BMRB Entry 26021

Name: Sr33 Coiled-coil domain
Published: 2016-10-13

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PDB ID: 2ncg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26021
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: Sr33 Coiled-coil domain PubMed: 27791121

Deposition date: 2016-03-30 Original release date: 2016-10-13

Authors: Lavrencic, Peter; Mobli, Mehdi

Citation: Casey, Lachlan; Lavrencic, Peter; Bentham, Adam; Cesari, Stella; Ericsson, Daniel; Croll, Tristan; Turk, Dusan; Anderson, Peter; Mark, Alan; Dodds, Peter; Mobli, Mehdi; Kobe, Bostjan; Williams, Simon. "The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins" Proc. Natl. Acad. Sci. U.S.A. ., .-. (2016).

Assembly members:
entity, polymer, 118 residues, 13138.456 Da.

Natural source: Common Name: bread wheat Taxonomy ID: 4565 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Triticum aestivum

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

Entity Sequences (FASTA):
entity: SNAGAIAKLIPKLGELLVGE YKLHKGVKKNIEDLLKELKT MNAALIKIGEVPPDQLDSQD KLWADEVRELSYVIEDAVDK FLVRVHGVEPDDNTNGFKGL MKRTTKLLKKVVDKHGIA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	506
15N chemical shifts	120
1H chemical shifts	865

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 118 residues - 13138.456 Da.

1

SER

ASN

ALA

GLY

ALA

ILE

ALA

LYS

LEU

ILE

2

PRO

LYS

LEU

GLY

GLU

LEU

VAL

GLY

GLU

3

TYR

LYS

LEU

HIS

LYS

GLY

VAL

LYS

ASN

4

ILE

GLU

ASP

LEU

LYS

GLU

LEU

LYS

THR

5

MET

ASN

ALA

LEU

ILE

LYS

ILE

GLY

GLU

6

VAL

PRO

ASP

GLN

LEU

ASP

SER

GLN

ASP

7

LYS

LEU

TRP

ALA

ASP

GLU

VAL

ARG

GLU

LEU

8

SER

TYR

VAL

ILE

GLU

ASP

ALA

VAL

ASP

LYS

9

PHE

LEU

VAL

ARG

VAL

HIS

GLY

VAL

GLU

PRO

10

ASP

ASN

THR

ASN

GLY

PHE

LYS

GLY

LEU

11

MET

LYS

ARG

THR

LYS

LEU

LYS

12

VAL

ASP

LYS

HIS

GLY

ILE

ALA

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 450 uM; HEPES 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift calculation, refinement, structure solution

TALOS vTALOS+, Cornilescu, Delaglio and Bax - geometry optimization

CCPNMR v2.4.1, Vranken WF et al. - data analysis, peak picking

Rowland_NMR_toolkit v3, JC Hoch et al. - processing

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts