BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25434

Title: Solution NMR Structure of the OCRE Domain of RBM10   PubMed: 26712279

Deposition date: 2015-01-20 Original release date: 2015-03-30

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

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).

Assembly members:
OCRE, polymer, 92 residues, 10856.678 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

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

Data sets:
Data typeCount
13C chemical shifts294
15N chemical shifts93
1H chemical shifts549

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1OCRE1

Entities:

Entity 1, OCRE 92 residues - 10856.678 Da.

1   GLYHISMETGLNGLUSERTYRSERGLNTYR
2   PROVALPROASPVALSERTHRTYRGLNTYR
3   ASPGLUTHRSERGLYTYRTYRTYRASPPRO
4   GLNTHRGLYLEUTYRTYRASPPROASNSER
5   GLNTYRTYRTYRASNALAGLNSERGLNGLN
6   TYRLEUTYRTRPASPGLYGLUARGARGTHR
7   TYRVALPROALALEUGLUGLNSERALAASP
8   GLYHISLYSGLUTHRGLYALAPROSERLYS
9   GLUGLYLYSGLULYSLYSGLULYSHISLYS
10   THRLYS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
APSY 4D-HACANHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_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 shifts
SPARKY: Backbone or all simulated shifts