BMRB Entry 34067

Name: Solution structure of the RBM5 OCRE domain in complex with polyproline SmN peptide.
Published: 2016-12-05

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PDB ID: 5mf9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34067
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 RBM5 OCRE domain in complex with polyproline SmN peptide.

Deposition date:

2016-11-17

Original release date:

2016-12-05

Authors:

Mourao, A.; Sattler, M.; Bonnal, S.; Komal, S.; Warner, L.; Bordonne, R.; Valcarcel, J.

Citation:

Citation: Mourao, A.; Bonnal, S.; Komal, S.; Warner, L.; Bordonne, R.; Valcarcel, J.; Sattler, M.. "Structural basis for the recognition ofspliceosomal SmN B B proteins by theRBM5 OCRE domain in splicing regulation" Elife 5, 1-25 (2016).
PubMed: 27894420

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7436.785 Da.
entity_2, polymer, 11 residues, 1136.371 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
entity_2: GMRPPPPGIRG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	292
15N chemical shifts	65
1H chemical shifts	443

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

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

Entity 2, entity_2 11 residues - 1136.371 Da.

1

GLY

MET

ARG

PRO

GLY

ILE

ARG

2

GLY

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 2 mM; entity_1, [U-99% 15N], 2 mM; entity_1, [U-13C; U-15N], 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 bar; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

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

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

NMR spectrometers:

Bruker DRX500 500 MHz
Bruker DRX600 600 MHz
Bruker DRX900 900 MHz

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