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 19792

Title: NMR structure of the RRM domain of RBMX from homo sapiens

Deposition date: 2014-02-14 Original release date: 2014-03-10

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

Citation: Serrano, Pedro; Wuthrich, Kurt; Geralt, Michael; Dutta, Samit. "NMR structure of the first RRM domain of the protein RBM39 from homo sapiens"  Not known ., .-..

Assembly members:
entity, polymer, 92 residues, 10093.535 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):
entity: GHMVEADRPGKLFIGGLNTE TNEKALEAVFGKYGRIVEVL LMKDRETNKSRGFAFVTFES PADAKDAARDMNGKSLDGKA IKVEQATKPSFE

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts92
1H chemical shifts581

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RBMX1

Entities:

Entity 1, RBMX 92 residues - 10093.535 Da.

1   GLYHISMETVALGLUALAASPARGPROGLY
2   LYSLEUPHEILEGLYGLYLEUASNTHRGLU
3   THRASNGLULYSALALEUGLUALAVALPHE
4   GLYLYSTYRGLYARGILEVALGLUVALLEU
5   LEUMETLYSASPARGGLUTHRASNLYSSER
6   ARGGLYPHEALAPHEVALTHRPHEGLUSER
7   PROALAASPALALYSASPALAALAARGASP
8   METASNGLYLYSSERLEUASPGLYLYSALA
9   ILELYSVALGLUGLNALATHRLYSPROSER
10   PHEGLU

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 10 mM; sodium azide 5 mM; DTT 2 mM

sample_conditions_1: ionic strength: 0.220 M; pH: 5; pressure: 1 atm; temperature: 298 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
4D APSY HACANHsample_1isotropicsample_conditions_1
5D APSY CBCACONHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P., Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, processing

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

UNIO, UNIO Herrmann and Wuthrich - chemical shift assignment, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19382
PDB
DBJ BAC31099 BAE00972 BAE22448 BAE37998 BAF62396
EMBL CAA80599 CAB51361 CAB51362 CAG31684 CAI46148
GB AAH03710 AAH06550 AAH07435 AAH11441 AAH12942
PIR S41766
REF NP_001020834 NP_001073196 NP_001100890 NP_001128678 NP_001156008
SP A5A6M3 D4AE41 P38159 P84586 Q4R7F0
TPG DAA13328 DAA13329

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