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 30126

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30126
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution NMR structure of human LARP7 xRRM2   PubMed: 27679474

Deposition date: 2016-06-28 Original release date: 2016-10-07

Authors: Eichhorn, Catherine; Feigon, Juli

Citation: Eichhorn, Catherine; Chug, Rahul; Feigon, Juli. "hLARP7 C-terminal domain contains an xRRM that binds the 3' hairpin of 7SK RNA"  Nucleic Acids Res. 44, 9977-9989 (2016).

Assembly members:
La-related protein 7, polymer, 125 residues, 14395.445 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 'BL21-Gold(DE3)pLysS AG'

Entity Sequences (FASTA):
La-related protein 7: MHHHHHHSNATGPQFVSGVI VKIISTEPLPGRKQVRDTLA AISEVLYVDLLEGDTECHAR FKTPEDAQAVINAYTEINKK HCWKLEILSGDHEQRYWQKI LVDRQAKLNQPREKKRGTEK LITKA

Data typeCount
13C chemical shifts520
15N chemical shifts121
1H chemical shifts869

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 125 residues - 14395.445 Da.

1   METHISHISHISHISHISHISSERASNALA
2   THRGLYPROGLNPHEVALSERGLYVALILE
3   VALLYSILEILESERTHRGLUPROLEUPRO
4   GLYARGLYSGLNVALARGASPTHRLEUALA
5   ALAILESERGLUVALLEUTYRVALASPLEU
6   LEUGLUGLYASPTHRGLUCYSHISALAARG
7   PHELYSTHRPROGLUASPALAGLNALAVAL
8   ILEASNALATYRTHRGLUILEASNLYSLYS
9   HISCYSTRPLYSLEUGLUILELEUSERGLY
10   ASPHISGLUGLNARGTYRTRPGLNLYSILE
11   LEUVALASPARGGLNALALYSLEUASNGLN
12   PROARGGLULYSLYSARGGLYTHRGLULYS
13   LEUILETHRLYSALA

Samples:

sample_1: hLARP7 xRRM2-1, [U-99% 13C; U-99% 15N], 0.8 mM; hLARP7 xRRM2-2, [U-99% 15N], 0.8 mM; H2O 90%; D2O 10%; NaPO4 20 mM; NaCl 100 mM; TCEP 1 mM

sample_2: hLARP7 xRRM2, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%; NaPO4 20 mM; NaCl 100 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.1; pressure: 760 mmHg; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3d HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCCONHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

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

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz

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