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Biological Magnetic Resonance Data Bank


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BMRB Entry 25159

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25159
MolProbity Validation Chart

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Title: Solution structure of the La motif of human LARP6   PubMed: 25488812

Deposition date: 2014-08-18 Original release date: 2014-12-22

Authors: Martino, Luigi; Salisbury, Nicholas; 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:
entity, polymer, 114 residues, 13485.439 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: TASGGENEREDLEQEWKPPD EELIKKLVDQIEFYFSDENL EKDAFLLKHVRRNKLGYVSV KLLTSFKKVKHLTRDWRTTA HALKYSVVLELNEDHRKVRR TTPVPLFPNENLPS

Data sets:
Data typeCount
1H chemical shifts669
13C chemical shifts416
15N chemical shifts98

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 114 residues - 13485.439 Da.

1   THRALASERGLYGLYGLUASNGLUARGGLU
2   ASPLEUGLUGLNGLUTRPLYSPROPROASP
3   GLUGLULEUILELYSLYSLEUVALASPGLN
4   ILEGLUPHETYRPHESERASPGLUASNLEU
5   GLULYSASPALAPHELEULEULYSHISVAL
6   ARGARGASNLYSLEUGLYTYRVALSERVAL
7   LYSLEULEUTHRSERPHELYSLYSVALLYS
8   HISLEUTHRARGASPTRPARGTHRTHRALA
9   HISALALEULYSTYRSERVALVALLEUGLU
10   LEUASNGLUASPHISARGLYSVALARGARG
11   THRTHRPROVALPROLEUPHEPROASNGLU
12   ASNLEUPROSER

Samples:

sample_1: LARP6-LaM, [U-95% 13C; U-95% 15N], 0.4 mM; TRIS 50 mM; potassium chloride 100 mM; DTT 1 mM; L-Arginine 50 mM; L-Glutamic acid 50 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 HN(CO)CAsample_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, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

ARIA, Linge, O, . - structure solution

NMR spectrometers:

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

Related Database Links:

DBJ BAA92061 BAK62255
EMBL CAD38733
GB AAH06082 AAH09446 AAH14018 AAN76710 AAN76711
REF NP_001233506 NP_060827 XP_001088126 XP_002753339 XP_002825664
SP Q9BRS8

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