BMRB Entry 25042

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25042
MolProbity Validation Chart

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Title:
Structural Investigation of hnRNP L bound to RNA
Deposition date:
2014-06-24
Original release date:
2015-12-21
Authors:
Blatter, Markus; Allain, Frederic
Citation:

Citation: Blatter, Markus; Allain, Frederic. "Second RNA Recognition Motif Domain of hnRNP L bound to ACACAC RNA"  To be Published ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 118 residues, 13079.807 Da.
RNA_(5'-R(*AP*CP*AP*CP*AP*C)-3'), polymer, 6 residues, 1858.218 Da.

Natural source:

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTYB11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QKISRPGDSDDSRSVNSVLL FTILNPIYSITTDVLYTICN PCGPVQRIVIFRKNGVQAMV EFDSVQSAQRAKASLNGADI YSGCCTLKIEYAKPTRLNVF KNDQDTWDYTNPNLSGQG
RNA_(5'-R(*AP*CP*AP*CP*AP*C)-3'): ACACAC

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts134
1H chemical shifts872

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hnRNP L1
2RNA (5'-R(*AP*CP*AP*CP*AP*C)-3')2

Entities:

Entity 1, hnRNP L 118 residues - 13079.807 Da.

1   GLNLYSILESERARGPROGLYASPSERASP
2   ASPSERARGSERVALASNSERVALLEULEU
3   PHETHRILELEUASNPROILETYRSERILE
4   THRTHRASPVALLEUTYRTHRILECYSASN
5   PROCYSGLYPROVALGLNARGILEVALILE
6   PHEARGLYSASNGLYVALGLNALAMETVAL
7   GLUPHEASPSERVALGLNSERALAGLNARG
8   ALALYSALASERLEUASNGLYALAASPILE
9   TYRSERGLYCYSCYSTHRLEULYSILEGLU
10   TYRALALYSPROTHRARGLEUASNVALPHE
11   LYSASNASPGLNASPTHRTRPASPTYRTHR
12   ASNPROASNLEUSERGLYGLNGLY

Entity 2, RNA (5'-R(*AP*CP*AP*CP*AP*C)-3') 6 residues - 1858.218 Da.

1   ACACAC

Samples:

sample_1: hnRNP L, [U-100% 15N], 2 mM; RNA (5'-R(*AP*CP*AP*CP*AP*C)-3') 2 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: hnRNP L, [U-100% 13C; U-100% 15N], 2 mM; RNA (5'-R(*AP*CP*AP*CP*AP*C)-3') 2 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_3: hnRNP L, [U-100% 15N], 2 mM; RNA (5'-R(*AP*CP*AP*CP*AP*C)-3') 2 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; D2O 100%

sample_4: hnRNP L, [U-100% 13C; U-100% 15N], 2 mM; RNA (5'-R(*AP*CP*AP*CP*AP*C)-3') 2 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 310.15 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
3D F3-filtered-F2-edited NOESYsample_4isotropicsample_conditions_1
2D F2-filtered NOESYsample_4isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz

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