1dya
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
SAXS Profile
P(r) Distribution
1. Structure Basics
| entry_id | 1dya |
| deposition_date | 1993-05-13 |
| title | DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME |
| keywords | HYDROLASE(O-GLYCOSYL); HYDROLASE(O-GLYCOSYL) |
| method | X-RAY DIFFRACTION |
Download Data
2. SAXS Parameters (CRYSOL)
| rg_guinier | 17.50 Å |
| rg_electron | 16.50 Å |
| i0 | 6762700.00 |
| molecular_weight | 18641.0 kDa |
| excluded_volume | 23251 ų |
| envelope_volume | 26672 ų |
| shell_volume | 14127 ų |
| envelope_diameter | 59.1 Å |
| shell_rg | 21.75 Å |
| envelope_rg | 16.57 Å |
| shape_rg | 16.48 Å |
| total_rg | 17.48 Å |
| total_atoms | 1303 |
| n_residues | 162 |
| 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 | 58.0 Å |
| rg_real | 17.49 Å |
| rg_real_error | 0.34 Å |
| i0_real | 6.7630e+06 |
| i0_real_error | 8.0400e+04 |
| rg_reciprocal | 17.49 Å |
| i0_reciprocal | 6763000.0000 |
| total_estimate | 0.7950 |
| solution_quality | GOOD a GOOD solution |
| n_peaks | 3 |
| r_peak_primary | 21.6 Å |
| skewness | 0.348 |
| kurtosis | -0.224 |
| angular_range | — – 0.4550 Å−1 |
| current_alpha | 0.0000 |
| highest_alpha | 1441000.0000 |
| n_real_points | 76 |
| gnom_version | 4.1.3 |
| quality_criteria | AN1: 0.000; Oscil: 0.785; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.000 |