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BMRB Entry 25958

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25958
MolProbity Validation Chart

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Title: p63/p73 hetero-tetramerisation domain   PubMed: 27716744

Deposition date: 2016-01-19 Original release date: 2016-12-01

Authors: Gebel, Jakob; Buchner, Lena; Loehr, Frank; Luh, Laura; Coutandin, Daniel; Guentert, Peter; Doetsch, Volker

Citation: Gebel, Jakob; Luh, Laura; Coutandin, Daniel; Osterburg, Christian; Lohr, Frank; Schafer, Birgit; Frombach, Ann-Sophie; Sumyk, Manuela; Buchner, Lena; Krojer, Tobias; Salah, Eidarus; Mathea, Sebastian; Guntert, Peter; Knapp, Stefan; Dotsch, Volker. "Mechanism of TAp73 inhibition by Delta Np63 and structural basis of p63/p73 hetero-tetramerization"  Cell Death Differ. 23, 1930-1940 (2016).

Assembly members:
p63_tetramerization_domain, polymer, 60 residues, 7323.260 Da.
p73_tetramerization_domain, polymer, 50 residues, 6034.947 Da.

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
p63_tetramerization_domain: SDDELLYLPVRGRETYEMLL EIKESLELMQYLPQHTIETY RQQQQQQHQHLLQKQTSIQS
p73_tetramerization_domain: GSDEDTYYLQVRGRKNFEIL MKLKESLELMELVPQPLVDS YRQQQQLLQR

Data sets:
Data typeCount
13C chemical shifts950
15N chemical shifts218
1H chemical shifts1538

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_1_11
2entity_2_12
3entity_1_21
4entity_2_22

Entities:

Entity 1, entity_1_1 60 residues - 7323.260 Da.

Residue 1 represents a cloning artifact.

1   SERASPASPGLULEULEUTYRLEUPROVAL
2   ARGGLYARGGLUTHRTYRGLUMETLEULEU
3   GLUILELYSGLUSERLEUGLULEUMETGLN
4   TYRLEUPROGLNHISTHRILEGLUTHRTYR
5   ARGGLNGLNGLNGLNGLNGLNHISGLNHIS
6   LEULEUGLNLYSGLNTHRSERILEGLNSER

Entity 2, entity_2_1 50 residues - 6034.947 Da.

Residue 1-2 represent a cloning artifact.

1   GLYSERASPGLUASPTHRTYRTYRLEUGLN
2   VALARGGLYARGLYSASNPHEGLUILELEU
3   METLYSLEULYSGLUSERLEUGLULEUMET
4   GLULEUVALPROGLNPROLEUVALASPSER
5   TYRARGGLNGLNGLNGLNLEULEUGLNARG

Samples:

p63_13C15N_p73: p63 tetramerization domain, [U-100% 13C; U-100% 15N], 0.5 mM; p73 tetramerization domain 0.5 mM; HEPES 25 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

p63_p73_13C15N: p63 tetramerization domain 0.5 mM; p73 tetramerization domain, [U-100% 13C; U-100% 15N], 0.5 mM; HEPES 25 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

p63_13C_p63_15N_p73: p63 tetramerization domain, [U-100% 15N], 0.5 mM; p63 tetramerization domain, [U-100% 13C], 0.5 mM; p73 tetramerization domain 1 mM; HEPES 25 mM; sodium chloride 50 mM

p63_p73_13C_p73_15N: p63 tetramerization domain 1 mM; p73 tetramerization domain, [U-100% 15N], 0.5 mM; p73 tetramerization domain, [U-100% 13C], 0.5 mM; HEPES 25 mM; sodium chloride 50 mM

p63_15N_D2O: p63 tetramerization domain, [U-100% 15N], 0.5 mM; p73 tetramerization domain 0.5 mM; HEPES 25 mM; sodium chloride 50 mM

p73_15N_D2O: p63 tetramerization domain 0.5 mM; p73 tetramerization domain, [U-100% 15N], 0.5 mM; HEPES 25 mM; sodium chloride 50 mM

