BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17475

Title: Structural basis of p63a SAM domain mutants involved in AEC syndrome   PubMed: 21615690

Deposition date: 2011-02-18 Original release date: 2011-06-01

Authors: Sathyamurthy, A.; Freund, S.; Johnson, C.; Allen, Mark

Citation: Sathyamurthy, Aruna; Freund, Stefan; Johnson, Christopher; Allen, Mark; Bycroft, Mark. "Structural basis of p63 SAM domain mutants involved in AEC syndrome."  FEBS J. 278, 2680-2688 (2011).

Assembly members:
TUMOR_PROTEIN_63, polymer, 82 residues, 9321.517 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):
TUMOR_PROTEIN_63: GSYPTDCSIVSFLARLGCSS CLDYFTTQGLTTIYQIEHYS MDDLASLKIPEQFRHAIWKG ILDHRQLHEFSSPSHLLRTP SS

Data sets:
Data typeCount
13C chemical shifts157
15N chemical shifts75
1H chemical shifts340

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TUMOR PROTEIN 631

Entities:

Entity 1, TUMOR PROTEIN 63 82 residues - 9321.517 Da.

1   GLYSERTYRPROTHRASPCYSSERILEVAL
2   SERPHELEUALAARGLEUGLYCYSSERSER
3   CYSLEUASPTYRPHETHRTHRGLNGLYLEU
4   THRTHRILETYRGLNILEGLUHISTYRSER
5   METASPASPLEUALASERLEULYSILEPRO
6   GLUGLNPHEARGHISALAILETRPLYSGLY
7   ILELEUASPHISARGGLNLEUHISGLUPHE
8   SERSERPROSERHISLEULEUARGTHRPRO
9   SERSER

Samples:

sample_1: TUMOR PROTEIN 63, [U-13C; U-15N], 1.5 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150.000 mM; pH: 6.500; pressure: 1 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H NOESYsample_1solutionsample_conditions_1
2D TOCSYsample_1solutionsample_conditions_1
DQF COSYsample_1solutionsample_conditions_1
HSQC (13C and 15N)sample_1solutionsample_conditions_1
3D HNCACBsample_1solutionsample_conditions_1
CBCACONHsample_1solutionsample_conditions_1
CCCONHsample_1solutionsample_conditions_1
HNCACOsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HNHBsample_1solutionsample_conditions_1

Software:

Ansig3.3 vany, Kraulis -

AutoDep v4.3, PDBe -

CNS vany, Brunger, Adams, Clore, Gros, Nilges and Read -

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

UNP P63_HUMAN
PDB
DBJ BAA32432 BAA32433 BAA32593 BAB20591 BAE23286
EMBL CAA76562 CAB88216 CAC37098 CAC37099
GB AAC43038 AAC62635 AAC62636 AAC62641 AAC62644
REF NP_001108452 NP_001120731 NP_001120736 NP_001120814 NP_003713
SP O88898 Q9H3D4 Q9JJP6

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