Structure of CK2 beta subunit crystallized in the presence of a p21WAF1 peptide

Structure of the regulatory subunit of CK2 in the presence of a p21WAF1 peptide demonstrates flexibility of the acidic loop.

Disordered segment of Cyclin-dependent kinase inhibitor 1

PEG 4000, bicine, magnesium chloride, DTT, isopropanol, pH 9.2, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K

SEQUENCE
The complete sequence crystallized by the authors
for chains M,N,O,P,Q,R,S,T is RERWNFDFVTETPLEGDFAW
(residues 46-65 of reference sequence SwissProt
P38936). The authors informed that they do not
know how the coordinates align with the sequence
since they could not identify the side chains of
the residues they could see, and since the rest
of the residues are disordered. Each group of
unknown residues has been assigned a unique chain
ID and is believed to be part of one chain.
UNK Q 1 and UNK R 1 are the only visible residues
in chains Q and R, respectively.

BIOMOLECULE: 1, 2, 3, 4
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
WHICH CONSISTS OF 16 CHAIN(S). SEE REMARK 350 FOR
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).

The peptide was chemically synthesized. The sequence of the peptide occurs naturally in Homo sapiens (human).

Used maximum likelihood with amplitudes procedure.

Casein kinase II beta chain (E.C.2.7.1.37), Disordered segment of Cyclin-dependent kinase inhibitor 1

The asymmetric unit contains 4 biological dimers of CK2 regulatory subunit

CASEIN KINASE BETA SUBUNIT, SER/THR PROTEIN KINASE, CYCLIN-DEPENDENT KINASE INHIBITOR, ZN FINGER, TRANSFERASE