Table 1.

Statistics for crystal structure

Data CollectionWild-TypeP1244L
PDB accession codes6FBB6FCP
Wavelength, Å1.0 Å1.0
Resolution, Å45.63–1.30 (1.32–1.30)45.55–1.45 (1.48–1.45)
Space groupC2221C2221
Cell parameters, Å
a82.5382.53
b112.24112.18
c62.7262.53
CC1/2, %a,b99.8 (87.3)99.9 (90.9)
Rsym, %a,c8.7 (76.8)6.8 (65.6)
Rmeas, %a,d,e9.5 (84.2)7.4 (71.2)
Average I/σ(I)a15.9 (3.2)21.1 (4.1)
Completeness, %a100 (100)99.6 (97.3)
No. of unique reflectionsa71785 (3534)51510 (2541)
Redundancya12.7 (11.9)12.9 (12.9)
Wilson B-factor, Å211.612.6
Refinement
 Number of nonhydrogen protein/solvent atoms2008/3042027/400
Rwork, %15.4113.32
Rfree, %16.6415.90
 No. of reflections in the “free” set35132554
 R.m.s. deviations from ideal values
 Bond lengths (Å)/bond angles (°)0.009/1.20.008/1.17
 Average protein/solvent B-factor, Å218.6/31.217.4/33.7
 Ramachandran plot: favored/outlier residues, %98.8/0.099.0/0.0
  • Multiple statistics (first column) for solved crystal structures of Wild-Type SHROOM3 (middle column) or P1244L (last column) when interacting with 14-3-3. PDB, Protein Data Bank; I/σ(I), signal to noise of intensity values; r.m.s., root mean square.

  • a Number in parentheses is for the highest resolution shell used in the refinement.

  • b CC1/2=Pearson’s intradataset correlation coefficient, as described by Karplus and Diederichs.43

  • c Rsym=∑hl│IhlIh│/∑hl<Ih>, where Ihl is the intensity of the lth observation of reflection h and <Ih> is the average intensity of reflection h.

  • d Rmeas=∑h│√(nh/(nh – 1))∑lIhl – <Ih>││/∑hl<Ih>, where nh is the number of observations of reflection h.

  • e Correlation of experimental intensities with intensities calculated from refined model, as described by Karplus and Diederichs.43