BMRB Entry 16542

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

Data sets:
Data typeCount
13C chemical shifts643
15N chemical shifts269
1H chemical shifts269

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Pdcd4 MA-3 M-C1

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   GLYPROLEUGLYSERLEUPROLEUASPGLU
2   THRALAPHEGLULYSTHRLEUTHRPROILE
3   ILEGLNGLUTYRPHEGLUHISGLYASPTHR
4   ASNGLUVALALAGLUMETLEUARGASPLEU
5   ASNLEUGLYGLUMETLYSSERGLYVALPRO
6   VALLEUALAVALSERLEUALALEUGLUGLY
7   LYSALASERHISARGGLUMETTHRSERLYS
8   LEULEUSERASPLEUCYSGLYTHRVALMET
9   SERTHRASNASPVALGLULYSSERPHEASP
10   LYSLEULEULYSASPLEUPROGLULEUALA
11   LEUASPTHRPROARGALAPROGLNLEUVAL
12   GLYGLNPHEILEALAARGALAVALGLYASP
13   GLYILELEUCYSASNTHRTYRILEASPSER
14   TYRLYSGLYTHRVALASPCYSVALGLNALA
15   ARGALAALALEUASPLYSALATHRVALLEU
16   LEUSERMETSERLYSGLYGLYLYSARGLYS
17   ASPSERVALTRPGLYSERGLYGLYGLYGLN
18   GLNPROVALASNHISLEUVALLYSGLUILE
19   ASPMETLEULEULYSGLUTYRLEULEUSER
20   GLYASPILESERGLUALAGLUHISCYSLEU
21   LYSGLULEUGLUVALPROHISPHEHISHIS
22   GLULEUVALTYRGLUALAILEVALMETVAL
23   LEUGLUSERTHRGLYGLUSERALAPHELYS
24   METILELEUASPLEULEULYSSERLEUTRP
25   LYSSERSERTHRILETHRILEASPGLNMET
26   LYSARGGLYTYRGLUARGILETYRASNGLU
27   ILEPROASPILEASNLEUASPVALPROHIS
28   SERTYRSERVALLEUGLUARGPHEVALGLU
29   GLUCYSPHEGLNALAGLYILEILESERLYS
30   GLNLEUARGASPLEUCYSPROSER

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:

NameSampleSample stateSample conditions
3D CBCA(CO)NH15N_13Cisotropicsample_conditions_1
3D HNCO15N_13Cisotropicsample_conditions_1
2D 1H-15N HSQC15Nisotropicsample_conditions_1
3D 1H-15N NOESY-HSQC15Nisotropicsample_conditions_1
3D HNCA15N_13Cisotropicsample_conditions_1
3D Trosy HN(CO)CA15N_13Cisotropicsample_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

Related Database Links:

PDB
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 Q9JID1 Q61823 Q5R8S3

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks