1ats
THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
SAXS Profile
P(r) Distribution
1. Structure Basics
| entry_id | 1ats |
| deposition_date | 1993-08-09 |
| title | THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS |
| keywords | CHAPERONE PROTEIN; CHAPERONE PROTEIN |
| method | X-RAY DIFFRACTION |
Download Data
2. SAXS Parameters (CRYSOL)
| rg_guinier | 22.30 Å |
| rg_electron | 21.40 Å |
| i0 | 31675500.00 |
| molecular_weight | 42440.0 kDa |
| excluded_volume | 52855 ų |
| envelope_volume | 63188 ų |
| shell_volume | 24460 ų |
| envelope_diameter | 76.5 Å |
| shell_rg | 28.43 Å |
| envelope_rg | 21.59 Å |
| shape_rg | 21.40 Å |
| total_rg | 22.28 Å |
| total_atoms | 2985 |
| n_residues | 382 |
| 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 | 72.7 Å |
| rg_real | 22.20 Å |
| rg_real_error | 0.45 Å |
| i0_real | 3.1680e+07 |
| i0_real_error | 4.1390e+05 |
| rg_reciprocal | 22.23 Å |
| i0_reciprocal | 31680000.0000 |
| total_estimate | 0.8132 |
| solution_quality | GOOD a GOOD solution |
| n_peaks | 2 |
| r_peak_primary | 27.5 Å |
| skewness | 0.204 |
| kurtosis | -0.400 |
| angular_range | — – 0.3550 Å−1 |
| current_alpha | 0.0000 |
| highest_alpha | 8702000.0000 |
| n_real_points | 67 |
| gnom_version | 4.1.3 |
| quality_criteria | AN1: 0.000; Oscil: 0.857; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000 |