BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17402

Title: Structure/function of the LBR Tudor domain   PubMed: 22052904

Deposition date: 2011-01-10 Original release date: 2011-12-02

Authors: Liokatis, Stamatios; Edlich, Christian; Soupsana, Katerina; Giannios, Ioannis; Sattler, Michael; Georgatos, Spyros; Politou, Anastasia

Citation: Liokatis, Stamatis; Edlich, Christian; Soupsana, Katerina; Giannios, Ioannis; Panagiotidou, Parthena; Tripsianes, Konstantinos; Sattler, Michael; Georgatos, Spyros; Politou, Anastasia. "Solution structure and molecular interactions of lamin B receptor Tudor domain."  J. Biol. Chem. 287, 1032-1042 (2012).

Assembly members:
LBR_Tudor_domain, polymer, 66 residues, 7490.461 Da.

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

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

Entity Sequences (FASTA):
LBR_Tudor_domain: GAMGMPNRKYADGEVVMGRW PGSVLYYEVQVTSYDDASHL YTVKYKDGTELALKESDIRL QSSFKQ

Data sets:
Data typeCount
13C chemical shifts230
15N chemical shifts69
1H chemical shifts451

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LBR_Tudor_domain1

Entities:

Entity 1, LBR_Tudor_domain 66 residues - 7490.461 Da.

1   GLYALAMETGLYMETPROASNARGLYSTYR
2   ALAASPGLYGLUVALVALMETGLYARGTRP
3   PROGLYSERVALLEUTYRTYRGLUVALGLN
4   VALTHRSERTYRASPASPALASERHISLEU
5   TYRTHRVALLYSTYRLYSASPGLYTHRGLU
6   LEUALALEULYSGLUSERASPILEARGLEU
7   GLNSERSERPHELYSGLN

Samples:

sample_1: LBR_Tudor_domain 0.8 mM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - dihedral angle restraints

ProcheckNMR, Laskowski and MacArthur - structure quality analysis

WhatIF, Vriend - structure quality analysis

Molmol, Koradi, Billeter and Wuthrich - molecular images

TOPSPIN, Bruker Biospin - collection

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

BMRB 15733
PDB
EMBL CAA68758 CAG31779
REF NP_990673 XP_010704965
SP P23913

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