BMRB Entry 15087

Name: SOLUTION STRUCTURE OF THE PABC DOMAIN FROM TRITICUM AEVESTIUM POLY(A)-BINDING PROTEIN
Published: 2007-03-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15087

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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:

SOLUTION STRUCTURE OF THE PABC DOMAIN FROM TRITICUM AEVESTIUM POLY(A)-BINDING PROTEIN

Deposition date:

2006-12-28

Original release date:

2007-03-05

Authors:

Siddiqui, Nadeem

Citation:

Citation: Siddiqui, Nadeem; Osborne, Michael; Gallie, Daniel; Gehring, Kalle. "Solution structure of the PABC domain from wheat poly (A)-binding protein: an insight into RNA metabolic and translational control in plants." Biochemistry 46, 4221-4231 (2007).
PubMed: 17358048

Assembly members:

Assembly members:
Poly(A)-binding_protein, polymer, 85 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Wheat Taxonomy ID: 4565 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Triticum aestivum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Poly(A)-binding_protein: GPLGSPIGALASALANSPPE TQRMMLGENLYPLVDQLEHD QAAKVTGMLLEMDQTEVLHL LESPDALKAKVAEAMEVLRS AQQHT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	78
1H chemical shifts	393

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PABC	1

Entities:

Entity 1, PABC 85 residues - Formula weight is not available

This is the C-terminal segment from wheat PABP.

1

GLY

PRO

LEU

GLY

SER

PRO

ILE

GLY

ALA

LEU

2

ALA

SER

ALA

LEU

ALA

ASN

SER

PRO

GLU

3

THR

GLN

ARG

MET

LEU

GLY

GLU

ASN

LEU

4

TYR

PRO

LEU

VAL

ASP

GLN

LEU

GLU

HIS

ASP

5

GLN

ALA

LYS

VAL

THR

GLY

MET

LEU

6

GLU

MET

ASP

GLN

THR

GLU

VAL

LEU

HIS

LEU

7

LEU

GLU

SER

PRO

ASP

ALA

LEU

LYS

ALA

LYS

8

VAL

ALA

GLU

ALA

MET

GLU

VAL

LEU

ARG

SER

9

ALA

GLN

HIS

THR

Samples:

sample_1: PABP; Sodium phosphate, Sodium Chloride, Sodium Azide, [U-15N], 1 – 2 mM; phosphate buffer 50 mM; NaCl 150 mM; NaN3 1 mM; H2O 90%; D2O 10%

sample_2: PABP; Sodium phosphate, Sodium Chloride, Sodium Azide, [U-100% 13C; U-100% 15N], 1 – 2 mM; phosphate buffer 50 mM; NaCl 150 mM; NaN3 1 mM; H2O 90%; D2O 10%

sample_3: PABP; Sodium phosphate, Sodium Chloride, Sodium Azide, none, 1 – 2 mM; phosphate buffer 50 mM; NaCl 150 mM; NaN3 1 mM; H2O 90%; D2O 10%

sample_4: Poly(A)-binding protein, [U-100% 13C; U-100% 15N], 1 – 2 mM; phosphate buffer 50 mM; NaCl 150 mM; NaN3 1 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6.3; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_3	isotropic	sample_conditions_1
2D TOCSY	sample_3	isotropic	sample_conditions_1
2D NOESY	sample_4	isotropic	sample_conditions_1
3D_15N-separated_NOESY	sample_1	isotropic	sample_conditions_1
HNCACB	sample_2	isotropic	sample_conditions_1
CBCACONH	sample_2	isotropic	sample_conditions_1

Software:

CNS v1.1, A Brunger, P Adams, M Clore, P Gros, M Nilges and R Read - refinement

NMR spectrometers:

Varian UNITY 800 MHz

PDB	2DYD
DBJ	BAJ96406
GB	AAB38974 EMS55649 EMT14398