BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19203

Title: NMR structure of RNA recognition motif 2 (RRM2) of Homo sapiens splicing factor, arginine/serine-rich 1

Deposition date: 2013-04-29 Original release date: 2013-05-13

Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of RNA recognition motif 2 (RRM2) of Homo sapiens splicing factor, arginine/serine-rich 1"  Not known ., .-..

Assembly members:
RRM2, polymer, 90 residues, 10207.483 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

Entity Sequences (FASTA):
RRM2: GAPRGRYGPPSRRSENRVVV SGLPPSGSWQDLKDHMREAG DVCYADVYRDGTGVVEFVRK EDMTYAVRKLDNTKFRSHEG ETAYIRVKVD

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts87
1H chemical shifts593

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM2 of Homo sapiens splicing factor, arginine/serine-rich 11

Entities:

Entity 1, RRM2 of Homo sapiens splicing factor, arginine/serine-rich 1 90 residues - 10207.483 Da.

1   GLYALAPROARGGLYARGTYRGLYPROPRO
2   SERARGARGSERGLUASNARGVALVALVAL
3   SERGLYLEUPROPROSERGLYSERTRPGLN
4   ASPLEULYSASPHISMETARGGLUALAGLY
5   ASPVALCYSTYRALAASPVALTYRARGASP
6   GLYTHRGLYVALVALGLUPHEVALARGLYS
7   GLUASPMETTHRTYRALAVALARGLYSLEU
8   ASPASNTHRLYSPHEARGSERHISGLUGLY
9   GLUTHRALATYRILEARGVALLYSVALASP

Samples:

sample_1: RRM2, [U-99% 13C; U-99% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
4D-HACANH-APSYsample_1isotropicsample_conditions_1
5D-CBCACONH-APSYsample_1isotropicsample_conditions_1
5D-HACACONH-APSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic with non-uniform samplingsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromatic with non-uniform samplingsample_1isotropicsample_conditions_1
3D 1H-15N NOESY with non-uniform samplingsample_1isotropicsample_conditions_1

Software:

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

j-UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19248
PDB
DBJ BAB93456 BAC37367 BAE29641 BAE88160 BAF82622
EMBL CAH92288
GB AAA03476 AAA35564 AAA35565 AAH10264 AAH42354
REF NP_001006919 NP_001033096 NP_001069862 NP_001071635 NP_001103022
SP Q07955 Q0VCY7 Q3YLA6 Q5R7H2 Q6DII2
TPG DAA19172

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts