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 25043

Title: Structural Investigation of hnRNP L bound to RNA

Authors: Blatter, Markus; Allain, Frederic

Citation: Blatter, Markus; Allain, Frederic. "Most two C-terminal RNA Recognition Motif Domain of hnRNP L bound to two equivalents ACACA RNA"  To be Published ., .-..

Assembly members:
entity_1, polymer, 215 residues, 24141.418 Da.
RNA_(5'-R(*AP*CP*AP*CP*A)-3'), polymer, 5 residues, 1553.035 Da.

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

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

Entity Sequences (FASTA):
entity_1: YGPHADSPVLMVYGLDQSKM NCDRVFNVFCLYGNVEKVKF MKSKPGAAMVEMADGYAVDR AITHLNNNFMFGQKMNVCVS KQPAIMPGQSYGLEDGSCSY KDFSESRNNRFSTPEQAAKN RIQHPSNVLHFFNAPLEVTE ENFFEICDELGVKRPTSVKV FSGKSERSSSGLLEWDSKSD ALETLGFLNHYQMKNPNGPY PYTLKLCFSTAQHAS
RNA_(5'-R(*AP*CP*AP*CP*A)-3'): ACACA

Data typeCount
13C chemical shifts700
15N chemical shifts223
1H chemical shifts1466

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2RNA (5'-R(*AP*CP*AP*CP*A)-3')_12
3RNA (5'-R(*AP*CP*AP*CP*A)-3')_22

Entities:

Entity 1, entity_1 215 residues - 24141.418 Da.

1   TYRGLYPROHISALAASPSERPROVALLEU
2   METVALTYRGLYLEUASPGLNSERLYSMET
3   ASNCYSASPARGVALPHEASNVALPHECYS
4   LEUTYRGLYASNVALGLULYSVALLYSPHE
5   METLYSSERLYSPROGLYALAALAMETVAL
6   GLUMETALAASPGLYTYRALAVALASPARG
7   ALAILETHRHISLEUASNASNASNPHEMET
8   PHEGLYGLNLYSMETASNVALCYSVALSER
9   LYSGLNPROALAILEMETPROGLYGLNSER
10   TYRGLYLEUGLUASPGLYSERCYSSERTYR
11   LYSASPPHESERGLUSERARGASNASNARG
12   PHESERTHRPROGLUGLNALAALALYSASN
13   ARGILEGLNHISPROSERASNVALLEUHIS
14   PHEPHEASNALAPROLEUGLUVALTHRGLU
15   GLUASNPHEPHEGLUILECYSASPGLULEU
16   GLYVALLYSARGPROTHRSERVALLYSVAL
17   PHESERGLYLYSSERGLUARGSERSERSER
18   GLYLEULEUGLUTRPASPSERLYSSERASP
19   ALALEUGLUTHRLEUGLYPHELEUASNHIS
20   TYRGLNMETLYSASNPROASNGLYPROTYR
21   PROTYRTHRLEULYSLEUCYSPHESERTHR
22   ALAGLNHISALASER

Entity 2, RNA (5'-R(*AP*CP*AP*CP*A)-3')_1 5 residues - 1553.035 Da.

1   ACACA

Samples:

sample_1: entity_1, [U-100% 15N], 1.5 mM; RNA (5'-R(*AP*CP*AP*CP*A)-3') 3.0 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: entity_1, [U-100% 13C; U-100% 15N], 1.5 mM; RNA (5'-R(*AP*CP*AP*CP*A)-3') 3.0 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_3: entity_1, [U-100% 15N], 1.5 mM; RNA (5'-R(*AP*CP*AP*CP*A)-3') 3.0 mM; sodium chloride 60 mM; sodium phosphate 40 mM; DTT 1 mM; D2O 100%

sample_4: entity_1, [U-100% 13C; U-100% 15N], 1.5 mM; RNA (5'-R(*AP*CP*AP*CP*A)-3') 3.0 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: 313.15 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

Related Database Links: