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. Author manuscript; available in PMC: 2011 Jul 7.
Published in final edited form as: J Am Chem Soc. 2010 Jul 7;132(26):8961–8972. doi: 10.1021/ja100447p

Table 6.

The results for PATIDOCK+ using a combination of CSP-like and alignment tensor constraints.

Protein Structurea RMSDb RMSD2c Δcd RMSDRDCe #Sol.f
B1 domain of protein G 3gb1 0.92 2.01 1.89 1.63 1
B3 domain of protein G 2oed 1.17 3.23 3.22 1.66 1
Cyanovirin-N 2ezm 1.44 3.93 3.93 3.98 1
Gα interacting protein 1cmz 1.15 3.53 3.10 2.67 1
Ubiquitin 1d3z 1.00 2.46 2.46 2.27 1
Hen lysozyme 1e8l 0.90 1.94 1.94 7.36 1
Oxidized putidaredoxin 1yjj 1.34 3.15 3.03 4.40 1
Ubiquitin/UBA 2jy6-II 0.57 1.37 1.28 4.91 1
di-Ubiquitin 2bgf-II 0.78 1.73 1.59 4.28 1

Mean 1.03 2.60 2.49 3.69 1.00
a

See previous tables and Results section for structure references.

b

The backbone RMSD (in Å) between the original complex structure and the predicted complex. The structures are optimally rotated and centered using the center of mass.39

c

The backbone RMSD (in Å) between the coordinates of atoms of the second domain for the original and predicted complex.

d

The distance (in Å) between the original and the predicted center of the second domain. The center is computed as the average of the positions of all the atoms in the domain.

e

The RMSD (in Hz) between the experimental and the predicted RDC values at the best predicted minimizer.

f

The number of possible solutions, all of which have a very similar χF2.