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 51253

Title: Solution NMR backbone chemical shift assignment for the La Module of human La-related protein 7   PubMed: 35320752

Deposition date: 2021-12-22 Original release date: 2022-03-28

Authors: Yang, Yuan; Hadjian, Tanya; Feigon, Juli

Citation: Yang, Yuan; Liu, Shiheng; Egloff, Sylvain; Eichhorn, Catherine; Hadjian, Tanya; Zhen, James; Kiss, Tamas; Zhou, Z. Hong; Feigon, Juli. "Structural basis of RNA conformational switching in the transcriptional regulator 7SK RNP"  Mol. Cell 82, 1724-1736 (2022).

Assembly members:
entity_1, polymer, 202 residues, 23424 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   Vector: pETDuet-1

Entity Sequences (FASTA):
entity_1: GEVEKKKRSRVKQVLADIAK QVDFWFGDANLHKDRFLREQ IEKSRDGYVDISLLVSFNKM KKLTTDGKLIARALRSSAVV ELDLEGTRIRRKKPLGERPK DEDERTVYVELLPKNVNHSW IERVFGKCGNVVYISIPHYK STGDPKGFAFVEFETKEQAA KAIEFLNNPPEEAPRKERHK MGEEVIPLRVLSKSEWMDLK KE

Data sets:
Data typeCount
13C chemical shifts499
15N chemical shifts182
1H chemical shifts182

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Larp7 La module1

Entities:

Entity 1, Larp7 La module 202 residues - 23424 Da.

First Glycine (residue 21) is a non-native residue as a result of TEV-protease cleavage site. Loop truncation between (including) native residues 197 and 364.

1   GLYGLUVALGLULYSLYSLYSARGSERARG
2   VALLYSGLNVALLEUALAASPILEALALYS
3   GLNVALASPPHETRPPHEGLYASPALAASN
4   LEUHISLYSASPARGPHELEUARGGLUGLN
5   ILEGLULYSSERARGASPGLYTYRVALASP
6   ILESERLEULEUVALSERPHEASNLYSMET
7   LYSLYSLEUTHRTHRASPGLYLYSLEUILE
8   ALAARGALALEUARGSERSERALAVALVAL
9   GLULEUASPLEUGLUGLYTHRARGILEARG
10   ARGLYSLYSPROLEUGLYGLUARGPROLYS
11   ASPGLUASPGLUARGTHRVALTYRVALGLU
12   LEULEUPROLYSASNVALASNHISSERTRP
13   ILEGLUARGVALPHEGLYLYSCYSGLYASN
14   VALVALTYRILESERILEPROHISTYRLYS
15   SERTHRGLYASPPROLYSGLYPHEALAPHE
16   VALGLUPHEGLUTHRLYSGLUGLNALAALA
17   LYSALAILEGLUPHELEUASNASNPROPRO
18   GLUGLUALAPROARGLYSGLUARGHISLYS
19   METGLYGLUGLUVALILEPROLEUARGVAL
20   LEUSERLYSSERGLUTRPMETASPLEULYS
21   LYSGLU

Samples:

sample_1: Larp7 La module 22-390 with loop deletion, [U-13C; U-15N], 0.8 mM; sodium phosphate 20 mM; potassium chloride 50 mM; TCEP 1 mM; D2O 5%

sample_conditions_1: ionic strength: 0.07 M; pH: 6.05; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN vv4.0.7 - collection

TOPSPIN vv3.5pl7 - collection

NMRPipe vv2016.273.11.31 - processing

NMRFAM-SPARKY vv1.470 - chemical shift assignment

NMR spectrometers:

  • Bruker Avance Neo 800 MHz
  • Bruker Avance III HD 600 MHz

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