BMRB Entry 19555

Name: Solution structure of the C-terminally encoded peptide of the plant parasitic nematode Meloidogyne hapla - CEP11
Published: 2013-12-09

Click here to enlarge.

PDB ID: 2mfm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19555
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 the C-terminally encoded peptide of the plant parasitic nematode Meloidogyne hapla - CEP11

Deposition date:

2013-10-14

Original release date:

2013-12-09

Authors:

Bobay, Benjamin; DiGennaro, Peter; McK. Bird, David

Citation:

Citation: Bobay, Benjamin; DiGennaro, Peter; Scholl, Elizabeth; Imin, Nijat; Djordjevic, Michael; McK. Bird, David. "Solution NMR studies of the plant peptide hormone CEP inform function" FEBS Lett. 587, 3979-3985 (2013).
PubMed: 24211833

Assembly members:

Assembly members:
entity, polymer, 15 residues, 1522.660 Da.

Natural source:

Natural source: Common Name: Northern root-knot nematode Taxonomy ID: 6305 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Meloidogyne hapla

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: AFRXTAPGHSXGVGH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	26
15N chemical shifts	12
1H chemical shifts	66

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CEP11	1

Entities:

Entity 1, CEP11 15 residues - 1522.660 Da.

1

ALA

PHE

ARG

HYP

THR

ALA

PRO

GLY

HIS

SER

2

HYP

GLY

VAL

GLY

HIS

Samples:

sample_1: entity 4 mg/mL; DSS 10 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; 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:

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

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

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

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