BMRB Entry 16542

Name: 15N, 13C and 1H Backbone Resonance Assignments for the Complete Tandem MA-3 Region of the Tumour Suppressor Protein Pdcd4
Published: 2010-01-12

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16542

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

15N, 13C and 1H Backbone Resonance Assignments for the Complete Tandem MA-3 Region of the Tumour Suppressor Protein Pdcd4

Deposition date:

2009-10-06

Original release date:

2010-01-12

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-3_M-C, polymer, 298 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-3_M-C: GPLGSLPLDETAFEKTLTPI IQEYFEHGDTNEVAEMLRDL NLGEMKSGVPVLAVSLALEG KASHREMTSKLLSDLCGTVM STNDVEKSFDKLLKDLPELA LDTPRAPQLVGQFIARAVGD GILCNTYIDSYKGTVDCVQA RAALDKATVLLSMSKGGKRK DSVWGSGGGQQPVNHLVKEI DMLLKEYLLSGDISEAEHCL KELEVPHFHHELVYEAIVMV LESTGESAFKMILDLLKSLW KSSTITIDQMKRGYERIYNE IPDINLDVPHSYSVLERFVE ECFQAGIISKQLRDLCPS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	643
15N chemical shifts	269
1H chemical shifts	269

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

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

Entities:

Entity 1, Pdcd4 MA-3 M-C 298 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

GLN

18

GLN

PRO

VAL

ASN

HIS

LEU

VAL

LYS

GLU

ILE

19

ASP

MET

LEU

LYS

GLU

TYR

LEU

SER

20

GLY

ASP

ILE

SER

GLU

ALA

GLU

HIS

CYS

LEU

21

LYS

GLU

LEU

GLU

VAL

PRO

HIS

PHE

HIS

22

GLU

LEU

VAL

TYR

GLU

ALA

ILE

VAL

MET

VAL

23

LEU

GLU

SER

THR

GLY

GLU

SER

ALA

PHE

LYS

24

MET

ILE

LEU

ASP

LEU

LYS

SER

LEU

TRP

25

LYS

SER

THR

ILE

THR

ILE

ASP

GLN

MET

26

LYS

ARG

GLY

TYR

GLU

ARG

ILE

TYR

ASN

GLU

27

ILE

PRO

ASP

ILE

ASN

LEU

ASP

VAL

PRO

HIS

28

SER

TYR

SER

VAL

LEU

GLU

ARG

PHE

VAL

GLU

29

GLU

CYS

PHE

GLN

ALA

GLY

ILE

SER

LYS

30

GLN

LEU

ARG

ASP

LEU

CYS

PRO

SER

Samples:

15N_13C: Pdcd4 MA-3 M-C, [U-99% 13C; U-99% 15N], 0.15-0.5 mM; Sodium Phosphate 25 mM; sodium chloride 100 mM; DTT 2.5 mM; EDTA 50 uM; AEBSF protease inhibitor 200 uM; Sodium Azide 0.02%; TCEP 2.5 mM

15N: Pdcd4 MA-3 M-C, [U-99% 15N], 0.5 mM; Sodium Phosphate 25 mM; sodium chloride 100 mM; DTT 2.5 mM; EDTA 50 uM; AEBSF protease inhibitor 200 uM; Sodium Azide 0.02%; TCEP 2.5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
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
3D 1H-15N NOESY-HSQC	15N	isotropic	sample_conditions_1
3D HNCA	15N_13C	isotropic	sample_conditions_1
3D Trosy HN(CO)CA	15N_13C	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

PDB	3EIJ 3EIQ
DBJ	BAA09056 BAA13072 BAA32356 BAD97343 BAE22118
EMBL	CAH91837 CAJ18396
GB	AAB42218 AAB67706 AAF73961 AAH26104 AAH31049
REF	NP_001077116 NP_001126062 NP_001161963 NP_001161964 NP_001186421
SP	Q53EL6 Q5R8S3 Q61823 Q9JID1
TPG	DAA14719
AlphaFold	Q53EL6 Q5R8S3 Q61823 Q9JID1