

SER

GLY

GLU

ARG

PHE

THR

3

VAL

ASP

ALA

VAL

ASP

ILE

THR

ALA

4

LYS

SER

ALA

GLN

ILE

LEU

GLY

GLU

5

GLU

PHE

GLU

GLY

LEU

VAL

TYR

ARG

GLU

THR

6

GLY

GLU

SER

ASN

GLY

SER

GLY

MET

PHE

GLN

7

ALA

TYR

HIS

LEU

HIS

GLY

THR

ASN

ARG

8

THR

GLU

THR

VAL

GLY

TYR

PRO

PHE

HIS

9

VAL

MET

GLU

LEU

GLU

HIS

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:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks