BMRB Entry 17402

Name: Structure/function of the LBR Tudor domain
Published: 2011-12-02

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PDB ID: 2l8d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17402
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Structure/function of the LBR Tudor domain

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:

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).
PubMed: 22052904

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24d

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	230
15N chemical shifts	69
1H chemical shifts	451

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LBR_Tudor_domain	1

Entities:

Entity 1, LBR_Tudor_domain 66 residues - 7490.461 Da.

1

GLY

ALA

MET

GLY

MET

PRO

ASN

ARG

LYS

TYR

2

ALA

ASP

GLY

GLU

VAL

MET

GLY

ARG

TRP

3

PRO

GLY

SER

VAL

LEU

TYR

GLU

VAL

GLN

4

VAL

THR

SER

TYR

ASP

ALA

SER

HIS

LEU

5

TYR

THR

VAL

LYS

TYR

LYS

ASP

GLY

THR

GLU

6

LEU

ALA

LEU

LYS

GLU

SER

ASP

ILE

ARG

LEU

7

GLN

SER

PHE

LYS

GLN

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_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

BMRB	15733
PDB	2L8D
EMBL	CAA68758 CAG31779
REF	NP_990673 XP_010704965
SP	P23913
AlphaFold	P23913