p63_13C_p63_15N_p73_13C_p73_15N: p63 tetramerization domain, [U-100% 15N], 0.5 mM; p63 tetramerization domain, [U-100% 13C], 0.5 mM; p73 tetramerization domain, [U-100% 15N], 0.5 mM; p73 tetramerization domain, [U-100% 13C], 0.5 mM; HEPES 25 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 75 mM; pH: 7; pressure: 1 atm; temperature: 310 K

sample_conditions_2: ionic strength: 5 mM; pH: 6; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBp63_13C15N_p73isotropicsample_conditions_1
3D HN(CA)COp63_13C15N_p73isotropicsample_conditions_1
3D 1H-15N NOESYp63_13C15N_p73isotropicsample_conditions_1
3D HNCACBp63_p73_13C15Nisotropicsample_conditions_1
3D HN(CA)COp63_p73_13C15Nisotropicsample_conditions_1
3D 1H-15N NOESYp63_p73_13C15Nisotropicsample_conditions_1
3D H(CCO)NHp63_13C15N_p73isotropicsample_conditions_1
3D C(CO)NHp63_13C15N_p73isotropicsample_conditions_1
3D H(CCO)NHp63_p73_13C15Nisotropicsample_conditions_1
3D C(CO)NHp63_p73_13C15Nisotropicsample_conditions_1
2D 1H-13C HSQC aromaticp63_13C15N_p73isotropicsample_conditions_1
2D 1H-13C HSQC aromaticp63_p73_13C15Nisotropicsample_conditions_1
2D (H)CB(CG)CCH-TOCSYp63_13C15N_p73isotropicsample_conditions_1
2D (H)CB(CG)CCH-TOCSYp63_p73_13C15Nisotropicsample_conditions_1
2D (HB)CB(CDCD)HDp63_13C15N_p73isotropicsample_conditions_1
2D (HB)CB(CDCD)HDp63_p73_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESY aromaticp63_13C15N_p73isotropicsample_conditions_1
3D 1H-13C NOESY aromaticp63_p73_13C15Nisotropicsample_conditions_1
3D 13C/15N-filtered NOESY-[13C,1H]-HSQCp63_13C15N_p73isotropicsample_conditions_1
3D 13C/15N-filtered NOESY-[13C,1H]-HSQCp63_p73_13C15Nisotropicsample_conditions_1
3D 13C/15N-filtered NOESY-[15N,1H]-TROSYp63_13C15N_p73isotropicsample_conditions_1
3D 13C/15N-filtered NOESY-[15N,1H]-TROSYp63_p73_13C15Nisotropicsample_conditions_1
3D 1H-13C NOESYp63_13C15N_p73isotropicsample_conditions_1
3D 1H-13C NOESYp63_p73_13C15Nisotropicsample_conditions_1
2D 1H-13C HSQCp63_13C15N_p73isotropicsample_conditions_1
2D 1H-13C HSQCp63_p73_13C15Nisotropicsample_conditions_1
2D 1H-15N HSQCp63_13C15N_p73isotropicsample_conditions_1
2D 1H-15N HSQCp63_p73_13C15Nisotropicsample_conditions_1
2D 1H-15N HSQCp63_15N_D2Oisotropicsample_conditions_1
2D 1H-15N HSQCp73_15N_D2Oisotropicsample_conditions_1
3D lr-HNCOp63_13C_p63_15N_p73isotropicsample_conditions_1
3D lr-HNCOp63_p73_13C_p73_15Nisotropicsample_conditions_1
3D lr-HNCOp63_13C_p63_15N_p73_13C_p73_15Nisotropicsample_conditions_2

Software:

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS+, Cornilescu, Delaglio and Bax - data analysis

OPALp v1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

SPARKY v3.114, Goddard - chemical shift assignment, peak picking

TOPSPIN v3.2, Bruker Biospin - data analysis, processing

NMR spectrometers:

  • Bruker Avance II 500 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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