BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 16538

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

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: 15N, 13C and 1H Resonance Assignments of the Middle MA-3 Domain of the Tumour Suppressor Protein Pdcd4   PubMed: 20020227

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: 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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts658
15N chemical shifts157
1H chemical shifts1092

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Pdcd4 MA-3M1

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   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   ASPSERVALTRPGLYSERGLY

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:

NameSampleSample stateSample conditions
3D HNCACB15N_13Cisotropicsample_conditions_1
3D CBCA(CO)NH15N_13Cisotropicsample_conditions_1
3D HNCO15N_13Cisotropicsample_conditions_1
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-1H TOCSYUnlabelledisotropicsample_conditions_1
2D 1H-1H NOESYUnlabelledisotropicsample_conditions_1
3D 1H-15N NOESY-HSQC15Nisotropicsample_conditions_1
3D 1H-15N TOCSY-HSQC15Nisotropicsample_conditions_1
3D HCCH-TOCSY13Cisotropicsample_conditions_1
3D 1H-13C HSQC-NOESY13C_unlabel_aromisotropicsample_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

Related Database Links:

PDB
GB EAW49553 ELK04959 ELW50500 ERE78070 ERE78071
REF XP_008053135 XP_008053136 XP_012028877

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