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. Author manuscript; available in PMC: 2014 Aug 1.
Published in final edited form as: J Biomol NMR. 2013 Jul 30;56(4):337–351. doi: 10.1007/s10858-013-9753-7

Table 3.

NMR structure statistics for the CNSw and rCS-Rosetta structures of PfR193A and ZR18a

PfR193A (CNSw) PfR193A (rCS-Rosetta) ZR18 (CNSw) ZR18 (rCS-Rosetta)
Completeness of resonance assignments b:
        backbone (%) 93.46 93.46 93.99 93.99
        side chain (%) 90.34 90.34 78.02 78.02
        aromatic (%) 100 100 100 100
        stereospecific methyl (%) 88.46 88.46 100 100
Conformationally-restricting restraintsc:
    Distance restraints
        Total 2719 2719 1137 1137
        intra-residue (i = j) 523 523 168 168
        sequential(|i-j|= 1) 686 686 337 337
        medium range (1 < |i - j| < 5) 271 271 217 217
        long range (|i - j| ≥ 5) 1239 1239 415 415
    Dihedral angle restraints 165 165 179 179
    Hydrogen bond restraints 0 0 54 54
    No. of restraints per residue 26.7 26.7 15.7 15.7
    No. of long range restraints per residue 11.5 11.5 5.1 5.1
Residual restraint violationsc:
    Average no. of distance viol per structure:
        0.1 - 0.2 Å 2.60 16.05 9.50 8.95
        0.2 - 0.5 Å 0.05 10.95 5.10 5.35
        > 0.5 Å 0 2.25 0.50 3.20
        largest violation (Å) 0.22 1.72 0.95 1.30
    Average no. of dihed angle viol per structure:
        1 - 10° 19.90 2.55 9.7 1.35
        > 10° 0 1.55 0.1 0.15
            largest violation (°) 9.6 59.7 11.0 22.2
Model QUalityc:
        RMSD backbone atoms (Å) d 0.4 0.4 0.7 0.6
        RMSD heavy atoms (Å) d 0.6 0.6 1.0 0.8
        RMSD bond lengths (Å) 0.008 0.010 0.019 0.010
        RMSD bond angles (°) 0.6 0.5 1.3 0.4
    MolProbity Ramachandran statistics c,d
        most favored regions (%) 96.7 98.4 88.9 97.1
        allowed regions (%) 3.2 1.3 9. 8 2.9
        disallowed regions (%) 0.1 0.3 1. 3 0.0
    Global quality scores (Raw / Z-score)c
        Verify3D 0.37 / −1.44 0.41 / −0.80 0.33 / -2.09 0.43 / −0.48
        ProsalI 0.35 / −1.24 0.35 / −1.24 0.43 / −0.91 0.67 / 0.08
        Procheck (phi-psi) −0.42 / −1.34 −0.30 / −0.87 −0.70 / -2.44 −0.20 / −0.47
        Procheck (all) d −0.27 / −1.60 −0.05 / 0.30 −0 .43 / -2.54 0.12 / 0.71
        MolProbity clash score 15.93 / −1.21 10.36 / −0.25 12.95 / −0.70 6.27 / 0.45
    RPF Scorese
        Recall / Precision 0.967 / 0.955 0.967 / 0.958 0.927 / 0.779 0.931 / 0.772
        F-measure / DP-score 0.961 / 0.874 0.963 / 0.881 0.847 / 0.747 0. 844 / 0.747
Model Contents:
436-541 436-520, 3-5,14-18,28- 2-11,14-
    Ordered residue range d 523-541 32,38-50,53- 22,27-83
68,70-82
BMRB accession number: 16385 16385 5844 5844
PDB id: 2kl6 2m8x 2m6q 2m8w
a

Structural statistics computed for the ensemble of deposited structures.

b

Computed using AVS software [54] from the expected number of resonances, excluding: highly exchangeable protons (N-terminal, Lys, and Arg amino groups, hydroxyls of Ser, Thr, Tyr), carboxyls of Asp and Glu, non-protonated aromatic carbons, and the C-terminal His6 tag.

c

Calculated using PSVS 1.5 [9]. Average distance violations were calculated using the sum over r−6.

d

For ordered residues with [S(phi) + S(psi) ≥ 1.8].

e

RPF scores [25] reflecting the goodness-of-fit of the final ensemble of structures (including disordered residues) to the NOESY data and resonance assignments.