1di3
ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
SAXS Profile
P(r) Distribution
1. Structure Basics
| entry_id | 1di3 |
| deposition_date | 1999-11-28 |
| title | ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME |
| keywords | STABILITY, TURN, MUTANT, HYDROLASE; HYDROLASE |
| method | X-RAY DIFFRACTION |
Download Data
2. SAXS Parameters (CRYSOL)
| rg_guinier | 15.40 Å |
| rg_electron | 14.05 Å |
| i0 | 4743850.00 |
| molecular_weight | 14632.0 kDa |
| excluded_volume | 17888 ų |
| envelope_volume | 19816 ų |
| shell_volume | 12103 ų |
| envelope_diameter | 47.1 Å |
| shell_rg | 19.66 Å |
| envelope_rg | 14.28 Å |
| shape_rg | 14.03 Å |
| total_rg | 15.13 Å |
| total_atoms | 1023 |
| n_residues | 130 |
| n_harmonics | 20 |
| q_range | — – 0.5000 Å−1 |
| n_points | 101 |
| shell_type | directional |
| solvent_density | 0.3340 e/ų |
| contrast_shell | 0.0300 e/ų |
| crysol_version | 4.1.3 |
3. P(r) Analysis (GNOM)
| dmax | 49.2 Å |
| rg_real | 15.32 Å |
| rg_real_error | 0.33 Å |
| i0_real | 4.7440e+06 |
| i0_real_error | 5.3770e+04 |
| rg_reciprocal | 15.33 Å |
| i0_reciprocal | 4744000.0000 |
| total_estimate | 0.8926 |
| solution_quality | GOOD a GOOD solution |
| n_peaks | 2 |
| r_peak_primary | 20.6 Å |
| skewness | 0.164 |
| kurtosis | -0.345 |
| angular_range | — – 0.5000 Å−1 |
| current_alpha | 0.0000 |
| highest_alpha | 752600.0000 |
| n_real_points | 80 |
| gnom_version | 4.1.3 |
| quality_criteria | AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.984 |