BMRB Entry 34068

Name: RBM5 OCRE domain
Published: 2016-12-05

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PDB ID: 5mfy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34068
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:

RBM5 OCRE domain

Deposition date:

2016-11-19

Original release date:

2016-12-05

Authors:

Warner, L.; Mourao, A.; Soni, K.; Sattler, M.

Citation:

Citation: Mourao, A.; Bonnal, S.; Soni, K.; Warner, L.; Bordonne, R.; Valcarcel, J.; Sattler, M.. "Structural basis for the recognition of spliceosomal SmN/B/B' proteins by the RBM5 OCRE domain in splicing regulation." Elife 5, .-. (2016).
PubMed: 27894420

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7436.785 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: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGTKYAVPDTSTYQYDES SGYYYDPTTGLYYDPNSQYY YNSLTQQYLYWDGEKETYVP AAES

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	282
15N chemical shifts	65
1H chemical shifts	397

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 64 residues - 7436.785 Da.

1

GLY

ALA

MET

GLY

THR

LYS

TYR

ALA

VAL

PRO

2

ASP

THR

SER

THR

TYR

GLN

TYR

ASP

GLU

SER

3

SER

GLY

TYR

ASP

PRO

THR

GLY

4

LEU

TYR

ASP

PRO

ASN

SER

GLN

TYR

5

TYR

ASN

SER

LEU

THR

GLN

TYR

LEU

TYR

6

TRP

ASP

GLY

GLU

LYS

GLU

THR

TYR

VAL

PRO

7

ALA

GLU

SER

Samples:

sample_1: D2O 10%; H2O 90%; ocre5, [U-100% 13C; U-100% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 70 mM; pH: 6.5 pD; 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_2
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
HDCB Kay	sample_1	isotropic	sample_conditions_2
HECB Kay	sample_1	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_2

Software:

Analysis, CCPN - chemical shift assignment, peak picking

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker AvanceIII 600 MHz
Bruker AvanceIII 900 MHz

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