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 19502

Title: Protein structure   PubMed: 24753571

Deposition date: 2013-09-17 Original release date: 2014-05-06

Authors: Barraud, Pierre; Allain, Frederic

Citation: Barraud, Pierre; Banerjee, Silpi; Mohamed, Weaam; Jantsch, Michael; Allain, Frederic H-T. "A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1."  Proc. Natl. Acad. Sci. U.S.A. ., .-. (2014).

Assembly members:
dsRBD3, polymer, 113 residues, 10452.122 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: pET28a

Entity Sequences (FASTA):
dsRBD3: GSSHHHHHHSSGLVPRGSHM MPNKVRKIGELVRYLNTNPV GGLLEYARSHGFAAEFKLVD QSGPPHEPKFVYQAKVGGRW FPAVCAHSKKQGKQEAADAA LRVLIGENEKAER

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts93
1H chemical shifts604

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1dsRBD31

Entities:

Entity 1, dsRBD3 113 residues - 10452.122 Da.

1   GLYSERSERHISHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERHISMET
3   METPROASNLYSVALARGLYSILEGLYGLU
4   LEUVALARGTYRLEUASNTHRASNPROVAL
5   GLYGLYLEULEUGLUTYRALAARGSERHIS
6   GLYPHEALAALAGLUPHELYSLEUVALASP
7   GLNSERGLYPROPROHISGLUPROLYSPHE
8   VALTYRGLNALALYSVALGLYGLYARGTRP
9   PHEPROALAVALCYSALAHISSERLYSLYS
10   GLNGLYLYSGLNGLUALAALAASPALAALA
11   LEUARGVALLEUILEGLYGLUASNGLULYS
12   ALAGLUARG

Samples:

13C-15N_H2O: dsRBD3, [U-99% 13C; U-99% 15N], 0.7 – 0.9 mM; sodium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

13C-15N_D20: dsRBD3, [U-99% 13C; U-99% 15N], 0.7 – 0.9 mM; sodium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; D2O 100%

15N_H20: dsRBD3, [U-99% 15N], 0.7 – 0.9 mM; sodium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

1H_D2O: dsRBD30.7 – 0.9 mM; sodium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 313.0 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_H20isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic13C-15N_H2Oisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic13C-15N_D20isotropicsample_conditions_1
3D HNCA13C-15N_H2Oisotropicsample_conditions_1
3D CBCA(CO)NH13C-15N_H2Oisotropicsample_conditions_1
3D HNCACB13C-15N_H2Oisotropicsample_conditions_1
3D HCCH-TOCSY13C-15N_D20isotropicsample_conditions_1
2D 1H-1H NOESY1H_D2Oisotropicsample_conditions_1
2D 1H-1H TOCSY1H_D2Oisotropicsample_conditions_1
3D 1H-15N NOESY15N_H20isotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13C-15N_H2Oisotropicsample_conditions_1
3D 1H-13C NOESY aromatic13C-15N_H2Oisotropicsample_conditions_1
15N{1H}-HeteroNOE15N_H20isotropicsample_conditions_1
long-range 2D 1H-15N HSQC15N_H20isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

ProcheckNMR, Laskowski and MacArthur - structure validation

CING, Nabuurs, Spronk, Krieger, Maassen, Vriend and Vuister - structure validation

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB

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