BMRB Entry 16833

Name: Minimal Constraint Solution NMR Structure of Translationally-controlled tumor protein (TCTP) from C.elegans, Northeast Structural Genomics Consortium Target Target WR73
Published: 2010-04-29

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PDB ID: 2loy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16833
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:

Minimal Constraint Solution NMR Structure of Translationally-controlled tumor protein (TCTP) from C.elegans, Northeast Structural Genomics Consortium Target Target WR73

Deposition date:

2010-04-02

Original release date:

2010-04-29

Authors:

Aramini, James; Rossi, Paolo; Cort, John; Cooper, Bonnie; Maglaqui, Melissa; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano

Citation:

Citation: Aramini, James; Rossi, Paolo; Cort, John; Cooper, Bonnie; Maglaqui, Melissa; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano. "Minimal Constraint Solution NMR Structure of Translationally-controlled tumor protein (TCTP) from C.elegans, Northeast Structural Genomics Consortium Target Target WR73" To be published ., .-..

Assembly members:

Assembly members:
WR73, polymer, 183 residues, 20813.826 Da.

Natural source:

Natural source: Common Name: Caenorhabditis elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WR73: MLIYKDIFTDDELSSDSFPM KLVDDLVYEFKGKHVVRKEG EIVLAGSNPSAEEGAEDDGS DEHVERGIDIVLNHKLVEMN CYEDASMFKAYIKKFMKNVI DHMEKNNRDKADVDAFKKKI QGWVVSLLAKDRFKNLAFFI GERAAEGAENGQVAIIEYRD VDGTEVPTLMLVKEAIIEEK CLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	602
15N chemical shifts	189
1H chemical shifts	484

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY-HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D TROSY-HNCACB	sample_1	isotropic	sample_conditions_1
3D TROSY-HN(CO)CACB	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
3D 15N-15N-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-13C-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 15N-13C-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-15N-1H NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC high resolution	sample_2	isotropic	sample_conditions_1

PDB	2KWB 2LOY
EMBL	CAB02099
REF	NP_492767
SP	Q93573
AlphaFold	Q93573

BMRB Entry 16833

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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