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 25160

Title: NMR structure of the RRM1 of human LARP6   PubMed: 25488812

Authors: Martino, Luigi; Atkinson, Andrew; Kelly, Geoff; Conte, Maria

Citation: Martino, Luigi; Pennell, Simon; Kelly, Geoff; Busi, Baptiste; Brown, Paul; Atkinson, Andrew; Salisbury, Nicholas; Ooi, Zi; See, Kang; Smerdon, Stephen; Alfano, Caterina; Bui, Tam; Conte, Maria. "Synergic interplay of the La motif, RRM1, and the interdomain linker of LARP6 in the recognition of collagen mRNA expands the RNA binding repertoire of the La module"  Nucleic Acids Res. ., .-. (2014).

Assembly members:
LARP6_RRM1, polymer, 116 residues, 13132.548 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):
LARP6_RRM1: NLPSKMLLVYDLYLSPKLWA LATPQKNGRVQEKVMEHLLK LFGTFGVISSVRILKPGREL PPDIRRISSRYSQVGTQECA IVEFEEVEAAIKAHEFMITE SQGKENMKAVLIGMKP

Data sets:
Data typeCount
1H chemical shifts689
13C chemical shifts461
15N chemical shifts104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 116 residues - 13132.548 Da.

1   ASNLEUPROSERLYSMETLEULEUVALTYR
2   ASPLEUTYRLEUSERPROLYSLEUTRPALA
3   LEUALATHRPROGLNLYSASNGLYARGVAL
4   GLNGLULYSVALMETGLUHISLEULEULYS
5   LEUPHEGLYTHRPHEGLYVALILESERSER
6   VALARGILELEULYSPROGLYARGGLULEU
7   PROPROASPILEARGARGILESERSERARG
8   TYRSERGLNVALGLYTHRGLNGLUCYSALA
9   ILEVALGLUPHEGLUGLUVALGLUALAALA
10   ILELYSALAHISGLUPHEMETILETHRGLU
11   SERGLNGLYLYSGLUASNMETLYSALAVAL
12   LEUILEGLYMETLYSPRO

Samples:

sample_1: LARP6 RRM1, [U-95% 13C; U-95% 15N], 0.5 mM; TRIS 50 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 298 K; pH: 7.25; pressure: 1 atm; ionic strength: 0.1 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

XEASY, Bartels et al. - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

DBJ BAA92061 BAK62255
EMBL CAD38733
GB AAH06082 AAH09446 AAH14018 AAN76710 AAN76711
REF NP_001233506 NP_001273608 NP_060827 XP_001088126 XP_002753339
SP Q9BRS8