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 16833

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

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

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:
WR73, polymer, 183 residues, 20813.826 Da.

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

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

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

Data typeCount
13C chemical shifts602
15N chemical shifts189
1H chemical shifts484

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WR731

Entities:

Entity 1, WR73 183 residues - 20813.826 Da.

1   METLEUILETYRLYSASPILEPHETHRASP
2   ASPGLULEUSERSERASPSERPHEPROMET
3   LYSLEUVALASPASPLEUVALTYRGLUPHE
4   LYSGLYLYSHISVALVALARGLYSGLUGLY
5   GLUILEVALLEUALAGLYSERASNPROSER
6   ALAGLUGLUGLYALAGLUASPASPGLYSER
7   ASPGLUHISVALGLUARGGLYILEASPILE
8   VALLEUASNHISLYSLEUVALGLUMETASN
9   CYSTYRGLUASPALASERMETPHELYSALA
10   TYRILELYSLYSPHEMETLYSASNVALILE
11   ASPHISMETGLULYSASNASNARGASPLYS
12   ALAASPVALASPALAPHELYSLYSLYSILE
13   GLNGLYTRPVALVALSERLEULEUALALYS
14   ASPARGPHELYSASNLEUALAPHEPHEILE
15   GLYGLUARGALAALAGLUGLYALAGLUASN
16   GLYGLNVALALAILEILEGLUTYRARGASP
17   VALASPGLYTHRGLUVALPROTHRLEUMET
18   LEUVALLYSGLUALAILEILEGLUGLULYS
19   CYSLEUGLU

Samples:

sample_1: WR73, [U-13C; U-15N; U-2H; ILVFY-1H], 0.82 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: WR73, [U-5% 13C; U-100% 15N], 0.85 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSY-HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 15N-15N-1H NOESYsample_1isotropicsample_conditions_1
3D 13C-13C-1H NOESYsample_1isotropicsample_conditions_1
3D 15N-13C-1H NOESYsample_1isotropicsample_conditions_1
3D 13C-15N-1H NOESYsample_1isotropicsample_conditions_1
3D C(CO)NH TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC high resolutionsample_2isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN v2.1, Bruker Biospin - collection

VNMRJ, Varian - collection

PSVS v1.4, Bhattacharya and Montelione - structure validation

TALOS vplus, Cornilescu, Delaglio and Bax - dihedral angle constraints

PDBStat v5.1, Tejero and Montelione - PDB coordinate analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAB02099
REF NP_492767
SP Q93573