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
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Nicholas Rego and David Koes
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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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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	WR73	1

Entities:

Entity 1, WR73 183 residues - 20813.826 Da.

1

MET

LEU

ILE

TYR

LYS

ASP

ILE

PHE

THR

ASP

2

ASP

GLU

LEU

SER

ASP

SER

PHE

PRO

MET

3

LYS

LEU

VAL

ASP

LEU

VAL

TYR

GLU

PHE

4

LYS

GLY

LYS

HIS

VAL

ARG

LYS

GLU

GLY

5

GLU

ILE

VAL

LEU

ALA

GLY

SER

ASN

PRO

SER

6

ALA

GLU

GLY

ALA

GLU

ASP

GLY

SER

7

ASP

GLU

HIS

VAL

GLU

ARG

GLY

ILE

ASP

ILE

8

VAL

LEU

ASN

HIS

LYS

LEU

VAL

GLU

MET

ASN

9

CYS

TYR

GLU

ASP

ALA

SER

MET

PHE

LYS

ALA

10

TYR

ILE

LYS

PHE

MET

LYS

ASN

VAL

ILE

11

ASP

HIS

MET

GLU

LYS

ASN

ARG

ASP

LYS

12

ALA

ASP

VAL

ASP

ALA

PHE

LYS

ILE

13

GLN

GLY

TRP

VAL

SER

LEU

ALA

LYS

14

ASP

ARG

PHE

LYS

ASN

LEU

ALA

PHE

ILE

15

GLY

GLU

ARG

ALA

GLU

GLY

ALA

GLU

ASN

16

GLY

GLN

VAL

ALA

ILE

GLU

TYR

ARG

ASP

17

VAL

ASP

GLY

THR

GLU

VAL

PRO

THR

LEU

MET

18

LEU

VAL

LYS

GLU

ALA

ILE

GLU

LYS

19

CYS

LEU

GLU

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:

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

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

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