BMRB Entry 25434

Name: Solution NMR Structure of the OCRE Domain of RBM10
Published: 2015-03-30

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PDB ID: 2mxw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25434
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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 NMR Structure of the OCRE Domain of RBM10

Deposition date:

2015-01-20

Original release date:

2015-03-30

Authors:

Martin, B.; Geralt, M.; Serrano, P.; Wuthrich, K.

Citation:

Citation: Martin, Bryan; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence Motif" Structure 24, 158-164 (2016).
PubMed: 26712279

Assembly members:

Assembly members:
OCRE, polymer, 92 residues, 10856.678 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 Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OCRE: GHMQESYSQYPVPDVSTYQY DETSGYYYDPQTGLYYDPNS QYYYNAQSQQYLYWDGERRT YVPALEQSADGHKETGAPSK EGKEKKEKHKTK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	294
15N chemical shifts	93
1H chemical shifts	549

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OCRE	1

Entities:

Entity 1, OCRE 92 residues - 10856.678 Da.

1

GLY

HIS

MET

GLN

GLU

SER

TYR

SER

GLN

TYR

2

PRO

VAL

PRO

ASP

VAL

SER

THR

TYR

GLN

TYR

3

ASP

GLU

THR

SER

GLY

TYR

ASP

PRO

4

GLN

THR

GLY

LEU

TYR

ASP

PRO

ASN

SER

5

GLN

TYR

ASN

ALA

GLN

SER

GLN

6

TYR

LEU

TYR

TRP

ASP

GLY

GLU

ARG

THR

7

TYR

VAL

PRO

ALA

LEU

GLU

GLN

SER

ALA

ASP

8

GLY

HIS

LYS

GLU

THR

GLY

ALA

PRO

SER

LYS

9

GLU

GLY

LYS

GLU

LYS

GLU

LYS

HIS

LYS

10

THR

LYS

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM

sample_conditions_1: ionic strength: 0.240 M; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
APSY 4D-HACANH	sample_1	isotropic	sample_conditions_1
APSY 5D-CBCACONH	sample_1	isotropic	sample_conditions_1
APSY 5D-HACACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.0, Bruker Biospin, Guntert, Mumenthaler and Wuthrich - collection, data analysis, processing, structure solution

UNIO vv2010, (UNIO) Hermann and Wuthrich - chemical shift assignment, peak picking, structure solution

CARA, (CARA) Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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