BMRB Entry 36471

Name: solution structure of an anti-CRISPR protein
Published: 2022-10-20

Click here to enlarge.

PDB ID: 7x31
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36471
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

solution structure of an anti-CRISPR protein

Deposition date:

2022-02-27

Original release date:

2022-10-20

Authors:

Zhao, Y.; Yang, F.

Citation:

Citation: Zhao, Y.; Yang, F.. "The solution structure of an anti-CRISPR protein" .

Assembly members:

Assembly members:
entity_1, polymer, 86 residues, 9637.853 Da.

Natural source:

Natural source: Common Name: Neisseria meningitidis Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria meningitidis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MANKTYKIGKNAGYDGCGLC LAAISENEAIKVKYLRDICP DYDGDDKAEDWLRWGTDSRV KAAALEMEQYAYTSVGMASC WEFVEL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	350
15N chemical shifts	93
1H chemical shifts	534

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 86 residues - 9637.853 Da.

1

MET

ALA

ASN

LYS

THR

TYR

LYS

ILE

GLY

LYS

2

ASN

ALA

GLY

TYR

ASP

GLY

CYS

GLY

LEU

CYS

3

LEU

ALA

ILE

SER

GLU

ASN

GLU

ALA

ILE

4

LYS

VAL

LYS

TYR

LEU

ARG

ASP

ILE

CYS

PRO

5

ASP

TYR

ASP

GLY

ASP

LYS

ALA

GLU

ASP

6

TRP

LEU

ARG

TRP

GLY

THR

ASP

SER

ARG

VAL

7

LYS

ALA

LEU

GLU

MET

GLU

GLN

TYR

8

ALA

TYR

THR

SER

VAL

GLY

MET

ALA

SER

CYS

9

TRP

GLU

PHE

VAL

GLU

LEU

Samples:

sample_1: unit_1, [U-15N], 1 mM; TRIS 20 mM; sodium chloride 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: unit_1, [U-13C; U-15N], 1 mM; TRIS 20 mM; sodium chloride 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: unit_1, [U-13C; U-15N], 1 mM; TRIS 20 mM; sodium chloride 100 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; 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	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY-HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY-HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1

Software:

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNmr Analysis, CCPN - data analysis

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

TopSpin, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE 600 MHz

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