129l
;STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT ;
SAXS Profile
P(r) Distribution
1. Structure Basics
| entry_id | 129l |
| deposition_date | 1993-05-28 |
| title | ;STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT ; |
| keywords | HYDROLASE(O-GLYCOSYL); HYDROLASE(O-GLYCOSYL) |
| method | X-RAY DIFFRACTION |
Download Data
2. SAXS Parameters (CRYSOL)
| rg_guinier | 17.47 Å |
| rg_electron | 16.49 Å |
| i0 | 6611230.00 |
| molecular_weight | 18622.0 kDa |
| excluded_volume | 23308 ų |
| envelope_volume | 26736 ų |
| shell_volume | 14154 ų |
| envelope_diameter | 58.6 Å |
| shell_rg | 21.78 Å |
| envelope_rg | 16.58 Å |
| shape_rg | 16.47 Å |
| total_rg | 17.47 Å |
| total_atoms | 1304 |
| 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 | 17.45 Å |
| rg_real_error | 0.35 Å |
| i0_real | 6.6110e+06 |
| i0_real_error | 7.8620e+04 |
| rg_reciprocal | 17.45 Å |
| i0_reciprocal | 6611000.0000 |
| total_estimate | 0.7972 |
| solution_quality | GOOD a GOOD solution |
| n_peaks | 3 |
| r_peak_primary | 21.7 Å |
| skewness | 0.345 |
| kurtosis | -0.226 |
| angular_range | — – 0.4550 Å−1 |
| current_alpha | 0.0000 |
| highest_alpha | 1498000.0000 |
| n_real_points | 76 |
| gnom_version | 4.1.3 |
| quality_criteria | AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000 |