Backbone and side chain assignment performance of PINE-NMR with NMR data from a representative group of twelve proteins.

aThe maximum number of backbone assignment achievable theoretically on the basis of the peak lists provided as input to PINE, divided by the total number of backbone assignments deposited in BMRB, multiplied by 100.
bNumber of correct PINE-NMR backbone assignments, divided by the total number of backbone assignments deposited in BMRB, multiplied by 100.
cNumber of correct PINE-NMR (backbone/side chain) assignments (i.e. in agreement with those in BMRB), divided by the maximum number of (backbone/side chain) assignments achievable theoretically on the basis the peak lists provided as input to PINE, multiplied by 100.
dPercentage of residues correctly assigned to helix, strand, or “other” by PINE-NMR on the basis of agreement with DSSP [50] analysis of the deposited three-dimensional structure of the protein.
eTotal number of C′, Cα, and Cβ atoms detected as possible outliers by LACS method [16] in the final assignment.
fDefined as (see Table S1).
gDefined as number of noise peaks divided by number of real peaks in HNCACB.
hAll input included data from an HSQC or HNCO experiment; data from additional experiments were as indicated by shaded boxes: 1 CBCA(CO)NH or HN(CO)CACB, 2 HNCACB, 3 HNCA, 4 HN(CO)CA, 5 HN(CA)CO, 6 H(CCO)NH, 7 C(CO)NH, 8 HBHA(CO)NH, 9 HCCH-TOCSY.
iStereo array isotope labeled (SAIL) protein; data were analyzed without corrections for isotope shifts due to deuterium labeling.