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 17427

Title: Chemical Shift Assignments for p21-KID Bound to Cdk2 and Cyclin A in Solution   PubMed: 21358637

Deposition date: 2011-01-25 Original release date: 2011-03-08

Authors: Wang, Yuefeng; Fisher, John; Mattew, Rose; Ou, Li; Otieno, Steve; Sublett, Jack; Xiao, Limin; Chen, Jianhan; Roussel, Martine; Kriwacki, Richard

Citation: Wang, Yuefeng; Fisher, John; Mathew, Rose; Ou, Li; Otieno, Steve; Sublet, Jack; Xiao, Limin; Chen, Jianhan; Roussel, Martine; Kriwacki, Richard. "Intrinsic disorder mediates the diverse regulatory functions of the Cdk inhibitor p21."  Nat. Chem. Biol. 7, 214-221 (2011).

Assembly members:
p21_kinase_inhibitory_domain, polymer, 76 residues, Formula weight is not available

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):
p21_kinase_inhibitory_domain: RQNPCGSKACRRLFGPVDSE QLSRDCDALMAGCIQEARER WNFDFVTETPLEGDFAWERV RGLGLPKLYLPTGPRR

Data sets:
Data typeCount
13C chemical shifts92
15N chemical shifts57
1H chemical shifts57

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p21-KID1

Entities:

Entity 1, p21-KID 76 residues - Formula weight is not available

1   ARGGLNASNPROCYSGLYSERLYSALACYS
2   ARGARGLEUPHEGLYPROVALASPSERGLU
3   GLNLEUSERARGASPCYSASPALALEUMET
4   ALAGLYCYSILEGLNGLUALAARGGLUARG
5   TRPASNPHEASPPHEVALTHRGLUTHRPRO
6   LEUGLUGLYASPPHEALATRPGLUARGVAL
7   ARGGLYLEUGLYLEUPROLYSLEUTYRLEU
8   PROTHRGLYPROARGARG

Samples:

sample_1: p21 kinase inhibitory domain, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AMX 800 MHz

Related Database Links:

DBJ BAD93118 BAE88691 BAG10980 BAG61011 BAG70104
EMBL CAG38770 CAL37589 CAL37798
GB AAA16109 AAA19811 AAA85641 AAB29246 AAB59559
PRF 2002363A
REF NP_000380 NP_001181651 NP_001207706 NP_001207707 NP_001278478
SP P38936

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