BMRB Entry 19081

Name: NMR structure of the P4 hairpin of the CPEB3 ribozyme
Published: 2014-03-31

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PDB ID: 2m5u
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19081
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the P4 hairpin of the CPEB3 ribozyme

Deposition date:

2013-03-08

Original release date:

2014-03-31

Authors:

Skilandat, Miriam; Rowinska-Zyrek, Magdalena; Sigel, Roland

Citation:

Citation: Skilandat, Miriam; Rowinska-Zyrek, Magdalena; Sigel, Roland. "Solution structure and metal ion binding sites of the human CPEB3 ribozyme's P4 domain." J. Biol. Inorg. Chem. ., .-. (2014).
PubMed: 24652468

Assembly members:

Assembly members:
P4_CPEB3, polymer, 22 residues, 7051.259 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: cell free synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
P4_CPEB3: GGCAGAUUCUGGUGAAUCUG CC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	179

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	P4_CPEB3	1

Entities:

Entity 1, P4_CPEB3 22 residues - 7051.259 Da.

sequence corresponds to residue 39 to 56 of the CPEB3 ribozyme

1

G

C

A

G

A

U

C

U

2

G

U

G

A

U

C

U

G

3

C

Samples:

sample_1: D2O 100%; P4_CPEB30.7 – 0.8 mM; KCl 50 mM; EDTA 10 uM

sample_2: D2O 10%; P4_CPEB30.7 – 0.8 mM; H2O 90%; KCl 50 mM; EDTA 10 uM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2
1D 31P	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0 -

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz
Bruker Avance 500 MHz