Table 1. NMR parameters, restraints, and statistics of the ATR13 structure.
| ATR13 Structural Restraints and StatisticsA | |||
| NOE | 448 | ||
| Intra | i = j | 155 | |
| Sequential | |i-j| = 1 | 142 | |
| Medium | |i-j| < 5 | 80 | |
| Long | |i-j| > 5 | 71 | |
| Dihedral | 43 | ||
| HN RDC | 27 | ||
| Hydrogen BondB | 28 | ||
| Restraint RMSDsC | |||
| NOE (Å) | 0.025 +/- 0.004 | ||
| Phi Dihedral (deg) | 0.2 +/- 0.2 | ||
| RDC (Hz), Qrdc | 0.8 +/- 0.2 , 7.4% | ||
| Hydrogen Bond (Å) | 0.029 +/- 0.006 | ||
| Coordinate RMSDsD | |||
| Backbone | 0.8 Å | ||
| Heavy atom | 1.5 Å | ||
| Close contacts(per structure)E,F | 0.2 | ||
| Ramachandran analysisD,E | |||
| Most favored region (%) | 83.2 | ||
| Additionally allowed (%) | 14.9 | ||
| Generously allowed (%) | 1.6 | ||
| Disallowed (%) | 0.3 | ||
| Structure Quality FactorsE,G | |||
| Verify3D | −5.14 | ||
| Prosall | −1.99 | ||
| Procheck | (phi-psi) | −2.28 | |
| Procheck | (all) | −4.7 | |
| MolProbity | −1.36 | ||
A. Parameters are for the 20 best of 200 structures.
B. Two restraints per hydrogen bond for a total of 14 hydrogen bonds.
C. For NOEs, on average, there was one NOE violation greater than 0.2 Å per structure, with the maximum violation equal to 0.5 Å. For phi dihedral restraints, on average, there were 0.4 violations greater than one degree, with the maximum violation of four degrees. For residual dipolar couplings, on average, there were 0.8 violations greater than 1.5 Hz, with the maximum violation equal to 3.4 Hz. For hydrogen bonds, on average, there were 0.4 violations greater than 0.1 Å, and all were less than 0.2 Å.
D. Includes residues 76–88, and 120–150.
E. Determined with the Protein Structure Validation Suite (PSVS) version 1.4.
F. Close contacts are defined as within 1.6 Å for H atoms, 2.2 Å for heavy atoms.
G. With respect to mean and standard deviation for a set of 252 X-ray structures < 500 residues, of resolution < = 1.80 Å, R-factor < = 0.25 and R-free < = 0.28.