BMRB Entry 36320

Name: Solution structure of anti-CRISPR AcrIF7
Published: 2020-09-05

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PDB ID: 6m3n
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR36320
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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 AcrIF7

Deposition date:

2020-03-04

Original release date:

2020-09-05

Authors:

Kim, I.; An, S.; Koo, J.; Bae, E.; Suh, J.

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:
anti-CRIPSR AcrIF7, polymer, 69 residues, 7526.073 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
anti-CRIPSR AcrIF7: GHMTTFTSIVTTNPDFGGFE FYVEAGQQFDDSAYEEAYGV SVPSAVVEEMNAKAAQLKDG EWLNVSHEA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

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	entity_1	1

Entities:

Entity 1, entity_1 69 residues - 7526.073 Da.

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; NaCl 150 mM; DTT 2 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

Sparky, Goddard - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

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