BMRB Entry 16538

Name: 15N, 13C and 1H Resonance Assignments of the Middle MA-3 Domain of the Tumour Suppressor Protein Pdcd4
Published: 2010-01-11

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16538

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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:

15N, 13C and 1H Resonance Assignments of the Middle MA-3 Domain of the Tumour Suppressor Protein Pdcd4

Deposition date:

2009-10-05

Original release date:

2010-01-11

Authors:

Waters, Lorna; Oka, Ojore; Muskett, Frederick; Strong, Sarah; Schmedt, Thore; Klempnauer, Karl-Heinz; Carr, Mark

Citation:

Citation: Waters, Lorna; Oka, Ojore; Muskett, Frederick; Strong, Sarah; Schmedt, Thore; Klempnauer, Karl-Heinz; Carr, Mark. "Resonance Assignment and Secondary Structure of the Middle MA-3 Domain and Complete Tandem MA-3 Region of the Tumour Suppressor Protein Pdcd4." Biomol. NMR Assignments 4, 49-53 (2009).
PubMed: 20020227

Assembly members:

Assembly members:
Pdcd4_MA-3M, polymer, 167 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGex-6P-2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Pdcd4_MA-3M: GPLGSLPLDETAFEKTLTPI IQEYFEHGDTNEVAEMLRDL NLGEMKSGVPVLAVSLALEG KASHREMTSKLLSDLCGTVM STNDVEKSFDKLLKDLPELA LDTPRAPQLVGQFIARAVGD GILCNTYIDSYKGTVDCVQA RAALDKATVLLSMSKGGKRK DSVWGSG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	658
15N chemical shifts	157
1H chemical shifts	1092

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Pdcd4 MA-3M	1

Entities:

Entity 1, Pdcd4 MA-3M 167 residues - Formula weight is not available

Residues 152-156 are cloning artifacts and not part of the native sequence.

1

GLY

PRO

LEU

GLY

SER

LEU

PRO

LEU

ASP

GLU

2

THR

ALA

PHE

GLU

LYS

THR

LEU

THR

PRO

ILE

3

ILE

GLN

GLU

TYR

PHE

GLU

HIS

GLY

ASP

THR

4

ASN

GLU

VAL

ALA

GLU

MET

LEU

ARG

ASP

LEU

5

ASN

LEU

GLY

GLU

MET

LYS

SER

GLY

VAL

PRO

6

VAL

LEU

ALA

VAL

SER

LEU

ALA

LEU

GLU

GLY

7

LYS

ALA

SER

HIS

ARG

GLU

MET

THR

SER

LYS

8

LEU

SER

ASP

LEU

CYS

GLY

THR

VAL

MET

9

SER

THR

ASN

ASP

VAL

GLU

LYS

SER

PHE

ASP

10

LYS

LEU

LYS

ASP

LEU

PRO

GLU

LEU

ALA

11

LEU

ASP

THR

PRO

ARG

ALA

PRO

GLN

LEU

VAL

12

GLY

GLN

PHE

ILE

ALA

ARG

ALA

VAL

GLY

ASP

13

GLY

ILE

LEU

CYS

ASN

THR

TYR

ILE

ASP

SER

14

TYR

LYS

GLY

THR

VAL

ASP

CYS

VAL

GLN

ALA

15

ARG

ALA

LEU

ASP

LYS

ALA

THR

VAL

LEU

16

LEU

SER

MET

SER

LYS

GLY

LYS

ARG

LYS

17

ASP

SER

VAL

TRP

GLY

SER

GLY

Samples:

15N_13C: Pdcd4 MA-3M, [U-99% 13C; U-99% 15N], 0.5 mM; Sodium Phosphate 25 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 10 uM; AEBSF protease inhibitor 200 uM; Sodium Azide 0.02%

15N: Pdcd4 MA-3M, [U-99% 15N], 0.5-1.4 mM; Sodium Phosphate 25 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 10 uM; AEBSF protease inhibitor 200 uM; Sodium Azide 0.02%

13C: Pdcd4 MA-3M, [U-99% 13C], 0.5 mM; Sodium Phosphate 25 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 10 uM; AEBSF protease inhibitor 200 uM; Sodium Azide 0.02%

13C_unlabel_arom: Pdcd4 MA-3M, [U-99% 13C], 0.5 mM; Sodium Phosphate 25 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 10 uM; AEBSF protease inhibitor 200 uM; Sodium Azide 0.02%

Unlabelled: Pdcd4 MA-3M 0.5 mM; Sodium Phosphate 25 mM; sodium chloride 100 mM; DTT 0.5 mM; EDTA 10 uM; AEBSF protease inhibitor 200 uM; Sodium Azide 0.02%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	15N_13C	isotropic	sample_conditions_1
3D CBCA(CO)NH	15N_13C	isotropic	sample_conditions_1
3D HNCO	15N_13C	isotropic	sample_conditions_1
2D 1H-15N HSQC	15N	isotropic	sample_conditions_1
2D 1H-1H TOCSY	Unlabelled	isotropic	sample_conditions_1
2D 1H-1H NOESY	Unlabelled	isotropic	sample_conditions_1
3D 1H-15N NOESY-HSQC	15N	isotropic	sample_conditions_1
3D 1H-15N TOCSY-HSQC	15N	isotropic	sample_conditions_1
3D HCCH-TOCSY	13C	isotropic	sample_conditions_1
3D 1H-13C HSQC-NOESY	13C_unlabel_arom	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY v3.110, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz
Bruker DRX 600 MHz
Bruker Avance 600 MHz

PDB	2KZT
GB	EAW49553 ELK04959 ELW50500 ERE78070 ERE78071
REF	XP_008053135 XP_008053136 XP_012028877