BMRB Entry 18606

Name: Solution structure of anti-CRISPR protein Acr30-35 from Pseudomonas aeruginosa Phage JBD30
Published: 2013-02-14

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PDB ID: 2lw5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18606
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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 Acr30-35 from Pseudomonas aeruginosa Phage JBD30

Deposition date:

2012-07-22

Original release date:

2013-02-14

Authors:

Maxwell, Karen; Bondy-Denomy, Joe; Davidson, Alan

Citation:

Citation: Bondy-Denomy, Joe; Pawluk, April; Maxwell, Karen; Davidson, Alan. "Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system." Nature 493, 429-432 (2013).
PubMed: 23242138

Assembly members:

Assembly members:
entity, polymer, 79 residues, 8825.006 Da.

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 1223260 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas Pseudomonas Bacteriophage JBD30

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GMKFIKYLSTAHLNYMNIAV YENGSKIKARVENVVNGKSV GARDFDSTEQLESWFYGLPG SGLGRIENAMNEISRRENP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	239
15N chemical shifts	75
1H chemical shifts	509

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	anti-CRISPR protein Acr30-35	1

Entities:

Entity 1, anti-CRISPR protein Acr30-35 79 residues - 8825.006 Da.

1

GLY

MET

LYS

PHE

ILE

LYS

TYR

LEU

SER

THR

2

ALA

HIS

LEU

ASN

TYR

MET

ASN

ILE

ALA

VAL

3

TYR

GLU

ASN

GLY

SER

LYS

ILE

LYS

ALA

ARG

4

VAL

GLU

ASN

VAL

ASN

GLY

LYS

SER

VAL

5

GLY

ALA

ARG

ASP

PHE

ASP

SER

THR

GLU

GLN

6

LEU

GLU

SER

TRP

PHE

TYR

GLY

LEU

PRO

GLY

7

SER

GLY

LEU

GLY

ARG

ILE

GLU

ASN

ALA

MET

8

ASN

GLU

ILE

SER

ARG

GLU

ASN

PRO

Samples:

sample_1: sodium phosphate 25 mM; sodium chloride 200 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 25 mM; sodium chloride 200 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 273 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	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1

Software:

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Varian INOVA 500 MHz
Varian INOVA 800 MHz

PDB	2LW5
DBJ	BAR65419
EMBL	CDM55208 CRN29922 CRN44629 CRN56640 CRN59456
GB	AFE86461 AFQ21949 ERX38869 EZO98398
REF	WP_016068276 WP_033975723 YP_006560529 YP_007392342