1bao
THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: THE CRYSTAL STRUCTURES OF TWO BARNASE MUTANTS
SAXS Profile
P(r) Distribution
1. Structure Basics
| entry_id | 1bao |
| deposition_date | 1993-05-19 |
| title | THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: THE CRYSTAL STRUCTURES OF TWO BARNASE MUTANTS |
| keywords | ENDONUCLEASE; ENDONUCLEASE |
| method | X-RAY DIFFRACTION |
Download Data
2. SAXS Parameters (CRYSOL)
| rg_guinier | 24.44 Å |
| rg_electron | 23.74 Å |
| i0 | 22569900.00 |
| molecular_weight | 35825.0 kDa |
| excluded_volume | 44631 ų |
| envelope_volume | 54691 ų |
| shell_volume | 20371 ų |
| envelope_diameter | 78.4 Å |
| shell_rg | 29.17 Å |
| envelope_rg | 23.59 Å |
| shape_rg | 23.73 Å |
| total_rg | 24.46 Å |
| total_atoms | 2539 |
| n_residues | 323 |
| 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 | 75.1 Å |
| rg_real | 24.40 Å |
| rg_real_error | 0.45 Å |
| i0_real | 2.2570e+07 |
| i0_real_error | 2.8470e+05 |
| rg_reciprocal | 24.42 Å |
| i0_reciprocal | 22570000.0000 |
| total_estimate | 0.9133 |
| solution_quality | EXCELLENT a EXCELLENT solution |
| n_peaks | 2 |
| r_peak_primary | 23.8 Å |
| skewness | 0.189 |
| kurtosis | -0.682 |
| angular_range | — – 0.3250 Å−1 |
| current_alpha | 0.0000 |
| highest_alpha | 4729000.0000 |
| n_real_points | 64 |
| gnom_version | 4.1.3 |
| quality_criteria | AN1: 0.000; Oscil: 0.973; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.981 |