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1b65

;Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold ;

Method: X-RAY DIFFRACTION Dmax: 141.1 Å Quality: REASONABLE

SAXS Profile

SAXS profile for 1b65

P(r) Distribution

P(r) distribution for 1b65

1. Structure Basics

entry_id1b65
deposition_date1999-01-20
title;Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold ;
keywordsHYDROLASE, PEPTIDE DEGRADATION, NTN HYDROLASE; HYDROLASE
methodX-RAY DIFFRACTION

Download Data

2. SAXS Parameters (CRYSOL)

rg_guinier41.63
rg_electron41.25
i0855970000.00
molecular_weight234100.0 kDa
excluded_volume290150 ų
envelope_volume365760 ų
shell_volume72167 ų
envelope_diameter150.0
shell_rg47.90
envelope_rg41.44
shape_rg41.26
total_rg41.54
total_atoms16482
n_residues2178
n_harmonics20
q_range— – 0.5000 −1
n_points101
shell_typedirectional
solvent_density0.3340 e/ų
contrast_shell0.0300 e/ų
crysol_version4.1.3

3. P(r) Analysis (GNOM)

dmax141.1
rg_real41.67
rg_real_error1.13
i0_real8.5600e+08
i0_real_error1.5350e+07
rg_reciprocal41.63
i0_reciprocal855900000.0000
total_estimate0.6430
solution_quality REASONABLE a REASONABLE solution
n_peaks1
r_peak_primary48.3
skewness0.408
kurtosis-0.253
angular_range— – 0.1900 −1
current_alpha0.0000
highest_alpha179100000.0000
n_real_points39
gnom_version4.1.3
quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 0.008; Positv: 1.000; Valcen: 1.000; Smooth: 0.846

4. Crystallography & Experiment

5. Entities & Polymer Info (2)

6. Citations (3)

7. Files & Curves (10)