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 25040

Click here to enlarge.

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/BMR25040
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: Structural Investigation of hnRNP L

Deposition date: 2014-06-24 Original release date: 2015-05-04

Authors: Blatter, Markus; Allain, Frederic

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

Assembly members:
entity, polymer, 216 residues, 24256.506 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: DYGPHADSPVLMVYGLDQSK MNCDRVFNVFCLYGNVEKVK FMKSKPGAAMVEMADGYAVD RAITHLNNNFMFGQKMNVCV SKQPAIMPGQSYGLEDGSCS YKDFSESRNNRFSTPEQAAK NRIQHPSNVLHFFNAPLEVT EENFFEICDELGVKRPTSVK VFSGKSERSSSGLLEWDSKS DALETLGFLNHYQMKNPNGP YPYTLKLCFSTAQHAS

Data sets:
Data typeCount
13C chemical shifts587
15N chemical shifts216
1H chemical shifts1272

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 216 residues - 24256.506 Da.

1   ASPTYRGLYPROHISALAASPSERPROVAL
2   LEUMETVALTYRGLYLEUASPGLNSERLYS
3   METASNCYSASPARGVALPHEASNVALPHE
4   CYSLEUTYRGLYASNVALGLULYSVALLYS
5   PHEMETLYSSERLYSPROGLYALAALAMET
6   VALGLUMETALAASPGLYTYRALAVALASP
7   ARGALAILETHRHISLEUASNASNASNPHE
8   METPHEGLYGLNLYSMETASNVALCYSVAL
9   SERLYSGLNPROALAILEMETPROGLYGLN
10   SERTYRGLYLEUGLUASPGLYSERCYSSER
11   TYRLYSASPPHESERGLUSERARGASNASN
12   ARGPHESERTHRPROGLUGLNALAALALYS
13   ASNARGILEGLNHISPROSERASNVALLEU
14   HISPHEPHEASNALAPROLEUGLUVALTHR
15   GLUGLUASNPHEPHEGLUILECYSASPGLU
16   LEUGLYVALLYSARGPROTHRSERVALLYS
17   VALPHESERGLYLYSSERGLUARGSERSER
18   SERGLYLEULEUGLUTRPASPSERLYSSER
19   ASPALALEUGLUTHRLEUGLYPHELEUASN
20   HISTYRGLNMETLYSASNPROASNGLYPRO
21   TYRPROTYRTHRLEULYSLEUCYSPHESER
22   THRALAGLNHISALASER

Samples:

sample_1: entity, [U-100% 15N], 0.5 – 0.7 mM; sodium chloride 200 mM; sodium phosphate 50 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 0.5 – 0.7 mM; sodium chloride 200 mM; sodium phosphate 50 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_3: entity, [U-100% 15N], 0.5 – 0.7 mM; sodium chloride 200 mM; sodium phosphate 50 mM; DTT 1 mM; D2O 100%

sample_conditions_1: ionic strength: 0.25 M; pH: 6.5; pressure: 1 atm; temperature: 303.15 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

Software:

TOPSPIN, Bruker Biospin - collection, refinement

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:

PDB
DBJ BAA24237 BAB18649 BAE02304 BAE26011 BAF84804
EMBL CAA34261
GB AAG01405 AAH27206 AAH30461 AAH69184 AAH86392
PRF 1604358A
REF NP_001005335 NP_001128232 NP_001178959 NP_001252929 NP_001267082
SP P14866 Q8R081
TPG DAA19831

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