BMRB Entry 19674

Name: Solution structure of the CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10
Published: 2015-01-12

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PDB ID: 2mid
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19674
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:

Solution structure of the CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10

Deposition date:

2013-12-16

Original release date:

2015-01-12

Authors:

Bobay, Benjamin; DiGennaro, Peter; Bird, David

Citation:

Citation: DiGennaro, Peter; Bobay, Benjamin; Mck Bird, David. "Inferring function of CLE peptides from high resolution tertiary structures" Proc. Natl. Acad. Sci. U.S.A. ., .-..

Assembly members:

Assembly members:
entity, polymer, 12 residues, 1302.495 Da.

Natural source:

Natural source: Common Name: thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: chemical synthesis Host organism: Synthetic Vector: N/A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: RLVPSGPNPLHN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	38
15N chemical shifts	11
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10	1

Entities:

Entity 1, CLAVATA encoded peptide of Arabidopsis thaliana - AtCLE10 12 residues - 1302.495 Da.

1

ARG

LEU

VAL

PRO

SER

GLY

PRO

ASN

PRO

LEU

2

HIS

ASN

Samples:

sample_1: entity 4 mg/mL; sodium chloride 137 mM; potassium chloride 2.7 mM; sodium phosphate 10 mM; potassium phosphate 1.8 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 140 mM; pH: 7.0; 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
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement, structure solution

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 700 MHz

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